data_4MMZ # _entry.id 4MMZ # _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 4MMZ RCSB RCSB082113 WWPDB D_1000082113 # 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 4MMY . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MMZ _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 4MMZ _cell.length_a 129.790 _cell.length_b 129.790 _cell.length_c 307.676 _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 4MMZ _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 10533.767 1 ? 'GRGDSPAS to PRGDWNEG' 'Fibronectin type-III domain 10 (UNP residues 1448-1540)' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 19 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 3 ? ? ? ? 6 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 7 non-polymer syn 'MANGANESE (II) ION' 54.938 8 ? ? ? ? 8 non-polymer syn 'SODIUM ION' 22.990 2 ? ? ? ? 9 non-polymer syn GLYCEROL 92.094 2 ? ? ? ? 10 non-polymer syn 'CHLORIDE ION' 35.453 2 ? ? ? ? 11 water nat water 18.015 9 ? ? ? ? # 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 ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTPRGDW NEGSKPISINYRTGKKGK ; ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTPRGDW NEGSKPISINYRTGKKGK ; 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 THR n 3 76 PRO n 3 77 ARG n 3 78 GLY n 3 79 ASP n 3 80 TRP n 3 81 ASN n 3 82 GLU 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 ? 'alphav, ITGAV, MSK8, VNRA' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 2 1 sample ? ? ? human ? 'GP3A, ITGB3' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 3 1 sample ? ? ? human ? 'FN1, FN' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 511693 ? ? ? ? ? ? BL21 ? ? ? ? ? ? ? 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 4MMZ A 1 ? 959 ? P06756 31 ? 989 ? 1 959 2 2 4MMZ B 1 ? 692 ? P05106 27 ? 718 ? 1 692 3 3 4MMZ 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 4MMZ PRO C 76 ? UNP P02751 GLY 1523 'ENGINEERED MUTATION' 1492 1 3 4MMZ TRP C 80 ? UNP P02751 SER 1527 'ENGINEERED MUTATION' 1496 2 3 4MMZ ASN C 81 ? UNP P02751 PRO 1528 'ENGINEERED MUTATION' 1497 3 3 4MMZ GLU C 82 ? UNP P02751 ALA 1529 'ENGINEERED MUTATION' 1498 4 3 4MMZ GLY C 83 ? UNP P02751 SER 1530 'ENGINEERED MUTATION' 1499 5 3 4MMZ GLY C 94 ? UNP P02751 ? ? 'EXPRESSION TAG' 1510 6 3 4MMZ LYS C 95 ? UNP P02751 ? ? 'EXPRESSION TAG' 1511 7 3 4MMZ LYS C 96 ? UNP P02751 ? ? 'EXPRESSION TAG' 1512 8 3 4MMZ GLY C 97 ? UNP P02751 ? ? 'EXPRESSION TAG' 1513 9 3 4MMZ LYS C 98 ? UNP P02751 ? ? 'EXPRESSION TAG' 1514 10 # 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 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 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 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 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 4MMZ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.87 _exptl_crystal.density_percent_sol 68.25 _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 2012-08-04 _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 0.97934 _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 0.97934 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MMZ _reflns.observed_criterion_sigma_I 5.4 _reflns.observed_criterion_sigma_F 5.4 _reflns.d_resolution_low 50 _reflns.d_resolution_high 3.10 _reflns.number_obs 55243 _reflns.number_all 55243 _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.079 _reflns.pdbx_netI_over_sigmaI 24.3 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.1 _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 3.1 _reflns_shell.d_res_low 3.21 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.739 _reflns_shell.meanI_over_sigI_obs 2.0 _reflns_shell.pdbx_redundancy 6.1 _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 4MMZ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 55185 _refine.ls_number_reflns_all 54602 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.37 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 42.484 _refine.ls_d_res_high 3.102 _refine.ls_percent_reflns_obs 99.87 _refine.ls_R_factor_obs 0.2056 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2031 _refine.ls_R_factor_R_free 0.2560 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.90 _refine.ls_number_reflns_R_free 2706 _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 'RAMACHANDRAN RESTRAINTS APPLIED' _refine.pdbx_starting_model 'PDB ENTRY 3IJE' _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 25.36 _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 13147 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 345 _refine_hist.number_atoms_solvent 9 _refine_hist.number_atoms_total 13501 _refine_hist.d_res_high 3.102 _refine_hist.d_res_low 42.484 # 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 ? ? 13864 'X-RAY DIFFRACTION' ? f_angle_d 0.904 ? ? 18703 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 13.016 ? ? 5097 'X-RAY DIFFRACTION' ? f_chiral_restr 0.035 ? ? 2118 'X-RAY DIFFRACTION' ? f_plane_restr 0.004 ? ? 2434 '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' . 3.1023 3.1587 2760 0.2778 100.00 0.3188 . . 114 . . . . 'X-RAY DIFFRACTION' . 3.1587 3.2194 2689 0.2727 100.00 0.2990 . . 175 . . . . 'X-RAY DIFFRACTION' . 3.2194 3.2851 2693 0.2706 100.00 0.3085 . . 129 . . . . 'X-RAY DIFFRACTION' . 3.2851 3.3565 2745 0.2657 100.00 0.3369 . . 151 . . . . 'X-RAY DIFFRACTION' . 3.3565 3.4345 2738 0.2756 100.00 0.3165 . . 133 . . . . 'X-RAY DIFFRACTION' . 3.4345 3.5204 2752 0.2525 100.00 0.2904 . . 149 . . . . 'X-RAY DIFFRACTION' . 3.5204 3.6155 2700 0.2383 100.00 0.3297 . . 143 . . . . 'X-RAY DIFFRACTION' . 3.6155 3.7218 2752 0.2265 100.00 0.2944 . . 127 . . . . 'X-RAY DIFFRACTION' . 3.7218 3.8419 2744 0.2245 100.00 0.2941 . . 120 . . . . 'X-RAY DIFFRACTION' . 3.8419 3.9791 2732 0.2226 100.00 0.2448 . . 150 . . . . 'X-RAY DIFFRACTION' . 3.9791 4.1383 2764 0.2049 100.00 0.2534 . . 133 . . . . 'X-RAY DIFFRACTION' . 4.1383 4.3265 2783 0.1961 100.00 0.2358 . . 140 . . . . 'X-RAY DIFFRACTION' . 4.3265 4.5543 2722 0.1724 100.00 0.2345 . . 140 . . . . 'X-RAY DIFFRACTION' . 4.5543 4.8393 2779 0.1614 100.00 0.1996 . . 155 . . . . 'X-RAY DIFFRACTION' . 4.8393 5.2123 2758 0.1684 100.00 0.2484 . . 164 . . . . 'X-RAY DIFFRACTION' . 5.2123 5.7357 2752 0.1897 100.00 0.2204 . . 157 . . . . 'X-RAY DIFFRACTION' . 5.7357 6.5631 2824 0.2092 100.00 0.2704 . . 147 . . . . 'X-RAY DIFFRACTION' . 6.5631 8.2588 2840 0.2101 100.00 0.2499 . . 156 . . . . 'X-RAY DIFFRACTION' . 8.2588 42.4884 2952 0.1782 98.00 0.2431 . . 123 . . . . # _struct.entry_id 4MMZ _struct.title 'Integrin AlphaVBeta3 ectodomain bound to an antagonistic tenth domain of Fibronectin' _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 4MMZ _struct_keywords.pdbx_keywords 'CELL ADHESION' _struct_keywords.text ;integrin, A domain, hybrid domain, PSI, EGF repeats, beta tail, calf, 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 4 ? G N N 4 ? H N N 4 ? I N N 5 ? J N N 6 ? K N N 5 ? L N N 6 ? M N N 4 ? N N N 4 ? O N N 4 ? P N N 4 ? Q N N 4 ? R N N 4 ? S N N 4 ? T N N 4 ? U N N 7 ? V N N 7 ? W N N 7 ? X N N 7 ? Y N N 7 ? Z N N 8 ? AA N N 9 ? BA N N 4 ? CA N N 4 ? DA N N 4 ? EA N N 4 ? FA N N 4 ? GA N N 4 ? HA N N 5 ? IA N N 7 ? JA N N 7 ? KA N N 7 ? LA N N 8 ? MA N N 10 ? NA N N 10 ? OA N N 9 ? PA N N 11 ? QA N N 11 ? RA N N 11 ? # _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 ARG A 245 ? LEU A 250 ? ARG A 245 LEU A 250 1 ? 6 HELX_P HELX_P5 5 GLY A 366 ? LYS A 370 ? GLY A 366 LYS A 370 5 ? 5 HELX_P HELX_P6 6 SER B 12 ? ALA B 18 ? SER B 12 ALA B 18 1 ? 7 HELX_P HELX_P7 7 LEU B 40 ? ASP B 47 ? LEU B 40 ASP B 47 1 ? 8 HELX_P HELX_P8 8 SER B 121 ? SER B 123 ? SER B 121 SER B 123 5 ? 3 HELX_P HELX_P9 9 MET B 124 ? ILE B 131 ? MET B 124 ILE B 131 1 ? 8 HELX_P HELX_P10 10 ASN B 133 ? THR B 146 ? ASN B 133 THR B 146 1 ? 14 HELX_P HELX_P11 11 VAL B 200 ? VAL B 207 ? VAL B 200 VAL B 207 1 ? 8 HELX_P HELX_P12 12 GLY B 222 ? CYS B 232 ? GLY B 222 CYS B 232 1 ? 11 HELX_P HELX_P13 13 CYS B 232 ? GLY B 237 ? CYS B 232 GLY B 237 1 ? 6 HELX_P HELX_P14 14 LEU B 258 ? LEU B 262 ? LEU B 258 LEU B 262 5 ? 5 HELX_P HELX_P15 15 TYR B 281 ? THR B 285 ? TYR B 281 THR B 285 5 ? 5 HELX_P HELX_P16 16 SER B 291 ? LYS B 302 ? SER B 291 LYS B 302 1 ? 12 HELX_P HELX_P17 17 VAL B 314 ? GLU B 323 ? VAL B 314 GLU B 323 1 ? 10 HELX_P HELX_P18 18 ASN B 339 ? ARG B 352 ? ASN B 339 ARG B 352 1 ? 14 HELX_P HELX_P19 19 ALA B 436 ? ALA B 441 ? ALA B 436 ALA B 441 5 ? 6 HELX_P HELX_P20 20 SER B 445 ? ASN B 449 ? SER B 445 ASN B 449 5 ? 5 HELX_P HELX_P21 21 PRO B 493 ? GLN B 497 ? PRO B 493 GLN B 497 5 ? 5 HELX_P HELX_P22 22 GLU B 534 ? GLY B 538 ? GLU B 534 GLY B 538 5 ? 5 HELX_P HELX_P23 23 THR B 564 ? MET B 568 ? THR B 564 MET B 568 5 ? 5 HELX_P HELX_P24 24 LEU B 573 ? GLY B 577 ? LEU B 573 GLY B 577 5 ? 5 HELX_P HELX_P25 25 ASP B 606 ? LYS B 611 ? ASP B 606 LYS B 611 1 ? 6 HELX_P HELX_P26 26 LYS B 611 ? PHE B 620 ? LYS B 611 PHE B 620 1 ? 10 # _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 ? ? ? ? ? ? ? 2.033 ? disulf2 disulf ? ? A CYS 108 SG ? ? ? 1_555 A CYS 128 SG ? ? A CYS 108 A CYS 128 1_555 ? ? ? ? ? ? ? 2.032 ? disulf3 disulf ? ? A CYS 142 SG ? ? ? 1_555 A CYS 155 SG ? ? A CYS 142 A CYS 155 1_555 ? ? ? ? ? ? ? 2.036 ? disulf4 disulf ? ? A CYS 478 SG ? ? ? 1_555 A CYS 535 SG ? ? A CYS 478 A CYS 535 1_555 ? ? ? ? ? ? ? 2.031 ? disulf5 disulf ? ? A CYS 596 SG ? ? ? 1_555 A CYS 602 SG ? ? A CYS 596 A CYS 602 1_555 ? ? ? ? ? ? ? 2.032 ? disulf6 disulf ? ? A CYS 668 SG ? ? ? 1_555 A CYS 681 SG ? ? A CYS 668 A CYS 681 1_555 ? ? ? ? ? ? ? 2.033 ? disulf7 disulf ? ? A CYS 822 SG ? ? ? 1_555 A CYS 884 SG ? ? A CYS 822 A CYS 884 1_555 ? ? ? ? ? ? ? 2.029 ? disulf8 disulf ? ? A CYS 874 SG ? ? ? 1_555 A CYS 879 SG ? ? A CYS 874 A CYS 879 1_555 ? ? ? ? ? ? ? 2.031 ? disulf9 disulf ? ? B CYS 5 SG ? ? ? 1_555 B CYS 23 SG ? ? B CYS 5 B CYS 23 1_555 ? ? ? ? ? ? ? 2.030 ? disulf10 disulf ? ? B CYS 13 SG ? ? ? 1_555 B CYS 435 SG ? ? B CYS 13 B CYS 435 1_555 ? ? ? ? ? ? ? 2.031 ? disulf11 disulf ? ? B CYS 16 SG ? ? ? 1_555 B CYS 38 SG ? ? B CYS 16 B CYS 38 1_555 ? ? ? ? ? ? ? 2.029 ? disulf12 disulf ? ? B CYS 26 SG ? ? ? 1_555 B CYS 49 SG ? ? B CYS 26 B CYS 49 1_555 ? ? ? ? ? ? ? 2.030 ? disulf13 disulf ? ? B CYS 177 SG ? ? ? 1_555 B CYS 184 SG ? ? B CYS 177 B CYS 184 1_555 ? ? ? ? ? ? ? 2.032 ? disulf14 disulf ? ? B CYS 232 SG ? ? ? 1_555 B CYS 273 SG ? ? B CYS 232 B CYS 273 1_555 ? ? ? ? ? ? ? 2.034 ? disulf15 disulf ? ? B CYS 374 SG ? ? ? 1_555 B CYS 386 SG ? ? B CYS 374 B CYS 386 1_555 ? ? ? ? ? ? ? 2.031 ? disulf16 disulf ? ? B CYS 406 SG ? ? ? 1_555 B CYS 433 SG ? ? B CYS 406 B CYS 433 1_555 ? ? ? ? ? ? ? 2.029 ? disulf17 disulf ? ? B CYS 437 SG ? ? ? 1_555 B CYS 457 SG ? ? B CYS 437 B CYS 457 1_555 ? ? ? ? ? ? ? 2.032 ? disulf18 disulf ? ? B CYS 448 SG ? ? ? 1_555 B CYS 460 SG ? ? B CYS 448 B CYS 460 1_555 ? ? ? ? ? ? ? 2.033 ? disulf19 disulf ? ? B CYS 462 SG ? ? ? 1_555 B CYS 471 SG ? ? B CYS 462 B CYS 471 1_555 ? ? ? ? ? ? ? 2.034 ? disulf20 disulf ? ? B CYS 473 SG ? ? ? 1_555 B CYS 503 SG ? ? B CYS 473 B CYS 503 1_555 ? ? ? ? ? ? ? 2.032 ? disulf21 disulf ? ? B CYS 486 SG ? ? ? 1_555 B CYS 501 SG ? ? B CYS 486 B CYS 501 1_555 ? ? ? ? ? ? ? 2.034 ? disulf22 disulf ? ? B CYS 495 SG ? ? ? 1_555 B CYS 506 SG ? ? B CYS 495 B CYS 506 1_555 ? ? ? ? ? ? ? 2.025 ? disulf23 disulf ? ? B CYS 508 SG ? ? ? 1_555 B CYS 521 SG ? ? B CYS 508 B CYS 521 1_555 ? ? ? ? ? ? ? 2.032 ? disulf24 disulf ? ? B CYS 523 SG ? ? ? 1_555 B CYS 544 SG ? ? B CYS 523 B CYS 544 1_555 ? ? ? ? ? ? ? 2.031 ? disulf25 disulf ? ? B CYS 528 SG ? ? ? 1_555 B CYS 542 SG ? ? B CYS 528 B CYS 542 1_555 ? ? ? ? ? ? ? 2.032 ? disulf26 disulf ? ? B CYS 536 SG ? ? ? 1_555 B CYS 547 SG ? ? B CYS 536 B CYS 547 1_555 ? ? ? ? ? ? ? 2.032 ? disulf27 disulf ? ? B CYS 549 SG ? ? ? 1_555 B CYS 558 SG ? ? B CYS 549 B CYS 558 1_555 ? ? ? ? ? ? ? 2.033 ? disulf28 disulf ? ? B CYS 560 SG ? ? ? 1_555 B CYS 583 SG ? ? B CYS 560 B CYS 583 1_555 ? ? ? ? ? ? ? 2.034 ? disulf29 disulf ? ? B CYS 567 SG ? ? ? 1_555 B CYS 581 SG ? ? B CYS 567 B CYS 581 1_555 ? ? ? ? ? ? ? 2.036 ? disulf30 disulf ? ? B CYS 575 SG ? ? ? 1_555 B CYS 586 SG ? ? B CYS 575 B CYS 586 1_555 ? ? ? ? ? ? ? 2.034 ? disulf31 disulf ? ? B CYS 588 SG ? ? ? 1_555 B CYS 598 SG ? ? B CYS 588 B CYS 598 1_555 ? ? ? ? ? ? ? 2.035 ? disulf32 disulf ? ? B CYS 601 SG ? ? ? 1_555 B CYS 604 SG ? ? B CYS 601 B CYS 604 1_555 ? ? ? ? ? ? ? 2.032 ? disulf33 disulf ? ? B CYS 608 SG ? ? ? 1_555 B CYS 655 SG ? ? B CYS 608 B CYS 655 1_555 ? ? ? ? ? ? ? 2.032 ? disulf34 disulf ? ? B CYS 614 SG ? ? ? 1_555 B CYS 635 SG ? ? B CYS 614 B CYS 635 1_555 ? ? ? ? ? ? ? 2.033 ? disulf35 disulf ? ? B CYS 617 SG ? ? ? 1_555 B CYS 631 SG ? ? B CYS 617 B CYS 631 1_555 ? ? ? ? ? ? ? 2.035 ? disulf36 disulf ? ? B CYS 663 SG ? ? ? 1_555 B CYS 687 SG ? ? B CYS 663 B CYS 687 1_555 ? ? ? ? ? ? ? 2.035 ? covale1 covale ? ? A ASN 458 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 458 A NAG 1010 1_555 ? ? ? ? ? ? ? 1.431 ? covale2 covale ? ? A ASN 266 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 266 A NAG 1004 1_555 ? ? ? ? ? ? ? 1.434 ? covale3 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 1004 A NAG 1005 1_555 ? ? ? ? ? ? ? 1.435 ? covale4 covale ? ? B ASN 320 ND2 ? ? ? 1_555 CA NAG . C1 ? ? B ASN 320 B NAG 702 1_555 ? ? ? ? ? ? ? 1.437 ? covale5 covale ? ? A ASN 821 ND2 ? ? ? 1_555 Q NAG . C1 ? ? A ASN 821 A NAG 1014 1_555 ? ? ? ? ? ? ? 1.437 ? covale6 covale ? ? FA NAG . O4 ? ? ? 1_555 GA NAG . C1 ? ? B NAG 705 B NAG 706 1_555 ? ? ? ? ? ? ? 1.437 ? covale7 covale ? ? H NAG . O4 ? ? ? 1_555 I BMA . C1 ? ? A NAG 1005 A BMA 1006 1_555 ? ? ? ? ? ? ? 1.438 ? covale8 covale ? ? B ASN 559 ND2 ? ? ? 1_555 FA NAG . C1 ? ? B ASN 559 B NAG 705 1_555 ? ? ? ? ? ? ? 1.439 ? covale9 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? A NAG 1010 A NAG 1011 1_555 ? ? ? ? ? ? ? 1.439 ? covale10 covale ? ? I BMA . O3 ? ? ? 1_555 J MAN . C1 ? ? A BMA 1006 A MAN 1007 1_555 ? ? ? ? ? ? ? 1.440 ? covale11 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1001 A NAG 1002 1_555 ? ? ? ? ? ? ? 1.440 ? covale12 covale ? ? A ASN 585 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 585 A NAG 1012 1_555 ? ? ? ? ? ? ? 1.440 ? covale13 covale ? ? A ASN 943 ND2 ? ? ? 1_555 S NAG . C1 ? ? A ASN 943 A NAG 1016 1_555 ? ? ? ? ? ? ? 1.440 ? covale14 covale ? ? A ASN 805 ND2 ? ? ? 1_555 P NAG . C1 ? ? A ASN 805 A NAG 1013 1_555 ? ? ? ? ? ? ? 1.440 ? covale15 covale ? ? K BMA . O4 ? ? ? 1_555 L MAN . C1 ? ? A BMA 1008 A MAN 1009 1_555 ? ? ? ? ? ? ? 1.441 ? covale16 covale ? ? A ASN 950 ND2 ? ? ? 1_555 T NAG . C1 ? ? A ASN 950 A NAG 1017 1_555 ? ? ? ? ? ? ? 1.441 ? covale17 covale ? ? A ASN 44 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 44 A NAG 1001 1_555 ? ? ? ? ? ? ? 1.441 ? covale18 covale ? ? GA NAG . O4 ? ? ? 1_555 HA BMA . C1 ? ? B NAG 706 B BMA 707 1_555 ? ? ? ? ? ? ? 1.442 ? covale19 covale ? ? A ASN 260 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 260 A NAG 1003 1_555 ? ? ? ? ? ? ? 1.444 ? covale20 covale ? ? I BMA . O6 ? ? ? 1_555 K BMA . C1 ? ? A BMA 1006 A BMA 1008 1_555 ? ? ? ? ? ? ? 1.445 ? covale21 covale ? ? B ASN 371 ND2 ? ? ? 1_555 DA NAG . C1 ? ? B ASN 371 B NAG 703 1_555 ? ? ? ? ? ? ? 1.445 ? covale22 covale ? ? B ASN 99 ND2 ? ? ? 1_555 BA NAG . C1 ? ? B ASN 99 B NAG 701 1_555 ? ? ? ? ? ? ? 1.446 ? covale23 covale ? ? Q NAG . O4 ? ? ? 1_555 R NAG . C1 ? ? A NAG 1014 A NAG 1015 1_555 ? ? ? ? ? ? ? 1.450 ? covale24 covale ? ? DA NAG . O4 ? ? ? 1_555 EA NAG . C1 ? ? B NAG 703 B NAG 704 1_555 ? ? ? ? ? ? ? 1.452 ? metalc1 metalc ? ? B PRO 219 O ? ? ? 1_555 KA MN . MN ? ? B PRO 219 B MN 710 1_555 ? ? ? ? ? ? ? 2.070 ? metalc2 metalc ? ? A ASP 238 OD1 ? ? ? 1_555 U MN . MN ? ? A ASP 238 A MN 1018 1_555 ? ? ? ? ? ? ? 2.074 ? metalc3 metalc ? ? A TYR 419 O ? ? ? 1_555 X MN . MN ? ? A TYR 419 A MN 1021 1_555 ? ? ? ? ? ? ? 2.077 ? metalc4 metalc ? ? A TYR 290 O ? ? ? 1_555 V MN . MN ? ? A TYR 290 A MN 1019 1_555 ? ? ? ? ? ? ? 2.086 ? metalc5 metalc ? ? A ASP 284 OD1 ? ? ? 1_555 V MN . MN ? ? A ASP 284 A MN 1019 1_555 ? ? ? ? ? ? ? 2.098 ? metalc6 metalc ? ? A ASP 234 OD1 ? ? ? 1_555 U MN . MN ? ? A ASP 234 A MN 1018 1_555 ? ? ? ? ? ? ? 2.131 ? metalc7 metalc ? ? A ASP 234 OD2 ? ? ? 1_555 U MN . MN ? ? A ASP 234 A MN 1018 1_555 ? ? ? ? ? ? ? 2.135 ? metalc8 metalc ? ? A ASP 599 OD1 ? ? ? 1_555 Y MN . MN ? ? A ASP 599 A MN 1022 1_555 ? ? ? ? ? ? ? 2.140 ? metalc9 metalc ? ? A ASP 349 OD1 ? ? ? 1_555 W MN . MN ? ? A ASP 349 A MN 1020 1_555 ? ? ? ? ? ? ? 2.144 ? metalc10 metalc ? ? B ASP 127 OD1 ? ? ? 1_555 JA MN . MN ? ? B ASP 127 B MN 709 1_555 ? ? ? ? ? ? ? 2.144 ? metalc11 metalc ? ? B ASP 126 OD1 ? ? ? 1_555 JA MN . MN ? ? B ASP 126 B MN 709 1_555 ? ? ? ? ? ? ? 2.145 ? metalc12 metalc ? ? A GLU 636 OE1 ? ? ? 1_555 Y MN . MN ? ? A GLU 636 A MN 1022 1_555 ? ? ? ? ? ? ? 2.146 ? metalc13 metalc ? ? A ASP 353 OD1 ? ? ? 1_555 W MN . MN ? ? A ASP 353 A MN 1020 1_555 ? ? ? ? ? ? ? 2.151 ? metalc14 metalc ? ? B GLU 220 OE1 ? ? ? 1_555 IA MN . MN ? ? B GLU 220 B MN 708 1_555 ? ? ? ? ? ? ? 2.151 ? metalc15 metalc ? ? A GLU 636 OE2 ? ? ? 1_555 Y MN . MN ? ? A GLU 636 A MN 1022 1_555 ? ? ? ? ? ? ? 2.152 ? metalc16 metalc ? ? B ASP 217 OD1 ? ? ? 1_555 KA MN . MN ? ? B ASP 217 B MN 710 1_555 ? ? ? ? ? ? ? 2.154 ? metalc17 metalc ? ? A ASP 357 OD1 ? ? ? 1_555 W MN . MN ? ? A ASP 357 A MN 1020 1_555 ? ? ? ? ? ? ? 2.157 ? metalc18 metalc ? ? A ASP 599 OD2 ? ? ? 1_555 Y MN . MN ? ? A ASP 599 A MN 1022 1_555 ? ? ? ? ? ? ? 2.157 ? metalc19 metalc ? ? B GLU 220 OE2 ? ? ? 1_555 KA MN . MN ? ? B GLU 220 B MN 710 1_555 ? ? ? ? ? ? ? 2.158 ? metalc20 metalc ? ? A ASN 232 OD1 ? ? ? 1_555 U MN . MN ? ? A ASN 232 A MN 1018 1_555 ? ? ? ? ? ? ? 2.158 ? metalc21 metalc ? ? A ASP 292 OD1 ? ? ? 1_555 V MN . MN ? ? A ASP 292 A MN 1019 1_555 ? ? ? ? ? ? ? 2.160 ? metalc22 metalc ? ? A ASP 351 OD1 ? ? ? 1_555 W MN . MN ? ? A ASP 351 A MN 1020 1_555 ? ? ? ? ? ? ? 2.163 ? metalc23 metalc ? ? C ASP 79 OD1 ? ? ? 1_555 IA MN . MN ? ? C ASP 1495 B MN 708 1_555 ? ? ? ? ? ? ? 2.164 ? metalc24 metalc ? ? A ASP 292 OD2 ? ? ? 1_555 V MN . MN ? ? A ASP 292 A MN 1019 1_555 ? ? ? ? ? ? ? 2.169 ? metalc25 metalc ? ? A ASP 415 OD1 ? ? ? 1_555 X MN . MN ? ? A ASP 415 A MN 1021 1_555 ? ? ? ? ? ? ? 2.169 ? metalc26 metalc ? ? A ASP 357 OD2 ? ? ? 1_555 W MN . MN ? ? A ASP 357 A MN 1020 1_555 ? ? ? ? ? ? ? 2.174 ? metalc27 metalc ? ? B ASP 158 OD2 ? ? ? 1_555 KA MN . MN ? ? B ASP 158 B MN 710 1_555 ? ? ? ? ? ? ? 2.180 ? metalc28 metalc ? ? A ASP 421 OD1 ? ? ? 1_555 X MN . MN ? ? A ASP 421 A MN 1021 1_555 ? ? ? ? ? ? ? 2.185 ? metalc29 metalc ? ? B SER 121 OG ? ? ? 1_555 IA MN . MN ? ? B SER 121 B MN 708 1_555 ? ? ? ? ? ? ? 2.189 ? metalc30 metalc ? ? A ASP 421 OD2 ? ? ? 1_555 X MN . MN ? ? A ASP 421 A MN 1021 1_555 ? ? ? ? ? ? ? 2.189 ? metalc31 metalc ? ? B ASP 126 OD2 ? ? ? 1_555 JA MN . MN ? ? B ASP 126 B MN 709 1_555 ? ? ? ? ? ? ? 2.190 ? metalc32 metalc ? ? B ASP 217 O ? ? ? 1_555 KA MN . MN ? ? B ASP 217 B MN 710 1_555 ? ? ? ? ? ? ? 2.195 ? metalc33 metalc ? ? B SER 123 O ? ? ? 1_555 JA MN . MN ? ? B SER 123 B MN 709 1_555 ? ? ? ? ? ? ? 2.198 ? metalc34 metalc ? ? A ASN 286 OD1 ? ? ? 1_555 V MN . MN ? ? A ASN 286 A MN 1019 1_555 ? ? ? ? ? ? ? 2.200 ? metalc35 metalc ? ? A ASP 230 OD1 ? ? ? 1_555 U MN . MN ? ? A ASP 230 A MN 1018 1_555 ? ? ? ? ? ? ? 2.204 ? metalc36 metalc ? ? B ASN 215 OD1 ? ? ? 1_555 KA MN . MN ? ? B ASN 215 B MN 710 1_555 ? ? ? ? ? ? ? 2.208 ? metalc37 metalc ? ? A ASN 417 OD1 ? ? ? 1_555 X MN . MN ? ? A ASN 417 A MN 1021 1_555 ? ? ? ? ? ? ? 2.214 ? metalc38 metalc ? ? A ASP 238 OD2 ? ? ? 1_555 U MN . MN ? ? A ASP 238 A MN 1018 1_555 ? ? ? ? ? ? ? 2.215 ? metalc39 metalc ? ? A ASP 288 OD1 ? ? ? 1_555 V MN . MN ? ? A ASP 288 A MN 1019 1_555 ? ? ? ? ? ? ? 2.220 ? metalc40 metalc ? ? A VAL 601 O ? ? ? 1_555 Y MN . MN ? ? A VAL 601 A MN 1022 1_555 ? ? ? ? ? ? ? 2.236 ? metalc41 metalc ? ? A ASP 413 OD1 ? ? ? 1_555 X MN . MN ? ? A ASP 413 A MN 1021 1_555 ? ? ? ? ? ? ? 2.277 ? metalc42 metalc ? ? A PHE 355 O ? ? ? 1_555 W MN . MN ? ? A PHE 355 A MN 1020 1_555 ? ? ? ? ? ? ? 2.304 ? metalc43 metalc ? ? A SER 546 O ? ? ? 1_555 Z NA . NA ? ? A SER 546 A NA 1023 1_555 ? ? ? ? ? ? ? 2.415 ? metalc44 metalc ? ? A ASP 544 OD1 ? ? ? 1_555 Z NA . NA ? ? A ASP 544 A NA 1023 1_555 ? ? ? ? ? ? ? 2.419 ? metalc45 metalc ? ? B ASN 654 OD1 ? ? ? 1_555 LA NA . NA ? ? B ASN 654 B NA 711 1_555 ? ? ? ? ? ? ? 2.440 ? metalc46 metalc ? ? A CYS 596 O ? ? ? 1_555 Y MN . MN ? ? A CYS 596 A MN 1022 1_555 ? ? ? ? ? ? ? 2.446 ? metalc47 metalc ? ? A ASN 417 ND2 ? ? ? 1_555 X MN . MN ? ? A ASN 417 A MN 1021 1_555 ? ? ? ? ? ? ? 2.508 ? metalc48 metalc ? ? A ILE 236 O ? ? ? 1_555 U MN . MN ? ? A ILE 236 A MN 1018 1_555 ? ? ? ? ? ? ? 2.542 ? metalc49 metalc ? ? B MET 335 O ? ? ? 1_555 JA MN . MN ? ? B MET 335 B MN 709 1_555 ? ? ? ? ? ? ? 2.580 ? metalc50 metalc ? ? IA MN . MN ? ? ? 1_555 QA HOH . O ? ? B MN 708 B HOH 801 1_555 ? ? ? ? ? ? ? 2.175 ? metalc51 metalc ? ? IA MN . MN ? ? ? 1_555 QA HOH . O ? ? B MN 708 B HOH 802 1_555 ? ? ? ? ? ? ? 2.180 ? metalc52 metalc ? ? IA MN . MN ? ? ? 1_555 RA HOH . O ? ? B MN 708 C HOH 1701 1_555 ? ? ? ? ? ? ? 2.193 ? metalc53 metalc ? ? JA MN . MN ? ? ? 1_555 RA HOH . O ? ? B MN 709 C HOH 1702 1_555 ? ? ? ? ? ? ? 2.199 ? # 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 -10.49 2 ASN 685 A . ? ASN 685 A PRO 686 A ? PRO 686 A 1 2.44 3 SER 749 A . ? SER 749 A PRO 750 A ? PRO 750 A 1 3.33 4 LEU 755 A . ? LEU 755 A PRO 756 A ? PRO 756 A 1 1.43 5 SER 84 B . ? SER 84 B PRO 85 B ? PRO 85 B 1 -1.16 6 SER 162 B . ? SER 162 B PRO 163 B ? PRO 163 B 1 -0.21 7 SER 168 B . ? SER 168 B PRO 169 B ? PRO 169 B 1 2.53 # 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 ? 4 ? L ? 5 ? M ? 2 ? N ? 2 ? O ? 4 ? P ? 6 ? Q ? 4 ? R ? 6 ? S ? 4 ? T ? 6 ? U ? 4 ? V ? 6 ? W ? 2 ? X ? 2 ? Y ? 2 ? Z ? 2 ? AA ? 4 ? AB ? 3 ? AC ? 4 ? AD ? 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 ? 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 N 1 2 ? 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 ? anti-parallel R 1 2 ? parallel R 2 3 ? anti-parallel R 3 4 ? anti-parallel R 4 5 ? anti-parallel R 5 6 ? anti-parallel S 1 2 ? anti-parallel S 2 3 ? anti-parallel S 3 4 ? parallel T 1 2 ? anti-parallel T 2 3 ? parallel T 3 4 ? anti-parallel T 4 5 ? anti-parallel T 5 6 ? anti-parallel U 1 2 ? anti-parallel U 2 3 ? anti-parallel U 3 4 ? anti-parallel V 1 2 ? anti-parallel V 2 3 ? parallel V 3 4 ? parallel V 4 5 ? parallel V 5 6 ? parallel W 1 2 ? anti-parallel X 1 2 ? anti-parallel Y 1 2 ? anti-parallel Z 1 2 ? anti-parallel AA 1 2 ? parallel AA 2 3 ? anti-parallel AA 3 4 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AC 1 2 ? anti-parallel AC 2 3 ? anti-parallel AC 3 4 ? anti-parallel AD 1 2 ? anti-parallel AD 2 3 ? anti-parallel AD 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 ALA A 9 ? SER A 12 ? ALA A 9 SER A 12 A 2 ARG A 431 ? TYR A 435 ? ARG A 431 TYR A 435 A 3 ASP A 421 ? GLY A 425 ? ASP A 421 GLY A 425 A 4 MET A 408 ? THR A 412 ? MET A 408 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 ILE A 161 ? PHE A 163 ? ILE A 161 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 ? LEU A 319 ? GLN A 314 LEU A 319 G 4 GLN A 327 ? ASN A 332 ? GLN A 327 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 ? LEU A 347 ? ALA A 343 LEU A 347 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 ? GLU A 392 ? GLN A 389 GLU A 392 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 GLN A 534 ? LEU A 538 ? GLN A 534 LEU A 538 K 2 ASN A 474 ? ASP A 482 ? ASN A 474 ASP A 482 K 3 VAL A 440 ? TYR A 450 ? VAL A 440 TYR A 450 K 4 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 ? LEU A 563 ? ILE A 555 LEU A 563 L 4 LYS A 490 ? LEU A 498 ? LYS A 490 LEU A 498 L 5 SER A 520 ? SER A 528 ? SER A 520 SER A 528 M 1 CYS A 461 ? SER A 462 ? CYS A 461 SER A 462 M 2 LYS A 469 ? VAL A 470 ? LYS A 469 VAL A 470 N 1 ALA A 511 ? LEU A 512 ? ALA A 511 LEU A 512 N 2 TYR A 541 ? LEU A 542 ? TYR A 541 LEU A 542 O 1 LEU A 606 ? ASP A 611 ? LEU A 606 ASP A 611 O 2 PRO A 624 ? ASN A 633 ? PRO A 624 ASN A 633 O 3 GLN A 692 ? SER A 700 ? GLN A 692 SER A 700 O 4 PHE A 653 ? ILE A 654 ? PHE A 653 ILE A 654 P 1 LYS A 616 ? TYR A 618 ? LYS A 616 TYR A 618 P 2 VAL A 730 ? ALA A 737 ? VAL A 730 ALA A 737 P 3 SER A 710 ? GLN A 718 ? SER A 710 GLN A 718 P 4 ALA A 641 ? SER A 646 ? ALA A 641 SER A 646 P 5 ARG A 677 ? GLY A 684 ? ARG A 677 GLY A 684 P 6 SER A 667 ? THR A 672 ? SER A 667 THR A 672 Q 1 VAL A 742 ? SER A 749 ? VAL A 742 SER A 749 Q 2 VAL A 775 ? ASN A 784 ? VAL A 775 ASN A 784 Q 3 SER A 894 ? LEU A 903 ? SER A 894 LEU A 903 Q 4 LEU A 809 ? ASP A 817 ? LEU A 809 ASP A 817 R 1 HIS A 752 ? PHE A 754 ? HIS A 752 PHE A 754 R 2 ILE A 941 ? THR A 952 ? ILE A 941 THR A 952 R 3 TYR A 918 ? GLU A 930 ? TYR A 918 GLU A 930 R 4 LYS A 792 ? TYR A 803 ? LYS A 792 TYR A 803 R 5 GLN A 878 ? VAL A 886 ? GLN A 878 VAL A 886 R 6 MET A 820 ? SER A 824 ? MET A 820 SER A 824 S 1 ASN A 806 ? THR A 807 ? ASN A 806 THR A 807 S 2 LYS A 792 ? TYR A 803 ? LYS A 792 TYR A 803 S 3 TYR A 918 ? GLU A 930 ? TYR A 918 GLU A 930 S 4 THR A 871 ? LEU A 872 ? THR A 871 LEU A 872 T 1 VAL B 63 ? GLU B 65 ? VAL B 63 GLU B 65 T 2 ARG B 87 ? LEU B 92 ? ARG B 87 LEU B 92 T 3 LEU B 425 ? PHE B 431 ? LEU B 425 PHE B 431 T 4 PHE B 414 ? PRO B 418 ? PHE B 414 PRO B 418 T 5 VAL B 355 ? ARG B 360 ? VAL B 355 ARG B 360 T 6 SER B 385 ? CYS B 386 ? SER B 385 CYS B 386 U 1 VAL B 83 ? SER B 84 ? VAL B 83 SER B 84 U 2 SER B 97 ? ARG B 105 ? SER B 97 ARG B 105 U 3 THR B 394 ? VAL B 403 ? THR B 394 VAL B 403 U 4 LEU B 366 ? THR B 373 ? LEU B 366 THR B 373 V 1 TYR B 190 ? THR B 197 ? TYR B 190 THR B 197 V 2 LEU B 149 ? PHE B 156 ? LEU B 149 PHE B 156 V 3 VAL B 112 ? ASP B 119 ? VAL B 112 ASP B 119 V 4 SER B 243 ? THR B 250 ? SER B 243 THR B 250 V 5 ILE B 304 ? VAL B 310 ? ILE B 304 VAL B 310 V 6 THR B 329 ? VAL B 332 ? THR B 329 VAL B 332 W 1 ILE B 516 ? THR B 517 ? ILE B 516 THR B 517 W 2 CYS B 523 ? ASP B 524 ? CYS B 523 ASP B 524 X 1 GLY B 540 ? SER B 543 ? GLY B 540 SER B 543 X 2 ASP B 546 ? CYS B 549 ? ASP B 546 CYS B 549 Y 1 TRP B 553 ? THR B 554 ? TRP B 553 THR B 554 Y 2 CYS B 560 ? THR B 561 ? CYS B 560 THR B 561 Z 1 GLY B 579 ? GLU B 582 ? GLY B 579 GLU B 582 Z 2 SER B 585 ? CYS B 588 ? SER B 585 CYS B 588 AA 1 GLU B 638 ? VAL B 642 ? GLU B 638 VAL B 642 AA 2 SER B 677 ? VAL B 682 ? SER B 677 VAL B 682 AA 3 VAL B 664 ? GLU B 671 ? VAL B 664 GLU B 671 AA 4 ALA B 652 ? LYS B 658 ? ALA B 652 LYS B 658 AB 1 ARG C 5 ? VAL C 9 ? ARG C 1421 VAL C 1425 AB 2 ILE C 19 ? ASP C 22 ? ILE C 1435 ASP C 1438 AB 3 THR C 55 ? ALA C 56 ? THR C 1471 ALA C 1472 AC 1 GLU C 46 ? PRO C 50 ? GLU C 1462 PRO C 1466 AC 2 TYR C 30 ? TYR C 35 ? TYR C 1446 TYR C 1451 AC 3 TYR C 67 ? THR C 75 ? TYR C 1483 THR C 1491 AC 4 ASN C 81 ? GLU C 82 ? ASN C 1497 GLU C 1498 AD 1 GLU C 46 ? PRO C 50 ? GLU C 1462 PRO C 1466 AD 2 TYR C 30 ? TYR C 35 ? TYR C 1446 TYR C 1451 AD 3 TYR C 67 ? THR C 75 ? TYR C 1483 THR C 1491 AD 4 ILE C 87 ? TYR C 91 ? ILE C 1503 TYR C 1507 # 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 ILE A 433 ? O ILE A 433 N VAL A 424 ? N VAL A 424 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 LEU A 36 ? N LEU A 36 O CYS A 59 ? O CYS A 59 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 LEU A 171 ? N LEU A 171 O ILE A 184 ? O ILE A 184 E 3 4 N SER A 185 ? N SER A 185 O LEU A 208 ? O LEU A 208 F 1 2 N GLY A 229 ? N GLY A 229 O ASP A 238 ? O ASP A 238 F 2 3 N VAL A 243 ? N VAL A 243 O MET A 252 ? O MET A 252 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 ILE A 295 ? N ILE A 295 O SER A 316 ? O SER A 316 G 3 4 N VAL A 317 ? N VAL A 317 O THR A 329 ? O THR A 329 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 358 ? N ILE A 358 O PHE A 376 ? O PHE A 376 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 O GLN A 534 ? O GLN A 534 N LEU A 479 ? N LEU A 479 K 2 3 O ASN A 474 ? O ASN A 474 N TYR A 450 ? N TYR A 450 K 3 4 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 PHE A 558 ? O PHE A 558 N LEU A 498 ? N LEU A 498 L 4 5 N LEU A 491 ? N LEU A 491 O ILE A 527 ? O ILE A 527 M 1 2 N CYS A 461 ? N CYS A 461 O VAL A 470 ? O VAL A 470 N 1 2 N LEU A 512 ? N LEU A 512 O TYR A 541 ? O TYR A 541 O 1 2 N SER A 609 ? N SER A 609 O LYS A 630 ? O LYS A 630 O 2 3 N LEU A 625 ? N LEU A 625 O PHE A 699 ? O PHE A 699 O 3 4 O ARG A 698 ? O ARG A 698 N ILE A 654 ? N ILE A 654 P 1 2 N ILE A 617 ? N ILE A 617 O ALA A 737 ? O ALA A 737 P 2 3 O VAL A 730 ? O VAL A 730 N LEU A 715 ? N LEU A 715 P 3 4 O GLN A 716 ? O GLN A 716 N ILE A 644 ? N ILE A 644 P 4 5 N LEU A 643 ? N LEU A 643 O CYS A 681 ? O CYS A 681 P 5 6 O ASP A 682 ? O ASP A 682 N SER A 667 ? N SER A 667 Q 1 2 N SER A 749 ? N SER A 749 O GLN A 777 ? O GLN A 777 Q 2 3 N LEU A 782 ? N LEU A 782 O ALA A 895 ? O ALA A 895 Q 3 4 O LEU A 902 ? O LEU A 902 N TYR A 810 ? N TYR A 810 R 1 2 N VAL A 753 ? N VAL A 753 O ASN A 950 ? O ASN A 950 R 2 3 O VAL A 947 ? O VAL A 947 N SER A 922 ? N SER A 922 R 3 4 O SER A 923 ? O SER A 923 N GLN A 798 ? N GLN A 798 R 4 5 N ALA A 793 ? N ALA A 793 O VAL A 886 ? O VAL A 886 R 5 6 O VAL A 883 ? O VAL A 883 N THR A 823 ? N THR A 823 S 1 2 O ASN A 806 ? O ASN A 806 N TYR A 803 ? N TYR A 803 S 2 3 N GLN A 798 ? N GLN A 798 O SER A 923 ? O SER A 923 S 3 4 O LYS A 921 ? O LYS A 921 N LEU A 872 ? N LEU A 872 T 1 2 N LEU B 64 ? N LEU B 64 O ARG B 87 ? O ARG B 87 T 2 3 N LEU B 92 ? N LEU B 92 O THR B 430 ? O THR B 430 T 3 4 O LEU B 425 ? O LEU B 425 N ILE B 416 ? N ILE B 416 T 4 5 O LYS B 417 ? O LYS B 417 N GLU B 358 ? N GLU B 358 T 5 6 N VAL B 355 ? N VAL B 355 O CYS B 386 ? O CYS B 386 U 1 2 N SER B 84 ? N SER B 84 O GLN B 103 ? O GLN B 103 U 2 3 N PHE B 100 ? N PHE B 100 O ILE B 399 ? O ILE B 399 U 3 4 O SER B 396 ? O SER B 396 N THR B 373 ? N THR B 373 V 1 2 O LYS B 191 ? O LYS B 191 N ALA B 155 ? N ALA B 155 V 2 3 O GLY B 152 ? O GLY B 152 N TYR B 116 ? N TYR B 116 V 3 4 N LEU B 117 ? N LEU B 117 O VAL B 247 ? O VAL B 247 V 4 5 N PHE B 248 ? N PHE B 248 O ALA B 309 ? O ALA B 309 V 5 6 N PHE B 308 ? N PHE B 308 O THR B 329 ? O THR B 329 W 1 2 N THR B 517 ? N THR B 517 O CYS B 523 ? O CYS B 523 X 1 2 N GLN B 541 ? N GLN B 541 O LEU B 548 ? O LEU B 548 Y 1 2 N THR B 554 ? N THR B 554 O CYS B 560 ? O CYS B 560 Z 1 2 N LYS B 580 ? N LYS B 580 O VAL B 587 ? O VAL B 587 AA 1 2 N GLU B 638 ? N GLU B 638 O LEU B 679 ? O LEU B 679 AA 2 3 O ILE B 678 ? O ILE B 678 N TYR B 670 ? N TYR B 670 AA 3 4 O PHE B 667 ? O PHE B 667 N CYS B 655 ? N CYS B 655 AB 1 2 N GLU C 8 ? N GLU C 1424 O SER C 20 ? O SER C 1436 AB 2 3 N ILE C 19 ? N ILE C 1435 O ALA C 56 ? O ALA C 1472 AC 1 2 O VAL C 49 ? O VAL C 1465 N TYR C 31 ? N TYR C 1447 AC 2 3 N ARG C 32 ? N ARG C 1448 O TYR C 72 ? O TYR C 1488 AC 3 4 N THR C 75 ? N THR C 1491 O ASN C 81 ? O ASN C 1497 AD 1 2 O VAL C 49 ? O VAL C 1465 N TYR C 31 ? N TYR C 1447 AD 2 3 N ARG C 32 ? N ARG C 1448 O TYR C 72 ? O TYR C 1488 AD 3 4 N TYR C 67 ? N TYR C 1483 O TYR C 91 ? O TYR C 1507 # 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 1018' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1019' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1020' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1021' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MN A 1022' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NA A 1023' AC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL A 1024' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN B 708' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN B 709' BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN B 710' BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NA B 711' BC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CL B 712' BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CL B 713' BC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL C 1601' BC6 Software ? ? ? ? 4 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 44 RESIDUES 1001 TO 1002' BC7 Software ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG A1003 BOUND TO ASN A 260' BC8 Software ? ? ? ? 6 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 266 RESIDUES 1004 TO 1009' BC9 Software ? ? ? ? 6 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 458 RESIDUES 1010 TO 1011' CC1 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A1012 BOUND TO ASN A 585' CC2 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A1013 BOUND TO ASN A 805' CC3 Software ? ? ? ? 2 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 821 RESIDUES 1014 TO 1015' CC4 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A1016 BOUND TO ASN A 943' CC5 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A1017 BOUND TO ASN A 950' CC6 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG B 701 BOUND TO ASN B 99' CC7 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG B 702 BOUND TO ASN B 320' CC8 Software ? ? ? ? 4 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 371 RESIDUES 703 TO 704' CC9 Software ? ? ? ? 4 '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 4 ASP A 544 ? ASP A 544 . ? 1_555 ? 26 AC6 4 GLU A 545 ? GLU A 545 . ? 1_555 ? 27 AC6 4 SER A 546 ? SER A 546 . ? 1_555 ? 28 AC6 4 GLU A 547 ? GLU A 547 . ? 1_555 ? 29 AC7 3 ASP A 148 ? ASP A 148 . ? 1_555 ? 30 AC7 3 ASP A 150 ? ASP A 150 . ? 1_555 ? 31 AC7 3 GLU A 930 ? GLU A 930 . ? 5_665 ? 32 AC8 6 SER B 121 ? SER B 121 . ? 1_555 ? 33 AC8 6 GLU B 220 ? GLU B 220 . ? 1_555 ? 34 AC8 6 HOH QA . ? HOH B 801 . ? 1_555 ? 35 AC8 6 HOH QA . ? HOH B 802 . ? 1_555 ? 36 AC8 6 ASP C 79 ? ASP C 1495 . ? 1_555 ? 37 AC8 6 HOH RA . ? HOH C 1701 . ? 1_555 ? 38 AC9 6 SER B 123 ? SER B 123 . ? 1_555 ? 39 AC9 6 MET B 124 ? MET B 124 . ? 1_555 ? 40 AC9 6 ASP B 126 ? ASP B 126 . ? 1_555 ? 41 AC9 6 ASP B 127 ? ASP B 127 . ? 1_555 ? 42 AC9 6 MET B 335 ? MET B 335 . ? 1_555 ? 43 AC9 6 HOH RA . ? HOH C 1702 . ? 1_555 ? 44 BC1 5 ASP B 158 ? ASP B 158 . ? 1_555 ? 45 BC1 5 ASN B 215 ? ASN B 215 . ? 1_555 ? 46 BC1 5 ASP B 217 ? ASP B 217 . ? 1_555 ? 47 BC1 5 PRO B 219 ? PRO B 219 . ? 1_555 ? 48 BC1 5 GLU B 220 ? GLU B 220 . ? 1_555 ? 49 BC2 4 ASP B 647 ? ASP B 647 . ? 1_555 ? 50 BC2 4 ASN B 654 ? ASN B 654 . ? 1_555 ? 51 BC2 4 CL MA . ? CL B 712 . ? 1_555 ? 52 BC2 4 CL NA . ? CL B 713 . ? 1_555 ? 53 BC3 3 LEU B 645 ? LEU B 645 . ? 1_555 ? 54 BC3 3 ASP B 647 ? ASP B 647 . ? 1_555 ? 55 BC3 3 NA LA . ? NA B 711 . ? 1_555 ? 56 BC4 3 ASP B 647 ? ASP B 647 . ? 1_555 ? 57 BC4 3 ASN B 654 ? ASN B 654 . ? 1_555 ? 58 BC4 3 NA LA . ? NA B 711 . ? 1_555 ? 59 BC5 3 THR C 75 ? THR C 1491 . ? 1_555 ? 60 BC5 3 ASN C 81 ? ASN C 1497 . ? 1_555 ? 61 BC5 3 GLU C 82 ? GLU C 1498 . ? 1_555 ? 62 BC6 4 GLU A 15 ? GLU A 15 . ? 1_555 ? 63 BC6 4 LYS A 42 ? LYS A 42 . ? 1_555 ? 64 BC6 4 ASN A 44 ? ASN A 44 . ? 1_555 ? 65 BC6 4 GLU A 52 ? GLU A 52 . ? 1_555 ? 66 BC7 4 ASP A 257 ? ASP A 257 . ? 1_555 ? 67 BC7 4 LYS A 259 ? LYS A 259 . ? 1_555 ? 68 BC7 4 ASN A 260 ? ASN A 260 . ? 1_555 ? 69 BC7 4 SER A 262 ? SER A 262 . ? 1_555 ? 70 BC8 6 GLN A 214 ? GLN A 214 . ? 1_555 ? 71 BC8 6 PHE A 217 ? PHE A 217 . ? 1_555 ? 72 BC8 6 TYR A 254 ? TYR A 254 . ? 1_555 ? 73 BC8 6 SER A 263 ? SER A 263 . ? 1_555 ? 74 BC8 6 LEU A 264 ? LEU A 264 . ? 1_555 ? 75 BC8 6 ASN A 266 ? ASN A 266 . ? 1_555 ? 76 BC9 6 TYR A 450 ? TYR A 450 . ? 1_555 ? 77 BC9 6 PRO A 451 ? PRO A 451 . ? 1_555 ? 78 BC9 6 ASN A 458 ? ASN A 458 . ? 1_555 ? 79 BC9 6 THR A 460 ? THR A 460 . ? 1_555 ? 80 BC9 6 CYS A 472 ? CYS A 472 . ? 1_555 ? 81 BC9 6 ASN A 474 ? ASN A 474 . ? 1_555 ? 82 CC1 3 LYS A 501 ? LYS A 501 . ? 1_555 ? 83 CC1 3 ASN A 585 ? ASN A 585 . ? 1_555 ? 84 CC1 3 ASP B 512 ? ASP B 512 . ? 1_555 ? 85 CC2 1 ASN A 805 ? ASN A 805 . ? 1_555 ? 86 CC3 2 ASN A 821 ? ASN A 821 . ? 1_555 ? 87 CC3 2 GLY A 887 ? GLY A 887 . ? 1_555 ? 88 CC4 2 THR A 942 ? THR A 942 . ? 1_555 ? 89 CC4 2 ASN A 943 ? ASN A 943 . ? 1_555 ? 90 CC5 3 ASP A 751 ? ASP A 751 . ? 1_555 ? 91 CC5 3 HIS A 752 ? HIS A 752 . ? 1_555 ? 92 CC5 3 ASN A 950 ? ASN A 950 . ? 1_555 ? 93 CC6 2 ASN B 99 ? ASN B 99 . ? 1_555 ? 94 CC6 2 NAG DA . ? NAG B 703 . ? 1_555 ? 95 CC7 5 ARG A 248 ? ARG A 248 . ? 1_555 ? 96 CC7 5 MET A 272 ? MET A 272 . ? 1_555 ? 97 CC7 5 ASN B 316 ? ASN B 316 . ? 1_555 ? 98 CC7 5 LEU B 317 ? LEU B 317 . ? 1_555 ? 99 CC7 5 ASN B 320 ? ASN B 320 . ? 1_555 ? 100 CC8 4 ASN B 371 ? ASN B 371 . ? 1_555 ? 101 CC8 4 SER B 398 ? SER B 398 . ? 1_555 ? 102 CC8 4 GLU B 400 ? GLU B 400 . ? 1_555 ? 103 CC8 4 NAG BA . ? NAG B 701 . ? 1_555 ? 104 CC9 4 ASP A 621 ? ASP A 621 . ? 1_555 ? 105 CC9 4 TYR B 531 ? TYR B 531 . ? 1_555 ? 106 CC9 4 TYR B 557 ? TYR B 557 . ? 1_555 ? 107 CC9 4 ASN B 559 ? ASN B 559 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MMZ _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 4MMZ _atom_sites.fract_transf_matrix[1][1] 0.007705 _atom_sites.fract_transf_matrix[1][2] 0.004448 _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] 0.008897 _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] 0.003250 _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 CL MN N NA 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 ? -17.557 49.220 8.320 1.00 90.05 ? 1 PHE A N 1 ATOM 2 C CA . PHE A 1 1 ? -18.062 48.405 7.222 1.00 93.02 ? 1 PHE A CA 1 ATOM 3 C C . PHE A 1 1 ? -17.755 49.041 5.870 1.00 106.44 ? 1 PHE A C 1 ATOM 4 O O . PHE A 1 1 ? -17.924 48.413 4.824 1.00 101.89 ? 1 PHE A O 1 ATOM 5 C CB . PHE A 1 1 ? -19.569 48.188 7.364 1.00 95.82 ? 1 PHE A CB 1 ATOM 6 C CG . PHE A 1 1 ? -20.381 49.444 7.214 1.00 98.35 ? 1 PHE A CG 1 ATOM 7 C CD1 . PHE A 1 1 ? -20.574 50.294 8.291 1.00 105.91 ? 1 PHE A CD1 1 ATOM 8 C CD2 . PHE A 1 1 ? -20.960 49.770 5.997 1.00 102.40 ? 1 PHE A CD2 1 ATOM 9 C CE1 . PHE A 1 1 ? -21.323 51.447 8.157 1.00 108.47 ? 1 PHE A CE1 1 ATOM 10 C CE2 . PHE A 1 1 ? -21.711 50.921 5.856 1.00 105.06 ? 1 PHE A CE2 1 ATOM 11 C CZ . PHE A 1 1 ? -21.893 51.761 6.937 1.00 105.42 ? 1 PHE A CZ 1 ATOM 12 N N . ASN A 1 2 ? -17.313 50.294 5.898 1.00 110.96 ? 2 ASN A N 1 ATOM 13 C CA . ASN A 1 2 ? -17.093 51.056 4.674 1.00 106.21 ? 2 ASN A CA 1 ATOM 14 C C . ASN A 1 2 ? -15.652 51.035 4.168 1.00 97.80 ? 2 ASN A C 1 ATOM 15 O O . ASN A 1 2 ? -15.329 51.713 3.195 1.00 98.40 ? 2 ASN A O 1 ATOM 16 C CB . ASN A 1 2 ? -17.544 52.505 4.874 1.00 99.05 ? 2 ASN A CB 1 ATOM 17 C CG . ASN A 1 2 ? -17.192 53.043 6.245 1.00 98.79 ? 2 ASN A CG 1 ATOM 18 O OD1 . ASN A 1 2 ? -17.235 52.317 7.240 1.00 99.34 ? 2 ASN A OD1 1 ATOM 19 N ND2 . ASN A 1 2 ? -16.846 54.322 6.307 1.00 100.59 ? 2 ASN A ND2 1 ATOM 20 N N . LEU A 1 3 ? -14.784 50.274 4.826 1.00 92.72 ? 3 LEU A N 1 ATOM 21 C CA . LEU A 1 3 ? -13.393 50.185 4.390 1.00 92.62 ? 3 LEU A CA 1 ATOM 22 C C . LEU A 1 3 ? -13.263 49.355 3.117 1.00 95.98 ? 3 LEU A C 1 ATOM 23 O O . LEU A 1 3 ? -13.872 48.294 2.996 1.00 99.40 ? 3 LEU A O 1 ATOM 24 C CB . LEU A 1 3 ? -12.518 49.594 5.495 1.00 87.13 ? 3 LEU A CB 1 ATOM 25 C CG . LEU A 1 3 ? -12.215 50.528 6.668 1.00 86.29 ? 3 LEU A CG 1 ATOM 26 C CD1 . LEU A 1 3 ? -11.344 49.829 7.693 1.00 93.04 ? 3 LEU A CD1 1 ATOM 27 C CD2 . LEU A 1 3 ? -11.548 51.804 6.180 1.00 84.89 ? 3 LEU A CD2 1 ATOM 28 N N . ASP A 1 4 ? -12.457 49.837 2.177 1.00 95.46 ? 4 ASP A N 1 ATOM 29 C CA . ASP A 1 4 ? -12.301 49.174 0.887 1.00 98.69 ? 4 ASP A CA 1 ATOM 30 C C . ASP A 1 4 ? -11.139 48.191 0.900 1.00 114.57 ? 4 ASP A C 1 ATOM 31 O O . ASP A 1 4 ? -9.976 48.592 0.961 1.00 116.93 ? 4 ASP A O 1 ATOM 32 C CB . ASP A 1 4 ? -12.088 50.207 -0.220 1.00 101.90 ? 4 ASP A CB 1 ATOM 33 C CG . ASP A 1 4 ? -11.656 49.578 -1.531 1.00 122.95 ? 4 ASP A CG 1 ATOM 34 O OD1 . ASP A 1 4 ? -12.227 48.532 -1.909 1.00 141.94 ? 4 ASP A OD1 1 ATOM 35 O OD2 . ASP A 1 4 ? -10.742 50.127 -2.182 1.00 123.15 ? 4 ASP A OD2 1 ATOM 36 N N . VAL A 1 5 ? -11.464 46.903 0.831 1.00 107.15 ? 5 VAL A N 1 ATOM 37 C CA . VAL A 1 5 ? -10.449 45.858 0.840 1.00 106.75 ? 5 VAL A CA 1 ATOM 38 C C . VAL A 1 5 ? -10.118 45.388 -0.576 1.00 100.09 ? 5 VAL A C 1 ATOM 39 O O . VAL A 1 5 ? -9.217 44.573 -0.775 1.00 99.85 ? 5 VAL A O 1 ATOM 40 C CB . VAL A 1 5 ? -10.900 44.655 1.688 1.00 119.08 ? 5 VAL A CB 1 ATOM 41 C CG1 . VAL A 1 5 ? -9.693 43.894 2.220 1.00 130.57 ? 5 VAL A CG1 1 ATOM 42 C CG2 . VAL A 1 5 ? -11.767 45.128 2.842 1.00 120.63 ? 5 VAL A CG2 1 ATOM 43 N N . ASP A 1 6 ? -10.839 45.915 -1.561 1.00 104.03 ? 6 ASP A N 1 ATOM 44 C CA . ASP A 1 6 ? -10.628 45.516 -2.949 1.00 120.25 ? 6 ASP A CA 1 ATOM 45 C C . ASP A 1 6 ? -9.315 46.050 -3.504 1.00 127.43 ? 6 ASP A C 1 ATOM 46 O O . ASP A 1 6 ? -8.494 45.291 -4.018 1.00 135.98 ? 6 ASP A O 1 ATOM 47 C CB . ASP A 1 6 ? -11.788 45.988 -3.826 1.00 123.55 ? 6 ASP A CB 1 ATOM 48 C CG . ASP A 1 6 ? -13.009 45.104 -3.697 1.00 133.64 ? 6 ASP A CG 1 ATOM 49 O OD1 . ASP A 1 6 ? -13.128 44.398 -2.673 1.00 140.29 ? 6 ASP A OD1 1 ATOM 50 O OD2 . ASP A 1 6 ? -13.849 45.114 -4.620 1.00 135.00 ? 6 ASP A OD2 1 ATOM 51 N N . SER A 1 7 ? -9.119 47.358 -3.395 1.00 133.00 ? 7 SER A N 1 ATOM 52 C CA . SER A 1 7 ? -7.922 47.991 -3.932 1.00 133.98 ? 7 SER A CA 1 ATOM 53 C C . SER A 1 7 ? -7.247 48.892 -2.904 1.00 117.01 ? 7 SER A C 1 ATOM 54 O O . SER A 1 7 ? -7.307 50.117 -3.012 1.00 128.14 ? 7 SER A O 1 ATOM 55 C CB . SER A 1 7 ? -8.266 48.795 -5.187 1.00 146.63 ? 7 SER A CB 1 ATOM 56 O OG . SER A 1 7 ? -9.279 49.749 -4.917 1.00 154.36 ? 7 SER A OG 1 ATOM 57 N N . PRO A 1 8 ? -6.597 48.286 -1.900 1.00 99.99 ? 8 PRO A N 1 ATOM 58 C CA . PRO A 1 8 ? -5.876 49.062 -0.891 1.00 96.05 ? 8 PRO A CA 1 ATOM 59 C C . PRO A 1 8 ? -4.527 49.533 -1.420 1.00 96.54 ? 8 PRO A C 1 ATOM 60 O O . PRO A 1 8 ? -4.208 49.284 -2.581 1.00 114.55 ? 8 PRO A O 1 ATOM 61 C CB . PRO A 1 8 ? -5.703 48.063 0.250 1.00 92.37 ? 8 PRO A CB 1 ATOM 62 C CG . PRO A 1 8 ? -5.582 46.758 -0.445 1.00 94.53 ? 8 PRO A CG 1 ATOM 63 C CD . PRO A 1 8 ? -6.483 46.838 -1.657 1.00 99.21 ? 8 PRO A CD 1 ATOM 64 N N . ALA A 1 9 ? -3.747 50.202 -0.578 1.00 95.68 ? 9 ALA A N 1 ATOM 65 C CA . ALA A 1 9 ? -2.426 50.667 -0.980 1.00 100.21 ? 9 ALA A CA 1 ATOM 66 C C . ALA A 1 9 ? -1.333 49.822 -0.338 1.00 105.11 ? 9 ALA A C 1 ATOM 67 O O . ALA A 1 9 ? -1.156 49.838 0.879 1.00 106.01 ? 9 ALA A O 1 ATOM 68 C CB . ALA A 1 9 ? -2.248 52.127 -0.618 1.00 97.57 ? 9 ALA A CB 1 ATOM 69 N N . GLU A 1 10 ? -0.603 49.082 -1.167 1.00 115.88 ? 10 GLU A N 1 ATOM 70 C CA . GLU A 1 10 ? 0.465 48.215 -0.685 1.00 119.61 ? 10 GLU A CA 1 ATOM 71 C C . GLU A 1 10 ? 1.797 48.953 -0.611 1.00 97.60 ? 10 GLU A C 1 ATOM 72 O O . GLU A 1 10 ? 2.269 49.503 -1.601 1.00 102.63 ? 10 GLU A O 1 ATOM 73 C CB . GLU A 1 10 ? 0.593 46.979 -1.584 1.00 142.71 ? 10 GLU A CB 1 ATOM 74 C CG . GLU A 1 10 ? 1.837 46.132 -1.331 1.00 156.81 ? 10 GLU A CG 1 ATOM 75 C CD . GLU A 1 10 ? 2.999 46.500 -2.241 1.00 164.69 ? 10 GLU A CD 1 ATOM 76 O OE1 . GLU A 1 10 ? 2.756 47.113 -3.302 1.00 160.44 ? 10 GLU A OE1 1 ATOM 77 O OE2 . GLU A 1 10 ? 4.156 46.180 -1.893 1.00 162.45 ? 10 GLU A OE2 1 ATOM 78 N N . TYR A 1 11 ? 2.399 48.957 0.571 1.00 86.45 ? 11 TYR A N 1 ATOM 79 C CA . TYR A 1 11 ? 3.720 49.542 0.755 1.00 88.03 ? 11 TYR A CA 1 ATOM 80 C C . TYR A 1 11 ? 4.674 48.496 1.308 1.00 88.54 ? 11 TYR A C 1 ATOM 81 O O . TYR A 1 11 ? 4.353 47.815 2.279 1.00 81.34 ? 11 TYR A O 1 ATOM 82 C CB . TYR A 1 11 ? 3.654 50.749 1.692 1.00 90.62 ? 11 TYR A CB 1 ATOM 83 C CG . TYR A 1 11 ? 2.973 51.957 1.092 1.00 89.69 ? 11 TYR A CG 1 ATOM 84 C CD1 . TYR A 1 11 ? 3.706 52.925 0.420 1.00 112.54 ? 11 TYR A CD1 1 ATOM 85 C CD2 . TYR A 1 11 ? 1.600 52.132 1.198 1.00 86.16 ? 11 TYR A CD2 1 ATOM 86 C CE1 . TYR A 1 11 ? 3.093 54.033 -0.131 1.00 113.95 ? 11 TYR A CE1 1 ATOM 87 C CE2 . TYR A 1 11 ? 0.977 53.237 0.649 1.00 94.48 ? 11 TYR A CE2 1 ATOM 88 C CZ . TYR A 1 11 ? 1.730 54.187 -0.012 1.00 109.54 ? 11 TYR A CZ 1 ATOM 89 O OH . TYR A 1 11 ? 1.120 55.292 -0.561 1.00 114.47 ? 11 TYR A OH 1 ATOM 90 N N . SER A 1 12 ? 5.841 48.367 0.687 1.00 91.20 ? 12 SER A N 1 ATOM 91 C CA . SER A 1 12 ? 6.816 47.369 1.111 1.00 95.68 ? 12 SER A CA 1 ATOM 92 C C . SER A 1 12 ? 8.223 47.944 1.227 1.00 95.40 ? 12 SER A C 1 ATOM 93 O O . SER A 1 12 ? 8.799 48.404 0.240 1.00 117.67 ? 12 SER A O 1 ATOM 94 C CB . SER A 1 12 ? 6.823 46.187 0.141 1.00 107.62 ? 12 SER A CB 1 ATOM 95 O OG . SER A 1 12 ? 7.265 46.587 -1.145 1.00 125.22 ? 12 SER A OG 1 ATOM 96 N N . GLY A 1 13 ? 8.769 47.907 2.437 1.00 82.96 ? 13 GLY A N 1 ATOM 97 C CA . GLY A 1 13 ? 10.154 48.272 2.663 1.00 83.95 ? 13 GLY A CA 1 ATOM 98 C C . GLY A 1 13 ? 11.059 47.074 2.446 1.00 106.13 ? 13 GLY A C 1 ATOM 99 O O . GLY A 1 13 ? 10.598 46.022 1.999 1.00 113.80 ? 13 GLY A O 1 ATOM 100 N N . PRO A 1 14 ? 12.354 47.222 2.765 1.00 107.93 ? 14 PRO A N 1 ATOM 101 C CA . PRO A 1 14 ? 13.337 46.141 2.612 1.00 108.23 ? 14 PRO A CA 1 ATOM 102 C C . PRO A 1 14 ? 13.057 44.992 3.572 1.00 91.89 ? 14 PRO A C 1 ATOM 103 O O . PRO A 1 14 ? 12.519 45.230 4.651 1.00 96.00 ? 14 PRO A O 1 ATOM 104 C CB . PRO A 1 14 ? 14.664 46.825 2.944 1.00 91.70 ? 14 PRO A CB 1 ATOM 105 C CG . PRO A 1 14 ? 14.287 47.950 3.838 1.00 85.46 ? 14 PRO A CG 1 ATOM 106 C CD . PRO A 1 14 ? 12.951 48.431 3.355 1.00 84.98 ? 14 PRO A CD 1 ATOM 107 N N . GLU A 1 15 ? 13.407 43.769 3.188 1.00 94.52 ? 15 GLU A N 1 ATOM 108 C CA . GLU A 1 15 ? 13.101 42.613 4.025 1.00 106.87 ? 15 GLU A CA 1 ATOM 109 C C . GLU A 1 15 ? 14.021 42.553 5.241 1.00 95.37 ? 15 GLU A C 1 ATOM 110 O O . GLU A 1 15 ? 15.184 42.955 5.177 1.00 89.42 ? 15 GLU A O 1 ATOM 111 C CB . GLU A 1 15 ? 13.197 41.314 3.220 1.00 99.76 ? 15 GLU A CB 1 ATOM 112 C CG . GLU A 1 15 ? 14.583 40.993 2.691 1.00 118.16 ? 15 GLU A CG 1 ATOM 113 C CD . GLU A 1 15 ? 14.651 39.621 2.046 1.00 139.24 ? 15 GLU A CD 1 ATOM 114 O OE1 . GLU A 1 15 ? 13.646 38.883 2.113 1.00 127.51 ? 15 GLU A OE1 1 ATOM 115 O OE2 . GLU A 1 15 ? 15.709 39.280 1.474 1.00 149.60 ? 15 GLU A OE2 1 ATOM 116 N N . GLY A 1 16 ? 13.482 42.055 6.350 1.00 86.24 ? 16 GLY A N 1 ATOM 117 C CA . GLY A 1 16 ? 14.231 41.939 7.588 1.00 77.40 ? 16 GLY A CA 1 ATOM 118 C C . GLY A 1 16 ? 14.275 43.245 8.353 1.00 75.66 ? 16 GLY A C 1 ATOM 119 O O . GLY A 1 16 ? 14.802 43.309 9.462 1.00 75.65 ? 16 GLY A O 1 ATOM 120 N N . SER A 1 17 ? 13.702 44.284 7.758 1.00 79.77 ? 17 SER A N 1 ATOM 121 C CA . SER A 1 17 ? 13.767 45.634 8.304 1.00 76.65 ? 17 SER A CA 1 ATOM 122 C C . SER A 1 17 ? 12.575 45.982 9.183 1.00 72.73 ? 17 SER A C 1 ATOM 123 O O . SER A 1 17 ? 12.413 47.137 9.562 1.00 95.23 ? 17 SER A O 1 ATOM 124 C CB . SER A 1 17 ? 13.867 46.655 7.173 1.00 86.01 ? 17 SER A CB 1 ATOM 125 O OG . SER A 1 17 ? 12.690 46.645 6.386 1.00 86.61 ? 17 SER A OG 1 ATOM 126 N N . TYR A 1 18 ? 11.714 45.005 9.448 1.00 82.04 ? 18 TYR A N 1 ATOM 127 C CA . TYR A 1 18 ? 10.517 45.222 10.264 1.00 85.61 ? 18 TYR A CA 1 ATOM 128 C C . TYR A 1 18 ? 9.731 46.453 9.814 1.00 75.32 ? 18 TYR A C 1 ATOM 129 O O . TYR A 1 18 ? 9.141 47.162 10.631 1.00 62.77 ? 18 TYR A O 1 ATOM 130 C CB . TYR A 1 18 ? 10.883 45.358 11.743 1.00 68.36 ? 18 TYR A CB 1 ATOM 131 C CG . TYR A 1 18 ? 11.205 44.051 12.434 1.00 65.57 ? 18 TYR A CG 1 ATOM 132 C CD1 . TYR A 1 18 ? 11.156 42.846 11.749 1.00 64.37 ? 18 TYR A CD1 1 ATOM 133 C CD2 . TYR A 1 18 ? 11.547 44.024 13.778 1.00 70.01 ? 18 TYR A CD2 1 ATOM 134 C CE1 . TYR A 1 18 ? 11.447 41.654 12.384 1.00 67.30 ? 18 TYR A CE1 1 ATOM 135 C CE2 . TYR A 1 18 ? 11.838 42.838 14.419 1.00 60.70 ? 18 TYR A CE2 1 ATOM 136 C CZ . TYR A 1 18 ? 11.787 41.658 13.719 1.00 67.10 ? 18 TYR A CZ 1 ATOM 137 O OH . TYR A 1 18 ? 12.079 40.477 14.361 1.00 88.18 ? 18 TYR A OH 1 ATOM 138 N N . PHE A 1 19 ? 9.748 46.706 8.509 1.00 76.60 ? 19 PHE A N 1 ATOM 139 C CA . PHE A 1 19 ? 9.007 47.808 7.921 1.00 68.73 ? 19 PHE A CA 1 ATOM 140 C C . PHE A 1 19 ? 7.529 47.631 8.232 1.00 71.51 ? 19 PHE A C 1 ATOM 141 O O . PHE A 1 19 ? 6.934 46.612 7.889 1.00 97.76 ? 19 PHE A O 1 ATOM 142 C CB . PHE A 1 19 ? 9.262 47.851 6.412 1.00 72.83 ? 19 PHE A CB 1 ATOM 143 C CG . PHE A 1 19 ? 8.420 48.847 5.665 1.00 75.71 ? 19 PHE A CG 1 ATOM 144 C CD1 . PHE A 1 19 ? 7.189 48.485 5.142 1.00 84.38 ? 19 PHE A CD1 1 ATOM 145 C CD2 . PHE A 1 19 ? 8.879 50.133 5.449 1.00 78.66 ? 19 PHE A CD2 1 ATOM 146 C CE1 . PHE A 1 19 ? 6.422 49.393 4.441 1.00 92.41 ? 19 PHE A CE1 1 ATOM 147 C CE2 . PHE A 1 19 ? 8.118 51.045 4.746 1.00 88.13 ? 19 PHE A CE2 1 ATOM 148 C CZ . PHE A 1 19 ? 6.887 50.675 4.243 1.00 93.79 ? 19 PHE A CZ 1 ATOM 149 N N . GLY A 1 20 ? 6.936 48.633 8.865 1.00 71.31 ? 20 GLY A N 1 ATOM 150 C CA . GLY A 1 20 ? 5.550 48.545 9.280 1.00 64.46 ? 20 GLY A CA 1 ATOM 151 C C . GLY A 1 20 ? 5.363 48.359 10.774 1.00 61.75 ? 20 GLY A C 1 ATOM 152 O O . GLY A 1 20 ? 4.232 48.335 11.257 1.00 63.61 ? 20 GLY A O 1 ATOM 153 N N . PHE A 1 21 ? 6.465 48.245 11.511 1.00 60.49 ? 21 PHE A N 1 ATOM 154 C CA . PHE A 1 21 ? 6.393 48.021 12.955 1.00 58.27 ? 21 PHE A CA 1 ATOM 155 C C . PHE A 1 21 ? 5.666 49.149 13.687 1.00 58.34 ? 21 PHE A C 1 ATOM 156 O O . PHE A 1 21 ? 5.099 48.936 14.759 1.00 55.69 ? 21 PHE A O 1 ATOM 157 C CB . PHE A 1 21 ? 7.793 47.847 13.543 1.00 58.94 ? 21 PHE A CB 1 ATOM 158 C CG . PHE A 1 21 ? 7.790 47.472 14.996 1.00 68.86 ? 21 PHE A CG 1 ATOM 159 C CD1 . PHE A 1 21 ? 7.597 46.154 15.383 1.00 57.58 ? 21 PHE A CD1 1 ATOM 160 C CD2 . PHE A 1 21 ? 7.970 48.435 15.976 1.00 56.11 ? 21 PHE A CD2 1 ATOM 161 C CE1 . PHE A 1 21 ? 7.587 45.804 16.719 1.00 54.42 ? 21 PHE A CE1 1 ATOM 162 C CE2 . PHE A 1 21 ? 7.962 48.089 17.312 1.00 53.06 ? 21 PHE A CE2 1 ATOM 163 C CZ . PHE A 1 21 ? 7.770 46.770 17.683 1.00 53.10 ? 21 PHE A CZ 1 ATOM 164 N N . ALA A 1 22 ? 5.698 50.346 13.110 1.00 74.47 ? 22 ALA A N 1 ATOM 165 C CA . ALA A 1 22 ? 4.962 51.484 13.648 1.00 57.20 ? 22 ALA A CA 1 ATOM 166 C C . ALA A 1 22 ? 4.484 52.375 12.507 1.00 73.99 ? 22 ALA A C 1 ATOM 167 O O . ALA A 1 22 ? 5.195 52.549 11.517 1.00 84.34 ? 22 ALA A O 1 ATOM 168 C CB . ALA A 1 22 ? 5.823 52.266 14.616 1.00 55.94 ? 22 ALA A CB 1 ATOM 169 N N . VAL A 1 23 ? 3.280 52.928 12.636 1.00 59.42 ? 23 VAL A N 1 ATOM 170 C CA . VAL A 1 23 ? 2.702 53.746 11.569 1.00 61.58 ? 23 VAL A CA 1 ATOM 171 C C . VAL A 1 23 ? 1.982 54.987 12.104 1.00 79.50 ? 23 VAL A C 1 ATOM 172 O O . VAL A 1 23 ? 1.422 54.967 13.201 1.00 80.03 ? 23 VAL A O 1 ATOM 173 C CB . VAL A 1 23 ? 1.707 52.926 10.704 1.00 77.60 ? 23 VAL A CB 1 ATOM 174 C CG1 . VAL A 1 23 ? 2.443 51.878 9.874 1.00 64.75 ? 23 VAL A CG1 1 ATOM 175 C CG2 . VAL A 1 23 ? 0.640 52.272 11.572 1.00 62.03 ? 23 VAL A CG2 1 ATOM 176 N N . ASP A 1 24 ? 2.022 56.070 11.329 1.00 84.74 ? 24 ASP A N 1 ATOM 177 C CA . ASP A 1 24 ? 1.254 57.277 11.631 1.00 70.21 ? 24 ASP A CA 1 ATOM 178 C C . ASP A 1 24 ? 1.061 58.121 10.372 1.00 73.79 ? 24 ASP A C 1 ATOM 179 O O . ASP A 1 24 ? 1.787 57.963 9.391 1.00 93.77 ? 24 ASP A O 1 ATOM 180 C CB . ASP A 1 24 ? 1.939 58.108 12.724 1.00 77.75 ? 24 ASP A CB 1 ATOM 181 C CG . ASP A 1 24 ? 1.009 59.150 13.346 1.00 105.82 ? 24 ASP A CG 1 ATOM 182 O OD1 . ASP A 1 24 ? 0.097 59.649 12.653 1.00 102.34 ? 24 ASP A OD1 1 ATOM 183 O OD2 . ASP A 1 24 ? 1.190 59.474 14.538 1.00 119.11 ? 24 ASP A OD2 1 ATOM 184 N N . PHE A 1 25 ? 0.068 59.005 10.407 1.00 78.88 ? 25 PHE A N 1 ATOM 185 C CA . PHE A 1 25 ? -0.160 59.968 9.335 1.00 74.04 ? 25 PHE A CA 1 ATOM 186 C C . PHE A 1 25 ? 0.702 61.215 9.503 1.00 84.68 ? 25 PHE A C 1 ATOM 187 O O . PHE A 1 25 ? 0.982 61.641 10.624 1.00 87.79 ? 25 PHE A O 1 ATOM 188 C CB . PHE A 1 25 ? -1.630 60.375 9.280 1.00 73.50 ? 25 PHE A CB 1 ATOM 189 C CG . PHE A 1 25 ? -2.523 59.342 8.673 1.00 74.32 ? 25 PHE A CG 1 ATOM 190 C CD1 . PHE A 1 25 ? -2.764 59.333 7.312 1.00 80.81 ? 25 PHE A CD1 1 ATOM 191 C CD2 . PHE A 1 25 ? -3.138 58.387 9.465 1.00 93.01 ? 25 PHE A CD2 1 ATOM 192 C CE1 . PHE A 1 25 ? -3.594 58.387 6.749 1.00 84.68 ? 25 PHE A CE1 1 ATOM 193 C CE2 . PHE A 1 25 ? -3.972 57.439 8.908 1.00 81.21 ? 25 PHE A CE2 1 ATOM 194 C CZ . PHE A 1 25 ? -4.198 57.438 7.548 1.00 76.36 ? 25 PHE A CZ 1 ATOM 195 N N . PHE A 1 26 ? 1.115 61.799 8.383 1.00 74.78 ? 26 PHE A N 1 ATOM 196 C CA . PHE A 1 26 ? 1.844 63.060 8.408 1.00 91.80 ? 26 PHE A CA 1 ATOM 197 C C . PHE A 1 26 ? 1.078 64.127 7.630 1.00 92.80 ? 26 PHE A C 1 ATOM 198 O O . PHE A 1 26 ? 0.925 64.032 6.413 1.00 82.05 ? 26 PHE A O 1 ATOM 199 C CB . PHE A 1 26 ? 3.251 62.879 7.839 1.00 75.97 ? 26 PHE A CB 1 ATOM 200 C CG . PHE A 1 26 ? 4.068 64.136 7.833 1.00 77.29 ? 26 PHE A CG 1 ATOM 201 C CD1 . PHE A 1 26 ? 4.306 64.830 9.007 1.00 82.80 ? 26 PHE A CD1 1 ATOM 202 C CD2 . PHE A 1 26 ? 4.610 64.619 6.653 1.00 105.75 ? 26 PHE A CD2 1 ATOM 203 C CE1 . PHE A 1 26 ? 5.062 65.991 9.003 1.00 96.66 ? 26 PHE A CE1 1 ATOM 204 C CE2 . PHE A 1 26 ? 5.369 65.776 6.642 1.00 81.69 ? 26 PHE A CE2 1 ATOM 205 C CZ . PHE A 1 26 ? 5.593 66.463 7.818 1.00 81.35 ? 26 PHE A CZ 1 ATOM 206 N N . VAL A 1 27 ? 0.593 65.139 8.344 1.00 103.51 ? 27 VAL A N 1 ATOM 207 C CA . VAL A 1 27 ? -0.202 66.200 7.734 1.00 102.48 ? 27 VAL A CA 1 ATOM 208 C C . VAL A 1 27 ? 0.399 67.580 7.979 1.00 102.53 ? 27 VAL A C 1 ATOM 209 O O . VAL A 1 27 ? -0.115 68.355 8.788 1.00 109.69 ? 27 VAL A O 1 ATOM 210 C CB . VAL A 1 27 ? -1.648 66.186 8.259 1.00 96.73 ? 27 VAL A CB 1 ATOM 211 C CG1 . VAL A 1 27 ? -2.495 65.225 7.448 1.00 84.73 ? 27 VAL A CG1 1 ATOM 212 C CG2 . VAL A 1 27 ? -1.673 65.818 9.738 1.00 105.84 ? 27 VAL A CG2 1 ATOM 213 N N . PRO A 1 28 ? 1.488 67.898 7.266 1.00 86.17 ? 28 PRO A N 1 ATOM 214 C CA . PRO A 1 28 ? 2.162 69.187 7.437 1.00 87.76 ? 28 PRO A CA 1 ATOM 215 C C . PRO A 1 28 ? 1.269 70.357 7.039 1.00 97.59 ? 28 PRO A C 1 ATOM 216 O O . PRO A 1 28 ? 0.475 70.236 6.106 1.00 109.48 ? 28 PRO A O 1 ATOM 217 C CB . PRO A 1 28 ? 3.367 69.076 6.501 1.00 96.79 ? 28 PRO A CB 1 ATOM 218 C CG . PRO A 1 28 ? 2.932 68.114 5.454 1.00 98.66 ? 28 PRO A CG 1 ATOM 219 C CD . PRO A 1 28 ? 2.073 67.112 6.167 1.00 86.72 ? 28 PRO A CD 1 ATOM 220 N N . SER A 1 29 ? 1.397 71.473 7.747 1.00 115.58 ? 29 SER A N 1 ATOM 221 C CA . SER A 1 29 ? 0.659 72.679 7.401 1.00 113.85 ? 29 SER A CA 1 ATOM 222 C C . SER A 1 29 ? 1.330 73.365 6.220 1.00 110.36 ? 29 SER A C 1 ATOM 223 O O . SER A 1 29 ? 0.759 74.258 5.593 1.00 104.23 ? 29 SER A O 1 ATOM 224 C CB . SER A 1 29 ? 0.571 73.629 8.597 1.00 116.95 ? 29 SER A CB 1 ATOM 225 O OG . SER A 1 29 ? -0.190 73.055 9.646 1.00 145.14 ? 29 SER A OG 1 ATOM 226 N N . ALA A 1 30 ? 2.548 72.925 5.921 1.00 103.47 ? 30 ALA A N 1 ATOM 227 C CA . ALA A 1 30 ? 3.334 73.482 4.829 1.00 104.36 ? 30 ALA A CA 1 ATOM 228 C C . ALA A 1 30 ? 2.695 73.240 3.462 1.00 105.28 ? 30 ALA A C 1 ATOM 229 O O . ALA A 1 30 ? 2.821 74.065 2.560 1.00 123.62 ? 30 ALA A O 1 ATOM 230 C CB . ALA A 1 30 ? 4.741 72.907 4.859 1.00 108.97 ? 30 ALA A CB 1 ATOM 231 N N . SER A 1 31 ? 2.011 72.110 3.305 1.00 145.71 ? 31 SER A N 1 ATOM 232 C CA . SER A 1 31 ? 1.408 71.780 2.018 1.00 130.36 ? 31 SER A CA 1 ATOM 233 C C . SER A 1 31 ? 0.070 71.060 2.154 1.00 118.95 ? 31 SER A C 1 ATOM 234 O O . SER A 1 31 ? -0.376 70.747 3.260 1.00 102.81 ? 31 SER A O 1 ATOM 235 C CB . SER A 1 31 ? 2.363 70.915 1.194 1.00 123.66 ? 31 SER A CB 1 ATOM 236 O OG . SER A 1 31 ? 2.346 69.571 1.640 1.00 102.50 ? 31 SER A OG 1 ATOM 237 N N . SER A 1 32 ? -0.560 70.798 1.012 1.00 116.56 ? 32 SER A N 1 ATOM 238 C CA . SER A 1 32 ? -1.845 70.114 0.975 1.00 115.67 ? 32 SER A CA 1 ATOM 239 C C . SER A 1 32 ? -1.669 68.606 0.878 1.00 114.67 ? 32 SER A C 1 ATOM 240 O O . SER A 1 32 ? -2.618 67.849 1.072 1.00 122.86 ? 32 SER A O 1 ATOM 241 C CB . SER A 1 32 ? -2.684 70.616 -0.201 1.00 114.58 ? 32 SER A CB 1 ATOM 242 O OG . SER A 1 32 ? -3.056 71.969 -0.021 1.00 117.51 ? 32 SER A OG 1 ATOM 243 N N . ARG A 1 33 ? -0.446 68.175 0.586 1.00 114.71 ? 33 ARG A N 1 ATOM 244 C CA . ARG A 1 33 ? -0.156 66.754 0.451 1.00 102.62 ? 33 ARG A CA 1 ATOM 245 C C . ARG A 1 33 ? -0.007 66.091 1.811 1.00 102.06 ? 33 ARG A C 1 ATOM 246 O O . ARG A 1 33 ? 0.573 66.665 2.736 1.00 95.46 ? 33 ARG A O 1 ATOM 247 C CB . ARG A 1 33 ? 1.112 66.535 -0.376 1.00 103.73 ? 33 ARG A CB 1 ATOM 248 C CG . ARG A 1 33 ? 0.960 66.862 -1.851 1.00 123.11 ? 33 ARG A CG 1 ATOM 249 C CD . ARG A 1 33 ? 1.548 65.757 -2.717 1.00 136.44 ? 33 ARG A CD 1 ATOM 250 N NE . ARG A 1 33 ? 2.966 65.539 -2.444 1.00 139.22 ? 33 ARG A NE 1 ATOM 251 C CZ . ARG A 1 33 ? 3.955 66.077 -3.151 1.00 149.74 ? 33 ARG A CZ 1 ATOM 252 N NH1 . ARG A 1 33 ? 3.683 66.865 -4.183 1.00 145.29 ? 33 ARG A NH1 1 ATOM 253 N NH2 . ARG A 1 33 ? 5.216 65.823 -2.829 1.00 147.64 ? 33 ARG A NH2 1 ATOM 254 N N . MET A 1 34 ? -0.538 64.879 1.925 1.00 120.22 ? 34 MET A N 1 ATOM 255 C CA . MET A 1 34 ? -0.418 64.100 3.150 1.00 93.65 ? 34 MET A CA 1 ATOM 256 C C . MET A 1 34 ? 0.411 62.854 2.873 1.00 89.40 ? 34 MET A C 1 ATOM 257 O O . MET A 1 34 ? 0.386 62.316 1.768 1.00 104.16 ? 34 MET A O 1 ATOM 258 C CB . MET A 1 34 ? -1.799 63.737 3.693 1.00 90.35 ? 34 MET A CB 1 ATOM 259 C CG . MET A 1 34 ? -2.734 64.933 3.790 1.00 115.06 ? 34 MET A CG 1 ATOM 260 S SD . MET A 1 34 ? -4.344 64.553 4.498 1.00 102.95 ? 34 MET A SD 1 ATOM 261 C CE . MET A 1 34 ? -5.151 66.146 4.366 1.00 98.84 ? 34 MET A CE 1 ATOM 262 N N . PHE A 1 35 ? 1.159 62.407 3.874 1.00 85.70 ? 35 PHE A N 1 ATOM 263 C CA . PHE A 1 35 ? 2.102 61.314 3.683 1.00 84.28 ? 35 PHE A CA 1 ATOM 264 C C . PHE A 1 35 ? 1.912 60.208 4.712 1.00 83.77 ? 35 PHE A C 1 ATOM 265 O O . PHE A 1 35 ? 1.259 60.405 5.736 1.00 86.61 ? 35 PHE A O 1 ATOM 266 C CB . PHE A 1 35 ? 3.540 61.834 3.755 1.00 90.28 ? 35 PHE A CB 1 ATOM 267 C CG . PHE A 1 35 ? 3.917 62.737 2.621 1.00 87.90 ? 35 PHE A CG 1 ATOM 268 C CD1 . PHE A 1 35 ? 3.540 64.070 2.621 1.00 89.84 ? 35 PHE A CD1 1 ATOM 269 C CD2 . PHE A 1 35 ? 4.663 62.256 1.558 1.00 89.98 ? 35 PHE A CD2 1 ATOM 270 C CE1 . PHE A 1 35 ? 3.887 64.903 1.578 1.00 93.75 ? 35 PHE A CE1 1 ATOM 271 C CE2 . PHE A 1 35 ? 5.017 63.087 0.511 1.00 134.58 ? 35 PHE A CE2 1 ATOM 272 C CZ . PHE A 1 35 ? 4.628 64.412 0.521 1.00 95.79 ? 35 PHE A CZ 1 ATOM 273 N N . LEU A 1 36 ? 2.492 59.046 4.433 1.00 79.83 ? 36 LEU A N 1 ATOM 274 C CA . LEU A 1 36 ? 2.511 57.958 5.401 1.00 90.35 ? 36 LEU A CA 1 ATOM 275 C C . LEU A 1 36 ? 3.858 57.898 6.107 1.00 87.37 ? 36 LEU A C 1 ATOM 276 O O . LEU A 1 36 ? 4.907 57.959 5.466 1.00 98.16 ? 36 LEU A O 1 ATOM 277 C CB . LEU A 1 36 ? 2.223 56.612 4.731 1.00 93.43 ? 36 LEU A CB 1 ATOM 278 C CG . LEU A 1 36 ? 0.890 56.434 4.006 1.00 99.71 ? 36 LEU A CG 1 ATOM 279 C CD1 . LEU A 1 36 ? 0.682 54.974 3.650 1.00 87.88 ? 36 LEU A CD1 1 ATOM 280 C CD2 . LEU A 1 36 ? -0.257 56.951 4.850 1.00 112.44 ? 36 LEU A CD2 1 ATOM 281 N N . LEU A 1 37 ? 3.823 57.783 7.428 1.00 81.05 ? 37 LEU A N 1 ATOM 282 C CA . LEU A 1 37 ? 5.034 57.558 8.203 1.00 71.57 ? 37 LEU A CA 1 ATOM 283 C C . LEU A 1 37 ? 5.103 56.097 8.619 1.00 84.17 ? 37 LEU A C 1 ATOM 284 O O . LEU A 1 37 ? 4.211 55.590 9.301 1.00 66.57 ? 37 LEU A O 1 ATOM 285 C CB . LEU A 1 37 ? 5.077 58.467 9.429 1.00 70.11 ? 37 LEU A CB 1 ATOM 286 C CG . LEU A 1 37 ? 5.083 59.962 9.115 1.00 72.83 ? 37 LEU A CG 1 ATOM 287 C CD1 . LEU A 1 37 ? 5.235 60.775 10.387 1.00 76.74 ? 37 LEU A CD1 1 ATOM 288 C CD2 . LEU A 1 37 ? 6.187 60.293 8.123 1.00 71.37 ? 37 LEU A CD2 1 ATOM 289 N N . VAL A 1 38 ? 6.159 55.416 8.188 1.00 87.19 ? 38 VAL A N 1 ATOM 290 C CA . VAL A 1 38 ? 6.336 54.012 8.522 1.00 67.17 ? 38 VAL A CA 1 ATOM 291 C C . VAL A 1 38 ? 7.684 53.776 9.187 1.00 65.01 ? 38 VAL A C 1 ATOM 292 O O . VAL A 1 38 ? 8.733 53.952 8.569 1.00 79.29 ? 38 VAL A O 1 ATOM 293 C CB . VAL A 1 38 ? 6.230 53.117 7.275 1.00 78.94 ? 38 VAL A CB 1 ATOM 294 C CG1 . VAL A 1 38 ? 6.374 51.662 7.668 1.00 84.04 ? 38 VAL A CG1 1 ATOM 295 C CG2 . VAL A 1 38 ? 4.908 53.352 6.559 1.00 73.98 ? 38 VAL A CG2 1 ATOM 296 N N . GLY A 1 39 ? 7.650 53.380 10.453 1.00 67.25 ? 39 GLY A N 1 ATOM 297 C CA . GLY A 1 39 ? 8.865 53.062 11.175 1.00 62.70 ? 39 GLY A CA 1 ATOM 298 C C . GLY A 1 39 ? 9.388 51.707 10.746 1.00 73.52 ? 39 GLY A C 1 ATOM 299 O O . GLY A 1 39 ? 8.614 50.782 10.497 1.00 68.68 ? 39 GLY A O 1 ATOM 300 N N . ALA A 1 40 ? 10.706 51.594 10.640 1.00 72.31 ? 40 ALA A N 1 ATOM 301 C CA . ALA A 1 40 ? 11.330 50.340 10.246 1.00 64.11 ? 40 ALA A CA 1 ATOM 302 C C . ALA A 1 40 ? 12.639 50.111 10.989 1.00 65.62 ? 40 ALA A C 1 ATOM 303 O O . ALA A 1 40 ? 13.708 50.357 10.439 1.00 72.26 ? 40 ALA A O 1 ATOM 304 C CB . ALA A 1 40 ? 11.564 50.316 8.746 1.00 68.10 ? 40 ALA A CB 1 ATOM 305 N N . PRO A 1 41 ? 12.565 49.644 12.246 1.00 77.57 ? 41 PRO A N 1 ATOM 306 C CA . PRO A 1 41 ? 13.793 49.364 13.000 1.00 75.42 ? 41 PRO A CA 1 ATOM 307 C C . PRO A 1 41 ? 14.540 48.192 12.374 1.00 97.38 ? 41 PRO A C 1 ATOM 308 O O . PRO A 1 41 ? 14.038 47.629 11.410 1.00 88.98 ? 41 PRO A O 1 ATOM 309 C CB . PRO A 1 41 ? 13.282 49.009 14.402 1.00 77.24 ? 41 PRO A CB 1 ATOM 310 C CG . PRO A 1 41 ? 11.830 49.414 14.420 1.00 77.79 ? 41 PRO A CG 1 ATOM 311 C CD . PRO A 1 41 ? 11.359 49.294 13.011 1.00 63.72 ? 41 PRO A CD 1 ATOM 312 N N . LYS A 1 42 ? 15.703 47.824 12.900 1.00 108.03 ? 42 LYS A N 1 ATOM 313 C CA . LYS A 1 42 ? 16.481 46.727 12.319 1.00 108.76 ? 42 LYS A CA 1 ATOM 314 C C . LYS A 1 42 ? 16.810 46.974 10.844 1.00 89.49 ? 42 LYS A C 1 ATOM 315 O O . LYS A 1 42 ? 17.012 46.029 10.084 1.00 108.53 ? 42 LYS A O 1 ATOM 316 C CB . LYS A 1 42 ? 15.733 45.391 12.454 1.00 72.09 ? 42 LYS A CB 1 ATOM 317 C CG . LYS A 1 42 ? 15.952 44.654 13.763 1.00 71.47 ? 42 LYS A CG 1 ATOM 318 C CD . LYS A 1 42 ? 15.353 43.256 13.700 1.00 73.76 ? 42 LYS A CD 1 ATOM 319 C CE . LYS A 1 42 ? 15.928 42.352 14.779 1.00 88.63 ? 42 LYS A CE 1 ATOM 320 N NZ . LYS A 1 42 ? 15.759 42.923 16.144 1.00 115.78 ? 42 LYS A NZ 1 ATOM 321 N N . ALA A 1 43 ? 16.861 48.241 10.443 1.00 84.13 ? 43 ALA A N 1 ATOM 322 C CA . ALA A 1 43 ? 17.115 48.589 9.048 1.00 82.28 ? 43 ALA A CA 1 ATOM 323 C C . ALA A 1 43 ? 18.497 49.196 8.876 1.00 89.30 ? 43 ALA A C 1 ATOM 324 O O . ALA A 1 43 ? 18.870 50.135 9.580 1.00 100.14 ? 43 ALA A O 1 ATOM 325 C CB . ALA A 1 43 ? 16.054 49.545 8.534 1.00 74.09 ? 43 ALA A CB 1 ATOM 326 N N . ASN A 1 44 ? 19.250 48.656 7.926 1.00 87.95 ? 44 ASN A N 1 ATOM 327 C CA . ASN A 1 44 ? 20.604 49.118 7.665 1.00 93.58 ? 44 ASN A CA 1 ATOM 328 C C . ASN A 1 44 ? 20.644 50.518 7.054 1.00 95.10 ? 44 ASN A C 1 ATOM 329 O O . ASN A 1 44 ? 19.964 50.798 6.068 1.00 100.03 ? 44 ASN A O 1 ATOM 330 C CB . ASN A 1 44 ? 21.322 48.115 6.762 1.00 98.24 ? 44 ASN A CB 1 ATOM 331 C CG . ASN A 1 44 ? 21.836 46.918 7.533 1.00 96.95 ? 44 ASN A CG 1 ATOM 332 O OD1 . ASN A 1 44 ? 22.164 47.034 8.712 1.00 94.29 ? 44 ASN A OD1 1 ATOM 333 N ND2 . ASN A 1 44 ? 21.908 45.762 6.883 1.00 112.55 ? 44 ASN A ND2 1 ATOM 334 N N . THR A 1 45 ? 21.443 51.395 7.655 1.00 97.59 ? 45 THR A N 1 ATOM 335 C CA . THR A 1 45 ? 21.531 52.784 7.216 1.00 95.75 ? 45 THR A CA 1 ATOM 336 C C . THR A 1 45 ? 22.925 53.154 6.727 1.00 87.44 ? 45 THR A C 1 ATOM 337 O O . THR A 1 45 ? 23.845 52.336 6.748 1.00 90.83 ? 45 THR A O 1 ATOM 338 C CB . THR A 1 45 ? 21.144 53.759 8.343 1.00 89.99 ? 45 THR A CB 1 ATOM 339 O OG1 . THR A 1 45 ? 22.071 53.630 9.428 1.00 82.85 ? 45 THR A OG1 1 ATOM 340 C CG2 . THR A 1 45 ? 19.742 53.468 8.843 1.00 104.51 ? 45 THR A CG2 1 ATOM 341 N N . THR A 1 46 ? 23.073 54.404 6.304 1.00 88.92 ? 46 THR A N 1 ATOM 342 C CA . THR A 1 46 ? 24.346 54.909 5.809 1.00 99.46 ? 46 THR A CA 1 ATOM 343 C C . THR A 1 46 ? 25.179 55.488 6.948 1.00 99.23 ? 46 THR A C 1 ATOM 344 O O . THR A 1 46 ? 26.247 56.056 6.727 1.00 94.11 ? 46 THR A O 1 ATOM 345 C CB . THR A 1 46 ? 24.142 55.982 4.730 1.00 91.95 ? 46 THR A CB 1 ATOM 346 O OG1 . THR A 1 46 ? 23.401 57.077 5.280 1.00 96.93 ? 46 THR A OG1 1 ATOM 347 C CG2 . THR A 1 46 ? 23.378 55.404 3.554 1.00 91.29 ? 46 THR A CG2 1 ATOM 348 N N . GLN A 1 47 ? 24.671 55.355 8.167 1.00 99.75 ? 47 GLN A N 1 ATOM 349 C CA . GLN A 1 47 ? 25.402 55.783 9.351 1.00 97.12 ? 47 GLN A CA 1 ATOM 350 C C . GLN A 1 47 ? 26.645 54.918 9.538 1.00 93.35 ? 47 GLN A C 1 ATOM 351 O O . GLN A 1 47 ? 26.541 53.698 9.655 1.00 89.78 ? 47 GLN A O 1 ATOM 352 C CB . GLN A 1 47 ? 24.503 55.713 10.586 1.00 83.20 ? 47 GLN A CB 1 ATOM 353 C CG . GLN A 1 47 ? 23.189 56.459 10.426 1.00 81.78 ? 47 GLN A CG 1 ATOM 354 C CD . GLN A 1 47 ? 22.254 56.245 11.594 1.00 96.37 ? 47 GLN A CD 1 ATOM 355 O OE1 . GLN A 1 47 ? 21.199 55.625 11.455 1.00 118.24 ? 47 GLN A OE1 1 ATOM 356 N NE2 . GLN A 1 47 ? 22.635 56.759 12.758 1.00 86.32 ? 47 GLN A NE2 1 ATOM 357 N N . PRO A 1 48 ? 27.828 55.553 9.557 1.00 93.97 ? 48 PRO A N 1 ATOM 358 C CA . PRO A 1 48 ? 29.125 54.866 9.629 1.00 88.74 ? 48 PRO A CA 1 ATOM 359 C C . PRO A 1 48 ? 29.298 54.008 10.880 1.00 88.42 ? 48 PRO A C 1 ATOM 360 O O . PRO A 1 48 ? 29.102 54.491 11.994 1.00 91.68 ? 48 PRO A O 1 ATOM 361 C CB . PRO A 1 48 ? 30.131 56.022 9.635 1.00 89.67 ? 48 PRO A CB 1 ATOM 362 C CG . PRO A 1 48 ? 29.403 57.165 9.013 1.00 94.03 ? 48 PRO A CG 1 ATOM 363 C CD . PRO A 1 48 ? 27.985 57.013 9.460 1.00 88.67 ? 48 PRO A CD 1 ATOM 364 N N . GLY A 1 49 ? 29.684 52.750 10.686 1.00 90.16 ? 49 GLY A N 1 ATOM 365 C CA . GLY A 1 49 ? 29.907 51.833 11.790 1.00 93.33 ? 49 GLY A CA 1 ATOM 366 C C . GLY A 1 49 ? 28.639 51.306 12.440 1.00 90.66 ? 49 GLY A C 1 ATOM 367 O O . GLY A 1 49 ? 28.698 50.481 13.351 1.00 94.48 ? 49 GLY A O 1 ATOM 368 N N . ILE A 1 50 ? 27.489 51.776 11.970 1.00 87.72 ? 50 ILE A N 1 ATOM 369 C CA . ILE A 1 50 ? 26.212 51.396 12.562 1.00 94.71 ? 50 ILE A CA 1 ATOM 370 C C . ILE A 1 50 ? 25.539 50.255 11.803 1.00 95.98 ? 50 ILE A C 1 ATOM 371 O O . ILE A 1 50 ? 25.329 50.336 10.592 1.00 107.55 ? 50 ILE A O 1 ATOM 372 C CB . ILE A 1 50 ? 25.248 52.595 12.618 1.00 82.80 ? 50 ILE A CB 1 ATOM 373 C CG1 . ILE A 1 50 ? 25.882 53.740 13.404 1.00 77.81 ? 50 ILE A CG1 1 ATOM 374 C CG2 . ILE A 1 50 ? 23.923 52.188 13.247 1.00 74.19 ? 50 ILE A CG2 1 ATOM 375 C CD1 . ILE A 1 50 ? 26.221 53.374 14.829 1.00 80.39 ? 50 ILE A CD1 1 ATOM 376 N N . VAL A 1 51 ? 25.202 49.192 12.526 1.00 81.25 ? 51 VAL A N 1 ATOM 377 C CA . VAL A 1 51 ? 24.509 48.053 11.935 1.00 82.42 ? 51 VAL A CA 1 ATOM 378 C C . VAL A 1 51 ? 23.046 48.024 12.364 1.00 81.91 ? 51 VAL A C 1 ATOM 379 O O . VAL A 1 51 ? 22.742 48.020 13.560 1.00 75.22 ? 51 VAL A O 1 ATOM 380 C CB . VAL A 1 51 ? 25.175 46.723 12.323 1.00 85.81 ? 51 VAL A CB 1 ATOM 381 C CG1 . VAL A 1 51 ? 24.416 45.557 11.718 1.00 85.54 ? 51 VAL A CG1 1 ATOM 382 C CG2 . VAL A 1 51 ? 26.626 46.708 11.879 1.00 96.37 ? 51 VAL A CG2 1 ATOM 383 N N . GLU A 1 52 ? 22.151 48.007 11.378 1.00 85.42 ? 52 GLU A N 1 ATOM 384 C CA . GLU A 1 52 ? 20.708 48.014 11.611 1.00 91.96 ? 52 GLU A CA 1 ATOM 385 C C . GLU A 1 52 ? 20.293 49.088 12.612 1.00 80.81 ? 52 GLU A C 1 ATOM 386 O O . GLU A 1 52 ? 19.805 48.781 13.698 1.00 83.58 ? 52 GLU A O 1 ATOM 387 C CB . GLU A 1 52 ? 20.234 46.641 12.094 1.00 86.26 ? 52 GLU A CB 1 ATOM 388 C CG . GLU A 1 52 ? 20.378 45.538 11.060 1.00 103.29 ? 52 GLU A CG 1 ATOM 389 C CD . GLU A 1 52 ? 19.839 44.209 11.549 1.00 116.91 ? 52 GLU A CD 1 ATOM 390 O OE1 . GLU A 1 52 ? 19.504 44.110 12.748 1.00 116.92 ? 52 GLU A OE1 1 ATOM 391 O OE2 . GLU A 1 52 ? 19.747 43.265 10.736 1.00 131.73 ? 52 GLU A OE2 1 ATOM 392 N N . GLY A 1 53 ? 20.496 50.347 12.241 1.00 79.70 ? 53 GLY A N 1 ATOM 393 C CA . GLY A 1 53 ? 20.142 51.452 13.108 1.00 70.26 ? 53 GLY A CA 1 ATOM 394 C C . GLY A 1 53 ? 18.647 51.687 13.097 1.00 67.61 ? 53 GLY A C 1 ATOM 395 O O . GLY A 1 53 ? 18.075 52.176 14.070 1.00 62.76 ? 53 GLY A O 1 ATOM 396 N N . GLY A 1 54 ? 18.012 51.326 11.987 1.00 67.26 ? 54 GLY A N 1 ATOM 397 C CA . GLY A 1 54 ? 16.588 51.543 11.824 1.00 72.58 ? 54 GLY A CA 1 ATOM 398 C C . GLY A 1 54 ? 16.305 52.849 11.111 1.00 71.28 ? 54 GLY A C 1 ATOM 399 O O . GLY A 1 54 ? 17.068 53.809 11.229 1.00 76.82 ? 54 GLY A O 1 ATOM 400 N N . GLN A 1 55 ? 15.205 52.886 10.368 1.00 73.21 ? 55 GLN A N 1 ATOM 401 C CA . GLN A 1 55 ? 14.824 54.086 9.639 1.00 75.98 ? 55 GLN A CA 1 ATOM 402 C C . GLN A 1 55 ? 13.404 54.516 9.969 1.00 71.27 ? 55 GLN A C 1 ATOM 403 O O . GLN A 1 55 ? 12.696 53.851 10.722 1.00 77.07 ? 55 GLN A O 1 ATOM 404 C CB . GLN A 1 55 ? 14.939 53.861 8.128 1.00 78.53 ? 55 GLN A CB 1 ATOM 405 C CG . GLN A 1 55 ? 16.355 53.701 7.609 1.00 94.53 ? 55 GLN A CG 1 ATOM 406 C CD . GLN A 1 55 ? 16.401 53.535 6.101 1.00 107.10 ? 55 GLN A CD 1 ATOM 407 O OE1 . GLN A 1 55 ? 15.374 53.320 5.457 1.00 103.13 ? 55 GLN A OE1 1 ATOM 408 N NE2 . GLN A 1 55 ? 17.596 53.638 5.530 1.00 118.65 ? 55 GLN A NE2 1 ATOM 409 N N . VAL A 1 56 ? 13.009 55.647 9.399 1.00 80.29 ? 56 VAL A N 1 ATOM 410 C CA . VAL A 1 56 ? 11.616 56.056 9.331 1.00 66.22 ? 56 VAL A CA 1 ATOM 411 C C . VAL A 1 56 ? 11.395 56.558 7.917 1.00 69.79 ? 56 VAL A C 1 ATOM 412 O O . VAL A 1 56 ? 12.037 57.516 7.489 1.00 71.77 ? 56 VAL A O 1 ATOM 413 C CB . VAL A 1 56 ? 11.263 57.158 10.345 1.00 64.78 ? 56 VAL A CB 1 ATOM 414 C CG1 . VAL A 1 56 ? 9.837 57.636 10.126 1.00 65.18 ? 56 VAL A CG1 1 ATOM 415 C CG2 . VAL A 1 56 ? 11.448 56.660 11.768 1.00 62.11 ? 56 VAL A CG2 1 ATOM 416 N N . LEU A 1 57 ? 10.500 55.910 7.183 1.00 70.28 ? 57 LEU A N 1 ATOM 417 C CA . LEU A 1 57 ? 10.328 56.240 5.778 1.00 78.81 ? 57 LEU A CA 1 ATOM 418 C C . LEU A 1 57 ? 9.096 57.098 5.546 1.00 88.60 ? 57 LEU A C 1 ATOM 419 O O . LEU A 1 57 ? 8.079 56.939 6.219 1.00 98.03 ? 57 LEU A O 1 ATOM 420 C CB . LEU A 1 57 ? 10.252 54.967 4.932 1.00 79.09 ? 57 LEU A CB 1 ATOM 421 C CG . LEU A 1 57 ? 11.553 54.163 4.858 1.00 82.90 ? 57 LEU A CG 1 ATOM 422 C CD1 . LEU A 1 57 ? 11.588 53.072 5.920 1.00 75.16 ? 57 LEU A CD1 1 ATOM 423 C CD2 . LEU A 1 57 ? 11.765 53.583 3.467 1.00 93.20 ? 57 LEU A CD2 1 ATOM 424 N N . LYS A 1 58 ? 9.203 58.017 4.592 1.00 84.78 ? 58 LYS A N 1 ATOM 425 C CA . LYS A 1 58 ? 8.078 58.854 4.209 1.00 78.87 ? 58 LYS A CA 1 ATOM 426 C C . LYS A 1 58 ? 7.460 58.311 2.927 1.00 84.21 ? 58 LYS A C 1 ATOM 427 O O . LYS A 1 58 ? 8.066 58.374 1.859 1.00 95.18 ? 58 LYS A O 1 ATOM 428 C CB . LYS A 1 58 ? 8.519 60.307 4.021 1.00 91.95 ? 58 LYS A CB 1 ATOM 429 C CG . LYS A 1 58 ? 7.370 61.291 3.852 1.00 90.60 ? 58 LYS A CG 1 ATOM 430 C CD . LYS A 1 58 ? 7.873 62.697 3.561 1.00 84.32 ? 58 LYS A CD 1 ATOM 431 C CE . LYS A 1 58 ? 8.540 62.771 2.195 1.00 114.29 ? 58 LYS A CE 1 ATOM 432 N NZ . LYS A 1 58 ? 8.927 64.162 1.833 1.00 123.79 ? 58 LYS A NZ 1 ATOM 433 N N . CYS A 1 59 ? 6.253 57.769 3.046 1.00 94.12 ? 59 CYS A N 1 ATOM 434 C CA . CYS A 1 59 ? 5.542 57.217 1.900 1.00 109.37 ? 59 CYS A CA 1 ATOM 435 C C . CYS A 1 59 ? 4.436 58.170 1.467 1.00 93.68 ? 59 CYS A C 1 ATOM 436 O O . CYS A 1 59 ? 3.761 58.765 2.306 1.00 89.91 ? 59 CYS A O 1 ATOM 437 C CB . CYS A 1 59 ? 4.963 55.843 2.237 1.00 122.60 ? 59 CYS A CB 1 ATOM 438 S SG . CYS A 1 59 ? 6.181 54.625 2.788 1.00 97.06 ? 59 CYS A SG 1 ATOM 439 N N . ASP A 1 60 ? 4.242 58.308 0.161 1.00 90.32 ? 60 ASP A N 1 ATOM 440 C CA . ASP A 1 60 ? 3.293 59.290 -0.348 1.00 93.04 ? 60 ASP A CA 1 ATOM 441 C C . ASP A 1 60 ? 2.064 58.640 -0.969 1.00 105.67 ? 60 ASP A C 1 ATOM 442 O O . ASP A 1 60 ? 2.121 57.512 -1.457 1.00 109.89 ? 60 ASP A O 1 ATOM 443 C CB . ASP A 1 60 ? 3.966 60.210 -1.369 1.00 118.81 ? 60 ASP A CB 1 ATOM 444 C CG . ASP A 1 60 ? 4.612 59.448 -2.504 1.00 127.98 ? 60 ASP A CG 1 ATOM 445 O OD1 . ASP A 1 60 ? 3.872 58.933 -3.367 1.00 131.01 ? 60 ASP A OD1 1 ATOM 446 O OD2 . ASP A 1 60 ? 5.859 59.372 -2.538 1.00 129.87 ? 60 ASP A OD2 1 ATOM 447 N N . TRP A 1 61 ? 0.953 59.367 -0.935 1.00 114.99 ? 61 TRP A N 1 ATOM 448 C CA . TRP A 1 61 ? -0.302 58.908 -1.514 1.00 99.52 ? 61 TRP A CA 1 ATOM 449 C C . TRP A 1 61 ? -0.375 59.334 -2.975 1.00 106.29 ? 61 TRP A C 1 ATOM 450 O O . TRP A 1 61 ? -1.394 59.150 -3.639 1.00 130.96 ? 61 TRP A O 1 ATOM 451 C CB . TRP A 1 61 ? -1.499 59.450 -0.732 1.00 97.26 ? 61 TRP A CB 1 ATOM 452 C CG . TRP A 1 61 ? -2.772 58.732 -1.040 1.00 102.53 ? 61 TRP A CG 1 ATOM 453 C CD1 . TRP A 1 61 ? -3.125 57.481 -0.627 1.00 102.84 ? 61 TRP A CD1 1 ATOM 454 C CD2 . TRP A 1 61 ? -3.864 59.215 -1.832 1.00 111.89 ? 61 TRP A CD2 1 ATOM 455 N NE1 . TRP A 1 61 ? -4.368 57.155 -1.110 1.00 110.45 ? 61 TRP A NE1 1 ATOM 456 C CE2 . TRP A 1 61 ? -4.844 58.203 -1.854 1.00 121.12 ? 61 TRP A CE2 1 ATOM 457 C CE3 . TRP A 1 61 ? -4.108 60.404 -2.526 1.00 137.23 ? 61 TRP A CE3 1 ATOM 458 C CZ2 . TRP A 1 61 ? -6.049 58.344 -2.540 1.00 136.36 ? 61 TRP A CZ2 1 ATOM 459 C CZ3 . TRP A 1 61 ? -5.306 60.542 -3.208 1.00 147.67 ? 61 TRP A CZ3 1 ATOM 460 C CH2 . TRP A 1 61 ? -6.260 59.518 -3.210 1.00 146.95 ? 61 TRP A CH2 1 ATOM 461 N N . SER A 1 62 ? 0.726 59.889 -3.472 1.00 107.28 ? 62 SER A N 1 ATOM 462 C CA . SER A 1 62 ? 0.824 60.362 -4.851 1.00 131.47 ? 62 SER A CA 1 ATOM 463 C C . SER A 1 62 ? 0.663 59.229 -5.866 1.00 151.77 ? 62 SER A C 1 ATOM 464 O O . SER A 1 62 ? 0.693 59.470 -7.075 1.00 145.93 ? 62 SER A O 1 ATOM 465 C CB . SER A 1 62 ? 2.160 61.073 -5.074 1.00 136.84 ? 62 SER A CB 1 ATOM 466 O OG . SER A 1 62 ? 2.304 61.475 -6.424 1.00 116.75 ? 62 SER A OG 1 ATOM 467 N N . SER A 1 63 ? 0.561 58.003 -5.350 1.00 166.67 ? 63 SER A N 1 ATOM 468 C CA . SER A 1 63 ? 0.207 56.792 -6.099 1.00 177.85 ? 63 SER A CA 1 ATOM 469 C C . SER A 1 63 ? 1.408 56.175 -6.804 1.00 182.15 ? 63 SER A C 1 ATOM 470 O O . SER A 1 63 ? 1.292 55.119 -7.425 1.00 178.56 ? 63 SER A O 1 ATOM 471 C CB . SER A 1 63 ? -0.915 57.062 -7.109 1.00 171.02 ? 63 SER A CB 1 ATOM 472 O OG . SER A 1 63 ? -1.284 55.874 -7.787 1.00 165.30 ? 63 SER A OG 1 ATOM 473 N N . THR A 1 64 ? 2.561 56.830 -6.707 1.00 176.68 ? 64 THR A N 1 ATOM 474 C CA . THR A 1 64 ? 3.801 56.223 -7.171 1.00 155.25 ? 64 THR A CA 1 ATOM 475 C C . THR A 1 64 ? 4.199 55.115 -6.200 1.00 134.27 ? 64 THR A C 1 ATOM 476 O O . THR A 1 64 ? 5.044 54.274 -6.513 1.00 129.78 ? 64 THR A O 1 ATOM 477 C CB . THR A 1 64 ? 4.942 57.251 -7.299 1.00 144.97 ? 64 THR A CB 1 ATOM 478 O OG1 . THR A 1 64 ? 6.112 56.606 -7.818 1.00 146.83 ? 64 THR A OG1 1 ATOM 479 C CG2 . THR A 1 64 ? 5.270 57.862 -5.950 1.00 125.21 ? 64 THR A CG2 1 ATOM 480 N N . ARG A 1 65 ? 3.580 55.136 -5.020 1.00 117.46 ? 65 ARG A N 1 ATOM 481 C CA . ARG A 1 65 ? 3.716 54.079 -4.020 1.00 127.87 ? 65 ARG A CA 1 ATOM 482 C C . ARG A 1 65 ? 5.153 53.936 -3.529 1.00 132.28 ? 65 ARG A C 1 ATOM 483 O O . ARG A 1 65 ? 5.592 52.843 -3.168 1.00 136.58 ? 65 ARG A O 1 ATOM 484 C CB . ARG A 1 65 ? 3.217 52.748 -4.589 1.00 143.51 ? 65 ARG A CB 1 ATOM 485 C CG . ARG A 1 65 ? 2.470 51.888 -3.593 1.00 128.95 ? 65 ARG A CG 1 ATOM 486 C CD . ARG A 1 65 ? 1.296 52.641 -2.991 1.00 124.83 ? 65 ARG A CD 1 ATOM 487 N NE . ARG A 1 65 ? 0.405 53.186 -4.011 1.00 142.97 ? 65 ARG A NE 1 ATOM 488 C CZ . ARG A 1 65 ? -0.678 52.566 -4.468 1.00 147.36 ? 65 ARG A CZ 1 ATOM 489 N NH1 . ARG A 1 65 ? -1.013 51.373 -3.996 1.00 125.31 ? 65 ARG A NH1 1 ATOM 490 N NH2 . ARG A 1 65 ? -1.429 53.142 -5.398 1.00 148.96 ? 65 ARG A NH2 1 ATOM 491 N N . ARG A 1 66 ? 5.875 55.051 -3.509 1.00 121.40 ? 66 ARG A N 1 ATOM 492 C CA . ARG A 1 66 ? 7.286 55.048 -3.151 1.00 101.11 ? 66 ARG A CA 1 ATOM 493 C C . ARG A 1 66 ? 7.512 55.643 -1.765 1.00 103.06 ? 66 ARG A C 1 ATOM 494 O O . ARG A 1 66 ? 6.795 56.549 -1.339 1.00 93.42 ? 66 ARG A O 1 ATOM 495 C CB . ARG A 1 66 ? 8.093 55.816 -4.201 1.00 102.91 ? 66 ARG A CB 1 ATOM 496 C CG . ARG A 1 66 ? 9.578 55.939 -3.908 1.00 121.43 ? 66 ARG A CG 1 ATOM 497 C CD . ARG A 1 66 ? 10.288 56.677 -5.028 1.00 139.96 ? 66 ARG A CD 1 ATOM 498 N NE . ARG A 1 66 ? 11.605 57.155 -4.624 1.00 136.36 ? 66 ARG A NE 1 ATOM 499 C CZ . ARG A 1 66 ? 12.425 57.834 -5.419 1.00 134.87 ? 66 ARG A CZ 1 ATOM 500 N NH1 . ARG A 1 66 ? 12.064 58.111 -6.664 1.00 135.68 ? 66 ARG A NH1 1 ATOM 501 N NH2 . ARG A 1 66 ? 13.607 58.233 -4.970 1.00 131.30 ? 66 ARG A NH2 1 ATOM 502 N N . CYS A 1 67 ? 8.507 55.117 -1.061 1.00 109.46 ? 67 CYS A N 1 ATOM 503 C CA . CYS A 1 67 ? 8.865 55.624 0.254 1.00 96.15 ? 67 CYS A CA 1 ATOM 504 C C . CYS A 1 67 ? 10.309 56.109 0.269 1.00 111.08 ? 67 CYS A C 1 ATOM 505 O O . CYS A 1 67 ? 11.175 55.520 -0.379 1.00 111.45 ? 67 CYS A O 1 ATOM 506 C CB . CYS A 1 67 ? 8.663 54.544 1.314 1.00 91.44 ? 67 CYS A CB 1 ATOM 507 S SG . CYS A 1 67 ? 7.073 53.701 1.212 1.00 141.76 ? 67 CYS A SG 1 ATOM 508 N N . GLN A 1 68 ? 10.565 57.184 1.007 1.00 114.15 ? 68 GLN A N 1 ATOM 509 C CA . GLN A 1 68 ? 11.925 57.680 1.170 1.00 92.20 ? 68 GLN A CA 1 ATOM 510 C C . GLN A 1 68 ? 12.275 57.754 2.645 1.00 87.96 ? 68 GLN A C 1 ATOM 511 O O . GLN A 1 68 ? 11.460 58.187 3.458 1.00 99.28 ? 68 GLN A O 1 ATOM 512 C CB . GLN A 1 68 ? 12.080 59.060 0.526 1.00 100.55 ? 68 GLN A CB 1 ATOM 513 C CG . GLN A 1 68 ? 11.850 59.083 -0.974 1.00 127.95 ? 68 GLN A CG 1 ATOM 514 C CD . GLN A 1 68 ? 13.011 58.496 -1.748 1.00 137.38 ? 68 GLN A CD 1 ATOM 515 O OE1 . GLN A 1 68 ? 12.887 57.443 -2.374 1.00 137.45 ? 68 GLN A OE1 1 ATOM 516 N NE2 . GLN A 1 68 ? 14.150 59.180 -1.715 1.00 131.13 ? 68 GLN A NE2 1 ATOM 517 N N . PRO A 1 69 ? 13.500 57.345 2.996 1.00 87.73 ? 69 PRO A N 1 ATOM 518 C CA . PRO A 1 69 ? 13.943 57.422 4.389 1.00 78.98 ? 69 PRO A CA 1 ATOM 519 C C . PRO A 1 69 ? 14.151 58.869 4.816 1.00 78.87 ? 69 PRO A C 1 ATOM 520 O O . PRO A 1 69 ? 14.729 59.649 4.064 1.00 81.83 ? 69 PRO A O 1 ATOM 521 C CB . PRO A 1 69 ? 15.267 56.650 4.385 1.00 79.50 ? 69 PRO A CB 1 ATOM 522 C CG . PRO A 1 69 ? 15.235 55.824 3.141 1.00 88.83 ? 69 PRO A CG 1 ATOM 523 C CD . PRO A 1 69 ? 14.475 56.643 2.148 1.00 99.05 ? 69 PRO A CD 1 ATOM 524 N N . ILE A 1 70 ? 13.677 59.220 6.004 1.00 83.81 ? 70 ILE A N 1 ATOM 525 C CA . ILE A 1 70 ? 13.862 60.563 6.531 1.00 78.00 ? 70 ILE A CA 1 ATOM 526 C C . ILE A 1 70 ? 15.199 60.667 7.249 1.00 76.77 ? 70 ILE A C 1 ATOM 527 O O . ILE A 1 70 ? 15.543 59.802 8.053 1.00 103.22 ? 70 ILE A O 1 ATOM 528 C CB . ILE A 1 70 ? 12.735 60.951 7.503 1.00 73.67 ? 70 ILE A CB 1 ATOM 529 C CG1 . ILE A 1 70 ? 11.373 60.809 6.827 1.00 74.64 ? 70 ILE A CG1 1 ATOM 530 C CG2 . ILE A 1 70 ? 12.928 62.370 8.011 1.00 74.05 ? 70 ILE A CG2 1 ATOM 531 C CD1 . ILE A 1 70 ? 10.217 61.173 7.729 1.00 72.84 ? 70 ILE A CD1 1 ATOM 532 N N . GLU A 1 71 ? 15.952 61.724 6.962 1.00 79.22 ? 71 GLU A N 1 ATOM 533 C CA . GLU A 1 71 ? 17.226 61.929 7.635 1.00 92.73 ? 71 GLU A CA 1 ATOM 534 C C . GLU A 1 71 ? 16.993 62.535 9.010 1.00 102.44 ? 71 GLU A C 1 ATOM 535 O O . GLU A 1 71 ? 16.482 63.647 9.133 1.00 103.08 ? 71 GLU A O 1 ATOM 536 C CB . GLU A 1 71 ? 18.143 62.835 6.811 1.00 108.16 ? 71 GLU A CB 1 ATOM 537 C CG . GLU A 1 71 ? 18.421 62.343 5.395 1.00 138.51 ? 71 GLU A CG 1 ATOM 538 C CD . GLU A 1 71 ? 17.323 62.711 4.410 1.00 143.46 ? 71 GLU A CD 1 ATOM 539 O OE1 . GLU A 1 71 ? 16.227 63.117 4.856 1.00 136.87 ? 71 GLU A OE1 1 ATOM 540 O OE2 . GLU A 1 71 ? 17.557 62.599 3.189 1.00 136.24 ? 71 GLU A OE2 1 ATOM 541 N N . PHE A 1 72 ? 17.387 61.799 10.042 1.00 102.38 ? 72 PHE A N 1 ATOM 542 C CA . PHE A 1 72 ? 17.245 62.260 11.414 1.00 93.18 ? 72 PHE A CA 1 ATOM 543 C C . PHE A 1 72 ? 18.619 62.463 12.037 1.00 90.17 ? 72 PHE A C 1 ATOM 544 O O . PHE A 1 72 ? 18.997 63.581 12.383 1.00 101.00 ? 72 PHE A O 1 ATOM 545 C CB . PHE A 1 72 ? 16.433 61.263 12.244 1.00 84.23 ? 72 PHE A CB 1 ATOM 546 C CG . PHE A 1 72 ? 14.942 61.423 12.113 1.00 97.41 ? 72 PHE A CG 1 ATOM 547 C CD1 . PHE A 1 72 ? 14.266 62.374 12.860 1.00 88.00 ? 72 PHE A CD1 1 ATOM 548 C CD2 . PHE A 1 72 ? 14.213 60.603 11.266 1.00 109.17 ? 72 PHE A CD2 1 ATOM 549 C CE1 . PHE A 1 72 ? 12.893 62.515 12.754 1.00 98.48 ? 72 PHE A CE1 1 ATOM 550 C CE2 . PHE A 1 72 ? 12.839 60.738 11.157 1.00 92.12 ? 72 PHE A CE2 1 ATOM 551 C CZ . PHE A 1 72 ? 12.179 61.696 11.901 1.00 88.99 ? 72 PHE A CZ 1 ATOM 552 N N . ASP A 1 73 ? 19.359 61.368 12.178 1.00 79.50 ? 73 ASP A N 1 ATOM 553 C CA . ASP A 1 73 ? 20.696 61.413 12.754 1.00 74.62 ? 73 ASP A CA 1 ATOM 554 C C . ASP A 1 73 ? 21.751 61.498 11.661 1.00 111.39 ? 73 ASP A C 1 ATOM 555 O O . ASP A 1 73 ? 22.502 62.474 11.600 1.00 153.69 ? 73 ASP A O 1 ATOM 556 C CB . ASP A 1 73 ? 20.949 60.192 13.637 1.00 90.77 ? 73 ASP A CB 1 ATOM 557 C CG . ASP A 1 73 ? 22.314 60.223 14.295 1.00 99.97 ? 73 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 73 ? 22.884 61.324 14.440 1.00 106.55 ? 73 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 73 ? 22.816 59.145 14.674 1.00 131.30 ? 73 ASP A OD2 1 ATOM 560 N N . ALA A 1 74 ? 21.825 60.456 10.833 1.00 74.41 ? 74 ALA A N 1 ATOM 561 C CA . ALA A 1 74 ? 22.744 60.405 9.686 1.00 104.10 ? 74 ALA A CA 1 ATOM 562 C C . ALA A 1 74 ? 24.215 60.328 10.099 1.00 80.28 ? 74 ALA A C 1 ATOM 563 O O . ALA A 1 74 ? 25.097 60.242 9.248 1.00 80.10 ? 74 ALA A O 1 ATOM 564 C CB . ALA A 1 74 ? 22.520 61.604 8.758 1.00 78.79 ? 74 ALA A CB 1 ATOM 565 N N . THR A 1 75 ? 24.474 60.362 11.402 1.00 81.93 ? 75 THR A N 1 ATOM 566 C CA . THR A 1 75 ? 25.836 60.310 11.918 1.00 83.68 ? 75 THR A CA 1 ATOM 567 C C . THR A 1 75 ? 26.056 59.049 12.744 1.00 87.52 ? 75 THR A C 1 ATOM 568 O O . THR A 1 75 ? 25.107 58.451 13.247 1.00 83.86 ? 75 THR A O 1 ATOM 569 C CB . THR A 1 75 ? 26.158 61.537 12.788 1.00 76.14 ? 75 THR A CB 1 ATOM 570 O OG1 . THR A 1 75 ? 25.465 61.435 14.037 1.00 88.05 ? 75 THR A OG1 1 ATOM 571 C CG2 . THR A 1 75 ? 25.733 62.812 12.083 1.00 88.40 ? 75 THR A CG2 1 ATOM 572 N N . GLY A 1 76 ? 27.314 58.650 12.885 1.00 94.25 ? 76 GLY A N 1 ATOM 573 C CA . GLY A 1 76 ? 27.654 57.464 13.646 1.00 80.99 ? 76 GLY A CA 1 ATOM 574 C C . GLY A 1 76 ? 27.759 57.747 15.133 1.00 79.27 ? 76 GLY A C 1 ATOM 575 O O . GLY A 1 76 ? 27.104 58.651 15.652 1.00 81.85 ? 76 GLY A O 1 ATOM 576 N N . ASN A 1 77 ? 28.582 56.963 15.820 1.00 75.95 ? 77 ASN A N 1 ATOM 577 C CA . ASN A 1 77 ? 28.754 57.101 17.261 1.00 81.88 ? 77 ASN A CA 1 ATOM 578 C C . ASN A 1 77 ? 29.718 58.209 17.673 1.00 96.85 ? 77 ASN A C 1 ATOM 579 O O . ASN A 1 77 ? 30.856 58.265 17.203 1.00 82.93 ? 77 ASN A O 1 ATOM 580 C CB . ASN A 1 77 ? 29.236 55.779 17.849 1.00 86.33 ? 77 ASN A CB 1 ATOM 581 C CG . ASN A 1 77 ? 28.226 54.676 17.685 1.00 76.79 ? 77 ASN A CG 1 ATOM 582 O OD1 . ASN A 1 77 ? 27.028 54.895 17.838 1.00 75.33 ? 77 ASN A OD1 1 ATOM 583 N ND2 . ASN A 1 77 ? 28.700 53.480 17.363 1.00 100.17 ? 77 ASN A ND2 1 ATOM 584 N N . ARG A 1 78 ? 29.254 59.084 18.559 1.00 98.98 ? 78 ARG A N 1 ATOM 585 C CA . ARG A 1 78 ? 30.117 60.085 19.173 1.00 81.90 ? 78 ARG A CA 1 ATOM 586 C C . ARG A 1 78 ? 31.063 59.406 20.152 1.00 91.86 ? 78 ARG A C 1 ATOM 587 O O . ARG A 1 78 ? 30.777 58.311 20.639 1.00 97.67 ? 78 ARG A O 1 ATOM 588 C CB . ARG A 1 78 ? 29.290 61.155 19.883 1.00 73.00 ? 78 ARG A CB 1 ATOM 589 C CG . ARG A 1 78 ? 28.562 62.094 18.944 1.00 74.90 ? 78 ARG A CG 1 ATOM 590 C CD . ARG A 1 78 ? 27.599 62.994 19.699 1.00 71.58 ? 78 ARG A CD 1 ATOM 591 N NE . ARG A 1 78 ? 26.441 62.255 20.187 1.00 68.96 ? 78 ARG A NE 1 ATOM 592 C CZ . ARG A 1 78 ? 25.351 62.822 20.692 1.00 91.00 ? 78 ARG A CZ 1 ATOM 593 N NH1 . ARG A 1 78 ? 25.268 64.143 20.778 1.00 77.51 ? 78 ARG A NH1 1 ATOM 594 N NH2 . ARG A 1 78 ? 24.341 62.068 21.108 1.00 81.99 ? 78 ARG A NH2 1 ATOM 595 N N . ASP A 1 79 ? 32.185 60.056 20.444 1.00 82.71 ? 79 ASP A N 1 ATOM 596 C CA . ASP A 1 79 ? 33.214 59.444 21.277 1.00 86.25 ? 79 ASP A CA 1 ATOM 597 C C . ASP A 1 79 ? 33.391 60.139 22.625 1.00 91.23 ? 79 ASP A C 1 ATOM 598 O O . ASP A 1 79 ? 33.345 61.366 22.723 1.00 114.86 ? 79 ASP A O 1 ATOM 599 C CB . ASP A 1 79 ? 34.550 59.423 20.529 1.00 104.27 ? 79 ASP A CB 1 ATOM 600 C CG . ASP A 1 79 ? 34.501 58.574 19.273 1.00 121.79 ? 79 ASP A CG 1 ATOM 601 O OD1 . ASP A 1 79 ? 33.758 57.568 19.263 1.00 137.44 ? 79 ASP A OD1 1 ATOM 602 O OD2 . ASP A 1 79 ? 35.204 58.912 18.297 1.00 105.58 ? 79 ASP A OD2 1 ATOM 603 N N . TYR A 1 80 ? 33.582 59.332 23.664 1.00 84.50 ? 80 TYR A N 1 ATOM 604 C CA . TYR A 1 80 ? 33.928 59.819 24.994 1.00 84.84 ? 80 TYR A CA 1 ATOM 605 C C . TYR A 1 80 ? 35.429 60.094 25.063 1.00 102.05 ? 80 TYR A C 1 ATOM 606 O O . TYR A 1 80 ? 35.902 60.868 25.899 1.00 100.31 ? 80 TYR A O 1 ATOM 607 C CB . TYR A 1 80 ? 33.505 58.796 26.054 1.00 77.77 ? 80 TYR A CB 1 ATOM 608 C CG . TYR A 1 80 ? 34.017 59.064 27.452 1.00 79.63 ? 80 TYR A CG 1 ATOM 609 C CD1 . TYR A 1 80 ? 33.340 59.921 28.308 1.00 81.11 ? 80 TYR A CD1 1 ATOM 610 C CD2 . TYR A 1 80 ? 35.165 58.441 27.923 1.00 81.50 ? 80 TYR A CD2 1 ATOM 611 C CE1 . TYR A 1 80 ? 33.800 60.160 29.592 1.00 79.47 ? 80 TYR A CE1 1 ATOM 612 C CE2 . TYR A 1 80 ? 35.632 58.676 29.202 1.00 82.56 ? 80 TYR A CE2 1 ATOM 613 C CZ . TYR A 1 80 ? 34.947 59.536 30.033 1.00 81.78 ? 80 TYR A CZ 1 ATOM 614 O OH . TYR A 1 80 ? 35.411 59.769 31.309 1.00 83.66 ? 80 TYR A OH 1 ATOM 615 N N . ALA A 1 81 ? 36.157 59.473 24.139 1.00 88.66 ? 81 ALA A N 1 ATOM 616 C CA . ALA A 1 81 ? 37.612 59.512 24.093 1.00 90.32 ? 81 ALA A CA 1 ATOM 617 C C . ALA A 1 81 ? 38.070 58.771 22.848 1.00 104.07 ? 81 ALA A C 1 ATOM 618 O O . ALA A 1 81 ? 37.254 58.165 22.153 1.00 130.84 ? 81 ALA A O 1 ATOM 619 C CB . ALA A 1 81 ? 38.214 58.886 25.342 1.00 88.96 ? 81 ALA A CB 1 ATOM 620 N N . LYS A 1 82 ? 39.366 58.822 22.557 1.00 104.91 ? 82 LYS A N 1 ATOM 621 C CA . LYS A 1 82 ? 39.896 58.120 21.396 1.00 110.92 ? 82 LYS A CA 1 ATOM 622 C C . LYS A 1 82 ? 39.695 56.619 21.571 1.00 116.78 ? 82 LYS A C 1 ATOM 623 O O . LYS A 1 82 ? 40.098 56.048 22.585 1.00 127.23 ? 82 LYS A O 1 ATOM 624 C CB . LYS A 1 82 ? 41.376 58.448 21.187 1.00 125.99 ? 82 LYS A CB 1 ATOM 625 C CG . LYS A 1 82 ? 41.934 57.968 19.855 1.00 144.35 ? 82 LYS A CG 1 ATOM 626 C CD . LYS A 1 82 ? 43.346 58.486 19.618 1.00 147.82 ? 82 LYS A CD 1 ATOM 627 C CE . LYS A 1 82 ? 43.869 58.055 18.256 1.00 148.67 ? 82 LYS A CE 1 ATOM 628 N NZ . LYS A 1 82 ? 45.253 58.546 18.007 1.00 146.74 ? 82 LYS A NZ 1 ATOM 629 N N . ASP A 1 83 ? 39.057 55.999 20.581 1.00 121.33 ? 83 ASP A N 1 ATOM 630 C CA . ASP A 1 83 ? 38.710 54.578 20.616 1.00 116.20 ? 83 ASP A CA 1 ATOM 631 C C . ASP A 1 83 ? 37.867 54.212 21.838 1.00 106.31 ? 83 ASP A C 1 ATOM 632 O O . ASP A 1 83 ? 37.961 53.099 22.355 1.00 122.16 ? 83 ASP A O 1 ATOM 633 C CB . ASP A 1 83 ? 39.975 53.715 20.574 1.00 132.81 ? 83 ASP A CB 1 ATOM 634 C CG . ASP A 1 83 ? 40.790 53.938 19.316 1.00 149.94 ? 83 ASP A CG 1 ATOM 635 O OD1 . ASP A 1 83 ? 40.199 54.330 18.287 1.00 158.91 ? 83 ASP A OD1 1 ATOM 636 O OD2 . ASP A 1 83 ? 42.019 53.721 19.354 1.00 146.81 ? 83 ASP A OD2 1 ATOM 637 N N . ASP A 1 84 ? 37.054 55.155 22.302 1.00 94.41 ? 84 ASP A N 1 ATOM 638 C CA . ASP A 1 84 ? 36.139 54.903 23.410 1.00 91.87 ? 84 ASP A CA 1 ATOM 639 C C . ASP A 1 84 ? 34.791 55.577 23.163 1.00 97.65 ? 84 ASP A C 1 ATOM 640 O O . ASP A 1 84 ? 34.563 56.697 23.618 1.00 89.91 ? 84 ASP A O 1 ATOM 641 C CB . ASP A 1 84 ? 36.738 55.383 24.731 1.00 94.26 ? 84 ASP A CB 1 ATOM 642 C CG . ASP A 1 84 ? 36.118 54.697 25.934 1.00 102.89 ? 84 ASP A CG 1 ATOM 643 O OD1 . ASP A 1 84 ? 34.915 54.364 25.882 1.00 124.24 ? 84 ASP A OD1 1 ATOM 644 O OD2 . ASP A 1 84 ? 36.837 54.481 26.933 1.00 103.89 ? 84 ASP A OD2 1 ATOM 645 N N . PRO A 1 85 ? 33.899 54.895 22.427 1.00 97.48 ? 85 PRO A N 1 ATOM 646 C CA . PRO A 1 85 ? 32.586 55.407 22.013 1.00 82.58 ? 85 PRO A CA 1 ATOM 647 C C . PRO A 1 85 ? 31.714 55.892 23.169 1.00 79.54 ? 85 PRO A C 1 ATOM 648 O O . PRO A 1 85 ? 31.631 55.230 24.206 1.00 79.45 ? 85 PRO A O 1 ATOM 649 C CB . PRO A 1 85 ? 31.940 54.196 21.334 1.00 80.71 ? 85 PRO A CB 1 ATOM 650 C CG . PRO A 1 85 ? 33.081 53.365 20.882 1.00 89.57 ? 85 PRO A CG 1 ATOM 651 C CD . PRO A 1 85 ? 34.129 53.525 21.939 1.00 93.04 ? 85 PRO A CD 1 ATOM 652 N N . LEU A 1 86 ? 31.082 57.048 22.983 1.00 77.30 ? 86 LEU A N 1 ATOM 653 C CA . LEU A 1 86 ? 30.131 57.581 23.952 1.00 74.33 ? 86 LEU A CA 1 ATOM 654 C C . LEU A 1 86 ? 28.769 56.922 23.792 1.00 82.69 ? 86 LEU A C 1 ATOM 655 O O . LEU A 1 86 ? 28.051 56.699 24.763 1.00 82.22 ? 86 LEU A O 1 ATOM 656 C CB . LEU A 1 86 ? 29.992 59.095 23.795 1.00 73.88 ? 86 LEU A CB 1 ATOM 657 C CG . LEU A 1 86 ? 29.067 59.787 24.797 1.00 69.63 ? 86 LEU A CG 1 ATOM 658 C CD1 . LEU A 1 86 ? 29.870 60.468 25.890 1.00 96.98 ? 86 LEU A CD1 1 ATOM 659 C CD2 . LEU A 1 86 ? 28.160 60.778 24.092 1.00 75.60 ? 86 LEU A CD2 1 ATOM 660 N N . GLU A 1 87 ? 28.414 56.629 22.547 1.00 108.11 ? 87 GLU A N 1 ATOM 661 C CA . GLU A 1 87 ? 27.141 55.995 22.233 1.00 80.28 ? 87 GLU A CA 1 ATOM 662 C C . GLU A 1 87 ? 27.375 54.787 21.334 1.00 82.11 ? 87 GLU A C 1 ATOM 663 O O . GLU A 1 87 ? 28.466 54.608 20.796 1.00 95.01 ? 87 GLU A O 1 ATOM 664 C CB . GLU A 1 87 ? 26.191 56.999 21.575 1.00 76.91 ? 87 GLU A CB 1 ATOM 665 C CG . GLU A 1 87 ? 26.866 57.925 20.575 1.00 79.87 ? 87 GLU A CG 1 ATOM 666 C CD . GLU A 1 87 ? 25.984 59.089 20.174 1.00 84.65 ? 87 GLU A CD 1 ATOM 667 O OE1 . GLU A 1 87 ? 24.978 59.340 20.870 1.00 82.41 ? 87 GLU A OE1 1 ATOM 668 O OE2 . GLU A 1 87 ? 26.297 59.752 19.163 1.00 87.52 ? 87 GLU A OE2 1 ATOM 669 N N . PHE A 1 88 ? 26.357 53.949 21.186 1.00 101.82 ? 88 PHE A N 1 ATOM 670 C CA . PHE A 1 88 ? 26.519 52.674 20.495 1.00 105.50 ? 88 PHE A CA 1 ATOM 671 C C . PHE A 1 88 ? 25.619 52.562 19.273 1.00 93.16 ? 88 PHE A C 1 ATOM 672 O O . PHE A 1 88 ? 26.107 52.313 18.166 1.00 103.92 ? 88 PHE A O 1 ATOM 673 C CB . PHE A 1 88 ? 26.310 51.531 21.481 1.00 70.78 ? 88 PHE A CB 1 ATOM 674 C CG . PHE A 1 88 ? 27.416 51.437 22.485 1.00 71.50 ? 88 PHE A CG 1 ATOM 675 C CD1 . PHE A 1 88 ? 28.578 50.748 22.184 1.00 76.55 ? 88 PHE A CD1 1 ATOM 676 C CD2 . PHE A 1 88 ? 27.332 52.104 23.695 1.00 74.76 ? 88 PHE A CD2 1 ATOM 677 C CE1 . PHE A 1 88 ? 29.615 50.687 23.086 1.00 100.35 ? 88 PHE A CE1 1 ATOM 678 C CE2 . PHE A 1 88 ? 28.369 52.050 24.603 1.00 75.09 ? 88 PHE A CE2 1 ATOM 679 C CZ . PHE A 1 88 ? 29.513 51.342 24.298 1.00 97.05 ? 88 PHE A CZ 1 ATOM 680 N N . LYS A 1 89 ? 24.310 52.670 19.481 1.00 65.75 ? 89 LYS A N 1 ATOM 681 C CA . LYS A 1 89 ? 23.390 53.012 18.395 1.00 78.18 ? 89 LYS A CA 1 ATOM 682 C C . LYS A 1 89 ? 23.183 51.893 17.364 1.00 79.80 ? 89 LYS A C 1 ATOM 683 O O . LYS A 1 89 ? 22.247 51.943 16.568 1.00 89.55 ? 89 LYS A O 1 ATOM 684 C CB . LYS A 1 89 ? 23.895 54.290 17.700 1.00 70.37 ? 89 LYS A CB 1 ATOM 685 C CG . LYS A 1 89 ? 22.919 54.977 16.767 1.00 83.49 ? 89 LYS A CG 1 ATOM 686 C CD . LYS A 1 89 ? 23.036 56.494 16.869 1.00 86.34 ? 89 LYS A CD 1 ATOM 687 C CE . LYS A 1 89 ? 24.460 56.965 16.608 1.00 79.67 ? 89 LYS A CE 1 ATOM 688 N NZ . LYS A 1 89 ? 24.570 58.455 16.581 1.00 69.64 ? 89 LYS A NZ 1 ATOM 689 N N . SER A 1 90 ? 24.034 50.874 17.389 1.00 86.15 ? 90 SER A N 1 ATOM 690 C CA . SER A 1 90 ? 23.813 49.703 16.553 1.00 75.95 ? 90 SER A CA 1 ATOM 691 C C . SER A 1 90 ? 22.683 48.889 17.162 1.00 78.02 ? 90 SER A C 1 ATOM 692 O O . SER A 1 90 ? 22.647 48.693 18.378 1.00 79.68 ? 90 SER A O 1 ATOM 693 C CB . SER A 1 90 ? 25.084 48.860 16.429 1.00 83.79 ? 90 SER A CB 1 ATOM 694 O OG . SER A 1 90 ? 26.119 49.588 15.793 1.00 103.44 ? 90 SER A OG 1 ATOM 695 N N . HIS A 1 91 ? 21.762 48.431 16.317 1.00 76.62 ? 91 HIS A N 1 ATOM 696 C CA . HIS A 1 91 ? 20.581 47.689 16.761 1.00 77.45 ? 91 HIS A CA 1 ATOM 697 C C . HIS A 1 91 ? 19.794 48.474 17.808 1.00 81.05 ? 91 HIS A C 1 ATOM 698 O O . HIS A 1 91 ? 19.342 47.914 18.808 1.00 63.60 ? 91 HIS A O 1 ATOM 699 C CB . HIS A 1 91 ? 20.978 46.323 17.323 1.00 67.09 ? 91 HIS A CB 1 ATOM 700 C CG . HIS A 1 91 ? 21.845 45.522 16.404 1.00 76.90 ? 91 HIS A CG 1 ATOM 701 N ND1 . HIS A 1 91 ? 21.358 44.902 15.274 1.00 81.47 ? 91 HIS A ND1 1 ATOM 702 C CD2 . HIS A 1 91 ? 23.168 45.238 16.449 1.00 84.55 ? 91 HIS A CD2 1 ATOM 703 C CE1 . HIS A 1 91 ? 22.344 44.271 14.661 1.00 84.40 ? 91 HIS A CE1 1 ATOM 704 N NE2 . HIS A 1 91 ? 23.453 44.459 15.354 1.00 85.86 ? 91 HIS A NE2 1 ATOM 705 N N . GLN A 1 92 ? 19.638 49.772 17.566 1.00 77.44 ? 92 GLN A N 1 ATOM 706 C CA . GLN A 1 92 ? 18.986 50.666 18.516 1.00 78.95 ? 92 GLN A CA 1 ATOM 707 C C . GLN A 1 92 ? 17.473 50.681 18.354 1.00 60.82 ? 92 GLN A C 1 ATOM 708 O O . GLN A 1 92 ? 16.767 51.284 19.164 1.00 70.46 ? 92 GLN A O 1 ATOM 709 C CB . GLN A 1 92 ? 19.520 52.086 18.353 1.00 75.00 ? 92 GLN A CB 1 ATOM 710 C CG . GLN A 1 92 ? 19.162 52.692 17.014 1.00 88.95 ? 92 GLN A CG 1 ATOM 711 C CD . GLN A 1 92 ? 19.651 54.109 16.867 1.00 80.49 ? 92 GLN A CD 1 ATOM 712 O OE1 . GLN A 1 92 ? 19.975 54.770 17.854 1.00 73.72 ? 92 GLN A OE1 1 ATOM 713 N NE2 . GLN A 1 92 ? 19.715 54.589 15.629 1.00 68.68 ? 92 GLN A NE2 1 ATOM 714 N N . TRP A 1 93 ? 16.990 50.030 17.299 1.00 59.94 ? 93 TRP A N 1 ATOM 715 C CA . TRP A 1 93 ? 15.566 50.012 16.967 1.00 70.22 ? 93 TRP A CA 1 ATOM 716 C C . TRP A 1 93 ? 14.985 51.416 16.794 1.00 72.86 ? 93 TRP A C 1 ATOM 717 O O . TRP A 1 93 ? 13.937 51.733 17.356 1.00 78.62 ? 93 TRP A O 1 ATOM 718 C CB . TRP A 1 93 ? 14.771 49.256 18.037 1.00 65.96 ? 93 TRP A CB 1 ATOM 719 C CG . TRP A 1 93 ? 14.780 47.771 17.874 1.00 56.52 ? 93 TRP A CG 1 ATOM 720 C CD1 . TRP A 1 93 ? 15.870 46.952 17.872 1.00 62.11 ? 93 TRP A CD1 1 ATOM 721 C CD2 . TRP A 1 93 ? 13.639 46.922 17.703 1.00 56.56 ? 93 TRP A CD2 1 ATOM 722 N NE1 . TRP A 1 93 ? 15.481 45.644 17.704 1.00 69.79 ? 93 TRP A NE1 1 ATOM 723 C CE2 . TRP A 1 93 ? 14.116 45.599 17.598 1.00 65.74 ? 93 TRP A CE2 1 ATOM 724 C CE3 . TRP A 1 93 ? 12.262 47.151 17.625 1.00 68.48 ? 93 TRP A CE3 1 ATOM 725 C CZ2 . TRP A 1 93 ? 13.264 44.511 17.421 1.00 70.43 ? 93 TRP A CZ2 1 ATOM 726 C CZ3 . TRP A 1 93 ? 11.417 46.067 17.448 1.00 78.40 ? 93 TRP A CZ3 1 ATOM 727 C CH2 . TRP A 1 93 ? 11.922 44.765 17.349 1.00 75.99 ? 93 TRP A CH2 1 ATOM 728 N N . PHE A 1 94 ? 15.662 52.257 16.021 1.00 64.86 ? 94 PHE A N 1 ATOM 729 C CA . PHE A 1 94 ? 15.124 53.578 15.728 1.00 71.59 ? 94 PHE A CA 1 ATOM 730 C C . PHE A 1 94 ? 13.933 53.455 14.793 1.00 69.78 ? 94 PHE A C 1 ATOM 731 O O . PHE A 1 94 ? 14.021 52.826 13.739 1.00 84.52 ? 94 PHE A O 1 ATOM 732 C CB . PHE A 1 94 ? 16.188 54.492 15.115 1.00 71.88 ? 94 PHE A CB 1 ATOM 733 C CG . PHE A 1 94 ? 15.649 55.816 14.647 1.00 64.91 ? 94 PHE A CG 1 ATOM 734 C CD1 . PHE A 1 94 ? 15.306 56.801 15.558 1.00 61.35 ? 94 PHE A CD1 1 ATOM 735 C CD2 . PHE A 1 94 ? 15.480 56.073 13.295 1.00 67.03 ? 94 PHE A CD2 1 ATOM 736 C CE1 . PHE A 1 94 ? 14.806 58.021 15.128 1.00 59.45 ? 94 PHE A CE1 1 ATOM 737 C CE2 . PHE A 1 94 ? 14.980 57.289 12.861 1.00 69.86 ? 94 PHE A CE2 1 ATOM 738 C CZ . PHE A 1 94 ? 14.643 58.263 13.778 1.00 61.28 ? 94 PHE A CZ 1 ATOM 739 N N . GLY A 1 95 ? 12.818 54.059 15.185 1.00 68.65 ? 95 GLY A N 1 ATOM 740 C CA . GLY A 1 95 ? 11.609 53.995 14.389 1.00 96.15 ? 95 GLY A CA 1 ATOM 741 C C . GLY A 1 95 ? 10.598 53.016 14.946 1.00 70.93 ? 95 GLY A C 1 ATOM 742 O O . GLY A 1 95 ? 9.555 52.780 14.342 1.00 71.00 ? 95 GLY A O 1 ATOM 743 N N . ALA A 1 96 ? 10.912 52.442 16.103 1.00 54.67 ? 96 ALA A N 1 ATOM 744 C CA . ALA A 1 96 ? 9.984 51.566 16.805 1.00 53.59 ? 96 ALA A CA 1 ATOM 745 C C . ALA A 1 96 ? 8.783 52.363 17.298 1.00 60.01 ? 96 ALA A C 1 ATOM 746 O O . ALA A 1 96 ? 7.695 51.819 17.491 1.00 80.02 ? 96 ALA A O 1 ATOM 747 C CB . ALA A 1 96 ? 10.678 50.879 17.964 1.00 52.68 ? 96 ALA A CB 1 ATOM 748 N N . SER A 1 97 ? 8.996 53.657 17.503 1.00 53.13 ? 97 SER A N 1 ATOM 749 C CA . SER A 1 97 ? 7.933 54.561 17.905 1.00 62.11 ? 97 SER A CA 1 ATOM 750 C C . SER A 1 97 ? 7.941 55.787 17.012 1.00 63.31 ? 97 SER A C 1 ATOM 751 O O . SER A 1 97 ? 8.909 56.542 16.990 1.00 93.56 ? 97 SER A O 1 ATOM 752 C CB . SER A 1 97 ? 8.092 54.975 19.368 1.00 68.51 ? 97 SER A CB 1 ATOM 753 O OG . SER A 1 97 ? 8.048 53.848 20.224 1.00 118.81 ? 97 SER A OG 1 ATOM 754 N N . VAL A 1 98 ? 6.864 55.975 16.262 1.00 67.12 ? 98 VAL A N 1 ATOM 755 C CA . VAL A 1 98 ? 6.740 57.135 15.394 1.00 64.60 ? 98 VAL A CA 1 ATOM 756 C C . VAL A 1 98 ? 5.376 57.772 15.572 1.00 75.01 ? 98 VAL A C 1 ATOM 757 O O . VAL A 1 98 ? 4.348 57.114 15.415 1.00 101.18 ? 98 VAL A O 1 ATOM 758 C CB . VAL A 1 98 ? 6.932 56.773 13.909 1.00 73.02 ? 98 VAL A CB 1 ATOM 759 C CG1 . VAL A 1 98 ? 6.815 58.021 13.046 1.00 60.70 ? 98 VAL A CG1 1 ATOM 760 C CG2 . VAL A 1 98 ? 8.272 56.093 13.689 1.00 94.20 ? 98 VAL A CG2 1 ATOM 761 N N . ARG A 1 99 ? 5.366 59.054 15.910 1.00 63.40 ? 99 ARG A N 1 ATOM 762 C CA . ARG A 1 99 ? 4.116 59.789 15.990 1.00 76.01 ? 99 ARG A CA 1 ATOM 763 C C . ARG A 1 99 ? 4.317 61.212 15.501 1.00 65.86 ? 99 ARG A C 1 ATOM 764 O O . ARG A 1 99 ? 5.345 61.829 15.766 1.00 80.92 ? 99 ARG A O 1 ATOM 765 C CB . ARG A 1 99 ? 3.566 59.781 17.416 1.00 66.33 ? 99 ARG A CB 1 ATOM 766 C CG . ARG A 1 99 ? 2.077 60.084 17.488 1.00 81.75 ? 99 ARG A CG 1 ATOM 767 C CD . ARG A 1 99 ? 1.430 59.377 18.660 1.00 96.36 ? 99 ARG A CD 1 ATOM 768 N NE . ARG A 1 99 ? 1.882 57.993 18.775 1.00 107.07 ? 99 ARG A NE 1 ATOM 769 C CZ . ARG A 1 99 ? 1.343 56.969 18.120 1.00 109.77 ? 99 ARG A CZ 1 ATOM 770 N NH1 . ARG A 1 99 ? 1.825 55.746 18.292 1.00 115.81 ? 99 ARG A NH1 1 ATOM 771 N NH2 . ARG A 1 99 ? 0.326 57.166 17.294 1.00 103.83 ? 99 ARG A NH2 1 ATOM 772 N N . SER A 1 100 ? 3.330 61.721 14.774 1.00 71.31 ? 100 SER A N 1 ATOM 773 C CA . SER A 1 100 ? 3.411 63.056 14.206 1.00 65.70 ? 100 SER A CA 1 ATOM 774 C C . SER A 1 100 ? 2.200 63.891 14.575 1.00 73.47 ? 100 SER A C 1 ATOM 775 O O . SER A 1 100 ? 1.072 63.399 14.588 1.00 109.85 ? 100 SER A O 1 ATOM 776 C CB . SER A 1 100 ? 3.544 62.980 12.685 1.00 85.61 ? 100 SER A CB 1 ATOM 777 O OG . SER A 1 100 ? 3.221 64.220 12.080 1.00 102.86 ? 100 SER A OG 1 ATOM 778 N N . LYS A 1 101 ? 2.444 65.157 14.887 1.00 68.41 ? 101 LYS A N 1 ATOM 779 C CA . LYS A 1 101 ? 1.368 66.121 15.048 1.00 80.71 ? 101 LYS A CA 1 ATOM 780 C C . LYS A 1 101 ? 1.639 67.322 14.154 1.00 73.87 ? 101 LYS A C 1 ATOM 781 O O . LYS A 1 101 ? 2.642 68.019 14.324 1.00 86.61 ? 101 LYS A O 1 ATOM 782 C CB . LYS A 1 101 ? 1.223 66.558 16.506 1.00 95.86 ? 101 LYS A CB 1 ATOM 783 C CG . LYS A 1 101 ? 0.136 67.600 16.714 1.00 104.14 ? 101 LYS A CG 1 ATOM 784 C CD . LYS A 1 101 ? 0.014 68.011 18.170 1.00 88.59 ? 101 LYS A CD 1 ATOM 785 C CE . LYS A 1 101 ? -0.914 69.207 18.318 1.00 115.31 ? 101 LYS A CE 1 ATOM 786 N NZ . LYS A 1 101 ? -0.415 70.395 17.562 1.00 114.05 ? 101 LYS A NZ 1 ATOM 787 N N . GLN A 1 102 ? 0.744 67.543 13.198 1.00 75.90 ? 102 GLN A N 1 ATOM 788 C CA . GLN A 1 102 ? 0.887 68.619 12.224 1.00 95.40 ? 102 GLN A CA 1 ATOM 789 C C . GLN A 1 102 ? 2.229 68.540 11.499 1.00 90.38 ? 102 GLN A C 1 ATOM 790 O O . GLN A 1 102 ? 2.519 67.558 10.819 1.00 127.50 ? 102 GLN A O 1 ATOM 791 C CB . GLN A 1 102 ? 0.719 69.984 12.896 1.00 83.39 ? 102 GLN A CB 1 ATOM 792 C CG . GLN A 1 102 ? -0.697 70.259 13.380 1.00 95.36 ? 102 GLN A CG 1 ATOM 793 C CD . GLN A 1 102 ? -0.877 71.673 13.898 1.00 130.71 ? 102 GLN A CD 1 ATOM 794 O OE1 . GLN A 1 102 ? 0.046 72.265 14.460 1.00 149.63 ? 102 GLN A OE1 1 ATOM 795 N NE2 . GLN A 1 102 ? -2.069 72.226 13.704 1.00 123.04 ? 102 GLN A NE2 1 ATOM 796 N N . ASP A 1 103 ? 3.046 69.572 11.655 1.00 80.26 ? 103 ASP A N 1 ATOM 797 C CA . ASP A 1 103 ? 4.279 69.686 10.886 1.00 99.31 ? 103 ASP A CA 1 ATOM 798 C C . ASP A 1 103 ? 5.486 69.081 11.601 1.00 99.28 ? 103 ASP A C 1 ATOM 799 O O . ASP A 1 103 ? 6.613 69.172 11.111 1.00 78.46 ? 103 ASP A O 1 ATOM 800 C CB . ASP A 1 103 ? 4.552 71.154 10.554 1.00 84.34 ? 103 ASP A CB 1 ATOM 801 C CG . ASP A 1 103 ? 4.937 71.357 9.106 1.00 99.21 ? 103 ASP A CG 1 ATOM 802 O OD1 . ASP A 1 103 ? 5.811 70.608 8.619 1.00 97.59 ? 103 ASP A OD1 1 ATOM 803 O OD2 . ASP A 1 103 ? 4.354 72.251 8.451 1.00 95.09 ? 103 ASP A OD2 1 ATOM 804 N N . LYS A 1 104 ? 5.248 68.466 12.756 1.00 78.19 ? 104 LYS A N 1 ATOM 805 C CA . LYS A 1 104 ? 6.338 67.943 13.575 1.00 72.66 ? 104 LYS A CA 1 ATOM 806 C C . LYS A 1 104 ? 6.307 66.421 13.683 1.00 92.88 ? 104 LYS A C 1 ATOM 807 O O . LYS A 1 104 ? 5.255 65.824 13.912 1.00 101.85 ? 104 LYS A O 1 ATOM 808 C CB . LYS A 1 104 ? 6.294 68.572 14.968 1.00 72.09 ? 104 LYS A CB 1 ATOM 809 C CG . LYS A 1 104 ? 6.396 70.089 14.938 1.00 117.90 ? 104 LYS A CG 1 ATOM 810 C CD . LYS A 1 104 ? 6.190 70.710 16.308 1.00 113.72 ? 104 LYS A CD 1 ATOM 811 C CE . LYS A 1 104 ? 6.166 72.230 16.212 1.00 122.08 ? 104 LYS A CE 1 ATOM 812 N NZ . LYS A 1 104 ? 5.935 72.886 17.528 1.00 152.45 ? 104 LYS A NZ 1 ATOM 813 N N . ILE A 1 105 ? 7.474 65.805 13.520 1.00 86.60 ? 105 ILE A N 1 ATOM 814 C CA . ILE A 1 105 ? 7.604 64.352 13.563 1.00 76.50 ? 105 ILE A CA 1 ATOM 815 C C . ILE A 1 105 ? 8.520 63.903 14.699 1.00 72.02 ? 105 ILE A C 1 ATOM 816 O O . ILE A 1 105 ? 9.637 64.395 14.836 1.00 95.39 ? 105 ILE A O 1 ATOM 817 C CB . ILE A 1 105 ? 8.155 63.799 12.235 1.00 67.70 ? 105 ILE A CB 1 ATOM 818 C CG1 . ILE A 1 105 ? 7.266 64.224 11.067 1.00 70.30 ? 105 ILE A CG1 1 ATOM 819 C CG2 . ILE A 1 105 ? 8.273 62.284 12.291 1.00 65.73 ? 105 ILE A CG2 1 ATOM 820 C CD1 . ILE A 1 105 ? 7.778 63.771 9.716 1.00 71.96 ? 105 ILE A CD1 1 ATOM 821 N N . LEU A 1 106 ? 8.042 62.961 15.506 1.00 74.73 ? 106 LEU A N 1 ATOM 822 C CA . LEU A 1 106 ? 8.841 62.400 16.590 1.00 71.38 ? 106 LEU A CA 1 ATOM 823 C C . LEU A 1 106 ? 9.102 60.909 16.389 1.00 72.56 ? 106 LEU A C 1 ATOM 824 O O . LEU A 1 106 ? 8.169 60.124 16.226 1.00 81.60 ? 106 LEU A O 1 ATOM 825 C CB . LEU A 1 106 ? 8.151 62.624 17.934 1.00 74.69 ? 106 LEU A CB 1 ATOM 826 C CG . LEU A 1 106 ? 8.896 62.057 19.141 1.00 70.94 ? 106 LEU A CG 1 ATOM 827 C CD1 . LEU A 1 106 ? 10.310 62.615 19.194 1.00 76.43 ? 106 LEU A CD1 1 ATOM 828 C CD2 . LEU A 1 106 ? 8.150 62.370 20.425 1.00 70.36 ? 106 LEU A CD2 1 ATOM 829 N N . ALA A 1 107 ? 10.375 60.525 16.402 1.00 72.24 ? 107 ALA A N 1 ATOM 830 C CA . ALA A 1 107 ? 10.760 59.124 16.252 1.00 62.52 ? 107 ALA A CA 1 ATOM 831 C C . ALA A 1 107 ? 11.796 58.741 17.305 1.00 73.40 ? 107 ALA A C 1 ATOM 832 O O . ALA A 1 107 ? 12.672 59.538 17.638 1.00 73.11 ? 107 ALA A O 1 ATOM 833 C CB . ALA A 1 107 ? 11.294 58.866 14.855 1.00 59.90 ? 107 ALA A CB 1 ATOM 834 N N . CYS A 1 108 ? 11.700 57.518 17.820 1.00 71.50 ? 108 CYS A N 1 ATOM 835 C CA . CYS A 1 108 ? 12.527 57.109 18.951 1.00 78.10 ? 108 CYS A CA 1 ATOM 836 C C . CYS A 1 108 ? 13.253 55.775 18.746 1.00 85.68 ? 108 CYS A C 1 ATOM 837 O O . CYS A 1 108 ? 12.821 54.925 17.966 1.00 68.09 ? 108 CYS A O 1 ATOM 838 C CB . CYS A 1 108 ? 11.667 57.033 20.211 1.00 66.31 ? 108 CYS A CB 1 ATOM 839 S SG . CYS A 1 108 ? 10.731 58.537 20.552 1.00 84.91 ? 108 CYS A SG 1 ATOM 840 N N . ALA A 1 109 ? 14.362 55.609 19.463 1.00 73.29 ? 109 ALA A N 1 ATOM 841 C CA . ALA A 1 109 ? 15.161 54.389 19.416 1.00 68.13 ? 109 ALA A CA 1 ATOM 842 C C . ALA A 1 109 ? 15.319 53.814 20.819 1.00 62.09 ? 109 ALA A C 1 ATOM 843 O O . ALA A 1 109 ? 16.284 54.125 21.514 1.00 80.55 ? 109 ALA A O 1 ATOM 844 C CB . ALA A 1 109 ? 16.526 54.667 18.800 1.00 55.40 ? 109 ALA A CB 1 ATOM 845 N N . PRO A 1 110 ? 14.367 52.969 21.239 1.00 52.16 ? 110 PRO A N 1 ATOM 846 C CA . PRO A 1 110 ? 14.301 52.484 22.623 1.00 51.54 ? 110 PRO A CA 1 ATOM 847 C C . PRO A 1 110 ? 15.441 51.543 22.997 1.00 58.19 ? 110 PRO A C 1 ATOM 848 O O . PRO A 1 110 ? 15.634 51.282 24.183 1.00 67.27 ? 110 PRO A O 1 ATOM 849 C CB . PRO A 1 110 ? 12.955 51.749 22.678 1.00 50.80 ? 110 PRO A CB 1 ATOM 850 C CG . PRO A 1 110 ? 12.206 52.191 21.453 1.00 62.92 ? 110 PRO A CG 1 ATOM 851 C CD . PRO A 1 110 ? 13.257 52.450 20.426 1.00 51.96 ? 110 PRO A CD 1 ATOM 852 N N . LEU A 1 111 ? 16.152 51.007 22.011 1.00 52.95 ? 111 LEU A N 1 ATOM 853 C CA . LEU A 1 111 ? 17.287 50.131 22.292 1.00 57.87 ? 111 LEU A CA 1 ATOM 854 C C . LEU A 1 111 ? 18.637 50.847 22.215 1.00 70.33 ? 111 LEU A C 1 ATOM 855 O O . LEU A 1 111 ? 19.689 50.212 22.335 1.00 60.88 ? 111 LEU A O 1 ATOM 856 C CB . LEU A 1 111 ? 17.270 48.921 21.358 1.00 83.25 ? 111 LEU A CB 1 ATOM 857 C CG . LEU A 1 111 ? 16.158 47.915 21.677 1.00 75.98 ? 111 LEU A CG 1 ATOM 858 C CD1 . LEU A 1 111 ? 16.501 46.541 21.131 1.00 69.52 ? 111 LEU A CD1 1 ATOM 859 C CD2 . LEU A 1 111 ? 15.895 47.845 23.176 1.00 53.21 ? 111 LEU A CD2 1 ATOM 860 N N . TYR A 1 112 ? 18.600 52.159 21.995 1.00 66.11 ? 112 TYR A N 1 ATOM 861 C CA . TYR A 1 112 ? 19.801 52.994 22.008 1.00 58.04 ? 112 TYR A CA 1 ATOM 862 C C . TYR A 1 112 ? 20.580 52.819 23.308 1.00 60.00 ? 112 TYR A C 1 ATOM 863 O O . TYR A 1 112 ? 19.995 52.827 24.391 1.00 65.63 ? 112 TYR A O 1 ATOM 864 C CB . TYR A 1 112 ? 19.416 54.464 21.806 1.00 77.58 ? 112 TYR A CB 1 ATOM 865 C CG . TYR A 1 112 ? 20.507 55.474 22.101 1.00 70.67 ? 112 TYR A CG 1 ATOM 866 C CD1 . TYR A 1 112 ? 21.519 55.724 21.181 1.00 61.28 ? 112 TYR A CD1 1 ATOM 867 C CD2 . TYR A 1 112 ? 20.507 56.200 23.285 1.00 69.32 ? 112 TYR A CD2 1 ATOM 868 C CE1 . TYR A 1 112 ? 22.512 56.656 21.442 1.00 63.33 ? 112 TYR A CE1 1 ATOM 869 C CE2 . TYR A 1 112 ? 21.494 57.132 23.553 1.00 90.14 ? 112 TYR A CE2 1 ATOM 870 C CZ . TYR A 1 112 ? 22.493 57.357 22.628 1.00 73.22 ? 112 TYR A CZ 1 ATOM 871 O OH . TYR A 1 112 ? 23.476 58.285 22.892 1.00 61.23 ? 112 TYR A OH 1 ATOM 872 N N . HIS A 1 113 ? 21.896 52.656 23.199 1.00 68.14 ? 113 HIS A N 1 ATOM 873 C CA . HIS A 1 113 ? 22.739 52.423 24.371 1.00 74.44 ? 113 HIS A CA 1 ATOM 874 C C . HIS A 1 113 ? 23.688 53.587 24.659 1.00 83.41 ? 113 HIS A C 1 ATOM 875 O O . HIS A 1 113 ? 24.077 54.327 23.755 1.00 87.10 ? 113 HIS A O 1 ATOM 876 C CB . HIS A 1 113 ? 23.537 51.128 24.205 1.00 94.20 ? 113 HIS A CB 1 ATOM 877 C CG . HIS A 1 113 ? 22.728 49.888 24.430 1.00 96.07 ? 113 HIS A CG 1 ATOM 878 N ND1 . HIS A 1 113 ? 22.153 49.176 23.400 1.00 89.08 ? 113 HIS A ND1 1 ATOM 879 C CD2 . HIS A 1 113 ? 22.391 49.239 25.570 1.00 81.68 ? 113 HIS A CD2 1 ATOM 880 C CE1 . HIS A 1 113 ? 21.501 48.139 23.895 1.00 96.05 ? 113 HIS A CE1 1 ATOM 881 N NE2 . HIS A 1 113 ? 21.629 48.155 25.210 1.00 71.56 ? 113 HIS A NE2 1 ATOM 882 N N . TRP A 1 114 ? 24.053 53.736 25.929 1.00 76.11 ? 114 TRP A N 1 ATOM 883 C CA . TRP A 1 114 ? 24.850 54.869 26.390 1.00 65.26 ? 114 TRP A CA 1 ATOM 884 C C . TRP A 1 114 ? 26.078 54.418 27.182 1.00 65.34 ? 114 TRP A C 1 ATOM 885 O O . TRP A 1 114 ? 26.067 53.357 27.800 1.00 95.57 ? 114 TRP A O 1 ATOM 886 C CB . TRP A 1 114 ? 23.984 55.789 27.250 1.00 80.83 ? 114 TRP A CB 1 ATOM 887 C CG . TRP A 1 114 ? 24.589 57.122 27.533 1.00 71.70 ? 114 TRP A CG 1 ATOM 888 C CD1 . TRP A 1 114 ? 25.467 57.811 26.748 1.00 100.80 ? 114 TRP A CD1 1 ATOM 889 C CD2 . TRP A 1 114 ? 24.360 57.934 28.687 1.00 69.09 ? 114 TRP A CD2 1 ATOM 890 N NE1 . TRP A 1 114 ? 25.798 59.005 27.343 1.00 103.00 ? 114 TRP A NE1 1 ATOM 891 C CE2 . TRP A 1 114 ? 25.131 59.104 28.535 1.00 85.46 ? 114 TRP A CE2 1 ATOM 892 C CE3 . TRP A 1 114 ? 23.575 57.786 29.835 1.00 85.72 ? 114 TRP A CE3 1 ATOM 893 C CZ2 . TRP A 1 114 ? 25.143 60.120 29.487 1.00 75.80 ? 114 TRP A CZ2 1 ATOM 894 C CZ3 . TRP A 1 114 ? 23.587 58.796 30.779 1.00 109.83 ? 114 TRP A CZ3 1 ATOM 895 C CH2 . TRP A 1 114 ? 24.366 59.948 30.599 1.00 94.81 ? 114 TRP A CH2 1 ATOM 896 N N . ARG A 1 115 ? 27.131 55.230 27.165 1.00 65.97 ? 115 ARG A N 1 ATOM 897 C CA . ARG A 1 115 ? 28.363 54.914 27.884 1.00 68.72 ? 115 ARG A CA 1 ATOM 898 C C . ARG A 1 115 ? 28.351 55.491 29.303 1.00 70.64 ? 115 ARG A C 1 ATOM 899 O O . ARG A 1 115 ? 29.204 55.154 30.123 1.00 88.98 ? 115 ARG A O 1 ATOM 900 C CB . ARG A 1 115 ? 29.573 55.437 27.099 1.00 80.29 ? 115 ARG A CB 1 ATOM 901 C CG . ARG A 1 115 ? 30.922 54.858 27.497 1.00 74.24 ? 115 ARG A CG 1 ATOM 902 C CD . ARG A 1 115 ? 31.708 55.836 28.351 1.00 75.36 ? 115 ARG A CD 1 ATOM 903 N NE . ARG A 1 115 ? 33.074 55.383 28.583 1.00 82.71 ? 115 ARG A NE 1 ATOM 904 C CZ . ARG A 1 115 ? 33.802 55.722 29.641 1.00 86.84 ? 115 ARG A CZ 1 ATOM 905 N NH1 . ARG A 1 115 ? 33.291 56.512 30.574 1.00 79.04 ? 115 ARG A NH1 1 ATOM 906 N NH2 . ARG A 1 115 ? 35.039 55.264 29.770 1.00 102.53 ? 115 ARG A NH2 1 ATOM 907 N N . THR A 1 116 ? 27.365 56.349 29.573 1.00 69.47 ? 116 THR A N 1 ATOM 908 C CA . THR A 1 116 ? 27.143 57.014 30.871 1.00 78.12 ? 116 THR A CA 1 ATOM 909 C C . THR A 1 116 ? 28.173 58.077 31.268 1.00 100.99 ? 116 THR A C 1 ATOM 910 O O . THR A 1 116 ? 27.959 58.796 32.247 1.00 124.08 ? 116 THR A O 1 ATOM 911 C CB . THR A 1 116 ? 27.079 56.012 32.040 1.00 79.00 ? 116 THR A CB 1 ATOM 912 O OG1 . THR A 1 116 ? 28.391 55.497 32.299 1.00 89.07 ? 116 THR A OG1 1 ATOM 913 C CG2 . THR A 1 116 ? 26.123 54.877 31.727 1.00 115.81 ? 116 THR A CG2 1 ATOM 914 N N . GLU A 1 117 ? 29.290 58.157 30.546 1.00 73.36 ? 117 GLU A N 1 ATOM 915 C CA . GLU A 1 117 ? 30.263 59.242 30.724 1.00 86.85 ? 117 GLU A CA 1 ATOM 916 C C . GLU A 1 117 ? 30.983 59.218 32.079 1.00 91.80 ? 117 GLU A C 1 ATOM 917 O O . GLU A 1 117 ? 31.870 60.033 32.331 1.00 77.52 ? 117 GLU A O 1 ATOM 918 C CB . GLU A 1 117 ? 29.579 60.601 30.527 1.00 85.07 ? 117 GLU A CB 1 ATOM 919 C CG . GLU A 1 117 ? 30.496 61.715 30.059 1.00 76.46 ? 117 GLU A CG 1 ATOM 920 C CD . GLU A 1 117 ? 29.727 62.955 29.657 1.00 85.51 ? 117 GLU A CD 1 ATOM 921 O OE1 . GLU A 1 117 ? 30.312 63.838 28.992 1.00 112.83 ? 117 GLU A OE1 1 ATOM 922 O OE2 . GLU A 1 117 ? 28.533 63.045 30.009 1.00 73.13 ? 117 GLU A OE2 1 ATOM 923 N N . MET A 1 118 ? 30.599 58.295 32.954 1.00 110.51 ? 118 MET A N 1 ATOM 924 C CA . MET A 1 118 ? 31.275 58.144 34.238 1.00 99.80 ? 118 MET A CA 1 ATOM 925 C C . MET A 1 118 ? 32.157 56.904 34.218 1.00 97.54 ? 118 MET A C 1 ATOM 926 O O . MET A 1 118 ? 33.381 56.998 34.114 1.00 92.72 ? 118 MET A O 1 ATOM 927 C CB . MET A 1 118 ? 30.256 58.059 35.372 1.00 83.53 ? 118 MET A CB 1 ATOM 928 C CG . MET A 1 118 ? 29.267 59.211 35.389 1.00 87.25 ? 118 MET A CG 1 ATOM 929 S SD . MET A 1 118 ? 28.097 59.093 36.750 1.00 98.02 ? 118 MET A SD 1 ATOM 930 C CE . MET A 1 118 ? 29.228 58.868 38.124 1.00 134.68 ? 118 MET A CE 1 ATOM 931 N N . LYS A 1 119 ? 31.525 55.740 34.302 1.00 96.29 ? 119 LYS A N 1 ATOM 932 C CA . LYS A 1 119 ? 32.227 54.478 34.126 1.00 102.43 ? 119 LYS A CA 1 ATOM 933 C C . LYS A 1 119 ? 31.975 53.972 32.713 1.00 91.07 ? 119 LYS A C 1 ATOM 934 O O . LYS A 1 119 ? 31.255 54.611 31.946 1.00 92.49 ? 119 LYS A O 1 ATOM 935 C CB . LYS A 1 119 ? 31.773 53.451 35.164 1.00 96.11 ? 119 LYS A CB 1 ATOM 936 C CG . LYS A 1 119 ? 30.265 53.276 35.249 1.00 95.56 ? 119 LYS A CG 1 ATOM 937 C CD . LYS A 1 119 ? 29.882 52.380 36.417 1.00 107.38 ? 119 LYS A CD 1 ATOM 938 C CE . LYS A 1 119 ? 28.375 52.222 36.526 1.00 109.26 ? 119 LYS A CE 1 ATOM 939 N NZ . LYS A 1 119 ? 27.994 51.350 37.673 1.00 115.19 ? 119 LYS A NZ 1 ATOM 940 N N . GLN A 1 120 ? 32.565 52.834 32.362 1.00 84.37 ? 120 GLN A N 1 ATOM 941 C CA . GLN A 1 120 ? 32.344 52.272 31.037 1.00 85.99 ? 120 GLN A CA 1 ATOM 942 C C . GLN A 1 120 ? 31.206 51.261 31.086 1.00 91.52 ? 120 GLN A C 1 ATOM 943 O O . GLN A 1 120 ? 31.326 50.196 31.691 1.00 97.87 ? 120 GLN A O 1 ATOM 944 C CB . GLN A 1 120 ? 33.619 51.626 30.493 1.00 88.10 ? 120 GLN A CB 1 ATOM 945 C CG . GLN A 1 120 ? 33.490 51.147 29.055 1.00 106.14 ? 120 GLN A CG 1 ATOM 946 C CD . GLN A 1 120 ? 34.827 50.813 28.424 1.00 135.62 ? 120 GLN A CD 1 ATOM 947 O OE1 . GLN A 1 120 ? 35.834 51.471 28.690 1.00 125.81 ? 120 GLN A OE1 1 ATOM 948 N NE2 . GLN A 1 120 ? 34.845 49.783 27.583 1.00 140.78 ? 120 GLN A NE2 1 ATOM 949 N N . GLU A 1 121 ? 30.099 51.611 30.441 1.00 85.72 ? 121 GLU A N 1 ATOM 950 C CA . GLU A 1 121 ? 28.895 50.794 30.459 1.00 90.91 ? 121 GLU A CA 1 ATOM 951 C C . GLU A 1 121 ? 28.160 50.902 29.132 1.00 75.37 ? 121 GLU A C 1 ATOM 952 O O . GLU A 1 121 ? 28.430 51.803 28.342 1.00 72.77 ? 121 GLU A O 1 ATOM 953 C CB . GLU A 1 121 ? 27.971 51.225 31.603 1.00 103.00 ? 121 GLU A CB 1 ATOM 954 C CG . GLU A 1 121 ? 28.404 50.766 32.987 1.00 109.63 ? 121 GLU A CG 1 ATOM 955 C CD . GLU A 1 121 ? 28.044 49.316 33.262 1.00 128.16 ? 121 GLU A CD 1 ATOM 956 O OE1 . GLU A 1 121 ? 27.283 48.726 32.465 1.00 114.44 ? 121 GLU A OE1 1 ATOM 957 O OE2 . GLU A 1 121 ? 28.519 48.765 34.277 1.00 129.33 ? 121 GLU A OE2 1 ATOM 958 N N . ARG A 1 122 ? 27.256 49.965 28.871 1.00 70.35 ? 122 ARG A N 1 ATOM 959 C CA . ARG A 1 122 ? 26.290 50.139 27.796 1.00 67.95 ? 122 ARG A CA 1 ATOM 960 C C . ARG A 1 122 ? 24.892 50.054 28.396 1.00 68.71 ? 122 ARG A C 1 ATOM 961 O O . ARG A 1 122 ? 24.428 48.976 28.762 1.00 106.06 ? 122 ARG A O 1 ATOM 962 C CB . ARG A 1 122 ? 26.496 49.086 26.702 1.00 69.42 ? 122 ARG A CB 1 ATOM 963 C CG . ARG A 1 122 ? 27.932 49.020 26.190 1.00 72.82 ? 122 ARG A CG 1 ATOM 964 C CD . ARG A 1 122 ? 28.107 48.078 25.006 1.00 74.69 ? 122 ARG A CD 1 ATOM 965 N NE . ARG A 1 122 ? 27.003 48.162 24.056 1.00 95.99 ? 122 ARG A NE 1 ATOM 966 C CZ . ARG A 1 122 ? 27.065 47.730 22.801 1.00 99.57 ? 122 ARG A CZ 1 ATOM 967 N NH1 . ARG A 1 122 ? 28.189 47.199 22.338 1.00 95.29 ? 122 ARG A NH1 1 ATOM 968 N NH2 . ARG A 1 122 ? 26.007 47.840 22.006 1.00 84.35 ? 122 ARG A NH2 1 ATOM 969 N N . GLU A 1 123 ? 24.217 51.195 28.483 1.00 77.10 ? 123 GLU A N 1 ATOM 970 C CA . GLU A 1 123 ? 22.933 51.269 29.172 1.00 77.74 ? 123 GLU A CA 1 ATOM 971 C C . GLU A 1 123 ? 21.802 51.687 28.240 1.00 75.84 ? 123 GLU A C 1 ATOM 972 O O . GLU A 1 123 ? 21.820 52.789 27.694 1.00 57.94 ? 123 GLU A O 1 ATOM 973 C CB . GLU A 1 123 ? 23.025 52.226 30.363 1.00 65.19 ? 123 GLU A CB 1 ATOM 974 C CG . GLU A 1 123 ? 24.011 51.771 31.434 1.00 68.95 ? 123 GLU A CG 1 ATOM 975 C CD . GLU A 1 123 ? 23.909 52.578 32.716 1.00 77.26 ? 123 GLU A CD 1 ATOM 976 O OE1 . GLU A 1 123 ? 24.708 52.332 33.645 1.00 92.83 ? 123 GLU A OE1 1 ATOM 977 O OE2 . GLU A 1 123 ? 23.032 53.461 32.796 1.00 83.92 ? 123 GLU A OE2 1 ATOM 978 N N . PRO A 1 124 ? 20.807 50.806 28.064 1.00 71.89 ? 124 PRO A N 1 ATOM 979 C CA . PRO A 1 124 ? 19.680 51.050 27.158 1.00 72.53 ? 124 PRO A CA 1 ATOM 980 C C . PRO A 1 124 ? 18.795 52.189 27.652 1.00 79.92 ? 124 PRO A C 1 ATOM 981 O O . PRO A 1 124 ? 17.692 51.974 28.161 1.00 61.96 ? 124 PRO A O 1 ATOM 982 C CB . PRO A 1 124 ? 18.928 49.719 27.171 1.00 56.87 ? 124 PRO A CB 1 ATOM 983 C CG . PRO A 1 124 ? 19.252 49.133 28.495 1.00 59.68 ? 124 PRO A CG 1 ATOM 984 C CD . PRO A 1 124 ? 20.670 49.527 28.777 1.00 63.77 ? 124 PRO A CD 1 ATOM 985 N N . VAL A 1 125 ? 19.309 53.404 27.501 1.00 80.36 ? 125 VAL A N 1 ATOM 986 C CA . VAL A 1 125 ? 18.614 54.614 27.908 1.00 60.08 ? 125 VAL A CA 1 ATOM 987 C C . VAL A 1 125 ? 17.498 54.967 26.931 1.00 57.99 ? 125 VAL A C 1 ATOM 988 O O . VAL A 1 125 ? 16.387 55.318 27.332 1.00 53.37 ? 125 VAL A O 1 ATOM 989 C CB . VAL A 1 125 ? 19.594 55.792 28.010 1.00 58.46 ? 125 VAL A CB 1 ATOM 990 C CG1 . VAL A 1 125 ? 18.859 57.102 27.899 1.00 101.34 ? 125 VAL A CG1 1 ATOM 991 C CG2 . VAL A 1 125 ? 20.386 55.713 29.305 1.00 60.70 ? 125 VAL A CG2 1 ATOM 992 N N . GLY A 1 126 ? 17.808 54.868 25.644 1.00 72.07 ? 126 GLY A N 1 ATOM 993 C CA . GLY A 1 126 ? 16.869 55.230 24.603 1.00 69.58 ? 126 GLY A CA 1 ATOM 994 C C . GLY A 1 126 ? 16.981 56.702 24.262 1.00 83.79 ? 126 GLY A C 1 ATOM 995 O O . GLY A 1 126 ? 17.321 57.525 25.112 1.00 72.33 ? 126 GLY A O 1 ATOM 996 N N . THR A 1 127 ? 16.688 57.036 23.011 1.00 63.69 ? 127 THR A N 1 ATOM 997 C CA . THR A 1 127 ? 16.746 58.417 22.566 1.00 55.17 ? 127 THR A CA 1 ATOM 998 C C . THR A 1 127 ? 15.698 58.673 21.494 1.00 67.07 ? 127 THR A C 1 ATOM 999 O O . THR A 1 127 ? 15.202 57.744 20.860 1.00 73.27 ? 127 THR A O 1 ATOM 1000 C CB . THR A 1 127 ? 18.140 58.773 22.013 1.00 80.30 ? 127 THR A CB 1 ATOM 1001 O OG1 . THR A 1 127 ? 18.185 60.165 21.670 1.00 88.80 ? 127 THR A OG1 1 ATOM 1002 C CG2 . THR A 1 127 ? 18.452 57.937 20.781 1.00 61.70 ? 127 THR A CG2 1 ATOM 1003 N N . CYS A 1 128 ? 15.361 59.940 21.295 1.00 74.58 ? 128 CYS A N 1 ATOM 1004 C CA . CYS A 1 128 ? 14.419 60.312 20.254 1.00 67.29 ? 128 CYS A CA 1 ATOM 1005 C C . CYS A 1 128 ? 14.970 61.454 19.415 1.00 89.08 ? 128 CYS A C 1 ATOM 1006 O O . CYS A 1 128 ? 15.840 62.206 19.860 1.00 76.94 ? 128 CYS A O 1 ATOM 1007 C CB . CYS A 1 128 ? 13.073 60.712 20.858 1.00 55.93 ? 128 CYS A CB 1 ATOM 1008 S SG . CYS A 1 128 ? 12.195 59.377 21.683 1.00 106.44 ? 128 CYS A SG 1 ATOM 1009 N N . PHE A 1 129 ? 14.461 61.570 18.194 1.00 75.10 ? 129 PHE A N 1 ATOM 1010 C CA . PHE A 1 129 ? 14.791 62.691 17.331 1.00 61.04 ? 129 PHE A CA 1 ATOM 1011 C C . PHE A 1 129 ? 13.516 63.402 16.904 1.00 67.20 ? 129 PHE A C 1 ATOM 1012 O O . PHE A 1 129 ? 12.658 62.819 16.243 1.00 89.09 ? 129 PHE A O 1 ATOM 1013 C CB . PHE A 1 129 ? 15.580 62.225 16.108 1.00 78.30 ? 129 PHE A CB 1 ATOM 1014 C CG . PHE A 1 129 ? 16.973 61.765 16.424 1.00 77.33 ? 129 PHE A CG 1 ATOM 1015 C CD1 . PHE A 1 129 ? 17.233 60.434 16.696 1.00 67.60 ? 129 PHE A CD1 1 ATOM 1016 C CD2 . PHE A 1 129 ? 18.023 62.665 16.445 1.00 63.69 ? 129 PHE A CD2 1 ATOM 1017 C CE1 . PHE A 1 129 ? 18.518 60.013 16.985 1.00 96.81 ? 129 PHE A CE1 1 ATOM 1018 C CE2 . PHE A 1 129 ? 19.307 62.248 16.733 1.00 63.95 ? 129 PHE A CE2 1 ATOM 1019 C CZ . PHE A 1 129 ? 19.555 60.925 17.003 1.00 82.94 ? 129 PHE A CZ 1 ATOM 1020 N N . LEU A 1 130 ? 13.390 64.662 17.301 1.00 78.08 ? 130 LEU A N 1 ATOM 1021 C CA . LEU A 1 130 ? 12.238 65.470 16.928 1.00 79.86 ? 130 LEU A CA 1 ATOM 1022 C C . LEU A 1 130 ? 12.581 66.351 15.737 1.00 78.15 ? 130 LEU A C 1 ATOM 1023 O O . LEU A 1 130 ? 13.456 67.213 15.829 1.00 85.45 ? 130 LEU A O 1 ATOM 1024 C CB . LEU A 1 130 ? 11.775 66.324 18.108 1.00 71.66 ? 130 LEU A CB 1 ATOM 1025 C CG . LEU A 1 130 ? 10.630 67.301 17.843 1.00 66.07 ? 130 LEU A CG 1 ATOM 1026 C CD1 . LEU A 1 130 ? 9.394 66.564 17.367 1.00 88.71 ? 130 LEU A CD1 1 ATOM 1027 C CD2 . LEU A 1 130 ? 10.324 68.111 19.093 1.00 84.34 ? 130 LEU A CD2 1 ATOM 1028 N N . GLN A 1 131 ? 11.899 66.128 14.619 1.00 67.62 ? 131 GLN A N 1 ATOM 1029 C CA . GLN A 1 131 ? 12.160 66.903 13.414 1.00 85.73 ? 131 GLN A CA 1 ATOM 1030 C C . GLN A 1 131 ? 10.997 67.820 13.050 1.00 87.34 ? 131 GLN A C 1 ATOM 1031 O O . GLN A 1 131 ? 9.850 67.384 12.955 1.00 80.75 ? 131 GLN A O 1 ATOM 1032 C CB . GLN A 1 131 ? 12.476 65.982 12.234 1.00 70.81 ? 131 GLN A CB 1 ATOM 1033 C CG . GLN A 1 131 ? 12.524 66.715 10.900 1.00 99.89 ? 131 GLN A CG 1 ATOM 1034 C CD . GLN A 1 131 ? 13.272 65.950 9.829 1.00 99.57 ? 131 GLN A CD 1 ATOM 1035 O OE1 . GLN A 1 131 ? 14.358 65.423 10.071 1.00 100.02 ? 131 GLN A OE1 1 ATOM 1036 N NE2 . GLN A 1 131 ? 12.693 65.886 8.634 1.00 101.38 ? 131 GLN A NE2 1 ATOM 1037 N N . ASP A 1 132 ? 11.310 69.099 12.865 1.00 93.58 ? 132 ASP A N 1 ATOM 1038 C CA . ASP A 1 132 ? 10.353 70.068 12.349 1.00 88.44 ? 132 ASP A CA 1 ATOM 1039 C C . ASP A 1 132 ? 10.987 70.815 11.181 1.00 80.61 ? 132 ASP A C 1 ATOM 1040 O O . ASP A 1 132 ? 11.931 71.582 11.365 1.00 112.12 ? 132 ASP A O 1 ATOM 1041 C CB . ASP A 1 132 ? 9.922 71.045 13.443 1.00 89.66 ? 132 ASP A CB 1 ATOM 1042 C CG . ASP A 1 132 ? 8.757 71.920 13.020 1.00 114.12 ? 132 ASP A CG 1 ATOM 1043 O OD1 . ASP A 1 132 ? 8.335 71.835 11.847 1.00 127.13 ? 132 ASP A OD1 1 ATOM 1044 O OD2 . ASP A 1 132 ? 8.267 72.701 13.862 1.00 120.77 ? 132 ASP A OD2 1 ATOM 1045 N N . GLY A 1 133 ? 10.453 70.603 9.984 1.00 83.50 ? 133 GLY A N 1 ATOM 1046 C CA . GLY A 1 133 ? 11.049 71.156 8.783 1.00 85.58 ? 133 GLY A CA 1 ATOM 1047 C C . GLY A 1 133 ? 12.445 70.604 8.568 1.00 99.69 ? 133 GLY A C 1 ATOM 1048 O O . GLY A 1 133 ? 12.662 69.395 8.632 1.00 108.18 ? 133 GLY A O 1 ATOM 1049 N N . THR A 1 134 ? 13.398 71.494 8.318 1.00 129.20 ? 134 THR A N 1 ATOM 1050 C CA . THR A 1 134 ? 14.780 71.088 8.094 1.00 120.50 ? 134 THR A CA 1 ATOM 1051 C C . THR A 1 134 ? 15.511 70.796 9.404 1.00 112.03 ? 134 THR A C 1 ATOM 1052 O O . THR A 1 134 ? 16.424 69.972 9.442 1.00 120.59 ? 134 THR A O 1 ATOM 1053 C CB . THR A 1 134 ? 15.556 72.165 7.315 1.00 117.26 ? 134 THR A CB 1 ATOM 1054 O OG1 . THR A 1 134 ? 15.481 73.412 8.016 1.00 116.57 ? 134 THR A OG1 1 ATOM 1055 C CG2 . THR A 1 134 ? 14.964 72.339 5.925 1.00 115.31 ? 134 THR A CG2 1 ATOM 1056 N N . LYS A 1 135 ? 15.103 71.471 10.474 1.00 83.64 ? 135 LYS A N 1 ATOM 1057 C CA . LYS A 1 135 ? 15.778 71.336 11.760 1.00 83.19 ? 135 LYS A CA 1 ATOM 1058 C C . LYS A 1 135 ? 15.469 70.000 12.436 1.00 92.87 ? 135 LYS A C 1 ATOM 1059 O O . LYS A 1 135 ? 14.344 69.502 12.377 1.00 78.50 ? 135 LYS A O 1 ATOM 1060 C CB . LYS A 1 135 ? 15.396 72.491 12.691 1.00 82.19 ? 135 LYS A CB 1 ATOM 1061 C CG . LYS A 1 135 ? 16.279 72.595 13.929 1.00 91.01 ? 135 LYS A CG 1 ATOM 1062 C CD . LYS A 1 135 ? 15.850 73.723 14.855 1.00 89.05 ? 135 LYS A CD 1 ATOM 1063 C CE . LYS A 1 135 ? 16.752 73.787 16.084 1.00 98.76 ? 135 LYS A CE 1 ATOM 1064 N NZ . LYS A 1 135 ? 16.377 74.883 17.023 1.00 112.34 ? 135 LYS A NZ 1 ATOM 1065 N N . THR A 1 136 ? 16.481 69.424 13.075 1.00 91.24 ? 136 THR A N 1 ATOM 1066 C CA . THR A 1 136 ? 16.312 68.184 13.819 1.00 77.02 ? 136 THR A CA 1 ATOM 1067 C C . THR A 1 136 ? 17.036 68.250 15.160 1.00 79.83 ? 136 THR A C 1 ATOM 1068 O O . THR A 1 136 ? 18.234 68.529 15.217 1.00 84.78 ? 136 THR A O 1 ATOM 1069 C CB . THR A 1 136 ? 16.830 66.980 13.022 1.00 72.62 ? 136 THR A CB 1 ATOM 1070 O OG1 . THR A 1 136 ? 16.075 66.848 11.812 1.00 95.76 ? 136 THR A OG1 1 ATOM 1071 C CG2 . THR A 1 136 ? 16.697 65.708 13.838 1.00 69.61 ? 136 THR A CG2 1 ATOM 1072 N N . VAL A 1 137 ? 16.306 67.994 16.239 1.00 69.87 ? 137 VAL A N 1 ATOM 1073 C CA . VAL A 1 137 ? 16.896 68.000 17.569 1.00 68.86 ? 137 VAL A CA 1 ATOM 1074 C C . VAL A 1 137 ? 16.797 66.621 18.202 1.00 83.19 ? 137 VAL A C 1 ATOM 1075 O O . VAL A 1 137 ? 15.959 65.806 17.814 1.00 78.77 ? 137 VAL A O 1 ATOM 1076 C CB . VAL A 1 137 ? 16.218 69.026 18.494 1.00 69.48 ? 137 VAL A CB 1 ATOM 1077 C CG1 . VAL A 1 137 ? 16.290 70.411 17.885 1.00 72.45 ? 137 VAL A CG1 1 ATOM 1078 C CG2 . VAL A 1 137 ? 14.775 68.629 18.761 1.00 73.94 ? 137 VAL A CG2 1 ATOM 1079 N N . GLU A 1 138 ? 17.666 66.359 19.171 1.00 66.76 ? 138 GLU A N 1 ATOM 1080 C CA . GLU A 1 138 ? 17.652 65.089 19.880 1.00 69.35 ? 138 GLU A CA 1 ATOM 1081 C C . GLU A 1 138 ? 16.962 65.226 21.232 1.00 78.65 ? 138 GLU A C 1 ATOM 1082 O O . GLU A 1 138 ? 17.364 66.042 22.062 1.00 95.08 ? 138 GLU A O 1 ATOM 1083 C CB . GLU A 1 138 ? 19.076 64.564 20.067 1.00 77.78 ? 138 GLU A CB 1 ATOM 1084 C CG . GLU A 1 138 ? 19.148 63.207 20.749 1.00 82.61 ? 138 GLU A CG 1 ATOM 1085 C CD . GLU A 1 138 ? 20.567 62.690 20.869 1.00 95.79 ? 138 GLU A CD 1 ATOM 1086 O OE1 . GLU A 1 138 ? 21.507 63.515 20.854 1.00 88.16 ? 138 GLU A OE1 1 ATOM 1087 O OE2 . GLU A 1 138 ? 20.742 61.456 20.971 1.00 98.57 ? 138 GLU A OE2 1 ATOM 1088 N N . TYR A 1 139 ? 15.920 64.429 21.450 1.00 75.15 ? 139 TYR A N 1 ATOM 1089 C CA . TYR A 1 139 ? 15.239 64.416 22.738 1.00 72.87 ? 139 TYR A CA 1 ATOM 1090 C C . TYR A 1 139 ? 15.462 63.094 23.451 1.00 58.43 ? 139 TYR A C 1 ATOM 1091 O O . TYR A 1 139 ? 14.952 62.063 23.026 1.00 70.91 ? 139 TYR A O 1 ATOM 1092 C CB . TYR A 1 139 ? 13.743 64.670 22.574 1.00 59.97 ? 139 TYR A CB 1 ATOM 1093 C CG . TYR A 1 139 ? 13.011 64.711 23.894 1.00 59.63 ? 139 TYR A CG 1 ATOM 1094 C CD1 . TYR A 1 139 ? 13.380 65.616 24.882 1.00 71.74 ? 139 TYR A CD1 1 ATOM 1095 C CD2 . TYR A 1 139 ? 11.957 63.849 24.155 1.00 58.31 ? 139 TYR A CD2 1 ATOM 1096 C CE1 . TYR A 1 139 ? 12.720 65.660 26.092 1.00 61.03 ? 139 TYR A CE1 1 ATOM 1097 C CE2 . TYR A 1 139 ? 11.288 63.887 25.361 1.00 58.33 ? 139 TYR A CE2 1 ATOM 1098 C CZ . TYR A 1 139 ? 11.675 64.795 26.328 1.00 81.90 ? 139 TYR A CZ 1 ATOM 1099 O OH . TYR A 1 139 ? 11.017 64.841 27.535 1.00 89.84 ? 139 TYR A OH 1 ATOM 1100 N N . ALA A 1 140 ? 16.224 63.130 24.538 1.00 65.78 ? 140 ALA A N 1 ATOM 1101 C CA . ALA A 1 140 ? 16.557 61.917 25.276 1.00 74.00 ? 140 ALA A CA 1 ATOM 1102 C C . ALA A 1 140 ? 16.519 62.162 26.777 1.00 70.61 ? 140 ALA A C 1 ATOM 1103 O O . ALA A 1 140 ? 17.554 62.126 27.438 1.00 68.07 ? 140 ALA A O 1 ATOM 1104 C CB . ALA A 1 140 ? 17.927 61.403 24.860 1.00 57.92 ? 140 ALA A CB 1 ATOM 1105 N N . PRO A 1 141 ? 15.317 62.393 27.320 1.00 57.88 ? 141 PRO A N 1 ATOM 1106 C CA . PRO A 1 141 ? 15.148 62.767 28.728 1.00 63.92 ? 141 PRO A CA 1 ATOM 1107 C C . PRO A 1 141 ? 15.682 61.712 29.693 1.00 62.30 ? 141 PRO A C 1 ATOM 1108 O O . PRO A 1 141 ? 16.135 62.059 30.783 1.00 64.55 ? 141 PRO A O 1 ATOM 1109 C CB . PRO A 1 141 ? 13.631 62.912 28.869 1.00 76.98 ? 141 PRO A CB 1 ATOM 1110 C CG . PRO A 1 141 ? 13.074 62.023 27.810 1.00 72.80 ? 141 PRO A CG 1 ATOM 1111 C CD . PRO A 1 141 ? 14.023 62.161 26.657 1.00 56.98 ? 141 PRO A CD 1 ATOM 1112 N N . CYS A 1 142 ? 15.636 60.444 29.297 1.00 70.69 ? 142 CYS A N 1 ATOM 1113 C CA . CYS A 1 142 ? 16.102 59.367 30.164 1.00 84.18 ? 142 CYS A CA 1 ATOM 1114 C C . CYS A 1 142 ? 17.627 59.315 30.228 1.00 87.48 ? 142 CYS A C 1 ATOM 1115 O O . CYS A 1 142 ? 18.197 58.568 31.023 1.00 76.42 ? 142 CYS A O 1 ATOM 1116 C CB . CYS A 1 142 ? 15.549 58.019 29.694 1.00 92.80 ? 142 CYS A CB 1 ATOM 1117 S SG . CYS A 1 142 ? 14.319 57.277 30.802 1.00 90.59 ? 142 CYS A SG 1 ATOM 1118 N N . ARG A 1 143 ? 18.285 60.110 29.388 1.00 58.36 ? 143 ARG A N 1 ATOM 1119 C CA . ARG A 1 143 ? 19.741 60.180 29.394 1.00 59.44 ? 143 ARG A CA 1 ATOM 1120 C C . ARG A 1 143 ? 20.179 61.327 30.292 1.00 83.95 ? 143 ARG A C 1 ATOM 1121 O O . ARG A 1 143 ? 20.010 62.498 29.952 1.00 103.47 ? 143 ARG A O 1 ATOM 1122 C CB . ARG A 1 143 ? 20.271 60.365 27.972 1.00 59.39 ? 143 ARG A CB 1 ATOM 1123 C CG . ARG A 1 143 ? 21.766 60.160 27.819 1.00 64.66 ? 143 ARG A CG 1 ATOM 1124 C CD . ARG A 1 143 ? 22.149 60.145 26.348 1.00 60.60 ? 143 ARG A CD 1 ATOM 1125 N NE . ARG A 1 143 ? 21.827 61.409 25.692 1.00 99.34 ? 143 ARG A NE 1 ATOM 1126 C CZ . ARG A 1 143 ? 21.919 61.617 24.383 1.00 85.29 ? 143 ARG A CZ 1 ATOM 1127 N NH1 . ARG A 1 143 ? 22.319 60.640 23.582 1.00 83.78 ? 143 ARG A NH1 1 ATOM 1128 N NH2 . ARG A 1 143 ? 21.607 62.801 23.875 1.00 62.32 ? 143 ARG A NH2 1 ATOM 1129 N N . SER A 1 144 ? 20.762 60.983 31.434 1.00 66.91 ? 144 SER A N 1 ATOM 1130 C CA . SER A 1 144 ? 20.955 61.959 32.496 1.00 94.06 ? 144 SER A CA 1 ATOM 1131 C C . SER A 1 144 ? 22.081 61.583 33.445 1.00 82.57 ? 144 SER A C 1 ATOM 1132 O O . SER A 1 144 ? 22.807 60.618 33.219 1.00 75.73 ? 144 SER A O 1 ATOM 1133 C CB . SER A 1 144 ? 19.655 62.128 33.284 1.00 101.71 ? 144 SER A CB 1 ATOM 1134 O OG . SER A 1 144 ? 19.139 60.867 33.682 1.00 65.08 ? 144 SER A OG 1 ATOM 1135 N N . GLN A 1 145 ? 22.202 62.348 34.524 1.00 74.97 ? 145 GLN A N 1 ATOM 1136 C CA . GLN A 1 145 ? 23.237 62.113 35.519 1.00 89.41 ? 145 GLN A CA 1 ATOM 1137 C C . GLN A 1 145 ? 22.776 61.047 36.508 1.00 94.96 ? 145 GLN A C 1 ATOM 1138 O O . GLN A 1 145 ? 23.484 60.714 37.458 1.00 106.96 ? 145 GLN A O 1 ATOM 1139 C CB . GLN A 1 145 ? 23.585 63.414 36.246 1.00 111.72 ? 145 GLN A CB 1 ATOM 1140 C CG . GLN A 1 145 ? 23.799 64.613 35.323 1.00 117.20 ? 145 GLN A CG 1 ATOM 1141 C CD . GLN A 1 145 ? 25.079 64.526 34.506 1.00 109.66 ? 145 GLN A CD 1 ATOM 1142 O OE1 . GLN A 1 145 ? 25.203 63.696 33.603 1.00 92.23 ? 145 GLN A OE1 1 ATOM 1143 N NE2 . GLN A 1 145 ? 26.035 65.393 34.816 1.00 75.81 ? 145 GLN A NE2 1 ATOM 1144 N N . ASP A 1 146 ? 21.578 60.521 36.273 1.00 91.68 ? 146 ASP A N 1 ATOM 1145 C CA . ASP A 1 146 ? 21.051 59.404 37.048 1.00 105.81 ? 146 ASP A CA 1 ATOM 1146 C C . ASP A 1 146 ? 21.233 58.131 36.226 1.00 101.19 ? 146 ASP A C 1 ATOM 1147 O O . ASP A 1 146 ? 20.541 57.928 35.228 1.00 115.32 ? 146 ASP A O 1 ATOM 1148 C CB . ASP A 1 146 ? 19.580 59.643 37.390 1.00 88.30 ? 146 ASP A CB 1 ATOM 1149 C CG . ASP A 1 146 ? 19.070 58.706 38.457 1.00 102.07 ? 146 ASP A CG 1 ATOM 1150 O OD1 . ASP A 1 146 ? 19.900 58.072 39.142 1.00 138.41 ? 146 ASP A OD1 1 ATOM 1151 O OD2 . ASP A 1 146 ? 17.836 58.612 38.617 1.00 98.55 ? 146 ASP A OD2 1 ATOM 1152 N N . ILE A 1 147 ? 22.151 57.269 36.656 1.00 76.54 ? 147 ILE A N 1 ATOM 1153 C CA . ILE A 1 147 ? 22.718 56.268 35.753 1.00 76.26 ? 147 ILE A CA 1 ATOM 1154 C C . ILE A 1 147 ? 22.179 54.843 35.855 1.00 98.30 ? 147 ILE A C 1 ATOM 1155 O O . ILE A 1 147 ? 21.473 54.393 34.968 1.00 119.38 ? 147 ILE A O 1 ATOM 1156 C CB . ILE A 1 147 ? 24.245 56.181 35.925 1.00 68.48 ? 147 ILE A CB 1 ATOM 1157 C CG1 . ILE A 1 147 ? 24.645 56.532 37.358 1.00 87.43 ? 147 ILE A CG1 1 ATOM 1158 C CG2 . ILE A 1 147 ? 24.934 57.102 34.943 1.00 74.46 ? 147 ILE A CG2 1 ATOM 1159 C CD1 . ILE A 1 147 ? 26.093 56.237 37.670 1.00 101.70 ? 147 ILE A CD1 1 ATOM 1160 N N . ASP A 1 148 ? 22.505 54.132 36.925 1.00 87.03 ? 148 ASP A N 1 ATOM 1161 C CA . ASP A 1 148 ? 22.324 52.681 36.942 1.00 90.18 ? 148 ASP A CA 1 ATOM 1162 C C . ASP A 1 148 ? 20.855 52.262 36.983 1.00 88.53 ? 148 ASP A C 1 ATOM 1163 O O . ASP A 1 148 ? 19.962 53.092 36.839 1.00 78.60 ? 148 ASP A O 1 ATOM 1164 C CB . ASP A 1 148 ? 23.075 52.076 38.128 1.00 119.55 ? 148 ASP A CB 1 ATOM 1165 C CG . ASP A 1 148 ? 24.568 52.325 38.053 1.00 126.43 ? 148 ASP A CG 1 ATOM 1166 O OD1 . ASP A 1 148 ? 25.089 52.453 36.924 1.00 98.19 ? 148 ASP A OD1 1 ATOM 1167 O OD2 . ASP A 1 148 ? 25.218 52.395 39.118 1.00 133.90 ? 148 ASP A OD2 1 ATOM 1168 N N . ALA A 1 149 ? 20.619 50.961 37.128 1.00 83.91 ? 149 ALA A N 1 ATOM 1169 C CA . ALA A 1 149 ? 19.266 50.410 37.159 1.00 74.16 ? 149 ALA A CA 1 ATOM 1170 C C . ALA A 1 149 ? 18.358 51.136 38.154 1.00 72.05 ? 149 ALA A C 1 ATOM 1171 O O . ALA A 1 149 ? 17.166 51.305 37.900 1.00 74.80 ? 149 ALA A O 1 ATOM 1172 C CB . ALA A 1 149 ? 19.315 48.926 37.484 1.00 98.37 ? 149 ALA A CB 1 ATOM 1173 N N . ASP A 1 150 ? 18.922 51.573 39.278 1.00 76.46 ? 150 ASP A N 1 ATOM 1174 C CA . ASP A 1 150 ? 18.166 52.354 40.253 1.00 80.49 ? 150 ASP A CA 1 ATOM 1175 C C . ASP A 1 150 ? 17.857 53.748 39.713 1.00 82.97 ? 150 ASP A C 1 ATOM 1176 O O . ASP A 1 150 ? 16.983 54.444 40.226 1.00 109.57 ? 150 ASP A O 1 ATOM 1177 C CB . ASP A 1 150 ? 18.921 52.455 41.581 1.00 84.64 ? 150 ASP A CB 1 ATOM 1178 C CG . ASP A 1 150 ? 20.425 52.405 41.405 1.00 101.79 ? 150 ASP A CG 1 ATOM 1179 O OD1 . ASP A 1 150 ? 20.900 51.640 40.540 1.00 101.47 ? 150 ASP A OD1 1 ATOM 1180 O OD2 . ASP A 1 150 ? 21.132 53.126 42.140 1.00 132.89 ? 150 ASP A OD2 1 ATOM 1181 N N . GLY A 1 151 ? 18.583 54.148 38.677 1.00 68.68 ? 151 GLY A N 1 ATOM 1182 C CA . GLY A 1 151 ? 18.312 55.394 37.987 1.00 66.53 ? 151 GLY A CA 1 ATOM 1183 C C . GLY A 1 151 ? 17.558 55.166 36.691 1.00 63.28 ? 151 GLY A C 1 ATOM 1184 O O . GLY A 1 151 ? 16.762 54.233 36.578 1.00 71.66 ? 151 GLY A O 1 ATOM 1185 N N . GLN A 1 152 ? 17.810 56.026 35.710 1.00 61.40 ? 152 GLN A N 1 ATOM 1186 C CA . GLN A 1 152 ? 17.098 55.985 34.436 1.00 63.23 ? 152 GLN A CA 1 ATOM 1187 C C . GLN A 1 152 ? 17.830 55.235 33.321 1.00 70.26 ? 152 GLN A C 1 ATOM 1188 O O . GLN A 1 152 ? 17.395 55.258 32.174 1.00 74.08 ? 152 GLN A O 1 ATOM 1189 C CB . GLN A 1 152 ? 16.799 57.407 33.965 1.00 62.39 ? 152 GLN A CB 1 ATOM 1190 C CG . GLN A 1 152 ? 16.119 58.265 35.005 1.00 60.67 ? 152 GLN A CG 1 ATOM 1191 C CD . GLN A 1 152 ? 15.770 59.633 34.475 1.00 78.28 ? 152 GLN A CD 1 ATOM 1192 O OE1 . GLN A 1 152 ? 16.428 60.623 34.791 1.00 107.03 ? 152 GLN A OE1 1 ATOM 1193 N NE2 . GLN A 1 152 ? 14.727 59.698 33.658 1.00 88.24 ? 152 GLN A NE2 1 ATOM 1194 N N . GLY A 1 153 ? 18.953 54.603 33.638 1.00 72.58 ? 153 GLY A N 1 ATOM 1195 C CA . GLY A 1 153 ? 19.800 54.018 32.610 1.00 65.12 ? 153 GLY A CA 1 ATOM 1196 C C . GLY A 1 153 ? 19.190 52.964 31.714 1.00 64.36 ? 153 GLY A C 1 ATOM 1197 O O . GLY A 1 153 ? 19.504 52.896 30.528 1.00 89.64 ? 153 GLY A O 1 ATOM 1198 N N . PHE A 1 154 ? 18.338 52.124 32.282 1.00 72.24 ? 154 PHE A N 1 ATOM 1199 C CA . PHE A 1 154 ? 17.711 51.047 31.527 1.00 56.03 ? 154 PHE A CA 1 ATOM 1200 C C . PHE A 1 154 ? 16.317 51.424 31.032 1.00 65.40 ? 154 PHE A C 1 ATOM 1201 O O . PHE A 1 154 ? 15.593 50.586 30.497 1.00 101.66 ? 154 PHE A O 1 ATOM 1202 C CB . PHE A 1 154 ? 17.684 49.777 32.372 1.00 57.08 ? 154 PHE A CB 1 ATOM 1203 C CG . PHE A 1 154 ? 19.052 49.226 32.639 1.00 68.85 ? 154 PHE A CG 1 ATOM 1204 C CD1 . PHE A 1 154 ? 19.838 49.750 33.651 1.00 90.99 ? 154 PHE A CD1 1 ATOM 1205 C CD2 . PHE A 1 154 ? 19.570 48.212 31.851 1.00 63.17 ? 154 PHE A CD2 1 ATOM 1206 C CE1 . PHE A 1 154 ? 21.105 49.260 33.886 1.00 87.64 ? 154 PHE A CE1 1 ATOM 1207 C CE2 . PHE A 1 154 ? 20.837 47.717 32.080 1.00 66.10 ? 154 PHE A CE2 1 ATOM 1208 C CZ . PHE A 1 154 ? 21.607 48.244 33.097 1.00 81.73 ? 154 PHE A CZ 1 ATOM 1209 N N . CYS A 1 155 ? 15.963 52.693 31.222 1.00 55.65 ? 155 CYS A N 1 ATOM 1210 C CA . CYS A 1 155 ? 14.636 53.229 30.917 1.00 64.75 ? 155 CYS A CA 1 ATOM 1211 C C . CYS A 1 155 ? 14.076 52.822 29.560 1.00 72.59 ? 155 CYS A C 1 ATOM 1212 O O . CYS A 1 155 ? 12.896 52.477 29.452 1.00 65.51 ? 155 CYS A O 1 ATOM 1213 C CB . CYS A 1 155 ? 14.675 54.758 30.994 1.00 70.86 ? 155 CYS A CB 1 ATOM 1214 S SG . CYS A 1 155 ? 13.264 55.616 30.280 1.00 126.23 ? 155 CYS A SG 1 ATOM 1215 N N . GLN A 1 156 ? 14.927 52.860 28.539 1.00 58.45 ? 156 GLN A N 1 ATOM 1216 C CA . GLN A 1 156 ? 14.504 52.643 27.157 1.00 62.57 ? 156 GLN A CA 1 ATOM 1217 C C . GLN A 1 156 ? 13.382 53.611 26.786 1.00 67.79 ? 156 GLN A C 1 ATOM 1218 O O . GLN A 1 156 ? 12.383 53.219 26.186 1.00 79.58 ? 156 GLN A O 1 ATOM 1219 C CB . GLN A 1 156 ? 14.060 51.194 26.937 1.00 51.21 ? 156 GLN A CB 1 ATOM 1220 C CG . GLN A 1 156 ? 15.140 50.171 27.248 1.00 69.44 ? 156 GLN A CG 1 ATOM 1221 C CD . GLN A 1 156 ? 14.730 48.757 26.895 1.00 68.86 ? 156 GLN A CD 1 ATOM 1222 O OE1 . GLN A 1 156 ? 14.029 48.529 25.912 1.00 71.62 ? 156 GLN A OE1 1 ATOM 1223 N NE2 . GLN A 1 156 ? 15.168 47.796 27.701 1.00 76.07 ? 156 GLN A NE2 1 ATOM 1224 N N . GLY A 1 157 ? 13.561 54.877 27.154 1.00 60.75 ? 157 GLY A N 1 ATOM 1225 C CA . GLY A 1 157 ? 12.581 55.911 26.872 1.00 62.53 ? 157 GLY A CA 1 ATOM 1226 C C . GLY A 1 157 ? 12.328 56.093 25.391 1.00 62.50 ? 157 GLY A C 1 ATOM 1227 O O . GLY A 1 157 ? 13.255 56.060 24.582 1.00 58.69 ? 157 GLY A O 1 ATOM 1228 N N . GLY A 1 158 ? 11.064 56.289 25.035 1.00 64.71 ? 158 GLY A N 1 ATOM 1229 C CA . GLY A 1 158 ? 10.671 56.347 23.642 1.00 60.06 ? 158 GLY A CA 1 ATOM 1230 C C . GLY A 1 158 ? 10.061 55.025 23.219 1.00 75.44 ? 158 GLY A C 1 ATOM 1231 O O . GLY A 1 158 ? 9.748 54.819 22.048 1.00 68.28 ? 158 GLY A O 1 ATOM 1232 N N . PHE A 1 159 ? 9.902 54.125 24.186 1.00 59.07 ? 159 PHE A N 1 ATOM 1233 C CA . PHE A 1 159 ? 9.264 52.835 23.955 1.00 57.44 ? 159 PHE A CA 1 ATOM 1234 C C . PHE A 1 159 ? 7.842 53.043 23.448 1.00 66.50 ? 159 PHE A C 1 ATOM 1235 O O . PHE A 1 159 ? 7.353 52.301 22.596 1.00 80.49 ? 159 PHE A O 1 ATOM 1236 C CB . PHE A 1 159 ? 9.264 52.007 25.241 1.00 72.07 ? 159 PHE A CB 1 ATOM 1237 C CG . PHE A 1 159 ? 8.880 50.571 25.042 1.00 73.53 ? 159 PHE A CG 1 ATOM 1238 C CD1 . PHE A 1 159 ? 9.791 49.661 24.535 1.00 58.03 ? 159 PHE A CD1 1 ATOM 1239 C CD2 . PHE A 1 159 ? 7.612 50.126 25.379 1.00 86.78 ? 159 PHE A CD2 1 ATOM 1240 C CE1 . PHE A 1 159 ? 9.442 48.337 24.356 1.00 63.26 ? 159 PHE A CE1 1 ATOM 1241 C CE2 . PHE A 1 159 ? 7.257 48.802 25.204 1.00 68.60 ? 159 PHE A CE2 1 ATOM 1242 C CZ . PHE A 1 159 ? 8.174 47.907 24.690 1.00 57.78 ? 159 PHE A CZ 1 ATOM 1243 N N . SER A 1 160 ? 7.187 54.064 23.990 1.00 68.19 ? 160 SER A N 1 ATOM 1244 C CA . SER A 1 160 ? 5.892 54.515 23.502 1.00 57.11 ? 160 SER A CA 1 ATOM 1245 C C . SER A 1 160 ? 5.809 56.030 23.645 1.00 69.97 ? 160 SER A C 1 ATOM 1246 O O . SER A 1 160 ? 6.252 56.591 24.647 1.00 83.58 ? 160 SER A O 1 ATOM 1247 C CB . SER A 1 160 ? 4.752 53.837 24.262 1.00 61.95 ? 160 SER A CB 1 ATOM 1248 O OG . SER A 1 160 ? 4.780 54.175 25.639 1.00 59.01 ? 160 SER A OG 1 ATOM 1249 N N . ILE A 1 161 ? 5.242 56.689 22.641 1.00 58.51 ? 161 ILE A N 1 ATOM 1250 C CA . ILE A 1 161 ? 5.153 58.144 22.638 1.00 53.20 ? 161 ILE A CA 1 ATOM 1251 C C . ILE A 1 161 ? 3.792 58.627 22.160 1.00 68.43 ? 161 ILE A C 1 ATOM 1252 O O . ILE A 1 161 ? 3.083 57.911 21.455 1.00 79.82 ? 161 ILE A O 1 ATOM 1253 C CB . ILE A 1 161 ? 6.228 58.771 21.741 1.00 74.36 ? 161 ILE A CB 1 ATOM 1254 C CG1 . ILE A 1 161 ? 6.220 58.089 20.369 1.00 63.81 ? 161 ILE A CG1 1 ATOM 1255 C CG2 . ILE A 1 161 ? 7.597 58.678 22.399 1.00 78.10 ? 161 ILE A CG2 1 ATOM 1256 C CD1 . ILE A 1 161 ? 7.190 58.682 19.378 1.00 85.19 ? 161 ILE A CD1 1 ATOM 1257 N N . ASP A 1 162 ? 3.430 59.841 22.557 1.00 55.56 ? 162 ASP A N 1 ATOM 1258 C CA . ASP A 1 162 ? 2.219 60.475 22.057 1.00 61.19 ? 162 ASP A CA 1 ATOM 1259 C C . ASP A 1 162 ? 2.306 61.988 22.219 1.00 72.28 ? 162 ASP A C 1 ATOM 1260 O O . ASP A 1 162 ? 3.058 62.485 23.060 1.00 59.44 ? 162 ASP A O 1 ATOM 1261 C CB . ASP A 1 162 ? 0.990 59.931 22.786 1.00 60.38 ? 162 ASP A CB 1 ATOM 1262 C CG . ASP A 1 162 ? -0.229 59.841 21.889 1.00 99.23 ? 162 ASP A CG 1 ATOM 1263 O OD1 . ASP A 1 162 ? -0.370 60.693 20.986 1.00 107.25 ? 162 ASP A OD1 1 ATOM 1264 O OD2 . ASP A 1 162 ? -1.044 58.913 22.084 1.00 105.99 ? 162 ASP A OD2 1 ATOM 1265 N N . PHE A 1 163 ? 1.532 62.719 21.422 1.00 76.42 ? 163 PHE A N 1 ATOM 1266 C CA . PHE A 1 163 ? 1.424 64.162 21.597 1.00 62.66 ? 163 PHE A CA 1 ATOM 1267 C C . PHE A 1 163 ? 0.161 64.499 22.376 1.00 73.69 ? 163 PHE A C 1 ATOM 1268 O O . PHE A 1 163 ? -0.649 63.626 22.674 1.00 93.72 ? 163 PHE A O 1 ATOM 1269 C CB . PHE A 1 163 ? 1.403 64.884 20.249 1.00 72.01 ? 163 PHE A CB 1 ATOM 1270 C CG . PHE A 1 163 ? 2.739 64.951 19.567 1.00 83.10 ? 163 PHE A CG 1 ATOM 1271 C CD1 . PHE A 1 163 ? 3.656 65.931 19.905 1.00 64.65 ? 163 PHE A CD1 1 ATOM 1272 C CD2 . PHE A 1 163 ? 3.069 64.047 18.571 1.00 85.91 ? 163 PHE A CD2 1 ATOM 1273 C CE1 . PHE A 1 163 ? 4.880 65.998 19.273 1.00 64.44 ? 163 PHE A CE1 1 ATOM 1274 C CE2 . PHE A 1 163 ? 4.294 64.110 17.936 1.00 86.01 ? 163 PHE A CE2 1 ATOM 1275 C CZ . PHE A 1 163 ? 5.200 65.086 18.288 1.00 63.53 ? 163 PHE A CZ 1 ATOM 1276 N N . THR A 1 164 ? -0.013 65.778 22.678 1.00 75.22 ? 164 THR A N 1 ATOM 1277 C CA . THR A 1 164 ? -1.204 66.254 23.365 1.00 80.36 ? 164 THR A CA 1 ATOM 1278 C C . THR A 1 164 ? -1.789 67.392 22.550 1.00 94.32 ? 164 THR A C 1 ATOM 1279 O O . THR A 1 164 ? -1.131 67.899 21.641 1.00 81.81 ? 164 THR A O 1 ATOM 1280 C CB . THR A 1 164 ? -0.904 66.732 24.794 1.00 92.90 ? 164 THR A CB 1 ATOM 1281 O OG1 . THR A 1 164 ? -0.046 67.880 24.747 1.00 90.24 ? 164 THR A OG1 1 ATOM 1282 C CG2 . THR A 1 164 ? -0.241 65.622 25.600 1.00 66.23 ? 164 THR A CG2 1 ATOM 1283 N N . LYS A 1 165 ? -3.020 67.780 22.873 1.00 100.98 ? 165 LYS A N 1 ATOM 1284 C CA . LYS A 1 165 ? -3.760 68.760 22.083 1.00 95.15 ? 165 LYS A CA 1 ATOM 1285 C C . LYS A 1 165 ? -2.930 70.005 21.775 1.00 90.47 ? 165 LYS A C 1 ATOM 1286 O O . LYS A 1 165 ? -2.982 70.520 20.659 1.00 101.53 ? 165 LYS A O 1 ATOM 1287 C CB . LYS A 1 165 ? -5.056 69.151 22.799 1.00 101.78 ? 165 LYS A CB 1 ATOM 1288 C CG . LYS A 1 165 ? -6.110 69.757 21.881 1.00 102.08 ? 165 LYS A CG 1 ATOM 1289 C CD . LYS A 1 165 ? -7.518 69.344 22.296 1.00 116.91 ? 165 LYS A CD 1 ATOM 1290 C CE . LYS A 1 165 ? -7.891 69.892 23.666 1.00 130.00 ? 165 LYS A CE 1 ATOM 1291 N NZ . LYS A 1 165 ? -7.999 71.380 23.668 1.00 127.47 ? 165 LYS A NZ 1 ATOM 1292 N N . ALA A 1 166 ? -2.162 70.490 22.749 1.00 84.51 ? 166 ALA A N 1 ATOM 1293 C CA . ALA A 1 166 ? -1.214 71.558 22.452 1.00 91.43 ? 166 ALA A CA 1 ATOM 1294 C C . ALA A 1 166 ? 0.239 71.213 22.794 1.00 98.64 ? 166 ALA A C 1 ATOM 1295 O O . ALA A 1 166 ? 0.619 71.203 23.962 1.00 116.76 ? 166 ALA A O 1 ATOM 1296 C CB . ALA A 1 166 ? -1.627 72.826 23.184 1.00 98.86 ? 166 ALA A CB 1 ATOM 1297 N N . ASP A 1 167 ? 1.037 70.959 21.756 1.00 104.70 ? 167 ASP A N 1 ATOM 1298 C CA . ASP A 1 167 ? 2.505 70.993 21.806 1.00 109.27 ? 167 ASP A CA 1 ATOM 1299 C C . ASP A 1 167 ? 3.188 70.368 23.027 1.00 99.75 ? 167 ASP A C 1 ATOM 1300 O O . ASP A 1 167 ? 4.054 70.997 23.635 1.00 120.74 ? 167 ASP A O 1 ATOM 1301 C CB . ASP A 1 167 ? 2.980 72.442 21.673 1.00 136.44 ? 167 ASP A CB 1 ATOM 1302 C CG . ASP A 1 167 ? 2.959 72.932 20.239 1.00 139.05 ? 167 ASP A CG 1 ATOM 1303 O OD1 . ASP A 1 167 ? 2.193 72.368 19.428 1.00 141.65 ? 167 ASP A OD1 1 ATOM 1304 O OD2 . ASP A 1 167 ? 3.711 73.878 19.922 1.00 124.18 ? 167 ASP A OD2 1 ATOM 1305 N N . ARG A 1 168 ? 2.814 69.149 23.394 1.00 75.73 ? 168 ARG A N 1 ATOM 1306 C CA . ARG A 1 168 ? 3.505 68.473 24.489 1.00 78.25 ? 168 ARG A CA 1 ATOM 1307 C C . ARG A 1 168 ? 3.649 66.977 24.224 1.00 68.60 ? 168 ARG A C 1 ATOM 1308 O O . ARG A 1 168 ? 2.691 66.317 23.828 1.00 91.99 ? 168 ARG A O 1 ATOM 1309 C CB . ARG A 1 168 ? 2.775 68.710 25.811 1.00 69.36 ? 168 ARG A CB 1 ATOM 1310 C CG . ARG A 1 168 ? 3.586 68.324 27.036 1.00 96.20 ? 168 ARG A CG 1 ATOM 1311 C CD . ARG A 1 168 ? 2.827 68.609 28.325 1.00 80.40 ? 168 ARG A CD 1 ATOM 1312 N NE . ARG A 1 168 ? 3.358 69.764 29.043 1.00 72.42 ? 168 ARG A NE 1 ATOM 1313 C CZ . ARG A 1 168 ? 4.374 69.711 29.898 1.00 78.31 ? 168 ARG A CZ 1 ATOM 1314 N NH1 . ARG A 1 168 ? 4.980 68.557 30.142 1.00 82.93 ? 168 ARG A NH1 1 ATOM 1315 N NH2 . ARG A 1 168 ? 4.789 70.813 30.508 1.00 95.61 ? 168 ARG A NH2 1 ATOM 1316 N N . VAL A 1 169 ? 4.847 66.445 24.442 1.00 63.68 ? 169 VAL A N 1 ATOM 1317 C CA . VAL A 1 169 ? 5.086 65.025 24.212 1.00 77.33 ? 169 VAL A CA 1 ATOM 1318 C C . VAL A 1 169 ? 4.895 64.218 25.486 1.00 85.25 ? 169 VAL A C 1 ATOM 1319 O O . VAL A 1 169 ? 5.234 64.666 26.580 1.00 74.05 ? 169 VAL A O 1 ATOM 1320 C CB . VAL A 1 169 ? 6.505 64.749 23.667 1.00 60.26 ? 169 VAL A CB 1 ATOM 1321 C CG1 . VAL A 1 169 ? 6.661 65.319 22.274 1.00 61.30 ? 169 VAL A CG1 1 ATOM 1322 C CG2 . VAL A 1 169 ? 7.559 65.309 24.605 1.00 110.11 ? 169 VAL A CG2 1 ATOM 1323 N N . LEU A 1 170 ? 4.326 63.029 25.333 1.00 80.41 ? 170 LEU A N 1 ATOM 1324 C CA . LEU A 1 170 ? 4.229 62.083 26.428 1.00 72.32 ? 170 LEU A CA 1 ATOM 1325 C C . LEU A 1 170 ? 5.109 60.886 26.110 1.00 79.72 ? 170 LEU A C 1 ATOM 1326 O O . LEU A 1 170 ? 4.827 60.124 25.186 1.00 74.59 ? 170 LEU A O 1 ATOM 1327 C CB . LEU A 1 170 ? 2.784 61.645 26.655 1.00 66.34 ? 170 LEU A CB 1 ATOM 1328 C CG . LEU A 1 170 ? 2.613 60.557 27.716 1.00 57.35 ? 170 LEU A CG 1 ATOM 1329 C CD1 . LEU A 1 170 ? 3.101 61.061 29.060 1.00 58.33 ? 170 LEU A CD1 1 ATOM 1330 C CD2 . LEU A 1 170 ? 1.167 60.098 27.801 1.00 62.16 ? 170 LEU A CD2 1 ATOM 1331 N N . LEU A 1 171 ? 6.185 60.733 26.869 1.00 84.74 ? 171 LEU A N 1 ATOM 1332 C CA . LEU A 1 171 ? 7.159 59.689 26.595 1.00 61.59 ? 171 LEU A CA 1 ATOM 1333 C C . LEU A 1 171 ? 7.305 58.768 27.787 1.00 75.09 ? 171 LEU A C 1 ATOM 1334 O O . LEU A 1 171 ? 7.729 59.191 28.863 1.00 85.56 ? 171 LEU A O 1 ATOM 1335 C CB . LEU A 1 171 ? 8.514 60.305 26.232 1.00 57.84 ? 171 LEU A CB 1 ATOM 1336 C CG . LEU A 1 171 ? 9.678 59.382 25.868 1.00 59.17 ? 171 LEU A CG 1 ATOM 1337 C CD1 . LEU A 1 171 ? 10.588 60.081 24.874 1.00 94.91 ? 171 LEU A CD1 1 ATOM 1338 C CD2 . LEU A 1 171 ? 10.475 58.970 27.096 1.00 65.23 ? 171 LEU A CD2 1 ATOM 1339 N N . GLY A 1 172 ? 6.941 57.507 27.601 1.00 61.01 ? 172 GLY A N 1 ATOM 1340 C CA . GLY A 1 172 ? 7.188 56.513 28.622 1.00 70.45 ? 172 GLY A CA 1 ATOM 1341 C C . GLY A 1 172 ? 8.416 55.674 28.333 1.00 75.83 ? 172 GLY A C 1 ATOM 1342 O O . GLY A 1 172 ? 8.881 55.604 27.194 1.00 64.79 ? 172 GLY A O 1 ATOM 1343 N N . GLY A 1 173 ? 8.942 55.031 29.370 1.00 61.90 ? 173 GLY A N 1 ATOM 1344 C CA . GLY A 1 173 ? 9.797 53.882 29.163 1.00 74.78 ? 173 GLY A CA 1 ATOM 1345 C C . GLY A 1 173 ? 9.709 52.953 30.356 1.00 85.53 ? 173 GLY A C 1 ATOM 1346 O O . GLY A 1 173 ? 9.600 53.396 31.500 1.00 88.87 ? 173 GLY A O 1 ATOM 1347 N N . PRO A 1 174 ? 9.799 51.647 30.087 1.00 61.45 ? 174 PRO A N 1 ATOM 1348 C CA . PRO A 1 174 ? 9.592 50.571 31.059 1.00 58.56 ? 174 PRO A CA 1 ATOM 1349 C C . PRO A 1 174 ? 10.726 50.382 32.054 1.00 70.37 ? 174 PRO A C 1 ATOM 1350 O O . PRO A 1 174 ? 10.485 49.895 33.155 1.00 106.05 ? 174 PRO A O 1 ATOM 1351 C CB . PRO A 1 174 ? 9.444 49.333 30.173 1.00 88.86 ? 174 PRO A CB 1 ATOM 1352 C CG . PRO A 1 174 ? 10.173 49.683 28.922 1.00 83.59 ? 174 PRO A CG 1 ATOM 1353 C CD . PRO A 1 174 ? 9.927 51.131 28.713 1.00 53.18 ? 174 PRO A CD 1 ATOM 1354 N N . GLY A 1 175 ? 11.941 50.753 31.671 1.00 55.47 ? 175 GLY A N 1 ATOM 1355 C CA . GLY A 1 175 ? 13.118 50.321 32.401 1.00 68.01 ? 175 GLY A CA 1 ATOM 1356 C C . GLY A 1 175 ? 13.566 51.159 33.582 1.00 73.04 ? 175 GLY A C 1 ATOM 1357 O O . GLY A 1 175 ? 14.482 50.765 34.303 1.00 97.58 ? 175 GLY A O 1 ATOM 1358 N N . SER A 1 176 ? 12.933 52.307 33.786 1.00 58.93 ? 176 SER A N 1 ATOM 1359 C CA . SER A 1 176 ? 13.355 53.211 34.850 1.00 71.28 ? 176 SER A CA 1 ATOM 1360 C C . SER A 1 176 ? 13.184 52.593 36.230 1.00 79.82 ? 176 SER A C 1 ATOM 1361 O O . SER A 1 176 ? 12.177 51.937 36.507 1.00 78.99 ? 176 SER A O 1 ATOM 1362 C CB . SER A 1 176 ? 12.581 54.526 34.783 1.00 85.59 ? 176 SER A CB 1 ATOM 1363 O OG . SER A 1 176 ? 13.021 55.331 33.705 1.00 86.01 ? 176 SER A OG 1 ATOM 1364 N N . PHE A 1 177 ? 14.188 52.804 37.079 1.00 67.07 ? 177 PHE A N 1 ATOM 1365 C CA . PHE A 1 177 ? 14.126 52.444 38.492 1.00 70.80 ? 177 PHE A CA 1 ATOM 1366 C C . PHE A 1 177 ? 13.831 50.962 38.682 1.00 80.91 ? 177 PHE A C 1 ATOM 1367 O O . PHE A 1 177 ? 12.782 50.591 39.209 1.00 67.71 ? 177 PHE A O 1 ATOM 1368 C CB . PHE A 1 177 ? 13.070 53.294 39.202 1.00 78.02 ? 177 PHE A CB 1 ATOM 1369 C CG . PHE A 1 177 ? 13.040 54.723 38.741 1.00 87.17 ? 177 PHE A CG 1 ATOM 1370 C CD1 . PHE A 1 177 ? 14.211 55.455 38.627 1.00 79.85 ? 177 PHE A CD1 1 ATOM 1371 C CD2 . PHE A 1 177 ? 11.843 55.327 38.397 1.00 102.54 ? 177 PHE A CD2 1 ATOM 1372 C CE1 . PHE A 1 177 ? 14.185 56.763 38.191 1.00 75.51 ? 177 PHE A CE1 1 ATOM 1373 C CE2 . PHE A 1 177 ? 11.811 56.638 37.961 1.00 90.57 ? 177 PHE A CE2 1 ATOM 1374 C CZ . PHE A 1 177 ? 12.983 57.355 37.858 1.00 80.04 ? 177 PHE A CZ 1 ATOM 1375 N N . TYR A 1 178 ? 14.772 50.126 38.253 1.00 88.90 ? 178 TYR A N 1 ATOM 1376 C CA . TYR A 1 178 ? 14.609 48.677 38.278 1.00 71.52 ? 178 TYR A CA 1 ATOM 1377 C C . TYR A 1 178 ? 13.286 48.268 37.632 1.00 76.23 ? 178 TYR A C 1 ATOM 1378 O O . TYR A 1 178 ? 12.520 47.475 38.181 1.00 64.91 ? 178 TYR A O 1 ATOM 1379 C CB . TYR A 1 178 ? 14.714 48.143 39.708 1.00 69.56 ? 178 TYR A CB 1 ATOM 1380 C CG . TYR A 1 178 ? 16.144 47.904 40.149 1.00 77.52 ? 178 TYR A CG 1 ATOM 1381 C CD1 . TYR A 1 178 ? 16.826 46.756 39.763 1.00 75.96 ? 178 TYR A CD1 1 ATOM 1382 C CD2 . TYR A 1 178 ? 16.815 48.829 40.939 1.00 77.93 ? 178 TYR A CD2 1 ATOM 1383 C CE1 . TYR A 1 178 ? 18.133 46.532 40.157 1.00 81.58 ? 178 TYR A CE1 1 ATOM 1384 C CE2 . TYR A 1 178 ? 18.122 48.614 41.340 1.00 84.93 ? 178 TYR A CE2 1 ATOM 1385 C CZ . TYR A 1 178 ? 18.776 47.464 40.945 1.00 101.49 ? 178 TYR A CZ 1 ATOM 1386 O OH . TYR A 1 178 ? 20.076 47.246 41.339 1.00 123.58 ? 178 TYR A OH 1 ATOM 1387 N N . TRP A 1 179 ? 13.037 48.842 36.459 1.00 84.80 ? 179 TRP A N 1 ATOM 1388 C CA . TRP A 1 179 ? 11.909 48.482 35.609 1.00 78.60 ? 179 TRP A CA 1 ATOM 1389 C C . TRP A 1 179 ? 10.552 48.752 36.246 1.00 71.24 ? 179 TRP A C 1 ATOM 1390 O O . TRP A 1 179 ? 9.565 48.089 35.929 1.00 68.04 ? 179 TRP A O 1 ATOM 1391 C CB . TRP A 1 179 ? 12.022 47.016 35.189 1.00 64.11 ? 179 TRP A CB 1 ATOM 1392 C CG . TRP A 1 179 ? 13.202 46.798 34.308 1.00 57.03 ? 179 TRP A CG 1 ATOM 1393 C CD1 . TRP A 1 179 ? 13.251 46.950 32.954 1.00 58.28 ? 179 TRP A CD1 1 ATOM 1394 C CD2 . TRP A 1 179 ? 14.522 46.426 34.719 1.00 58.84 ? 179 TRP A CD2 1 ATOM 1395 N NE1 . TRP A 1 179 ? 14.518 46.684 32.494 1.00 66.51 ? 179 TRP A NE1 1 ATOM 1396 C CE2 . TRP A 1 179 ? 15.316 46.358 33.559 1.00 60.30 ? 179 TRP A CE2 1 ATOM 1397 C CE3 . TRP A 1 179 ? 15.107 46.134 35.954 1.00 61.64 ? 179 TRP A CE3 1 ATOM 1398 C CZ2 . TRP A 1 179 ? 16.664 46.012 33.597 1.00 63.06 ? 179 TRP A CZ2 1 ATOM 1399 C CZ3 . TRP A 1 179 ? 16.445 45.796 35.991 1.00 64.49 ? 179 TRP A CZ3 1 ATOM 1400 C CH2 . TRP A 1 179 ? 17.209 45.736 34.821 1.00 62.80 ? 179 TRP A CH2 1 ATOM 1401 N N . GLN A 1 180 ? 10.503 49.741 37.131 1.00 69.94 ? 180 GLN A N 1 ATOM 1402 C CA . GLN A 1 180 ? 9.226 50.246 37.611 1.00 71.70 ? 180 GLN A CA 1 ATOM 1403 C C . GLN A 1 180 ? 8.527 50.967 36.469 1.00 65.68 ? 180 GLN A C 1 ATOM 1404 O O . GLN A 1 180 ? 7.302 50.935 36.351 1.00 70.96 ? 180 GLN A O 1 ATOM 1405 C CB . GLN A 1 180 ? 9.412 51.185 38.803 1.00 68.47 ? 180 GLN A CB 1 ATOM 1406 C CG . GLN A 1 180 ? 9.828 50.486 40.079 1.00 74.61 ? 180 GLN A CG 1 ATOM 1407 C CD . GLN A 1 180 ? 10.034 51.446 41.232 1.00 80.85 ? 180 GLN A CD 1 ATOM 1408 O OE1 . GLN A 1 180 ? 9.596 52.596 41.186 1.00 80.19 ? 180 GLN A OE1 1 ATOM 1409 N NE2 . GLN A 1 180 ? 10.705 50.976 42.277 1.00 85.13 ? 180 GLN A NE2 1 ATOM 1410 N N . GLY A 1 181 ? 9.323 51.608 35.622 1.00 63.37 ? 181 GLY A N 1 ATOM 1411 C CA . GLY A 1 181 ? 8.797 52.359 34.499 1.00 69.97 ? 181 GLY A CA 1 ATOM 1412 C C . GLY A 1 181 ? 8.699 53.835 34.818 1.00 78.05 ? 181 GLY A C 1 ATOM 1413 O O . GLY A 1 181 ? 8.724 54.231 35.983 1.00 84.05 ? 181 GLY A O 1 ATOM 1414 N N . GLN A 1 182 ? 8.593 54.656 33.781 1.00 79.99 ? 182 GLN A N 1 ATOM 1415 C CA . GLN A 1 182 ? 8.522 56.097 33.973 1.00 69.84 ? 182 GLN A CA 1 ATOM 1416 C C . GLN A 1 182 ? 7.745 56.779 32.856 1.00 77.00 ? 182 GLN A C 1 ATOM 1417 O O . GLN A 1 182 ? 7.763 56.329 31.712 1.00 58.73 ? 182 GLN A O 1 ATOM 1418 C CB . GLN A 1 182 ? 9.930 56.684 34.060 1.00 56.74 ? 182 GLN A CB 1 ATOM 1419 C CG . GLN A 1 182 ? 9.986 58.138 34.472 1.00 77.58 ? 182 GLN A CG 1 ATOM 1420 C CD . GLN A 1 182 ? 11.405 58.626 34.651 1.00 82.17 ? 182 GLN A CD 1 ATOM 1421 O OE1 . GLN A 1 182 ? 12.340 58.077 34.067 1.00 82.58 ? 182 GLN A OE1 1 ATOM 1422 N NE2 . GLN A 1 182 ? 11.577 59.657 35.469 1.00 78.59 ? 182 GLN A NE2 1 ATOM 1423 N N . LEU A 1 183 ? 7.056 57.861 33.200 1.00 89.14 ? 183 LEU A N 1 ATOM 1424 C CA . LEU A 1 183 ? 6.446 58.729 32.205 1.00 70.38 ? 183 LEU A CA 1 ATOM 1425 C C . LEU A 1 183 ? 7.112 60.092 32.263 1.00 68.82 ? 183 LEU A C 1 ATOM 1426 O O . LEU A 1 183 ? 7.278 60.661 33.341 1.00 60.68 ? 183 LEU A O 1 ATOM 1427 C CB . LEU A 1 183 ? 4.942 58.869 32.434 1.00 57.70 ? 183 LEU A CB 1 ATOM 1428 C CG . LEU A 1 183 ? 4.094 57.613 32.262 1.00 57.53 ? 183 LEU A CG 1 ATOM 1429 C CD1 . LEU A 1 183 ? 2.622 57.964 32.363 1.00 61.04 ? 183 LEU A CD1 1 ATOM 1430 C CD2 . LEU A 1 183 ? 4.403 56.946 30.936 1.00 56.54 ? 183 LEU A CD2 1 ATOM 1431 N N . ILE A 1 184 ? 7.507 60.610 31.107 1.00 73.83 ? 184 ILE A N 1 ATOM 1432 C CA . ILE A 1 184 ? 8.102 61.938 31.045 1.00 70.61 ? 184 ILE A CA 1 ATOM 1433 C C . ILE A 1 184 ? 7.391 62.789 30.004 1.00 69.60 ? 184 ILE A C 1 ATOM 1434 O O . ILE A 1 184 ? 7.202 62.362 28.866 1.00 71.73 ? 184 ILE A O 1 ATOM 1435 C CB . ILE A 1 184 ? 9.601 61.878 30.711 1.00 64.21 ? 184 ILE A CB 1 ATOM 1436 C CG1 . ILE A 1 184 ? 10.318 60.884 31.627 1.00 60.71 ? 184 ILE A CG1 1 ATOM 1437 C CG2 . ILE A 1 184 ? 10.222 63.260 30.831 1.00 81.70 ? 184 ILE A CG2 1 ATOM 1438 C CD1 . ILE A 1 184 ? 11.771 60.669 31.271 1.00 66.46 ? 184 ILE A CD1 1 ATOM 1439 N N . SER A 1 185 ? 6.991 63.993 30.397 1.00 75.83 ? 185 SER A N 1 ATOM 1440 C CA . SER A 1 185 ? 6.310 64.892 29.476 1.00 81.77 ? 185 SER A CA 1 ATOM 1441 C C . SER A 1 185 ? 7.028 66.228 29.344 1.00 80.80 ? 185 SER A C 1 ATOM 1442 O O . SER A 1 185 ? 7.389 66.852 30.341 1.00 79.05 ? 185 SER A O 1 ATOM 1443 C CB . SER A 1 185 ? 4.870 65.124 29.922 1.00 71.46 ? 185 SER A CB 1 ATOM 1444 O OG . SER A 1 185 ? 4.148 65.816 28.921 1.00 66.37 ? 185 SER A OG 1 ATOM 1445 N N . ASP A 1 186 ? 7.223 66.669 28.106 1.00 69.55 ? 186 ASP A N 1 ATOM 1446 C CA . ASP A 1 186 ? 7.931 67.917 27.851 1.00 86.90 ? 186 ASP A CA 1 ATOM 1447 C C . ASP A 1 186 ? 7.250 68.766 26.787 1.00 80.84 ? 186 ASP A C 1 ATOM 1448 O O . ASP A 1 186 ? 6.698 68.248 25.818 1.00 66.14 ? 186 ASP A O 1 ATOM 1449 C CB . ASP A 1 186 ? 9.375 67.632 27.435 1.00 82.33 ? 186 ASP A CB 1 ATOM 1450 C CG . ASP A 1 186 ? 10.334 67.677 28.604 1.00 100.21 ? 186 ASP A CG 1 ATOM 1451 O OD1 . ASP A 1 186 ? 10.268 68.653 29.380 1.00 110.38 ? 186 ASP A OD1 1 ATOM 1452 O OD2 . ASP A 1 186 ? 11.147 66.739 28.749 1.00 97.06 ? 186 ASP A OD2 1 ATOM 1453 N N . GLN A 1 187 ? 7.292 70.078 26.979 1.00 74.68 ? 187 GLN A N 1 ATOM 1454 C CA . GLN A 1 187 ? 6.806 71.005 25.972 1.00 80.11 ? 187 GLN A CA 1 ATOM 1455 C C . GLN A 1 187 ? 7.666 70.899 24.717 1.00 78.84 ? 187 GLN A C 1 ATOM 1456 O O . GLN A 1 187 ? 8.893 70.939 24.793 1.00 75.28 ? 187 GLN A O 1 ATOM 1457 C CB . GLN A 1 187 ? 6.811 72.435 26.512 1.00 88.58 ? 187 GLN A CB 1 ATOM 1458 C CG . GLN A 1 187 ? 5.974 72.611 27.768 1.00 83.45 ? 187 GLN A CG 1 ATOM 1459 C CD . GLN A 1 187 ? 6.194 73.948 28.442 1.00 88.85 ? 187 GLN A CD 1 ATOM 1460 O OE1 . GLN A 1 187 ? 7.004 74.760 27.994 1.00 107.32 ? 187 GLN A OE1 1 ATOM 1461 N NE2 . GLN A 1 187 ? 5.473 74.183 29.531 1.00 98.18 ? 187 GLN A NE2 1 ATOM 1462 N N . VAL A 1 188 ? 7.013 70.745 23.571 1.00 84.01 ? 188 VAL A N 1 ATOM 1463 C CA . VAL A 1 188 ? 7.702 70.652 22.289 1.00 77.92 ? 188 VAL A CA 1 ATOM 1464 C C . VAL A 1 188 ? 8.627 71.844 22.072 1.00 82.94 ? 188 VAL A C 1 ATOM 1465 O O . VAL A 1 188 ? 9.772 71.682 21.648 1.00 81.12 ? 188 VAL A O 1 ATOM 1466 C CB . VAL A 1 188 ? 6.696 70.565 21.127 1.00 91.31 ? 188 VAL A CB 1 ATOM 1467 C CG1 . VAL A 1 188 ? 7.392 70.780 19.793 1.00 71.85 ? 188 VAL A CG1 1 ATOM 1468 C CG2 . VAL A 1 188 ? 5.975 69.225 21.157 1.00 96.70 ? 188 VAL A CG2 1 ATOM 1469 N N . ALA A 1 189 ? 8.124 73.036 22.379 1.00 87.76 ? 189 ALA A N 1 ATOM 1470 C CA . ALA A 1 189 ? 8.917 74.255 22.279 1.00 78.07 ? 189 ALA A CA 1 ATOM 1471 C C . ALA A 1 189 ? 10.170 74.158 23.141 1.00 82.93 ? 189 ALA A C 1 ATOM 1472 O O . ALA A 1 189 ? 11.265 74.502 22.698 1.00 80.08 ? 189 ALA A O 1 ATOM 1473 C CB . ALA A 1 189 ? 8.089 75.456 22.683 1.00 81.27 ? 189 ALA A CB 1 ATOM 1474 N N . GLU A 1 190 ? 9.996 73.680 24.370 1.00 89.99 ? 190 GLU A N 1 ATOM 1475 C CA . GLU A 1 190 ? 11.108 73.484 25.294 1.00 75.57 ? 190 GLU A CA 1 ATOM 1476 C C . GLU A 1 190 ? 12.167 72.564 24.706 1.00 77.76 ? 190 GLU A C 1 ATOM 1477 O O . GLU A 1 190 ? 13.362 72.838 24.809 1.00 73.97 ? 190 GLU A O 1 ATOM 1478 C CB . GLU A 1 190 ? 10.605 72.916 26.623 1.00 87.04 ? 190 GLU A CB 1 ATOM 1479 C CG . GLU A 1 190 ? 10.226 73.970 27.641 1.00 92.99 ? 190 GLU A CG 1 ATOM 1480 C CD . GLU A 1 190 ? 11.438 74.684 28.204 1.00 120.81 ? 190 GLU A CD 1 ATOM 1481 O OE1 . GLU A 1 190 ? 12.403 73.993 28.594 1.00 103.86 ? 190 GLU A OE1 1 ATOM 1482 O OE2 . GLU A 1 190 ? 11.428 75.933 28.249 1.00 140.74 ? 190 GLU A OE2 1 ATOM 1483 N N . ILE A 1 191 ? 11.721 71.478 24.082 1.00 71.68 ? 191 ILE A N 1 ATOM 1484 C CA . ILE A 1 191 ? 12.629 70.502 23.493 1.00 71.76 ? 191 ILE A CA 1 ATOM 1485 C C . ILE A 1 191 ? 13.465 71.127 22.383 1.00 82.14 ? 191 ILE A C 1 ATOM 1486 O O . ILE A 1 191 ? 14.655 70.838 22.248 1.00 104.64 ? 191 ILE A O 1 ATOM 1487 C CB . ILE A 1 191 ? 11.862 69.291 22.934 1.00 74.21 ? 191 ILE A CB 1 ATOM 1488 C CG1 . ILE A 1 191 ? 11.083 68.597 24.052 1.00 81.32 ? 191 ILE A CG1 1 ATOM 1489 C CG2 . ILE A 1 191 ? 12.815 68.311 22.269 1.00 72.66 ? 191 ILE A CG2 1 ATOM 1490 C CD1 . ILE A 1 191 ? 10.359 67.350 23.604 1.00 79.20 ? 191 ILE A CD1 1 ATOM 1491 N N . VAL A 1 192 ? 12.842 71.996 21.598 1.00 72.63 ? 192 VAL A N 1 ATOM 1492 C CA . VAL A 1 192 ? 13.539 72.659 20.504 1.00 87.12 ? 192 VAL A CA 1 ATOM 1493 C C . VAL A 1 192 ? 14.410 73.814 20.999 1.00 83.99 ? 192 VAL A C 1 ATOM 1494 O O . VAL A 1 192 ? 15.534 73.996 20.534 1.00 90.90 ? 192 VAL A O 1 ATOM 1495 C CB . VAL A 1 192 ? 12.550 73.191 19.452 1.00 76.21 ? 192 VAL A CB 1 ATOM 1496 C CG1 . VAL A 1 192 ? 13.301 73.773 18.269 1.00 78.33 ? 192 VAL A CG1 1 ATOM 1497 C CG2 . VAL A 1 192 ? 11.621 72.082 18.995 1.00 75.32 ? 192 VAL A CG2 1 ATOM 1498 N N . SER A 1 193 ? 13.892 74.586 21.949 1.00 78.28 ? 193 SER A N 1 ATOM 1499 C CA . SER A 1 193 ? 14.578 75.793 22.402 1.00 85.87 ? 193 SER A CA 1 ATOM 1500 C C . SER A 1 193 ? 15.773 75.496 23.303 1.00 86.74 ? 193 SER A C 1 ATOM 1501 O O . SER A 1 193 ? 16.721 76.278 23.361 1.00 83.67 ? 193 SER A O 1 ATOM 1502 C CB . SER A 1 193 ? 13.600 76.719 23.133 1.00 89.39 ? 193 SER A CB 1 ATOM 1503 O OG . SER A 1 193 ? 13.051 76.092 24.279 1.00 94.25 ? 193 SER A OG 1 ATOM 1504 N N . LYS A 1 194 ? 15.726 74.374 24.010 1.00 94.74 ? 194 LYS A N 1 ATOM 1505 C CA . LYS A 1 194 ? 16.777 74.044 24.966 1.00 89.37 ? 194 LYS A CA 1 ATOM 1506 C C . LYS A 1 194 ? 17.847 73.103 24.408 1.00 87.21 ? 194 LYS A C 1 ATOM 1507 O O . LYS A 1 194 ? 18.753 72.699 25.139 1.00 75.22 ? 194 LYS A O 1 ATOM 1508 C CB . LYS A 1 194 ? 16.165 73.429 26.228 1.00 88.00 ? 194 LYS A CB 1 ATOM 1509 C CG . LYS A 1 194 ? 15.279 74.379 27.017 1.00 84.44 ? 194 LYS A CG 1 ATOM 1510 C CD . LYS A 1 194 ? 16.086 75.510 27.629 1.00 92.45 ? 194 LYS A CD 1 ATOM 1511 C CE . LYS A 1 194 ? 15.185 76.504 28.341 1.00 107.35 ? 194 LYS A CE 1 ATOM 1512 N NZ . LYS A 1 194 ? 14.216 77.138 27.404 1.00 107.46 ? 194 LYS A NZ 1 ATOM 1513 N N . TYR A 1 195 ? 17.752 72.745 23.130 1.00 74.95 ? 195 TYR A N 1 ATOM 1514 C CA . TYR A 1 195 ? 18.668 71.745 22.588 1.00 73.51 ? 195 TYR A CA 1 ATOM 1515 C C . TYR A 1 195 ? 20.089 72.265 22.417 1.00 75.41 ? 195 TYR A C 1 ATOM 1516 O O . TYR A 1 195 ? 20.320 73.280 21.765 1.00 107.93 ? 195 TYR A O 1 ATOM 1517 C CB . TYR A 1 195 ? 18.174 71.207 21.249 1.00 81.63 ? 195 TYR A CB 1 ATOM 1518 C CG . TYR A 1 195 ? 19.119 70.176 20.678 1.00 88.45 ? 195 TYR A CG 1 ATOM 1519 C CD1 . TYR A 1 195 ? 19.301 68.951 21.308 1.00 91.61 ? 195 TYR A CD1 1 ATOM 1520 C CD2 . TYR A 1 195 ? 19.845 70.432 19.527 1.00 73.17 ? 195 TYR A CD2 1 ATOM 1521 C CE1 . TYR A 1 195 ? 20.173 68.008 20.800 1.00 83.40 ? 195 TYR A CE1 1 ATOM 1522 C CE2 . TYR A 1 195 ? 20.718 69.494 19.009 1.00 77.59 ? 195 TYR A CE2 1 ATOM 1523 C CZ . TYR A 1 195 ? 20.878 68.284 19.649 1.00 87.68 ? 195 TYR A CZ 1 ATOM 1524 O OH . TYR A 1 195 ? 21.748 67.350 19.135 1.00 102.45 ? 195 TYR A OH 1 ATOM 1525 N N . ASP A 1 196 ? 21.034 71.551 23.019 1.00 84.24 ? 196 ASP A N 1 ATOM 1526 C CA . ASP A 1 196 ? 22.454 71.881 22.944 1.00 95.93 ? 196 ASP A CA 1 ATOM 1527 C C . ASP A 1 196 ? 23.274 70.653 22.550 1.00 101.37 ? 196 ASP A C 1 ATOM 1528 O O . ASP A 1 196 ? 23.593 69.822 23.401 1.00 92.92 ? 196 ASP A O 1 ATOM 1529 C CB . ASP A 1 196 ? 22.958 72.453 24.271 1.00 95.76 ? 196 ASP A CB 1 ATOM 1530 C CG . ASP A 1 196 ? 24.290 73.176 24.127 1.00 99.84 ? 196 ASP A CG 1 ATOM 1531 O OD1 . ASP A 1 196 ? 25.021 72.906 23.150 1.00 83.88 ? 196 ASP A OD1 1 ATOM 1532 O OD2 . ASP A 1 196 ? 24.607 74.018 24.994 1.00 116.39 ? 196 ASP A OD2 1 ATOM 1533 N N . PRO A 1 197 ? 23.602 70.528 21.255 1.00 75.51 ? 197 PRO A N 1 ATOM 1534 C CA . PRO A 1 197 ? 24.317 69.381 20.679 1.00 84.70 ? 197 PRO A CA 1 ATOM 1535 C C . PRO A 1 197 ? 25.609 69.024 21.414 1.00 82.37 ? 197 PRO A C 1 ATOM 1536 O O . PRO A 1 197 ? 26.072 67.888 21.310 1.00 74.12 ? 197 PRO A O 1 ATOM 1537 C CB . PRO A 1 197 ? 24.629 69.847 19.253 1.00 76.61 ? 197 PRO A CB 1 ATOM 1538 C CG . PRO A 1 197 ? 24.607 71.324 19.329 1.00 79.03 ? 197 PRO A CG 1 ATOM 1539 C CD . PRO A 1 197 ? 23.521 71.646 20.303 1.00 77.90 ? 197 PRO A CD 1 ATOM 1540 N N . ASN A 1 198 ? 26.184 69.986 22.129 1.00 85.21 ? 198 ASN A N 1 ATOM 1541 C CA . ASN A 1 198 ? 27.385 69.745 22.920 1.00 80.52 ? 198 ASN A CA 1 ATOM 1542 C C . ASN A 1 198 ? 27.071 69.346 24.361 1.00 102.79 ? 198 ASN A C 1 ATOM 1543 O O . ASN A 1 198 ? 27.976 69.188 25.180 1.00 127.08 ? 198 ASN A O 1 ATOM 1544 C CB . ASN A 1 198 ? 28.283 70.982 22.908 1.00 85.29 ? 198 ASN A CB 1 ATOM 1545 C CG . ASN A 1 198 ? 28.972 71.187 21.574 1.00 93.76 ? 198 ASN A CG 1 ATOM 1546 O OD1 . ASN A 1 198 ? 29.229 70.230 20.841 1.00 99.23 ? 198 ASN A OD1 1 ATOM 1547 N ND2 . ASN A 1 198 ? 29.280 72.438 21.252 1.00 85.72 ? 198 ASN A ND2 1 ATOM 1548 N N . VAL A 1 199 ? 25.786 69.194 24.668 1.00 87.61 ? 199 VAL A N 1 ATOM 1549 C CA . VAL A 1 199 ? 25.360 68.799 26.008 1.00 78.79 ? 199 VAL A CA 1 ATOM 1550 C C . VAL A 1 199 ? 24.548 67.505 25.966 1.00 72.84 ? 199 VAL A C 1 ATOM 1551 O O . VAL A 1 199 ? 23.458 67.462 25.396 1.00 71.26 ? 199 VAL A O 1 ATOM 1552 C CB . VAL A 1 199 ? 24.529 69.907 26.682 1.00 74.76 ? 199 VAL A CB 1 ATOM 1553 C CG1 . VAL A 1 199 ? 23.972 69.421 28.007 1.00 75.70 ? 199 VAL A CG1 1 ATOM 1554 C CG2 . VAL A 1 199 ? 25.376 71.154 26.883 1.00 79.66 ? 199 VAL A CG2 1 ATOM 1555 N N . TYR A 1 200 ? 25.083 66.456 26.582 1.00 91.89 ? 200 TYR A N 1 ATOM 1556 C CA . TYR A 1 200 ? 24.496 65.122 26.487 1.00 90.29 ? 200 TYR A CA 1 ATOM 1557 C C . TYR A 1 200 ? 23.281 64.938 27.396 1.00 89.01 ? 200 TYR A C 1 ATOM 1558 O O . TYR A 1 200 ? 22.435 64.079 27.140 1.00 79.17 ? 200 TYR A O 1 ATOM 1559 C CB . TYR A 1 200 ? 25.554 64.061 26.804 1.00 74.72 ? 200 TYR A CB 1 ATOM 1560 C CG . TYR A 1 200 ? 26.756 64.109 25.882 1.00 83.86 ? 200 TYR A CG 1 ATOM 1561 C CD1 . TYR A 1 200 ? 26.603 64.304 24.514 1.00 69.53 ? 200 TYR A CD1 1 ATOM 1562 C CD2 . TYR A 1 200 ? 28.045 63.975 26.382 1.00 88.56 ? 200 TYR A CD2 1 ATOM 1563 C CE1 . TYR A 1 200 ? 27.698 64.352 23.670 1.00 71.23 ? 200 TYR A CE1 1 ATOM 1564 C CE2 . TYR A 1 200 ? 29.147 64.025 25.545 1.00 101.68 ? 200 TYR A CE2 1 ATOM 1565 C CZ . TYR A 1 200 ? 28.968 64.213 24.190 1.00 90.30 ? 200 TYR A CZ 1 ATOM 1566 O OH . TYR A 1 200 ? 30.065 64.264 23.357 1.00 90.90 ? 200 TYR A OH 1 ATOM 1567 N N . SER A 1 201 ? 23.198 65.740 28.455 1.00 68.29 ? 201 SER A N 1 ATOM 1568 C CA . SER A 1 201 ? 22.043 65.699 29.349 1.00 70.89 ? 201 SER A CA 1 ATOM 1569 C C . SER A 1 201 ? 21.421 67.082 29.487 1.00 68.57 ? 201 SER A C 1 ATOM 1570 O O . SER A 1 201 ? 22.021 67.983 30.063 1.00 92.90 ? 201 SER A O 1 ATOM 1571 C CB . SER A 1 201 ? 22.440 65.165 30.724 1.00 74.52 ? 201 SER A CB 1 ATOM 1572 O OG . SER A 1 201 ? 23.046 63.889 30.622 1.00 87.11 ? 201 SER A OG 1 ATOM 1573 N N . ILE A 1 202 ? 20.205 67.238 28.979 1.00 67.58 ? 202 ILE A N 1 ATOM 1574 C CA . ILE A 1 202 ? 19.569 68.548 28.922 1.00 78.11 ? 202 ILE A CA 1 ATOM 1575 C C . ILE A 1 202 ? 18.426 68.684 29.921 1.00 70.74 ? 202 ILE A C 1 ATOM 1576 O O . ILE A 1 202 ? 17.490 67.886 29.923 1.00 90.39 ? 202 ILE A O 1 ATOM 1577 C CB . ILE A 1 202 ? 19.032 68.844 27.505 1.00 81.93 ? 202 ILE A CB 1 ATOM 1578 C CG1 . ILE A 1 202 ? 20.177 68.835 26.489 1.00 75.71 ? 202 ILE A CG1 1 ATOM 1579 C CG2 . ILE A 1 202 ? 18.308 70.179 27.474 1.00 80.28 ? 202 ILE A CG2 1 ATOM 1580 C CD1 . ILE A 1 202 ? 19.739 69.128 25.072 1.00 69.15 ? 202 ILE A CD1 1 ATOM 1581 N N . LYS A 1 203 ? 18.506 69.708 30.765 1.00 99.96 ? 203 LYS A N 1 ATOM 1582 C CA . LYS A 1 203 ? 17.446 69.992 31.723 1.00 112.21 ? 203 LYS A CA 1 ATOM 1583 C C . LYS A 1 203 ? 16.363 70.851 31.088 1.00 105.58 ? 203 LYS A C 1 ATOM 1584 O O . LYS A 1 203 ? 16.617 71.983 30.676 1.00 104.89 ? 203 LYS A O 1 ATOM 1585 C CB . LYS A 1 203 ? 18.006 70.695 32.959 1.00 112.52 ? 203 LYS A CB 1 ATOM 1586 C CG . LYS A 1 203 ? 16.934 71.193 33.914 1.00 103.65 ? 203 LYS A CG 1 ATOM 1587 C CD . LYS A 1 203 ? 17.538 71.938 35.090 1.00 124.35 ? 203 LYS A CD 1 ATOM 1588 C CE . LYS A 1 203 ? 16.456 72.472 36.013 1.00 132.83 ? 203 LYS A CE 1 ATOM 1589 N NZ . LYS A 1 203 ? 17.024 73.268 37.136 1.00 123.94 ? 203 LYS A NZ 1 ATOM 1590 N N . TYR A 1 204 ? 15.152 70.312 31.020 1.00 105.10 ? 204 TYR A N 1 ATOM 1591 C CA . TYR A 1 204 ? 14.043 71.026 30.406 1.00 102.07 ? 204 TYR A CA 1 ATOM 1592 C C . TYR A 1 204 ? 13.168 71.688 31.461 1.00 106.84 ? 204 TYR A C 1 ATOM 1593 O O . TYR A 1 204 ? 12.797 71.067 32.457 1.00 105.79 ? 204 TYR A O 1 ATOM 1594 C CB . TYR A 1 204 ? 13.206 70.078 29.542 1.00 84.12 ? 204 TYR A CB 1 ATOM 1595 C CG . TYR A 1 204 ? 13.965 69.498 28.368 1.00 84.26 ? 204 TYR A CG 1 ATOM 1596 C CD1 . TYR A 1 204 ? 14.105 70.214 27.187 1.00 86.06 ? 204 TYR A CD1 1 ATOM 1597 C CD2 . TYR A 1 204 ? 14.544 68.238 28.442 1.00 67.93 ? 204 TYR A CD2 1 ATOM 1598 C CE1 . TYR A 1 204 ? 14.801 69.692 26.112 1.00 84.70 ? 204 TYR A CE1 1 ATOM 1599 C CE2 . TYR A 1 204 ? 15.242 67.708 27.372 1.00 70.08 ? 204 TYR A CE2 1 ATOM 1600 C CZ . TYR A 1 204 ? 15.366 68.440 26.209 1.00 88.55 ? 204 TYR A CZ 1 ATOM 1601 O OH . TYR A 1 204 ? 16.057 67.921 25.138 1.00 96.63 ? 204 TYR A OH 1 ATOM 1602 N N . ASN A 1 205 ? 12.851 72.959 31.243 1.00 99.72 ? 205 ASN A N 1 ATOM 1603 C CA . ASN A 1 205 ? 11.909 73.653 32.104 1.00 87.07 ? 205 ASN A CA 1 ATOM 1604 C C . ASN A 1 205 ? 10.506 73.117 31.866 1.00 104.55 ? 205 ASN A C 1 ATOM 1605 O O . ASN A 1 205 ? 10.159 72.748 30.742 1.00 119.31 ? 205 ASN A O 1 ATOM 1606 C CB . ASN A 1 205 ? 11.960 75.160 31.861 1.00 101.79 ? 205 ASN A CB 1 ATOM 1607 C CG . ASN A 1 205 ? 13.305 75.762 32.215 1.00 129.43 ? 205 ASN A CG 1 ATOM 1608 O OD1 . ASN A 1 205 ? 13.990 75.288 33.122 1.00 128.18 ? 205 ASN A OD1 1 ATOM 1609 N ND2 . ASN A 1 205 ? 13.691 76.812 31.500 1.00 136.49 ? 205 ASN A ND2 1 ATOM 1610 N N . ASN A 1 206 ? 9.710 73.075 32.929 1.00 93.74 ? 206 ASN A N 1 ATOM 1611 C CA . ASN A 1 206 ? 8.366 72.504 32.885 1.00 94.69 ? 206 ASN A CA 1 ATOM 1612 C C . ASN A 1 206 ? 8.365 71.071 32.375 1.00 80.31 ? 206 ASN A C 1 ATOM 1613 O O . ASN A 1 206 ? 7.576 70.722 31.500 1.00 99.18 ? 206 ASN A O 1 ATOM 1614 C CB . ASN A 1 206 ? 7.435 73.348 32.011 1.00 94.43 ? 206 ASN A CB 1 ATOM 1615 C CG . ASN A 1 206 ? 7.671 74.831 32.170 1.00 98.20 ? 206 ASN A CG 1 ATOM 1616 O OD1 . ASN A 1 206 ? 7.905 75.536 31.190 1.00 90.34 ? 206 ASN A OD1 1 ATOM 1617 N ND2 . ASN A 1 206 ? 7.612 75.316 33.406 1.00 103.83 ? 206 ASN A ND2 1 ATOM 1618 N N . GLN A 1 207 ? 9.258 70.245 32.910 1.00 94.23 ? 207 GLN A N 1 ATOM 1619 C CA . GLN A 1 207 ? 9.257 68.829 32.571 1.00 73.30 ? 207 GLN A CA 1 ATOM 1620 C C . GLN A 1 207 ? 8.432 68.059 33.585 1.00 85.44 ? 207 GLN A C 1 ATOM 1621 O O . GLN A 1 207 ? 8.709 68.098 34.783 1.00 106.57 ? 207 GLN A O 1 ATOM 1622 C CB . GLN A 1 207 ? 10.675 68.258 32.518 1.00 71.63 ? 207 GLN A CB 1 ATOM 1623 C CG . GLN A 1 207 ? 10.712 66.813 32.032 1.00 85.99 ? 207 GLN A CG 1 ATOM 1624 C CD . GLN A 1 207 ? 12.048 66.133 32.266 1.00 90.54 ? 207 GLN A CD 1 ATOM 1625 O OE1 . GLN A 1 207 ? 12.488 65.980 33.406 1.00 90.05 ? 207 GLN A OE1 1 ATOM 1626 N NE2 . GLN A 1 207 ? 12.697 65.713 31.184 1.00 75.52 ? 207 GLN A NE2 1 ATOM 1627 N N . LEU A 1 208 ? 7.413 67.364 33.097 1.00 82.73 ? 208 LEU A N 1 ATOM 1628 C CA . LEU A 1 208 ? 6.582 66.529 33.949 1.00 73.79 ? 208 LEU A CA 1 ATOM 1629 C C . LEU A 1 208 ? 7.069 65.090 33.903 1.00 84.06 ? 208 LEU A C 1 ATOM 1630 O O . LEU A 1 208 ? 7.216 64.510 32.827 1.00 97.69 ? 208 LEU A O 1 ATOM 1631 C CB . LEU A 1 208 ? 5.121 66.616 33.515 1.00 91.83 ? 208 LEU A CB 1 ATOM 1632 C CG . LEU A 1 208 ? 4.483 67.993 33.692 1.00 72.34 ? 208 LEU A CG 1 ATOM 1633 C CD1 . LEU A 1 208 ? 3.130 68.040 33.008 1.00 84.56 ? 208 LEU A CD1 1 ATOM 1634 C CD2 . LEU A 1 208 ? 4.354 68.312 35.168 1.00 74.94 ? 208 LEU A CD2 1 ATOM 1635 N N . ALA A 1 209 ? 7.328 64.515 35.073 1.00 86.48 ? 209 ALA A N 1 ATOM 1636 C CA . ALA A 1 209 ? 7.847 63.156 35.140 1.00 82.15 ? 209 ALA A CA 1 ATOM 1637 C C . ALA A 1 209 ? 7.397 62.422 36.398 1.00 77.75 ? 209 ALA A C 1 ATOM 1638 O O . ALA A 1 209 ? 7.250 63.027 37.459 1.00 80.68 ? 209 ALA A O 1 ATOM 1639 C CB . ALA A 1 209 ? 9.364 63.176 35.059 1.00 64.38 ? 209 ALA A CB 1 ATOM 1640 N N . THR A 1 210 ? 7.176 61.117 36.271 1.00 72.68 ? 210 THR A N 1 ATOM 1641 C CA . THR A 1 210 ? 6.923 60.274 37.432 1.00 67.80 ? 210 THR A CA 1 ATOM 1642 C C . THR A 1 210 ? 8.237 60.007 38.150 1.00 75.00 ? 210 THR A C 1 ATOM 1643 O O . THR A 1 210 ? 9.304 60.053 37.540 1.00 87.71 ? 210 THR A O 1 ATOM 1644 C CB . THR A 1 210 ? 6.264 58.938 37.049 1.00 72.33 ? 210 THR A CB 1 ATOM 1645 O OG1 . THR A 1 210 ? 7.167 58.161 36.250 1.00 70.79 ? 210 THR A OG1 1 ATOM 1646 C CG2 . THR A 1 210 ? 4.980 59.185 36.273 1.00 86.29 ? 210 THR A CG2 1 ATOM 1647 N N . ARG A 1 211 ? 8.158 59.717 39.443 1.00 86.38 ? 211 ARG A N 1 ATOM 1648 C CA . ARG A 1 211 ? 9.352 59.568 40.264 1.00 95.21 ? 211 ARG A CA 1 ATOM 1649 C C . ARG A 1 211 ? 9.464 58.141 40.788 1.00 96.86 ? 211 ARG A C 1 ATOM 1650 O O . ARG A 1 211 ? 8.470 57.418 40.848 1.00 108.12 ? 211 ARG A O 1 ATOM 1651 C CB . ARG A 1 211 ? 9.329 60.566 41.427 1.00 107.43 ? 211 ARG A CB 1 ATOM 1652 C CG . ARG A 1 211 ? 10.693 60.859 42.034 1.00 118.89 ? 211 ARG A CG 1 ATOM 1653 C CD . ARG A 1 211 ? 10.573 61.737 43.272 1.00 129.91 ? 211 ARG A CD 1 ATOM 1654 N NE . ARG A 1 211 ? 11.879 62.162 43.771 1.00 136.07 ? 211 ARG A NE 1 ATOM 1655 C CZ . ARG A 1 211 ? 12.064 62.853 44.892 1.00 145.88 ? 211 ARG A CZ 1 ATOM 1656 N NH1 . ARG A 1 211 ? 11.026 63.197 45.642 1.00 143.96 ? 211 ARG A NH1 1 ATOM 1657 N NH2 . ARG A 1 211 ? 13.289 63.196 45.266 1.00 142.53 ? 211 ARG A NH2 1 ATOM 1658 N N . THR A 1 212 ? 10.680 57.742 41.154 1.00 87.19 ? 212 THR A N 1 ATOM 1659 C CA . THR A 1 212 ? 10.939 56.399 41.661 1.00 82.13 ? 212 THR A CA 1 ATOM 1660 C C . THR A 1 212 ? 10.067 56.075 42.876 1.00 93.41 ? 212 THR A C 1 ATOM 1661 O O . THR A 1 212 ? 9.712 56.958 43.657 1.00 94.63 ? 212 THR A O 1 ATOM 1662 C CB . THR A 1 212 ? 12.427 56.217 42.034 1.00 81.29 ? 212 THR A CB 1 ATOM 1663 O OG1 . THR A 1 212 ? 12.668 54.858 42.422 1.00 86.63 ? 212 THR A OG1 1 ATOM 1664 C CG2 . THR A 1 212 ? 12.815 57.140 43.176 1.00 80.11 ? 212 THR A CG2 1 ATOM 1665 N N . ALA A 1 213 ? 9.713 54.801 43.011 1.00 99.08 ? 213 ALA A N 1 ATOM 1666 C CA . ALA A 1 213 ? 8.820 54.349 44.073 1.00 86.42 ? 213 ALA A CA 1 ATOM 1667 C C . ALA A 1 213 ? 9.466 53.236 44.884 1.00 86.69 ? 213 ALA A C 1 ATOM 1668 O O . ALA A 1 213 ? 10.644 52.932 44.702 1.00 90.50 ? 213 ALA A O 1 ATOM 1669 C CB . ALA A 1 213 ? 7.497 53.879 43.492 1.00 98.44 ? 213 ALA A CB 1 ATOM 1670 N N . GLN A 1 214 ? 8.695 52.639 45.788 1.00 93.99 ? 214 GLN A N 1 ATOM 1671 C CA . GLN A 1 214 ? 9.187 51.534 46.603 1.00 104.03 ? 214 GLN A CA 1 ATOM 1672 C C . GLN A 1 214 ? 9.569 50.349 45.719 1.00 107.43 ? 214 GLN A C 1 ATOM 1673 O O . GLN A 1 214 ? 9.026 50.176 44.626 1.00 108.40 ? 214 GLN A O 1 ATOM 1674 C CB . GLN A 1 214 ? 8.140 51.108 47.636 1.00 111.29 ? 214 GLN A CB 1 ATOM 1675 C CG . GLN A 1 214 ? 7.808 52.168 48.680 1.00 108.16 ? 214 GLN A CG 1 ATOM 1676 C CD . GLN A 1 214 ? 6.789 53.183 48.194 1.00 103.45 ? 214 GLN A CD 1 ATOM 1677 O OE1 . GLN A 1 214 ? 6.411 53.192 47.021 1.00 96.67 ? 214 GLN A OE1 1 ATOM 1678 N NE2 . GLN A 1 214 ? 6.335 54.043 49.099 1.00 109.02 ? 214 GLN A NE2 1 ATOM 1679 N N . ALA A 1 215 ? 10.507 49.538 46.200 1.00 105.39 ? 215 ALA A N 1 ATOM 1680 C CA . ALA A 1 215 ? 11.051 48.429 45.420 1.00 104.41 ? 215 ALA A CA 1 ATOM 1681 C C . ALA A 1 215 ? 10.011 47.354 45.105 1.00 101.49 ? 215 ALA A C 1 ATOM 1682 O O . ALA A 1 215 ? 10.233 46.499 44.248 1.00 96.75 ? 215 ALA A O 1 ATOM 1683 C CB . ALA A 1 215 ? 12.232 47.812 46.150 1.00 101.08 ? 215 ALA A CB 1 ATOM 1684 N N . ILE A 1 216 ? 8.877 47.401 45.795 1.00 95.53 ? 216 ILE A N 1 ATOM 1685 C CA . ILE A 1 216 ? 7.807 46.438 45.565 1.00 86.98 ? 216 ILE A CA 1 ATOM 1686 C C . ILE A 1 216 ? 7.154 46.670 44.201 1.00 78.64 ? 216 ILE A C 1 ATOM 1687 O O . ILE A 1 216 ? 6.472 45.795 43.668 1.00 82.90 ? 216 ILE A O 1 ATOM 1688 C CB . ILE A 1 216 ? 6.744 46.507 46.687 1.00 83.63 ? 216 ILE A CB 1 ATOM 1689 C CG1 . ILE A 1 216 ? 5.852 45.261 46.672 1.00 101.89 ? 216 ILE A CG1 1 ATOM 1690 C CG2 . ILE A 1 216 ? 5.928 47.788 46.583 1.00 84.17 ? 216 ILE A CG2 1 ATOM 1691 C CD1 . ILE A 1 216 ? 4.850 45.209 47.808 1.00 104.76 ? 216 ILE A CD1 1 ATOM 1692 N N . PHE A 1 217 ? 7.380 47.850 43.633 1.00 85.57 ? 217 PHE A N 1 ATOM 1693 C CA . PHE A 1 217 ? 6.837 48.193 42.323 1.00 74.72 ? 217 PHE A CA 1 ATOM 1694 C C . PHE A 1 217 ? 7.804 47.850 41.193 1.00 84.29 ? 217 PHE A C 1 ATOM 1695 O O . PHE A 1 217 ? 7.545 48.172 40.033 1.00 73.59 ? 217 PHE A O 1 ATOM 1696 C CB . PHE A 1 217 ? 6.481 49.678 42.262 1.00 76.15 ? 217 PHE A CB 1 ATOM 1697 C CG . PHE A 1 217 ? 5.332 50.066 43.148 1.00 83.62 ? 217 PHE A CG 1 ATOM 1698 C CD1 . PHE A 1 217 ? 4.024 49.907 42.718 1.00 79.55 ? 217 PHE A CD1 1 ATOM 1699 C CD2 . PHE A 1 217 ? 5.558 50.602 44.405 1.00 91.26 ? 217 PHE A CD2 1 ATOM 1700 C CE1 . PHE A 1 217 ? 2.962 50.268 43.528 1.00 81.73 ? 217 PHE A CE1 1 ATOM 1701 C CE2 . PHE A 1 217 ? 4.501 50.964 45.220 1.00 84.65 ? 217 PHE A CE2 1 ATOM 1702 C CZ . PHE A 1 217 ? 3.201 50.797 44.780 1.00 84.60 ? 217 PHE A CZ 1 ATOM 1703 N N . ASP A 1 218 ? 8.922 47.216 41.536 1.00 81.16 ? 218 ASP A N 1 ATOM 1704 C CA . ASP A 1 218 ? 9.915 46.820 40.540 1.00 74.14 ? 218 ASP A CA 1 ATOM 1705 C C . ASP A 1 218 ? 9.313 45.920 39.468 1.00 73.56 ? 218 ASP A C 1 ATOM 1706 O O . ASP A 1 218 ? 8.397 45.142 39.740 1.00 86.76 ? 218 ASP A O 1 ATOM 1707 C CB . ASP A 1 218 ? 11.098 46.105 41.199 1.00 91.00 ? 218 ASP A CB 1 ATOM 1708 C CG . ASP A 1 218 ? 12.091 47.064 41.824 1.00 83.39 ? 218 ASP A CG 1 ATOM 1709 O OD1 . ASP A 1 218 ? 12.005 48.278 41.549 1.00 80.99 ? 218 ASP A OD1 1 ATOM 1710 O OD2 . ASP A 1 218 ? 12.969 46.598 42.580 1.00 100.41 ? 218 ASP A OD2 1 ATOM 1711 N N . ASP A 1 219 ? 9.834 46.048 38.252 1.00 76.99 ? 219 ASP A N 1 ATOM 1712 C CA . ASP A 1 219 ? 9.426 45.220 37.121 1.00 74.58 ? 219 ASP A CA 1 ATOM 1713 C C . ASP A 1 219 ? 7.942 45.367 36.808 1.00 81.37 ? 219 ASP A C 1 ATOM 1714 O O . ASP A 1 219 ? 7.275 44.391 36.474 1.00 74.42 ? 219 ASP A O 1 ATOM 1715 C CB . ASP A 1 219 ? 9.769 43.752 37.384 1.00 61.73 ? 219 ASP A CB 1 ATOM 1716 C CG . ASP A 1 219 ? 11.222 43.556 37.761 1.00 71.14 ? 219 ASP A CG 1 ATOM 1717 O OD1 . ASP A 1 219 ? 12.090 43.701 36.874 1.00 85.00 ? 219 ASP A OD1 1 ATOM 1718 O OD2 . ASP A 1 219 ? 11.500 43.246 38.939 1.00 72.93 ? 219 ASP A OD2 1 ATOM 1719 N N . SER A 1 220 ? 7.426 46.584 36.953 1.00 68.77 ? 220 SER A N 1 ATOM 1720 C CA . SER A 1 220 ? 6.054 46.897 36.563 1.00 67.17 ? 220 SER A CA 1 ATOM 1721 C C . SER A 1 220 ? 5.930 47.201 35.069 1.00 70.97 ? 220 SER A C 1 ATOM 1722 O O . SER A 1 220 ? 4.896 46.932 34.455 1.00 75.42 ? 220 SER A O 1 ATOM 1723 C CB . SER A 1 220 ? 5.527 48.076 37.381 1.00 79.48 ? 220 SER A CB 1 ATOM 1724 O OG . SER A 1 220 ? 5.452 47.747 38.757 1.00 114.12 ? 220 SER A OG 1 ATOM 1725 N N . TYR A 1 221 ? 6.996 47.763 34.503 1.00 74.72 ? 221 TYR A N 1 ATOM 1726 C CA . TYR A 1 221 ? 7.044 48.211 33.106 1.00 84.28 ? 221 TYR A CA 1 ATOM 1727 C C . TYR A 1 221 ? 6.033 49.318 32.790 1.00 67.14 ? 221 TYR A C 1 ATOM 1728 O O . TYR A 1 221 ? 5.325 49.249 31.783 1.00 60.78 ? 221 TYR A O 1 ATOM 1729 C CB . TYR A 1 221 ? 6.821 47.040 32.136 1.00 70.24 ? 221 TYR A CB 1 ATOM 1730 C CG . TYR A 1 221 ? 7.891 45.968 32.146 1.00 61.26 ? 221 TYR A CG 1 ATOM 1731 C CD1 . TYR A 1 221 ? 9.059 46.117 32.882 1.00 59.76 ? 221 TYR A CD1 1 ATOM 1732 C CD2 . TYR A 1 221 ? 7.729 44.803 31.409 1.00 62.23 ? 221 TYR A CD2 1 ATOM 1733 C CE1 . TYR A 1 221 ? 10.030 45.131 32.887 1.00 86.02 ? 221 TYR A CE1 1 ATOM 1734 C CE2 . TYR A 1 221 ? 8.693 43.814 31.407 1.00 67.92 ? 221 TYR A CE2 1 ATOM 1735 C CZ . TYR A 1 221 ? 9.841 43.980 32.146 1.00 89.82 ? 221 TYR A CZ 1 ATOM 1736 O OH . TYR A 1 221 ? 10.801 42.992 32.141 1.00 89.52 ? 221 TYR A OH 1 ATOM 1737 N N . LEU A 1 222 ? 5.972 50.339 33.641 1.00 55.08 ? 222 LEU A N 1 ATOM 1738 C CA . LEU A 1 222 ? 5.197 51.539 33.328 1.00 60.28 ? 222 LEU A CA 1 ATOM 1739 C C . LEU A 1 222 ? 5.754 52.220 32.080 1.00 67.17 ? 222 LEU A C 1 ATOM 1740 O O . LEU A 1 222 ? 6.967 52.272 31.887 1.00 65.88 ? 222 LEU A O 1 ATOM 1741 C CB . LEU A 1 222 ? 5.204 52.517 34.507 1.00 62.98 ? 222 LEU A CB 1 ATOM 1742 C CG . LEU A 1 222 ? 4.764 53.963 34.239 1.00 65.11 ? 222 LEU A CG 1 ATOM 1743 C CD1 . LEU A 1 222 ? 3.300 54.042 33.827 1.00 61.18 ? 222 LEU A CD1 1 ATOM 1744 C CD2 . LEU A 1 222 ? 5.023 54.842 35.451 1.00 71.77 ? 222 LEU A CD2 1 ATOM 1745 N N . GLY A 1 223 ? 4.870 52.737 31.234 1.00 64.79 ? 223 GLY A N 1 ATOM 1746 C CA . GLY A 1 223 ? 5.291 53.438 30.036 1.00 54.35 ? 223 GLY A CA 1 ATOM 1747 C C . GLY A 1 223 ? 5.425 52.493 28.862 1.00 63.31 ? 223 GLY A C 1 ATOM 1748 O O . GLY A 1 223 ? 6.004 52.833 27.831 1.00 74.12 ? 223 GLY A O 1 ATOM 1749 N N . TYR A 1 224 ? 4.888 51.291 29.032 1.00 68.77 ? 224 TYR A N 1 ATOM 1750 C CA . TYR A 1 224 ? 4.899 50.280 27.985 1.00 51.68 ? 224 TYR A CA 1 ATOM 1751 C C . TYR A 1 224 ? 4.064 50.747 26.795 1.00 50.01 ? 224 TYR A C 1 ATOM 1752 O O . TYR A 1 224 ? 4.383 50.456 25.642 1.00 52.56 ? 224 TYR A O 1 ATOM 1753 C CB . TYR A 1 224 ? 4.370 48.962 28.539 1.00 59.94 ? 224 TYR A CB 1 ATOM 1754 C CG . TYR A 1 224 ? 4.702 47.733 27.726 1.00 68.20 ? 224 TYR A CG 1 ATOM 1755 C CD1 . TYR A 1 224 ? 4.016 47.442 26.554 1.00 52.67 ? 224 TYR A CD1 1 ATOM 1756 C CD2 . TYR A 1 224 ? 5.675 46.842 28.155 1.00 69.41 ? 224 TYR A CD2 1 ATOM 1757 C CE1 . TYR A 1 224 ? 4.307 46.310 25.821 1.00 52.02 ? 224 TYR A CE1 1 ATOM 1758 C CE2 . TYR A 1 224 ? 5.971 45.707 27.431 1.00 50.56 ? 224 TYR A CE2 1 ATOM 1759 C CZ . TYR A 1 224 ? 5.283 45.445 26.267 1.00 58.57 ? 224 TYR A CZ 1 ATOM 1760 O OH . TYR A 1 224 ? 5.576 44.314 25.546 1.00 50.87 ? 224 TYR A OH 1 ATOM 1761 N N . SER A 1 225 ? 2.993 51.475 27.091 1.00 63.04 ? 225 SER A N 1 ATOM 1762 C CA . SER A 1 225 ? 2.140 52.072 26.071 1.00 71.16 ? 225 SER A CA 1 ATOM 1763 C C . SER A 1 225 ? 1.576 53.382 26.605 1.00 74.96 ? 225 SER A C 1 ATOM 1764 O O . SER A 1 225 ? 1.449 53.548 27.816 1.00 72.00 ? 225 SER A O 1 ATOM 1765 C CB . SER A 1 225 ? 1.013 51.119 25.681 1.00 77.86 ? 225 SER A CB 1 ATOM 1766 O OG . SER A 1 225 ? 0.279 50.714 26.825 1.00 67.96 ? 225 SER A OG 1 ATOM 1767 N N . VAL A 1 226 ? 1.251 54.318 25.717 1.00 65.84 ? 226 VAL A N 1 ATOM 1768 C CA . VAL A 1 226 ? 0.720 55.609 26.158 1.00 53.94 ? 226 VAL A CA 1 ATOM 1769 C C . VAL A 1 226 ? -0.417 56.131 25.281 1.00 54.57 ? 226 VAL A C 1 ATOM 1770 O O . VAL A 1 226 ? -0.507 55.822 24.092 1.00 69.38 ? 226 VAL A O 1 ATOM 1771 C CB . VAL A 1 226 ? 1.820 56.697 26.209 1.00 65.58 ? 226 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 226 ? 2.848 56.381 27.285 1.00 66.41 ? 226 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 226 ? 2.484 56.861 24.850 1.00 53.15 ? 226 VAL A CG2 1 ATOM 1774 N N . ALA A 1 227 ? -1.279 56.937 25.888 1.00 57.47 ? 227 ALA A N 1 ATOM 1775 C CA . ALA A 1 227 ? -2.412 57.538 25.199 1.00 64.50 ? 227 ALA A CA 1 ATOM 1776 C C . ALA A 1 227 ? -2.809 58.816 25.923 1.00 68.85 ? 227 ALA A C 1 ATOM 1777 O O . ALA A 1 227 ? -2.429 59.017 27.076 1.00 89.96 ? 227 ALA A O 1 ATOM 1778 C CB . ALA A 1 227 ? -3.577 56.565 25.135 1.00 76.30 ? 227 ALA A CB 1 ATOM 1779 N N . VAL A 1 228 ? -3.565 59.684 25.259 1.00 61.88 ? 228 VAL A N 1 ATOM 1780 C CA . VAL A 1 228 ? -3.924 60.962 25.866 1.00 64.56 ? 228 VAL A CA 1 ATOM 1781 C C . VAL A 1 228 ? -5.412 61.286 25.771 1.00 80.19 ? 228 VAL A C 1 ATOM 1782 O O . VAL A 1 228 ? -6.094 60.885 24.828 1.00 91.44 ? 228 VAL A O 1 ATOM 1783 C CB . VAL A 1 228 ? -3.132 62.113 25.237 1.00 63.87 ? 228 VAL A CB 1 ATOM 1784 C CG1 . VAL A 1 228 ? -1.664 62.023 25.636 1.00 62.06 ? 228 VAL A CG1 1 ATOM 1785 C CG2 . VAL A 1 228 ? -3.292 62.094 23.727 1.00 87.51 ? 228 VAL A CG2 1 ATOM 1786 N N . GLY A 1 229 ? -5.896 62.024 26.765 1.00 74.69 ? 229 GLY A N 1 ATOM 1787 C CA . GLY A 1 229 ? -7.293 62.408 26.865 1.00 74.02 ? 229 GLY A CA 1 ATOM 1788 C C . GLY A 1 229 ? -7.484 63.196 28.146 1.00 76.32 ? 229 GLY A C 1 ATOM 1789 O O . GLY A 1 229 ? -6.554 63.298 28.940 1.00 77.38 ? 229 GLY A O 1 ATOM 1790 N N . ASP A 1 230 ? -8.690 63.732 28.292 1.00 80.55 ? 230 ASP A N 1 ATOM 1791 C CA . ASP A 1 230 ? -9.078 64.605 29.380 1.00 85.53 ? 230 ASP A CA 1 ATOM 1792 C C . ASP A 1 230 ? -10.133 63.891 30.204 1.00 92.21 ? 230 ASP A C 1 ATOM 1793 O O . ASP A 1 230 ? -11.280 63.779 29.771 1.00 101.90 ? 230 ASP A O 1 ATOM 1794 C CB . ASP A 1 230 ? -9.689 65.872 28.786 1.00 86.01 ? 230 ASP A CB 1 ATOM 1795 C CG . ASP A 1 230 ? -9.771 66.993 29.780 1.00 92.76 ? 230 ASP A CG 1 ATOM 1796 O OD1 . ASP A 1 230 ? -8.989 66.958 30.742 1.00 88.32 ? 230 ASP A OD1 1 ATOM 1797 O OD2 . ASP A 1 230 ? -10.610 67.902 29.603 1.00 96.86 ? 230 ASP A OD2 1 ATOM 1798 N N . PHE A 1 231 ? -9.710 63.476 31.379 1.00 92.20 ? 231 PHE A N 1 ATOM 1799 C CA . PHE A 1 231 ? -10.527 62.699 32.255 1.00 106.51 ? 231 PHE A CA 1 ATOM 1800 C C . PHE A 1 231 ? -10.833 63.529 33.455 1.00 107.41 ? 231 PHE A C 1 ATOM 1801 O O . PHE A 1 231 ? -11.152 63.037 34.524 1.00 115.35 ? 231 PHE A O 1 ATOM 1802 C CB . PHE A 1 231 ? -9.767 61.460 32.621 1.00 93.33 ? 231 PHE A CB 1 ATOM 1803 C CG . PHE A 1 231 ? -9.258 60.736 31.437 1.00 89.49 ? 231 PHE A CG 1 ATOM 1804 C CD1 . PHE A 1 231 ? -10.126 60.102 30.599 1.00 101.27 ? 231 PHE A CD1 1 ATOM 1805 C CD2 . PHE A 1 231 ? -7.932 60.730 31.143 1.00 86.48 ? 231 PHE A CD2 1 ATOM 1806 C CE1 . PHE A 1 231 ? -9.678 59.441 29.493 1.00 106.48 ? 231 PHE A CE1 1 ATOM 1807 C CE2 . PHE A 1 231 ? -7.468 60.071 30.039 1.00 89.54 ? 231 PHE A CE2 1 ATOM 1808 C CZ . PHE A 1 231 ? -8.343 59.427 29.211 1.00 106.66 ? 231 PHE A CZ 1 ATOM 1809 N N . ASN A 1 232 ? -10.738 64.820 33.244 1.00 102.46 ? 232 ASN A N 1 ATOM 1810 C CA . ASN A 1 232 ? -11.171 65.803 34.233 1.00 119.38 ? 232 ASN A CA 1 ATOM 1811 C C . ASN A 1 232 ? -11.459 67.134 33.547 1.00 112.76 ? 232 ASN A C 1 ATOM 1812 O O . ASN A 1 232 ? -11.056 67.349 32.408 1.00 126.65 ? 232 ASN A O 1 ATOM 1813 C CB . ASN A 1 232 ? -10.136 65.975 35.351 1.00 114.20 ? 232 ASN A CB 1 ATOM 1814 C CG . ASN A 1 232 ? -8.760 66.338 34.834 1.00 97.69 ? 232 ASN A CG 1 ATOM 1815 O OD1 . ASN A 1 232 ? -8.553 66.490 33.632 1.00 101.98 ? 232 ASN A OD1 1 ATOM 1816 N ND2 . ASN A 1 232 ? -7.807 66.484 35.748 1.00 92.28 ? 232 ASN A ND2 1 ATOM 1817 N N . GLY A 1 233 ? -12.157 68.026 34.238 1.00 101.22 ? 233 GLY A N 1 ATOM 1818 C CA . GLY A 1 233 ? -12.675 69.228 33.609 1.00 107.50 ? 233 GLY A CA 1 ATOM 1819 C C . GLY A 1 233 ? -11.668 70.275 33.163 1.00 134.78 ? 233 GLY A C 1 ATOM 1820 O O . GLY A 1 233 ? -12.066 71.324 32.656 1.00 159.04 ? 233 GLY A O 1 ATOM 1821 N N . ASP A 1 234 ? -10.376 70.005 33.342 1.00 122.50 ? 234 ASP A N 1 ATOM 1822 C CA . ASP A 1 234 ? -9.345 71.011 33.074 1.00 100.95 ? 234 ASP A CA 1 ATOM 1823 C C . ASP A 1 234 ? -9.308 71.449 31.610 1.00 95.29 ? 234 ASP A C 1 ATOM 1824 O O . ASP A 1 234 ? -9.099 72.625 31.314 1.00 116.95 ? 234 ASP A O 1 ATOM 1825 C CB . ASP A 1 234 ? -7.962 70.499 33.502 1.00 98.56 ? 234 ASP A CB 1 ATOM 1826 C CG . ASP A 1 234 ? -7.609 69.157 32.884 1.00 129.46 ? 234 ASP A CG 1 ATOM 1827 O OD1 . ASP A 1 234 ? -8.142 68.827 31.804 1.00 138.86 ? 234 ASP A OD1 1 ATOM 1828 O OD2 . ASP A 1 234 ? -6.786 68.432 33.481 1.00 134.43 ? 234 ASP A OD2 1 ATOM 1829 N N . GLY A 1 235 ? -9.513 70.504 30.700 1.00 92.92 ? 235 GLY A N 1 ATOM 1830 C CA . GLY A 1 235 ? -9.498 70.810 29.282 1.00 91.84 ? 235 GLY A CA 1 ATOM 1831 C C . GLY A 1 235 ? -8.233 70.352 28.581 1.00 98.81 ? 235 GLY A C 1 ATOM 1832 O O . GLY A 1 235 ? -8.196 70.258 27.355 1.00 114.55 ? 235 GLY A O 1 ATOM 1833 N N . ILE A 1 236 ? -7.193 70.065 29.359 1.00 98.29 ? 236 ILE A N 1 ATOM 1834 C CA . ILE A 1 236 ? -5.920 69.621 28.799 1.00 100.53 ? 236 ILE A CA 1 ATOM 1835 C C . ILE A 1 236 ? -5.822 68.098 28.768 1.00 92.00 ? 236 ILE A C 1 ATOM 1836 O O . ILE A 1 236 ? -6.232 67.424 29.715 1.00 85.97 ? 236 ILE A O 1 ATOM 1837 C CB . ILE A 1 236 ? -4.729 70.177 29.599 1.00 98.13 ? 236 ILE A CB 1 ATOM 1838 C CG1 . ILE A 1 236 ? -4.929 71.664 29.893 1.00 107.09 ? 236 ILE A CG1 1 ATOM 1839 C CG2 . ILE A 1 236 ? -3.424 69.938 28.850 1.00 96.84 ? 236 ILE A CG2 1 ATOM 1840 C CD1 . ILE A 1 236 ? -3.803 72.282 30.692 1.00 125.28 ? 236 ILE A CD1 1 ATOM 1841 N N . ASP A 1 237 ? -5.281 67.569 27.673 1.00 95.98 ? 237 ASP A N 1 ATOM 1842 C CA . ASP A 1 237 ? -5.041 66.135 27.540 1.00 88.56 ? 237 ASP A CA 1 ATOM 1843 C C . ASP A 1 237 ? -4.145 65.625 28.664 1.00 92.06 ? 237 ASP A C 1 ATOM 1844 O O . ASP A 1 237 ? -3.111 66.220 28.973 1.00 90.33 ? 237 ASP A O 1 ATOM 1845 C CB . ASP A 1 237 ? -4.415 65.813 26.179 1.00 86.77 ? 237 ASP A CB 1 ATOM 1846 C CG . ASP A 1 237 ? -5.430 65.824 25.053 1.00 111.64 ? 237 ASP A CG 1 ATOM 1847 O OD1 . ASP A 1 237 ? -6.477 66.492 25.197 1.00 126.92 ? 237 ASP A OD1 1 ATOM 1848 O OD2 . ASP A 1 237 ? -5.182 65.163 24.023 1.00 116.13 ? 237 ASP A OD2 1 ATOM 1849 N N . ASP A 1 238 ? -4.567 64.528 29.286 1.00 95.10 ? 238 ASP A N 1 ATOM 1850 C CA . ASP A 1 238 ? -3.853 63.963 30.423 1.00 79.61 ? 238 ASP A CA 1 ATOM 1851 C C . ASP A 1 238 ? -3.253 62.625 30.026 1.00 79.66 ? 238 ASP A C 1 ATOM 1852 O O . ASP A 1 238 ? -3.432 62.171 28.896 1.00 91.42 ? 238 ASP A O 1 ATOM 1853 C CB . ASP A 1 238 ? -4.790 63.818 31.623 1.00 82.30 ? 238 ASP A CB 1 ATOM 1854 C CG . ASP A 1 238 ? -5.641 65.055 31.836 1.00 114.72 ? 238 ASP A CG 1 ATOM 1855 O OD1 . ASP A 1 238 ? -6.853 64.887 32.074 1.00 150.88 ? 238 ASP A OD1 1 ATOM 1856 O OD2 . ASP A 1 238 ? -5.119 66.188 31.776 1.00 109.09 ? 238 ASP A OD2 1 ATOM 1857 N N . PHE A 1 239 ? -2.547 61.990 30.952 1.00 76.23 ? 239 PHE A N 1 ATOM 1858 C CA . PHE A 1 239 ? -1.683 60.876 30.584 1.00 72.78 ? 239 PHE A CA 1 ATOM 1859 C C . PHE A 1 239 ? -2.260 59.520 30.953 1.00 71.02 ? 239 PHE A C 1 ATOM 1860 O O . PHE A 1 239 ? -2.659 59.288 32.092 1.00 79.19 ? 239 PHE A O 1 ATOM 1861 C CB . PHE A 1 239 ? -0.313 61.056 31.232 1.00 79.82 ? 239 PHE A CB 1 ATOM 1862 C CG . PHE A 1 239 ? 0.315 62.388 30.938 1.00 73.75 ? 239 PHE A CG 1 ATOM 1863 C CD1 . PHE A 1 239 ? 0.179 62.968 29.688 1.00 66.32 ? 239 PHE A CD1 1 ATOM 1864 C CD2 . PHE A 1 239 ? 1.023 63.068 31.914 1.00 74.11 ? 239 PHE A CD2 1 ATOM 1865 C CE1 . PHE A 1 239 ? 0.747 64.192 29.413 1.00 77.39 ? 239 PHE A CE1 1 ATOM 1866 C CE2 . PHE A 1 239 ? 1.594 64.294 31.645 1.00 90.01 ? 239 PHE A CE2 1 ATOM 1867 C CZ . PHE A 1 239 ? 1.453 64.858 30.392 1.00 102.11 ? 239 PHE A CZ 1 ATOM 1868 N N . VAL A 1 240 ? -2.299 58.631 29.965 1.00 68.32 ? 240 VAL A N 1 ATOM 1869 C CA . VAL A 1 240 ? -2.739 57.258 30.165 1.00 65.68 ? 240 VAL A CA 1 ATOM 1870 C C . VAL A 1 240 ? -1.635 56.296 29.739 1.00 78.56 ? 240 VAL A C 1 ATOM 1871 O O . VAL A 1 240 ? -1.120 56.389 28.625 1.00 69.98 ? 240 VAL A O 1 ATOM 1872 C CB . VAL A 1 240 ? -4.023 56.954 29.374 1.00 64.29 ? 240 VAL A CB 1 ATOM 1873 C CG1 . VAL A 1 240 ? -4.383 55.483 29.489 1.00 63.64 ? 240 VAL A CG1 1 ATOM 1874 C CG2 . VAL A 1 240 ? -5.162 57.820 29.871 1.00 81.43 ? 240 VAL A CG2 1 ATOM 1875 N N . SER A 1 241 ? -1.267 55.380 30.630 1.00 69.91 ? 241 SER A N 1 ATOM 1876 C CA . SER A 1 241 ? -0.201 54.431 30.335 1.00 62.66 ? 241 SER A CA 1 ATOM 1877 C C . SER A 1 241 ? -0.499 53.033 30.860 1.00 71.31 ? 241 SER A C 1 ATOM 1878 O O . SER A 1 241 ? -0.987 52.868 31.980 1.00 66.44 ? 241 SER A O 1 ATOM 1879 C CB . SER A 1 241 ? 1.125 54.922 30.916 1.00 67.12 ? 241 SER A CB 1 ATOM 1880 O OG . SER A 1 241 ? 2.159 53.986 30.666 1.00 84.99 ? 241 SER A OG 1 ATOM 1881 N N . GLY A 1 242 ? -0.208 52.028 30.040 1.00 75.74 ? 242 GLY A N 1 ATOM 1882 C CA . GLY A 1 242 ? -0.336 50.645 30.457 1.00 86.45 ? 242 GLY A CA 1 ATOM 1883 C C . GLY A 1 242 ? 0.830 50.210 31.325 1.00 83.12 ? 242 GLY A C 1 ATOM 1884 O O . GLY A 1 242 ? 1.975 50.595 31.084 1.00 91.69 ? 242 GLY A O 1 ATOM 1885 N N . VAL A 1 243 ? 0.539 49.413 32.347 1.00 65.43 ? 243 VAL A N 1 ATOM 1886 C CA . VAL A 1 243 ? 1.577 48.867 33.215 1.00 69.85 ? 243 VAL A CA 1 ATOM 1887 C C . VAL A 1 243 ? 1.360 47.362 33.352 1.00 61.79 ? 243 VAL A C 1 ATOM 1888 O O . VAL A 1 243 ? 0.852 46.893 34.370 1.00 61.53 ? 243 VAL A O 1 ATOM 1889 C CB . VAL A 1 243 ? 1.574 49.527 34.611 1.00 75.80 ? 243 VAL A CB 1 ATOM 1890 C CG1 . VAL A 1 243 ? 2.956 49.451 35.226 1.00 81.53 ? 243 VAL A CG1 1 ATOM 1891 C CG2 . VAL A 1 243 ? 1.124 50.976 34.525 1.00 64.27 ? 243 VAL A CG2 1 ATOM 1892 N N . PRO A 1 244 ? 1.749 46.604 32.316 1.00 57.84 ? 244 PRO A N 1 ATOM 1893 C CA . PRO A 1 244 ? 1.382 45.194 32.123 1.00 64.99 ? 244 PRO A CA 1 ATOM 1894 C C . PRO A 1 244 ? 1.817 44.242 33.232 1.00 61.66 ? 244 PRO A C 1 ATOM 1895 O O . PRO A 1 244 ? 1.097 43.286 33.512 1.00 96.29 ? 244 PRO A O 1 ATOM 1896 C CB . PRO A 1 244 ? 2.081 44.829 30.809 1.00 61.28 ? 244 PRO A CB 1 ATOM 1897 C CG . PRO A 1 244 ? 3.161 45.842 30.644 1.00 69.23 ? 244 PRO A CG 1 ATOM 1898 C CD . PRO A 1 244 ? 2.617 47.098 31.235 1.00 53.01 ? 244 PRO A CD 1 ATOM 1899 N N . ARG A 1 245 ? 2.970 44.481 33.844 1.00 59.05 ? 245 ARG A N 1 ATOM 1900 C CA . ARG A 1 245 ? 3.455 43.583 34.885 1.00 62.28 ? 245 ARG A CA 1 ATOM 1901 C C . ARG A 1 245 ? 3.100 44.065 36.287 1.00 65.49 ? 245 ARG A C 1 ATOM 1902 O O . ARG A 1 245 ? 3.433 43.411 37.276 1.00 76.99 ? 245 ARG A O 1 ATOM 1903 C CB . ARG A 1 245 ? 4.968 43.404 34.772 1.00 71.21 ? 245 ARG A CB 1 ATOM 1904 C CG . ARG A 1 245 ? 5.408 42.433 33.694 1.00 75.91 ? 245 ARG A CG 1 ATOM 1905 C CD . ARG A 1 245 ? 6.874 42.085 33.865 1.00 65.61 ? 245 ARG A CD 1 ATOM 1906 N NE . ARG A 1 245 ? 7.155 41.599 35.212 1.00 79.98 ? 245 ARG A NE 1 ATOM 1907 C CZ . ARG A 1 245 ? 7.197 40.315 35.551 1.00 65.89 ? 245 ARG A CZ 1 ATOM 1908 N NH1 . ARG A 1 245 ? 6.984 39.378 34.638 1.00 60.62 ? 245 ARG A NH1 1 ATOM 1909 N NH2 . ARG A 1 245 ? 7.461 39.969 36.803 1.00 88.29 ? 245 ARG A NH2 1 ATOM 1910 N N . ALA A 1 246 ? 2.423 45.205 36.370 1.00 70.06 ? 246 ALA A N 1 ATOM 1911 C CA . ALA A 1 246 ? 2.090 45.793 37.662 1.00 88.63 ? 246 ALA A CA 1 ATOM 1912 C C . ALA A 1 246 ? 1.144 44.902 38.450 1.00 79.89 ? 246 ALA A C 1 ATOM 1913 O O . ALA A 1 246 ? 0.408 44.099 37.874 1.00 88.86 ? 246 ALA A O 1 ATOM 1914 C CB . ALA A 1 246 ? 1.478 47.166 37.481 1.00 94.01 ? 246 ALA A CB 1 ATOM 1915 N N . ALA A 1 247 ? 1.182 45.058 39.771 1.00 79.30 ? 247 ALA A N 1 ATOM 1916 C CA . ALA A 1 247 ? 0.313 44.325 40.684 1.00 81.00 ? 247 ALA A CA 1 ATOM 1917 C C . ALA A 1 247 ? 0.378 42.828 40.442 1.00 89.46 ? 247 ALA A C 1 ATOM 1918 O O . ALA A 1 247 ? -0.607 42.228 40.017 1.00 79.76 ? 247 ALA A O 1 ATOM 1919 C CB . ALA A 1 247 ? -1.123 44.816 40.558 1.00 73.05 ? 247 ALA A CB 1 ATOM 1920 N N . ARG A 1 248 ? 1.543 42.240 40.702 1.00 108.81 ? 248 ARG A N 1 ATOM 1921 C CA . ARG A 1 248 ? 1.733 40.797 40.587 1.00 93.22 ? 248 ARG A CA 1 ATOM 1922 C C . ARG A 1 248 ? 1.346 40.299 39.197 1.00 77.56 ? 248 ARG A C 1 ATOM 1923 O O . ARG A 1 248 ? 0.727 39.246 39.050 1.00 90.15 ? 248 ARG A O 1 ATOM 1924 C CB . ARG A 1 248 ? 0.926 40.077 41.668 1.00 91.67 ? 248 ARG A CB 1 ATOM 1925 C CG . ARG A 1 248 ? 1.165 40.642 43.061 1.00 103.12 ? 248 ARG A CG 1 ATOM 1926 C CD . ARG A 1 248 ? 0.030 40.303 44.009 1.00 134.95 ? 248 ARG A CD 1 ATOM 1927 N NE . ARG A 1 248 ? 0.249 40.853 45.344 1.00 160.03 ? 248 ARG A NE 1 ATOM 1928 C CZ . ARG A 1 248 ? -0.544 40.626 46.387 1.00 168.20 ? 248 ARG A CZ 1 ATOM 1929 N NH1 . ARG A 1 248 ? -1.614 39.854 46.255 1.00 169.07 ? 248 ARG A NH1 1 ATOM 1930 N NH2 . ARG A 1 248 ? -0.266 41.168 47.565 1.00 162.19 ? 248 ARG A NH2 1 ATOM 1931 N N . THR A 1 249 ? 1.711 41.089 38.190 1.00 86.56 ? 249 THR A N 1 ATOM 1932 C CA . THR A 1 249 ? 1.453 40.800 36.777 1.00 73.84 ? 249 THR A CA 1 ATOM 1933 C C . THR A 1 249 ? -0.032 40.656 36.439 1.00 67.92 ? 249 THR A C 1 ATOM 1934 O O . THR A 1 249 ? -0.385 40.028 35.441 1.00 68.20 ? 249 THR A O 1 ATOM 1935 C CB . THR A 1 249 ? 2.194 39.524 36.310 1.00 65.90 ? 249 THR A CB 1 ATOM 1936 O OG1 . THR A 1 249 ? 1.677 38.379 36.996 1.00 66.41 ? 249 THR A OG1 1 ATOM 1937 C CG2 . THR A 1 249 ? 3.685 39.646 36.583 1.00 96.04 ? 249 THR A CG2 1 ATOM 1938 N N . LEU A 1 250 ? -0.896 41.254 37.254 1.00 68.63 ? 250 LEU A N 1 ATOM 1939 C CA . LEU A 1 250 ? -2.305 41.380 36.893 1.00 69.62 ? 250 LEU A CA 1 ATOM 1940 C C . LEU A 1 250 ? -2.436 42.404 35.779 1.00 79.25 ? 250 LEU A C 1 ATOM 1941 O O . LEU A 1 250 ? -3.313 42.309 34.919 1.00 69.69 ? 250 LEU A O 1 ATOM 1942 C CB . LEU A 1 250 ? -3.160 41.804 38.090 1.00 74.06 ? 250 LEU A CB 1 ATOM 1943 C CG . LEU A 1 250 ? -3.867 40.714 38.895 1.00 90.71 ? 250 LEU A CG 1 ATOM 1944 C CD1 . LEU A 1 250 ? -2.922 40.098 39.903 1.00 107.87 ? 250 LEU A CD1 1 ATOM 1945 C CD2 . LEU A 1 250 ? -5.099 41.273 39.587 1.00 84.27 ? 250 LEU A CD2 1 ATOM 1946 N N . GLY A 1 251 ? -1.548 43.390 35.816 1.00 74.78 ? 251 GLY A N 1 ATOM 1947 C CA . GLY A 1 251 ? -1.544 44.470 34.852 1.00 61.31 ? 251 GLY A CA 1 ATOM 1948 C C . GLY A 1 251 ? -2.332 45.642 35.386 1.00 73.79 ? 251 GLY A C 1 ATOM 1949 O O . GLY A 1 251 ? -3.334 45.464 36.080 1.00 70.09 ? 251 GLY A O 1 ATOM 1950 N N . MET A 1 252 ? -1.888 46.847 35.051 1.00 82.73 ? 252 MET A N 1 ATOM 1951 C CA . MET A 1 252 ? -2.551 48.057 35.511 1.00 71.25 ? 252 MET A CA 1 ATOM 1952 C C . MET A 1 252 ? -2.483 49.151 34.462 1.00 70.73 ? 252 MET A C 1 ATOM 1953 O O . MET A 1 252 ? -1.603 49.149 33.601 1.00 64.05 ? 252 MET A O 1 ATOM 1954 C CB . MET A 1 252 ? -1.929 48.563 36.816 1.00 68.22 ? 252 MET A CB 1 ATOM 1955 C CG . MET A 1 252 ? -2.223 47.710 38.036 1.00 73.27 ? 252 MET A CG 1 ATOM 1956 S SD . MET A 1 252 ? -1.909 48.587 39.577 1.00 82.80 ? 252 MET A SD 1 ATOM 1957 C CE . MET A 1 252 ? -3.254 49.770 39.569 1.00 82.06 ? 252 MET A CE 1 ATOM 1958 N N . VAL A 1 253 ? -3.423 50.086 34.536 1.00 77.98 ? 253 VAL A N 1 ATOM 1959 C CA . VAL A 1 253 ? -3.358 51.285 33.718 1.00 76.89 ? 253 VAL A CA 1 ATOM 1960 C C . VAL A 1 253 ? -3.467 52.512 34.609 1.00 85.00 ? 253 VAL A C 1 ATOM 1961 O O . VAL A 1 253 ? -4.446 52.685 35.338 1.00 93.98 ? 253 VAL A O 1 ATOM 1962 C CB . VAL A 1 253 ? -4.458 51.312 32.643 1.00 65.89 ? 253 VAL A CB 1 ATOM 1963 C CG1 . VAL A 1 253 ? -4.648 52.723 32.108 1.00 67.52 ? 253 VAL A CG1 1 ATOM 1964 C CG2 . VAL A 1 253 ? -4.102 50.364 31.517 1.00 62.42 ? 253 VAL A CG2 1 ATOM 1965 N N . TYR A 1 254 ? -2.438 53.351 34.558 1.00 69.64 ? 254 TYR A N 1 ATOM 1966 C CA . TYR A 1 254 ? -2.401 54.569 35.348 1.00 75.50 ? 254 TYR A CA 1 ATOM 1967 C C . TYR A 1 254 ? -2.905 55.757 34.537 1.00 81.01 ? 254 TYR A C 1 ATOM 1968 O O . TYR A 1 254 ? -2.622 55.868 33.343 1.00 73.04 ? 254 TYR A O 1 ATOM 1969 C CB . TYR A 1 254 ? -0.980 54.842 35.844 1.00 70.82 ? 254 TYR A CB 1 ATOM 1970 C CG . TYR A 1 254 ? -0.419 53.784 36.768 1.00 74.61 ? 254 TYR A CG 1 ATOM 1971 C CD1 . TYR A 1 254 ? -1.256 52.930 37.473 1.00 87.93 ? 254 TYR A CD1 1 ATOM 1972 C CD2 . TYR A 1 254 ? 0.951 53.646 36.938 1.00 76.82 ? 254 TYR A CD2 1 ATOM 1973 C CE1 . TYR A 1 254 ? -0.743 51.965 38.320 1.00 83.28 ? 254 TYR A CE1 1 ATOM 1974 C CE2 . TYR A 1 254 ? 1.473 52.685 37.782 1.00 89.50 ? 254 TYR A CE2 1 ATOM 1975 C CZ . TYR A 1 254 ? 0.622 51.847 38.470 1.00 82.21 ? 254 TYR A CZ 1 ATOM 1976 O OH . TYR A 1 254 ? 1.143 50.889 39.310 1.00 80.15 ? 254 TYR A OH 1 ATOM 1977 N N . ILE A 1 255 ? -3.659 56.639 35.183 1.00 88.04 ? 255 ILE A N 1 ATOM 1978 C CA . ILE A 1 255 ? -4.029 57.901 34.560 1.00 81.51 ? 255 ILE A CA 1 ATOM 1979 C C . ILE A 1 255 ? -3.498 59.064 35.381 1.00 86.23 ? 255 ILE A C 1 ATOM 1980 O O . ILE A 1 255 ? -3.932 59.296 36.511 1.00 94.52 ? 255 ILE A O 1 ATOM 1981 C CB . ILE A 1 255 ? -5.548 58.045 34.391 1.00 77.03 ? 255 ILE A CB 1 ATOM 1982 C CG1 . ILE A 1 255 ? -6.059 57.048 33.351 1.00 75.05 ? 255 ILE A CG1 1 ATOM 1983 C CG2 . ILE A 1 255 ? -5.897 59.459 33.959 1.00 78.14 ? 255 ILE A CG2 1 ATOM 1984 C CD1 . ILE A 1 255 ? -7.500 57.274 32.939 1.00 77.60 ? 255 ILE A CD1 1 ATOM 1985 N N . TYR A 1 256 ? -2.549 59.792 34.805 1.00 86.50 ? 256 TYR A N 1 ATOM 1986 C CA . TYR A 1 256 ? -1.956 60.940 35.473 1.00 97.16 ? 256 TYR A CA 1 ATOM 1987 C C . TYR A 1 256 ? -2.548 62.235 34.946 1.00 85.81 ? 256 TYR A C 1 ATOM 1988 O O . TYR A 1 256 ? -2.886 62.338 33.765 1.00 78.23 ? 256 TYR A O 1 ATOM 1989 C CB . TYR A 1 256 ? -0.439 60.959 35.290 1.00 88.16 ? 256 TYR A CB 1 ATOM 1990 C CG . TYR A 1 256 ? 0.296 59.849 36.005 1.00 91.36 ? 256 TYR A CG 1 ATOM 1991 C CD1 . TYR A 1 256 ? 0.734 60.012 37.313 1.00 83.98 ? 256 TYR A CD1 1 ATOM 1992 C CD2 . TYR A 1 256 ? 0.565 58.643 35.368 1.00 78.20 ? 256 TYR A CD2 1 ATOM 1993 C CE1 . TYR A 1 256 ? 1.414 59.003 37.967 1.00 87.23 ? 256 TYR A CE1 1 ATOM 1994 C CE2 . TYR A 1 256 ? 1.245 57.629 36.013 1.00 68.15 ? 256 TYR A CE2 1 ATOM 1995 C CZ . TYR A 1 256 ? 1.667 57.813 37.312 1.00 76.94 ? 256 TYR A CZ 1 ATOM 1996 O OH . TYR A 1 256 ? 2.343 56.805 37.960 1.00 86.83 ? 256 TYR A OH 1 ATOM 1997 N N . ASP A 1 257 ? -2.682 63.215 35.833 1.00 78.86 ? 257 ASP A N 1 ATOM 1998 C CA . ASP A 1 257 ? -3.103 64.553 35.445 1.00 88.99 ? 257 ASP A CA 1 ATOM 1999 C C . ASP A 1 257 ? -2.061 65.156 34.511 1.00 87.85 ? 257 ASP A C 1 ATOM 2000 O O . ASP A 1 257 ? -0.874 65.180 34.826 1.00 97.04 ? 257 ASP A O 1 ATOM 2001 C CB . ASP A 1 257 ? -3.296 65.435 36.682 1.00 103.74 ? 257 ASP A CB 1 ATOM 2002 C CG . ASP A 1 257 ? -4.092 66.695 36.390 1.00 99.46 ? 257 ASP A CG 1 ATOM 2003 O OD1 . ASP A 1 257 ? -3.924 67.282 35.301 1.00 96.30 ? 257 ASP A OD1 1 ATOM 2004 O OD2 . ASP A 1 257 ? -4.893 67.099 37.258 1.00 115.63 ? 257 ASP A OD2 1 ATOM 2005 N N . GLY A 1 258 ? -2.507 65.652 33.363 1.00 77.99 ? 258 GLY A N 1 ATOM 2006 C CA . GLY A 1 258 ? -1.597 66.199 32.375 1.00 78.37 ? 258 GLY A CA 1 ATOM 2007 C C . GLY A 1 258 ? -1.041 67.560 32.751 1.00 87.36 ? 258 GLY A C 1 ATOM 2008 O O . GLY A 1 258 ? -0.359 68.198 31.950 1.00 81.71 ? 258 GLY A O 1 ATOM 2009 N N . LYS A 1 259 ? -1.326 68.005 33.971 1.00 85.78 ? 259 LYS A N 1 ATOM 2010 C CA . LYS A 1 259 ? -0.880 69.316 34.423 1.00 87.71 ? 259 LYS A CA 1 ATOM 2011 C C . LYS A 1 259 ? 0.221 69.208 35.475 1.00 89.81 ? 259 LYS A C 1 ATOM 2012 O O . LYS A 1 259 ? 1.372 69.540 35.202 1.00 94.38 ? 259 LYS A O 1 ATOM 2013 C CB . LYS A 1 259 ? -2.060 70.121 34.972 1.00 101.91 ? 259 LYS A CB 1 ATOM 2014 C CG . LYS A 1 259 ? -1.835 71.625 34.967 1.00 96.10 ? 259 LYS A CG 1 ATOM 2015 C CD . LYS A 1 259 ? -3.133 72.378 35.207 1.00 100.16 ? 259 LYS A CD 1 ATOM 2016 C CE . LYS A 1 259 ? -2.933 73.880 35.072 1.00 123.73 ? 259 LYS A CE 1 ATOM 2017 N NZ . LYS A 1 259 ? -4.201 74.634 35.290 1.00 127.41 ? 259 LYS A NZ 1 ATOM 2018 N N . ASN A 1 260 ? -0.132 68.773 36.682 1.00 99.30 ? 260 ASN A N 1 ATOM 2019 C CA . ASN A 1 260 ? 0.864 68.620 37.741 1.00 96.83 ? 260 ASN A CA 1 ATOM 2020 C C . ASN A 1 260 ? 1.383 67.183 37.919 1.00 83.36 ? 260 ASN A C 1 ATOM 2021 O O . ASN A 1 260 ? 2.153 66.912 38.843 1.00 87.22 ? 260 ASN A O 1 ATOM 2022 C CB . ASN A 1 260 ? 0.320 69.171 39.070 1.00 117.78 ? 260 ASN A CB 1 ATOM 2023 C CG . ASN A 1 260 ? -0.969 68.505 39.522 1.00 121.65 ? 260 ASN A CG 1 ATOM 2024 O OD1 . ASN A 1 260 ? -1.395 67.488 38.976 1.00 130.19 ? 260 ASN A OD1 1 ATOM 2025 N ND2 . ASN A 1 260 ? -1.594 69.092 40.542 1.00 126.08 ? 260 ASN A ND2 1 ATOM 2026 N N . MET A 1 261 ? 0.949 66.279 37.040 1.00 79.00 ? 261 MET A N 1 ATOM 2027 C CA . MET A 1 261 ? 1.418 64.884 36.999 1.00 87.08 ? 261 MET A CA 1 ATOM 2028 C C . MET A 1 261 ? 1.013 64.068 38.240 1.00 89.92 ? 261 MET A C 1 ATOM 2029 O O . MET A 1 261 ? 1.642 63.062 38.573 1.00 77.08 ? 261 MET A O 1 ATOM 2030 C CB . MET A 1 261 ? 2.945 64.853 36.807 1.00 95.39 ? 261 MET A CB 1 ATOM 2031 C CG . MET A 1 261 ? 3.557 63.509 36.400 1.00 78.62 ? 261 MET A CG 1 ATOM 2032 S SD . MET A 1 261 ? 2.864 62.788 34.905 1.00 92.80 ? 261 MET A SD 1 ATOM 2033 C CE . MET A 1 261 ? 4.349 62.126 34.154 1.00 63.94 ? 261 MET A CE 1 ATOM 2034 N N . SER A 1 262 ? -0.055 64.487 38.910 1.00 91.75 ? 262 SER A N 1 ATOM 2035 C CA . SER A 1 262 ? -0.610 63.698 40.006 1.00 85.70 ? 262 SER A CA 1 ATOM 2036 C C . SER A 1 262 ? -1.457 62.555 39.449 1.00 85.97 ? 262 SER A C 1 ATOM 2037 O O . SER A 1 262 ? -1.949 62.632 38.323 1.00 83.49 ? 262 SER A O 1 ATOM 2038 C CB . SER A 1 262 ? -1.442 64.571 40.947 1.00 94.76 ? 262 SER A CB 1 ATOM 2039 O OG . SER A 1 262 ? -2.596 65.070 40.297 1.00 109.96 ? 262 SER A OG 1 ATOM 2040 N N . SER A 1 263 ? -1.614 61.492 40.231 1.00 91.55 ? 263 SER A N 1 ATOM 2041 C CA . SER A 1 263 ? -2.429 60.356 39.813 1.00 94.16 ? 263 SER A CA 1 ATOM 2042 C C . SER A 1 263 ? -3.912 60.715 39.849 1.00 95.44 ? 263 SER A C 1 ATOM 2043 O O . SER A 1 263 ? -4.357 61.449 40.732 1.00 104.70 ? 263 SER A O 1 ATOM 2044 C CB . SER A 1 263 ? -2.157 59.139 40.701 1.00 95.93 ? 263 SER A CB 1 ATOM 2045 O OG . SER A 1 263 ? -2.879 58.005 40.252 1.00 113.74 ? 263 SER A OG 1 ATOM 2046 N N . LEU A 1 264 ? -4.671 60.202 38.884 1.00 90.73 ? 264 LEU A N 1 ATOM 2047 C CA . LEU A 1 264 ? -6.104 60.473 38.816 1.00 99.20 ? 264 LEU A CA 1 ATOM 2048 C C . LEU A 1 264 ? -6.930 59.210 39.014 1.00 109.42 ? 264 LEU A C 1 ATOM 2049 O O . LEU A 1 264 ? -7.596 59.044 40.037 1.00 116.47 ? 264 LEU A O 1 ATOM 2050 C CB . LEU A 1 264 ? -6.468 61.119 37.479 1.00 95.35 ? 264 LEU A CB 1 ATOM 2051 C CG . LEU A 1 264 ? -6.005 62.560 37.269 1.00 102.06 ? 264 LEU A CG 1 ATOM 2052 C CD1 . LEU A 1 264 ? -6.550 63.107 35.959 1.00 98.87 ? 264 LEU A CD1 1 ATOM 2053 C CD2 . LEU A 1 264 ? -6.431 63.432 38.439 1.00 116.26 ? 264 LEU A CD2 1 ATOM 2054 N N . TYR A 1 265 ? -6.884 58.323 38.026 1.00 96.67 ? 265 TYR A N 1 ATOM 2055 C CA . TYR A 1 265 ? -7.663 57.095 38.070 1.00 99.59 ? 265 TYR A CA 1 ATOM 2056 C C . TYR A 1 265 ? -6.777 55.880 37.849 1.00 105.21 ? 265 TYR A C 1 ATOM 2057 O O . TYR A 1 265 ? -5.632 56.003 37.410 1.00 91.38 ? 265 TYR A O 1 ATOM 2058 C CB . TYR A 1 265 ? -8.779 57.125 37.026 1.00 104.80 ? 265 TYR A CB 1 ATOM 2059 C CG . TYR A 1 265 ? -9.805 58.215 37.242 1.00 128.41 ? 265 TYR A CG 1 ATOM 2060 C CD1 . TYR A 1 265 ? -10.873 58.029 38.111 1.00 137.14 ? 265 TYR A CD1 1 ATOM 2061 C CD2 . TYR A 1 265 ? -9.711 59.427 36.571 1.00 123.83 ? 265 TYR A CD2 1 ATOM 2062 C CE1 . TYR A 1 265 ? -11.815 59.022 38.309 1.00 139.13 ? 265 TYR A CE1 1 ATOM 2063 C CE2 . TYR A 1 265 ? -10.648 60.426 36.762 1.00 122.44 ? 265 TYR A CE2 1 ATOM 2064 C CZ . TYR A 1 265 ? -11.697 60.218 37.631 1.00 134.31 ? 265 TYR A CZ 1 ATOM 2065 O OH . TYR A 1 265 ? -12.631 61.210 37.823 1.00 147.33 ? 265 TYR A OH 1 ATOM 2066 N N . ASN A 1 266 ? -7.316 54.708 38.165 1.00 115.63 ? 266 ASN A N 1 ATOM 2067 C CA . ASN A 1 266 ? -6.597 53.455 37.984 1.00 93.23 ? 266 ASN A CA 1 ATOM 2068 C C . ASN A 1 266 ? -7.451 52.371 37.350 1.00 91.20 ? 266 ASN A C 1 ATOM 2069 O O . ASN A 1 266 ? -8.677 52.376 37.466 1.00 107.80 ? 266 ASN A O 1 ATOM 2070 C CB . ASN A 1 266 ? -6.062 52.947 39.321 1.00 95.69 ? 266 ASN A CB 1 ATOM 2071 C CG . ASN A 1 266 ? -4.713 53.527 39.666 1.00 94.87 ? 266 ASN A CG 1 ATOM 2072 O OD1 . ASN A 1 266 ? -3.936 53.894 38.787 1.00 84.13 ? 266 ASN A OD1 1 ATOM 2073 N ND2 . ASN A 1 266 ? -4.425 53.611 40.955 1.00 114.87 ? 266 ASN A ND2 1 ATOM 2074 N N . PHE A 1 267 ? -6.785 51.440 36.680 1.00 86.65 ? 267 PHE A N 1 ATOM 2075 C CA . PHE A 1 267 ? -7.436 50.255 36.145 1.00 89.67 ? 267 PHE A CA 1 ATOM 2076 C C . PHE A 1 267 ? -6.588 49.031 36.474 1.00 87.56 ? 267 PHE A C 1 ATOM 2077 O O . PHE A 1 267 ? -5.364 49.127 36.559 1.00 75.30 ? 267 PHE A O 1 ATOM 2078 C CB . PHE A 1 267 ? -7.645 50.380 34.635 1.00 81.66 ? 267 PHE A CB 1 ATOM 2079 C CG . PHE A 1 267 ? -8.605 51.468 34.242 1.00 79.54 ? 267 PHE A CG 1 ATOM 2080 C CD1 . PHE A 1 267 ? -9.971 51.234 34.233 1.00 86.52 ? 267 PHE A CD1 1 ATOM 2081 C CD2 . PHE A 1 267 ? -8.144 52.721 33.875 1.00 80.28 ? 267 PHE A CD2 1 ATOM 2082 C CE1 . PHE A 1 267 ? -10.860 52.230 33.870 1.00 85.64 ? 267 PHE A CE1 1 ATOM 2083 C CE2 . PHE A 1 267 ? -9.028 53.721 33.510 1.00 86.88 ? 267 PHE A CE2 1 ATOM 2084 C CZ . PHE A 1 267 ? -10.387 53.474 33.507 1.00 88.10 ? 267 PHE A CZ 1 ATOM 2085 N N . THR A 1 268 ? -7.238 47.888 36.670 1.00 88.21 ? 268 THR A N 1 ATOM 2086 C CA . THR A 1 268 ? -6.520 46.658 36.991 1.00 89.08 ? 268 THR A CA 1 ATOM 2087 C C . THR A 1 268 ? -7.130 45.444 36.289 1.00 82.58 ? 268 THR A C 1 ATOM 2088 O O . THR A 1 268 ? -8.346 45.257 36.295 1.00 91.82 ? 268 THR A O 1 ATOM 2089 C CB . THR A 1 268 ? -6.497 46.406 38.511 1.00 83.18 ? 268 THR A CB 1 ATOM 2090 O OG1 . THR A 1 268 ? -6.063 47.591 39.191 1.00 78.99 ? 268 THR A OG1 1 ATOM 2091 C CG2 . THR A 1 268 ? -5.555 45.262 38.846 1.00 77.65 ? 268 THR A CG2 1 ATOM 2092 N N . GLY A 1 269 ? -6.277 44.623 35.684 1.00 77.62 ? 269 GLY A N 1 ATOM 2093 C CA . GLY A 1 269 ? -6.723 43.418 35.009 1.00 90.36 ? 269 GLY A CA 1 ATOM 2094 C C . GLY A 1 269 ? -7.238 42.374 35.980 1.00 104.90 ? 269 GLY A C 1 ATOM 2095 O O . GLY A 1 269 ? -6.854 42.363 37.149 1.00 88.13 ? 269 GLY A O 1 ATOM 2096 N N . GLU A 1 270 ? -8.117 41.499 35.500 1.00 110.47 ? 270 GLU A N 1 ATOM 2097 C CA . GLU A 1 270 ? -8.712 40.472 36.347 1.00 89.50 ? 270 GLU A CA 1 ATOM 2098 C C . GLU A 1 270 ? -7.929 39.161 36.318 1.00 85.98 ? 270 GLU A C 1 ATOM 2099 O O . GLU A 1 270 ? -8.193 38.258 37.111 1.00 112.76 ? 270 GLU A O 1 ATOM 2100 C CB . GLU A 1 270 ? -10.162 40.214 35.927 1.00 97.61 ? 270 GLU A CB 1 ATOM 2101 C CG . GLU A 1 270 ? -11.051 41.451 35.940 1.00 112.16 ? 270 GLU A CG 1 ATOM 2102 C CD . GLU A 1 270 ? -11.340 41.958 37.342 1.00 120.04 ? 270 GLU A CD 1 ATOM 2103 O OE1 . GLU A 1 270 ? -11.177 41.181 38.307 1.00 131.86 ? 270 GLU A OE1 1 ATOM 2104 O OE2 . GLU A 1 270 ? -11.732 43.137 37.478 1.00 109.54 ? 270 GLU A OE2 1 ATOM 2105 N N . GLN A 1 271 ? -6.962 39.062 35.410 1.00 74.14 ? 271 GLN A N 1 ATOM 2106 C CA . GLN A 1 271 ? -6.226 37.815 35.215 1.00 79.06 ? 271 GLN A CA 1 ATOM 2107 C C . GLN A 1 271 ? -4.732 38.051 35.021 1.00 70.07 ? 271 GLN A C 1 ATOM 2108 O O . GLN A 1 271 ? -4.328 38.930 34.261 1.00 92.28 ? 271 GLN A O 1 ATOM 2109 C CB . GLN A 1 271 ? -6.789 37.050 34.014 1.00 72.65 ? 271 GLN A CB 1 ATOM 2110 C CG . GLN A 1 271 ? -6.057 35.757 33.689 1.00 71.64 ? 271 GLN A CG 1 ATOM 2111 C CD . GLN A 1 271 ? -6.561 35.109 32.413 1.00 88.88 ? 271 GLN A CD 1 ATOM 2112 O OE1 . GLN A 1 271 ? -5.810 34.942 31.449 1.00 90.23 ? 271 GLN A OE1 1 ATOM 2113 N NE2 . GLN A 1 271 ? -7.837 34.737 32.400 1.00 86.10 ? 271 GLN A NE2 1 ATOM 2114 N N . MET A 1 272 ? -3.919 37.251 35.704 1.00 70.84 ? 272 MET A N 1 ATOM 2115 C CA . MET A 1 272 ? -2.468 37.379 35.626 1.00 81.50 ? 272 MET A CA 1 ATOM 2116 C C . MET A 1 272 ? -1.912 36.928 34.281 1.00 79.94 ? 272 MET A C 1 ATOM 2117 O O . MET A 1 272 ? -2.521 36.109 33.588 1.00 93.92 ? 272 MET A O 1 ATOM 2118 C CB . MET A 1 272 ? -1.802 36.581 36.744 1.00 80.67 ? 272 MET A CB 1 ATOM 2119 C CG . MET A 1 272 ? -2.277 36.966 38.125 1.00 92.23 ? 272 MET A CG 1 ATOM 2120 S SD . MET A 1 272 ? -1.264 36.251 39.427 1.00 84.42 ? 272 MET A SD 1 ATOM 2121 C CE . MET A 1 272 ? -2.156 36.827 40.862 1.00 121.46 ? 272 MET A CE 1 ATOM 2122 N N . ALA A 1 273 ? -0.767 37.503 33.916 1.00 63.16 ? 273 ALA A N 1 ATOM 2123 C CA . ALA A 1 273 ? -0.016 37.152 32.709 1.00 61.94 ? 273 ALA A CA 1 ATOM 2124 C C . ALA A 1 273 ? -0.756 37.495 31.414 1.00 67.13 ? 273 ALA A C 1 ATOM 2125 O O . ALA A 1 273 ? -0.216 37.319 30.322 1.00 62.27 ? 273 ALA A O 1 ATOM 2126 C CB . ALA A 1 273 ? 0.359 35.678 32.727 1.00 63.60 ? 273 ALA A CB 1 ATOM 2127 N N . ALA A 1 274 ? -1.987 37.983 31.540 1.00 63.58 ? 274 ALA A N 1 ATOM 2128 C CA . ALA A 1 274 ? -2.797 38.376 30.390 1.00 60.19 ? 274 ALA A CA 1 ATOM 2129 C C . ALA A 1 274 ? -2.239 39.623 29.712 1.00 73.92 ? 274 ALA A C 1 ATOM 2130 O O . ALA A 1 274 ? -2.692 40.010 28.632 1.00 74.37 ? 274 ALA A O 1 ATOM 2131 C CB . ALA A 1 274 ? -4.233 38.611 30.819 1.00 61.32 ? 274 ALA A CB 1 ATOM 2132 N N . TYR A 1 275 ? -1.257 40.242 30.363 1.00 64.26 ? 275 TYR A N 1 ATOM 2133 C CA . TYR A 1 275 ? -0.648 41.489 29.913 1.00 64.37 ? 275 TYR A CA 1 ATOM 2134 C C . TYR A 1 275 ? -1.692 42.583 29.722 1.00 71.19 ? 275 TYR A C 1 ATOM 2135 O O . TYR A 1 275 ? -1.891 43.093 28.622 1.00 68.98 ? 275 TYR A O 1 ATOM 2136 C CB . TYR A 1 275 ? 0.145 41.271 28.619 1.00 55.04 ? 275 TYR A CB 1 ATOM 2137 C CG . TYR A 1 275 ? 1.595 41.686 28.736 1.00 64.86 ? 275 TYR A CG 1 ATOM 2138 C CD1 . TYR A 1 275 ? 2.465 40.995 29.569 1.00 56.16 ? 275 TYR A CD1 1 ATOM 2139 C CD2 . TYR A 1 275 ? 2.093 42.769 28.022 1.00 68.21 ? 275 TYR A CD2 1 ATOM 2140 C CE1 . TYR A 1 275 ? 3.785 41.367 29.690 1.00 57.71 ? 275 TYR A CE1 1 ATOM 2141 C CE2 . TYR A 1 275 ? 3.420 43.150 28.135 1.00 64.68 ? 275 TYR A CE2 1 ATOM 2142 C CZ . TYR A 1 275 ? 4.259 42.443 28.973 1.00 79.04 ? 275 TYR A CZ 1 ATOM 2143 O OH . TYR A 1 275 ? 5.578 42.808 29.095 1.00 96.68 ? 275 TYR A OH 1 ATOM 2144 N N . PHE A 1 276 ? -2.343 42.939 30.822 1.00 82.68 ? 276 PHE A N 1 ATOM 2145 C CA . PHE A 1 276 ? -3.291 44.041 30.850 1.00 73.24 ? 276 PHE A CA 1 ATOM 2146 C C . PHE A 1 276 ? -2.521 45.348 30.722 1.00 77.40 ? 276 PHE A C 1 ATOM 2147 O O . PHE A 1 276 ? -1.660 45.648 31.546 1.00 75.22 ? 276 PHE A O 1 ATOM 2148 C CB . PHE A 1 276 ? -4.093 43.990 32.153 1.00 68.01 ? 276 PHE A CB 1 ATOM 2149 C CG . PHE A 1 276 ? -5.162 45.038 32.273 1.00 64.03 ? 276 PHE A CG 1 ATOM 2150 C CD1 . PHE A 1 276 ? -4.933 46.199 32.993 1.00 71.16 ? 276 PHE A CD1 1 ATOM 2151 C CD2 . PHE A 1 276 ? -6.411 44.842 31.710 1.00 69.44 ? 276 PHE A CD2 1 ATOM 2152 C CE1 . PHE A 1 276 ? -5.921 47.156 33.125 1.00 79.33 ? 276 PHE A CE1 1 ATOM 2153 C CE2 . PHE A 1 276 ? -7.404 45.794 31.840 1.00 76.90 ? 276 PHE A CE2 1 ATOM 2154 C CZ . PHE A 1 276 ? -7.159 46.952 32.549 1.00 81.55 ? 276 PHE A CZ 1 ATOM 2155 N N . GLY A 1 277 ? -2.833 46.130 29.695 1.00 76.06 ? 277 GLY A N 1 ATOM 2156 C CA . GLY A 1 277 ? -2.131 47.379 29.460 1.00 84.04 ? 277 GLY A CA 1 ATOM 2157 C C . GLY A 1 277 ? -1.059 47.311 28.385 1.00 83.95 ? 277 GLY A C 1 ATOM 2158 O O . GLY A 1 277 ? -0.270 48.243 28.230 1.00 90.74 ? 277 GLY A O 1 ATOM 2159 N N . PHE A 1 278 ? -1.026 46.208 27.645 1.00 76.47 ? 278 PHE A N 1 ATOM 2160 C CA . PHE A 1 278 ? -0.114 46.065 26.514 1.00 61.38 ? 278 PHE A CA 1 ATOM 2161 C C . PHE A 1 278 ? -0.396 47.152 25.489 1.00 63.25 ? 278 PHE A C 1 ATOM 2162 O O . PHE A 1 278 ? 0.515 47.713 24.883 1.00 60.25 ? 278 PHE A O 1 ATOM 2163 C CB . PHE A 1 278 ? -0.261 44.678 25.879 1.00 52.45 ? 278 PHE A CB 1 ATOM 2164 C CG . PHE A 1 278 ? 0.584 44.469 24.653 1.00 52.02 ? 278 PHE A CG 1 ATOM 2165 C CD1 . PHE A 1 278 ? 1.884 44.001 24.763 1.00 51.94 ? 278 PHE A CD1 1 ATOM 2166 C CD2 . PHE A 1 278 ? 0.073 44.719 23.387 1.00 52.27 ? 278 PHE A CD2 1 ATOM 2167 C CE1 . PHE A 1 278 ? 2.665 43.798 23.634 1.00 59.37 ? 278 PHE A CE1 1 ATOM 2168 C CE2 . PHE A 1 278 ? 0.849 44.518 22.254 1.00 52.25 ? 278 PHE A CE2 1 ATOM 2169 C CZ . PHE A 1 278 ? 2.146 44.058 22.378 1.00 51.96 ? 278 PHE A CZ 1 ATOM 2170 N N . SER A 1 279 ? -1.679 47.438 25.304 1.00 76.61 ? 279 SER A N 1 ATOM 2171 C CA . SER A 1 279 ? -2.117 48.462 24.374 1.00 68.83 ? 279 SER A CA 1 ATOM 2172 C C . SER A 1 279 ? -3.160 49.344 25.041 1.00 78.06 ? 279 SER A C 1 ATOM 2173 O O . SER A 1 279 ? -4.041 48.850 25.744 1.00 82.70 ? 279 SER A O 1 ATOM 2174 C CB . SER A 1 279 ? -2.685 47.827 23.103 1.00 73.00 ? 279 SER A CB 1 ATOM 2175 O OG . SER A 1 279 ? -3.047 48.814 22.153 1.00 108.64 ? 279 SER A OG 1 ATOM 2176 N N . VAL A 1 280 ? -3.049 50.651 24.831 1.00 76.89 ? 280 VAL A N 1 ATOM 2177 C CA . VAL A 1 280 ? -4.038 51.591 25.341 1.00 57.61 ? 280 VAL A CA 1 ATOM 2178 C C . VAL A 1 280 ? -4.444 52.575 24.254 1.00 59.48 ? 280 VAL A C 1 ATOM 2179 O O . VAL A 1 280 ? -3.652 52.895 23.364 1.00 68.77 ? 280 VAL A O 1 ATOM 2180 C CB . VAL A 1 280 ? -3.513 52.370 26.563 1.00 72.15 ? 280 VAL A CB 1 ATOM 2181 C CG1 . VAL A 1 280 ? -3.337 51.441 27.755 1.00 67.07 ? 280 VAL A CG1 1 ATOM 2182 C CG2 . VAL A 1 280 ? -2.206 53.079 26.226 1.00 74.89 ? 280 VAL A CG2 1 ATOM 2183 N N . ALA A 1 281 ? -5.684 53.045 24.325 1.00 60.27 ? 281 ALA A N 1 ATOM 2184 C CA . ALA A 1 281 ? -6.182 54.035 23.378 1.00 74.30 ? 281 ALA A CA 1 ATOM 2185 C C . ALA A 1 281 ? -7.278 54.880 24.015 1.00 81.58 ? 281 ALA A C 1 ATOM 2186 O O . ALA A 1 281 ? -7.969 54.431 24.931 1.00 66.85 ? 281 ALA A O 1 ATOM 2187 C CB . ALA A 1 281 ? -6.696 53.359 22.115 1.00 67.56 ? 281 ALA A CB 1 ATOM 2188 N N . ALA A 1 282 ? -7.436 56.104 23.524 1.00 87.60 ? 282 ALA A N 1 ATOM 2189 C CA . ALA A 1 282 ? -8.430 57.016 24.074 1.00 67.38 ? 282 ALA A CA 1 ATOM 2190 C C . ALA A 1 282 ? -9.240 57.684 22.969 1.00 68.98 ? 282 ALA A C 1 ATOM 2191 O O . ALA A 1 282 ? -8.685 58.302 22.062 1.00 72.98 ? 282 ALA A O 1 ATOM 2192 C CB . ALA A 1 282 ? -7.759 58.059 24.945 1.00 67.83 ? 282 ALA A CB 1 ATOM 2193 N N . THR A 1 283 ? -10.558 57.541 23.049 1.00 72.13 ? 283 THR A N 1 ATOM 2194 C CA . THR A 1 283 ? -11.475 58.140 22.082 1.00 78.53 ? 283 THR A CA 1 ATOM 2195 C C . THR A 1 283 ? -12.835 58.325 22.725 1.00 98.11 ? 283 THR A C 1 ATOM 2196 O O . THR A 1 283 ? -13.125 57.713 23.752 1.00 121.41 ? 283 THR A O 1 ATOM 2197 C CB . THR A 1 283 ? -11.653 57.270 20.823 1.00 80.08 ? 283 THR A CB 1 ATOM 2198 O OG1 . THR A 1 283 ? -10.603 56.300 20.744 1.00 108.14 ? 283 THR A OG1 1 ATOM 2199 C CG2 . THR A 1 283 ? -11.662 58.132 19.570 1.00 78.85 ? 283 THR A CG2 1 ATOM 2200 N N . ASP A 1 284 ? -13.680 59.150 22.120 1.00 86.24 ? 284 ASP A N 1 ATOM 2201 C CA . ASP A 1 284 ? -15.052 59.231 22.585 1.00 93.37 ? 284 ASP A CA 1 ATOM 2202 C C . ASP A 1 284 ? -15.923 58.405 21.651 1.00 107.13 ? 284 ASP A C 1 ATOM 2203 O O . ASP A 1 284 ? -16.236 58.821 20.537 1.00 121.70 ? 284 ASP A O 1 ATOM 2204 C CB . ASP A 1 284 ? -15.526 60.679 22.635 1.00 95.57 ? 284 ASP A CB 1 ATOM 2205 C CG . ASP A 1 284 ? -16.971 60.802 23.058 1.00 120.87 ? 284 ASP A CG 1 ATOM 2206 O OD1 . ASP A 1 284 ? -17.302 60.367 24.183 1.00 122.04 ? 284 ASP A OD1 1 ATOM 2207 O OD2 . ASP A 1 284 ? -17.773 61.333 22.263 1.00 138.80 ? 284 ASP A OD2 1 ATOM 2208 N N . ILE A 1 285 ? -16.320 57.232 22.130 1.00 92.42 ? 285 ILE A N 1 ATOM 2209 C CA . ILE A 1 285 ? -17.045 56.276 21.310 1.00 87.33 ? 285 ILE A CA 1 ATOM 2210 C C . ILE A 1 285 ? -18.544 56.572 21.282 1.00 94.70 ? 285 ILE A C 1 ATOM 2211 O O . ILE A 1 285 ? -19.229 56.248 20.312 1.00 106.65 ? 285 ILE A O 1 ATOM 2212 C CB . ILE A 1 285 ? -16.785 54.822 21.795 1.00 86.34 ? 285 ILE A CB 1 ATOM 2213 C CG1 . ILE A 1 285 ? -16.775 53.853 20.611 1.00 90.04 ? 285 ILE A CG1 1 ATOM 2214 C CG2 . ILE A 1 285 ? -17.772 54.400 22.875 1.00 86.10 ? 285 ILE A CG2 1 ATOM 2215 C CD1 . ILE A 1 285 ? -15.613 54.072 19.661 1.00 92.56 ? 285 ILE A CD1 1 ATOM 2216 N N . ASN A 1 286 ? -19.051 57.181 22.350 1.00 96.91 ? 286 ASN A N 1 ATOM 2217 C CA . ASN A 1 286 ? -20.485 57.401 22.492 1.00 101.55 ? 286 ASN A CA 1 ATOM 2218 C C . ASN A 1 286 ? -20.953 58.799 22.094 1.00 108.90 ? 286 ASN A C 1 ATOM 2219 O O . ASN A 1 286 ? -22.143 59.102 22.172 1.00 123.33 ? 286 ASN A O 1 ATOM 2220 C CB . ASN A 1 286 ? -20.914 57.102 23.930 1.00 106.80 ? 286 ASN A CB 1 ATOM 2221 C CG . ASN A 1 286 ? -20.043 57.798 24.961 1.00 112.16 ? 286 ASN A CG 1 ATOM 2222 O OD1 . ASN A 1 286 ? -18.931 58.245 24.666 1.00 112.00 ? 286 ASN A OD1 1 ATOM 2223 N ND2 . ASN A 1 286 ? -20.546 57.886 26.187 1.00 123.04 ? 286 ASN A ND2 1 ATOM 2224 N N . GLY A 1 287 ? -19.985 59.630 21.734 1.00 99.16 ? 287 GLY A N 1 ATOM 2225 C CA . GLY A 1 287 ? -20.238 61.009 21.400 1.00 101.81 ? 287 GLY A CA 1 ATOM 2226 C C . GLY A 1 287 ? -20.621 61.865 22.589 1.00 111.63 ? 287 GLY A C 1 ATOM 2227 O O . GLY A 1 287 ? -21.130 62.968 22.388 1.00 117.26 ? 287 GLY A O 1 ATOM 2228 N N . ASP A 1 288 ? -20.396 61.406 23.822 1.00 111.13 ? 288 ASP A N 1 ATOM 2229 C CA . ASP A 1 288 ? -20.773 62.296 24.918 1.00 106.80 ? 288 ASP A CA 1 ATOM 2230 C C . ASP A 1 288 ? -19.625 63.214 25.325 1.00 108.33 ? 288 ASP A C 1 ATOM 2231 O O . ASP A 1 288 ? -19.797 64.090 26.172 1.00 115.85 ? 288 ASP A O 1 ATOM 2232 C CB . ASP A 1 288 ? -21.232 61.479 26.133 1.00 106.89 ? 288 ASP A CB 1 ATOM 2233 C CG . ASP A 1 288 ? -20.221 60.412 26.544 1.00 123.50 ? 288 ASP A CG 1 ATOM 2234 O OD1 . ASP A 1 288 ? -19.249 60.176 25.798 1.00 154.79 ? 288 ASP A OD1 1 ATOM 2235 O OD2 . ASP A 1 288 ? -20.398 59.796 27.618 1.00 109.63 ? 288 ASP A OD2 1 ATOM 2236 N N . ASP A 1 289 ? -18.644 63.233 24.439 1.00 106.47 ? 289 ASP A N 1 ATOM 2237 C CA . ASP A 1 289 ? -17.722 64.345 24.311 1.00 109.87 ? 289 ASP A CA 1 ATOM 2238 C C . ASP A 1 289 ? -16.863 64.294 25.509 1.00 107.86 ? 289 ASP A C 1 ATOM 2239 O O . ASP A 1 289 ? -16.214 65.243 25.901 1.00 127.52 ? 289 ASP A O 1 ATOM 2240 C CB . ASP A 1 289 ? -18.459 65.666 24.228 1.00 129.93 ? 289 ASP A CB 1 ATOM 2241 C CG . ASP A 1 289 ? -18.262 66.345 22.897 1.00 137.05 ? 289 ASP A CG 1 ATOM 2242 O OD1 . ASP A 1 289 ? -17.239 66.080 22.248 1.00 132.42 ? 289 ASP A OD1 1 ATOM 2243 O OD2 . ASP A 1 289 ? -19.127 67.138 22.491 1.00 147.93 ? 289 ASP A OD2 1 ATOM 2244 N N . TYR A 1 290 ? -16.900 63.113 26.071 1.00 105.79 ? 290 TYR A N 1 ATOM 2245 C CA . TYR A 1 290 ? -16.072 62.667 27.184 1.00 101.85 ? 290 TYR A CA 1 ATOM 2246 C C . TYR A 1 290 ? -15.228 61.481 26.732 1.00 104.00 ? 290 TYR A C 1 ATOM 2247 O O . TYR A 1 290 ? -15.763 60.432 26.350 1.00 113.04 ? 290 TYR A O 1 ATOM 2248 C CB . TYR A 1 290 ? -16.924 62.284 28.396 1.00 102.49 ? 290 TYR A CB 1 ATOM 2249 C CG . TYR A 1 290 ? -17.450 63.460 29.189 1.00 110.76 ? 290 TYR A CG 1 ATOM 2250 C CD1 . TYR A 1 290 ? -16.597 64.238 29.962 1.00 123.01 ? 290 TYR A CD1 1 ATOM 2251 C CD2 . TYR A 1 290 ? -18.800 63.783 29.180 1.00 116.63 ? 290 TYR A CD2 1 ATOM 2252 C CE1 . TYR A 1 290 ? -17.071 65.311 30.693 1.00 125.94 ? 290 TYR A CE1 1 ATOM 2253 C CE2 . TYR A 1 290 ? -19.284 64.855 29.910 1.00 119.55 ? 290 TYR A CE2 1 ATOM 2254 C CZ . TYR A 1 290 ? -18.415 65.615 30.663 1.00 120.44 ? 290 TYR A CZ 1 ATOM 2255 O OH . TYR A 1 290 ? -18.892 66.682 31.390 1.00 135.04 ? 290 TYR A OH 1 ATOM 2256 N N . ALA A 1 291 ? -13.911 61.664 26.772 1.00 98.92 ? 291 ALA A N 1 ATOM 2257 C CA . ALA A 1 291 ? -12.963 60.652 26.320 1.00 91.74 ? 291 ALA A CA 1 ATOM 2258 C C . ALA A 1 291 ? -13.149 59.340 27.067 1.00 90.08 ? 291 ALA A C 1 ATOM 2259 O O . ALA A 1 291 ? -13.288 59.321 28.288 1.00 95.12 ? 291 ALA A O 1 ATOM 2260 C CB . ALA A 1 291 ? -11.535 61.154 26.486 1.00 109.08 ? 291 ALA A CB 1 ATOM 2261 N N . ASP A 1 292 ? -13.146 58.243 26.320 1.00 84.08 ? 292 ASP A N 1 ATOM 2262 C CA . ASP A 1 292 ? -13.386 56.929 26.893 1.00 81.35 ? 292 ASP A CA 1 ATOM 2263 C C . ASP A 1 292 ? -12.128 56.074 26.773 1.00 81.40 ? 292 ASP A C 1 ATOM 2264 O O . ASP A 1 292 ? -11.336 56.250 25.846 1.00 74.77 ? 292 ASP A O 1 ATOM 2265 C CB . ASP A 1 292 ? -14.582 56.276 26.204 1.00 82.84 ? 292 ASP A CB 1 ATOM 2266 C CG . ASP A 1 292 ? -15.784 57.208 26.128 1.00 97.24 ? 292 ASP A CG 1 ATOM 2267 O OD1 . ASP A 1 292 ? -16.109 57.849 27.149 1.00 99.93 ? 292 ASP A OD1 1 ATOM 2268 O OD2 . ASP A 1 292 ? -16.395 57.319 25.045 1.00 102.91 ? 292 ASP A OD2 1 ATOM 2269 N N . VAL A 1 293 ? -11.943 55.158 27.720 1.00 78.12 ? 293 VAL A N 1 ATOM 2270 C CA . VAL A 1 293 ? -10.690 54.419 27.839 1.00 75.88 ? 293 VAL A CA 1 ATOM 2271 C C . VAL A 1 293 ? -10.754 53.020 27.231 1.00 81.16 ? 293 VAL A C 1 ATOM 2272 O O . VAL A 1 293 ? -11.702 52.270 27.466 1.00 97.90 ? 293 VAL A O 1 ATOM 2273 C CB . VAL A 1 293 ? -10.263 54.288 29.315 1.00 78.86 ? 293 VAL A CB 1 ATOM 2274 C CG1 . VAL A 1 293 ? -8.882 53.661 29.418 1.00 77.27 ? 293 VAL A CG1 1 ATOM 2275 C CG2 . VAL A 1 293 ? -10.279 55.642 29.992 1.00 90.39 ? 293 VAL A CG2 1 ATOM 2276 N N . PHE A 1 294 ? -9.729 52.680 26.454 1.00 81.34 ? 294 PHE A N 1 ATOM 2277 C CA . PHE A 1 294 ? -9.605 51.352 25.863 1.00 80.61 ? 294 PHE A CA 1 ATOM 2278 C C . PHE A 1 294 ? -8.308 50.681 26.302 1.00 72.25 ? 294 PHE A C 1 ATOM 2279 O O . PHE A 1 294 ? -7.221 51.221 26.102 1.00 90.25 ? 294 PHE A O 1 ATOM 2280 C CB . PHE A 1 294 ? -9.665 51.435 24.337 1.00 68.44 ? 294 PHE A CB 1 ATOM 2281 C CG . PHE A 1 294 ? -11.006 51.849 23.809 1.00 77.44 ? 294 PHE A CG 1 ATOM 2282 C CD1 . PHE A 1 294 ? -11.374 53.184 23.785 1.00 72.56 ? 294 PHE A CD1 1 ATOM 2283 C CD2 . PHE A 1 294 ? -11.901 50.901 23.342 1.00 75.05 ? 294 PHE A CD2 1 ATOM 2284 C CE1 . PHE A 1 294 ? -12.609 53.565 23.302 1.00 76.72 ? 294 PHE A CE1 1 ATOM 2285 C CE2 . PHE A 1 294 ? -13.136 51.276 22.857 1.00 76.17 ? 294 PHE A CE2 1 ATOM 2286 C CZ . PHE A 1 294 ? -13.491 52.611 22.836 1.00 82.75 ? 294 PHE A CZ 1 ATOM 2287 N N . ILE A 1 295 ? -8.429 49.501 26.902 1.00 68.86 ? 295 ILE A N 1 ATOM 2288 C CA . ILE A 1 295 ? -7.269 48.780 27.413 1.00 63.25 ? 295 ILE A CA 1 ATOM 2289 C C . ILE A 1 295 ? -7.208 47.354 26.877 1.00 67.14 ? 295 ILE A C 1 ATOM 2290 O O . ILE A 1 295 ? -8.113 46.554 27.119 1.00 83.48 ? 295 ILE A O 1 ATOM 2291 C CB . ILE A 1 295 ? -7.277 48.728 28.950 1.00 66.35 ? 295 ILE A CB 1 ATOM 2292 C CG1 . ILE A 1 295 ? -7.452 50.133 29.531 1.00 66.23 ? 295 ILE A CG1 1 ATOM 2293 C CG2 . ILE A 1 295 ? -6.003 48.081 29.460 1.00 60.75 ? 295 ILE A CG2 1 ATOM 2294 C CD1 . ILE A 1 295 ? -7.660 50.152 31.022 1.00 67.65 ? 295 ILE A CD1 1 ATOM 2295 N N . GLY A 1 296 ? -6.144 47.040 26.145 1.00 58.75 ? 296 GLY A N 1 ATOM 2296 C CA . GLY A 1 296 ? -5.968 45.700 25.613 1.00 65.12 ? 296 GLY A CA 1 ATOM 2297 C C . GLY A 1 296 ? -5.284 44.731 26.561 1.00 68.25 ? 296 GLY A C 1 ATOM 2298 O O . GLY A 1 296 ? -4.386 45.110 27.311 1.00 66.67 ? 296 GLY A O 1 ATOM 2299 N N . ALA A 1 297 ? -5.707 43.471 26.512 1.00 101.95 ? 297 ALA A N 1 ATOM 2300 C CA . ALA A 1 297 ? -5.060 42.390 27.257 1.00 89.12 ? 297 ALA A CA 1 ATOM 2301 C C . ALA A 1 297 ? -5.006 41.147 26.376 1.00 74.04 ? 297 ALA A C 1 ATOM 2302 O O . ALA A 1 297 ? -5.834 40.248 26.513 1.00 76.52 ? 297 ALA A O 1 ATOM 2303 C CB . ALA A 1 297 ? -5.799 42.104 28.552 1.00 60.54 ? 297 ALA A CB 1 ATOM 2304 N N . PRO A 1 298 ? -4.024 41.103 25.463 1.00 56.83 ? 298 PRO A N 1 ATOM 2305 C CA . PRO A 1 298 ? -3.952 40.154 24.344 1.00 61.09 ? 298 PRO A CA 1 ATOM 2306 C C . PRO A 1 298 ? -3.870 38.687 24.753 1.00 63.89 ? 298 PRO A C 1 ATOM 2307 O O . PRO A 1 298 ? -4.270 37.820 23.981 1.00 82.53 ? 298 PRO A O 1 ATOM 2308 C CB . PRO A 1 298 ? -2.665 40.569 23.619 1.00 86.51 ? 298 PRO A CB 1 ATOM 2309 C CG . PRO A 1 298 ? -2.381 41.956 24.079 1.00 55.05 ? 298 PRO A CG 1 ATOM 2310 C CD . PRO A 1 298 ? -2.867 42.010 25.484 1.00 55.38 ? 298 PRO A CD 1 ATOM 2311 N N . LEU A 1 299 ? -3.331 38.413 25.933 1.00 64.46 ? 299 LEU A N 1 ATOM 2312 C CA . LEU A 1 299 ? -3.153 37.037 26.383 1.00 63.82 ? 299 LEU A CA 1 ATOM 2313 C C . LEU A 1 299 ? -4.270 36.559 27.313 1.00 64.82 ? 299 LEU A C 1 ATOM 2314 O O . LEU A 1 299 ? -4.195 35.458 27.858 1.00 75.94 ? 299 LEU A O 1 ATOM 2315 C CB . LEU A 1 299 ? -1.793 36.887 27.064 1.00 79.85 ? 299 LEU A CB 1 ATOM 2316 C CG . LEU A 1 299 ? -0.617 37.394 26.222 1.00 69.01 ? 299 LEU A CG 1 ATOM 2317 C CD1 . LEU A 1 299 ? 0.706 37.162 26.936 1.00 75.06 ? 299 LEU A CD1 1 ATOM 2318 C CD2 . LEU A 1 299 ? -0.605 36.756 24.837 1.00 58.82 ? 299 LEU A CD2 1 ATOM 2319 N N . PHE A 1 300 ? -5.289 37.394 27.510 1.00 70.09 ? 300 PHE A N 1 ATOM 2320 C CA . PHE A 1 300 ? -6.400 37.059 28.402 1.00 63.19 ? 300 PHE A CA 1 ATOM 2321 C C . PHE A 1 300 ? -7.075 35.758 28.012 1.00 72.62 ? 300 PHE A C 1 ATOM 2322 O O . PHE A 1 300 ? -7.299 35.491 26.832 1.00 70.89 ? 300 PHE A O 1 ATOM 2323 C CB . PHE A 1 300 ? -7.444 38.176 28.422 1.00 69.76 ? 300 PHE A CB 1 ATOM 2324 C CG . PHE A 1 300 ? -8.614 37.893 29.325 1.00 66.83 ? 300 PHE A CG 1 ATOM 2325 C CD1 . PHE A 1 300 ? -8.544 38.172 30.680 1.00 78.24 ? 300 PHE A CD1 1 ATOM 2326 C CD2 . PHE A 1 300 ? -9.784 37.350 28.819 1.00 75.30 ? 300 PHE A CD2 1 ATOM 2327 C CE1 . PHE A 1 300 ? -9.616 37.914 31.515 1.00 71.87 ? 300 PHE A CE1 1 ATOM 2328 C CE2 . PHE A 1 300 ? -10.860 37.088 29.649 1.00 76.89 ? 300 PHE A CE2 1 ATOM 2329 C CZ . PHE A 1 300 ? -10.775 37.372 30.998 1.00 75.26 ? 300 PHE A CZ 1 ATOM 2330 N N . MET A 1 301 ? -7.411 34.957 29.015 1.00 80.22 ? 301 MET A N 1 ATOM 2331 C CA . MET A 1 301 ? -8.058 33.680 28.769 1.00 80.21 ? 301 MET A CA 1 ATOM 2332 C C . MET A 1 301 ? -9.472 33.651 29.326 1.00 83.07 ? 301 MET A C 1 ATOM 2333 O O . MET A 1 301 ? -9.676 33.729 30.539 1.00 88.62 ? 301 MET A O 1 ATOM 2334 C CB . MET A 1 301 ? -7.234 32.539 29.366 1.00 70.11 ? 301 MET A CB 1 ATOM 2335 C CG . MET A 1 301 ? -5.804 32.488 28.857 1.00 69.58 ? 301 MET A CG 1 ATOM 2336 S SD . MET A 1 301 ? -4.862 31.104 29.520 1.00 91.21 ? 301 MET A SD 1 ATOM 2337 C CE . MET A 1 301 ? -5.059 31.365 31.280 1.00 83.76 ? 301 MET A CE 1 ATOM 2338 N N . ASP A 1 302 ? -10.447 33.550 28.429 1.00 71.61 ? 302 ASP A N 1 ATOM 2339 C CA . ASP A 1 302 ? -11.832 33.341 28.827 1.00 87.30 ? 302 ASP A CA 1 ATOM 2340 C C . ASP A 1 302 ? -12.104 31.845 28.881 1.00 76.26 ? 302 ASP A C 1 ATOM 2341 O O . ASP A 1 302 ? -11.179 31.039 28.789 1.00 89.91 ? 302 ASP A O 1 ATOM 2342 C CB . ASP A 1 302 ? -12.798 34.039 27.865 1.00 90.05 ? 302 ASP A CB 1 ATOM 2343 C CG . ASP A 1 302 ? -12.871 33.362 26.508 1.00 113.45 ? 302 ASP A CG 1 ATOM 2344 O OD1 . ASP A 1 302 ? -11.862 32.767 26.076 1.00 124.94 ? 302 ASP A OD1 1 ATOM 2345 O OD2 . ASP A 1 302 ? -13.943 33.428 25.871 1.00 121.92 ? 302 ASP A OD2 1 ATOM 2346 N N . ARG A 1 303 ? -13.368 31.471 29.032 1.00 78.60 ? 303 ARG A N 1 ATOM 2347 C CA . ARG A 1 303 ? -13.726 30.060 29.087 1.00 88.31 ? 303 ARG A CA 1 ATOM 2348 C C . ARG A 1 303 ? -14.650 29.692 27.937 1.00 99.94 ? 303 ARG A C 1 ATOM 2349 O O . ARG A 1 303 ? -15.669 30.346 27.714 1.00 107.83 ? 303 ARG A O 1 ATOM 2350 C CB . ARG A 1 303 ? -14.387 29.726 30.424 1.00 83.64 ? 303 ARG A CB 1 ATOM 2351 C CG . ARG A 1 303 ? -13.640 30.280 31.623 1.00 103.20 ? 303 ARG A CG 1 ATOM 2352 C CD . ARG A 1 303 ? -13.251 29.185 32.594 1.00 90.51 ? 303 ARG A CD 1 ATOM 2353 N NE . ARG A 1 303 ? -12.319 29.670 33.605 1.00 93.78 ? 303 ARG A NE 1 ATOM 2354 C CZ . ARG A 1 303 ? -11.747 28.900 34.522 1.00 108.32 ? 303 ARG A CZ 1 ATOM 2355 N NH1 . ARG A 1 303 ? -12.013 27.601 34.555 1.00 88.17 ? 303 ARG A NH1 1 ATOM 2356 N NH2 . ARG A 1 303 ? -10.909 29.428 35.404 1.00 122.97 ? 303 ARG A NH2 1 ATOM 2357 N N . GLY A 1 304 ? -14.291 28.641 27.209 1.00 83.59 ? 304 GLY A N 1 ATOM 2358 C CA . GLY A 1 304 ? -15.122 28.156 26.124 1.00 97.80 ? 304 GLY A CA 1 ATOM 2359 C C . GLY A 1 304 ? -16.372 27.489 26.661 1.00 103.46 ? 304 GLY A C 1 ATOM 2360 O O . GLY A 1 304 ? -16.622 27.508 27.866 1.00 108.81 ? 304 GLY A O 1 ATOM 2361 N N . SER A 1 305 ? -17.159 26.899 25.768 1.00 104.24 ? 305 SER A N 1 ATOM 2362 C CA . SER A 1 305 ? -18.374 26.200 26.168 1.00 95.77 ? 305 SER A CA 1 ATOM 2363 C C . SER A 1 305 ? -18.047 25.072 27.139 1.00 112.93 ? 305 SER A C 1 ATOM 2364 O O . SER A 1 305 ? -18.765 24.851 28.113 1.00 113.98 ? 305 SER A O 1 ATOM 2365 C CB . SER A 1 305 ? -19.104 25.650 24.943 1.00 104.39 ? 305 SER A CB 1 ATOM 2366 O OG . SER A 1 305 ? -19.361 26.678 24.003 1.00 128.25 ? 305 SER A OG 1 ATOM 2367 N N . ASP A 1 306 ? -16.948 24.373 26.871 1.00 132.11 ? 306 ASP A N 1 ATOM 2368 C CA . ASP A 1 306 ? -16.507 23.267 27.712 1.00 136.28 ? 306 ASP A CA 1 ATOM 2369 C C . ASP A 1 306 ? -16.161 23.745 29.118 1.00 121.73 ? 306 ASP A C 1 ATOM 2370 O O . ASP A 1 306 ? -16.329 23.015 30.094 1.00 123.30 ? 306 ASP A O 1 ATOM 2371 C CB . ASP A 1 306 ? -15.300 22.567 27.082 1.00 148.71 ? 306 ASP A CB 1 ATOM 2372 C CG . ASP A 1 306 ? -14.803 21.398 27.913 1.00 173.92 ? 306 ASP A CG 1 ATOM 2373 O OD1 . ASP A 1 306 ? -15.278 20.263 27.693 1.00 175.36 ? 306 ASP A OD1 1 ATOM 2374 O OD2 . ASP A 1 306 ? -13.937 21.614 28.786 1.00 184.10 ? 306 ASP A OD2 1 ATOM 2375 N N . GLY A 1 307 ? -15.681 24.979 29.213 1.00 106.41 ? 307 GLY A N 1 ATOM 2376 C CA . GLY A 1 307 ? -15.294 25.544 30.491 1.00 96.73 ? 307 GLY A CA 1 ATOM 2377 C C . GLY A 1 307 ? -13.790 25.619 30.653 1.00 101.16 ? 307 GLY A C 1 ATOM 2378 O O . GLY A 1 307 ? -13.292 26.230 31.596 1.00 97.22 ? 307 GLY A O 1 ATOM 2379 N N . LYS A 1 308 ? -13.060 24.998 29.732 1.00 104.51 ? 308 LYS A N 1 ATOM 2380 C CA . LYS A 1 308 ? -11.604 25.033 29.781 1.00 96.46 ? 308 LYS A CA 1 ATOM 2381 C C . LYS A 1 308 ? -11.092 26.403 29.372 1.00 89.99 ? 308 LYS A C 1 ATOM 2382 O O . LYS A 1 308 ? -11.685 27.068 28.523 1.00 96.81 ? 308 LYS A O 1 ATOM 2383 C CB . LYS A 1 308 ? -10.999 23.949 28.885 1.00 96.03 ? 308 LYS A CB 1 ATOM 2384 C CG . LYS A 1 308 ? -10.940 22.583 29.546 1.00 117.87 ? 308 LYS A CG 1 ATOM 2385 C CD . LYS A 1 308 ? -10.283 21.543 28.653 1.00 145.51 ? 308 LYS A CD 1 ATOM 2386 C CE . LYS A 1 308 ? -10.294 20.170 29.318 1.00 154.48 ? 308 LYS A CE 1 ATOM 2387 N NZ . LYS A 1 308 ? -9.710 19.110 28.449 1.00 142.34 ? 308 LYS A NZ 1 ATOM 2388 N N . LEU A 1 309 ? -9.995 26.826 29.992 1.00 106.97 ? 309 LEU A N 1 ATOM 2389 C CA . LEU A 1 309 ? -9.366 28.093 29.645 1.00 79.74 ? 309 LEU A CA 1 ATOM 2390 C C . LEU A 1 309 ? -8.836 28.058 28.222 1.00 84.11 ? 309 LEU A C 1 ATOM 2391 O O . LEU A 1 309 ? -8.302 27.046 27.766 1.00 95.02 ? 309 LEU A O 1 ATOM 2392 C CB . LEU A 1 309 ? -8.227 28.426 30.611 1.00 78.67 ? 309 LEU A CB 1 ATOM 2393 C CG . LEU A 1 309 ? -8.628 28.856 32.019 1.00 79.41 ? 309 LEU A CG 1 ATOM 2394 C CD1 . LEU A 1 309 ? -7.401 29.050 32.893 1.00 78.76 ? 309 LEU A CD1 1 ATOM 2395 C CD2 . LEU A 1 309 ? -9.450 30.127 31.955 1.00 87.53 ? 309 LEU A CD2 1 ATOM 2396 N N . GLN A 1 310 ? -9.004 29.172 27.524 1.00 77.94 ? 310 GLN A N 1 ATOM 2397 C CA . GLN A 1 310 ? -8.467 29.341 26.184 1.00 83.97 ? 310 GLN A CA 1 ATOM 2398 C C . GLN A 1 310 ? -8.053 30.792 26.038 1.00 77.21 ? 310 GLN A C 1 ATOM 2399 O O . GLN A 1 310 ? -8.750 31.681 26.519 1.00 81.21 ? 310 GLN A O 1 ATOM 2400 C CB . GLN A 1 310 ? -9.499 28.953 25.123 1.00 96.26 ? 310 GLN A CB 1 ATOM 2401 C CG . GLN A 1 310 ? -10.775 29.780 25.156 1.00 76.74 ? 310 GLN A CG 1 ATOM 2402 C CD . GLN A 1 310 ? -11.824 29.282 24.182 1.00 99.49 ? 310 GLN A CD 1 ATOM 2403 O OE1 . GLN A 1 310 ? -11.750 28.155 23.691 1.00 98.91 ? 310 GLN A OE1 1 ATOM 2404 N NE2 . GLN A 1 310 ? -12.810 30.125 23.897 1.00 100.62 ? 310 GLN A NE2 1 ATOM 2405 N N . GLU A 1 311 ? -6.929 31.049 25.380 1.00 76.52 ? 311 GLU A N 1 ATOM 2406 C CA . GLU A 1 311 ? -6.484 32.428 25.261 1.00 84.27 ? 311 GLU A CA 1 ATOM 2407 C C . GLU A 1 311 ? -7.018 33.025 23.969 1.00 85.32 ? 311 GLU A C 1 ATOM 2408 O O . GLU A 1 311 ? -6.546 32.700 22.880 1.00 79.68 ? 311 GLU A O 1 ATOM 2409 C CB . GLU A 1 311 ? -4.954 32.492 25.295 1.00 77.36 ? 311 GLU A CB 1 ATOM 2410 C CG . GLU A 1 311 ? -4.354 33.797 24.796 1.00 113.41 ? 311 GLU A CG 1 ATOM 2411 C CD . GLU A 1 311 ? -2.915 33.634 24.343 1.00 112.35 ? 311 GLU A CD 1 ATOM 2412 O OE1 . GLU A 1 311 ? -2.493 34.365 23.422 1.00 106.24 ? 311 GLU A OE1 1 ATOM 2413 O OE2 . GLU A 1 311 ? -2.207 32.772 24.905 1.00 109.23 ? 311 GLU A OE2 1 ATOM 2414 N N . VAL A 1 312 ? -8.037 33.870 24.094 1.00 75.23 ? 312 VAL A N 1 ATOM 2415 C CA . VAL A 1 312 ? -8.520 34.652 22.967 1.00 89.20 ? 312 VAL A CA 1 ATOM 2416 C C . VAL A 1 312 ? -8.145 36.131 23.031 1.00 74.52 ? 312 VAL A C 1 ATOM 2417 O O . VAL A 1 312 ? -8.339 36.861 22.062 1.00 64.81 ? 312 VAL A O 1 ATOM 2418 C CB . VAL A 1 312 ? -10.046 34.541 22.848 1.00 87.17 ? 312 VAL A CB 1 ATOM 2419 C CG1 . VAL A 1 312 ? -10.450 33.085 22.688 1.00 81.90 ? 312 VAL A CG1 1 ATOM 2420 C CG2 . VAL A 1 312 ? -10.713 35.152 24.068 1.00 71.58 ? 312 VAL A CG2 1 ATOM 2421 N N . GLY A 1 313 ? -7.601 36.564 24.165 1.00 88.57 ? 313 GLY A N 1 ATOM 2422 C CA . GLY A 1 313 ? -7.382 37.982 24.416 1.00 75.90 ? 313 GLY A CA 1 ATOM 2423 C C . GLY A 1 313 ? -8.676 38.722 24.726 1.00 72.43 ? 313 GLY A C 1 ATOM 2424 O O . GLY A 1 313 ? -9.759 38.237 24.402 1.00 81.32 ? 313 GLY A O 1 ATOM 2425 N N . GLN A 1 314 ? -8.575 39.899 25.341 1.00 81.06 ? 314 GLN A N 1 ATOM 2426 C CA . GLN A 1 314 ? -9.759 40.732 25.577 1.00 83.01 ? 314 GLN A CA 1 ATOM 2427 C C . GLN A 1 314 ? -9.414 42.216 25.725 1.00 81.88 ? 314 GLN A C 1 ATOM 2428 O O . GLN A 1 314 ? -8.272 42.582 26.010 1.00 60.28 ? 314 GLN A O 1 ATOM 2429 C CB . GLN A 1 314 ? -10.522 40.257 26.819 1.00 78.51 ? 314 GLN A CB 1 ATOM 2430 C CG . GLN A 1 314 ? -10.067 40.893 28.124 1.00 94.55 ? 314 GLN A CG 1 ATOM 2431 C CD . GLN A 1 314 ? -11.050 40.666 29.260 1.00 93.89 ? 314 GLN A CD 1 ATOM 2432 O OE1 . GLN A 1 314 ? -12.135 40.121 29.057 1.00 77.20 ? 314 GLN A OE1 1 ATOM 2433 N NE2 . GLN A 1 314 ? -10.674 41.087 30.463 1.00 108.60 ? 314 GLN A NE2 1 ATOM 2434 N N . VAL A 1 315 ? -10.418 43.066 25.533 1.00 81.03 ? 315 VAL A N 1 ATOM 2435 C CA . VAL A 1 315 ? -10.227 44.511 25.597 1.00 76.44 ? 315 VAL A CA 1 ATOM 2436 C C . VAL A 1 315 ? -11.202 45.161 26.573 1.00 93.27 ? 315 VAL A C 1 ATOM 2437 O O . VAL A 1 315 ? -12.411 44.952 26.488 1.00 91.38 ? 315 VAL A O 1 ATOM 2438 C CB . VAL A 1 315 ? -10.401 45.162 24.211 1.00 76.22 ? 315 VAL A CB 1 ATOM 2439 C CG1 . VAL A 1 315 ? -10.386 46.677 24.327 1.00 91.87 ? 315 VAL A CG1 1 ATOM 2440 C CG2 . VAL A 1 315 ? -9.316 44.686 23.259 1.00 89.47 ? 315 VAL A CG2 1 ATOM 2441 N N . SER A 1 316 ? -10.667 45.949 27.500 1.00 99.57 ? 316 SER A N 1 ATOM 2442 C CA . SER A 1 316 ? -11.491 46.662 28.467 1.00 86.53 ? 316 SER A CA 1 ATOM 2443 C C . SER A 1 316 ? -11.985 47.985 27.892 1.00 93.56 ? 316 SER A C 1 ATOM 2444 O O . SER A 1 316 ? -11.187 48.828 27.481 1.00 90.58 ? 316 SER A O 1 ATOM 2445 C CB . SER A 1 316 ? -10.707 46.908 29.758 1.00 87.78 ? 316 SER A CB 1 ATOM 2446 O OG . SER A 1 316 ? -11.462 47.671 30.682 1.00 84.84 ? 316 SER A OG 1 ATOM 2447 N N . VAL A 1 317 ? -13.302 48.159 27.859 1.00 101.95 ? 317 VAL A N 1 ATOM 2448 C CA . VAL A 1 317 ? -13.896 49.406 27.384 1.00 88.34 ? 317 VAL A CA 1 ATOM 2449 C C . VAL A 1 317 ? -14.524 50.187 28.534 1.00 89.50 ? 317 VAL A C 1 ATOM 2450 O O . VAL A 1 317 ? -15.547 49.784 29.085 1.00 95.39 ? 317 VAL A O 1 ATOM 2451 C CB . VAL A 1 317 ? -14.962 49.146 26.307 1.00 77.35 ? 317 VAL A CB 1 ATOM 2452 C CG1 . VAL A 1 317 ? -15.733 50.420 26.003 1.00 80.75 ? 317 VAL A CG1 1 ATOM 2453 C CG2 . VAL A 1 317 ? -14.313 48.596 25.049 1.00 74.26 ? 317 VAL A CG2 1 ATOM 2454 N N . SER A 1 318 ? -13.905 51.309 28.887 1.00 87.08 ? 318 SER A N 1 ATOM 2455 C CA . SER A 1 318 ? -14.368 52.110 30.013 1.00 93.17 ? 318 SER A CA 1 ATOM 2456 C C . SER A 1 318 ? -14.896 53.467 29.563 1.00 91.74 ? 318 SER A C 1 ATOM 2457 O O . SER A 1 318 ? -14.131 54.332 29.133 1.00 88.02 ? 318 SER A O 1 ATOM 2458 C CB . SER A 1 318 ? -13.240 52.301 31.028 1.00 91.94 ? 318 SER A CB 1 ATOM 2459 O OG . SER A 1 318 ? -12.781 51.055 31.518 1.00 88.65 ? 318 SER A OG 1 ATOM 2460 N N . LEU A 1 319 ? -16.207 53.650 29.675 1.00 91.76 ? 319 LEU A N 1 ATOM 2461 C CA . LEU A 1 319 ? -16.838 54.910 29.307 1.00 94.95 ? 319 LEU A CA 1 ATOM 2462 C C . LEU A 1 319 ? -16.769 55.908 30.455 1.00 102.30 ? 319 LEU A C 1 ATOM 2463 O O . LEU A 1 319 ? -17.188 55.608 31.572 1.00 108.38 ? 319 LEU A O 1 ATOM 2464 C CB . LEU A 1 319 ? -18.294 54.684 28.901 1.00 95.92 ? 319 LEU A CB 1 ATOM 2465 C CG . LEU A 1 319 ? -18.532 53.721 27.740 1.00 92.43 ? 319 LEU A CG 1 ATOM 2466 C CD1 . LEU A 1 319 ? -20.008 53.684 27.377 1.00 96.06 ? 319 LEU A CD1 1 ATOM 2467 C CD2 . LEU A 1 319 ? -17.683 54.114 26.543 1.00 88.98 ? 319 LEU A CD2 1 ATOM 2468 N N . GLN A 1 320 ? -16.243 57.095 30.178 1.00 106.01 ? 320 GLN A N 1 ATOM 2469 C CA . GLN A 1 320 ? -16.133 58.121 31.206 1.00 107.42 ? 320 GLN A CA 1 ATOM 2470 C C . GLN A 1 320 ? -17.455 58.831 31.438 1.00 114.13 ? 320 GLN A C 1 ATOM 2471 O O . GLN A 1 320 ? -18.113 59.269 30.494 1.00 106.35 ? 320 GLN A O 1 ATOM 2472 C CB . GLN A 1 320 ? -15.064 59.149 30.840 1.00 106.01 ? 320 GLN A CB 1 ATOM 2473 C CG . GLN A 1 320 ? -14.983 60.304 31.821 1.00 107.18 ? 320 GLN A CG 1 ATOM 2474 C CD . GLN A 1 320 ? -13.995 61.371 31.399 1.00 100.94 ? 320 GLN A CD 1 ATOM 2475 O OE1 . GLN A 1 320 ? -13.930 62.440 32.005 1.00 107.77 ? 320 GLN A OE1 1 ATOM 2476 N NE2 . GLN A 1 320 ? -13.219 61.089 30.358 1.00 90.68 ? 320 GLN A NE2 1 ATOM 2477 N N . ARG A 1 321 ? -17.837 58.940 32.705 1.00 129.07 ? 321 ARG A N 1 ATOM 2478 C CA . ARG A 1 321 ? -19.012 59.707 33.087 1.00 132.71 ? 321 ARG A CA 1 ATOM 2479 C C . ARG A 1 321 ? -18.579 61.049 33.656 1.00 137.01 ? 321 ARG A C 1 ATOM 2480 O O . ARG A 1 321 ? -17.536 61.149 34.304 1.00 140.50 ? 321 ARG A O 1 ATOM 2481 C CB . ARG A 1 321 ? -19.856 58.940 34.103 1.00 138.93 ? 321 ARG A CB 1 ATOM 2482 C CG . ARG A 1 321 ? -20.290 57.568 33.626 1.00 142.75 ? 321 ARG A CG 1 ATOM 2483 C CD . ARG A 1 321 ? -21.271 56.934 34.592 1.00 157.55 ? 321 ARG A CD 1 ATOM 2484 N NE . ARG A 1 321 ? -21.671 55.600 34.157 1.00 167.01 ? 321 ARG A NE 1 ATOM 2485 C CZ . ARG A 1 321 ? -22.610 54.872 34.751 1.00 176.28 ? 321 ARG A CZ 1 ATOM 2486 N NH1 . ARG A 1 321 ? -23.255 55.350 35.807 1.00 180.42 ? 321 ARG A NH1 1 ATOM 2487 N NH2 . ARG A 1 321 ? -22.908 53.666 34.286 1.00 175.79 ? 321 ARG A NH2 1 ATOM 2488 N N . ALA A 1 322 ? -19.378 62.081 33.406 1.00 139.66 ? 322 ALA A N 1 ATOM 2489 C CA . ALA A 1 322 ? -19.072 63.423 33.888 1.00 145.02 ? 322 ALA A CA 1 ATOM 2490 C C . ALA A 1 322 ? -18.964 63.459 35.409 1.00 152.05 ? 322 ALA A C 1 ATOM 2491 O O . ALA A 1 322 ? -18.308 64.332 35.976 1.00 159.04 ? 322 ALA A O 1 ATOM 2492 C CB . ALA A 1 322 ? -20.129 64.406 33.412 1.00 135.80 ? 322 ALA A CB 1 ATOM 2493 N N . SER A 1 323 ? -19.612 62.501 36.062 1.00 142.28 ? 323 SER A N 1 ATOM 2494 C CA . SER A 1 323 ? -19.685 62.468 37.515 1.00 146.80 ? 323 SER A CA 1 ATOM 2495 C C . SER A 1 323 ? -18.446 61.893 38.200 1.00 141.57 ? 323 SER A C 1 ATOM 2496 O O . SER A 1 323 ? -17.995 62.422 39.216 1.00 151.49 ? 323 SER A O 1 ATOM 2497 C CB . SER A 1 323 ? -20.915 61.669 37.951 1.00 144.94 ? 323 SER A CB 1 ATOM 2498 O OG . SER A 1 323 ? -20.842 60.334 37.483 1.00 138.14 ? 323 SER A OG 1 ATOM 2499 N N . GLY A 1 324 ? -17.885 60.825 37.644 1.00 142.16 ? 324 GLY A N 1 ATOM 2500 C CA . GLY A 1 324 ? -16.972 59.997 38.413 1.00 160.05 ? 324 GLY A CA 1 ATOM 2501 C C . GLY A 1 324 ? -16.557 58.703 37.743 1.00 160.48 ? 324 GLY A C 1 ATOM 2502 O O . GLY A 1 324 ? -16.474 58.626 36.516 1.00 153.37 ? 324 GLY A O 1 ATOM 2503 N N . ASP A 1 325 ? -16.270 57.697 38.566 1.00 171.63 ? 325 ASP A N 1 ATOM 2504 C CA . ASP A 1 325 ? -15.725 56.421 38.111 1.00 177.41 ? 325 ASP A CA 1 ATOM 2505 C C . ASP A 1 325 ? -16.524 55.816 36.964 1.00 161.63 ? 325 ASP A C 1 ATOM 2506 O O . ASP A 1 325 ? -17.747 55.933 36.899 1.00 164.32 ? 325 ASP A O 1 ATOM 2507 C CB . ASP A 1 325 ? -15.656 55.426 39.271 1.00 191.88 ? 325 ASP A CB 1 ATOM 2508 C CG . ASP A 1 325 ? -14.610 55.805 40.300 1.00 200.98 ? 325 ASP A CG 1 ATOM 2509 O OD1 . ASP A 1 325 ? -13.635 56.492 39.931 1.00 204.05 ? 325 ASP A OD1 1 ATOM 2510 O OD2 . ASP A 1 325 ? -14.760 55.412 41.476 1.00 202.33 ? 325 ASP A OD2 1 ATOM 2511 N N . PHE A 1 326 ? -15.798 55.169 36.062 1.00 132.89 ? 326 PHE A N 1 ATOM 2512 C CA . PHE A 1 326 ? -16.285 54.845 34.731 1.00 113.63 ? 326 PHE A CA 1 ATOM 2513 C C . PHE A 1 326 ? -17.340 53.749 34.696 1.00 114.94 ? 326 PHE A C 1 ATOM 2514 O O . PHE A 1 326 ? -17.712 53.182 35.722 1.00 124.06 ? 326 PHE A O 1 ATOM 2515 C CB . PHE A 1 326 ? -15.107 54.418 33.846 1.00 103.72 ? 326 PHE A CB 1 ATOM 2516 C CG . PHE A 1 326 ? -13.928 55.353 33.902 1.00 102.81 ? 326 PHE A CG 1 ATOM 2517 C CD1 . PHE A 1 326 ? -13.020 55.292 34.948 1.00 101.11 ? 326 PHE A CD1 1 ATOM 2518 C CD2 . PHE A 1 326 ? -13.716 56.278 32.896 1.00 102.36 ? 326 PHE A CD2 1 ATOM 2519 C CE1 . PHE A 1 326 ? -11.940 56.147 34.997 1.00 98.28 ? 326 PHE A CE1 1 ATOM 2520 C CE2 . PHE A 1 326 ? -12.635 57.135 32.938 1.00 90.11 ? 326 PHE A CE2 1 ATOM 2521 C CZ . PHE A 1 326 ? -11.746 57.069 33.989 1.00 96.62 ? 326 PHE A CZ 1 ATOM 2522 N N . GLN A 1 327 ? -17.815 53.470 33.487 1.00 107.18 ? 327 GLN A N 1 ATOM 2523 C CA . GLN A 1 327 ? -18.619 52.291 33.206 1.00 108.90 ? 327 GLN A CA 1 ATOM 2524 C C . GLN A 1 327 ? -17.808 51.374 32.305 1.00 103.83 ? 327 GLN A C 1 ATOM 2525 O O . GLN A 1 327 ? -17.561 51.697 31.143 1.00 111.23 ? 327 GLN A O 1 ATOM 2526 C CB . GLN A 1 327 ? -19.941 52.662 32.536 1.00 119.07 ? 327 GLN A CB 1 ATOM 2527 C CG . GLN A 1 327 ? -20.681 51.463 31.967 1.00 137.16 ? 327 GLN A CG 1 ATOM 2528 C CD . GLN A 1 327 ? -21.722 51.849 30.938 1.00 136.17 ? 327 GLN A CD 1 ATOM 2529 O OE1 . GLN A 1 327 ? -22.366 52.893 31.049 1.00 135.48 ? 327 GLN A OE1 1 ATOM 2530 N NE2 . GLN A 1 327 ? -21.887 51.010 29.921 1.00 129.44 ? 327 GLN A NE2 1 ATOM 2531 N N . THR A 1 328 ? -17.391 50.233 32.839 1.00 101.32 ? 328 THR A N 1 ATOM 2532 C CA . THR A 1 328 ? -16.453 49.373 32.133 1.00 88.18 ? 328 THR A CA 1 ATOM 2533 C C . THR A 1 328 ? -17.101 48.083 31.639 1.00 96.56 ? 328 THR A C 1 ATOM 2534 O O . THR A 1 328 ? -17.770 47.382 32.397 1.00 104.65 ? 328 THR A O 1 ATOM 2535 C CB . THR A 1 328 ? -15.247 49.028 33.031 1.00 91.49 ? 328 THR A CB 1 ATOM 2536 O OG1 . THR A 1 328 ? -14.580 50.236 33.420 1.00 90.35 ? 328 THR A OG1 1 ATOM 2537 C CG2 . THR A 1 328 ? -14.267 48.135 32.295 1.00 98.69 ? 328 THR A CG2 1 ATOM 2538 N N . THR A 1 329 ? -16.903 47.785 30.358 1.00 102.46 ? 329 THR A N 1 ATOM 2539 C CA . THR A 1 329 ? -17.363 46.533 29.763 1.00 88.04 ? 329 THR A CA 1 ATOM 2540 C C . THR A 1 329 ? -16.196 45.764 29.150 1.00 84.50 ? 329 THR A C 1 ATOM 2541 O O . THR A 1 329 ? -15.164 46.347 28.814 1.00 103.90 ? 329 THR A O 1 ATOM 2542 C CB . THR A 1 329 ? -18.424 46.774 28.678 1.00 88.81 ? 329 THR A CB 1 ATOM 2543 O OG1 . THR A 1 329 ? -17.871 47.596 27.643 1.00 93.48 ? 329 THR A OG1 1 ATOM 2544 C CG2 . THR A 1 329 ? -19.642 47.463 29.269 1.00 106.00 ? 329 THR A CG2 1 ATOM 2545 N N . LYS A 1 330 ? -16.363 44.455 29.004 1.00 78.64 ? 330 LYS A N 1 ATOM 2546 C CA . LYS A 1 330 ? -15.306 43.607 28.463 1.00 76.55 ? 330 LYS A CA 1 ATOM 2547 C C . LYS A 1 330 ? -15.668 43.061 27.086 1.00 83.15 ? 330 LYS A C 1 ATOM 2548 O O . LYS A 1 330 ? -16.800 42.635 26.850 1.00 100.62 ? 330 LYS A O 1 ATOM 2549 C CB . LYS A 1 330 ? -15.004 42.446 29.414 1.00 75.21 ? 330 LYS A CB 1 ATOM 2550 C CG . LYS A 1 330 ? -13.886 42.713 30.412 1.00 80.37 ? 330 LYS A CG 1 ATOM 2551 C CD . LYS A 1 330 ? -14.252 43.804 31.407 1.00 81.27 ? 330 LYS A CD 1 ATOM 2552 C CE . LYS A 1 330 ? -13.193 43.935 32.493 1.00 83.61 ? 330 LYS A CE 1 ATOM 2553 N NZ . LYS A 1 330 ? -12.990 42.653 33.231 1.00 97.29 ? 330 LYS A NZ 1 ATOM 2554 N N . LEU A 1 331 ? -14.697 43.083 26.180 1.00 79.66 ? 331 LEU A N 1 ATOM 2555 C CA . LEU A 1 331 ? -14.880 42.521 24.849 1.00 70.62 ? 331 LEU A CA 1 ATOM 2556 C C . LEU A 1 331 ? -13.865 41.411 24.599 1.00 68.49 ? 331 LEU A C 1 ATOM 2557 O O . LEU A 1 331 ? -12.669 41.670 24.459 1.00 68.04 ? 331 LEU A O 1 ATOM 2558 C CB . LEU A 1 331 ? -14.752 43.616 23.789 1.00 70.19 ? 331 LEU A CB 1 ATOM 2559 C CG . LEU A 1 331 ? -14.902 43.214 22.323 1.00 77.90 ? 331 LEU A CG 1 ATOM 2560 C CD1 . LEU A 1 331 ? -16.300 42.691 22.043 1.00 100.04 ? 331 LEU A CD1 1 ATOM 2561 C CD2 . LEU A 1 331 ? -14.579 44.391 21.420 1.00 84.53 ? 331 LEU A CD2 1 ATOM 2562 N N . ASN A 1 332 ? -14.352 40.176 24.545 1.00 69.92 ? 332 ASN A N 1 ATOM 2563 C CA . ASN A 1 332 ? -13.497 39.014 24.327 1.00 69.29 ? 332 ASN A CA 1 ATOM 2564 C C . ASN A 1 332 ? -13.141 38.794 22.859 1.00 81.09 ? 332 ASN A C 1 ATOM 2565 O O . ASN A 1 332 ? -13.857 39.241 21.963 1.00 97.72 ? 332 ASN A O 1 ATOM 2566 C CB . ASN A 1 332 ? -14.161 37.762 24.896 1.00 92.05 ? 332 ASN A CB 1 ATOM 2567 C CG . ASN A 1 332 ? -14.174 37.753 26.410 1.00 95.92 ? 332 ASN A CG 1 ATOM 2568 O OD1 . ASN A 1 332 ? -13.831 38.748 27.048 1.00 78.03 ? 332 ASN A OD1 1 ATOM 2569 N ND2 . ASN A 1 332 ? -14.574 36.630 26.995 1.00 98.50 ? 332 ASN A ND2 1 ATOM 2570 N N . GLY A 1 333 ? -12.031 38.100 22.624 1.00 78.98 ? 333 GLY A N 1 ATOM 2571 C CA . GLY A 1 333 ? -11.582 37.798 21.276 1.00 77.84 ? 333 GLY A CA 1 ATOM 2572 C C . GLY A 1 333 ? -12.394 36.693 20.622 1.00 100.63 ? 333 GLY A C 1 ATOM 2573 O O . GLY A 1 333 ? -13.502 36.383 21.060 1.00 107.16 ? 333 GLY A O 1 ATOM 2574 N N . PHE A 1 334 ? -11.847 36.099 19.567 1.00 101.19 ? 334 PHE A N 1 ATOM 2575 C CA . PHE A 1 334 ? -12.578 35.102 18.789 1.00 84.09 ? 334 PHE A CA 1 ATOM 2576 C C . PHE A 1 334 ? -11.776 33.813 18.599 1.00 74.16 ? 334 PHE A C 1 ATOM 2577 O O . PHE A 1 334 ? -12.191 32.743 19.044 1.00 110.62 ? 334 PHE A O 1 ATOM 2578 C CB . PHE A 1 334 ? -12.973 35.684 17.430 1.00 94.33 ? 334 PHE A CB 1 ATOM 2579 C CG . PHE A 1 334 ? -13.726 36.985 17.521 1.00 80.37 ? 334 PHE A CG 1 ATOM 2580 C CD1 . PHE A 1 334 ? -15.108 36.997 17.614 1.00 76.22 ? 334 PHE A CD1 1 ATOM 2581 C CD2 . PHE A 1 334 ? -13.051 38.195 17.508 1.00 85.39 ? 334 PHE A CD2 1 ATOM 2582 C CE1 . PHE A 1 334 ? -15.804 38.190 17.694 1.00 86.66 ? 334 PHE A CE1 1 ATOM 2583 C CE2 . PHE A 1 334 ? -13.741 39.392 17.590 1.00 94.45 ? 334 PHE A CE2 1 ATOM 2584 C CZ . PHE A 1 334 ? -15.120 39.389 17.683 1.00 80.83 ? 334 PHE A CZ 1 ATOM 2585 N N . GLU A 1 335 ? -10.638 33.924 17.921 1.00 79.22 ? 335 GLU A N 1 ATOM 2586 C CA . GLU A 1 335 ? -9.754 32.786 17.678 1.00 73.94 ? 335 GLU A CA 1 ATOM 2587 C C . GLU A 1 335 ? -8.683 32.683 18.762 1.00 72.12 ? 335 GLU A C 1 ATOM 2588 O O . GLU A 1 335 ? -8.220 33.696 19.285 1.00 87.00 ? 335 GLU A O 1 ATOM 2589 C CB . GLU A 1 335 ? -9.087 32.899 16.305 1.00 74.40 ? 335 GLU A CB 1 ATOM 2590 C CG . GLU A 1 335 ? -10.045 32.929 15.128 1.00 101.55 ? 335 GLU A CG 1 ATOM 2591 C CD . GLU A 1 335 ? -9.322 32.953 13.796 1.00 106.98 ? 335 GLU A CD 1 ATOM 2592 O OE1 . GLU A 1 335 ? -9.958 32.654 12.762 1.00 133.66 ? 335 GLU A OE1 1 ATOM 2593 O OE2 . GLU A 1 335 ? -8.114 33.268 13.783 1.00 88.17 ? 335 GLU A OE2 1 ATOM 2594 N N . VAL A 1 336 ? -8.303 31.456 19.105 1.00 88.81 ? 336 VAL A N 1 ATOM 2595 C CA . VAL A 1 336 ? -7.271 31.232 20.113 1.00 72.19 ? 336 VAL A CA 1 ATOM 2596 C C . VAL A 1 336 ? -5.882 31.580 19.590 1.00 70.86 ? 336 VAL A C 1 ATOM 2597 O O . VAL A 1 336 ? -5.589 31.394 18.407 1.00 88.61 ? 336 VAL A O 1 ATOM 2598 C CB . VAL A 1 336 ? -7.270 29.776 20.601 1.00 76.65 ? 336 VAL A CB 1 ATOM 2599 C CG1 . VAL A 1 336 ? -8.511 29.501 21.430 1.00 75.57 ? 336 VAL A CG1 1 ATOM 2600 C CG2 . VAL A 1 336 ? -7.187 28.824 19.418 1.00 113.61 ? 336 VAL A CG2 1 ATOM 2601 N N . PHE A 1 337 ? -5.042 32.092 20.488 1.00 77.64 ? 337 PHE A N 1 ATOM 2602 C CA . PHE A 1 337 ? -3.681 32.536 20.175 1.00 87.36 ? 337 PHE A CA 1 ATOM 2603 C C . PHE A 1 337 ? -3.650 33.647 19.130 1.00 90.35 ? 337 PHE A C 1 ATOM 2604 O O . PHE A 1 337 ? -2.629 33.870 18.480 1.00 109.82 ? 337 PHE A O 1 ATOM 2605 C CB . PHE A 1 337 ? -2.830 31.360 19.694 1.00 87.46 ? 337 PHE A CB 1 ATOM 2606 C CG . PHE A 1 337 ? -2.628 30.300 20.728 1.00 70.50 ? 337 PHE A CG 1 ATOM 2607 C CD1 . PHE A 1 337 ? -2.534 30.634 22.068 1.00 69.26 ? 337 PHE A CD1 1 ATOM 2608 C CD2 . PHE A 1 337 ? -2.537 28.968 20.364 1.00 96.40 ? 337 PHE A CD2 1 ATOM 2609 C CE1 . PHE A 1 337 ? -2.346 29.657 23.027 1.00 102.34 ? 337 PHE A CE1 1 ATOM 2610 C CE2 . PHE A 1 337 ? -2.351 27.985 21.318 1.00 96.81 ? 337 PHE A CE2 1 ATOM 2611 C CZ . PHE A 1 337 ? -2.256 28.330 22.652 1.00 96.06 ? 337 PHE A CZ 1 ATOM 2612 N N . ALA A 1 338 ? -4.764 34.352 18.985 1.00 82.31 ? 338 ALA A N 1 ATOM 2613 C CA . ALA A 1 338 ? -4.856 35.423 18.010 1.00 65.74 ? 338 ALA A CA 1 ATOM 2614 C C . ALA A 1 338 ? -4.388 36.733 18.625 1.00 67.85 ? 338 ALA A C 1 ATOM 2615 O O . ALA A 1 338 ? -4.102 37.694 17.912 1.00 70.76 ? 338 ALA A O 1 ATOM 2616 C CB . ALA A 1 338 ? -6.280 35.547 17.493 1.00 67.13 ? 338 ALA A CB 1 ATOM 2617 N N . ARG A 1 339 ? -4.290 36.744 19.953 1.00 88.33 ? 339 ARG A N 1 ATOM 2618 C CA . ARG A 1 339 ? -3.916 37.937 20.714 1.00 102.28 ? 339 ARG A CA 1 ATOM 2619 C C . ARG A 1 339 ? -4.744 39.149 20.290 1.00 66.41 ? 339 ARG A C 1 ATOM 2620 O O . ARG A 1 339 ? -4.237 40.081 19.674 1.00 67.78 ? 339 ARG A O 1 ATOM 2621 C CB . ARG A 1 339 ? -2.419 38.211 20.568 1.00 59.23 ? 339 ARG A CB 1 ATOM 2622 C CG . ARG A 1 339 ? -1.568 37.054 21.068 1.00 69.65 ? 339 ARG A CG 1 ATOM 2623 C CD . ARG A 1 339 ? -0.091 37.387 21.119 1.00 58.77 ? 339 ARG A CD 1 ATOM 2624 N NE . ARG A 1 339 ? 0.694 36.257 21.607 1.00 59.68 ? 339 ARG A NE 1 ATOM 2625 C CZ . ARG A 1 339 ? 2.014 36.265 21.756 1.00 80.15 ? 339 ARG A CZ 1 ATOM 2626 N NH1 . ARG A 1 339 ? 2.714 37.352 21.458 1.00 94.93 ? 339 ARG A NH1 1 ATOM 2627 N NH2 . ARG A 1 339 ? 2.635 35.184 22.204 1.00 82.60 ? 339 ARG A NH2 1 ATOM 2628 N N . PHE A 1 340 ? -6.026 39.107 20.639 1.00 64.63 ? 340 PHE A N 1 ATOM 2629 C CA . PHE A 1 340 ? -7.027 40.065 20.184 1.00 61.40 ? 340 PHE A CA 1 ATOM 2630 C C . PHE A 1 340 ? -6.759 41.512 20.593 1.00 76.97 ? 340 PHE A C 1 ATOM 2631 O O . PHE A 1 340 ? -7.011 42.430 19.818 1.00 80.87 ? 340 PHE A O 1 ATOM 2632 C CB . PHE A 1 340 ? -8.402 39.634 20.699 1.00 65.04 ? 340 PHE A CB 1 ATOM 2633 C CG . PHE A 1 340 ? -9.498 40.612 20.408 1.00 63.64 ? 340 PHE A CG 1 ATOM 2634 C CD1 . PHE A 1 340 ? -9.940 40.815 19.113 1.00 64.81 ? 340 PHE A CD1 1 ATOM 2635 C CD2 . PHE A 1 340 ? -10.105 41.312 21.436 1.00 69.89 ? 340 PHE A CD2 1 ATOM 2636 C CE1 . PHE A 1 340 ? -10.956 41.712 18.845 1.00 73.56 ? 340 PHE A CE1 1 ATOM 2637 C CE2 . PHE A 1 340 ? -11.121 42.209 21.176 1.00 80.80 ? 340 PHE A CE2 1 ATOM 2638 C CZ . PHE A 1 340 ? -11.548 42.409 19.879 1.00 81.46 ? 340 PHE A CZ 1 ATOM 2639 N N . GLY A 1 341 ? -6.253 41.724 21.801 1.00 68.33 ? 341 GLY A N 1 ATOM 2640 C CA . GLY A 1 341 ? -6.075 43.079 22.293 1.00 87.41 ? 341 GLY A CA 1 ATOM 2641 C C . GLY A 1 341 ? -4.736 43.718 21.964 1.00 92.27 ? 341 GLY A C 1 ATOM 2642 O O . GLY A 1 341 ? -4.347 44.703 22.592 1.00 108.63 ? 341 GLY A O 1 ATOM 2643 N N . SER A 1 342 ? -4.040 43.170 20.972 1.00 73.36 ? 342 SER A N 1 ATOM 2644 C CA . SER A 1 342 ? -2.665 43.571 20.680 1.00 72.18 ? 342 SER A CA 1 ATOM 2645 C C . SER A 1 342 ? -2.522 45.042 20.311 1.00 68.17 ? 342 SER A C 1 ATOM 2646 O O . SER A 1 342 ? -1.621 45.722 20.795 1.00 73.00 ? 342 SER A O 1 ATOM 2647 C CB . SER A 1 342 ? -2.091 42.713 19.554 1.00 73.32 ? 342 SER A CB 1 ATOM 2648 O OG . SER A 1 342 ? -1.887 41.379 19.979 1.00 98.10 ? 342 SER A OG 1 ATOM 2649 N N . ALA A 1 343 ? -3.401 45.528 19.445 1.00 64.75 ? 343 ALA A N 1 ATOM 2650 C CA . ALA A 1 343 ? -3.339 46.920 19.021 1.00 57.41 ? 343 ALA A CA 1 ATOM 2651 C C . ALA A 1 343 ? -4.729 47.531 18.953 1.00 76.54 ? 343 ALA A C 1 ATOM 2652 O O . ALA A 1 343 ? -5.645 46.954 18.367 1.00 75.28 ? 343 ALA A O 1 ATOM 2653 C CB . ALA A 1 343 ? -2.642 47.034 17.678 1.00 57.19 ? 343 ALA A CB 1 ATOM 2654 N N . ILE A 1 344 ? -4.880 48.702 19.562 1.00 90.48 ? 344 ILE A N 1 ATOM 2655 C CA . ILE A 1 344 ? -6.152 49.406 19.557 1.00 59.13 ? 344 ILE A CA 1 ATOM 2656 C C . ILE A 1 344 ? -5.996 50.759 18.884 1.00 61.87 ? 344 ILE A C 1 ATOM 2657 O O . ILE A 1 344 ? -5.329 51.649 19.411 1.00 85.43 ? 344 ILE A O 1 ATOM 2658 C CB . ILE A 1 344 ? -6.690 49.605 20.980 1.00 60.13 ? 344 ILE A CB 1 ATOM 2659 C CG1 . ILE A 1 344 ? -6.641 48.290 21.758 1.00 60.28 ? 344 ILE A CG1 1 ATOM 2660 C CG2 . ILE A 1 344 ? -8.103 50.149 20.938 1.00 77.47 ? 344 ILE A CG2 1 ATOM 2661 C CD1 . ILE A 1 344 ? -7.115 48.413 23.189 1.00 75.11 ? 344 ILE A CD1 1 ATOM 2662 N N . ALA A 1 345 ? -6.609 50.911 17.715 1.00 70.10 ? 345 ALA A N 1 ATOM 2663 C CA . ALA A 1 345 ? -6.491 52.147 16.953 1.00 84.13 ? 345 ALA A CA 1 ATOM 2664 C C . ALA A 1 345 ? -7.830 52.854 16.797 1.00 76.29 ? 345 ALA A C 1 ATOM 2665 O O . ALA A 1 345 ? -8.745 52.326 16.167 1.00 76.32 ? 345 ALA A O 1 ATOM 2666 C CB . ALA A 1 345 ? -5.886 51.869 15.589 1.00 60.31 ? 345 ALA A CB 1 ATOM 2667 N N . PRO A 1 346 ? -7.951 54.052 17.384 1.00 79.63 ? 346 PRO A N 1 ATOM 2668 C CA . PRO A 1 346 ? -9.128 54.888 17.141 1.00 70.76 ? 346 PRO A CA 1 ATOM 2669 C C . PRO A 1 346 ? -9.106 55.412 15.717 1.00 70.97 ? 346 PRO A C 1 ATOM 2670 O O . PRO A 1 346 ? -8.048 55.856 15.272 1.00 68.27 ? 346 PRO A O 1 ATOM 2671 C CB . PRO A 1 346 ? -8.967 56.035 18.144 1.00 66.51 ? 346 PRO A CB 1 ATOM 2672 C CG . PRO A 1 346 ? -7.904 55.589 19.106 1.00 65.37 ? 346 PRO A CG 1 ATOM 2673 C CD . PRO A 1 346 ? -7.014 54.685 18.324 1.00 70.10 ? 346 PRO A CD 1 ATOM 2674 N N . LEU A 1 347 ? -10.221 55.343 14.999 1.00 84.00 ? 347 LEU A N 1 ATOM 2675 C CA . LEU A 1 347 ? -10.274 56.009 13.705 1.00 92.25 ? 347 LEU A CA 1 ATOM 2676 C C . LEU A 1 347 ? -11.514 56.877 13.534 1.00 81.59 ? 347 LEU A C 1 ATOM 2677 O O . LEU A 1 347 ? -12.610 56.367 13.317 1.00 117.72 ? 347 LEU A O 1 ATOM 2678 C CB . LEU A 1 347 ? -10.208 54.964 12.588 1.00 84.83 ? 347 LEU A CB 1 ATOM 2679 C CG . LEU A 1 347 ? -10.675 53.547 12.955 1.00 68.61 ? 347 LEU A CG 1 ATOM 2680 C CD1 . LEU A 1 347 ? -12.180 53.372 12.819 1.00 66.55 ? 347 LEU A CD1 1 ATOM 2681 C CD2 . LEU A 1 347 ? -9.946 52.510 12.120 1.00 85.15 ? 347 LEU A CD2 1 ATOM 2682 N N . GLY A 1 348 ? -11.317 58.189 13.617 1.00 73.29 ? 348 GLY A N 1 ATOM 2683 C CA . GLY A 1 348 ? -12.288 59.176 13.179 1.00 110.71 ? 348 GLY A CA 1 ATOM 2684 C C . GLY A 1 348 ? -13.715 58.886 13.588 1.00 109.62 ? 348 GLY A C 1 ATOM 2685 O O . GLY A 1 348 ? -13.983 58.352 14.663 1.00 97.59 ? 348 GLY A O 1 ATOM 2686 N N . ASP A 1 349 ? -14.629 59.244 12.694 1.00 119.10 ? 349 ASP A N 1 ATOM 2687 C CA . ASP A 1 349 ? -15.922 58.595 12.593 1.00 89.96 ? 349 ASP A CA 1 ATOM 2688 C C . ASP A 1 349 ? -15.914 57.951 11.213 1.00 89.02 ? 349 ASP A C 1 ATOM 2689 O O . ASP A 1 349 ? -16.012 58.642 10.199 1.00 82.61 ? 349 ASP A O 1 ATOM 2690 C CB . ASP A 1 349 ? -17.070 59.593 12.757 1.00 90.92 ? 349 ASP A CB 1 ATOM 2691 C CG . ASP A 1 349 ? -18.435 58.935 12.687 1.00 123.93 ? 349 ASP A CG 1 ATOM 2692 O OD1 . ASP A 1 349 ? -18.512 57.695 12.814 1.00 131.28 ? 349 ASP A OD1 1 ATOM 2693 O OD2 . ASP A 1 349 ? -19.435 59.663 12.515 1.00 127.40 ? 349 ASP A OD2 1 ATOM 2694 N N . LEU A 1 350 ? -15.795 56.629 11.173 1.00 90.40 ? 350 LEU A N 1 ATOM 2695 C CA . LEU A 1 350 ? -15.521 55.938 9.918 1.00 80.16 ? 350 LEU A CA 1 ATOM 2696 C C . LEU A 1 350 ? -16.684 56.041 8.940 1.00 89.46 ? 350 LEU A C 1 ATOM 2697 O O . LEU A 1 350 ? -16.487 56.316 7.757 1.00 88.10 ? 350 LEU A O 1 ATOM 2698 C CB . LEU A 1 350 ? -15.188 54.469 10.184 1.00 78.57 ? 350 LEU A CB 1 ATOM 2699 C CG . LEU A 1 350 ? -14.666 53.677 8.984 1.00 73.37 ? 350 LEU A CG 1 ATOM 2700 C CD1 . LEU A 1 350 ? -13.335 54.238 8.520 1.00 69.75 ? 350 LEU A CD1 1 ATOM 2701 C CD2 . LEU A 1 350 ? -14.542 52.198 9.320 1.00 70.17 ? 350 LEU A CD2 1 ATOM 2702 N N . ASP A 1 351 ? -17.895 55.826 9.441 1.00 99.51 ? 351 ASP A N 1 ATOM 2703 C CA . ASP A 1 351 ? -19.079 55.818 8.591 1.00 104.83 ? 351 ASP A CA 1 ATOM 2704 C C . ASP A 1 351 ? -19.771 57.180 8.550 1.00 95.60 ? 351 ASP A C 1 ATOM 2705 O O . ASP A 1 351 ? -20.798 57.340 7.887 1.00 102.53 ? 351 ASP A O 1 ATOM 2706 C CB . ASP A 1 351 ? -20.057 54.740 9.064 1.00 91.02 ? 351 ASP A CB 1 ATOM 2707 C CG . ASP A 1 351 ? -20.375 54.848 10.543 1.00 104.14 ? 351 ASP A CG 1 ATOM 2708 O OD1 . ASP A 1 351 ? -19.591 55.486 11.282 1.00 115.27 ? 351 ASP A OD1 1 ATOM 2709 O OD2 . ASP A 1 351 ? -21.408 54.286 10.968 1.00 100.24 ? 351 ASP A OD2 1 ATOM 2710 N N . GLN A 1 352 ? -19.196 58.152 9.255 1.00 82.39 ? 352 GLN A N 1 ATOM 2711 C CA . GLN A 1 352 ? -19.755 59.500 9.341 1.00 91.41 ? 352 GLN A CA 1 ATOM 2712 C C . GLN A 1 352 ? -21.195 59.480 9.839 1.00 105.43 ? 352 GLN A C 1 ATOM 2713 O O . GLN A 1 352 ? -22.035 60.245 9.367 1.00 126.65 ? 352 GLN A O 1 ATOM 2714 C CB . GLN A 1 352 ? -19.677 60.206 7.986 1.00 83.36 ? 352 GLN A CB 1 ATOM 2715 C CG . GLN A 1 352 ? -18.269 60.572 7.563 1.00 91.10 ? 352 GLN A CG 1 ATOM 2716 C CD . GLN A 1 352 ? -17.711 61.755 8.328 1.00 113.06 ? 352 GLN A CD 1 ATOM 2717 O OE1 . GLN A 1 352 ? -18.456 62.612 8.806 1.00 137.62 ? 352 GLN A OE1 1 ATOM 2718 N NE2 . GLN A 1 352 ? -16.391 61.808 8.446 1.00 85.56 ? 352 GLN A NE2 1 ATOM 2719 N N . ASP A 1 353 ? -21.471 58.599 10.795 1.00 90.47 ? 353 ASP A N 1 ATOM 2720 C CA . ASP A 1 353 ? -22.813 58.463 11.349 1.00 103.04 ? 353 ASP A CA 1 ATOM 2721 C C . ASP A 1 353 ? -23.009 59.397 12.541 1.00 100.92 ? 353 ASP A C 1 ATOM 2722 O O . ASP A 1 353 ? -24.110 59.508 13.083 1.00 106.29 ? 353 ASP A O 1 ATOM 2723 C CB . ASP A 1 353 ? -23.076 57.013 11.763 1.00 94.93 ? 353 ASP A CB 1 ATOM 2724 C CG . ASP A 1 353 ? -22.270 56.598 12.977 1.00 112.55 ? 353 ASP A CG 1 ATOM 2725 O OD1 . ASP A 1 353 ? -21.035 56.451 12.856 1.00 118.27 ? 353 ASP A OD1 1 ATOM 2726 O OD2 . ASP A 1 353 ? -22.872 56.416 14.055 1.00 123.66 ? 353 ASP A OD2 1 ATOM 2727 N N . GLY A 1 354 ? -21.936 60.070 12.942 1.00 88.11 ? 354 GLY A N 1 ATOM 2728 C CA . GLY A 1 354 ? -21.995 61.004 14.051 1.00 89.46 ? 354 GLY A CA 1 ATOM 2729 C C . GLY A 1 354 ? -21.321 60.484 15.305 1.00 94.68 ? 354 GLY A C 1 ATOM 2730 O O . GLY A 1 354 ? -21.126 61.229 16.266 1.00 94.02 ? 354 GLY A O 1 ATOM 2731 N N . PHE A 1 355 ? -20.968 59.203 15.299 1.00 113.28 ? 355 PHE A N 1 ATOM 2732 C CA . PHE A 1 355 ? -20.277 58.593 16.430 1.00 112.32 ? 355 PHE A CA 1 ATOM 2733 C C . PHE A 1 355 ? -18.929 58.023 16.004 1.00 109.18 ? 355 PHE A C 1 ATOM 2734 O O . PHE A 1 355 ? -18.836 57.328 14.990 1.00 120.05 ? 355 PHE A O 1 ATOM 2735 C CB . PHE A 1 355 ? -21.136 57.493 17.058 1.00 105.26 ? 355 PHE A CB 1 ATOM 2736 C CG . PHE A 1 355 ? -22.430 57.989 17.633 1.00 95.79 ? 355 PHE A CG 1 ATOM 2737 C CD1 . PHE A 1 355 ? -22.473 58.543 18.903 1.00 96.73 ? 355 PHE A CD1 1 ATOM 2738 C CD2 . PHE A 1 355 ? -23.605 57.899 16.906 1.00 95.50 ? 355 PHE A CD2 1 ATOM 2739 C CE1 . PHE A 1 355 ? -23.662 59.000 19.435 1.00 104.94 ? 355 PHE A CE1 1 ATOM 2740 C CE2 . PHE A 1 355 ? -24.798 58.353 17.433 1.00 111.69 ? 355 PHE A CE2 1 ATOM 2741 C CZ . PHE A 1 355 ? -24.827 58.905 18.699 1.00 122.30 ? 355 PHE A CZ 1 ATOM 2742 N N . ASN A 1 356 ? -17.892 58.316 16.785 1.00 94.13 ? 356 ASN A N 1 ATOM 2743 C CA . ASN A 1 356 ? -16.545 57.834 16.488 1.00 88.30 ? 356 ASN A CA 1 ATOM 2744 C C . ASN A 1 356 ? -16.465 56.315 16.529 1.00 85.95 ? 356 ASN A C 1 ATOM 2745 O O . ASN A 1 356 ? -17.236 55.662 17.231 1.00 106.19 ? 356 ASN A O 1 ATOM 2746 C CB . ASN A 1 356 ? -15.527 58.429 17.466 1.00 87.25 ? 356 ASN A CB 1 ATOM 2747 C CG . ASN A 1 356 ? -15.283 59.908 17.233 1.00 83.58 ? 356 ASN A CG 1 ATOM 2748 O OD1 . ASN A 1 356 ? -15.354 60.393 16.104 1.00 90.00 ? 356 ASN A OD1 1 ATOM 2749 N ND2 . ASN A 1 356 ? -14.991 60.634 18.305 1.00 95.30 ? 356 ASN A ND2 1 ATOM 2750 N N . ASP A 1 357 ? -15.531 55.754 15.771 1.00 85.88 ? 357 ASP A N 1 ATOM 2751 C CA . ASP A 1 357 ? -15.381 54.307 15.711 1.00 101.20 ? 357 ASP A CA 1 ATOM 2752 C C . ASP A 1 357 ? -13.961 53.885 16.091 1.00 89.69 ? 357 ASP A C 1 ATOM 2753 O O . ASP A 1 357 ? -13.106 54.733 16.352 1.00 96.27 ? 357 ASP A O 1 ATOM 2754 C CB . ASP A 1 357 ? -15.750 53.805 14.315 1.00 88.49 ? 357 ASP A CB 1 ATOM 2755 C CG . ASP A 1 357 ? -17.050 54.408 13.810 1.00 102.32 ? 357 ASP A CG 1 ATOM 2756 O OD1 . ASP A 1 357 ? -18.122 54.023 14.317 1.00 100.15 ? 357 ASP A OD1 1 ATOM 2757 O OD2 . ASP A 1 357 ? -17.004 55.276 12.913 1.00 114.89 ? 357 ASP A OD2 1 ATOM 2758 N N . ILE A 1 358 ? -13.709 52.580 16.119 1.00 76.72 ? 358 ILE A N 1 ATOM 2759 C CA . ILE A 1 358 ? -12.421 52.074 16.582 1.00 82.19 ? 358 ILE A CA 1 ATOM 2760 C C . ILE A 1 358 ? -12.075 50.720 15.962 1.00 74.56 ? 358 ILE A C 1 ATOM 2761 O O . ILE A 1 358 ? -12.957 49.985 15.518 1.00 88.91 ? 358 ILE A O 1 ATOM 2762 C CB . ILE A 1 358 ? -12.404 51.956 18.123 1.00 78.28 ? 358 ILE A CB 1 ATOM 2763 C CG1 . ILE A 1 358 ? -10.992 52.153 18.670 1.00 79.52 ? 358 ILE A CG1 1 ATOM 2764 C CG2 . ILE A 1 358 ? -12.983 50.625 18.575 1.00 64.39 ? 358 ILE A CG2 1 ATOM 2765 C CD1 . ILE A 1 358 ? -10.946 52.216 20.173 1.00 76.97 ? 358 ILE A CD1 1 ATOM 2766 N N . ALA A 1 359 ? -10.786 50.398 15.932 1.00 84.14 ? 359 ALA A N 1 ATOM 2767 C CA . ALA A 1 359 ? -10.323 49.148 15.335 1.00 88.13 ? 359 ALA A CA 1 ATOM 2768 C C . ALA A 1 359 ? -9.410 48.369 16.276 1.00 79.80 ? 359 ALA A C 1 ATOM 2769 O O . ALA A 1 359 ? -8.401 48.887 16.751 1.00 81.32 ? 359 ALA A O 1 ATOM 2770 C CB . ALA A 1 359 ? -9.608 49.425 14.024 1.00 79.94 ? 359 ALA A CB 1 ATOM 2771 N N . ILE A 1 360 ? -9.773 47.117 16.534 1.00 88.72 ? 360 ILE A N 1 ATOM 2772 C CA . ILE A 1 360 ? -8.989 46.240 17.396 1.00 68.04 ? 360 ILE A CA 1 ATOM 2773 C C . ILE A 1 360 ? -8.366 45.132 16.555 1.00 65.08 ? 360 ILE A C 1 ATOM 2774 O O . ILE A 1 360 ? -9.025 44.566 15.684 1.00 92.70 ? 360 ILE A O 1 ATOM 2775 C CB . ILE A 1 360 ? -9.854 45.635 18.515 1.00 61.03 ? 360 ILE A CB 1 ATOM 2776 C CG1 . ILE A 1 360 ? -10.623 46.740 19.245 1.00 61.61 ? 360 ILE A CG1 1 ATOM 2777 C CG2 . ILE A 1 360 ? -8.998 44.854 19.490 1.00 66.23 ? 360 ILE A CG2 1 ATOM 2778 C CD1 . ILE A 1 360 ? -11.517 46.236 20.352 1.00 65.34 ? 360 ILE A CD1 1 ATOM 2779 N N . ALA A 1 361 ? -7.099 44.823 16.812 1.00 67.79 ? 361 ALA A N 1 ATOM 2780 C CA . ALA A 1 361 ? -6.351 43.930 15.931 1.00 89.90 ? 361 ALA A CA 1 ATOM 2781 C C . ALA A 1 361 ? -5.858 42.652 16.605 1.00 96.05 ? 361 ALA A C 1 ATOM 2782 O O . ALA A 1 361 ? -5.336 42.685 17.719 1.00 103.53 ? 361 ALA A O 1 ATOM 2783 C CB . ALA A 1 361 ? -5.179 44.676 15.336 1.00 59.46 ? 361 ALA A CB 1 ATOM 2784 N N . ALA A 1 362 ? -6.008 41.530 15.904 1.00 75.72 ? 362 ALA A N 1 ATOM 2785 C CA . ALA A 1 362 ? -5.487 40.245 16.362 1.00 79.70 ? 362 ALA A CA 1 ATOM 2786 C C . ALA A 1 362 ? -4.495 39.692 15.339 1.00 72.98 ? 362 ALA A C 1 ATOM 2787 O O . ALA A 1 362 ? -4.865 38.907 14.465 1.00 65.78 ? 362 ALA A O 1 ATOM 2788 C CB . ALA A 1 362 ? -6.616 39.265 16.598 1.00 64.95 ? 362 ALA A CB 1 ATOM 2789 N N . PRO A 1 363 ? -3.223 40.099 15.464 1.00 63.36 ? 363 PRO A N 1 ATOM 2790 C CA . PRO A 1 363 ? -2.148 39.937 14.477 1.00 70.97 ? 363 PRO A CA 1 ATOM 2791 C C . PRO A 1 363 ? -1.844 38.503 14.071 1.00 71.98 ? 363 PRO A C 1 ATOM 2792 O O . PRO A 1 363 ? -1.373 38.273 12.958 1.00 82.20 ? 363 PRO A O 1 ATOM 2793 C CB . PRO A 1 363 ? -0.931 40.538 15.188 1.00 91.30 ? 363 PRO A CB 1 ATOM 2794 C CG . PRO A 1 363 ? -1.499 41.435 16.225 1.00 87.82 ? 363 PRO A CG 1 ATOM 2795 C CD . PRO A 1 363 ? -2.742 40.762 16.686 1.00 61.93 ? 363 PRO A CD 1 ATOM 2796 N N . TYR A 1 364 ? -2.035 37.563 14.985 1.00 67.53 ? 364 TYR A N 1 ATOM 2797 C CA . TYR A 1 364 ? -1.697 36.177 14.712 1.00 70.39 ? 364 TYR A CA 1 ATOM 2798 C C . TYR A 1 364 ? -2.905 35.315 14.371 1.00 83.28 ? 364 TYR A C 1 ATOM 2799 O O . TYR A 1 364 ? -2.775 34.113 14.149 1.00 120.26 ? 364 TYR A O 1 ATOM 2800 C CB . TYR A 1 364 ? -0.924 35.620 15.897 1.00 70.87 ? 364 TYR A CB 1 ATOM 2801 C CG . TYR A 1 364 ? 0.238 36.524 16.243 1.00 68.75 ? 364 TYR A CG 1 ATOM 2802 C CD1 . TYR A 1 364 ? 1.389 36.530 15.468 1.00 69.23 ? 364 TYR A CD1 1 ATOM 2803 C CD2 . TYR A 1 364 ? 0.166 37.401 17.316 1.00 75.40 ? 364 TYR A CD2 1 ATOM 2804 C CE1 . TYR A 1 364 ? 2.444 37.368 15.764 1.00 97.69 ? 364 TYR A CE1 1 ATOM 2805 C CE2 . TYR A 1 364 ? 1.219 38.243 17.621 1.00 88.65 ? 364 TYR A CE2 1 ATOM 2806 C CZ . TYR A 1 364 ? 2.355 38.222 16.842 1.00 91.13 ? 364 TYR A CZ 1 ATOM 2807 O OH . TYR A 1 364 ? 3.406 39.057 17.142 1.00 83.58 ? 364 TYR A OH 1 ATOM 2808 N N . GLY A 1 365 ? -4.081 35.932 14.328 1.00 75.23 ? 365 GLY A N 1 ATOM 2809 C CA . GLY A 1 365 ? -5.305 35.202 14.055 1.00 72.91 ? 365 GLY A CA 1 ATOM 2810 C C . GLY A 1 365 ? -5.613 35.097 12.575 1.00 83.71 ? 365 GLY A C 1 ATOM 2811 O O . GLY A 1 365 ? -4.815 35.510 11.738 1.00 81.39 ? 365 GLY A O 1 ATOM 2812 N N . GLY A 1 366 ? -6.771 34.528 12.255 1.00 105.28 ? 366 GLY A N 1 ATOM 2813 C CA . GLY A 1 366 ? -7.224 34.429 10.879 1.00 108.29 ? 366 GLY A CA 1 ATOM 2814 C C . GLY A 1 366 ? -6.753 33.201 10.129 1.00 130.21 ? 366 GLY A C 1 ATOM 2815 O O . GLY A 1 366 ? -6.105 32.318 10.695 1.00 125.14 ? 366 GLY A O 1 ATOM 2816 N N . GLU A 1 367 ? -7.091 33.149 8.844 1.00 142.36 ? 367 GLU A N 1 ATOM 2817 C CA . GLU A 1 367 ? -6.687 32.049 7.979 1.00 140.23 ? 367 GLU A CA 1 ATOM 2818 C C . GLU A 1 367 ? -5.174 32.031 7.798 1.00 130.37 ? 367 GLU A C 1 ATOM 2819 O O . GLU A 1 367 ? -4.563 33.054 7.481 1.00 105.75 ? 367 GLU A O 1 ATOM 2820 C CB . GLU A 1 367 ? -7.385 32.148 6.620 1.00 143.76 ? 367 GLU A CB 1 ATOM 2821 C CG . GLU A 1 367 ? -7.239 33.500 5.939 1.00 147.99 ? 367 GLU A CG 1 ATOM 2822 C CD . GLU A 1 367 ? -7.917 33.546 4.586 1.00 147.59 ? 367 GLU A CD 1 ATOM 2823 O OE1 . GLU A 1 367 ? -7.747 34.556 3.870 1.00 143.17 ? 367 GLU A OE1 1 ATOM 2824 O OE2 . GLU A 1 367 ? -8.619 32.573 4.237 1.00 143.01 ? 367 GLU A OE2 1 ATOM 2825 N N . ASP A 1 368 ? -4.581 30.863 8.030 1.00 132.53 ? 368 ASP A N 1 ATOM 2826 C CA . ASP A 1 368 ? -3.136 30.668 7.932 1.00 116.27 ? 368 ASP A CA 1 ATOM 2827 C C . ASP A 1 368 ? -2.391 31.600 8.884 1.00 97.27 ? 368 ASP A C 1 ATOM 2828 O O . ASP A 1 368 ? -1.211 31.888 8.686 1.00 114.21 ? 368 ASP A O 1 ATOM 2829 C CB . ASP A 1 368 ? -2.661 30.881 6.493 1.00 120.22 ? 368 ASP A CB 1 ATOM 2830 C CG . ASP A 1 368 ? -3.549 30.185 5.476 1.00 154.59 ? 368 ASP A CG 1 ATOM 2831 O OD1 . ASP A 1 368 ? -4.077 29.097 5.790 1.00 158.16 ? 368 ASP A OD1 1 ATOM 2832 O OD2 . ASP A 1 368 ? -3.724 30.729 4.366 1.00 156.65 ? 368 ASP A OD2 1 ATOM 2833 N N . LYS A 1 369 ? -3.095 32.046 9.923 1.00 84.72 ? 369 LYS A N 1 ATOM 2834 C CA . LYS A 1 369 ? -2.547 32.920 10.958 1.00 81.28 ? 369 LYS A CA 1 ATOM 2835 C C . LYS A 1 369 ? -1.830 34.141 10.378 1.00 79.12 ? 369 LYS A C 1 ATOM 2836 O O . LYS A 1 369 ? -0.745 34.506 10.826 1.00 77.99 ? 369 LYS A O 1 ATOM 2837 C CB . LYS A 1 369 ? -1.604 32.125 11.864 1.00 98.74 ? 369 LYS A CB 1 ATOM 2838 C CG . LYS A 1 369 ? -2.166 30.767 12.273 1.00 103.07 ? 369 LYS A CG 1 ATOM 2839 C CD . LYS A 1 369 ? -1.494 30.216 13.521 1.00 116.08 ? 369 LYS A CD 1 ATOM 2840 C CE . LYS A 1 369 ? -1.924 30.985 14.761 1.00 125.28 ? 369 LYS A CE 1 ATOM 2841 N NZ . LYS A 1 369 ? -1.368 30.390 16.008 1.00 130.59 ? 369 LYS A NZ 1 ATOM 2842 N N . LYS A 1 370 ? -2.449 34.761 9.377 1.00 101.04 ? 370 LYS A N 1 ATOM 2843 C CA . LYS A 1 370 ? -1.883 35.931 8.711 1.00 82.94 ? 370 LYS A CA 1 ATOM 2844 C C . LYS A 1 370 ? -2.270 37.241 9.398 1.00 83.68 ? 370 LYS A C 1 ATOM 2845 O O . LYS A 1 370 ? -1.699 38.290 9.107 1.00 86.91 ? 370 LYS A O 1 ATOM 2846 C CB . LYS A 1 370 ? -2.327 35.975 7.247 1.00 96.80 ? 370 LYS A CB 1 ATOM 2847 C CG . LYS A 1 370 ? -1.885 34.786 6.408 1.00 95.58 ? 370 LYS A CG 1 ATOM 2848 C CD . LYS A 1 370 ? -2.501 34.848 5.016 1.00 96.93 ? 370 LYS A CD 1 ATOM 2849 C CE . LYS A 1 370 ? -2.101 33.648 4.172 1.00 120.72 ? 370 LYS A CE 1 ATOM 2850 N NZ . LYS A 1 370 ? -2.786 33.646 2.849 1.00 123.45 ? 370 LYS A NZ 1 ATOM 2851 N N . GLY A 1 371 ? -3.234 37.173 10.310 1.00 84.35 ? 371 GLY A N 1 ATOM 2852 C CA . GLY A 1 371 ? -3.697 38.343 11.039 1.00 71.50 ? 371 GLY A CA 1 ATOM 2853 C C . GLY A 1 371 ? -5.020 38.930 10.586 1.00 72.16 ? 371 GLY A C 1 ATOM 2854 O O . GLY A 1 371 ? -5.355 38.905 9.402 1.00 79.39 ? 371 GLY A O 1 ATOM 2855 N N . ILE A 1 372 ? -5.764 39.476 11.547 1.00 67.03 ? 372 ILE A N 1 ATOM 2856 C CA . ILE A 1 372 ? -7.098 40.027 11.312 1.00 66.48 ? 372 ILE A CA 1 ATOM 2857 C C . ILE A 1 372 ? -7.269 41.358 12.039 1.00 73.54 ? 372 ILE A C 1 ATOM 2858 O O . ILE A 1 372 ? -6.817 41.514 13.174 1.00 68.05 ? 372 ILE A O 1 ATOM 2859 C CB . ILE A 1 372 ? -8.213 39.055 11.783 1.00 87.48 ? 372 ILE A CB 1 ATOM 2860 C CG1 . ILE A 1 372 ? -8.128 37.724 11.040 1.00 93.84 ? 372 ILE A CG1 1 ATOM 2861 C CG2 . ILE A 1 372 ? -9.597 39.659 11.579 1.00 78.52 ? 372 ILE A CG2 1 ATOM 2862 C CD1 . ILE A 1 372 ? -8.414 37.825 9.561 1.00 110.57 ? 372 ILE A CD1 1 ATOM 2863 N N . VAL A 1 373 ? -7.915 42.316 11.383 1.00 66.85 ? 373 VAL A N 1 ATOM 2864 C CA . VAL A 1 373 ? -8.288 43.563 12.038 1.00 69.13 ? 373 VAL A CA 1 ATOM 2865 C C . VAL A 1 373 ? -9.806 43.683 12.113 1.00 77.94 ? 373 VAL A C 1 ATOM 2866 O O . VAL A 1 373 ? -10.494 43.592 11.097 1.00 85.27 ? 373 VAL A O 1 ATOM 2867 C CB . VAL A 1 373 ? -7.718 44.788 11.306 1.00 72.26 ? 373 VAL A CB 1 ATOM 2868 C CG1 . VAL A 1 373 ? -8.186 46.070 11.980 1.00 68.65 ? 373 VAL A CG1 1 ATOM 2869 C CG2 . VAL A 1 373 ? -6.199 44.723 11.271 1.00 65.85 ? 373 VAL A CG2 1 ATOM 2870 N N . TYR A 1 374 ? -10.322 43.881 13.322 1.00 77.60 ? 374 TYR A N 1 ATOM 2871 C CA . TYR A 1 374 ? -11.758 44.019 13.531 1.00 79.01 ? 374 TYR A CA 1 ATOM 2872 C C . TYR A 1 374 ? -12.156 45.484 13.688 1.00 95.19 ? 374 TYR A C 1 ATOM 2873 O O . TYR A 1 374 ? -11.559 46.219 14.475 1.00 92.43 ? 374 TYR A O 1 ATOM 2874 C CB . TYR A 1 374 ? -12.202 43.228 14.762 1.00 72.45 ? 374 TYR A CB 1 ATOM 2875 C CG . TYR A 1 374 ? -11.892 41.747 14.714 1.00 80.39 ? 374 TYR A CG 1 ATOM 2876 C CD1 . TYR A 1 374 ? -10.680 41.256 15.183 1.00 77.23 ? 374 TYR A CD1 1 ATOM 2877 C CD2 . TYR A 1 374 ? -12.819 40.838 14.218 1.00 65.16 ? 374 TYR A CD2 1 ATOM 2878 C CE1 . TYR A 1 374 ? -10.394 39.904 15.149 1.00 89.95 ? 374 TYR A CE1 1 ATOM 2879 C CE2 . TYR A 1 374 ? -12.542 39.483 14.182 1.00 72.05 ? 374 TYR A CE2 1 ATOM 2880 C CZ . TYR A 1 374 ? -11.329 39.021 14.649 1.00 94.07 ? 374 TYR A CZ 1 ATOM 2881 O OH . TYR A 1 374 ? -11.046 37.673 14.616 1.00 92.04 ? 374 TYR A OH 1 ATOM 2882 N N . ILE A 1 375 ? -13.171 45.903 12.939 1.00 96.50 ? 375 ILE A N 1 ATOM 2883 C CA . ILE A 1 375 ? -13.672 47.271 13.021 1.00 66.29 ? 375 ILE A CA 1 ATOM 2884 C C . ILE A 1 375 ? -14.944 47.319 13.863 1.00 74.63 ? 375 ILE A C 1 ATOM 2885 O O . ILE A 1 375 ? -15.876 46.542 13.644 1.00 72.95 ? 375 ILE A O 1 ATOM 2886 C CB . ILE A 1 375 ? -13.950 47.858 11.620 1.00 63.51 ? 375 ILE A CB 1 ATOM 2887 C CG1 . ILE A 1 375 ? -12.670 48.435 11.013 1.00 66.26 ? 375 ILE A CG1 1 ATOM 2888 C CG2 . ILE A 1 375 ? -15.002 48.952 11.691 1.00 75.41 ? 375 ILE A CG2 1 ATOM 2889 C CD1 . ILE A 1 375 ? -11.685 47.400 10.526 1.00 87.32 ? 375 ILE A CD1 1 ATOM 2890 N N . PHE A 1 376 ? -14.974 48.229 14.831 1.00 65.63 ? 376 PHE A N 1 ATOM 2891 C CA . PHE A 1 376 ? -16.122 48.362 15.720 1.00 80.75 ? 376 PHE A CA 1 ATOM 2892 C C . PHE A 1 376 ? -16.742 49.752 15.644 1.00 71.92 ? 376 PHE A C 1 ATOM 2893 O O . PHE A 1 376 ? -16.076 50.750 15.913 1.00 72.82 ? 376 PHE A O 1 ATOM 2894 C CB . PHE A 1 376 ? -15.716 48.057 17.162 1.00 66.83 ? 376 PHE A CB 1 ATOM 2895 C CG . PHE A 1 376 ? -15.300 46.635 17.387 1.00 82.63 ? 376 PHE A CG 1 ATOM 2896 C CD1 . PHE A 1 376 ? -13.979 46.253 17.228 1.00 90.88 ? 376 PHE A CD1 1 ATOM 2897 C CD2 . PHE A 1 376 ? -16.229 45.679 17.762 1.00 100.05 ? 376 PHE A CD2 1 ATOM 2898 C CE1 . PHE A 1 376 ? -13.592 44.945 17.438 1.00 85.37 ? 376 PHE A CE1 1 ATOM 2899 C CE2 . PHE A 1 376 ? -15.848 44.370 17.975 1.00 92.78 ? 376 PHE A CE2 1 ATOM 2900 C CZ . PHE A 1 376 ? -14.528 44.002 17.810 1.00 88.01 ? 376 PHE A CZ 1 ATOM 2901 N N . ASN A 1 377 ? -18.020 49.814 15.288 1.00 80.20 ? 377 ASN A N 1 ATOM 2902 C CA . ASN A 1 377 ? -18.722 51.089 15.215 1.00 78.67 ? 377 ASN A CA 1 ATOM 2903 C C . ASN A 1 377 ? -19.203 51.571 16.580 1.00 94.64 ? 377 ASN A C 1 ATOM 2904 O O . ASN A 1 377 ? -19.571 50.772 17.438 1.00 86.42 ? 377 ASN A O 1 ATOM 2905 C CB . ASN A 1 377 ? -19.909 50.993 14.257 1.00 78.16 ? 377 ASN A CB 1 ATOM 2906 C CG . ASN A 1 377 ? -19.481 50.895 12.809 1.00 87.80 ? 377 ASN A CG 1 ATOM 2907 O OD1 . ASN A 1 377 ? -18.377 51.301 12.450 1.00 76.77 ? 377 ASN A OD1 1 ATOM 2908 N ND2 . ASN A 1 377 ? -20.357 50.362 11.967 1.00 109.23 ? 377 ASN A ND2 1 ATOM 2909 N N . GLY A 1 378 ? -19.190 52.885 16.775 1.00 100.52 ? 378 GLY A N 1 ATOM 2910 C CA . GLY A 1 378 ? -19.691 53.475 18.002 1.00 87.59 ? 378 GLY A CA 1 ATOM 2911 C C . GLY A 1 378 ? -21.159 53.827 17.870 1.00 98.35 ? 378 GLY A C 1 ATOM 2912 O O . GLY A 1 378 ? -21.664 54.002 16.760 1.00 114.32 ? 378 GLY A O 1 ATOM 2913 N N . ARG A 1 379 ? -21.849 53.923 19.002 1.00 92.62 ? 379 ARG A N 1 ATOM 2914 C CA . ARG A 1 379 ? -23.265 54.271 19.009 1.00 94.01 ? 379 ARG A CA 1 ATOM 2915 C C . ARG A 1 379 ? -23.600 55.221 20.153 1.00 101.97 ? 379 ARG A C 1 ATOM 2916 O O . ARG A 1 379 ? -22.720 55.642 20.904 1.00 104.44 ? 379 ARG A O 1 ATOM 2917 C CB . ARG A 1 379 ? -24.131 53.014 19.115 1.00 111.51 ? 379 ARG A CB 1 ATOM 2918 C CG . ARG A 1 379 ? -24.091 52.105 17.897 1.00 104.98 ? 379 ARG A CG 1 ATOM 2919 C CD . ARG A 1 379 ? -24.866 50.827 18.164 1.00 117.45 ? 379 ARG A CD 1 ATOM 2920 N NE . ARG A 1 379 ? -24.421 50.180 19.396 1.00 127.40 ? 379 ARG A NE 1 ATOM 2921 C CZ . ARG A 1 379 ? -24.937 49.055 19.879 1.00 117.82 ? 379 ARG A CZ 1 ATOM 2922 N NH1 . ARG A 1 379 ? -25.922 48.446 19.234 1.00 108.89 ? 379 ARG A NH1 1 ATOM 2923 N NH2 . ARG A 1 379 ? -24.468 48.539 21.008 1.00 111.09 ? 379 ARG A NH2 1 ATOM 2924 N N . SER A 1 380 ? -24.882 55.548 20.279 1.00 109.75 ? 380 SER A N 1 ATOM 2925 C CA . SER A 1 380 ? -25.366 56.408 21.352 1.00 112.27 ? 380 SER A CA 1 ATOM 2926 C C . SER A 1 380 ? -25.159 55.764 22.720 1.00 111.66 ? 380 SER A C 1 ATOM 2927 O O . SER A 1 380 ? -24.968 56.451 23.723 1.00 104.97 ? 380 SER A O 1 ATOM 2928 C CB . SER A 1 380 ? -26.849 56.728 21.143 1.00 115.76 ? 380 SER A CB 1 ATOM 2929 O OG . SER A 1 380 ? -27.403 57.366 22.279 1.00 124.84 ? 380 SER A OG 1 ATOM 2930 N N . THR A 1 381 ? -25.189 54.436 22.741 1.00 125.40 ? 381 THR A N 1 ATOM 2931 C CA . THR A 1 381 ? -25.123 53.670 23.980 1.00 118.03 ? 381 THR A CA 1 ATOM 2932 C C . THR A 1 381 ? -23.696 53.281 24.350 1.00 116.98 ? 381 THR A C 1 ATOM 2933 O O . THR A 1 381 ? -23.473 52.570 25.330 1.00 105.64 ? 381 THR A O 1 ATOM 2934 C CB . THR A 1 381 ? -25.964 52.390 23.876 1.00 108.41 ? 381 THR A CB 1 ATOM 2935 O OG1 . THR A 1 381 ? -25.386 51.520 22.894 1.00 106.33 ? 381 THR A OG1 1 ATOM 2936 C CG2 . THR A 1 381 ? -27.390 52.725 23.470 1.00 112.62 ? 381 THR A CG2 1 ATOM 2937 N N . GLY A 1 382 ? -22.731 53.759 23.571 1.00 116.70 ? 382 GLY A N 1 ATOM 2938 C CA . GLY A 1 382 ? -21.363 53.289 23.692 1.00 99.41 ? 382 GLY A CA 1 ATOM 2939 C C . GLY A 1 382 ? -21.019 52.364 22.541 1.00 98.60 ? 382 GLY A C 1 ATOM 2940 O O . GLY A 1 382 ? -21.753 52.293 21.555 1.00 132.90 ? 382 GLY A O 1 ATOM 2941 N N . LEU A 1 383 ? -19.896 51.662 22.658 1.00 87.22 ? 383 LEU A N 1 ATOM 2942 C CA . LEU A 1 383 ? -19.400 50.825 21.569 1.00 85.69 ? 383 LEU A CA 1 ATOM 2943 C C . LEU A 1 383 ? -20.323 49.657 21.234 1.00 96.39 ? 383 LEU A C 1 ATOM 2944 O O . LEU A 1 383 ? -20.798 48.952 22.124 1.00 104.98 ? 383 LEU A O 1 ATOM 2945 C CB . LEU A 1 383 ? -18.010 50.287 21.907 1.00 80.92 ? 383 LEU A CB 1 ATOM 2946 C CG . LEU A 1 383 ? -17.368 49.445 20.804 1.00 76.75 ? 383 LEU A CG 1 ATOM 2947 C CD1 . LEU A 1 383 ? -17.207 50.273 19.541 1.00 75.87 ? 383 LEU A CD1 1 ATOM 2948 C CD2 . LEU A 1 383 ? -16.031 48.886 21.255 1.00 79.55 ? 383 LEU A CD2 1 ATOM 2949 N N . ASN A 1 384 ? -20.569 49.457 19.943 1.00 96.56 ? 384 ASN A N 1 ATOM 2950 C CA . ASN A 1 384 ? -21.293 48.281 19.482 1.00 84.11 ? 384 ASN A CA 1 ATOM 2951 C C . ASN A 1 384 ? -20.416 47.056 19.674 1.00 89.53 ? 384 ASN A C 1 ATOM 2952 O O . ASN A 1 384 ? -19.306 46.987 19.147 1.00 84.38 ? 384 ASN A O 1 ATOM 2953 C CB . ASN A 1 384 ? -21.696 48.428 18.013 1.00 81.95 ? 384 ASN A CB 1 ATOM 2954 C CG . ASN A 1 384 ? -22.689 47.374 17.568 1.00 89.76 ? 384 ASN A CG 1 ATOM 2955 O OD1 . ASN A 1 384 ? -22.808 46.314 18.181 1.00 96.67 ? 384 ASN A OD1 1 ATOM 2956 N ND2 . ASN A 1 384 ? -23.409 47.661 16.489 1.00 106.90 ? 384 ASN A ND2 1 ATOM 2957 N N . ALA A 1 385 ? -20.930 46.083 20.416 1.00 97.62 ? 385 ALA A N 1 ATOM 2958 C CA . ALA A 1 385 ? -20.150 44.919 20.821 1.00 84.36 ? 385 ALA A CA 1 ATOM 2959 C C . ALA A 1 385 ? -19.768 44.017 19.650 1.00 83.55 ? 385 ALA A C 1 ATOM 2960 O O . ALA A 1 385 ? -18.976 43.089 19.811 1.00 101.71 ? 385 ALA A O 1 ATOM 2961 C CB . ALA A 1 385 ? -20.915 44.123 21.866 1.00 103.69 ? 385 ALA A CB 1 ATOM 2962 N N . VAL A 1 386 ? -20.310 44.300 18.470 1.00 73.11 ? 386 VAL A N 1 ATOM 2963 C CA . VAL A 1 386 ? -20.122 43.418 17.329 1.00 69.37 ? 386 VAL A CA 1 ATOM 2964 C C . VAL A 1 386 ? -19.355 44.127 16.222 1.00 89.63 ? 386 VAL A C 1 ATOM 2965 O O . VAL A 1 386 ? -19.587 45.307 15.960 1.00 129.99 ? 386 VAL A O 1 ATOM 2966 C CB . VAL A 1 386 ? -21.485 42.938 16.783 1.00 76.38 ? 386 VAL A CB 1 ATOM 2967 C CG1 . VAL A 1 386 ? -21.309 41.988 15.610 1.00 83.15 ? 386 VAL A CG1 1 ATOM 2968 C CG2 . VAL A 1 386 ? -22.295 42.281 17.888 1.00 80.94 ? 386 VAL A CG2 1 ATOM 2969 N N . PRO A 1 387 ? -18.436 43.403 15.564 1.00 73.03 ? 387 PRO A N 1 ATOM 2970 C CA . PRO A 1 387 ? -17.670 43.954 14.442 1.00 93.26 ? 387 PRO A CA 1 ATOM 2971 C C . PRO A 1 387 ? -18.545 44.253 13.235 1.00 84.70 ? 387 PRO A C 1 ATOM 2972 O O . PRO A 1 387 ? -19.411 43.450 12.887 1.00 89.57 ? 387 PRO A O 1 ATOM 2973 C CB . PRO A 1 387 ? -16.666 42.844 14.122 1.00 84.06 ? 387 PRO A CB 1 ATOM 2974 C CG . PRO A 1 387 ? -16.501 42.112 15.403 1.00 79.00 ? 387 PRO A CG 1 ATOM 2975 C CD . PRO A 1 387 ? -17.856 42.140 16.052 1.00 81.85 ? 387 PRO A CD 1 ATOM 2976 N N . SER A 1 388 ? -18.324 45.405 12.612 1.00 75.67 ? 388 SER A N 1 ATOM 2977 C CA . SER A 1 388 ? -19.065 45.774 11.416 1.00 78.56 ? 388 SER A CA 1 ATOM 2978 C C . SER A 1 388 ? -18.279 45.409 10.163 1.00 85.08 ? 388 SER A C 1 ATOM 2979 O O . SER A 1 388 ? -18.771 45.575 9.046 1.00 100.86 ? 388 SER A O 1 ATOM 2980 C CB . SER A 1 388 ? -19.392 47.266 11.422 1.00 85.29 ? 388 SER A CB 1 ATOM 2981 O OG . SER A 1 388 ? -18.212 48.047 11.437 1.00 99.95 ? 388 SER A OG 1 ATOM 2982 N N . GLN A 1 389 ? -17.076 44.877 10.360 1.00 85.63 ? 389 GLN A N 1 ATOM 2983 C CA . GLN A 1 389 ? -16.191 44.518 9.256 1.00 95.09 ? 389 GLN A CA 1 ATOM 2984 C C . GLN A 1 389 ? -14.921 43.849 9.777 1.00 90.07 ? 389 GLN A C 1 ATOM 2985 O O . GLN A 1 389 ? -14.547 44.023 10.938 1.00 68.36 ? 389 GLN A O 1 ATOM 2986 C CB . GLN A 1 389 ? -15.820 45.765 8.438 1.00 80.53 ? 389 GLN A CB 1 ATOM 2987 C CG . GLN A 1 389 ? -15.177 45.483 7.087 1.00 81.71 ? 389 GLN A CG 1 ATOM 2988 C CD . GLN A 1 389 ? -14.784 46.749 6.349 1.00 81.45 ? 389 GLN A CD 1 ATOM 2989 O OE1 . GLN A 1 389 ? -14.992 47.858 6.839 1.00 96.92 ? 389 GLN A OE1 1 ATOM 2990 N NE2 . GLN A 1 389 ? -14.207 46.588 5.164 1.00 82.78 ? 389 GLN A NE2 1 ATOM 2991 N N . ILE A 1 390 ? -14.253 43.102 8.903 1.00 77.59 ? 390 ILE A N 1 ATOM 2992 C CA . ILE A 1 390 ? -12.979 42.477 9.235 1.00 69.41 ? 390 ILE A CA 1 ATOM 2993 C C . ILE A 1 390 ? -11.987 42.656 8.096 1.00 81.52 ? 390 ILE A C 1 ATOM 2994 O O . ILE A 1 390 ? -12.361 42.653 6.922 1.00 96.01 ? 390 ILE A O 1 ATOM 2995 C CB . ILE A 1 390 ? -13.127 40.971 9.537 1.00 71.49 ? 390 ILE A CB 1 ATOM 2996 C CG1 . ILE A 1 390 ? -13.753 40.240 8.348 1.00 108.21 ? 390 ILE A CG1 1 ATOM 2997 C CG2 . ILE A 1 390 ? -13.949 40.753 10.796 1.00 75.15 ? 390 ILE A CG2 1 ATOM 2998 C CD1 . ILE A 1 390 ? -13.802 38.736 8.513 1.00 127.61 ? 390 ILE A CD1 1 ATOM 2999 N N . LEU A 1 391 ? -10.718 42.820 8.451 1.00 75.92 ? 391 LEU A N 1 ATOM 3000 C CA . LEU A 1 391 ? -9.660 42.946 7.462 1.00 79.73 ? 391 LEU A CA 1 ATOM 3001 C C . LEU A 1 391 ? -8.698 41.772 7.588 1.00 75.68 ? 391 LEU A C 1 ATOM 3002 O O . LEU A 1 391 ? -8.153 41.521 8.662 1.00 73.62 ? 391 LEU A O 1 ATOM 3003 C CB . LEU A 1 391 ? -8.921 44.274 7.632 1.00 87.97 ? 391 LEU A CB 1 ATOM 3004 C CG . LEU A 1 391 ? -9.793 45.534 7.623 1.00 79.45 ? 391 LEU A CG 1 ATOM 3005 C CD1 . LEU A 1 391 ? -8.931 46.786 7.688 1.00 84.72 ? 391 LEU A CD1 1 ATOM 3006 C CD2 . LEU A 1 391 ? -10.696 45.567 6.399 1.00 87.65 ? 391 LEU A CD2 1 ATOM 3007 N N . GLU A 1 392 ? -8.494 41.051 6.493 1.00 77.90 ? 392 GLU A N 1 ATOM 3008 C CA . GLU A 1 392 ? -7.646 39.866 6.522 1.00 83.24 ? 392 GLU A CA 1 ATOM 3009 C C . GLU A 1 392 ? -6.273 40.143 5.915 1.00 82.25 ? 392 GLU A C 1 ATOM 3010 O O . GLU A 1 392 ? -6.151 40.885 4.941 1.00 83.92 ? 392 GLU A O 1 ATOM 3011 C CB . GLU A 1 392 ? -8.328 38.707 5.790 1.00 92.61 ? 392 GLU A CB 1 ATOM 3012 C CG . GLU A 1 392 ? -9.762 38.457 6.239 1.00 105.98 ? 392 GLU A CG 1 ATOM 3013 C CD . GLU A 1 392 ? -10.370 37.209 5.623 1.00 116.30 ? 392 GLU A CD 1 ATOM 3014 O OE1 . GLU A 1 392 ? -9.631 36.225 5.409 1.00 121.61 ? 392 GLU A OE1 1 ATOM 3015 O OE2 . GLU A 1 392 ? -11.590 37.214 5.351 1.00 113.69 ? 392 GLU A OE2 1 ATOM 3016 N N . GLY A 1 393 ? -5.242 39.549 6.508 1.00 84.15 ? 393 GLY A N 1 ATOM 3017 C CA . GLY A 1 393 ? -3.887 39.678 6.005 1.00 86.43 ? 393 GLY A CA 1 ATOM 3018 C C . GLY A 1 393 ? -3.704 38.922 4.705 1.00 98.25 ? 393 GLY A C 1 ATOM 3019 O O . GLY A 1 393 ? -4.101 37.763 4.589 1.00 135.27 ? 393 GLY A O 1 ATOM 3020 N N . GLN A 1 394 ? -3.108 39.585 3.722 1.00 102.24 ? 394 GLN A N 1 ATOM 3021 C CA . GLN A 1 394 ? -2.934 39.002 2.398 1.00 111.73 ? 394 GLN A CA 1 ATOM 3022 C C . GLN A 1 394 ? -1.551 38.386 2.192 1.00 114.11 ? 394 GLN A C 1 ATOM 3023 O O . GLN A 1 394 ? -1.270 37.825 1.133 1.00 129.50 ? 394 GLN A O 1 ATOM 3024 C CB . GLN A 1 394 ? -3.191 40.067 1.332 1.00 130.02 ? 394 GLN A CB 1 ATOM 3025 C CG . GLN A 1 394 ? -4.571 40.698 1.418 1.00 139.34 ? 394 GLN A CG 1 ATOM 3026 C CD . GLN A 1 394 ? -4.570 42.158 1.011 1.00 141.26 ? 394 GLN A CD 1 ATOM 3027 O OE1 . GLN A 1 394 ? -3.522 42.805 0.982 1.00 135.83 ? 394 GLN A OE1 1 ATOM 3028 N NE2 . GLN A 1 394 ? -5.748 42.687 0.697 1.00 134.15 ? 394 GLN A NE2 1 ATOM 3029 N N . TRP A 1 395 ? -0.692 38.480 3.203 1.00 108.19 ? 395 TRP A N 1 ATOM 3030 C CA . TRP A 1 395 ? 0.707 38.095 3.039 1.00 110.40 ? 395 TRP A CA 1 ATOM 3031 C C . TRP A 1 395 ? 1.103 36.886 3.884 1.00 106.76 ? 395 TRP A C 1 ATOM 3032 O O . TRP A 1 395 ? 0.673 36.742 5.029 1.00 95.89 ? 395 TRP A O 1 ATOM 3033 C CB . TRP A 1 395 ? 1.604 39.286 3.366 1.00 106.90 ? 395 TRP A CB 1 ATOM 3034 C CG . TRP A 1 395 ? 1.065 40.566 2.816 1.00 109.46 ? 395 TRP A CG 1 ATOM 3035 C CD1 . TRP A 1 395 ? 0.291 41.478 3.472 1.00 108.41 ? 395 TRP A CD1 1 ATOM 3036 C CD2 . TRP A 1 395 ? 1.239 41.069 1.487 1.00 113.40 ? 395 TRP A CD2 1 ATOM 3037 N NE1 . TRP A 1 395 ? -0.021 42.522 2.637 1.00 111.60 ? 395 TRP A NE1 1 ATOM 3038 C CE2 . TRP A 1 395 ? 0.550 42.296 1.413 1.00 118.76 ? 395 TRP A CE2 1 ATOM 3039 C CE3 . TRP A 1 395 ? 1.915 40.605 0.354 1.00 125.78 ? 395 TRP A CE3 1 ATOM 3040 C CZ2 . TRP A 1 395 ? 0.518 43.065 0.252 1.00 144.64 ? 395 TRP A CZ2 1 ATOM 3041 C CZ3 . TRP A 1 395 ? 1.881 41.370 -0.798 1.00 149.22 ? 395 TRP A CZ3 1 ATOM 3042 C CH2 . TRP A 1 395 ? 1.187 42.586 -0.841 1.00 159.12 ? 395 TRP A CH2 1 ATOM 3043 N N . ALA A 1 396 ? 1.947 36.033 3.308 1.00 110.70 ? 396 ALA A N 1 ATOM 3044 C CA . ALA A 1 396 ? 2.282 34.740 3.897 1.00 105.85 ? 396 ALA A CA 1 ATOM 3045 C C . ALA A 1 396 ? 3.268 34.849 5.054 1.00 102.21 ? 396 ALA A C 1 ATOM 3046 O O . ALA A 1 396 ? 3.625 35.941 5.482 1.00 98.83 ? 396 ALA A O 1 ATOM 3047 C CB . ALA A 1 396 ? 2.837 33.813 2.828 1.00 130.10 ? 396 ALA A CB 1 ATOM 3048 N N . ALA A 1 397 ? 3.716 33.698 5.542 1.00 113.83 ? 397 ALA A N 1 ATOM 3049 C CA . ALA A 1 397 ? 4.495 33.621 6.771 1.00 102.28 ? 397 ALA A CA 1 ATOM 3050 C C . ALA A 1 397 ? 5.939 34.072 6.604 1.00 109.15 ? 397 ALA A C 1 ATOM 3051 O O . ALA A 1 397 ? 6.355 35.055 7.214 1.00 146.38 ? 397 ALA A O 1 ATOM 3052 C CB . ALA A 1 397 ? 4.457 32.203 7.319 1.00 128.19 ? 397 ALA A CB 1 ATOM 3053 N N . ARG A 1 398 ? 6.689 33.346 5.778 1.00 111.61 ? 398 ARG A N 1 ATOM 3054 C CA . ARG A 1 398 ? 8.151 33.447 5.717 1.00 122.80 ? 398 ARG A CA 1 ATOM 3055 C C . ARG A 1 398 ? 8.778 33.097 7.066 1.00 106.00 ? 398 ARG A C 1 ATOM 3056 O O . ARG A 1 398 ? 8.381 32.123 7.707 1.00 110.41 ? 398 ARG A O 1 ATOM 3057 C CB . ARG A 1 398 ? 8.605 34.844 5.275 1.00 122.26 ? 398 ARG A CB 1 ATOM 3058 C CG . ARG A 1 398 ? 8.348 35.159 3.812 1.00 153.08 ? 398 ARG A CG 1 ATOM 3059 C CD . ARG A 1 398 ? 8.901 36.527 3.440 1.00 157.15 ? 398 ARG A CD 1 ATOM 3060 N NE . ARG A 1 398 ? 8.765 36.806 2.013 1.00 168.79 ? 398 ARG A NE 1 ATOM 3061 C CZ . ARG A 1 398 ? 9.163 37.932 1.430 1.00 166.14 ? 398 ARG A CZ 1 ATOM 3062 N NH1 . ARG A 1 398 ? 9.723 38.893 2.152 1.00 164.04 ? 398 ARG A NH1 1 ATOM 3063 N NH2 . ARG A 1 398 ? 9.000 38.098 0.124 1.00 158.60 ? 398 ARG A NH2 1 ATOM 3064 N N . SER A 1 399 ? 9.750 33.896 7.495 1.00 109.58 ? 399 SER A N 1 ATOM 3065 C CA . SER A 1 399 ? 10.518 33.595 8.702 1.00 129.79 ? 399 SER A CA 1 ATOM 3066 C C . SER A 1 399 ? 9.673 33.647 9.973 1.00 124.84 ? 399 SER A C 1 ATOM 3067 O O . SER A 1 399 ? 9.611 32.677 10.728 1.00 139.12 ? 399 SER A O 1 ATOM 3068 C CB . SER A 1 399 ? 11.698 34.562 8.831 1.00 136.37 ? 399 SER A CB 1 ATOM 3069 O OG . SER A 1 399 ? 11.250 35.902 8.951 1.00 131.62 ? 399 SER A OG 1 ATOM 3070 N N . MET A 1 400 ? 9.025 34.783 10.201 1.00 103.44 ? 400 MET A N 1 ATOM 3071 C CA . MET A 1 400 ? 8.215 34.987 11.395 1.00 90.07 ? 400 MET A CA 1 ATOM 3072 C C . MET A 1 400 ? 6.801 35.391 10.984 1.00 102.74 ? 400 MET A C 1 ATOM 3073 O O . MET A 1 400 ? 6.603 35.838 9.855 1.00 97.67 ? 400 MET A O 1 ATOM 3074 C CB . MET A 1 400 ? 8.849 36.052 12.293 1.00 82.76 ? 400 MET A CB 1 ATOM 3075 C CG . MET A 1 400 ? 8.781 37.459 11.729 1.00 83.14 ? 400 MET A CG 1 ATOM 3076 S SD . MET A 1 400 ? 9.445 38.682 12.873 1.00 100.48 ? 400 MET A SD 1 ATOM 3077 C CE . MET A 1 400 ? 8.357 38.462 14.282 1.00 71.85 ? 400 MET A CE 1 ATOM 3078 N N . PRO A 1 401 ? 5.816 35.232 11.891 1.00 111.68 ? 401 PRO A N 1 ATOM 3079 C CA . PRO A 1 401 ? 4.422 35.557 11.569 1.00 100.05 ? 401 PRO A CA 1 ATOM 3080 C C . PRO A 1 401 ? 4.261 36.930 10.937 1.00 81.58 ? 401 PRO A C 1 ATOM 3081 O O . PRO A 1 401 ? 4.940 37.866 11.357 1.00 72.42 ? 401 PRO A O 1 ATOM 3082 C CB . PRO A 1 401 ? 3.735 35.514 12.933 1.00 92.46 ? 401 PRO A CB 1 ATOM 3083 C CG . PRO A 1 401 ? 4.500 34.499 13.683 1.00 113.40 ? 401 PRO A CG 1 ATOM 3084 C CD . PRO A 1 401 ? 5.933 34.641 13.237 1.00 127.21 ? 401 PRO A CD 1 ATOM 3085 N N . PRO A 1 402 ? 3.387 37.038 9.924 1.00 77.80 ? 402 PRO A N 1 ATOM 3086 C CA . PRO A 1 402 ? 3.134 38.288 9.202 1.00 78.15 ? 402 PRO A CA 1 ATOM 3087 C C . PRO A 1 402 ? 2.843 39.442 10.153 1.00 74.92 ? 402 PRO A C 1 ATOM 3088 O O . PRO A 1 402 ? 3.222 40.572 9.870 1.00 72.38 ? 402 PRO A O 1 ATOM 3089 C CB . PRO A 1 402 ? 1.908 37.957 8.348 1.00 80.65 ? 402 PRO A CB 1 ATOM 3090 C CG . PRO A 1 402 ? 1.978 36.494 8.153 1.00 87.57 ? 402 PRO A CG 1 ATOM 3091 C CD . PRO A 1 402 ? 2.545 35.938 9.425 1.00 86.57 ? 402 PRO A CD 1 ATOM 3092 N N . SER A 1 403 ? 2.178 39.140 11.265 1.00 93.57 ? 403 SER A N 1 ATOM 3093 C CA . SER A 1 403 ? 1.890 40.122 12.305 1.00 73.64 ? 403 SER A CA 1 ATOM 3094 C C . SER A 1 403 ? 1.063 41.290 11.780 1.00 66.34 ? 403 SER A C 1 ATOM 3095 O O . SER A 1 403 ? 1.182 42.410 12.268 1.00 63.29 ? 403 SER A O 1 ATOM 3096 C CB . SER A 1 403 ? 3.190 40.636 12.930 1.00 64.91 ? 403 SER A CB 1 ATOM 3097 O OG . SER A 1 403 ? 3.885 39.592 13.592 1.00 78.28 ? 403 SER A OG 1 ATOM 3098 N N . PHE A 1 404 ? 0.224 41.015 10.785 1.00 69.55 ? 404 PHE A N 1 ATOM 3099 C CA . PHE A 1 404 ? -0.695 42.009 10.238 1.00 68.79 ? 404 PHE A CA 1 ATOM 3100 C C . PHE A 1 404 ? -1.598 42.559 11.336 1.00 64.95 ? 404 PHE A C 1 ATOM 3101 O O . PHE A 1 404 ? -2.308 41.807 11.996 1.00 76.45 ? 404 PHE A O 1 ATOM 3102 C CB . PHE A 1 404 ? -1.528 41.376 9.118 1.00 75.01 ? 404 PHE A CB 1 ATOM 3103 C CG . PHE A 1 404 ? -2.530 42.301 8.489 1.00 76.47 ? 404 PHE A CG 1 ATOM 3104 C CD1 . PHE A 1 404 ? -3.848 42.309 8.914 1.00 81.77 ? 404 PHE A CD1 1 ATOM 3105 C CD2 . PHE A 1 404 ? -2.164 43.135 7.448 1.00 86.68 ? 404 PHE A CD2 1 ATOM 3106 C CE1 . PHE A 1 404 ? -4.775 43.148 8.327 1.00 83.89 ? 404 PHE A CE1 1 ATOM 3107 C CE2 . PHE A 1 404 ? -3.087 43.975 6.855 1.00 87.69 ? 404 PHE A CE2 1 ATOM 3108 C CZ . PHE A 1 404 ? -4.394 43.982 7.297 1.00 89.76 ? 404 PHE A CZ 1 ATOM 3109 N N . GLY A 1 405 ? -1.586 43.875 11.516 1.00 69.45 ? 405 GLY A N 1 ATOM 3110 C CA . GLY A 1 405 ? -2.367 44.497 12.569 1.00 70.65 ? 405 GLY A CA 1 ATOM 3111 C C . GLY A 1 405 ? -1.612 44.737 13.867 1.00 80.59 ? 405 GLY A C 1 ATOM 3112 O O . GLY A 1 405 ? -2.186 45.225 14.836 1.00 77.26 ? 405 GLY A O 1 ATOM 3113 N N . TYR A 1 406 ? -0.324 44.409 13.897 1.00 88.98 ? 406 TYR A N 1 ATOM 3114 C CA . TYR A 1 406 ? 0.478 44.637 15.097 1.00 67.29 ? 406 TYR A CA 1 ATOM 3115 C C . TYR A 1 406 ? 0.604 46.131 15.388 1.00 69.10 ? 406 TYR A C 1 ATOM 3116 O O . TYR A 1 406 ? 0.811 46.532 16.531 1.00 94.46 ? 406 TYR A O 1 ATOM 3117 C CB . TYR A 1 406 ? 1.865 44.007 14.956 1.00 77.81 ? 406 TYR A CB 1 ATOM 3118 C CG . TYR A 1 406 ? 2.654 43.968 16.246 1.00 80.39 ? 406 TYR A CG 1 ATOM 3119 C CD1 . TYR A 1 406 ? 2.490 42.925 17.147 1.00 58.49 ? 406 TYR A CD1 1 ATOM 3120 C CD2 . TYR A 1 406 ? 3.565 44.973 16.561 1.00 76.65 ? 406 TYR A CD2 1 ATOM 3121 C CE1 . TYR A 1 406 ? 3.207 42.882 18.329 1.00 73.36 ? 406 TYR A CE1 1 ATOM 3122 C CE2 . TYR A 1 406 ? 4.290 44.938 17.743 1.00 65.94 ? 406 TYR A CE2 1 ATOM 3123 C CZ . TYR A 1 406 ? 4.104 43.889 18.623 1.00 77.08 ? 406 TYR A CZ 1 ATOM 3124 O OH . TYR A 1 406 ? 4.815 43.840 19.801 1.00 74.71 ? 406 TYR A OH 1 ATOM 3125 N N . SER A 1 407 ? 0.479 46.948 14.346 1.00 78.11 ? 407 SER A N 1 ATOM 3126 C CA . SER A 1 407 ? 0.479 48.400 14.501 1.00 63.13 ? 407 SER A CA 1 ATOM 3127 C C . SER A 1 407 ? -0.518 49.031 13.539 1.00 73.81 ? 407 SER A C 1 ATOM 3128 O O . SER A 1 407 ? -0.648 48.594 12.395 1.00 60.17 ? 407 SER A O 1 ATOM 3129 C CB . SER A 1 407 ? 1.872 48.973 14.261 1.00 77.70 ? 407 SER A CB 1 ATOM 3130 O OG . SER A 1 407 ? 2.267 48.799 12.912 1.00 76.26 ? 407 SER A OG 1 ATOM 3131 N N . MET A 1 408 ? -1.227 50.054 14.011 1.00 85.47 ? 408 MET A N 1 ATOM 3132 C CA . MET A 1 408 ? -2.253 50.725 13.214 1.00 73.90 ? 408 MET A CA 1 ATOM 3133 C C . MET A 1 408 ? -2.341 52.211 13.537 1.00 65.96 ? 408 MET A C 1 ATOM 3134 O O . MET A 1 408 ? -2.047 52.627 14.659 1.00 89.55 ? 408 MET A O 1 ATOM 3135 C CB . MET A 1 408 ? -3.629 50.091 13.445 1.00 59.84 ? 408 MET A CB 1 ATOM 3136 C CG . MET A 1 408 ? -3.758 48.631 13.067 1.00 59.77 ? 408 MET A CG 1 ATOM 3137 S SD . MET A 1 408 ? -5.417 48.005 13.404 1.00 96.57 ? 408 MET A SD 1 ATOM 3138 C CE . MET A 1 408 ? -5.545 48.314 15.162 1.00 58.86 ? 408 MET A CE 1 ATOM 3139 N N . LYS A 1 409 ? -2.747 53.006 12.551 1.00 66.14 ? 409 LYS A N 1 ATOM 3140 C CA . LYS A 1 409 ? -3.115 54.400 12.794 1.00 77.93 ? 409 LYS A CA 1 ATOM 3141 C C . LYS A 1 409 ? -4.340 54.773 11.964 1.00 69.99 ? 409 LYS A C 1 ATOM 3142 O O . LYS A 1 409 ? -4.368 54.557 10.753 1.00 66.08 ? 409 LYS A O 1 ATOM 3143 C CB . LYS A 1 409 ? -1.952 55.343 12.476 1.00 69.50 ? 409 LYS A CB 1 ATOM 3144 C CG . LYS A 1 409 ? -2.154 56.769 12.971 1.00 73.04 ? 409 LYS A CG 1 ATOM 3145 C CD . LYS A 1 409 ? -2.245 56.816 14.488 1.00 101.05 ? 409 LYS A CD 1 ATOM 3146 C CE . LYS A 1 409 ? -2.379 58.244 14.998 1.00 109.22 ? 409 LYS A CE 1 ATOM 3147 N NZ . LYS A 1 409 ? -2.454 58.292 16.487 1.00 123.58 ? 409 LYS A NZ 1 ATOM 3148 N N . GLY A 1 410 ? -5.364 55.299 12.628 1.00 75.09 ? 410 GLY A N 1 ATOM 3149 C CA . GLY A 1 410 ? -6.570 55.748 11.953 1.00 93.53 ? 410 GLY A CA 1 ATOM 3150 C C . GLY A 1 410 ? -6.760 57.253 11.977 1.00 85.82 ? 410 GLY A C 1 ATOM 3151 O O . GLY A 1 410 ? -5.793 58.013 12.052 1.00 94.69 ? 410 GLY A O 1 ATOM 3152 N N . ALA A 1 411 ? -8.022 57.667 11.866 1.00 73.22 ? 411 ALA A N 1 ATOM 3153 C CA . ALA A 1 411 ? -8.478 59.007 12.247 1.00 72.88 ? 411 ALA A CA 1 ATOM 3154 C C . ALA A 1 411 ? -8.089 60.144 11.295 1.00 75.90 ? 411 ALA A C 1 ATOM 3155 O O . ALA A 1 411 ? -8.476 61.292 11.516 1.00 78.51 ? 411 ALA A O 1 ATOM 3156 C CB . ALA A 1 411 ? -7.996 59.331 13.660 1.00 72.48 ? 411 ALA A CB 1 ATOM 3157 N N . THR A 1 412 ? -7.327 59.842 10.250 1.00 76.03 ? 412 THR A N 1 ATOM 3158 C CA . THR A 1 412 ? -6.923 60.878 9.305 1.00 79.36 ? 412 THR A CA 1 ATOM 3159 C C . THR A 1 412 ? -7.430 60.569 7.900 1.00 96.00 ? 412 THR A C 1 ATOM 3160 O O . THR A 1 412 ? -7.434 59.417 7.471 1.00 102.49 ? 412 THR A O 1 ATOM 3161 C CB . THR A 1 412 ? -5.394 61.042 9.277 1.00 79.51 ? 412 THR A CB 1 ATOM 3162 O OG1 . THR A 1 412 ? -4.898 61.141 10.618 1.00 81.56 ? 412 THR A OG1 1 ATOM 3163 C CG2 . THR A 1 412 ? -4.995 62.285 8.498 1.00 83.60 ? 412 THR A CG2 1 ATOM 3164 N N . ASP A 1 413 ? -7.856 61.605 7.186 1.00 97.70 ? 413 ASP A N 1 ATOM 3165 C CA . ASP A 1 413 ? -8.423 61.428 5.857 1.00 85.90 ? 413 ASP A CA 1 ATOM 3166 C C . ASP A 1 413 ? -7.388 61.789 4.794 1.00 91.02 ? 413 ASP A C 1 ATOM 3167 O O . ASP A 1 413 ? -7.153 62.965 4.519 1.00 92.31 ? 413 ASP A O 1 ATOM 3168 C CB . ASP A 1 413 ? -9.675 62.300 5.722 1.00 88.43 ? 413 ASP A CB 1 ATOM 3169 C CG . ASP A 1 413 ? -10.457 62.017 4.465 1.00 114.72 ? 413 ASP A CG 1 ATOM 3170 O OD1 . ASP A 1 413 ? -10.143 61.020 3.778 1.00 130.43 ? 413 ASP A OD1 1 ATOM 3171 O OD2 . ASP A 1 413 ? -11.392 62.793 4.167 1.00 93.26 ? 413 ASP A OD2 1 ATOM 3172 N N . ILE A 1 414 ? -6.814 60.771 4.159 1.00 87.51 ? 414 ILE A N 1 ATOM 3173 C CA . ILE A 1 414 ? -5.640 60.965 3.310 1.00 92.32 ? 414 ILE A CA 1 ATOM 3174 C C . ILE A 1 414 ? -6.047 61.318 1.888 1.00 93.99 ? 414 ILE A C 1 ATOM 3175 O O . ILE A 1 414 ? -5.235 61.766 1.078 1.00 99.04 ? 414 ILE A O 1 ATOM 3176 C CB . ILE A 1 414 ? -4.744 59.711 3.296 1.00 92.70 ? 414 ILE A CB 1 ATOM 3177 C CG1 . ILE A 1 414 ? -3.351 60.051 2.758 1.00 90.53 ? 414 ILE A CG1 1 ATOM 3178 C CG2 . ILE A 1 414 ? -5.401 58.593 2.499 1.00 90.73 ? 414 ILE A CG2 1 ATOM 3179 C CD1 . ILE A 1 414 ? -2.416 58.874 2.705 1.00 100.29 ? 414 ILE A CD1 1 ATOM 3180 N N . ASP A 1 415 ? -7.323 61.119 1.599 1.00 93.89 ? 415 ASP A N 1 ATOM 3181 C CA . ASP A 1 415 ? -7.900 61.529 0.333 1.00 97.86 ? 415 ASP A CA 1 ATOM 3182 C C . ASP A 1 415 ? -9.033 62.470 0.688 1.00 100.98 ? 415 ASP A C 1 ATOM 3183 O O . ASP A 1 415 ? -9.418 62.557 1.846 1.00 124.93 ? 415 ASP A O 1 ATOM 3184 C CB . ASP A 1 415 ? -8.377 60.329 -0.491 1.00 98.54 ? 415 ASP A CB 1 ATOM 3185 C CG . ASP A 1 415 ? -9.406 59.478 0.235 1.00 112.37 ? 415 ASP A CG 1 ATOM 3186 O OD1 . ASP A 1 415 ? -9.485 59.543 1.483 1.00 116.59 ? 415 ASP A OD1 1 ATOM 3187 O OD2 . ASP A 1 415 ? -10.136 58.730 -0.451 1.00 116.63 ? 415 ASP A OD2 1 ATOM 3188 N N . LYS A 1 416 ? -9.558 63.197 -0.282 1.00 103.39 ? 416 LYS A N 1 ATOM 3189 C CA . LYS A 1 416 ? -10.527 64.229 0.044 1.00 120.51 ? 416 LYS A CA 1 ATOM 3190 C C . LYS A 1 416 ? -11.936 63.662 0.127 1.00 137.73 ? 416 LYS A C 1 ATOM 3191 O O . LYS A 1 416 ? -12.898 64.416 0.261 1.00 164.47 ? 416 LYS A O 1 ATOM 3192 C CB . LYS A 1 416 ? -10.465 65.371 -0.971 1.00 155.60 ? 416 LYS A CB 1 ATOM 3193 C CG . LYS A 1 416 ? -9.178 66.183 -0.891 1.00 172.12 ? 416 LYS A CG 1 ATOM 3194 C CD . LYS A 1 416 ? -8.846 66.577 0.547 1.00 151.46 ? 416 LYS A CD 1 ATOM 3195 C CE . LYS A 1 416 ? -9.875 67.540 1.128 1.00 156.14 ? 416 LYS A CE 1 ATOM 3196 N NZ . LYS A 1 416 ? -9.982 68.795 0.334 1.00 151.71 ? 416 LYS A NZ 1 ATOM 3197 N N . ASN A 1 417 ? -12.048 62.335 0.065 1.00 113.84 ? 417 ASN A N 1 ATOM 3198 C CA . ASN A 1 417 ? -13.344 61.655 0.027 1.00 121.29 ? 417 ASN A CA 1 ATOM 3199 C C . ASN A 1 417 ? -14.282 62.046 1.169 1.00 122.15 ? 417 ASN A C 1 ATOM 3200 O O . ASN A 1 417 ? -15.491 61.839 1.080 1.00 133.25 ? 417 ASN A O 1 ATOM 3201 C CB . ASN A 1 417 ? -13.154 60.129 0.023 1.00 118.06 ? 417 ASN A CB 1 ATOM 3202 C CG . ASN A 1 417 ? -12.458 59.602 1.277 1.00 121.95 ? 417 ASN A CG 1 ATOM 3203 O OD1 . ASN A 1 417 ? -12.020 60.362 2.141 1.00 143.23 ? 417 ASN A OD1 1 ATOM 3204 N ND2 . ASN A 1 417 ? -12.352 58.282 1.373 1.00 103.99 ? 417 ASN A ND2 1 ATOM 3205 N N . GLY A 1 418 ? -13.725 62.612 2.234 1.00 95.64 ? 418 GLY A N 1 ATOM 3206 C CA . GLY A 1 418 ? -14.531 63.101 3.335 1.00 95.07 ? 418 GLY A CA 1 ATOM 3207 C C . GLY A 1 418 ? -14.707 62.057 4.416 1.00 105.12 ? 418 GLY A C 1 ATOM 3208 O O . GLY A 1 418 ? -15.459 62.254 5.370 1.00 93.94 ? 418 GLY A O 1 ATOM 3209 N N . TYR A 1 419 ? -14.014 60.935 4.259 1.00 87.73 ? 419 TYR A N 1 ATOM 3210 C CA . TYR A 1 419 ? -14.052 59.878 5.256 1.00 83.71 ? 419 TYR A CA 1 ATOM 3211 C C . TYR A 1 419 ? -12.640 59.528 5.708 1.00 82.08 ? 419 TYR A C 1 ATOM 3212 O O . TYR A 1 419 ? -11.721 59.448 4.886 1.00 83.08 ? 419 TYR A O 1 ATOM 3213 C CB . TYR A 1 419 ? -14.755 58.637 4.699 1.00 104.09 ? 419 TYR A CB 1 ATOM 3214 C CG . TYR A 1 419 ? -16.224 58.836 4.394 1.00 90.56 ? 419 TYR A CG 1 ATOM 3215 C CD1 . TYR A 1 419 ? -16.632 59.582 3.297 1.00 94.49 ? 419 TYR A CD1 1 ATOM 3216 C CD2 . TYR A 1 419 ? -17.203 58.262 5.194 1.00 81.07 ? 419 TYR A CD2 1 ATOM 3217 C CE1 . TYR A 1 419 ? -17.971 59.768 3.014 1.00 99.65 ? 419 TYR A CE1 1 ATOM 3218 C CE2 . TYR A 1 419 ? -18.546 58.435 4.914 1.00 99.72 ? 419 TYR A CE2 1 ATOM 3219 C CZ . TYR A 1 419 ? -18.924 59.190 3.823 1.00 105.30 ? 419 TYR A CZ 1 ATOM 3220 O OH . TYR A 1 419 ? -20.257 59.369 3.537 1.00 104.12 ? 419 TYR A OH 1 ATOM 3221 N N . PRO A 1 420 ? -12.472 59.295 7.020 1.00 80.83 ? 420 PRO A N 1 ATOM 3222 C CA . PRO A 1 420 ? -11.173 58.954 7.604 1.00 78.07 ? 420 PRO A CA 1 ATOM 3223 C C . PRO A 1 420 ? -10.735 57.567 7.169 1.00 77.78 ? 420 PRO A C 1 ATOM 3224 O O . PRO A 1 420 ? -11.568 56.676 7.035 1.00 87.05 ? 420 PRO A O 1 ATOM 3225 C CB . PRO A 1 420 ? -11.440 59.005 9.110 1.00 76.55 ? 420 PRO A CB 1 ATOM 3226 C CG . PRO A 1 420 ? -12.883 58.693 9.237 1.00 77.44 ? 420 PRO A CG 1 ATOM 3227 C CD . PRO A 1 420 ? -13.538 59.321 8.036 1.00 98.19 ? 420 PRO A CD 1 ATOM 3228 N N . ASP A 1 421 ? -9.439 57.391 6.955 1.00 80.58 ? 421 ASP A N 1 ATOM 3229 C CA . ASP A 1 421 ? -8.930 56.143 6.414 1.00 82.79 ? 421 ASP A CA 1 ATOM 3230 C C . ASP A 1 421 ? -8.010 55.457 7.434 1.00 92.49 ? 421 ASP A C 1 ATOM 3231 O O . ASP A 1 421 ? -7.872 55.934 8.562 1.00 79.54 ? 421 ASP A O 1 ATOM 3232 C CB . ASP A 1 421 ? -8.231 56.423 5.084 1.00 80.84 ? 421 ASP A CB 1 ATOM 3233 C CG . ASP A 1 421 ? -9.052 57.353 4.188 1.00 111.46 ? 421 ASP A CG 1 ATOM 3234 O OD1 . ASP A 1 421 ? -9.966 56.872 3.486 1.00 115.06 ? 421 ASP A OD1 1 ATOM 3235 O OD2 . ASP A 1 421 ? -8.803 58.576 4.195 1.00 131.21 ? 421 ASP A OD2 1 ATOM 3236 N N . LEU A 1 422 ? -7.407 54.332 7.059 1.00 94.26 ? 422 LEU A N 1 ATOM 3237 C CA . LEU A 1 422 ? -6.693 53.509 8.037 1.00 68.55 ? 422 LEU A CA 1 ATOM 3238 C C . LEU A 1 422 ? -5.392 52.894 7.522 1.00 70.44 ? 422 LEU A C 1 ATOM 3239 O O . LEU A 1 422 ? -5.324 52.399 6.397 1.00 88.59 ? 422 LEU A O 1 ATOM 3240 C CB . LEU A 1 422 ? -7.613 52.390 8.532 1.00 67.12 ? 422 LEU A CB 1 ATOM 3241 C CG . LEU A 1 422 ? -7.001 51.351 9.472 1.00 64.82 ? 422 LEU A CG 1 ATOM 3242 C CD1 . LEU A 1 422 ? -6.596 51.985 10.795 1.00 63.79 ? 422 LEU A CD1 1 ATOM 3243 C CD2 . LEU A 1 422 ? -7.964 50.199 9.695 1.00 79.32 ? 422 LEU A CD2 1 ATOM 3244 N N . ILE A 1 423 ? -4.364 52.917 8.366 1.00 67.53 ? 423 ILE A N 1 ATOM 3245 C CA . ILE A 1 423 ? -3.098 52.259 8.063 1.00 75.41 ? 423 ILE A CA 1 ATOM 3246 C C . ILE A 1 423 ? -2.908 51.033 8.944 1.00 72.07 ? 423 ILE A C 1 ATOM 3247 O O . ILE A 1 423 ? -3.134 51.093 10.151 1.00 90.15 ? 423 ILE A O 1 ATOM 3248 C CB . ILE A 1 423 ? -1.897 53.200 8.272 1.00 82.29 ? 423 ILE A CB 1 ATOM 3249 C CG1 . ILE A 1 423 ? -2.158 54.562 7.635 1.00 72.87 ? 423 ILE A CG1 1 ATOM 3250 C CG2 . ILE A 1 423 ? -0.622 52.580 7.713 1.00 68.80 ? 423 ILE A CG2 1 ATOM 3251 C CD1 . ILE A 1 423 ? -1.128 55.598 8.012 1.00 84.15 ? 423 ILE A CD1 1 ATOM 3252 N N . VAL A 1 424 ? -2.489 49.925 8.341 1.00 69.66 ? 424 VAL A N 1 ATOM 3253 C CA . VAL A 1 424 ? -2.176 48.713 9.092 1.00 64.41 ? 424 VAL A CA 1 ATOM 3254 C C . VAL A 1 424 ? -0.750 48.250 8.797 1.00 68.91 ? 424 VAL A C 1 ATOM 3255 O O . VAL A 1 424 ? -0.366 48.103 7.635 1.00 73.75 ? 424 VAL A O 1 ATOM 3256 C CB . VAL A 1 424 ? -3.158 47.571 8.766 1.00 70.59 ? 424 VAL A CB 1 ATOM 3257 C CG1 . VAL A 1 424 ? -2.740 46.293 9.473 1.00 68.24 ? 424 VAL A CG1 1 ATOM 3258 C CG2 . VAL A 1 424 ? -4.576 47.960 9.153 1.00 67.50 ? 424 VAL A CG2 1 ATOM 3259 N N . GLY A 1 425 ? 0.038 48.046 9.847 1.00 63.55 ? 425 GLY A N 1 ATOM 3260 C CA . GLY A 1 425 ? 1.397 47.562 9.686 1.00 70.59 ? 425 GLY A CA 1 ATOM 3261 C C . GLY A 1 425 ? 1.499 46.052 9.774 1.00 85.21 ? 425 GLY A C 1 ATOM 3262 O O . GLY A 1 425 ? 0.713 45.409 10.467 1.00 94.98 ? 425 GLY A O 1 ATOM 3263 N N . ALA A 1 426 ? 2.488 45.488 9.090 1.00 90.02 ? 426 ALA A N 1 ATOM 3264 C CA . ALA A 1 426 ? 2.687 44.044 9.087 1.00 80.46 ? 426 ALA A CA 1 ATOM 3265 C C . ALA A 1 426 ? 4.004 43.686 9.757 1.00 85.33 ? 426 ALA A C 1 ATOM 3266 O O . ALA A 1 426 ? 4.016 43.028 10.788 1.00 138.23 ? 426 ALA A O 1 ATOM 3267 C CB . ALA A 1 426 ? 2.649 43.506 7.675 1.00 81.01 ? 426 ALA A CB 1 ATOM 3268 N N . PHE A 1 427 ? 5.103 44.073 9.115 1.00 82.22 ? 427 PHE A N 1 ATOM 3269 C CA . PHE A 1 427 ? 6.466 44.024 9.664 1.00 95.21 ? 427 PHE A CA 1 ATOM 3270 C C . PHE A 1 427 ? 7.015 42.602 9.744 1.00 90.66 ? 427 PHE A C 1 ATOM 3271 O O . PHE A 1 427 ? 8.228 42.409 9.822 1.00 97.59 ? 427 PHE A O 1 ATOM 3272 C CB . PHE A 1 427 ? 6.535 44.749 11.037 1.00 82.12 ? 427 PHE A CB 1 ATOM 3273 C CG . PHE A 1 427 ? 6.645 43.839 12.252 1.00 76.39 ? 427 PHE A CG 1 ATOM 3274 C CD1 . PHE A 1 427 ? 7.852 43.251 12.607 1.00 86.30 ? 427 PHE A CD1 1 ATOM 3275 C CD2 . PHE A 1 427 ? 5.559 43.657 13.094 1.00 61.80 ? 427 PHE A CD2 1 ATOM 3276 C CE1 . PHE A 1 427 ? 7.948 42.438 13.722 1.00 75.09 ? 427 PHE A CE1 1 ATOM 3277 C CE2 . PHE A 1 427 ? 5.651 42.850 14.214 1.00 61.16 ? 427 PHE A CE2 1 ATOM 3278 C CZ . PHE A 1 427 ? 6.846 42.243 14.530 1.00 63.86 ? 427 PHE A CZ 1 ATOM 3279 N N . GLY A 1 428 ? 6.138 41.608 9.672 1.00 77.81 ? 428 GLY A N 1 ATOM 3280 C CA . GLY A 1 428 ? 6.586 40.235 9.556 1.00 80.30 ? 428 GLY A CA 1 ATOM 3281 C C . GLY A 1 428 ? 6.995 40.027 8.115 1.00 90.86 ? 428 GLY A C 1 ATOM 3282 O O . GLY A 1 428 ? 8.021 39.418 7.814 1.00 103.99 ? 428 GLY A O 1 ATOM 3283 N N . VAL A 1 429 ? 6.166 40.553 7.220 1.00 91.43 ? 429 VAL A N 1 ATOM 3284 C CA . VAL A 1 429 ? 6.437 40.530 5.794 1.00 99.51 ? 429 VAL A CA 1 ATOM 3285 C C . VAL A 1 429 ? 7.059 41.849 5.350 1.00 109.88 ? 429 VAL A C 1 ATOM 3286 O O . VAL A 1 429 ? 7.299 42.063 4.160 1.00 120.70 ? 429 VAL A O 1 ATOM 3287 C CB . VAL A 1 429 ? 5.158 40.261 4.994 1.00 103.87 ? 429 VAL A CB 1 ATOM 3288 C CG1 . VAL A 1 429 ? 4.539 38.955 5.441 1.00 93.09 ? 429 VAL A CG1 1 ATOM 3289 C CG2 . VAL A 1 429 ? 4.173 41.396 5.182 1.00 107.72 ? 429 VAL A CG2 1 ATOM 3290 N N . ASP A 1 430 ? 7.304 42.727 6.323 1.00 124.38 ? 430 ASP A N 1 ATOM 3291 C CA . ASP A 1 430 ? 7.890 44.048 6.087 1.00 104.16 ? 430 ASP A CA 1 ATOM 3292 C C . ASP A 1 430 ? 7.052 44.872 5.116 1.00 98.19 ? 430 ASP A C 1 ATOM 3293 O O . ASP A 1 430 ? 7.559 45.381 4.117 1.00 101.30 ? 430 ASP A O 1 ATOM 3294 C CB . ASP A 1 430 ? 9.325 43.920 5.566 1.00 102.87 ? 430 ASP A CB 1 ATOM 3295 C CG . ASP A 1 430 ? 10.232 43.182 6.531 1.00 105.02 ? 430 ASP A CG 1 ATOM 3296 O OD1 . ASP A 1 430 ? 9.755 42.237 7.194 1.00 125.10 ? 430 ASP A OD1 1 ATOM 3297 O OD2 . ASP A 1 430 ? 11.419 43.550 6.633 1.00 105.70 ? 430 ASP A OD2 1 ATOM 3298 N N . ARG A 1 431 ? 5.762 44.993 5.413 1.00 94.03 ? 431 ARG A N 1 ATOM 3299 C CA . ARG A 1 431 ? 4.851 45.740 4.554 1.00 92.12 ? 431 ARG A CA 1 ATOM 3300 C C . ARG A 1 431 ? 3.895 46.619 5.359 1.00 91.24 ? 431 ARG A C 1 ATOM 3301 O O . ARG A 1 431 ? 3.710 46.424 6.563 1.00 78.30 ? 431 ARG A O 1 ATOM 3302 C CB . ARG A 1 431 ? 4.051 44.784 3.664 1.00 97.50 ? 431 ARG A CB 1 ATOM 3303 C CG . ARG A 1 431 ? 4.904 43.958 2.713 1.00 104.67 ? 431 ARG A CG 1 ATOM 3304 C CD . ARG A 1 431 ? 4.059 43.009 1.884 1.00 102.39 ? 431 ARG A CD 1 ATOM 3305 N NE . ARG A 1 431 ? 4.070 43.365 0.470 1.00 109.14 ? 431 ARG A NE 1 ATOM 3306 C CZ . ARG A 1 431 ? 5.040 43.030 -0.375 1.00 130.28 ? 431 ARG A CZ 1 ATOM 3307 N NH1 . ARG A 1 431 ? 6.083 42.335 0.056 1.00 136.12 ? 431 ARG A NH1 1 ATOM 3308 N NH2 . ARG A 1 431 ? 4.970 43.395 -1.648 1.00 149.91 ? 431 ARG A NH2 1 ATOM 3309 N N . ALA A 1 432 ? 3.294 47.592 4.683 1.00 84.17 ? 432 ALA A N 1 ATOM 3310 C CA . ALA A 1 432 ? 2.278 48.439 5.294 1.00 79.52 ? 432 ALA A CA 1 ATOM 3311 C C . ALA A 1 432 ? 1.131 48.640 4.314 1.00 87.91 ? 432 ALA A C 1 ATOM 3312 O O . ALA A 1 432 ? 1.356 48.869 3.125 1.00 87.32 ? 432 ALA A O 1 ATOM 3313 C CB . ALA A 1 432 ? 2.867 49.769 5.711 1.00 92.71 ? 432 ALA A CB 1 ATOM 3314 N N . ILE A 1 433 ? -0.098 48.546 4.813 1.00 80.38 ? 433 ILE A N 1 ATOM 3315 C CA . ILE A 1 433 ? -1.273 48.596 3.951 1.00 88.11 ? 433 ILE A CA 1 ATOM 3316 C C . ILE A 1 433 ? -2.188 49.761 4.310 1.00 83.47 ? 433 ILE A C 1 ATOM 3317 O O . ILE A 1 433 ? -2.458 50.011 5.485 1.00 76.48 ? 433 ILE A O 1 ATOM 3318 C CB . ILE A 1 433 ? -2.080 47.282 4.026 1.00 93.63 ? 433 ILE A CB 1 ATOM 3319 C CG1 . ILE A 1 433 ? -1.148 46.072 3.928 1.00 96.04 ? 433 ILE A CG1 1 ATOM 3320 C CG2 . ILE A 1 433 ? -3.141 47.238 2.931 1.00 99.14 ? 433 ILE A CG2 1 ATOM 3321 C CD1 . ILE A 1 433 ? -0.413 45.971 2.606 1.00 121.64 ? 433 ILE A CD1 1 ATOM 3322 N N . LEU A 1 434 ? -2.663 50.468 3.290 1.00 82.93 ? 434 LEU A N 1 ATOM 3323 C CA . LEU A 1 434 ? -3.577 51.584 3.496 1.00 86.26 ? 434 LEU A CA 1 ATOM 3324 C C . LEU A 1 434 ? -4.972 51.280 2.956 1.00 87.93 ? 434 LEU A C 1 ATOM 3325 O O . LEU A 1 434 ? -5.150 51.045 1.761 1.00 89.57 ? 434 LEU A O 1 ATOM 3326 C CB . LEU A 1 434 ? -3.028 52.850 2.839 1.00 82.24 ? 434 LEU A CB 1 ATOM 3327 C CG . LEU A 1 434 ? -3.996 54.026 2.692 1.00 82.00 ? 434 LEU A CG 1 ATOM 3328 C CD1 . LEU A 1 434 ? -4.527 54.481 4.042 1.00 77.59 ? 434 LEU A CD1 1 ATOM 3329 C CD2 . LEU A 1 434 ? -3.311 55.171 1.977 1.00 91.44 ? 434 LEU A CD2 1 ATOM 3330 N N . TYR A 1 435 ? -5.957 51.291 3.848 1.00 79.32 ? 435 TYR A N 1 ATOM 3331 C CA . TYR A 1 435 ? -7.345 51.085 3.461 1.00 85.13 ? 435 TYR A CA 1 ATOM 3332 C C . TYR A 1 435 ? -8.106 52.402 3.440 1.00 82.26 ? 435 TYR A C 1 ATOM 3333 O O . TYR A 1 435 ? -8.178 53.102 4.449 1.00 76.60 ? 435 TYR A O 1 ATOM 3334 C CB . TYR A 1 435 ? -8.031 50.102 4.413 1.00 94.14 ? 435 TYR A CB 1 ATOM 3335 C CG . TYR A 1 435 ? -7.446 48.711 4.370 1.00 86.12 ? 435 TYR A CG 1 ATOM 3336 C CD1 . TYR A 1 435 ? -7.884 47.781 3.437 1.00 96.40 ? 435 TYR A CD1 1 ATOM 3337 C CD2 . TYR A 1 435 ? -6.455 48.329 5.259 1.00 79.96 ? 435 TYR A CD2 1 ATOM 3338 C CE1 . TYR A 1 435 ? -7.349 46.508 3.393 1.00 96.99 ? 435 TYR A CE1 1 ATOM 3339 C CE2 . TYR A 1 435 ? -5.915 47.059 5.222 1.00 93.16 ? 435 TYR A CE2 1 ATOM 3340 C CZ . TYR A 1 435 ? -6.364 46.153 4.289 1.00 87.73 ? 435 TYR A CZ 1 ATOM 3341 O OH . TYR A 1 435 ? -5.823 44.888 4.254 1.00 86.23 ? 435 TYR A OH 1 ATOM 3342 N N . ARG A 1 436 ? -8.672 52.735 2.284 1.00 86.94 ? 436 ARG A N 1 ATOM 3343 C CA . ARG A 1 436 ? -9.467 53.948 2.150 1.00 84.00 ? 436 ARG A CA 1 ATOM 3344 C C . ARG A 1 436 ? -10.932 53.678 2.455 1.00 88.71 ? 436 ARG A C 1 ATOM 3345 O O . ARG A 1 436 ? -11.502 52.697 1.980 1.00 108.75 ? 436 ARG A O 1 ATOM 3346 C CB . ARG A 1 436 ? -9.332 54.534 0.745 1.00 87.77 ? 436 ARG A CB 1 ATOM 3347 C CG . ARG A 1 436 ? -7.955 55.078 0.423 1.00 94.46 ? 436 ARG A CG 1 ATOM 3348 C CD . ARG A 1 436 ? -7.913 55.599 -0.998 1.00 109.33 ? 436 ARG A CD 1 ATOM 3349 N NE . ARG A 1 436 ? -8.340 54.579 -1.950 1.00 123.74 ? 436 ARG A NE 1 ATOM 3350 C CZ . ARG A 1 436 ? -8.547 54.803 -3.242 1.00 132.33 ? 436 ARG A CZ 1 ATOM 3351 N NH1 . ARG A 1 436 ? -8.370 56.019 -3.741 1.00 135.34 ? 436 ARG A NH1 1 ATOM 3352 N NH2 . ARG A 1 436 ? -8.935 53.813 -4.035 1.00 130.95 ? 436 ARG A NH2 1 ATOM 3353 N N . ALA A 1 437 ? -11.537 54.552 3.251 1.00 92.42 ? 437 ALA A N 1 ATOM 3354 C CA . ALA A 1 437 ? -12.951 54.427 3.572 1.00 84.61 ? 437 ALA A CA 1 ATOM 3355 C C . ALA A 1 437 ? -13.803 54.824 2.377 1.00 97.69 ? 437 ALA A C 1 ATOM 3356 O O . ALA A 1 437 ? -13.536 55.828 1.717 1.00 100.09 ? 437 ALA A O 1 ATOM 3357 C CB . ALA A 1 437 ? -13.304 55.278 4.778 1.00 77.06 ? 437 ALA A CB 1 ATOM 3358 N N . ARG A 1 438 ? -14.824 54.024 2.098 1.00 91.90 ? 438 ARG A N 1 ATOM 3359 C CA . ARG A 1 438 ? -15.756 54.336 1.028 1.00 89.47 ? 438 ARG A CA 1 ATOM 3360 C C . ARG A 1 438 ? -16.887 55.195 1.581 1.00 85.68 ? 438 ARG A C 1 ATOM 3361 O O . ARG A 1 438 ? -17.256 55.060 2.749 1.00 81.88 ? 438 ARG A O 1 ATOM 3362 C CB . ARG A 1 438 ? -16.301 53.053 0.394 1.00 107.75 ? 438 ARG A CB 1 ATOM 3363 C CG . ARG A 1 438 ? -15.230 52.003 0.132 1.00 119.78 ? 438 ARG A CG 1 ATOM 3364 C CD . ARG A 1 438 ? -15.680 50.947 -0.862 1.00 121.95 ? 438 ARG A CD 1 ATOM 3365 N NE . ARG A 1 438 ? -17.032 50.466 -0.598 1.00 117.96 ? 438 ARG A NE 1 ATOM 3366 C CZ . ARG A 1 438 ? -17.649 49.551 -1.338 1.00 102.41 ? 438 ARG A CZ 1 ATOM 3367 N NH1 . ARG A 1 438 ? -18.880 49.167 -1.037 1.00 91.42 ? 438 ARG A NH1 1 ATOM 3368 N NH2 . ARG A 1 438 ? -17.032 49.020 -2.383 1.00 118.23 ? 438 ARG A NH2 1 ATOM 3369 N N . PRO A 1 439 ? -17.426 56.099 0.750 1.00 87.24 ? 439 PRO A N 1 ATOM 3370 C CA . PRO A 1 439 ? -18.551 56.944 1.164 1.00 87.78 ? 439 PRO A CA 1 ATOM 3371 C C . PRO A 1 439 ? -19.825 56.142 1.435 1.00 95.05 ? 439 PRO A C 1 ATOM 3372 O O . PRO A 1 439 ? -20.065 55.118 0.794 1.00 86.39 ? 439 PRO A O 1 ATOM 3373 C CB . PRO A 1 439 ? -18.738 57.892 -0.027 1.00 90.43 ? 439 PRO A CB 1 ATOM 3374 C CG . PRO A 1 439 ? -18.086 57.203 -1.180 1.00 95.80 ? 439 PRO A CG 1 ATOM 3375 C CD . PRO A 1 439 ? -16.942 56.441 -0.598 1.00 90.91 ? 439 PRO A CD 1 ATOM 3376 N N . VAL A 1 440 ? -20.630 56.616 2.382 1.00 105.80 ? 440 VAL A N 1 ATOM 3377 C CA . VAL A 1 440 ? -21.843 55.916 2.794 1.00 96.43 ? 440 VAL A CA 1 ATOM 3378 C C . VAL A 1 440 ? -23.112 56.604 2.289 1.00 106.95 ? 440 VAL A C 1 ATOM 3379 O O . VAL A 1 440 ? -23.304 57.805 2.494 1.00 100.73 ? 440 VAL A O 1 ATOM 3380 C CB . VAL A 1 440 ? -21.915 55.796 4.330 1.00 87.97 ? 440 VAL A CB 1 ATOM 3381 C CG1 . VAL A 1 440 ? -23.288 55.314 4.773 1.00 84.97 ? 440 VAL A CG1 1 ATOM 3382 C CG2 . VAL A 1 440 ? -20.826 54.868 4.838 1.00 95.30 ? 440 VAL A CG2 1 ATOM 3383 N N . ILE A 1 441 ? -23.973 55.833 1.630 1.00 107.72 ? 441 ILE A N 1 ATOM 3384 C CA . ILE A 1 441 ? -25.247 56.343 1.133 1.00 98.22 ? 441 ILE A CA 1 ATOM 3385 C C . ILE A 1 441 ? -26.426 55.775 1.914 1.00 90.91 ? 441 ILE A C 1 ATOM 3386 O O . ILE A 1 441 ? -26.570 54.560 2.032 1.00 92.98 ? 441 ILE A O 1 ATOM 3387 C CB . ILE A 1 441 ? -25.453 56.009 -0.353 1.00 93.32 ? 441 ILE A CB 1 ATOM 3388 C CG1 . ILE A 1 441 ? -24.237 56.430 -1.178 1.00 105.18 ? 441 ILE A CG1 1 ATOM 3389 C CG2 . ILE A 1 441 ? -26.714 56.677 -0.875 1.00 97.93 ? 441 ILE A CG2 1 ATOM 3390 C CD1 . ILE A 1 441 ? -24.388 56.134 -2.652 1.00 96.29 ? 441 ILE A CD1 1 ATOM 3391 N N . THR A 1 442 ? -27.269 56.657 2.442 1.00 101.91 ? 442 THR A N 1 ATOM 3392 C CA . THR A 1 442 ? -28.490 56.232 3.117 1.00 106.52 ? 442 THR A CA 1 ATOM 3393 C C . THR A 1 442 ? -29.677 56.392 2.173 1.00 109.37 ? 442 THR A C 1 ATOM 3394 O O . THR A 1 442 ? -30.032 57.508 1.789 1.00 90.49 ? 442 THR A O 1 ATOM 3395 C CB . THR A 1 442 ? -28.742 57.029 4.411 1.00 112.81 ? 442 THR A CB 1 ATOM 3396 O OG1 . THR A 1 442 ? -28.897 58.418 4.099 1.00 132.54 ? 442 THR A OG1 1 ATOM 3397 C CG2 . THR A 1 442 ? -27.578 56.858 5.379 1.00 107.50 ? 442 THR A CG2 1 ATOM 3398 N N . VAL A 1 443 ? -30.284 55.269 1.802 1.00 120.16 ? 443 VAL A N 1 ATOM 3399 C CA . VAL A 1 443 ? -31.340 55.258 0.795 1.00 111.63 ? 443 VAL A CA 1 ATOM 3400 C C . VAL A 1 443 ? -32.680 54.787 1.361 1.00 120.37 ? 443 VAL A C 1 ATOM 3401 O O . VAL A 1 443 ? -32.746 53.798 2.092 1.00 141.72 ? 443 VAL A O 1 ATOM 3402 C CB . VAL A 1 443 ? -30.945 54.360 -0.405 1.00 111.87 ? 443 VAL A CB 1 ATOM 3403 C CG1 . VAL A 1 443 ? -30.508 52.978 0.070 1.00 131.13 ? 443 VAL A CG1 1 ATOM 3404 C CG2 . VAL A 1 443 ? -32.083 54.261 -1.409 1.00 105.58 ? 443 VAL A CG2 1 ATOM 3405 N N . ASN A 1 444 ? -33.746 55.508 1.029 1.00 109.63 ? 444 ASN A N 1 ATOM 3406 C CA . ASN A 1 444 ? -35.093 55.099 1.410 1.00 126.39 ? 444 ASN A CA 1 ATOM 3407 C C . ASN A 1 444 ? -36.013 55.015 0.192 1.00 116.65 ? 444 ASN A C 1 ATOM 3408 O O . ASN A 1 444 ? -36.017 55.906 -0.660 1.00 98.55 ? 444 ASN A O 1 ATOM 3409 C CB . ASN A 1 444 ? -35.674 56.058 2.451 1.00 130.14 ? 444 ASN A CB 1 ATOM 3410 C CG . ASN A 1 444 ? -35.666 57.499 1.987 1.00 141.00 ? 444 ASN A CG 1 ATOM 3411 O OD1 . ASN A 1 444 ? -36.603 57.959 1.335 1.00 148.27 ? 444 ASN A OD1 1 ATOM 3412 N ND2 . ASN A 1 444 ? -34.605 58.223 2.325 1.00 138.17 ? 444 ASN A ND2 1 ATOM 3413 N N . ALA A 1 445 ? -36.788 53.936 0.115 1.00 105.69 ? 445 ALA A N 1 ATOM 3414 C CA . ALA A 1 445 ? -37.640 53.691 -1.043 1.00 100.57 ? 445 ALA A CA 1 ATOM 3415 C C . ALA A 1 445 ? -39.096 53.491 -0.650 1.00 98.46 ? 445 ALA A C 1 ATOM 3416 O O . ALA A 1 445 ? -39.422 52.592 0.123 1.00 118.41 ? 445 ALA A O 1 ATOM 3417 C CB . ALA A 1 445 ? -37.140 52.482 -1.816 1.00 105.27 ? 445 ALA A CB 1 ATOM 3418 N N . GLY A 1 446 ? -39.968 54.339 -1.185 1.00 97.89 ? 446 GLY A N 1 ATOM 3419 C CA . GLY A 1 446 ? -41.397 54.204 -0.970 1.00 108.02 ? 446 GLY A CA 1 ATOM 3420 C C . GLY A 1 446 ? -42.070 53.318 -2.003 1.00 114.09 ? 446 GLY A C 1 ATOM 3421 O O . GLY A 1 446 ? -41.653 53.264 -3.161 1.00 101.17 ? 446 GLY A O 1 ATOM 3422 N N . LEU A 1 447 ? -43.124 52.628 -1.580 1.00 118.21 ? 447 LEU A N 1 ATOM 3423 C CA . LEU A 1 447 ? -43.918 51.802 -2.481 1.00 99.11 ? 447 LEU A CA 1 ATOM 3424 C C . LEU A 1 447 ? -45.396 51.952 -2.147 1.00 103.66 ? 447 LEU A C 1 ATOM 3425 O O . LEU A 1 447 ? -45.785 51.866 -0.982 1.00 109.11 ? 447 LEU A O 1 ATOM 3426 C CB . LEU A 1 447 ? -43.499 50.334 -2.392 1.00 91.44 ? 447 LEU A CB 1 ATOM 3427 C CG . LEU A 1 447 ? -44.200 49.379 -3.361 1.00 94.86 ? 447 LEU A CG 1 ATOM 3428 C CD1 . LEU A 1 447 ? -43.891 49.752 -4.803 1.00 93.60 ? 447 LEU A CD1 1 ATOM 3429 C CD2 . LEU A 1 447 ? -43.812 47.935 -3.084 1.00 90.50 ? 447 LEU A CD2 1 ATOM 3430 N N . GLU A 1 448 ? -46.215 52.179 -3.168 1.00 105.84 ? 448 GLU A N 1 ATOM 3431 C CA . GLU A 1 448 ? -47.646 52.366 -2.961 1.00 121.61 ? 448 GLU A CA 1 ATOM 3432 C C . GLU A 1 448 ? -48.456 51.666 -4.049 1.00 117.03 ? 448 GLU A C 1 ATOM 3433 O O . GLU A 1 448 ? -47.968 51.459 -5.161 1.00 105.84 ? 448 GLU A O 1 ATOM 3434 C CB . GLU A 1 448 ? -47.984 53.858 -2.918 1.00 135.27 ? 448 GLU A CB 1 ATOM 3435 C CG . GLU A 1 448 ? -49.348 54.176 -2.326 1.00 147.51 ? 448 GLU A CG 1 ATOM 3436 C CD . GLU A 1 448 ? -49.564 55.662 -2.129 1.00 158.95 ? 448 GLU A CD 1 ATOM 3437 O OE1 . GLU A 1 448 ? -48.622 56.441 -2.389 1.00 153.42 ? 448 GLU A OE1 1 ATOM 3438 O OE2 . GLU A 1 448 ? -50.677 56.052 -1.714 1.00 161.72 ? 448 GLU A OE2 1 ATOM 3439 N N . VAL A 1 449 ? -49.693 51.301 -3.723 1.00 112.31 ? 449 VAL A N 1 ATOM 3440 C CA . VAL A 1 449 ? -50.555 50.594 -4.664 1.00 102.48 ? 449 VAL A CA 1 ATOM 3441 C C . VAL A 1 449 ? -51.931 51.252 -4.803 1.00 116.09 ? 449 VAL A C 1 ATOM 3442 O O . VAL A 1 449 ? -52.680 51.363 -3.830 1.00 111.15 ? 449 VAL A O 1 ATOM 3443 C CB . VAL A 1 449 ? -50.734 49.124 -4.247 1.00 101.24 ? 449 VAL A CB 1 ATOM 3444 C CG1 . VAL A 1 449 ? -51.775 48.456 -5.109 1.00 114.32 ? 449 VAL A CG1 1 ATOM 3445 C CG2 . VAL A 1 449 ? -49.412 48.383 -4.349 1.00 100.02 ? 449 VAL A CG2 1 ATOM 3446 N N . TYR A 1 450 ? -52.251 51.684 -6.022 1.00 124.22 ? 450 TYR A N 1 ATOM 3447 C CA . TYR A 1 450 ? -53.523 52.338 -6.328 1.00 113.23 ? 450 TYR A CA 1 ATOM 3448 C C . TYR A 1 450 ? -54.484 51.415 -7.068 1.00 112.23 ? 450 TYR A C 1 ATOM 3449 O O . TYR A 1 450 ? -54.269 51.142 -8.243 1.00 109.61 ? 450 TYR A O 1 ATOM 3450 C CB . TYR A 1 450 ? -53.308 53.575 -7.210 1.00 123.26 ? 450 TYR A CB 1 ATOM 3451 C CG . TYR A 1 450 ? -52.597 54.761 -6.594 1.00 116.86 ? 450 TYR A CG 1 ATOM 3452 C CD1 . TYR A 1 450 ? -52.375 54.848 -5.227 1.00 120.86 ? 450 TYR A CD1 1 ATOM 3453 C CD2 . TYR A 1 450 ? -52.166 55.811 -7.397 1.00 119.64 ? 450 TYR A CD2 1 ATOM 3454 C CE1 . TYR A 1 450 ? -51.730 55.949 -4.679 1.00 134.13 ? 450 TYR A CE1 1 ATOM 3455 C CE2 . TYR A 1 450 ? -51.524 56.909 -6.862 1.00 149.13 ? 450 TYR A CE2 1 ATOM 3456 C CZ . TYR A 1 450 ? -51.307 56.976 -5.504 1.00 149.48 ? 450 TYR A CZ 1 ATOM 3457 O OH . TYR A 1 450 ? -50.665 58.076 -4.974 1.00 126.51 ? 450 TYR A OH 1 ATOM 3458 N N . PRO A 1 451 ? -55.559 50.951 -6.408 1.00 120.80 ? 451 PRO A N 1 ATOM 3459 C CA . PRO A 1 451 ? -55.850 51.040 -4.977 1.00 125.08 ? 451 PRO A CA 1 ATOM 3460 C C . PRO A 1 451 ? -55.371 49.795 -4.240 1.00 117.42 ? 451 PRO A C 1 ATOM 3461 O O . PRO A 1 451 ? -54.887 48.863 -4.880 1.00 99.24 ? 451 PRO A O 1 ATOM 3462 C CB . PRO A 1 451 ? -57.371 51.142 -4.947 1.00 113.61 ? 451 PRO A CB 1 ATOM 3463 C CG . PRO A 1 451 ? -57.793 50.294 -6.103 1.00 101.24 ? 451 PRO A CG 1 ATOM 3464 C CD . PRO A 1 451 ? -56.710 50.410 -7.155 1.00 102.28 ? 451 PRO A CD 1 ATOM 3465 N N . SER A 1 452 ? -55.538 49.763 -2.922 1.00 124.17 ? 452 SER A N 1 ATOM 3466 C CA . SER A 1 452 ? -55.066 48.637 -2.125 1.00 117.97 ? 452 SER A CA 1 ATOM 3467 C C . SER A 1 452 ? -56.003 47.434 -2.229 1.00 119.62 ? 452 SER A C 1 ATOM 3468 O O . SER A 1 452 ? -55.604 46.302 -1.962 1.00 107.90 ? 452 SER A O 1 ATOM 3469 C CB . SER A 1 452 ? -54.897 49.055 -0.661 1.00 109.06 ? 452 SER A CB 1 ATOM 3470 O OG . SER A 1 452 ? -56.007 49.813 -0.209 1.00 105.56 ? 452 SER A OG 1 ATOM 3471 N N . ILE A 1 453 ? -57.247 47.683 -2.624 1.00 123.17 ? 453 ILE A N 1 ATOM 3472 C CA . ILE A 1 453 ? -58.242 46.620 -2.724 1.00 116.52 ? 453 ILE A CA 1 ATOM 3473 C C . ILE A 1 453 ? -58.721 46.454 -4.165 1.00 111.96 ? 453 ILE A C 1 ATOM 3474 O O . ILE A 1 453 ? -59.024 47.435 -4.841 1.00 134.20 ? 453 ILE A O 1 ATOM 3475 C CB . ILE A 1 453 ? -59.448 46.897 -1.809 1.00 108.75 ? 453 ILE A CB 1 ATOM 3476 C CG1 . ILE A 1 453 ? -58.976 47.188 -0.383 1.00 110.60 ? 453 ILE A CG1 1 ATOM 3477 C CG2 . ILE A 1 453 ? -60.415 45.727 -1.826 1.00 104.36 ? 453 ILE A CG2 1 ATOM 3478 C CD1 . ILE A 1 453 ? -60.047 47.779 0.503 1.00 130.01 ? 453 ILE A CD1 1 ATOM 3479 N N . LEU A 1 454 ? -58.792 45.210 -4.628 1.00 98.15 ? 454 LEU A N 1 ATOM 3480 C CA . LEU A 1 454 ? -59.111 44.934 -6.026 1.00 101.53 ? 454 LEU A CA 1 ATOM 3481 C C . LEU A 1 454 ? -60.500 44.321 -6.211 1.00 112.27 ? 454 LEU A C 1 ATOM 3482 O O . LEU A 1 454 ? -60.905 43.433 -5.461 1.00 111.58 ? 454 LEU A O 1 ATOM 3483 C CB . LEU A 1 454 ? -58.057 44.004 -6.628 1.00 106.46 ? 454 LEU A CB 1 ATOM 3484 C CG . LEU A 1 454 ? -56.600 44.371 -6.340 1.00 96.35 ? 454 LEU A CG 1 ATOM 3485 C CD1 . LEU A 1 454 ? -55.653 43.404 -7.034 1.00 99.26 ? 454 LEU A CD1 1 ATOM 3486 C CD2 . LEU A 1 454 ? -56.316 45.799 -6.761 1.00 97.07 ? 454 LEU A CD2 1 ATOM 3487 N N . ASN A 1 455 ? -61.218 44.801 -7.223 1.00 116.44 ? 455 ASN A N 1 ATOM 3488 C CA . ASN A 1 455 ? -62.536 44.276 -7.566 1.00 102.88 ? 455 ASN A CA 1 ATOM 3489 C C . ASN A 1 455 ? -62.524 43.673 -8.970 1.00 105.31 ? 455 ASN A C 1 ATOM 3490 O O . ASN A 1 455 ? -62.302 44.376 -9.955 1.00 114.57 ? 455 ASN A O 1 ATOM 3491 C CB . ASN A 1 455 ? -63.592 45.379 -7.464 1.00 104.29 ? 455 ASN A CB 1 ATOM 3492 C CG . ASN A 1 455 ? -65.015 44.852 -7.580 1.00 116.12 ? 455 ASN A CG 1 ATOM 3493 O OD1 . ASN A 1 455 ? -65.273 43.840 -8.232 1.00 115.99 ? 455 ASN A OD1 1 ATOM 3494 N ND2 . ASN A 1 455 ? -65.950 45.548 -6.945 1.00 129.43 ? 455 ASN A ND2 1 ATOM 3495 N N . GLN A 1 456 ? -62.777 42.371 -9.052 1.00 100.07 ? 456 GLN A N 1 ATOM 3496 C CA . GLN A 1 456 ? -62.689 41.642 -10.313 1.00 102.86 ? 456 GLN A CA 1 ATOM 3497 C C . GLN A 1 456 ? -63.814 41.987 -11.289 1.00 111.73 ? 456 GLN A C 1 ATOM 3498 O O . GLN A 1 456 ? -63.691 41.755 -12.490 1.00 114.56 ? 456 GLN A O 1 ATOM 3499 C CB . GLN A 1 456 ? -62.692 40.139 -10.041 1.00 116.06 ? 456 GLN A CB 1 ATOM 3500 C CG . GLN A 1 456 ? -61.595 39.680 -9.102 1.00 102.11 ? 456 GLN A CG 1 ATOM 3501 C CD . GLN A 1 456 ? -61.830 38.274 -8.590 1.00 104.24 ? 456 GLN A CD 1 ATOM 3502 O OE1 . GLN A 1 456 ? -62.819 38.007 -7.910 1.00 107.05 ? 456 GLN A OE1 1 ATOM 3503 N NE2 . GLN A 1 456 ? -60.922 37.366 -8.919 1.00 108.54 ? 456 GLN A NE2 1 ATOM 3504 N N . ASP A 1 457 ? -64.909 42.529 -10.767 1.00 112.59 ? 457 ASP A N 1 ATOM 3505 C CA . ASP A 1 457 ? -66.059 42.894 -11.590 1.00 117.33 ? 457 ASP A CA 1 ATOM 3506 C C . ASP A 1 457 ? -65.931 44.342 -12.054 1.00 131.90 ? 457 ASP A C 1 ATOM 3507 O O . ASP A 1 457 ? -66.740 44.845 -12.833 1.00 137.31 ? 457 ASP A O 1 ATOM 3508 C CB . ASP A 1 457 ? -67.356 42.687 -10.804 1.00 129.62 ? 457 ASP A CB 1 ATOM 3509 C CG . ASP A 1 457 ? -68.593 42.887 -11.651 1.00 128.11 ? 457 ASP A CG 1 ATOM 3510 O OD1 . ASP A 1 457 ? -69.126 44.015 -11.663 1.00 131.42 ? 457 ASP A OD1 1 ATOM 3511 O OD2 . ASP A 1 457 ? -69.031 41.916 -12.302 1.00 136.85 ? 457 ASP A OD2 1 ATOM 3512 N N . ASN A 1 458 ? -64.880 44.993 -11.572 1.00 138.10 ? 458 ASN A N 1 ATOM 3513 C CA . ASN A 1 458 ? -64.634 46.410 -11.807 1.00 129.23 ? 458 ASN A CA 1 ATOM 3514 C C . ASN A 1 458 ? -63.779 46.666 -13.061 1.00 128.61 ? 458 ASN A C 1 ATOM 3515 O O . ASN A 1 458 ? -63.290 47.776 -13.268 1.00 143.73 ? 458 ASN A O 1 ATOM 3516 C CB . ASN A 1 458 ? -63.996 47.044 -10.563 1.00 129.23 ? 458 ASN A CB 1 ATOM 3517 C CG . ASN A 1 458 ? -63.801 48.536 -10.709 1.00 139.82 ? 458 ASN A CG 1 ATOM 3518 O OD1 . ASN A 1 458 ? -64.640 49.231 -11.280 1.00 148.49 ? 458 ASN A OD1 1 ATOM 3519 N ND2 . ASN A 1 458 ? -62.684 49.033 -10.212 1.00 161.03 ? 458 ASN A ND2 1 ATOM 3520 N N . LYS A 1 459 ? -63.591 45.635 -13.885 1.00 126.42 ? 459 LYS A N 1 ATOM 3521 C CA . LYS A 1 459 ? -62.630 45.680 -14.994 1.00 131.14 ? 459 LYS A CA 1 ATOM 3522 C C . LYS A 1 459 ? -62.718 46.959 -15.825 1.00 139.27 ? 459 LYS A C 1 ATOM 3523 O O . LYS A 1 459 ? -63.794 47.348 -16.280 1.00 150.12 ? 459 LYS A O 1 ATOM 3524 C CB . LYS A 1 459 ? -62.846 44.487 -15.928 1.00 124.19 ? 459 LYS A CB 1 ATOM 3525 C CG . LYS A 1 459 ? -63.020 43.147 -15.245 1.00 123.27 ? 459 LYS A CG 1 ATOM 3526 C CD . LYS A 1 459 ? -63.512 42.103 -16.238 1.00 122.52 ? 459 LYS A CD 1 ATOM 3527 C CE . LYS A 1 459 ? -63.630 40.733 -15.596 1.00 135.35 ? 459 LYS A CE 1 ATOM 3528 N NZ . LYS A 1 459 ? -64.266 39.743 -16.511 1.00 142.96 ? 459 LYS A NZ 1 ATOM 3529 N N . THR A 1 460 ? -61.569 47.601 -16.024 1.00 140.54 ? 460 THR A N 1 ATOM 3530 C CA . THR A 1 460 ? -61.517 48.921 -16.645 1.00 134.03 ? 460 THR A CA 1 ATOM 3531 C C . THR A 1 460 ? -60.536 48.990 -17.810 1.00 126.38 ? 460 THR A C 1 ATOM 3532 O O . THR A 1 460 ? -60.937 49.172 -18.960 1.00 152.07 ? 460 THR A O 1 ATOM 3533 C CB . THR A 1 460 ? -61.126 50.006 -15.618 1.00 123.44 ? 460 THR A CB 1 ATOM 3534 O OG1 . THR A 1 460 ? -62.102 50.053 -14.570 1.00 133.46 ? 460 THR A OG1 1 ATOM 3535 C CG2 . THR A 1 460 ? -61.044 51.369 -16.286 1.00 124.49 ? 460 THR A CG2 1 ATOM 3536 N N . CYS A 1 461 ? -59.250 48.848 -17.505 1.00 118.85 ? 461 CYS A N 1 ATOM 3537 C CA . CYS A 1 461 ? -58.198 49.022 -18.502 1.00 125.95 ? 461 CYS A CA 1 ATOM 3538 C C . CYS A 1 461 ? -58.244 47.959 -19.594 1.00 117.28 ? 461 CYS A C 1 ATOM 3539 O O . CYS A 1 461 ? -58.555 46.798 -19.335 1.00 116.42 ? 461 CYS A O 1 ATOM 3540 C CB . CYS A 1 461 ? -56.822 49.010 -17.834 1.00 128.38 ? 461 CYS A CB 1 ATOM 3541 S SG . CYS A 1 461 ? -55.441 49.278 -18.967 1.00 213.44 ? 461 CYS A SG 1 ATOM 3542 N N . SER A 1 462 ? -57.920 48.369 -20.816 1.00 120.67 ? 462 SER A N 1 ATOM 3543 C CA . SER A 1 462 ? -57.914 47.460 -21.953 1.00 133.03 ? 462 SER A CA 1 ATOM 3544 C C . SER A 1 462 ? -56.530 46.854 -22.173 1.00 139.19 ? 462 SER A C 1 ATOM 3545 O O . SER A 1 462 ? -55.517 47.554 -22.117 1.00 146.02 ? 462 SER A O 1 ATOM 3546 C CB . SER A 1 462 ? -58.381 48.185 -23.219 1.00 149.56 ? 462 SER A CB 1 ATOM 3547 O OG . SER A 1 462 ? -58.527 47.285 -24.304 1.00 160.71 ? 462 SER A OG 1 ATOM 3548 N N . LEU A 1 463 ? -56.500 45.547 -22.417 1.00 133.83 ? 463 LEU A N 1 ATOM 3549 C CA . LEU A 1 463 ? -55.260 44.831 -22.694 1.00 139.62 ? 463 LEU A CA 1 ATOM 3550 C C . LEU A 1 463 ? -54.647 45.325 -24.007 1.00 164.08 ? 463 LEU A C 1 ATOM 3551 O O . LEU A 1 463 ? -55.370 45.601 -24.963 1.00 181.71 ? 463 LEU A O 1 ATOM 3552 C CB . LEU A 1 463 ? -55.530 43.324 -22.743 1.00 139.72 ? 463 LEU A CB 1 ATOM 3553 C CG . LEU A 1 463 ? -54.376 42.345 -22.517 1.00 140.27 ? 463 LEU A CG 1 ATOM 3554 C CD1 . LEU A 1 463 ? -54.870 41.107 -21.785 1.00 134.67 ? 463 LEU A CD1 1 ATOM 3555 C CD2 . LEU A 1 463 ? -53.737 41.960 -23.839 1.00 144.40 ? 463 LEU A CD2 1 ATOM 3556 N N . PRO A 1 464 ? -53.311 45.465 -24.051 1.00 164.63 ? 464 PRO A N 1 ATOM 3557 C CA . PRO A 1 464 ? -52.641 45.993 -25.247 1.00 171.62 ? 464 PRO A CA 1 ATOM 3558 C C . PRO A 1 464 ? -52.831 45.149 -26.511 1.00 179.65 ? 464 PRO A C 1 ATOM 3559 O O . PRO A 1 464 ? -53.146 45.703 -27.566 1.00 183.44 ? 464 PRO A O 1 ATOM 3560 C CB . PRO A 1 464 ? -51.161 46.014 -24.837 1.00 166.85 ? 464 PRO A CB 1 ATOM 3561 C CG . PRO A 1 464 ? -51.060 45.060 -23.691 1.00 161.43 ? 464 PRO A CG 1 ATOM 3562 C CD . PRO A 1 464 ? -52.356 45.198 -22.963 1.00 159.59 ? 464 PRO A CD 1 ATOM 3563 N N . GLY A 1 465 ? -52.650 43.836 -26.405 1.00 171.11 ? 465 GLY A N 1 ATOM 3564 C CA . GLY A 1 465 ? -52.724 42.966 -27.566 1.00 171.86 ? 465 GLY A CA 1 ATOM 3565 C C . GLY A 1 465 ? -54.114 42.874 -28.166 1.00 175.33 ? 465 GLY A C 1 ATOM 3566 O O . GLY A 1 465 ? -54.314 43.155 -29.348 1.00 182.28 ? 465 GLY A O 1 ATOM 3567 N N . THR A 1 466 ? -55.078 42.483 -27.339 1.00 174.19 ? 466 THR A N 1 ATOM 3568 C CA . THR A 1 466 ? -56.468 42.371 -27.763 1.00 179.16 ? 466 THR A CA 1 ATOM 3569 C C . THR A 1 466 ? -57.333 43.282 -26.909 1.00 169.98 ? 466 THR A C 1 ATOM 3570 O O . THR A 1 466 ? -56.964 43.611 -25.784 1.00 154.37 ? 466 THR A O 1 ATOM 3571 C CB . THR A 1 466 ? -56.981 40.925 -27.654 1.00 182.23 ? 466 THR A CB 1 ATOM 3572 O OG1 . THR A 1 466 ? -58.386 40.892 -27.937 1.00 183.06 ? 466 THR A OG1 1 ATOM 3573 C CG2 . THR A 1 466 ? -56.740 40.380 -26.253 1.00 163.83 ? 466 THR A CG2 1 ATOM 3574 N N . ALA A 1 467 ? -58.498 43.669 -27.418 1.00 175.92 ? 467 ALA A N 1 ATOM 3575 C CA . ALA A 1 467 ? -59.319 44.617 -26.682 1.00 166.31 ? 467 ALA A CA 1 ATOM 3576 C C . ALA A 1 467 ? -60.295 43.889 -25.768 1.00 154.50 ? 467 ALA A C 1 ATOM 3577 O O . ALA A 1 467 ? -61.278 43.294 -26.216 1.00 132.90 ? 467 ALA A O 1 ATOM 3578 C CB . ALA A 1 467 ? -60.066 45.532 -27.642 1.00 168.71 ? 467 ALA A CB 1 ATOM 3579 N N . LEU A 1 468 ? -60.002 43.965 -24.475 1.00 158.59 ? 468 LEU A N 1 ATOM 3580 C CA . LEU A 1 468 ? -60.837 43.417 -23.416 1.00 152.48 ? 468 LEU A CA 1 ATOM 3581 C C . LEU A 1 468 ? -60.608 44.256 -22.168 1.00 144.03 ? 468 LEU A C 1 ATOM 3582 O O . LEU A 1 468 ? -59.487 44.691 -21.913 1.00 146.37 ? 468 LEU A O 1 ATOM 3583 C CB . LEU A 1 468 ? -60.506 41.946 -23.143 1.00 148.01 ? 468 LEU A CB 1 ATOM 3584 C CG . LEU A 1 468 ? -60.966 40.888 -24.149 1.00 136.68 ? 468 LEU A CG 1 ATOM 3585 C CD1 . LEU A 1 468 ? -60.495 39.501 -23.734 1.00 126.76 ? 468 LEU A CD1 1 ATOM 3586 C CD2 . LEU A 1 468 ? -62.477 40.921 -24.298 1.00 142.96 ? 468 LEU A CD2 1 ATOM 3587 N N . LYS A 1 469 ? -61.656 44.480 -21.386 1.00 144.30 ? 469 LYS A N 1 ATOM 3588 C CA . LYS A 1 469 ? -61.516 45.271 -20.170 1.00 142.46 ? 469 LYS A CA 1 ATOM 3589 C C . LYS A 1 469 ? -61.111 44.382 -18.998 1.00 139.19 ? 469 LYS A C 1 ATOM 3590 O O . LYS A 1 469 ? -61.731 43.351 -18.737 1.00 134.99 ? 469 LYS A O 1 ATOM 3591 C CB . LYS A 1 469 ? -62.809 46.026 -19.867 1.00 150.25 ? 469 LYS A CB 1 ATOM 3592 C CG . LYS A 1 469 ? -63.119 47.107 -20.891 1.00 163.45 ? 469 LYS A CG 1 ATOM 3593 C CD . LYS A 1 469 ? -64.471 47.751 -20.645 1.00 176.03 ? 469 LYS A CD 1 ATOM 3594 C CE . LYS A 1 469 ? -64.791 48.767 -21.730 1.00 183.55 ? 469 LYS A CE 1 ATOM 3595 N NZ . LYS A 1 469 ? -66.150 49.351 -21.562 1.00 187.72 ? 469 LYS A NZ 1 ATOM 3596 N N . VAL A 1 470 ? -60.053 44.789 -18.306 1.00 143.25 ? 470 VAL A N 1 ATOM 3597 C CA . VAL A 1 470 ? -59.463 43.985 -17.244 1.00 131.31 ? 470 VAL A CA 1 ATOM 3598 C C . VAL A 1 470 ? -59.383 44.783 -15.945 1.00 126.31 ? 470 VAL A C 1 ATOM 3599 O O . VAL A 1 470 ? -59.152 45.992 -15.969 1.00 126.22 ? 470 VAL A O 1 ATOM 3600 C CB . VAL A 1 470 ? -58.050 43.499 -17.635 1.00 125.08 ? 470 VAL A CB 1 ATOM 3601 C CG1 . VAL A 1 470 ? -57.546 42.473 -16.646 1.00 120.98 ? 470 VAL A CG1 1 ATOM 3602 C CG2 . VAL A 1 470 ? -58.055 42.915 -19.040 1.00 132.44 ? 470 VAL A CG2 1 ATOM 3603 N N . SER A 1 471 ? -59.584 44.110 -14.815 1.00 121.14 ? 471 SER A N 1 ATOM 3604 C CA . SER A 1 471 ? -59.446 44.758 -13.515 1.00 119.84 ? 471 SER A CA 1 ATOM 3605 C C . SER A 1 471 ? -57.984 45.091 -13.256 1.00 121.43 ? 471 SER A C 1 ATOM 3606 O O . SER A 1 471 ? -57.117 44.220 -13.304 1.00 127.85 ? 471 SER A O 1 ATOM 3607 C CB . SER A 1 471 ? -59.993 43.869 -12.399 1.00 109.25 ? 471 SER A CB 1 ATOM 3608 O OG . SER A 1 471 ? -59.764 44.461 -11.131 1.00 105.84 ? 471 SER A OG 1 ATOM 3609 N N . CYS A 1 472 ? -57.712 46.357 -12.977 1.00 115.79 ? 472 CYS A N 1 ATOM 3610 C CA . CYS A 1 472 ? -56.336 46.811 -12.872 1.00 121.21 ? 472 CYS A CA 1 ATOM 3611 C C . CYS A 1 472 ? -56.111 47.692 -11.657 1.00 116.00 ? 472 CYS A C 1 ATOM 3612 O O . CYS A 1 472 ? -57.053 48.212 -11.062 1.00 125.80 ? 472 CYS A O 1 ATOM 3613 C CB . CYS A 1 472 ? -55.933 47.573 -14.136 1.00 125.29 ? 472 CYS A CB 1 ATOM 3614 S SG . CYS A 1 472 ? -56.864 49.102 -14.392 1.00 143.84 ? 472 CYS A SG 1 ATOM 3615 N N . PHE A 1 473 ? -54.846 47.850 -11.294 1.00 111.71 ? 473 PHE A N 1 ATOM 3616 C CA . PHE A 1 473 ? -54.468 48.790 -10.255 1.00 113.04 ? 473 PHE A CA 1 ATOM 3617 C C . PHE A 1 473 ? -53.136 49.426 -10.625 1.00 111.59 ? 473 PHE A C 1 ATOM 3618 O O . PHE A 1 473 ? -52.583 49.138 -11.685 1.00 103.82 ? 473 PHE A O 1 ATOM 3619 C CB . PHE A 1 473 ? -54.414 48.113 -8.876 1.00 110.58 ? 473 PHE A CB 1 ATOM 3620 C CG . PHE A 1 473 ? -53.537 46.888 -8.807 1.00 105.50 ? 473 PHE A CG 1 ATOM 3621 C CD1 . PHE A 1 473 ? -53.941 45.688 -9.374 1.00 110.01 ? 473 PHE A CD1 1 ATOM 3622 C CD2 . PHE A 1 473 ? -52.336 46.923 -8.122 1.00 97.63 ? 473 PHE A CD2 1 ATOM 3623 C CE1 . PHE A 1 473 ? -53.144 44.561 -9.291 1.00 108.82 ? 473 PHE A CE1 1 ATOM 3624 C CE2 . PHE A 1 473 ? -51.536 45.798 -8.029 1.00 100.95 ? 473 PHE A CE2 1 ATOM 3625 C CZ . PHE A 1 473 ? -51.941 44.616 -8.616 1.00 109.52 ? 473 PHE A CZ 1 ATOM 3626 N N . ASN A 1 474 ? -52.641 50.321 -9.777 1.00 116.86 ? 474 ASN A N 1 ATOM 3627 C CA . ASN A 1 474 ? -51.377 50.992 -10.050 1.00 116.31 ? 474 ASN A CA 1 ATOM 3628 C C . ASN A 1 474 ? -50.349 50.696 -8.972 1.00 110.86 ? 474 ASN A C 1 ATOM 3629 O O . ASN A 1 474 ? -50.697 50.516 -7.807 1.00 112.22 ? 474 ASN A O 1 ATOM 3630 C CB . ASN A 1 474 ? -51.577 52.505 -10.173 1.00 124.90 ? 474 ASN A CB 1 ATOM 3631 C CG . ASN A 1 474 ? -52.636 52.877 -11.194 1.00 151.58 ? 474 ASN A CG 1 ATOM 3632 O OD1 . ASN A 1 474 ? -53.016 52.069 -12.041 1.00 162.06 ? 474 ASN A OD1 1 ATOM 3633 N ND2 . ASN A 1 474 ? -53.115 54.113 -11.121 1.00 161.05 ? 474 ASN A ND2 1 ATOM 3634 N N . VAL A 1 475 ? -49.083 50.632 -9.365 1.00 104.12 ? 475 VAL A N 1 ATOM 3635 C CA . VAL A 1 475 ? -48.005 50.489 -8.397 1.00 104.36 ? 475 VAL A CA 1 ATOM 3636 C C . VAL A 1 475 ? -46.937 51.553 -8.637 1.00 107.61 ? 475 VAL A C 1 ATOM 3637 O O . VAL A 1 475 ? -46.294 51.586 -9.688 1.00 109.99 ? 475 VAL A O 1 ATOM 3638 C CB . VAL A 1 475 ? -47.377 49.075 -8.442 1.00 104.45 ? 475 VAL A CB 1 ATOM 3639 C CG1 . VAL A 1 475 ? -47.271 48.566 -9.870 1.00 105.30 ? 475 VAL A CG1 1 ATOM 3640 C CG2 . VAL A 1 475 ? -46.021 49.067 -7.751 1.00 105.86 ? 475 VAL A CG2 1 ATOM 3641 N N . ARG A 1 476 ? -46.774 52.438 -7.658 1.00 115.07 ? 476 ARG A N 1 ATOM 3642 C CA . ARG A 1 476 ? -45.761 53.484 -7.723 1.00 117.45 ? 476 ARG A CA 1 ATOM 3643 C C . ARG A 1 476 ? -44.601 53.160 -6.795 1.00 111.18 ? 476 ARG A C 1 ATOM 3644 O O . ARG A 1 476 ? -44.792 52.934 -5.599 1.00 104.19 ? 476 ARG A O 1 ATOM 3645 C CB . ARG A 1 476 ? -46.358 54.845 -7.359 1.00 129.99 ? 476 ARG A CB 1 ATOM 3646 C CG . ARG A 1 476 ? -47.401 55.344 -8.341 1.00 150.06 ? 476 ARG A CG 1 ATOM 3647 C CD . ARG A 1 476 ? -48.053 56.641 -7.883 1.00 144.98 ? 476 ARG A CD 1 ATOM 3648 N NE . ARG A 1 476 ? -47.095 57.733 -7.740 1.00 144.36 ? 476 ARG A NE 1 ATOM 3649 C CZ . ARG A 1 476 ? -46.615 58.158 -6.576 1.00 141.94 ? 476 ARG A CZ 1 ATOM 3650 N NH1 . ARG A 1 476 ? -47.005 57.583 -5.447 1.00 128.95 ? 476 ARG A NH1 1 ATOM 3651 N NH2 . ARG A 1 476 ? -45.747 59.161 -6.540 1.00 142.35 ? 476 ARG A NH2 1 ATOM 3652 N N . PHE A 1 477 ? -43.397 53.134 -7.353 1.00 113.73 ? 477 PHE A N 1 ATOM 3653 C CA . PHE A 1 477 ? -42.205 52.894 -6.555 1.00 113.24 ? 477 PHE A CA 1 ATOM 3654 C C . PHE A 1 477 ? -41.313 54.132 -6.557 1.00 111.43 ? 477 PHE A C 1 ATOM 3655 O O . PHE A 1 477 ? -40.793 54.542 -7.594 1.00 115.11 ? 477 PHE A O 1 ATOM 3656 C CB . PHE A 1 477 ? -41.449 51.659 -7.062 1.00 105.77 ? 477 PHE A CB 1 ATOM 3657 C CG . PHE A 1 477 ? -41.044 51.729 -8.509 1.00 105.16 ? 477 PHE A CG 1 ATOM 3658 C CD1 . PHE A 1 477 ? -41.967 51.496 -9.515 1.00 107.77 ? 477 PHE A CD1 1 ATOM 3659 C CD2 . PHE A 1 477 ? -39.731 51.998 -8.860 1.00 120.60 ? 477 PHE A CD2 1 ATOM 3660 C CE1 . PHE A 1 477 ? -41.593 51.554 -10.843 1.00 130.81 ? 477 PHE A CE1 1 ATOM 3661 C CE2 . PHE A 1 477 ? -39.351 52.057 -10.187 1.00 135.37 ? 477 PHE A CE2 1 ATOM 3662 C CZ . PHE A 1 477 ? -40.283 51.833 -11.179 1.00 141.70 ? 477 PHE A CZ 1 ATOM 3663 N N . CYS A 1 478 ? -41.158 54.737 -5.385 1.00 109.61 ? 478 CYS A N 1 ATOM 3664 C CA . CYS A 1 478 ? -40.367 55.954 -5.258 1.00 122.80 ? 478 CYS A CA 1 ATOM 3665 C C . CYS A 1 478 ? -38.990 55.658 -4.681 1.00 113.30 ? 478 CYS A C 1 ATOM 3666 O O . CYS A 1 478 ? -38.837 54.771 -3.843 1.00 107.99 ? 478 CYS A O 1 ATOM 3667 C CB . CYS A 1 478 ? -41.097 56.982 -4.394 1.00 129.82 ? 478 CYS A CB 1 ATOM 3668 S SG . CYS A 1 478 ? -42.530 57.733 -5.201 1.00 229.83 ? 478 CYS A SG 1 ATOM 3669 N N . LEU A 1 479 ? -37.989 56.400 -5.144 1.00 123.22 ? 479 LEU A N 1 ATOM 3670 C CA . LEU A 1 479 ? -36.609 56.144 -4.748 1.00 129.50 ? 479 LEU A CA 1 ATOM 3671 C C . LEU A 1 479 ? -35.826 57.429 -4.469 1.00 115.25 ? 479 LEU A C 1 ATOM 3672 O O . LEU A 1 479 ? -35.735 58.310 -5.325 1.00 112.11 ? 479 LEU A O 1 ATOM 3673 C CB . LEU A 1 479 ? -35.910 55.327 -5.834 1.00 132.56 ? 479 LEU A CB 1 ATOM 3674 C CG . LEU A 1 479 ? -34.606 54.626 -5.463 1.00 114.71 ? 479 LEU A CG 1 ATOM 3675 C CD1 . LEU A 1 479 ? -34.799 53.780 -4.222 1.00 98.10 ? 479 LEU A CD1 1 ATOM 3676 C CD2 . LEU A 1 479 ? -34.147 53.768 -6.621 1.00 111.54 ? 479 LEU A CD2 1 ATOM 3677 N N . LYS A 1 480 ? -35.256 57.525 -3.271 1.00 119.52 ? 480 LYS A N 1 ATOM 3678 C CA . LYS A 1 480 ? -34.441 58.678 -2.892 1.00 134.70 ? 480 LYS A CA 1 ATOM 3679 C C . LYS A 1 480 ? -33.238 58.254 -2.054 1.00 125.47 ? 480 LYS A C 1 ATOM 3680 O O . LYS A 1 480 ? -33.372 57.455 -1.127 1.00 133.17 ? 480 LYS A O 1 ATOM 3681 C CB . LYS A 1 480 ? -35.279 59.696 -2.119 1.00 138.33 ? 480 LYS A CB 1 ATOM 3682 C CG . LYS A 1 480 ? -34.523 60.949 -1.712 1.00 149.85 ? 480 LYS A CG 1 ATOM 3683 C CD . LYS A 1 480 ? -35.293 61.728 -0.661 1.00 163.93 ? 480 LYS A CD 1 ATOM 3684 C CE . LYS A 1 480 ? -35.523 60.880 0.580 1.00 151.39 ? 480 LYS A CE 1 ATOM 3685 N NZ . LYS A 1 480 ? -36.304 61.595 1.627 1.00 154.36 ? 480 LYS A NZ 1 ATOM 3686 N N . ALA A 1 481 ? -32.067 58.793 -2.378 1.00 115.12 ? 481 ALA A N 1 ATOM 3687 C CA . ALA A 1 481 ? -30.842 58.443 -1.664 1.00 114.81 ? 481 ALA A CA 1 ATOM 3688 C C . ALA A 1 481 ? -29.863 59.607 -1.586 1.00 107.51 ? 481 ALA A C 1 ATOM 3689 O O . ALA A 1 481 ? -29.680 60.333 -2.558 1.00 118.70 ? 481 ALA A O 1 ATOM 3690 C CB . ALA A 1 481 ? -30.176 57.256 -2.331 1.00 140.94 ? 481 ALA A CB 1 ATOM 3691 N N . ASP A 1 482 ? -29.215 59.764 -0.436 1.00 122.98 ? 482 ASP A N 1 ATOM 3692 C CA . ASP A 1 482 ? -28.174 60.776 -0.277 1.00 131.55 ? 482 ASP A CA 1 ATOM 3693 C C . ASP A 1 482 ? -27.127 60.308 0.733 1.00 131.70 ? 482 ASP A C 1 ATOM 3694 O O . ASP A 1 482 ? -27.256 59.230 1.316 1.00 133.98 ? 482 ASP A O 1 ATOM 3695 C CB . ASP A 1 482 ? -28.782 62.114 0.157 1.00 133.88 ? 482 ASP A CB 1 ATOM 3696 C CG . ASP A 1 482 ? -27.866 63.294 -0.126 1.00 154.82 ? 482 ASP A CG 1 ATOM 3697 O OD1 . ASP A 1 482 ? -27.051 63.202 -1.069 1.00 152.46 ? 482 ASP A OD1 1 ATOM 3698 O OD2 . ASP A 1 482 ? -27.960 64.311 0.595 1.00 157.90 ? 482 ASP A OD2 1 ATOM 3699 N N . GLY A 1 483 ? -26.094 61.120 0.938 1.00 130.03 ? 483 GLY A N 1 ATOM 3700 C CA . GLY A 1 483 ? -25.023 60.781 1.859 1.00 118.64 ? 483 GLY A CA 1 ATOM 3701 C C . GLY A 1 483 ? -23.997 61.890 1.982 1.00 109.32 ? 483 GLY A C 1 ATOM 3702 O O . GLY A 1 483 ? -23.928 62.780 1.134 1.00 116.88 ? 483 GLY A O 1 ATOM 3703 N N . LYS A 1 484 ? -23.195 61.837 3.040 1.00 113.41 ? 484 LYS A N 1 ATOM 3704 C CA . LYS A 1 484 ? -22.196 62.871 3.289 1.00 110.49 ? 484 LYS A CA 1 ATOM 3705 C C . LYS A 1 484 ? -20.913 62.629 2.499 1.00 110.88 ? 484 LYS A C 1 ATOM 3706 O O . LYS A 1 484 ? -20.775 61.619 1.808 1.00 94.29 ? 484 LYS A O 1 ATOM 3707 C CB . LYS A 1 484 ? -21.875 62.949 4.783 1.00 97.88 ? 484 LYS A CB 1 ATOM 3708 C CG . LYS A 1 484 ? -23.082 63.209 5.668 1.00 114.50 ? 484 LYS A CG 1 ATOM 3709 C CD . LYS A 1 484 ? -22.678 63.322 7.127 1.00 125.00 ? 484 LYS A CD 1 ATOM 3710 C CE . LYS A 1 484 ? -23.882 63.586 8.013 1.00 130.50 ? 484 LYS A CE 1 ATOM 3711 N NZ . LYS A 1 484 ? -23.492 63.733 9.442 1.00 146.97 ? 484 LYS A NZ 1 ATOM 3712 N N . GLY A 1 485 ? -19.971 63.560 2.620 1.00 123.97 ? 485 GLY A N 1 ATOM 3713 C CA . GLY A 1 485 ? -18.672 63.435 1.985 1.00 120.44 ? 485 GLY A CA 1 ATOM 3714 C C . GLY A 1 485 ? -18.695 63.486 0.469 1.00 116.61 ? 485 GLY A C 1 ATOM 3715 O O . GLY A 1 485 ? -19.674 63.920 -0.138 1.00 126.09 ? 485 GLY A O 1 ATOM 3716 N N . VAL A 1 486 ? -17.601 63.038 -0.140 1.00 105.27 ? 486 VAL A N 1 ATOM 3717 C CA . VAL A 1 486 ? -17.476 63.020 -1.592 1.00 111.43 ? 486 VAL A CA 1 ATOM 3718 C C . VAL A 1 486 ? -18.163 61.800 -2.193 1.00 134.17 ? 486 VAL A C 1 ATOM 3719 O O . VAL A 1 486 ? -17.962 60.671 -1.743 1.00 132.91 ? 486 VAL A O 1 ATOM 3720 C CB . VAL A 1 486 ? -15.999 63.042 -2.029 1.00 109.34 ? 486 VAL A CB 1 ATOM 3721 C CG1 . VAL A 1 486 ? -15.875 62.814 -3.529 1.00 116.73 ? 486 VAL A CG1 1 ATOM 3722 C CG2 . VAL A 1 486 ? -15.359 64.357 -1.637 1.00 109.02 ? 486 VAL A CG2 1 ATOM 3723 N N . LEU A 1 487 ? -18.952 62.050 -3.233 1.00 146.09 ? 487 LEU A N 1 ATOM 3724 C CA . LEU A 1 487 ? -19.739 61.031 -3.916 1.00 137.10 ? 487 LEU A CA 1 ATOM 3725 C C . LEU A 1 487 ? -20.406 61.705 -5.107 1.00 144.14 ? 487 LEU A C 1 ATOM 3726 O O . LEU A 1 487 ? -20.579 62.923 -5.103 1.00 150.93 ? 487 LEU A O 1 ATOM 3727 C CB . LEU A 1 487 ? -20.774 60.399 -2.973 1.00 117.41 ? 487 LEU A CB 1 ATOM 3728 C CG . LEU A 1 487 ? -21.680 61.294 -2.120 1.00 122.03 ? 487 LEU A CG 1 ATOM 3729 C CD1 . LEU A 1 487 ? -22.884 61.801 -2.902 1.00 130.44 ? 487 LEU A CD1 1 ATOM 3730 C CD2 . LEU A 1 487 ? -22.131 60.542 -0.880 1.00 120.01 ? 487 LEU A CD2 1 ATOM 3731 N N . PRO A 1 488 ? -20.774 60.925 -6.136 1.00 152.80 ? 488 PRO A N 1 ATOM 3732 C CA . PRO A 1 488 ? -21.291 61.552 -7.359 1.00 150.03 ? 488 PRO A CA 1 ATOM 3733 C C . PRO A 1 488 ? -22.597 62.318 -7.149 1.00 149.26 ? 488 PRO A C 1 ATOM 3734 O O . PRO A 1 488 ? -23.165 62.306 -6.058 1.00 147.43 ? 488 PRO A O 1 ATOM 3735 C CB . PRO A 1 488 ? -21.515 60.359 -8.295 1.00 151.50 ? 488 PRO A CB 1 ATOM 3736 C CG . PRO A 1 488 ? -20.603 59.295 -7.782 1.00 147.67 ? 488 PRO A CG 1 ATOM 3737 C CD . PRO A 1 488 ? -20.587 59.472 -6.297 1.00 146.67 ? 488 PRO A CD 1 ATOM 3738 N N . ARG A 1 489 ? -23.068 62.969 -8.206 1.00 140.68 ? 489 ARG A N 1 ATOM 3739 C CA . ARG A 1 489 ? -24.293 63.751 -8.137 1.00 138.27 ? 489 ARG A CA 1 ATOM 3740 C C . ARG A 1 489 ? -25.494 62.860 -8.414 1.00 143.97 ? 489 ARG A C 1 ATOM 3741 O O . ARG A 1 489 ? -26.347 62.659 -7.550 1.00 149.41 ? 489 ARG A O 1 ATOM 3742 C CB . ARG A 1 489 ? -24.244 64.913 -9.128 1.00 146.28 ? 489 ARG A CB 1 ATOM 3743 C CG . ARG A 1 489 ? -23.067 65.853 -8.917 1.00 151.99 ? 489 ARG A CG 1 ATOM 3744 C CD . ARG A 1 489 ? -23.042 66.944 -9.973 1.00 168.48 ? 489 ARG A CD 1 ATOM 3745 N NE . ARG A 1 489 ? -24.295 67.692 -10.005 1.00 182.09 ? 489 ARG A NE 1 ATOM 3746 C CZ . ARG A 1 489 ? -24.584 68.630 -10.900 1.00 193.47 ? 489 ARG A CZ 1 ATOM 3747 N NH1 . ARG A 1 489 ? -23.707 68.939 -11.846 1.00 203.30 ? 489 ARG A NH1 1 ATOM 3748 N NH2 . ARG A 1 489 ? -25.751 69.258 -10.852 1.00 185.05 ? 489 ARG A NH2 1 ATOM 3749 N N . LYS A 1 490 ? -25.552 62.330 -9.631 1.00 158.22 ? 490 LYS A N 1 ATOM 3750 C CA . LYS A 1 490 ? -26.588 61.378 -10.006 1.00 163.55 ? 490 LYS A CA 1 ATOM 3751 C C . LYS A 1 490 ? -26.130 59.947 -9.733 1.00 157.96 ? 490 LYS A C 1 ATOM 3752 O O . LYS A 1 490 ? -24.990 59.584 -10.024 1.00 158.17 ? 490 LYS A O 1 ATOM 3753 C CB . LYS A 1 490 ? -26.964 61.544 -11.479 1.00 152.69 ? 490 LYS A CB 1 ATOM 3754 C CG . LYS A 1 490 ? -27.769 62.797 -11.780 1.00 159.73 ? 490 LYS A CG 1 ATOM 3755 C CD . LYS A 1 490 ? -28.003 62.950 -13.274 1.00 174.01 ? 490 LYS A CD 1 ATOM 3756 C CE . LYS A 1 490 ? -29.050 64.012 -13.570 1.00 180.71 ? 490 LYS A CE 1 ATOM 3757 N NZ . LYS A 1 490 ? -30.406 63.602 -13.106 1.00 181.89 ? 490 LYS A NZ 1 ATOM 3758 N N . LEU A 1 491 ? -27.024 59.139 -9.171 1.00 137.80 ? 491 LEU A N 1 ATOM 3759 C CA . LEU A 1 491 ? -26.705 57.755 -8.843 1.00 130.79 ? 491 LEU A CA 1 ATOM 3760 C C . LEU A 1 491 ? -27.515 56.777 -9.686 1.00 144.52 ? 491 LEU A C 1 ATOM 3761 O O . LEU A 1 491 ? -28.658 57.055 -10.051 1.00 142.65 ? 491 LEU A O 1 ATOM 3762 C CB . LEU A 1 491 ? -26.951 57.489 -7.358 1.00 124.82 ? 491 LEU A CB 1 ATOM 3763 C CG . LEU A 1 491 ? -26.073 58.264 -6.375 1.00 125.22 ? 491 LEU A CG 1 ATOM 3764 C CD1 . LEU A 1 491 ? -26.544 58.037 -4.948 1.00 120.62 ? 491 LEU A CD1 1 ATOM 3765 C CD2 . LEU A 1 491 ? -24.614 57.861 -6.532 1.00 128.08 ? 491 LEU A CD2 1 ATOM 3766 N N . ASN A 1 492 ? -26.917 55.629 -9.988 1.00 145.79 ? 492 ASN A N 1 ATOM 3767 C CA . ASN A 1 492 ? -27.579 54.610 -10.795 1.00 142.27 ? 492 ASN A CA 1 ATOM 3768 C C . ASN A 1 492 ? -28.125 53.464 -9.954 1.00 147.44 ? 492 ASN A C 1 ATOM 3769 O O . ASN A 1 492 ? -27.366 52.687 -9.375 1.00 153.90 ? 492 ASN A O 1 ATOM 3770 C CB . ASN A 1 492 ? -26.618 54.061 -11.849 1.00 146.21 ? 492 ASN A CB 1 ATOM 3771 C CG . ASN A 1 492 ? -26.285 55.078 -12.917 1.00 159.81 ? 492 ASN A CG 1 ATOM 3772 O OD1 . ASN A 1 492 ? -27.120 55.905 -13.283 1.00 166.98 ? 492 ASN A OD1 1 ATOM 3773 N ND2 . ASN A 1 492 ? -25.060 55.024 -13.424 1.00 169.77 ? 492 ASN A ND2 1 ATOM 3774 N N . PHE A 1 493 ? -29.447 53.364 -9.895 1.00 140.51 ? 493 PHE A N 1 ATOM 3775 C CA . PHE A 1 493 ? -30.097 52.290 -9.158 1.00 131.57 ? 493 PHE A CA 1 ATOM 3776 C C . PHE A 1 493 ? -30.820 51.327 -10.092 1.00 138.38 ? 493 PHE A C 1 ATOM 3777 O O . PHE A 1 493 ? -31.494 51.745 -11.034 1.00 138.60 ? 493 PHE A O 1 ATOM 3778 C CB . PHE A 1 493 ? -31.086 52.856 -8.140 1.00 125.50 ? 493 PHE A CB 1 ATOM 3779 C CG . PHE A 1 493 ? -30.452 53.301 -6.856 1.00 113.46 ? 493 PHE A CG 1 ATOM 3780 C CD1 . PHE A 1 493 ? -30.142 54.633 -6.644 1.00 128.94 ? 493 PHE A CD1 1 ATOM 3781 C CD2 . PHE A 1 493 ? -30.173 52.386 -5.854 1.00 108.80 ? 493 PHE A CD2 1 ATOM 3782 C CE1 . PHE A 1 493 ? -29.562 55.044 -5.459 1.00 131.43 ? 493 PHE A CE1 1 ATOM 3783 C CE2 . PHE A 1 493 ? -29.594 52.790 -4.668 1.00 108.16 ? 493 PHE A CE2 1 ATOM 3784 C CZ . PHE A 1 493 ? -29.288 54.120 -4.470 1.00 121.68 ? 493 PHE A CZ 1 ATOM 3785 N N . GLN A 1 494 ? -30.671 50.035 -9.822 1.00 142.52 ? 494 GLN A N 1 ATOM 3786 C CA . GLN A 1 494 ? -31.389 49.010 -10.564 1.00 138.04 ? 494 GLN A CA 1 ATOM 3787 C C . GLN A 1 494 ? -32.456 48.393 -9.668 1.00 127.51 ? 494 GLN A C 1 ATOM 3788 O O . GLN A 1 494 ? -32.141 47.690 -8.708 1.00 123.08 ? 494 GLN A O 1 ATOM 3789 C CB . GLN A 1 494 ? -30.428 47.937 -11.077 1.00 144.07 ? 494 GLN A CB 1 ATOM 3790 C CG . GLN A 1 494 ? -30.983 47.106 -12.219 1.00 156.38 ? 494 GLN A CG 1 ATOM 3791 C CD . GLN A 1 494 ? -31.176 47.917 -13.487 1.00 165.65 ? 494 GLN A CD 1 ATOM 3792 O OE1 . GLN A 1 494 ? -32.109 47.678 -14.254 1.00 172.70 ? 494 GLN A OE1 1 ATOM 3793 N NE2 . GLN A 1 494 ? -30.288 48.878 -13.718 1.00 161.14 ? 494 GLN A NE2 1 ATOM 3794 N N . VAL A 1 495 ? -33.718 48.662 -9.984 1.00 131.47 ? 495 VAL A N 1 ATOM 3795 C CA . VAL A 1 495 ? -34.824 48.233 -9.135 1.00 138.23 ? 495 VAL A CA 1 ATOM 3796 C C . VAL A 1 495 ? -35.634 47.108 -9.779 1.00 125.49 ? 495 VAL A C 1 ATOM 3797 O O . VAL A 1 495 ? -35.906 47.128 -10.980 1.00 126.63 ? 495 VAL A O 1 ATOM 3798 C CB . VAL A 1 495 ? -35.756 49.423 -8.798 1.00 142.79 ? 495 VAL A CB 1 ATOM 3799 C CG1 . VAL A 1 495 ? -36.197 50.139 -10.067 1.00 150.42 ? 495 VAL A CG1 1 ATOM 3800 C CG2 . VAL A 1 495 ? -36.956 48.965 -7.978 1.00 131.58 ? 495 VAL A CG2 1 ATOM 3801 N N . GLU A 1 496 ? -36.004 46.121 -8.970 1.00 116.69 ? 496 GLU A N 1 ATOM 3802 C CA . GLU A 1 496 ? -36.809 44.998 -9.433 1.00 121.87 ? 496 GLU A CA 1 ATOM 3803 C C . GLU A 1 496 ? -38.190 45.016 -8.783 1.00 108.21 ? 496 GLU A C 1 ATOM 3804 O O . GLU A 1 496 ? -38.318 45.318 -7.596 1.00 102.92 ? 496 GLU A O 1 ATOM 3805 C CB . GLU A 1 496 ? -36.098 43.676 -9.133 1.00 131.94 ? 496 GLU A CB 1 ATOM 3806 C CG . GLU A 1 496 ? -36.829 42.439 -9.629 1.00 136.64 ? 496 GLU A CG 1 ATOM 3807 C CD . GLU A 1 496 ? -36.816 42.319 -11.140 1.00 149.10 ? 496 GLU A CD 1 ATOM 3808 O OE1 . GLU A 1 496 ? -37.653 41.568 -11.686 1.00 152.77 ? 496 GLU A OE1 1 ATOM 3809 O OE2 . GLU A 1 496 ? -35.966 42.971 -11.782 1.00 151.21 ? 496 GLU A OE2 1 ATOM 3810 N N . LEU A 1 497 ? -39.220 44.699 -9.563 1.00 101.97 ? 497 LEU A N 1 ATOM 3811 C CA . LEU A 1 497 ? -40.582 44.623 -9.039 1.00 100.37 ? 497 LEU A CA 1 ATOM 3812 C C . LEU A 1 497 ? -41.175 43.225 -9.204 1.00 107.75 ? 497 LEU A C 1 ATOM 3813 O O . LEU A 1 497 ? -41.118 42.638 -10.284 1.00 118.79 ? 497 LEU A O 1 ATOM 3814 C CB . LEU A 1 497 ? -41.479 45.656 -9.724 1.00 101.54 ? 497 LEU A CB 1 ATOM 3815 C CG . LEU A 1 497 ? -41.868 46.872 -8.881 1.00 104.66 ? 497 LEU A CG 1 ATOM 3816 C CD1 . LEU A 1 497 ? -40.634 47.638 -8.435 1.00 109.84 ? 497 LEU A CD1 1 ATOM 3817 C CD2 . LEU A 1 497 ? -42.817 47.779 -9.648 1.00 106.84 ? 497 LEU A CD2 1 ATOM 3818 N N . LEU A 1 498 ? -41.746 42.699 -8.124 1.00 109.79 ? 498 LEU A N 1 ATOM 3819 C CA . LEU A 1 498 ? -42.348 41.369 -8.140 1.00 117.31 ? 498 LEU A CA 1 ATOM 3820 C C . LEU A 1 498 ? -43.789 41.402 -7.645 1.00 109.08 ? 498 LEU A C 1 ATOM 3821 O O . LEU A 1 498 ? -44.072 41.914 -6.562 1.00 107.37 ? 498 LEU A O 1 ATOM 3822 C CB . LEU A 1 498 ? -41.531 40.399 -7.286 1.00 138.39 ? 498 LEU A CB 1 ATOM 3823 C CG . LEU A 1 498 ? -40.089 40.139 -7.724 1.00 153.67 ? 498 LEU A CG 1 ATOM 3824 C CD1 . LEU A 1 498 ? -39.407 39.167 -6.771 1.00 153.60 ? 498 LEU A CD1 1 ATOM 3825 C CD2 . LEU A 1 498 ? -40.049 39.615 -9.150 1.00 147.67 ? 498 LEU A CD2 1 ATOM 3826 N N . LEU A 1 499 ? -44.696 40.850 -8.443 1.00 107.18 ? 499 LEU A N 1 ATOM 3827 C CA . LEU A 1 499 ? -46.105 40.790 -8.073 1.00 105.37 ? 499 LEU A CA 1 ATOM 3828 C C . LEU A 1 499 ? -46.448 39.452 -7.425 1.00 119.19 ? 499 LEU A C 1 ATOM 3829 O O . LEU A 1 499 ? -46.024 38.400 -7.903 1.00 120.45 ? 499 LEU A O 1 ATOM 3830 C CB . LEU A 1 499 ? -46.989 41.021 -9.298 1.00 102.87 ? 499 LEU A CB 1 ATOM 3831 C CG . LEU A 1 499 ? -46.777 42.355 -10.014 1.00 107.01 ? 499 LEU A CG 1 ATOM 3832 C CD1 . LEU A 1 499 ? -47.722 42.491 -11.196 1.00 106.34 ? 499 LEU A CD1 1 ATOM 3833 C CD2 . LEU A 1 499 ? -46.955 43.510 -9.043 1.00 116.36 ? 499 LEU A CD2 1 ATOM 3834 N N . ASP A 1 500 ? -47.221 39.507 -6.342 1.00 120.60 ? 500 ASP A N 1 ATOM 3835 C CA . ASP A 1 500 ? -47.633 38.314 -5.603 1.00 114.08 ? 500 ASP A CA 1 ATOM 3836 C C . ASP A 1 500 ? -46.441 37.490 -5.121 1.00 109.15 ? 500 ASP A C 1 ATOM 3837 O O . ASP A 1 500 ? -46.318 36.311 -5.449 1.00 109.28 ? 500 ASP A O 1 ATOM 3838 C CB . ASP A 1 500 ? -48.558 37.444 -6.456 1.00 106.65 ? 500 ASP A CB 1 ATOM 3839 C CG . ASP A 1 500 ? -49.590 36.710 -5.628 1.00 108.33 ? 500 ASP A CG 1 ATOM 3840 O OD1 . ASP A 1 500 ? -49.401 36.607 -4.397 1.00 130.75 ? 500 ASP A OD1 1 ATOM 3841 O OD2 . ASP A 1 500 ? -50.589 36.237 -6.205 1.00 96.96 ? 500 ASP A OD2 1 ATOM 3842 N N . LYS A 1 501 ? -45.563 38.126 -4.350 1.00 118.33 ? 501 LYS A N 1 ATOM 3843 C CA . LYS A 1 501 ? -44.356 37.488 -3.824 1.00 115.30 ? 501 LYS A CA 1 ATOM 3844 C C . LYS A 1 501 ? -44.649 36.193 -3.061 1.00 113.31 ? 501 LYS A C 1 ATOM 3845 O O . LYS A 1 501 ? -43.780 35.330 -2.932 1.00 100.97 ? 501 LYS A O 1 ATOM 3846 C CB . LYS A 1 501 ? -43.603 38.463 -2.914 1.00 110.87 ? 501 LYS A CB 1 ATOM 3847 C CG . LYS A 1 501 ? -42.247 37.964 -2.432 1.00 114.65 ? 501 LYS A CG 1 ATOM 3848 C CD . LYS A 1 501 ? -41.746 38.781 -1.251 1.00 118.11 ? 501 LYS A CD 1 ATOM 3849 C CE . LYS A 1 501 ? -40.417 38.254 -0.731 1.00 121.46 ? 501 LYS A CE 1 ATOM 3850 N NZ . LYS A 1 501 ? -39.915 39.051 0.425 1.00 116.59 ? 501 LYS A NZ 1 ATOM 3851 N N . LEU A 1 502 ? -45.882 36.047 -2.585 1.00 128.16 ? 502 LEU A N 1 ATOM 3852 C CA . LEU A 1 502 ? -46.255 34.889 -1.781 1.00 125.95 ? 502 LEU A CA 1 ATOM 3853 C C . LEU A 1 502 ? -46.295 33.642 -2.651 1.00 120.80 ? 502 LEU A C 1 ATOM 3854 O O . LEU A 1 502 ? -45.515 32.713 -2.449 1.00 131.94 ? 502 LEU A O 1 ATOM 3855 C CB . LEU A 1 502 ? -47.610 35.103 -1.103 1.00 125.79 ? 502 LEU A CB 1 ATOM 3856 C CG . LEU A 1 502 ? -47.698 36.204 -0.044 1.00 125.36 ? 502 LEU A CG 1 ATOM 3857 C CD1 . LEU A 1 502 ? -49.073 36.217 0.606 1.00 115.73 ? 502 LEU A CD1 1 ATOM 3858 C CD2 . LEU A 1 502 ? -46.612 36.035 1.003 1.00 112.60 ? 502 LEU A CD2 1 ATOM 3859 N N . LYS A 1 503 ? -47.197 33.621 -3.625 1.00 128.90 ? 503 LYS A N 1 ATOM 3860 C CA . LYS A 1 503 ? -47.268 32.481 -4.523 1.00 137.43 ? 503 LYS A CA 1 ATOM 3861 C C . LYS A 1 503 ? -46.236 32.626 -5.633 1.00 153.85 ? 503 LYS A C 1 ATOM 3862 O O . LYS A 1 503 ? -46.300 33.545 -6.449 1.00 165.34 ? 503 LYS A O 1 ATOM 3863 C CB . LYS A 1 503 ? -48.671 32.342 -5.114 1.00 122.42 ? 503 LYS A CB 1 ATOM 3864 C CG . LYS A 1 503 ? -49.731 31.979 -4.092 1.00 130.34 ? 503 LYS A CG 1 ATOM 3865 C CD . LYS A 1 503 ? -51.048 31.630 -4.762 1.00 138.74 ? 503 LYS A CD 1 ATOM 3866 C CE . LYS A 1 503 ? -52.048 31.100 -3.754 1.00 131.67 ? 503 LYS A CE 1 ATOM 3867 N NZ . LYS A 1 503 ? -51.545 29.881 -3.059 1.00 140.74 ? 503 LYS A NZ 1 ATOM 3868 N N . GLN A 1 504 ? -45.289 31.695 -5.651 1.00 149.22 ? 504 GLN A N 1 ATOM 3869 C CA . GLN A 1 504 ? -44.215 31.684 -6.634 1.00 144.42 ? 504 GLN A CA 1 ATOM 3870 C C . GLN A 1 504 ? -43.730 30.246 -6.772 1.00 141.10 ? 504 GLN A C 1 ATOM 3871 O O . GLN A 1 504 ? -44.411 29.335 -6.308 1.00 128.27 ? 504 GLN A O 1 ATOM 3872 C CB . GLN A 1 504 ? -43.081 32.631 -6.239 1.00 143.53 ? 504 GLN A CB 1 ATOM 3873 C CG . GLN A 1 504 ? -42.416 33.303 -7.436 1.00 147.37 ? 504 GLN A CG 1 ATOM 3874 C CD . GLN A 1 504 ? -41.546 34.481 -7.046 1.00 155.97 ? 504 GLN A CD 1 ATOM 3875 O OE1 . GLN A 1 504 ? -41.421 34.814 -5.868 1.00 159.73 ? 504 GLN A OE1 1 ATOM 3876 N NE2 . GLN A 1 504 ? -40.940 35.122 -8.040 1.00 149.34 ? 504 GLN A NE2 1 ATOM 3877 N N . LYS A 1 505 ? -42.576 30.057 -7.416 1.00 151.44 ? 505 LYS A N 1 ATOM 3878 C CA . LYS A 1 505 ? -42.123 28.754 -7.925 1.00 161.47 ? 505 LYS A CA 1 ATOM 3879 C C . LYS A 1 505 ? -43.321 28.099 -8.616 1.00 166.29 ? 505 LYS A C 1 ATOM 3880 O O . LYS A 1 505 ? -43.993 28.760 -9.408 1.00 176.81 ? 505 LYS A O 1 ATOM 3881 C CB . LYS A 1 505 ? -41.486 27.862 -6.828 1.00 178.25 ? 505 LYS A CB 1 ATOM 3882 C CG . LYS A 1 505 ? -42.332 27.421 -5.627 1.00 179.50 ? 505 LYS A CG 1 ATOM 3883 C CD . LYS A 1 505 ? -42.134 28.321 -4.414 1.00 182.58 ? 505 LYS A CD 1 ATOM 3884 C CE . LYS A 1 505 ? -43.075 27.924 -3.284 1.00 175.17 ? 505 LYS A CE 1 ATOM 3885 N NZ . LYS A 1 505 ? -42.944 28.813 -2.097 1.00 162.77 ? 505 LYS A NZ 1 ATOM 3886 N N . GLY A 1 506 ? -43.601 26.826 -8.355 1.00 161.08 ? 506 GLY A N 1 ATOM 3887 C CA . GLY A 1 506 ? -44.861 26.282 -8.824 1.00 154.82 ? 506 GLY A CA 1 ATOM 3888 C C . GLY A 1 506 ? -45.984 26.944 -8.047 1.00 150.50 ? 506 GLY A C 1 ATOM 3889 O O . GLY A 1 506 ? -46.067 26.777 -6.828 1.00 159.26 ? 506 GLY A O 1 ATOM 3890 N N . ALA A 1 507 ? -46.860 27.653 -8.761 1.00 136.62 ? 507 ALA A N 1 ATOM 3891 C CA . ALA A 1 507 ? -47.957 28.425 -8.167 1.00 138.15 ? 507 ALA A CA 1 ATOM 3892 C C . ALA A 1 507 ? -48.698 29.234 -9.227 1.00 149.67 ? 507 ALA A C 1 ATOM 3893 O O . ALA A 1 507 ? -48.311 29.253 -10.395 1.00 155.96 ? 507 ALA A O 1 ATOM 3894 C CB . ALA A 1 507 ? -47.448 29.362 -7.078 1.00 130.72 ? 507 ALA A CB 1 ATOM 3895 N N . ILE A 1 508 ? -49.764 29.906 -8.802 1.00 149.10 ? 508 ILE A N 1 ATOM 3896 C CA . ILE A 1 508 ? -50.457 30.876 -9.643 1.00 142.05 ? 508 ILE A CA 1 ATOM 3897 C C . ILE A 1 508 ? -49.896 32.275 -9.419 1.00 148.05 ? 508 ILE A C 1 ATOM 3898 O O . ILE A 1 508 ? -49.695 32.696 -8.280 1.00 159.62 ? 508 ILE A O 1 ATOM 3899 C CB . ILE A 1 508 ? -51.969 30.897 -9.361 1.00 152.74 ? 508 ILE A CB 1 ATOM 3900 C CG1 . ILE A 1 508 ? -52.261 30.250 -8.005 1.00 161.94 ? 508 ILE A CG1 1 ATOM 3901 C CG2 . ILE A 1 508 ? -52.733 30.206 -10.481 1.00 154.17 ? 508 ILE A CG2 1 ATOM 3902 C CD1 . ILE A 1 508 ? -53.730 30.167 -7.667 1.00 163.78 ? 508 ILE A CD1 1 ATOM 3903 N N . ARG A 1 509 ? -49.648 32.992 -10.510 1.00 162.06 ? 509 ARG A N 1 ATOM 3904 C CA . ARG A 1 509 ? -49.131 34.354 -10.432 1.00 166.55 ? 509 ARG A CA 1 ATOM 3905 C C . ARG A 1 509 ? -50.200 35.317 -9.924 1.00 148.59 ? 509 ARG A C 1 ATOM 3906 O O . ARG A 1 509 ? -49.934 36.142 -9.049 1.00 156.09 ? 509 ARG A O 1 ATOM 3907 C CB . ARG A 1 509 ? -48.616 34.805 -11.800 1.00 175.25 ? 509 ARG A CB 1 ATOM 3908 C CG . ARG A 1 509 ? -47.449 33.980 -12.315 1.00 178.51 ? 509 ARG A CG 1 ATOM 3909 C CD . ARG A 1 509 ? -47.299 34.101 -13.823 1.00 176.95 ? 509 ARG A CD 1 ATOM 3910 N NE . ARG A 1 509 ? -46.151 33.345 -14.315 1.00 174.89 ? 509 ARG A NE 1 ATOM 3911 C CZ . ARG A 1 509 ? -46.162 32.037 -14.551 1.00 171.85 ? 509 ARG A CZ 1 ATOM 3912 N NH1 . ARG A 1 509 ? -47.264 31.331 -14.338 1.00 169.93 ? 509 ARG A NH1 1 ATOM 3913 N NH2 . ARG A 1 509 ? -45.068 31.433 -14.997 1.00 169.61 ? 509 ARG A NH2 1 ATOM 3914 N N . ARG A 1 510 ? -51.388 35.222 -10.518 1.00 126.67 ? 510 ARG A N 1 ATOM 3915 C CA . ARG A 1 510 ? -52.593 35.943 -10.091 1.00 110.16 ? 510 ARG A CA 1 ATOM 3916 C C . ARG A 1 510 ? -52.566 37.433 -10.427 1.00 115.57 ? 510 ARG A C 1 ATOM 3917 O O . ARG A 1 510 ? -53.606 38.088 -10.421 1.00 111.96 ? 510 ARG A O 1 ATOM 3918 C CB . ARG A 1 510 ? -52.827 35.765 -8.587 1.00 99.53 ? 510 ARG A CB 1 ATOM 3919 C CG . ARG A 1 510 ? -53.108 34.336 -8.168 1.00 112.54 ? 510 ARG A CG 1 ATOM 3920 C CD . ARG A 1 510 ? -52.947 34.168 -6.671 1.00 109.09 ? 510 ARG A CD 1 ATOM 3921 N NE . ARG A 1 510 ? -53.768 35.114 -5.923 1.00 103.00 ? 510 ARG A NE 1 ATOM 3922 C CZ . ARG A 1 510 ? -53.472 35.555 -4.706 1.00 105.63 ? 510 ARG A CZ 1 ATOM 3923 N NH1 . ARG A 1 510 ? -52.367 35.143 -4.101 1.00 108.57 ? 510 ARG A NH1 1 ATOM 3924 N NH2 . ARG A 1 510 ? -54.275 36.414 -4.094 1.00 116.66 ? 510 ARG A NH2 1 ATOM 3925 N N . ALA A 1 511 ? -51.388 37.963 -10.736 1.00 127.95 ? 511 ALA A N 1 ATOM 3926 C CA . ALA A 1 511 ? -51.261 39.368 -11.110 1.00 115.71 ? 511 ALA A CA 1 ATOM 3927 C C . ALA A 1 511 ? -50.102 39.571 -12.075 1.00 113.40 ? 511 ALA A C 1 ATOM 3928 O O . ALA A 1 511 ? -49.053 38.945 -11.934 1.00 117.48 ? 511 ALA A O 1 ATOM 3929 C CB . ALA A 1 511 ? -51.079 40.234 -9.873 1.00 106.03 ? 511 ALA A CB 1 ATOM 3930 N N . LEU A 1 512 ? -50.294 40.451 -13.052 1.00 109.40 ? 512 LEU A N 1 ATOM 3931 C CA . LEU A 1 512 ? -49.246 40.752 -14.021 1.00 115.30 ? 512 LEU A CA 1 ATOM 3932 C C . LEU A 1 512 ? -49.276 42.222 -14.426 1.00 115.64 ? 512 LEU A C 1 ATOM 3933 O O . LEU A 1 512 ? -50.257 42.925 -14.181 1.00 115.87 ? 512 LEU A O 1 ATOM 3934 C CB . LEU A 1 512 ? -49.378 39.868 -15.265 1.00 123.37 ? 512 LEU A CB 1 ATOM 3935 C CG . LEU A 1 512 ? -49.305 38.346 -15.125 1.00 126.32 ? 512 LEU A CG 1 ATOM 3936 C CD1 . LEU A 1 512 ? -50.695 37.747 -14.957 1.00 123.05 ? 512 LEU A CD1 1 ATOM 3937 C CD2 . LEU A 1 512 ? -48.590 37.731 -16.317 1.00 142.51 ? 512 LEU A CD2 1 ATOM 3938 N N . PHE A 1 513 ? -48.194 42.682 -15.042 1.00 117.05 ? 513 PHE A N 1 ATOM 3939 C CA . PHE A 1 513 ? -48.132 44.046 -15.549 1.00 128.21 ? 513 PHE A CA 1 ATOM 3940 C C . PHE A 1 513 ? -48.856 44.152 -16.887 1.00 143.10 ? 513 PHE A C 1 ATOM 3941 O O . PHE A 1 513 ? -48.900 43.193 -17.658 1.00 141.67 ? 513 PHE A O 1 ATOM 3942 C CB . PHE A 1 513 ? -46.680 44.507 -15.681 1.00 135.78 ? 513 PHE A CB 1 ATOM 3943 C CG . PHE A 1 513 ? -45.994 44.715 -14.360 1.00 128.34 ? 513 PHE A CG 1 ATOM 3944 C CD1 . PHE A 1 513 ? -46.158 45.899 -13.660 1.00 120.67 ? 513 PHE A CD1 1 ATOM 3945 C CD2 . PHE A 1 513 ? -45.193 43.726 -13.814 1.00 115.88 ? 513 PHE A CD2 1 ATOM 3946 C CE1 . PHE A 1 513 ? -45.536 46.094 -12.443 1.00 111.89 ? 513 PHE A CE1 1 ATOM 3947 C CE2 . PHE A 1 513 ? -44.567 43.916 -12.598 1.00 109.13 ? 513 PHE A CE2 1 ATOM 3948 C CZ . PHE A 1 513 ? -44.739 45.101 -11.912 1.00 109.63 ? 513 PHE A CZ 1 ATOM 3949 N N . LEU A 1 514 ? -49.427 45.323 -17.148 1.00 148.28 ? 514 LEU A N 1 ATOM 3950 C CA . LEU A 1 514 ? -50.255 45.541 -18.329 1.00 142.57 ? 514 LEU A CA 1 ATOM 3951 C C . LEU A 1 514 ? -49.505 45.324 -19.637 1.00 148.48 ? 514 LEU A C 1 ATOM 3952 O O . LEU A 1 514 ? -49.889 44.488 -20.454 1.00 157.68 ? 514 LEU A O 1 ATOM 3953 C CB . LEU A 1 514 ? -50.829 46.958 -18.305 1.00 146.54 ? 514 LEU A CB 1 ATOM 3954 C CG . LEU A 1 514 ? -51.644 47.393 -19.521 1.00 165.78 ? 514 LEU A CG 1 ATOM 3955 C CD1 . LEU A 1 514 ? -52.954 46.625 -19.592 1.00 159.62 ? 514 LEU A CD1 1 ATOM 3956 C CD2 . LEU A 1 514 ? -51.890 48.893 -19.485 1.00 177.53 ? 514 LEU A CD2 1 ATOM 3957 N N . TYR A 1 515 ? -48.428 46.077 -19.822 1.00 153.73 ? 515 TYR A N 1 ATOM 3958 C CA . TYR A 1 515 ? -47.701 46.091 -21.085 1.00 157.91 ? 515 TYR A CA 1 ATOM 3959 C C . TYR A 1 515 ? -46.831 44.855 -21.265 1.00 155.83 ? 515 TYR A C 1 ATOM 3960 O O . TYR A 1 515 ? -47.020 44.084 -22.204 1.00 150.77 ? 515 TYR A O 1 ATOM 3961 C CB . TYR A 1 515 ? -46.852 47.355 -21.185 1.00 170.73 ? 515 TYR A CB 1 ATOM 3962 C CG . TYR A 1 515 ? -47.663 48.620 -21.037 1.00 175.97 ? 515 TYR A CG 1 ATOM 3963 C CD1 . TYR A 1 515 ? -48.455 49.083 -22.079 1.00 170.19 ? 515 TYR A CD1 1 ATOM 3964 C CD2 . TYR A 1 515 ? -47.646 49.345 -19.852 1.00 179.16 ? 515 TYR A CD2 1 ATOM 3965 C CE1 . TYR A 1 515 ? -49.203 50.235 -21.949 1.00 171.61 ? 515 TYR A CE1 1 ATOM 3966 C CE2 . TYR A 1 515 ? -48.392 50.500 -19.713 1.00 180.79 ? 515 TYR A CE2 1 ATOM 3967 C CZ . TYR A 1 515 ? -49.168 50.940 -20.765 1.00 178.85 ? 515 TYR A CZ 1 ATOM 3968 O OH . TYR A 1 515 ? -49.913 52.089 -20.635 1.00 182.65 ? 515 TYR A OH 1 ATOM 3969 N N . SER A 1 516 ? -45.865 44.683 -20.369 1.00 158.88 ? 516 SER A N 1 ATOM 3970 C CA . SER A 1 516 ? -44.924 43.572 -20.446 1.00 158.04 ? 516 SER A CA 1 ATOM 3971 C C . SER A 1 516 ? -45.602 42.202 -20.365 1.00 149.43 ? 516 SER A C 1 ATOM 3972 O O . SER A 1 516 ? -45.006 41.192 -20.742 1.00 147.09 ? 516 SER A O 1 ATOM 3973 C CB . SER A 1 516 ? -43.879 43.698 -19.336 1.00 156.76 ? 516 SER A CB 1 ATOM 3974 O OG . SER A 1 516 ? -43.205 44.943 -19.417 1.00 152.75 ? 516 SER A OG 1 ATOM 3975 N N . ARG A 1 517 ? -46.842 42.180 -19.876 1.00 145.61 ? 517 ARG A N 1 ATOM 3976 C CA . ARG A 1 517 ? -47.612 40.946 -19.715 1.00 146.36 ? 517 ARG A CA 1 ATOM 3977 C C . ARG A 1 517 ? -46.854 39.933 -18.863 1.00 151.73 ? 517 ARG A C 1 ATOM 3978 O O . ARG A 1 517 ? -46.927 38.729 -19.102 1.00 152.75 ? 517 ARG A O 1 ATOM 3979 C CB . ARG A 1 517 ? -47.951 40.332 -21.077 1.00 158.58 ? 517 ARG A CB 1 ATOM 3980 C CG . ARG A 1 517 ? -48.541 41.311 -22.079 1.00 168.94 ? 517 ARG A CG 1 ATOM 3981 C CD . ARG A 1 517 ? -48.611 40.697 -23.469 1.00 161.63 ? 517 ARG A CD 1 ATOM 3982 N NE . ARG A 1 517 ? -49.734 39.775 -23.609 1.00 160.27 ? 517 ARG A NE 1 ATOM 3983 C CZ . ARG A 1 517 ? -50.783 39.996 -24.394 1.00 164.13 ? 517 ARG A CZ 1 ATOM 3984 N NH1 . ARG A 1 517 ? -51.763 39.106 -24.461 1.00 153.66 ? 517 ARG A NH1 1 ATOM 3985 N NH2 . ARG A 1 517 ? -50.848 41.105 -25.119 1.00 173.00 ? 517 ARG A NH2 1 ATOM 3986 N N . SER A 1 518 ? -46.126 40.432 -17.869 1.00 152.63 ? 518 SER A N 1 ATOM 3987 C CA . SER A 1 518 ? -45.253 39.590 -17.062 1.00 148.56 ? 518 SER A CA 1 ATOM 3988 C C . SER A 1 518 ? -45.504 39.782 -15.570 1.00 142.09 ? 518 SER A C 1 ATOM 3989 O O . SER A 1 518 ? -45.911 40.861 -15.142 1.00 146.63 ? 518 SER A O 1 ATOM 3990 C CB . SER A 1 518 ? -43.788 39.890 -17.389 1.00 158.74 ? 518 SER A CB 1 ATOM 3991 O OG . SER A 1 518 ? -43.479 41.248 -17.129 1.00 160.97 ? 518 SER A OG 1 ATOM 3992 N N . PRO A 1 519 ? -45.266 38.727 -14.774 1.00 137.06 ? 519 PRO A N 1 ATOM 3993 C CA . PRO A 1 519 ? -45.378 38.816 -13.314 1.00 133.71 ? 519 PRO A CA 1 ATOM 3994 C C . PRO A 1 519 ? -44.274 39.673 -12.697 1.00 142.97 ? 519 PRO A C 1 ATOM 3995 O O . PRO A 1 519 ? -44.410 40.134 -11.563 1.00 145.96 ? 519 PRO A O 1 ATOM 3996 C CB . PRO A 1 519 ? -45.251 37.357 -12.865 1.00 130.30 ? 519 PRO A CB 1 ATOM 3997 C CG . PRO A 1 519 ? -44.464 36.703 -13.946 1.00 136.89 ? 519 PRO A CG 1 ATOM 3998 C CD . PRO A 1 519 ? -44.913 37.366 -15.216 1.00 143.53 ? 519 PRO A CD 1 ATOM 3999 N N . SER A 1 520 ? -43.193 39.882 -13.442 1.00 143.43 ? 520 SER A N 1 ATOM 4000 C CA . SER A 1 520 ? -42.060 40.656 -12.950 1.00 132.21 ? 520 SER A CA 1 ATOM 4001 C C . SER A 1 520 ? -41.657 41.750 -13.934 1.00 137.44 ? 520 SER A C 1 ATOM 4002 O O . SER A 1 520 ? -41.991 41.689 -15.118 1.00 137.92 ? 520 SER A O 1 ATOM 4003 C CB . SER A 1 520 ? -40.869 39.739 -12.676 1.00 138.43 ? 520 SER A CB 1 ATOM 4004 O OG . SER A 1 520 ? -40.445 39.090 -13.862 1.00 149.78 ? 520 SER A OG 1 ATOM 4005 N N . HIS A 1 521 ? -40.934 42.748 -13.435 1.00 133.02 ? 521 HIS A N 1 ATOM 4006 C CA . HIS A 1 521 ? -40.471 43.848 -14.271 1.00 127.79 ? 521 HIS A CA 1 ATOM 4007 C C . HIS A 1 521 ? -39.182 44.443 -13.717 1.00 128.17 ? 521 HIS A C 1 ATOM 4008 O O . HIS A 1 521 ? -38.918 44.362 -12.517 1.00 130.61 ? 521 HIS A O 1 ATOM 4009 C CB . HIS A 1 521 ? -41.547 44.929 -14.378 1.00 130.32 ? 521 HIS A CB 1 ATOM 4010 C CG . HIS A 1 521 ? -41.368 45.844 -15.549 1.00 153.00 ? 521 HIS A CG 1 ATOM 4011 N ND1 . HIS A 1 521 ? -40.443 46.866 -15.564 1.00 150.20 ? 521 HIS A ND1 1 ATOM 4012 C CD2 . HIS A 1 521 ? -41.998 45.889 -16.747 1.00 167.22 ? 521 HIS A CD2 1 ATOM 4013 C CE1 . HIS A 1 521 ? -40.511 47.501 -16.720 1.00 164.83 ? 521 HIS A CE1 1 ATOM 4014 N NE2 . HIS A 1 521 ? -41.446 46.928 -17.456 1.00 176.76 ? 521 HIS A NE2 1 ATOM 4015 N N . SER A 1 522 ? -38.385 45.041 -14.597 1.00 138.39 ? 522 SER A N 1 ATOM 4016 C CA . SER A 1 522 ? -37.133 45.679 -14.201 1.00 127.74 ? 522 SER A CA 1 ATOM 4017 C C . SER A 1 522 ? -37.075 47.119 -14.701 1.00 131.88 ? 522 SER A C 1 ATOM 4018 O O . SER A 1 522 ? -37.665 47.448 -15.729 1.00 145.36 ? 522 SER A O 1 ATOM 4019 C CB . SER A 1 522 ? -35.938 44.888 -14.733 1.00 130.06 ? 522 SER A CB 1 ATOM 4020 O OG . SER A 1 522 ? -36.002 43.534 -14.321 1.00 140.69 ? 522 SER A OG 1 ATOM 4021 N N . LYS A 1 523 ? -36.360 47.973 -13.974 1.00 135.62 ? 523 LYS A N 1 ATOM 4022 C CA . LYS A 1 523 ? -36.263 49.387 -14.327 1.00 143.93 ? 523 LYS A CA 1 ATOM 4023 C C . LYS A 1 523 ? -34.890 49.975 -14.018 1.00 148.65 ? 523 LYS A C 1 ATOM 4024 O O . LYS A 1 523 ? -34.260 49.620 -13.021 1.00 144.91 ? 523 LYS A O 1 ATOM 4025 C CB . LYS A 1 523 ? -37.339 50.194 -13.594 1.00 144.99 ? 523 LYS A CB 1 ATOM 4026 C CG . LYS A 1 523 ? -38.711 50.173 -14.251 1.00 158.63 ? 523 LYS A CG 1 ATOM 4027 C CD . LYS A 1 523 ? -38.737 51.031 -15.506 1.00 163.96 ? 523 LYS A CD 1 ATOM 4028 C CE . LYS A 1 523 ? -40.157 51.217 -16.015 1.00 158.95 ? 523 LYS A CE 1 ATOM 4029 N NZ . LYS A 1 523 ? -40.223 52.168 -17.160 1.00 159.66 ? 523 LYS A NZ 1 ATOM 4030 N N . ASN A 1 524 ? -34.434 50.879 -14.881 1.00 160.06 ? 524 ASN A N 1 ATOM 4031 C CA . ASN A 1 524 ? -33.207 51.629 -14.639 1.00 158.64 ? 524 ASN A CA 1 ATOM 4032 C C . ASN A 1 524 ? -33.531 53.045 -14.171 1.00 161.71 ? 524 ASN A C 1 ATOM 4033 O O . ASN A 1 524 ? -34.027 53.864 -14.946 1.00 168.56 ? 524 ASN A O 1 ATOM 4034 C CB . ASN A 1 524 ? -32.343 51.682 -15.903 1.00 164.54 ? 524 ASN A CB 1 ATOM 4035 C CG . ASN A 1 524 ? -31.900 50.307 -16.370 1.00 162.09 ? 524 ASN A CG 1 ATOM 4036 O OD1 . ASN A 1 524 ? -30.805 49.851 -16.043 1.00 153.43 ? 524 ASN A OD1 1 ATOM 4037 N ND2 . ASN A 1 524 ? -32.751 49.643 -17.144 1.00 168.29 ? 524 ASN A ND2 1 ATOM 4038 N N . MET A 1 525 ? -33.249 53.334 -12.904 1.00 147.21 ? 525 MET A N 1 ATOM 4039 C CA . MET A 1 525 ? -33.560 54.646 -12.345 1.00 144.61 ? 525 MET A CA 1 ATOM 4040 C C . MET A 1 525 ? -32.309 55.461 -12.048 1.00 141.84 ? 525 MET A C 1 ATOM 4041 O O . MET A 1 525 ? -31.269 54.913 -11.686 1.00 146.93 ? 525 MET A O 1 ATOM 4042 C CB . MET A 1 525 ? -34.391 54.505 -11.069 1.00 135.88 ? 525 MET A CB 1 ATOM 4043 C CG . MET A 1 525 ? -35.845 54.143 -11.305 1.00 133.99 ? 525 MET A CG 1 ATOM 4044 S SD . MET A 1 525 ? -36.879 54.571 -9.891 1.00 147.49 ? 525 MET A SD 1 ATOM 4045 C CE . MET A 1 525 ? -36.621 56.343 -9.815 1.00 121.54 ? 525 MET A CE 1 ATOM 4046 N N . THR A 1 526 ? -32.423 56.775 -12.207 1.00 144.49 ? 526 THR A N 1 ATOM 4047 C CA . THR A 1 526 ? -31.340 57.688 -11.866 1.00 156.61 ? 526 THR A CA 1 ATOM 4048 C C . THR A 1 526 ? -31.855 58.867 -11.046 1.00 160.26 ? 526 THR A C 1 ATOM 4049 O O . THR A 1 526 ? -32.638 59.679 -11.538 1.00 169.25 ? 526 THR A O 1 ATOM 4050 C CB . THR A 1 526 ? -30.636 58.222 -13.126 1.00 161.54 ? 526 THR A CB 1 ATOM 4051 O OG1 . THR A 1 526 ? -30.068 57.130 -13.858 1.00 167.49 ? 526 THR A OG1 1 ATOM 4052 C CG2 . THR A 1 526 ? -29.537 59.201 -12.746 1.00 150.98 ? 526 THR A CG2 1 ATOM 4053 N N . ILE A 1 527 ? -31.403 58.965 -9.800 1.00 149.25 ? 527 ILE A N 1 ATOM 4054 C CA . ILE A 1 527 ? -31.797 60.070 -8.933 1.00 150.06 ? 527 ILE A CA 1 ATOM 4055 C C . ILE A 1 527 ? -30.590 60.933 -8.590 1.00 140.06 ? 527 ILE A C 1 ATOM 4056 O O . ILE A 1 527 ? -29.465 60.606 -8.962 1.00 123.59 ? 527 ILE A O 1 ATOM 4057 C CB . ILE A 1 527 ? -32.446 59.564 -7.636 1.00 143.31 ? 527 ILE A CB 1 ATOM 4058 C CG1 . ILE A 1 527 ? -31.466 58.675 -6.870 1.00 130.73 ? 527 ILE A CG1 1 ATOM 4059 C CG2 . ILE A 1 527 ? -33.729 58.805 -7.944 1.00 145.50 ? 527 ILE A CG2 1 ATOM 4060 C CD1 . ILE A 1 527 ? -32.053 58.047 -5.630 1.00 130.28 ? 527 ILE A CD1 1 ATOM 4061 N N . SER A 1 528 ? -30.819 62.027 -7.872 1.00 135.99 ? 528 SER A N 1 ATOM 4062 C CA . SER A 1 528 ? -29.738 62.955 -7.565 1.00 130.28 ? 528 SER A CA 1 ATOM 4063 C C . SER A 1 528 ? -29.751 63.448 -6.122 1.00 134.13 ? 528 SER A C 1 ATOM 4064 O O . SER A 1 528 ? -30.702 64.100 -5.690 1.00 145.59 ? 528 SER A O 1 ATOM 4065 C CB . SER A 1 528 ? -29.800 64.152 -8.517 1.00 152.21 ? 528 SER A CB 1 ATOM 4066 O OG . SER A 1 528 ? -31.098 64.722 -8.530 1.00 153.13 ? 528 SER A OG 1 ATOM 4067 N N . ARG A 1 529 ? -28.688 63.118 -5.392 1.00 133.11 ? 529 ARG A N 1 ATOM 4068 C CA . ARG A 1 529 ? -28.382 63.689 -4.078 1.00 136.80 ? 529 ARG A CA 1 ATOM 4069 C C . ARG A 1 529 ? -29.565 63.789 -3.114 1.00 149.47 ? 529 ARG A C 1 ATOM 4070 O O . ARG A 1 529 ? -30.379 62.874 -3.009 1.00 156.75 ? 529 ARG A O 1 ATOM 4071 C CB . ARG A 1 529 ? -27.761 65.076 -4.254 1.00 156.94 ? 529 ARG A CB 1 ATOM 4072 C CG . ARG A 1 529 ? -26.312 65.054 -4.721 1.00 181.35 ? 529 ARG A CG 1 ATOM 4073 C CD . ARG A 1 529 ? -25.365 64.647 -3.597 1.00 178.73 ? 529 ARG A CD 1 ATOM 4074 N NE . ARG A 1 529 ? -25.336 65.637 -2.522 1.00 176.32 ? 529 ARG A NE 1 ATOM 4075 C CZ . ARG A 1 529 ? -24.519 65.584 -1.475 1.00 164.91 ? 529 ARG A CZ 1 ATOM 4076 N NH1 . ARG A 1 529 ? -23.652 64.589 -1.354 1.00 152.45 ? 529 ARG A NH1 1 ATOM 4077 N NH2 . ARG A 1 529 ? -24.566 66.531 -0.547 1.00 162.27 ? 529 ARG A NH2 1 ATOM 4078 N N . GLY A 1 530 ? -29.669 64.932 -2.442 1.00 141.29 ? 530 GLY A N 1 ATOM 4079 C CA . GLY A 1 530 ? -30.660 65.118 -1.397 1.00 148.93 ? 530 GLY A CA 1 ATOM 4080 C C . GLY A 1 530 ? -32.033 65.488 -1.916 1.00 168.45 ? 530 GLY A C 1 ATOM 4081 O O . GLY A 1 530 ? -32.160 66.212 -2.904 1.00 179.14 ? 530 GLY A O 1 ATOM 4082 N N . GLY A 1 531 ? -33.064 64.995 -1.236 1.00 165.85 ? 531 GLY A N 1 ATOM 4083 C CA . GLY A 1 531 ? -34.436 65.261 -1.625 1.00 164.69 ? 531 GLY A CA 1 ATOM 4084 C C . GLY A 1 531 ? -34.744 64.739 -3.013 1.00 172.86 ? 531 GLY A C 1 ATOM 4085 O O . GLY A 1 531 ? -34.068 63.832 -3.502 1.00 171.13 ? 531 GLY A O 1 ATOM 4086 N N . LEU A 1 532 ? -35.761 65.322 -3.643 1.00 184.16 ? 532 LEU A N 1 ATOM 4087 C CA . LEU A 1 532 ? -36.183 64.947 -4.991 1.00 176.22 ? 532 LEU A CA 1 ATOM 4088 C C . LEU A 1 532 ? -36.383 63.444 -5.137 1.00 151.52 ? 532 LEU A C 1 ATOM 4089 O O . LEU A 1 532 ? -35.669 62.781 -5.889 1.00 150.55 ? 532 LEU A O 1 ATOM 4090 C CB . LEU A 1 532 ? -35.171 65.438 -6.029 1.00 179.39 ? 532 LEU A CB 1 ATOM 4091 C CG . LEU A 1 532 ? -35.252 66.918 -6.403 1.00 181.81 ? 532 LEU A CG 1 ATOM 4092 C CD1 . LEU A 1 532 ? -34.200 67.265 -7.444 1.00 183.11 ? 532 LEU A CD1 1 ATOM 4093 C CD2 . LEU A 1 532 ? -36.646 67.263 -6.908 1.00 173.54 ? 532 LEU A CD2 1 ATOM 4094 N N . MET A 1 533 ? -37.362 62.911 -4.418 1.00 139.43 ? 533 MET A N 1 ATOM 4095 C CA . MET A 1 533 ? -37.673 61.496 -4.513 1.00 137.78 ? 533 MET A CA 1 ATOM 4096 C C . MET A 1 533 ? -38.379 61.255 -5.836 1.00 133.90 ? 533 MET A C 1 ATOM 4097 O O . MET A 1 533 ? -39.432 61.836 -6.091 1.00 156.12 ? 533 MET A O 1 ATOM 4098 C CB . MET A 1 533 ? -38.545 61.060 -3.335 1.00 123.64 ? 533 MET A CB 1 ATOM 4099 C CG . MET A 1 533 ? -38.669 59.561 -3.155 1.00 124.74 ? 533 MET A CG 1 ATOM 4100 S SD . MET A 1 533 ? -39.165 59.150 -1.471 1.00 172.32 ? 533 MET A SD 1 ATOM 4101 C CE . MET A 1 533 ? -38.886 57.385 -1.456 1.00 127.36 ? 533 MET A CE 1 ATOM 4102 N N . GLN A 1 534 ? -37.806 60.404 -6.679 1.00 128.65 ? 534 GLN A N 1 ATOM 4103 C CA . GLN A 1 534 ? -38.358 60.216 -8.013 1.00 145.95 ? 534 GLN A CA 1 ATOM 4104 C C . GLN A 1 534 ? -39.382 59.086 -8.005 1.00 144.17 ? 534 GLN A C 1 ATOM 4105 O O . GLN A 1 534 ? -39.521 58.382 -7.008 1.00 127.64 ? 534 GLN A O 1 ATOM 4106 C CB . GLN A 1 534 ? -37.236 59.926 -9.014 1.00 141.89 ? 534 GLN A CB 1 ATOM 4107 C CG . GLN A 1 534 ? -37.565 60.276 -10.456 1.00 154.60 ? 534 GLN A CG 1 ATOM 4108 C CD . GLN A 1 534 ? -36.427 59.959 -11.400 1.00 158.27 ? 534 GLN A CD 1 ATOM 4109 O OE1 . GLN A 1 534 ? -35.347 59.556 -10.971 1.00 144.77 ? 534 GLN A OE1 1 ATOM 4110 N NE2 . GLN A 1 534 ? -36.662 60.137 -12.695 1.00 166.92 ? 534 GLN A NE2 1 ATOM 4111 N N . CYS A 1 535 ? -40.074 58.899 -9.126 1.00 144.06 ? 535 CYS A N 1 ATOM 4112 C CA . CYS A 1 535 ? -41.136 57.904 -9.230 1.00 140.68 ? 535 CYS A CA 1 ATOM 4113 C C . CYS A 1 535 ? -41.317 57.430 -10.671 1.00 138.20 ? 535 CYS A C 1 ATOM 4114 O O . CYS A 1 535 ? -41.106 58.193 -11.613 1.00 149.66 ? 535 CYS A O 1 ATOM 4115 C CB . CYS A 1 535 ? -42.461 58.470 -8.705 1.00 145.01 ? 535 CYS A CB 1 ATOM 4116 S SG . CYS A 1 535 ? -42.530 58.807 -6.925 1.00 168.12 ? 535 CYS A SG 1 ATOM 4117 N N . GLU A 1 536 ? -41.713 56.172 -10.836 1.00 126.80 ? 536 GLU A N 1 ATOM 4118 C CA . GLU A 1 536 ? -42.082 55.645 -12.149 1.00 142.08 ? 536 GLU A CA 1 ATOM 4119 C C . GLU A 1 536 ? -43.292 54.724 -12.015 1.00 135.85 ? 536 GLU A C 1 ATOM 4120 O O . GLU A 1 536 ? -43.644 54.317 -10.908 1.00 126.28 ? 536 GLU A O 1 ATOM 4121 C CB . GLU A 1 536 ? -40.908 54.907 -12.798 1.00 147.15 ? 536 GLU A CB 1 ATOM 4122 C CG . GLU A 1 536 ? -39.756 55.813 -13.218 1.00 153.12 ? 536 GLU A CG 1 ATOM 4123 C CD . GLU A 1 536 ? -38.800 55.145 -14.188 1.00 160.32 ? 536 GLU A CD 1 ATOM 4124 O OE1 . GLU A 1 536 ? -39.185 54.129 -14.801 1.00 159.69 ? 536 GLU A OE1 1 ATOM 4125 O OE2 . GLU A 1 536 ? -37.663 55.639 -14.340 1.00 174.69 ? 536 GLU A OE2 1 ATOM 4126 N N . GLU A 1 537 ? -43.929 54.399 -13.138 1.00 134.41 ? 537 GLU A N 1 ATOM 4127 C CA . GLU A 1 537 ? -45.159 53.610 -13.106 1.00 136.12 ? 537 GLU A CA 1 ATOM 4128 C C . GLU A 1 537 ? -45.278 52.561 -14.211 1.00 147.36 ? 537 GLU A C 1 ATOM 4129 O O . GLU A 1 537 ? -44.975 52.818 -15.376 1.00 172.24 ? 537 GLU A O 1 ATOM 4130 C CB . GLU A 1 537 ? -46.378 54.534 -13.178 1.00 149.14 ? 537 GLU A CB 1 ATOM 4131 C CG . GLU A 1 537 ? -46.799 55.133 -11.850 1.00 147.23 ? 537 GLU A CG 1 ATOM 4132 C CD . GLU A 1 537 ? -48.109 55.893 -11.949 1.00 155.36 ? 537 GLU A CD 1 ATOM 4133 O OE1 . GLU A 1 537 ? -48.280 56.663 -12.918 1.00 159.95 ? 537 GLU A OE1 1 ATOM 4134 O OE2 . GLU A 1 537 ? -48.973 55.713 -11.065 1.00 148.12 ? 537 GLU A OE2 1 ATOM 4135 N N . LEU A 1 538 ? -45.722 51.375 -13.812 1.00 140.28 ? 538 LEU A N 1 ATOM 4136 C CA . LEU A 1 538 ? -46.158 50.316 -14.718 1.00 151.08 ? 538 LEU A CA 1 ATOM 4137 C C . LEU A 1 538 ? -47.370 49.715 -14.035 1.00 156.40 ? 538 LEU A C 1 ATOM 4138 O O . LEU A 1 538 ? -47.383 49.646 -12.808 1.00 150.72 ? 538 LEU A O 1 ATOM 4139 C CB . LEU A 1 538 ? -45.072 49.264 -14.929 1.00 153.62 ? 538 LEU A CB 1 ATOM 4140 C CG . LEU A 1 538 ? -43.661 49.755 -15.244 1.00 167.41 ? 538 LEU A CG 1 ATOM 4141 C CD1 . LEU A 1 538 ? -42.648 48.986 -14.416 1.00 157.51 ? 538 LEU A CD1 1 ATOM 4142 C CD2 . LEU A 1 538 ? -43.371 49.617 -16.730 1.00 178.53 ? 538 LEU A CD2 1 ATOM 4143 N N . ILE A 1 539 ? -48.405 49.299 -14.762 1.00 155.64 ? 539 ILE A N 1 ATOM 4144 C CA . ILE A 1 539 ? -49.569 48.870 -13.999 1.00 134.53 ? 539 ILE A CA 1 ATOM 4145 C C . ILE A 1 539 ? -50.217 47.502 -14.258 1.00 117.54 ? 539 ILE A C 1 ATOM 4146 O O . ILE A 1 539 ? -50.973 47.305 -15.204 1.00 121.63 ? 539 ILE A O 1 ATOM 4147 C CB . ILE A 1 539 ? -50.691 49.929 -14.166 1.00 136.55 ? 539 ILE A CB 1 ATOM 4148 C CG1 . ILE A 1 539 ? -50.928 50.244 -15.646 1.00 130.47 ? 539 ILE A CG1 1 ATOM 4149 C CG2 . ILE A 1 539 ? -50.314 51.215 -13.452 1.00 139.43 ? 539 ILE A CG2 1 ATOM 4150 C CD1 . ILE A 1 539 ? -52.139 51.114 -15.898 1.00 122.37 ? 539 ILE A CD1 1 ATOM 4151 N N . ALA A 1 540 ? -49.885 46.562 -13.378 1.00 118.25 ? 540 ALA A N 1 ATOM 4152 C CA . ALA A 1 540 ? -50.838 45.797 -12.576 1.00 114.66 ? 540 ALA A CA 1 ATOM 4153 C C . ALA A 1 540 ? -52.195 45.416 -13.167 1.00 119.66 ? 540 ALA A C 1 ATOM 4154 O O . ALA A 1 540 ? -53.202 46.001 -12.772 1.00 120.78 ? 540 ALA A O 1 ATOM 4155 C CB . ALA A 1 540 ? -51.065 46.544 -11.294 1.00 113.31 ? 540 ALA A CB 1 ATOM 4156 N N . TYR A 1 541 ? -52.260 44.470 -14.096 1.00 121.72 ? 541 TYR A N 1 ATOM 4157 C CA . TYR A 1 541 ? -53.578 43.944 -14.449 1.00 117.53 ? 541 TYR A CA 1 ATOM 4158 C C . TYR A 1 541 ? -53.838 42.626 -13.715 1.00 116.47 ? 541 TYR A C 1 ATOM 4159 O O . TYR A 1 541 ? -52.928 41.818 -13.521 1.00 116.53 ? 541 TYR A O 1 ATOM 4160 C CB . TYR A 1 541 ? -53.731 43.780 -15.968 1.00 118.40 ? 541 TYR A CB 1 ATOM 4161 C CG . TYR A 1 541 ? -53.245 42.473 -16.554 1.00 123.23 ? 541 TYR A CG 1 ATOM 4162 C CD1 . TYR A 1 541 ? -54.091 41.375 -16.654 1.00 122.50 ? 541 TYR A CD1 1 ATOM 4163 C CD2 . TYR A 1 541 ? -51.953 42.350 -17.046 1.00 146.59 ? 541 TYR A CD2 1 ATOM 4164 C CE1 . TYR A 1 541 ? -53.656 40.185 -17.200 1.00 130.76 ? 541 TYR A CE1 1 ATOM 4165 C CE2 . TYR A 1 541 ? -51.511 41.164 -17.599 1.00 156.52 ? 541 TYR A CE2 1 ATOM 4166 C CZ . TYR A 1 541 ? -52.366 40.085 -17.671 1.00 146.12 ? 541 TYR A CZ 1 ATOM 4167 O OH . TYR A 1 541 ? -51.927 38.903 -18.219 1.00 158.45 ? 541 TYR A OH 1 ATOM 4168 N N . LEU A 1 542 ? -55.085 42.433 -13.294 1.00 118.23 ? 542 LEU A N 1 ATOM 4169 C CA . LEU A 1 542 ? -55.489 41.256 -12.524 1.00 106.10 ? 542 LEU A CA 1 ATOM 4170 C C . LEU A 1 542 ? -56.056 40.168 -13.434 1.00 107.66 ? 542 LEU A C 1 ATOM 4171 O O . LEU A 1 542 ? -56.737 40.464 -14.413 1.00 115.01 ? 542 LEU A O 1 ATOM 4172 C CB . LEU A 1 542 ? -56.521 41.648 -11.464 1.00 101.75 ? 542 LEU A CB 1 ATOM 4173 C CG . LEU A 1 542 ? -56.840 40.643 -10.358 1.00 100.90 ? 542 LEU A CG 1 ATOM 4174 C CD1 . LEU A 1 542 ? -55.611 40.384 -9.510 1.00 106.50 ? 542 LEU A CD1 1 ATOM 4175 C CD2 . LEU A 1 542 ? -57.987 41.144 -9.495 1.00 99.11 ? 542 LEU A CD2 1 ATOM 4176 N N . ARG A 1 543 ? -55.793 38.908 -13.105 1.00 107.51 ? 543 ARG A N 1 ATOM 4177 C CA . ARG A 1 543 ? -56.168 37.806 -13.985 1.00 114.45 ? 543 ARG A CA 1 ATOM 4178 C C . ARG A 1 543 ? -57.679 37.567 -14.013 1.00 129.63 ? 543 ARG A C 1 ATOM 4179 O O . ARG A 1 543 ? -58.440 38.249 -13.327 1.00 133.75 ? 543 ARG A O 1 ATOM 4180 C CB . ARG A 1 543 ? -55.442 36.527 -13.564 1.00 115.86 ? 543 ARG A CB 1 ATOM 4181 C CG . ARG A 1 543 ? -54.801 35.775 -14.720 1.00 126.39 ? 543 ARG A CG 1 ATOM 4182 C CD . ARG A 1 543 ? -53.512 35.095 -14.285 1.00 134.05 ? 543 ARG A CD 1 ATOM 4183 N NE . ARG A 1 543 ? -52.756 34.574 -15.421 1.00 143.99 ? 543 ARG A NE 1 ATOM 4184 C CZ . ARG A 1 543 ? -51.505 34.130 -15.346 1.00 140.56 ? 543 ARG A CZ 1 ATOM 4185 N NH1 . ARG A 1 543 ? -50.862 34.145 -14.187 1.00 132.11 ? 543 ARG A NH1 1 ATOM 4186 N NH2 . ARG A 1 543 ? -50.894 33.674 -16.432 1.00 132.26 ? 543 ARG A NH2 1 ATOM 4187 N N . ASP A 1 544 ? -58.096 36.590 -14.814 1.00 136.47 ? 544 ASP A N 1 ATOM 4188 C CA . ASP A 1 544 ? -59.510 36.292 -15.043 1.00 139.74 ? 544 ASP A CA 1 ATOM 4189 C C . ASP A 1 544 ? -60.247 35.880 -13.766 1.00 134.54 ? 544 ASP A C 1 ATOM 4190 O O . ASP A 1 544 ? -59.663 35.268 -12.874 1.00 130.55 ? 544 ASP A O 1 ATOM 4191 C CB . ASP A 1 544 ? -59.632 35.197 -16.111 1.00 160.52 ? 544 ASP A CB 1 ATOM 4192 C CG . ASP A 1 544 ? -60.914 34.393 -15.994 1.00 177.71 ? 544 ASP A CG 1 ATOM 4193 O OD1 . ASP A 1 544 ? -60.859 33.257 -15.476 1.00 179.45 ? 544 ASP A OD1 1 ATOM 4194 O OD2 . ASP A 1 544 ? -61.975 34.892 -16.425 1.00 179.80 ? 544 ASP A OD2 1 ATOM 4195 N N . GLU A 1 545 ? -61.526 36.238 -13.678 1.00 137.83 ? 545 GLU A N 1 ATOM 4196 C CA . GLU A 1 545 ? -62.360 35.831 -12.552 1.00 138.62 ? 545 GLU A CA 1 ATOM 4197 C C . GLU A 1 545 ? -62.414 34.309 -12.464 1.00 148.93 ? 545 GLU A C 1 ATOM 4198 O O . GLU A 1 545 ? -62.713 33.636 -13.452 1.00 164.64 ? 545 GLU A O 1 ATOM 4199 C CB . GLU A 1 545 ? -63.778 36.399 -12.681 1.00 156.06 ? 545 GLU A CB 1 ATOM 4200 C CG . GLU A 1 545 ? -63.857 37.914 -12.832 1.00 152.70 ? 545 GLU A CG 1 ATOM 4201 C CD . GLU A 1 545 ? -65.290 38.428 -12.795 1.00 144.39 ? 545 GLU A CD 1 ATOM 4202 O OE1 . GLU A 1 545 ? -66.124 37.819 -12.093 1.00 142.02 ? 545 GLU A OE1 1 ATOM 4203 O OE2 . GLU A 1 545 ? -65.585 39.438 -13.468 1.00 133.36 ? 545 GLU A OE2 1 ATOM 4204 N N . SER A 1 546 ? -62.121 33.781 -11.278 1.00 153.08 ? 546 SER A N 1 ATOM 4205 C CA . SER A 1 546 ? -62.064 32.339 -11.038 1.00 172.15 ? 546 SER A CA 1 ATOM 4206 C C . SER A 1 546 ? -61.030 31.651 -11.931 1.00 171.99 ? 546 SER A C 1 ATOM 4207 O O . SER A 1 546 ? -61.256 30.544 -12.420 1.00 173.18 ? 546 SER A O 1 ATOM 4208 C CB . SER A 1 546 ? -63.443 31.696 -11.239 1.00 168.46 ? 546 SER A CB 1 ATOM 4209 O OG . SER A 1 546 ? -64.389 32.208 -10.316 1.00 161.16 ? 546 SER A OG 1 ATOM 4210 N N . GLU A 1 547 ? -59.900 32.319 -12.146 1.00 162.33 ? 547 GLU A N 1 ATOM 4211 C CA . GLU A 1 547 ? -58.774 31.725 -12.862 1.00 158.60 ? 547 GLU A CA 1 ATOM 4212 C C . GLU A 1 547 ? -57.775 31.149 -11.863 1.00 137.74 ? 547 GLU A C 1 ATOM 4213 O O . GLU A 1 547 ? -56.737 30.606 -12.237 1.00 125.15 ? 547 GLU A O 1 ATOM 4214 C CB . GLU A 1 547 ? -58.093 32.758 -13.762 1.00 160.00 ? 547 GLU A CB 1 ATOM 4215 C CG . GLU A 1 547 ? -57.770 32.261 -15.163 1.00 164.75 ? 547 GLU A CG 1 ATOM 4216 C CD . GLU A 1 547 ? -56.747 31.146 -15.169 1.00 167.30 ? 547 GLU A CD 1 ATOM 4217 O OE1 . GLU A 1 547 ? -55.536 31.448 -15.231 1.00 151.94 ? 547 GLU A OE1 1 ATOM 4218 O OE2 . GLU A 1 547 ? -57.153 29.966 -15.112 1.00 179.68 ? 547 GLU A OE2 1 ATOM 4219 N N . PHE A 1 548 ? -58.098 31.290 -10.583 1.00 126.18 ? 548 PHE A N 1 ATOM 4220 C CA . PHE A 1 548 ? -57.267 30.763 -9.510 1.00 132.20 ? 548 PHE A CA 1 ATOM 4221 C C . PHE A 1 548 ? -58.053 29.785 -8.650 1.00 147.39 ? 548 PHE A C 1 ATOM 4222 O O . PHE A 1 548 ? -57.651 28.629 -8.506 1.00 171.86 ? 548 PHE A O 1 ATOM 4223 C CB . PHE A 1 548 ? -56.695 31.883 -8.637 1.00 147.16 ? 548 PHE A CB 1 ATOM 4224 C CG . PHE A 1 548 ? -57.210 33.248 -8.975 1.00 141.66 ? 548 PHE A CG 1 ATOM 4225 C CD1 . PHE A 1 548 ? -56.556 34.037 -9.905 1.00 125.05 ? 548 PHE A CD1 1 ATOM 4226 C CD2 . PHE A 1 548 ? -58.335 33.752 -8.347 1.00 149.65 ? 548 PHE A CD2 1 ATOM 4227 C CE1 . PHE A 1 548 ? -57.023 35.298 -10.212 1.00 127.48 ? 548 PHE A CE1 1 ATOM 4228 C CE2 . PHE A 1 548 ? -58.806 35.012 -8.649 1.00 131.11 ? 548 PHE A CE2 1 ATOM 4229 C CZ . PHE A 1 548 ? -58.149 35.787 -9.583 1.00 126.82 ? 548 PHE A CZ 1 ATOM 4230 N N . ARG A 1 549 ? -59.153 30.295 -8.085 1.00 134.34 ? 549 ARG A N 1 ATOM 4231 C CA . ARG A 1 549 ? -59.921 29.716 -6.972 1.00 150.51 ? 549 ARG A CA 1 ATOM 4232 C C . ARG A 1 549 ? -59.275 30.223 -5.680 1.00 132.69 ? 549 ARG A C 1 ATOM 4233 O O . ARG A 1 549 ? -59.822 30.064 -4.587 1.00 141.48 ? 549 ARG A O 1 ATOM 4234 C CB . ARG A 1 549 ? -59.995 28.172 -7.037 1.00 156.49 ? 549 ARG A CB 1 ATOM 4235 C CG . ARG A 1 549 ? -60.441 27.441 -5.768 1.00 146.92 ? 549 ARG A CG 1 ATOM 4236 C CD . ARG A 1 549 ? -61.850 27.817 -5.330 1.00 150.86 ? 549 ARG A CD 1 ATOM 4237 N NE . ARG A 1 549 ? -62.010 27.674 -3.884 1.00 156.12 ? 549 ARG A NE 1 ATOM 4238 C CZ . ARG A 1 549 ? -63.145 27.888 -3.226 1.00 167.86 ? 549 ARG A CZ 1 ATOM 4239 N NH1 . ARG A 1 549 ? -63.188 27.734 -1.909 1.00 165.42 ? 549 ARG A NH1 1 ATOM 4240 N NH2 . ARG A 1 549 ? -64.239 28.252 -3.882 1.00 174.12 ? 549 ARG A NH2 1 ATOM 4241 N N . ASP A 1 550 ? -58.140 30.905 -5.809 1.00 117.49 ? 550 ASP A N 1 ATOM 4242 C CA . ASP A 1 550 ? -57.540 31.509 -4.631 1.00 113.61 ? 550 ASP A CA 1 ATOM 4243 C C . ASP A 1 550 ? -57.817 33.009 -4.563 1.00 114.25 ? 550 ASP A C 1 ATOM 4244 O O . ASP A 1 550 ? -57.186 33.825 -5.241 1.00 110.02 ? 550 ASP A O 1 ATOM 4245 C CB . ASP A 1 550 ? -56.035 31.252 -4.613 1.00 119.72 ? 550 ASP A CB 1 ATOM 4246 C CG . ASP A 1 550 ? -55.352 31.899 -3.432 1.00 133.89 ? 550 ASP A CG 1 ATOM 4247 O OD1 . ASP A 1 550 ? -55.315 31.275 -2.352 1.00 143.90 ? 550 ASP A OD1 1 ATOM 4248 O OD2 . ASP A 1 550 ? -54.847 33.030 -3.582 1.00 143.80 ? 550 ASP A OD2 1 ATOM 4249 N N . LYS A 1 551 ? -58.790 33.330 -3.718 1.00 126.86 ? 551 LYS A N 1 ATOM 4250 C CA . LYS A 1 551 ? -59.095 34.663 -3.206 1.00 109.27 ? 551 LYS A CA 1 ATOM 4251 C C . LYS A 1 551 ? -58.465 34.766 -1.834 1.00 117.96 ? 551 LYS A C 1 ATOM 4252 O O . LYS A 1 551 ? -57.500 34.044 -1.564 1.00 130.78 ? 551 LYS A O 1 ATOM 4253 C CB . LYS A 1 551 ? -60.593 34.916 -3.170 1.00 120.76 ? 551 LYS A CB 1 ATOM 4254 C CG . LYS A 1 551 ? -61.229 34.862 -4.546 1.00 105.60 ? 551 LYS A CG 1 ATOM 4255 C CD . LYS A 1 551 ? -62.720 35.120 -4.473 1.00 111.41 ? 551 LYS A CD 1 ATOM 4256 C CE . LYS A 1 551 ? -63.349 35.106 -5.857 1.00 117.29 ? 551 LYS A CE 1 ATOM 4257 N NZ . LYS A 1 551 ? -64.824 35.297 -5.790 1.00 113.79 ? 551 LYS A NZ 1 ATOM 4258 N N . LEU A 1 552 ? -58.947 35.676 -0.984 1.00 116.07 ? 552 LEU A N 1 ATOM 4259 C CA . LEU A 1 552 ? -58.323 35.798 0.333 1.00 124.23 ? 552 LEU A CA 1 ATOM 4260 C C . LEU A 1 552 ? -56.863 36.231 0.170 1.00 133.49 ? 552 LEU A C 1 ATOM 4261 O O . LEU A 1 552 ? -56.590 37.434 0.187 1.00 153.47 ? 552 LEU A O 1 ATOM 4262 C CB . LEU A 1 552 ? -58.455 34.507 1.153 1.00 122.02 ? 552 LEU A CB 1 ATOM 4263 C CG . LEU A 1 552 ? -59.864 34.276 1.718 1.00 139.43 ? 552 LEU A CG 1 ATOM 4264 C CD1 . LEU A 1 552 ? -59.965 33.009 2.571 1.00 136.33 ? 552 LEU A CD1 1 ATOM 4265 C CD2 . LEU A 1 552 ? -60.321 35.491 2.509 1.00 136.46 ? 552 LEU A CD2 1 ATOM 4266 N N . THR A 1 553 ? -55.938 35.270 0.131 1.00 102.68 ? 553 THR A N 1 ATOM 4267 C CA . THR A 1 553 ? -54.499 35.518 0.246 1.00 102.95 ? 553 THR A CA 1 ATOM 4268 C C . THR A 1 553 ? -54.043 36.780 -0.472 1.00 105.27 ? 553 THR A C 1 ATOM 4269 O O . THR A 1 553 ? -54.304 36.965 -1.658 1.00 116.56 ? 553 THR A O 1 ATOM 4270 C CB . THR A 1 553 ? -53.707 34.335 -0.365 1.00 105.86 ? 553 THR A CB 1 ATOM 4271 O OG1 . THR A 1 553 ? -54.149 33.097 0.199 1.00 132.00 ? 553 THR A OG1 1 ATOM 4272 C CG2 . THR A 1 553 ? -52.250 34.470 -0.104 1.00 91.74 ? 553 THR A CG2 1 ATOM 4273 N N . PRO A 1 554 ? -53.349 37.658 0.263 1.00 102.84 ? 554 PRO A N 1 ATOM 4274 C CA . PRO A 1 554 ? -53.045 38.943 -0.361 1.00 103.25 ? 554 PRO A CA 1 ATOM 4275 C C . PRO A 1 554 ? -52.026 38.791 -1.472 1.00 105.70 ? 554 PRO A C 1 ATOM 4276 O O . PRO A 1 554 ? -51.242 37.839 -1.490 1.00 98.05 ? 554 PRO A O 1 ATOM 4277 C CB . PRO A 1 554 ? -52.492 39.775 0.794 1.00 95.13 ? 554 PRO A CB 1 ATOM 4278 C CG . PRO A 1 554 ? -51.970 38.781 1.762 1.00 91.41 ? 554 PRO A CG 1 ATOM 4279 C CD . PRO A 1 554 ? -52.847 37.573 1.646 1.00 92.16 ? 554 PRO A CD 1 ATOM 4280 N N . ILE A 1 555 ? -52.069 39.725 -2.410 1.00 103.96 ? 555 ILE A N 1 ATOM 4281 C CA . ILE A 1 555 ? -51.083 39.786 -3.467 1.00 98.93 ? 555 ILE A CA 1 ATOM 4282 C C . ILE A 1 555 ? -50.002 40.743 -3.010 1.00 90.81 ? 555 ILE A C 1 ATOM 4283 O O . ILE A 1 555 ? -50.239 41.943 -2.889 1.00 98.72 ? 555 ILE A O 1 ATOM 4284 C CB . ILE A 1 555 ? -51.699 40.252 -4.794 1.00 92.87 ? 555 ILE A CB 1 ATOM 4285 C CG1 . ILE A 1 555 ? -52.783 39.269 -5.243 1.00 94.58 ? 555 ILE A CG1 1 ATOM 4286 C CG2 . ILE A 1 555 ? -50.630 40.394 -5.856 1.00 93.72 ? 555 ILE A CG2 1 ATOM 4287 C CD1 . ILE A 1 555 ? -53.504 39.682 -6.504 1.00 95.12 ? 555 ILE A CD1 1 ATOM 4288 N N . THR A 1 556 ? -48.820 40.205 -2.737 1.00 93.44 ? 556 THR A N 1 ATOM 4289 C CA . THR A 1 556 ? -47.738 41.008 -2.193 1.00 94.11 ? 556 THR A CA 1 ATOM 4290 C C . THR A 1 556 ? -46.895 41.607 -3.307 1.00 94.05 ? 556 THR A C 1 ATOM 4291 O O . THR A 1 556 ? -46.266 40.885 -4.080 1.00 93.98 ? 556 THR A O 1 ATOM 4292 C CB . THR A 1 556 ? -46.832 40.178 -1.260 1.00 103.99 ? 556 THR A CB 1 ATOM 4293 O OG1 . THR A 1 556 ? -47.602 39.684 -0.157 1.00 98.13 ? 556 THR A OG1 1 ATOM 4294 C CG2 . THR A 1 556 ? -45.688 41.028 -0.732 1.00 101.08 ? 556 THR A CG2 1 ATOM 4295 N N . ILE A 1 557 ? -46.886 42.933 -3.385 1.00 94.42 ? 557 ILE A N 1 ATOM 4296 C CA . ILE A 1 557 ? -46.035 43.627 -4.339 1.00 91.01 ? 557 ILE A CA 1 ATOM 4297 C C . ILE A 1 557 ? -44.662 43.833 -3.715 1.00 92.98 ? 557 ILE A C 1 ATOM 4298 O O . ILE A 1 557 ? -44.532 44.488 -2.681 1.00 91.59 ? 557 ILE A O 1 ATOM 4299 C CB . ILE A 1 557 ? -46.620 44.982 -4.764 1.00 97.57 ? 557 ILE A CB 1 ATOM 4300 C CG1 . ILE A 1 557 ? -47.951 44.793 -5.501 1.00 99.64 ? 557 ILE A CG1 1 ATOM 4301 C CG2 . ILE A 1 557 ? -45.633 45.724 -5.648 1.00 99.76 ? 557 ILE A CG2 1 ATOM 4302 C CD1 . ILE A 1 557 ? -49.170 44.761 -4.598 1.00 97.09 ? 557 ILE A CD1 1 ATOM 4303 N N . PHE A 1 558 ? -43.641 43.267 -4.349 1.00 91.98 ? 558 PHE A N 1 ATOM 4304 C CA . PHE A 1 558 ? -42.298 43.258 -3.784 1.00 90.12 ? 558 PHE A CA 1 ATOM 4305 C C . PHE A 1 558 ? -41.317 44.066 -4.621 1.00 95.58 ? 558 PHE A C 1 ATOM 4306 O O . PHE A 1 558 ? -41.123 43.791 -5.805 1.00 96.38 ? 558 PHE A O 1 ATOM 4307 C CB . PHE A 1 558 ? -41.803 41.817 -3.645 1.00 103.22 ? 558 PHE A CB 1 ATOM 4308 C CG . PHE A 1 558 ? -40.390 41.700 -3.145 1.00 114.66 ? 558 PHE A CG 1 ATOM 4309 C CD1 . PHE A 1 558 ? -40.106 41.813 -1.793 1.00 112.16 ? 558 PHE A CD1 1 ATOM 4310 C CD2 . PHE A 1 558 ? -39.347 41.458 -4.026 1.00 102.36 ? 558 PHE A CD2 1 ATOM 4311 C CE1 . PHE A 1 558 ? -38.809 41.695 -1.331 1.00 107.57 ? 558 PHE A CE1 1 ATOM 4312 C CE2 . PHE A 1 558 ? -38.050 41.341 -3.570 1.00 99.91 ? 558 PHE A CE2 1 ATOM 4313 C CZ . PHE A 1 558 ? -37.780 41.459 -2.221 1.00 108.08 ? 558 PHE A CZ 1 ATOM 4314 N N . MET A 1 559 ? -40.701 45.065 -3.998 1.00 102.85 ? 559 MET A N 1 ATOM 4315 C CA . MET A 1 559 ? -39.652 45.837 -4.650 1.00 97.34 ? 559 MET A CA 1 ATOM 4316 C C . MET A 1 559 ? -38.315 45.625 -3.962 1.00 94.40 ? 559 MET A C 1 ATOM 4317 O O . MET A 1 559 ? -38.215 45.751 -2.745 1.00 88.31 ? 559 MET A O 1 ATOM 4318 C CB . MET A 1 559 ? -39.987 47.331 -4.661 1.00 100.47 ? 559 MET A CB 1 ATOM 4319 C CG . MET A 1 559 ? -38.743 48.216 -4.689 1.00 117.66 ? 559 MET A CG 1 ATOM 4320 S SD . MET A 1 559 ? -39.017 49.934 -5.147 1.00 118.42 ? 559 MET A SD 1 ATOM 4321 C CE . MET A 1 559 ? -40.231 50.433 -3.934 1.00 106.85 ? 559 MET A CE 1 ATOM 4322 N N . GLU A 1 560 ? -37.294 45.298 -4.747 1.00 102.23 ? 560 GLU A N 1 ATOM 4323 C CA . GLU A 1 560 ? -35.922 45.270 -4.254 1.00 101.91 ? 560 GLU A CA 1 ATOM 4324 C C . GLU A 1 560 ? -35.039 46.077 -5.197 1.00 105.30 ? 560 GLU A C 1 ATOM 4325 O O . GLU A 1 560 ? -35.295 46.134 -6.400 1.00 105.76 ? 560 GLU A O 1 ATOM 4326 C CB . GLU A 1 560 ? -35.406 43.835 -4.122 1.00 105.18 ? 560 GLU A CB 1 ATOM 4327 C CG . GLU A 1 560 ? -35.348 43.058 -5.428 1.00 121.62 ? 560 GLU A CG 1 ATOM 4328 C CD . GLU A 1 560 ? -34.772 41.665 -5.251 1.00 132.80 ? 560 GLU A CD 1 ATOM 4329 O OE1 . GLU A 1 560 ? -34.229 41.378 -4.163 1.00 129.71 ? 560 GLU A OE1 1 ATOM 4330 O OE2 . GLU A 1 560 ? -34.865 40.857 -6.200 1.00 140.37 ? 560 GLU A OE2 1 ATOM 4331 N N . TYR A 1 561 ? -34.008 46.710 -4.651 1.00 115.68 ? 561 TYR A N 1 ATOM 4332 C CA . TYR A 1 561 ? -33.134 47.555 -5.456 1.00 119.83 ? 561 TYR A CA 1 ATOM 4333 C C . TYR A 1 561 ? -31.661 47.333 -5.131 1.00 122.10 ? 561 TYR A C 1 ATOM 4334 O O . TYR A 1 561 ? -31.286 47.168 -3.970 1.00 125.93 ? 561 TYR A O 1 ATOM 4335 C CB . TYR A 1 561 ? -33.497 49.032 -5.267 1.00 110.15 ? 561 TYR A CB 1 ATOM 4336 C CG . TYR A 1 561 ? -33.496 49.500 -3.826 1.00 102.19 ? 561 TYR A CG 1 ATOM 4337 C CD1 . TYR A 1 561 ? -32.355 50.046 -3.253 1.00 102.41 ? 561 TYR A CD1 1 ATOM 4338 C CD2 . TYR A 1 561 ? -34.639 49.402 -3.041 1.00 107.15 ? 561 TYR A CD2 1 ATOM 4339 C CE1 . TYR A 1 561 ? -32.349 50.476 -1.937 1.00 106.66 ? 561 TYR A CE1 1 ATOM 4340 C CE2 . TYR A 1 561 ? -34.643 49.829 -1.724 1.00 102.86 ? 561 TYR A CE2 1 ATOM 4341 C CZ . TYR A 1 561 ? -33.495 50.366 -1.178 1.00 112.62 ? 561 TYR A CZ 1 ATOM 4342 O OH . TYR A 1 561 ? -33.491 50.794 0.130 1.00 114.17 ? 561 TYR A OH 1 ATOM 4343 N N . ARG A 1 562 ? -30.832 47.321 -6.170 1.00 123.98 ? 562 ARG A N 1 ATOM 4344 C CA . ARG A 1 562 ? -29.387 47.232 -6.000 1.00 131.60 ? 562 ARG A CA 1 ATOM 4345 C C . ARG A 1 562 ? -28.725 48.497 -6.524 1.00 124.89 ? 562 ARG A C 1 ATOM 4346 O O . ARG A 1 562 ? -29.402 49.427 -6.960 1.00 131.15 ? 562 ARG A O 1 ATOM 4347 C CB . ARG A 1 562 ? -28.819 46.007 -6.719 1.00 137.39 ? 562 ARG A CB 1 ATOM 4348 C CG . ARG A 1 562 ? -28.936 46.068 -8.234 1.00 148.33 ? 562 ARG A CG 1 ATOM 4349 C CD . ARG A 1 562 ? -27.907 45.172 -8.909 1.00 154.47 ? 562 ARG A CD 1 ATOM 4350 N NE . ARG A 1 562 ? -27.982 43.790 -8.443 1.00 162.83 ? 562 ARG A NE 1 ATOM 4351 C CZ . ARG A 1 562 ? -27.219 42.804 -8.904 1.00 162.45 ? 562 ARG A CZ 1 ATOM 4352 N NH1 . ARG A 1 562 ? -26.320 43.046 -9.849 1.00 162.61 ? 562 ARG A NH1 1 ATOM 4353 N NH2 . ARG A 1 562 ? -27.354 41.576 -8.422 1.00 152.35 ? 562 ARG A NH2 1 ATOM 4354 N N . LEU A 1 563 ? -27.399 48.529 -6.480 1.00 116.30 ? 563 LEU A N 1 ATOM 4355 C CA . LEU A 1 563 ? -26.655 49.672 -6.987 1.00 118.50 ? 563 LEU A CA 1 ATOM 4356 C C . LEU A 1 563 ? -25.629 49.216 -8.018 1.00 126.49 ? 563 LEU A C 1 ATOM 4357 O O . LEU A 1 563 ? -24.681 48.506 -7.687 1.00 124.11 ? 563 LEU A O 1 ATOM 4358 C CB . LEU A 1 563 ? -25.967 50.413 -5.836 1.00 125.82 ? 563 LEU A CB 1 ATOM 4359 C CG . LEU A 1 563 ? -25.880 51.942 -5.882 1.00 119.06 ? 563 LEU A CG 1 ATOM 4360 C CD1 . LEU A 1 563 ? -25.289 52.478 -4.584 1.00 100.83 ? 563 LEU A CD1 1 ATOM 4361 C CD2 . LEU A 1 563 ? -25.069 52.424 -7.074 1.00 124.04 ? 563 LEU A CD2 1 ATOM 4362 N N . ASP A 1 564 ? -25.826 49.622 -9.269 1.00 145.76 ? 564 ASP A N 1 ATOM 4363 C CA . ASP A 1 564 ? -24.851 49.347 -10.318 1.00 161.19 ? 564 ASP A CA 1 ATOM 4364 C C . ASP A 1 564 ? -23.619 50.195 -10.044 1.00 172.81 ? 564 ASP A C 1 ATOM 4365 O O . ASP A 1 564 ? -23.738 51.408 -9.869 1.00 175.13 ? 564 ASP A O 1 ATOM 4366 C CB . ASP A 1 564 ? -25.431 49.648 -11.700 1.00 163.66 ? 564 ASP A CB 1 ATOM 4367 C CG . ASP A 1 564 ? -26.735 48.916 -11.957 1.00 172.58 ? 564 ASP A CG 1 ATOM 4368 O OD1 . ASP A 1 564 ? -26.914 47.806 -11.413 1.00 170.36 ? 564 ASP A OD1 1 ATOM 4369 O OD2 . ASP A 1 564 ? -27.582 49.453 -12.702 1.00 181.63 ? 564 ASP A OD2 1 ATOM 4370 N N . TYR A 1 565 ? -22.448 49.561 -9.997 1.00 180.13 ? 565 TYR A N 1 ATOM 4371 C CA . TYR A 1 565 ? -21.250 50.220 -9.478 1.00 181.40 ? 565 TYR A CA 1 ATOM 4372 C C . TYR A 1 565 ? -20.943 51.529 -10.207 1.00 183.83 ? 565 TYR A C 1 ATOM 4373 O O . TYR A 1 565 ? -21.194 52.599 -9.651 1.00 177.42 ? 565 TYR A O 1 ATOM 4374 C CB . TYR A 1 565 ? -20.039 49.267 -9.531 1.00 182.19 ? 565 TYR A CB 1 ATOM 4375 C CG . TYR A 1 565 ? -19.758 48.601 -10.868 1.00 184.97 ? 565 TYR A CG 1 ATOM 4376 C CD1 . TYR A 1 565 ? -20.563 47.571 -11.343 1.00 184.00 ? 565 TYR A CD1 1 ATOM 4377 C CD2 . TYR A 1 565 ? -18.662 48.978 -11.637 1.00 174.70 ? 565 TYR A CD2 1 ATOM 4378 C CE1 . TYR A 1 565 ? -20.302 46.959 -12.555 1.00 185.40 ? 565 TYR A CE1 1 ATOM 4379 C CE2 . TYR A 1 565 ? -18.395 48.372 -12.850 1.00 178.83 ? 565 TYR A CE2 1 ATOM 4380 C CZ . TYR A 1 565 ? -19.216 47.362 -13.303 1.00 186.53 ? 565 TYR A CZ 1 ATOM 4381 O OH . TYR A 1 565 ? -18.952 46.754 -14.509 1.00 192.14 ? 565 TYR A OH 1 ATOM 4382 N N . ARG A 1 566 ? -20.427 51.446 -11.434 1.00 190.19 ? 566 ARG A N 1 ATOM 4383 C CA . ARG A 1 566 ? -20.312 52.603 -12.324 1.00 190.49 ? 566 ARG A CA 1 ATOM 4384 C C . ARG A 1 566 ? -19.728 53.813 -11.603 1.00 189.51 ? 566 ARG A C 1 ATOM 4385 O O . ARG A 1 566 ? -18.547 53.837 -11.258 1.00 193.96 ? 566 ARG A O 1 ATOM 4386 C CB . ARG A 1 566 ? -21.652 52.951 -12.977 1.00 183.74 ? 566 ARG A CB 1 ATOM 4387 C CG . ARG A 1 566 ? -21.553 52.887 -14.502 1.00 185.05 ? 566 ARG A CG 1 ATOM 4388 C CD . ARG A 1 566 ? -22.748 53.470 -15.240 1.00 196.06 ? 566 ARG A CD 1 ATOM 4389 N NE . ARG A 1 566 ? -22.482 53.534 -16.677 1.00 201.33 ? 566 ARG A NE 1 ATOM 4390 C CZ . ARG A 1 566 ? -23.359 53.932 -17.594 1.00 196.22 ? 566 ARG A CZ 1 ATOM 4391 N NH1 . ARG A 1 566 ? -24.579 54.306 -17.235 1.00 189.38 ? 566 ARG A NH1 1 ATOM 4392 N NH2 . ARG A 1 566 ? -23.015 53.954 -18.875 1.00 195.04 ? 566 ARG A NH2 1 ATOM 4393 N N . THR A 1 567 ? -20.582 54.812 -11.399 1.00 188.10 ? 567 THR A N 1 ATOM 4394 C CA . THR A 1 567 ? -20.209 56.083 -10.790 1.00 185.22 ? 567 THR A CA 1 ATOM 4395 C C . THR A 1 567 ? -19.391 55.933 -9.508 1.00 164.56 ? 567 THR A C 1 ATOM 4396 O O . THR A 1 567 ? -19.684 55.095 -8.653 1.00 146.75 ? 567 THR A O 1 ATOM 4397 C CB . THR A 1 567 ? -21.461 56.919 -10.457 1.00 183.37 ? 567 THR A CB 1 ATOM 4398 O OG1 . THR A 1 567 ? -22.161 56.315 -9.361 1.00 183.73 ? 567 THR A OG1 1 ATOM 4399 C CG2 . THR A 1 567 ? -22.386 57.003 -11.661 1.00 170.52 ? 567 THR A CG2 1 ATOM 4400 N N . ALA A 1 568 ? -18.373 56.780 -9.398 1.00 158.41 ? 568 ALA A N 1 ATOM 4401 C CA . ALA A 1 568 ? -17.392 56.747 -8.322 1.00 147.16 ? 568 ALA A CA 1 ATOM 4402 C C . ALA A 1 568 ? -16.464 57.939 -8.511 1.00 155.76 ? 568 ALA A C 1 ATOM 4403 O O . ALA A 1 568 ? -16.555 58.642 -9.516 1.00 165.73 ? 568 ALA A O 1 ATOM 4404 C CB . ALA A 1 568 ? -16.609 55.442 -8.330 1.00 135.00 ? 568 ALA A CB 1 ATOM 4405 N N . ALA A 1 569 ? -15.573 58.171 -7.554 1.00 145.33 ? 569 ALA A N 1 ATOM 4406 C CA . ALA A 1 569 ? -14.734 59.364 -7.590 1.00 156.77 ? 569 ALA A CA 1 ATOM 4407 C C . ALA A 1 569 ? -13.535 59.207 -8.523 1.00 166.76 ? 569 ALA A C 1 ATOM 4408 O O . ALA A 1 569 ? -13.329 58.150 -9.122 1.00 166.65 ? 569 ALA A O 1 ATOM 4409 C CB . ALA A 1 569 ? -14.264 59.712 -6.186 1.00 146.67 ? 569 ALA A CB 1 ATOM 4410 N N . ASP A 1 570 ? -12.745 60.273 -8.631 1.00 170.38 ? 570 ASP A N 1 ATOM 4411 C CA . ASP A 1 570 ? -11.490 60.261 -9.381 1.00 181.62 ? 570 ASP A CA 1 ATOM 4412 C C . ASP A 1 570 ? -10.430 59.475 -8.615 1.00 195.37 ? 570 ASP A C 1 ATOM 4413 O O . ASP A 1 570 ? -9.306 59.296 -9.084 1.00 204.24 ? 570 ASP A O 1 ATOM 4414 C CB . ASP A 1 570 ? -11.005 61.685 -9.662 1.00 190.99 ? 570 ASP A CB 1 ATOM 4415 C CG . ASP A 1 570 ? -10.674 62.450 -8.397 1.00 193.26 ? 570 ASP A CG 1 ATOM 4416 O OD1 . ASP A 1 570 ? -11.342 62.219 -7.368 1.00 189.62 ? 570 ASP A OD1 1 ATOM 4417 O OD2 . ASP A 1 570 ? -9.744 63.284 -8.431 1.00 191.17 ? 570 ASP A OD2 1 ATOM 4418 N N . THR A 1 571 ? -10.815 59.010 -7.430 1.00 194.00 ? 571 THR A N 1 ATOM 4419 C CA . THR A 1 571 ? -9.956 58.242 -6.534 1.00 185.86 ? 571 THR A CA 1 ATOM 4420 C C . THR A 1 571 ? -9.508 56.911 -7.142 1.00 190.23 ? 571 THR A C 1 ATOM 4421 O O . THR A 1 571 ? -8.737 56.173 -6.525 1.00 193.13 ? 571 THR A O 1 ATOM 4422 C CB . THR A 1 571 ? -10.668 57.966 -5.198 1.00 171.33 ? 571 THR A CB 1 ATOM 4423 O OG1 . THR A 1 571 ? -11.990 57.479 -5.457 1.00 161.39 ? 571 THR A OG1 1 ATOM 4424 C CG2 . THR A 1 571 ? -10.762 59.240 -4.373 1.00 158.19 ? 571 THR A CG2 1 ATOM 4425 N N . THR A 1 572 ? -10.015 56.608 -8.336 1.00 188.70 ? 572 THR A N 1 ATOM 4426 C CA . THR A 1 572 ? -9.629 55.419 -9.093 1.00 183.82 ? 572 THR A CA 1 ATOM 4427 C C . THR A 1 572 ? -9.975 54.125 -8.365 1.00 174.34 ? 572 THR A C 1 ATOM 4428 O O . THR A 1 572 ? -9.104 53.441 -7.825 1.00 174.63 ? 572 THR A O 1 ATOM 4429 C CB . THR A 1 572 ? -8.118 55.421 -9.429 1.00 183.69 ? 572 THR A CB 1 ATOM 4430 O OG1 . THR A 1 572 ? -7.724 56.728 -9.864 1.00 195.11 ? 572 THR A OG1 1 ATOM 4431 C CG2 . THR A 1 572 ? -7.808 54.410 -10.525 1.00 179.74 ? 572 THR A CG2 1 ATOM 4432 N N . GLY A 1 573 ? -11.265 53.809 -8.340 1.00 156.49 ? 573 GLY A N 1 ATOM 4433 C CA . GLY A 1 573 ? -11.724 52.546 -7.799 1.00 148.02 ? 573 GLY A CA 1 ATOM 4434 C C . GLY A 1 573 ? -12.375 52.599 -6.433 1.00 148.52 ? 573 GLY A C 1 ATOM 4435 O O . GLY A 1 573 ? -12.554 51.560 -5.797 1.00 158.55 ? 573 GLY A O 1 ATOM 4436 N N . LEU A 1 574 ? -12.731 53.792 -5.968 1.00 135.95 ? 574 LEU A N 1 ATOM 4437 C CA . LEU A 1 574 ? -13.479 53.875 -4.722 1.00 136.08 ? 574 LEU A CA 1 ATOM 4438 C C . LEU A 1 574 ? -14.955 54.136 -5.012 1.00 125.62 ? 574 LEU A C 1 ATOM 4439 O O . LEU A 1 574 ? -15.351 55.255 -5.336 1.00 113.81 ? 574 LEU A O 1 ATOM 4440 C CB . LEU A 1 574 ? -12.905 54.977 -3.829 1.00 118.77 ? 574 LEU A CB 1 ATOM 4441 C CG . LEU A 1 574 ? -13.305 54.996 -2.354 1.00 108.43 ? 574 LEU A CG 1 ATOM 4442 C CD1 . LEU A 1 574 ? -12.618 53.865 -1.608 1.00 96.85 ? 574 LEU A CD1 1 ATOM 4443 C CD2 . LEU A 1 574 ? -12.971 56.341 -1.728 1.00 120.82 ? 574 LEU A CD2 1 ATOM 4444 N N . GLN A 1 575 ? -15.761 53.086 -4.887 1.00 119.74 ? 575 GLN A N 1 ATOM 4445 C CA . GLN A 1 575 ? -17.211 53.183 -5.017 1.00 117.39 ? 575 GLN A CA 1 ATOM 4446 C C . GLN A 1 575 ? -17.884 53.331 -3.655 1.00 109.24 ? 575 GLN A C 1 ATOM 4447 O O . GLN A 1 575 ? -17.357 52.858 -2.651 1.00 108.80 ? 575 GLN A O 1 ATOM 4448 C CB . GLN A 1 575 ? -17.758 51.965 -5.762 1.00 130.65 ? 575 GLN A CB 1 ATOM 4449 C CG . GLN A 1 575 ? -17.253 50.635 -5.241 1.00 148.29 ? 575 GLN A CG 1 ATOM 4450 C CD . GLN A 1 575 ? -17.595 49.486 -6.169 1.00 156.16 ? 575 GLN A CD 1 ATOM 4451 O OE1 . GLN A 1 575 ? -17.566 49.632 -7.392 1.00 147.35 ? 575 GLN A OE1 1 ATOM 4452 N NE2 . GLN A 1 575 ? -17.926 48.336 -5.592 1.00 150.24 ? 575 GLN A NE2 1 ATOM 4453 N N . PRO A 1 576 ? -19.053 53.987 -3.614 1.00 104.72 ? 576 PRO A N 1 ATOM 4454 C CA . PRO A 1 576 ? -19.793 54.129 -2.355 1.00 94.63 ? 576 PRO A CA 1 ATOM 4455 C C . PRO A 1 576 ? -20.324 52.800 -1.826 1.00 104.46 ? 576 PRO A C 1 ATOM 4456 O O . PRO A 1 576 ? -20.371 51.815 -2.561 1.00 104.36 ? 576 PRO A O 1 ATOM 4457 C CB . PRO A 1 576 ? -20.952 55.059 -2.729 1.00 95.09 ? 576 PRO A CB 1 ATOM 4458 C CG . PRO A 1 576 ? -20.507 55.756 -3.967 1.00 114.71 ? 576 PRO A CG 1 ATOM 4459 C CD . PRO A 1 576 ? -19.678 54.753 -4.704 1.00 117.80 ? 576 PRO A CD 1 ATOM 4460 N N . ILE A 1 577 ? -20.708 52.783 -0.554 1.00 116.00 ? 577 ILE A N 1 ATOM 4461 C CA . ILE A 1 577 ? -21.337 51.616 0.053 1.00 95.53 ? 577 ILE A CA 1 ATOM 4462 C C . ILE A 1 577 ? -22.682 52.022 0.650 1.00 94.73 ? 577 ILE A C 1 ATOM 4463 O O . ILE A 1 577 ? -22.812 53.100 1.232 1.00 112.43 ? 577 ILE A O 1 ATOM 4464 C CB . ILE A 1 577 ? -20.435 50.983 1.141 1.00 93.70 ? 577 ILE A CB 1 ATOM 4465 C CG1 . ILE A 1 577 ? -21.136 49.805 1.824 1.00 91.22 ? 577 ILE A CG1 1 ATOM 4466 C CG2 . ILE A 1 577 ? -20.014 52.025 2.167 1.00 119.29 ? 577 ILE A CG2 1 ATOM 4467 C CD1 . ILE A 1 577 ? -21.516 48.681 0.881 1.00 126.57 ? 577 ILE A CD1 1 ATOM 4468 N N . LEU A 1 578 ? -23.689 51.172 0.482 1.00 100.87 ? 578 LEU A N 1 ATOM 4469 C CA . LEU A 1 578 ? -25.000 51.435 1.061 1.00 96.36 ? 578 LEU A CA 1 ATOM 4470 C C . LEU A 1 578 ? -24.916 51.387 2.581 1.00 90.55 ? 578 LEU A C 1 ATOM 4471 O O . LEU A 1 578 ? -24.038 50.727 3.139 1.00 100.57 ? 578 LEU A O 1 ATOM 4472 C CB . LEU A 1 578 ? -26.038 50.431 0.552 1.00 100.79 ? 578 LEU A CB 1 ATOM 4473 C CG . LEU A 1 578 ? -26.439 50.501 -0.924 1.00 108.13 ? 578 LEU A CG 1 ATOM 4474 C CD1 . LEU A 1 578 ? -25.437 49.776 -1.817 1.00 121.16 ? 578 LEU A CD1 1 ATOM 4475 C CD2 . LEU A 1 578 ? -27.840 49.944 -1.121 1.00 111.49 ? 578 LEU A CD2 1 ATOM 4476 N N . ASN A 1 579 ? -25.832 52.090 3.241 1.00 87.42 ? 579 ASN A N 1 ATOM 4477 C CA . ASN A 1 579 ? -25.864 52.156 4.698 1.00 96.56 ? 579 ASN A CA 1 ATOM 4478 C C . ASN A 1 579 ? -25.916 50.763 5.320 1.00 104.07 ? 579 ASN A C 1 ATOM 4479 O O . ASN A 1 579 ? -26.563 49.862 4.786 1.00 87.31 ? 579 ASN A O 1 ATOM 4480 C CB . ASN A 1 579 ? -27.060 52.991 5.161 1.00 105.18 ? 579 ASN A CB 1 ATOM 4481 C CG . ASN A 1 579 ? -27.047 53.255 6.653 1.00 113.55 ? 579 ASN A CG 1 ATOM 4482 O OD1 . ASN A 1 579 ? -26.494 54.253 7.112 1.00 100.85 ? 579 ASN A OD1 1 ATOM 4483 N ND2 . ASN A 1 579 ? -27.664 52.360 7.418 1.00 126.03 ? 579 ASN A ND2 1 ATOM 4484 N N . GLN A 1 580 ? -25.215 50.596 6.439 1.00 112.00 ? 580 GLN A N 1 ATOM 4485 C CA . GLN A 1 580 ? -25.071 49.297 7.091 1.00 100.30 ? 580 GLN A CA 1 ATOM 4486 C C . GLN A 1 580 ? -26.411 48.625 7.359 1.00 107.12 ? 580 GLN A C 1 ATOM 4487 O O . GLN A 1 580 ? -26.749 47.619 6.735 1.00 103.35 ? 580 GLN A O 1 ATOM 4488 C CB . GLN A 1 580 ? -24.304 49.449 8.404 1.00 107.36 ? 580 GLN A CB 1 ATOM 4489 C CG . GLN A 1 580 ? -24.018 48.137 9.113 1.00 104.50 ? 580 GLN A CG 1 ATOM 4490 C CD . GLN A 1 580 ? -23.434 48.344 10.495 1.00 118.71 ? 580 GLN A CD 1 ATOM 4491 O OE1 . GLN A 1 580 ? -23.533 49.430 11.068 1.00 120.56 ? 580 GLN A OE1 1 ATOM 4492 N NE2 . GLN A 1 580 ? -22.818 47.300 11.039 1.00 128.27 ? 580 GLN A NE2 1 ATOM 4493 N N . PHE A 1 581 ? -27.179 49.187 8.285 1.00 121.70 ? 581 PHE A N 1 ATOM 4494 C CA . PHE A 1 581 ? -28.481 48.628 8.605 1.00 122.70 ? 581 PHE A CA 1 ATOM 4495 C C . PHE A 1 581 ? -29.585 49.436 7.943 1.00 140.90 ? 581 PHE A C 1 ATOM 4496 O O . PHE A 1 581 ? -29.878 50.562 8.348 1.00 139.99 ? 581 PHE A O 1 ATOM 4497 C CB . PHE A 1 581 ? -28.693 48.574 10.119 1.00 128.26 ? 581 PHE A CB 1 ATOM 4498 C CG . PHE A 1 581 ? -27.717 47.686 10.836 1.00 136.21 ? 581 PHE A CG 1 ATOM 4499 C CD1 . PHE A 1 581 ? -27.646 46.333 10.544 1.00 136.57 ? 581 PHE A CD1 1 ATOM 4500 C CD2 . PHE A 1 581 ? -26.876 48.200 11.810 1.00 129.59 ? 581 PHE A CD2 1 ATOM 4501 C CE1 . PHE A 1 581 ? -26.750 45.512 11.203 1.00 133.68 ? 581 PHE A CE1 1 ATOM 4502 C CE2 . PHE A 1 581 ? -25.979 47.383 12.474 1.00 124.28 ? 581 PHE A CE2 1 ATOM 4503 C CZ . PHE A 1 581 ? -25.915 46.037 12.170 1.00 116.03 ? 581 PHE A CZ 1 ATOM 4504 N N . THR A 1 582 ? -30.198 48.828 6.933 1.00 148.94 ? 582 THR A N 1 ATOM 4505 C CA . THR A 1 582 ? -31.294 49.422 6.178 1.00 141.51 ? 582 THR A CA 1 ATOM 4506 C C . THR A 1 582 ? -31.783 48.407 5.151 1.00 126.79 ? 582 THR A C 1 ATOM 4507 O O . THR A 1 582 ? -30.981 47.718 4.518 1.00 116.62 ? 582 THR A O 1 ATOM 4508 C CB . THR A 1 582 ? -30.883 50.733 5.463 1.00 134.73 ? 582 THR A CB 1 ATOM 4509 O OG1 . THR A 1 582 ? -31.973 51.207 4.663 1.00 144.53 ? 582 THR A OG1 1 ATOM 4510 C CG2 . THR A 1 582 ? -29.670 50.514 4.574 1.00 121.53 ? 582 THR A CG2 1 ATOM 4511 N N . PRO A 1 583 ? -33.109 48.301 4.997 1.00 122.46 ? 583 PRO A N 1 ATOM 4512 C CA . PRO A 1 583 ? -33.700 47.315 4.088 1.00 119.23 ? 583 PRO A CA 1 ATOM 4513 C C . PRO A 1 583 ? -33.399 47.620 2.625 1.00 107.75 ? 583 PRO A C 1 ATOM 4514 O O . PRO A 1 583 ? -33.512 48.767 2.196 1.00 103.40 ? 583 PRO A O 1 ATOM 4515 C CB . PRO A 1 583 ? -35.202 47.431 4.371 1.00 133.28 ? 583 PRO A CB 1 ATOM 4516 C CG . PRO A 1 583 ? -35.293 48.068 5.723 1.00 121.07 ? 583 PRO A CG 1 ATOM 4517 C CD . PRO A 1 583 ? -34.133 49.004 5.787 1.00 114.77 ? 583 PRO A CD 1 ATOM 4518 N N . ALA A 1 584 ? -33.018 46.594 1.874 1.00 108.34 ? 584 ALA A N 1 ATOM 4519 C CA . ALA A 1 584 ? -32.779 46.744 0.445 1.00 119.27 ? 584 ALA A CA 1 ATOM 4520 C C . ALA A 1 584 ? -34.057 46.447 -0.327 1.00 117.08 ? 584 ALA A C 1 ATOM 4521 O O . ALA A 1 584 ? -34.097 46.564 -1.552 1.00 103.69 ? 584 ALA A O 1 ATOM 4522 C CB . ALA A 1 584 ? -31.653 45.831 -0.009 1.00 134.80 ? 584 ALA A CB 1 ATOM 4523 N N . ASN A 1 585 ? -35.100 46.060 0.399 1.00 114.61 ? 585 ASN A N 1 ATOM 4524 C CA . ASN A 1 585 ? -36.374 45.739 -0.225 1.00 101.18 ? 585 ASN A CA 1 ATOM 4525 C C . ASN A 1 585 ? -37.574 46.110 0.642 1.00 101.24 ? 585 ASN A C 1 ATOM 4526 O O . ASN A 1 585 ? -37.512 46.047 1.870 1.00 114.31 ? 585 ASN A O 1 ATOM 4527 C CB . ASN A 1 585 ? -36.426 44.253 -0.582 1.00 108.50 ? 585 ASN A CB 1 ATOM 4528 C CG . ASN A 1 585 ? -36.417 43.353 0.637 1.00 128.56 ? 585 ASN A CG 1 ATOM 4529 O OD1 . ASN A 1 585 ? -37.434 43.194 1.313 1.00 125.83 ? 585 ASN A OD1 1 ATOM 4530 N ND2 . ASN A 1 585 ? -35.270 42.748 0.920 1.00 159.46 ? 585 ASN A ND2 1 ATOM 4531 N N . ILE A 1 586 ? -38.664 46.494 -0.015 1.00 90.54 ? 586 ILE A N 1 ATOM 4532 C CA . ILE A 1 586 ? -39.891 46.900 0.664 1.00 87.39 ? 586 ILE A CA 1 ATOM 4533 C C . ILE A 1 586 ? -41.096 46.215 0.022 1.00 93.18 ? 586 ILE A C 1 ATOM 4534 O O . ILE A 1 586 ? -41.137 46.033 -1.195 1.00 95.17 ? 586 ILE A O 1 ATOM 4535 C CB . ILE A 1 586 ? -40.068 48.433 0.622 1.00 94.31 ? 586 ILE A CB 1 ATOM 4536 C CG1 . ILE A 1 586 ? -41.404 48.856 1.235 1.00 101.96 ? 586 ILE A CG1 1 ATOM 4537 C CG2 . ILE A 1 586 ? -39.961 48.939 -0.801 1.00 87.56 ? 586 ILE A CG2 1 ATOM 4538 C CD1 . ILE A 1 586 ? -41.728 50.327 1.038 1.00 92.98 ? 586 ILE A CD1 1 ATOM 4539 N N . SER A 1 587 ? -42.068 45.824 0.842 1.00 104.70 ? 587 SER A N 1 ATOM 4540 C CA . SER A 1 587 ? -43.235 45.102 0.347 1.00 107.47 ? 587 SER A CA 1 ATOM 4541 C C . SER A 1 587 ? -44.553 45.795 0.688 1.00 99.35 ? 587 SER A C 1 ATOM 4542 O O . SER A 1 587 ? -44.714 46.360 1.769 1.00 97.46 ? 587 SER A O 1 ATOM 4543 C CB . SER A 1 587 ? -43.250 43.675 0.904 1.00 111.06 ? 587 SER A CB 1 ATOM 4544 O OG . SER A 1 587 ? -42.084 42.964 0.525 1.00 113.17 ? 587 SER A OG 1 ATOM 4545 N N . ARG A 1 588 ? -45.487 45.748 -0.256 1.00 100.09 ? 588 ARG A N 1 ATOM 4546 C CA . ARG A 1 588 ? -46.855 46.198 -0.030 1.00 96.21 ? 588 ARG A CA 1 ATOM 4547 C C . ARG A 1 588 ? -47.804 45.076 -0.420 1.00 95.79 ? 588 ARG A C 1 ATOM 4548 O O . ARG A 1 588 ? -47.421 44.157 -1.145 1.00 93.67 ? 588 ARG A O 1 ATOM 4549 C CB . ARG A 1 588 ? -47.162 47.463 -0.831 1.00 100.11 ? 588 ARG A CB 1 ATOM 4550 C CG . ARG A 1 588 ? -46.456 48.710 -0.333 1.00 109.78 ? 588 ARG A CG 1 ATOM 4551 C CD . ARG A 1 588 ? -47.022 49.171 0.998 1.00 114.61 ? 588 ARG A CD 1 ATOM 4552 N NE . ARG A 1 588 ? -46.013 49.154 2.051 1.00 117.88 ? 588 ARG A NE 1 ATOM 4553 C CZ . ARG A 1 588 ? -45.155 50.142 2.279 1.00 124.88 ? 588 ARG A CZ 1 ATOM 4554 N NH1 . ARG A 1 588 ? -45.179 51.234 1.525 1.00 125.66 ? 588 ARG A NH1 1 ATOM 4555 N NH2 . ARG A 1 588 ? -44.270 50.039 3.260 1.00 127.22 ? 588 ARG A NH2 1 ATOM 4556 N N . GLN A 1 589 ? -49.042 45.143 0.057 1.00 97.18 ? 589 GLN A N 1 ATOM 4557 C CA . GLN A 1 589 ? -49.992 44.072 -0.211 1.00 94.35 ? 589 GLN A CA 1 ATOM 4558 C C . GLN A 1 589 ? -51.349 44.578 -0.682 1.00 100.09 ? 589 GLN A C 1 ATOM 4559 O O . GLN A 1 589 ? -52.004 45.371 -0.005 1.00 99.45 ? 589 GLN A O 1 ATOM 4560 C CB . GLN A 1 589 ? -50.171 43.203 1.034 1.00 90.54 ? 589 GLN A CB 1 ATOM 4561 C CG . GLN A 1 589 ? -48.932 42.416 1.411 1.00 97.51 ? 589 GLN A CG 1 ATOM 4562 C CD . GLN A 1 589 ? -49.172 41.489 2.578 1.00 111.71 ? 589 GLN A CD 1 ATOM 4563 O OE1 . GLN A 1 589 ? -50.282 41.415 3.106 1.00 115.33 ? 589 GLN A OE1 1 ATOM 4564 N NE2 . GLN A 1 589 ? -48.132 40.770 2.989 1.00 110.53 ? 589 GLN A NE2 1 ATOM 4565 N N . ALA A 1 590 ? -51.759 44.107 -1.855 1.00 110.06 ? 590 ALA A N 1 ATOM 4566 C CA . ALA A 1 590 ? -53.101 44.353 -2.360 1.00 93.76 ? 590 ALA A CA 1 ATOM 4567 C C . ALA A 1 590 ? -53.999 43.178 -2.001 1.00 93.14 ? 590 ALA A C 1 ATOM 4568 O O . ALA A 1 590 ? -53.552 42.031 -1.992 1.00 92.48 ? 590 ALA A O 1 ATOM 4569 C CB . ALA A 1 590 ? -53.082 44.574 -3.863 1.00 93.46 ? 590 ALA A CB 1 ATOM 4570 N N . HIS A 1 591 ? -55.258 43.467 -1.690 1.00 101.67 ? 591 HIS A N 1 ATOM 4571 C CA . HIS A 1 591 ? -56.217 42.422 -1.348 1.00 99.95 ? 591 HIS A CA 1 ATOM 4572 C C . HIS A 1 591 ? -57.388 42.406 -2.320 1.00 101.48 ? 591 HIS A C 1 ATOM 4573 O O . HIS A 1 591 ? -57.903 43.455 -2.702 1.00 102.82 ? 591 HIS A O 1 ATOM 4574 C CB . HIS A 1 591 ? -56.736 42.610 0.079 1.00 95.69 ? 591 HIS A CB 1 ATOM 4575 C CG . HIS A 1 591 ? -55.674 42.509 1.128 1.00 101.60 ? 591 HIS A CG 1 ATOM 4576 N ND1 . HIS A 1 591 ? -54.747 43.505 1.348 1.00 117.45 ? 591 HIS A ND1 1 ATOM 4577 C CD2 . HIS A 1 591 ? -55.390 41.529 2.018 1.00 110.40 ? 591 HIS A CD2 1 ATOM 4578 C CE1 . HIS A 1 591 ? -53.940 43.145 2.329 1.00 120.83 ? 591 HIS A CE1 1 ATOM 4579 N NE2 . HIS A 1 591 ? -54.308 41.949 2.753 1.00 128.19 ? 591 HIS A NE2 1 ATOM 4580 N N . ILE A 1 592 ? -57.804 41.210 -2.722 1.00 103.04 ? 592 ILE A N 1 ATOM 4581 C CA . ILE A 1 592 ? -58.997 41.057 -3.544 1.00 102.25 ? 592 ILE A CA 1 ATOM 4582 C C . ILE A 1 592 ? -60.231 41.260 -2.669 1.00 101.20 ? 592 ILE A C 1 ATOM 4583 O O . ILE A 1 592 ? -60.257 40.830 -1.515 1.00 102.51 ? 592 ILE A O 1 ATOM 4584 C CB . ILE A 1 592 ? -59.047 39.671 -4.223 1.00 106.73 ? 592 ILE A CB 1 ATOM 4585 C CG1 . ILE A 1 592 ? -57.776 39.429 -5.039 1.00 103.54 ? 592 ILE A CG1 1 ATOM 4586 C CG2 . ILE A 1 592 ? -60.271 39.548 -5.112 1.00 120.52 ? 592 ILE A CG2 1 ATOM 4587 C CD1 . ILE A 1 592 ? -57.784 38.127 -5.811 1.00 96.18 ? 592 ILE A CD1 1 ATOM 4588 N N . LEU A 1 593 ? -61.250 41.918 -3.212 1.00 98.05 ? 593 LEU A N 1 ATOM 4589 C CA . LEU A 1 593 ? -62.450 42.219 -2.441 1.00 100.81 ? 593 LEU A CA 1 ATOM 4590 C C . LEU A 1 593 ? -63.290 40.961 -2.251 1.00 104.39 ? 593 LEU A C 1 ATOM 4591 O O . LEU A 1 593 ? -63.739 40.353 -3.222 1.00 110.06 ? 593 LEU A O 1 ATOM 4592 C CB . LEU A 1 593 ? -63.268 43.315 -3.139 1.00 103.72 ? 593 LEU A CB 1 ATOM 4593 C CG . LEU A 1 593 ? -64.525 43.900 -2.483 1.00 111.05 ? 593 LEU A CG 1 ATOM 4594 C CD1 . LEU A 1 593 ? -64.759 45.313 -2.985 1.00 105.07 ? 593 LEU A CD1 1 ATOM 4595 C CD2 . LEU A 1 593 ? -65.761 43.049 -2.756 1.00 135.25 ? 593 LEU A CD2 1 ATOM 4596 N N . LEU A 1 594 ? -63.505 40.585 -0.994 1.00 108.37 ? 594 LEU A N 1 ATOM 4597 C CA . LEU A 1 594 ? -64.318 39.420 -0.661 1.00 107.80 ? 594 LEU A CA 1 ATOM 4598 C C . LEU A 1 594 ? -65.133 39.671 0.607 1.00 110.01 ? 594 LEU A C 1 ATOM 4599 O O . LEU A 1 594 ? -64.581 40.073 1.632 1.00 115.93 ? 594 LEU A O 1 ATOM 4600 C CB . LEU A 1 594 ? -63.428 38.186 -0.483 1.00 108.32 ? 594 LEU A CB 1 ATOM 4601 C CG . LEU A 1 594 ? -63.941 36.797 -0.879 1.00 108.98 ? 594 LEU A CG 1 ATOM 4602 C CD1 . LEU A 1 594 ? -62.895 35.746 -0.547 1.00 122.70 ? 594 LEU A CD1 1 ATOM 4603 C CD2 . LEU A 1 594 ? -65.251 36.456 -0.202 1.00 110.16 ? 594 LEU A CD2 1 ATOM 4604 N N . ASP A 1 595 ? -66.436 39.408 0.536 1.00 114.51 ? 595 ASP A N 1 ATOM 4605 C CA . ASP A 1 595 ? -67.326 39.507 1.693 1.00 120.62 ? 595 ASP A CA 1 ATOM 4606 C C . ASP A 1 595 ? -67.234 40.850 2.416 1.00 116.89 ? 595 ASP A C 1 ATOM 4607 O O . ASP A 1 595 ? -67.166 40.896 3.644 1.00 117.74 ? 595 ASP A O 1 ATOM 4608 C CB . ASP A 1 595 ? -67.032 38.373 2.681 1.00 121.94 ? 595 ASP A CB 1 ATOM 4609 C CG . ASP A 1 595 ? -67.703 37.068 2.290 1.00 126.38 ? 595 ASP A CG 1 ATOM 4610 O OD1 . ASP A 1 595 ? -68.868 37.109 1.837 1.00 107.86 ? 595 ASP A OD1 1 ATOM 4611 O OD2 . ASP A 1 595 ? -67.068 36.002 2.440 1.00 133.09 ? 595 ASP A OD2 1 ATOM 4612 N N . CYS A 1 596 ? -67.227 41.939 1.654 1.00 123.87 ? 596 CYS A N 1 ATOM 4613 C CA . CYS A 1 596 ? -67.138 43.276 2.237 1.00 131.67 ? 596 CYS A CA 1 ATOM 4614 C C . CYS A 1 596 ? -68.509 43.927 2.401 1.00 128.58 ? 596 CYS A C 1 ATOM 4615 O O . CYS A 1 596 ? -68.616 45.071 2.849 1.00 121.99 ? 596 CYS A O 1 ATOM 4616 C CB . CYS A 1 596 ? -66.229 44.168 1.391 1.00 121.57 ? 596 CYS A CB 1 ATOM 4617 S SG . CYS A 1 596 ? -64.468 43.781 1.555 1.00 172.84 ? 596 CYS A SG 1 ATOM 4618 N N . GLY A 1 597 ? -69.555 43.193 2.039 1.00 134.31 ? 597 GLY A N 1 ATOM 4619 C CA . GLY A 1 597 ? -70.910 43.691 2.167 1.00 141.23 ? 597 GLY A CA 1 ATOM 4620 C C . GLY A 1 597 ? -71.361 44.476 0.952 1.00 145.32 ? 597 GLY A C 1 ATOM 4621 O O . GLY A 1 597 ? -70.671 44.516 -0.067 1.00 142.33 ? 597 GLY A O 1 ATOM 4622 N N . GLU A 1 598 ? -72.524 45.109 1.066 1.00 152.36 ? 598 GLU A N 1 ATOM 4623 C CA . GLU A 1 598 ? -73.102 45.864 -0.039 1.00 157.49 ? 598 GLU A CA 1 ATOM 4624 C C . GLU A 1 598 ? -72.367 47.183 -0.269 1.00 155.56 ? 598 GLU A C 1 ATOM 4625 O O . GLU A 1 598 ? -72.432 47.753 -1.357 1.00 159.78 ? 598 GLU A O 1 ATOM 4626 C CB . GLU A 1 598 ? -74.590 46.130 0.215 1.00 161.04 ? 598 GLU A CB 1 ATOM 4627 C CG . GLU A 1 598 ? -74.879 47.255 1.205 1.00 172.77 ? 598 GLU A CG 1 ATOM 4628 C CD . GLU A 1 598 ? -74.373 46.962 2.607 1.00 178.28 ? 598 GLU A CD 1 ATOM 4629 O OE1 . GLU A 1 598 ? -74.251 45.771 2.963 1.00 177.76 ? 598 GLU A OE1 1 ATOM 4630 O OE2 . GLU A 1 598 ? -74.094 47.926 3.351 1.00 179.76 ? 598 GLU A OE2 1 ATOM 4631 N N . ASP A 1 599 ? -71.666 47.662 0.755 1.00 124.21 ? 599 ASP A N 1 ATOM 4632 C CA . ASP A 1 599 ? -70.940 48.925 0.658 1.00 118.93 ? 599 ASP A CA 1 ATOM 4633 C C . ASP A 1 599 ? -69.634 48.762 -0.114 1.00 112.83 ? 599 ASP A C 1 ATOM 4634 O O . ASP A 1 599 ? -68.972 49.747 -0.442 1.00 109.50 ? 599 ASP A O 1 ATOM 4635 C CB . ASP A 1 599 ? -70.662 49.496 2.055 1.00 107.90 ? 599 ASP A CB 1 ATOM 4636 C CG . ASP A 1 599 ? -70.005 48.489 2.986 1.00 137.68 ? 599 ASP A CG 1 ATOM 4637 O OD1 . ASP A 1 599 ? -69.404 47.511 2.493 1.00 148.33 ? 599 ASP A OD1 1 ATOM 4638 O OD2 . ASP A 1 599 ? -70.085 48.680 4.218 1.00 145.30 ? 599 ASP A OD2 1 ATOM 4639 N N . ASN A 1 600 ? -69.273 47.510 -0.386 1.00 125.15 ? 600 ASN A N 1 ATOM 4640 C CA . ASN A 1 600 ? -68.037 47.166 -1.087 1.00 131.53 ? 600 ASN A CA 1 ATOM 4641 C C . ASN A 1 600 ? -66.794 47.703 -0.384 1.00 129.24 ? 600 ASN A C 1 ATOM 4642 O O . ASN A 1 600 ? -65.762 47.936 -1.013 1.00 135.54 ? 600 ASN A O 1 ATOM 4643 C CB . ASN A 1 600 ? -68.081 47.667 -2.533 1.00 126.28 ? 600 ASN A CB 1 ATOM 4644 C CG . ASN A 1 600 ? -69.065 46.891 -3.387 1.00 140.29 ? 600 ASN A CG 1 ATOM 4645 O OD1 . ASN A 1 600 ? -69.281 45.697 -3.176 1.00 126.82 ? 600 ASN A OD1 1 ATOM 4646 N ND2 . ASN A 1 600 ? -69.667 47.566 -4.358 1.00 149.52 ? 600 ASN A ND2 1 ATOM 4647 N N . VAL A 1 601 ? -66.906 47.895 0.926 1.00 115.76 ? 601 VAL A N 1 ATOM 4648 C CA . VAL A 1 601 ? -65.770 48.259 1.763 1.00 102.29 ? 601 VAL A CA 1 ATOM 4649 C C . VAL A 1 601 ? -65.855 47.471 3.063 1.00 108.77 ? 601 VAL A C 1 ATOM 4650 O O . VAL A 1 601 ? -66.947 47.246 3.590 1.00 101.45 ? 601 VAL A O 1 ATOM 4651 C CB . VAL A 1 601 ? -65.721 49.774 2.069 1.00 100.30 ? 601 VAL A CB 1 ATOM 4652 C CG1 . VAL A 1 601 ? -65.370 50.566 0.816 1.00 104.81 ? 601 VAL A CG1 1 ATOM 4653 C CG2 . VAL A 1 601 ? -67.038 50.251 2.664 1.00 112.51 ? 601 VAL A CG2 1 ATOM 4654 N N . CYS A 1 602 ? -64.708 47.039 3.574 1.00 100.94 ? 602 CYS A N 1 ATOM 4655 C CA . CYS A 1 602 ? -64.696 46.224 4.781 1.00 86.82 ? 602 CYS A CA 1 ATOM 4656 C C . CYS A 1 602 ? -64.498 47.074 6.026 1.00 106.07 ? 602 CYS A C 1 ATOM 4657 O O . CYS A 1 602 ? -63.424 47.634 6.250 1.00 124.30 ? 602 CYS A O 1 ATOM 4658 C CB . CYS A 1 602 ? -63.612 45.148 4.692 1.00 82.64 ? 602 CYS A CB 1 ATOM 4659 S SG . CYS A 1 602 ? -63.999 43.805 3.532 1.00 120.20 ? 602 CYS A SG 1 ATOM 4660 N N . LYS A 1 603 ? -65.550 47.166 6.831 1.00 97.51 ? 603 LYS A N 1 ATOM 4661 C CA . LYS A 1 603 ? -65.488 47.874 8.099 1.00 108.95 ? 603 LYS A CA 1 ATOM 4662 C C . LYS A 1 603 ? -65.673 46.884 9.238 1.00 117.10 ? 603 LYS A C 1 ATOM 4663 O O . LYS A 1 603 ? -66.776 46.384 9.456 1.00 125.94 ? 603 LYS A O 1 ATOM 4664 C CB . LYS A 1 603 ? -66.554 48.971 8.166 1.00 108.24 ? 603 LYS A CB 1 ATOM 4665 C CG . LYS A 1 603 ? -66.385 50.070 7.129 1.00 125.14 ? 603 LYS A CG 1 ATOM 4666 C CD . LYS A 1 603 ? -67.534 51.066 7.182 1.00 141.60 ? 603 LYS A CD 1 ATOM 4667 C CE . LYS A 1 603 ? -68.856 50.404 6.825 1.00 143.40 ? 603 LYS A CE 1 ATOM 4668 N NZ . LYS A 1 603 ? -69.982 51.380 6.807 1.00 143.63 ? 603 LYS A NZ 1 ATOM 4669 N N . PRO A 1 604 ? -64.589 46.589 9.966 1.00 118.96 ? 604 PRO A N 1 ATOM 4670 C CA . PRO A 1 604 ? -64.678 45.638 11.073 1.00 112.19 ? 604 PRO A CA 1 ATOM 4671 C C . PRO A 1 604 ? -64.996 46.309 12.400 1.00 114.03 ? 604 PRO A C 1 ATOM 4672 O O . PRO A 1 604 ? -65.085 47.533 12.476 1.00 118.65 ? 604 PRO A O 1 ATOM 4673 C CB . PRO A 1 604 ? -63.277 45.017 11.107 1.00 80.72 ? 604 PRO A CB 1 ATOM 4674 C CG . PRO A 1 604 ? -62.368 46.035 10.434 1.00 77.29 ? 604 PRO A CG 1 ATOM 4675 C CD . PRO A 1 604 ? -63.224 47.117 9.815 1.00 91.59 ? 604 PRO A CD 1 ATOM 4676 N N . LYS A 1 605 ? -65.172 45.498 13.436 1.00 107.76 ? 605 LYS A N 1 ATOM 4677 C CA . LYS A 1 605 ? -65.185 45.997 14.800 1.00 130.87 ? 605 LYS A CA 1 ATOM 4678 C C . LYS A 1 605 ? -64.228 45.137 15.610 1.00 134.64 ? 605 LYS A C 1 ATOM 4679 O O . LYS A 1 605 ? -64.473 43.950 15.828 1.00 102.10 ? 605 LYS A O 1 ATOM 4680 C CB . LYS A 1 605 ? -66.594 45.971 15.395 1.00 114.15 ? 605 LYS A CB 1 ATOM 4681 C CG . LYS A 1 605 ? -66.719 46.696 16.727 1.00 130.26 ? 605 LYS A CG 1 ATOM 4682 C CD . LYS A 1 605 ? -68.154 46.691 17.231 1.00 119.98 ? 605 LYS A CD 1 ATOM 4683 C CE . LYS A 1 605 ? -68.593 45.295 17.638 1.00 124.36 ? 605 LYS A CE 1 ATOM 4684 N NZ . LYS A 1 605 ? -67.777 44.765 18.766 1.00 124.80 ? 605 LYS A NZ 1 ATOM 4685 N N . LEU A 1 606 ? -63.134 45.740 16.053 1.00 131.34 ? 606 LEU A N 1 ATOM 4686 C CA . LEU A 1 606 ? -62.092 44.993 16.734 1.00 123.53 ? 606 LEU A CA 1 ATOM 4687 C C . LEU A 1 606 ? -62.190 45.207 18.236 1.00 127.42 ? 606 LEU A C 1 ATOM 4688 O O . LEU A 1 606 ? -62.492 46.307 18.698 1.00 125.05 ? 606 LEU A O 1 ATOM 4689 C CB . LEU A 1 606 ? -60.721 45.406 16.205 1.00 114.39 ? 606 LEU A CB 1 ATOM 4690 C CG . LEU A 1 606 ? -60.591 45.266 14.687 1.00 92.74 ? 606 LEU A CG 1 ATOM 4691 C CD1 . LEU A 1 606 ? -59.350 45.977 14.178 1.00 117.31 ? 606 LEU A CD1 1 ATOM 4692 C CD2 . LEU A 1 606 ? -60.568 43.799 14.299 1.00 76.18 ? 606 LEU A CD2 1 ATOM 4693 N N . GLU A 1 607 ? -61.948 44.144 18.994 1.00 120.52 ? 607 GLU A N 1 ATOM 4694 C CA . GLU A 1 607 ? -62.130 44.185 20.438 1.00 121.95 ? 607 GLU A CA 1 ATOM 4695 C C . GLU A 1 607 ? -61.041 43.408 21.166 1.00 117.13 ? 607 GLU A C 1 ATOM 4696 O O . GLU A 1 607 ? -60.719 42.279 20.797 1.00 107.24 ? 607 GLU A O 1 ATOM 4697 C CB . GLU A 1 607 ? -63.510 43.635 20.801 1.00 134.01 ? 607 GLU A CB 1 ATOM 4698 C CG . GLU A 1 607 ? -63.848 43.684 22.279 1.00 144.40 ? 607 GLU A CG 1 ATOM 4699 C CD . GLU A 1 607 ? -65.288 43.296 22.550 1.00 160.15 ? 607 GLU A CD 1 ATOM 4700 O OE1 . GLU A 1 607 ? -65.580 42.830 23.671 1.00 164.06 ? 607 GLU A OE1 1 ATOM 4701 O OE2 . GLU A 1 607 ? -66.130 43.458 21.639 1.00 156.12 ? 607 GLU A OE2 1 ATOM 4702 N N . VAL A 1 608 ? -60.473 44.023 22.197 1.00 123.38 ? 608 VAL A N 1 ATOM 4703 C CA . VAL A 1 608 ? -59.448 43.376 23.005 1.00 116.56 ? 608 VAL A CA 1 ATOM 4704 C C . VAL A 1 608 ? -59.927 43.217 24.441 1.00 115.36 ? 608 VAL A C 1 ATOM 4705 O O . VAL A 1 608 ? -60.479 44.147 25.027 1.00 108.00 ? 608 VAL A O 1 ATOM 4706 C CB . VAL A 1 608 ? -58.131 44.168 23.004 1.00 114.53 ? 608 VAL A CB 1 ATOM 4707 C CG1 . VAL A 1 608 ? -56.997 43.300 23.520 1.00 118.02 ? 608 VAL A CG1 1 ATOM 4708 C CG2 . VAL A 1 608 ? -57.818 44.673 21.611 1.00 115.28 ? 608 VAL A CG2 1 ATOM 4709 N N . SER A 1 609 ? -59.713 42.034 25.006 1.00 117.44 ? 609 SER A N 1 ATOM 4710 C CA . SER A 1 609 ? -60.141 41.755 26.369 1.00 121.38 ? 609 SER A CA 1 ATOM 4711 C C . SER A 1 609 ? -59.076 40.957 27.111 1.00 130.70 ? 609 SER A C 1 ATOM 4712 O O . SER A 1 609 ? -58.535 39.989 26.578 1.00 136.74 ? 609 SER A O 1 ATOM 4713 C CB . SER A 1 609 ? -61.473 40.999 26.365 1.00 120.92 ? 609 SER A CB 1 ATOM 4714 O OG . SER A 1 609 ? -61.952 40.798 27.683 1.00 127.51 ? 609 SER A OG 1 ATOM 4715 N N . VAL A 1 610 ? -58.764 41.377 28.333 1.00 132.94 ? 610 VAL A N 1 ATOM 4716 C CA . VAL A 1 610 ? -57.774 40.683 29.153 1.00 130.48 ? 610 VAL A CA 1 ATOM 4717 C C . VAL A 1 610 ? -58.223 40.552 30.604 1.00 147.39 ? 610 VAL A C 1 ATOM 4718 O O . VAL A 1 610 ? -58.517 41.550 31.262 1.00 152.97 ? 610 VAL A O 1 ATOM 4719 C CB . VAL A 1 610 ? -56.413 41.405 29.123 1.00 112.22 ? 610 VAL A CB 1 ATOM 4720 C CG1 . VAL A 1 610 ? -55.474 40.816 30.160 1.00 120.32 ? 610 VAL A CG1 1 ATOM 4721 C CG2 . VAL A 1 610 ? -55.800 41.309 27.748 1.00 103.97 ? 610 VAL A CG2 1 ATOM 4722 N N . ASP A 1 611 ? -58.273 39.320 31.101 1.00 155.21 ? 611 ASP A N 1 ATOM 4723 C CA . ASP A 1 611 ? -58.574 39.087 32.508 1.00 165.07 ? 611 ASP A CA 1 ATOM 4724 C C . ASP A 1 611 ? -57.264 38.946 33.276 1.00 166.13 ? 611 ASP A C 1 ATOM 4725 O O . ASP A 1 611 ? -56.189 38.947 32.676 1.00 148.70 ? 611 ASP A O 1 ATOM 4726 C CB . ASP A 1 611 ? -59.443 37.837 32.675 1.00 166.05 ? 611 ASP A CB 1 ATOM 4727 C CG . ASP A 1 611 ? -60.198 37.817 33.993 1.00 173.57 ? 611 ASP A CG 1 ATOM 4728 O OD1 . ASP A 1 611 ? -59.706 38.410 34.977 1.00 164.88 ? 611 ASP A OD1 1 ATOM 4729 O OD2 . ASP A 1 611 ? -61.287 37.207 34.043 1.00 184.54 ? 611 ASP A OD2 1 ATOM 4730 N N . SER A 1 612 ? -57.347 38.819 34.596 1.00 180.16 ? 612 SER A N 1 ATOM 4731 C CA . SER A 1 612 ? -56.140 38.664 35.398 1.00 191.69 ? 612 SER A CA 1 ATOM 4732 C C . SER A 1 612 ? -56.079 37.316 36.105 1.00 191.63 ? 612 SER A C 1 ATOM 4733 O O . SER A 1 612 ? -56.798 37.082 37.077 1.00 195.42 ? 612 SER A O 1 ATOM 4734 C CB . SER A 1 612 ? -56.044 39.790 36.430 1.00 195.88 ? 612 SER A CB 1 ATOM 4735 O OG . SER A 1 612 ? -56.057 41.061 35.804 1.00 199.11 ? 612 SER A OG 1 ATOM 4736 N N . ASP A 1 613 ? -55.214 36.433 35.617 1.00 182.08 ? 613 ASP A N 1 ATOM 4737 C CA . ASP A 1 613 ? -54.858 35.234 36.361 1.00 178.78 ? 613 ASP A CA 1 ATOM 4738 C C . ASP A 1 613 ? -53.773 35.608 37.359 1.00 185.72 ? 613 ASP A C 1 ATOM 4739 O O . ASP A 1 613 ? -53.794 35.189 38.516 1.00 188.10 ? 613 ASP A O 1 ATOM 4740 C CB . ASP A 1 613 ? -54.386 34.119 35.428 1.00 174.02 ? 613 ASP A CB 1 ATOM 4741 C CG . ASP A 1 613 ? -54.264 32.783 36.135 1.00 175.32 ? 613 ASP A CG 1 ATOM 4742 O OD1 . ASP A 1 613 ? -55.269 32.042 36.187 1.00 171.25 ? 613 ASP A OD1 1 ATOM 4743 O OD2 . ASP A 1 613 ? -53.164 32.473 36.641 1.00 171.83 ? 613 ASP A OD2 1 ATOM 4744 N N . GLN A 1 614 ? -52.826 36.414 36.887 1.00 185.87 ? 614 GLN A N 1 ATOM 4745 C CA . GLN A 1 614 ? -51.779 36.967 37.733 1.00 175.55 ? 614 GLN A CA 1 ATOM 4746 C C . GLN A 1 614 ? -52.323 38.158 38.511 1.00 163.27 ? 614 GLN A C 1 ATOM 4747 O O . GLN A 1 614 ? -53.006 39.016 37.951 1.00 159.49 ? 614 GLN A O 1 ATOM 4748 C CB . GLN A 1 614 ? -50.571 37.389 36.893 1.00 173.37 ? 614 GLN A CB 1 ATOM 4749 C CG . GLN A 1 614 ? -49.852 36.244 36.194 1.00 168.05 ? 614 GLN A CG 1 ATOM 4750 C CD . GLN A 1 614 ? -48.910 35.495 37.116 1.00 169.82 ? 614 GLN A CD 1 ATOM 4751 O OE1 . GLN A 1 614 ? -48.681 35.902 38.255 1.00 171.82 ? 614 GLN A OE1 1 ATOM 4752 N NE2 . GLN A 1 614 ? -48.353 34.394 36.624 1.00 167.83 ? 614 GLN A NE2 1 ATOM 4753 N N . LYS A 1 615 ? -52.020 38.206 39.802 1.00 153.58 ? 615 LYS A N 1 ATOM 4754 C CA . LYS A 1 615 ? -52.494 39.290 40.652 1.00 155.32 ? 615 LYS A CA 1 ATOM 4755 C C . LYS A 1 615 ? -51.331 40.097 41.212 1.00 152.40 ? 615 LYS A C 1 ATOM 4756 O O . LYS A 1 615 ? -51.194 41.288 40.931 1.00 160.48 ? 615 LYS A O 1 ATOM 4757 C CB . LYS A 1 615 ? -53.355 38.743 41.792 1.00 152.78 ? 615 LYS A CB 1 ATOM 4758 C CG . LYS A 1 615 ? -54.613 38.027 41.329 1.00 152.74 ? 615 LYS A CG 1 ATOM 4759 C CD . LYS A 1 615 ? -55.515 38.950 40.524 1.00 145.18 ? 615 LYS A CD 1 ATOM 4760 C CE . LYS A 1 615 ? -56.016 40.112 41.368 1.00 140.12 ? 615 LYS A CE 1 ATOM 4761 N NZ . LYS A 1 615 ? -56.929 41.002 40.599 1.00 140.47 ? 615 LYS A NZ 1 ATOM 4762 N N . LYS A 1 616 ? -50.497 39.442 42.010 1.00 140.92 ? 616 LYS A N 1 ATOM 4763 C CA . LYS A 1 616 ? -49.399 40.115 42.688 1.00 131.20 ? 616 LYS A CA 1 ATOM 4764 C C . LYS A 1 616 ? -48.063 39.896 41.983 1.00 125.78 ? 616 LYS A C 1 ATOM 4765 O O . LYS A 1 616 ? -47.723 38.774 41.603 1.00 131.51 ? 616 LYS A O 1 ATOM 4766 C CB . LYS A 1 616 ? -49.308 39.632 44.138 1.00 144.00 ? 616 LYS A CB 1 ATOM 4767 C CG . LYS A 1 616 ? -50.634 39.674 44.883 1.00 159.27 ? 616 LYS A CG 1 ATOM 4768 C CD . LYS A 1 616 ? -50.572 38.885 46.182 1.00 157.13 ? 616 LYS A CD 1 ATOM 4769 C CE . LYS A 1 616 ? -51.945 38.780 46.829 1.00 152.76 ? 616 LYS A CE 1 ATOM 4770 N NZ . LYS A 1 616 ? -51.932 37.896 48.028 1.00 153.75 ? 616 LYS A NZ 1 ATOM 4771 N N . ILE A 1 617 ? -47.312 40.980 41.810 1.00 115.29 ? 617 ILE A N 1 ATOM 4772 C CA . ILE A 1 617 ? -45.948 40.901 41.299 1.00 109.32 ? 617 ILE A CA 1 ATOM 4773 C C . ILE A 1 617 ? -44.976 41.478 42.322 1.00 112.88 ? 617 ILE A C 1 ATOM 4774 O O . ILE A 1 617 ? -45.056 42.655 42.676 1.00 116.99 ? 617 ILE A O 1 ATOM 4775 C CB . ILE A 1 617 ? -45.796 41.638 39.961 1.00 105.13 ? 617 ILE A CB 1 ATOM 4776 C CG1 . ILE A 1 617 ? -46.428 40.814 38.840 1.00 107.61 ? 617 ILE A CG1 1 ATOM 4777 C CG2 . ILE A 1 617 ? -44.331 41.883 39.654 1.00 103.10 ? 617 ILE A CG2 1 ATOM 4778 C CD1 . ILE A 1 617 ? -45.881 39.405 38.747 1.00 108.15 ? 617 ILE A CD1 1 ATOM 4779 N N . TYR A 1 618 ? -44.058 40.641 42.794 1.00 110.72 ? 618 TYR A N 1 ATOM 4780 C CA . TYR A 1 618 ? -43.163 41.014 43.882 1.00 100.55 ? 618 TYR A CA 1 ATOM 4781 C C . TYR A 1 618 ? -41.912 41.729 43.384 1.00 108.79 ? 618 TYR A C 1 ATOM 4782 O O . TYR A 1 618 ? -41.294 41.313 42.404 1.00 118.67 ? 618 TYR A O 1 ATOM 4783 C CB . TYR A 1 618 ? -42.779 39.774 44.686 1.00 97.25 ? 618 TYR A CB 1 ATOM 4784 C CG . TYR A 1 618 ? -43.973 39.043 45.257 1.00 104.08 ? 618 TYR A CG 1 ATOM 4785 C CD1 . TYR A 1 618 ? -45.001 39.739 45.878 1.00 114.54 ? 618 TYR A CD1 1 ATOM 4786 C CD2 . TYR A 1 618 ? -44.083 37.663 45.159 1.00 109.89 ? 618 TYR A CD2 1 ATOM 4787 C CE1 . TYR A 1 618 ? -46.100 39.082 46.397 1.00 120.56 ? 618 TYR A CE1 1 ATOM 4788 C CE2 . TYR A 1 618 ? -45.179 36.995 45.676 1.00 118.71 ? 618 TYR A CE2 1 ATOM 4789 C CZ . TYR A 1 618 ? -46.185 37.710 46.293 1.00 121.28 ? 618 TYR A CZ 1 ATOM 4790 O OH . TYR A 1 618 ? -47.279 37.055 46.808 1.00 126.65 ? 618 TYR A OH 1 ATOM 4791 N N . ILE A 1 619 ? -41.550 42.808 44.072 1.00 108.54 ? 619 ILE A N 1 ATOM 4792 C CA . ILE A 1 619 ? -40.400 43.624 43.698 1.00 106.91 ? 619 ILE A CA 1 ATOM 4793 C C . ILE A 1 619 ? -39.077 42.981 44.108 1.00 114.76 ? 619 ILE A C 1 ATOM 4794 O O . ILE A 1 619 ? -38.973 42.387 45.180 1.00 110.69 ? 619 ILE A O 1 ATOM 4795 C CB . ILE A 1 619 ? -40.485 45.027 44.334 1.00 95.72 ? 619 ILE A CB 1 ATOM 4796 C CG1 . ILE A 1 619 ? -41.848 45.659 44.056 1.00 105.19 ? 619 ILE A CG1 1 ATOM 4797 C CG2 . ILE A 1 619 ? -39.371 45.924 43.818 1.00 111.63 ? 619 ILE A CG2 1 ATOM 4798 C CD1 . ILE A 1 619 ? -41.923 47.130 44.426 1.00 111.14 ? 619 ILE A CD1 1 ATOM 4799 N N . GLY A 1 620 ? -38.066 43.111 43.253 1.00 122.67 ? 620 GLY A N 1 ATOM 4800 C CA . GLY A 1 620 ? -36.727 42.655 43.578 1.00 129.85 ? 620 GLY A CA 1 ATOM 4801 C C . GLY A 1 620 ? -36.261 41.430 42.818 1.00 136.17 ? 620 GLY A C 1 ATOM 4802 O O . GLY A 1 620 ? -35.092 41.051 42.904 1.00 147.40 ? 620 GLY A O 1 ATOM 4803 N N . ASP A 1 621 ? -37.164 40.808 42.069 1.00 136.11 ? 621 ASP A N 1 ATOM 4804 C CA . ASP A 1 621 ? -36.804 39.622 41.302 1.00 144.11 ? 621 ASP A CA 1 ATOM 4805 C C . ASP A 1 621 ? -37.653 39.466 40.048 1.00 134.08 ? 621 ASP A C 1 ATOM 4806 O O . ASP A 1 621 ? -38.774 39.969 39.975 1.00 125.27 ? 621 ASP A O 1 ATOM 4807 C CB . ASP A 1 621 ? -36.936 38.366 42.169 1.00 141.89 ? 621 ASP A CB 1 ATOM 4808 C CG . ASP A 1 621 ? -38.381 38.029 42.491 1.00 134.68 ? 621 ASP A CG 1 ATOM 4809 O OD1 . ASP A 1 621 ? -39.201 38.964 42.612 1.00 137.27 ? 621 ASP A OD1 1 ATOM 4810 O OD2 . ASP A 1 621 ? -38.699 36.829 42.624 1.00 115.54 ? 621 ASP A OD2 1 ATOM 4811 N N . ASP A 1 622 ? -37.106 38.767 39.060 1.00 137.03 ? 622 ASP A N 1 ATOM 4812 C CA . ASP A 1 622 ? -37.891 38.360 37.907 1.00 147.42 ? 622 ASP A CA 1 ATOM 4813 C C . ASP A 1 622 ? -38.895 37.304 38.353 1.00 139.54 ? 622 ASP A C 1 ATOM 4814 O O . ASP A 1 622 ? -38.712 36.667 39.391 1.00 132.39 ? 622 ASP A O 1 ATOM 4815 C CB . ASP A 1 622 ? -36.996 37.833 36.782 1.00 161.10 ? 622 ASP A CB 1 ATOM 4816 C CG . ASP A 1 622 ? -35.929 36.873 37.277 1.00 170.82 ? 622 ASP A CG 1 ATOM 4817 O OD1 . ASP A 1 622 ? -36.211 36.072 38.193 1.00 171.95 ? 622 ASP A OD1 1 ATOM 4818 O OD2 . ASP A 1 622 ? -34.800 36.919 36.744 1.00 175.26 ? 622 ASP A OD2 1 ATOM 4819 N N . ASN A 1 623 ? -39.941 37.114 37.560 1.00 140.70 ? 623 ASN A N 1 ATOM 4820 C CA . ASN A 1 623 ? -41.059 36.261 37.941 1.00 135.14 ? 623 ASN A CA 1 ATOM 4821 C C . ASN A 1 623 ? -42.050 36.144 36.797 1.00 122.86 ? 623 ASN A C 1 ATOM 4822 O O . ASN A 1 623 ? -42.253 37.102 36.052 1.00 120.53 ? 623 ASN A O 1 ATOM 4823 C CB . ASN A 1 623 ? -41.762 36.811 39.188 1.00 145.77 ? 623 ASN A CB 1 ATOM 4824 C CG . ASN A 1 623 ? -41.955 38.317 39.134 1.00 130.10 ? 623 ASN A CG 1 ATOM 4825 O OD1 . ASN A 1 623 ? -41.615 38.962 38.142 1.00 125.16 ? 623 ASN A OD1 1 ATOM 4826 N ND2 . ASN A 1 623 ? -42.503 38.884 40.204 1.00 118.31 ? 623 ASN A ND2 1 ATOM 4827 N N . PRO A 1 624 ? -42.669 34.964 36.648 1.00 126.47 ? 624 PRO A N 1 ATOM 4828 C CA . PRO A 1 624 ? -43.574 34.764 35.514 1.00 131.83 ? 624 PRO A CA 1 ATOM 4829 C C . PRO A 1 624 ? -44.761 35.717 35.546 1.00 131.57 ? 624 PRO A C 1 ATOM 4830 O O . PRO A 1 624 ? -45.470 35.807 36.548 1.00 139.93 ? 624 PRO A O 1 ATOM 4831 C CB . PRO A 1 624 ? -44.035 33.312 35.683 1.00 141.21 ? 624 PRO A CB 1 ATOM 4832 C CG . PRO A 1 624 ? -43.844 33.020 37.136 1.00 145.48 ? 624 PRO A CG 1 ATOM 4833 C CD . PRO A 1 624 ? -42.621 33.788 37.534 1.00 136.12 ? 624 PRO A CD 1 ATOM 4834 N N . LEU A 1 625 ? -44.965 36.422 34.440 1.00 125.31 ? 625 LEU A N 1 ATOM 4835 C CA . LEU A 1 625 ? -46.122 37.285 34.277 1.00 124.05 ? 625 LEU A CA 1 ATOM 4836 C C . LEU A 1 625 ? -46.777 36.933 32.955 1.00 125.78 ? 625 LEU A C 1 ATOM 4837 O O . LEU A 1 625 ? -46.206 37.163 31.889 1.00 125.32 ? 625 LEU A O 1 ATOM 4838 C CB . LEU A 1 625 ? -45.717 38.762 34.322 1.00 123.15 ? 625 LEU A CB 1 ATOM 4839 C CG . LEU A 1 625 ? -46.810 39.827 34.463 1.00 122.63 ? 625 LEU A CG 1 ATOM 4840 C CD1 . LEU A 1 625 ? -47.441 40.183 33.123 1.00 128.90 ? 625 LEU A CD1 1 ATOM 4841 C CD2 . LEU A 1 625 ? -47.874 39.374 35.450 1.00 123.57 ? 625 LEU A CD2 1 ATOM 4842 N N . THR A 1 626 ? -47.978 36.377 33.023 1.00 128.00 ? 626 THR A N 1 ATOM 4843 C CA . THR A 1 626 ? -48.646 35.904 31.822 1.00 132.34 ? 626 THR A CA 1 ATOM 4844 C C . THR A 1 626 ? -49.998 36.578 31.652 1.00 126.28 ? 626 THR A C 1 ATOM 4845 O O . THR A 1 626 ? -50.865 36.490 32.522 1.00 131.68 ? 626 THR A O 1 ATOM 4846 C CB . THR A 1 626 ? -48.830 34.375 31.848 1.00 142.46 ? 626 THR A CB 1 ATOM 4847 O OG1 . THR A 1 626 ? -47.566 33.742 32.088 1.00 134.04 ? 626 THR A OG1 1 ATOM 4848 C CG2 . THR A 1 626 ? -49.392 33.885 30.523 1.00 148.49 ? 626 THR A CG2 1 ATOM 4849 N N . LEU A 1 627 ? -50.164 37.263 30.526 1.00 116.00 ? 627 LEU A N 1 ATOM 4850 C CA . LEU A 1 627 ? -51.420 37.922 30.208 1.00 110.11 ? 627 LEU A CA 1 ATOM 4851 C C . LEU A 1 627 ? -52.187 37.109 29.179 1.00 112.22 ? 627 LEU A C 1 ATOM 4852 O O . LEU A 1 627 ? -51.618 36.670 28.183 1.00 114.04 ? 627 LEU A O 1 ATOM 4853 C CB . LEU A 1 627 ? -51.172 39.337 29.682 1.00 105.91 ? 627 LEU A CB 1 ATOM 4854 C CG . LEU A 1 627 ? -50.348 40.263 30.578 1.00 113.01 ? 627 LEU A CG 1 ATOM 4855 C CD1 . LEU A 1 627 ? -50.121 41.607 29.903 1.00 108.76 ? 627 LEU A CD1 1 ATOM 4856 C CD2 . LEU A 1 627 ? -51.027 40.444 31.926 1.00 136.44 ? 627 LEU A CD2 1 ATOM 4857 N N . ILE A 1 628 ? -53.476 36.902 29.422 1.00 108.68 ? 628 ILE A N 1 ATOM 4858 C CA . ILE A 1 628 ? -54.316 36.220 28.448 1.00 102.08 ? 628 ILE A CA 1 ATOM 4859 C C . ILE A 1 628 ? -55.104 37.241 27.632 1.00 105.07 ? 628 ILE A C 1 ATOM 4860 O O . ILE A 1 628 ? -55.922 37.992 28.166 1.00 103.45 ? 628 ILE A O 1 ATOM 4861 C CB . ILE A 1 628 ? -55.278 35.219 29.118 1.00 104.79 ? 628 ILE A CB 1 ATOM 4862 C CG1 . ILE A 1 628 ? -55.987 35.858 30.313 1.00 130.84 ? 628 ILE A CG1 1 ATOM 4863 C CG2 . ILE A 1 628 ? -54.515 33.986 29.570 1.00 99.46 ? 628 ILE A CG2 1 ATOM 4864 C CD1 . ILE A 1 628 ? -57.481 35.597 30.346 1.00 132.37 ? 628 ILE A CD1 1 ATOM 4865 N N . VAL A 1 629 ? -54.837 37.275 26.331 1.00 110.16 ? 629 VAL A N 1 ATOM 4866 C CA . VAL A 1 629 ? -55.483 38.238 25.449 1.00 114.28 ? 629 VAL A CA 1 ATOM 4867 C C . VAL A 1 629 ? -56.632 37.602 24.675 1.00 114.86 ? 629 VAL A C 1 ATOM 4868 O O . VAL A 1 629 ? -56.506 36.503 24.136 1.00 114.50 ? 629 VAL A O 1 ATOM 4869 C CB . VAL A 1 629 ? -54.477 38.860 24.454 1.00 108.90 ? 629 VAL A CB 1 ATOM 4870 C CG1 . VAL A 1 629 ? -53.515 39.782 25.180 1.00 108.44 ? 629 VAL A CG1 1 ATOM 4871 C CG2 . VAL A 1 629 ? -53.713 37.776 23.709 1.00 124.74 ? 629 VAL A CG2 1 ATOM 4872 N N . LYS A 1 630 ? -57.763 38.294 24.649 1.00 112.48 ? 630 LYS A N 1 ATOM 4873 C CA . LYS A 1 630 ? -58.897 37.858 23.854 1.00 103.02 ? 630 LYS A CA 1 ATOM 4874 C C . LYS A 1 630 ? -59.148 38.879 22.750 1.00 99.35 ? 630 LYS A C 1 ATOM 4875 O O . LYS A 1 630 ? -59.634 39.982 23.006 1.00 105.02 ? 630 LYS A O 1 ATOM 4876 C CB . LYS A 1 630 ? -60.130 37.676 24.742 1.00 111.06 ? 630 LYS A CB 1 ATOM 4877 C CG . LYS A 1 630 ? -61.400 37.267 24.018 1.00 122.13 ? 630 LYS A CG 1 ATOM 4878 C CD . LYS A 1 630 ? -62.417 36.717 25.008 1.00 122.91 ? 630 LYS A CD 1 ATOM 4879 C CE . LYS A 1 630 ? -63.818 36.701 24.426 1.00 130.80 ? 630 LYS A CE 1 ATOM 4880 N NZ . LYS A 1 630 ? -64.351 38.082 24.269 1.00 119.71 ? 630 LYS A NZ 1 ATOM 4881 N N . ALA A 1 631 ? -58.814 38.499 21.521 1.00 93.95 ? 631 ALA A N 1 ATOM 4882 C CA . ALA A 1 631 ? -58.938 39.395 20.378 1.00 94.87 ? 631 ALA A CA 1 ATOM 4883 C C . ALA A 1 631 ? -59.991 38.884 19.410 1.00 103.56 ? 631 ALA A C 1 ATOM 4884 O O . ALA A 1 631 ? -59.794 37.870 18.744 1.00 112.47 ? 631 ALA A O 1 ATOM 4885 C CB . ALA A 1 631 ? -57.602 39.546 19.672 1.00 88.86 ? 631 ALA A CB 1 ATOM 4886 N N . GLN A 1 632 ? -61.108 39.596 19.329 1.00 105.15 ? 632 GLN A N 1 ATOM 4887 C CA . GLN A 1 632 ? -62.209 39.175 18.479 1.00 117.49 ? 632 GLN A CA 1 ATOM 4888 C C . GLN A 1 632 ? -62.568 40.250 17.464 1.00 121.22 ? 632 GLN A C 1 ATOM 4889 O O . GLN A 1 632 ? -62.484 41.445 17.751 1.00 121.00 ? 632 GLN A O 1 ATOM 4890 C CB . GLN A 1 632 ? -63.433 38.819 19.328 1.00 134.22 ? 632 GLN A CB 1 ATOM 4891 C CG . GLN A 1 632 ? -63.803 39.874 20.358 1.00 133.85 ? 632 GLN A CG 1 ATOM 4892 C CD . GLN A 1 632 ? -64.996 39.473 21.205 1.00 144.95 ? 632 GLN A CD 1 ATOM 4893 O OE1 . GLN A 1 632 ? -64.924 39.466 22.433 1.00 151.66 ? 632 GLN A OE1 1 ATOM 4894 N NE2 . GLN A 1 632 ? -66.104 39.142 20.550 1.00 148.64 ? 632 GLN A NE2 1 ATOM 4895 N N . ASN A 1 633 ? -62.956 39.815 16.270 1.00 122.26 ? 633 ASN A N 1 ATOM 4896 C CA . ASN A 1 633 ? -63.433 40.732 15.246 1.00 115.41 ? 633 ASN A CA 1 ATOM 4897 C C . ASN A 1 633 ? -64.868 40.412 14.854 1.00 101.86 ? 633 ASN A C 1 ATOM 4898 O O . ASN A 1 633 ? -65.132 39.405 14.201 1.00 95.06 ? 633 ASN A O 1 ATOM 4899 C CB . ASN A 1 633 ? -62.527 40.676 14.012 1.00 112.31 ? 633 ASN A CB 1 ATOM 4900 C CG . ASN A 1 633 ? -63.081 41.470 12.837 1.00 102.27 ? 633 ASN A CG 1 ATOM 4901 O OD1 . ASN A 1 633 ? -63.797 42.455 13.018 1.00 103.50 ? 633 ASN A OD1 1 ATOM 4902 N ND2 . ASN A 1 633 ? -62.748 41.041 11.625 1.00 79.30 ? 633 ASN A ND2 1 ATOM 4903 N N . GLN A 1 634 ? -65.793 41.284 15.236 1.00 93.46 ? 634 GLN A N 1 ATOM 4904 C CA . GLN A 1 634 ? -67.171 41.138 14.797 1.00 107.64 ? 634 GLN A CA 1 ATOM 4905 C C . GLN A 1 634 ? -67.470 42.199 13.751 1.00 114.99 ? 634 GLN A C 1 ATOM 4906 O O . GLN A 1 634 ? -67.616 43.377 14.065 1.00 117.68 ? 634 GLN A O 1 ATOM 4907 C CB . GLN A 1 634 ? -68.140 41.247 15.976 1.00 103.46 ? 634 GLN A CB 1 ATOM 4908 C CG . GLN A 1 634 ? -68.627 39.905 16.502 1.00 108.40 ? 634 GLN A CG 1 ATOM 4909 C CD . GLN A 1 634 ? -67.496 39.013 16.976 1.00 115.65 ? 634 GLN A CD 1 ATOM 4910 O OE1 . GLN A 1 634 ? -66.532 39.481 17.583 1.00 116.68 ? 634 GLN A OE1 1 ATOM 4911 N NE2 . GLN A 1 634 ? -67.608 37.719 16.698 1.00 123.26 ? 634 GLN A NE2 1 ATOM 4912 N N . GLY A 1 635 ? -67.568 41.763 12.503 1.00 126.56 ? 635 GLY A N 1 ATOM 4913 C CA . GLY A 1 635 ? -67.758 42.667 11.389 1.00 120.80 ? 635 GLY A CA 1 ATOM 4914 C C . GLY A 1 635 ? -67.054 42.110 10.171 1.00 122.90 ? 635 GLY A C 1 ATOM 4915 O O . GLY A 1 635 ? -66.553 40.987 10.196 1.00 110.94 ? 635 GLY A O 1 ATOM 4916 N N . GLU A 1 636 ? -66.998 42.901 9.108 1.00 122.59 ? 636 GLU A N 1 ATOM 4917 C CA . GLU A 1 636 ? -66.358 42.466 7.875 1.00 129.93 ? 636 GLU A CA 1 ATOM 4918 C C . GLU A 1 636 ? -64.850 42.315 8.094 1.00 126.90 ? 636 GLU A C 1 ATOM 4919 O O . GLU A 1 636 ? -64.298 42.879 9.038 1.00 120.32 ? 636 GLU A O 1 ATOM 4920 C CB . GLU A 1 636 ? -66.677 43.450 6.747 1.00 121.85 ? 636 GLU A CB 1 ATOM 4921 C CG . GLU A 1 636 ? -68.182 43.636 6.545 1.00 104.57 ? 636 GLU A CG 1 ATOM 4922 C CD . GLU A 1 636 ? -68.530 44.735 5.559 1.00 124.15 ? 636 GLU A CD 1 ATOM 4923 O OE1 . GLU A 1 636 ? -67.619 45.229 4.868 1.00 119.49 ? 636 GLU A OE1 1 ATOM 4924 O OE2 . GLU A 1 636 ? -69.720 45.107 5.474 1.00 119.20 ? 636 GLU A OE2 1 ATOM 4925 N N . GLY A 1 637 ? -64.199 41.534 7.235 1.00 113.33 ? 637 GLY A N 1 ATOM 4926 C CA . GLY A 1 637 ? -62.803 41.163 7.414 1.00 93.54 ? 637 GLY A CA 1 ATOM 4927 C C . GLY A 1 637 ? -61.824 42.306 7.609 1.00 109.85 ? 637 GLY A C 1 ATOM 4928 O O . GLY A 1 637 ? -61.987 43.384 7.039 1.00 119.88 ? 637 GLY A O 1 ATOM 4929 N N . ALA A 1 638 ? -60.798 42.063 8.420 1.00 112.88 ? 638 ALA A N 1 ATOM 4930 C CA . ALA A 1 638 ? -59.799 43.082 8.731 1.00 94.22 ? 638 ALA A CA 1 ATOM 4931 C C . ALA A 1 638 ? -58.455 42.772 8.077 1.00 86.24 ? 638 ALA A C 1 ATOM 4932 O O . ALA A 1 638 ? -57.803 41.786 8.417 1.00 83.48 ? 638 ALA A O 1 ATOM 4933 C CB . ALA A 1 638 ? -59.636 43.213 10.235 1.00 80.83 ? 638 ALA A CB 1 ATOM 4934 N N . TYR A 1 639 ? -58.045 43.627 7.144 1.00 96.30 ? 639 TYR A N 1 ATOM 4935 C CA . TYR A 1 639 ? -56.787 43.449 6.421 1.00 103.13 ? 639 TYR A CA 1 ATOM 4936 C C . TYR A 1 639 ? -55.573 43.618 7.324 1.00 103.98 ? 639 TYR A C 1 ATOM 4937 O O . TYR A 1 639 ? -55.460 44.616 8.038 1.00 102.80 ? 639 TYR A O 1 ATOM 4938 C CB . TYR A 1 639 ? -56.693 44.443 5.262 1.00 106.34 ? 639 TYR A CB 1 ATOM 4939 C CG . TYR A 1 639 ? -57.808 44.328 4.254 1.00 116.16 ? 639 TYR A CG 1 ATOM 4940 C CD1 . TYR A 1 639 ? -58.199 43.094 3.757 1.00 104.14 ? 639 TYR A CD1 1 ATOM 4941 C CD2 . TYR A 1 639 ? -58.476 45.456 3.804 1.00 124.79 ? 639 TYR A CD2 1 ATOM 4942 C CE1 . TYR A 1 639 ? -59.220 42.990 2.834 1.00 123.10 ? 639 TYR A CE1 1 ATOM 4943 C CE2 . TYR A 1 639 ? -59.498 45.362 2.885 1.00 111.87 ? 639 TYR A CE2 1 ATOM 4944 C CZ . TYR A 1 639 ? -59.866 44.129 2.402 1.00 119.26 ? 639 TYR A CZ 1 ATOM 4945 O OH . TYR A 1 639 ? -60.886 44.037 1.484 1.00 140.54 ? 639 TYR A OH 1 ATOM 4946 N N . GLU A 1 640 ? -54.671 42.641 7.276 1.00 101.90 ? 640 GLU A N 1 ATOM 4947 C CA . GLU A 1 640 ? -53.406 42.695 8.006 1.00 101.46 ? 640 GLU A CA 1 ATOM 4948 C C . GLU A 1 640 ? -53.605 43.038 9.479 1.00 99.29 ? 640 GLU A C 1 ATOM 4949 O O . GLU A 1 640 ? -52.984 43.962 10.001 1.00 101.61 ? 640 GLU A O 1 ATOM 4950 C CB . GLU A 1 640 ? -52.463 43.707 7.350 1.00 102.76 ? 640 GLU A CB 1 ATOM 4951 C CG . GLU A 1 640 ? -52.281 43.492 5.853 1.00 122.67 ? 640 GLU A CG 1 ATOM 4952 C CD . GLU A 1 640 ? -51.332 44.493 5.222 1.00 132.80 ? 640 GLU A CD 1 ATOM 4953 O OE1 . GLU A 1 640 ? -51.432 44.715 3.996 1.00 135.46 ? 640 GLU A OE1 1 ATOM 4954 O OE2 . GLU A 1 640 ? -50.484 45.053 5.948 1.00 139.84 ? 640 GLU A OE2 1 ATOM 4955 N N . ALA A 1 641 ? -54.484 42.293 10.140 1.00 95.46 ? 641 ALA A N 1 ATOM 4956 C CA . ALA A 1 641 ? -54.784 42.536 11.544 1.00 97.82 ? 641 ALA A CA 1 ATOM 4957 C C . ALA A 1 641 ? -53.599 42.181 12.430 1.00 103.39 ? 641 ALA A C 1 ATOM 4958 O O . ALA A 1 641 ? -52.982 41.129 12.270 1.00 110.85 ? 641 ALA A O 1 ATOM 4959 C CB . ALA A 1 641 ? -56.011 41.750 11.968 1.00 95.87 ? 641 ALA A CB 1 ATOM 4960 N N . GLU A 1 642 ? -53.284 43.070 13.365 1.00 99.17 ? 642 GLU A N 1 ATOM 4961 C CA . GLU A 1 642 ? -52.179 42.852 14.284 1.00 100.37 ? 642 GLU A CA 1 ATOM 4962 C C . GLU A 1 642 ? -52.539 43.299 15.693 1.00 100.88 ? 642 GLU A C 1 ATOM 4963 O O . GLU A 1 642 ? -53.120 44.365 15.886 1.00 101.04 ? 642 GLU A O 1 ATOM 4964 C CB . GLU A 1 642 ? -50.928 43.593 13.810 1.00 103.83 ? 642 GLU A CB 1 ATOM 4965 C CG . GLU A 1 642 ? -50.287 43.016 12.561 1.00 111.19 ? 642 GLU A CG 1 ATOM 4966 C CD . GLU A 1 642 ? -49.126 43.856 12.068 1.00 127.92 ? 642 GLU A CD 1 ATOM 4967 O OE1 . GLU A 1 642 ? -49.004 45.020 12.507 1.00 139.68 ? 642 GLU A OE1 1 ATOM 4968 O OE2 . GLU A 1 642 ? -48.333 43.352 11.244 1.00 131.26 ? 642 GLU A OE2 1 ATOM 4969 N N . LEU A 1 643 ? -52.196 42.473 16.674 1.00 103.43 ? 643 LEU A N 1 ATOM 4970 C CA . LEU A 1 643 ? -52.349 42.852 18.068 1.00 101.92 ? 643 LEU A CA 1 ATOM 4971 C C . LEU A 1 643 ? -51.113 43.620 18.511 1.00 105.48 ? 643 LEU A C 1 ATOM 4972 O O . LEU A 1 643 ? -49.994 43.123 18.399 1.00 112.49 ? 643 LEU A O 1 ATOM 4973 C CB . LEU A 1 643 ? -52.562 41.624 18.953 1.00 100.35 ? 643 LEU A CB 1 ATOM 4974 C CG . LEU A 1 643 ? -52.750 41.924 20.441 1.00 104.12 ? 643 LEU A CG 1 ATOM 4975 C CD1 . LEU A 1 643 ? -54.030 42.713 20.673 1.00 102.86 ? 643 LEU A CD1 1 ATOM 4976 C CD2 . LEU A 1 643 ? -52.746 40.642 21.259 1.00 109.64 ? 643 LEU A CD2 1 ATOM 4977 N N . ILE A 1 644 ? -51.316 44.836 19.003 1.00 103.37 ? 644 ILE A N 1 ATOM 4978 C CA . ILE A 1 644 ? -50.200 45.673 19.419 1.00 99.50 ? 644 ILE A CA 1 ATOM 4979 C C . ILE A 1 644 ? -50.128 45.789 20.933 1.00 103.54 ? 644 ILE A C 1 ATOM 4980 O O . ILE A 1 644 ? -50.998 46.388 21.567 1.00 104.24 ? 644 ILE A O 1 ATOM 4981 C CB . ILE A 1 644 ? -50.294 47.080 18.811 1.00 97.75 ? 644 ILE A CB 1 ATOM 4982 C CG1 . ILE A 1 644 ? -50.381 46.989 17.287 1.00 102.35 ? 644 ILE A CG1 1 ATOM 4983 C CG2 . ILE A 1 644 ? -49.104 47.924 19.239 1.00 99.70 ? 644 ILE A CG2 1 ATOM 4984 C CD1 . ILE A 1 644 ? -49.285 46.153 16.663 1.00 107.66 ? 644 ILE A CD1 1 ATOM 4985 N N . VAL A 1 645 ? -49.079 45.211 21.507 1.00 109.55 ? 645 VAL A N 1 ATOM 4986 C CA . VAL A 1 645 ? -48.868 45.273 22.944 1.00 106.91 ? 645 VAL A CA 1 ATOM 4987 C C . VAL A 1 645 ? -47.813 46.317 23.271 1.00 112.45 ? 645 VAL A C 1 ATOM 4988 O O . VAL A 1 645 ? -46.628 46.098 23.037 1.00 126.65 ? 645 VAL A O 1 ATOM 4989 C CB . VAL A 1 645 ? -48.417 43.912 23.506 1.00 106.10 ? 645 VAL A CB 1 ATOM 4990 C CG1 . VAL A 1 645 ? -48.162 44.010 25.002 1.00 112.27 ? 645 VAL A CG1 1 ATOM 4991 C CG2 . VAL A 1 645 ? -49.446 42.835 23.194 1.00 105.90 ? 645 VAL A CG2 1 ATOM 4992 N N . SER A 1 646 ? -48.239 47.443 23.831 1.00 108.03 ? 646 SER A N 1 ATOM 4993 C CA . SER A 1 646 ? -47.295 48.486 24.205 1.00 111.30 ? 646 SER A CA 1 ATOM 4994 C C . SER A 1 646 ? -46.909 48.291 25.661 1.00 124.43 ? 646 SER A C 1 ATOM 4995 O O . SER A 1 646 ? -47.728 48.446 26.566 1.00 134.93 ? 646 SER A O 1 ATOM 4996 C CB . SER A 1 646 ? -47.883 49.879 23.969 1.00 115.44 ? 646 SER A CB 1 ATOM 4997 O OG . SER A 1 646 ? -49.062 50.075 24.724 1.00 114.64 ? 646 SER A OG 1 ATOM 4998 N N . ILE A 1 647 ? -45.646 47.942 25.871 1.00 127.39 ? 647 ILE A N 1 ATOM 4999 C CA . ILE A 1 647 ? -45.165 47.509 27.173 1.00 132.27 ? 647 ILE A CA 1 ATOM 5000 C C . ILE A 1 647 ? -44.528 48.652 27.967 1.00 143.00 ? 647 ILE A C 1 ATOM 5001 O O . ILE A 1 647 ? -44.387 49.762 27.453 1.00 138.19 ? 647 ILE A O 1 ATOM 5002 C CB . ILE A 1 647 ? -44.144 46.379 26.990 1.00 118.60 ? 647 ILE A CB 1 ATOM 5003 C CG1 . ILE A 1 647 ? -42.986 46.869 26.120 1.00 132.87 ? 647 ILE A CG1 1 ATOM 5004 C CG2 . ILE A 1 647 ? -44.807 45.165 26.369 1.00 113.62 ? 647 ILE A CG2 1 ATOM 5005 C CD1 . ILE A 1 647 ? -42.081 45.773 25.625 1.00 146.09 ? 647 ILE A CD1 1 ATOM 5006 N N . PRO A 1 648 ? -44.144 48.387 29.229 1.00 142.01 ? 648 PRO A N 1 ATOM 5007 C CA . PRO A 1 648 ? -43.317 49.367 29.935 1.00 140.35 ? 648 PRO A CA 1 ATOM 5008 C C . PRO A 1 648 ? -41.832 49.087 29.740 1.00 137.05 ? 648 PRO A C 1 ATOM 5009 O O . PRO A 1 648 ? -41.466 48.169 29.005 1.00 131.37 ? 648 PRO A O 1 ATOM 5010 C CB . PRO A 1 648 ? -43.725 49.175 31.394 1.00 136.47 ? 648 PRO A CB 1 ATOM 5011 C CG . PRO A 1 648 ? -44.061 47.732 31.475 1.00 137.44 ? 648 PRO A CG 1 ATOM 5012 C CD . PRO A 1 648 ? -44.705 47.386 30.157 1.00 134.97 ? 648 PRO A CD 1 ATOM 5013 N N . LEU A 1 649 ? -40.989 49.875 30.397 1.00 130.38 ? 649 LEU A N 1 ATOM 5014 C CA . LEU A 1 649 ? -39.544 49.715 30.295 1.00 132.86 ? 649 LEU A CA 1 ATOM 5015 C C . LEU A 1 649 ? -39.078 48.435 30.987 1.00 136.34 ? 649 LEU A C 1 ATOM 5016 O O . LEU A 1 649 ? -37.983 47.935 30.725 1.00 130.70 ? 649 LEU A O 1 ATOM 5017 C CB . LEU A 1 649 ? -38.824 50.927 30.900 1.00 121.47 ? 649 LEU A CB 1 ATOM 5018 C CG . LEU A 1 649 ? -38.840 52.268 30.153 1.00 121.57 ? 649 LEU A CG 1 ATOM 5019 C CD1 . LEU A 1 649 ? -40.216 52.925 30.160 1.00 121.48 ? 649 LEU A CD1 1 ATOM 5020 C CD2 . LEU A 1 649 ? -37.800 53.211 30.738 1.00 124.27 ? 649 LEU A CD2 1 ATOM 5021 N N . GLN A 1 650 ? -39.923 47.909 31.867 1.00 139.53 ? 650 GLN A N 1 ATOM 5022 C CA . GLN A 1 650 ? -39.566 46.782 32.721 1.00 139.39 ? 650 GLN A CA 1 ATOM 5023 C C . GLN A 1 650 ? -40.004 45.440 32.140 1.00 150.72 ? 650 GLN A C 1 ATOM 5024 O O . GLN A 1 650 ? -39.831 44.397 32.772 1.00 156.16 ? 650 GLN A O 1 ATOM 5025 C CB . GLN A 1 650 ? -40.184 46.968 34.109 1.00 127.63 ? 650 GLN A CB 1 ATOM 5026 C CG . GLN A 1 650 ? -40.168 48.407 34.610 1.00 129.97 ? 650 GLN A CG 1 ATOM 5027 C CD . GLN A 1 650 ? -41.392 49.202 34.194 1.00 136.44 ? 650 GLN A CD 1 ATOM 5028 O OE1 . GLN A 1 650 ? -42.525 48.760 34.379 1.00 141.38 ? 650 GLN A OE1 1 ATOM 5029 N NE2 . GLN A 1 650 ? -41.166 50.384 33.631 1.00 139.60 ? 650 GLN A NE2 1 ATOM 5030 N N . ALA A 1 651 ? -40.573 45.479 30.938 1.00 142.12 ? 651 ALA A N 1 ATOM 5031 C CA . ALA A 1 651 ? -41.252 44.326 30.347 1.00 140.11 ? 651 ALA A CA 1 ATOM 5032 C C . ALA A 1 651 ? -40.402 43.064 30.208 1.00 137.26 ? 651 ALA A C 1 ATOM 5033 O O . ALA A 1 651 ? -40.632 42.081 30.914 1.00 137.75 ? 651 ALA A O 1 ATOM 5034 C CB . ALA A 1 651 ? -41.799 44.707 28.996 1.00 156.03 ? 651 ALA A CB 1 ATOM 5035 N N . ASP A 1 652 ? -39.439 43.097 29.288 1.00 138.80 ? 652 ASP A N 1 ATOM 5036 C CA . ASP A 1 652 ? -38.622 41.927 28.959 1.00 155.65 ? 652 ASP A CA 1 ATOM 5037 C C . ASP A 1 652 ? -39.502 40.745 28.528 1.00 150.98 ? 652 ASP A C 1 ATOM 5038 O O . ASP A 1 652 ? -39.638 39.758 29.249 1.00 159.61 ? 652 ASP A O 1 ATOM 5039 C CB . ASP A 1 652 ? -37.732 41.537 30.145 1.00 165.78 ? 652 ASP A CB 1 ATOM 5040 C CG . ASP A 1 652 ? -36.545 40.685 29.733 1.00 165.47 ? 652 ASP A CG 1 ATOM 5041 O OD1 . ASP A 1 652 ? -36.064 40.844 28.591 1.00 165.44 ? 652 ASP A OD1 1 ATOM 5042 O OD2 . ASP A 1 652 ? -36.090 39.860 30.554 1.00 161.44 ? 652 ASP A OD2 1 ATOM 5043 N N . PHE A 1 653 ? -40.101 40.867 27.346 1.00 142.48 ? 653 PHE A N 1 ATOM 5044 C CA . PHE A 1 653 ? -41.032 39.868 26.819 1.00 141.15 ? 653 PHE A CA 1 ATOM 5045 C C . PHE A 1 653 ? -40.343 38.603 26.312 1.00 139.39 ? 653 PHE A C 1 ATOM 5046 O O . PHE A 1 653 ? -39.285 38.672 25.686 1.00 142.84 ? 653 PHE A O 1 ATOM 5047 C CB . PHE A 1 653 ? -41.862 40.492 25.692 1.00 150.00 ? 653 PHE A CB 1 ATOM 5048 C CG . PHE A 1 653 ? -42.445 39.491 24.734 1.00 141.61 ? 653 PHE A CG 1 ATOM 5049 C CD1 . PHE A 1 653 ? -43.578 38.768 25.067 1.00 136.47 ? 653 PHE A CD1 1 ATOM 5050 C CD2 . PHE A 1 653 ? -41.869 39.287 23.489 1.00 145.44 ? 653 PHE A CD2 1 ATOM 5051 C CE1 . PHE A 1 653 ? -44.116 37.852 24.182 1.00 135.23 ? 653 PHE A CE1 1 ATOM 5052 C CE2 . PHE A 1 653 ? -42.402 38.373 22.602 1.00 142.31 ? 653 PHE A CE2 1 ATOM 5053 C CZ . PHE A 1 653 ? -43.528 37.657 22.947 1.00 135.75 ? 653 PHE A CZ 1 ATOM 5054 N N . ILE A 1 654 ? -40.953 37.448 26.576 1.00 134.94 ? 654 ILE A N 1 ATOM 5055 C CA . ILE A 1 654 ? -40.441 36.176 26.067 1.00 140.56 ? 654 ILE A CA 1 ATOM 5056 C C . ILE A 1 654 ? -41.553 35.238 25.583 1.00 144.02 ? 654 ILE A C 1 ATOM 5057 O O . ILE A 1 654 ? -42.601 35.114 26.219 1.00 145.65 ? 654 ILE A O 1 ATOM 5058 C CB . ILE A 1 654 ? -39.595 35.425 27.134 1.00 159.16 ? 654 ILE A CB 1 ATOM 5059 C CG1 . ILE A 1 654 ? -40.428 35.098 28.378 1.00 145.18 ? 654 ILE A CG1 1 ATOM 5060 C CG2 . ILE A 1 654 ? -38.356 36.221 27.512 1.00 164.31 ? 654 ILE A CG2 1 ATOM 5061 C CD1 . ILE A 1 654 ? -40.776 33.627 28.506 1.00 132.91 ? 654 ILE A CD1 1 ATOM 5062 N N . GLY A 1 655 ? -41.314 34.605 24.436 1.00 148.32 ? 655 GLY A N 1 ATOM 5063 C CA . GLY A 1 655 ? -42.135 33.511 23.942 1.00 142.37 ? 655 GLY A CA 1 ATOM 5064 C C . GLY A 1 655 ? -43.638 33.717 23.910 1.00 141.64 ? 655 GLY A C 1 ATOM 5065 O O . GLY A 1 655 ? -44.123 34.807 23.628 1.00 137.14 ? 655 GLY A O 1 ATOM 5066 N N . VAL A 1 656 ? -44.362 32.649 24.240 1.00 149.14 ? 656 VAL A N 1 ATOM 5067 C CA . VAL A 1 656 ? -45.826 32.586 24.227 1.00 141.96 ? 656 VAL A CA 1 ATOM 5068 C C . VAL A 1 656 ? -46.236 31.240 24.807 1.00 143.91 ? 656 VAL A C 1 ATOM 5069 O O . VAL A 1 656 ? -45.385 30.386 25.057 1.00 153.35 ? 656 VAL A O 1 ATOM 5070 C CB . VAL A 1 656 ? -46.448 32.721 22.809 1.00 145.18 ? 656 VAL A CB 1 ATOM 5071 C CG1 . VAL A 1 656 ? -46.841 34.163 22.505 1.00 149.54 ? 656 VAL A CG1 1 ATOM 5072 C CG2 . VAL A 1 656 ? -45.530 32.138 21.737 1.00 150.00 ? 656 VAL A CG2 1 ATOM 5073 N N . VAL A 1 657 ? -47.533 31.040 25.013 1.00 131.88 ? 657 VAL A N 1 ATOM 5074 C CA . VAL A 1 657 ? -47.994 29.842 25.707 1.00 141.67 ? 657 VAL A CA 1 ATOM 5075 C C . VAL A 1 657 ? -48.352 28.711 24.744 1.00 137.72 ? 657 VAL A C 1 ATOM 5076 O O . VAL A 1 657 ? -49.354 28.770 24.030 1.00 121.99 ? 657 VAL A O 1 ATOM 5077 C CB . VAL A 1 657 ? -49.210 30.157 26.596 1.00 131.45 ? 657 VAL A CB 1 ATOM 5078 C CG1 . VAL A 1 657 ? -49.723 28.894 27.264 1.00 138.49 ? 657 VAL A CG1 1 ATOM 5079 C CG2 . VAL A 1 657 ? -48.846 31.207 27.636 1.00 125.89 ? 657 VAL A CG2 1 ATOM 5080 N N . ARG A 1 658 ? -47.514 27.680 24.740 1.00 144.96 ? 658 ARG A N 1 ATOM 5081 C CA . ARG A 1 658 ? -47.697 26.513 23.885 1.00 146.90 ? 658 ARG A CA 1 ATOM 5082 C C . ARG A 1 658 ? -48.651 25.472 24.471 1.00 151.99 ? 658 ARG A C 1 ATOM 5083 O O . ARG A 1 658 ? -49.323 24.747 23.736 1.00 148.50 ? 658 ARG A O 1 ATOM 5084 C CB . ARG A 1 658 ? -46.343 25.855 23.610 1.00 148.23 ? 658 ARG A CB 1 ATOM 5085 C CG . ARG A 1 658 ? -45.203 26.835 23.376 1.00 155.86 ? 658 ARG A CG 1 ATOM 5086 C CD . ARG A 1 658 ? -45.349 27.564 22.052 1.00 168.72 ? 658 ARG A CD 1 ATOM 5087 N NE . ARG A 1 658 ? -44.234 28.475 21.810 1.00 176.64 ? 658 ARG A NE 1 ATOM 5088 C CZ . ARG A 1 658 ? -44.055 29.154 20.681 1.00 181.47 ? 658 ARG A CZ 1 ATOM 5089 N NH1 . ARG A 1 658 ? -44.920 29.027 19.683 1.00 174.37 ? 658 ARG A NH1 1 ATOM 5090 N NH2 . ARG A 1 658 ? -43.012 29.961 20.550 1.00 186.77 ? 658 ARG A NH2 1 ATOM 5091 N N . ASN A 1 659 ? -48.704 25.407 25.798 1.00 149.30 ? 659 ASN A N 1 ATOM 5092 C CA . ASN A 1 659 ? -49.220 24.228 26.494 1.00 139.81 ? 659 ASN A CA 1 ATOM 5093 C C . ASN A 1 659 ? -50.742 24.062 26.561 1.00 140.62 ? 659 ASN A C 1 ATOM 5094 O O . ASN A 1 659 ? -51.226 23.002 26.957 1.00 152.14 ? 659 ASN A O 1 ATOM 5095 C CB . ASN A 1 659 ? -48.655 24.203 27.919 1.00 127.58 ? 659 ASN A CB 1 ATOM 5096 C CG . ASN A 1 659 ? -48.873 25.508 28.659 1.00 144.79 ? 659 ASN A CG 1 ATOM 5097 O OD1 . ASN A 1 659 ? -49.977 26.050 28.674 1.00 151.10 ? 659 ASN A OD1 1 ATOM 5098 N ND2 . ASN A 1 659 ? -47.814 26.023 29.275 1.00 141.92 ? 659 ASN A ND2 1 ATOM 5099 N N . ASN A 1 660 ? -51.499 25.087 26.181 1.00 126.21 ? 660 ASN A N 1 ATOM 5100 C CA . ASN A 1 660 ? -52.957 24.990 26.241 1.00 130.51 ? 660 ASN A CA 1 ATOM 5101 C C . ASN A 1 660 ? -53.614 24.867 24.872 1.00 134.55 ? 660 ASN A C 1 ATOM 5102 O O . ASN A 1 660 ? -53.189 25.501 23.911 1.00 134.74 ? 660 ASN A O 1 ATOM 5103 C CB . ASN A 1 660 ? -53.544 26.197 26.976 1.00 128.59 ? 660 ASN A CB 1 ATOM 5104 C CG . ASN A 1 660 ? -53.304 26.142 28.472 1.00 133.51 ? 660 ASN A CG 1 ATOM 5105 O OD1 . ASN A 1 660 ? -53.056 25.076 29.033 1.00 145.70 ? 660 ASN A OD1 1 ATOM 5106 N ND2 . ASN A 1 660 ? -53.384 27.294 29.127 1.00 134.13 ? 660 ASN A ND2 1 ATOM 5107 N N . GLU A 1 661 ? -54.641 24.027 24.788 1.00 151.65 ? 661 GLU A N 1 ATOM 5108 C CA . GLU A 1 661 ? -55.454 23.933 23.581 1.00 143.83 ? 661 GLU A CA 1 ATOM 5109 C C . GLU A 1 661 ? -56.490 25.050 23.541 1.00 134.53 ? 661 GLU A C 1 ATOM 5110 O O . GLU A 1 661 ? -56.932 25.458 22.466 1.00 150.91 ? 661 GLU A O 1 ATOM 5111 C CB . GLU A 1 661 ? -56.148 22.573 23.490 1.00 146.98 ? 661 GLU A CB 1 ATOM 5112 C CG . GLU A 1 661 ? -55.212 21.407 23.229 1.00 153.04 ? 661 GLU A CG 1 ATOM 5113 C CD . GLU A 1 661 ? -55.943 20.181 22.719 1.00 163.87 ? 661 GLU A CD 1 ATOM 5114 O OE1 . GLU A 1 661 ? -56.986 20.345 22.051 1.00 155.41 ? 661 GLU A OE1 1 ATOM 5115 O OE2 . GLU A 1 661 ? -55.478 19.053 22.989 1.00 166.90 ? 661 GLU A OE2 1 ATOM 5116 N N . ALA A 1 662 ? -56.876 25.530 24.721 1.00 128.18 ? 662 ALA A N 1 ATOM 5117 C CA . ALA A 1 662 ? -57.871 26.592 24.845 1.00 140.18 ? 662 ALA A CA 1 ATOM 5118 C C . ALA A 1 662 ? -57.410 27.846 24.115 1.00 139.03 ? 662 ALA A C 1 ATOM 5119 O O . ALA A 1 662 ? -58.187 28.498 23.415 1.00 127.28 ? 662 ALA A O 1 ATOM 5120 C CB . ALA A 1 662 ? -58.140 26.898 26.310 1.00 136.38 ? 662 ALA A CB 1 ATOM 5121 N N . LEU A 1 663 ? -56.137 28.175 24.290 1.00 140.96 ? 663 LEU A N 1 ATOM 5122 C CA . LEU A 1 663 ? -55.514 29.256 23.546 1.00 127.61 ? 663 LEU A CA 1 ATOM 5123 C C . LEU A 1 663 ? -54.503 28.657 22.574 1.00 134.80 ? 663 LEU A C 1 ATOM 5124 O O . LEU A 1 663 ? -53.553 27.999 22.988 1.00 117.20 ? 663 LEU A O 1 ATOM 5125 C CB . LEU A 1 663 ? -54.857 30.258 24.500 1.00 137.15 ? 663 LEU A CB 1 ATOM 5126 C CG . LEU A 1 663 ? -53.768 29.811 25.482 1.00 136.23 ? 663 LEU A CG 1 ATOM 5127 C CD1 . LEU A 1 663 ? -52.388 30.132 24.930 1.00 138.01 ? 663 LEU A CD1 1 ATOM 5128 C CD2 . LEU A 1 663 ? -53.964 30.457 26.843 1.00 119.16 ? 663 LEU A CD2 1 ATOM 5129 N N . ALA A 1 664 ? -54.706 28.864 21.277 1.00 159.26 ? 664 ALA A N 1 ATOM 5130 C CA . ALA A 1 664 ? -53.863 28.178 20.305 1.00 166.44 ? 664 ALA A CA 1 ATOM 5131 C C . ALA A 1 664 ? -52.775 29.095 19.769 1.00 154.37 ? 664 ALA A C 1 ATOM 5132 O O . ALA A 1 664 ? -53.036 29.994 18.971 1.00 140.89 ? 664 ALA A O 1 ATOM 5133 C CB . ALA A 1 664 ? -54.709 27.634 19.162 1.00 157.95 ? 664 ALA A CB 1 ATOM 5134 N N . ARG A 1 665 ? -51.559 28.847 20.253 1.00 157.05 ? 665 ARG A N 1 ATOM 5135 C CA . ARG A 1 665 ? -50.307 29.480 19.823 1.00 149.30 ? 665 ARG A CA 1 ATOM 5136 C C . ARG A 1 665 ? -50.435 30.984 19.619 1.00 141.97 ? 665 ARG A C 1 ATOM 5137 O O . ARG A 1 665 ? -51.213 31.645 20.307 1.00 145.38 ? 665 ARG A O 1 ATOM 5138 C CB . ARG A 1 665 ? -49.767 28.822 18.538 1.00 148.77 ? 665 ARG A CB 1 ATOM 5139 C CG . ARG A 1 665 ? -50.716 28.791 17.338 1.00 156.55 ? 665 ARG A CG 1 ATOM 5140 C CD . ARG A 1 665 ? -50.038 28.260 16.086 1.00 179.91 ? 665 ARG A CD 1 ATOM 5141 N NE . ARG A 1 665 ? -49.315 29.304 15.364 1.00 183.80 ? 665 ARG A NE 1 ATOM 5142 C CZ . ARG A 1 665 ? -49.833 30.019 14.369 1.00 171.44 ? 665 ARG A CZ 1 ATOM 5143 N NH1 . ARG A 1 665 ? -51.082 29.805 13.974 1.00 152.25 ? 665 ARG A NH1 1 ATOM 5144 N NH2 . ARG A 1 665 ? -49.103 30.949 13.768 1.00 169.22 ? 665 ARG A NH2 1 ATOM 5145 N N . LEU A 1 666 ? -49.655 31.484 18.661 1.00 141.36 ? 666 LEU A N 1 ATOM 5146 C CA . LEU A 1 666 ? -49.816 32.772 17.982 1.00 138.62 ? 666 LEU A CA 1 ATOM 5147 C C . LEU A 1 666 ? -48.556 33.004 17.164 1.00 135.28 ? 666 LEU A C 1 ATOM 5148 O O . LEU A 1 666 ? -47.600 32.233 17.258 1.00 137.27 ? 666 LEU A O 1 ATOM 5149 C CB . LEU A 1 666 ? -50.051 33.943 18.939 1.00 127.76 ? 666 LEU A CB 1 ATOM 5150 C CG . LEU A 1 666 ? -51.477 34.506 18.893 1.00 109.52 ? 666 LEU A CG 1 ATOM 5151 C CD1 . LEU A 1 666 ? -51.510 35.956 19.346 1.00 108.44 ? 666 LEU A CD1 1 ATOM 5152 C CD2 . LEU A 1 666 ? -52.089 34.361 17.504 1.00 105.19 ? 666 LEU A CD2 1 ATOM 5153 N N . SER A 1 667 ? -48.545 34.066 16.369 1.00 129.98 ? 667 SER A N 1 ATOM 5154 C CA . SER A 1 667 ? -47.306 34.513 15.754 1.00 130.63 ? 667 SER A CA 1 ATOM 5155 C C . SER A 1 667 ? -46.930 35.866 16.338 1.00 133.42 ? 667 SER A C 1 ATOM 5156 O O . SER A 1 667 ? -47.572 36.873 16.046 1.00 146.72 ? 667 SER A O 1 ATOM 5157 C CB . SER A 1 667 ? -47.443 34.598 14.235 1.00 137.69 ? 667 SER A CB 1 ATOM 5158 O OG . SER A 1 667 ? -46.199 34.914 13.637 1.00 148.22 ? 667 SER A OG 1 ATOM 5159 N N . CYS A 1 668 ? -45.887 35.887 17.160 1.00 136.67 ? 668 CYS A N 1 ATOM 5160 C CA . CYS A 1 668 ? -45.504 37.105 17.864 1.00 135.09 ? 668 CYS A CA 1 ATOM 5161 C C . CYS A 1 668 ? -44.005 37.357 17.800 1.00 139.19 ? 668 CYS A C 1 ATOM 5162 O O . CYS A 1 668 ? -43.201 36.431 17.914 1.00 150.48 ? 668 CYS A O 1 ATOM 5163 C CB . CYS A 1 668 ? -45.955 37.042 19.325 1.00 126.43 ? 668 CYS A CB 1 ATOM 5164 S SG . CYS A 1 668 ? -47.748 37.096 19.553 1.00 139.48 ? 668 CYS A SG 1 ATOM 5165 N N . ALA A 1 669 ? -43.639 38.620 17.620 1.00 128.89 ? 669 ALA A N 1 ATOM 5166 C CA . ALA A 1 669 ? -42.239 39.008 17.562 1.00 128.04 ? 669 ALA A CA 1 ATOM 5167 C C . ALA A 1 669 ? -42.017 40.332 18.278 1.00 133.37 ? 669 ALA A C 1 ATOM 5168 O O . ALA A 1 669 ? -42.793 41.274 18.118 1.00 125.82 ? 669 ALA A O 1 ATOM 5169 C CB . ALA A 1 669 ? -41.772 39.098 16.119 1.00 125.97 ? 669 ALA A CB 1 ATOM 5170 N N . PHE A 1 670 ? -40.956 40.392 19.076 1.00 146.83 ? 670 PHE A N 1 ATOM 5171 C CA . PHE A 1 670 ? -40.594 41.611 19.786 1.00 147.29 ? 670 PHE A CA 1 ATOM 5172 C C . PHE A 1 670 ? -39.884 42.570 18.841 1.00 140.41 ? 670 PHE A C 1 ATOM 5173 O O . PHE A 1 670 ? -38.955 42.177 18.136 1.00 148.67 ? 670 PHE A O 1 ATOM 5174 C CB . PHE A 1 670 ? -39.700 41.289 20.989 1.00 152.68 ? 670 PHE A CB 1 ATOM 5175 C CG . PHE A 1 670 ? -39.422 42.470 21.880 1.00 150.08 ? 670 PHE A CG 1 ATOM 5176 C CD1 . PHE A 1 670 ? -38.430 43.385 21.560 1.00 143.45 ? 670 PHE A CD1 1 ATOM 5177 C CD2 . PHE A 1 670 ? -40.145 42.657 23.045 1.00 150.76 ? 670 PHE A CD2 1 ATOM 5178 C CE1 . PHE A 1 670 ? -38.175 44.469 22.378 1.00 144.14 ? 670 PHE A CE1 1 ATOM 5179 C CE2 . PHE A 1 670 ? -39.892 43.736 23.868 1.00 154.94 ? 670 PHE A CE2 1 ATOM 5180 C CZ . PHE A 1 670 ? -38.906 44.644 23.534 1.00 152.97 ? 670 PHE A CZ 1 ATOM 5181 N N . LYS A 1 671 ? -40.321 43.824 18.822 1.00 129.80 ? 671 LYS A N 1 ATOM 5182 C CA . LYS A 1 671 ? -39.650 44.831 18.012 1.00 140.23 ? 671 LYS A CA 1 ATOM 5183 C C . LYS A 1 671 ? -39.758 46.222 18.628 1.00 140.58 ? 671 LYS A C 1 ATOM 5184 O O . LYS A 1 671 ? -40.786 46.582 19.203 1.00 126.12 ? 671 LYS A O 1 ATOM 5185 C CB . LYS A 1 671 ? -40.224 44.843 16.592 1.00 145.91 ? 671 LYS A CB 1 ATOM 5186 C CG . LYS A 1 671 ? -39.357 45.571 15.567 1.00 155.38 ? 671 LYS A CG 1 ATOM 5187 C CD . LYS A 1 671 ? -38.061 44.815 15.297 1.00 153.50 ? 671 LYS A CD 1 ATOM 5188 C CE . LYS A 1 671 ? -37.227 45.486 14.212 1.00 149.09 ? 671 LYS A CE 1 ATOM 5189 N NZ . LYS A 1 671 ? -36.653 46.788 14.653 1.00 141.48 ? 671 LYS A NZ 1 ATOM 5190 N N . THR A 1 672 ? -38.681 46.991 18.510 1.00 155.41 ? 672 THR A N 1 ATOM 5191 C CA . THR A 1 672 ? -38.690 48.403 18.866 1.00 155.99 ? 672 THR A CA 1 ATOM 5192 C C . THR A 1 672 ? -38.026 49.211 17.756 1.00 160.16 ? 672 THR A C 1 ATOM 5193 O O . THR A 1 672 ? -36.834 49.055 17.489 1.00 170.41 ? 672 THR A O 1 ATOM 5194 C CB . THR A 1 672 ? -37.974 48.664 20.207 1.00 150.91 ? 672 THR A CB 1 ATOM 5195 O OG1 . THR A 1 672 ? -37.558 50.034 20.268 1.00 152.68 ? 672 THR A OG1 1 ATOM 5196 C CG2 . THR A 1 672 ? -36.754 47.764 20.352 1.00 149.92 ? 672 THR A CG2 1 ATOM 5197 N N . GLU A 1 673 ? -38.799 50.073 17.108 1.00 154.52 ? 673 GLU A N 1 ATOM 5198 C CA . GLU A 1 673 ? -38.284 50.841 15.982 1.00 166.06 ? 673 GLU A CA 1 ATOM 5199 C C . GLU A 1 673 ? -38.271 52.332 16.283 1.00 167.77 ? 673 GLU A C 1 ATOM 5200 O O . GLU A 1 673 ? -37.208 52.920 16.477 1.00 158.19 ? 673 GLU A O 1 ATOM 5201 C CB . GLU A 1 673 ? -39.103 50.560 14.722 1.00 161.83 ? 673 GLU A CB 1 ATOM 5202 C CG . GLU A 1 673 ? -38.941 49.143 14.196 1.00 162.04 ? 673 GLU A CG 1 ATOM 5203 C CD . GLU A 1 673 ? -39.686 48.911 12.898 1.00 174.14 ? 673 GLU A CD 1 ATOM 5204 O OE1 . GLU A 1 673 ? -40.535 49.753 12.538 1.00 179.88 ? 673 GLU A OE1 1 ATOM 5205 O OE2 . GLU A 1 673 ? -39.418 47.886 12.235 1.00 178.31 ? 673 GLU A OE2 1 ATOM 5206 N N . ASN A 1 674 ? -39.449 52.944 16.327 1.00 169.71 ? 674 ASN A N 1 ATOM 5207 C CA . ASN A 1 674 ? -39.522 54.366 16.622 1.00 159.61 ? 674 ASN A CA 1 ATOM 5208 C C . ASN A 1 674 ? -39.947 54.632 18.057 1.00 147.80 ? 674 ASN A C 1 ATOM 5209 O O . ASN A 1 674 ? -41.112 54.455 18.414 1.00 127.92 ? 674 ASN A O 1 ATOM 5210 C CB . ASN A 1 674 ? -40.495 55.064 15.667 1.00 150.06 ? 674 ASN A CB 1 ATOM 5211 C CG . ASN A 1 674 ? -40.120 54.883 14.210 1.00 155.56 ? 674 ASN A CG 1 ATOM 5212 O OD1 . ASN A 1 674 ? -38.946 54.742 13.871 1.00 167.46 ? 674 ASN A OD1 1 ATOM 5213 N ND2 . ASN A 1 674 ? -41.122 54.889 13.337 1.00 147.72 ? 674 ASN A ND2 1 ATOM 5214 N N . GLN A 1 675 ? -38.984 55.039 18.879 1.00 153.55 ? 675 GLN A N 1 ATOM 5215 C CA . GLN A 1 675 ? -39.251 55.681 20.164 1.00 155.34 ? 675 GLN A CA 1 ATOM 5216 C C . GLN A 1 675 ? -39.996 54.814 21.188 1.00 147.11 ? 675 GLN A C 1 ATOM 5217 O O . GLN A 1 675 ? -40.140 55.213 22.343 1.00 143.35 ? 675 GLN A O 1 ATOM 5218 C CB . GLN A 1 675 ? -40.027 56.982 19.924 1.00 158.99 ? 675 GLN A CB 1 ATOM 5219 C CG . GLN A 1 675 ? -39.338 57.923 18.939 1.00 164.78 ? 675 GLN A CG 1 ATOM 5220 C CD . GLN A 1 675 ? -40.212 59.089 18.515 1.00 167.59 ? 675 GLN A CD 1 ATOM 5221 O OE1 . GLN A 1 675 ? -40.677 59.867 19.348 1.00 175.05 ? 675 GLN A OE1 1 ATOM 5222 N NE2 . GLN A 1 675 ? -40.439 59.216 17.211 1.00 150.48 ? 675 GLN A NE2 1 ATOM 5223 N N . THR A 1 676 ? -40.467 53.638 20.776 1.00 143.46 ? 676 THR A N 1 ATOM 5224 C CA . THR A 1 676 ? -41.312 52.816 21.645 1.00 140.73 ? 676 THR A CA 1 ATOM 5225 C C . THR A 1 676 ? -41.019 51.318 21.580 1.00 147.98 ? 676 THR A C 1 ATOM 5226 O O . THR A 1 676 ? -40.868 50.747 20.499 1.00 150.25 ? 676 THR A O 1 ATOM 5227 C CB . THR A 1 676 ? -42.807 53.003 21.312 1.00 130.26 ? 676 THR A CB 1 ATOM 5228 O OG1 . THR A 1 676 ? -43.024 52.737 19.921 1.00 120.37 ? 676 THR A OG1 1 ATOM 5229 C CG2 . THR A 1 676 ? -43.269 54.418 21.638 1.00 139.65 ? 676 THR A CG2 1 ATOM 5230 N N . ARG A 1 677 ? -40.952 50.692 22.753 1.00 150.55 ? 677 ARG A N 1 ATOM 5231 C CA . ARG A 1 677 ? -40.913 49.237 22.866 1.00 149.82 ? 677 ARG A CA 1 ATOM 5232 C C . ARG A 1 677 ? -42.328 48.684 22.771 1.00 147.88 ? 677 ARG A C 1 ATOM 5233 O O . ARG A 1 677 ? -43.269 49.317 23.253 1.00 147.37 ? 677 ARG A O 1 ATOM 5234 C CB . ARG A 1 677 ? -40.275 48.804 24.189 1.00 147.96 ? 677 ARG A CB 1 ATOM 5235 C CG . ARG A 1 677 ? -38.766 48.961 24.263 1.00 153.97 ? 677 ARG A CG 1 ATOM 5236 C CD . ARG A 1 677 ? -38.278 48.859 25.704 1.00 143.72 ? 677 ARG A CD 1 ATOM 5237 N NE . ARG A 1 677 ? -38.805 47.682 26.391 1.00 137.20 ? 677 ARG A NE 1 ATOM 5238 C CZ . ARG A 1 677 ? -38.146 46.535 26.528 1.00 136.07 ? 677 ARG A CZ 1 ATOM 5239 N NH1 . ARG A 1 677 ? -36.926 46.405 26.023 1.00 134.61 ? 677 ARG A NH1 1 ATOM 5240 N NH2 . ARG A 1 677 ? -38.705 45.519 27.171 1.00 136.45 ? 677 ARG A NH2 1 ATOM 5241 N N . GLN A 1 678 ? -42.470 47.498 22.180 1.00 143.97 ? 678 GLN A N 1 ATOM 5242 C CA . GLN A 1 678 ? -43.782 46.873 22.008 1.00 124.20 ? 678 GLN A CA 1 ATOM 5243 C C . GLN A 1 678 ? -43.706 45.475 21.399 1.00 117.69 ? 678 GLN A C 1 ATOM 5244 O O . GLN A 1 678 ? -42.687 45.085 20.829 1.00 124.63 ? 678 GLN A O 1 ATOM 5245 C CB . GLN A 1 678 ? -44.685 47.750 21.133 1.00 124.27 ? 678 GLN A CB 1 ATOM 5246 C CG . GLN A 1 678 ? -44.070 48.165 19.809 1.00 127.22 ? 678 GLN A CG 1 ATOM 5247 C CD . GLN A 1 678 ? -44.907 49.202 19.088 1.00 131.45 ? 678 GLN A CD 1 ATOM 5248 O OE1 . GLN A 1 678 ? -45.978 49.588 19.560 1.00 113.80 ? 678 GLN A OE1 1 ATOM 5249 N NE2 . GLN A 1 678 ? -44.422 49.662 17.940 1.00 139.44 ? 678 GLN A NE2 1 ATOM 5250 N N . VAL A 1 679 ? -44.803 44.731 21.525 1.00 115.16 ? 679 VAL A N 1 ATOM 5251 C CA . VAL A 1 679 ? -44.897 43.374 20.993 1.00 117.65 ? 679 VAL A CA 1 ATOM 5252 C C . VAL A 1 679 ? -46.033 43.257 19.979 1.00 117.37 ? 679 VAL A C 1 ATOM 5253 O O . VAL A 1 679 ? -47.176 43.612 20.271 1.00 111.73 ? 679 VAL A O 1 ATOM 5254 C CB . VAL A 1 679 ? -45.122 42.342 22.113 1.00 113.55 ? 679 VAL A CB 1 ATOM 5255 C CG1 . VAL A 1 679 ? -45.255 40.945 21.528 1.00 113.92 ? 679 VAL A CG1 1 ATOM 5256 C CG2 . VAL A 1 679 ? -43.986 42.395 23.120 1.00 122.06 ? 679 VAL A CG2 1 ATOM 5257 N N . VAL A 1 680 ? -45.714 42.751 18.792 1.00 118.63 ? 680 VAL A N 1 ATOM 5258 C CA . VAL A 1 680 ? -46.691 42.638 17.714 1.00 111.59 ? 680 VAL A CA 1 ATOM 5259 C C . VAL A 1 680 ? -47.119 41.191 17.481 1.00 110.39 ? 680 VAL A C 1 ATOM 5260 O O . VAL A 1 680 ? -46.280 40.305 17.331 1.00 116.69 ? 680 VAL A O 1 ATOM 5261 C CB . VAL A 1 680 ? -46.135 43.211 16.400 1.00 109.98 ? 680 VAL A CB 1 ATOM 5262 C CG1 . VAL A 1 680 ? -47.167 43.095 15.291 1.00 111.18 ? 680 VAL A CG1 1 ATOM 5263 C CG2 . VAL A 1 680 ? -45.711 44.657 16.593 1.00 107.02 ? 680 VAL A CG2 1 ATOM 5264 N N . CYS A 1 681 ? -48.427 40.961 17.450 1.00 112.36 ? 681 CYS A N 1 ATOM 5265 C CA . CYS A 1 681 ? -48.966 39.627 17.205 1.00 124.26 ? 681 CYS A CA 1 ATOM 5266 C C . CYS A 1 681 ? -49.896 39.616 15.995 1.00 121.58 ? 681 CYS A C 1 ATOM 5267 O O . CYS A 1 681 ? -50.824 40.418 15.911 1.00 123.24 ? 681 CYS A O 1 ATOM 5268 C CB . CYS A 1 681 ? -49.708 39.113 18.441 1.00 123.33 ? 681 CYS A CB 1 ATOM 5269 S SG . CYS A 1 681 ? -48.660 38.881 19.891 1.00 150.32 ? 681 CYS A SG 1 ATOM 5270 N N . ASP A 1 682 ? -49.648 38.699 15.065 1.00 122.17 ? 682 ASP A N 1 ATOM 5271 C CA . ASP A 1 682 ? -50.457 38.610 13.856 1.00 125.39 ? 682 ASP A CA 1 ATOM 5272 C C . ASP A 1 682 ? -51.775 37.891 14.130 1.00 117.15 ? 682 ASP A C 1 ATOM 5273 O O . ASP A 1 682 ? -51.791 36.734 14.547 1.00 116.50 ? 682 ASP A O 1 ATOM 5274 C CB . ASP A 1 682 ? -49.686 37.897 12.742 1.00 141.33 ? 682 ASP A CB 1 ATOM 5275 C CG . ASP A 1 682 ? -50.458 37.852 11.432 1.00 162.14 ? 682 ASP A CG 1 ATOM 5276 O OD1 . ASP A 1 682 ? -51.271 38.768 11.183 1.00 163.30 ? 682 ASP A OD1 1 ATOM 5277 O OD2 . ASP A 1 682 ? -50.251 36.901 10.648 1.00 165.66 ? 682 ASP A OD2 1 ATOM 5278 N N . LEU A 1 683 ? -52.877 38.593 13.888 1.00 107.94 ? 683 LEU A N 1 ATOM 5279 C CA . LEU A 1 683 ? -54.213 38.051 14.102 1.00 104.26 ? 683 LEU A CA 1 ATOM 5280 C C . LEU A 1 683 ? -54.772 37.446 12.818 1.00 100.28 ? 683 LEU A C 1 ATOM 5281 O O . LEU A 1 683 ? -55.935 37.043 12.758 1.00 90.31 ? 683 LEU A O 1 ATOM 5282 C CB . LEU A 1 683 ? -55.147 39.136 14.635 1.00 102.83 ? 683 LEU A CB 1 ATOM 5283 C CG . LEU A 1 683 ? -54.711 39.740 15.970 1.00 98.87 ? 683 LEU A CG 1 ATOM 5284 C CD1 . LEU A 1 683 ? -55.757 40.706 16.488 1.00 106.72 ? 683 LEU A CD1 1 ATOM 5285 C CD2 . LEU A 1 683 ? -54.444 38.643 16.984 1.00 100.07 ? 683 LEU A CD2 1 ATOM 5286 N N . GLY A 1 684 ? -53.931 37.396 11.791 1.00 101.37 ? 684 GLY A N 1 ATOM 5287 C CA . GLY A 1 684 ? -54.315 36.846 10.506 1.00 109.32 ? 684 GLY A CA 1 ATOM 5288 C C . GLY A 1 684 ? -54.557 37.907 9.453 1.00 115.19 ? 684 GLY A C 1 ATOM 5289 O O . GLY A 1 684 ? -54.987 39.020 9.751 1.00 121.64 ? 684 GLY A O 1 ATOM 5290 N N . ASN A 1 685 ? -54.277 37.543 8.207 1.00 114.02 ? 685 ASN A N 1 ATOM 5291 C CA . ASN A 1 685 ? -54.320 38.474 7.090 1.00 106.63 ? 685 ASN A CA 1 ATOM 5292 C C . ASN A 1 685 ? -55.031 37.880 5.879 1.00 105.86 ? 685 ASN A C 1 ATOM 5293 O O . ASN A 1 685 ? -54.396 37.229 5.050 1.00 116.79 ? 685 ASN A O 1 ATOM 5294 C CB . ASN A 1 685 ? -52.899 38.900 6.712 1.00 116.61 ? 685 ASN A CB 1 ATOM 5295 C CG . ASN A 1 685 ? -52.875 39.961 5.632 1.00 118.74 ? 685 ASN A CG 1 ATOM 5296 O OD1 . ASN A 1 685 ? -53.851 40.682 5.432 1.00 124.39 ? 685 ASN A OD1 1 ATOM 5297 N ND2 . ASN A 1 685 ? -51.753 40.063 4.928 1.00 115.75 ? 685 ASN A ND2 1 ATOM 5298 N N . PRO A 1 686 ? -56.350 38.100 5.763 1.00 100.85 ? 686 PRO A N 1 ATOM 5299 C CA . PRO A 1 686 ? -57.224 38.893 6.635 1.00 97.13 ? 686 PRO A CA 1 ATOM 5300 C C . PRO A 1 686 ? -57.651 38.179 7.911 1.00 94.53 ? 686 PRO A C 1 ATOM 5301 O O . PRO A 1 686 ? -57.621 36.952 7.977 1.00 99.73 ? 686 PRO A O 1 ATOM 5302 C CB . PRO A 1 686 ? -58.458 39.158 5.754 1.00 94.99 ? 686 PRO A CB 1 ATOM 5303 C CG . PRO A 1 686 ? -58.104 38.645 4.376 1.00 101.88 ? 686 PRO A CG 1 ATOM 5304 C CD . PRO A 1 686 ? -57.082 37.590 4.595 1.00 102.34 ? 686 PRO A CD 1 ATOM 5305 N N . MET A 1 687 ? -58.056 38.955 8.910 1.00 95.21 ? 687 MET A N 1 ATOM 5306 C CA . MET A 1 687 ? -58.738 38.408 10.072 1.00 83.49 ? 687 MET A CA 1 ATOM 5307 C C . MET A 1 687 ? -60.230 38.480 9.797 1.00 94.00 ? 687 MET A C 1 ATOM 5308 O O . MET A 1 687 ? -60.810 39.564 9.760 1.00 87.75 ? 687 MET A O 1 ATOM 5309 C CB . MET A 1 687 ? -58.376 39.184 11.337 1.00 91.54 ? 687 MET A CB 1 ATOM 5310 C CG . MET A 1 687 ? -59.149 38.775 12.582 1.00 86.28 ? 687 MET A CG 1 ATOM 5311 S SD . MET A 1 687 ? -58.652 39.733 14.031 1.00 113.33 ? 687 MET A SD 1 ATOM 5312 C CE . MET A 1 687 ? -59.585 38.920 15.324 1.00 98.84 ? 687 MET A CE 1 ATOM 5313 N N . LYS A 1 688 ? -60.847 37.319 9.609 1.00 127.50 ? 688 LYS A N 1 ATOM 5314 C CA . LYS A 1 688 ? -62.220 37.256 9.123 1.00 115.04 ? 688 LYS A CA 1 ATOM 5315 C C . LYS A 1 688 ? -63.215 37.550 10.235 1.00 121.29 ? 688 LYS A C 1 ATOM 5316 O O . LYS A 1 688 ? -62.821 37.861 11.358 1.00 130.98 ? 688 LYS A O 1 ATOM 5317 C CB . LYS A 1 688 ? -62.491 35.887 8.497 1.00 84.36 ? 688 LYS A CB 1 ATOM 5318 C CG . LYS A 1 688 ? -61.448 35.494 7.458 1.00 97.80 ? 688 LYS A CG 1 ATOM 5319 C CD . LYS A 1 688 ? -62.005 34.559 6.397 1.00 105.70 ? 688 LYS A CD 1 ATOM 5320 C CE . LYS A 1 688 ? -62.202 33.153 6.931 1.00 113.84 ? 688 LYS A CE 1 ATOM 5321 N NZ . LYS A 1 688 ? -62.675 32.230 5.862 1.00 132.93 ? 688 LYS A NZ 1 ATOM 5322 N N . ALA A 1 689 ? -64.504 37.449 9.927 1.00 122.07 ? 689 ALA A N 1 ATOM 5323 C CA . ALA A 1 689 ? -65.532 37.719 10.924 1.00 104.25 ? 689 ALA A CA 1 ATOM 5324 C C . ALA A 1 689 ? -65.539 36.590 11.945 1.00 119.45 ? 689 ALA A C 1 ATOM 5325 O O . ALA A 1 689 ? -64.812 35.607 11.787 1.00 106.63 ? 689 ALA A O 1 ATOM 5326 C CB . ALA A 1 689 ? -66.893 37.862 10.270 1.00 85.10 ? 689 ALA A CB 1 ATOM 5327 N N . GLY A 1 690 ? -66.372 36.708 12.974 1.00 125.49 ? 690 GLY A N 1 ATOM 5328 C CA . GLY A 1 690 ? -66.291 35.770 14.076 1.00 117.75 ? 690 GLY A CA 1 ATOM 5329 C C . GLY A 1 690 ? -64.892 35.885 14.647 1.00 126.85 ? 690 GLY A C 1 ATOM 5330 O O . GLY A 1 690 ? -64.488 36.952 15.109 1.00 115.68 ? 690 GLY A O 1 ATOM 5331 N N . THR A 1 691 ? -64.161 34.775 14.626 1.00 135.21 ? 691 THR A N 1 ATOM 5332 C CA . THR A 1 691 ? -62.735 34.773 14.939 1.00 147.51 ? 691 THR A CA 1 ATOM 5333 C C . THR A 1 691 ? -62.453 35.294 16.343 1.00 143.12 ? 691 THR A C 1 ATOM 5334 O O . THR A 1 691 ? -61.871 36.365 16.515 1.00 136.41 ? 691 THR A O 1 ATOM 5335 C CB . THR A 1 691 ? -61.930 35.622 13.922 1.00 89.42 ? 691 THR A CB 1 ATOM 5336 O OG1 . THR A 1 691 ? -62.489 35.471 12.612 1.00 94.21 ? 691 THR A OG1 1 ATOM 5337 C CG2 . THR A 1 691 ? -60.467 35.200 13.901 1.00 80.02 ? 691 THR A CG2 1 ATOM 5338 N N . GLN A 1 692 ? -62.880 34.538 17.347 1.00 135.56 ? 692 GLN A N 1 ATOM 5339 C CA . GLN A 1 692 ? -62.530 34.860 18.719 1.00 128.20 ? 692 GLN A CA 1 ATOM 5340 C C . GLN A 1 692 ? -61.275 34.082 19.074 1.00 122.89 ? 692 GLN A C 1 ATOM 5341 O O . GLN A 1 692 ? -61.304 32.857 19.183 1.00 127.17 ? 692 GLN A O 1 ATOM 5342 C CB . GLN A 1 692 ? -63.673 34.521 19.678 1.00 141.40 ? 692 GLN A CB 1 ATOM 5343 C CG . GLN A 1 692 ? -64.987 35.213 19.351 1.00 144.98 ? 692 GLN A CG 1 ATOM 5344 C CD . GLN A 1 692 ? -66.061 34.940 20.385 1.00 154.79 ? 692 GLN A CD 1 ATOM 5345 O OE1 . GLN A 1 692 ? -65.765 34.588 21.528 1.00 162.08 ? 692 GLN A OE1 1 ATOM 5346 N NE2 . GLN A 1 692 ? -67.319 35.099 19.989 1.00 141.83 ? 692 GLN A NE2 1 ATOM 5347 N N . LEU A 1 693 ? -60.170 34.798 19.249 1.00 110.39 ? 693 LEU A N 1 ATOM 5348 C CA . LEU A 1 693 ? -58.894 34.151 19.513 1.00 101.73 ? 693 LEU A CA 1 ATOM 5349 C C . LEU A 1 693 ? -58.439 34.344 20.948 1.00 108.89 ? 693 LEU A C 1 ATOM 5350 O O . LEU A 1 693 ? -58.482 35.450 21.485 1.00 108.62 ? 693 LEU A O 1 ATOM 5351 C CB . LEU A 1 693 ? -57.819 34.672 18.561 1.00 85.67 ? 693 LEU A CB 1 ATOM 5352 C CG . LEU A 1 693 ? -58.054 34.426 17.072 1.00 97.11 ? 693 LEU A CG 1 ATOM 5353 C CD1 . LEU A 1 693 ? -56.778 34.685 16.288 1.00 103.51 ? 693 LEU A CD1 1 ATOM 5354 C CD2 . LEU A 1 693 ? -58.566 33.015 16.831 1.00 123.13 ? 693 LEU A CD2 1 ATOM 5355 N N . LEU A 1 694 ? -58.002 33.251 21.561 1.00 120.35 ? 694 LEU A N 1 ATOM 5356 C CA . LEU A 1 694 ? -57.406 33.292 22.886 1.00 109.40 ? 694 LEU A CA 1 ATOM 5357 C C . LEU A 1 694 ? -55.922 32.983 22.755 1.00 115.82 ? 694 LEU A C 1 ATOM 5358 O O . LEU A 1 694 ? -55.515 32.233 21.865 1.00 131.50 ? 694 LEU A O 1 ATOM 5359 C CB . LEU A 1 694 ? -58.085 32.297 23.834 1.00 111.96 ? 694 LEU A CB 1 ATOM 5360 C CG . LEU A 1 694 ? -59.526 32.575 24.281 1.00 118.40 ? 694 LEU A CG 1 ATOM 5361 C CD1 . LEU A 1 694 ? -59.688 34.028 24.710 1.00 101.79 ? 694 LEU A CD1 1 ATOM 5362 C CD2 . LEU A 1 694 ? -60.550 32.197 23.210 1.00 128.02 ? 694 LEU A CD2 1 ATOM 5363 N N . ALA A 1 695 ? -55.124 33.539 23.659 1.00 114.58 ? 695 ALA A N 1 ATOM 5364 C CA . ALA A 1 695 ? -53.671 33.423 23.594 1.00 111.22 ? 695 ALA A CA 1 ATOM 5365 C C . ALA A 1 695 ? -53.049 34.047 24.828 1.00 114.19 ? 695 ALA A C 1 ATOM 5366 O O . ALA A 1 695 ? -53.731 34.706 25.611 1.00 121.14 ? 695 ALA A O 1 ATOM 5367 C CB . ALA A 1 695 ? -53.130 34.089 22.336 1.00 107.35 ? 695 ALA A CB 1 ATOM 5368 N N . GLY A 1 696 ? -51.748 33.848 24.997 1.00 113.07 ? 696 GLY A N 1 ATOM 5369 C CA . GLY A 1 696 ? -51.065 34.393 26.151 1.00 110.62 ? 696 GLY A CA 1 ATOM 5370 C C . GLY A 1 696 ? -49.608 34.698 25.886 1.00 110.10 ? 696 GLY A C 1 ATOM 5371 O O . GLY A 1 696 ? -48.971 34.088 25.028 1.00 110.88 ? 696 GLY A O 1 ATOM 5372 N N . LEU A 1 697 ? -49.078 35.644 26.650 1.00 113.57 ? 697 LEU A N 1 ATOM 5373 C CA . LEU A 1 697 ? -47.723 36.127 26.446 1.00 128.73 ? 697 LEU A CA 1 ATOM 5374 C C . LEU A 1 697 ? -46.992 36.188 27.778 1.00 134.49 ? 697 LEU A C 1 ATOM 5375 O O . LEU A 1 697 ? -47.509 36.729 28.756 1.00 129.73 ? 697 LEU A O 1 ATOM 5376 C CB . LEU A 1 697 ? -47.730 37.505 25.777 1.00 129.84 ? 697 LEU A CB 1 ATOM 5377 C CG . LEU A 1 697 ? -48.351 37.671 24.384 1.00 114.04 ? 697 LEU A CG 1 ATOM 5378 C CD1 . LEU A 1 697 ? -49.864 37.844 24.448 1.00 100.22 ? 697 LEU A CD1 1 ATOM 5379 C CD2 . LEU A 1 697 ? -47.711 38.845 23.659 1.00 108.82 ? 697 LEU A CD2 1 ATOM 5380 N N . ARG A 1 698 ? -45.788 35.630 27.812 1.00 130.66 ? 698 ARG A N 1 ATOM 5381 C CA . ARG A 1 698 ? -45.027 35.556 29.049 1.00 129.38 ? 698 ARG A CA 1 ATOM 5382 C C . ARG A 1 698 ? -44.068 36.732 29.188 1.00 126.85 ? 698 ARG A C 1 ATOM 5383 O O . ARG A 1 698 ? -43.455 37.171 28.216 1.00 127.84 ? 698 ARG A O 1 ATOM 5384 C CB . ARG A 1 698 ? -44.264 34.233 29.123 1.00 144.86 ? 698 ARG A CB 1 ATOM 5385 C CG . ARG A 1 698 ? -45.159 33.010 29.015 1.00 141.57 ? 698 ARG A CG 1 ATOM 5386 C CD . ARG A 1 698 ? -44.428 31.741 29.413 1.00 136.81 ? 698 ARG A CD 1 ATOM 5387 N NE . ARG A 1 698 ? -45.316 30.583 29.398 1.00 139.85 ? 698 ARG A NE 1 ATOM 5388 C CZ . ARG A 1 698 ? -46.136 30.258 30.392 1.00 150.48 ? 698 ARG A CZ 1 ATOM 5389 N NH1 . ARG A 1 698 ? -46.186 31.008 31.485 1.00 149.21 ? 698 ARG A NH1 1 ATOM 5390 N NH2 . ARG A 1 698 ? -46.910 29.186 30.292 1.00 157.28 ? 698 ARG A NH2 1 ATOM 5391 N N . PHE A 1 699 ? -43.956 37.243 30.408 1.00 129.13 ? 699 PHE A N 1 ATOM 5392 C CA . PHE A 1 699 ? -43.090 38.376 30.696 1.00 135.68 ? 699 PHE A CA 1 ATOM 5393 C C . PHE A 1 699 ? -42.334 38.165 32.001 1.00 145.86 ? 699 PHE A C 1 ATOM 5394 O O . PHE A 1 699 ? -42.813 37.474 32.901 1.00 156.72 ? 699 PHE A O 1 ATOM 5395 C CB . PHE A 1 699 ? -43.902 39.670 30.777 1.00 146.81 ? 699 PHE A CB 1 ATOM 5396 C CG . PHE A 1 699 ? -44.601 40.037 29.501 1.00 144.65 ? 699 PHE A CG 1 ATOM 5397 C CD1 . PHE A 1 699 ? -45.827 39.478 29.181 1.00 136.73 ? 699 PHE A CD1 1 ATOM 5398 C CD2 . PHE A 1 699 ? -44.043 40.957 28.630 1.00 143.57 ? 699 PHE A CD2 1 ATOM 5399 C CE1 . PHE A 1 699 ? -46.472 39.818 28.012 1.00 129.75 ? 699 PHE A CE1 1 ATOM 5400 C CE2 . PHE A 1 699 ? -44.688 41.303 27.460 1.00 134.92 ? 699 PHE A CE2 1 ATOM 5401 C CZ . PHE A 1 699 ? -45.902 40.731 27.150 1.00 131.73 ? 699 PHE A CZ 1 ATOM 5402 N N . SER A 1 700 ? -41.152 38.762 32.100 1.00 143.49 ? 700 SER A N 1 ATOM 5403 C CA . SER A 1 700 ? -40.408 38.780 33.353 1.00 154.17 ? 700 SER A CA 1 ATOM 5404 C C . SER A 1 700 ? -40.018 40.214 33.687 1.00 159.32 ? 700 SER A C 1 ATOM 5405 O O . SER A 1 700 ? -39.235 40.836 32.971 1.00 156.90 ? 700 SER A O 1 ATOM 5406 C CB . SER A 1 700 ? -39.167 37.889 33.271 1.00 155.04 ? 700 SER A CB 1 ATOM 5407 O OG . SER A 1 700 ? -38.221 38.409 32.353 1.00 158.23 ? 700 SER A OG 1 ATOM 5408 N N . VAL A 1 701 ? -40.566 40.737 34.779 1.00 157.13 ? 701 VAL A N 1 ATOM 5409 C CA . VAL A 1 701 ? -40.354 42.134 35.132 1.00 146.06 ? 701 VAL A CA 1 ATOM 5410 C C . VAL A 1 701 ? -39.180 42.334 36.088 1.00 148.73 ? 701 VAL A C 1 ATOM 5411 O O . VAL A 1 701 ? -39.135 41.762 37.178 1.00 145.24 ? 701 VAL A O 1 ATOM 5412 C CB . VAL A 1 701 ? -41.624 42.744 35.751 1.00 134.21 ? 701 VAL A CB 1 ATOM 5413 C CG1 . VAL A 1 701 ? -42.581 43.184 34.659 1.00 132.86 ? 701 VAL A CG1 1 ATOM 5414 C CG2 . VAL A 1 701 ? -42.294 41.746 36.675 1.00 136.87 ? 701 VAL A CG2 1 ATOM 5415 N N . HIS A 1 702 ? -38.227 43.151 35.652 1.00 151.17 ? 702 HIS A N 1 ATOM 5416 C CA . HIS A 1 702 ? -37.063 43.514 36.452 1.00 152.54 ? 702 HIS A CA 1 ATOM 5417 C C . HIS A 1 702 ? -37.351 44.815 37.190 1.00 155.55 ? 702 HIS A C 1 ATOM 5418 O O . HIS A 1 702 ? -36.466 45.413 37.801 1.00 164.04 ? 702 HIS A O 1 ATOM 5419 C CB . HIS A 1 702 ? -35.825 43.648 35.567 1.00 163.94 ? 702 HIS A CB 1 ATOM 5420 C CG . HIS A 1 702 ? -35.586 42.463 34.682 1.00 173.75 ? 702 HIS A CG 1 ATOM 5421 N ND1 . HIS A 1 702 ? -34.835 42.534 33.529 1.00 179.23 ? 702 HIS A ND1 1 ATOM 5422 C CD2 . HIS A 1 702 ? -36.001 41.178 34.782 1.00 170.34 ? 702 HIS A CD2 1 ATOM 5423 C CE1 . HIS A 1 702 ? -34.798 41.344 32.956 1.00 174.91 ? 702 HIS A CE1 1 ATOM 5424 N NE2 . HIS A 1 702 ? -35.497 40.503 33.697 1.00 170.20 ? 702 HIS A NE2 1 ATOM 5425 N N . GLN A 1 703 ? -38.602 45.250 37.061 1.00 154.42 ? 703 GLN A N 1 ATOM 5426 C CA . GLN A 1 703 ? -39.174 46.471 37.642 1.00 156.59 ? 703 GLN A CA 1 ATOM 5427 C C . GLN A 1 703 ? -38.337 47.735 37.401 1.00 161.55 ? 703 GLN A C 1 ATOM 5428 O O . GLN A 1 703 ? -37.691 47.871 36.362 1.00 170.16 ? 703 GLN A O 1 ATOM 5429 C CB . GLN A 1 703 ? -39.457 46.287 39.154 1.00 149.59 ? 703 GLN A CB 1 ATOM 5430 C CG . GLN A 1 703 ? -38.264 46.102 40.104 1.00 149.70 ? 703 GLN A CG 1 ATOM 5431 C CD . GLN A 1 703 ? -37.913 44.647 40.342 1.00 154.85 ? 703 GLN A CD 1 ATOM 5432 O OE1 . GLN A 1 703 ? -38.760 43.762 40.221 1.00 164.47 ? 703 GLN A OE1 1 ATOM 5433 N NE2 . GLN A 1 703 ? -36.653 44.392 40.677 1.00 152.51 ? 703 GLN A NE2 1 ATOM 5434 N N . GLN A 1 704 ? -38.315 48.622 38.392 1.00 154.27 ? 704 GLN A N 1 ATOM 5435 C CA . GLN A 1 704 ? -37.922 50.014 38.201 1.00 157.88 ? 704 GLN A CA 1 ATOM 5436 C C . GLN A 1 704 ? -38.126 50.719 39.533 1.00 161.52 ? 704 GLN A C 1 ATOM 5437 O O . GLN A 1 704 ? -38.582 50.083 40.487 1.00 163.55 ? 704 GLN A O 1 ATOM 5438 C CB . GLN A 1 704 ? -38.769 50.671 37.103 1.00 145.56 ? 704 GLN A CB 1 ATOM 5439 C CG . GLN A 1 704 ? -38.196 51.944 36.506 1.00 139.30 ? 704 GLN A CG 1 ATOM 5440 C CD . GLN A 1 704 ? -36.966 51.685 35.667 1.00 149.92 ? 704 GLN A CD 1 ATOM 5441 O OE1 . GLN A 1 704 ? -35.841 51.734 36.163 1.00 167.99 ? 704 GLN A OE1 1 ATOM 5442 N NE2 . GLN A 1 704 ? -37.173 51.404 34.385 1.00 134.61 ? 704 GLN A NE2 1 ATOM 5443 N N . SER A 1 705 ? -37.795 52.009 39.612 1.00 148.40 ? 705 SER A N 1 ATOM 5444 C CA . SER A 1 705 ? -38.334 52.830 40.694 1.00 136.32 ? 705 SER A CA 1 ATOM 5445 C C . SER A 1 705 ? -37.977 52.304 42.077 1.00 146.01 ? 705 SER A C 1 ATOM 5446 O O . SER A 1 705 ? -36.859 52.510 42.549 1.00 145.46 ? 705 SER A O 1 ATOM 5447 C CB . SER A 1 705 ? -39.847 52.959 40.559 1.00 135.58 ? 705 SER A CB 1 ATOM 5448 O OG . SER A 1 705 ? -40.186 53.665 39.378 1.00 154.19 ? 705 SER A OG 1 ATOM 5449 N N . GLU A 1 706 ? -38.962 51.629 42.680 1.00 148.97 ? 706 GLU A N 1 ATOM 5450 C CA . GLU A 1 706 ? -39.186 51.402 44.115 1.00 138.43 ? 706 GLU A CA 1 ATOM 5451 C C . GLU A 1 706 ? -40.127 52.481 44.626 1.00 120.40 ? 706 GLU A C 1 ATOM 5452 O O . GLU A 1 706 ? -40.588 52.430 45.765 1.00 125.85 ? 706 GLU A O 1 ATOM 5453 C CB . GLU A 1 706 ? -37.889 51.396 44.938 1.00 128.65 ? 706 GLU A CB 1 ATOM 5454 C CG . GLU A 1 706 ? -36.934 50.247 44.625 1.00 135.82 ? 706 GLU A CG 1 ATOM 5455 C CD . GLU A 1 706 ? -35.556 50.452 45.232 1.00 141.47 ? 706 GLU A CD 1 ATOM 5456 O OE1 . GLU A 1 706 ? -35.393 51.390 46.042 1.00 134.43 ? 706 GLU A OE1 1 ATOM 5457 O OE2 . GLU A 1 706 ? -34.635 49.678 44.896 1.00 139.89 ? 706 GLU A OE2 1 ATOM 5458 N N . MET A 1 707 ? -40.418 53.452 43.769 1.00 111.09 ? 707 MET A N 1 ATOM 5459 C CA . MET A 1 707 ? -41.541 54.351 43.996 1.00 114.22 ? 707 MET A CA 1 ATOM 5460 C C . MET A 1 707 ? -42.759 53.929 43.174 1.00 125.03 ? 707 MET A C 1 ATOM 5461 O O . MET A 1 707 ? -43.820 54.547 43.265 1.00 139.37 ? 707 MET A O 1 ATOM 5462 C CB . MET A 1 707 ? -41.151 55.792 43.671 1.00 108.18 ? 707 MET A CB 1 ATOM 5463 C CG . MET A 1 707 ? -40.117 56.373 44.622 1.00 118.97 ? 707 MET A CG 1 ATOM 5464 S SD . MET A 1 707 ? -40.633 56.274 46.349 1.00 180.58 ? 707 MET A SD 1 ATOM 5465 C CE . MET A 1 707 ? -39.196 56.955 47.176 1.00 126.01 ? 707 MET A CE 1 ATOM 5466 N N . ASP A 1 708 ? -42.606 52.875 42.377 1.00 111.19 ? 708 ASP A N 1 ATOM 5467 C CA . ASP A 1 708 ? -43.665 52.452 41.460 1.00 120.47 ? 708 ASP A CA 1 ATOM 5468 C C . ASP A 1 708 ? -44.723 51.592 42.135 1.00 121.44 ? 708 ASP A C 1 ATOM 5469 O O . ASP A 1 708 ? -44.410 50.593 42.780 1.00 133.48 ? 708 ASP A O 1 ATOM 5470 C CB . ASP A 1 708 ? -43.079 51.689 40.271 1.00 119.75 ? 708 ASP A CB 1 ATOM 5471 C CG . ASP A 1 708 ? -42.940 52.554 39.033 1.00 131.49 ? 708 ASP A CG 1 ATOM 5472 O OD1 . ASP A 1 708 ? -43.783 53.455 38.837 1.00 147.81 ? 708 ASP A OD1 1 ATOM 5473 O OD2 . ASP A 1 708 ? -41.988 52.334 38.255 1.00 128.01 ? 708 ASP A OD2 1 ATOM 5474 N N . THR A 1 709 ? -45.978 52.001 41.988 1.00 113.29 ? 709 THR A N 1 ATOM 5475 C CA . THR A 1 709 ? -47.108 51.227 42.482 1.00 115.29 ? 709 THR A CA 1 ATOM 5476 C C . THR A 1 709 ? -47.531 50.116 41.517 1.00 110.94 ? 709 THR A C 1 ATOM 5477 O O . THR A 1 709 ? -47.846 49.004 41.943 1.00 99.53 ? 709 THR A O 1 ATOM 5478 C CB . THR A 1 709 ? -48.317 52.132 42.754 1.00 123.09 ? 709 THR A CB 1 ATOM 5479 O OG1 . THR A 1 709 ? -48.759 52.719 41.525 1.00 134.24 ? 709 THR A OG1 1 ATOM 5480 C CG2 . THR A 1 709 ? -47.941 53.233 43.735 1.00 117.90 ? 709 THR A CG2 1 ATOM 5481 N N . SER A 1 710 ? -47.542 50.424 40.222 1.00 118.41 ? 710 SER A N 1 ATOM 5482 C CA . SER A 1 710 ? -48.072 49.504 39.214 1.00 114.70 ? 710 SER A CA 1 ATOM 5483 C C . SER A 1 710 ? -47.223 49.459 37.945 1.00 112.26 ? 710 SER A C 1 ATOM 5484 O O . SER A 1 710 ? -46.338 50.292 37.749 1.00 128.72 ? 710 SER A O 1 ATOM 5485 C CB . SER A 1 710 ? -49.507 49.893 38.847 1.00 126.32 ? 710 SER A CB 1 ATOM 5486 O OG . SER A 1 710 ? -50.322 50.014 39.999 1.00 151.29 ? 710 SER A OG 1 ATOM 5487 N N . VAL A 1 711 ? -47.496 48.477 37.091 1.00 110.43 ? 711 VAL A N 1 ATOM 5488 C CA . VAL A 1 711 ? -46.893 48.422 35.759 1.00 120.10 ? 711 VAL A CA 1 ATOM 5489 C C . VAL A 1 711 ? -47.977 48.441 34.680 1.00 129.59 ? 711 VAL A C 1 ATOM 5490 O O . VAL A 1 711 ? -49.016 47.794 34.816 1.00 128.76 ? 711 VAL A O 1 ATOM 5491 C CB . VAL A 1 711 ? -46.007 47.180 35.582 1.00 111.30 ? 711 VAL A CB 1 ATOM 5492 C CG1 . VAL A 1 711 ? -44.722 47.333 36.379 1.00 114.95 ? 711 VAL A CG1 1 ATOM 5493 C CG2 . VAL A 1 711 ? -46.756 45.931 36.000 1.00 105.82 ? 711 VAL A CG2 1 ATOM 5494 N N . LYS A 1 712 ? -47.724 49.182 33.605 1.00 130.87 ? 712 LYS A N 1 ATOM 5495 C CA . LYS A 1 712 ? -48.764 49.494 32.629 1.00 119.91 ? 712 LYS A CA 1 ATOM 5496 C C . LYS A 1 712 ? -48.616 48.769 31.293 1.00 113.11 ? 712 LYS A C 1 ATOM 5497 O O . LYS A 1 712 ? -47.593 48.886 30.617 1.00 113.34 ? 712 LYS A O 1 ATOM 5498 C CB . LYS A 1 712 ? -48.799 51.004 32.381 1.00 130.57 ? 712 LYS A CB 1 ATOM 5499 C CG . LYS A 1 712 ? -49.678 51.424 31.216 1.00 129.76 ? 712 LYS A CG 1 ATOM 5500 C CD . LYS A 1 712 ? -49.460 52.886 30.861 1.00 130.15 ? 712 LYS A CD 1 ATOM 5501 C CE . LYS A 1 712 ? -49.206 53.057 29.371 1.00 124.92 ? 712 LYS A CE 1 ATOM 5502 N NZ . LYS A 1 712 ? -47.990 52.317 28.925 1.00 112.67 ? 712 LYS A NZ 1 ATOM 5503 N N . PHE A 1 713 ? -49.659 48.032 30.919 1.00 109.76 ? 713 PHE A N 1 ATOM 5504 C CA . PHE A 1 713 ? -49.762 47.429 29.594 1.00 106.47 ? 713 PHE A CA 1 ATOM 5505 C C . PHE A 1 713 ? -50.977 47.986 28.856 1.00 108.49 ? 713 PHE A C 1 ATOM 5506 O O . PHE A 1 713 ? -52.081 47.997 29.397 1.00 114.89 ? 713 PHE A O 1 ATOM 5507 C CB . PHE A 1 713 ? -49.871 45.906 29.690 1.00 112.16 ? 713 PHE A CB 1 ATOM 5508 C CG . PHE A 1 713 ? -48.579 45.217 30.025 1.00 115.92 ? 713 PHE A CG 1 ATOM 5509 C CD1 . PHE A 1 713 ? -48.245 44.946 31.340 1.00 111.75 ? 713 PHE A CD1 1 ATOM 5510 C CD2 . PHE A 1 713 ? -47.707 44.826 29.023 1.00 126.55 ? 713 PHE A CD2 1 ATOM 5511 C CE1 . PHE A 1 713 ? -47.060 44.305 31.651 1.00 117.12 ? 713 PHE A CE1 1 ATOM 5512 C CE2 . PHE A 1 713 ? -46.521 44.185 29.328 1.00 133.10 ? 713 PHE A CE2 1 ATOM 5513 C CZ . PHE A 1 713 ? -46.198 43.925 30.643 1.00 124.70 ? 713 PHE A CZ 1 ATOM 5514 N N . ASP A 1 714 ? -50.772 48.456 27.628 1.00 113.54 ? 714 ASP A N 1 ATOM 5515 C CA . ASP A 1 714 ? -51.873 48.947 26.800 1.00 112.64 ? 714 ASP A CA 1 ATOM 5516 C C . ASP A 1 714 ? -52.018 48.091 25.544 1.00 108.85 ? 714 ASP A C 1 ATOM 5517 O O . ASP A 1 714 ? -51.032 47.795 24.868 1.00 104.46 ? 714 ASP A O 1 ATOM 5518 C CB . ASP A 1 714 ? -51.658 50.414 26.418 1.00 122.94 ? 714 ASP A CB 1 ATOM 5519 C CG . ASP A 1 714 ? -51.753 51.349 27.606 1.00 135.47 ? 714 ASP A CG 1 ATOM 5520 O OD1 . ASP A 1 714 ? -51.675 50.867 28.754 1.00 139.52 ? 714 ASP A OD1 1 ATOM 5521 O OD2 . ASP A 1 714 ? -51.902 52.571 27.393 1.00 139.50 ? 714 ASP A OD2 1 ATOM 5522 N N . LEU A 1 715 ? -53.249 47.695 25.235 1.00 117.27 ? 715 LEU A N 1 ATOM 5523 C CA . LEU A 1 715 ? -53.497 46.787 24.119 1.00 112.17 ? 715 LEU A CA 1 ATOM 5524 C C . LEU A 1 715 ? -54.543 47.314 23.144 1.00 102.65 ? 715 LEU A C 1 ATOM 5525 O O . LEU A 1 715 ? -55.576 47.844 23.553 1.00 109.08 ? 715 LEU A O 1 ATOM 5526 C CB . LEU A 1 715 ? -53.945 45.420 24.636 1.00 102.08 ? 715 LEU A CB 1 ATOM 5527 C CG . LEU A 1 715 ? -53.102 44.768 25.731 1.00 102.98 ? 715 LEU A CG 1 ATOM 5528 C CD1 . LEU A 1 715 ? -53.614 43.378 26.012 1.00 96.32 ? 715 LEU A CD1 1 ATOM 5529 C CD2 . LEU A 1 715 ? -51.648 44.716 25.328 1.00 122.16 ? 715 LEU A CD2 1 ATOM 5530 N N . GLN A 1 716 ? -54.267 47.162 21.854 1.00 94.83 ? 716 GLN A N 1 ATOM 5531 C CA . GLN A 1 716 ? -55.257 47.444 20.823 1.00 98.98 ? 716 GLN A CA 1 ATOM 5532 C C . GLN A 1 716 ? -54.928 46.691 19.542 1.00 98.11 ? 716 GLN A C 1 ATOM 5533 O O . GLN A 1 716 ? -53.807 46.218 19.357 1.00 100.44 ? 716 GLN A O 1 ATOM 5534 C CB . GLN A 1 716 ? -55.349 48.943 20.538 1.00 97.04 ? 716 GLN A CB 1 ATOM 5535 C CG . GLN A 1 716 ? -54.233 49.478 19.662 1.00 114.42 ? 716 GLN A CG 1 ATOM 5536 C CD . GLN A 1 716 ? -54.620 50.763 18.959 1.00 112.91 ? 716 GLN A CD 1 ATOM 5537 O OE1 . GLN A 1 716 ? -55.776 51.184 19.004 1.00 113.58 ? 716 GLN A OE1 1 ATOM 5538 N NE2 . GLN A 1 716 ? -53.654 51.392 18.300 1.00 103.35 ? 716 GLN A NE2 1 ATOM 5539 N N . ILE A 1 717 ? -55.915 46.578 18.662 1.00 100.42 ? 717 ILE A N 1 ATOM 5540 C CA . ILE A 1 717 ? -55.726 45.928 17.375 1.00 98.75 ? 717 ILE A CA 1 ATOM 5541 C C . ILE A 1 717 ? -55.673 46.974 16.265 1.00 93.79 ? 717 ILE A C 1 ATOM 5542 O O . ILE A 1 717 ? -56.384 47.975 16.320 1.00 104.55 ? 717 ILE A O 1 ATOM 5543 C CB . ILE A 1 717 ? -56.854 44.920 17.092 1.00 84.47 ? 717 ILE A CB 1 ATOM 5544 C CG1 . ILE A 1 717 ? -57.001 43.953 18.266 1.00 87.51 ? 717 ILE A CG1 1 ATOM 5545 C CG2 . ILE A 1 717 ? -56.588 44.158 15.806 1.00 82.08 ? 717 ILE A CG2 1 ATOM 5546 C CD1 . ILE A 1 717 ? -58.245 43.093 18.203 1.00 93.50 ? 717 ILE A CD1 1 ATOM 5547 N N . GLN A 1 718 ? -54.818 46.749 15.272 1.00 89.22 ? 718 GLN A N 1 ATOM 5548 C CA . GLN A 1 718 ? -54.727 47.645 14.124 1.00 98.94 ? 718 GLN A CA 1 ATOM 5549 C C . GLN A 1 718 ? -54.909 46.885 12.815 1.00 100.37 ? 718 GLN A C 1 ATOM 5550 O O . GLN A 1 718 ? -54.646 45.684 12.745 1.00 104.62 ? 718 GLN A O 1 ATOM 5551 C CB . GLN A 1 718 ? -53.385 48.376 14.115 1.00 99.03 ? 718 GLN A CB 1 ATOM 5552 C CG . GLN A 1 718 ? -53.151 49.270 15.315 1.00 98.99 ? 718 GLN A CG 1 ATOM 5553 C CD . GLN A 1 718 ? -51.789 49.928 15.276 1.00 112.31 ? 718 GLN A CD 1 ATOM 5554 O OE1 . GLN A 1 718 ? -51.337 50.508 16.263 1.00 121.89 ? 718 GLN A OE1 1 ATOM 5555 N NE2 . GLN A 1 718 ? -51.124 49.840 14.130 1.00 115.58 ? 718 GLN A NE2 1 ATOM 5556 N N . SER A 1 719 ? -55.352 47.589 11.778 1.00 86.82 ? 719 SER A N 1 ATOM 5557 C CA . SER A 1 719 ? -55.543 46.970 10.474 1.00 86.81 ? 719 SER A CA 1 ATOM 5558 C C . SER A 1 719 ? -55.344 47.969 9.339 1.00 81.26 ? 719 SER A C 1 ATOM 5559 O O . SER A 1 719 ? -55.116 49.151 9.577 1.00 100.55 ? 719 SER A O 1 ATOM 5560 C CB . SER A 1 719 ? -56.934 46.348 10.386 1.00 97.56 ? 719 SER A CB 1 ATOM 5561 O OG . SER A 1 719 ? -57.931 47.304 10.697 1.00 123.59 ? 719 SER A OG 1 ATOM 5562 N N . SER A 1 720 ? -55.439 47.481 8.106 1.00 82.48 ? 720 SER A N 1 ATOM 5563 C CA . SER A 1 720 ? -55.213 48.300 6.921 1.00 82.94 ? 720 SER A CA 1 ATOM 5564 C C . SER A 1 720 ? -56.507 48.844 6.325 1.00 83.64 ? 720 SER A C 1 ATOM 5565 O O . SER A 1 720 ? -56.488 49.509 5.289 1.00 83.18 ? 720 SER A O 1 ATOM 5566 C CB . SER A 1 720 ? -54.462 47.497 5.859 1.00 87.34 ? 720 SER A CB 1 ATOM 5567 O OG . SER A 1 720 ? -53.208 47.058 6.346 1.00 102.87 ? 720 SER A OG 1 ATOM 5568 N N . ASN A 1 721 ? -57.631 48.548 6.969 1.00 86.11 ? 721 ASN A N 1 ATOM 5569 C CA . ASN A 1 721 ? -58.922 49.031 6.492 1.00 104.72 ? 721 ASN A CA 1 ATOM 5570 C C . ASN A 1 721 ? -59.003 50.548 6.591 1.00 119.12 ? 721 ASN A C 1 ATOM 5571 O O . ASN A 1 721 ? -58.303 51.157 7.391 1.00 132.30 ? 721 ASN A O 1 ATOM 5572 C CB . ASN A 1 721 ? -60.060 48.384 7.279 1.00 94.12 ? 721 ASN A CB 1 ATOM 5573 C CG . ASN A 1 721 ? -60.029 46.872 7.205 1.00 109.04 ? 721 ASN A CG 1 ATOM 5574 O OD1 . ASN A 1 721 ? -58.967 46.272 7.043 1.00 115.91 ? 721 ASN A OD1 1 ATOM 5575 N ND2 . ASN A 1 721 ? -61.195 46.248 7.314 1.00 113.69 ? 721 ASN A ND2 1 ATOM 5576 N N . LEU A 1 722 ? -59.846 51.159 5.768 1.00 106.31 ? 722 LEU A N 1 ATOM 5577 C CA . LEU A 1 722 ? -59.960 52.611 5.764 1.00 102.05 ? 722 LEU A CA 1 ATOM 5578 C C . LEU A 1 722 ? -60.802 53.106 6.934 1.00 117.44 ? 722 LEU A C 1 ATOM 5579 O O . LEU A 1 722 ? -60.489 54.129 7.547 1.00 126.52 ? 722 LEU A O 1 ATOM 5580 C CB . LEU A 1 722 ? -60.553 53.097 4.442 1.00 101.41 ? 722 LEU A CB 1 ATOM 5581 C CG . LEU A 1 722 ? -59.759 52.724 3.187 1.00 100.76 ? 722 LEU A CG 1 ATOM 5582 C CD1 . LEU A 1 722 ? -60.355 53.386 1.955 1.00 91.85 ? 722 LEU A CD1 1 ATOM 5583 C CD2 . LEU A 1 722 ? -58.290 53.089 3.342 1.00 81.87 ? 722 LEU A CD2 1 ATOM 5584 N N . PHE A 1 723 ? -61.865 52.372 7.247 1.00 99.05 ? 723 PHE A N 1 ATOM 5585 C CA . PHE A 1 723 ? -62.780 52.776 8.307 1.00 114.18 ? 723 PHE A CA 1 ATOM 5586 C C . PHE A 1 723 ? -62.829 51.752 9.433 1.00 115.65 ? 723 PHE A C 1 ATOM 5587 O O . PHE A 1 723 ? -62.843 50.546 9.182 1.00 103.70 ? 723 PHE A O 1 ATOM 5588 C CB . PHE A 1 723 ? -64.179 52.998 7.737 1.00 119.61 ? 723 PHE A CB 1 ATOM 5589 C CG . PHE A 1 723 ? -64.209 53.939 6.571 1.00 123.86 ? 723 PHE A CG 1 ATOM 5590 C CD1 . PHE A 1 723 ? -64.161 55.309 6.769 1.00 126.91 ? 723 PHE A CD1 1 ATOM 5591 C CD2 . PHE A 1 723 ? -64.277 53.456 5.276 1.00 117.25 ? 723 PHE A CD2 1 ATOM 5592 C CE1 . PHE A 1 723 ? -64.184 56.180 5.696 1.00 131.50 ? 723 PHE A CE1 1 ATOM 5593 C CE2 . PHE A 1 723 ? -64.302 54.321 4.198 1.00 124.02 ? 723 PHE A CE2 1 ATOM 5594 C CZ . PHE A 1 723 ? -64.254 55.685 4.409 1.00 129.39 ? 723 PHE A CZ 1 ATOM 5595 N N . ASP A 1 724 ? -62.855 52.249 10.668 1.00 127.29 ? 724 ASP A N 1 ATOM 5596 C CA . ASP A 1 724 ? -62.866 51.409 11.864 1.00 116.85 ? 724 ASP A CA 1 ATOM 5597 C C . ASP A 1 724 ? -61.667 50.466 11.870 1.00 111.16 ? 724 ASP A C 1 ATOM 5598 O O . ASP A 1 724 ? -61.783 49.294 12.225 1.00 100.50 ? 724 ASP A O 1 ATOM 5599 C CB . ASP A 1 724 ? -64.173 50.619 11.955 1.00 107.35 ? 724 ASP A CB 1 ATOM 5600 C CG . ASP A 1 724 ? -65.396 51.504 11.821 1.00 131.31 ? 724 ASP A CG 1 ATOM 5601 O OD1 . ASP A 1 724 ? -65.357 52.650 12.316 1.00 140.90 ? 724 ASP A OD1 1 ATOM 5602 O OD2 . ASP A 1 724 ? -66.394 51.057 11.217 1.00 134.28 ? 724 ASP A OD2 1 ATOM 5603 N N . LYS A 1 725 ? -60.514 50.999 11.480 1.00 120.29 ? 725 LYS A N 1 ATOM 5604 C CA . LYS A 1 725 ? -59.312 50.198 11.275 1.00 103.69 ? 725 LYS A CA 1 ATOM 5605 C C . LYS A 1 725 ? -58.686 49.691 12.565 1.00 106.51 ? 725 LYS A C 1 ATOM 5606 O O . LYS A 1 725 ? -57.791 48.847 12.533 1.00 110.99 ? 725 LYS A O 1 ATOM 5607 C CB . LYS A 1 725 ? -58.269 51.008 10.511 1.00 92.45 ? 725 LYS A CB 1 ATOM 5608 C CG . LYS A 1 725 ? -57.734 52.203 11.281 1.00 97.80 ? 725 LYS A CG 1 ATOM 5609 C CD . LYS A 1 725 ? -56.589 52.854 10.532 1.00 110.00 ? 725 LYS A CD 1 ATOM 5610 C CE . LYS A 1 725 ? -57.042 53.344 9.170 1.00 98.34 ? 725 LYS A CE 1 ATOM 5611 N NZ . LYS A 1 725 ? -55.904 53.462 8.219 1.00 120.42 ? 725 LYS A NZ 1 ATOM 5612 N N . VAL A 1 726 ? -59.139 50.213 13.698 1.00 90.93 ? 726 VAL A N 1 ATOM 5613 C CA . VAL A 1 726 ? -58.530 49.853 14.970 1.00 79.36 ? 726 VAL A CA 1 ATOM 5614 C C . VAL A 1 726 ? -59.541 49.412 16.014 1.00 91.61 ? 726 VAL A C 1 ATOM 5615 O O . VAL A 1 726 ? -60.736 49.305 15.742 1.00 101.78 ? 726 VAL A O 1 ATOM 5616 C CB . VAL A 1 726 ? -57.720 51.021 15.554 1.00 77.59 ? 726 VAL A CB 1 ATOM 5617 C CG1 . VAL A 1 726 ? -56.519 51.326 14.675 1.00 82.33 ? 726 VAL A CG1 1 ATOM 5618 C CG2 . VAL A 1 726 ? -58.607 52.243 15.717 1.00 86.37 ? 726 VAL A CG2 1 ATOM 5619 N N . SER A 1 727 ? -59.035 49.155 17.214 1.00 105.22 ? 727 SER A N 1 ATOM 5620 C CA . SER A 1 727 ? -59.859 48.775 18.349 1.00 96.46 ? 727 SER A CA 1 ATOM 5621 C C . SER A 1 727 ? -59.693 49.802 19.459 1.00 107.54 ? 727 SER A C 1 ATOM 5622 O O . SER A 1 727 ? -58.690 50.517 19.497 1.00 91.98 ? 727 SER A O 1 ATOM 5623 C CB . SER A 1 727 ? -59.474 47.385 18.856 1.00 92.94 ? 727 SER A CB 1 ATOM 5624 O OG . SER A 1 727 ? -58.240 47.422 19.550 1.00 95.33 ? 727 SER A OG 1 ATOM 5625 N N . PRO A 1 728 ? -60.679 49.888 20.364 1.00 106.40 ? 728 PRO A N 1 ATOM 5626 C CA . PRO A 1 728 ? -60.476 50.729 21.545 1.00 90.43 ? 728 PRO A CA 1 ATOM 5627 C C . PRO A 1 728 ? -59.298 50.214 22.359 1.00 98.69 ? 728 PRO A C 1 ATOM 5628 O O . PRO A 1 728 ? -59.220 49.013 22.622 1.00 122.80 ? 728 PRO A O 1 ATOM 5629 C CB . PRO A 1 728 ? -61.793 50.585 22.314 1.00 106.08 ? 728 PRO A CB 1 ATOM 5630 C CG . PRO A 1 728 ? -62.384 49.297 21.823 1.00 102.83 ? 728 PRO A CG 1 ATOM 5631 C CD . PRO A 1 728 ? -61.991 49.219 20.381 1.00 102.52 ? 728 PRO A CD 1 ATOM 5632 N N . VAL A 1 729 ? -58.387 51.103 22.738 1.00 92.33 ? 729 VAL A N 1 ATOM 5633 C CA . VAL A 1 729 ? -57.211 50.692 23.491 1.00 94.83 ? 729 VAL A CA 1 ATOM 5634 C C . VAL A 1 729 ? -57.595 50.273 24.904 1.00 94.89 ? 729 VAL A C 1 ATOM 5635 O O . VAL A 1 729 ? -58.212 51.036 25.644 1.00 105.34 ? 729 VAL A O 1 ATOM 5636 C CB . VAL A 1 729 ? -56.161 51.812 23.566 1.00 87.65 ? 729 VAL A CB 1 ATOM 5637 C CG1 . VAL A 1 729 ? -54.958 51.353 24.378 1.00 88.18 ? 729 VAL A CG1 1 ATOM 5638 C CG2 . VAL A 1 729 ? -55.739 52.233 22.170 1.00 91.43 ? 729 VAL A CG2 1 ATOM 5639 N N . VAL A 1 730 ? -57.225 49.052 25.270 1.00 96.58 ? 730 VAL A N 1 ATOM 5640 C CA . VAL A 1 730 ? -57.543 48.526 26.588 1.00 101.31 ? 730 VAL A CA 1 ATOM 5641 C C . VAL A 1 730 ? -56.275 48.432 27.426 1.00 106.51 ? 730 VAL A C 1 ATOM 5642 O O . VAL A 1 730 ? -55.219 48.047 26.924 1.00 105.04 ? 730 VAL A O 1 ATOM 5643 C CB . VAL A 1 730 ? -58.217 47.145 26.496 1.00 100.68 ? 730 VAL A CB 1 ATOM 5644 C CG1 . VAL A 1 730 ? -58.665 46.675 27.871 1.00 103.46 ? 730 VAL A CG1 1 ATOM 5645 C CG2 . VAL A 1 730 ? -59.400 47.203 25.541 1.00 104.04 ? 730 VAL A CG2 1 ATOM 5646 N N . SER A 1 731 ? -56.379 48.798 28.699 1.00 116.32 ? 731 SER A N 1 ATOM 5647 C CA . SER A 1 731 ? -55.230 48.771 29.593 1.00 114.68 ? 731 SER A CA 1 ATOM 5648 C C . SER A 1 731 ? -55.437 47.816 30.763 1.00 110.54 ? 731 SER A C 1 ATOM 5649 O O . SER A 1 731 ? -56.509 47.771 31.367 1.00 116.20 ? 731 SER A O 1 ATOM 5650 C CB . SER A 1 731 ? -54.928 50.176 30.115 1.00 110.77 ? 731 SER A CB 1 ATOM 5651 O OG . SER A 1 731 ? -54.600 51.052 29.051 1.00 117.60 ? 731 SER A OG 1 ATOM 5652 N N . HIS A 1 732 ? -54.399 47.049 31.071 1.00 104.24 ? 732 HIS A N 1 ATOM 5653 C CA . HIS A 1 732 ? -54.416 46.153 32.217 1.00 106.39 ? 732 HIS A CA 1 ATOM 5654 C C . HIS A 1 732 ? -53.176 46.381 33.068 1.00 109.91 ? 732 HIS A C 1 ATOM 5655 O O . HIS A 1 732 ? -52.059 46.434 32.553 1.00 105.74 ? 732 HIS A O 1 ATOM 5656 C CB . HIS A 1 732 ? -54.488 44.694 31.768 1.00 108.35 ? 732 HIS A CB 1 ATOM 5657 C CG . HIS A 1 732 ? -54.340 43.711 32.887 1.00 119.39 ? 732 HIS A CG 1 ATOM 5658 N ND1 . HIS A 1 732 ? -53.639 42.531 32.753 1.00 120.30 ? 732 HIS A ND1 1 ATOM 5659 C CD2 . HIS A 1 732 ? -54.802 43.731 34.160 1.00 133.53 ? 732 HIS A CD2 1 ATOM 5660 C CE1 . HIS A 1 732 ? -53.675 41.868 33.895 1.00 124.96 ? 732 HIS A CE1 1 ATOM 5661 N NE2 . HIS A 1 732 ? -54.374 42.574 34.765 1.00 134.79 ? 732 HIS A NE2 1 ATOM 5662 N N . LYS A 1 733 ? -53.376 46.524 34.372 1.00 111.68 ? 733 LYS A N 1 ATOM 5663 C CA . LYS A 1 733 ? -52.259 46.721 35.282 1.00 104.10 ? 733 LYS A CA 1 ATOM 5664 C C . LYS A 1 733 ? -52.227 45.644 36.355 1.00 108.80 ? 733 LYS A C 1 ATOM 5665 O O . LYS A 1 733 ? -53.265 45.213 36.858 1.00 116.18 ? 733 LYS A O 1 ATOM 5666 C CB . LYS A 1 733 ? -52.327 48.107 35.931 1.00 102.39 ? 733 LYS A CB 1 ATOM 5667 C CG . LYS A 1 733 ? -53.529 48.319 36.836 1.00 106.63 ? 733 LYS A CG 1 ATOM 5668 C CD . LYS A 1 733 ? -53.460 49.659 37.549 1.00 118.36 ? 733 LYS A CD 1 ATOM 5669 C CE . LYS A 1 733 ? -54.637 49.839 38.494 1.00 130.31 ? 733 LYS A CE 1 ATOM 5670 N NZ . LYS A 1 733 ? -54.623 51.168 39.162 1.00 130.76 ? 733 LYS A NZ 1 ATOM 5671 N N . VAL A 1 734 ? -51.024 45.195 36.687 1.00 115.18 ? 734 VAL A N 1 ATOM 5672 C CA . VAL A 1 734 ? -50.832 44.339 37.844 1.00 125.42 ? 734 VAL A CA 1 ATOM 5673 C C . VAL A 1 734 ? -49.981 45.104 38.848 1.00 121.02 ? 734 VAL A C 1 ATOM 5674 O O . VAL A 1 734 ? -49.006 45.758 38.477 1.00 120.97 ? 734 VAL A O 1 ATOM 5675 C CB . VAL A 1 734 ? -50.176 42.994 37.475 1.00 131.94 ? 734 VAL A CB 1 ATOM 5676 C CG1 . VAL A 1 734 ? -51.203 42.059 36.850 1.00 141.72 ? 734 VAL A CG1 1 ATOM 5677 C CG2 . VAL A 1 734 ? -49.004 43.207 36.535 1.00 122.79 ? 734 VAL A CG2 1 ATOM 5678 N N . ASP A 1 735 ? -50.370 45.039 40.115 1.00 121.97 ? 735 ASP A N 1 ATOM 5679 C CA . ASP A 1 735 ? -49.748 45.863 41.142 1.00 116.84 ? 735 ASP A CA 1 ATOM 5680 C C . ASP A 1 735 ? -48.453 45.254 41.665 1.00 110.26 ? 735 ASP A C 1 ATOM 5681 O O . ASP A 1 735 ? -48.338 44.037 41.811 1.00 111.94 ? 735 ASP A O 1 ATOM 5682 C CB . ASP A 1 735 ? -50.723 46.084 42.301 1.00 120.50 ? 735 ASP A CB 1 ATOM 5683 C CG . ASP A 1 735 ? -52.070 46.600 41.837 1.00 140.58 ? 735 ASP A CG 1 ATOM 5684 O OD1 . ASP A 1 735 ? -52.102 47.459 40.931 1.00 161.76 ? 735 ASP A OD1 1 ATOM 5685 O OD2 . ASP A 1 735 ? -53.100 46.141 42.375 1.00 148.26 ? 735 ASP A OD2 1 ATOM 5686 N N . LEU A 1 736 ? -47.475 46.112 41.934 1.00 102.71 ? 736 LEU A N 1 ATOM 5687 C CA . LEU A 1 736 ? -46.262 45.689 42.615 1.00 96.49 ? 736 LEU A CA 1 ATOM 5688 C C . LEU A 1 736 ? -46.588 45.356 44.064 1.00 104.42 ? 736 LEU A C 1 ATOM 5689 O O . LEU A 1 736 ? -47.363 46.058 44.713 1.00 115.46 ? 736 LEU A O 1 ATOM 5690 C CB . LEU A 1 736 ? -45.182 46.773 42.552 1.00 100.17 ? 736 LEU A CB 1 ATOM 5691 C CG . LEU A 1 736 ? -44.369 46.929 41.264 1.00 104.51 ? 736 LEU A CG 1 ATOM 5692 C CD1 . LEU A 1 736 ? -43.898 45.572 40.754 1.00 112.68 ? 736 LEU A CD1 1 ATOM 5693 C CD2 . LEU A 1 736 ? -45.149 47.675 40.197 1.00 107.60 ? 736 LEU A CD2 1 ATOM 5694 N N . ALA A 1 737 ? -46.000 44.281 44.569 1.00 105.56 ? 737 ALA A N 1 ATOM 5695 C CA . ALA A 1 737 ? -46.199 43.897 45.957 1.00 104.91 ? 737 ALA A CA 1 ATOM 5696 C C . ALA A 1 737 ? -44.857 43.724 46.654 1.00 107.91 ? 737 ALA A C 1 ATOM 5697 O O . ALA A 1 737 ? -43.835 43.486 46.007 1.00 104.59 ? 737 ALA A O 1 ATOM 5698 C CB . ALA A 1 737 ? -47.018 42.622 46.046 1.00 110.46 ? 737 ALA A CB 1 ATOM 5699 N N . VAL A 1 738 ? -44.867 43.849 47.976 1.00 109.16 ? 738 VAL A N 1 ATOM 5700 C CA . VAL A 1 738 ? -43.653 43.704 48.762 1.00 102.66 ? 738 VAL A CA 1 ATOM 5701 C C . VAL A 1 738 ? -43.665 42.402 49.550 1.00 104.27 ? 738 VAL A C 1 ATOM 5702 O O . VAL A 1 738 ? -44.527 42.188 50.403 1.00 111.28 ? 738 VAL A O 1 ATOM 5703 C CB . VAL A 1 738 ? -43.466 44.882 49.736 1.00 110.61 ? 738 VAL A CB 1 ATOM 5704 C CG1 . VAL A 1 738 ? -42.285 44.628 50.658 1.00 105.18 ? 738 VAL A CG1 1 ATOM 5705 C CG2 . VAL A 1 738 ? -43.280 46.180 48.969 1.00 122.53 ? 738 VAL A CG2 1 ATOM 5706 N N . LEU A 1 739 ? -42.712 41.528 49.245 1.00 100.56 ? 739 LEU A N 1 ATOM 5707 C CA . LEU A 1 739 ? -42.531 40.297 50.002 1.00 108.10 ? 739 LEU A CA 1 ATOM 5708 C C . LEU A 1 739 ? -41.060 40.105 50.352 1.00 103.65 ? 739 LEU A C 1 ATOM 5709 O O . LEU A 1 739 ? -40.214 39.954 49.471 1.00 100.82 ? 739 LEU A O 1 ATOM 5710 C CB . LEU A 1 739 ? -43.046 39.092 49.216 1.00 110.22 ? 739 LEU A CB 1 ATOM 5711 C CG . LEU A 1 739 ? -42.970 37.764 49.970 1.00 108.91 ? 739 LEU A CG 1 ATOM 5712 C CD1 . LEU A 1 739 ? -43.947 37.764 51.136 1.00 111.80 ? 739 LEU A CD1 1 ATOM 5713 C CD2 . LEU A 1 739 ? -43.231 36.593 49.037 1.00 117.17 ? 739 LEU A CD2 1 ATOM 5714 N N . ALA A 1 740 ? -40.761 40.112 51.644 1.00 102.81 ? 740 ALA A N 1 ATOM 5715 C CA . ALA A 1 740 ? -39.391 39.929 52.101 1.00 105.27 ? 740 ALA A CA 1 ATOM 5716 C C . ALA A 1 740 ? -39.317 38.815 53.134 1.00 110.01 ? 740 ALA A C 1 ATOM 5717 O O . ALA A 1 740 ? -39.887 38.924 54.220 1.00 112.75 ? 740 ALA A O 1 ATOM 5718 C CB . ALA A 1 740 ? -38.844 41.224 52.676 1.00 95.71 ? 740 ALA A CB 1 ATOM 5719 N N . ALA A 1 741 ? -38.608 37.745 52.798 1.00 104.16 ? 741 ALA A N 1 ATOM 5720 C CA . ALA A 1 741 ? -38.472 36.633 53.723 1.00 95.30 ? 741 ALA A CA 1 ATOM 5721 C C . ALA A 1 741 ? -37.227 36.847 54.561 1.00 92.51 ? 741 ALA A C 1 ATOM 5722 O O . ALA A 1 741 ? -36.103 36.749 54.068 1.00 95.81 ? 741 ALA A O 1 ATOM 5723 C CB . ALA A 1 741 ? -38.402 35.313 52.976 1.00 93.30 ? 741 ALA A CB 1 ATOM 5724 N N . VAL A 1 742 ? -37.440 37.136 55.838 1.00 90.96 ? 742 VAL A N 1 ATOM 5725 C CA . VAL A 1 742 ? -36.348 37.475 56.733 1.00 88.71 ? 742 VAL A CA 1 ATOM 5726 C C . VAL A 1 742 ? -36.251 36.438 57.832 1.00 91.69 ? 742 VAL A C 1 ATOM 5727 O O . VAL A 1 742 ? -37.215 36.201 58.560 1.00 105.58 ? 742 VAL A O 1 ATOM 5728 C CB . VAL A 1 742 ? -36.535 38.871 57.358 1.00 94.46 ? 742 VAL A CB 1 ATOM 5729 C CG1 . VAL A 1 742 ? -35.252 39.323 58.028 1.00 84.97 ? 742 VAL A CG1 1 ATOM 5730 C CG2 . VAL A 1 742 ? -36.962 39.874 56.300 1.00 91.73 ? 742 VAL A CG2 1 ATOM 5731 N N . GLU A 1 743 ? -35.088 35.812 57.945 1.00 87.47 ? 743 GLU A N 1 ATOM 5732 C CA . GLU A 1 743 ? -34.876 34.825 58.987 1.00 96.53 ? 743 GLU A CA 1 ATOM 5733 C C . GLU A 1 743 ? -33.794 35.295 59.943 1.00 90.50 ? 743 GLU A C 1 ATOM 5734 O O . GLU A 1 743 ? -32.876 36.018 59.555 1.00 93.21 ? 743 GLU A O 1 ATOM 5735 C CB . GLU A 1 743 ? -34.499 33.466 58.389 1.00 107.69 ? 743 GLU A CB 1 ATOM 5736 C CG . GLU A 1 743 ? -33.142 33.432 57.702 1.00 111.04 ? 743 GLU A CG 1 ATOM 5737 C CD . GLU A 1 743 ? -32.633 32.018 57.490 1.00 127.65 ? 743 GLU A CD 1 ATOM 5738 O OE1 . GLU A 1 743 ? -31.556 31.856 56.878 1.00 140.97 ? 743 GLU A OE1 1 ATOM 5739 O OE2 . GLU A 1 743 ? -33.309 31.069 57.941 1.00 123.05 ? 743 GLU A OE2 1 ATOM 5740 N N . ILE A 1 744 ? -33.918 34.895 61.201 1.00 83.95 ? 744 ILE A N 1 ATOM 5741 C CA . ILE A 1 744 ? -32.855 35.123 62.162 1.00 83.84 ? 744 ILE A CA 1 ATOM 5742 C C . ILE A 1 744 ? -32.335 33.774 62.654 1.00 87.67 ? 744 ILE A C 1 ATOM 5743 O O . ILE A 1 744 ? -33.101 32.908 63.076 1.00 90.96 ? 744 ILE A O 1 ATOM 5744 C CB . ILE A 1 744 ? -33.326 36.004 63.342 1.00 83.94 ? 744 ILE A CB 1 ATOM 5745 C CG1 . ILE A 1 744 ? -32.180 36.232 64.331 1.00 82.66 ? 744 ILE A CG1 1 ATOM 5746 C CG2 . ILE A 1 744 ? -34.554 35.407 64.029 1.00 87.90 ? 744 ILE A CG2 1 ATOM 5747 C CD1 . ILE A 1 744 ? -32.505 37.226 65.429 1.00 93.67 ? 744 ILE A CD1 1 ATOM 5748 N N . ARG A 1 745 ? -31.026 33.586 62.557 1.00 87.93 ? 745 ARG A N 1 ATOM 5749 C CA . ARG A 1 745 ? -30.404 32.335 62.960 1.00 74.14 ? 745 ARG A CA 1 ATOM 5750 C C . ARG A 1 745 ? -29.338 32.596 64.007 1.00 72.88 ? 745 ARG A C 1 ATOM 5751 O O . ARG A 1 745 ? -28.827 33.707 64.121 1.00 82.65 ? 745 ARG A O 1 ATOM 5752 C CB . ARG A 1 745 ? -29.802 31.619 61.752 1.00 71.46 ? 745 ARG A CB 1 ATOM 5753 C CG . ARG A 1 745 ? -30.823 31.236 60.691 1.00 87.44 ? 745 ARG A CG 1 ATOM 5754 C CD . ARG A 1 745 ? -30.174 30.478 59.547 1.00 89.84 ? 745 ARG A CD 1 ATOM 5755 N NE . ARG A 1 745 ? -29.367 29.360 60.027 1.00 111.96 ? 745 ARG A NE 1 ATOM 5756 C CZ . ARG A 1 745 ? -29.841 28.142 60.267 1.00 118.61 ? 745 ARG A CZ 1 ATOM 5757 N NH1 . ARG A 1 745 ? -31.126 27.877 60.072 1.00 119.88 ? 745 ARG A NH1 1 ATOM 5758 N NH2 . ARG A 1 745 ? -29.028 27.189 60.703 1.00 109.87 ? 745 ARG A NH2 1 ATOM 5759 N N . GLY A 1 746 ? -29.000 31.565 64.770 1.00 75.02 ? 746 GLY A N 1 ATOM 5760 C CA . GLY A 1 746 ? -28.010 31.704 65.818 1.00 70.58 ? 746 GLY A CA 1 ATOM 5761 C C . GLY A 1 746 ? -27.278 30.410 66.103 1.00 70.44 ? 746 GLY A C 1 ATOM 5762 O O . GLY A 1 746 ? -27.781 29.324 65.823 1.00 78.20 ? 746 GLY A O 1 ATOM 5763 N N . VAL A 1 747 ? -26.078 30.530 66.656 1.00 65.67 ? 747 VAL A N 1 ATOM 5764 C CA . VAL A 1 747 ? -25.258 29.364 66.931 1.00 71.78 ? 747 VAL A CA 1 ATOM 5765 C C . VAL A 1 747 ? -24.345 29.626 68.124 1.00 77.21 ? 747 VAL A C 1 ATOM 5766 O O . VAL A 1 747 ? -23.865 30.743 68.312 1.00 62.24 ? 747 VAL A O 1 ATOM 5767 C CB . VAL A 1 747 ? -24.425 28.977 65.693 1.00 70.26 ? 747 VAL A CB 1 ATOM 5768 C CG1 . VAL A 1 747 ? -23.576 30.151 65.233 1.00 59.86 ? 747 VAL A CG1 1 ATOM 5769 C CG2 . VAL A 1 747 ? -23.566 27.752 65.973 1.00 74.95 ? 747 VAL A CG2 1 ATOM 5770 N N . SER A 1 748 ? -24.122 28.598 68.936 1.00 98.54 ? 748 SER A N 1 ATOM 5771 C CA . SER A 1 748 ? -23.220 28.708 70.071 1.00 88.28 ? 748 SER A CA 1 ATOM 5772 C C . SER A 1 748 ? -21.906 27.997 69.771 1.00 86.00 ? 748 SER A C 1 ATOM 5773 O O . SER A 1 748 ? -21.900 26.852 69.325 1.00 90.55 ? 748 SER A O 1 ATOM 5774 C CB . SER A 1 748 ? -23.864 28.130 71.328 1.00 80.83 ? 748 SER A CB 1 ATOM 5775 O OG . SER A 1 748 ? -23.032 28.335 72.454 1.00 104.29 ? 748 SER A OG 1 ATOM 5776 N N . SER A 1 749 ? -20.796 28.684 70.015 1.00 78.82 ? 749 SER A N 1 ATOM 5777 C CA . SER A 1 749 ? -19.477 28.143 69.713 1.00 77.96 ? 749 SER A CA 1 ATOM 5778 C C . SER A 1 749 ? -18.554 28.214 70.927 1.00 84.01 ? 749 SER A C 1 ATOM 5779 O O . SER A 1 749 ? -17.913 29.237 71.161 1.00 69.35 ? 749 SER A O 1 ATOM 5780 C CB . SER A 1 749 ? -18.854 28.884 68.531 1.00 83.85 ? 749 SER A CB 1 ATOM 5781 O OG . SER A 1 749 ? -17.622 28.291 68.160 1.00 111.85 ? 749 SER A OG 1 ATOM 5782 N N . PRO A 1 750 ? -18.488 27.124 71.708 1.00 63.68 ? 750 PRO A N 1 ATOM 5783 C CA . PRO A 1 750 ? -19.184 25.866 71.429 1.00 75.78 ? 750 PRO A CA 1 ATOM 5784 C C . PRO A 1 750 ? -20.578 25.827 72.036 1.00 76.98 ? 750 PRO A C 1 ATOM 5785 O O . PRO A 1 750 ? -20.974 26.771 72.717 1.00 109.55 ? 750 PRO A O 1 ATOM 5786 C CB . PRO A 1 750 ? -18.281 24.814 72.088 1.00 93.16 ? 750 PRO A CB 1 ATOM 5787 C CG . PRO A 1 750 ? -17.264 25.599 72.931 1.00 79.58 ? 750 PRO A CG 1 ATOM 5788 C CD . PRO A 1 750 ? -17.693 27.027 72.940 1.00 58.98 ? 750 PRO A CD 1 ATOM 5789 N N . ASP A 1 751 ? -21.309 24.745 71.793 1.00 61.10 ? 751 ASP A N 1 ATOM 5790 C CA . ASP A 1 751 ? -22.615 24.566 72.410 1.00 81.09 ? 751 ASP A CA 1 ATOM 5791 C C . ASP A 1 751 ? -22.465 23.785 73.710 1.00 98.37 ? 751 ASP A C 1 ATOM 5792 O O . ASP A 1 751 ? -23.430 23.582 74.445 1.00 120.11 ? 751 ASP A O 1 ATOM 5793 C CB . ASP A 1 751 ? -23.582 23.855 71.457 1.00 86.39 ? 751 ASP A CB 1 ATOM 5794 C CG . ASP A 1 751 ? -22.996 22.588 70.857 1.00 104.21 ? 751 ASP A CG 1 ATOM 5795 O OD1 . ASP A 1 751 ? -21.924 22.135 71.313 1.00 122.98 ? 751 ASP A OD1 1 ATOM 5796 O OD2 . ASP A 1 751 ? -23.620 22.037 69.925 1.00 100.02 ? 751 ASP A OD2 1 ATOM 5797 N N . HIS A 1 752 ? -21.238 23.357 73.986 1.00 103.50 ? 752 HIS A N 1 ATOM 5798 C CA . HIS A 1 752 ? -20.944 22.558 75.167 1.00 89.92 ? 752 HIS A CA 1 ATOM 5799 C C . HIS A 1 752 ? -19.745 23.087 75.932 1.00 105.22 ? 752 HIS A C 1 ATOM 5800 O O . HIS A 1 752 ? -18.714 23.410 75.344 1.00 119.41 ? 752 HIS A O 1 ATOM 5801 C CB . HIS A 1 752 ? -20.683 21.100 74.777 1.00 75.88 ? 752 HIS A CB 1 ATOM 5802 C CG . HIS A 1 752 ? -21.905 20.238 74.800 1.00 117.72 ? 752 HIS A CG 1 ATOM 5803 N ND1 . HIS A 1 752 ? -22.388 19.664 75.956 1.00 131.03 ? 752 HIS A ND1 1 ATOM 5804 C CD2 . HIS A 1 752 ? -22.737 19.843 73.807 1.00 129.94 ? 752 HIS A CD2 1 ATOM 5805 C CE1 . HIS A 1 752 ? -23.468 18.957 75.676 1.00 123.74 ? 752 HIS A CE1 1 ATOM 5806 N NE2 . HIS A 1 752 ? -23.701 19.049 74.378 1.00 133.60 ? 752 HIS A NE2 1 ATOM 5807 N N . VAL A 1 753 ? -19.884 23.181 77.248 1.00 68.14 ? 753 VAL A N 1 ATOM 5808 C CA . VAL A 1 753 ? -18.725 23.360 78.108 1.00 72.65 ? 753 VAL A CA 1 ATOM 5809 C C . VAL A 1 753 ? -18.763 22.315 79.217 1.00 111.22 ? 753 VAL A C 1 ATOM 5810 O O . VAL A 1 753 ? -19.651 22.335 80.067 1.00 109.07 ? 753 VAL A O 1 ATOM 5811 C CB . VAL A 1 753 ? -18.662 24.769 78.716 1.00 68.68 ? 753 VAL A CB 1 ATOM 5812 C CG1 . VAL A 1 753 ? -17.495 24.868 79.683 1.00 74.33 ? 753 VAL A CG1 1 ATOM 5813 C CG2 . VAL A 1 753 ? -18.535 25.815 77.621 1.00 87.70 ? 753 VAL A CG2 1 ATOM 5814 N N . PHE A 1 754 ? -17.799 21.400 79.202 1.00 133.85 ? 754 PHE A N 1 ATOM 5815 C CA . PHE A 1 754 ? -17.770 20.308 80.169 1.00 111.37 ? 754 PHE A CA 1 ATOM 5816 C C . PHE A 1 754 ? -17.043 20.715 81.444 1.00 109.24 ? 754 PHE A C 1 ATOM 5817 O O . PHE A 1 754 ? -16.023 21.402 81.396 1.00 98.35 ? 754 PHE A O 1 ATOM 5818 C CB . PHE A 1 754 ? -17.109 19.069 79.561 1.00 82.46 ? 754 PHE A CB 1 ATOM 5819 C CG . PHE A 1 754 ? -17.883 18.465 78.424 1.00 64.63 ? 754 PHE A CG 1 ATOM 5820 C CD1 . PHE A 1 754 ? -17.710 18.925 77.128 1.00 108.74 ? 754 PHE A CD1 1 ATOM 5821 C CD2 . PHE A 1 754 ? -18.781 17.438 78.650 1.00 66.72 ? 754 PHE A CD2 1 ATOM 5822 C CE1 . PHE A 1 754 ? -18.422 18.371 76.080 1.00 111.46 ? 754 PHE A CE1 1 ATOM 5823 C CE2 . PHE A 1 754 ? -19.494 16.879 77.607 1.00 67.42 ? 754 PHE A CE2 1 ATOM 5824 C CZ . PHE A 1 754 ? -19.314 17.346 76.320 1.00 80.28 ? 754 PHE A CZ 1 ATOM 5825 N N . LEU A 1 755 ? -17.562 20.271 82.583 1.00 96.52 ? 755 LEU A N 1 ATOM 5826 C CA . LEU A 1 755 ? -17.012 20.665 83.874 1.00 102.89 ? 755 LEU A CA 1 ATOM 5827 C C . LEU A 1 755 ? -16.408 19.473 84.615 1.00 109.45 ? 755 LEU A C 1 ATOM 5828 O O . LEU A 1 755 ? -16.893 18.347 84.486 1.00 101.21 ? 755 LEU A O 1 ATOM 5829 C CB . LEU A 1 755 ? -18.094 21.328 84.732 1.00 103.67 ? 755 LEU A CB 1 ATOM 5830 C CG . LEU A 1 755 ? -18.594 22.695 84.259 1.00 107.79 ? 755 LEU A CG 1 ATOM 5831 C CD1 . LEU A 1 755 ? -19.454 23.343 85.331 1.00 102.66 ? 755 LEU A CD1 1 ATOM 5832 C CD2 . LEU A 1 755 ? -17.432 23.599 83.877 1.00 73.09 ? 755 LEU A CD2 1 ATOM 5833 N N . PRO A 1 756 ? -15.346 19.719 85.401 1.00 80.22 ? 756 PRO A N 1 ATOM 5834 C CA . PRO A 1 756 ? -14.747 21.041 85.622 1.00 77.97 ? 756 PRO A CA 1 ATOM 5835 C C . PRO A 1 756 ? -13.798 21.474 84.509 1.00 79.69 ? 756 PRO A C 1 ATOM 5836 O O . PRO A 1 756 ? -13.544 20.713 83.575 1.00 103.94 ? 756 PRO A O 1 ATOM 5837 C CB . PRO A 1 756 ? -13.985 20.852 86.931 1.00 101.50 ? 756 PRO A CB 1 ATOM 5838 C CG . PRO A 1 756 ? -13.563 19.428 86.889 1.00 117.47 ? 756 PRO A CG 1 ATOM 5839 C CD . PRO A 1 756 ? -14.677 18.678 86.200 1.00 68.53 ? 756 PRO A CD 1 ATOM 5840 N N . ILE A 1 757 ? -13.275 22.691 84.624 1.00 87.52 ? 757 ILE A N 1 ATOM 5841 C CA . ILE A 1 757 ? -12.340 23.226 83.643 1.00 112.01 ? 757 ILE A CA 1 ATOM 5842 C C . ILE A 1 757 ? -10.928 22.750 83.952 1.00 119.11 ? 757 ILE A C 1 ATOM 5843 O O . ILE A 1 757 ? -10.452 22.900 85.077 1.00 127.55 ? 757 ILE A O 1 ATOM 5844 C CB . ILE A 1 757 ? -12.362 24.770 83.615 1.00 119.37 ? 757 ILE A CB 1 ATOM 5845 C CG1 . ILE A 1 757 ? -13.777 25.287 83.339 1.00 103.86 ? 757 ILE A CG1 1 ATOM 5846 C CG2 . ILE A 1 757 ? -11.380 25.302 82.580 1.00 96.70 ? 757 ILE A CG2 1 ATOM 5847 C CD1 . ILE A 1 757 ? -14.306 24.927 81.968 1.00 97.00 ? 757 ILE A CD1 1 ATOM 5848 N N . PRO A 1 758 ? -10.253 22.165 82.952 1.00 127.87 ? 758 PRO A N 1 ATOM 5849 C CA . PRO A 1 758 ? -8.880 21.685 83.144 1.00 128.09 ? 758 PRO A CA 1 ATOM 5850 C C . PRO A 1 758 ? -7.920 22.808 83.529 1.00 96.43 ? 758 PRO A C 1 ATOM 5851 O O . PRO A 1 758 ? -7.910 23.855 82.881 1.00 89.71 ? 758 PRO A O 1 ATOM 5852 C CB . PRO A 1 758 ? -8.518 21.096 81.773 1.00 130.31 ? 758 PRO A CB 1 ATOM 5853 C CG . PRO A 1 758 ? -9.487 21.714 80.812 1.00 132.57 ? 758 PRO A CG 1 ATOM 5854 C CD . PRO A 1 758 ? -10.748 21.901 81.591 1.00 118.95 ? 758 PRO A CD 1 ATOM 5855 N N . ASN A 1 759 ? -7.135 22.579 84.580 1.00 116.00 ? 759 ASN A N 1 ATOM 5856 C CA . ASN A 1 759 ? -6.141 23.540 85.053 1.00 128.42 ? 759 ASN A CA 1 ATOM 5857 C C . ASN A 1 759 ? -6.727 24.917 85.359 1.00 128.46 ? 759 ASN A C 1 ATOM 5858 O O . ASN A 1 759 ? -6.263 25.928 84.832 1.00 110.48 ? 759 ASN A O 1 ATOM 5859 C CB . ASN A 1 759 ? -5.007 23.675 84.032 1.00 121.14 ? 759 ASN A CB 1 ATOM 5860 C CG . ASN A 1 759 ? -4.175 22.411 83.916 1.00 145.26 ? 759 ASN A CG 1 ATOM 5861 O OD1 . ASN A 1 759 ? -3.968 21.696 84.897 1.00 146.28 ? 759 ASN A OD1 1 ATOM 5862 N ND2 . ASN A 1 759 ? -3.692 22.129 82.711 1.00 139.69 ? 759 ASN A ND2 1 ATOM 5863 N N . TRP A 1 760 ? -7.750 24.951 86.206 1.00 148.55 ? 760 TRP A N 1 ATOM 5864 C CA . TRP A 1 760 ? -8.371 26.211 86.600 1.00 144.54 ? 760 TRP A CA 1 ATOM 5865 C C . TRP A 1 760 ? -8.353 26.406 88.112 1.00 125.59 ? 760 TRP A C 1 ATOM 5866 O O . TRP A 1 760 ? -8.735 25.513 88.871 1.00 118.00 ? 760 TRP A O 1 ATOM 5867 C CB . TRP A 1 760 ? -9.812 26.287 86.086 1.00 127.95 ? 760 TRP A CB 1 ATOM 5868 C CG . TRP A 1 760 ? -10.542 27.525 86.524 1.00 121.44 ? 760 TRP A CG 1 ATOM 5869 C CD1 . TRP A 1 760 ? -10.558 28.734 85.891 1.00 121.32 ? 760 TRP A CD1 1 ATOM 5870 C CD2 . TRP A 1 760 ? -11.365 27.673 87.690 1.00 124.25 ? 760 TRP A CD2 1 ATOM 5871 N NE1 . TRP A 1 760 ? -11.338 29.626 86.590 1.00 108.52 ? 760 TRP A NE1 1 ATOM 5872 C CE2 . TRP A 1 760 ? -11.844 28.999 87.698 1.00 114.62 ? 760 TRP A CE2 1 ATOM 5873 C CE3 . TRP A 1 760 ? -11.742 26.814 88.727 1.00 108.39 ? 760 TRP A CE3 1 ATOM 5874 C CZ2 . TRP A 1 760 ? -12.679 29.486 88.703 1.00 98.70 ? 760 TRP A CZ2 1 ATOM 5875 C CZ3 . TRP A 1 760 ? -12.573 27.300 89.723 1.00 104.62 ? 760 TRP A CZ3 1 ATOM 5876 C CH2 . TRP A 1 760 ? -13.032 28.623 89.703 1.00 98.60 ? 760 TRP A CH2 1 ATOM 5877 N N . GLU A 1 761 ? -7.901 27.579 88.542 1.00 99.74 ? 761 GLU A N 1 ATOM 5878 C CA . GLU A 1 761 ? -7.970 27.957 89.947 1.00 119.01 ? 761 GLU A CA 1 ATOM 5879 C C . GLU A 1 761 ? -8.712 29.283 90.081 1.00 125.40 ? 761 GLU A C 1 ATOM 5880 O O . GLU A 1 761 ? -9.137 29.866 89.084 1.00 130.36 ? 761 GLU A O 1 ATOM 5881 C CB . GLU A 1 761 ? -6.572 28.049 90.562 1.00 137.29 ? 761 GLU A CB 1 ATOM 5882 C CG . GLU A 1 761 ? -5.651 29.058 89.899 1.00 143.14 ? 761 GLU A CG 1 ATOM 5883 C CD . GLU A 1 761 ? -4.286 29.117 90.560 1.00 151.33 ? 761 GLU A CD 1 ATOM 5884 O OE1 . GLU A 1 761 ? -3.451 29.943 90.133 1.00 146.50 ? 761 GLU A OE1 1 ATOM 5885 O OE2 . GLU A 1 761 ? -4.048 28.337 91.507 1.00 147.40 ? 761 GLU A OE2 1 ATOM 5886 N N . HIS A 1 762 ? -8.863 29.760 91.311 1.00 129.48 ? 762 HIS A N 1 ATOM 5887 C CA . HIS A 1 762 ? -9.679 30.941 91.567 1.00 125.35 ? 762 HIS A CA 1 ATOM 5888 C C . HIS A 1 762 ? -8.866 32.160 91.991 1.00 117.02 ? 762 HIS A C 1 ATOM 5889 O O . HIS A 1 762 ? -8.287 32.188 93.076 1.00 137.22 ? 762 HIS A O 1 ATOM 5890 C CB . HIS A 1 762 ? -10.725 30.631 92.639 1.00 113.87 ? 762 HIS A CB 1 ATOM 5891 C CG . HIS A 1 762 ? -11.540 31.817 93.047 1.00 130.95 ? 762 HIS A CG 1 ATOM 5892 N ND1 . HIS A 1 762 ? -11.922 32.044 94.352 1.00 139.70 ? 762 HIS A ND1 1 ATOM 5893 C CD2 . HIS A 1 762 ? -12.049 32.842 92.323 1.00 130.01 ? 762 HIS A CD2 1 ATOM 5894 C CE1 . HIS A 1 762 ? -12.628 33.158 94.415 1.00 134.62 ? 762 HIS A CE1 1 ATOM 5895 N NE2 . HIS A 1 762 ? -12.721 33.662 93.197 1.00 135.99 ? 762 HIS A NE2 1 ATOM 5896 N N . LYS A 1 763 ? -8.830 33.165 91.123 1.00 108.86 ? 763 LYS A N 1 ATOM 5897 C CA . LYS A 1 763 ? -8.304 34.476 91.482 1.00 138.18 ? 763 LYS A CA 1 ATOM 5898 C C . LYS A 1 763 ? -9.478 35.382 91.835 1.00 145.43 ? 763 LYS A C 1 ATOM 5899 O O . LYS A 1 763 ? -10.437 35.480 91.072 1.00 161.51 ? 763 LYS A O 1 ATOM 5900 C CB . LYS A 1 763 ? -7.480 35.069 90.339 1.00 148.08 ? 763 LYS A CB 1 ATOM 5901 C CG . LYS A 1 763 ? -6.109 34.435 90.154 1.00 145.53 ? 763 LYS A CG 1 ATOM 5902 C CD . LYS A 1 763 ? -5.073 35.066 91.073 1.00 152.65 ? 763 LYS A CD 1 ATOM 5903 C CE . LYS A 1 763 ? -3.668 34.592 90.729 1.00 146.51 ? 763 LYS A CE 1 ATOM 5904 N NZ . LYS A 1 763 ? -2.631 35.283 91.544 1.00 142.12 ? 763 LYS A NZ 1 ATOM 5905 N N . GLU A 1 764 ? -9.412 36.038 92.989 1.00 134.03 ? 764 GLU A N 1 ATOM 5906 C CA . GLU A 1 764 ? -10.558 36.797 93.483 1.00 147.31 ? 764 GLU A CA 1 ATOM 5907 C C . GLU A 1 764 ? -10.706 38.161 92.806 1.00 145.45 ? 764 GLU A C 1 ATOM 5908 O O . GLU A 1 764 ? -11.790 38.746 92.816 1.00 155.70 ? 764 GLU A O 1 ATOM 5909 C CB . GLU A 1 764 ? -10.468 36.971 95.001 1.00 157.26 ? 764 GLU A CB 1 ATOM 5910 C CG . GLU A 1 764 ? -9.240 37.715 95.487 1.00 164.57 ? 764 GLU A CG 1 ATOM 5911 C CD . GLU A 1 764 ? -9.187 37.805 97.000 1.00 172.77 ? 764 GLU A CD 1 ATOM 5912 O OE1 . GLU A 1 764 ? -8.400 38.622 97.523 1.00 182.61 ? 764 GLU A OE1 1 ATOM 5913 O OE2 . GLU A 1 764 ? -9.934 37.057 97.666 1.00 163.15 ? 764 GLU A OE2 1 ATOM 5914 N N . ASN A 1 765 ? -9.626 38.665 92.219 1.00 171.61 ? 765 ASN A N 1 ATOM 5915 C CA . ASN A 1 765 ? -9.699 39.894 91.429 1.00 168.42 ? 765 ASN A CA 1 ATOM 5916 C C . ASN A 1 765 ? -8.970 39.762 90.093 1.00 161.16 ? 765 ASN A C 1 ATOM 5917 O O . ASN A 1 765 ? -8.024 40.500 89.823 1.00 167.86 ? 765 ASN A O 1 ATOM 5918 C CB . ASN A 1 765 ? -9.126 41.071 92.220 1.00 178.17 ? 765 ASN A CB 1 ATOM 5919 C CG . ASN A 1 765 ? -9.912 41.364 93.483 1.00 187.31 ? 765 ASN A CG 1 ATOM 5920 O OD1 . ASN A 1 765 ? -9.597 40.851 94.557 1.00 196.05 ? 765 ASN A OD1 1 ATOM 5921 N ND2 . ASN A 1 765 ? -10.942 42.194 93.360 1.00 174.54 ? 765 ASN A ND2 1 ATOM 5922 N N . PRO A 1 766 ? -9.409 38.810 89.256 1.00 141.18 ? 766 PRO A N 1 ATOM 5923 C CA . PRO A 1 766 ? -8.721 38.471 88.007 1.00 140.47 ? 766 PRO A CA 1 ATOM 5924 C C . PRO A 1 766 ? -8.889 39.484 86.875 1.00 129.54 ? 766 PRO A C 1 ATOM 5925 O O . PRO A 1 766 ? -10.005 39.947 86.644 1.00 128.48 ? 766 PRO A O 1 ATOM 5926 C CB . PRO A 1 766 ? -9.375 37.146 87.621 1.00 140.41 ? 766 PRO A CB 1 ATOM 5927 C CG . PRO A 1 766 ? -10.784 37.301 88.092 1.00 121.41 ? 766 PRO A CG 1 ATOM 5928 C CD . PRO A 1 766 ? -10.726 38.151 89.342 1.00 128.13 ? 766 PRO A CD 1 ATOM 5929 N N . GLU A 1 767 ? -7.805 39.831 86.187 1.00 136.80 ? 767 GLU A N 1 ATOM 5930 C CA . GLU A 1 767 ? -7.932 40.258 84.798 1.00 144.52 ? 767 GLU A CA 1 ATOM 5931 C C . GLU A 1 767 ? -7.050 39.335 83.954 1.00 142.36 ? 767 GLU A C 1 ATOM 5932 O O . GLU A 1 767 ? -5.827 39.459 83.928 1.00 167.21 ? 767 GLU A O 1 ATOM 5933 C CB . GLU A 1 767 ? -7.558 41.743 84.624 1.00 164.10 ? 767 GLU A CB 1 ATOM 5934 C CG . GLU A 1 767 ? -6.140 42.162 85.044 1.00 178.06 ? 767 GLU A CG 1 ATOM 5935 C CD . GLU A 1 767 ? -5.889 42.049 86.537 1.00 190.66 ? 767 GLU A CD 1 ATOM 5936 O OE1 . GLU A 1 767 ? -6.870 42.027 87.309 1.00 197.27 ? 767 GLU A OE1 1 ATOM 5937 O OE2 . GLU A 1 767 ? -4.707 41.975 86.937 1.00 193.90 ? 767 GLU A OE2 1 ATOM 5938 N N . THR A 1 768 ? -7.683 38.382 83.283 1.00 130.83 ? 768 THR A N 1 ATOM 5939 C CA . THR A 1 768 ? -6.947 37.392 82.506 1.00 130.69 ? 768 THR A CA 1 ATOM 5940 C C . THR A 1 768 ? -7.627 37.049 81.187 1.00 125.06 ? 768 THR A C 1 ATOM 5941 O O . THR A 1 768 ? -7.055 37.233 80.112 1.00 146.77 ? 768 THR A O 1 ATOM 5942 C CB . THR A 1 768 ? -6.717 36.115 83.316 1.00 139.86 ? 768 THR A CB 1 ATOM 5943 O OG1 . THR A 1 768 ? -6.664 36.445 84.708 1.00 145.99 ? 768 THR A OG1 1 ATOM 5944 C CG2 . THR A 1 768 ? -5.399 35.483 82.915 1.00 140.38 ? 768 THR A CG2 1 ATOM 5945 N N . GLU A 1 769 ? -8.854 36.539 81.335 1.00 113.20 ? 769 GLU A N 1 ATOM 5946 C CA . GLU A 1 769 ? -9.645 35.765 80.365 1.00 111.84 ? 769 GLU A CA 1 ATOM 5947 C C . GLU A 1 769 ? -9.276 34.286 80.470 1.00 113.51 ? 769 GLU A C 1 ATOM 5948 O O . GLU A 1 769 ? -10.021 33.414 80.020 1.00 108.82 ? 769 GLU A O 1 ATOM 5949 C CB . GLU A 1 769 ? -9.458 36.272 78.923 1.00 117.52 ? 769 GLU A CB 1 ATOM 5950 C CG . GLU A 1 769 ? -10.215 35.490 77.852 1.00 116.08 ? 769 GLU A CG 1 ATOM 5951 C CD . GLU A 1 769 ? -9.974 36.018 76.450 1.00 130.15 ? 769 GLU A CD 1 ATOM 5952 O OE1 . GLU A 1 769 ? -9.882 35.197 75.513 1.00 133.97 ? 769 GLU A OE1 1 ATOM 5953 O OE2 . GLU A 1 769 ? -9.884 37.251 76.282 1.00 140.77 ? 769 GLU A OE2 1 ATOM 5954 N N . GLU A 1 770 ? -8.150 33.999 81.112 1.00 120.02 ? 770 GLU A N 1 ATOM 5955 C CA . GLU A 1 770 ? -7.829 32.630 81.498 1.00 128.60 ? 770 GLU A CA 1 ATOM 5956 C C . GLU A 1 770 ? -8.491 32.280 82.829 1.00 136.84 ? 770 GLU A C 1 ATOM 5957 O O . GLU A 1 770 ? -8.971 31.163 83.024 1.00 137.84 ? 770 GLU A O 1 ATOM 5958 C CB . GLU A 1 770 ? -6.317 32.427 81.583 1.00 150.64 ? 770 GLU A CB 1 ATOM 5959 C CG . GLU A 1 770 ? -5.885 30.982 81.768 1.00 171.48 ? 770 GLU A CG 1 ATOM 5960 C CD . GLU A 1 770 ? -5.937 30.181 80.480 1.00 173.58 ? 770 GLU A CD 1 ATOM 5961 O OE1 . GLU A 1 770 ? -6.292 30.757 79.429 1.00 162.17 ? 770 GLU A OE1 1 ATOM 5962 O OE2 . GLU A 1 770 ? -5.617 28.974 80.518 1.00 171.81 ? 770 GLU A OE2 1 ATOM 5963 N N . ASP A 1 771 ? -8.504 33.248 83.742 1.00 138.71 ? 771 ASP A N 1 ATOM 5964 C CA . ASP A 1 771 ? -8.978 33.027 85.105 1.00 143.47 ? 771 ASP A CA 1 ATOM 5965 C C . ASP A 1 771 ? -10.496 33.076 85.226 1.00 126.82 ? 771 ASP A C 1 ATOM 5966 O O . ASP A 1 771 ? -11.062 32.594 86.207 1.00 123.49 ? 771 ASP A O 1 ATOM 5967 C CB . ASP A 1 771 ? -8.358 34.055 86.050 1.00 161.17 ? 771 ASP A CB 1 ATOM 5968 C CG . ASP A 1 771 ? -6.852 33.927 86.140 1.00 182.06 ? 771 ASP A CG 1 ATOM 5969 O OD1 . ASP A 1 771 ? -6.266 33.204 85.308 1.00 186.93 ? 771 ASP A OD1 1 ATOM 5970 O OD2 . ASP A 1 771 ? -6.253 34.564 87.030 1.00 189.71 ? 771 ASP A OD2 1 ATOM 5971 N N . VAL A 1 772 ? -11.154 33.665 84.237 1.00 116.20 ? 772 VAL A N 1 ATOM 5972 C CA . VAL A 1 772 ? -12.608 33.699 84.235 1.00 113.13 ? 772 VAL A CA 1 ATOM 5973 C C . VAL A 1 772 ? -13.145 32.331 83.842 1.00 110.18 ? 772 VAL A C 1 ATOM 5974 O O . VAL A 1 772 ? -13.827 31.669 84.625 1.00 126.03 ? 772 VAL A O 1 ATOM 5975 C CB . VAL A 1 772 ? -13.154 34.768 83.279 1.00 108.40 ? 772 VAL A CB 1 ATOM 5976 C CG1 . VAL A 1 772 ? -14.673 34.811 83.349 1.00 108.92 ? 772 VAL A CG1 1 ATOM 5977 C CG2 . VAL A 1 772 ? -12.568 36.122 83.623 1.00 107.36 ? 772 VAL A CG2 1 ATOM 5978 N N . GLY A 1 773 ? -12.833 31.914 82.621 1.00 92.58 ? 773 GLY A N 1 ATOM 5979 C CA . GLY A 1 773 ? -13.263 30.622 82.125 1.00 89.07 ? 773 GLY A CA 1 ATOM 5980 C C . GLY A 1 773 ? -13.111 30.525 80.622 1.00 86.85 ? 773 GLY A C 1 ATOM 5981 O O . GLY A 1 773 ? -12.536 31.414 79.995 1.00 88.67 ? 773 GLY A O 1 ATOM 5982 N N . PRO A 1 774 ? -13.636 29.442 80.031 1.00 83.66 ? 774 PRO A N 1 ATOM 5983 C CA . PRO A 1 774 ? -13.538 29.222 78.586 1.00 91.30 ? 774 PRO A CA 1 ATOM 5984 C C . PRO A 1 774 ? -14.319 30.268 77.803 1.00 89.53 ? 774 PRO A C 1 ATOM 5985 O O . PRO A 1 774 ? -15.162 30.964 78.371 1.00 79.35 ? 774 PRO A O 1 ATOM 5986 C CB . PRO A 1 774 ? -14.146 27.830 78.402 1.00 89.17 ? 774 PRO A CB 1 ATOM 5987 C CG . PRO A 1 774 ? -15.086 27.687 79.545 1.00 87.88 ? 774 PRO A CG 1 ATOM 5988 C CD . PRO A 1 774 ? -14.419 28.388 80.696 1.00 89.21 ? 774 PRO A CD 1 ATOM 5989 N N . VAL A 1 775 ? -14.038 30.377 76.510 1.00 100.55 ? 775 VAL A N 1 ATOM 5990 C CA . VAL A 1 775 ? -14.707 31.363 75.676 1.00 82.83 ? 775 VAL A CA 1 ATOM 5991 C C . VAL A 1 775 ? -15.973 30.781 75.062 1.00 86.81 ? 775 VAL A C 1 ATOM 5992 O O . VAL A 1 775 ? -15.916 29.853 74.256 1.00 91.37 ? 775 VAL A O 1 ATOM 5993 C CB . VAL A 1 775 ? -13.786 31.871 74.548 1.00 79.40 ? 775 VAL A CB 1 ATOM 5994 C CG1 . VAL A 1 775 ? -14.511 32.893 73.691 1.00 83.94 ? 775 VAL A CG1 1 ATOM 5995 C CG2 . VAL A 1 775 ? -12.510 32.461 75.124 1.00 88.25 ? 775 VAL A CG2 1 ATOM 5996 N N . VAL A 1 776 ? -17.116 31.330 75.458 1.00 91.21 ? 776 VAL A N 1 ATOM 5997 C CA . VAL A 1 776 ? -18.392 30.963 74.863 1.00 72.51 ? 776 VAL A CA 1 ATOM 5998 C C . VAL A 1 776 ? -18.771 32.038 73.857 1.00 87.48 ? 776 VAL A C 1 ATOM 5999 O O . VAL A 1 776 ? -18.697 33.231 74.153 1.00 96.20 ? 776 VAL A O 1 ATOM 6000 C CB . VAL A 1 776 ? -19.499 30.808 75.923 1.00 93.83 ? 776 VAL A CB 1 ATOM 6001 C CG1 . VAL A 1 776 ? -20.831 30.484 75.263 1.00 95.28 ? 776 VAL A CG1 1 ATOM 6002 C CG2 . VAL A 1 776 ? -19.120 29.729 76.926 1.00 110.94 ? 776 VAL A CG2 1 ATOM 6003 N N . GLN A 1 777 ? -19.165 31.614 72.662 1.00 101.71 ? 777 GLN A N 1 ATOM 6004 C CA . GLN A 1 777 ? -19.405 32.550 71.574 1.00 86.86 ? 777 GLN A CA 1 ATOM 6005 C C . GLN A 1 777 ? -20.781 32.354 70.943 1.00 84.56 ? 777 GLN A C 1 ATOM 6006 O O . GLN A 1 777 ? -21.063 31.309 70.360 1.00 95.32 ? 777 GLN A O 1 ATOM 6007 C CB . GLN A 1 777 ? -18.309 32.398 70.518 1.00 86.40 ? 777 GLN A CB 1 ATOM 6008 C CG . GLN A 1 777 ? -18.236 33.517 69.504 1.00 89.59 ? 777 GLN A CG 1 ATOM 6009 C CD . GLN A 1 777 ? -17.078 33.340 68.540 1.00 113.78 ? 777 GLN A CD 1 ATOM 6010 O OE1 . GLN A 1 777 ? -16.220 32.479 68.734 1.00 126.39 ? 777 GLN A OE1 1 ATOM 6011 N NE2 . GLN A 1 777 ? -17.050 34.156 67.493 1.00 114.68 ? 777 GLN A NE2 1 ATOM 6012 N N . HIS A 1 778 ? -21.636 33.363 71.072 1.00 76.77 ? 778 HIS A N 1 ATOM 6013 C CA . HIS A 1 778 ? -22.940 33.348 70.417 1.00 71.51 ? 778 HIS A CA 1 ATOM 6014 C C . HIS A 1 778 ? -22.916 34.235 69.181 1.00 74.24 ? 778 HIS A C 1 ATOM 6015 O O . HIS A 1 778 ? -22.515 35.396 69.251 1.00 102.92 ? 778 HIS A O 1 ATOM 6016 C CB . HIS A 1 778 ? -24.043 33.813 71.370 1.00 57.40 ? 778 HIS A CB 1 ATOM 6017 C CG . HIS A 1 778 ? -24.347 32.841 72.466 1.00 73.60 ? 778 HIS A CG 1 ATOM 6018 N ND1 . HIS A 1 778 ? -25.551 32.830 73.136 1.00 88.19 ? 778 HIS A ND1 1 ATOM 6019 C CD2 . HIS A 1 778 ? -23.603 31.850 73.012 1.00 92.23 ? 778 HIS A CD2 1 ATOM 6020 C CE1 . HIS A 1 778 ? -25.538 31.873 74.046 1.00 81.23 ? 778 HIS A CE1 1 ATOM 6021 N NE2 . HIS A 1 778 ? -24.367 31.263 73.992 1.00 97.93 ? 778 HIS A NE2 1 ATOM 6022 N N . ILE A 1 779 ? -23.339 33.684 68.049 1.00 67.29 ? 779 ILE A N 1 ATOM 6023 C CA . ILE A 1 779 ? -23.403 34.445 66.808 1.00 73.02 ? 779 ILE A CA 1 ATOM 6024 C C . ILE A 1 779 ? -24.835 34.503 66.300 1.00 80.94 ? 779 ILE A C 1 ATOM 6025 O O . ILE A 1 779 ? -25.470 33.469 66.104 1.00 62.75 ? 779 ILE A O 1 ATOM 6026 C CB . ILE A 1 779 ? -22.507 33.839 65.712 1.00 85.52 ? 779 ILE A CB 1 ATOM 6027 C CG1 . ILE A 1 779 ? -21.150 33.433 66.286 1.00 99.99 ? 779 ILE A CG1 1 ATOM 6028 C CG2 . ILE A 1 779 ? -22.329 34.823 64.570 1.00 74.41 ? 779 ILE A CG2 1 ATOM 6029 C CD1 . ILE A 1 779 ? -20.372 34.586 66.865 1.00 102.15 ? 779 ILE A CD1 1 ATOM 6030 N N . TYR A 1 780 ? -25.341 35.714 66.094 1.00 80.84 ? 780 TYR A N 1 ATOM 6031 C CA . TYR A 1 780 ? -26.686 35.905 65.566 1.00 50.19 ? 780 TYR A CA 1 ATOM 6032 C C . TYR A 1 780 ? -26.632 36.522 64.176 1.00 59.78 ? 780 TYR A C 1 ATOM 6033 O O . TYR A 1 780 ? -25.851 37.440 63.931 1.00 56.62 ? 780 TYR A O 1 ATOM 6034 C CB . TYR A 1 780 ? -27.512 36.783 66.502 1.00 53.06 ? 780 TYR A CB 1 ATOM 6035 C CG . TYR A 1 780 ? -27.854 36.125 67.816 1.00 68.52 ? 780 TYR A CG 1 ATOM 6036 C CD1 . TYR A 1 780 ? -28.990 35.336 67.942 1.00 72.24 ? 780 TYR A CD1 1 ATOM 6037 C CD2 . TYR A 1 780 ? -27.045 36.294 68.933 1.00 72.29 ? 780 TYR A CD2 1 ATOM 6038 C CE1 . TYR A 1 780 ? -29.313 34.732 69.141 1.00 73.56 ? 780 TYR A CE1 1 ATOM 6039 C CE2 . TYR A 1 780 ? -27.359 35.693 70.139 1.00 93.43 ? 780 TYR A CE2 1 ATOM 6040 C CZ . TYR A 1 780 ? -28.494 34.912 70.236 1.00 88.41 ? 780 TYR A CZ 1 ATOM 6041 O OH . TYR A 1 780 ? -28.815 34.308 71.430 1.00 81.44 ? 780 TYR A OH 1 ATOM 6042 N N . GLU A 1 781 ? -27.459 36.012 63.268 1.00 57.20 ? 781 GLU A N 1 ATOM 6043 C CA . GLU A 1 781 ? -27.472 36.506 61.896 1.00 53.11 ? 781 GLU A CA 1 ATOM 6044 C C . GLU A 1 781 ? -28.874 36.855 61.423 1.00 65.37 ? 781 GLU A C 1 ATOM 6045 O O . GLU A 1 781 ? -29.764 36.007 61.400 1.00 96.08 ? 781 GLU A O 1 ATOM 6046 C CB . GLU A 1 781 ? -26.858 35.479 60.945 1.00 56.00 ? 781 GLU A CB 1 ATOM 6047 C CG . GLU A 1 781 ? -26.900 35.910 59.491 1.00 73.06 ? 781 GLU A CG 1 ATOM 6048 C CD . GLU A 1 781 ? -26.357 34.859 58.545 1.00 97.70 ? 781 GLU A CD 1 ATOM 6049 O OE1 . GLU A 1 781 ? -25.981 35.229 57.414 1.00 98.23 ? 781 GLU A OE1 1 ATOM 6050 O OE2 . GLU A 1 781 ? -26.311 33.669 58.926 1.00 118.01 ? 781 GLU A OE2 1 ATOM 6051 N N . LEU A 1 782 ? -29.057 38.111 61.037 1.00 57.41 ? 782 LEU A N 1 ATOM 6052 C CA . LEU A 1 782 ? -30.318 38.568 60.479 1.00 52.89 ? 782 LEU A CA 1 ATOM 6053 C C . LEU A 1 782 ? -30.179 38.652 58.968 1.00 65.97 ? 782 LEU A C 1 ATOM 6054 O O . LEU A 1 782 ? -29.472 39.515 58.453 1.00 99.61 ? 782 LEU A O 1 ATOM 6055 C CB . LEU A 1 782 ? -30.707 39.928 61.064 1.00 51.68 ? 782 LEU A CB 1 ATOM 6056 C CG . LEU A 1 782 ? -32.002 40.574 60.567 1.00 58.70 ? 782 LEU A CG 1 ATOM 6057 C CD1 . LEU A 1 782 ? -33.206 39.787 61.044 1.00 52.89 ? 782 LEU A CD1 1 ATOM 6058 C CD2 . LEU A 1 782 ? -32.091 42.023 61.018 1.00 54.27 ? 782 LEU A CD2 1 ATOM 6059 N N . ARG A 1 783 ? -30.851 37.756 58.255 1.00 58.30 ? 783 ARG A N 1 ATOM 6060 C CA . ARG A 1 783 ? -30.697 37.704 56.808 1.00 82.33 ? 783 ARG A CA 1 ATOM 6061 C C . ARG A 1 783 ? -32.007 37.939 56.077 1.00 61.56 ? 783 ARG A C 1 ATOM 6062 O O . ARG A 1 783 ? -33.030 37.330 56.393 1.00 61.98 ? 783 ARG A O 1 ATOM 6063 C CB . ARG A 1 783 ? -30.100 36.361 56.375 1.00 91.69 ? 783 ARG A CB 1 ATOM 6064 C CG . ARG A 1 783 ? -29.760 36.298 54.892 1.00 66.91 ? 783 ARG A CG 1 ATOM 6065 C CD . ARG A 1 783 ? -28.748 35.207 54.586 1.00 73.24 ? 783 ARG A CD 1 ATOM 6066 N NE . ARG A 1 783 ? -28.389 35.173 53.169 1.00 81.45 ? 783 ARG A NE 1 ATOM 6067 C CZ . ARG A 1 783 ? -27.385 35.863 52.635 1.00 82.96 ? 783 ARG A CZ 1 ATOM 6068 N NH1 . ARG A 1 783 ? -26.634 36.646 53.398 1.00 79.49 ? 783 ARG A NH1 1 ATOM 6069 N NH2 . ARG A 1 783 ? -27.133 35.773 51.336 1.00 91.95 ? 783 ARG A NH2 1 ATOM 6070 N N . ASN A 1 784 ? -31.961 38.835 55.097 1.00 63.70 ? 784 ASN A N 1 ATOM 6071 C CA . ASN A 1 784 ? -33.100 39.074 54.225 1.00 67.73 ? 784 ASN A CA 1 ATOM 6072 C C . ASN A 1 784 ? -32.947 38.275 52.944 1.00 73.05 ? 784 ASN A C 1 ATOM 6073 O O . ASN A 1 784 ? -32.053 38.529 52.145 1.00 78.45 ? 784 ASN A O 1 ATOM 6074 C CB . ASN A 1 784 ? -33.244 40.562 53.907 1.00 66.95 ? 784 ASN A CB 1 ATOM 6075 C CG . ASN A 1 784 ? -34.398 40.848 52.966 1.00 76.23 ? 784 ASN A CG 1 ATOM 6076 O OD1 . ASN A 1 784 ? -35.301 40.026 52.805 1.00 78.71 ? 784 ASN A OD1 1 ATOM 6077 N ND2 . ASN A 1 784 ? -34.376 42.020 52.342 1.00 84.92 ? 784 ASN A ND2 1 ATOM 6078 N N . ASN A 1 785 ? -33.830 37.305 52.758 1.00 71.60 ? 785 ASN A N 1 ATOM 6079 C CA . ASN A 1 785 ? -33.793 36.440 51.591 1.00 81.45 ? 785 ASN A CA 1 ATOM 6080 C C . ASN A 1 785 ? -34.749 36.909 50.508 1.00 99.82 ? 785 ASN A C 1 ATOM 6081 O O . ASN A 1 785 ? -34.329 37.178 49.382 1.00 114.50 ? 785 ASN A O 1 ATOM 6082 C CB . ASN A 1 785 ? -34.093 34.999 51.986 1.00 78.51 ? 785 ASN A CB 1 ATOM 6083 C CG . ASN A 1 785 ? -32.908 34.327 52.641 1.00 96.60 ? 785 ASN A CG 1 ATOM 6084 O OD1 . ASN A 1 785 ? -32.798 34.296 53.866 1.00 94.91 ? 785 ASN A OD1 1 ATOM 6085 N ND2 . ASN A 1 785 ? -31.999 33.801 51.823 1.00 90.11 ? 785 ASN A ND2 1 ATOM 6086 N N . GLY A 1 786 ? -36.032 36.990 50.854 1.00 110.82 ? 786 GLY A N 1 ATOM 6087 C CA . GLY A 1 786 ? -37.085 37.270 49.894 1.00 91.40 ? 786 GLY A CA 1 ATOM 6088 C C . GLY A 1 786 ? -36.810 38.509 49.072 1.00 87.97 ? 786 GLY A C 1 ATOM 6089 O O . GLY A 1 786 ? -36.088 39.401 49.516 1.00 114.01 ? 786 GLY A O 1 ATOM 6090 N N . PRO A 1 787 ? -37.387 38.564 47.863 1.00 91.69 ? 787 PRO A N 1 ATOM 6091 C CA . PRO A 1 787 ? -37.011 39.492 46.788 1.00 96.15 ? 787 PRO A CA 1 ATOM 6092 C C . PRO A 1 787 ? -36.950 40.947 47.229 1.00 91.20 ? 787 PRO A C 1 ATOM 6093 O O . PRO A 1 787 ? -35.984 41.643 46.917 1.00 92.68 ? 787 PRO A O 1 ATOM 6094 C CB . PRO A 1 787 ? -38.120 39.291 45.747 1.00 95.77 ? 787 PRO A CB 1 ATOM 6095 C CG . PRO A 1 787 ? -39.255 38.680 46.501 1.00 95.37 ? 787 PRO A CG 1 ATOM 6096 C CD . PRO A 1 787 ? -38.614 37.820 47.538 1.00 93.42 ? 787 PRO A CD 1 ATOM 6097 N N . SER A 1 788 ? -37.963 41.391 47.961 1.00 84.46 ? 788 SER A N 1 ATOM 6098 C CA . SER A 1 788 ? -38.024 42.775 48.395 1.00 87.65 ? 788 SER A CA 1 ATOM 6099 C C . SER A 1 788 ? -37.006 43.038 49.495 1.00 86.66 ? 788 SER A C 1 ATOM 6100 O O . SER A 1 788 ? -36.756 42.178 50.340 1.00 80.62 ? 788 SER A O 1 ATOM 6101 C CB . SER A 1 788 ? -39.432 43.119 48.879 1.00 116.47 ? 788 SER A CB 1 ATOM 6102 O OG . SER A 1 788 ? -40.395 42.827 47.882 1.00 134.53 ? 788 SER A OG 1 ATOM 6103 N N . SER A 1 789 ? -36.412 44.226 49.476 1.00 82.27 ? 789 SER A N 1 ATOM 6104 C CA . SER A 1 789 ? -35.488 44.622 50.529 1.00 84.87 ? 789 SER A CA 1 ATOM 6105 C C . SER A 1 789 ? -36.229 45.388 51.619 1.00 82.55 ? 789 SER A C 1 ATOM 6106 O O . SER A 1 789 ? -37.429 45.632 51.503 1.00 79.24 ? 789 SER A O 1 ATOM 6107 C CB . SER A 1 789 ? -34.356 45.472 49.952 1.00 83.69 ? 789 SER A CB 1 ATOM 6108 O OG . SER A 1 789 ? -34.869 46.496 49.121 1.00 86.27 ? 789 SER A OG 1 ATOM 6109 N N . PHE A 1 790 ? -35.522 45.764 52.679 1.00 76.23 ? 790 PHE A N 1 ATOM 6110 C CA . PHE A 1 790 ? -36.117 46.618 53.699 1.00 69.70 ? 790 PHE A CA 1 ATOM 6111 C C . PHE A 1 790 ? -35.110 47.646 54.200 1.00 73.27 ? 790 PHE A C 1 ATOM 6112 O O . PHE A 1 790 ? -33.918 47.367 54.306 1.00 79.20 ? 790 PHE A O 1 ATOM 6113 C CB . PHE A 1 790 ? -36.683 45.786 54.860 1.00 67.74 ? 790 PHE A CB 1 ATOM 6114 C CG . PHE A 1 790 ? -35.648 45.044 55.662 1.00 62.87 ? 790 PHE A CG 1 ATOM 6115 C CD1 . PHE A 1 790 ? -34.985 45.661 56.711 1.00 71.24 ? 790 PHE A CD1 1 ATOM 6116 C CD2 . PHE A 1 790 ? -35.370 43.716 55.395 1.00 65.46 ? 790 PHE A CD2 1 ATOM 6117 C CE1 . PHE A 1 790 ? -34.043 44.976 57.454 1.00 58.37 ? 790 PHE A CE1 1 ATOM 6118 C CE2 . PHE A 1 790 ? -34.431 43.025 56.142 1.00 73.91 ? 790 PHE A CE2 1 ATOM 6119 C CZ . PHE A 1 790 ? -33.769 43.657 57.174 1.00 58.75 ? 790 PHE A CZ 1 ATOM 6120 N N . SER A 1 791 ? -35.606 48.844 54.491 1.00 89.79 ? 791 SER A N 1 ATOM 6121 C CA . SER A 1 791 ? -34.752 49.970 54.841 1.00 74.55 ? 791 SER A CA 1 ATOM 6122 C C . SER A 1 791 ? -34.290 49.962 56.296 1.00 68.30 ? 791 SER A C 1 ATOM 6123 O O . SER A 1 791 ? -33.133 50.261 56.577 1.00 71.12 ? 791 SER A O 1 ATOM 6124 C CB . SER A 1 791 ? -35.477 51.278 54.537 1.00 76.18 ? 791 SER A CB 1 ATOM 6125 O OG . SER A 1 791 ? -36.797 51.247 55.046 1.00 107.03 ? 791 SER A OG 1 ATOM 6126 N N . LYS A 1 792 ? -35.188 49.630 57.218 1.00 65.10 ? 792 LYS A N 1 ATOM 6127 C CA . LYS A 1 792 ? -34.857 49.684 58.641 1.00 74.04 ? 792 LYS A CA 1 ATOM 6128 C C . LYS A 1 792 ? -35.437 48.522 59.443 1.00 81.74 ? 792 LYS A C 1 ATOM 6129 O O . LYS A 1 792 ? -36.557 48.077 59.190 1.00 89.15 ? 792 LYS A O 1 ATOM 6130 C CB . LYS A 1 792 ? -35.335 51.007 59.248 1.00 66.57 ? 792 LYS A CB 1 ATOM 6131 C CG . LYS A 1 792 ? -34.461 52.205 58.914 1.00 70.75 ? 792 LYS A CG 1 ATOM 6132 C CD . LYS A 1 792 ? -34.877 53.428 59.715 1.00 89.81 ? 792 LYS A CD 1 ATOM 6133 C CE . LYS A 1 792 ? -33.957 54.609 59.454 1.00 92.70 ? 792 LYS A CE 1 ATOM 6134 N NZ . LYS A 1 792 ? -34.349 55.795 60.266 1.00 96.93 ? 792 LYS A NZ 1 ATOM 6135 N N . ALA A 1 793 ? -34.668 48.044 60.417 1.00 77.56 ? 793 ALA A N 1 ATOM 6136 C CA . ALA A 1 793 ? -35.129 46.981 61.305 1.00 87.64 ? 793 ALA A CA 1 ATOM 6137 C C . ALA A 1 793 ? -34.522 47.110 62.696 1.00 81.18 ? 793 ALA A C 1 ATOM 6138 O O . ALA A 1 793 ? -33.476 47.734 62.877 1.00 73.13 ? 793 ALA A O 1 ATOM 6139 C CB . ALA A 1 793 ? -34.806 45.621 60.722 1.00 56.46 ? 793 ALA A CB 1 ATOM 6140 N N . MET A 1 794 ? -35.192 46.511 63.674 1.00 63.73 ? 794 MET A N 1 ATOM 6141 C CA . MET A 1 794 ? -34.710 46.507 65.047 1.00 57.51 ? 794 MET A CA 1 ATOM 6142 C C . MET A 1 794 ? -34.364 45.091 65.479 1.00 73.13 ? 794 MET A C 1 ATOM 6143 O O . MET A 1 794 ? -35.015 44.132 65.069 1.00 64.03 ? 794 MET A O 1 ATOM 6144 C CB . MET A 1 794 ? -35.754 47.105 65.989 1.00 60.50 ? 794 MET A CB 1 ATOM 6145 C CG . MET A 1 794 ? -36.074 48.562 65.711 1.00 65.52 ? 794 MET A CG 1 ATOM 6146 S SD . MET A 1 794 ? -34.640 49.632 65.911 1.00 96.71 ? 794 MET A SD 1 ATOM 6147 C CE . MET A 1 794 ? -34.227 49.329 67.625 1.00 64.89 ? 794 MET A CE 1 ATOM 6148 N N . LEU A 1 795 ? -33.333 44.965 66.307 1.00 63.87 ? 795 LEU A N 1 ATOM 6149 C CA . LEU A 1 795 ? -32.911 43.662 66.799 1.00 57.88 ? 795 LEU A CA 1 ATOM 6150 C C . LEU A 1 795 ? -32.688 43.716 68.305 1.00 78.68 ? 795 LEU A C 1 ATOM 6151 O O . LEU A 1 795 ? -31.918 44.540 68.799 1.00 101.14 ? 795 LEU A O 1 ATOM 6152 C CB . LEU A 1 795 ? -31.640 43.207 66.079 1.00 60.88 ? 795 LEU A CB 1 ATOM 6153 C CG . LEU A 1 795 ? -31.247 41.733 66.187 1.00 59.81 ? 795 LEU A CG 1 ATOM 6154 C CD1 . LEU A 1 795 ? -30.516 41.301 64.930 1.00 57.20 ? 795 LEU A CD1 1 ATOM 6155 C CD2 . LEU A 1 795 ? -30.379 41.486 67.406 1.00 66.72 ? 795 LEU A CD2 1 ATOM 6156 N N . HIS A 1 796 ? -33.366 42.833 69.031 1.00 69.81 ? 796 HIS A N 1 ATOM 6157 C CA . HIS A 1 796 ? -33.268 42.806 70.484 1.00 71.11 ? 796 HIS A CA 1 ATOM 6158 C C . HIS A 1 796 ? -32.647 41.510 70.987 1.00 72.12 ? 796 HIS A C 1 ATOM 6159 O O . HIS A 1 796 ? -33.203 40.427 70.805 1.00 69.46 ? 796 HIS A O 1 ATOM 6160 C CB . HIS A 1 796 ? -34.647 43.002 71.115 1.00 59.33 ? 796 HIS A CB 1 ATOM 6161 C CG . HIS A 1 796 ? -35.218 44.368 70.902 1.00 68.52 ? 796 HIS A CG 1 ATOM 6162 N ND1 . HIS A 1 796 ? -35.329 45.295 71.916 1.00 98.92 ? 796 HIS A ND1 1 ATOM 6163 C CD2 . HIS A 1 796 ? -35.702 44.968 69.789 1.00 67.51 ? 796 HIS A CD2 1 ATOM 6164 C CE1 . HIS A 1 796 ? -35.863 46.405 71.439 1.00 91.55 ? 796 HIS A CE1 1 ATOM 6165 N NE2 . HIS A 1 796 ? -36.098 46.233 70.150 1.00 100.65 ? 796 HIS A NE2 1 ATOM 6166 N N . LEU A 1 797 ? -31.487 41.631 71.623 1.00 66.17 ? 797 LEU A N 1 ATOM 6167 C CA . LEU A 1 797 ? -30.821 40.487 72.224 1.00 56.63 ? 797 LEU A CA 1 ATOM 6168 C C . LEU A 1 797 ? -31.048 40.461 73.726 1.00 73.81 ? 797 LEU A C 1 ATOM 6169 O O . LEU A 1 797 ? -30.771 41.438 74.424 1.00 82.33 ? 797 LEU A O 1 ATOM 6170 C CB . LEU A 1 797 ? -29.322 40.510 71.925 1.00 73.86 ? 797 LEU A CB 1 ATOM 6171 C CG . LEU A 1 797 ? -28.496 39.444 72.650 1.00 72.27 ? 797 LEU A CG 1 ATOM 6172 C CD1 . LEU A 1 797 ? -28.976 38.052 72.280 1.00 59.05 ? 797 LEU A CD1 1 ATOM 6173 C CD2 . LEU A 1 797 ? -27.016 39.601 72.340 1.00 70.04 ? 797 LEU A CD2 1 ATOM 6174 N N . GLN A 1 798 ? -31.567 39.342 74.217 1.00 67.01 ? 798 GLN A N 1 ATOM 6175 C CA . GLN A 1 798 ? -31.694 39.126 75.648 1.00 66.19 ? 798 GLN A CA 1 ATOM 6176 C C . GLN A 1 798 ? -30.574 38.198 76.098 1.00 80.00 ? 798 GLN A C 1 ATOM 6177 O O . GLN A 1 798 ? -30.418 37.102 75.560 1.00 94.37 ? 798 GLN A O 1 ATOM 6178 C CB . GLN A 1 798 ? -33.062 38.539 75.995 1.00 64.88 ? 798 GLN A CB 1 ATOM 6179 C CG . GLN A 1 798 ? -34.237 39.383 75.538 1.00 70.65 ? 798 GLN A CG 1 ATOM 6180 C CD . GLN A 1 798 ? -35.559 38.921 76.126 1.00 87.44 ? 798 GLN A CD 1 ATOM 6181 O OE1 . GLN A 1 798 ? -35.591 38.180 77.109 1.00 82.93 ? 798 GLN A OE1 1 ATOM 6182 N NE2 . GLN A 1 798 ? -36.660 39.360 75.526 1.00 108.48 ? 798 GLN A NE2 1 ATOM 6183 N N . TRP A 1 799 ? -29.789 38.636 77.076 1.00 81.74 ? 799 TRP A N 1 ATOM 6184 C CA . TRP A 1 799 ? -28.623 37.869 77.495 1.00 74.83 ? 799 TRP A CA 1 ATOM 6185 C C . TRP A 1 799 ? -28.667 37.551 78.985 1.00 86.29 ? 799 TRP A C 1 ATOM 6186 O O . TRP A 1 799 ? -29.054 38.393 79.795 1.00 73.88 ? 799 TRP A O 1 ATOM 6187 C CB . TRP A 1 799 ? -27.344 38.639 77.155 1.00 64.66 ? 799 TRP A CB 1 ATOM 6188 C CG . TRP A 1 799 ? -26.087 37.854 77.328 1.00 74.50 ? 799 TRP A CG 1 ATOM 6189 C CD1 . TRP A 1 799 ? -25.335 37.748 78.460 1.00 82.78 ? 799 TRP A CD1 1 ATOM 6190 C CD2 . TRP A 1 799 ? -25.424 37.069 76.332 1.00 85.59 ? 799 TRP A CD2 1 ATOM 6191 N NE1 . TRP A 1 799 ? -24.246 36.942 78.233 1.00 69.92 ? 799 TRP A NE1 1 ATOM 6192 C CE2 . TRP A 1 799 ? -24.277 36.513 76.932 1.00 76.62 ? 799 TRP A CE2 1 ATOM 6193 C CE3 . TRP A 1 799 ? -25.690 36.781 74.990 1.00 93.76 ? 799 TRP A CE3 1 ATOM 6194 C CZ2 . TRP A 1 799 ? -23.399 35.687 76.238 1.00 79.70 ? 799 TRP A CZ2 1 ATOM 6195 C CZ3 . TRP A 1 799 ? -24.818 35.960 74.303 1.00 78.25 ? 799 TRP A CZ3 1 ATOM 6196 C CH2 . TRP A 1 799 ? -23.686 35.422 74.927 1.00 91.91 ? 799 TRP A CH2 1 ATOM 6197 N N . PRO A 1 800 ? -28.258 36.326 79.350 1.00 91.96 ? 800 PRO A N 1 ATOM 6198 C CA . PRO A 1 800 ? -28.208 35.876 80.745 1.00 94.38 ? 800 PRO A CA 1 ATOM 6199 C C . PRO A 1 800 ? -26.975 36.393 81.480 1.00 101.26 ? 800 PRO A C 1 ATOM 6200 O O . PRO A 1 800 ? -25.999 35.654 81.620 1.00 103.51 ? 800 PRO A O 1 ATOM 6201 C CB . PRO A 1 800 ? -28.163 34.354 80.614 1.00 88.21 ? 800 PRO A CB 1 ATOM 6202 C CG . PRO A 1 800 ? -27.475 34.124 79.311 1.00 79.90 ? 800 PRO A CG 1 ATOM 6203 C CD . PRO A 1 800 ? -27.927 35.240 78.409 1.00 73.16 ? 800 PRO A CD 1 ATOM 6204 N N . TYR A 1 801 ? -27.015 37.641 81.939 1.00 87.74 ? 801 TYR A N 1 ATOM 6205 C CA . TYR A 1 801 ? -25.851 38.234 82.585 1.00 91.03 ? 801 TYR A CA 1 ATOM 6206 C C . TYR A 1 801 ? -25.525 37.563 83.915 1.00 92.36 ? 801 TYR A C 1 ATOM 6207 O O . TYR A 1 801 ? -24.415 37.069 84.112 1.00 88.79 ? 801 TYR A O 1 ATOM 6208 C CB . TYR A 1 801 ? -26.055 39.733 82.803 1.00 102.74 ? 801 TYR A CB 1 ATOM 6209 C CG . TYR A 1 801 ? -24.788 40.444 83.220 1.00 115.44 ? 801 TYR A CG 1 ATOM 6210 C CD1 . TYR A 1 801 ? -23.616 40.295 82.485 1.00 122.23 ? 801 TYR A CD1 1 ATOM 6211 C CD2 . TYR A 1 801 ? -24.760 41.262 84.342 1.00 100.24 ? 801 TYR A CD2 1 ATOM 6212 C CE1 . TYR A 1 801 ? -22.451 40.937 82.855 1.00 124.25 ? 801 TYR A CE1 1 ATOM 6213 C CE2 . TYR A 1 801 ? -23.597 41.911 84.721 1.00 124.33 ? 801 TYR A CE2 1 ATOM 6214 C CZ . TYR A 1 801 ? -22.446 41.744 83.973 1.00 138.08 ? 801 TYR A CZ 1 ATOM 6215 O OH . TYR A 1 801 ? -21.285 42.385 84.341 1.00 137.54 ? 801 TYR A OH 1 ATOM 6216 N N . LYS A 1 802 ? -26.496 37.539 84.823 1.00 88.58 ? 802 LYS A N 1 ATOM 6217 C CA . LYS A 1 802 ? -26.290 36.936 86.134 1.00 90.62 ? 802 LYS A CA 1 ATOM 6218 C C . LYS A 1 802 ? -27.455 36.043 86.541 1.00 103.95 ? 802 LYS A C 1 ATOM 6219 O O . LYS A 1 802 ? -28.555 36.149 86.000 1.00 97.89 ? 802 LYS A O 1 ATOM 6220 C CB . LYS A 1 802 ? -26.076 38.015 87.201 1.00 94.14 ? 802 LYS A CB 1 ATOM 6221 C CG . LYS A 1 802 ? -24.749 38.752 87.104 1.00 93.10 ? 802 LYS A CG 1 ATOM 6222 C CD . LYS A 1 802 ? -24.599 39.767 88.228 1.00 102.32 ? 802 LYS A CD 1 ATOM 6223 C CE . LYS A 1 802 ? -25.691 40.831 88.160 1.00 134.85 ? 802 LYS A CE 1 ATOM 6224 N NZ . LYS A 1 802 ? -25.581 41.841 89.252 1.00 122.79 ? 802 LYS A NZ 1 ATOM 6225 N N . TYR A 1 803 ? -27.190 35.146 87.484 1.00 112.01 ? 803 TYR A N 1 ATOM 6226 C CA . TYR A 1 803 ? -28.230 34.338 88.109 1.00 111.30 ? 803 TYR A CA 1 ATOM 6227 C C . TYR A 1 803 ? -27.993 34.306 89.609 1.00 113.98 ? 803 TYR A C 1 ATOM 6228 O O . TYR A 1 803 ? -26.952 33.836 90.062 1.00 108.50 ? 803 TYR A O 1 ATOM 6229 C CB . TYR A 1 803 ? -28.246 32.921 87.537 1.00 105.83 ? 803 TYR A CB 1 ATOM 6230 C CG . TYR A 1 803 ? -29.183 31.972 88.254 1.00 110.85 ? 803 TYR A CG 1 ATOM 6231 C CD1 . TYR A 1 803 ? -30.561 32.097 88.130 1.00 117.42 ? 803 TYR A CD1 1 ATOM 6232 C CD2 . TYR A 1 803 ? -28.688 30.943 89.046 1.00 113.21 ? 803 TYR A CD2 1 ATOM 6233 C CE1 . TYR A 1 803 ? -31.420 31.229 88.781 1.00 121.63 ? 803 TYR A CE1 1 ATOM 6234 C CE2 . TYR A 1 803 ? -29.539 30.069 89.699 1.00 119.16 ? 803 TYR A CE2 1 ATOM 6235 C CZ . TYR A 1 803 ? -30.903 30.217 89.562 1.00 124.31 ? 803 TYR A CZ 1 ATOM 6236 O OH . TYR A 1 803 ? -31.753 29.351 90.211 1.00 126.46 ? 803 TYR A OH 1 ATOM 6237 N N . ASN A 1 804 ? -28.963 34.801 90.371 1.00 117.82 ? 804 ASN A N 1 ATOM 6238 C CA . ASN A 1 804 ? -28.813 34.959 91.814 1.00 130.63 ? 804 ASN A CA 1 ATOM 6239 C C . ASN A 1 804 ? -27.580 35.788 92.168 1.00 129.14 ? 804 ASN A C 1 ATOM 6240 O O . ASN A 1 804 ? -26.704 35.332 92.905 1.00 138.91 ? 804 ASN A O 1 ATOM 6241 C CB . ASN A 1 804 ? -28.757 33.596 92.511 1.00 138.41 ? 804 ASN A CB 1 ATOM 6242 C CG . ASN A 1 804 ? -30.106 32.904 92.546 1.00 142.39 ? 804 ASN A CG 1 ATOM 6243 O OD1 . ASN A 1 804 ? -31.151 33.553 92.505 1.00 152.02 ? 804 ASN A OD1 1 ATOM 6244 N ND2 . ASN A 1 804 ? -30.090 31.578 92.629 1.00 140.56 ? 804 ASN A ND2 1 ATOM 6245 N N . ASN A 1 805 ? -27.512 36.987 91.590 1.00 131.34 ? 805 ASN A N 1 ATOM 6246 C CA . ASN A 1 805 ? -26.543 38.023 91.957 1.00 139.30 ? 805 ASN A CA 1 ATOM 6247 C C . ASN A 1 805 ? -25.106 37.793 91.481 1.00 135.10 ? 805 ASN A C 1 ATOM 6248 O O . ASN A 1 805 ? -24.243 38.639 91.712 1.00 149.90 ? 805 ASN A O 1 ATOM 6249 C CB . ASN A 1 805 ? -26.543 38.234 93.477 1.00 159.66 ? 805 ASN A CB 1 ATOM 6250 C CG . ASN A 1 805 ? -27.485 39.342 93.912 1.00 175.34 ? 805 ASN A CG 1 ATOM 6251 O OD1 . ASN A 1 805 ? -27.713 40.300 93.174 1.00 158.95 ? 805 ASN A OD1 1 ATOM 6252 N ND2 . ASN A 1 805 ? -28.035 39.218 95.117 1.00 225.82 ? 805 ASN A ND2 1 ATOM 6253 N N . ASN A 1 806 ? -24.837 36.666 90.828 1.00 125.02 ? 806 ASN A N 1 ATOM 6254 C CA . ASN A 1 806 ? -23.485 36.421 90.324 1.00 122.27 ? 806 ASN A CA 1 ATOM 6255 C C . ASN A 1 806 ? -23.428 35.909 88.874 1.00 109.72 ? 806 ASN A C 1 ATOM 6256 O O . ASN A 1 806 ? -24.331 35.215 88.402 1.00 101.33 ? 806 ASN A O 1 ATOM 6257 C CB . ASN A 1 806 ? -22.751 35.461 91.264 1.00 122.95 ? 806 ASN A CB 1 ATOM 6258 C CG . ASN A 1 806 ? -23.646 34.364 91.796 1.00 128.51 ? 806 ASN A CG 1 ATOM 6259 O OD1 . ASN A 1 806 ? -24.418 33.763 91.054 1.00 139.53 ? 806 ASN A OD1 1 ATOM 6260 N ND2 . ASN A 1 806 ? -23.549 34.100 93.094 1.00 119.64 ? 806 ASN A ND2 1 ATOM 6261 N N . THR A 1 807 ? -22.335 36.256 88.195 1.00 101.31 ? 807 THR A N 1 ATOM 6262 C CA . THR A 1 807 ? -22.212 36.199 86.734 1.00 94.36 ? 807 THR A CA 1 ATOM 6263 C C . THR A 1 807 ? -22.392 34.821 86.090 1.00 94.42 ? 807 THR A C 1 ATOM 6264 O O . THR A 1 807 ? -21.884 33.823 86.586 1.00 122.94 ? 807 THR A O 1 ATOM 6265 C CB . THR A 1 807 ? -20.829 36.748 86.304 1.00 96.09 ? 807 THR A CB 1 ATOM 6266 O OG1 . THR A 1 807 ? -20.623 38.042 86.887 1.00 97.19 ? 807 THR A OG1 1 ATOM 6267 C CG2 . THR A 1 807 ? -20.723 36.855 84.788 1.00 95.86 ? 807 THR A CG2 1 ATOM 6268 N N . LEU A 1 808 ? -23.107 34.785 84.968 1.00 86.87 ? 808 LEU A N 1 ATOM 6269 C CA . LEU A 1 808 ? -23.261 33.562 84.182 1.00 83.06 ? 808 LEU A CA 1 ATOM 6270 C C . LEU A 1 808 ? -22.332 33.568 82.973 1.00 85.58 ? 808 LEU A C 1 ATOM 6271 O O . LEU A 1 808 ? -21.323 32.866 82.946 1.00 95.85 ? 808 LEU A O 1 ATOM 6272 C CB . LEU A 1 808 ? -24.707 33.398 83.715 1.00 83.09 ? 808 LEU A CB 1 ATOM 6273 C CG . LEU A 1 808 ? -25.752 32.972 84.744 1.00 87.71 ? 808 LEU A CG 1 ATOM 6274 C CD1 . LEU A 1 808 ? -27.140 33.050 84.133 1.00 88.10 ? 808 LEU A CD1 1 ATOM 6275 C CD2 . LEU A 1 808 ? -25.460 31.564 85.230 1.00 93.64 ? 808 LEU A CD2 1 ATOM 6276 N N . LEU A 1 809 ? -22.684 34.366 81.970 1.00 93.25 ? 809 LEU A N 1 ATOM 6277 C CA . LEU A 1 809 ? -21.820 34.574 80.818 1.00 76.94 ? 809 LEU A CA 1 ATOM 6278 C C . LEU A 1 809 ? -21.337 36.016 80.784 1.00 89.21 ? 809 LEU A C 1 ATOM 6279 O O . LEU A 1 809 ? -22.107 36.931 80.495 1.00 102.20 ? 809 LEU A O 1 ATOM 6280 C CB . LEU A 1 809 ? -22.550 34.231 79.523 1.00 77.90 ? 809 LEU A CB 1 ATOM 6281 C CG . LEU A 1 809 ? -22.819 32.748 79.285 1.00 74.48 ? 809 LEU A CG 1 ATOM 6282 C CD1 . LEU A 1 809 ? -23.615 32.551 78.007 1.00 70.05 ? 809 LEU A CD1 1 ATOM 6283 C CD2 . LEU A 1 809 ? -21.512 31.979 79.224 1.00 84.75 ? 809 LEU A CD2 1 ATOM 6284 N N . TYR A 1 810 ? -20.055 36.209 81.070 1.00 104.52 ? 810 TYR A N 1 ATOM 6285 C CA . TYR A 1 810 ? -19.470 37.541 81.131 1.00 100.58 ? 810 TYR A CA 1 ATOM 6286 C C . TYR A 1 810 ? -19.043 37.968 79.737 1.00 96.43 ? 810 TYR A C 1 ATOM 6287 O O . TYR A 1 810 ? -18.168 37.350 79.135 1.00 84.99 ? 810 TYR A O 1 ATOM 6288 C CB . TYR A 1 810 ? -18.280 37.546 82.096 1.00 88.41 ? 810 TYR A CB 1 ATOM 6289 C CG . TYR A 1 810 ? -17.566 38.871 82.256 1.00 89.28 ? 810 TYR A CG 1 ATOM 6290 C CD1 . TYR A 1 810 ? -16.514 39.220 81.421 1.00 90.58 ? 810 TYR A CD1 1 ATOM 6291 C CD2 . TYR A 1 810 ? -17.922 39.756 83.264 1.00 95.49 ? 810 TYR A CD2 1 ATOM 6292 C CE1 . TYR A 1 810 ? -15.850 40.422 81.571 1.00 96.36 ? 810 TYR A CE1 1 ATOM 6293 C CE2 . TYR A 1 810 ? -17.263 40.961 83.423 1.00 103.83 ? 810 TYR A CE2 1 ATOM 6294 C CZ . TYR A 1 810 ? -16.227 41.288 82.573 1.00 101.15 ? 810 TYR A CZ 1 ATOM 6295 O OH . TYR A 1 810 ? -15.564 42.484 82.724 1.00 106.06 ? 810 TYR A OH 1 ATOM 6296 N N . ILE A 1 811 ? -19.656 39.031 79.227 1.00 95.08 ? 811 ILE A N 1 ATOM 6297 C CA . ILE A 1 811 ? -19.373 39.477 77.870 1.00 80.83 ? 811 ILE A CA 1 ATOM 6298 C C . ILE A 1 811 ? -18.147 40.375 77.840 1.00 85.65 ? 811 ILE A C 1 ATOM 6299 O O . ILE A 1 811 ? -18.120 41.426 78.482 1.00 88.86 ? 811 ILE A O 1 ATOM 6300 C CB . ILE A 1 811 ? -20.565 40.235 77.256 1.00 76.41 ? 811 ILE A CB 1 ATOM 6301 C CG1 . ILE A 1 811 ? -21.804 39.338 77.198 1.00 75.19 ? 811 ILE A CG1 1 ATOM 6302 C CG2 . ILE A 1 811 ? -20.210 40.742 75.867 1.00 71.17 ? 811 ILE A CG2 1 ATOM 6303 C CD1 . ILE A 1 811 ? -23.017 40.008 76.567 1.00 62.20 ? 811 ILE A CD1 1 ATOM 6304 N N . LEU A 1 812 ? -17.127 39.943 77.106 1.00 81.80 ? 812 LEU A N 1 ATOM 6305 C CA . LEU A 1 812 ? -15.927 40.747 76.909 1.00 96.00 ? 812 LEU A CA 1 ATOM 6306 C C . LEU A 1 812 ? -16.144 41.823 75.858 1.00 91.72 ? 812 LEU A C 1 ATOM 6307 O O . LEU A 1 812 ? -15.815 42.991 76.060 1.00 98.49 ? 812 LEU A O 1 ATOM 6308 C CB . LEU A 1 812 ? -14.750 39.868 76.486 1.00 100.84 ? 812 LEU A CB 1 ATOM 6309 C CG . LEU A 1 812 ? -14.159 38.878 77.485 1.00 102.19 ? 812 LEU A CG 1 ATOM 6310 C CD1 . LEU A 1 812 ? -13.040 38.097 76.819 1.00 97.43 ? 812 LEU A CD1 1 ATOM 6311 C CD2 . LEU A 1 812 ? -13.651 39.604 78.718 1.00 117.79 ? 812 LEU A CD2 1 ATOM 6312 N N . HIS A 1 813 ? -16.706 41.409 74.730 1.00 84.52 ? 813 HIS A N 1 ATOM 6313 C CA . HIS A 1 813 ? -16.761 42.253 73.549 1.00 88.96 ? 813 HIS A CA 1 ATOM 6314 C C . HIS A 1 813 ? -17.879 41.793 72.620 1.00 84.43 ? 813 HIS A C 1 ATOM 6315 O O . HIS A 1 813 ? -18.329 40.650 72.704 1.00 86.48 ? 813 HIS A O 1 ATOM 6316 C CB . HIS A 1 813 ? -15.408 42.211 72.832 1.00 99.29 ? 813 HIS A CB 1 ATOM 6317 C CG . HIS A 1 813 ? -15.235 43.267 71.786 1.00 121.13 ? 813 HIS A CG 1 ATOM 6318 N ND1 . HIS A 1 813 ? -15.369 44.612 72.056 1.00 147.14 ? 813 HIS A ND1 1 ATOM 6319 C CD2 . HIS A 1 813 ? -14.918 43.176 70.473 1.00 123.75 ? 813 HIS A CD2 1 ATOM 6320 C CE1 . HIS A 1 813 ? -15.153 45.304 70.952 1.00 149.11 ? 813 HIS A CE1 1 ATOM 6321 N NE2 . HIS A 1 813 ? -14.876 44.456 69.977 1.00 142.12 ? 813 HIS A NE2 1 ATOM 6322 N N . TYR A 1 814 ? -18.335 42.679 71.741 1.00 81.01 ? 814 TYR A N 1 ATOM 6323 C CA . TYR A 1 814 ? -19.241 42.271 70.672 1.00 78.93 ? 814 TYR A CA 1 ATOM 6324 C C . TYR A 1 814 ? -18.930 43.031 69.387 1.00 80.87 ? 814 TYR A C 1 ATOM 6325 O O . TYR A 1 814 ? -18.690 44.237 69.409 1.00 93.40 ? 814 TYR A O 1 ATOM 6326 C CB . TYR A 1 814 ? -20.713 42.460 71.075 1.00 68.50 ? 814 TYR A CB 1 ATOM 6327 C CG . TYR A 1 814 ? -21.163 43.891 71.287 1.00 75.69 ? 814 TYR A CG 1 ATOM 6328 C CD1 . TYR A 1 814 ? -21.680 44.643 70.237 1.00 77.89 ? 814 TYR A CD1 1 ATOM 6329 C CD2 . TYR A 1 814 ? -21.099 44.480 72.542 1.00 92.70 ? 814 TYR A CD2 1 ATOM 6330 C CE1 . TYR A 1 814 ? -22.101 45.950 70.429 1.00 72.89 ? 814 TYR A CE1 1 ATOM 6331 C CE2 . TYR A 1 814 ? -21.518 45.785 72.744 1.00 103.00 ? 814 TYR A CE2 1 ATOM 6332 C CZ . TYR A 1 814 ? -22.017 46.515 71.685 1.00 98.41 ? 814 TYR A CZ 1 ATOM 6333 O OH . TYR A 1 814 ? -22.434 47.814 71.883 1.00 109.66 ? 814 TYR A OH 1 ATOM 6334 N N . ASP A 1 815 ? -18.923 42.310 68.270 1.00 76.43 ? 815 ASP A N 1 ATOM 6335 C CA . ASP A 1 815 ? -18.597 42.902 66.978 1.00 85.92 ? 815 ASP A CA 1 ATOM 6336 C C . ASP A 1 815 ? -19.762 42.790 66.002 1.00 77.91 ? 815 ASP A C 1 ATOM 6337 O O . ASP A 1 815 ? -20.619 41.919 66.135 1.00 69.47 ? 815 ASP A O 1 ATOM 6338 C CB . ASP A 1 815 ? -17.348 42.244 66.386 1.00 96.31 ? 815 ASP A CB 1 ATOM 6339 C CG . ASP A 1 815 ? -16.072 42.690 67.075 1.00 113.29 ? 815 ASP A CG 1 ATOM 6340 O OD1 . ASP A 1 815 ? -15.964 43.890 67.406 1.00 136.08 ? 815 ASP A OD1 1 ATOM 6341 O OD2 . ASP A 1 815 ? -15.179 41.844 67.288 1.00 107.76 ? 815 ASP A OD2 1 ATOM 6342 N N . ILE A 1 816 ? -19.787 43.685 65.021 1.00 80.32 ? 816 ILE A N 1 ATOM 6343 C CA . ILE A 1 816 ? -20.869 43.726 64.048 1.00 74.71 ? 816 ILE A CA 1 ATOM 6344 C C . ILE A 1 816 ? -20.333 43.486 62.642 1.00 81.61 ? 816 ILE A C 1 ATOM 6345 O O . ILE A 1 816 ? -19.177 43.789 62.346 1.00 96.26 ? 816 ILE A O 1 ATOM 6346 C CB . ILE A 1 816 ? -21.610 45.084 64.077 1.00 82.56 ? 816 ILE A CB 1 ATOM 6347 C CG1 . ILE A 1 816 ? -21.655 45.655 65.498 1.00 83.35 ? 816 ILE A CG1 1 ATOM 6348 C CG2 . ILE A 1 816 ? -23.011 44.951 63.493 1.00 69.67 ? 816 ILE A CG2 1 ATOM 6349 C CD1 . ILE A 1 816 ? -22.586 44.922 66.430 1.00 70.77 ? 816 ILE A CD1 1 ATOM 6350 N N . ASP A 1 817 ? -21.174 42.925 61.782 1.00 80.87 ? 817 ASP A N 1 ATOM 6351 C CA . ASP A 1 817 ? -20.840 42.778 60.375 1.00 87.63 ? 817 ASP A CA 1 ATOM 6352 C C . ASP A 1 817 ? -22.046 43.179 59.531 1.00 94.44 ? 817 ASP A C 1 ATOM 6353 O O . ASP A 1 817 ? -23.114 42.576 59.639 1.00 99.56 ? 817 ASP A O 1 ATOM 6354 C CB . ASP A 1 817 ? -20.412 41.343 60.070 1.00 91.48 ? 817 ASP A CB 1 ATOM 6355 C CG . ASP A 1 817 ? -19.318 41.271 59.027 1.00 119.21 ? 817 ASP A CG 1 ATOM 6356 O OD1 . ASP A 1 817 ? -19.270 42.159 58.149 1.00 139.84 ? 817 ASP A OD1 1 ATOM 6357 O OD2 . ASP A 1 817 ? -18.503 40.326 59.089 1.00 109.02 ? 817 ASP A OD2 1 ATOM 6358 N N . GLY A 1 818 ? -21.878 44.202 58.700 1.00 91.83 ? 818 GLY A N 1 ATOM 6359 C CA . GLY A 1 818 ? -22.974 44.697 57.887 1.00 91.55 ? 818 GLY A CA 1 ATOM 6360 C C . GLY A 1 818 ? -23.600 45.954 58.461 1.00 87.78 ? 818 GLY A C 1 ATOM 6361 O O . GLY A 1 818 ? -23.136 46.472 59.475 1.00 91.70 ? 818 GLY A O 1 ATOM 6362 N N . PRO A 1 819 ? -24.669 46.445 57.819 1.00 86.81 ? 819 PRO A N 1 ATOM 6363 C CA . PRO A 1 819 ? -25.311 47.715 58.178 1.00 81.38 ? 819 PRO A CA 1 ATOM 6364 C C . PRO A 1 819 ? -26.095 47.645 59.483 1.00 72.65 ? 819 PRO A C 1 ATOM 6365 O O . PRO A 1 819 ? -27.324 47.600 59.461 1.00 74.07 ? 819 PRO A O 1 ATOM 6366 C CB . PRO A 1 819 ? -26.252 47.968 56.999 1.00 84.25 ? 819 PRO A CB 1 ATOM 6367 C CG . PRO A 1 819 ? -26.608 46.610 56.523 1.00 90.65 ? 819 PRO A CG 1 ATOM 6368 C CD . PRO A 1 819 ? -25.368 45.771 56.711 1.00 106.35 ? 819 PRO A CD 1 ATOM 6369 N N . MET A 1 820 ? -25.389 47.636 60.608 1.00 73.35 ? 820 MET A N 1 ATOM 6370 C CA . MET A 1 820 ? -26.048 47.575 61.905 1.00 66.16 ? 820 MET A CA 1 ATOM 6371 C C . MET A 1 820 ? -25.236 48.264 62.998 1.00 68.71 ? 820 MET A C 1 ATOM 6372 O O . MET A 1 820 ? -24.008 48.199 63.009 1.00 90.56 ? 820 MET A O 1 ATOM 6373 C CB . MET A 1 820 ? -26.311 46.116 62.282 1.00 61.71 ? 820 MET A CB 1 ATOM 6374 C CG . MET A 1 820 ? -26.912 45.913 63.657 1.00 57.92 ? 820 MET A CG 1 ATOM 6375 S SD . MET A 1 820 ? -26.908 44.177 64.137 1.00 84.55 ? 820 MET A SD 1 ATOM 6376 C CE . MET A 1 820 ? -28.078 43.502 62.967 1.00 94.60 ? 820 MET A CE 1 ATOM 6377 N N . ASN A 1 821 ? -25.935 48.932 63.910 1.00 68.78 ? 821 ASN A N 1 ATOM 6378 C CA . ASN A 1 821 ? -25.330 49.453 65.128 1.00 72.47 ? 821 ASN A CA 1 ATOM 6379 C C . ASN A 1 821 ? -25.939 48.742 66.323 1.00 72.52 ? 821 ASN A C 1 ATOM 6380 O O . ASN A 1 821 ? -27.063 48.258 66.244 1.00 92.56 ? 821 ASN A O 1 ATOM 6381 C CB . ASN A 1 821 ? -25.540 50.961 65.251 1.00 80.83 ? 821 ASN A CB 1 ATOM 6382 C CG . ASN A 1 821 ? -24.794 51.744 64.195 1.00 102.25 ? 821 ASN A CG 1 ATOM 6383 O OD1 . ASN A 1 821 ? -23.755 51.312 63.700 1.00 123.28 ? 821 ASN A OD1 1 ATOM 6384 N ND2 . ASN A 1 821 ? -25.324 52.910 63.848 1.00 147.03 ? 821 ASN A ND2 1 ATOM 6385 N N . CYS A 1 822 ? -25.206 48.669 67.427 1.00 72.99 ? 822 CYS A N 1 ATOM 6386 C CA . CYS A 1 822 ? -25.729 48.017 68.623 1.00 69.04 ? 822 CYS A CA 1 ATOM 6387 C C . CYS A 1 822 ? -25.343 48.756 69.899 1.00 94.93 ? 822 CYS A C 1 ATOM 6388 O O . CYS A 1 822 ? -24.321 49.440 69.953 1.00 115.87 ? 822 CYS A O 1 ATOM 6389 C CB . CYS A 1 822 ? -25.248 46.570 68.692 1.00 65.62 ? 822 CYS A CB 1 ATOM 6390 S SG . CYS A 1 822 ? -25.912 45.526 67.386 1.00 107.06 ? 822 CYS A SG 1 ATOM 6391 N N . THR A 1 823 ? -26.173 48.610 70.925 1.00 66.31 ? 823 THR A N 1 ATOM 6392 C CA . THR A 1 823 ? -25.942 49.281 72.195 1.00 80.70 ? 823 THR A CA 1 ATOM 6393 C C . THR A 1 823 ? -26.318 48.372 73.358 1.00 82.23 ? 823 THR A C 1 ATOM 6394 O O . THR A 1 823 ? -27.323 47.664 73.302 1.00 79.49 ? 823 THR A O 1 ATOM 6395 C CB . THR A 1 823 ? -26.741 50.590 72.285 1.00 81.93 ? 823 THR A CB 1 ATOM 6396 O OG1 . THR A 1 823 ? -26.517 51.369 71.104 1.00 83.31 ? 823 THR A OG1 1 ATOM 6397 C CG2 . THR A 1 823 ? -26.318 51.392 73.504 1.00 81.83 ? 823 THR A CG2 1 ATOM 6398 N N . SER A 1 824 ? -25.500 48.386 74.404 1.00 71.99 ? 824 SER A N 1 ATOM 6399 C CA . SER A 1 824 ? -25.754 47.570 75.582 1.00 71.83 ? 824 SER A CA 1 ATOM 6400 C C . SER A 1 824 ? -26.320 48.424 76.708 1.00 76.96 ? 824 SER A C 1 ATOM 6401 O O . SER A 1 824 ? -25.801 49.501 76.998 1.00 108.36 ? 824 SER A O 1 ATOM 6402 C CB . SER A 1 824 ? -24.471 46.871 76.034 1.00 86.95 ? 824 SER A CB 1 ATOM 6403 O OG . SER A 1 824 ? -24.688 46.113 77.211 1.00 87.29 ? 824 SER A OG 1 ATOM 6404 N N . ASP A 1 825 ? -27.386 47.943 77.340 1.00 76.92 ? 825 ASP A N 1 ATOM 6405 C CA . ASP A 1 825 ? -28.005 48.667 78.447 1.00 83.60 ? 825 ASP A CA 1 ATOM 6406 C C . ASP A 1 825 ? -27.100 48.634 79.673 1.00 86.34 ? 825 ASP A C 1 ATOM 6407 O O . ASP A 1 825 ? -27.238 49.446 80.584 1.00 92.43 ? 825 ASP A O 1 ATOM 6408 C CB . ASP A 1 825 ? -29.383 48.083 78.778 1.00 82.34 ? 825 ASP A CB 1 ATOM 6409 C CG . ASP A 1 825 ? -29.317 46.631 79.217 1.00 113.99 ? 825 ASP A CG 1 ATOM 6410 O OD1 . ASP A 1 825 ? -28.275 45.980 78.992 1.00 112.66 ? 825 ASP A OD1 1 ATOM 6411 O OD2 . ASP A 1 825 ? -30.313 46.135 79.784 1.00 98.94 ? 825 ASP A OD2 1 ATOM 6412 N N . MET A 1 826 ? -26.174 47.680 79.686 1.00 112.52 ? 826 MET A N 1 ATOM 6413 C CA . MET A 1 826 ? -25.170 47.589 80.737 1.00 95.60 ? 826 MET A CA 1 ATOM 6414 C C . MET A 1 826 ? -23.777 47.656 80.131 1.00 85.67 ? 826 MET A C 1 ATOM 6415 O O . MET A 1 826 ? -23.544 47.117 79.049 1.00 80.86 ? 826 MET A O 1 ATOM 6416 C CB . MET A 1 826 ? -25.329 46.295 81.535 1.00 103.30 ? 826 MET A CB 1 ATOM 6417 C CG . MET A 1 826 ? -26.733 46.040 82.046 1.00 107.92 ? 826 MET A CG 1 ATOM 6418 S SD . MET A 1 826 ? -26.772 44.701 83.248 1.00 91.41 ? 826 MET A SD 1 ATOM 6419 C CE . MET A 1 826 ? -25.857 45.443 84.601 1.00 143.43 ? 826 MET A CE 1 ATOM 6420 N N . GLU A 1 827 ? -22.855 48.312 80.830 1.00 96.48 ? 827 GLU A N 1 ATOM 6421 C CA . GLU A 1 827 ? -21.479 48.435 80.361 1.00 98.13 ? 827 GLU A CA 1 ATOM 6422 C C . GLU A 1 827 ? -20.860 47.065 80.113 1.00 103.84 ? 827 GLU A C 1 ATOM 6423 O O . GLU A 1 827 ? -20.814 46.228 81.014 1.00 108.45 ? 827 GLU A O 1 ATOM 6424 C CB . GLU A 1 827 ? -20.641 49.209 81.381 1.00 99.29 ? 827 GLU A CB 1 ATOM 6425 C CG . GLU A 1 827 ? -19.154 49.255 81.071 1.00 114.74 ? 827 GLU A CG 1 ATOM 6426 C CD . GLU A 1 827 ? -18.351 49.923 82.174 1.00 147.10 ? 827 GLU A CD 1 ATOM 6427 O OE1 . GLU A 1 827 ? -17.720 50.967 81.906 1.00 150.95 ? 827 GLU A OE1 1 ATOM 6428 O OE2 . GLU A 1 827 ? -18.348 49.403 83.310 1.00 153.19 ? 827 GLU A OE2 1 ATOM 6429 N N . ILE A 1 828 ? -20.376 46.841 78.894 1.00 103.66 ? 828 ILE A N 1 ATOM 6430 C CA . ILE A 1 828 ? -19.756 45.564 78.560 1.00 100.25 ? 828 ILE A CA 1 ATOM 6431 C C . ILE A 1 828 ? -18.324 45.540 79.069 1.00 100.11 ? 828 ILE A C 1 ATOM 6432 O O . ILE A 1 828 ? -17.605 46.538 78.978 1.00 98.43 ? 828 ILE A O 1 ATOM 6433 C CB . ILE A 1 828 ? -19.771 45.277 77.041 1.00 84.92 ? 828 ILE A CB 1 ATOM 6434 C CG1 . ILE A 1 828 ? -19.173 46.452 76.262 1.00 122.05 ? 828 ILE A CG1 1 ATOM 6435 C CG2 . ILE A 1 828 ? -21.187 44.978 76.570 1.00 74.64 ? 828 ILE A CG2 1 ATOM 6436 C CD1 . ILE A 1 828 ? -18.724 46.094 74.860 1.00 113.51 ? 828 ILE A CD1 1 ATOM 6437 N N . ASN A 1 829 ? -17.925 44.394 79.610 1.00 101.48 ? 829 ASN A N 1 ATOM 6438 C CA . ASN A 1 829 ? -16.611 44.234 80.218 1.00 101.20 ? 829 ASN A CA 1 ATOM 6439 C C . ASN A 1 829 ? -16.316 45.328 81.242 1.00 100.87 ? 829 ASN A C 1 ATOM 6440 O O . ASN A 1 829 ? -15.413 46.139 81.045 1.00 105.60 ? 829 ASN A O 1 ATOM 6441 C CB . ASN A 1 829 ? -15.528 44.217 79.136 1.00 106.18 ? 829 ASN A CB 1 ATOM 6442 C CG . ASN A 1 829 ? -14.177 43.798 79.670 1.00 115.83 ? 829 ASN A CG 1 ATOM 6443 O OD1 . ASN A 1 829 ? -14.082 43.151 80.713 1.00 117.88 ? 829 ASN A OD1 1 ATOM 6444 N ND2 . ASN A 1 829 ? -13.121 44.167 78.956 1.00 127.14 ? 829 ASN A ND2 1 ATOM 6445 N N . PRO A 1 830 ? -17.093 45.364 82.336 1.00 104.64 ? 830 PRO A N 1 ATOM 6446 C CA . PRO A 1 830 ? -16.903 46.395 83.361 1.00 109.28 ? 830 PRO A CA 1 ATOM 6447 C C . PRO A 1 830 ? -15.616 46.198 84.156 1.00 113.87 ? 830 PRO A C 1 ATOM 6448 O O . PRO A 1 830 ? -15.138 47.135 84.795 1.00 117.50 ? 830 PRO A O 1 ATOM 6449 C CB . PRO A 1 830 ? -18.127 46.220 84.258 1.00 114.04 ? 830 PRO A CB 1 ATOM 6450 C CG . PRO A 1 830 ? -18.452 44.772 84.143 1.00 113.64 ? 830 PRO A CG 1 ATOM 6451 C CD . PRO A 1 830 ? -18.141 44.399 82.718 1.00 102.04 ? 830 PRO A CD 1 ATOM 6452 N N . LEU A 1 831 ? -15.068 44.987 84.116 1.00 120.56 ? 831 LEU A N 1 ATOM 6453 C CA . LEU A 1 831 ? -13.868 44.660 84.878 1.00 125.27 ? 831 LEU A CA 1 ATOM 6454 C C . LEU A 1 831 ? -12.601 44.850 84.050 1.00 128.88 ? 831 LEU A C 1 ATOM 6455 O O . LEU A 1 831 ? -11.495 44.590 84.527 1.00 124.33 ? 831 LEU A O 1 ATOM 6456 C CB . LEU A 1 831 ? -13.946 43.223 85.395 1.00 120.59 ? 831 LEU A CB 1 ATOM 6457 C CG . LEU A 1 831 ? -15.060 42.938 86.404 1.00 119.60 ? 831 LEU A CG 1 ATOM 6458 C CD1 . LEU A 1 831 ? -15.269 41.444 86.562 1.00 114.89 ? 831 LEU A CD1 1 ATOM 6459 C CD2 . LEU A 1 831 ? -14.734 43.575 87.744 1.00 135.97 ? 831 LEU A CD2 1 ATOM 6460 N N . ARG A 1 832 ? -12.779 45.299 82.810 1.00 139.15 ? 832 ARG A N 1 ATOM 6461 C CA . ARG A 1 832 ? -11.675 45.591 81.895 1.00 137.18 ? 832 ARG A CA 1 ATOM 6462 C C . ARG A 1 832 ? -10.740 44.399 81.699 1.00 135.71 ? 832 ARG A C 1 ATOM 6463 O O . ARG A 1 832 ? -9.529 44.566 81.547 1.00 153.43 ? 832 ARG A O 1 ATOM 6464 C CB . ARG A 1 832 ? -10.878 46.803 82.386 1.00 138.55 ? 832 ARG A CB 1 ATOM 6465 C CG . ARG A 1 832 ? -11.724 48.045 82.614 1.00 144.18 ? 832 ARG A CG 1 ATOM 6466 C CD . ARG A 1 832 ? -12.668 48.288 81.446 1.00 151.42 ? 832 ARG A CD 1 ATOM 6467 N NE . ARG A 1 832 ? -13.567 49.413 81.687 1.00 156.67 ? 832 ARG A NE 1 ATOM 6468 C CZ . ARG A 1 832 ? -14.673 49.649 80.987 1.00 145.07 ? 832 ARG A CZ 1 ATOM 6469 N NH1 . ARG A 1 832 ? -15.025 48.832 80.004 1.00 135.62 ? 832 ARG A NH1 1 ATOM 6470 N NH2 . ARG A 1 832 ? -15.430 50.698 81.275 1.00 149.58 ? 832 ARG A NH2 1 ATOM 6471 N N . ILE A 1 833 ? -11.309 43.199 81.704 1.00 122.33 ? 833 ILE A N 1 ATOM 6472 C CA . ILE A 1 833 ? -10.544 41.990 81.434 1.00 120.53 ? 833 ILE A CA 1 ATOM 6473 C C . ILE A 1 833 ? -10.169 41.935 79.962 1.00 127.96 ? 833 ILE A C 1 ATOM 6474 O O . ILE A 1 833 ? -11.036 42.012 79.094 1.00 147.85 ? 833 ILE A O 1 ATOM 6475 C CB . ILE A 1 833 ? -11.336 40.728 81.802 1.00 115.47 ? 833 ILE A CB 1 ATOM 6476 C CG1 . ILE A 1 833 ? -11.831 40.816 83.245 1.00 120.84 ? 833 ILE A CG1 1 ATOM 6477 C CG2 . ILE A 1 833 ? -10.485 39.489 81.596 1.00 116.82 ? 833 ILE A CG2 1 ATOM 6478 C CD1 . ILE A 1 833 ? -12.800 39.724 83.620 1.00 118.05 ? 833 ILE A CD1 1 ATOM 6479 N N . LYS A 1 834 ? -8.879 41.799 79.678 1.00 135.69 ? 834 LYS A N 1 ATOM 6480 C CA . LYS A 1 834 ? -8.418 41.790 78.295 1.00 154.79 ? 834 LYS A CA 1 ATOM 6481 C C . LYS A 1 834 ? -7.704 40.493 77.939 1.00 159.82 ? 834 LYS A C 1 ATOM 6482 O O . LYS A 1 834 ? -7.148 39.818 78.806 1.00 159.15 ? 834 LYS A O 1 ATOM 6483 C CB . LYS A 1 834 ? -7.500 42.986 78.033 1.00 169.23 ? 834 LYS A CB 1 ATOM 6484 C CG . LYS A 1 834 ? -8.220 44.327 78.041 1.00 164.95 ? 834 LYS A CG 1 ATOM 6485 C CD . LYS A 1 834 ? -9.331 44.359 77.003 1.00 142.83 ? 834 LYS A CD 1 ATOM 6486 C CE . LYS A 1 834 ? -10.088 45.675 77.039 1.00 143.61 ? 834 LYS A CE 1 ATOM 6487 N NZ . LYS A 1 834 ? -11.201 45.702 76.049 1.00 136.30 ? 834 LYS A NZ 1 ATOM 6488 N N . ILE A 1 835 ? -7.730 40.152 76.654 1.00 161.87 ? 835 ILE A N 1 ATOM 6489 C CA . ILE A 1 835 ? -7.097 38.936 76.157 1.00 157.00 ? 835 ILE A CA 1 ATOM 6490 C C . ILE A 1 835 ? -5.582 38.983 76.323 1.00 166.60 ? 835 ILE A C 1 ATOM 6491 O O . ILE A 1 835 ? -5.010 38.223 77.104 1.00 165.70 ? 835 ILE A O 1 ATOM 6492 C CB . ILE A 1 835 ? -7.433 38.697 74.673 1.00 147.07 ? 835 ILE A CB 1 ATOM 6493 C CG1 . ILE A 1 835 ? -6.733 37.436 74.164 1.00 125.32 ? 835 ILE A CG1 1 ATOM 6494 C CG2 . ILE A 1 835 ? -7.040 39.906 73.836 1.00 150.48 ? 835 ILE A CG2 1 ATOM 6495 C CD1 . ILE A 1 835 ? -7.005 37.140 72.707 1.00 121.84 ? 835 ILE A CD1 1 ATOM 6496 N N . HIS A 1 870 ? -32.992 24.212 85.834 1.00 132.68 ? 870 HIS A N 1 ATOM 6497 C CA . HIS A 1 870 ? -32.203 23.523 84.820 1.00 127.58 ? 870 HIS A CA 1 ATOM 6498 C C . HIS A 1 870 ? -31.841 24.470 83.677 1.00 116.95 ? 870 HIS A C 1 ATOM 6499 O O . HIS A 1 870 ? -30.668 24.632 83.345 1.00 112.10 ? 870 HIS A O 1 ATOM 6500 C CB . HIS A 1 870 ? -32.965 22.307 84.284 1.00 142.98 ? 870 HIS A CB 1 ATOM 6501 C CG . HIS A 1 870 ? -32.100 21.321 83.560 1.00 137.21 ? 870 HIS A CG 1 ATOM 6502 N ND1 . HIS A 1 870 ? -31.749 21.469 82.236 1.00 122.04 ? 870 HIS A ND1 1 ATOM 6503 C CD2 . HIS A 1 870 ? -31.521 20.171 83.977 1.00 138.01 ? 870 HIS A CD2 1 ATOM 6504 C CE1 . HIS A 1 870 ? -30.987 20.454 81.868 1.00 112.12 ? 870 HIS A CE1 1 ATOM 6505 N NE2 . HIS A 1 870 ? -30.834 19.652 82.906 1.00 130.24 ? 870 HIS A NE2 1 ATOM 6506 N N . THR A 1 871 ? -32.851 25.098 83.083 1.00 124.38 ? 871 THR A N 1 ATOM 6507 C CA . THR A 1 871 ? -32.634 26.035 81.983 1.00 114.56 ? 871 THR A CA 1 ATOM 6508 C C . THR A 1 871 ? -32.642 27.482 82.465 1.00 105.49 ? 871 THR A C 1 ATOM 6509 O O . THR A 1 871 ? -33.574 27.907 83.146 1.00 101.83 ? 871 THR A O 1 ATOM 6510 C CB . THR A 1 871 ? -33.705 25.877 80.888 1.00 111.47 ? 871 THR A CB 1 ATOM 6511 O OG1 . THR A 1 871 ? -33.684 24.536 80.385 1.00 135.77 ? 871 THR A OG1 1 ATOM 6512 C CG2 . THR A 1 871 ? -33.448 26.851 79.749 1.00 93.48 ? 871 THR A CG2 1 ATOM 6513 N N . LEU A 1 872 ? -31.602 28.234 82.116 1.00 102.07 ? 872 LEU A N 1 ATOM 6514 C CA . LEU A 1 872 ? -31.524 29.642 82.495 1.00 93.13 ? 872 LEU A CA 1 ATOM 6515 C C . LEU A 1 872 ? -31.586 30.561 81.282 1.00 99.95 ? 872 LEU A C 1 ATOM 6516 O O . LEU A 1 872 ? -30.624 30.666 80.522 1.00 100.82 ? 872 LEU A O 1 ATOM 6517 C CB . LEU A 1 872 ? -30.242 29.914 83.280 1.00 92.27 ? 872 LEU A CB 1 ATOM 6518 C CG . LEU A 1 872 ? -30.095 29.140 84.589 1.00 101.85 ? 872 LEU A CG 1 ATOM 6519 C CD1 . LEU A 1 872 ? -28.755 29.436 85.245 1.00 98.64 ? 872 LEU A CD1 1 ATOM 6520 C CD2 . LEU A 1 872 ? -31.243 29.473 85.527 1.00 111.09 ? 872 LEU A CD2 1 ATOM 6521 N N . GLY A 1 873 ? -32.713 31.246 81.122 1.00 109.98 ? 873 GLY A N 1 ATOM 6522 C CA . GLY A 1 873 ? -32.875 32.211 80.053 1.00 114.49 ? 873 GLY A CA 1 ATOM 6523 C C . GLY A 1 873 ? -32.774 33.609 80.622 1.00 117.93 ? 873 GLY A C 1 ATOM 6524 O O . GLY A 1 873 ? -32.433 33.773 81.791 1.00 106.82 ? 873 GLY A O 1 ATOM 6525 N N . CYS A 1 874 ? -33.065 34.618 79.807 1.00 123.65 ? 874 CYS A N 1 ATOM 6526 C CA . CYS A 1 874 ? -33.086 35.988 80.304 1.00 100.36 ? 874 CYS A CA 1 ATOM 6527 C C . CYS A 1 874 ? -34.293 36.156 81.220 1.00 105.53 ? 874 CYS A C 1 ATOM 6528 O O . CYS A 1 874 ? -34.312 37.025 82.092 1.00 129.01 ? 874 CYS A O 1 ATOM 6529 C CB . CYS A 1 874 ? -33.125 36.994 79.156 1.00 76.89 ? 874 CYS A CB 1 ATOM 6530 S SG . CYS A 1 874 ? -32.599 38.663 79.612 1.00 145.43 ? 874 CYS A SG 1 ATOM 6531 N N . GLY A 1 875 ? -35.302 35.316 81.010 1.00 101.38 ? 875 GLY A N 1 ATOM 6532 C CA . GLY A 1 875 ? -36.392 35.187 81.956 1.00 109.90 ? 875 GLY A CA 1 ATOM 6533 C C . GLY A 1 875 ? -35.862 34.447 83.168 1.00 132.09 ? 875 GLY A C 1 ATOM 6534 O O . GLY A 1 875 ? -34.917 33.668 83.042 1.00 141.92 ? 875 GLY A O 1 ATOM 6535 N N . VAL A 1 876 ? -36.449 34.725 84.332 1.00 129.87 ? 876 VAL A N 1 ATOM 6536 C CA . VAL A 1 876 ? -36.050 34.168 85.637 1.00 147.06 ? 876 VAL A CA 1 ATOM 6537 C C . VAL A 1 876 ? -34.528 34.205 85.867 1.00 131.59 ? 876 VAL A C 1 ATOM 6538 O O . VAL A 1 876 ? -33.961 33.344 86.542 1.00 109.11 ? 876 VAL A O 1 ATOM 6539 C CB . VAL A 1 876 ? -36.603 32.712 85.851 1.00 139.46 ? 876 VAL A CB 1 ATOM 6540 C CG1 . VAL A 1 876 ? -38.111 32.681 85.626 1.00 151.42 ? 876 VAL A CG1 1 ATOM 6541 C CG2 . VAL A 1 876 ? -35.904 31.659 84.982 1.00 110.68 ? 876 VAL A CG2 1 ATOM 6542 N N . ALA A 1 877 ? -33.885 35.236 85.323 1.00 138.86 ? 877 ALA A N 1 ATOM 6543 C CA . ALA A 1 877 ? -32.468 35.499 85.558 1.00 114.10 ? 877 ALA A CA 1 ATOM 6544 C C . ALA A 1 877 ? -32.157 36.963 85.255 1.00 119.28 ? 877 ALA A C 1 ATOM 6545 O O . ALA A 1 877 ? -32.920 37.630 84.556 1.00 132.58 ? 877 ALA A O 1 ATOM 6546 C CB . ALA A 1 877 ? -31.603 34.582 84.714 1.00 98.11 ? 877 ALA A CB 1 ATOM 6547 N N . GLN A 1 878 ? -31.041 37.461 85.780 1.00 118.57 ? 878 GLN A N 1 ATOM 6548 C CA . GLN A 1 878 ? -30.634 38.842 85.535 1.00 111.64 ? 878 GLN A CA 1 ATOM 6549 C C . GLN A 1 878 ? -30.346 39.041 84.054 1.00 97.89 ? 878 GLN A C 1 ATOM 6550 O O . GLN A 1 878 ? -29.605 38.268 83.447 1.00 84.51 ? 878 GLN A O 1 ATOM 6551 C CB . GLN A 1 878 ? -29.407 39.210 86.372 1.00 123.28 ? 878 GLN A CB 1 ATOM 6552 C CG . GLN A 1 878 ? -29.060 40.693 86.367 1.00 111.71 ? 878 GLN A CG 1 ATOM 6553 C CD . GLN A 1 878 ? -29.963 41.508 87.274 1.00 141.71 ? 878 GLN A CD 1 ATOM 6554 O OE1 . GLN A 1 878 ? -30.815 40.963 87.976 1.00 157.72 ? 878 GLN A OE1 1 ATOM 6555 N NE2 . GLN A 1 878 ? -29.775 42.823 87.267 1.00 150.38 ? 878 GLN A NE2 1 ATOM 6556 N N . CYS A 1 879 ? -30.936 40.079 83.473 1.00 114.76 ? 879 CYS A N 1 ATOM 6557 C CA . CYS A 1 879 ? -30.882 40.262 82.029 1.00 109.26 ? 879 CYS A CA 1 ATOM 6558 C C . CYS A 1 879 ? -29.968 41.401 81.593 1.00 88.50 ? 879 CYS A C 1 ATOM 6559 O O . CYS A 1 879 ? -29.989 42.491 82.164 1.00 83.79 ? 879 CYS A O 1 ATOM 6560 C CB . CYS A 1 879 ? -32.290 40.502 81.479 1.00 100.96 ? 879 CYS A CB 1 ATOM 6561 S SG . CYS A 1 879 ? -32.363 40.679 79.682 1.00 138.45 ? 879 CYS A SG 1 ATOM 6562 N N . LEU A 1 880 ? -29.161 41.128 80.574 1.00 74.22 ? 880 LEU A N 1 ATOM 6563 C CA . LEU A 1 880 ? -28.395 42.164 79.902 1.00 72.09 ? 880 LEU A CA 1 ATOM 6564 C C . LEU A 1 880 ? -28.929 42.302 78.488 1.00 72.83 ? 880 LEU A C 1 ATOM 6565 O O . LEU A 1 880 ? -28.808 41.386 77.679 1.00 63.63 ? 880 LEU A O 1 ATOM 6566 C CB . LEU A 1 880 ? -26.901 41.834 79.890 1.00 84.15 ? 880 LEU A CB 1 ATOM 6567 C CG . LEU A 1 880 ? -25.973 42.895 79.293 1.00 79.31 ? 880 LEU A CG 1 ATOM 6568 C CD1 . LEU A 1 880 ? -24.708 43.021 80.126 1.00 78.00 ? 880 LEU A CD1 1 ATOM 6569 C CD2 . LEU A 1 880 ? -25.627 42.565 77.848 1.00 65.02 ? 880 LEU A CD2 1 ATOM 6570 N N . LYS A 1 881 ? -29.532 43.448 78.197 1.00 85.40 ? 881 LYS A N 1 ATOM 6571 C CA . LYS A 1 881 ? -30.153 43.670 76.901 1.00 71.30 ? 881 LYS A CA 1 ATOM 6572 C C . LYS A 1 881 ? -29.198 44.335 75.918 1.00 71.64 ? 881 LYS A C 1 ATOM 6573 O O . LYS A 1 881 ? -28.462 45.256 76.271 1.00 93.38 ? 881 LYS A O 1 ATOM 6574 C CB . LYS A 1 881 ? -31.414 44.520 77.057 1.00 91.09 ? 881 LYS A CB 1 ATOM 6575 C CG . LYS A 1 881 ? -32.682 43.851 76.555 1.00 97.78 ? 881 LYS A CG 1 ATOM 6576 C CD . LYS A 1 881 ? -33.899 44.720 76.820 1.00 73.53 ? 881 LYS A CD 1 ATOM 6577 C CE . LYS A 1 881 ? -33.984 45.091 78.288 1.00 87.87 ? 881 LYS A CE 1 ATOM 6578 N NZ . LYS A 1 881 ? -33.926 43.889 79.166 1.00 89.42 ? 881 LYS A NZ 1 ATOM 6579 N N . ILE A 1 882 ? -29.210 43.853 74.682 1.00 70.92 ? 882 ILE A N 1 ATOM 6580 C CA . ILE A 1 882 ? -28.449 44.478 73.611 1.00 70.87 ? 882 ILE A CA 1 ATOM 6581 C C . ILE A 1 882 ? -29.384 44.795 72.454 1.00 69.61 ? 882 ILE A C 1 ATOM 6582 O O . ILE A 1 882 ? -29.914 43.893 71.808 1.00 85.71 ? 882 ILE A O 1 ATOM 6583 C CB . ILE A 1 882 ? -27.302 43.577 73.121 1.00 73.20 ? 882 ILE A CB 1 ATOM 6584 C CG1 . ILE A 1 882 ? -26.343 43.270 74.271 1.00 67.23 ? 882 ILE A CG1 1 ATOM 6585 C CG2 . ILE A 1 882 ? -26.557 44.238 71.973 1.00 73.53 ? 882 ILE A CG2 1 ATOM 6586 C CD1 . ILE A 1 882 ? -25.129 42.476 73.852 1.00 67.29 ? 882 ILE A CD1 1 ATOM 6587 N N . VAL A 1 883 ? -29.581 46.081 72.195 1.00 69.41 ? 883 VAL A N 1 ATOM 6588 C CA . VAL A 1 883 ? -30.521 46.514 71.172 1.00 85.41 ? 883 VAL A CA 1 ATOM 6589 C C . VAL A 1 883 ? -29.762 46.994 69.936 1.00 72.61 ? 883 VAL A C 1 ATOM 6590 O O . VAL A 1 883 ? -28.710 47.623 70.049 1.00 82.30 ? 883 VAL A O 1 ATOM 6591 C CB . VAL A 1 883 ? -31.455 47.626 71.714 1.00 64.47 ? 883 VAL A CB 1 ATOM 6592 C CG1 . VAL A 1 883 ? -30.640 48.757 72.323 1.00 68.14 ? 883 VAL A CG1 1 ATOM 6593 C CG2 . VAL A 1 883 ? -32.394 48.138 70.630 1.00 64.56 ? 883 VAL A CG2 1 ATOM 6594 N N . CYS A 1 884 ? -30.288 46.676 68.758 1.00 64.13 ? 884 CYS A N 1 ATOM 6595 C CA . CYS A 1 884 ? -29.618 47.014 67.509 1.00 63.86 ? 884 CYS A CA 1 ATOM 6596 C C . CYS A 1 884 ? -30.548 47.668 66.494 1.00 66.76 ? 884 CYS A C 1 ATOM 6597 O O . CYS A 1 884 ? -31.710 47.281 66.362 1.00 60.97 ? 884 CYS A O 1 ATOM 6598 C CB . CYS A 1 884 ? -28.998 45.761 66.887 1.00 67.22 ? 884 CYS A CB 1 ATOM 6599 S SG . CYS A 1 884 ? -27.777 44.930 67.919 1.00 100.51 ? 884 CYS A SG 1 ATOM 6600 N N . GLN A 1 885 ? -30.024 48.657 65.775 1.00 63.06 ? 885 GLN A N 1 ATOM 6601 C CA . GLN A 1 885 ? -30.731 49.252 64.645 1.00 60.75 ? 885 GLN A CA 1 ATOM 6602 C C . GLN A 1 885 ? -30.126 48.743 63.334 1.00 72.49 ? 885 GLN A C 1 ATOM 6603 O O . GLN A 1 885 ? -28.910 48.783 63.147 1.00 72.09 ? 885 GLN A O 1 ATOM 6604 C CB . GLN A 1 885 ? -30.670 50.779 64.708 1.00 66.27 ? 885 GLN A CB 1 ATOM 6605 C CG . GLN A 1 885 ? -30.973 51.362 66.082 1.00 95.67 ? 885 GLN A CG 1 ATOM 6606 C CD . GLN A 1 885 ? -29.723 51.830 66.812 1.00 123.55 ? 885 GLN A CD 1 ATOM 6607 O OE1 . GLN A 1 885 ? -28.932 52.607 66.275 1.00 132.50 ? 885 GLN A OE1 1 ATOM 6608 N NE2 . GLN A 1 885 ? -29.541 51.358 68.041 1.00 101.75 ? 885 GLN A NE2 1 ATOM 6609 N N . VAL A 1 886 ? -30.973 48.259 62.431 1.00 77.77 ? 886 VAL A N 1 ATOM 6610 C CA . VAL A 1 886 ? -30.494 47.682 61.178 1.00 57.95 ? 886 VAL A CA 1 ATOM 6611 C C . VAL A 1 886 ? -30.794 48.579 59.978 1.00 67.24 ? 886 VAL A C 1 ATOM 6612 O O . VAL A 1 886 ? -31.892 49.119 59.850 1.00 63.51 ? 886 VAL A O 1 ATOM 6613 C CB . VAL A 1 886 ? -31.115 46.300 60.932 1.00 55.71 ? 886 VAL A CB 1 ATOM 6614 C CG1 . VAL A 1 886 ? -30.425 45.606 59.767 1.00 55.98 ? 886 VAL A CG1 1 ATOM 6615 C CG2 . VAL A 1 886 ? -31.014 45.453 62.184 1.00 69.74 ? 886 VAL A CG2 1 ATOM 6616 N N . GLY A 1 887 ? -29.812 48.719 59.092 1.00 66.48 ? 887 GLY A N 1 ATOM 6617 C CA . GLY A 1 887 ? -29.954 49.548 57.910 1.00 66.97 ? 887 GLY A CA 1 ATOM 6618 C C . GLY A 1 887 ? -30.598 48.795 56.764 1.00 66.49 ? 887 GLY A C 1 ATOM 6619 O O . GLY A 1 887 ? -31.409 47.899 56.986 1.00 79.51 ? 887 GLY A O 1 ATOM 6620 N N . ARG A 1 888 ? -30.252 49.166 55.536 1.00 70.88 ? 888 ARG A N 1 ATOM 6621 C CA . ARG A 1 888 ? -30.845 48.535 54.364 1.00 75.12 ? 888 ARG A CA 1 ATOM 6622 C C . ARG A 1 888 ? -30.252 47.149 54.117 1.00 83.41 ? 888 ARG A C 1 ATOM 6623 O O . ARG A 1 888 ? -29.040 47.002 53.943 1.00 77.93 ? 888 ARG A O 1 ATOM 6624 C CB . ARG A 1 888 ? -30.654 49.411 53.124 1.00 76.96 ? 888 ARG A CB 1 ATOM 6625 C CG . ARG A 1 888 ? -31.461 48.958 51.913 1.00 78.13 ? 888 ARG A CG 1 ATOM 6626 C CD . ARG A 1 888 ? -30.970 49.624 50.638 1.00 92.30 ? 888 ARG A CD 1 ATOM 6627 N NE . ARG A 1 888 ? -31.746 49.224 49.467 1.00 95.06 ? 888 ARG A NE 1 ATOM 6628 C CZ . ARG A 1 888 ? -32.781 49.908 48.987 1.00 101.45 ? 888 ARG A CZ 1 ATOM 6629 N NH1 . ARG A 1 888 ? -33.171 51.030 49.577 1.00 104.62 ? 888 ARG A NH1 1 ATOM 6630 N NH2 . ARG A 1 888 ? -33.428 49.471 47.915 1.00 97.80 ? 888 ARG A NH2 1 ATOM 6631 N N . LEU A 1 889 ? -31.119 46.140 54.100 1.00 69.88 ? 889 LEU A N 1 ATOM 6632 C CA . LEU A 1 889 ? -30.722 44.780 53.753 1.00 75.32 ? 889 LEU A CA 1 ATOM 6633 C C . LEU A 1 889 ? -31.444 44.306 52.497 1.00 88.97 ? 889 LEU A C 1 ATOM 6634 O O . LEU A 1 889 ? -32.667 44.175 52.485 1.00 88.51 ? 889 LEU A O 1 ATOM 6635 C CB . LEU A 1 889 ? -31.004 43.812 54.905 1.00 63.56 ? 889 LEU A CB 1 ATOM 6636 C CG . LEU A 1 889 ? -30.039 43.810 56.090 1.00 64.90 ? 889 LEU A CG 1 ATOM 6637 C CD1 . LEU A 1 889 ? -30.384 42.683 57.050 1.00 74.25 ? 889 LEU A CD1 1 ATOM 6638 C CD2 . LEU A 1 889 ? -28.601 43.682 55.617 1.00 72.71 ? 889 LEU A CD2 1 ATOM 6639 N N . ASP A 1 890 ? -30.678 44.057 51.441 1.00 89.85 ? 890 ASP A N 1 ATOM 6640 C CA . ASP A 1 890 ? -31.227 43.523 50.201 1.00 84.27 ? 890 ASP A CA 1 ATOM 6641 C C . ASP A 1 890 ? -31.154 41.997 50.193 1.00 81.14 ? 890 ASP A C 1 ATOM 6642 O O . ASP A 1 890 ? -30.896 41.379 51.226 1.00 79.60 ? 890 ASP A O 1 ATOM 6643 C CB . ASP A 1 890 ? -30.490 44.105 48.996 1.00 95.25 ? 890 ASP A CB 1 ATOM 6644 C CG . ASP A 1 890 ? -30.461 45.619 49.013 1.00 100.60 ? 890 ASP A CG 1 ATOM 6645 O OD1 . ASP A 1 890 ? -31.476 46.242 48.636 1.00 101.17 ? 890 ASP A OD1 1 ATOM 6646 O OD2 . ASP A 1 890 ? -29.422 46.188 49.406 1.00 108.66 ? 890 ASP A OD2 1 ATOM 6647 N N . ARG A 1 891 ? -31.397 41.402 49.029 1.00 79.97 ? 891 ARG A N 1 ATOM 6648 C CA . ARG A 1 891 ? -31.416 39.950 48.878 1.00 88.95 ? 891 ARG A CA 1 ATOM 6649 C C . ARG A 1 891 ? -30.131 39.273 49.355 1.00 115.02 ? 891 ARG A C 1 ATOM 6650 O O . ARG A 1 891 ? -30.123 38.562 50.358 1.00 78.19 ? 891 ARG A O 1 ATOM 6651 C CB . ARG A 1 891 ? -31.670 39.584 47.416 1.00 87.22 ? 891 ARG A CB 1 ATOM 6652 C CG . ARG A 1 891 ? -32.846 40.318 46.790 1.00 117.35 ? 891 ARG A CG 1 ATOM 6653 C CD . ARG A 1 891 ? -33.017 39.975 45.314 1.00 120.26 ? 891 ARG A CD 1 ATOM 6654 N NE . ARG A 1 891 ? -33.534 38.625 45.115 1.00 141.25 ? 891 ARG A NE 1 ATOM 6655 C CZ . ARG A 1 891 ? -32.784 37.574 44.800 1.00 156.53 ? 891 ARG A CZ 1 ATOM 6656 N NH1 . ARG A 1 891 ? -31.475 37.714 44.640 1.00 155.35 ? 891 ARG A NH1 1 ATOM 6657 N NH2 . ARG A 1 891 ? -33.344 36.383 44.641 1.00 162.27 ? 891 ARG A NH2 1 ATOM 6658 N N . GLY A 1 892 ? -29.038 39.501 48.640 1.00 134.18 ? 892 GLY A N 1 ATOM 6659 C CA . GLY A 1 892 ? -27.807 38.781 48.907 1.00 141.54 ? 892 GLY A CA 1 ATOM 6660 C C . GLY A 1 892 ? -27.126 39.089 50.228 1.00 124.85 ? 892 GLY A C 1 ATOM 6661 O O . GLY A 1 892 ? -26.130 38.452 50.571 1.00 128.00 ? 892 GLY A O 1 ATOM 6662 N N . LYS A 1 893 ? -27.657 40.046 50.982 1.00 107.13 ? 893 LYS A N 1 ATOM 6663 C CA . LYS A 1 893 ? -26.947 40.532 52.160 1.00 112.48 ? 893 LYS A CA 1 ATOM 6664 C C . LYS A 1 893 ? -27.662 40.228 53.478 1.00 90.50 ? 893 LYS A C 1 ATOM 6665 O O . LYS A 1 893 ? -28.879 40.054 53.520 1.00 67.60 ? 893 LYS A O 1 ATOM 6666 C CB . LYS A 1 893 ? -26.701 42.040 52.037 1.00 111.31 ? 893 LYS A CB 1 ATOM 6667 C CG . LYS A 1 893 ? -25.650 42.578 53.007 1.00 133.24 ? 893 LYS A CG 1 ATOM 6668 C CD . LYS A 1 893 ? -24.365 41.754 52.941 1.00 139.42 ? 893 LYS A CD 1 ATOM 6669 C CE . LYS A 1 893 ? -23.497 41.953 54.178 1.00 118.74 ? 893 LYS A CE 1 ATOM 6670 N NZ . LYS A 1 893 ? -23.114 43.377 54.385 1.00 129.04 ? 893 LYS A NZ 1 ATOM 6671 N N . SER A 1 894 ? -26.874 40.149 54.546 1.00 82.42 ? 894 SER A N 1 ATOM 6672 C CA . SER A 1 894 ? -27.379 39.940 55.895 1.00 64.05 ? 894 SER A CA 1 ATOM 6673 C C . SER A 1 894 ? -26.619 40.817 56.886 1.00 66.76 ? 894 SER A C 1 ATOM 6674 O O . SER A 1 894 ? -25.714 41.560 56.506 1.00 77.10 ? 894 SER A O 1 ATOM 6675 C CB . SER A 1 894 ? -27.254 38.471 56.292 1.00 82.81 ? 894 SER A CB 1 ATOM 6676 O OG . SER A 1 894 ? -25.907 38.037 56.237 1.00 104.03 ? 894 SER A OG 1 ATOM 6677 N N . ALA A 1 895 ? -26.989 40.724 58.158 1.00 80.64 ? 895 ALA A N 1 ATOM 6678 C CA . ALA A 1 895 ? -26.335 41.494 59.212 1.00 65.55 ? 895 ALA A CA 1 ATOM 6679 C C . ALA A 1 895 ? -26.054 40.597 60.409 1.00 79.24 ? 895 ALA A C 1 ATOM 6680 O O . ALA A 1 895 ? -26.923 39.843 60.844 1.00 98.54 ? 895 ALA A O 1 ATOM 6681 C CB . ALA A 1 895 ? -27.190 42.671 59.616 1.00 63.91 ? 895 ALA A CB 1 ATOM 6682 N N . ILE A 1 896 ? -24.839 40.676 60.940 1.00 73.30 ? 896 ILE A N 1 ATOM 6683 C CA . ILE A 1 896 ? -24.393 39.713 61.944 1.00 71.62 ? 896 ILE A CA 1 ATOM 6684 C C . ILE A 1 896 ? -23.883 40.360 63.231 1.00 69.02 ? 896 ILE A C 1 ATOM 6685 O O . ILE A 1 896 ? -23.167 41.361 63.199 1.00 85.72 ? 896 ILE A O 1 ATOM 6686 C CB . ILE A 1 896 ? -23.275 38.813 61.383 1.00 61.42 ? 896 ILE A CB 1 ATOM 6687 C CG1 . ILE A 1 896 ? -23.599 38.378 59.954 1.00 59.93 ? 896 ILE A CG1 1 ATOM 6688 C CG2 . ILE A 1 896 ? -23.063 37.604 62.276 1.00 79.17 ? 896 ILE A CG2 1 ATOM 6689 C CD1 . ILE A 1 896 ? -22.438 37.735 59.244 1.00 67.94 ? 896 ILE A CD1 1 ATOM 6690 N N . LEU A 1 897 ? -24.255 39.771 64.362 1.00 65.75 ? 897 LEU A N 1 ATOM 6691 C CA . LEU A 1 897 ? -23.756 40.205 65.660 1.00 66.81 ? 897 LEU A CA 1 ATOM 6692 C C . LEU A 1 897 ? -22.946 39.090 66.309 1.00 79.44 ? 897 LEU A C 1 ATOM 6693 O O . LEU A 1 897 ? -23.462 38.003 66.569 1.00 79.30 ? 897 LEU A O 1 ATOM 6694 C CB . LEU A 1 897 ? -24.912 40.627 66.570 1.00 53.35 ? 897 LEU A CB 1 ATOM 6695 C CG . LEU A 1 897 ? -24.612 40.839 68.056 1.00 52.55 ? 897 LEU A CG 1 ATOM 6696 C CD1 . LEU A 1 897 ? -23.524 41.881 68.270 1.00 57.56 ? 897 LEU A CD1 1 ATOM 6697 C CD2 . LEU A 1 897 ? -25.880 41.231 68.793 1.00 50.59 ? 897 LEU A CD2 1 ATOM 6698 N N . TYR A 1 898 ? -21.671 39.368 66.559 1.00 76.18 ? 898 TYR A N 1 ATOM 6699 C CA . TYR A 1 898 ? -20.783 38.409 67.200 1.00 64.70 ? 898 TYR A CA 1 ATOM 6700 C C . TYR A 1 898 ? -20.582 38.770 68.665 1.00 65.98 ? 898 TYR A C 1 ATOM 6701 O O . TYR A 1 898 ? -19.998 39.803 68.976 1.00 83.32 ? 898 TYR A O 1 ATOM 6702 C CB . TYR A 1 898 ? -19.427 38.364 66.492 1.00 67.39 ? 898 TYR A CB 1 ATOM 6703 C CG . TYR A 1 898 ? -19.491 38.103 65.003 1.00 78.30 ? 898 TYR A CG 1 ATOM 6704 C CD1 . TYR A 1 898 ? -19.706 39.140 64.104 1.00 87.65 ? 898 TYR A CD1 1 ATOM 6705 C CD2 . TYR A 1 898 ? -19.308 36.824 64.493 1.00 64.79 ? 898 TYR A CD2 1 ATOM 6706 C CE1 . TYR A 1 898 ? -19.754 38.906 62.741 1.00 103.89 ? 898 TYR A CE1 1 ATOM 6707 C CE2 . TYR A 1 898 ? -19.355 36.581 63.134 1.00 65.44 ? 898 TYR A CE2 1 ATOM 6708 C CZ . TYR A 1 898 ? -19.577 37.624 62.262 1.00 91.26 ? 898 TYR A CZ 1 ATOM 6709 O OH . TYR A 1 898 ? -19.623 37.387 60.908 1.00 93.75 ? 898 TYR A OH 1 ATOM 6710 N N . VAL A 1 899 ? -21.060 37.916 69.562 1.00 60.93 ? 899 VAL A N 1 ATOM 6711 C CA . VAL A 1 899 ? -20.897 38.151 70.991 1.00 60.54 ? 899 VAL A CA 1 ATOM 6712 C C . VAL A 1 899 ? -19.867 37.203 71.595 1.00 73.57 ? 899 VAL A C 1 ATOM 6713 O O . VAL A 1 899 ? -20.108 36.000 71.696 1.00 87.82 ? 899 VAL A O 1 ATOM 6714 C CB . VAL A 1 899 ? -22.227 37.981 71.744 1.00 59.67 ? 899 VAL A CB 1 ATOM 6715 C CG1 . VAL A 1 899 ? -22.033 38.249 73.230 1.00 69.20 ? 899 VAL A CG1 1 ATOM 6716 C CG2 . VAL A 1 899 ? -23.286 38.902 71.162 1.00 56.98 ? 899 VAL A CG2 1 ATOM 6717 N N . LYS A 1 900 ? -18.721 37.745 71.999 1.00 68.76 ? 900 LYS A N 1 ATOM 6718 C CA . LYS A 1 900 ? -17.707 36.938 72.668 1.00 72.48 ? 900 LYS A CA 1 ATOM 6719 C C . LYS A 1 900 ? -17.827 37.093 74.179 1.00 75.41 ? 900 LYS A C 1 ATOM 6720 O O . LYS A 1 900 ? -17.660 38.187 74.721 1.00 90.15 ? 900 LYS A O 1 ATOM 6721 C CB . LYS A 1 900 ? -16.297 37.317 72.204 1.00 80.92 ? 900 LYS A CB 1 ATOM 6722 C CG . LYS A 1 900 ? -15.210 36.429 72.804 1.00 91.08 ? 900 LYS A CG 1 ATOM 6723 C CD . LYS A 1 900 ? -13.859 36.617 72.126 1.00 100.88 ? 900 LYS A CD 1 ATOM 6724 C CE . LYS A 1 900 ? -13.245 37.971 72.445 1.00 116.79 ? 900 LYS A CE 1 ATOM 6725 N NZ . LYS A 1 900 ? -11.857 38.080 71.910 1.00 123.05 ? 900 LYS A NZ 1 ATOM 6726 N N . SER A 1 901 ? -18.125 35.989 74.854 1.00 69.19 ? 901 SER A N 1 ATOM 6727 C CA . SER A 1 901 ? -18.306 36.009 76.297 1.00 72.44 ? 901 SER A CA 1 ATOM 6728 C C . SER A 1 901 ? -17.450 34.953 76.972 1.00 76.16 ? 901 SER A C 1 ATOM 6729 O O . SER A 1 901 ? -16.959 34.030 76.325 1.00 81.47 ? 901 SER A O 1 ATOM 6730 C CB . SER A 1 901 ? -19.773 35.786 76.659 1.00 78.30 ? 901 SER A CB 1 ATOM 6731 O OG . SER A 1 901 ? -20.146 34.438 76.427 1.00 70.82 ? 901 SER A OG 1 ATOM 6732 N N . LEU A 1 902 ? -17.278 35.093 78.281 1.00 79.33 ? 902 LEU A N 1 ATOM 6733 C CA . LEU A 1 902 ? -16.545 34.109 79.063 1.00 80.56 ? 902 LEU A CA 1 ATOM 6734 C C . LEU A 1 902 ? -17.454 33.437 80.072 1.00 89.14 ? 902 LEU A C 1 ATOM 6735 O O . LEU A 1 902 ? -18.226 34.100 80.765 1.00 96.85 ? 902 LEU A O 1 ATOM 6736 C CB . LEU A 1 902 ? -15.369 34.756 79.788 1.00 83.32 ? 902 LEU A CB 1 ATOM 6737 C CG . LEU A 1 902 ? -14.275 35.348 78.908 1.00 90.88 ? 902 LEU A CG 1 ATOM 6738 C CD1 . LEU A 1 902 ? -13.214 35.992 79.777 1.00 94.15 ? 902 LEU A CD1 1 ATOM 6739 C CD2 . LEU A 1 902 ? -13.677 34.271 78.027 1.00 99.66 ? 902 LEU A CD2 1 ATOM 6740 N N . LEU A 1 903 ? -17.369 32.115 80.146 1.00 96.60 ? 903 LEU A N 1 ATOM 6741 C CA . LEU A 1 903 ? -18.059 31.387 81.194 1.00 80.62 ? 903 LEU A CA 1 ATOM 6742 C C . LEU A 1 903 ? -17.440 31.779 82.522 1.00 84.91 ? 903 LEU A C 1 ATOM 6743 O O . LEU A 1 903 ? -16.225 31.699 82.688 1.00 92.29 ? 903 LEU A O 1 ATOM 6744 C CB . LEU A 1 903 ? -17.956 29.879 80.978 1.00 79.92 ? 903 LEU A CB 1 ATOM 6745 C CG . LEU A 1 903 ? -18.819 29.017 81.900 1.00 89.96 ? 903 LEU A CG 1 ATOM 6746 C CD1 . LEU A 1 903 ? -20.261 29.011 81.420 1.00 95.38 ? 903 LEU A CD1 1 ATOM 6747 C CD2 . LEU A 1 903 ? -18.271 27.607 81.983 1.00 86.27 ? 903 LEU A CD2 1 ATOM 6748 N N . TRP A 1 904 ? -18.262 32.197 83.474 1.00 86.53 ? 904 TRP A N 1 ATOM 6749 C CA . TRP A 1 904 ? -17.722 32.581 84.766 1.00 90.61 ? 904 TRP A CA 1 ATOM 6750 C C . TRP A 1 904 ? -17.724 31.335 85.626 1.00 97.78 ? 904 TRP A C 1 ATOM 6751 O O . TRP A 1 904 ? -18.771 30.874 86.072 1.00 126.45 ? 904 TRP A O 1 ATOM 6752 C CB . TRP A 1 904 ? -18.552 33.697 85.401 1.00 96.68 ? 904 TRP A CB 1 ATOM 6753 C CG . TRP A 1 904 ? -17.869 34.399 86.531 1.00 99.76 ? 904 TRP A CG 1 ATOM 6754 C CD1 . TRP A 1 904 ? -17.757 33.965 87.818 1.00 107.35 ? 904 TRP A CD1 1 ATOM 6755 C CD2 . TRP A 1 904 ? -17.211 35.670 86.478 1.00 97.20 ? 904 TRP A CD2 1 ATOM 6756 N NE1 . TRP A 1 904 ? -17.067 34.885 88.571 1.00 108.54 ? 904 TRP A NE1 1 ATOM 6757 C CE2 . TRP A 1 904 ? -16.719 35.941 87.771 1.00 107.51 ? 904 TRP A CE2 1 ATOM 6758 C CE3 . TRP A 1 904 ? -16.987 36.605 85.462 1.00 95.60 ? 904 TRP A CE3 1 ATOM 6759 C CZ2 . TRP A 1 904 ? -16.019 37.105 88.075 1.00 111.09 ? 904 TRP A CZ2 1 ATOM 6760 C CZ3 . TRP A 1 904 ? -16.292 37.760 85.766 1.00 109.19 ? 904 TRP A CZ3 1 ATOM 6761 C CH2 . TRP A 1 904 ? -15.816 38.000 87.062 1.00 111.55 ? 904 TRP A CH2 1 ATOM 6762 N N . THR A 1 905 ? -16.535 30.806 85.872 1.00 98.53 ? 905 THR A N 1 ATOM 6763 C CA . THR A 1 905 ? -16.404 29.487 86.465 1.00 102.44 ? 905 THR A CA 1 ATOM 6764 C C . THR A 1 905 ? -16.659 29.556 87.960 1.00 116.89 ? 905 THR A C 1 ATOM 6765 O O . THR A 1 905 ? -17.158 28.604 88.561 1.00 135.66 ? 905 THR A O 1 ATOM 6766 C CB . THR A 1 905 ? -15.009 28.893 86.197 1.00 99.56 ? 905 THR A CB 1 ATOM 6767 O OG1 . THR A 1 905 ? -14.690 29.030 84.807 1.00 93.57 ? 905 THR A OG1 1 ATOM 6768 C CG2 . THR A 1 905 ? -14.964 27.424 86.583 1.00 118.57 ? 905 THR A CG2 1 ATOM 6769 N N . GLU A 1 906 ? -16.326 30.702 88.545 1.00 101.40 ? 906 GLU A N 1 ATOM 6770 C CA . GLU A 1 906 ? -16.454 30.909 89.980 1.00 108.36 ? 906 GLU A CA 1 ATOM 6771 C C . GLU A 1 906 ? -17.888 30.699 90.460 1.00 111.83 ? 906 GLU A C 1 ATOM 6772 O O . GLU A 1 906 ? -18.117 30.193 91.559 1.00 118.98 ? 906 GLU A O 1 ATOM 6773 C CB . GLU A 1 906 ? -15.977 32.314 90.351 1.00 116.38 ? 906 GLU A CB 1 ATOM 6774 C CG . GLU A 1 906 ? -16.078 32.644 91.830 1.00 126.59 ? 906 GLU A CG 1 ATOM 6775 C CD . GLU A 1 906 ? -15.862 34.117 92.110 1.00 138.95 ? 906 GLU A CD 1 ATOM 6776 O OE1 . GLU A 1 906 ? -15.670 34.477 93.290 1.00 148.35 ? 906 GLU A OE1 1 ATOM 6777 O OE2 . GLU A 1 906 ? -15.889 34.915 91.149 1.00 147.43 ? 906 GLU A OE2 1 ATOM 6778 N N . THR A 1 907 ? -18.850 31.076 89.625 1.00 112.20 ? 907 THR A N 1 ATOM 6779 C CA . THR A 1 907 ? -20.255 31.022 90.012 1.00 122.36 ? 907 THR A CA 1 ATOM 6780 C C . THR A 1 907 ? -20.807 29.603 89.949 1.00 106.09 ? 907 THR A C 1 ATOM 6781 O O . THR A 1 907 ? -21.596 29.201 90.803 1.00 117.50 ? 907 THR A O 1 ATOM 6782 C CB . THR A 1 907 ? -21.105 31.944 89.137 1.00 121.15 ? 907 THR A CB 1 ATOM 6783 O OG1 . THR A 1 907 ? -20.899 31.619 87.757 1.00 134.07 ? 907 THR A OG1 1 ATOM 6784 C CG2 . THR A 1 907 ? -20.700 33.385 89.378 1.00 118.35 ? 907 THR A CG2 1 ATOM 6785 N N . PHE A 1 908 ? -20.394 28.842 88.942 1.00 100.59 ? 908 PHE A N 1 ATOM 6786 C CA . PHE A 1 908 ? -20.651 27.410 88.956 1.00 104.70 ? 908 PHE A CA 1 ATOM 6787 C C . PHE A 1 908 ? -19.690 26.796 89.955 1.00 110.30 ? 908 PHE A C 1 ATOM 6788 O O . PHE A 1 908 ? -18.886 27.506 90.560 1.00 136.23 ? 908 PHE A O 1 ATOM 6789 C CB . PHE A 1 908 ? -20.452 26.782 87.576 1.00 94.37 ? 908 PHE A CB 1 ATOM 6790 C CG . PHE A 1 908 ? -21.211 27.469 86.479 1.00 103.29 ? 908 PHE A CG 1 ATOM 6791 C CD1 . PHE A 1 908 ? -22.526 27.130 86.207 1.00 100.93 ? 908 PHE A CD1 1 ATOM 6792 C CD2 . PHE A 1 908 ? -20.606 28.450 85.712 1.00 107.78 ? 908 PHE A CD2 1 ATOM 6793 C CE1 . PHE A 1 908 ? -23.227 27.761 85.193 1.00 87.72 ? 908 PHE A CE1 1 ATOM 6794 C CE2 . PHE A 1 908 ? -21.301 29.087 84.699 1.00 90.37 ? 908 PHE A CE2 1 ATOM 6795 C CZ . PHE A 1 908 ? -22.611 28.741 84.437 1.00 86.95 ? 908 PHE A CZ 1 ATOM 6796 N N . MET A 1 909 ? -19.785 25.486 90.149 1.00 106.41 ? 909 MET A N 1 ATOM 6797 C CA . MET A 1 909 ? -18.693 24.743 90.766 1.00 126.46 ? 909 MET A CA 1 ATOM 6798 C C . MET A 1 909 ? -18.442 25.071 92.249 1.00 144.51 ? 909 MET A C 1 ATOM 6799 O O . MET A 1 909 ? -17.588 24.446 92.880 1.00 156.26 ? 909 MET A O 1 ATOM 6800 C CB . MET A 1 909 ? -17.413 24.988 89.950 1.00 109.65 ? 909 MET A CB 1 ATOM 6801 C CG . MET A 1 909 ? -16.301 23.977 90.124 1.00 121.44 ? 909 MET A CG 1 ATOM 6802 S SD . MET A 1 909 ? -14.906 24.384 89.058 1.00 154.57 ? 909 MET A SD 1 ATOM 6803 C CE . MET A 1 909 ? -13.670 23.240 89.667 1.00 182.02 ? 909 MET A CE 1 ATOM 6804 N N . ASN A 1 910 ? -19.180 26.020 92.822 1.00 133.32 ? 910 ASN A N 1 ATOM 6805 C CA . ASN A 1 910 ? -18.792 26.531 94.137 1.00 145.34 ? 910 ASN A CA 1 ATOM 6806 C C . ASN A 1 910 ? -19.555 25.947 95.333 1.00 163.37 ? 910 ASN A C 1 ATOM 6807 O O . ASN A 1 910 ? -19.028 25.078 96.028 1.00 182.91 ? 910 ASN A O 1 ATOM 6808 C CB . ASN A 1 910 ? -18.924 28.061 94.150 1.00 141.22 ? 910 ASN A CB 1 ATOM 6809 C CG . ASN A 1 910 ? -20.271 28.541 93.637 1.00 142.30 ? 910 ASN A CG 1 ATOM 6810 O OD1 . ASN A 1 910 ? -21.256 27.802 93.655 1.00 146.56 ? 910 ASN A OD1 1 ATOM 6811 N ND2 . ASN A 1 910 ? -20.321 29.788 93.183 1.00 131.54 ? 910 ASN A ND2 1 ATOM 6812 N N . LYS A 1 911 ? -20.777 26.407 95.584 1.00 144.52 ? 911 LYS A N 1 ATOM 6813 C CA . LYS A 1 911 ? -21.551 25.870 96.700 1.00 154.04 ? 911 LYS A CA 1 ATOM 6814 C C . LYS A 1 911 ? -22.988 25.546 96.312 1.00 150.60 ? 911 LYS A C 1 ATOM 6815 O O . LYS A 1 911 ? -23.375 24.380 96.250 1.00 142.97 ? 911 LYS A O 1 ATOM 6816 C CB . LYS A 1 911 ? -21.537 26.843 97.882 1.00 156.14 ? 911 LYS A CB 1 ATOM 6817 C CG . LYS A 1 911 ? -22.315 26.346 99.093 1.00 153.16 ? 911 LYS A CG 1 ATOM 6818 C CD . LYS A 1 911 ? -21.921 27.089 100.361 1.00 160.77 ? 911 LYS A CD 1 ATOM 6819 C CE . LYS A 1 911 ? -20.504 26.734 100.790 1.00 159.80 ? 911 LYS A CE 1 ATOM 6820 N NZ . LYS A 1 911 ? -20.134 27.368 102.087 1.00 163.59 ? 911 LYS A NZ 1 ATOM 6821 N N . GLU A 1 912 ? -23.775 26.587 96.054 1.00 163.89 ? 912 GLU A N 1 ATOM 6822 C CA . GLU A 1 912 ? -25.166 26.406 95.660 1.00 169.94 ? 912 GLU A CA 1 ATOM 6823 C C . GLU A 1 912 ? -25.217 25.758 94.285 1.00 154.05 ? 912 GLU A C 1 ATOM 6824 O O . GLU A 1 912 ? -26.171 25.058 93.948 1.00 155.67 ? 912 GLU A O 1 ATOM 6825 C CB . GLU A 1 912 ? -25.916 27.740 95.670 1.00 174.97 ? 912 GLU A CB 1 ATOM 6826 C CG . GLU A 1 912 ? -25.218 28.864 94.924 1.00 178.98 ? 912 GLU A CG 1 ATOM 6827 C CD . GLU A 1 912 ? -25.924 30.196 95.093 1.00 185.56 ? 912 GLU A CD 1 ATOM 6828 O OE1 . GLU A 1 912 ? -25.476 31.192 94.487 1.00 180.18 ? 912 GLU A OE1 1 ATOM 6829 O OE2 . GLU A 1 912 ? -26.928 30.247 95.835 1.00 191.21 ? 912 GLU A OE2 1 ATOM 6830 N N . ASN A 1 913 ? -24.177 26.000 93.494 1.00 142.79 ? 913 ASN A N 1 ATOM 6831 C CA . ASN A 1 913 ? -23.957 25.241 92.275 1.00 138.18 ? 913 ASN A CA 1 ATOM 6832 C C . ASN A 1 913 ? -22.693 24.406 92.424 1.00 145.32 ? 913 ASN A C 1 ATOM 6833 O O . ASN A 1 913 ? -21.587 24.944 92.412 1.00 155.83 ? 913 ASN A O 1 ATOM 6834 C CB . ASN A 1 913 ? -23.833 26.167 91.063 1.00 130.99 ? 913 ASN A CB 1 ATOM 6835 C CG . ASN A 1 913 ? -24.851 27.290 91.076 1.00 120.29 ? 913 ASN A CG 1 ATOM 6836 O OD1 . ASN A 1 913 ? -24.673 28.294 91.765 1.00 118.70 ? 913 ASN A OD1 1 ATOM 6837 N ND2 . ASN A 1 913 ? -25.918 27.134 90.301 1.00 108.82 ? 913 ASN A ND2 1 ATOM 6838 N N . GLN A 1 914 ? -22.852 23.095 92.566 1.00 145.37 ? 914 GLN A N 1 ATOM 6839 C CA . GLN A 1 914 ? -21.699 22.207 92.605 1.00 136.00 ? 914 GLN A CA 1 ATOM 6840 C C . GLN A 1 914 ? -21.778 21.223 91.452 1.00 141.12 ? 914 GLN A C 1 ATOM 6841 O O . GLN A 1 914 ? -21.099 21.392 90.444 1.00 144.68 ? 914 GLN A O 1 ATOM 6842 C CB . GLN A 1 914 ? -21.621 21.459 93.937 1.00 146.11 ? 914 GLN A CB 1 ATOM 6843 C CG . GLN A 1 914 ? -21.198 22.318 95.115 1.00 151.02 ? 914 GLN A CG 1 ATOM 6844 C CD . GLN A 1 914 ? -21.048 21.516 96.393 1.00 162.98 ? 914 GLN A CD 1 ATOM 6845 O OE1 . GLN A 1 914 ? -21.247 20.301 96.403 1.00 164.48 ? 914 GLN A OE1 1 ATOM 6846 N NE2 . GLN A 1 914 ? -20.695 22.193 97.479 1.00 167.40 ? 914 GLN A NE2 1 ATOM 6847 N N . ASN A 1 915 ? -22.620 20.205 91.590 1.00 146.49 ? 915 ASN A N 1 ATOM 6848 C CA . ASN A 1 915 ? -22.897 19.330 90.463 1.00 138.98 ? 915 ASN A CA 1 ATOM 6849 C C . ASN A 1 915 ? -24.358 19.431 90.048 1.00 140.49 ? 915 ASN A C 1 ATOM 6850 O O . ASN A 1 915 ? -25.238 18.886 90.716 1.00 155.86 ? 915 ASN A O 1 ATOM 6851 C CB . ASN A 1 915 ? -22.554 17.876 90.805 1.00 145.33 ? 915 ASN A CB 1 ATOM 6852 C CG . ASN A 1 915 ? -21.217 17.735 91.517 1.00 135.94 ? 915 ASN A CG 1 ATOM 6853 O OD1 . ASN A 1 915 ? -20.900 18.497 92.432 1.00 124.47 ? 915 ASN A OD1 1 ATOM 6854 N ND2 . ASN A 1 915 ? -20.427 16.752 91.100 1.00 127.14 ? 915 ASN A ND2 1 ATOM 6855 N N . HIS A 1 916 ? -24.612 20.118 88.940 1.00 132.68 ? 916 HIS A N 1 ATOM 6856 C CA . HIS A 1 916 ? -25.935 20.118 88.327 1.00 142.96 ? 916 HIS A CA 1 ATOM 6857 C C . HIS A 1 916 ? -25.857 20.581 86.878 1.00 139.51 ? 916 HIS A C 1 ATOM 6858 O O . HIS A 1 916 ? -24.913 21.266 86.485 1.00 124.80 ? 916 HIS A O 1 ATOM 6859 C CB . HIS A 1 916 ? -26.908 20.992 89.119 1.00 146.07 ? 916 HIS A CB 1 ATOM 6860 C CG . HIS A 1 916 ? -28.198 20.304 89.445 1.00 171.79 ? 916 HIS A CG 1 ATOM 6861 N ND1 . HIS A 1 916 ? -28.888 20.527 90.617 1.00 178.10 ? 916 HIS A ND1 1 ATOM 6862 C CD2 . HIS A 1 916 ? -28.919 19.391 88.752 1.00 176.86 ? 916 HIS A CD2 1 ATOM 6863 C CE1 . HIS A 1 916 ? -29.980 19.784 90.631 1.00 177.42 ? 916 HIS A CE1 1 ATOM 6864 N NE2 . HIS A 1 916 ? -30.022 19.085 89.511 1.00 183.05 ? 916 HIS A NE2 1 ATOM 6865 N N . SER A 1 917 ? -26.868 20.225 86.094 1.00 141.62 ? 917 SER A N 1 ATOM 6866 C CA . SER A 1 917 ? -26.880 20.540 84.672 1.00 131.90 ? 917 SER A CA 1 ATOM 6867 C C . SER A 1 917 ? -27.626 21.841 84.390 1.00 122.08 ? 917 SER A C 1 ATOM 6868 O O . SER A 1 917 ? -28.833 21.938 84.615 1.00 125.76 ? 917 SER A O 1 ATOM 6869 C CB . SER A 1 917 ? -27.504 19.387 83.881 1.00 148.46 ? 917 SER A CB 1 ATOM 6870 O OG . SER A 1 917 ? -28.730 18.972 84.461 1.00 162.74 ? 917 SER A OG 1 ATOM 6871 N N . TYR A 1 918 ? -26.897 22.838 83.896 1.00 119.32 ? 918 TYR A N 1 ATOM 6872 C CA . TYR A 1 918 ? -27.481 24.140 83.585 1.00 109.51 ? 918 TYR A CA 1 ATOM 6873 C C . TYR A 1 918 ? -27.409 24.458 82.093 1.00 100.55 ? 918 TYR A C 1 ATOM 6874 O O . TYR A 1 918 ? -26.364 24.304 81.462 1.00 104.65 ? 918 TYR A O 1 ATOM 6875 C CB . TYR A 1 918 ? -26.786 25.245 84.387 1.00 93.11 ? 918 TYR A CB 1 ATOM 6876 C CG . TYR A 1 918 ? -27.123 25.233 85.860 1.00 98.30 ? 918 TYR A CG 1 ATOM 6877 C CD1 . TYR A 1 918 ? -28.339 25.722 86.317 1.00 107.73 ? 918 TYR A CD1 1 ATOM 6878 C CD2 . TYR A 1 918 ? -26.226 24.734 86.793 1.00 108.89 ? 918 TYR A CD2 1 ATOM 6879 C CE1 . TYR A 1 918 ? -28.654 25.712 87.663 1.00 122.72 ? 918 TYR A CE1 1 ATOM 6880 C CE2 . TYR A 1 918 ? -26.532 24.720 88.142 1.00 130.50 ? 918 TYR A CE2 1 ATOM 6881 C CZ . TYR A 1 918 ? -27.747 25.211 88.571 1.00 133.28 ? 918 TYR A CZ 1 ATOM 6882 O OH . TYR A 1 918 ? -28.055 25.199 89.913 1.00 141.50 ? 918 TYR A OH 1 ATOM 6883 N N . SER A 1 919 ? -28.530 24.905 81.536 1.00 89.17 ? 919 SER A N 1 ATOM 6884 C CA . SER A 1 919 ? -28.586 25.295 80.133 1.00 84.82 ? 919 SER A CA 1 ATOM 6885 C C . SER A 1 919 ? -28.728 26.805 79.989 1.00 87.97 ? 919 SER A C 1 ATOM 6886 O O . SER A 1 919 ? -29.784 27.367 80.275 1.00 101.40 ? 919 SER A O 1 ATOM 6887 C CB . SER A 1 919 ? -29.749 24.594 79.430 1.00 87.35 ? 919 SER A CB 1 ATOM 6888 O OG . SER A 1 919 ? -29.999 25.173 78.162 1.00 83.73 ? 919 SER A OG 1 ATOM 6889 N N . LEU A 1 920 ? -27.665 27.455 79.530 1.00 82.90 ? 920 LEU A N 1 ATOM 6890 C CA . LEU A 1 920 ? -27.667 28.903 79.366 1.00 74.74 ? 920 LEU A CA 1 ATOM 6891 C C . LEU A 1 920 ? -28.341 29.285 78.057 1.00 81.69 ? 920 LEU A C 1 ATOM 6892 O O . LEU A 1 920 ? -27.941 28.837 76.985 1.00 82.97 ? 920 LEU A O 1 ATOM 6893 C CB . LEU A 1 920 ? -26.242 29.452 79.418 1.00 71.49 ? 920 LEU A CB 1 ATOM 6894 C CG . LEU A 1 920 ? -25.476 29.087 80.691 1.00 83.39 ? 920 LEU A CG 1 ATOM 6895 C CD1 . LEU A 1 920 ? -24.072 29.660 80.665 1.00 85.44 ? 920 LEU A CD1 1 ATOM 6896 C CD2 . LEU A 1 920 ? -26.228 29.557 81.926 1.00 87.35 ? 920 LEU A CD2 1 ATOM 6897 N N . LYS A 1 921 ? -29.367 30.121 78.155 1.00 85.82 ? 921 LYS A N 1 ATOM 6898 C CA . LYS A 1 921 ? -30.212 30.436 77.014 1.00 71.86 ? 921 LYS A CA 1 ATOM 6899 C C . LYS A 1 921 ? -30.270 31.931 76.738 1.00 83.78 ? 921 LYS A C 1 ATOM 6900 O O . LYS A 1 921 ? -30.563 32.728 77.628 1.00 103.43 ? 921 LYS A O 1 ATOM 6901 C CB . LYS A 1 921 ? -31.619 29.882 77.249 1.00 77.34 ? 921 LYS A CB 1 ATOM 6902 C CG . LYS A 1 921 ? -32.702 30.461 76.358 1.00 94.64 ? 921 LYS A CG 1 ATOM 6903 C CD . LYS A 1 921 ? -34.000 29.679 76.526 1.00 114.38 ? 921 LYS A CD 1 ATOM 6904 C CE . LYS A 1 921 ? -35.206 30.478 76.060 1.00 123.76 ? 921 LYS A CE 1 ATOM 6905 N NZ . LYS A 1 921 ? -35.495 31.626 76.965 1.00 124.47 ? 921 LYS A NZ 1 ATOM 6906 N N . SER A 1 922 ? -29.976 32.306 75.499 1.00 87.29 ? 922 SER A N 1 ATOM 6907 C CA . SER A 1 922 ? -30.114 33.689 75.069 1.00 73.87 ? 922 SER A CA 1 ATOM 6908 C C . SER A 1 922 ? -31.035 33.747 73.861 1.00 79.00 ? 922 SER A C 1 ATOM 6909 O O . SER A 1 922 ? -30.978 32.883 72.986 1.00 76.31 ? 922 SER A O 1 ATOM 6910 C CB . SER A 1 922 ? -28.756 34.303 74.734 1.00 57.00 ? 922 SER A CB 1 ATOM 6911 O OG . SER A 1 922 ? -28.221 33.732 73.554 1.00 59.17 ? 922 SER A OG 1 ATOM 6912 N N . SER A 1 923 ? -31.886 34.766 73.820 1.00 77.66 ? 923 SER A N 1 ATOM 6913 C CA . SER A 1 923 ? -32.852 34.907 72.741 1.00 66.45 ? 923 SER A CA 1 ATOM 6914 C C . SER A 1 923 ? -32.639 36.205 71.980 1.00 63.92 ? 923 SER A C 1 ATOM 6915 O O . SER A 1 923 ? -32.199 37.204 72.549 1.00 83.02 ? 923 SER A O 1 ATOM 6916 C CB . SER A 1 923 ? -34.280 34.845 73.289 1.00 76.43 ? 923 SER A CB 1 ATOM 6917 O OG . SER A 1 923 ? -34.469 35.784 74.332 1.00 81.01 ? 923 SER A OG 1 ATOM 6918 N N . ALA A 1 924 ? -32.943 36.179 70.687 1.00 62.81 ? 924 ALA A N 1 ATOM 6919 C CA . ALA A 1 924 ? -32.856 37.374 69.857 1.00 53.00 ? 924 ALA A CA 1 ATOM 6920 C C . ALA A 1 924 ? -34.051 37.473 68.922 1.00 71.43 ? 924 ALA A C 1 ATOM 6921 O O . ALA A 1 924 ? -34.326 36.551 68.152 1.00 62.61 ? 924 ALA A O 1 ATOM 6922 C CB . ALA A 1 924 ? -31.569 37.380 69.066 1.00 66.19 ? 924 ALA A CB 1 ATOM 6923 N N . SER A 1 925 ? -34.756 38.597 68.995 1.00 88.67 ? 925 SER A N 1 ATOM 6924 C CA . SER A 1 925 ? -35.914 38.835 68.144 1.00 70.87 ? 925 SER A CA 1 ATOM 6925 C C . SER A 1 925 ? -35.642 40.001 67.212 1.00 68.59 ? 925 SER A C 1 ATOM 6926 O O . SER A 1 925 ? -34.817 40.864 67.513 1.00 82.83 ? 925 SER A O 1 ATOM 6927 C CB . SER A 1 925 ? -37.158 39.115 68.983 1.00 77.02 ? 925 SER A CB 1 ATOM 6928 O OG . SER A 1 925 ? -37.020 40.328 69.699 1.00 112.45 ? 925 SER A OG 1 ATOM 6929 N N . PHE A 1 926 ? -36.328 40.023 66.075 1.00 62.48 ? 926 PHE A N 1 ATOM 6930 C CA . PHE A 1 926 ? -36.169 41.120 65.131 1.00 74.69 ? 926 PHE A CA 1 ATOM 6931 C C . PHE A 1 926 ? -37.516 41.622 64.637 1.00 72.16 ? 926 PHE A C 1 ATOM 6932 O O . PHE A 1 926 ? -38.470 40.856 64.506 1.00 73.29 ? 926 PHE A O 1 ATOM 6933 C CB . PHE A 1 926 ? -35.302 40.696 63.943 1.00 87.29 ? 926 PHE A CB 1 ATOM 6934 C CG . PHE A 1 926 ? -36.043 39.915 62.897 1.00 84.44 ? 926 PHE A CG 1 ATOM 6935 C CD1 . PHE A 1 926 ? -36.604 40.553 61.801 1.00 90.08 ? 926 PHE A CD1 1 ATOM 6936 C CD2 . PHE A 1 926 ? -36.169 38.541 63.002 1.00 69.94 ? 926 PHE A CD2 1 ATOM 6937 C CE1 . PHE A 1 926 ? -37.284 39.838 60.840 1.00 89.29 ? 926 PHE A CE1 1 ATOM 6938 C CE2 . PHE A 1 926 ? -36.847 37.820 62.041 1.00 77.41 ? 926 PHE A CE2 1 ATOM 6939 C CZ . PHE A 1 926 ? -37.404 38.470 60.958 1.00 85.05 ? 926 PHE A CZ 1 ATOM 6940 N N . ASN A 1 927 ? -37.577 42.918 64.357 1.00 85.30 ? 927 ASN A N 1 ATOM 6941 C CA . ASN A 1 927 ? -38.783 43.545 63.841 1.00 66.85 ? 927 ASN A CA 1 ATOM 6942 C C . ASN A 1 927 ? -38.431 44.494 62.701 1.00 64.70 ? 927 ASN A C 1 ATOM 6943 O O . ASN A 1 927 ? -37.572 45.361 62.856 1.00 59.64 ? 927 ASN A O 1 ATOM 6944 C CB . ASN A 1 927 ? -39.512 44.290 64.958 1.00 68.62 ? 927 ASN A CB 1 ATOM 6945 C CG . ASN A 1 927 ? -40.935 44.648 64.591 1.00 105.19 ? 927 ASN A CG 1 ATOM 6946 O OD1 . ASN A 1 927 ? -41.301 44.670 63.416 1.00 128.69 ? 927 ASN A OD1 1 ATOM 6947 N ND2 . ASN A 1 927 ? -41.748 44.937 65.600 1.00 118.77 ? 927 ASN A ND2 1 ATOM 6948 N N . VAL A 1 928 ? -39.087 44.325 61.557 1.00 61.91 ? 928 VAL A N 1 ATOM 6949 C CA . VAL A 1 928 ? -38.816 45.165 60.396 1.00 67.27 ? 928 VAL A CA 1 ATOM 6950 C C . VAL A 1 928 ? -39.773 46.347 60.394 1.00 73.62 ? 928 VAL A C 1 ATOM 6951 O O . VAL A 1 928 ? -40.975 46.180 60.195 1.00 89.09 ? 928 VAL A O 1 ATOM 6952 C CB . VAL A 1 928 ? -38.958 44.379 59.078 1.00 66.04 ? 928 VAL A CB 1 ATOM 6953 C CG1 . VAL A 1 928 ? -38.704 45.287 57.887 1.00 65.70 ? 928 VAL A CG1 1 ATOM 6954 C CG2 . VAL A 1 928 ? -38.007 43.195 59.061 1.00 64.86 ? 928 VAL A CG2 1 ATOM 6955 N N . ILE A 1 929 ? -39.238 47.539 60.634 1.00 69.92 ? 929 ILE A N 1 ATOM 6956 C CA . ILE A 1 929 ? -40.078 48.718 60.816 1.00 84.33 ? 929 ILE A CA 1 ATOM 6957 C C . ILE A 1 929 ? -40.312 49.576 59.571 1.00 70.57 ? 929 ILE A C 1 ATOM 6958 O O . ILE A 1 929 ? -41.183 50.443 59.589 1.00 98.69 ? 929 ILE A O 1 ATOM 6959 C CB . ILE A 1 929 ? -39.489 49.632 61.906 1.00 92.77 ? 929 ILE A CB 1 ATOM 6960 C CG1 . ILE A 1 929 ? -38.156 50.217 61.443 1.00 97.13 ? 929 ILE A CG1 1 ATOM 6961 C CG2 . ILE A 1 929 ? -39.315 48.864 63.209 1.00 68.11 ? 929 ILE A CG2 1 ATOM 6962 C CD1 . ILE A 1 929 ? -37.455 51.036 62.496 1.00 98.45 ? 929 ILE A CD1 1 ATOM 6963 N N . GLU A 1 930 ? -39.565 49.338 58.495 1.00 68.96 ? 930 GLU A N 1 ATOM 6964 C CA . GLU A 1 930 ? -39.647 50.222 57.326 1.00 93.69 ? 930 GLU A CA 1 ATOM 6965 C C . GLU A 1 930 ? -39.197 49.593 56.009 1.00 82.69 ? 930 GLU A C 1 ATOM 6966 O O . GLU A 1 930 ? -38.447 48.618 55.991 1.00 94.33 ? 930 GLU A O 1 ATOM 6967 C CB . GLU A 1 930 ? -38.822 51.490 57.567 1.00 95.11 ? 930 GLU A CB 1 ATOM 6968 C CG . GLU A 1 930 ? -39.627 52.695 58.027 1.00 105.81 ? 930 GLU A CG 1 ATOM 6969 C CD . GLU A 1 930 ? -38.786 53.953 58.118 1.00 115.78 ? 930 GLU A CD 1 ATOM 6970 O OE1 . GLU A 1 930 ? -37.749 54.025 57.424 1.00 114.78 ? 930 GLU A OE1 1 ATOM 6971 O OE2 . GLU A 1 930 ? -39.158 54.867 58.885 1.00 126.49 ? 930 GLU A OE2 1 ATOM 6972 N N . PHE A 1 931 ? -39.650 50.188 54.908 1.00 77.68 ? 931 PHE A N 1 ATOM 6973 C CA . PHE A 1 931 ? -39.275 49.760 53.563 1.00 77.31 ? 931 PHE A CA 1 ATOM 6974 C C . PHE A 1 931 ? -39.020 50.980 52.671 1.00 96.99 ? 931 PHE A C 1 ATOM 6975 O O . PHE A 1 931 ? -39.617 52.037 52.882 1.00 101.61 ? 931 PHE A O 1 ATOM 6976 C CB . PHE A 1 931 ? -40.370 48.881 52.946 1.00 75.36 ? 931 PHE A CB 1 ATOM 6977 C CG . PHE A 1 931 ? -40.658 47.624 53.717 1.00 75.07 ? 931 PHE A CG 1 ATOM 6978 C CD1 . PHE A 1 931 ? -41.655 47.598 54.678 1.00 74.25 ? 931 PHE A CD1 1 ATOM 6979 C CD2 . PHE A 1 931 ? -39.945 46.462 53.468 1.00 95.16 ? 931 PHE A CD2 1 ATOM 6980 C CE1 . PHE A 1 931 ? -41.927 46.440 55.383 1.00 80.82 ? 931 PHE A CE1 1 ATOM 6981 C CE2 . PHE A 1 931 ? -40.213 45.299 54.170 1.00 73.68 ? 931 PHE A CE2 1 ATOM 6982 C CZ . PHE A 1 931 ? -41.204 45.289 55.129 1.00 80.33 ? 931 PHE A CZ 1 ATOM 6983 N N . PRO A 1 932 ? -38.134 50.834 51.669 1.00 87.66 ? 932 PRO A N 1 ATOM 6984 C CA . PRO A 1 932 ? -37.833 51.860 50.657 1.00 88.11 ? 932 PRO A CA 1 ATOM 6985 C C . PRO A 1 932 ? -39.013 52.123 49.725 1.00 91.45 ? 932 PRO A C 1 ATOM 6986 O O . PRO A 1 932 ? -39.021 53.089 48.962 1.00 129.65 ? 932 PRO A O 1 ATOM 6987 C CB . PRO A 1 932 ? -36.657 51.256 49.885 1.00 84.65 ? 932 PRO A CB 1 ATOM 6988 C CG . PRO A 1 932 ? -36.815 49.795 50.056 1.00 82.03 ? 932 PRO A CG 1 ATOM 6989 C CD . PRO A 1 932 ? -37.337 49.615 51.452 1.00 75.70 ? 932 PRO A CD 1 ATOM 6990 N N . TYR A 1 933 ? -40.000 51.242 49.804 1.00 83.81 ? 933 TYR A N 1 ATOM 6991 C CA . TYR A 1 933 ? -41.092 51.136 48.844 1.00 87.28 ? 933 TYR A CA 1 ATOM 6992 C C . TYR A 1 933 ? -42.296 52.020 49.162 1.00 94.95 ? 933 TYR A C 1 ATOM 6993 O O . TYR A 1 933 ? -43.371 51.810 48.610 1.00 106.12 ? 933 TYR A O 1 ATOM 6994 C CB . TYR A 1 933 ? -41.523 49.677 48.719 1.00 90.17 ? 933 TYR A CB 1 ATOM 6995 C CG . TYR A 1 933 ? -40.388 48.787 48.271 1.00 101.33 ? 933 TYR A CG 1 ATOM 6996 C CD1 . TYR A 1 933 ? -39.892 48.865 46.977 1.00 102.48 ? 933 TYR A CD1 1 ATOM 6997 C CD2 . TYR A 1 933 ? -39.800 47.882 49.145 1.00 95.36 ? 933 TYR A CD2 1 ATOM 6998 C CE1 . TYR A 1 933 ? -38.849 48.060 46.561 1.00 100.23 ? 933 TYR A CE1 1 ATOM 6999 C CE2 . TYR A 1 933 ? -38.755 47.071 48.736 1.00 95.15 ? 933 TYR A CE2 1 ATOM 7000 C CZ . TYR A 1 933 ? -38.283 47.165 47.443 1.00 93.57 ? 933 TYR A CZ 1 ATOM 7001 O OH . TYR A 1 933 ? -37.244 46.361 47.032 1.00 95.96 ? 933 TYR A OH 1 ATOM 7002 N N . LYS A 1 934 ? -42.110 52.991 50.055 1.00 104.75 ? 934 LYS A N 1 ATOM 7003 C CA . LYS A 1 934 ? -43.203 53.776 50.637 1.00 119.04 ? 934 LYS A CA 1 ATOM 7004 C C . LYS A 1 934 ? -44.218 54.281 49.612 1.00 127.94 ? 934 LYS A C 1 ATOM 7005 O O . LYS A 1 934 ? -43.872 54.569 48.465 1.00 135.99 ? 934 LYS A O 1 ATOM 7006 C CB . LYS A 1 934 ? -42.639 54.975 51.402 1.00 125.08 ? 934 LYS A CB 1 ATOM 7007 C CG . LYS A 1 934 ? -42.074 54.647 52.771 1.00 122.66 ? 934 LYS A CG 1 ATOM 7008 C CD . LYS A 1 934 ? -40.623 55.082 52.888 1.00 122.84 ? 934 LYS A CD 1 ATOM 7009 C CE . LYS A 1 934 ? -40.312 55.576 54.291 1.00 140.14 ? 934 LYS A CE 1 ATOM 7010 N NZ . LYS A 1 934 ? -40.914 54.702 55.335 1.00 145.85 ? 934 LYS A NZ 1 ATOM 7011 N N . ASN A 1 935 ? -45.472 54.355 50.063 1.00 139.80 ? 935 ASN A N 1 ATOM 7012 C CA . ASN A 1 935 ? -46.670 54.465 49.226 1.00 154.49 ? 935 ASN A CA 1 ATOM 7013 C C . ASN A 1 935 ? -46.898 53.174 48.446 1.00 139.18 ? 935 ASN A C 1 ATOM 7014 O O . ASN A 1 935 ? -47.357 53.183 47.304 1.00 138.89 ? 935 ASN A O 1 ATOM 7015 C CB . ASN A 1 935 ? -46.595 55.669 48.280 1.00 154.26 ? 935 ASN A CB 1 ATOM 7016 C CG . ASN A 1 935 ? -46.807 56.988 49.002 1.00 147.77 ? 935 ASN A CG 1 ATOM 7017 O OD1 . ASN A 1 935 ? -45.860 57.601 49.496 1.00 150.76 ? 935 ASN A OD1 1 ATOM 7018 N ND2 . ASN A 1 935 ? -48.057 57.430 49.069 1.00 139.97 ? 935 ASN A ND2 1 ATOM 7019 N N . LEU A 1 936 ? -46.558 52.064 49.095 1.00 126.56 ? 936 LEU A N 1 ATOM 7020 C CA . LEU A 1 936 ? -46.922 50.726 48.645 1.00 131.89 ? 936 LEU A CA 1 ATOM 7021 C C . LEU A 1 936 ? -47.194 49.880 49.889 1.00 127.23 ? 936 LEU A C 1 ATOM 7022 O O . LEU A 1 936 ? -46.526 50.062 50.908 1.00 106.51 ? 936 LEU A O 1 ATOM 7023 C CB . LEU A 1 936 ? -45.809 50.112 47.792 1.00 126.74 ? 936 LEU A CB 1 ATOM 7024 C CG . LEU A 1 936 ? -46.140 48.932 46.878 1.00 127.33 ? 936 LEU A CG 1 ATOM 7025 C CD1 . LEU A 1 936 ? -47.083 49.364 45.762 1.00 139.21 ? 936 LEU A CD1 1 ATOM 7026 C CD2 . LEU A 1 936 ? -44.870 48.322 46.309 1.00 112.88 ? 936 LEU A CD2 1 ATOM 7027 N N . PRO A 1 937 ? -48.170 48.957 49.813 1.00 127.58 ? 937 PRO A N 1 ATOM 7028 C CA . PRO A 1 937 ? -48.533 48.102 50.951 1.00 126.19 ? 937 PRO A CA 1 ATOM 7029 C C . PRO A 1 937 ? -47.331 47.443 51.628 1.00 131.24 ? 937 PRO A C 1 ATOM 7030 O O . PRO A 1 937 ? -46.364 47.078 50.962 1.00 141.17 ? 937 PRO A O 1 ATOM 7031 C CB . PRO A 1 937 ? -49.441 47.054 50.310 1.00 135.15 ? 937 PRO A CB 1 ATOM 7032 C CG . PRO A 1 937 ? -50.130 47.810 49.224 1.00 130.90 ? 937 PRO A CG 1 ATOM 7033 C CD . PRO A 1 937 ? -49.125 48.810 48.699 1.00 123.11 ? 937 PRO A CD 1 ATOM 7034 N N . ILE A 1 938 ? -47.405 47.308 52.948 1.00 136.36 ? 938 ILE A N 1 ATOM 7035 C CA . ILE A 1 938 ? -46.251 46.943 53.764 1.00 116.85 ? 938 ILE A CA 1 ATOM 7036 C C . ILE A 1 938 ? -46.376 45.587 54.469 1.00 114.15 ? 938 ILE A C 1 ATOM 7037 O O . ILE A 1 938 ? -45.542 44.701 54.261 1.00 106.92 ? 938 ILE A O 1 ATOM 7038 C CB . ILE A 1 938 ? -45.961 48.030 54.825 1.00 118.99 ? 938 ILE A CB 1 ATOM 7039 C CG1 . ILE A 1 938 ? -47.263 48.629 55.362 1.00 130.47 ? 938 ILE A CG1 1 ATOM 7040 C CG2 . ILE A 1 938 ? -45.108 49.137 54.228 1.00 117.24 ? 938 ILE A CG2 1 ATOM 7041 C CD1 . ILE A 1 938 ? -47.054 49.670 56.440 1.00 123.47 ? 938 ILE A CD1 1 ATOM 7042 N N . GLU A 1 939 ? -47.404 45.454 55.308 1.00 132.97 ? 939 GLU A N 1 ATOM 7043 C CA . GLU A 1 939 ? -47.517 44.388 56.308 1.00 158.77 ? 939 GLU A CA 1 ATOM 7044 C C . GLU A 1 939 ? -46.377 44.548 57.317 1.00 163.35 ? 939 GLU A C 1 ATOM 7045 O O . GLU A 1 939 ? -46.120 45.661 57.777 1.00 169.75 ? 939 GLU A O 1 ATOM 7046 C CB . GLU A 1 939 ? -47.507 42.996 55.654 1.00 161.85 ? 939 GLU A CB 1 ATOM 7047 C CG . GLU A 1 939 ? -48.084 41.866 56.509 1.00 154.08 ? 939 GLU A CG 1 ATOM 7048 C CD . GLU A 1 939 ? -49.587 41.957 56.683 1.00 163.39 ? 939 GLU A CD 1 ATOM 7049 O OE1 . GLU A 1 939 ? -50.234 42.713 55.928 1.00 163.50 ? 939 GLU A OE1 1 ATOM 7050 O OE2 . GLU A 1 939 ? -50.123 41.266 57.576 1.00 164.59 ? 939 GLU A OE2 1 ATOM 7051 N N . ASP A 1 940 ? -45.680 43.460 57.638 1.00 146.02 ? 940 ASP A N 1 ATOM 7052 C CA . ASP A 1 940 ? -44.635 43.485 58.660 1.00 139.17 ? 940 ASP A CA 1 ATOM 7053 C C . ASP A 1 940 ? -43.941 42.138 58.779 1.00 131.17 ? 940 ASP A C 1 ATOM 7054 O O . ASP A 1 940 ? -44.468 41.113 58.348 1.00 137.93 ? 940 ASP A O 1 ATOM 7055 C CB . ASP A 1 940 ? -45.215 43.867 60.023 1.00 140.59 ? 940 ASP A CB 1 ATOM 7056 C CG . ASP A 1 940 ? -46.113 42.789 60.590 1.00 143.32 ? 940 ASP A CG 1 ATOM 7057 O OD1 . ASP A 1 940 ? -47.319 42.789 60.267 1.00 153.29 ? 940 ASP A OD1 1 ATOM 7058 O OD2 . ASP A 1 940 ? -45.612 41.937 61.353 1.00 136.03 ? 940 ASP A OD2 1 ATOM 7059 N N . ILE A 1 941 ? -42.756 42.148 59.382 1.00 98.43 ? 941 ILE A N 1 ATOM 7060 C CA . ILE A 1 941 ? -41.947 40.944 59.515 1.00 81.69 ? 941 ILE A CA 1 ATOM 7061 C C . ILE A 1 941 ? -41.335 40.850 60.907 1.00 82.56 ? 941 ILE A C 1 ATOM 7062 O O . ILE A 1 941 ? -40.608 41.746 61.334 1.00 86.79 ? 941 ILE A O 1 ATOM 7063 C CB . ILE A 1 941 ? -40.822 40.907 58.466 1.00 82.01 ? 941 ILE A CB 1 ATOM 7064 C CG1 . ILE A 1 941 ? -41.394 41.079 57.056 1.00 81.91 ? 941 ILE A CG1 1 ATOM 7065 C CG2 . ILE A 1 941 ? -40.038 39.609 58.574 1.00 96.15 ? 941 ILE A CG2 1 ATOM 7066 C CD1 . ILE A 1 941 ? -40.395 41.586 56.046 1.00 94.53 ? 941 ILE A CD1 1 ATOM 7067 N N . THR A 1 942 ? -41.629 39.761 61.608 1.00 90.54 ? 942 THR A N 1 ATOM 7068 C CA . THR A 1 942 ? -41.133 39.558 62.965 1.00 85.49 ? 942 THR A CA 1 ATOM 7069 C C . THR A 1 942 ? -40.956 38.068 63.250 1.00 94.50 ? 942 THR A C 1 ATOM 7070 O O . THR A 1 942 ? -41.755 37.247 62.796 1.00 124.44 ? 942 THR A O 1 ATOM 7071 C CB . THR A 1 942 ? -42.090 40.179 64.013 1.00 94.49 ? 942 THR A CB 1 ATOM 7072 O OG1 . THR A 1 942 ? -42.345 41.549 63.681 1.00 118.30 ? 942 THR A OG1 1 ATOM 7073 C CG2 . THR A 1 942 ? -41.494 40.110 65.413 1.00 92.15 ? 942 THR A CG2 1 ATOM 7074 N N . ASN A 1 943 ? -39.920 37.736 64.018 1.00 82.02 ? 943 ASN A N 1 ATOM 7075 C CA . ASN A 1 943 ? -39.631 36.359 64.413 1.00 82.22 ? 943 ASN A CA 1 ATOM 7076 C C . ASN A 1 943 ? -38.450 36.341 65.370 1.00 72.19 ? 943 ASN A C 1 ATOM 7077 O O . ASN A 1 943 ? -37.756 37.346 65.525 1.00 69.54 ? 943 ASN A O 1 ATOM 7078 C CB . ASN A 1 943 ? -39.335 35.478 63.195 1.00 92.76 ? 943 ASN A CB 1 ATOM 7079 C CG . ASN A 1 943 ? -39.968 34.101 63.302 1.00 108.26 ? 943 ASN A CG 1 ATOM 7080 O OD1 . ASN A 1 943 ? -39.889 33.448 64.342 1.00 93.59 ? 943 ASN A OD1 1 ATOM 7081 N ND2 . ASN A 1 943 ? -40.605 33.658 62.221 1.00 143.71 ? 943 ASN A ND2 1 ATOM 7082 N N . SER A 1 944 ? -38.229 35.208 66.025 1.00 75.89 ? 944 SER A N 1 ATOM 7083 C CA . SER A 1 944 ? -37.151 35.112 66.999 1.00 71.60 ? 944 SER A CA 1 ATOM 7084 C C . SER A 1 944 ? -36.595 33.701 67.108 1.00 72.61 ? 944 SER A C 1 ATOM 7085 O O . SER A 1 944 ? -37.320 32.719 66.940 1.00 83.65 ? 944 SER A O 1 ATOM 7086 C CB . SER A 1 944 ? -37.637 35.577 68.370 1.00 70.20 ? 944 SER A CB 1 ATOM 7087 O OG . SER A 1 944 ? -38.716 34.777 68.821 1.00 86.06 ? 944 SER A OG 1 ATOM 7088 N N . THR A 1 945 ? -35.302 33.612 67.393 1.00 63.41 ? 945 THR A N 1 ATOM 7089 C CA . THR A 1 945 ? -34.659 32.334 67.651 1.00 64.88 ? 945 THR A CA 1 ATOM 7090 C C . THR A 1 945 ? -33.830 32.433 68.923 1.00 67.98 ? 945 THR A C 1 ATOM 7091 O O . THR A 1 945 ? -33.387 33.517 69.300 1.00 72.07 ? 945 THR A O 1 ATOM 7092 C CB . THR A 1 945 ? -33.762 31.895 66.484 1.00 72.35 ? 945 THR A CB 1 ATOM 7093 O OG1 . THR A 1 945 ? -33.218 30.597 66.759 1.00 94.85 ? 945 THR A OG1 1 ATOM 7094 C CG2 . THR A 1 945 ? -32.627 32.893 66.280 1.00 56.51 ? 945 THR A CG2 1 ATOM 7095 N N . LEU A 1 946 ? -33.628 31.304 69.589 1.00 70.53 ? 946 LEU A N 1 ATOM 7096 C CA . LEU A 1 946 ? -32.855 31.292 70.821 1.00 81.43 ? 946 LEU A CA 1 ATOM 7097 C C . LEU A 1 946 ? -31.597 30.446 70.666 1.00 89.67 ? 946 LEU A C 1 ATOM 7098 O O . LEU A 1 946 ? -31.592 29.450 69.943 1.00 69.92 ? 946 LEU A O 1 ATOM 7099 C CB . LEU A 1 946 ? -33.711 30.784 71.985 1.00 80.36 ? 946 LEU A CB 1 ATOM 7100 C CG . LEU A 1 946 ? -34.506 29.493 71.773 1.00 78.51 ? 946 LEU A CG 1 ATOM 7101 C CD1 . LEU A 1 946 ? -33.682 28.264 72.137 1.00 90.95 ? 946 LEU A CD1 1 ATOM 7102 C CD2 . LEU A 1 946 ? -35.799 29.530 72.569 1.00 80.29 ? 946 LEU A CD2 1 ATOM 7103 N N . VAL A 1 947 ? -30.532 30.858 71.343 1.00 85.76 ? 947 VAL A N 1 ATOM 7104 C CA . VAL A 1 947 ? -29.265 30.143 71.288 1.00 79.20 ? 947 VAL A CA 1 ATOM 7105 C C . VAL A 1 947 ? -28.890 29.628 72.667 1.00 86.57 ? 947 VAL A C 1 ATOM 7106 O O . VAL A 1 947 ? -28.902 30.375 73.646 1.00 84.35 ? 947 VAL A O 1 ATOM 7107 C CB . VAL A 1 947 ? -28.138 31.035 70.745 1.00 71.07 ? 947 VAL A CB 1 ATOM 7108 C CG1 . VAL A 1 947 ? -26.794 30.339 70.879 1.00 59.82 ? 947 VAL A CG1 1 ATOM 7109 C CG2 . VAL A 1 947 ? -28.409 31.385 69.301 1.00 72.77 ? 947 VAL A CG2 1 ATOM 7110 N N . THR A 1 948 ? -28.552 28.345 72.736 1.00 82.42 ? 948 THR A N 1 ATOM 7111 C CA . THR A 1 948 ? -28.297 27.702 74.014 1.00 75.12 ? 948 THR A CA 1 ATOM 7112 C C . THR A 1 948 ? -26.859 27.205 74.161 1.00 83.21 ? 948 THR A C 1 ATOM 7113 O O . THR A 1 948 ? -26.268 26.672 73.221 1.00 95.01 ? 948 THR A O 1 ATOM 7114 C CB . THR A 1 948 ? -29.261 26.522 74.230 1.00 82.17 ? 948 THR A CB 1 ATOM 7115 O OG1 . THR A 1 948 ? -28.871 25.795 75.399 1.00 108.62 ? 948 THR A OG1 1 ATOM 7116 C CG2 . THR A 1 948 ? -29.250 25.590 73.022 1.00 80.99 ? 948 THR A CG2 1 ATOM 7117 N N . THR A 1 949 ? -26.303 27.412 75.350 1.00 76.33 ? 949 THR A N 1 ATOM 7118 C CA . THR A 1 949 ? -25.012 26.851 75.727 1.00 70.98 ? 949 THR A CA 1 ATOM 7119 C C . THR A 1 949 ? -25.179 25.986 76.970 1.00 79.97 ? 949 THR A C 1 ATOM 7120 O O . THR A 1 949 ? -25.470 26.495 78.051 1.00 94.94 ? 949 THR A O 1 ATOM 7121 C CB . THR A 1 949 ? -23.966 27.945 76.008 1.00 79.54 ? 949 THR A CB 1 ATOM 7122 O OG1 . THR A 1 949 ? -23.733 28.709 74.819 1.00 88.58 ? 949 THR A OG1 1 ATOM 7123 C CG2 . THR A 1 949 ? -22.658 27.323 76.468 1.00 76.28 ? 949 THR A CG2 1 ATOM 7124 N N . ASN A 1 950 ? -24.994 24.679 76.820 1.00 85.36 ? 950 ASN A N 1 ATOM 7125 C CA . ASN A 1 950 ? -25.185 23.762 77.936 1.00 77.34 ? 950 ASN A CA 1 ATOM 7126 C C . ASN A 1 950 ? -23.871 23.398 78.625 1.00 88.09 ? 950 ASN A C 1 ATOM 7127 O O . ASN A 1 950 ? -22.953 22.871 77.992 1.00 122.73 ? 950 ASN A O 1 ATOM 7128 C CB . ASN A 1 950 ? -25.894 22.489 77.464 1.00 79.75 ? 950 ASN A CB 1 ATOM 7129 C CG . ASN A 1 950 ? -27.254 22.768 76.844 1.00 104.21 ? 950 ASN A CG 1 ATOM 7130 O OD1 . ASN A 1 950 ? -27.751 23.890 76.894 1.00 124.37 ? 950 ASN A OD1 1 ATOM 7131 N ND2 . ASN A 1 950 ? -27.863 21.739 76.262 1.00 131.96 ? 950 ASN A ND2 1 ATOM 7132 N N . VAL A 1 951 ? -23.781 23.691 79.920 1.00 82.26 ? 951 VAL A N 1 ATOM 7133 C CA . VAL A 1 951 ? -22.645 23.251 80.725 1.00 82.02 ? 951 VAL A CA 1 ATOM 7134 C C . VAL A 1 951 ? -23.072 22.059 81.575 1.00 91.67 ? 951 VAL A C 1 ATOM 7135 O O . VAL A 1 951 ? -24.189 22.023 82.093 1.00 99.49 ? 951 VAL A O 1 ATOM 7136 C CB . VAL A 1 951 ? -22.090 24.377 81.626 1.00 88.33 ? 951 VAL A CB 1 ATOM 7137 C CG1 . VAL A 1 951 ? -21.622 25.550 80.778 1.00 97.46 ? 951 VAL A CG1 1 ATOM 7138 C CG2 . VAL A 1 951 ? -23.130 24.834 82.633 1.00 104.29 ? 951 VAL A CG2 1 ATOM 7139 N N . THR A 1 952 ? -22.188 21.076 81.704 1.00 107.05 ? 952 THR A N 1 ATOM 7140 C CA . THR A 1 952 ? -22.559 19.807 82.323 1.00 101.57 ? 952 THR A CA 1 ATOM 7141 C C . THR A 1 952 ? -21.429 19.178 83.127 1.00 109.66 ? 952 THR A C 1 ATOM 7142 O O . THR A 1 952 ? -20.262 19.536 82.970 1.00 103.49 ? 952 THR A O 1 ATOM 7143 C CB . THR A 1 952 ? -23.023 18.794 81.261 1.00 115.39 ? 952 THR A CB 1 ATOM 7144 O OG1 . THR A 1 952 ? -22.249 18.968 80.067 1.00 128.31 ? 952 THR A OG1 1 ATOM 7145 C CG2 . THR A 1 952 ? -24.495 18.998 80.933 1.00 116.34 ? 952 THR A CG2 1 ATOM 7146 N N . TRP A 1 953 ? -21.793 18.231 83.987 1.00 116.13 ? 953 TRP A N 1 ATOM 7147 C CA . TRP A 1 953 ? -20.823 17.498 84.789 1.00 108.59 ? 953 TRP A CA 1 ATOM 7148 C C . TRP A 1 953 ? -20.792 16.020 84.406 1.00 126.45 ? 953 TRP A C 1 ATOM 7149 O O . TRP A 1 953 ? -19.835 15.550 83.791 1.00 138.01 ? 953 TRP A O 1 ATOM 7150 C CB . TRP A 1 953 ? -21.138 17.649 86.279 1.00 125.76 ? 953 TRP A CB 1 ATOM 7151 C CG . TRP A 1 953 ? -20.832 19.009 86.822 1.00 124.22 ? 953 TRP A CG 1 ATOM 7152 C CD1 . TRP A 1 953 ? -21.651 20.099 86.811 1.00 125.10 ? 953 TRP A CD1 1 ATOM 7153 C CD2 . TRP A 1 953 ? -19.619 19.424 87.462 1.00 133.25 ? 953 TRP A CD2 1 ATOM 7154 N NE1 . TRP A 1 953 ? -21.022 21.168 87.402 1.00 131.63 ? 953 TRP A NE1 1 ATOM 7155 C CE2 . TRP A 1 953 ? -19.773 20.780 87.809 1.00 135.83 ? 953 TRP A CE2 1 ATOM 7156 C CE3 . TRP A 1 953 ? -18.416 18.781 87.772 1.00 133.99 ? 953 TRP A CE3 1 ATOM 7157 C CZ2 . TRP A 1 953 ? -18.770 21.505 88.452 1.00 132.14 ? 953 TRP A CZ2 1 ATOM 7158 C CZ3 . TRP A 1 953 ? -17.423 19.502 88.411 1.00 128.06 ? 953 TRP A CZ3 1 ATOM 7159 C CH2 . TRP A 1 953 ? -17.606 20.849 88.745 1.00 126.24 ? 953 TRP A CH2 1 ATOM 7160 N N . GLY A 1 954 ? -21.844 15.294 84.772 1.00 138.38 ? 954 GLY A N 1 ATOM 7161 C CA . GLY A 1 954 ? -21.929 13.872 84.487 1.00 141.59 ? 954 GLY A CA 1 ATOM 7162 C C . GLY A 1 954 ? -22.635 13.095 85.582 1.00 128.47 ? 954 GLY A C 1 ATOM 7163 O O . GLY A 1 954 ? -22.059 12.193 86.191 1.00 133.72 ? 954 GLY A O 1 ATOM 7164 N N . GLY B 2 1 ? -49.785 4.607 16.179 1.00 178.17 ? 1 GLY B N 1 ATOM 7165 C CA . GLY B 2 1 ? -50.905 5.507 15.972 1.00 184.82 ? 1 GLY B CA 1 ATOM 7166 C C . GLY B 2 1 ? -50.534 6.704 15.118 1.00 185.02 ? 1 GLY B C 1 ATOM 7167 O O . GLY B 2 1 ? -49.663 6.603 14.254 1.00 182.06 ? 1 GLY B O 1 ATOM 7168 N N . PRO B 2 2 ? -51.202 7.846 15.351 1.00 192.06 ? 2 PRO B N 1 ATOM 7169 C CA . PRO B 2 2 ? -50.929 9.093 14.625 1.00 199.31 ? 2 PRO B CA 1 ATOM 7170 C C . PRO B 2 2 ? -49.495 9.585 14.827 1.00 205.56 ? 2 PRO B C 1 ATOM 7171 O O . PRO B 2 2 ? -48.838 9.954 13.855 1.00 208.25 ? 2 PRO B O 1 ATOM 7172 C CB . PRO B 2 2 ? -51.940 10.078 15.225 1.00 195.70 ? 2 PRO B CB 1 ATOM 7173 C CG . PRO B 2 2 ? -52.315 9.494 16.547 1.00 192.67 ? 2 PRO B CG 1 ATOM 7174 C CD . PRO B 2 2 ? -52.266 8.012 16.355 1.00 193.41 ? 2 PRO B CD 1 ATOM 7175 N N . ASN B 2 3 ? -49.038 9.597 16.077 1.00 203.07 ? 3 ASN B N 1 ATOM 7176 C CA . ASN B 2 3 ? -47.636 9.838 16.422 1.00 193.17 ? 3 ASN B CA 1 ATOM 7177 C C . ASN B 2 3 ? -46.990 11.046 15.734 1.00 182.43 ? 3 ASN B C 1 ATOM 7178 O O . ASN B 2 3 ? -47.576 12.127 15.663 1.00 180.83 ? 3 ASN B O 1 ATOM 7179 C CB . ASN B 2 3 ? -46.816 8.580 16.116 1.00 195.81 ? 3 ASN B CB 1 ATOM 7180 C CG . ASN B 2 3 ? -45.583 8.459 16.991 1.00 202.70 ? 3 ASN B CG 1 ATOM 7181 O OD1 . ASN B 2 3 ? -44.506 8.940 16.636 1.00 204.13 ? 3 ASN B OD1 1 ATOM 7182 N ND2 . ASN B 2 3 ? -45.734 7.813 18.141 1.00 203.59 ? 3 ASN B ND2 1 ATOM 7183 N N . ILE B 2 4 ? -45.775 10.840 15.233 1.00 173.91 ? 4 ILE B N 1 ATOM 7184 C CA . ILE B 2 4 ? -44.991 11.879 14.573 1.00 175.09 ? 4 ILE B CA 1 ATOM 7185 C C . ILE B 2 4 ? -44.519 11.381 13.210 1.00 182.21 ? 4 ILE B C 1 ATOM 7186 O O . ILE B 2 4 ? -44.798 11.996 12.186 1.00 186.03 ? 4 ILE B O 1 ATOM 7187 C CB . ILE B 2 4 ? -43.770 12.319 15.411 1.00 161.48 ? 4 ILE B CB 1 ATOM 7188 C CG1 . ILE B 2 4 ? -44.215 13.034 16.690 1.00 159.31 ? 4 ILE B CG1 1 ATOM 7189 C CG2 . ILE B 2 4 ? -42.871 13.239 14.598 1.00 144.26 ? 4 ILE B CG2 1 ATOM 7190 C CD1 . ILE B 2 4 ? -44.436 12.116 17.877 1.00 158.09 ? 4 ILE B CD1 1 ATOM 7191 N N . CYS B 2 5 ? -43.757 10.291 13.214 1.00 181.26 ? 5 CYS B N 1 ATOM 7192 C CA . CYS B 2 5 ? -43.286 9.672 11.978 1.00 182.73 ? 5 CYS B CA 1 ATOM 7193 C C . CYS B 2 5 ? -44.417 9.455 10.973 1.00 189.01 ? 5 CYS B C 1 ATOM 7194 O O . CYS B 2 5 ? -44.251 9.712 9.780 1.00 192.05 ? 5 CYS B O 1 ATOM 7195 C CB . CYS B 2 5 ? -42.597 8.341 12.282 1.00 176.61 ? 5 CYS B CB 1 ATOM 7196 S SG . CYS B 2 5 ? -41.131 8.487 13.327 1.00 212.47 ? 5 CYS B SG 1 ATOM 7197 N N . THR B 2 6 ? -45.563 8.985 11.462 1.00 194.44 ? 6 THR B N 1 ATOM 7198 C CA . THR B 2 6 ? -46.735 8.761 10.617 1.00 198.87 ? 6 THR B CA 1 ATOM 7199 C C . THR B 2 6 ? -47.174 10.039 9.903 1.00 195.26 ? 6 THR B C 1 ATOM 7200 O O . THR B 2 6 ? -47.098 10.132 8.681 1.00 194.53 ? 6 THR B O 1 ATOM 7201 C CB . THR B 2 6 ? -47.923 8.216 11.431 1.00 199.14 ? 6 THR B CB 1 ATOM 7202 O OG1 . THR B 2 6 ? -47.497 7.102 12.224 1.00 197.27 ? 6 THR B OG1 1 ATOM 7203 C CG2 . THR B 2 6 ? -49.052 7.780 10.507 1.00 199.77 ? 6 THR B CG2 1 ATOM 7204 N N . THR B 2 7 ? -47.641 11.017 10.672 1.00 195.74 ? 7 THR B N 1 ATOM 7205 C CA . THR B 2 7 ? -48.034 12.308 10.115 1.00 200.79 ? 7 THR B CA 1 ATOM 7206 C C . THR B 2 7 ? -47.170 13.417 10.709 1.00 187.58 ? 7 THR B C 1 ATOM 7207 O O . THR B 2 7 ? -46.931 13.424 11.915 1.00 182.89 ? 7 THR B O 1 ATOM 7208 C CB . THR B 2 7 ? -49.522 12.609 10.371 1.00 209.52 ? 7 THR B CB 1 ATOM 7209 O OG1 . THR B 2 7 ? -49.810 12.463 11.766 1.00 215.60 ? 7 THR B OG1 1 ATOM 7210 C CG2 . THR B 2 7 ? -50.401 11.652 9.578 1.00 204.42 ? 7 THR B CG2 1 ATOM 7211 N N . ARG B 2 8 ? -46.784 14.366 9.848 1.00 179.58 ? 8 ARG B N 1 ATOM 7212 C CA . ARG B 2 8 ? -45.671 15.323 10.012 1.00 177.87 ? 8 ARG B CA 1 ATOM 7213 C C . ARG B 2 8 ? -44.378 14.689 9.504 1.00 185.19 ? 8 ARG B C 1 ATOM 7214 O O . ARG B 2 8 ? -43.341 15.347 9.420 1.00 173.78 ? 8 ARG B O 1 ATOM 7215 C CB . ARG B 2 8 ? -45.479 15.799 11.460 1.00 174.42 ? 8 ARG B CB 1 ATOM 7216 C CG . ARG B 2 8 ? -46.652 16.563 12.054 1.00 177.33 ? 8 ARG B CG 1 ATOM 7217 C CD . ARG B 2 8 ? -46.357 16.962 13.494 1.00 171.96 ? 8 ARG B CD 1 ATOM 7218 N NE . ARG B 2 8 ? -47.551 17.416 14.201 1.00 175.49 ? 8 ARG B NE 1 ATOM 7219 C CZ . ARG B 2 8 ? -48.332 16.626 14.932 1.00 175.85 ? 8 ARG B CZ 1 ATOM 7220 N NH1 . ARG B 2 8 ? -48.045 15.336 15.056 1.00 169.82 ? 8 ARG B NH1 1 ATOM 7221 N NH2 . ARG B 2 8 ? -49.399 17.124 15.541 1.00 179.48 ? 8 ARG B NH2 1 ATOM 7222 N N . GLY B 2 9 ? -44.450 13.405 9.170 1.00 199.55 ? 9 GLY B N 1 ATOM 7223 C CA . GLY B 2 9 ? -43.354 12.707 8.522 1.00 202.53 ? 9 GLY B CA 1 ATOM 7224 C C . GLY B 2 9 ? -43.629 12.586 7.036 1.00 201.86 ? 9 GLY B C 1 ATOM 7225 O O . GLY B 2 9 ? -44.253 13.464 6.449 1.00 210.42 ? 9 GLY B O 1 ATOM 7226 N N . VAL B 2 10 ? -43.165 11.493 6.433 1.00 190.35 ? 10 VAL B N 1 ATOM 7227 C CA . VAL B 2 10 ? -43.465 11.160 5.037 1.00 176.86 ? 10 VAL B CA 1 ATOM 7228 C C . VAL B 2 10 ? -43.012 12.225 4.037 1.00 171.02 ? 10 VAL B C 1 ATOM 7229 O O . VAL B 2 10 ? -43.829 12.946 3.463 1.00 169.18 ? 10 VAL B O 1 ATOM 7230 C CB . VAL B 2 10 ? -44.977 10.908 4.826 1.00 173.64 ? 10 VAL B CB 1 ATOM 7231 C CG1 . VAL B 2 10 ? -45.218 10.176 3.511 1.00 174.04 ? 10 VAL B CG1 1 ATOM 7232 C CG2 . VAL B 2 10 ? -45.545 10.108 5.978 1.00 173.55 ? 10 VAL B CG2 1 ATOM 7233 N N . SER B 2 11 ? -41.701 12.332 3.850 1.00 172.59 ? 11 SER B N 1 ATOM 7234 C CA . SER B 2 11 ? -41.144 13.159 2.786 1.00 173.35 ? 11 SER B CA 1 ATOM 7235 C C . SER B 2 11 ? -40.236 12.311 1.909 1.00 184.78 ? 11 SER B C 1 ATOM 7236 O O . SER B 2 11 ? -40.563 12.002 0.763 1.00 180.59 ? 11 SER B O 1 ATOM 7237 C CB . SER B 2 11 ? -40.367 14.342 3.361 1.00 159.12 ? 11 SER B CB 1 ATOM 7238 O OG . SER B 2 11 ? -39.881 15.178 2.327 1.00 154.15 ? 11 SER B OG 1 ATOM 7239 N N . SER B 2 12 ? -39.092 11.938 2.471 1.00 192.44 ? 12 SER B N 1 ATOM 7240 C CA . SER B 2 12 ? -38.150 11.046 1.813 1.00 190.97 ? 12 SER B CA 1 ATOM 7241 C C . SER B 2 12 ? -37.528 10.122 2.849 1.00 181.51 ? 12 SER B C 1 ATOM 7242 O O . SER B 2 12 ? -37.630 10.377 4.049 1.00 178.22 ? 12 SER B O 1 ATOM 7243 C CB . SER B 2 12 ? -37.065 11.837 1.082 1.00 188.02 ? 12 SER B CB 1 ATOM 7244 O OG . SER B 2 12 ? -36.134 10.968 0.461 1.00 188.95 ? 12 SER B OG 1 ATOM 7245 N N . CYS B 2 13 ? -36.893 9.052 2.383 1.00 173.40 ? 13 CYS B N 1 ATOM 7246 C CA . CYS B 2 13 ? -36.262 8.083 3.272 1.00 161.02 ? 13 CYS B CA 1 ATOM 7247 C C . CYS B 2 13 ? -35.244 8.747 4.192 1.00 157.44 ? 13 CYS B C 1 ATOM 7248 O O . CYS B 2 13 ? -35.269 8.548 5.406 1.00 154.33 ? 13 CYS B O 1 ATOM 7249 C CB . CYS B 2 13 ? -35.588 6.976 2.461 1.00 155.66 ? 13 CYS B CB 1 ATOM 7250 S SG . CYS B 2 13 ? -34.669 5.788 3.462 1.00 177.76 ? 13 CYS B SG 1 ATOM 7251 N N . GLN B 2 14 ? -34.357 9.541 3.605 1.00 161.55 ? 14 GLN B N 1 ATOM 7252 C CA . GLN B 2 14 ? -33.342 10.253 4.370 1.00 166.62 ? 14 GLN B CA 1 ATOM 7253 C C . GLN B 2 14 ? -33.976 11.323 5.252 1.00 170.19 ? 14 GLN B C 1 ATOM 7254 O O . GLN B 2 14 ? -33.544 11.547 6.383 1.00 169.68 ? 14 GLN B O 1 ATOM 7255 C CB . GLN B 2 14 ? -32.309 10.878 3.430 1.00 163.29 ? 14 GLN B CB 1 ATOM 7256 C CG . GLN B 2 14 ? -31.207 11.653 4.133 1.00 155.65 ? 14 GLN B CG 1 ATOM 7257 C CD . GLN B 2 14 ? -30.100 12.070 3.188 1.00 155.53 ? 14 GLN B CD 1 ATOM 7258 O OE1 . GLN B 2 14 ? -30.001 11.565 2.070 1.00 153.97 ? 14 GLN B OE1 1 ATOM 7259 N NE2 . GLN B 2 14 ? -29.258 12.998 3.632 1.00 157.66 ? 14 GLN B NE2 1 ATOM 7260 N N . GLN B 2 15 ? -35.010 11.975 4.730 1.00 170.31 ? 15 GLN B N 1 ATOM 7261 C CA . GLN B 2 15 ? -35.692 13.037 5.460 1.00 170.47 ? 15 GLN B CA 1 ATOM 7262 C C . GLN B 2 15 ? -36.548 12.470 6.587 1.00 153.00 ? 15 GLN B C 1 ATOM 7263 O O . GLN B 2 15 ? -36.942 13.190 7.504 1.00 150.41 ? 15 GLN B O 1 ATOM 7264 C CB . GLN B 2 15 ? -36.555 13.870 4.510 1.00 177.72 ? 15 GLN B CB 1 ATOM 7265 C CG . GLN B 2 15 ? -35.782 14.475 3.349 1.00 187.73 ? 15 GLN B CG 1 ATOM 7266 C CD . GLN B 2 15 ? -36.625 15.415 2.510 1.00 191.79 ? 15 GLN B CD 1 ATOM 7267 O OE1 . GLN B 2 15 ? -37.639 15.937 2.972 1.00 193.64 ? 15 GLN B OE1 1 ATOM 7268 N NE2 . GLN B 2 15 ? -36.208 15.635 1.268 1.00 189.45 ? 15 GLN B NE2 1 ATOM 7269 N N . CYS B 2 16 ? -36.831 11.175 6.512 1.00 144.72 ? 16 CYS B N 1 ATOM 7270 C CA . CYS B 2 16 ? -37.648 10.514 7.522 1.00 144.52 ? 16 CYS B CA 1 ATOM 7271 C C . CYS B 2 16 ? -36.852 10.189 8.782 1.00 143.95 ? 16 CYS B C 1 ATOM 7272 O O . CYS B 2 16 ? -37.347 10.345 9.899 1.00 145.37 ? 16 CYS B O 1 ATOM 7273 C CB . CYS B 2 16 ? -38.259 9.237 6.954 1.00 141.79 ? 16 CYS B CB 1 ATOM 7274 S SG . CYS B 2 16 ? -39.277 8.340 8.131 1.00 156.99 ? 16 CYS B SG 1 ATOM 7275 N N . LEU B 2 17 ? -35.619 9.730 8.596 1.00 137.93 ? 17 LEU B N 1 ATOM 7276 C CA . LEU B 2 17 ? -34.765 9.350 9.715 1.00 129.90 ? 17 LEU B CA 1 ATOM 7277 C C . LEU B 2 17 ? -34.326 10.565 10.519 1.00 129.08 ? 17 LEU B C 1 ATOM 7278 O O . LEU B 2 17 ? -34.086 10.470 11.723 1.00 133.09 ? 17 LEU B O 1 ATOM 7279 C CB . LEU B 2 17 ? -33.536 8.585 9.220 1.00 130.31 ? 17 LEU B CB 1 ATOM 7280 C CG . LEU B 2 17 ? -33.649 7.067 9.048 1.00 127.59 ? 17 LEU B CG 1 ATOM 7281 C CD1 . LEU B 2 17 ? -34.721 6.689 8.036 1.00 125.04 ? 17 LEU B CD1 1 ATOM 7282 C CD2 . LEU B 2 17 ? -32.302 6.486 8.646 1.00 128.94 ? 17 LEU B CD2 1 ATOM 7283 N N . ALA B 2 18 ? -34.234 11.708 9.846 1.00 131.83 ? 18 ALA B N 1 ATOM 7284 C CA . ALA B 2 18 ? -33.763 12.940 10.469 1.00 133.19 ? 18 ALA B CA 1 ATOM 7285 C C . ALA B 2 18 ? -34.793 13.519 11.435 1.00 135.08 ? 18 ALA B C 1 ATOM 7286 O O . ALA B 2 18 ? -34.512 14.479 12.154 1.00 131.81 ? 18 ALA B O 1 ATOM 7287 C CB . ALA B 2 18 ? -33.406 13.965 9.402 1.00 128.46 ? 18 ALA B CB 1 ATOM 7288 N N . VAL B 2 19 ? -35.983 12.928 11.452 1.00 136.72 ? 19 VAL B N 1 ATOM 7289 C CA . VAL B 2 19 ? -37.053 13.394 12.324 1.00 145.87 ? 19 VAL B CA 1 ATOM 7290 C C . VAL B 2 19 ? -36.788 13.003 13.773 1.00 148.32 ? 19 VAL B C 1 ATOM 7291 O O . VAL B 2 19 ? -36.566 13.862 14.626 1.00 149.47 ? 19 VAL B O 1 ATOM 7292 C CB . VAL B 2 19 ? -38.418 12.831 11.892 1.00 152.91 ? 19 VAL B CB 1 ATOM 7293 C CG1 . VAL B 2 19 ? -39.506 13.271 12.861 1.00 149.96 ? 19 VAL B CG1 1 ATOM 7294 C CG2 . VAL B 2 19 ? -38.747 13.276 10.476 1.00 166.92 ? 19 VAL B CG2 1 ATOM 7295 N N . SER B 2 20 ? -36.808 11.703 14.045 1.00 144.67 ? 20 SER B N 1 ATOM 7296 C CA . SER B 2 20 ? -36.616 11.209 15.402 1.00 145.16 ? 20 SER B CA 1 ATOM 7297 C C . SER B 2 20 ? -35.726 9.974 15.428 1.00 151.98 ? 20 SER B C 1 ATOM 7298 O O . SER B 2 20 ? -35.736 9.180 14.487 1.00 150.64 ? 20 SER B O 1 ATOM 7299 C CB . SER B 2 20 ? -37.969 10.893 16.046 1.00 138.66 ? 20 SER B CB 1 ATOM 7300 O OG . SER B 2 20 ? -37.804 10.296 17.320 1.00 130.80 ? 20 SER B OG 1 ATOM 7301 N N . PRO B 2 21 ? -34.941 9.818 16.507 1.00 150.35 ? 21 PRO B N 1 ATOM 7302 C CA . PRO B 2 21 ? -34.169 8.596 16.752 1.00 137.83 ? 21 PRO B CA 1 ATOM 7303 C C . PRO B 2 21 ? -35.054 7.358 16.676 1.00 135.63 ? 21 PRO B C 1 ATOM 7304 O O . PRO B 2 21 ? -34.618 6.317 16.187 1.00 141.74 ? 21 PRO B O 1 ATOM 7305 C CB . PRO B 2 21 ? -33.627 8.805 18.165 1.00 139.88 ? 21 PRO B CB 1 ATOM 7306 C CG . PRO B 2 21 ? -33.502 10.282 18.287 1.00 143.86 ? 21 PRO B CG 1 ATOM 7307 C CD . PRO B 2 21 ? -34.656 10.858 17.512 1.00 145.85 ? 21 PRO B CD 1 ATOM 7308 N N . MET B 2 22 ? -36.287 7.474 17.159 1.00 139.81 ? 22 MET B N 1 ATOM 7309 C CA . MET B 2 22 ? -37.273 6.428 16.935 1.00 156.87 ? 22 MET B CA 1 ATOM 7310 C C . MET B 2 22 ? -38.099 6.788 15.705 1.00 165.20 ? 22 MET B C 1 ATOM 7311 O O . MET B 2 22 ? -38.913 7.710 15.733 1.00 170.42 ? 22 MET B O 1 ATOM 7312 C CB . MET B 2 22 ? -38.167 6.235 18.165 1.00 156.39 ? 22 MET B CB 1 ATOM 7313 C CG . MET B 2 22 ? -38.687 7.523 18.787 1.00 156.71 ? 22 MET B CG 1 ATOM 7314 S SD . MET B 2 22 ? -39.873 7.219 20.110 1.00 195.91 ? 22 MET B SD 1 ATOM 7315 C CE . MET B 2 22 ? -41.110 6.260 19.241 1.00 169.50 ? 22 MET B CE 1 ATOM 7316 N N . CYS B 2 23 ? -37.885 6.026 14.637 1.00 161.92 ? 23 CYS B N 1 ATOM 7317 C CA . CYS B 2 23 ? -38.465 6.284 13.322 1.00 156.25 ? 23 CYS B CA 1 ATOM 7318 C C . CYS B 2 23 ? -38.006 5.181 12.380 1.00 154.59 ? 23 CYS B C 1 ATOM 7319 O O . CYS B 2 23 ? -37.033 4.487 12.668 1.00 159.55 ? 23 CYS B O 1 ATOM 7320 C CB . CYS B 2 23 ? -38.034 7.650 12.772 1.00 161.14 ? 23 CYS B CB 1 ATOM 7321 S SG . CYS B 2 23 ? -39.195 9.019 13.028 1.00 175.72 ? 23 CYS B SG 1 ATOM 7322 N N . ALA B 2 24 ? -38.689 5.025 11.253 1.00 154.58 ? 24 ALA B N 1 ATOM 7323 C CA . ALA B 2 24 ? -38.256 4.058 10.252 1.00 158.70 ? 24 ALA B CA 1 ATOM 7324 C C . ALA B 2 24 ? -38.786 4.413 8.869 1.00 171.16 ? 24 ALA B C 1 ATOM 7325 O O . ALA B 2 24 ? -39.564 5.351 8.714 1.00 174.79 ? 24 ALA B O 1 ATOM 7326 C CB . ALA B 2 24 ? -38.701 2.656 10.643 1.00 158.45 ? 24 ALA B CB 1 ATOM 7327 N N . TRP B 2 25 ? -38.373 3.639 7.872 1.00 172.75 ? 25 TRP B N 1 ATOM 7328 C CA . TRP B 2 25 ? -38.824 3.841 6.503 1.00 166.14 ? 25 TRP B CA 1 ATOM 7329 C C . TRP B 2 25 ? -39.187 2.484 5.912 1.00 155.74 ? 25 TRP B C 1 ATOM 7330 O O . TRP B 2 25 ? -38.986 1.455 6.557 1.00 148.80 ? 25 TRP B O 1 ATOM 7331 C CB . TRP B 2 25 ? -37.733 4.536 5.679 1.00 160.66 ? 25 TRP B CB 1 ATOM 7332 C CG . TRP B 2 25 ? -38.137 4.903 4.284 1.00 168.90 ? 25 TRP B CG 1 ATOM 7333 C CD1 . TRP B 2 25 ? -37.785 4.259 3.134 1.00 173.06 ? 25 TRP B CD1 1 ATOM 7334 C CD2 . TRP B 2 25 ? -38.974 5.996 3.892 1.00 180.10 ? 25 TRP B CD2 1 ATOM 7335 N NE1 . TRP B 2 25 ? -38.348 4.885 2.050 1.00 177.82 ? 25 TRP B NE1 1 ATOM 7336 C CE2 . TRP B 2 25 ? -39.083 5.955 2.488 1.00 182.34 ? 25 TRP B CE2 1 ATOM 7337 C CE3 . TRP B 2 25 ? -39.640 7.008 4.590 1.00 185.03 ? 25 TRP B CE3 1 ATOM 7338 C CZ2 . TRP B 2 25 ? -39.831 6.885 1.769 1.00 188.36 ? 25 TRP B CZ2 1 ATOM 7339 C CZ3 . TRP B 2 25 ? -40.382 7.930 3.875 1.00 185.90 ? 25 TRP B CZ3 1 ATOM 7340 C CH2 . TRP B 2 25 ? -40.472 7.862 2.480 1.00 187.61 ? 25 TRP B CH2 1 ATOM 7341 N N . CYS B 2 26 ? -39.723 2.472 4.697 1.00 153.52 ? 26 CYS B N 1 ATOM 7342 C CA . CYS B 2 26 ? -40.057 1.210 4.053 1.00 162.13 ? 26 CYS B CA 1 ATOM 7343 C C . CYS B 2 26 ? -40.021 1.272 2.529 1.00 168.76 ? 26 CYS B C 1 ATOM 7344 O O . CYS B 2 26 ? -40.394 2.279 1.927 1.00 174.16 ? 26 CYS B O 1 ATOM 7345 C CB . CYS B 2 26 ? -41.442 0.745 4.511 1.00 167.86 ? 26 CYS B CB 1 ATOM 7346 S SG . CYS B 2 26 ? -41.948 -0.853 3.841 1.00 197.72 ? 26 CYS B SG 1 ATOM 7347 N N . SER B 2 27 ? -39.555 0.188 1.917 1.00 175.14 ? 27 SER B N 1 ATOM 7348 C CA . SER B 2 27 ? -39.842 -0.090 0.516 1.00 179.65 ? 27 SER B CA 1 ATOM 7349 C C . SER B 2 27 ? -40.547 -1.442 0.465 1.00 192.75 ? 27 SER B C 1 ATOM 7350 O O . SER B 2 27 ? -39.927 -2.482 0.681 1.00 195.07 ? 27 SER B O 1 ATOM 7351 C CB . SER B 2 27 ? -38.564 -0.091 -0.325 1.00 167.73 ? 27 SER B CB 1 ATOM 7352 O OG . SER B 2 27 ? -37.578 -0.936 0.242 1.00 159.58 ? 27 SER B OG 1 ATOM 7353 N N . ASP B 2 28 ? -41.842 -1.423 0.168 1.00 199.59 ? 28 ASP B N 1 ATOM 7354 C CA . ASP B 2 28 ? -42.694 -2.590 0.388 1.00 213.86 ? 28 ASP B CA 1 ATOM 7355 C C . ASP B 2 28 ? -42.920 -3.464 -0.842 1.00 220.45 ? 28 ASP B C 1 ATOM 7356 O O . ASP B 2 28 ? -43.692 -4.423 -0.781 1.00 222.34 ? 28 ASP B O 1 ATOM 7357 C CB . ASP B 2 28 ? -44.049 -2.142 0.941 1.00 222.95 ? 28 ASP B CB 1 ATOM 7358 C CG . ASP B 2 28 ? -44.666 -1.021 0.134 1.00 225.85 ? 28 ASP B CG 1 ATOM 7359 O OD1 . ASP B 2 28 ? -43.950 -0.415 -0.690 1.00 226.37 ? 28 ASP B OD1 1 ATOM 7360 O OD2 . ASP B 2 28 ? -45.865 -0.739 0.332 1.00 225.12 ? 28 ASP B OD2 1 ATOM 7361 N N . GLU B 2 29 ? -42.279 -3.107 -1.955 1.00 214.34 ? 29 GLU B N 1 ATOM 7362 C CA . GLU B 2 29 ? -42.384 -3.841 -3.224 1.00 212.65 ? 29 GLU B CA 1 ATOM 7363 C C . GLU B 2 29 ? -43.777 -3.728 -3.851 1.00 201.49 ? 29 GLU B C 1 ATOM 7364 O O . GLU B 2 29 ? -43.977 -4.107 -5.005 1.00 207.18 ? 29 GLU B O 1 ATOM 7365 C CB . GLU B 2 29 ? -42.025 -5.321 -3.036 1.00 217.85 ? 29 GLU B CB 1 ATOM 7366 C CG . GLU B 2 29 ? -40.708 -5.576 -2.321 1.00 216.97 ? 29 GLU B CG 1 ATOM 7367 C CD . GLU B 2 29 ? -40.763 -6.809 -1.438 1.00 218.42 ? 29 GLU B CD 1 ATOM 7368 O OE1 . GLU B 2 29 ? -41.633 -6.861 -0.543 1.00 219.76 ? 29 GLU B OE1 1 ATOM 7369 O OE2 . GLU B 2 29 ? -39.942 -7.728 -1.642 1.00 217.71 ? 29 GLU B OE2 1 ATOM 7370 N N . ALA B 2 30 ? -44.734 -3.206 -3.090 1.00 189.94 ? 30 ALA B N 1 ATOM 7371 C CA . ALA B 2 30 ? -46.104 -3.050 -3.559 1.00 196.72 ? 30 ALA B CA 1 ATOM 7372 C C . ALA B 2 30 ? -46.539 -1.597 -3.435 1.00 201.24 ? 30 ALA B C 1 ATOM 7373 O O . ALA B 2 30 ? -45.755 -0.743 -3.020 1.00 193.91 ? 30 ALA B O 1 ATOM 7374 C CB . ALA B 2 30 ? -47.042 -3.956 -2.777 1.00 190.95 ? 30 ALA B CB 1 ATOM 7375 N N . LEU B 2 31 ? -47.788 -1.314 -3.790 1.00 214.42 ? 31 LEU B N 1 ATOM 7376 C CA . LEU B 2 31 ? -48.304 0.047 -3.671 1.00 220.37 ? 31 LEU B CA 1 ATOM 7377 C C . LEU B 2 31 ? -49.642 0.159 -2.928 1.00 227.02 ? 31 LEU B C 1 ATOM 7378 O O . LEU B 2 31 ? -50.631 0.612 -3.506 1.00 231.99 ? 31 LEU B O 1 ATOM 7379 C CB . LEU B 2 31 ? -48.449 0.669 -5.062 1.00 220.99 ? 31 LEU B CB 1 ATOM 7380 C CG . LEU B 2 31 ? -47.574 1.889 -5.359 1.00 217.15 ? 31 LEU B CG 1 ATOM 7381 C CD1 . LEU B 2 31 ? -47.792 2.367 -6.786 1.00 219.31 ? 31 LEU B CD1 1 ATOM 7382 C CD2 . LEU B 2 31 ? -47.854 3.007 -4.366 1.00 208.33 ? 31 LEU B CD2 1 ATOM 7383 N N . PRO B 2 32 ? -49.682 -0.249 -1.646 1.00 219.40 ? 32 PRO B N 1 ATOM 7384 C CA . PRO B 2 32 ? -50.852 0.088 -0.833 1.00 216.11 ? 32 PRO B CA 1 ATOM 7385 C C . PRO B 2 32 ? -50.699 1.494 -0.265 1.00 213.17 ? 32 PRO B C 1 ATOM 7386 O O . PRO B 2 32 ? -50.236 1.628 0.868 1.00 211.36 ? 32 PRO B O 1 ATOM 7387 C CB . PRO B 2 32 ? -50.832 -0.971 0.269 1.00 204.57 ? 32 PRO B CB 1 ATOM 7388 C CG . PRO B 2 32 ? -49.388 -1.290 0.440 1.00 195.94 ? 32 PRO B CG 1 ATOM 7389 C CD . PRO B 2 32 ? -48.733 -1.103 -0.906 1.00 202.45 ? 32 PRO B CD 1 ATOM 7390 N N . LEU B 2 33 ? -51.071 2.511 -1.043 1.00 212.44 ? 33 LEU B N 1 ATOM 7391 C CA . LEU B 2 33 ? -50.706 3.895 -0.742 1.00 211.97 ? 33 LEU B CA 1 ATOM 7392 C C . LEU B 2 33 ? -51.003 4.265 0.705 1.00 210.18 ? 33 LEU B C 1 ATOM 7393 O O . LEU B 2 33 ? -50.093 4.687 1.417 1.00 204.40 ? 33 LEU B O 1 ATOM 7394 C CB . LEU B 2 33 ? -51.431 4.859 -1.684 1.00 215.05 ? 33 LEU B CB 1 ATOM 7395 C CG . LEU B 2 33 ? -51.096 6.343 -1.511 1.00 208.82 ? 33 LEU B CG 1 ATOM 7396 C CD1 . LEU B 2 33 ? -49.602 6.583 -1.677 1.00 196.49 ? 33 LEU B CD1 1 ATOM 7397 C CD2 . LEU B 2 33 ? -51.891 7.192 -2.490 1.00 211.03 ? 33 LEU B CD2 1 ATOM 7398 N N . GLY B 2 34 ? -52.265 4.130 1.119 1.00 206.13 ? 34 GLY B N 1 ATOM 7399 C CA . GLY B 2 34 ? -52.629 4.028 2.526 1.00 199.78 ? 34 GLY B CA 1 ATOM 7400 C C . GLY B 2 34 ? -51.918 5.031 3.408 1.00 200.10 ? 34 GLY B C 1 ATOM 7401 O O . GLY B 2 34 ? -51.875 6.224 3.105 1.00 200.93 ? 34 GLY B O 1 ATOM 7402 N N . SER B 2 35 ? -51.363 4.542 4.513 1.00 206.88 ? 35 SER B N 1 ATOM 7403 C CA . SER B 2 35 ? -50.229 5.212 5.134 1.00 215.27 ? 35 SER B CA 1 ATOM 7404 C C . SER B 2 35 ? -49.184 4.245 5.711 1.00 205.95 ? 35 SER B C 1 ATOM 7405 O O . SER B 2 35 ? -48.899 4.305 6.908 1.00 200.89 ? 35 SER B O 1 ATOM 7406 C CB . SER B 2 35 ? -50.717 6.150 6.240 1.00 219.04 ? 35 SER B CB 1 ATOM 7407 O OG . SER B 2 35 ? -51.408 5.435 7.249 1.00 222.42 ? 35 SER B OG 1 ATOM 7408 N N . PRO B 2 36 ? -48.611 3.346 4.882 1.00 198.41 ? 36 PRO B N 1 ATOM 7409 C CA . PRO B 2 36 ? -47.426 2.670 5.421 1.00 192.72 ? 36 PRO B CA 1 ATOM 7410 C C . PRO B 2 36 ? -46.279 3.658 5.600 1.00 193.19 ? 36 PRO B C 1 ATOM 7411 O O . PRO B 2 36 ? -45.699 3.742 6.682 1.00 200.48 ? 36 PRO B O 1 ATOM 7412 C CB . PRO B 2 36 ? -47.094 1.623 4.351 1.00 187.38 ? 36 PRO B CB 1 ATOM 7413 C CG . PRO B 2 36 ? -48.361 1.438 3.585 1.00 179.20 ? 36 PRO B CG 1 ATOM 7414 C CD . PRO B 2 36 ? -49.019 2.781 3.586 1.00 186.74 ? 36 PRO B CD 1 ATOM 7415 N N . ARG B 2 37 ? -45.983 4.389 4.525 1.00 190.66 ? 37 ARG B N 1 ATOM 7416 C CA . ARG B 2 37 ? -45.171 5.607 4.543 1.00 182.58 ? 37 ARG B CA 1 ATOM 7417 C C . ARG B 2 37 ? -43.936 5.532 5.441 1.00 177.11 ? 37 ARG B C 1 ATOM 7418 O O . ARG B 2 37 ? -43.137 4.600 5.348 1.00 170.98 ? 37 ARG B O 1 ATOM 7419 C CB . ARG B 2 37 ? -46.052 6.789 4.947 1.00 178.85 ? 37 ARG B CB 1 ATOM 7420 C CG . ARG B 2 37 ? -47.237 6.984 4.010 1.00 189.45 ? 37 ARG B CG 1 ATOM 7421 C CD . ARG B 2 37 ? -48.122 8.148 4.420 1.00 192.88 ? 37 ARG B CD 1 ATOM 7422 N NE . ARG B 2 37 ? -49.314 8.239 3.580 1.00 198.85 ? 37 ARG B NE 1 ATOM 7423 C CZ . ARG B 2 37 ? -49.360 8.868 2.410 1.00 194.31 ? 37 ARG B CZ 1 ATOM 7424 N NH1 . ARG B 2 37 ? -48.277 9.466 1.933 1.00 192.31 ? 37 ARG B NH1 1 ATOM 7425 N NH2 . ARG B 2 37 ? -50.490 8.898 1.715 1.00 188.44 ? 37 ARG B NH2 1 ATOM 7426 N N . CYS B 2 38 ? -43.793 6.532 6.304 1.00 182.69 ? 38 CYS B N 1 ATOM 7427 C CA . CYS B 2 38 ? -42.779 6.522 7.350 1.00 182.65 ? 38 CYS B CA 1 ATOM 7428 C C . CYS B 2 38 ? -43.450 6.334 8.703 1.00 187.54 ? 38 CYS B C 1 ATOM 7429 O O . CYS B 2 38 ? -44.405 7.038 9.027 1.00 190.80 ? 38 CYS B O 1 ATOM 7430 C CB . CYS B 2 38 ? -41.968 7.817 7.337 1.00 170.36 ? 38 CYS B CB 1 ATOM 7431 S SG . CYS B 2 38 ? -41.145 8.174 8.905 1.00 167.08 ? 38 CYS B SG 1 ATOM 7432 N N . ASP B 2 39 ? -42.959 5.385 9.493 1.00 187.17 ? 39 ASP B N 1 ATOM 7433 C CA . ASP B 2 39 ? -43.591 5.090 10.772 1.00 184.57 ? 39 ASP B CA 1 ATOM 7434 C C . ASP B 2 39 ? -42.647 4.413 11.756 1.00 181.65 ? 39 ASP B C 1 ATOM 7435 O O . ASP B 2 39 ? -41.477 4.177 11.456 1.00 175.23 ? 39 ASP B O 1 ATOM 7436 C CB . ASP B 2 39 ? -44.823 4.208 10.557 1.00 191.22 ? 39 ASP B CB 1 ATOM 7437 C CG . ASP B 2 39 ? -45.999 4.637 11.408 1.00 196.94 ? 39 ASP B CG 1 ATOM 7438 O OD1 . ASP B 2 39 ? -45.919 4.507 12.646 1.00 195.63 ? 39 ASP B OD1 1 ATOM 7439 O OD2 . ASP B 2 39 ? -47.007 5.103 10.837 1.00 203.12 ? 39 ASP B OD2 1 ATOM 7440 N N . LEU B 2 40 ? -43.174 4.110 12.938 1.00 180.61 ? 40 LEU B N 1 ATOM 7441 C CA . LEU B 2 40 ? -42.434 3.381 13.960 1.00 169.08 ? 40 LEU B CA 1 ATOM 7442 C C . LEU B 2 40 ? -42.329 1.907 13.590 1.00 156.85 ? 40 LEU B C 1 ATOM 7443 O O . LEU B 2 40 ? -43.095 1.413 12.762 1.00 154.73 ? 40 LEU B O 1 ATOM 7444 C CB . LEU B 2 40 ? -43.102 3.528 15.331 1.00 162.62 ? 40 LEU B CB 1 ATOM 7445 C CG . LEU B 2 40 ? -43.305 4.933 15.911 1.00 156.89 ? 40 LEU B CG 1 ATOM 7446 C CD1 . LEU B 2 40 ? -42.104 5.825 15.625 1.00 155.89 ? 40 LEU B CD1 1 ATOM 7447 C CD2 . LEU B 2 40 ? -44.596 5.568 15.409 1.00 153.28 ? 40 LEU B CD2 1 ATOM 7448 N N . LYS B 2 41 ? -41.371 1.214 14.196 1.00 151.65 ? 41 LYS B N 1 ATOM 7449 C CA . LYS B 2 41 ? -41.223 -0.223 14.004 1.00 152.68 ? 41 LYS B CA 1 ATOM 7450 C C . LYS B 2 41 ? -42.512 -0.960 14.347 1.00 166.65 ? 41 LYS B C 1 ATOM 7451 O O . LYS B 2 41 ? -43.159 -1.524 13.468 1.00 177.99 ? 41 LYS B O 1 ATOM 7452 C CB . LYS B 2 41 ? -40.069 -0.761 14.853 1.00 150.86 ? 41 LYS B CB 1 ATOM 7453 C CG . LYS B 2 41 ? -38.721 -0.747 14.153 1.00 146.77 ? 41 LYS B CG 1 ATOM 7454 C CD . LYS B 2 41 ? -38.504 -2.023 13.354 1.00 142.02 ? 41 LYS B CD 1 ATOM 7455 C CE . LYS B 2 41 ? -38.478 -3.238 14.269 1.00 143.48 ? 41 LYS B CE 1 ATOM 7456 N NZ . LYS B 2 41 ? -38.196 -4.500 13.531 1.00 143.75 ? 41 LYS B NZ 1 ATOM 7457 N N . GLU B 2 42 ? -42.886 -0.926 15.624 1.00 173.54 ? 42 GLU B N 1 ATOM 7458 C CA . GLU B 2 42 ? -44.054 -1.646 16.136 1.00 185.70 ? 42 GLU B CA 1 ATOM 7459 C C . GLU B 2 42 ? -45.339 -1.374 15.352 1.00 192.31 ? 42 GLU B C 1 ATOM 7460 O O . GLU B 2 42 ? -46.192 -2.252 15.223 1.00 192.65 ? 42 GLU B O 1 ATOM 7461 C CB . GLU B 2 42 ? -44.270 -1.302 17.610 1.00 186.93 ? 42 GLU B CB 1 ATOM 7462 C CG . GLU B 2 42 ? -44.208 0.185 17.914 1.00 184.10 ? 42 GLU B CG 1 ATOM 7463 C CD . GLU B 2 42 ? -44.438 0.488 19.380 1.00 182.90 ? 42 GLU B CD 1 ATOM 7464 O OE1 . GLU B 2 42 ? -45.138 -0.302 20.049 1.00 188.48 ? 42 GLU B OE1 1 ATOM 7465 O OE2 . GLU B 2 42 ? -43.915 1.513 19.865 1.00 170.10 ? 42 GLU B OE2 1 ATOM 7466 N N . ASN B 2 43 ? -45.469 -0.159 14.828 1.00 191.98 ? 43 ASN B N 1 ATOM 7467 C CA . ASN B 2 43 ? -46.614 0.197 13.996 1.00 191.00 ? 43 ASN B CA 1 ATOM 7468 C C . ASN B 2 43 ? -46.497 -0.437 12.617 1.00 188.86 ? 43 ASN B C 1 ATOM 7469 O O . ASN B 2 43 ? -47.351 -1.226 12.211 1.00 197.80 ? 43 ASN B O 1 ATOM 7470 C CB . ASN B 2 43 ? -46.746 1.715 13.872 1.00 178.58 ? 43 ASN B CB 1 ATOM 7471 C CG . ASN B 2 43 ? -47.409 2.344 15.082 1.00 177.55 ? 43 ASN B CG 1 ATOM 7472 O OD1 . ASN B 2 43 ? -48.634 2.449 15.148 1.00 183.69 ? 43 ASN B OD1 1 ATOM 7473 N ND2 . ASN B 2 43 ? -46.601 2.769 16.046 1.00 176.26 ? 43 ASN B ND2 1 ATOM 7474 N N . LEU B 2 44 ? -45.439 -0.072 11.898 1.00 170.06 ? 44 LEU B N 1 ATOM 7475 C CA . LEU B 2 44 ? -45.150 -0.633 10.581 1.00 165.66 ? 44 LEU B CA 1 ATOM 7476 C C . LEU B 2 44 ? -45.082 -2.162 10.618 1.00 156.99 ? 44 LEU B C 1 ATOM 7477 O O . LEU B 2 44 ? -45.333 -2.824 9.615 1.00 154.96 ? 44 LEU B O 1 ATOM 7478 C CB . LEU B 2 44 ? -43.832 -0.058 10.049 1.00 173.44 ? 44 LEU B CB 1 ATOM 7479 C CG . LEU B 2 44 ? -43.665 0.206 8.549 1.00 180.27 ? 44 LEU B CG 1 ATOM 7480 C CD1 . LEU B 2 44 ? -42.526 1.189 8.318 1.00 165.23 ? 44 LEU B CD1 1 ATOM 7481 C CD2 . LEU B 2 44 ? -43.418 -1.082 7.777 1.00 177.13 ? 44 LEU B CD2 1 ATOM 7482 N N . LEU B 2 45 ? -44.758 -2.715 11.784 1.00 150.82 ? 45 LEU B N 1 ATOM 7483 C CA . LEU B 2 45 ? -44.642 -4.161 11.956 1.00 150.68 ? 45 LEU B CA 1 ATOM 7484 C C . LEU B 2 45 ? -45.965 -4.895 11.745 1.00 176.98 ? 45 LEU B C 1 ATOM 7485 O O . LEU B 2 45 ? -46.014 -5.896 11.030 1.00 190.96 ? 45 LEU B O 1 ATOM 7486 C CB . LEU B 2 45 ? -44.094 -4.482 13.348 1.00 141.55 ? 45 LEU B CB 1 ATOM 7487 C CG . LEU B 2 45 ? -42.644 -4.967 13.430 1.00 142.47 ? 45 LEU B CG 1 ATOM 7488 C CD1 . LEU B 2 45 ? -41.734 -4.169 12.507 1.00 129.37 ? 45 LEU B CD1 1 ATOM 7489 C CD2 . LEU B 2 45 ? -42.145 -4.894 14.866 1.00 138.57 ? 45 LEU B CD2 1 ATOM 7490 N N . LYS B 2 46 ? -47.034 -4.398 12.361 1.00 184.22 ? 46 LYS B N 1 ATOM 7491 C CA . LYS B 2 46 ? -48.335 -5.056 12.272 1.00 198.71 ? 46 LYS B CA 1 ATOM 7492 C C . LYS B 2 46 ? -49.035 -4.671 10.971 1.00 199.23 ? 46 LYS B C 1 ATOM 7493 O O . LYS B 2 46 ? -50.116 -5.166 10.653 1.00 210.78 ? 46 LYS B O 1 ATOM 7494 C CB . LYS B 2 46 ? -49.206 -4.699 13.481 1.00 202.43 ? 46 LYS B CB 1 ATOM 7495 C CG . LYS B 2 46 ? -50.351 -5.675 13.753 1.00 215.83 ? 46 LYS B CG 1 ATOM 7496 C CD . LYS B 2 46 ? -50.030 -6.641 14.894 1.00 213.99 ? 46 LYS B CD 1 ATOM 7497 C CE . LYS B 2 46 ? -49.011 -7.699 14.490 1.00 205.05 ? 46 LYS B CE 1 ATOM 7498 N NZ . LYS B 2 46 ? -48.659 -8.598 15.624 1.00 197.79 ? 46 LYS B NZ 1 ATOM 7499 N N . ASP B 2 47 ? -48.391 -3.784 10.222 1.00 181.82 ? 47 ASP B N 1 ATOM 7500 C CA . ASP B 2 47 ? -48.825 -3.406 8.885 1.00 178.82 ? 47 ASP B CA 1 ATOM 7501 C C . ASP B 2 47 ? -48.166 -4.323 7.862 1.00 177.89 ? 47 ASP B C 1 ATOM 7502 O O . ASP B 2 47 ? -48.229 -4.073 6.658 1.00 179.78 ? 47 ASP B O 1 ATOM 7503 C CB . ASP B 2 47 ? -48.492 -1.942 8.597 1.00 176.62 ? 47 ASP B CB 1 ATOM 7504 C CG . ASP B 2 47 ? -49.253 -0.987 9.495 1.00 178.63 ? 47 ASP B CG 1 ATOM 7505 O OD1 . ASP B 2 47 ? -50.397 -1.313 9.876 1.00 174.18 ? 47 ASP B OD1 1 ATOM 7506 O OD2 . ASP B 2 47 ? -48.707 0.088 9.820 1.00 188.97 ? 47 ASP B OD2 1 ATOM 7507 N N . ASN B 2 48 ? -47.515 -5.366 8.375 1.00 183.86 ? 48 ASN B N 1 ATOM 7508 C CA . ASN B 2 48 ? -46.644 -6.255 7.607 1.00 180.37 ? 48 ASN B CA 1 ATOM 7509 C C . ASN B 2 48 ? -45.441 -5.492 7.077 1.00 177.99 ? 48 ASN B C 1 ATOM 7510 O O . ASN B 2 48 ? -44.800 -4.755 7.824 1.00 174.43 ? 48 ASN B O 1 ATOM 7511 C CB . ASN B 2 48 ? -47.401 -6.923 6.453 1.00 162.78 ? 48 ASN B CB 1 ATOM 7512 C CG . ASN B 2 48 ? -48.602 -7.715 6.923 1.00 160.27 ? 48 ASN B CG 1 ATOM 7513 O OD1 . ASN B 2 48 ? -49.099 -7.512 8.030 1.00 156.85 ? 48 ASN B OD1 1 ATOM 7514 N ND2 . ASN B 2 48 ? -49.078 -8.623 6.080 1.00 179.11 ? 48 ASN B ND2 1 ATOM 7515 N N . CYS B 2 49 ? -45.143 -5.672 5.794 1.00 180.16 ? 49 CYS B N 1 ATOM 7516 C CA . CYS B 2 49 ? -43.997 -5.024 5.165 1.00 181.56 ? 49 CYS B CA 1 ATOM 7517 C C . CYS B 2 49 ? -42.710 -5.252 5.960 1.00 188.77 ? 49 CYS B C 1 ATOM 7518 O O . CYS B 2 49 ? -42.125 -4.311 6.497 1.00 184.99 ? 49 CYS B O 1 ATOM 7519 C CB . CYS B 2 49 ? -44.262 -3.523 5.003 1.00 181.31 ? 49 CYS B CB 1 ATOM 7520 S SG . CYS B 2 49 ? -42.939 -2.588 4.197 1.00 226.90 ? 49 CYS B SG 1 ATOM 7521 N N . ALA B 2 50 ? -42.287 -6.507 6.065 1.00 189.99 ? 50 ALA B N 1 ATOM 7522 C CA . ALA B 2 50 ? -40.979 -6.794 6.640 1.00 184.04 ? 50 ALA B CA 1 ATOM 7523 C C . ALA B 2 50 ? -40.211 -7.913 5.927 1.00 199.43 ? 50 ALA B C 1 ATOM 7524 O O . ALA B 2 50 ? -39.878 -8.923 6.547 1.00 203.28 ? 50 ALA B O 1 ATOM 7525 C CB . ALA B 2 50 ? -41.130 -7.134 8.117 1.00 172.14 ? 50 ALA B CB 1 ATOM 7526 N N . PRO B 2 51 ? -39.924 -7.743 4.624 1.00 209.73 ? 51 PRO B N 1 ATOM 7527 C CA . PRO B 2 51 ? -38.869 -8.580 4.051 1.00 209.60 ? 51 PRO B CA 1 ATOM 7528 C C . PRO B 2 51 ? -37.540 -7.839 4.122 1.00 200.64 ? 51 PRO B C 1 ATOM 7529 O O . PRO B 2 51 ? -36.926 -7.600 3.080 1.00 203.46 ? 51 PRO B O 1 ATOM 7530 C CB . PRO B 2 51 ? -39.326 -8.775 2.608 1.00 211.99 ? 51 PRO B CB 1 ATOM 7531 C CG . PRO B 2 51 ? -40.029 -7.500 2.289 1.00 213.50 ? 51 PRO B CG 1 ATOM 7532 C CD . PRO B 2 51 ? -40.672 -7.027 3.574 1.00 211.34 ? 51 PRO B CD 1 ATOM 7533 N N . GLU B 2 52 ? -37.137 -7.463 5.338 1.00 192.60 ? 52 GLU B N 1 ATOM 7534 C CA . GLU B 2 52 ? -35.997 -6.573 5.587 1.00 186.82 ? 52 GLU B CA 1 ATOM 7535 C C . GLU B 2 52 ? -36.292 -5.149 5.111 1.00 180.23 ? 52 GLU B C 1 ATOM 7536 O O . GLU B 2 52 ? -35.456 -4.256 5.255 1.00 180.90 ? 52 GLU B O 1 ATOM 7537 C CB . GLU B 2 52 ? -34.716 -7.099 4.929 1.00 193.24 ? 52 GLU B CB 1 ATOM 7538 C CG . GLU B 2 52 ? -34.277 -8.467 5.423 1.00 202.55 ? 52 GLU B CG 1 ATOM 7539 C CD . GLU B 2 52 ? -33.019 -8.955 4.732 1.00 206.58 ? 52 GLU B CD 1 ATOM 7540 O OE1 . GLU B 2 52 ? -32.484 -8.216 3.878 1.00 207.73 ? 52 GLU B OE1 1 ATOM 7541 O OE2 . GLU B 2 52 ? -32.565 -10.077 5.041 1.00 203.92 ? 52 GLU B OE2 1 ATOM 7542 N N . SER B 2 53 ? -37.476 -4.955 4.534 1.00 182.95 ? 53 SER B N 1 ATOM 7543 C CA . SER B 2 53 ? -37.915 -3.659 4.020 1.00 188.23 ? 53 SER B CA 1 ATOM 7544 C C . SER B 2 53 ? -37.774 -2.541 5.043 1.00 195.21 ? 53 SER B C 1 ATOM 7545 O O . SER B 2 53 ? -37.365 -1.430 4.705 1.00 192.53 ? 53 SER B O 1 ATOM 7546 C CB . SER B 2 53 ? -39.370 -3.742 3.558 1.00 185.96 ? 53 SER B CB 1 ATOM 7547 O OG . SER B 2 53 ? -39.886 -2.454 3.270 1.00 189.34 ? 53 SER B OG 1 ATOM 7548 N N . ILE B 2 54 ? -38.126 -2.837 6.290 1.00 200.79 ? 54 ILE B N 1 ATOM 7549 C CA . ILE B 2 54 ? -37.984 -1.867 7.365 1.00 197.60 ? 54 ILE B CA 1 ATOM 7550 C C . ILE B 2 54 ? -36.520 -1.480 7.543 1.00 190.15 ? 54 ILE B C 1 ATOM 7551 O O . ILE B 2 54 ? -35.652 -2.339 7.703 1.00 189.94 ? 54 ILE B O 1 ATOM 7552 C CB . ILE B 2 54 ? -38.541 -2.408 8.700 1.00 194.19 ? 54 ILE B CB 1 ATOM 7553 C CG1 . ILE B 2 54 ? -38.103 -3.858 8.917 1.00 192.57 ? 54 ILE B CG1 1 ATOM 7554 C CG2 . ILE B 2 54 ? -40.057 -2.313 8.722 1.00 196.13 ? 54 ILE B CG2 1 ATOM 7555 C CD1 . ILE B 2 54 ? -38.593 -4.457 10.216 1.00 192.57 ? 54 ILE B CD1 1 ATOM 7556 N N . GLU B 2 55 ? -36.248 -0.182 7.498 1.00 181.50 ? 55 GLU B N 1 ATOM 7557 C CA . GLU B 2 55 ? -34.902 0.307 7.748 1.00 182.04 ? 55 GLU B CA 1 ATOM 7558 C C . GLU B 2 55 ? -34.892 1.052 9.073 1.00 186.75 ? 55 GLU B C 1 ATOM 7559 O O . GLU B 2 55 ? -35.427 2.155 9.184 1.00 190.69 ? 55 GLU B O 1 ATOM 7560 C CB . GLU B 2 55 ? -34.428 1.213 6.609 1.00 183.28 ? 55 GLU B CB 1 ATOM 7561 C CG . GLU B 2 55 ? -32.918 1.373 6.533 1.00 181.42 ? 55 GLU B CG 1 ATOM 7562 C CD . GLU B 2 55 ? -32.215 0.083 6.153 1.00 182.24 ? 55 GLU B CD 1 ATOM 7563 O OE1 . GLU B 2 55 ? -32.842 -0.762 5.478 1.00 185.44 ? 55 GLU B OE1 1 ATOM 7564 O OE2 . GLU B 2 55 ? -31.037 -0.088 6.531 1.00 174.18 ? 55 GLU B OE2 1 ATOM 7565 N N . PHE B 2 56 ? -34.275 0.441 10.077 1.00 181.19 ? 56 PHE B N 1 ATOM 7566 C CA . PHE B 2 56 ? -34.273 0.999 11.422 1.00 168.87 ? 56 PHE B CA 1 ATOM 7567 C C . PHE B 2 56 ? -32.893 0.868 12.046 1.00 157.54 ? 56 PHE B C 1 ATOM 7568 O O . PHE B 2 56 ? -32.648 -0.035 12.845 1.00 166.80 ? 56 PHE B O 1 ATOM 7569 C CB . PHE B 2 56 ? -35.325 0.305 12.291 1.00 160.36 ? 56 PHE B CB 1 ATOM 7570 C CG . PHE B 2 56 ? -35.376 0.810 13.705 1.00 158.79 ? 56 PHE B CG 1 ATOM 7571 C CD1 . PHE B 2 56 ? -35.662 2.137 13.969 1.00 164.69 ? 56 PHE B CD1 1 ATOM 7572 C CD2 . PHE B 2 56 ? -35.148 -0.046 14.769 1.00 163.28 ? 56 PHE B CD2 1 ATOM 7573 C CE1 . PHE B 2 56 ? -35.712 2.606 15.268 1.00 172.99 ? 56 PHE B CE1 1 ATOM 7574 C CE2 . PHE B 2 56 ? -35.198 0.415 16.071 1.00 167.95 ? 56 PHE B CE2 1 ATOM 7575 C CZ . PHE B 2 56 ? -35.480 1.743 16.321 1.00 173.27 ? 56 PHE B CZ 1 ATOM 7576 N N . PRO B 2 57 ? -31.978 1.770 11.668 1.00 136.16 ? 57 PRO B N 1 ATOM 7577 C CA . PRO B 2 57 ? -30.629 1.747 12.234 1.00 134.09 ? 57 PRO B CA 1 ATOM 7578 C C . PRO B 2 57 ? -30.647 2.078 13.721 1.00 140.30 ? 57 PRO B C 1 ATOM 7579 O O . PRO B 2 57 ? -31.310 3.030 14.136 1.00 151.37 ? 57 PRO B O 1 ATOM 7580 C CB . PRO B 2 57 ? -29.893 2.824 11.433 1.00 138.84 ? 57 PRO B CB 1 ATOM 7581 C CG . PRO B 2 57 ? -30.968 3.747 10.972 1.00 142.35 ? 57 PRO B CG 1 ATOM 7582 C CD . PRO B 2 57 ? -32.165 2.880 10.719 1.00 131.31 ? 57 PRO B CD 1 ATOM 7583 N N . VAL B 2 58 ? -29.934 1.286 14.513 1.00 130.34 ? 58 VAL B N 1 ATOM 7584 C CA . VAL B 2 58 ? -29.837 1.528 15.944 1.00 128.62 ? 58 VAL B CA 1 ATOM 7585 C C . VAL B 2 58 ? -28.429 2.014 16.284 1.00 114.01 ? 58 VAL B C 1 ATOM 7586 O O . VAL B 2 58 ? -27.446 1.559 15.699 1.00 122.21 ? 58 VAL B O 1 ATOM 7587 C CB . VAL B 2 58 ? -30.188 0.259 16.759 1.00 129.53 ? 58 VAL B CB 1 ATOM 7588 C CG1 . VAL B 2 58 ? -29.259 -0.893 16.397 1.00 133.53 ? 58 VAL B CG1 1 ATOM 7589 C CG2 . VAL B 2 58 ? -30.153 0.545 18.255 1.00 132.99 ? 58 VAL B CG2 1 ATOM 7590 N N . SER B 2 59 ? -28.339 2.959 17.214 1.00 102.47 ? 59 SER B N 1 ATOM 7591 C CA . SER B 2 59 ? -27.054 3.529 17.593 1.00 107.56 ? 59 SER B CA 1 ATOM 7592 C C . SER B 2 59 ? -26.230 2.547 18.428 1.00 120.06 ? 59 SER B C 1 ATOM 7593 O O . SER B 2 59 ? -26.755 1.898 19.333 1.00 131.25 ? 59 SER B O 1 ATOM 7594 C CB . SER B 2 59 ? -27.264 4.838 18.352 1.00 121.73 ? 59 SER B CB 1 ATOM 7595 O OG . SER B 2 59 ? -28.012 5.760 17.576 1.00 127.09 ? 59 SER B OG 1 ATOM 7596 N N . GLU B 2 60 ? -24.938 2.448 18.124 1.00 111.98 ? 60 GLU B N 1 ATOM 7597 C CA . GLU B 2 60 ? -24.091 1.408 18.710 1.00 107.45 ? 60 GLU B CA 1 ATOM 7598 C C . GLU B 2 60 ? -22.962 1.943 19.592 1.00 106.61 ? 60 GLU B C 1 ATOM 7599 O O . GLU B 2 60 ? -22.246 2.876 19.223 1.00 96.83 ? 60 GLU B O 1 ATOM 7600 C CB . GLU B 2 60 ? -23.498 0.534 17.602 1.00 102.88 ? 60 GLU B CB 1 ATOM 7601 C CG . GLU B 2 60 ? -24.523 -0.299 16.852 1.00 118.48 ? 60 GLU B CG 1 ATOM 7602 C CD . GLU B 2 60 ? -23.907 -1.107 15.727 1.00 132.86 ? 60 GLU B CD 1 ATOM 7603 O OE1 . GLU B 2 60 ? -22.893 -0.653 15.154 1.00 122.53 ? 60 GLU B OE1 1 ATOM 7604 O OE2 . GLU B 2 60 ? -24.433 -2.198 15.421 1.00 138.78 ? 60 GLU B OE2 1 ATOM 7605 N N . ALA B 2 61 ? -22.826 1.336 20.766 1.00 120.63 ? 61 ALA B N 1 ATOM 7606 C CA . ALA B 2 61 ? -21.774 1.663 21.724 1.00 115.86 ? 61 ALA B CA 1 ATOM 7607 C C . ALA B 2 61 ? -20.571 0.718 21.646 1.00 107.22 ? 61 ALA B C 1 ATOM 7608 O O . ALA B 2 61 ? -19.673 0.799 22.482 1.00 124.88 ? 61 ALA B O 1 ATOM 7609 C CB . ALA B 2 61 ? -22.342 1.663 23.135 1.00 134.61 ? 61 ALA B CB 1 ATOM 7610 N N . ARG B 2 62 ? -20.561 -0.167 20.649 1.00 98.30 ? 62 ARG B N 1 ATOM 7611 C CA . ARG B 2 62 ? -19.675 -1.341 20.622 1.00 96.63 ? 62 ARG B CA 1 ATOM 7612 C C . ARG B 2 62 ? -18.205 -1.059 20.924 1.00 95.36 ? 62 ARG B C 1 ATOM 7613 O O . ARG B 2 62 ? -17.601 -0.159 20.339 1.00 96.16 ? 62 ARG B O 1 ATOM 7614 C CB . ARG B 2 62 ? -19.751 -2.018 19.251 1.00 100.13 ? 62 ARG B CB 1 ATOM 7615 C CG . ARG B 2 62 ? -21.130 -2.034 18.628 1.00 122.48 ? 62 ARG B CG 1 ATOM 7616 C CD . ARG B 2 62 ? -21.057 -2.451 17.168 1.00 125.01 ? 62 ARG B CD 1 ATOM 7617 N NE . ARG B 2 62 ? -20.630 -3.837 17.012 1.00 125.93 ? 62 ARG B NE 1 ATOM 7618 C CZ . ARG B 2 62 ? -21.464 -4.869 16.952 1.00 137.83 ? 62 ARG B CZ 1 ATOM 7619 N NH1 . ARG B 2 62 ? -22.773 -4.670 17.033 1.00 141.77 ? 62 ARG B NH1 1 ATOM 7620 N NH2 . ARG B 2 62 ? -20.992 -6.099 16.809 1.00 139.99 ? 62 ARG B NH2 1 ATOM 7621 N N . VAL B 2 63 ? -17.633 -1.841 21.836 1.00 88.96 ? 63 VAL B N 1 ATOM 7622 C CA . VAL B 2 63 ? -16.217 -1.719 22.154 1.00 86.47 ? 63 VAL B CA 1 ATOM 7623 C C . VAL B 2 63 ? -15.393 -2.516 21.148 1.00 87.86 ? 63 VAL B C 1 ATOM 7624 O O . VAL B 2 63 ? -15.703 -3.669 20.845 1.00 103.01 ? 63 VAL B O 1 ATOM 7625 C CB . VAL B 2 63 ? -15.899 -2.188 23.595 1.00 87.20 ? 63 VAL B CB 1 ATOM 7626 C CG1 . VAL B 2 63 ? -16.656 -1.350 24.600 1.00 86.01 ? 63 VAL B CG1 1 ATOM 7627 C CG2 . VAL B 2 63 ? -16.249 -3.641 23.784 1.00 136.15 ? 63 VAL B CG2 1 ATOM 7628 N N . LEU B 2 64 ? -14.371 -1.879 20.587 1.00 95.06 ? 64 LEU B N 1 ATOM 7629 C CA . LEU B 2 64 ? -13.470 -2.566 19.671 1.00 95.30 ? 64 LEU B CA 1 ATOM 7630 C C . LEU B 2 64 ? -12.418 -3.352 20.442 1.00 94.54 ? 64 LEU B C 1 ATOM 7631 O O . LEU B 2 64 ? -12.053 -4.459 20.049 1.00 126.71 ? 64 LEU B O 1 ATOM 7632 C CB . LEU B 2 64 ? -12.820 -1.576 18.706 1.00 104.55 ? 64 LEU B CB 1 ATOM 7633 C CG . LEU B 2 64 ? -13.779 -1.064 17.627 1.00 114.56 ? 64 LEU B CG 1 ATOM 7634 C CD1 . LEU B 2 64 ? -13.072 -0.157 16.631 1.00 119.20 ? 64 LEU B CD1 1 ATOM 7635 C CD2 . LEU B 2 64 ? -14.443 -2.234 16.912 1.00 107.66 ? 64 LEU B CD2 1 ATOM 7636 N N . GLU B 2 65 ? -11.916 -2.774 21.529 1.00 88.15 ? 65 GLU B N 1 ATOM 7637 C CA . GLU B 2 65 ? -11.089 -3.531 22.462 1.00 93.22 ? 65 GLU B CA 1 ATOM 7638 C C . GLU B 2 65 ? -11.196 -3.006 23.890 1.00 91.17 ? 65 GLU B C 1 ATOM 7639 O O . GLU B 2 65 ? -11.244 -1.797 24.110 1.00 92.61 ? 65 GLU B O 1 ATOM 7640 C CB . GLU B 2 65 ? -9.625 -3.509 22.016 1.00 101.21 ? 65 GLU B CB 1 ATOM 7641 C CG . GLU B 2 65 ? -9.011 -2.123 21.942 1.00 103.51 ? 65 GLU B CG 1 ATOM 7642 C CD . GLU B 2 65 ? -7.504 -2.160 21.778 1.00 122.48 ? 65 GLU B CD 1 ATOM 7643 O OE1 . GLU B 2 65 ? -6.835 -2.856 22.572 1.00 102.38 ? 65 GLU B OE1 1 ATOM 7644 O OE2 . GLU B 2 65 ? -6.991 -1.493 20.853 1.00 133.53 ? 65 GLU B OE2 1 ATOM 7645 N N . ASP B 2 66 ? -11.238 -3.917 24.859 1.00 112.51 ? 66 ASP B N 1 ATOM 7646 C CA . ASP B 2 66 ? -11.051 -3.536 26.255 1.00 114.53 ? 66 ASP B CA 1 ATOM 7647 C C . ASP B 2 66 ? -10.107 -4.496 26.972 1.00 92.30 ? 66 ASP B C 1 ATOM 7648 O O . ASP B 2 66 ? -10.438 -5.651 27.204 1.00 94.76 ? 66 ASP B O 1 ATOM 7649 C CB . ASP B 2 66 ? -12.396 -3.466 26.987 1.00 109.51 ? 66 ASP B CB 1 ATOM 7650 C CG . ASP B 2 66 ? -13.179 -4.754 26.903 1.00 106.44 ? 66 ASP B CG 1 ATOM 7651 O OD1 . ASP B 2 66 ? -13.033 -5.475 25.895 1.00 121.91 ? 66 ASP B OD1 1 ATOM 7652 O OD2 . ASP B 2 66 ? -13.941 -5.042 27.849 1.00 112.20 ? 66 ASP B OD2 1 ATOM 7653 N N . ARG B 2 67 ? -8.939 -3.998 27.351 1.00 99.39 ? 67 ARG B N 1 ATOM 7654 C CA . ARG B 2 67 ? -7.984 -4.791 28.109 1.00 93.92 ? 67 ARG B CA 1 ATOM 7655 C C . ARG B 2 67 ? -8.257 -4.601 29.593 1.00 94.17 ? 67 ARG B C 1 ATOM 7656 O O . ARG B 2 67 ? -8.712 -3.538 30.009 1.00 109.37 ? 67 ARG B O 1 ATOM 7657 C CB . ARG B 2 67 ? -6.548 -4.390 27.761 1.00 120.21 ? 67 ARG B CB 1 ATOM 7658 C CG . ARG B 2 67 ? -6.162 -4.659 26.314 1.00 111.65 ? 67 ARG B CG 1 ATOM 7659 C CD . ARG B 2 67 ? -4.833 -4.009 25.959 1.00 111.78 ? 67 ARG B CD 1 ATOM 7660 N NE . ARG B 2 67 ? -4.875 -2.559 26.138 1.00 109.40 ? 67 ARG B NE 1 ATOM 7661 C CZ . ARG B 2 67 ? -3.911 -1.726 25.757 1.00 105.11 ? 67 ARG B CZ 1 ATOM 7662 N NH1 . ARG B 2 67 ? -2.820 -2.193 25.165 1.00 115.10 ? 67 ARG B NH1 1 ATOM 7663 N NH2 . ARG B 2 67 ? -4.040 -0.423 25.962 1.00 108.72 ? 67 ARG B NH2 1 ATOM 7664 N N . PRO B 2 68 ? -7.990 -5.633 30.401 1.00 97.00 ? 68 PRO B N 1 ATOM 7665 C CA . PRO B 2 68 ? -8.247 -5.510 31.838 1.00 107.90 ? 68 PRO B CA 1 ATOM 7666 C C . PRO B 2 68 ? -7.264 -4.569 32.529 1.00 103.10 ? 68 PRO B C 1 ATOM 7667 O O . PRO B 2 68 ? -6.076 -4.593 32.216 1.00 96.73 ? 68 PRO B O 1 ATOM 7668 C CB . PRO B 2 68 ? -8.079 -6.943 32.345 1.00 101.39 ? 68 PRO B CB 1 ATOM 7669 C CG . PRO B 2 68 ? -7.133 -7.564 31.378 1.00 103.69 ? 68 PRO B CG 1 ATOM 7670 C CD . PRO B 2 68 ? -7.462 -6.960 30.043 1.00 99.99 ? 68 PRO B CD 1 ATOM 7671 N N . LEU B 2 69 ? -7.766 -3.753 33.452 1.00 99.85 ? 69 LEU B N 1 ATOM 7672 C CA . LEU B 2 69 ? -6.921 -2.891 34.270 1.00 94.60 ? 69 LEU B CA 1 ATOM 7673 C C . LEU B 2 69 ? -5.883 -3.725 35.006 1.00 97.50 ? 69 LEU B C 1 ATOM 7674 O O . LEU B 2 69 ? -6.228 -4.692 35.682 1.00 146.07 ? 69 LEU B O 1 ATOM 7675 C CB . LEU B 2 69 ? -7.765 -2.109 35.274 1.00 93.81 ? 69 LEU B CB 1 ATOM 7676 C CG . LEU B 2 69 ? -8.961 -1.343 34.713 1.00 91.48 ? 69 LEU B CG 1 ATOM 7677 C CD1 . LEU B 2 69 ? -9.860 -0.877 35.843 1.00 96.91 ? 69 LEU B CD1 1 ATOM 7678 C CD2 . LEU B 2 69 ? -8.493 -0.163 33.882 1.00 120.19 ? 69 LEU B CD2 1 ATOM 7679 N N . SER B 2 70 ? -4.613 -3.358 34.878 1.00 97.11 ? 70 SER B N 1 ATOM 7680 C CA . SER B 2 70 ? -3.560 -4.154 35.491 1.00 126.53 ? 70 SER B CA 1 ATOM 7681 C C . SER B 2 70 ? -3.478 -3.911 36.993 1.00 125.00 ? 70 SER B C 1 ATOM 7682 O O . SER B 2 70 ? -4.191 -3.071 37.544 1.00 99.77 ? 70 SER B O 1 ATOM 7683 C CB . SER B 2 70 ? -2.210 -3.861 34.837 1.00 104.97 ? 70 SER B CB 1 ATOM 7684 O OG . SER B 2 70 ? -1.888 -2.488 34.928 1.00 97.37 ? 70 SER B OG 1 ATOM 7685 N N . ASP B 2 71 ? -2.587 -4.651 37.640 1.00 133.73 ? 71 ASP B N 1 ATOM 7686 C CA . ASP B 2 71 ? -2.461 -4.634 39.090 1.00 127.58 ? 71 ASP B CA 1 ATOM 7687 C C . ASP B 2 71 ? -1.185 -3.918 39.489 1.00 113.91 ? 71 ASP B C 1 ATOM 7688 O O . ASP B 2 71 ? -1.228 -2.915 40.194 1.00 129.82 ? 71 ASP B O 1 ATOM 7689 C CB . ASP B 2 71 ? -2.488 -6.056 39.645 1.00 136.11 ? 71 ASP B CB 1 ATOM 7690 C CG . ASP B 2 71 ? -3.805 -6.752 39.377 1.00 138.69 ? 71 ASP B CG 1 ATOM 7691 O OD1 . ASP B 2 71 ? -4.855 -6.230 39.809 1.00 128.40 ? 71 ASP B OD1 1 ATOM 7692 O OD2 . ASP B 2 71 ? -3.795 -7.808 38.714 1.00 146.00 ? 71 ASP B OD2 1 ATOM 7693 N N . LYS B 2 72 ? -0.048 -4.457 39.065 1.00 110.84 ? 72 LYS B N 1 ATOM 7694 C CA . LYS B 2 72 ? 1.214 -3.741 39.177 1.00 135.61 ? 72 LYS B CA 1 ATOM 7695 C C . LYS B 2 72 ? 1.699 -3.340 37.788 1.00 140.32 ? 72 LYS B C 1 ATOM 7696 O O . LYS B 2 72 ? 1.766 -4.170 36.880 1.00 140.08 ? 72 LYS B O 1 ATOM 7697 C CB . LYS B 2 72 ? 2.266 -4.586 39.896 1.00 141.38 ? 72 LYS B CB 1 ATOM 7698 C CG . LYS B 2 72 ? 1.984 -4.791 41.376 1.00 141.00 ? 72 LYS B CG 1 ATOM 7699 C CD . LYS B 2 72 ? 3.250 -4.633 42.204 1.00 143.10 ? 72 LYS B CD 1 ATOM 7700 C CE . LYS B 2 72 ? 2.997 -4.929 43.675 1.00 149.57 ? 72 LYS B CE 1 ATOM 7701 N NZ . LYS B 2 72 ? 2.661 -6.363 43.911 1.00 147.11 ? 72 LYS B NZ 1 ATOM 7702 N N . GLY B 2 73 ? 2.030 -2.062 37.627 1.00 127.84 ? 73 GLY B N 1 ATOM 7703 C CA . GLY B 2 73 ? 2.419 -1.532 36.334 1.00 116.35 ? 73 GLY B CA 1 ATOM 7704 C C . GLY B 2 73 ? 3.916 -1.499 36.107 1.00 120.62 ? 73 GLY B C 1 ATOM 7705 O O . GLY B 2 73 ? 4.405 -0.756 35.256 1.00 111.86 ? 73 GLY B O 1 ATOM 7706 N N . SER B 2 74 ? 4.649 -2.306 36.865 1.00 125.61 ? 74 SER B N 1 ATOM 7707 C CA . SER B 2 74 ? 6.101 -2.325 36.752 1.00 138.11 ? 74 SER B CA 1 ATOM 7708 C C . SER B 2 74 ? 6.619 -3.612 36.121 1.00 125.24 ? 74 SER B C 1 ATOM 7709 O O . SER B 2 74 ? 6.553 -4.682 36.722 1.00 111.46 ? 74 SER B O 1 ATOM 7710 C CB . SER B 2 74 ? 6.744 -2.132 38.125 1.00 142.22 ? 74 SER B CB 1 ATOM 7711 O OG . SER B 2 74 ? 6.352 -3.153 39.026 1.00 121.11 ? 74 SER B OG 1 ATOM 7712 N N . GLY B 2 75 ? 7.127 -3.495 34.900 1.00 131.36 ? 75 GLY B N 1 ATOM 7713 C CA . GLY B 2 75 ? 7.829 -4.584 34.251 1.00 132.02 ? 75 GLY B CA 1 ATOM 7714 C C . GLY B 2 75 ? 6.964 -5.740 33.788 1.00 153.63 ? 75 GLY B C 1 ATOM 7715 O O . GLY B 2 75 ? 5.792 -5.848 34.150 1.00 162.74 ? 75 GLY B O 1 ATOM 7716 N N . ASP B 2 76 ? 7.573 -6.601 32.979 1.00 163.54 ? 76 ASP B N 1 ATOM 7717 C CA . ASP B 2 76 ? 6.961 -7.818 32.452 1.00 164.39 ? 76 ASP B CA 1 ATOM 7718 C C . ASP B 2 76 ? 5.597 -7.564 31.811 1.00 175.51 ? 76 ASP B C 1 ATOM 7719 O O . ASP B 2 76 ? 5.379 -6.511 31.208 1.00 173.37 ? 76 ASP B O 1 ATOM 7720 C CB . ASP B 2 76 ? 6.830 -8.863 33.566 1.00 159.54 ? 76 ASP B CB 1 ATOM 7721 C CG . ASP B 2 76 ? 6.850 -10.289 33.041 1.00 173.85 ? 76 ASP B CG 1 ATOM 7722 O OD1 . ASP B 2 76 ? 6.393 -10.510 31.900 1.00 174.10 ? 76 ASP B OD1 1 ATOM 7723 O OD2 . ASP B 2 76 ? 7.321 -11.187 33.770 1.00 175.49 ? 76 ASP B OD2 1 ATOM 7724 N N . SER B 2 77 ? 4.685 -8.522 31.987 1.00 167.01 ? 77 SER B N 1 ATOM 7725 C CA . SER B 2 77 ? 3.348 -8.492 31.394 1.00 165.31 ? 77 SER B CA 1 ATOM 7726 C C . SER B 2 77 ? 3.412 -8.028 29.945 1.00 165.28 ? 77 SER B C 1 ATOM 7727 O O . SER B 2 77 ? 4.280 -8.452 29.181 1.00 164.63 ? 77 SER B O 1 ATOM 7728 C CB . SER B 2 77 ? 2.417 -7.580 32.200 1.00 161.61 ? 77 SER B CB 1 ATOM 7729 O OG . SER B 2 77 ? 1.154 -7.446 31.568 1.00 133.81 ? 77 SER B OG 1 ATOM 7730 N N . SER B 2 78 ? 2.473 -7.162 29.581 1.00 150.82 ? 78 SER B N 1 ATOM 7731 C CA . SER B 2 78 ? 2.640 -6.214 28.489 1.00 141.81 ? 78 SER B CA 1 ATOM 7732 C C . SER B 2 78 ? 1.568 -5.149 28.654 1.00 129.73 ? 78 SER B C 1 ATOM 7733 O O . SER B 2 78 ? 0.553 -5.410 29.300 1.00 138.41 ? 78 SER B O 1 ATOM 7734 C CB . SER B 2 78 ? 2.534 -6.894 27.123 1.00 141.63 ? 78 SER B CB 1 ATOM 7735 O OG . SER B 2 78 ? 1.254 -7.463 26.933 1.00 152.68 ? 78 SER B OG 1 ATOM 7736 N N . GLN B 2 79 ? 1.782 -3.970 28.073 1.00 124.03 ? 79 GLN B N 1 ATOM 7737 C CA . GLN B 2 79 ? 0.705 -2.992 27.918 1.00 140.43 ? 79 GLN B CA 1 ATOM 7738 C C . GLN B 2 79 ? -0.025 -2.680 29.226 1.00 143.23 ? 79 GLN B C 1 ATOM 7739 O O . GLN B 2 79 ? -1.126 -3.172 29.450 1.00 147.58 ? 79 GLN B O 1 ATOM 7740 C CB . GLN B 2 79 ? -0.286 -3.480 26.860 1.00 148.26 ? 79 GLN B CB 1 ATOM 7741 C CG . GLN B 2 79 ? 0.287 -3.476 25.449 1.00 151.96 ? 79 GLN B CG 1 ATOM 7742 C CD . GLN B 2 79 ? -0.564 -4.251 24.462 1.00 156.75 ? 79 GLN B CD 1 ATOM 7743 O OE1 . GLN B 2 79 ? -1.224 -5.225 24.825 1.00 135.29 ? 79 GLN B OE1 1 ATOM 7744 N NE2 . GLN B 2 79 ? -0.553 -3.821 23.206 1.00 162.21 ? 79 GLN B NE2 1 ATOM 7745 N N . VAL B 2 80 ? 0.612 -1.889 30.087 1.00 138.64 ? 80 VAL B N 1 ATOM 7746 C CA . VAL B 2 80 ? 0.158 -1.640 31.459 1.00 123.88 ? 80 VAL B CA 1 ATOM 7747 C C . VAL B 2 80 ? -1.338 -1.312 31.604 1.00 119.22 ? 80 VAL B C 1 ATOM 7748 O O . VAL B 2 80 ? -1.958 -1.684 32.602 1.00 109.29 ? 80 VAL B O 1 ATOM 7749 C CB . VAL B 2 80 ? 0.980 -0.489 32.081 1.00 99.23 ? 80 VAL B CB 1 ATOM 7750 C CG1 . VAL B 2 80 ? 0.598 -0.266 33.534 1.00 92.34 ? 80 VAL B CG1 1 ATOM 7751 C CG2 . VAL B 2 80 ? 2.465 -0.786 31.964 1.00 102.03 ? 80 VAL B CG2 1 ATOM 7752 N N . THR B 2 81 ? -1.909 -0.634 30.608 1.00 109.49 ? 81 THR B N 1 ATOM 7753 C CA . THR B 2 81 ? -3.357 -0.359 30.513 1.00 122.25 ? 81 THR B CA 1 ATOM 7754 C C . THR B 2 81 ? -4.030 0.087 31.825 1.00 107.45 ? 81 THR B C 1 ATOM 7755 O O . THR B 2 81 ? -4.748 -0.676 32.470 1.00 98.10 ? 81 THR B O 1 ATOM 7756 C CB . THR B 2 81 ? -4.161 -1.575 29.905 1.00 109.78 ? 81 THR B CB 1 ATOM 7757 O OG1 . THR B 2 81 ? -5.562 -1.273 29.907 1.00 115.63 ? 81 THR B OG1 1 ATOM 7758 C CG2 . THR B 2 81 ? -3.939 -2.899 30.638 1.00 112.60 ? 81 THR B CG2 1 ATOM 7759 N N . GLN B 2 82 ? -3.776 1.331 32.220 1.00 100.14 ? 82 GLN B N 1 ATOM 7760 C CA . GLN B 2 82 ? -4.403 1.905 33.409 1.00 111.83 ? 82 GLN B CA 1 ATOM 7761 C C . GLN B 2 82 ? -5.745 2.571 33.085 1.00 96.60 ? 82 GLN B C 1 ATOM 7762 O O . GLN B 2 82 ? -6.354 3.214 33.939 1.00 82.87 ? 82 GLN B O 1 ATOM 7763 C CB . GLN B 2 82 ? -3.462 2.909 34.074 1.00 103.74 ? 82 GLN B CB 1 ATOM 7764 C CG . GLN B 2 82 ? -2.935 3.978 33.140 1.00 108.84 ? 82 GLN B CG 1 ATOM 7765 C CD . GLN B 2 82 ? -1.799 4.764 33.754 1.00 118.58 ? 82 GLN B CD 1 ATOM 7766 O OE1 . GLN B 2 82 ? -1.454 4.570 34.920 1.00 120.54 ? 82 GLN B OE1 1 ATOM 7767 N NE2 . GLN B 2 82 ? -1.205 5.657 32.969 1.00 122.08 ? 82 GLN B NE2 1 ATOM 7768 N N . VAL B 2 83 ? -6.183 2.435 31.839 1.00 85.95 ? 83 VAL B N 1 ATOM 7769 C CA . VAL B 2 83 ? -7.500 2.905 31.415 1.00 81.12 ? 83 VAL B CA 1 ATOM 7770 C C . VAL B 2 83 ? -8.191 1.785 30.631 1.00 82.76 ? 83 VAL B C 1 ATOM 7771 O O . VAL B 2 83 ? -7.519 0.977 29.989 1.00 83.56 ? 83 VAL B O 1 ATOM 7772 C CB . VAL B 2 83 ? -7.393 4.190 30.550 1.00 85.95 ? 83 VAL B CB 1 ATOM 7773 C CG1 . VAL B 2 83 ? -8.766 4.699 30.134 1.00 77.30 ? 83 VAL B CG1 1 ATOM 7774 C CG2 . VAL B 2 83 ? -6.644 5.275 31.300 1.00 91.06 ? 83 VAL B CG2 1 ATOM 7775 N N . SER B 2 84 ? -9.523 1.756 30.657 1.00 85.14 ? 84 SER B N 1 ATOM 7776 C CA . SER B 2 84 ? -10.293 0.701 30.000 1.00 88.75 ? 84 SER B CA 1 ATOM 7777 C C . SER B 2 84 ? -11.791 0.984 30.042 1.00 83.26 ? 84 SER B C 1 ATOM 7778 O O . SER B 2 84 ? -12.314 1.411 31.071 1.00 83.27 ? 84 SER B O 1 ATOM 7779 C CB . SER B 2 84 ? -10.021 -0.658 30.652 1.00 87.13 ? 84 SER B CB 1 ATOM 7780 O OG . SER B 2 84 ? -10.872 -1.660 30.120 1.00 88.06 ? 84 SER B OG 1 ATOM 7781 N N . PRO B 2 85 ? -12.492 0.735 28.919 1.00 88.28 ? 85 PRO B N 1 ATOM 7782 C CA . PRO B 2 85 ? -11.952 0.238 27.644 1.00 88.29 ? 85 PRO B CA 1 ATOM 7783 C C . PRO B 2 85 ? -11.070 1.248 26.905 1.00 101.92 ? 85 PRO B C 1 ATOM 7784 O O . PRO B 2 85 ? -10.923 2.387 27.349 1.00 102.47 ? 85 PRO B O 1 ATOM 7785 C CB . PRO B 2 85 ? -13.212 -0.060 26.827 1.00 83.66 ? 85 PRO B CB 1 ATOM 7786 C CG . PRO B 2 85 ? -14.244 0.833 27.394 1.00 82.51 ? 85 PRO B CG 1 ATOM 7787 C CD . PRO B 2 85 ? -13.954 0.901 28.862 1.00 85.65 ? 85 PRO B CD 1 ATOM 7788 N N . GLN B 2 86 ? -10.502 0.825 25.781 1.00 89.14 ? 86 GLN B N 1 ATOM 7789 C CA . GLN B 2 86 ? -9.553 1.649 25.042 1.00 82.65 ? 86 GLN B CA 1 ATOM 7790 C C . GLN B 2 86 ? -10.162 2.191 23.755 1.00 89.10 ? 86 GLN B C 1 ATOM 7791 O O . GLN B 2 86 ? -10.240 3.400 23.562 1.00 113.30 ? 86 GLN B O 1 ATOM 7792 C CB . GLN B 2 86 ? -8.279 0.862 24.736 1.00 81.84 ? 86 GLN B CB 1 ATOM 7793 C CG . GLN B 2 86 ? -7.480 0.479 25.976 1.00 89.03 ? 86 GLN B CG 1 ATOM 7794 C CD . GLN B 2 86 ? -8.006 -0.775 26.651 1.00 85.82 ? 86 GLN B CD 1 ATOM 7795 O OE1 . GLN B 2 86 ? -8.468 -1.701 25.987 1.00 86.75 ? 86 GLN B OE1 1 ATOM 7796 N NE2 . GLN B 2 86 ? -7.937 -0.810 27.976 1.00 86.85 ? 86 GLN B NE2 1 ATOM 7797 N N . ARG B 2 87 ? -10.560 1.300 22.858 1.00 80.77 ? 87 ARG B N 1 ATOM 7798 C CA . ARG B 2 87 ? -11.215 1.734 21.633 1.00 81.17 ? 87 ARG B CA 1 ATOM 7799 C C . ARG B 2 87 ? -12.640 1.196 21.536 1.00 88.93 ? 87 ARG B C 1 ATOM 7800 O O . ARG B 2 87 ? -12.863 -0.011 21.619 1.00 92.24 ? 87 ARG B O 1 ATOM 7801 C CB . ARG B 2 87 ? -10.403 1.301 20.410 1.00 89.07 ? 87 ARG B CB 1 ATOM 7802 C CG . ARG B 2 87 ? -11.051 1.662 19.081 1.00 111.59 ? 87 ARG B CG 1 ATOM 7803 C CD . ARG B 2 87 ? -10.100 1.454 17.914 1.00 110.10 ? 87 ARG B CD 1 ATOM 7804 N NE . ARG B 2 87 ? -9.061 2.478 17.867 1.00 126.81 ? 87 ARG B NE 1 ATOM 7805 C CZ . ARG B 2 87 ? -7.829 2.313 18.336 1.00 130.09 ? 87 ARG B CZ 1 ATOM 7806 N NH1 . ARG B 2 87 ? -7.476 1.157 18.884 1.00 119.72 ? 87 ARG B NH1 1 ATOM 7807 N NH2 . ARG B 2 87 ? -6.948 3.301 18.253 1.00 120.11 ? 87 ARG B NH2 1 ATOM 7808 N N . ILE B 2 88 ? -13.606 2.097 21.380 1.00 92.14 ? 88 ILE B N 1 ATOM 7809 C CA . ILE B 2 88 ? -14.979 1.689 21.098 1.00 102.85 ? 88 ILE B CA 1 ATOM 7810 C C . ILE B 2 88 ? -15.483 2.406 19.849 1.00 95.54 ? 88 ILE B C 1 ATOM 7811 O O . ILE B 2 88 ? -14.985 3.477 19.488 1.00 80.79 ? 88 ILE B O 1 ATOM 7812 C CB . ILE B 2 88 ? -15.940 1.968 22.285 1.00 87.60 ? 88 ILE B CB 1 ATOM 7813 C CG1 . ILE B 2 88 ? -16.624 3.327 22.139 1.00 90.34 ? 88 ILE B CG1 1 ATOM 7814 C CG2 . ILE B 2 88 ? -15.214 1.858 23.619 1.00 89.14 ? 88 ILE B CG2 1 ATOM 7815 C CD1 . ILE B 2 88 ? -17.673 3.579 23.193 1.00 99.87 ? 88 ILE B CD1 1 ATOM 7816 N N . ALA B 2 89 ? -16.464 1.805 19.184 1.00 90.54 ? 89 ALA B N 1 ATOM 7817 C CA . ALA B 2 89 ? -17.006 2.373 17.957 1.00 83.96 ? 89 ALA B CA 1 ATOM 7818 C C . ALA B 2 89 ? -18.383 2.977 18.193 1.00 87.72 ? 89 ALA B C 1 ATOM 7819 O O . ALA B 2 89 ? -19.359 2.265 18.424 1.00 93.90 ? 89 ALA B O 1 ATOM 7820 C CB . ALA B 2 89 ? -17.071 1.317 16.869 1.00 91.33 ? 89 ALA B CB 1 ATOM 7821 N N . LEU B 2 90 ? -18.454 4.299 18.131 1.00 95.98 ? 90 LEU B N 1 ATOM 7822 C CA . LEU B 2 90 ? -19.715 5.001 18.296 1.00 93.65 ? 90 LEU B CA 1 ATOM 7823 C C . LEU B 2 90 ? -20.371 5.209 16.940 1.00 96.19 ? 90 LEU B C 1 ATOM 7824 O O . LEU B 2 90 ? -19.766 5.769 16.027 1.00 97.82 ? 90 LEU B O 1 ATOM 7825 C CB . LEU B 2 90 ? -19.498 6.342 18.996 1.00 95.45 ? 90 LEU B CB 1 ATOM 7826 C CG . LEU B 2 90 ? -20.756 7.153 19.299 1.00 94.07 ? 90 LEU B CG 1 ATOM 7827 C CD1 . LEU B 2 90 ? -21.615 6.436 20.325 1.00 90.11 ? 90 LEU B CD1 1 ATOM 7828 C CD2 . LEU B 2 90 ? -20.387 8.544 19.778 1.00 93.53 ? 90 LEU B CD2 1 ATOM 7829 N N . ARG B 2 91 ? -21.609 4.747 16.811 1.00 94.98 ? 91 ARG B N 1 ATOM 7830 C CA . ARG B 2 91 ? -22.348 4.875 15.562 1.00 94.86 ? 91 ARG B CA 1 ATOM 7831 C C . ARG B 2 91 ? -23.702 5.512 15.838 1.00 107.68 ? 91 ARG B C 1 ATOM 7832 O O . ARG B 2 91 ? -24.532 4.929 16.526 1.00 115.79 ? 91 ARG B O 1 ATOM 7833 C CB . ARG B 2 91 ? -22.510 3.506 14.902 1.00 92.47 ? 91 ARG B CB 1 ATOM 7834 C CG . ARG B 2 91 ? -23.152 3.528 13.530 1.00 105.75 ? 91 ARG B CG 1 ATOM 7835 C CD . ARG B 2 91 ? -23.201 2.124 12.947 1.00 119.68 ? 91 ARG B CD 1 ATOM 7836 N NE . ARG B 2 91 ? -24.002 2.055 11.730 1.00 134.15 ? 91 ARG B NE 1 ATOM 7837 C CZ . ARG B 2 91 ? -24.279 0.927 11.083 1.00 148.47 ? 91 ARG B CZ 1 ATOM 7838 N NH1 . ARG B 2 91 ? -23.818 -0.230 11.537 1.00 146.71 ? 91 ARG B NH1 1 ATOM 7839 N NH2 . ARG B 2 91 ? -25.018 0.956 9.982 1.00 155.96 ? 91 ARG B NH2 1 ATOM 7840 N N . LEU B 2 92 ? -23.923 6.710 15.305 1.00 107.71 ? 92 LEU B N 1 ATOM 7841 C CA . LEU B 2 92 ? -25.116 7.476 15.653 1.00 103.20 ? 92 LEU B CA 1 ATOM 7842 C C . LEU B 2 92 ? -26.000 7.825 14.460 1.00 117.03 ? 92 LEU B C 1 ATOM 7843 O O . LEU B 2 92 ? -25.524 8.323 13.437 1.00 109.08 ? 92 LEU B O 1 ATOM 7844 C CB . LEU B 2 92 ? -24.717 8.762 16.380 1.00 93.03 ? 92 LEU B CB 1 ATOM 7845 C CG . LEU B 2 92 ? -24.137 8.561 17.780 1.00 97.24 ? 92 LEU B CG 1 ATOM 7846 C CD1 . LEU B 2 92 ? -23.669 9.878 18.376 1.00 89.99 ? 92 LEU B CD1 1 ATOM 7847 C CD2 . LEU B 2 92 ? -25.167 7.903 18.681 1.00 99.14 ? 92 LEU B CD2 1 ATOM 7848 N N . ARG B 2 93 ? -27.293 7.553 14.609 1.00 120.39 ? 93 ARG B N 1 ATOM 7849 C CA . ARG B 2 93 ? -28.298 7.991 13.651 1.00 115.70 ? 93 ARG B CA 1 ATOM 7850 C C . ARG B 2 93 ? -28.679 9.436 13.991 1.00 129.28 ? 93 ARG B C 1 ATOM 7851 O O . ARG B 2 93 ? -28.384 9.900 15.093 1.00 124.25 ? 93 ARG B O 1 ATOM 7852 C CB . ARG B 2 93 ? -29.513 7.058 13.682 1.00 124.00 ? 93 ARG B CB 1 ATOM 7853 C CG . ARG B 2 93 ? -30.349 7.150 14.938 1.00 137.77 ? 93 ARG B CG 1 ATOM 7854 C CD . ARG B 2 93 ? -31.648 6.383 14.775 1.00 144.16 ? 93 ARG B CD 1 ATOM 7855 N NE . ARG B 2 93 ? -32.495 6.964 13.737 1.00 139.14 ? 93 ARG B NE 1 ATOM 7856 C CZ . ARG B 2 93 ? -33.628 6.420 13.308 1.00 142.05 ? 93 ARG B CZ 1 ATOM 7857 N NH1 . ARG B 2 93 ? -34.053 5.274 13.825 1.00 138.07 ? 93 ARG B NH1 1 ATOM 7858 N NH2 . ARG B 2 93 ? -34.337 7.020 12.362 1.00 148.01 ? 93 ARG B NH2 1 ATOM 7859 N N . PRO B 2 94 ? -29.314 10.159 13.048 1.00 136.13 ? 94 PRO B N 1 ATOM 7860 C CA . PRO B 2 94 ? -29.583 11.590 13.244 1.00 125.51 ? 94 PRO B CA 1 ATOM 7861 C C . PRO B 2 94 ? -30.297 11.951 14.546 1.00 114.51 ? 94 PRO B C 1 ATOM 7862 O O . PRO B 2 94 ? -31.296 11.325 14.908 1.00 114.92 ? 94 PRO B O 1 ATOM 7863 C CB . PRO B 2 94 ? -30.468 11.949 12.039 1.00 139.27 ? 94 PRO B CB 1 ATOM 7864 C CG . PRO B 2 94 ? -30.885 10.638 11.437 1.00 148.02 ? 94 PRO B CG 1 ATOM 7865 C CD . PRO B 2 94 ? -29.755 9.717 11.715 1.00 142.71 ? 94 PRO B CD 1 ATOM 7866 N N . ASP B 2 95 ? -29.754 12.957 15.231 1.00 108.25 ? 95 ASP B N 1 ATOM 7867 C CA . ASP B 2 95 ? -30.327 13.518 16.456 1.00 110.75 ? 95 ASP B CA 1 ATOM 7868 C C . ASP B 2 95 ? -30.472 12.492 17.576 1.00 113.73 ? 95 ASP B C 1 ATOM 7869 O O . ASP B 2 95 ? -31.300 12.661 18.471 1.00 110.41 ? 95 ASP B O 1 ATOM 7870 C CB . ASP B 2 95 ? -31.689 14.160 16.166 1.00 122.84 ? 95 ASP B CB 1 ATOM 7871 C CG . ASP B 2 95 ? -31.569 15.469 15.405 1.00 138.51 ? 95 ASP B CG 1 ATOM 7872 O OD1 . ASP B 2 95 ? -30.632 16.244 15.691 1.00 128.17 ? 95 ASP B OD1 1 ATOM 7873 O OD2 . ASP B 2 95 ? -32.415 15.724 14.522 1.00 148.60 ? 95 ASP B OD2 1 ATOM 7874 N N . ASP B 2 96 ? -29.659 11.441 17.533 1.00 123.33 ? 96 ASP B N 1 ATOM 7875 C CA . ASP B 2 96 ? -29.742 10.378 18.529 1.00 114.12 ? 96 ASP B CA 1 ATOM 7876 C C . ASP B 2 96 ? -28.607 10.480 19.542 1.00 119.05 ? 96 ASP B C 1 ATOM 7877 O O . ASP B 2 96 ? -27.748 11.355 19.444 1.00 118.69 ? 96 ASP B O 1 ATOM 7878 C CB . ASP B 2 96 ? -29.716 9.006 17.852 1.00 112.85 ? 96 ASP B CB 1 ATOM 7879 C CG . ASP B 2 96 ? -30.317 7.909 18.717 1.00 122.22 ? 96 ASP B CG 1 ATOM 7880 O OD1 . ASP B 2 96 ? -30.417 8.101 19.947 1.00 120.86 ? 96 ASP B OD1 1 ATOM 7881 O OD2 . ASP B 2 96 ? -30.686 6.851 18.166 1.00 132.97 ? 96 ASP B OD2 1 ATOM 7882 N N . SER B 2 97 ? -28.618 9.576 20.516 1.00 127.18 ? 97 SER B N 1 ATOM 7883 C CA . SER B 2 97 ? -27.569 9.511 21.521 1.00 110.76 ? 97 SER B CA 1 ATOM 7884 C C . SER B 2 97 ? -27.400 8.098 22.061 1.00 118.58 ? 97 SER B C 1 ATOM 7885 O O . SER B 2 97 ? -28.365 7.339 22.161 1.00 119.71 ? 97 SER B O 1 ATOM 7886 C CB . SER B 2 97 ? -27.873 10.467 22.672 1.00 109.90 ? 97 SER B CB 1 ATOM 7887 O OG . SER B 2 97 ? -29.080 10.109 23.322 1.00 126.76 ? 97 SER B OG 1 ATOM 7888 N N . LYS B 2 98 ? -26.165 7.753 22.406 1.00 110.11 ? 98 LYS B N 1 ATOM 7889 C CA . LYS B 2 98 ? -25.880 6.524 23.133 1.00 104.27 ? 98 LYS B CA 1 ATOM 7890 C C . LYS B 2 98 ? -24.876 6.821 24.230 1.00 94.18 ? 98 LYS B C 1 ATOM 7891 O O . LYS B 2 98 ? -24.201 7.850 24.205 1.00 93.07 ? 98 LYS B O 1 ATOM 7892 C CB . LYS B 2 98 ? -25.351 5.427 22.206 1.00 110.44 ? 98 LYS B CB 1 ATOM 7893 C CG . LYS B 2 98 ? -26.418 4.451 21.731 1.00 107.42 ? 98 LYS B CG 1 ATOM 7894 C CD . LYS B 2 98 ? -27.130 3.783 22.899 1.00 116.71 ? 98 LYS B CD 1 ATOM 7895 C CE . LYS B 2 98 ? -28.309 2.948 22.421 1.00 128.52 ? 98 LYS B CE 1 ATOM 7896 N NZ . LYS B 2 98 ? -29.334 3.774 21.721 1.00 124.97 ? 98 LYS B NZ 1 ATOM 7897 N N . ASN B 2 99 ? -24.780 5.920 25.198 1.00 111.77 ? 99 ASN B N 1 ATOM 7898 C CA . ASN B 2 99 ? -23.908 6.144 26.338 1.00 115.52 ? 99 ASN B CA 1 ATOM 7899 C C . ASN B 2 99 ? -23.000 4.959 26.624 1.00 101.39 ? 99 ASN B C 1 ATOM 7900 O O . ASN B 2 99 ? -23.402 3.804 26.483 1.00 113.46 ? 99 ASN B O 1 ATOM 7901 C CB . ASN B 2 99 ? -24.739 6.470 27.576 1.00 130.70 ? 99 ASN B CB 1 ATOM 7902 C CG . ASN B 2 99 ? -25.807 5.435 27.845 1.00 145.36 ? 99 ASN B CG 1 ATOM 7903 O OD1 . ASN B 2 99 ? -26.457 4.945 26.923 1.00 137.64 ? 99 ASN B OD1 1 ATOM 7904 N ND2 . ASN B 2 99 ? -25.991 5.098 29.116 1.00 182.55 ? 99 ASN B ND2 1 ATOM 7905 N N . PHE B 2 100 ? -21.772 5.260 27.027 1.00 82.06 ? 100 PHE B N 1 ATOM 7906 C CA . PHE B 2 100 ? -20.796 4.234 27.364 1.00 80.79 ? 100 PHE B CA 1 ATOM 7907 C C . PHE B 2 100 ? -20.108 4.558 28.688 1.00 81.84 ? 100 PHE B C 1 ATOM 7908 O O . PHE B 2 100 ? -20.422 5.558 29.333 1.00 81.37 ? 100 PHE B O 1 ATOM 7909 C CB . PHE B 2 100 ? -19.766 4.082 26.242 1.00 80.08 ? 100 PHE B CB 1 ATOM 7910 C CG . PHE B 2 100 ? -19.152 5.377 25.798 1.00 81.85 ? 100 PHE B CG 1 ATOM 7911 C CD1 . PHE B 2 100 ? -19.734 6.125 24.786 1.00 90.56 ? 100 PHE B CD1 1 ATOM 7912 C CD2 . PHE B 2 100 ? -17.987 5.844 26.383 1.00 90.82 ? 100 PHE B CD2 1 ATOM 7913 C CE1 . PHE B 2 100 ? -19.171 7.319 24.374 1.00 83.32 ? 100 PHE B CE1 1 ATOM 7914 C CE2 . PHE B 2 100 ? -17.418 7.039 25.974 1.00 91.66 ? 100 PHE B CE2 1 ATOM 7915 C CZ . PHE B 2 100 ? -18.011 7.775 24.968 1.00 86.61 ? 100 PHE B CZ 1 ATOM 7916 N N . SER B 2 101 ? -19.177 3.702 29.095 1.00 98.78 ? 101 SER B N 1 ATOM 7917 C CA . SER B 2 101 ? -18.477 3.883 30.361 1.00 82.12 ? 101 SER B CA 1 ATOM 7918 C C . SER B 2 101 ? -16.971 3.854 30.167 1.00 83.72 ? 101 SER B C 1 ATOM 7919 O O . SER B 2 101 ? -16.473 3.347 29.164 1.00 99.94 ? 101 SER B O 1 ATOM 7920 C CB . SER B 2 101 ? -18.888 2.802 31.364 1.00 86.78 ? 101 SER B CB 1 ATOM 7921 O OG . SER B 2 101 ? -20.281 2.836 31.616 1.00 119.76 ? 101 SER B OG 1 ATOM 7922 N N . ILE B 2 102 ? -16.249 4.413 31.130 1.00 85.00 ? 102 ILE B N 1 ATOM 7923 C CA . ILE B 2 102 ? -14.798 4.316 31.144 1.00 79.42 ? 102 ILE B CA 1 ATOM 7924 C C . ILE B 2 102 ? -14.300 4.197 32.583 1.00 80.56 ? 102 ILE B C 1 ATOM 7925 O O . ILE B 2 102 ? -14.789 4.885 33.478 1.00 94.38 ? 102 ILE B O 1 ATOM 7926 C CB . ILE B 2 102 ? -14.142 5.523 30.447 1.00 77.06 ? 102 ILE B CB 1 ATOM 7927 C CG1 . ILE B 2 102 ? -12.619 5.441 30.553 1.00 80.64 ? 102 ILE B CG1 1 ATOM 7928 C CG2 . ILE B 2 102 ? -14.655 6.830 31.031 1.00 77.86 ? 102 ILE B CG2 1 ATOM 7929 C CD1 . ILE B 2 102 ? -11.901 6.565 29.852 1.00 90.70 ? 102 ILE B CD1 1 ATOM 7930 N N . GLN B 2 103 ? -13.348 3.296 32.806 1.00 81.83 ? 103 GLN B N 1 ATOM 7931 C CA . GLN B 2 103 ? -12.757 3.121 34.126 1.00 83.75 ? 103 GLN B CA 1 ATOM 7932 C C . GLN B 2 103 ? -11.267 3.431 34.084 1.00 86.35 ? 103 GLN B C 1 ATOM 7933 O O . GLN B 2 103 ? -10.564 3.020 33.162 1.00 93.84 ? 103 GLN B O 1 ATOM 7934 C CB . GLN B 2 103 ? -12.983 1.697 34.644 1.00 101.62 ? 103 GLN B CB 1 ATOM 7935 C CG . GLN B 2 103 ? -14.444 1.308 34.838 1.00 112.74 ? 103 GLN B CG 1 ATOM 7936 C CD . GLN B 2 103 ? -15.061 0.681 33.599 1.00 119.51 ? 103 GLN B CD 1 ATOM 7937 O OE1 . GLN B 2 103 ? -15.179 1.320 32.553 1.00 104.71 ? 103 GLN B OE1 1 ATOM 7938 N NE2 . GLN B 2 103 ? -15.456 -0.582 33.713 1.00 134.04 ? 103 GLN B NE2 1 ATOM 7939 N N . VAL B 2 104 ? -10.791 4.164 35.086 1.00 95.57 ? 104 VAL B N 1 ATOM 7940 C CA . VAL B 2 104 ? -9.377 4.507 35.176 1.00 97.41 ? 104 VAL B CA 1 ATOM 7941 C C . VAL B 2 104 ? -8.823 4.164 36.553 1.00 85.98 ? 104 VAL B C 1 ATOM 7942 O O . VAL B 2 104 ? -9.543 4.200 37.552 1.00 85.03 ? 104 VAL B O 1 ATOM 7943 C CB . VAL B 2 104 ? -9.135 5.998 34.891 1.00 84.13 ? 104 VAL B CB 1 ATOM 7944 C CG1 . VAL B 2 104 ? -9.461 6.320 33.443 1.00 91.14 ? 104 VAL B CG1 1 ATOM 7945 C CG2 . VAL B 2 104 ? -9.967 6.846 35.820 1.00 90.92 ? 104 VAL B CG2 1 ATOM 7946 N N . ARG B 2 105 ? -7.539 3.829 36.601 1.00 84.50 ? 105 ARG B N 1 ATOM 7947 C CA . ARG B 2 105 ? -6.918 3.398 37.845 1.00 108.43 ? 105 ARG B CA 1 ATOM 7948 C C . ARG B 2 105 ? -5.514 3.969 38.001 1.00 104.70 ? 105 ARG B C 1 ATOM 7949 O O . ARG B 2 105 ? -4.730 3.988 37.051 1.00 104.09 ? 105 ARG B O 1 ATOM 7950 C CB . ARG B 2 105 ? -6.867 1.868 37.910 1.00 89.59 ? 105 ARG B CB 1 ATOM 7951 C CG . ARG B 2 105 ? -6.331 1.316 39.221 1.00 92.50 ? 105 ARG B CG 1 ATOM 7952 C CD . ARG B 2 105 ? -5.843 -0.121 39.071 1.00 109.72 ? 105 ARG B CD 1 ATOM 7953 N NE . ARG B 2 105 ? -6.891 -1.030 38.615 1.00 104.84 ? 105 ARG B NE 1 ATOM 7954 C CZ . ARG B 2 105 ? -7.639 -1.774 39.422 1.00 103.00 ? 105 ARG B CZ 1 ATOM 7955 N NH1 . ARG B 2 105 ? -8.570 -2.570 38.917 1.00 99.20 ? 105 ARG B NH1 1 ATOM 7956 N NH2 . ARG B 2 105 ? -7.457 -1.721 40.735 1.00 117.63 ? 105 ARG B NH2 1 ATOM 7957 N N . GLN B 2 106 ? -5.199 4.430 39.208 1.00 90.13 ? 106 GLN B N 1 ATOM 7958 C CA . GLN B 2 106 ? -3.836 4.819 39.532 1.00 95.15 ? 106 GLN B CA 1 ATOM 7959 C C . GLN B 2 106 ? -3.148 3.572 40.051 1.00 91.32 ? 106 GLN B C 1 ATOM 7960 O O . GLN B 2 106 ? -3.478 3.080 41.127 1.00 93.40 ? 106 GLN B O 1 ATOM 7961 C CB . GLN B 2 106 ? -3.811 5.938 40.574 1.00 98.05 ? 106 GLN B CB 1 ATOM 7962 C CG . GLN B 2 106 ? -4.286 7.286 40.061 1.00 90.42 ? 106 GLN B CG 1 ATOM 7963 C CD . GLN B 2 106 ? -3.208 8.028 39.300 1.00 113.61 ? 106 GLN B CD 1 ATOM 7964 O OE1 . GLN B 2 106 ? -2.166 7.462 38.966 1.00 120.30 ? 106 GLN B OE1 1 ATOM 7965 N NE2 . GLN B 2 106 ? -3.448 9.307 39.029 1.00 101.87 ? 106 GLN B NE2 1 ATOM 7966 N N . VAL B 2 107 ? -2.179 3.066 39.296 1.00 90.74 ? 107 VAL B N 1 ATOM 7967 C CA . VAL B 2 107 ? -1.782 1.681 39.485 1.00 110.40 ? 107 VAL B CA 1 ATOM 7968 C C . VAL B 2 107 ? -0.489 1.485 40.261 1.00 118.52 ? 107 VAL B C 1 ATOM 7969 O O . VAL B 2 107 ? 0.599 1.680 39.720 1.00 128.75 ? 107 VAL B O 1 ATOM 7970 C CB . VAL B 2 107 ? -1.625 0.997 38.114 1.00 109.88 ? 107 VAL B CB 1 ATOM 7971 C CG1 . VAL B 2 107 ? -1.348 -0.481 38.282 1.00 130.57 ? 107 VAL B CG1 1 ATOM 7972 C CG2 . VAL B 2 107 ? -2.869 1.221 37.270 1.00 91.23 ? 107 VAL B CG2 1 ATOM 7973 N N . GLU B 2 108 ? -0.638 1.097 41.530 1.00 124.76 ? 108 GLU B N 1 ATOM 7974 C CA . GLU B 2 108 ? 0.409 0.469 42.342 1.00 123.22 ? 108 GLU B CA 1 ATOM 7975 C C . GLU B 2 108 ? 1.787 1.084 42.130 1.00 143.35 ? 108 GLU B C 1 ATOM 7976 O O . GLU B 2 108 ? 1.989 2.284 42.312 1.00 157.44 ? 108 GLU B O 1 ATOM 7977 C CB . GLU B 2 108 ? 0.456 -1.036 42.077 1.00 135.17 ? 108 GLU B CB 1 ATOM 7978 C CG . GLU B 2 108 ? 0.974 -1.851 43.260 1.00 170.65 ? 108 GLU B CG 1 ATOM 7979 C CD . GLU B 2 108 ? 0.450 -1.347 44.592 1.00 180.88 ? 108 GLU B CD 1 ATOM 7980 O OE1 . GLU B 2 108 ? -0.785 -1.318 44.779 1.00 187.33 ? 108 GLU B OE1 1 ATOM 7981 O OE2 . GLU B 2 108 ? 1.276 -0.972 45.452 1.00 176.53 ? 108 GLU B OE2 1 ATOM 7982 N N . ASP B 2 109 ? 2.729 0.233 41.740 1.00 128.68 ? 109 ASP B N 1 ATOM 7983 C CA . ASP B 2 109 ? 4.038 0.676 41.304 1.00 120.16 ? 109 ASP B CA 1 ATOM 7984 C C . ASP B 2 109 ? 3.962 1.010 39.820 1.00 111.88 ? 109 ASP B C 1 ATOM 7985 O O . ASP B 2 109 ? 3.697 0.141 38.987 1.00 113.91 ? 109 ASP B O 1 ATOM 7986 C CB . ASP B 2 109 ? 5.086 -0.404 41.579 1.00 122.87 ? 109 ASP B CB 1 ATOM 7987 C CG . ASP B 2 109 ? 6.455 -0.054 41.030 1.00 133.83 ? 109 ASP B CG 1 ATOM 7988 O OD1 . ASP B 2 109 ? 6.697 1.125 40.692 1.00 136.50 ? 109 ASP B OD1 1 ATOM 7989 O OD2 . ASP B 2 109 ? 7.301 -0.968 40.949 1.00 129.37 ? 109 ASP B OD2 1 ATOM 7990 N N . TYR B 2 110 ? 4.194 2.278 39.504 1.00 101.61 ? 110 TYR B N 1 ATOM 7991 C CA . TYR B 2 110 ? 4.152 2.756 38.130 1.00 100.14 ? 110 TYR B CA 1 ATOM 7992 C C . TYR B 2 110 ? 5.437 3.520 37.860 1.00 103.84 ? 110 TYR B C 1 ATOM 7993 O O . TYR B 2 110 ? 5.896 4.267 38.722 1.00 119.13 ? 110 TYR B O 1 ATOM 7994 C CB . TYR B 2 110 ? 2.923 3.644 37.909 1.00 90.86 ? 110 TYR B CB 1 ATOM 7995 C CG . TYR B 2 110 ? 2.610 3.958 36.461 1.00 97.75 ? 110 TYR B CG 1 ATOM 7996 C CD1 . TYR B 2 110 ? 3.040 5.142 35.877 1.00 115.32 ? 110 TYR B CD1 1 ATOM 7997 C CD2 . TYR B 2 110 ? 1.873 3.076 35.684 1.00 95.74 ? 110 TYR B CD2 1 ATOM 7998 C CE1 . TYR B 2 110 ? 2.749 5.433 34.556 1.00 108.52 ? 110 TYR B CE1 1 ATOM 7999 C CE2 . TYR B 2 110 ? 1.579 3.358 34.365 1.00 86.60 ? 110 TYR B CE2 1 ATOM 8000 C CZ . TYR B 2 110 ? 2.018 4.536 33.806 1.00 96.44 ? 110 TYR B CZ 1 ATOM 8001 O OH . TYR B 2 110 ? 1.726 4.817 32.491 1.00 106.51 ? 110 TYR B OH 1 ATOM 8002 N N . PRO B 2 111 ? 6.017 3.346 36.663 1.00 101.07 ? 111 PRO B N 1 ATOM 8003 C CA . PRO B 2 111 ? 7.293 3.999 36.350 1.00 111.66 ? 111 PRO B CA 1 ATOM 8004 C C . PRO B 2 111 ? 7.198 5.518 36.460 1.00 113.60 ? 111 PRO B C 1 ATOM 8005 O O . PRO B 2 111 ? 6.211 6.113 36.032 1.00 103.06 ? 111 PRO B O 1 ATOM 8006 C CB . PRO B 2 111 ? 7.574 3.559 34.907 1.00 114.24 ? 111 PRO B CB 1 ATOM 8007 C CG . PRO B 2 111 ? 6.257 3.103 34.372 1.00 115.40 ? 111 PRO B CG 1 ATOM 8008 C CD . PRO B 2 111 ? 5.526 2.529 35.542 1.00 112.33 ? 111 PRO B CD 1 ATOM 8009 N N . VAL B 2 112 ? 8.210 6.130 37.064 1.00 118.53 ? 112 VAL B N 1 ATOM 8010 C CA . VAL B 2 112 ? 8.204 7.569 37.291 1.00 110.01 ? 112 VAL B CA 1 ATOM 8011 C C . VAL B 2 112 ? 9.543 8.200 36.930 1.00 102.12 ? 112 VAL B C 1 ATOM 8012 O O . VAL B 2 112 ? 10.574 7.865 37.512 1.00 98.05 ? 112 VAL B O 1 ATOM 8013 C CB . VAL B 2 112 ? 7.874 7.904 38.761 1.00 96.46 ? 112 VAL B CB 1 ATOM 8014 C CG1 . VAL B 2 112 ? 8.102 9.378 39.033 1.00 86.47 ? 112 VAL B CG1 1 ATOM 8015 C CG2 . VAL B 2 112 ? 6.442 7.506 39.096 1.00 96.49 ? 112 VAL B CG2 1 ATOM 8016 N N . ASP B 2 113 ? 9.526 9.113 35.965 1.00 93.64 ? 113 ASP B N 1 ATOM 8017 C CA . ASP B 2 113 ? 10.718 9.886 35.648 1.00 99.66 ? 113 ASP B CA 1 ATOM 8018 C C . ASP B 2 113 ? 10.529 11.341 36.062 1.00 89.32 ? 113 ASP B C 1 ATOM 8019 O O . ASP B 2 113 ? 9.549 11.984 35.688 1.00 83.52 ? 113 ASP B O 1 ATOM 8020 C CB . ASP B 2 113 ? 11.064 9.790 34.159 1.00 103.57 ? 113 ASP B CB 1 ATOM 8021 C CG . ASP B 2 113 ? 9.845 9.801 33.270 1.00 103.08 ? 113 ASP B CG 1 ATOM 8022 O OD1 . ASP B 2 113 ? 8.755 10.177 33.748 1.00 127.00 ? 113 ASP B OD1 1 ATOM 8023 O OD2 . ASP B 2 113 ? 9.984 9.436 32.085 1.00 88.96 ? 113 ASP B OD2 1 ATOM 8024 N N . ILE B 2 114 ? 11.472 11.848 36.847 1.00 93.03 ? 114 ILE B N 1 ATOM 8025 C CA . ILE B 2 114 ? 11.380 13.201 37.381 1.00 96.06 ? 114 ILE B CA 1 ATOM 8026 C C . ILE B 2 114 ? 12.548 14.065 36.909 1.00 83.97 ? 114 ILE B C 1 ATOM 8027 O O . ILE B 2 114 ? 13.715 13.720 37.101 1.00 84.72 ? 114 ILE B O 1 ATOM 8028 C CB . ILE B 2 114 ? 11.324 13.184 38.920 1.00 102.61 ? 114 ILE B CB 1 ATOM 8029 C CG1 . ILE B 2 114 ? 12.415 12.278 39.484 1.00 105.47 ? 114 ILE B CG1 1 ATOM 8030 C CG2 . ILE B 2 114 ? 9.985 12.663 39.390 1.00 98.07 ? 114 ILE B CG2 1 ATOM 8031 C CD1 . ILE B 2 114 ? 12.193 11.875 40.923 1.00 107.28 ? 114 ILE B CD1 1 ATOM 8032 N N . TYR B 2 115 ? 12.223 15.186 36.276 1.00 78.78 ? 115 TYR B N 1 ATOM 8033 C CA . TYR B 2 115 ? 13.240 16.059 35.705 1.00 78.19 ? 115 TYR B CA 1 ATOM 8034 C C . TYR B 2 115 ? 13.400 17.328 36.528 1.00 77.52 ? 115 TYR B C 1 ATOM 8035 O O . TYR B 2 115 ? 12.454 18.102 36.682 1.00 87.29 ? 115 TYR B O 1 ATOM 8036 C CB . TYR B 2 115 ? 12.888 16.411 34.262 1.00 82.79 ? 115 TYR B CB 1 ATOM 8037 C CG . TYR B 2 115 ? 13.982 17.136 33.511 1.00 85.39 ? 115 TYR B CG 1 ATOM 8038 C CD1 . TYR B 2 115 ? 15.031 16.435 32.935 1.00 99.20 ? 115 TYR B CD1 1 ATOM 8039 C CD2 . TYR B 2 115 ? 13.958 18.517 33.365 1.00 76.37 ? 115 TYR B CD2 1 ATOM 8040 C CE1 . TYR B 2 115 ? 16.029 17.088 32.239 1.00 96.99 ? 115 TYR B CE1 1 ATOM 8041 C CE2 . TYR B 2 115 ? 14.952 19.179 32.670 1.00 78.76 ? 115 TYR B CE2 1 ATOM 8042 C CZ . TYR B 2 115 ? 15.985 18.457 32.109 1.00 85.63 ? 115 TYR B CZ 1 ATOM 8043 O OH . TYR B 2 115 ? 16.981 19.102 31.414 1.00 94.22 ? 115 TYR B OH 1 ATOM 8044 N N . TYR B 2 116 ? 14.604 17.541 37.046 1.00 79.15 ? 116 TYR B N 1 ATOM 8045 C CA . TYR B 2 116 ? 14.872 18.691 37.899 1.00 85.44 ? 116 TYR B CA 1 ATOM 8046 C C . TYR B 2 116 ? 15.239 19.922 37.073 1.00 79.01 ? 116 TYR B C 1 ATOM 8047 O O . TYR B 2 116 ? 16.253 19.933 36.377 1.00 82.19 ? 116 TYR B O 1 ATOM 8048 C CB . TYR B 2 116 ? 15.993 18.359 38.884 1.00 92.40 ? 116 TYR B CB 1 ATOM 8049 C CG . TYR B 2 116 ? 15.895 19.086 40.202 1.00 92.85 ? 116 TYR B CG 1 ATOM 8050 C CD1 . TYR B 2 116 ? 15.277 18.495 41.297 1.00 83.93 ? 116 TYR B CD1 1 ATOM 8051 C CD2 . TYR B 2 116 ? 16.422 20.361 40.355 1.00 100.94 ? 116 TYR B CD2 1 ATOM 8052 C CE1 . TYR B 2 116 ? 15.186 19.153 42.506 1.00 87.56 ? 116 TYR B CE1 1 ATOM 8053 C CE2 . TYR B 2 116 ? 16.334 21.028 41.558 1.00 97.01 ? 116 TYR B CE2 1 ATOM 8054 C CZ . TYR B 2 116 ? 15.716 20.419 42.630 1.00 98.54 ? 116 TYR B CZ 1 ATOM 8055 O OH . TYR B 2 116 ? 15.629 21.081 43.831 1.00 106.69 ? 116 TYR B OH 1 ATOM 8056 N N . LEU B 2 117 ? 14.411 20.959 37.162 1.00 85.96 ? 117 LEU B N 1 ATOM 8057 C CA . LEU B 2 117 ? 14.645 22.198 36.424 1.00 90.85 ? 117 LEU B CA 1 ATOM 8058 C C . LEU B 2 117 ? 14.948 23.326 37.402 1.00 87.65 ? 117 LEU B C 1 ATOM 8059 O O . LEU B 2 117 ? 14.066 23.782 38.132 1.00 79.50 ? 117 LEU B O 1 ATOM 8060 C CB . LEU B 2 117 ? 13.436 22.542 35.555 1.00 87.81 ? 117 LEU B CB 1 ATOM 8061 C CG . LEU B 2 117 ? 13.625 23.635 34.505 1.00 95.32 ? 117 LEU B CG 1 ATOM 8062 C CD1 . LEU B 2 117 ? 14.874 23.369 33.683 1.00 89.02 ? 117 LEU B CD1 1 ATOM 8063 C CD2 . LEU B 2 117 ? 12.399 23.717 33.606 1.00 87.02 ? 117 LEU B CD2 1 ATOM 8064 N N . MET B 2 118 ? 16.196 23.783 37.405 1.00 87.10 ? 118 MET B N 1 ATOM 8065 C CA . MET B 2 118 ? 16.681 24.628 38.490 1.00 94.15 ? 118 MET B CA 1 ATOM 8066 C C . MET B 2 118 ? 17.190 26.002 38.057 1.00 95.63 ? 118 MET B C 1 ATOM 8067 O O . MET B 2 118 ? 17.916 26.136 37.070 1.00 79.93 ? 118 MET B O 1 ATOM 8068 C CB . MET B 2 118 ? 17.791 23.896 39.245 1.00 78.43 ? 118 MET B CB 1 ATOM 8069 C CG . MET B 2 118 ? 18.267 24.606 40.495 1.00 79.98 ? 118 MET B CG 1 ATOM 8070 S SD . MET B 2 118 ? 19.595 23.715 41.317 1.00 103.83 ? 118 MET B SD 1 ATOM 8071 C CE . MET B 2 118 ? 19.795 24.707 42.791 1.00 88.67 ? 118 MET B CE 1 ATOM 8072 N N . ASP B 2 119 ? 16.799 27.015 38.825 1.00 93.91 ? 119 ASP B N 1 ATOM 8073 C CA . ASP B 2 119 ? 17.299 28.374 38.670 1.00 84.50 ? 119 ASP B CA 1 ATOM 8074 C C . ASP B 2 119 ? 18.763 28.421 39.102 1.00 90.00 ? 119 ASP B C 1 ATOM 8075 O O . ASP B 2 119 ? 19.097 28.017 40.210 1.00 102.47 ? 119 ASP B O 1 ATOM 8076 C CB . ASP B 2 119 ? 16.447 29.334 39.507 1.00 84.93 ? 119 ASP B CB 1 ATOM 8077 C CG . ASP B 2 119 ? 16.790 30.789 39.279 1.00 101.29 ? 119 ASP B CG 1 ATOM 8078 O OD1 . ASP B 2 119 ? 17.799 31.083 38.606 1.00 137.73 ? 119 ASP B OD1 1 ATOM 8079 O OD2 . ASP B 2 119 ? 16.042 31.649 39.790 1.00 89.99 ? 119 ASP B OD2 1 ATOM 8080 N N . LEU B 2 120 ? 19.642 28.864 38.210 1.00 83.31 ? 120 LEU B N 1 ATOM 8081 C CA . LEU B 2 120 ? 21.060 28.992 38.547 1.00 95.86 ? 120 LEU B CA 1 ATOM 8082 C C . LEU B 2 120 ? 21.529 30.416 38.887 1.00 93.71 ? 120 LEU B C 1 ATOM 8083 O O . LEU B 2 120 ? 22.727 30.645 39.057 1.00 85.80 ? 120 LEU B O 1 ATOM 8084 C CB . LEU B 2 120 ? 21.921 28.409 37.426 1.00 98.76 ? 120 LEU B CB 1 ATOM 8085 C CG . LEU B 2 120 ? 22.004 26.878 37.494 1.00 102.63 ? 120 LEU B CG 1 ATOM 8086 C CD1 . LEU B 2 120 ? 23.222 26.347 36.754 1.00 116.17 ? 120 LEU B CD1 1 ATOM 8087 C CD2 . LEU B 2 120 ? 21.999 26.385 38.939 1.00 82.31 ? 120 LEU B CD2 1 ATOM 8088 N N . SER B 2 121 ? 20.607 31.374 38.956 1.00 82.94 ? 121 SER B N 1 ATOM 8089 C CA . SER B 2 121 ? 20.976 32.734 39.348 1.00 85.13 ? 121 SER B CA 1 ATOM 8090 C C . SER B 2 121 ? 21.503 32.726 40.786 1.00 107.09 ? 121 SER B C 1 ATOM 8091 O O . SER B 2 121 ? 21.204 31.810 41.554 1.00 106.54 ? 121 SER B O 1 ATOM 8092 C CB . SER B 2 121 ? 19.791 33.696 39.201 1.00 79.09 ? 121 SER B CB 1 ATOM 8093 O OG . SER B 2 121 ? 18.770 33.433 40.146 1.00 85.71 ? 121 SER B OG 1 ATOM 8094 N N . TYR B 2 122 ? 22.287 33.743 41.138 1.00 97.60 ? 122 TYR B N 1 ATOM 8095 C CA . TYR B 2 122 ? 23.148 33.700 42.326 1.00 92.65 ? 122 TYR B CA 1 ATOM 8096 C C . TYR B 2 122 ? 22.438 33.378 43.643 1.00 87.84 ? 122 TYR B C 1 ATOM 8097 O O . TYR B 2 122 ? 23.053 32.846 44.569 1.00 87.59 ? 122 TYR B O 1 ATOM 8098 C CB . TYR B 2 122 ? 23.898 35.027 42.478 1.00 89.27 ? 122 TYR B CB 1 ATOM 8099 C CG . TYR B 2 122 ? 25.281 34.860 43.069 1.00 102.64 ? 122 TYR B CG 1 ATOM 8100 C CD1 . TYR B 2 122 ? 26.389 34.677 42.250 1.00 106.05 ? 122 TYR B CD1 1 ATOM 8101 C CD2 . TYR B 2 122 ? 25.479 34.866 44.444 1.00 96.78 ? 122 TYR B CD2 1 ATOM 8102 C CE1 . TYR B 2 122 ? 27.655 34.511 42.784 1.00 97.97 ? 122 TYR B CE1 1 ATOM 8103 C CE2 . TYR B 2 122 ? 26.742 34.702 44.988 1.00 96.81 ? 122 TYR B CE2 1 ATOM 8104 C CZ . TYR B 2 122 ? 27.826 34.525 44.153 1.00 98.65 ? 122 TYR B CZ 1 ATOM 8105 O OH . TYR B 2 122 ? 29.083 34.362 44.691 1.00 112.06 ? 122 TYR B OH 1 ATOM 8106 N N . SER B 2 123 ? 21.148 33.681 43.721 1.00 86.69 ? 123 SER B N 1 ATOM 8107 C CA . SER B 2 123 ? 20.379 33.432 44.934 1.00 95.14 ? 123 SER B CA 1 ATOM 8108 C C . SER B 2 123 ? 20.257 31.933 45.222 1.00 132.00 ? 123 SER B C 1 ATOM 8109 O O . SER B 2 123 ? 19.920 31.519 46.337 1.00 146.61 ? 123 SER B O 1 ATOM 8110 C CB . SER B 2 123 ? 18.993 34.066 44.811 1.00 91.68 ? 123 SER B CB 1 ATOM 8111 O OG . SER B 2 123 ? 18.308 34.062 46.051 1.00 116.61 ? 123 SER B OG 1 ATOM 8112 N N . MET B 2 124 ? 20.528 31.127 44.202 1.00 118.31 ? 124 MET B N 1 ATOM 8113 C CA . MET B 2 124 ? 20.408 29.679 44.301 1.00 96.61 ? 124 MET B CA 1 ATOM 8114 C C . MET B 2 124 ? 21.732 28.973 44.585 1.00 102.80 ? 124 MET B C 1 ATOM 8115 O O . MET B 2 124 ? 21.787 27.743 44.604 1.00 122.60 ? 124 MET B O 1 ATOM 8116 C CB . MET B 2 124 ? 19.790 29.129 43.020 1.00 97.41 ? 124 MET B CB 1 ATOM 8117 C CG . MET B 2 124 ? 18.432 29.731 42.679 1.00 95.82 ? 124 MET B CG 1 ATOM 8118 S SD . MET B 2 124 ? 17.043 28.903 43.479 1.00 109.05 ? 124 MET B SD 1 ATOM 8119 C CE . MET B 2 124 ? 16.980 29.750 45.055 1.00 116.67 ? 124 MET B CE 1 ATOM 8120 N N . LYS B 2 125 ? 22.796 29.746 44.784 1.00 119.93 ? 125 LYS B N 1 ATOM 8121 C CA . LYS B 2 125 ? 24.112 29.180 45.080 1.00 112.66 ? 125 LYS B CA 1 ATOM 8122 C C . LYS B 2 125 ? 24.064 28.332 46.354 1.00 111.46 ? 125 LYS B C 1 ATOM 8123 O O . LYS B 2 125 ? 24.695 27.277 46.436 1.00 98.73 ? 125 LYS B O 1 ATOM 8124 C CB . LYS B 2 125 ? 25.155 30.293 45.214 1.00 109.46 ? 125 LYS B CB 1 ATOM 8125 C CG . LYS B 2 125 ? 26.598 29.810 45.165 1.00 115.92 ? 125 LYS B CG 1 ATOM 8126 C CD . LYS B 2 125 ? 27.571 30.982 45.208 1.00 104.01 ? 125 LYS B CD 1 ATOM 8127 C CE . LYS B 2 125 ? 29.014 30.523 45.056 1.00 99.48 ? 125 LYS B CE 1 ATOM 8128 N NZ . LYS B 2 125 ? 29.450 29.651 46.182 1.00 108.65 ? 125 LYS B NZ 1 ATOM 8129 N N . ASP B 2 126 ? 23.303 28.805 47.337 1.00 118.20 ? 126 ASP B N 1 ATOM 8130 C CA . ASP B 2 126 ? 23.051 28.057 48.565 1.00 100.30 ? 126 ASP B CA 1 ATOM 8131 C C . ASP B 2 126 ? 22.337 26.747 48.260 1.00 109.94 ? 126 ASP B C 1 ATOM 8132 O O . ASP B 2 126 ? 22.591 25.719 48.887 1.00 123.50 ? 126 ASP B O 1 ATOM 8133 C CB . ASP B 2 126 ? 22.210 28.893 49.536 1.00 97.41 ? 126 ASP B CB 1 ATOM 8134 C CG . ASP B 2 126 ? 20.920 29.393 48.905 1.00 105.08 ? 126 ASP B CG 1 ATOM 8135 O OD1 . ASP B 2 126 ? 20.890 29.555 47.666 1.00 110.67 ? 126 ASP B OD1 1 ATOM 8136 O OD2 . ASP B 2 126 ? 19.935 29.622 49.639 1.00 105.47 ? 126 ASP B OD2 1 ATOM 8137 N N . ASP B 2 127 ? 21.444 26.800 47.279 1.00 122.14 ? 127 ASP B N 1 ATOM 8138 C CA . ASP B 2 127 ? 20.592 25.672 46.937 1.00 113.05 ? 127 ASP B CA 1 ATOM 8139 C C . ASP B 2 127 ? 21.355 24.583 46.192 1.00 115.71 ? 127 ASP B C 1 ATOM 8140 O O . ASP B 2 127 ? 21.193 23.397 46.479 1.00 109.37 ? 127 ASP B O 1 ATOM 8141 C CB . ASP B 2 127 ? 19.408 26.158 46.101 1.00 101.87 ? 127 ASP B CB 1 ATOM 8142 C CG . ASP B 2 127 ? 18.630 27.264 46.787 1.00 111.42 ? 127 ASP B CG 1 ATOM 8143 O OD1 . ASP B 2 127 ? 19.183 28.372 46.937 1.00 129.76 ? 127 ASP B OD1 1 ATOM 8144 O OD2 . ASP B 2 127 ? 17.466 27.030 47.171 1.00 116.57 ? 127 ASP B OD2 1 ATOM 8145 N N . LEU B 2 128 ? 22.188 24.992 45.239 1.00 107.55 ? 128 LEU B N 1 ATOM 8146 C CA . LEU B 2 128 ? 22.955 24.051 44.428 1.00 102.56 ? 128 LEU B CA 1 ATOM 8147 C C . LEU B 2 128 ? 23.878 23.198 45.289 1.00 118.76 ? 128 LEU B C 1 ATOM 8148 O O . LEU B 2 128 ? 24.125 22.029 44.986 1.00 111.21 ? 128 LEU B O 1 ATOM 8149 C CB . LEU B 2 128 ? 23.768 24.797 43.367 1.00 93.77 ? 128 LEU B CB 1 ATOM 8150 C CG . LEU B 2 128 ? 24.594 23.938 42.405 1.00 101.40 ? 128 LEU B CG 1 ATOM 8151 C CD1 . LEU B 2 128 ? 23.695 23.006 41.611 1.00 108.79 ? 128 LEU B CD1 1 ATOM 8152 C CD2 . LEU B 2 128 ? 25.424 24.807 41.471 1.00 92.63 ? 128 LEU B CD2 1 ATOM 8153 N N . TRP B 2 129 ? 24.379 23.790 46.368 1.00 125.93 ? 129 TRP B N 1 ATOM 8154 C CA . TRP B 2 129 ? 25.294 23.096 47.262 1.00 126.79 ? 129 TRP B CA 1 ATOM 8155 C C . TRP B 2 129 ? 24.655 21.886 47.935 1.00 121.12 ? 129 TRP B C 1 ATOM 8156 O O . TRP B 2 129 ? 25.152 20.771 47.810 1.00 106.04 ? 129 TRP B O 1 ATOM 8157 C CB . TRP B 2 129 ? 25.825 24.048 48.332 1.00 113.35 ? 129 TRP B CB 1 ATOM 8158 C CG . TRP B 2 129 ? 26.677 23.351 49.338 1.00 116.86 ? 129 TRP B CG 1 ATOM 8159 C CD1 . TRP B 2 129 ? 26.342 23.039 50.623 1.00 131.06 ? 129 TRP B CD1 1 ATOM 8160 C CD2 . TRP B 2 129 ? 28.004 22.853 49.136 1.00 125.26 ? 129 TRP B CD2 1 ATOM 8161 N NE1 . TRP B 2 129 ? 27.385 22.388 51.239 1.00 139.12 ? 129 TRP B NE1 1 ATOM 8162 C CE2 . TRP B 2 129 ? 28.417 22.261 50.346 1.00 132.29 ? 129 TRP B CE2 1 ATOM 8163 C CE3 . TRP B 2 129 ? 28.885 22.856 48.050 1.00 122.07 ? 129 TRP B CE3 1 ATOM 8164 C CZ2 . TRP B 2 129 ? 29.672 21.678 50.500 1.00 138.08 ? 129 TRP B CZ2 1 ATOM 8165 C CZ3 . TRP B 2 129 ? 30.130 22.277 48.206 1.00 127.74 ? 129 TRP B CZ3 1 ATOM 8166 C CH2 . TRP B 2 129 ? 30.512 21.695 49.421 1.00 137.35 ? 129 TRP B CH2 1 ATOM 8167 N N . SER B 2 130 ? 23.551 22.112 48.640 1.00 126.98 ? 130 SER B N 1 ATOM 8168 C CA . SER B 2 130 ? 22.918 21.067 49.444 1.00 130.04 ? 130 SER B CA 1 ATOM 8169 C C . SER B 2 130 ? 22.207 20.016 48.595 1.00 118.74 ? 130 SER B C 1 ATOM 8170 O O . SER B 2 130 ? 21.726 19.011 49.114 1.00 124.49 ? 130 SER B O 1 ATOM 8171 C CB . SER B 2 130 ? 21.929 21.689 50.433 1.00 117.47 ? 130 SER B CB 1 ATOM 8172 O OG . SER B 2 130 ? 20.977 22.501 49.769 1.00 102.12 ? 130 SER B OG 1 ATOM 8173 N N . ILE B 2 131 ? 22.147 20.253 47.291 1.00 106.03 ? 131 ILE B N 1 ATOM 8174 C CA . ILE B 2 131 ? 21.438 19.369 46.378 1.00 99.28 ? 131 ILE B CA 1 ATOM 8175 C C . ILE B 2 131 ? 22.353 18.233 45.912 1.00 104.32 ? 131 ILE B C 1 ATOM 8176 O O . ILE B 2 131 ? 21.921 17.304 45.224 1.00 116.02 ? 131 ILE B O 1 ATOM 8177 C CB . ILE B 2 131 ? 20.889 20.176 45.177 1.00 95.27 ? 131 ILE B CB 1 ATOM 8178 C CG1 . ILE B 2 131 ? 19.414 19.873 44.943 1.00 94.54 ? 131 ILE B CG1 1 ATOM 8179 C CG2 . ILE B 2 131 ? 21.718 19.970 43.912 1.00 94.66 ? 131 ILE B CG2 1 ATOM 8180 C CD1 . ILE B 2 131 ? 18.798 20.793 43.927 1.00 91.02 ? 131 ILE B CD1 1 ATOM 8181 N N . GLN B 2 132 ? 23.609 18.300 46.345 1.00 106.66 ? 132 GLN B N 1 ATOM 8182 C CA . GLN B 2 132 ? 24.656 17.365 45.940 1.00 115.71 ? 132 GLN B CA 1 ATOM 8183 C C . GLN B 2 132 ? 24.287 15.887 46.105 1.00 132.04 ? 132 GLN B C 1 ATOM 8184 O O . GLN B 2 132 ? 24.349 15.114 45.149 1.00 130.43 ? 132 GLN B O 1 ATOM 8185 C CB . GLN B 2 132 ? 25.937 17.666 46.729 1.00 130.13 ? 132 GLN B CB 1 ATOM 8186 C CG . GLN B 2 132 ? 25.743 17.777 48.244 1.00 148.05 ? 132 GLN B CG 1 ATOM 8187 C CD . GLN B 2 132 ? 26.913 18.438 48.947 1.00 160.55 ? 132 GLN B CD 1 ATOM 8188 O OE1 . GLN B 2 132 ? 27.855 18.904 48.307 1.00 165.94 ? 132 GLN B OE1 1 ATOM 8189 N NE2 . GLN B 2 132 ? 26.856 18.486 50.274 1.00 160.79 ? 132 GLN B NE2 1 ATOM 8190 N N . ASN B 2 133 ? 23.907 15.501 47.318 1.00 130.86 ? 133 ASN B N 1 ATOM 8191 C CA . ASN B 2 133 ? 23.600 14.112 47.624 1.00 123.45 ? 133 ASN B CA 1 ATOM 8192 C C . ASN B 2 133 ? 22.111 13.813 47.563 1.00 131.93 ? 133 ASN B C 1 ATOM 8193 O O . ASN B 2 133 ? 21.683 12.696 47.850 1.00 135.00 ? 133 ASN B O 1 ATOM 8194 C CB . ASN B 2 133 ? 24.150 13.743 49.002 1.00 132.92 ? 133 ASN B CB 1 ATOM 8195 C CG . ASN B 2 133 ? 25.665 13.706 49.031 1.00 148.71 ? 133 ASN B CG 1 ATOM 8196 O OD1 . ASN B 2 133 ? 26.319 14.719 49.286 1.00 147.28 ? 133 ASN B OD1 1 ATOM 8197 N ND2 . ASN B 2 133 ? 26.233 12.535 48.767 1.00 154.81 ? 133 ASN B ND2 1 ATOM 8198 N N . LEU B 2 134 ? 21.321 14.809 47.177 1.00 138.76 ? 134 LEU B N 1 ATOM 8199 C CA . LEU B 2 134 ? 19.870 14.670 47.193 1.00 148.29 ? 134 LEU B CA 1 ATOM 8200 C C . LEU B 2 134 ? 19.363 13.913 45.969 1.00 139.01 ? 134 LEU B C 1 ATOM 8201 O O . LEU B 2 134 ? 18.161 13.702 45.816 1.00 145.99 ? 134 LEU B O 1 ATOM 8202 C CB . LEU B 2 134 ? 19.198 16.043 47.286 1.00 130.68 ? 134 LEU B CB 1 ATOM 8203 C CG . LEU B 2 134 ? 18.760 16.479 48.690 1.00 126.13 ? 134 LEU B CG 1 ATOM 8204 C CD1 . LEU B 2 134 ? 19.927 16.471 49.666 1.00 120.21 ? 134 LEU B CD1 1 ATOM 8205 C CD2 . LEU B 2 134 ? 18.101 17.849 48.659 1.00 130.54 ? 134 LEU B CD2 1 ATOM 8206 N N . GLY B 2 135 ? 20.282 13.512 45.095 1.00 118.12 ? 135 GLY B N 1 ATOM 8207 C CA . GLY B 2 135 ? 19.943 12.632 43.992 1.00 103.17 ? 135 GLY B CA 1 ATOM 8208 C C . GLY B 2 135 ? 19.741 11.202 44.463 1.00 114.45 ? 135 GLY B C 1 ATOM 8209 O O . GLY B 2 135 ? 18.760 10.549 44.106 1.00 113.22 ? 135 GLY B O 1 ATOM 8210 N N . THR B 2 136 ? 20.672 10.714 45.277 1.00 111.09 ? 136 THR B N 1 ATOM 8211 C CA . THR B 2 136 ? 20.583 9.362 45.813 1.00 114.99 ? 136 THR B CA 1 ATOM 8212 C C . THR B 2 136 ? 19.590 9.302 46.967 1.00 120.37 ? 136 THR B C 1 ATOM 8213 O O . THR B 2 136 ? 18.984 8.263 47.219 1.00 135.49 ? 136 THR B O 1 ATOM 8214 C CB . THR B 2 136 ? 21.953 8.847 46.299 1.00 133.79 ? 136 THR B CB 1 ATOM 8215 O OG1 . THR B 2 136 ? 22.431 9.676 47.365 1.00 133.59 ? 136 THR B OG1 1 ATOM 8216 C CG2 . THR B 2 136 ? 22.962 8.857 45.161 1.00 142.21 ? 136 THR B CG2 1 ATOM 8217 N N . LYS B 2 137 ? 19.435 10.418 47.672 1.00 137.70 ? 137 LYS B N 1 ATOM 8218 C CA . LYS B 2 137 ? 18.456 10.507 48.749 1.00 145.89 ? 137 LYS B CA 1 ATOM 8219 C C . LYS B 2 137 ? 17.053 10.386 48.179 1.00 125.85 ? 137 LYS B C 1 ATOM 8220 O O . LYS B 2 137 ? 16.164 9.797 48.795 1.00 124.36 ? 137 LYS B O 1 ATOM 8221 C CB . LYS B 2 137 ? 18.598 11.822 49.518 1.00 148.78 ? 137 LYS B CB 1 ATOM 8222 C CG . LYS B 2 137 ? 19.855 11.925 50.361 1.00 149.93 ? 137 LYS B CG 1 ATOM 8223 C CD . LYS B 2 137 ? 19.878 13.229 51.139 1.00 143.70 ? 137 LYS B CD 1 ATOM 8224 C CE . LYS B 2 137 ? 21.225 13.460 51.803 1.00 153.52 ? 137 LYS B CE 1 ATOM 8225 N NZ . LYS B 2 137 ? 21.303 14.807 52.432 1.00 144.89 ? 137 LYS B NZ 1 ATOM 8226 N N . LEU B 2 138 ? 16.864 10.955 46.995 1.00 106.98 ? 138 LEU B N 1 ATOM 8227 C CA . LEU B 2 138 ? 15.587 10.887 46.307 1.00 117.79 ? 138 LEU B CA 1 ATOM 8228 C C . LEU B 2 138 ? 15.346 9.476 45.784 1.00 124.12 ? 138 LEU B C 1 ATOM 8229 O O . LEU B 2 138 ? 14.204 9.019 45.697 1.00 116.85 ? 138 LEU B O 1 ATOM 8230 C CB . LEU B 2 138 ? 15.547 11.900 45.165 1.00 100.10 ? 138 LEU B CB 1 ATOM 8231 C CG . LEU B 2 138 ? 14.263 12.020 44.347 1.00 96.82 ? 138 LEU B CG 1 ATOM 8232 C CD1 . LEU B 2 138 ? 13.069 12.264 45.251 1.00 96.62 ? 138 LEU B CD1 1 ATOM 8233 C CD2 . LEU B 2 138 ? 14.417 13.149 43.348 1.00 100.24 ? 138 LEU B CD2 1 ATOM 8234 N N . ALA B 2 139 ? 16.433 8.791 45.441 1.00 122.10 ? 139 ALA B N 1 ATOM 8235 C CA . ALA B 2 139 ? 16.357 7.420 44.953 1.00 115.27 ? 139 ALA B CA 1 ATOM 8236 C C . ALA B 2 139 ? 15.694 6.509 45.976 1.00 111.98 ? 139 ALA B C 1 ATOM 8237 O O . ALA B 2 139 ? 14.781 5.757 45.647 1.00 116.27 ? 139 ALA B O 1 ATOM 8238 C CB . ALA B 2 139 ? 17.742 6.903 44.610 1.00 120.16 ? 139 ALA B CB 1 ATOM 8239 N N . THR B 2 140 ? 16.155 6.591 47.219 1.00 114.82 ? 140 THR B N 1 ATOM 8240 C CA . THR B 2 140 ? 15.644 5.740 48.286 1.00 118.18 ? 140 THR B CA 1 ATOM 8241 C C . THR B 2 140 ? 14.186 6.049 48.620 1.00 119.53 ? 140 THR B C 1 ATOM 8242 O O . THR B 2 140 ? 13.396 5.142 48.884 1.00 124.13 ? 140 THR B O 1 ATOM 8243 C CB . THR B 2 140 ? 16.493 5.882 49.563 1.00 121.77 ? 140 THR B CB 1 ATOM 8244 O OG1 . THR B 2 140 ? 16.377 7.216 50.072 1.00 132.59 ? 140 THR B OG1 1 ATOM 8245 C CG2 . THR B 2 140 ? 17.955 5.582 49.266 1.00 124.00 ? 140 THR B CG2 1 ATOM 8246 N N . GLN B 2 141 ? 13.832 7.330 48.605 1.00 115.70 ? 141 GLN B N 1 ATOM 8247 C CA . GLN B 2 141 ? 12.475 7.747 48.941 1.00 112.54 ? 141 GLN B CA 1 ATOM 8248 C C . GLN B 2 141 ? 11.478 7.334 47.865 1.00 122.45 ? 141 GLN B C 1 ATOM 8249 O O . GLN B 2 141 ? 10.409 6.798 48.165 1.00 109.05 ? 141 GLN B O 1 ATOM 8250 C CB . GLN B 2 141 ? 12.422 9.258 49.156 1.00 108.88 ? 141 GLN B CB 1 ATOM 8251 C CG . GLN B 2 141 ? 13.219 9.731 50.358 1.00 125.84 ? 141 GLN B CG 1 ATOM 8252 C CD . GLN B 2 141 ? 12.680 9.179 51.664 1.00 125.99 ? 141 GLN B CD 1 ATOM 8253 O OE1 . GLN B 2 141 ? 11.489 8.887 51.783 1.00 114.65 ? 141 GLN B OE1 1 ATOM 8254 N NE2 . GLN B 2 141 ? 13.557 9.030 52.651 1.00 118.91 ? 141 GLN B NE2 1 ATOM 8255 N N . MET B 2 142 ? 11.834 7.583 46.610 1.00 114.18 ? 142 MET B N 1 ATOM 8256 C CA . MET B 2 142 ? 10.981 7.205 45.491 1.00 115.23 ? 142 MET B CA 1 ATOM 8257 C C . MET B 2 142 ? 10.995 5.698 45.272 1.00 114.43 ? 142 MET B C 1 ATOM 8258 O O . MET B 2 142 ? 10.095 5.147 44.636 1.00 117.69 ? 142 MET B O 1 ATOM 8259 C CB . MET B 2 142 ? 11.418 7.925 44.215 1.00 110.04 ? 142 MET B CB 1 ATOM 8260 C CG . MET B 2 142 ? 11.035 9.389 44.180 1.00 97.24 ? 142 MET B CG 1 ATOM 8261 S SD . MET B 2 142 ? 9.260 9.619 44.388 1.00 124.44 ? 142 MET B SD 1 ATOM 8262 C CE . MET B 2 142 ? 8.634 8.754 42.949 1.00 108.84 ? 142 MET B CE 1 ATOM 8263 N N . ARG B 2 143 ? 12.022 5.038 45.799 1.00 111.96 ? 143 ARG B N 1 ATOM 8264 C CA . ARG B 2 143 ? 12.140 3.590 45.696 1.00 120.23 ? 143 ARG B CA 1 ATOM 8265 C C . ARG B 2 143 ? 10.941 2.913 46.344 1.00 113.87 ? 143 ARG B C 1 ATOM 8266 O O . ARG B 2 143 ? 10.461 1.889 45.862 1.00 127.00 ? 143 ARG B O 1 ATOM 8267 C CB . ARG B 2 143 ? 13.438 3.107 46.350 1.00 129.51 ? 143 ARG B CB 1 ATOM 8268 C CG . ARG B 2 143 ? 13.722 1.625 46.185 1.00 127.57 ? 143 ARG B CG 1 ATOM 8269 C CD . ARG B 2 143 ? 15.072 1.258 46.783 1.00 124.19 ? 143 ARG B CD 1 ATOM 8270 N NE . ARG B 2 143 ? 15.298 -0.185 46.762 1.00 157.42 ? 143 ARG B NE 1 ATOM 8271 C CZ . ARG B 2 143 ? 16.367 -0.785 47.278 1.00 160.00 ? 143 ARG B CZ 1 ATOM 8272 N NH1 . ARG B 2 143 ? 17.318 -0.067 47.860 1.00 167.44 ? 143 ARG B NH1 1 ATOM 8273 N NH2 . ARG B 2 143 ? 16.485 -2.105 47.212 1.00 144.72 ? 143 ARG B NH2 1 ATOM 8274 N N . LYS B 2 144 ? 10.460 3.502 47.435 1.00 114.24 ? 144 LYS B N 1 ATOM 8275 C CA . LYS B 2 144 ? 9.334 2.956 48.181 1.00 115.71 ? 144 LYS B CA 1 ATOM 8276 C C . LYS B 2 144 ? 8.065 2.937 47.338 1.00 118.43 ? 144 LYS B C 1 ATOM 8277 O O . LYS B 2 144 ? 7.350 1.935 47.294 1.00 135.89 ? 144 LYS B O 1 ATOM 8278 C CB . LYS B 2 144 ? 9.102 3.765 49.459 1.00 116.59 ? 144 LYS B CB 1 ATOM 8279 C CG . LYS B 2 144 ? 10.353 3.962 50.302 1.00 129.57 ? 144 LYS B CG 1 ATOM 8280 C CD . LYS B 2 144 ? 10.929 2.632 50.762 1.00 140.14 ? 144 LYS B CD 1 ATOM 8281 C CE . LYS B 2 144 ? 12.255 2.822 51.483 1.00 145.87 ? 144 LYS B CE 1 ATOM 8282 N NZ . LYS B 2 144 ? 13.302 3.392 50.589 1.00 128.22 ? 144 LYS B NZ 1 ATOM 8283 N N . LEU B 2 145 ? 7.791 4.053 46.673 1.00 124.16 ? 145 LEU B N 1 ATOM 8284 C CA . LEU B 2 145 ? 6.606 4.182 45.833 1.00 125.88 ? 145 LEU B CA 1 ATOM 8285 C C . LEU B 2 145 ? 6.790 3.548 44.455 1.00 114.85 ? 145 LEU B C 1 ATOM 8286 O O . LEU B 2 145 ? 5.844 3.009 43.884 1.00 109.60 ? 145 LEU B O 1 ATOM 8287 C CB . LEU B 2 145 ? 6.227 5.656 45.679 1.00 128.74 ? 145 LEU B CB 1 ATOM 8288 C CG . LEU B 2 145 ? 5.985 6.415 46.985 1.00 130.68 ? 145 LEU B CG 1 ATOM 8289 C CD1 . LEU B 2 145 ? 5.560 7.847 46.700 1.00 126.76 ? 145 LEU B CD1 1 ATOM 8290 C CD2 . LEU B 2 145 ? 4.951 5.699 47.846 1.00 111.01 ? 145 LEU B CD2 1 ATOM 8291 N N . THR B 2 146 ? 8.005 3.622 43.920 1.00 123.54 ? 146 THR B N 1 ATOM 8292 C CA . THR B 2 146 ? 8.262 3.141 42.566 1.00 119.33 ? 146 THR B CA 1 ATOM 8293 C C . THR B 2 146 ? 9.606 2.427 42.429 1.00 130.53 ? 146 THR B C 1 ATOM 8294 O O . THR B 2 146 ? 10.636 2.930 42.878 1.00 133.88 ? 146 THR B O 1 ATOM 8295 C CB . THR B 2 146 ? 8.210 4.301 41.557 1.00 126.83 ? 146 THR B CB 1 ATOM 8296 O OG1 . THR B 2 146 ? 6.880 4.831 41.506 1.00 137.33 ? 146 THR B OG1 1 ATOM 8297 C CG2 . THR B 2 146 ? 8.602 3.821 40.180 1.00 116.31 ? 146 THR B CG2 1 ATOM 8298 N N . SER B 2 147 ? 9.587 1.254 41.802 1.00 129.12 ? 147 SER B N 1 ATOM 8299 C CA . SER B 2 147 ? 10.803 0.479 41.575 1.00 132.84 ? 147 SER B CA 1 ATOM 8300 C C . SER B 2 147 ? 11.601 1.001 40.384 1.00 138.68 ? 147 SER B C 1 ATOM 8301 O O . SER B 2 147 ? 12.830 0.927 40.375 1.00 145.25 ? 147 SER B O 1 ATOM 8302 C CB . SER B 2 147 ? 10.467 -0.998 41.359 1.00 123.85 ? 147 SER B CB 1 ATOM 8303 O OG . SER B 2 147 ? 9.754 -1.183 40.149 1.00 128.12 ? 147 SER B OG 1 ATOM 8304 N N . ASN B 2 148 ? 10.904 1.522 39.378 1.00 124.51 ? 148 ASN B N 1 ATOM 8305 C CA . ASN B 2 148 ? 11.575 2.026 38.186 1.00 121.76 ? 148 ASN B CA 1 ATOM 8306 C C . ASN B 2 148 ? 11.573 3.554 38.146 1.00 119.67 ? 148 ASN B C 1 ATOM 8307 O O . ASN B 2 148 ? 10.554 4.177 37.846 1.00 104.78 ? 148 ASN B O 1 ATOM 8308 C CB . ASN B 2 148 ? 10.902 1.459 36.932 1.00 114.55 ? 148 ASN B CB 1 ATOM 8309 C CG . ASN B 2 148 ? 11.804 1.495 35.713 1.00 124.73 ? 148 ASN B CG 1 ATOM 8310 O OD1 . ASN B 2 148 ? 12.594 2.423 35.532 1.00 128.67 ? 148 ASN B OD1 1 ATOM 8311 N ND2 . ASN B 2 148 ? 11.688 0.478 34.865 1.00 103.73 ? 148 ASN B ND2 1 ATOM 8312 N N . LEU B 2 149 ? 12.734 4.149 38.404 1.00 114.30 ? 149 LEU B N 1 ATOM 8313 C CA . LEU B 2 149 ? 12.841 5.599 38.536 1.00 98.16 ? 149 LEU B CA 1 ATOM 8314 C C . LEU B 2 149 ? 13.864 6.185 37.571 1.00 99.71 ? 149 LEU B C 1 ATOM 8315 O O . LEU B 2 149 ? 14.881 5.560 37.272 1.00 99.63 ? 149 LEU B O 1 ATOM 8316 C CB . LEU B 2 149 ? 13.209 5.978 39.975 1.00 109.79 ? 149 LEU B CB 1 ATOM 8317 C CG . LEU B 2 149 ? 13.381 7.468 40.302 1.00 97.50 ? 149 LEU B CG 1 ATOM 8318 C CD1 . LEU B 2 149 ? 12.041 8.185 40.318 1.00 94.50 ? 149 LEU B CD1 1 ATOM 8319 C CD2 . LEU B 2 149 ? 14.110 7.662 41.623 1.00 100.00 ? 149 LEU B CD2 1 ATOM 8320 N N . ARG B 2 150 ? 13.581 7.388 37.084 1.00 102.25 ? 150 ARG B N 1 ATOM 8321 C CA . ARG B 2 150 ? 14.509 8.115 36.229 1.00 102.64 ? 150 ARG B CA 1 ATOM 8322 C C . ARG B 2 150 ? 14.646 9.555 36.706 1.00 99.86 ? 150 ARG B C 1 ATOM 8323 O O . ARG B 2 150 ? 13.650 10.196 37.038 1.00 104.18 ? 150 ARG B O 1 ATOM 8324 C CB . ARG B 2 150 ? 14.036 8.095 34.775 1.00 106.05 ? 150 ARG B CB 1 ATOM 8325 C CG . ARG B 2 150 ? 13.888 6.719 34.165 1.00 97.97 ? 150 ARG B CG 1 ATOM 8326 C CD . ARG B 2 150 ? 15.240 6.137 33.812 1.00 120.69 ? 150 ARG B CD 1 ATOM 8327 N NE . ARG B 2 150 ? 15.166 5.240 32.663 1.00 140.15 ? 150 ARG B NE 1 ATOM 8328 C CZ . ARG B 2 150 ? 15.154 5.650 31.399 1.00 133.50 ? 150 ARG B CZ 1 ATOM 8329 N NH1 . ARG B 2 150 ? 15.203 6.947 31.121 1.00 127.86 ? 150 ARG B NH1 1 ATOM 8330 N NH2 . ARG B 2 150 ? 15.088 4.767 30.413 1.00 116.60 ? 150 ARG B NH2 1 ATOM 8331 N N . ILE B 2 151 ? 15.873 10.066 36.744 1.00 106.06 ? 151 ILE B N 1 ATOM 8332 C CA . ILE B 2 151 ? 16.086 11.475 37.066 1.00 102.04 ? 151 ILE B CA 1 ATOM 8333 C C . ILE B 2 151 ? 16.942 12.161 36.012 1.00 102.09 ? 151 ILE B C 1 ATOM 8334 O O . ILE B 2 151 ? 17.752 11.525 35.337 1.00 108.47 ? 151 ILE B O 1 ATOM 8335 C CB . ILE B 2 151 ? 16.747 11.666 38.448 1.00 93.27 ? 151 ILE B CB 1 ATOM 8336 C CG1 . ILE B 2 151 ? 18.035 10.852 38.550 1.00 112.74 ? 151 ILE B CG1 1 ATOM 8337 C CG2 . ILE B 2 151 ? 15.792 11.277 39.559 1.00 109.27 ? 151 ILE B CG2 1 ATOM 8338 C CD1 . ILE B 2 151 ? 18.616 10.834 39.944 1.00 119.10 ? 151 ILE B CD1 1 ATOM 8339 N N . GLY B 2 152 ? 16.742 13.467 35.873 1.00 101.91 ? 152 GLY B N 1 ATOM 8340 C CA . GLY B 2 152 ? 17.507 14.276 34.944 1.00 117.11 ? 152 GLY B CA 1 ATOM 8341 C C . GLY B 2 152 ? 17.556 15.716 35.416 1.00 111.35 ? 152 GLY B C 1 ATOM 8342 O O . GLY B 2 152 ? 16.690 16.157 36.172 1.00 101.38 ? 152 GLY B O 1 ATOM 8343 N N . PHE B 2 153 ? 18.564 16.456 34.967 1.00 104.64 ? 153 PHE B N 1 ATOM 8344 C CA . PHE B 2 153 ? 18.767 17.819 35.443 1.00 85.28 ? 153 PHE B CA 1 ATOM 8345 C C . PHE B 2 153 ? 18.880 18.818 34.300 1.00 83.85 ? 153 PHE B C 1 ATOM 8346 O O . PHE B 2 153 ? 19.419 18.510 33.236 1.00 81.50 ? 153 PHE B O 1 ATOM 8347 C CB . PHE B 2 153 ? 20.020 17.890 36.321 1.00 89.93 ? 153 PHE B CB 1 ATOM 8348 C CG . PHE B 2 153 ? 20.147 19.169 37.099 1.00 96.05 ? 153 PHE B CG 1 ATOM 8349 C CD1 . PHE B 2 153 ? 19.511 19.317 38.319 1.00 108.61 ? 153 PHE B CD1 1 ATOM 8350 C CD2 . PHE B 2 153 ? 20.910 20.219 36.615 1.00 89.76 ? 153 PHE B CD2 1 ATOM 8351 C CE1 . PHE B 2 153 ? 19.631 20.491 39.038 1.00 117.36 ? 153 PHE B CE1 1 ATOM 8352 C CE2 . PHE B 2 153 ? 21.033 21.394 37.327 1.00 83.32 ? 153 PHE B CE2 1 ATOM 8353 C CZ . PHE B 2 153 ? 20.393 21.532 38.540 1.00 83.50 ? 153 PHE B CZ 1 ATOM 8354 N N . GLY B 2 154 ? 18.372 20.021 34.537 1.00 95.82 ? 154 GLY B N 1 ATOM 8355 C CA . GLY B 2 154 ? 18.468 21.104 33.578 1.00 90.40 ? 154 GLY B CA 1 ATOM 8356 C C . GLY B 2 154 ? 18.444 22.439 34.295 1.00 91.44 ? 154 GLY B C 1 ATOM 8357 O O . GLY B 2 154 ? 17.903 22.554 35.396 1.00 82.44 ? 154 GLY B O 1 ATOM 8358 N N . ALA B 2 155 ? 19.018 23.458 33.667 1.00 92.71 ? 155 ALA B N 1 ATOM 8359 C CA . ALA B 2 155 ? 19.198 24.737 34.336 1.00 80.83 ? 155 ALA B CA 1 ATOM 8360 C C . ALA B 2 155 ? 18.801 25.910 33.458 1.00 78.03 ? 155 ALA B C 1 ATOM 8361 O O . ALA B 2 155 ? 18.805 25.815 32.231 1.00 89.99 ? 155 ALA B O 1 ATOM 8362 C CB . ALA B 2 155 ? 20.635 24.888 34.784 1.00 82.24 ? 155 ALA B CB 1 ATOM 8363 N N . PHE B 2 156 ? 18.465 27.019 34.105 1.00 75.25 ? 156 PHE B N 1 ATOM 8364 C CA . PHE B 2 156 ? 18.086 28.236 33.404 1.00 90.41 ? 156 PHE B CA 1 ATOM 8365 C C . PHE B 2 156 ? 18.493 29.460 34.215 1.00 90.89 ? 156 PHE B C 1 ATOM 8366 O O . PHE B 2 156 ? 18.578 29.400 35.444 1.00 73.28 ? 156 PHE B O 1 ATOM 8367 C CB . PHE B 2 156 ? 16.579 28.260 33.142 1.00 73.19 ? 156 PHE B CB 1 ATOM 8368 C CG . PHE B 2 156 ? 15.754 28.488 34.379 1.00 82.68 ? 156 PHE B CG 1 ATOM 8369 C CD1 . PHE B 2 156 ? 15.416 27.430 35.205 1.00 86.37 ? 156 PHE B CD1 1 ATOM 8370 C CD2 . PHE B 2 156 ? 15.323 29.761 34.719 1.00 82.58 ? 156 PHE B CD2 1 ATOM 8371 C CE1 . PHE B 2 156 ? 14.662 27.637 36.346 1.00 91.72 ? 156 PHE B CE1 1 ATOM 8372 C CE2 . PHE B 2 156 ? 14.570 29.973 35.856 1.00 82.32 ? 156 PHE B CE2 1 ATOM 8373 C CZ . PHE B 2 156 ? 14.239 28.910 36.671 1.00 86.73 ? 156 PHE B CZ 1 ATOM 8374 N N . VAL B 2 157 ? 18.749 30.566 33.523 1.00 81.67 ? 157 VAL B N 1 ATOM 8375 C CA . VAL B 2 157 ? 18.955 31.848 34.183 1.00 83.47 ? 157 VAL B CA 1 ATOM 8376 C C . VAL B 2 157 ? 17.956 32.863 33.641 1.00 83.31 ? 157 VAL B C 1 ATOM 8377 O O . VAL B 2 157 ? 16.974 33.201 34.302 1.00 88.17 ? 157 VAL B O 1 ATOM 8378 C CB . VAL B 2 157 ? 20.385 32.381 33.984 1.00 78.86 ? 157 VAL B CB 1 ATOM 8379 C CG1 . VAL B 2 157 ? 20.552 33.715 34.692 1.00 98.31 ? 157 VAL B CG1 1 ATOM 8380 C CG2 . VAL B 2 157 ? 21.404 31.378 34.494 1.00 83.19 ? 157 VAL B CG2 1 ATOM 8381 N N . ASP B 2 158 ? 18.200 33.307 32.414 1.00 70.31 ? 158 ASP B N 1 ATOM 8382 C CA . ASP B 2 158 ? 17.379 34.318 31.762 1.00 68.78 ? 158 ASP B CA 1 ATOM 8383 C C . ASP B 2 158 ? 17.917 34.518 30.355 1.00 69.64 ? 158 ASP B C 1 ATOM 8384 O O . ASP B 2 158 ? 18.951 33.959 30.000 1.00 71.50 ? 158 ASP B O 1 ATOM 8385 C CB . ASP B 2 158 ? 17.399 35.633 32.545 1.00 69.65 ? 158 ASP B CB 1 ATOM 8386 C CG . ASP B 2 158 ? 16.133 36.444 32.363 1.00 72.33 ? 158 ASP B CG 1 ATOM 8387 O OD1 . ASP B 2 158 ? 15.489 36.302 31.301 1.00 65.79 ? 158 ASP B OD1 1 ATOM 8388 O OD2 . ASP B 2 158 ? 15.789 37.225 33.284 1.00 70.06 ? 158 ASP B OD2 1 ATOM 8389 N N . LYS B 2 159 ? 17.216 35.303 29.549 1.00 68.55 ? 159 LYS B N 1 ATOM 8390 C CA . LYS B 2 159 ? 17.663 35.575 28.190 1.00 69.60 ? 159 LYS B CA 1 ATOM 8391 C C . LYS B 2 159 ? 18.994 36.326 28.185 1.00 81.52 ? 159 LYS B C 1 ATOM 8392 O O . LYS B 2 159 ? 19.094 37.423 28.733 1.00 77.99 ? 159 LYS B O 1 ATOM 8393 C CB . LYS B 2 159 ? 16.604 36.374 27.436 1.00 68.15 ? 159 LYS B CB 1 ATOM 8394 C CG . LYS B 2 159 ? 15.371 35.576 27.080 1.00 66.90 ? 159 LYS B CG 1 ATOM 8395 C CD . LYS B 2 159 ? 14.301 36.467 26.484 1.00 69.55 ? 159 LYS B CD 1 ATOM 8396 C CE . LYS B 2 159 ? 13.274 35.651 25.721 1.00 69.63 ? 159 LYS B CE 1 ATOM 8397 N NZ . LYS B 2 159 ? 12.836 34.447 26.473 1.00 81.78 ? 159 LYS B NZ 1 ATOM 8398 N N . PRO B 2 160 ? 20.024 35.731 27.562 1.00 82.10 ? 160 PRO B N 1 ATOM 8399 C CA . PRO B 2 160 ? 21.372 36.309 27.507 1.00 80.29 ? 160 PRO B CA 1 ATOM 8400 C C . PRO B 2 160 ? 21.457 37.494 26.552 1.00 92.53 ? 160 PRO B C 1 ATOM 8401 O O . PRO B 2 160 ? 22.185 37.444 25.562 1.00 90.32 ? 160 PRO B O 1 ATOM 8402 C CB . PRO B 2 160 ? 22.225 35.147 27.004 1.00 77.94 ? 160 PRO B CB 1 ATOM 8403 C CG . PRO B 2 160 ? 21.289 34.357 26.164 1.00 83.39 ? 160 PRO B CG 1 ATOM 8404 C CD . PRO B 2 160 ? 19.948 34.448 26.843 1.00 78.12 ? 160 PRO B CD 1 ATOM 8405 N N . VAL B 2 161 ? 20.712 38.548 26.856 1.00 86.23 ? 161 VAL B N 1 ATOM 8406 C CA . VAL B 2 161 ? 20.687 39.741 26.026 1.00 81.59 ? 161 VAL B CA 1 ATOM 8407 C C . VAL B 2 161 ? 20.283 40.929 26.900 1.00 76.47 ? 161 VAL B C 1 ATOM 8408 O O . VAL B 2 161 ? 19.688 40.746 27.961 1.00 71.64 ? 161 VAL B O 1 ATOM 8409 C CB . VAL B 2 161 ? 19.713 39.570 24.828 1.00 76.05 ? 161 VAL B CB 1 ATOM 8410 C CG1 . VAL B 2 161 ? 18.267 39.533 25.306 1.00 70.87 ? 161 VAL B CG1 1 ATOM 8411 C CG2 . VAL B 2 161 ? 19.916 40.672 23.794 1.00 122.87 ? 161 VAL B CG2 1 ATOM 8412 N N . SER B 2 162 ? 20.625 42.141 26.479 1.00 73.13 ? 162 SER B N 1 ATOM 8413 C CA . SER B 2 162 ? 20.181 43.327 27.199 1.00 86.42 ? 162 SER B CA 1 ATOM 8414 C C . SER B 2 162 ? 18.671 43.462 27.042 1.00 79.16 ? 162 SER B C 1 ATOM 8415 O O . SER B 2 162 ? 18.118 43.047 26.022 1.00 69.69 ? 162 SER B O 1 ATOM 8416 C CB . SER B 2 162 ? 20.899 44.579 26.687 1.00 95.85 ? 162 SER B CB 1 ATOM 8417 O OG . SER B 2 162 ? 20.698 44.750 25.296 1.00 128.52 ? 162 SER B OG 1 ATOM 8418 N N . PRO B 2 163 ? 17.992 44.050 28.043 1.00 77.05 ? 163 PRO B N 1 ATOM 8419 C CA . PRO B 2 163 ? 18.495 44.598 29.310 1.00 85.13 ? 163 PRO B CA 1 ATOM 8420 C C . PRO B 2 163 ? 18.919 43.556 30.348 1.00 70.28 ? 163 PRO B C 1 ATOM 8421 O O . PRO B 2 163 ? 19.633 43.903 31.287 1.00 101.19 ? 163 PRO B O 1 ATOM 8422 C CB . PRO B 2 163 ? 17.304 45.404 29.827 1.00 79.92 ? 163 PRO B CB 1 ATOM 8423 C CG . PRO B 2 163 ? 16.131 44.665 29.316 1.00 83.02 ? 163 PRO B CG 1 ATOM 8424 C CD . PRO B 2 163 ? 16.525 44.150 27.957 1.00 67.03 ? 163 PRO B CD 1 ATOM 8425 N N . TYR B 2 164 ? 18.479 42.313 30.191 1.00 68.84 ? 164 TYR B N 1 ATOM 8426 C CA . TYR B 2 164 ? 18.651 41.303 31.236 1.00 79.74 ? 164 TYR B CA 1 ATOM 8427 C C . TYR B 2 164 ? 20.113 40.972 31.538 1.00 71.02 ? 164 TYR B C 1 ATOM 8428 O O . TYR B 2 164 ? 20.501 40.861 32.699 1.00 71.64 ? 164 TYR B O 1 ATOM 8429 C CB . TYR B 2 164 ? 17.907 40.015 30.858 1.00 81.32 ? 164 TYR B CB 1 ATOM 8430 C CG . TYR B 2 164 ? 16.554 40.248 30.224 1.00 75.63 ? 164 TYR B CG 1 ATOM 8431 C CD1 . TYR B 2 164 ? 15.541 40.891 30.922 1.00 83.93 ? 164 TYR B CD1 1 ATOM 8432 C CD2 . TYR B 2 164 ? 16.289 39.824 28.928 1.00 71.27 ? 164 TYR B CD2 1 ATOM 8433 C CE1 . TYR B 2 164 ? 14.303 41.110 30.347 1.00 97.81 ? 164 TYR B CE1 1 ATOM 8434 C CE2 . TYR B 2 164 ? 15.053 40.037 28.345 1.00 73.02 ? 164 TYR B CE2 1 ATOM 8435 C CZ . TYR B 2 164 ? 14.064 40.682 29.060 1.00 92.60 ? 164 TYR B CZ 1 ATOM 8436 O OH . TYR B 2 164 ? 12.830 40.899 28.489 1.00 94.18 ? 164 TYR B OH 1 ATOM 8437 N N . MET B 2 165 ? 20.915 40.806 30.493 1.00 72.28 ? 165 MET B N 1 ATOM 8438 C CA . MET B 2 165 ? 22.303 40.378 30.644 1.00 74.44 ? 165 MET B CA 1 ATOM 8439 C C . MET B 2 165 ? 23.228 41.517 31.064 1.00 84.07 ? 165 MET B C 1 ATOM 8440 O O . MET B 2 165 ? 22.939 42.686 30.804 1.00 76.82 ? 165 MET B O 1 ATOM 8441 C CB . MET B 2 165 ? 22.806 39.767 29.331 1.00 77.55 ? 165 MET B CB 1 ATOM 8442 C CG . MET B 2 165 ? 24.155 39.069 29.435 1.00 89.08 ? 165 MET B CG 1 ATOM 8443 S SD . MET B 2 165 ? 24.721 38.347 27.885 1.00 84.24 ? 165 MET B SD 1 ATOM 8444 C CE . MET B 2 165 ? 26.153 37.430 28.453 1.00 143.47 ? 165 MET B CE 1 ATOM 8445 N N . TYR B 2 166 ? 24.342 41.179 31.712 1.00 86.11 ? 166 TYR B N 1 ATOM 8446 C CA . TYR B 2 166 ? 25.401 42.158 31.890 1.00 81.48 ? 166 TYR B CA 1 ATOM 8447 C C . TYR B 2 166 ? 26.148 42.230 30.565 1.00 88.34 ? 166 TYR B C 1 ATOM 8448 O O . TYR B 2 166 ? 26.790 41.267 30.145 1.00 87.71 ? 166 TYR B O 1 ATOM 8449 C CB . TYR B 2 166 ? 26.343 41.768 33.033 1.00 80.46 ? 166 TYR B CB 1 ATOM 8450 C CG . TYR B 2 166 ? 25.859 42.157 34.412 1.00 79.79 ? 166 TYR B CG 1 ATOM 8451 C CD1 . TYR B 2 166 ? 24.863 41.436 35.051 1.00 83.59 ? 166 TYR B CD1 1 ATOM 8452 C CD2 . TYR B 2 166 ? 26.412 43.239 35.082 1.00 82.48 ? 166 TYR B CD2 1 ATOM 8453 C CE1 . TYR B 2 166 ? 24.421 41.788 36.315 1.00 87.08 ? 166 TYR B CE1 1 ATOM 8454 C CE2 . TYR B 2 166 ? 25.978 43.598 36.346 1.00 94.02 ? 166 TYR B CE2 1 ATOM 8455 C CZ . TYR B 2 166 ? 24.981 42.869 36.957 1.00 87.27 ? 166 TYR B CZ 1 ATOM 8456 O OH . TYR B 2 166 ? 24.544 43.222 38.214 1.00 94.50 ? 166 TYR B OH 1 ATOM 8457 N N . ILE B 2 167 ? 26.057 43.382 29.914 1.00 91.61 ? 167 ILE B N 1 ATOM 8458 C CA . ILE B 2 167 ? 26.601 43.556 28.576 1.00 86.11 ? 167 ILE B CA 1 ATOM 8459 C C . ILE B 2 167 ? 27.954 44.267 28.616 1.00 95.78 ? 167 ILE B C 1 ATOM 8460 O O . ILE B 2 167 ? 28.629 44.401 27.593 1.00 95.53 ? 167 ILE B O 1 ATOM 8461 C CB . ILE B 2 167 ? 25.603 44.344 27.691 1.00 96.21 ? 167 ILE B CB 1 ATOM 8462 C CG1 . ILE B 2 167 ? 25.919 44.175 26.203 1.00 119.04 ? 167 ILE B CG1 1 ATOM 8463 C CG2 . ILE B 2 167 ? 25.557 45.812 28.101 1.00 89.53 ? 167 ILE B CG2 1 ATOM 8464 C CD1 . ILE B 2 167 ? 25.026 45.001 25.298 1.00 125.14 ? 167 ILE B CD1 1 ATOM 8465 N N . SER B 2 168 ? 28.367 44.674 29.813 1.00 98.13 ? 168 SER B N 1 ATOM 8466 C CA . SER B 2 168 ? 29.515 45.564 29.972 1.00 96.89 ? 168 SER B CA 1 ATOM 8467 C C . SER B 2 168 ? 29.832 45.799 31.452 1.00 97.57 ? 168 SER B C 1 ATOM 8468 O O . SER B 2 168 ? 28.945 45.697 32.299 1.00 92.42 ? 168 SER B O 1 ATOM 8469 C CB . SER B 2 168 ? 29.253 46.903 29.273 1.00 98.66 ? 168 SER B CB 1 ATOM 8470 O OG . SER B 2 168 ? 28.143 47.569 29.849 1.00 111.72 ? 168 SER B OG 1 ATOM 8471 N N . PRO B 2 169 ? 31.100 46.115 31.775 1.00 101.21 ? 169 PRO B N 1 ATOM 8472 C CA . PRO B 2 169 ? 32.260 46.325 30.896 1.00 98.13 ? 169 PRO B CA 1 ATOM 8473 C C . PRO B 2 169 ? 32.699 45.050 30.181 1.00 111.50 ? 169 PRO B C 1 ATOM 8474 O O . PRO B 2 169 ? 32.339 43.962 30.625 1.00 102.75 ? 169 PRO B O 1 ATOM 8475 C CB . PRO B 2 169 ? 33.346 46.806 31.865 1.00 94.06 ? 169 PRO B CB 1 ATOM 8476 C CG . PRO B 2 169 ? 32.960 46.228 33.172 1.00 91.22 ? 169 PRO B CG 1 ATOM 8477 C CD . PRO B 2 169 ? 31.462 46.267 33.195 1.00 95.78 ? 169 PRO B CD 1 ATOM 8478 N N . PRO B 2 170 ? 33.452 45.184 29.076 1.00 131.17 ? 170 PRO B N 1 ATOM 8479 C CA . PRO B 2 170 ? 33.948 44.006 28.357 1.00 129.80 ? 170 PRO B CA 1 ATOM 8480 C C . PRO B 2 170 ? 34.797 43.126 29.265 1.00 134.63 ? 170 PRO B C 1 ATOM 8481 O O . PRO B 2 170 ? 34.892 41.916 29.051 1.00 122.68 ? 170 PRO B O 1 ATOM 8482 C CB . PRO B 2 170 ? 34.786 44.608 27.223 1.00 129.61 ? 170 PRO B CB 1 ATOM 8483 C CG . PRO B 2 170 ? 35.110 45.999 27.678 1.00 133.60 ? 170 PRO B CG 1 ATOM 8484 C CD . PRO B 2 170 ? 33.913 46.438 28.457 1.00 139.39 ? 170 PRO B CD 1 ATOM 8485 N N . GLU B 2 171 ? 35.401 43.749 30.274 1.00 148.82 ? 171 GLU B N 1 ATOM 8486 C CA . GLU B 2 171 ? 36.155 43.038 31.296 1.00 150.93 ? 171 GLU B CA 1 ATOM 8487 C C . GLU B 2 171 ? 35.292 41.971 31.961 1.00 137.74 ? 171 GLU B C 1 ATOM 8488 O O . GLU B 2 171 ? 35.786 40.904 32.326 1.00 133.31 ? 171 GLU B O 1 ATOM 8489 C CB . GLU B 2 171 ? 36.695 44.021 32.337 1.00 147.13 ? 171 GLU B CB 1 ATOM 8490 C CG . GLU B 2 171 ? 37.716 45.003 31.780 1.00 152.04 ? 171 GLU B CG 1 ATOM 8491 C CD . GLU B 2 171 ? 37.991 46.164 32.716 1.00 164.77 ? 171 GLU B CD 1 ATOM 8492 O OE1 . GLU B 2 171 ? 39.157 46.608 32.790 1.00 166.14 ? 171 GLU B OE1 1 ATOM 8493 O OE2 . GLU B 2 171 ? 37.039 46.639 33.371 1.00 166.44 ? 171 GLU B OE2 1 ATOM 8494 N N . ALA B 2 172 ? 34.003 42.257 32.121 1.00 128.84 ? 172 ALA B N 1 ATOM 8495 C CA . ALA B 2 172 ? 33.083 41.235 32.596 1.00 123.02 ? 172 ALA B CA 1 ATOM 8496 C C . ALA B 2 172 ? 32.056 40.857 31.535 1.00 129.85 ? 172 ALA B C 1 ATOM 8497 O O . ALA B 2 172 ? 31.080 41.568 31.306 1.00 145.74 ? 172 ALA B O 1 ATOM 8498 C CB . ALA B 2 172 ? 32.381 41.712 33.845 1.00 117.74 ? 172 ALA B CB 1 ATOM 8499 N N . LEU B 2 173 ? 32.287 39.713 30.910 1.00 116.77 ? 173 LEU B N 1 ATOM 8500 C CA . LEU B 2 173 ? 31.317 39.047 30.059 1.00 105.64 ? 173 LEU B CA 1 ATOM 8501 C C . LEU B 2 173 ? 31.354 37.585 30.449 1.00 115.58 ? 173 LEU B C 1 ATOM 8502 O O . LEU B 2 173 ? 30.366 37.017 30.911 1.00 143.24 ? 173 LEU B O 1 ATOM 8503 C CB . LEU B 2 173 ? 31.629 39.250 28.578 1.00 121.38 ? 173 LEU B CB 1 ATOM 8504 C CG . LEU B 2 173 ? 31.114 40.573 28.006 1.00 104.57 ? 173 LEU B CG 1 ATOM 8505 C CD1 . LEU B 2 173 ? 31.538 40.754 26.557 1.00 95.41 ? 173 LEU B CD1 1 ATOM 8506 C CD2 . LEU B 2 173 ? 29.600 40.637 28.135 1.00 101.44 ? 173 LEU B CD2 1 ATOM 8507 N N . GLU B 2 174 ? 32.524 36.989 30.238 1.00 115.27 ? 174 GLU B N 1 ATOM 8508 C CA . GLU B 2 174 ? 32.835 35.650 30.719 1.00 131.28 ? 174 GLU B CA 1 ATOM 8509 C C . GLU B 2 174 ? 32.678 35.557 32.234 1.00 123.77 ? 174 GLU B C 1 ATOM 8510 O O . GLU B 2 174 ? 32.561 34.466 32.790 1.00 134.62 ? 174 GLU B O 1 ATOM 8511 C CB . GLU B 2 174 ? 34.259 35.260 30.319 1.00 147.42 ? 174 GLU B CB 1 ATOM 8512 C CG . GLU B 2 174 ? 34.535 35.351 28.827 1.00 159.00 ? 174 GLU B CG 1 ATOM 8513 C CD . GLU B 2 174 ? 36.004 35.167 28.497 1.00 166.57 ? 174 GLU B CD 1 ATOM 8514 O OE1 . GLU B 2 174 ? 36.836 35.229 29.426 1.00 158.87 ? 174 GLU B OE1 1 ATOM 8515 O OE2 . GLU B 2 174 ? 36.326 34.962 27.307 1.00 169.54 ? 174 GLU B OE2 1 ATOM 8516 N N . ASN B 2 175 ? 32.691 36.708 32.898 1.00 106.29 ? 175 ASN B N 1 ATOM 8517 C CA . ASN B 2 175 ? 32.458 36.765 34.333 1.00 107.61 ? 175 ASN B CA 1 ATOM 8518 C C . ASN B 2 175 ? 31.427 37.829 34.697 1.00 107.17 ? 175 ASN B C 1 ATOM 8519 O O . ASN B 2 175 ? 31.790 38.917 35.139 1.00 107.89 ? 175 ASN B O 1 ATOM 8520 C CB . ASN B 2 175 ? 33.768 37.033 35.072 1.00 109.05 ? 175 ASN B CB 1 ATOM 8521 C CG . ASN B 2 175 ? 33.619 36.922 36.573 1.00 116.45 ? 175 ASN B CG 1 ATOM 8522 O OD1 . ASN B 2 175 ? 32.705 36.264 37.068 1.00 100.81 ? 175 ASN B OD1 1 ATOM 8523 N ND2 . ASN B 2 175 ? 34.515 37.570 37.308 1.00 144.83 ? 175 ASN B ND2 1 ATOM 8524 N N . PRO B 2 176 ? 30.133 37.512 34.523 1.00 110.05 ? 176 PRO B N 1 ATOM 8525 C CA . PRO B 2 176 ? 29.051 38.471 34.776 1.00 94.18 ? 176 PRO B CA 1 ATOM 8526 C C . PRO B 2 176 ? 29.069 39.017 36.200 1.00 90.64 ? 176 PRO B C 1 ATOM 8527 O O . PRO B 2 176 ? 28.541 40.100 36.442 1.00 110.84 ? 176 PRO B O 1 ATOM 8528 C CB . PRO B 2 176 ? 27.779 37.652 34.519 1.00 90.25 ? 176 PRO B CB 1 ATOM 8529 C CG . PRO B 2 176 ? 28.203 36.227 34.613 1.00 92.10 ? 176 PRO B CG 1 ATOM 8530 C CD . PRO B 2 176 ? 29.616 36.190 34.128 1.00 101.04 ? 176 PRO B CD 1 ATOM 8531 N N . CYS B 2 177 ? 29.669 38.281 37.129 1.00 88.37 ? 177 CYS B N 1 ATOM 8532 C CA . CYS B 2 177 ? 29.872 38.810 38.468 1.00 98.64 ? 177 CYS B CA 1 ATOM 8533 C C . CYS B 2 177 ? 31.322 39.258 38.603 1.00 125.06 ? 177 CYS B C 1 ATOM 8534 O O . CYS B 2 177 ? 32.235 38.445 38.713 1.00 132.61 ? 177 CYS B O 1 ATOM 8535 C CB . CYS B 2 177 ? 29.511 37.771 39.534 1.00 92.99 ? 177 CYS B CB 1 ATOM 8536 S SG . CYS B 2 177 ? 30.154 36.108 39.238 1.00 174.99 ? 177 CYS B SG 1 ATOM 8537 N N . TYR B 2 178 ? 31.512 40.570 38.618 1.00 121.27 ? 178 TYR B N 1 ATOM 8538 C CA . TYR B 2 178 ? 32.833 41.174 38.548 1.00 96.94 ? 178 TYR B CA 1 ATOM 8539 C C . TYR B 2 178 ? 33.031 42.054 39.762 1.00 100.22 ? 178 TYR B C 1 ATOM 8540 O O . TYR B 2 178 ? 33.936 41.833 40.565 1.00 114.93 ? 178 TYR B O 1 ATOM 8541 C CB . TYR B 2 178 ? 32.984 41.985 37.265 1.00 99.25 ? 178 TYR B CB 1 ATOM 8542 C CG . TYR B 2 178 ? 34.404 42.378 36.933 1.00 123.29 ? 178 TYR B CG 1 ATOM 8543 C CD1 . TYR B 2 178 ? 35.249 41.500 36.268 1.00 133.13 ? 178 TYR B CD1 1 ATOM 8544 C CD2 . TYR B 2 178 ? 34.895 43.634 37.267 1.00 134.50 ? 178 TYR B CD2 1 ATOM 8545 C CE1 . TYR B 2 178 ? 36.548 41.856 35.955 1.00 139.74 ? 178 TYR B CE1 1 ATOM 8546 C CE2 . TYR B 2 178 ? 36.192 44.000 36.957 1.00 137.78 ? 178 TYR B CE2 1 ATOM 8547 C CZ . TYR B 2 178 ? 37.014 43.107 36.302 1.00 144.14 ? 178 TYR B CZ 1 ATOM 8548 O OH . TYR B 2 178 ? 38.306 43.466 35.992 1.00 152.84 ? 178 TYR B OH 1 ATOM 8549 N N . ASP B 2 179 ? 32.165 43.055 39.883 1.00 96.08 ? 179 ASP B N 1 ATOM 8550 C CA . ASP B 2 179 ? 32.160 43.963 41.025 1.00 112.89 ? 179 ASP B CA 1 ATOM 8551 C C . ASP B 2 179 ? 31.952 43.220 42.342 1.00 113.76 ? 179 ASP B C 1 ATOM 8552 O O . ASP B 2 179 ? 32.159 43.777 43.420 1.00 109.59 ? 179 ASP B O 1 ATOM 8553 C CB . ASP B 2 179 ? 31.072 45.021 40.848 1.00 121.49 ? 179 ASP B CB 1 ATOM 8554 C CG . ASP B 2 179 ? 29.742 44.424 40.428 1.00 112.70 ? 179 ASP B CG 1 ATOM 8555 O OD1 . ASP B 2 179 ? 28.989 43.961 41.312 1.00 105.64 ? 179 ASP B OD1 1 ATOM 8556 O OD2 . ASP B 2 179 ? 29.451 44.419 39.213 1.00 111.22 ? 179 ASP B OD2 1 ATOM 8557 N N . MET B 2 180 ? 31.539 41.961 42.245 1.00 118.11 ? 180 MET B N 1 ATOM 8558 C CA . MET B 2 180 ? 31.379 41.105 43.410 1.00 112.35 ? 180 MET B CA 1 ATOM 8559 C C . MET B 2 180 ? 32.727 40.571 43.883 1.00 119.13 ? 180 MET B C 1 ATOM 8560 O O . MET B 2 180 ? 32.817 39.932 44.933 1.00 119.20 ? 180 MET B O 1 ATOM 8561 C CB . MET B 2 180 ? 30.438 39.951 43.084 1.00 97.20 ? 180 MET B CB 1 ATOM 8562 C CG . MET B 2 180 ? 29.343 40.333 42.114 1.00 94.96 ? 180 MET B CG 1 ATOM 8563 S SD . MET B 2 180 ? 27.736 39.734 42.643 1.00 143.80 ? 180 MET B SD 1 ATOM 8564 C CE . MET B 2 180 ? 28.089 37.996 42.868 1.00 91.52 ? 180 MET B CE 1 ATOM 8565 N N . LYS B 2 181 ? 33.764 40.839 43.093 1.00 122.29 ? 181 LYS B N 1 ATOM 8566 C CA . LYS B 2 181 ? 35.131 40.417 43.393 1.00 125.16 ? 181 LYS B CA 1 ATOM 8567 C C . LYS B 2 181 ? 35.222 38.901 43.539 1.00 115.59 ? 181 LYS B C 1 ATOM 8568 O O . LYS B 2 181 ? 35.928 38.384 44.404 1.00 116.85 ? 181 LYS B O 1 ATOM 8569 C CB . LYS B 2 181 ? 35.646 41.114 44.656 1.00 128.04 ? 181 LYS B CB 1 ATOM 8570 C CG . LYS B 2 181 ? 35.381 42.614 44.679 1.00 129.38 ? 181 LYS B CG 1 ATOM 8571 C CD . LYS B 2 181 ? 36.205 43.316 45.744 1.00 137.91 ? 181 LYS B CD 1 ATOM 8572 C CE . LYS B 2 181 ? 37.644 43.504 45.291 1.00 150.00 ? 181 LYS B CE 1 ATOM 8573 N NZ . LYS B 2 181 ? 37.736 44.394 44.098 1.00 147.31 ? 181 LYS B NZ 1 ATOM 8574 N N . THR B 2 182 ? 34.492 38.199 42.679 1.00 111.98 ? 182 THR B N 1 ATOM 8575 C CA . THR B 2 182 ? 34.521 36.744 42.627 1.00 109.52 ? 182 THR B CA 1 ATOM 8576 C C . THR B 2 182 ? 34.289 36.301 41.185 1.00 106.19 ? 182 THR B C 1 ATOM 8577 O O . THR B 2 182 ? 34.214 37.135 40.285 1.00 116.64 ? 182 THR B O 1 ATOM 8578 C CB . THR B 2 182 ? 33.464 36.116 43.556 1.00 111.00 ? 182 THR B CB 1 ATOM 8579 O OG1 . THR B 2 182 ? 33.588 34.689 43.533 1.00 123.52 ? 182 THR B OG1 1 ATOM 8580 C CG2 . THR B 2 182 ? 32.063 36.511 43.116 1.00 114.81 ? 182 THR B CG2 1 ATOM 8581 N N . THR B 2 183 ? 34.179 34.997 40.958 1.00 103.29 ? 183 THR B N 1 ATOM 8582 C CA . THR B 2 183 ? 34.021 34.490 39.600 1.00 100.51 ? 183 THR B CA 1 ATOM 8583 C C . THR B 2 183 ? 32.816 33.569 39.441 1.00 98.48 ? 183 THR B C 1 ATOM 8584 O O . THR B 2 183 ? 32.667 32.588 40.169 1.00 102.79 ? 183 THR B O 1 ATOM 8585 C CB . THR B 2 183 ? 35.276 33.722 39.134 1.00 115.16 ? 183 THR B CB 1 ATOM 8586 O OG1 . THR B 2 183 ? 35.470 32.569 39.963 1.00 142.95 ? 183 THR B OG1 1 ATOM 8587 C CG2 . THR B 2 183 ? 36.510 34.612 39.201 1.00 109.31 ? 183 THR B CG2 1 ATOM 8588 N N . CYS B 2 184 ? 31.959 33.902 38.482 1.00 102.77 ? 184 CYS B N 1 ATOM 8589 C CA . CYS B 2 184 ? 30.890 33.010 38.052 1.00 103.21 ? 184 CYS B CA 1 ATOM 8590 C C . CYS B 2 184 ? 30.973 32.846 36.537 1.00 102.78 ? 184 CYS B C 1 ATOM 8591 O O . CYS B 2 184 ? 31.904 33.351 35.907 1.00 100.76 ? 184 CYS B O 1 ATOM 8592 C CB . CYS B 2 184 ? 29.518 33.540 38.476 1.00 92.25 ? 184 CYS B CB 1 ATOM 8593 S SG . CYS B 2 184 ? 29.065 35.150 37.815 1.00 111.25 ? 184 CYS B SG 1 ATOM 8594 N N . LEU B 2 185 ? 30.013 32.142 35.949 1.00 91.67 ? 185 LEU B N 1 ATOM 8595 C CA . LEU B 2 185 ? 30.093 31.821 34.528 1.00 95.12 ? 185 LEU B CA 1 ATOM 8596 C C . LEU B 2 185 ? 28.981 32.518 33.755 1.00 88.92 ? 185 LEU B C 1 ATOM 8597 O O . LEU B 2 185 ? 27.931 32.804 34.323 1.00 86.81 ? 185 LEU B O 1 ATOM 8598 C CB . LEU B 2 185 ? 30.040 30.301 34.314 1.00 106.39 ? 185 LEU B CB 1 ATOM 8599 C CG . LEU B 2 185 ? 28.773 29.513 34.644 1.00 102.84 ? 185 LEU B CG 1 ATOM 8600 C CD1 . LEU B 2 185 ? 28.784 28.188 33.899 1.00 96.64 ? 185 LEU B CD1 1 ATOM 8601 C CD2 . LEU B 2 185 ? 28.653 29.273 36.136 1.00 95.03 ? 185 LEU B CD2 1 ATOM 8602 N N . PRO B 2 186 ? 29.219 32.806 32.459 1.00 95.92 ? 186 PRO B N 1 ATOM 8603 C CA . PRO B 2 186 ? 28.268 33.565 31.637 1.00 103.13 ? 186 PRO B CA 1 ATOM 8604 C C . PRO B 2 186 ? 26.862 32.996 31.699 1.00 101.15 ? 186 PRO B C 1 ATOM 8605 O O . PRO B 2 186 ? 26.690 31.778 31.680 1.00 114.62 ? 186 PRO B O 1 ATOM 8606 C CB . PRO B 2 186 ? 28.840 33.431 30.224 1.00 103.46 ? 186 PRO B CB 1 ATOM 8607 C CG . PRO B 2 186 ? 30.284 33.226 30.427 1.00 100.83 ? 186 PRO B CG 1 ATOM 8608 C CD . PRO B 2 186 ? 30.415 32.424 31.687 1.00 102.14 ? 186 PRO B CD 1 ATOM 8609 N N . MET B 2 187 ? 25.870 33.875 31.775 1.00 92.43 ? 187 MET B N 1 ATOM 8610 C CA . MET B 2 187 ? 24.490 33.444 31.919 1.00 92.19 ? 187 MET B CA 1 ATOM 8611 C C . MET B 2 187 ? 24.003 32.719 30.673 1.00 92.58 ? 187 MET B C 1 ATOM 8612 O O . MET B 2 187 ? 24.576 32.859 29.592 1.00 96.16 ? 187 MET B O 1 ATOM 8613 C CB . MET B 2 187 ? 23.587 34.637 32.221 1.00 78.14 ? 187 MET B CB 1 ATOM 8614 C CG . MET B 2 187 ? 23.546 35.668 31.117 1.00 77.83 ? 187 MET B CG 1 ATOM 8615 S SD . MET B 2 187 ? 22.305 36.917 31.465 1.00 120.83 ? 187 MET B SD 1 ATOM 8616 C CE . MET B 2 187 ? 20.862 35.891 31.685 1.00 73.33 ? 187 MET B CE 1 ATOM 8617 N N . PHE B 2 188 ? 22.946 31.935 30.847 1.00 82.98 ? 188 PHE B N 1 ATOM 8618 C CA . PHE B 2 188 ? 22.381 31.129 29.774 1.00 94.10 ? 188 PHE B CA 1 ATOM 8619 C C . PHE B 2 188 ? 20.861 31.107 29.885 1.00 90.75 ? 188 PHE B C 1 ATOM 8620 O O . PHE B 2 188 ? 20.319 31.147 30.990 1.00 97.78 ? 188 PHE B O 1 ATOM 8621 C CB . PHE B 2 188 ? 22.944 29.710 29.834 1.00 103.76 ? 188 PHE B CB 1 ATOM 8622 C CG . PHE B 2 188 ? 23.084 29.181 31.231 1.00 94.69 ? 188 PHE B CG 1 ATOM 8623 C CD1 . PHE B 2 188 ? 22.004 28.609 31.883 1.00 86.73 ? 188 PHE B CD1 1 ATOM 8624 C CD2 . PHE B 2 188 ? 24.293 29.270 31.900 1.00 102.39 ? 188 PHE B CD2 1 ATOM 8625 C CE1 . PHE B 2 188 ? 22.129 28.130 33.172 1.00 78.99 ? 188 PHE B CE1 1 ATOM 8626 C CE2 . PHE B 2 188 ? 24.424 28.792 33.188 1.00 96.02 ? 188 PHE B CE2 1 ATOM 8627 C CZ . PHE B 2 188 ? 23.340 28.222 33.824 1.00 81.90 ? 188 PHE B CZ 1 ATOM 8628 N N . GLY B 2 189 ? 20.171 31.060 28.749 1.00 80.04 ? 189 GLY B N 1 ATOM 8629 C CA . GLY B 2 189 ? 18.721 31.017 28.775 1.00 87.45 ? 189 GLY B CA 1 ATOM 8630 C C . GLY B 2 189 ? 18.213 29.717 29.362 1.00 97.39 ? 189 GLY B C 1 ATOM 8631 O O . GLY B 2 189 ? 17.530 29.713 30.386 1.00 98.71 ? 189 GLY B O 1 ATOM 8632 N N . TYR B 2 190 ? 18.567 28.606 28.723 1.00 95.09 ? 190 TYR B N 1 ATOM 8633 C CA . TYR B 2 190 ? 18.255 27.284 29.253 1.00 82.79 ? 190 TYR B CA 1 ATOM 8634 C C . TYR B 2 190 ? 19.369 26.299 28.947 1.00 87.90 ? 190 TYR B C 1 ATOM 8635 O O . TYR B 2 190 ? 19.796 26.158 27.799 1.00 82.35 ? 190 TYR B O 1 ATOM 8636 C CB . TYR B 2 190 ? 16.935 26.762 28.691 1.00 76.52 ? 190 TYR B CB 1 ATOM 8637 C CG . TYR B 2 190 ? 16.718 25.283 28.939 1.00 86.04 ? 190 TYR B CG 1 ATOM 8638 C CD1 . TYR B 2 190 ? 16.613 24.783 30.230 1.00 73.51 ? 190 TYR B CD1 1 ATOM 8639 C CD2 . TYR B 2 190 ? 16.613 24.388 27.881 1.00 98.59 ? 190 TYR B CD2 1 ATOM 8640 C CE1 . TYR B 2 190 ? 16.413 23.438 30.461 1.00 74.85 ? 190 TYR B CE1 1 ATOM 8641 C CE2 . TYR B 2 190 ? 16.412 23.038 28.102 1.00 79.96 ? 190 TYR B CE2 1 ATOM 8642 C CZ . TYR B 2 190 ? 16.314 22.569 29.394 1.00 81.32 ? 190 TYR B CZ 1 ATOM 8643 O OH . TYR B 2 190 ? 16.115 21.227 29.621 1.00 84.29 ? 190 TYR B OH 1 ATOM 8644 N N . LYS B 2 191 ? 19.812 25.590 29.976 1.00 90.91 ? 191 LYS B N 1 ATOM 8645 C CA . LYS B 2 191 ? 20.906 24.650 29.827 1.00 83.04 ? 191 LYS B CA 1 ATOM 8646 C C . LYS B 2 191 ? 20.471 23.273 30.291 1.00 92.71 ? 191 LYS B C 1 ATOM 8647 O O . LYS B 2 191 ? 20.150 23.075 31.462 1.00 104.07 ? 191 LYS B O 1 ATOM 8648 C CB . LYS B 2 191 ? 22.130 25.124 30.615 1.00 83.87 ? 191 LYS B CB 1 ATOM 8649 C CG . LYS B 2 191 ? 23.403 24.351 30.322 1.00 87.48 ? 191 LYS B CG 1 ATOM 8650 C CD . LYS B 2 191 ? 24.619 25.028 30.941 1.00 89.01 ? 191 LYS B CD 1 ATOM 8651 C CE . LYS B 2 191 ? 24.482 25.144 32.449 1.00 85.21 ? 191 LYS B CE 1 ATOM 8652 N NZ . LYS B 2 191 ? 25.696 25.740 33.085 1.00 89.78 ? 191 LYS B NZ 1 ATOM 8653 N N . HIS B 2 192 ? 20.440 22.329 29.358 1.00 82.27 ? 192 HIS B N 1 ATOM 8654 C CA . HIS B 2 192 ? 20.142 20.945 29.683 1.00 82.27 ? 192 HIS B CA 1 ATOM 8655 C C . HIS B 2 192 ? 21.438 20.166 29.832 1.00 91.25 ? 192 HIS B C 1 ATOM 8656 O O . HIS B 2 192 ? 22.188 20.020 28.870 1.00 99.72 ? 192 HIS B O 1 ATOM 8657 C CB . HIS B 2 192 ? 19.263 20.310 28.609 1.00 87.01 ? 192 HIS B CB 1 ATOM 8658 C CG . HIS B 2 192 ? 19.113 18.828 28.756 1.00 117.43 ? 192 HIS B CG 1 ATOM 8659 N ND1 . HIS B 2 192 ? 18.740 18.232 29.941 1.00 110.69 ? 192 HIS B ND1 1 ATOM 8660 C CD2 . HIS B 2 192 ? 19.291 17.820 27.868 1.00 111.65 ? 192 HIS B CD2 1 ATOM 8661 C CE1 . HIS B 2 192 ? 18.691 16.922 29.776 1.00 106.53 ? 192 HIS B CE1 1 ATOM 8662 N NE2 . HIS B 2 192 ? 19.022 16.646 28.528 1.00 102.11 ? 192 HIS B NE2 1 ATOM 8663 N N . VAL B 2 193 ? 21.703 19.669 31.035 1.00 102.18 ? 193 VAL B N 1 ATOM 8664 C CA . VAL B 2 193 ? 22.949 18.956 31.290 1.00 122.93 ? 193 VAL B CA 1 ATOM 8665 C C . VAL B 2 193 ? 22.761 17.438 31.241 1.00 101.60 ? 193 VAL B C 1 ATOM 8666 O O . VAL B 2 193 ? 23.355 16.771 30.394 1.00 112.55 ? 193 VAL B O 1 ATOM 8667 C CB . VAL B 2 193 ? 23.575 19.376 32.646 1.00 113.07 ? 193 VAL B CB 1 ATOM 8668 C CG1 . VAL B 2 193 ? 22.509 19.562 33.709 1.00 92.31 ? 193 VAL B CG1 1 ATOM 8669 C CG2 . VAL B 2 193 ? 24.647 18.381 33.087 1.00 117.67 ? 193 VAL B CG2 1 ATOM 8670 N N . LEU B 2 194 ? 21.945 16.890 32.137 1.00 104.59 ? 194 LEU B N 1 ATOM 8671 C CA . LEU B 2 194 ? 21.788 15.440 32.229 1.00 116.31 ? 194 LEU B CA 1 ATOM 8672 C C . LEU B 2 194 ? 20.418 14.961 31.768 1.00 94.74 ? 194 LEU B C 1 ATOM 8673 O O . LEU B 2 194 ? 19.396 15.319 32.351 1.00 90.76 ? 194 LEU B O 1 ATOM 8674 C CB . LEU B 2 194 ? 22.029 14.966 33.663 1.00 114.45 ? 194 LEU B CB 1 ATOM 8675 C CG . LEU B 2 194 ? 21.817 13.467 33.883 1.00 104.76 ? 194 LEU B CG 1 ATOM 8676 C CD1 . LEU B 2 194 ? 22.786 12.663 33.029 1.00 116.70 ? 194 LEU B CD1 1 ATOM 8677 C CD2 . LEU B 2 194 ? 21.958 13.103 35.352 1.00 102.76 ? 194 LEU B CD2 1 ATOM 8678 N N . THR B 2 195 ? 20.406 14.139 30.725 1.00 92.36 ? 195 THR B N 1 ATOM 8679 C CA . THR B 2 195 ? 19.169 13.533 30.253 1.00 103.57 ? 195 THR B CA 1 ATOM 8680 C C . THR B 2 195 ? 18.717 12.447 31.231 1.00 119.97 ? 195 THR B C 1 ATOM 8681 O O . THR B 2 195 ? 19.533 11.899 31.974 1.00 115.05 ? 195 THR B O 1 ATOM 8682 C CB . THR B 2 195 ? 19.335 12.940 28.844 1.00 91.40 ? 195 THR B CB 1 ATOM 8683 O OG1 . THR B 2 195 ? 18.121 12.288 28.454 1.00 97.05 ? 195 THR B OG1 1 ATOM 8684 C CG2 . THR B 2 195 ? 20.480 11.939 28.818 1.00 98.55 ? 195 THR B CG2 1 ATOM 8685 N N . LEU B 2 196 ? 17.420 12.147 31.228 1.00 104.08 ? 196 LEU B N 1 ATOM 8686 C CA . LEU B 2 196 ? 16.833 11.218 32.195 1.00 95.22 ? 196 LEU B CA 1 ATOM 8687 C C . LEU B 2 196 ? 17.507 9.847 32.185 1.00 99.97 ? 196 LEU B C 1 ATOM 8688 O O . LEU B 2 196 ? 17.612 9.202 31.143 1.00 110.09 ? 196 LEU B O 1 ATOM 8689 C CB . LEU B 2 196 ? 15.334 11.058 31.929 1.00 86.37 ? 196 LEU B CB 1 ATOM 8690 C CG . LEU B 2 196 ? 14.413 12.165 32.446 1.00 82.81 ? 196 LEU B CG 1 ATOM 8691 C CD1 . LEU B 2 196 ? 13.072 12.125 31.742 1.00 80.75 ? 196 LEU B CD1 1 ATOM 8692 C CD2 . LEU B 2 196 ? 14.218 12.029 33.942 1.00 83.80 ? 196 LEU B CD2 1 ATOM 8693 N N . THR B 2 197 ? 17.955 9.409 33.358 1.00 93.34 ? 197 THR B N 1 ATOM 8694 C CA . THR B 2 197 ? 18.644 8.130 33.489 1.00 101.00 ? 197 THR B CA 1 ATOM 8695 C C . THR B 2 197 ? 18.238 7.407 34.767 1.00 112.06 ? 197 THR B C 1 ATOM 8696 O O . THR B 2 197 ? 17.734 8.024 35.706 1.00 114.43 ? 197 THR B O 1 ATOM 8697 C CB . THR B 2 197 ? 20.174 8.306 33.483 1.00 108.02 ? 197 THR B CB 1 ATOM 8698 O OG1 . THR B 2 197 ? 20.806 7.035 33.684 1.00 113.55 ? 197 THR B OG1 1 ATOM 8699 C CG2 . THR B 2 197 ? 20.604 9.257 34.589 1.00 102.20 ? 197 THR B CG2 1 ATOM 8700 N N . ASP B 2 198 ? 18.461 6.096 34.793 1.00 101.82 ? 198 ASP B N 1 ATOM 8701 C CA . ASP B 2 198 ? 18.128 5.281 35.956 1.00 104.48 ? 198 ASP B CA 1 ATOM 8702 C C . ASP B 2 198 ? 19.305 5.189 36.921 1.00 109.01 ? 198 ASP B C 1 ATOM 8703 O O . ASP B 2 198 ? 19.241 4.481 37.927 1.00 113.79 ? 198 ASP B O 1 ATOM 8704 C CB . ASP B 2 198 ? 17.689 3.881 35.523 1.00 120.61 ? 198 ASP B CB 1 ATOM 8705 C CG . ASP B 2 198 ? 18.751 3.157 34.723 1.00 131.05 ? 198 ASP B CG 1 ATOM 8706 O OD1 . ASP B 2 198 ? 19.519 3.832 34.005 1.00 132.95 ? 198 ASP B OD1 1 ATOM 8707 O OD2 . ASP B 2 198 ? 18.818 1.913 34.811 1.00 134.04 ? 198 ASP B OD2 1 ATOM 8708 N N . GLN B 2 199 ? 20.380 5.906 36.608 1.00 107.26 ? 199 GLN B N 1 ATOM 8709 C CA . GLN B 2 199 ? 21.547 5.949 37.479 1.00 113.70 ? 199 GLN B CA 1 ATOM 8710 C C . GLN B 2 199 ? 21.559 7.241 38.286 1.00 118.63 ? 199 GLN B C 1 ATOM 8711 O O . GLN B 2 199 ? 21.784 8.322 37.744 1.00 110.29 ? 199 GLN B O 1 ATOM 8712 C CB . GLN B 2 199 ? 22.833 5.819 36.662 1.00 112.15 ? 199 GLN B CB 1 ATOM 8713 C CG . GLN B 2 199 ? 22.899 4.557 35.821 1.00 123.10 ? 199 GLN B CG 1 ATOM 8714 C CD . GLN B 2 199 ? 22.809 3.296 36.658 1.00 150.18 ? 199 GLN B CD 1 ATOM 8715 O OE1 . GLN B 2 199 ? 23.276 3.258 37.797 1.00 170.46 ? 199 GLN B OE1 1 ATOM 8716 N NE2 . GLN B 2 199 ? 22.201 2.256 36.099 1.00 153.40 ? 199 GLN B NE2 1 ATOM 8717 N N . VAL B 2 200 ? 21.324 7.120 39.587 1.00 121.91 ? 200 VAL B N 1 ATOM 8718 C CA . VAL B 2 200 ? 21.220 8.286 40.453 1.00 115.68 ? 200 VAL B CA 1 ATOM 8719 C C . VAL B 2 200 ? 22.592 8.830 40.834 1.00 122.88 ? 200 VAL B C 1 ATOM 8720 O O . VAL B 2 200 ? 22.716 9.978 41.258 1.00 127.03 ? 200 VAL B O 1 ATOM 8721 C CB . VAL B 2 200 ? 20.421 7.961 41.725 1.00 123.52 ? 200 VAL B CB 1 ATOM 8722 C CG1 . VAL B 2 200 ? 19.028 7.490 41.349 1.00 113.55 ? 200 VAL B CG1 1 ATOM 8723 C CG2 . VAL B 2 200 ? 21.138 6.904 42.552 1.00 132.12 ? 200 VAL B CG2 1 ATOM 8724 N N . THR B 2 201 ? 23.621 8.002 40.685 1.00 128.89 ? 201 THR B N 1 ATOM 8725 C CA . THR B 2 201 ? 24.989 8.458 40.890 1.00 133.14 ? 201 THR B CA 1 ATOM 8726 C C . THR B 2 201 ? 25.368 9.402 39.759 1.00 132.32 ? 201 THR B C 1 ATOM 8727 O O . THR B 2 201 ? 26.078 10.385 39.963 1.00 137.12 ? 201 THR B O 1 ATOM 8728 C CB . THR B 2 201 ? 25.984 7.289 40.944 1.00 130.47 ? 201 THR B CB 1 ATOM 8729 O OG1 . THR B 2 201 ? 25.873 6.512 39.745 1.00 138.26 ? 201 THR B OG1 1 ATOM 8730 C CG2 . THR B 2 201 ? 25.695 6.402 42.143 1.00 146.75 ? 201 THR B CG2 1 ATOM 8731 N N . ARG B 2 202 ? 24.864 9.095 38.567 1.00 119.76 ? 202 ARG B N 1 ATOM 8732 C CA . ARG B 2 202 ? 25.087 9.909 37.378 1.00 127.27 ? 202 ARG B CA 1 ATOM 8733 C C . ARG B 2 202 ? 24.533 11.325 37.570 1.00 128.70 ? 202 ARG B C 1 ATOM 8734 O O . ARG B 2 202 ? 24.969 12.275 36.917 1.00 113.35 ? 202 ARG B O 1 ATOM 8735 C CB . ARG B 2 202 ? 24.448 9.226 36.161 1.00 121.83 ? 202 ARG B CB 1 ATOM 8736 C CG . ARG B 2 202 ? 24.604 9.964 34.842 1.00 131.93 ? 202 ARG B CG 1 ATOM 8737 C CD . ARG B 2 202 ? 26.060 10.245 34.524 1.00 138.04 ? 202 ARG B CD 1 ATOM 8738 N NE . ARG B 2 202 ? 26.200 11.018 33.295 1.00 140.37 ? 202 ARG B NE 1 ATOM 8739 C CZ . ARG B 2 202 ? 27.224 11.823 33.030 1.00 136.21 ? 202 ARG B CZ 1 ATOM 8740 N NH1 . ARG B 2 202 ? 28.202 11.968 33.914 1.00 142.42 ? 202 ARG B NH1 1 ATOM 8741 N NH2 . ARG B 2 202 ? 27.268 12.489 31.885 1.00 131.32 ? 202 ARG B NH2 1 ATOM 8742 N N . PHE B 2 203 ? 23.586 11.457 38.492 1.00 120.91 ? 203 PHE B N 1 ATOM 8743 C CA . PHE B 2 203 ? 22.982 12.743 38.818 1.00 104.14 ? 203 PHE B CA 1 ATOM 8744 C C . PHE B 2 203 ? 23.947 13.594 39.626 1.00 114.18 ? 203 PHE B C 1 ATOM 8745 O O . PHE B 2 203 ? 24.346 14.677 39.197 1.00 103.15 ? 203 PHE B O 1 ATOM 8746 C CB . PHE B 2 203 ? 21.681 12.536 39.593 1.00 107.65 ? 203 PHE B CB 1 ATOM 8747 C CG . PHE B 2 203 ? 20.989 13.812 39.984 1.00 96.98 ? 203 PHE B CG 1 ATOM 8748 C CD1 . PHE B 2 203 ? 21.278 14.436 41.187 1.00 98.01 ? 203 PHE B CD1 1 ATOM 8749 C CD2 . PHE B 2 203 ? 20.032 14.375 39.155 1.00 104.22 ? 203 PHE B CD2 1 ATOM 8750 C CE1 . PHE B 2 203 ? 20.637 15.606 41.549 1.00 101.53 ? 203 PHE B CE1 1 ATOM 8751 C CE2 . PHE B 2 203 ? 19.386 15.546 39.513 1.00 91.10 ? 203 PHE B CE2 1 ATOM 8752 C CZ . PHE B 2 203 ? 19.689 16.161 40.711 1.00 92.17 ? 203 PHE B CZ 1 ATOM 8753 N N . ASN B 2 204 ? 24.298 13.100 40.810 1.00 123.25 ? 204 ASN B N 1 ATOM 8754 C CA . ASN B 2 204 ? 25.202 13.797 41.716 1.00 115.03 ? 204 ASN B CA 1 ATOM 8755 C C . ASN B 2 204 ? 26.517 14.186 41.049 1.00 113.50 ? 204 ASN B C 1 ATOM 8756 O O . ASN B 2 204 ? 27.129 15.188 41.412 1.00 113.20 ? 204 ASN B O 1 ATOM 8757 C CB . ASN B 2 204 ? 25.484 12.930 42.944 1.00 128.51 ? 204 ASN B CB 1 ATOM 8758 C CG . ASN B 2 204 ? 24.217 12.416 43.597 1.00 133.37 ? 204 ASN B CG 1 ATOM 8759 O OD1 . ASN B 2 204 ? 23.145 12.430 42.994 1.00 132.60 ? 204 ASN B OD1 1 ATOM 8760 N ND2 . ASN B 2 204 ? 24.335 11.955 44.837 1.00 131.35 ? 204 ASN B ND2 1 ATOM 8761 N N . GLU B 2 205 ? 26.941 13.393 40.069 1.00 126.07 ? 205 GLU B N 1 ATOM 8762 C CA . GLU B 2 205 ? 28.175 13.668 39.340 1.00 134.88 ? 205 GLU B CA 1 ATOM 8763 C C . GLU B 2 205 ? 28.067 14.943 38.511 1.00 131.02 ? 205 GLU B C 1 ATOM 8764 O O . GLU B 2 205 ? 28.978 15.769 38.514 1.00 123.02 ? 205 GLU B O 1 ATOM 8765 C CB . GLU B 2 205 ? 28.541 12.489 38.436 1.00 124.20 ? 205 GLU B CB 1 ATOM 8766 C CG . GLU B 2 205 ? 29.046 11.264 39.183 1.00 140.79 ? 205 GLU B CG 1 ATOM 8767 C CD . GLU B 2 205 ? 29.337 10.095 38.260 1.00 154.20 ? 205 GLU B CD 1 ATOM 8768 O OE1 . GLU B 2 205 ? 29.729 9.020 38.763 1.00 143.71 ? 205 GLU B OE1 1 ATOM 8769 O OE2 . GLU B 2 205 ? 29.171 10.249 37.031 1.00 160.57 ? 205 GLU B OE2 1 ATOM 8770 N N . GLU B 2 206 ? 26.951 15.099 37.804 1.00 136.12 ? 206 GLU B N 1 ATOM 8771 C CA . GLU B 2 206 ? 26.745 16.263 36.946 1.00 130.19 ? 206 GLU B CA 1 ATOM 8772 C C . GLU B 2 206 ? 26.468 17.517 37.767 1.00 126.11 ? 206 GLU B C 1 ATOM 8773 O O . GLU B 2 206 ? 26.840 18.624 37.375 1.00 114.45 ? 206 GLU B O 1 ATOM 8774 C CB . GLU B 2 206 ? 25.607 16.006 35.959 1.00 121.69 ? 206 GLU B CB 1 ATOM 8775 C CG . GLU B 2 206 ? 25.953 14.965 34.912 1.00 136.50 ? 206 GLU B CG 1 ATOM 8776 C CD . GLU B 2 206 ? 27.272 15.262 34.224 1.00 146.67 ? 206 GLU B CD 1 ATOM 8777 O OE1 . GLU B 2 206 ? 27.390 16.338 33.601 1.00 138.80 ? 206 GLU B OE1 1 ATOM 8778 O OE2 . GLU B 2 206 ? 28.196 14.425 34.316 1.00 144.75 ? 206 GLU B OE2 1 ATOM 8779 N N . VAL B 2 207 ? 25.808 17.340 38.905 1.00 124.35 ? 207 VAL B N 1 ATOM 8780 C CA . VAL B 2 207 ? 25.697 18.410 39.883 1.00 111.43 ? 207 VAL B CA 1 ATOM 8781 C C . VAL B 2 207 ? 27.091 18.632 40.465 1.00 121.86 ? 207 VAL B C 1 ATOM 8782 O O . VAL B 2 207 ? 27.898 17.702 40.504 1.00 138.65 ? 207 VAL B O 1 ATOM 8783 C CB . VAL B 2 207 ? 24.677 18.067 40.990 1.00 110.17 ? 207 VAL B CB 1 ATOM 8784 C CG1 . VAL B 2 207 ? 24.604 19.172 42.027 1.00 127.82 ? 207 VAL B CG1 1 ATOM 8785 C CG2 . VAL B 2 207 ? 23.307 17.828 40.382 1.00 95.07 ? 207 VAL B CG2 1 ATOM 8786 N N . LYS B 2 208 ? 27.374 19.872 40.863 1.00 115.29 ? 208 LYS B N 1 ATOM 8787 C CA . LYS B 2 208 ? 28.665 20.302 41.415 1.00 136.49 ? 208 LYS B CA 1 ATOM 8788 C C . LYS B 2 208 ? 29.722 20.429 40.319 1.00 144.39 ? 208 LYS B C 1 ATOM 8789 O O . LYS B 2 208 ? 30.767 21.046 40.527 1.00 164.94 ? 208 LYS B O 1 ATOM 8790 C CB . LYS B 2 208 ? 29.154 19.357 42.519 1.00 136.06 ? 208 LYS B CB 1 ATOM 8791 C CG . LYS B 2 208 ? 28.165 19.161 43.654 1.00 136.55 ? 208 LYS B CG 1 ATOM 8792 C CD . LYS B 2 208 ? 28.764 18.314 44.759 1.00 150.43 ? 208 LYS B CD 1 ATOM 8793 C CE . LYS B 2 208 ? 29.873 19.056 45.484 1.00 153.40 ? 208 LYS B CE 1 ATOM 8794 N NZ . LYS B 2 208 ? 30.423 18.258 46.615 1.00 160.25 ? 208 LYS B NZ 1 ATOM 8795 N N . LYS B 2 209 ? 29.448 19.853 39.153 1.00 116.59 ? 209 LYS B N 1 ATOM 8796 C CA . LYS B 2 209 ? 30.156 20.241 37.943 1.00 112.69 ? 209 LYS B CA 1 ATOM 8797 C C . LYS B 2 209 ? 29.523 21.546 37.500 1.00 118.08 ? 209 LYS B C 1 ATOM 8798 O O . LYS B 2 209 ? 30.189 22.443 36.982 1.00 128.19 ? 209 LYS B O 1 ATOM 8799 C CB . LYS B 2 209 ? 30.051 19.181 36.845 1.00 111.31 ? 209 LYS B CB 1 ATOM 8800 C CG . LYS B 2 209 ? 30.992 17.996 37.000 1.00 120.75 ? 209 LYS B CG 1 ATOM 8801 C CD . LYS B 2 209 ? 31.041 17.175 35.715 1.00 123.96 ? 209 LYS B CD 1 ATOM 8802 C CE . LYS B 2 209 ? 31.959 15.965 35.842 1.00 140.64 ? 209 LYS B CE 1 ATOM 8803 N NZ . LYS B 2 209 ? 31.403 14.912 36.740 1.00 133.85 ? 209 LYS B NZ 1 ATOM 8804 N N . GLN B 2 210 ? 28.216 21.634 37.728 1.00 121.54 ? 210 GLN B N 1 ATOM 8805 C CA . GLN B 2 210 ? 27.446 22.836 37.454 1.00 122.87 ? 210 GLN B CA 1 ATOM 8806 C C . GLN B 2 210 ? 27.800 23.943 38.435 1.00 113.67 ? 210 GLN B C 1 ATOM 8807 O O . GLN B 2 210 ? 28.187 23.676 39.573 1.00 116.21 ? 210 GLN B O 1 ATOM 8808 C CB . GLN B 2 210 ? 25.947 22.535 37.524 1.00 114.74 ? 210 GLN B CB 1 ATOM 8809 C CG . GLN B 2 210 ? 25.445 21.637 36.410 1.00 102.50 ? 210 GLN B CG 1 ATOM 8810 C CD . GLN B 2 210 ? 25.544 22.300 35.053 1.00 111.76 ? 210 GLN B CD 1 ATOM 8811 O OE1 . GLN B 2 210 ? 25.452 23.522 34.942 1.00 125.91 ? 210 GLN B OE1 1 ATOM 8812 N NE2 . GLN B 2 210 ? 25.744 21.499 34.014 1.00 109.65 ? 210 GLN B NE2 1 ATOM 8813 N N . SER B 2 211 ? 27.666 25.186 37.987 1.00 111.16 ? 211 SER B N 1 ATOM 8814 C CA . SER B 2 211 ? 27.907 26.332 38.851 1.00 115.58 ? 211 SER B CA 1 ATOM 8815 C C . SER B 2 211 ? 26.918 27.456 38.557 1.00 109.07 ? 211 SER B C 1 ATOM 8816 O O . SER B 2 211 ? 26.087 27.348 37.656 1.00 108.73 ? 211 SER B O 1 ATOM 8817 C CB . SER B 2 211 ? 29.349 26.824 38.702 1.00 108.54 ? 211 SER B CB 1 ATOM 8818 O OG . SER B 2 211 ? 29.837 26.588 37.394 1.00 112.07 ? 211 SER B OG 1 ATOM 8819 N N . VAL B 2 212 ? 27.029 28.540 39.314 1.00 92.87 ? 212 VAL B N 1 ATOM 8820 C CA . VAL B 2 212 ? 26.008 29.580 39.344 1.00 89.45 ? 212 VAL B CA 1 ATOM 8821 C C . VAL B 2 212 ? 26.388 30.805 38.510 1.00 95.21 ? 212 VAL B C 1 ATOM 8822 O O . VAL B 2 212 ? 27.555 31.187 38.457 1.00 126.49 ? 212 VAL B O 1 ATOM 8823 C CB . VAL B 2 212 ? 25.733 29.997 40.814 1.00 101.30 ? 212 VAL B CB 1 ATOM 8824 C CG1 . VAL B 2 212 ? 25.532 31.495 40.951 1.00 91.77 ? 212 VAL B CG1 1 ATOM 8825 C CG2 . VAL B 2 212 ? 24.550 29.222 41.375 1.00 107.08 ? 212 VAL B CG2 1 ATOM 8826 N N . SER B 2 213 ? 25.400 31.412 37.853 1.00 84.97 ? 213 SER B N 1 ATOM 8827 C CA . SER B 2 213 ? 25.625 32.634 37.084 1.00 90.18 ? 213 SER B CA 1 ATOM 8828 C C . SER B 2 213 ? 24.925 33.838 37.711 1.00 92.34 ? 213 SER B C 1 ATOM 8829 O O . SER B 2 213 ? 24.290 33.724 38.759 1.00 92.99 ? 213 SER B O 1 ATOM 8830 C CB . SER B 2 213 ? 25.146 32.461 35.643 1.00 91.83 ? 213 SER B CB 1 ATOM 8831 O OG . SER B 2 213 ? 25.395 33.638 34.893 1.00 84.75 ? 213 SER B OG 1 ATOM 8832 N N . ARG B 2 214 ? 25.042 34.993 37.061 1.00 87.73 ? 214 ARG B N 1 ATOM 8833 C CA . ARG B 2 214 ? 24.433 36.218 37.569 1.00 94.17 ? 214 ARG B CA 1 ATOM 8834 C C . ARG B 2 214 ? 23.576 36.908 36.512 1.00 99.32 ? 214 ARG B C 1 ATOM 8835 O O . ARG B 2 214 ? 23.865 36.846 35.318 1.00 100.06 ? 214 ARG B O 1 ATOM 8836 C CB . ARG B 2 214 ? 25.508 37.183 38.074 1.00 94.80 ? 214 ARG B CB 1 ATOM 8837 C CG . ARG B 2 214 ? 24.963 38.351 38.888 1.00 88.13 ? 214 ARG B CG 1 ATOM 8838 C CD . ARG B 2 214 ? 26.018 39.427 39.092 1.00 100.21 ? 214 ARG B CD 1 ATOM 8839 N NE . ARG B 2 214 ? 25.537 40.518 39.936 1.00 88.27 ? 214 ARG B NE 1 ATOM 8840 C CZ . ARG B 2 214 ? 26.247 41.603 40.225 1.00 90.88 ? 214 ARG B CZ 1 ATOM 8841 N NH1 . ARG B 2 214 ? 27.470 41.745 39.733 1.00 96.33 ? 214 ARG B NH1 1 ATOM 8842 N NH2 . ARG B 2 214 ? 25.735 42.546 41.003 1.00 101.53 ? 214 ARG B NH2 1 ATOM 8843 N N . ASN B 2 215 ? 22.526 37.575 36.974 1.00 97.68 ? 215 ASN B N 1 ATOM 8844 C CA . ASN B 2 215 ? 21.584 38.270 36.110 1.00 88.37 ? 215 ASN B CA 1 ATOM 8845 C C . ASN B 2 215 ? 21.364 39.676 36.657 1.00 87.23 ? 215 ASN B C 1 ATOM 8846 O O . ASN B 2 215 ? 21.819 39.987 37.757 1.00 113.16 ? 215 ASN B O 1 ATOM 8847 C CB . ASN B 2 215 ? 20.267 37.491 36.023 1.00 81.15 ? 215 ASN B CB 1 ATOM 8848 C CG . ASN B 2 215 ? 19.388 37.951 34.877 1.00 80.24 ? 215 ASN B CG 1 ATOM 8849 O OD1 . ASN B 2 215 ? 18.230 38.321 35.077 1.00 73.18 ? 215 ASN B OD1 1 ATOM 8850 N ND2 . ASN B 2 215 ? 19.938 37.937 33.670 1.00 106.91 ? 215 ASN B ND2 1 ATOM 8851 N N . ARG B 2 216 ? 20.701 40.537 35.894 1.00 73.19 ? 216 ARG B N 1 ATOM 8852 C CA . ARG B 2 216 ? 20.462 41.898 36.365 1.00 72.97 ? 216 ARG B CA 1 ATOM 8853 C C . ARG B 2 216 ? 19.052 42.103 36.912 1.00 79.69 ? 216 ARG B C 1 ATOM 8854 O O . ARG B 2 216 ? 18.889 42.467 38.074 1.00 80.32 ? 216 ARG B O 1 ATOM 8855 C CB . ARG B 2 216 ? 20.732 42.916 35.264 1.00 76.85 ? 216 ARG B CB 1 ATOM 8856 C CG . ARG B 2 216 ? 20.479 44.335 35.734 1.00 112.33 ? 216 ARG B CG 1 ATOM 8857 C CD . ARG B 2 216 ? 21.031 45.363 34.777 1.00 114.16 ? 216 ARG B CD 1 ATOM 8858 N NE . ARG B 2 216 ? 22.388 45.778 35.120 1.00 100.28 ? 216 ARG B NE 1 ATOM 8859 C CZ . ARG B 2 216 ? 23.438 45.625 34.319 1.00 92.89 ? 216 ARG B CZ 1 ATOM 8860 N NH1 . ARG B 2 216 ? 23.286 45.063 33.128 1.00 106.59 ? 216 ARG B NH1 1 ATOM 8861 N NH2 . ARG B 2 216 ? 24.637 46.038 34.706 1.00 77.82 ? 216 ARG B NH2 1 ATOM 8862 N N . ASP B 2 217 ? 18.039 41.913 36.069 1.00 87.75 ? 217 ASP B N 1 ATOM 8863 C CA . ASP B 2 217 ? 16.653 42.119 36.491 1.00 76.28 ? 217 ASP B CA 1 ATOM 8864 C C . ASP B 2 217 ? 16.085 40.903 37.222 1.00 73.99 ? 217 ASP B C 1 ATOM 8865 O O . ASP B 2 217 ? 16.279 39.760 36.798 1.00 75.20 ? 217 ASP B O 1 ATOM 8866 C CB . ASP B 2 217 ? 15.768 42.464 35.293 1.00 71.25 ? 217 ASP B CB 1 ATOM 8867 C CG . ASP B 2 217 ? 15.484 41.271 34.412 1.00 75.08 ? 217 ASP B CG 1 ATOM 8868 O OD1 . ASP B 2 217 ? 16.316 40.342 34.371 1.00 95.90 ? 217 ASP B OD1 1 ATOM 8869 O OD2 . ASP B 2 217 ? 14.422 41.266 33.757 1.00 87.92 ? 217 ASP B OD2 1 ATOM 8870 N N . ALA B 2 218 ? 15.364 41.179 38.308 1.00 87.78 ? 218 ALA B N 1 ATOM 8871 C CA . ALA B 2 218 ? 14.871 40.156 39.236 1.00 79.44 ? 218 ALA B CA 1 ATOM 8872 C C . ALA B 2 218 ? 14.078 39.007 38.599 1.00 74.01 ? 218 ALA B C 1 ATOM 8873 O O . ALA B 2 218 ? 14.332 37.847 38.923 1.00 86.40 ? 218 ALA B O 1 ATOM 8874 C CB . ALA B 2 218 ? 14.028 40.817 40.332 1.00 70.92 ? 218 ALA B CB 1 ATOM 8875 N N . PRO B 2 219 ? 13.104 39.309 37.715 1.00 74.09 ? 219 PRO B N 1 ATOM 8876 C CA . PRO B 2 219 ? 12.405 38.168 37.121 1.00 75.45 ? 219 PRO B CA 1 ATOM 8877 C C . PRO B 2 219 ? 13.328 37.357 36.228 1.00 89.12 ? 219 PRO B C 1 ATOM 8878 O O . PRO B 2 219 ? 14.012 37.921 35.371 1.00 67.81 ? 219 PRO B O 1 ATOM 8879 C CB . PRO B 2 219 ? 11.287 38.823 36.298 1.00 72.37 ? 219 PRO B CB 1 ATOM 8880 C CG . PRO B 2 219 ? 11.144 40.188 36.857 1.00 92.55 ? 219 PRO B CG 1 ATOM 8881 C CD . PRO B 2 219 ? 12.530 40.582 37.255 1.00 104.96 ? 219 PRO B CD 1 ATOM 8882 N N . GLU B 2 220 ? 13.338 36.045 36.430 1.00 76.13 ? 220 GLU B N 1 ATOM 8883 C CA . GLU B 2 220 ? 14.179 35.158 35.645 1.00 81.66 ? 220 GLU B CA 1 ATOM 8884 C C . GLU B 2 220 ? 13.297 34.198 34.874 1.00 81.24 ? 220 GLU B C 1 ATOM 8885 O O . GLU B 2 220 ? 12.664 33.327 35.472 1.00 130.63 ? 220 GLU B O 1 ATOM 8886 C CB . GLU B 2 220 ? 15.143 34.390 36.552 1.00 80.14 ? 220 GLU B CB 1 ATOM 8887 C CG . GLU B 2 220 ? 15.777 35.226 37.657 1.00 78.25 ? 220 GLU B CG 1 ATOM 8888 C CD . GLU B 2 220 ? 16.957 36.054 37.182 1.00 88.08 ? 220 GLU B CD 1 ATOM 8889 O OE1 . GLU B 2 220 ? 17.945 36.154 37.939 1.00 109.92 ? 220 GLU B OE1 1 ATOM 8890 O OE2 . GLU B 2 220 ? 16.902 36.611 36.064 1.00 96.74 ? 220 GLU B OE2 1 ATOM 8891 N N . GLY B 2 221 ? 13.240 34.350 33.555 1.00 69.52 ? 221 GLY B N 1 ATOM 8892 C CA . GLY B 2 221 ? 12.334 33.521 32.789 1.00 92.26 ? 221 GLY B CA 1 ATOM 8893 C C . GLY B 2 221 ? 12.768 32.074 32.815 1.00 97.98 ? 221 GLY B C 1 ATOM 8894 O O . GLY B 2 221 ? 13.832 31.720 32.305 1.00 84.11 ? 221 GLY B O 1 ATOM 8895 N N . GLY B 2 222 ? 11.917 31.235 33.393 1.00 87.84 ? 222 GLY B N 1 ATOM 8896 C CA . GLY B 2 222 ? 12.115 29.802 33.394 1.00 68.84 ? 222 GLY B CA 1 ATOM 8897 C C . GLY B 2 222 ? 11.114 29.169 32.458 1.00 75.45 ? 222 GLY B C 1 ATOM 8898 O O . GLY B 2 222 ? 11.163 27.974 32.177 1.00 84.65 ? 222 GLY B O 1 ATOM 8899 N N . PHE B 2 223 ? 10.185 29.989 31.984 1.00 73.12 ? 223 PHE B N 1 ATOM 8900 C CA . PHE B 2 223 ? 9.131 29.509 31.109 1.00 64.88 ? 223 PHE B CA 1 ATOM 8901 C C . PHE B 2 223 ? 9.735 29.089 29.782 1.00 69.54 ? 223 PHE B C 1 ATOM 8902 O O . PHE B 2 223 ? 9.211 28.207 29.110 1.00 79.68 ? 223 PHE B O 1 ATOM 8903 C CB . PHE B 2 223 ? 8.057 30.578 30.913 1.00 67.41 ? 223 PHE B CB 1 ATOM 8904 C CG . PHE B 2 223 ? 7.234 30.839 32.143 1.00 59.76 ? 223 PHE B CG 1 ATOM 8905 C CD1 . PHE B 2 223 ? 7.417 30.084 33.290 1.00 60.71 ? 223 PHE B CD1 1 ATOM 8906 C CD2 . PHE B 2 223 ? 6.269 31.831 32.149 1.00 87.74 ? 223 PHE B CD2 1 ATOM 8907 C CE1 . PHE B 2 223 ? 6.662 30.318 34.420 1.00 61.16 ? 223 PHE B CE1 1 ATOM 8908 C CE2 . PHE B 2 223 ? 5.506 32.069 33.278 1.00 72.81 ? 223 PHE B CE2 1 ATOM 8909 C CZ . PHE B 2 223 ? 5.703 31.311 34.414 1.00 61.52 ? 223 PHE B CZ 1 ATOM 8910 N N . ASP B 2 224 ? 10.843 29.724 29.415 1.00 69.50 ? 224 ASP B N 1 ATOM 8911 C CA . ASP B 2 224 ? 11.642 29.257 28.292 1.00 73.88 ? 224 ASP B CA 1 ATOM 8912 C C . ASP B 2 224 ? 12.109 27.833 28.565 1.00 73.89 ? 224 ASP B C 1 ATOM 8913 O O . ASP B 2 224 ? 12.043 26.967 27.692 1.00 73.13 ? 224 ASP B O 1 ATOM 8914 C CB . ASP B 2 224 ? 12.842 30.176 28.053 1.00 76.45 ? 224 ASP B CB 1 ATOM 8915 C CG . ASP B 2 224 ? 12.489 31.395 27.227 1.00 83.56 ? 224 ASP B CG 1 ATOM 8916 O OD1 . ASP B 2 224 ? 11.284 31.673 27.058 1.00 74.40 ? 224 ASP B OD1 1 ATOM 8917 O OD2 . ASP B 2 224 ? 13.420 32.079 26.749 1.00 97.65 ? 224 ASP B OD2 1 ATOM 8918 N N . ALA B 2 225 ? 12.568 27.597 29.791 1.00 71.07 ? 225 ALA B N 1 ATOM 8919 C CA . ALA B 2 225 ? 13.075 26.288 30.185 1.00 76.80 ? 225 ALA B CA 1 ATOM 8920 C C . ALA B 2 225 ? 11.954 25.259 30.267 1.00 88.68 ? 225 ALA B C 1 ATOM 8921 O O . ALA B 2 225 ? 12.066 24.166 29.712 1.00 95.04 ? 225 ALA B O 1 ATOM 8922 C CB . ALA B 2 225 ? 13.804 26.383 31.515 1.00 85.50 ? 225 ALA B CB 1 ATOM 8923 N N . ILE B 2 226 ? 10.877 25.616 30.963 1.00 75.13 ? 226 ILE B N 1 ATOM 8924 C CA . ILE B 2 226 ? 9.727 24.731 31.120 1.00 69.25 ? 226 ILE B CA 1 ATOM 8925 C C . ILE B 2 226 ? 9.168 24.310 29.766 1.00 69.86 ? 226 ILE B C 1 ATOM 8926 O O . ILE B 2 226 ? 8.851 23.141 29.548 1.00 91.75 ? 226 ILE B O 1 ATOM 8927 C CB . ILE B 2 226 ? 8.609 25.399 31.939 1.00 62.86 ? 226 ILE B CB 1 ATOM 8928 C CG1 . ILE B 2 226 ? 9.093 25.698 33.355 1.00 72.96 ? 226 ILE B CG1 1 ATOM 8929 C CG2 . ILE B 2 226 ? 7.391 24.507 31.998 1.00 69.03 ? 226 ILE B CG2 1 ATOM 8930 C CD1 . ILE B 2 226 ? 8.041 26.328 34.239 1.00 72.06 ? 226 ILE B CD1 1 ATOM 8931 N N . MET B 2 227 ? 9.061 25.270 28.856 1.00 63.59 ? 227 MET B N 1 ATOM 8932 C CA . MET B 2 227 ? 8.564 24.999 27.517 1.00 63.71 ? 227 MET B CA 1 ATOM 8933 C C . MET B 2 227 ? 9.471 24.028 26.780 1.00 68.14 ? 227 MET B C 1 ATOM 8934 O O . MET B 2 227 ? 9.003 23.078 26.152 1.00 93.72 ? 227 MET B O 1 ATOM 8935 C CB . MET B 2 227 ? 8.439 26.293 26.717 1.00 77.48 ? 227 MET B CB 1 ATOM 8936 C CG . MET B 2 227 ? 8.125 26.077 25.253 1.00 76.68 ? 227 MET B CG 1 ATOM 8937 S SD . MET B 2 227 ? 6.609 25.135 25.058 1.00 75.53 ? 227 MET B SD 1 ATOM 8938 C CE . MET B 2 227 ? 5.446 26.218 25.886 1.00 60.96 ? 227 MET B CE 1 ATOM 8939 N N . GLN B 2 228 ? 10.773 24.268 26.862 1.00 72.26 ? 228 GLN B N 1 ATOM 8940 C CA . GLN B 2 228 ? 11.731 23.457 26.125 1.00 84.39 ? 228 GLN B CA 1 ATOM 8941 C C . GLN B 2 228 ? 11.834 22.050 26.695 1.00 84.43 ? 228 GLN B C 1 ATOM 8942 O O . GLN B 2 228 ? 11.836 21.078 25.946 1.00 75.35 ? 228 GLN B O 1 ATOM 8943 C CB . GLN B 2 228 ? 13.103 24.129 26.114 1.00 72.46 ? 228 GLN B CB 1 ATOM 8944 C CG . GLN B 2 228 ? 13.178 25.302 25.157 1.00 75.60 ? 228 GLN B CG 1 ATOM 8945 C CD . GLN B 2 228 ? 12.627 24.961 23.784 1.00 76.00 ? 228 GLN B CD 1 ATOM 8946 O OE1 . GLN B 2 228 ? 13.205 24.157 23.051 1.00 73.06 ? 228 GLN B OE1 1 ATOM 8947 N NE2 . GLN B 2 228 ? 11.498 25.568 23.433 1.00 77.11 ? 228 GLN B NE2 1 ATOM 8948 N N . ALA B 2 229 ? 11.903 21.940 28.017 1.00 90.54 ? 229 ALA B N 1 ATOM 8949 C CA . ALA B 2 229 ? 12.032 20.638 28.667 1.00 85.95 ? 229 ALA B CA 1 ATOM 8950 C C . ALA B 2 229 ? 10.834 19.743 28.369 1.00 79.94 ? 229 ALA B C 1 ATOM 8951 O O . ALA B 2 229 ? 10.935 18.519 28.414 1.00 106.40 ? 229 ALA B O 1 ATOM 8952 C CB . ALA B 2 229 ? 12.201 20.809 30.168 1.00 79.49 ? 229 ALA B CB 1 ATOM 8953 N N . THR B 2 230 ? 9.700 20.365 28.068 1.00 73.78 ? 230 THR B N 1 ATOM 8954 C CA . THR B 2 230 ? 8.478 19.634 27.763 1.00 74.00 ? 230 THR B CA 1 ATOM 8955 C C . THR B 2 230 ? 8.453 19.065 26.344 1.00 82.17 ? 230 THR B C 1 ATOM 8956 O O . THR B 2 230 ? 8.160 17.886 26.145 1.00 117.40 ? 230 THR B O 1 ATOM 8957 C CB . THR B 2 230 ? 7.248 20.539 27.953 1.00 73.18 ? 230 THR B CB 1 ATOM 8958 O OG1 . THR B 2 230 ? 7.176 20.961 29.320 1.00 73.05 ? 230 THR B OG1 1 ATOM 8959 C CG2 . THR B 2 230 ? 5.973 19.801 27.588 1.00 82.77 ? 230 THR B CG2 1 ATOM 8960 N N . VAL B 2 231 ? 8.773 19.904 25.365 1.00 69.13 ? 231 VAL B N 1 ATOM 8961 C CA . VAL B 2 231 ? 8.598 19.550 23.957 1.00 72.62 ? 231 VAL B CA 1 ATOM 8962 C C . VAL B 2 231 ? 9.838 18.935 23.305 1.00 73.81 ? 231 VAL B C 1 ATOM 8963 O O . VAL B 2 231 ? 9.780 18.447 22.175 1.00 90.11 ? 231 VAL B O 1 ATOM 8964 C CB . VAL B 2 231 ? 8.182 20.784 23.146 1.00 75.74 ? 231 VAL B CB 1 ATOM 8965 C CG1 . VAL B 2 231 ? 6.965 21.435 23.783 1.00 85.51 ? 231 VAL B CG1 1 ATOM 8966 C CG2 . VAL B 2 231 ? 9.334 21.775 23.064 1.00 71.56 ? 231 VAL B CG2 1 ATOM 8967 N N . CYS B 2 232 ? 10.951 18.957 24.026 1.00 73.27 ? 232 CYS B N 1 ATOM 8968 C CA . CYS B 2 232 ? 12.231 18.468 23.524 1.00 87.74 ? 232 CYS B CA 1 ATOM 8969 C C . CYS B 2 232 ? 12.426 16.998 23.830 1.00 95.47 ? 232 CYS B C 1 ATOM 8970 O O . CYS B 2 232 ? 13.528 16.477 23.691 1.00 97.98 ? 232 CYS B O 1 ATOM 8971 C CB . CYS B 2 232 ? 13.392 19.275 24.092 1.00 99.69 ? 232 CYS B CB 1 ATOM 8972 S SG . CYS B 2 232 ? 13.589 20.867 23.285 1.00 79.60 ? 232 CYS B SG 1 ATOM 8973 N N . ASP B 2 233 ? 11.341 16.344 24.236 1.00 115.34 ? 233 ASP B N 1 ATOM 8974 C CA . ASP B 2 233 ? 11.357 15.055 24.924 1.00 112.31 ? 233 ASP B CA 1 ATOM 8975 C C . ASP B 2 233 ? 12.373 14.046 24.395 1.00 95.55 ? 233 ASP B C 1 ATOM 8976 O O . ASP B 2 233 ? 12.961 13.300 25.175 1.00 96.01 ? 233 ASP B O 1 ATOM 8977 C CB . ASP B 2 233 ? 9.963 14.439 24.842 1.00 112.61 ? 233 ASP B CB 1 ATOM 8978 C CG . ASP B 2 233 ? 9.384 14.518 23.443 1.00 114.23 ? 233 ASP B CG 1 ATOM 8979 O OD1 . ASP B 2 233 ? 10.083 15.020 22.536 1.00 97.31 ? 233 ASP B OD1 1 ATOM 8980 O OD2 . ASP B 2 233 ? 8.237 14.069 23.244 1.00 141.16 ? 233 ASP B OD2 1 ATOM 8981 N N . GLU B 2 234 ? 12.568 14.010 23.081 1.00 84.57 ? 234 GLU B N 1 ATOM 8982 C CA . GLU B 2 234 ? 13.653 13.222 22.505 1.00 88.15 ? 234 GLU B CA 1 ATOM 8983 C C . GLU B 2 234 ? 14.990 13.548 23.174 1.00 90.31 ? 234 GLU B C 1 ATOM 8984 O O . GLU B 2 234 ? 15.772 12.650 23.482 1.00 88.64 ? 234 GLU B O 1 ATOM 8985 C CB . GLU B 2 234 ? 13.749 13.460 20.995 1.00 111.22 ? 234 GLU B CB 1 ATOM 8986 C CG . GLU B 2 234 ? 15.014 12.907 20.339 1.00 125.85 ? 234 GLU B CG 1 ATOM 8987 C CD . GLU B 2 234 ? 14.999 11.394 20.184 1.00 142.83 ? 234 GLU B CD 1 ATOM 8988 O OE1 . GLU B 2 234 ? 13.983 10.760 20.540 1.00 144.93 ? 234 GLU B OE1 1 ATOM 8989 O OE2 . GLU B 2 234 ? 16.008 10.837 19.700 1.00 146.77 ? 234 GLU B OE2 1 ATOM 8990 N N . LYS B 2 235 ? 15.234 14.835 23.413 1.00 110.70 ? 235 LYS B N 1 ATOM 8991 C CA . LYS B 2 235 ? 16.497 15.293 23.990 1.00 110.33 ? 235 LYS B CA 1 ATOM 8992 C C . LYS B 2 235 ? 16.607 14.975 25.480 1.00 93.07 ? 235 LYS B C 1 ATOM 8993 O O . LYS B 2 235 ? 17.625 14.455 25.934 1.00 103.71 ? 235 LYS B O 1 ATOM 8994 C CB . LYS B 2 235 ? 16.668 16.803 23.773 1.00 110.61 ? 235 LYS B CB 1 ATOM 8995 C CG . LYS B 2 235 ? 18.112 17.291 23.823 1.00 93.74 ? 235 LYS B CG 1 ATOM 8996 C CD . LYS B 2 235 ? 18.886 16.824 22.599 1.00 106.07 ? 235 LYS B CD 1 ATOM 8997 C CE . LYS B 2 235 ? 20.352 17.210 22.680 1.00 100.75 ? 235 LYS B CE 1 ATOM 8998 N NZ . LYS B 2 235 ? 21.117 16.764 21.480 1.00 101.22 ? 235 LYS B NZ 1 ATOM 8999 N N . ILE B 2 236 ? 15.565 15.292 26.241 1.00 81.16 ? 236 ILE B N 1 ATOM 9000 C CA . ILE B 2 236 ? 15.627 15.129 27.690 1.00 88.08 ? 236 ILE B CA 1 ATOM 9001 C C . ILE B 2 236 ? 15.194 13.722 28.122 1.00 110.22 ? 236 ILE B C 1 ATOM 9002 O O . ILE B 2 236 ? 15.404 13.322 29.270 1.00 112.11 ? 236 ILE B O 1 ATOM 9003 C CB . ILE B 2 236 ? 14.769 16.198 28.410 1.00 88.01 ? 236 ILE B CB 1 ATOM 9004 C CG1 . ILE B 2 236 ? 13.353 15.694 28.670 1.00 81.18 ? 236 ILE B CG1 1 ATOM 9005 C CG2 . ILE B 2 236 ? 14.757 17.502 27.623 1.00 85.46 ? 236 ILE B CG2 1 ATOM 9006 C CD1 . ILE B 2 236 ? 13.059 15.529 30.137 1.00 89.07 ? 236 ILE B CD1 1 ATOM 9007 N N . GLY B 2 237 ? 14.607 12.971 27.194 1.00 106.77 ? 237 GLY B N 1 ATOM 9008 C CA . GLY B 2 237 ? 14.346 11.556 27.398 1.00 108.48 ? 237 GLY B CA 1 ATOM 9009 C C . GLY B 2 237 ? 13.196 11.132 28.298 1.00 118.09 ? 237 GLY B C 1 ATOM 9010 O O . GLY B 2 237 ? 13.373 10.268 29.156 1.00 136.43 ? 237 GLY B O 1 ATOM 9011 N N . TRP B 2 238 ? 12.018 11.720 28.106 1.00 98.12 ? 238 TRP B N 1 ATOM 9012 C CA . TRP B 2 238 ? 10.824 11.272 28.821 1.00 88.54 ? 238 TRP B CA 1 ATOM 9013 C C . TRP B 2 238 ? 10.420 9.856 28.411 1.00 87.53 ? 238 TRP B C 1 ATOM 9014 O O . TRP B 2 238 ? 10.359 9.552 27.220 1.00 89.37 ? 238 TRP B O 1 ATOM 9015 C CB . TRP B 2 238 ? 9.643 12.211 28.563 1.00 90.98 ? 238 TRP B CB 1 ATOM 9016 C CG . TRP B 2 238 ? 9.740 13.573 29.182 1.00 89.96 ? 238 TRP B CG 1 ATOM 9017 C CD1 . TRP B 2 238 ? 9.874 14.761 28.525 1.00 79.14 ? 238 TRP B CD1 1 ATOM 9018 C CD2 . TRP B 2 238 ? 9.679 13.893 30.579 1.00 86.57 ? 238 TRP B CD2 1 ATOM 9019 N NE1 . TRP B 2 238 ? 9.908 15.799 29.424 1.00 78.97 ? 238 TRP B NE1 1 ATOM 9020 C CE2 . TRP B 2 238 ? 9.789 15.293 30.692 1.00 78.71 ? 238 TRP B CE2 1 ATOM 9021 C CE3 . TRP B 2 238 ? 9.545 13.131 31.744 1.00 87.98 ? 238 TRP B CE3 1 ATOM 9022 C CZ2 . TRP B 2 238 ? 9.776 15.946 31.921 1.00 71.93 ? 238 TRP B CZ2 1 ATOM 9023 C CZ3 . TRP B 2 238 ? 9.530 13.783 32.964 1.00 89.20 ? 238 TRP B CZ3 1 ATOM 9024 C CH2 . TRP B 2 238 ? 9.645 15.176 33.043 1.00 83.76 ? 238 TRP B CH2 1 ATOM 9025 N N . ARG B 2 239 ? 10.141 8.998 29.391 1.00 104.67 ? 239 ARG B N 1 ATOM 9026 C CA . ARG B 2 239 ? 9.531 7.692 29.122 1.00 114.48 ? 239 ARG B CA 1 ATOM 9027 C C . ARG B 2 239 ? 8.182 8.061 28.515 1.00 115.48 ? 239 ARG B C 1 ATOM 9028 O O . ARG B 2 239 ? 7.673 9.150 28.761 1.00 105.13 ? 239 ARG B O 1 ATOM 9029 C CB . ARG B 2 239 ? 9.621 6.763 30.336 1.00 99.31 ? 239 ARG B CB 1 ATOM 9030 C CG . ARG B 2 239 ? 10.986 6.179 30.653 1.00 95.35 ? 239 ARG B CG 1 ATOM 9031 C CD . ARG B 2 239 ? 10.940 5.500 32.021 1.00 97.03 ? 239 ARG B CD 1 ATOM 9032 N NE . ARG B 2 239 ? 12.136 4.717 32.320 1.00 117.21 ? 239 ARG B NE 1 ATOM 9033 C CZ . ARG B 2 239 ? 12.181 3.388 32.321 1.00 132.13 ? 239 ARG B CZ 1 ATOM 9034 N NH1 . ARG B 2 239 ? 11.093 2.683 32.039 1.00 136.73 ? 239 ARG B NH1 1 ATOM 9035 N NH2 . ARG B 2 239 ? 13.315 2.762 32.609 1.00 122.38 ? 239 ARG B NH2 1 ATOM 9036 N N . ASN B 2 240 ? 7.594 7.160 27.736 1.00 119.09 ? 240 ASN B N 1 ATOM 9037 C CA . ASN B 2 240 ? 6.195 7.273 27.334 1.00 112.77 ? 240 ASN B CA 1 ATOM 9038 C C . ASN B 2 240 ? 5.269 6.447 28.221 1.00 98.43 ? 240 ASN B C 1 ATOM 9039 O O . ASN B 2 240 ? 4.067 6.699 28.282 1.00 99.40 ? 240 ASN B O 1 ATOM 9040 C CB . ASN B 2 240 ? 6.020 6.861 25.870 1.00 102.68 ? 240 ASN B CB 1 ATOM 9041 C CG . ASN B 2 240 ? 6.714 5.555 25.542 1.00 115.96 ? 240 ASN B CG 1 ATOM 9042 O OD1 . ASN B 2 240 ? 7.133 4.819 26.435 1.00 145.06 ? 240 ASN B OD1 1 ATOM 9043 N ND2 . ASN B 2 240 ? 6.841 5.261 24.253 1.00 103.89 ? 240 ASN B ND2 1 ATOM 9044 N N . ASP B 2 241 ? 5.838 5.467 28.913 1.00 113.53 ? 241 ASP B N 1 ATOM 9045 C CA . ASP B 2 241 ? 5.061 4.555 29.745 1.00 96.25 ? 241 ASP B CA 1 ATOM 9046 C C . ASP B 2 241 ? 5.003 4.993 31.206 1.00 93.77 ? 241 ASP B C 1 ATOM 9047 O O . ASP B 2 241 ? 4.436 4.295 32.042 1.00 119.82 ? 241 ASP B O 1 ATOM 9048 C CB . ASP B 2 241 ? 5.642 3.140 29.653 1.00 110.61 ? 241 ASP B CB 1 ATOM 9049 C CG . ASP B 2 241 ? 7.125 3.085 30.009 1.00 124.60 ? 241 ASP B CG 1 ATOM 9050 O OD1 . ASP B 2 241 ? 7.511 3.552 31.104 1.00 99.36 ? 241 ASP B OD1 1 ATOM 9051 O OD2 . ASP B 2 241 ? 7.911 2.569 29.186 1.00 131.20 ? 241 ASP B OD2 1 ATOM 9052 N N . ALA B 2 242 ? 5.582 6.149 31.508 1.00 108.86 ? 242 ALA B N 1 ATOM 9053 C CA . ALA B 2 242 ? 5.843 6.528 32.894 1.00 105.46 ? 242 ALA B CA 1 ATOM 9054 C C . ALA B 2 242 ? 5.145 7.815 33.316 1.00 85.87 ? 242 ALA B C 1 ATOM 9055 O O . ALA B 2 242 ? 4.684 8.592 32.482 1.00 88.64 ? 242 ALA B O 1 ATOM 9056 C CB . ALA B 2 242 ? 7.343 6.660 33.119 1.00 108.46 ? 242 ALA B CB 1 ATOM 9057 N N . SER B 2 243 ? 5.063 8.018 34.628 1.00 88.42 ? 243 SER B N 1 ATOM 9058 C CA . SER B 2 243 ? 4.528 9.250 35.192 1.00 103.10 ? 243 SER B CA 1 ATOM 9059 C C . SER B 2 243 ? 5.575 10.358 35.129 1.00 94.64 ? 243 SER B C 1 ATOM 9060 O O . SER B 2 243 ? 6.659 10.226 35.695 1.00 120.37 ? 243 SER B O 1 ATOM 9061 C CB . SER B 2 243 ? 4.080 9.027 36.636 1.00 108.38 ? 243 SER B CB 1 ATOM 9062 O OG . SER B 2 243 ? 3.631 10.234 37.225 1.00 100.55 ? 243 SER B OG 1 ATOM 9063 N N . HIS B 2 244 ? 5.243 11.450 34.447 1.00 77.20 ? 244 HIS B N 1 ATOM 9064 C CA . HIS B 2 244 ? 6.202 12.526 34.202 1.00 90.07 ? 244 HIS B CA 1 ATOM 9065 C C . HIS B 2 244 ? 6.071 13.675 35.193 1.00 92.81 ? 244 HIS B C 1 ATOM 9066 O O . HIS B 2 244 ? 5.047 14.356 35.229 1.00 104.34 ? 244 HIS B O 1 ATOM 9067 C CB . HIS B 2 244 ? 6.032 13.078 32.788 1.00 89.27 ? 244 HIS B CB 1 ATOM 9068 C CG . HIS B 2 244 ? 6.051 12.030 31.722 1.00 79.37 ? 244 HIS B CG 1 ATOM 9069 N ND1 . HIS B 2 244 ? 5.494 12.230 30.477 1.00 96.42 ? 244 HIS B ND1 1 ATOM 9070 C CD2 . HIS B 2 244 ? 6.562 10.778 31.709 1.00 87.72 ? 244 HIS B CD2 1 ATOM 9071 C CE1 . HIS B 2 244 ? 5.659 11.143 29.744 1.00 112.22 ? 244 HIS B CE1 1 ATOM 9072 N NE2 . HIS B 2 244 ? 6.302 10.246 30.470 1.00 116.93 ? 244 HIS B NE2 1 ATOM 9073 N N . LEU B 2 245 ? 7.113 13.902 35.984 1.00 75.42 ? 245 LEU B N 1 ATOM 9074 C CA . LEU B 2 245 ? 7.119 15.032 36.904 1.00 74.92 ? 245 LEU B CA 1 ATOM 9075 C C . LEU B 2 245 ? 8.230 16.011 36.555 1.00 85.71 ? 245 LEU B C 1 ATOM 9076 O O . LEU B 2 245 ? 9.399 15.634 36.463 1.00 91.33 ? 245 LEU B O 1 ATOM 9077 C CB . LEU B 2 245 ? 7.280 14.567 38.351 1.00 77.28 ? 245 LEU B CB 1 ATOM 9078 C CG . LEU B 2 245 ? 6.397 13.425 38.849 1.00 103.80 ? 245 LEU B CG 1 ATOM 9079 C CD1 . LEU B 2 245 ? 6.519 13.296 40.358 1.00 93.51 ? 245 LEU B CD1 1 ATOM 9080 C CD2 . LEU B 2 245 ? 4.950 13.628 38.438 1.00 110.41 ? 245 LEU B CD2 1 ATOM 9081 N N . LEU B 2 246 ? 7.855 17.270 36.363 1.00 85.11 ? 246 LEU B N 1 ATOM 9082 C CA . LEU B 2 246 ? 8.819 18.328 36.098 1.00 81.21 ? 246 LEU B CA 1 ATOM 9083 C C . LEU B 2 246 ? 8.854 19.307 37.266 1.00 79.36 ? 246 LEU B C 1 ATOM 9084 O O . LEU B 2 246 ? 7.920 20.087 37.457 1.00 79.22 ? 246 LEU B O 1 ATOM 9085 C CB . LEU B 2 246 ? 8.466 19.057 34.802 1.00 70.72 ? 246 LEU B CB 1 ATOM 9086 C CG . LEU B 2 246 ? 9.371 20.220 34.414 1.00 68.64 ? 246 LEU B CG 1 ATOM 9087 C CD1 . LEU B 2 246 ? 10.810 19.749 34.345 1.00 87.63 ? 246 LEU B CD1 1 ATOM 9088 C CD2 . LEU B 2 246 ? 8.932 20.812 33.086 1.00 66.77 ? 246 LEU B CD2 1 ATOM 9089 N N . VAL B 2 247 ? 9.937 19.275 38.037 1.00 73.56 ? 247 VAL B N 1 ATOM 9090 C CA . VAL B 2 247 ? 10.024 20.098 39.239 1.00 97.43 ? 247 VAL B CA 1 ATOM 9091 C C . VAL B 2 247 ? 10.788 21.396 38.982 1.00 100.20 ? 247 VAL B C 1 ATOM 9092 O O . VAL B 2 247 ? 11.947 21.389 38.564 1.00 90.08 ? 247 VAL B O 1 ATOM 9093 C CB . VAL B 2 247 ? 10.677 19.330 40.409 1.00 89.97 ? 247 VAL B CB 1 ATOM 9094 C CG1 . VAL B 2 247 ? 11.873 18.530 39.932 1.00 86.54 ? 247 VAL B CG1 1 ATOM 9095 C CG2 . VAL B 2 247 ? 11.068 20.289 41.524 1.00 113.26 ? 247 VAL B CG2 1 ATOM 9096 N N . PHE B 2 248 ? 10.113 22.508 39.249 1.00 94.15 ? 248 PHE B N 1 ATOM 9097 C CA . PHE B 2 248 ? 10.611 23.836 38.919 1.00 83.75 ? 248 PHE B CA 1 ATOM 9098 C C . PHE B 2 248 ? 11.024 24.581 40.183 1.00 81.17 ? 248 PHE B C 1 ATOM 9099 O O . PHE B 2 248 ? 10.187 24.885 41.032 1.00 84.66 ? 248 PHE B O 1 ATOM 9100 C CB . PHE B 2 248 ? 9.532 24.608 38.157 1.00 70.46 ? 248 PHE B CB 1 ATOM 9101 C CG . PHE B 2 248 ? 10.013 25.876 37.528 1.00 79.80 ? 248 PHE B CG 1 ATOM 9102 C CD1 . PHE B 2 248 ? 10.826 25.844 36.410 1.00 85.57 ? 248 PHE B CD1 1 ATOM 9103 C CD2 . PHE B 2 248 ? 9.625 27.104 38.037 1.00 78.54 ? 248 PHE B CD2 1 ATOM 9104 C CE1 . PHE B 2 248 ? 11.261 27.014 35.820 1.00 69.60 ? 248 PHE B CE1 1 ATOM 9105 C CE2 . PHE B 2 248 ? 10.055 28.277 37.454 1.00 71.35 ? 248 PHE B CE2 1 ATOM 9106 C CZ . PHE B 2 248 ? 10.874 28.232 36.343 1.00 85.42 ? 248 PHE B CZ 1 ATOM 9107 N N . THR B 2 249 ? 12.316 24.867 40.311 1.00 80.49 ? 249 THR B N 1 ATOM 9108 C CA . THR B 2 249 ? 12.829 25.507 41.520 1.00 94.63 ? 249 THR B CA 1 ATOM 9109 C C . THR B 2 249 ? 13.377 26.911 41.262 1.00 102.87 ? 249 THR B C 1 ATOM 9110 O O . THR B 2 249 ? 14.364 27.086 40.547 1.00 104.20 ? 249 THR B O 1 ATOM 9111 C CB . THR B 2 249 ? 13.937 24.658 42.180 1.00 78.74 ? 249 THR B CB 1 ATOM 9112 O OG1 . THR B 2 249 ? 14.990 24.419 41.239 1.00 88.50 ? 249 THR B OG1 1 ATOM 9113 C CG2 . THR B 2 249 ? 13.380 23.328 42.642 1.00 86.36 ? 249 THR B CG2 1 ATOM 9114 N N . THR B 2 250 ? 12.718 27.906 41.848 1.00 85.33 ? 250 THR B N 1 ATOM 9115 C CA . THR B 2 250 ? 13.185 29.285 41.797 1.00 76.80 ? 250 THR B CA 1 ATOM 9116 C C . THR B 2 250 ? 12.713 30.048 43.032 1.00 83.59 ? 250 THR B C 1 ATOM 9117 O O . THR B 2 250 ? 11.653 29.754 43.584 1.00 82.97 ? 250 THR B O 1 ATOM 9118 C CB . THR B 2 250 ? 12.698 30.002 40.527 1.00 83.86 ? 250 THR B CB 1 ATOM 9119 O OG1 . THR B 2 250 ? 13.128 31.370 40.553 1.00 93.36 ? 250 THR B OG1 1 ATOM 9120 C CG2 . THR B 2 250 ? 11.179 29.951 40.430 1.00 80.57 ? 250 THR B CG2 1 ATOM 9121 N N . ASP B 2 251 ? 13.514 31.008 43.482 1.00 89.13 ? 251 ASP B N 1 ATOM 9122 C CA . ASP B 2 251 ? 13.153 31.816 44.643 1.00 84.44 ? 251 ASP B CA 1 ATOM 9123 C C . ASP B 2 251 ? 12.551 33.169 44.279 1.00 81.52 ? 251 ASP B C 1 ATOM 9124 O O . ASP B 2 251 ? 12.147 33.923 45.162 1.00 94.40 ? 251 ASP B O 1 ATOM 9125 C CB . ASP B 2 251 ? 14.372 32.044 45.528 1.00 84.70 ? 251 ASP B CB 1 ATOM 9126 C CG . ASP B 2 251 ? 15.397 32.939 44.874 1.00 92.56 ? 251 ASP B CG 1 ATOM 9127 O OD1 . ASP B 2 251 ? 15.603 32.812 43.650 1.00 85.76 ? 251 ASP B OD1 1 ATOM 9128 O OD2 . ASP B 2 251 ? 15.989 33.778 45.584 1.00 126.25 ? 251 ASP B OD2 1 ATOM 9129 N N . ALA B 2 252 ? 12.491 33.481 42.989 1.00 73.51 ? 252 ALA B N 1 ATOM 9130 C CA . ALA B 2 252 ? 12.084 34.818 42.570 1.00 89.37 ? 252 ALA B CA 1 ATOM 9131 C C . ALA B 2 252 ? 10.946 34.811 41.561 1.00 72.04 ? 252 ALA B C 1 ATOM 9132 O O . ALA B 2 252 ? 10.403 33.765 41.215 1.00 74.66 ? 252 ALA B O 1 ATOM 9133 C CB . ALA B 2 252 ? 13.278 35.570 41.997 1.00 119.09 ? 252 ALA B CB 1 ATOM 9134 N N . LYS B 2 253 ? 10.609 35.999 41.075 1.00 84.94 ? 253 LYS B N 1 ATOM 9135 C CA . LYS B 2 253 ? 9.534 36.163 40.110 1.00 75.08 ? 253 LYS B CA 1 ATOM 9136 C C . LYS B 2 253 ? 9.955 35.581 38.772 1.00 71.73 ? 253 LYS B C 1 ATOM 9137 O O . LYS B 2 253 ? 11.061 35.063 38.632 1.00 91.43 ? 253 LYS B O 1 ATOM 9138 C CB . LYS B 2 253 ? 9.174 37.642 39.957 1.00 86.37 ? 253 LYS B CB 1 ATOM 9139 C CG . LYS B 2 253 ? 8.820 38.326 41.268 1.00 85.84 ? 253 LYS B CG 1 ATOM 9140 C CD . LYS B 2 253 ? 9.345 39.751 41.319 1.00 94.07 ? 253 LYS B CD 1 ATOM 9141 C CE . LYS B 2 253 ? 8.708 40.628 40.255 1.00 94.55 ? 253 LYS B CE 1 ATOM 9142 N NZ . LYS B 2 253 ? 9.191 42.035 40.357 1.00 100.40 ? 253 LYS B NZ 1 ATOM 9143 N N . THR B 2 254 ? 9.073 35.666 37.786 1.00 76.73 ? 254 THR B N 1 ATOM 9144 C CA . THR B 2 254 ? 9.382 35.115 36.475 1.00 73.44 ? 254 THR B CA 1 ATOM 9145 C C . THR B 2 254 ? 8.930 36.014 35.347 1.00 70.83 ? 254 THR B C 1 ATOM 9146 O O . THR B 2 254 ? 7.980 36.784 35.483 1.00 82.34 ? 254 THR B O 1 ATOM 9147 C CB . THR B 2 254 ? 8.733 33.742 36.262 1.00 64.54 ? 254 THR B CB 1 ATOM 9148 O OG1 . THR B 2 254 ? 8.996 33.303 34.924 1.00 68.12 ? 254 THR B OG1 1 ATOM 9149 C CG2 . THR B 2 254 ? 7.231 33.831 36.464 1.00 62.73 ? 254 THR B CG2 1 ATOM 9150 N N . HIS B 2 255 ? 9.619 35.901 34.221 1.00 69.75 ? 255 HIS B N 1 ATOM 9151 C CA . HIS B 2 255 ? 9.193 36.587 33.021 1.00 89.34 ? 255 HIS B CA 1 ATOM 9152 C C . HIS B 2 255 ? 8.013 35.862 32.402 1.00 76.38 ? 255 HIS B C 1 ATOM 9153 O O . HIS B 2 255 ? 7.919 34.636 32.446 1.00 85.77 ? 255 HIS B O 1 ATOM 9154 C CB . HIS B 2 255 ? 10.338 36.701 32.019 1.00 93.74 ? 255 HIS B CB 1 ATOM 9155 C CG . HIS B 2 255 ? 11.279 37.824 32.314 1.00 80.39 ? 255 HIS B CG 1 ATOM 9156 N ND1 . HIS B 2 255 ? 10.852 39.126 32.468 1.00 65.37 ? 255 HIS B ND1 1 ATOM 9157 C CD2 . HIS B 2 255 ? 12.621 37.844 32.489 1.00 64.12 ? 255 HIS B CD2 1 ATOM 9158 C CE1 . HIS B 2 255 ? 11.892 39.899 32.725 1.00 64.11 ? 255 HIS B CE1 1 ATOM 9159 N NE2 . HIS B 2 255 ? 12.977 39.146 32.744 1.00 63.83 ? 255 HIS B NE2 1 ATOM 9160 N N . ILE B 2 256 ? 7.117 36.648 31.826 1.00 60.58 ? 256 ILE B N 1 ATOM 9161 C CA . ILE B 2 256 ? 5.912 36.151 31.193 1.00 59.22 ? 256 ILE B CA 1 ATOM 9162 C C . ILE B 2 256 ? 5.931 36.625 29.752 1.00 60.25 ? 256 ILE B C 1 ATOM 9163 O O . ILE B 2 256 ? 6.720 37.498 29.403 1.00 58.74 ? 256 ILE B O 1 ATOM 9164 C CB . ILE B 2 256 ? 4.648 36.656 31.903 1.00 70.62 ? 256 ILE B CB 1 ATOM 9165 C CG1 . ILE B 2 256 ? 4.511 38.170 31.722 1.00 62.50 ? 256 ILE B CG1 1 ATOM 9166 C CG2 . ILE B 2 256 ? 4.693 36.305 33.380 1.00 59.94 ? 256 ILE B CG2 1 ATOM 9167 C CD1 . ILE B 2 256 ? 3.316 38.761 32.433 1.00 60.07 ? 256 ILE B CD1 1 ATOM 9168 N N . ALA B 2 257 ? 5.080 36.044 28.914 1.00 80.51 ? 257 ALA B N 1 ATOM 9169 C CA . ALA B 2 257 ? 5.049 36.397 27.500 1.00 62.29 ? 257 ALA B CA 1 ATOM 9170 C C . ALA B 2 257 ? 4.834 37.896 27.315 1.00 70.84 ? 257 ALA B C 1 ATOM 9171 O O . ALA B 2 257 ? 4.181 38.535 28.142 1.00 66.63 ? 257 ALA B O 1 ATOM 9172 C CB . ALA B 2 257 ? 3.969 35.614 26.781 1.00 61.01 ? 257 ALA B CB 1 ATOM 9173 N N . LEU B 2 258 ? 5.430 38.428 26.245 1.00 81.40 ? 258 LEU B N 1 ATOM 9174 C CA . LEU B 2 258 ? 5.392 39.845 25.855 1.00 68.35 ? 258 LEU B CA 1 ATOM 9175 C C . LEU B 2 258 ? 6.380 40.712 26.640 1.00 75.69 ? 258 LEU B C 1 ATOM 9176 O O . LEU B 2 258 ? 6.564 41.886 26.323 1.00 76.06 ? 258 LEU B O 1 ATOM 9177 C CB . LEU B 2 258 ? 3.977 40.421 25.982 1.00 59.90 ? 258 LEU B CB 1 ATOM 9178 C CG . LEU B 2 258 ? 2.926 39.802 25.061 1.00 58.87 ? 258 LEU B CG 1 ATOM 9179 C CD1 . LEU B 2 258 ? 1.566 40.440 25.291 1.00 59.30 ? 258 LEU B CD1 1 ATOM 9180 C CD2 . LEU B 2 258 ? 3.345 39.938 23.606 1.00 67.97 ? 258 LEU B CD2 1 ATOM 9181 N N . ASP B 2 259 ? 7.029 40.138 27.648 1.00 84.70 ? 259 ASP B N 1 ATOM 9182 C CA . ASP B 2 259 ? 8.082 40.856 28.360 1.00 66.95 ? 259 ASP B CA 1 ATOM 9183 C C . ASP B 2 259 ? 9.295 41.058 27.456 1.00 76.58 ? 259 ASP B C 1 ATOM 9184 O O . ASP B 2 259 ? 10.045 42.022 27.610 1.00 90.97 ? 259 ASP B O 1 ATOM 9185 C CB . ASP B 2 259 ? 8.497 40.110 29.632 1.00 77.02 ? 259 ASP B CB 1 ATOM 9186 C CG . ASP B 2 259 ? 7.528 40.320 30.779 1.00 69.12 ? 259 ASP B CG 1 ATOM 9187 O OD1 . ASP B 2 259 ? 6.648 41.197 30.663 1.00 72.41 ? 259 ASP B OD1 1 ATOM 9188 O OD2 . ASP B 2 259 ? 7.658 39.618 31.804 1.00 60.59 ? 259 ASP B OD2 1 ATOM 9189 N N . GLY B 2 260 ? 9.473 40.145 26.507 1.00 70.06 ? 260 GLY B N 1 ATOM 9190 C CA . GLY B 2 260 ? 10.631 40.160 25.632 1.00 61.86 ? 260 GLY B CA 1 ATOM 9191 C C . GLY B 2 260 ? 10.675 41.315 24.652 1.00 67.82 ? 260 GLY B C 1 ATOM 9192 O O . GLY B 2 260 ? 11.662 41.489 23.939 1.00 69.33 ? 260 GLY B O 1 ATOM 9193 N N . ARG B 2 261 ? 9.608 42.106 24.613 1.00 61.89 ? 261 ARG B N 1 ATOM 9194 C CA . ARG B 2 261 ? 9.545 43.257 23.717 1.00 63.49 ? 261 ARG B CA 1 ATOM 9195 C C . ARG B 2 261 ? 10.623 44.273 24.081 1.00 73.21 ? 261 ARG B C 1 ATOM 9196 O O . ARG B 2 261 ? 11.141 44.980 23.218 1.00 64.90 ? 261 ARG B O 1 ATOM 9197 C CB . ARG B 2 261 ? 8.161 43.905 23.778 1.00 62.21 ? 261 ARG B CB 1 ATOM 9198 C CG . ARG B 2 261 ? 7.769 44.729 22.560 1.00 63.14 ? 261 ARG B CG 1 ATOM 9199 C CD . ARG B 2 261 ? 6.447 45.438 22.826 1.00 63.41 ? 261 ARG B CD 1 ATOM 9200 N NE . ARG B 2 261 ? 5.740 45.827 21.611 1.00 78.62 ? 261 ARG B NE 1 ATOM 9201 C CZ . ARG B 2 261 ? 5.822 47.028 21.050 1.00 72.76 ? 261 ARG B CZ 1 ATOM 9202 N NH1 . ARG B 2 261 ? 6.592 47.963 21.587 1.00 77.47 ? 261 ARG B NH1 1 ATOM 9203 N NH2 . ARG B 2 261 ? 5.137 47.291 19.947 1.00 77.09 ? 261 ARG B NH2 1 ATOM 9204 N N . LEU B 2 262 ? 10.961 44.337 25.366 1.00 77.63 ? 262 LEU B N 1 ATOM 9205 C CA . LEU B 2 262 ? 11.961 45.286 25.839 1.00 65.46 ? 262 LEU B CA 1 ATOM 9206 C C . LEU B 2 262 ? 13.330 44.927 25.286 1.00 73.49 ? 262 LEU B C 1 ATOM 9207 O O . LEU B 2 262 ? 14.128 45.803 24.962 1.00 88.84 ? 262 LEU B O 1 ATOM 9208 C CB . LEU B 2 262 ? 12.016 45.321 27.368 1.00 63.94 ? 262 LEU B CB 1 ATOM 9209 C CG . LEU B 2 262 ? 10.745 45.602 28.173 1.00 69.04 ? 262 LEU B CG 1 ATOM 9210 C CD1 . LEU B 2 262 ? 11.109 46.199 29.524 1.00 64.48 ? 262 LEU B CD1 1 ATOM 9211 C CD2 . LEU B 2 262 ? 9.782 46.502 27.425 1.00 65.77 ? 262 LEU B CD2 1 ATOM 9212 N N . ALA B 2 263 ? 13.589 43.629 25.167 1.00 65.59 ? 263 ALA B N 1 ATOM 9213 C CA . ALA B 2 263 ? 14.875 43.151 24.678 1.00 67.22 ? 263 ALA B CA 1 ATOM 9214 C C . ALA B 2 263 ? 14.913 43.198 23.158 1.00 68.98 ? 263 ALA B C 1 ATOM 9215 O O . ALA B 2 263 ? 15.915 42.837 22.538 1.00 71.01 ? 263 ALA B O 1 ATOM 9216 C CB . ALA B 2 263 ? 15.144 41.743 25.176 1.00 72.04 ? 263 ALA B CB 1 ATOM 9217 N N . GLY B 2 264 ? 13.810 43.641 22.563 1.00 66.89 ? 264 GLY B N 1 ATOM 9218 C CA . GLY B 2 264 ? 13.700 43.721 21.120 1.00 68.33 ? 264 GLY B CA 1 ATOM 9219 C C . GLY B 2 264 ? 13.274 42.404 20.502 1.00 73.90 ? 264 GLY B C 1 ATOM 9220 O O . GLY B 2 264 ? 13.571 42.138 19.339 1.00 77.77 ? 264 GLY B O 1 ATOM 9221 N N . ILE B 2 265 ? 12.584 41.573 21.280 1.00 66.68 ? 265 ILE B N 1 ATOM 9222 C CA . ILE B 2 265 ? 12.114 40.290 20.773 1.00 67.96 ? 265 ILE B CA 1 ATOM 9223 C C . ILE B 2 265 ? 10.612 40.311 20.507 1.00 65.71 ? 265 ILE B C 1 ATOM 9224 O O . ILE B 2 265 ? 9.803 40.240 21.433 1.00 64.07 ? 265 ILE B O 1 ATOM 9225 C CB . ILE B 2 265 ? 12.429 39.163 21.767 1.00 67.91 ? 265 ILE B CB 1 ATOM 9226 C CG1 . ILE B 2 265 ? 13.883 39.255 22.228 1.00 67.47 ? 265 ILE B CG1 1 ATOM 9227 C CG2 . ILE B 2 265 ? 12.135 37.814 21.151 1.00 69.42 ? 265 ILE B CG2 1 ATOM 9228 C CD1 . ILE B 2 265 ? 14.238 38.253 23.299 1.00 70.59 ? 265 ILE B CD1 1 ATOM 9229 N N . VAL B 2 266 ? 10.246 40.392 19.233 1.00 66.57 ? 266 VAL B N 1 ATOM 9230 C CA . VAL B 2 266 ? 8.844 40.463 18.842 1.00 65.88 ? 266 VAL B CA 1 ATOM 9231 C C . VAL B 2 266 ? 8.257 39.150 18.322 1.00 75.08 ? 266 VAL B C 1 ATOM 9232 O O . VAL B 2 266 ? 7.082 39.095 17.961 1.00 73.36 ? 266 VAL B O 1 ATOM 9233 C CB . VAL B 2 266 ? 8.643 41.546 17.785 1.00 78.37 ? 266 VAL B CB 1 ATOM 9234 C CG1 . VAL B 2 266 ? 8.793 42.915 18.422 1.00 68.46 ? 266 VAL B CG1 1 ATOM 9235 C CG2 . VAL B 2 266 ? 9.640 41.362 16.657 1.00 101.99 ? 266 VAL B CG2 1 ATOM 9236 N N . GLN B 2 267 ? 9.069 38.102 18.259 1.00 72.35 ? 267 GLN B N 1 ATOM 9237 C CA . GLN B 2 267 ? 8.599 36.833 17.712 1.00 77.52 ? 267 GLN B CA 1 ATOM 9238 C C . GLN B 2 267 ? 8.016 35.934 18.792 1.00 73.80 ? 267 GLN B C 1 ATOM 9239 O O . GLN B 2 267 ? 8.699 35.603 19.761 1.00 68.58 ? 267 GLN B O 1 ATOM 9240 C CB . GLN B 2 267 ? 9.728 36.099 16.993 1.00 91.71 ? 267 GLN B CB 1 ATOM 9241 C CG . GLN B 2 267 ? 9.279 34.818 16.314 1.00 81.93 ? 267 GLN B CG 1 ATOM 9242 C CD . GLN B 2 267 ? 10.434 34.028 15.743 1.00 96.95 ? 267 GLN B CD 1 ATOM 9243 O OE1 . GLN B 2 267 ? 11.581 34.197 16.158 1.00 103.06 ? 267 GLN B OE1 1 ATOM 9244 N NE2 . GLN B 2 267 ? 10.140 33.159 14.782 1.00 106.98 ? 267 GLN B NE2 1 ATOM 9245 N N . PRO B 2 268 ? 6.749 35.525 18.615 1.00 80.74 ? 268 PRO B N 1 ATOM 9246 C CA . PRO B 2 268 ? 6.040 34.682 19.582 1.00 63.86 ? 268 PRO B CA 1 ATOM 9247 C C . PRO B 2 268 ? 6.667 33.305 19.697 1.00 64.55 ? 268 PRO B C 1 ATOM 9248 O O . PRO B 2 268 ? 7.228 32.797 18.727 1.00 79.52 ? 268 PRO B O 1 ATOM 9249 C CB . PRO B 2 268 ? 4.625 34.583 19.001 1.00 63.70 ? 268 PRO B CB 1 ATOM 9250 C CG . PRO B 2 268 ? 4.526 35.689 18.013 1.00 64.62 ? 268 PRO B CG 1 ATOM 9251 C CD . PRO B 2 268 ? 5.902 35.853 17.460 1.00 76.84 ? 268 PRO B CD 1 ATOM 9252 N N . ASN B 2 269 ? 6.574 32.718 20.883 1.00 67.71 ? 269 ASN B N 1 ATOM 9253 C CA . ASN B 2 269 ? 7.105 31.387 21.130 1.00 67.61 ? 269 ASN B CA 1 ATOM 9254 C C . ASN B 2 269 ? 6.384 30.345 20.285 1.00 71.74 ? 269 ASN B C 1 ATOM 9255 O O . ASN B 2 269 ? 5.153 30.329 20.231 1.00 71.19 ? 269 ASN B O 1 ATOM 9256 C CB . ASN B 2 269 ? 6.986 31.045 22.620 1.00 63.10 ? 269 ASN B CB 1 ATOM 9257 C CG . ASN B 2 269 ? 7.929 29.939 23.049 1.00 67.57 ? 269 ASN B CG 1 ATOM 9258 O OD1 . ASN B 2 269 ? 8.142 28.971 22.327 1.00 72.13 ? 269 ASN B OD1 1 ATOM 9259 N ND2 . ASN B 2 269 ? 8.507 30.084 24.234 1.00 100.35 ? 269 ASN B ND2 1 ATOM 9260 N N . ASP B 2 270 ? 7.150 29.494 19.605 1.00 79.64 ? 270 ASP B N 1 ATOM 9261 C CA . ASP B 2 270 ? 6.576 28.302 18.989 1.00 75.19 ? 270 ASP B CA 1 ATOM 9262 C C . ASP B 2 270 ? 6.829 27.104 19.898 1.00 89.35 ? 270 ASP B C 1 ATOM 9263 O O . ASP B 2 270 ? 7.867 27.008 20.550 1.00 114.55 ? 270 ASP B O 1 ATOM 9264 C CB . ASP B 2 270 ? 7.133 28.056 17.578 1.00 76.31 ? 270 ASP B CB 1 ATOM 9265 C CG . ASP B 2 270 ? 8.655 28.045 17.521 1.00 90.81 ? 270 ASP B CG 1 ATOM 9266 O OD1 . ASP B 2 270 ? 9.317 27.853 18.560 1.00 100.47 ? 270 ASP B OD1 1 ATOM 9267 O OD2 . ASP B 2 270 ? 9.197 28.218 16.408 1.00 106.16 ? 270 ASP B OD2 1 ATOM 9268 N N . GLY B 2 271 ? 5.880 26.183 19.944 1.00 77.47 ? 271 GLY B N 1 ATOM 9269 C CA . GLY B 2 271 ? 5.967 25.079 20.879 1.00 84.77 ? 271 GLY B CA 1 ATOM 9270 C C . GLY B 2 271 ? 6.988 24.039 20.468 1.00 88.57 ? 271 GLY B C 1 ATOM 9271 O O . GLY B 2 271 ? 7.001 22.934 21.004 1.00 129.01 ? 271 GLY B O 1 ATOM 9272 N N . GLN B 2 272 ? 7.839 24.382 19.506 1.00 77.35 ? 272 GLN B N 1 ATOM 9273 C CA . GLN B 2 272 ? 8.802 23.429 18.974 1.00 95.81 ? 272 GLN B CA 1 ATOM 9274 C C . GLN B 2 272 ? 10.058 23.330 19.841 1.00 89.79 ? 272 GLN B C 1 ATOM 9275 O O . GLN B 2 272 ? 10.225 24.084 20.798 1.00 80.71 ? 272 GLN B O 1 ATOM 9276 C CB . GLN B 2 272 ? 9.166 23.817 17.542 1.00 95.69 ? 272 GLN B CB 1 ATOM 9277 C CG . GLN B 2 272 ? 7.946 24.055 16.662 1.00 101.97 ? 272 GLN B CG 1 ATOM 9278 C CD . GLN B 2 272 ? 8.306 24.397 15.231 1.00 128.20 ? 272 GLN B CD 1 ATOM 9279 O OE1 . GLN B 2 272 ? 9.444 24.209 14.802 1.00 146.34 ? 272 GLN B OE1 1 ATOM 9280 N NE2 . GLN B 2 272 ? 7.333 24.904 14.483 1.00 127.42 ? 272 GLN B NE2 1 ATOM 9281 N N . CYS B 2 273 ? 10.947 22.407 19.487 1.00 105.36 ? 273 CYS B N 1 ATOM 9282 C CA . CYS B 2 273 ? 12.133 22.145 20.293 1.00 103.13 ? 273 CYS B CA 1 ATOM 9283 C C . CYS B 2 273 ? 13.383 22.717 19.641 1.00 104.68 ? 273 CYS B C 1 ATOM 9284 O O . CYS B 2 273 ? 13.854 22.208 18.624 1.00 120.03 ? 273 CYS B O 1 ATOM 9285 C CB . CYS B 2 273 ? 12.302 20.641 20.521 1.00 97.11 ? 273 CYS B CB 1 ATOM 9286 S SG . CYS B 2 273 ? 13.825 20.183 21.384 1.00 98.79 ? 273 CYS B SG 1 ATOM 9287 N N . HIS B 2 274 ? 13.910 23.785 20.228 1.00 100.86 ? 274 HIS B N 1 ATOM 9288 C CA . HIS B 2 274 ? 15.088 24.449 19.683 1.00 115.33 ? 274 HIS B CA 1 ATOM 9289 C C . HIS B 2 274 ? 16.398 24.086 20.384 1.00 110.42 ? 274 HIS B C 1 ATOM 9290 O O . HIS B 2 274 ? 17.453 24.623 20.045 1.00 130.48 ? 274 HIS B O 1 ATOM 9291 C CB . HIS B 2 274 ? 14.869 25.959 19.698 1.00 96.04 ? 274 HIS B CB 1 ATOM 9292 C CG . HIS B 2 274 ? 13.700 26.391 18.869 1.00 92.33 ? 274 HIS B CG 1 ATOM 9293 N ND1 . HIS B 2 274 ? 13.677 26.261 17.497 1.00 90.17 ? 274 HIS B ND1 1 ATOM 9294 C CD2 . HIS B 2 274 ? 12.504 26.920 19.218 1.00 90.60 ? 274 HIS B CD2 1 ATOM 9295 C CE1 . HIS B 2 274 ? 12.523 26.706 17.035 1.00 91.73 ? 274 HIS B CE1 1 ATOM 9296 N NE2 . HIS B 2 274 ? 11.793 27.112 18.058 1.00 89.69 ? 274 HIS B NE2 1 ATOM 9297 N N . VAL B 2 275 ? 16.337 23.185 21.360 1.00 91.64 ? 275 VAL B N 1 ATOM 9298 C CA . VAL B 2 275 ? 17.554 22.724 22.022 1.00 93.73 ? 275 VAL B CA 1 ATOM 9299 C C . VAL B 2 275 ? 18.312 21.762 21.109 1.00 102.81 ? 275 VAL B C 1 ATOM 9300 O O . VAL B 2 275 ? 17.777 20.735 20.694 1.00 112.72 ? 275 VAL B O 1 ATOM 9301 C CB . VAL B 2 275 ? 17.252 22.025 23.361 1.00 79.60 ? 275 VAL B CB 1 ATOM 9302 C CG1 . VAL B 2 275 ? 18.545 21.635 24.057 1.00 81.19 ? 275 VAL B CG1 1 ATOM 9303 C CG2 . VAL B 2 275 ? 16.417 22.925 24.254 1.00 77.27 ? 275 VAL B CG2 1 ATOM 9304 N N . GLY B 2 276 ? 19.562 22.097 20.805 1.00 107.80 ? 276 GLY B N 1 ATOM 9305 C CA . GLY B 2 276 ? 20.348 21.324 19.860 1.00 121.25 ? 276 GLY B CA 1 ATOM 9306 C C . GLY B 2 276 ? 21.375 20.409 20.498 1.00 115.83 ? 276 GLY B C 1 ATOM 9307 O O . GLY B 2 276 ? 21.291 20.093 21.683 1.00 110.98 ? 276 GLY B O 1 ATOM 9308 N N . SER B 2 277 ? 22.353 19.989 19.701 1.00 120.23 ? 277 SER B N 1 ATOM 9309 C CA . SER B 2 277 ? 23.395 19.076 20.161 1.00 130.13 ? 277 SER B CA 1 ATOM 9310 C C . SER B 2 277 ? 24.293 19.727 21.206 1.00 118.05 ? 277 SER B C 1 ATOM 9311 O O . SER B 2 277 ? 24.977 19.040 21.964 1.00 122.45 ? 277 SER B O 1 ATOM 9312 C CB . SER B 2 277 ? 24.240 18.594 18.982 1.00 133.56 ? 277 SER B CB 1 ATOM 9313 O OG . SER B 2 277 ? 24.914 19.678 18.367 1.00 124.91 ? 277 SER B OG 1 ATOM 9314 N N . ASP B 2 278 ? 24.286 21.055 21.239 1.00 106.89 ? 278 ASP B N 1 ATOM 9315 C CA . ASP B 2 278 ? 25.075 21.799 22.211 1.00 103.75 ? 278 ASP B CA 1 ATOM 9316 C C . ASP B 2 278 ? 24.327 21.914 23.536 1.00 98.12 ? 278 ASP B C 1 ATOM 9317 O O . ASP B 2 278 ? 24.827 22.512 24.488 1.00 92.03 ? 278 ASP B O 1 ATOM 9318 C CB . ASP B 2 278 ? 25.421 23.188 21.673 1.00 118.58 ? 278 ASP B CB 1 ATOM 9319 C CG . ASP B 2 278 ? 24.191 24.018 21.367 1.00 137.06 ? 278 ASP B CG 1 ATOM 9320 O OD1 . ASP B 2 278 ? 23.153 23.430 20.992 1.00 144.41 ? 278 ASP B OD1 1 ATOM 9321 O OD2 . ASP B 2 278 ? 24.263 25.258 21.503 1.00 124.88 ? 278 ASP B OD2 1 ATOM 9322 N N . ASN B 2 279 ? 23.123 21.347 23.574 1.00 111.89 ? 279 ASN B N 1 ATOM 9323 C CA . ASN B 2 279 ? 22.303 21.296 24.784 1.00 107.90 ? 279 ASN B CA 1 ATOM 9324 C C . ASN B 2 279 ? 21.952 22.673 25.337 1.00 95.34 ? 279 ASN B C 1 ATOM 9325 O O . ASN B 2 279 ? 21.741 22.835 26.539 1.00 92.49 ? 279 ASN B O 1 ATOM 9326 C CB . ASN B 2 279 ? 23.004 20.470 25.863 1.00 111.41 ? 279 ASN B CB 1 ATOM 9327 C CG . ASN B 2 279 ? 23.163 19.019 25.471 1.00 114.91 ? 279 ASN B CG 1 ATOM 9328 O OD1 . ASN B 2 279 ? 22.243 18.405 24.933 1.00 122.12 ? 279 ASN B OD1 1 ATOM 9329 N ND2 . ASN B 2 279 ? 24.340 18.461 25.732 1.00 128.59 ? 279 ASN B ND2 1 ATOM 9330 N N . HIS B 2 280 ? 21.888 23.662 24.454 1.00 105.30 ? 280 HIS B N 1 ATOM 9331 C CA . HIS B 2 280 ? 21.477 25.005 24.839 1.00 93.24 ? 280 HIS B CA 1 ATOM 9332 C C . HIS B 2 280 ? 20.234 25.418 24.063 1.00 90.62 ? 280 HIS B C 1 ATOM 9333 O O . HIS B 2 280 ? 19.965 24.897 22.980 1.00 95.04 ? 280 HIS B O 1 ATOM 9334 C CB . HIS B 2 280 ? 22.609 26.007 24.603 1.00 95.96 ? 280 HIS B CB 1 ATOM 9335 C CG . HIS B 2 280 ? 23.572 26.112 25.745 1.00 96.58 ? 280 HIS B CG 1 ATOM 9336 N ND1 . HIS B 2 280 ? 24.902 26.431 25.570 1.00 104.22 ? 280 HIS B ND1 1 ATOM 9337 C CD2 . HIS B 2 280 ? 23.396 25.955 27.078 1.00 100.15 ? 280 HIS B CD2 1 ATOM 9338 C CE1 . HIS B 2 280 ? 25.504 26.459 26.746 1.00 104.31 ? 280 HIS B CE1 1 ATOM 9339 N NE2 . HIS B 2 280 ? 24.612 26.174 27.677 1.00 95.28 ? 280 HIS B NE2 1 ATOM 9340 N N . TYR B 2 281 ? 19.484 26.367 24.608 1.00 86.99 ? 281 TYR B N 1 ATOM 9341 C CA . TYR B 2 281 ? 18.269 26.824 23.954 1.00 84.96 ? 281 TYR B CA 1 ATOM 9342 C C . TYR B 2 281 ? 18.639 27.979 23.033 1.00 93.44 ? 281 TYR B C 1 ATOM 9343 O O . TYR B 2 281 ? 18.989 29.068 23.489 1.00 97.60 ? 281 TYR B O 1 ATOM 9344 C CB . TYR B 2 281 ? 17.227 27.246 24.995 1.00 77.24 ? 281 TYR B CB 1 ATOM 9345 C CG . TYR B 2 281 ? 15.934 27.788 24.430 1.00 74.65 ? 281 TYR B CG 1 ATOM 9346 C CD1 . TYR B 2 281 ? 15.426 27.329 23.222 1.00 81.63 ? 281 TYR B CD1 1 ATOM 9347 C CD2 . TYR B 2 281 ? 15.221 28.770 25.107 1.00 81.69 ? 281 TYR B CD2 1 ATOM 9348 C CE1 . TYR B 2 281 ? 14.242 27.829 22.708 1.00 81.79 ? 281 TYR B CE1 1 ATOM 9349 C CE2 . TYR B 2 281 ? 14.041 29.276 24.602 1.00 88.26 ? 281 TYR B CE2 1 ATOM 9350 C CZ . TYR B 2 281 ? 13.555 28.803 23.403 1.00 86.61 ? 281 TYR B CZ 1 ATOM 9351 O OH . TYR B 2 281 ? 12.377 29.309 22.903 1.00 91.32 ? 281 TYR B OH 1 ATOM 9352 N N . SER B 2 282 ? 18.552 27.728 21.731 1.00 81.39 ? 282 SER B N 1 ATOM 9353 C CA . SER B 2 282 ? 19.076 28.646 20.728 1.00 83.80 ? 282 SER B CA 1 ATOM 9354 C C . SER B 2 282 ? 18.155 29.830 20.474 1.00 88.72 ? 282 SER B C 1 ATOM 9355 O O . SER B 2 282 ? 18.616 30.950 20.243 1.00 126.10 ? 282 SER B O 1 ATOM 9356 C CB . SER B 2 282 ? 19.326 27.900 19.419 1.00 91.99 ? 282 SER B CB 1 ATOM 9357 O OG . SER B 2 282 ? 18.143 27.265 18.971 1.00 118.23 ? 282 SER B OG 1 ATOM 9358 N N . ALA B 2 283 ? 16.853 29.580 20.520 1.00 78.17 ? 283 ALA B N 1 ATOM 9359 C CA . ALA B 2 283 ? 15.867 30.612 20.227 1.00 87.33 ? 283 ALA B CA 1 ATOM 9360 C C . ALA B 2 283 ? 15.747 31.615 21.366 1.00 87.19 ? 283 ALA B C 1 ATOM 9361 O O . ALA B 2 283 ? 15.071 32.635 21.227 1.00 85.29 ? 283 ALA B O 1 ATOM 9362 C CB . ALA B 2 283 ? 14.514 29.982 19.934 1.00 97.69 ? 283 ALA B CB 1 ATOM 9363 N N . SER B 2 284 ? 16.416 31.324 22.479 1.00 85.74 ? 284 SER B N 1 ATOM 9364 C CA . SER B 2 284 ? 16.331 32.136 23.692 1.00 81.33 ? 284 SER B CA 1 ATOM 9365 C C . SER B 2 284 ? 16.503 33.629 23.433 1.00 76.96 ? 284 SER B C 1 ATOM 9366 O O . SER B 2 284 ? 15.774 34.444 23.997 1.00 81.82 ? 284 SER B O 1 ATOM 9367 C CB . SER B 2 284 ? 17.374 31.675 24.709 1.00 83.64 ? 284 SER B CB 1 ATOM 9368 O OG . SER B 2 284 ? 17.254 32.400 25.920 1.00 82.77 ? 284 SER B OG 1 ATOM 9369 N N . THR B 2 285 ? 17.460 33.987 22.582 1.00 80.25 ? 285 THR B N 1 ATOM 9370 C CA . THR B 2 285 ? 17.668 35.391 22.232 1.00 73.94 ? 285 THR B CA 1 ATOM 9371 C C . THR B 2 285 ? 16.670 35.880 21.186 1.00 80.09 ? 285 THR B C 1 ATOM 9372 O O . THR B 2 285 ? 16.282 37.044 21.191 1.00 76.95 ? 285 THR B O 1 ATOM 9373 C CB . THR B 2 285 ? 19.089 35.649 21.694 1.00 76.59 ? 285 THR B CB 1 ATOM 9374 O OG1 . THR B 2 285 ? 19.268 34.957 20.452 1.00 90.35 ? 285 THR B OG1 1 ATOM 9375 C CG2 . THR B 2 285 ? 20.137 35.190 22.691 1.00 77.69 ? 285 THR B CG2 1 ATOM 9376 N N . THR B 2 286 ? 16.267 34.994 20.282 1.00 87.05 ? 286 THR B N 1 ATOM 9377 C CA . THR B 2 286 ? 15.442 35.397 19.148 1.00 77.35 ? 286 THR B CA 1 ATOM 9378 C C . THR B 2 286 ? 13.939 35.189 19.346 1.00 83.56 ? 286 THR B C 1 ATOM 9379 O O . THR B 2 286 ? 13.144 35.589 18.495 1.00 78.75 ? 286 THR B O 1 ATOM 9380 C CB . THR B 2 286 ? 15.863 34.638 17.877 1.00 79.93 ? 286 THR B CB 1 ATOM 9381 O OG1 . THR B 2 286 ? 15.607 33.237 18.046 1.00 77.96 ? 286 THR B OG1 1 ATOM 9382 C CG2 . THR B 2 286 ? 17.341 34.844 17.605 1.00 87.92 ? 286 THR B CG2 1 ATOM 9383 N N . MET B 2 287 ? 13.547 34.585 20.465 1.00 74.55 ? 287 MET B N 1 ATOM 9384 C CA . MET B 2 287 ? 12.149 34.199 20.664 1.00 74.72 ? 287 MET B CA 1 ATOM 9385 C C . MET B 2 287 ? 11.626 34.560 22.057 1.00 73.18 ? 287 MET B C 1 ATOM 9386 O O . MET B 2 287 ? 12.326 34.398 23.056 1.00 74.97 ? 287 MET B O 1 ATOM 9387 C CB . MET B 2 287 ? 11.984 32.699 20.411 1.00 105.04 ? 287 MET B CB 1 ATOM 9388 C CG . MET B 2 287 ? 10.552 32.201 20.483 1.00 124.81 ? 287 MET B CG 1 ATOM 9389 S SD . MET B 2 287 ? 10.373 30.510 19.876 1.00 82.58 ? 287 MET B SD 1 ATOM 9390 C CE . MET B 2 287 ? 10.958 30.702 18.190 1.00 71.69 ? 287 MET B CE 1 ATOM 9391 N N . ASP B 2 288 ? 10.387 35.046 22.104 1.00 64.75 ? 288 ASP B N 1 ATOM 9392 C CA . ASP B 2 288 ? 9.765 35.535 23.334 1.00 62.95 ? 288 ASP B CA 1 ATOM 9393 C C . ASP B 2 288 ? 9.408 34.410 24.304 1.00 62.14 ? 288 ASP B C 1 ATOM 9394 O O . ASP B 2 288 ? 9.326 33.245 23.919 1.00 70.53 ? 288 ASP B O 1 ATOM 9395 C CB . ASP B 2 288 ? 8.507 36.342 22.993 1.00 62.00 ? 288 ASP B CB 1 ATOM 9396 C CG . ASP B 2 288 ? 8.040 37.231 24.139 1.00 68.32 ? 288 ASP B CG 1 ATOM 9397 O OD1 . ASP B 2 288 ? 8.481 37.031 25.291 1.00 61.10 ? 288 ASP B OD1 1 ATOM 9398 O OD2 . ASP B 2 288 ? 7.217 38.134 23.885 1.00 60.62 ? 288 ASP B OD2 1 ATOM 9399 N N . TYR B 2 289 ? 9.215 34.772 25.570 1.00 61.09 ? 289 TYR B N 1 ATOM 9400 C CA . TYR B 2 289 ? 8.702 33.847 26.575 1.00 60.35 ? 289 TYR B CA 1 ATOM 9401 C C . TYR B 2 289 ? 7.323 33.338 26.166 1.00 70.50 ? 289 TYR B C 1 ATOM 9402 O O . TYR B 2 289 ? 6.549 34.073 25.553 1.00 59.23 ? 289 TYR B O 1 ATOM 9403 C CB . TYR B 2 289 ? 8.629 34.524 27.945 1.00 59.70 ? 289 TYR B CB 1 ATOM 9404 C CG . TYR B 2 289 ? 9.927 35.156 28.393 1.00 65.55 ? 289 TYR B CG 1 ATOM 9405 C CD1 . TYR B 2 289 ? 10.883 34.417 29.074 1.00 74.05 ? 289 TYR B CD1 1 ATOM 9406 C CD2 . TYR B 2 289 ? 10.194 36.493 28.138 1.00 78.33 ? 289 TYR B CD2 1 ATOM 9407 C CE1 . TYR B 2 289 ? 12.069 34.992 29.487 1.00 71.64 ? 289 TYR B CE1 1 ATOM 9408 C CE2 . TYR B 2 289 ? 11.377 37.076 28.547 1.00 74.95 ? 289 TYR B CE2 1 ATOM 9409 C CZ . TYR B 2 289 ? 12.310 36.322 29.222 1.00 68.47 ? 289 TYR B CZ 1 ATOM 9410 O OH . TYR B 2 289 ? 13.491 36.903 29.630 1.00 73.74 ? 289 TYR B OH 1 ATOM 9411 N N . PRO B 2 290 ? 7.015 32.073 26.494 1.00 75.46 ? 290 PRO B N 1 ATOM 9412 C CA . PRO B 2 290 ? 5.729 31.461 26.141 1.00 58.95 ? 290 PRO B CA 1 ATOM 9413 C C . PRO B 2 290 ? 4.583 31.925 27.036 1.00 58.27 ? 290 PRO B C 1 ATOM 9414 O O . PRO B 2 290 ? 4.789 32.152 28.228 1.00 70.55 ? 290 PRO B O 1 ATOM 9415 C CB . PRO B 2 290 ? 5.997 29.974 26.343 1.00 59.49 ? 290 PRO B CB 1 ATOM 9416 C CG . PRO B 2 290 ? 6.980 29.943 27.456 1.00 63.98 ? 290 PRO B CG 1 ATOM 9417 C CD . PRO B 2 290 ? 7.865 31.147 27.263 1.00 60.16 ? 290 PRO B CD 1 ATOM 9418 N N . SER B 2 291 ? 3.388 32.051 26.469 1.00 58.01 ? 291 SER B N 1 ATOM 9419 C CA . SER B 2 291 ? 2.212 32.420 27.251 1.00 71.20 ? 291 SER B CA 1 ATOM 9420 C C . SER B 2 291 ? 1.735 31.247 28.103 1.00 81.22 ? 291 SER B C 1 ATOM 9421 O O . SER B 2 291 ? 2.063 30.093 27.817 1.00 60.05 ? 291 SER B O 1 ATOM 9422 C CB . SER B 2 291 ? 1.083 32.897 26.335 1.00 61.54 ? 291 SER B CB 1 ATOM 9423 O OG . SER B 2 291 ? 0.678 31.869 25.448 1.00 70.89 ? 291 SER B OG 1 ATOM 9424 N N . LEU B 2 292 ? 0.968 31.548 29.149 1.00 85.35 ? 292 LEU B N 1 ATOM 9425 C CA . LEU B 2 292 ? 0.377 30.513 29.996 1.00 76.40 ? 292 LEU B CA 1 ATOM 9426 C C . LEU B 2 292 ? -0.441 29.526 29.167 1.00 67.55 ? 292 LEU B C 1 ATOM 9427 O O . LEU B 2 292 ? -0.452 28.329 29.444 1.00 64.26 ? 292 LEU B O 1 ATOM 9428 C CB . LEU B 2 292 ? -0.508 31.131 31.082 1.00 65.82 ? 292 LEU B CB 1 ATOM 9429 C CG . LEU B 2 292 ? 0.131 31.961 32.198 1.00 72.55 ? 292 LEU B CG 1 ATOM 9430 C CD1 . LEU B 2 292 ? -0.938 32.413 33.174 1.00 75.85 ? 292 LEU B CD1 1 ATOM 9431 C CD2 . LEU B 2 292 ? 1.207 31.186 32.932 1.00 58.85 ? 292 LEU B CD2 1 ATOM 9432 N N . GLY B 2 293 ? -1.123 30.040 28.149 1.00 79.55 ? 293 GLY B N 1 ATOM 9433 C CA . GLY B 2 293 ? -1.912 29.208 27.261 1.00 85.98 ? 293 GLY B CA 1 ATOM 9434 C C . GLY B 2 293 ? -1.082 28.186 26.508 1.00 83.82 ? 293 GLY B C 1 ATOM 9435 O O . GLY B 2 293 ? -1.383 26.991 26.540 1.00 75.81 ? 293 GLY B O 1 ATOM 9436 N N . LEU B 2 294 ? -0.036 28.654 25.830 1.00 87.95 ? 294 LEU B N 1 ATOM 9437 C CA . LEU B 2 294 ? 0.813 27.769 25.041 1.00 73.30 ? 294 LEU B CA 1 ATOM 9438 C C . LEU B 2 294 ? 1.498 26.743 25.927 1.00 68.52 ? 294 LEU B C 1 ATOM 9439 O O . LEU B 2 294 ? 1.651 25.586 25.540 1.00 77.29 ? 294 LEU B O 1 ATOM 9440 C CB . LEU B 2 294 ? 1.863 28.559 24.264 1.00 60.66 ? 294 LEU B CB 1 ATOM 9441 C CG . LEU B 2 294 ? 2.655 27.701 23.275 1.00 68.77 ? 294 LEU B CG 1 ATOM 9442 C CD1 . LEU B 2 294 ? 1.752 27.242 22.142 1.00 82.17 ? 294 LEU B CD1 1 ATOM 9443 C CD2 . LEU B 2 294 ? 3.879 28.431 22.733 1.00 81.99 ? 294 LEU B CD2 1 ATOM 9444 N N . MET B 2 295 ? 1.909 27.173 27.115 1.00 62.52 ? 295 MET B N 1 ATOM 9445 C CA . MET B 2 295 ? 2.510 26.262 28.080 1.00 65.26 ? 295 MET B CA 1 ATOM 9446 C C . MET B 2 295 ? 1.517 25.183 28.485 1.00 86.22 ? 295 MET B C 1 ATOM 9447 O O . MET B 2 295 ? 1.851 24.001 28.494 1.00 94.81 ? 295 MET B O 1 ATOM 9448 C CB . MET B 2 295 ? 3.002 27.018 29.316 1.00 69.01 ? 295 MET B CB 1 ATOM 9449 C CG . MET B 2 295 ? 4.270 27.819 29.080 1.00 95.65 ? 295 MET B CG 1 ATOM 9450 S SD . MET B 2 295 ? 5.007 28.420 30.610 1.00 91.41 ? 295 MET B SD 1 ATOM 9451 C CE . MET B 2 295 ? 3.733 29.532 31.172 1.00 84.73 ? 295 MET B CE 1 ATOM 9452 N N . THR B 2 296 ? 0.295 25.599 28.805 1.00 73.66 ? 296 THR B N 1 ATOM 9453 C CA . THR B 2 296 ? -0.764 24.674 29.198 1.00 66.73 ? 296 THR B CA 1 ATOM 9454 C C . THR B 2 296 ? -1.006 23.604 28.134 1.00 75.81 ? 296 THR B C 1 ATOM 9455 O O . THR B 2 296 ? -1.076 22.411 28.442 1.00 77.90 ? 296 THR B O 1 ATOM 9456 C CB . THR B 2 296 ? -2.084 25.426 29.477 1.00 61.18 ? 296 THR B CB 1 ATOM 9457 O OG1 . THR B 2 296 ? -2.001 26.081 30.750 1.00 60.80 ? 296 THR B OG1 1 ATOM 9458 C CG2 . THR B 2 296 ? -3.266 24.465 29.486 1.00 68.37 ? 296 THR B CG2 1 ATOM 9459 N N . GLU B 2 297 ? -1.115 24.037 26.883 1.00 68.34 ? 297 GLU B N 1 ATOM 9460 C CA . GLU B 2 297 ? -1.392 23.129 25.776 1.00 69.94 ? 297 GLU B CA 1 ATOM 9461 C C . GLU B 2 297 ? -0.316 22.059 25.614 1.00 81.38 ? 297 GLU B C 1 ATOM 9462 O O . GLU B 2 297 ? -0.622 20.869 25.559 1.00 104.28 ? 297 GLU B O 1 ATOM 9463 C CB . GLU B 2 297 ? -1.543 23.917 24.473 1.00 62.79 ? 297 GLU B CB 1 ATOM 9464 C CG . GLU B 2 297 ? -1.490 23.062 23.221 1.00 68.54 ? 297 GLU B CG 1 ATOM 9465 C CD . GLU B 2 297 ? -1.793 23.853 21.966 1.00 98.93 ? 297 GLU B CD 1 ATOM 9466 O OE1 . GLU B 2 297 ? -0.981 23.803 21.018 1.00 109.65 ? 297 GLU B OE1 1 ATOM 9467 O OE2 . GLU B 2 297 ? -2.848 24.521 21.928 1.00 105.11 ? 297 GLU B OE2 1 ATOM 9468 N N . LYS B 2 298 ? 0.942 22.482 25.544 1.00 84.32 ? 298 LYS B N 1 ATOM 9469 C CA . LYS B 2 298 ? 2.041 21.549 25.328 1.00 68.99 ? 298 LYS B CA 1 ATOM 9470 C C . LYS B 2 298 ? 2.323 20.720 26.577 1.00 75.85 ? 298 LYS B C 1 ATOM 9471 O O . LYS B 2 298 ? 2.829 19.603 26.486 1.00 69.56 ? 298 LYS B O 1 ATOM 9472 C CB . LYS B 2 298 ? 3.305 22.293 24.890 1.00 62.33 ? 298 LYS B CB 1 ATOM 9473 C CG . LYS B 2 298 ? 3.204 22.921 23.509 1.00 64.08 ? 298 LYS B CG 1 ATOM 9474 C CD . LYS B 2 298 ? 2.515 21.982 22.528 1.00 80.32 ? 298 LYS B CD 1 ATOM 9475 C CE . LYS B 2 298 ? 2.536 22.535 21.112 1.00 94.51 ? 298 LYS B CE 1 ATOM 9476 N NZ . LYS B 2 298 ? 3.902 22.488 20.521 1.00 105.17 ? 298 LYS B NZ 1 ATOM 9477 N N . LEU B 2 299 ? 1.995 21.267 27.741 1.00 67.91 ? 299 LEU B N 1 ATOM 9478 C CA . LEU B 2 299 ? 2.167 20.532 28.987 1.00 77.18 ? 299 LEU B CA 1 ATOM 9479 C C . LEU B 2 299 ? 1.161 19.388 29.040 1.00 83.09 ? 299 LEU B C 1 ATOM 9480 O O . LEU B 2 299 ? 1.458 18.301 29.538 1.00 106.81 ? 299 LEU B O 1 ATOM 9481 C CB . LEU B 2 299 ? 1.998 21.462 30.191 1.00 90.57 ? 299 LEU B CB 1 ATOM 9482 C CG . LEU B 2 299 ? 2.966 21.300 31.366 1.00 86.21 ? 299 LEU B CG 1 ATOM 9483 C CD1 . LEU B 2 299 ? 4.397 21.163 30.880 1.00 69.79 ? 299 LEU B CD1 1 ATOM 9484 C CD2 . LEU B 2 299 ? 2.840 22.486 32.305 1.00 65.83 ? 299 LEU B CD2 1 ATOM 9485 N N . SER B 2 300 ? -0.029 19.644 28.506 1.00 80.15 ? 300 SER B N 1 ATOM 9486 C CA . SER B 2 300 ? -1.086 18.643 28.439 1.00 63.26 ? 300 SER B CA 1 ATOM 9487 C C . SER B 2 300 ? -0.794 17.571 27.391 1.00 62.59 ? 300 SER B C 1 ATOM 9488 O O . SER B 2 300 ? -0.960 16.379 27.650 1.00 94.42 ? 300 SER B O 1 ATOM 9489 C CB . SER B 2 300 ? -2.427 19.313 28.138 1.00 82.91 ? 300 SER B CB 1 ATOM 9490 O OG . SER B 2 300 ? -3.447 18.351 27.938 1.00 111.16 ? 300 SER B OG 1 ATOM 9491 N N . GLN B 2 301 ? -0.359 18.001 26.211 1.00 62.80 ? 301 GLN B N 1 ATOM 9492 C CA . GLN B 2 301 ? -0.103 17.087 25.101 1.00 70.85 ? 301 GLN B CA 1 ATOM 9493 C C . GLN B 2 301 ? 0.984 16.056 25.402 1.00 78.80 ? 301 GLN B C 1 ATOM 9494 O O . GLN B 2 301 ? 0.876 14.899 24.994 1.00 105.75 ? 301 GLN B O 1 ATOM 9495 C CB . GLN B 2 301 ? 0.276 17.872 23.843 1.00 85.76 ? 301 GLN B CB 1 ATOM 9496 C CG . GLN B 2 301 ? -0.868 18.668 23.235 1.00 101.12 ? 301 GLN B CG 1 ATOM 9497 C CD . GLN B 2 301 ? -0.483 19.335 21.929 1.00 118.33 ? 301 GLN B CD 1 ATOM 9498 O OE1 . GLN B 2 301 ? 0.583 19.068 21.372 1.00 123.70 ? 301 GLN B OE1 1 ATOM 9499 N NE2 . GLN B 2 301 ? -1.351 20.209 21.433 1.00 113.15 ? 301 GLN B NE2 1 ATOM 9500 N N . LYS B 2 302 ? 2.030 16.474 26.108 1.00 77.35 ? 302 LYS B N 1 ATOM 9501 C CA . LYS B 2 302 ? 3.153 15.583 26.396 1.00 74.65 ? 302 LYS B CA 1 ATOM 9502 C C . LYS B 2 302 ? 2.998 14.893 27.749 1.00 84.89 ? 302 LYS B C 1 ATOM 9503 O O . LYS B 2 302 ? 3.895 14.168 28.184 1.00 68.46 ? 302 LYS B O 1 ATOM 9504 C CB . LYS B 2 302 ? 4.473 16.351 26.348 1.00 67.41 ? 302 LYS B CB 1 ATOM 9505 C CG . LYS B 2 302 ? 4.588 17.301 25.169 1.00 71.86 ? 302 LYS B CG 1 ATOM 9506 C CD . LYS B 2 302 ? 4.672 16.568 23.841 1.00 72.05 ? 302 LYS B CD 1 ATOM 9507 C CE . LYS B 2 302 ? 6.117 16.341 23.440 1.00 77.70 ? 302 LYS B CE 1 ATOM 9508 N NZ . LYS B 2 302 ? 6.250 15.947 22.011 1.00 96.78 ? 302 LYS B NZ 1 ATOM 9509 N N . ASN B 2 303 ? 1.862 15.127 28.404 1.00 87.51 ? 303 ASN B N 1 ATOM 9510 C CA . ASN B 2 303 ? 1.548 14.507 29.693 1.00 85.04 ? 303 ASN B CA 1 ATOM 9511 C C . ASN B 2 303 ? 2.597 14.792 30.757 1.00 86.35 ? 303 ASN B C 1 ATOM 9512 O O . ASN B 2 303 ? 3.114 13.871 31.389 1.00 79.23 ? 303 ASN B O 1 ATOM 9513 C CB . ASN B 2 303 ? 1.384 12.989 29.545 1.00 91.03 ? 303 ASN B CB 1 ATOM 9514 C CG . ASN B 2 303 ? 0.211 12.609 28.669 1.00 87.63 ? 303 ASN B CG 1 ATOM 9515 O OD1 . ASN B 2 303 ? -0.939 12.635 29.106 1.00 83.42 ? 303 ASN B OD1 1 ATOM 9516 N ND2 . ASN B 2 303 ? 0.497 12.241 27.424 1.00 83.75 ? 303 ASN B ND2 1 ATOM 9517 N N . ILE B 2 304 ? 2.912 16.066 30.950 1.00 85.76 ? 304 ILE B N 1 ATOM 9518 C CA . ILE B 2 304 ? 3.903 16.458 31.943 1.00 81.34 ? 304 ILE B CA 1 ATOM 9519 C C . ILE B 2 304 ? 3.236 17.097 33.152 1.00 77.87 ? 304 ILE B C 1 ATOM 9520 O O . ILE B 2 304 ? 2.432 18.017 33.007 1.00 101.51 ? 304 ILE B O 1 ATOM 9521 C CB . ILE B 2 304 ? 4.927 17.448 31.356 1.00 89.00 ? 304 ILE B CB 1 ATOM 9522 C CG1 . ILE B 2 304 ? 5.533 16.894 30.064 1.00 72.84 ? 304 ILE B CG1 1 ATOM 9523 C CG2 . ILE B 2 304 ? 6.010 17.767 32.380 1.00 94.43 ? 304 ILE B CG2 1 ATOM 9524 C CD1 . ILE B 2 304 ? 6.369 15.651 30.260 1.00 73.34 ? 304 ILE B CD1 1 ATOM 9525 N N . ASN B 2 305 ? 3.567 16.611 34.344 1.00 68.43 ? 305 ASN B N 1 ATOM 9526 C CA . ASN B 2 305 ? 3.078 17.231 35.570 1.00 71.70 ? 305 ASN B CA 1 ATOM 9527 C C . ASN B 2 305 ? 4.082 18.252 36.082 1.00 96.96 ? 305 ASN B C 1 ATOM 9528 O O . ASN B 2 305 ? 5.178 17.895 36.511 1.00 108.48 ? 305 ASN B O 1 ATOM 9529 C CB . ASN B 2 305 ? 2.803 16.181 36.647 1.00 83.23 ? 305 ASN B CB 1 ATOM 9530 C CG . ASN B 2 305 ? 1.703 15.217 36.254 1.00 95.41 ? 305 ASN B CG 1 ATOM 9531 O OD1 . ASN B 2 305 ? 0.519 15.531 36.376 1.00 91.56 ? 305 ASN B OD1 1 ATOM 9532 N ND2 . ASN B 2 305 ? 2.087 14.033 35.788 1.00 97.88 ? 305 ASN B ND2 1 ATOM 9533 N N . LEU B 2 306 ? 3.702 19.524 36.035 1.00 89.98 ? 306 LEU B N 1 ATOM 9534 C CA . LEU B 2 306 ? 4.597 20.601 36.432 1.00 67.29 ? 306 LEU B CA 1 ATOM 9535 C C . LEU B 2 306 ? 4.462 20.933 37.910 1.00 68.40 ? 306 LEU B C 1 ATOM 9536 O O . LEU B 2 306 ? 3.371 21.237 38.393 1.00 84.65 ? 306 LEU B O 1 ATOM 9537 C CB . LEU B 2 306 ? 4.330 21.851 35.596 1.00 79.96 ? 306 LEU B CB 1 ATOM 9538 C CG . LEU B 2 306 ? 5.118 23.097 36.003 1.00 73.25 ? 306 LEU B CG 1 ATOM 9539 C CD1 . LEU B 2 306 ? 6.613 22.850 35.886 1.00 78.23 ? 306 LEU B CD1 1 ATOM 9540 C CD2 . LEU B 2 306 ? 4.699 24.290 35.163 1.00 63.39 ? 306 LEU B CD2 1 ATOM 9541 N N . ILE B 2 307 ? 5.580 20.878 38.623 1.00 69.83 ? 307 ILE B N 1 ATOM 9542 C CA . ILE B 2 307 ? 5.601 21.220 40.038 1.00 87.03 ? 307 ILE B CA 1 ATOM 9543 C C . ILE B 2 307 ? 6.358 22.526 40.255 1.00 88.12 ? 307 ILE B C 1 ATOM 9544 O O . ILE B 2 307 ? 7.453 22.714 39.724 1.00 75.04 ? 307 ILE B O 1 ATOM 9545 C CB . ILE B 2 307 ? 6.249 20.108 40.889 1.00 74.15 ? 307 ILE B CB 1 ATOM 9546 C CG1 . ILE B 2 307 ? 5.541 18.773 40.665 1.00 83.56 ? 307 ILE B CG1 1 ATOM 9547 C CG2 . ILE B 2 307 ? 6.210 20.469 42.357 1.00 84.38 ? 307 ILE B CG2 1 ATOM 9548 C CD1 . ILE B 2 307 ? 6.217 17.887 39.644 1.00 114.47 ? 307 ILE B CD1 1 ATOM 9549 N N . PHE B 2 308 ? 5.769 23.425 41.036 1.00 78.80 ? 308 PHE B N 1 ATOM 9550 C CA . PHE B 2 308 ? 6.423 24.680 41.375 1.00 71.17 ? 308 PHE B CA 1 ATOM 9551 C C . PHE B 2 308 ? 7.026 24.621 42.774 1.00 90.63 ? 308 PHE B C 1 ATOM 9552 O O . PHE B 2 308 ? 6.305 24.622 43.773 1.00 91.02 ? 308 PHE B O 1 ATOM 9553 C CB . PHE B 2 308 ? 5.433 25.841 41.292 1.00 69.99 ? 308 PHE B CB 1 ATOM 9554 C CG . PHE B 2 308 ? 5.157 26.309 39.893 1.00 92.00 ? 308 PHE B CG 1 ATOM 9555 C CD1 . PHE B 2 308 ? 6.146 26.274 38.927 1.00 104.59 ? 308 PHE B CD1 1 ATOM 9556 C CD2 . PHE B 2 308 ? 3.906 26.795 39.548 1.00 86.74 ? 308 PHE B CD2 1 ATOM 9557 C CE1 . PHE B 2 308 ? 5.892 26.712 37.639 1.00 96.50 ? 308 PHE B CE1 1 ATOM 9558 C CE2 . PHE B 2 308 ? 3.646 27.232 38.263 1.00 82.94 ? 308 PHE B CE2 1 ATOM 9559 C CZ . PHE B 2 308 ? 4.639 27.191 37.308 1.00 84.23 ? 308 PHE B CZ 1 ATOM 9560 N N . ALA B 2 309 ? 8.352 24.579 42.843 1.00 84.24 ? 309 ALA B N 1 ATOM 9561 C CA . ALA B 2 309 ? 9.040 24.651 44.123 1.00 81.90 ? 309 ALA B CA 1 ATOM 9562 C C . ALA B 2 309 ? 9.587 26.057 44.297 1.00 94.72 ? 309 ALA B C 1 ATOM 9563 O O . ALA B 2 309 ? 10.540 26.451 43.627 1.00 97.43 ? 309 ALA B O 1 ATOM 9564 C CB . ALA B 2 309 ? 10.147 23.625 44.197 1.00 78.50 ? 309 ALA B CB 1 ATOM 9565 N N . VAL B 2 310 ? 8.976 26.815 45.198 1.00 88.50 ? 310 VAL B N 1 ATOM 9566 C CA . VAL B 2 310 ? 9.261 28.237 45.305 1.00 77.76 ? 310 VAL B CA 1 ATOM 9567 C C . VAL B 2 310 ? 9.287 28.703 46.756 1.00 82.69 ? 310 VAL B C 1 ATOM 9568 O O . VAL B 2 310 ? 8.680 28.086 47.630 1.00 99.61 ? 310 VAL B O 1 ATOM 9569 C CB . VAL B 2 310 ? 8.224 29.068 44.526 1.00 77.73 ? 310 VAL B CB 1 ATOM 9570 C CG1 . VAL B 2 310 ? 8.382 28.853 43.027 1.00 75.33 ? 310 VAL B CG1 1 ATOM 9571 C CG2 . VAL B 2 310 ? 6.821 28.708 44.968 1.00 84.70 ? 310 VAL B CG2 1 ATOM 9572 N N . THR B 2 311 ? 9.993 29.800 47.001 1.00 80.04 ? 311 THR B N 1 ATOM 9573 C CA . THR B 2 311 ? 10.167 30.317 48.351 1.00 89.68 ? 311 THR B CA 1 ATOM 9574 C C . THR B 2 311 ? 8.902 30.981 48.886 1.00 101.50 ? 311 THR B C 1 ATOM 9575 O O . THR B 2 311 ? 8.043 31.416 48.117 1.00 90.11 ? 311 THR B O 1 ATOM 9576 C CB . THR B 2 311 ? 11.325 31.314 48.406 1.00 101.12 ? 311 THR B CB 1 ATOM 9577 O OG1 . THR B 2 311 ? 11.193 32.257 47.335 1.00 88.25 ? 311 THR B OG1 1 ATOM 9578 C CG2 . THR B 2 311 ? 12.646 30.580 48.266 1.00 96.81 ? 311 THR B CG2 1 ATOM 9579 N N . GLU B 2 312 ? 8.810 31.063 50.211 1.00 118.82 ? 312 GLU B N 1 ATOM 9580 C CA . GLU B 2 312 ? 7.595 31.500 50.897 1.00 125.95 ? 312 GLU B CA 1 ATOM 9581 C C . GLU B 2 312 ? 7.158 32.911 50.506 1.00 118.75 ? 312 GLU B C 1 ATOM 9582 O O . GLU B 2 312 ? 5.982 33.256 50.610 1.00 126.12 ? 312 GLU B O 1 ATOM 9583 C CB . GLU B 2 312 ? 7.795 31.419 52.415 1.00 131.60 ? 312 GLU B CB 1 ATOM 9584 C CG . GLU B 2 312 ? 6.578 30.912 53.182 1.00 145.45 ? 312 GLU B CG 1 ATOM 9585 C CD . GLU B 2 312 ? 5.450 31.926 53.243 1.00 145.88 ? 312 GLU B CD 1 ATOM 9586 O OE1 . GLU B 2 312 ? 4.279 31.527 53.067 1.00 145.93 ? 312 GLU B OE1 1 ATOM 9587 O OE2 . GLU B 2 312 ? 5.735 33.120 53.472 1.00 140.01 ? 312 GLU B OE2 1 ATOM 9588 N N . ASN B 2 313 ? 8.101 33.726 50.055 1.00 116.18 ? 313 ASN B N 1 ATOM 9589 C CA . ASN B 2 313 ? 7.768 35.079 49.634 1.00 123.20 ? 313 ASN B CA 1 ATOM 9590 C C . ASN B 2 313 ? 7.007 35.080 48.313 1.00 125.31 ? 313 ASN B C 1 ATOM 9591 O O . ASN B 2 313 ? 6.003 35.774 48.161 1.00 139.08 ? 313 ASN B O 1 ATOM 9592 C CB . ASN B 2 313 ? 9.034 35.929 49.516 1.00 108.83 ? 313 ASN B CB 1 ATOM 9593 C CG . ASN B 2 313 ? 10.078 35.300 48.616 1.00 90.29 ? 313 ASN B CG 1 ATOM 9594 O OD1 . ASN B 2 313 ? 10.066 35.498 47.403 1.00 85.01 ? 313 ASN B OD1 1 ATOM 9595 N ND2 . ASN B 2 313 ? 10.989 34.536 49.208 1.00 94.26 ? 313 ASN B ND2 1 ATOM 9596 N N . VAL B 2 314 ? 7.493 34.289 47.364 1.00 107.62 ? 314 VAL B N 1 ATOM 9597 C CA . VAL B 2 314 ? 6.940 34.267 46.019 1.00 93.29 ? 314 VAL B CA 1 ATOM 9598 C C . VAL B 2 314 ? 5.942 33.115 45.827 1.00 102.08 ? 314 VAL B C 1 ATOM 9599 O O . VAL B 2 314 ? 5.410 32.916 44.733 1.00 91.17 ? 314 VAL B O 1 ATOM 9600 C CB . VAL B 2 314 ? 8.079 34.177 44.973 1.00 85.92 ? 314 VAL B CB 1 ATOM 9601 C CG1 . VAL B 2 314 ? 8.522 32.734 44.774 1.00 98.34 ? 314 VAL B CG1 1 ATOM 9602 C CG2 . VAL B 2 314 ? 7.665 34.816 43.656 1.00 85.18 ? 314 VAL B CG2 1 ATOM 9603 N N . VAL B 2 315 ? 5.680 32.365 46.895 1.00 102.53 ? 315 VAL B N 1 ATOM 9604 C CA . VAL B 2 315 ? 4.853 31.162 46.790 1.00 99.96 ? 315 VAL B CA 1 ATOM 9605 C C . VAL B 2 315 ? 3.388 31.470 46.457 1.00 99.56 ? 315 VAL B C 1 ATOM 9606 O O . VAL B 2 315 ? 2.747 30.715 45.726 1.00 102.88 ? 315 VAL B O 1 ATOM 9607 C CB . VAL B 2 315 ? 4.922 30.310 48.089 1.00 101.46 ? 315 VAL B CB 1 ATOM 9608 C CG1 . VAL B 2 315 ? 4.239 31.011 49.251 1.00 117.31 ? 315 VAL B CG1 1 ATOM 9609 C CG2 . VAL B 2 315 ? 4.309 28.935 47.862 1.00 103.53 ? 315 VAL B CG2 1 ATOM 9610 N N . ASN B 2 316 ? 2.865 32.580 46.971 1.00 97.64 ? 316 ASN B N 1 ATOM 9611 C CA . ASN B 2 316 ? 1.489 32.971 46.683 1.00 90.00 ? 316 ASN B CA 1 ATOM 9612 C C . ASN B 2 316 ? 1.305 33.332 45.215 1.00 90.19 ? 316 ASN B C 1 ATOM 9613 O O . ASN B 2 316 ? 0.229 33.149 44.645 1.00 86.08 ? 316 ASN B O 1 ATOM 9614 C CB . ASN B 2 316 ? 1.070 34.146 47.564 1.00 91.57 ? 316 ASN B CB 1 ATOM 9615 C CG . ASN B 2 316 ? 0.675 33.715 48.955 1.00 110.47 ? 316 ASN B CG 1 ATOM 9616 O OD1 . ASN B 2 316 ? 0.942 32.587 49.366 1.00 136.15 ? 316 ASN B OD1 1 ATOM 9617 N ND2 . ASN B 2 316 ? 0.032 34.612 49.691 1.00 116.97 ? 316 ASN B ND2 1 ATOM 9618 N N . LEU B 2 317 ? 2.368 33.848 44.611 1.00 81.80 ? 317 LEU B N 1 ATOM 9619 C CA . LEU B 2 317 ? 2.344 34.228 43.208 1.00 75.18 ? 317 LEU B CA 1 ATOM 9620 C C . LEU B 2 317 ? 2.189 33.007 42.311 1.00 77.79 ? 317 LEU B C 1 ATOM 9621 O O . LEU B 2 317 ? 1.314 32.968 41.446 1.00 95.45 ? 317 LEU B O 1 ATOM 9622 C CB . LEU B 2 317 ? 3.618 34.993 42.844 1.00 83.73 ? 317 LEU B CB 1 ATOM 9623 C CG . LEU B 2 317 ? 3.866 35.229 41.354 1.00 74.68 ? 317 LEU B CG 1 ATOM 9624 C CD1 . LEU B 2 317 ? 2.807 36.151 40.766 1.00 88.11 ? 317 LEU B CD1 1 ATOM 9625 C CD2 . LEU B 2 317 ? 5.260 35.783 41.132 1.00 67.98 ? 317 LEU B CD2 1 ATOM 9626 N N . TYR B 2 318 ? 3.037 32.007 42.525 1.00 80.11 ? 318 TYR B N 1 ATOM 9627 C CA . TYR B 2 318 ? 3.023 30.813 41.688 1.00 83.29 ? 318 TYR B CA 1 ATOM 9628 C C . TYR B 2 318 ? 1.784 29.958 41.937 1.00 90.06 ? 318 TYR B C 1 ATOM 9629 O O . TYR B 2 318 ? 1.364 29.204 41.059 1.00 71.23 ? 318 TYR B O 1 ATOM 9630 C CB . TYR B 2 318 ? 4.294 29.994 41.910 1.00 72.29 ? 318 TYR B CB 1 ATOM 9631 C CG . TYR B 2 318 ? 5.513 30.627 41.282 1.00 84.00 ? 318 TYR B CG 1 ATOM 9632 C CD1 . TYR B 2 318 ? 5.844 30.370 39.958 1.00 88.22 ? 318 TYR B CD1 1 ATOM 9633 C CD2 . TYR B 2 318 ? 6.324 31.493 42.005 1.00 79.43 ? 318 TYR B CD2 1 ATOM 9634 C CE1 . TYR B 2 318 ? 6.956 30.949 39.372 1.00 81.39 ? 318 TYR B CE1 1 ATOM 9635 C CE2 . TYR B 2 318 ? 7.438 32.075 41.428 1.00 72.75 ? 318 TYR B CE2 1 ATOM 9636 C CZ . TYR B 2 318 ? 7.748 31.800 40.112 1.00 85.48 ? 318 TYR B CZ 1 ATOM 9637 O OH . TYR B 2 318 ? 8.854 32.377 39.530 1.00 109.40 ? 318 TYR B OH 1 ATOM 9638 N N . GLN B 2 319 ? 1.203 30.077 43.129 1.00 80.35 ? 319 GLN B N 1 ATOM 9639 C CA . GLN B 2 319 ? -0.098 29.476 43.396 1.00 77.20 ? 319 GLN B CA 1 ATOM 9640 C C . GLN B 2 319 ? -1.088 29.959 42.350 1.00 83.29 ? 319 GLN B C 1 ATOM 9641 O O . GLN B 2 319 ? -1.792 29.171 41.722 1.00 88.62 ? 319 GLN B O 1 ATOM 9642 C CB . GLN B 2 319 ? -0.606 29.835 44.795 1.00 83.60 ? 319 GLN B CB 1 ATOM 9643 C CG . GLN B 2 319 ? -0.028 28.997 45.916 1.00 105.10 ? 319 GLN B CG 1 ATOM 9644 C CD . GLN B 2 319 ? -0.670 29.290 47.257 1.00 123.21 ? 319 GLN B CD 1 ATOM 9645 O OE1 . GLN B 2 319 ? -1.344 30.307 47.427 1.00 131.29 ? 319 GLN B OE1 1 ATOM 9646 N NE2 . GLN B 2 319 ? -0.467 28.395 48.218 1.00 125.93 ? 319 GLN B NE2 1 ATOM 9647 N N . ASN B 2 320 ? -1.112 31.271 42.157 1.00 92.24 ? 320 ASN B N 1 ATOM 9648 C CA . ASN B 2 320 ? -2.066 31.892 41.258 1.00 85.21 ? 320 ASN B CA 1 ATOM 9649 C C . ASN B 2 320 ? -1.745 31.640 39.794 1.00 81.05 ? 320 ASN B C 1 ATOM 9650 O O . ASN B 2 320 ? -2.644 31.602 38.955 1.00 77.94 ? 320 ASN B O 1 ATOM 9651 C CB . ASN B 2 320 ? -2.141 33.387 41.549 1.00 83.71 ? 320 ASN B CB 1 ATOM 9652 C CG . ASN B 2 320 ? -2.883 33.675 42.833 1.00 109.83 ? 320 ASN B CG 1 ATOM 9653 O OD1 . ASN B 2 320 ? -3.675 32.850 43.288 1.00 141.87 ? 320 ASN B OD1 1 ATOM 9654 N ND2 . ASN B 2 320 ? -2.639 34.831 43.429 1.00 121.73 ? 320 ASN B ND2 1 ATOM 9655 N N . TYR B 2 321 ? -0.466 31.459 39.487 1.00 84.04 ? 321 TYR B N 1 ATOM 9656 C CA . TYR B 2 321 ? -0.080 31.050 38.144 1.00 86.81 ? 321 TYR B CA 1 ATOM 9657 C C . TYR B 2 321 ? -0.561 29.625 37.910 1.00 84.46 ? 321 TYR B C 1 ATOM 9658 O O . TYR B 2 321 ? -1.034 29.288 36.824 1.00 82.48 ? 321 TYR B O 1 ATOM 9659 C CB . TYR B 2 321 ? 1.434 31.150 37.944 1.00 79.34 ? 321 TYR B CB 1 ATOM 9660 C CG . TYR B 2 321 ? 1.938 32.558 37.715 1.00 81.43 ? 321 TYR B CG 1 ATOM 9661 C CD1 . TYR B 2 321 ? 1.134 33.516 37.116 1.00 74.30 ? 321 TYR B CD1 1 ATOM 9662 C CD2 . TYR B 2 321 ? 3.219 32.927 38.101 1.00 99.44 ? 321 TYR B CD2 1 ATOM 9663 C CE1 . TYR B 2 321 ? 1.592 34.804 36.905 1.00 85.68 ? 321 TYR B CE1 1 ATOM 9664 C CE2 . TYR B 2 321 ? 3.687 34.211 37.895 1.00 79.82 ? 321 TYR B CE2 1 ATOM 9665 C CZ . TYR B 2 321 ? 2.870 35.146 37.297 1.00 90.67 ? 321 TYR B CZ 1 ATOM 9666 O OH . TYR B 2 321 ? 3.336 36.426 37.092 1.00 86.94 ? 321 TYR B OH 1 ATOM 9667 N N . SER B 2 322 ? -0.454 28.797 38.945 1.00 83.85 ? 322 SER B N 1 ATOM 9668 C CA . SER B 2 322 ? -0.861 27.401 38.851 1.00 86.17 ? 322 SER B CA 1 ATOM 9669 C C . SER B 2 322 ? -2.374 27.280 38.718 1.00 93.51 ? 322 SER B C 1 ATOM 9670 O O . SER B 2 322 ? -2.874 26.356 38.079 1.00 83.29 ? 322 SER B O 1 ATOM 9671 C CB . SER B 2 322 ? -0.377 26.612 40.068 1.00 80.14 ? 322 SER B CB 1 ATOM 9672 O OG . SER B 2 322 ? -1.022 27.057 41.246 1.00 110.62 ? 322 SER B OG 1 ATOM 9673 N N . GLU B 2 323 ? -3.101 28.217 39.319 1.00 85.96 ? 323 GLU B N 1 ATOM 9674 C CA . GLU B 2 323 ? -4.557 28.227 39.222 1.00 74.58 ? 323 GLU B CA 1 ATOM 9675 C C . GLU B 2 323 ? -5.011 28.481 37.787 1.00 79.97 ? 323 GLU B C 1 ATOM 9676 O O . GLU B 2 323 ? -6.150 28.187 37.427 1.00 89.34 ? 323 GLU B O 1 ATOM 9677 C CB . GLU B 2 323 ? -5.156 29.278 40.158 1.00 83.30 ? 323 GLU B CB 1 ATOM 9678 C CG . GLU B 2 323 ? -4.981 28.971 41.637 1.00 115.33 ? 323 GLU B CG 1 ATOM 9679 C CD . GLU B 2 323 ? -5.564 30.050 42.531 1.00 147.41 ? 323 GLU B CD 1 ATOM 9680 O OE1 . GLU B 2 323 ? -6.391 30.849 42.041 1.00 156.50 ? 323 GLU B OE1 1 ATOM 9681 O OE2 . GLU B 2 323 ? -5.193 30.102 43.724 1.00 155.97 ? 323 GLU B OE2 1 ATOM 9682 N N . LEU B 2 324 ? -4.117 29.039 36.975 1.00 98.30 ? 324 LEU B N 1 ATOM 9683 C CA . LEU B 2 324 ? -4.399 29.256 35.561 1.00 83.90 ? 324 LEU B CA 1 ATOM 9684 C C . LEU B 2 324 ? -3.856 28.110 34.713 1.00 87.64 ? 324 LEU B C 1 ATOM 9685 O O . LEU B 2 324 ? -4.072 28.063 33.502 1.00 105.99 ? 324 LEU B O 1 ATOM 9686 C CB . LEU B 2 324 ? -3.807 30.588 35.098 1.00 61.22 ? 324 LEU B CB 1 ATOM 9687 C CG . LEU B 2 324 ? -4.424 31.813 35.775 1.00 65.00 ? 324 LEU B CG 1 ATOM 9688 C CD1 . LEU B 2 324 ? -3.789 33.105 35.285 1.00 75.97 ? 324 LEU B CD1 1 ATOM 9689 C CD2 . LEU B 2 324 ? -5.928 31.837 35.550 1.00 72.83 ? 324 LEU B CD2 1 ATOM 9690 N N . ILE B 2 325 ? -3.157 27.183 35.360 1.00 72.51 ? 325 ILE B N 1 ATOM 9691 C CA . ILE B 2 325 ? -2.631 26.005 34.681 1.00 81.44 ? 325 ILE B CA 1 ATOM 9692 C C . ILE B 2 325 ? -2.999 24.752 35.465 1.00 102.92 ? 325 ILE B C 1 ATOM 9693 O O . ILE B 2 325 ? -2.213 24.277 36.287 1.00 120.18 ? 325 ILE B O 1 ATOM 9694 C CB . ILE B 2 325 ? -1.101 26.067 34.514 1.00 74.23 ? 325 ILE B CB 1 ATOM 9695 C CG1 . ILE B 2 325 ? -0.669 27.425 33.959 1.00 76.76 ? 325 ILE B CG1 1 ATOM 9696 C CG2 . ILE B 2 325 ? -0.620 24.947 33.607 1.00 69.52 ? 325 ILE B CG2 1 ATOM 9697 C CD1 . ILE B 2 325 ? 0.831 27.590 33.867 1.00 72.73 ? 325 ILE B CD1 1 ATOM 9698 N N . PRO B 2 326 ? -4.205 24.217 35.218 1.00 91.71 ? 326 PRO B N 1 ATOM 9699 C CA . PRO B 2 326 ? -4.745 23.071 35.957 1.00 83.44 ? 326 PRO B CA 1 ATOM 9700 C C . PRO B 2 326 ? -3.815 21.864 35.929 1.00 89.92 ? 326 PRO B C 1 ATOM 9701 O O . PRO B 2 326 ? -3.200 21.579 34.901 1.00 91.30 ? 326 PRO B O 1 ATOM 9702 C CB . PRO B 2 326 ? -6.054 22.769 35.222 1.00 99.60 ? 326 PRO B CB 1 ATOM 9703 C CG . PRO B 2 326 ? -6.436 24.063 34.590 1.00 89.79 ? 326 PRO B CG 1 ATOM 9704 C CD . PRO B 2 326 ? -5.143 24.698 34.189 1.00 85.95 ? 326 PRO B CD 1 ATOM 9705 N N . GLY B 2 327 ? -3.712 21.171 37.057 1.00 98.14 ? 327 GLY B N 1 ATOM 9706 C CA . GLY B 2 327 ? -2.872 19.993 37.151 1.00 116.35 ? 327 GLY B CA 1 ATOM 9707 C C . GLY B 2 327 ? -1.526 20.304 37.771 1.00 119.25 ? 327 GLY B C 1 ATOM 9708 O O . GLY B 2 327 ? -0.778 19.400 38.148 1.00 118.79 ? 327 GLY B O 1 ATOM 9709 N N . THR B 2 328 ? -1.215 21.591 37.877 1.00 96.23 ? 328 THR B N 1 ATOM 9710 C CA . THR B 2 328 ? 0.055 22.016 38.448 1.00 103.00 ? 328 THR B CA 1 ATOM 9711 C C . THR B 2 328 ? -0.088 22.330 39.928 1.00 113.12 ? 328 THR B C 1 ATOM 9712 O O . THR B 2 328 ? -0.967 23.092 40.332 1.00 126.64 ? 328 THR B O 1 ATOM 9713 C CB . THR B 2 328 ? 0.616 23.250 37.725 1.00 92.31 ? 328 THR B CB 1 ATOM 9714 O OG1 . THR B 2 328 ? -0.328 24.323 37.807 1.00 100.91 ? 328 THR B OG1 1 ATOM 9715 C CG2 . THR B 2 328 ? 0.886 22.930 36.265 1.00 85.68 ? 328 THR B CG2 1 ATOM 9716 N N . THR B 2 329 ? 0.788 21.737 40.732 1.00 97.14 ? 329 THR B N 1 ATOM 9717 C CA . THR B 2 329 ? 0.775 21.948 42.172 1.00 107.31 ? 329 THR B CA 1 ATOM 9718 C C . THR B 2 329 ? 2.011 22.719 42.616 1.00 109.23 ? 329 THR B C 1 ATOM 9719 O O . THR B 2 329 ? 3.061 22.652 41.976 1.00 112.23 ? 329 THR B O 1 ATOM 9720 C CB . THR B 2 329 ? 0.707 20.616 42.935 1.00 115.02 ? 329 THR B CB 1 ATOM 9721 O OG1 . THR B 2 329 ? 1.801 19.782 42.536 1.00 108.25 ? 329 THR B OG1 1 ATOM 9722 C CG2 . THR B 2 329 ? -0.602 19.901 42.640 1.00 129.48 ? 329 THR B CG2 1 ATOM 9723 N N . VAL B 2 330 ? 1.879 23.455 43.712 1.00 95.50 ? 330 VAL B N 1 ATOM 9724 C CA . VAL B 2 330 ? 2.985 24.239 44.241 1.00 82.57 ? 330 VAL B CA 1 ATOM 9725 C C . VAL B 2 330 ? 3.356 23.773 45.641 1.00 81.06 ? 330 VAL B C 1 ATOM 9726 O O . VAL B 2 330 ? 2.551 23.149 46.333 1.00 98.91 ? 330 VAL B O 1 ATOM 9727 C CB . VAL B 2 330 ? 2.647 25.739 44.290 1.00 79.96 ? 330 VAL B CB 1 ATOM 9728 C CG1 . VAL B 2 330 ? 2.205 26.228 42.924 1.00 79.69 ? 330 VAL B CG1 1 ATOM 9729 C CG2 . VAL B 2 330 ? 1.564 25.992 45.317 1.00 81.92 ? 330 VAL B CG2 1 ATOM 9730 N N . GLY B 2 331 ? 4.578 24.081 46.054 1.00 81.69 ? 331 GLY B N 1 ATOM 9731 C CA . GLY B 2 331 ? 5.029 23.747 47.391 1.00 82.75 ? 331 GLY B CA 1 ATOM 9732 C C . GLY B 2 331 ? 6.083 24.720 47.873 1.00 92.27 ? 331 GLY B C 1 ATOM 9733 O O . GLY B 2 331 ? 6.789 25.338 47.074 1.00 88.29 ? 331 GLY B O 1 ATOM 9734 N N . VAL B 2 332 ? 6.198 24.849 49.189 1.00 85.21 ? 332 VAL B N 1 ATOM 9735 C CA . VAL B 2 332 ? 7.110 25.819 49.769 1.00 86.57 ? 332 VAL B CA 1 ATOM 9736 C C . VAL B 2 332 ? 8.535 25.291 49.740 1.00 88.77 ? 332 VAL B C 1 ATOM 9737 O O . VAL B 2 332 ? 8.831 24.224 50.280 1.00 95.72 ? 332 VAL B O 1 ATOM 9738 C CB . VAL B 2 332 ? 6.716 26.173 51.212 1.00 104.76 ? 332 VAL B CB 1 ATOM 9739 C CG1 . VAL B 2 332 ? 7.718 27.147 51.811 1.00 119.11 ? 332 VAL B CG1 1 ATOM 9740 C CG2 . VAL B 2 332 ? 5.313 26.758 51.245 1.00 96.99 ? 332 VAL B CG2 1 ATOM 9741 N N . LEU B 2 333 ? 9.411 26.050 49.093 1.00 90.09 ? 333 LEU B N 1 ATOM 9742 C CA . LEU B 2 333 ? 10.816 25.696 48.992 1.00 90.61 ? 333 LEU B CA 1 ATOM 9743 C C . LEU B 2 333 ? 11.625 26.463 50.032 1.00 104.03 ? 333 LEU B C 1 ATOM 9744 O O . LEU B 2 333 ? 11.520 27.686 50.134 1.00 114.10 ? 333 LEU B O 1 ATOM 9745 C CB . LEU B 2 333 ? 11.342 25.992 47.585 1.00 86.60 ? 333 LEU B CB 1 ATOM 9746 C CG . LEU B 2 333 ? 12.278 24.978 46.928 1.00 91.61 ? 333 LEU B CG 1 ATOM 9747 C CD1 . LEU B 2 333 ? 12.886 25.554 45.660 1.00 95.15 ? 333 LEU B CD1 1 ATOM 9748 C CD2 . LEU B 2 333 ? 13.362 24.540 47.883 1.00 90.98 ? 333 LEU B CD2 1 ATOM 9749 N N . SER B 2 334 ? 12.428 25.741 50.805 1.00 114.88 ? 334 SER B N 1 ATOM 9750 C CA . SER B 2 334 ? 13.332 26.374 51.754 1.00 118.11 ? 334 SER B CA 1 ATOM 9751 C C . SER B 2 334 ? 14.370 27.186 50.991 1.00 113.69 ? 334 SER B C 1 ATOM 9752 O O . SER B 2 334 ? 14.629 26.923 49.818 1.00 115.77 ? 334 SER B O 1 ATOM 9753 C CB . SER B 2 334 ? 14.007 25.331 52.645 1.00 120.91 ? 334 SER B CB 1 ATOM 9754 O OG . SER B 2 334 ? 14.672 24.349 51.870 1.00 121.13 ? 334 SER B OG 1 ATOM 9755 N N . MET B 2 335 ? 14.954 28.177 51.655 1.00 111.24 ? 335 MET B N 1 ATOM 9756 C CA . MET B 2 335 ? 15.913 29.069 51.012 1.00 121.33 ? 335 MET B CA 1 ATOM 9757 C C . MET B 2 335 ? 17.135 28.317 50.485 1.00 101.64 ? 335 MET B C 1 ATOM 9758 O O . MET B 2 335 ? 17.684 28.665 49.440 1.00 97.34 ? 335 MET B O 1 ATOM 9759 C CB . MET B 2 335 ? 16.353 30.164 51.987 1.00 147.43 ? 335 MET B CB 1 ATOM 9760 C CG . MET B 2 335 ? 15.199 30.881 52.676 1.00 157.19 ? 335 MET B CG 1 ATOM 9761 S SD . MET B 2 335 ? 14.038 31.627 51.513 1.00 179.99 ? 335 MET B SD 1 ATOM 9762 C CE . MET B 2 335 ? 12.837 32.340 52.635 1.00 130.16 ? 335 MET B CE 1 ATOM 9763 N N . ASP B 2 336 ? 17.555 27.290 51.218 1.00 112.64 ? 336 ASP B N 1 ATOM 9764 C CA . ASP B 2 336 ? 18.740 26.513 50.860 1.00 114.85 ? 336 ASP B CA 1 ATOM 9765 C C . ASP B 2 336 ? 18.400 25.247 50.075 1.00 122.32 ? 336 ASP B C 1 ATOM 9766 O O . ASP B 2 336 ? 19.289 24.459 49.747 1.00 122.22 ? 336 ASP B O 1 ATOM 9767 C CB . ASP B 2 336 ? 19.533 26.149 52.121 1.00 115.52 ? 336 ASP B CB 1 ATOM 9768 C CG . ASP B 2 336 ? 18.646 25.661 53.254 1.00 127.77 ? 336 ASP B CG 1 ATOM 9769 O OD1 . ASP B 2 336 ? 17.608 25.024 52.974 1.00 139.37 ? 336 ASP B OD1 1 ATOM 9770 O OD2 . ASP B 2 336 ? 18.989 25.917 54.429 1.00 120.11 ? 336 ASP B OD2 1 ATOM 9771 N N . SER B 2 337 ? 17.113 25.063 49.790 1.00 132.64 ? 337 SER B N 1 ATOM 9772 C CA . SER B 2 337 ? 16.604 23.894 49.065 1.00 123.47 ? 337 SER B CA 1 ATOM 9773 C C . SER B 2 337 ? 16.914 22.574 49.759 1.00 122.75 ? 337 SER B C 1 ATOM 9774 O O . SER B 2 337 ? 17.245 21.581 49.112 1.00 127.11 ? 337 SER B O 1 ATOM 9775 C CB . SER B 2 337 ? 17.147 23.860 47.635 1.00 125.30 ? 337 SER B CB 1 ATOM 9776 O OG . SER B 2 337 ? 16.500 24.823 46.823 1.00 137.31 ? 337 SER B OG 1 ATOM 9777 N N . SER B 2 338 ? 16.801 22.567 51.080 1.00 113.80 ? 338 SER B N 1 ATOM 9778 C CA . SER B 2 338 ? 16.940 21.338 51.841 1.00 109.90 ? 338 SER B CA 1 ATOM 9779 C C . SER B 2 338 ? 15.610 20.597 51.867 1.00 117.20 ? 338 SER B C 1 ATOM 9780 O O . SER B 2 338 ? 15.546 19.416 52.205 1.00 144.98 ? 338 SER B O 1 ATOM 9781 C CB . SER B 2 338 ? 17.408 21.642 53.261 1.00 116.17 ? 338 SER B CB 1 ATOM 9782 O OG . SER B 2 338 ? 16.551 22.586 53.877 1.00 109.25 ? 338 SER B OG 1 ATOM 9783 N N . ASN B 2 339 ? 14.552 21.309 51.494 1.00 101.60 ? 339 ASN B N 1 ATOM 9784 C CA . ASN B 2 339 ? 13.192 20.806 51.621 1.00 105.67 ? 339 ASN B CA 1 ATOM 9785 C C . ASN B 2 339 ? 12.684 20.048 50.391 1.00 106.17 ? 339 ASN B C 1 ATOM 9786 O O . ASN B 2 339 ? 11.652 19.379 50.456 1.00 105.89 ? 339 ASN B O 1 ATOM 9787 C CB . ASN B 2 339 ? 12.252 21.976 51.937 1.00 109.92 ? 339 ASN B CB 1 ATOM 9788 C CG . ASN B 2 339 ? 10.849 21.525 52.292 1.00 137.87 ? 339 ASN B CG 1 ATOM 9789 O OD1 . ASN B 2 339 ? 9.925 21.643 51.488 1.00 151.46 ? 339 ASN B OD1 1 ATOM 9790 N ND2 . ASN B 2 339 ? 10.683 21.001 53.502 1.00 138.71 ? 339 ASN B ND2 1 ATOM 9791 N N . VAL B 2 340 ? 13.414 20.135 49.282 1.00 100.87 ? 340 VAL B N 1 ATOM 9792 C CA . VAL B 2 340 ? 12.919 19.610 48.007 1.00 94.76 ? 340 VAL B CA 1 ATOM 9793 C C . VAL B 2 340 ? 12.665 18.111 48.017 1.00 103.24 ? 340 VAL B C 1 ATOM 9794 O O . VAL B 2 340 ? 11.646 17.659 47.502 1.00 114.06 ? 340 VAL B O 1 ATOM 9795 C CB . VAL B 2 340 ? 13.884 19.916 46.842 1.00 99.71 ? 340 VAL B CB 1 ATOM 9796 C CG1 . VAL B 2 340 ? 13.612 21.300 46.278 1.00 110.31 ? 340 VAL B CG1 1 ATOM 9797 C CG2 . VAL B 2 340 ? 15.330 19.774 47.287 1.00 101.18 ? 340 VAL B CG2 1 ATOM 9798 N N . LEU B 2 341 ? 13.588 17.349 48.599 1.00 120.55 ? 341 LEU B N 1 ATOM 9799 C CA . LEU B 2 341 ? 13.487 15.893 48.601 1.00 110.50 ? 341 LEU B CA 1 ATOM 9800 C C . LEU B 2 341 ? 12.154 15.456 49.196 1.00 105.70 ? 341 LEU B C 1 ATOM 9801 O O . LEU B 2 341 ? 11.517 14.530 48.698 1.00 123.69 ? 341 LEU B O 1 ATOM 9802 C CB . LEU B 2 341 ? 14.662 15.267 49.365 1.00 145.95 ? 341 LEU B CB 1 ATOM 9803 C CG . LEU B 2 341 ? 14.780 15.450 50.882 1.00 168.51 ? 341 LEU B CG 1 ATOM 9804 C CD1 . LEU B 2 341 ? 14.247 14.225 51.618 1.00 171.27 ? 341 LEU B CD1 1 ATOM 9805 C CD2 . LEU B 2 341 ? 16.217 15.744 51.292 1.00 164.81 ? 341 LEU B CD2 1 ATOM 9806 N N . GLN B 2 342 ? 11.726 16.148 50.246 1.00 109.74 ? 342 GLN B N 1 ATOM 9807 C CA . GLN B 2 342 ? 10.437 15.878 50.861 1.00 105.23 ? 342 GLN B CA 1 ATOM 9808 C C . GLN B 2 342 ? 9.319 16.471 50.020 1.00 98.39 ? 342 GLN B C 1 ATOM 9809 O O . GLN B 2 342 ? 8.261 15.866 49.856 1.00 108.02 ? 342 GLN B O 1 ATOM 9810 C CB . GLN B 2 342 ? 10.384 16.440 52.282 1.00 110.82 ? 342 GLN B CB 1 ATOM 9811 C CG . GLN B 2 342 ? 9.089 16.126 53.008 1.00 114.91 ? 342 GLN B CG 1 ATOM 9812 C CD . GLN B 2 342 ? 8.809 14.635 53.068 1.00 130.14 ? 342 GLN B CD 1 ATOM 9813 O OE1 . GLN B 2 342 ? 9.712 13.829 53.297 1.00 131.75 ? 342 GLN B OE1 1 ATOM 9814 N NE2 . GLN B 2 342 ? 7.553 14.260 52.853 1.00 128.52 ? 342 GLN B NE2 1 ATOM 9815 N N . LEU B 2 343 ? 9.567 17.659 49.481 1.00 101.35 ? 343 LEU B N 1 ATOM 9816 C CA . LEU B 2 343 ? 8.564 18.376 48.704 1.00 100.89 ? 343 LEU B CA 1 ATOM 9817 C C . LEU B 2 343 ? 8.186 17.617 47.435 1.00 94.75 ? 343 LEU B C 1 ATOM 9818 O O . LEU B 2 343 ? 7.050 17.703 46.970 1.00 90.63 ? 343 LEU B O 1 ATOM 9819 C CB . LEU B 2 343 ? 9.068 19.777 48.355 1.00 107.08 ? 343 LEU B CB 1 ATOM 9820 C CG . LEU B 2 343 ? 8.038 20.720 47.733 1.00 113.47 ? 343 LEU B CG 1 ATOM 9821 C CD1 . LEU B 2 343 ? 6.773 20.745 48.578 1.00 132.75 ? 343 LEU B CD1 1 ATOM 9822 C CD2 . LEU B 2 343 ? 8.615 22.119 47.584 1.00 102.26 ? 343 LEU B CD2 1 ATOM 9823 N N . ILE B 2 344 ? 9.141 16.875 46.880 1.00 100.24 ? 344 ILE B N 1 ATOM 9824 C CA . ILE B 2 344 ? 8.890 16.067 45.692 1.00 94.36 ? 344 ILE B CA 1 ATOM 9825 C C . ILE B 2 344 ? 7.920 14.936 46.004 1.00 99.35 ? 344 ILE B C 1 ATOM 9826 O O . ILE B 2 344 ? 6.912 14.762 45.318 1.00 87.46 ? 344 ILE B O 1 ATOM 9827 C CB . ILE B 2 344 ? 10.188 15.463 45.123 1.00 102.10 ? 344 ILE B CB 1 ATOM 9828 C CG1 . ILE B 2 344 ? 11.120 16.562 44.623 1.00 87.29 ? 344 ILE B CG1 1 ATOM 9829 C CG2 . ILE B 2 344 ? 9.874 14.508 43.985 1.00 97.57 ? 344 ILE B CG2 1 ATOM 9830 C CD1 . ILE B 2 344 ? 10.552 17.343 43.481 1.00 87.06 ? 344 ILE B CD1 1 ATOM 9831 N N . VAL B 2 345 ? 8.236 14.171 47.045 1.00 92.57 ? 345 VAL B N 1 ATOM 9832 C CA . VAL B 2 345 ? 7.407 13.044 47.457 1.00 105.39 ? 345 VAL B CA 1 ATOM 9833 C C . VAL B 2 345 ? 5.981 13.497 47.751 1.00 103.62 ? 345 VAL B C 1 ATOM 9834 O O . VAL B 2 345 ? 5.017 12.846 47.350 1.00 117.43 ? 345 VAL B O 1 ATOM 9835 C CB . VAL B 2 345 ? 7.987 12.342 48.700 1.00 98.48 ? 345 VAL B CB 1 ATOM 9836 C CG1 . VAL B 2 345 ? 7.105 11.175 49.113 1.00 110.02 ? 345 VAL B CG1 1 ATOM 9837 C CG2 . VAL B 2 345 ? 9.408 11.871 48.429 1.00 99.81 ? 345 VAL B CG2 1 ATOM 9838 N N . ASP B 2 346 ? 5.858 14.625 48.442 1.00 93.24 ? 346 ASP B N 1 ATOM 9839 C CA . ASP B 2 346 ? 4.553 15.193 48.753 1.00 104.38 ? 346 ASP B CA 1 ATOM 9840 C C . ASP B 2 346 ? 3.796 15.552 47.479 1.00 99.32 ? 346 ASP B C 1 ATOM 9841 O O . ASP B 2 346 ? 2.589 15.332 47.379 1.00 109.22 ? 346 ASP B O 1 ATOM 9842 C CB . ASP B 2 346 ? 4.706 16.431 49.640 1.00 120.62 ? 346 ASP B CB 1 ATOM 9843 C CG . ASP B 2 346 ? 5.396 16.124 50.953 1.00 122.17 ? 346 ASP B CG 1 ATOM 9844 O OD1 . ASP B 2 346 ? 5.272 14.977 51.432 1.00 99.34 ? 346 ASP B OD1 1 ATOM 9845 O OD2 . ASP B 2 346 ? 6.063 17.027 51.504 1.00 124.36 ? 346 ASP B OD2 1 ATOM 9846 N N . ALA B 2 347 ? 4.517 16.098 46.506 1.00 86.67 ? 347 ALA B N 1 ATOM 9847 C CA . ALA B 2 347 ? 3.913 16.539 45.254 1.00 88.48 ? 347 ALA B CA 1 ATOM 9848 C C . ALA B 2 347 ? 3.358 15.367 44.455 1.00 93.58 ? 347 ALA B C 1 ATOM 9849 O O . ALA B 2 347 ? 2.253 15.443 43.916 1.00 84.31 ? 347 ALA B O 1 ATOM 9850 C CB . ALA B 2 347 ? 4.925 17.311 44.422 1.00 92.61 ? 347 ALA B CB 1 ATOM 9851 N N . TYR B 2 348 ? 4.130 14.286 44.382 1.00 103.71 ? 348 TYR B N 1 ATOM 9852 C CA . TYR B 2 348 ? 3.708 13.087 43.667 1.00 87.51 ? 348 TYR B CA 1 ATOM 9853 C C . TYR B 2 348 ? 2.427 12.541 44.281 1.00 88.54 ? 348 TYR B C 1 ATOM 9854 O O . TYR B 2 348 ? 1.567 12.012 43.577 1.00 101.48 ? 348 TYR B O 1 ATOM 9855 C CB . TYR B 2 348 ? 4.812 12.027 43.687 1.00 102.97 ? 348 TYR B CB 1 ATOM 9856 C CG . TYR B 2 348 ? 4.474 10.756 42.935 1.00 113.10 ? 348 TYR B CG 1 ATOM 9857 C CD1 . TYR B 2 348 ? 4.349 10.756 41.552 1.00 106.71 ? 348 TYR B CD1 1 ATOM 9858 C CD2 . TYR B 2 348 ? 4.293 9.553 43.609 1.00 99.43 ? 348 TYR B CD2 1 ATOM 9859 C CE1 . TYR B 2 348 ? 4.044 9.596 40.860 1.00 112.02 ? 348 TYR B CE1 1 ATOM 9860 C CE2 . TYR B 2 348 ? 3.988 8.388 42.925 1.00 102.44 ? 348 TYR B CE2 1 ATOM 9861 C CZ . TYR B 2 348 ? 3.865 8.415 41.551 1.00 108.37 ? 348 TYR B CZ 1 ATOM 9862 O OH . TYR B 2 348 ? 3.562 7.262 40.863 1.00 99.42 ? 348 TYR B OH 1 ATOM 9863 N N . GLY B 2 349 ? 2.307 12.688 45.598 1.00 88.07 ? 349 GLY B N 1 ATOM 9864 C CA . GLY B 2 349 ? 1.114 12.276 46.312 1.00 99.34 ? 349 GLY B CA 1 ATOM 9865 C C . GLY B 2 349 ? -0.116 12.996 45.799 1.00 107.95 ? 349 GLY B C 1 ATOM 9866 O O . GLY B 2 349 ? -1.129 12.367 45.498 1.00 105.52 ? 349 GLY B O 1 ATOM 9867 N N . LYS B 2 350 ? -0.021 14.318 45.695 1.00 104.24 ? 350 LYS B N 1 ATOM 9868 C CA . LYS B 2 350 ? -1.104 15.131 45.151 1.00 106.80 ? 350 LYS B CA 1 ATOM 9869 C C . LYS B 2 350 ? -1.459 14.711 43.730 1.00 109.95 ? 350 LYS B C 1 ATOM 9870 O O . LYS B 2 350 ? -2.628 14.508 43.403 1.00 96.80 ? 350 LYS B O 1 ATOM 9871 C CB . LYS B 2 350 ? -0.726 16.615 45.160 1.00 117.02 ? 350 LYS B CB 1 ATOM 9872 C CG . LYS B 2 350 ? -0.922 17.324 46.488 1.00 123.33 ? 350 LYS B CG 1 ATOM 9873 C CD . LYS B 2 350 ? -0.723 18.826 46.323 1.00 124.81 ? 350 LYS B CD 1 ATOM 9874 C CE . LYS B 2 350 ? -1.111 19.586 47.579 1.00 126.56 ? 350 LYS B CE 1 ATOM 9875 N NZ . LYS B 2 350 ? -0.998 21.059 47.384 1.00 125.88 ? 350 LYS B NZ 1 ATOM 9876 N N . ILE B 2 351 ? -0.434 14.589 42.894 1.00 108.63 ? 351 ILE B N 1 ATOM 9877 C CA . ILE B 2 351 ? -0.613 14.313 41.474 1.00 94.87 ? 351 ILE B CA 1 ATOM 9878 C C . ILE B 2 351 ? -1.349 13.002 41.233 1.00 88.41 ? 351 ILE B C 1 ATOM 9879 O O . ILE B 2 351 ? -2.199 12.910 40.347 1.00 109.80 ? 351 ILE B O 1 ATOM 9880 C CB . ILE B 2 351 ? 0.743 14.287 40.754 1.00 86.75 ? 351 ILE B CB 1 ATOM 9881 C CG1 . ILE B 2 351 ? 1.402 15.662 40.856 1.00 79.45 ? 351 ILE B CG1 1 ATOM 9882 C CG2 . ILE B 2 351 ? 0.578 13.888 39.298 1.00 88.09 ? 351 ILE B CG2 1 ATOM 9883 C CD1 . ILE B 2 351 ? 2.791 15.715 40.291 1.00 95.84 ? 351 ILE B CD1 1 ATOM 9884 N N . ARG B 2 352 ? -1.036 11.991 42.034 1.00 94.19 ? 352 ARG B N 1 ATOM 9885 C CA . ARG B 2 352 ? -1.700 10.702 41.896 1.00 99.52 ? 352 ARG B CA 1 ATOM 9886 C C . ARG B 2 352 ? -2.936 10.632 42.787 1.00 98.30 ? 352 ARG B C 1 ATOM 9887 O O . ARG B 2 352 ? -3.598 9.599 42.862 1.00 111.57 ? 352 ARG B O 1 ATOM 9888 C CB . ARG B 2 352 ? -0.731 9.554 42.211 1.00 85.27 ? 352 ARG B CB 1 ATOM 9889 C CG . ARG B 2 352 ? 0.218 9.191 41.060 1.00 89.77 ? 352 ARG B CG 1 ATOM 9890 C CD . ARG B 2 352 ? -0.157 9.919 39.767 1.00 118.36 ? 352 ARG B CD 1 ATOM 9891 N NE . ARG B 2 352 ? 0.439 9.324 38.574 1.00 148.40 ? 352 ARG B NE 1 ATOM 9892 C CZ . ARG B 2 352 ? 0.312 9.826 37.348 1.00 142.13 ? 352 ARG B CZ 1 ATOM 9893 N NH1 . ARG B 2 352 ? -0.386 10.938 37.153 1.00 129.22 ? 352 ARG B NH1 1 ATOM 9894 N NH2 . ARG B 2 352 ? 0.882 9.218 36.316 1.00 131.19 ? 352 ARG B NH2 1 ATOM 9895 N N . SER B 2 353 ? -3.244 11.736 43.459 1.00 104.08 ? 353 SER B N 1 ATOM 9896 C CA . SER B 2 353 ? -4.432 11.806 44.304 1.00 127.19 ? 353 SER B CA 1 ATOM 9897 C C . SER B 2 353 ? -5.685 12.175 43.518 1.00 126.78 ? 353 SER B C 1 ATOM 9898 O O . SER B 2 353 ? -6.802 12.004 44.006 1.00 130.18 ? 353 SER B O 1 ATOM 9899 C CB . SER B 2 353 ? -4.230 12.816 45.436 1.00 130.73 ? 353 SER B CB 1 ATOM 9900 O OG . SER B 2 353 ? -5.460 13.130 46.065 1.00 138.50 ? 353 SER B OG 1 ATOM 9901 N N . LYS B 2 354 ? -5.501 12.677 42.302 1.00 119.53 ? 354 LYS B N 1 ATOM 9902 C CA . LYS B 2 354 ? -6.629 13.161 41.516 1.00 117.88 ? 354 LYS B CA 1 ATOM 9903 C C . LYS B 2 354 ? -6.765 12.457 40.170 1.00 113.11 ? 354 LYS B C 1 ATOM 9904 O O . LYS B 2 354 ? -5.790 11.951 39.614 1.00 104.02 ? 354 LYS B O 1 ATOM 9905 C CB . LYS B 2 354 ? -6.510 14.672 41.290 1.00 97.16 ? 354 LYS B CB 1 ATOM 9906 C CG . LYS B 2 354 ? -7.618 15.485 41.942 1.00 117.20 ? 354 LYS B CG 1 ATOM 9907 C CD . LYS B 2 354 ? -7.630 16.923 41.438 1.00 125.89 ? 354 LYS B CD 1 ATOM 9908 C CE . LYS B 2 354 ? -7.973 16.988 39.955 1.00 115.36 ? 354 LYS B CE 1 ATOM 9909 N NZ . LYS B 2 354 ? -8.020 18.391 39.456 1.00 106.91 ? 354 LYS B NZ 1 ATOM 9910 N N . VAL B 2 355 ? -7.993 12.424 39.664 1.00 94.61 ? 355 VAL B N 1 ATOM 9911 C CA . VAL B 2 355 ? -8.274 11.929 38.324 1.00 75.61 ? 355 VAL B CA 1 ATOM 9912 C C . VAL B 2 355 ? -9.276 12.841 37.621 1.00 75.45 ? 355 VAL B C 1 ATOM 9913 O O . VAL B 2 355 ? -10.368 13.080 38.136 1.00 85.59 ? 355 VAL B O 1 ATOM 9914 C CB . VAL B 2 355 ? -8.824 10.491 38.352 1.00 86.58 ? 355 VAL B CB 1 ATOM 9915 C CG1 . VAL B 2 355 ? -9.501 10.152 37.033 1.00 76.59 ? 355 VAL B CG1 1 ATOM 9916 C CG2 . VAL B 2 355 ? -7.713 9.500 38.663 1.00 93.90 ? 355 VAL B CG2 1 ATOM 9917 N N . GLU B 2 356 ? -8.900 13.357 36.454 1.00 72.46 ? 356 GLU B N 1 ATOM 9918 C CA . GLU B 2 356 ? -9.805 14.184 35.661 1.00 92.56 ? 356 GLU B CA 1 ATOM 9919 C C . GLU B 2 356 ? -9.668 13.887 34.171 1.00 105.18 ? 356 GLU B C 1 ATOM 9920 O O . GLU B 2 356 ? -8.560 13.834 33.636 1.00 112.94 ? 356 GLU B O 1 ATOM 9921 C CB . GLU B 2 356 ? -9.552 15.671 35.923 1.00 104.19 ? 356 GLU B CB 1 ATOM 9922 C CG . GLU B 2 356 ? -10.442 16.596 35.103 1.00 112.42 ? 356 GLU B CG 1 ATOM 9923 C CD . GLU B 2 356 ? -10.353 18.043 35.544 1.00 125.25 ? 356 GLU B CD 1 ATOM 9924 O OE1 . GLU B 2 356 ? -9.554 18.342 36.457 1.00 135.99 ? 356 GLU B OE1 1 ATOM 9925 O OE2 . GLU B 2 356 ? -11.087 18.882 34.979 1.00 118.68 ? 356 GLU B OE2 1 ATOM 9926 N N . LEU B 2 357 ? -10.803 13.704 33.505 1.00 84.68 ? 357 LEU B N 1 ATOM 9927 C CA . LEU B 2 357 ? -10.815 13.384 32.084 1.00 79.81 ? 357 LEU B CA 1 ATOM 9928 C C . LEU B 2 357 ? -10.673 14.629 31.213 1.00 101.47 ? 357 LEU B C 1 ATOM 9929 O O . LEU B 2 357 ? -11.268 15.670 31.496 1.00 108.30 ? 357 LEU B O 1 ATOM 9930 C CB . LEU B 2 357 ? -12.104 12.646 31.718 1.00 73.02 ? 357 LEU B CB 1 ATOM 9931 C CG . LEU B 2 357 ? -12.336 11.277 32.361 1.00 92.09 ? 357 LEU B CG 1 ATOM 9932 C CD1 . LEU B 2 357 ? -13.717 10.745 32.002 1.00 79.86 ? 357 LEU B CD1 1 ATOM 9933 C CD2 . LEU B 2 357 ? -11.251 10.299 31.936 1.00 93.52 ? 357 LEU B CD2 1 ATOM 9934 N N . GLU B 2 358 ? -9.879 14.511 30.153 1.00 102.08 ? 358 GLU B N 1 ATOM 9935 C CA . GLU B 2 358 ? -9.779 15.562 29.149 1.00 87.12 ? 358 GLU B CA 1 ATOM 9936 C C . GLU B 2 358 ? -10.206 15.023 27.787 1.00 88.98 ? 358 GLU B C 1 ATOM 9937 O O . GLU B 2 358 ? -10.113 13.825 27.526 1.00 83.24 ? 358 GLU B O 1 ATOM 9938 C CB . GLU B 2 358 ? -8.357 16.130 29.083 1.00 79.22 ? 358 GLU B CB 1 ATOM 9939 C CG . GLU B 2 358 ? -7.276 15.128 28.709 1.00 90.30 ? 358 GLU B CG 1 ATOM 9940 C CD . GLU B 2 358 ? -5.934 15.790 28.444 1.00 124.94 ? 358 GLU B CD 1 ATOM 9941 O OE1 . GLU B 2 358 ? -5.870 16.671 27.560 1.00 153.85 ? 358 GLU B OE1 1 ATOM 9942 O OE2 . GLU B 2 358 ? -4.943 15.435 29.119 1.00 105.26 ? 358 GLU B OE2 1 ATOM 9943 N N . VAL B 2 359 ? -10.684 15.911 26.925 1.00 94.64 ? 359 VAL B N 1 ATOM 9944 C CA . VAL B 2 359 ? -11.172 15.511 25.613 1.00 74.74 ? 359 VAL B CA 1 ATOM 9945 C C . VAL B 2 359 ? -10.347 16.138 24.494 1.00 74.22 ? 359 VAL B C 1 ATOM 9946 O O . VAL B 2 359 ? -10.097 17.342 24.494 1.00 123.62 ? 359 VAL B O 1 ATOM 9947 C CB . VAL B 2 359 ? -12.648 15.899 25.425 1.00 66.96 ? 359 VAL B CB 1 ATOM 9948 C CG1 . VAL B 2 359 ? -13.197 15.285 24.151 1.00 75.26 ? 359 VAL B CG1 1 ATOM 9949 C CG2 . VAL B 2 359 ? -13.464 15.458 26.626 1.00 66.43 ? 359 VAL B CG2 1 ATOM 9950 N N . ARG B 2 360 ? -9.926 15.314 23.541 1.00 70.08 ? 360 ARG B N 1 ATOM 9951 C CA . ARG B 2 360 ? -9.175 15.793 22.390 1.00 72.36 ? 360 ARG B CA 1 ATOM 9952 C C . ARG B 2 360 ? -9.902 15.505 21.080 1.00 97.86 ? 360 ARG B C 1 ATOM 9953 O O . ARG B 2 360 ? -10.523 14.452 20.921 1.00 123.98 ? 360 ARG B O 1 ATOM 9954 C CB . ARG B 2 360 ? -7.784 15.157 22.358 1.00 66.07 ? 360 ARG B CB 1 ATOM 9955 C CG . ARG B 2 360 ? -6.897 15.548 23.524 1.00 72.38 ? 360 ARG B CG 1 ATOM 9956 C CD . ARG B 2 360 ? -5.525 14.911 23.396 1.00 98.13 ? 360 ARG B CD 1 ATOM 9957 N NE . ARG B 2 360 ? -4.653 15.253 24.516 1.00 109.83 ? 360 ARG B NE 1 ATOM 9958 C CZ . ARG B 2 360 ? -3.491 14.658 24.764 1.00 111.70 ? 360 ARG B CZ 1 ATOM 9959 N NH1 . ARG B 2 360 ? -3.060 13.683 23.973 1.00 108.20 ? 360 ARG B NH1 1 ATOM 9960 N NH2 . ARG B 2 360 ? -2.762 15.032 25.807 1.00 89.90 ? 360 ARG B NH2 1 ATOM 9961 N N . ASP B 2 361 ? -9.825 16.459 20.155 1.00 91.09 ? 361 ASP B N 1 ATOM 9962 C CA . ASP B 2 361 ? -10.316 16.290 18.788 1.00 90.16 ? 361 ASP B CA 1 ATOM 9963 C C . ASP B 2 361 ? -11.807 15.966 18.708 1.00 81.08 ? 361 ASP B C 1 ATOM 9964 O O . ASP B 2 361 ? -12.257 15.315 17.764 1.00 80.60 ? 361 ASP B O 1 ATOM 9965 C CB . ASP B 2 361 ? -9.511 15.200 18.079 1.00 97.84 ? 361 ASP B CB 1 ATOM 9966 C CG . ASP B 2 361 ? -8.014 15.427 18.174 1.00 126.35 ? 361 ASP B CG 1 ATOM 9967 O OD1 . ASP B 2 361 ? -7.575 16.587 18.020 1.00 127.19 ? 361 ASP B OD1 1 ATOM 9968 O OD2 . ASP B 2 361 ? -7.277 14.447 18.411 1.00 145.76 ? 361 ASP B OD2 1 ATOM 9969 N N . LEU B 2 362 ? -12.570 16.432 19.692 1.00 69.36 ? 362 LEU B N 1 ATOM 9970 C CA . LEU B 2 362 ? -14.010 16.212 19.712 1.00 70.36 ? 362 LEU B CA 1 ATOM 9971 C C . LEU B 2 362 ? -14.724 17.007 18.629 1.00 79.38 ? 362 LEU B C 1 ATOM 9972 O O . LEU B 2 362 ? -14.638 18.234 18.602 1.00 116.32 ? 362 LEU B O 1 ATOM 9973 C CB . LEU B 2 362 ? -14.589 16.585 21.076 1.00 77.83 ? 362 LEU B CB 1 ATOM 9974 C CG . LEU B 2 362 ? -16.117 16.558 21.184 1.00 81.79 ? 362 LEU B CG 1 ATOM 9975 C CD1 . LEU B 2 362 ? -16.640 15.152 20.977 1.00 88.35 ? 362 LEU B CD1 1 ATOM 9976 C CD2 . LEU B 2 362 ? -16.582 17.110 22.523 1.00 93.12 ? 362 LEU B CD2 1 ATOM 9977 N N . PRO B 2 363 ? -15.432 16.310 17.731 1.00 87.29 ? 363 PRO B N 1 ATOM 9978 C CA . PRO B 2 363 ? -16.293 16.995 16.762 1.00 111.81 ? 363 PRO B CA 1 ATOM 9979 C C . PRO B 2 363 ? -17.393 17.780 17.470 1.00 124.68 ? 363 PRO B C 1 ATOM 9980 O O . PRO B 2 363 ? -18.080 17.232 18.333 1.00 138.49 ? 363 PRO B O 1 ATOM 9981 C CB . PRO B 2 363 ? -16.875 15.847 15.929 1.00 109.01 ? 363 PRO B CB 1 ATOM 9982 C CG . PRO B 2 363 ? -16.715 14.631 16.780 1.00 94.89 ? 363 PRO B CG 1 ATOM 9983 C CD . PRO B 2 363 ? -15.457 14.849 17.556 1.00 94.36 ? 363 PRO B CD 1 ATOM 9984 N N . GLU B 2 364 ? -17.555 19.046 17.099 1.00 104.89 ? 364 GLU B N 1 ATOM 9985 C CA . GLU B 2 364 ? -18.479 19.944 17.786 1.00 116.83 ? 364 GLU B CA 1 ATOM 9986 C C . GLU B 2 364 ? -19.936 19.550 17.565 1.00 124.45 ? 364 GLU B C 1 ATOM 9987 O O . GLU B 2 364 ? -20.817 19.956 18.325 1.00 113.87 ? 364 GLU B O 1 ATOM 9988 C CB . GLU B 2 364 ? -18.257 21.388 17.324 1.00 130.30 ? 364 GLU B CB 1 ATOM 9989 C CG . GLU B 2 364 ? -18.912 21.737 15.992 1.00 137.07 ? 364 GLU B CG 1 ATOM 9990 C CD . GLU B 2 364 ? -18.419 20.880 14.837 1.00 154.12 ? 364 GLU B CD 1 ATOM 9991 O OE1 . GLU B 2 364 ? -17.293 20.344 14.920 1.00 155.32 ? 364 GLU B OE1 1 ATOM 9992 O OE2 . GLU B 2 364 ? -19.163 20.741 13.844 1.00 166.72 ? 364 GLU B OE2 1 ATOM 9993 N N . GLU B 2 365 ? -20.180 18.758 16.525 1.00 121.68 ? 365 GLU B N 1 ATOM 9994 C CA . GLU B 2 365 ? -21.528 18.311 16.193 1.00 119.40 ? 365 GLU B CA 1 ATOM 9995 C C . GLU B 2 365 ? -22.151 17.490 17.316 1.00 116.66 ? 365 GLU B C 1 ATOM 9996 O O . GLU B 2 365 ? -23.371 17.480 17.488 1.00 102.75 ? 365 GLU B O 1 ATOM 9997 C CB . GLU B 2 365 ? -21.517 17.496 14.898 1.00 127.90 ? 365 GLU B CB 1 ATOM 9998 C CG . GLU B 2 365 ? -21.396 18.336 13.640 1.00 140.85 ? 365 GLU B CG 1 ATOM 9999 C CD . GLU B 2 365 ? -22.591 19.249 13.431 1.00 155.29 ? 365 GLU B CD 1 ATOM 10000 O OE1 . GLU B 2 365 ? -22.430 20.298 12.772 1.00 157.29 ? 365 GLU B OE1 1 ATOM 10001 O OE2 . GLU B 2 365 ? -23.693 18.918 13.920 1.00 156.31 ? 365 GLU B OE2 1 ATOM 10002 N N . LEU B 2 366 ? -21.311 16.800 18.079 1.00 111.28 ? 366 LEU B N 1 ATOM 10003 C CA . LEU B 2 366 ? -21.805 16.014 19.198 1.00 118.56 ? 366 LEU B CA 1 ATOM 10004 C C . LEU B 2 366 ? -21.243 16.495 20.528 1.00 96.61 ? 366 LEU B C 1 ATOM 10005 O O . LEU B 2 366 ? -20.110 16.970 20.601 1.00 85.71 ? 366 LEU B O 1 ATOM 10006 C CB . LEU B 2 366 ? -21.491 14.529 18.998 1.00 131.80 ? 366 LEU B CB 1 ATOM 10007 C CG . LEU B 2 366 ? -20.052 14.080 18.757 1.00 124.91 ? 366 LEU B CG 1 ATOM 10008 C CD1 . LEU B 2 366 ? -19.531 13.345 19.972 1.00 114.91 ? 366 LEU B CD1 1 ATOM 10009 C CD2 . LEU B 2 366 ? -19.987 13.192 17.529 1.00 118.54 ? 366 LEU B CD2 1 ATOM 10010 N N . SER B 2 367 ? -22.051 16.366 21.577 1.00 92.63 ? 367 SER B N 1 ATOM 10011 C CA . SER B 2 367 ? -21.655 16.803 22.909 1.00 114.50 ? 367 SER B CA 1 ATOM 10012 C C . SER B 2 367 ? -21.535 15.625 23.866 1.00 112.46 ? 367 SER B C 1 ATOM 10013 O O . SER B 2 367 ? -22.183 14.592 23.687 1.00 90.85 ? 367 SER B O 1 ATOM 10014 C CB . SER B 2 367 ? -22.652 17.823 23.461 1.00 130.25 ? 367 SER B CB 1 ATOM 10015 O OG . SER B 2 367 ? -22.210 18.348 24.703 1.00 125.03 ? 367 SER B OG 1 ATOM 10016 N N . LEU B 2 368 ? -20.698 15.795 24.885 1.00 109.14 ? 368 LEU B N 1 ATOM 10017 C CA . LEU B 2 368 ? -20.434 14.745 25.858 1.00 98.42 ? 368 LEU B CA 1 ATOM 10018 C C . LEU B 2 368 ? -20.948 15.115 27.241 1.00 84.84 ? 368 LEU B C 1 ATOM 10019 O O . LEU B 2 368 ? -20.491 16.090 27.835 1.00 89.48 ? 368 LEU B O 1 ATOM 10020 C CB . LEU B 2 368 ? -18.933 14.453 25.932 1.00 85.16 ? 368 LEU B CB 1 ATOM 10021 C CG . LEU B 2 368 ? -18.354 13.361 25.033 1.00 90.43 ? 368 LEU B CG 1 ATOM 10022 C CD1 . LEU B 2 368 ? -18.735 13.579 23.582 1.00 89.61 ? 368 LEU B CD1 1 ATOM 10023 C CD2 . LEU B 2 368 ? -16.844 13.319 25.190 1.00 105.21 ? 368 LEU B CD2 1 ATOM 10024 N N . SER B 2 369 ? -21.897 14.339 27.757 1.00 84.46 ? 369 SER B N 1 ATOM 10025 C CA . SER B 2 369 ? -22.323 14.524 29.136 1.00 91.20 ? 369 SER B CA 1 ATOM 10026 C C . SER B 2 369 ? -21.412 13.705 30.039 1.00 99.09 ? 369 SER B C 1 ATOM 10027 O O . SER B 2 369 ? -20.607 12.916 29.550 1.00 118.05 ? 369 SER B O 1 ATOM 10028 C CB . SER B 2 369 ? -23.780 14.098 29.316 1.00 103.07 ? 369 SER B CB 1 ATOM 10029 O OG . SER B 2 369 ? -24.582 14.568 28.246 1.00 119.86 ? 369 SER B OG 1 ATOM 10030 N N . PHE B 2 370 ? -21.554 13.863 31.351 1.00 107.01 ? 370 PHE B N 1 ATOM 10031 C CA . PHE B 2 370 ? -20.739 13.097 32.290 1.00 95.90 ? 370 PHE B CA 1 ATOM 10032 C C . PHE B 2 370 ? -21.435 12.852 33.624 1.00 103.16 ? 370 PHE B C 1 ATOM 10033 O O . PHE B 2 370 ? -22.090 13.738 34.171 1.00 109.42 ? 370 PHE B O 1 ATOM 10034 C CB . PHE B 2 370 ? -19.403 13.806 32.549 1.00 85.56 ? 370 PHE B CB 1 ATOM 10035 C CG . PHE B 2 370 ? -18.446 13.751 31.392 1.00 89.21 ? 370 PHE B CG 1 ATOM 10036 C CD1 . PHE B 2 370 ? -17.672 12.623 31.168 1.00 97.55 ? 370 PHE B CD1 1 ATOM 10037 C CD2 . PHE B 2 370 ? -18.314 14.829 30.531 1.00 92.25 ? 370 PHE B CD2 1 ATOM 10038 C CE1 . PHE B 2 370 ? -16.791 12.569 30.104 1.00 85.60 ? 370 PHE B CE1 1 ATOM 10039 C CE2 . PHE B 2 370 ? -17.436 14.781 29.465 1.00 81.73 ? 370 PHE B CE2 1 ATOM 10040 C CZ . PHE B 2 370 ? -16.673 13.650 29.251 1.00 84.91 ? 370 PHE B CZ 1 ATOM 10041 N N . ASN B 2 371 ? -21.257 11.647 34.148 1.00 96.14 ? 371 ASN B N 1 ATOM 10042 C CA . ASN B 2 371 ? -21.567 11.340 35.535 1.00 100.10 ? 371 ASN B CA 1 ATOM 10043 C C . ASN B 2 371 ? -20.305 10.717 36.122 1.00 102.13 ? 371 ASN B C 1 ATOM 10044 O O . ASN B 2 371 ? -19.499 10.149 35.386 1.00 101.56 ? 371 ASN B O 1 ATOM 10045 C CB . ASN B 2 371 ? -22.774 10.397 35.659 1.00 100.04 ? 371 ASN B CB 1 ATOM 10046 C CG . ASN B 2 371 ? -24.092 11.063 35.269 1.00 94.11 ? 371 ASN B CG 1 ATOM 10047 O OD1 . ASN B 2 371 ? -24.164 12.280 35.126 1.00 99.29 ? 371 ASN B OD1 1 ATOM 10048 N ND2 . ASN B 2 371 ? -25.142 10.261 35.104 1.00 114.31 ? 371 ASN B ND2 1 ATOM 10049 N N . ALA B 2 372 ? -20.112 10.833 37.431 1.00 111.67 ? 372 ALA B N 1 ATOM 10050 C CA . ALA B 2 372 ? -18.883 10.331 38.040 1.00 108.27 ? 372 ALA B CA 1 ATOM 10051 C C . ALA B 2 372 ? -19.137 9.418 39.237 1.00 119.84 ? 372 ALA B C 1 ATOM 10052 O O . ALA B 2 372 ? -19.875 9.767 40.157 1.00 127.07 ? 372 ALA B O 1 ATOM 10053 C CB . ALA B 2 372 ? -17.996 11.489 38.453 1.00 95.35 ? 372 ALA B CB 1 ATOM 10054 N N . THR B 2 373 ? -18.513 8.246 39.212 1.00 102.60 ? 373 THR B N 1 ATOM 10055 C CA . THR B 2 373 ? -18.548 7.333 40.344 1.00 90.21 ? 373 THR B CA 1 ATOM 10056 C C . THR B 2 373 ? -17.162 7.263 40.972 1.00 88.38 ? 373 THR B C 1 ATOM 10057 O O . THR B 2 373 ? -16.229 6.734 40.373 1.00 98.83 ? 373 THR B O 1 ATOM 10058 C CB . THR B 2 373 ? -19.002 5.927 39.926 1.00 107.73 ? 373 THR B CB 1 ATOM 10059 O OG1 . THR B 2 373 ? -20.257 6.015 39.241 1.00 122.28 ? 373 THR B OG1 1 ATOM 10060 C CG2 . THR B 2 373 ? -19.157 5.034 41.144 1.00 126.09 ? 373 THR B CG2 1 ATOM 10061 N N . CYS B 2 374 ? -17.031 7.804 42.178 1.00 97.46 ? 374 CYS B N 1 ATOM 10062 C CA . CYS B 2 374 ? -15.732 7.911 42.832 1.00 89.97 ? 374 CYS B CA 1 ATOM 10063 C C . CYS B 2 374 ? -15.717 7.172 44.160 1.00 122.22 ? 374 CYS B C 1 ATOM 10064 O O . CYS B 2 374 ? -14.973 6.207 44.342 1.00 145.22 ? 374 CYS B O 1 ATOM 10065 C CB . CYS B 2 374 ? -15.370 9.377 43.049 1.00 88.46 ? 374 CYS B CB 1 ATOM 10066 S SG . CYS B 2 374 ? -15.682 10.411 41.610 1.00 130.96 ? 374 CYS B SG 1 ATOM 10067 N N . LEU B 2 375 ? -16.549 7.635 45.085 1.00 121.50 ? 375 LEU B N 1 ATOM 10068 C CA . LEU B 2 375 ? -16.626 7.049 46.414 1.00 122.51 ? 375 LEU B CA 1 ATOM 10069 C C . LEU B 2 375 ? -17.687 5.958 46.439 1.00 115.35 ? 375 LEU B C 1 ATOM 10070 O O . LEU B 2 375 ? -18.880 6.243 46.326 1.00 101.04 ? 375 LEU B O 1 ATOM 10071 C CB . LEU B 2 375 ? -16.937 8.133 47.443 1.00 123.32 ? 375 LEU B CB 1 ATOM 10072 C CG . LEU B 2 375 ? -17.250 7.735 48.882 1.00 135.32 ? 375 LEU B CG 1 ATOM 10073 C CD1 . LEU B 2 375 ? -16.131 6.899 49.482 1.00 133.14 ? 375 LEU B CD1 1 ATOM 10074 C CD2 . LEU B 2 375 ? -17.481 8.995 49.694 1.00 153.54 ? 375 LEU B CD2 1 ATOM 10075 N N . ASN B 2 376 ? -17.226 4.714 46.578 1.00 108.56 ? 376 ASN B N 1 ATOM 10076 C CA . ASN B 2 376 ? -18.050 3.505 46.464 1.00 127.13 ? 376 ASN B CA 1 ATOM 10077 C C . ASN B 2 376 ? -19.039 3.602 45.301 1.00 139.01 ? 376 ASN B C 1 ATOM 10078 O O . ASN B 2 376 ? -18.639 3.831 44.160 1.00 141.53 ? 376 ASN B O 1 ATOM 10079 C CB . ASN B 2 376 ? -18.775 3.158 47.780 1.00 114.30 ? 376 ASN B CB 1 ATOM 10080 C CG . ASN B 2 376 ? -19.391 4.357 48.467 1.00 124.48 ? 376 ASN B CG 1 ATOM 10081 O OD1 . ASN B 2 376 ? -20.466 4.822 48.089 1.00 143.60 ? 376 ASN B OD1 1 ATOM 10082 N ND2 . ASN B 2 376 ? -18.723 4.849 49.502 1.00 121.66 ? 376 ASN B ND2 1 ATOM 10083 N N . ASN B 2 377 ? -20.324 3.430 45.590 1.00 122.86 ? 377 ASN B N 1 ATOM 10084 C CA . ASN B 2 377 ? -21.341 3.417 44.545 1.00 113.96 ? 377 ASN B CA 1 ATOM 10085 C C . ASN B 2 377 ? -22.039 4.760 44.329 1.00 134.17 ? 377 ASN B C 1 ATOM 10086 O O . ASN B 2 377 ? -22.943 4.864 43.499 1.00 139.82 ? 377 ASN B O 1 ATOM 10087 C CB . ASN B 2 377 ? -22.381 2.344 44.857 1.00 118.23 ? 377 ASN B CB 1 ATOM 10088 C CG . ASN B 2 377 ? -21.751 1.004 45.173 1.00 141.39 ? 377 ASN B CG 1 ATOM 10089 O OD1 . ASN B 2 377 ? -20.629 0.719 44.752 1.00 130.52 ? 377 ASN B OD1 1 ATOM 10090 N ND2 . ASN B 2 377 ? -22.469 0.172 45.920 1.00 146.26 ? 377 ASN B ND2 1 ATOM 10091 N N . GLU B 2 378 ? -21.622 5.784 45.069 1.00 135.38 ? 378 GLU B N 1 ATOM 10092 C CA . GLU B 2 378 ? -22.261 7.097 44.981 1.00 122.79 ? 378 GLU B CA 1 ATOM 10093 C C . GLU B 2 378 ? -21.853 7.853 43.717 1.00 131.84 ? 378 GLU B C 1 ATOM 10094 O O . GLU B 2 378 ? -20.668 8.082 43.469 1.00 121.34 ? 378 GLU B O 1 ATOM 10095 C CB . GLU B 2 378 ? -21.936 7.936 46.220 1.00 130.97 ? 378 GLU B CB 1 ATOM 10096 C CG . GLU B 2 378 ? -22.529 7.390 47.512 1.00 141.08 ? 378 GLU B CG 1 ATOM 10097 C CD . GLU B 2 378 ? -22.352 8.335 48.686 1.00 150.09 ? 378 GLU B CD 1 ATOM 10098 O OE1 . GLU B 2 378 ? -22.763 7.971 49.810 1.00 151.47 ? 378 GLU B OE1 1 ATOM 10099 O OE2 . GLU B 2 378 ? -21.807 9.441 48.486 1.00 132.18 ? 378 GLU B OE2 1 ATOM 10100 N N . VAL B 2 379 ? -22.849 8.245 42.929 1.00 142.37 ? 379 VAL B N 1 ATOM 10101 C CA . VAL B 2 379 ? -22.616 8.941 41.667 1.00 129.95 ? 379 VAL B CA 1 ATOM 10102 C C . VAL B 2 379 ? -22.706 10.461 41.816 1.00 128.25 ? 379 VAL B C 1 ATOM 10103 O O . VAL B 2 379 ? -23.527 10.974 42.576 1.00 139.15 ? 379 VAL B O 1 ATOM 10104 C CB . VAL B 2 379 ? -23.617 8.483 40.585 1.00 127.90 ? 379 VAL B CB 1 ATOM 10105 C CG1 . VAL B 2 379 ? -23.299 7.065 40.134 1.00 132.43 ? 379 VAL B CG1 1 ATOM 10106 C CG2 . VAL B 2 379 ? -25.047 8.577 41.101 1.00 128.01 ? 379 VAL B CG2 1 ATOM 10107 N N . ILE B 2 380 ? -21.849 11.173 41.088 1.00 125.11 ? 380 ILE B N 1 ATOM 10108 C CA . ILE B 2 380 ? -21.829 12.635 41.118 1.00 117.39 ? 380 ILE B CA 1 ATOM 10109 C C . ILE B 2 380 ? -21.935 13.190 39.696 1.00 122.69 ? 380 ILE B C 1 ATOM 10110 O O . ILE B 2 380 ? -20.922 13.398 39.025 1.00 127.99 ? 380 ILE B O 1 ATOM 10111 C CB . ILE B 2 380 ? -20.548 13.181 41.796 1.00 97.59 ? 380 ILE B CB 1 ATOM 10112 C CG1 . ILE B 2 380 ? -20.414 12.644 43.224 1.00 107.81 ? 380 ILE B CG1 1 ATOM 10113 C CG2 . ILE B 2 380 ? -20.559 14.701 41.821 1.00 100.63 ? 380 ILE B CG2 1 ATOM 10114 C CD1 . ILE B 2 380 ? -19.600 11.367 43.342 1.00 127.29 ? 380 ILE B CD1 1 ATOM 10115 N N . PRO B 2 381 ? -23.173 13.423 39.232 1.00 127.47 ? 381 PRO B N 1 ATOM 10116 C CA . PRO B 2 381 ? -23.462 13.844 37.855 1.00 128.19 ? 381 PRO B CA 1 ATOM 10117 C C . PRO B 2 381 ? -22.811 15.168 37.465 1.00 117.70 ? 381 PRO B C 1 ATOM 10118 O O . PRO B 2 381 ? -22.585 16.028 38.317 1.00 129.84 ? 381 PRO B O 1 ATOM 10119 C CB . PRO B 2 381 ? -24.989 13.974 37.843 1.00 128.73 ? 381 PRO B CB 1 ATOM 10120 C CG . PRO B 2 381 ? -25.454 13.091 38.947 1.00 127.76 ? 381 PRO B CG 1 ATOM 10121 C CD . PRO B 2 381 ? -24.406 13.216 40.009 1.00 128.45 ? 381 PRO B CD 1 ATOM 10122 N N . GLY B 2 382 ? -22.508 15.317 36.180 1.00 104.25 ? 382 GLY B N 1 ATOM 10123 C CA . GLY B 2 382 ? -21.955 16.553 35.660 1.00 106.38 ? 382 GLY B CA 1 ATOM 10124 C C . GLY B 2 382 ? -20.461 16.696 35.871 1.00 100.10 ? 382 GLY B C 1 ATOM 10125 O O . GLY B 2 382 ? -19.820 17.553 35.260 1.00 117.50 ? 382 GLY B O 1 ATOM 10126 N N . LEU B 2 383 ? -19.900 15.854 36.732 1.00 85.99 ? 383 LEU B N 1 ATOM 10127 C CA . LEU B 2 383 ? -18.489 15.960 37.079 1.00 102.53 ? 383 LEU B CA 1 ATOM 10128 C C . LEU B 2 383 ? -17.634 14.973 36.286 1.00 97.33 ? 383 LEU B C 1 ATOM 10129 O O . LEU B 2 383 ? -17.908 13.776 36.264 1.00 94.72 ? 383 LEU B O 1 ATOM 10130 C CB . LEU B 2 383 ? -18.296 15.743 38.580 1.00 106.49 ? 383 LEU B CB 1 ATOM 10131 C CG . LEU B 2 383 ? -16.954 16.198 39.152 1.00 121.59 ? 383 LEU B CG 1 ATOM 10132 C CD1 . LEU B 2 383 ? -16.673 17.647 38.776 1.00 105.32 ? 383 LEU B CD1 1 ATOM 10133 C CD2 . LEU B 2 383 ? -16.934 16.020 40.663 1.00 127.20 ? 383 LEU B CD2 1 ATOM 10134 N N . LYS B 2 384 ? -16.618 15.496 35.610 1.00 107.29 ? 384 LYS B N 1 ATOM 10135 C CA . LYS B 2 384 ? -15.680 14.677 34.847 1.00 85.11 ? 384 LYS B CA 1 ATOM 10136 C C . LYS B 2 384 ? -14.404 14.382 35.639 1.00 98.62 ? 384 LYS B C 1 ATOM 10137 O O . LYS B 2 384 ? -13.445 13.835 35.094 1.00 100.75 ? 384 LYS B O 1 ATOM 10138 C CB . LYS B 2 384 ? -15.336 15.355 33.516 1.00 85.80 ? 384 LYS B CB 1 ATOM 10139 C CG . LYS B 2 384 ? -14.687 16.723 33.657 1.00 124.55 ? 384 LYS B CG 1 ATOM 10140 C CD . LYS B 2 384 ? -14.631 17.449 32.320 1.00 127.56 ? 384 LYS B CD 1 ATOM 10141 C CE . LYS B 2 384 ? -16.029 17.749 31.796 1.00 124.60 ? 384 LYS B CE 1 ATOM 10142 N NZ . LYS B 2 384 ? -15.997 18.507 30.512 1.00 123.02 ? 384 LYS B NZ 1 ATOM 10143 N N . SER B 2 385 ? -14.377 14.777 36.910 1.00 97.85 ? 385 SER B N 1 ATOM 10144 C CA . SER B 2 385 ? -13.181 14.604 37.735 1.00 89.32 ? 385 SER B CA 1 ATOM 10145 C C . SER B 2 385 ? -13.451 13.908 39.071 1.00 94.16 ? 385 SER B C 1 ATOM 10146 O O . SER B 2 385 ? -14.595 13.808 39.513 1.00 99.14 ? 385 SER B O 1 ATOM 10147 C CB . SER B 2 385 ? -12.525 15.961 37.993 1.00 100.10 ? 385 SER B CB 1 ATOM 10148 O OG . SER B 2 385 ? -13.442 16.865 38.584 1.00 124.57 ? 385 SER B OG 1 ATOM 10149 N N . CYS B 2 386 ? -12.382 13.427 39.705 1.00 99.39 ? 386 CYS B N 1 ATOM 10150 C CA . CYS B 2 386 ? -12.467 12.792 41.021 1.00 104.42 ? 386 CYS B CA 1 ATOM 10151 C C . CYS B 2 386 ? -11.322 13.234 41.928 1.00 102.48 ? 386 CYS B C 1 ATOM 10152 O O . CYS B 2 386 ? -10.207 13.474 41.465 1.00 94.88 ? 386 CYS B O 1 ATOM 10153 C CB . CYS B 2 386 ? -12.464 11.270 40.892 1.00 81.27 ? 386 CYS B CB 1 ATOM 10154 S SG . CYS B 2 386 ? -14.050 10.567 40.411 1.00 144.65 ? 386 CYS B SG 1 ATOM 10155 N N . MET B 2 387 ? -11.601 13.323 43.225 1.00 92.57 ? 387 MET B N 1 ATOM 10156 C CA . MET B 2 387 ? -10.638 13.855 44.183 1.00 88.62 ? 387 MET B CA 1 ATOM 10157 C C . MET B 2 387 ? -10.528 12.966 45.422 1.00 95.47 ? 387 MET B C 1 ATOM 10158 O O . MET B 2 387 ? -11.427 12.176 45.710 1.00 118.24 ? 387 MET B O 1 ATOM 10159 C CB . MET B 2 387 ? -11.038 15.278 44.586 1.00 108.96 ? 387 MET B CB 1 ATOM 10160 C CG . MET B 2 387 ? -9.943 16.086 45.265 1.00 126.67 ? 387 MET B CG 1 ATOM 10161 S SD . MET B 2 387 ? -10.581 17.582 46.041 1.00 150.66 ? 387 MET B SD 1 ATOM 10162 C CE . MET B 2 387 ? -11.734 16.879 47.219 1.00 108.06 ? 387 MET B CE 1 ATOM 10163 N N . GLY B 2 388 ? -9.423 13.097 46.148 1.00 88.83 ? 388 GLY B N 1 ATOM 10164 C CA . GLY B 2 388 ? -9.236 12.382 47.398 1.00 99.13 ? 388 GLY B CA 1 ATOM 10165 C C . GLY B 2 388 ? -8.987 10.900 47.208 1.00 114.03 ? 388 GLY B C 1 ATOM 10166 O O . GLY B 2 388 ? -9.620 10.066 47.857 1.00 115.35 ? 388 GLY B O 1 ATOM 10167 N N . LEU B 2 389 ? -8.059 10.572 46.316 1.00 112.97 ? 389 LEU B N 1 ATOM 10168 C CA . LEU B 2 389 ? -7.759 9.180 46.008 1.00 124.01 ? 389 LEU B CA 1 ATOM 10169 C C . LEU B 2 389 ? -6.346 8.794 46.433 1.00 128.49 ? 389 LEU B C 1 ATOM 10170 O O . LEU B 2 389 ? -5.438 9.624 46.435 1.00 112.63 ? 389 LEU B O 1 ATOM 10171 C CB . LEU B 2 389 ? -7.936 8.917 44.511 1.00 108.31 ? 389 LEU B CB 1 ATOM 10172 C CG . LEU B 2 389 ? -9.260 9.359 43.885 1.00 107.32 ? 389 LEU B CG 1 ATOM 10173 C CD1 . LEU B 2 389 ? -9.335 8.932 42.427 1.00 91.51 ? 389 LEU B CD1 1 ATOM 10174 C CD2 . LEU B 2 389 ? -10.439 8.807 44.667 1.00 141.11 ? 389 LEU B CD2 1 ATOM 10175 N N . LYS B 2 390 ? -6.171 7.530 46.801 1.00 124.81 ? 390 LYS B N 1 ATOM 10176 C CA . LYS B 2 390 ? -4.843 6.990 47.060 1.00 126.02 ? 390 LYS B CA 1 ATOM 10177 C C . LYS B 2 390 ? -4.517 5.943 46.000 1.00 129.52 ? 390 LYS B C 1 ATOM 10178 O O . LYS B 2 390 ? -5.422 5.322 45.439 1.00 113.18 ? 390 LYS B O 1 ATOM 10179 C CB . LYS B 2 390 ? -4.749 6.395 48.468 1.00 115.70 ? 390 LYS B CB 1 ATOM 10180 C CG . LYS B 2 390 ? -5.726 5.266 48.748 1.00 127.72 ? 390 LYS B CG 1 ATOM 10181 C CD . LYS B 2 390 ? -5.481 4.656 50.121 1.00 141.68 ? 390 LYS B CD 1 ATOM 10182 C CE . LYS B 2 390 ? -5.558 5.709 51.217 1.00 145.34 ? 390 LYS B CE 1 ATOM 10183 N NZ . LYS B 2 390 ? -5.321 5.128 52.568 1.00 137.66 ? 390 LYS B NZ 1 ATOM 10184 N N . ILE B 2 391 ? -3.229 5.768 45.719 1.00 128.58 ? 391 ILE B N 1 ATOM 10185 C CA . ILE B 2 391 ? -2.771 4.863 44.667 1.00 112.74 ? 391 ILE B CA 1 ATOM 10186 C C . ILE B 2 391 ? -3.345 3.458 44.824 1.00 114.80 ? 391 ILE B C 1 ATOM 10187 O O . ILE B 2 391 ? -3.306 2.878 45.909 1.00 138.56 ? 391 ILE B O 1 ATOM 10188 C CB . ILE B 2 391 ? -1.232 4.771 44.638 1.00 114.22 ? 391 ILE B CB 1 ATOM 10189 C CG1 . ILE B 2 391 ? -0.615 6.167 44.533 1.00 125.23 ? 391 ILE B CG1 1 ATOM 10190 C CG2 . ILE B 2 391 ? -0.769 3.899 43.483 1.00 104.33 ? 391 ILE B CG2 1 ATOM 10191 C CD1 . ILE B 2 391 ? 0.897 6.159 44.442 1.00 121.02 ? 391 ILE B CD1 1 ATOM 10192 N N . GLY B 2 392 ? -3.880 2.921 43.732 1.00 112.01 ? 392 GLY B N 1 ATOM 10193 C CA . GLY B 2 392 ? -4.505 1.611 43.745 1.00 125.46 ? 392 GLY B CA 1 ATOM 10194 C C . GLY B 2 392 ? -6.014 1.696 43.626 1.00 118.90 ? 392 GLY B C 1 ATOM 10195 O O . GLY B 2 392 ? -6.683 0.699 43.353 1.00 106.55 ? 392 GLY B O 1 ATOM 10196 N N . ASP B 2 393 ? -6.552 2.895 43.823 1.00 123.47 ? 393 ASP B N 1 ATOM 10197 C CA . ASP B 2 393 ? -7.991 3.108 43.727 1.00 120.44 ? 393 ASP B CA 1 ATOM 10198 C C . ASP B 2 393 ? -8.445 3.157 42.274 1.00 104.45 ? 393 ASP B C 1 ATOM 10199 O O . ASP B 2 393 ? -7.683 3.537 41.384 1.00 91.74 ? 393 ASP B O 1 ATOM 10200 C CB . ASP B 2 393 ? -8.398 4.397 44.445 1.00 107.71 ? 393 ASP B CB 1 ATOM 10201 C CG . ASP B 2 393 ? -8.280 4.289 45.952 1.00 128.62 ? 393 ASP B CG 1 ATOM 10202 O OD1 . ASP B 2 393 ? -8.383 3.162 46.483 1.00 141.39 ? 393 ASP B OD1 1 ATOM 10203 O OD2 . ASP B 2 393 ? -8.089 5.337 46.605 1.00 124.51 ? 393 ASP B OD2 1 ATOM 10204 N N . THR B 2 394 ? -9.694 2.772 42.042 1.00 107.00 ? 394 THR B N 1 ATOM 10205 C CA . THR B 2 394 ? -10.251 2.759 40.699 1.00 91.95 ? 394 THR B CA 1 ATOM 10206 C C . THR B 2 394 ? -11.597 3.462 40.672 1.00 102.91 ? 394 THR B C 1 ATOM 10207 O O . THR B 2 394 ? -12.453 3.210 41.521 1.00 112.94 ? 394 THR B O 1 ATOM 10208 C CB . THR B 2 394 ? -10.426 1.328 40.176 1.00 100.53 ? 394 THR B CB 1 ATOM 10209 O OG1 . THR B 2 394 ? -9.265 0.553 40.500 1.00 120.26 ? 394 THR B OG1 1 ATOM 10210 C CG2 . THR B 2 394 ? -10.635 1.334 38.672 1.00 91.35 ? 394 THR B CG2 1 ATOM 10211 N N . VAL B 2 395 ? -11.784 4.344 39.697 1.00 88.09 ? 395 VAL B N 1 ATOM 10212 C CA . VAL B 2 395 ? -13.043 5.067 39.570 1.00 104.60 ? 395 VAL B CA 1 ATOM 10213 C C . VAL B 2 395 ? -13.672 4.884 38.192 1.00 94.89 ? 395 VAL B C 1 ATOM 10214 O O . VAL B 2 395 ? -13.006 4.479 37.239 1.00 87.50 ? 395 VAL B O 1 ATOM 10215 C CB . VAL B 2 395 ? -12.855 6.565 39.843 1.00 85.42 ? 395 VAL B CB 1 ATOM 10216 C CG1 . VAL B 2 395 ? -12.453 6.790 41.294 1.00 87.29 ? 395 VAL B CG1 1 ATOM 10217 C CG2 . VAL B 2 395 ? -11.820 7.142 38.902 1.00 82.96 ? 395 VAL B CG2 1 ATOM 10218 N N . SER B 2 396 ? -14.964 5.184 38.100 1.00 88.01 ? 396 SER B N 1 ATOM 10219 C CA . SER B 2 396 ? -15.705 5.031 36.855 1.00 84.46 ? 396 SER B CA 1 ATOM 10220 C C . SER B 2 396 ? -16.363 6.327 36.395 1.00 115.41 ? 396 SER B C 1 ATOM 10221 O O . SER B 2 396 ? -16.644 7.220 37.194 1.00 97.18 ? 396 SER B O 1 ATOM 10222 C CB . SER B 2 396 ? -16.774 3.953 37.005 1.00 86.66 ? 396 SER B CB 1 ATOM 10223 O OG . SER B 2 396 ? -17.757 4.082 35.994 1.00 98.51 ? 396 SER B OG 1 ATOM 10224 N N . PHE B 2 397 ? -16.609 6.411 35.092 1.00 104.14 ? 397 PHE B N 1 ATOM 10225 C CA . PHE B 2 397 ? -17.326 7.531 34.505 1.00 82.17 ? 397 PHE B CA 1 ATOM 10226 C C . PHE B 2 397 ? -18.309 7.024 33.462 1.00 89.34 ? 397 PHE B C 1 ATOM 10227 O O . PHE B 2 397 ? -17.962 6.175 32.641 1.00 106.06 ? 397 PHE B O 1 ATOM 10228 C CB . PHE B 2 397 ? -16.362 8.525 33.856 1.00 92.35 ? 397 PHE B CB 1 ATOM 10229 C CG . PHE B 2 397 ? -15.392 9.156 34.812 1.00 100.74 ? 397 PHE B CG 1 ATOM 10230 C CD1 . PHE B 2 397 ? -15.744 10.286 35.533 1.00 103.93 ? 397 PHE B CD1 1 ATOM 10231 C CD2 . PHE B 2 397 ? -14.119 8.636 34.971 1.00 94.89 ? 397 PHE B CD2 1 ATOM 10232 C CE1 . PHE B 2 397 ? -14.849 10.878 36.405 1.00 90.50 ? 397 PHE B CE1 1 ATOM 10233 C CE2 . PHE B 2 397 ? -13.219 9.223 35.840 1.00 102.11 ? 397 PHE B CE2 1 ATOM 10234 C CZ . PHE B 2 397 ? -13.585 10.345 36.558 1.00 100.30 ? 397 PHE B CZ 1 ATOM 10235 N N . SER B 2 398 ? -19.534 7.537 33.492 1.00 97.83 ? 398 SER B N 1 ATOM 10236 C CA . SER B 2 398 ? -20.488 7.257 32.425 1.00 96.46 ? 398 SER B CA 1 ATOM 10237 C C . SER B 2 398 ? -20.614 8.483 31.528 1.00 107.45 ? 398 SER B C 1 ATOM 10238 O O . SER B 2 398 ? -20.768 9.607 32.008 1.00 116.82 ? 398 SER B O 1 ATOM 10239 C CB . SER B 2 398 ? -21.851 6.856 32.988 1.00 89.80 ? 398 SER B CB 1 ATOM 10240 O OG . SER B 2 398 ? -22.438 7.921 33.710 1.00 108.02 ? 398 SER B OG 1 ATOM 10241 N N . ILE B 2 399 ? -20.530 8.258 30.223 1.00 95.89 ? 399 ILE B N 1 ATOM 10242 C CA . ILE B 2 399 ? -20.516 9.344 29.255 1.00 80.35 ? 399 ILE B CA 1 ATOM 10243 C C . ILE B 2 399 ? -21.639 9.177 28.242 1.00 85.33 ? 399 ILE B C 1 ATOM 10244 O O . ILE B 2 399 ? -21.939 8.061 27.829 1.00 86.34 ? 399 ILE B O 1 ATOM 10245 C CB . ILE B 2 399 ? -19.168 9.403 28.515 1.00 87.14 ? 399 ILE B CB 1 ATOM 10246 C CG1 . ILE B 2 399 ? -18.013 9.243 29.506 1.00 91.25 ? 399 ILE B CG1 1 ATOM 10247 C CG2 . ILE B 2 399 ? -19.040 10.697 27.726 1.00 103.30 ? 399 ILE B CG2 1 ATOM 10248 C CD1 . ILE B 2 399 ? -16.658 9.116 28.850 1.00 93.43 ? 399 ILE B CD1 1 ATOM 10249 N N . GLU B 2 400 ? -22.265 10.282 27.852 1.00 86.15 ? 400 GLU B N 1 ATOM 10250 C CA . GLU B 2 400 ? -23.284 10.251 26.807 1.00 87.32 ? 400 GLU B CA 1 ATOM 10251 C C . GLU B 2 400 ? -22.875 11.128 25.631 1.00 84.02 ? 400 GLU B C 1 ATOM 10252 O O . GLU B 2 400 ? -22.439 12.264 25.815 1.00 93.62 ? 400 GLU B O 1 ATOM 10253 C CB . GLU B 2 400 ? -24.640 10.701 27.353 1.00 96.46 ? 400 GLU B CB 1 ATOM 10254 C CG . GLU B 2 400 ? -25.718 10.857 26.288 1.00 101.26 ? 400 GLU B CG 1 ATOM 10255 C CD . GLU B 2 400 ? -27.053 11.301 26.863 1.00 123.16 ? 400 GLU B CD 1 ATOM 10256 O OE1 . GLU B 2 400 ? -27.665 10.517 27.620 1.00 129.36 ? 400 GLU B OE1 1 ATOM 10257 O OE2 . GLU B 2 400 ? -27.488 12.432 26.558 1.00 118.01 ? 400 GLU B OE2 1 ATOM 10258 N N . ALA B 2 401 ? -23.013 10.596 24.422 1.00 80.01 ? 401 ALA B N 1 ATOM 10259 C CA . ALA B 2 401 ? -22.691 11.354 23.220 1.00 93.12 ? 401 ALA B CA 1 ATOM 10260 C C . ALA B 2 401 ? -23.936 11.546 22.361 1.00 112.51 ? 401 ALA B C 1 ATOM 10261 O O . ALA B 2 401 ? -24.582 10.575 21.968 1.00 112.83 ? 401 ALA B O 1 ATOM 10262 C CB . ALA B 2 401 ? -21.600 10.659 22.433 1.00 93.73 ? 401 ALA B CB 1 ATOM 10263 N N . LYS B 2 402 ? -24.265 12.803 22.074 1.00 108.58 ? 402 LYS B N 1 ATOM 10264 C CA . LYS B 2 402 ? -25.470 13.133 21.319 1.00 110.57 ? 402 LYS B CA 1 ATOM 10265 C C . LYS B 2 402 ? -25.153 14.125 20.212 1.00 111.44 ? 402 LYS B C 1 ATOM 10266 O O . LYS B 2 402 ? -24.376 15.049 20.419 1.00 122.44 ? 402 LYS B O 1 ATOM 10267 C CB . LYS B 2 402 ? -26.541 13.714 22.244 1.00 126.44 ? 402 LYS B CB 1 ATOM 10268 C CG . LYS B 2 402 ? -27.896 13.922 21.583 1.00 127.82 ? 402 LYS B CG 1 ATOM 10269 C CD . LYS B 2 402 ? -28.765 14.876 22.390 1.00 126.00 ? 402 LYS B CD 1 ATOM 10270 C CE . LYS B 2 402 ? -28.829 14.470 23.854 1.00 132.78 ? 402 LYS B CE 1 ATOM 10271 N NZ . LYS B 2 402 ? -29.365 13.093 24.031 1.00 131.73 ? 402 LYS B NZ 1 ATOM 10272 N N . VAL B 2 403 ? -25.775 13.951 19.050 1.00 118.28 ? 403 VAL B N 1 ATOM 10273 C CA . VAL B 2 403 ? -25.508 14.823 17.911 1.00 134.69 ? 403 VAL B CA 1 ATOM 10274 C C . VAL B 2 403 ? -26.702 15.697 17.545 1.00 136.94 ? 403 VAL B C 1 ATOM 10275 O O . VAL B 2 403 ? -27.773 15.594 18.143 1.00 139.68 ? 403 VAL B O 1 ATOM 10276 C CB . VAL B 2 403 ? -25.120 14.009 16.664 1.00 124.89 ? 403 VAL B CB 1 ATOM 10277 C CG1 . VAL B 2 403 ? -23.924 13.139 16.954 1.00 116.40 ? 403 VAL B CG1 1 ATOM 10278 C CG2 . VAL B 2 403 ? -26.293 13.156 16.210 1.00 121.51 ? 403 VAL B CG2 1 ATOM 10279 N N . ARG B 2 404 ? -26.503 16.555 16.549 1.00 125.37 ? 404 ARG B N 1 ATOM 10280 C CA . ARG B 2 404 ? -27.589 17.330 15.963 1.00 130.07 ? 404 ARG B CA 1 ATOM 10281 C C . ARG B 2 404 ? -27.609 17.079 14.464 1.00 122.00 ? 404 ARG B C 1 ATOM 10282 O O . ARG B 2 404 ? -26.614 17.316 13.777 1.00 115.93 ? 404 ARG B O 1 ATOM 10283 C CB . ARG B 2 404 ? -27.431 18.822 16.259 1.00 131.57 ? 404 ARG B CB 1 ATOM 10284 C CG . ARG B 2 404 ? -27.567 19.180 17.727 1.00 133.92 ? 404 ARG B CG 1 ATOM 10285 C CD . ARG B 2 404 ? -27.699 20.682 17.915 1.00 138.70 ? 404 ARG B CD 1 ATOM 10286 N NE . ARG B 2 404 ? -26.636 21.412 17.233 1.00 150.99 ? 404 ARG B NE 1 ATOM 10287 C CZ . ARG B 2 404 ? -25.427 21.623 17.744 1.00 158.14 ? 404 ARG B CZ 1 ATOM 10288 N NH1 . ARG B 2 404 ? -25.122 21.157 18.948 1.00 159.63 ? 404 ARG B NH1 1 ATOM 10289 N NH2 . ARG B 2 404 ? -24.521 22.299 17.051 1.00 153.35 ? 404 ARG B NH2 1 ATOM 10290 N N . GLY B 2 405 ? -28.743 16.602 13.960 1.00 133.70 ? 405 GLY B N 1 ATOM 10291 C CA . GLY B 2 405 ? -28.815 16.132 12.590 1.00 145.93 ? 405 GLY B CA 1 ATOM 10292 C C . GLY B 2 405 ? -27.796 15.022 12.435 1.00 142.02 ? 405 GLY B C 1 ATOM 10293 O O . GLY B 2 405 ? -27.737 14.121 13.270 1.00 148.20 ? 405 GLY B O 1 ATOM 10294 N N . CYS B 2 406 ? -26.963 15.121 11.403 1.00 129.23 ? 406 CYS B N 1 ATOM 10295 C CA . CYS B 2 406 ? -25.867 14.179 11.193 1.00 129.07 ? 406 CYS B CA 1 ATOM 10296 C C . CYS B 2 406 ? -25.021 14.584 9.995 1.00 125.49 ? 406 CYS B C 1 ATOM 10297 O O . CYS B 2 406 ? -25.549 14.931 8.940 1.00 136.04 ? 406 CYS B O 1 ATOM 10298 C CB . CYS B 2 406 ? -26.397 12.756 10.988 1.00 140.84 ? 406 CYS B CB 1 ATOM 10299 S SG . CYS B 2 406 ? -27.728 12.628 9.775 1.00 188.12 ? 406 CYS B SG 1 ATOM 10300 N N . PRO B 2 407 ? -23.693 14.533 10.165 1.00 118.81 ? 407 PRO B N 1 ATOM 10301 C CA . PRO B 2 407 ? -22.697 14.879 9.147 1.00 122.17 ? 407 PRO B CA 1 ATOM 10302 C C . PRO B 2 407 ? -22.437 13.788 8.110 1.00 143.10 ? 407 PRO B C 1 ATOM 10303 O O . PRO B 2 407 ? -22.692 12.606 8.343 1.00 150.73 ? 407 PRO B O 1 ATOM 10304 C CB . PRO B 2 407 ? -21.427 15.131 9.974 1.00 107.48 ? 407 PRO B CB 1 ATOM 10305 C CG . PRO B 2 407 ? -21.890 15.285 11.387 1.00 109.71 ? 407 PRO B CG 1 ATOM 10306 C CD . PRO B 2 407 ? -23.076 14.392 11.492 1.00 119.55 ? 407 PRO B CD 1 ATOM 10307 N N . GLN B 2 408 ? -21.931 14.220 6.961 1.00 143.79 ? 408 GLN B N 1 ATOM 10308 C CA . GLN B 2 408 ? -21.378 13.350 5.929 1.00 146.64 ? 408 GLN B CA 1 ATOM 10309 C C . GLN B 2 408 ? -19.867 13.238 6.136 1.00 143.22 ? 408 GLN B C 1 ATOM 10310 O O . GLN B 2 408 ? -19.139 12.734 5.281 1.00 154.77 ? 408 GLN B O 1 ATOM 10311 C CB . GLN B 2 408 ? -21.710 13.872 4.530 1.00 148.17 ? 408 GLN B CB 1 ATOM 10312 C CG . GLN B 2 408 ? -23.201 13.871 4.204 1.00 153.12 ? 408 GLN B CG 1 ATOM 10313 C CD . GLN B 2 408 ? -23.795 12.472 4.125 1.00 163.59 ? 408 GLN B CD 1 ATOM 10314 O OE1 . GLN B 2 408 ? -23.074 11.481 4.005 1.00 169.91 ? 408 GLN B OE1 1 ATOM 10315 N NE2 . GLN B 2 408 ? -25.120 12.389 4.189 1.00 161.05 ? 408 GLN B NE2 1 ATOM 10316 N N . GLU B 2 409 ? -19.421 13.713 7.295 1.00 136.11 ? 409 GLU B N 1 ATOM 10317 C CA . GLU B 2 409 ? -18.042 14.123 7.565 1.00 144.32 ? 409 GLU B CA 1 ATOM 10318 C C . GLU B 2 409 ? -16.926 13.103 7.342 1.00 150.71 ? 409 GLU B C 1 ATOM 10319 O O . GLU B 2 409 ? -15.762 13.453 7.551 1.00 156.69 ? 409 GLU B O 1 ATOM 10320 C CB . GLU B 2 409 ? -17.939 14.606 9.014 1.00 146.02 ? 409 GLU B CB 1 ATOM 10321 C CG . GLU B 2 409 ? -18.141 16.097 9.206 1.00 151.22 ? 409 GLU B CG 1 ATOM 10322 C CD . GLU B 2 409 ? -18.130 16.491 10.670 1.00 154.72 ? 409 GLU B CD 1 ATOM 10323 O OE1 . GLU B 2 409 ? -17.928 15.599 11.522 1.00 151.73 ? 409 GLU B OE1 1 ATOM 10324 O OE2 . GLU B 2 409 ? -18.324 17.688 10.970 1.00 153.54 ? 409 GLU B OE2 1 ATOM 10325 N N . LYS B 2 410 ? -17.274 11.858 7.000 1.00 135.24 ? 410 LYS B N 1 ATOM 10326 C CA . LYS B 2 410 ? -16.304 10.768 6.774 1.00 138.80 ? 410 LYS B CA 1 ATOM 10327 C C . LYS B 2 410 ? -15.931 10.124 8.105 1.00 136.52 ? 410 LYS B C 1 ATOM 10328 O O . LYS B 2 410 ? -15.016 9.304 8.169 1.00 136.06 ? 410 LYS B O 1 ATOM 10329 C CB . LYS B 2 410 ? -15.048 11.228 6.018 1.00 149.82 ? 410 LYS B CB 1 ATOM 10330 C CG . LYS B 2 410 ? -15.320 11.779 4.625 1.00 151.84 ? 410 LYS B CG 1 ATOM 10331 C CD . LYS B 2 410 ? -15.989 10.742 3.736 1.00 142.37 ? 410 LYS B CD 1 ATOM 10332 C CE . LYS B 2 410 ? -16.212 11.282 2.333 1.00 134.19 ? 410 LYS B CE 1 ATOM 10333 N NZ . LYS B 2 410 ? -14.932 11.692 1.688 1.00 130.05 ? 410 LYS B NZ 1 ATOM 10334 N N . GLU B 2 411 ? -16.592 10.603 9.158 1.00 138.28 ? 411 GLU B N 1 ATOM 10335 C CA . GLU B 2 411 ? -16.700 9.959 10.474 1.00 146.98 ? 411 GLU B CA 1 ATOM 10336 C C . GLU B 2 411 ? -15.573 10.236 11.475 1.00 146.55 ? 411 GLU B C 1 ATOM 10337 O O . GLU B 2 411 ? -15.768 10.048 12.677 1.00 161.02 ? 411 GLU B O 1 ATOM 10338 C CB . GLU B 2 411 ? -16.817 8.435 10.286 1.00 155.78 ? 411 GLU B CB 1 ATOM 10339 C CG . GLU B 2 411 ? -15.543 7.658 10.654 1.00 156.41 ? 411 GLU B CG 1 ATOM 10340 C CD . GLU B 2 411 ? -15.239 6.514 9.706 1.00 164.39 ? 411 GLU B CD 1 ATOM 10341 O OE1 . GLU B 2 411 ? -15.857 5.439 9.843 1.00 174.48 ? 411 GLU B OE1 1 ATOM 10342 O OE2 . GLU B 2 411 ? -14.369 6.686 8.826 1.00 161.56 ? 411 GLU B OE2 1 ATOM 10343 N N . LYS B 2 412 ? -14.434 10.726 10.998 1.00 130.19 ? 412 LYS B N 1 ATOM 10344 C CA . LYS B 2 412 ? -13.341 11.181 11.864 1.00 133.55 ? 412 LYS B CA 1 ATOM 10345 C C . LYS B 2 412 ? -13.020 10.217 13.020 1.00 128.56 ? 412 LYS B C 1 ATOM 10346 O O . LYS B 2 412 ? -13.040 8.998 12.843 1.00 131.63 ? 412 LYS B O 1 ATOM 10347 C CB . LYS B 2 412 ? -13.670 12.566 12.432 1.00 124.89 ? 412 LYS B CB 1 ATOM 10348 C CG . LYS B 2 412 ? -14.369 13.504 11.450 1.00 133.84 ? 412 LYS B CG 1 ATOM 10349 C CD . LYS B 2 412 ? -13.551 13.731 10.182 1.00 145.94 ? 412 LYS B CD 1 ATOM 10350 C CE . LYS B 2 412 ? -12.255 14.476 10.465 1.00 142.89 ? 412 LYS B CE 1 ATOM 10351 N NZ . LYS B 2 412 ? -11.485 14.735 9.215 1.00 131.84 ? 412 LYS B NZ 1 ATOM 10352 N N . SER B 2 413 ? -12.764 10.794 14.197 1.00 120.38 ? 413 SER B N 1 ATOM 10353 C CA . SER B 2 413 ? -12.555 10.084 15.468 1.00 96.92 ? 413 SER B CA 1 ATOM 10354 C C . SER B 2 413 ? -12.146 11.099 16.536 1.00 98.70 ? 413 SER B C 1 ATOM 10355 O O . SER B 2 413 ? -11.752 12.218 16.207 1.00 130.56 ? 413 SER B O 1 ATOM 10356 C CB . SER B 2 413 ? -11.479 9.001 15.356 1.00 96.61 ? 413 SER B CB 1 ATOM 10357 O OG . SER B 2 413 ? -10.185 9.564 15.470 1.00 107.92 ? 413 SER B OG 1 ATOM 10358 N N . PHE B 2 414 ? -12.219 10.716 17.809 1.00 82.93 ? 414 PHE B N 1 ATOM 10359 C CA . PHE B 2 414 ? -11.735 11.592 18.876 1.00 86.89 ? 414 PHE B CA 1 ATOM 10360 C C . PHE B 2 414 ? -11.243 10.812 20.093 1.00 89.57 ? 414 PHE B C 1 ATOM 10361 O O . PHE B 2 414 ? -11.317 9.585 20.133 1.00 80.64 ? 414 PHE B O 1 ATOM 10362 C CB . PHE B 2 414 ? -12.821 12.592 19.295 1.00 84.50 ? 414 PHE B CB 1 ATOM 10363 C CG . PHE B 2 414 ? -13.944 11.989 20.094 1.00 86.06 ? 414 PHE B CG 1 ATOM 10364 C CD1 . PHE B 2 414 ? -13.921 12.014 21.478 1.00 97.35 ? 414 PHE B CD1 1 ATOM 10365 C CD2 . PHE B 2 414 ? -15.034 11.422 19.461 1.00 83.48 ? 414 PHE B CD2 1 ATOM 10366 C CE1 . PHE B 2 414 ? -14.955 11.469 22.213 1.00 82.88 ? 414 PHE B CE1 1 ATOM 10367 C CE2 . PHE B 2 414 ? -16.072 10.879 20.193 1.00 80.32 ? 414 PHE B CE2 1 ATOM 10368 C CZ . PHE B 2 414 ? -16.032 10.902 21.570 1.00 76.72 ? 414 PHE B CZ 1 ATOM 10369 N N . THR B 2 415 ? -10.754 11.539 21.091 1.00 91.90 ? 415 THR B N 1 ATOM 10370 C CA . THR B 2 415 ? -10.062 10.922 22.214 1.00 77.82 ? 415 THR B CA 1 ATOM 10371 C C . THR B 2 415 ? -10.603 11.358 23.571 1.00 90.72 ? 415 THR B C 1 ATOM 10372 O O . THR B 2 415 ? -10.773 12.547 23.831 1.00 100.35 ? 415 THR B O 1 ATOM 10373 C CB . THR B 2 415 ? -8.557 11.243 22.169 1.00 77.33 ? 415 THR B CB 1 ATOM 10374 O OG1 . THR B 2 415 ? -8.001 10.768 20.937 1.00 105.24 ? 415 THR B OG1 1 ATOM 10375 C CG2 . THR B 2 415 ? -7.832 10.592 23.333 1.00 73.81 ? 415 THR B CG2 1 ATOM 10376 N N . ILE B 2 416 ? -10.878 10.381 24.429 1.00 93.05 ? 416 ILE B N 1 ATOM 10377 C CA . ILE B 2 416 ? -11.170 10.645 25.832 1.00 80.82 ? 416 ILE B CA 1 ATOM 10378 C C . ILE B 2 416 ? -10.034 10.061 26.659 1.00 84.11 ? 416 ILE B C 1 ATOM 10379 O O . ILE B 2 416 ? -9.528 8.984 26.345 1.00 79.60 ? 416 ILE B O 1 ATOM 10380 C CB . ILE B 2 416 ? -12.516 10.045 26.268 1.00 75.18 ? 416 ILE B CB 1 ATOM 10381 C CG1 . ILE B 2 416 ? -13.640 10.563 25.368 1.00 84.79 ? 416 ILE B CG1 1 ATOM 10382 C CG2 . ILE B 2 416 ? -12.806 10.373 27.727 1.00 69.46 ? 416 ILE B CG2 1 ATOM 10383 C CD1 . ILE B 2 416 ? -15.007 10.002 25.703 1.00 83.91 ? 416 ILE B CD1 1 ATOM 10384 N N . LYS B 2 417 ? -9.652 10.751 27.727 1.00 92.59 ? 417 LYS B N 1 ATOM 10385 C CA . LYS B 2 417 ? -8.417 10.434 28.426 1.00 74.83 ? 417 LYS B CA 1 ATOM 10386 C C . LYS B 2 417 ? -8.250 11.262 29.688 1.00 82.10 ? 417 LYS B C 1 ATOM 10387 O O . LYS B 2 417 ? -8.558 12.449 29.702 1.00 108.13 ? 417 LYS B O 1 ATOM 10388 C CB . LYS B 2 417 ? -7.220 10.673 27.501 1.00 87.74 ? 417 LYS B CB 1 ATOM 10389 C CG . LYS B 2 417 ? -5.871 10.354 28.115 1.00 108.45 ? 417 LYS B CG 1 ATOM 10390 C CD . LYS B 2 417 ? -4.737 10.714 27.174 1.00 92.82 ? 417 LYS B CD 1 ATOM 10391 C CE . LYS B 2 417 ? -4.534 12.207 27.125 1.00 67.33 ? 417 LYS B CE 1 ATOM 10392 N NZ . LYS B 2 417 ? -4.161 12.718 28.466 1.00 85.25 ? 417 LYS B NZ 1 ATOM 10393 N N . PRO B 2 418 ? -7.768 10.625 30.762 1.00 90.68 ? 418 PRO B N 1 ATOM 10394 C CA . PRO B 2 418 ? -7.375 11.336 31.980 1.00 84.32 ? 418 PRO B CA 1 ATOM 10395 C C . PRO B 2 418 ? -6.088 12.121 31.755 1.00 85.18 ? 418 PRO B C 1 ATOM 10396 O O . PRO B 2 418 ? -5.249 11.696 30.961 1.00 83.17 ? 418 PRO B O 1 ATOM 10397 C CB . PRO B 2 418 ? -7.169 10.209 32.994 1.00 78.81 ? 418 PRO B CB 1 ATOM 10398 C CG . PRO B 2 418 ? -6.863 9.014 32.164 1.00 80.44 ? 418 PRO B CG 1 ATOM 10399 C CD . PRO B 2 418 ? -7.667 9.164 30.917 1.00 86.15 ? 418 PRO B CD 1 ATOM 10400 N N . VAL B 2 419 ? -5.937 13.248 32.442 1.00 85.19 ? 419 VAL B N 1 ATOM 10401 C CA . VAL B 2 419 ? -4.769 14.103 32.257 1.00 76.18 ? 419 VAL B CA 1 ATOM 10402 C C . VAL B 2 419 ? -3.504 13.488 32.852 1.00 74.79 ? 419 VAL B C 1 ATOM 10403 O O . VAL B 2 419 ? -3.547 12.817 33.884 1.00 96.73 ? 419 VAL B O 1 ATOM 10404 C CB . VAL B 2 419 ? -4.993 15.495 32.877 1.00 80.86 ? 419 VAL B CB 1 ATOM 10405 C CG1 . VAL B 2 419 ? -6.087 16.234 32.127 1.00 79.99 ? 419 VAL B CG1 1 ATOM 10406 C CG2 . VAL B 2 419 ? -5.346 15.372 34.350 1.00 100.73 ? 419 VAL B CG2 1 ATOM 10407 N N . GLY B 2 420 ? -2.377 13.712 32.185 1.00 81.64 ? 420 GLY B N 1 ATOM 10408 C CA . GLY B 2 420 ? -1.098 13.215 32.658 1.00 99.07 ? 420 GLY B CA 1 ATOM 10409 C C . GLY B 2 420 ? -0.908 11.731 32.418 1.00 101.40 ? 420 GLY B C 1 ATOM 10410 O O . GLY B 2 420 ? 0.100 11.153 32.823 1.00 129.27 ? 420 GLY B O 1 ATOM 10411 N N . PHE B 2 421 ? -1.879 11.115 31.752 1.00 84.17 ? 421 PHE B N 1 ATOM 10412 C CA . PHE B 2 421 ? -1.842 9.682 31.492 1.00 87.42 ? 421 PHE B CA 1 ATOM 10413 C C . PHE B 2 421 ? -1.572 9.359 30.029 1.00 96.54 ? 421 PHE B C 1 ATOM 10414 O O . PHE B 2 421 ? -2.036 10.059 29.128 1.00 93.77 ? 421 PHE B O 1 ATOM 10415 C CB . PHE B 2 421 ? -3.153 9.029 31.926 1.00 90.42 ? 421 PHE B CB 1 ATOM 10416 C CG . PHE B 2 421 ? -3.163 8.587 33.358 1.00 108.59 ? 421 PHE B CG 1 ATOM 10417 C CD1 . PHE B 2 421 ? -2.101 8.884 34.195 1.00 115.16 ? 421 PHE B CD1 1 ATOM 10418 C CD2 . PHE B 2 421 ? -4.223 7.853 33.862 1.00 87.27 ? 421 PHE B CD2 1 ATOM 10419 C CE1 . PHE B 2 421 ? -2.106 8.470 35.512 1.00 113.29 ? 421 PHE B CE1 1 ATOM 10420 C CE2 . PHE B 2 421 ? -4.235 7.439 35.176 1.00 92.31 ? 421 PHE B CE2 1 ATOM 10421 C CZ . PHE B 2 421 ? -3.174 7.746 36.002 1.00 115.76 ? 421 PHE B CZ 1 ATOM 10422 N N . LYS B 2 422 ? -0.822 8.286 29.803 1.00 90.39 ? 422 LYS B N 1 ATOM 10423 C CA . LYS B 2 422 ? -0.532 7.826 28.454 1.00 82.26 ? 422 LYS B CA 1 ATOM 10424 C C . LYS B 2 422 ? -1.738 7.103 27.871 1.00 87.47 ? 422 LYS B C 1 ATOM 10425 O O . LYS B 2 422 ? -2.092 7.298 26.708 1.00 106.67 ? 422 LYS B O 1 ATOM 10426 C CB . LYS B 2 422 ? 0.688 6.902 28.448 1.00 91.83 ? 422 LYS B CB 1 ATOM 10427 C CG . LYS B 2 422 ? 1.100 6.424 27.063 1.00 117.63 ? 422 LYS B CG 1 ATOM 10428 C CD . LYS B 2 422 ? 1.518 7.593 26.181 1.00 135.16 ? 422 LYS B CD 1 ATOM 10429 C CE . LYS B 2 422 ? 1.998 7.118 24.818 1.00 131.44 ? 422 LYS B CE 1 ATOM 10430 N NZ . LYS B 2 422 ? 0.931 6.396 24.071 1.00 127.13 ? 422 LYS B NZ 1 ATOM 10431 N N . ASP B 2 423 ? -2.369 6.271 28.691 1.00 91.31 ? 423 ASP B N 1 ATOM 10432 C CA . ASP B 2 423 ? -3.505 5.471 28.250 1.00 96.84 ? 423 ASP B CA 1 ATOM 10433 C C . ASP B 2 423 ? -4.726 6.340 27.984 1.00 92.43 ? 423 ASP B C 1 ATOM 10434 O O . ASP B 2 423 ? -4.910 7.376 28.624 1.00 74.30 ? 423 ASP B O 1 ATOM 10435 C CB . ASP B 2 423 ? -3.830 4.399 29.286 1.00 98.21 ? 423 ASP B CB 1 ATOM 10436 C CG . ASP B 2 423 ? -2.719 3.386 29.436 1.00 113.62 ? 423 ASP B CG 1 ATOM 10437 O OD1 . ASP B 2 423 ? -1.765 3.658 30.195 1.00 104.59 ? 423 ASP B OD1 1 ATOM 10438 O OD2 . ASP B 2 423 ? -2.798 2.322 28.787 1.00 116.31 ? 423 ASP B OD2 1 ATOM 10439 N N . SER B 2 424 ? -5.558 5.913 27.040 1.00 99.35 ? 424 SER B N 1 ATOM 10440 C CA . SER B 2 424 ? -6.699 6.718 26.623 1.00 104.84 ? 424 SER B CA 1 ATOM 10441 C C . SER B 2 424 ? -7.831 5.888 26.028 1.00 85.43 ? 424 SER B C 1 ATOM 10442 O O . SER B 2 424 ? -7.634 4.748 25.608 1.00 80.38 ? 424 SER B O 1 ATOM 10443 C CB . SER B 2 424 ? -6.256 7.771 25.605 1.00 92.32 ? 424 SER B CB 1 ATOM 10444 O OG . SER B 2 424 ? -5.776 7.164 24.418 1.00 93.76 ? 424 SER B OG 1 ATOM 10445 N N . LEU B 2 425 ? -9.017 6.484 25.993 1.00 81.11 ? 425 LEU B N 1 ATOM 10446 C CA . LEU B 2 425 ? -10.171 5.882 25.345 1.00 73.83 ? 425 LEU B CA 1 ATOM 10447 C C . LEU B 2 425 ? -10.414 6.536 23.989 1.00 78.11 ? 425 LEU B C 1 ATOM 10448 O O . LEU B 2 425 ? -10.817 7.696 23.915 1.00 97.25 ? 425 LEU B O 1 ATOM 10449 C CB . LEU B 2 425 ? -11.413 6.013 26.229 1.00 83.86 ? 425 LEU B CB 1 ATOM 10450 C CG . LEU B 2 425 ? -12.775 5.687 25.609 1.00 84.31 ? 425 LEU B CG 1 ATOM 10451 C CD1 . LEU B 2 425 ? -12.878 4.217 25.228 1.00 76.46 ? 425 LEU B CD1 1 ATOM 10452 C CD2 . LEU B 2 425 ? -13.896 6.080 26.560 1.00 76.25 ? 425 LEU B CD2 1 ATOM 10453 N N . ILE B 2 426 ? -10.164 5.792 22.917 1.00 81.16 ? 426 ILE B N 1 ATOM 10454 C CA . ILE B 2 426 ? -10.365 6.315 21.570 1.00 77.92 ? 426 ILE B CA 1 ATOM 10455 C C . ILE B 2 426 ? -11.741 5.943 21.030 1.00 77.64 ? 426 ILE B C 1 ATOM 10456 O O . ILE B 2 426 ? -12.104 4.767 20.970 1.00 91.16 ? 426 ILE B O 1 ATOM 10457 C CB . ILE B 2 426 ? -9.283 5.808 20.600 1.00 83.01 ? 426 ILE B CB 1 ATOM 10458 C CG1 . ILE B 2 426 ? -7.949 6.491 20.903 1.00 96.12 ? 426 ILE B CG1 1 ATOM 10459 C CG2 . ILE B 2 426 ? -9.690 6.069 19.160 1.00 82.83 ? 426 ILE B CG2 1 ATOM 10460 C CD1 . ILE B 2 426 ? -6.854 6.154 19.919 1.00 113.50 ? 426 ILE B CD1 1 ATOM 10461 N N . VAL B 2 427 ? -12.504 6.956 20.640 1.00 75.35 ? 427 VAL B N 1 ATOM 10462 C CA . VAL B 2 427 ? -13.855 6.743 20.146 1.00 79.79 ? 427 VAL B CA 1 ATOM 10463 C C . VAL B 2 427 ? -13.962 7.047 18.659 1.00 85.73 ? 427 VAL B C 1 ATOM 10464 O O . VAL B 2 427 ? -13.825 8.194 18.240 1.00 100.96 ? 427 VAL B O 1 ATOM 10465 C CB . VAL B 2 427 ? -14.875 7.612 20.903 1.00 79.40 ? 427 VAL B CB 1 ATOM 10466 C CG1 . VAL B 2 427 ? -16.280 7.342 20.390 1.00 76.96 ? 427 VAL B CG1 1 ATOM 10467 C CG2 . VAL B 2 427 ? -14.790 7.353 22.399 1.00 77.33 ? 427 VAL B CG2 1 ATOM 10468 N N . GLN B 2 428 ? -14.207 6.012 17.866 1.00 101.66 ? 428 GLN B N 1 ATOM 10469 C CA . GLN B 2 428 ? -14.447 6.195 16.443 1.00 94.18 ? 428 GLN B CA 1 ATOM 10470 C C . GLN B 2 428 ? -15.924 6.490 16.223 1.00 103.41 ? 428 GLN B C 1 ATOM 10471 O O . GLN B 2 428 ? -16.783 5.659 16.517 1.00 131.17 ? 428 GLN B O 1 ATOM 10472 C CB . GLN B 2 428 ? -14.018 4.955 15.657 1.00 86.55 ? 428 GLN B CB 1 ATOM 10473 C CG . GLN B 2 428 ? -12.569 4.555 15.884 1.00 85.67 ? 428 GLN B CG 1 ATOM 10474 C CD . GLN B 2 428 ? -12.205 3.250 15.205 1.00 89.99 ? 428 GLN B CD 1 ATOM 10475 O OE1 . GLN B 2 428 ? -13.073 2.527 14.714 1.00 101.70 ? 428 GLN B OE1 1 ATOM 10476 N NE2 . GLN B 2 428 ? -10.915 2.943 15.171 1.00 97.33 ? 428 GLN B NE2 1 ATOM 10477 N N . VAL B 2 429 ? -16.214 7.677 15.703 1.00 89.98 ? 429 VAL B N 1 ATOM 10478 C CA . VAL B 2 429 ? -17.592 8.107 15.501 1.00 92.11 ? 429 VAL B CA 1 ATOM 10479 C C . VAL B 2 429 ? -18.046 7.760 14.097 1.00 95.52 ? 429 VAL B C 1 ATOM 10480 O O . VAL B 2 429 ? -17.255 7.804 13.172 1.00 96.65 ? 429 VAL B O 1 ATOM 10481 C CB . VAL B 2 429 ? -17.756 9.618 15.716 1.00 93.69 ? 429 VAL B CB 1 ATOM 10482 C CG1 . VAL B 2 429 ? -19.217 9.958 15.947 1.00 110.51 ? 429 VAL B CG1 1 ATOM 10483 C CG2 . VAL B 2 429 ? -16.917 10.075 16.887 1.00 95.67 ? 429 VAL B CG2 1 ATOM 10484 N N . THR B 2 430 ? -19.311 7.391 13.942 1.00 108.68 ? 430 THR B N 1 ATOM 10485 C CA . THR B 2 430 ? -19.866 7.124 12.621 1.00 101.22 ? 430 THR B CA 1 ATOM 10486 C C . THR B 2 430 ? -21.313 7.587 12.545 1.00 108.22 ? 430 THR B C 1 ATOM 10487 O O . THR B 2 430 ? -22.047 7.525 13.530 1.00 115.73 ? 430 THR B O 1 ATOM 10488 C CB . THR B 2 430 ? -19.787 5.631 12.260 1.00 107.17 ? 430 THR B CB 1 ATOM 10489 O OG1 . THR B 2 430 ? -19.838 4.847 13.458 1.00 132.86 ? 430 THR B OG1 1 ATOM 10490 C CG2 . THR B 2 430 ? -18.494 5.330 11.532 1.00 89.51 ? 430 THR B CG2 1 ATOM 10491 N N . PHE B 2 431 ? -21.718 8.054 11.370 1.00 117.98 ? 431 PHE B N 1 ATOM 10492 C CA . PHE B 2 431 ? -23.068 8.565 11.178 1.00 120.67 ? 431 PHE B CA 1 ATOM 10493 C C . PHE B 2 431 ? -23.747 7.912 9.985 1.00 117.94 ? 431 PHE B C 1 ATOM 10494 O O . PHE B 2 431 ? -23.210 7.920 8.878 1.00 128.00 ? 431 PHE B O 1 ATOM 10495 C CB . PHE B 2 431 ? -23.051 10.081 10.973 1.00 118.72 ? 431 PHE B CB 1 ATOM 10496 C CG . PHE B 2 431 ? -22.311 10.837 12.037 1.00 105.86 ? 431 PHE B CG 1 ATOM 10497 C CD1 . PHE B 2 431 ? -20.960 11.109 11.899 1.00 106.47 ? 431 PHE B CD1 1 ATOM 10498 C CD2 . PHE B 2 431 ? -22.968 11.295 13.165 1.00 105.39 ? 431 PHE B CD2 1 ATOM 10499 C CE1 . PHE B 2 431 ? -20.278 11.814 12.871 1.00 108.53 ? 431 PHE B CE1 1 ATOM 10500 C CE2 . PHE B 2 431 ? -22.291 12.001 14.140 1.00 100.59 ? 431 PHE B CE2 1 ATOM 10501 C CZ . PHE B 2 431 ? -20.946 12.262 13.993 1.00 98.89 ? 431 PHE B CZ 1 ATOM 10502 N N . ASP B 2 432 ? -24.923 7.340 10.209 1.00 120.28 ? 432 ASP B N 1 ATOM 10503 C CA . ASP B 2 432 ? -25.765 6.933 9.094 1.00 137.05 ? 432 ASP B CA 1 ATOM 10504 C C . ASP B 2 432 ? -27.027 7.783 9.099 1.00 138.60 ? 432 ASP B C 1 ATOM 10505 O O . ASP B 2 432 ? -27.922 7.590 9.921 1.00 128.68 ? 432 ASP B O 1 ATOM 10506 C CB . ASP B 2 432 ? -26.102 5.443 9.180 1.00 135.53 ? 432 ASP B CB 1 ATOM 10507 C CG . ASP B 2 432 ? -26.417 4.998 10.593 1.00 129.88 ? 432 ASP B CG 1 ATOM 10508 O OD1 . ASP B 2 432 ? -26.159 5.776 11.535 1.00 119.08 ? 432 ASP B OD1 1 ATOM 10509 O OD2 . ASP B 2 432 ? -26.911 3.863 10.762 1.00 136.27 ? 432 ASP B OD2 1 ATOM 10510 N N . CYS B 2 433 ? -27.086 8.726 8.165 1.00 138.60 ? 433 CYS B N 1 ATOM 10511 C CA . CYS B 2 433 ? -28.191 9.670 8.091 1.00 133.52 ? 433 CYS B CA 1 ATOM 10512 C C . CYS B 2 433 ? -29.213 9.265 7.037 1.00 143.96 ? 433 CYS B C 1 ATOM 10513 O O . CYS B 2 433 ? -30.233 9.931 6.861 1.00 150.61 ? 433 CYS B O 1 ATOM 10514 C CB . CYS B 2 433 ? -27.657 11.073 7.804 1.00 136.47 ? 433 CYS B CB 1 ATOM 10515 S SG . CYS B 2 433 ? -26.271 11.546 8.867 1.00 155.76 ? 433 CYS B SG 1 ATOM 10516 N N . ASP B 2 434 ? -28.933 8.170 6.340 1.00 152.83 ? 434 ASP B N 1 ATOM 10517 C CA . ASP B 2 434 ? -29.758 7.750 5.213 1.00 157.35 ? 434 ASP B CA 1 ATOM 10518 C C . ASP B 2 434 ? -29.922 6.236 5.157 1.00 156.25 ? 434 ASP B C 1 ATOM 10519 O O . ASP B 2 434 ? -29.139 5.496 5.754 1.00 158.23 ? 434 ASP B O 1 ATOM 10520 C CB . ASP B 2 434 ? -29.151 8.263 3.906 1.00 157.65 ? 434 ASP B CB 1 ATOM 10521 C CG . ASP B 2 434 ? -27.636 8.298 3.944 1.00 160.47 ? 434 ASP B CG 1 ATOM 10522 O OD1 . ASP B 2 434 ? -27.036 7.424 4.606 1.00 156.69 ? 434 ASP B OD1 1 ATOM 10523 O OD2 . ASP B 2 434 ? -27.044 9.205 3.321 1.00 162.12 ? 434 ASP B OD2 1 ATOM 10524 N N . CYS B 2 435 ? -30.944 5.781 4.436 1.00 154.30 ? 435 CYS B N 1 ATOM 10525 C CA . CYS B 2 435 ? -31.235 4.355 4.334 1.00 157.05 ? 435 CYS B CA 1 ATOM 10526 C C . CYS B 2 435 ? -30.284 3.648 3.373 1.00 156.00 ? 435 CYS B C 1 ATOM 10527 O O . CYS B 2 435 ? -29.437 4.279 2.743 1.00 166.57 ? 435 CYS B O 1 ATOM 10528 C CB . CYS B 2 435 ? -32.683 4.135 3.889 1.00 167.03 ? 435 CYS B CB 1 ATOM 10529 S SG . CYS B 2 435 ? -33.929 4.753 5.045 1.00 210.10 ? 435 CYS B SG 1 ATOM 10530 N N . ALA B 2 436 ? -30.437 2.332 3.265 1.00 152.23 ? 436 ALA B N 1 ATOM 10531 C CA . ALA B 2 436 ? -29.569 1.517 2.422 1.00 155.47 ? 436 ALA B CA 1 ATOM 10532 C C . ALA B 2 436 ? -29.974 1.555 0.950 1.00 166.66 ? 436 ALA B C 1 ATOM 10533 O O . ALA B 2 436 ? -29.133 1.403 0.064 1.00 167.93 ? 436 ALA B O 1 ATOM 10534 C CB . ALA B 2 436 ? -29.556 0.080 2.925 1.00 153.86 ? 436 ALA B CB 1 ATOM 10535 N N . CYS B 2 437 ? -31.262 1.760 0.695 1.00 169.60 ? 437 CYS B N 1 ATOM 10536 C CA . CYS B 2 437 ? -31.812 1.632 -0.652 1.00 164.90 ? 437 CYS B CA 1 ATOM 10537 C C . CYS B 2 437 ? -31.399 2.759 -1.600 1.00 170.77 ? 437 CYS B C 1 ATOM 10538 O O . CYS B 2 437 ? -31.668 2.691 -2.799 1.00 173.68 ? 437 CYS B O 1 ATOM 10539 C CB . CYS B 2 437 ? -33.340 1.560 -0.586 1.00 160.22 ? 437 CYS B CB 1 ATOM 10540 S SG . CYS B 2 437 ? -34.127 3.053 0.063 1.00 240.12 ? 437 CYS B SG 1 ATOM 10541 N N . GLN B 2 438 ? -30.748 3.788 -1.067 1.00 169.88 ? 438 GLN B N 1 ATOM 10542 C CA . GLN B 2 438 ? -30.366 4.946 -1.874 1.00 172.23 ? 438 GLN B CA 1 ATOM 10543 C C . GLN B 2 438 ? -29.246 4.632 -2.867 1.00 176.34 ? 438 GLN B C 1 ATOM 10544 O O . GLN B 2 438 ? -29.093 5.320 -3.876 1.00 174.14 ? 438 GLN B O 1 ATOM 10545 C CB . GLN B 2 438 ? -29.943 6.106 -0.971 1.00 172.26 ? 438 GLN B CB 1 ATOM 10546 C CG . GLN B 2 438 ? -31.083 6.719 -0.173 1.00 179.51 ? 438 GLN B CG 1 ATOM 10547 C CD . GLN B 2 438 ? -30.659 7.963 0.584 1.00 182.31 ? 438 GLN B CD 1 ATOM 10548 O OE1 . GLN B 2 438 ? -31.490 8.672 1.152 1.00 183.99 ? 438 GLN B OE1 1 ATOM 10549 N NE2 . GLN B 2 438 ? -29.359 8.235 0.594 1.00 178.19 ? 438 GLN B NE2 1 ATOM 10550 N N . ALA B 2 439 ? -28.470 3.591 -2.580 1.00 179.61 ? 439 ALA B N 1 ATOM 10551 C CA . ALA B 2 439 ? -27.358 3.193 -3.440 1.00 175.44 ? 439 ALA B CA 1 ATOM 10552 C C . ALA B 2 439 ? -27.841 2.522 -4.724 1.00 176.40 ? 439 ALA B C 1 ATOM 10553 O O . ALA B 2 439 ? -27.047 2.208 -5.610 1.00 183.71 ? 439 ALA B O 1 ATOM 10554 C CB . ALA B 2 439 ? -26.415 2.268 -2.686 1.00 172.23 ? 439 ALA B CB 1 ATOM 10555 N N . GLN B 2 440 ? -29.149 2.308 -4.813 1.00 169.62 ? 440 GLN B N 1 ATOM 10556 C CA . GLN B 2 440 ? -29.750 1.561 -5.912 1.00 170.60 ? 440 GLN B CA 1 ATOM 10557 C C . GLN B 2 440 ? -30.135 2.445 -7.100 1.00 183.11 ? 440 GLN B C 1 ATOM 10558 O O . GLN B 2 440 ? -30.809 1.984 -8.023 1.00 187.99 ? 440 GLN B O 1 ATOM 10559 C CB . GLN B 2 440 ? -30.964 0.779 -5.409 1.00 164.89 ? 440 GLN B CB 1 ATOM 10560 C CG . GLN B 2 440 ? -30.581 -0.395 -4.518 1.00 163.10 ? 440 GLN B CG 1 ATOM 10561 C CD . GLN B 2 440 ? -31.779 -1.111 -3.930 1.00 173.76 ? 440 GLN B CD 1 ATOM 10562 O OE1 . GLN B 2 440 ? -32.909 -0.630 -4.015 1.00 175.35 ? 440 GLN B OE1 1 ATOM 10563 N NE2 . GLN B 2 440 ? -31.537 -2.270 -3.326 1.00 177.10 ? 440 GLN B NE2 1 ATOM 10564 N N . ALA B 2 441 ? -29.721 3.712 -7.059 1.00 186.52 ? 441 ALA B N 1 ATOM 10565 C CA . ALA B 2 441 ? -29.888 4.635 -8.187 1.00 194.56 ? 441 ALA B CA 1 ATOM 10566 C C . ALA B 2 441 ? -31.346 4.848 -8.597 1.00 204.16 ? 441 ALA B C 1 ATOM 10567 O O . ALA B 2 441 ? -32.123 5.434 -7.840 1.00 193.88 ? 441 ALA B O 1 ATOM 10568 C CB . ALA B 2 441 ? -29.072 4.154 -9.384 1.00 197.35 ? 441 ALA B CB 1 ATOM 10569 N N . GLU B 2 442 ? -31.696 4.391 -9.802 1.00 221.30 ? 442 GLU B N 1 ATOM 10570 C CA . GLU B 2 442 ? -32.986 4.687 -10.436 1.00 225.55 ? 442 GLU B CA 1 ATOM 10571 C C . GLU B 2 442 ? -33.144 6.190 -10.649 1.00 224.71 ? 442 GLU B C 1 ATOM 10572 O O . GLU B 2 442 ? -33.938 6.838 -9.967 1.00 227.70 ? 442 GLU B O 1 ATOM 10573 C CB . GLU B 2 442 ? -34.151 4.145 -9.597 1.00 220.42 ? 442 GLU B CB 1 ATOM 10574 C CG . GLU B 2 442 ? -33.958 2.723 -9.091 1.00 219.07 ? 442 GLU B CG 1 ATOM 10575 C CD . GLU B 2 442 ? -33.722 1.726 -10.207 1.00 222.74 ? 442 GLU B CD 1 ATOM 10576 O OE1 . GLU B 2 442 ? -34.311 1.893 -11.296 1.00 228.14 ? 442 GLU B OE1 1 ATOM 10577 O OE2 . GLU B 2 442 ? -32.943 0.773 -9.996 1.00 224.17 ? 442 GLU B OE2 1 ATOM 10578 N N . PRO B 2 443 ? -32.377 6.745 -11.604 1.00 219.03 ? 443 PRO B N 1 ATOM 10579 C CA . PRO B 2 443 ? -32.167 8.196 -11.689 1.00 211.12 ? 443 PRO B CA 1 ATOM 10580 C C . PRO B 2 443 ? -33.418 9.053 -11.901 1.00 208.55 ? 443 PRO B C 1 ATOM 10581 O O . PRO B 2 443 ? -33.604 9.980 -11.112 1.00 199.35 ? 443 PRO B O 1 ATOM 10582 C CB . PRO B 2 443 ? -31.229 8.335 -12.896 1.00 210.12 ? 443 PRO B CB 1 ATOM 10583 C CG . PRO B 2 443 ? -31.477 7.112 -13.715 1.00 209.02 ? 443 PRO B CG 1 ATOM 10584 C CD . PRO B 2 443 ? -31.744 6.025 -12.723 1.00 211.68 ? 443 PRO B CD 1 ATOM 10585 N N . ASN B 2 444 ? -34.251 8.790 -12.908 1.00 215.29 ? 444 ASN B N 1 ATOM 10586 C CA . ASN B 2 444 ? -35.519 9.519 -12.968 1.00 213.33 ? 444 ASN B CA 1 ATOM 10587 C C . ASN B 2 444 ? -36.800 8.762 -13.351 1.00 208.13 ? 444 ASN B C 1 ATOM 10588 O O . ASN B 2 444 ? -37.591 8.401 -12.484 1.00 206.01 ? 444 ASN B O 1 ATOM 10589 C CB . ASN B 2 444 ? -35.364 10.716 -13.917 1.00 216.13 ? 444 ASN B CB 1 ATOM 10590 C CG . ASN B 2 444 ? -34.647 10.358 -15.202 1.00 214.90 ? 444 ASN B CG 1 ATOM 10591 O OD1 . ASN B 2 444 ? -34.636 9.201 -15.621 1.00 211.27 ? 444 ASN B OD1 1 ATOM 10592 N ND2 . ASN B 2 444 ? -34.043 11.356 -15.838 1.00 213.87 ? 444 ASN B ND2 1 ATOM 10593 N N . SER B 2 445 ? -36.966 8.467 -14.639 1.00 205.67 ? 445 SER B N 1 ATOM 10594 C CA . SER B 2 445 ? -38.310 8.310 -15.208 1.00 210.41 ? 445 SER B CA 1 ATOM 10595 C C . SER B 2 445 ? -39.191 7.258 -14.536 1.00 218.04 ? 445 SER B C 1 ATOM 10596 O O . SER B 2 445 ? -40.089 7.602 -13.766 1.00 219.52 ? 445 SER B O 1 ATOM 10597 C CB . SER B 2 445 ? -38.203 7.984 -16.699 1.00 209.32 ? 445 SER B CB 1 ATOM 10598 O OG . SER B 2 445 ? -39.488 7.860 -17.284 1.00 211.28 ? 445 SER B OG 1 ATOM 10599 N N . HIS B 2 446 ? -38.909 5.988 -14.813 1.00 227.89 ? 446 HIS B N 1 ATOM 10600 C CA . HIS B 2 446 ? -39.583 4.857 -14.173 1.00 224.19 ? 446 HIS B CA 1 ATOM 10601 C C . HIS B 2 446 ? -41.107 4.991 -14.076 1.00 223.74 ? 446 HIS B C 1 ATOM 10602 O O . HIS B 2 446 ? -41.793 5.159 -15.085 1.00 220.61 ? 446 HIS B O 1 ATOM 10603 C CB . HIS B 2 446 ? -38.987 4.626 -12.785 1.00 215.18 ? 446 HIS B CB 1 ATOM 10604 C CG . HIS B 2 446 ? -37.548 4.213 -12.818 1.00 218.85 ? 446 HIS B CG 1 ATOM 10605 N ND1 . HIS B 2 446 ? -36.813 4.176 -13.983 1.00 219.86 ? 446 HIS B ND1 1 ATOM 10606 C CD2 . HIS B 2 446 ? -36.710 3.815 -11.832 1.00 219.25 ? 446 HIS B CD2 1 ATOM 10607 C CE1 . HIS B 2 446 ? -35.583 3.777 -13.714 1.00 222.59 ? 446 HIS B CE1 1 ATOM 10608 N NE2 . HIS B 2 446 ? -35.495 3.550 -12.417 1.00 221.91 ? 446 HIS B NE2 1 ATOM 10609 N N . ARG B 2 447 ? -41.622 4.916 -12.852 1.00 223.13 ? 447 ARG B N 1 ATOM 10610 C CA . ARG B 2 447 ? -43.062 4.886 -12.606 1.00 221.24 ? 447 ARG B CA 1 ATOM 10611 C C . ARG B 2 447 ? -43.747 6.233 -12.836 1.00 220.49 ? 447 ARG B C 1 ATOM 10612 O O . ARG B 2 447 ? -44.972 6.304 -12.928 1.00 213.01 ? 447 ARG B O 1 ATOM 10613 C CB . ARG B 2 447 ? -43.335 4.412 -11.178 1.00 214.73 ? 447 ARG B CB 1 ATOM 10614 C CG . ARG B 2 447 ? -42.544 3.178 -10.779 1.00 214.51 ? 447 ARG B CG 1 ATOM 10615 C CD . ARG B 2 447 ? -42.855 2.755 -9.354 1.00 210.66 ? 447 ARG B CD 1 ATOM 10616 N NE . ARG B 2 447 ? -41.990 1.666 -8.910 1.00 212.28 ? 447 ARG B NE 1 ATOM 10617 C CZ . ARG B 2 447 ? -42.255 0.377 -9.098 1.00 215.90 ? 447 ARG B CZ 1 ATOM 10618 N NH1 . ARG B 2 447 ? -43.364 0.010 -9.726 1.00 217.30 ? 447 ARG B NH1 1 ATOM 10619 N NH2 . ARG B 2 447 ? -41.409 -0.545 -8.659 1.00 216.06 ? 447 ARG B NH2 1 ATOM 10620 N N . CYS B 2 448 ? -42.955 7.297 -12.929 1.00 229.56 ? 448 CYS B N 1 ATOM 10621 C CA . CYS B 2 448 ? -43.496 8.639 -13.128 1.00 229.84 ? 448 CYS B CA 1 ATOM 10622 C C . CYS B 2 448 ? -43.639 8.964 -14.613 1.00 229.03 ? 448 CYS B C 1 ATOM 10623 O O . CYS B 2 448 ? -43.996 10.084 -14.981 1.00 228.86 ? 448 CYS B O 1 ATOM 10624 C CB . CYS B 2 448 ? -42.614 9.682 -12.438 1.00 230.82 ? 448 CYS B CB 1 ATOM 10625 S SG . CYS B 2 448 ? -42.620 9.591 -10.628 1.00 268.13 ? 448 CYS B SG 1 ATOM 10626 N N . ASN B 2 449 ? -43.349 7.972 -15.451 1.00 224.66 ? 449 ASN B N 1 ATOM 10627 C CA . ASN B 2 449 ? -43.464 8.084 -16.905 1.00 225.54 ? 449 ASN B CA 1 ATOM 10628 C C . ASN B 2 449 ? -42.655 9.234 -17.499 1.00 225.40 ? 449 ASN B C 1 ATOM 10629 O O . ASN B 2 449 ? -41.519 9.481 -17.095 1.00 219.59 ? 449 ASN B O 1 ATOM 10630 C CB . ASN B 2 449 ? -44.934 8.231 -17.309 1.00 226.72 ? 449 ASN B CB 1 ATOM 10631 C CG . ASN B 2 449 ? -45.771 7.032 -16.912 1.00 223.46 ? 449 ASN B CG 1 ATOM 10632 O OD1 . ASN B 2 449 ? -45.260 5.919 -16.781 1.00 218.93 ? 449 ASN B OD1 1 ATOM 10633 N ND2 . ASN B 2 449 ? -47.067 7.252 -16.720 1.00 226.59 ? 449 ASN B ND2 1 ATOM 10634 N N . ASN B 2 450 ? -43.253 9.937 -18.457 1.00 228.31 ? 450 ASN B N 1 ATOM 10635 C CA . ASN B 2 450 ? -42.566 11.009 -19.170 1.00 230.06 ? 450 ASN B CA 1 ATOM 10636 C C . ASN B 2 450 ? -42.626 12.334 -18.419 1.00 231.25 ? 450 ASN B C 1 ATOM 10637 O O . ASN B 2 450 ? -43.157 12.404 -17.310 1.00 225.57 ? 450 ASN B O 1 ATOM 10638 C CB . ASN B 2 450 ? -43.153 11.173 -20.573 1.00 227.84 ? 450 ASN B CB 1 ATOM 10639 C CG . ASN B 2 450 ? -42.151 10.849 -21.665 1.00 231.46 ? 450 ASN B CG 1 ATOM 10640 O OD1 . ASN B 2 450 ? -41.019 10.453 -21.386 1.00 231.04 ? 450 ASN B OD1 1 ATOM 10641 N ND2 . ASN B 2 450 ? -42.566 11.009 -22.917 1.00 231.91 ? 450 ASN B ND2 1 ATOM 10642 N N . GLY B 2 451 ? -42.083 13.383 -19.031 1.00 233.69 ? 451 GLY B N 1 ATOM 10643 C CA . GLY B 2 451 ? -41.975 14.672 -18.372 1.00 237.77 ? 451 GLY B CA 1 ATOM 10644 C C . GLY B 2 451 ? -41.034 14.562 -17.189 1.00 245.26 ? 451 GLY B C 1 ATOM 10645 O O . GLY B 2 451 ? -41.393 14.906 -16.062 1.00 243.24 ? 451 GLY B O 1 ATOM 10646 N N . ASN B 2 452 ? -39.827 14.073 -17.463 1.00 253.16 ? 452 ASN B N 1 ATOM 10647 C CA . ASN B 2 452 ? -38.837 13.740 -16.441 1.00 251.66 ? 452 ASN B CA 1 ATOM 10648 C C . ASN B 2 452 ? -39.400 12.781 -15.395 1.00 241.21 ? 452 ASN B C 1 ATOM 10649 O O . ASN B 2 452 ? -40.162 11.871 -15.725 1.00 242.10 ? 452 ASN B O 1 ATOM 10650 C CB . ASN B 2 452 ? -38.314 15.009 -15.760 1.00 252.23 ? 452 ASN B CB 1 ATOM 10651 C CG . ASN B 2 452 ? -37.723 16.001 -16.745 1.00 260.66 ? 452 ASN B CG 1 ATOM 10652 O OD1 . ASN B 2 452 ? -37.211 15.620 -17.797 1.00 264.80 ? 452 ASN B OD1 1 ATOM 10653 N ND2 . ASN B 2 452 ? -37.791 17.283 -16.405 1.00 260.57 ? 452 ASN B ND2 1 ATOM 10654 N N . GLY B 2 453 ? -39.021 12.984 -14.137 1.00 231.92 ? 453 GLY B N 1 ATOM 10655 C CA . GLY B 2 453 ? -39.540 12.178 -13.047 1.00 221.23 ? 453 GLY B CA 1 ATOM 10656 C C . GLY B 2 453 ? -38.485 11.912 -11.990 1.00 220.32 ? 453 GLY B C 1 ATOM 10657 O O . GLY B 2 453 ? -37.445 12.571 -11.969 1.00 217.96 ? 453 GLY B O 1 ATOM 10658 N N . THR B 2 454 ? -38.760 10.926 -11.135 1.00 221.86 ? 454 THR B N 1 ATOM 10659 C CA . THR B 2 454 ? -37.772 10.327 -10.235 1.00 221.46 ? 454 THR B CA 1 ATOM 10660 C C . THR B 2 454 ? -38.431 9.176 -9.473 1.00 211.35 ? 454 THR B C 1 ATOM 10661 O O . THR B 2 454 ? -39.648 9.151 -9.305 1.00 210.45 ? 454 THR B O 1 ATOM 10662 C CB . THR B 2 454 ? -37.177 11.375 -9.240 1.00 194.10 ? 454 THR B CB 1 ATOM 10663 O OG1 . THR B 2 454 ? -35.805 11.625 -9.574 1.00 195.12 ? 454 THR B OG1 1 ATOM 10664 C CG2 . THR B 2 454 ? -37.260 10.912 -7.788 1.00 186.44 ? 454 THR B CG2 1 ATOM 10665 N N . PHE B 2 455 ? -37.623 8.219 -9.022 1.00 206.82 ? 455 PHE B N 1 ATOM 10666 C CA . PHE B 2 455 ? -38.094 7.165 -8.136 1.00 200.37 ? 455 PHE B CA 1 ATOM 10667 C C . PHE B 2 455 ? -36.995 6.819 -7.142 1.00 191.28 ? 455 PHE B C 1 ATOM 10668 O O . PHE B 2 455 ? -35.860 6.555 -7.536 1.00 194.39 ? 455 PHE B O 1 ATOM 10669 C CB . PHE B 2 455 ? -38.513 5.933 -8.939 1.00 217.29 ? 455 PHE B CB 1 ATOM 10670 C CG . PHE B 2 455 ? -38.963 4.778 -8.091 1.00 218.51 ? 455 PHE B CG 1 ATOM 10671 C CD1 . PHE B 2 455 ? -40.220 4.776 -7.510 1.00 210.99 ? 455 PHE B CD1 1 ATOM 10672 C CD2 . PHE B 2 455 ? -38.132 3.689 -7.885 1.00 218.00 ? 455 PHE B CD2 1 ATOM 10673 C CE1 . PHE B 2 455 ? -40.637 3.713 -6.733 1.00 203.63 ? 455 PHE B CE1 1 ATOM 10674 C CE2 . PHE B 2 455 ? -38.543 2.623 -7.110 1.00 210.90 ? 455 PHE B CE2 1 ATOM 10675 C CZ . PHE B 2 455 ? -39.797 2.634 -6.535 1.00 204.74 ? 455 PHE B CZ 1 ATOM 10676 N N . GLU B 2 456 ? -37.327 6.816 -5.856 1.00 185.96 ? 456 GLU B N 1 ATOM 10677 C CA . GLU B 2 456 ? -36.335 6.513 -4.831 1.00 190.29 ? 456 GLU B CA 1 ATOM 10678 C C . GLU B 2 456 ? -36.915 5.725 -3.662 1.00 186.06 ? 456 GLU B C 1 ATOM 10679 O O . GLU B 2 456 ? -37.940 6.106 -3.097 1.00 189.15 ? 456 GLU B O 1 ATOM 10680 C CB . GLU B 2 456 ? -35.699 7.807 -4.319 1.00 195.80 ? 456 GLU B CB 1 ATOM 10681 C CG . GLU B 2 456 ? -34.646 7.604 -3.241 1.00 191.24 ? 456 GLU B CG 1 ATOM 10682 C CD . GLU B 2 456 ? -34.038 8.911 -2.766 1.00 184.89 ? 456 GLU B CD 1 ATOM 10683 O OE1 . GLU B 2 456 ? -34.439 9.978 -3.278 1.00 184.37 ? 456 GLU B OE1 1 ATOM 10684 O OE2 . GLU B 2 456 ? -33.159 8.871 -1.880 1.00 178.63 ? 456 GLU B OE2 1 ATOM 10685 N N . CYS B 2 457 ? -36.244 4.632 -3.305 1.00 185.75 ? 457 CYS B N 1 ATOM 10686 C CA . CYS B 2 457 ? -36.554 3.857 -2.102 1.00 187.96 ? 457 CYS B CA 1 ATOM 10687 C C . CYS B 2 457 ? -38.021 3.448 -1.978 1.00 185.68 ? 457 CYS B C 1 ATOM 10688 O O . CYS B 2 457 ? -38.543 3.326 -0.870 1.00 179.64 ? 457 CYS B O 1 ATOM 10689 C CB . CYS B 2 457 ? -36.141 4.644 -0.854 1.00 186.10 ? 457 CYS B CB 1 ATOM 10690 S SG . CYS B 2 457 ? -34.361 4.924 -0.694 1.00 208.82 ? 457 CYS B SG 1 ATOM 10691 N N . GLY B 2 458 ? -38.681 3.233 -3.111 1.00 187.37 ? 458 GLY B N 1 ATOM 10692 C CA . GLY B 2 458 ? -40.071 2.813 -3.105 1.00 186.76 ? 458 GLY B CA 1 ATOM 10693 C C . GLY B 2 458 ? -41.062 3.960 -3.163 1.00 192.65 ? 458 GLY B C 1 ATOM 10694 O O . GLY B 2 458 ? -42.250 3.772 -2.902 1.00 191.66 ? 458 GLY B O 1 ATOM 10695 N N . VAL B 2 459 ? -40.581 5.150 -3.508 1.00 201.70 ? 459 VAL B N 1 ATOM 10696 C CA . VAL B 2 459 ? -41.449 6.321 -3.607 1.00 201.11 ? 459 VAL B CA 1 ATOM 10697 C C . VAL B 2 459 ? -40.965 7.265 -4.709 1.00 204.15 ? 459 VAL B C 1 ATOM 10698 O O . VAL B 2 459 ? -39.821 7.177 -5.159 1.00 206.29 ? 459 VAL B O 1 ATOM 10699 C CB . VAL B 2 459 ? -41.529 7.079 -2.259 1.00 193.98 ? 459 VAL B CB 1 ATOM 10700 C CG1 . VAL B 2 459 ? -40.353 8.032 -2.105 1.00 200.16 ? 459 VAL B CG1 1 ATOM 10701 C CG2 . VAL B 2 459 ? -42.850 7.830 -2.140 1.00 189.57 ? 459 VAL B CG2 1 ATOM 10702 N N . CYS B 2 460 ? -41.847 8.157 -5.148 1.00 202.63 ? 460 CYS B N 1 ATOM 10703 C CA . CYS B 2 460 ? -41.535 9.086 -6.228 1.00 207.86 ? 460 CYS B CA 1 ATOM 10704 C C . CYS B 2 460 ? -41.666 10.546 -5.795 1.00 208.27 ? 460 CYS B C 1 ATOM 10705 O O . CYS B 2 460 ? -42.766 11.021 -5.513 1.00 209.11 ? 460 CYS B O 1 ATOM 10706 C CB . CYS B 2 460 ? -42.447 8.810 -7.428 1.00 208.79 ? 460 CYS B CB 1 ATOM 10707 S SG . CYS B 2 460 ? -42.509 10.123 -8.669 1.00 263.98 ? 460 CYS B SG 1 ATOM 10708 N N . ARG B 2 461 ? -40.540 11.252 -5.743 1.00 206.36 ? 461 ARG B N 1 ATOM 10709 C CA . ARG B 2 461 ? -40.547 12.695 -5.520 1.00 198.61 ? 461 ARG B CA 1 ATOM 10710 C C . ARG B 2 461 ? -40.097 13.379 -6.804 1.00 195.06 ? 461 ARG B C 1 ATOM 10711 O O . ARG B 2 461 ? -38.912 13.375 -7.123 1.00 190.01 ? 461 ARG B O 1 ATOM 10712 C CB . ARG B 2 461 ? -39.620 13.077 -4.364 1.00 191.69 ? 461 ARG B CB 1 ATOM 10713 C CG . ARG B 2 461 ? -39.622 12.104 -3.196 1.00 183.18 ? 461 ARG B CG 1 ATOM 10714 C CD . ARG B 2 461 ? -38.205 11.860 -2.689 1.00 180.80 ? 461 ARG B CD 1 ATOM 10715 N NE . ARG B 2 461 ? -37.507 13.104 -2.376 1.00 183.83 ? 461 ARG B NE 1 ATOM 10716 C CZ . ARG B 2 461 ? -36.229 13.175 -2.016 1.00 183.69 ? 461 ARG B CZ 1 ATOM 10717 N NH1 . ARG B 2 461 ? -35.501 12.071 -1.924 1.00 186.72 ? 461 ARG B NH1 1 ATOM 10718 N NH2 . ARG B 2 461 ? -35.677 14.352 -1.749 1.00 178.76 ? 461 ARG B NH2 1 ATOM 10719 N N . CYS B 2 462 ? -41.021 14.006 -7.522 1.00 199.41 ? 462 CYS B N 1 ATOM 10720 C CA . CYS B 2 462 ? -40.718 14.401 -8.894 1.00 211.71 ? 462 CYS B CA 1 ATOM 10721 C C . CYS B 2 462 ? -41.133 15.818 -9.272 1.00 219.46 ? 462 CYS B C 1 ATOM 10722 O O . CYS B 2 462 ? -42.251 16.241 -9.002 1.00 223.45 ? 462 CYS B O 1 ATOM 10723 C CB . CYS B 2 462 ? -41.376 13.417 -9.867 1.00 216.58 ? 462 CYS B CB 1 ATOM 10724 S SG . CYS B 2 462 ? -43.191 13.394 -9.825 1.00 247.00 ? 462 CYS B SG 1 ATOM 10725 N N . GLY B 2 463 ? -40.209 16.548 -9.888 1.00 223.65 ? 463 GLY B N 1 ATOM 10726 C CA . GLY B 2 463 ? -40.541 17.753 -10.628 1.00 225.64 ? 463 GLY B CA 1 ATOM 10727 C C . GLY B 2 463 ? -40.797 19.033 -9.856 1.00 221.66 ? 463 GLY B C 1 ATOM 10728 O O . GLY B 2 463 ? -41.115 19.003 -8.667 1.00 215.83 ? 463 GLY B O 1 ATOM 10729 N N . PRO B 2 464 ? -40.651 20.176 -10.546 1.00 223.24 ? 464 PRO B N 1 ATOM 10730 C CA . PRO B 2 464 ? -40.972 21.540 -10.111 1.00 224.36 ? 464 PRO B CA 1 ATOM 10731 C C . PRO B 2 464 ? -42.450 21.881 -10.302 1.00 226.96 ? 464 PRO B C 1 ATOM 10732 O O . PRO B 2 464 ? -42.824 22.462 -11.321 1.00 221.84 ? 464 PRO B O 1 ATOM 10733 C CB . PRO B 2 464 ? -40.094 22.420 -11.014 1.00 227.10 ? 464 PRO B CB 1 ATOM 10734 C CG . PRO B 2 464 ? -39.144 21.476 -11.701 1.00 230.03 ? 464 PRO B CG 1 ATOM 10735 C CD . PRO B 2 464 ? -39.889 20.191 -11.803 1.00 226.37 ? 464 PRO B CD 1 ATOM 10736 N N . GLY B 2 465 ? -43.275 21.515 -9.329 1.00 230.71 ? 465 GLY B N 1 ATOM 10737 C CA . GLY B 2 465 ? -44.705 21.759 -9.392 1.00 237.61 ? 465 GLY B CA 1 ATOM 10738 C C . GLY B 2 465 ? -45.502 20.502 -9.676 1.00 241.84 ? 465 GLY B C 1 ATOM 10739 O O . GLY B 2 465 ? -46.676 20.418 -9.322 1.00 244.76 ? 465 GLY B O 1 ATOM 10740 N N . TRP B 2 466 ? -44.866 19.511 -10.289 1.00 243.11 ? 466 TRP B N 1 ATOM 10741 C CA . TRP B 2 466 ? -45.433 18.170 -10.306 1.00 237.10 ? 466 TRP B CA 1 ATOM 10742 C C . TRP B 2 466 ? -45.191 17.604 -8.917 1.00 231.72 ? 466 TRP B C 1 ATOM 10743 O O . TRP B 2 466 ? -44.160 17.884 -8.311 1.00 237.54 ? 466 TRP B O 1 ATOM 10744 C CB . TRP B 2 466 ? -44.805 17.302 -11.396 1.00 235.73 ? 466 TRP B CB 1 ATOM 10745 C CG . TRP B 2 466 ? -45.443 17.491 -12.738 1.00 242.78 ? 466 TRP B CG 1 ATOM 10746 C CD1 . TRP B 2 466 ? -46.477 16.771 -13.261 1.00 245.21 ? 466 TRP B CD1 1 ATOM 10747 C CD2 . TRP B 2 466 ? -45.098 18.471 -13.726 1.00 254.66 ? 466 TRP B CD2 1 ATOM 10748 N NE1 . TRP B 2 466 ? -46.794 17.236 -14.513 1.00 256.72 ? 466 TRP B NE1 1 ATOM 10749 C CE2 . TRP B 2 466 ? -45.963 18.280 -14.822 1.00 260.53 ? 466 TRP B CE2 1 ATOM 10750 C CE3 . TRP B 2 466 ? -44.142 19.489 -13.790 1.00 260.29 ? 466 TRP B CE3 1 ATOM 10751 C CZ2 . TRP B 2 466 ? -45.900 19.069 -15.970 1.00 264.48 ? 466 TRP B CZ2 1 ATOM 10752 C CZ3 . TRP B 2 466 ? -44.081 20.271 -14.930 1.00 270.47 ? 466 TRP B CZ3 1 ATOM 10753 C CH2 . TRP B 2 466 ? -44.954 20.057 -16.004 1.00 269.95 ? 466 TRP B CH2 1 ATOM 10754 N N . LEU B 2 467 ? -46.142 16.845 -8.386 1.00 222.75 ? 467 LEU B N 1 ATOM 10755 C CA . LEU B 2 467 ? -46.088 16.508 -6.967 1.00 222.29 ? 467 LEU B CA 1 ATOM 10756 C C . LEU B 2 467 ? -46.222 15.021 -6.640 1.00 222.19 ? 467 LEU B C 1 ATOM 10757 O O . LEU B 2 467 ? -45.254 14.382 -6.226 1.00 220.46 ? 467 LEU B O 1 ATOM 10758 C CB . LEU B 2 467 ? -47.178 17.285 -6.221 1.00 222.11 ? 467 LEU B CB 1 ATOM 10759 C CG . LEU B 2 467 ? -46.789 18.547 -5.441 1.00 219.15 ? 467 LEU B CG 1 ATOM 10760 C CD1 . LEU B 2 467 ? -45.961 19.512 -6.271 1.00 220.79 ? 467 LEU B CD1 1 ATOM 10761 C CD2 . LEU B 2 467 ? -48.039 19.241 -4.938 1.00 223.15 ? 467 LEU B CD2 1 ATOM 10762 N N . GLY B 2 468 ? -47.419 14.477 -6.836 1.00 219.86 ? 468 GLY B N 1 ATOM 10763 C CA . GLY B 2 468 ? -47.773 13.179 -6.285 1.00 214.25 ? 468 GLY B CA 1 ATOM 10764 C C . GLY B 2 468 ? -47.028 11.976 -6.828 1.00 210.95 ? 468 GLY B C 1 ATOM 10765 O O . GLY B 2 468 ? -46.186 12.101 -7.719 1.00 213.23 ? 468 GLY B O 1 ATOM 10766 N N . SER B 2 469 ? -47.337 10.807 -6.266 1.00 201.49 ? 469 SER B N 1 ATOM 10767 C CA . SER B 2 469 ? -46.787 9.538 -6.731 1.00 201.49 ? 469 SER B CA 1 ATOM 10768 C C . SER B 2 469 ? -47.036 9.394 -8.225 1.00 212.42 ? 469 SER B C 1 ATOM 10769 O O . SER B 2 469 ? -46.167 8.946 -8.974 1.00 212.32 ? 469 SER B O 1 ATOM 10770 C CB . SER B 2 469 ? -47.403 8.366 -5.965 1.00 190.76 ? 469 SER B CB 1 ATOM 10771 O OG . SER B 2 469 ? -48.816 8.376 -6.072 1.00 187.39 ? 469 SER B OG 1 ATOM 10772 N N . GLN B 2 470 ? -48.235 9.778 -8.648 1.00 223.78 ? 470 GLN B N 1 ATOM 10773 C CA . GLN B 2 470 ? -48.493 10.031 -10.055 1.00 236.02 ? 470 GLN B CA 1 ATOM 10774 C C . GLN B 2 470 ? -48.355 11.539 -10.263 1.00 235.88 ? 470 GLN B C 1 ATOM 10775 O O . GLN B 2 470 ? -48.925 12.335 -9.515 1.00 240.43 ? 470 GLN B O 1 ATOM 10776 C CB . GLN B 2 470 ? -49.875 9.507 -10.482 1.00 238.17 ? 470 GLN B CB 1 ATOM 10777 C CG . GLN B 2 470 ? -51.086 10.324 -10.025 1.00 239.39 ? 470 GLN B CG 1 ATOM 10778 C CD . GLN B 2 470 ? -51.287 10.315 -8.520 1.00 233.56 ? 470 GLN B CD 1 ATOM 10779 O OE1 . GLN B 2 470 ? -50.739 9.471 -7.811 1.00 228.24 ? 470 GLN B OE1 1 ATOM 10780 N NE2 . GLN B 2 470 ? -52.080 11.259 -8.026 1.00 233.04 ? 470 GLN B NE2 1 ATOM 10781 N N . CYS B 2 471 ? -47.558 11.934 -11.249 1.00 229.25 ? 471 CYS B N 1 ATOM 10782 C CA . CYS B 2 471 ? -47.275 13.349 -11.456 1.00 226.93 ? 471 CYS B CA 1 ATOM 10783 C C . CYS B 2 471 ? -48.448 14.052 -12.134 1.00 224.82 ? 471 CYS B C 1 ATOM 10784 O O . CYS B 2 471 ? -48.877 13.663 -13.219 1.00 214.94 ? 471 CYS B O 1 ATOM 10785 C CB . CYS B 2 471 ? -45.993 13.523 -12.273 1.00 226.69 ? 471 CYS B CB 1 ATOM 10786 S SG . CYS B 2 471 ? -44.483 13.092 -11.366 1.00 248.45 ? 471 CYS B SG 1 ATOM 10787 N N . GLU B 2 472 ? -48.961 15.089 -11.476 1.00 232.09 ? 472 GLU B N 1 ATOM 10788 C CA . GLU B 2 472 ? -50.160 15.788 -11.930 1.00 239.97 ? 472 GLU B CA 1 ATOM 10789 C C . GLU B 2 472 ? -50.218 17.218 -11.396 1.00 240.56 ? 472 GLU B C 1 ATOM 10790 O O . GLU B 2 472 ? -49.229 17.734 -10.872 1.00 242.09 ? 472 GLU B O 1 ATOM 10791 C CB . GLU B 2 472 ? -51.416 15.026 -11.503 1.00 241.15 ? 472 GLU B CB 1 ATOM 10792 C CG . GLU B 2 472 ? -51.484 14.740 -10.012 1.00 238.39 ? 472 GLU B CG 1 ATOM 10793 C CD . GLU B 2 472 ? -52.902 14.537 -9.519 1.00 238.90 ? 472 GLU B CD 1 ATOM 10794 O OE1 . GLU B 2 472 ? -53.845 14.785 -10.299 1.00 244.94 ? 472 GLU B OE1 1 ATOM 10795 O OE2 . GLU B 2 472 ? -53.074 14.133 -8.349 1.00 230.90 ? 472 GLU B OE2 1 ATOM 10796 N N . CYS B 2 473 ? -51.384 17.846 -11.543 1.00 236.84 ? 473 CYS B N 1 ATOM 10797 C CA . CYS B 2 473 ? -51.648 19.180 -10.999 1.00 234.63 ? 473 CYS B CA 1 ATOM 10798 C C . CYS B 2 473 ? -50.688 20.251 -11.514 1.00 226.70 ? 473 CYS B C 1 ATOM 10799 O O . CYS B 2 473 ? -50.695 20.578 -12.702 1.00 221.76 ? 473 CYS B O 1 ATOM 10800 C CB . CYS B 2 473 ? -51.606 19.145 -9.468 1.00 231.81 ? 473 CYS B CB 1 ATOM 10801 S SG . CYS B 2 473 ? -52.842 18.062 -8.712 1.00 259.81 ? 473 CYS B SG 1 ATOM 10802 N N . SER B 2 474 ? -49.894 20.805 -10.598 1.00 227.95 ? 474 SER B N 1 ATOM 10803 C CA . SER B 2 474 ? -48.980 21.918 -10.867 1.00 240.78 ? 474 SER B CA 1 ATOM 10804 C C . SER B 2 474 ? -49.723 23.200 -11.231 1.00 250.08 ? 474 SER B C 1 ATOM 10805 O O . SER B 2 474 ? -49.348 23.899 -12.173 1.00 256.83 ? 474 SER B O 1 ATOM 10806 C CB . SER B 2 474 ? -47.986 21.559 -11.977 1.00 246.41 ? 474 SER B CB 1 ATOM 10807 O OG . SER B 2 474 ? -47.051 22.606 -12.180 1.00 251.61 ? 474 SER B OG 1 ATOM 10808 N N . GLU B 2 475 ? -50.771 23.494 -10.465 1.00 247.08 ? 475 GLU B N 1 ATOM 10809 C CA . GLU B 2 475 ? -51.521 24.746 -10.570 1.00 255.25 ? 475 GLU B CA 1 ATOM 10810 C C . GLU B 2 475 ? -52.008 25.020 -11.992 1.00 254.59 ? 475 GLU B C 1 ATOM 10811 O O . GLU B 2 475 ? -51.745 26.072 -12.573 1.00 261.46 ? 475 GLU B O 1 ATOM 10812 C CB . GLU B 2 475 ? -50.675 25.913 -10.063 1.00 266.16 ? 475 GLU B CB 1 ATOM 10813 C CG . GLU B 2 475 ? -51.501 27.046 -9.489 1.00 273.57 ? 475 GLU B CG 1 ATOM 10814 C CD . GLU B 2 475 ? -52.497 26.573 -8.445 1.00 268.51 ? 475 GLU B CD 1 ATOM 10815 O OE1 . GLU B 2 475 ? -52.110 25.773 -7.567 1.00 258.34 ? 475 GLU B OE1 1 ATOM 10816 O OE2 . GLU B 2 475 ? -53.670 26.999 -8.506 1.00 272.34 ? 475 GLU B OE2 1 ATOM 10817 N N . GLU B 2 476 ? -52.719 24.041 -12.530 1.00 245.89 ? 476 GLU B N 1 ATOM 10818 C CA . GLU B 2 476 ? -53.292 24.073 -13.867 1.00 252.35 ? 476 GLU B CA 1 ATOM 10819 C C . GLU B 2 476 ? -54.705 24.650 -13.827 1.00 253.66 ? 476 GLU B C 1 ATOM 10820 O O . GLU B 2 476 ? -55.447 24.539 -14.806 1.00 256.20 ? 476 GLU B O 1 ATOM 10821 C CB . GLU B 2 476 ? -53.302 22.668 -14.482 1.00 242.72 ? 476 GLU B CB 1 ATOM 10822 C CG . GLU B 2 476 ? -53.388 22.645 -16.005 1.00 247.29 ? 476 GLU B CG 1 ATOM 10823 C CD . GLU B 2 476 ? -53.563 21.247 -16.561 1.00 241.37 ? 476 GLU B CD 1 ATOM 10824 O OE1 . GLU B 2 476 ? -54.043 21.119 -17.707 1.00 239.60 ? 476 GLU B OE1 1 ATOM 10825 O OE2 . GLU B 2 476 ? -53.219 20.278 -15.854 1.00 237.36 ? 476 GLU B OE2 1 ATOM 10826 N N . ASP B 2 477 ? -55.053 25.298 -12.713 1.00 248.39 ? 477 ASP B N 1 ATOM 10827 C CA . ASP B 2 477 ? -56.337 25.113 -12.039 1.00 242.87 ? 477 ASP B CA 1 ATOM 10828 C C . ASP B 2 477 ? -56.230 23.726 -11.439 1.00 238.88 ? 477 ASP B C 1 ATOM 10829 O O . ASP B 2 477 ? -55.382 23.539 -10.565 1.00 226.61 ? 477 ASP B O 1 ATOM 10830 C CB . ASP B 2 477 ? -57.547 25.255 -12.963 1.00 239.16 ? 477 ASP B CB 1 ATOM 10831 C CG . ASP B 2 477 ? -58.029 26.688 -13.074 1.00 242.68 ? 477 ASP B CG 1 ATOM 10832 O OD1 . ASP B 2 477 ? -57.946 27.423 -12.068 1.00 229.79 ? 477 ASP B OD1 1 ATOM 10833 O OD2 . ASP B 2 477 ? -58.493 27.074 -14.166 1.00 245.80 ? 477 ASP B OD2 1 ATOM 10834 N N . TYR B 2 478 ? -57.061 22.771 -11.859 1.00 242.48 ? 478 TYR B N 1 ATOM 10835 C CA . TYR B 2 478 ? -56.980 21.430 -11.284 1.00 235.26 ? 478 TYR B CA 1 ATOM 10836 C C . TYR B 2 478 ? -57.288 21.514 -9.803 1.00 228.10 ? 478 TYR B C 1 ATOM 10837 O O . TYR B 2 478 ? -56.364 21.508 -8.999 1.00 215.76 ? 478 TYR B O 1 ATOM 10838 C CB . TYR B 2 478 ? -55.584 20.821 -11.488 1.00 231.96 ? 478 TYR B CB 1 ATOM 10839 C CG . TYR B 2 478 ? -55.522 19.547 -12.289 1.00 232.34 ? 478 TYR B CG 1 ATOM 10840 C CD1 . TYR B 2 478 ? -55.493 19.579 -13.675 1.00 242.66 ? 478 TYR B CD1 1 ATOM 10841 C CD2 . TYR B 2 478 ? -55.451 18.313 -11.659 1.00 224.27 ? 478 TYR B CD2 1 ATOM 10842 C CE1 . TYR B 2 478 ? -55.422 18.415 -14.415 1.00 243.04 ? 478 TYR B CE1 1 ATOM 10843 C CE2 . TYR B 2 478 ? -55.379 17.142 -12.389 1.00 226.15 ? 478 TYR B CE2 1 ATOM 10844 C CZ . TYR B 2 478 ? -55.365 17.199 -13.768 1.00 235.33 ? 478 TYR B CZ 1 ATOM 10845 O OH . TYR B 2 478 ? -55.293 16.037 -14.501 1.00 236.64 ? 478 TYR B OH 1 ATOM 10846 N N . ARG B 2 479 ? -58.550 21.619 -9.427 1.00 231.63 ? 479 ARG B N 1 ATOM 10847 C CA . ARG B 2 479 ? -58.865 21.931 -8.042 1.00 225.83 ? 479 ARG B CA 1 ATOM 10848 C C . ARG B 2 479 ? -59.402 20.775 -7.204 1.00 228.13 ? 479 ARG B C 1 ATOM 10849 O O . ARG B 2 479 ? -60.574 20.432 -7.288 1.00 228.24 ? 479 ARG B O 1 ATOM 10850 C CB . ARG B 2 479 ? -59.837 23.098 -8.011 1.00 230.33 ? 479 ARG B CB 1 ATOM 10851 C CG . ARG B 2 479 ? -59.829 23.895 -9.302 1.00 238.07 ? 479 ARG B CG 1 ATOM 10852 C CD . ARG B 2 479 ? -61.109 24.693 -9.460 1.00 247.18 ? 479 ARG B CD 1 ATOM 10853 N NE . ARG B 2 479 ? -61.795 24.864 -8.185 1.00 247.40 ? 479 ARG B NE 1 ATOM 10854 C CZ . ARG B 2 479 ? -62.931 24.256 -7.857 1.00 249.95 ? 479 ARG B CZ 1 ATOM 10855 N NH1 . ARG B 2 479 ? -63.515 23.432 -8.714 1.00 246.65 ? 479 ARG B NH1 1 ATOM 10856 N NH2 . ARG B 2 479 ? -63.484 24.473 -6.671 1.00 250.25 ? 479 ARG B NH2 1 ATOM 10857 N N . PRO B 2 480 ? -58.524 20.196 -6.390 1.00 231.44 ? 480 PRO B N 1 ATOM 10858 C CA . PRO B 2 480 ? -58.914 19.160 -5.430 1.00 228.98 ? 480 PRO B CA 1 ATOM 10859 C C . PRO B 2 480 ? -59.412 19.811 -4.146 1.00 236.64 ? 480 PRO B C 1 ATOM 10860 O O . PRO B 2 480 ? -58.656 20.516 -3.478 1.00 236.58 ? 480 PRO B O 1 ATOM 10861 C CB . PRO B 2 480 ? -57.603 18.417 -5.172 1.00 216.30 ? 480 PRO B CB 1 ATOM 10862 C CG . PRO B 2 480 ? -56.821 18.600 -6.428 1.00 218.06 ? 480 PRO B CG 1 ATOM 10863 C CD . PRO B 2 480 ? -57.174 19.970 -6.934 1.00 228.34 ? 480 PRO B CD 1 ATOM 10864 N N . SER B 2 481 ? -60.677 19.581 -3.816 1.00 238.02 ? 481 SER B N 1 ATOM 10865 C CA . SER B 2 481 ? -61.315 20.251 -2.683 1.00 236.64 ? 481 SER B CA 1 ATOM 10866 C C . SER B 2 481 ? -60.776 19.704 -1.349 1.00 238.36 ? 481 SER B C 1 ATOM 10867 O O . SER B 2 481 ? -61.467 19.732 -0.333 1.00 240.84 ? 481 SER B O 1 ATOM 10868 C CB . SER B 2 481 ? -62.839 20.099 -2.747 1.00 229.20 ? 481 SER B CB 1 ATOM 10869 O OG . SER B 2 481 ? -63.481 20.988 -1.848 1.00 223.75 ? 481 SER B OG 1 ATOM 10870 N N . GLN B 2 482 ? -59.530 19.222 -1.377 1.00 237.65 ? 482 GLN B N 1 ATOM 10871 C CA . GLN B 2 482 ? -58.987 18.114 -0.594 1.00 228.85 ? 482 GLN B CA 1 ATOM 10872 C C . GLN B 2 482 ? -59.533 17.932 0.814 1.00 230.05 ? 482 GLN B C 1 ATOM 10873 O O . GLN B 2 482 ? -59.723 16.789 1.229 1.00 223.32 ? 482 GLN B O 1 ATOM 10874 C CB . GLN B 2 482 ? -57.460 18.279 -0.480 1.00 220.77 ? 482 GLN B CB 1 ATOM 10875 C CG . GLN B 2 482 ? -56.735 18.658 -1.773 1.00 221.02 ? 482 GLN B CG 1 ATOM 10876 C CD . GLN B 2 482 ? -56.285 20.119 -1.815 1.00 218.61 ? 482 GLN B CD 1 ATOM 10877 O OE1 . GLN B 2 482 ? -56.591 20.907 -0.920 1.00 214.93 ? 482 GLN B OE1 1 ATOM 10878 N NE2 . GLN B 2 482 ? -55.561 20.481 -2.870 1.00 217.88 ? 482 GLN B NE2 1 ATOM 10879 N N . GLN B 2 483 ? -59.778 19.016 1.548 1.00 236.40 ? 483 GLN B N 1 ATOM 10880 C CA . GLN B 2 483 ? -60.502 18.895 2.814 1.00 237.36 ? 483 GLN B CA 1 ATOM 10881 C C . GLN B 2 483 ? -59.821 17.899 3.747 1.00 233.88 ? 483 GLN B C 1 ATOM 10882 O O . GLN B 2 483 ? -58.734 18.155 4.265 1.00 229.29 ? 483 GLN B O 1 ATOM 10883 C CB . GLN B 2 483 ? -61.955 18.477 2.568 1.00 239.83 ? 483 GLN B CB 1 ATOM 10884 C CG . GLN B 2 483 ? -62.996 19.394 3.200 1.00 241.78 ? 483 GLN B CG 1 ATOM 10885 C CD . GLN B 2 483 ? -63.317 20.619 2.352 1.00 249.21 ? 483 GLN B CD 1 ATOM 10886 O OE1 . GLN B 2 483 ? -64.264 21.351 2.640 1.00 253.82 ? 483 GLN B OE1 1 ATOM 10887 N NE2 . GLN B 2 483 ? -62.534 20.845 1.304 1.00 251.70 ? 483 GLN B NE2 1 ATOM 10888 N N . ASP B 2 484 ? -60.502 16.776 3.968 1.00 234.19 ? 484 ASP B N 1 ATOM 10889 C CA . ASP B 2 484 ? -60.005 15.685 4.799 1.00 227.27 ? 484 ASP B CA 1 ATOM 10890 C C . ASP B 2 484 ? -58.580 15.285 4.431 1.00 222.48 ? 484 ASP B C 1 ATOM 10891 O O . ASP B 2 484 ? -58.217 15.257 3.253 1.00 223.25 ? 484 ASP B O 1 ATOM 10892 C CB . ASP B 2 484 ? -60.921 14.464 4.674 1.00 225.99 ? 484 ASP B CB 1 ATOM 10893 C CG . ASP B 2 484 ? -62.288 14.813 4.116 1.00 231.41 ? 484 ASP B CG 1 ATOM 10894 O OD1 . ASP B 2 484 ? -62.848 15.853 4.518 1.00 224.09 ? 484 ASP B OD1 1 ATOM 10895 O OD2 . ASP B 2 484 ? -62.800 14.048 3.270 1.00 237.19 ? 484 ASP B OD2 1 ATOM 10896 N N . GLU B 2 485 ? -57.782 15.027 5.466 1.00 214.50 ? 485 GLU B N 1 ATOM 10897 C CA . GLU B 2 485 ? -56.394 14.563 5.367 1.00 205.75 ? 485 GLU B CA 1 ATOM 10898 C C . GLU B 2 485 ? -55.410 15.655 4.934 1.00 199.58 ? 485 GLU B C 1 ATOM 10899 O O . GLU B 2 485 ? -54.200 15.480 5.069 1.00 201.55 ? 485 GLU B O 1 ATOM 10900 C CB . GLU B 2 485 ? -56.282 13.363 4.418 1.00 210.32 ? 485 GLU B CB 1 ATOM 10901 C CG . GLU B 2 485 ? -56.974 12.102 4.913 1.00 206.57 ? 485 GLU B CG 1 ATOM 10902 C CD . GLU B 2 485 ? -56.853 10.951 3.933 1.00 204.69 ? 485 GLU B CD 1 ATOM 10903 O OE1 . GLU B 2 485 ? -56.976 11.192 2.714 1.00 205.44 ? 485 GLU B OE1 1 ATOM 10904 O OE2 . GLU B 2 485 ? -56.627 9.808 4.381 1.00 205.09 ? 485 GLU B OE2 1 ATOM 10905 N N . CYS B 2 486 ? -55.914 16.774 4.420 1.00 199.93 ? 486 CYS B N 1 ATOM 10906 C CA . CYS B 2 486 ? -55.061 17.928 4.147 1.00 196.27 ? 486 CYS B CA 1 ATOM 10907 C C . CYS B 2 486 ? -54.842 18.689 5.455 1.00 181.57 ? 486 CYS B C 1 ATOM 10908 O O . CYS B 2 486 ? -53.864 19.418 5.610 1.00 169.36 ? 486 CYS B O 1 ATOM 10909 C CB . CYS B 2 486 ? -55.676 18.834 3.074 1.00 202.49 ? 486 CYS B CB 1 ATOM 10910 S SG . CYS B 2 486 ? -54.480 19.769 2.078 1.00 185.05 ? 486 CYS B SG 1 ATOM 10911 N N . SER B 2 487 ? -55.778 18.517 6.385 1.00 183.16 ? 487 SER B N 1 ATOM 10912 C CA . SER B 2 487 ? -55.647 19.039 7.743 1.00 173.04 ? 487 SER B CA 1 ATOM 10913 C C . SER B 2 487 ? -56.254 18.052 8.739 1.00 185.25 ? 487 SER B C 1 ATOM 10914 O O . SER B 2 487 ? -57.267 17.419 8.445 1.00 186.99 ? 487 SER B O 1 ATOM 10915 C CB . SER B 2 487 ? -56.324 20.407 7.864 1.00 160.91 ? 487 SER B CB 1 ATOM 10916 O OG . SER B 2 487 ? -56.284 20.885 9.198 1.00 161.22 ? 487 SER B OG 1 ATOM 10917 N N . PRO B 2 488 ? -55.640 17.916 9.926 1.00 196.15 ? 488 PRO B N 1 ATOM 10918 C CA . PRO B 2 488 ? -56.188 16.994 10.926 1.00 203.75 ? 488 PRO B CA 1 ATOM 10919 C C . PRO B 2 488 ? -57.350 17.627 11.681 1.00 207.59 ? 488 PRO B C 1 ATOM 10920 O O . PRO B 2 488 ? -57.615 18.811 11.468 1.00 215.01 ? 488 PRO B O 1 ATOM 10921 C CB . PRO B 2 488 ? -55.000 16.738 11.867 1.00 200.74 ? 488 PRO B CB 1 ATOM 10922 C CG . PRO B 2 488 ? -53.796 17.358 11.189 1.00 192.81 ? 488 PRO B CG 1 ATOM 10923 C CD . PRO B 2 488 ? -54.339 18.459 10.342 1.00 192.84 ? 488 PRO B CD 1 ATOM 10924 N N . ARG B 2 489 ? -57.994 16.863 12.564 1.00 198.66 ? 489 ARG B N 1 ATOM 10925 C CA . ARG B 2 489 ? -59.153 17.337 13.323 1.00 200.90 ? 489 ARG B CA 1 ATOM 10926 C C . ARG B 2 489 ? -60.128 18.076 12.407 1.00 207.82 ? 489 ARG B C 1 ATOM 10927 O O . ARG B 2 489 ? -60.233 19.302 12.466 1.00 210.55 ? 489 ARG B O 1 ATOM 10928 C CB . ARG B 2 489 ? -58.712 18.235 14.483 1.00 190.53 ? 489 ARG B CB 1 ATOM 10929 C CG . ARG B 2 489 ? -59.695 18.272 15.649 1.00 183.83 ? 489 ARG B CG 1 ATOM 10930 C CD . ARG B 2 489 ? -59.087 18.950 16.870 1.00 177.88 ? 489 ARG B CD 1 ATOM 10931 N NE . ARG B 2 489 ? -59.961 18.866 18.039 1.00 179.52 ? 489 ARG B NE 1 ATOM 10932 C CZ . ARG B 2 489 ? -59.664 19.373 19.232 1.00 173.04 ? 489 ARG B CZ 1 ATOM 10933 N NH1 . ARG B 2 489 ? -58.513 20.004 19.420 1.00 168.48 ? 489 ARG B NH1 1 ATOM 10934 N NH2 . ARG B 2 489 ? -60.519 19.250 20.239 1.00 166.54 ? 489 ARG B NH2 1 ATOM 10935 N N . GLU B 2 490 ? -60.824 17.316 11.564 1.00 203.34 ? 490 GLU B N 1 ATOM 10936 C CA . GLU B 2 490 ? -61.573 17.852 10.426 1.00 201.26 ? 490 GLU B CA 1 ATOM 10937 C C . GLU B 2 490 ? -62.492 19.022 10.773 1.00 209.02 ? 490 GLU B C 1 ATOM 10938 O O . GLU B 2 490 ? -63.147 19.033 11.815 1.00 217.19 ? 490 GLU B O 1 ATOM 10939 C CB . GLU B 2 490 ? -62.398 16.738 9.774 1.00 199.01 ? 490 GLU B CB 1 ATOM 10940 C CG . GLU B 2 490 ? -63.386 16.062 10.712 1.00 203.78 ? 490 GLU B CG 1 ATOM 10941 C CD . GLU B 2 490 ? -64.301 15.089 9.995 1.00 216.74 ? 490 GLU B CD 1 ATOM 10942 O OE1 . GLU B 2 490 ? -65.181 14.499 10.657 1.00 218.42 ? 490 GLU B OE1 1 ATOM 10943 O OE2 . GLU B 2 490 ? -64.142 14.916 8.768 1.00 219.82 ? 490 GLU B OE2 1 ATOM 10944 N N . GLY B 2 491 ? -62.522 20.010 9.883 1.00 202.28 ? 491 GLY B N 1 ATOM 10945 C CA . GLY B 2 491 ? -63.273 21.232 10.105 1.00 198.27 ? 491 GLY B CA 1 ATOM 10946 C C . GLY B 2 491 ? -62.359 22.415 10.361 1.00 190.99 ? 491 GLY B C 1 ATOM 10947 O O . GLY B 2 491 ? -62.807 23.561 10.400 1.00 190.47 ? 491 GLY B O 1 ATOM 10948 N N . GLN B 2 492 ? -61.071 22.135 10.532 1.00 193.24 ? 492 GLN B N 1 ATOM 10949 C CA . GLN B 2 492 ? -60.073 23.180 10.729 1.00 203.66 ? 492 GLN B CA 1 ATOM 10950 C C . GLN B 2 492 ? -59.534 23.672 9.385 1.00 204.78 ? 492 GLN B C 1 ATOM 10951 O O . GLN B 2 492 ? -59.579 22.940 8.396 1.00 201.00 ? 492 GLN B O 1 ATOM 10952 C CB . GLN B 2 492 ? -58.934 22.669 11.618 1.00 199.20 ? 492 GLN B CB 1 ATOM 10953 C CG . GLN B 2 492 ? -59.273 22.660 13.101 1.00 199.99 ? 492 GLN B CG 1 ATOM 10954 C CD . GLN B 2 492 ? -58.066 22.384 13.975 1.00 195.09 ? 492 GLN B CD 1 ATOM 10955 O OE1 . GLN B 2 492 ? -57.066 21.831 13.517 1.00 195.25 ? 492 GLN B OE1 1 ATOM 10956 N NE2 . GLN B 2 492 ? -58.151 22.774 15.242 1.00 190.49 ? 492 GLN B NE2 1 ATOM 10957 N N . PRO B 2 493 ? -59.029 24.920 9.345 1.00 209.84 ? 493 PRO B N 1 ATOM 10958 C CA . PRO B 2 493 ? -58.527 25.511 8.098 1.00 207.61 ? 493 PRO B CA 1 ATOM 10959 C C . PRO B 2 493 ? -57.398 24.715 7.457 1.00 198.70 ? 493 PRO B C 1 ATOM 10960 O O . PRO B 2 493 ? -56.722 23.925 8.118 1.00 199.89 ? 493 PRO B O 1 ATOM 10961 C CB . PRO B 2 493 ? -58.029 26.896 8.536 1.00 205.03 ? 493 PRO B CB 1 ATOM 10962 C CG . PRO B 2 493 ? -57.883 26.812 10.017 1.00 199.56 ? 493 PRO B CG 1 ATOM 10963 C CD . PRO B 2 493 ? -58.959 25.879 10.460 1.00 207.54 ? 493 PRO B CD 1 ATOM 10964 N N . VAL B 2 494 ? -57.202 24.936 6.164 1.00 187.25 ? 494 VAL B N 1 ATOM 10965 C CA . VAL B 2 494 ? -56.273 24.135 5.384 1.00 171.92 ? 494 VAL B CA 1 ATOM 10966 C C . VAL B 2 494 ? -54.812 24.525 5.603 1.00 166.29 ? 494 VAL B C 1 ATOM 10967 O O . VAL B 2 494 ? -54.431 25.687 5.434 1.00 160.13 ? 494 VAL B O 1 ATOM 10968 C CB . VAL B 2 494 ? -56.607 24.236 3.885 1.00 171.72 ? 494 VAL B CB 1 ATOM 10969 C CG1 . VAL B 2 494 ? -55.433 23.789 3.058 1.00 157.27 ? 494 VAL B CG1 1 ATOM 10970 C CG2 . VAL B 2 494 ? -57.839 23.398 3.568 1.00 164.10 ? 494 VAL B CG2 1 ATOM 10971 N N . CYS B 2 495 ? -54.013 23.534 5.991 1.00 176.94 ? 495 CYS B N 1 ATOM 10972 C CA . CYS B 2 495 ? -52.580 23.692 6.214 1.00 183.88 ? 495 CYS B CA 1 ATOM 10973 C C . CYS B 2 495 ? -52.243 24.762 7.259 1.00 182.15 ? 495 CYS B C 1 ATOM 10974 O O . CYS B 2 495 ? -51.177 25.361 7.203 1.00 182.19 ? 495 CYS B O 1 ATOM 10975 C CB . CYS B 2 495 ? -51.872 24.001 4.878 1.00 189.14 ? 495 CYS B CB 1 ATOM 10976 S SG . CYS B 2 495 ? -51.877 22.621 3.684 1.00 218.75 ? 495 CYS B SG 1 ATOM 10977 N N . SER B 2 496 ? -53.150 24.985 8.212 1.00 174.96 ? 496 SER B N 1 ATOM 10978 C CA . SER B 2 496 ? -52.933 25.949 9.304 1.00 172.91 ? 496 SER B CA 1 ATOM 10979 C C . SER B 2 496 ? -52.955 27.397 8.793 1.00 170.93 ? 496 SER B C 1 ATOM 10980 O O . SER B 2 496 ? -52.857 28.344 9.574 1.00 163.44 ? 496 SER B O 1 ATOM 10981 C CB . SER B 2 496 ? -51.613 25.656 10.038 1.00 160.51 ? 496 SER B CB 1 ATOM 10982 O OG . SER B 2 496 ? -51.354 24.259 10.051 1.00 153.82 ? 496 SER B OG 1 ATOM 10983 N N . GLN B 2 497 ? -53.119 27.532 7.476 1.00 178.57 ? 497 GLN B N 1 ATOM 10984 C CA . GLN B 2 497 ? -53.068 28.791 6.706 1.00 178.19 ? 497 GLN B CA 1 ATOM 10985 C C . GLN B 2 497 ? -51.646 29.303 6.457 1.00 176.63 ? 497 GLN B C 1 ATOM 10986 O O . GLN B 2 497 ? -51.418 30.092 5.543 1.00 174.38 ? 497 GLN B O 1 ATOM 10987 C CB . GLN B 2 497 ? -53.868 29.895 7.394 1.00 171.22 ? 497 GLN B CB 1 ATOM 10988 C CG . GLN B 2 497 ? -55.366 29.705 7.424 1.00 175.43 ? 497 GLN B CG 1 ATOM 10989 C CD . GLN B 2 497 ? -55.922 30.369 8.650 1.00 183.43 ? 497 GLN B CD 1 ATOM 10990 O OE1 . GLN B 2 497 ? -55.197 30.539 9.629 1.00 169.72 ? 497 GLN B OE1 1 ATOM 10991 N NE2 . GLN B 2 497 ? -57.179 30.787 8.604 1.00 190.26 ? 497 GLN B NE2 1 ATOM 10992 N N . ARG B 2 498 ? -50.683 28.838 7.241 1.00 181.87 ? 498 ARG B N 1 ATOM 10993 C CA . ARG B 2 498 ? -49.296 28.990 6.845 1.00 185.80 ? 498 ARG B CA 1 ATOM 10994 C C . ARG B 2 498 ? -49.128 27.923 5.772 1.00 188.85 ? 498 ARG B C 1 ATOM 10995 O O . ARG B 2 498 ? -49.418 26.747 6.026 1.00 184.57 ? 498 ARG B O 1 ATOM 10996 C CB . ARG B 2 498 ? -48.346 28.828 8.051 1.00 184.97 ? 498 ARG B CB 1 ATOM 10997 C CG . ARG B 2 498 ? -48.637 29.805 9.229 1.00 184.06 ? 498 ARG B CG 1 ATOM 10998 C CD . ARG B 2 498 ? -47.881 29.456 10.509 1.00 182.33 ? 498 ARG B CD 1 ATOM 10999 N NE . ARG B 2 498 ? -48.413 28.249 11.130 1.00 182.35 ? 498 ARG B NE 1 ATOM 11000 C CZ . ARG B 2 498 ? -47.967 27.747 12.274 1.00 175.71 ? 498 ARG B CZ 1 ATOM 11001 N NH1 . ARG B 2 498 ? -46.982 28.353 12.918 1.00 158.47 ? 498 ARG B NH1 1 ATOM 11002 N NH2 . ARG B 2 498 ? -48.503 26.643 12.772 1.00 174.49 ? 498 ARG B NH2 1 ATOM 11003 N N . GLY B 2 499 ? -48.723 28.339 4.566 1.00 186.94 ? 499 GLY B N 1 ATOM 11004 C CA . GLY B 2 499 ? -48.681 27.449 3.402 1.00 186.35 ? 499 GLY B CA 1 ATOM 11005 C C . GLY B 2 499 ? -50.002 27.583 2.684 1.00 183.91 ? 499 GLY B C 1 ATOM 11006 O O . GLY B 2 499 ? -50.493 28.704 2.665 1.00 192.79 ? 499 GLY B O 1 ATOM 11007 N N . GLU B 2 500 ? -50.502 26.505 2.066 1.00 178.79 ? 500 GLU B N 1 ATOM 11008 C CA . GLU B 2 500 ? -51.847 26.333 1.510 1.00 180.59 ? 500 GLU B CA 1 ATOM 11009 C C . GLU B 2 500 ? -51.839 24.905 0.932 1.00 190.34 ? 500 GLU B C 1 ATOM 11010 O O . GLU B 2 500 ? -50.827 24.230 1.052 1.00 189.56 ? 500 GLU B O 1 ATOM 11011 C CB . GLU B 2 500 ? -52.191 27.382 0.445 1.00 180.35 ? 500 GLU B CB 1 ATOM 11012 C CG . GLU B 2 500 ? -52.906 28.604 0.951 1.00 182.58 ? 500 GLU B CG 1 ATOM 11013 C CD . GLU B 2 500 ? -52.846 29.767 -0.035 1.00 193.32 ? 500 GLU B CD 1 ATOM 11014 O OE1 . GLU B 2 500 ? -53.222 29.601 -1.214 1.00 204.84 ? 500 GLU B OE1 1 ATOM 11015 O OE2 . GLU B 2 500 ? -52.345 30.837 0.371 1.00 193.79 ? 500 GLU B OE2 1 ATOM 11016 N N . CYS B 2 501 ? -52.930 24.441 0.318 1.00 193.58 ? 501 CYS B N 1 ATOM 11017 C CA . CYS B 2 501 ? -52.901 23.074 -0.231 1.00 193.99 ? 501 CYS B CA 1 ATOM 11018 C C . CYS B 2 501 ? -53.152 23.080 -1.727 1.00 195.06 ? 501 CYS B C 1 ATOM 11019 O O . CYS B 2 501 ? -54.161 23.627 -2.184 1.00 197.44 ? 501 CYS B O 1 ATOM 11020 C CB . CYS B 2 501 ? -53.927 22.170 0.457 1.00 197.86 ? 501 CYS B CB 1 ATOM 11021 S SG . CYS B 2 501 ? -53.471 20.405 0.431 1.00 258.62 ? 501 CYS B SG 1 ATOM 11022 N N . LEU B 2 502 ? -52.219 22.506 -2.486 1.00 190.37 ? 502 LEU B N 1 ATOM 11023 C CA . LEU B 2 502 ? -52.376 22.315 -3.936 1.00 189.67 ? 502 LEU B CA 1 ATOM 11024 C C . LEU B 2 502 ? -52.019 20.886 -4.366 1.00 189.79 ? 502 LEU B C 1 ATOM 11025 O O . LEU B 2 502 ? -51.010 20.324 -3.931 1.00 188.25 ? 502 LEU B O 1 ATOM 11026 C CB . LEU B 2 502 ? -51.528 23.328 -4.720 1.00 193.86 ? 502 LEU B CB 1 ATOM 11027 C CG . LEU B 2 502 ? -50.000 23.312 -4.626 1.00 197.27 ? 502 LEU B CG 1 ATOM 11028 C CD1 . LEU B 2 502 ? -49.365 22.543 -5.784 1.00 195.17 ? 502 LEU B CD1 1 ATOM 11029 C CD2 . LEU B 2 502 ? -49.482 24.736 -4.574 1.00 200.25 ? 502 LEU B CD2 1 ATOM 11030 N N . CYS B 2 503 ? -52.879 20.314 -5.211 1.00 192.80 ? 503 CYS B N 1 ATOM 11031 C CA . CYS B 2 503 ? -52.734 18.958 -5.757 1.00 184.25 ? 503 CYS B CA 1 ATOM 11032 C C . CYS B 2 503 ? -52.918 17.910 -4.661 1.00 189.92 ? 503 CYS B C 1 ATOM 11033 O O . CYS B 2 503 ? -52.843 16.709 -4.913 1.00 200.66 ? 503 CYS B O 1 ATOM 11034 C CB . CYS B 2 503 ? -51.387 18.775 -6.470 1.00 178.36 ? 503 CYS B CB 1 ATOM 11035 S SG . CYS B 2 503 ? -51.303 17.348 -7.593 1.00 238.85 ? 503 CYS B SG 1 ATOM 11036 N N . GLY B 2 504 ? -53.161 18.386 -3.444 1.00 189.53 ? 504 GLY B N 1 ATOM 11037 C CA . GLY B 2 504 ? -53.351 17.545 -2.277 1.00 193.45 ? 504 GLY B CA 1 ATOM 11038 C C . GLY B 2 504 ? -52.161 17.536 -1.338 1.00 198.46 ? 504 GLY B C 1 ATOM 11039 O O . GLY B 2 504 ? -52.310 17.272 -0.144 1.00 198.96 ? 504 GLY B O 1 ATOM 11040 N N . GLN B 2 505 ? -50.977 17.826 -1.867 1.00 195.79 ? 505 GLN B N 1 ATOM 11041 C CA . GLN B 2 505 ? -49.826 18.126 -1.026 1.00 178.46 ? 505 GLN B CA 1 ATOM 11042 C C . GLN B 2 505 ? -49.889 19.590 -0.617 1.00 184.60 ? 505 GLN B C 1 ATOM 11043 O O . GLN B 2 505 ? -50.509 20.401 -1.300 1.00 193.83 ? 505 GLN B O 1 ATOM 11044 C CB . GLN B 2 505 ? -48.507 17.828 -1.743 1.00 178.02 ? 505 GLN B CB 1 ATOM 11045 C CG . GLN B 2 505 ? -48.223 16.350 -1.983 1.00 181.71 ? 505 GLN B CG 1 ATOM 11046 C CD . GLN B 2 505 ? -48.992 15.782 -3.161 1.00 198.28 ? 505 GLN B CD 1 ATOM 11047 O OE1 . GLN B 2 505 ? -49.708 16.501 -3.858 1.00 213.20 ? 505 GLN B OE1 1 ATOM 11048 N NE2 . GLN B 2 505 ? -48.845 14.482 -3.391 1.00 195.60 ? 505 GLN B NE2 1 ATOM 11049 N N . CYS B 2 506 ? -49.257 19.932 0.498 1.00 182.48 ? 506 CYS B N 1 ATOM 11050 C CA . CYS B 2 506 ? -49.172 21.331 0.886 1.00 168.29 ? 506 CYS B CA 1 ATOM 11051 C C . CYS B 2 506 ? -47.808 21.906 0.556 1.00 168.25 ? 506 CYS B C 1 ATOM 11052 O O . CYS B 2 506 ? -46.806 21.546 1.173 1.00 168.71 ? 506 CYS B O 1 ATOM 11053 C CB . CYS B 2 506 ? -49.457 21.502 2.375 1.00 155.38 ? 506 CYS B CB 1 ATOM 11054 S SG . CYS B 2 506 ? -51.090 20.934 2.886 1.00 217.54 ? 506 CYS B SG 1 ATOM 11055 N N . VAL B 2 507 ? -47.773 22.797 -0.427 1.00 182.00 ? 507 VAL B N 1 ATOM 11056 C CA . VAL B 2 507 ? -46.559 23.539 -0.722 1.00 193.75 ? 507 VAL B CA 1 ATOM 11057 C C . VAL B 2 507 ? -46.649 24.888 -0.026 1.00 197.97 ? 507 VAL B C 1 ATOM 11058 O O . VAL B 2 507 ? -47.465 25.735 -0.392 1.00 198.49 ? 507 VAL B O 1 ATOM 11059 C CB . VAL B 2 507 ? -46.350 23.731 -2.234 1.00 197.00 ? 507 VAL B CB 1 ATOM 11060 C CG1 . VAL B 2 507 ? -45.109 24.570 -2.490 1.00 200.43 ? 507 VAL B CG1 1 ATOM 11061 C CG2 . VAL B 2 507 ? -46.239 22.381 -2.928 1.00 186.05 ? 507 VAL B CG2 1 ATOM 11062 N N . CYS B 2 508 ? -45.806 25.078 0.983 1.00 199.74 ? 508 CYS B N 1 ATOM 11063 C CA . CYS B 2 508 ? -45.908 26.242 1.850 1.00 202.93 ? 508 CYS B CA 1 ATOM 11064 C C . CYS B 2 508 ? -45.489 27.531 1.157 1.00 203.81 ? 508 CYS B C 1 ATOM 11065 O O . CYS B 2 508 ? -44.375 27.643 0.646 1.00 198.79 ? 508 CYS B O 1 ATOM 11066 C CB . CYS B 2 508 ? -45.069 26.038 3.113 1.00 200.28 ? 508 CYS B CB 1 ATOM 11067 S SG . CYS B 2 508 ? -45.514 24.571 4.072 1.00 188.37 ? 508 CYS B SG 1 ATOM 11068 N N . HIS B 2 509 ? -46.393 28.505 1.151 1.00 211.60 ? 509 HIS B N 1 ATOM 11069 C CA . HIS B 2 509 ? -46.086 29.814 0.598 1.00 224.25 ? 509 HIS B CA 1 ATOM 11070 C C . HIS B 2 509 ? -45.595 30.725 1.718 1.00 226.26 ? 509 HIS B C 1 ATOM 11071 O O . HIS B 2 509 ? -45.381 30.264 2.840 1.00 211.73 ? 509 HIS B O 1 ATOM 11072 C CB . HIS B 2 509 ? -47.308 30.408 -0.121 1.00 224.97 ? 509 HIS B CB 1 ATOM 11073 C CG . HIS B 2 509 ? -48.362 30.964 0.792 1.00 216.38 ? 509 HIS B CG 1 ATOM 11074 N ND1 . HIS B 2 509 ? -48.436 30.661 2.136 1.00 209.02 ? 509 HIS B ND1 1 ATOM 11075 C CD2 . HIS B 2 509 ? -49.391 31.808 0.542 1.00 211.86 ? 509 HIS B CD2 1 ATOM 11076 C CE1 . HIS B 2 509 ? -49.456 31.304 2.675 1.00 204.88 ? 509 HIS B CE1 1 ATOM 11077 N NE2 . HIS B 2 509 ? -50.057 32.000 1.728 1.00 207.50 ? 509 HIS B NE2 1 ATOM 11078 N N . SER B 2 510 ? -45.427 32.007 1.409 1.00 246.77 ? 510 SER B N 1 ATOM 11079 C CA . SER B 2 510 ? -44.957 32.993 2.380 1.00 255.57 ? 510 SER B CA 1 ATOM 11080 C C . SER B 2 510 ? -43.622 32.587 2.996 1.00 240.72 ? 510 SER B C 1 ATOM 11081 O O . SER B 2 510 ? -43.472 32.572 4.218 1.00 236.58 ? 510 SER B O 1 ATOM 11082 C CB . SER B 2 510 ? -45.997 33.204 3.485 1.00 258.68 ? 510 SER B CB 1 ATOM 11083 O OG . SER B 2 510 ? -47.265 33.527 2.944 1.00 268.33 ? 510 SER B OG 1 ATOM 11084 N N . SER B 2 511 ? -42.653 32.258 2.148 1.00 231.20 ? 511 SER B N 1 ATOM 11085 C CA . SER B 2 511 ? -41.334 31.887 2.638 1.00 213.17 ? 511 SER B CA 1 ATOM 11086 C C . SER B 2 511 ? -40.425 33.108 2.669 1.00 207.88 ? 511 SER B C 1 ATOM 11087 O O . SER B 2 511 ? -39.994 33.608 1.628 1.00 217.34 ? 511 SER B O 1 ATOM 11088 C CB . SER B 2 511 ? -40.725 30.784 1.769 1.00 212.20 ? 511 SER B CB 1 ATOM 11089 O OG . SER B 2 511 ? -40.692 31.167 0.406 1.00 219.02 ? 511 SER B OG 1 ATOM 11090 N N . ASP B 2 512 ? -40.127 33.554 3.885 1.00 189.57 ? 512 ASP B N 1 ATOM 11091 C CA . ASP B 2 512 ? -39.335 34.749 4.150 1.00 184.95 ? 512 ASP B CA 1 ATOM 11092 C C . ASP B 2 512 ? -39.283 34.899 5.662 1.00 177.89 ? 512 ASP B C 1 ATOM 11093 O O . ASP B 2 512 ? -40.109 34.310 6.362 1.00 171.91 ? 512 ASP B O 1 ATOM 11094 C CB . ASP B 2 512 ? -39.948 35.994 3.498 1.00 194.52 ? 512 ASP B CB 1 ATOM 11095 C CG . ASP B 2 512 ? -38.976 37.160 3.426 1.00 208.34 ? 512 ASP B CG 1 ATOM 11096 O OD1 . ASP B 2 512 ? -38.065 37.241 4.277 1.00 204.76 ? 512 ASP B OD1 1 ATOM 11097 O OD2 . ASP B 2 512 ? -39.126 38.001 2.513 1.00 208.77 ? 512 ASP B OD2 1 ATOM 11098 N N . PHE B 2 513 ? -38.331 35.688 6.159 1.00 170.22 ? 513 PHE B N 1 ATOM 11099 C CA . PHE B 2 513 ? -38.127 35.843 7.599 1.00 167.68 ? 513 PHE B CA 1 ATOM 11100 C C . PHE B 2 513 ? -37.934 34.458 8.228 1.00 175.71 ? 513 PHE B C 1 ATOM 11101 O O . PHE B 2 513 ? -38.406 34.182 9.326 1.00 169.22 ? 513 PHE B O 1 ATOM 11102 C CB . PHE B 2 513 ? -39.308 36.601 8.229 1.00 163.07 ? 513 PHE B CB 1 ATOM 11103 C CG . PHE B 2 513 ? -39.161 36.862 9.706 1.00 168.28 ? 513 PHE B CG 1 ATOM 11104 C CD1 . PHE B 2 513 ? -38.120 37.640 10.190 1.00 173.70 ? 513 PHE B CD1 1 ATOM 11105 C CD2 . PHE B 2 513 ? -40.074 36.335 10.608 1.00 151.74 ? 513 PHE B CD2 1 ATOM 11106 C CE1 . PHE B 2 513 ? -37.986 37.877 11.548 1.00 164.93 ? 513 PHE B CE1 1 ATOM 11107 C CE2 . PHE B 2 513 ? -39.946 36.569 11.965 1.00 157.14 ? 513 PHE B CE2 1 ATOM 11108 C CZ . PHE B 2 513 ? -38.901 37.342 12.436 1.00 160.30 ? 513 PHE B CZ 1 ATOM 11109 N N . GLY B 2 514 ? -37.226 33.588 7.514 1.00 194.46 ? 514 GLY B N 1 ATOM 11110 C CA . GLY B 2 514 ? -37.114 32.194 7.905 1.00 198.92 ? 514 GLY B CA 1 ATOM 11111 C C . GLY B 2 514 ? -37.931 31.310 6.981 1.00 203.41 ? 514 GLY B C 1 ATOM 11112 O O . GLY B 2 514 ? -38.714 31.809 6.171 1.00 201.31 ? 514 GLY B O 1 ATOM 11113 N N . LYS B 2 515 ? -37.751 29.997 7.093 1.00 202.15 ? 515 LYS B N 1 ATOM 11114 C CA . LYS B 2 515 ? -38.425 29.062 6.196 1.00 212.04 ? 515 LYS B CA 1 ATOM 11115 C C . LYS B 2 515 ? -39.582 28.328 6.873 1.00 205.23 ? 515 LYS B C 1 ATOM 11116 O O . LYS B 2 515 ? -39.541 28.049 8.072 1.00 200.68 ? 515 LYS B O 1 ATOM 11117 C CB . LYS B 2 515 ? -37.426 28.044 5.638 1.00 209.62 ? 515 LYS B CB 1 ATOM 11118 C CG . LYS B 2 515 ? -36.860 27.084 6.673 1.00 198.09 ? 515 LYS B CG 1 ATOM 11119 C CD . LYS B 2 515 ? -36.085 25.956 6.011 1.00 188.90 ? 515 LYS B CD 1 ATOM 11120 C CE . LYS B 2 515 ? -35.654 24.910 7.025 1.00 179.75 ? 515 LYS B CE 1 ATOM 11121 N NZ . LYS B 2 515 ? -34.946 23.772 6.377 1.00 179.58 ? 515 LYS B NZ 1 ATOM 11122 N N . ILE B 2 516 ? -40.617 28.027 6.093 1.00 193.35 ? 516 ILE B N 1 ATOM 11123 C CA . ILE B 2 516 ? -41.758 27.259 6.580 1.00 179.02 ? 516 ILE B CA 1 ATOM 11124 C C . ILE B 2 516 ? -41.727 25.843 6.013 1.00 176.19 ? 516 ILE B C 1 ATOM 11125 O O . ILE B 2 516 ? -41.687 25.654 4.798 1.00 181.12 ? 516 ILE B O 1 ATOM 11126 C CB . ILE B 2 516 ? -43.097 27.922 6.205 1.00 177.65 ? 516 ILE B CB 1 ATOM 11127 C CG1 . ILE B 2 516 ? -43.185 29.328 6.800 1.00 169.18 ? 516 ILE B CG1 1 ATOM 11128 C CG2 . ILE B 2 516 ? -44.265 27.070 6.682 1.00 167.25 ? 516 ILE B CG2 1 ATOM 11129 C CD1 . ILE B 2 516 ? -43.237 29.348 8.310 1.00 162.54 ? 516 ILE B CD1 1 ATOM 11130 N N . THR B 2 517 ? -41.748 24.852 6.898 1.00 174.80 ? 517 THR B N 1 ATOM 11131 C CA . THR B 2 517 ? -41.673 23.457 6.479 1.00 171.45 ? 517 THR B CA 1 ATOM 11132 C C . THR B 2 517 ? -42.790 22.624 7.096 1.00 162.75 ? 517 THR B C 1 ATOM 11133 O O . THR B 2 517 ? -43.673 23.153 7.767 1.00 162.16 ? 517 THR B O 1 ATOM 11134 C CB . THR B 2 517 ? -40.320 22.830 6.852 1.00 174.60 ? 517 THR B CB 1 ATOM 11135 O OG1 . THR B 2 517 ? -40.300 21.457 6.442 1.00 174.15 ? 517 THR B OG1 1 ATOM 11136 C CG2 . THR B 2 517 ? -40.091 22.910 8.354 1.00 174.94 ? 517 THR B CG2 1 ATOM 11137 N N . GLY B 2 518 ? -42.745 21.318 6.863 1.00 161.16 ? 518 GLY B N 1 ATOM 11138 C CA . GLY B 2 518 ? -43.775 20.423 7.356 1.00 163.05 ? 518 GLY B CA 1 ATOM 11139 C C . GLY B 2 518 ? -44.796 20.113 6.280 1.00 174.51 ? 518 GLY B C 1 ATOM 11140 O O . GLY B 2 518 ? -44.986 20.897 5.349 1.00 182.51 ? 518 GLY B O 1 ATOM 11141 N N . LYS B 2 519 ? -45.457 18.967 6.406 1.00 169.78 ? 519 LYS B N 1 ATOM 11142 C CA . LYS B 2 519 ? -46.434 18.536 5.412 1.00 171.17 ? 519 LYS B CA 1 ATOM 11143 C C . LYS B 2 519 ? -47.735 19.300 5.577 1.00 166.61 ? 519 LYS B C 1 ATOM 11144 O O . LYS B 2 519 ? -48.417 19.609 4.603 1.00 164.26 ? 519 LYS B O 1 ATOM 11145 C CB . LYS B 2 519 ? -46.688 17.035 5.521 1.00 180.55 ? 519 LYS B CB 1 ATOM 11146 C CG . LYS B 2 519 ? -45.422 16.218 5.652 1.00 187.19 ? 519 LYS B CG 1 ATOM 11147 C CD . LYS B 2 519 ? -44.423 16.561 4.559 1.00 189.31 ? 519 LYS B CD 1 ATOM 11148 C CE . LYS B 2 519 ? -43.079 15.921 4.836 1.00 182.25 ? 519 LYS B CE 1 ATOM 11149 N NZ . LYS B 2 519 ? -42.591 16.215 6.212 1.00 179.41 ? 519 LYS B NZ 1 ATOM 11150 N N . TYR B 2 520 ? -48.077 19.591 6.824 1.00 167.98 ? 520 TYR B N 1 ATOM 11151 C CA . TYR B 2 520 ? -49.214 20.444 7.127 1.00 171.17 ? 520 TYR B CA 1 ATOM 11152 C C . TYR B 2 520 ? -48.742 21.884 7.295 1.00 175.81 ? 520 TYR B C 1 ATOM 11153 O O . TYR B 2 520 ? -49.521 22.757 7.683 1.00 175.57 ? 520 TYR B O 1 ATOM 11154 C CB . TYR B 2 520 ? -49.938 19.957 8.383 1.00 169.26 ? 520 TYR B CB 1 ATOM 11155 C CG . TYR B 2 520 ? -50.577 18.597 8.218 1.00 176.34 ? 520 TYR B CG 1 ATOM 11156 C CD1 . TYR B 2 520 ? -49.863 17.434 8.477 1.00 178.88 ? 520 TYR B CD1 1 ATOM 11157 C CD2 . TYR B 2 520 ? -51.894 18.474 7.793 1.00 180.03 ? 520 TYR B CD2 1 ATOM 11158 C CE1 . TYR B 2 520 ? -50.443 16.189 8.322 1.00 175.53 ? 520 TYR B CE1 1 ATOM 11159 C CE2 . TYR B 2 520 ? -52.482 17.234 7.635 1.00 178.01 ? 520 TYR B CE2 1 ATOM 11160 C CZ . TYR B 2 520 ? -51.752 16.096 7.901 1.00 177.83 ? 520 TYR B CZ 1 ATOM 11161 O OH . TYR B 2 520 ? -52.335 14.860 7.745 1.00 180.02 ? 520 TYR B OH 1 ATOM 11162 N N . CYS B 2 521 ? -47.451 22.103 7.032 1.00 177.65 ? 521 CYS B N 1 ATOM 11163 C CA . CYS B 2 521 ? -46.802 23.411 7.163 1.00 177.75 ? 521 CYS B CA 1 ATOM 11164 C C . CYS B 2 521 ? -46.695 23.838 8.628 1.00 181.45 ? 521 CYS B C 1 ATOM 11165 O O . CYS B 2 521 ? -46.190 24.918 8.936 1.00 181.90 ? 521 CYS B O 1 ATOM 11166 C CB . CYS B 2 521 ? -47.531 24.477 6.344 1.00 176.75 ? 521 CYS B CB 1 ATOM 11167 S SG . CYS B 2 521 ? -47.456 24.223 4.557 1.00 147.21 ? 521 CYS B SG 1 ATOM 11168 N N . GLU B 2 522 ? -47.190 22.983 9.517 1.00 185.71 ? 522 GLU B N 1 ATOM 11169 C CA . GLU B 2 522 ? -47.251 23.251 10.951 1.00 187.42 ? 522 GLU B CA 1 ATOM 11170 C C . GLU B 2 522 ? -45.894 23.577 11.588 1.00 176.93 ? 522 GLU B C 1 ATOM 11171 O O . GLU B 2 522 ? -45.839 24.185 12.658 1.00 177.28 ? 522 GLU B O 1 ATOM 11172 C CB . GLU B 2 522 ? -47.878 22.047 11.662 1.00 186.31 ? 522 GLU B CB 1 ATOM 11173 C CG . GLU B 2 522 ? -48.224 22.270 13.125 1.00 188.24 ? 522 GLU B CG 1 ATOM 11174 C CD . GLU B 2 522 ? -48.730 21.009 13.794 1.00 185.63 ? 522 GLU B CD 1 ATOM 11175 O OE1 . GLU B 2 522 ? -48.855 19.978 13.100 1.00 185.28 ? 522 GLU B OE1 1 ATOM 11176 O OE2 . GLU B 2 522 ? -48.999 21.048 15.013 1.00 184.25 ? 522 GLU B OE2 1 ATOM 11177 N N . CYS B 2 523 ? -44.800 23.203 10.929 1.00 163.73 ? 523 CYS B N 1 ATOM 11178 C CA . CYS B 2 523 ? -43.485 23.419 11.520 1.00 146.85 ? 523 CYS B CA 1 ATOM 11179 C C . CYS B 2 523 ? -42.700 24.485 10.768 1.00 157.88 ? 523 CYS B C 1 ATOM 11180 O O . CYS B 2 523 ? -43.140 24.965 9.722 1.00 161.06 ? 523 CYS B O 1 ATOM 11181 C CB . CYS B 2 523 ? -42.693 22.110 11.547 1.00 135.42 ? 523 CYS B CB 1 ATOM 11182 S SG . CYS B 2 523 ? -43.416 20.823 12.588 1.00 203.86 ? 523 CYS B SG 1 ATOM 11183 N N . ASP B 2 524 ? -41.529 24.826 11.301 1.00 173.10 ? 524 ASP B N 1 ATOM 11184 C CA . ASP B 2 524 ? -40.774 25.993 10.848 1.00 180.13 ? 524 ASP B CA 1 ATOM 11185 C C . ASP B 2 524 ? -39.518 26.234 11.677 1.00 172.35 ? 524 ASP B C 1 ATOM 11186 O O . ASP B 2 524 ? -39.184 25.472 12.582 1.00 167.78 ? 524 ASP B O 1 ATOM 11187 C CB . ASP B 2 524 ? -41.639 27.256 10.876 1.00 182.54 ? 524 ASP B CB 1 ATOM 11188 C CG . ASP B 2 524 ? -42.076 27.631 12.272 1.00 176.01 ? 524 ASP B CG 1 ATOM 11189 O OD1 . ASP B 2 524 ? -42.303 26.715 13.091 1.00 172.38 ? 524 ASP B OD1 1 ATOM 11190 O OD2 . ASP B 2 524 ? -42.192 28.843 12.548 1.00 171.50 ? 524 ASP B OD2 1 ATOM 11191 N N . ASP B 2 525 ? -38.832 27.317 11.336 1.00 176.85 ? 525 ASP B N 1 ATOM 11192 C CA . ASP B 2 525 ? -37.729 27.851 12.119 1.00 170.96 ? 525 ASP B CA 1 ATOM 11193 C C . ASP B 2 525 ? -38.253 29.154 12.704 1.00 170.39 ? 525 ASP B C 1 ATOM 11194 O O . ASP B 2 525 ? -39.332 29.581 12.327 1.00 183.88 ? 525 ASP B O 1 ATOM 11195 C CB . ASP B 2 525 ? -36.477 28.083 11.270 1.00 165.73 ? 525 ASP B CB 1 ATOM 11196 C CG . ASP B 2 525 ? -35.874 26.793 10.751 1.00 164.77 ? 525 ASP B CG 1 ATOM 11197 O OD1 . ASP B 2 525 ? -36.097 25.737 11.379 1.00 156.93 ? 525 ASP B OD1 1 ATOM 11198 O OD2 . ASP B 2 525 ? -35.172 26.834 9.719 1.00 173.54 ? 525 ASP B OD2 1 ATOM 11199 N N . PHE B 2 526 ? -37.567 29.674 13.719 1.00 156.90 ? 526 PHE B N 1 ATOM 11200 C CA . PHE B 2 526 ? -37.860 30.950 14.404 1.00 163.43 ? 526 PHE B CA 1 ATOM 11201 C C . PHE B 2 526 ? -39.096 30.898 15.312 1.00 162.12 ? 526 PHE B C 1 ATOM 11202 O O . PHE B 2 526 ? -39.362 31.849 16.046 1.00 169.77 ? 526 PHE B O 1 ATOM 11203 C CB . PHE B 2 526 ? -37.953 32.145 13.398 1.00 166.41 ? 526 PHE B CB 1 ATOM 11204 C CG . PHE B 2 526 ? -39.307 32.335 12.708 1.00 159.85 ? 526 PHE B CG 1 ATOM 11205 C CD1 . PHE B 2 526 ? -40.430 32.773 13.402 1.00 157.02 ? 526 PHE B CD1 1 ATOM 11206 C CD2 . PHE B 2 526 ? -39.419 32.162 11.334 1.00 159.55 ? 526 PHE B CD2 1 ATOM 11207 C CE1 . PHE B 2 526 ? -41.643 32.954 12.760 1.00 155.40 ? 526 PHE B CE1 1 ATOM 11208 C CE2 . PHE B 2 526 ? -40.632 32.342 10.688 1.00 153.94 ? 526 PHE B CE2 1 ATOM 11209 C CZ . PHE B 2 526 ? -41.742 32.744 11.401 1.00 151.50 ? 526 PHE B CZ 1 ATOM 11210 N N . SER B 2 527 ? -39.831 29.793 15.292 1.00 166.87 ? 527 SER B N 1 ATOM 11211 C CA . SER B 2 527 ? -41.019 29.668 16.137 1.00 172.74 ? 527 SER B CA 1 ATOM 11212 C C . SER B 2 527 ? -40.681 29.434 17.610 1.00 169.12 ? 527 SER B C 1 ATOM 11213 O O . SER B 2 527 ? -41.573 29.393 18.458 1.00 165.59 ? 527 SER B O 1 ATOM 11214 C CB . SER B 2 527 ? -41.915 28.538 15.632 1.00 175.16 ? 527 SER B CB 1 ATOM 11215 O OG . SER B 2 527 ? -41.147 27.429 15.199 1.00 172.28 ? 527 SER B OG 1 ATOM 11216 N N . CYS B 2 528 ? -39.395 29.280 17.909 1.00 165.61 ? 528 CYS B N 1 ATOM 11217 C CA . CYS B 2 528 ? -38.951 28.935 19.257 1.00 154.11 ? 528 CYS B CA 1 ATOM 11218 C C . CYS B 2 528 ? -39.095 30.093 20.245 1.00 151.24 ? 528 CYS B C 1 ATOM 11219 O O . CYS B 2 528 ? -39.562 31.175 19.888 1.00 154.92 ? 528 CYS B O 1 ATOM 11220 C CB . CYS B 2 528 ? -37.498 28.461 19.220 1.00 152.80 ? 528 CYS B CB 1 ATOM 11221 S SG . CYS B 2 528 ? -37.191 27.122 18.043 1.00 143.39 ? 528 CYS B SG 1 ATOM 11222 N N . VAL B 2 529 ? -38.686 29.853 21.488 1.00 146.44 ? 529 VAL B N 1 ATOM 11223 C CA . VAL B 2 529 ? -38.852 30.826 22.566 1.00 139.76 ? 529 VAL B CA 1 ATOM 11224 C C . VAL B 2 529 ? -37.618 31.704 22.765 1.00 151.11 ? 529 VAL B C 1 ATOM 11225 O O . VAL B 2 529 ? -36.609 31.540 22.078 1.00 146.79 ? 529 VAL B O 1 ATOM 11226 C CB . VAL B 2 529 ? -39.174 30.123 23.898 1.00 120.47 ? 529 VAL B CB 1 ATOM 11227 C CG1 . VAL B 2 529 ? -40.591 29.571 23.879 1.00 126.83 ? 529 VAL B CG1 1 ATOM 11228 C CG2 . VAL B 2 529 ? -38.168 29.016 24.160 1.00 114.74 ? 529 VAL B CG2 1 ATOM 11229 N N . ARG B 2 530 ? -37.708 32.637 23.713 1.00 153.60 ? 530 ARG B N 1 ATOM 11230 C CA . ARG B 2 530 ? -36.621 33.576 23.990 1.00 129.53 ? 530 ARG B CA 1 ATOM 11231 C C . ARG B 2 530 ? -36.313 33.646 25.487 1.00 123.46 ? 530 ARG B C 1 ATOM 11232 O O . ARG B 2 530 ? -37.164 33.335 26.319 1.00 120.48 ? 530 ARG B O 1 ATOM 11233 C CB . ARG B 2 530 ? -36.968 34.972 23.463 1.00 129.48 ? 530 ARG B CB 1 ATOM 11234 C CG . ARG B 2 530 ? -37.998 34.984 22.340 1.00 138.61 ? 530 ARG B CG 1 ATOM 11235 C CD . ARG B 2 530 ? -38.201 36.378 21.768 1.00 156.56 ? 530 ARG B CD 1 ATOM 11236 N NE . ARG B 2 530 ? -37.159 36.739 20.811 1.00 160.70 ? 530 ARG B NE 1 ATOM 11237 C CZ . ARG B 2 530 ? -37.219 36.475 19.509 1.00 157.51 ? 530 ARG B CZ 1 ATOM 11238 N NH1 . ARG B 2 530 ? -38.273 35.846 19.007 1.00 161.77 ? 530 ARG B NH1 1 ATOM 11239 N NH2 . ARG B 2 530 ? -36.226 36.839 18.709 1.00 150.90 ? 530 ARG B NH2 1 ATOM 11240 N N . TYR B 2 531 ? -35.095 34.064 25.822 1.00 134.26 ? 531 TYR B N 1 ATOM 11241 C CA . TYR B 2 531 ? -34.665 34.154 27.216 1.00 147.24 ? 531 TYR B CA 1 ATOM 11242 C C . TYR B 2 531 ? -34.505 35.610 27.654 1.00 154.48 ? 531 TYR B C 1 ATOM 11243 O O . TYR B 2 531 ? -35.317 36.128 28.420 1.00 165.82 ? 531 TYR B O 1 ATOM 11244 C CB . TYR B 2 531 ? -33.357 33.376 27.412 1.00 147.92 ? 531 TYR B CB 1 ATOM 11245 C CG . TYR B 2 531 ? -32.609 33.665 28.700 1.00 140.41 ? 531 TYR B CG 1 ATOM 11246 C CD1 . TYR B 2 531 ? -33.260 33.662 29.929 1.00 133.63 ? 531 TYR B CD1 1 ATOM 11247 C CD2 . TYR B 2 531 ? -31.242 33.914 28.686 1.00 130.20 ? 531 TYR B CD2 1 ATOM 11248 C CE1 . TYR B 2 531 ? -32.573 33.920 31.103 1.00 127.47 ? 531 TYR B CE1 1 ATOM 11249 C CE2 . TYR B 2 531 ? -30.547 34.169 29.854 1.00 134.07 ? 531 TYR B CE2 1 ATOM 11250 C CZ . TYR B 2 531 ? -31.218 34.172 31.059 1.00 140.26 ? 531 TYR B CZ 1 ATOM 11251 O OH . TYR B 2 531 ? -30.530 34.426 32.224 1.00 147.46 ? 531 TYR B OH 1 ATOM 11252 N N . LYS B 2 532 ? -33.450 36.261 27.177 1.00 132.82 ? 532 LYS B N 1 ATOM 11253 C CA . LYS B 2 532 ? -33.238 37.680 27.443 1.00 131.10 ? 532 LYS B CA 1 ATOM 11254 C C . LYS B 2 532 ? -33.794 38.521 26.301 1.00 151.53 ? 532 LYS B C 1 ATOM 11255 O O . LYS B 2 532 ? -33.594 39.735 26.251 1.00 162.54 ? 532 LYS B O 1 ATOM 11256 C CB . LYS B 2 532 ? -31.755 37.981 27.670 1.00 127.03 ? 532 LYS B CB 1 ATOM 11257 C CG . LYS B 2 532 ? -31.234 37.472 29.007 1.00 122.41 ? 532 LYS B CG 1 ATOM 11258 C CD . LYS B 2 532 ? -29.785 37.864 29.246 1.00 130.15 ? 532 LYS B CD 1 ATOM 11259 C CE . LYS B 2 532 ? -29.645 39.360 29.473 1.00 134.02 ? 532 LYS B CE 1 ATOM 11260 N NZ . LYS B 2 532 ? -28.250 39.734 29.832 1.00 123.66 ? 532 LYS B NZ 1 ATOM 11261 N N . GLY B 2 533 ? -34.494 37.860 25.384 1.00 153.30 ? 533 GLY B N 1 ATOM 11262 C CA . GLY B 2 533 ? -34.961 38.490 24.163 1.00 156.96 ? 533 GLY B CA 1 ATOM 11263 C C . GLY B 2 533 ? -34.221 37.931 22.966 1.00 154.61 ? 533 GLY B C 1 ATOM 11264 O O . GLY B 2 533 ? -34.553 38.222 21.816 1.00 146.61 ? 533 GLY B O 1 ATOM 11265 N N . GLU B 2 534 ? -33.207 37.119 23.248 1.00 157.91 ? 534 GLU B N 1 ATOM 11266 C CA . GLU B 2 534 ? -32.486 36.392 22.213 1.00 154.14 ? 534 GLU B CA 1 ATOM 11267 C C . GLU B 2 534 ? -33.046 34.974 22.112 1.00 154.01 ? 534 GLU B C 1 ATOM 11268 O O . GLU B 2 534 ? -33.092 34.251 23.108 1.00 155.17 ? 534 GLU B O 1 ATOM 11269 C CB . GLU B 2 534 ? -30.988 36.370 22.524 1.00 138.95 ? 534 GLU B CB 1 ATOM 11270 C CG . GLU B 2 534 ? -30.105 35.959 21.360 1.00 146.61 ? 534 GLU B CG 1 ATOM 11271 C CD . GLU B 2 534 ? -28.631 36.156 21.659 1.00 149.50 ? 534 GLU B CD 1 ATOM 11272 O OE1 . GLU B 2 534 ? -28.294 36.430 22.831 1.00 139.26 ? 534 GLU B OE1 1 ATOM 11273 O OE2 . GLU B 2 534 ? -27.811 36.043 20.723 1.00 150.29 ? 534 GLU B OE2 1 ATOM 11274 N N . MET B 2 535 ? -33.483 34.587 20.916 1.00 148.35 ? 535 MET B N 1 ATOM 11275 C CA . MET B 2 535 ? -34.107 33.281 20.711 1.00 142.38 ? 535 MET B CA 1 ATOM 11276 C C . MET B 2 535 ? -33.152 32.142 21.039 1.00 132.91 ? 535 MET B C 1 ATOM 11277 O O . MET B 2 535 ? -32.030 32.105 20.530 1.00 134.88 ? 535 MET B O 1 ATOM 11278 C CB . MET B 2 535 ? -34.596 33.137 19.270 1.00 159.44 ? 535 MET B CB 1 ATOM 11279 C CG . MET B 2 535 ? -35.244 31.792 18.976 1.00 160.41 ? 535 MET B CG 1 ATOM 11280 S SD . MET B 2 535 ? -35.721 31.620 17.249 1.00 142.09 ? 535 MET B SD 1 ATOM 11281 C CE . MET B 2 535 ? -36.584 33.170 16.995 1.00 165.37 ? 535 MET B CE 1 ATOM 11282 N N . CYS B 2 536 ? -33.599 31.238 21.912 1.00 125.52 ? 536 CYS B N 1 ATOM 11283 C CA . CYS B 2 536 ? -32.807 30.081 22.344 1.00 129.47 ? 536 CYS B CA 1 ATOM 11284 C C . CYS B 2 536 ? -31.585 30.508 23.155 1.00 137.52 ? 536 CYS B C 1 ATOM 11285 O O . CYS B 2 536 ? -30.794 29.660 23.575 1.00 137.42 ? 536 CYS B O 1 ATOM 11286 C CB . CYS B 2 536 ? -32.379 29.220 21.149 1.00 126.39 ? 536 CYS B CB 1 ATOM 11287 S SG . CYS B 2 536 ? -33.683 28.154 20.491 1.00 144.33 ? 536 CYS B SG 1 ATOM 11288 N N . SER B 2 537 ? -31.438 31.825 23.326 1.00 136.89 ? 537 SER B N 1 ATOM 11289 C CA . SER B 2 537 ? -30.277 32.484 23.934 1.00 123.29 ? 537 SER B CA 1 ATOM 11290 C C . SER B 2 537 ? -29.117 32.516 22.941 1.00 125.37 ? 537 SER B C 1 ATOM 11291 O O . SER B 2 537 ? -28.055 33.065 23.231 1.00 125.84 ? 537 SER B O 1 ATOM 11292 C CB . SER B 2 537 ? -29.851 31.806 25.242 1.00 118.39 ? 537 SER B CB 1 ATOM 11293 O OG . SER B 2 537 ? -30.966 31.564 26.083 1.00 109.38 ? 537 SER B OG 1 ATOM 11294 N N . GLY B 2 538 ? -29.331 31.924 21.770 1.00 136.85 ? 538 GLY B N 1 ATOM 11295 C CA . GLY B 2 538 ? -28.290 31.800 20.768 1.00 142.95 ? 538 GLY B CA 1 ATOM 11296 C C . GLY B 2 538 ? -27.484 30.544 21.027 1.00 151.82 ? 538 GLY B C 1 ATOM 11297 O O . GLY B 2 538 ? -26.544 30.225 20.300 1.00 159.66 ? 538 GLY B O 1 ATOM 11298 N N . HIS B 2 539 ? -27.867 29.833 22.082 1.00 143.16 ? 539 HIS B N 1 ATOM 11299 C CA . HIS B 2 539 ? -27.166 28.635 22.516 1.00 131.70 ? 539 HIS B CA 1 ATOM 11300 C C . HIS B 2 539 ? -27.801 27.361 21.971 1.00 129.26 ? 539 HIS B C 1 ATOM 11301 O O . HIS B 2 539 ? -27.388 26.257 22.323 1.00 135.23 ? 539 HIS B O 1 ATOM 11302 C CB . HIS B 2 539 ? -27.113 28.587 24.041 1.00 127.61 ? 539 HIS B CB 1 ATOM 11303 C CG . HIS B 2 539 ? -26.440 29.775 24.652 1.00 128.11 ? 539 HIS B CG 1 ATOM 11304 N ND1 . HIS B 2 539 ? -25.393 30.431 24.041 1.00 134.44 ? 539 HIS B ND1 1 ATOM 11305 C CD2 . HIS B 2 539 ? -26.671 30.433 25.812 1.00 133.76 ? 539 HIS B CD2 1 ATOM 11306 C CE1 . HIS B 2 539 ? -25.003 31.438 24.802 1.00 138.33 ? 539 HIS B CE1 1 ATOM 11307 N NE2 . HIS B 2 539 ? -25.763 31.461 25.883 1.00 140.03 ? 539 HIS B NE2 1 ATOM 11308 N N . GLY B 2 540 ? -28.813 27.510 21.123 1.00 127.98 ? 540 GLY B N 1 ATOM 11309 C CA . GLY B 2 540 ? -29.435 26.356 20.504 1.00 136.97 ? 540 GLY B CA 1 ATOM 11310 C C . GLY B 2 540 ? -30.084 26.639 19.164 1.00 147.06 ? 540 GLY B C 1 ATOM 11311 O O . GLY B 2 540 ? -30.475 27.770 18.876 1.00 134.44 ? 540 GLY B O 1 ATOM 11312 N N . GLN B 2 541 ? -30.195 25.596 18.346 1.00 170.27 ? 541 GLN B N 1 ATOM 11313 C CA . GLN B 2 541 ? -30.851 25.679 17.043 1.00 178.17 ? 541 GLN B CA 1 ATOM 11314 C C . GLN B 2 541 ? -32.363 25.565 17.187 1.00 174.41 ? 541 GLN B C 1 ATOM 11315 O O . GLN B 2 541 ? -32.856 24.891 18.089 1.00 178.59 ? 541 GLN B O 1 ATOM 11316 C CB . GLN B 2 541 ? -30.333 24.583 16.107 1.00 179.08 ? 541 GLN B CB 1 ATOM 11317 C CG . GLN B 2 541 ? -28.863 24.705 15.745 1.00 183.91 ? 541 GLN B CG 1 ATOM 11318 C CD . GLN B 2 541 ? -28.384 23.562 14.872 1.00 184.37 ? 541 GLN B CD 1 ATOM 11319 O OE1 . GLN B 2 541 ? -28.969 22.478 14.872 1.00 181.60 ? 541 GLN B OE1 1 ATOM 11320 N NE2 . GLN B 2 541 ? -27.318 23.800 14.117 1.00 186.43 ? 541 GLN B NE2 1 ATOM 11321 N N . CYS B 2 542 ? -33.098 26.219 16.293 1.00 171.91 ? 542 CYS B N 1 ATOM 11322 C CA . CYS B 2 542 ? -34.554 26.168 16.335 1.00 162.64 ? 542 CYS B CA 1 ATOM 11323 C C . CYS B 2 542 ? -35.115 25.216 15.284 1.00 160.20 ? 542 CYS B C 1 ATOM 11324 O O . CYS B 2 542 ? -35.083 25.506 14.088 1.00 159.10 ? 542 CYS B O 1 ATOM 11325 C CB . CYS B 2 542 ? -35.144 27.565 16.137 1.00 167.91 ? 542 CYS B CB 1 ATOM 11326 S SG . CYS B 2 542 ? -36.949 27.603 16.084 1.00 148.83 ? 542 CYS B SG 1 ATOM 11327 N N . SER B 2 543 ? -35.635 24.081 15.741 1.00 157.83 ? 543 SER B N 1 ATOM 11328 C CA . SER B 2 543 ? -36.246 23.104 14.849 1.00 151.66 ? 543 SER B CA 1 ATOM 11329 C C . SER B 2 543 ? -37.701 22.844 15.226 1.00 139.79 ? 543 SER B C 1 ATOM 11330 O O . SER B 2 543 ? -37.982 22.237 16.260 1.00 131.27 ? 543 SER B O 1 ATOM 11331 C CB . SER B 2 543 ? -35.455 21.795 14.870 1.00 150.54 ? 543 SER B CB 1 ATOM 11332 O OG . SER B 2 543 ? -36.092 20.799 14.089 1.00 156.01 ? 543 SER B OG 1 ATOM 11333 N N . CYS B 2 544 ? -38.612 23.292 14.365 1.00 136.38 ? 544 CYS B N 1 ATOM 11334 C CA . CYS B 2 544 ? -40.052 23.118 14.554 1.00 136.75 ? 544 CYS B CA 1 ATOM 11335 C C . CYS B 2 544 ? -40.521 23.523 15.952 1.00 138.96 ? 544 CYS B C 1 ATOM 11336 O O . CYS B 2 544 ? -41.009 22.692 16.718 1.00 141.80 ? 544 CYS B O 1 ATOM 11337 C CB . CYS B 2 544 ? -40.448 21.667 14.271 1.00 138.25 ? 544 CYS B CB 1 ATOM 11338 S SG . CYS B 2 544 ? -42.228 21.392 14.134 1.00 175.63 ? 544 CYS B SG 1 ATOM 11339 N N . GLY B 2 545 ? -40.366 24.802 16.279 1.00 141.72 ? 545 GLY B N 1 ATOM 11340 C CA . GLY B 2 545 ? -40.842 25.339 17.543 1.00 140.82 ? 545 GLY B CA 1 ATOM 11341 C C . GLY B 2 545 ? -40.092 24.869 18.776 1.00 137.94 ? 545 GLY B C 1 ATOM 11342 O O . GLY B 2 545 ? -40.417 25.270 19.893 1.00 134.47 ? 545 GLY B O 1 ATOM 11343 N N . ASP B 2 546 ? -39.087 24.022 18.578 1.00 139.66 ? 546 ASP B N 1 ATOM 11344 C CA . ASP B 2 546 ? -38.333 23.460 19.692 1.00 138.58 ? 546 ASP B CA 1 ATOM 11345 C C . ASP B 2 546 ? -36.837 23.708 19.526 1.00 135.96 ? 546 ASP B C 1 ATOM 11346 O O . ASP B 2 546 ? -36.342 23.837 18.407 1.00 143.81 ? 546 ASP B O 1 ATOM 11347 C CB . ASP B 2 546 ? -38.613 21.962 19.820 1.00 139.72 ? 546 ASP B CB 1 ATOM 11348 C CG . ASP B 2 546 ? -40.086 21.663 20.030 1.00 146.98 ? 546 ASP B CG 1 ATOM 11349 O OD1 . ASP B 2 546 ? -40.753 22.436 20.749 1.00 149.16 ? 546 ASP B OD1 1 ATOM 11350 O OD2 . ASP B 2 546 ? -40.577 20.659 19.472 1.00 145.74 ? 546 ASP B OD2 1 ATOM 11351 N N . CYS B 2 547 ? -36.121 23.768 20.644 1.00 127.26 ? 547 CYS B N 1 ATOM 11352 C CA . CYS B 2 547 ? -34.702 24.103 20.619 1.00 125.37 ? 547 CYS B CA 1 ATOM 11353 C C . CYS B 2 547 ? -33.786 22.886 20.717 1.00 129.17 ? 547 CYS B C 1 ATOM 11354 O O . CYS B 2 547 ? -33.900 22.080 21.639 1.00 117.66 ? 547 CYS B O 1 ATOM 11355 C CB . CYS B 2 547 ? -34.372 25.082 21.748 1.00 125.97 ? 547 CYS B CB 1 ATOM 11356 S SG . CYS B 2 547 ? -34.866 26.792 21.427 1.00 168.17 ? 547 CYS B SG 1 ATOM 11357 N N . LEU B 2 548 ? -32.872 22.770 19.758 1.00 134.27 ? 548 LEU B N 1 ATOM 11358 C CA . LEU B 2 548 ? -31.814 21.772 19.820 1.00 140.67 ? 548 LEU B CA 1 ATOM 11359 C C . LEU B 2 548 ? -30.533 22.459 20.274 1.00 137.96 ? 548 LEU B C 1 ATOM 11360 O O . LEU B 2 548 ? -29.920 23.214 19.520 1.00 137.72 ? 548 LEU B O 1 ATOM 11361 C CB . LEU B 2 548 ? -31.614 21.096 18.463 1.00 150.21 ? 548 LEU B CB 1 ATOM 11362 C CG . LEU B 2 548 ? -32.840 20.409 17.857 1.00 148.87 ? 548 LEU B CG 1 ATOM 11363 C CD1 . LEU B 2 548 ? -32.483 19.749 16.534 1.00 154.53 ? 548 LEU B CD1 1 ATOM 11364 C CD2 . LEU B 2 548 ? -33.421 19.396 18.831 1.00 142.87 ? 548 LEU B CD2 1 ATOM 11365 N N . CYS B 2 549 ? -30.123 22.176 21.505 1.00 131.18 ? 549 CYS B N 1 ATOM 11366 C CA . CYS B 2 549 ? -29.078 22.950 22.160 1.00 123.59 ? 549 CYS B CA 1 ATOM 11367 C C . CYS B 2 549 ? -27.671 22.635 21.665 1.00 126.47 ? 549 CYS B C 1 ATOM 11368 O O . CYS B 2 549 ? -27.364 21.502 21.294 1.00 131.72 ? 549 CYS B O 1 ATOM 11369 C CB . CYS B 2 549 ? -29.144 22.734 23.672 1.00 122.73 ? 549 CYS B CB 1 ATOM 11370 S SG . CYS B 2 549 ? -30.713 23.206 24.427 1.00 136.70 ? 549 CYS B SG 1 ATOM 11371 N N . ASP B 2 550 ? -26.823 23.660 21.669 1.00 129.63 ? 550 ASP B N 1 ATOM 11372 C CA . ASP B 2 550 ? -25.403 23.509 21.375 1.00 127.36 ? 550 ASP B CA 1 ATOM 11373 C C . ASP B 2 550 ? -24.714 22.733 22.487 1.00 125.91 ? 550 ASP B C 1 ATOM 11374 O O . ASP B 2 550 ? -25.253 22.608 23.587 1.00 122.11 ? 550 ASP B O 1 ATOM 11375 C CB . ASP B 2 550 ? -24.732 24.873 21.198 1.00 126.72 ? 550 ASP B CB 1 ATOM 11376 C CG . ASP B 2 550 ? -25.073 25.526 19.875 1.00 134.07 ? 550 ASP B CG 1 ATOM 11377 O OD1 . ASP B 2 550 ? -26.079 26.262 19.815 1.00 127.33 ? 550 ASP B OD1 1 ATOM 11378 O OD2 . ASP B 2 550 ? -24.331 25.305 18.895 1.00 148.34 ? 550 ASP B OD2 1 ATOM 11379 N N . SER B 2 551 ? -23.528 22.207 22.190 1.00 128.93 ? 551 SER B N 1 ATOM 11380 C CA . SER B 2 551 ? -22.736 21.472 23.171 1.00 127.39 ? 551 SER B CA 1 ATOM 11381 C C . SER B 2 551 ? -22.578 22.278 24.457 1.00 129.07 ? 551 SER B C 1 ATOM 11382 O O . SER B 2 551 ? -22.388 23.493 24.414 1.00 142.26 ? 551 SER B O 1 ATOM 11383 C CB . SER B 2 551 ? -21.360 21.122 22.598 1.00 126.75 ? 551 SER B CB 1 ATOM 11384 O OG . SER B 2 551 ? -21.475 20.353 21.413 1.00 135.49 ? 551 SER B OG 1 ATOM 11385 N N . ASP B 2 552 ? -22.693 21.588 25.589 1.00 126.77 ? 552 ASP B N 1 ATOM 11386 C CA . ASP B 2 552 ? -22.578 22.192 26.916 1.00 124.62 ? 552 ASP B CA 1 ATOM 11387 C C . ASP B 2 552 ? -23.699 23.195 27.199 1.00 116.94 ? 552 ASP B C 1 ATOM 11388 O O . ASP B 2 552 ? -23.519 24.146 27.957 1.00 116.42 ? 552 ASP B O 1 ATOM 11389 C CB . ASP B 2 552 ? -21.211 22.860 27.084 1.00 125.42 ? 552 ASP B CB 1 ATOM 11390 C CG . ASP B 2 552 ? -20.068 21.937 26.718 1.00 137.27 ? 552 ASP B CG 1 ATOM 11391 O OD1 . ASP B 2 552 ? -20.082 20.768 27.159 1.00 148.12 ? 552 ASP B OD1 1 ATOM 11392 O OD2 . ASP B 2 552 ? -19.163 22.376 25.979 1.00 139.43 ? 552 ASP B OD2 1 ATOM 11393 N N . TRP B 2 553 ? -24.857 22.969 26.588 1.00 117.95 ? 553 TRP B N 1 ATOM 11394 C CA . TRP B 2 553 ? -26.055 23.744 26.895 1.00 118.39 ? 553 TRP B CA 1 ATOM 11395 C C . TRP B 2 553 ? -27.265 22.822 26.985 1.00 117.99 ? 553 TRP B C 1 ATOM 11396 O O . TRP B 2 553 ? -27.428 21.924 26.162 1.00 125.85 ? 553 TRP B O 1 ATOM 11397 C CB . TRP B 2 553 ? -26.300 24.826 25.839 1.00 132.98 ? 553 TRP B CB 1 ATOM 11398 C CG . TRP B 2 553 ? -25.293 25.933 25.856 1.00 126.13 ? 553 TRP B CG 1 ATOM 11399 C CD1 . TRP B 2 553 ? -24.245 26.100 25.000 1.00 121.48 ? 553 TRP B CD1 1 ATOM 11400 C CD2 . TRP B 2 553 ? -25.237 27.030 26.776 1.00 123.89 ? 553 TRP B CD2 1 ATOM 11401 N NE1 . TRP B 2 553 ? -23.541 27.231 25.329 1.00 121.14 ? 553 TRP B NE1 1 ATOM 11402 C CE2 . TRP B 2 553 ? -24.129 27.821 26.417 1.00 118.84 ? 553 TRP B CE2 1 ATOM 11403 C CE3 . TRP B 2 553 ? -26.018 27.419 27.870 1.00 124.59 ? 553 TRP B CE3 1 ATOM 11404 C CZ2 . TRP B 2 553 ? -23.780 28.978 27.110 1.00 117.63 ? 553 TRP B CZ2 1 ATOM 11405 C CZ3 . TRP B 2 553 ? -25.673 28.569 28.555 1.00 118.24 ? 553 TRP B CZ3 1 ATOM 11406 C CH2 . TRP B 2 553 ? -24.561 29.333 28.175 1.00 118.03 ? 553 TRP B CH2 1 ATOM 11407 N N . THR B 2 554 ? -28.106 23.037 27.992 1.00 118.01 ? 554 THR B N 1 ATOM 11408 C CA . THR B 2 554 ? -29.322 22.246 28.159 1.00 117.48 ? 554 THR B CA 1 ATOM 11409 C C . THR B 2 554 ? -30.490 23.130 28.575 1.00 113.19 ? 554 THR B C 1 ATOM 11410 O O . THR B 2 554 ? -30.329 24.335 28.766 1.00 111.81 ? 554 THR B O 1 ATOM 11411 C CB . THR B 2 554 ? -29.144 21.128 29.209 1.00 110.51 ? 554 THR B CB 1 ATOM 11412 O OG1 . THR B 2 554 ? -28.690 21.696 30.444 1.00 108.13 ? 554 THR B OG1 1 ATOM 11413 C CG2 . THR B 2 554 ? -28.141 20.085 28.729 1.00 111.73 ? 554 THR B CG2 1 ATOM 11414 N N . GLY B 2 555 ? -31.664 22.525 28.723 1.00 109.94 ? 555 GLY B N 1 ATOM 11415 C CA . GLY B 2 555 ? -32.853 23.257 29.120 1.00 105.08 ? 555 GLY B CA 1 ATOM 11416 C C . GLY B 2 555 ? -33.757 23.621 27.957 1.00 106.45 ? 555 GLY B C 1 ATOM 11417 O O . GLY B 2 555 ? -33.351 23.570 26.795 1.00 110.22 ? 555 GLY B O 1 ATOM 11418 N N . TYR B 2 556 ? -34.992 23.993 28.279 1.00 104.93 ? 556 TYR B N 1 ATOM 11419 C CA . TYR B 2 556 ? -35.984 24.364 27.275 1.00 106.82 ? 556 TYR B CA 1 ATOM 11420 C C . TYR B 2 556 ? -35.547 25.606 26.509 1.00 109.98 ? 556 TYR B C 1 ATOM 11421 O O . TYR B 2 556 ? -35.718 25.689 25.293 1.00 107.29 ? 556 TYR B O 1 ATOM 11422 C CB . TYR B 2 556 ? -37.343 24.599 27.940 1.00 114.26 ? 556 TYR B CB 1 ATOM 11423 C CG . TYR B 2 556 ? -38.495 24.825 26.983 1.00 135.96 ? 556 TYR B CG 1 ATOM 11424 C CD1 . TYR B 2 556 ? -38.898 26.110 26.638 1.00 138.66 ? 556 TYR B CD1 1 ATOM 11425 C CD2 . TYR B 2 556 ? -39.192 23.753 26.438 1.00 134.62 ? 556 TYR B CD2 1 ATOM 11426 C CE1 . TYR B 2 556 ? -39.956 26.320 25.770 1.00 132.47 ? 556 TYR B CE1 1 ATOM 11427 C CE2 . TYR B 2 556 ? -40.251 23.954 25.570 1.00 132.65 ? 556 TYR B CE2 1 ATOM 11428 C CZ . TYR B 2 556 ? -40.628 25.239 25.239 1.00 133.78 ? 556 TYR B CZ 1 ATOM 11429 O OH . TYR B 2 556 ? -41.680 25.443 24.376 1.00 138.34 ? 556 TYR B OH 1 ATOM 11430 N N . TYR B 2 557 ? -34.978 26.564 27.235 1.00 125.41 ? 557 TYR B N 1 ATOM 11431 C CA . TYR B 2 557 ? -34.529 27.823 26.649 1.00 126.53 ? 557 TYR B CA 1 ATOM 11432 C C . TYR B 2 557 ? -33.053 27.766 26.257 1.00 126.91 ? 557 TYR B C 1 ATOM 11433 O O . TYR B 2 557 ? -32.509 28.733 25.720 1.00 134.63 ? 557 TYR B O 1 ATOM 11434 C CB . TYR B 2 557 ? -34.768 28.979 27.626 1.00 127.98 ? 557 TYR B CB 1 ATOM 11435 C CG . TYR B 2 557 ? -36.226 29.229 27.958 1.00 127.35 ? 557 TYR B CG 1 ATOM 11436 C CD1 . TYR B 2 557 ? -36.978 30.140 27.226 1.00 125.83 ? 557 TYR B CD1 1 ATOM 11437 C CD2 . TYR B 2 557 ? -36.847 28.562 29.007 1.00 121.12 ? 557 TYR B CD2 1 ATOM 11438 C CE1 . TYR B 2 557 ? -38.309 30.375 27.524 1.00 125.50 ? 557 TYR B CE1 1 ATOM 11439 C CE2 . TYR B 2 557 ? -38.178 28.791 29.314 1.00 120.34 ? 557 TYR B CE2 1 ATOM 11440 C CZ . TYR B 2 557 ? -38.904 29.699 28.569 1.00 125.42 ? 557 TYR B CZ 1 ATOM 11441 O OH . TYR B 2 557 ? -40.227 29.930 28.869 1.00 119.17 ? 557 TYR B OH 1 ATOM 11442 N N . CYS B 2 558 ? -32.418 26.630 26.538 1.00 130.42 ? 558 CYS B N 1 ATOM 11443 C CA . CYS B 2 558 ? -31.001 26.402 26.248 1.00 125.45 ? 558 CYS B CA 1 ATOM 11444 C C . CYS B 2 558 ? -30.076 27.390 26.956 1.00 124.19 ? 558 CYS B C 1 ATOM 11445 O O . CYS B 2 558 ? -28.961 27.634 26.498 1.00 129.27 ? 558 CYS B O 1 ATOM 11446 C CB . CYS B 2 558 ? -30.741 26.456 24.739 1.00 124.83 ? 558 CYS B CB 1 ATOM 11447 S SG . CYS B 2 558 ? -31.358 25.035 23.818 1.00 133.92 ? 558 CYS B SG 1 ATOM 11448 N N . ASN B 2 559 ? -30.536 27.960 28.065 1.00 120.59 ? 559 ASN B N 1 ATOM 11449 C CA . ASN B 2 559 ? -29.714 28.893 28.829 1.00 120.83 ? 559 ASN B CA 1 ATOM 11450 C C . ASN B 2 559 ? -29.016 28.244 30.027 1.00 124.80 ? 559 ASN B C 1 ATOM 11451 O O . ASN B 2 559 ? -28.340 28.923 30.800 1.00 136.01 ? 559 ASN B O 1 ATOM 11452 C CB . ASN B 2 559 ? -30.556 30.088 29.289 1.00 122.35 ? 559 ASN B CB 1 ATOM 11453 C CG . ASN B 2 559 ? -31.757 29.681 30.115 1.00 126.94 ? 559 ASN B CG 1 ATOM 11454 O OD1 . ASN B 2 559 ? -32.133 28.510 30.157 1.00 127.93 ? 559 ASN B OD1 1 ATOM 11455 N ND2 . ASN B 2 559 ? -32.374 30.656 30.775 1.00 135.06 ? 559 ASN B ND2 1 ATOM 11456 N N . CYS B 2 560 ? -29.180 26.933 30.181 1.00 116.70 ? 560 CYS B N 1 ATOM 11457 C CA . CYS B 2 560 ? -28.571 26.215 31.299 1.00 110.49 ? 560 CYS B CA 1 ATOM 11458 C C . CYS B 2 560 ? -27.276 25.503 30.906 1.00 117.50 ? 560 CYS B C 1 ATOM 11459 O O . CYS B 2 560 ? -27.267 24.667 30.003 1.00 121.74 ? 560 CYS B O 1 ATOM 11460 C CB . CYS B 2 560 ? -29.557 25.201 31.880 1.00 104.33 ? 560 CYS B CB 1 ATOM 11461 S SG . CYS B 2 560 ? -28.906 24.254 33.275 1.00 153.97 ? 560 CYS B SG 1 ATOM 11462 N N . THR B 2 561 ? -26.188 25.841 31.593 1.00 125.40 ? 561 THR B N 1 ATOM 11463 C CA . THR B 2 561 ? -24.880 25.237 31.338 1.00 128.92 ? 561 THR B CA 1 ATOM 11464 C C . THR B 2 561 ? -24.724 23.854 31.968 1.00 119.80 ? 561 THR B C 1 ATOM 11465 O O . THR B 2 561 ? -25.415 23.509 32.926 1.00 117.30 ? 561 THR B O 1 ATOM 11466 C CB . THR B 2 561 ? -23.728 26.124 31.859 1.00 133.94 ? 561 THR B CB 1 ATOM 11467 O OG1 . THR B 2 561 ? -23.906 26.370 33.259 1.00 145.13 ? 561 THR B OG1 1 ATOM 11468 C CG2 . THR B 2 561 ? -23.687 27.445 31.123 1.00 143.13 ? 561 THR B CG2 1 ATOM 11469 N N . THR B 2 562 ? -23.817 23.064 31.405 1.00 112.61 ? 562 THR B N 1 ATOM 11470 C CA . THR B 2 562 ? -23.427 21.792 31.994 1.00 113.38 ? 562 THR B CA 1 ATOM 11471 C C . THR B 2 562 ? -22.157 21.968 32.820 1.00 112.12 ? 562 THR B C 1 ATOM 11472 O O . THR B 2 562 ? -21.628 21.009 33.389 1.00 104.48 ? 562 THR B O 1 ATOM 11473 C CB . THR B 2 562 ? -23.190 20.724 30.919 1.00 124.26 ? 562 THR B CB 1 ATOM 11474 O OG1 . THR B 2 562 ? -22.053 21.087 30.126 1.00 122.75 ? 562 THR B OG1 1 ATOM 11475 C CG2 . THR B 2 562 ? -24.412 20.598 30.021 1.00 123.30 ? 562 THR B CG2 1 ATOM 11476 N N . ARG B 2 563 ? -21.676 23.207 32.877 1.00 107.26 ? 563 ARG B N 1 ATOM 11477 C CA . ARG B 2 563 ? -20.395 23.520 33.502 1.00 109.23 ? 563 ARG B CA 1 ATOM 11478 C C . ARG B 2 563 ? -20.445 23.457 35.024 1.00 109.04 ? 563 ARG B C 1 ATOM 11479 O O . ARG B 2 563 ? -21.265 24.121 35.655 1.00 106.18 ? 563 ARG B O 1 ATOM 11480 C CB . ARG B 2 563 ? -19.928 24.907 33.063 1.00 107.98 ? 563 ARG B CB 1 ATOM 11481 C CG . ARG B 2 563 ? -19.722 25.049 31.567 1.00 116.36 ? 563 ARG B CG 1 ATOM 11482 C CD . ARG B 2 563 ? -19.457 26.495 31.196 1.00 122.06 ? 563 ARG B CD 1 ATOM 11483 N NE . ARG B 2 563 ? -18.408 27.081 32.025 1.00 122.34 ? 563 ARG B NE 1 ATOM 11484 C CZ . ARG B 2 563 ? -18.015 28.347 31.946 1.00 119.14 ? 563 ARG B CZ 1 ATOM 11485 N NH1 . ARG B 2 563 ? -18.585 29.165 31.071 1.00 120.86 ? 563 ARG B NH1 1 ATOM 11486 N NH2 . ARG B 2 563 ? -17.052 28.797 32.740 1.00 111.24 ? 563 ARG B NH2 1 ATOM 11487 N N . THR B 2 564 ? -19.569 22.646 35.606 1.00 128.13 ? 564 THR B N 1 ATOM 11488 C CA . THR B 2 564 ? -19.450 22.560 37.057 1.00 116.63 ? 564 THR B CA 1 ATOM 11489 C C . THR B 2 564 ? -18.295 23.398 37.598 1.00 122.22 ? 564 THR B C 1 ATOM 11490 O O . THR B 2 564 ? -18.102 23.482 38.811 1.00 118.36 ? 564 THR B O 1 ATOM 11491 C CB . THR B 2 564 ? -19.253 21.106 37.514 1.00 102.68 ? 564 THR B CB 1 ATOM 11492 O OG1 . THR B 2 564 ? -18.053 20.581 36.930 1.00 101.38 ? 564 THR B OG1 1 ATOM 11493 C CG2 . THR B 2 564 ? -20.439 20.254 37.090 1.00 101.01 ? 564 THR B CG2 1 ATOM 11494 N N . ASP B 2 565 ? -17.533 24.018 36.702 1.00 134.22 ? 565 ASP B N 1 ATOM 11495 C CA . ASP B 2 565 ? -16.297 24.693 37.093 1.00 134.44 ? 565 ASP B CA 1 ATOM 11496 C C . ASP B 2 565 ? -16.551 25.952 37.917 1.00 117.37 ? 565 ASP B C 1 ATOM 11497 O O . ASP B 2 565 ? -15.737 26.319 38.764 1.00 121.48 ? 565 ASP B O 1 ATOM 11498 C CB . ASP B 2 565 ? -15.457 25.036 35.859 1.00 134.25 ? 565 ASP B CB 1 ATOM 11499 C CG . ASP B 2 565 ? -16.225 25.845 34.837 1.00 139.05 ? 565 ASP B CG 1 ATOM 11500 O OD1 . ASP B 2 565 ? -16.249 27.088 34.957 1.00 132.56 ? 565 ASP B OD1 1 ATOM 11501 O OD2 . ASP B 2 565 ? -16.798 25.237 33.909 1.00 154.51 ? 565 ASP B OD2 1 ATOM 11502 N N . THR B 2 566 ? -17.677 26.611 37.673 1.00 116.01 ? 566 THR B N 1 ATOM 11503 C CA . THR B 2 566 ? -18.032 27.795 38.447 1.00 108.17 ? 566 THR B CA 1 ATOM 11504 C C . THR B 2 566 ? -18.695 27.396 39.760 1.00 103.94 ? 566 THR B C 1 ATOM 11505 O O . THR B 2 566 ? -18.936 28.237 40.625 1.00 100.35 ? 566 THR B O 1 ATOM 11506 C CB . THR B 2 566 ? -18.969 28.735 37.663 1.00 106.96 ? 566 THR B CB 1 ATOM 11507 O OG1 . THR B 2 566 ? -20.128 28.013 37.230 1.00 110.90 ? 566 THR B OG1 1 ATOM 11508 C CG2 . THR B 2 566 ? -18.254 29.308 36.451 1.00 111.21 ? 566 THR B CG2 1 ATOM 11509 N N . CYS B 2 567 ? -18.997 26.110 39.898 1.00 102.78 ? 567 CYS B N 1 ATOM 11510 C CA . CYS B 2 567 ? -19.536 25.584 41.145 1.00 101.35 ? 567 CYS B CA 1 ATOM 11511 C C . CYS B 2 567 ? -18.410 25.066 42.030 1.00 120.85 ? 567 CYS B C 1 ATOM 11512 O O . CYS B 2 567 ? -18.636 24.676 43.175 1.00 120.06 ? 567 CYS B O 1 ATOM 11513 C CB . CYS B 2 567 ? -20.545 24.466 40.875 1.00 100.35 ? 567 CYS B CB 1 ATOM 11514 S SG . CYS B 2 567 ? -22.003 24.955 39.927 1.00 107.93 ? 567 CYS B SG 1 ATOM 11515 N N . MET B 2 568 ? -17.194 25.072 41.492 1.00 142.04 ? 568 MET B N 1 ATOM 11516 C CA . MET B 2 568 ? -16.044 24.499 42.183 1.00 136.30 ? 568 MET B CA 1 ATOM 11517 C C . MET B 2 568 ? -15.485 25.459 43.226 1.00 133.95 ? 568 MET B C 1 ATOM 11518 O O . MET B 2 568 ? -15.166 26.607 42.917 1.00 135.53 ? 568 MET B O 1 ATOM 11519 C CB . MET B 2 568 ? -14.952 24.124 41.181 1.00 131.21 ? 568 MET B CB 1 ATOM 11520 C CG . MET B 2 568 ? -14.062 22.984 41.637 1.00 136.68 ? 568 MET B CG 1 ATOM 11521 S SD . MET B 2 568 ? -14.993 21.452 41.818 1.00 159.94 ? 568 MET B SD 1 ATOM 11522 C CE . MET B 2 568 ? -15.657 21.264 40.164 1.00 135.75 ? 568 MET B CE 1 ATOM 11523 N N . SER B 2 569 ? -15.365 24.982 44.460 1.00 140.53 ? 569 SER B N 1 ATOM 11524 C CA . SER B 2 569 ? -14.845 25.804 45.546 1.00 132.17 ? 569 SER B CA 1 ATOM 11525 C C . SER B 2 569 ? -13.324 25.722 45.619 1.00 138.19 ? 569 SER B C 1 ATOM 11526 O O . SER B 2 569 ? -12.687 25.061 44.798 1.00 130.41 ? 569 SER B O 1 ATOM 11527 C CB . SER B 2 569 ? -15.461 25.382 46.881 1.00 127.64 ? 569 SER B CB 1 ATOM 11528 O OG . SER B 2 569 ? -15.005 26.212 47.936 1.00 130.82 ? 569 SER B OG 1 ATOM 11529 N N . SER B 2 570 ? -12.750 26.397 46.610 1.00 132.95 ? 570 SER B N 1 ATOM 11530 C CA . SER B 2 570 ? -11.301 26.453 46.765 1.00 127.53 ? 570 SER B CA 1 ATOM 11531 C C . SER B 2 570 ? -10.750 25.216 47.468 1.00 132.27 ? 570 SER B C 1 ATOM 11532 O O . SER B 2 570 ? -9.553 24.938 47.402 1.00 140.51 ? 570 SER B O 1 ATOM 11533 C CB . SER B 2 570 ? -10.900 27.711 47.538 1.00 131.52 ? 570 SER B CB 1 ATOM 11534 O OG . SER B 2 570 ? -11.521 27.747 48.811 1.00 139.00 ? 570 SER B OG 1 ATOM 11535 N N . ASN B 2 571 ? -11.626 24.475 48.138 1.00 129.31 ? 571 ASN B N 1 ATOM 11536 C CA . ASN B 2 571 ? -11.210 23.281 48.862 1.00 129.92 ? 571 ASN B CA 1 ATOM 11537 C C . ASN B 2 571 ? -11.295 22.029 47.995 1.00 126.06 ? 571 ASN B C 1 ATOM 11538 O O . ASN B 2 571 ? -10.868 20.950 48.403 1.00 136.07 ? 571 ASN B O 1 ATOM 11539 C CB . ASN B 2 571 ? -12.052 23.102 50.126 1.00 133.54 ? 571 ASN B CB 1 ATOM 11540 C CG . ASN B 2 571 ? -13.508 22.822 49.822 1.00 141.28 ? 571 ASN B CG 1 ATOM 11541 O OD1 . ASN B 2 571 ? -13.923 21.668 49.733 1.00 150.36 ? 571 ASN B OD1 1 ATOM 11542 N ND2 . ASN B 2 571 ? -14.294 23.880 49.663 1.00 128.57 ? 571 ASN B ND2 1 ATOM 11543 N N . GLY B 2 572 ? -11.846 22.181 46.796 1.00 121.20 ? 572 GLY B N 1 ATOM 11544 C CA . GLY B 2 572 ? -11.936 21.081 45.854 1.00 133.61 ? 572 GLY B CA 1 ATOM 11545 C C . GLY B 2 572 ? -13.316 20.460 45.754 1.00 142.63 ? 572 GLY B C 1 ATOM 11546 O O . GLY B 2 572 ? -13.635 19.805 44.761 1.00 138.00 ? 572 GLY B O 1 ATOM 11547 N N . LEU B 2 573 ? -14.137 20.660 46.780 1.00 142.25 ? 573 LEU B N 1 ATOM 11548 C CA . LEU B 2 573 ? -15.508 20.162 46.761 1.00 139.17 ? 573 LEU B CA 1 ATOM 11549 C C . LEU B 2 573 ? -16.433 21.157 46.074 1.00 123.85 ? 573 LEU B C 1 ATOM 11550 O O . LEU B 2 573 ? -16.427 22.345 46.395 1.00 103.59 ? 573 LEU B O 1 ATOM 11551 C CB . LEU B 2 573 ? -16.007 19.879 48.181 1.00 126.40 ? 573 LEU B CB 1 ATOM 11552 C CG . LEU B 2 573 ? -15.548 18.576 48.834 1.00 116.21 ? 573 LEU B CG 1 ATOM 11553 C CD1 . LEU B 2 573 ? -15.983 18.527 50.290 1.00 110.11 ? 573 LEU B CD1 1 ATOM 11554 C CD2 . LEU B 2 573 ? -16.097 17.383 48.068 1.00 116.30 ? 573 LEU B CD2 1 ATOM 11555 N N . LEU B 2 574 ? -17.224 20.670 45.124 1.00 127.28 ? 574 LEU B N 1 ATOM 11556 C CA . LEU B 2 574 ? -18.180 21.525 44.436 1.00 130.34 ? 574 LEU B CA 1 ATOM 11557 C C . LEU B 2 574 ? -19.305 21.909 45.394 1.00 122.11 ? 574 LEU B C 1 ATOM 11558 O O . LEU B 2 574 ? -19.920 21.049 46.029 1.00 133.89 ? 574 LEU B O 1 ATOM 11559 C CB . LEU B 2 574 ? -18.735 20.843 43.176 1.00 130.04 ? 574 LEU B CB 1 ATOM 11560 C CG . LEU B 2 574 ? -19.685 19.643 43.251 1.00 128.11 ? 574 LEU B CG 1 ATOM 11561 C CD1 . LEU B 2 574 ? -20.320 19.406 41.891 1.00 128.49 ? 574 LEU B CD1 1 ATOM 11562 C CD2 . LEU B 2 574 ? -18.978 18.384 43.733 1.00 121.74 ? 574 LEU B CD2 1 ATOM 11563 N N . CYS B 2 575 ? -19.535 23.214 45.511 1.00 101.22 ? 575 CYS B N 1 ATOM 11564 C CA . CYS B 2 575 ? -20.542 23.784 46.405 1.00 93.09 ? 575 CYS B CA 1 ATOM 11565 C C . CYS B 2 575 ? -20.297 23.427 47.873 1.00 97.74 ? 575 CYS B C 1 ATOM 11566 O O . CYS B 2 575 ? -21.227 23.433 48.681 1.00 99.34 ? 575 CYS B O 1 ATOM 11567 C CB . CYS B 2 575 ? -21.945 23.338 45.986 1.00 93.06 ? 575 CYS B CB 1 ATOM 11568 S SG . CYS B 2 575 ? -22.441 23.867 44.329 1.00 132.65 ? 575 CYS B SG 1 ATOM 11569 N N . SER B 2 576 ? -19.045 23.109 48.199 1.00 111.49 ? 576 SER B N 1 ATOM 11570 C CA . SER B 2 576 ? -18.607 22.858 49.575 1.00 120.96 ? 576 SER B CA 1 ATOM 11571 C C . SER B 2 576 ? -19.384 21.741 50.271 1.00 128.46 ? 576 SER B C 1 ATOM 11572 O O . SER B 2 576 ? -19.440 21.690 51.500 1.00 125.81 ? 576 SER B O 1 ATOM 11573 C CB . SER B 2 576 ? -18.717 24.139 50.405 1.00 89.07 ? 576 SER B CB 1 ATOM 11574 O OG . SER B 2 576 ? -18.122 25.236 49.736 1.00 88.47 ? 576 SER B OG 1 ATOM 11575 N N . GLY B 2 577 ? -19.988 20.851 49.489 1.00 119.19 ? 577 GLY B N 1 ATOM 11576 C CA . GLY B 2 577 ? -20.838 19.807 50.035 1.00 113.24 ? 577 GLY B CA 1 ATOM 11577 C C . GLY B 2 577 ? -22.091 20.365 50.688 1.00 115.30 ? 577 GLY B C 1 ATOM 11578 O O . GLY B 2 577 ? -22.896 19.622 51.253 1.00 116.50 ? 577 GLY B O 1 ATOM 11579 N N . ARG B 2 578 ? -22.250 21.683 50.611 1.00 99.57 ? 578 ARG B N 1 ATOM 11580 C CA . ARG B 2 578 ? -23.361 22.377 51.249 1.00 93.91 ? 578 ARG B CA 1 ATOM 11581 C C . ARG B 2 578 ? -24.517 22.659 50.295 1.00 96.42 ? 578 ARG B C 1 ATOM 11582 O O . ARG B 2 578 ? -25.479 23.324 50.676 1.00 110.22 ? 578 ARG B O 1 ATOM 11583 C CB . ARG B 2 578 ? -22.876 23.687 51.873 1.00 102.62 ? 578 ARG B CB 1 ATOM 11584 C CG . ARG B 2 578 ? -22.006 23.498 53.103 1.00 109.23 ? 578 ARG B CG 1 ATOM 11585 C CD . ARG B 2 578 ? -21.502 24.827 53.646 1.00 88.87 ? 578 ARG B CD 1 ATOM 11586 N NE . ARG B 2 578 ? -20.858 24.669 54.947 1.00 89.90 ? 578 ARG B NE 1 ATOM 11587 C CZ . ARG B 2 578 ? -20.017 25.550 55.478 1.00 91.72 ? 578 ARG B CZ 1 ATOM 11588 N NH1 . ARG B 2 578 ? -19.706 26.655 54.814 1.00 91.73 ? 578 ARG B NH1 1 ATOM 11589 N NH2 . ARG B 2 578 ? -19.481 25.323 56.669 1.00 103.24 ? 578 ARG B NH2 1 ATOM 11590 N N . GLY B 2 579 ? -24.418 22.184 49.056 1.00 100.84 ? 579 GLY B N 1 ATOM 11591 C CA . GLY B 2 579 ? -25.485 22.405 48.093 1.00 114.97 ? 579 GLY B CA 1 ATOM 11592 C C . GLY B 2 579 ? -25.329 21.742 46.734 1.00 104.84 ? 579 GLY B C 1 ATOM 11593 O O . GLY B 2 579 ? -24.251 21.269 46.377 1.00 91.22 ? 579 GLY B O 1 ATOM 11594 N N . LYS B 2 580 ? -26.427 21.704 45.982 1.00 108.44 ? 580 LYS B N 1 ATOM 11595 C CA . LYS B 2 580 ? -26.440 21.178 44.619 1.00 97.78 ? 580 LYS B CA 1 ATOM 11596 C C . LYS B 2 580 ? -25.890 22.191 43.619 1.00 98.35 ? 580 LYS B C 1 ATOM 11597 O O . LYS B 2 580 ? -25.898 23.392 43.877 1.00 99.23 ? 580 LYS B O 1 ATOM 11598 C CB . LYS B 2 580 ? -27.860 20.773 44.212 1.00 98.06 ? 580 LYS B CB 1 ATOM 11599 C CG . LYS B 2 580 ? -28.378 19.511 44.883 1.00 110.75 ? 580 LYS B CG 1 ATOM 11600 C CD . LYS B 2 580 ? -27.579 18.289 44.456 1.00 125.43 ? 580 LYS B CD 1 ATOM 11601 C CE . LYS B 2 580 ? -28.209 17.006 44.976 1.00 119.90 ? 580 LYS B CE 1 ATOM 11602 N NZ . LYS B 2 580 ? -29.581 16.801 44.430 1.00 119.94 ? 580 LYS B NZ 1 ATOM 11603 N N . CYS B 2 581 ? -25.409 21.702 42.480 1.00 102.36 ? 581 CYS B N 1 ATOM 11604 C CA . CYS B 2 581 ? -24.934 22.580 41.415 1.00 91.52 ? 581 CYS B CA 1 ATOM 11605 C C . CYS B 2 581 ? -25.869 22.562 40.212 1.00 92.40 ? 581 CYS B C 1 ATOM 11606 O O . CYS B 2 581 ? -26.017 21.540 39.548 1.00 103.27 ? 581 CYS B O 1 ATOM 11607 C CB . CYS B 2 581 ? -23.527 22.185 40.972 1.00 92.46 ? 581 CYS B CB 1 ATOM 11608 S SG . CYS B 2 581 ? -22.911 23.166 39.583 1.00 103.25 ? 581 CYS B SG 1 ATOM 11609 N N . GLU B 2 582 ? -26.492 23.701 39.932 1.00 93.16 ? 582 GLU B N 1 ATOM 11610 C CA . GLU B 2 582 ? -27.429 23.808 38.819 1.00 96.15 ? 582 GLU B CA 1 ATOM 11611 C C . GLU B 2 582 ? -27.088 24.975 37.897 1.00 96.93 ? 582 GLU B C 1 ATOM 11612 O O . GLU B 2 582 ? -27.077 26.131 38.321 1.00 101.73 ? 582 GLU B O 1 ATOM 11613 C CB . GLU B 2 582 ? -28.861 23.962 39.337 1.00 100.47 ? 582 GLU B CB 1 ATOM 11614 C CG . GLU B 2 582 ? -29.340 22.815 40.207 1.00 104.10 ? 582 GLU B CG 1 ATOM 11615 C CD . GLU B 2 582 ? -30.758 23.017 40.699 1.00 122.02 ? 582 GLU B CD 1 ATOM 11616 O OE1 . GLU B 2 582 ? -31.385 24.027 40.311 1.00 113.67 ? 582 GLU B OE1 1 ATOM 11617 O OE2 . GLU B 2 582 ? -31.247 22.167 41.473 1.00 145.51 ? 582 GLU B OE2 1 ATOM 11618 N N . CYS B 2 583 ? -26.808 24.653 36.638 1.00 103.19 ? 583 CYS B N 1 ATOM 11619 C CA . CYS B 2 583 ? -26.543 25.647 35.601 1.00 102.83 ? 583 CYS B CA 1 ATOM 11620 C C . CYS B 2 583 ? -25.368 26.561 35.937 1.00 103.11 ? 583 CYS B C 1 ATOM 11621 O O . CYS B 2 583 ? -25.414 27.765 35.684 1.00 110.39 ? 583 CYS B O 1 ATOM 11622 C CB . CYS B 2 583 ? -27.799 26.481 35.341 1.00 105.82 ? 583 CYS B CB 1 ATOM 11623 S SG . CYS B 2 583 ? -29.232 25.495 34.853 1.00 108.02 ? 583 CYS B SG 1 ATOM 11624 N N . GLY B 2 584 ? -24.314 25.982 36.501 1.00 103.87 ? 584 GLY B N 1 ATOM 11625 C CA . GLY B 2 584 ? -23.114 26.734 36.818 1.00 105.90 ? 584 GLY B CA 1 ATOM 11626 C C . GLY B 2 584 ? -23.218 27.499 38.122 1.00 104.79 ? 584 GLY B C 1 ATOM 11627 O O . GLY B 2 584 ? -22.249 28.108 38.575 1.00 107.86 ? 584 GLY B O 1 ATOM 11628 N N . SER B 2 585 ? -24.399 27.464 38.729 1.00 99.36 ? 585 SER B N 1 ATOM 11629 C CA . SER B 2 585 ? -24.627 28.138 39.999 1.00 95.06 ? 585 SER B CA 1 ATOM 11630 C C . SER B 2 585 ? -25.005 27.129 41.070 1.00 89.53 ? 585 SER B C 1 ATOM 11631 O O . SER B 2 585 ? -25.777 26.208 40.821 1.00 89.92 ? 585 SER B O 1 ATOM 11632 C CB . SER B 2 585 ? -25.722 29.199 39.862 1.00 106.30 ? 585 SER B CB 1 ATOM 11633 O OG . SER B 2 585 ? -25.344 30.215 38.948 1.00 123.84 ? 585 SER B OG 1 ATOM 11634 N N . CYS B 2 586 ? -24.452 27.301 42.264 1.00 95.98 ? 586 CYS B N 1 ATOM 11635 C CA . CYS B 2 586 ? -24.800 26.440 43.383 1.00 87.34 ? 586 CYS B CA 1 ATOM 11636 C C . CYS B 2 586 ? -26.135 26.850 43.982 1.00 86.54 ? 586 CYS B C 1 ATOM 11637 O O . CYS B 2 586 ? -26.484 28.029 43.994 1.00 91.91 ? 586 CYS B O 1 ATOM 11638 C CB . CYS B 2 586 ? -23.718 26.481 44.463 1.00 86.61 ? 586 CYS B CB 1 ATOM 11639 S SG . CYS B 2 586 ? -22.112 25.840 43.960 1.00 113.38 ? 586 CYS B SG 1 ATOM 11640 N N . VAL B 2 587 ? -26.882 25.868 44.466 1.00 87.20 ? 587 VAL B N 1 ATOM 11641 C CA . VAL B 2 587 ? -28.069 26.137 45.262 1.00 90.92 ? 587 VAL B CA 1 ATOM 11642 C C . VAL B 2 587 ? -27.885 25.482 46.630 1.00 93.00 ? 587 VAL B C 1 ATOM 11643 O O . VAL B 2 587 ? -27.792 24.260 46.744 1.00 89.66 ? 587 VAL B O 1 ATOM 11644 C CB . VAL B 2 587 ? -29.353 25.636 44.570 1.00 94.80 ? 587 VAL B CB 1 ATOM 11645 C CG1 . VAL B 2 587 ? -29.130 24.269 43.930 1.00 118.84 ? 587 VAL B CG1 1 ATOM 11646 C CG2 . VAL B 2 587 ? -30.516 25.613 45.552 1.00 113.73 ? 587 VAL B CG2 1 ATOM 11647 N N . CYS B 2 588 ? -27.815 26.309 47.666 1.00 93.45 ? 588 CYS B N 1 ATOM 11648 C CA . CYS B 2 588 ? -27.438 25.841 48.994 1.00 99.74 ? 588 CYS B CA 1 ATOM 11649 C C . CYS B 2 588 ? -28.549 25.058 49.692 1.00 95.33 ? 588 CYS B C 1 ATOM 11650 O O . CYS B 2 588 ? -29.683 25.528 49.793 1.00 96.02 ? 588 CYS B O 1 ATOM 11651 C CB . CYS B 2 588 ? -27.014 27.031 49.855 1.00 102.18 ? 588 CYS B CB 1 ATOM 11652 S SG . CYS B 2 588 ? -25.680 28.014 49.126 1.00 106.16 ? 588 CYS B SG 1 ATOM 11653 N N . ILE B 2 589 ? -28.214 23.862 50.172 1.00 92.09 ? 589 ILE B N 1 ATOM 11654 C CA . ILE B 2 589 ? -29.159 23.051 50.933 1.00 98.17 ? 589 ILE B CA 1 ATOM 11655 C C . ILE B 2 589 ? -29.042 23.347 52.433 1.00 109.96 ? 589 ILE B C 1 ATOM 11656 O O . ILE B 2 589 ? -30.021 23.761 53.055 1.00 116.14 ? 589 ILE B O 1 ATOM 11657 C CB . ILE B 2 589 ? -28.989 21.526 50.661 1.00 119.44 ? 589 ILE B CB 1 ATOM 11658 C CG1 . ILE B 2 589 ? -27.536 21.069 50.804 1.00 126.44 ? 589 ILE B CG1 1 ATOM 11659 C CG2 . ILE B 2 589 ? -29.487 21.185 49.267 1.00 105.45 ? 589 ILE B CG2 1 ATOM 11660 C CD1 . ILE B 2 589 ? -27.369 19.788 51.602 1.00 117.02 ? 589 ILE B CD1 1 ATOM 11661 N N . GLN B 2 590 ? -27.859 23.118 53.005 1.00 106.48 ? 590 GLN B N 1 ATOM 11662 C CA . GLN B 2 590 ? -27.622 23.302 54.437 1.00 114.52 ? 590 GLN B CA 1 ATOM 11663 C C . GLN B 2 590 ? -28.093 24.673 54.907 1.00 102.27 ? 590 GLN B C 1 ATOM 11664 O O . GLN B 2 590 ? -27.745 25.690 54.310 1.00 98.41 ? 590 GLN B O 1 ATOM 11665 C CB . GLN B 2 590 ? -26.136 23.119 54.760 1.00 115.18 ? 590 GLN B CB 1 ATOM 11666 C CG . GLN B 2 590 ? -25.839 22.936 56.243 1.00 120.45 ? 590 GLN B CG 1 ATOM 11667 C CD . GLN B 2 590 ? -24.358 22.817 56.533 1.00 128.93 ? 590 GLN B CD 1 ATOM 11668 O OE1 . GLN B 2 590 ? -23.532 23.431 55.861 1.00 129.53 ? 590 GLN B OE1 1 ATOM 11669 N NE2 . GLN B 2 590 ? -24.013 22.020 57.538 1.00 127.69 ? 590 GLN B NE2 1 ATOM 11670 N N . PRO B 2 591 ? -28.897 24.699 55.981 1.00 107.48 ? 591 PRO B N 1 ATOM 11671 C CA . PRO B 2 591 ? -29.528 25.928 56.473 1.00 109.63 ? 591 PRO B CA 1 ATOM 11672 C C . PRO B 2 591 ? -28.524 27.009 56.843 1.00 107.09 ? 591 PRO B C 1 ATOM 11673 O O . PRO B 2 591 ? -27.478 26.717 57.420 1.00 112.21 ? 591 PRO B O 1 ATOM 11674 C CB . PRO B 2 591 ? -30.295 25.456 57.715 1.00 129.62 ? 591 PRO B CB 1 ATOM 11675 C CG . PRO B 2 591 ? -29.635 24.178 58.112 1.00 143.51 ? 591 PRO B CG 1 ATOM 11676 C CD . PRO B 2 591 ? -29.235 23.540 56.822 1.00 124.58 ? 591 PRO B CD 1 ATOM 11677 N N . GLY B 2 592 ? -28.849 28.250 56.499 1.00 108.59 ? 592 GLY B N 1 ATOM 11678 C CA . GLY B 2 592 ? -28.024 29.384 56.861 1.00 112.24 ? 592 GLY B CA 1 ATOM 11679 C C . GLY B 2 592 ? -26.711 29.449 56.111 1.00 104.64 ? 592 GLY B C 1 ATOM 11680 O O . GLY B 2 592 ? -25.754 30.063 56.581 1.00 126.06 ? 592 GLY B O 1 ATOM 11681 N N . SER B 2 593 ? -26.659 28.816 54.945 1.00 90.11 ? 593 SER B N 1 ATOM 11682 C CA . SER B 2 593 ? -25.468 28.883 54.108 1.00 87.12 ? 593 SER B CA 1 ATOM 11683 C C . SER B 2 593 ? -25.766 29.608 52.803 1.00 91.68 ? 593 SER B C 1 ATOM 11684 O O . SER B 2 593 ? -26.873 29.523 52.269 1.00 92.23 ? 593 SER B O 1 ATOM 11685 C CB . SER B 2 593 ? -24.924 27.483 53.820 1.00 88.17 ? 593 SER B CB 1 ATOM 11686 O OG . SER B 2 593 ? -25.797 26.759 52.973 1.00 89.68 ? 593 SER B OG 1 ATOM 11687 N N . TYR B 2 594 ? -24.765 30.321 52.297 1.00 82.84 ? 594 TYR B N 1 ATOM 11688 C CA . TYR B 2 594 ? -24.899 31.080 51.061 1.00 81.75 ? 594 TYR B CA 1 ATOM 11689 C C . TYR B 2 594 ? -23.533 31.369 50.451 1.00 83.97 ? 594 TYR B C 1 ATOM 11690 O O . TYR B 2 594 ? -22.507 30.922 50.961 1.00 96.96 ? 594 TYR B O 1 ATOM 11691 C CB . TYR B 2 594 ? -25.649 32.386 51.311 1.00 84.12 ? 594 TYR B CB 1 ATOM 11692 C CG . TYR B 2 594 ? -25.127 33.157 52.497 1.00 79.80 ? 594 TYR B CG 1 ATOM 11693 C CD1 . TYR B 2 594 ? -24.041 34.015 52.372 1.00 81.25 ? 594 TYR B CD1 1 ATOM 11694 C CD2 . TYR B 2 594 ? -25.715 33.023 53.746 1.00 81.57 ? 594 TYR B CD2 1 ATOM 11695 C CE1 . TYR B 2 594 ? -23.557 34.719 53.458 1.00 76.48 ? 594 TYR B CE1 1 ATOM 11696 C CE2 . TYR B 2 594 ? -25.241 33.721 54.834 1.00 83.72 ? 594 TYR B CE2 1 ATOM 11697 C CZ . TYR B 2 594 ? -24.163 34.568 54.687 1.00 78.18 ? 594 TYR B CZ 1 ATOM 11698 O OH . TYR B 2 594 ? -23.694 35.265 55.775 1.00 77.41 ? 594 TYR B OH 1 ATOM 11699 N N . GLY B 2 595 ? -23.527 32.139 49.369 1.00 79.01 ? 595 GLY B N 1 ATOM 11700 C CA . GLY B 2 595 ? -22.312 32.388 48.620 1.00 78.58 ? 595 GLY B CA 1 ATOM 11701 C C . GLY B 2 595 ? -22.346 31.616 47.318 1.00 91.46 ? 595 GLY B C 1 ATOM 11702 O O . GLY B 2 595 ? -23.183 30.731 47.139 1.00 98.22 ? 595 GLY B O 1 ATOM 11703 N N . ASP B 2 596 ? -21.440 31.952 46.406 1.00 96.27 ? 596 ASP B N 1 ATOM 11704 C CA . ASP B 2 596 ? -21.393 31.307 45.099 1.00 96.06 ? 596 ASP B CA 1 ATOM 11705 C C . ASP B 2 596 ? -21.135 29.814 45.243 1.00 104.13 ? 596 ASP B C 1 ATOM 11706 O O . ASP B 2 596 ? -21.813 28.992 44.631 1.00 122.95 ? 596 ASP B O 1 ATOM 11707 C CB . ASP B 2 596 ? -20.313 31.943 44.222 1.00 103.20 ? 596 ASP B CB 1 ATOM 11708 C CG . ASP B 2 596 ? -20.465 33.448 44.106 1.00 118.35 ? 596 ASP B CG 1 ATOM 11709 O OD1 . ASP B 2 596 ? -21.604 33.947 44.233 1.00 111.92 ? 596 ASP B OD1 1 ATOM 11710 O OD2 . ASP B 2 596 ? -19.442 34.130 43.885 1.00 126.21 ? 596 ASP B OD2 1 ATOM 11711 N N . THR B 2 597 ? -20.135 29.479 46.048 1.00 111.00 ? 597 THR B N 1 ATOM 11712 C CA . THR B 2 597 ? -19.773 28.094 46.317 1.00 101.89 ? 597 THR B CA 1 ATOM 11713 C C . THR B 2 597 ? -20.397 27.576 47.613 1.00 112.22 ? 597 THR B C 1 ATOM 11714 O O . THR B 2 597 ? -20.063 26.482 48.066 1.00 121.97 ? 597 THR B O 1 ATOM 11715 C CB . THR B 2 597 ? -18.248 27.925 46.390 1.00 107.97 ? 597 THR B CB 1 ATOM 11716 O OG1 . THR B 2 597 ? -17.727 28.728 47.456 1.00 127.28 ? 597 THR B OG1 1 ATOM 11717 C CG2 . THR B 2 597 ? -17.610 28.357 45.080 1.00 105.02 ? 597 THR B CG2 1 ATOM 11718 N N . CYS B 2 598 ? -21.267 28.385 48.216 1.00 100.92 ? 598 CYS B N 1 ATOM 11719 C CA . CYS B 2 598 ? -21.859 28.095 49.525 1.00 89.07 ? 598 CYS B CA 1 ATOM 11720 C C . CYS B 2 598 ? -20.773 28.060 50.594 1.00 90.32 ? 598 CYS B C 1 ATOM 11721 O O . CYS B 2 598 ? -20.874 27.329 51.580 1.00 92.19 ? 598 CYS B O 1 ATOM 11722 C CB . CYS B 2 598 ? -22.637 26.771 49.515 1.00 87.47 ? 598 CYS B CB 1 ATOM 11723 S SG . CYS B 2 598 ? -24.168 26.777 48.555 1.00 97.48 ? 598 CYS B SG 1 ATOM 11724 N N . GLU B 2 599 ? -19.737 28.867 50.393 1.00 91.09 ? 599 GLU B N 1 ATOM 11725 C CA . GLU B 2 599 ? -18.577 28.868 51.276 1.00 106.39 ? 599 GLU B CA 1 ATOM 11726 C C . GLU B 2 599 ? -18.852 29.592 52.588 1.00 101.24 ? 599 GLU B C 1 ATOM 11727 O O . GLU B 2 599 ? -18.167 29.361 53.585 1.00 113.78 ? 599 GLU B O 1 ATOM 11728 C CB . GLU B 2 599 ? -17.375 29.510 50.574 1.00 111.38 ? 599 GLU B CB 1 ATOM 11729 C CG . GLU B 2 599 ? -17.473 31.021 50.379 1.00 104.77 ? 599 GLU B CG 1 ATOM 11730 C CD . GLU B 2 599 ? -18.452 31.424 49.291 1.00 114.22 ? 599 GLU B CD 1 ATOM 11731 O OE1 . GLU B 2 599 ? -18.698 32.639 49.131 1.00 126.45 ? 599 GLU B OE1 1 ATOM 11732 O OE2 . GLU B 2 599 ? -18.976 30.531 48.594 1.00 115.49 ? 599 GLU B OE2 1 ATOM 11733 N N . LYS B 2 600 ? -19.854 30.464 52.587 1.00 89.23 ? 600 LYS B N 1 ATOM 11734 C CA . LYS B 2 600 ? -20.138 31.290 53.754 1.00 86.28 ? 600 LYS B CA 1 ATOM 11735 C C . LYS B 2 600 ? -21.309 30.743 54.567 1.00 86.94 ? 600 LYS B C 1 ATOM 11736 O O . LYS B 2 600 ? -22.447 30.718 54.100 1.00 98.82 ? 600 LYS B O 1 ATOM 11737 C CB . LYS B 2 600 ? -20.412 32.735 53.324 1.00 81.23 ? 600 LYS B CB 1 ATOM 11738 C CG . LYS B 2 600 ? -19.241 33.392 52.599 1.00 80.80 ? 600 LYS B CG 1 ATOM 11739 C CD . LYS B 2 600 ? -19.446 34.889 52.412 1.00 107.70 ? 600 LYS B CD 1 ATOM 11740 C CE . LYS B 2 600 ? -20.617 35.188 51.487 1.00 131.63 ? 600 LYS B CE 1 ATOM 11741 N NZ . LYS B 2 600 ? -20.850 36.654 51.326 1.00 108.85 ? 600 LYS B NZ 1 ATOM 11742 N N . CYS B 2 601 ? -21.012 30.281 55.778 1.00 88.32 ? 601 CYS B N 1 ATOM 11743 C CA . CYS B 2 601 ? -22.037 29.784 56.689 1.00 86.72 ? 601 CYS B CA 1 ATOM 11744 C C . CYS B 2 601 ? -21.703 30.132 58.141 1.00 86.11 ? 601 CYS B C 1 ATOM 11745 O O . CYS B 2 601 ? -21.250 29.277 58.898 1.00 107.96 ? 601 CYS B O 1 ATOM 11746 C CB . CYS B 2 601 ? -22.201 28.272 56.529 1.00 87.45 ? 601 CYS B CB 1 ATOM 11747 S SG . CYS B 2 601 ? -23.618 27.576 57.404 1.00 109.18 ? 601 CYS B SG 1 ATOM 11748 N N . PRO B 2 602 ? -21.932 31.391 58.534 1.00 84.85 ? 602 PRO B N 1 ATOM 11749 C CA . PRO B 2 602 ? -21.573 31.880 59.870 1.00 90.00 ? 602 PRO B CA 1 ATOM 11750 C C . PRO B 2 602 ? -22.398 31.247 60.987 1.00 92.51 ? 602 PRO B C 1 ATOM 11751 O O . PRO B 2 602 ? -21.953 31.194 62.132 1.00 91.28 ? 602 PRO B O 1 ATOM 11752 C CB . PRO B 2 602 ? -21.858 33.380 59.777 1.00 83.11 ? 602 PRO B CB 1 ATOM 11753 C CG . PRO B 2 602 ? -22.925 33.487 58.752 1.00 93.50 ? 602 PRO B CG 1 ATOM 11754 C CD . PRO B 2 602 ? -22.619 32.422 57.738 1.00 102.66 ? 602 PRO B CD 1 ATOM 11755 N N . THR B 2 603 ? -23.594 30.781 60.653 1.00 95.26 ? 603 THR B N 1 ATOM 11756 C CA . THR B 2 603 ? -24.485 30.191 61.640 1.00 101.96 ? 603 THR B CA 1 ATOM 11757 C C . THR B 2 603 ? -24.342 28.669 61.692 1.00 119.02 ? 603 THR B C 1 ATOM 11758 O O . THR B 2 603 ? -25.069 27.992 62.419 1.00 137.00 ? 603 THR B O 1 ATOM 11759 C CB . THR B 2 603 ? -25.948 30.567 61.354 1.00 112.67 ? 603 THR B CB 1 ATOM 11760 O OG1 . THR B 2 603 ? -26.821 29.707 62.097 1.00 133.77 ? 603 THR B OG1 1 ATOM 11761 C CG2 . THR B 2 603 ? -26.249 30.434 59.870 1.00 125.49 ? 603 THR B CG2 1 ATOM 11762 N N . CYS B 2 604 ? -23.405 28.136 60.913 1.00 113.36 ? 604 CYS B N 1 ATOM 11763 C CA . CYS B 2 604 ? -23.115 26.705 60.927 1.00 103.85 ? 604 CYS B CA 1 ATOM 11764 C C . CYS B 2 604 ? -22.309 26.330 62.169 1.00 102.01 ? 604 CYS B C 1 ATOM 11765 O O . CYS B 2 604 ? -21.619 27.175 62.740 1.00 98.74 ? 604 CYS B O 1 ATOM 11766 C CB . CYS B 2 604 ? -22.362 26.295 59.657 1.00 101.51 ? 604 CYS B CB 1 ATOM 11767 S SG . CYS B 2 604 ? -23.432 25.762 58.300 1.00 187.13 ? 604 CYS B SG 1 ATOM 11768 N N . PRO B 2 605 ? -22.403 25.059 62.598 1.00 123.93 ? 605 PRO B N 1 ATOM 11769 C CA . PRO B 2 605 ? -21.688 24.593 63.793 1.00 119.67 ? 605 PRO B CA 1 ATOM 11770 C C . PRO B 2 605 ? -20.171 24.671 63.649 1.00 110.96 ? 605 PRO B C 1 ATOM 11771 O O . PRO B 2 605 ? -19.649 24.615 62.534 1.00 102.75 ? 605 PRO B O 1 ATOM 11772 C CB . PRO B 2 605 ? -22.141 23.136 63.926 1.00 111.96 ? 605 PRO B CB 1 ATOM 11773 C CG . PRO B 2 605 ? -23.428 23.065 63.184 1.00 110.60 ? 605 PRO B CG 1 ATOM 11774 C CD . PRO B 2 605 ? -23.277 24.011 62.042 1.00 111.41 ? 605 PRO B CD 1 ATOM 11775 N N . ASP B 2 606 ? -19.478 24.786 64.779 1.00 108.10 ? 606 ASP B N 1 ATOM 11776 C CA . ASP B 2 606 ? -18.025 24.919 64.788 1.00 107.79 ? 606 ASP B CA 1 ATOM 11777 C C . ASP B 2 606 ? -17.333 23.644 64.316 1.00 128.31 ? 606 ASP B C 1 ATOM 11778 O O . ASP B 2 606 ? -17.938 22.571 64.290 1.00 136.04 ? 606 ASP B O 1 ATOM 11779 C CB . ASP B 2 606 ? -17.528 25.301 66.187 1.00 111.44 ? 606 ASP B CB 1 ATOM 11780 C CG . ASP B 2 606 ? -18.079 24.396 67.279 1.00 124.32 ? 606 ASP B CG 1 ATOM 11781 O OD1 . ASP B 2 606 ? -18.357 23.210 67.008 1.00 131.14 ? 606 ASP B OD1 1 ATOM 11782 O OD2 . ASP B 2 606 ? -18.227 24.876 68.422 1.00 129.21 ? 606 ASP B OD2 1 ATOM 11783 N N . ALA B 2 607 ? -16.067 23.777 63.930 1.00 114.41 ? 607 ALA B N 1 ATOM 11784 C CA . ALA B 2 607 ? -15.266 22.647 63.475 1.00 106.68 ? 607 ALA B CA 1 ATOM 11785 C C . ALA B 2 607 ? -15.225 21.525 64.511 1.00 137.97 ? 607 ALA B C 1 ATOM 11786 O O . ALA B 2 607 ? -15.109 20.349 64.160 1.00 118.42 ? 607 ALA B O 1 ATOM 11787 C CB . ALA B 2 607 ? -13.857 23.108 63.141 1.00 107.47 ? 607 ALA B CB 1 ATOM 11788 N N . CYS B 2 608 ? -15.327 21.896 65.784 1.00 132.94 ? 608 CYS B N 1 ATOM 11789 C CA . CYS B 2 608 ? -15.340 20.929 66.876 1.00 121.79 ? 608 CYS B CA 1 ATOM 11790 C C . CYS B 2 608 ? -16.486 19.936 66.721 1.00 106.71 ? 608 CYS B C 1 ATOM 11791 O O . CYS B 2 608 ? -16.363 18.771 67.090 1.00 97.42 ? 608 CYS B O 1 ATOM 11792 C CB . CYS B 2 608 ? -15.448 21.644 68.225 1.00 126.75 ? 608 CYS B CB 1 ATOM 11793 S SG . CYS B 2 608 ? -14.057 22.732 68.608 1.00 161.09 ? 608 CYS B SG 1 ATOM 11794 N N . THR B 2 609 ? -17.600 20.410 66.174 1.00 113.08 ? 609 THR B N 1 ATOM 11795 C CA . THR B 2 609 ? -18.759 19.563 65.919 1.00 118.57 ? 609 THR B CA 1 ATOM 11796 C C . THR B 2 609 ? -18.547 18.737 64.654 1.00 119.70 ? 609 THR B C 1 ATOM 11797 O O . THR B 2 609 ? -18.952 17.577 64.576 1.00 97.65 ? 609 THR B O 1 ATOM 11798 C CB . THR B 2 609 ? -20.042 20.401 65.783 1.00 103.42 ? 609 THR B CB 1 ATOM 11799 O OG1 . THR B 2 609 ? -20.243 21.163 66.979 1.00 104.72 ? 609 THR B OG1 1 ATOM 11800 C CG2 . THR B 2 609 ? -21.250 19.508 65.550 1.00 114.93 ? 609 THR B CG2 1 ATOM 11801 N N . PHE B 2 610 ? -17.893 19.345 63.672 1.00 123.23 ? 610 PHE B N 1 ATOM 11802 C CA . PHE B 2 610 ? -17.634 18.693 62.395 1.00 121.29 ? 610 PHE B CA 1 ATOM 11803 C C . PHE B 2 610 ? -16.533 17.648 62.523 1.00 119.05 ? 610 PHE B C 1 ATOM 11804 O O . PHE B 2 610 ? -16.763 16.458 62.315 1.00 110.64 ? 610 PHE B O 1 ATOM 11805 C CB . PHE B 2 610 ? -17.248 19.725 61.333 1.00 135.51 ? 610 PHE B CB 1 ATOM 11806 C CG . PHE B 2 610 ? -18.271 19.891 60.243 1.00 146.47 ? 610 PHE B CG 1 ATOM 11807 C CD1 . PHE B 2 610 ? -19.226 20.892 60.316 1.00 154.77 ? 610 PHE B CD1 1 ATOM 11808 C CD2 . PHE B 2 610 ? -18.271 19.050 59.142 1.00 147.63 ? 610 PHE B CD2 1 ATOM 11809 C CE1 . PHE B 2 610 ? -20.166 21.051 59.312 1.00 159.91 ? 610 PHE B CE1 1 ATOM 11810 C CE2 . PHE B 2 610 ? -19.208 19.202 58.135 1.00 160.71 ? 610 PHE B CE2 1 ATOM 11811 C CZ . PHE B 2 610 ? -20.157 20.204 58.220 1.00 166.19 ? 610 PHE B CZ 1 ATOM 11812 N N . LYS B 2 611 ? -15.333 18.105 62.866 1.00 121.00 ? 611 LYS B N 1 ATOM 11813 C CA . LYS B 2 611 ? -14.153 17.248 62.876 1.00 105.52 ? 611 LYS B CA 1 ATOM 11814 C C . LYS B 2 611 ? -14.210 16.123 63.911 1.00 99.24 ? 611 LYS B C 1 ATOM 11815 O O . LYS B 2 611 ? -13.395 15.202 63.865 1.00 121.07 ? 611 LYS B O 1 ATOM 11816 C CB . LYS B 2 611 ? -12.896 18.094 63.107 1.00 102.67 ? 611 LYS B CB 1 ATOM 11817 C CG . LYS B 2 611 ? -12.726 19.240 62.114 1.00 127.40 ? 611 LYS B CG 1 ATOM 11818 C CD . LYS B 2 611 ? -12.781 18.752 60.671 1.00 135.92 ? 611 LYS B CD 1 ATOM 11819 C CE . LYS B 2 611 ? -11.615 17.831 60.341 1.00 139.40 ? 611 LYS B CE 1 ATOM 11820 N NZ . LYS B 2 611 ? -11.731 17.261 58.969 1.00 141.05 ? 611 LYS B NZ 1 ATOM 11821 N N . LYS B 2 612 ? -15.163 16.185 64.837 1.00 104.54 ? 612 LYS B N 1 ATOM 11822 C CA . LYS B 2 612 ? -15.301 15.116 65.824 1.00 102.85 ? 612 LYS B CA 1 ATOM 11823 C C . LYS B 2 612 ? -15.911 13.884 65.167 1.00 105.51 ? 612 LYS B C 1 ATOM 11824 O O . LYS B 2 612 ? -15.752 12.765 65.654 1.00 91.42 ? 612 LYS B O 1 ATOM 11825 C CB . LYS B 2 612 ? -16.150 15.561 67.019 1.00 92.16 ? 612 LYS B CB 1 ATOM 11826 C CG . LYS B 2 612 ? -17.639 15.296 66.879 1.00 92.37 ? 612 LYS B CG 1 ATOM 11827 C CD . LYS B 2 612 ? -18.384 15.705 68.139 1.00 117.78 ? 612 LYS B CD 1 ATOM 11828 C CE . LYS B 2 612 ? -19.891 15.660 67.939 1.00 132.92 ? 612 LYS B CE 1 ATOM 11829 N NZ . LYS B 2 612 ? -20.626 16.212 69.114 1.00 118.70 ? 612 LYS B NZ 1 ATOM 11830 N N . GLU B 2 613 ? -16.600 14.098 64.052 1.00 116.58 ? 613 GLU B N 1 ATOM 11831 C CA . GLU B 2 613 ? -17.163 12.997 63.284 1.00 115.70 ? 613 GLU B CA 1 ATOM 11832 C C . GLU B 2 613 ? -16.037 12.157 62.693 1.00 103.70 ? 613 GLU B C 1 ATOM 11833 O O . GLU B 2 613 ? -16.173 10.946 62.520 1.00 106.60 ? 613 GLU B O 1 ATOM 11834 C CB . GLU B 2 613 ? -18.076 13.522 62.175 1.00 120.45 ? 613 GLU B CB 1 ATOM 11835 C CG . GLU B 2 613 ? -19.138 12.536 61.732 1.00 133.21 ? 613 GLU B CG 1 ATOM 11836 C CD . GLU B 2 613 ? -20.139 12.239 62.831 1.00 147.15 ? 613 GLU B CD 1 ATOM 11837 O OE1 . GLU B 2 613 ? -21.033 13.080 63.061 1.00 141.77 ? 613 GLU B OE1 1 ATOM 11838 O OE2 . GLU B 2 613 ? -20.027 11.170 63.468 1.00 155.98 ? 613 GLU B OE2 1 ATOM 11839 N N . CYS B 2 614 ? -14.922 12.814 62.392 1.00 105.48 ? 614 CYS B N 1 ATOM 11840 C CA . CYS B 2 614 ? -13.761 12.140 61.831 1.00 103.59 ? 614 CYS B CA 1 ATOM 11841 C C . CYS B 2 614 ? -13.023 11.324 62.884 1.00 102.72 ? 614 CYS B C 1 ATOM 11842 O O . CYS B 2 614 ? -12.626 10.190 62.625 1.00 116.45 ? 614 CYS B O 1 ATOM 11843 C CB . CYS B 2 614 ? -12.807 13.152 61.193 1.00 113.00 ? 614 CYS B CB 1 ATOM 11844 S SG . CYS B 2 614 ? -13.384 13.833 59.624 1.00 166.36 ? 614 CYS B SG 1 ATOM 11845 N N . VAL B 2 615 ? -12.845 11.896 64.071 1.00 94.33 ? 615 VAL B N 1 ATOM 11846 C CA . VAL B 2 615 ? -12.082 11.220 65.115 1.00 97.02 ? 615 VAL B CA 1 ATOM 11847 C C . VAL B 2 615 ? -12.825 9.988 65.628 1.00 102.46 ? 615 VAL B C 1 ATOM 11848 O O . VAL B 2 615 ? -12.206 9.044 66.113 1.00 115.30 ? 615 VAL B O 1 ATOM 11849 C CB . VAL B 2 615 ? -11.757 12.165 66.297 1.00 88.32 ? 615 VAL B CB 1 ATOM 11850 C CG1 . VAL B 2 615 ? -11.210 13.486 65.780 1.00 104.19 ? 615 VAL B CG1 1 ATOM 11851 C CG2 . VAL B 2 615 ? -12.977 12.402 67.161 1.00 88.14 ? 615 VAL B CG2 1 ATOM 11852 N N . GLU B 2 616 ? -14.151 9.999 65.521 1.00 99.98 ? 616 GLU B N 1 ATOM 11853 C CA . GLU B 2 616 ? -14.953 8.835 65.877 1.00 105.29 ? 616 GLU B CA 1 ATOM 11854 C C . GLU B 2 616 ? -14.574 7.617 65.042 1.00 113.73 ? 616 GLU B C 1 ATOM 11855 O O . GLU B 2 616 ? -14.063 6.627 65.565 1.00 115.58 ? 616 GLU B O 1 ATOM 11856 C CB . GLU B 2 616 ? -16.444 9.139 65.721 1.00 116.10 ? 616 GLU B CB 1 ATOM 11857 C CG . GLU B 2 616 ? -17.037 9.934 66.876 1.00 122.91 ? 616 GLU B CG 1 ATOM 11858 C CD . GLU B 2 616 ? -17.018 9.167 68.188 1.00 122.47 ? 616 GLU B CD 1 ATOM 11859 O OE1 . GLU B 2 616 ? -18.013 8.472 68.485 1.00 113.41 ? 616 GLU B OE1 1 ATOM 11860 O OE2 . GLU B 2 616 ? -16.010 9.262 68.924 1.00 113.16 ? 616 GLU B OE2 1 ATOM 11861 N N . CYS B 2 617 ? -14.823 7.699 63.740 1.00 110.03 ? 617 CYS B N 1 ATOM 11862 C CA . CYS B 2 617 ? -14.586 6.569 62.850 1.00 120.91 ? 617 CYS B CA 1 ATOM 11863 C C . CYS B 2 617 ? -13.102 6.231 62.710 1.00 100.17 ? 617 CYS B C 1 ATOM 11864 O O . CYS B 2 617 ? -12.730 5.062 62.684 1.00 101.29 ? 617 CYS B O 1 ATOM 11865 C CB . CYS B 2 617 ? -15.186 6.846 61.467 1.00 137.04 ? 617 CYS B CB 1 ATOM 11866 S SG . CYS B 2 617 ? -14.177 7.895 60.389 1.00 123.21 ? 617 CYS B SG 1 ATOM 11867 N N . LYS B 2 618 ? -12.256 7.251 62.608 1.00 94.21 ? 618 LYS B N 1 ATOM 11868 C CA . LYS B 2 618 ? -10.841 7.020 62.335 1.00 94.75 ? 618 LYS B CA 1 ATOM 11869 C C . LYS B 2 618 ? -10.108 6.436 63.537 1.00 93.80 ? 618 LYS B C 1 ATOM 11870 O O . LYS B 2 618 ? -9.231 5.584 63.384 1.00 103.07 ? 618 LYS B O 1 ATOM 11871 C CB . LYS B 2 618 ? -10.162 8.314 61.887 1.00 90.56 ? 618 LYS B CB 1 ATOM 11872 C CG . LYS B 2 618 ? -10.594 8.790 60.509 1.00 96.60 ? 618 LYS B CG 1 ATOM 11873 C CD . LYS B 2 618 ? -10.122 7.841 59.419 1.00 98.14 ? 618 LYS B CD 1 ATOM 11874 C CE . LYS B 2 618 ? -8.601 7.814 59.333 1.00 118.09 ? 618 LYS B CE 1 ATOM 11875 N NZ . LYS B 2 618 ? -8.109 6.931 58.235 1.00 121.30 ? 618 LYS B NZ 1 ATOM 11876 N N . LYS B 2 619 ? -10.471 6.887 64.731 1.00 86.54 ? 619 LYS B N 1 ATOM 11877 C CA . LYS B 2 619 ? -9.805 6.418 65.939 1.00 86.21 ? 619 LYS B CA 1 ATOM 11878 C C . LYS B 2 619 ? -10.635 5.354 66.640 1.00 100.28 ? 619 LYS B C 1 ATOM 11879 O O . LYS B 2 619 ? -10.194 4.218 66.791 1.00 143.55 ? 619 LYS B O 1 ATOM 11880 C CB . LYS B 2 619 ? -9.516 7.581 66.886 1.00 87.05 ? 619 LYS B CB 1 ATOM 11881 C CG . LYS B 2 619 ? -8.618 8.651 66.281 1.00 87.52 ? 619 LYS B CG 1 ATOM 11882 C CD . LYS B 2 619 ? -7.232 8.111 65.954 1.00 100.17 ? 619 LYS B CD 1 ATOM 11883 C CE . LYS B 2 619 ? -6.399 7.919 67.212 1.00 115.99 ? 619 LYS B CE 1 ATOM 11884 N NZ . LYS B 2 619 ? -5.020 7.435 66.914 1.00 102.85 ? 619 LYS B NZ 1 ATOM 11885 N N . PHE B 2 620 ? -11.835 5.720 67.075 1.00 86.29 ? 620 PHE B N 1 ATOM 11886 C CA . PHE B 2 620 ? -12.666 4.794 67.835 1.00 93.40 ? 620 PHE B CA 1 ATOM 11887 C C . PHE B 2 620 ? -13.490 3.846 66.963 1.00 98.47 ? 620 PHE B C 1 ATOM 11888 O O . PHE B 2 620 ? -14.207 2.989 67.484 1.00 88.27 ? 620 PHE B O 1 ATOM 11889 C CB . PHE B 2 620 ? -13.577 5.576 68.773 1.00 85.48 ? 620 PHE B CB 1 ATOM 11890 C CG . PHE B 2 620 ? -12.840 6.251 69.885 1.00 85.43 ? 620 PHE B CG 1 ATOM 11891 C CD1 . PHE B 2 620 ? -12.469 5.542 71.013 1.00 85.00 ? 620 PHE B CD1 1 ATOM 11892 C CD2 . PHE B 2 620 ? -12.499 7.588 69.797 1.00 103.21 ? 620 PHE B CD2 1 ATOM 11893 C CE1 . PHE B 2 620 ? -11.781 6.157 72.040 1.00 93.87 ? 620 PHE B CE1 1 ATOM 11894 C CE2 . PHE B 2 620 ? -11.812 8.210 70.820 1.00 104.36 ? 620 PHE B CE2 1 ATOM 11895 C CZ . PHE B 2 620 ? -11.452 7.493 71.943 1.00 88.50 ? 620 PHE B CZ 1 ATOM 11896 N N . ASP B 2 621 ? -13.383 4.005 65.644 1.00 99.67 ? 621 ASP B N 1 ATOM 11897 C CA . ASP B 2 621 ? -13.962 3.062 64.683 1.00 103.43 ? 621 ASP B CA 1 ATOM 11898 C C . ASP B 2 621 ? -15.465 2.864 64.874 1.00 103.30 ? 621 ASP B C 1 ATOM 11899 O O . ASP B 2 621 ? -15.945 1.734 64.943 1.00 113.11 ? 621 ASP B O 1 ATOM 11900 C CB . ASP B 2 621 ? -13.242 1.712 64.776 1.00 121.70 ? 621 ASP B CB 1 ATOM 11901 C CG . ASP B 2 621 ? -13.482 0.835 63.562 1.00 124.83 ? 621 ASP B CG 1 ATOM 11902 O OD1 . ASP B 2 621 ? -13.414 1.359 62.430 1.00 124.86 ? 621 ASP B OD1 1 ATOM 11903 O OD2 . ASP B 2 621 ? -13.742 -0.375 63.743 1.00 113.65 ? 621 ASP B OD2 1 ATOM 11904 N N . ARG B 2 622 ? -16.204 3.965 64.957 1.00 113.12 ? 622 ARG B N 1 ATOM 11905 C CA . ARG B 2 622 ? -17.633 3.892 65.238 1.00 106.69 ? 622 ARG B CA 1 ATOM 11906 C C . ARG B 2 622 ? -18.361 5.180 64.874 1.00 114.99 ? 622 ARG B C 1 ATOM 11907 O O . ARG B 2 622 ? -17.784 6.087 64.272 1.00 99.40 ? 622 ARG B O 1 ATOM 11908 C CB . ARG B 2 622 ? -17.861 3.571 66.715 1.00 108.87 ? 622 ARG B CB 1 ATOM 11909 C CG . ARG B 2 622 ? -17.300 4.617 67.660 1.00 117.14 ? 622 ARG B CG 1 ATOM 11910 C CD . ARG B 2 622 ? -17.300 4.119 69.092 1.00 121.47 ? 622 ARG B CD 1 ATOM 11911 N NE . ARG B 2 622 ? -16.821 5.139 70.019 1.00 115.09 ? 622 ARG B NE 1 ATOM 11912 C CZ . ARG B 2 622 ? -16.652 4.940 71.321 1.00 115.43 ? 622 ARG B CZ 1 ATOM 11913 N NH1 . ARG B 2 622 ? -16.918 3.755 71.852 1.00 122.90 ? 622 ARG B NH1 1 ATOM 11914 N NH2 . ARG B 2 622 ? -16.213 5.925 72.092 1.00 114.80 ? 622 ARG B NH2 1 ATOM 11915 N N . GLY B 2 623 ? -19.636 5.246 65.246 1.00 140.16 ? 623 GLY B N 1 ATOM 11916 C CA . GLY B 2 623 ? -20.459 6.409 64.975 1.00 145.75 ? 623 GLY B CA 1 ATOM 11917 C C . GLY B 2 623 ? -20.838 6.511 63.512 1.00 138.92 ? 623 GLY B C 1 ATOM 11918 O O . GLY B 2 623 ? -20.682 5.556 62.751 1.00 142.12 ? 623 GLY B O 1 ATOM 11919 N N . ALA B 2 624 ? -21.336 7.677 63.114 1.00 131.81 ? 624 ALA B N 1 ATOM 11920 C CA . ALA B 2 624 ? -21.683 7.911 61.721 1.00 123.87 ? 624 ALA B CA 1 ATOM 11921 C C . ALA B 2 624 ? -20.415 8.072 60.895 1.00 120.52 ? 624 ALA B C 1 ATOM 11922 O O . ALA B 2 624 ? -19.308 7.994 61.432 1.00 132.87 ? 624 ALA B O 1 ATOM 11923 C CB . ALA B 2 624 ? -22.568 9.134 61.589 1.00 129.51 ? 624 ALA B CB 1 ATOM 11924 N N . LEU B 2 625 ? -20.585 8.263 59.587 1.00 116.10 ? 625 LEU B N 1 ATOM 11925 C CA . LEU B 2 625 ? -19.474 8.441 58.645 1.00 118.43 ? 625 LEU B CA 1 ATOM 11926 C C . LEU B 2 625 ? -18.631 7.167 58.513 1.00 125.01 ? 625 LEU B C 1 ATOM 11927 O O . LEU B 2 625 ? -17.766 7.067 57.642 1.00 116.70 ? 625 LEU B O 1 ATOM 11928 C CB . LEU B 2 625 ? -18.592 9.624 59.065 1.00 121.96 ? 625 LEU B CB 1 ATOM 11929 C CG . LEU B 2 625 ? -17.661 10.238 58.019 1.00 122.70 ? 625 LEU B CG 1 ATOM 11930 C CD1 . LEU B 2 625 ? -18.466 10.944 56.937 1.00 121.84 ? 625 LEU B CD1 1 ATOM 11931 C CD2 . LEU B 2 625 ? -16.671 11.192 58.673 1.00 108.00 ? 625 LEU B CD2 1 ATOM 11932 N N . HIS B 2 626 ? -18.903 6.196 59.377 1.00 143.66 ? 626 HIS B N 1 ATOM 11933 C CA . HIS B 2 626 ? -18.228 4.906 59.367 1.00 144.46 ? 626 HIS B CA 1 ATOM 11934 C C . HIS B 2 626 ? -18.973 3.932 58.466 1.00 145.40 ? 626 HIS B C 1 ATOM 11935 O O . HIS B 2 626 ? -18.425 3.432 57.484 1.00 160.29 ? 626 HIS B O 1 ATOM 11936 C CB . HIS B 2 626 ? -18.120 4.343 60.786 1.00 143.77 ? 626 HIS B CB 1 ATOM 11937 C CG . HIS B 2 626 ? -17.381 3.043 60.868 1.00 138.06 ? 626 HIS B CG 1 ATOM 11938 N ND1 . HIS B 2 626 ? -17.462 2.210 61.962 1.00 127.96 ? 626 HIS B ND1 1 ATOM 11939 C CD2 . HIS B 2 626 ? -16.545 2.436 59.993 1.00 134.38 ? 626 HIS B CD2 1 ATOM 11940 C CE1 . HIS B 2 626 ? -16.711 1.143 61.757 1.00 122.63 ? 626 HIS B CE1 1 ATOM 11941 N NE2 . HIS B 2 626 ? -16.144 1.255 60.570 1.00 126.69 ? 626 HIS B NE2 1 ATOM 11942 N N . ASP B 2 627 ? -20.227 3.664 58.819 1.00 138.65 ? 627 ASP B N 1 ATOM 11943 C CA . ASP B 2 627 ? -21.057 2.693 58.112 1.00 141.61 ? 627 ASP B CA 1 ATOM 11944 C C . ASP B 2 627 ? -21.283 3.025 56.636 1.00 140.95 ? 627 ASP B C 1 ATOM 11945 O O . ASP B 2 627 ? -21.738 2.176 55.871 1.00 150.31 ? 627 ASP B O 1 ATOM 11946 C CB . ASP B 2 627 ? -22.406 2.556 58.819 1.00 142.01 ? 627 ASP B CB 1 ATOM 11947 C CG . ASP B 2 627 ? -22.841 3.839 59.494 1.00 142.73 ? 627 ASP B CG 1 ATOM 11948 O OD1 . ASP B 2 627 ? -21.975 4.532 60.071 1.00 137.92 ? 627 ASP B OD1 1 ATOM 11949 O OD2 . ASP B 2 627 ? -24.047 4.154 59.448 1.00 156.99 ? 627 ASP B OD2 1 ATOM 11950 N N . GLU B 2 628 ? -20.970 4.253 56.236 1.00 134.11 ? 628 GLU B N 1 ATOM 11951 C CA . GLU B 2 628 ? -21.029 4.621 54.825 1.00 134.52 ? 628 GLU B CA 1 ATOM 11952 C C . GLU B 2 628 ? -19.731 4.246 54.118 1.00 139.33 ? 628 GLU B C 1 ATOM 11953 O O . GLU B 2 628 ? -19.606 4.417 52.904 1.00 151.26 ? 628 GLU B O 1 ATOM 11954 C CB . GLU B 2 628 ? -21.299 6.118 54.658 1.00 134.09 ? 628 GLU B CB 1 ATOM 11955 C CG . GLU B 2 628 ? -22.685 6.568 55.083 1.00 133.73 ? 628 GLU B CG 1 ATOM 11956 C CD . GLU B 2 628 ? -22.788 6.827 56.572 1.00 141.06 ? 628 GLU B CD 1 ATOM 11957 O OE1 . GLU B 2 628 ? -21.822 6.521 57.304 1.00 142.73 ? 628 GLU B OE1 1 ATOM 11958 O OE2 . GLU B 2 628 ? -23.838 7.342 57.010 1.00 144.18 ? 628 GLU B OE2 1 ATOM 11959 N N . ASN B 2 629 ? -18.768 3.751 54.894 1.00 138.33 ? 629 ASN B N 1 ATOM 11960 C CA . ASN B 2 629 ? -17.438 3.392 54.398 1.00 147.46 ? 629 ASN B CA 1 ATOM 11961 C C . ASN B 2 629 ? -16.743 4.582 53.750 1.00 137.92 ? 629 ASN B C 1 ATOM 11962 O O . ASN B 2 629 ? -15.851 4.424 52.917 1.00 139.92 ? 629 ASN B O 1 ATOM 11963 C CB . ASN B 2 629 ? -17.518 2.219 53.417 1.00 153.86 ? 629 ASN B CB 1 ATOM 11964 C CG . ASN B 2 629 ? -17.900 0.916 54.095 1.00 154.66 ? 629 ASN B CG 1 ATOM 11965 O OD1 . ASN B 2 629 ? -18.897 0.288 53.742 1.00 156.31 ? 629 ASN B OD1 1 ATOM 11966 N ND2 . ASN B 2 629 ? -17.106 0.506 55.078 1.00 152.44 ? 629 ASN B ND2 1 ATOM 11967 N N . THR B 2 630 ? -17.169 5.776 54.144 1.00 134.17 ? 630 THR B N 1 ATOM 11968 C CA . THR B 2 630 ? -16.537 7.013 53.715 1.00 135.98 ? 630 THR B CA 1 ATOM 11969 C C . THR B 2 630 ? -15.544 7.457 54.777 1.00 134.55 ? 630 THR B C 1 ATOM 11970 O O . THR B 2 630 ? -14.972 8.544 54.682 1.00 116.86 ? 630 THR B O 1 ATOM 11971 C CB . THR B 2 630 ? -17.566 8.132 53.469 1.00 125.09 ? 630 THR B CB 1 ATOM 11972 O OG1 . THR B 2 630 ? -18.041 8.635 54.723 1.00 122.19 ? 630 THR B OG1 1 ATOM 11973 C CG2 . THR B 2 630 ? -18.740 7.605 52.663 1.00 119.91 ? 630 THR B CG2 1 ATOM 11974 N N . CYS B 2 631 ? -15.367 6.608 55.790 1.00 148.77 ? 631 CYS B N 1 ATOM 11975 C CA . CYS B 2 631 ? -14.590 6.944 56.981 1.00 156.88 ? 631 CYS B CA 1 ATOM 11976 C C . CYS B 2 631 ? -13.252 7.566 56.622 1.00 153.71 ? 631 CYS B C 1 ATOM 11977 O O . CYS B 2 631 ? -12.880 8.597 57.182 1.00 161.96 ? 631 CYS B O 1 ATOM 11978 C CB . CYS B 2 631 ? -14.372 5.712 57.855 1.00 167.56 ? 631 CYS B CB 1 ATOM 11979 S SG . CYS B 2 631 ? -13.735 6.122 59.493 1.00 254.63 ? 631 CYS B SG 1 ATOM 11980 N N . ASN B 2 632 ? -12.524 6.957 55.692 1.00 146.40 ? 632 ASN B N 1 ATOM 11981 C CA . ASN B 2 632 ? -11.501 7.738 55.029 1.00 147.21 ? 632 ASN B CA 1 ATOM 11982 C C . ASN B 2 632 ? -11.842 7.908 53.558 1.00 135.66 ? 632 ASN B C 1 ATOM 11983 O O . ASN B 2 632 ? -11.499 7.080 52.714 1.00 139.78 ? 632 ASN B O 1 ATOM 11984 C CB . ASN B 2 632 ? -10.134 7.063 55.187 1.00 163.77 ? 632 ASN B CB 1 ATOM 11985 C CG . ASN B 2 632 ? -8.978 7.954 54.762 1.00 160.62 ? 632 ASN B CG 1 ATOM 11986 O OD1 . ASN B 2 632 ? -9.148 8.895 53.986 1.00 157.19 ? 632 ASN B OD1 1 ATOM 11987 N ND2 . ASN B 2 632 ? -7.788 7.651 55.268 1.00 155.25 ? 632 ASN B ND2 1 ATOM 11988 N N . ARG B 2 633 ? -12.530 9.004 53.275 1.00 138.35 ? 633 ARG B N 1 ATOM 11989 C CA . ARG B 2 633 ? -12.464 9.741 52.029 1.00 147.82 ? 633 ARG B CA 1 ATOM 11990 C C . ARG B 2 633 ? -12.531 11.191 52.469 1.00 142.09 ? 633 ARG B C 1 ATOM 11991 O O . ARG B 2 633 ? -11.599 11.976 52.294 1.00 137.66 ? 633 ARG B O 1 ATOM 11992 C CB . ARG B 2 633 ? -13.595 9.381 51.066 1.00 154.23 ? 633 ARG B CB 1 ATOM 11993 C CG . ARG B 2 633 ? -13.620 10.254 49.816 1.00 157.26 ? 633 ARG B CG 1 ATOM 11994 C CD . ARG B 2 633 ? -13.710 9.430 48.539 1.00 159.93 ? 633 ARG B CD 1 ATOM 11995 N NE . ARG B 2 633 ? -12.580 8.519 48.381 1.00 156.24 ? 633 ARG B NE 1 ATOM 11996 C CZ . ARG B 2 633 ? -12.395 7.735 47.323 1.00 151.79 ? 633 ARG B CZ 1 ATOM 11997 N NH1 . ARG B 2 633 ? -13.266 7.752 46.323 1.00 153.60 ? 633 ARG B NH1 1 ATOM 11998 N NH2 . ARG B 2 633 ? -11.339 6.934 47.263 1.00 147.79 ? 633 ARG B NH2 1 ATOM 11999 N N . TYR B 2 634 ? -13.684 11.508 53.055 1.00 142.79 ? 634 TYR B N 1 ATOM 12000 C CA . TYR B 2 634 ? -14.006 12.820 53.597 1.00 146.36 ? 634 TYR B CA 1 ATOM 12001 C C . TYR B 2 634 ? -13.045 13.267 54.696 1.00 147.12 ? 634 TYR B C 1 ATOM 12002 O O . TYR B 2 634 ? -12.838 14.467 54.886 1.00 157.74 ? 634 TYR B O 1 ATOM 12003 C CB . TYR B 2 634 ? -15.439 12.822 54.138 1.00 138.17 ? 634 TYR B CB 1 ATOM 12004 C CG . TYR B 2 634 ? -16.499 12.540 53.093 1.00 145.98 ? 634 TYR B CG 1 ATOM 12005 C CD1 . TYR B 2 634 ? -16.269 12.809 51.749 1.00 158.03 ? 634 TYR B CD1 1 ATOM 12006 C CD2 . TYR B 2 634 ? -17.731 12.010 53.453 1.00 148.09 ? 634 TYR B CD2 1 ATOM 12007 C CE1 . TYR B 2 634 ? -17.236 12.555 50.792 1.00 159.71 ? 634 TYR B CE1 1 ATOM 12008 C CE2 . TYR B 2 634 ? -18.704 11.753 52.502 1.00 160.85 ? 634 TYR B CE2 1 ATOM 12009 C CZ . TYR B 2 634 ? -18.451 12.028 51.174 1.00 157.61 ? 634 TYR B CZ 1 ATOM 12010 O OH . TYR B 2 634 ? -19.415 11.775 50.223 1.00 148.04 ? 634 TYR B OH 1 ATOM 12011 N N . CYS B 2 635 ? -12.457 12.318 55.421 1.00 132.82 ? 635 CYS B N 1 ATOM 12012 C CA . CYS B 2 635 ? -11.447 12.689 56.404 1.00 135.84 ? 635 CYS B CA 1 ATOM 12013 C C . CYS B 2 635 ? -10.068 12.433 55.820 1.00 136.57 ? 635 CYS B C 1 ATOM 12014 O O . CYS B 2 635 ? -9.612 11.292 55.756 1.00 144.80 ? 635 CYS B O 1 ATOM 12015 C CB . CYS B 2 635 ? -11.613 11.889 57.704 1.00 125.15 ? 635 CYS B CB 1 ATOM 12016 S SG . CYS B 2 635 ? -13.181 12.095 58.589 1.00 107.90 ? 635 CYS B SG 1 ATOM 12017 N N . ARG B 2 636 ? -9.405 13.504 55.398 1.00 136.92 ? 636 ARG B N 1 ATOM 12018 C CA . ARG B 2 636 ? -8.025 13.425 54.941 1.00 139.02 ? 636 ARG B CA 1 ATOM 12019 C C . ARG B 2 636 ? -7.059 13.920 56.012 1.00 139.06 ? 636 ARG B C 1 ATOM 12020 O O . ARG B 2 636 ? -5.842 13.872 55.835 1.00 149.39 ? 636 ARG B O 1 ATOM 12021 C CB . ARG B 2 636 ? -7.851 14.216 53.642 1.00 154.68 ? 636 ARG B CB 1 ATOM 12022 C CG . ARG B 2 636 ? -8.463 13.526 52.427 1.00 153.83 ? 636 ARG B CG 1 ATOM 12023 C CD . ARG B 2 636 ? -8.432 14.414 51.191 1.00 158.59 ? 636 ARG B CD 1 ATOM 12024 N NE . ARG B 2 636 ? -9.422 15.485 51.257 1.00 165.97 ? 636 ARG B NE 1 ATOM 12025 C CZ . ARG B 2 636 ? -10.661 15.388 50.782 1.00 164.12 ? 636 ARG B CZ 1 ATOM 12026 N NH1 . ARG B 2 636 ? -11.065 14.265 50.203 1.00 164.52 ? 636 ARG B NH1 1 ATOM 12027 N NH2 . ARG B 2 636 ? -11.496 16.413 50.884 1.00 158.99 ? 636 ARG B NH2 1 ATOM 12028 N N . ASP B 2 637 ? -7.612 14.388 57.127 1.00 136.17 ? 637 ASP B N 1 ATOM 12029 C CA . ASP B 2 637 ? -6.815 15.015 58.176 1.00 129.17 ? 637 ASP B CA 1 ATOM 12030 C C . ASP B 2 637 ? -5.937 14.006 58.904 1.00 127.81 ? 637 ASP B C 1 ATOM 12031 O O . ASP B 2 637 ? -6.404 12.944 59.318 1.00 129.11 ? 637 ASP B O 1 ATOM 12032 C CB . ASP B 2 637 ? -7.723 15.730 59.181 1.00 137.95 ? 637 ASP B CB 1 ATOM 12033 C CG . ASP B 2 637 ? -8.584 16.799 58.534 1.00 148.42 ? 637 ASP B CG 1 ATOM 12034 O OD1 . ASP B 2 637 ? -8.168 17.977 58.529 1.00 142.26 ? 637 ASP B OD1 1 ATOM 12035 O OD2 . ASP B 2 637 ? -9.677 16.460 58.034 1.00 156.50 ? 637 ASP B OD2 1 ATOM 12036 N N . GLU B 2 638 ? -4.660 14.341 59.053 1.00 130.65 ? 638 GLU B N 1 ATOM 12037 C CA . GLU B 2 638 ? -3.744 13.513 59.824 1.00 122.89 ? 638 GLU B CA 1 ATOM 12038 C C . GLU B 2 638 ? -4.131 13.539 61.295 1.00 126.31 ? 638 GLU B C 1 ATOM 12039 O O . GLU B 2 638 ? -4.287 14.606 61.887 1.00 143.15 ? 638 GLU B O 1 ATOM 12040 C CB . GLU B 2 638 ? -2.300 13.986 59.645 1.00 128.64 ? 638 GLU B CB 1 ATOM 12041 C CG . GLU B 2 638 ? -1.661 13.556 58.333 1.00 149.61 ? 638 GLU B CG 1 ATOM 12042 C CD . GLU B 2 638 ? -1.364 12.066 58.285 1.00 161.91 ? 638 GLU B CD 1 ATOM 12043 O OE1 . GLU B 2 638 ? -1.155 11.534 57.174 1.00 155.92 ? 638 GLU B OE1 1 ATOM 12044 O OE2 . GLU B 2 638 ? -1.333 11.426 59.359 1.00 161.70 ? 638 GLU B OE2 1 ATOM 12045 N N . ILE B 2 639 ? -4.292 12.358 61.880 1.00 112.18 ? 639 ILE B N 1 ATOM 12046 C CA . ILE B 2 639 ? -4.684 12.246 63.279 1.00 101.57 ? 639 ILE B CA 1 ATOM 12047 C C . ILE B 2 639 ? -3.642 11.462 64.066 1.00 104.07 ? 639 ILE B C 1 ATOM 12048 O O . ILE B 2 639 ? -3.179 10.417 63.617 1.00 110.76 ? 639 ILE B O 1 ATOM 12049 C CB . ILE B 2 639 ? -6.059 11.567 63.424 1.00 100.54 ? 639 ILE B CB 1 ATOM 12050 C CG1 . ILE B 2 639 ? -7.099 12.282 62.558 1.00 101.76 ? 639 ILE B CG1 1 ATOM 12051 C CG2 . ILE B 2 639 ? -6.494 11.550 64.878 1.00 113.47 ? 639 ILE B CG2 1 ATOM 12052 C CD1 . ILE B 2 639 ? -8.496 11.713 62.678 1.00 95.24 ? 639 ILE B CD1 1 ATOM 12053 N N . GLU B 2 640 ? -3.260 11.976 65.230 1.00 99.41 ? 640 GLU B N 1 ATOM 12054 C CA . GLU B 2 640 ? -2.287 11.294 66.077 1.00 99.22 ? 640 GLU B CA 1 ATOM 12055 C C . GLU B 2 640 ? -2.687 11.326 67.548 1.00 107.45 ? 640 GLU B C 1 ATOM 12056 O O . GLU B 2 640 ? -2.885 12.394 68.125 1.00 129.46 ? 640 GLU B O 1 ATOM 12057 C CB . GLU B 2 640 ? -0.897 11.913 65.900 1.00 110.71 ? 640 GLU B CB 1 ATOM 12058 C CG . GLU B 2 640 ? -0.256 11.632 64.546 1.00 131.43 ? 640 GLU B CG 1 ATOM 12059 C CD . GLU B 2 640 ? -0.044 10.147 64.290 1.00 142.74 ? 640 GLU B CD 1 ATOM 12060 O OE1 . GLU B 2 640 ? 0.152 9.389 65.265 1.00 130.05 ? 640 GLU B OE1 1 ATOM 12061 O OE2 . GLU B 2 640 ? -0.075 9.736 63.110 1.00 147.11 ? 640 GLU B OE2 1 ATOM 12062 N N . SER B 2 641 ? -2.795 10.146 68.152 1.00 106.54 ? 641 SER B N 1 ATOM 12063 C CA . SER B 2 641 ? -3.130 10.037 69.568 1.00 100.99 ? 641 SER B CA 1 ATOM 12064 C C . SER B 2 641 ? -1.931 10.417 70.432 1.00 95.28 ? 641 SER B C 1 ATOM 12065 O O . SER B 2 641 ? -0.846 9.858 70.283 1.00 120.81 ? 641 SER B O 1 ATOM 12066 C CB . SER B 2 641 ? -3.607 8.619 69.899 1.00 107.40 ? 641 SER B CB 1 ATOM 12067 O OG . SER B 2 641 ? -2.711 7.640 69.398 1.00 135.58 ? 641 SER B OG 1 ATOM 12068 N N . VAL B 2 642 ? -2.132 11.376 71.331 1.00 95.62 ? 642 VAL B N 1 ATOM 12069 C CA . VAL B 2 642 ? -1.039 11.920 72.134 1.00 106.52 ? 642 VAL B CA 1 ATOM 12070 C C . VAL B 2 642 ? -1.429 12.214 73.582 1.00 100.98 ? 642 VAL B C 1 ATOM 12071 O O . VAL B 2 642 ? -2.605 12.211 73.938 1.00 103.01 ? 642 VAL B O 1 ATOM 12072 C CB . VAL B 2 642 ? -0.495 13.228 71.518 1.00 105.95 ? 642 VAL B CB 1 ATOM 12073 C CG1 . VAL B 2 642 ? 0.294 12.946 70.246 1.00 114.21 ? 642 VAL B CG1 1 ATOM 12074 C CG2 . VAL B 2 642 ? -1.635 14.195 71.246 1.00 98.10 ? 642 VAL B CG2 1 ATOM 12075 N N . LYS B 2 643 ? -0.419 12.462 74.409 1.00 99.72 ? 643 LYS B N 1 ATOM 12076 C CA . LYS B 2 643 ? -0.608 13.070 75.722 1.00 100.39 ? 643 LYS B CA 1 ATOM 12077 C C . LYS B 2 643 ? -0.723 14.568 75.494 1.00 126.57 ? 643 LYS B C 1 ATOM 12078 O O . LYS B 2 643 ? -0.944 15.003 74.363 1.00 135.47 ? 643 LYS B O 1 ATOM 12079 C CB . LYS B 2 643 ? 0.553 12.772 76.671 1.00 102.61 ? 643 LYS B CB 1 ATOM 12080 C CG . LYS B 2 643 ? 1.198 11.406 76.522 1.00 118.21 ? 643 LYS B CG 1 ATOM 12081 C CD . LYS B 2 643 ? 2.406 11.311 77.445 1.00 116.02 ? 643 LYS B CD 1 ATOM 12082 C CE . LYS B 2 643 ? 3.206 10.041 77.225 1.00 115.70 ? 643 LYS B CE 1 ATOM 12083 N NZ . LYS B 2 643 ? 4.428 10.024 78.080 1.00 123.29 ? 643 LYS B NZ 1 ATOM 12084 N N . GLU B 2 644 ? -0.588 15.356 76.559 1.00 134.96 ? 644 GLU B N 1 ATOM 12085 C CA . GLU B 2 644 ? -0.410 16.795 76.386 1.00 142.19 ? 644 GLU B CA 1 ATOM 12086 C C . GLU B 2 644 ? -1.572 17.452 75.654 1.00 139.06 ? 644 GLU B C 1 ATOM 12087 O O . GLU B 2 644 ? -2.641 17.638 76.239 1.00 149.58 ? 644 GLU B O 1 ATOM 12088 C CB . GLU B 2 644 ? 0.907 17.093 75.661 1.00 172.17 ? 644 GLU B CB 1 ATOM 12089 C CG . GLU B 2 644 ? 2.130 17.051 76.570 1.00 179.58 ? 644 GLU B CG 1 ATOM 12090 C CD . GLU B 2 644 ? 2.083 18.106 77.664 1.00 170.55 ? 644 GLU B CD 1 ATOM 12091 O OE1 . GLU B 2 644 ? 1.509 19.190 77.426 1.00 171.88 ? 644 GLU B OE1 1 ATOM 12092 O OE2 . GLU B 2 644 ? 2.617 17.850 78.763 1.00 164.82 ? 644 GLU B OE2 1 ATOM 12093 N N . LEU B 2 645 ? -1.344 17.803 74.386 1.00 123.25 ? 645 LEU B N 1 ATOM 12094 C CA . LEU B 2 645 ? -2.048 18.878 73.690 1.00 123.42 ? 645 LEU B CA 1 ATOM 12095 C C . LEU B 2 645 ? -1.630 20.180 74.356 1.00 113.45 ? 645 LEU B C 1 ATOM 12096 O O . LEU B 2 645 ? -2.396 20.819 75.073 1.00 119.95 ? 645 LEU B O 1 ATOM 12097 C CB . LEU B 2 645 ? -3.572 18.685 73.722 1.00 101.33 ? 645 LEU B CB 1 ATOM 12098 C CG . LEU B 2 645 ? -4.440 19.258 72.601 1.00 113.98 ? 645 LEU B CG 1 ATOM 12099 C CD1 . LEU B 2 645 ? -5.877 18.784 72.756 1.00 106.32 ? 645 LEU B CD1 1 ATOM 12100 C CD2 . LEU B 2 645 ? -4.386 20.771 72.587 1.00 135.16 ? 645 LEU B CD2 1 ATOM 12101 N N . LYS B 2 646 ? -0.369 20.530 74.115 1.00 119.99 ? 646 LYS B N 1 ATOM 12102 C CA . LYS B 2 646 ? 0.285 21.695 74.699 1.00 144.78 ? 646 LYS B CA 1 ATOM 12103 C C . LYS B 2 646 ? -0.432 22.997 74.362 1.00 157.23 ? 646 LYS B C 1 ATOM 12104 O O . LYS B 2 646 ? -1.066 23.121 73.313 1.00 153.82 ? 646 LYS B O 1 ATOM 12105 C CB . LYS B 2 646 ? 1.742 21.759 74.232 1.00 154.15 ? 646 LYS B CB 1 ATOM 12106 C CG . LYS B 2 646 ? 2.586 20.579 74.699 1.00 148.45 ? 646 LYS B CG 1 ATOM 12107 C CD . LYS B 2 646 ? 3.730 20.272 73.744 1.00 144.04 ? 646 LYS B CD 1 ATOM 12108 C CE . LYS B 2 646 ? 4.518 19.058 74.217 1.00 139.58 ? 646 LYS B CE 1 ATOM 12109 N NZ . LYS B 2 646 ? 5.525 18.605 73.218 1.00 145.77 ? 646 LYS B NZ 1 ATOM 12110 N N . ASP B 2 647 ? -0.319 23.962 75.271 1.00 162.48 ? 647 ASP B N 1 ATOM 12111 C CA . ASP B 2 647 ? -1.054 25.220 75.189 1.00 164.74 ? 647 ASP B CA 1 ATOM 12112 C C . ASP B 2 647 ? -0.785 26.020 73.919 1.00 170.99 ? 647 ASP B C 1 ATOM 12113 O O . ASP B 2 647 ? -1.585 26.880 73.549 1.00 169.82 ? 647 ASP B O 1 ATOM 12114 C CB . ASP B 2 647 ? -0.734 26.088 76.407 1.00 163.85 ? 647 ASP B CB 1 ATOM 12115 C CG . ASP B 2 647 ? -1.066 25.400 77.713 1.00 156.16 ? 647 ASP B CG 1 ATOM 12116 O OD1 . ASP B 2 647 ? -2.004 24.576 77.729 1.00 138.47 ? 647 ASP B OD1 1 ATOM 12117 O OD2 . ASP B 2 647 ? -0.386 25.682 78.722 1.00 157.42 ? 647 ASP B OD2 1 ATOM 12118 N N . THR B 2 648 ? 0.329 25.745 73.247 1.00 167.17 ? 648 THR B N 1 ATOM 12119 C CA . THR B 2 648 ? 0.634 26.480 72.027 1.00 176.84 ? 648 THR B CA 1 ATOM 12120 C C . THR B 2 648 ? 0.296 25.657 70.791 1.00 171.06 ? 648 THR B C 1 ATOM 12121 O O . THR B 2 648 ? 1.004 24.718 70.427 1.00 159.31 ? 648 THR B O 1 ATOM 12122 C CB . THR B 2 648 ? 2.119 26.897 71.977 1.00 181.86 ? 648 THR B CB 1 ATOM 12123 O OG1 . THR B 2 648 ? 2.506 27.131 70.617 1.00 179.15 ? 648 THR B OG1 1 ATOM 12124 C CG2 . THR B 2 648 ? 3.007 25.810 72.573 1.00 178.92 ? 648 THR B CG2 1 ATOM 12125 N N . GLY B 2 649 ? -0.807 26.029 70.152 1.00 182.08 ? 649 GLY B N 1 ATOM 12126 C CA . GLY B 2 649 ? -1.216 25.435 68.897 1.00 186.06 ? 649 GLY B CA 1 ATOM 12127 C C . GLY B 2 649 ? -1.138 26.422 67.752 1.00 186.98 ? 649 GLY B C 1 ATOM 12128 O O . GLY B 2 649 ? -1.623 26.133 66.661 1.00 199.94 ? 649 GLY B O 1 ATOM 12129 N N . LYS B 2 650 ? -0.542 27.586 68.007 1.00 172.55 ? 650 LYS B N 1 ATOM 12130 C CA . LYS B 2 650 ? -0.621 28.716 67.083 1.00 170.34 ? 650 LYS B CA 1 ATOM 12131 C C . LYS B 2 650 ? -2.095 29.016 66.826 1.00 160.22 ? 650 LYS B C 1 ATOM 12132 O O . LYS B 2 650 ? -2.830 29.368 67.749 1.00 152.90 ? 650 LYS B O 1 ATOM 12133 C CB . LYS B 2 650 ? 0.123 28.435 65.770 1.00 171.26 ? 650 LYS B CB 1 ATOM 12134 C CG . LYS B 2 650 ? 1.646 28.421 65.882 1.00 173.22 ? 650 LYS B CG 1 ATOM 12135 C CD . LYS B 2 650 ? 2.172 27.094 66.417 1.00 168.93 ? 650 LYS B CD 1 ATOM 12136 C CE . LYS B 2 650 ? 3.693 27.075 66.465 1.00 171.31 ? 650 LYS B CE 1 ATOM 12137 N NZ . LYS B 2 650 ? 4.304 27.183 65.109 1.00 168.47 ? 650 LYS B NZ 1 ATOM 12138 N N . ASP B 2 651 ? -2.531 28.867 65.580 1.00 158.22 ? 651 ASP B N 1 ATOM 12139 C CA . ASP B 2 651 ? -3.954 28.947 65.282 1.00 153.94 ? 651 ASP B CA 1 ATOM 12140 C C . ASP B 2 651 ? -4.562 27.561 65.403 1.00 157.68 ? 651 ASP B C 1 ATOM 12141 O O . ASP B 2 651 ? -4.267 26.672 64.603 1.00 165.99 ? 651 ASP B O 1 ATOM 12142 C CB . ASP B 2 651 ? -4.198 29.510 63.882 1.00 162.94 ? 651 ASP B CB 1 ATOM 12143 C CG . ASP B 2 651 ? -4.040 31.012 63.824 1.00 185.57 ? 651 ASP B CG 1 ATOM 12144 O OD1 . ASP B 2 651 ? -4.186 31.664 64.879 1.00 189.54 ? 651 ASP B OD1 1 ATOM 12145 O OD2 . ASP B 2 651 ? -3.777 31.541 62.723 1.00 196.88 ? 651 ASP B OD2 1 ATOM 12146 N N . ALA B 2 652 ? -5.422 27.382 66.399 1.00 150.37 ? 652 ALA B N 1 ATOM 12147 C CA . ALA B 2 652 ? -6.003 26.074 66.660 1.00 128.44 ? 652 ALA B CA 1 ATOM 12148 C C . ALA B 2 652 ? -7.272 26.158 67.493 1.00 115.13 ? 652 ALA B C 1 ATOM 12149 O O . ALA B 2 652 ? -7.677 27.233 67.931 1.00 123.16 ? 652 ALA B O 1 ATOM 12150 C CB . ALA B 2 652 ? -4.984 25.180 67.353 1.00 112.18 ? 652 ALA B CB 1 ATOM 12151 N N . VAL B 2 653 ? -7.891 25.004 67.714 1.00 110.20 ? 653 VAL B N 1 ATOM 12152 C CA . VAL B 2 653 ? -9.101 24.915 68.515 1.00 109.42 ? 653 VAL B CA 1 ATOM 12153 C C . VAL B 2 653 ? -9.067 23.679 69.401 1.00 113.84 ? 653 VAL B C 1 ATOM 12154 O O . VAL B 2 653 ? -8.816 22.573 68.925 1.00 108.46 ? 653 VAL B O 1 ATOM 12155 C CB . VAL B 2 653 ? -10.368 24.871 67.634 1.00 109.33 ? 653 VAL B CB 1 ATOM 12156 C CG1 . VAL B 2 653 ? -11.106 26.194 67.693 1.00 129.42 ? 653 VAL B CG1 1 ATOM 12157 C CG2 . VAL B 2 653 ? -10.014 24.503 66.196 1.00 108.98 ? 653 VAL B CG2 1 ATOM 12158 N N . ASN B 2 654 ? -9.313 23.870 70.691 1.00 118.39 ? 654 ASN B N 1 ATOM 12159 C CA . ASN B 2 654 ? -9.435 22.748 71.609 1.00 104.13 ? 654 ASN B CA 1 ATOM 12160 C C . ASN B 2 654 ? -10.893 22.326 71.718 1.00 102.93 ? 654 ASN B C 1 ATOM 12161 O O . ASN B 2 654 ? -11.744 23.103 72.153 1.00 124.38 ? 654 ASN B O 1 ATOM 12162 C CB . ASN B 2 654 ? -8.870 23.103 72.986 1.00 105.11 ? 654 ASN B CB 1 ATOM 12163 C CG . ASN B 2 654 ? -7.396 23.451 72.936 1.00 107.93 ? 654 ASN B CG 1 ATOM 12164 O OD1 . ASN B 2 654 ? -6.897 24.216 73.762 1.00 118.84 ? 654 ASN B OD1 1 ATOM 12165 N ND2 . ASN B 2 654 ? -6.693 22.899 71.956 1.00 105.67 ? 654 ASN B ND2 1 ATOM 12166 N N . CYS B 2 655 ? -11.181 21.096 71.311 1.00 100.45 ? 655 CYS B N 1 ATOM 12167 C CA . CYS B 2 655 ? -12.555 20.621 71.262 1.00 99.65 ? 655 CYS B CA 1 ATOM 12168 C C . CYS B 2 655 ? -12.816 19.530 72.289 1.00 103.56 ? 655 CYS B C 1 ATOM 12169 O O . CYS B 2 655 ? -11.959 18.687 72.547 1.00 98.72 ? 655 CYS B O 1 ATOM 12170 C CB . CYS B 2 655 ? -12.886 20.110 69.861 1.00 98.57 ? 655 CYS B CB 1 ATOM 12171 S SG . CYS B 2 655 ? -12.596 21.321 68.554 1.00 112.45 ? 655 CYS B SG 1 ATOM 12172 N N . THR B 2 656 ? -14.008 19.560 72.875 1.00 113.00 ? 656 THR B N 1 ATOM 12173 C CA . THR B 2 656 ? -14.417 18.555 73.845 1.00 95.98 ? 656 THR B CA 1 ATOM 12174 C C . THR B 2 656 ? -15.798 18.021 73.502 1.00 95.29 ? 656 THR B C 1 ATOM 12175 O O . THR B 2 656 ? -16.704 18.785 73.168 1.00 125.92 ? 656 THR B O 1 ATOM 12176 C CB . THR B 2 656 ? -14.439 19.115 75.279 1.00 97.17 ? 656 THR B CB 1 ATOM 12177 O OG1 . THR B 2 656 ? -15.327 20.238 75.341 1.00 153.22 ? 656 THR B OG1 1 ATOM 12178 C CG2 . THR B 2 656 ? -13.048 19.553 75.704 1.00 97.98 ? 656 THR B CG2 1 ATOM 12179 N N . TYR B 2 657 ? -15.954 16.706 73.576 1.00 93.31 ? 657 TYR B N 1 ATOM 12180 C CA . TYR B 2 657 ? -17.248 16.087 73.345 1.00 92.76 ? 657 TYR B CA 1 ATOM 12181 C C . TYR B 2 657 ? -17.343 14.774 74.106 1.00 91.15 ? 657 TYR B C 1 ATOM 12182 O O . TYR B 2 657 ? -16.331 14.219 74.535 1.00 90.33 ? 657 TYR B O 1 ATOM 12183 C CB . TYR B 2 657 ? -17.487 15.866 71.849 1.00 92.43 ? 657 TYR B CB 1 ATOM 12184 C CG . TYR B 2 657 ? -16.751 14.686 71.265 1.00 90.61 ? 657 TYR B CG 1 ATOM 12185 C CD1 . TYR B 2 657 ? -15.408 14.777 70.925 1.00 98.23 ? 657 TYR B CD1 1 ATOM 12186 C CD2 . TYR B 2 657 ? -17.403 13.480 71.042 1.00 111.76 ? 657 TYR B CD2 1 ATOM 12187 C CE1 . TYR B 2 657 ? -14.732 13.696 70.386 1.00 90.10 ? 657 TYR B CE1 1 ATOM 12188 C CE2 . TYR B 2 657 ? -16.735 12.393 70.506 1.00 114.01 ? 657 TYR B CE2 1 ATOM 12189 C CZ . TYR B 2 657 ? -15.401 12.506 70.179 1.00 93.41 ? 657 TYR B CZ 1 ATOM 12190 O OH . TYR B 2 657 ? -14.737 11.424 69.644 1.00 98.36 ? 657 TYR B OH 1 ATOM 12191 N N . LYS B 2 658 ? -18.567 14.288 74.282 1.00 98.21 ? 658 LYS B N 1 ATOM 12192 C CA . LYS B 2 658 ? -18.803 13.042 74.997 1.00 93.09 ? 658 LYS B CA 1 ATOM 12193 C C . LYS B 2 658 ? -19.285 11.953 74.045 1.00 94.35 ? 658 LYS B C 1 ATOM 12194 O O . LYS B 2 658 ? -20.341 12.085 73.426 1.00 99.94 ? 658 LYS B O 1 ATOM 12195 C CB . LYS B 2 658 ? -19.819 13.256 76.121 1.00 95.94 ? 658 LYS B CB 1 ATOM 12196 C CG . LYS B 2 658 ? -20.233 11.985 76.838 1.00 99.51 ? 658 LYS B CG 1 ATOM 12197 C CD . LYS B 2 658 ? -21.142 12.285 78.019 1.00 108.06 ? 658 LYS B CD 1 ATOM 12198 C CE . LYS B 2 658 ? -20.437 13.153 79.051 1.00 124.46 ? 658 LYS B CE 1 ATOM 12199 N NZ . LYS B 2 658 ? -21.275 13.377 80.262 1.00 134.55 ? 658 LYS B NZ 1 ATOM 12200 N N . ASN B 2 659 ? -18.506 10.882 73.925 1.00 95.84 ? 659 ASN B N 1 ATOM 12201 C CA . ASN B 2 659 ? -18.877 9.766 73.061 1.00 104.19 ? 659 ASN B CA 1 ATOM 12202 C C . ASN B 2 659 ? -19.985 8.918 73.678 1.00 115.95 ? 659 ASN B C 1 ATOM 12203 O O . ASN B 2 659 ? -20.451 9.201 74.781 1.00 125.62 ? 659 ASN B O 1 ATOM 12204 C CB . ASN B 2 659 ? -17.657 8.896 72.746 1.00 97.49 ? 659 ASN B CB 1 ATOM 12205 C CG . ASN B 2 659 ? -16.898 8.474 73.992 1.00 96.14 ? 659 ASN B CG 1 ATOM 12206 O OD1 . ASN B 2 659 ? -17.455 8.422 75.088 1.00 97.67 ? 659 ASN B OD1 1 ATOM 12207 N ND2 . ASN B 2 659 ? -15.613 8.171 73.827 1.00 86.95 ? 659 ASN B ND2 1 ATOM 12208 N N . GLU B 2 660 ? -20.393 7.872 72.968 1.00 111.60 ? 660 GLU B N 1 ATOM 12209 C CA . GLU B 2 660 ? -21.508 7.035 73.402 1.00 116.10 ? 660 GLU B CA 1 ATOM 12210 C C . GLU B 2 660 ? -21.156 6.179 74.617 1.00 111.51 ? 660 GLU B C 1 ATOM 12211 O O . GLU B 2 660 ? -22.022 5.532 75.204 1.00 109.82 ? 660 GLU B O 1 ATOM 12212 C CB . GLU B 2 660 ? -21.983 6.141 72.252 1.00 126.26 ? 660 GLU B CB 1 ATOM 12213 C CG . GLU B 2 660 ? -20.866 5.525 71.416 1.00 147.53 ? 660 GLU B CG 1 ATOM 12214 C CD . GLU B 2 660 ? -20.416 6.425 70.275 1.00 161.37 ? 660 GLU B CD 1 ATOM 12215 O OE1 . GLU B 2 660 ? -20.438 7.663 70.442 1.00 149.81 ? 660 GLU B OE1 1 ATOM 12216 O OE2 . GLU B 2 660 ? -20.045 5.892 69.208 1.00 167.13 ? 660 GLU B OE2 1 ATOM 12217 N N . ASP B 2 661 ? -19.881 6.184 74.988 1.00 115.12 ? 661 ASP B N 1 ATOM 12218 C CA . ASP B 2 661 ? -19.413 5.455 76.160 1.00 114.00 ? 661 ASP B CA 1 ATOM 12219 C C . ASP B 2 661 ? -19.444 6.337 77.405 1.00 120.32 ? 661 ASP B C 1 ATOM 12220 O O . ASP B 2 661 ? -18.955 5.942 78.466 1.00 129.10 ? 661 ASP B O 1 ATOM 12221 C CB . ASP B 2 661 ? -18.005 4.914 75.922 1.00 111.48 ? 661 ASP B CB 1 ATOM 12222 C CG . ASP B 2 661 ? -17.976 3.810 74.882 1.00 120.67 ? 661 ASP B CG 1 ATOM 12223 O OD1 . ASP B 2 661 ? -18.982 3.079 74.761 1.00 115.32 ? 661 ASP B OD1 1 ATOM 12224 O OD2 . ASP B 2 661 ? -16.948 3.673 74.186 1.00 122.28 ? 661 ASP B OD2 1 ATOM 12225 N N . ASP B 2 662 ? -19.998 7.539 77.247 1.00 106.77 ? 662 ASP B N 1 ATOM 12226 C CA . ASP B 2 662 ? -20.122 8.526 78.321 1.00 105.01 ? 662 ASP B CA 1 ATOM 12227 C C . ASP B 2 662 ? -18.756 8.992 78.812 1.00 99.93 ? 662 ASP B C 1 ATOM 12228 O O . ASP B 2 662 ? -18.583 9.314 79.987 1.00 101.40 ? 662 ASP B O 1 ATOM 12229 C CB . ASP B 2 662 ? -20.941 7.964 79.489 1.00 114.62 ? 662 ASP B CB 1 ATOM 12230 C CG . ASP B 2 662 ? -22.358 7.600 79.085 1.00 137.80 ? 662 ASP B CG 1 ATOM 12231 O OD1 . ASP B 2 662 ? -22.977 8.372 78.322 1.00 146.34 ? 662 ASP B OD1 1 ATOM 12232 O OD2 . ASP B 2 662 ? -22.850 6.540 79.527 1.00 140.69 ? 662 ASP B OD2 1 ATOM 12233 N N . CYS B 2 663 ? -17.792 9.030 77.898 1.00 98.05 ? 663 CYS B N 1 ATOM 12234 C CA . CYS B 2 663 ? -16.444 9.495 78.207 1.00 91.89 ? 663 CYS B CA 1 ATOM 12235 C C . CYS B 2 663 ? -16.146 10.799 77.483 1.00 90.00 ? 663 CYS B C 1 ATOM 12236 O O . CYS B 2 663 ? -16.677 11.052 76.402 1.00 93.17 ? 663 CYS B O 1 ATOM 12237 C CB . CYS B 2 663 ? -15.404 8.437 77.831 1.00 89.06 ? 663 CYS B CB 1 ATOM 12238 S SG . CYS B 2 663 ? -15.367 7.004 78.924 1.00 103.07 ? 663 CYS B SG 1 ATOM 12239 N N . VAL B 2 664 ? -15.292 11.624 78.078 1.00 89.45 ? 664 VAL B N 1 ATOM 12240 C CA . VAL B 2 664 ? -14.962 12.916 77.490 1.00 89.91 ? 664 VAL B CA 1 ATOM 12241 C C . VAL B 2 664 ? -13.675 12.855 76.674 1.00 94.83 ? 664 VAL B C 1 ATOM 12242 O O . VAL B 2 664 ? -12.588 12.646 77.213 1.00 89.94 ? 664 VAL B O 1 ATOM 12243 C CB . VAL B 2 664 ? -14.823 14.003 78.566 1.00 91.46 ? 664 VAL B CB 1 ATOM 12244 C CG1 . VAL B 2 664 ? -14.468 15.333 77.924 1.00 94.72 ? 664 VAL B CG1 1 ATOM 12245 C CG2 . VAL B 2 664 ? -16.110 14.120 79.365 1.00 92.82 ? 664 VAL B CG2 1 ATOM 12246 N N . VAL B 2 665 ? -13.816 13.046 75.368 1.00 110.62 ? 665 VAL B N 1 ATOM 12247 C CA . VAL B 2 665 ? -12.683 13.054 74.454 1.00 89.23 ? 665 VAL B CA 1 ATOM 12248 C C . VAL B 2 665 ? -12.264 14.492 74.167 1.00 99.30 ? 665 VAL B C 1 ATOM 12249 O O . VAL B 2 665 ? -13.108 15.371 73.991 1.00 91.48 ? 665 VAL B O 1 ATOM 12250 C CB . VAL B 2 665 ? -13.025 12.331 73.136 1.00 88.19 ? 665 VAL B CB 1 ATOM 12251 C CG1 . VAL B 2 665 ? -11.836 12.328 72.192 1.00 88.32 ? 665 VAL B CG1 1 ATOM 12252 C CG2 . VAL B 2 665 ? -13.494 10.912 73.419 1.00 87.09 ? 665 VAL B CG2 1 ATOM 12253 N N . ARG B 2 666 ? -10.958 14.727 74.132 1.00 110.63 ? 666 ARG B N 1 ATOM 12254 C CA . ARG B 2 666 ? -10.418 16.063 73.916 1.00 100.53 ? 666 ARG B CA 1 ATOM 12255 C C . ARG B 2 666 ? -9.431 16.047 72.750 1.00 105.21 ? 666 ARG B C 1 ATOM 12256 O O . ARG B 2 666 ? -8.469 15.279 72.761 1.00 100.02 ? 666 ARG B O 1 ATOM 12257 C CB . ARG B 2 666 ? -9.743 16.565 75.195 1.00 94.27 ? 666 ARG B CB 1 ATOM 12258 C CG . ARG B 2 666 ? -9.449 18.052 75.229 1.00 139.48 ? 666 ARG B CG 1 ATOM 12259 C CD . ARG B 2 666 ? -8.852 18.445 76.574 1.00 135.22 ? 666 ARG B CD 1 ATOM 12260 N NE . ARG B 2 666 ? -9.695 18.019 77.689 1.00 135.21 ? 666 ARG B NE 1 ATOM 12261 C CZ . ARG B 2 666 ? -10.545 18.813 78.333 1.00 140.49 ? 666 ARG B CZ 1 ATOM 12262 N NH1 . ARG B 2 666 ? -10.664 20.086 77.980 1.00 126.71 ? 666 ARG B NH1 1 ATOM 12263 N NH2 . ARG B 2 666 ? -11.273 18.336 79.335 1.00 133.30 ? 666 ARG B NH2 1 ATOM 12264 N N . PHE B 2 667 ? -9.675 16.876 71.738 1.00 101.19 ? 667 PHE B N 1 ATOM 12265 C CA . PHE B 2 667 ? -8.780 16.930 70.583 1.00 94.43 ? 667 PHE B CA 1 ATOM 12266 C C . PHE B 2 667 ? -8.554 18.356 70.085 1.00 96.59 ? 667 PHE B C 1 ATOM 12267 O O . PHE B 2 667 ? -9.242 19.286 70.501 1.00 97.95 ? 667 PHE B O 1 ATOM 12268 C CB . PHE B 2 667 ? -9.309 16.046 69.444 1.00 93.02 ? 667 PHE B CB 1 ATOM 12269 C CG . PHE B 2 667 ? -10.589 16.536 68.822 1.00 93.23 ? 667 PHE B CG 1 ATOM 12270 C CD1 . PHE B 2 667 ? -10.564 17.386 67.727 1.00 109.34 ? 667 PHE B CD1 1 ATOM 12271 C CD2 . PHE B 2 667 ? -11.815 16.125 69.314 1.00 92.33 ? 667 PHE B CD2 1 ATOM 12272 C CE1 . PHE B 2 667 ? -11.738 17.831 67.148 1.00 100.04 ? 667 PHE B CE1 1 ATOM 12273 C CE2 . PHE B 2 667 ? -12.993 16.566 68.738 1.00 93.98 ? 667 PHE B CE2 1 ATOM 12274 C CZ . PHE B 2 667 ? -12.953 17.419 67.652 1.00 100.12 ? 667 PHE B CZ 1 ATOM 12275 N N . GLN B 2 668 ? -7.576 18.513 69.196 1.00 97.39 ? 668 GLN B N 1 ATOM 12276 C CA . GLN B 2 668 ? -7.195 19.822 68.674 1.00 99.78 ? 668 GLN B CA 1 ATOM 12277 C C . GLN B 2 668 ? -7.140 19.829 67.143 1.00 119.64 ? 668 GLN B C 1 ATOM 12278 O O . GLN B 2 668 ? -6.865 18.805 66.522 1.00 122.11 ? 668 GLN B O 1 ATOM 12279 C CB . GLN B 2 668 ? -5.839 20.236 69.250 1.00 101.30 ? 668 GLN B CB 1 ATOM 12280 C CG . GLN B 2 668 ? -5.460 21.690 69.025 1.00 104.87 ? 668 GLN B CG 1 ATOM 12281 C CD . GLN B 2 668 ? -4.031 21.986 69.443 1.00 120.33 ? 668 GLN B CD 1 ATOM 12282 O OE1 . GLN B 2 668 ? -3.179 21.097 69.460 1.00 120.22 ? 668 GLN B OE1 1 ATOM 12283 N NE2 . GLN B 2 668 ? -3.764 23.238 69.794 1.00 148.41 ? 668 GLN B NE2 1 ATOM 12284 N N . TYR B 2 669 ? -7.403 20.989 66.543 1.00 113.80 ? 669 TYR B N 1 ATOM 12285 C CA . TYR B 2 669 ? -7.338 21.152 65.091 1.00 117.05 ? 669 TYR B CA 1 ATOM 12286 C C . TYR B 2 669 ? -6.349 22.259 64.724 1.00 130.38 ? 669 TYR B C 1 ATOM 12287 O O . TYR B 2 669 ? -6.504 23.396 65.158 1.00 135.14 ? 669 TYR B O 1 ATOM 12288 C CB . TYR B 2 669 ? -8.728 21.462 64.528 1.00 131.64 ? 669 TYR B CB 1 ATOM 12289 C CG . TYR B 2 669 ? -8.738 21.870 63.071 1.00 158.44 ? 669 TYR B CG 1 ATOM 12290 C CD1 . TYR B 2 669 ? -8.717 20.917 62.061 1.00 164.23 ? 669 TYR B CD1 1 ATOM 12291 C CD2 . TYR B 2 669 ? -8.779 23.210 62.706 1.00 170.67 ? 669 TYR B CD2 1 ATOM 12292 C CE1 . TYR B 2 669 ? -8.728 21.287 60.727 1.00 168.72 ? 669 TYR B CE1 1 ATOM 12293 C CE2 . TYR B 2 669 ? -8.789 23.590 61.376 1.00 175.80 ? 669 TYR B CE2 1 ATOM 12294 C CZ . TYR B 2 669 ? -8.764 22.625 60.391 1.00 176.62 ? 669 TYR B CZ 1 ATOM 12295 O OH . TYR B 2 669 ? -8.776 23.002 59.067 1.00 177.63 ? 669 TYR B OH 1 ATOM 12296 N N . TYR B 2 670 ? -5.342 21.930 63.918 1.00 130.97 ? 670 TYR B N 1 ATOM 12297 C CA . TYR B 2 670 ? -4.247 22.863 63.643 1.00 131.15 ? 670 TYR B CA 1 ATOM 12298 C C . TYR B 2 670 ? -3.657 22.680 62.242 1.00 136.44 ? 670 TYR B C 1 ATOM 12299 O O . TYR B 2 670 ? -3.565 21.560 61.745 1.00 143.05 ? 670 TYR B O 1 ATOM 12300 C CB . TYR B 2 670 ? -3.164 22.695 64.715 1.00 136.33 ? 670 TYR B CB 1 ATOM 12301 C CG . TYR B 2 670 ? -1.795 23.236 64.364 1.00 155.62 ? 670 TYR B CG 1 ATOM 12302 C CD1 . TYR B 2 670 ? -1.599 24.587 64.114 1.00 166.08 ? 670 TYR B CD1 1 ATOM 12303 C CD2 . TYR B 2 670 ? -0.690 22.395 64.318 1.00 165.49 ? 670 TYR B CD2 1 ATOM 12304 C CE1 . TYR B 2 670 ? -0.345 25.083 63.807 1.00 173.80 ? 670 TYR B CE1 1 ATOM 12305 C CE2 . TYR B 2 670 ? 0.567 22.880 64.012 1.00 172.98 ? 670 TYR B CE2 1 ATOM 12306 C CZ . TYR B 2 670 ? 0.735 24.225 63.758 1.00 182.86 ? 670 TYR B CZ 1 ATOM 12307 O OH . TYR B 2 670 ? 1.985 24.713 63.453 1.00 192.13 ? 670 TYR B OH 1 ATOM 12308 N N . GLU B 2 671 ? -3.262 23.785 61.610 0.50 148.04 ? 671 GLU B N 1 ATOM 12309 C CA . GLU B 2 671 ? -2.685 23.740 60.266 1.00 159.57 ? 671 GLU B CA 1 ATOM 12310 C C . GLU B 2 671 ? -1.510 24.705 60.099 0.50 154.70 ? 671 GLU B C 1 ATOM 12311 O O . GLU B 2 671 ? -1.352 25.650 60.872 0.50 148.55 ? 671 GLU B O 1 ATOM 12312 C CB . GLU B 2 671 ? -3.754 24.052 59.214 1.00 159.00 ? 671 GLU B CB 1 ATOM 12313 C CG . GLU B 2 671 ? -4.030 25.536 59.018 1.00 156.60 ? 671 GLU B CG 1 ATOM 12314 C CD . GLU B 2 671 ? -4.702 26.175 60.217 1.00 161.09 ? 671 GLU B CD 1 ATOM 12315 O OE1 . GLU B 2 671 ? -4.621 27.415 60.355 1.00 162.01 ? 671 GLU B OE1 1 ATOM 12316 O OE2 . GLU B 2 671 ? -5.317 25.440 61.018 1.00 154.49 ? 671 GLU B OE2 1 ATOM 12317 N N . ASP B 2 672 ? -0.691 24.459 59.080 0.50 157.72 ? 672 ASP B N 1 ATOM 12318 C CA . ASP B 2 672 ? 0.447 25.321 58.768 0.50 164.87 ? 672 ASP B CA 1 ATOM 12319 C C . ASP B 2 672 ? 0.275 26.011 57.420 0.50 173.40 ? 672 ASP B C 1 ATOM 12320 O O . ASP B 2 672 ? 0.312 25.357 56.379 0.50 171.77 ? 672 ASP B O 1 ATOM 12321 C CB . ASP B 2 672 ? 1.749 24.518 58.771 1.00 165.16 ? 672 ASP B CB 1 ATOM 12322 C CG . ASP B 2 672 ? 2.226 24.191 60.168 1.00 171.21 ? 672 ASP B CG 1 ATOM 12323 O OD1 . ASP B 2 672 ? 1.918 24.969 61.094 1.00 175.10 ? 672 ASP B OD1 1 ATOM 12324 O OD2 . ASP B 2 672 ? 2.912 23.161 60.340 1.00 169.71 ? 672 ASP B OD2 1 ATOM 12325 N N . SER B 2 673 ? 0.104 27.331 57.453 1.00 185.66 ? 673 SER B N 1 ATOM 12326 C CA . SER B 2 673 ? -0.094 28.135 56.248 1.00 192.18 ? 673 SER B CA 1 ATOM 12327 C C . SER B 2 673 ? -1.240 27.592 55.400 1.00 195.15 ? 673 SER B C 1 ATOM 12328 O O . SER B 2 673 ? -2.323 27.307 55.912 1.00 190.27 ? 673 SER B O 1 ATOM 12329 C CB . SER B 2 673 ? 1.193 28.193 55.418 1.00 192.83 ? 673 SER B CB 1 ATOM 12330 O OG . SER B 2 673 ? 2.255 28.771 56.157 1.00 191.72 ? 673 SER B OG 1 ATOM 12331 N N . SER B 2 674 ? -0.992 27.448 54.102 1.00 201.57 ? 674 SER B N 1 ATOM 12332 C CA . SER B 2 674 ? -1.963 26.846 53.196 1.00 197.17 ? 674 SER B CA 1 ATOM 12333 C C . SER B 2 674 ? -1.790 25.331 53.173 1.00 192.33 ? 674 SER B C 1 ATOM 12334 O O . SER B 2 674 ? -2.487 24.626 52.445 1.00 195.50 ? 674 SER B O 1 ATOM 12335 C CB . SER B 2 674 ? -1.820 27.421 51.784 1.00 196.05 ? 674 SER B CB 1 ATOM 12336 O OG . SER B 2 674 ? -0.545 27.132 51.237 1.00 195.10 ? 674 SER B OG 1 ATOM 12337 N N . GLY B 2 675 ? -0.853 24.840 53.978 1.00 183.28 ? 675 GLY B N 1 ATOM 12338 C CA . GLY B 2 675 ? -0.549 23.423 54.028 1.00 172.13 ? 675 GLY B CA 1 ATOM 12339 C C . GLY B 2 675 ? -1.589 22.602 54.767 1.00 169.77 ? 675 GLY B C 1 ATOM 12340 O O . GLY B 2 675 ? -2.696 23.067 55.036 1.00 170.17 ? 675 GLY B O 1 ATOM 12341 N N . LYS B 2 676 ? -1.216 21.371 55.099 1.00 167.78 ? 676 LYS B N 1 ATOM 12342 C CA . LYS B 2 676 ? -2.130 20.400 55.692 1.00 163.09 ? 676 LYS B CA 1 ATOM 12343 C C . LYS B 2 676 ? -2.605 20.775 57.095 1.00 153.84 ? 676 LYS B C 1 ATOM 12344 O O . LYS B 2 676 ? -1.941 21.525 57.812 1.00 149.37 ? 676 LYS B O 1 ATOM 12345 C CB . LYS B 2 676 ? -1.458 19.026 55.726 1.00 164.92 ? 676 LYS B CB 1 ATOM 12346 C CG . LYS B 2 676 ? -0.021 19.064 56.224 1.00 164.58 ? 676 LYS B CG 1 ATOM 12347 C CD . LYS B 2 676 ? 0.700 17.757 55.945 1.00 162.06 ? 676 LYS B CD 1 ATOM 12348 C CE . LYS B 2 676 ? 2.178 17.861 56.287 1.00 165.81 ? 676 LYS B CE 1 ATOM 12349 N NZ . LYS B 2 676 ? 2.917 16.614 55.945 1.00 166.61 ? 676 LYS B NZ 1 ATOM 12350 N N . SER B 2 677 ? -3.763 20.240 57.473 1.00 147.63 ? 677 SER B N 1 ATOM 12351 C CA . SER B 2 677 ? -4.309 20.425 58.813 1.00 149.42 ? 677 SER B CA 1 ATOM 12352 C C . SER B 2 677 ? -4.280 19.106 59.585 1.00 149.25 ? 677 SER B C 1 ATOM 12353 O O . SER B 2 677 ? -4.630 18.055 59.048 1.00 145.19 ? 677 SER B O 1 ATOM 12354 C CB . SER B 2 677 ? -5.736 20.972 58.747 1.00 147.61 ? 677 SER B CB 1 ATOM 12355 O OG . SER B 2 677 ? -6.598 20.073 58.070 1.00 148.50 ? 677 SER B OG 1 ATOM 12356 N N . ILE B 2 678 ? -3.867 19.169 60.847 1.00 139.64 ? 678 ILE B N 1 ATOM 12357 C CA . ILE B 2 678 ? -3.672 17.964 61.648 1.00 121.94 ? 678 ILE B CA 1 ATOM 12358 C C . ILE B 2 678 ? -4.555 17.945 62.898 1.00 115.89 ? 678 ILE B C 1 ATOM 12359 O O . ILE B 2 678 ? -4.770 18.975 63.538 1.00 118.69 ? 678 ILE B O 1 ATOM 12360 C CB . ILE B 2 678 ? -2.184 17.816 62.061 1.00 108.06 ? 678 ILE B CB 1 ATOM 12361 C CG1 . ILE B 2 678 ? -1.980 16.598 62.967 1.00 110.07 ? 678 ILE B CG1 1 ATOM 12362 C CG2 . ILE B 2 678 ? -1.683 19.081 62.738 1.00 107.66 ? 678 ILE B CG2 1 ATOM 12363 C CD1 . ILE B 2 678 ? -0.532 16.313 63.297 1.00 119.11 ? 678 ILE B CD1 1 ATOM 12364 N N . LEU B 2 679 ? -5.078 16.767 63.227 1.00 108.09 ? 679 LEU B N 1 ATOM 12365 C CA . LEU B 2 679 ? -5.853 16.579 64.447 1.00 98.68 ? 679 LEU B CA 1 ATOM 12366 C C . LEU B 2 679 ? -5.035 15.873 65.522 1.00 99.59 ? 679 LEU B C 1 ATOM 12367 O O . LEU B 2 679 ? -4.615 14.730 65.344 1.00 101.64 ? 679 LEU B O 1 ATOM 12368 C CB . LEU B 2 679 ? -7.122 15.774 64.163 1.00 94.84 ? 679 LEU B CB 1 ATOM 12369 C CG . LEU B 2 679 ? -8.157 16.377 63.216 1.00 109.11 ? 679 LEU B CG 1 ATOM 12370 C CD1 . LEU B 2 679 ? -9.338 15.431 63.067 1.00 93.70 ? 679 LEU B CD1 1 ATOM 12371 C CD2 . LEU B 2 679 ? -8.612 17.741 63.715 1.00 130.88 ? 679 LEU B CD2 1 ATOM 12372 N N . TYR B 2 680 ? -4.807 16.554 66.638 1.00 97.83 ? 680 TYR B N 1 ATOM 12373 C CA . TYR B 2 680 ? -4.180 15.916 67.787 1.00 96.63 ? 680 TYR B CA 1 ATOM 12374 C C . TYR B 2 680 ? -5.252 15.430 68.754 1.00 95.82 ? 680 TYR B C 1 ATOM 12375 O O . TYR B 2 680 ? -5.957 16.235 69.358 1.00 103.98 ? 680 TYR B O 1 ATOM 12376 C CB . TYR B 2 680 ? -3.227 16.878 68.498 1.00 106.50 ? 680 TYR B CB 1 ATOM 12377 C CG . TYR B 2 680 ? -2.045 17.325 67.668 1.00 113.86 ? 680 TYR B CG 1 ATOM 12378 C CD1 . TYR B 2 680 ? -0.888 16.561 67.605 1.00 112.77 ? 680 TYR B CD1 1 ATOM 12379 C CD2 . TYR B 2 680 ? -2.080 18.519 66.962 1.00 125.29 ? 680 TYR B CD2 1 ATOM 12380 C CE1 . TYR B 2 680 ? 0.198 16.970 66.854 1.00 119.58 ? 680 TYR B CE1 1 ATOM 12381 C CE2 . TYR B 2 680 ? -1.000 18.936 66.209 1.00 128.40 ? 680 TYR B CE2 1 ATOM 12382 C CZ . TYR B 2 680 ? 0.136 18.158 66.158 1.00 134.89 ? 680 TYR B CZ 1 ATOM 12383 O OH . TYR B 2 680 ? 1.214 18.569 65.408 1.00 158.75 ? 680 TYR B OH 1 ATOM 12384 N N . VAL B 2 681 ? -5.378 14.115 68.897 1.00 105.61 ? 681 VAL B N 1 ATOM 12385 C CA . VAL B 2 681 ? -6.346 13.542 69.826 1.00 107.10 ? 681 VAL B CA 1 ATOM 12386 C C . VAL B 2 681 ? -5.659 13.132 71.120 1.00 96.92 ? 681 VAL B C 1 ATOM 12387 O O . VAL B 2 681 ? -4.616 12.482 71.094 1.00 96.17 ? 681 VAL B O 1 ATOM 12388 C CB . VAL B 2 681 ? -7.065 12.319 69.220 1.00 90.63 ? 681 VAL B CB 1 ATOM 12389 C CG1 . VAL B 2 681 ? -7.924 11.627 70.267 1.00 89.57 ? 681 VAL B CG1 1 ATOM 12390 C CG2 . VAL B 2 681 ? -7.910 12.739 68.030 1.00 90.37 ? 681 VAL B CG2 1 ATOM 12391 N N . VAL B 2 682 ? -6.242 13.511 72.252 1.00 95.77 ? 682 VAL B N 1 ATOM 12392 C CA . VAL B 2 682 ? -5.665 13.151 73.538 1.00 95.85 ? 682 VAL B CA 1 ATOM 12393 C C . VAL B 2 682 ? -5.990 11.704 73.868 1.00 92.07 ? 682 VAL B C 1 ATOM 12394 O O . VAL B 2 682 ? -7.157 11.334 73.987 1.00 96.37 ? 682 VAL B O 1 ATOM 12395 C CB . VAL B 2 682 ? -6.181 14.057 74.669 1.00 93.88 ? 682 VAL B CB 1 ATOM 12396 C CG1 . VAL B 2 682 ? -5.726 13.531 76.020 1.00 94.43 ? 682 VAL B CG1 1 ATOM 12397 C CG2 . VAL B 2 682 ? -5.709 15.486 74.460 1.00 95.58 ? 682 VAL B CG2 1 ATOM 12398 N N . GLU B 2 683 ? -4.951 10.890 74.018 1.00 102.73 ? 683 GLU B N 1 ATOM 12399 C CA . GLU B 2 683 ? -5.130 9.487 74.361 1.00 92.22 ? 683 GLU B CA 1 ATOM 12400 C C . GLU B 2 683 ? -5.562 9.372 75.811 1.00 104.82 ? 683 GLU B C 1 ATOM 12401 O O . GLU B 2 683 ? -5.337 10.287 76.605 1.00 114.24 ? 683 GLU B O 1 ATOM 12402 C CB . GLU B 2 683 ? -3.846 8.693 74.129 1.00 93.49 ? 683 GLU B CB 1 ATOM 12403 C CG . GLU B 2 683 ? -2.747 8.995 75.133 1.00 95.48 ? 683 GLU B CG 1 ATOM 12404 C CD . GLU B 2 683 ? -1.653 7.940 75.146 1.00 120.98 ? 683 GLU B CD 1 ATOM 12405 O OE1 . GLU B 2 683 ? -1.581 7.125 74.198 1.00 96.70 ? 683 GLU B OE1 1 ATOM 12406 O OE2 . GLU B 2 683 ? -0.864 7.926 76.113 1.00 118.74 ? 683 GLU B OE2 1 ATOM 12407 N N . GLU B 2 684 ? -6.175 8.243 76.149 1.00 102.78 ? 684 GLU B N 1 ATOM 12408 C CA . GLU B 2 684 ? -6.705 8.009 77.490 1.00 121.73 ? 684 GLU B CA 1 ATOM 12409 C C . GLU B 2 684 ? -7.626 9.143 77.954 1.00 117.21 ? 684 GLU B C 1 ATOM 12410 O O . GLU B 2 684 ? -7.241 9.959 78.793 1.00 98.97 ? 684 GLU B O 1 ATOM 12411 C CB . GLU B 2 684 ? -5.563 7.808 78.490 1.00 111.46 ? 684 GLU B CB 1 ATOM 12412 C CG . GLU B 2 684 ? -5.819 6.704 79.504 1.00 115.90 ? 684 GLU B CG 1 ATOM 12413 C CD . GLU B 2 684 ? -4.651 6.493 80.447 1.00 153.93 ? 684 GLU B CD 1 ATOM 12414 O OE1 . GLU B 2 684 ? -3.824 7.419 80.589 1.00 160.09 ? 684 GLU B OE1 1 ATOM 12415 O OE2 . GLU B 2 684 ? -4.557 5.399 81.044 1.00 171.31 ? 684 GLU B OE2 1 ATOM 12416 N N . PRO B 2 685 ? -8.844 9.202 77.392 1.00 90.15 ? 685 PRO B N 1 ATOM 12417 C CA . PRO B 2 685 ? -9.867 10.179 77.774 1.00 89.98 ? 685 PRO B CA 1 ATOM 12418 C C . PRO B 2 685 ? -10.296 10.053 79.230 1.00 90.56 ? 685 PRO B C 1 ATOM 12419 O O . PRO B 2 685 ? -9.783 9.212 79.965 1.00 127.06 ? 685 PRO B O 1 ATOM 12420 C CB . PRO B 2 685 ? -11.038 9.835 76.849 1.00 88.65 ? 685 PRO B CB 1 ATOM 12421 C CG . PRO B 2 685 ? -10.421 9.150 75.694 1.00 88.18 ? 685 PRO B CG 1 ATOM 12422 C CD . PRO B 2 685 ? -9.287 8.370 76.263 1.00 88.99 ? 685 PRO B CD 1 ATOM 12423 N N . GLU B 2 686 ? -11.243 10.888 79.636 1.00 101.34 ? 686 GLU B N 1 ATOM 12424 C CA . GLU B 2 686 ? -11.746 10.865 81.003 1.00 104.89 ? 686 GLU B CA 1 ATOM 12425 C C . GLU B 2 686 ? -13.075 10.120 81.073 1.00 90.53 ? 686 GLU B C 1 ATOM 12426 O O . GLU B 2 686 ? -14.058 10.521 80.452 1.00 91.75 ? 686 GLU B O 1 ATOM 12427 C CB . GLU B 2 686 ? -11.893 12.291 81.543 1.00 98.14 ? 686 GLU B CB 1 ATOM 12428 C CG . GLU B 2 686 ? -10.564 13.029 81.675 1.00 115.30 ? 686 GLU B CG 1 ATOM 12429 C CD . GLU B 2 686 ? -10.727 14.493 82.042 1.00 146.68 ? 686 GLU B CD 1 ATOM 12430 O OE1 . GLU B 2 686 ? -11.820 15.053 81.811 1.00 148.51 ? 686 GLU B OE1 1 ATOM 12431 O OE2 . GLU B 2 686 ? -9.758 15.086 82.562 1.00 155.27 ? 686 GLU B OE2 1 ATOM 12432 N N . CYS B 2 687 ? -13.088 9.028 81.831 1.00 91.47 ? 687 CYS B N 1 ATOM 12433 C CA . CYS B 2 687 ? -14.267 8.181 81.954 1.00 92.64 ? 687 CYS B CA 1 ATOM 12434 C C . CYS B 2 687 ? -14.754 8.128 83.403 1.00 96.21 ? 687 CYS B C 1 ATOM 12435 O O . CYS B 2 687 ? -13.978 8.381 84.323 1.00 99.80 ? 687 CYS B O 1 ATOM 12436 C CB . CYS B 2 687 ? -13.953 6.774 81.439 1.00 91.42 ? 687 CYS B CB 1 ATOM 12437 S SG . CYS B 2 687 ? -13.505 6.709 79.690 1.00 129.71 ? 687 CYS B SG 1 ATOM 12438 N N . PRO B 2 688 ? -16.046 7.815 83.610 1.00 104.54 ? 688 PRO B N 1 ATOM 12439 C CA . PRO B 2 688 ? -16.583 7.689 84.971 1.00 112.86 ? 688 PRO B CA 1 ATOM 12440 C C . PRO B 2 688 ? -15.850 6.632 85.793 1.00 123.44 ? 688 PRO B C 1 ATOM 12441 O O . PRO B 2 688 ? -15.647 5.514 85.320 1.00 137.02 ? 688 PRO B O 1 ATOM 12442 C CB . PRO B 2 688 ? -18.044 7.283 84.738 1.00 126.74 ? 688 PRO B CB 1 ATOM 12443 C CG . PRO B 2 688 ? -18.086 6.760 83.333 1.00 121.45 ? 688 PRO B CG 1 ATOM 12444 C CD . PRO B 2 688 ? -17.086 7.586 82.594 1.00 108.57 ? 688 PRO B CD 1 ATOM 12445 N N . LYS B 2 689 ? -15.462 6.991 87.013 1.00 121.72 ? 689 LYS B N 1 ATOM 12446 C CA . LYS B 2 689 ? -14.664 6.112 87.861 1.00 125.76 ? 689 LYS B CA 1 ATOM 12447 C C . LYS B 2 689 ? -15.505 4.974 88.436 1.00 134.35 ? 689 LYS B C 1 ATOM 12448 O O . LYS B 2 689 ? -16.712 5.120 88.634 1.00 125.68 ? 689 LYS B O 1 ATOM 12449 C CB . LYS B 2 689 ? -14.013 6.919 88.988 1.00 131.39 ? 689 LYS B CB 1 ATOM 12450 C CG . LYS B 2 689 ? -12.734 6.312 89.546 1.00 143.66 ? 689 LYS B CG 1 ATOM 12451 C CD . LYS B 2 689 ? -12.016 7.299 90.459 1.00 147.53 ? 689 LYS B CD 1 ATOM 12452 C CE . LYS B 2 689 ? -10.668 6.761 90.919 1.00 150.04 ? 689 LYS B CE 1 ATOM 12453 N NZ . LYS B 2 689 ? -9.926 7.754 91.748 1.00 134.34 ? 689 LYS B NZ 1 ATOM 12454 N N . GLY B 2 690 ? -14.859 3.842 88.698 1.00 142.74 ? 690 GLY B N 1 ATOM 12455 C CA . GLY B 2 690 ? -15.543 2.669 89.211 1.00 126.42 ? 690 GLY B CA 1 ATOM 12456 C C . GLY B 2 690 ? -15.874 2.773 90.687 1.00 126.61 ? 690 GLY B C 1 ATOM 12457 O O . GLY B 2 690 ? -16.686 2.006 91.205 1.00 128.13 ? 690 GLY B O 1 ATOM 12458 N N . SER C 3 1 ? 23.401 53.130 56.628 1.00 192.18 ? 1417 SER C N 1 ATOM 12459 C CA . SER C 3 1 ? 22.263 52.614 55.876 1.00 200.88 ? 1417 SER C CA 1 ATOM 12460 C C . SER C 3 1 ? 22.694 51.569 54.852 1.00 207.56 ? 1417 SER C C 1 ATOM 12461 O O . SER C 3 1 ? 22.435 50.378 55.019 1.00 198.63 ? 1417 SER C O 1 ATOM 12462 C CB . SER C 3 1 ? 21.521 53.756 55.178 1.00 193.79 ? 1417 SER C CB 1 ATOM 12463 O OG . SER C 3 1 ? 20.427 53.267 54.421 1.00 185.73 ? 1417 SER C OG 1 ATOM 12464 N N . ASP C 3 2 ? 23.364 52.025 53.799 1.00 217.71 ? 1418 ASP C N 1 ATOM 12465 C CA . ASP C 3 2 ? 23.782 51.154 52.705 1.00 216.15 ? 1418 ASP C CA 1 ATOM 12466 C C . ASP C 3 2 ? 24.935 50.226 53.087 1.00 223.91 ? 1418 ASP C C 1 ATOM 12467 O O . ASP C 3 2 ? 25.327 49.360 52.305 1.00 218.97 ? 1418 ASP C O 1 ATOM 12468 C CB . ASP C 3 2 ? 24.177 51.994 51.485 1.00 212.57 ? 1418 ASP C CB 1 ATOM 12469 C CG . ASP C 3 2 ? 25.072 53.171 51.845 1.00 212.82 ? 1418 ASP C CG 1 ATOM 12470 O OD1 . ASP C 3 2 ? 25.744 53.119 52.896 1.00 219.79 ? 1418 ASP C OD1 1 ATOM 12471 O OD2 . ASP C 3 2 ? 25.104 54.152 51.071 1.00 207.90 ? 1418 ASP C OD2 1 ATOM 12472 N N . VAL C 3 3 ? 25.472 50.406 54.290 1.00 236.82 ? 1419 VAL C N 1 ATOM 12473 C CA . VAL C 3 3 ? 26.671 49.688 54.705 1.00 243.17 ? 1419 VAL C CA 1 ATOM 12474 C C . VAL C 3 3 ? 26.518 49.067 56.099 1.00 236.78 ? 1419 VAL C C 1 ATOM 12475 O O . VAL C 3 3 ? 25.918 49.670 56.989 1.00 243.76 ? 1419 VAL C O 1 ATOM 12476 C CB . VAL C 3 3 ? 27.898 50.643 54.678 1.00 257.18 ? 1419 VAL C CB 1 ATOM 12477 C CG1 . VAL C 3 3 ? 27.644 51.875 55.540 1.00 258.82 ? 1419 VAL C CG1 1 ATOM 12478 C CG2 . VAL C 3 3 ? 29.171 49.934 55.107 1.00 259.11 ? 1419 VAL C CG2 1 ATOM 12479 N N . PRO C 3 4 ? 27.044 47.843 56.284 1.00 223.48 ? 1420 PRO C N 1 ATOM 12480 C CA . PRO C 3 4 ? 27.124 47.217 57.610 1.00 220.27 ? 1420 PRO C CA 1 ATOM 12481 C C . PRO C 3 4 ? 28.141 47.919 58.507 1.00 225.38 ? 1420 PRO C C 1 ATOM 12482 O O . PRO C 3 4 ? 29.080 48.530 57.997 1.00 227.84 ? 1420 PRO C O 1 ATOM 12483 C CB . PRO C 3 4 ? 27.563 45.782 57.297 1.00 219.19 ? 1420 PRO C CB 1 ATOM 12484 C CG . PRO C 3 4 ? 28.205 45.862 55.952 1.00 215.28 ? 1420 PRO C CG 1 ATOM 12485 C CD . PRO C 3 4 ? 27.435 46.910 55.214 1.00 215.45 ? 1420 PRO C CD 1 ATOM 12486 N N . ARG C 3 5 ? 27.963 47.830 59.822 1.00 227.78 ? 1421 ARG C N 1 ATOM 12487 C CA . ARG C 3 5 ? 28.789 48.607 60.742 1.00 224.22 ? 1421 ARG C CA 1 ATOM 12488 C C . ARG C 3 5 ? 29.489 47.767 61.808 1.00 233.70 ? 1421 ARG C C 1 ATOM 12489 O O . ARG C 3 5 ? 28.927 46.799 62.322 1.00 228.77 ? 1421 ARG C O 1 ATOM 12490 C CB . ARG C 3 5 ? 27.940 49.680 61.427 1.00 215.04 ? 1421 ARG C CB 1 ATOM 12491 C CG . ARG C 3 5 ? 27.093 50.516 60.481 1.00 209.98 ? 1421 ARG C CG 1 ATOM 12492 C CD . ARG C 3 5 ? 26.346 51.617 61.220 1.00 210.50 ? 1421 ARG C CD 1 ATOM 12493 N NE . ARG C 3 5 ? 25.548 51.104 62.331 1.00 213.99 ? 1421 ARG C NE 1 ATOM 12494 C CZ . ARG C 3 5 ? 25.891 51.213 63.611 1.00 217.58 ? 1421 ARG C CZ 1 ATOM 12495 N NH1 . ARG C 3 5 ? 27.022 51.818 63.947 1.00 212.78 ? 1421 ARG C NH1 1 ATOM 12496 N NH2 . ARG C 3 5 ? 25.104 50.716 64.555 1.00 217.78 ? 1421 ARG C NH2 1 ATOM 12497 N N . ASP C 3 6 ? 30.721 48.167 62.123 1.00 181.22 ? 1422 ASP C N 1 ATOM 12498 C CA . ASP C 3 6 ? 31.528 47.637 63.231 1.00 195.12 ? 1422 ASP C CA 1 ATOM 12499 C C . ASP C 3 6 ? 31.458 46.122 63.435 1.00 193.13 ? 1422 ASP C C 1 ATOM 12500 O O . ASP C 3 6 ? 30.940 45.646 64.445 1.00 200.36 ? 1422 ASP C O 1 ATOM 12501 C CB . ASP C 3 6 ? 31.165 48.348 64.551 1.00 210.23 ? 1422 ASP C CB 1 ATOM 12502 C CG . ASP C 3 6 ? 29.671 48.353 64.840 1.00 209.05 ? 1422 ASP C CG 1 ATOM 12503 O OD1 . ASP C 3 6 ? 29.178 47.407 65.491 1.00 211.80 ? 1422 ASP C OD1 1 ATOM 12504 O OD2 . ASP C 3 6 ? 28.990 49.315 64.429 1.00 203.74 ? 1422 ASP C OD2 1 ATOM 12505 N N . LEU C 3 7 ? 31.993 45.363 62.484 1.00 175.24 ? 1423 LEU C N 1 ATOM 12506 C CA . LEU C 3 7 ? 32.088 43.922 62.670 1.00 170.84 ? 1423 LEU C CA 1 ATOM 12507 C C . LEU C 3 7 ? 33.198 43.631 63.681 1.00 170.57 ? 1423 LEU C C 1 ATOM 12508 O O . LEU C 3 7 ? 34.318 44.128 63.557 1.00 163.05 ? 1423 LEU C O 1 ATOM 12509 C CB . LEU C 3 7 ? 32.332 43.199 61.338 1.00 163.04 ? 1423 LEU C CB 1 ATOM 12510 C CG . LEU C 3 7 ? 33.736 43.033 60.748 1.00 160.73 ? 1423 LEU C CG 1 ATOM 12511 C CD1 . LEU C 3 7 ? 33.690 42.153 59.507 1.00 142.39 ? 1423 LEU C CD1 1 ATOM 12512 C CD2 . LEU C 3 7 ? 34.380 44.374 60.431 1.00 161.37 ? 1423 LEU C CD2 1 ATOM 12513 N N . GLU C 3 8 ? 32.872 42.858 64.709 1.00 169.05 ? 1424 GLU C N 1 ATOM 12514 C CA . GLU C 3 8 ? 33.832 42.578 65.768 1.00 189.06 ? 1424 GLU C CA 1 ATOM 12515 C C . GLU C 3 8 ? 33.801 41.112 66.181 1.00 193.45 ? 1424 GLU C C 1 ATOM 12516 O O . GLU C 3 8 ? 32.731 40.524 66.339 1.00 186.19 ? 1424 GLU C O 1 ATOM 12517 C CB . GLU C 3 8 ? 33.566 43.473 66.985 1.00 203.41 ? 1424 GLU C CB 1 ATOM 12518 C CG . GLU C 3 8 ? 33.736 44.964 66.717 1.00 198.99 ? 1424 GLU C CG 1 ATOM 12519 C CD . GLU C 3 8 ? 33.553 45.812 67.962 1.00 209.55 ? 1424 GLU C CD 1 ATOM 12520 O OE1 . GLU C 3 8 ? 33.706 45.277 69.081 1.00 213.79 ? 1424 GLU C OE1 1 ATOM 12521 O OE2 . GLU C 3 8 ? 33.252 47.016 67.819 1.00 209.01 ? 1424 GLU C OE2 1 ATOM 12522 N N . VAL C 3 9 ? 34.985 40.529 66.344 1.00 203.01 ? 1425 VAL C N 1 ATOM 12523 C CA . VAL C 3 9 ? 35.113 39.154 66.809 1.00 200.58 ? 1425 VAL C CA 1 ATOM 12524 C C . VAL C 3 9 ? 34.516 39.020 68.205 1.00 213.16 ? 1425 VAL C C 1 ATOM 12525 O O . VAL C 3 9 ? 34.809 39.822 69.092 1.00 228.91 ? 1425 VAL C O 1 ATOM 12526 C CB . VAL C 3 9 ? 36.586 38.700 66.832 1.00 208.73 ? 1425 VAL C CB 1 ATOM 12527 C CG1 . VAL C 3 9 ? 36.685 37.229 67.207 1.00 215.91 ? 1425 VAL C CG1 1 ATOM 12528 C CG2 . VAL C 3 9 ? 37.242 38.955 65.484 1.00 194.07 ? 1425 VAL C CG2 1 ATOM 12529 N N . VAL C 3 10 ? 33.673 38.011 68.394 1.00 202.33 ? 1426 VAL C N 1 ATOM 12530 C CA . VAL C 3 10 ? 32.981 37.830 69.665 1.00 211.32 ? 1426 VAL C CA 1 ATOM 12531 C C . VAL C 3 10 ? 33.642 36.763 70.533 1.00 226.35 ? 1426 VAL C C 1 ATOM 12532 O O . VAL C 3 10 ? 34.166 37.062 71.605 1.00 237.25 ? 1426 VAL C O 1 ATOM 12533 C CB . VAL C 3 10 ? 31.504 37.455 69.450 1.00 203.18 ? 1426 VAL C CB 1 ATOM 12534 C CG1 . VAL C 3 10 ? 30.802 37.280 70.788 1.00 218.73 ? 1426 VAL C CG1 1 ATOM 12535 C CG2 . VAL C 3 10 ? 30.806 38.513 68.612 1.00 188.95 ? 1426 VAL C CG2 1 ATOM 12536 N N . ALA C 3 11 ? 33.613 35.520 70.064 1.00 223.65 ? 1427 ALA C N 1 ATOM 12537 C CA . ALA C 3 11 ? 34.118 34.398 70.848 1.00 237.34 ? 1427 ALA C CA 1 ATOM 12538 C C . ALA C 3 11 ? 35.593 34.116 70.580 1.00 250.50 ? 1427 ALA C C 1 ATOM 12539 O O . ALA C 3 11 ? 35.978 33.790 69.456 1.00 240.09 ? 1427 ALA C O 1 ATOM 12540 C CB . ALA C 3 11 ? 33.289 33.153 70.570 1.00 225.45 ? 1427 ALA C CB 1 ATOM 12541 N N . ALA C 3 12 ? 36.414 34.238 71.620 1.00 268.74 ? 1428 ALA C N 1 ATOM 12542 C CA . ALA C 3 12 ? 37.813 33.840 71.530 1.00 275.62 ? 1428 ALA C CA 1 ATOM 12543 C C . ALA C 3 12 ? 37.878 32.326 71.661 1.00 282.25 ? 1428 ALA C C 1 ATOM 12544 O O . ALA C 3 12 ? 37.495 31.767 72.689 1.00 292.85 ? 1428 ALA C O 1 ATOM 12545 C CB . ALA C 3 12 ? 38.645 34.517 72.606 1.00 281.81 ? 1428 ALA C CB 1 ATOM 12546 N N . THR C 3 13 ? 38.381 31.670 70.621 1.00 275.27 ? 1429 THR C N 1 ATOM 12547 C CA . THR C 3 13 ? 38.183 30.237 70.437 1.00 268.45 ? 1429 THR C CA 1 ATOM 12548 C C . THR C 3 13 ? 38.939 29.792 69.185 1.00 253.49 ? 1429 THR C C 1 ATOM 12549 O O . THR C 3 13 ? 39.150 30.591 68.272 1.00 237.15 ? 1429 THR C O 1 ATOM 12550 C CB . THR C 3 13 ? 36.652 29.895 70.307 1.00 246.94 ? 1429 THR C CB 1 ATOM 12551 O OG1 . THR C 3 13 ? 35.972 30.215 71.528 1.00 253.50 ? 1429 THR C OG1 1 ATOM 12552 C CG2 . THR C 3 13 ? 36.394 28.426 69.988 1.00 244.25 ? 1429 THR C CG2 1 ATOM 12553 N N . PRO C 3 14 ? 39.355 28.516 69.139 1.00 259.03 ? 1430 PRO C N 1 ATOM 12554 C CA . PRO C 3 14 ? 39.787 27.868 67.896 1.00 259.56 ? 1430 PRO C CA 1 ATOM 12555 C C . PRO C 3 14 ? 38.668 27.861 66.855 1.00 264.63 ? 1430 PRO C C 1 ATOM 12556 O O . PRO C 3 14 ? 37.652 28.528 67.046 1.00 264.22 ? 1430 PRO C O 1 ATOM 12557 C CB . PRO C 3 14 ? 40.144 26.440 68.339 1.00 263.90 ? 1430 PRO C CB 1 ATOM 12558 C CG . PRO C 3 14 ? 39.655 26.317 69.760 1.00 269.97 ? 1430 PRO C CG 1 ATOM 12559 C CD . PRO C 3 14 ? 39.703 27.699 70.312 1.00 269.08 ? 1430 PRO C CD 1 ATOM 12560 N N . THR C 3 15 ? 38.855 27.130 65.761 1.00 272.58 ? 1431 THR C N 1 ATOM 12561 C CA . THR C 3 15 ? 37.950 27.219 64.619 1.00 267.33 ? 1431 THR C CA 1 ATOM 12562 C C . THR C 3 15 ? 36.518 26.888 65.033 1.00 269.39 ? 1431 THR C C 1 ATOM 12563 O O . THR C 3 15 ? 36.302 26.250 66.065 1.00 282.37 ? 1431 THR C O 1 ATOM 12564 C CB . THR C 3 15 ? 38.382 26.281 63.482 1.00 265.06 ? 1431 THR C CB 1 ATOM 12565 O OG1 . THR C 3 15 ? 37.553 26.503 62.334 1.00 250.62 ? 1431 THR C OG1 1 ATOM 12566 C CG2 . THR C 3 15 ? 38.273 24.826 63.915 1.00 273.17 ? 1431 THR C CG2 1 ATOM 12567 N N . SER C 3 16 ? 35.566 27.322 64.205 1.00 192.15 ? 1432 SER C N 1 ATOM 12568 C CA . SER C 3 16 ? 34.190 27.649 64.602 1.00 179.22 ? 1432 SER C CA 1 ATOM 12569 C C . SER C 3 16 ? 34.191 28.931 65.431 1.00 171.17 ? 1432 SER C C 1 ATOM 12570 O O . SER C 3 16 ? 33.460 29.061 66.413 1.00 170.14 ? 1432 SER C O 1 ATOM 12571 C CB . SER C 3 16 ? 33.519 26.507 65.375 1.00 183.64 ? 1432 SER C CB 1 ATOM 12572 O OG . SER C 3 16 ? 33.521 25.308 64.620 1.00 183.14 ? 1432 SER C OG 1 ATOM 12573 N N . LEU C 3 17 ? 35.033 29.873 65.013 1.00 168.35 ? 1433 LEU C N 1 ATOM 12574 C CA . LEU C 3 17 ? 35.052 31.223 65.564 1.00 168.55 ? 1433 LEU C CA 1 ATOM 12575 C C . LEU C 3 17 ? 33.806 31.997 65.135 1.00 159.98 ? 1433 LEU C C 1 ATOM 12576 O O . LEU C 3 17 ? 33.169 31.651 64.141 1.00 150.33 ? 1433 LEU C O 1 ATOM 12577 C CB . LEU C 3 17 ? 36.319 31.959 65.119 1.00 169.48 ? 1433 LEU C CB 1 ATOM 12578 C CG . LEU C 3 17 ? 36.564 32.049 63.608 1.00 155.04 ? 1433 LEU C CG 1 ATOM 12579 C CD1 . LEU C 3 17 ? 36.078 33.377 63.044 1.00 140.73 ? 1433 LEU C CD1 1 ATOM 12580 C CD2 . LEU C 3 17 ? 38.034 31.830 63.282 1.00 154.41 ? 1433 LEU C CD2 1 ATOM 12581 N N . LEU C 3 18 ? 33.468 33.049 65.875 1.00 158.51 ? 1434 LEU C N 1 ATOM 12582 C CA . LEU C 3 18 ? 32.227 33.783 65.636 1.00 150.52 ? 1434 LEU C CA 1 ATOM 12583 C C . LEU C 3 18 ? 32.458 35.285 65.454 1.00 157.26 ? 1434 LEU C C 1 ATOM 12584 O O . LEU C 3 18 ? 33.312 35.876 66.115 1.00 170.60 ? 1434 LEU C O 1 ATOM 12585 C CB . LEU C 3 18 ? 31.250 33.535 66.792 1.00 148.47 ? 1434 LEU C CB 1 ATOM 12586 C CG . LEU C 3 18 ? 29.781 33.929 66.625 1.00 148.11 ? 1434 LEU C CG 1 ATOM 12587 C CD1 . LEU C 3 18 ? 28.895 32.934 67.355 1.00 151.31 ? 1434 LEU C CD1 1 ATOM 12588 C CD2 . LEU C 3 18 ? 29.524 35.337 67.141 1.00 148.08 ? 1434 LEU C CD2 1 ATOM 12589 N N . ILE C 3 19 ? 31.689 35.894 64.552 1.00 157.77 ? 1435 ILE C N 1 ATOM 12590 C CA . ILE C 3 19 ? 31.754 37.337 64.315 1.00 164.79 ? 1435 ILE C CA 1 ATOM 12591 C C . ILE C 3 19 ? 30.362 37.968 64.326 1.00 154.23 ? 1435 ILE C C 1 ATOM 12592 O O . ILE C 3 19 ? 29.361 37.289 64.093 1.00 146.68 ? 1435 ILE C O 1 ATOM 12593 C CB . ILE C 3 19 ? 32.436 37.669 62.969 1.00 160.77 ? 1435 ILE C CB 1 ATOM 12594 C CG1 . ILE C 3 19 ? 31.600 37.146 61.798 1.00 148.39 ? 1435 ILE C CG1 1 ATOM 12595 C CG2 . ILE C 3 19 ? 33.850 37.107 62.926 1.00 164.70 ? 1435 ILE C CG2 1 ATOM 12596 C CD1 . ILE C 3 19 ? 32.188 37.460 60.439 1.00 135.42 ? 1435 ILE C CD1 1 ATOM 12597 N N . SER C 3 20 ? 30.301 39.268 64.603 1.00 152.92 ? 1436 SER C N 1 ATOM 12598 C CA . SER C 3 20 ? 29.026 39.978 64.634 1.00 154.70 ? 1436 SER C CA 1 ATOM 12599 C C . SER C 3 20 ? 29.132 41.390 64.062 1.00 161.89 ? 1436 SER C C 1 ATOM 12600 O O . SER C 3 20 ? 30.038 42.147 64.410 1.00 167.07 ? 1436 SER C O 1 ATOM 12601 C CB . SER C 3 20 ? 28.488 40.039 66.066 1.00 157.39 ? 1436 SER C CB 1 ATOM 12602 O OG . SER C 3 20 ? 27.226 40.682 66.108 1.00 160.51 ? 1436 SER C OG 1 ATOM 12603 N N . TRP C 3 21 ? 28.193 41.736 63.186 1.00 162.98 ? 1437 TRP C N 1 ATOM 12604 C CA . TRP C 3 21 ? 28.104 43.080 62.624 1.00 164.38 ? 1437 TRP C CA 1 ATOM 12605 C C . TRP C 3 21 ? 26.821 43.748 63.106 1.00 165.62 ? 1437 TRP C C 1 ATOM 12606 O O . TRP C 3 21 ? 26.045 43.140 63.843 1.00 160.66 ? 1437 TRP C O 1 ATOM 12607 C CB . TRP C 3 21 ? 28.152 43.033 61.097 1.00 168.41 ? 1437 TRP C CB 1 ATOM 12608 C CG . TRP C 3 21 ? 27.232 42.013 60.504 1.00 172.06 ? 1437 TRP C CG 1 ATOM 12609 C CD1 . TRP C 3 21 ? 25.964 42.220 60.048 1.00 175.90 ? 1437 TRP C CD1 1 ATOM 12610 C CD2 . TRP C 3 21 ? 27.509 40.622 60.304 1.00 173.38 ? 1437 TRP C CD2 1 ATOM 12611 N NE1 . TRP C 3 21 ? 25.433 41.044 59.575 1.00 172.52 ? 1437 TRP C NE1 1 ATOM 12612 C CE2 . TRP C 3 21 ? 26.362 40.048 59.722 1.00 172.47 ? 1437 TRP C CE2 1 ATOM 12613 C CE3 . TRP C 3 21 ? 28.614 39.806 60.563 1.00 177.13 ? 1437 TRP C CE3 1 ATOM 12614 C CZ2 . TRP C 3 21 ? 26.289 38.696 59.393 1.00 165.28 ? 1437 TRP C CZ2 1 ATOM 12615 C CZ3 . TRP C 3 21 ? 28.540 38.464 60.235 1.00 167.57 ? 1437 TRP C CZ3 1 ATOM 12616 C CH2 . TRP C 3 21 ? 27.385 37.923 59.657 1.00 160.40 ? 1437 TRP C CH2 1 ATOM 12617 N N . ASP C 3 22 ? 26.590 44.994 62.698 1.00 170.86 ? 1438 ASP C N 1 ATOM 12618 C CA . ASP C 3 22 ? 25.480 45.743 63.275 1.00 174.96 ? 1438 ASP C CA 1 ATOM 12619 C C . ASP C 3 22 ? 24.578 46.481 62.284 1.00 181.12 ? 1438 ASP C C 1 ATOM 12620 O O . ASP C 3 22 ? 25.013 47.406 61.599 1.00 198.78 ? 1438 ASP C O 1 ATOM 12621 C CB . ASP C 3 22 ? 26.027 46.752 64.290 1.00 176.72 ? 1438 ASP C CB 1 ATOM 12622 C CG . ASP C 3 22 ? 24.936 47.387 65.128 1.00 179.43 ? 1438 ASP C CG 1 ATOM 12623 O OD1 . ASP C 3 22 ? 24.371 48.414 64.697 1.00 177.32 ? 1438 ASP C OD1 1 ATOM 12624 O OD2 . ASP C 3 22 ? 24.646 46.859 66.223 1.00 182.84 ? 1438 ASP C OD2 1 ATOM 12625 N N . ALA C 3 23 ? 23.327 46.028 62.217 1.00 176.19 ? 1439 ALA C N 1 ATOM 12626 C CA . ALA C 3 23 ? 22.161 46.829 61.820 1.00 184.01 ? 1439 ALA C CA 1 ATOM 12627 C C . ALA C 3 23 ? 22.341 47.901 60.739 1.00 180.01 ? 1439 ALA C C 1 ATOM 12628 O O . ALA C 3 23 ? 22.289 49.094 61.044 1.00 190.00 ? 1439 ALA C O 1 ATOM 12629 C CB . ALA C 3 23 ? 21.574 47.486 63.067 1.00 200.36 ? 1439 ALA C CB 1 ATOM 12630 N N . PRO C 3 24 ? 22.564 47.492 59.480 1.00 154.23 ? 1440 PRO C N 1 ATOM 12631 C CA . PRO C 3 24 ? 22.455 48.478 58.397 1.00 148.11 ? 1440 PRO C CA 1 ATOM 12632 C C . PRO C 3 24 ? 21.042 49.062 58.329 1.00 149.11 ? 1440 PRO C C 1 ATOM 12633 O O . PRO C 3 24 ? 20.072 48.304 58.333 1.00 138.58 ? 1440 PRO C O 1 ATOM 12634 C CB . PRO C 3 24 ? 22.775 47.664 57.141 1.00 138.65 ? 1440 PRO C CB 1 ATOM 12635 C CG . PRO C 3 24 ? 23.579 46.511 57.633 1.00 152.79 ? 1440 PRO C CG 1 ATOM 12636 C CD . PRO C 3 24 ? 23.043 46.188 58.998 1.00 155.67 ? 1440 PRO C CD 1 ATOM 12637 N N . ALA C 3 25 ? 20.932 50.386 58.265 1.00 160.26 ? 1441 ALA C N 1 ATOM 12638 C CA . ALA C 3 25 ? 19.634 51.055 58.348 1.00 163.16 ? 1441 ALA C CA 1 ATOM 12639 C C . ALA C 3 25 ? 18.739 50.767 57.143 1.00 156.10 ? 1441 ALA C C 1 ATOM 12640 O O . ALA C 3 25 ? 17.518 50.902 57.227 1.00 159.19 ? 1441 ALA C O 1 ATOM 12641 C CB . ALA C 3 25 ? 19.827 52.557 58.511 1.00 163.60 ? 1441 ALA C CB 1 ATOM 12642 N N . VAL C 3 26 ? 19.342 50.373 56.026 1.00 142.14 ? 1442 VAL C N 1 ATOM 12643 C CA . VAL C 3 26 ? 18.573 50.029 54.836 1.00 133.52 ? 1442 VAL C CA 1 ATOM 12644 C C . VAL C 3 26 ? 17.963 48.636 55.011 1.00 134.81 ? 1442 VAL C C 1 ATOM 12645 O O . VAL C 3 26 ? 18.216 47.967 56.014 1.00 142.18 ? 1442 VAL C O 1 ATOM 12646 C CB . VAL C 3 26 ? 19.454 50.078 53.560 1.00 146.12 ? 1442 VAL C CB 1 ATOM 12647 C CG1 . VAL C 3 26 ? 20.218 48.769 53.373 1.00 133.18 ? 1442 VAL C CG1 1 ATOM 12648 C CG2 . VAL C 3 26 ? 18.617 50.401 52.325 1.00 138.66 ? 1442 VAL C CG2 1 ATOM 12649 N N . THR C 3 27 ? 17.165 48.201 54.041 1.00 122.88 ? 1443 THR C N 1 ATOM 12650 C CA . THR C 3 27 ? 16.585 46.864 54.071 1.00 134.54 ? 1443 THR C CA 1 ATOM 12651 C C . THR C 3 27 ? 17.514 45.879 53.369 1.00 131.84 ? 1443 THR C C 1 ATOM 12652 O O . THR C 3 27 ? 17.826 46.041 52.191 1.00 135.11 ? 1443 THR C O 1 ATOM 12653 C CB . THR C 3 27 ? 15.198 46.832 53.404 1.00 135.18 ? 1443 THR C CB 1 ATOM 12654 O OG1 . THR C 3 27 ? 14.354 47.826 54.000 1.00 125.09 ? 1443 THR C OG1 1 ATOM 12655 C CG2 . THR C 3 27 ? 14.560 45.458 53.566 1.00 106.82 ? 1443 THR C CG2 1 ATOM 12656 N N . VAL C 3 28 ? 17.956 44.860 54.099 1.00 124.52 ? 1444 VAL C N 1 ATOM 12657 C CA . VAL C 3 28 ? 18.950 43.925 53.584 1.00 106.77 ? 1444 VAL C CA 1 ATOM 12658 C C . VAL C 3 28 ? 18.356 42.569 53.212 1.00 114.86 ? 1444 VAL C C 1 ATOM 12659 O O . VAL C 3 28 ? 17.678 41.930 54.015 1.00 120.79 ? 1444 VAL C O 1 ATOM 12660 C CB . VAL C 3 28 ? 20.078 43.710 54.604 1.00 116.74 ? 1444 VAL C CB 1 ATOM 12661 C CG1 . VAL C 3 28 ? 21.064 44.864 54.547 1.00 131.30 ? 1444 VAL C CG1 1 ATOM 12662 C CG2 . VAL C 3 28 ? 19.500 43.561 56.005 1.00 122.22 ? 1444 VAL C CG2 1 ATOM 12663 N N . ARG C 3 29 ? 18.610 42.143 51.979 1.00 124.59 ? 1445 ARG C N 1 ATOM 12664 C CA . ARG C 3 29 ? 18.141 40.849 51.500 1.00 111.13 ? 1445 ARG C CA 1 ATOM 12665 C C . ARG C 3 29 ? 18.986 39.709 52.055 1.00 112.95 ? 1445 ARG C C 1 ATOM 12666 O O . ARG C 3 29 ? 18.461 38.733 52.590 1.00 107.64 ? 1445 ARG C O 1 ATOM 12667 C CB . ARG C 3 29 ? 18.162 40.814 49.972 1.00 104.66 ? 1445 ARG C CB 1 ATOM 12668 C CG . ARG C 3 29 ? 17.667 39.513 49.363 1.00 109.06 ? 1445 ARG C CG 1 ATOM 12669 C CD . ARG C 3 29 ? 17.932 39.485 47.864 1.00 98.94 ? 1445 ARG C CD 1 ATOM 12670 N NE . ARG C 3 29 ? 17.193 38.425 47.187 1.00 71.81 ? 1445 ARG C NE 1 ATOM 12671 C CZ . ARG C 3 29 ? 17.341 38.115 45.904 1.00 104.16 ? 1445 ARG C CZ 1 ATOM 12672 N NH1 . ARG C 3 29 ? 16.624 37.136 45.368 1.00 118.79 ? 1445 ARG C NH1 1 ATOM 12673 N NH2 . ARG C 3 29 ? 18.209 38.783 45.155 1.00 91.60 ? 1445 ARG C NH2 1 ATOM 12674 N N . TYR C 3 30 ? 20.302 39.854 51.930 1.00 125.54 ? 1446 TYR C N 1 ATOM 12675 C CA . TYR C 3 30 ? 21.249 38.805 52.291 1.00 126.12 ? 1446 TYR C CA 1 ATOM 12676 C C . TYR C 3 30 ? 22.575 39.389 52.764 1.00 116.71 ? 1446 TYR C C 1 ATOM 12677 O O . TYR C 3 30 ? 22.856 40.568 52.553 1.00 133.56 ? 1446 TYR C O 1 ATOM 12678 C CB . TYR C 3 30 ? 21.502 37.876 51.099 1.00 131.05 ? 1446 TYR C CB 1 ATOM 12679 C CG . TYR C 3 30 ? 20.429 36.841 50.852 1.00 126.09 ? 1446 TYR C CG 1 ATOM 12680 C CD1 . TYR C 3 30 ? 19.880 36.113 51.900 1.00 132.70 ? 1446 TYR C CD1 1 ATOM 12681 C CD2 . TYR C 3 30 ? 19.973 36.584 49.566 1.00 111.47 ? 1446 TYR C CD2 1 ATOM 12682 C CE1 . TYR C 3 30 ? 18.901 35.163 51.673 1.00 124.64 ? 1446 TYR C CE1 1 ATOM 12683 C CE2 . TYR C 3 30 ? 18.996 35.636 49.330 1.00 116.48 ? 1446 TYR C CE2 1 ATOM 12684 C CZ . TYR C 3 30 ? 18.465 34.929 50.386 1.00 114.81 ? 1446 TYR C CZ 1 ATOM 12685 O OH . TYR C 3 30 ? 17.492 33.986 50.154 1.00 115.93 ? 1446 TYR C OH 1 ATOM 12686 N N . TYR C 3 31 ? 23.385 38.556 53.408 1.00 111.49 ? 1447 TYR C N 1 ATOM 12687 C CA . TYR C 3 31 ? 24.754 38.921 53.748 1.00 114.22 ? 1447 TYR C CA 1 ATOM 12688 C C . TYR C 3 31 ? 25.723 37.888 53.181 1.00 115.50 ? 1447 TYR C C 1 ATOM 12689 O O . TYR C 3 31 ? 25.500 36.684 53.305 1.00 139.63 ? 1447 TYR C O 1 ATOM 12690 C CB . TYR C 3 31 ? 24.933 39.040 55.263 1.00 145.48 ? 1447 TYR C CB 1 ATOM 12691 C CG . TYR C 3 31 ? 24.200 40.205 55.891 1.00 147.47 ? 1447 TYR C CG 1 ATOM 12692 C CD1 . TYR C 3 31 ? 24.687 41.501 55.777 1.00 138.68 ? 1447 TYR C CD1 1 ATOM 12693 C CD2 . TYR C 3 31 ? 23.028 40.007 56.611 1.00 143.66 ? 1447 TYR C CD2 1 ATOM 12694 C CE1 . TYR C 3 31 ? 24.023 42.567 56.354 1.00 134.48 ? 1447 TYR C CE1 1 ATOM 12695 C CE2 . TYR C 3 31 ? 22.358 41.067 57.192 1.00 133.19 ? 1447 TYR C CE2 1 ATOM 12696 C CZ . TYR C 3 31 ? 22.860 42.343 57.060 1.00 134.95 ? 1447 TYR C CZ 1 ATOM 12697 O OH . TYR C 3 31 ? 22.194 43.397 57.638 1.00 127.40 ? 1447 TYR C OH 1 ATOM 12698 N N . ARG C 3 32 ? 26.798 38.363 52.560 1.00 107.03 ? 1448 ARG C N 1 ATOM 12699 C CA . ARG C 3 32 ? 27.774 37.483 51.926 1.00 110.23 ? 1448 ARG C CA 1 ATOM 12700 C C . ARG C 3 32 ? 29.146 37.579 52.600 1.00 130.52 ? 1448 ARG C C 1 ATOM 12701 O O . ARG C 3 32 ? 29.787 38.629 52.571 1.00 142.97 ? 1448 ARG C O 1 ATOM 12702 C CB . ARG C 3 32 ? 27.881 37.816 50.436 1.00 104.34 ? 1448 ARG C CB 1 ATOM 12703 C CG . ARG C 3 32 ? 28.986 37.089 49.692 1.00 105.62 ? 1448 ARG C CG 1 ATOM 12704 C CD . ARG C 3 32 ? 28.863 37.317 48.192 1.00 101.62 ? 1448 ARG C CD 1 ATOM 12705 N NE . ARG C 3 32 ? 30.121 37.080 47.489 1.00 120.72 ? 1448 ARG C NE 1 ATOM 12706 C CZ . ARG C 3 32 ? 30.966 38.040 47.128 1.00 127.44 ? 1448 ARG C CZ 1 ATOM 12707 N NH1 . ARG C 3 32 ? 30.686 39.308 47.398 1.00 113.71 ? 1448 ARG C NH1 1 ATOM 12708 N NH2 . ARG C 3 32 ? 32.090 37.735 46.493 1.00 141.14 ? 1448 ARG C NH2 1 ATOM 12709 N N . ILE C 3 33 ? 29.588 36.479 53.204 1.00 122.93 ? 1449 ILE C N 1 ATOM 12710 C CA . ILE C 3 33 ? 30.852 36.451 53.941 1.00 134.44 ? 1449 ILE C CA 1 ATOM 12711 C C . ILE C 3 33 ? 31.960 35.767 53.138 1.00 127.58 ? 1449 ILE C C 1 ATOM 12712 O O . ILE C 3 33 ? 31.771 34.665 52.631 1.00 127.40 ? 1449 ILE C O 1 ATOM 12713 C CB . ILE C 3 33 ? 30.702 35.729 55.303 1.00 125.41 ? 1449 ILE C CB 1 ATOM 12714 C CG1 . ILE C 3 33 ? 29.683 36.444 56.197 1.00 129.58 ? 1449 ILE C CG1 1 ATOM 12715 C CG2 . ILE C 3 33 ? 32.045 35.634 56.010 1.00 131.14 ? 1449 ILE C CG2 1 ATOM 12716 C CD1 . ILE C 3 33 ? 28.257 35.944 56.047 1.00 120.98 ? 1449 ILE C CD1 1 ATOM 12717 N N . THR C 3 34 ? 33.112 36.425 53.030 1.00 131.00 ? 1450 THR C N 1 ATOM 12718 C CA . THR C 3 34 ? 34.247 35.888 52.280 1.00 139.31 ? 1450 THR C CA 1 ATOM 12719 C C . THR C 3 34 ? 35.528 35.914 53.109 1.00 153.24 ? 1450 THR C C 1 ATOM 12720 O O . THR C 3 34 ? 35.884 36.948 53.674 1.00 163.74 ? 1450 THR C O 1 ATOM 12721 C CB . THR C 3 34 ? 34.486 36.676 50.979 1.00 138.89 ? 1450 THR C CB 1 ATOM 12722 O OG1 . THR C 3 34 ? 33.301 36.652 50.176 1.00 144.06 ? 1450 THR C OG1 1 ATOM 12723 C CG2 . THR C 3 34 ? 35.645 36.076 50.194 1.00 139.55 ? 1450 THR C CG2 1 ATOM 12724 N N . TYR C 3 35 ? 36.219 34.780 53.189 1.00 143.01 ? 1451 TYR C N 1 ATOM 12725 C CA . TYR C 3 35 ? 37.437 34.712 53.989 1.00 149.64 ? 1451 TYR C CA 1 ATOM 12726 C C . TYR C 3 35 ? 38.528 33.790 53.436 1.00 163.43 ? 1451 TYR C C 1 ATOM 12727 O O . TYR C 3 35 ? 38.247 32.665 53.023 1.00 179.23 ? 1451 TYR C O 1 ATOM 12728 C CB . TYR C 3 35 ? 37.084 34.261 55.412 1.00 158.66 ? 1451 TYR C CB 1 ATOM 12729 C CG . TYR C 3 35 ? 36.484 32.869 55.489 1.00 158.16 ? 1451 TYR C CG 1 ATOM 12730 C CD1 . TYR C 3 35 ? 35.126 32.662 55.279 1.00 156.17 ? 1451 TYR C CD1 1 ATOM 12731 C CD2 . TYR C 3 35 ? 37.276 31.763 55.775 1.00 147.75 ? 1451 TYR C CD2 1 ATOM 12732 C CE1 . TYR C 3 35 ? 34.576 31.393 55.347 1.00 152.42 ? 1451 TYR C CE1 1 ATOM 12733 C CE2 . TYR C 3 35 ? 36.735 30.493 55.843 1.00 146.95 ? 1451 TYR C CE2 1 ATOM 12734 C CZ . TYR C 3 35 ? 35.385 30.313 55.630 1.00 152.83 ? 1451 TYR C CZ 1 ATOM 12735 O OH . TYR C 3 35 ? 34.844 29.049 55.700 1.00 154.59 ? 1451 TYR C OH 1 ATOM 12736 N N . GLY C 3 36 ? 39.768 34.279 53.409 1.00 151.97 ? 1452 GLY C N 1 ATOM 12737 C CA . GLY C 3 36 ? 40.916 33.399 53.554 1.00 167.00 ? 1452 GLY C CA 1 ATOM 12738 C C . GLY C 3 36 ? 42.272 34.075 53.679 1.00 170.88 ? 1452 GLY C C 1 ATOM 12739 O O . GLY C 3 36 ? 42.539 35.099 53.049 1.00 169.55 ? 1452 GLY C O 1 ATOM 12740 N N . GLU C 3 37 ? 43.125 33.456 54.495 1.00 177.66 ? 1453 GLU C N 1 ATOM 12741 C CA . GLU C 3 37 ? 44.544 33.782 54.693 1.00 202.02 ? 1453 GLU C CA 1 ATOM 12742 C C . GLU C 3 37 ? 44.892 35.273 54.668 1.00 198.54 ? 1453 GLU C C 1 ATOM 12743 O O . GLU C 3 37 ? 44.121 36.106 55.146 1.00 190.28 ? 1453 GLU C O 1 ATOM 12744 C CB . GLU C 3 37 ? 45.390 33.025 53.669 1.00 214.04 ? 1453 GLU C CB 1 ATOM 12745 C CG . GLU C 3 37 ? 45.922 31.708 54.225 1.00 223.95 ? 1453 GLU C CG 1 ATOM 12746 C CD . GLU C 3 37 ? 46.019 30.613 53.185 1.00 227.70 ? 1453 GLU C CD 1 ATOM 12747 O OE1 . GLU C 3 37 ? 45.580 29.480 53.477 1.00 225.37 ? 1453 GLU C OE1 1 ATOM 12748 O OE2 . GLU C 3 37 ? 46.538 30.880 52.082 1.00 231.60 ? 1453 GLU C OE2 1 ATOM 12749 N N . THR C 3 38 ? 46.054 35.602 54.103 1.00 195.72 ? 1454 THR C N 1 ATOM 12750 C CA . THR C 3 38 ? 46.415 36.994 53.841 1.00 201.04 ? 1454 THR C CA 1 ATOM 12751 C C . THR C 3 38 ? 47.076 37.232 52.481 1.00 205.82 ? 1454 THR C C 1 ATOM 12752 O O . THR C 3 38 ? 46.470 37.784 51.563 1.00 197.80 ? 1454 THR C O 1 ATOM 12753 C CB . THR C 3 38 ? 47.371 37.540 54.926 1.00 213.52 ? 1454 THR C CB 1 ATOM 12754 O OG1 . THR C 3 38 ? 48.474 36.640 55.093 1.00 225.14 ? 1454 THR C OG1 1 ATOM 12755 C CG2 . THR C 3 38 ? 46.650 37.707 56.257 1.00 207.37 ? 1454 THR C CG2 1 ATOM 12756 N N . GLY C 3 39 ? 48.332 36.799 52.373 1.00 216.78 ? 1455 GLY C N 1 ATOM 12757 C CA . GLY C 3 39 ? 49.196 37.180 51.267 1.00 219.69 ? 1455 GLY C CA 1 ATOM 12758 C C . GLY C 3 39 ? 49.533 36.151 50.203 1.00 220.52 ? 1455 GLY C C 1 ATOM 12759 O O . GLY C 3 39 ? 50.135 36.493 49.185 1.00 222.21 ? 1455 GLY C O 1 ATOM 12760 N N . GLY C 3 40 ? 49.161 34.896 50.426 1.00 221.77 ? 1456 GLY C N 1 ATOM 12761 C CA . GLY C 3 40 ? 49.490 33.841 49.483 1.00 225.74 ? 1456 GLY C CA 1 ATOM 12762 C C . GLY C 3 40 ? 48.643 33.913 48.229 1.00 224.90 ? 1456 GLY C C 1 ATOM 12763 O O . GLY C 3 40 ? 47.954 34.907 47.994 1.00 221.07 ? 1456 GLY C O 1 ATOM 12764 N N . ASN C 3 41 ? 48.702 32.865 47.412 1.00 230.03 ? 1457 ASN C N 1 ATOM 12765 C CA . ASN C 3 41 ? 47.800 32.732 46.271 1.00 234.79 ? 1457 ASN C CA 1 ATOM 12766 C C . ASN C 3 41 ? 46.355 32.759 46.758 1.00 234.14 ? 1457 ASN C C 1 ATOM 12767 O O . ASN C 3 41 ? 45.446 33.193 46.050 1.00 233.10 ? 1457 ASN C O 1 ATOM 12768 C CB . ASN C 3 41 ? 48.086 31.440 45.504 1.00 239.48 ? 1457 ASN C CB 1 ATOM 12769 C CG . ASN C 3 41 ? 47.906 30.199 46.362 1.00 238.85 ? 1457 ASN C CG 1 ATOM 12770 O OD1 . ASN C 3 41 ? 48.814 29.797 47.091 1.00 243.86 ? 1457 ASN C OD1 1 ATOM 12771 N ND2 . ASN C 3 41 ? 46.731 29.586 46.279 1.00 229.44 ? 1457 ASN C ND2 1 ATOM 12772 N N . SER C 3 42 ? 46.187 32.262 47.981 1.00 236.56 ? 1458 SER C N 1 ATOM 12773 C CA . SER C 3 42 ? 44.952 32.278 48.762 1.00 228.63 ? 1458 SER C CA 1 ATOM 12774 C C . SER C 3 42 ? 43.866 31.349 48.214 1.00 215.41 ? 1458 SER C C 1 ATOM 12775 O O . SER C 3 42 ? 43.720 31.188 47.001 1.00 212.68 ? 1458 SER C O 1 ATOM 12776 C CB . SER C 3 42 ? 44.414 33.714 48.855 1.00 227.93 ? 1458 SER C CB 1 ATOM 12777 O OG . SER C 3 42 ? 43.268 33.790 49.683 1.00 222.67 ? 1458 SER C OG 1 ATOM 12778 N N . PRO C 3 43 ? 43.059 30.793 49.100 1.00 205.54 ? 1459 PRO C N 1 ATOM 12779 C CA . PRO C 3 43 ? 41.990 29.890 48.680 1.00 200.53 ? 1459 PRO C CA 1 ATOM 12780 C C . PRO C 3 43 ? 40.619 30.466 48.992 1.00 193.37 ? 1459 PRO C C 1 ATOM 12781 O O . PRO C 3 43 ? 39.907 29.909 49.819 1.00 200.57 ? 1459 PRO C O 1 ATOM 12782 C CB . PRO C 3 43 ? 42.228 28.675 49.563 1.00 198.80 ? 1459 PRO C CB 1 ATOM 12783 C CG . PRO C 3 43 ? 42.729 29.271 50.835 1.00 199.64 ? 1459 PRO C CG 1 ATOM 12784 C CD . PRO C 3 43 ? 43.564 30.458 50.441 1.00 203.81 ? 1459 PRO C CD 1 ATOM 12785 N N . VAL C 3 44 ? 40.247 31.564 48.354 1.00 174.98 ? 1460 VAL C N 1 ATOM 12786 C CA . VAL C 3 44 ? 38.984 32.205 48.679 1.00 159.27 ? 1460 VAL C CA 1 ATOM 12787 C C . VAL C 3 44 ? 37.950 31.202 49.147 1.00 153.69 ? 1460 VAL C C 1 ATOM 12788 O O . VAL C 3 44 ? 37.916 30.081 48.682 1.00 168.12 ? 1460 VAL C O 1 ATOM 12789 C CB . VAL C 3 44 ? 38.424 32.949 47.477 1.00 150.31 ? 1460 VAL C CB 1 ATOM 12790 C CG1 . VAL C 3 44 ? 38.073 34.368 47.878 1.00 141.10 ? 1460 VAL C CG1 1 ATOM 12791 C CG2 . VAL C 3 44 ? 39.441 32.928 46.351 1.00 151.95 ? 1460 VAL C CG2 1 ATOM 12792 N N . GLN C 3 45 ? 37.110 31.618 50.077 1.00 148.85 ? 1461 GLN C N 1 ATOM 12793 C CA . GLN C 3 45 ? 36.023 30.784 50.581 1.00 155.20 ? 1461 GLN C CA 1 ATOM 12794 C C . GLN C 3 45 ? 34.865 31.670 51.022 1.00 152.41 ? 1461 GLN C C 1 ATOM 12795 O O . GLN C 3 45 ? 35.079 32.717 51.633 1.00 147.98 ? 1461 GLN C O 1 ATOM 12796 C CB . GLN C 3 45 ? 36.504 29.909 51.744 1.00 157.28 ? 1461 GLN C CB 1 ATOM 12797 C CG . GLN C 3 45 ? 35.437 28.998 52.342 1.00 154.77 ? 1461 GLN C CG 1 ATOM 12798 C CD . GLN C 3 45 ? 35.456 27.600 51.752 1.00 164.41 ? 1461 GLN C CD 1 ATOM 12799 O OE1 . GLN C 3 45 ? 34.410 27.030 51.439 1.00 159.40 ? 1461 GLN C OE1 1 ATOM 12800 N NE2 . GLN C 3 45 ? 36.649 27.035 51.608 1.00 170.50 ? 1461 GLN C NE2 1 ATOM 12801 N N . GLU C 3 46 ? 33.640 31.253 50.717 1.00 146.90 ? 1462 GLU C N 1 ATOM 12802 C CA . GLU C 3 46 ? 32.479 32.092 50.985 1.00 133.36 ? 1462 GLU C CA 1 ATOM 12803 C C . GLU C 3 46 ? 31.199 31.304 51.247 1.00 131.42 ? 1462 GLU C C 1 ATOM 12804 O O . GLU C 3 46 ? 31.094 30.129 50.897 1.00 142.00 ? 1462 GLU C O 1 ATOM 12805 C CB . GLU C 3 46 ? 32.251 33.048 49.813 1.00 133.41 ? 1462 GLU C CB 1 ATOM 12806 C CG . GLU C 3 46 ? 31.877 32.349 48.514 1.00 144.10 ? 1462 GLU C CG 1 ATOM 12807 C CD . GLU C 3 46 ? 31.785 33.305 47.339 1.00 151.84 ? 1462 GLU C CD 1 ATOM 12808 O OE1 . GLU C 3 46 ? 32.609 34.242 47.265 1.00 150.13 ? 1462 GLU C OE1 1 ATOM 12809 O OE2 . GLU C 3 46 ? 30.887 33.122 46.490 1.00 149.19 ? 1462 GLU C OE2 1 ATOM 12810 N N . PHE C 3 47 ? 30.230 31.970 51.871 1.00 120.13 ? 1463 PHE C N 1 ATOM 12811 C CA . PHE C 3 47 ? 28.892 31.416 52.051 1.00 126.46 ? 1463 PHE C CA 1 ATOM 12812 C C . PHE C 3 47 ? 27.876 32.543 52.206 1.00 129.53 ? 1463 PHE C C 1 ATOM 12813 O O . PHE C 3 47 ? 28.242 33.718 52.213 1.00 122.09 ? 1463 PHE C O 1 ATOM 12814 C CB . PHE C 3 47 ? 28.842 30.476 53.257 1.00 126.46 ? 1463 PHE C CB 1 ATOM 12815 C CG . PHE C 3 47 ? 29.205 31.133 54.557 1.00 129.58 ? 1463 PHE C CG 1 ATOM 12816 C CD1 . PHE C 3 47 ? 30.528 31.221 54.958 1.00 134.15 ? 1463 PHE C CD1 1 ATOM 12817 C CD2 . PHE C 3 47 ? 28.222 31.647 55.387 1.00 121.20 ? 1463 PHE C CD2 1 ATOM 12818 C CE1 . PHE C 3 47 ? 30.866 31.819 56.157 1.00 129.47 ? 1463 PHE C CE1 1 ATOM 12819 C CE2 . PHE C 3 47 ? 28.553 32.246 56.587 1.00 123.91 ? 1463 PHE C CE2 1 ATOM 12820 C CZ . PHE C 3 47 ? 29.877 32.332 56.973 1.00 128.22 ? 1463 PHE C CZ 1 ATOM 12821 N N . THR C 3 48 ? 26.604 32.182 52.340 1.00 137.40 ? 1464 THR C N 1 ATOM 12822 C CA . THR C 3 48 ? 25.530 33.171 52.359 1.00 129.13 ? 1464 THR C CA 1 ATOM 12823 C C . THR C 3 48 ? 24.702 33.081 53.638 1.00 127.91 ? 1464 THR C C 1 ATOM 12824 O O . THR C 3 48 ? 24.445 31.991 54.147 1.00 138.61 ? 1464 THR C O 1 ATOM 12825 C CB . THR C 3 48 ? 24.602 33.002 51.134 1.00 124.55 ? 1464 THR C CB 1 ATOM 12826 O OG1 . THR C 3 48 ? 25.380 33.061 49.933 1.00 121.11 ? 1464 THR C OG1 1 ATOM 12827 C CG2 . THR C 3 48 ? 23.540 34.093 51.095 1.00 115.09 ? 1464 THR C CG2 1 ATOM 12828 N N . VAL C 3 49 ? 24.301 34.238 54.155 1.00 115.89 ? 1465 VAL C N 1 ATOM 12829 C CA . VAL C 3 49 ? 23.476 34.312 55.354 1.00 114.49 ? 1465 VAL C CA 1 ATOM 12830 C C . VAL C 3 49 ? 22.268 35.215 55.101 1.00 119.09 ? 1465 VAL C C 1 ATOM 12831 O O . VAL C 3 49 ? 22.400 36.255 54.455 1.00 110.19 ? 1465 VAL C O 1 ATOM 12832 C CB . VAL C 3 49 ? 24.306 34.836 56.551 1.00 119.03 ? 1465 VAL C CB 1 ATOM 12833 C CG1 . VAL C 3 49 ? 23.417 35.320 57.685 1.00 119.22 ? 1465 VAL C CG1 1 ATOM 12834 C CG2 . VAL C 3 49 ? 25.271 33.764 57.036 1.00 118.85 ? 1465 VAL C CG2 1 ATOM 12835 N N . PRO C 3 50 ? 21.085 34.821 55.606 1.00 117.77 ? 1466 PRO C N 1 ATOM 12836 C CA . PRO C 3 50 ? 19.884 35.652 55.462 1.00 124.28 ? 1466 PRO C CA 1 ATOM 12837 C C . PRO C 3 50 ? 20.049 37.023 56.108 1.00 136.60 ? 1466 PRO C C 1 ATOM 12838 O O . PRO C 3 50 ? 20.792 37.161 57.080 1.00 144.53 ? 1466 PRO C O 1 ATOM 12839 C CB . PRO C 3 50 ? 18.796 34.837 56.176 1.00 117.46 ? 1466 PRO C CB 1 ATOM 12840 C CG . PRO C 3 50 ? 19.530 33.832 57.004 1.00 117.18 ? 1466 PRO C CG 1 ATOM 12841 C CD . PRO C 3 50 ? 20.780 33.531 56.244 1.00 117.50 ? 1466 PRO C CD 1 ATOM 12842 N N . GLY C 3 51 ? 19.355 38.021 55.570 1.00 138.21 ? 1467 GLY C N 1 ATOM 12843 C CA . GLY C 3 51 ? 19.467 39.385 56.055 1.00 134.78 ? 1467 GLY C CA 1 ATOM 12844 C C . GLY C 3 51 ? 18.966 39.575 57.474 1.00 135.69 ? 1467 GLY C C 1 ATOM 12845 O O . GLY C 3 51 ? 19.209 40.611 58.091 1.00 143.99 ? 1467 GLY C O 1 ATOM 12846 N N . SER C 3 52 ? 18.263 38.573 57.991 1.00 134.88 ? 1468 SER C N 1 ATOM 12847 C CA . SER C 3 52 ? 17.710 38.640 59.337 1.00 140.87 ? 1468 SER C CA 1 ATOM 12848 C C . SER C 3 52 ? 18.734 38.226 60.395 1.00 145.98 ? 1468 SER C C 1 ATOM 12849 O O . SER C 3 52 ? 18.538 38.474 61.584 1.00 152.56 ? 1468 SER C O 1 ATOM 12850 C CB . SER C 3 52 ? 16.463 37.758 59.437 1.00 148.52 ? 1468 SER C CB 1 ATOM 12851 O OG . SER C 3 52 ? 15.828 37.909 60.695 1.00 161.66 ? 1468 SER C OG 1 ATOM 12852 N N . LYS C 3 53 ? 19.824 37.600 59.961 1.00 141.91 ? 1469 LYS C N 1 ATOM 12853 C CA . LYS C 3 53 ? 20.856 37.130 60.884 1.00 145.87 ? 1469 LYS C CA 1 ATOM 12854 C C . LYS C 3 53 ? 22.075 38.047 60.882 1.00 142.42 ? 1469 LYS C C 1 ATOM 12855 O O . LYS C 3 53 ? 22.618 38.369 59.826 1.00 144.18 ? 1469 LYS C O 1 ATOM 12856 C CB . LYS C 3 53 ? 21.282 35.700 60.537 1.00 159.28 ? 1469 LYS C CB 1 ATOM 12857 C CG . LYS C 3 53 ? 20.237 34.631 60.833 1.00 160.45 ? 1469 LYS C CG 1 ATOM 12858 C CD . LYS C 3 53 ? 20.737 33.250 60.424 1.00 150.20 ? 1469 LYS C CD 1 ATOM 12859 C CE . LYS C 3 53 ? 19.757 32.156 60.819 1.00 156.16 ? 1469 LYS C CE 1 ATOM 12860 N NZ . LYS C 3 53 ? 19.650 32.006 62.298 1.00 155.33 ? 1469 LYS C NZ 1 ATOM 12861 N N . SER C 3 54 ? 22.497 38.465 62.072 1.00 148.10 ? 1470 SER C N 1 ATOM 12862 C CA . SER C 3 54 ? 23.623 39.383 62.217 1.00 149.19 ? 1470 SER C CA 1 ATOM 12863 C C . SER C 3 54 ? 24.948 38.682 62.527 1.00 153.25 ? 1470 SER C C 1 ATOM 12864 O O . SER C 3 54 ? 25.974 39.342 62.696 1.00 155.24 ? 1470 SER C O 1 ATOM 12865 C CB . SER C 3 54 ? 23.321 40.412 63.311 1.00 151.79 ? 1470 SER C CB 1 ATOM 12866 O OG . SER C 3 54 ? 24.407 41.305 63.491 1.00 157.14 ? 1470 SER C OG 1 ATOM 12867 N N . THR C 3 55 ? 24.931 37.354 62.607 1.00 179.66 ? 1471 THR C N 1 ATOM 12868 C CA . THR C 3 55 ? 26.124 36.606 63.005 1.00 169.97 ? 1471 THR C CA 1 ATOM 12869 C C . THR C 3 55 ? 26.441 35.441 62.067 1.00 165.14 ? 1471 THR C C 1 ATOM 12870 O O . THR C 3 55 ? 25.600 35.026 61.269 1.00 154.44 ? 1471 THR C O 1 ATOM 12871 C CB . THR C 3 55 ? 25.985 36.059 64.438 1.00 163.19 ? 1471 THR C CB 1 ATOM 12872 O OG1 . THR C 3 55 ? 24.757 35.329 64.556 1.00 167.82 ? 1471 THR C OG1 1 ATOM 12873 C CG2 . THR C 3 55 ? 25.988 37.198 65.448 1.00 162.98 ? 1471 THR C CG2 1 ATOM 12874 N N . ALA C 3 56 ? 27.662 34.919 62.177 1.00 168.87 ? 1472 ALA C N 1 ATOM 12875 C CA . ALA C 3 56 ? 28.126 33.829 61.319 1.00 175.71 ? 1472 ALA C CA 1 ATOM 12876 C C . ALA C 3 56 ? 29.254 33.026 61.972 1.00 179.81 ? 1472 ALA C C 1 ATOM 12877 O O . ALA C 3 56 ? 29.864 33.473 62.943 1.00 182.95 ? 1472 ALA C O 1 ATOM 12878 C CB . ALA C 3 56 ? 28.580 34.376 59.975 1.00 170.88 ? 1472 ALA C CB 1 ATOM 12879 N N . THR C 3 57 ? 29.522 31.839 61.432 1.00 172.69 ? 1473 THR C N 1 ATOM 12880 C CA . THR C 3 57 ? 30.573 30.968 61.955 1.00 164.28 ? 1473 THR C CA 1 ATOM 12881 C C . THR C 3 57 ? 31.442 30.428 60.814 1.00 156.82 ? 1473 THR C C 1 ATOM 12882 O O . THR C 3 57 ? 31.043 30.476 59.651 1.00 152.75 ? 1473 THR C O 1 ATOM 12883 C CB . THR C 3 57 ? 29.974 29.797 62.758 1.00 161.09 ? 1473 THR C CB 1 ATOM 12884 O OG1 . THR C 3 57 ? 28.783 30.237 63.422 1.00 162.35 ? 1473 THR C OG1 1 ATOM 12885 C CG2 . THR C 3 57 ? 30.965 29.283 63.794 1.00 164.37 ? 1473 THR C CG2 1 ATOM 12886 N N . ILE C 3 58 ? 32.626 29.918 61.148 1.00 166.67 ? 1474 ILE C N 1 ATOM 12887 C CA . ILE C 3 58 ? 33.589 29.481 60.138 1.00 172.61 ? 1474 ILE C CA 1 ATOM 12888 C C . ILE C 3 58 ? 34.256 28.144 60.476 1.00 186.06 ? 1474 ILE C C 1 ATOM 12889 O O . ILE C 3 58 ? 34.788 27.965 61.569 1.00 183.37 ? 1474 ILE C O 1 ATOM 12890 C CB . ILE C 3 58 ? 34.690 30.547 59.935 1.00 162.87 ? 1474 ILE C CB 1 ATOM 12891 C CG1 . ILE C 3 58 ? 34.142 31.730 59.133 1.00 147.72 ? 1474 ILE C CG1 1 ATOM 12892 C CG2 . ILE C 3 58 ? 35.903 29.953 59.236 1.00 163.08 ? 1474 ILE C CG2 1 ATOM 12893 C CD1 . ILE C 3 58 ? 35.165 32.810 58.858 1.00 145.35 ? 1474 ILE C CD1 1 ATOM 12894 N N . SER C 3 59 ? 34.229 27.210 59.528 1.00 193.70 ? 1475 SER C N 1 ATOM 12895 C CA . SER C 3 59 ? 34.912 25.929 59.692 1.00 193.99 ? 1475 SER C CA 1 ATOM 12896 C C . SER C 3 59 ? 36.155 25.854 58.807 1.00 194.26 ? 1475 SER C C 1 ATOM 12897 O O . SER C 3 59 ? 36.053 25.872 57.580 1.00 205.55 ? 1475 SER C O 1 ATOM 12898 C CB . SER C 3 59 ? 33.967 24.770 59.370 1.00 191.35 ? 1475 SER C CB 1 ATOM 12899 O OG . SER C 3 59 ? 34.641 23.525 59.441 1.00 186.56 ? 1475 SER C OG 1 ATOM 12900 N N . GLY C 3 60 ? 37.326 25.772 59.432 1.00 178.30 ? 1476 GLY C N 1 ATOM 12901 C CA . GLY C 3 60 ? 38.575 25.709 58.692 1.00 174.09 ? 1476 GLY C CA 1 ATOM 12902 C C . GLY C 3 60 ? 39.763 26.240 59.473 1.00 177.93 ? 1476 GLY C C 1 ATOM 12903 O O . GLY C 3 60 ? 39.760 26.227 60.700 1.00 180.15 ? 1476 GLY C O 1 ATOM 12904 N N . LEU C 3 61 ? 40.783 26.688 58.742 1.00 183.14 ? 1477 LEU C N 1 ATOM 12905 C CA . LEU C 3 61 ? 41.985 27.342 59.286 1.00 180.17 ? 1477 LEU C CA 1 ATOM 12906 C C . LEU C 3 61 ? 42.606 26.656 60.512 1.00 173.58 ? 1477 LEU C C 1 ATOM 12907 O O . LEU C 3 61 ? 42.768 25.436 60.537 1.00 160.56 ? 1477 LEU C O 1 ATOM 12908 C CB . LEU C 3 61 ? 41.693 28.823 59.606 1.00 172.00 ? 1477 LEU C CB 1 ATOM 12909 C CG . LEU C 3 61 ? 40.342 29.350 60.114 1.00 170.88 ? 1477 LEU C CG 1 ATOM 12910 C CD1 . LEU C 3 61 ? 40.201 29.212 61.623 1.00 171.60 ? 1477 LEU C CD1 1 ATOM 12911 C CD2 . LEU C 3 61 ? 40.123 30.793 59.689 1.00 149.27 ? 1477 LEU C CD2 1 ATOM 12912 N N . LYS C 3 62 ? 42.952 27.451 61.522 1.00 182.24 ? 1478 LYS C N 1 ATOM 12913 C CA . LYS C 3 62 ? 43.691 26.963 62.685 1.00 197.00 ? 1478 LYS C CA 1 ATOM 12914 C C . LYS C 3 62 ? 42.999 27.333 64.002 1.00 200.98 ? 1478 LYS C C 1 ATOM 12915 O O . LYS C 3 62 ? 41.977 28.018 63.990 1.00 197.04 ? 1478 LYS C O 1 ATOM 12916 C CB . LYS C 3 62 ? 45.117 27.529 62.663 1.00 200.26 ? 1478 LYS C CB 1 ATOM 12917 C CG . LYS C 3 62 ? 46.076 26.810 61.730 1.00 190.05 ? 1478 LYS C CG 1 ATOM 12918 C CD . LYS C 3 62 ? 47.494 27.332 61.913 1.00 174.88 ? 1478 LYS C CD 1 ATOM 12919 C CE . LYS C 3 62 ? 48.488 26.560 61.063 1.00 163.58 ? 1478 LYS C CE 1 ATOM 12920 N NZ . LYS C 3 62 ? 49.877 27.058 61.260 1.00 158.87 ? 1478 LYS C NZ 1 ATOM 12921 N N . PRO C 3 63 ? 43.546 26.878 65.148 1.00 207.35 ? 1479 PRO C N 1 ATOM 12922 C CA . PRO C 3 63 ? 43.062 27.432 66.417 1.00 212.78 ? 1479 PRO C CA 1 ATOM 12923 C C . PRO C 3 63 ? 43.352 28.926 66.512 1.00 215.14 ? 1479 PRO C C 1 ATOM 12924 O O . PRO C 3 63 ? 42.556 29.687 67.062 1.00 219.17 ? 1479 PRO C O 1 ATOM 12925 C CB . PRO C 3 63 ? 43.845 26.644 67.477 1.00 218.12 ? 1479 PRO C CB 1 ATOM 12926 C CG . PRO C 3 63 ? 44.968 25.983 66.735 1.00 219.49 ? 1479 PRO C CG 1 ATOM 12927 C CD . PRO C 3 63 ? 44.426 25.718 65.371 1.00 212.25 ? 1479 PRO C CD 1 ATOM 12928 N N . GLY C 3 64 ? 44.492 29.332 65.964 1.00 211.08 ? 1480 GLY C N 1 ATOM 12929 C CA . GLY C 3 64 ? 44.798 30.736 65.788 1.00 201.68 ? 1480 GLY C CA 1 ATOM 12930 C C . GLY C 3 64 ? 45.739 30.893 64.614 1.00 192.58 ? 1480 GLY C C 1 ATOM 12931 O O . GLY C 3 64 ? 46.544 30.003 64.329 1.00 186.41 ? 1480 GLY C O 1 ATOM 12932 N N . VAL C 3 65 ? 45.663 32.051 63.966 1.00 186.80 ? 1481 VAL C N 1 ATOM 12933 C CA . VAL C 3 65 ? 46.310 32.282 62.680 1.00 188.48 ? 1481 VAL C CA 1 ATOM 12934 C C . VAL C 3 65 ? 45.920 33.687 62.224 1.00 184.60 ? 1481 VAL C C 1 ATOM 12935 O O . VAL C 3 65 ? 44.953 34.253 62.730 1.00 183.77 ? 1481 VAL C O 1 ATOM 12936 C CB . VAL C 3 65 ? 45.885 31.211 61.631 1.00 157.40 ? 1481 VAL C CB 1 ATOM 12937 C CG1 . VAL C 3 65 ? 44.386 31.264 61.393 1.00 154.21 ? 1481 VAL C CG1 1 ATOM 12938 C CG2 . VAL C 3 65 ? 46.666 31.343 60.323 1.00 150.94 ? 1481 VAL C CG2 1 ATOM 12939 N N . ASP C 3 66 ? 46.667 34.254 61.281 1.00 184.58 ? 1482 ASP C N 1 ATOM 12940 C CA . ASP C 3 66 ? 46.354 35.579 60.759 1.00 183.58 ? 1482 ASP C CA 1 ATOM 12941 C C . ASP C 3 66 ? 45.544 35.472 59.466 1.00 167.94 ? 1482 ASP C C 1 ATOM 12942 O O . ASP C 3 66 ? 46.049 35.012 58.443 1.00 167.10 ? 1482 ASP C O 1 ATOM 12943 C CB . ASP C 3 66 ? 47.639 36.378 60.524 1.00 185.93 ? 1482 ASP C CB 1 ATOM 12944 C CG . ASP C 3 66 ? 48.556 36.383 61.738 1.00 182.38 ? 1482 ASP C CG 1 ATOM 12945 O OD1 . ASP C 3 66 ? 48.061 36.153 62.862 1.00 178.90 ? 1482 ASP C OD1 1 ATOM 12946 O OD2 . ASP C 3 66 ? 49.772 36.617 61.567 1.00 172.55 ? 1482 ASP C OD2 1 ATOM 12947 N N . TYR C 3 67 ? 44.287 35.902 59.521 1.00 209.58 ? 1483 TYR C N 1 ATOM 12948 C CA . TYR C 3 67 ? 43.378 35.779 58.385 1.00 198.76 ? 1483 TYR C CA 1 ATOM 12949 C C . TYR C 3 67 ? 42.764 37.117 57.986 1.00 196.28 ? 1483 TYR C C 1 ATOM 12950 O O . TYR C 3 67 ? 43.079 38.157 58.566 1.00 197.19 ? 1483 TYR C O 1 ATOM 12951 C CB . TYR C 3 67 ? 42.262 34.781 58.706 1.00 202.96 ? 1483 TYR C CB 1 ATOM 12952 C CG . TYR C 3 67 ? 42.429 33.417 58.071 1.00 210.37 ? 1483 TYR C CG 1 ATOM 12953 C CD1 . TYR C 3 67 ? 43.529 32.623 58.360 1.00 217.91 ? 1483 TYR C CD1 1 ATOM 12954 C CD2 . TYR C 3 67 ? 41.473 32.917 57.195 1.00 202.82 ? 1483 TYR C CD2 1 ATOM 12955 C CE1 . TYR C 3 67 ? 43.680 31.371 57.787 1.00 217.63 ? 1483 TYR C CE1 1 ATOM 12956 C CE2 . TYR C 3 67 ? 41.614 31.667 56.617 1.00 200.50 ? 1483 TYR C CE2 1 ATOM 12957 C CZ . TYR C 3 67 ? 42.719 30.899 56.916 1.00 208.36 ? 1483 TYR C CZ 1 ATOM 12958 O OH . TYR C 3 67 ? 42.863 29.656 56.343 1.00 199.39 ? 1483 TYR C OH 1 ATOM 12959 N N . THR C 3 68 ? 41.887 37.077 56.987 1.00 192.10 ? 1484 THR C N 1 ATOM 12960 C CA . THR C 3 68 ? 41.164 38.263 56.538 1.00 191.26 ? 1484 THR C CA 1 ATOM 12961 C C . THR C 3 68 ? 39.706 37.919 56.234 1.00 179.25 ? 1484 THR C C 1 ATOM 12962 O O . THR C 3 68 ? 39.423 36.996 55.471 1.00 177.37 ? 1484 THR C O 1 ATOM 12963 C CB . THR C 3 68 ? 41.819 38.883 55.288 1.00 182.18 ? 1484 THR C CB 1 ATOM 12964 O OG1 . THR C 3 68 ? 43.175 39.240 55.585 1.00 184.61 ? 1484 THR C OG1 1 ATOM 12965 C CG2 . THR C 3 68 ? 41.056 40.121 54.842 1.00 164.81 ? 1484 THR C CG2 1 ATOM 12966 N N . ILE C 3 69 ? 38.783 38.667 56.833 1.00 166.42 ? 1485 ILE C N 1 ATOM 12967 C CA . ILE C 3 69 ? 37.357 38.390 56.688 1.00 157.28 ? 1485 ILE C CA 1 ATOM 12968 C C . ILE C 3 69 ? 36.609 39.604 56.149 1.00 166.08 ? 1485 ILE C C 1 ATOM 12969 O O . ILE C 3 69 ? 36.741 40.705 56.679 1.00 181.38 ? 1485 ILE C O 1 ATOM 12970 C CB . ILE C 3 69 ? 36.717 37.969 58.030 1.00 164.72 ? 1485 ILE C CB 1 ATOM 12971 C CG1 . ILE C 3 69 ? 37.429 36.747 58.619 1.00 176.04 ? 1485 ILE C CG1 1 ATOM 12972 C CG2 . ILE C 3 69 ? 35.229 37.693 57.854 1.00 155.52 ? 1485 ILE C CG2 1 ATOM 12973 C CD1 . ILE C 3 69 ? 38.558 37.083 59.580 1.00 184.95 ? 1485 ILE C CD1 1 ATOM 12974 N N . THR C 3 70 ? 35.821 39.396 55.098 1.00 157.39 ? 1486 THR C N 1 ATOM 12975 C CA . THR C 3 70 ? 35.042 40.473 54.495 1.00 145.18 ? 1486 THR C CA 1 ATOM 12976 C C . THR C 3 70 ? 33.552 40.143 54.482 1.00 147.04 ? 1486 THR C C 1 ATOM 12977 O O . THR C 3 70 ? 33.168 38.983 54.334 1.00 153.12 ? 1486 THR C O 1 ATOM 12978 C CB . THR C 3 70 ? 35.498 40.763 53.055 1.00 145.83 ? 1486 THR C CB 1 ATOM 12979 O OG1 . THR C 3 70 ? 35.269 39.607 52.240 1.00 148.11 ? 1486 THR C OG1 1 ATOM 12980 C CG2 . THR C 3 70 ? 36.977 41.116 53.022 1.00 157.73 ? 1486 THR C CG2 1 ATOM 12981 N N . VAL C 3 71 ? 32.717 41.167 54.634 1.00 139.45 ? 1487 VAL C N 1 ATOM 12982 C CA . VAL C 3 71 ? 31.268 40.981 54.635 1.00 137.74 ? 1487 VAL C CA 1 ATOM 12983 C C . VAL C 3 71 ? 30.583 41.927 53.651 1.00 141.02 ? 1487 VAL C C 1 ATOM 12984 O O . VAL C 3 71 ? 30.711 43.146 53.753 1.00 145.92 ? 1487 VAL C O 1 ATOM 12985 C CB . VAL C 3 71 ? 30.668 41.199 56.041 1.00 138.27 ? 1487 VAL C CB 1 ATOM 12986 C CG1 . VAL C 3 71 ? 29.150 41.141 55.988 1.00 135.25 ? 1487 VAL C CG1 1 ATOM 12987 C CG2 . VAL C 3 71 ? 31.208 40.167 57.018 1.00 150.34 ? 1487 VAL C CG2 1 ATOM 12988 N N . TYR C 3 72 ? 29.855 41.351 52.699 1.00 145.00 ? 1488 TYR C N 1 ATOM 12989 C CA . TYR C 3 72 ? 29.142 42.128 51.690 1.00 125.98 ? 1488 TYR C CA 1 ATOM 12990 C C . TYR C 3 72 ? 27.651 42.215 52.007 1.00 125.30 ? 1488 TYR C C 1 ATOM 12991 O O . TYR C 3 72 ? 27.058 41.261 52.508 1.00 136.82 ? 1488 TYR C O 1 ATOM 12992 C CB . TYR C 3 72 ? 29.340 41.514 50.300 1.00 124.08 ? 1488 TYR C CB 1 ATOM 12993 C CG . TYR C 3 72 ? 30.769 41.526 49.803 1.00 125.03 ? 1488 TYR C CG 1 ATOM 12994 C CD1 . TYR C 3 72 ? 31.673 40.551 50.203 1.00 132.66 ? 1488 TYR C CD1 1 ATOM 12995 C CD2 . TYR C 3 72 ? 31.209 42.504 48.921 1.00 124.26 ? 1488 TYR C CD2 1 ATOM 12996 C CE1 . TYR C 3 72 ? 32.978 40.555 49.748 1.00 141.21 ? 1488 TYR C CE1 1 ATOM 12997 C CE2 . TYR C 3 72 ? 32.511 42.517 48.459 1.00 127.20 ? 1488 TYR C CE2 1 ATOM 12998 C CZ . TYR C 3 72 ? 33.391 41.540 48.876 1.00 142.21 ? 1488 TYR C CZ 1 ATOM 12999 O OH . TYR C 3 72 ? 34.689 41.548 48.421 1.00 160.05 ? 1488 TYR C OH 1 ATOM 13000 N N . ALA C 3 73 ? 27.051 43.363 51.714 1.00 124.76 ? 1489 ALA C N 1 ATOM 13001 C CA . ALA C 3 73 ? 25.611 43.537 51.867 1.00 124.68 ? 1489 ALA C CA 1 ATOM 13002 C C . ALA C 3 73 ? 24.916 43.330 50.525 1.00 137.66 ? 1489 ALA C C 1 ATOM 13003 O O . ALA C 3 73 ? 25.450 43.701 49.480 1.00 142.26 ? 1489 ALA C O 1 ATOM 13004 C CB . ALA C 3 73 ? 25.295 44.910 52.430 1.00 126.47 ? 1489 ALA C CB 1 ATOM 13005 N N . VAL C 3 74 ? 23.730 42.733 50.552 1.00 133.58 ? 1490 VAL C N 1 ATOM 13006 C CA . VAL C 3 74 ? 23.030 42.395 49.318 1.00 121.10 ? 1490 VAL C CA 1 ATOM 13007 C C . VAL C 3 74 ? 21.729 43.170 49.147 1.00 137.72 ? 1490 VAL C C 1 ATOM 13008 O O . VAL C 3 74 ? 20.785 42.999 49.918 1.00 131.10 ? 1490 VAL C O 1 ATOM 13009 C CB . VAL C 3 74 ? 22.724 40.897 49.256 1.00 120.46 ? 1490 VAL C CB 1 ATOM 13010 C CG1 . VAL C 3 74 ? 22.085 40.546 47.925 1.00 135.99 ? 1490 VAL C CG1 1 ATOM 13011 C CG2 . VAL C 3 74 ? 23.996 40.100 49.468 1.00 120.32 ? 1490 VAL C CG2 1 ATOM 13012 N N . THR C 3 75 ? 21.692 44.019 48.123 1.00 149.33 ? 1491 THR C N 1 ATOM 13013 C CA . THR C 3 75 ? 20.510 44.811 47.799 1.00 142.79 ? 1491 THR C CA 1 ATOM 13014 C C . THR C 3 75 ? 19.353 43.913 47.377 1.00 134.57 ? 1491 THR C C 1 ATOM 13015 O O . THR C 3 75 ? 19.525 43.027 46.540 1.00 132.22 ? 1491 THR C O 1 ATOM 13016 C CB . THR C 3 75 ? 20.805 45.825 46.669 1.00 143.14 ? 1491 THR C CB 1 ATOM 13017 O OG1 . THR C 3 75 ? 21.870 46.697 47.070 1.00 163.13 ? 1491 THR C OG1 1 ATOM 13018 C CG2 . THR C 3 75 ? 19.572 46.655 46.342 1.00 129.51 ? 1491 THR C CG2 1 ATOM 13019 N N . PRO C 3 76 ? 18.164 44.136 47.959 1.00 91.65 ? 1492 PRO C N 1 ATOM 13020 C CA . PRO C 3 76 ? 16.979 43.372 47.564 1.00 93.57 ? 1492 PRO C CA 1 ATOM 13021 C C . PRO C 3 76 ? 16.351 43.910 46.287 1.00 95.01 ? 1492 PRO C C 1 ATOM 13022 O O . PRO C 3 76 ? 15.146 44.149 46.259 1.00 93.07 ? 1492 PRO C O 1 ATOM 13023 C CB . PRO C 3 76 ? 16.035 43.572 48.745 1.00 81.63 ? 1492 PRO C CB 1 ATOM 13024 C CG . PRO C 3 76 ? 16.371 44.938 49.226 1.00 86.34 ? 1492 PRO C CG 1 ATOM 13025 C CD . PRO C 3 76 ? 17.868 45.067 49.062 1.00 87.94 ? 1492 PRO C CD 1 ATOM 13026 N N . ARG C 3 77 ? 17.161 44.098 45.249 1.00 91.39 ? 1493 ARG C N 1 ATOM 13027 C CA . ARG C 3 77 ? 16.676 44.578 43.961 1.00 82.45 ? 1493 ARG C CA 1 ATOM 13028 C C . ARG C 3 77 ? 17.429 43.866 42.845 1.00 84.07 ? 1493 ARG C C 1 ATOM 13029 O O . ARG C 3 77 ? 18.645 43.689 42.920 1.00 83.08 ? 1493 ARG C O 1 ATOM 13030 C CB . ARG C 3 77 ? 16.837 46.098 43.835 1.00 78.76 ? 1493 ARG C CB 1 ATOM 13031 C CG . ARG C 3 77 ? 16.145 46.898 44.933 1.00 83.08 ? 1493 ARG C CG 1 ATOM 13032 C CD . ARG C 3 77 ? 16.037 48.373 44.585 1.00 102.71 ? 1493 ARG C CD 1 ATOM 13033 N NE . ARG C 3 77 ? 14.948 48.633 43.648 1.00 98.41 ? 1493 ARG C NE 1 ATOM 13034 C CZ . ARG C 3 77 ? 14.665 49.832 43.151 1.00 108.21 ? 1493 ARG C CZ 1 ATOM 13035 N NH1 . ARG C 3 77 ? 15.398 50.881 43.493 1.00 107.31 ? 1493 ARG C NH1 1 ATOM 13036 N NH2 . ARG C 3 77 ? 13.656 49.980 42.304 1.00 123.77 ? 1493 ARG C NH2 1 ATOM 13037 N N . GLY C 3 78 ? 16.701 43.451 41.814 1.00 83.37 ? 1494 GLY C N 1 ATOM 13038 C CA . GLY C 3 78 ? 17.294 42.690 40.731 1.00 69.74 ? 1494 GLY C CA 1 ATOM 13039 C C . GLY C 3 78 ? 17.672 41.286 41.166 1.00 75.38 ? 1494 GLY C C 1 ATOM 13040 O O . GLY C 3 78 ? 17.195 40.792 42.190 1.00 74.33 ? 1494 GLY C O 1 ATOM 13041 N N . ASP C 3 79 ? 18.540 40.642 40.394 1.00 80.62 ? 1495 ASP C N 1 ATOM 13042 C CA . ASP C 3 79 ? 18.928 39.269 40.682 1.00 70.10 ? 1495 ASP C CA 1 ATOM 13043 C C . ASP C 3 79 ? 19.884 39.234 41.865 1.00 83.73 ? 1495 ASP C C 1 ATOM 13044 O O . ASP C 3 79 ? 19.513 38.805 42.957 1.00 90.52 ? 1495 ASP C O 1 ATOM 13045 C CB . ASP C 3 79 ? 19.570 38.626 39.452 1.00 69.82 ? 1495 ASP C CB 1 ATOM 13046 C CG . ASP C 3 79 ? 20.032 37.205 39.708 1.00 89.94 ? 1495 ASP C CG 1 ATOM 13047 O OD1 . ASP C 3 79 ? 19.349 36.481 40.466 1.00 89.24 ? 1495 ASP C OD1 1 ATOM 13048 O OD2 . ASP C 3 79 ? 21.078 36.814 39.146 1.00 80.54 ? 1495 ASP C OD2 1 ATOM 13049 N N . TRP C 3 80 ? 21.110 39.695 41.649 1.00 92.08 ? 1496 TRP C N 1 ATOM 13050 C CA . TRP C 3 80 ? 22.061 39.850 42.742 1.00 91.60 ? 1496 TRP C CA 1 ATOM 13051 C C . TRP C 3 80 ? 22.757 41.199 42.649 1.00 99.22 ? 1496 TRP C C 1 ATOM 13052 O O . TRP C 3 80 ? 23.508 41.456 41.708 1.00 105.77 ? 1496 TRP C O 1 ATOM 13053 C CB . TRP C 3 80 ? 23.090 38.721 42.731 1.00 93.09 ? 1496 TRP C CB 1 ATOM 13054 C CG . TRP C 3 80 ? 23.804 38.557 44.038 1.00 109.75 ? 1496 TRP C CG 1 ATOM 13055 C CD1 . TRP C 3 80 ? 25.009 39.091 44.388 1.00 116.43 ? 1496 TRP C CD1 1 ATOM 13056 C CD2 . TRP C 3 80 ? 23.353 37.808 45.172 1.00 112.70 ? 1496 TRP C CD2 1 ATOM 13057 N NE1 . TRP C 3 80 ? 25.339 38.718 45.669 1.00 113.46 ? 1496 TRP C NE1 1 ATOM 13058 C CE2 . TRP C 3 80 ? 24.337 37.931 46.173 1.00 116.07 ? 1496 TRP C CE2 1 ATOM 13059 C CE3 . TRP C 3 80 ? 22.212 37.044 45.438 1.00 107.91 ? 1496 TRP C CE3 1 ATOM 13060 C CZ2 . TRP C 3 80 ? 24.216 37.318 47.418 1.00 114.02 ? 1496 TRP C CZ2 1 ATOM 13061 C CZ3 . TRP C 3 80 ? 22.093 36.439 46.676 1.00 100.91 ? 1496 TRP C CZ3 1 ATOM 13062 C CH2 . TRP C 3 80 ? 23.089 36.580 47.650 1.00 98.44 ? 1496 TRP C CH2 1 ATOM 13063 N N . ASN C 3 81 ? 22.517 42.053 43.636 1.00 101.81 ? 1497 ASN C N 1 ATOM 13064 C CA . ASN C 3 81 ? 23.117 43.380 43.659 1.00 111.92 ? 1497 ASN C CA 1 ATOM 13065 C C . ASN C 3 81 ? 23.696 43.695 45.026 1.00 123.03 ? 1497 ASN C C 1 ATOM 13066 O O . ASN C 3 81 ? 23.023 43.548 46.045 1.00 115.69 ? 1497 ASN C O 1 ATOM 13067 C CB . ASN C 3 81 ? 22.092 44.442 43.260 1.00 103.18 ? 1497 ASN C CB 1 ATOM 13068 C CG . ASN C 3 81 ? 22.368 45.031 41.892 1.00 117.30 ? 1497 ASN C CG 1 ATOM 13069 O OD1 . ASN C 3 81 ? 22.795 46.179 41.775 1.00 141.40 ? 1497 ASN C OD1 1 ATOM 13070 N ND2 . ASN C 3 81 ? 22.137 44.243 40.847 1.00 103.49 ? 1497 ASN C ND2 1 ATOM 13071 N N . GLU C 3 82 ? 24.952 44.121 45.045 1.00 133.02 ? 1498 GLU C N 1 ATOM 13072 C CA . GLU C 3 82 ? 25.632 44.403 46.299 1.00 127.60 ? 1498 GLU C CA 1 ATOM 13073 C C . GLU C 3 82 ? 25.942 45.887 46.439 1.00 131.79 ? 1498 GLU C C 1 ATOM 13074 O O . GLU C 3 82 ? 26.117 46.596 45.446 1.00 138.60 ? 1498 GLU C O 1 ATOM 13075 C CB . GLU C 3 82 ? 26.914 43.575 46.408 1.00 118.88 ? 1498 GLU C CB 1 ATOM 13076 C CG . GLU C 3 82 ? 26.661 42.077 46.496 1.00 114.46 ? 1498 GLU C CG 1 ATOM 13077 C CD . GLU C 3 82 ? 27.940 41.265 46.529 1.00 122.94 ? 1498 GLU C CD 1 ATOM 13078 O OE1 . GLU C 3 82 ? 29.033 41.868 46.494 1.00 139.85 ? 1498 GLU C OE1 1 ATOM 13079 O OE2 . GLU C 3 82 ? 27.851 40.020 46.589 1.00 121.60 ? 1498 GLU C OE2 1 ATOM 13080 N N . GLY C 3 83 ? 25.998 46.348 47.683 1.00 124.40 ? 1499 GLY C N 1 ATOM 13081 C CA . GLY C 3 83 ? 26.282 47.739 47.975 1.00 135.66 ? 1499 GLY C CA 1 ATOM 13082 C C . GLY C 3 83 ? 27.683 48.139 47.563 1.00 144.55 ? 1499 GLY C C 1 ATOM 13083 O O . GLY C 3 83 ? 28.485 47.304 47.143 1.00 145.69 ? 1499 GLY C O 1 ATOM 13084 N N . SER C 3 84 ? 27.979 49.427 47.684 1.00 137.72 ? 1500 SER C N 1 ATOM 13085 C CA . SER C 3 84 ? 29.262 49.955 47.251 1.00 132.65 ? 1500 SER C CA 1 ATOM 13086 C C . SER C 3 84 ? 30.374 49.666 48.253 1.00 138.15 ? 1500 SER C C 1 ATOM 13087 O O . SER C 3 84 ? 31.540 49.555 47.877 1.00 144.90 ? 1500 SER C O 1 ATOM 13088 C CB . SER C 3 84 ? 29.154 51.462 47.015 1.00 156.15 ? 1500 SER C CB 1 ATOM 13089 O OG . SER C 3 84 ? 28.623 52.116 48.154 1.00 175.51 ? 1500 SER C OG 1 ATOM 13090 N N . LYS C 3 85 ? 30.009 49.529 49.524 1.00 150.27 ? 1501 LYS C N 1 ATOM 13091 C CA . LYS C 3 85 ? 30.998 49.497 50.599 1.00 169.10 ? 1501 LYS C CA 1 ATOM 13092 C C . LYS C 3 85 ? 30.916 48.260 51.496 1.00 165.70 ? 1501 LYS C C 1 ATOM 13093 O O . LYS C 3 85 ? 30.165 48.245 52.472 1.00 166.13 ? 1501 LYS C O 1 ATOM 13094 C CB . LYS C 3 85 ? 30.863 50.757 51.461 1.00 178.29 ? 1501 LYS C CB 1 ATOM 13095 C CG . LYS C 3 85 ? 31.160 52.056 50.721 1.00 180.70 ? 1501 LYS C CG 1 ATOM 13096 C CD . LYS C 3 85 ? 30.127 53.130 51.038 1.00 178.23 ? 1501 LYS C CD 1 ATOM 13097 C CE . LYS C 3 85 ? 30.077 53.442 52.525 1.00 175.31 ? 1501 LYS C CE 1 ATOM 13098 N NZ . LYS C 3 85 ? 28.995 54.414 52.848 1.00 168.17 ? 1501 LYS C NZ 1 ATOM 13099 N N . PRO C 3 86 ? 31.688 47.213 51.160 1.00 154.17 ? 1502 PRO C N 1 ATOM 13100 C CA . PRO C 3 86 ? 31.872 46.054 52.043 1.00 137.26 ? 1502 PRO C CA 1 ATOM 13101 C C . PRO C 3 86 ? 32.828 46.362 53.200 1.00 153.10 ? 1502 PRO C C 1 ATOM 13102 O O . PRO C 3 86 ? 33.672 47.248 53.068 1.00 168.50 ? 1502 PRO C O 1 ATOM 13103 C CB . PRO C 3 86 ? 32.461 44.996 51.109 1.00 126.46 ? 1502 PRO C CB 1 ATOM 13104 C CG . PRO C 3 86 ? 33.166 45.783 50.059 1.00 129.25 ? 1502 PRO C CG 1 ATOM 13105 C CD . PRO C 3 86 ? 32.339 47.019 49.852 1.00 141.64 ? 1502 PRO C CD 1 ATOM 13106 N N . ILE C 3 87 ? 32.699 45.639 54.311 1.00 148.63 ? 1503 ILE C N 1 ATOM 13107 C CA . ILE C 3 87 ? 33.510 45.901 55.502 1.00 151.43 ? 1503 ILE C CA 1 ATOM 13108 C C . ILE C 3 87 ? 34.382 44.697 55.868 1.00 140.21 ? 1503 ILE C C 1 ATOM 13109 O O . ILE C 3 87 ? 33.958 43.551 55.724 1.00 136.50 ? 1503 ILE C O 1 ATOM 13110 C CB . ILE C 3 87 ? 32.620 46.278 56.707 1.00 159.49 ? 1503 ILE C CB 1 ATOM 13111 C CG1 . ILE C 3 87 ? 31.693 47.434 56.336 1.00 174.07 ? 1503 ILE C CG1 1 ATOM 13112 C CG2 . ILE C 3 87 ? 33.465 46.683 57.904 1.00 156.10 ? 1503 ILE C CG2 1 ATOM 13113 C CD1 . ILE C 3 87 ? 32.430 48.733 56.061 1.00 175.48 ? 1503 ILE C CD1 1 ATOM 13114 N N . SER C 3 88 ? 35.599 44.963 56.339 1.00 147.39 ? 1504 SER C N 1 ATOM 13115 C CA . SER C 3 88 ? 36.536 43.896 56.679 1.00 155.15 ? 1504 SER C CA 1 ATOM 13116 C C . SER C 3 88 ? 37.306 44.150 57.977 1.00 171.71 ? 1504 SER C C 1 ATOM 13117 O O . SER C 3 88 ? 37.455 45.291 58.416 1.00 185.33 ? 1504 SER C O 1 ATOM 13118 C CB . SER C 3 88 ? 37.528 43.687 55.532 1.00 153.89 ? 1504 SER C CB 1 ATOM 13119 O OG . SER C 3 88 ? 38.467 42.672 55.846 1.00 161.28 ? 1504 SER C OG 1 ATOM 13120 N N . ILE C 3 89 ? 37.787 43.068 58.584 1.00 166.66 ? 1505 ILE C N 1 ATOM 13121 C CA . ILE C 3 89 ? 38.665 43.142 59.748 1.00 173.49 ? 1505 ILE C CA 1 ATOM 13122 C C . ILE C 3 89 ? 39.590 41.926 59.750 1.00 173.93 ? 1505 ILE C C 1 ATOM 13123 O O . ILE C 3 89 ? 39.209 40.852 59.282 1.00 148.05 ? 1505 ILE C O 1 ATOM 13124 C CB . ILE C 3 89 ? 37.866 43.208 61.074 1.00 177.87 ? 1505 ILE C CB 1 ATOM 13125 C CG1 . ILE C 3 89 ? 38.788 43.537 62.253 1.00 184.21 ? 1505 ILE C CG1 1 ATOM 13126 C CG2 . ILE C 3 89 ? 37.113 41.906 61.322 1.00 148.16 ? 1505 ILE C CG2 1 ATOM 13127 C CD1 . ILE C 3 89 ? 39.541 44.848 62.108 1.00 175.28 ? 1505 ILE C CD1 1 ATOM 13128 N N . ASN C 3 90 ? 40.809 42.097 60.253 1.00 175.39 ? 1506 ASN C N 1 ATOM 13129 C CA . ASN C 3 90 ? 41.757 40.991 60.303 1.00 164.33 ? 1506 ASN C CA 1 ATOM 13130 C C . ASN C 3 90 ? 41.821 40.342 61.678 1.00 172.07 ? 1506 ASN C C 1 ATOM 13131 O O . ASN C 3 90 ? 41.214 40.826 62.635 1.00 176.52 ? 1506 ASN C O 1 ATOM 13132 C CB . ASN C 3 90 ? 43.153 41.468 59.900 1.00 166.71 ? 1506 ASN C CB 1 ATOM 13133 C CG . ASN C 3 90 ? 43.183 42.083 58.516 1.00 167.18 ? 1506 ASN C CG 1 ATOM 13134 O OD1 . ASN C 3 90 ? 42.386 41.729 57.649 1.00 166.17 ? 1506 ASN C OD1 1 ATOM 13135 N ND2 . ASN C 3 90 ? 44.109 43.011 58.303 1.00 172.38 ? 1506 ASN C ND2 1 ATOM 13136 N N . TYR C 3 91 ? 42.594 39.261 61.761 1.00 184.37 ? 1507 TYR C N 1 ATOM 13137 C CA . TYR C 3 91 ? 42.815 38.514 62.996 1.00 192.61 ? 1507 TYR C CA 1 ATOM 13138 C C . TYR C 3 91 ? 43.760 37.350 62.733 1.00 190.04 ? 1507 TYR C C 1 ATOM 13139 O O . TYR C 3 91 ? 43.428 36.436 61.979 1.00 177.79 ? 1507 TYR C O 1 ATOM 13140 C CB . TYR C 3 91 ? 41.501 37.989 63.581 1.00 175.22 ? 1507 TYR C CB 1 ATOM 13141 C CG . TYR C 3 91 ? 41.708 37.014 64.714 1.00 170.33 ? 1507 TYR C CG 1 ATOM 13142 C CD1 . TYR C 3 91 ? 42.446 37.371 65.836 1.00 174.74 ? 1507 TYR C CD1 1 ATOM 13143 C CD2 . TYR C 3 91 ? 41.169 35.737 64.664 1.00 156.18 ? 1507 TYR C CD2 1 ATOM 13144 C CE1 . TYR C 3 91 ? 42.642 36.483 66.873 1.00 184.30 ? 1507 TYR C CE1 1 ATOM 13145 C CE2 . TYR C 3 91 ? 41.358 34.841 65.697 1.00 162.70 ? 1507 TYR C CE2 1 ATOM 13146 C CZ . TYR C 3 91 ? 42.096 35.220 66.799 1.00 191.29 ? 1507 TYR C CZ 1 ATOM 13147 O OH . TYR C 3 91 ? 42.288 34.331 67.832 1.00 206.83 ? 1507 TYR C OH 1 HETATM 13148 C C1 . NAG D 4 . ? 22.409 44.626 7.615 1.00 61.80 ? 1001 NAG A C1 1 HETATM 13149 C C2 . NAG D 4 . ? 21.600 43.336 7.490 1.00 78.54 ? 1001 NAG A C2 1 HETATM 13150 C C3 . NAG D 4 . ? 22.184 42.259 8.405 1.00 95.84 ? 1001 NAG A C3 1 HETATM 13151 C C4 . NAG D 4 . ? 23.686 42.106 8.188 1.00 107.24 ? 1001 NAG A C4 1 HETATM 13152 C C5 . NAG D 4 . ? 24.382 43.465 8.239 1.00 103.47 ? 1001 NAG A C5 1 HETATM 13153 C C6 . NAG D 4 . ? 25.848 43.400 7.874 1.00 121.53 ? 1001 NAG A C6 1 HETATM 13154 C C7 . NAG D 4 . ? 19.289 43.930 6.897 1.00 85.15 ? 1001 NAG A C7 1 HETATM 13155 C C8 . NAG D 4 . ? 17.892 44.123 7.407 1.00 60.20 ? 1001 NAG A C8 1 HETATM 13156 N N2 . NAG D 4 . ? 20.199 43.567 7.808 1.00 67.28 ? 1001 NAG A N2 1 HETATM 13157 O O3 . NAG D 4 . ? 21.530 41.020 8.159 1.00 99.70 ? 1001 NAG A O3 1 HETATM 13158 O O4 . NAG D 4 . ? 24.227 41.283 9.216 1.00 106.06 ? 1001 NAG A O4 1 HETATM 13159 O O5 . NAG D 4 . ? 23.767 44.366 7.308 1.00 80.26 ? 1001 NAG A O5 1 HETATM 13160 O O6 . NAG D 4 . ? 26.615 42.802 8.910 1.00 133.09 ? 1001 NAG A O6 1 HETATM 13161 O O7 . NAG D 4 . ? 19.580 44.095 5.716 1.00 107.85 ? 1001 NAG A O7 1 HETATM 13162 C C1 . NAG E 4 . ? 24.811 40.090 8.661 1.00 116.75 ? 1002 NAG A C1 1 HETATM 13163 C C2 . NAG E 4 . ? 25.530 39.330 9.775 1.00 124.45 ? 1002 NAG A C2 1 HETATM 13164 C C3 . NAG E 4 . ? 26.153 38.047 9.225 1.00 141.58 ? 1002 NAG A C3 1 HETATM 13165 C C4 . NAG E 4 . ? 25.112 37.225 8.476 1.00 140.45 ? 1002 NAG A C4 1 HETATM 13166 C C5 . NAG E 4 . ? 24.425 38.087 7.421 1.00 134.88 ? 1002 NAG A C5 1 HETATM 13167 C C6 . NAG E 4 . ? 23.304 37.369 6.707 1.00 138.84 ? 1002 NAG A C6 1 HETATM 13168 C C7 . NAG E 4 . ? 26.981 39.974 11.649 1.00 150.30 ? 1002 NAG A C7 1 HETATM 13169 C C8 . NAG E 4 . ? 28.032 40.929 12.129 1.00 146.36 ? 1002 NAG A C8 1 HETATM 13170 N N2 . NAG E 4 . ? 26.544 40.164 10.399 1.00 129.58 ? 1002 NAG A N2 1 HETATM 13171 O O3 . NAG E 4 . ? 26.694 37.279 10.294 1.00 147.31 ? 1002 NAG A O3 1 HETATM 13172 O O4 . NAG E 4 . ? 25.734 36.110 7.848 1.00 144.73 ? 1002 NAG A O4 1 HETATM 13173 O O5 . NAG E 4 . ? 23.846 39.241 8.046 1.00 127.55 ? 1002 NAG A O5 1 HETATM 13174 O O6 . NAG E 4 . ? 22.094 37.436 7.448 1.00 148.41 ? 1002 NAG A O6 1 HETATM 13175 O O7 . NAG E 4 . ? 26.549 39.071 12.359 1.00 164.37 ? 1002 NAG A O7 1 HETATM 13176 C C1 . NAG F 4 . ? -2.815 68.611 41.144 1.00 84.13 ? 1003 NAG A C1 1 HETATM 13177 C C2 . NAG F 4 . ? -3.088 69.260 42.501 1.00 86.75 ? 1003 NAG A C2 1 HETATM 13178 C C3 . NAG F 4 . ? -4.586 69.330 42.756 1.00 100.82 ? 1003 NAG A C3 1 HETATM 13179 C C4 . NAG F 4 . ? -5.243 70.233 41.723 1.00 113.84 ? 1003 NAG A C4 1 HETATM 13180 C C5 . NAG F 4 . ? -4.834 69.814 40.310 1.00 120.27 ? 1003 NAG A C5 1 HETATM 13181 C C6 . NAG F 4 . ? -4.041 70.863 39.564 1.00 128.00 ? 1003 NAG A C6 1 HETATM 13182 C C7 . NAG F 4 . ? -1.093 68.551 43.741 1.00 121.55 ? 1003 NAG A C7 1 HETATM 13183 C C8 . NAG F 4 . ? -0.572 67.746 44.894 1.00 134.10 ? 1003 NAG A C8 1 HETATM 13184 N N2 . NAG F 4 . ? -2.419 68.536 43.569 1.00 112.74 ? 1003 NAG A N2 1 HETATM 13185 O O3 . NAG F 4 . ? -4.825 69.831 44.067 1.00 95.70 ? 1003 NAG A O3 1 HETATM 13186 O O4 . NAG F 4 . ? -6.659 70.163 41.845 1.00 100.77 ? 1003 NAG A O4 1 HETATM 13187 O O5 . NAG F 4 . ? -4.047 68.608 40.331 1.00 114.95 ? 1003 NAG A O5 1 HETATM 13188 O O6 . NAG F 4 . ? -4.296 70.800 38.168 1.00 121.56 ? 1003 NAG A O6 1 HETATM 13189 O O7 . NAG F 4 . ? -0.348 69.186 43.000 1.00 94.00 ? 1003 NAG A O7 1 HETATM 13190 C C1 . NAG G 4 . ? -3.169 54.139 41.403 1.00 55.92 ? 1004 NAG A C1 1 HETATM 13191 C C2 . NAG G 4 . ? -3.311 54.939 42.693 1.00 69.47 ? 1004 NAG A C2 1 HETATM 13192 C C3 . NAG G 4 . ? -1.950 55.464 43.145 1.00 66.52 ? 1004 NAG A C3 1 HETATM 13193 C C4 . NAG G 4 . ? -0.917 54.344 43.190 1.00 53.75 ? 1004 NAG A C4 1 HETATM 13194 C C5 . NAG G 4 . ? -0.921 53.559 41.882 1.00 69.65 ? 1004 NAG A C5 1 HETATM 13195 C C6 . NAG G 4 . ? -0.031 52.339 41.923 1.00 63.17 ? 1004 NAG A C6 1 HETATM 13196 C C7 . NAG G 4 . ? -5.572 55.902 42.675 1.00 103.01 ? 1004 NAG A C7 1 HETATM 13197 C C8 . NAG G 4 . ? -6.387 57.141 42.462 1.00 117.97 ? 1004 NAG A C8 1 HETATM 13198 N N2 . NAG G 4 . ? -4.250 56.036 42.523 1.00 78.06 ? 1004 NAG A N2 1 HETATM 13199 O O3 . NAG G 4 . ? -2.082 56.043 44.438 1.00 90.88 ? 1004 NAG A O3 1 HETATM 13200 O O4 . NAG G 4 . ? 0.380 54.904 43.356 1.00 71.32 ? 1004 NAG A O4 1 HETATM 13201 O O5 . NAG G 4 . ? -2.246 53.094 41.595 1.00 63.60 ? 1004 NAG A O5 1 HETATM 13202 O O6 . NAG G 4 . ? 0.123 51.855 43.249 1.00 62.75 ? 1004 NAG A O6 1 HETATM 13203 O O7 . NAG G 4 . ? -6.087 54.827 42.968 1.00 118.12 ? 1004 NAG A O7 1 HETATM 13204 C C1 . NAG H 4 . ? 0.888 54.633 44.670 1.00 64.02 ? 1005 NAG A C1 1 HETATM 13205 C C2 . NAG H 4 . ? 2.391 54.912 44.696 1.00 56.20 ? 1005 NAG A C2 1 HETATM 13206 C C3 . NAG H 4 . ? 2.946 54.670 46.096 1.00 69.35 ? 1005 NAG A C3 1 HETATM 13207 C C4 . NAG H 4 . ? 2.161 55.475 47.123 1.00 73.54 ? 1005 NAG A C4 1 HETATM 13208 C C5 . NAG H 4 . ? 0.671 55.171 46.996 1.00 85.68 ? 1005 NAG A C5 1 HETATM 13209 C C6 . NAG H 4 . ? -0.186 56.020 47.906 1.00 97.31 ? 1005 NAG A C6 1 HETATM 13210 C C7 . NAG H 4 . ? 3.354 54.510 42.473 1.00 70.51 ? 1005 NAG A C7 1 HETATM 13211 C C8 . NAG H 4 . ? 4.102 53.544 41.605 1.00 69.81 ? 1005 NAG A C8 1 HETATM 13212 N N2 . NAG H 4 . ? 3.099 54.100 43.720 1.00 46.81 ? 1005 NAG A N2 1 HETATM 13213 O O3 . NAG H 4 . ? 4.322 55.028 46.130 1.00 77.61 ? 1005 NAG A O3 1 HETATM 13214 O O4 . NAG H 4 . ? 2.595 55.142 48.436 1.00 92.65 ? 1005 NAG A O4 1 HETATM 13215 O O5 . NAG H 4 . ? 0.234 55.434 45.654 1.00 81.98 ? 1005 NAG A O5 1 HETATM 13216 O O6 . NAG H 4 . ? 0.289 57.358 47.959 1.00 115.18 ? 1005 NAG A O6 1 HETATM 13217 O O7 . NAG H 4 . ? 2.994 55.610 42.061 1.00 90.51 ? 1005 NAG A O7 1 HETATM 13218 C C1 . BMA I 5 . ? 3.280 56.273 49.001 1.00 116.24 ? 1006 BMA A C1 1 HETATM 13219 C C2 . BMA I 5 . ? 3.098 56.262 50.518 1.00 123.19 ? 1006 BMA A C2 1 HETATM 13220 C C3 . BMA I 5 . ? 3.842 57.447 51.120 1.00 132.50 ? 1006 BMA A C3 1 HETATM 13221 C C4 . BMA I 5 . ? 5.302 57.505 50.629 1.00 123.13 ? 1006 BMA A C4 1 HETATM 13222 C C5 . BMA I 5 . ? 5.367 57.452 49.084 1.00 117.81 ? 1006 BMA A C5 1 HETATM 13223 C C6 . BMA I 5 . ? 6.782 57.307 48.522 1.00 129.98 ? 1006 BMA A C6 1 HETATM 13224 O O2 . BMA I 5 . ? 3.667 55.087 51.090 1.00 107.82 ? 1006 BMA A O2 1 HETATM 13225 O O3 . BMA I 5 . ? 3.803 57.413 52.544 1.00 142.19 ? 1006 BMA A O3 1 HETATM 13226 O O4 . BMA I 5 . ? 5.915 58.697 51.087 1.00 121.89 ? 1006 BMA A O4 1 HETATM 13227 O O5 . BMA I 5 . ? 4.635 56.301 48.633 1.00 126.11 ? 1006 BMA A O5 1 HETATM 13228 O O6 . BMA I 5 . ? 7.668 58.259 49.115 1.00 145.21 ? 1006 BMA A O6 1 HETATM 13229 C C1 . MAN J 6 . ? 2.450 57.642 52.979 1.00 142.76 ? 1007 MAN A C1 1 HETATM 13230 C C2 . MAN J 6 . ? 2.306 59.101 53.448 1.00 152.27 ? 1007 MAN A C2 1 HETATM 13231 C C3 . MAN J 6 . ? 2.979 59.288 54.809 1.00 151.78 ? 1007 MAN A C3 1 HETATM 13232 C C4 . MAN J 6 . ? 2.524 58.207 55.809 1.00 155.06 ? 1007 MAN A C4 1 HETATM 13233 C C5 . MAN J 6 . ? 2.743 56.805 55.210 1.00 148.23 ? 1007 MAN A C5 1 HETATM 13234 C C6 . MAN J 6 . ? 2.224 55.691 56.102 1.00 145.24 ? 1007 MAN A C6 1 HETATM 13235 O O2 . MAN J 6 . ? 0.934 59.450 53.651 1.00 162.02 ? 1007 MAN A O2 1 HETATM 13236 O O3 . MAN J 6 . ? 2.734 60.590 55.341 1.00 137.70 ? 1007 MAN A O3 1 HETATM 13237 O O4 . MAN J 6 . ? 3.262 58.324 57.014 1.00 156.21 ? 1007 MAN A O4 1 HETATM 13238 O O5 . MAN J 6 . ? 2.044 56.714 53.950 1.00 139.75 ? 1007 MAN A O5 1 HETATM 13239 O O6 . MAN J 6 . ? 2.195 54.487 55.341 1.00 145.82 ? 1007 MAN A O6 1 HETATM 13240 C C1 . BMA K 5 . ? 8.735 57.555 49.788 1.00 150.68 ? 1008 BMA A C1 1 HETATM 13241 C C2 . BMA K 5 . ? 9.380 56.475 48.917 1.00 146.89 ? 1008 BMA A C2 1 HETATM 13242 C C3 . BMA K 5 . ? 10.258 55.574 49.802 1.00 140.65 ? 1008 BMA A C3 1 HETATM 13243 C C4 . BMA K 5 . ? 10.508 56.154 51.233 1.00 152.75 ? 1008 BMA A C4 1 HETATM 13244 C C5 . BMA K 5 . ? 10.641 57.726 51.259 1.00 158.82 ? 1008 BMA A C5 1 HETATM 13245 C C6 . BMA K 5 . ? 12.062 58.217 50.991 1.00 149.91 ? 1008 BMA A C6 1 HETATM 13246 O O2 . BMA K 5 . ? 10.239 57.056 47.949 1.00 149.15 ? 1008 BMA A O2 1 HETATM 13247 O O3 . BMA K 5 . ? 11.495 55.251 49.171 1.00 135.51 ? 1008 BMA A O3 1 HETATM 13248 O O4 . BMA K 5 . ? 9.449 55.720 52.094 1.00 154.19 ? 1008 BMA A O4 1 HETATM 13249 O O5 . BMA K 5 . ? 9.737 58.385 50.316 1.00 159.75 ? 1008 BMA A O5 1 HETATM 13250 O O6 . BMA K 5 . ? 12.307 58.160 49.587 1.00 140.05 ? 1008 BMA A O6 1 HETATM 13251 C C1 . MAN L 6 . ? 9.856 55.398 53.438 1.00 160.20 ? 1009 MAN A C1 1 HETATM 13252 C C2 . MAN L 6 . ? 11.205 54.634 53.486 1.00 158.80 ? 1009 MAN A C2 1 HETATM 13253 C C3 . MAN L 6 . ? 11.033 53.155 53.070 1.00 158.40 ? 1009 MAN A C3 1 HETATM 13254 C C4 . MAN L 6 . ? 9.777 52.518 53.699 1.00 162.32 ? 1009 MAN A C4 1 HETATM 13255 C C5 . MAN L 6 . ? 8.568 53.422 53.435 1.00 164.49 ? 1009 MAN A C5 1 HETATM 13256 C C6 . MAN L 6 . ? 7.264 52.885 53.991 1.00 166.85 ? 1009 MAN A C6 1 HETATM 13257 O O2 . MAN L 6 . ? 11.733 54.603 54.817 1.00 154.62 ? 1009 MAN A O2 1 HETATM 13258 O O3 . MAN L 6 . ? 12.188 52.382 53.383 1.00 153.21 ? 1009 MAN A O3 1 HETATM 13259 O O4 . MAN L 6 . ? 9.549 51.240 53.128 1.00 155.62 ? 1009 MAN A O4 1 HETATM 13260 O O5 . MAN L 6 . ? 8.828 54.691 54.057 1.00 161.25 ? 1009 MAN A O5 1 HETATM 13261 O O6 . MAN L 6 . ? 6.195 53.578 53.347 1.00 164.42 ? 1009 MAN A O6 1 HETATM 13262 C C1 . NAG M 4 . ? -62.399 50.428 -10.358 1.00 98.77 ? 1010 NAG A C1 1 HETATM 13263 C C2 . NAG M 4 . ? -62.180 51.214 -9.050 1.00 121.76 ? 1010 NAG A C2 1 HETATM 13264 C C3 . NAG M 4 . ? -61.690 52.642 -9.333 1.00 129.47 ? 1010 NAG A C3 1 HETATM 13265 C C4 . NAG M 4 . ? -60.494 52.617 -10.277 1.00 139.72 ? 1010 NAG A C4 1 HETATM 13266 C C5 . NAG M 4 . ? -60.852 51.834 -11.534 1.00 136.90 ? 1010 NAG A C5 1 HETATM 13267 C C6 . NAG M 4 . ? -59.702 51.702 -12.505 1.00 130.19 ? 1010 NAG A C6 1 HETATM 13268 C C7 . NAG M 4 . ? -64.574 51.701 -8.350 1.00 139.54 ? 1010 NAG A C7 1 HETATM 13269 C C8 . NAG M 4 . ? -64.860 52.380 -9.667 1.00 134.82 ? 1010 NAG A C8 1 HETATM 13270 N N2 . NAG M 4 . ? -63.336 51.198 -8.152 1.00 132.08 ? 1010 NAG A N2 1 HETATM 13271 O O3 . NAG M 4 . ? -61.342 53.285 -8.112 1.00 132.34 ? 1010 NAG A O3 1 HETATM 13272 O O4 . NAG M 4 . ? -60.110 53.940 -10.633 1.00 154.98 ? 1010 NAG A O4 1 HETATM 13273 O O5 . NAG M 4 . ? -61.229 50.502 -11.165 1.00 122.76 ? 1010 NAG A O5 1 HETATM 13274 O O6 . NAG M 4 . ? -58.613 50.998 -11.922 1.00 120.31 ? 1010 NAG A O6 1 HETATM 13275 O O7 . NAG M 4 . ? -65.440 51.607 -7.485 1.00 143.07 ? 1010 NAG A O7 1 HETATM 13276 C C1 . NAG N 4 . ? -58.792 54.171 -10.103 1.00 163.53 ? 1011 NAG A C1 1 HETATM 13277 C C2 . NAG N 4 . ? -57.997 55.078 -11.046 1.00 160.06 ? 1011 NAG A C2 1 HETATM 13278 C C3 . NAG N 4 . ? -56.606 55.345 -10.474 1.00 164.38 ? 1011 NAG A C3 1 HETATM 13279 C C4 . NAG N 4 . ? -56.708 55.867 -9.047 1.00 171.40 ? 1011 NAG A C4 1 HETATM 13280 C C5 . NAG N 4 . ? -57.545 54.911 -8.203 1.00 162.73 ? 1011 NAG A C5 1 HETATM 13281 C C6 . NAG N 4 . ? -57.775 55.404 -6.794 1.00 156.35 ? 1011 NAG A C6 1 HETATM 13282 C C7 . NAG N 4 . ? -58.598 54.926 -13.427 1.00 136.85 ? 1011 NAG A C7 1 HETATM 13283 C C8 . NAG N 4 . ? -59.523 56.079 -13.175 1.00 124.70 ? 1011 NAG A C8 1 HETATM 13284 N N2 . NAG N 4 . ? -57.897 54.492 -12.373 1.00 150.03 ? 1011 NAG A N2 1 HETATM 13285 O O3 . NAG N 4 . ? -55.930 56.292 -11.294 1.00 161.21 ? 1011 NAG A O3 1 HETATM 13286 O O4 . NAG N 4 . ? -55.409 55.988 -8.478 1.00 183.49 ? 1011 NAG A O4 1 HETATM 13287 O O5 . NAG N 4 . ? -58.839 54.754 -8.803 1.00 167.26 ? 1011 NAG A O5 1 HETATM 13288 O O6 . NAG N 4 . ? -58.530 54.470 -6.035 1.00 146.47 ? 1011 NAG A O6 1 HETATM 13289 O O7 . NAG N 4 . ? -58.490 54.409 -14.535 1.00 137.45 ? 1011 NAG A O7 1 HETATM 13290 C C1 . NAG O 4 . ? -35.177 41.864 2.053 1.00 116.13 ? 1012 NAG A C1 1 HETATM 13291 C C2 . NAG O 4 . ? -34.108 40.773 1.868 1.00 140.10 ? 1012 NAG A C2 1 HETATM 13292 C C3 . NAG O 4 . ? -34.078 39.818 3.070 1.00 145.63 ? 1012 NAG A C3 1 HETATM 13293 C C4 . NAG O 4 . ? -33.983 40.603 4.371 1.00 145.99 ? 1012 NAG A C4 1 HETATM 13294 C C5 . NAG O 4 . ? -35.078 41.667 4.427 1.00 141.66 ? 1012 NAG A C5 1 HETATM 13295 C C6 . NAG O 4 . ? -34.993 42.545 5.653 1.00 155.45 ? 1012 NAG A C6 1 HETATM 13296 C C7 . NAG O 4 . ? -35.220 39.305 0.117 1.00 140.00 ? 1012 NAG A C7 1 HETATM 13297 C C8 . NAG O 4 . ? -36.447 39.144 0.979 1.00 117.94 ? 1012 NAG A C8 1 HETATM 13298 N N2 . NAG O 4 . ? -34.204 40.057 0.597 1.00 144.35 ? 1012 NAG A N2 1 HETATM 13299 O O3 . NAG O 4 . ? -32.966 38.938 2.951 1.00 141.12 ? 1012 NAG A O3 1 HETATM 13300 O O4 . NAG O 4 . ? -34.118 39.725 5.483 1.00 144.32 ? 1012 NAG A O4 1 HETATM 13301 O O5 . NAG O 4 . ? -34.970 42.537 3.290 1.00 128.85 ? 1012 NAG A O5 1 HETATM 13302 O O6 . NAG O 4 . ? -35.525 43.838 5.401 1.00 157.06 ? 1012 NAG A O6 1 HETATM 13303 O O7 . NAG O 4 . ? -35.143 38.768 -0.983 1.00 146.52 ? 1012 NAG A O7 1 HETATM 13304 C C1 . NAG P 4 . ? -28.934 40.224 95.621 1.00 129.30 ? 1013 NAG A C1 1 HETATM 13305 C C2 . NAG P 4 . ? -29.687 39.782 96.877 1.00 148.93 ? 1013 NAG A C2 1 HETATM 13306 C C3 . NAG P 4 . ? -30.622 40.893 97.351 1.00 154.78 ? 1013 NAG A C3 1 HETATM 13307 C C4 . NAG P 4 . ? -29.852 42.195 97.530 1.00 161.89 ? 1013 NAG A C4 1 HETATM 13308 C C5 . NAG P 4 . ? -29.109 42.539 96.242 1.00 156.70 ? 1013 NAG A C5 1 HETATM 13309 C C6 . NAG P 4 . ? -28.237 43.767 96.371 1.00 156.08 ? 1013 NAG A C6 1 HETATM 13310 C C7 . NAG P 4 . ? -30.070 37.370 97.139 1.00 154.01 ? 1013 NAG A C7 1 HETATM 13311 C C8 . NAG P 4 . ? -30.955 36.211 96.789 1.00 151.76 ? 1013 NAG A C8 1 HETATM 13312 N N2 . NAG P 4 . ? -30.431 38.556 96.637 1.00 158.30 ? 1013 NAG A N2 1 HETATM 13313 O O3 . NAG P 4 . ? -31.232 40.513 98.580 1.00 157.81 ? 1013 NAG A O3 1 HETATM 13314 O O4 . NAG P 4 . ? -30.745 43.252 97.859 1.00 171.68 ? 1013 NAG A O4 1 HETATM 13315 O O5 . NAG P 4 . ? -28.244 41.453 95.880 1.00 147.39 ? 1013 NAG A O5 1 HETATM 13316 O O6 . NAG P 4 . ? -28.804 44.717 97.263 1.00 154.30 ? 1013 NAG A O6 1 HETATM 13317 O O7 . NAG P 4 . ? -29.073 37.238 97.842 1.00 148.70 ? 1013 NAG A O7 1 HETATM 13318 C C1 . NAG Q 4 . ? -24.747 53.786 62.866 1.00 103.48 ? 1014 NAG A C1 1 HETATM 13319 C C2 . NAG Q 4 . ? -25.820 54.204 61.853 1.00 117.90 ? 1014 NAG A C2 1 HETATM 13320 C C3 . NAG Q 4 . ? -25.278 55.256 60.882 1.00 119.41 ? 1014 NAG A C3 1 HETATM 13321 C C4 . NAG Q 4 . ? -24.637 56.409 61.647 1.00 137.05 ? 1014 NAG A C4 1 HETATM 13322 C C5 . NAG Q 4 . ? -23.583 55.866 62.603 1.00 123.19 ? 1014 NAG A C5 1 HETATM 13323 C C6 . NAG Q 4 . ? -22.932 56.938 63.446 1.00 126.59 ? 1014 NAG A C6 1 HETATM 13324 C C7 . NAG Q 4 . ? -27.590 52.630 61.199 1.00 116.14 ? 1014 NAG A C7 1 HETATM 13325 C C8 . NAG Q 4 . ? -27.930 51.418 60.383 1.00 101.33 ? 1014 NAG A C8 1 HETATM 13326 N N2 . NAG Q 4 . ? -26.322 53.049 61.126 1.00 130.80 ? 1014 NAG A N2 1 HETATM 13327 O O3 . NAG Q 4 . ? -26.378 55.725 60.109 1.00 122.97 ? 1014 NAG A O3 1 HETATM 13328 O O4 . NAG Q 4 . ? -24.048 57.411 60.819 1.00 163.56 ? 1014 NAG A O4 1 HETATM 13329 O O5 . NAG Q 4 . ? -24.207 54.945 63.506 1.00 119.99 ? 1014 NAG A O5 1 HETATM 13330 O O6 . NAG Q 4 . ? -23.889 57.694 64.176 1.00 120.96 ? 1014 NAG A O6 1 HETATM 13331 O O7 . NAG Q 4 . ? -28.425 53.203 61.891 1.00 106.38 ? 1014 NAG A O7 1 HETATM 13332 C C1 . NAG R 4 . ? -23.809 57.128 59.417 1.00 173.83 ? 1015 NAG A C1 1 HETATM 13333 C C2 . NAG R 4 . ? -24.765 57.946 58.539 1.00 176.30 ? 1015 NAG A C2 1 HETATM 13334 C C3 . NAG R 4 . ? -24.169 59.321 58.224 1.00 174.67 ? 1015 NAG A C3 1 HETATM 13335 C C4 . NAG R 4 . ? -23.070 59.682 59.216 1.00 158.11 ? 1015 NAG A C4 1 HETATM 13336 C C5 . NAG R 4 . ? -21.932 58.664 59.143 1.00 157.43 ? 1015 NAG A C5 1 HETATM 13337 C C6 . NAG R 4 . ? -21.067 58.645 60.382 1.00 144.51 ? 1015 NAG A C6 1 HETATM 13338 C C7 . NAG R 4 . ? -26.215 56.547 57.130 1.00 147.11 ? 1015 NAG A C7 1 HETATM 13339 C C8 . NAG R 4 . ? -26.372 55.876 55.798 1.00 132.76 ? 1015 NAG A C8 1 HETATM 13340 N N2 . NAG R 4 . ? -25.082 57.234 57.310 1.00 166.32 ? 1015 NAG A N2 1 HETATM 13341 O O3 . NAG R 4 . ? -25.198 60.303 58.272 1.00 176.10 ? 1015 NAG A O3 1 HETATM 13342 O O4 . NAG R 4 . ? -22.564 60.982 58.934 1.00 147.52 ? 1015 NAG A O4 1 HETATM 13343 O O5 . NAG R 4 . ? -22.446 57.332 58.972 1.00 169.84 ? 1015 NAG A O5 1 HETATM 13344 O O6 . NAG R 4 . ? -19.883 57.888 60.171 1.00 137.49 ? 1015 NAG A O6 1 HETATM 13345 O O7 . NAG R 4 . ? -27.075 56.470 58.001 1.00 141.29 ? 1015 NAG A O7 1 HETATM 13346 C C1 . NAG S 4 . ? -41.259 32.376 62.169 1.00 103.82 ? 1016 NAG A C1 1 HETATM 13347 C C2 . NAG S 4 . ? -42.487 32.409 61.258 1.00 132.71 ? 1016 NAG A C2 1 HETATM 13348 C C3 . NAG S 4 . ? -43.164 31.040 61.229 1.00 142.05 ? 1016 NAG A C3 1 HETATM 13349 C C4 . NAG S 4 . ? -42.158 29.957 60.866 1.00 145.19 ? 1016 NAG A C4 1 HETATM 13350 C C5 . NAG S 4 . ? -40.958 30.029 61.805 1.00 136.48 ? 1016 NAG A C5 1 HETATM 13351 C C6 . NAG S 4 . ? -39.864 29.050 61.448 1.00 142.39 ? 1016 NAG A C6 1 HETATM 13352 C C7 . NAG S 4 . ? -43.413 34.681 61.202 1.00 144.89 ? 1016 NAG A C7 1 HETATM 13353 C C8 . NAG S 4 . ? -44.452 35.610 61.753 1.00 133.58 ? 1016 NAG A C8 1 HETATM 13354 N N2 . NAG S 4 . ? -43.426 33.434 61.685 1.00 142.46 ? 1016 NAG A N2 1 HETATM 13355 O O3 . NAG S 4 . ? -44.225 31.056 60.280 1.00 140.58 ? 1016 NAG A O3 1 HETATM 13356 O O4 . NAG S 4 . ? -42.762 28.672 60.965 1.00 146.42 ? 1016 NAG A O4 1 HETATM 13357 O O5 . NAG S 4 . ? -40.375 31.339 61.745 1.00 115.04 ? 1016 NAG A O5 1 HETATM 13358 O O6 . NAG S 4 . ? -38.661 29.345 62.145 1.00 134.98 ? 1016 NAG A O6 1 HETATM 13359 O O7 . NAG S 4 . ? -42.599 35.042 60.359 1.00 150.06 ? 1016 NAG A O7 1 HETATM 13360 C C1 . NAG T 4 . ? -29.154 21.861 75.634 1.00 82.89 ? 1017 NAG A C1 1 HETATM 13361 C C2 . NAG T 4 . ? -29.128 21.314 74.205 1.00 123.10 ? 1017 NAG A C2 1 HETATM 13362 C C3 . NAG T 4 . ? -30.503 21.460 73.556 1.00 119.36 ? 1017 NAG A C3 1 HETATM 13363 C C4 . NAG T 4 . ? -31.571 20.815 74.429 1.00 116.47 ? 1017 NAG A C4 1 HETATM 13364 C C5 . NAG T 4 . ? -31.508 21.399 75.838 1.00 117.67 ? 1017 NAG A C5 1 HETATM 13365 C C6 . NAG T 4 . ? -32.478 20.743 76.794 1.00 120.79 ? 1017 NAG A C6 1 HETATM 13366 C C7 . NAG T 4 . ? -27.036 21.364 72.913 1.00 151.50 ? 1017 NAG A C7 1 HETATM 13367 C C8 . NAG T 4 . ? -26.919 19.899 73.220 1.00 140.15 ? 1017 NAG A C8 1 HETATM 13368 N N2 . NAG T 4 . ? -28.112 21.985 73.409 1.00 149.38 ? 1017 NAG A N2 1 HETATM 13369 O O3 . NAG T 4 . ? -30.493 20.849 72.270 1.00 118.38 ? 1017 NAG A O3 1 HETATM 13370 O O4 . NAG T 4 . ? -32.862 21.036 73.874 1.00 97.46 ? 1017 NAG A O4 1 HETATM 13371 O O5 . NAG T 4 . ? -30.193 21.209 76.383 1.00 107.67 ? 1017 NAG A O5 1 HETATM 13372 O O6 . NAG T 4 . ? -33.774 20.631 76.222 1.00 126.18 ? 1017 NAG A O6 1 HETATM 13373 O O7 . NAG T 4 . ? -26.194 21.957 72.245 1.00 148.26 ? 1017 NAG A O7 1 HETATM 13374 MN MN . MN U 7 . ? -7.191 66.932 32.017 1.00 132.57 ? 1018 MN A MN 1 HETATM 13375 MN MN . MN V 7 . ? -17.302 59.111 25.864 1.00 181.43 ? 1019 MN A MN 1 HETATM 13376 MN MN . MN W 7 . ? -19.085 55.706 13.373 1.00 132.34 ? 1020 MN A MN 1 HETATM 13377 MN MN . MN X 7 . ? -10.704 58.902 3.159 1.00 175.06 ? 1021 MN A MN 1 HETATM 13378 MN MN . MN Y 7 . ? -68.960 46.859 4.482 1.00 131.42 ? 1022 MN A MN 1 HETATM 13379 NA NA . NA Z 8 . ? -60.795 30.948 -14.756 1.00 89.28 ? 1023 NA A NA 1 HETATM 13380 C C1 . GOL AA 9 . ? 24.010 54.214 42.067 1.00 142.86 ? 1024 GOL A C1 1 HETATM 13381 O O1 . GOL AA 9 . ? 23.212 55.009 41.217 1.00 139.51 ? 1024 GOL A O1 1 HETATM 13382 C C2 . GOL AA 9 . ? 23.693 54.537 43.523 1.00 149.16 ? 1024 GOL A C2 1 HETATM 13383 O O2 . GOL AA 9 . ? 22.403 55.098 43.617 1.00 143.91 ? 1024 GOL A O2 1 HETATM 13384 C C3 . GOL AA 9 . ? 23.750 53.256 44.348 1.00 151.40 ? 1024 GOL A C3 1 HETATM 13385 O O3 . GOL AA 9 . ? 23.460 53.553 45.697 1.00 147.53 ? 1024 GOL A O3 1 HETATM 13386 C C1 . NAG BA 4 . ? -26.958 4.131 29.587 1.00 141.70 ? 701 NAG B C1 1 HETATM 13387 C C2 . NAG BA 4 . ? -26.796 2.710 29.033 1.00 161.52 ? 701 NAG B C2 1 HETATM 13388 C C3 . NAG BA 4 . ? -25.969 1.851 29.990 1.00 156.04 ? 701 NAG B C3 1 HETATM 13389 C C4 . NAG BA 4 . ? -25.053 2.718 30.844 1.00 168.66 ? 701 NAG B C4 1 HETATM 13390 C C5 . NAG BA 4 . ? -25.882 3.652 31.723 1.00 171.50 ? 701 NAG B C5 1 HETATM 13391 C C6 . NAG BA 4 . ? -25.137 4.899 32.145 1.00 165.98 ? 701 NAG B C6 1 HETATM 13392 C C7 . NAG BA 4 . ? -28.799 2.279 27.671 1.00 182.39 ? 701 NAG B C7 1 HETATM 13393 C C8 . NAG BA 4 . ? -30.117 1.568 27.602 1.00 187.20 ? 701 NAG B C8 1 HETATM 13394 N N2 . NAG BA 4 . ? -28.094 2.098 28.793 1.00 177.20 ? 701 NAG B N2 1 HETATM 13395 O O3 . NAG BA 4 . ? -25.194 0.921 29.241 1.00 141.00 ? 701 NAG B O3 1 HETATM 13396 O O4 . NAG BA 4 . ? -24.232 1.897 31.666 1.00 169.31 ? 701 NAG B O4 1 HETATM 13397 O O5 . NAG BA 4 . ? -27.068 4.080 31.031 1.00 163.55 ? 701 NAG B O5 1 HETATM 13398 O O6 . NAG BA 4 . ? -25.989 5.814 32.821 1.00 150.16 ? 701 NAG B O6 1 HETATM 13399 O O7 . NAG BA 4 . ? -28.391 2.982 26.752 1.00 178.56 ? 701 NAG B O7 1 HETATM 13400 C C1 . NAG CA 4 . ? -3.359 35.094 44.644 1.00 104.58 ? 702 NAG B C1 1 HETATM 13401 C C2 . NAG CA 4 . ? -2.975 36.396 45.342 1.00 140.15 ? 702 NAG B C2 1 HETATM 13402 C C3 . NAG CA 4 . ? -3.795 36.572 46.620 1.00 152.77 ? 702 NAG B C3 1 HETATM 13403 C C4 . NAG CA 4 . ? -5.283 36.425 46.330 1.00 150.75 ? 702 NAG B C4 1 HETATM 13404 C C5 . NAG CA 4 . ? -5.550 35.122 45.585 1.00 148.00 ? 702 NAG B C5 1 HETATM 13405 C C6 . NAG CA 4 . ? -6.990 34.966 45.155 1.00 156.80 ? 702 NAG B C6 1 HETATM 13406 C C7 . NAG CA 4 . ? -0.637 36.892 44.782 1.00 161.28 ? 702 NAG B C7 1 HETATM 13407 C C8 . NAG CA 4 . ? 0.785 36.859 45.256 1.00 165.08 ? 702 NAG B C8 1 HETATM 13408 N N2 . NAG CA 4 . ? -1.552 36.431 45.640 1.00 156.00 ? 702 NAG B N2 1 HETATM 13409 O O3 . NAG CA 4 . ? -3.535 37.856 47.174 1.00 160.64 ? 702 NAG B O3 1 HETATM 13410 O O4 . NAG CA 4 . ? -6.017 36.423 47.549 1.00 158.89 ? 702 NAG B O4 1 HETATM 13411 O O5 . NAG CA 4 . ? -4.758 35.083 44.391 1.00 130.96 ? 702 NAG B O5 1 HETATM 13412 O O6 . NAG CA 4 . ? -7.105 34.091 44.041 1.00 157.95 ? 702 NAG B O6 1 HETATM 13413 O O7 . NAG CA 4 . ? -0.942 37.317 43.674 1.00 160.63 ? 702 NAG B O7 1 HETATM 13414 C C1 . NAG DA 4 . ? -26.433 10.799 34.740 1.00 80.25 ? 703 NAG B C1 1 HETATM 13415 C C2 . NAG DA 4 . ? -26.923 10.319 33.382 1.00 96.91 ? 703 NAG B C2 1 HETATM 13416 C C3 . NAG DA 4 . ? -28.233 11.019 33.016 1.00 109.82 ? 703 NAG B C3 1 HETATM 13417 C C4 . NAG DA 4 . ? -29.259 10.866 34.136 1.00 117.41 ? 703 NAG B C4 1 HETATM 13418 C C5 . NAG DA 4 . ? -28.646 11.278 35.475 1.00 112.91 ? 703 NAG B C5 1 HETATM 13419 C C6 . NAG DA 4 . ? -29.555 11.010 36.651 1.00 121.78 ? 703 NAG B C6 1 HETATM 13420 C C7 . NAG DA 4 . ? -25.015 9.618 32.010 1.00 115.09 ? 703 NAG B C7 1 HETATM 13421 C C8 . NAG DA 4 . ? -24.048 10.014 30.936 1.00 109.02 ? 703 NAG B C8 1 HETATM 13422 N N2 . NAG DA 4 . ? -25.917 10.542 32.357 1.00 110.54 ? 703 NAG B N2 1 HETATM 13423 O O3 . NAG DA 4 . ? -28.719 10.459 31.801 1.00 116.30 ? 703 NAG B O3 1 HETATM 13424 O O4 . NAG DA 4 . ? -30.384 11.716 33.925 1.00 136.10 ? 703 NAG B O4 1 HETATM 13425 O O5 . NAG DA 4 . ? -27.430 10.554 35.717 1.00 119.48 ? 703 NAG B O5 1 HETATM 13426 O O6 . NAG DA 4 . ? -30.702 11.848 36.622 1.00 117.19 ? 703 NAG B O6 1 HETATM 13427 O O7 . NAG DA 4 . ? -24.983 8.511 32.540 1.00 125.91 ? 703 NAG B O7 1 HETATM 13428 C C1 . NAG EA 4 . ? -31.372 11.277 32.956 1.00 161.71 ? 704 NAG B C1 1 HETATM 13429 C C2 . NAG EA 4 . ? -32.012 9.906 33.235 1.00 171.90 ? 704 NAG B C2 1 HETATM 13430 C C3 . NAG EA 4 . ? -32.873 9.958 34.500 1.00 177.39 ? 704 NAG B C3 1 HETATM 13431 C C4 . NAG EA 4 . ? -33.326 11.381 34.798 1.00 175.61 ? 704 NAG B C4 1 HETATM 13432 C C5 . NAG EA 4 . ? -33.619 12.125 33.498 1.00 173.69 ? 704 NAG B C5 1 HETATM 13433 C C6 . NAG EA 4 . ? -34.168 13.515 33.725 1.00 169.81 ? 704 NAG B C6 1 HETATM 13434 C C7 . NAG EA 4 . ? -32.765 8.207 31.617 1.00 172.16 ? 704 NAG B C7 1 HETATM 13435 C C8 . NAG EA 4 . ? -31.844 7.254 32.319 1.00 169.15 ? 704 NAG B C8 1 HETATM 13436 N N2 . NAG EA 4 . ? -32.801 9.455 32.097 1.00 172.19 ? 704 NAG B N2 1 HETATM 13437 O O3 . NAG EA 4 . ? -32.139 9.435 35.601 1.00 178.85 ? 704 NAG B O3 1 HETATM 13438 O O4 . NAG EA 4 . ? -34.503 11.359 35.598 1.00 174.15 ? 704 NAG B O4 1 HETATM 13439 O O5 . NAG EA 4 . ? -32.417 12.275 32.723 1.00 174.07 ? 704 NAG B O5 1 HETATM 13440 O O6 . NAG EA 4 . ? -34.179 13.850 35.106 1.00 167.15 ? 704 NAG B O6 1 HETATM 13441 O O7 . NAG EA 4 . ? -33.447 7.863 30.655 1.00 173.34 ? 704 NAG B O7 1 HETATM 13442 C C1 . NAG FA 4 . ? -33.530 30.411 31.596 1.00 75.17 ? 705 NAG B C1 1 HETATM 13443 C C2 . NAG FA 4 . ? -33.242 30.637 33.072 1.00 92.34 ? 705 NAG B C2 1 HETATM 13444 C C3 . NAG FA 4 . ? -34.466 30.271 33.906 1.00 94.35 ? 705 NAG B C3 1 HETATM 13445 C C4 . NAG FA 4 . ? -35.701 31.010 33.400 1.00 99.96 ? 705 NAG B C4 1 HETATM 13446 C C5 . NAG FA 4 . ? -35.861 30.812 31.894 1.00 91.62 ? 705 NAG B C5 1 HETATM 13447 C C6 . NAG FA 4 . ? -36.979 31.640 31.302 1.00 108.51 ? 705 NAG B C6 1 HETATM 13448 C C7 . NAG FA 4 . ? -30.879 30.426 33.695 1.00 112.42 ? 705 NAG B C7 1 HETATM 13449 C C8 . NAG FA 4 . ? -29.792 29.492 34.135 1.00 124.25 ? 705 NAG B C8 1 HETATM 13450 N N2 . NAG FA 4 . ? -32.082 29.874 33.502 1.00 97.76 ? 705 NAG B N2 1 HETATM 13451 O O3 . NAG FA 4 . ? -34.207 30.599 35.266 1.00 107.65 ? 705 NAG B O3 1 HETATM 13452 O O4 . NAG FA 4 . ? -36.875 30.484 34.010 1.00 116.31 ? 705 NAG B O4 1 HETATM 13453 O O5 . NAG FA 4 . ? -34.655 31.184 31.208 1.00 92.97 ? 705 NAG B O5 1 HETATM 13454 O O6 . NAG FA 4 . ? -36.523 32.916 30.874 1.00 122.01 ? 705 NAG B O6 1 HETATM 13455 O O7 . NAG FA 4 . ? -30.677 31.624 33.521 1.00 121.22 ? 705 NAG B O7 1 HETATM 13456 C C1 . NAG GA 4 . ? -37.260 31.135 35.232 1.00 130.87 ? 706 NAG B C1 1 HETATM 13457 C C2 . NAG GA 4 . ? -38.755 30.781 35.423 1.00 127.57 ? 706 NAG B C2 1 HETATM 13458 C C3 . NAG GA 4 . ? -39.259 31.137 36.829 1.00 127.15 ? 706 NAG B C3 1 HETATM 13459 C C4 . NAG GA 4 . ? -38.324 30.550 37.877 1.00 139.08 ? 706 NAG B C4 1 HETATM 13460 C C5 . NAG GA 4 . ? -36.914 31.063 37.626 1.00 145.10 ? 706 NAG B C5 1 HETATM 13461 C C6 . NAG GA 4 . ? -35.905 30.540 38.622 1.00 154.88 ? 706 NAG B C6 1 HETATM 13462 C C7 . NAG GA 4 . ? -39.866 32.604 34.048 1.00 156.08 ? 706 NAG B C7 1 HETATM 13463 C C8 . NAG GA 4 . ? -39.173 33.677 34.850 1.00 163.25 ? 706 NAG B C8 1 HETATM 13464 N N2 . NAG GA 4 . ? -39.625 31.316 34.374 1.00 132.75 ? 706 NAG B N2 1 HETATM 13465 O O3 . NAG GA 4 . ? -40.571 30.608 36.987 1.00 137.63 ? 706 NAG B O3 1 HETATM 13466 O O4 . NAG GA 4 . ? -38.722 30.816 39.220 1.00 150.23 ? 706 NAG B O4 1 HETATM 13467 O O5 . NAG GA 4 . ? -36.489 30.616 36.332 1.00 139.25 ? 706 NAG B O5 1 HETATM 13468 O O6 . NAG GA 4 . ? -34.587 30.959 38.295 1.00 159.62 ? 706 NAG B O6 1 HETATM 13469 O O7 . NAG GA 4 . ? -40.628 32.891 33.130 1.00 158.56 ? 706 NAG B O7 1 HETATM 13470 C C1 . BMA HA 5 . ? -39.471 32.025 39.456 1.00 154.89 ? 707 BMA B C1 1 HETATM 13471 C C2 . BMA HA 5 . ? -40.818 31.625 40.115 1.00 143.45 ? 707 BMA B C2 1 HETATM 13472 C C3 . BMA HA 5 . ? -40.589 31.086 41.544 1.00 142.75 ? 707 BMA B C3 1 HETATM 13473 C C4 . BMA HA 5 . ? -39.273 31.608 42.156 1.00 150.25 ? 707 BMA B C4 1 HETATM 13474 C C5 . BMA HA 5 . ? -39.011 33.039 41.645 1.00 158.49 ? 707 BMA B C5 1 HETATM 13475 C C6 . BMA HA 5 . ? -37.842 33.722 42.339 1.00 150.93 ? 707 BMA B C6 1 HETATM 13476 O O2 . BMA HA 5 . ? -41.455 30.584 39.384 1.00 119.58 ? 707 BMA B O2 1 HETATM 13477 O O3 . BMA HA 5 . ? -40.631 29.661 41.585 1.00 115.87 ? 707 BMA B O3 1 HETATM 13478 O O4 . BMA HA 5 . ? -39.345 31.595 43.575 1.00 139.98 ? 707 BMA B O4 1 HETATM 13479 O O5 . BMA HA 5 . ? -38.732 32.992 40.211 1.00 158.76 ? 707 BMA B O5 1 HETATM 13480 O O6 . BMA HA 5 . ? -38.033 33.625 43.746 1.00 141.88 ? 707 BMA B O6 1 HETATM 13481 MN MN . MN IA 7 . ? 17.639 35.289 39.884 1.00 73.44 ? 708 MN B MN 1 HETATM 13482 MN MN . MN JA 7 . ? 18.884 30.294 47.839 1.00 99.85 ? 709 MN B MN 1 HETATM 13483 MN MN . MN KA 7 . ? 16.023 38.350 35.136 1.00 103.33 ? 710 MN B MN 1 HETATM 13484 NA NA . NA LA 8 . ? -4.586 24.568 74.460 1.00 115.85 ? 711 NA B NA 1 HETATM 13485 CL CL . CL MA 10 . ? -4.452 23.345 76.523 1.00 123.87 ? 712 CL B CL 1 HETATM 13486 CL CL . CL NA 10 . ? -4.792 26.364 72.874 1.00 142.63 ? 713 CL B CL 1 HETATM 13487 C C1 . GOL OA 9 . ? 23.149 49.132 43.230 1.00 136.56 ? 1601 GOL C C1 1 HETATM 13488 O O1 . GOL OA 9 . ? 23.043 49.187 44.635 1.00 131.20 ? 1601 GOL C O1 1 HETATM 13489 C C2 . GOL OA 9 . ? 24.521 49.642 42.799 1.00 144.18 ? 1601 GOL C C2 1 HETATM 13490 O O2 . GOL OA 9 . ? 25.439 49.475 43.857 1.00 145.03 ? 1601 GOL C O2 1 HETATM 13491 C C3 . GOL OA 9 . ? 24.999 48.854 41.584 1.00 140.68 ? 1601 GOL C C3 1 HETATM 13492 O O3 . GOL OA 9 . ? 26.234 49.369 41.139 1.00 131.47 ? 1601 GOL C O3 1 HETATM 13493 O O . HOH PA 11 . ? 16.939 51.919 34.671 1.00 71.46 ? 1101 HOH A O 1 HETATM 13494 O O . HOH PA 11 . ? 22.526 48.473 37.981 1.00 86.09 ? 1102 HOH A O 1 HETATM 13495 O O . HOH QA 11 . ? 15.972 34.225 40.789 1.00 117.17 ? 801 HOH B O 1 HETATM 13496 O O . HOH QA 11 . ? 16.304 36.686 40.893 1.00 45.98 ? 802 HOH B O 1 HETATM 13497 O O . HOH RA 11 . ? 17.880 35.368 42.062 1.00 75.04 ? 1701 HOH C O 1 HETATM 13498 O O . HOH RA 11 . ? 18.565 31.960 49.238 1.00 128.77 ? 1702 HOH C O 1 HETATM 13499 O O . HOH RA 11 . ? 19.873 42.066 44.107 1.00 88.02 ? 1703 HOH C O 1 HETATM 13500 O O . HOH RA 11 . ? 21.337 44.975 38.783 1.00 83.46 ? 1704 HOH C O 1 HETATM 13501 O O . HOH RA 11 . ? 16.719 37.089 43.149 1.00 112.69 ? 1705 HOH C 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 ? 1.1472 0.9952 1.2790 -0.4132 -0.4666 0.2152 1 PHE A N 2 C CA . PHE A 1 ? 1.1866 1.0526 1.2951 -0.4443 -0.4983 0.2114 1 PHE A CA 3 C C . PHE A 1 ? 1.3746 1.2440 1.4256 -0.4636 -0.5333 0.2304 1 PHE A C 4 O O . PHE A 1 ? 1.3273 1.2077 1.3363 -0.4931 -0.5590 0.2242 1 PHE A O 5 C CB . PHE A 1 ? 1.1819 1.0844 1.3744 -0.4458 -0.5199 0.2243 1 PHE A CB 6 C CG . PHE A 1 ? 1.1855 1.1122 1.4391 -0.4328 -0.5480 0.2618 1 PHE A CG 7 C CD1 . PHE A 1 ? 1.2603 1.1859 1.5780 -0.4003 -0.5259 0.2719 1 PHE A CD1 8 C CD2 . PHE A 1 ? 1.2304 1.1811 1.4790 -0.4533 -0.5973 0.2867 1 PHE A CD2 9 C CE1 . PHE A 1 ? 1.2646 1.2105 1.6461 -0.3865 -0.5510 0.3049 1 PHE A CE1 10 C CE2 . PHE A 1 ? 1.2360 1.2083 1.5476 -0.4402 -0.6254 0.3239 1 PHE A CE2 11 C CZ . PHE A 1 ? 1.2183 1.1874 1.5997 -0.4058 -0.6016 0.3325 1 PHE A CZ 12 N N . ASN A 2 ? 1.4360 1.2957 1.4843 -0.4483 -0.5344 0.2538 2 ASN A N 13 C CA . ASN A 2 ? 1.3900 1.2545 1.3910 -0.4656 -0.5690 0.2800 2 ASN A CA 14 C C . ASN A 2 ? 1.3241 1.1620 1.2297 -0.4774 -0.5519 0.2658 2 ASN A C 15 O O . ASN A 2 ? 1.3464 1.1865 1.2058 -0.4923 -0.5758 0.2883 2 ASN A O 16 C CB . ASN A 2 ? 1.2772 1.1480 1.3381 -0.4443 -0.5860 0.3194 2 ASN A CB 17 C CG . ASN A 2 ? 1.2661 1.1157 1.3719 -0.4095 -0.5465 0.3119 2 ASN A CG 18 O OD1 . ASN A 2 ? 1.2665 1.1115 1.3964 -0.3977 -0.5140 0.2851 2 ASN A OD1 19 N ND2 . ASN A 2 ? 1.2898 1.1259 1.4063 -0.3944 -0.5498 0.3361 2 ASN A ND2 20 N N . LEU A 3 ? 1.2766 1.0909 1.1553 -0.4710 -0.5110 0.2305 3 LEU A N 21 C CA . LEU A 3 ? 1.3107 1.1025 1.1061 -0.4810 -0.4916 0.2142 3 LEU A CA 22 C C . LEU A 3 ? 1.3738 1.1752 1.0980 -0.5164 -0.5091 0.1983 3 LEU A C 23 O O . LEU A 3 ? 1.4108 1.2223 1.1438 -0.5294 -0.5153 0.1777 3 LEU A O 24 C CB . LEU A 3 ? 1.2501 1.0157 1.0447 -0.4628 -0.4445 0.1822 3 LEU A CB 25 C CG . LEU A 3 ? 1.2300 0.9803 1.0681 -0.4310 -0.4220 0.1936 3 LEU A CG 26 C CD1 . LEU A 3 ? 1.3258 1.0530 1.1564 -0.4171 -0.3794 0.1624 3 LEU A CD1 27 C CD2 . LEU A 3 ? 1.2248 0.9667 1.0338 -0.4303 -0.4310 0.2191 3 LEU A CD2 28 N N . ASP A 4 ? 1.3921 1.1902 1.0449 -0.5331 -0.5158 0.2066 4 ASP A N 29 C CA . ASP A 4 ? 1.4545 1.2638 1.0313 -0.5689 -0.5323 0.1918 4 ASP A CA 30 C C . ASP A 4 ? 1.6813 1.4698 1.2020 -0.5748 -0.4933 0.1461 4 ASP A C 31 O O . ASP A 4 ? 1.7289 1.5012 1.2127 -0.5688 -0.4678 0.1426 4 ASP A O 32 C CB . ASP A 4 ? 1.5084 1.3294 1.0338 -0.5876 -0.5612 0.2272 4 ASP A CB 33 C CG . ASP A 4 ? 1.8035 1.6340 1.2341 -0.6254 -0.5697 0.2078 4 ASP A CG 34 O OD1 . ASP A 4 ? 2.0434 1.8851 1.4646 -0.6438 -0.5808 0.1824 4 ASP A OD1 35 O OD2 . ASP A 4 ? 1.8288 1.6561 1.1943 -0.6377 -0.5642 0.2170 4 ASP A OD2 36 N N . VAL A 5 ? 1.5876 1.3769 1.1065 -0.5868 -0.4895 0.1113 5 VAL A N 37 C CA . VAL A 5 ? 1.6039 1.3727 1.0793 -0.5916 -0.4537 0.0655 5 VAL A CA 38 C C . VAL A 5 ? 1.5451 1.3236 0.9344 -0.6279 -0.4650 0.0450 5 VAL A C 39 O O . VAL A 5 ? 1.5602 1.3245 0.9093 -0.6317 -0.4334 0.0059 5 VAL A O 40 C CB . VAL A 5 ? 1.7464 1.5044 1.2739 -0.5821 -0.4382 0.0363 5 VAL A CB 41 C CG1 . VAL A 5 ? 1.9071 1.6365 1.4173 -0.5710 -0.3935 -0.0008 5 VAL A CG1 42 C CG2 . VAL A 5 ? 1.7354 1.4978 1.3503 -0.5554 -0.4419 0.0628 5 VAL A CG2 43 N N . ASP A 6 ? 1.5926 1.3975 0.9624 -0.6453 -0.5015 0.0732 6 ASP A N 44 C CA . ASP A 6 ? 1.8172 1.6364 1.1153 -0.6684 -0.5016 0.0581 6 ASP A CA 45 C C . ASP A 6 ? 1.9335 1.7474 1.1610 -0.6752 -0.4790 0.0575 6 ASP A C 46 O O . ASP A 6 ? 2.0597 1.8685 1.2383 -0.6833 -0.4488 0.0189 6 ASP A O 47 C CB . ASP A 6 ? 1.8480 1.6973 1.1490 -0.6836 -0.5465 0.0929 6 ASP A CB 48 C CG . ASP A 6 ? 1.9552 1.8155 1.3071 -0.6851 -0.5644 0.0804 6 ASP A CG 49 O OD1 . ASP A 6 ? 2.0274 1.8719 1.4310 -0.6701 -0.5472 0.0577 6 ASP A OD1 50 O OD2 . ASP A 6 ? 1.9677 1.8527 1.3090 -0.7021 -0.5955 0.0944 6 ASP A OD2 51 N N . SER A 7 ? 2.0032 1.8193 1.2307 -0.6715 -0.4931 0.1005 7 SER A N 52 C CA . SER A 7 ? 2.0372 1.8511 1.2022 -0.6793 -0.4737 0.1067 7 SER A CA 53 C C . SER A 7 ? 1.8206 1.6147 1.0107 -0.6604 -0.4639 0.1261 7 SER A C 54 O O . SER A 7 ? 1.9576 1.7566 1.1544 -0.6574 -0.4824 0.1715 7 SER A O 55 C CB . SER A 7 ? 2.2026 2.0416 1.3272 -0.7004 -0.5023 0.1449 7 SER A CB 56 O OG . SER A 7 ? 2.2799 2.1272 1.4578 -0.6931 -0.5435 0.1946 7 SER A OG 57 N N . PRO A 8 ? 1.6018 1.3731 0.8242 -0.6360 -0.4234 0.0935 8 PRO A N 58 C CA . PRO A 8 ? 1.5453 1.2979 0.8065 -0.6061 -0.3986 0.1083 8 PRO A CA 59 C C . PRO A 8 ? 1.5724 1.3233 0.7723 -0.6160 -0.3754 0.1076 8 PRO A C 60 O O . PRO A 8 ? 1.8199 1.5860 0.9464 -0.6463 -0.3783 0.0970 8 PRO A O 61 C CB . PRO A 8 ? 1.4892 1.2217 0.7986 -0.5822 -0.3671 0.0716 8 PRO A CB 62 C CG . PRO A 8 ? 1.5303 1.2658 0.7956 -0.6042 -0.3589 0.0276 8 PRO A CG 63 C CD . PRO A 8 ? 1.5946 1.3552 0.8196 -0.6362 -0.4000 0.0417 8 PRO A CD 64 N N . ALA A 9 ? 1.5572 1.2917 0.7865 -0.5923 -0.3521 0.1177 9 ALA A N 65 C CA . ALA A 9 ? 1.6310 1.3649 0.8116 -0.6005 -0.3279 0.1178 9 ALA A CA 66 C C . ALA A 9 ? 1.6961 1.4152 0.8826 -0.5859 -0.2826 0.0743 9 ALA A C 67 O O . ALA A 9 ? 1.6943 1.3950 0.9386 -0.5569 -0.2667 0.0708 9 ALA A O 68 C CB . ALA A 9 ? 1.5911 1.3182 0.7978 -0.5883 -0.3371 0.1633 9 ALA A CB 69 N N . GLU A 10 ? 1.8493 1.5774 0.9763 -0.6065 -0.2622 0.0410 10 GLU A N 70 C CA . GLU A 10 ? 1.8981 1.6144 1.0320 -0.5940 -0.2198 -0.0017 10 GLU A CA 71 C C . GLU A 10 ? 1.6237 1.3404 0.7443 -0.5901 -0.1933 0.0071 10 GLU A C 72 O O . GLU A 10 ? 1.7008 1.4349 0.7639 -0.6140 -0.1934 0.0198 10 GLU A O 73 C CB . GLU A 10 ? 2.2044 1.9293 1.2887 -0.6164 -0.2079 -0.0478 10 GLU A CB 74 C CG . GLU A 10 ? 2.3854 2.1016 1.4710 -0.6069 -0.1627 -0.0923 10 GLU A CG 75 C CD . GLU A 10 ? 2.4998 2.2341 1.5237 -0.6263 -0.1392 -0.0981 10 GLU A CD 76 O OE1 . GLU A 10 ? 2.4591 2.2140 1.4228 -0.6546 -0.1582 -0.0767 10 GLU A OE1 77 O OE2 . GLU A 10 ? 2.4685 2.1984 1.5056 -0.6140 -0.1020 -0.1225 10 GLU A OE2 78 N N . TYR A 11 ? 1.4706 1.1695 0.6445 -0.5615 -0.1711 0.0012 11 TYR A N 79 C CA . TYR A 11 ? 1.4918 1.1910 0.6619 -0.5564 -0.1444 0.0053 11 TYR A CA 80 C C . TYR A 11 ? 1.4939 1.1852 0.6852 -0.5414 -0.1070 -0.0378 11 TYR A C 81 O O . TYR A 11 ? 1.3917 1.0659 0.6329 -0.5195 -0.1041 -0.0525 11 TYR A O 82 C CB . TYR A 11 ? 1.5133 1.1993 0.7304 -0.5364 -0.1558 0.0441 11 TYR A CB 83 C CG . TYR A 11 ? 1.5050 1.1982 0.7045 -0.5508 -0.1896 0.0904 11 TYR A CG 84 C CD1 . TYR A 11 ? 1.8033 1.5067 0.9662 -0.5680 -0.1876 0.1157 11 TYR A CD1 85 C CD2 . TYR A 11 ? 1.4530 1.1437 0.6771 -0.5475 -0.2240 0.1107 11 TYR A CD2 86 C CE1 . TYR A 11 ? 1.8240 1.5318 0.9740 -0.5814 -0.2205 0.1617 11 TYR A CE1 87 C CE2 . TYR A 11 ? 1.5593 1.2564 0.7742 -0.5593 -0.2570 0.1552 11 TYR A CE2 88 C CZ . TYR A 11 ? 1.7602 1.4643 0.9377 -0.5761 -0.2559 0.1814 11 TYR A CZ 89 O OH . TYR A 11 ? 1.8232 1.5316 0.9944 -0.5882 -0.2905 0.2292 11 TYR A OH 90 N N . SER A 12 ? 1.5347 1.2397 0.6906 -0.5535 -0.0784 -0.0565 12 SER A N 91 C CA . SER A 12 ? 1.5853 1.2853 0.7647 -0.5397 -0.0424 -0.0977 12 SER A CA 92 C C . SER A 12 ? 1.5776 1.2871 0.7601 -0.5364 -0.0148 -0.0938 12 SER A C 93 O O . SER A 12 ? 1.8691 1.6003 1.0015 -0.5594 -0.0049 -0.0892 12 SER A O 94 C CB . SER A 12 ? 1.7470 1.4564 0.8856 -0.5581 -0.0287 -0.1420 12 SER A CB 95 O OG . SER A 12 ? 1.9846 1.7198 1.0533 -0.5882 -0.0215 -0.1414 12 SER A OG 96 N N . GLY A 13 ? 1.4052 1.1002 0.6466 -0.5091 -0.0030 -0.0948 13 GLY A N 97 C CA . GLY A 13 ? 1.4101 1.1145 0.6652 -0.5039 0.0241 -0.0962 13 GLY A CA 98 C C . GLY A 13 ? 1.6862 1.3986 0.9477 -0.5010 0.0590 -0.1428 13 GLY A C 99 O O . GLY A 13 ? 1.7890 1.4985 1.0365 -0.5062 0.0618 -0.1742 13 GLY A O 100 N N . PRO A 14 ? 1.6971 1.4195 0.9843 -0.4926 0.0855 -0.1484 14 PRO A N 101 C CA . PRO A 14 ? 1.6918 1.4237 0.9967 -0.4868 0.1209 -0.1919 14 PRO A CA 102 C C . PRO A 14 ? 1.4748 1.1820 0.8346 -0.4610 0.1202 -0.2146 14 PRO A C 103 O O . PRO A 14 ? 1.5217 1.2084 0.9173 -0.4433 0.0990 -0.1920 14 PRO A O 104 C CB . PRO A 14 ? 1.4682 1.2164 0.7994 -0.4815 0.1410 -0.1804 14 PRO A CB 105 C CG . PRO A 14 ? 1.3875 1.1206 0.7390 -0.4722 0.1133 -0.1366 14 PRO A CG 106 C CD . PRO A 14 ? 1.3986 1.1230 0.7072 -0.4868 0.0820 -0.1137 14 PRO A CD 107 N N . GLU A 15 ? 1.5053 1.2139 0.8722 -0.4596 0.1437 -0.2585 15 GLU A N 108 C CA . GLU A 15 ? 1.6530 1.3357 1.0720 -0.4373 0.1419 -0.2788 15 GLU A CA 109 C C . GLU A 15 ? 1.4864 1.1635 0.9736 -0.4102 0.1516 -0.2720 15 GLU A C 110 O O . GLU A 15 ? 1.4003 1.0980 0.8993 -0.4090 0.1722 -0.2718 15 GLU A O 111 C CB . GLU A 15 ? 1.5661 1.2487 0.9758 -0.4443 0.1635 -0.3296 15 GLU A CB 112 C CG . GLU A 15 ? 1.7887 1.4942 1.2068 -0.4450 0.2035 -0.3612 15 GLU A CG 113 C CD . GLU A 15 ? 2.0568 1.7566 1.4769 -0.4475 0.2257 -0.4158 15 GLU A CD 114 O OE1 . GLU A 15 ? 1.9166 1.5916 1.3366 -0.4477 0.2081 -0.4276 15 GLU A OE1 115 O OE2 . GLU A 15 ? 2.1798 1.9002 1.6043 -0.4497 0.2614 -0.4481 15 GLU A OE2 116 N N . GLY A 16 ? 1.3647 1.0158 0.8963 -0.3899 0.1356 -0.2647 16 GLY A N 117 C CA . GLY A 16 ? 1.2342 0.8784 0.8281 -0.3650 0.1394 -0.2554 16 GLY A CA 118 C C . GLY A 16 ? 1.2107 0.8574 0.8068 -0.3610 0.1222 -0.2141 16 GLY A C 119 O O . GLY A 16 ? 1.1971 0.8384 0.8387 -0.3424 0.1202 -0.2017 16 GLY A O 120 N N . SER A 17 ? 1.2765 0.9306 0.8236 -0.3791 0.1083 -0.1928 17 SER A N 121 C CA . SER A 17 ? 1.2367 0.8928 0.7828 -0.3783 0.0933 -0.1557 17 SER A CA 122 C C . SER A 17 ? 1.1919 0.8257 0.7460 -0.3692 0.0645 -0.1311 17 SER A C 123 O O . SER A 17 ? 1.4788 1.1109 1.0287 -0.3698 0.0498 -0.1020 17 SER A O 124 C CB . SER A 17 ? 1.3662 1.0423 0.8597 -0.4032 0.0941 -0.1424 17 SER A CB 125 O OG . SER A 17 ? 1.3900 1.0622 0.8386 -0.4192 0.0776 -0.1400 17 SER A OG 126 N N . TYR A 18 ? 1.3114 0.9286 0.8773 -0.3623 0.0572 -0.1436 18 TYR A N 127 C CA . TYR A 18 ? 1.3591 0.9582 0.9353 -0.3542 0.0328 -0.1228 18 TYR A CA 128 C C . TYR A 18 ? 1.2389 0.8421 0.7809 -0.3675 0.0126 -0.0958 18 TYR A C 129 O O . TYR A 18 ? 1.0785 0.6717 0.6350 -0.3586 -0.0041 -0.0719 18 TYR A O 130 C CB . TYR A 18 ? 1.1296 0.7180 0.7497 -0.3328 0.0303 -0.1092 18 TYR A CB 131 C CG . TYR A 18 ? 1.0844 0.6620 0.7451 -0.3173 0.0402 -0.1275 18 TYR A CG 132 C CD1 . TYR A 18 ? 1.0696 0.6445 0.7315 -0.3214 0.0516 -0.1567 18 TYR A CD1 133 C CD2 . TYR A 18 ? 1.1309 0.7000 0.8289 -0.2994 0.0369 -0.1151 18 TYR A CD2 134 C CE1 . TYR A 18 ? 1.0968 0.6588 0.8016 -0.3067 0.0593 -0.1714 18 TYR A CE1 135 C CE2 . TYR A 18 ? 1.0036 0.5624 0.7403 -0.2859 0.0434 -0.1271 18 TYR A CE2 136 C CZ . TYR A 18 ? 1.0842 0.6383 0.8269 -0.2889 0.0544 -0.1542 18 TYR A CZ 137 O OH . TYR A 18 ? 1.3410 0.8819 1.1277 -0.2749 0.0596 -0.1642 18 TYR A OH 138 N N . PHE A 19 ? 1.2648 0.8833 0.7623 -0.3890 0.0147 -0.0996 19 PHE A N 139 C CA . PHE A 19 ? 1.1747 0.7980 0.6387 -0.4040 -0.0063 -0.0722 19 PHE A CA 140 C C . PHE A 19 ? 1.2112 0.8218 0.6841 -0.4001 -0.0304 -0.0630 19 PHE A C 141 O O . PHE A 19 ? 1.5460 1.1541 1.0143 -0.4045 -0.0317 -0.0832 19 PHE A O 142 C CB . PHE A 19 ? 1.2378 0.8814 0.6478 -0.4302 0.0008 -0.0810 19 PHE A CB 143 C CG . PHE A 19 ? 1.2849 0.9344 0.6574 -0.4484 -0.0242 -0.0514 19 PHE A CG 144 C CD1 . PHE A 19 ? 1.4016 1.0498 0.7545 -0.4585 -0.0449 -0.0518 19 PHE A CD1 145 C CD2 . PHE A 19 ? 1.3243 0.9811 0.6833 -0.4568 -0.0282 -0.0221 19 PHE A CD2 146 C CE1 . PHE A 19 ? 1.5112 1.1665 0.8334 -0.4751 -0.0706 -0.0220 19 PHE A CE1 147 C CE2 . PHE A 19 ? 1.4532 1.1141 0.7813 -0.4734 -0.0531 0.0082 19 PHE A CE2 148 C CZ . PHE A 19 ? 1.5308 1.1918 0.8409 -0.4821 -0.0749 0.0090 19 PHE A CZ 149 N N . GLY A 20 ? 1.2062 0.8091 0.6944 -0.3925 -0.0490 -0.0336 20 GLY A N 150 C CA . GLY A 20 ? 1.1166 0.7102 0.6223 -0.3866 -0.0700 -0.0235 20 GLY A CA 151 C C . GLY A 20 ? 1.0717 0.6501 0.6242 -0.3631 -0.0681 -0.0215 20 GLY A C 152 O O . GLY A 20 ? 1.0906 0.6631 0.6630 -0.3567 -0.0826 -0.0124 20 GLY A O 153 N N . PHE A 21 ? 1.0513 0.6257 0.6214 -0.3512 -0.0507 -0.0290 21 PHE A N 154 C CA . PHE A 21 ? 1.0146 0.5760 0.6232 -0.3309 -0.0485 -0.0270 21 PHE A CA 155 C C . PHE A 21 ? 1.0130 0.5680 0.6355 -0.3229 -0.0637 -0.0028 21 PHE A C 156 O O . PHE A 21 ? 0.9736 0.5200 0.6225 -0.3093 -0.0658 -0.0003 21 PHE A O 157 C CB . PHE A 21 ? 1.0183 0.5798 0.6414 -0.3218 -0.0307 -0.0359 21 PHE A CB 158 C CG . PHE A 21 ? 1.1364 0.6863 0.7938 -0.3033 -0.0291 -0.0343 21 PHE A CG 159 C CD1 . PHE A 21 ? 0.9892 0.5323 0.6662 -0.2966 -0.0234 -0.0485 21 PHE A CD1 160 C CD2 . PHE A 21 ? 0.9727 0.5178 0.6415 -0.2940 -0.0339 -0.0184 21 PHE A CD2 161 C CE1 . PHE A 21 ? 0.9431 0.4767 0.6479 -0.2817 -0.0230 -0.0433 21 PHE A CE1 162 C CE2 . PHE A 21 ? 0.9287 0.4652 0.6221 -0.2794 -0.0327 -0.0168 21 PHE A CE2 163 C CZ . PHE A 21 ? 0.9252 0.4570 0.6354 -0.2736 -0.0275 -0.0275 21 PHE A CZ 164 N N . ALA A 22 ? 1.2217 0.7807 0.8271 -0.3317 -0.0733 0.0148 22 ALA A N 165 C CA . ALA A 22 ? 1.0002 0.5517 0.6216 -0.3246 -0.0884 0.0366 22 ALA A CA 166 C C . ALA A 22 ? 1.2180 0.7758 0.8177 -0.3400 -0.1056 0.0560 22 ALA A C 167 O O . ALA A 22 ? 1.3564 0.9233 0.9251 -0.3558 -0.1022 0.0571 22 ALA A O 168 C CB . ALA A 22 ? 0.9821 0.5249 0.6183 -0.3140 -0.0816 0.0414 22 ALA A CB 169 N N . VAL A 23 ? 1.0285 0.5831 0.6459 -0.3359 -0.1239 0.0723 23 VAL A N 170 C CA . VAL A 23 ? 1.0590 0.6198 0.6610 -0.3500 -0.1449 0.0949 23 VAL A CA 171 C C . VAL A 23 ? 1.2784 0.8286 0.9135 -0.3388 -0.1605 0.1177 23 VAL A C 172 O O . VAL A 23 ? 1.2759 0.8186 0.9464 -0.3210 -0.1577 0.1130 23 VAL A O 173 C CB . VAL A 23 ? 1.2621 0.8359 0.8505 -0.3620 -0.1578 0.0913 23 VAL A CB 174 C CG1 . VAL A 23 ? 1.1090 0.6928 0.6584 -0.3774 -0.1440 0.0686 23 VAL A CG1 175 C CG2 . VAL A 23 ? 1.0530 0.6246 0.6792 -0.3475 -0.1599 0.0835 23 VAL A CG2 176 N N . ASP A 24 ? 1.3486 0.8983 0.9727 -0.3498 -0.1759 0.1424 24 ASP A N 177 C CA . ASP A 24 ? 1.1565 0.6952 0.8159 -0.3405 -0.1940 0.1659 24 ASP A CA 178 C C . ASP A 24 ? 1.2066 0.7501 0.8470 -0.3588 -0.2172 0.1967 24 ASP A C 179 O O . ASP A 24 ? 1.4713 1.0250 1.0667 -0.3792 -0.2148 0.1996 24 ASP A O 180 C CB . ASP A 24 ? 1.2505 0.7698 0.9337 -0.3260 -0.1825 0.1635 24 ASP A CB 181 C CG . ASP A 24 ? 1.5949 1.1004 1.3254 -0.3103 -0.1959 0.1775 24 ASP A CG 182 O OD1 . ASP A 24 ? 1.5452 1.0544 1.2887 -0.3144 -0.2184 0.2002 24 ASP A OD1 183 O OD2 . ASP A 24 ? 1.7594 1.2509 1.5153 -0.2940 -0.1840 0.1652 24 ASP A OD2 184 N N . PHE A 25 ? 1.2611 0.7986 0.9375 -0.3516 -0.2393 0.2201 25 PHE A N 185 C CA . PHE A 25 ? 1.2025 0.7412 0.8696 -0.3670 -0.2651 0.2557 25 PHE A CA 186 C C . PHE A 25 ? 1.3417 0.8600 1.0158 -0.3672 -0.2634 0.2721 25 PHE A C 187 O O . PHE A 25 ? 1.3763 0.8760 1.0835 -0.3490 -0.2506 0.2602 25 PHE A O 188 C CB . PHE A 25 ? 1.1798 0.7214 0.8916 -0.3582 -0.2921 0.2758 25 PHE A CB 189 C CG . PHE A 25 ? 1.1865 0.7519 0.8855 -0.3673 -0.3038 0.2708 25 PHE A CG 190 C CD1 . PHE A 25 ? 1.2758 0.8577 0.9369 -0.3918 -0.3276 0.2928 25 PHE A CD1 191 C CD2 . PHE A 25 ? 1.4128 0.9844 1.1368 -0.3531 -0.2920 0.2450 25 PHE A CD2 192 C CE1 . PHE A 25 ? 1.3216 0.9253 0.9704 -0.4020 -0.3403 0.2864 25 PHE A CE1 193 C CE2 . PHE A 25 ? 1.2591 0.8515 0.9749 -0.3630 -0.3039 0.2401 25 PHE A CE2 194 C CZ . PHE A 25 ? 1.2049 0.8131 0.8833 -0.3874 -0.3286 0.2595 25 PHE A CZ 195 N N . PHE A 26 ? 1.2258 0.7480 0.8673 -0.3895 -0.2767 0.2996 26 PHE A N 196 C CA . PHE A 26 ? 1.4449 0.9472 1.0960 -0.3931 -0.2792 0.3213 26 PHE A CA 197 C C . PHE A 26 ? 1.4537 0.9503 1.1219 -0.4009 -0.3134 0.3654 26 PHE A C 198 O O . PHE A 26 ? 1.3250 0.8393 0.9533 -0.4240 -0.3302 0.3884 26 PHE A O 199 C CB . PHE A 26 ? 1.2587 0.7699 0.8579 -0.4144 -0.2606 0.3172 26 PHE A CB 200 C CG . PHE A 26 ? 1.2785 0.7708 0.8873 -0.4213 -0.2624 0.3401 26 PHE A CG 201 C CD1 . PHE A 26 ? 1.3415 0.8074 0.9973 -0.4018 -0.2558 0.3314 26 PHE A CD1 202 C CD2 . PHE A 26 ? 1.6491 1.1504 1.2185 -0.4492 -0.2703 0.3700 26 PHE A CD2 203 C CE1 . PHE A 26 ? 1.5140 0.9719 1.1866 -0.4027 -0.2558 0.3444 26 PHE A CE1 204 C CE2 . PHE A 26 ? 1.3394 0.8359 0.9286 -0.4486 -0.2692 0.3833 26 PHE A CE2 205 C CZ . PHE A 26 ? 1.3250 0.7988 0.9670 -0.4252 -0.2624 0.3704 26 PHE A CZ 206 N N . VAL A 27 ? 1.5776 1.0495 1.3059 -0.3818 -0.3239 0.3768 27 VAL A N 207 C CA . VAL A 27 ? 1.5562 1.0213 1.3163 -0.3836 -0.3572 0.4181 27 VAL A CA 208 C C . VAL A 27 ? 1.5500 1.0006 1.3450 -0.3738 -0.3555 0.4267 27 VAL A C 209 O O . VAL A 27 ? 1.6260 1.0578 1.4841 -0.3497 -0.3588 0.4236 27 VAL A O 210 C CB . VAL A 27 ? 1.4638 0.9273 1.2843 -0.3609 -0.3726 0.4178 27 VAL A CB 211 C CG1 . VAL A 27 ? 1.3095 0.8051 1.1047 -0.3720 -0.3881 0.4218 27 VAL A CG1 212 C CG2 . VAL A 27 ? 1.5710 1.0245 1.4259 -0.3339 -0.3448 0.3758 27 VAL A CG2 213 N N . PRO A 28 ? 1.3533 0.8128 1.1081 -0.3937 -0.3496 0.4370 28 PRO A N 214 C CA . PRO A 28 ? 1.3681 0.8136 1.1528 -0.3883 -0.3476 0.4462 28 PRO A CA 215 C C . PRO A 28 ? 1.4776 0.9171 1.3131 -0.3805 -0.3777 0.4793 28 PRO A C 216 O O . PRO A 28 ? 1.6256 1.0825 1.4516 -0.3914 -0.4031 0.5058 28 PRO A O 217 C CB . PRO A 28 ? 1.4962 0.9604 1.2210 -0.4166 -0.3375 0.4549 28 PRO A CB 218 C CG . PRO A 28 ? 1.5294 1.0196 1.1997 -0.4382 -0.3478 0.4651 28 PRO A CG 219 C CD . PRO A 28 ? 1.3766 0.8613 1.0571 -0.4240 -0.3456 0.4426 28 PRO A CD 220 N N . SER A 29 ? 1.6954 1.1106 1.5855 -0.3624 -0.3756 0.4769 29 SER A N 221 C CA . SER A 29 ? 1.6583 1.0650 1.6024 -0.3544 -0.4023 0.5074 29 SER A CA 222 C C . SER A 29 ? 1.6196 1.0378 1.5356 -0.3792 -0.4143 0.5412 29 SER A C 223 O O . SER A 29 ? 1.5314 0.9496 1.4792 -0.3804 -0.4409 0.5744 29 SER A O 224 C CB . SER A 29 ? 1.6859 1.0601 1.6976 -0.3271 -0.3936 0.4894 29 SER A CB 225 O OG . SER A 29 ? 2.0359 1.4017 2.0772 -0.3045 -0.3838 0.4604 29 SER A OG 226 N N . ALA A 30 ? 1.5479 0.9775 1.4059 -0.3993 -0.3940 0.5326 30 ALA A N 227 C CA . ALA A 30 ? 1.5656 1.0087 1.3909 -0.4251 -0.3995 0.5612 30 ALA A CA 228 C C . ALA A 30 ? 1.5794 1.0509 1.3700 -0.4470 -0.4257 0.5946 30 ALA A C 229 O O . ALA A 30 ? 1.8099 1.2884 1.5987 -0.4625 -0.4428 0.6287 30 ALA A O 230 C CB . ALA A 30 ? 1.6381 1.0912 1.4111 -0.4411 -0.3689 0.5406 30 ALA A CB 231 N N . SER A 31 ? 2.0953 1.5833 1.8576 -0.4496 -0.4294 0.5849 31 SER A N 232 C CA . SER A 31 ? 1.9042 1.4212 1.6277 -0.4726 -0.4542 0.6127 31 SER A CA 233 C C . SER A 31 ? 1.7523 1.2753 1.4919 -0.4623 -0.4726 0.6098 31 SER A C 234 O O . SER A 31 ? 1.5408 1.0460 1.3196 -0.4371 -0.4634 0.5850 31 SER A O 235 C CB . SER A 31 ? 1.8390 1.3828 1.4768 -0.5033 -0.4354 0.6047 31 SER A CB 236 O OG . SER A 31 ? 1.5804 1.1289 1.1852 -0.5013 -0.4165 0.5705 31 SER A OG 237 N N . SER A 32 ? 1.7234 1.2731 1.4321 -0.4832 -0.4983 0.6350 32 SER A N 238 C CA . SER A 32 ? 1.7043 1.2646 1.4260 -0.4779 -0.5199 0.6365 32 SER A CA 239 C C . SER A 32 ? 1.7091 1.2848 1.3630 -0.4920 -0.5030 0.6083 32 SER A C 240 O O . SER A 32 ? 1.8082 1.3892 1.4707 -0.4860 -0.5144 0.6012 32 SER A O 241 C CB . SER A 32 ? 1.6813 1.2636 1.4085 -0.4940 -0.5595 0.6784 32 SER A CB 242 O OG . SER A 32 ? 1.6990 1.2648 1.5010 -0.4774 -0.5781 0.7045 32 SER A OG 243 N N . ARG A 33 ? 1.7285 1.3117 1.3181 -0.5108 -0.4751 0.5917 33 ARG A N 244 C CA . ARG A 33 ? 1.5929 1.1901 1.1159 -0.5256 -0.4556 0.5624 33 ARG A CA 245 C C . ARG A 33 ? 1.5865 1.1597 1.1316 -0.5024 -0.4297 0.5260 33 ARG A C 246 O O . ARG A 33 ? 1.4975 1.0477 1.0819 -0.4833 -0.4118 0.5147 33 ARG A O 247 C CB . ARG A 33 ? 1.6246 1.2410 1.0756 -0.5537 -0.4327 0.5561 33 ARG A CB 248 C CG . ARG A 33 ? 1.8736 1.5196 1.2846 -0.5830 -0.4545 0.5865 33 ARG A CG 249 C CD . ARG A 33 ? 2.0621 1.7367 1.3854 -0.6124 -0.4347 0.5648 33 ARG A CD 250 N NE . ARG A 33 ? 2.1072 1.7798 1.4025 -0.6163 -0.3942 0.5397 33 ARG A NE 251 C CZ . ARG A 33 ? 2.2449 1.9321 1.5124 -0.6350 -0.3814 0.5508 33 ARG A CZ 252 N NH1 . ARG A 33 ? 2.1858 1.8888 1.4459 -0.6525 -0.4059 0.5872 33 ARG A NH1 253 N NH2 . ARG A 33 ? 2.2244 1.9115 1.4736 -0.6369 -0.3442 0.5267 33 ARG A NH2 254 N N . MET A 34 ? 1.8232 1.4022 1.3426 -0.5052 -0.4283 0.5072 34 MET A N 255 C CA . MET A 34 ? 1.4852 1.0483 1.0248 -0.4840 -0.4011 0.4673 34 MET A CA 256 C C . MET A 34 ? 1.4458 1.0294 0.9215 -0.4981 -0.3703 0.4289 34 MET A C 257 O O . MET A 34 ? 1.6446 1.2528 1.0602 -0.5242 -0.3777 0.4330 34 MET A O 258 C CB . MET A 34 ? 1.4244 0.9904 1.0182 -0.4617 -0.4169 0.4590 34 MET A CB 259 C CG . MET A 34 ? 1.7204 1.2709 1.3805 -0.4489 -0.4503 0.4988 34 MET A CG 260 S SD . MET A 34 ? 1.5398 1.0977 1.2742 -0.4211 -0.4650 0.4879 34 MET A SD 261 C CE . MET A 34 ? 1.4694 1.0085 1.2776 -0.4105 -0.5041 0.5408 34 MET A CE 262 N N . PHE A 35 ? 1.3977 0.9713 0.8870 -0.4811 -0.3364 0.3913 35 PHE A N 263 C CA . PHE A 35 ? 1.3913 0.9812 0.8297 -0.4919 -0.3049 0.3553 35 PHE A CA 264 C C . PHE A 35 ? 1.3769 0.9651 0.8409 -0.4688 -0.2841 0.3113 35 PHE A C 265 O O . PHE A 35 ? 1.3991 0.9718 0.9198 -0.4436 -0.2881 0.3073 35 PHE A O 266 C CB . PHE A 35 ? 1.4747 1.0578 0.8976 -0.4996 -0.2813 0.3559 35 PHE A CB 267 C CG . PHE A 35 ? 1.4551 1.0444 0.8404 -0.5284 -0.2958 0.3972 35 PHE A CG 268 C CD1 . PHE A 35 ? 1.4715 1.0449 0.8970 -0.5236 -0.3214 0.4358 35 PHE A CD1 269 C CD2 . PHE A 35 ? 1.4960 1.1112 0.8117 -0.5575 -0.2817 0.3931 35 PHE A CD2 270 C CE1 . PHE A 35 ? 1.5211 1.1124 0.9287 -0.5415 -0.3322 0.4636 35 PHE A CE1 271 C CE2 . PHE A 35 ? 2.0649 1.6950 1.3537 -0.5802 -0.2922 0.4251 35 PHE A CE2 272 C CZ . PHE A 35 ? 1.5604 1.1803 0.8991 -0.5704 -0.3177 0.4591 35 PHE A CZ 273 N N . LEU A 36 ? 1.3354 0.9397 0.7583 -0.4779 -0.2610 0.2785 36 LEU A N 274 C CA . LEU A 36 ? 1.4621 1.0633 0.9075 -0.4579 -0.2389 0.2381 36 LEU A CA 275 C C . LEU A 36 ? 1.4257 1.0188 0.8751 -0.4497 -0.2072 0.2176 36 LEU A C 276 O O . LEU A 36 ? 1.5715 1.1748 0.9832 -0.4671 -0.1925 0.2169 36 LEU A O 277 C CB . LEU A 36 ? 1.5071 1.1281 0.9146 -0.4707 -0.2347 0.2121 36 LEU A CB 278 C CG . LEU A 36 ? 1.5848 1.2183 0.9853 -0.4814 -0.2665 0.2267 36 LEU A CG 279 C CD1 . LEU A 36 ? 1.4395 1.0869 0.8127 -0.4897 -0.2573 0.1912 36 LEU A CD1 280 C CD2 . LEU A 36 ? 1.7284 1.3497 1.1941 -0.4588 -0.2868 0.2430 36 LEU A CD2 281 N N . LEU A 37 ? 1.3356 0.9128 0.8311 -0.4240 -0.1968 0.2014 37 LEU A N 282 C CA . LEU A 37 ? 1.2149 0.7865 0.7177 -0.4149 -0.1689 0.1795 37 LEU A CA 283 C C . LEU A 37 ? 1.3725 0.9509 0.8747 -0.4062 -0.1501 0.1431 37 LEU A C 284 O O . LEU A 37 ? 1.1422 0.7150 0.6722 -0.3909 -0.1551 0.1338 37 LEU A O 285 C CB . LEU A 37 ? 1.1882 0.7369 0.7387 -0.3945 -0.1703 0.1864 37 LEU A CB 286 C CG . LEU A 37 ? 1.2238 0.7600 0.7836 -0.4015 -0.1881 0.2213 37 LEU A CG 287 C CD1 . LEU A 37 ? 1.2660 0.7778 0.8721 -0.3815 -0.1857 0.2201 37 LEU A CD1 288 C CD2 . LEU A 37 ? 1.2149 0.7627 0.7340 -0.4263 -0.1808 0.2336 37 LEU A CD2 289 N N . VAL A 38 ? 1.4160 1.0071 0.8895 -0.4164 -0.1280 0.1232 38 VAL A N 290 C CA . VAL A 38 ? 1.1602 0.7557 0.6363 -0.4085 -0.1097 0.0888 38 VAL A CA 291 C C . VAL A 38 ? 1.1286 0.7234 0.6183 -0.3998 -0.0842 0.0715 38 VAL A C 292 O O . VAL A 38 ? 1.3126 0.9198 0.7802 -0.4131 -0.0701 0.0700 38 VAL A O 293 C CB . VAL A 38 ? 1.3179 0.9317 0.7497 -0.4287 -0.1065 0.0737 38 VAL A CB 294 C CG1 . VAL A 38 ? 1.3790 0.9924 0.8216 -0.4191 -0.0883 0.0375 38 VAL A CG1 295 C CG2 . VAL A 38 ? 1.2588 0.8765 0.6757 -0.4400 -0.1354 0.0927 38 VAL A CG2 296 N N . GLY A 39 ? 1.1487 0.7310 0.6756 -0.3782 -0.0787 0.0596 39 GLY A N 297 C CA . GLY A 39 ? 1.0852 0.6678 0.6295 -0.3688 -0.0581 0.0440 39 GLY A CA 298 C C . GLY A 39 ? 1.2214 0.8162 0.7557 -0.3718 -0.0388 0.0153 39 GLY A C 299 O O . GLY A 39 ? 1.1622 0.7564 0.6911 -0.3720 -0.0416 0.0021 39 GLY A O 300 N N . ALA A 40 ? 1.2020 0.8080 0.7373 -0.3745 -0.0189 0.0048 40 ALA A N 301 C CA . ALA A 40 ? 1.0950 0.7126 0.6281 -0.3755 0.0023 -0.0248 40 ALA A CA 302 C C . ALA A 40 ? 1.1015 0.7238 0.6679 -0.3638 0.0202 -0.0352 40 ALA A C 303 O O . ALA A 40 ? 1.1819 0.8220 0.7418 -0.3736 0.0361 -0.0386 40 ALA A O 304 C CB . ALA A 40 ? 1.1539 0.7911 0.6423 -0.3992 0.0113 -0.0309 40 ALA A CB 305 N N . PRO A 41 ? 1.2452 0.8538 0.8481 -0.3437 0.0172 -0.0388 41 PRO A N 306 C CA . PRO A 41 ? 1.2046 0.8189 0.8421 -0.3322 0.0304 -0.0469 41 PRO A CA 307 C C . PRO A 41 ? 1.4755 1.1041 1.1203 -0.3332 0.0531 -0.0746 41 PRO A C 308 O O . PRO A 41 ? 1.3769 1.0083 0.9958 -0.3433 0.0579 -0.0889 41 PRO A O 309 C CB . PRO A 41 ? 1.2241 0.8199 0.8906 -0.3130 0.0190 -0.0430 41 PRO A CB 310 C CG . PRO A 41 ? 1.2418 0.8235 0.8905 -0.3147 0.0007 -0.0301 41 PRO A CG 311 C CD . PRO A 41 ? 1.0722 0.6623 0.6866 -0.3318 0.0018 -0.0352 41 PRO A CD 312 N N . LYS A 42 ? 1.5952 1.2329 1.2765 -0.3231 0.0662 -0.0833 42 LYS A N 313 C CA . LYS A 42 ? 1.5944 1.2463 1.2917 -0.3219 0.0898 -0.1115 42 LYS A CA 314 C C . LYS A 42 ? 1.3556 1.0292 1.0156 -0.3432 0.1071 -0.1223 42 LYS A C 315 O O . LYS A 42 ? 1.5950 1.2770 1.2519 -0.3464 0.1261 -0.1504 42 LYS A O 316 C CB . LYS A 42 ? 1.1321 0.7669 0.8401 -0.3122 0.0889 -0.1301 42 LYS A CB 317 C CG . LYS A 42 ? 1.1121 0.7338 0.8695 -0.2906 0.0838 -0.1287 42 LYS A CG 318 C CD . LYS A 42 ? 1.1419 0.7477 0.9130 -0.2839 0.0867 -0.1489 42 LYS A CD 319 C CE . LYS A 42 ? 1.3144 0.9120 1.1410 -0.2638 0.0872 -0.1502 42 LYS A CE 320 N NZ . LYS A 42 ? 1.6575 1.2466 1.4950 -0.2543 0.0675 -0.1216 42 LYS A NZ 321 N N . ALA A 43 ? 1.2944 0.9764 0.9256 -0.3585 0.1010 -0.1002 43 ALA A N 322 C CA . ALA A 43 ? 1.2781 0.9817 0.8667 -0.3820 0.1155 -0.1044 43 ALA A CA 323 C C . ALA A 43 ? 1.3530 1.0827 0.9573 -0.3890 0.1338 -0.1002 43 ALA A C 324 O O . ALA A 43 ? 1.4848 1.2120 1.1080 -0.3864 0.1228 -0.0769 43 ALA A O 325 C CB . ALA A 43 ? 1.1930 0.8877 0.7342 -0.3980 0.0937 -0.0792 43 ALA A CB 326 N N . ASN A 44 ? 1.3296 1.0852 0.9268 -0.3989 0.1628 -0.1245 44 ASN A N 327 C CA . ASN A 44 ? 1.3845 1.1707 1.0004 -0.4068 0.1850 -0.1236 44 ASN A CA 328 C C . ASN A 44 ? 1.4134 1.2099 0.9900 -0.4312 0.1788 -0.0929 44 ASN A C 329 O O . ASN A 44 ? 1.4944 1.2920 1.0142 -0.4510 0.1754 -0.0867 44 ASN A O 330 C CB . ASN A 44 ? 1.4337 1.2464 1.0525 -0.4108 0.2208 -0.1613 44 ASN A CB 331 C CG . ASN A 44 ? 1.3972 1.2061 1.0804 -0.3844 0.2309 -0.1871 44 ASN A CG 332 O OD1 . ASN A 44 ? 1.3503 1.1501 1.0820 -0.3665 0.2171 -0.1731 44 ASN A OD1 333 N ND2 . ASN A 44 ? 1.5924 1.4073 1.2768 -0.3823 0.2540 -0.2248 44 ASN A ND2 334 N N . THR A 45 ? 1.4322 1.2354 1.0404 -0.4306 0.1756 -0.0723 45 THR A N 335 C CA . THR A 45 ? 1.4163 1.2248 0.9968 -0.4530 0.1675 -0.0398 45 THR A CA 336 C C . THR A 45 ? 1.2930 1.1391 0.8901 -0.4678 0.1949 -0.0398 45 THR A C 337 O O . THR A 45 ? 1.3157 1.1856 0.9497 -0.4591 0.2208 -0.0664 45 THR A O 338 C CB . THR A 45 ? 1.3462 1.1259 0.9471 -0.4437 0.1360 -0.0108 45 THR A CB 339 O OG1 . THR A 45 ? 1.2346 1.0187 0.8945 -0.4271 0.1384 -0.0163 45 THR A OG1 340 C CG2 . THR A 45 ? 1.5459 1.2917 1.1332 -0.4297 0.1107 -0.0094 45 THR A CG2 341 N N . THR A 46 ? 1.3177 1.1688 0.8922 -0.4901 0.1887 -0.0086 46 THR A N 342 C CA . THR A 46 ? 1.4343 1.3220 1.0229 -0.5083 0.2135 -0.0028 46 THR A CA 343 C C . THR A 46 ? 1.4110 1.2971 1.0622 -0.4979 0.2043 0.0096 46 THR A C 344 O O . THR A 46 ? 1.3294 1.2437 1.0025 -0.5127 0.2199 0.0190 46 THR A O 345 C CB . THR A 46 ? 1.3553 1.2505 0.8880 -0.5412 0.2117 0.0280 46 THR A CB 346 O OG1 . THR A 46 ? 1.4316 1.2912 0.9600 -0.5416 0.1752 0.0632 46 THR A OG1 347 C CG2 . THR A 46 ? 1.3671 1.2683 0.8333 -0.5548 0.2201 0.0155 46 THR A CG2 348 N N . GLN A 47 ? 1.4191 1.2734 1.0976 -0.4741 0.1784 0.0098 47 GLN A N 349 C CA . GLN A 47 ? 1.3678 1.2192 1.1030 -0.4630 0.1668 0.0177 47 GLN A CA 350 C C . GLN A 47 ? 1.2901 1.1767 1.0802 -0.4528 0.1924 -0.0068 47 GLN A C 351 O O . GLN A 47 ? 1.2396 1.1280 1.0435 -0.4345 0.2022 -0.0337 47 GLN A O 352 C CB . GLN A 47 ? 1.2019 1.0132 0.9463 -0.4405 0.1355 0.0203 47 GLN A CB 353 C CG . GLN A 47 ? 1.2107 0.9879 0.9087 -0.4467 0.1112 0.0413 47 GLN A CG 354 C CD . GLN A 47 ? 1.4042 1.1463 1.1111 -0.4238 0.0859 0.0391 47 GLN A CD 355 O OE1 . GLN A 47 ? 1.6948 1.4214 1.3764 -0.4155 0.0803 0.0310 47 GLN A OE1 356 N NE2 . GLN A 47 ? 1.2688 0.9997 1.0111 -0.4151 0.0709 0.0458 47 GLN A NE2 357 N N . PRO A 48 ? 1.2764 1.1913 1.1027 -0.4650 0.2027 0.0033 48 PRO A N 358 C CA . PRO A 48 ? 1.1767 1.1323 1.0626 -0.4580 0.2287 -0.0169 48 PRO A CA 359 C C . PRO A 48 ? 1.1577 1.1038 1.0981 -0.4278 0.2154 -0.0316 48 PRO A C 360 O O . PRO A 48 ? 1.2022 1.1238 1.1576 -0.4194 0.1851 -0.0165 48 PRO A O 361 C CB . PRO A 48 ? 1.1719 1.1503 1.0850 -0.4787 0.2303 0.0063 48 PRO A CB 362 C CG . PRO A 48 ? 1.2540 1.2114 1.1074 -0.5028 0.2181 0.0347 48 PRO A CG 363 C CD . PRO A 48 ? 1.2145 1.1245 1.0300 -0.4877 0.1899 0.0362 48 PRO A CD 364 N N . GLY A 49 ? 1.1631 1.1292 1.1333 -0.4126 0.2382 -0.0608 49 GLY A N 365 C CA . GLY A 49 ? 1.1870 1.1466 1.2125 -0.3844 0.2268 -0.0729 49 GLY A CA 366 C C . GLY A 49 ? 1.1775 1.0922 1.1749 -0.3669 0.2019 -0.0745 49 GLY A C 367 O O . GLY A 49 ? 1.2156 1.1215 1.2526 -0.3442 0.1912 -0.0823 49 GLY A O 368 N N . ILE A 50 ? 1.1714 1.0591 1.1026 -0.3780 0.1924 -0.0654 50 ILE A N 369 C CA . ILE A 50 ? 1.2826 1.1296 1.1866 -0.3638 0.1688 -0.0646 50 ILE A CA 370 C C . ILE A 50 ? 1.3086 1.1502 1.1879 -0.3585 0.1846 -0.0898 50 ILE A C 371 O O . ILE A 50 ? 1.4656 1.3181 1.3027 -0.3758 0.2026 -0.0970 50 ILE A O 372 C CB . ILE A 50 ? 1.1579 0.9763 1.0119 -0.3768 0.1448 -0.0389 50 ILE A CB 373 C CG1 . ILE A 50 ? 1.0860 0.9051 0.9651 -0.3827 0.1280 -0.0167 50 ILE A CG1 374 C CG2 . ILE A 50 ? 1.0689 0.8495 0.9003 -0.3618 0.1227 -0.0389 50 ILE A CG2 375 C CD1 . ILE A 50 ? 1.1056 0.9178 1.0311 -0.3624 0.1104 -0.0181 50 ILE A CD1 376 N N . VAL A 51 ? 1.1195 0.9438 1.0240 -0.3361 0.1769 -0.1026 51 VAL A N 377 C CA . VAL A 51 ? 1.1438 0.9576 1.0302 -0.3300 0.1886 -0.1276 51 VAL A CA 378 C C . VAL A 51 ? 1.1630 0.9378 1.0112 -0.3255 0.1626 -0.1177 51 VAL A C 379 O O . VAL A 51 ? 1.0787 0.8332 0.9462 -0.3111 0.1398 -0.1046 51 VAL A O 380 C CB . VAL A 51 ? 1.1632 0.9852 1.1120 -0.3083 0.2016 -0.1511 51 VAL A CB 381 C CG1 . VAL A 51 ? 1.1709 0.9774 1.1019 -0.3032 0.2126 -0.1786 51 VAL A CG1 382 C CG2 . VAL A 51 ? 1.2675 1.1319 1.2622 -0.3113 0.2294 -0.1628 51 VAL A CG2 383 N N . GLU A 52 ? 1.2280 0.9953 1.0222 -0.3388 0.1665 -0.1240 52 GLU A N 384 C CA . GLU A 52 ? 1.3335 1.0685 1.0918 -0.3370 0.1434 -0.1149 52 GLU A CA 385 C C . GLU A 52 ? 1.1992 0.9158 0.9552 -0.3346 0.1155 -0.0845 52 GLU A C 386 O O . GLU A 52 ? 1.2353 0.9309 1.0092 -0.3185 0.0983 -0.0793 52 GLU A O 387 C CB . GLU A 52 ? 1.2595 0.9764 1.0418 -0.3181 0.1419 -0.1340 52 GLU A CB 388 C CG . GLU A 52 ? 1.4726 1.1998 1.2522 -0.3209 0.1675 -0.1682 52 GLU A CG 389 C CD . GLU A 52 ? 1.6440 1.3481 1.4498 -0.3033 0.1635 -0.1852 52 GLU A CD 390 O OE1 . GLU A 52 ? 1.6426 1.3272 1.4728 -0.2883 0.1428 -0.1685 52 GLU A OE1 391 O OE2 . GLU A 52 ? 1.8328 1.5381 1.6341 -0.3056 0.1814 -0.2155 52 GLU A OE2 392 N N . GLY A 53 ? 1.1899 0.9142 0.9241 -0.3514 0.1120 -0.0649 53 GLY A N 393 C CA . GLY A 53 ? 1.0770 0.7827 0.8101 -0.3504 0.0873 -0.0390 53 GLY A CA 394 C C . GLY A 53 ? 1.0644 0.7430 0.7614 -0.3507 0.0679 -0.0291 53 GLY A C 395 O O . GLY A 53 ? 1.0082 0.6655 0.7111 -0.3418 0.0477 -0.0157 53 GLY A O 396 N N . GLY A 54 ? 1.0712 0.7527 0.7318 -0.3615 0.0744 -0.0369 54 GLY A N 397 C CA . GLY A 54 ? 1.1561 0.8167 0.7848 -0.3638 0.0556 -0.0266 54 GLY A CA 398 C C . GLY A 54 ? 1.1505 0.8113 0.7464 -0.3831 0.0454 -0.0016 54 GLY A C 399 O O . GLY A 54 ? 1.2155 0.8822 0.8210 -0.3902 0.0457 0.0135 54 GLY A O 400 N N . GLN A 55 ? 1.1892 0.8434 0.7490 -0.3923 0.0347 0.0043 55 GLN A N 401 C CA . GLN A 55 ? 1.2349 0.8879 0.7641 -0.4108 0.0214 0.0318 55 GLN A CA 402 C C . GLN A 55 ? 1.1845 0.8137 0.7096 -0.4045 -0.0056 0.0485 55 GLN A C 403 O O . GLN A 55 ? 1.2567 0.8725 0.7993 -0.3874 -0.0119 0.0375 55 GLN A O 404 C CB . GLN A 55 ? 1.2750 0.9506 0.7581 -0.4344 0.0340 0.0275 55 GLN A CB 405 C CG . GLN A 55 ? 1.4678 1.1719 0.9520 -0.4452 0.0630 0.0149 55 GLN A CG 406 C CD . GLN A 55 ? 1.6368 1.3644 1.0681 -0.4708 0.0766 0.0102 55 GLN A CD 407 O OE1 . GLN A 55 ? 1.6009 1.3234 0.9944 -0.4793 0.0638 0.0117 55 GLN A OE1 408 N NE2 . GLN A 55 ? 1.7749 1.5306 1.2027 -0.4846 0.1027 0.0045 55 GLN A NE2 409 N N . VAL A 56 ? 1.3068 0.9317 0.8122 -0.4189 -0.0211 0.0765 56 VAL A N 410 C CA . VAL A 56 ? 1.1365 0.7449 0.6345 -0.4173 -0.0465 0.0940 56 VAL A CA 411 C C . VAL A 56 ? 1.1923 0.8133 0.6462 -0.4430 -0.0538 0.1143 56 VAL A C 412 O O . VAL A 56 ? 1.2187 0.8443 0.6639 -0.4581 -0.0532 0.1355 56 VAL A O 413 C CB . VAL A 56 ? 1.1154 0.6994 0.6466 -0.4045 -0.0640 0.1132 56 VAL A CB 414 C CG1 . VAL A 56 ? 1.1259 0.6966 0.6541 -0.4037 -0.0893 0.1327 56 VAL A CG1 415 C CG2 . VAL A 56 ? 1.0730 0.6464 0.6407 -0.3813 -0.0577 0.0938 56 VAL A CG2 416 N N . LEU A 57 ? 1.2058 0.8332 0.6312 -0.4500 -0.0614 0.1090 57 LEU A N 417 C CA . LEU A 57 ? 1.3252 0.9685 0.7007 -0.4773 -0.0682 0.1262 57 LEU A CA 418 C C . LEU A 57 ? 1.4542 1.0846 0.8278 -0.4808 -0.1019 0.1598 57 LEU A C 419 O O . LEU A 57 ? 1.5692 1.1844 0.9713 -0.4632 -0.1177 0.1586 57 LEU A O 420 C CB . LEU A 57 ? 1.3347 0.9976 0.6727 -0.4880 -0.0546 0.0969 57 LEU A CB 421 C CG . LEU A 57 ? 1.3776 1.0580 0.7144 -0.4888 -0.0190 0.0646 57 LEU A CG 422 C CD1 . LEU A 57 ? 1.2692 0.9386 0.6480 -0.4627 -0.0083 0.0333 57 LEU A CD1 423 C CD2 . LEU A 57 ? 1.5184 1.2247 0.7982 -0.5142 -0.0046 0.0492 57 LEU A CD2 424 N N . LYS A 58 ? 1.4135 1.0513 0.7563 -0.5039 -0.1127 0.1913 58 LYS A N 425 C CA . LYS A 58 ? 1.3425 0.9705 0.6837 -0.5097 -0.1469 0.2274 58 LYS A CA 426 C C . LYS A 58 ? 1.4215 1.0707 0.7075 -0.5326 -0.1576 0.2297 58 LYS A C 427 O O . LYS A 58 ? 1.5706 1.2406 0.8054 -0.5593 -0.1486 0.2362 58 LYS A O 428 C CB . LYS A 58 ? 1.5093 1.1279 0.8564 -0.5209 -0.1573 0.2668 58 LYS A CB 429 C CG . LYS A 58 ? 1.4923 1.0945 0.8556 -0.5209 -0.1946 0.3064 58 LYS A CG 430 C CD . LYS A 58 ? 1.4146 1.0061 0.7830 -0.5348 -0.2046 0.3468 58 LYS A CD 431 C CE . LYS A 58 ? 1.8065 1.4246 1.1114 -0.5702 -0.1978 0.3640 58 LYS A CE 432 N NZ . LYS A 58 ? 1.9181 1.5385 1.2466 -0.5732 -0.2095 0.3951 58 LYS A NZ 433 N N . CYS A 59 ? 1.5450 1.1904 0.8409 -0.5234 -0.1762 0.2234 59 CYS A N 434 C CA . CYS A 59 ? 1.7481 1.4128 0.9946 -0.5450 -0.1908 0.2238 59 CYS A CA 435 C C . CYS A 59 ? 1.5494 1.2096 0.8003 -0.5522 -0.2315 0.2686 59 CYS A C 436 O O . CYS A 59 ? 1.4898 1.1297 0.7968 -0.5307 -0.2486 0.2842 59 CYS A O 437 C CB . CYS A 59 ? 1.9123 1.5787 1.1674 -0.5329 -0.1845 0.1847 59 CYS A CB 438 S SG . CYS A 59 ? 1.5862 1.2553 0.8462 -0.5215 -0.1396 0.1329 59 CYS A SG 439 N N . ASP A 60 ? 1.5196 1.1998 0.7125 -0.5827 -0.2472 0.2889 60 ASP A N 440 C CA . ASP A 60 ? 1.5536 1.2314 0.7502 -0.5921 -0.2884 0.3376 60 ASP A CA 441 C C . ASP A 60 ? 1.7151 1.4079 0.8921 -0.6017 -0.3160 0.3366 60 ASP A C 442 O O . ASP A 60 ? 1.7770 1.4873 0.9112 -0.6139 -0.3031 0.3023 60 ASP A O 443 C CB . ASP A 60 ? 1.8926 1.5809 1.0405 -0.6224 -0.2931 0.3753 60 ASP A CB 444 C CG . ASP A 60 ? 2.0251 1.7447 1.0927 -0.6531 -0.2729 0.3545 60 ASP A CG 445 O OD1 . ASP A 60 ? 2.0681 1.8082 1.1013 -0.6685 -0.2903 0.3504 60 ASP A OD1 446 O OD2 . ASP A 60 ? 2.0526 1.7797 1.1023 -0.6591 -0.2378 0.3376 60 ASP A OD2 447 N N . TRP A 61 ? 1.8233 1.5088 1.0368 -0.5958 -0.3546 0.3736 61 TRP A N 448 C CA . TRP A 61 ? 1.6253 1.3266 0.8295 -0.6052 -0.3873 0.3799 61 TRP A CA 449 C C . TRP A 61 ? 1.7253 1.4495 0.8637 -0.6422 -0.4122 0.4143 61 TRP A C 450 O O . TRP A 61 ? 2.0328 1.7751 1.1680 -0.6525 -0.4424 0.4246 61 TRP A O 451 C CB . TRP A 61 ? 1.5746 1.2610 0.8599 -0.5789 -0.4159 0.4015 61 TRP A CB 452 C CG . TRP A 61 ? 1.6336 1.3370 0.9250 -0.5824 -0.4428 0.3965 61 TRP A CG 453 C CD1 . TRP A 61 ? 1.6330 1.3416 0.9327 -0.5736 -0.4288 0.3531 61 TRP A CD1 454 C CD2 . TRP A 61 ? 1.7468 1.4649 1.0397 -0.5969 -0.4903 0.4379 61 TRP A CD2 455 N NE1 . TRP A 61 ? 1.7214 1.4475 1.0277 -0.5825 -0.4637 0.3632 61 TRP A NE1 456 C CE2 . TRP A 61 ? 1.8553 1.5889 1.1578 -0.5966 -0.5025 0.4151 61 TRP A CE2 457 C CE3 . TRP A 61 ? 2.0668 1.7873 1.3599 -0.6097 -0.5237 0.4921 61 TRP A CE3 458 C CZ2 . TRP A 61 ? 2.0395 1.7925 1.3491 -0.6096 -0.5488 0.4453 61 TRP A CZ2 459 C CZ3 . TRP A 61 ? 2.1852 1.9270 1.4988 -0.6177 -0.5632 0.5161 61 TRP A CZ3 460 C CH2 . TRP A 61 ? 2.1709 1.9278 1.4849 -0.6199 -0.5793 0.4970 61 TRP A CH2 461 N N . SER A 62 ? 1.7438 1.4751 0.8574 -0.6545 -0.3908 0.4201 62 SER A N 462 C CA . SER A 62 ? 2.0528 1.8127 1.1298 -0.6817 -0.4014 0.4413 62 SER A CA 463 C C . SER A 62 ? 2.3220 2.1112 1.3334 -0.7065 -0.3959 0.4115 62 SER A C 464 O O . SER A 62 ? 2.2523 2.0670 1.2254 -0.7316 -0.4035 0.4257 62 SER A O 465 C CB . SER A 62 ? 2.1244 1.8869 1.1881 -0.6893 -0.3745 0.4481 62 SER A CB 466 O OG . SER A 62 ? 1.8740 1.6652 0.8968 -0.7174 -0.3827 0.4679 62 SER A OG 467 N N . SER A 63 ? 2.5163 2.3005 1.5158 -0.6992 -0.3802 0.3682 63 SER A N 468 C CA . SER A 63 ? 2.6663 2.4723 1.6191 -0.7164 -0.3767 0.3324 63 SER A CA 469 C C . SER A 63 ? 2.7348 2.5592 1.6270 -0.7348 -0.3344 0.2959 63 SER A C 470 O O . SER A 63 ? 2.6967 2.5375 1.5504 -0.7479 -0.3238 0.2592 63 SER A O 471 C CB . SER A 63 ? 2.5746 2.4013 1.5220 -0.7334 -0.4168 0.3616 63 SER A CB 472 O OG . SER A 63 ? 2.5097 2.3551 1.4158 -0.7489 -0.4129 0.3251 63 SER A OG 473 N N . THR A 64 ? 2.6672 2.4895 1.5561 -0.7350 -0.3095 0.3047 64 THR A N 474 C CA . THR A 64 ? 2.4057 2.2448 1.2483 -0.7478 -0.2646 0.2670 64 THR A CA 475 C C . THR A 64 ? 2.1422 1.9648 0.9945 -0.7295 -0.2347 0.2171 64 THR A C 476 O O . THR A 64 ? 2.0916 1.9272 0.9122 -0.7365 -0.1972 0.1741 64 THR A O 477 C CB . THR A 64 ? 2.2737 2.1172 1.1171 -0.7528 -0.2465 0.2910 64 THR A CB 478 O OG1 . THR A 64 ? 2.3046 2.1694 1.1051 -0.7661 -0.2023 0.2530 64 THR A OG1 479 C CG2 . THR A 64 ? 2.0151 1.8269 0.9152 -0.7263 -0.2433 0.3051 64 THR A CG2 480 N N . ARG A 65 ? 1.9231 1.7172 0.8224 -0.7056 -0.2518 0.2234 65 ARG A N 481 C CA . ARG A 65 ? 2.0502 1.8276 0.9808 -0.6820 -0.2289 0.1770 65 ARG A CA 482 C C . ARG A 65 ? 2.1030 1.8773 1.0458 -0.6707 -0.1826 0.1513 65 ARG A C 483 O O . ARG A 65 ? 2.1544 1.9267 1.1085 -0.6589 -0.1530 0.1032 65 ARG A O 484 C CB . ARG A 65 ? 2.2565 2.0460 1.1503 -0.6950 -0.2279 0.1341 65 ARG A CB 485 C CG . ARG A 65 ? 2.0574 1.8277 1.0144 -0.6668 -0.2315 0.1072 65 ARG A CG 486 C CD . ARG A 65 ? 1.9906 1.7485 1.0038 -0.6507 -0.2710 0.1482 65 ARG A CD 487 N NE . ARG A 65 ? 2.2277 2.0029 1.2018 -0.6772 -0.3130 0.1852 65 ARG A NE 488 C CZ . ARG A 65 ? 2.2833 2.0690 1.2467 -0.6889 -0.3403 0.1780 65 ARG A CZ 489 N NH1 . ARG A 65 ? 1.9983 1.7768 0.9859 -0.6775 -0.3294 0.1347 65 ARG A NH1 490 N NH2 . ARG A 65 ? 2.3006 2.1051 1.2541 -0.7047 -0.3719 0.2136 65 ARG A NH2 491 N N . ARG A 66 ? 1.9645 1.7383 0.9100 -0.6743 -0.1781 0.1851 66 ARG A N 492 C CA . ARG A 66 ? 1.7032 1.4791 0.6592 -0.6677 -0.1366 0.1664 66 ARG A CA 493 C C . ARG A 66 ? 1.7107 1.4594 0.7457 -0.6347 -0.1352 0.1780 66 ARG A C 494 O O . ARG A 66 ? 1.5830 1.3141 0.6525 -0.6250 -0.1658 0.2153 66 ARG A O 495 C CB . ARG A 66 ? 1.7380 1.5373 0.6348 -0.7005 -0.1275 0.1925 66 ARG A CB 496 C CG . ARG A 66 ? 1.9657 1.7720 0.8761 -0.6969 -0.0857 0.1783 66 ARG A CG 497 C CD . ARG A 66 ? 2.2016 2.0376 1.0787 -0.7228 -0.0771 0.1998 66 ARG A CD 498 N NE . ARG A 66 ? 2.1471 1.9866 1.0474 -0.7197 -0.0463 0.2019 66 ARG A NE 499 C CZ . ARG A 66 ? 2.1241 1.9895 1.0108 -0.7374 -0.0339 0.2181 66 ARG A CZ 500 N NH1 . ARG A 66 ? 2.1402 2.0290 0.9860 -0.7599 -0.0490 0.2343 66 ARG A NH1 501 N NH2 . ARG A 66 ? 2.0684 1.9373 0.9833 -0.7334 -0.0068 0.2189 66 ARG A NH2 502 N N . CYS A 67 ? 1.7827 1.5287 0.8475 -0.6175 -0.1000 0.1447 67 CYS A N 503 C CA . CYS A 67 ? 1.5990 1.3220 0.7324 -0.5888 -0.0960 0.1516 67 CYS A CA 504 C C . CYS A 67 ? 1.7842 1.5173 0.9190 -0.5948 -0.0670 0.1535 67 CYS A C 505 O O . CYS A 67 ? 1.7922 1.5494 0.8929 -0.6094 -0.0369 0.1282 67 CYS A O 506 C CB . CYS A 67 ? 1.5286 1.2370 0.7087 -0.5595 -0.0853 0.1132 67 CYS A CB 507 S SG . CYS A 67 ? 2.1688 1.8711 1.3464 -0.5559 -0.1125 0.1024 67 CYS A SG 508 N N . GLN A 68 ? 1.8149 1.5305 0.9917 -0.5838 -0.0756 0.1820 68 GLN A N 509 C CA . GLN A 68 ? 1.5302 1.2538 0.7191 -0.5879 -0.0503 0.1846 68 GLN A CA 510 C C . GLN A 68 ? 1.4611 1.1624 0.7186 -0.5568 -0.0451 0.1736 68 GLN A C 511 O O . GLN A 68 ? 1.6010 1.2760 0.8951 -0.5383 -0.0692 0.1872 68 GLN A O 512 C CB . GLN A 68 ? 1.6422 1.3675 0.8107 -0.6116 -0.0656 0.2338 68 GLN A CB 513 C CG . GLN A 68 ? 2.0058 1.7564 1.0994 -0.6468 -0.0708 0.2501 68 GLN A CG 514 C CD . GLN A 68 ? 2.1276 1.9134 1.1788 -0.6674 -0.0307 0.2241 68 GLN A CD 515 O OE1 . GLN A 68 ? 2.1358 1.9406 1.1461 -0.6757 -0.0167 0.1908 68 GLN A OE1 516 N NE2 . GLN A 68 ? 2.0413 1.8364 1.1045 -0.6764 -0.0110 0.2378 68 GLN A NE2 517 N N . PRO A 69 ? 1.4479 1.1616 0.7240 -0.5515 -0.0136 0.1487 69 PRO A N 518 C CA . PRO A 69 ? 1.3225 1.0183 0.6601 -0.5248 -0.0095 0.1393 69 PRO A CA 519 C C . PRO A 69 ? 1.3184 0.9971 0.6813 -0.5268 -0.0253 0.1755 69 PRO A C 520 O O . PRO A 69 ? 1.3589 1.0502 0.7000 -0.5504 -0.0216 0.1997 69 PRO A O 521 C CB . PRO A 69 ? 1.3180 1.0383 0.6642 -0.5245 0.0272 0.1074 69 PRO A CB 522 C CG . PRO A 69 ? 1.4454 1.1915 0.7381 -0.5438 0.0434 0.0882 69 PRO A CG 523 C CD . PRO A 69 ? 1.5912 1.3381 0.8340 -0.5686 0.0203 0.1236 69 PRO A CD 524 N N . ILE A 70 ? 1.3754 1.0256 0.7834 -0.5033 -0.0419 0.1787 70 ILE A N 525 C CA . ILE A 70 ? 1.2988 0.9282 0.7367 -0.5028 -0.0565 0.2073 70 ILE A CA 526 C C . ILE A 70 ? 1.2703 0.9054 0.7412 -0.4982 -0.0364 0.1946 70 ILE A C 527 O O . ILE A 70 ? 1.5964 1.2346 1.0910 -0.4796 -0.0230 0.1643 70 ILE A O 528 C CB . ILE A 70 ? 1.2435 0.8400 0.7155 -0.4801 -0.0821 0.2136 70 ILE A CB 529 C CG1 . ILE A 70 ? 1.2649 0.8588 0.7124 -0.4835 -0.1037 0.2265 70 ILE A CG1 530 C CG2 . ILE A 70 ? 1.2457 0.8180 0.7499 -0.4802 -0.0966 0.2401 70 ILE A CG2 531 C CD1 . ILE A 70 ? 1.2387 0.8047 0.7242 -0.4610 -0.1266 0.2320 70 ILE A CD1 532 N N . GLU A 71 ? 1.2995 0.9365 0.7742 -0.5160 -0.0357 0.2195 71 GLU A N 533 C CA . GLU A 71 ? 1.4565 1.1002 0.9667 -0.5139 -0.0197 0.2102 71 GLU A CA 534 C C . GLU A 71 ? 1.5751 1.1856 1.1317 -0.4931 -0.0374 0.2102 71 GLU A C 535 O O . GLU A 71 ? 1.5886 1.1724 1.1555 -0.4957 -0.0593 0.2360 71 GLU A O 536 C CB . GLU A 71 ? 1.6502 1.3099 1.1494 -0.5433 -0.0115 0.2371 71 GLU A CB 537 C CG . GLU A 71 ? 2.0400 1.7356 1.4870 -0.5680 0.0083 0.2383 71 GLU A CG 538 C CD . GLU A 71 ? 2.1207 1.8089 1.5210 -0.5833 -0.0128 0.2666 71 GLU A CD 539 O OE1 . GLU A 71 ? 2.0437 1.7002 1.4565 -0.5697 -0.0418 0.2797 71 GLU A OE1 540 O OE2 . GLU A 71 ? 2.0364 1.7524 1.3878 -0.6096 -0.0004 0.2759 71 GLU A OE2 541 N N . PHE A 72 ? 1.5643 1.1766 1.1490 -0.4729 -0.0278 0.1810 72 PHE A N 542 C CA . PHE A 72 ? 1.4441 1.0287 1.0675 -0.4540 -0.0418 0.1760 72 PHE A CA 543 C C . PHE A 72 ? 1.3916 0.9874 1.0469 -0.4566 -0.0306 0.1680 72 PHE A C 544 O O . PHE A 72 ? 1.5269 1.1071 1.2034 -0.4642 -0.0410 0.1834 72 PHE A O 545 C CB . PHE A 72 ? 1.3318 0.9075 0.9609 -0.4285 -0.0446 0.1516 72 PHE A CB 546 C CG . PHE A 72 ? 1.5100 1.0647 1.1265 -0.4213 -0.0636 0.1617 72 PHE A CG 547 C CD1 . PHE A 72 ? 1.3936 0.9172 1.0329 -0.4114 -0.0833 0.1723 72 PHE A CD1 548 C CD2 . PHE A 72 ? 1.6652 1.2322 1.2505 -0.4240 -0.0617 0.1583 72 PHE A CD2 549 C CE1 . PHE A 72 ? 1.5328 1.0404 1.1686 -0.4034 -0.1000 0.1813 72 PHE A CE1 550 C CE2 . PHE A 72 ? 1.4566 1.0077 1.0359 -0.4177 -0.0809 0.1684 72 PHE A CE2 551 C CZ . PHE A 72 ? 1.4174 0.9398 1.0242 -0.4067 -0.0997 0.1808 72 PHE A CZ 552 N N . ASP A 73 ? 1.2452 0.8678 0.9077 -0.4503 -0.0106 0.1438 73 ASP A N 553 C CA . ASP A 73 ? 1.1661 0.8054 0.8637 -0.4518 -0.0001 0.1353 73 ASP A CA 554 C C . ASP A 73 ? 1.6223 1.2964 1.3137 -0.4755 0.0216 0.1431 73 ASP A C 555 O O . ASP A 73 ? 2.1515 1.8284 1.8598 -0.4921 0.0203 0.1604 73 ASP A O 556 C CB . ASP A 73 ? 1.3605 1.0095 1.0789 -0.4298 0.0075 0.1066 73 ASP A CB 557 C CG . ASP A 73 ? 1.4569 1.1249 1.2165 -0.4304 0.0144 0.0993 73 ASP A CG 558 O OD1 . ASP A 73 ? 1.5364 1.1999 1.3122 -0.4441 0.0070 0.1146 73 ASP A OD1 559 O OD2 . ASP A 73 ? 1.8409 1.5280 1.6200 -0.4175 0.0258 0.0791 73 ASP A OD2 560 N N . ALA A 74 ? 1.1524 0.8534 0.8215 -0.4774 0.0428 0.1283 74 ALA A N 561 C CA . ALA A 74 ? 1.5200 1.2585 1.1767 -0.5003 0.0685 0.1316 74 ALA A CA 562 C C . ALA A 74 ? 1.1930 0.9603 0.8970 -0.5019 0.0856 0.1219 74 ALA A C 563 O O . ALA A 74 ? 1.1792 0.9824 0.8817 -0.5196 0.1108 0.1216 74 ALA A O 564 C CB . ALA A 74 ? 1.2115 0.9442 0.8378 -0.5273 0.0605 0.1668 74 ALA A CB 565 N N . THR A 75 ? 1.2046 0.9582 0.9503 -0.4844 0.0719 0.1141 75 THR A N 566 C CA . THR A 75 ? 1.2010 0.9814 0.9972 -0.4850 0.0825 0.1064 75 THR A CA 567 C C . THR A 75 ? 1.2367 1.0258 1.0629 -0.4590 0.0868 0.0783 75 THR A C 568 O O . THR A 75 ? 1.2030 0.9682 1.0150 -0.4399 0.0750 0.0681 75 THR A O 569 C CB . THR A 75 ? 1.1029 0.8626 0.9273 -0.4909 0.0598 0.1237 75 THR A CB 570 O OG1 . THR A 75 ? 1.2624 0.9891 1.0941 -0.4685 0.0361 0.1147 75 THR A OG1 571 C CG2 . THR A 75 ? 1.2736 1.0141 1.0709 -0.5136 0.0499 0.1541 75 THR A CG2 572 N N . GLY A 76 ? 1.2950 1.1195 1.1664 -0.4588 0.1033 0.0677 76 GLY A N 573 C CA . GLY A 76 ? 1.1114 0.9466 1.0193 -0.4349 0.1066 0.0446 76 GLY A CA 574 C C . GLY A 76 ? 1.0857 0.9017 1.0246 -0.4219 0.0789 0.0476 76 GLY A C 575 O O . GLY A 76 ? 1.1359 0.9186 1.0555 -0.4248 0.0555 0.0611 76 GLY A O 576 N N . ASN A 77 ? 1.0203 0.8578 1.0077 -0.4077 0.0812 0.0346 77 ASN A N 577 C CA . ASN A 77 ? 1.0907 0.9148 1.1055 -0.3962 0.0544 0.0367 77 ASN A CA 578 C C . ASN A 77 ? 1.2661 1.1013 1.3126 -0.4130 0.0431 0.0501 77 ASN A C 579 O O . ASN A 77 ? 1.0642 0.9377 1.1491 -0.4244 0.0596 0.0511 77 ASN A O 580 C CB . ASN A 77 ? 1.1272 0.9699 1.1831 -0.3746 0.0578 0.0209 77 ASN A CB 581 C CG . ASN A 77 ? 1.0214 0.8463 1.0501 -0.3571 0.0635 0.0077 77 ASN A CG 582 O OD1 . ASN A 77 ? 1.0294 0.8196 1.0131 -0.3544 0.0510 0.0115 77 ASN A OD1 583 N ND2 . ASN A 77 ? 1.2992 1.1477 1.3590 -0.3450 0.0829 -0.0086 77 ASN A ND2 584 N N . ARG A 78 ? 1.3087 1.1107 1.3412 -0.4150 0.0158 0.0587 78 ARG A N 585 C CA . ARG A 78 ? 1.0802 0.8874 1.1443 -0.4296 -0.0001 0.0680 78 ARG A CA 586 C C . ARG A 78 ? 1.1807 1.0140 1.2954 -0.4183 -0.0094 0.0598 78 ARG A C 587 O O . ARG A 78 ? 1.2537 1.0867 1.3705 -0.3970 -0.0113 0.0493 78 ARG A O 588 C CB . ARG A 78 ? 0.9928 0.7540 1.0268 -0.4333 -0.0262 0.0747 78 ARG A CB 589 C CG . ARG A 78 ? 1.0371 0.7742 1.0346 -0.4484 -0.0218 0.0888 78 ARG A CG 590 C CD . ARG A 78 ? 1.0195 0.7085 0.9918 -0.4462 -0.0463 0.0912 78 ARG A CD 591 N NE . ARG A 78 ? 1.0037 0.6707 0.9458 -0.4235 -0.0514 0.0798 78 ARG A NE 592 C CZ . ARG A 78 ? 1.3050 0.9319 1.2206 -0.4175 -0.0668 0.0792 78 ARG A CZ 593 N NH1 . ARG A 78 ? 1.1424 0.7436 1.0591 -0.4313 -0.0795 0.0884 78 ARG A NH1 594 N NH2 . ARG A 78 ? 1.2036 0.8163 1.0955 -0.3978 -0.0686 0.0692 78 ARG A NH2 595 N N . ASP A 79 ? 1.0430 0.8988 1.2007 -0.4334 -0.0169 0.0665 79 ASP A N 596 C CA . ASP A 79 ? 1.0587 0.9463 1.2721 -0.4250 -0.0267 0.0617 79 ASP A CA 597 C C . ASP A 79 ? 1.1253 0.9960 1.3449 -0.4296 -0.0622 0.0645 79 ASP A C 598 O O . ASP A 79 ? 1.4355 1.2859 1.6428 -0.4483 -0.0741 0.0713 79 ASP A O 599 C CB . ASP A 79 ? 1.2505 1.1901 1.5213 -0.4380 -0.0052 0.0649 79 ASP A CB 600 C CG . ASP A 79 ? 1.4656 1.4280 1.7338 -0.4323 0.0321 0.0568 79 ASP A CG 601 O OD1 . ASP A 79 ? 1.6761 1.6248 1.9215 -0.4115 0.0375 0.0453 79 ASP A OD1 602 O OD2 . ASP A 79 ? 1.2431 1.2374 1.5312 -0.4499 0.0565 0.0612 79 ASP A OD2 603 N N . TYR A 80 ? 1.0314 0.9096 1.2694 -0.4131 -0.0794 0.0592 80 TYR A N 604 C CA . TYR A 80 ? 1.0350 0.9065 1.2822 -0.4181 -0.1136 0.0604 80 TYR A CA 605 C C . TYR A 80 ? 1.2152 1.1317 1.5305 -0.4329 -0.1190 0.0666 80 TYR A C 606 O O . TYR A 80 ? 1.1901 1.1044 1.5170 -0.4471 -0.1458 0.0689 80 TYR A O 607 C CB . TYR A 80 ? 0.9518 0.8155 1.1876 -0.3960 -0.1305 0.0557 80 TYR A CB 608 C CG . TYR A 80 ? 0.9703 0.8370 1.2182 -0.4008 -0.1661 0.0574 80 TYR A CG 609 C CD1 . TYR A 80 ? 1.0180 0.8462 1.2178 -0.4085 -0.1878 0.0523 80 TYR A CD1 610 C CD2 . TYR A 80 ? 0.9600 0.8688 1.2678 -0.3977 -0.1784 0.0631 80 TYR A CD2 611 C CE1 . TYR A 80 ? 0.9945 0.8262 1.1988 -0.4151 -0.2205 0.0515 80 TYR A CE1 612 C CE2 . TYR A 80 ? 0.9693 0.8828 1.2848 -0.4041 -0.2140 0.0660 80 TYR A CE2 613 C CZ . TYR A 80 ? 0.9909 0.8656 1.2509 -0.4138 -0.2348 0.0594 80 TYR A CZ 614 O OH . TYR A 80 ? 1.0124 0.8925 1.2739 -0.4223 -0.2703 0.0600 80 TYR A OH 615 N N . ALA A 81 ? 1.0166 0.9747 1.3773 -0.4305 -0.0921 0.0678 81 ALA A N 616 C CA . ALA A 81 ? 0.9951 1.0049 1.4316 -0.4411 -0.0916 0.0732 81 ALA A CA 617 C C . ALA A 81 ? 1.1448 1.1932 1.6162 -0.4355 -0.0517 0.0698 81 ALA A C 618 O O . ALA A 81 ? 1.5015 1.5341 1.9355 -0.4228 -0.0291 0.0622 81 ALA A O 619 C CB . ALA A 81 ? 0.9582 0.9871 1.4347 -0.4295 -0.1219 0.0744 81 ALA A CB 620 N N . LYS A 82 ? 1.1142 1.2143 1.6577 -0.4458 -0.0423 0.0739 82 LYS A N 621 C CA . LYS A 82 ? 1.1636 1.3055 1.7454 -0.4411 -0.0013 0.0675 82 LYS A CA 622 C C . LYS A 82 ? 1.2303 1.3781 1.8286 -0.4094 0.0051 0.0554 82 LYS A C 623 O O . LYS A 82 ? 1.3457 1.5041 1.9844 -0.3952 -0.0206 0.0579 82 LYS A O 624 C CB . LYS A 82 ? 1.3071 1.5076 1.9724 -0.4574 0.0063 0.0740 82 LYS A CB 625 C CG . LYS A 82 ? 1.5129 1.7585 2.2130 -0.4585 0.0547 0.0662 82 LYS A CG 626 C CD . LYS A 82 ? 1.5107 1.8145 2.2912 -0.4792 0.0637 0.0747 82 LYS A CD 627 C CE . LYS A 82 ? 1.4961 1.8464 2.3061 -0.4822 0.1164 0.0651 82 LYS A CE 628 N NZ . LYS A 82 ? 1.4236 1.8354 2.3166 -0.5030 0.1284 0.0736 82 LYS A NZ 629 N N . ASP A 83 ? 1.3014 1.4409 1.8676 -0.3998 0.0379 0.0433 83 ASP A N 630 C CA . ASP A 83 ? 1.2342 1.3712 1.8095 -0.3708 0.0470 0.0296 83 ASP A CA 631 C C . ASP A 83 ? 1.1345 1.2294 1.6754 -0.3543 0.0109 0.0338 83 ASP A C 632 O O . ASP A 83 ? 1.3224 1.4227 1.8965 -0.3315 0.0037 0.0304 83 ASP A O 633 C CB . ASP A 83 ? 1.3935 1.5863 2.0662 -0.3583 0.0597 0.0240 83 ASP A CB 634 C CG . ASP A 83 ? 1.5832 1.8223 2.2914 -0.3730 0.1018 0.0166 83 ASP A CG 635 O OD1 . ASP A 83 ? 1.7210 1.9462 2.3708 -0.3863 0.1280 0.0114 83 ASP A OD1 636 O OD2 . ASP A 83 ? 1.4971 1.7885 2.2924 -0.3720 0.1086 0.0168 83 ASP A OD2 637 N N . ASP A 84 ? 1.0190 1.0724 1.4956 -0.3664 -0.0109 0.0416 84 ASP A N 638 C CA . ASP A 84 ? 1.0148 1.0273 1.4487 -0.3535 -0.0410 0.0443 84 ASP A CA 639 C C . ASP A 84 ? 1.1325 1.0955 1.4824 -0.3604 -0.0402 0.0429 84 ASP A C 640 O O . ASP A 84 ? 1.0516 0.9926 1.3719 -0.3761 -0.0595 0.0497 84 ASP A O 641 C CB . ASP A 84 ? 1.0351 1.0535 1.4927 -0.3600 -0.0803 0.0557 84 ASP A CB 642 C CG . ASP A 84 ? 1.1606 1.1538 1.5949 -0.3425 -0.1085 0.0587 84 ASP A CG 643 O OD1 . ASP A 84 ? 1.4626 1.4182 1.8396 -0.3322 -0.1031 0.0535 84 ASP A OD1 644 O OD2 . ASP A 84 ? 1.1535 1.1664 1.6274 -0.3401 -0.1366 0.0677 84 ASP A OD2 645 N N . PRO A 85 ? 1.1477 1.0934 1.4627 -0.3488 -0.0182 0.0334 85 PRO A N 646 C CA . PRO A 85 ? 0.9976 0.9011 1.2390 -0.3538 -0.0144 0.0324 85 PRO A CA 647 C C . PRO A 85 ? 0.9872 0.8500 1.1850 -0.3517 -0.0454 0.0374 85 PRO A C 648 O O . PRO A 85 ? 0.9852 0.8431 1.1903 -0.3373 -0.0644 0.0378 85 PRO A O 649 C CB . PRO A 85 ? 0.9798 0.8787 1.2079 -0.3364 0.0082 0.0197 85 PRO A CB 650 C CG . PRO A 85 ? 1.0548 0.9988 1.3497 -0.3296 0.0285 0.0118 85 PRO A CG 651 C CD . PRO A 85 ? 1.0725 1.0397 1.4231 -0.3296 0.0039 0.0219 85 PRO A CD 652 N N . LEU A 86 ? 0.9829 0.8172 1.1370 -0.3666 -0.0498 0.0417 86 LEU A N 653 C CA . LEU A 86 ? 0.9736 0.7673 1.0833 -0.3648 -0.0738 0.0425 86 LEU A CA 654 C C . LEU A 86 ? 1.1041 0.8692 1.1684 -0.3492 -0.0666 0.0370 86 LEU A C 655 O O . LEU A 86 ? 1.1141 0.8562 1.1538 -0.3388 -0.0830 0.0351 86 LEU A O 656 C CB . LEU A 86 ? 0.9816 0.7546 1.0709 -0.3857 -0.0810 0.0483 86 LEU A CB 657 C CG . LEU A 86 ? 0.9554 0.6864 1.0037 -0.3847 -0.1038 0.0455 86 LEU A CG 658 C CD1 . LEU A 86 ? 1.2933 1.0286 1.3628 -0.3959 -0.1296 0.0452 86 LEU A CD1 659 C CD2 . LEU A 86 ? 1.0540 0.7525 1.0659 -0.3941 -0.0977 0.0491 86 LEU A CD2 660 N N . GLU A 87 ? 1.4291 1.1973 1.4812 -0.3496 -0.0418 0.0343 87 GLU A N 661 C CA . GLU A 87 ? 1.0980 0.8422 1.1102 -0.3372 -0.0341 0.0288 87 GLU A CA 662 C C . GLU A 87 ? 1.1073 0.8746 1.1379 -0.3283 -0.0094 0.0195 87 GLU A C 663 O O . GLU A 87 ? 1.2460 1.0475 1.3165 -0.3333 0.0055 0.0173 87 GLU A O 664 C CB . GLU A 87 ? 1.0793 0.7961 1.0468 -0.3487 -0.0320 0.0340 87 GLU A CB 665 C CG . GLU A 87 ? 1.1089 0.8410 1.0848 -0.3702 -0.0205 0.0425 87 GLU A CG 666 C CD . GLU A 87 ? 1.1926 0.8933 1.1303 -0.3822 -0.0265 0.0527 87 GLU A CD 667 O OE1 . GLU A 87 ? 1.1838 0.8517 1.0959 -0.3737 -0.0421 0.0514 87 GLU A OE1 668 O OE2 . GLU A 87 ? 1.2268 0.9366 1.1621 -0.4002 -0.0154 0.0628 87 GLU A OE2 669 N N . PHE A 88 ? 1.3716 1.1209 1.3762 -0.3153 -0.0043 0.0126 88 PHE A N 670 C CA . PHE A 88 ? 1.4062 1.1724 1.4301 -0.3047 0.0170 -0.0001 88 PHE A CA 671 C C . PHE A 88 ? 1.2673 1.0227 1.2498 -0.3098 0.0352 -0.0071 88 PHE A C 672 O O . PHE A 88 ? 1.3931 1.1716 1.3836 -0.3167 0.0591 -0.0159 88 PHE A O 673 C CB . PHE A 88 ? 0.9631 0.7213 1.0048 -0.2843 0.0055 -0.0027 88 PHE A CB 674 C CG . PHE A 88 ? 0.9493 0.7278 1.0395 -0.2799 -0.0102 0.0042 88 PHE A CG 675 C CD1 . PHE A 88 ? 0.9822 0.7951 1.1313 -0.2745 0.0024 -0.0012 88 PHE A CD1 676 C CD2 . PHE A 88 ? 0.9990 0.7644 1.0773 -0.2826 -0.0373 0.0155 88 PHE A CD2 677 C CE1 . PHE A 88 ? 1.2599 1.0945 1.4583 -0.2711 -0.0147 0.0074 88 PHE A CE1 678 C CE2 . PHE A 88 ? 0.9821 0.7683 1.1026 -0.2811 -0.0547 0.0228 88 PHE A CE2 679 C CZ . PHE A 88 ? 1.2280 1.0494 1.4102 -0.2753 -0.0448 0.0204 88 PHE A CZ 680 N N . LYS A 89 ? 0.9450 0.6682 0.8850 -0.3064 0.0243 -0.0042 89 LYS A N 681 C CA . LYS A 89 ? 1.1213 0.8323 1.0167 -0.3165 0.0333 -0.0043 89 LYS A CA 682 C C . LYS A 89 ? 1.1404 0.8613 1.0303 -0.3132 0.0554 -0.0210 89 LYS A C 683 O O . LYS A 89 ? 1.2811 0.9900 1.1312 -0.3196 0.0593 -0.0224 89 LYS A O 684 C CB . LYS A 89 ? 1.0219 0.7431 0.9088 -0.3379 0.0372 0.0073 89 LYS A CB 685 C CG . LYS A 89 ? 1.2094 0.9142 1.0487 -0.3509 0.0379 0.0158 89 LYS A CG 686 C CD . LYS A 89 ? 1.2513 0.9454 1.0839 -0.3663 0.0247 0.0348 89 LYS A CD 687 C CE . LYS A 89 ? 1.1463 0.8703 1.0108 -0.3806 0.0350 0.0391 89 LYS A CE 688 N NZ . LYS A 89 ? 1.0251 0.7368 0.8840 -0.3985 0.0228 0.0586 89 LYS A NZ 689 N N . SER A 90 ? 1.1998 0.9420 1.1316 -0.3032 0.0686 -0.0346 90 SER A N 690 C CA . SER A 90 ? 1.0692 0.8164 1.0001 -0.2977 0.0891 -0.0551 90 SER A CA 691 C C . SER A 90 ? 1.1092 0.8270 1.0281 -0.2831 0.0760 -0.0577 90 SER A C 692 O O . SER A 90 ? 1.1275 0.8341 1.0659 -0.2707 0.0581 -0.0489 90 SER A O 693 C CB . SER A 90 ? 1.1391 0.9170 1.1273 -0.2896 0.1079 -0.0701 90 SER A CB 694 O OG . SER A 90 ? 1.3733 1.1826 1.3744 -0.3047 0.1233 -0.0683 90 SER A OG 695 N N . HIS A 91 ? 1.1064 0.8131 0.9917 -0.2865 0.0845 -0.0688 91 HIS A N 696 C CA . HIS A 91 ? 1.1304 0.8098 1.0025 -0.2757 0.0732 -0.0709 91 HIS A CA 697 C C . HIS A 91 ? 1.1895 0.8469 1.0433 -0.2736 0.0483 -0.0502 91 HIS A C 698 O O . HIS A 91 ? 0.9699 0.6119 0.8347 -0.2607 0.0361 -0.0463 91 HIS A O 699 C CB . HIS A 91 ? 0.9837 0.6630 0.9024 -0.2575 0.0770 -0.0826 91 HIS A CB 700 C CG . HIS A 91 ? 1.0912 0.7923 1.0385 -0.2567 0.1032 -0.1063 91 HIS A CG 701 N ND1 . HIS A 91 ? 1.1573 0.8562 1.0820 -0.2626 0.1206 -0.1285 91 HIS A ND1 702 C CD2 . HIS A 91 ? 1.1623 0.8892 1.1611 -0.2506 0.1158 -0.1133 91 HIS A CD2 703 C CE1 . HIS A 91 ? 1.1755 0.8969 1.1346 -0.2600 0.1449 -0.1503 91 HIS A CE1 704 N NE2 . HIS A 91 ? 1.1718 0.9113 1.1793 -0.2519 0.1429 -0.1409 91 HIS A NE2 705 N N . GLN A 92 ? 1.1532 0.8093 0.9799 -0.2868 0.0419 -0.0371 92 GLN A N 706 C CA . GLN A 92 ? 1.1837 0.8199 0.9961 -0.2854 0.0207 -0.0206 92 GLN A CA 707 C C . GLN A 92 ? 0.9725 0.5867 0.7516 -0.2852 0.0129 -0.0179 92 GLN A C 708 O O . GLN A 92 ? 1.1035 0.7004 0.8731 -0.2816 -0.0023 -0.0075 92 GLN A O 709 C CB . GLN A 92 ? 1.1341 0.7759 0.9398 -0.2994 0.0165 -0.0080 92 GLN A CB 710 C CG . GLN A 92 ? 1.3205 0.9651 1.0940 -0.3161 0.0242 -0.0044 92 GLN A CG 711 C CD . GLN A 92 ? 1.2140 0.8608 0.9837 -0.3308 0.0187 0.0115 92 GLN A CD 712 O OE1 . GLN A 92 ? 1.1254 0.7645 0.9111 -0.3281 0.0056 0.0188 92 GLN A OE1 713 N NE2 . GLN A 92 ? 1.0684 0.7254 0.8157 -0.3482 0.0282 0.0171 92 GLN A NE2 714 N N . TRP A 93 ? 0.9659 0.5825 0.7289 -0.2896 0.0236 -0.0287 93 TRP A N 715 C CA . TRP A 93 ? 1.1112 0.7115 0.8452 -0.2917 0.0157 -0.0262 93 TRP A CA 716 C C . TRP A 93 ? 1.1557 0.7472 0.8656 -0.3014 0.0029 -0.0084 93 TRP A C 717 O O . TRP A 93 ? 1.2365 0.8108 0.9399 -0.2959 -0.0106 -0.0002 93 TRP A O 718 C CB . TRP A 93 ? 1.0589 0.6425 0.8049 -0.2767 0.0066 -0.0266 93 TRP A CB 719 C CG . TRP A 93 ? 0.9335 0.5180 0.6959 -0.2697 0.0166 -0.0430 93 TRP A CG 720 C CD1 . TRP A 93 ? 0.9903 0.5866 0.7832 -0.2639 0.0289 -0.0551 93 TRP A CD1 721 C CD2 . TRP A 93 ? 0.9408 0.5127 0.6956 -0.2675 0.0144 -0.0493 93 TRP A CD2 722 N NE1 . TRP A 93 ? 1.0860 0.6750 0.8908 -0.2578 0.0349 -0.0693 93 TRP A NE1 723 C CE2 . TRP A 93 ? 1.0479 0.6217 0.8283 -0.2609 0.0259 -0.0660 93 TRP A CE2 724 C CE3 . TRP A 93 ? 1.1028 0.6628 0.8365 -0.2707 0.0036 -0.0425 93 TRP A CE3 725 C CZ2 . TRP A 93 ? 1.1105 0.6720 0.8935 -0.2587 0.0265 -0.0764 93 TRP A CZ2 726 C CZ3 . TRP A 93 ? 1.2303 0.7818 0.9667 -0.2690 0.0040 -0.0520 93 TRP A CZ3 727 C CH2 . TRP A 93 ? 1.1922 0.7432 0.9518 -0.2637 0.0152 -0.0689 93 TRP A CH2 728 N N . PHE A 94 ? 1.0536 0.6571 0.7536 -0.3158 0.0077 -0.0018 94 PHE A N 729 C CA . PHE A 94 ? 1.1489 0.7422 0.8290 -0.3261 -0.0051 0.0172 94 PHE A CA 730 C C . PHE A 94 ? 1.1374 0.7260 0.7879 -0.3331 -0.0102 0.0203 94 PHE A C 731 O O . PHE A 94 ? 1.3256 0.9281 0.9577 -0.3427 0.0010 0.0106 94 PHE A O 732 C CB . PHE A 94 ? 1.1484 0.7560 0.8269 -0.3421 0.0012 0.0267 94 PHE A CB 733 C CG . PHE A 94 ? 1.0704 0.6662 0.7297 -0.3546 -0.0123 0.0488 94 PHE A CG 734 C CD1 . PHE A 94 ? 1.0284 0.6025 0.7002 -0.3487 -0.0287 0.0604 94 PHE A CD1 735 C CD2 . PHE A 94 ? 1.1041 0.7098 0.7328 -0.3728 -0.0089 0.0579 94 PHE A CD2 736 C CE1 . PHE A 94 ? 1.0123 0.5728 0.6737 -0.3589 -0.0419 0.0812 94 PHE A CE1 737 C CE2 . PHE A 94 ? 1.1486 0.7424 0.7632 -0.3845 -0.0239 0.0825 94 PHE A CE2 738 C CZ . PHE A 94 ? 1.0413 0.6113 0.6757 -0.3765 -0.0405 0.0943 94 PHE A CZ 739 N N . GLY A 95 ? 1.1303 0.7004 0.7775 -0.3286 -0.0272 0.0328 95 GLY A N 740 C CA . GLY A 95 ? 1.4872 1.0538 1.1122 -0.3346 -0.0364 0.0385 95 GLY A CA 741 C C . GLY A 95 ? 1.1674 0.7261 0.8014 -0.3213 -0.0397 0.0279 95 GLY A C 742 O O . GLY A 95 ? 1.1732 0.7311 0.7935 -0.3257 -0.0478 0.0302 95 GLY A O 743 N N . ALA A 96 ? 0.9551 0.5092 0.6127 -0.3066 -0.0347 0.0181 96 ALA A N 744 C CA . ALA A 96 ? 0.9405 0.4862 0.6096 -0.2944 -0.0375 0.0114 96 ALA A CA 745 C C . ALA A 96 ? 1.0248 0.5578 0.6975 -0.2892 -0.0521 0.0247 96 ALA A C 746 O O . ALA A 96 ? 1.2776 0.8071 0.9556 -0.2841 -0.0564 0.0231 96 ALA A O 747 C CB . ALA A 96 ? 0.9217 0.4661 0.6136 -0.2815 -0.0303 0.0027 96 ALA A CB 748 N N . SER A 97 ? 0.9393 0.4657 0.6135 -0.2907 -0.0589 0.0370 97 SER A N 749 C CA . SER A 97 ? 1.0545 0.5681 0.7374 -0.2852 -0.0716 0.0484 97 SER A CA 750 C C . SER A 97 ? 1.0735 0.5841 0.7477 -0.2969 -0.0819 0.0656 97 SER A C 751 O O . SER A 97 ? 1.4577 0.9663 1.1310 -0.3029 -0.0804 0.0704 97 SER A O 752 C CB . SER A 97 ? 1.1335 0.6361 0.8335 -0.2725 -0.0706 0.0447 97 SER A CB 753 O OG . SER A 97 ? 1.7673 1.2731 1.4737 -0.2631 -0.0628 0.0333 97 SER A OG 754 N N . VAL A 98 ? 1.1231 0.6341 0.7929 -0.3013 -0.0938 0.0767 98 VAL A N 755 C CA . VAL A 98 ? 1.0946 0.6019 0.7579 -0.3127 -0.1071 0.0981 98 VAL A CA 756 C C . VAL A 98 ? 1.2226 0.7197 0.9077 -0.3045 -0.1233 0.1106 98 VAL A C 757 O O . VAL A 98 ? 1.5504 1.0545 1.2393 -0.3013 -0.1281 0.1086 98 VAL A O 758 C CB . VAL A 98 ? 1.2068 0.7305 0.8373 -0.3323 -0.1081 0.1040 98 VAL A CB 759 C CG1 . VAL A 98 ? 1.0548 0.5744 0.6772 -0.3457 -0.1238 0.1313 98 VAL A CG1 760 C CG2 . VAL A 98 ? 1.4761 1.0128 1.0901 -0.3394 -0.0887 0.0886 98 VAL A CG2 761 N N . ARG A 99 ? 1.0748 0.5554 0.7788 -0.3010 -0.1316 0.1229 99 ARG A N 762 C CA . ARG A 99 ? 1.2285 0.6992 0.9602 -0.2925 -0.1472 0.1360 99 ARG A CA 763 C C . ARG A 99 ? 1.1021 0.5577 0.8428 -0.2999 -0.1613 0.1592 99 ARG A C 764 O O . ARG A 99 ? 1.2969 0.7419 1.0356 -0.3040 -0.1560 0.1587 99 ARG A O 765 C CB . ARG A 99 ? 1.0991 0.5605 0.8607 -0.2721 -0.1396 0.1197 99 ARG A CB 766 C CG . ARG A 99 ? 1.2839 0.7442 1.0781 -0.2614 -0.1510 0.1276 99 ARG A CG 767 C CD . ARG A 99 ? 1.4617 0.9267 1.2729 -0.2457 -0.1378 0.1078 99 ARG A CD 768 N NE . ARG A 99 ? 1.6014 1.0801 1.3868 -0.2498 -0.1250 0.0937 99 ARG A NE 769 C CZ . ARG A 99 ? 1.6332 1.1278 1.4099 -0.2559 -0.1277 0.0944 99 ARG A CZ 770 N NH1 . ARG A 99 ? 1.7131 1.2157 1.4714 -0.2585 -0.1154 0.0803 99 ARG A NH1 771 N NH2 . ARG A 99 ? 1.5514 1.0532 1.3403 -0.2597 -0.1440 0.1093 99 ARG A NH2 772 N N . SER A 100 ? 1.1671 0.6220 0.9204 -0.3023 -0.1808 0.1813 100 SER A N 773 C CA . SER A 100 ? 1.0973 0.5367 0.8623 -0.3101 -0.1977 0.2087 100 SER A CA 774 C C . SER A 100 ? 1.1842 0.6086 0.9987 -0.2942 -0.2132 0.2193 100 SER A C 775 O O . SER A 100 ? 1.6356 1.0715 1.4666 -0.2854 -0.2189 0.2178 100 SER A O 776 C CB . SER A 100 ? 1.3563 0.8111 1.0855 -0.3336 -0.2104 0.2334 100 SER A CB 777 O OG . SER A 100 ? 1.5736 1.0145 1.3202 -0.3400 -0.2329 0.2668 100 SER A OG 778 N N . LYS A 101 ? 1.1195 0.5181 0.9618 -0.2906 -0.2193 0.2289 101 LYS A N 779 C CA . LYS A 101 ? 1.2633 0.6451 1.1580 -0.2768 -0.2359 0.2427 101 LYS A CA 780 C C . LYS A 101 ? 1.1770 0.5491 1.0807 -0.2873 -0.2547 0.2751 101 LYS A C 781 O O . LYS A 101 ? 1.3418 0.7059 1.2431 -0.2900 -0.2470 0.2720 101 LYS A O 782 C CB . LYS A 101 ? 1.4493 0.8113 1.3818 -0.2549 -0.2218 0.2153 101 LYS A CB 783 C CG . LYS A 101 ? 1.5397 0.8832 1.5339 -0.2385 -0.2359 0.2256 101 LYS A CG 784 C CD . LYS A 101 ? 1.3380 0.6630 1.3649 -0.2180 -0.2183 0.1934 101 LYS A CD 785 C CE . LYS A 101 ? 1.6617 0.9640 1.7554 -0.2018 -0.2312 0.2024 101 LYS A CE 786 N NZ . LYS A 101 ? 1.6457 0.9377 1.7501 -0.2085 -0.2459 0.2271 101 LYS A NZ 787 N N . GLN A 102 ? 1.1961 0.5763 1.1115 -0.2918 -0.2788 0.3052 102 GLN A N 788 C CA . GLN A 102 ? 1.4403 0.8212 1.3631 -0.3009 -0.2982 0.3385 102 GLN A CA 789 C C . GLN A 102 ? 1.3908 0.7834 1.2598 -0.3244 -0.2902 0.3451 102 GLN A C 790 O O . GLN A 102 ? 1.8718 1.2839 1.6888 -0.3431 -0.2869 0.3465 102 GLN A O 791 C CB . GLN A 102 ? 1.2764 0.6326 1.2596 -0.2813 -0.3006 0.3374 102 GLN A CB 792 C CG . GLN A 102 ? 1.4104 0.7576 1.4554 -0.2588 -0.3115 0.3372 102 GLN A CG 793 C CD . GLN A 102 ? 1.8460 1.1683 1.9520 -0.2409 -0.3145 0.3371 102 GLN A CD 794 O OE1 . GLN A 102 ? 2.0919 1.3972 2.1961 -0.2399 -0.3000 0.3211 102 GLN A OE1 795 N NE2 . GLN A 102 ? 1.7305 1.0509 1.8936 -0.2270 -0.3341 0.3546 102 GLN A NE2 796 N N . ASP A 103 ? 1.2619 0.6423 1.1453 -0.3240 -0.2860 0.3478 103 ASP A N 797 C CA . ASP A 103 ? 1.5129 0.9057 1.3547 -0.3468 -0.2802 0.3591 103 ASP A CA 798 C C . ASP A 103 ? 1.5203 0.9149 1.3371 -0.3496 -0.2527 0.3283 103 ASP A C 799 O O . ASP A 103 ? 1.2623 0.6677 1.0512 -0.3672 -0.2441 0.3338 103 ASP A O 800 C CB . ASP A 103 ? 1.3171 0.6976 1.1898 -0.3481 -0.2923 0.3830 103 ASP A CB 801 C CG . ASP A 103 ? 1.5108 0.9118 1.3468 -0.3743 -0.3048 0.4175 103 ASP A CG 802 O OD1 . ASP A 103 ? 1.5013 0.9223 1.2844 -0.3940 -0.2906 0.4129 103 ASP A OD1 803 O OD2 . ASP A 103 ? 1.4515 0.8497 1.3118 -0.3756 -0.3284 0.4488 103 ASP A OD2 804 N N . LYS A 104 ? 1.2521 0.6381 1.0808 -0.3329 -0.2393 0.2969 104 LYS A N 805 C CA . LYS A 104 ? 1.1871 0.5743 0.9994 -0.3331 -0.2160 0.2676 104 LYS A CA 806 C C . LYS A 104 ? 1.4499 0.8524 1.2266 -0.3366 -0.2035 0.2488 104 LYS A C 807 O O . LYS A 104 ? 1.5617 0.9628 1.3451 -0.3271 -0.2079 0.2432 104 LYS A O 808 C CB . LYS A 104 ? 1.1739 0.5374 1.0277 -0.3122 -0.2092 0.2441 104 LYS A CB 809 C CG . LYS A 104 ? 1.7478 1.0922 1.6396 -0.3089 -0.2194 0.2584 104 LYS A CG 810 C CD . LYS A 104 ? 1.6902 1.0086 1.6221 -0.2890 -0.2128 0.2322 104 LYS A CD 811 C CE . LYS A 104 ? 1.7897 1.0858 1.7628 -0.2855 -0.2238 0.2462 104 LYS A CE 812 N NZ . LYS A 104 ? 2.1709 1.4393 2.1822 -0.2673 -0.2165 0.2177 104 LYS A NZ 813 N N . ILE A 105 ? 1.3769 0.7937 1.1198 -0.3505 -0.1875 0.2391 105 ILE A N 814 C CA . ILE A 105 ? 1.2553 0.6859 0.9654 -0.3553 -0.1737 0.2204 105 ILE A CA 815 C C . ILE A 105 ? 1.1970 0.6280 0.9116 -0.3463 -0.1542 0.1907 105 ILE A C 816 O O . ILE A 105 ? 1.4920 0.9234 1.2090 -0.3531 -0.1475 0.1899 105 ILE A O 817 C CB . ILE A 105 ? 1.1501 0.6070 0.8153 -0.3785 -0.1692 0.2317 105 ILE A CB 818 C CG1 . ILE A 105 ? 1.1859 0.6450 0.8400 -0.3906 -0.1914 0.2638 105 ILE A CG1 819 C CG2 . ILE A 105 ? 1.1251 0.6056 0.7668 -0.3748 -0.1517 0.2041 105 ILE A CG2 820 C CD1 . ILE A 105 ? 1.2151 0.7006 0.8184 -0.4166 -0.1873 0.2753 105 ILE A CD1 821 N N . LEU A 106 ? 1.2279 0.6648 0.9465 -0.3296 -0.1455 0.1667 106 LEU A N 822 C CA . LEU A 106 ? 1.1840 0.6239 0.9044 -0.3213 -0.1293 0.1408 106 LEU A CA 823 C C . LEU A 106 ? 1.1983 0.6630 0.8955 -0.3218 -0.1152 0.1253 106 LEU A C 824 O O . LEU A 106 ? 1.3119 0.7841 1.0045 -0.3157 -0.1163 0.1212 106 LEU A O 825 C CB . LEU A 106 ? 1.2228 0.6453 0.9699 -0.3010 -0.1300 0.1253 106 LEU A CB 826 C CG . LEU A 106 ? 1.1745 0.6003 0.9205 -0.2932 -0.1164 0.1009 106 LEU A CG 827 C CD1 . LEU A 106 ? 1.2451 0.6691 0.9897 -0.3054 -0.1141 0.1018 106 LEU A CD1 828 C CD2 . LEU A 106 ? 1.1657 0.5754 0.9322 -0.2758 -0.1164 0.0861 106 LEU A CD2 829 N N . ALA A 107 ? 1.1933 0.6708 0.8808 -0.3292 -0.1022 0.1165 107 ALA A N 830 C CA . ALA A 107 ? 1.0679 0.5669 0.7406 -0.3285 -0.0875 0.1000 107 ALA A CA 831 C C . ALA A 107 ? 1.2002 0.7028 0.8858 -0.3213 -0.0767 0.0830 107 ALA A C 832 O O . ALA A 107 ? 1.1947 0.6926 0.8907 -0.3264 -0.0776 0.0863 107 ALA A O 833 C CB . ALA A 107 ? 1.0369 0.5556 0.6834 -0.3476 -0.0812 0.1075 107 ALA A CB 834 N N . CYS A 108 ? 1.1731 0.6841 0.8597 -0.3105 -0.0683 0.0664 108 CYS A N 835 C CA . CYS A 108 ? 1.2510 0.7646 0.9518 -0.3019 -0.0621 0.0532 108 CYS A CA 836 C C . CYS A 108 ? 1.3402 0.8740 1.0412 -0.3010 -0.0483 0.0407 108 CYS A C 837 O O . CYS A 108 ? 1.1186 0.6604 0.8081 -0.3028 -0.0426 0.0364 108 CYS A O 838 C CB . CYS A 108 ? 1.1035 0.6028 0.8131 -0.2863 -0.0674 0.0466 108 CYS A CB 839 S SG . CYS A 108 ? 1.3446 0.8192 1.0624 -0.2835 -0.0808 0.0558 108 CYS A SG 840 N N . ALA A 109 ? 1.1754 0.7167 0.8923 -0.2984 -0.0442 0.0343 109 ALA A N 841 C CA . ALA A 109 ? 1.1005 0.6601 0.8283 -0.2950 -0.0320 0.0228 109 ALA A CA 842 C C . ALA A 109 ? 1.0195 0.5757 0.7637 -0.2811 -0.0360 0.0169 109 ALA A C 843 O O . ALA A 109 ? 1.2465 0.8081 1.0059 -0.2813 -0.0393 0.0172 109 ALA A O 844 C CB . ALA A 109 ? 0.9294 0.5085 0.6668 -0.3067 -0.0228 0.0235 109 ALA A CB 845 N N . PRO A 110 ? 0.8976 0.4460 0.6384 -0.2708 -0.0368 0.0130 110 PRO A N 846 C CA . PRO A 110 ? 0.8882 0.4317 0.6382 -0.2593 -0.0420 0.0114 110 PRO A CA 847 C C . PRO A 110 ? 0.9600 0.5181 0.7328 -0.2548 -0.0381 0.0074 110 PRO A C 848 O O . PRO A 110 ? 1.0731 0.6297 0.8532 -0.2479 -0.0453 0.0098 110 PRO A O 849 C CB . PRO A 110 ? 0.8847 0.4190 0.6264 -0.2525 -0.0412 0.0101 110 PRO A CB 850 C CG . PRO A 110 ? 1.0439 0.5756 0.7713 -0.2604 -0.0403 0.0122 110 PRO A CG 851 C CD . PRO A 110 ? 0.9008 0.4455 0.6278 -0.2714 -0.0339 0.0113 110 PRO A CD 852 N N . LEU A 111 ? 0.8847 0.4577 0.6696 -0.2586 -0.0267 0.0014 111 LEU A N 853 C CA . LEU A 111 ? 0.9315 0.5200 0.7475 -0.2529 -0.0222 -0.0028 111 LEU A CA 854 C C . LEU A 111 ? 1.0773 0.6836 0.9112 -0.2603 -0.0218 -0.0008 111 LEU A C 855 O O . LEU A 111 ? 0.9410 0.5647 0.8076 -0.2561 -0.0177 -0.0039 111 LEU A O 856 C CB . LEU A 111 ? 1.2472 0.8421 1.0738 -0.2503 -0.0075 -0.0148 111 LEU A CB 857 C CG . LEU A 111 ? 1.1619 0.7410 0.9841 -0.2417 -0.0094 -0.0166 111 LEU A CG 858 C CD1 . LEU A 111 ? 1.0700 0.6544 0.9171 -0.2362 0.0030 -0.0299 111 LEU A CD1 859 C CD2 . LEU A 111 ? 0.8756 0.4452 0.7010 -0.2332 -0.0233 -0.0051 111 LEU A CD2 860 N N . TYR A 112 ? 1.0310 0.6328 0.8480 -0.2713 -0.0264 0.0051 112 TYR A N 861 C CA . TYR A 112 ? 0.9184 0.5348 0.7523 -0.2808 -0.0282 0.0090 112 TYR A CA 862 C C . TYR A 112 ? 0.9329 0.5559 0.7909 -0.2745 -0.0408 0.0114 112 TYR A C 863 O O . TYR A 112 ? 1.0135 0.6213 0.8589 -0.2680 -0.0537 0.0141 112 TYR A O 864 C CB . TYR A 112 ? 1.1778 0.7799 0.9898 -0.2927 -0.0355 0.0170 112 TYR A CB 865 C CG . TYR A 112 ? 1.0820 0.6924 0.9109 -0.3036 -0.0421 0.0222 112 TYR A CG 866 C CD1 . TYR A 112 ? 0.9502 0.5828 0.7954 -0.3160 -0.0308 0.0243 112 TYR A CD1 867 C CD2 . TYR A 112 ? 1.0699 0.6665 0.8976 -0.3030 -0.0591 0.0240 112 TYR A CD2 868 C CE1 . TYR A 112 ? 0.9668 0.6080 0.8313 -0.3277 -0.0373 0.0301 112 TYR A CE1 869 C CE2 . TYR A 112 ? 1.3259 0.9289 1.1702 -0.3147 -0.0669 0.0274 112 TYR A CE2 870 C CZ . TYR A 112 ? 1.0974 0.7226 0.9620 -0.3271 -0.0565 0.0316 112 TYR A CZ 871 O OH . TYR A 112 ? 0.9362 0.5688 0.8213 -0.3404 -0.0647 0.0360 112 TYR A OH 872 N N . HIS A 113 ? 1.0161 0.6641 0.9090 -0.2771 -0.0372 0.0108 113 HIS A N 873 C CA . HIS A 113 ? 1.0831 0.7419 1.0034 -0.2720 -0.0517 0.0150 113 HIS A CA 874 C C . HIS A 113 ? 1.1891 0.8583 1.1218 -0.2852 -0.0618 0.0198 113 HIS A C 875 O O . HIS A 113 ? 1.2323 0.9094 1.1676 -0.2979 -0.0522 0.0201 113 HIS A O 876 C CB . HIS A 113 ? 1.3115 0.9928 1.2748 -0.2616 -0.0430 0.0114 113 HIS A CB 877 C CG . HIS A 113 ? 1.3411 1.0090 1.3003 -0.2473 -0.0411 0.0091 113 HIS A CG 878 N ND1 . HIS A 113 ? 1.2561 0.9194 1.2092 -0.2441 -0.0229 -0.0014 113 HIS A ND1 879 C CD2 . HIS A 113 ? 1.1621 0.8200 1.1215 -0.2373 -0.0557 0.0168 113 HIS A CD2 880 C CE1 . HIS A 113 ? 1.3487 0.9983 1.3026 -0.2323 -0.0265 -0.0006 113 HIS A CE1 881 N NE2 . HIS A 113 ? 1.0383 0.6848 0.9959 -0.2279 -0.0458 0.0118 113 HIS A NE2 882 N N . TRP A 114 ? 1.0945 0.7639 1.0335 -0.2839 -0.0819 0.0243 114 TRP A N 883 C CA . TRP A 114 ? 0.9523 0.6275 0.9000 -0.2976 -0.0958 0.0273 114 TRP A CA 884 C C . TRP A 114 ? 0.9305 0.6327 0.9195 -0.2960 -0.1099 0.0322 114 TRP A C 885 O O . TRP A 114 ? 1.3082 1.0155 1.3077 -0.2832 -0.1161 0.0357 114 TRP A O 886 C CB . TRP A 114 ? 1.1728 0.8181 1.0801 -0.3014 -0.1104 0.0254 114 TRP A CB 887 C CG . TRP A 114 ? 1.0570 0.6997 0.9677 -0.3176 -0.1226 0.0250 114 TRP A CG 888 C CD1 . TRP A 114 ? 1.4121 1.0694 1.3485 -0.3317 -0.1174 0.0282 114 TRP A CD1 889 C CD2 . TRP A 114 ? 1.0375 0.6616 0.9258 -0.3229 -0.1416 0.0200 114 TRP A CD2 890 N NE1 . TRP A 114 ? 1.4443 1.0909 1.3784 -0.3456 -0.1336 0.0265 114 TRP A NE1 891 C CE2 . TRP A 114 ? 1.2392 0.8647 1.1432 -0.3402 -0.1486 0.0197 114 TRP A CE2 892 C CE3 . TRP A 114 ? 1.2649 0.8717 1.1204 -0.3160 -0.1522 0.0148 114 TRP A CE3 893 C CZ2 . TRP A 114 ? 1.1278 0.7355 1.0168 -0.3501 -0.1668 0.0118 114 TRP A CZ2 894 C CZ3 . TRP A 114 ? 1.5814 1.1730 1.4187 -0.3257 -0.1683 0.0061 114 TRP A CZ3 895 C CH2 . TRP A 114 ? 1.3857 0.9765 1.2401 -0.3424 -0.1760 0.0035 114 TRP A CH2 896 N N . ARG A 115 ? 0.9239 0.6438 0.9388 -0.3099 -0.1166 0.0344 115 ARG A N 897 C CA . ARG A 115 ? 0.9340 0.6835 0.9937 -0.3104 -0.1327 0.0404 115 ARG A CA 898 C C . ARG A 115 ? 0.9693 0.7075 1.0073 -0.3168 -0.1621 0.0425 115 ARG A C 899 O O . ARG A 115 ? 1.1848 0.9448 1.2513 -0.3168 -0.1816 0.0494 115 ARG A O 900 C CB . ARG A 115 ? 1.0552 0.8351 1.1603 -0.3236 -0.1239 0.0416 115 ARG A CB 901 C CG . ARG A 115 ? 0.9442 0.7640 1.1124 -0.3210 -0.1339 0.0479 115 ARG A CG 902 C CD . ARG A 115 ? 0.9513 0.7802 1.1317 -0.3378 -0.1604 0.0525 115 ARG A CD 903 N NE . ARG A 115 ? 1.0072 0.8796 1.2559 -0.3375 -0.1698 0.0600 115 ARG A NE 904 C CZ . ARG A 115 ? 1.0487 0.9351 1.3157 -0.3464 -0.2006 0.0666 115 ARG A CZ 905 N NH1 . ARG A 115 ? 0.9757 0.8343 1.1931 -0.3567 -0.2232 0.0639 115 ARG A NH1 906 N NH2 . ARG A 115 ? 1.2100 1.1393 1.5463 -0.3451 -0.2091 0.0749 115 ARG A NH2 907 N N . THR A 116 ? 0.9823 0.6871 0.9703 -0.3222 -0.1649 0.0357 116 THR A N 908 C CA . THR A 116 ? 1.1079 0.7963 1.0642 -0.3293 -0.1885 0.0317 116 THR A CA 909 C C . THR A 116 ? 1.3878 1.0864 1.3630 -0.3485 -0.2068 0.0299 116 THR A C 910 O O . THR A 116 ? 1.6960 1.3775 1.6410 -0.3572 -0.2248 0.0220 116 THR A O 911 C CB . THR A 116 ? 1.1196 0.8148 1.0673 -0.3192 -0.2049 0.0383 116 THR A CB 912 O OG1 . THR A 116 ? 1.2185 0.9493 1.2164 -0.3203 -0.2191 0.0491 116 THR A OG1 913 C CG2 . THR A 116 ? 1.5932 1.2789 1.5279 -0.3013 -0.1886 0.0416 116 THR A CG2 914 N N . GLU A 117 ? 1.0113 0.7390 1.0370 -0.3560 -0.2020 0.0357 117 GLU A N 915 C CA . GLU A 117 ? 1.1708 0.9087 1.2203 -0.3768 -0.2168 0.0346 117 GLU A CA 916 C C . GLU A 117 ? 1.2260 0.9790 1.2831 -0.3834 -0.2492 0.0360 117 GLU A C 917 O O . GLU A 117 ? 1.0333 0.7981 1.1140 -0.4017 -0.2653 0.0349 117 GLU A O 918 C CB . GLU A 117 ? 1.1722 0.8728 1.1872 -0.3895 -0.2143 0.0248 117 GLU A CB 919 C CG . GLU A 117 ? 1.0494 0.7582 1.0974 -0.4115 -0.2173 0.0265 117 GLU A CG 920 C CD . GLU A 117 ? 1.1870 0.8556 1.2065 -0.4214 -0.2116 0.0201 117 GLU A CD 921 O OE1 . GLU A 117 ? 1.5234 1.1946 1.5688 -0.4391 -0.2084 0.0252 117 GLU A OE1 922 O OE2 . GLU A 117 ? 1.0565 0.6913 1.0309 -0.4116 -0.2103 0.0110 117 GLU A OE2 923 N N . MET A 118 ? 1.4699 1.2229 1.5061 -0.3703 -0.2601 0.0396 118 MET A N 924 C CA . MET A 118 ? 1.3270 1.0977 1.3671 -0.3768 -0.2928 0.0445 118 MET A CA 925 C C . MET A 118 ? 1.2665 1.0771 1.3625 -0.3651 -0.2984 0.0624 118 MET A C 926 O O . MET A 118 ? 1.1751 1.0200 1.3279 -0.3734 -0.3091 0.0693 118 MET A O 927 C CB . MET A 118 ? 1.1521 0.8956 1.1261 -0.3735 -0.3043 0.0382 118 MET A CB 928 C CG . MET A 118 ? 1.2299 0.9323 1.1529 -0.3811 -0.2956 0.0182 118 MET A CG 929 S SD . MET A 118 ? 1.4001 1.0763 1.2481 -0.3776 -0.3048 0.0080 118 MET A SD 930 C CE . MET A 118 ? 1.8527 1.5597 1.7047 -0.3912 -0.3450 0.0163 118 MET A CE 931 N N . LYS A 119 ? 1.2559 1.0619 1.3406 -0.3458 -0.2906 0.0700 119 LYS A N 932 C CA . LYS A 119 ? 1.3037 1.1418 1.4464 -0.3309 -0.2911 0.0860 119 LYS A CA 933 C C . LYS A 119 ? 1.1516 0.9894 1.3192 -0.3178 -0.2546 0.0814 119 LYS A C 934 O O . LYS A 119 ? 1.1882 1.0022 1.3241 -0.3216 -0.2329 0.0690 119 LYS A O 935 C CB . LYS A 119 ? 1.2331 1.0663 1.3524 -0.3193 -0.3084 0.0995 119 LYS A CB 936 C CG . LYS A 119 ? 1.2611 1.0556 1.3143 -0.3114 -0.2930 0.0924 119 LYS A CG 937 C CD . LYS A 119 ? 1.4206 1.2123 1.4473 -0.3049 -0.3129 0.1083 119 LYS A CD 938 C CE . LYS A 119 ? 1.4769 1.2334 1.4410 -0.2984 -0.2961 0.1014 119 LYS A CE 939 N NZ . LYS A 119 ? 1.5617 1.3169 1.4981 -0.2944 -0.3140 0.1192 119 LYS A NZ 940 N N . GLN A 120 ? 1.0390 0.9030 1.2639 -0.3027 -0.2484 0.0909 120 GLN A N 941 C CA . GLN A 120 ? 1.0520 0.9167 1.2986 -0.2906 -0.2130 0.0832 120 GLN A CA 942 C C . GLN A 120 ? 1.1417 0.9796 1.3561 -0.2733 -0.2035 0.0838 120 GLN A C 943 O O . GLN A 120 ? 1.2126 1.0570 1.4490 -0.2602 -0.2162 0.0967 120 GLN A O 944 C CB . GLN A 120 ? 1.0356 0.9437 1.3682 -0.2837 -0.2059 0.0878 120 GLN A CB 945 C CG . GLN A 120 ? 1.2558 1.1678 1.6093 -0.2744 -0.1664 0.0751 120 GLN A CG 946 C CD . GLN A 120 ? 1.5852 1.5437 2.0239 -0.2716 -0.1543 0.0748 120 GLN A CD 947 O OE1 . GLN A 120 ? 1.4391 1.4266 1.9146 -0.2848 -0.1685 0.0806 120 GLN A OE1 948 N NE2 . GLN A 120 ? 1.6364 1.6031 2.1094 -0.2549 -0.1272 0.0662 120 GLN A NE2 949 N N . GLU A 121 ? 1.0949 0.9027 1.2594 -0.2742 -0.1824 0.0717 121 GLU A N 950 C CA . GLU A 121 ? 1.1814 0.9619 1.3108 -0.2608 -0.1731 0.0710 121 GLU A CA 951 C C . GLU A 121 ? 0.9957 0.7612 1.1070 -0.2595 -0.1416 0.0566 121 GLU A C 952 O O . GLU A 121 ? 0.9610 0.7317 1.0724 -0.2713 -0.1297 0.0489 121 GLU A O 953 C CB . GLU A 121 ? 1.3645 1.1181 1.4311 -0.2660 -0.1915 0.0740 121 GLU A CB 954 C CG . GLU A 121 ? 1.4431 1.2078 1.5145 -0.2652 -0.2224 0.0907 121 GLU A CG 955 C CD . GLU A 121 ? 1.6746 1.4360 1.7589 -0.2482 -0.2230 0.1041 121 GLU A CD 956 O OE1 . GLU A 121 ? 1.5074 1.2529 1.5878 -0.2378 -0.1993 0.0972 121 GLU A OE1 957 O OE2 . GLU A 121 ? 1.6803 1.4545 1.7789 -0.2464 -0.2486 0.1227 121 GLU A OE2 958 N N . ARG A 122 ? 0.9427 0.6906 1.0397 -0.2465 -0.1293 0.0544 122 ARG A N 959 C CA . ARG A 122 ? 0.9297 0.6580 0.9942 -0.2474 -0.1052 0.0419 122 ARG A CA 960 C C . ARG A 122 ? 0.9678 0.6640 0.9788 -0.2440 -0.1106 0.0436 122 ARG A C 961 O O . ARG A 122 ? 1.4426 1.1310 1.4561 -0.2322 -0.1121 0.0488 122 ARG A O 962 C CB . ARG A 122 ? 0.9325 0.6721 1.0331 -0.2368 -0.0813 0.0332 122 ARG A CB 963 C CG . ARG A 122 ? 0.9428 0.7192 1.1048 -0.2381 -0.0736 0.0307 122 ARG A CG 964 C CD . ARG A 122 ? 0.9521 0.7395 1.1462 -0.2289 -0.0450 0.0163 122 ARG A CD 965 N NE . ARG A 122 ? 1.2454 1.0105 1.3912 -0.2326 -0.0256 0.0040 122 ARG A NE 966 C CZ . ARG A 122 ? 1.2847 1.0587 1.4400 -0.2321 0.0021 -0.0125 122 ARG A CZ 967 N NH1 . ARG A 122 ? 1.2006 1.0056 1.4145 -0.2270 0.0169 -0.0208 122 ARG A NH1 968 N NH2 . ARG A 122 ? 1.1149 0.8685 1.2217 -0.2373 0.0149 -0.0215 122 ARG A NH2 969 N N . GLU A 123 ? 1.0949 0.7728 1.0618 -0.2544 -0.1128 0.0393 123 GLU A N 970 C CA . GLU A 123 ? 1.1278 0.7788 1.0471 -0.2520 -0.1178 0.0399 123 GLU A CA 971 C C . GLU A 123 ? 1.1206 0.7514 1.0096 -0.2535 -0.1008 0.0309 123 GLU A C 972 O O . GLU A 123 ? 0.8988 0.5252 0.7774 -0.2639 -0.0972 0.0261 123 GLU A O 973 C CB . GLU A 123 ? 0.9792 0.6248 0.8731 -0.2614 -0.1384 0.0418 123 GLU A CB 974 C CG . GLU A 123 ? 1.0125 0.6781 0.9291 -0.2612 -0.1604 0.0533 123 GLU A CG 975 C CD . GLU A 123 ? 1.1326 0.7905 1.0126 -0.2713 -0.1811 0.0530 123 GLU A CD 976 O OE1 . GLU A 123 ? 1.3200 0.9950 1.2123 -0.2743 -0.2028 0.0632 123 GLU A OE1 977 O OE2 . GLU A 123 ? 1.2377 0.8731 1.0776 -0.2765 -0.1762 0.0420 123 GLU A OE2 978 N N . PRO A 124 ? 1.0787 0.6970 0.9557 -0.2441 -0.0919 0.0304 124 PRO A N 979 C CA . PRO A 124 ? 1.1008 0.7025 0.9526 -0.2450 -0.0779 0.0234 124 PRO A CA 980 C C . PRO A 124 ? 1.2131 0.7953 1.0283 -0.2504 -0.0842 0.0218 124 PRO A C 981 O O . PRO A 124 ? 0.9981 0.5657 0.7905 -0.2453 -0.0844 0.0222 124 PRO A O 982 C CB . PRO A 124 ? 0.9041 0.4991 0.7578 -0.2340 -0.0719 0.0246 124 PRO A CB 983 C CG . PRO A 124 ? 0.9358 0.5345 0.7973 -0.2285 -0.0869 0.0355 124 PRO A CG 984 C CD . PRO A 124 ? 0.9720 0.5909 0.8602 -0.2330 -0.0973 0.0387 124 PRO A CD 985 N N . VAL A 125 ? 1.2190 0.8015 1.0329 -0.2610 -0.0885 0.0197 125 VAL A N 986 C CA . VAL A 125 ? 0.9778 0.5402 0.7648 -0.2663 -0.0942 0.0158 125 VAL A CA 987 C C . VAL A 125 ? 0.9613 0.5085 0.7334 -0.2660 -0.0835 0.0141 125 VAL A C 988 O O . VAL A 125 ? 0.9155 0.4451 0.6672 -0.2623 -0.0843 0.0113 125 VAL A O 989 C CB . VAL A 125 ? 0.9530 0.5187 0.7494 -0.2790 -0.1034 0.0146 125 VAL A CB 990 C CG1 . VAL A 125 ? 1.5105 1.0522 1.2876 -0.2849 -0.1047 0.0098 125 VAL A CG1 991 C CG2 . VAL A 125 ? 0.9768 0.5522 0.7775 -0.2807 -0.1201 0.0150 125 VAL A CG2 992 N N . GLY A 126 ? 1.1330 0.6892 0.9164 -0.2706 -0.0734 0.0160 126 GLY A N 993 C CA . GLY A 126 ? 1.1098 0.6549 0.8789 -0.2732 -0.0661 0.0173 126 GLY A CA 994 C C . GLY A 126 ? 1.2945 0.8289 1.0601 -0.2846 -0.0713 0.0210 126 GLY A C 995 O O . GLY A 126 ? 1.1517 0.6778 0.9188 -0.2878 -0.0815 0.0188 126 GLY A O 996 N N . THR A 127 ? 1.0422 0.5756 0.8022 -0.2918 -0.0651 0.0270 127 THR A N 997 C CA . THR A 127 ? 0.9386 0.4599 0.6975 -0.3036 -0.0707 0.0349 127 THR A CA 998 C C . THR A 127 ? 1.0974 0.6094 0.8416 -0.3062 -0.0688 0.0435 127 THR A C 999 O O . THR A 127 ? 1.1761 0.6970 0.9109 -0.3027 -0.0612 0.0424 127 THR A O 1000 C CB . THR A 127 ? 1.2455 0.7850 1.0206 -0.3180 -0.0672 0.0399 127 THR A CB 1001 O OG1 . THR A 127 ? 1.3579 0.8822 1.1338 -0.3308 -0.0742 0.0499 127 THR A OG1 1002 C CG2 . THR A 127 ? 1.0027 0.5650 0.7765 -0.3224 -0.0515 0.0415 127 THR A CG2 1003 N N . CYS A 128 ? 1.1988 0.6920 0.9429 -0.3129 -0.0775 0.0526 128 CYS A N 1004 C CA . CYS A 128 ? 1.1128 0.5977 0.8462 -0.3169 -0.0797 0.0654 128 CYS A CA 1005 C C . CYS A 128 ? 1.3890 0.8699 1.1257 -0.3345 -0.0840 0.0822 128 CYS A C 1006 O O . CYS A 128 ? 1.2320 0.7081 0.9833 -0.3416 -0.0877 0.0824 128 CYS A O 1007 C CB . CYS A 128 ? 0.9760 0.4382 0.7109 -0.3044 -0.0882 0.0633 128 CYS A CB 1008 S SG . CYS A 128 ? 1.6157 1.0836 1.3448 -0.2865 -0.0822 0.0485 128 CYS A SG 1009 N N . PHE A 129 ? 1.2157 0.6992 0.9384 -0.3431 -0.0844 0.0976 129 PHE A N 1010 C CA . PHE A 129 ? 1.0394 0.5170 0.7627 -0.3611 -0.0903 0.1192 129 PHE A CA 1011 C C . PHE A 129 ? 1.1253 0.5813 0.8468 -0.3592 -0.1047 0.1356 129 PHE A C 1012 O O . PHE A 129 ? 1.4055 0.8690 1.1105 -0.3571 -0.1054 0.1398 129 PHE A O 1013 C CB . PHE A 129 ? 1.2542 0.7606 0.9601 -0.3782 -0.0772 0.1268 129 PHE A CB 1014 C CG . PHE A 129 ? 1.2303 0.7592 0.9486 -0.3820 -0.0635 0.1144 129 PHE A CG 1015 C CD1 . PHE A 129 ? 1.1006 0.6493 0.8186 -0.3712 -0.0508 0.0948 129 PHE A CD1 1016 C CD2 . PHE A 129 ? 1.0513 0.5819 0.7866 -0.3965 -0.0642 0.1236 129 PHE A CD2 1017 C CE1 . PHE A 129 ? 1.4569 1.0278 1.1938 -0.3733 -0.0396 0.0849 129 PHE A CE1 1018 C CE2 . PHE A 129 ? 1.0406 0.5955 0.7935 -0.3999 -0.0527 0.1131 129 PHE A CE2 1019 C CZ . PHE A 129 ? 1.2737 0.8493 1.0285 -0.3876 -0.0407 0.0940 129 PHE A CZ 1020 N N . LEU A 130 ? 1.2604 0.6997 1.0068 -0.3536 -0.1154 0.1415 130 LEU A N 1021 C CA . LEU A 130 ? 1.2846 0.7079 1.0419 -0.3473 -0.1294 0.1572 130 LEU A CA 1022 C C . LEU A 130 ? 1.2619 0.6898 1.0175 -0.3642 -0.1360 0.1854 130 LEU A C 1023 O O . LEU A 130 ? 1.3496 0.7754 1.1218 -0.3710 -0.1361 0.1901 130 LEU A O 1024 C CB . LEU A 130 ? 1.1780 0.5773 0.9673 -0.3297 -0.1359 0.1446 130 LEU A CB 1025 C CG . LEU A 130 ? 1.1061 0.4858 0.9187 -0.3214 -0.1500 0.1593 130 LEU A CG 1026 C CD1 . LEU A 130 ? 1.3953 0.7789 1.1965 -0.3162 -0.1545 0.1658 130 LEU A CD1 1027 C CD2 . LEU A 130 ? 1.3351 0.6899 1.1794 -0.3057 -0.1517 0.1408 130 LEU A CD2 1028 N N . GLN A 131 ? 1.1331 0.5683 0.8679 -0.3726 -0.1422 0.2049 131 GLN A N 1029 C CA . GLN A 131 ? 1.3626 0.8051 1.0896 -0.3904 -0.1494 0.2347 131 GLN A CA 1030 C C . GLN A 131 ? 1.3820 0.8082 1.1283 -0.3831 -0.1703 0.2565 131 GLN A C 1031 O O . GLN A 131 ? 1.3007 0.7236 1.0438 -0.3748 -0.1790 0.2578 131 GLN A O 1032 C CB . GLN A 131 ? 1.1802 0.6486 0.8615 -0.4120 -0.1402 0.2431 131 GLN A CB 1033 C CG . GLN A 131 ? 1.5505 1.0291 1.2158 -0.4315 -0.1493 0.2763 131 GLN A CG 1034 C CD . GLN A 131 ? 1.5519 1.0602 1.1710 -0.4570 -0.1332 0.2803 131 GLN A CD 1035 O OE1 . GLN A 131 ? 1.5546 1.0766 1.1692 -0.4640 -0.1125 0.2636 131 GLN A OE1 1036 N NE2 . GLN A 131 ? 1.5821 1.1023 1.1674 -0.4718 -0.1421 0.3018 131 GLN A NE2 1037 N N . ASP A 132 ? 1.4563 0.8722 1.2270 -0.3865 -0.1788 0.2740 132 ASP A N 1038 C CA . ASP A 132 ? 1.3886 0.7908 1.1808 -0.3825 -0.1996 0.2998 132 ASP A CA 1039 C C . ASP A 132 ? 1.2895 0.7027 1.0706 -0.4043 -0.2053 0.3315 132 ASP A C 1040 O O . ASP A 132 ? 1.6848 1.0929 1.4824 -0.4103 -0.2004 0.3333 132 ASP A O 1041 C CB . ASP A 132 ? 1.3973 0.7689 1.2404 -0.3614 -0.2056 0.2882 132 ASP A CB 1042 C CG . ASP A 132 ? 1.7023 1.0585 1.5753 -0.3530 -0.2268 0.3117 132 ASP A CG 1043 O OD1 . ASP A 132 ? 1.8688 1.2394 1.7223 -0.3650 -0.2398 0.3402 132 ASP A OD1 1044 O OD2 . ASP A 132 ? 1.7806 1.1108 1.6971 -0.3351 -0.2309 0.3012 132 ASP A OD2 1045 N N . GLY A 133 ? 1.3304 0.7592 1.0829 -0.4174 -0.2164 0.3569 133 GLY A N 1046 C CA . GLY A 133 ? 1.3584 0.8030 1.0904 -0.4411 -0.2202 0.3874 133 GLY A CA 1047 C C . GLY A 133 ? 1.5396 1.0075 1.2408 -0.4599 -0.1962 0.3772 133 GLY A C 1048 O O . GLY A 133 ? 1.6520 1.1360 1.3222 -0.4633 -0.1805 0.3568 133 GLY A O 1049 N N . THR A 134 ? 1.9088 1.3784 1.6220 -0.4722 -0.1928 0.3914 134 THR A N 1050 C CA . THR A 134 ? 1.7975 1.2915 1.4895 -0.4908 -0.1695 0.3840 134 THR A CA 1051 C C . THR A 134 ? 1.6843 1.1700 1.4025 -0.4784 -0.1547 0.3509 134 THR A C 1052 O O . THR A 134 ? 1.7912 1.2991 1.4916 -0.4882 -0.1340 0.3350 134 THR A O 1053 C CB . THR A 134 ? 1.7523 1.2534 1.4496 -0.5106 -0.1712 0.4134 134 THR A CB 1054 O OG1 . THR A 134 ? 1.7369 1.2062 1.4862 -0.4978 -0.1844 0.4182 134 THR A OG1 1055 C CG2 . THR A 134 ? 1.7341 1.2499 1.3973 -0.5270 -0.1847 0.4468 134 THR A CG2 1056 N N . LYS A 135 ? 1.3206 0.7759 1.0816 -0.4576 -0.1652 0.3399 135 LYS A N 1057 C CA . LYS A 135 ? 1.3094 0.7562 1.0952 -0.4468 -0.1547 0.3096 135 LYS A CA 1058 C C . LYS A 135 ? 1.4357 0.8882 1.2047 -0.4345 -0.1452 0.2804 135 LYS A C 1059 O O . LYS A 135 ? 1.2595 0.7064 1.0168 -0.4237 -0.1524 0.2786 135 LYS A O 1060 C CB . LYS A 135 ? 1.2928 0.7048 1.1252 -0.4299 -0.1678 0.3043 135 LYS A CB 1061 C CG . LYS A 135 ? 1.3989 0.8035 1.2555 -0.4245 -0.1590 0.2764 135 LYS A CG 1062 C CD . LYS A 135 ? 1.3720 0.7410 1.2704 -0.4092 -0.1703 0.2671 135 LYS A CD 1063 C CE . LYS A 135 ? 1.4906 0.8544 1.4073 -0.4068 -0.1630 0.2381 135 LYS A CE 1064 N NZ . LYS A 135 ? 1.6622 0.9904 1.6159 -0.3940 -0.1718 0.2245 135 LYS A NZ 1065 N N . THR A 136 ? 1.4105 0.8748 1.1812 -0.4369 -0.1298 0.2587 136 THR A N 1066 C CA . THR A 136 ? 1.2329 0.7015 0.9920 -0.4253 -0.1208 0.2308 136 THR A CA 1067 C C . THR A 136 ? 1.2617 0.7232 1.0482 -0.4160 -0.1172 0.2060 136 THR A C 1068 O O . THR A 136 ? 1.3163 0.7897 1.1153 -0.4287 -0.1104 0.2063 136 THR A O 1069 C CB . THR A 136 ? 1.1794 0.6783 0.9016 -0.4417 -0.1032 0.2292 136 THR A CB 1070 O OG1 . THR A 136 ? 1.4807 0.9866 1.1709 -0.4515 -0.1079 0.2497 136 THR A OG1 1071 C CG2 . THR A 136 ? 1.1430 0.6435 0.8585 -0.4294 -0.0943 0.2005 136 THR A CG2 1072 N N . VAL A 137 ? 1.1386 0.5824 0.9338 -0.3953 -0.1220 0.1851 137 VAL A N 1073 C CA . VAL A 137 ? 1.1214 0.5591 0.9361 -0.3870 -0.1205 0.1606 137 VAL A CA 1074 C C . VAL A 137 ? 1.3053 0.7528 1.1028 -0.3780 -0.1120 0.1390 137 VAL A C 1075 O O . VAL A 137 ? 1.2555 0.7057 1.0317 -0.3728 -0.1095 0.1395 137 VAL A O 1076 C CB . VAL A 137 ? 1.1307 0.5374 0.9720 -0.3714 -0.1324 0.1516 137 VAL A CB 1077 C CG1 . VAL A 137 ? 1.1655 0.5589 1.0285 -0.3795 -0.1413 0.1733 137 VAL A CG1 1078 C CG2 . VAL A 137 ? 1.1939 0.5871 1.0283 -0.3531 -0.1361 0.1448 137 VAL A CG2 1079 N N . GLU A 138 ? 1.0920 0.5448 0.8999 -0.3773 -0.1091 0.1210 138 GLU A N 1080 C CA . GLU A 138 ? 1.1263 0.5873 0.9215 -0.3687 -0.1028 0.1019 138 GLU A CA 1081 C C . GLU A 138 ? 1.2491 0.6895 1.0495 -0.3504 -0.1105 0.0826 138 GLU A C 1082 O O . GLU A 138 ? 1.4552 0.8845 1.2728 -0.3499 -0.1176 0.0736 138 GLU A O 1083 C CB . GLU A 138 ? 1.2228 0.7065 1.0259 -0.3812 -0.0955 0.0962 138 GLU A CB 1084 C CG . GLU A 138 ? 1.2810 0.7801 1.0777 -0.3684 -0.0889 0.0782 138 GLU A CG 1085 C CD . GLU A 138 ? 1.4313 0.9618 1.2466 -0.3751 -0.0815 0.0736 138 GLU A CD 1086 O OE1 . GLU A 138 ? 1.3271 0.8606 1.1620 -0.3907 -0.0855 0.0799 138 GLU A OE1 1087 O OE2 . GLU A 138 ? 1.4594 1.0117 1.2741 -0.3648 -0.0721 0.0641 138 GLU A OE2 1088 N N . TYR A 139 ? 1.2117 0.6473 0.9964 -0.3372 -0.1082 0.0755 139 TYR A N 1089 C CA . TYR A 139 ? 1.1882 0.6073 0.9733 -0.3218 -0.1120 0.0567 139 TYR A CA 1090 C C . TYR A 139 ? 1.0057 0.4382 0.7762 -0.3166 -0.1059 0.0432 139 TYR A C 1091 O O . TYR A 139 ? 1.1628 0.6095 0.9222 -0.3094 -0.0981 0.0449 139 TYR A O 1092 C CB . TYR A 139 ? 1.0304 0.4325 0.8155 -0.3093 -0.1145 0.0596 139 TYR A CB 1093 C CG . TYR A 139 ? 1.0318 0.4165 0.8172 -0.2953 -0.1154 0.0390 139 TYR A CG 1094 C CD1 . TYR A 139 ? 1.1865 0.5558 0.9833 -0.2949 -0.1203 0.0242 139 TYR A CD1 1095 C CD2 . TYR A 139 ? 1.0196 0.4033 0.7925 -0.2844 -0.1105 0.0333 139 TYR A CD2 1096 C CE1 . TYR A 139 ? 1.0583 0.4109 0.8496 -0.2848 -0.1193 0.0029 139 TYR A CE1 1097 C CE2 . TYR A 139 ? 1.0234 0.3969 0.7959 -0.2716 -0.1079 0.0143 139 TYR A CE2 1098 C CZ . TYR A 139 ? 1.3262 0.6812 1.1044 -0.2733 -0.1123 -0.0014 139 TYR A CZ 1099 O OH . TYR A 139 ? 1.4312 0.7779 1.2043 -0.2620 -0.1075 -0.0228 139 TYR A OH 1100 N N . ALA A 140 ? 1.0968 0.5314 0.8713 -0.3172 -0.1098 0.0299 140 ALA A N 1101 C CA . ALA A 140 ? 1.1964 0.6519 0.9634 -0.3091 -0.1056 0.0202 140 ALA A CA 1102 C C . ALA A 140 ? 1.1592 0.6038 0.9198 -0.3041 -0.1132 0.0034 140 ALA A C 1103 O O . ALA A 140 ? 1.1219 0.5772 0.8872 -0.3105 -0.1198 -0.0017 140 ALA A O 1104 C CB . ALA A 140 ? 0.9793 0.4625 0.7589 -0.3187 -0.1024 0.0258 140 ALA A CB 1105 N N . PRO A 141 ? 1.0079 0.4336 0.7579 -0.2934 -0.1120 -0.0057 141 PRO A N 1106 C CA . PRO A 141 ? 1.0920 0.5055 0.8309 -0.2899 -0.1168 -0.0246 141 PRO A CA 1107 C C . PRO A 141 ? 1.0693 0.5042 0.7934 -0.2876 -0.1181 -0.0296 141 PRO A C 1108 O O . PRO A 141 ? 1.1021 0.5341 0.8165 -0.2923 -0.1264 -0.0425 141 PRO A O 1109 C CB . PRO A 141 ? 1.2647 0.6620 0.9983 -0.2767 -0.1095 -0.0308 141 PRO A CB 1110 C CG . PRO A 141 ? 1.2065 0.6173 0.9421 -0.2712 -0.1019 -0.0149 141 PRO A CG 1111 C CD . PRO A 141 ? 0.9994 0.4189 0.7466 -0.2836 -0.1049 0.0006 141 PRO A CD 1112 N N . CYS A 142 ? 1.1692 0.6246 0.8921 -0.2814 -0.1112 -0.0193 142 CYS A N 1113 C CA . CYS A 142 ? 1.3366 0.8113 1.0504 -0.2784 -0.1137 -0.0196 142 CYS A CA 1114 C C . CYS A 142 ? 1.3671 0.8597 1.0970 -0.2888 -0.1239 -0.0153 142 CYS A C 1115 O O . CYS A 142 ? 1.2226 0.7315 0.9496 -0.2879 -0.1308 -0.0138 142 CYS A O 1116 C CB . CYS A 142 ? 1.4416 0.9291 1.1552 -0.2682 -0.1034 -0.0102 142 CYS A CB 1117 S SG . CYS A 142 ? 1.4227 0.9073 1.1120 -0.2568 -0.0978 -0.0152 142 CYS A SG 1118 N N . ARG A 143 ? 0.9924 0.4834 0.7416 -0.2992 -0.1256 -0.0112 143 ARG A N 1119 C CA . ARG A 143 ? 0.9924 0.5028 0.7634 -0.3106 -0.1344 -0.0072 143 ARG A CA 1120 C C . ARG A 143 ? 1.3085 0.8053 1.0760 -0.3219 -0.1493 -0.0188 143 ARG A C 1121 O O . ARG A 143 ? 1.5614 1.0365 1.3333 -0.3295 -0.1506 -0.0226 143 ARG A O 1122 C CB . ARG A 143 ? 0.9807 0.5007 0.7751 -0.3182 -0.1259 0.0043 143 ARG A CB 1123 C CG . ARG A 143 ? 1.0281 0.5765 0.8523 -0.3279 -0.1298 0.0100 143 ARG A CG 1124 C CD . ARG A 143 ? 0.9661 0.5281 0.8085 -0.3345 -0.1156 0.0207 143 ARG A CD 1125 N NE . ARG A 143 ? 1.4653 1.0057 1.3036 -0.3458 -0.1154 0.0251 143 ARG A NE 1126 C CZ . ARG A 143 ? 1.2834 0.8298 1.1274 -0.3542 -0.1039 0.0365 143 ARG A CZ 1127 N NH1 . ARG A 143 ? 1.2523 0.8263 1.1047 -0.3522 -0.0892 0.0405 143 ARG A NH1 1128 N NH2 . ARG A 143 ? 1.0007 0.5253 0.8420 -0.3650 -0.1069 0.0440 143 ARG A NH2 1129 N N . SER A 144 ? 1.0910 0.6001 0.8513 -0.3240 -0.1621 -0.0239 144 SER A N 1130 C CA . SER A 144 ? 1.4444 0.9387 1.1906 -0.3341 -0.1767 -0.0400 144 SER A CA 1131 C C . SER A 144 ? 1.2901 0.8081 1.0391 -0.3423 -0.1953 -0.0395 144 SER A C 1132 O O . SER A 144 ? 1.1869 0.7335 0.9571 -0.3396 -0.1971 -0.0248 144 SER A O 1133 C CB . SER A 144 ? 1.5609 1.0324 1.2713 -0.3250 -0.1712 -0.0554 144 SER A CB 1134 O OG . SER A 144 ? 1.0980 0.5839 0.7907 -0.3128 -0.1652 -0.0489 144 SER A OG 1135 N N . GLN A 145 ? 1.2048 0.7107 0.9332 -0.3523 -0.2097 -0.0564 145 GLN A N 1136 C CA . GLN A 145 ? 1.3809 0.9087 1.1076 -0.3629 -0.2317 -0.0565 145 GLN A CA 1137 C C . GLN A 145 ? 1.4587 0.9979 1.1514 -0.3536 -0.2344 -0.0534 145 GLN A C 1138 O O . GLN A 145 ? 1.6073 1.1655 1.2911 -0.3614 -0.2544 -0.0506 145 GLN A O 1139 C CB . GLN A 145 ? 1.6730 1.1827 1.3891 -0.3805 -0.2475 -0.0778 145 GLN A CB 1140 C CG . GLN A 145 ? 1.7391 1.2284 1.4855 -0.3901 -0.2437 -0.0815 145 GLN A CG 1141 C CD . GLN A 145 ? 1.6185 1.1347 1.4132 -0.4001 -0.2492 -0.0629 145 GLN A CD 1142 O OE1 . GLN A 145 ? 1.3836 0.9203 1.2002 -0.3908 -0.2364 -0.0440 145 GLN A OE1 1143 N NE2 . GLN A 145 ? 1.1835 0.7005 0.9965 -0.4199 -0.2674 -0.0698 145 GLN A NE2 1144 N N . ASP A 146 ? 1.4268 0.9551 1.1016 -0.3384 -0.2152 -0.0519 146 ASP A N 1145 C CA . ASP A 146 ? 1.6115 1.1506 1.2582 -0.3293 -0.2141 -0.0445 146 ASP A CA 1146 C C . ASP A 146 ? 1.5361 1.0947 1.2138 -0.3173 -0.2065 -0.0213 146 ASP A C 1147 O O . ASP A 146 ? 1.7143 1.2640 1.4033 -0.3071 -0.1876 -0.0184 146 ASP A O 1148 C CB . ASP A 146 ? 1.4097 0.9256 1.0197 -0.3214 -0.1971 -0.0592 146 ASP A CB 1149 C CG . ASP A 146 ? 1.5928 1.1194 1.1658 -0.3176 -0.1977 -0.0541 146 ASP A CG 1150 O OD1 . ASP A 146 ? 2.0472 1.5957 1.6160 -0.3238 -0.2162 -0.0413 146 ASP A OD1 1151 O OD2 . ASP A 146 ? 1.5600 1.0744 1.1100 -0.3090 -0.1801 -0.0612 146 ASP A OD2 1152 N N . ILE A 147 ? 1.2101 0.7952 0.9028 -0.3186 -0.2221 -0.0054 147 ILE A N 1153 C CA . ILE A 147 ? 1.1849 0.7899 0.9227 -0.3095 -0.2170 0.0129 147 ILE A CA 1154 C C . ILE A 147 ? 1.4626 1.0738 1.1986 -0.2953 -0.2103 0.0282 147 ILE A C 1155 O O . ILE A 147 ? 1.7297 1.3324 1.4737 -0.2846 -0.1906 0.0294 147 ILE A O 1156 C CB . ILE A 147 ? 1.0642 0.6976 0.8401 -0.3182 -0.2379 0.0227 147 ILE A CB 1157 C CG1 . ILE A 147 ? 1.3122 0.9511 1.0586 -0.3312 -0.2643 0.0196 147 ILE A CG1 1158 C CG2 . ILE A 147 ? 1.1281 0.7632 0.9380 -0.3269 -0.2332 0.0163 147 ILE A CG2 1159 C CD1 . ILE A 147 ? 1.4689 1.1403 1.2549 -0.3386 -0.2891 0.0336 147 ILE A CD1 1160 N N . ASP A 148 ? 1.3184 0.9438 1.0443 -0.2964 -0.2280 0.0410 148 ASP A N 1161 C CA . ASP A 148 ? 1.3506 0.9850 1.0909 -0.2839 -0.2256 0.0609 148 ASP A CA 1162 C C . ASP A 148 ? 1.3472 0.9622 1.0541 -0.2756 -0.2069 0.0590 148 ASP A C 1163 O O . ASP A 148 ? 1.2373 0.8331 0.9160 -0.2774 -0.1935 0.0418 148 ASP A O 1164 C CB . ASP A 148 ? 1.7163 1.3710 1.4549 -0.2888 -0.2529 0.0795 148 ASP A CB 1165 C CG . ASP A 148 ? 1.7806 1.4597 1.5633 -0.2957 -0.2729 0.0845 148 ASP A CG 1166 O OD1 . ASP A 148 ? 1.4056 1.0910 1.2341 -0.2918 -0.2614 0.0802 148 ASP A OD1 1167 O OD2 . ASP A 148 ? 1.8739 1.5682 1.6455 -0.3063 -0.3000 0.0930 148 ASP A OD2 1168 N N . ALA A 149 ? 1.2838 0.9039 1.0007 -0.2664 -0.2061 0.0776 149 ALA A N 1169 C CA . ALA A 149 ? 1.1735 0.7783 0.8657 -0.2594 -0.1891 0.0790 149 ALA A CA 1170 C C . ALA A 149 ? 1.1697 0.7637 0.8041 -0.2674 -0.1868 0.0677 149 ALA A C 1171 O O . ALA A 149 ? 1.2155 0.7946 0.8321 -0.2632 -0.1674 0.0577 149 ALA A O 1172 C CB . ALA A 149 ? 1.4717 1.0842 1.1817 -0.2520 -0.1950 0.1039 149 ALA A CB 1173 N N . ASP A 150 ? 1.2318 0.8350 0.8385 -0.2794 -0.2063 0.0678 150 ASP A N 1174 C CA . ASP A 150 ? 1.3047 0.8990 0.8547 -0.2885 -0.2029 0.0518 150 ASP A CA 1175 C C . ASP A 150 ? 1.3432 0.9198 0.8894 -0.2906 -0.1911 0.0227 150 ASP A C 1176 O O . ASP A 150 ? 1.6968 1.2608 1.2057 -0.2937 -0.1802 0.0040 150 ASP A O 1177 C CB . ASP A 150 ? 1.3626 0.9724 0.8808 -0.3031 -0.2289 0.0581 150 ASP A CB 1178 C CG . ASP A 150 ? 1.5606 1.1880 1.1189 -0.3071 -0.2538 0.0691 150 ASP A CG 1179 O OD1 . ASP A 150 ? 1.5365 1.1711 1.1478 -0.2962 -0.2527 0.0843 150 ASP A OD1 1180 O OD2 . ASP A 150 ? 1.9583 1.5938 1.4972 -0.3216 -0.2741 0.0612 150 ASP A OD2 1181 N N . GLY A 151 ? 1.1486 0.7247 0.7361 -0.2890 -0.1926 0.0196 151 GLY A N 1182 C CA . GLY A 151 ? 1.1260 0.6838 0.7180 -0.2905 -0.1821 -0.0023 151 GLY A CA 1183 C C . GLY A 151 ? 1.0800 0.6274 0.6968 -0.2784 -0.1611 -0.0009 151 GLY A C 1184 O O . GLY A 151 ? 1.1867 0.7345 0.8014 -0.2692 -0.1498 0.0088 151 GLY A O 1185 N N . GLN A 152 ? 1.0517 0.5900 0.6914 -0.2801 -0.1571 -0.0096 152 GLN A N 1186 C CA . GLN A 152 ? 1.0719 0.6002 0.7302 -0.2716 -0.1395 -0.0089 152 GLN A CA 1187 C C . GLN A 152 ? 1.1434 0.6863 0.8400 -0.2682 -0.1373 0.0046 152 GLN A C 1188 O O . GLN A 152 ? 1.1893 0.7261 0.8993 -0.2641 -0.1245 0.0046 152 GLN A O 1189 C CB . GLN A 152 ? 1.0680 0.5760 0.7266 -0.2761 -0.1353 -0.0244 152 GLN A CB 1190 C CG . GLN A 152 ? 1.0623 0.5540 0.6888 -0.2789 -0.1352 -0.0432 152 GLN A CG 1191 C CD . GLN A 152 ? 1.2903 0.7584 0.9257 -0.2813 -0.1310 -0.0575 152 GLN A CD 1192 O OE1 . GLN A 152 ? 1.6571 1.1164 1.2930 -0.2920 -0.1418 -0.0690 152 GLN A OE1 1193 N NE2 . GLN A 152 ? 1.4170 0.8739 1.0619 -0.2719 -0.1170 -0.0557 152 GLN A NE2 1194 N N . GLY A 153 ? 1.1599 0.7230 0.8750 -0.2703 -0.1500 0.0152 153 GLY A N 1195 C CA . GLY A 153 ? 1.0462 0.6253 0.8028 -0.2677 -0.1466 0.0238 153 GLY A CA 1196 C C . GLY A 153 ? 1.0325 0.6109 0.8020 -0.2565 -0.1303 0.0290 153 GLY A C 1197 O O . GLY A 153 ? 1.3428 0.9265 1.1365 -0.2559 -0.1198 0.0279 153 GLY A O 1198 N N . PHE A 154 ? 1.1397 0.7126 0.8926 -0.2491 -0.1279 0.0345 154 PHE A N 1199 C CA . PHE A 154 ? 0.9309 0.5014 0.6967 -0.2396 -0.1142 0.0388 154 PHE A CA 1200 C C . PHE A 154 ? 1.0629 0.6156 0.8066 -0.2378 -0.1005 0.0307 154 PHE A C 1201 O O . PHE A 154 ? 1.5215 1.0704 1.2706 -0.2315 -0.0903 0.0329 154 PHE A O 1202 C CB . PHE A 154 ? 0.9410 0.5170 0.7107 -0.2334 -0.1208 0.0532 154 PHE A CB 1203 C CG . PHE A 154 ? 1.0723 0.6676 0.8761 -0.2326 -0.1346 0.0640 154 PHE A CG 1204 C CD1 . PHE A 154 ? 1.3519 0.9577 1.1476 -0.2403 -0.1540 0.0685 154 PHE A CD1 1205 C CD2 . PHE A 154 ? 0.9832 0.5870 0.8300 -0.2244 -0.1284 0.0679 154 PHE A CD2 1206 C CE1 . PHE A 154 ? 1.2902 0.9167 1.1231 -0.2396 -0.1690 0.0801 154 PHE A CE1 1207 C CE2 . PHE A 154 ? 1.0005 0.6238 0.8872 -0.2220 -0.1406 0.0777 154 PHE A CE2 1208 C CZ . PHE A 154 ? 1.1961 0.8318 1.0775 -0.2295 -0.1619 0.0853 154 PHE A CZ 1209 N N . CYS A 155 ? 0.9499 0.4916 0.6729 -0.2434 -0.1015 0.0210 155 CYS A N 1210 C CA . CYS A 155 ? 1.0762 0.6018 0.7824 -0.2412 -0.0912 0.0138 155 CYS A CA 1211 C C . CYS A 155 ? 1.1716 0.6950 0.8913 -0.2377 -0.0797 0.0150 155 CYS A C 1212 O O . CYS A 155 ? 1.0867 0.6033 0.7991 -0.2328 -0.0721 0.0151 155 CYS A O 1213 C CB . CYS A 155 ? 1.1607 0.6744 0.8572 -0.2480 -0.0950 0.0029 155 CYS A CB 1214 S SG . CYS A 155 ? 1.8702 1.3646 1.5616 -0.2448 -0.0845 -0.0041 155 CYS A SG 1215 N N . GLN A 156 ? 0.9835 0.5148 0.7225 -0.2416 -0.0783 0.0157 156 GLN A N 1216 C CA . GLN A 156 ? 1.0337 0.5642 0.7794 -0.2419 -0.0680 0.0150 156 GLN A CA 1217 C C . GLN A 156 ? 1.1098 0.6251 0.8407 -0.2435 -0.0663 0.0125 156 GLN A C 1218 O O . GLN A 156 ? 1.2613 0.7729 0.9895 -0.2405 -0.0604 0.0133 156 GLN A O 1219 C CB . GLN A 156 ? 0.8859 0.4201 0.6397 -0.2348 -0.0612 0.0172 156 GLN A CB 1220 C CG . GLN A 156 ? 1.1046 0.6522 0.8814 -0.2313 -0.0633 0.0209 156 GLN A CG 1221 C CD . GLN A 156 ? 1.0929 0.6401 0.8832 -0.2247 -0.0560 0.0216 156 GLN A CD 1222 O OE1 . GLN A 156 ? 1.1305 0.6731 0.9176 -0.2257 -0.0471 0.0159 156 GLN A OE1 1223 N NE2 . GLN A 156 ? 1.1774 0.7289 0.9839 -0.2187 -0.0613 0.0293 156 GLN A NE2 1224 N N . GLY A 157 ? 1.0256 0.5319 0.7507 -0.2482 -0.0727 0.0095 157 GLY A N 1225 C CA . GLY A 157 ? 1.0557 0.5457 0.7744 -0.2486 -0.0727 0.0077 157 GLY A CA 1226 C C . GLY A 157 ? 1.0536 0.5438 0.7774 -0.2534 -0.0695 0.0142 157 GLY A C 1227 O O . GLY A 157 ? 0.9999 0.5001 0.7300 -0.2614 -0.0682 0.0179 157 GLY A O 1228 N N . GLY A 158 ? 1.0854 0.5666 0.8066 -0.2495 -0.0684 0.0161 158 GLY A N 1229 C CA . GLY A 158 ? 1.0258 0.5087 0.7475 -0.2550 -0.0679 0.0242 158 GLY A CA 1230 C C . GLY A 158 ? 1.2180 0.7109 0.9375 -0.2513 -0.0617 0.0235 158 GLY A C 1231 O O . GLY A 158 ? 1.1271 0.6247 0.8428 -0.2571 -0.0612 0.0281 158 GLY A O 1232 N N . PHE A 159 ? 1.0093 0.5052 0.7300 -0.2432 -0.0579 0.0183 159 PHE A N 1233 C CA . PHE A 159 ? 0.9858 0.4880 0.7085 -0.2397 -0.0527 0.0175 159 PHE A CA 1234 C C . PHE A 159 ? 1.1017 0.5997 0.8251 -0.2387 -0.0547 0.0209 159 PHE A C 1235 O O . PHE A 159 ? 1.2771 0.7804 1.0007 -0.2418 -0.0535 0.0214 159 PHE A O 1236 C CB . PHE A 159 ? 1.1700 0.6737 0.8946 -0.2321 -0.0500 0.0156 159 PHE A CB 1237 C CG . PHE A 159 ? 1.1846 0.6931 0.9162 -0.2297 -0.0449 0.0157 159 PHE A CG 1238 C CD1 . PHE A 159 ? 0.9831 0.4983 0.7236 -0.2314 -0.0417 0.0131 159 PHE A CD1 1239 C CD2 . PHE A 159 ? 1.3524 0.8587 1.0860 -0.2259 -0.0427 0.0177 159 PHE A CD2 1240 C CE1 . PHE A 159 ? 1.0458 0.5616 0.7964 -0.2292 -0.0373 0.0115 159 PHE A CE1 1241 C CE2 . PHE A 159 ? 1.1184 0.6270 0.8612 -0.2253 -0.0389 0.0182 159 PHE A CE2 1242 C CZ . PHE A 159 ? 0.9777 0.4890 0.7287 -0.2268 -0.0368 0.0146 159 PHE A CZ 1243 N N . SER A 160 ? 1.1252 0.6140 0.8516 -0.2345 -0.0583 0.0220 160 SER A N 1244 C CA . SER A 160 ? 0.9830 0.4687 0.7182 -0.2328 -0.0623 0.0270 160 SER A CA 1245 C C . SER A 160 ? 1.1481 0.6207 0.8899 -0.2315 -0.0685 0.0291 160 SER A C 1246 O O . SER A 160 ? 1.3234 0.7882 1.0640 -0.2280 -0.0665 0.0217 160 SER A O 1247 C CB . SER A 160 ? 1.0400 0.5297 0.7841 -0.2245 -0.0566 0.0243 160 SER A CB 1248 O OG . SER A 160 ? 1.0047 0.4902 0.7473 -0.2176 -0.0510 0.0176 160 SER A OG 1249 N N . ILE A 161 ? 1.0014 0.4708 0.7510 -0.2353 -0.0772 0.0394 161 ILE A N 1250 C CA . ILE A 161 ? 0.9352 0.3890 0.6970 -0.2344 -0.0849 0.0440 161 ILE A CA 1251 C C . ILE A 161 ? 1.1215 0.5730 0.9054 -0.2296 -0.0929 0.0534 161 ILE A C 1252 O O . ILE A 161 ? 1.2614 0.7254 1.0459 -0.2319 -0.0961 0.0600 161 ILE A O 1253 C CB . ILE A 161 ? 1.2078 0.6576 0.9598 -0.2475 -0.0916 0.0537 161 ILE A CB 1254 C CG1 . ILE A 161 ? 1.0741 0.5383 0.8122 -0.2584 -0.0945 0.0641 161 ILE A CG1 1255 C CG2 . ILE A 161 ? 1.2586 0.7090 1.0000 -0.2508 -0.0855 0.0442 161 ILE A CG2 1256 C CD1 . ILE A 161 ? 1.3488 0.8132 1.0747 -0.2735 -0.0989 0.0756 161 ILE A CD1 1257 N N . ASP A 162 ? 0.9567 0.3922 0.7620 -0.2228 -0.0970 0.0532 162 ASP A N 1258 C CA . ASP A 162 ? 1.0192 0.4516 0.8542 -0.2173 -0.1071 0.0646 162 ASP A CA 1259 C C . ASP A 162 ? 1.1599 0.5686 1.0178 -0.2137 -0.1142 0.0671 162 ASP A C 1260 O O . ASP A 162 ? 1.0036 0.3986 0.8562 -0.2125 -0.1078 0.0531 162 ASP A O 1261 C CB . ASP A 162 ? 0.9986 0.4420 0.8537 -0.2044 -0.0981 0.0552 162 ASP A CB 1262 C CG . ASP A 162 ? 1.4787 0.9332 1.3582 -0.2035 -0.1099 0.0708 162 ASP A CG 1263 O OD1 . ASP A 162 ? 1.5785 1.0252 1.4713 -0.2074 -0.1266 0.0884 162 ASP A OD1 1264 O OD2 . ASP A 162 ? 1.5562 1.0280 1.4428 -0.1999 -0.1041 0.0672 162 ASP A OD2 1265 N N . PHE A 163 ? 1.2051 0.6082 1.0903 -0.2126 -0.1291 0.0851 163 PHE A N 1266 C CA . PHE A 163 ? 1.0287 0.4063 0.9459 -0.2068 -0.1367 0.0881 163 PHE A CA 1267 C C . PHE A 163 ? 1.1549 0.5303 1.1148 -0.1875 -0.1307 0.0761 163 PHE A C 1268 O O . PHE A 163 ? 1.4005 0.7964 1.3643 -0.1805 -0.1220 0.0694 163 PHE A O 1269 C CB . PHE A 163 ? 1.1463 0.5168 1.0728 -0.2175 -0.1585 0.1190 163 PHE A CB 1270 C CG . PHE A 163 ? 1.2994 0.6675 1.1905 -0.2370 -0.1623 0.1299 163 PHE A CG 1271 C CD1 . PHE A 163 ? 1.0721 0.4169 0.9673 -0.2414 -0.1627 0.1273 163 PHE A CD1 1272 C CD2 . PHE A 163 ? 1.3395 0.7294 1.1955 -0.2517 -0.1645 0.1417 163 PHE A CD2 1273 C CE1 . PHE A 163 ? 1.0784 0.4246 0.9456 -0.2601 -0.1648 0.1383 163 PHE A CE1 1274 C CE2 . PHE A 163 ? 1.3502 0.7414 1.1763 -0.2696 -0.1647 0.1504 163 PHE A CE2 1275 C CZ . PHE A 163 ? 1.0700 0.4408 0.9030 -0.2739 -0.1646 0.1499 163 PHE A CZ 1276 N N . THR A 164 ? 1.1707 0.5210 1.1661 -0.1791 -0.1348 0.0733 164 THR A N 1277 C CA . THR A 164 ? 1.2208 0.5678 1.2646 -0.1595 -0.1279 0.0604 164 THR A CA 1278 C C . THR A 164 ? 1.3869 0.7167 1.4801 -0.1552 -0.1488 0.0835 164 THR A C 1279 O O . THR A 164 ? 1.2361 0.5526 1.3198 -0.1687 -0.1666 0.1070 164 THR A O 1280 C CB . THR A 164 ? 1.3848 0.7156 1.4295 -0.1504 -0.1086 0.0263 164 THR A CB 1281 O OG1 . THR A 164 ? 1.3603 0.6590 1.4095 -0.1560 -0.1175 0.0262 164 THR A OG1 1282 C CG2 . THR A 164 ? 1.0584 0.4062 1.0520 -0.1565 -0.0915 0.0081 164 THR A CG2 1283 N N . LYS A 165 ? 1.4524 0.7840 1.6004 -0.1368 -0.1464 0.0784 165 LYS A N 1284 C CA . LYS A 165 ? 1.3637 0.6828 1.5688 -0.1301 -0.1685 0.1036 165 LYS A CA 1285 C C . LYS A 165 ? 1.3144 0.5957 1.5275 -0.1367 -0.1824 0.1145 165 LYS A C 1286 O O . LYS A 165 ? 1.4519 0.7256 1.6802 -0.1448 -0.2079 0.1497 165 LYS A O 1287 C CB . LYS A 165 ? 1.4245 0.7470 1.6956 -0.1058 -0.1578 0.0870 165 LYS A CB 1288 C CG . LYS A 165 ? 1.4061 0.7302 1.7421 -0.0975 -0.1826 0.1179 165 LYS A CG 1289 C CD . LYS A 165 ? 1.5675 0.9206 1.9540 -0.0791 -0.1717 0.1080 165 LYS A CD 1290 C CE . LYS A 165 ? 1.7243 1.0665 2.1487 -0.0579 -0.1428 0.0678 165 LYS A CE 1291 N NZ . LYS A 165 ? 1.6841 0.9892 2.1701 -0.0447 -0.1523 0.0684 165 LYS A NZ 1292 N N . ALA A 166 ? 1.2502 0.5083 1.4524 -0.1353 -0.1672 0.0858 166 ALA A N 1293 C CA . ALA A 166 ? 1.3490 0.5720 1.5528 -0.1459 -0.1801 0.0959 166 ALA A CA 1294 C C . ALA A 166 ? 1.4615 0.6820 1.6045 -0.1636 -0.1712 0.0829 166 ALA A C 1295 O O . ALA A 166 ? 1.6976 0.9114 1.8272 -0.1591 -0.1526 0.0480 166 ALA A O 1296 C CB . ALA A 166 ? 1.4342 0.6255 1.6966 -0.1280 -0.1754 0.0756 166 ALA A CB 1297 N N . ASP A 167 ? 1.5459 0.7794 1.6529 -0.1827 -0.1827 0.1104 167 ASP A N 1298 C CA . ASP A 167 ? 1.6172 0.8524 1.6824 -0.1988 -0.1771 0.1057 167 ASP A CA 1299 C C . ASP A 167 ? 1.5085 0.7416 1.5399 -0.2008 -0.1592 0.0710 167 ASP A C 1300 O O . ASP A 167 ? 1.7800 0.9998 1.8077 -0.2044 -0.1538 0.0543 167 ASP A O 1301 C CB . ASP A 167 ? 1.9586 1.1731 2.0524 -0.1992 -0.1832 0.1115 167 ASP A CB 1302 C CG . ASP A 167 ? 1.9859 1.2092 2.0882 -0.2082 -0.2027 0.1531 167 ASP A CG 1303 O OD1 . ASP A 167 ? 2.0132 1.2541 2.1147 -0.2086 -0.2139 0.1757 167 ASP A OD1 1304 O OD2 . ASP A 167 ? 1.7988 1.0118 1.9076 -0.2163 -0.2078 0.1635 167 ASP A OD2 1305 N N . ARG A 168 ? 1.2043 0.4623 1.2109 -0.1965 -0.1474 0.0597 168 ARG A N 1306 C CA . ARG A 168 ? 1.2450 0.5130 1.2150 -0.1979 -0.1299 0.0309 168 ARG A CA 1307 C C . ARG A 168 ? 1.1244 0.4271 1.0550 -0.2034 -0.1234 0.0363 168 ARG A C 1308 O O . ARG A 168 ? 1.4120 0.7333 1.3497 -0.1969 -0.1230 0.0451 168 ARG A O 1309 C CB . ARG A 168 ? 1.1287 0.3895 1.1172 -0.1802 -0.1138 -0.0023 168 ARG A CB 1310 C CG . ARG A 168 ? 1.4800 0.7445 1.4307 -0.1841 -0.0994 -0.0316 168 ARG A CG 1311 C CD . ARG A 168 ? 1.2773 0.5360 1.2416 -0.1686 -0.0819 -0.0654 168 ARG A CD 1312 N NE . ARG A 168 ? 1.1838 0.4105 1.1572 -0.1701 -0.0819 -0.0893 168 ARG A NE 1313 C CZ . ARG A 168 ? 1.2717 0.4957 1.2082 -0.1807 -0.0782 -0.1096 168 ARG A CZ 1314 N NH1 . ARG A 168 ? 1.3361 0.5875 1.2272 -0.1892 -0.0745 -0.1065 168 ARG A NH1 1315 N NH2 . ARG A 168 ? 1.4973 0.6905 1.4450 -0.1830 -0.0798 -0.1329 168 ARG A NH2 1316 N N . VAL A 169 ? 1.0717 0.3828 0.9652 -0.2155 -0.1190 0.0306 169 VAL A N 1317 C CA . VAL A 169 ? 1.2456 0.5864 1.1061 -0.2203 -0.1125 0.0342 169 VAL A CA 1318 C C . VAL A 169 ? 1.3470 0.6999 1.1922 -0.2112 -0.0964 0.0100 169 VAL A C 1319 O O . VAL A 169 ? 1.2102 0.5515 1.0518 -0.2085 -0.0903 -0.0111 169 VAL A O 1320 C CB . VAL A 169 ? 1.0361 0.3841 0.8693 -0.2378 -0.1159 0.0435 169 VAL A CB 1321 C CG1 . VAL A 169 ? 1.0486 0.3919 0.8886 -0.2500 -0.1298 0.0713 169 VAL A CG1 1322 C CG2 . VAL A 169 ? 1.6738 1.0085 1.5013 -0.2425 -0.1138 0.0263 169 VAL A CG2 1323 N N . LEU A 170 ? 1.2813 0.6573 1.1165 -0.2079 -0.0903 0.0138 170 LEU A N 1324 C CA . LEU A 170 ? 1.1802 0.5706 0.9969 -0.2025 -0.0759 -0.0029 170 LEU A CA 1325 C C . LEU A 170 ? 1.2775 0.6858 1.0655 -0.2122 -0.0753 0.0040 170 LEU A C 1326 O O . LEU A 170 ? 1.2087 0.6304 0.9951 -0.2153 -0.0778 0.0173 170 LEU A O 1327 C CB . LEU A 170 ? 1.0943 0.4964 0.9297 -0.1903 -0.0675 -0.0053 170 LEU A CB 1328 C CG . LEU A 170 ? 0.9815 0.4007 0.7967 -0.1870 -0.0521 -0.0177 170 LEU A CG 1329 C CD1 . LEU A 170 ? 1.0022 0.4118 0.8022 -0.1854 -0.0435 -0.0397 170 LEU A CD1 1330 C CD2 . LEU A 170 ? 1.0300 0.4639 0.8679 -0.1772 -0.0436 -0.0169 170 LEU A CD2 1331 N N . LEU A 171 ? 1.3479 0.7564 1.1154 -0.2171 -0.0726 -0.0060 171 LEU A N 1332 C CA . LEU A 171 ? 1.0559 0.4804 0.8040 -0.2252 -0.0726 0.0000 171 LEU A CA 1333 C C . LEU A 171 ? 1.2289 0.6645 0.9598 -0.2215 -0.0642 -0.0103 171 LEU A C 1334 O O . LEU A 171 ? 1.3667 0.7965 1.0875 -0.2216 -0.0633 -0.0230 171 LEU A O 1335 C CB . LEU A 171 ? 1.0114 0.4301 0.7561 -0.2369 -0.0805 0.0035 171 LEU A CB 1336 C CG . LEU A 171 ? 1.0264 0.4627 0.7592 -0.2451 -0.0799 0.0089 171 LEU A CG 1337 C CD1 . LEU A 171 ? 1.4781 0.9118 1.2162 -0.2578 -0.0864 0.0193 171 LEU A CD1 1338 C CD2 . LEU A 171 ? 1.1050 0.5474 0.8262 -0.2448 -0.0785 -0.0020 171 LEU A CD2 1339 N N . GLY A 172 ? 1.0467 0.4977 0.7736 -0.2194 -0.0591 -0.0042 172 GLY A N 1340 C CA . GLY A 172 ? 1.1678 0.6296 0.8793 -0.2178 -0.0532 -0.0082 172 GLY A CA 1341 C C . GLY A 172 ? 1.2346 0.7065 0.9400 -0.2241 -0.0572 -0.0017 172 GLY A C 1342 O O . GLY A 172 ? 1.0917 0.5660 0.8041 -0.2293 -0.0605 0.0050 172 GLY A O 1343 N N . GLY A 173 ? 1.0599 0.5389 0.7530 -0.2240 -0.0566 -0.0035 173 GLY A N 1344 C CA . GLY A 173 ? 1.2182 0.7091 0.9139 -0.2261 -0.0585 0.0044 173 GLY A CA 1345 C C . GLY A 173 ? 1.3556 0.8539 1.0404 -0.2233 -0.0566 0.0074 173 GLY A C 1346 O O . GLY A 173 ? 1.4043 0.9008 1.0717 -0.2236 -0.0570 0.0017 173 GLY A O 1347 N N . PRO A 174 ? 1.0449 0.5508 0.7391 -0.2216 -0.0549 0.0164 174 PRO A N 1348 C CA . PRO A 174 ? 1.0082 0.5201 0.6966 -0.2196 -0.0535 0.0247 174 PRO A CA 1349 C C . PRO A 174 ? 1.1585 0.6771 0.8383 -0.2224 -0.0637 0.0300 174 PRO A C 1350 O O . PRO A 174 ? 1.6141 1.1367 1.2785 -0.2229 -0.0644 0.0371 174 PRO A O 1351 C CB . PRO A 174 ? 1.3843 0.8983 1.0935 -0.2175 -0.0501 0.0314 174 PRO A CB 1352 C CG . PRO A 174 ? 1.3134 0.8274 1.0353 -0.2198 -0.0518 0.0259 174 PRO A CG 1353 C CD . PRO A 174 ? 0.9337 0.4415 0.6456 -0.2223 -0.0529 0.0185 174 PRO A CD 1354 N N . GLY A 175 ? 0.9653 0.4871 0.6553 -0.2253 -0.0720 0.0282 175 GLY A N 1355 C CA . GLY A 175 ? 1.1196 0.6517 0.8128 -0.2275 -0.0842 0.0365 175 GLY A CA 1356 C C . GLY A 175 ? 1.1910 0.7250 0.8594 -0.2339 -0.0946 0.0326 175 GLY A C 1357 O O . GLY A 175 ? 1.4980 1.0427 1.1670 -0.2368 -0.1077 0.0419 175 GLY A O 1358 N N . SER A 176 ? 1.0223 0.5461 0.6708 -0.2363 -0.0899 0.0184 176 SER A N 1359 C CA . SER A 176 ? 1.1872 0.7104 0.8108 -0.2437 -0.0991 0.0092 176 SER A CA 1360 C C . SER A 176 ? 1.3023 0.8340 0.8967 -0.2465 -0.1031 0.0167 176 SER A C 1361 O O . SER A 176 ? 1.2948 0.8269 0.8796 -0.2426 -0.0920 0.0224 176 SER A O 1362 C CB . SER A 176 ? 1.3775 0.8848 0.9899 -0.2441 -0.0909 -0.0099 176 SER A CB 1363 O OG . SER A 176 ? 1.3780 0.8772 1.0127 -0.2457 -0.0929 -0.0146 176 SER A OG 1364 N N . PHE A 177 ? 1.1425 0.6826 0.7232 -0.2549 -0.1199 0.0181 177 PHE A N 1365 C CA . PHE A 177 ? 1.1991 0.7483 0.7428 -0.2615 -0.1268 0.0245 177 PHE A CA 1366 C C . PHE A 177 ? 1.3221 0.8802 0.8719 -0.2571 -0.1256 0.0493 177 PHE A C 1367 O O . PHE A 177 ? 1.1627 0.7202 0.6899 -0.2567 -0.1133 0.0523 177 PHE A O 1368 C CB . PHE A 177 ? 1.3060 0.8464 0.8118 -0.2644 -0.1131 0.0040 177 PHE A CB 1369 C CG . PHE A 177 ? 1.4255 0.9500 0.9368 -0.2650 -0.1093 -0.0212 177 PHE A CG 1370 C CD1 . PHE A 177 ? 1.3302 0.8532 0.8504 -0.2725 -0.1259 -0.0276 177 PHE A CD1 1371 C CD2 . PHE A 177 ? 1.6241 1.1350 1.1370 -0.2581 -0.0900 -0.0367 177 PHE A CD2 1372 C CE1 . PHE A 177 ? 1.2782 0.7840 0.8067 -0.2741 -0.1232 -0.0485 177 PHE A CE1 1373 C CE2 . PHE A 177 ? 1.4747 0.9685 0.9980 -0.2581 -0.0881 -0.0573 177 PHE A CE2 1374 C CZ . PHE A 177 ? 1.3405 0.8301 0.8705 -0.2666 -0.1047 -0.0628 177 PHE A CZ 1375 N N . TYR A 178 ? 1.4092 0.9755 0.9932 -0.2540 -0.1379 0.0668 178 TYR A N 1376 C CA . TYR A 178 ? 1.1818 0.7525 0.7831 -0.2486 -0.1383 0.0907 178 TYR A CA 1377 C C . TYR A 178 ? 1.2430 0.8027 0.8506 -0.2415 -0.1164 0.0878 178 TYR A C 1378 O O . TYR A 178 ? 1.1034 0.6640 0.6989 -0.2421 -0.1107 0.1014 178 TYR A O 1379 C CB . TYR A 178 ? 1.1642 0.7459 0.7329 -0.2570 -0.1516 0.1100 178 TYR A CB 1380 C CG . TYR A 178 ? 1.2555 0.8516 0.8382 -0.2613 -0.1785 0.1253 178 TYR A CG 1381 C CD1 . TYR A 178 ? 1.2183 0.8199 0.8481 -0.2537 -0.1886 0.1475 178 TYR A CD1 1382 C CD2 . TYR A 178 ? 1.2677 0.8723 0.8209 -0.2730 -0.1945 0.1165 178 TYR A CD2 1383 C CE1 . TYR A 178 ? 1.2771 0.8946 0.9280 -0.2563 -0.2142 0.1628 178 TYR A CE1 1384 C CE2 . TYR A 178 ? 1.3454 0.9662 0.9153 -0.2777 -0.2216 0.1317 178 TYR A CE2 1385 C CZ . TYR A 178 ? 1.5357 1.1641 1.1565 -0.2688 -0.2315 0.1560 178 TYR A CZ 1386 O OH . TYR A 178 ? 1.8010 1.4481 1.4462 -0.2723 -0.2593 0.1724 178 TYR A OH 1387 N N . TRP A 179 ? 1.3481 0.8988 0.9750 -0.2364 -0.1055 0.0713 179 TRP A N 1388 C CA . TRP A 179 ? 1.2680 0.8099 0.9083 -0.2301 -0.0883 0.0680 179 TRP A CA 1389 C C . TRP A 179 ? 1.1852 0.7246 0.7970 -0.2317 -0.0745 0.0630 179 TRP A C 1390 O O . TRP A 179 ? 1.1422 0.6792 0.7640 -0.2284 -0.0629 0.0681 179 TRP A O 1391 C CB . TRP A 179 ? 1.0739 0.6167 0.7454 -0.2251 -0.0892 0.0854 179 TRP A CB 1392 C CG . TRP A 179 ? 0.9714 0.5171 0.6785 -0.2213 -0.0965 0.0846 179 TRP A CG 1393 C CD1 . TRP A 179 ? 0.9809 0.5223 0.7111 -0.2177 -0.0880 0.0723 179 TRP A CD1 1394 C CD2 . TRP A 179 ? 0.9849 0.5414 0.7092 -0.2216 -0.1132 0.0963 179 TRP A CD2 1395 N NE1 . TRP A 179 ? 1.0723 0.6218 0.8328 -0.2157 -0.0952 0.0738 179 TRP A NE1 1396 C CE2 . TRP A 179 ? 0.9902 0.5493 0.7517 -0.2171 -0.1111 0.0886 179 TRP A CE2 1397 C CE3 . TRP A 179 ? 1.0211 0.5872 0.7336 -0.2260 -0.1303 0.1136 179 TRP A CE3 1398 C CZ2 . TRP A 179 ? 1.0101 0.5821 0.8036 -0.2151 -0.1240 0.0964 179 TRP A CZ2 1399 C CZ3 . TRP A 179 ? 1.0428 0.6209 0.7866 -0.2243 -0.1467 0.1235 179 TRP A CZ3 1400 C CH2 . TRP A 179 ? 1.0059 0.5872 0.7930 -0.2181 -0.1426 0.1143 179 TRP A CH2 1401 N N . GLN A 180 ? 1.1793 0.7201 0.7578 -0.2373 -0.0749 0.0510 180 GLN A N 1402 C CA . GLN A 180 ? 1.2097 0.7487 0.7659 -0.2375 -0.0580 0.0393 180 GLN A CA 1403 C C . GLN A 180 ? 1.1292 0.6575 0.7089 -0.2304 -0.0472 0.0239 180 GLN A C 1404 O O . GLN A 180 ? 1.1946 0.7227 0.7787 -0.2267 -0.0321 0.0205 180 GLN A O 1405 C CB . GLN A 180 ? 1.1814 0.7233 0.6967 -0.2454 -0.0601 0.0252 180 GLN A CB 1406 C CG . GLN A 180 ? 1.2657 0.8210 0.7481 -0.2549 -0.0698 0.0421 180 GLN A CG 1407 C CD . GLN A 180 ? 1.3590 0.9177 0.7953 -0.2649 -0.0725 0.0247 180 GLN A CD 1408 O OE1 . GLN A 180 ? 1.3560 0.9056 0.7852 -0.2635 -0.0618 -0.0023 180 GLN A OE1 1409 N NE2 . GLN A 180 ? 1.4193 0.9906 0.8246 -0.2757 -0.0880 0.0399 180 GLN A NE2 1410 N N . GLY A 181 ? 1.0967 0.6179 0.6933 -0.2295 -0.0558 0.0168 181 GLY A N 1411 C CA . GLY A 181 ? 1.1768 0.6877 0.7940 -0.2247 -0.0494 0.0059 181 GLY A CA 1412 C C . GLY A 181 ? 1.2864 0.7874 0.8919 -0.2260 -0.0482 -0.0139 181 GLY A C 1413 O O . GLY A 181 ? 1.3710 0.8736 0.9487 -0.2301 -0.0474 -0.0231 181 GLY A O 1414 N N . GLN A 182 ? 1.3077 0.7976 0.9339 -0.2234 -0.0484 -0.0204 182 GLN A N 1415 C CA . GLN A 182 ? 1.1848 0.6608 0.8079 -0.2242 -0.0484 -0.0385 182 GLN A CA 1416 C C . GLN A 182 ? 1.2702 0.7349 0.9204 -0.2184 -0.0443 -0.0405 182 GLN A C 1417 O O . GLN A 182 ? 1.0320 0.4991 0.7002 -0.2177 -0.0470 -0.0279 182 GLN A O 1418 C CB . GLN A 182 ? 1.0217 0.4938 0.6404 -0.2328 -0.0634 -0.0418 182 GLN A CB 1419 C CG . GLN A 182 ? 1.2930 0.7483 0.9063 -0.2359 -0.0652 -0.0622 182 GLN A CG 1420 C CD . GLN A 182 ? 1.3528 0.8067 0.9625 -0.2468 -0.0814 -0.0647 182 GLN A CD 1421 O OE1 . GLN A 182 ? 1.3503 0.8147 0.9727 -0.2505 -0.0903 -0.0500 182 GLN A OE1 1422 N NE2 . GLN A 182 ? 1.3165 0.7584 0.9111 -0.2524 -0.0847 -0.0849 182 GLN A NE2 1423 N N . LEU A 183 ? 1.4271 0.8796 1.0803 -0.2145 -0.0381 -0.0565 183 LEU A N 1424 C CA . LEU A 183 ? 1.1841 0.6233 0.8666 -0.2094 -0.0385 -0.0571 183 LEU A CA 1425 C C . LEU A 183 ? 1.1699 0.5890 0.8560 -0.2138 -0.0468 -0.0694 183 LEU A C 1426 O O . LEU A 183 ? 1.0746 0.4870 0.7441 -0.2156 -0.0443 -0.0883 183 LEU A O 1427 C CB . LEU A 183 ? 1.0182 0.4590 0.7153 -0.1990 -0.0243 -0.0641 183 LEU A CB 1428 C CG . LEU A 183 ? 1.0082 0.4678 0.7097 -0.1955 -0.0160 -0.0512 183 LEU A CG 1429 C CD1 . LEU A 183 ? 1.0438 0.5061 0.7695 -0.1854 -0.0030 -0.0581 183 LEU A CD1 1430 C CD2 . LEU A 183 ? 0.9905 0.4537 0.7041 -0.1988 -0.0263 -0.0322 183 LEU A CD2 1431 N N . ILE A 184 ? 1.2298 0.6393 0.9359 -0.2171 -0.0568 -0.0589 184 ILE A N 1432 C CA . ILE A 184 ? 1.1931 0.5812 0.9086 -0.2225 -0.0655 -0.0674 184 ILE A CA 1433 C C . ILE A 184 ? 1.1748 0.5471 0.9227 -0.2180 -0.0685 -0.0595 184 ILE A C 1434 O O . ILE A 184 ? 1.1957 0.5758 0.9539 -0.2187 -0.0721 -0.0398 184 ILE A O 1435 C CB . ILE A 184 ? 1.1130 0.5050 0.8217 -0.2356 -0.0778 -0.0589 184 ILE A CB 1436 C CG1 . ILE A 184 ? 1.0711 0.4821 0.7533 -0.2395 -0.0781 -0.0609 184 ILE A CG1 1437 C CG2 . ILE A 184 ? 1.3388 0.7081 1.0571 -0.2433 -0.0868 -0.0693 184 ILE A CG2 1438 C CD1 . ILE A 184 ? 1.1403 0.5610 0.8237 -0.2506 -0.0894 -0.0511 184 ILE A CD1 1439 N N . SER A 185 ? 1.2556 0.6053 1.0201 -0.2137 -0.0678 -0.0751 185 SER A N 1440 C CA . SER A 185 ? 1.3245 0.6568 1.1256 -0.2086 -0.0732 -0.0656 185 SER A CA 1441 C C . SER A 185 ? 1.3166 0.6205 1.1328 -0.2164 -0.0845 -0.0697 185 SER A C 1442 O O . SER A 185 ? 1.3016 0.5910 1.1111 -0.2182 -0.0826 -0.0936 185 SER A O 1443 C CB . SER A 185 ? 1.1874 0.5170 1.0106 -0.1926 -0.0611 -0.0781 185 SER A CB 1444 O OG . SER A 185 ? 1.1138 0.4311 0.9769 -0.1868 -0.0691 -0.0631 185 SER A OG 1445 N N . ASP A 186 ? 1.1703 0.4661 1.0060 -0.2226 -0.0967 -0.0460 186 ASP A N 1446 C CA . ASP A 186 ? 1.3932 0.6618 1.2467 -0.2323 -0.1086 -0.0442 186 ASP A CA 1447 C C . ASP A 186 ? 1.3100 0.5600 1.2014 -0.2293 -0.1186 -0.0233 186 ASP A C 1448 O O . ASP A 186 ? 1.1177 0.3827 1.0125 -0.2276 -0.1216 -0.0002 186 ASP A O 1449 C CB . ASP A 186 ? 1.3382 0.6179 1.1719 -0.2505 -0.1162 -0.0318 186 ASP A CB 1450 C CG . ASP A 186 ? 1.5715 0.8509 1.3852 -0.2576 -0.1155 -0.0549 186 ASP A CG 1451 O OD1 . ASP A 186 ? 1.7051 0.9598 1.5292 -0.2563 -0.1166 -0.0768 186 ASP A OD1 1452 O OD2 . ASP A 186 ? 1.5314 0.8357 1.3207 -0.2643 -0.1145 -0.0518 186 ASP A OD2 1453 N N . GLN A 187 ? 1.2313 0.4530 1.1533 -0.2281 -0.1238 -0.0312 187 GLN A N 1454 C CA . GLN A 187 ? 1.2894 0.5016 1.2527 -0.2241 -0.1330 -0.0079 187 GLN A CA 1455 C C . GLN A 187 ? 1.2693 0.5035 1.2229 -0.2387 -0.1414 0.0248 187 GLN A C 1456 O O . GLN A 187 ? 1.2262 0.4698 1.1641 -0.2514 -0.1413 0.0233 187 GLN A O 1457 C CB . GLN A 187 ? 1.3951 0.5764 1.3940 -0.2192 -0.1335 -0.0252 187 GLN A CB 1458 C CG . GLN A 187 ? 1.3345 0.4931 1.3433 -0.2048 -0.1227 -0.0627 187 GLN A CG 1459 C CD . GLN A 187 ? 1.4038 0.5327 1.4393 -0.2025 -0.1202 -0.0874 187 GLN A CD 1460 O OE1 . GLN A 187 ? 1.6356 0.7594 1.6827 -0.2126 -0.1276 -0.0748 187 GLN A OE1 1461 N NE2 . GLN A 187 ? 1.5256 0.6347 1.5703 -0.1898 -0.1086 -0.1242 187 GLN A NE2 1462 N N . VAL A 188 ? 1.3287 0.5722 1.2912 -0.2376 -0.1490 0.0536 188 VAL A N 1463 C CA . VAL A 188 ? 1.2491 0.5128 1.1987 -0.2525 -0.1565 0.0844 188 VAL A CA 1464 C C . VAL A 188 ? 1.3105 0.5633 1.2774 -0.2621 -0.1616 0.0918 188 VAL A C 1465 O O . VAL A 188 ? 1.2884 0.5578 1.2361 -0.2775 -0.1610 0.1009 188 VAL A O 1466 C CB . VAL A 188 ? 1.4131 0.6833 1.3731 -0.2501 -0.1674 0.1137 188 VAL A CB 1467 C CG1 . VAL A 188 ? 1.1656 0.4512 1.1133 -0.2672 -0.1764 0.1455 188 VAL A CG1 1468 C CG2 . VAL A 188 ? 1.4834 0.7698 1.4210 -0.2458 -0.1628 0.1097 188 VAL A CG2 1469 N N . ALA A 189 ? 1.3682 0.5924 1.3738 -0.2529 -0.1658 0.0868 189 ALA A N 1470 C CA . ALA A 189 ? 1.2439 0.4524 1.2700 -0.2614 -0.1705 0.0915 189 ALA A CA 1471 C C . ALA A 189 ? 1.3102 0.5224 1.3185 -0.2717 -0.1630 0.0679 189 ALA A C 1472 O O . ALA A 189 ? 1.2723 0.4926 1.2777 -0.2873 -0.1660 0.0805 189 ALA A O 1473 C CB . ALA A 189 ? 1.2809 0.4548 1.3521 -0.2474 -0.1739 0.0827 189 ALA A CB 1474 N N . GLU A 190 ? 1.4051 0.6127 1.4016 -0.2637 -0.1541 0.0346 190 GLU A N 1475 C CA . GLU A 190 ? 1.2269 0.4406 1.2040 -0.2731 -0.1498 0.0112 190 GLU A CA 1476 C C . GLU A 190 ? 1.2531 0.5007 1.2008 -0.2875 -0.1500 0.0279 190 GLU A C 1477 O O . GLU A 190 ? 1.2030 0.4577 1.1499 -0.3011 -0.1520 0.0268 190 GLU A O 1478 C CB . GLU A 190 ? 1.3800 0.5873 1.3400 -0.2627 -0.1413 -0.0237 190 GLU A CB 1479 C CG . GLU A 190 ? 1.4587 0.6325 1.4421 -0.2553 -0.1382 -0.0549 190 GLU A CG 1480 C CD . GLU A 190 ? 1.8125 0.9803 1.7973 -0.2690 -0.1415 -0.0701 190 GLU A CD 1481 O OE1 . GLU A 190 ? 1.6001 0.7903 1.5557 -0.2799 -0.1430 -0.0754 190 GLU A OE1 1482 O OE2 . GLU A 190 ? 2.0634 1.2042 2.0799 -0.2693 -0.1434 -0.0759 190 GLU A OE2 1483 N N . ILE A 191 ? 1.1764 0.4446 1.1026 -0.2850 -0.1474 0.0423 191 ILE A N 1484 C CA . ILE A 191 ? 1.1760 0.4757 1.0748 -0.2974 -0.1449 0.0553 191 ILE A CA 1485 C C . ILE A 191 ? 1.3015 0.6093 1.2102 -0.3132 -0.1497 0.0816 191 ILE A C 1486 O O . ILE A 191 ? 1.5834 0.9103 1.4823 -0.3269 -0.1473 0.0843 191 ILE A O 1487 C CB . ILE A 191 ? 1.2090 0.5255 1.0851 -0.2920 -0.1408 0.0651 191 ILE A CB 1488 C CG1 . ILE A 191 ? 1.3051 0.6151 1.1695 -0.2783 -0.1346 0.0403 191 ILE A CG1 1489 C CG2 . ILE A 191 ? 1.1878 0.5346 1.0383 -0.3052 -0.1361 0.0761 191 ILE A CG2 1490 C CD1 . ILE A 191 ? 1.2799 0.6059 1.1234 -0.2740 -0.1301 0.0478 191 ILE A CD1 1491 N N . VAL A 192 ? 1.1787 0.4722 1.1086 -0.3118 -0.1569 0.1019 192 VAL A N 1492 C CA . VAL A 192 ? 1.3577 0.6573 1.2950 -0.3278 -0.1620 0.1299 192 VAL A CA 1493 C C . VAL A 192 ? 1.3149 0.5981 1.2782 -0.3355 -0.1648 0.1224 192 VAL A C 1494 O O . VAL A 192 ? 1.3981 0.6953 1.3603 -0.3527 -0.1643 0.1346 192 VAL A O 1495 C CB . VAL A 192 ? 1.2184 0.5092 1.1679 -0.3247 -0.1716 0.1581 192 VAL A CB 1496 C CG1 . VAL A 192 ? 1.2421 0.5425 1.1918 -0.3439 -0.1766 0.1895 192 VAL A CG1 1497 C CG2 . VAL A 192 ? 1.2099 0.5160 1.1358 -0.3180 -0.1708 0.1641 192 VAL A CG2 1498 N N . SER A 193 ? 1.2447 0.4980 1.2318 -0.3238 -0.1668 0.1009 193 SER A N 1499 C CA . SER A 193 ? 1.3389 0.5711 1.3528 -0.3312 -0.1704 0.0923 193 SER A CA 1500 C C . SER A 193 ? 1.3494 0.5935 1.3528 -0.3411 -0.1670 0.0694 193 SER A C 1501 O O . SER A 193 ? 1.3065 0.5457 1.3267 -0.3547 -0.1704 0.0702 193 SER A O 1502 C CB . SER A 193 ? 1.3866 0.5809 1.4291 -0.3157 -0.1722 0.0733 193 SER A CB 1503 O OG . SER A 193 ? 1.4536 0.6443 1.4831 -0.3026 -0.1650 0.0404 193 SER A OG 1504 N N . LYS A 194 ? 1.4543 0.7142 1.4312 -0.3351 -0.1616 0.0503 194 LYS A N 1505 C CA . LYS A 194 ? 1.3858 0.6575 1.3522 -0.3434 -0.1614 0.0285 194 LYS A CA 1506 C C . LYS A 194 ? 1.3522 0.6605 1.3010 -0.3568 -0.1590 0.0437 194 LYS A C 1507 O O . LYS A 194 ? 1.1981 0.5204 1.1394 -0.3639 -0.1604 0.0290 194 LYS A O 1508 C CB . LYS A 194 ? 1.3770 0.6426 1.3240 -0.3302 -0.1582 -0.0030 194 LYS A CB 1509 C CG . LYS A 194 ? 1.3377 0.5673 1.3032 -0.3189 -0.1580 -0.0268 194 LYS A CG 1510 C CD . LYS A 194 ? 1.4381 0.6502 1.4243 -0.3298 -0.1634 -0.0436 194 LYS A CD 1511 C CE . LYS A 194 ? 1.6330 0.8065 1.6394 -0.3189 -0.1605 -0.0693 194 LYS A CE 1512 N NZ . LYS A 194 ? 1.6319 0.7857 1.6653 -0.3091 -0.1597 -0.0473 194 LYS A NZ 1513 N N . TYR A 195 ? 1.1938 0.5180 1.1360 -0.3611 -0.1555 0.0721 195 TYR A N 1514 C CA . TYR A 195 ? 1.1698 0.5285 1.0947 -0.3730 -0.1496 0.0831 195 TYR A CA 1515 C C . TYR A 195 ? 1.1834 0.5550 1.1269 -0.3927 -0.1512 0.0901 195 TYR A C 1516 O O . TYR A 195 ? 1.5915 0.9542 1.5550 -0.4025 -0.1540 0.1074 195 TYR A O 1517 C CB . TYR A 195 ? 1.2733 0.6461 1.1819 -0.3745 -0.1441 0.1088 195 TYR A CB 1518 C CG . TYR A 195 ? 1.3539 0.7611 1.2459 -0.3876 -0.1348 0.1166 195 TYR A CG 1519 C CD1 . TYR A 195 ? 1.3945 0.8169 1.2693 -0.3824 -0.1294 0.0996 195 TYR A CD1 1520 C CD2 . TYR A 195 ? 1.1535 0.5779 1.0486 -0.4061 -0.1303 0.1407 195 TYR A CD2 1521 C CE1 . TYR A 195 ? 1.2835 0.7361 1.1493 -0.3942 -0.1196 0.1050 195 TYR A CE1 1522 C CE2 . TYR A 195 ? 1.2028 0.6595 1.0858 -0.4190 -0.1186 0.1452 195 TYR A CE2 1523 C CZ . TYR A 195 ? 1.3303 0.8003 1.2010 -0.4126 -0.1132 0.1265 195 TYR A CZ 1524 O OH . TYR A 195 ? 1.5090 1.0101 1.3735 -0.4254 -0.1002 0.1295 195 TYR A OH 1525 N N . ASP A 196 ? 1.2897 0.6826 1.2283 -0.3990 -0.1500 0.0775 196 ASP A N 1526 C CA . ASP A 196 ? 1.4249 0.8357 1.3844 -0.4184 -0.1515 0.0826 196 ASP A CA 1527 C C . ASP A 196 ? 1.4843 0.9328 1.4344 -0.4272 -0.1425 0.0888 196 ASP A C 1528 O O . ASP A 196 ? 1.3758 0.8359 1.3188 -0.4236 -0.1447 0.0721 196 ASP A O 1529 C CB . ASP A 196 ? 1.4220 0.8204 1.3963 -0.4201 -0.1627 0.0577 196 ASP A CB 1530 C CG . ASP A 196 ? 1.4596 0.8697 1.4642 -0.4410 -0.1667 0.0648 196 ASP A CG 1531 O OD1 . ASP A 196 ? 1.2461 0.6828 1.2582 -0.4547 -0.1587 0.0864 196 ASP A OD1 1532 O OD2 . ASP A 196 ? 1.6693 1.0625 1.6903 -0.4449 -0.1770 0.0477 196 ASP A OD2 1533 N N . PRO A 197 ? 1.1504 0.6182 1.1003 -0.4395 -0.1319 0.1129 197 PRO A N 1534 C CA . PRO A 197 ? 1.2571 0.7612 1.2001 -0.4493 -0.1189 0.1191 197 PRO A CA 1535 C C . PRO A 197 ? 1.2119 0.7396 1.1782 -0.4592 -0.1214 0.1077 197 PRO A C 1536 O O . PRO A 197 ? 1.0993 0.6539 1.0630 -0.4622 -0.1126 0.1054 197 PRO A O 1537 C CB . PRO A 197 ? 1.1492 0.6664 1.0950 -0.4663 -0.1086 0.1467 197 PRO A CB 1538 C CG . PRO A 197 ? 1.1810 0.6736 1.1484 -0.4699 -0.1196 0.1541 197 PRO A CG 1539 C CD . PRO A 197 ? 1.1802 0.6375 1.1420 -0.4490 -0.1320 0.1357 197 PRO A CD 1540 N N . ASN A 198 ? 1.2426 0.7608 1.2342 -0.4651 -0.1339 0.1007 198 ASN A N 1541 C CA . ASN A 198 ? 1.1674 0.7081 1.1839 -0.4751 -0.1411 0.0899 198 ASN A CA 1542 C C . ASN A 198 ? 1.4581 0.9860 1.4616 -0.4616 -0.1557 0.0648 198 ASN A C 1543 O O . ASN A 198 ? 1.7544 1.2984 1.7756 -0.4690 -0.1669 0.0548 198 ASN A O 1544 C CB . ASN A 198 ? 1.2163 0.7568 1.2675 -0.4921 -0.1475 0.0956 198 ASN A CB 1545 C CG . ASN A 198 ? 1.3095 0.8750 1.3779 -0.5106 -0.1320 0.1213 198 ASN A CG 1546 O OD1 . ASN A 198 ? 1.3707 0.9662 1.4336 -0.5153 -0.1163 0.1305 198 ASN A OD1 1547 N ND2 . ASN A 198 ? 1.2048 0.7583 1.2939 -0.5225 -0.1350 0.1325 198 ASN A ND2 1548 N N . VAL A 199 ? 1.2850 0.7861 1.2578 -0.4430 -0.1562 0.0557 199 VAL A N 1549 C CA . VAL A 199 ? 1.1837 0.6723 1.1375 -0.4307 -0.1675 0.0326 199 VAL A CA 1550 C C . VAL A 199 ? 1.1174 0.6091 1.0412 -0.4162 -0.1595 0.0311 199 VAL A C 1551 O O . VAL A 199 ? 1.1084 0.5849 1.0143 -0.4049 -0.1506 0.0363 199 VAL A O 1552 C CB . VAL A 199 ? 1.1473 0.5984 1.0947 -0.4221 -0.1753 0.0173 199 VAL A CB 1553 C CG1 . VAL A 199 ? 1.1721 0.6119 1.0924 -0.4103 -0.1834 -0.0067 199 VAL A CG1 1554 C CG2 . VAL A 199 ? 1.2009 0.6465 1.1791 -0.4371 -0.1846 0.0149 199 VAL A CG2 1555 N N . TYR A 200 ? 1.3528 0.8644 1.2741 -0.4173 -0.1641 0.0250 200 TYR A N 1556 C CA . TYR A 200 ? 1.3365 0.8575 1.2365 -0.4030 -0.1545 0.0251 200 TYR A CA 1557 C C . TYR A 200 ? 1.3400 0.8352 1.2067 -0.3861 -0.1586 0.0100 200 TYR A C 1558 O O . TYR A 200 ? 1.2208 0.7182 1.0691 -0.3704 -0.1474 0.0115 200 TYR A O 1559 C CB . TYR A 200 ? 1.1188 0.6813 1.0388 -0.4009 -0.1548 0.0254 200 TYR A CB 1560 C CG . TYR A 200 ? 1.2113 0.8062 1.1690 -0.4160 -0.1463 0.0388 200 TYR A CG 1561 C CD1 . TYR A 200 ? 1.0287 0.6261 0.9872 -0.4225 -0.1285 0.0526 200 TYR A CD1 1562 C CD2 . TYR A 200 ? 1.2489 0.8744 1.2417 -0.4248 -0.1563 0.0383 200 TYR A CD2 1563 C CE1 . TYR A 200 ? 1.0285 0.6585 1.0195 -0.4377 -0.1175 0.0643 200 TYR A CE1 1564 C CE2 . TYR A 200 ? 1.3909 1.0497 1.4230 -0.4387 -0.1461 0.0500 200 TYR A CE2 1565 C CZ . TYR A 200 ? 1.2467 0.9078 1.2767 -0.4452 -0.1251 0.0623 200 TYR A CZ 1566 O OH . TYR A 200 ? 1.2298 0.9270 1.2970 -0.4604 -0.1118 0.0733 200 TYR A OH 1567 N N . SER A 201 ? 1.0869 0.5607 0.9471 -0.3888 -0.1728 -0.0059 201 SER A N 1568 C CA . SER A 201 ? 1.1385 0.5879 0.9671 -0.3749 -0.1743 -0.0226 201 SER A CA 1569 C C . SER A 201 ? 1.1171 0.5382 0.9502 -0.3713 -0.1749 -0.0329 201 SER A C 1570 O O . SER A 201 ? 1.4229 0.8382 1.2685 -0.3805 -0.1856 -0.0439 201 SER A O 1571 C CB . SER A 201 ? 1.1858 0.6471 0.9987 -0.3742 -0.1868 -0.0367 201 SER A CB 1572 O OG . SER A 201 ? 1.3303 0.8284 1.1511 -0.3688 -0.1842 -0.0252 201 SER A OG 1573 N N . ILE A 202 ? 1.1128 0.5161 0.9389 -0.3582 -0.1643 -0.0301 202 ILE A N 1574 C CA . ILE A 202 ? 1.2507 0.6265 1.0907 -0.3541 -0.1642 -0.0365 202 ILE A CA 1575 C C . ILE A 202 ? 1.1722 0.5236 0.9918 -0.3411 -0.1627 -0.0598 202 ILE A C 1576 O O . ILE A 202 ? 1.4282 0.7785 1.2276 -0.3294 -0.1547 -0.0594 202 ILE A O 1577 C CB . ILE A 202 ? 1.2949 0.6679 1.1502 -0.3506 -0.1555 -0.0135 202 ILE A CB 1578 C CG1 . ILE A 202 ? 1.2022 0.5988 1.0756 -0.3662 -0.1545 0.0083 202 ILE A CG1 1579 C CG2 . ILE A 202 ? 1.2777 0.6201 1.1523 -0.3454 -0.1570 -0.0183 202 ILE A CG2 1580 C CD1 . ILE A 202 ? 1.1166 0.5126 0.9982 -0.3668 -0.1472 0.0325 202 ILE A CD1 1581 N N . LYS A 203 ? 1.5467 0.8787 1.3727 -0.3441 -0.1694 -0.0814 203 LYS A N 1582 C CA . LYS A 203 ? 1.7156 1.0230 1.5247 -0.3333 -0.1656 -0.1077 203 LYS A CA 1583 C C . LYS A 203 ? 1.6316 0.9135 1.4664 -0.3217 -0.1578 -0.1049 203 LYS A C 1584 O O . LYS A 203 ? 1.6165 0.8846 1.4841 -0.3262 -0.1612 -0.1017 203 LYS A O 1585 C CB . LYS A 203 ? 1.7248 1.0228 1.5275 -0.3425 -0.1754 -0.1366 203 LYS A CB 1586 C CG . LYS A 203 ? 1.6264 0.8971 1.4148 -0.3326 -0.1688 -0.1684 203 LYS A CG 1587 C CD . LYS A 203 ? 1.8937 1.1566 1.6745 -0.3435 -0.1785 -0.1994 203 LYS A CD 1588 C CE . LYS A 203 ? 2.0145 1.2506 1.7817 -0.3336 -0.1686 -0.2350 203 LYS A CE 1589 N NZ . LYS A 203 ? 1.9069 1.1355 1.6665 -0.3449 -0.1774 -0.2686 203 LYS A NZ 1590 N N . TYR A 204 ? 1.6320 0.9073 1.4540 -0.3074 -0.1481 -0.1052 204 TYR A N 1591 C CA . TYR A 204 ? 1.5920 0.8448 1.4414 -0.2955 -0.1424 -0.1003 204 TYR A CA 1592 C C . TYR A 204 ? 1.6618 0.8853 1.5123 -0.2861 -0.1372 -0.1340 204 TYR A C 1593 O O . TYR A 204 ? 1.6599 0.8838 1.4759 -0.2827 -0.1317 -0.1556 204 TYR A O 1594 C CB . TYR A 204 ? 1.3632 0.6277 1.2051 -0.2861 -0.1356 -0.0782 204 TYR A CB 1595 C CG . TYR A 204 ? 1.3557 0.6474 1.1983 -0.2949 -0.1381 -0.0474 204 TYR A CG 1596 C CD1 . TYR A 204 ? 1.3698 0.6603 1.2398 -0.2992 -0.1413 -0.0237 204 TYR A CD1 1597 C CD2 . TYR A 204 ? 1.1493 0.4672 0.9648 -0.2997 -0.1364 -0.0426 204 TYR A CD2 1598 C CE1 . TYR A 204 ? 1.3455 0.6611 1.2116 -0.3090 -0.1413 0.0017 204 TYR A CE1 1599 C CE2 . TYR A 204 ? 1.1677 0.5096 0.9855 -0.3079 -0.1360 -0.0187 204 TYR A CE2 1600 C CZ . TYR A 204 ? 1.3941 0.7353 1.2351 -0.3130 -0.1377 0.0023 204 TYR A CZ 1601 O OH . TYR A 204 ? 1.4891 0.8542 1.3280 -0.3231 -0.1352 0.0239 204 TYR A OH 1602 N N . ASN A 205 ? 1.5673 0.7648 1.4567 -0.2828 -0.1377 -0.1389 205 ASN A N 1603 C CA . ASN A 205 ? 1.4141 0.5812 1.3130 -0.2719 -0.1299 -0.1721 205 ASN A CA 1604 C C . ASN A 205 ? 1.6375 0.7987 1.5363 -0.2548 -0.1199 -0.1680 205 ASN A C 1605 O O . ASN A 205 ? 1.8167 0.9883 1.7282 -0.2509 -0.1218 -0.1355 205 ASN A O 1606 C CB . ASN A 205 ? 1.5945 0.7332 1.5400 -0.2729 -0.1317 -0.1766 205 ASN A CB 1607 C CG . ASN A 205 ? 1.9430 1.0845 1.8901 -0.2910 -0.1410 -0.1849 205 ASN A CG 1608 O OD1 . ASN A 205 ? 1.9330 1.0895 1.8476 -0.2999 -0.1453 -0.2036 205 ASN A OD1 1609 N ND2 . ASN A 205 ? 2.0253 1.1520 2.0087 -0.2975 -0.1453 -0.1692 205 ASN A ND2 1610 N N . ASN A 206 ? 1.5111 0.6567 1.3940 -0.2457 -0.1089 -0.2020 206 ASN A N 1611 C CA . ASN A 206 ? 1.5252 0.6668 1.4057 -0.2297 -0.0969 -0.2025 206 ASN A CA 1612 C C . ASN A 206 ? 1.3383 0.5212 1.1920 -0.2293 -0.0944 -0.1742 206 ASN A C 1613 O O . ASN A 206 ? 1.5675 0.7596 1.4413 -0.2193 -0.0926 -0.1508 206 ASN A O 1614 C CB . ASN A 206 ? 1.5099 0.6289 1.4490 -0.2162 -0.0986 -0.1888 206 ASN A CB 1615 C CG . ASN A 206 ? 1.5534 0.6457 1.5320 -0.2165 -0.0995 -0.2042 206 ASN A CG 1616 O OD1 . ASN A 206 ? 1.4445 0.5319 1.4560 -0.2191 -0.1079 -0.1763 206 ASN A OD1 1617 N ND2 . ASN A 206 ? 1.6342 0.7078 1.6030 -0.2154 -0.0898 -0.2486 206 ASN A ND2 1618 N N . GLN A 207 ? 1.5209 0.7279 1.3316 -0.2407 -0.0959 -0.1762 207 GLN A N 1619 C CA . GLN A 207 ? 1.2514 0.4954 1.0381 -0.2393 -0.0922 -0.1538 207 GLN A CA 1620 C C . GLN A 207 ? 1.4077 0.6704 1.1683 -0.2285 -0.0746 -0.1717 207 GLN A C 1621 O O . GLN A 207 ? 1.6849 0.9487 1.4155 -0.2331 -0.0702 -0.1977 207 GLN A O 1622 C CB . GLN A 207 ? 1.2324 0.4948 0.9945 -0.2562 -0.1039 -0.1417 207 GLN A CB 1623 C CG . GLN A 207 ? 1.4083 0.7052 1.1536 -0.2541 -0.1004 -0.1180 207 GLN A CG 1624 C CD . GLN A 207 ? 1.4662 0.7847 1.1892 -0.2675 -0.1093 -0.1114 207 GLN A CD 1625 O OE1 . GLN A 207 ? 1.4668 0.7913 1.1636 -0.2724 -0.1111 -0.1288 207 GLN A OE1 1626 N NE2 . GLN A 207 ? 1.2679 0.5999 1.0017 -0.2739 -0.1150 -0.0862 207 GLN A NE2 1627 N N . LEU A 208 ? 1.3646 0.6431 1.1356 -0.2159 -0.0649 -0.1571 208 LEU A N 1628 C CA . LEU A 208 ? 1.2514 0.5514 1.0008 -0.2069 -0.0471 -0.1687 208 LEU A CA 1629 C C . LEU A 208 ? 1.3816 0.7128 1.0994 -0.2129 -0.0488 -0.1488 208 LEU A C 1630 O O . LEU A 208 ? 1.5473 0.8886 1.2760 -0.2141 -0.0558 -0.1221 208 LEU A O 1631 C CB . LEU A 208 ? 1.4678 0.7680 1.2534 -0.1898 -0.0353 -0.1654 208 LEU A CB 1632 C CG . LEU A 208 ? 1.2182 0.4881 1.0424 -0.1800 -0.0308 -0.1877 208 LEU A CG 1633 C CD1 . LEU A 208 ? 1.3564 0.6297 1.2266 -0.1634 -0.0245 -0.1760 208 LEU A CD1 1634 C CD2 . LEU A 208 ? 1.2604 0.5266 1.0605 -0.1790 -0.0145 -0.2276 208 LEU A CD2 1635 N N . ALA A 209 ? 1.4205 0.7664 1.0991 -0.2175 -0.0428 -0.1621 209 ALA A N 1636 C CA . ALA A 209 ? 1.3654 0.7385 1.0175 -0.2230 -0.0460 -0.1429 209 ALA A CA 1637 C C . ALA A 209 ? 1.3155 0.7069 0.9317 -0.2222 -0.0326 -0.1538 209 ALA A C 1638 O O . ALA A 209 ? 1.3616 0.7463 0.9576 -0.2242 -0.0252 -0.1806 209 ALA A O 1639 C CB . ALA A 209 ? 1.1439 0.5176 0.7847 -0.2374 -0.0645 -0.1359 209 ALA A CB 1640 N N . THR A 210 ? 1.2464 0.6608 0.8542 -0.2205 -0.0290 -0.1331 210 THR A N 1641 C CA . THR A 210 ? 1.1904 0.6244 0.7615 -0.2232 -0.0192 -0.1359 210 THR A CA 1642 C C . THR A 210 ? 1.2907 0.7315 0.8274 -0.2370 -0.0350 -0.1339 210 THR A C 1643 O O . THR A 210 ? 1.4490 0.8865 0.9972 -0.2428 -0.0525 -0.1227 210 THR A O 1644 C CB . THR A 210 ? 1.2388 0.6927 0.8168 -0.2179 -0.0118 -0.1122 210 THR A CB 1645 O OG1 . THR A 210 ? 1.2147 0.6743 0.8006 -0.2220 -0.0273 -0.0885 210 THR A OG1 1646 C CG2 . THR A 210 ? 1.4042 0.8545 1.0201 -0.2053 0.0006 -0.1121 210 THR A CG2 1647 N N . ARG A 211 ? 1.4448 0.8974 0.9399 -0.2433 -0.0292 -0.1437 211 ARG A N 1648 C CA . ARG A 211 ? 1.5658 1.0259 1.0257 -0.2577 -0.0467 -0.1432 211 ARG A CA 1649 C C . ARG A 211 ? 1.5865 1.0716 1.0220 -0.2617 -0.0491 -0.1183 211 ARG A C 1650 O O . ARG A 211 ? 1.7257 1.2212 1.1612 -0.2552 -0.0326 -0.1092 211 ARG A O 1651 C CB . ARG A 211 ? 1.7352 1.1865 1.1601 -0.2658 -0.0425 -0.1773 211 ARG A CB 1652 C CG . ARG A 211 ? 1.8890 1.3409 1.2875 -0.2823 -0.0663 -0.1822 211 ARG A CG 1653 C CD . ARG A 211 ? 2.0450 1.4898 1.4011 -0.2921 -0.0608 -0.2187 211 ARG A CD 1654 N NE . ARG A 211 ? 2.1305 1.5737 1.4657 -0.3094 -0.0864 -0.2259 211 ARG A NE 1655 C CZ . ARG A 211 ? 2.2708 1.7096 1.5626 -0.3228 -0.0885 -0.2570 211 ARG A CZ 1656 N NH1 . ARG A 211 ? 2.2568 1.6926 1.5205 -0.3201 -0.0636 -0.2856 211 ARG A NH1 1657 N NH2 . ARG A 211 ? 2.2331 1.6721 1.5103 -0.3398 -0.1152 -0.2610 211 ARG A NH2 1658 N N . THR A 212 ? 1.4662 0.9610 0.8857 -0.2726 -0.0707 -0.1057 212 THR A N 1659 C CA . THR A 212 ? 1.4011 0.9176 0.8021 -0.2768 -0.0776 -0.0785 212 THR A CA 1660 C C . THR A 212 ? 1.5551 1.0837 0.9104 -0.2815 -0.0621 -0.0834 212 THR A C 1661 O O . THR A 212 ? 1.5824 1.1062 0.9068 -0.2866 -0.0523 -0.1120 212 THR A O 1662 C CB . THR A 212 ? 1.3903 0.9162 0.7819 -0.2888 -0.1059 -0.0670 212 THR A CB 1663 O OG1 . THR A 212 ? 1.4544 0.9997 0.8376 -0.2909 -0.1143 -0.0364 212 THR A OG1 1664 C CG2 . THR A 212 ? 1.3907 0.9148 0.7382 -0.3031 -0.1139 -0.0919 212 THR A CG2 1665 N N . ALA A 213 ? 1.6226 1.1667 0.9751 -0.2802 -0.0584 -0.0561 213 ALA A N 1666 C CA . ALA A 213 ? 1.4709 1.0296 0.7830 -0.2856 -0.0414 -0.0549 213 ALA A CA 1667 C C . ALA A 213 ? 1.4781 1.0553 0.7602 -0.2974 -0.0587 -0.0241 213 ALA A C 1668 O O . ALA A 213 ? 1.5220 1.1007 0.8157 -0.3007 -0.0847 -0.0078 213 ALA A O 1669 C CB . ALA A 213 ? 1.6133 1.1731 0.9541 -0.2737 -0.0170 -0.0493 213 ALA A CB 1670 N N . GLN A 214 ? 1.5775 1.1701 0.8236 -0.3041 -0.0443 -0.0149 214 GLN A N 1671 C CA . GLN A 214 ? 1.7086 1.3187 0.9254 -0.3163 -0.0606 0.0192 214 GLN A CA 1672 C C . GLN A 214 ? 1.7354 1.3433 1.0031 -0.3074 -0.0740 0.0543 214 GLN A C 1673 O O . GLN A 214 ? 1.7354 1.3329 1.0504 -0.2937 -0.0618 0.0532 214 GLN A O 1674 C CB . GLN A 214 ? 1.8100 1.4371 0.9813 -0.3257 -0.0382 0.0243 214 GLN A CB 1675 C CG . GLN A 214 ? 1.7880 1.4208 0.9010 -0.3368 -0.0235 -0.0114 214 GLN A CG 1676 C CD . GLN A 214 ? 1.7246 1.3455 0.8606 -0.3240 0.0066 -0.0502 214 GLN A CD 1677 O OE1 . GLN A 214 ? 1.6235 1.2314 0.8182 -0.3075 0.0126 -0.0497 214 GLN A OE1 1678 N NE2 . GLN A 214 ? 1.8087 1.4345 0.8991 -0.3318 0.0254 -0.0843 214 GLN A NE2 1679 N N . ALA A 215 ? 1.7091 1.3271 0.9681 -0.3156 -0.0997 0.0846 215 ALA A N 1680 C CA . ALA A 215 ? 1.6804 1.2954 0.9914 -0.3069 -0.1147 0.1156 215 ALA A CA 1681 C C . ALA A 215 ? 1.6365 1.2504 0.9693 -0.3012 -0.0968 0.1358 215 ALA A C 1682 O O . ALA A 215 ? 1.5623 1.1687 0.9450 -0.2916 -0.1029 0.1536 215 ALA A O 1683 C CB . ALA A 215 ? 1.6381 1.2656 0.9367 -0.3171 -0.1469 0.1448 215 ALA A CB 1684 N N . ILE A 216 ? 1.5702 1.1922 0.8672 -0.3078 -0.0739 0.1312 216 ILE A N 1685 C CA . ILE A 216 ? 1.4549 1.0778 0.7723 -0.3048 -0.0557 0.1496 216 ILE A CA 1686 C C . ILE A 216 ? 1.3364 0.9450 0.7066 -0.2887 -0.0399 0.1312 216 ILE A C 1687 O O . ILE A 216 ? 1.3804 0.9860 0.7835 -0.2842 -0.0307 0.1463 216 ILE A O 1688 C CB . ILE A 216 ? 1.4240 1.0638 0.6897 -0.3175 -0.0323 0.1480 216 ILE A CB 1689 C CG1 . ILE A 216 ? 1.6473 1.2919 0.9320 -0.3195 -0.0199 0.1786 216 ILE A CG1 1690 C CG2 . ILE A 216 ? 1.4346 1.0733 0.6903 -0.3125 -0.0062 0.1051 216 ILE A CG2 1691 C CD1 . ILE A 216 ? 1.6934 1.3589 0.9282 -0.3342 0.0041 0.1819 216 ILE A CD1 1692 N N . PHE A 217 ? 1.4246 1.0239 0.8027 -0.2816 -0.0385 0.0996 217 PHE A N 1693 C CA . PHE A 217 ? 1.2761 0.8625 0.7003 -0.2678 -0.0270 0.0832 217 PHE A CA 1694 C C . PHE A 217 ? 1.3866 0.9614 0.8547 -0.2597 -0.0455 0.0908 217 PHE A C 1695 O O . PHE A 217 ? 1.2430 0.8074 0.7456 -0.2501 -0.0397 0.0780 217 PHE A O 1696 C CB . PHE A 217 ? 1.2995 0.8806 0.7131 -0.2645 -0.0147 0.0469 217 PHE A CB 1697 C CG . PHE A 217 ? 1.4008 0.9932 0.7832 -0.2689 0.0104 0.0328 217 PHE A CG 1698 C CD1 . PHE A 217 ? 1.3393 0.9351 0.7483 -0.2620 0.0332 0.0298 217 PHE A CD1 1699 C CD2 . PHE A 217 ? 1.5127 1.1145 0.8402 -0.2806 0.0118 0.0209 217 PHE A CD2 1700 C CE1 . PHE A 217 ? 1.3700 0.9796 0.7559 -0.2654 0.0591 0.0156 217 PHE A CE1 1701 C CE2 . PHE A 217 ? 1.4346 1.0488 0.7330 -0.2849 0.0386 0.0046 217 PHE A CE2 1702 C CZ . PHE A 217 ? 1.4218 1.0407 0.7519 -0.2766 0.0634 0.0021 217 PHE A CZ 1703 N N . ASP A 218 ? 1.3461 0.9245 0.8131 -0.2641 -0.0676 0.1117 218 ASP A N 1704 C CA . ASP A 218 ? 1.2450 0.8158 0.7561 -0.2564 -0.0833 0.1185 218 ASP A CA 1705 C C . ASP A 218 ? 1.2260 0.7881 0.7810 -0.2475 -0.0737 0.1260 218 ASP A C 1706 O O . ASP A 218 ? 1.3928 0.9566 0.9471 -0.2497 -0.0630 0.1396 218 ASP A O 1707 C CB . ASP A 218 ? 1.4563 1.0354 0.9659 -0.2617 -0.1082 0.1440 218 ASP A CB 1708 C CG . ASP A 218 ? 1.3667 0.9531 0.8487 -0.2692 -0.1249 0.1332 218 ASP A CG 1709 O OD1 . ASP A 218 ? 1.3413 0.9223 0.8137 -0.2687 -0.1177 0.1045 218 ASP A OD1 1710 O OD2 . ASP A 218 ? 1.5818 1.1789 1.0545 -0.2761 -0.1470 0.1544 218 ASP A OD2 1711 N N . ASP A 219 ? 1.2600 0.8137 0.8517 -0.2393 -0.0771 0.1162 219 ASP A N 1712 C CA . ASP A 219 ? 1.2188 0.7637 0.8510 -0.2321 -0.0702 0.1193 219 ASP A CA 1713 C C . ASP A 219 ? 1.3062 0.8485 0.9368 -0.2313 -0.0504 0.1101 219 ASP A C 1714 O O . ASP A 219 ? 1.2123 0.7512 0.8641 -0.2304 -0.0443 0.1207 219 ASP A O 1715 C CB . ASP A 219 ? 1.0491 0.5934 0.7029 -0.2321 -0.0795 0.1466 219 ASP A CB 1716 C CG . ASP A 219 ? 1.1637 0.7135 0.8258 -0.2321 -0.1009 0.1587 219 ASP A CG 1717 O OD1 . ASP A 219 ? 1.3296 0.8776 1.0222 -0.2257 -0.1062 0.1488 219 ASP A OD1 1718 O OD2 . ASP A 219 ? 1.1912 0.7495 0.8304 -0.2392 -0.1128 0.1791 219 ASP A OD2 1719 N N . SER A 220 ? 1.1533 0.6973 0.7624 -0.2317 -0.0412 0.0904 220 SER A N 1720 C CA . SER A 220 ? 1.1311 0.6747 0.7465 -0.2292 -0.0235 0.0796 220 SER A CA 1721 C C . SER A 220 ? 1.1718 0.7062 0.8186 -0.2226 -0.0230 0.0675 220 SER A C 1722 O O . SER A 220 ? 1.2219 0.7560 0.8876 -0.2207 -0.0137 0.0664 220 SER A O 1723 C CB . SER A 220 ? 1.2955 0.8445 0.8798 -0.2312 -0.0129 0.0627 220 SER A CB 1724 O OG . SER A 220 ? 1.7421 1.3024 1.2916 -0.2396 -0.0102 0.0733 220 SER A OG 1725 N N . TYR A 221 ? 1.2195 0.7486 0.8709 -0.2208 -0.0338 0.0596 221 TYR A N 1726 C CA . TYR A 221 ? 1.3356 0.8577 1.0091 -0.2171 -0.0343 0.0487 221 TYR A CA 1727 C C . TYR A 221 ? 1.1198 0.6392 0.7921 -0.2147 -0.0254 0.0346 221 TYR A C 1728 O O . TYR A 221 ? 1.0334 0.5506 0.7254 -0.2126 -0.0220 0.0327 221 TYR A O 1729 C CB . TYR A 221 ? 1.1494 0.6688 0.8507 -0.2157 -0.0333 0.0559 221 TYR A CB 1730 C CG . TYR A 221 ? 1.0311 0.5501 0.7464 -0.2155 -0.0421 0.0672 221 TYR A CG 1731 C CD1 . TYR A 221 ? 1.0138 0.5371 0.7198 -0.2164 -0.0527 0.0725 221 TYR A CD1 1732 C CD2 . TYR A 221 ? 1.0362 0.5504 0.7779 -0.2143 -0.0405 0.0717 221 TYR A CD2 1733 C CE1 . TYR A 221 ? 1.3390 0.8633 1.0660 -0.2146 -0.0617 0.0841 221 TYR A CE1 1734 C CE2 . TYR A 221 ? 1.1021 0.6144 0.8641 -0.2123 -0.0476 0.0806 221 TYR A CE2 1735 C CZ . TYR A 221 ? 1.3793 0.8973 1.1361 -0.2116 -0.0582 0.0878 221 TYR A CZ 1736 O OH . TYR A 221 ? 1.3665 0.8838 1.1512 -0.2081 -0.0662 0.0979 221 TYR A OH 1737 N N . LEU A 222 ? 0.9741 0.4935 0.6253 -0.2153 -0.0227 0.0243 222 LEU A N 1738 C CA . LEU A 222 ? 1.0399 0.5540 0.6966 -0.2114 -0.0161 0.0093 222 LEU A CA 1739 C C . LEU A 222 ? 1.1251 0.6293 0.7978 -0.2107 -0.0253 0.0052 222 LEU A C 1740 O O . LEU A 222 ? 1.1105 0.6126 0.7799 -0.2143 -0.0354 0.0067 222 LEU A O 1741 C CB . LEU A 222 ? 1.0828 0.5960 0.7140 -0.2125 -0.0115 -0.0049 222 LEU A CB 1742 C CG . LEU A 222 ? 1.1104 0.6128 0.7508 -0.2079 -0.0079 -0.0232 222 LEU A CG 1743 C CD1 . LEU A 222 ? 1.0510 0.5571 0.7166 -0.2007 0.0047 -0.0250 222 LEU A CD1 1744 C CD2 . LEU A 222 ? 1.2051 0.7043 0.8176 -0.2107 -0.0046 -0.0408 222 LEU A CD2 1745 N N . GLY A 223 ? 1.0898 0.5903 0.7815 -0.2070 -0.0222 0.0017 223 GLY A N 1746 C CA . GLY A 223 ? 0.9564 0.4484 0.6603 -0.2082 -0.0309 0.0008 223 GLY A CA 1747 C C . GLY A 223 ? 1.0646 0.5608 0.7801 -0.2111 -0.0347 0.0103 223 GLY A C 1748 O O . GLY A 223 ? 1.2013 0.6939 0.9211 -0.2149 -0.0414 0.0115 223 GLY A O 1749 N N . TYR A 224 ? 1.1297 0.6336 0.8496 -0.2106 -0.0295 0.0166 224 TYR A N 1750 C CA . TYR A 224 ? 0.9085 0.4149 0.6401 -0.2136 -0.0318 0.0220 224 TYR A CA 1751 C C . TYR A 224 ? 0.8834 0.3893 0.6274 -0.2149 -0.0348 0.0214 224 TYR A C 1752 O O . TYR A 224 ? 0.9149 0.4208 0.6611 -0.2200 -0.0396 0.0220 224 TYR A O 1753 C CB . TYR A 224 ? 1.0095 0.5214 0.7466 -0.2134 -0.0260 0.0288 224 TYR A CB 1754 C CG . TYR A 224 ? 1.1104 0.6215 0.8592 -0.2167 -0.0282 0.0318 224 TYR A CG 1755 C CD1 . TYR A 224 ? 0.9095 0.4211 0.6705 -0.2201 -0.0295 0.0294 224 TYR A CD1 1756 C CD2 . TYR A 224 ? 1.1258 0.6358 0.8755 -0.2165 -0.0297 0.0365 224 TYR A CD2 1757 C CE1 . TYR A 224 ? 0.8989 0.4082 0.6695 -0.2238 -0.0303 0.0276 224 TYR A CE1 1758 C CE2 . TYR A 224 ? 0.8827 0.3899 0.6483 -0.2182 -0.0302 0.0362 224 TYR A CE2 1759 C CZ . TYR A 224 ? 0.9816 0.4877 0.7562 -0.2221 -0.0294 0.0299 224 TYR A CZ 1760 O OH . TYR A 224 ? 0.8805 0.3823 0.6700 -0.2245 -0.0288 0.0254 224 TYR A OH 1761 N N . SER A 225 ? 1.0453 0.5520 0.7978 -0.2105 -0.0320 0.0200 225 SER A N 1762 C CA . SER A 225 ? 1.1428 0.6499 0.9112 -0.2109 -0.0380 0.0224 225 SER A CA 1763 C C . SER A 225 ? 1.1893 0.6917 0.9672 -0.2037 -0.0361 0.0179 225 SER A C 1764 O O . SER A 225 ? 1.1532 0.6562 0.9264 -0.1987 -0.0263 0.0110 225 SER A O 1765 C CB . SER A 225 ? 1.2187 0.7360 1.0037 -0.2126 -0.0367 0.0270 225 SER A CB 1766 O OG . SER A 225 ? 1.0884 0.6130 0.8807 -0.2080 -0.0253 0.0267 225 SER A OG 1767 N N . VAL A 226 ? 1.0709 0.5684 0.8622 -0.2037 -0.0455 0.0217 226 VAL A N 1768 C CA . VAL A 226 ? 0.9171 0.4069 0.7252 -0.1955 -0.0445 0.0168 226 VAL A CA 1769 C C . VAL A 226 ? 0.9137 0.4067 0.7530 -0.1926 -0.0535 0.0257 226 VAL A C 1770 O O . VAL A 226 ? 1.0996 0.5970 0.9395 -0.2002 -0.0655 0.0372 226 VAL A O 1771 C CB . VAL A 226 ? 1.0742 0.5470 0.8705 -0.1975 -0.0500 0.0127 226 VAL A CB 1772 C CG1 . VAL A 226 ? 1.0939 0.5650 0.8643 -0.1992 -0.0428 0.0029 226 VAL A CG1 1773 C CG2 . VAL A 226 ? 0.9201 0.3891 0.7104 -0.2074 -0.0635 0.0246 226 VAL A CG2 1774 N N . ALA A 227 ? 0.9419 0.4336 0.8080 -0.1819 -0.0477 0.0196 227 ALA A N 1775 C CA . ALA A 227 ? 1.0166 0.5123 0.9219 -0.1765 -0.0570 0.0288 227 ALA A CA 1776 C C . ALA A 227 ? 1.0663 0.5507 0.9989 -0.1637 -0.0507 0.0178 227 ALA A C 1777 O O . ALA A 227 ? 1.3404 0.8187 1.2588 -0.1596 -0.0357 0.0002 227 ALA A O 1778 C CB . ALA A 227 ? 1.1516 0.6700 1.0774 -0.1758 -0.0530 0.0332 227 ALA A CB 1779 N N . VAL A 228 ? 0.9660 0.4470 0.9382 -0.1577 -0.0627 0.0275 228 VAL A N 1780 C CA . VAL A 228 ? 0.9937 0.4603 0.9991 -0.1443 -0.0573 0.0157 228 VAL A CA 1781 C C . VAL A 228 ? 1.1674 0.6477 1.2317 -0.1313 -0.0570 0.0193 228 VAL A C 1782 O O . VAL A 228 ? 1.2982 0.7939 1.3823 -0.1346 -0.0717 0.0387 228 VAL A O 1783 C CB . VAL A 228 ? 0.9941 0.4336 0.9992 -0.1478 -0.0741 0.0238 228 VAL A CB 1784 C CG1 . VAL A 228 ? 0.9918 0.4180 0.9483 -0.1580 -0.0702 0.0145 228 VAL A CG1 1785 C CG2 . VAL A 228 ? 1.2897 0.7330 1.3023 -0.1567 -0.0984 0.0524 228 VAL A CG2 1786 N N . GLY A 229 ? 1.0897 0.5652 1.1829 -0.1168 -0.0400 -0.0011 229 GLY A N 1787 C CA . GLY A 229 ? 1.0552 0.5453 1.2121 -0.1016 -0.0349 -0.0024 229 GLY A CA 1788 C C . GLY A 229 ? 1.0815 0.5627 1.2557 -0.0874 -0.0101 -0.0332 229 GLY A C 1789 O O . GLY A 229 ? 1.1146 0.5807 1.2447 -0.0919 0.0012 -0.0518 229 GLY A O 1790 N N . ASP A 230 ? 1.1101 0.6021 1.3484 -0.0708 -0.0012 -0.0400 230 ASP A N 1791 C CA . ASP A 230 ? 1.1695 0.6499 1.4303 -0.0561 0.0226 -0.0726 230 ASP A CA 1792 C C . ASP A 230 ? 1.2545 0.7580 1.4910 -0.0554 0.0575 -0.0988 230 ASP A C 1793 O O . ASP A 230 ? 1.3983 0.8890 1.5843 -0.0610 0.0715 -0.1207 230 ASP A O 1794 C CB . ASP A 230 ? 1.1466 0.6274 1.4941 -0.0366 0.0186 -0.0708 230 ASP A CB 1795 C CG . ASP A 230 ? 1.2346 0.6833 1.6067 -0.0233 0.0288 -0.0986 230 ASP A CG 1796 O OD1 . ASP A 230 ? 1.2030 0.6319 1.5209 -0.0307 0.0400 -0.1211 230 ASP A OD1 1797 O OD2 . ASP A 230 ? 1.2628 0.7062 1.7111 -0.0057 0.0250 -0.0985 230 ASP A OD2 1798 N N . PHE A 231 ? 1.2303 0.7689 1.5038 -0.0498 0.0708 -0.0956 231 PHE A N 1799 C CA . PHE A 231 ? 1.4093 0.9752 1.6625 -0.0513 0.1047 -0.1152 231 PHE A CA 1800 C C . PHE A 231 ? 1.4180 0.9790 1.6841 -0.0382 0.1360 -0.1542 231 PHE A C 1801 O O . PHE A 231 ? 1.5156 1.1012 1.7660 -0.0394 0.1672 -0.1725 231 PHE A O 1802 C CB . PHE A 231 ? 1.2697 0.8354 1.4410 -0.0708 0.1049 -0.1100 231 PHE A CB 1803 C CG . PHE A 231 ? 1.2270 0.7925 1.3808 -0.0839 0.0760 -0.0777 231 PHE A CG 1804 C CD1 . PHE A 231 ? 1.3580 0.9523 1.5377 -0.0875 0.0719 -0.0580 231 PHE A CD1 1805 C CD2 . PHE A 231 ? 1.2117 0.7494 1.3248 -0.0933 0.0539 -0.0687 231 PHE A CD2 1806 C CE1 . PHE A 231 ? 1.4303 1.0234 1.5920 -0.1003 0.0463 -0.0324 231 PHE A CE1 1807 C CE2 . PHE A 231 ? 1.2557 0.7946 1.3519 -0.1055 0.0304 -0.0425 231 PHE A CE2 1808 C CZ . PHE A 231 ? 1.4562 1.0217 1.5748 -0.1090 0.0267 -0.0256 231 PHE A CZ 1809 N N . ASN A 232 ? 1.3569 0.8856 1.6504 -0.0271 0.1281 -0.1674 232 ASN A N 1810 C CA . ASN A 232 ? 1.5630 1.0855 1.8874 -0.0114 0.1566 -0.2067 232 ASN A CA 1811 C C . ASN A 232 ? 1.4641 0.9586 1.8619 0.0061 0.1397 -0.2063 232 ASN A C 1812 O O . ASN A 232 ? 1.6434 1.1185 2.0500 0.0021 0.1049 -0.1761 232 ASN A O 1813 C CB . ASN A 232 ? 1.5283 1.0317 1.7789 -0.0213 0.1726 -0.2377 232 ASN A CB 1814 C CG . ASN A 232 ? 1.3466 0.8112 1.5540 -0.0330 0.1429 -0.2273 232 ASN A CG 1815 O OD1 . ASN A 232 ? 1.3982 0.8490 1.6276 -0.0341 0.1121 -0.1972 232 ASN A OD1 1816 N ND2 . ASN A 232 ? 1.3042 0.7530 1.4492 -0.0432 0.1522 -0.2519 232 ASN A ND2 1817 N N . GLY A 233 ? 1.3006 0.7931 1.7521 0.0250 0.1647 -0.2396 233 GLY A N 1818 C CA . GLY A 233 ? 1.3583 0.8289 1.8972 0.0450 0.1504 -0.2373 233 GLY A CA 1819 C C . GLY A 233 ? 1.7241 1.1418 2.2552 0.0429 0.1245 -0.2357 233 GLY A C 1820 O O . GLY A 233 ? 2.0139 1.4091 2.6198 0.0592 0.1113 -0.2321 233 GLY A O 1821 N N . ASP A 234 ? 1.6034 1.0014 2.0496 0.0229 0.1165 -0.2367 234 ASP A N 1822 C CA . ASP A 234 ? 1.3506 0.6992 1.7859 0.0185 0.0959 -0.2394 234 ASP A CA 1823 C C . ASP A 234 ? 1.2706 0.6009 1.7492 0.0191 0.0559 -0.1956 234 ASP A C 1824 O O . ASP A 234 ? 1.5441 0.8357 2.0638 0.0264 0.0419 -0.1973 234 ASP A O 1825 C CB . ASP A 234 ? 1.3562 0.6949 1.6937 -0.0049 0.0934 -0.2446 234 ASP A CB 1826 C CG . ASP A 234 ? 1.7556 1.1213 2.0421 -0.0222 0.0786 -0.2083 234 ASP A CG 1827 O OD1 . ASP A 234 ? 1.8585 1.2381 2.1796 -0.0202 0.0590 -0.1731 234 ASP A OD1 1828 O OD2 . ASP A 234 ? 1.8410 1.2135 2.0533 -0.0382 0.0856 -0.2156 234 ASP A OD2 1829 N N . GLY A 235 ? 1.2347 0.5925 1.7032 0.0101 0.0373 -0.1564 235 GLY A N 1830 C CA . GLY A 235 ? 1.2146 0.5606 1.7144 0.0073 -0.0010 -0.1127 235 GLY A CA 1831 C C . GLY A 235 ? 1.3311 0.6654 1.7580 -0.0170 -0.0245 -0.0872 235 GLY A C 1832 O O . GLY A 235 ? 1.5277 0.8629 1.9617 -0.0248 -0.0544 -0.0479 235 GLY A O 1833 N N . ILE A 236 ? 1.3507 0.6763 1.7077 -0.0297 -0.0108 -0.1096 236 ILE A N 1834 C CA . ILE A 236 ? 1.4041 0.7209 1.6948 -0.0520 -0.0295 -0.0894 236 ILE A CA 1835 C C . ILE A 236 ? 1.3018 0.6550 1.5388 -0.0645 -0.0241 -0.0788 236 ILE A C 1836 O O . ILE A 236 ? 1.2228 0.5994 1.4444 -0.0610 0.0013 -0.1001 236 ILE A O 1837 C CB . ILE A 236 ? 1.3979 0.6843 1.6463 -0.0604 -0.0224 -0.1168 236 ILE A CB 1838 C CG1 . ILE A 236 ? 1.5050 0.7539 1.8099 -0.0465 -0.0214 -0.1373 236 ILE A CG1 1839 C CG2 . ILE A 236 ? 1.4022 0.6779 1.5994 -0.0820 -0.0447 -0.0921 236 ILE A CG2 1840 C CD1 . ILE A 236 ? 1.7586 0.9758 2.0258 -0.0558 -0.0158 -0.1670 236 ILE A CD1 1841 N N . ASP A 237 ? 1.3601 0.7173 1.5693 -0.0797 -0.0475 -0.0461 237 ASP A N 1842 C CA . ASP A 237 ? 1.2734 0.6593 1.4320 -0.0927 -0.0448 -0.0361 237 ASP A CA 1843 C C . ASP A 237 ? 1.3375 0.7235 1.4369 -0.1005 -0.0256 -0.0610 237 ASP A C 1844 O O . ASP A 237 ? 1.3323 0.6934 1.4063 -0.1069 -0.0281 -0.0721 237 ASP A O 1845 C CB . ASP A 237 ? 1.2590 0.6435 1.3943 -0.1088 -0.0719 -0.0021 237 ASP A CB 1846 C CG . ASP A 237 ? 1.5545 0.9526 1.7349 -0.1053 -0.0915 0.0267 237 ASP A CG 1847 O OD1 . ASP A 237 ? 1.7271 1.1255 1.9698 -0.0886 -0.0901 0.0238 237 ASP A OD1 1848 O OD2 . ASP A 237 ? 1.6161 1.0256 1.7708 -0.1195 -0.1087 0.0514 237 ASP A OD2 1849 N N . ASP A 238 ? 1.3730 0.7878 1.4526 -0.1010 -0.0076 -0.0683 238 ASP A N 1850 C CA . ASP A 238 ? 1.1936 0.6126 1.2185 -0.1083 0.0101 -0.0889 238 ASP A CA 1851 C C . ASP A 238 ? 1.2036 0.6393 1.1837 -0.1231 0.0029 -0.0698 238 ASP A C 1852 O O . ASP A 238 ? 1.3465 0.7902 1.3367 -0.1275 -0.0133 -0.0450 238 ASP A O 1853 C CB . ASP A 238 ? 1.2175 0.6551 1.2543 -0.0978 0.0395 -0.1140 238 ASP A CB 1854 C CG . ASP A 238 ? 1.6121 1.0378 1.7091 -0.0799 0.0479 -0.1321 238 ASP A CG 1855 O OD1 . ASP A 238 ? 2.0582 1.4718 2.2026 -0.0736 0.0284 -0.1144 238 ASP A OD1 1856 O OD2 . ASP A 238 ? 1.5393 0.9680 1.6376 -0.0724 0.0737 -0.1637 238 ASP A OD2 1857 N N . PHE A 239 ? 1.1747 0.6157 1.1061 -0.1309 0.0144 -0.0817 239 PHE A N 1858 C CA . PHE A 239 ? 1.1418 0.5911 1.0326 -0.1447 0.0053 -0.0652 239 PHE A CA 1859 C C . PHE A 239 ? 1.1139 0.5907 0.9937 -0.1468 0.0176 -0.0596 239 PHE A C 1860 O O . PHE A 239 ? 1.2168 0.7054 1.0865 -0.1441 0.0376 -0.0745 239 PHE A O 1861 C CB . PHE A 239 ? 1.2503 0.6854 1.0972 -0.1538 0.0034 -0.0763 239 PHE A CB 1862 C CG . PHE A 239 ? 1.1791 0.5858 1.0371 -0.1540 -0.0084 -0.0824 239 PHE A CG 1863 C CD1 . PHE A 239 ? 1.0783 0.4737 0.9680 -0.1531 -0.0254 -0.0643 239 PHE A CD1 1864 C CD2 . PHE A 239 ? 1.1960 0.5872 1.0328 -0.1567 -0.0037 -0.1054 239 PHE A CD2 1865 C CE1 . PHE A 239 ? 1.2234 0.5912 1.1259 -0.1547 -0.0367 -0.0668 239 PHE A CE1 1866 C CE2 . PHE A 239 ? 1.4021 0.7650 1.2528 -0.1582 -0.0152 -0.1111 239 PHE A CE2 1867 C CZ . PHE A 239 ? 1.5480 0.8986 1.4332 -0.1570 -0.0313 -0.0908 239 PHE A CZ 1868 N N . VAL A 240 ? 1.0759 0.5627 0.9571 -0.1531 0.0056 -0.0381 240 VAL A N 1869 C CA . VAL A 240 ? 1.0379 0.5472 0.9106 -0.1575 0.0138 -0.0301 240 VAL A CA 1870 C C . VAL A 240 ? 1.2134 0.7204 1.0513 -0.1695 0.0030 -0.0183 240 VAL A C 1871 O O . VAL A 240 ? 1.1074 0.6061 0.9455 -0.1745 -0.0135 -0.0076 240 VAL A O 1872 C CB . VAL A 240 ? 1.0005 0.5263 0.9162 -0.1537 0.0104 -0.0177 240 VAL A CB 1873 C CG1 . VAL A 240 ? 0.9882 0.5341 0.8957 -0.1610 0.0166 -0.0083 240 VAL A CG1 1874 C CG2 . VAL A 240 ? 1.2011 0.7334 1.1595 -0.1401 0.0235 -0.0297 240 VAL A CG2 1875 N N . SER A 241 ? 1.1105 0.6258 0.9198 -0.1744 0.0128 -0.0198 241 SER A N 1876 C CA . SER A 241 ? 1.0283 0.5415 0.8111 -0.1838 0.0037 -0.0097 241 SER A CA 1877 C C . SER A 241 ? 1.1355 0.6638 0.9103 -0.1882 0.0124 -0.0016 241 SER A C 1878 O O . SER A 241 ? 1.0729 0.6112 0.8404 -0.1869 0.0275 -0.0063 241 SER A O 1879 C CB . SER A 241 ? 1.0991 0.5997 0.8515 -0.1872 -0.0001 -0.0177 241 SER A CB 1880 O OG . SER A 241 ? 1.3313 0.8325 1.0653 -0.1947 -0.0081 -0.0079 241 SER A OG 1881 N N . GLY A 242 ? 1.1908 0.7201 0.9669 -0.1942 0.0034 0.0103 242 GLY A N 1882 C CA . GLY A 242 ? 1.3250 0.8635 1.0964 -0.1993 0.0088 0.0198 242 GLY A CA 1883 C C . GLY A 242 ? 1.2944 0.8286 1.0351 -0.2030 0.0084 0.0218 242 GLY A C 1884 O O . GLY A 242 ? 1.4108 0.9349 1.1382 -0.2039 -0.0014 0.0188 242 GLY A O 1885 N N . VAL A 243 ? 1.0704 0.6140 0.8015 -0.2060 0.0181 0.0287 243 VAL A N 1886 C CA . VAL A 243 ? 1.1362 0.6778 0.8399 -0.2105 0.0150 0.0355 243 VAL A CA 1887 C C . VAL A 243 ? 1.0299 0.5762 0.7417 -0.2158 0.0161 0.0531 243 VAL A C 1888 O O . VAL A 243 ? 1.0266 0.5831 0.7284 -0.2198 0.0265 0.0617 243 VAL A O 1889 C CB . VAL A 243 ? 1.2194 0.7670 0.8937 -0.2111 0.0247 0.0279 243 VAL A CB 1890 C CG1 . VAL A 243 ? 1.3034 0.8459 0.9486 -0.2155 0.0133 0.0313 243 VAL A CG1 1891 C CG2 . VAL A 243 ? 1.0727 0.6170 0.7522 -0.2045 0.0304 0.0080 243 VAL A CG2 1892 N N . PRO A 244 ? 0.9765 0.5149 0.7065 -0.2169 0.0062 0.0582 244 PRO A N 1893 C CA . PRO A 244 ? 1.0608 0.5991 0.8096 -0.2216 0.0065 0.0716 244 PRO A CA 1894 C C . PRO A 244 ? 1.0223 0.5614 0.7591 -0.2261 0.0067 0.0891 244 PRO A C 1895 O O . PRO A 244 ? 1.4554 0.9981 1.2052 -0.2314 0.0123 0.1022 244 PRO A O 1896 C CB . PRO A 244 ? 1.0125 0.5394 0.7764 -0.2210 -0.0048 0.0668 244 PRO A CB 1897 C CG . PRO A 244 ? 1.1200 0.6427 0.8675 -0.2173 -0.0114 0.0572 244 PRO A CG 1898 C CD . PRO A 244 ? 0.9173 0.4458 0.6510 -0.2145 -0.0051 0.0495 244 PRO A CD 1899 N N . ARG A 245 ? 0.9976 0.5340 0.7121 -0.2253 -0.0009 0.0913 245 ARG A N 1900 C CA . ARG A 245 ? 1.0419 0.5796 0.7450 -0.2302 -0.0047 0.1116 245 ARG A CA 1901 C C . ARG A 245 ? 1.0899 0.6409 0.7575 -0.2352 0.0042 0.1157 245 ARG A C 1902 O O . ARG A 245 ? 1.2399 0.7948 0.8906 -0.2415 0.0006 0.1351 245 ARG A O 1903 C CB . ARG A 245 ? 1.1574 0.6875 0.8609 -0.2275 -0.0207 0.1148 245 ARG A CB 1904 C CG . ARG A 245 ? 1.2089 0.7271 0.9483 -0.2245 -0.0274 0.1164 245 ARG A CG 1905 C CD . ARG A 245 ? 1.0776 0.5923 0.8229 -0.2216 -0.0415 0.1239 245 ARG A CD 1906 N NE . ARG A 245 ? 1.2632 0.7831 0.9927 -0.2261 -0.0482 0.1471 245 ARG A NE 1907 C CZ . ARG A 245 ? 1.0802 0.5940 0.8293 -0.2281 -0.0532 0.1696 245 ARG A CZ 1908 N NH1 . ARG A 245 ? 1.0049 0.5058 0.7925 -0.2253 -0.0513 0.1682 245 ARG A NH1 1909 N NH2 . ARG A 245 ? 1.3682 0.8883 1.0983 -0.2338 -0.0611 0.1937 245 ARG A NH2 1910 N N . ALA A 246 ? 1.1491 0.7072 0.8057 -0.2327 0.0157 0.0973 246 ALA A N 1911 C CA . ALA A 246 ? 1.3919 0.9630 1.0127 -0.2372 0.0273 0.0942 246 ALA A CA 1912 C C . ALA A 246 ? 1.2778 0.8623 0.8955 -0.2456 0.0410 0.1125 246 ALA A C 1913 O O . ALA A 246 ? 1.3806 0.9649 1.0309 -0.2465 0.0450 0.1220 246 ALA A O 1914 C CB . ALA A 246 ? 1.4594 1.0331 1.0795 -0.2309 0.0386 0.0683 246 ALA A CB 1915 N N . ALA A 247 ? 1.2799 0.8767 0.8565 -0.2535 0.0480 0.1174 247 ALA A N 1916 C CA . ALA A 247 ? 1.2997 0.9130 0.8650 -0.2642 0.0636 0.1359 247 ALA A CA 1917 C C . ALA A 247 ? 1.4006 1.0068 0.9916 -0.2696 0.0540 0.1665 247 ALA A C 1918 O O . ALA A 247 ? 1.2658 0.8753 0.8894 -0.2714 0.0641 0.1730 247 ALA A O 1919 C CB . ALA A 247 ? 1.1880 0.8160 0.7716 -0.2616 0.0885 0.1204 247 ALA A CB 1920 N N . ARG A 248 ? 1.6525 1.2487 1.2330 -0.2721 0.0334 0.1847 248 ARG A N 1921 C CA . ARG A 248 ? 1.4497 1.0359 1.0565 -0.2767 0.0225 0.2151 248 ARG A CA 1922 C C . ARG A 248 ? 1.2382 0.8100 0.8987 -0.2695 0.0214 0.2076 248 ARG A C 1923 O O . ARG A 248 ? 1.3895 0.9577 1.0779 -0.2753 0.0245 0.2251 248 ARG A O 1924 C CB . ARG A 248 ? 1.4308 1.0320 1.0203 -0.2916 0.0353 0.2417 248 ARG A CB 1925 C CG . ARG A 248 ? 1.5902 1.2095 1.1182 -0.3014 0.0396 0.2459 248 ARG A CG 1926 C CD . ARG A 248 ? 1.9931 1.6342 1.5004 -0.3161 0.0628 0.2615 248 ARG A CD 1927 N NE . ARG A 248 ? 2.3262 1.9863 1.7680 -0.3273 0.0684 0.2627 248 ARG A NE 1928 C CZ . ARG A 248 ? 2.4330 2.1161 1.8419 -0.3431 0.0889 0.2772 248 ARG A CZ 1929 N NH1 . ARG A 248 ? 2.4310 2.1214 1.8714 -0.3493 0.1055 0.2936 248 ARG A NH1 1930 N NH2 . ARG A 248 ? 2.3729 2.0732 1.7165 -0.3543 0.0932 0.2749 248 ARG A NH2 1931 N N . THR A 249 ? 1.3509 0.9147 1.0234 -0.2585 0.0167 0.1816 249 THR A N 1932 C CA . THR A 249 ? 1.1797 0.7311 0.8948 -0.2523 0.0142 0.1699 249 THR A CA 1933 C C . THR A 249 ? 1.0942 0.6545 0.8319 -0.2560 0.0298 0.1668 249 THR A C 1934 O O . THR A 249 ? 1.0889 0.6398 0.8625 -0.2558 0.0265 0.1646 249 THR A O 1935 C CB . THR A 249 ? 1.0752 0.6083 0.8205 -0.2520 -0.0008 0.1853 249 THR A CB 1936 O OG1 . THR A 249 ? 1.0786 0.6116 0.8330 -0.2619 0.0020 0.2130 249 THR A OG1 1937 C CG2 . THR A 249 ? 1.4630 0.9903 1.1955 -0.2472 -0.0172 0.1890 249 THR A CG2 1938 N N . LEU A 250 ? 1.1031 0.6831 0.8213 -0.2598 0.0471 0.1647 250 LEU A N 1939 C CA . LEU A 250 ? 1.1026 0.6959 0.8469 -0.2613 0.0626 0.1576 250 LEU A CA 1940 C C . LEU A 250 ? 1.2203 0.8106 0.9800 -0.2505 0.0594 0.1313 250 LEU A C 1941 O O . LEU A 250 ? 1.0869 0.6804 0.8807 -0.2500 0.0612 0.1257 250 LEU A O 1942 C CB . LEU A 250 ? 1.1579 0.7761 0.8798 -0.2672 0.0850 0.1600 250 LEU A CB 1943 C CG . LEU A 250 ? 1.3635 0.9940 1.0892 -0.2816 0.0965 0.1873 250 LEU A CG 1944 C CD1 . LEU A 250 ? 1.5948 1.2196 1.2841 -0.2898 0.0876 0.2116 250 LEU A CD1 1945 C CD2 . LEU A 250 ? 1.2732 0.9334 0.9954 -0.2855 0.1240 0.1806 250 LEU A CD2 1946 N N . GLY A 251 ? 1.1743 0.7586 0.9086 -0.2431 0.0531 0.1170 251 GLY A N 1947 C CA . GLY A 251 ? 1.0016 0.5815 0.7463 -0.2338 0.0488 0.0951 251 GLY A CA 1948 C C . GLY A 251 ? 1.1571 0.7519 0.8949 -0.2295 0.0648 0.0802 251 GLY A C 1949 O O . GLY A 251 ? 1.1026 0.7154 0.8451 -0.2336 0.0823 0.0847 251 GLY A O 1950 N N . MET A 252 ? 1.2753 0.8628 1.0055 -0.2214 0.0599 0.0619 252 MET A N 1951 C CA . MET A 252 ? 1.1271 0.7245 0.8556 -0.2154 0.0744 0.0442 252 MET A CA 1952 C C . MET A 252 ? 1.1177 0.7041 0.8654 -0.2061 0.0648 0.0289 252 MET A C 1953 O O . MET A 252 ? 1.0386 0.6096 0.7853 -0.2057 0.0474 0.0302 252 MET A O 1954 C CB . MET A 252 ? 1.1031 0.7022 0.7866 -0.2179 0.0812 0.0371 252 MET A CB 1955 C CG . MET A 252 ? 1.1698 0.7848 0.8293 -0.2283 0.0946 0.0521 252 MET A CG 1956 S SD . MET A 252 ? 1.3057 0.9293 0.9110 -0.2321 0.1081 0.0365 252 MET A SD 1957 C CE . MET A 252 ? 1.2829 0.9195 0.9156 -0.2219 0.1331 0.0087 252 MET A CE 1958 N N . VAL A 253 ? 1.2000 0.7953 0.9676 -0.1988 0.0768 0.0154 253 VAL A N 1959 C CA . VAL A 253 ? 1.1842 0.7677 0.9694 -0.1898 0.0676 0.0023 253 VAL A CA 1960 C C . VAL A 253 ? 1.2905 0.8736 1.0654 -0.1831 0.0812 -0.0186 253 VAL A C 1961 O O . VAL A 253 ? 1.3949 0.9951 1.1810 -0.1801 0.1020 -0.0267 253 VAL A O 1962 C CB . VAL A 253 ? 1.0263 0.6178 0.8594 -0.1857 0.0638 0.0066 253 VAL A CB 1963 C CG1 . VAL A 253 ? 1.0425 0.6254 0.8975 -0.1753 0.0585 -0.0058 253 VAL A CG1 1964 C CG2 . VAL A 253 ? 0.9828 0.5678 0.8211 -0.1927 0.0457 0.0211 253 VAL A CG2 1965 N N . TYR A 254 ? 1.1091 0.6731 0.8639 -0.1816 0.0703 -0.0288 254 TYR A N 1966 C CA . TYR A 254 ? 1.1888 0.7469 0.9329 -0.1762 0.0807 -0.0521 254 TYR A CA 1967 C C . TYR A 254 ? 1.2484 0.7957 1.0339 -0.1649 0.0764 -0.0623 254 TYR A C 1968 O O . TYR A 254 ? 1.1453 0.6814 0.9486 -0.1643 0.0575 -0.0514 254 TYR A O 1969 C CB . TYR A 254 ? 1.1492 0.6920 0.8496 -0.1827 0.0700 -0.0578 254 TYR A CB 1970 C CG . TYR A 254 ? 1.2074 0.7604 0.8669 -0.1937 0.0717 -0.0465 254 TYR A CG 1971 C CD1 . TYR A 254 ? 1.3707 0.9447 1.0256 -0.1976 0.0889 -0.0382 254 TYR A CD1 1972 C CD2 . TYR A 254 ? 1.2492 0.7920 0.8777 -0.2009 0.0552 -0.0419 254 TYR A CD2 1973 C CE1 . TYR A 254 ? 1.3213 0.9035 0.9392 -0.2086 0.0883 -0.0237 254 TYR A CE1 1974 C CE2 . TYR A 254 ? 1.4178 0.9701 1.0127 -0.2105 0.0536 -0.0283 254 TYR A CE2 1975 C CZ . TYR A 254 ? 1.3214 0.8922 0.9099 -0.2145 0.0696 -0.0182 254 TYR A CZ 1976 O OH . TYR A 254 ? 1.3035 0.8827 0.8591 -0.2251 0.0660 -0.0005 254 TYR A OH 1977 N N . ILE A 255 ? 1.3308 0.8819 1.1324 -0.1562 0.0942 -0.0830 255 ILE A N 1978 C CA . ILE A 255 ? 1.2392 0.7759 1.0819 -0.1443 0.0892 -0.0938 255 ILE A CA 1979 C C . ILE A 255 ? 1.3112 0.8297 1.1354 -0.1415 0.0958 -0.1212 255 ILE A C 1980 O O . ILE A 255 ? 1.4166 0.9448 1.2297 -0.1393 0.1190 -0.1427 255 ILE A O 1981 C CB . ILE A 255 ? 1.1575 0.7134 1.0557 -0.1331 0.1030 -0.0953 255 ILE A CB 1982 C CG1 . ILE A 255 ? 1.1195 0.6898 1.0421 -0.1369 0.0905 -0.0685 255 ILE A CG1 1983 C CG2 . ILE A 255 ? 1.1623 0.7013 1.1052 -0.1194 0.0988 -0.1083 255 ILE A CG2 1984 C CD1 . ILE A 255 ? 1.1245 0.7136 1.1104 -0.1264 0.0966 -0.0662 255 ILE A CD1 1985 N N . TYR A 256 ? 1.3247 0.8170 1.1448 -0.1430 0.0759 -0.1213 256 TYR A N 1986 C CA . TYR A 256 ? 1.4718 0.9425 1.2773 -0.1421 0.0782 -0.1475 256 TYR A CA 1987 C C . TYR A 256 ? 1.3162 0.7685 1.1755 -0.1286 0.0764 -0.1584 256 TYR A C 1988 O O . TYR A 256 ? 1.2085 0.6574 1.1067 -0.1239 0.0613 -0.1382 256 TYR A O 1989 C CB . TYR A 256 ? 1.3759 0.8293 1.1443 -0.1544 0.0573 -0.1410 256 TYR A CB 1990 C CG . TYR A 256 ? 1.4287 0.8970 1.1454 -0.1670 0.0576 -0.1334 256 TYR A CG 1991 C CD1 . TYR A 256 ? 1.3492 0.8187 1.0230 -0.1737 0.0670 -0.1536 256 TYR A CD1 1992 C CD2 . TYR A 256 ? 1.2599 0.7401 0.9712 -0.1727 0.0473 -0.1061 256 TYR A CD2 1993 C CE1 . TYR A 256 ? 1.4008 0.8843 1.0291 -0.1857 0.0639 -0.1424 256 TYR A CE1 1994 C CE2 . TYR A 256 ? 1.1422 0.6341 0.8132 -0.1831 0.0459 -0.0969 256 TYR A CE2 1995 C CZ . TYR A 256 ? 1.2664 0.7604 0.8966 -0.1895 0.0531 -0.1130 256 TYR A CZ 1996 O OH . TYR A 256 ? 1.4004 0.9067 0.9922 -0.2003 0.0486 -0.0998 256 TYR A OH 1997 N N . ASP A 257 ? 1.2316 0.6719 1.0929 -0.1227 0.0913 -0.1904 257 ASP A N 1998 C CA . ASP A 257 ? 1.3501 0.7667 1.2645 -0.1095 0.0889 -0.2038 257 ASP A CA 1999 C C . ASP A 257 ? 1.3451 0.7319 1.2611 -0.1159 0.0600 -0.1891 257 ASP A C 2000 O O . ASP A 257 ? 1.4801 0.8551 1.3521 -0.1288 0.0510 -0.1934 257 ASP A O 2001 C CB . ASP A 257 ? 1.5416 0.9487 1.4514 -0.1039 0.1120 -0.2462 257 ASP A CB 2002 C CG . ASP A 257 ? 1.4708 0.8583 1.4500 -0.0857 0.1163 -0.2624 257 ASP A CG 2003 O OD1 . ASP A 257 ? 1.4253 0.7909 1.4426 -0.0821 0.0926 -0.2432 257 ASP A OD1 2004 O OD2 . ASP A 257 ? 1.6672 1.0621 1.6643 -0.0750 0.1440 -0.2940 257 ASP A OD2 2005 N N . GLY A 258 ? 1.2063 0.5830 1.1740 -0.1080 0.0448 -0.1703 258 GLY A N 2006 C CA . GLY A 258 ? 1.2186 0.5701 1.1892 -0.1156 0.0182 -0.1517 258 GLY A CA 2007 C C . GLY A 258 ? 1.3412 0.6566 1.3216 -0.1148 0.0150 -0.1747 258 GLY A C 2008 O O . GLY A 258 ? 1.2740 0.5657 1.2650 -0.1210 -0.0062 -0.1597 258 GLY A O 2009 N N . LYS A 259 ? 1.3239 0.6352 1.3001 -0.1086 0.0368 -0.2119 259 LYS A N 2010 C CA . LYS A 259 ? 1.3566 0.6315 1.3444 -0.1077 0.0357 -0.2400 259 LYS A CA 2011 C C . LYS A 259 ? 1.4059 0.6771 1.3296 -0.1234 0.0394 -0.2636 259 LYS A C 2012 O O . LYS A 259 ? 1.4762 0.7282 1.3816 -0.1369 0.0200 -0.2569 259 LYS A O 2013 C CB . LYS A 259 ? 1.5215 0.7896 1.5611 -0.0879 0.0574 -0.2702 259 LYS A CB 2014 C CG . LYS A 259 ? 1.4494 0.6727 1.5291 -0.0825 0.0504 -0.2908 259 LYS A CG 2015 C CD . LYS A 259 ? 1.4796 0.6972 1.6289 -0.0590 0.0692 -0.3135 259 LYS A CD 2016 C CE . LYS A 259 ? 1.7779 0.9464 1.9769 -0.0526 0.0594 -0.3302 259 LYS A CE 2017 N NZ . LYS A 259 ? 1.8009 0.9629 2.0773 -0.0273 0.0779 -0.3532 259 LYS A NZ 2018 N N . ASN A 260 ? 1.5305 0.8214 1.4209 -0.1228 0.0638 -0.2904 260 ASN A N 2019 C CA . ASN A 260 ? 1.5209 0.8119 1.3464 -0.1391 0.0655 -0.3114 260 ASN A CA 2020 C C . ASN A 260 ? 1.3578 0.6814 1.1279 -0.1522 0.0619 -0.2880 260 ASN A C 2021 O O . ASN A 260 ? 1.4232 0.7526 1.1382 -0.1660 0.0622 -0.3011 260 ASN A O 2022 C CB . ASN A 260 ? 1.7905 1.0795 1.6049 -0.1340 0.0933 -0.3593 260 ASN A CB 2023 C CG . ASN A 260 ? 1.8258 1.1485 1.6480 -0.1223 0.1225 -0.3643 260 ASN A CG 2024 O OD1 . ASN A 260 ? 1.9232 1.2729 1.7507 -0.1205 0.1212 -0.3319 260 ASN A OD1 2025 N ND2 . ASN A 260 ? 1.8817 1.2033 1.7055 -0.1153 0.1504 -0.4072 260 ASN A ND2 2026 N N . MET A 261 ? 1.2903 0.6343 1.0772 -0.1481 0.0574 -0.2537 261 MET A N 2027 C CA . MET A 261 ? 1.3971 0.7682 1.1435 -0.1589 0.0518 -0.2278 261 MET A CA 2028 C C . MET A 261 ? 1.4378 0.8364 1.1422 -0.1622 0.0739 -0.2402 261 MET A C 2029 O O . MET A 261 ? 1.2840 0.6997 0.9449 -0.1740 0.0684 -0.2253 261 MET A O 2030 C CB . MET A 261 ? 1.5164 0.8765 1.2316 -0.1748 0.0283 -0.2174 261 MET A CB 2031 C CG . MET A 261 ? 1.3049 0.6873 0.9948 -0.1838 0.0172 -0.1859 261 MET A CG 2032 S SD . MET A 261 ? 1.4676 0.8614 1.1972 -0.1759 0.0118 -0.1513 261 MET A SD 2033 C CE . MET A 261 ? 1.1081 0.5042 0.8171 -0.1900 -0.0110 -0.1257 261 MET A CE 2034 N N . SER A 262 ? 1.4540 0.8580 1.1740 -0.1517 0.0994 -0.2662 262 SER A N 2035 C CA . SER A 262 ? 1.3794 0.8134 1.0632 -0.1552 0.1238 -0.2750 262 SER A CA 2036 C C . SER A 262 ? 1.3663 0.8283 1.0718 -0.1504 0.1292 -0.2445 262 SER A C 2037 O O . SER A 262 ? 1.3189 0.7771 1.0762 -0.1404 0.1202 -0.2267 262 SER A O 2038 C CB . SER A 262 ? 1.4917 0.9243 1.1847 -0.1465 0.1529 -0.3172 262 SER A CB 2039 O OG . SER A 262 ? 1.6610 1.0919 1.4252 -0.1272 0.1634 -0.3192 262 SER A OG 2040 N N . SER A 263 ? 1.4411 0.9310 1.1065 -0.1593 0.1422 -0.2372 263 SER A N 2041 C CA . SER A 263 ? 1.4587 0.9750 1.1438 -0.1570 0.1484 -0.2096 263 SER A CA 2042 C C . SER A 263 ? 1.4531 0.9839 1.1893 -0.1423 0.1742 -0.2233 263 SER A C 2043 O O . SER A 263 ? 1.5706 1.1030 1.3046 -0.1376 0.1978 -0.2565 263 SER A O 2044 C CB . SER A 263 ? 1.4919 1.0318 1.1213 -0.1720 0.1547 -0.1961 263 SER A CB 2045 O OG . SER A 263 ? 1.7029 1.2650 1.3538 -0.1715 0.1584 -0.1681 263 SER A OG 2046 N N . LEU A 264 ? 1.3736 0.9162 1.1576 -0.1352 0.1696 -0.1991 264 LEU A N 2047 C CA . LEU A 264 ? 1.4554 1.0161 1.2976 -0.1209 0.1911 -0.2077 264 LEU A CA 2048 C C . LEU A 264 ? 1.5720 1.1688 1.4165 -0.1262 0.2060 -0.1882 264 LEU A C 2049 O O . LEU A 264 ? 1.6567 1.2779 1.4909 -0.1275 0.2363 -0.2033 264 LEU A O 2050 C CB . LEU A 264 ? 1.3898 0.9349 1.2983 -0.1076 0.1717 -0.1967 264 LEU A CB 2051 C CG . LEU A 264 ? 1.4804 0.9903 1.4073 -0.0990 0.1616 -0.2172 264 LEU A CG 2052 C CD1 . LEU A 264 ? 1.4202 0.9198 1.4164 -0.0864 0.1430 -0.2003 264 LEU A CD1 2053 C CD2 . LEU A 264 ? 1.6599 1.1688 1.5888 -0.0913 0.1913 -0.2592 264 LEU A CD2 2054 N N . TYR A 265 ? 1.4049 1.0053 1.2627 -0.1304 0.1853 -0.1553 265 TYR A N 2055 C CA . TYR A 265 ? 1.4286 1.0599 1.2956 -0.1365 0.1956 -0.1344 265 TYR A CA 2056 C C . TYR A 265 ? 1.5150 1.1429 1.3396 -0.1519 0.1766 -0.1069 265 TYR A C 2057 O O . TYR A 265 ? 1.3564 0.9600 1.1557 -0.1557 0.1533 -0.1018 265 TYR A O 2058 C CB . TYR A 265 ? 1.4661 1.1093 1.4065 -0.1257 0.1909 -0.1224 265 TYR A CB 2059 C CG . TYR A 265 ? 1.7439 1.3953 1.7398 -0.1085 0.2109 -0.1467 265 TYR A CG 2060 C CD1 . TYR A 265 ? 1.8369 1.5218 1.8521 -0.1060 0.2450 -0.1590 265 TYR A CD1 2061 C CD2 . TYR A 265 ? 1.6818 1.3082 1.7151 -0.0949 0.1963 -0.1567 265 TYR A CD2 2062 C CE1 . TYR A 265 ? 1.8398 1.5338 1.9127 -0.0886 0.2654 -0.1834 265 TYR A CE1 2063 C CE2 . TYR A 265 ? 1.6427 1.2748 1.7346 -0.0774 0.2139 -0.1790 265 TYR A CE2 2064 C CZ . TYR A 265 ? 1.7745 1.4409 1.8876 -0.0734 0.2490 -0.1937 265 TYR A CZ 2065 O OH . TYR A 265 ? 1.9155 1.5891 2.0933 -0.0544 0.2685 -0.2179 265 TYR A OH 2066 N N . ASN A 266 ? 1.6399 1.2926 1.4609 -0.1607 0.1876 -0.0894 266 ASN A N 2067 C CA . ASN A 266 ? 1.3677 1.0175 1.1572 -0.1744 0.1713 -0.0626 266 ASN A CA 2068 C C . ASN A 266 ? 1.3236 0.9911 1.1506 -0.1782 0.1699 -0.0391 266 ASN A C 2069 O O . ASN A 266 ? 1.5124 1.2041 1.3795 -0.1742 0.1886 -0.0416 266 ASN A O 2070 C CB . ASN A 266 ? 1.4166 1.0741 1.1451 -0.1873 0.1836 -0.0622 266 ASN A CB 2071 C CG . ASN A 266 ? 1.4299 1.0640 1.1106 -0.1901 0.1692 -0.0733 266 ASN A CG 2072 O OD1 . ASN A 266 ? 1.2991 0.9101 0.9875 -0.1862 0.1456 -0.0717 266 ASN A OD1 2073 N ND2 . ASN A 266 ? 1.6975 1.3394 1.3276 -0.1986 0.1833 -0.0843 266 ASN A ND2 2074 N N . PHE A 267 ? 1.2732 0.9291 1.0898 -0.1862 0.1480 -0.0176 267 PHE A N 2075 C CA . PHE A 267 ? 1.2978 0.9667 1.1425 -0.1932 0.1447 0.0044 267 PHE A CA 2076 C C . PHE A 267 ? 1.2862 0.9478 1.0928 -0.2065 0.1364 0.0241 267 PHE A C 2077 O O . PHE A 267 ? 1.1498 0.7919 0.9196 -0.2080 0.1227 0.0235 267 PHE A O 2078 C CB . PHE A 267 ? 1.1856 0.8453 1.0718 -0.1879 0.1228 0.0093 267 PHE A CB 2079 C CG . PHE A 267 ? 1.1397 0.8086 1.0737 -0.1748 0.1278 -0.0039 267 PHE A CG 2080 C CD1 . PHE A 267 ? 1.2026 0.8995 1.1854 -0.1734 0.1411 -0.0003 267 PHE A CD1 2081 C CD2 . PHE A 267 ? 1.1551 0.8049 1.0903 -0.1642 0.1182 -0.0184 267 PHE A CD2 2082 C CE1 . PHE A 267 ? 1.1709 0.8777 1.2054 -0.1600 0.1443 -0.0111 267 PHE A CE1 2083 C CE2 . PHE A 267 ? 1.2199 0.8762 1.2051 -0.1512 0.1210 -0.0283 267 PHE A CE2 2084 C CZ . PHE A 267 ? 1.2086 0.8939 1.2447 -0.1483 0.1337 -0.0246 267 PHE A CZ 2085 N N . THR A 268 ? 1.2848 0.9623 1.1046 -0.2164 0.1441 0.0426 268 THR A N 2086 C CA . THR A 268 ? 1.3078 0.9772 1.0996 -0.2287 0.1358 0.0643 268 THR A CA 2087 C C . THR A 268 ? 1.2118 0.8848 1.0409 -0.2366 0.1294 0.0836 268 THR A C 2088 O O . THR A 268 ? 1.3095 1.0045 1.1745 -0.2390 0.1432 0.0865 268 THR A O 2089 C CB . THR A 268 ? 1.2418 0.9261 0.9927 -0.2381 0.1555 0.0703 268 THR A CB 2090 O OG1 . THR A 268 ? 1.2006 0.8832 0.9174 -0.2320 0.1632 0.0477 268 THR A OG1 2091 C CG2 . THR A 268 ? 1.1859 0.8576 0.9069 -0.2494 0.1416 0.0948 268 THR A CG2 2092 N N . GLY A 269 ? 1.1580 0.8097 0.9816 -0.2407 0.1087 0.0952 269 GLY A N 2093 C CA . GLY A 269 ? 1.3090 0.9587 1.1655 -0.2493 0.1009 0.1107 269 GLY A CA 2094 C C . GLY A 269 ? 1.4889 1.1521 1.3449 -0.2626 0.1153 0.1324 269 GLY A C 2095 O O . GLY A 269 ? 1.2873 0.9554 1.1058 -0.2667 0.1255 0.1400 269 GLY A O 2096 N N . GLU A 270 ? 1.5434 1.2134 1.4404 -0.2710 0.1151 0.1434 270 GLU A N 2097 C CA . GLU A 270 ? 1.2712 0.9546 1.1748 -0.2858 0.1290 0.1668 270 GLU A CA 2098 C C . GLU A 270 ? 1.2368 0.8952 1.1349 -0.2952 0.1135 0.1881 270 GLU A C 2099 O O . GLU A 270 ? 1.5743 1.2382 1.4718 -0.3085 0.1219 0.2123 270 GLU A O 2100 C CB . GLU A 270 ? 1.3483 1.0548 1.3057 -0.2918 0.1381 0.1686 270 GLU A CB 2101 C CG . GLU A 270 ? 1.5173 1.2509 1.4932 -0.2814 0.1538 0.1491 270 GLU A CG 2102 C CD . GLU A 270 ? 1.6179 1.3760 1.5670 -0.2822 0.1831 0.1483 270 GLU A CD 2103 O OE1 . GLU A 270 ? 1.7751 1.5368 1.6982 -0.2953 0.1932 0.1686 270 GLU A OE1 2104 O OE2 . GLU A 270 ? 1.4781 1.2517 1.4322 -0.2702 0.1961 0.1272 270 GLU A OE2 2105 N N . GLN A 271 ? 1.0966 0.7277 0.9927 -0.2884 0.0916 0.1796 271 GLN A N 2106 C CA . GLN A 271 ? 1.1655 0.7708 1.0675 -0.2947 0.0764 0.1957 271 GLN A CA 2107 C C . GLN A 271 ? 1.0685 0.6513 0.9424 -0.2848 0.0605 0.1888 271 GLN A C 2108 O O . GLN A 271 ? 1.3533 0.9318 1.2212 -0.2741 0.0535 0.1667 271 GLN A O 2109 C CB . GLN A 271 ? 1.0722 0.6674 1.0206 -0.3000 0.0660 0.1915 271 GLN A CB 2110 C CG . GLN A 271 ? 1.0649 0.6300 1.0269 -0.3053 0.0510 0.2028 271 GLN A CG 2111 C CD . GLN A 271 ? 1.2734 0.8270 1.2767 -0.3108 0.0403 0.1913 271 GLN A CD 2112 O OE1 . GLN A 271 ? 1.2970 0.8288 1.3026 -0.3055 0.0260 0.1755 271 GLN A OE1 2113 N NE2 . GLN A 271 ? 1.2218 0.7917 1.2579 -0.3227 0.0476 0.1982 271 GLN A NE2 2114 N N . MET A 272 ? 1.0873 0.6568 0.9476 -0.2890 0.0541 0.2097 272 MET A N 2115 C CA . MET A 272 ? 1.2351 0.7866 1.0749 -0.2802 0.0388 0.2063 272 MET A CA 2116 C C . MET A 272 ? 1.2135 0.7418 1.0822 -0.2746 0.0237 0.1922 272 MET A C 2117 O O . MET A 272 ? 1.3814 0.9014 1.2856 -0.2807 0.0219 0.1922 272 MET A O 2118 C CB . MET A 272 ? 1.2321 0.7776 1.0554 -0.2868 0.0339 0.2363 272 MET A CB 2119 C CG . MET A 272 ? 1.3828 0.9525 1.1691 -0.2951 0.0493 0.2509 272 MET A CG 2120 S SD . MET A 272 ? 1.2960 0.8602 1.0512 -0.3028 0.0378 0.2868 272 MET A SD 2121 C CE . MET A 272 ? 1.7695 1.3679 1.4776 -0.3155 0.0622 0.2963 272 MET A CE 2122 N N . ALA A 273 ? 1.0092 0.5288 0.8618 -0.2642 0.0138 0.1785 273 ALA A N 2123 C CA . ALA A 273 ? 0.9932 0.4933 0.8668 -0.2584 0.0017 0.1634 273 ALA A CA 2124 C C . ALA A 273 ? 1.0528 0.5547 0.9432 -0.2587 0.0027 0.1406 273 ALA A C 2125 O O . ALA A 273 ? 0.9917 0.4806 0.8935 -0.2555 -0.0052 0.1243 273 ALA A O 2126 C CB . ALA A 273 ? 1.0112 0.4905 0.9147 -0.2624 -0.0060 0.1796 273 ALA A CB 2127 N N . ALA A 274 ? 1.0012 0.5213 0.8934 -0.2629 0.0124 0.1396 274 ALA A N 2128 C CA . ALA A 274 ? 0.9506 0.4766 0.8598 -0.2641 0.0108 0.1218 274 ALA A CA 2129 C C . ALA A 274 ? 1.1307 0.6585 1.0194 -0.2546 0.0060 0.1026 274 ALA A C 2130 O O . ALA A 274 ? 1.1322 0.6629 1.0305 -0.2554 0.0008 0.0887 274 ALA A O 2131 C CB . ALA A 274 ? 0.9530 0.5015 0.8756 -0.2699 0.0225 0.1282 274 ALA A CB 2132 N N . TYR A 275 ? 1.0182 0.5447 0.8788 -0.2474 0.0063 0.1036 275 TYR A N 2133 C CA . TYR A 275 ? 1.0258 0.5534 0.8664 -0.2395 0.0024 0.0883 275 TYR A CA 2134 C C . TYR A 275 ? 1.1063 0.6494 0.9494 -0.2375 0.0076 0.0803 275 TYR A C 2135 O O . TYR A 275 ? 1.0759 0.6188 0.9262 -0.2366 0.0007 0.0690 275 TYR A O 2136 C CB . TYR A 275 ? 0.9103 0.4244 0.7565 -0.2386 -0.0081 0.0751 275 TYR A CB 2137 C CG . TYR A 275 ? 1.0432 0.5507 0.8704 -0.2322 -0.0127 0.0713 275 TYR A CG 2138 C CD1 . TYR A 275 ? 0.9357 0.4368 0.7615 -0.2306 -0.0144 0.0835 275 TYR A CD1 2139 C CD2 . TYR A 275 ? 1.0897 0.5986 0.9034 -0.2286 -0.0164 0.0580 275 TYR A CD2 2140 C CE1 . TYR A 275 ? 0.9601 0.4585 0.7740 -0.2252 -0.0200 0.0809 275 TYR A CE1 2141 C CE2 . TYR A 275 ? 1.0507 0.5559 0.8511 -0.2242 -0.0203 0.0552 275 TYR A CE2 2142 C CZ . TYR A 275 ? 1.2335 0.7345 1.0353 -0.2222 -0.0221 0.0659 275 TYR A CZ 2143 O OH . TYR A 275 ? 1.4597 0.9601 1.2535 -0.2182 -0.0274 0.0639 275 TYR A OH 2144 N N . PHE A 276 ? 1.2490 0.8061 1.0864 -0.2370 0.0201 0.0869 276 PHE A N 2145 C CA . PHE A 276 ? 1.1219 0.6946 0.9661 -0.2326 0.0276 0.0787 276 PHE A CA 2146 C C . PHE A 276 ? 1.1839 0.7505 1.0064 -0.2240 0.0232 0.0657 276 PHE A C 2147 O O . PHE A 276 ? 1.1670 0.7293 0.9618 -0.2218 0.0252 0.0655 276 PHE A O 2148 C CB . PHE A 276 ? 1.0503 0.6407 0.8930 -0.2349 0.0459 0.0871 276 PHE A CB 2149 C CG . PHE A 276 ? 0.9885 0.5974 0.8469 -0.2292 0.0573 0.0773 276 PHE A CG 2150 C CD1 . PHE A 276 ? 1.0851 0.6970 0.9217 -0.2214 0.0661 0.0658 276 PHE A CD1 2151 C CD2 . PHE A 276 ? 1.0387 0.6623 0.9373 -0.2318 0.0591 0.0790 276 PHE A CD2 2152 C CE1 . PHE A 276 ? 1.1764 0.8041 1.0338 -0.2145 0.0780 0.0550 276 PHE A CE1 2153 C CE2 . PHE A 276 ? 1.1194 0.7619 1.0406 -0.2250 0.0696 0.0708 276 PHE A CE2 2154 C CZ . PHE A 276 ? 1.1842 0.8281 1.0862 -0.2154 0.0800 0.0583 276 PHE A CZ 2155 N N . GLY A 277 ? 1.1625 0.7291 0.9983 -0.2206 0.0157 0.0564 277 GLY A N 2156 C CA . GLY A 277 ? 1.2715 0.8303 1.0915 -0.2139 0.0102 0.0461 277 GLY A CA 2157 C C . GLY A 277 ? 1.2782 0.8229 1.0885 -0.2161 -0.0041 0.0431 277 GLY A C 2158 O O . GLY A 277 ? 1.3717 0.9088 1.1671 -0.2127 -0.0089 0.0368 277 GLY A O 2159 N N . PHE A 278 ? 1.1815 0.7229 1.0013 -0.2227 -0.0098 0.0463 278 PHE A N 2160 C CA . PHE A 278 ? 0.9961 0.5273 0.8085 -0.2258 -0.0203 0.0407 278 PHE A CA 2161 C C . PHE A 278 ? 1.0189 0.5520 0.8325 -0.2257 -0.0288 0.0359 278 PHE A C 2162 O O . PHE A 278 ? 0.9880 0.5145 0.7867 -0.2263 -0.0347 0.0316 278 PHE A O 2163 C CB . PHE A 278 ? 0.8797 0.4073 0.7058 -0.2334 -0.0231 0.0412 278 PHE A CB 2164 C CG . PHE A 278 ? 0.8795 0.3990 0.6979 -0.2376 -0.0307 0.0315 278 PHE A CG 2165 C CD1 . PHE A 278 ? 0.8843 0.3946 0.6946 -0.2357 -0.0292 0.0284 278 PHE A CD1 2166 C CD2 . PHE A 278 ? 0.8809 0.4040 0.7010 -0.2441 -0.0391 0.0256 278 PHE A CD2 2167 C CE1 . PHE A 278 ? 0.9817 0.4875 0.7867 -0.2396 -0.0325 0.0171 278 PHE A CE1 2168 C CE2 . PHE A 278 ? 0.8865 0.4045 0.6944 -0.2498 -0.0436 0.0153 278 PHE A CE2 2169 C CZ . PHE A 278 ? 0.8879 0.3976 0.6888 -0.2473 -0.0385 0.0097 278 PHE A CZ 2170 N N . SER A 279 ? 1.1776 0.7213 1.0121 -0.2257 -0.0299 0.0387 279 SER A N 2171 C CA . SER A 279 ? 1.0756 0.6224 0.9171 -0.2255 -0.0406 0.0387 279 SER A CA 2172 C C . SER A 279 ? 1.1818 0.7385 1.0457 -0.2170 -0.0352 0.0409 279 SER A C 2173 O O . SER A 279 ? 1.2304 0.7988 1.1132 -0.2158 -0.0253 0.0433 279 SER A O 2174 C CB . SER A 279 ? 1.1236 0.6755 0.9747 -0.2358 -0.0526 0.0398 279 SER A CB 2175 O OG . SER A 279 ? 1.5725 1.1280 1.4274 -0.2373 -0.0662 0.0435 279 SER A OG 2176 N N . VAL A 280 ? 1.1682 0.7203 1.0329 -0.2113 -0.0405 0.0399 280 VAL A N 2177 C CA . VAL A 280 ? 0.9121 0.4721 0.8049 -0.2015 -0.0356 0.0395 280 VAL A CA 2178 C C . VAL A 280 ? 0.9299 0.4890 0.8409 -0.2007 -0.0527 0.0461 280 VAL A C 2179 O O . VAL A 280 ? 1.0578 0.6061 0.9489 -0.2067 -0.0654 0.0495 280 VAL A O 2180 C CB . VAL A 280 ? 1.1034 0.6551 0.9829 -0.1927 -0.0222 0.0299 280 VAL A CB 2181 C CG1 . VAL A 280 ? 1.0427 0.5995 0.9061 -0.1941 -0.0061 0.0270 280 VAL A CG1 2182 C CG2 . VAL A 280 ? 1.1530 0.6862 1.0061 -0.1942 -0.0308 0.0272 280 VAL A CG2 2183 N N . ALA A 281 ? 0.9221 0.4944 0.8735 -0.1938 -0.0530 0.0495 281 ALA A N 2184 C CA . ALA A 281 ? 1.0915 0.6639 1.0679 -0.1916 -0.0713 0.0593 281 ALA A CA 2185 C C . ALA A 281 ? 1.1643 0.7464 1.1889 -0.1770 -0.0638 0.0572 281 ALA A C 2186 O O . ALA A 281 ? 0.9665 0.5638 1.0096 -0.1721 -0.0457 0.0503 281 ALA A O 2187 C CB . ALA A 281 ? 1.0002 0.5845 0.9822 -0.2040 -0.0904 0.0711 281 ALA A CB 2188 N N . ALA A 282 ? 1.2357 0.8095 1.2831 -0.1704 -0.0769 0.0637 282 ALA A N 2189 C CA . ALA A 282 ? 0.9597 0.5405 1.0601 -0.1543 -0.0699 0.0600 282 ALA A CA 2190 C C . ALA A 282 ? 0.9632 0.5503 1.1075 -0.1525 -0.0952 0.0792 282 ALA A C 2191 O O . ALA A 282 ? 1.0236 0.5948 1.1543 -0.1579 -0.1158 0.0921 282 ALA A O 2192 C CB . ALA A 282 ? 0.9757 0.5344 1.0673 -0.1438 -0.0568 0.0444 282 ALA A CB 2193 N N . THR A 283 ? 0.9766 0.5891 1.1750 -0.1459 -0.0943 0.0830 283 THR A N 2194 C CA . THR A 283 ? 1.0369 0.6603 1.2867 -0.1430 -0.1200 0.1032 283 THR A CA 2195 C C . THR A 283 ? 1.2524 0.9016 1.5738 -0.1277 -0.1074 0.0986 283 THR A C 2196 O O . THR A 283 ? 1.5420 1.2053 1.8656 -0.1245 -0.0798 0.0822 283 THR A O 2197 C CB . THR A 283 ? 1.0574 0.6946 1.2906 -0.1622 -0.1459 0.1217 283 THR A CB 2198 O OG1 . THR A 283 ? 1.4385 1.0653 1.6051 -0.1772 -0.1397 0.1138 283 THR A OG1 2199 C CG2 . THR A 283 ? 1.0413 0.6712 1.2836 -0.1664 -0.1794 0.1458 283 THR A CG2 2200 N N . ASP A 284 ? 1.0791 0.7365 1.4613 -0.1188 -0.1275 0.1146 284 ASP A N 2201 C CA . ASP A 284 ? 1.1334 0.8216 1.5925 -0.1050 -0.1175 0.1122 284 ASP A CA 2202 C C . ASP A 284 ? 1.2895 1.0086 1.7723 -0.1182 -0.1416 0.1329 284 ASP A C 2203 O O . ASP A 284 ? 1.4658 1.1877 1.9706 -0.1222 -0.1759 0.1570 284 ASP A O 2204 C CB . ASP A 284 ? 1.1421 0.8220 1.6673 -0.0838 -0.1228 0.1148 284 ASP A CB 2205 C CG . ASP A 284 ? 1.4213 1.1361 2.0350 -0.0679 -0.1116 0.1117 284 ASP A CG 2206 O OD1 . ASP A 284 ? 1.4268 1.1668 2.0435 -0.0692 -0.0844 0.0967 284 ASP A OD1 2207 O OD2 . ASP A 284 ? 1.6242 1.3421 2.3076 -0.0542 -0.1300 0.1257 284 ASP A OD2 2208 N N . ILE A 285 ? 1.0971 0.8394 1.5752 -0.1262 -0.1244 0.1243 285 ILE A N 2209 C CA . ILE A 285 ? 1.0186 0.7882 1.5112 -0.1425 -0.1457 0.1400 285 ILE A CA 2210 C C . ILE A 285 ? 1.0680 0.8750 1.6552 -0.1318 -0.1519 0.1500 285 ILE A C 2211 O O . ILE A 285 ? 1.2032 1.0317 1.8174 -0.1429 -0.1824 0.1698 285 ILE A O 2212 C CB . ILE A 285 ? 1.0188 0.7943 1.4676 -0.1579 -0.1262 0.1279 285 ILE A CB 2213 C CG1 . ILE A 285 ? 1.0729 0.8540 1.4944 -0.1815 -0.1553 0.1412 285 ILE A CG1 2214 C CG2 . ILE A 285 ? 0.9886 0.7950 1.4880 -0.1505 -0.0966 0.1178 285 ILE A CG2 2215 C CD1 . ILE A 285 ? 1.1367 0.8877 1.4925 -0.1921 -0.1765 0.1469 285 ILE A CD1 2216 N N . ASN A 286 ? 1.0758 0.8921 1.7140 -0.1107 -0.1227 0.1351 286 ASN A N 2217 C CA . ASN A 286 ? 1.0889 0.9452 1.8241 -0.0986 -0.1213 0.1407 286 ASN A CA 2218 C C . ASN A 286 ? 1.1597 1.0135 1.9643 -0.0784 -0.1401 0.1526 286 ASN A C 2219 O O . ASN A 286 ? 1.3012 1.1886 2.1964 -0.0655 -0.1407 0.1581 286 ASN A O 2220 C CB . ASN A 286 ? 1.1416 1.0175 1.8989 -0.0887 -0.0739 0.1160 286 ASN A CB 2221 C CG . ASN A 286 ? 1.2327 1.0776 1.9514 -0.0751 -0.0428 0.0907 286 ASN A CG 2222 O OD1 . ASN A 286 ? 1.2628 1.0688 1.9239 -0.0772 -0.0543 0.0902 286 ASN A OD1 2223 N ND2 . ASN A 286 ? 1.3538 1.2176 2.1034 -0.0626 -0.0024 0.0687 286 ASN A ND2 2224 N N . GLY A 287 ? 1.0620 0.8766 1.8289 -0.0758 -0.1558 0.1576 287 GLY A N 2225 C CA . GLY A 287 ? 1.0775 0.8831 1.9079 -0.0576 -0.1760 0.1716 287 GLY A CA 2226 C C . GLY A 287 ? 1.1804 0.9870 2.0741 -0.0296 -0.1410 0.1469 287 GLY A C 2227 O O . GLY A 287 ? 1.2197 1.0349 2.2008 -0.0104 -0.1520 0.1561 287 GLY A O 2228 N N . ASP A 288 ? 1.1915 0.9895 2.0414 -0.0276 -0.0990 0.1149 288 ASP A N 2229 C CA . ASP A 288 ? 1.1210 0.9199 2.0172 -0.0037 -0.0601 0.0847 288 ASP A CA 2230 C C . ASP A 288 ? 1.1633 0.9140 2.0388 0.0081 -0.0589 0.0726 288 ASP A C 2231 O O . ASP A 288 ? 1.2479 0.9923 2.1617 0.0285 -0.0297 0.0453 288 ASP A O 2232 C CB . ASP A 288 ? 1.1306 0.9454 1.9852 -0.0097 -0.0155 0.0568 288 ASP A CB 2233 C CG . ASP A 288 ? 1.3880 1.1741 2.1303 -0.0305 -0.0138 0.0526 288 ASP A CG 2234 O OD1 . ASP A 288 ? 1.8111 1.5629 2.5075 -0.0377 -0.0407 0.0650 288 ASP A OD1 2235 O OD2 . ASP A 288 ? 1.2214 1.0206 1.9235 -0.0401 0.0145 0.0383 288 ASP A OD2 2236 N N . ASP A 289 ? 1.1708 0.8886 1.9859 -0.0062 -0.0896 0.0916 289 ASP A N 2237 C CA . ASP A 289 ? 1.2422 0.9118 2.0205 -0.0017 -0.0898 0.0819 289 ASP A CA 2238 C C . ASP A 289 ? 1.2420 0.8974 1.9588 -0.0024 -0.0490 0.0445 289 ASP A C 2239 O O . ASP A 289 ? 1.5056 1.1275 2.2123 0.0070 -0.0374 0.0246 289 ASP A O 2240 C CB . ASP A 289 ? 1.4719 1.1270 2.3379 0.0228 -0.0978 0.0835 289 ASP A CB 2241 C CG . ASP A 289 ? 1.5505 1.2030 2.4539 0.0194 -0.1474 0.1270 289 ASP A CG 2242 O OD1 . ASP A 289 ? 1.5197 1.1565 2.3553 -0.0022 -0.1748 0.1500 289 ASP A OD1 2243 O OD2 . ASP A 289 ? 1.6505 1.3184 2.6517 0.0378 -0.1590 0.1387 289 ASP A OD2 2244 N N . TYR A 290 ? 1.2207 0.9016 1.8971 -0.0150 -0.0292 0.0362 290 TYR A N 2245 C CA . TYR A 290 ? 1.1983 0.8682 1.8031 -0.0213 0.0033 0.0081 290 TYR A CA 2246 C C . TYR A 290 ? 1.2538 0.9208 1.7768 -0.0461 -0.0092 0.0221 290 TYR A C 2247 O O . TYR A 290 ? 1.3579 1.0534 1.8839 -0.0574 -0.0156 0.0367 290 TYR A O 2248 C CB . TYR A 290 ? 1.1856 0.8892 1.8195 -0.0127 0.0446 -0.0168 290 TYR A CB 2249 C CG . TYR A 290 ? 1.2707 0.9711 1.9666 0.0119 0.0694 -0.0443 290 TYR A CG 2250 C CD1 . TYR A 290 ? 1.4498 1.1153 2.1087 0.0176 0.0865 -0.0729 290 TYR A CD1 2251 C CD2 . TYR A 290 ? 1.3013 1.0345 2.0955 0.0292 0.0763 -0.0438 290 TYR A CD2 2252 C CE1 . TYR A 290 ? 1.4698 1.1300 2.1852 0.0398 0.1105 -0.1026 290 TYR A CE1 2253 C CE2 . TYR A 290 ? 1.3188 1.0489 2.1747 0.0531 0.1015 -0.0724 290 TYR A CE2 2254 C CZ . TYR A 290 ? 1.3565 1.0486 2.1711 0.0582 0.1191 -0.1030 290 TYR A CZ 2255 O OH . TYR A 290 ? 1.5227 1.2095 2.3986 0.0818 0.1453 -0.1355 290 TYR A OH 2256 N N . ALA A 291 ? 1.2239 0.8561 1.6784 -0.0542 -0.0129 0.0167 291 ALA A N 2257 C CA . ALA A 291 ? 1.1602 0.7856 1.5398 -0.0758 -0.0245 0.0280 291 ALA A CA 2258 C C . ALA A 291 ? 1.1402 0.7904 1.4920 -0.0851 -0.0011 0.0194 291 ALA A C 2259 O O . ALA A 291 ? 1.2025 0.8601 1.5513 -0.0785 0.0307 -0.0031 291 ALA A O 2260 C CB . ALA A 291 ? 1.4125 0.9999 1.7322 -0.0804 -0.0259 0.0189 291 ALA A CB 2261 N N . ASP A 292 ? 1.0673 0.7295 1.3978 -0.1015 -0.0172 0.0376 292 ASP A N 2262 C CA . ASP A 292 ? 1.0318 0.7163 1.3430 -0.1119 0.0008 0.0344 292 ASP A CA 2263 C C . ASP A 292 ? 1.0643 0.7294 1.2991 -0.1285 -0.0039 0.0362 292 ASP A C 2264 O O . ASP A 292 ? 0.9968 0.6413 1.2030 -0.1355 -0.0274 0.0461 292 ASP A O 2265 C CB . ASP A 292 ? 1.0228 0.7400 1.3849 -0.1171 -0.0122 0.0517 292 ASP A CB 2266 C CG . ASP A 292 ? 1.1703 0.9073 1.6170 -0.0997 -0.0136 0.0537 292 ASP A CG 2267 O OD1 . ASP A 292 ? 1.1937 0.9352 1.6678 -0.0839 0.0143 0.0341 292 ASP A OD1 2268 O OD2 . ASP A 292 ? 1.2251 0.9733 1.7118 -0.1018 -0.0429 0.0743 292 ASP A OD2 2269 N N . VAL A 293 ? 1.0304 0.7032 1.2346 -0.1348 0.0188 0.0275 293 VAL A N 2270 C CA . VAL A 293 ? 1.0308 0.6845 1.1678 -0.1472 0.0178 0.0269 293 VAL A CA 2271 C C . VAL A 293 ? 1.0987 0.7615 1.2235 -0.1634 0.0072 0.0406 293 VAL A C 2272 O O . VAL A 293 ? 1.2928 0.9803 1.4468 -0.1673 0.0160 0.0450 293 VAL A O 2273 C CB . VAL A 293 ? 1.0801 0.7323 1.1840 -0.1453 0.0468 0.0104 293 VAL A CB 2274 C CG1 . VAL A 293 ? 1.0882 0.7195 1.1284 -0.1563 0.0420 0.0116 293 VAL A CG1 2275 C CG2 . VAL A 293 ? 1.2247 0.8681 1.3415 -0.1300 0.0599 -0.0083 293 VAL A CG2 2276 N N . PHE A 294 ? 1.1213 0.7641 1.2052 -0.1733 -0.0105 0.0459 294 PHE A N 2277 C CA . PHE A 294 ? 1.1166 0.7622 1.1842 -0.1887 -0.0199 0.0543 294 PHE A CA 2278 C C . PHE A 294 ? 1.0349 0.6615 1.0488 -0.1950 -0.0132 0.0494 294 PHE A C 2279 O O . PHE A 294 ? 1.2803 0.8866 1.2623 -0.1936 -0.0194 0.0455 294 PHE A O 2280 C CB . PHE A 294 ? 0.9615 0.6045 1.0343 -0.1964 -0.0488 0.0648 294 PHE A CB 2281 C CG . PHE A 294 ? 1.0490 0.7146 1.1787 -0.1931 -0.0606 0.0741 294 PHE A CG 2282 C CD1 . PHE A 294 ? 0.9764 0.6422 1.1382 -0.1791 -0.0647 0.0757 294 PHE A CD1 2283 C CD2 . PHE A 294 ? 1.0033 0.6896 1.1588 -0.2040 -0.0688 0.0816 294 PHE A CD2 2284 C CE1 . PHE A 294 ? 1.0019 0.6900 1.2230 -0.1748 -0.0773 0.0862 294 PHE A CE1 2285 C CE2 . PHE A 294 ? 0.9905 0.7009 1.2027 -0.2014 -0.0820 0.0916 294 PHE A CE2 2286 C CZ . PHE A 294 ? 1.0619 0.7741 1.3082 -0.1862 -0.0865 0.0947 294 PHE A CZ 2287 N N . ILE A 295 ? 0.9915 0.6253 0.9995 -0.2023 -0.0013 0.0514 295 ILE A N 2288 C CA . ILE A 295 ? 0.9403 0.5579 0.9049 -0.2074 0.0044 0.0496 295 ILE A CA 2289 C C . ILE A 295 ? 0.9910 0.6067 0.9533 -0.2206 -0.0030 0.0563 295 ILE A C 2290 O O . ILE A 295 ? 1.1843 0.8152 1.1722 -0.2266 0.0031 0.0624 295 ILE A O 2291 C CB . ILE A 295 ? 0.9812 0.6051 0.9345 -0.2035 0.0281 0.0463 295 ILE A CB 2292 C CG1 . ILE A 295 ? 0.9772 0.6031 0.9361 -0.1905 0.0380 0.0347 295 ILE A CG1 2293 C CG2 . ILE A 295 ? 0.9304 0.5377 0.8403 -0.2084 0.0295 0.0474 295 ILE A CG2 2294 C CD1 . ILE A 295 ? 0.9952 0.6321 0.9432 -0.1879 0.0634 0.0284 295 ILE A CD1 2295 N N . GLY A 296 ? 0.9001 0.4975 0.8348 -0.2256 -0.0152 0.0540 296 GLY A N 2296 C CA . GLY A 296 ? 0.9834 0.5749 0.9161 -0.2372 -0.0213 0.0560 296 GLY A CA 2297 C C . GLY A 296 ? 1.0316 0.6137 0.9480 -0.2392 -0.0099 0.0592 296 GLY A C 2298 O O . GLY A 296 ? 1.0227 0.5966 0.9137 -0.2330 -0.0034 0.0579 296 GLY A O 2299 N N . ALA A 297 ? 1.4527 1.0353 1.3856 -0.2489 -0.0096 0.0645 297 ALA A N 2300 C CA . ALA A 297 ? 1.2974 0.8681 1.2205 -0.2522 -0.0027 0.0710 297 ALA A CA 2301 C C . ALA A 297 ? 1.1062 0.6646 1.0425 -0.2629 -0.0125 0.0684 297 ALA A C 2302 O O . ALA A 297 ? 1.1274 0.6904 1.0898 -0.2718 -0.0104 0.0756 297 ALA A O 2303 C CB . ALA A 297 ? 0.9272 0.5120 0.8612 -0.2535 0.0136 0.0838 297 ALA A CB 2304 N N . PRO A 298 ? 0.8991 0.4421 0.8183 -0.2627 -0.0221 0.0568 298 PRO A N 2305 C CA . PRO A 298 ? 0.9539 0.4855 0.8819 -0.2726 -0.0319 0.0464 298 PRO A CA 2306 C C . PRO A 298 ? 0.9879 0.5052 0.9344 -0.2789 -0.0283 0.0514 298 PRO A C 2307 O O . PRO A 298 ? 1.2204 0.7308 1.1846 -0.2895 -0.0350 0.0434 298 PRO A O 2308 C CB . PRO A 298 ? 1.2889 0.8091 1.1892 -0.2684 -0.0363 0.0334 298 PRO A CB 2309 C CG . PRO A 298 ? 0.8938 0.4226 0.7754 -0.2582 -0.0336 0.0375 298 PRO A CG 2310 C CD . PRO A 298 ? 0.8926 0.4293 0.7823 -0.2534 -0.0225 0.0512 298 PRO A CD 2311 N N . LEU A 299 ? 0.9984 0.5103 0.9406 -0.2732 -0.0192 0.0646 299 LEU A N 2312 C CA . LEU A 299 ? 0.9892 0.4849 0.9508 -0.2784 -0.0174 0.0738 299 LEU A CA 2313 C C . LEU A 299 ? 0.9909 0.4976 0.9743 -0.2860 -0.0097 0.0935 299 LEU A C 2314 O O . LEU A 299 ? 1.1303 0.6242 1.1307 -0.2914 -0.0078 0.1070 299 LEU A O 2315 C CB . LEU A 299 ? 1.2016 0.6842 1.1480 -0.2692 -0.0153 0.0799 299 LEU A CB 2316 C CG . LEU A 299 ? 1.0730 0.5484 1.0008 -0.2619 -0.0202 0.0613 299 LEU A CG 2317 C CD1 . LEU A 299 ? 1.1551 0.6203 1.0766 -0.2532 -0.0196 0.0691 299 LEU A CD1 2318 C CD2 . LEU A 299 ? 0.9436 0.4074 0.8839 -0.2687 -0.0262 0.0403 299 LEU A CD2 2319 N N . PHE A 300 ? 1.0487 0.5798 1.0345 -0.2863 -0.0047 0.0964 300 PHE A N 2320 C CA . PHE A 300 ? 0.9486 0.4963 0.9560 -0.2937 0.0062 0.1142 300 PHE A CA 2321 C C . PHE A 300 ? 1.0585 0.5980 1.1029 -0.3086 0.0013 0.1184 300 PHE A C 2322 O O . PHE A 300 ? 1.0341 0.5671 1.0922 -0.3147 -0.0110 0.1026 300 PHE A O 2323 C CB . PHE A 300 ? 1.0199 0.5967 1.0340 -0.2908 0.0119 0.1115 300 PHE A CB 2324 C CG . PHE A 300 ? 0.9668 0.5661 1.0063 -0.2983 0.0264 0.1279 300 PHE A CG 2325 C CD1 . PHE A 300 ? 1.1137 0.7241 1.1350 -0.2948 0.0440 0.1410 300 PHE A CD1 2326 C CD2 . PHE A 300 ? 1.0562 0.6677 1.1372 -0.3104 0.0229 0.1300 300 PHE A CD2 2327 C CE1 . PHE A 300 ? 1.0179 0.6521 1.0607 -0.3031 0.0606 0.1559 300 PHE A CE1 2328 C CE2 . PHE A 300 ? 1.0593 0.6948 1.1675 -0.3183 0.0383 0.1458 300 PHE A CE2 2329 C CZ . PHE A 300 ? 1.0412 0.6886 1.1298 -0.3145 0.0585 0.1588 300 PHE A CZ 2330 N N . MET A 301 ? 1.1497 0.6896 1.2088 -0.3162 0.0107 0.1403 301 MET A N 2331 C CA . MET A 301 ? 1.1398 0.6699 1.2379 -0.3319 0.0066 0.1471 301 MET A CA 2332 C C . MET A 301 ? 1.1570 0.7159 1.2835 -0.3429 0.0177 0.1625 301 MET A C 2333 O O . MET A 301 ? 1.2249 0.7983 1.3442 -0.3436 0.0335 0.1831 301 MET A O 2334 C CB . MET A 301 ? 1.0203 0.5221 1.1215 -0.3344 0.0059 0.1629 301 MET A CB 2335 C CG . MET A 301 ? 1.0289 0.5044 1.1106 -0.3228 -0.0035 0.1479 301 MET A CG 2336 S SD . MET A 301 ? 1.3082 0.7515 1.4058 -0.3231 -0.0063 0.1674 301 MET A SD 2337 C CE . MET A 301 ? 1.2143 0.6768 1.2913 -0.3254 0.0063 0.2052 301 MET A CE 2338 N N . ASP A 302 ? 0.9975 0.5672 1.1560 -0.3524 0.0094 0.1520 302 ASP A N 2339 C CA . ASP A 302 ? 1.1739 0.7718 1.3712 -0.3652 0.0184 0.1662 302 ASP A CA 2340 C C . ASP A 302 ? 1.0290 0.6077 1.2607 -0.3836 0.0147 0.1790 302 ASP A C 2341 O O . ASP A 302 ? 1.2162 0.7599 1.4400 -0.3838 0.0076 0.1785 302 ASP A O 2342 C CB . ASP A 302 ? 1.1927 0.8157 1.4129 -0.3666 0.0089 0.1509 302 ASP A CB 2343 C CG . ASP A 302 ? 1.4895 1.0942 1.7267 -0.3781 -0.0138 0.1333 302 ASP A CG 2344 O OD1 . ASP A 302 ? 1.6529 1.2232 1.8709 -0.3773 -0.0222 0.1227 302 ASP A OD1 2345 O OD2 . ASP A 302 ? 1.5784 1.2046 1.8494 -0.3882 -0.0232 0.1291 302 ASP A OD2 2346 N N . ARG A 303 ? 1.0367 0.6384 1.3114 -0.3991 0.0196 0.1905 303 ARG A N 2347 C CA . ARG A 303 ? 1.1539 0.7418 1.4596 -0.4135 0.0179 0.1993 303 ARG A CA 2348 C C . ARG A 303 ? 1.2865 0.8827 1.6281 -0.4246 0.0029 0.1806 303 ARG A C 2349 O O . ARG A 303 ? 1.3661 0.9955 1.7352 -0.4313 0.0019 0.1815 303 ARG A O 2350 C CB . ARG A 303 ? 1.0827 0.6921 1.4033 -0.4230 0.0392 0.2313 303 ARG A CB 2351 C CG . ARG A 303 ? 1.3431 0.9532 1.6247 -0.4154 0.0546 0.2518 303 ARG A CG 2352 C CD . ARG A 303 ? 1.1909 0.7851 1.4630 -0.4185 0.0624 0.2751 303 ARG A CD 2353 N NE . ARG A 303 ? 1.2488 0.8390 1.4755 -0.4104 0.0711 0.2918 303 ARG A NE 2354 C CZ . ARG A 303 ? 1.4434 1.0195 1.6528 -0.4104 0.0750 0.3144 303 ARG A CZ 2355 N NH1 . ARG A 303 ? 1.1840 0.7461 1.4199 -0.4177 0.0719 0.3231 303 ARG A NH1 2356 N NH2 . ARG A 303 ? 1.6437 1.2195 1.8088 -0.4040 0.0802 0.3287 303 ARG A NH2 2357 N N . GLY A 304 ? 1.0884 0.6557 1.4320 -0.4268 -0.0089 0.1636 304 GLY A N 2358 C CA . GLY A 304 ? 1.2567 0.8292 1.6299 -0.4399 -0.0242 0.1450 304 GLY A CA 2359 C C . GLY A 304 ? 1.3063 0.9011 1.7236 -0.4563 -0.0168 0.1639 304 GLY A C 2360 O O . GLY A 304 ? 1.3671 0.9767 1.7903 -0.4576 0.0019 0.1916 304 GLY A O 2361 N N . SER A 305 ? 1.3049 0.9038 1.7519 -0.4703 -0.0311 0.1490 305 SER A N 2362 C CA . SER A 305 ? 1.1753 0.7956 1.6680 -0.4876 -0.0261 0.1651 305 SER A CA 2363 C C . SER A 305 ? 1.4005 0.9973 1.8929 -0.4901 -0.0127 0.1851 305 SER A C 2364 O O . SER A 305 ? 1.3989 1.0175 1.9142 -0.4991 0.0026 0.2119 305 SER A O 2365 C CB . SER A 305 ? 1.2748 0.8968 1.7946 -0.5027 -0.0472 0.1423 305 SER A CB 2366 O OG . SER A 305 ? 1.5708 1.2141 2.0880 -0.5009 -0.0631 0.1255 305 SER A OG 2367 N N . ASP A 306 ? 1.6663 1.2197 2.1337 -0.4822 -0.0184 0.1726 306 ASP A N 2368 C CA . ASP A 306 ? 1.7279 1.2544 2.1959 -0.4829 -0.0099 0.1916 306 ASP A CA 2369 C C . ASP A 306 ? 1.5464 1.0847 1.9942 -0.4749 0.0093 0.2238 306 ASP A C 2370 O O . ASP A 306 ? 1.5640 1.0997 2.0212 -0.4817 0.0199 0.2509 306 ASP A O 2371 C CB . ASP A 306 ? 1.9074 1.3872 2.3556 -0.4730 -0.0201 0.1697 306 ASP A CB 2372 C CG . ASP A 306 ? 2.2345 1.6850 2.6888 -0.4724 -0.0146 0.1905 306 ASP A CG 2373 O OD1 . ASP A 306 ? 2.2477 1.6828 2.7323 -0.4856 -0.0202 0.1890 306 ASP A OD1 2374 O OD2 . ASP A 306 ? 2.3741 1.8171 2.8039 -0.4592 -0.0062 0.2092 306 ASP A OD2 2375 N N . GLY A 307 ? 1.3579 0.9090 1.7762 -0.4617 0.0134 0.2210 307 GLY A N 2376 C CA . GLY A 307 ? 1.2399 0.8025 1.6328 -0.4547 0.0311 0.2482 307 GLY A CA 2377 C C . GLY A 307 ? 1.3202 0.8509 1.6727 -0.4369 0.0278 0.2452 307 GLY A C 2378 O O . GLY A 307 ? 1.2772 0.8157 1.6009 -0.4295 0.0392 0.2637 307 GLY A O 2379 N N . LYS A 308 ? 1.3744 0.8711 1.7255 -0.4306 0.0128 0.2212 308 LYS A N 2380 C CA . LYS A 308 ? 1.2922 0.7604 1.6122 -0.4132 0.0090 0.2160 308 LYS A CA 2381 C C . LYS A 308 ? 1.2170 0.6956 1.5067 -0.4012 0.0072 0.2002 308 LYS A C 2382 O O . LYS A 308 ? 1.2959 0.7911 1.5915 -0.4050 0.0014 0.1812 308 LYS A O 2383 C CB . LYS A 308 ? 1.2954 0.7261 1.6274 -0.4107 -0.0038 0.1930 308 LYS A CB 2384 C CG . LYS A 308 ? 1.5720 0.9809 1.9256 -0.4158 -0.0029 0.2139 308 LYS A CG 2385 C CD . LYS A 308 ? 1.9303 1.3005 2.2979 -0.4122 -0.0148 0.1893 308 LYS A CD 2386 C CE . LYS A 308 ? 2.0422 1.3900 2.4373 -0.4177 -0.0155 0.2120 308 LYS A CE 2387 N NZ . LYS A 308 ? 1.8949 1.2040 2.3093 -0.4146 -0.0263 0.1871 308 LYS A NZ 2388 N N . LEU A 309 ? 1.4455 0.9150 1.7037 -0.3873 0.0106 0.2098 309 LEU A N 2389 C CA . LEU A 309 ? 1.1091 0.5843 1.3365 -0.3757 0.0078 0.1956 309 LEU A CA 2390 C C . LEU A 309 ? 1.1711 0.6276 1.3971 -0.3700 -0.0058 0.1595 309 LEU A C 2391 O O . LEU A 309 ? 1.3147 0.7442 1.5516 -0.3680 -0.0112 0.1473 309 LEU A O 2392 C CB . LEU A 309 ? 1.1090 0.5765 1.3037 -0.3634 0.0122 0.2134 309 LEU A CB 2393 C CG . LEU A 309 ? 1.1155 0.6067 1.2950 -0.3692 0.0268 0.2468 309 LEU A CG 2394 C CD1 . LEU A 309 ? 1.1224 0.6033 1.2670 -0.3583 0.0266 0.2629 309 LEU A CD1 2395 C CD2 . LEU A 309 ? 1.2104 0.7323 1.3829 -0.3746 0.0337 0.2429 309 LEU A CD2 2396 N N . GLN A 310 ? 1.0927 0.5641 1.3045 -0.3685 -0.0109 0.1428 310 GLN A N 2397 C CA . GLN A 310 ? 1.1770 0.6351 1.3783 -0.3642 -0.0229 0.1095 310 GLN A CA 2398 C C . GLN A 310 ? 1.0992 0.5688 1.2658 -0.3559 -0.0254 0.1046 310 GLN A C 2399 O O . GLN A 310 ? 1.1431 0.6371 1.3055 -0.3589 -0.0212 0.1181 310 GLN A O 2400 C CB . GLN A 310 ? 1.3220 0.7874 1.5482 -0.3787 -0.0325 0.0906 310 GLN A CB 2401 C CG . GLN A 310 ? 1.0589 0.5590 1.2980 -0.3886 -0.0343 0.0998 310 GLN A CG 2402 C CD . GLN A 310 ? 1.3341 0.8435 1.6024 -0.4044 -0.0462 0.0843 310 GLN A CD 2403 O OE1 . GLN A 310 ? 1.3293 0.8183 1.6104 -0.4106 -0.0500 0.0703 310 GLN A OE1 2404 N NE2 . GLN A 310 ? 1.3342 0.8744 1.6145 -0.4116 -0.0530 0.0867 310 GLN A NE2 2405 N N . GLU A 311 ? 1.1042 0.5572 1.2459 -0.3456 -0.0309 0.0846 311 GLU A N 2406 C CA . GLU A 311 ? 1.2111 0.6759 1.3148 -0.3361 -0.0317 0.0795 311 GLU A CA 2407 C C . GLU A 311 ? 1.2221 0.7000 1.3195 -0.3413 -0.0427 0.0569 311 GLU A C 2408 O O . GLU A 311 ? 1.1584 0.6202 1.2490 -0.3448 -0.0516 0.0331 311 GLU A O 2409 C CB . GLU A 311 ? 1.1384 0.5835 1.2174 -0.3220 -0.0305 0.0724 311 GLU A CB 2410 C CG . GLU A 311 ? 1.6033 1.0611 1.6445 -0.3106 -0.0316 0.0581 311 GLU A CG 2411 C CD . GLU A 311 ? 1.6015 1.0391 1.6281 -0.3015 -0.0328 0.0425 311 GLU A CD 2412 O OE1 . GLU A 311 ? 1.5304 0.9732 1.5331 -0.2984 -0.0362 0.0232 311 GLU A OE1 2413 O OE2 . GLU A 311 ? 1.5636 0.9814 1.6054 -0.2978 -0.0304 0.0510 311 GLU A OE2 2414 N N . VAL A 312 ? 1.0829 0.5911 1.1843 -0.3427 -0.0422 0.0648 312 VAL A N 2415 C CA . VAL A 312 ? 1.2571 0.7816 1.3504 -0.3458 -0.0549 0.0492 312 VAL A CA 2416 C C . VAL A 312 ? 1.0764 0.6167 1.1383 -0.3307 -0.0524 0.0497 312 VAL A C 2417 O O . VAL A 312 ? 0.9537 0.5045 1.0041 -0.3319 -0.0643 0.0388 312 VAL A O 2418 C CB . VAL A 312 ? 1.2106 0.7595 1.3420 -0.3593 -0.0607 0.0567 312 VAL A CB 2419 C CG1 . VAL A 312 ? 1.1383 0.6701 1.3034 -0.3769 -0.0652 0.0548 312 VAL A CG1 2420 C CG2 . VAL A 312 ? 0.9997 0.5749 1.1451 -0.3522 -0.0453 0.0794 312 VAL A CG2 2421 N N . GLY A 313 ? 1.2589 0.7999 1.3066 -0.3178 -0.0383 0.0627 313 GLY A N 2422 C CA . GLY A 313 ? 1.1014 0.6572 1.1254 -0.3043 -0.0345 0.0642 313 GLY A CA 2423 C C . GLY A 313 ? 1.0395 0.6254 1.0870 -0.3040 -0.0314 0.0735 313 GLY A C 2424 O O . GLY A 313 ? 1.1366 0.7351 1.2180 -0.3156 -0.0369 0.0762 313 GLY A O 2425 N N . GLN A 314 ? 1.1494 0.7474 1.1831 -0.2908 -0.0227 0.0771 314 GLN A N 2426 C CA . GLN A 314 ? 1.1555 0.7825 1.2160 -0.2876 -0.0186 0.0827 314 GLN A CA 2427 C C . GLN A 314 ? 1.1460 0.7779 1.1872 -0.2722 -0.0161 0.0784 314 GLN A C 2428 O O . GLN A 314 ? 0.8898 0.5052 0.8953 -0.2643 -0.0128 0.0741 314 GLN A O 2429 C CB . GLN A 314 ? 1.0852 0.7284 1.1696 -0.2906 0.0007 0.0972 314 GLN A CB 2430 C CG . GLN A 314 ? 1.2954 0.9418 1.3552 -0.2790 0.0206 0.1019 314 GLN A CG 2431 C CD . GLN A 314 ? 1.2707 0.9419 1.3547 -0.2829 0.0417 0.1150 314 GLN A CD 2432 O OE1 . GLN A 314 ? 1.0398 0.7284 1.1652 -0.2933 0.0417 0.1215 314 GLN A OE1 2433 N NE2 . GLN A 314 ? 1.4646 1.1395 1.5221 -0.2760 0.0602 0.1185 314 GLN A NE2 2434 N N . VAL A 315 ? 1.1179 0.7728 1.1880 -0.2681 -0.0184 0.0798 315 VAL A N 2435 C CA . VAL A 315 ? 1.0618 0.7198 1.1229 -0.2536 -0.0176 0.0756 315 VAL A CA 2436 C C . VAL A 315 ? 1.2559 0.9390 1.3487 -0.2446 0.0006 0.0791 315 VAL A C 2437 O O . VAL A 315 ? 1.2088 0.9163 1.3469 -0.2489 0.0011 0.0849 315 VAL A O 2438 C CB . VAL A 315 ? 1.0566 0.7158 1.1237 -0.2548 -0.0416 0.0729 315 VAL A CB 2439 C CG1 . VAL A 315 ? 1.2528 0.9156 1.3223 -0.2399 -0.0412 0.0717 315 VAL A CG1 2440 C CG2 . VAL A 315 ? 1.2450 0.8807 1.2738 -0.2630 -0.0557 0.0659 315 VAL A CG2 2441 N N . SER A 316 ? 1.3449 1.0233 1.4152 -0.2327 0.0162 0.0740 316 SER A N 2442 C CA . SER A 316 ? 1.1636 0.8645 1.2595 -0.2230 0.0370 0.0721 316 SER A CA 2443 C C . SER A 316 ? 1.2403 0.9489 1.3654 -0.2108 0.0279 0.0669 316 SER A C 2444 O O . SER A 316 ? 1.2171 0.9061 1.3183 -0.2038 0.0171 0.0610 316 SER A O 2445 C CB . SER A 316 ? 1.1958 0.8879 1.2516 -0.2174 0.0576 0.0665 316 SER A CB 2446 O OG . SER A 316 ? 1.1447 0.8581 1.2209 -0.2081 0.0801 0.0599 316 SER A OG 2447 N N . VAL A 317 ? 1.3184 1.0559 1.4994 -0.2085 0.0316 0.0705 317 VAL A N 2448 C CA . VAL A 317 ? 1.1298 0.8769 1.3499 -0.1953 0.0229 0.0680 317 VAL A CA 2449 C C . VAL A 317 ? 1.1286 0.8945 1.3773 -0.1809 0.0515 0.0580 317 VAL A C 2450 O O . VAL A 317 ? 1.1800 0.9760 1.4684 -0.1827 0.0692 0.0605 317 VAL A O 2451 C CB . VAL A 317 ? 0.9662 0.7346 1.2381 -0.2021 0.0008 0.0797 317 VAL A CB 2452 C CG1 . VAL A 317 ? 0.9869 0.7701 1.3113 -0.1868 -0.0062 0.0803 317 VAL A CG1 2453 C CG2 . VAL A 317 ? 0.9444 0.6930 1.1840 -0.2158 -0.0286 0.0851 317 VAL A CG2 2454 N N . SER A 318 ? 1.1103 0.8587 1.3398 -0.1674 0.0569 0.0454 318 SER A N 2455 C CA . SER A 318 ? 1.1761 0.9380 1.4259 -0.1535 0.0860 0.0301 318 SER A CA 2456 C C . SER A 318 ? 1.1405 0.9041 1.4413 -0.1361 0.0779 0.0246 318 SER A C 2457 O O . SER A 318 ? 1.1090 0.8449 1.3905 -0.1296 0.0628 0.0209 318 SER A O 2458 C CB . SER A 318 ? 1.1890 0.9289 1.3753 -0.1526 0.1027 0.0162 318 SER A CB 2459 O OG . SER A 318 ? 1.1616 0.9007 1.3059 -0.1678 0.1096 0.0242 318 SER A OG 2460 N N . LEU A 319 ? 1.1064 0.9033 1.4767 -0.1286 0.0880 0.0252 319 LEU A N 2461 C CA . LEU A 319 ? 1.1248 0.9264 1.5566 -0.1101 0.0811 0.0213 319 LEU A CA 2462 C C . LEU A 319 ? 1.2184 1.0155 1.6530 -0.0934 0.1123 -0.0050 319 LEU A C 2463 O O . LEU A 319 ? 1.2876 1.1067 1.7235 -0.0931 0.1467 -0.0182 319 LEU A O 2464 C CB . LEU A 319 ? 1.0961 0.9383 1.6101 -0.1084 0.0772 0.0333 319 LEU A CB 2465 C CG . LEU A 319 ? 1.0478 0.8980 1.5663 -0.1262 0.0451 0.0570 319 LEU A CG 2466 C CD1 . LEU A 319 ? 1.0498 0.9424 1.6578 -0.1232 0.0394 0.0681 319 LEU A CD1 2467 C CD2 . LEU A 319 ? 1.0261 0.8437 1.5109 -0.1297 0.0079 0.0676 319 LEU A CD2 2468 N N . GLN A 320 ? 1.2750 1.0433 1.7097 -0.0809 0.1006 -0.0129 320 GLN A N 2469 C CA . GLN A 320 ? 1.2948 1.0538 1.7327 -0.0652 0.1280 -0.0415 320 GLN A CA 2470 C C . GLN A 320 ? 1.3400 1.1278 1.8686 -0.0462 0.1446 -0.0514 320 GLN A C 2471 O O . GLN A 320 ? 1.2175 1.0122 1.8113 -0.0377 0.1207 -0.0357 320 GLN A O 2472 C CB . GLN A 320 ? 1.3013 1.0164 1.7101 -0.0597 0.1093 -0.0469 320 GLN A CB 2473 C CG . GLN A 320 ? 1.3175 1.0192 1.7358 -0.0434 0.1348 -0.0791 320 GLN A CG 2474 C CD . GLN A 320 ? 1.2594 0.9169 1.6587 -0.0388 0.1140 -0.0828 320 GLN A CD 2475 O OE1 . GLN A 320 ? 1.3461 0.9869 1.7616 -0.0250 0.1288 -0.1084 320 GLN A OE1 2476 N NE2 . GLN A 320 ? 1.1471 0.7854 1.5129 -0.0511 0.0809 -0.0585 320 GLN A NE2 2477 N N . ARG A 321 ? 1.5217 1.3278 2.0545 -0.0398 0.1859 -0.0773 321 ARG A N 2478 C CA . ARG A 321 ? 1.5301 1.3631 2.1494 -0.0194 0.2088 -0.0939 321 ARG A CA 2479 C C . ARG A 321 ? 1.5945 1.3975 2.2137 -0.0019 0.2227 -0.1256 321 ARG A C 2480 O O . ARG A 321 ? 1.6732 1.4488 2.2164 -0.0088 0.2318 -0.1426 321 ARG A O 2481 C CB . ARG A 321 ? 1.5895 1.4683 2.2210 -0.0246 0.2495 -0.1036 321 ARG A CB 2482 C CG . ARG A 321 ? 1.6281 1.5350 2.2609 -0.0438 0.2375 -0.0735 321 ARG A CG 2483 C CD . ARG A 321 ? 1.7900 1.7456 2.4504 -0.0480 0.2786 -0.0809 321 ARG A CD 2484 N NE . ARG A 321 ? 1.9009 1.8807 2.5642 -0.0683 0.2665 -0.0519 321 ARG A NE 2485 C CZ . ARG A 321 ? 1.9922 2.0175 2.6882 -0.0762 0.2950 -0.0490 321 ARG A CZ 2486 N NH1 . ARG A 321 ? 2.0246 2.0792 2.7515 -0.0653 0.3394 -0.0739 321 ARG A NH1 2487 N NH2 . ARG A 321 ? 1.9796 2.0213 2.6784 -0.0960 0.2801 -0.0221 321 ARG A NH2 2488 N N . ALA A 322 ? 1.5968 1.4048 2.3048 0.0205 0.2226 -0.1334 322 ALA A N 2489 C CA . ALA A 322 ? 1.6703 1.4476 2.3921 0.0389 0.2350 -0.1651 322 ALA A CA 2490 C C . ALA A 322 ? 1.7702 1.5559 2.4512 0.0389 0.2842 -0.2061 322 ALA A C 2491 O O . ALA A 322 ? 1.8790 1.6318 2.5320 0.0454 0.2948 -0.2360 322 ALA A O 2492 C CB . ALA A 322 ? 1.5114 1.2989 2.3494 0.0643 0.2295 -0.1654 322 ALA A CB 2493 N N . SER A 323 ? 1.6333 1.4635 2.3093 0.0296 0.3136 -0.2068 323 SER A N 2494 C CA . SER A 323 ? 1.6968 1.5441 2.3370 0.0278 0.3632 -0.2433 323 SER A CA 2495 C C . SER A 323 ? 1.6775 1.5032 2.1984 0.0056 0.3666 -0.2479 323 SER A C 2496 O O . SER A 323 ? 1.8222 1.6350 2.2988 0.0066 0.3928 -0.2832 323 SER A O 2497 C CB . SER A 323 ? 1.6382 1.5453 2.3237 0.0249 0.3948 -0.2391 323 SER A CB 2498 O OG . SER A 323 ? 1.5578 1.4802 2.2106 0.0028 0.3754 -0.2014 323 SER A OG 2499 N N . GLY A 324 ? 1.7031 1.5247 2.1738 -0.0143 0.3391 -0.2131 324 GLY A N 2500 C CA . GLY A 324 ? 1.9651 1.7810 2.3350 -0.0362 0.3476 -0.2125 324 GLY A CA 2501 C C . GLY A 324 ? 1.9827 1.7993 2.3155 -0.0562 0.3193 -0.1728 324 GLY A C 2502 O O . GLY A 324 ? 1.8881 1.6914 2.2480 -0.0551 0.2828 -0.1478 324 GLY A O 2503 N N . ASP A 325 ? 2.1404 1.9715 2.4094 -0.0752 0.3363 -0.1676 325 ASP A N 2504 C CA . ASP A 325 ? 2.2294 2.0563 2.4550 -0.0951 0.3125 -0.1337 325 ASP A CA 2505 C C . ASP A 325 ? 2.0024 1.8469 2.2918 -0.0957 0.2909 -0.1046 325 ASP A C 2506 O O . ASP A 325 ? 2.0008 1.8791 2.3636 -0.0871 0.3056 -0.1059 325 ASP A O 2507 C CB . ASP A 325 ? 2.4245 2.2737 2.5924 -0.1137 0.3399 -0.1307 325 ASP A CB 2508 C CG . ASP A 325 ? 2.5738 2.4020 2.6604 -0.1192 0.3511 -0.1525 325 ASP A CG 2509 O OD1 . ASP A 325 ? 2.6337 2.4237 2.6954 -0.1141 0.3277 -0.1606 325 ASP A OD1 2510 O OD2 . ASP A 325 ? 2.5967 2.4478 2.6433 -0.1303 0.3825 -0.1605 325 ASP A OD2 2511 N N . PHE A 326 ? 1.6555 1.4776 1.9162 -0.1067 0.2557 -0.0797 326 PHE A N 2512 C CA . PHE A 326 ? 1.3929 1.2194 1.7049 -0.1069 0.2250 -0.0555 326 PHE A CA 2513 C C . PHE A 326 ? 1.3834 1.2493 1.7343 -0.1178 0.2337 -0.0373 326 PHE A C 2514 O O . PHE A 326 ? 1.4946 1.3858 1.8332 -0.1259 0.2653 -0.0407 326 PHE A O 2515 C CB . PHE A 326 ? 1.2963 1.0873 1.5572 -0.1176 0.1888 -0.0383 326 PHE A CB 2516 C CG . PHE A 326 ? 1.3125 1.0649 1.5288 -0.1113 0.1793 -0.0530 326 PHE A CG 2517 C CD1 . PHE A 326 ? 1.3180 1.0572 1.4667 -0.1174 0.1950 -0.0666 326 PHE A CD1 2518 C CD2 . PHE A 326 ? 1.3057 1.0357 1.5477 -0.1010 0.1528 -0.0511 326 PHE A CD2 2519 C CE1 . PHE A 326 ? 1.3059 1.0111 1.4173 -0.1131 0.1850 -0.0803 326 PHE A CE1 2520 C CE2 . PHE A 326 ? 1.1749 0.8696 1.3793 -0.0970 0.1442 -0.0634 326 PHE A CE2 2521 C CZ . PHE A 326 ? 1.2826 0.9652 1.4232 -0.1030 0.1603 -0.0790 326 PHE A CZ 2522 N N . GLN A 327 ? 1.2681 1.1392 1.6652 -0.1194 0.2043 -0.0171 327 GLN A N 2523 C CA . GLN A 327 ? 1.2696 1.1706 1.6975 -0.1341 0.2020 0.0038 327 GLN A CA 2524 C C . GLN A 327 ? 1.2289 1.1034 1.6128 -0.1505 0.1684 0.0237 327 GLN A C 2525 O O . GLN A 327 ? 1.3255 1.1822 1.7185 -0.1479 0.1352 0.0311 327 GLN A O 2526 C CB . GLN A 327 ? 1.3557 1.2892 1.8792 -0.1244 0.1947 0.0097 327 GLN A CB 2527 C CG . GLN A 327 ? 1.5652 1.5246 2.1217 -0.1420 0.1818 0.0332 327 GLN A CG 2528 C CD . GLN A 327 ? 1.5161 1.4989 2.1588 -0.1346 0.1581 0.0438 327 GLN A CD 2529 O OE1 . GLN A 327 ? 1.4819 1.4809 2.1848 -0.1148 0.1672 0.0330 327 GLN A OE1 2530 N NE2 . GLN A 327 ? 1.4276 1.4121 2.0783 -0.1506 0.1262 0.0646 327 GLN A NE2 2531 N N . THR A 328 ? 1.2135 1.0858 1.5506 -0.1677 0.1774 0.0324 328 THR A N 2532 C CA . THR A 328 ? 1.0724 0.9153 1.3629 -0.1816 0.1499 0.0463 328 THR A CA 2533 C C . THR A 328 ? 1.1637 1.0233 1.4817 -0.1992 0.1401 0.0658 328 THR A C 2534 O O . THR A 328 ? 1.2520 1.1378 1.5865 -0.2085 0.1631 0.0722 328 THR A O 2535 C CB . THR A 328 ? 1.1479 0.9669 1.3612 -0.1878 0.1612 0.0426 328 THR A CB 2536 O OG1 . THR A 328 ? 1.1485 0.9495 1.3348 -0.1734 0.1667 0.0230 328 THR A OG1 2537 C CG2 . THR A 328 ? 1.2623 1.0519 1.4355 -0.2002 0.1343 0.0555 328 THR A CG2 2538 N N . THR A 329 ? 1.2422 1.0866 1.5644 -0.2052 0.1060 0.0747 329 THR A N 2539 C CA . THR A 329 ? 1.0501 0.9030 1.3920 -0.2238 0.0919 0.0902 329 THR A CA 2540 C C . THR A 329 ? 1.0362 0.8519 1.3226 -0.2349 0.0703 0.0939 329 THR A C 2541 O O . THR A 329 ? 1.3051 1.0927 1.5498 -0.2275 0.0587 0.0863 329 THR A O 2542 C CB . THR A 329 ? 1.0302 0.9059 1.4385 -0.2235 0.0694 0.0962 329 THR A CB 2543 O OG1 . THR A 329 ? 1.1014 0.9549 1.4956 -0.2153 0.0410 0.0929 329 THR A OG1 2544 C CG2 . THR A 329 ? 1.2121 1.1283 1.6873 -0.2117 0.0915 0.0930 329 THR A CG2 2545 N N . LYS A 330 ? 0.9608 0.7767 1.2506 -0.2529 0.0658 0.1049 330 LYS A N 2546 C CA . LYS A 330 ? 0.9609 0.7424 1.2054 -0.2634 0.0483 0.1065 330 LYS A CA 2547 C C . LYS A 330 ? 1.0374 0.8170 1.3050 -0.2756 0.0186 0.1089 330 LYS A C 2548 O O . LYS A 330 ? 1.2328 1.0384 1.5518 -0.2851 0.0151 0.1160 330 LYS A O 2549 C CB . LYS A 330 ? 0.9531 0.7278 1.1767 -0.2752 0.0655 0.1162 330 LYS A CB 2550 C CG . LYS A 330 ? 1.0434 0.7993 1.2108 -0.2675 0.0808 0.1131 330 LYS A CG 2551 C CD . LYS A 330 ? 1.0470 0.8244 1.2166 -0.2543 0.1058 0.1057 330 LYS A CD 2552 C CE . LYS A 330 ? 1.1015 0.8626 1.2125 -0.2509 0.1204 0.1034 330 LYS A CE 2553 N NZ . LYS A 330 ? 1.2820 1.0396 1.3749 -0.2663 0.1293 0.1211 330 LYS A NZ 2554 N N . LEU A 331 ? 1.0156 0.7663 1.2448 -0.2764 -0.0025 0.1021 331 LEU A N 2555 C CA . LEU A 331 ? 0.8998 0.6454 1.1379 -0.2901 -0.0305 0.1010 331 LEU A CA 2556 C C . LEU A 331 ? 0.8969 0.6100 1.0953 -0.3011 -0.0354 0.0963 331 LEU A C 2557 O O . LEU A 331 ? 0.9151 0.6029 1.0674 -0.2946 -0.0373 0.0887 331 LEU A O 2558 C CB . LEU A 331 ? 0.8968 0.6412 1.1288 -0.2827 -0.0528 0.0963 331 LEU A CB 2559 C CG . LEU A 331 ? 0.9956 0.7368 1.2275 -0.2978 -0.0839 0.0942 331 LEU A CG 2560 C CD1 . LEU A 331 ? 1.2463 1.0178 1.5369 -0.3105 -0.0937 0.1020 331 LEU A CD1 2561 C CD2 . LEU A 331 ? 1.0865 0.8240 1.3015 -0.2901 -0.1035 0.0932 331 LEU A CD2 2562 N N . ASN A 332 ? 0.9070 0.6211 1.1283 -0.3177 -0.0373 0.1007 332 ASN A N 2563 C CA . ASN A 332 ? 0.9185 0.6009 1.1133 -0.3281 -0.0413 0.0956 332 ASN A CA 2564 C C . ASN A 332 ? 1.0787 0.7453 1.2570 -0.3371 -0.0671 0.0809 332 ASN A C 2565 O O . ASN A 332 ? 1.2774 0.9618 1.4737 -0.3419 -0.0855 0.0788 332 ASN A O 2566 C CB . ASN A 332 ? 1.1941 0.8807 1.4229 -0.3432 -0.0325 0.1066 332 ASN A CB 2567 C CG . ASN A 332 ? 1.2403 0.9354 1.4690 -0.3371 -0.0047 0.1215 332 ASN A CG 2568 O OD1 . ASN A 332 ? 1.0188 0.7203 1.2255 -0.3214 0.0082 0.1212 332 ASN A OD1 2569 N ND2 . ASN A 332 ? 1.2653 0.9601 1.5171 -0.3510 0.0043 0.1347 332 ASN A ND2 2570 N N . GLY A 333 ? 1.0737 0.7085 1.2185 -0.3397 -0.0682 0.0709 333 GLY A N 2571 C CA . GLY A 333 ? 1.0717 0.6904 1.1953 -0.3493 -0.0881 0.0532 333 GLY A CA 2572 C C . GLY A 333 ? 1.3500 0.9694 1.5042 -0.3704 -0.1018 0.0477 333 GLY A C 2573 O O . GLY A 333 ? 1.4112 1.0508 1.6095 -0.3779 -0.0998 0.0599 333 GLY A O 2574 N N . PHE A 334 ? 1.3717 0.9699 1.5033 -0.3811 -0.1150 0.0277 334 PHE A N 2575 C CA . PHE A 334 ? 1.1474 0.7443 1.3033 -0.4033 -0.1312 0.0173 334 PHE A CA 2576 C C . PHE A 334 ? 1.0371 0.5969 1.1836 -0.4112 -0.1274 -0.0006 334 PHE A C 2577 O O . PHE A 334 ? 1.4902 1.0417 1.6714 -0.4198 -0.1225 0.0030 334 PHE A O 2578 C CB . PHE A 334 ? 1.2768 0.8895 1.4177 -0.4133 -0.1566 0.0066 334 PHE A CB 2579 C CG . PHE A 334 ? 1.0838 0.7308 1.2392 -0.4042 -0.1632 0.0247 334 PHE A CG 2580 C CD1 . PHE A 334 ? 1.0035 0.6814 1.2111 -0.4125 -0.1728 0.0379 334 PHE A CD1 2581 C CD2 . PHE A 334 ? 1.1579 0.8064 1.2802 -0.3873 -0.1599 0.0285 334 PHE A CD2 2582 C CE1 . PHE A 334 ? 1.1181 0.8276 1.3470 -0.4022 -0.1785 0.0539 334 PHE A CE1 2583 C CE2 . PHE A 334 ? 1.2568 0.9336 1.3982 -0.3779 -0.1663 0.0445 334 PHE A CE2 2584 C CZ . PHE A 334 ? 1.0560 0.7632 1.2520 -0.3844 -0.1754 0.0569 334 PHE A CZ 2585 N N . GLU A 335 ? 1.1224 0.6623 1.2254 -0.4066 -0.1282 -0.0203 335 GLU A N 2586 C CA . GLU A 335 ? 1.0680 0.5767 1.1646 -0.4076 -0.1211 -0.0413 335 GLU A CA 2587 C C . GLU A 335 ? 1.0533 0.5426 1.1443 -0.3897 -0.1008 -0.0309 335 GLU A C 2588 O O . GLU A 335 ? 1.2466 0.7435 1.3155 -0.3759 -0.0940 -0.0181 335 GLU A O 2589 C CB . GLU A 335 ? 1.0899 0.5916 1.1452 -0.4128 -0.1306 -0.0708 335 GLU A CB 2590 C CG . GLU A 335 ? 1.4281 0.9488 1.4816 -0.4324 -0.1534 -0.0828 335 GLU A CG 2591 C CD . GLU A 335 ? 1.5146 1.0288 1.5214 -0.4391 -0.1602 -0.1128 335 GLU A CD 2592 O OE1 . GLU A 335 ? 1.8504 1.3756 1.8527 -0.4564 -0.1777 -0.1287 335 GLU A OE1 2593 O OE2 . GLU A 335 ? 1.2920 0.7920 1.2659 -0.4277 -0.1475 -0.1204 335 GLU A OE2 2594 N N . VAL A 336 ? 1.2640 0.7325 1.3780 -0.3873 -0.0908 -0.0361 336 VAL A N 2595 C CA . VAL A 336 ? 1.0599 0.5103 1.1726 -0.3714 -0.0749 -0.0244 336 VAL A CA 2596 C C . VAL A 336 ? 1.0599 0.4956 1.1368 -0.3609 -0.0721 -0.0430 336 VAL A C 2597 O O . VAL A 336 ? 1.2914 0.7218 1.3534 -0.3669 -0.0782 -0.0713 336 VAL A O 2598 C CB . VAL A 336 ? 1.1104 0.5413 1.2608 -0.3728 -0.0663 -0.0224 336 VAL A CB 2599 C CG1 . VAL A 336 ? 1.0808 0.5275 1.2632 -0.3815 -0.0641 0.0031 336 VAL A CG1 2600 C CG2 . VAL A 336 ? 1.5811 0.9959 1.7398 -0.3826 -0.0716 -0.0562 336 VAL A CG2 2601 N N . PHE A 337 ? 1.1521 0.5833 1.2146 -0.3464 -0.0624 -0.0270 337 PHE A N 2602 C CA . PHE A 337 ? 1.2893 0.7098 1.3202 -0.3355 -0.0578 -0.0401 337 PHE A CA 2603 C C . PHE A 337 ? 1.3343 0.7723 1.3263 -0.3383 -0.0647 -0.0543 337 PHE A C 2604 O O . PHE A 337 ? 1.5911 1.0236 1.5580 -0.3338 -0.0612 -0.0724 337 PHE A O 2605 C CB . PHE A 337 ? 1.2927 0.6890 1.3413 -0.3331 -0.0534 -0.0630 337 PHE A CB 2606 C CG . PHE A 337 ? 1.0706 0.4496 1.1587 -0.3265 -0.0459 -0.0466 337 PHE A CG 2607 C CD1 . PHE A 337 ? 1.0530 0.4368 1.1418 -0.3180 -0.0410 -0.0142 337 PHE A CD1 2608 C CD2 . PHE A 337 ? 1.3951 0.7524 1.5154 -0.3304 -0.0426 -0.0638 337 PHE A CD2 2609 C CE1 . PHE A 337 ? 1.4669 0.8364 1.5852 -0.3133 -0.0348 0.0044 337 PHE A CE1 2610 C CE2 . PHE A 337 ? 1.3994 0.7370 1.5421 -0.3260 -0.0358 -0.0450 337 PHE A CE2 2611 C CZ . PHE A 337 ? 1.3863 0.7325 1.5309 -0.3168 -0.0328 -0.0095 337 PHE A CZ 2612 N N . ALA A 338 ? 1.2251 0.6869 1.2156 -0.3451 -0.0740 -0.0444 338 ALA A N 2613 C CA . ALA A 338 ? 1.0200 0.5001 0.9776 -0.3482 -0.0835 -0.0524 338 ALA A CA 2614 C C . ALA A 338 ? 1.0490 0.5426 0.9865 -0.3321 -0.0774 -0.0358 338 ALA A C 2615 O O . ALA A 338 ? 1.0923 0.5963 1.0000 -0.3316 -0.0829 -0.0404 338 ALA A O 2616 C CB . ALA A 338 ? 1.0264 0.5259 0.9981 -0.3631 -0.0997 -0.0489 338 ALA A CB 2617 N N . ARG A 339 ? 1.3038 0.7960 1.2565 -0.3206 -0.0665 -0.0167 339 ARG A N 2618 C CA . ARG A 339 ? 1.4821 0.9856 1.4184 -0.3061 -0.0600 -0.0020 339 ARG A CA 2619 C C . ARG A 339 ? 1.0224 0.5488 0.9522 -0.3072 -0.0695 0.0036 339 ARG A C 2620 O O . ARG A 339 ? 1.0473 0.5777 0.9502 -0.3043 -0.0740 -0.0010 339 ARG A O 2621 C CB . ARG A 339 ? 0.9497 0.4418 0.8592 -0.2969 -0.0541 -0.0114 339 ARG A CB 2622 C CG . ARG A 339 ? 1.0840 0.5546 1.0080 -0.2931 -0.0458 -0.0144 339 ARG A CG 2623 C CD . ARG A 339 ? 0.9545 0.4187 0.8599 -0.2822 -0.0393 -0.0201 339 ARG A CD 2624 N NE . ARG A 339 ? 0.9653 0.4099 0.8925 -0.2773 -0.0333 -0.0209 339 ARG A NE 2625 C CZ . ARG A 339 ? 1.2277 0.6662 1.1514 -0.2673 -0.0279 -0.0248 339 ARG A CZ 2626 N NH1 . ARG A 339 ? 1.4199 0.8702 1.3166 -0.2625 -0.0266 -0.0288 339 ARG A NH1 2627 N NH2 . ARG A 339 ? 1.2555 0.6761 1.2069 -0.2624 -0.0245 -0.0232 339 ARG A NH2 2628 N N . PHE A 340 ? 0.9849 0.5267 0.9438 -0.3117 -0.0724 0.0152 340 PHE A N 2629 C CA . PHE A 340 ? 0.9338 0.4988 0.9005 -0.3138 -0.0839 0.0214 340 PHE A CA 2630 C C . PHE A 340 ? 1.1327 0.7067 1.0853 -0.2992 -0.0802 0.0302 340 PHE A C 2631 O O . PHE A 340 ? 1.1810 0.7654 1.1262 -0.3001 -0.0930 0.0310 340 PHE A O 2632 C CB . PHE A 340 ? 0.9598 0.5415 0.9699 -0.3197 -0.0837 0.0330 340 PHE A CB 2633 C CG . PHE A 340 ? 0.9264 0.5352 0.9566 -0.3192 -0.0943 0.0420 340 PHE A CG 2634 C CD1 . PHE A 340 ? 0.9391 0.5566 0.9667 -0.3306 -0.1164 0.0364 340 PHE A CD1 2635 C CD2 . PHE A 340 ? 0.9919 0.6184 1.0453 -0.3077 -0.0825 0.0558 340 PHE A CD2 2636 C CE1 . PHE A 340 ? 1.0331 0.6763 1.0855 -0.3293 -0.1290 0.0477 340 PHE A CE1 2637 C CE2 . PHE A 340 ? 1.1126 0.7642 1.1934 -0.3052 -0.0918 0.0636 340 PHE A CE2 2638 C CZ . PHE A 340 ? 1.1174 0.7773 1.2002 -0.3155 -0.1164 0.0612 340 PHE A CZ 2639 N N . GLY A 341 ? 1.0260 0.5954 0.9748 -0.2869 -0.0641 0.0371 341 GLY A N 2640 C CA . GLY A 341 ? 1.2687 0.8451 1.2075 -0.2738 -0.0597 0.0430 341 GLY A CA 2641 C C . GLY A 341 ? 1.3468 0.9096 1.2495 -0.2683 -0.0606 0.0361 341 GLY A C 2642 O O . GLY A 341 ? 1.5573 1.1203 1.4500 -0.2575 -0.0546 0.0397 341 GLY A O 2643 N N . SER A 342 ? 1.1171 0.6688 1.0014 -0.2766 -0.0673 0.0248 342 SER A N 2644 C CA . SER A 342 ? 1.1162 0.6566 0.9696 -0.2729 -0.0650 0.0175 342 SER A CA 2645 C C . SER A 342 ? 1.0683 0.6148 0.9070 -0.2687 -0.0717 0.0223 342 SER A C 2646 O O . SER A 342 ? 1.1364 0.6769 0.9603 -0.2605 -0.0654 0.0233 342 SER A O 2647 C CB . SER A 342 ? 1.1383 0.6698 0.9778 -0.2839 -0.0691 0.0017 342 SER A CB 2648 O OG . SER A 342 ? 1.4513 0.9706 1.3056 -0.2852 -0.0614 -0.0040 342 SER A OG 2649 N N . ALA A 343 ? 0.8982 0.6310 0.9309 -0.3650 0.0126 0.1179 343 ALA A N 2650 C CA . ALA A 343 ? 0.8185 0.5354 0.8273 -0.3633 0.0165 0.1093 343 ALA A CA 2651 C C . ALA A 343 ? 1.0602 0.7805 1.0676 -0.3707 0.0101 0.1077 343 ALA A C 2652 O O . ALA A 343 ? 1.0438 0.7610 1.0554 -0.3727 0.0024 0.1097 343 ALA A O 2653 C CB . ALA A 343 ? 0.8306 0.5204 0.8220 -0.3585 0.0159 0.1034 343 ALA A CB 2654 N N . ILE A 344 ? 1.2350 0.9617 1.2412 -0.3765 0.0111 0.1013 344 ILE A N 2655 C CA . ILE A 344 ? 0.8299 0.5704 0.8462 -0.3713 0.0033 0.0910 344 ILE A CA 2656 C C . ILE A 344 ? 0.8743 0.5860 0.8903 -0.3621 -0.0041 0.0821 344 ILE A C 2657 O O . ILE A 344 ? 1.1693 0.8820 1.1945 -0.3575 -0.0039 0.0731 344 ILE A O 2658 C CB . ILE A 344 ? 0.8161 0.6166 0.8521 -0.3706 0.0060 0.0808 344 ILE A CB 2659 C CG1 . ILE A 344 ? 0.8038 0.6412 0.8455 -0.3854 0.0104 0.1008 344 ILE A CG1 2660 C CG2 . ILE A 344 ? 1.0230 0.8465 1.0740 -0.3622 -0.0032 0.0658 344 ILE A CG2 2661 C CD1 . ILE A 344 ? 0.9586 0.8770 1.0180 -0.3892 0.0136 0.0957 344 ILE A CD1 2662 N N . ALA A 345 ? 0.9882 0.6767 0.9987 -0.3609 -0.0135 0.0869 345 ALA A N 2663 C CA . ALA A 345 ? 1.1721 0.8356 1.1890 -0.3568 -0.0261 0.0887 345 ALA A CA 2664 C C . ALA A 345 ? 1.0631 0.7314 1.1041 -0.3489 -0.0413 0.0792 345 ALA A C 2665 O O . ALA A 345 ? 1.0658 0.7347 1.0994 -0.3507 -0.0441 0.0839 345 ALA A O 2666 C CB . ALA A 345 ? 0.8860 0.5276 0.8780 -0.3650 -0.0268 0.1072 345 ALA A CB 2667 N N . PRO A 346 ? 1.0923 0.7653 1.1679 -0.3390 -0.0535 0.0623 346 PRO A N 2668 C CA . PRO A 346 ? 0.9688 0.6420 1.0780 -0.3299 -0.0736 0.0506 346 PRO A CA 2669 C C . PRO A 346 ? 0.9838 0.6202 1.0927 -0.3370 -0.0903 0.0773 346 PRO A C 2670 O O . PRO A 346 ? 0.9575 0.5735 1.0631 -0.3444 -0.0947 0.0961 346 PRO A O 2671 C CB . PRO A 346 ? 0.8945 0.5823 1.0503 -0.3164 -0.0857 0.0209 346 PRO A CB 2672 C CG . PRO A 346 ? 0.8790 0.5870 1.0177 -0.3192 -0.0663 0.0157 346 PRO A CG 2673 C CD . PRO A 346 ? 0.9636 0.6438 1.0561 -0.3345 -0.0519 0.0489 346 PRO A CD 2674 N N . LEU A 347 ? 1.1484 0.7831 1.2601 -0.3370 -0.0999 0.0823 347 LEU A N 2675 C CA . LEU A 347 ? 1.2583 0.8691 1.3779 -0.3454 -0.1201 0.1102 347 LEU A CA 2676 C C . LEU A 347 ? 1.1092 0.7158 1.2751 -0.3370 -0.1459 0.1023 347 LEU A C 2677 O O . LEU A 347 ? 1.5659 1.1836 1.7234 -0.3344 -0.1434 0.0964 347 LEU A O 2678 C CB . LEU A 347 ? 1.1789 0.7937 1.2505 -0.3583 -0.1076 0.1323 347 LEU A CB 2679 C CG . LEU A 347 ? 0.9773 0.6094 1.0202 -0.3559 -0.0865 0.1171 347 LEU A CG 2680 C CD1 . LEU A 347 ? 0.9447 0.5852 0.9985 -0.3506 -0.0935 0.1088 347 LEU A CD1 2681 C CD2 . LEU A 347 ? 1.1986 0.8347 1.2021 -0.3663 -0.0735 0.1294 347 LEU A CD2 2682 N N . GLY A 348 ? 0.9916 0.5809 1.2121 -0.3330 -0.1738 0.1025 348 GLY A N 2683 C CA . GLY A 348 ? 1.4511 1.0279 1.7276 -0.3283 -0.2076 0.1040 348 GLY A CA 2684 C C . GLY A 348 ? 1.4265 1.0246 1.7138 -0.3139 -0.2058 0.0720 348 GLY A C 2685 O O . GLY A 348 ? 1.2668 0.8968 1.5445 -0.3022 -0.1865 0.0367 348 GLY A O 2686 N N . ASP A 349 ? 1.5436 1.1303 1.8516 -0.3173 -0.2273 0.0886 349 ASP A N 2687 C CA . ASP A 349 ? 1.1734 0.7788 1.4657 -0.3120 -0.2190 0.0758 349 ASP A CA 2688 C C . ASP A 349 ? 1.1805 0.7775 1.4244 -0.3318 -0.2127 0.1191 349 ASP A C 2689 O O . ASP A 349 ? 1.0969 0.6786 1.3633 -0.3428 -0.2380 0.1518 349 ASP A O 2690 C CB . ASP A 349 ? 1.1618 0.7669 1.5258 -0.2966 -0.2514 0.0516 349 ASP A CB 2691 C CG . ASP A 349 ? 1.5775 1.2059 1.9252 -0.2912 -0.2425 0.0379 349 ASP A CG 2692 O OD1 . ASP A 349 ? 1.6836 1.3330 1.9716 -0.2965 -0.2111 0.0395 349 ASP A OD1 2693 O OD2 . ASP A 349 ? 1.6047 1.2304 2.0056 -0.2817 -0.2698 0.0259 349 ASP A OD2 2694 N N . LEU A 350 ? 1.2127 0.8258 1.3964 -0.3369 -0.1819 0.1190 350 LEU A N 2695 C CA . LEU A 350 ? 1.0976 0.7126 1.2355 -0.3539 -0.1740 0.1510 350 LEU A CA 2696 C C . LEU A 350 ? 1.2123 0.8296 1.3572 -0.3580 -0.1895 0.1653 350 LEU A C 2697 O O . LEU A 350 ? 1.1960 0.8168 1.3344 -0.3736 -0.2019 0.1998 350 LEU A O 2698 C CB . LEU A 350 ? 1.0892 0.7196 1.1764 -0.3551 -0.1430 0.1395 350 LEU A CB 2699 C CG . LEU A 350 ? 1.0340 0.6753 1.0783 -0.3693 -0.1341 0.1601 350 LEU A CG 2700 C CD1 . LEU A 350 ? 0.9898 0.6320 1.0284 -0.3808 -0.1378 0.1834 350 LEU A CD1 2701 C CD2 . LEU A 350 ? 1.0003 0.6526 1.0134 -0.3671 -0.1111 0.1421 350 LEU A CD2 2702 N N . ASP A 351 ? 1.3331 0.9564 1.4916 -0.3455 -0.1892 0.1404 351 ASP A N 2703 C CA . ASP A 351 ? 1.3979 1.0239 1.5612 -0.3481 -0.2019 0.1508 351 ASP A CA 2704 C C . ASP A 351 ? 1.2639 0.8752 1.4933 -0.3419 -0.2366 0.1523 351 ASP A C 2705 O O . ASP A 351 ? 1.3470 0.9587 1.5899 -0.3435 -0.2516 0.1617 351 ASP A O 2706 C CB . ASP A 351 ? 1.2241 0.8679 1.3664 -0.3398 -0.1839 0.1262 351 ASP A CB 2707 C CG . ASP A 351 ? 1.3764 1.0363 1.5443 -0.3235 -0.1784 0.0901 351 ASP A CG 2708 O OD1 . ASP A 351 ? 1.5108 1.1680 1.7008 -0.3179 -0.1808 0.0786 351 ASP A OD1 2709 O OD2 . ASP A 351 ? 1.3196 1.0026 1.4864 -0.3173 -0.1721 0.0731 351 ASP A OD2 2710 N N . GLN A 352 ? 1.0853 0.6836 1.3615 -0.3343 -0.2520 0.1414 352 GLN A N 2711 C CA . GLN A 352 ? 1.1781 0.7600 1.5350 -0.3254 -0.2915 0.1358 352 GLN A CA 2712 C C . GLN A 352 ? 1.3416 0.9386 1.7258 -0.3070 -0.2962 0.0981 352 GLN A C 2713 O O . GLN A 352 ? 1.5966 1.1823 2.0331 -0.3045 -0.3278 0.1038 352 GLN A O 2714 C CB . GLN A 352 ? 1.0741 0.6400 1.4532 -0.3462 -0.3225 0.1900 352 GLN A CB 2715 C CG . GLN A 352 ? 1.1758 0.7400 1.5456 -0.3609 -0.3254 0.2268 352 GLN A CG 2716 C CD . GLN A 352 ? 1.4364 0.9864 1.8730 -0.3443 -0.3489 0.2116 352 GLN A CD 2717 O OE1 . GLN A 352 ? 1.7268 1.2656 2.2364 -0.3262 -0.3777 0.1853 352 GLN A OE1 2718 N NE2 . GLN A 352 ? 1.0939 0.6472 1.5099 -0.3493 -0.3382 0.2249 352 GLN A NE2 2719 N N . ASP A 353 ? 1.1526 0.7805 1.5044 -0.2957 -0.2665 0.0625 353 ASP A N 2720 C CA . ASP A 353 ? 1.2952 0.9530 1.6668 -0.2798 -0.2671 0.0266 353 ASP A CA 2721 C C . ASP A 353 ? 1.2374 0.9184 1.6787 -0.2564 -0.2842 -0.0255 353 ASP A C 2722 O O . ASP A 353 ? 1.2833 1.0002 1.7550 -0.2402 -0.2898 -0.0631 353 ASP A O 2723 C CB . ASP A 353 ? 1.2025 0.8941 1.5103 -0.2831 -0.2304 0.0203 353 ASP A CB 2724 C CG . ASP A 353 ? 1.4211 1.1420 1.7132 -0.2789 -0.2079 -0.0017 353 ASP A CG 2725 O OD1 . ASP A 353 ? 1.5089 1.2087 1.7760 -0.2886 -0.1983 0.0172 353 ASP A OD1 2726 O OD2 . ASP A 353 ? 1.5403 1.3128 1.8454 -0.2670 -0.2002 -0.0370 353 ASP A OD2 2727 N N . GLY A 354 ? 1.0707 0.7372 1.5400 -0.2539 -0.2936 -0.0308 354 GLY A N 2728 C CA . GLY A 354 ? 1.0550 0.7467 1.5976 -0.2302 -0.3129 -0.0860 354 GLY A CA 2729 C C . GLY A 354 ? 1.1151 0.8533 1.6290 -0.2238 -0.2830 -0.1172 354 GLY A C 2730 O O . GLY A 354 ? 1.0785 0.8451 1.6488 -0.2051 -0.2963 -0.1649 354 GLY A O 2731 N N . PHE A 355 ? 1.3740 1.1240 1.8063 -0.2395 -0.2453 -0.0915 355 PHE A N 2732 C CA . PHE A 355 ? 1.3569 1.1518 1.7590 -0.2387 -0.2171 -0.1100 355 PHE A CA 2733 C C . PHE A 355 ? 1.3482 1.1038 1.6962 -0.2578 -0.1985 -0.0678 355 PHE A C 2734 O O . PHE A 355 ? 1.5122 1.2355 1.8135 -0.2746 -0.1893 -0.0263 355 PHE A O 2735 C CB . PHE A 355 ? 1.2577 1.1180 1.6236 -0.2400 -0.1919 -0.1213 355 PHE A CB 2736 C CG . PHE A 355 ? 1.1014 1.0203 1.5177 -0.2207 -0.2064 -0.1685 355 PHE A CG 2737 C CD1 . PHE A 355 ? 1.0741 1.0660 1.5352 -0.2018 -0.2103 -0.2252 355 PHE A CD1 2738 C CD2 . PHE A 355 ? 1.0996 1.0087 1.5201 -0.2206 -0.2165 -0.1599 355 PHE A CD2 2739 C CE1 . PHE A 355 ? 1.1391 1.1981 1.6501 -0.1823 -0.2243 -0.2757 355 PHE A CE1 2740 C CE2 . PHE A 355 ? 1.2691 1.2367 1.7378 -0.2020 -0.2303 -0.2061 355 PHE A CE2 2741 C CZ . PHE A 355 ? 1.3622 1.4074 1.8772 -0.1823 -0.2343 -0.2657 355 PHE A CZ 2742 N N . ASN A 356 ? 1.1518 0.9162 1.5086 -0.2541 -0.1937 -0.0827 356 ASN A N 2743 C CA . ASN A 356 ? 1.1040 0.8364 1.4146 -0.2704 -0.1767 -0.0478 356 ASN A CA 2744 C C . ASN A 356 ? 1.0906 0.8415 1.3337 -0.2844 -0.1441 -0.0271 356 ASN A C 2745 O O . ASN A 356 ? 1.3323 1.1346 1.5679 -0.2816 -0.1318 -0.0436 356 ASN A O 2746 C CB . ASN A 356 ? 1.0777 0.8230 1.4143 -0.2622 -0.1776 -0.0727 356 ASN A CB 2747 C CG . ASN A 356 ? 1.0189 0.7291 1.4278 -0.2522 -0.2154 -0.0832 356 ASN A CG 2748 O OD1 . ASN A 356 ? 1.1112 0.7727 1.5356 -0.2609 -0.2379 -0.0495 356 ASN A OD1 2749 N ND2 . ASN A 356 ? 1.1405 0.8805 1.5999 -0.2349 -0.2255 -0.1292 356 ASN A ND2 2750 N N . ASP A 357 ? 1.1162 0.8302 1.3167 -0.3001 -0.1331 0.0091 357 ASP A N 2751 C CA . ASP A 357 ? 1.3240 1.0484 1.4729 -0.3126 -0.1086 0.0269 357 ASP A CA 2752 C C . ASP A 357 ? 1.1883 0.9069 1.3126 -0.3201 -0.0922 0.0363 357 ASP A C 2753 O O . ASP A 357 ? 1.2698 0.9759 1.4120 -0.3164 -0.0983 0.0307 357 ASP A O 2754 C CB . ASP A 357 ? 1.1816 0.8762 1.3043 -0.3229 -0.1115 0.0550 357 ASP A CB 2755 C CG . ASP A 357 ? 1.3482 1.0410 1.4985 -0.3162 -0.1311 0.0499 357 ASP A CG 2756 O OD1 . ASP A 357 ? 1.3075 1.0330 1.4646 -0.3104 -0.1283 0.0333 357 ASP A OD1 2757 O OD2 . ASP A 357 ? 1.5112 1.1744 1.6797 -0.3184 -0.1511 0.0652 357 ASP A OD2 2758 N N . ILE A 358 ? 1.0329 0.7595 1.1226 -0.3307 -0.0745 0.0504 358 ILE A N 2759 C CA . ILE A 358 ? 1.1088 0.8343 1.1799 -0.3374 -0.0598 0.0574 358 ILE A CA 2760 C C . ILE A 358 ? 1.0267 0.7392 1.0670 -0.3493 -0.0499 0.0773 358 ILE A C 2761 O O . ILE A 358 ? 1.2086 0.9251 1.2446 -0.3523 -0.0524 0.0824 358 ILE A O 2762 C CB . ILE A 358 ? 1.0367 0.8151 1.1223 -0.3343 -0.0507 0.0394 358 ILE A CB 2763 C CG1 . ILE A 358 ? 1.0560 0.8290 1.1366 -0.3362 -0.0420 0.0395 358 ILE A CG1 2764 C CG2 . ILE A 358 ? 0.8517 0.6672 0.9275 -0.3444 -0.0418 0.0506 358 ILE A CG2 2765 C CD1 . ILE A 358 ? 0.9974 0.8325 1.0948 -0.3331 -0.0346 0.0197 358 ILE A CD1 2766 N N . ALA A 359 ? 1.1582 0.8563 1.1826 -0.3550 -0.0410 0.0854 359 ALA A N 2767 C CA . ALA A 359 ? 1.2185 0.9059 1.2240 -0.3634 -0.0354 0.0962 359 ALA A CA 2768 C C . ALA A 359 ? 1.1086 0.8079 1.1153 -0.3690 -0.0250 0.0989 359 ALA A C 2769 O O . ALA A 359 ? 1.1298 0.8264 1.1338 -0.3683 -0.0186 0.0973 359 ALA A O 2770 C CB . ALA A 359 ? 1.1293 0.7923 1.1156 -0.3657 -0.0382 0.1031 359 ALA A CB 2771 N N . ILE A 360 ? 1.2140 0.9266 1.2302 -0.3759 -0.0262 0.1058 360 ILE A N 2772 C CA . ILE A 360 ? 0.9443 0.6698 0.9710 -0.3844 -0.0216 0.1148 360 ILE A CA 2773 C C . ILE A 360 ? 0.9120 0.6180 0.9427 -0.3794 -0.0250 0.1132 360 ILE A C 2774 O O . ILE A 360 ? 1.2642 0.9593 1.2989 -0.3807 -0.0350 0.1103 360 ILE A O 2775 C CB . ILE A 360 ? 0.8321 0.6041 0.8826 -0.3932 -0.0252 0.1272 360 ILE A CB 2776 C CG1 . ILE A 360 ? 0.8258 0.6370 0.8781 -0.3866 -0.0218 0.1153 360 ILE A CG1 2777 C CG2 . ILE A 360 ? 0.8846 0.6805 0.9513 -0.3975 -0.0217 0.1405 360 ILE A CG2 2778 C CD1 . ILE A 360 ? 0.8437 0.7220 0.9171 -0.3965 -0.0243 0.1267 360 ILE A CD1 2779 N N . ALA A 361 ? 0.9463 0.6500 0.9794 -0.3750 -0.0187 0.1118 361 ALA A N 2780 C CA . ALA A 361 ? 1.2305 0.9159 1.2693 -0.3733 -0.0238 0.1025 361 ALA A CA 2781 C C . ALA A 361 ? 1.2928 0.9878 1.3687 -0.3722 -0.0296 0.1075 361 ALA A C 2782 O O . ALA A 361 ? 1.3788 1.0925 1.4625 -0.3709 -0.0225 0.1182 361 ALA A O 2783 C CB . ALA A 361 ? 0.8590 0.5305 0.8699 -0.3720 -0.0150 0.0942 361 ALA A CB 2784 N N . ALA A 362 ? 1.0304 0.7136 1.1329 -0.3740 -0.0454 0.0985 362 ALA A N 2785 C CA . ALA A 362 ? 1.0649 0.7512 1.2121 -0.3725 -0.0569 0.1004 362 ALA A CA 2786 C C . ALA A 362 ? 0.9834 0.6470 1.1425 -0.3726 -0.0665 0.0731 362 ALA A C 2787 O O . ALA A 362 ? 0.8866 0.5398 1.0728 -0.3739 -0.0864 0.0543 362 ALA A O 2788 C CB . ALA A 362 ? 0.8620 0.5593 1.0464 -0.3748 -0.0750 0.1125 362 ALA A CB 2789 N N . PRO A 363 ? 0.8681 0.5286 1.0105 -0.3717 -0.0547 0.0677 363 PRO A N 2790 C CA . PRO A 363 ? 0.9706 0.6173 1.1086 -0.3769 -0.0604 0.0395 363 PRO A CA 2791 C C . PRO A 363 ? 0.9646 0.6050 1.1653 -0.3738 -0.0875 0.0139 363 PRO A C 2792 O O . PRO A 363 ? 1.0893 0.7432 1.2908 -0.3622 -0.0914 -0.0257 363 PRO A O 2793 C CB . PRO A 363 ? 1.2332 0.8847 1.3510 -0.3738 -0.0416 0.0487 363 PRO A CB 2794 C CG . PRO A 363 ? 1.1907 0.8575 1.2883 -0.3674 -0.0252 0.0756 363 PRO A CG 2795 C CD . PRO A 363 ? 0.8497 0.5264 0.9770 -0.3673 -0.0362 0.0880 363 PRO A CD 2796 N N . TYR A 364 ? 0.8916 0.5372 1.1371 -0.3662 -0.0961 0.0294 364 TYR A N 2797 C CA . TYR A 364 ? 0.9080 0.5489 1.2176 -0.3585 -0.1243 0.0070 364 TYR A CA 2798 C C . TYR A 364 ? 1.0578 0.6989 1.4075 -0.3540 -0.1482 0.0046 364 TYR A C 2799 O O . TYR A 364 ? 1.5065 1.1454 1.9176 -0.3439 -0.1762 -0.0130 364 TYR A O 2800 C CB . TYR A 364 ? 0.9046 0.5510 1.2371 -0.3553 -0.1249 0.0296 364 TYR A CB 2801 C CG . TYR A 364 ? 0.8912 0.5380 1.1827 -0.3587 -0.0997 0.0315 364 TYR A CG 2802 C CD1 . TYR A 364 ? 0.8983 0.5373 1.1948 -0.3578 -0.1030 -0.0035 364 TYR A CD1 2803 C CD2 . TYR A 364 ? 0.9838 0.6450 1.2361 -0.3615 -0.0747 0.0641 364 TYR A CD2 2804 C CE1 . TYR A 364 ? 1.2709 0.9108 1.5300 -0.3623 -0.0812 0.0014 364 TYR A CE1 2805 C CE2 . TYR A 364 ? 1.1619 0.8246 1.3819 -0.3613 -0.0532 0.0649 364 TYR A CE2 2806 C CZ . TYR A 364 ? 1.1973 0.8469 1.4183 -0.3627 -0.0557 0.0370 364 TYR A CZ 2807 O OH . TYR A 364 ? 1.1111 0.7639 1.3007 -0.3627 -0.0358 0.0411 364 TYR A OH 2808 N N . GLY A 365 ? 0.9650 0.6099 1.2834 -0.3600 -0.1390 0.0220 365 GLY A N 2809 C CA . GLY A 365 ? 0.9240 0.5702 1.2760 -0.3572 -0.1599 0.0240 365 GLY A CA 2810 C C . GLY A 365 ? 1.0596 0.6993 1.4216 -0.3537 -0.1743 -0.0209 365 GLY A C 2811 O O . GLY A 365 ? 1.0344 0.6750 1.3829 -0.3542 -0.1716 -0.0566 365 GLY A O 2812 N N . GLY A 366 ? 1.3236 0.9642 1.7125 -0.3506 -0.1918 -0.0209 366 GLY A N 2813 C CA . GLY A 366 ? 1.3575 1.0002 1.7568 -0.3463 -0.2062 -0.0653 366 GLY A CA 2814 C C . GLY A 366 ? 1.6096 1.2597 2.0782 -0.3277 -0.2361 -0.1167 366 GLY A C 2815 O O . GLY A 366 ? 1.5310 1.1772 2.0465 -0.3183 -0.2500 -0.1126 366 GLY A O 2816 N N . GLU A 367 ? 1.7546 1.4223 2.2320 -0.3207 -0.2475 -0.1676 367 GLU A N 2817 C CA . GLU A 367 ? 1.6988 1.3887 2.2407 -0.2974 -0.2747 -0.2297 367 GLU A CA 2818 C C . GLU A 367 ? 1.5644 1.2746 2.1145 -0.2885 -0.2712 -0.2688 367 GLU A C 2819 O O . GLU A 367 ? 1.2666 1.0035 1.7479 -0.2923 -0.2410 -0.2748 367 GLU A O 2820 C CB . GLU A 367 ? 1.7334 1.4570 2.2717 -0.2910 -0.2823 -0.2814 367 GLU A CB 2821 C CG . GLU A 367 ? 1.8080 1.5761 2.2388 -0.2912 -0.2397 -0.2792 367 GLU A CG 2822 C CD . GLU A 367 ? 1.7913 1.6114 2.2052 -0.2805 -0.2411 -0.3207 367 GLU A CD 2823 O OE1 . GLU A 367 ? 1.7447 1.6135 2.0817 -0.2818 -0.2125 -0.3210 367 GLU A OE1 2824 O OE2 . GLU A 367 ? 1.7125 1.5278 2.1936 -0.2721 -0.2732 -0.3508 367 GLU A OE2 2825 N N . ASP A 368 ? 1.5697 1.2776 2.1883 -0.2692 -0.2944 -0.2834 368 ASP A N 2826 C CA . ASP A 368 ? 1.3509 1.0783 1.9884 -0.2572 -0.2948 -0.3205 368 ASP A CA 2827 C C . ASP A 368 ? 1.1354 0.8422 1.7183 -0.2777 -0.2665 -0.2751 368 ASP A C 2828 O O . ASP A 368 ? 1.3462 1.0741 1.9193 -0.2747 -0.2569 -0.3055 368 ASP A O 2829 C CB . ASP A 368 ? 1.3819 1.1750 2.0107 -0.2430 -0.2927 -0.4037 368 ASP A CB 2830 C CG . ASP A 368 ? 1.7944 1.6176 2.4617 -0.2242 -0.3146 -0.4483 368 ASP A CG 2831 O OD1 . ASP A 368 ? 1.8264 1.6208 2.5623 -0.2109 -0.3424 -0.4346 368 ASP A OD1 2832 O OD2 . ASP A 368 ? 1.8131 1.6960 2.4429 -0.2231 -0.3045 -0.4957 368 ASP A OD2 2833 N N . LYS A 369 ? 0.9989 0.6724 1.5477 -0.2967 -0.2529 -0.2047 369 LYS A N 2834 C CA . LYS A 369 ? 0.9780 0.6356 1.4746 -0.3141 -0.2252 -0.1563 369 LYS A CA 2835 C C . LYS A 369 ? 0.9654 0.6432 1.3977 -0.3206 -0.1973 -0.1774 369 LYS A C 2836 O O . LYS A 369 ? 0.9576 0.6363 1.3693 -0.3227 -0.1819 -0.1700 369 LYS A O 2837 C CB . LYS A 369 ? 1.1878 0.8371 1.7268 -0.3064 -0.2356 -0.1405 369 LYS A CB 2838 C CG . LYS A 369 ? 1.2197 0.8623 1.8341 -0.2946 -0.2692 -0.1242 369 LYS A CG 2839 C CD . LYS A 369 ? 1.3767 1.0125 2.0211 -0.2955 -0.2766 -0.0831 369 LYS A CD 2840 C CE . LYS A 369 ? 1.5124 1.1489 2.0988 -0.3159 -0.2505 -0.0187 369 LYS A CE 2841 N NZ . LYS A 369 ? 1.5673 1.2087 2.1858 -0.3176 -0.2611 0.0218 369 LYS A NZ 2842 N N . LYS A 370 ? 1.2502 0.9598 1.6293 -0.3149 -0.1822 -0.1939 370 LYS A N 2843 C CA . LYS A 370 ? 1.0347 0.7860 1.3306 -0.3129 -0.1487 -0.2004 370 LYS A CA 2844 C C . LYS A 370 ? 1.0748 0.8056 1.2990 -0.3289 -0.1197 -0.1412 370 LYS A C 2845 O O . LYS A 370 ? 1.1280 0.8828 1.2914 -0.3312 -0.0952 -0.1335 370 LYS A O 2846 C CB . LYS A 370 ? 1.1972 1.0048 1.4760 -0.3015 -0.1498 -0.2444 370 LYS A CB 2847 C CG . LYS A 370 ? 1.1453 0.9921 1.4943 -0.2815 -0.1779 -0.3178 370 LYS A CG 2848 C CD . LYS A 370 ? 1.1467 1.0587 1.4774 -0.2720 -0.1789 -0.3589 370 LYS A CD 2849 C CE . LYS A 370 ? 1.4056 1.3673 1.8139 -0.2491 -0.2093 -0.4428 370 LYS A CE 2850 N NZ . LYS A 370 ? 1.4209 1.4544 1.8153 -0.2401 -0.2120 -0.4852 370 LYS A NZ 2851 N N . GLY A 371 ? 1.0916 0.7840 1.3293 -0.3400 -0.1256 -0.1007 371 GLY A N 2852 C CA . GLY A 371 ? 0.9520 0.6303 1.1346 -0.3524 -0.1026 -0.0530 371 GLY A CA 2853 C C . GLY A 371 ? 0.9691 0.6520 1.1209 -0.3543 -0.0982 -0.0412 371 GLY A C 2854 O O . GLY A 371 ? 1.0552 0.7643 1.1970 -0.3465 -0.1015 -0.0690 371 GLY A O 2855 N N . ILE A 372 ? 0.9148 0.5795 1.0527 -0.3648 -0.0910 -0.0014 372 ILE A N 2856 C CA . ILE A 372 ? 0.9146 0.5810 1.0303 -0.3669 -0.0887 0.0123 372 ILE A CA 2857 C C . ILE A 372 ? 1.0192 0.6825 1.0925 -0.3730 -0.0687 0.0424 372 ILE A C 2858 O O . ILE A 372 ? 0.9502 0.6076 1.0279 -0.3792 -0.0623 0.0615 372 ILE A O 2859 C CB . ILE A 372 ? 1.1679 0.8231 1.3328 -0.3724 -0.1103 0.0245 372 ILE A CB 2860 C CG1 . ILE A 372 ? 1.2297 0.8846 1.4510 -0.3647 -0.1369 -0.0095 372 ILE A CG1 2861 C CG2 . ILE A 372 ? 1.0611 0.7206 1.2018 -0.3742 -0.1068 0.0380 372 ILE A CG2 2862 C CD1 . ILE A 372 ? 1.4403 1.1184 1.6425 -0.3526 -0.1375 -0.0471 372 ILE A CD1 2863 N N . VAL A 373 ? 0.9436 0.6145 0.9819 -0.3710 -0.0617 0.0449 373 VAL A N 2864 C CA . VAL A 373 ? 0.9821 0.6493 0.9954 -0.3743 -0.0500 0.0676 373 VAL A CA 2865 C C . VAL A 373 ? 1.0913 0.7598 1.1104 -0.3751 -0.0567 0.0765 373 VAL A C 2866 O O . VAL A 373 ? 1.1842 0.8573 1.1984 -0.3721 -0.0637 0.0674 373 VAL A O 2867 C CB . VAL A 373 ? 1.0317 0.7055 1.0083 -0.3730 -0.0405 0.0687 373 VAL A CB 2868 C CG1 . VAL A 373 ? 0.9917 0.6581 0.9586 -0.3742 -0.0357 0.0871 373 VAL A CG1 2869 C CG2 . VAL A 373 ? 0.9514 0.6300 0.9205 -0.3732 -0.0329 0.0616 373 VAL A CG2 2870 N N . TYR A 374 ? 1.0818 0.7548 1.1119 -0.3794 -0.0546 0.0931 374 TYR A N 2871 C CA . TYR A 374 ? 1.0937 0.7771 1.1310 -0.3803 -0.0603 0.1008 374 TYR A CA 2872 C C . TYR A 374 ? 1.3037 0.9916 1.3217 -0.3754 -0.0532 0.1023 374 TYR A C 2873 O O . TYR A 374 ? 1.2682 0.9612 1.2824 -0.3745 -0.0448 0.1041 374 TYR A O 2874 C CB . TYR A 374 ? 0.9932 0.6972 1.0622 -0.3898 -0.0660 0.1177 374 TYR A CB 2875 C CG . TYR A 374 ? 1.0822 0.7846 1.1876 -0.3887 -0.0785 0.1181 374 TYR A CG 2876 C CD1 . TYR A 374 ? 1.0374 0.7400 1.1568 -0.3854 -0.0754 0.1176 374 TYR A CD1 2877 C CD2 . TYR A 374 ? 0.8810 0.5817 1.0132 -0.3902 -0.0960 0.1179 374 TYR A CD2 2878 C CE1 . TYR A 374 ? 1.1854 0.8847 1.3475 -0.3835 -0.0911 0.1159 374 TYR A CE1 2879 C CE2 . TYR A 374 ? 0.9544 0.6521 1.1310 -0.3877 -0.1124 0.1156 374 TYR A CE2 2880 C CZ . TYR A 374 ? 1.2283 0.9248 1.4212 -0.3843 -0.1108 0.1143 374 TYR A CZ 2881 O OH . TYR A 374 ? 1.1871 0.8791 1.4308 -0.3809 -0.1312 0.1106 374 TYR A OH 2882 N N . ILE A 375 ? 1.3227 1.0090 1.3349 -0.3717 -0.0595 0.1000 375 ILE A N 2883 C CA . ILE A 375 ? 0.9411 0.6292 0.9485 -0.3662 -0.0597 0.0999 375 ILE A CA 2884 C C . ILE A 375 ? 1.0321 0.7454 1.0583 -0.3646 -0.0632 0.0994 375 ILE A C 2885 O O . ILE A 375 ? 1.0056 0.7266 1.0397 -0.3676 -0.0697 0.1027 375 ILE A O 2886 C CB . ILE A 375 ? 0.9148 0.5905 0.9080 -0.3646 -0.0672 0.1012 375 ILE A CB 2887 C CG1 . ILE A 375 ? 0.9579 0.6255 0.9341 -0.3671 -0.0640 0.1058 375 ILE A CG1 2888 C CG2 . ILE A 375 ? 1.0609 0.7384 1.0661 -0.3594 -0.0759 0.1021 375 ILE A CG2 2889 C CD1 . ILE A 375 ? 1.2270 0.8989 1.1917 -0.3705 -0.0585 0.0989 375 ILE A CD1 2890 N N . PHE A 376 ? 0.9082 0.6408 0.9448 -0.3596 -0.0602 0.0925 376 PHE A N 2891 C CA . PHE A 376 ? 1.0791 0.8539 1.1352 -0.3571 -0.0628 0.0860 376 PHE A CA 2892 C C . PHE A 376 ? 0.9619 0.7385 1.0321 -0.3444 -0.0711 0.0686 376 PHE A C 2893 O O . PHE A 376 ? 0.9729 0.7422 1.0519 -0.3376 -0.0721 0.0578 376 PHE A O 2894 C CB . PHE A 376 ? 0.8838 0.7048 0.9508 -0.3623 -0.0542 0.0867 376 PHE A CB 2895 C CG . PHE A 376 ? 1.0820 0.9073 1.1501 -0.3769 -0.0525 0.1084 376 PHE A CG 2896 C CD1 . PHE A 376 ? 1.1994 0.9951 1.2587 -0.3807 -0.0475 0.1141 376 PHE A CD1 2897 C CD2 . PHE A 376 ? 1.2853 1.1458 1.3705 -0.3875 -0.0594 0.1242 376 PHE A CD2 2898 C CE1 . PHE A 376 ? 1.1246 0.9218 1.1971 -0.3932 -0.0514 0.1320 376 PHE A CE1 2899 C CE2 . PHE A 376 ? 1.1877 1.0496 1.2880 -0.4024 -0.0650 0.1475 376 PHE A CE2 2900 C CZ . PHE A 376 ? 1.1398 0.9679 1.2365 -0.4044 -0.0620 0.1499 376 PHE A CZ 2901 N N . ASN A 377 ? 1.0608 0.8464 1.1400 -0.3411 -0.0800 0.0654 377 ASN A N 2902 C CA . ASN A 377 ? 1.0325 0.8205 1.1361 -0.3281 -0.0928 0.0469 377 ASN A CA 2903 C C . ASN A 377 ? 1.2046 1.0540 1.3373 -0.3188 -0.0923 0.0197 377 ASN A C 2904 O O . ASN A 377 ? 1.0830 0.9865 1.2142 -0.3253 -0.0835 0.0214 377 ASN A O 2905 C CB . ASN A 377 ? 1.0302 0.8058 1.1339 -0.3278 -0.1035 0.0528 377 ASN A CB 2906 C CG . ASN A 377 ? 1.1756 0.9035 1.2571 -0.3345 -0.1078 0.0729 377 ASN A CG 2907 O OD1 . ASN A 377 ? 1.0467 0.7505 1.1196 -0.3371 -0.1071 0.0805 377 ASN A OD1 2908 N ND2 . ASN A 377 ? 1.4517 1.1743 1.5244 -0.3380 -0.1128 0.0813 377 ASN A ND2 2909 N N . GLY A 378 ? 1.2685 1.1171 1.4336 -0.3042 -0.1047 -0.0058 378 GLY A N 2910 C CA . GLY A 378 ? 1.0701 0.9869 1.2710 -0.2911 -0.1075 -0.0437 378 GLY A CA 2911 C C . GLY A 378 ? 1.1884 1.1322 1.4163 -0.2809 -0.1211 -0.0629 378 GLY A C 2912 O O . GLY A 378 ? 1.4071 1.3020 1.6345 -0.2811 -0.1332 -0.0489 378 GLY A O 2913 N N . ARG A 379 ? 1.0789 1.1094 1.3308 -0.2726 -0.1193 -0.0955 379 ARG A N 2914 C CA . ARG A 379 ? 1.0733 1.1436 1.3549 -0.2611 -0.1319 -0.1203 379 ARG A CA 2915 C C . ARG A 379 ? 1.1289 1.2824 1.4631 -0.2400 -0.1409 -0.1796 379 ARG A C 2916 O O . ARG A 379 ? 1.1480 1.3246 1.4959 -0.2343 -0.1381 -0.2012 379 ARG A O 2917 C CB . ARG A 379 ? 1.2898 1.4048 1.5422 -0.2768 -0.1196 -0.0950 379 ARG A CB 2918 C CG . ARG A 379 ? 1.2452 1.2846 1.4588 -0.2930 -0.1166 -0.0480 379 ARG A CG 2919 C CD . ARG A 379 ? 1.3931 1.4807 1.5890 -0.3092 -0.1084 -0.0234 379 ARG A CD 2920 N NE . ARG A 379 ? 1.4955 1.6575 1.6877 -0.3214 -0.0954 -0.0162 379 ARG A NE 2921 C CZ . ARG A 379 ? 1.3570 1.5766 1.5430 -0.3401 -0.0912 0.0117 379 ARG A CZ 2922 N NH1 . ARG A 379 ? 1.2493 1.4562 1.4316 -0.3468 -0.0981 0.0309 379 ARG A NH1 2923 N NH2 . ARG A 379 ? 1.2469 1.5398 1.4343 -0.3539 -0.0823 0.0238 379 ARG A NH2 2924 N N . SER A 380 ? 1.1999 1.4038 1.5661 -0.2276 -0.1526 -0.2097 380 SER A N 2925 C CA . SER A 380 ? 1.1807 1.4814 1.6038 -0.2048 -0.1633 -0.2763 380 SER A CA 2926 C C . SER A 380 ? 1.1386 1.5595 1.5446 -0.2135 -0.1412 -0.2861 380 SER A C 2927 O O . SER A 380 ? 1.0139 1.5153 1.4593 -0.1970 -0.1451 -0.3402 380 SER A O 2928 C CB . SER A 380 ? 1.2018 1.5377 1.6590 -0.1915 -0.1791 -0.3037 380 SER A CB 2929 O OG . SER A 380 ? 1.2594 1.7145 1.7696 -0.1699 -0.1867 -0.3731 380 SER A OG 2930 N N . THR A 381 ? 1.3251 1.7616 1.6778 -0.2404 -0.1208 -0.2328 381 THR A N 2931 C CA . THR A 381 ? 1.1961 1.7548 1.5336 -0.2560 -0.1027 -0.2266 381 THR A CA 2932 C C . THR A 381 ? 1.1991 1.7354 1.5100 -0.2699 -0.0886 -0.2003 381 THR A C 2933 O O . THR A 381 ? 1.0290 1.6588 1.3261 -0.2875 -0.0746 -0.1838 381 THR A O 2934 C CB . THR A 381 ? 1.0728 1.6671 1.3792 -0.2810 -0.0943 -0.1769 381 THR A CB 2935 O OG1 . THR A 381 ? 1.0979 1.5776 1.3645 -0.2996 -0.0899 -0.1175 381 THR A OG1 2936 C CG2 . THR A 381 ? 1.1117 1.7262 1.4411 -0.2683 -0.1073 -0.2000 381 THR A CG2 2937 N N . GLY A 382 ? 1.2363 1.6551 1.5428 -0.2635 -0.0938 -0.1938 382 GLY A N 2938 C CA . GLY A 382 ? 1.0406 1.4196 1.3169 -0.2780 -0.0805 -0.1620 382 GLY A CA 2939 C C . GLY A 382 ? 1.0793 1.3534 1.3138 -0.2963 -0.0762 -0.1037 382 GLY A C 2940 O O . GLY A 382 ? 1.5324 1.7542 1.7631 -0.2949 -0.0850 -0.0922 382 GLY A O 2941 N N . LEU A 383 ? 0.9532 1.2009 1.1599 -0.3125 -0.0640 -0.0705 383 LEU A N 2942 C CA . LEU A 383 ? 0.9765 1.1289 1.1503 -0.3265 -0.0617 -0.0252 383 LEU A CA 2943 C C . LEU A 383 ? 1.1123 1.2758 1.2745 -0.3427 -0.0627 0.0084 383 LEU A C 2944 O O . LEU A 383 ? 1.1904 1.4399 1.3583 -0.3568 -0.0591 0.0222 383 LEU A O 2945 C CB . LEU A 383 ? 0.9284 1.0631 1.0832 -0.3393 -0.0501 -0.0024 383 LEU A CB 2946 C CG . LEU A 383 ? 0.9149 0.9591 1.0421 -0.3508 -0.0490 0.0346 383 LEU A CG 2947 C CD1 . LEU A 383 ? 0.9335 0.8937 1.0557 -0.3377 -0.0575 0.0249 383 LEU A CD1 2948 C CD2 . LEU A 383 ? 0.9569 0.9936 1.0721 -0.3625 -0.0390 0.0535 383 LEU A CD2 2949 N N . ASN A 384 ? 1.1459 1.2281 1.2947 -0.3422 -0.0696 0.0233 384 ASN A N 2950 C CA . ASN A 384 ? 0.9926 1.0703 1.1329 -0.3572 -0.0730 0.0552 384 ASN A CA 2951 C C . ASN A 384 ? 1.0680 1.1352 1.1986 -0.3771 -0.0684 0.0910 384 ASN A C 2952 O O . ASN A 384 ? 1.0287 1.0324 1.1450 -0.3766 -0.0651 0.0959 384 ASN A O 2953 C CB . ASN A 384 ? 0.9952 0.9935 1.1251 -0.3504 -0.0819 0.0571 384 ASN A CB 2954 C CG . ASN A 384 ? 1.0931 1.0954 1.2220 -0.3619 -0.0885 0.0804 384 ASN A CG 2955 O OD1 . ASN A 384 ? 1.1645 1.2083 1.3002 -0.3789 -0.0884 0.1055 384 ASN A OD1 2956 N ND2 . ASN A 384 ? 1.3254 1.2859 1.4505 -0.3542 -0.0969 0.0753 384 ASN A ND2 2957 N N . ALA A 385 ? 1.1440 1.2773 1.2878 -0.3956 -0.0711 0.1176 385 ALA A N 2958 C CA . ALA A 385 ? 0.9729 1.1097 1.1227 -0.4168 -0.0725 0.1546 385 ALA A CA 2959 C C . ALA A 385 ? 0.9935 1.0410 1.1402 -0.4209 -0.0817 0.1724 385 ALA A C 2960 O O . ALA A 385 ? 1.2242 1.2574 1.3828 -0.4347 -0.0866 0.1969 385 ALA A O 2961 C CB . ALA A 385 ? 1.1761 1.4139 1.3500 -0.4392 -0.0790 0.1860 385 ALA A CB 2962 N N . VAL A 386 ? 0.8834 0.8760 1.0184 -0.4084 -0.0859 0.1572 386 VAL A N 2963 C CA . VAL A 386 ? 0.8581 0.7838 0.9937 -0.4111 -0.0962 0.1670 386 VAL A CA 2964 C C . VAL A 386 ? 1.1461 1.0047 1.2548 -0.3954 -0.0899 0.1434 386 VAL A C 2965 O O . VAL A 386 ? 1.6642 1.5168 1.7582 -0.3821 -0.0846 0.1233 386 VAL A O 2966 C CB . VAL A 386 ? 0.9416 0.8717 1.0887 -0.4139 -0.1093 0.1744 386 VAL A CB 2967 C CG1 . VAL A 386 ? 1.0451 0.9145 1.1995 -0.4151 -0.1224 0.1776 386 VAL A CG1 2968 C CG2 . VAL A 386 ? 0.9637 0.9724 1.1392 -0.4326 -0.1173 0.2033 386 VAL A CG2 2969 N N . PRO A 387 ? 0.9508 0.7650 1.0590 -0.3979 -0.0933 0.1462 387 PRO A N 2970 C CA . PRO A 387 ? 1.2317 0.9974 1.3145 -0.3866 -0.0883 0.1277 387 PRO A CA 2971 C C . PRO A 387 ? 1.1335 0.8798 1.2048 -0.3793 -0.0945 0.1179 387 PRO A C 2972 O O . PRO A 387 ? 1.1894 0.9382 1.2756 -0.3833 -0.1059 0.1229 387 PRO A O 2973 C CB . PRO A 387 ? 1.1191 0.8608 1.2140 -0.3920 -0.0939 0.1302 387 PRO A CB 2974 C CG . PRO A 387 ? 1.0347 0.8080 1.1590 -0.4058 -0.0978 0.1526 387 PRO A CG 2975 C CD . PRO A 387 ? 1.0514 0.8704 1.1881 -0.4124 -0.1025 0.1671 387 PRO A CD 2976 N N . SER A 388 ? 1.0320 0.7615 1.0815 -0.3703 -0.0895 0.1071 388 SER A N 2977 C CA . SER A 388 ? 1.0767 0.7923 1.1157 -0.3657 -0.0966 0.1025 388 SER A CA 2978 C C . SER A 388 ? 1.1711 0.8674 1.1941 -0.3663 -0.0979 0.0966 388 SER A C 2979 O O . SER A 388 ? 1.3751 1.0692 1.3880 -0.3649 -0.1042 0.0938 388 SER A O 2980 C CB . SER A 388 ? 1.1631 0.8786 1.1989 -0.3581 -0.0970 0.0989 388 SER A CB 2981 O OG . SER A 388 ? 1.3562 1.0584 1.3830 -0.3565 -0.0917 0.0983 388 SER A OG 2982 N N . GLN A 389 ? 1.1797 0.8711 1.2026 -0.3686 -0.0928 0.0933 389 GLN A N 2983 C CA . GLN A 389 ? 1.3050 0.9926 1.3153 -0.3679 -0.0933 0.0813 389 GLN A CA 2984 C C . GLN A 389 ? 1.2397 0.9233 1.2592 -0.3695 -0.0888 0.0759 389 GLN A C 2985 O O . GLN A 389 ? 0.9630 0.6451 0.9894 -0.3721 -0.0823 0.0862 389 GLN A O 2986 C CB . GLN A 389 ? 1.1286 0.8192 1.1120 -0.3674 -0.0897 0.0859 389 GLN A CB 2987 C CG . GLN A 389 ? 1.1426 0.8525 1.1096 -0.3688 -0.0915 0.0746 389 GLN A CG 2988 C CD . GLN A 389 ? 1.1422 0.8656 1.0869 -0.3739 -0.0910 0.0908 389 GLN A CD 2989 O OE1 . GLN A 389 ? 1.3420 1.0502 1.2901 -0.3749 -0.0924 0.1087 389 GLN A OE1 2990 N NE2 . GLN A 389 ? 1.1527 0.9119 1.0807 -0.3780 -0.0920 0.0842 389 GLN A NE2 2991 N N . ILE A 390 ? 1.0791 0.7677 1.1013 -0.3674 -0.0932 0.0568 390 ILE A N 2992 C CA . ILE A 390 ? 0.9722 0.6582 1.0069 -0.3672 -0.0912 0.0470 390 ILE A CA 2993 C C . ILE A 390 ? 1.1260 0.8325 1.1390 -0.3636 -0.0871 0.0271 390 ILE A C 2994 O O . ILE A 390 ? 1.3052 1.0353 1.3076 -0.3613 -0.0920 0.0134 390 ILE A O 2995 C CB . ILE A 390 ? 0.9845 0.6638 1.0680 -0.3680 -0.1085 0.0377 390 ILE A CB 2996 C CG1 . ILE A 390 ? 1.4409 1.1306 1.5401 -0.3621 -0.1240 0.0122 390 ILE A CG1 2997 C CG2 . ILE A 390 ? 1.0248 0.6987 1.1317 -0.3766 -0.1131 0.0656 390 ILE A CG2 2998 C CD1 . ILE A 390 ? 1.6689 1.3496 1.8300 -0.3615 -0.1482 -0.0017 390 ILE A CD1 2999 N N . LEU A 391 ? 1.0573 0.7635 1.0636 -0.3641 -0.0780 0.0261 391 LEU A N 3000 C CA . LEU A 391 ? 1.1015 0.8390 1.0888 -0.3621 -0.0736 0.0078 391 LEU A CA 3001 C C . LEU A 391 ? 1.0385 0.7794 1.0575 -0.3564 -0.0796 -0.0205 391 LEU A C 3002 O O . LEU A 391 ? 1.0151 0.7308 1.0515 -0.3583 -0.0775 -0.0107 391 LEU A O 3003 C CB . LEU A 391 ? 1.2163 0.9558 1.1704 -0.3680 -0.0600 0.0313 391 LEU A CB 3004 C CG . LEU A 391 ? 1.1170 0.8479 1.0539 -0.3730 -0.0598 0.0593 391 LEU A CG 3005 C CD1 . LEU A 391 ? 1.1893 0.9229 1.1066 -0.3792 -0.0532 0.0809 391 LEU A CD1 3006 C CD2 . LEU A 391 ? 1.2146 0.9725 1.1433 -0.3742 -0.0686 0.0560 391 LEU A CD2 3007 N N . GLU A 392 ? 1.0504 0.8277 1.0817 -0.3490 -0.0891 -0.0580 392 GLU A N 3008 C CA . GLU A 392 ? 1.1015 0.8845 1.1766 -0.3405 -0.1008 -0.0940 392 GLU A CA 3009 C C . GLU A 392 ? 1.0813 0.9096 1.1345 -0.3375 -0.0904 -0.1153 392 GLU A C 3010 O O . GLU A 392 ? 1.0991 0.9775 1.1119 -0.3407 -0.0813 -0.1161 392 GLU A O 3011 C CB . GLU A 392 ? 1.2001 0.9978 1.3209 -0.3307 -0.1241 -0.1329 392 GLU A CB 3012 C CG . GLU A 392 ? 1.3749 1.1364 1.5153 -0.3353 -0.1354 -0.1098 392 GLU A CG 3013 C CD . GLU A 392 ? 1.4838 1.2534 1.6816 -0.3258 -0.1632 -0.1481 392 GLU A CD 3014 O OE1 . GLU A 392 ? 1.5303 1.3108 1.7795 -0.3154 -0.1809 -0.1893 392 GLU A OE1 3015 O OE2 . GLU A 392 ? 1.4525 1.2177 1.6493 -0.3277 -0.1695 -0.1395 392 GLU A OE2 3016 N N . GLY A 393 ? 1.0997 0.9155 1.1820 -0.3335 -0.0932 -0.1289 393 GLY A N 3017 C CA . GLY A 393 ? 1.1180 0.9800 1.1861 -0.3296 -0.0847 -0.1531 393 GLY A CA 3018 C C . GLY A 393 ? 1.2375 1.1687 1.3270 -0.3167 -0.0974 -0.2126 393 GLY A C 3019 O O . GLY A 393 ? 1.6890 1.6129 1.8376 -0.3052 -0.1206 -0.2496 393 GLY A O 3020 N N . GLN A 394 ? 1.2772 1.2837 1.3237 -0.3194 -0.0847 -0.2220 394 GLN A N 3021 C CA . GLN A 394 ? 1.3626 1.4604 1.4223 -0.3082 -0.0942 -0.2812 394 GLN A CA 3022 C C . GLN A 394 ? 1.3669 1.5152 1.4536 -0.2961 -0.0973 -0.3321 394 GLN A C 3023 O O . GLN A 394 ? 1.5258 1.7634 1.6313 -0.2837 -0.1065 -0.3928 394 GLN A O 3024 C CB . GLN A 394 ? 1.5893 1.7626 1.5882 -0.3215 -0.0810 -0.2595 394 GLN A CB 3025 C CG . GLN A 394 ? 1.7292 1.8591 1.7061 -0.3322 -0.0805 -0.2139 394 GLN A CG 3026 C CD . GLN A 394 ? 1.7624 1.9246 1.6804 -0.3526 -0.0662 -0.1596 394 GLN A CD 3027 O OE1 . GLN A 394 ? 1.6913 1.8861 1.5836 -0.3617 -0.0553 -0.1421 394 GLN A OE1 3028 N NE2 . GLN A 394 ? 1.6807 1.8338 1.5828 -0.3609 -0.0694 -0.1305 394 GLN A NE2 3029 N N . TRP A 395 ? 1.3071 1.4051 1.3984 -0.2987 -0.0904 -0.3113 395 TRP A N 3030 C CA . TRP A 395 ? 1.3128 1.4602 1.4216 -0.2893 -0.0900 -0.3526 395 TRP A CA 3031 C C . TRP A 395 ? 1.2599 1.3487 1.4477 -0.2752 -0.1119 -0.3828 395 TRP A C 3032 O O . TRP A 395 ? 1.1456 1.1436 1.3541 -0.2816 -0.1172 -0.3429 395 TRP A O 3033 C CB . TRP A 395 ? 1.2866 1.4405 1.3347 -0.3055 -0.0645 -0.3042 395 TRP A CB 3034 C CG . TRP A 395 ? 1.3306 1.5152 1.3133 -0.3242 -0.0493 -0.2551 395 TRP A CG 3035 C CD1 . TRP A 395 ? 1.3500 1.4652 1.3038 -0.3385 -0.0417 -0.1926 395 TRP A CD1 3036 C CD2 . TRP A 395 ? 1.3543 1.6539 1.3002 -0.3316 -0.0439 -0.2641 395 TRP A CD2 3037 N NE1 . TRP A 395 ? 1.3879 1.5575 1.2948 -0.3539 -0.0346 -0.1608 395 TRP A NE1 3038 C CE2 . TRP A 395 ? 1.4427 1.7278 1.3419 -0.3521 -0.0354 -0.1990 395 TRP A CE2 3039 C CE3 . TRP A 395 ? 1.4681 1.8912 1.4199 -0.3235 -0.0470 -0.3216 395 TRP A CE3 3040 C CZ2 . TRP A 395 ? 1.7501 2.1356 1.6098 -0.3680 -0.0318 -0.1808 395 TRP A CZ2 3041 C CZ3 . TRP A 395 ? 1.7432 2.2774 1.6492 -0.3394 -0.0401 -0.3060 395 TRP A CZ3 3042 C CH2 . TRP A 395 ? 1.8907 2.4035 1.7517 -0.3630 -0.0334 -0.2317 395 TRP A CH2 3043 N N . ALA A 396 ? 1.2733 1.4234 1.5092 -0.2568 -0.1267 -0.4533 396 ALA A N 3044 C CA . ALA A 396 ? 1.1953 1.3001 1.5263 -0.2409 -0.1573 -0.4928 396 ALA A CA 3045 C C . ALA A 396 ? 1.1665 1.2148 1.5023 -0.2476 -0.1501 -0.4598 396 ALA A C 3046 O O . ALA A 396 ? 1.1512 1.1878 1.4161 -0.2641 -0.1208 -0.4057 396 ALA A O 3047 C CB . ALA A 396 ? 1.4520 1.6494 1.8418 -0.2158 -0.1791 -0.5890 396 ALA A CB 3048 N N . ALA A 397 ? 1.2942 1.3096 1.7212 -0.2348 -0.1804 -0.4939 397 ALA A N 3049 C CA . ALA A 397 ? 1.1627 1.1146 1.6090 -0.2426 -0.1801 -0.4581 397 ALA A CA 3050 C C . ALA A 397 ? 1.2436 1.2474 1.6563 -0.2395 -0.1597 -0.4757 397 ALA A C 3051 O O . ALA A 397 ? 1.7444 1.7268 2.0906 -0.2560 -0.1308 -0.4200 397 ALA A O 3052 C CB . ALA A 397 ? 1.4677 1.3690 2.0341 -0.2324 -0.2256 -0.4836 397 ALA A CB 3053 N N . ARG A 398 ? 1.2337 1.3102 1.6969 -0.2175 -0.1767 -0.5563 398 ARG A N 3054 C CA . ARG A 398 ? 1.3609 1.4861 1.8189 -0.2109 -0.1665 -0.5841 398 ARG A CA 3055 C C . ARG A 398 ? 1.1627 1.2008 1.6639 -0.2169 -0.1760 -0.5495 398 ARG A C 3056 O O . ARG A 398 ? 1.2116 1.1832 1.8002 -0.2136 -0.2104 -0.5494 398 ARG A O 3057 C CB . ARG A 398 ? 1.3705 1.5583 1.7165 -0.2264 -0.1239 -0.5493 398 ARG A CB 3058 C CG . ARG A 398 ? 1.7339 2.0408 2.0415 -0.2216 -0.1158 -0.5897 398 ARG A CG 3059 C CD . ARG A 398 ? 1.7975 2.1679 2.0057 -0.2415 -0.0796 -0.5451 398 ARG A CD 3060 N NE . ARG A 398 ? 1.9114 2.4156 2.0861 -0.2405 -0.0736 -0.5801 398 ARG A NE 3061 C CZ . ARG A 398 ? 1.8766 2.4625 1.9735 -0.2599 -0.0486 -0.5438 398 ARG A CZ 3062 N NH1 . ARG A 398 ? 1.8821 2.4210 1.9297 -0.2796 -0.0281 -0.4753 398 ARG A NH1 3063 N NH2 . ARG A 398 ? 1.7445 2.4643 1.8172 -0.2611 -0.0464 -0.5743 398 ARG A NH2 3064 N N . SER A 399 ? 1.2260 1.2684 1.6690 -0.2277 -0.1475 -0.5164 399 SER A N 3065 C CA . SER A 399 ? 1.4917 1.4676 1.9722 -0.2330 -0.1544 -0.4886 399 SER A CA 3066 C C . SER A 399 ? 1.4603 1.3366 1.9464 -0.2530 -0.1584 -0.4127 399 SER A C 3067 O O . SER A 399 ? 1.6304 1.4523 2.2032 -0.2527 -0.1909 -0.4080 399 SER A O 3068 C CB . SER A 399 ? 1.5886 1.5963 1.9964 -0.2414 -0.1202 -0.4677 399 SER A CB 3069 O OG . SER A 399 ? 1.5642 1.5636 1.8732 -0.2623 -0.0858 -0.4028 399 SER A OG 3070 N N . MET A 400 ? 1.2236 1.0840 1.6224 -0.2712 -0.1278 -0.3534 400 MET A N 3071 C CA . MET A 400 ? 1.0811 0.8665 1.4747 -0.2905 -0.1268 -0.2837 400 MET A CA 3072 C C . MET A 400 ? 1.2537 1.0373 1.6126 -0.2957 -0.1219 -0.2657 400 MET A C 3073 O O . MET A 400 ? 1.1850 1.0240 1.5019 -0.2889 -0.1104 -0.2933 400 MET A O 3074 C CB . MET A 400 ? 1.0174 0.7823 1.3449 -0.3068 -0.0953 -0.2292 400 MET A CB 3075 C CG . MET A 400 ? 1.0429 0.8426 1.2735 -0.3133 -0.0608 -0.2105 400 MET A CG 3076 S SD . MET A 400 ? 1.2934 1.0619 1.4625 -0.3312 -0.0309 -0.1493 400 MET A SD 3077 C CE . MET A 400 ? 0.9443 0.6459 1.1398 -0.3454 -0.0404 -0.0969 400 MET A CE 3078 N N . PRO A 401 ? 1.3793 1.1074 1.7567 -0.3092 -0.1314 -0.2179 401 PRO A N 3079 C CA . PRO A 401 ? 1.2423 0.9663 1.5927 -0.3139 -0.1289 -0.2006 401 PRO A CA 3080 C C . PRO A 401 ? 1.0291 0.7864 1.2842 -0.3177 -0.0948 -0.1880 401 PRO A C 3081 O O . PRO A 401 ? 0.9306 0.6874 1.1336 -0.3260 -0.0703 -0.1601 401 PRO A O 3082 C CB . PRO A 401 ? 1.1590 0.8295 1.5245 -0.3327 -0.1338 -0.1386 401 PRO A CB 3083 C CG . PRO A 401 ? 1.4084 1.0635 1.8366 -0.3276 -0.1542 -0.1360 401 PRO A CG 3084 C CD . PRO A 401 ? 1.5749 1.2513 2.0073 -0.3216 -0.1487 -0.1783 401 PRO A CD 3085 N N . PRO A 402 ? 0.9766 0.7641 1.2153 -0.3125 -0.0966 -0.2075 402 PRO A N 3086 C CA . PRO A 402 ? 0.9953 0.8196 1.1545 -0.3182 -0.0711 -0.1925 402 PRO A CA 3087 C C . PRO A 402 ? 0.9848 0.7681 1.0935 -0.3346 -0.0502 -0.1302 402 PRO A C 3088 O O . PRO A 402 ? 0.9641 0.7699 1.0160 -0.3411 -0.0299 -0.1118 402 PRO A O 3089 C CB . PRO A 402 ? 1.0175 0.8593 1.1875 -0.3128 -0.0842 -0.2120 402 PRO A CB 3090 C CG . PRO A 402 ? 1.0763 0.9194 1.3314 -0.2976 -0.1162 -0.2634 402 PRO A CG 3091 C CD . PRO A 402 ? 1.0661 0.8538 1.3695 -0.3021 -0.1272 -0.2424 402 PRO A CD 3092 N N . SER A 403 ? 1.2294 0.9604 1.3652 -0.3417 -0.0581 -0.0993 403 SER A N 3093 C CA . SER A 403 ? 0.9992 0.7000 1.0986 -0.3549 -0.0413 -0.0490 403 SER A CA 3094 C C . SER A 403 ? 0.9208 0.6325 0.9672 -0.3588 -0.0281 -0.0314 403 SER A C 3095 O O . SER A 403 ? 0.8976 0.6001 0.9069 -0.3662 -0.0124 -0.0019 403 SER A O 3096 C CB . SER A 403 ? 0.8961 0.5942 0.9760 -0.3588 -0.0258 -0.0369 403 SER A CB 3097 O OG . SER A 403 ? 1.0526 0.7353 1.1862 -0.3574 -0.0397 -0.0455 403 SER A OG 3098 N N . PHE A 404 ? 0.9537 0.6857 1.0033 -0.3536 -0.0376 -0.0509 404 PHE A N 3099 C CA . PHE A 404 ? 0.9543 0.6962 0.9633 -0.3580 -0.0302 -0.0329 404 PHE A CA 3100 C C . PHE A 404 ? 0.9200 0.6228 0.9249 -0.3656 -0.0266 0.0043 404 PHE A C 3101 O O . PHE A 404 ? 1.0611 0.7429 1.1008 -0.3666 -0.0379 0.0094 404 PHE A O 3102 C CB . PHE A 404 ? 1.0191 0.7884 1.0425 -0.3510 -0.0441 -0.0621 404 PHE A CB 3103 C CG . PHE A 404 ? 1.0456 0.8272 1.0327 -0.3562 -0.0396 -0.0432 404 PHE A CG 3104 C CD1 . PHE A 404 ? 1.1201 0.8704 1.1165 -0.3585 -0.0456 -0.0252 404 PHE A CD1 3105 C CD2 . PHE A 404 ? 1.1714 1.0025 1.1196 -0.3605 -0.0318 -0.0413 404 PHE A CD2 3106 C CE1 . PHE A 404 ? 1.1529 0.9132 1.1214 -0.3625 -0.0438 -0.0091 404 PHE A CE1 3107 C CE2 . PHE A 404 ? 1.1887 1.0317 1.1113 -0.3672 -0.0320 -0.0196 404 PHE A CE2 3108 C CZ . PHE A 404 ? 1.2243 1.0282 1.1578 -0.3671 -0.0380 -0.0054 404 PHE A CZ 3109 N N . GLY A 405 ? 0.9902 0.6902 0.9583 -0.3713 -0.0139 0.0296 405 GLY A N 3110 C CA . GLY A 405 ? 1.0141 0.6888 0.9816 -0.3758 -0.0108 0.0559 405 GLY A CA 3111 C C . GLY A 405 ? 1.1433 0.8038 1.1151 -0.3795 -0.0021 0.0700 405 GLY A C 3112 O O . GLY A 405 ? 1.0981 0.7601 1.0771 -0.3722 0.0014 0.0838 405 GLY A O 3113 N N . TYR A 406 ? 1.2477 0.9117 1.2212 -0.3791 0.0023 0.0613 406 TYR A N 3114 C CA . TYR A 406 ? 0.9707 0.6338 0.9520 -0.3724 0.0113 0.0728 406 TYR A CA 3115 C C . TYR A 406 ? 1.0003 0.6675 0.9579 -0.3666 0.0211 0.0864 406 TYR A C 3116 O O . TYR A 406 ? 1.3157 0.9897 1.2839 -0.3563 0.0269 0.0937 406 TYR A O 3117 C CB . TYR A 406 ? 1.1026 0.7646 1.0893 -0.3773 0.0126 0.0597 406 TYR A CB 3118 C CG . TYR A 406 ? 1.1269 0.7951 1.1327 -0.3643 0.0193 0.0706 406 TYR A CG 3119 C CD1 . TYR A 406 ? 0.8334 0.5055 0.8835 -0.3586 0.0116 0.0753 406 TYR A CD1 3120 C CD2 . TYR A 406 ? 1.0852 0.7589 1.0681 -0.3596 0.0317 0.0781 406 TYR A CD2 3121 C CE1 . TYR A 406 ? 1.0126 0.6965 1.0783 -0.3508 0.0185 0.0868 406 TYR A CE1 3122 C CE2 . TYR A 406 ? 0.9412 0.6234 0.9408 -0.3494 0.0372 0.0860 406 TYR A CE2 3123 C CZ . TYR A 406 ? 1.0670 0.7558 1.1060 -0.3460 0.0314 0.0905 406 TYR A CZ 3124 O OH . TYR A 406 ? 1.0273 0.7299 1.0814 -0.3396 0.0374 0.1003 406 TYR A OH 3125 N N . SER A 407 ? 1.1236 0.7898 1.0543 -0.3760 0.0198 0.0900 407 SER A N 3126 C CA . SER A 407 ? 0.9367 0.6032 0.8588 -0.3712 0.0210 0.1044 407 SER A CA 3127 C C . SER A 407 ? 1.0758 0.7408 0.9879 -0.3800 0.0111 0.1131 407 SER A C 3128 O O . SER A 407 ? 0.9029 0.5818 0.8015 -0.3890 0.0072 0.1094 407 SER A O 3129 C CB . SER A 407 ? 1.1239 0.7971 1.0311 -0.3746 0.0264 0.1110 407 SER A CB 3130 O OG . SER A 407 ? 1.1088 0.7974 0.9915 -0.3947 0.0245 0.1125 407 SER A OG 3131 N N . MET A 408 ? 1.2214 0.8793 1.1467 -0.3724 0.0056 0.1206 408 MET A N 3132 C CA . MET A 408 ? 1.0761 0.7307 1.0012 -0.3788 -0.0074 0.1309 408 MET A CA 3133 C C . MET A 408 ? 0.9718 0.6173 0.9170 -0.3739 -0.0179 0.1419 408 MET A C 3134 O O . MET A 408 ? 1.2670 0.9061 1.2294 -0.3653 -0.0145 0.1336 408 MET A O 3135 C CB . MET A 408 ? 0.8964 0.5463 0.8309 -0.3767 -0.0104 0.1211 408 MET A CB 3136 C CG . MET A 408 ? 0.8957 0.5510 0.8242 -0.3812 -0.0075 0.1094 408 MET A CG 3137 S SD . MET A 408 ? 1.3561 1.0102 1.3029 -0.3774 -0.0142 0.1035 408 MET A SD 3138 C CE . MET A 408 ? 0.8694 0.5299 0.8371 -0.3699 -0.0080 0.1036 408 MET A CE 3139 N N . LYS A 409 ? 0.9726 0.6197 0.9208 -0.3820 -0.0337 0.1607 409 LYS A N 3140 C CA . LYS A 409 ? 1.1150 0.7485 1.0975 -0.3775 -0.0520 0.1698 409 LYS A CA 3141 C C . LYS A 409 ? 1.0112 0.6433 1.0049 -0.3831 -0.0702 0.1817 409 LYS A C 3142 O O . LYS A 409 ? 0.9618 0.6134 0.9356 -0.3965 -0.0745 0.2010 409 LYS A O 3143 C CB . LYS A 409 ? 1.0035 0.6432 0.9939 -0.3805 -0.0599 0.1908 409 LYS A CB 3144 C CG . LYS A 409 ? 1.0387 0.6591 1.0773 -0.3735 -0.0818 0.1942 409 LYS A CG 3145 C CD . LYS A 409 ? 1.3923 0.9956 1.4514 -0.3624 -0.0754 0.1628 409 LYS A CD 3146 C CE . LYS A 409 ? 1.4829 1.0682 1.5986 -0.3561 -0.1019 0.1582 409 LYS A CE 3147 N NZ . LYS A 409 ? 1.6595 1.2381 1.7979 -0.3499 -0.0988 0.1232 409 LYS A NZ 3148 N N . GLY A 410 ? 1.0707 0.6852 1.0970 -0.3754 -0.0818 0.1689 410 GLY A N 3149 C CA . GLY A 410 ? 1.2993 0.9099 1.3445 -0.3781 -0.1016 0.1785 410 GLY A CA 3150 C C . GLY A 410 ? 1.1883 0.7857 1.2869 -0.3731 -0.1306 0.1883 410 GLY A C 3151 O O . GLY A 410 ? 1.2955 0.8919 1.4104 -0.3718 -0.1380 0.1996 410 GLY A O 3152 N N . ALA A 411 ? 1.0213 0.6094 1.1513 -0.3699 -0.1496 0.1839 411 ALA A N 3153 C CA . ALA A 411 ? 1.0000 0.5715 1.1976 -0.3594 -0.1808 0.1770 411 ALA A CA 3154 C C . ALA A 411 ? 1.0270 0.6013 1.2555 -0.3634 -0.2089 0.2149 411 ALA A C 3155 O O . ALA A 411 ? 1.0430 0.6036 1.3365 -0.3534 -0.2405 0.2109 411 ALA A O 3156 C CB . ALA A 411 ? 0.9885 0.5507 1.2145 -0.3484 -0.1791 0.1432 411 ALA A CB 3157 N N . THR A 412 ? 1.0339 0.6324 1.2225 -0.3789 -0.2014 0.2509 412 THR A N 3158 C CA . THR A 412 ? 1.0613 0.6755 1.2786 -0.3883 -0.2308 0.2944 412 THR A CA 3159 C C . THR A 412 ? 1.2694 0.9162 1.4622 -0.4069 -0.2368 0.3298 412 THR A C 3160 O O . THR A 412 ? 1.3636 1.0306 1.5000 -0.4170 -0.2112 0.3266 412 THR A O 3161 C CB . THR A 412 ? 1.0632 0.6933 1.2646 -0.3946 -0.2240 0.3118 412 THR A CB 3162 O OG1 . THR A 412 ? 1.0933 0.6966 1.3088 -0.3789 -0.2134 0.2761 412 THR A OG1 3163 C CG2 . THR A 412 ? 1.0942 0.7423 1.3398 -0.4040 -0.2617 0.3575 412 THR A CG2 3164 N N . ASP A 413 ? 1.2723 0.9279 1.5121 -0.4123 -0.2735 0.3636 413 ASP A N 3165 C CA . ASP A 413 ? 1.1158 0.8090 1.3390 -0.4318 -0.2835 0.4001 413 ASP A CA 3166 C C . ASP A 413 ? 1.1654 0.9147 1.3781 -0.4551 -0.2962 0.4519 413 ASP A C 3167 O O . ASP A 413 ? 1.1609 0.9188 1.4276 -0.4587 -0.3327 0.4858 413 ASP A O 3168 C CB . ASP A 413 ? 1.1334 0.8077 1.4190 -0.4245 -0.3188 0.4065 413 ASP A CB 3169 C CG . ASP A 413 ? 1.4603 1.1708 1.7278 -0.4433 -0.3269 0.4386 413 ASP A CG 3170 O OD1 . ASP A 413 ? 1.6714 1.4104 1.8741 -0.4565 -0.2979 0.4363 413 ASP A OD1 3171 O OD2 . ASP A 413 ? 1.1694 0.8825 1.4918 -0.4452 -0.3645 0.4655 413 ASP A OD2 3172 N N . ILE A 414 ? 1.1274 0.9224 1.2752 -0.4724 -0.2693 0.4584 414 ILE A N 3173 C CA . ILE A 414 ? 1.1724 1.0325 1.3030 -0.4945 -0.2748 0.4993 414 ILE A CA 3174 C C . ILE A 414 ? 1.1685 1.0976 1.3052 -0.5202 -0.3009 0.5509 414 ILE A C 3175 O O . ILE A 414 ? 1.2093 1.2058 1.3480 -0.5411 -0.3172 0.5946 414 ILE A O 3176 C CB . ILE A 414 ? 1.1900 1.0798 1.2522 -0.5021 -0.2352 0.4783 414 ILE A CB 3177 C CG1 . ILE A 414 ? 1.1453 1.0967 1.1978 -0.5190 -0.2403 0.5116 414 ILE A CG1 3178 C CG2 . ILE A 414 ? 1.1675 1.0973 1.1824 -0.5176 -0.2176 0.4721 414 ILE A CG2 3179 C CD1 . ILE A 414 ? 1.2769 1.2652 1.2683 -0.5270 -0.2043 0.4898 414 ILE A CD1 3180 N N . ASP A 415 ? 1.1693 1.0872 1.3109 -0.5193 -0.3058 0.5464 415 ASP A N 3181 C CA . ASP A 415 ? 1.1945 1.1735 1.3501 -0.5418 -0.3338 0.5945 415 ASP A CA 3182 C C . ASP A 415 ? 1.2300 1.1520 1.4549 -0.5258 -0.3670 0.5959 415 ASP A C 3183 O O . ASP A 415 ? 1.5504 1.3974 1.7989 -0.4989 -0.3608 0.5529 415 ASP A O 3184 C CB . ASP A 415 ? 1.2061 1.2382 1.3000 -0.5589 -0.3085 0.5882 415 ASP A CB 3185 C CG . ASP A 415 ? 1.4090 1.3739 1.4867 -0.5401 -0.2850 0.5370 415 ASP A CG 3186 O OD1 . ASP A 415 ? 1.4818 1.3692 1.5790 -0.5138 -0.2769 0.4983 415 ASP A OD1 3187 O OD2 . ASP A 415 ? 1.4623 1.4603 1.5087 -0.5531 -0.2753 0.5353 415 ASP A OD2 3188 N N . LYS A 416 ? 1.2341 1.1983 1.4961 -0.5426 -0.4042 0.6442 416 LYS A N 3189 C CA . LYS A 416 ? 1.4415 1.3552 1.7820 -0.5275 -0.4426 0.6480 416 LYS A CA 3190 C C . LYS A 416 ? 1.6742 1.5544 2.0044 -0.5170 -0.4312 0.6183 416 LYS A C 3191 O O . LYS A 416 ? 2.0031 1.8503 2.3958 -0.5057 -0.4626 0.6202 416 LYS A O 3192 C CB . LYS A 416 ? 1.8469 1.8184 2.2467 -0.5500 -0.4952 0.7164 416 LYS A CB 3193 C CG . LYS A 416 ? 2.0375 2.0319 2.4706 -0.5573 -0.5174 0.7463 416 LYS A CG 3194 C CD . LYS A 416 ? 1.7925 1.7020 2.2604 -0.5255 -0.5137 0.7003 416 LYS A CD 3195 C CE . LYS A 416 ? 1.8423 1.6907 2.3996 -0.5029 -0.5520 0.6864 416 LYS A CE 3196 N NZ . LYS A 416 ? 1.7450 1.6315 2.3877 -0.5197 -0.6150 0.7493 416 LYS A NZ 3197 N N . ASN A 417 ? 1.3931 1.2834 1.6491 -0.5205 -0.3886 0.5897 417 ASN A N 3198 C CA . ASN A 417 ? 1.5003 1.3689 1.7394 -0.5150 -0.3764 0.5645 417 ASN A CA 3199 C C . ASN A 417 ? 1.5214 1.3091 1.8104 -0.4839 -0.3843 0.5221 417 ASN A C 3200 O O . ASN A 417 ? 1.6652 1.4362 1.9615 -0.4788 -0.3873 0.5097 417 ASN A O 3201 C CB . ASN A 417 ? 1.4808 1.3651 1.6399 -0.5211 -0.3301 0.5323 417 ASN A CB 3202 C CG . ASN A 417 ? 1.5530 1.3877 1.6929 -0.5013 -0.3004 0.4841 417 ASN A CG 3203 O OD1 . ASN A 417 ? 1.8224 1.6173 2.0023 -0.4838 -0.3107 0.4744 417 ASN A OD1 3204 N ND2 . ASN A 417 ? 1.3426 1.1842 1.4244 -0.5053 -0.2654 0.4536 417 ASN A ND2 3205 N N . GLY A 418 ? 1.1881 0.9333 1.5126 -0.4640 -0.3883 0.4985 418 GLY A N 3206 C CA . GLY A 418 ? 1.1824 0.8673 1.5625 -0.4356 -0.3996 0.4563 418 GLY A CA 3207 C C . GLY A 418 ? 1.3345 0.9863 1.6734 -0.4194 -0.3594 0.3973 418 GLY A C 3208 O O . GLY A 418 ? 1.1929 0.8072 1.5691 -0.3976 -0.3636 0.3559 418 GLY A O 3209 N N . TYR A 419 ? 1.1313 0.8044 1.3975 -0.4311 -0.3232 0.3934 419 TYR A N 3210 C CA . TYR A 419 ? 1.1014 0.7499 1.3295 -0.4189 -0.2876 0.3438 419 TYR A CA 3211 C C . TYR A 419 ? 1.0896 0.7438 1.2853 -0.4201 -0.2648 0.3373 419 TYR A C 3212 O O . TYR A 419 ? 1.0987 0.7916 1.2663 -0.4384 -0.2623 0.3702 419 TYR A O 3213 C CB . TYR A 419 ? 1.3718 1.0366 1.5466 -0.4301 -0.2663 0.3376 419 TYR A CB 3214 C CG . TYR A 419 ? 1.1944 0.8497 1.3967 -0.4269 -0.2843 0.3372 419 TYR A CG 3215 C CD1 . TYR A 419 ? 1.2273 0.9070 1.4562 -0.4398 -0.3139 0.3806 419 TYR A CD1 3216 C CD2 . TYR A 419 ? 1.0825 0.7140 1.2837 -0.4096 -0.2715 0.2939 419 TYR A CD2 3217 C CE1 . TYR A 419 ? 1.2866 0.9573 1.5423 -0.4366 -0.3310 0.3804 419 TYR A CE1 3218 C CE2 . TYR A 419 ? 1.3121 0.9391 1.5376 -0.4047 -0.2869 0.2912 419 TYR A CE2 3219 C CZ . TYR A 419 ? 1.3688 1.0087 1.6234 -0.4208 -0.3179 0.3356 419 TYR A CZ 3220 O OH . TYR A 419 ? 1.3471 0.9802 1.6287 -0.4176 -0.3349 0.3345 419 TYR A OH 3221 N N . PRO A 420 ? 1.0828 0.7059 1.2826 -0.4023 -0.2486 0.2948 420 PRO A N 3222 C CA . PRO A 420 ? 1.0564 0.6809 1.2289 -0.4011 -0.2267 0.2847 420 PRO A CA 3223 C C . PRO A 420 ? 1.0676 0.7163 1.1712 -0.4145 -0.1956 0.2830 420 PRO A C 3224 O O . PRO A 420 ? 1.1927 0.8430 1.2719 -0.4152 -0.1839 0.2674 420 PRO A O 3225 C CB . PRO A 420 ? 1.0389 0.6315 1.2381 -0.3808 -0.2207 0.2384 420 PRO A CB 3226 C CG . PRO A 420 ? 1.0494 0.6334 1.2595 -0.3758 -0.2247 0.2186 420 PRO A CG 3227 C CD . PRO A 420 ? 1.3018 0.8951 1.5337 -0.3840 -0.2513 0.2535 420 PRO A CD 3228 N N . ASP A 421 ? 1.1050 0.7752 1.1815 -0.4234 -0.1840 0.2958 421 ASP A N 3229 C CA . ASP A 421 ? 1.1419 0.8426 1.1609 -0.4378 -0.1596 0.2929 421 ASP A CA 3230 C C . ASP A 421 ? 1.2764 0.9630 1.2749 -0.4262 -0.1337 0.2618 421 ASP A C 3231 O O . ASP A 421 ? 1.1139 0.7688 1.1395 -0.4112 -0.1343 0.2454 421 ASP A O 3232 C CB . ASP A 421 ? 1.1037 0.8610 1.1070 -0.4632 -0.1695 0.3366 421 ASP A CB 3233 C CG . ASP A 421 ? 1.4747 1.2501 1.5103 -0.4719 -0.2005 0.3738 421 ASP A CG 3234 O OD1 . ASP A 421 ? 1.5186 1.3134 1.5396 -0.4802 -0.2011 0.3760 421 ASP A OD1 3235 O OD2 . ASP A 421 ? 1.7112 1.4828 1.7913 -0.4683 -0.2262 0.3991 421 ASP A OD2 3236 N N . LEU A 422 ? 1.3027 1.0204 1.2585 -0.4278 -0.1117 0.2480 422 LEU A N 3237 C CA . LEU A 422 ? 0.9868 0.6896 0.9280 -0.4163 -0.0889 0.2175 422 LEU A CA 3238 C C . LEU A 422 ? 1.0087 0.7491 0.9185 -0.4239 -0.0750 0.2166 422 LEU A C 3239 O O . LEU A 422 ? 1.2295 1.0192 1.1173 -0.4317 -0.0737 0.2181 422 LEU A O 3240 C CB . LEU A 422 ? 0.9746 0.6652 0.9105 -0.4024 -0.0767 0.1846 422 LEU A CB 3241 C CG . LEU A 422 ? 0.9517 0.6329 0.8784 -0.3937 -0.0572 0.1582 422 LEU A CG 3242 C CD1 . LEU A 422 ? 0.9411 0.5955 0.8873 -0.3880 -0.0550 0.1558 422 LEU A CD1 3243 C CD2 . LEU A 422 ? 1.1358 0.8144 1.0637 -0.3856 -0.0521 0.1361 422 LEU A CD2 3244 N N . ILE A 423 ? 0.9774 0.7011 0.8874 -0.4206 -0.0650 0.2102 423 ILE A N 3245 C CA . ILE A 423 ? 1.0747 0.8313 0.9591 -0.4246 -0.0507 0.2024 423 ILE A CA 3246 C C . ILE A 423 ? 1.0404 0.7772 0.9209 -0.4104 -0.0329 0.1658 423 ILE A C 3247 O O . ILE A 423 ? 1.2769 0.9745 1.1738 -0.4019 -0.0294 0.1579 423 ILE A O 3248 C CB . ILE A 423 ? 1.1601 0.9174 1.0492 -0.4347 -0.0545 0.2279 423 ILE A CB 3249 C CG1 . ILE A 423 ? 1.0307 0.7964 0.9418 -0.4506 -0.0804 0.2722 423 ILE A CG1 3250 C CG2 . ILE A 423 ? 0.9822 0.7889 0.8431 -0.4409 -0.0415 0.2221 423 ILE A CG2 3251 C CD1 . ILE A 423 ? 1.1672 0.9305 1.0995 -0.4442 -0.0883 0.2894 423 ILE A CD1 3252 N N . VAL A 424 ? 1.0036 0.7747 0.8686 -0.4086 -0.0245 0.1433 424 VAL A N 3253 C CA . VAL A 424 ? 0.9402 0.6946 0.8126 -0.3975 -0.0137 0.1126 424 VAL A CA 3254 C C . VAL A 424 ? 0.9901 0.7768 0.8514 -0.3988 -0.0053 0.0995 424 VAL A C 3255 O O . VAL A 424 ? 1.0373 0.8811 0.8838 -0.4036 -0.0067 0.0930 424 VAL A O 3256 C CB . VAL A 424 ? 1.0137 0.7720 0.8964 -0.3897 -0.0176 0.0874 424 VAL A CB 3257 C CG1 . VAL A 424 ? 0.9822 0.7256 0.8850 -0.3812 -0.0135 0.0611 424 VAL A CG1 3258 C CG2 . VAL A 424 ? 0.9806 0.7093 0.8747 -0.3879 -0.0249 0.0989 424 VAL A CG2 3259 N N . GLY A 425 ? 0.9289 0.6876 0.7981 -0.3951 0.0032 0.0950 425 GLY A N 3260 C CA . GLY A 425 ? 1.0112 0.7967 0.8744 -0.3948 0.0108 0.0800 425 GLY A CA 3261 C C . GLY A 425 ? 1.1881 0.9757 1.0738 -0.3837 0.0100 0.0420 425 GLY A C 3262 O O . GLY A 425 ? 1.3154 1.0679 1.2253 -0.3783 0.0052 0.0361 425 GLY A O 3263 N N . ALA A 426 ? 1.2343 1.0677 1.1185 -0.3808 0.0117 0.0162 426 ALA A N 3264 C CA . ALA A 426 ? 1.1000 0.9381 1.0191 -0.3685 0.0047 -0.0260 426 ALA A CA 3265 C C . ALA A 426 ? 1.1602 0.9902 1.0917 -0.3659 0.0103 -0.0352 426 ALA A C 3266 O O . ALA A 426 ? 1.8344 1.6199 1.7978 -0.3625 0.0063 -0.0359 426 ALA A O 3267 C CB . ALA A 426 ? 1.0833 0.9915 1.0033 -0.3628 -0.0024 -0.0631 426 ALA A CB 3268 N N . PHE A 427 ? 1.1112 0.9926 1.0200 -0.3688 0.0179 -0.0411 427 PHE A N 3269 C CA . PHE A 427 ? 1.2756 1.1556 1.1864 -0.3686 0.0259 -0.0438 427 PHE A CA 3270 C C . PHE A 427 ? 1.2003 1.0860 1.1582 -0.3543 0.0159 -0.0913 427 PHE A C 3271 O O . PHE A 427 ? 1.2796 1.1859 1.2423 -0.3516 0.0202 -0.1065 427 PHE A O 3272 C CB . PHE A 427 ? 1.1335 0.9489 1.0378 -0.3761 0.0341 -0.0036 427 PHE A CB 3273 C CG . PHE A 427 ? 1.0639 0.8315 1.0069 -0.3708 0.0302 -0.0100 427 PHE A CG 3274 C CD1 . PHE A 427 ? 1.1821 0.9530 1.1439 -0.3670 0.0314 -0.0265 427 PHE A CD1 3275 C CD2 . PHE A 427 ? 0.8873 0.6121 0.8487 -0.3723 0.0245 0.0063 427 PHE A CD2 3276 C CE1 . PHE A 427 ? 1.0399 0.7711 1.0422 -0.3658 0.0244 -0.0246 427 PHE A CE1 3277 C CE2 . PHE A 427 ? 0.8770 0.5707 0.8761 -0.3725 0.0185 0.0096 427 PHE A CE2 3278 C CZ . PHE A 427 ? 0.9034 0.5987 0.9242 -0.3700 0.0175 -0.0036 427 PHE A CZ 3279 N N . GLY A 428 ? 1.0292 0.8993 1.0279 -0.3451 -0.0006 -0.1157 428 GLY A N 3280 C CA . GLY A 428 ? 1.0375 0.9182 1.0955 -0.3304 -0.0183 -0.1658 428 GLY A CA 3281 C C . GLY A 428 ? 1.1427 1.1142 1.1954 -0.3209 -0.0207 -0.2155 428 GLY A C 3282 O O . GLY A 428 ? 1.2860 1.2995 1.3655 -0.3100 -0.0258 -0.2591 428 GLY A O 3283 N N . VAL A 429 ? 1.1481 1.1580 1.1677 -0.3255 -0.0177 -0.2095 429 VAL A N 3284 C CA . VAL A 429 ? 1.2201 1.3356 1.2253 -0.3209 -0.0179 -0.2492 429 VAL A CA 3285 C C . VAL A 429 ? 1.3548 1.5249 1.2955 -0.3388 0.0018 -0.2099 429 VAL A C 3286 O O . VAL A 429 ? 1.4646 1.7384 1.3830 -0.3419 0.0039 -0.2281 429 VAL A O 3287 C CB . VAL A 429 ? 1.2659 1.4032 1.2776 -0.3172 -0.0292 -0.2652 429 VAL A CB 3288 C CG1 . VAL A 429 ? 1.1239 1.2061 1.2072 -0.3015 -0.0532 -0.2996 429 VAL A CG1 3289 C CG2 . VAL A 429 ? 1.3431 1.4418 1.3081 -0.3349 -0.0192 -0.2017 429 VAL A CG2 3290 N N . ASP A 430 ? 1.5680 1.6739 1.4840 -0.3517 0.0136 -0.1552 430 ASP A N 3291 C CA . ASP A 430 ? 1.3171 1.4574 1.1831 -0.3707 0.0271 -0.1089 430 ASP A CA 3292 C C . ASP A 430 ? 1.2360 1.4244 1.0701 -0.3848 0.0251 -0.0803 430 ASP A C 3293 O O . ASP A 430 ? 1.2522 1.5371 1.0594 -0.3969 0.0277 -0.0728 430 ASP A O 3294 C CB . ASP A 430 ? 1.2750 1.4995 1.1342 -0.3699 0.0333 -0.1349 430 ASP A CB 3295 C CG . ASP A 430 ? 1.3070 1.4834 1.1997 -0.3573 0.0340 -0.1593 430 ASP A CG 3296 O OD1 . ASP A 430 ? 1.5679 1.6795 1.5057 -0.3438 0.0229 -0.1820 430 ASP A OD1 3297 O OD2 . ASP A 430 ? 1.3113 1.5167 1.1882 -0.3628 0.0437 -0.1519 430 ASP A OD2 3298 N N . ARG A 431 ? 1.2018 1.3295 1.0416 -0.3848 0.0190 -0.0619 431 ARG A N 3299 C CA . ARG A 431 ? 1.1733 1.3372 0.9896 -0.3978 0.0143 -0.0333 431 ARG A CA 3300 C C . ARG A 431 ? 1.1925 1.2686 1.0055 -0.4054 0.0121 0.0159 431 ARG A C 3301 O O . ARG A 431 ? 1.0503 1.0431 0.8815 -0.3977 0.0142 0.0183 431 ARG A O 3302 C CB . ARG A 431 ? 1.2202 1.4309 1.0534 -0.3860 0.0046 -0.0803 431 ARG A CB 3303 C CG . ARG A 431 ? 1.2722 1.5901 1.1146 -0.3764 0.0035 -0.1391 431 ARG A CG 3304 C CD . ARG A 431 ? 1.2204 1.5825 1.0876 -0.3624 -0.0091 -0.1917 431 ARG A CD 3305 N NE . ARG A 431 ? 1.2713 1.7655 1.1102 -0.3733 -0.0091 -0.1971 431 ARG A NE 3306 C CZ . ARG A 431 ? 1.4985 2.1158 1.3358 -0.3702 -0.0072 -0.2403 431 ARG A CZ 3307 N NH1 . ARG A 431 ? 1.5640 2.1790 1.4289 -0.3544 -0.0059 -0.2840 431 ARG A NH1 3308 N NH2 . ARG A 431 ? 1.7117 2.4626 1.5217 -0.3836 -0.0075 -0.2396 431 ARG A NH2 3309 N N . ALA A 432 ? 1.1000 1.2038 0.8941 -0.4212 0.0059 0.0546 432 ALA A N 3310 C CA . ALA A 432 ? 1.0639 1.0949 0.8628 -0.4263 -0.0005 0.0938 432 ALA A CA 3311 C C . ALA A 432 ? 1.1600 1.2262 0.9539 -0.4328 -0.0114 0.1038 432 ALA A C 3312 O O . ALA A 432 ? 1.1281 1.2850 0.9048 -0.4458 -0.0154 0.1122 432 ALA A O 3313 C CB . ALA A 432 ? 1.2396 1.2509 1.0323 -0.4417 -0.0024 0.1437 432 ALA A CB 3314 N N . ILE A 433 ? 1.0808 1.0835 0.8897 -0.4249 -0.0165 0.1036 433 ILE A N 3315 C CA . ILE A 433 ? 1.1706 1.1997 0.9775 -0.4285 -0.0267 0.1081 433 ILE A CA 3316 C C . ILE A 433 ? 1.1262 1.1039 0.9413 -0.4371 -0.0377 0.1529 433 ILE A C 3317 O O . ILE A 433 ? 1.0572 0.9599 0.8887 -0.4294 -0.0365 0.1573 433 ILE A O 3318 C CB . ILE A 433 ? 1.2408 1.2515 1.0651 -0.4102 -0.0269 0.0609 433 ILE A CB 3319 C CG1 . ILE A 433 ? 1.2569 1.3007 1.0916 -0.3975 -0.0212 0.0100 433 ILE A CG1 3320 C CG2 . ILE A 433 ? 1.2974 1.3533 1.1163 -0.4141 -0.0366 0.0596 433 ILE A CG2 3321 C CD1 . ILE A 433 ? 1.5493 1.7062 1.3663 -0.4035 -0.0208 -0.0083 433 ILE A CD1 3322 N N . LEU A 434 ? 1.1056 1.1316 0.9137 -0.4531 -0.0506 0.1844 434 LEU A N 3323 C CA . LEU A 434 ? 1.1564 1.1386 0.9826 -0.4610 -0.0669 0.2251 434 LEU A CA 3324 C C . LEU A 434 ? 1.1752 1.1608 1.0047 -0.4575 -0.0744 0.2174 434 LEU A C 3325 O O . LEU A 434 ? 1.1759 1.2370 0.9903 -0.4668 -0.0783 0.2179 434 LEU A O 3326 C CB . LEU A 434 ? 1.0898 1.1167 0.9182 -0.4866 -0.0833 0.2817 434 LEU A CB 3327 C CG . LEU A 434 ? 1.0860 1.0861 0.9435 -0.4985 -0.1089 0.3273 434 LEU A CG 3328 C CD1 . LEU A 434 ? 1.0524 0.9528 0.9427 -0.4823 -0.1130 0.3196 434 LEU A CD1 3329 C CD2 . LEU A 434 ? 1.1844 1.2380 1.0520 -0.5278 -0.1298 0.3888 434 LEU A CD2 3330 N N . TYR A 435 ? 1.0842 0.9958 0.9337 -0.4445 -0.0765 0.2093 435 TYR A N 3331 C CA . TYR A 435 ? 1.1575 1.0639 1.0132 -0.4408 -0.0844 0.2044 435 TYR A CA 3332 C C . TYR A 435 ? 1.1215 1.0031 1.0009 -0.4507 -0.1054 0.2465 435 TYR A C 3333 O O . TYR A 435 ? 1.0605 0.8843 0.9654 -0.4451 -0.1108 0.2543 435 TYR A O 3334 C CB . TYR A 435 ? 1.2862 1.1387 1.1522 -0.4206 -0.0749 0.1662 435 TYR A CB 3335 C CG . TYR A 435 ? 1.1804 1.0534 1.0384 -0.4106 -0.0621 0.1241 435 TYR A CG 3336 C CD1 . TYR A 435 ? 1.2973 1.2147 1.1509 -0.4069 -0.0642 0.0963 435 TYR A CD1 3337 C CD2 . TYR A 435 ? 1.1090 0.9585 0.9707 -0.4042 -0.0511 0.1100 435 TYR A CD2 3338 C CE1 . TYR A 435 ? 1.2965 1.2318 1.1570 -0.3957 -0.0586 0.0524 435 TYR A CE1 3339 C CE2 . TYR A 435 ? 1.2693 1.1351 1.1353 -0.3947 -0.0447 0.0712 435 TYR A CE2 3340 C CZ . TYR A 435 ? 1.1856 1.0930 1.0546 -0.3897 -0.0500 0.0409 435 TYR A CZ 3341 O OH . TYR A 435 ? 1.1557 1.0781 1.0426 -0.3782 -0.0495 -0.0030 435 TYR A OH 3342 N N . ARG A 436 ? 1.1655 1.0960 1.0419 -0.4651 -0.1196 0.2714 436 ARG A N 3343 C CA . ARG A 436 ? 1.1247 1.0338 1.0329 -0.4755 -0.1451 0.3130 436 ARG A CA 3344 C C . ARG A 436 ? 1.1940 1.0608 1.1159 -0.4610 -0.1480 0.2930 436 ARG A C 3345 O O . ARG A 436 ? 1.4466 1.3373 1.3481 -0.4549 -0.1383 0.2668 436 ARG A O 3346 C CB . ARG A 436 ? 1.1471 1.1373 1.0505 -0.5031 -0.1630 0.3603 436 ARG A CB 3347 C CG . ARG A 436 ? 1.2172 1.2569 1.1152 -0.5231 -0.1668 0.3941 436 ARG A CG 3348 C CD . ARG A 436 ? 1.3740 1.5120 1.2680 -0.5544 -0.1860 0.4462 436 ARG A CD 3349 N NE . ARG A 436 ? 1.5435 1.7566 1.4015 -0.5528 -0.1728 0.4165 436 ARG A NE 3350 C CZ . ARG A 436 ? 1.6219 1.9350 1.4710 -0.5775 -0.1862 0.4514 436 ARG A CZ 3351 N NH1 . ARG A 436 ? 1.6396 1.9876 1.5153 -0.6088 -0.2153 0.5251 436 ARG A NH1 3352 N NH2 . ARG A 436 ? 1.5912 1.9740 1.4102 -0.5721 -0.1733 0.4136 436 ARG A NH2 3353 N N . ALA A 437 ? 1.2474 1.0557 1.2086 -0.4546 -0.1630 0.3024 437 ALA A N 3354 C CA . ALA A 437 ? 1.1540 0.9285 1.1324 -0.4415 -0.1677 0.2852 437 ALA A CA 3355 C C . ALA A 437 ? 1.3061 1.1146 1.2910 -0.4560 -0.1878 0.3158 437 ALA A C 3356 O O . ALA A 437 ? 1.3217 1.1537 1.3274 -0.4760 -0.2113 0.3623 437 ALA A O 3357 C CB . ALA A 437 ? 1.0629 0.7788 1.0863 -0.4287 -0.1792 0.2790 437 ALA A CB 3358 N N . ARG A 438 ? 1.2357 1.0498 1.2062 -0.4479 -0.1808 0.2930 438 ARG A N 3359 C CA . ARG A 438 ? 1.1925 1.0377 1.1691 -0.4602 -0.1989 0.3187 438 ARG A CA 3360 C C . ARG A 438 ? 1.1463 0.9384 1.1707 -0.4522 -0.2201 0.3257 438 ARG A C 3361 O O . ARG A 438 ? 1.1094 0.8527 1.1489 -0.4321 -0.2123 0.2933 438 ARG A O 3362 C CB . ARG A 438 ? 1.4238 1.3048 1.3652 -0.4549 -0.1830 0.2881 438 ARG A CB 3363 C CG . ARG A 438 ? 1.5738 1.4986 1.4786 -0.4536 -0.1614 0.2605 438 ARG A CG 3364 C CD . ARG A 438 ? 1.5904 1.5720 1.4712 -0.4529 -0.1553 0.2350 438 ARG A CD 3365 N NE . ARG A 438 ? 1.5491 1.4921 1.4407 -0.4397 -0.1568 0.2150 438 ARG A NE 3366 C CZ . ARG A 438 ? 1.3441 1.3233 1.2237 -0.4362 -0.1548 0.1899 438 ARG A CZ 3367 N NH1 . ARG A 438 ? 1.2135 1.1545 1.1055 -0.4254 -0.1576 0.1760 438 ARG A NH1 3368 N NH2 . ARG A 438 ? 1.5248 1.5852 1.3824 -0.4433 -0.1510 0.1761 438 ARG A NH2 3369 N N . PRO A 439 ? 1.1508 0.9602 1.2037 -0.4687 -0.2491 0.3682 439 PRO A N 3370 C CA . PRO A 439 ? 1.1548 0.9180 1.2623 -0.4605 -0.2742 0.3724 439 PRO A CA 3371 C C . PRO A 439 ? 1.2563 1.0033 1.3517 -0.4423 -0.2612 0.3342 439 PRO A C 3372 O O . PRO A 439 ? 1.1496 0.9311 1.2016 -0.4443 -0.2440 0.3222 439 PRO A O 3373 C CB . PRO A 439 ? 1.1666 0.9658 1.3034 -0.4876 -0.3089 0.4333 439 PRO A CB 3374 C CG . PRO A 439 ? 1.2263 1.1063 1.3074 -0.5079 -0.2940 0.4510 439 PRO A CG 3375 C CD . PRO A 439 ? 1.1771 1.0581 1.2190 -0.4979 -0.2630 0.4174 439 PRO A CD 3376 N N . VAL A 440 ? 1.3937 1.0945 1.5318 -0.4244 -0.2713 0.3130 440 VAL A N 3377 C CA . VAL A 440 ? 1.2813 0.9702 1.4124 -0.4074 -0.2599 0.2778 440 VAL A CA 3378 C C . VAL A 440 ? 1.4030 1.0868 1.5738 -0.4092 -0.2878 0.2941 440 VAL A C 3379 O O . VAL A 440 ? 1.3115 0.9723 1.5437 -0.4084 -0.3185 0.3083 440 VAL A O 3380 C CB . VAL A 440 ? 1.1791 0.8375 1.3260 -0.3847 -0.2474 0.2351 440 VAL A CB 3381 C CG1 . VAL A 440 ? 1.1404 0.7956 1.2925 -0.3700 -0.2428 0.2063 440 VAL A CG1 3382 C CG2 . VAL A 440 ? 1.2838 0.9488 1.3883 -0.3829 -0.2179 0.2177 440 VAL A CG2 3383 N N . ILE A 441 ? 1.4155 1.1201 1.5571 -0.4110 -0.2797 0.2903 441 ILE A N 3384 C CA . ILE A 441 ? 1.2853 0.9871 1.4595 -0.4123 -0.3035 0.3038 441 ILE A CA 3385 C C . ILE A 441 ? 1.1977 0.8821 1.3743 -0.3910 -0.2923 0.2622 441 ILE A C 3386 O O . ILE A 441 ? 1.2347 0.9308 1.3673 -0.3859 -0.2662 0.2386 441 ILE A O 3387 C CB . ILE A 441 ? 1.2177 0.9671 1.3609 -0.4335 -0.3072 0.3366 441 ILE A CB 3388 C CG1 . ILE A 441 ? 1.3579 1.1472 1.4911 -0.4582 -0.3152 0.3797 441 ILE A CG1 3389 C CG2 . ILE A 441 ? 1.2641 1.0092 1.4476 -0.4373 -0.3358 0.3574 441 ILE A CG2 3390 C CD1 . ILE A 441 ? 1.2325 1.0905 1.3356 -0.4810 -0.3191 0.4113 441 ILE A CD1 3391 N N . THR A 442 ? 1.3257 0.9867 1.5599 -0.3790 -0.3151 0.2529 442 THR A N 3392 C CA . THR A 442 ? 1.3829 1.0406 1.6239 -0.3606 -0.3078 0.2165 442 THR A CA 3393 C C . THR A 442 ? 1.4126 1.0771 1.6659 -0.3668 -0.3261 0.2351 442 THR A C 3394 O O . THR A 442 ? 1.1589 0.8121 1.4673 -0.3709 -0.3600 0.2574 442 THR A O 3395 C CB . THR A 442 ? 1.4483 1.0904 1.7474 -0.3393 -0.3195 0.1817 442 THR A CB 3396 O OG1 . THR A 442 ? 1.6809 1.3040 2.0512 -0.3408 -0.3600 0.2001 442 THR A OG1 3397 C CG2 . THR A 442 ? 1.3860 1.0266 1.6720 -0.3336 -0.3007 0.1629 442 THR A CG2 3398 N N . VAL A 443 ? 1.5584 1.2410 1.7660 -0.3680 -0.3066 0.2269 443 VAL A N 3399 C CA . VAL A 443 ? 1.4459 1.1405 1.6548 -0.3760 -0.3202 0.2456 443 VAL A CA 3400 C C . VAL A 443 ? 1.5551 1.2478 1.7705 -0.3598 -0.3146 0.2143 443 VAL A C 3401 O O . VAL A 443 ? 1.8327 1.5316 2.0203 -0.3508 -0.2902 0.1860 443 VAL A O 3402 C CB . VAL A 443 ? 1.4564 1.1854 1.6086 -0.3941 -0.3066 0.2653 443 VAL A CB 3403 C CG1 . VAL A 443 ? 1.7138 1.4494 1.8189 -0.3869 -0.2743 0.2332 443 VAL A CG1 3404 C CG2 . VAL A 443 ? 1.3710 1.1188 1.5217 -0.4018 -0.3187 0.2809 443 VAL A CG2 3405 N N . ASN A 444 ? 1.4069 1.0945 1.6640 -0.3578 -0.3399 0.2225 444 ASN A N 3406 C CA . ASN A 444 ? 1.6152 1.3084 1.8785 -0.3445 -0.3366 0.1967 444 ASN A CA 3407 C C . ASN A 444 ? 1.4907 1.1936 1.7478 -0.3562 -0.3495 0.2223 444 ASN A C 3408 O O . ASN A 444 ? 1.2526 0.9528 1.5391 -0.3689 -0.3766 0.2574 444 ASN A O 3409 C CB . ASN A 444 ? 1.6436 1.3281 1.9730 -0.3241 -0.3549 0.1669 444 ASN A CB 3410 C CG . ASN A 444 ? 1.7654 1.4289 2.1632 -0.3272 -0.3953 0.1895 444 ASN A CG 3411 O OD1 . ASN A 444 ? 1.8476 1.5082 2.2778 -0.3301 -0.4196 0.2047 444 ASN A OD1 3412 N ND2 . ASN A 444 ? 1.7250 1.3733 2.1514 -0.3277 -0.4060 0.1940 444 ASN A ND2 3413 N N . ALA A 445 ? 1.3586 1.0759 1.5811 -0.3537 -0.3322 0.2077 445 ALA A N 3414 C CA . ALA A 445 ? 1.2934 1.0246 1.5032 -0.3645 -0.3408 0.2281 445 ALA A CA 3415 C C . ALA A 445 ? 1.2605 0.9926 1.4879 -0.3516 -0.3436 0.2070 445 ALA A C 3416 O O . ALA A 445 ? 1.5168 1.2565 1.7258 -0.3421 -0.3240 0.1798 445 ALA A O 3417 C CB . ALA A 445 ? 1.3648 1.1197 1.5152 -0.3767 -0.3203 0.2323 445 ALA A CB 3418 N N . GLY A 446 ? 1.2414 0.9694 1.5084 -0.3530 -0.3703 0.2229 446 GLY A N 3419 C CA . GLY A 446 ? 1.3623 1.0953 1.6468 -0.3420 -0.3752 0.2053 446 GLY A CA 3420 C C . GLY A 446 ? 1.4469 1.1966 1.6914 -0.3537 -0.3689 0.2198 446 GLY A C 3421 O O . GLY A 446 ? 1.2870 1.0487 1.5084 -0.3717 -0.3732 0.2502 446 GLY A O 3422 N N . LEU A 447 ? 1.4980 1.2567 1.7367 -0.3440 -0.3598 0.1973 447 LEU A N 3423 C CA . LEU A 447 ? 1.2612 1.0342 1.4703 -0.3526 -0.3569 0.2063 447 LEU A CA 3424 C C . LEU A 447 ? 1.3077 1.0849 1.5461 -0.3415 -0.3666 0.1931 447 LEU A C 3425 O O . LEU A 447 ? 1.3685 1.1532 1.6241 -0.3269 -0.3598 0.1652 447 LEU A O 3426 C CB . LEU A 447 ? 1.1762 0.9599 1.3380 -0.3558 -0.3319 0.1927 447 LEU A CB 3427 C CG . LEU A 447 ? 1.2230 1.0230 1.3583 -0.3638 -0.3306 0.1963 447 LEU A CG 3428 C CD1 . LEU A 447 ? 1.2057 1.0234 1.3272 -0.3797 -0.3418 0.2233 447 LEU A CD1 3429 C CD2 . LEU A 447 ? 1.1750 0.9806 1.2829 -0.3639 -0.3126 0.1773 447 LEU A CD2 3430 N N . GLU A 448 ? 1.3321 1.1130 1.5764 -0.3494 -0.3828 0.2134 448 GLU A N 3431 C CA . GLU A 448 ? 1.5203 1.3061 1.7941 -0.3393 -0.3940 0.2022 448 GLU A CA 3432 C C . GLU A 448 ? 1.4675 1.2660 1.7131 -0.3507 -0.3946 0.2178 448 GLU A C 3433 O O . GLU A 448 ? 1.3322 1.1397 1.5496 -0.3671 -0.3955 0.2418 448 GLU A O 3434 C CB . GLU A 448 ? 1.6756 1.4478 2.0163 -0.3324 -0.4253 0.2080 448 GLU A CB 3435 C CG . GLU A 448 ? 1.8131 1.5949 2.1967 -0.3151 -0.4368 0.1818 448 GLU A CG 3436 C CD . GLU A 448 ? 1.9358 1.7030 2.4005 -0.3039 -0.4718 0.1770 448 GLU A CD 3437 O OE1 . GLU A 448 ? 1.8646 1.6109 2.3537 -0.3109 -0.4880 0.1976 448 GLU A OE1 3438 O OE2 . GLU A 448 ? 1.9519 1.7309 2.4618 -0.2880 -0.4859 0.1518 448 GLU A OE2 3439 N N . VAL A 449 ? 1.4017 1.2096 1.6560 -0.3421 -0.3943 0.2024 449 VAL A N 3440 C CA . VAL A 449 ? 1.2810 1.1009 1.5119 -0.3511 -0.3953 0.2133 449 VAL A CA 3441 C C . VAL A 449 ? 1.4399 1.2619 1.7092 -0.3450 -0.4155 0.2155 449 VAL A C 3442 O O . VAL A 449 ? 1.3658 1.1955 1.6620 -0.3298 -0.4154 0.1910 449 VAL A O 3443 C CB . VAL A 449 ? 1.2724 1.1038 1.4705 -0.3502 -0.3745 0.1950 449 VAL A CB 3444 C CG1 . VAL A 449 ? 1.4387 1.2816 1.6234 -0.3567 -0.3792 0.2012 449 VAL A CG1 3445 C CG2 . VAL A 449 ? 1.2690 1.0982 1.4333 -0.3574 -0.3590 0.1930 449 VAL A CG2 3446 N N . TYR A 450 ? 1.5410 1.3646 1.8142 -0.3578 -0.4335 0.2450 450 TYR A N 3447 C CA . TYR A 450 ? 1.3886 1.2125 1.7012 -0.3543 -0.4562 0.2523 450 TYR A CA 3448 C C . TYR A 450 ? 1.3806 1.2219 1.6616 -0.3615 -0.4509 0.2566 450 TYR A C 3449 O O . TYR A 450 ? 1.3521 1.2080 1.6047 -0.3786 -0.4530 0.2807 450 TYR A O 3450 C CB . TYR A 450 ? 1.5054 1.3218 1.8562 -0.3667 -0.4872 0.2905 450 TYR A CB 3451 C CG . TYR A 450 ? 1.4134 1.2079 1.8190 -0.3595 -0.5055 0.2905 450 TYR A CG 3452 C CD1 . TYR A 450 ? 1.4603 1.2463 1.8855 -0.3381 -0.4952 0.2494 450 TYR A CD1 3453 C CD2 . TYR A 450 ? 1.4379 1.2266 1.8814 -0.3757 -0.5363 0.3338 450 TYR A CD2 3454 C CE1 . TYR A 450 ? 1.6157 1.3833 2.0972 -0.3300 -0.5147 0.2445 450 TYR A CE1 3455 C CE2 . TYR A 450 ? 1.7990 1.5645 2.3028 -0.3698 -0.5586 0.3351 450 TYR A CE2 3456 C CZ . TYR A 450 ? 1.8013 1.5539 2.3244 -0.3453 -0.5475 0.2869 450 TYR A CZ 3457 O OH . TYR A 450 ? 1.4957 1.2267 2.0844 -0.3377 -0.5720 0.2832 450 TYR A OH 3458 N N . PRO A 451 ? 1.4845 1.3324 1.7728 -0.3492 -0.4455 0.2332 451 PRO A N 3459 C CA . PRO A 451 ? 1.5281 1.3820 1.8424 -0.3304 -0.4388 0.2006 451 PRO A CA 3460 C C . PRO A 451 ? 1.4398 1.3055 1.7160 -0.3308 -0.4123 0.1848 451 PRO A C 3461 O O . PRO A 451 ? 1.2241 1.0865 1.4601 -0.3431 -0.4020 0.1950 451 PRO A O 3462 C CB . PRO A 451 ? 1.3692 1.2382 1.7092 -0.3228 -0.4501 0.1929 451 PRO A CB 3463 C CG . PRO A 451 ? 1.2249 1.0960 1.5258 -0.3385 -0.4477 0.2143 451 PRO A CG 3464 C CD . PRO A 451 ? 1.2498 1.1107 1.5258 -0.3549 -0.4496 0.2408 451 PRO A CD 3465 N N . SER A 452 ? 1.5124 1.3989 1.8067 -0.3179 -0.4042 0.1596 452 SER A N 3466 C CA . SER A 452 ? 1.4375 1.3401 1.7047 -0.3212 -0.3832 0.1515 452 SER A CA 3467 C C . SER A 452 ? 1.4576 1.3790 1.7085 -0.3286 -0.3792 0.1567 452 SER A C 3468 O O . SER A 452 ? 1.3144 1.2404 1.5447 -0.3371 -0.3683 0.1601 452 SER A O 3469 C CB . SER A 452 ? 1.3053 1.2391 1.5993 -0.3077 -0.3771 0.1261 452 SER A CB 3470 O OG . SER A 452 ? 1.2368 1.2012 1.5728 -0.2935 -0.3896 0.1063 452 SER A OG 3471 N N . ILE A 453 ? 1.4941 1.4253 1.7604 -0.3260 -0.3912 0.1585 453 ILE A N 3472 C CA . ILE A 453 ? 1.4068 1.3570 1.6633 -0.3330 -0.3904 0.1646 453 ILE A CA 3473 C C . ILE A 453 ? 1.3615 1.2894 1.6032 -0.3413 -0.4009 0.1802 453 ILE A C 3474 O O . ILE A 453 ? 1.6423 1.5589 1.8977 -0.3384 -0.4139 0.1861 453 ILE A O 3475 C CB . ILE A 453 ? 1.2825 1.2800 1.5696 -0.3233 -0.3940 0.1509 453 ILE A CB 3476 C CG1 . ILE A 453 ? 1.2870 1.3241 1.5914 -0.3145 -0.3844 0.1311 453 ILE A CG1 3477 C CG2 . ILE A 453 ? 1.2217 1.2430 1.5004 -0.3337 -0.3941 0.1628 453 ILE A CG2 3478 C CD1 . ILE A 453 ? 1.4998 1.5985 1.8414 -0.3008 -0.3895 0.1073 453 ILE A CD1 3479 N N . LEU A 454 ? 1.1945 1.1203 1.4145 -0.3522 -0.3982 0.1868 454 LEU A N 3480 C CA . LEU A 454 ? 1.2467 1.1608 1.4503 -0.3603 -0.4070 0.1963 454 LEU A CA 3481 C C . LEU A 454 ? 1.3751 1.3044 1.5863 -0.3628 -0.4150 0.1995 454 LEU A C 3482 O O . LEU A 454 ? 1.3581 1.3034 1.5779 -0.3651 -0.4128 0.1982 454 LEU A O 3483 C CB . LEU A 454 ? 1.3210 1.2245 1.4996 -0.3689 -0.4017 0.1929 454 LEU A CB 3484 C CG . LEU A 454 ? 1.2000 1.0919 1.3688 -0.3677 -0.3918 0.1891 454 LEU A CG 3485 C CD1 . LEU A 454 ? 1.2446 1.1342 1.3927 -0.3747 -0.3887 0.1800 454 LEU A CD1 3486 C CD2 . LEU A 454 ? 1.2099 1.0958 1.3826 -0.3658 -0.3972 0.2002 454 LEU A CD2 3487 N N . ASN A 455 ? 1.4288 1.3562 1.6393 -0.3644 -0.4262 0.2080 455 ASN A N 3488 C CA . ASN A 455 ? 1.2509 1.1909 1.4670 -0.3672 -0.4348 0.2118 455 ASN A CA 3489 C C . ASN A 455 ? 1.2901 1.2268 1.4846 -0.3771 -0.4411 0.2152 455 ASN A C 3490 O O . ASN A 455 ? 1.4105 1.3477 1.5948 -0.3811 -0.4466 0.2245 455 ASN A O 3491 C CB . ASN A 455 ? 1.2573 1.2067 1.4987 -0.3589 -0.4447 0.2154 455 ASN A CB 3492 C CG . ASN A 455 ? 1.3984 1.3656 1.6479 -0.3605 -0.4520 0.2184 455 ASN A CG 3493 O OD1 . ASN A 455 ? 1.4024 1.3681 1.6366 -0.3698 -0.4545 0.2224 455 ASN A OD1 3494 N ND2 . ASN A 455 ? 1.5506 1.5385 1.8288 -0.3504 -0.4573 0.2131 455 ASN A ND2 3495 N N . GLN A 456 ? 1.2228 1.1632 1.4161 -0.3821 -0.4432 0.2079 456 GLN A N 3496 C CA . GLN A 456 ? 1.2612 1.2070 1.4399 -0.3891 -0.4502 0.1999 456 GLN A CA 3497 C C . GLN A 456 ? 1.3699 1.3292 1.5460 -0.3923 -0.4611 0.2094 456 GLN A C 3498 O O . GLN A 456 ? 1.4053 1.3817 1.5659 -0.3984 -0.4665 0.2041 456 GLN A O 3499 C CB . GLN A 456 ? 1.4243 1.3671 1.6181 -0.3919 -0.4557 0.1863 456 GLN A CB 3500 C CG . GLN A 456 ? 1.2491 1.1799 1.4508 -0.3909 -0.4484 0.1799 456 GLN A CG 3501 C CD . GLN A 456 ? 1.2665 1.1939 1.5001 -0.3960 -0.4607 0.1771 456 GLN A CD 3502 O OE1 . GLN A 456 ? 1.2922 1.2287 1.5465 -0.3999 -0.4669 0.1937 456 GLN A OE1 3503 N NE2 . GLN A 456 ? 1.3205 1.2393 1.5644 -0.3969 -0.4672 0.1566 456 GLN A NE2 3504 N N . ASP A 457 ? 1.3750 1.3346 1.5682 -0.3881 -0.4648 0.2214 457 ASP A N 3505 C CA . ASP A 457 ? 1.4306 1.4011 1.6260 -0.3907 -0.4763 0.2322 457 ASP A CA 3506 C C . ASP A 457 ? 1.6145 1.5852 1.8120 -0.3907 -0.4813 0.2493 457 ASP A C 3507 O O . ASP A 457 ? 1.6782 1.6587 1.8804 -0.3948 -0.4934 0.2637 457 ASP A O 3508 C CB . ASP A 457 ? 1.5768 1.5531 1.7950 -0.3863 -0.4803 0.2352 457 ASP A CB 3509 C CG . ASP A 457 ? 1.5532 1.5397 1.7746 -0.3891 -0.4926 0.2447 457 ASP A CG 3510 O OD1 . ASP A 457 ? 1.5899 1.5780 1.8253 -0.3843 -0.4984 0.2550 457 ASP A OD1 3511 O OD2 . ASP A 457 ? 1.6638 1.6567 1.8792 -0.3956 -0.4990 0.2404 457 ASP A OD2 3512 N N . ASN A 458 ? 1.6961 1.6558 1.8950 -0.3875 -0.4748 0.2499 458 ASN A N 3513 C CA . ASN A 458 ? 1.5801 1.5352 1.7949 -0.3877 -0.4842 0.2683 458 ASN A CA 3514 C C . ASN A 458 ? 1.5739 1.5464 1.7664 -0.4027 -0.4886 0.2859 458 ASN A C 3515 O O . ASN A 458 ? 1.7609 1.7315 1.9684 -0.4071 -0.4984 0.3075 458 ASN A O 3516 C CB . ASN A 458 ? 1.5786 1.5170 1.8144 -0.3758 -0.4780 0.2589 458 ASN A CB 3517 C CG . ASN A 458 ? 1.7051 1.6341 1.9733 -0.3743 -0.4942 0.2758 458 ASN A CG 3518 O OD1 . ASN A 458 ? 1.8058 1.7376 2.0987 -0.3765 -0.5132 0.2924 458 ASN A OD1 3519 N ND2 . ASN A 458 ? 1.9759 1.8927 2.2500 -0.3713 -0.4900 0.2734 458 ASN A ND2 3520 N N . LYS A 459 ? 1.5483 1.5449 1.7104 -0.4110 -0.4838 0.2759 459 LYS A N 3521 C CA . LYS A 459 ? 1.6044 1.6375 1.7411 -0.4251 -0.4843 0.2842 459 LYS A CA 3522 C C . LYS A 459 ? 1.6962 1.7513 1.8440 -0.4391 -0.5016 0.3250 459 LYS A C 3523 O O . LYS A 459 ? 1.8263 1.8878 1.9896 -0.4432 -0.5161 0.3432 459 LYS A O 3524 C CB . LYS A 459 ? 1.5115 1.5817 1.6252 -0.4303 -0.4834 0.2628 459 LYS A CB 3525 C CG . LYS A 459 ? 1.5059 1.5541 1.6235 -0.4191 -0.4761 0.2278 459 LYS A CG 3526 C CD . LYS A 459 ? 1.4875 1.5704 1.5973 -0.4228 -0.4832 0.2061 459 LYS A CD 3527 C CE . LYS A 459 ? 1.6522 1.7114 1.7791 -0.4136 -0.4831 0.1744 459 LYS A CE 3528 N NZ . LYS A 459 ? 1.7374 1.8255 1.8689 -0.4153 -0.4953 0.1506 459 LYS A NZ 3529 N N . THR A 460 ? 1.7091 1.7778 1.8531 -0.4482 -0.5023 0.3425 460 THR A N 3530 C CA . THR A 460 ? 1.6130 1.6990 1.7805 -0.4642 -0.5240 0.3900 460 THR A CA 3531 C C . THR A 460 ? 1.5024 1.6573 1.6423 -0.4873 -0.5260 0.4126 460 THR A C 3532 O O . THR A 460 ? 1.8108 2.0223 1.9450 -0.5063 -0.5395 0.4403 460 THR A O 3533 C CB . THR A 460 ? 1.4812 1.5183 1.6905 -0.4549 -0.5319 0.4006 460 THR A CB 3534 O OG1 . THR A 460 ? 1.6132 1.6053 1.8524 -0.4340 -0.5321 0.3783 460 THR A OG1 3535 C CG2 . THR A 460 ? 1.4768 1.5290 1.7244 -0.4734 -0.5619 0.4540 460 THR A CG2 3536 N N . CYS A 461 ? 1.4114 1.5698 1.5347 -0.4867 -0.5128 0.4013 461 CYS A N 3537 C CA . CYS A 461 ? 1.4842 1.7170 1.5842 -0.5090 -0.5147 0.4237 461 CYS A CA 3538 C C . CYS A 461 ? 1.3614 1.6732 1.4215 -0.5167 -0.5064 0.3989 461 CYS A C 3539 O O . CYS A 461 ? 1.3604 1.6565 1.4063 -0.4998 -0.4926 0.3493 461 CYS A O 3540 C CB . CYS A 461 ? 1.5235 1.7398 1.6146 -0.5035 -0.5004 0.4101 461 CYS A CB 3541 S SG . CYS A 461 ? 2.5763 2.8932 2.6402 -0.5316 -0.5023 0.4385 461 CYS A SG 3542 N N . SER A 462 ? 1.3778 1.7816 1.4254 -0.5433 -0.5177 0.4339 462 SER A N 3543 C CA . SER A 462 ? 1.5137 2.0146 1.5263 -0.5518 -0.5119 0.4076 462 SER A CA 3544 C C . SER A 462 ? 1.5815 2.1428 1.5644 -0.5522 -0.4958 0.3741 462 SER A C 3545 O O . SER A 462 ? 1.6617 2.2420 1.6445 -0.5649 -0.4970 0.4045 462 SER A O 3546 C CB . SER A 462 ? 1.6926 2.2827 1.7074 -0.5826 -0.5335 0.4631 462 SER A CB 3547 O OG . SER A 462 ? 1.8105 2.5022 1.7937 -0.5888 -0.5284 0.4312 462 SER A OG 3548 N N . LEU A 463 ? 1.5098 2.1014 1.4736 -0.5377 -0.4833 0.3098 463 LEU A N 3549 C CA . LEU A 463 ? 1.5686 2.2257 1.5105 -0.5345 -0.4702 0.2655 463 LEU A CA 3550 C C . LEU A 463 ? 1.8377 2.6392 1.7573 -0.5645 -0.4768 0.2953 463 LEU A C 3551 O O . LEU A 463 ? 2.0384 2.9116 1.9541 -0.5832 -0.4897 0.3229 463 LEU A O 3552 C CB . LEU A 463 ? 1.5690 2.2286 1.5112 -0.5117 -0.4636 0.1876 463 LEU A CB 3553 C CG . LEU A 463 ? 1.5711 2.2480 1.5105 -0.4956 -0.4518 0.1243 463 LEU A CG 3554 C CD1 . LEU A 463 ? 1.5178 2.1152 1.4839 -0.4684 -0.4516 0.0678 463 LEU A CD1 3555 C CD2 . LEU A 463 ? 1.5797 2.4083 1.4986 -0.5062 -0.4526 0.0918 463 LEU A CD2 3556 N N . PRO A 464 ? 1.8327 2.6843 1.7383 -0.5714 -0.4688 0.2939 464 PRO A N 3557 C CA . PRO A 464 ? 1.8776 2.8805 1.7626 -0.6038 -0.4757 0.3293 464 PRO A CA 3558 C C . PRO A 464 ? 1.9386 3.0851 1.8022 -0.6087 -0.4755 0.2836 464 PRO A C 3559 O O . PRO A 464 ? 1.9524 3.2104 1.8070 -0.6386 -0.4888 0.3300 464 PRO A O 3560 C CB . PRO A 464 ? 1.8168 2.8311 1.6918 -0.6016 -0.4630 0.3170 464 PRO A CB 3561 C CG . PRO A 464 ? 1.7837 2.6808 1.6691 -0.5644 -0.4475 0.2504 464 PRO A CG 3562 C CD . PRO A 464 ? 1.7931 2.5679 1.7026 -0.5520 -0.4540 0.2653 464 PRO A CD 3563 N N . GLY A 465 ? 1.8304 2.9785 1.6924 -0.5802 -0.4637 0.1941 465 GLY A N 3564 C CA . GLY A 465 ? 1.7966 3.0868 1.6463 -0.5799 -0.4650 0.1354 465 GLY A CA 3565 C C . GLY A 465 ? 1.8341 3.1389 1.6885 -0.5849 -0.4773 0.1440 465 GLY A C 3566 O O . GLY A 465 ? 1.8805 3.3272 1.7182 -0.6102 -0.4857 0.1656 465 GLY A O 3567 N N . THR A 466 ? 1.8589 3.0232 1.7364 -0.5622 -0.4788 0.1296 466 THR A N 3568 C CA . THR A 466 ? 1.9214 3.0794 1.8064 -0.5641 -0.4902 0.1373 466 THR A CA 3569 C C . THR A 466 ? 1.8448 2.8676 1.7461 -0.5674 -0.4963 0.2058 466 THR A C 3570 O O . THR A 466 ? 1.6797 2.5927 1.5930 -0.5570 -0.4900 0.2208 466 THR A O 3571 C CB . THR A 466 ? 1.9635 3.0915 1.8689 -0.5328 -0.4907 0.0489 466 THR A CB 3572 O OG1 . THR A 466 ? 1.9787 3.0842 1.8926 -0.5348 -0.5017 0.0634 466 THR A OG1 3573 C CG2 . THR A 466 ? 1.7715 2.7511 1.7023 -0.5049 -0.4835 0.0204 466 THR A CG2 3574 N N . ALA A 467 ? 1.9149 2.9489 1.8203 -0.5804 -0.5095 0.2425 467 ALA A N 3575 C CA . ALA A 467 ? 1.8241 2.7436 1.7514 -0.5837 -0.5185 0.3054 467 ALA A CA 3576 C C . ALA A 467 ? 1.7086 2.5054 1.6564 -0.5544 -0.5152 0.2673 467 ALA A C 3577 O O . ALA A 467 ? 1.4292 2.2408 1.3798 -0.5495 -0.5209 0.2439 467 ALA A O 3578 C CB . ALA A 467 ? 1.8304 2.8208 1.7590 -0.6148 -0.5379 0.3733 467 ALA A CB 3579 N N . LEU A 468 ? 1.7934 2.4758 1.7566 -0.5369 -0.5069 0.2643 468 LEU A N 3580 C CA . LEU A 468 ? 1.7467 2.3145 1.7323 -0.5127 -0.5042 0.2402 468 LEU A CA 3581 C C . LEU A 468 ? 1.6667 2.1359 1.6698 -0.5070 -0.5008 0.2738 468 LEU A C 3582 O O . LEU A 468 ? 1.6966 2.1710 1.6937 -0.5112 -0.4945 0.2847 468 LEU A O 3583 C CB . LEU A 468 ? 1.6921 2.2499 1.6817 -0.4904 -0.4959 0.1651 468 LEU A CB 3584 C CG . LEU A 468 ? 1.5237 2.1573 1.5124 -0.4870 -0.5032 0.1140 468 LEU A CG 3585 C CD1 . LEU A 468 ? 1.3987 2.0095 1.4083 -0.4636 -0.5013 0.0407 468 LEU A CD1 3586 C CD2 . LEU A 468 ? 1.6091 2.2140 1.6088 -0.4881 -0.5141 0.1323 468 LEU A CD2 3587 N N . LYS A 469 ? 1.6899 2.0761 1.7165 -0.4967 -0.5053 0.2871 469 LYS A N 3588 C CA . LYS A 469 ? 1.6872 1.9899 1.7358 -0.4886 -0.5033 0.3104 469 LYS A CA 3589 C C . LYS A 469 ? 1.6649 1.9062 1.7176 -0.4668 -0.4879 0.2669 469 LYS A C 3590 O O . LYS A 469 ? 1.6168 1.8368 1.6753 -0.4547 -0.4860 0.2333 469 LYS A O 3591 C CB . LYS A 469 ? 1.7914 2.0484 1.8688 -0.4876 -0.5173 0.3427 469 LYS A CB 3592 C CG . LYS A 469 ? 1.9387 2.2473 2.0243 -0.5115 -0.5378 0.3973 469 LYS A CG 3593 C CD . LYS A 469 ? 2.1012 2.3658 2.2216 -0.5084 -0.5542 0.4224 469 LYS A CD 3594 C CE . LYS A 469 ? 2.1732 2.4920 2.3087 -0.5348 -0.5793 0.4808 469 LYS A CE 3595 N NZ . LYS A 469 ? 2.2265 2.5050 2.4010 -0.5309 -0.5980 0.5018 469 LYS A NZ 3596 N N . VAL A 470 ? 1.7244 1.9407 1.7778 -0.4640 -0.4795 0.2715 470 VAL A N 3597 C CA . VAL A 470 ? 1.5876 1.7570 1.6445 -0.4471 -0.4656 0.2352 470 VAL A CA 3598 C C . VAL A 470 ? 1.5394 1.6425 1.6173 -0.4386 -0.4621 0.2538 470 VAL A C 3599 O O . VAL A 470 ? 1.5357 1.6370 1.6231 -0.4463 -0.4691 0.2891 470 VAL A O 3600 C CB . VAL A 470 ? 1.5006 1.7151 1.5368 -0.4497 -0.4563 0.2099 470 VAL A CB 3601 C CG1 . VAL A 470 ? 1.4605 1.6294 1.5067 -0.4329 -0.4463 0.1701 470 VAL A CG1 3602 C CG2 . VAL A 470 ? 1.5702 1.8740 1.5881 -0.4591 -0.4616 0.1892 470 VAL A CG2 3603 N N . SER A 471 ? 1.4856 1.5407 1.5765 -0.4236 -0.4542 0.2305 471 SER A N 3604 C CA . SER A 471 ? 1.4787 1.4857 1.5891 -0.4141 -0.4491 0.2395 471 SER A CA 3605 C C . SER A 471 ? 1.5023 1.5086 1.6029 -0.4155 -0.4399 0.2395 471 SER A C 3606 O O . SER A 471 ? 1.5849 1.6024 1.6703 -0.4143 -0.4306 0.2145 471 SER A O 3607 C CB . SER A 471 ? 1.3501 1.3252 1.4755 -0.4019 -0.4434 0.2184 471 SER A CB 3608 O OG . SER A 471 ? 1.3110 1.2570 1.4536 -0.3931 -0.4371 0.2223 471 SER A OG 3609 N N . CYS A 472 ? 1.4303 1.4233 1.5460 -0.4174 -0.4452 0.2661 472 CYS A N 3610 C CA . CYS A 472 ? 1.5004 1.4969 1.6082 -0.4216 -0.4394 0.2724 472 CYS A CA 3611 C C . CYS A 472 ? 1.4392 1.3924 1.5760 -0.4110 -0.4393 0.2779 472 CYS A C 3612 O O . CYS A 472 ? 1.5608 1.4910 1.7282 -0.4019 -0.4477 0.2805 472 CYS A O 3613 C CB . CYS A 472 ? 1.5386 1.5841 1.6378 -0.4417 -0.4519 0.3064 472 CYS A CB 3614 S SG . CYS A 472 ? 1.7626 1.7981 1.9044 -0.4499 -0.4796 0.3545 472 CYS A SG 3615 N N . PHE A 473 ? 1.3891 1.3371 1.5184 -0.4112 -0.4304 0.2754 473 PHE A N 3616 C CA . PHE A 473 ? 1.4071 1.3217 1.5661 -0.4022 -0.4325 0.2796 473 PHE A CA 3617 C C . PHE A 473 ? 1.3869 1.3131 1.5399 -0.4134 -0.4345 0.2995 473 PHE A C 3618 O O . PHE A 473 ? 1.2841 1.2521 1.4085 -0.4287 -0.4336 0.3105 473 PHE A O 3619 C CB . PHE A 473 ? 1.3835 1.2733 1.5447 -0.3859 -0.4157 0.2476 473 PHE A CB 3620 C CG . PHE A 473 ? 1.3275 1.2239 1.4572 -0.3872 -0.3982 0.2269 473 PHE A CG 3621 C CD1 . PHE A 473 ? 1.3849 1.2978 1.4972 -0.3902 -0.3959 0.2124 473 PHE A CD1 3622 C CD2 . PHE A 473 ? 1.2333 1.1178 1.3585 -0.3840 -0.3868 0.2191 473 PHE A CD2 3623 C CE1 . PHE A 473 ? 1.3734 1.2903 1.4710 -0.3896 -0.3857 0.1894 473 PHE A CE1 3624 C CE2 . PHE A 473 ? 1.2807 1.1696 1.3853 -0.3844 -0.3740 0.1989 473 PHE A CE2 3625 C CZ . PHE A 473 ? 1.3875 1.2920 1.4817 -0.3868 -0.3749 0.1831 473 PHE A CZ 3626 N N . ASN A 474 ? 1.4533 1.3506 1.6363 -0.4063 -0.4390 0.3034 474 ASN A N 3627 C CA . ASN A 474 ? 1.4434 1.3491 1.6267 -0.4177 -0.4434 0.3258 474 ASN A CA 3628 C C . ASN A 474 ? 1.3849 1.2679 1.5595 -0.4062 -0.4243 0.3002 474 ASN A C 3629 O O . ASN A 474 ? 1.4062 1.2623 1.5954 -0.3887 -0.4160 0.2732 474 ASN A O 3630 C CB . ASN A 474 ? 1.5380 1.4308 1.7769 -0.4233 -0.4744 0.3615 474 ASN A CB 3631 C CG . ASN A 474 ? 1.8633 1.7775 2.1187 -0.4359 -0.4971 0.3919 474 ASN A CG 3632 O OD1 . ASN A 474 ? 1.9967 1.9471 2.2137 -0.4451 -0.4889 0.3919 474 ASN A OD1 3633 N ND2 . ASN A 474 ? 1.9688 1.8623 2.2879 -0.4362 -0.5287 0.4164 474 ASN A ND2 3634 N N . VAL A 475 ? 1.3010 1.2036 1.4516 -0.4171 -0.4174 0.3093 475 VAL A N 3635 C CA . VAL A 475 ? 1.3130 1.1941 1.4582 -0.4081 -0.4016 0.2900 475 VAL A CA 3636 C C . VAL A 475 ? 1.3475 1.2334 1.5080 -0.4200 -0.4137 0.3210 475 VAL A C 3637 O O . VAL A 475 ? 1.3704 1.2998 1.5091 -0.4393 -0.4171 0.3459 475 VAL A O 3638 C CB . VAL A 475 ? 1.3232 1.2209 1.4247 -0.4068 -0.3781 0.2610 475 VAL A CB 3639 C CG1 . VAL A 475 ? 1.3259 1.2780 1.3971 -0.4223 -0.3798 0.2682 475 VAL A CG1 3640 C CG2 . VAL A 475 ? 1.3475 1.2330 1.4416 -0.4035 -0.3649 0.2515 475 VAL A CG2 3641 N N . ARG A 476 ? 1.4406 1.2890 1.6427 -0.4089 -0.4225 0.3189 476 ARG A N 3642 C CA . ARG A 476 ? 1.4634 1.3083 1.6910 -0.4187 -0.4377 0.3474 476 ARG A CA 3643 C C . ARG A 476 ? 1.3949 1.2239 1.6055 -0.4093 -0.4163 0.3227 476 ARG A C 3644 O O . ARG A 476 ? 1.3120 1.1141 1.5325 -0.3896 -0.4045 0.2878 476 ARG A O 3645 C CB . ARG A 476 ? 1.6075 1.4220 1.9094 -0.4128 -0.4708 0.3619 476 ARG A CB 3646 C CG . ARG A 476 ? 1.8478 1.6771 2.1768 -0.4253 -0.4983 0.3955 476 ARG A CG 3647 C CD . ARG A 476 ? 1.7660 1.5608 2.1817 -0.4154 -0.5350 0.4014 476 ARG A CD 3648 N NE . ARG A 476 ? 1.7465 1.5256 2.2127 -0.4225 -0.5601 0.4271 476 ARG A NE 3649 C CZ . ARG A 476 ? 1.7151 1.4618 2.2161 -0.4026 -0.5602 0.3947 476 ARG A CZ 3650 N NH1 . ARG A 476 ? 1.5588 1.2940 2.0465 -0.3761 -0.5353 0.3374 476 ARG A NH1 3651 N NH2 . ARG A 476 ? 1.7082 1.4405 2.2601 -0.4109 -0.5868 0.4212 476 ARG A NH2 3652 N N . PHE A 477 ? 1.4273 1.2818 1.6123 -0.4248 -0.4115 0.3418 477 PHE A N 3653 C CA . PHE A 477 ? 1.4306 1.2712 1.6008 -0.4179 -0.3931 0.3225 477 PHE A CA 3654 C C . PHE A 477 ? 1.3981 1.2317 1.6040 -0.4280 -0.4134 0.3555 477 PHE A C 3655 O O . PHE A 477 ? 1.4333 1.3052 1.6350 -0.4513 -0.4269 0.3973 477 PHE A O 3656 C CB . PHE A 477 ? 1.3433 1.2202 1.4554 -0.4241 -0.3684 0.3072 477 PHE A CB 3657 C CG . PHE A 477 ? 1.3222 1.2617 1.4118 -0.4480 -0.3764 0.3391 477 PHE A CG 3658 C CD1 . PHE A 477 ? 1.3458 1.3220 1.4269 -0.4574 -0.3850 0.3500 477 PHE A CD1 3659 C CD2 . PHE A 477 ? 1.5114 1.4833 1.5874 -0.4620 -0.3747 0.3577 477 PHE A CD2 3660 C CE1 . PHE A 477 ? 1.6196 1.6711 1.6795 -0.4810 -0.3921 0.3787 477 PHE A CE1 3661 C CE2 . PHE A 477 ? 1.6798 1.7291 1.7346 -0.4862 -0.3818 0.3877 477 PHE A CE2 3662 C CZ . PHE A 477 ? 1.7482 1.8412 1.7947 -0.4960 -0.3904 0.3978 477 PHE A CZ 3663 N N . CYS A 478 ? 1.3757 1.1675 1.6214 -0.4113 -0.4178 0.3373 478 CYS A N 3664 C CA . CYS A 478 ? 1.5319 1.3092 1.8247 -0.4180 -0.4418 0.3644 478 CYS A CA 3665 C C . CYS A 478 ? 1.4218 1.1959 1.6872 -0.4161 -0.4205 0.3511 478 CYS A C 3666 O O . CYS A 478 ? 1.3681 1.1328 1.6021 -0.4003 -0.3917 0.3103 478 CYS A O 3667 C CB . CYS A 478 ? 1.6084 1.3459 1.9783 -0.3995 -0.4681 0.3490 478 CYS A CB 3668 S SG . CYS A 478 ? 2.8564 2.5947 3.2815 -0.4059 -0.5067 0.3774 478 CYS A SG 3669 N N . LEU A 479 ? 1.5388 1.3242 1.8190 -0.4342 -0.4366 0.3899 479 LEU A N 3670 C CA . LEU A 479 ? 1.6268 1.4149 1.8788 -0.4354 -0.4173 0.3825 479 LEU A CA 3671 C C . LEU A 479 ? 1.4341 1.2013 1.7437 -0.4416 -0.4453 0.4105 479 LEU A C 3672 O O . LEU A 479 ? 1.3763 1.1616 1.7219 -0.4643 -0.4781 0.4640 479 LEU A O 3673 C CB . LEU A 479 ? 1.6668 1.5140 1.8557 -0.4556 -0.3997 0.3993 479 LEU A CB 3674 C CG . LEU A 479 ? 1.4519 1.3088 1.5977 -0.4530 -0.3714 0.3777 479 LEU A CG 3675 C CD1 . LEU A 479 ? 1.2594 1.0763 1.3919 -0.4268 -0.3457 0.3234 479 LEU A CD1 3676 C CD2 . LEU A 479 ? 1.4067 1.3336 1.4977 -0.4695 -0.3573 0.3835 479 LEU A CD2 3677 N N . LYS A 480 ? 1.4952 1.2286 1.8175 -0.4230 -0.4347 0.3766 480 LYS A N 3678 C CA . LYS A 480 ? 1.6758 1.3864 2.0557 -0.4260 -0.4608 0.3954 480 LYS A CA 3679 C C . LYS A 480 ? 1.5724 1.2753 1.9198 -0.4174 -0.4328 0.3688 480 LYS A C 3680 O O . LYS A 480 ? 1.6829 1.3757 2.0011 -0.3970 -0.4032 0.3202 480 LYS A O 3681 C CB . LYS A 480 ? 1.7062 1.3760 2.1738 -0.4060 -0.4931 0.3748 480 LYS A CB 3682 C CG . LYS A 480 ? 1.8357 1.4781 2.3800 -0.4067 -0.5277 0.3895 480 LYS A CG 3683 C CD . LYS A 480 ? 1.9973 1.6051 2.6262 -0.3773 -0.5524 0.3428 480 LYS A CD 3684 C CE . LYS A 480 ? 1.8505 1.4621 2.4394 -0.3486 -0.5120 0.2732 480 LYS A CE 3685 N NZ . LYS A 480 ? 1.8657 1.4646 2.5347 -0.3186 -0.5336 0.2196 480 LYS A NZ 3686 N N . ALA A 481 ? 1.4356 1.1476 1.7908 -0.4352 -0.4439 0.4047 481 ALA A N 3687 C CA . ALA A 481 ? 1.4435 1.1499 1.7689 -0.4293 -0.4190 0.3841 481 ALA A CA 3688 C C . ALA A 481 ? 1.3376 1.0309 1.7166 -0.4406 -0.4483 0.4175 481 ALA A C 3689 O O . ALA A 481 ? 1.4623 1.1774 1.8702 -0.4667 -0.4795 0.4758 481 ALA A O 3690 C CB . ALA A 481 ? 1.7869 1.5385 2.0297 -0.4418 -0.3853 0.3865 481 ALA A CB 3691 N N . ASP A 482 ? 1.5386 1.2017 1.9323 -0.4229 -0.4395 0.3836 482 ASP A N 3692 C CA . ASP A 482 ? 1.6354 1.2858 2.0770 -0.4305 -0.4642 0.4097 482 ASP A CA 3693 C C . ASP A 482 ? 1.6521 1.2906 2.0613 -0.4186 -0.4336 0.3739 482 ASP A C 3694 O O . ASP A 482 ? 1.6980 1.3408 2.0519 -0.4031 -0.3951 0.3305 482 ASP A O 3695 C CB . ASP A 482 ? 1.6414 1.2644 2.1810 -0.4085 -0.5065 0.4016 482 ASP A CB 3696 C CG . ASP A 482 ? 1.8866 1.5182 2.4777 -0.4117 -0.5393 0.4410 482 ASP A CG 3697 O OD1 . ASP A 482 ? 1.8554 1.5276 2.4097 -0.4377 -0.5375 0.4919 482 ASP A OD1 3698 O OD2 . ASP A 482 ? 1.9076 1.5120 2.5800 -0.3885 -0.5691 0.4197 482 ASP A OD2 3699 N N . GLY A 483 ? 1.6220 1.2559 2.0627 -0.4183 -0.4483 0.3898 483 GLY A N 3700 C CA . GLY A 483 ? 1.4899 1.1120 1.9057 -0.4105 -0.4232 0.3618 483 GLY A CA 3701 C C . GLY A 483 ? 1.3570 0.9776 1.8189 -0.4070 -0.4464 0.3826 483 GLY A C 3702 O O . GLY A 483 ? 1.4334 1.0731 1.9343 -0.4176 -0.4802 0.4300 483 GLY A O 3703 N N . LYS A 484 ? 1.4156 1.0176 1.8757 -0.3935 -0.4305 0.3491 484 LYS A N 3704 C CA . LYS A 484 ? 1.3647 0.9625 1.8710 -0.3881 -0.4523 0.3630 484 LYS A CA 3705 C C . LYS A 484 ? 1.3748 1.0081 1.8301 -0.4125 -0.4404 0.4086 484 LYS A C 3706 O O . LYS A 484 ? 1.1784 0.8414 1.5627 -0.4322 -0.4138 0.4233 484 LYS A O 3707 C CB . LYS A 484 ? 1.2070 0.7760 1.7360 -0.3636 -0.4414 0.3055 484 LYS A CB 3708 C CG . LYS A 484 ? 1.4056 0.9542 1.9907 -0.3390 -0.4542 0.2522 484 LYS A CG 3709 C CD . LYS A 484 ? 1.5339 1.0710 2.1443 -0.3175 -0.4457 0.1946 484 LYS A CD 3710 C CE . LYS A 484 ? 1.5842 1.1191 2.2551 -0.2931 -0.4602 0.1345 484 LYS A CE 3711 N NZ . LYS A 484 ? 1.7810 1.3215 2.4818 -0.2727 -0.4544 0.0734 484 LYS A NZ 3712 N N . GLY A 485 ? 1.5265 1.1611 2.0225 -0.4110 -0.4621 0.4279 485 GLY A N 3713 C CA . GLY A 485 ? 1.4826 1.1559 1.9377 -0.4329 -0.4534 0.4681 485 GLY A CA 3714 C C . GLY A 485 ? 1.4200 1.1527 1.8580 -0.4635 -0.4691 0.5308 485 GLY A C 3715 O O . GLY A 485 ? 1.5253 1.2657 1.9997 -0.4676 -0.4970 0.5529 485 GLY A O 3716 N N . VAL A 486 ? 1.2778 1.0603 1.6617 -0.4859 -0.4520 0.5589 486 VAL A N 3717 C CA . VAL A 486 ? 1.3370 1.1976 1.6993 -0.5187 -0.4645 0.6176 486 VAL A CA 3718 C C . VAL A 486 ? 1.6379 1.5263 1.9337 -0.5315 -0.4350 0.6075 486 VAL A C 3719 O O . VAL A 486 ? 1.6456 1.5210 1.8833 -0.5272 -0.3948 0.5672 486 VAL A O 3720 C CB . VAL A 486 ? 1.3006 1.2196 1.6343 -0.5389 -0.4594 0.6495 486 VAL A CB 3721 C CG1 . VAL A 486 ? 1.3712 1.3923 1.6718 -0.5751 -0.4658 0.7031 486 VAL A CG1 3722 C CG2 . VAL A 486 ? 1.2775 1.1791 1.6855 -0.5312 -0.4972 0.6706 486 VAL A CG2 3723 N N . LEU A 487 ? 1.7701 1.7011 2.0796 -0.5489 -0.4584 0.6461 487 LEU A N 3724 C CA . LEU A 487 ? 1.6631 1.6264 1.9198 -0.5628 -0.4375 0.6410 487 LEU A CA 3725 C C . LEU A 487 ? 1.7222 1.7427 2.0117 -0.5838 -0.4749 0.6973 487 LEU A C 3726 O O . LEU A 487 ? 1.7881 1.7941 2.1526 -0.5789 -0.5178 0.7262 487 LEU A O 3727 C CB . LEU A 487 ? 1.4406 1.3276 1.6931 -0.5372 -0.4175 0.5821 487 LEU A CB 3728 C CG . LEU A 487 ? 1.4979 1.3134 1.8252 -0.5083 -0.4439 0.5606 487 LEU A CG 3729 C CD1 . LEU A 487 ? 1.5870 1.4161 1.9530 -0.5150 -0.4757 0.5901 487 LEU A CD1 3730 C CD2 . LEU A 487 ? 1.4981 1.2521 1.8095 -0.4825 -0.4144 0.4939 487 LEU A CD2 3731 N N . PRO A 488 ? 1.8252 1.9169 2.0634 -0.6082 -0.4612 0.7129 488 PRO A N 3732 C CA . PRO A 488 ? 1.7565 1.9214 2.0227 -0.6324 -0.4970 0.7717 488 PRO A CA 3733 C C . PRO A 488 ? 1.7441 1.8477 2.0796 -0.6160 -0.5309 0.7744 488 PRO A C 3734 O O . PRO A 488 ? 1.7445 1.7543 2.1028 -0.5850 -0.5240 0.7257 488 PRO A O 3735 C CB . PRO A 488 ? 1.7726 2.0209 1.9626 -0.6567 -0.4667 0.7701 488 PRO A CB 3736 C CG . PRO A 488 ? 1.7457 1.9929 1.8723 -0.6535 -0.4215 0.7264 488 PRO A CG 3737 C CD . PRO A 488 ? 1.7640 1.8885 1.9204 -0.6185 -0.4154 0.6806 488 PRO A CD 3738 N N . ARG A 489 ? 1.6026 1.7689 1.9736 -0.6378 -0.5682 0.8301 489 ARG A N 3739 C CA . ARG A 489 ? 1.5638 1.6827 2.0070 -0.6251 -0.6054 0.8382 489 ARG A CA 3740 C C . ARG A 489 ? 1.6517 1.7648 2.0537 -0.6249 -0.5836 0.8150 489 ARG A C 3741 O O . ARG A 489 ? 1.7444 1.7729 2.1595 -0.5969 -0.5740 0.7665 489 ARG A O 3742 C CB . ARG A 489 ? 1.6187 1.8089 2.1303 -0.6505 -0.6614 0.9123 489 ARG A CB 3743 C CG . ARG A 489 ? 1.6701 1.8725 2.2322 -0.6543 -0.6895 0.9408 489 ARG A CG 3744 C CD . ARG A 489 ? 1.8265 2.1126 2.4624 -0.6855 -0.7488 1.0189 489 ARG A CD 3745 N NE . ARG A 489 ? 1.9856 2.2310 2.7019 -0.6754 -0.7912 1.0301 489 ARG A NE 3746 C CZ . ARG A 489 ? 2.0826 2.3926 2.8758 -0.7016 -0.8478 1.0962 489 ARG A CZ 3747 N NH1 . ARG A 489 ? 2.1663 2.5913 2.9669 -0.7418 -0.8684 1.1582 489 ARG A NH1 3748 N NH2 . ARG A 489 ? 1.9656 2.2320 2.8334 -0.6892 -0.8853 1.1002 489 ARG A NH2 3749 N N . LYS A 490 ? 1.8148 2.0278 2.1691 -0.6571 -0.5766 0.8488 490 LYS A N 3750 C CA . LYS A 490 ? 1.8949 2.1168 2.2027 -0.6613 -0.5535 0.8284 490 LYS A CA 3751 C C . LYS A 490 ? 1.8503 2.0799 2.0717 -0.6624 -0.4990 0.7802 490 LYS A C 3752 O O . LYS A 490 ? 1.8451 2.1409 2.0238 -0.6781 -0.4808 0.7870 490 LYS A O 3753 C CB . LYS A 490 ? 1.7200 2.0564 2.0254 -0.6960 -0.5757 0.8867 490 LYS A CB 3754 C CG . LYS A 490 ? 1.7830 2.1066 2.1793 -0.6963 -0.6312 0.9303 490 LYS A CG 3755 C CD . LYS A 490 ? 1.9204 2.3748 2.3165 -0.7359 -0.6536 0.9912 490 LYS A CD 3756 C CE . LYS A 490 ? 1.9816 2.4173 2.4674 -0.7364 -0.7068 1.0290 490 LYS A CE 3757 N NZ . LYS A 490 ? 2.0267 2.3758 2.5086 -0.7113 -0.6954 0.9877 490 LYS A NZ 3758 N N . LEU A 491 ? 1.6225 1.7925 1.8210 -0.6341 -0.4738 0.7182 491 LEU A N 3759 C CA . LEU A 491 ? 1.5561 1.7325 1.6809 -0.6093 -0.4246 0.6450 491 LEU A CA 3760 C C . LEU A 491 ? 1.7258 1.9614 1.8040 -0.6083 -0.4078 0.6204 491 LEU A C 3761 O O . LEU A 491 ? 1.6965 1.9242 1.7992 -0.6119 -0.4267 0.6378 491 LEU A O 3762 C CB . LEU A 491 ? 1.5138 1.5784 1.6503 -0.5703 -0.4073 0.5832 491 LEU A CB 3763 C CG . LEU A 491 ? 1.5249 1.5318 1.7011 -0.5647 -0.4171 0.5893 491 LEU A CG 3764 C CD1 . LEU A 491 ? 1.4928 1.4057 1.6844 -0.5274 -0.4026 0.5283 491 LEU A CD1 3765 C CD2 . LEU A 491 ? 1.5585 1.6176 1.6902 -0.5750 -0.3958 0.5898 491 LEU A CD2 3766 N N . ASN A 492 ? 1.7427 2.0377 1.7591 -0.6022 -0.3744 0.5767 492 ASN A N 3767 C CA . ASN A 492 ? 1.6909 2.0483 1.6665 -0.5989 -0.3590 0.5439 492 ASN A CA 3768 C C . ASN A 492 ? 1.7871 2.0713 1.7437 -0.5615 -0.3314 0.4669 492 ASN A C 3769 O O . ASN A 492 ? 1.8821 2.1503 1.8150 -0.5440 -0.3068 0.4200 492 ASN A O 3770 C CB . ASN A 492 ? 1.7110 2.2037 1.6406 -0.6179 -0.3462 0.5423 492 ASN A CB 3771 C CG . ASN A 492 ? 1.8436 2.4400 1.7886 -0.6617 -0.3756 0.6260 492 ASN A CG 3772 O OD1 . ASN A 492 ? 1.9235 2.5142 1.9068 -0.6797 -0.4061 0.6809 492 ASN A OD1 3773 N ND2 . ASN A 492 ? 1.9444 2.6421 1.8638 -0.6806 -0.3688 0.6390 492 ASN A ND2 3774 N N . PHE A 493 ? 1.7082 1.9514 1.6793 -0.5512 -0.3380 0.4577 493 PHE A N 3775 C CA . PHE A 493 ? 1.6194 1.8016 1.5781 -0.5201 -0.3165 0.3938 493 PHE A CA 3776 C C . PHE A 493 ? 1.6946 1.9375 1.6257 -0.5195 -0.3101 0.3667 493 PHE A C 3777 O O . PHE A 493 ? 1.6786 1.9728 1.6147 -0.5379 -0.3275 0.4014 493 PHE A O 3778 C CB . PHE A 493 ? 1.5618 1.6442 1.5624 -0.5042 -0.3278 0.3954 493 PHE A CB 3779 C CG . PHE A 493 ? 1.4255 1.4364 1.4491 -0.4906 -0.3241 0.3873 493 PHE A CG 3780 C CD1 . PHE A 493 ? 1.6141 1.6027 1.6824 -0.5020 -0.3494 0.4320 493 PHE A CD1 3781 C CD2 . PHE A 493 ? 1.3862 1.3552 1.3927 -0.4674 -0.2986 0.3358 493 PHE A CD2 3782 C CE1 . PHE A 493 ? 1.6578 1.5857 1.7502 -0.4880 -0.3470 0.4190 493 PHE A CE1 3783 C CE2 . PHE A 493 ? 1.3900 1.3030 1.4164 -0.4559 -0.2947 0.3278 493 PHE A CE2 3784 C CZ . PHE A 493 ? 1.5540 1.4474 1.6217 -0.4650 -0.3177 0.3662 493 PHE A CZ 3785 N N . GLN A 494 ? 1.7562 1.9943 1.6646 -0.4989 -0.2878 0.3050 494 GLN A N 3786 C CA . GLN A 494 ? 1.6897 1.9739 1.5815 -0.4931 -0.2835 0.2681 494 GLN A CA 3787 C C . GLN A 494 ? 1.5808 1.7752 1.4890 -0.4693 -0.2792 0.2357 494 GLN A C 3788 O O . GLN A 494 ? 1.5415 1.6816 1.4534 -0.4504 -0.2659 0.1992 494 GLN A O 3789 C CB . GLN A 494 ? 1.7494 2.1097 1.6150 -0.4883 -0.2684 0.2187 494 GLN A CB 3790 C CG . GLN A 494 ? 1.8809 2.3277 1.7331 -0.4890 -0.2703 0.1860 494 GLN A CG 3791 C CD . GLN A 494 ? 1.9673 2.5190 1.8079 -0.5190 -0.2850 0.2363 494 GLN A CD 3792 O OE1 . GLN A 494 ? 2.0429 2.6379 1.8810 -0.5230 -0.2927 0.2323 494 GLN A OE1 3793 N NE2 . GLN A 494 ? 1.8961 2.4938 1.7325 -0.5424 -0.2909 0.2874 494 GLN A NE2 3794 N N . VAL A 495 ? 1.6303 1.8148 1.5501 -0.4722 -0.2920 0.2529 495 VAL A N 3795 C CA . VAL A 495 ? 1.7358 1.8425 1.6737 -0.4529 -0.2904 0.2309 495 VAL A CA 3796 C C . VAL A 495 ? 1.5672 1.7048 1.4960 -0.4462 -0.2892 0.1946 495 VAL A C 3797 O O . VAL A 495 ? 1.5609 1.7736 1.4768 -0.4597 -0.2970 0.2032 495 VAL A O 3798 C CB . VAL A 495 ? 1.7992 1.8586 1.7674 -0.4571 -0.3080 0.2729 495 VAL A CB 3799 C CG1 . VAL A 495 ? 1.8743 1.9972 1.8436 -0.4803 -0.3277 0.3166 495 VAL A CG1 3800 C CG2 . VAL A 495 ? 1.6725 1.6691 1.6576 -0.4382 -0.3059 0.2489 495 VAL A CG2 3801 N N . GLU A 496 ? 1.4698 1.5546 1.4093 -0.4269 -0.2814 0.1558 496 GLU A N 3802 C CA . GLU A 496 ? 1.5290 1.6305 1.4711 -0.4188 -0.2842 0.1198 496 GLU A CA 3803 C C . GLU A 496 ? 1.3698 1.4094 1.3322 -0.4112 -0.2901 0.1281 496 GLU A C 3804 O O . GLU A 496 ? 1.3186 1.2955 1.2966 -0.4037 -0.2865 0.1373 496 GLU A O 3805 C CB . GLU A 496 ? 1.6545 1.7551 1.6034 -0.4046 -0.2768 0.0674 496 GLU A CB 3806 C CG . GLU A 496 ? 1.7030 1.8215 1.6671 -0.3952 -0.2851 0.0249 496 GLU A CG 3807 C CD . GLU A 496 ? 1.8332 2.0517 1.7802 -0.4034 -0.2908 0.0088 496 GLU A CD 3808 O OE1 . GLU A 496 ? 1.8691 2.1072 1.8284 -0.3979 -0.3005 -0.0190 496 GLU A OE1 3809 O OE2 . GLU A 496 ? 1.8457 2.1308 1.7687 -0.4165 -0.2866 0.0246 496 GLU A OE2 3810 N N . LEU A 497 ? 1.2819 1.3479 1.2445 -0.4133 -0.2993 0.1233 497 LEU A N 3811 C CA . LEU A 497 ? 1.2718 1.2886 1.2533 -0.4064 -0.3054 0.1287 497 LEU A CA 3812 C C . LEU A 497 ? 1.3604 1.3800 1.3535 -0.3967 -0.3090 0.0886 497 LEU A C 3813 O O . LEU A 497 ? 1.4832 1.5615 1.4687 -0.3989 -0.3138 0.0640 497 LEU A O 3814 C CB . LEU A 497 ? 1.2810 1.3155 1.2615 -0.4184 -0.3178 0.1671 497 LEU A CB 3815 C CG . LEU A 497 ? 1.3309 1.3133 1.3324 -0.4180 -0.3233 0.2019 497 LEU A CG 3816 C CD1 . LEU A 497 ? 1.3993 1.3732 1.4009 -0.4218 -0.3190 0.2180 497 LEU A CD1 3817 C CD2 . LEU A 497 ? 1.3493 1.3497 1.3603 -0.4297 -0.3410 0.2375 497 LEU A CD2 3818 N N . LEU A 498 ? 1.3974 1.3605 1.4138 -0.3869 -0.3091 0.0823 498 LEU A N 3819 C CA . LEU A 498 ? 1.4868 1.4442 1.5263 -0.3794 -0.3179 0.0510 498 LEU A CA 3820 C C . LEU A 498 ? 1.3883 1.3127 1.4437 -0.3782 -0.3246 0.0685 498 LEU A C 3821 O O . LEU A 498 ? 1.3763 1.2641 1.4394 -0.3767 -0.3198 0.0901 498 LEU A O 3822 C CB . LEU A 498 ? 1.7548 1.6855 1.8178 -0.3717 -0.3164 0.0269 498 LEU A CB 3823 C CG . LEU A 498 ? 1.9399 1.9043 1.9944 -0.3700 -0.3113 0.0002 498 LEU A CG 3824 C CD1 . LEU A 498 ? 1.9398 1.8693 2.0270 -0.3624 -0.3137 -0.0200 498 LEU A CD1 3825 C CD2 . LEU A 498 ? 1.8425 1.8754 1.8929 -0.3694 -0.3199 -0.0354 498 LEU A CD2 3826 N N . LEU A 499 ? 1.3550 1.3004 1.4168 -0.3785 -0.3362 0.0559 499 LEU A N 3827 C CA . LEU A 499 ? 1.3351 1.2559 1.4125 -0.3779 -0.3437 0.0707 499 LEU A CA 3828 C C . LEU A 499 ? 1.5058 1.4023 1.6206 -0.3731 -0.3541 0.0527 499 LEU A C 3829 O O . LEU A 499 ? 1.5107 1.4212 1.6447 -0.3694 -0.3643 0.0190 499 LEU A O 3830 C CB . LEU A 499 ? 1.2955 1.2525 1.3607 -0.3829 -0.3522 0.0733 499 LEU A CB 3831 C CG . LEU A 499 ? 1.3471 1.3343 1.3843 -0.3926 -0.3485 0.1015 499 LEU A CG 3832 C CD1 . LEU A 499 ? 1.3278 1.3559 1.3567 -0.3998 -0.3591 0.1075 499 LEU A CD1 3833 C CD2 . LEU A 499 ? 1.4775 1.4239 1.5198 -0.3924 -0.3442 0.1352 499 LEU A CD2 3834 N N . ASP A 500 ? 1.5279 1.3950 1.6593 -0.3737 -0.3546 0.0752 500 ASP A N 3835 C CA . ASP A 500 ? 1.4375 1.2868 1.6102 -0.3743 -0.3678 0.0720 500 ASP A CA 3836 C C . ASP A 500 ? 1.3709 1.2091 1.5670 -0.3729 -0.3708 0.0555 500 ASP A C 3837 O O . ASP A 500 ? 1.3604 1.1981 1.5934 -0.3711 -0.3896 0.0306 500 ASP A O 3838 C CB . ASP A 500 ? 1.3327 1.1928 1.5266 -0.3744 -0.3872 0.0555 500 ASP A CB 3839 C CG . ASP A 500 ? 1.3463 1.1904 1.5792 -0.3795 -0.4018 0.0738 500 ASP A CG 3840 O OD1 . ASP A 500 ? 1.6288 1.4610 1.8781 -0.3840 -0.3992 0.0950 500 ASP A OD1 3841 O OD2 . ASP A 500 ? 1.1951 1.0456 1.4432 -0.3805 -0.4166 0.0691 500 ASP A OD2 3842 N N . LYS A 501 ? 1.4955 1.3247 1.6758 -0.3729 -0.3548 0.0675 501 LYS A N 3843 C CA . LYS A 501 ? 1.4543 1.2725 1.6540 -0.3720 -0.3557 0.0554 501 LYS A CA 3844 C C . LYS A 501 ? 1.4153 1.2183 1.6716 -0.3772 -0.3770 0.0605 501 LYS A C 3845 O O . LYS A 501 ? 1.2509 1.0449 1.5406 -0.3761 -0.3885 0.0432 501 LYS A O 3846 C CB . LYS A 501 ? 1.4089 1.2196 1.5843 -0.3725 -0.3353 0.0746 501 LYS A CB 3847 C CG . LYS A 501 ? 1.4554 1.2566 1.6441 -0.3716 -0.3333 0.0632 501 LYS A CG 3848 C CD . LYS A 501 ? 1.5064 1.3004 1.6807 -0.3735 -0.3161 0.0860 501 LYS A CD 3849 C CE . LYS A 501 ? 1.5473 1.3314 1.7360 -0.3736 -0.3146 0.0773 501 LYS A CE 3850 N NZ . LYS A 501 ? 1.4910 1.2731 1.6658 -0.3753 -0.2977 0.0973 501 LYS A NZ 3851 N N . LEU A 502 ? 1.5976 1.4015 1.8704 -0.3841 -0.3853 0.0857 502 LEU A N 3852 C CA . LEU A 502 ? 1.5525 1.3497 1.8834 -0.3943 -0.4087 0.1033 502 LEU A CA 3853 C C . LEU A 502 ? 1.4738 1.2618 1.8541 -0.3913 -0.4386 0.0728 502 LEU A C 3854 O O . LEU A 502 ? 1.6034 1.3780 2.0320 -0.3919 -0.4573 0.0601 502 LEU A O 3855 C CB . LEU A 502 ? 1.5438 1.3577 1.8781 -0.4038 -0.4100 0.1392 502 LEU A CB 3856 C CG . LEU A 502 ? 1.5419 1.3767 1.8444 -0.4059 -0.3862 0.1645 502 LEU A CG 3857 C CD1 . LEU A 502 ? 1.4054 1.2709 1.7210 -0.4152 -0.3917 0.1940 502 LEU A CD1 3858 C CD2 . LEU A 502 ? 1.3757 1.2121 1.6905 -0.4113 -0.3813 0.1755 502 LEU A CD2 3859 N N . LYS A 503 ? 1.5756 1.3723 1.9495 -0.3872 -0.4454 0.0581 503 LYS A N 3860 C CA . LYS A 503 ? 1.6677 1.4624 2.0917 -0.3817 -0.4752 0.0204 503 LYS A CA 3861 C C . LYS A 503 ? 1.8770 1.6902 2.2785 -0.3675 -0.4675 -0.0311 503 LYS A C 3862 O O . LYS A 503 ? 2.0327 1.8722 2.3771 -0.3630 -0.4468 -0.0401 503 LYS A O 3863 C CB . LYS A 503 ? 1.4731 1.2762 1.9021 -0.3836 -0.4870 0.0238 503 LYS A CB 3864 C CG . LYS A 503 ? 1.5647 1.3603 2.0274 -0.3990 -0.5009 0.0720 503 LYS A CG 3865 C CD . LYS A 503 ? 1.6638 1.4656 2.1423 -0.4002 -0.5181 0.0700 503 LYS A CD 3866 C CE . LYS A 503 ? 1.5595 1.3618 2.0815 -0.4180 -0.5371 0.1192 503 LYS A CE 3867 N NZ . LYS A 503 ? 1.6556 1.4443 2.2477 -0.4202 -0.5621 0.1312 503 LYS A NZ 3868 N N . GLN A 504 ? 1.8035 1.6099 2.2561 -0.3618 -0.4869 -0.0636 504 GLN A N 3869 C CA . GLN A 504 ? 1.7368 1.5731 2.1775 -0.3478 -0.4824 -0.1185 504 GLN A CA 3870 C C . GLN A 504 ? 1.6675 1.4955 2.1982 -0.3395 -0.5213 -0.1633 504 GLN A C 3871 O O . GLN A 504 ? 1.4918 1.2908 2.0911 -0.3459 -0.5534 -0.1486 504 GLN A O 3872 C CB . GLN A 504 ? 1.7420 1.5823 2.1292 -0.3481 -0.4511 -0.1064 504 GLN A CB 3873 C CG . GLN A 504 ? 1.7906 1.6831 2.1258 -0.3397 -0.4325 -0.1415 504 GLN A CG 3874 C CD . GLN A 504 ? 1.9183 1.8134 2.1944 -0.3438 -0.4010 -0.1156 504 GLN A CD 3875 O OE1 . GLN A 504 ? 1.9797 1.8371 2.2523 -0.3504 -0.3914 -0.0771 504 GLN A OE1 3876 N NE2 . GLN A 504 ? 1.8316 1.7788 2.0638 -0.3410 -0.3863 -0.1358 504 GLN A NE2 3877 N N . LYS A 505 ? 1.7869 1.6443 2.3228 -0.3258 -0.5213 -0.2175 505 LYS A N 3878 C CA . LYS A 505 ? 1.8814 1.7477 2.5059 -0.3114 -0.5608 -0.2821 505 LYS A CA 3879 C C . LYS A 505 ? 1.9268 1.8020 2.5895 -0.3062 -0.5852 -0.3009 505 LYS A C 3880 O O . LYS A 505 ? 2.0662 1.9771 2.6748 -0.3082 -0.5705 -0.3044 505 LYS A O 3881 C CB . LYS A 505 ? 2.0881 1.9092 2.7752 -0.3066 -0.5732 -0.2621 505 LYS A CB 3882 C CG . LYS A 505 ? 2.1096 1.8837 2.8269 -0.3170 -0.5808 -0.1913 505 LYS A CG 3883 C CD . LYS A 505 ? 2.1711 1.9248 2.8412 -0.3383 -0.5568 -0.1282 505 LYS A CD 3884 C CE . LYS A 505 ? 2.0762 1.8080 2.7714 -0.3492 -0.5639 -0.0602 505 LYS A CE 3885 N NZ . LYS A 505 ? 1.9359 1.6638 2.5847 -0.3681 -0.5390 -0.0037 505 LYS A NZ 3886 N N . GLY A 506 ? 1.8445 1.6933 2.5826 -0.2914 -0.6080 -0.3025 506 GLY A N 3887 C CA . GLY A 506 ? 1.7555 1.6042 2.5227 -0.2876 -0.6262 -0.3039 506 GLY A CA 3888 C C . GLY A 506 ? 1.7228 1.5416 2.4540 -0.3126 -0.6169 -0.2295 506 GLY A C 3889 O O . GLY A 506 ? 1.8410 1.6225 2.5878 -0.3223 -0.6163 -0.1710 506 GLY A O 3890 N N . ALA A 507 ? 1.5538 1.3974 2.2398 -0.3220 -0.6111 -0.2323 507 ALA A N 3891 C CA . ALA A 507 ? 1.5930 1.4175 2.2385 -0.3447 -0.6006 -0.1677 507 ALA A CA 3892 C C . ALA A 507 ? 1.7479 1.6124 2.3265 -0.3419 -0.5802 -0.1791 507 ALA A C 3893 O O . ALA A 507 ? 1.8161 1.7291 2.3806 -0.3285 -0.5780 -0.2351 507 ALA A O 3894 C CB . ALA A 507 ? 1.5226 1.3302 2.1139 -0.3566 -0.5686 -0.1153 507 ALA A CB 3895 N N . ILE A 508 ? 1.7579 1.6103 2.2967 -0.3544 -0.5648 -0.1250 508 ILE A N 3896 C CA . ILE A 508 ? 1.6807 1.5666 2.1500 -0.3537 -0.5412 -0.1218 508 ILE A CA 3897 C C . ILE A 508 ? 1.7800 1.6759 2.1692 -0.3569 -0.5012 -0.0942 508 ILE A C 3898 O O . ILE A 508 ? 1.9398 1.8066 2.3184 -0.3644 -0.4882 -0.0532 508 ILE A O 3899 C CB . ILE A 508 ? 1.8198 1.6895 2.2940 -0.3641 -0.5486 -0.0815 508 ILE A CB 3900 C CG1 . ILE A 508 ? 1.9315 1.7608 2.4607 -0.3769 -0.5673 -0.0378 508 ILE A CG1 3901 C CG2 . ILE A 508 ? 1.8198 1.7122 2.3259 -0.3574 -0.5734 -0.1209 508 ILE A CG2 3902 C CD1 . ILE A 508 ? 1.9531 1.7760 2.4938 -0.3887 -0.5773 0.0026 508 ILE A CD1 3903 N N . ARG A 509 ? 1.9586 1.9021 2.2967 -0.3523 -0.4844 -0.1157 509 ARG A N 3904 C CA . ARG A 509 ? 2.0340 1.9897 2.3045 -0.3568 -0.4523 -0.0877 509 ARG A CA 3905 C C . ARG A 509 ? 1.8241 1.7585 2.0632 -0.3659 -0.4392 -0.0347 509 ARG A C 3906 O O . ARG A 509 ? 1.9341 1.8468 2.1500 -0.3699 -0.4216 -0.0009 509 ARG A O 3907 C CB . ARG A 509 ? 2.1338 2.1586 2.3662 -0.3538 -0.4434 -0.1190 509 ARG A CB 3908 C CG . ARG A 509 ? 2.1534 2.2154 2.4138 -0.3428 -0.4535 -0.1785 509 ARG A CG 3909 C CD . ARG A 509 ? 2.1111 2.2645 2.3476 -0.3400 -0.4529 -0.2189 509 ARG A CD 3910 N NE . ARG A 509 ? 2.0591 2.2617 2.3243 -0.3275 -0.4623 -0.2835 509 ARG A NE 3911 C CZ . ARG A 509 ? 1.9954 2.2033 2.3309 -0.3130 -0.4922 -0.3434 509 ARG A CZ 3912 N NH1 . ARG A 509 ? 1.9698 2.1341 2.3525 -0.3116 -0.5159 -0.3411 509 ARG A NH1 3913 N NH2 . ARG A 509 ? 1.9403 2.1993 2.3050 -0.2996 -0.5012 -0.4072 509 ARG A NH2 3914 N N . ARG A 510 ? 1.5417 1.4878 1.7833 -0.3677 -0.4491 -0.0329 510 ARG A N 3915 C CA . ARG A 510 ? 1.3440 1.2730 1.5685 -0.3744 -0.4428 0.0101 510 ARG A CA 3916 C C . ARG A 510 ? 1.4244 1.3711 1.5956 -0.3780 -0.4221 0.0351 510 ARG A C 3917 O O . ARG A 510 ? 1.3837 1.3271 1.5431 -0.3817 -0.4204 0.0617 510 ARG A O 3918 C CB . ARG A 510 ? 1.2145 1.1032 1.4641 -0.3787 -0.4433 0.0420 510 ARG A CB 3919 C CG . ARG A 510 ? 1.3642 1.2347 1.6772 -0.3808 -0.4706 0.0336 510 ARG A CG 3920 C CD . ARG A 510 ? 1.3205 1.1678 1.6568 -0.3885 -0.4700 0.0675 510 ARG A CD 3921 N NE . ARG A 510 ? 1.2508 1.1028 1.5598 -0.3939 -0.4539 0.1064 510 ARG A NE 3922 C CZ . ARG A 510 ? 1.2859 1.1372 1.5901 -0.3982 -0.4410 0.1325 510 ARG A CZ 3923 N NH1 . ARG A 510 ? 1.3210 1.1619 1.6423 -0.3997 -0.4413 0.1299 510 ARG A NH1 3924 N NH2 . ARG A 510 ? 1.4270 1.2934 1.7122 -0.4002 -0.4286 0.1578 510 ARG A NH2 3925 N N . ALA A 511 ? 1.5831 1.5502 1.7282 -0.3777 -0.4096 0.0277 511 ALA A N 3926 C CA . ALA A 511 ? 1.4352 1.4211 1.5402 -0.3838 -0.3961 0.0557 511 ALA A CA 3927 C C . ALA A 511 ? 1.3963 1.4352 1.4771 -0.3865 -0.3907 0.0374 511 ALA A C 3928 O O . ALA A 511 ? 1.4432 1.4872 1.5332 -0.3812 -0.3891 0.0087 511 ALA A O 3929 C CB . ALA A 511 ? 1.3272 1.2726 1.4290 -0.3837 -0.3840 0.0873 511 ALA A CB 3930 N N . LEU A 512 ? 1.3395 1.4244 1.3926 -0.3963 -0.3896 0.0561 512 LEU A N 3931 C CA . LEU A 512 ? 1.3995 1.5538 1.4274 -0.4035 -0.3852 0.0471 512 LEU A CA 3932 C C . LEU A 512 ? 1.4043 1.5815 1.4078 -0.4191 -0.3828 0.0979 512 LEU A C 3933 O O . LEU A 512 ? 1.4161 1.5609 1.4256 -0.4224 -0.3878 0.1320 512 LEU A O 3934 C CB . LEU A 512 ? 1.4764 1.7049 1.5062 -0.4023 -0.3953 0.0035 512 LEU A CB 3935 C CG . LEU A 512 ? 1.5045 1.7225 1.5726 -0.3866 -0.4063 -0.0546 512 LEU A CG 3936 C CD1 . LEU A 512 ? 1.4665 1.6463 1.5624 -0.3825 -0.4205 -0.0557 512 LEU A CD1 3937 C CD2 . LEU A 512 ? 1.6779 1.9917 1.7452 -0.3835 -0.4117 -0.1089 512 LEU A CD2 3938 N N . PHE A 513 ? 1.4095 1.6460 1.3917 -0.4293 -0.3782 0.1038 513 PHE A N 3939 C CA . PHE A 513 ? 1.5449 1.8137 1.5126 -0.4486 -0.3822 0.1576 513 PHE A CA 3940 C C . PHE A 513 ? 1.7109 2.0590 1.6674 -0.4630 -0.3936 0.1684 513 PHE A C 3941 O O . PHE A 513 ? 1.6744 2.0837 1.6246 -0.4594 -0.3947 0.1252 513 PHE A O 3942 C CB . PHE A 513 ? 1.6327 1.9419 1.5843 -0.4577 -0.3749 0.1670 513 PHE A CB 3943 C CG . PHE A 513 ? 1.5610 1.7921 1.5234 -0.4470 -0.3650 0.1690 513 PHE A CG 3944 C CD1 . PHE A 513 ? 1.4772 1.6544 1.4535 -0.4509 -0.3690 0.2138 513 PHE A CD1 3945 C CD2 . PHE A 513 ? 1.4077 1.6224 1.3727 -0.4325 -0.3543 0.1239 513 PHE A CD2 3946 C CE1 . PHE A 513 ? 1.3832 1.4977 1.3704 -0.4405 -0.3600 0.2117 513 PHE A CE1 3947 C CE2 . PHE A 513 ? 1.3409 1.4903 1.3151 -0.4243 -0.3452 0.1280 513 PHE A CE2 3948 C CZ . PHE A 513 ? 1.3601 1.4624 1.3428 -0.4282 -0.3468 0.1709 513 PHE A CZ 3949 N N . LEU A 514 ? 1.7748 2.1240 1.7350 -0.4789 -0.4049 0.2246 514 LEU A N 3950 C CA . LEU A 514 ? 1.6816 2.1003 1.6353 -0.4951 -0.4181 0.2453 514 LEU A CA 3951 C C . LEU A 514 ? 1.7214 2.2718 1.6484 -0.5120 -0.4181 0.2362 514 LEU A C 3952 O O . LEU A 514 ? 1.8190 2.4355 1.7368 -0.5098 -0.4193 0.1983 514 LEU A O 3953 C CB . LEU A 514 ? 1.7336 2.1278 1.7066 -0.5111 -0.4347 0.3136 514 LEU A CB 3954 C CG . LEU A 514 ? 1.9534 2.4210 1.9246 -0.5330 -0.4522 0.3500 514 LEU A CG 3955 C CD1 . LEU A 514 ? 1.8820 2.3259 1.8570 -0.5196 -0.4532 0.3199 514 LEU A CD1 3956 C CD2 . LEU A 514 ? 2.0989 2.5453 2.1011 -0.5515 -0.4743 0.4226 514 LEU A CD2 3957 N N . TYR A 515 ? 1.7760 2.3716 1.6934 -0.5289 -0.4177 0.2694 515 TYR A N 3958 C CA . TYR A 515 ? 1.7890 2.5296 1.6812 -0.5508 -0.4193 0.2734 515 TYR A CA 3959 C C . TYR A 515 ? 1.7492 2.5452 1.6263 -0.5342 -0.4044 0.1962 515 TYR A C 3960 O O . TYR A 515 ? 1.6565 2.5484 1.5238 -0.5332 -0.4057 0.1529 515 TYR A O 3961 C CB . TYR A 515 ? 1.9406 2.7127 1.8336 -0.5774 -0.4274 0.3423 515 TYR A CB 3962 C CG . TYR A 515 ? 2.0148 2.7335 1.9378 -0.5936 -0.4494 0.4172 515 TYR A CG 3963 C CD1 . TYR A 515 ? 1.9157 2.7087 1.8422 -0.6182 -0.4686 0.4616 515 TYR A CD1 3964 C CD2 . TYR A 515 ? 2.0849 2.6835 2.0390 -0.5835 -0.4534 0.4405 515 TYR A CD2 3965 C CE1 . TYR A 515 ? 1.9379 2.6800 1.9025 -0.6324 -0.4935 0.5289 515 TYR A CE1 3966 C CE2 . TYR A 515 ? 2.1081 2.6595 2.1017 -0.5952 -0.4780 0.5010 515 TYR A CE2 3967 C CZ . TYR A 515 ? 2.0581 2.6780 2.0592 -0.6196 -0.4992 0.5458 515 TYR A CZ 3968 O OH . TYR A 515 ? 2.1061 2.6772 2.1566 -0.6309 -0.5283 0.6052 515 TYR A OH 3969 N N . SER A 516 ? 1.8057 2.5450 1.6861 -0.5206 -0.3924 0.1766 516 SER A N 3970 C CA . SER A 516 ? 1.7817 2.5663 1.6570 -0.5039 -0.3812 0.1040 516 SER A CA 3971 C C . SER A 516 ? 1.6754 2.4314 1.5709 -0.4778 -0.3830 0.0318 516 SER A C 3972 O O . SER A 516 ? 1.6232 2.4409 1.5247 -0.4643 -0.3813 -0.0367 516 SER A O 3973 C CB . SER A 516 ? 1.7892 2.4974 1.6696 -0.4938 -0.3697 0.1034 516 SER A CB 3974 O OG . SER A 516 ? 1.7336 2.4684 1.6017 -0.5178 -0.3712 0.1686 516 SER A OG 3975 N N . ARG A 517 ? 1.6514 2.3172 1.5638 -0.4708 -0.3893 0.0466 517 ARG A N 3976 C CA . ARG A 517 ? 1.6649 2.2924 1.6037 -0.4489 -0.3953 -0.0104 517 ARG A CA 3977 C C . ARG A 517 ? 1.7426 2.3150 1.7073 -0.4260 -0.3912 -0.0647 517 ARG A C 3978 O O . ARG A 517 ? 1.7402 2.3310 1.7327 -0.4094 -0.4002 -0.1297 517 ARG A O 3979 C CB . ARG A 517 ? 1.7806 2.5294 1.7154 -0.4515 -0.4044 -0.0526 517 ARG A CB 3980 C CG . ARG A 517 ? 1.8934 2.7237 1.8017 -0.4787 -0.4099 0.0029 517 ARG A CG 3981 C CD . ARG A 517 ? 1.7539 2.7328 1.6544 -0.4826 -0.4166 -0.0447 517 ARG A CD 3982 N NE . ARG A 517 ? 1.7374 2.6891 1.6629 -0.4661 -0.4274 -0.0883 517 ARG A NE 3983 C CZ . ARG A 517 ? 1.7732 2.7722 1.6908 -0.4785 -0.4365 -0.0682 517 ARG A CZ 3984 N NH1 . ARG A 517 ? 1.6420 2.6109 1.5856 -0.4622 -0.4470 -0.1106 517 ARG A NH1 3985 N NH2 . ARG A 517 ? 1.8689 2.9472 1.7571 -0.5087 -0.4377 -0.0025 517 ARG A NH2 3986 N N . SER A 518 ? 1.7771 2.2830 1.7390 -0.4256 -0.3807 -0.0376 518 SER A N 3987 C CA . SER A 518 ? 1.7327 2.1937 1.7181 -0.4076 -0.3769 -0.0807 518 SER A CA 3988 C C . SER A 518 ? 1.6874 2.0227 1.6888 -0.4011 -0.3724 -0.0499 518 SER A C 3989 O O . SER A 518 ? 1.7632 2.0578 1.7503 -0.4113 -0.3677 0.0061 518 SER A O 3990 C CB . SER A 518 ? 1.8449 2.3771 1.8093 -0.4135 -0.3667 -0.0889 518 SER A CB 3991 O OG . SER A 518 ? 1.8869 2.4053 1.8239 -0.4319 -0.3579 -0.0206 518 SER A OG 3992 N N . PRO A 519 ? 1.6299 1.9105 1.6672 -0.3845 -0.3766 -0.0875 519 PRO A N 3993 C CA . PRO A 519 ? 1.6158 1.7953 1.6693 -0.3800 -0.3721 -0.0603 519 PRO A CA 3994 C C . PRO A 519 ? 1.7456 1.9091 1.7775 -0.3849 -0.3561 -0.0329 519 PRO A C 3995 O O . PRO A 519 ? 1.8050 1.8996 1.8411 -0.3846 -0.3499 -0.0010 519 PRO A O 3996 C CB . PRO A 519 ? 1.5659 1.7153 1.6696 -0.3649 -0.3861 -0.1089 519 PRO A CB 3997 C CG . PRO A 519 ? 1.6191 1.8524 1.7296 -0.3583 -0.3927 -0.1677 519 PRO A CG 3998 C CD . PRO A 519 ? 1.6877 2.0051 1.7606 -0.3696 -0.3900 -0.1586 519 PRO A CD 3999 N N . SER A 520 ? 1.7346 1.9696 1.7453 -0.3897 -0.3503 -0.0470 520 SER A N 4000 C CA . SER A 520 ? 1.6017 1.8283 1.5936 -0.3951 -0.3367 -0.0227 520 SER A CA 4001 C C . SER A 520 ? 1.6532 1.9597 1.6094 -0.4141 -0.3331 0.0100 520 SER A C 4002 O O . SER A 520 ? 1.6352 2.0253 1.5797 -0.4222 -0.3398 0.0014 520 SER A O 4003 C CB . SER A 520 ? 1.6724 1.9055 1.6816 -0.3830 -0.3345 -0.0707 520 SER A CB 4004 O OG . SER A 520 ? 1.7838 2.1135 1.7938 -0.3800 -0.3408 -0.1214 520 SER A OG 4005 N N . HIS A 521 ? 1.6085 1.8944 1.5513 -0.4228 -0.3248 0.0498 521 HIS A N 4006 C CA . HIS A 521 ? 1.5264 1.8853 1.4439 -0.4448 -0.3258 0.0918 521 HIS A CA 4007 C C . HIS A 521 ? 1.5375 1.8849 1.4474 -0.4491 -0.3165 0.1102 521 HIS A C 4008 O O . HIS A 521 ? 1.5919 1.8552 1.5156 -0.4365 -0.3094 0.1060 521 HIS A O 4009 C CB . HIS A 521 ? 1.5651 1.9007 1.4857 -0.4582 -0.3367 0.1491 521 HIS A CB 4010 C CG . HIS A 521 ? 1.8264 2.2571 1.7299 -0.4849 -0.3461 0.1936 521 HIS A CG 4011 N ND1 . HIS A 521 ? 1.7851 2.2381 1.6836 -0.5024 -0.3480 0.2388 521 HIS A ND1 4012 C CD2 . HIS A 521 ? 1.9815 2.4971 1.8751 -0.4997 -0.3565 0.2042 521 HIS A CD2 4013 C CE1 . HIS A 521 ? 1.9416 2.4914 1.8299 -0.5289 -0.3607 0.2799 521 HIS A CE1 4014 N NE2 . HIS A 521 ? 2.0802 2.6722 1.9636 -0.5278 -0.3651 0.2594 521 HIS A NE2 4015 N N . SER A 522 ? 1.6432 2.0829 1.5321 -0.4685 -0.3173 0.1328 522 SER A N 4016 C CA . SER A 522 ? 1.5107 1.9505 1.3922 -0.4760 -0.3105 0.1554 522 SER A CA 4017 C C . SER A 522 ? 1.5519 2.0293 1.4297 -0.5044 -0.3231 0.2295 522 SER A C 4018 O O . SER A 522 ? 1.7004 2.2504 1.5724 -0.5226 -0.3355 0.2563 522 SER A O 4019 C CB . SER A 522 ? 1.5161 2.0434 1.3824 -0.4727 -0.3011 0.1070 522 SER A CB 4020 O OG . SER A 522 ? 1.6566 2.1490 1.5402 -0.4468 -0.2965 0.0384 522 SER A OG 4021 N N . LYS A 523 ? 1.6120 2.0420 1.4989 -0.5093 -0.3231 0.2644 523 LYS A N 4022 C CA . LYS A 523 ? 1.7057 2.1586 1.6045 -0.5366 -0.3418 0.3389 523 LYS A CA 4023 C C . LYS A 523 ? 1.7625 2.2255 1.6599 -0.5465 -0.3391 0.3622 523 LYS A C 4024 O O . LYS A 523 ? 1.7364 2.1348 1.6345 -0.5273 -0.3240 0.3303 523 LYS A O 4025 C CB . LYS A 523 ? 1.7404 2.0924 1.6761 -0.5316 -0.3569 0.3708 523 LYS A CB 4026 C CG . LYS A 523 ? 1.9058 2.2732 1.8483 -0.5361 -0.3699 0.3811 523 LYS A CG 4027 C CD . LYS A 523 ? 1.9397 2.4055 1.8845 -0.5711 -0.3923 0.4442 523 LYS A CD 4028 C CE . LYS A 523 ? 1.8713 2.3366 1.8314 -0.5763 -0.4089 0.4635 523 LYS A CE 4029 N NZ . LYS A 523 ? 1.8457 2.4032 1.8173 -0.6140 -0.4358 0.5364 523 LYS A NZ 4030 N N . ASN A 524 ? 1.8782 2.4272 1.7762 -0.5786 -0.3556 0.4220 524 ASN A N 4031 C CA . ASN A 524 ? 1.8546 2.4147 1.7585 -0.5932 -0.3591 0.4582 524 ASN A CA 4032 C C . ASN A 524 ? 1.9005 2.3893 1.8545 -0.6060 -0.3873 0.5259 524 ASN A C 4033 O O . ASN A 524 ? 1.9643 2.4994 1.9409 -0.6331 -0.4148 0.5872 524 ASN A O 4034 C CB . ASN A 524 ? 1.8856 2.6039 1.7624 -0.6236 -0.3617 0.4828 524 ASN A CB 4035 C CG . ASN A 524 ? 1.8408 2.6404 1.6775 -0.6083 -0.3368 0.4059 524 ASN A CG 4036 O OD1 . ASN A 524 ? 1.7320 2.5437 1.5538 -0.5982 -0.3201 0.3706 524 ASN A OD1 4037 N ND2 . ASN A 524 ? 1.9042 2.7612 1.7288 -0.6055 -0.3366 0.3769 524 ASN A ND2 4038 N N . MET A 525 ? 1.7451 2.1259 1.7225 -0.5865 -0.3834 0.5136 525 MET A N 4039 C CA . MET A 525 ? 1.7168 2.0244 1.7532 -0.5925 -0.4127 0.5638 525 MET A CA 4040 C C . MET A 525 ? 1.6750 1.9834 1.7309 -0.6066 -0.4227 0.6005 525 MET A C 4041 O O . MET A 525 ? 1.7473 2.0638 1.7716 -0.5978 -0.3986 0.5682 525 MET A O 4042 C CB . MET A 525 ? 1.6384 1.8255 1.6989 -0.5586 -0.4062 0.5210 525 MET A CB 4043 C CG . MET A 525 ? 1.6182 1.7910 1.6818 -0.5495 -0.4094 0.5057 525 MET A CG 4044 S SD . MET A 525 ? 1.8131 1.8630 1.9278 -0.5197 -0.4170 0.4818 525 MET A SD 4045 C CE . MET A 525 ? 1.4669 1.4928 1.6582 -0.5379 -0.4612 0.5480 525 MET A CE 4046 N N . THR A 526 ? 1.6923 1.9911 1.8067 -0.6289 -0.4616 0.6692 526 THR A N 4047 C CA . THR A 526 ? 1.8380 2.1261 1.9864 -0.6430 -0.4790 0.7101 526 THR A CA 4048 C C . THR A 526 ? 1.8898 2.0764 2.1228 -0.6353 -0.5148 0.7334 526 THR A C 4049 O O . THR A 526 ? 1.9849 2.1740 2.2719 -0.6525 -0.5529 0.7835 526 THR A O 4050 C CB . THR A 526 ? 1.8591 2.2725 2.0063 -0.6892 -0.5009 0.7863 526 THR A CB 4051 O OG1 . THR A 526 ? 1.9235 2.4447 1.9956 -0.6935 -0.4675 0.7543 526 THR A OG1 4052 C CG2 . THR A 526 ? 1.7163 2.1144 1.9060 -0.7053 -0.5229 0.8335 526 THR A CG2 4053 N N . ILE A 527 ? 1.7730 1.8755 2.0225 -0.6093 -0.5047 0.6950 527 ILE A N 4054 C CA . ILE A 527 ? 1.7844 1.7972 2.1201 -0.5975 -0.5389 0.7038 527 ILE A CA 4055 C C . ILE A 527 ? 1.6476 1.6557 2.0182 -0.5983 -0.5559 0.7271 527 ILE A C 4056 O O . ILE A 527 ? 1.4344 1.5004 1.7609 -0.6173 -0.5397 0.7436 527 ILE A O 4057 C CB . ILE A 527 ? 1.7282 1.6550 2.0619 -0.5541 -0.5150 0.6254 527 ILE A CB 4058 C CG1 . ILE A 527 ? 1.5914 1.5083 1.8673 -0.5360 -0.4720 0.5740 527 ILE A CG1 4059 C CG2 . ILE A 527 ? 1.7636 1.6965 2.0684 -0.5430 -0.5011 0.5971 527 ILE A CG2 4060 C CD1 . ILE A 527 ? 1.6101 1.4622 1.8778 -0.4985 -0.4467 0.5029 527 ILE A CD1 4061 N N . SER A 528 ? 1.5898 1.5362 2.0410 -0.5733 -0.5883 0.7215 528 SER A N 4062 C CA . SER A 528 ? 1.5036 1.4482 1.9982 -0.5698 -0.6099 0.7411 528 SER A CA 4063 C C . SER A 528 ? 1.5644 1.4197 2.1120 -0.5315 -0.6138 0.6883 528 SER A C 4064 O O . SER A 528 ? 1.7019 1.5116 2.3181 -0.5099 -0.6408 0.6713 528 SER A O 4065 C CB . SER A 528 ? 1.7410 1.7381 2.3043 -0.5891 -0.6647 0.8111 528 SER A CB 4066 O OG . SER A 528 ? 1.7425 1.7055 2.3703 -0.5763 -0.6969 0.8115 528 SER A OG 4067 N N . ARG A 529 ? 1.5674 1.4062 2.0838 -0.5237 -0.5868 0.6609 529 ARG A N 4068 C CA . ARG A 529 ? 1.6190 1.3929 2.1859 -0.4919 -0.5922 0.6176 529 ARG A CA 4069 C C . ARG A 529 ? 1.7854 1.4973 2.3966 -0.4599 -0.5961 0.5613 529 ARG A C 4070 O O . ARG A 529 ? 1.8949 1.5971 2.4636 -0.4574 -0.5699 0.5310 529 ARG A O 4071 C CB . ARG A 529 ? 1.8434 1.6288 2.4907 -0.4939 -0.6407 0.6602 529 ARG A CB 4072 C CG . ARG A 529 ? 2.1471 1.9849 2.7585 -0.5175 -0.6338 0.6989 529 ARG A CG 4073 C CD . ARG A 529 ? 2.1370 1.9362 2.7176 -0.4996 -0.5997 0.6508 529 ARG A CD 4074 N NE . ARG A 529 ? 2.0975 1.8401 2.7616 -0.4695 -0.6261 0.6210 529 ARG A NE 4075 C CZ . ARG A 529 ? 1.9656 1.6758 2.6246 -0.4520 -0.6072 0.5820 529 ARG A CZ 4076 N NH1 . ARG A 529 ? 1.8310 1.5552 2.4063 -0.4614 -0.5623 0.5700 529 ARG A NH1 4077 N NH2 . ARG A 529 ? 1.9185 1.5865 2.6604 -0.4248 -0.6351 0.5533 529 ARG A NH2 4078 N N . GLY A 530 ? 1.6629 1.3403 2.3653 -0.4363 -0.6323 0.5474 530 GLY A N 4079 C CA . GLY A 530 ? 1.7588 1.3878 2.5121 -0.4034 -0.6377 0.4859 530 GLY A CA 4080 C C . GLY A 530 ? 1.9904 1.6184 2.7917 -0.4008 -0.6676 0.4962 530 GLY A C 4081 O O . GLY A 530 ? 2.1032 1.7581 2.9453 -0.4169 -0.7061 0.5544 530 GLY A O 4082 N N . GLY A 531 ? 1.9666 1.5690 2.7659 -0.3815 -0.6519 0.4404 531 GLY A N 4083 C CA . GLY A 531 ? 1.9386 1.5377 2.7811 -0.3763 -0.6768 0.4418 531 GLY A CA 4084 C C . GLY A 531 ? 2.0477 1.6856 2.8347 -0.4096 -0.6720 0.5005 531 GLY A C 4085 O O . GLY A 531 ? 2.0450 1.7122 2.7451 -0.4334 -0.6376 0.5209 531 GLY A O 4086 N N . LEU A 532 ? 2.1710 1.8140 3.0125 -0.4106 -0.7081 0.5252 532 LEU A N 4087 C CA . LEU A 532 ? 2.0694 1.7566 2.8695 -0.4420 -0.7097 0.5815 532 LEU A CA 4088 C C . LEU A 532 ? 1.7872 1.4877 2.4821 -0.4555 -0.6573 0.5616 532 LEU A C 4089 O O . LEU A 532 ? 1.7839 1.5294 2.4070 -0.4835 -0.6347 0.5948 532 LEU A O 4090 C CB . LEU A 532 ? 2.0921 1.8335 2.8904 -0.4726 -0.7307 0.6560 532 LEU A CB 4091 C CG . LEU A 532 ? 2.0830 1.8325 2.9923 -0.4717 -0.7960 0.7010 532 LEU A CG 4092 C CD1 . LEU A 532 ? 2.0795 1.8988 2.9792 -0.5076 -0.8141 0.7763 532 LEU A CD1 4093 C CD2 . LEU A 532 ? 1.9618 1.7102 2.9217 -0.4696 -0.8273 0.7137 532 LEU A CD2 4094 N N . MET A 533 ? 1.6460 1.3144 2.3375 -0.4360 -0.6408 0.5059 533 MET A N 4095 C CA . MET A 533 ? 1.6503 1.3339 2.2509 -0.4437 -0.5954 0.4831 533 MET A CA 4096 C C . MET A 533 ? 1.5954 1.3200 2.1722 -0.4682 -0.6034 0.5290 533 MET A C 4097 O O . MET A 533 ? 1.8612 1.5735 2.4969 -0.4669 -0.6358 0.5405 533 MET A O 4098 C CB . MET A 533 ? 1.4798 1.1371 2.0810 -0.4065 -0.5745 0.4081 533 MET A CB 4099 C CG . MET A 533 ? 1.5191 1.1990 2.0215 -0.3987 -0.5210 0.3729 533 MET A CG 4100 S SD . MET A 533 ? 2.1261 1.7876 2.6335 -0.3598 -0.4964 0.2920 533 MET A SD 4101 C CE . MET A 533 ? 1.5845 1.2732 1.9814 -0.3623 -0.4410 0.2740 533 MET A CE 4102 N N . GLN A 534 ? 1.5384 1.3172 2.0324 -0.4895 -0.5751 0.5519 534 GLN A N 4103 C CA . GLN A 534 ? 1.7467 1.5805 2.2184 -0.5157 -0.5840 0.5976 534 GLN A CA 4104 C C . GLN A 534 ? 1.7411 1.5801 2.1565 -0.4985 -0.5515 0.5516 534 GLN A C 4105 O O . GLN A 534 ? 1.5514 1.3585 1.9399 -0.4703 -0.5209 0.4911 534 GLN A O 4106 C CB . GLN A 534 ? 1.6881 1.5967 2.1063 -0.5485 -0.5741 0.6434 534 GLN A CB 4107 C CG . GLN A 534 ? 1.8225 1.8030 2.2485 -0.5857 -0.6019 0.7139 534 GLN A CG 4108 C CD . GLN A 534 ? 1.8559 1.9305 2.2271 -0.6176 -0.5899 0.7533 534 GLN A CD 4109 O OE1 . GLN A 534 ? 1.6964 1.7743 2.0297 -0.6114 -0.5637 0.7293 534 GLN A OE1 4110 N NE2 . GLN A 534 ? 1.9380 2.0986 2.3057 -0.6526 -0.6095 0.8133 534 GLN A NE2 4111 N N . CYS A 535 ? 1.7296 1.6149 2.1289 -0.5176 -0.5597 0.5836 535 CYS A N 4112 C CA . CYS A 535 ? 1.6996 1.5907 2.0547 -0.5037 -0.5355 0.5458 535 CYS A CA 4113 C C . CYS A 535 ? 1.6568 1.6272 1.9669 -0.5313 -0.5337 0.5816 535 CYS A C 4114 O O . CYS A 535 ? 1.7774 1.7944 2.1147 -0.5624 -0.5645 0.6463 535 CYS A O 4115 C CB . CYS A 535 ? 1.7500 1.5905 2.1691 -0.4846 -0.5590 0.5297 535 CYS A CB 4116 S SG . CYS A 535 ? 2.0509 1.8191 2.5179 -0.4456 -0.5554 0.4666 535 CYS A SG 4117 N N . GLU A 536 ? 1.5264 1.5183 1.7730 -0.5209 -0.5004 0.5402 536 GLU A N 4118 C CA . GLU A 536 ? 1.7069 1.7770 1.9144 -0.5416 -0.4984 0.5606 536 GLU A CA 4119 C C . GLU A 536 ? 1.6419 1.6932 1.8266 -0.5215 -0.4815 0.5154 536 GLU A C 4120 O O . GLU A 536 ? 1.5404 1.5295 1.7281 -0.4936 -0.4656 0.4677 536 GLU A O 4121 C CB . GLU A 536 ? 1.7655 1.9136 1.9118 -0.5559 -0.4751 0.5570 536 GLU A CB 4122 C CG . GLU A 536 ? 1.8203 2.0127 1.9849 -0.5841 -0.4945 0.6142 536 GLU A CG 4123 C CD . GLU A 536 ? 1.8945 2.1966 2.0002 -0.6041 -0.4765 0.6175 536 GLU A CD 4124 O OE1 . GLU A 536 ? 1.8840 2.2394 1.9441 -0.6006 -0.4574 0.5839 536 GLU A OE1 4125 O OE2 . GLU A 536 ? 2.0629 2.4030 2.1716 -0.6228 -0.4829 0.6512 536 GLU A OE2 4126 N N . GLU A 537 ? 1.6104 1.7226 1.7742 -0.5373 -0.4861 0.5323 537 GLU A N 4127 C CA . GLU A 537 ? 1.6422 1.7381 1.7914 -0.5210 -0.4754 0.4961 537 GLU A CA 4128 C C . GLU A 537 ? 1.7757 1.9524 1.8709 -0.5312 -0.4603 0.4824 537 GLU A C 4129 O O . GLU A 537 ? 2.0659 2.3287 2.1496 -0.5589 -0.4720 0.5219 537 GLU A O 4130 C CB . GLU A 537 ? 1.7983 1.8639 2.0043 -0.5232 -0.5074 0.5270 537 GLU A CB 4131 C CG . GLU A 537 ? 1.7854 1.7637 2.0451 -0.4978 -0.5159 0.5049 537 GLU A CG 4132 C CD . GLU A 537 ? 1.8771 1.8309 2.1948 -0.4960 -0.5470 0.5236 537 GLU A CD 4133 O OE1 . GLU A 537 ? 1.9134 1.9018 2.2621 -0.5218 -0.5789 0.5810 537 GLU A OE1 4134 O OE2 . GLU A 537 ? 1.7956 1.7021 2.1303 -0.4700 -0.5410 0.4824 537 GLU A OE2 4135 N N . LEU A 538 ? 1.7027 1.8570 1.7703 -0.5090 -0.4368 0.4257 538 LEU A N 4136 C CA . LEU A 538 ? 1.8315 2.0467 1.8623 -0.5115 -0.4268 0.4003 538 LEU A CA 4137 C C . LEU A 538 ? 1.9167 2.0683 1.9574 -0.4887 -0.4213 0.3657 538 LEU A C 4138 O O . LEU A 538 ? 1.8635 1.9439 1.9195 -0.4690 -0.4127 0.3434 538 LEU A O 4139 C CB . LEU A 538 ? 1.8608 2.1247 1.8512 -0.5079 -0.4042 0.3586 538 LEU A CB 4140 C CG . LEU A 538 ? 2.0214 2.3388 2.0006 -0.5251 -0.4037 0.3829 538 LEU A CG 4141 C CD1 . LEU A 538 ? 1.9115 2.1981 1.8750 -0.5063 -0.3806 0.3352 538 LEU A CD1 4142 C CD2 . LEU A 538 ? 2.1280 2.5751 2.0801 -0.5501 -0.4085 0.3981 538 LEU A CD2 4143 N N . ILE A 539 ? 1.8997 2.0803 1.9336 -0.4918 -0.4267 0.3620 539 ILE A N 4144 C CA . ILE A 539 ? 1.6484 1.7654 1.6978 -0.4715 -0.4239 0.3362 539 ILE A CA 4145 C C . ILE A 539 ? 1.4355 1.5661 1.4643 -0.4614 -0.4133 0.2926 539 ILE A C 4146 O O . ILE A 539 ? 1.4752 1.6494 1.4969 -0.4700 -0.4217 0.2977 539 ILE A O 4147 C CB . ILE A 539 ? 1.6676 1.7667 1.7540 -0.4781 -0.4483 0.3763 539 ILE A CB 4148 C CG1 . ILE A 539 ? 1.5669 1.7460 1.6445 -0.5043 -0.4649 0.4147 539 ILE A CG1 4149 C CG2 . ILE A 539 ? 1.7046 1.7593 1.8340 -0.4780 -0.4633 0.4060 539 ILE A CG2 4150 C CD1 . ILE A 539 ? 1.4564 1.6198 1.5732 -0.5110 -0.4910 0.4522 539 ILE A CD1 4151 N N . ALA A 540 ? 1.4583 1.5515 1.4831 -0.4438 -0.3972 0.2512 540 ALA A N 4152 C CA . ALA A 540 ? 1.4246 1.4688 1.4632 -0.4273 -0.3936 0.2250 540 ALA A CA 4153 C C . ALA A 540 ? 1.4825 1.5391 1.5248 -0.4280 -0.4033 0.2229 540 ALA A C 4154 O O . ALA A 540 ? 1.5003 1.5252 1.5635 -0.4250 -0.4116 0.2412 540 ALA A O 4155 C CB . ALA A 540 ? 1.4190 1.4025 1.4840 -0.4173 -0.3934 0.2373 540 ALA A CB 4156 N N . TYR A 541 ? 1.4977 1.6029 1.5243 -0.4309 -0.4039 0.1976 541 TYR A N 4157 C CA . TYR A 541 ? 1.4416 1.5481 1.4759 -0.4285 -0.4124 0.1894 541 TYR A CA 4158 C C . TYR A 541 ? 1.4353 1.5056 1.4846 -0.4136 -0.4088 0.1507 541 TYR A C 4159 O O . TYR A 541 ? 1.4348 1.5081 1.4847 -0.4079 -0.4030 0.1199 541 TYR A O 4160 C CB . TYR A 541 ? 1.4317 1.6197 1.4474 -0.4416 -0.4203 0.1872 541 TYR A CB 4161 C CG . TYR A 541 ? 1.4795 1.7152 1.4876 -0.4359 -0.4177 0.1345 541 TYR A CG 4162 C CD1 . TYR A 541 ? 1.4676 1.6952 1.4917 -0.4261 -0.4246 0.1002 541 TYR A CD1 4163 C CD2 . TYR A 541 ? 1.7614 2.0558 1.7526 -0.4403 -0.4114 0.1168 541 TYR A CD2 4164 C CE1 . TYR A 541 ? 1.5555 1.8267 1.5860 -0.4187 -0.4280 0.0458 541 TYR A CE1 4165 C CE2 . TYR A 541 ? 1.8696 2.2144 1.8629 -0.4322 -0.4122 0.0599 541 TYR A CE2 4166 C CZ . TYR A 541 ? 1.7348 2.0657 1.7512 -0.4206 -0.4219 0.0226 541 TYR A CZ 4167 O OH . TYR A 541 ? 1.8695 2.2498 1.9010 -0.4102 -0.4282 -0.0403 541 TYR A OH 4168 N N . LEU A 542 ? 1.4621 1.5008 1.5292 -0.4087 -0.4149 0.1553 542 LEU A N 4169 C CA . LEU A 542 ? 1.3119 1.3179 1.4017 -0.3989 -0.4165 0.1311 542 LEU A CA 4170 C C . LEU A 542 ? 1.3192 1.3549 1.4163 -0.3987 -0.4286 0.1025 542 LEU A C 4171 O O . LEU A 542 ? 1.4045 1.4750 1.4905 -0.4051 -0.4353 0.1099 542 LEU A O 4172 C CB . LEU A 542 ? 1.2641 1.2298 1.3724 -0.3947 -0.4171 0.1530 542 LEU A CB 4173 C CG . LEU A 542 ? 1.2539 1.1911 1.3888 -0.3890 -0.4185 0.1427 542 LEU A CG 4174 C CD1 . LEU A 542 ? 1.3290 1.2498 1.4677 -0.3859 -0.4091 0.1341 542 LEU A CD1 4175 C CD2 . LEU A 542 ? 1.2312 1.1535 1.3809 -0.3867 -0.4194 0.1642 542 LEU A CD2 4176 N N . ARG A 543 ? 1.3132 1.3362 1.4356 -0.3918 -0.4346 0.0702 543 ARG A N 4177 C CA . ARG A 543 ? 1.3851 1.4379 1.5255 -0.3892 -0.4505 0.0335 543 ARG A CA 4178 C C . ARG A 543 ? 1.5768 1.6156 1.7331 -0.3906 -0.4624 0.0459 543 ARG A C 4179 O O . ARG A 543 ? 1.6397 1.6493 1.7927 -0.3932 -0.4576 0.0817 543 ARG A O 4180 C CB . ARG A 543 ? 1.3954 1.4324 1.5741 -0.3808 -0.4604 -0.0045 543 ARG A CB 4181 C CG . ARG A 543 ? 1.5067 1.6015 1.6940 -0.3753 -0.4705 -0.0587 543 ARG A CG 4182 C CD . ARG A 543 ? 1.5983 1.6845 1.8106 -0.3673 -0.4725 -0.0909 543 ARG A CD 4183 N NE . ARG A 543 ? 1.6988 1.8561 1.9160 -0.3604 -0.4796 -0.1482 543 ARG A NE 4184 C CZ . ARG A 543 ? 1.6454 1.8169 1.8782 -0.3526 -0.4800 -0.1842 543 ARG A CZ 4185 N NH1 . ARG A 543 ? 1.5541 1.6679 1.7974 -0.3520 -0.4737 -0.1642 543 ARG A NH1 4186 N NH2 . ARG A 543 ? 1.5116 1.7629 1.7507 -0.3450 -0.4872 -0.2424 543 ARG A NH2 4187 N N . ASP A 544 ? 1.6478 1.7125 1.8250 -0.3879 -0.4793 0.0119 544 ASP A N 4188 C CA . ASP A 544 ? 1.6859 1.7455 1.8782 -0.3898 -0.4925 0.0196 544 ASP A CA 4189 C C . ASP A 544 ? 1.6275 1.6316 1.8528 -0.3899 -0.4990 0.0435 544 ASP A C 4190 O O . ASP A 544 ? 1.5770 1.5525 1.8307 -0.3878 -0.5026 0.0396 544 ASP A O 4191 C CB . ASP A 544 ? 1.9270 2.0276 2.1443 -0.3848 -0.5123 -0.0306 544 ASP A CB 4192 C CG . ASP A 544 ? 2.1398 2.2165 2.3960 -0.3844 -0.5330 -0.0308 544 ASP A CG 4193 O OD1 . ASP A 544 ? 2.1537 2.2009 2.4638 -0.3798 -0.5527 -0.0502 544 ASP A OD1 4194 O OD2 . ASP A 544 ? 2.1686 2.2569 2.4060 -0.3898 -0.5321 -0.0091 544 ASP A OD2 4195 N N . GLU A 545 ? 1.6725 1.6692 1.8952 -0.3940 -0.5013 0.0708 545 GLU A N 4196 C CA . GLU A 545 ? 1.6832 1.6467 1.9371 -0.3966 -0.5087 0.0949 545 GLU A CA 4197 C C . GLU A 545 ? 1.7992 1.7514 2.1081 -0.3964 -0.5343 0.0720 545 GLU A C 4198 O O . GLU A 545 ? 1.9863 1.9569 2.3123 -0.3937 -0.5514 0.0414 545 GLU A O 4199 C CB . GLU A 545 ? 1.9056 1.8743 2.1498 -0.4001 -0.5094 0.1207 545 GLU A CB 4200 C CG . GLU A 545 ? 1.8730 1.8507 2.0784 -0.4002 -0.4922 0.1434 545 GLU A CG 4201 C CD . GLU A 545 ? 1.7667 1.7463 1.9733 -0.4021 -0.4958 0.1671 545 GLU A CD 4202 O OE1 . GLU A 545 ? 1.7307 1.7013 1.9639 -0.4036 -0.5041 0.1760 545 GLU A OE1 4203 O OE2 . GLU A 545 ? 1.6294 1.6235 1.8143 -0.4034 -0.4925 0.1793 545 GLU A OE2 4204 N N . SER A 546 ? 1.8494 1.7756 2.1915 -0.4000 -0.5398 0.0875 546 SER A N 4205 C CA . SER A 546 ? 2.0738 1.9843 2.4827 -0.4025 -0.5703 0.0738 546 SER A CA 4206 C C . SER A 546 ? 2.0620 1.9817 2.4912 -0.3923 -0.5826 0.0189 546 SER A C 4207 O O . SER A 546 ? 2.0586 1.9781 2.5432 -0.3895 -0.6133 -0.0115 546 SER A O 4208 C CB . SER A 546 ? 2.0154 1.9264 2.4588 -0.4085 -0.5938 0.0841 546 SER A CB 4209 O OG . SER A 546 ? 1.9262 1.8381 2.3589 -0.4181 -0.5849 0.1324 546 SER A OG 4210 N N . GLU A 547 ? 1.9488 1.8815 2.3377 -0.3864 -0.5606 0.0038 547 GLU A N 4211 C CA . GLU A 547 ? 1.8889 1.8411 2.2961 -0.3762 -0.5696 -0.0503 547 GLU A CA 4212 C C . GLU A 547 ? 1.6221 1.5427 2.0688 -0.3762 -0.5770 -0.0492 547 GLU A C 4213 O O . GLU A 547 ? 1.4508 1.3824 1.9218 -0.3669 -0.5862 -0.0939 547 GLU A O 4214 C CB . GLU A 547 ? 1.9133 1.9107 2.2553 -0.3722 -0.5435 -0.0654 547 GLU A CB 4215 C CG . GLU A 547 ? 1.9514 2.0076 2.3008 -0.3633 -0.5552 -0.1257 547 GLU A CG 4216 C CD . GLU A 547 ? 1.9640 2.0223 2.3704 -0.3520 -0.5759 -0.1794 547 GLU A CD 4217 O OE1 . GLU A 547 ? 1.7693 1.8493 2.1545 -0.3480 -0.5615 -0.1965 547 GLU A OE1 4218 O OE2 . GLU A 547 ? 2.1033 2.1419 2.5817 -0.3474 -0.6094 -0.2045 547 GLU A OE2 4219 N N . PHE A 548 ? 1.4836 1.3729 1.9376 -0.3870 -0.5732 0.0014 548 PHE A N 4220 C CA . PHE A 548 ? 1.5555 1.4187 2.0486 -0.3912 -0.5813 0.0136 548 PHE A CA 4221 C C . PHE A 548 ? 1.7319 1.5738 2.2945 -0.4047 -0.6127 0.0473 548 PHE A C 4222 O O . PHE A 548 ? 2.0237 1.8489 2.6572 -0.4025 -0.6423 0.0326 548 PHE A O 4223 C CB . PHE A 548 ? 1.7639 1.6244 2.2030 -0.3944 -0.5473 0.0463 548 PHE A CB 4224 C CG . PHE A 548 ? 1.7113 1.5900 2.0811 -0.3930 -0.5183 0.0620 548 PHE A CG 4225 C CD1 . PHE A 548 ? 1.5098 1.4103 1.8312 -0.3852 -0.4998 0.0384 548 PHE A CD1 4226 C CD2 . PHE A 548 ? 1.8158 1.6954 2.1748 -0.4005 -0.5123 0.1018 548 PHE A CD2 4227 C CE1 . PHE A 548 ? 1.5530 1.4680 1.8226 -0.3861 -0.4796 0.0584 548 PHE A CE1 4228 C CE2 . PHE A 548 ? 1.5936 1.4870 1.9010 -0.3979 -0.4908 0.1138 548 PHE A CE2 4229 C CZ . PHE A 548 ? 1.5486 1.4557 1.8142 -0.3913 -0.4762 0.0942 548 PHE A CZ 4230 N N . ARG A 549 ? 1.5717 1.4204 2.1123 -0.4156 -0.6029 0.0937 549 ARG A N 4231 C CA . ARG A 549 ? 1.7612 1.6075 2.3499 -0.4341 -0.6228 0.1447 549 ARG A CA 4232 C C . ARG A 549 ? 1.5394 1.3924 2.1099 -0.4423 -0.6026 0.1801 549 ARG A C 4233 O O . ARG A 549 ? 1.6387 1.5101 2.2270 -0.4560 -0.6055 0.2283 549 ARG A O 4234 C CB . ARG A 549 ? 1.8176 1.6459 2.4825 -0.4242 -0.6540 0.1371 549 ARG A CB 4235 C CG . ARG A 549 ? 1.6815 1.5120 2.3888 -0.4331 -0.6655 0.1958 549 ARG A CG 4236 C CD . ARG A 549 ? 1.7276 1.5860 2.4183 -0.4488 -0.6623 0.2419 549 ARG A CD 4237 N NE . ARG A 549 ? 1.7814 1.6662 2.4842 -0.4635 -0.6606 0.3024 549 ARG A NE 4238 C CZ . ARG A 549 ? 1.9194 1.8435 2.6148 -0.4788 -0.6586 0.3485 549 ARG A CZ 4239 N NH1 . ARG A 549 ? 1.8724 1.8343 2.5784 -0.4929 -0.6574 0.4010 549 ARG A NH1 4240 N NH2 . ARG A 549 ? 2.0019 1.9348 2.6792 -0.4804 -0.6582 0.3419 549 ARG A NH2 4241 N N . ASP A 550 ? 1.3631 1.2108 1.8901 -0.4307 -0.5770 0.1564 550 ASP A N 4242 C CA . ASP A 550 ? 1.3183 1.1754 1.8229 -0.4365 -0.5554 0.1855 550 ASP A CA 4243 C C . ASP A 550 ? 1.3446 1.2207 1.7759 -0.4293 -0.5183 0.1915 550 ASP A C 4244 O O . ASP A 550 ? 1.3085 1.1783 1.6934 -0.4164 -0.4975 0.1647 550 ASP A O 4245 C CB . ASP A 550 ? 1.3990 1.2365 1.9133 -0.4300 -0.5546 0.1602 550 ASP A CB 4246 C CG . ASP A 550 ? 1.5831 1.4312 2.0728 -0.4351 -0.5315 0.1872 550 ASP A CG 4247 O OD1 . ASP A 550 ? 1.6920 1.5493 2.2265 -0.4514 -0.5471 0.2232 550 ASP A OD1 4248 O OD2 . ASP A 550 ? 1.7275 1.5790 2.1570 -0.4243 -0.5001 0.1742 550 ASP A OD2 4249 N N . LYS A 551 ? 1.4950 1.4004 1.9248 -0.4391 -0.5141 0.2281 551 LYS A N 4250 C CA . LYS A 551 ? 1.2793 1.2112 1.6613 -0.4340 -0.4852 0.2383 551 LYS A CA 4251 C C . LYS A 551 ? 1.3787 1.3349 1.7684 -0.4418 -0.4763 0.2609 551 LYS A C 4252 O O . LYS A 551 ? 1.5377 1.4772 1.9540 -0.4472 -0.4862 0.2614 551 LYS A O 4253 C CB . LYS A 551 ? 1.4155 1.3764 1.7963 -0.4377 -0.4881 0.2561 551 LYS A CB 4254 C CG . LYS A 551 ? 1.2337 1.1738 1.6050 -0.4304 -0.4963 0.2346 551 LYS A CG 4255 C CD . LYS A 551 ? 1.2978 1.2662 1.6691 -0.4341 -0.4992 0.2532 551 LYS A CD 4256 C CE . LYS A 551 ? 1.3820 1.3324 1.7421 -0.4275 -0.5069 0.2328 551 LYS A CE 4257 N NZ . LYS A 551 ? 1.3280 1.3044 1.6912 -0.4314 -0.5114 0.2514 551 LYS A NZ 4258 N N . LEU A 552 ? 1.3472 1.3466 1.7164 -0.4414 -0.4585 0.2751 552 LEU A N 4259 C CA . LEU A 552 ? 1.4364 1.4717 1.8121 -0.4487 -0.4492 0.2929 552 LEU A CA 4260 C C . LEU A 552 ? 1.5739 1.5724 1.9258 -0.4374 -0.4339 0.2686 552 LEU A C 4261 O O . LEU A 552 ? 1.8383 1.8386 2.1541 -0.4236 -0.4121 0.2511 552 LEU A O 4262 C CB . LEU A 552 ? 1.3807 1.4442 1.8114 -0.4731 -0.4744 0.3329 552 LEU A CB 4263 C CG . LEU A 552 ? 1.5729 1.6998 2.0251 -0.4884 -0.4855 0.3670 552 LEU A CG 4264 C CD1 . LEU A 552 ? 1.5008 1.6645 2.0145 -0.5179 -0.5149 0.4174 552 LEU A CD1 4265 C CD2 . LEU A 552 ? 1.5241 1.7172 1.9437 -0.4808 -0.4596 0.3627 552 LEU A CD2 4266 N N . THR A 553 ? 1.1840 1.1544 1.5631 -0.4442 -0.4476 0.2695 553 THR A N 4267 C CA . THR A 553 ? 1.2004 1.1469 1.5644 -0.4373 -0.4348 0.2528 553 THR A CA 4268 C C . THR A 553 ? 1.2541 1.1798 1.5660 -0.4184 -0.4110 0.2221 553 THR A C 4269 O O . THR A 553 ? 1.4102 1.3134 1.7051 -0.4101 -0.4128 0.2023 553 THR A O 4270 C CB . THR A 553 ? 1.2390 1.1439 1.6391 -0.4398 -0.4572 0.2396 553 THR A CB 4271 O OG1 . THR A 553 ? 1.5449 1.4626 2.0080 -0.4592 -0.4879 0.2716 553 THR A OG1 4272 C CG2 . THR A 553 ? 1.0691 0.9565 1.4600 -0.4350 -0.4460 0.2264 553 THR A CG2 4273 N N . PRO A 554 ? 1.2263 1.1645 1.5168 -0.4132 -0.3909 0.2205 554 PRO A N 4274 C CA . PRO A 554 ? 1.2502 1.1718 1.5010 -0.3977 -0.3736 0.1987 554 PRO A CA 4275 C C . PRO A 554 ? 1.2997 1.1819 1.5347 -0.3924 -0.3736 0.1768 554 PRO A C 4276 O O . PRO A 554 ? 1.2014 1.0690 1.4550 -0.3969 -0.3821 0.1716 554 PRO A O 4277 C CB . PRO A 554 ? 1.1414 1.0880 1.3851 -0.3941 -0.3569 0.2009 554 PRO A CB 4278 C CG . PRO A 554 ? 1.0797 1.0435 1.3500 -0.4077 -0.3626 0.2192 554 PRO A CG 4279 C CD . PRO A 554 ? 1.0749 1.0473 1.3794 -0.4218 -0.3853 0.2393 554 PRO A CD 4280 N N . ILE A 555 ? 1.2906 1.1632 1.4963 -0.3838 -0.3667 0.1647 555 ILE A N 4281 C CA . ILE A 555 ? 1.2395 1.0944 1.4250 -0.3802 -0.3643 0.1458 555 ILE A CA 4282 C C . ILE A 555 ? 1.1446 0.9944 1.3112 -0.3756 -0.3482 0.1456 555 ILE A C 4283 O O . ILE A 555 ? 1.2472 1.1009 1.4027 -0.3707 -0.3414 0.1521 555 ILE A O 4284 C CB . ILE A 555 ? 1.1676 1.0269 1.3341 -0.3781 -0.3686 0.1401 555 ILE A CB 4285 C CG1 . ILE A 555 ? 1.1806 1.0451 1.3679 -0.3820 -0.3855 0.1377 555 ILE A CG1 4286 C CG2 . ILE A 555 ? 1.1851 1.0470 1.3289 -0.3770 -0.3652 0.1231 555 ILE A CG2 4287 C CD1 . ILE A 555 ? 1.1896 1.0650 1.3594 -0.3811 -0.3903 0.1337 555 ILE A CD1 4288 N N . THR A 556 ? 1.1800 1.0204 1.3499 -0.3768 -0.3449 0.1372 556 THR A N 4289 C CA . THR A 556 ? 1.1952 1.0305 1.3501 -0.3733 -0.3301 0.1377 556 THR A CA 4290 C C . THR A 556 ? 1.2048 1.0364 1.3322 -0.3710 -0.3255 0.1274 556 THR A C 4291 O O . THR A 556 ? 1.2041 1.0386 1.3282 -0.3722 -0.3295 0.1100 556 THR A O 4292 C CB . THR A 556 ? 1.3157 1.1465 1.4888 -0.3771 -0.3286 0.1374 556 THR A CB 4293 O OG1 . THR A 556 ? 1.2264 1.0752 1.4269 -0.3837 -0.3342 0.1555 556 THR A OG1 4294 C CG2 . THR A 556 ? 1.2862 1.1120 1.4423 -0.3730 -0.3128 0.1363 556 THR A CG2 4295 N N . ILE A 557 ? 1.2140 1.0460 1.3276 -0.3683 -0.3200 0.1379 557 ILE A N 4296 C CA . ILE A 557 ? 1.1766 1.0137 1.2678 -0.3705 -0.3176 0.1387 557 ILE A CA 4297 C C . ILE A 557 ? 1.2064 1.0342 1.2922 -0.3691 -0.3064 0.1356 557 ILE A C 4298 O O . ILE A 557 ? 1.1891 1.0064 1.2847 -0.3647 -0.3008 0.1420 557 ILE A O 4299 C CB . ILE A 557 ? 1.2588 1.0990 1.3494 -0.3711 -0.3238 0.1579 557 ILE A CB 4300 C CG1 . ILE A 557 ? 1.2801 1.1316 1.3741 -0.3733 -0.3352 0.1618 557 ILE A CG1 4301 C CG2 . ILE A 557 ? 1.2883 1.1411 1.3612 -0.3782 -0.3243 0.1686 557 ILE A CG2 4302 C CD1 . ILE A 557 ? 1.2424 1.0875 1.3593 -0.3672 -0.3382 0.1631 557 ILE A CD1 4303 N N . PHE A 558 ? 1.1949 1.0325 1.2673 -0.3720 -0.3039 0.1217 558 PHE A N 4304 C CA . PHE A 558 ? 1.1755 1.0050 1.2436 -0.3708 -0.2936 0.1161 558 PHE A CA 4305 C C . PHE A 558 ? 1.2462 1.0944 1.2909 -0.3757 -0.2901 0.1222 558 PHE A C 4306 O O . PHE A 558 ? 1.2499 1.1321 1.2800 -0.3808 -0.2941 0.1135 558 PHE A O 4307 C CB . PHE A 558 ? 1.3374 1.1654 1.4193 -0.3695 -0.2958 0.0927 558 PHE A CB 4308 C CG . PHE A 558 ? 1.4854 1.3065 1.5646 -0.3683 -0.2864 0.0848 558 PHE A CG 4309 C CD1 . PHE A 558 ? 1.4563 1.2577 1.5474 -0.3671 -0.2792 0.0954 558 PHE A CD1 4310 C CD2 . PHE A 558 ? 1.3267 1.1702 1.3924 -0.3687 -0.2850 0.0651 558 PHE A CD2 4311 C CE1 . PHE A 558 ? 1.4010 1.1959 1.4901 -0.3665 -0.2709 0.0891 558 PHE A CE1 4312 C CE2 . PHE A 558 ? 1.2979 1.1359 1.3622 -0.3672 -0.2766 0.0570 558 PHE A CE2 4313 C CZ . PHE A 558 ? 1.4072 1.2162 1.4831 -0.3662 -0.2697 0.0702 558 PHE A CZ 4314 N N . MET A 559 ? 1.3432 1.1772 1.3875 -0.3752 -0.2843 0.1370 559 MET A N 4315 C CA . MET A 559 ? 1.2729 1.1253 1.3003 -0.3825 -0.2829 0.1491 559 MET A CA 4316 C C . MET A 559 ? 1.2405 1.0826 1.2635 -0.3798 -0.2708 0.1388 559 MET A C 4317 O O . MET A 559 ? 1.1683 0.9818 1.2053 -0.3732 -0.2649 0.1379 559 MET A O 4318 C CB . MET A 559 ? 1.3112 1.1555 1.3509 -0.3861 -0.2927 0.1795 559 MET A CB 4319 C CG . MET A 559 ? 1.5288 1.3767 1.5650 -0.3925 -0.2920 0.1964 559 MET A CG 4320 S SD . MET A 559 ? 1.5295 1.3776 1.5924 -0.4025 -0.3148 0.2389 559 MET A SD 4321 C CE . MET A 559 ? 1.3834 1.1886 1.4877 -0.3853 -0.3219 0.2280 559 MET A CE 4322 N N . GLU A 560 ? 1.3354 1.2093 1.3395 -0.3852 -0.2673 0.1292 560 GLU A N 4323 C CA . GLU A 560 ? 1.3350 1.2041 1.3330 -0.3841 -0.2567 0.1226 560 GLU A CA 4324 C C . GLU A 560 ? 1.3708 1.2813 1.3488 -0.3961 -0.2578 0.1405 560 GLU A C 4325 O O . GLU A 560 ? 1.3644 1.3241 1.3298 -0.4055 -0.2651 0.1461 560 GLU A O 4326 C CB . GLU A 560 ? 1.3736 1.2459 1.3769 -0.3777 -0.2526 0.0871 560 GLU A CB 4327 C CG . GLU A 560 ? 1.5672 1.4909 1.5630 -0.3794 -0.2589 0.0609 560 GLU A CG 4328 C CD . GLU A 560 ? 1.7020 1.6254 1.7185 -0.3705 -0.2609 0.0202 560 GLU A CD 4329 O OE1 . GLU A 560 ? 1.6703 1.5561 1.7019 -0.3664 -0.2560 0.0195 560 GLU A OE1 4330 O OE2 . GLU A 560 ? 1.7820 1.7461 1.8052 -0.3677 -0.2699 -0.0125 560 GLU A OE2 4331 N N . TYR A 561 ? 1.5070 1.4046 1.4836 -0.3977 -0.2517 0.1521 561 TYR A N 4332 C CA . TYR A 561 ? 1.5504 1.4898 1.5128 -0.4122 -0.2552 0.1774 561 TYR A CA 4333 C C . TYR A 561 ? 1.5805 1.5271 1.5315 -0.4115 -0.2429 0.1653 561 TYR A C 4334 O O . TYR A 561 ? 1.6412 1.5414 1.6023 -0.4012 -0.2340 0.1542 561 TYR A O 4335 C CB . TYR A 561 ? 1.4282 1.3450 1.4118 -0.4193 -0.2695 0.2192 561 TYR A CB 4336 C CG . TYR A 561 ? 1.3395 1.1949 1.3484 -0.4065 -0.2667 0.2158 561 TYR A CG 4337 C CD1 . TYR A 561 ? 1.3453 1.1875 1.3582 -0.4072 -0.2626 0.2229 561 TYR A CD1 4338 C CD2 . TYR A 561 ? 1.4069 1.2274 1.4368 -0.3939 -0.2686 0.2039 561 TYR A CD2 4339 C CE1 . TYR A 561 ? 1.4059 1.2029 1.4437 -0.3947 -0.2604 0.2149 561 TYR A CE1 4340 C CE2 . TYR A 561 ? 1.3570 1.1405 1.4109 -0.3821 -0.2659 0.1959 561 TYR A CE2 4341 C CZ . TYR A 561 ? 1.4828 1.2553 1.5410 -0.3821 -0.2619 0.1999 561 TYR A CZ 4342 O OH . TYR A 561 ? 1.5028 1.2486 1.5866 -0.3697 -0.2597 0.1872 561 TYR A OH 4343 N N . ARG A 562 ? 1.5890 1.6029 1.5189 -0.4233 -0.2425 0.1676 562 ARG A N 4344 C CA . ARG A 562 ? 1.6836 1.7150 1.6018 -0.4246 -0.2320 0.1592 562 ARG A CA 4345 C C . ARG A 562 ? 1.5881 1.6568 1.5005 -0.4447 -0.2401 0.2063 562 ARG A C 4346 O O . ARG A 562 ? 1.6615 1.7366 1.5851 -0.4573 -0.2564 0.2463 562 ARG A O 4347 C CB . ARG A 562 ? 1.7414 1.8333 1.6456 -0.4202 -0.2254 0.1138 562 ARG A CB 4348 C CG . ARG A 562 ? 1.8530 2.0438 1.7389 -0.4346 -0.2328 0.1176 562 ARG A CG 4349 C CD . ARG A 562 ? 1.9082 2.1790 1.7818 -0.4314 -0.2260 0.0720 562 ARG A CD 4350 N NE . ARG A 562 ? 2.0181 2.2553 1.9133 -0.4092 -0.2235 0.0132 562 ARG A NE 4351 C CZ . ARG A 562 ? 1.9923 2.2870 1.8930 -0.3998 -0.2221 -0.0409 562 ARG A CZ 4352 N NH1 . ARG A 562 ? 1.9670 2.3659 1.8455 -0.4105 -0.2190 -0.0462 562 ARG A NH1 4353 N NH2 . ARG A 562 ? 1.8667 2.1209 1.8010 -0.3804 -0.2267 -0.0897 562 ARG A NH2 4354 N N . LEU A 563 ? 1.4748 1.5690 1.3750 -0.4488 -0.2317 0.2043 563 LEU A N 4355 C CA . LEU A 563 ? 1.4892 1.6262 1.3869 -0.4709 -0.2415 0.2530 563 LEU A CA 4356 C C . LEU A 563 ? 1.5652 1.8072 1.4339 -0.4825 -0.2348 0.2413 563 LEU A C 4357 O O . LEU A 563 ? 1.5367 1.7841 1.3949 -0.4719 -0.2197 0.2044 563 LEU A O 4358 C CB . LEU A 563 ? 1.5981 1.6685 1.5140 -0.4669 -0.2402 0.2692 563 LEU A CB 4359 C CG . LEU A 563 ? 1.5062 1.5676 1.4500 -0.4849 -0.2626 0.3290 563 LEU A CG 4360 C CD1 . LEU A 563 ? 1.2917 1.2806 1.2586 -0.4741 -0.2602 0.3281 563 LEU A CD1 4361 C CD2 . LEU A 563 ? 1.5418 1.6994 1.4716 -0.5135 -0.2725 0.3701 563 LEU A CD2 4362 N N . ASP A 564 ? 1.7821 2.1156 1.6406 -0.5048 -0.2472 0.2721 564 ASP A N 4363 C CA . ASP A 564 ? 1.9449 2.4030 1.7766 -0.5196 -0.2427 0.2656 564 ASP A CA 4364 C C . ASP A 564 ? 2.0887 2.5560 1.9211 -0.5347 -0.2439 0.3047 564 ASP A C 4365 O O . ASP A 564 ? 2.1210 2.5570 1.9761 -0.5517 -0.2621 0.3666 564 ASP A O 4366 C CB . ASP A 564 ? 1.9432 2.5097 1.7654 -0.5436 -0.2574 0.2962 564 ASP A CB 4367 C CG . ASP A 564 ? 2.0605 2.6116 1.8852 -0.5295 -0.2584 0.2621 564 ASP A CG 4368 O OD1 . ASP A 564 ? 2.0482 2.5495 1.8752 -0.5021 -0.2455 0.1993 564 ASP A OD1 4369 O OD2 . ASP A 564 ? 2.1610 2.7505 1.9895 -0.5473 -0.2745 0.3012 564 ASP A OD2 4370 N N . TYR A 565 ? 2.1739 2.6822 1.9881 -0.5280 -0.2276 0.2676 565 TYR A N 4371 C CA . TYR A 565 ? 2.1937 2.6891 2.0096 -0.5365 -0.2255 0.2955 565 TYR A CA 4372 C C . TYR A 565 ? 2.1993 2.7643 2.0213 -0.5734 -0.2469 0.3761 565 TYR A C 4373 O O . TYR A 565 ? 2.1322 2.6228 1.9861 -0.5815 -0.2645 0.4270 565 TYR A O 4374 C CB . TYR A 565 ? 2.1921 2.7434 1.9868 -0.5253 -0.2059 0.2406 565 TYR A CB 4375 C CG . TYR A 565 ? 2.1846 2.8876 1.9557 -0.5332 -0.2031 0.2093 565 TYR A CG 4376 C CD1 . TYR A 565 ? 2.1639 2.8924 1.9348 -0.5168 -0.2011 0.1536 565 TYR A CD1 4377 C CD2 . TYR A 565 ? 2.0188 2.8478 1.7710 -0.5565 -0.2033 0.2319 565 TYR A CD2 4378 C CE1 . TYR A 565 ? 2.1377 3.0146 1.8921 -0.5215 -0.1999 0.1160 565 TYR A CE1 4379 C CE2 . TYR A 565 ? 2.0256 3.0117 1.7575 -0.5630 -0.2005 0.1974 565 TYR A CE2 4380 C CZ . TYR A 565 ? 2.1144 3.1246 1.8483 -0.5442 -0.1988 0.1361 565 TYR A CZ 4381 O OH . TYR A 565 ? 2.1352 3.3114 1.8537 -0.5484 -0.1973 0.0930 565 TYR A OH 4382 N N . ARG A 566 ? 2.2386 2.9509 2.0368 -0.5961 -0.2487 0.3873 566 ARG A N 4383 C CA . ARG A 566 ? 2.2095 3.0117 2.0164 -0.6373 -0.2738 0.4720 566 ARG A CA 4384 C C . ARG A 566 ? 2.2094 2.9418 2.0492 -0.6513 -0.2906 0.5346 566 ARG A C 4385 O O . ARG A 566 ? 2.2651 3.0081 2.0962 -0.6520 -0.2808 0.5307 566 ARG A O 4386 C CB . ARG A 566 ? 2.1149 2.9300 1.9362 -0.6502 -0.2939 0.5054 566 ARG A CB 4387 C CG . ARG A 566 ? 2.0784 3.0772 1.8753 -0.6812 -0.3008 0.5283 566 ARG A CG 4388 C CD . ARG A 566 ? 2.2024 3.2291 2.0178 -0.7034 -0.3264 0.5821 566 ARG A CD 4389 N NE . ARG A 566 ? 2.2118 3.4331 2.0049 -0.7394 -0.3347 0.6150 566 ARG A NE 4390 C CZ . ARG A 566 ? 2.1201 3.4138 1.9217 -0.7654 -0.3562 0.6632 566 ARG A CZ 4391 N NH1 . ARG A 566 ? 2.0605 3.2409 1.8942 -0.7578 -0.3720 0.6822 566 ARG A NH1 4392 N NH2 . ARG A 566 ? 2.0479 3.5300 1.8328 -0.7973 -0.3578 0.6884 566 ARG A NH2 4393 N N . THR A 567 ? 2.2004 2.8633 2.0833 -0.6617 -0.3184 0.5896 567 THR A N 4394 C CA . THR A 567 ? 2.1701 2.7660 2.1015 -0.6758 -0.3443 0.6515 567 THR A CA 4395 C C . THR A 567 ? 1.9399 2.4396 1.8729 -0.6501 -0.3259 0.6128 567 THR A C 4396 O O . THR A 567 ? 1.7459 2.1649 1.6651 -0.6149 -0.3014 0.5448 567 THR A O 4397 C CB . THR A 567 ? 2.1592 2.6616 2.1463 -0.6745 -0.3741 0.6847 567 THR A CB 4398 O OG1 . THR A 567 ? 2.2036 2.5863 2.1909 -0.6336 -0.3547 0.6172 567 THR A OG1 4399 C CG2 . THR A 567 ? 1.9683 2.5561 1.9546 -0.6977 -0.3917 0.7201 567 THR A CG2 4400 N N . ALA A 568 ? 1.8503 2.3645 1.8040 -0.6708 -0.3408 0.6625 568 ALA A N 4401 C CA . ALA A 568 ? 1.7305 2.1761 1.6849 -0.6532 -0.3257 0.6359 568 ALA A CA 4402 C C . ALA A 568 ? 1.8164 2.2961 1.8057 -0.6867 -0.3547 0.7132 568 ALA A C 4403 O O . ALA A 568 ? 1.9068 2.4726 1.9177 -0.7151 -0.3848 0.7740 568 ALA A O 4404 C CB . ALA A 568 ? 1.5799 2.0734 1.4762 -0.6351 -0.2864 0.5670 568 ALA A CB 4405 N N . ALA A 569 ? 1.7018 2.1174 1.7027 -0.6755 -0.3486 0.7026 569 ALA A N 4406 C CA . ALA A 569 ? 1.8263 2.2564 1.8738 -0.6819 -0.3807 0.7491 569 ALA A CA 4407 C C . ALA A 569 ? 1.9173 2.4881 1.9307 -0.7084 -0.3751 0.7733 569 ALA A C 4408 O O . ALA A 569 ? 1.9066 2.5685 1.8569 -0.7205 -0.3440 0.7501 569 ALA A O 4409 C CB . ALA A 569 ? 1.7285 2.0398 1.8045 -0.6526 -0.3772 0.7195 569 ALA A CB 4410 N N . ASP A 570 ? 1.9396 2.5344 1.9996 -0.7163 -0.4067 0.8163 570 ASP A N 4411 C CA . ASP A 570 ? 2.0451 2.7707 2.0851 -0.7401 -0.4049 0.8386 570 ASP A CA 4412 C C . ASP A 570 ? 2.2440 2.9436 2.2354 -0.7255 -0.3648 0.7903 570 ASP A C 4413 O O . ASP A 570 ? 2.3302 3.1318 2.2981 -0.7400 -0.3559 0.7949 570 ASP A O 4414 C CB . ASP A 570 ? 2.1296 2.8826 2.2446 -0.7552 -0.4555 0.9023 570 ASP A CB 4415 C CG . ASP A 570 ? 2.1873 2.8063 2.3495 -0.7286 -0.4693 0.8946 570 ASP A CG 4416 O OD1 . ASP A 570 ? 2.1832 2.6755 2.3461 -0.6981 -0.4545 0.8513 570 ASP A OD1 4417 O OD2 . ASP A 570 ? 2.1377 2.7859 2.3398 -0.7386 -0.4955 0.9300 570 ASP A OD2 4418 N N . THR A 571 ? 2.2738 2.8413 2.2559 -0.6974 -0.3421 0.7426 571 THR A N 4419 C CA . THR A 571 ? 2.1980 2.7214 2.1426 -0.6821 -0.3053 0.6939 571 THR A CA 4420 C C . THR A 571 ? 2.2419 2.8706 2.1154 -0.6888 -0.2670 0.6524 571 THR A C 4421 O O . THR A 571 ? 2.2952 2.9007 2.1423 -0.6659 -0.2386 0.5963 571 THR A O 4422 C CB . THR A 571 ? 2.0599 2.4323 2.0176 -0.6524 -0.2919 0.6487 571 THR A CB 4423 O OG1 . THR A 571 ? 1.9412 2.2985 1.8925 -0.6437 -0.2889 0.6264 571 THR A OG1 4424 C CG2 . THR A 571 ? 1.9024 2.1780 1.9302 -0.6322 -0.3244 0.6653 571 THR A CG2 4425 N N . THR A 572 ? 2.1915 2.9344 2.0439 -0.7055 -0.2701 0.6616 572 THR A N 4426 C CA . THR A 572 ? 2.1070 2.9713 1.9059 -0.6986 -0.2418 0.6035 572 THR A CA 4427 C C . THR A 572 ? 2.0211 2.8026 1.8002 -0.6523 -0.2106 0.5049 572 THR A C 4428 O O . THR A 572 ? 2.0355 2.8022 1.7976 -0.6322 -0.1878 0.4533 572 THR A O 4429 C CB . THR A 572 ? 2.0760 3.0512 1.8523 -0.7164 -0.2332 0.6141 572 THR A CB 4430 O OG1 . THR A 572 ? 2.1905 3.2095 2.0132 -0.7453 -0.2700 0.6943 572 THR A OG1 4431 C CG2 . THR A 572 ? 1.9851 3.1277 1.7164 -0.7175 -0.2139 0.5649 572 THR A CG2 4432 N N . GLY A 573 ? 1.8107 2.5378 1.5973 -0.6372 -0.2128 0.4832 573 GLY A N 4433 C CA . GLY A 573 ? 1.7288 2.3927 1.5025 -0.5984 -0.1889 0.3975 573 GLY A CA 4434 C C . GLY A 573 ? 1.7814 2.2804 1.5813 -0.5723 -0.1870 0.3812 573 GLY A C 4435 O O . GLY A 573 ? 1.9295 2.3716 1.7233 -0.5423 -0.1682 0.3166 573 GLY A O 4436 N N . LEU A 574 ? 1.6341 2.0625 1.4690 -0.5838 -0.2090 0.4384 574 LEU A N 4437 C CA . LEU A 574 ? 1.6725 1.9631 1.5347 -0.5588 -0.2086 0.4187 574 LEU A CA 4438 C C . LEU A 574 ? 1.5418 1.8071 1.4240 -0.5593 -0.2254 0.4330 574 LEU A C 4439 O O . LEU A 574 ? 1.3809 1.6470 1.2965 -0.5804 -0.2545 0.4930 574 LEU A O 4440 C CB . LEU A 574 ? 1.4649 1.6856 1.3623 -0.5637 -0.2225 0.4563 574 LEU A CB 4441 C CG . LEU A 574 ? 1.3674 1.4628 1.2898 -0.5355 -0.2167 0.4243 574 LEU A CG 4442 C CD1 . LEU A 574 ? 1.2376 1.3113 1.1308 -0.5123 -0.1850 0.3645 574 LEU A CD1 4443 C CD2 . LEU A 574 ? 1.5257 1.5679 1.4970 -0.5442 -0.2414 0.4682 574 LEU A CD2 4444 N N . GLN A 575 ? 1.4801 1.7223 1.3474 -0.5365 -0.2098 0.3787 575 GLN A N 4445 C CA . GLN A 575 ? 1.4558 1.6645 1.3400 -0.5322 -0.2219 0.3826 575 GLN A CA 4446 C C . GLN A 575 ? 1.3830 1.4709 1.2967 -0.5085 -0.2213 0.3635 575 GLN A C 4447 O O . GLN A 575 ? 1.3954 1.4334 1.3050 -0.4902 -0.2037 0.3286 575 GLN A O 4448 C CB . GLN A 575 ? 1.6147 1.8797 1.4696 -0.5233 -0.2086 0.3366 575 GLN A CB 4449 C CG . GLN A 575 ? 1.8493 2.0993 1.6858 -0.4982 -0.1833 0.2677 575 GLN A CG 4450 C CD . GLN A 575 ? 1.9304 2.2556 1.7475 -0.4919 -0.1765 0.2215 575 GLN A CD 4451 O OE1 . GLN A 575 ? 1.7880 2.2208 1.5900 -0.5108 -0.1836 0.2376 575 GLN A OE1 4452 N NE2 . GLN A 575 ? 1.8701 2.1453 1.6929 -0.4663 -0.1653 0.1643 575 GLN A NE2 4453 N N . PRO A 576 ? 1.3281 1.3770 1.2737 -0.5094 -0.2414 0.3858 576 PRO A N 4454 C CA . PRO A 576 ? 1.2227 1.1749 1.1980 -0.4863 -0.2415 0.3626 576 PRO A CA 4455 C C . PRO A 576 ? 1.3632 1.2898 1.3160 -0.4625 -0.2172 0.3047 576 PRO A C 4456 O O . PRO A 576 ? 1.3555 1.3320 1.2778 -0.4627 -0.2059 0.2821 576 PRO A O 4457 C CB . PRO A 576 ? 1.2196 1.1587 1.2346 -0.4949 -0.2712 0.3984 576 PRO A CB 4458 C CG . PRO A 576 ? 1.4416 1.4574 1.4594 -0.5274 -0.2925 0.4573 576 PRO A CG 4459 C CD . PRO A 576 ? 1.4715 1.5709 1.4336 -0.5339 -0.2685 0.4380 576 PRO A CD 4460 N N . ILE A 577 ? 1.5261 1.3824 1.4992 -0.4431 -0.2121 0.2812 577 ILE A N 4461 C CA . ILE A 577 ? 1.2786 1.1099 1.2410 -0.4241 -0.1949 0.2368 577 ILE A CA 4462 C C . ILE A 577 ? 1.2726 1.0608 1.2658 -0.4137 -0.2058 0.2347 577 ILE A C 4463 O O . ILE A 577 ? 1.4954 1.2525 1.5241 -0.4116 -0.2203 0.2491 577 ILE A O 4464 C CB . ILE A 577 ? 1.2667 1.0716 1.2217 -0.4119 -0.1752 0.2079 577 ILE A CB 4465 C CG1 . ILE A 577 ? 1.2432 1.0251 1.1977 -0.3965 -0.1634 0.1719 577 ILE A CG1 4466 C CG2 . ILE A 577 ? 1.5951 1.3597 1.5776 -0.4086 -0.1807 0.2201 577 ILE A CG2 4467 C CD1 . ILE A 577 ? 1.6847 1.5024 1.6218 -0.3970 -0.1611 0.1525 577 ILE A CD1 4468 N N . LEU A 578 ? 1.3523 1.1431 1.3373 -0.4067 -0.2013 0.2144 578 LEU A N 4469 C CA . LEU A 578 ? 1.2968 1.0557 1.3088 -0.3963 -0.2098 0.2087 578 LEU A CA 4470 C C . LEU A 578 ? 1.2293 0.9528 1.2582 -0.3811 -0.2001 0.1860 578 LEU A C 4471 O O . LEU A 578 ? 1.3620 1.0836 1.3756 -0.3781 -0.1838 0.1706 578 LEU A O 4472 C CB . LEU A 578 ? 1.3527 1.1260 1.3509 -0.3934 -0.2066 0.1927 578 LEU A CB 4473 C CG . LEU A 578 ? 1.4356 1.2522 1.4209 -0.4072 -0.2179 0.2117 578 LEU A CG 4474 C CD1 . LEU A 578 ? 1.5939 1.4633 1.5465 -0.4158 -0.2081 0.2037 578 LEU A CD1 4475 C CD2 . LEU A 578 ? 1.4779 1.2913 1.4668 -0.4011 -0.2213 0.1992 578 LEU A CD2 4476 N N . ASN A 579 ? 1.1849 0.8884 1.2483 -0.3719 -0.2115 0.1825 579 ASN A N 4477 C CA . ASN A 579 ? 1.2990 0.9875 1.3823 -0.3578 -0.2041 0.1586 579 ASN A CA 4478 C C . ASN A 579 ? 1.3988 1.0958 1.4596 -0.3538 -0.1837 0.1378 579 ASN A C 4479 O O . ASN A 579 ? 1.1882 0.8947 1.2344 -0.3565 -0.1815 0.1354 579 ASN A O 4480 C CB . ASN A 579 ? 1.3959 1.0782 1.5221 -0.3469 -0.2211 0.1502 579 ASN A CB 4481 C CG . ASN A 579 ? 1.4924 1.1774 1.6446 -0.3321 -0.2160 0.1216 579 ASN A CG 4482 O OD1 . ASN A 579 ? 1.3243 0.9993 1.5083 -0.3269 -0.2267 0.1176 579 ASN A OD1 4483 N ND2 . ASN A 579 ? 1.6466 1.3526 1.7894 -0.3264 -0.2017 0.1023 579 ASN A ND2 4484 N N . GLN A 580 ? 1.4989 1.1943 1.5624 -0.3489 -0.1717 0.1251 580 GLN A N 4485 C CA . GLN A 580 ? 1.3518 1.0570 1.4023 -0.3490 -0.1565 0.1134 580 GLN A CA 4486 C C . GLN A 580 ? 1.4303 1.1500 1.4900 -0.3467 -0.1588 0.1073 580 GLN A C 4487 O O . GLN A 580 ? 1.3856 1.1070 1.4342 -0.3517 -0.1592 0.1089 580 GLN A O 4488 C CB . GLN A 580 ? 1.4366 1.1461 1.4964 -0.3448 -0.1466 0.1041 580 GLN A CB 4489 C CG . GLN A 580 ? 1.3984 1.1205 1.4516 -0.3489 -0.1346 0.1003 580 GLN A CG 4490 C CD . GLN A 580 ? 1.5691 1.3077 1.6336 -0.3461 -0.1257 0.0934 580 GLN A CD 4491 O OE1 . GLN A 580 ? 1.5838 1.3311 1.6658 -0.3378 -0.1288 0.0832 580 GLN A OE1 4492 N NE2 . GLN A 580 ? 1.6890 1.4353 1.7495 -0.3530 -0.1174 0.0973 580 GLN A NE2 4493 N N . PHE A 581 ? 1.6013 1.3373 1.6854 -0.3387 -0.1619 0.0977 581 PHE A N 4494 C CA . PHE A 581 ? 1.6026 1.3625 1.6969 -0.3377 -0.1645 0.0939 581 PHE A CA 4495 C C . PHE A 581 ? 1.8297 1.5856 1.9382 -0.3321 -0.1792 0.0931 581 PHE A C 4496 O O . PHE A 581 ? 1.8071 1.5686 1.9435 -0.3222 -0.1882 0.0816 581 PHE A O 4497 C CB . PHE A 581 ? 1.6529 1.4547 1.7658 -0.3339 -0.1579 0.0821 581 PHE A CB 4498 C CG . PHE A 581 ? 1.7534 1.5646 1.8572 -0.3423 -0.1458 0.0886 581 PHE A CG 4499 C CD1 . PHE A 581 ? 1.7627 1.5676 1.8586 -0.3535 -0.1455 0.1028 581 PHE A CD1 4500 C CD2 . PHE A 581 ? 1.6621 1.4892 1.7724 -0.3387 -0.1381 0.0793 581 PHE A CD2 4501 C CE1 . PHE A 581 ? 1.7234 1.5350 1.8208 -0.3619 -0.1392 0.1108 581 PHE A CE1 4502 C CE2 . PHE A 581 ? 1.5935 1.4307 1.6977 -0.3477 -0.1283 0.0883 581 PHE A CE2 4503 C CZ . PHE A 581 ? 1.4937 1.3219 1.5928 -0.3598 -0.1297 0.1057 581 PHE A CZ 4504 N N . THR A 582 ? 1.9387 1.6868 2.0335 -0.3380 -0.1839 0.1030 582 THR A N 4505 C CA . THR A 582 ? 1.8420 1.5869 1.9479 -0.3354 -0.1984 0.1066 582 THR A CA 4506 C C . THR A 582 ? 1.6631 1.4059 1.7485 -0.3435 -0.1996 0.1152 582 THR A C 4507 O O . THR A 582 ? 1.5438 1.2799 1.6075 -0.3505 -0.1945 0.1187 582 THR A O 4508 C CB . THR A 582 ? 1.7592 1.4836 1.8766 -0.3351 -0.2122 0.1171 582 THR A CB 4509 O OG1 . THR A 582 ? 1.8793 1.6017 2.0105 -0.3350 -0.2289 0.1254 582 THR A OG1 4510 C CG2 . THR A 582 ? 1.6052 1.3185 1.6938 -0.3463 -0.2076 0.1332 582 THR A CG2 4511 N N . PRO A 583 ? 1.6012 1.3544 1.6971 -0.3414 -0.2075 0.1144 583 PRO A N 4512 C CA . PRO A 583 ? 1.5647 1.3186 1.6468 -0.3479 -0.2107 0.1190 583 PRO A CA 4513 C C . PRO A 583 ? 1.4278 1.1739 1.4921 -0.3539 -0.2175 0.1290 583 PRO A C 4514 O O . PRO A 583 ? 1.3714 1.1130 1.4441 -0.3539 -0.2276 0.1404 583 PRO A O 4515 C CB . PRO A 583 ? 1.7311 1.5006 1.8322 -0.3434 -0.2185 0.1168 583 PRO A CB 4516 C CG . PRO A 583 ? 1.5620 1.3520 1.6861 -0.3348 -0.2152 0.1054 583 PRO A CG 4517 C CD . PRO A 583 ? 1.4878 1.2599 1.6131 -0.3316 -0.2139 0.1038 583 PRO A CD 4518 N N . ALA A 584 ? 1.4395 1.1912 1.4855 -0.3597 -0.2148 0.1245 584 ALA A N 4519 C CA . ALA A 584 ? 1.5794 1.3454 1.6068 -0.3668 -0.2205 0.1308 584 ALA A CA 4520 C C . ALA A 584 ? 1.5475 1.3245 1.5766 -0.3682 -0.2307 0.1316 584 ALA A C 4521 O O . ALA A 584 ? 1.3748 1.1750 1.3898 -0.3752 -0.2370 0.1376 584 ALA A O 4522 C CB . ALA A 584 ? 1.7771 1.5567 1.7880 -0.3698 -0.2134 0.1160 584 ALA A CB 4523 N N . ASN A 585 ? 1.5132 1.2817 1.5597 -0.3628 -0.2325 0.1268 585 ASN A N 4524 C CA . ASN A 585 ? 1.3391 1.1159 1.3894 -0.3637 -0.2422 0.1275 585 ASN A CA 4525 C C . ASN A 585 ? 1.3339 1.1066 1.4063 -0.3578 -0.2461 0.1311 585 ASN A C 4526 O O . ASN A 585 ? 1.4947 1.2678 1.5808 -0.3536 -0.2398 0.1268 585 ASN A O 4527 C CB . ASN A 585 ? 1.4293 1.2135 1.4797 -0.3652 -0.2438 0.1103 585 ASN A CB 4528 C CG . ASN A 585 ? 1.6796 1.4535 1.7515 -0.3635 -0.2412 0.1052 585 ASN A CG 4529 O OD1 . ASN A 585 ? 1.6386 1.4146 1.7276 -0.3631 -0.2450 0.1122 585 ASN A OD1 4530 N ND2 . ASN A 585 ? 2.0720 1.8412 2.1456 -0.3641 -0.2363 0.0955 585 ASN A ND2 4531 N N . ILE A 586 ? 1.1952 0.9729 1.2720 -0.3582 -0.2569 0.1382 586 ILE A N 4532 C CA . ILE A 586 ? 1.1462 0.9279 1.2462 -0.3516 -0.2625 0.1381 586 ILE A CA 4533 C C . ILE A 586 ? 1.2169 1.0072 1.3164 -0.3544 -0.2703 0.1392 586 ILE A C 4534 O O . ILE A 586 ? 1.2461 1.0394 1.3305 -0.3603 -0.2759 0.1432 586 ILE A O 4535 C CB . ILE A 586 ? 1.2295 1.0049 1.3490 -0.3466 -0.2731 0.1456 586 ILE A CB 4536 C CG1 . ILE A 586 ? 1.3126 1.0996 1.4618 -0.3372 -0.2812 0.1377 586 ILE A CG1 4537 C CG2 . ILE A 586 ? 1.1480 0.9217 1.2573 -0.3559 -0.2847 0.1651 586 ILE A CG2 4538 C CD1 . ILE A 586 ? 1.1906 0.9690 1.3731 -0.3309 -0.2995 0.1418 586 ILE A CD1 4539 N N . SER A 587 ? 1.3529 1.1556 1.4696 -0.3512 -0.2710 0.1356 587 SER A N 4540 C CA . SER A 587 ? 1.3842 1.1951 1.5039 -0.3544 -0.2793 0.1377 587 SER A CA 4541 C C . SER A 587 ? 1.2700 1.0958 1.4092 -0.3483 -0.2864 0.1391 587 SER A C 4542 O O . SER A 587 ? 1.2340 1.0773 1.3916 -0.3411 -0.2833 0.1324 587 SER A O 4543 C CB . SER A 587 ? 1.4243 1.2427 1.5527 -0.3602 -0.2783 0.1361 587 SER A CB 4544 O OG . SER A 587 ? 1.4587 1.2635 1.5777 -0.3639 -0.2757 0.1291 587 SER A OG 4545 N N . ARG A 588 ? 1.2803 1.1053 1.4174 -0.3504 -0.2965 0.1443 588 ARG A N 4546 C CA . ARG A 588 ? 1.2192 1.0601 1.3763 -0.3450 -0.3048 0.1444 588 ARG A CA 4547 C C . ARG A 588 ? 1.2117 1.0614 1.3664 -0.3515 -0.3098 0.1484 588 ARG A C 4548 O O . ARG A 588 ? 1.1931 1.0322 1.3337 -0.3587 -0.3109 0.1487 588 ARG A O 4549 C CB . ARG A 588 ? 1.2695 1.0988 1.4354 -0.3414 -0.3172 0.1506 588 ARG A CB 4550 C CG . ARG A 588 ? 1.3881 1.2090 1.5739 -0.3336 -0.3198 0.1465 588 ARG A CG 4551 C CD . ARG A 588 ? 1.4297 1.2763 1.6485 -0.3200 -0.3196 0.1257 588 ARG A CD 4552 N NE . ARG A 588 ? 1.4683 1.3235 1.6873 -0.3165 -0.3070 0.1139 588 ARG A NE 4553 C CZ . ARG A 588 ? 1.5561 1.3972 1.7916 -0.3102 -0.3107 0.1079 588 ARG A CZ 4554 N NH1 . ARG A 588 ? 1.5665 1.3835 1.8247 -0.3084 -0.3296 0.1165 588 ARG A NH1 4555 N NH2 . ARG A 588 ? 1.5825 1.4351 1.8162 -0.3074 -0.2981 0.0962 588 ARG A NH2 4556 N N . GLN A 589 ? 1.2153 1.0887 1.3883 -0.3484 -0.3148 0.1485 589 GLN A N 4557 C CA . GLN A 589 ? 1.1752 1.0588 1.3510 -0.3557 -0.3216 0.1552 589 GLN A CA 4558 C C . GLN A 589 ? 1.2418 1.1348 1.4264 -0.3518 -0.3317 0.1571 589 GLN A C 4559 O O . GLN A 589 ? 1.2191 1.1362 1.4232 -0.3432 -0.3330 0.1508 589 GLN A O 4560 C CB . GLN A 589 ? 1.1105 1.0266 1.3031 -0.3617 -0.3188 0.1610 589 GLN A CB 4561 C CG . GLN A 589 ? 1.2034 1.1082 1.3934 -0.3686 -0.3135 0.1635 589 GLN A CG 4562 C CD . GLN A 589 ? 1.3628 1.3054 1.5763 -0.3797 -0.3160 0.1791 589 GLN A CD 4563 O OE1 . GLN A 589 ? 1.3895 1.3741 1.6185 -0.3831 -0.3206 0.1885 589 GLN A OE1 4564 N NE2 . GLN A 589 ? 1.3486 1.2828 1.5681 -0.3871 -0.3149 0.1848 589 GLN A NE2 4565 N N . ALA A 590 ? 1.3765 1.2554 1.5499 -0.3574 -0.3399 0.1620 590 ALA A N 4566 C CA . ALA A 590 ? 1.1643 1.0523 1.3457 -0.3560 -0.3503 0.1663 590 ALA A CA 4567 C C . ALA A 590 ? 1.1462 1.0537 1.3390 -0.3627 -0.3550 0.1714 590 ALA A C 4568 O O . ALA A 590 ? 1.1396 1.0410 1.3330 -0.3708 -0.3564 0.1733 590 ALA A O 4569 C CB . ALA A 590 ? 1.1719 1.0431 1.3359 -0.3599 -0.3579 0.1710 590 ALA A CB 4570 N N . HIS A 591 ? 1.2405 1.1737 1.4489 -0.3596 -0.3603 0.1741 591 HIS A N 4571 C CA . HIS A 591 ? 1.2054 1.1640 1.4282 -0.3682 -0.3672 0.1846 591 HIS A CA 4572 C C . HIS A 591 ? 1.2264 1.1805 1.4488 -0.3686 -0.3786 0.1878 591 HIS A C 4573 O O . HIS A 591 ? 1.2437 1.1968 1.4662 -0.3600 -0.3809 0.1832 591 HIS A O 4574 C CB . HIS A 591 ? 1.1260 1.1402 1.3695 -0.3670 -0.3629 0.1866 591 HIS A CB 4575 C CG . HIS A 591 ? 1.1949 1.2250 1.4407 -0.3691 -0.3524 0.1860 591 HIS A CG 4576 N ND1 . HIS A 591 ? 1.4020 1.4197 1.6408 -0.3579 -0.3426 0.1698 591 HIS A ND1 4577 C CD2 . HIS A 591 ? 1.2923 1.3518 1.5507 -0.3826 -0.3525 0.2027 591 HIS A CD2 4578 C CE1 . HIS A 591 ? 1.4367 1.4756 1.6788 -0.3630 -0.3344 0.1730 591 HIS A CE1 4579 N NE2 . HIS A 591 ? 1.5169 1.5827 1.7712 -0.3787 -0.3405 0.1946 591 HIS A NE2 4580 N N . ILE A 592 ? 1.2455 1.1962 1.4735 -0.3787 -0.3887 0.1957 592 ILE A N 4581 C CA . ILE A 592 ? 1.2343 1.1861 1.4644 -0.3802 -0.4001 0.1992 592 ILE A CA 4582 C C . ILE A 592 ? 1.2001 1.1955 1.4497 -0.3798 -0.4022 0.2083 592 ILE A C 4583 O O . ILE A 592 ? 1.1988 1.2308 1.4651 -0.3859 -0.4001 0.2180 592 ILE A O 4584 C CB . ILE A 592 ? 1.2932 1.2301 1.5319 -0.3899 -0.4139 0.2002 592 ILE A CB 4585 C CG1 . ILE A 592 ? 1.2673 1.1761 1.4906 -0.3885 -0.4120 0.1831 592 ILE A CG1 4586 C CG2 . ILE A 592 ? 1.4666 1.4060 1.7066 -0.3910 -0.4256 0.2020 592 ILE A CG2 4587 C CD1 . ILE A 592 ? 1.1719 1.0704 1.4121 -0.3939 -0.4290 0.1717 592 ILE A CD1 4588 N N . LEU A 593 ? 1.1587 1.1586 1.4082 -0.3738 -0.4072 0.2061 593 LEU A N 4589 C CA . LEU A 593 ? 1.1708 1.2195 1.4401 -0.3709 -0.4093 0.2088 593 LEU A CA 4590 C C . LEU A 593 ? 1.2031 1.2764 1.4869 -0.3856 -0.4198 0.2284 593 LEU A C 4591 O O . LEU A 593 ? 1.2843 1.3319 1.5656 -0.3911 -0.4310 0.2336 593 LEU A O 4592 C CB . LEU A 593 ? 1.2091 1.2512 1.4806 -0.3596 -0.4150 0.1998 593 LEU A CB 4593 C CG . LEU A 593 ? 1.2765 1.3699 1.5729 -0.3513 -0.4187 0.1927 593 LEU A CG 4594 C CD1 . LEU A 593 ? 1.2021 1.2787 1.5113 -0.3358 -0.4255 0.1776 593 LEU A CD1 4595 C CD2 . LEU A 593 ? 1.5750 1.6881 1.8759 -0.3612 -0.4281 0.2082 593 LEU A CD2 4596 N N . LEU A 594 ? 1.2283 1.3582 1.5310 -0.3932 -0.4180 0.2405 594 LEU A N 4597 C CA . LEU A 594 ? 1.2023 1.3665 1.5273 -0.4112 -0.4317 0.2679 594 LEU A CA 4598 C C . LEU A 594 ? 1.1935 1.4497 1.5365 -0.4147 -0.4283 0.2766 594 LEU A C 4599 O O . LEU A 594 ? 1.2528 1.5537 1.5983 -0.4124 -0.4169 0.2707 594 LEU A O 4600 C CB . LEU A 594 ? 1.2110 1.3545 1.5502 -0.4272 -0.4407 0.2865 594 LEU A CB 4601 C CG . LEU A 594 ? 1.2134 1.3450 1.5822 -0.4447 -0.4653 0.3103 594 LEU A CG 4602 C CD1 . LEU A 594 ? 1.3850 1.4972 1.7796 -0.4579 -0.4769 0.3244 594 LEU A CD1 4603 C CD2 . LEU A 594 ? 1.1974 1.3973 1.5908 -0.4586 -0.4757 0.3394 594 LEU A CD2 4604 N N . ASP A 595 ? 1.2341 1.5267 1.5902 -0.4207 -0.4385 0.2893 595 ASP A N 4605 C CA . ASP A 595 ? 1.2701 1.6676 1.6454 -0.4269 -0.4374 0.2994 595 ASP A CA 4606 C C . ASP A 595 ? 1.2064 1.6553 1.5795 -0.4060 -0.4211 0.2627 595 ASP A C 4607 O O . ASP A 595 ? 1.1829 1.7221 1.5686 -0.4112 -0.4146 0.2647 595 ASP A O 4608 C CB . ASP A 595 ? 1.2611 1.7129 1.6590 -0.4538 -0.4454 0.3401 595 ASP A CB 4609 C CG . ASP A 595 ? 1.3125 1.7543 1.7352 -0.4769 -0.4698 0.3804 595 ASP A CG 4610 O OD1 . ASP A 595 ? 1.0732 1.5263 1.4988 -0.4757 -0.4769 0.3816 595 ASP A OD1 4611 O OD2 . ASP A 595 ? 1.3967 1.8185 1.8418 -0.4962 -0.4846 0.4103 595 ASP A OD2 4612 N N . CYS A 596 ? 1.3155 1.7125 1.6787 -0.3831 -0.4177 0.2293 596 CYS A N 4613 C CA . CYS A 596 ? 1.3978 1.8329 1.7723 -0.3603 -0.4090 0.1890 596 CYS A CA 4614 C C . CYS A 596 ? 1.3297 1.8283 1.7273 -0.3479 -0.4148 0.1680 596 CYS A C 4615 O O . CYS A 596 ? 1.2265 1.7622 1.6462 -0.3259 -0.4131 0.1271 596 CYS A O 4616 C CB . CYS A 596 ? 1.3038 1.6484 1.6668 -0.3438 -0.4073 0.1676 596 CYS A CB 4617 S SG . CYS A 596 ? 1.9763 2.2728 2.3181 -0.3512 -0.3966 0.1765 596 CYS A SG 4618 N N . GLY A 597 ? 1.3977 1.9097 1.7956 -0.3613 -0.4240 0.1934 597 GLY A N 4619 C CA . GLY A 597 ? 1.4571 2.0326 1.8765 -0.3514 -0.4300 0.1762 597 GLY A CA 4620 C C . GLY A 597 ? 1.5337 2.0329 1.9548 -0.3347 -0.4395 0.1590 597 GLY A C 4621 O O . GLY A 597 ? 1.5347 1.9369 1.9364 -0.3347 -0.4416 0.1669 597 GLY A O 4622 N N . GLU A 598 ? 1.5965 2.1485 2.0439 -0.3213 -0.4466 0.1361 598 GLU A N 4623 C CA . GLU A 598 ? 1.6789 2.1687 2.1361 -0.3072 -0.4595 0.1238 598 GLU A CA 4624 C C . GLU A 598 ? 1.6638 2.1051 2.1419 -0.2847 -0.4644 0.0905 598 GLU A C 4625 O O . GLU A 598 ? 1.7400 2.1082 2.2226 -0.2791 -0.4769 0.0932 598 GLU A O 4626 C CB . GLU A 598 ? 1.6891 2.2547 2.1749 -0.2993 -0.4680 0.1080 598 GLU A CB 4627 C CG . GLU A 598 ? 1.7931 2.4459 2.3254 -0.2734 -0.4699 0.0530 598 GLU A CG 4628 C CD . GLU A 598 ? 1.8290 2.5825 2.3623 -0.2779 -0.4553 0.0429 598 GLU A CD 4629 O OE1 . GLU A 598 ? 1.8216 2.6058 2.3267 -0.3047 -0.4466 0.0854 598 GLU A OE1 4630 O OE2 . GLU A 598 ? 1.8190 2.6241 2.3869 -0.2551 -0.4553 -0.0072 598 GLU A OE2 4631 N N . ASP A 599 ? 1.7885 1.1516 1.7793 -0.3210 -0.2941 0.1245 599 ASP A N 4632 C CA . ASP A 599 ? 1.7117 1.1049 1.7023 -0.3437 -0.3041 0.1285 599 ASP A CA 4633 C C . ASP A 599 ? 1.6382 1.0415 1.6074 -0.3615 -0.2991 0.1276 599 ASP A C 4634 O O . ASP A 599 ? 1.5876 1.0197 1.5534 -0.3852 -0.3116 0.1360 599 ASP A O 4635 C CB . ASP A 599 ? 1.5580 0.9717 1.5702 -0.3403 -0.3000 0.1248 599 ASP A CB 4636 C CG . ASP A 599 ? 1.9360 1.3444 1.9509 -0.3259 -0.2753 0.1142 599 ASP A CG 4637 O OD1 . ASP A 599 ? 2.0812 1.4753 2.0795 -0.3231 -0.2633 0.1100 599 ASP A OD1 4638 O OD2 . ASP A 599 ? 2.0237 1.4403 2.0566 -0.3167 -0.2694 0.1104 599 ASP A OD2 4639 N N . ASN A 600 ? 1.8063 1.1867 1.7620 -0.3501 -0.2835 0.1194 600 ASN A N 4640 C CA . ASN A 600 ? 1.8909 1.2791 1.8278 -0.3647 -0.2760 0.1156 600 ASN A CA 4641 C C . ASN A 600 ? 1.8445 1.2739 1.7921 -0.3811 -0.2690 0.1140 600 ASN A C 4642 O O . ASN A 600 ? 1.9170 1.3768 1.8559 -0.4056 -0.2700 0.1167 600 ASN A O 4643 C CB . ASN A 600 ? 1.8288 1.2227 1.7466 -0.3871 -0.2919 0.1253 600 ASN A CB 4644 C CG . ASN A 600 ? 2.0257 1.3764 1.9282 -0.3711 -0.2978 0.1244 600 ASN A CG 4645 O OD1 . ASN A 600 ? 1.8682 1.1840 1.7663 -0.3460 -0.2895 0.1156 600 ASN A OD1 4646 N ND2 . ASN A 600 ? 2.1451 1.4974 2.0385 -0.3853 -0.3163 0.1354 600 ASN A ND2 4647 N N . VAL A 601 ? 1.6651 1.1005 1.6329 -0.3690 -0.2635 0.1106 601 VAL A N 4648 C CA . VAL A 601 ? 1.4788 0.9494 1.4584 -0.3796 -0.2570 0.1075 601 VAL A CA 4649 C C . VAL A 601 ? 1.5634 1.0145 1.5548 -0.3534 -0.2380 0.0963 601 VAL A C 4650 O O . VAL A 601 ? 1.4762 0.9032 1.4753 -0.3329 -0.2374 0.0966 601 VAL A O 4651 C CB . VAL A 601 ? 1.4377 0.9435 1.4296 -0.3980 -0.2799 0.1201 601 VAL A CB 4652 C CG1 . VAL A 601 ? 1.4906 1.0229 1.4687 -0.4280 -0.3008 0.1369 601 VAL A CG1 4653 C CG2 . VAL A 601 ? 1.5947 1.0803 1.6000 -0.3810 -0.2904 0.1217 601 VAL A CG2 4654 N N . CYS A 602 ? 1.4586 0.9241 1.4526 -0.3555 -0.2233 0.0879 602 CYS A N 4655 C CA . CYS A 602 ? 1.2843 0.7288 1.2859 -0.3306 -0.2052 0.0792 602 CYS A CA 4656 C C . CYS A 602 ? 1.5120 0.9842 1.5339 -0.3338 -0.2073 0.0789 602 CYS A C 4657 O O . CYS A 602 ? 1.7274 1.2387 1.7566 -0.3526 -0.2105 0.0777 602 CYS A O 4658 C CB . CYS A 602 ? 1.2376 0.6729 1.2293 -0.3259 -0.1889 0.0685 602 CYS A CB 4659 S SG . CYS A 602 ? 1.7413 1.1205 1.7051 -0.3059 -0.1887 0.0653 602 CYS A SG 4660 N N . LYS A 603 ? 1.4059 0.8611 1.4381 -0.3159 -0.2078 0.0804 603 LYS A N 4661 C CA . LYS A 603 ? 1.5389 1.0118 1.5889 -0.3141 -0.2101 0.0778 603 LYS A CA 4662 C C . LYS A 603 ? 1.6487 1.0982 1.7024 -0.2892 -0.1887 0.0730 603 LYS A C 4663 O O . LYS A 603 ? 1.7677 1.1935 1.8237 -0.2715 -0.1855 0.0778 603 LYS A O 4664 C CB . LYS A 603 ? 1.5246 1.0021 1.5861 -0.3160 -0.2317 0.0840 603 LYS A CB 4665 C CG . LYS A 603 ? 1.7331 1.2316 1.7902 -0.3396 -0.2579 0.0938 603 LYS A CG 4666 C CD . LYS A 603 ? 1.9391 1.4337 2.0074 -0.3373 -0.2809 0.1003 603 LYS A CD 4667 C CE . LYS A 603 ? 1.9716 1.4380 2.0388 -0.3220 -0.2740 0.1012 603 LYS A CE 4668 N NZ . LYS A 603 ? 1.9704 1.4359 2.0509 -0.3211 -0.2970 0.1072 603 LYS A NZ 4669 N N . PRO A 604 ? 1.6687 1.1276 1.7236 -0.2887 -0.1758 0.0659 604 PRO A N 4670 C CA . PRO A 604 ? 1.5909 1.0257 1.6462 -0.2644 -0.1563 0.0648 604 PRO A CA 4671 C C . PRO A 604 ? 1.6053 1.0510 1.6764 -0.2594 -0.1575 0.0628 604 PRO A C 4672 O O . PRO A 604 ? 1.6518 1.1221 1.7342 -0.2734 -0.1763 0.0601 604 PRO A O 4673 C CB . PRO A 604 ? 1.1967 0.6293 1.2410 -0.2695 -0.1530 0.0615 604 PRO A CB 4674 C CG . PRO A 604 ? 1.1389 0.6129 1.1850 -0.3045 -0.1753 0.0612 604 PRO A CG 4675 C CD . PRO A 604 ? 1.3087 0.8051 1.3662 -0.3115 -0.1805 0.0610 604 PRO A CD 4676 N N . LYS A 605 ? 1.5328 0.9581 1.6036 -0.2378 -0.1404 0.0658 605 LYS A N 4677 C CA . LYS A 605 ? 1.8189 1.2525 1.9009 -0.2322 -0.1378 0.0619 605 LYS A CA 4678 C C . LYS A 605 ? 1.8768 1.2871 1.9520 -0.2241 -0.1463 0.0713 605 LYS A C 4679 O O . LYS A 605 ? 1.4769 0.8583 1.5443 -0.2025 -0.1370 0.0840 605 LYS A O 4680 C CB . LYS A 605 ? 1.6082 1.0294 1.6997 -0.2174 -0.1379 0.0709 605 LYS A CB 4681 C CG . LYS A 605 ? 1.8054 1.2351 1.9088 -0.2127 -0.1394 0.0647 605 LYS A CG 4682 C CD . LYS A 605 ? 1.6744 1.0950 1.7892 -0.2001 -0.1395 0.0747 605 LYS A CD 4683 C CE . LYS A 605 ? 1.7398 1.1377 1.8475 -0.1786 -0.1200 0.0954 605 LYS A CE 4684 N NZ . LYS A 605 ? 1.7498 1.1359 1.8560 -0.1652 -0.1178 0.1041 605 LYS A NZ 4685 N N . LEU A 606 ? 1.8296 1.2525 1.9082 -0.2413 -0.1720 0.0682 606 LEU A N 4686 C CA . LEU A 606 ? 1.7418 1.1403 1.8115 -0.2369 -0.1873 0.0776 606 LEU A CA 4687 C C . LEU A 606 ? 1.7888 1.1793 1.8732 -0.2222 -0.1954 0.0805 606 LEU A C 4688 O O . LEU A 606 ? 1.7465 1.1582 1.8465 -0.2290 -0.2066 0.0699 606 LEU A O 4689 C CB . LEU A 606 ? 1.6222 1.0419 1.6824 -0.2691 -0.2124 0.0750 606 LEU A CB 4690 C CG . LEU A 606 ? 1.3494 0.7787 1.3955 -0.2863 -0.2101 0.0747 606 LEU A CG 4691 C CD1 . LEU A 606 ? 1.6463 1.1220 1.6889 -0.3275 -0.2372 0.0774 606 LEU A CD1 4692 C CD2 . LEU A 606 ? 1.1656 0.5424 1.1865 -0.2654 -0.2047 0.0813 606 LEU A CD2 4693 N N . GLU A 607 ? 1.7136 1.0716 1.7938 -0.1976 -0.1933 0.0954 607 GLU A N 4694 C CA . GLU A 607 ? 1.7242 1.0912 1.8181 -0.1705 -0.1919 0.1003 607 GLU A CA 4695 C C . GLU A 607 ? 1.6506 1.0744 1.7254 -0.1332 -0.1735 0.0969 607 GLU A C 4696 O O . GLU A 607 ? 1.5327 0.9493 1.5929 -0.1180 -0.1640 0.1045 607 GLU A O 4697 C CB . GLU A 607 ? 1.8796 1.2236 1.9887 -0.1509 -0.1773 0.1210 607 GLU A CB 4698 C CG . GLU A 607 ? 1.9980 1.3647 2.1240 -0.1195 -0.1740 0.1308 607 GLU A CG 4699 C CD . GLU A 607 ? 2.1968 1.5443 2.3439 -0.1085 -0.1657 0.1588 607 GLU A CD 4700 O OE1 . GLU A 607 ? 2.2316 1.6099 2.3921 -0.0754 -0.1564 0.1805 607 GLU A OE1 4701 O OE2 . GLU A 607 ? 2.1467 1.5018 2.2833 -0.1227 -0.1515 0.1494 607 GLU A OE2 4702 N N . VAL A 608 ? 1.7121 1.1884 1.7873 -0.1173 -0.1732 0.0836 608 VAL A N 4703 C CA . VAL A 608 ? 1.6137 1.1419 1.6732 -0.0836 -0.1565 0.0801 608 VAL A CA 4704 C C . VAL A 608 ? 1.5870 1.1389 1.6571 -0.0475 -0.1450 0.0873 608 VAL A C 4705 O O . VAL A 608 ? 1.4878 1.0459 1.5698 -0.0450 -0.1553 0.0799 608 VAL A O 4706 C CB . VAL A 608 ? 1.5757 1.1527 1.6234 -0.0939 -0.1668 0.0616 608 VAL A CB 4707 C CG1 . VAL A 608 ? 1.6113 1.2325 1.6407 -0.0642 -0.1479 0.0593 608 VAL A CG1 4708 C CG2 . VAL A 608 ? 1.5890 1.1575 1.6337 -0.1366 -0.1840 0.0590 608 VAL A CG2 4709 N N . SER A 609 ? 1.6087 1.1784 1.6749 -0.0182 -0.1274 0.1012 609 SER A N 4710 C CA . SER A 609 ? 1.6433 1.2480 1.7206 0.0154 -0.1155 0.1143 609 SER A CA 4711 C C . SER A 609 ? 1.7508 1.3990 1.8161 0.0412 -0.1025 0.1125 609 SER A C 4712 O O . SER A 609 ? 1.8337 1.4706 1.8913 0.0409 -0.1013 0.1160 609 SER A O 4713 C CB . SER A 609 ? 1.6390 1.2160 1.7395 0.0200 -0.1132 0.1499 609 SER A CB 4714 O OG . SER A 609 ? 1.7010 1.3283 1.8154 0.0511 -0.1020 0.1683 609 SER A OG 4715 N N . VAL A 610 ? 1.7641 1.4603 1.8269 0.0654 -0.0961 0.1044 610 VAL A N 4716 C CA . VAL A 610 ? 1.7228 1.4589 1.7761 0.0885 -0.0841 0.1029 610 VAL A CA 4717 C C . VAL A 610 ? 1.9176 1.7017 1.9808 0.1209 -0.0732 0.1167 610 VAL A C 4718 O O . VAL A 610 ? 1.9817 1.7881 2.0423 0.1345 -0.0765 0.1040 610 VAL A O 4719 C CB . VAL A 610 ? 1.4929 1.2460 1.5251 0.0835 -0.0889 0.0743 610 VAL A CB 4720 C CG1 . VAL A 610 ? 1.5849 1.3776 1.6091 0.1091 -0.0763 0.0724 610 VAL A CG1 4721 C CG2 . VAL A 610 ? 1.3997 1.1288 1.4217 0.0554 -0.0959 0.0663 610 VAL A CG2 4722 N N . ASP A 611 ? 2.0060 1.8100 2.0815 0.1345 -0.0649 0.1427 611 ASP A N 4723 C CA . ASP A 611 ? 2.1073 1.9715 2.1931 0.1638 -0.0539 0.1606 611 ASP A CA 4724 C C . ASP A 611 ? 2.1164 2.0107 2.1850 0.1783 -0.0469 0.1419 611 ASP A C 4725 O O . ASP A 611 ? 1.9094 1.7789 1.9616 0.1654 -0.0504 0.1194 611 ASP A O 4726 C CB . ASP A 611 ? 2.1055 1.9810 2.2228 0.1658 -0.0559 0.2089 611 ASP A CB 4727 C CG . ASP A 611 ? 2.1700 2.1204 2.3045 0.1924 -0.0454 0.2376 611 ASP A CG 4728 O OD1 . ASP A 611 ? 2.0500 2.0475 2.1673 0.2160 -0.0346 0.2166 611 ASP A OD1 4729 O OD2 . ASP A 611 ? 2.2935 2.2591 2.4590 0.1910 -0.0501 0.2838 611 ASP A OD2 4730 N N . SER A 612 ? 2.2734 2.2256 2.3463 0.2054 -0.0369 0.1531 612 SER A N 4731 C CA . SER A 612 ? 2.4164 2.3929 2.4742 0.2188 -0.0306 0.1374 612 SER A CA 4732 C C . SER A 612 ? 2.3966 2.4087 2.4759 0.2249 -0.0264 0.1690 612 SER A C 4733 O O . SER A 612 ? 2.4200 2.4894 2.5157 0.2428 -0.0202 0.1974 612 SER A O 4734 C CB . SER A 612 ? 2.4641 2.4757 2.5028 0.2477 -0.0282 0.1161 612 SER A CB 4735 O OG . SER A 612 ? 2.5218 2.4982 2.5454 0.2405 -0.0434 0.0871 612 SER A OG 4736 N N . ASP A 613 ? 2.2843 2.2685 2.3654 0.2104 -0.0332 0.1648 613 ASP A N 4737 C CA . ASP A 613 ? 2.2260 2.2400 2.3269 0.2146 -0.0368 0.1865 613 ASP A CA 4738 C C . ASP A 613 ? 2.3118 2.3523 2.3922 0.2298 -0.0244 0.1632 613 ASP A C 4739 O O . ASP A 613 ? 2.3212 2.4121 2.4136 0.2429 -0.0196 0.1821 613 ASP A O 4740 C CB . ASP A 613 ? 2.1766 2.1471 2.2883 0.1978 -0.0566 0.1863 613 ASP A CB 4741 C CG . ASP A 613 ? 2.1737 2.1709 2.3168 0.1986 -0.0731 0.2151 613 ASP A CG 4742 O OD1 . ASP A 613 ? 2.1066 2.1155 2.2848 0.1938 -0.0920 0.2593 613 ASP A OD1 4743 O OD2 . ASP A 613 ? 2.1287 2.1351 2.2650 0.2020 -0.0711 0.1968 613 ASP A OD2 4744 N N . GLN A 614 ? 2.3344 2.3423 2.3856 0.2263 -0.0217 0.1257 614 GLN A N 4745 C CA . GLN A 614 ? 2.2067 2.2273 2.2360 0.2403 -0.0144 0.1034 614 GLN A CA 4746 C C . GLN A 614 ? 2.0476 2.0938 2.0620 0.2647 -0.0110 0.0966 614 GLN A C 4747 O O . GLN A 614 ? 2.0065 2.0376 2.0157 0.2633 -0.0174 0.0893 614 GLN A O 4748 C CB . GLN A 614 ? 2.1990 2.1806 2.2075 0.2263 -0.0188 0.0739 614 GLN A CB 4749 C CG . GLN A 614 ? 2.1344 2.0990 2.1516 0.2115 -0.0232 0.0719 614 GLN A CG 4750 C CD . GLN A 614 ? 2.1499 2.1311 2.1716 0.2186 -0.0201 0.0706 614 GLN A CD 4751 O OE1 . GLN A 614 ? 2.1704 2.1729 2.1851 0.2331 -0.0123 0.0707 614 GLN A OE1 4752 N NE2 . GLN A 614 ? 2.1246 2.0944 2.1577 0.2102 -0.0295 0.0669 614 GLN A NE2 4753 N N . LYS A 615 ? 1.9146 1.9989 1.9219 0.2887 -0.0042 0.0969 615 LYS A N 4754 C CA . LYS A 615 ? 1.9329 2.0468 1.9219 0.3219 -0.0052 0.0857 615 LYS A CA 4755 C C . LYS A 615 ? 1.9127 2.0057 1.8722 0.3376 -0.0138 0.0556 615 LYS A C 4756 O O . LYS A 615 ? 2.0313 2.0946 1.9719 0.3447 -0.0327 0.0312 615 LYS A O 4757 C CB . LYS A 615 ? 1.8701 2.0607 1.8743 0.3457 0.0073 0.1156 615 LYS A CB 4758 C CG . LYS A 615 ? 1.8496 2.0665 1.8875 0.3321 0.0100 0.1544 615 LYS A CG 4759 C CD . LYS A 615 ? 1.7631 1.9569 1.7963 0.3325 0.0032 0.1437 615 LYS A CD 4760 C CE . LYS A 615 ? 1.6922 1.9282 1.7035 0.3749 0.0019 0.1241 615 LYS A CE 4761 N NZ . LYS A 615 ? 1.7046 1.9173 1.7155 0.3742 -0.0094 0.1120 615 LYS A NZ 4762 N N . LYS A 616 ? 1.7633 1.8689 1.7219 0.3413 -0.0052 0.0600 616 LYS A N 4763 C CA . LYS A 616 ? 1.6562 1.7405 1.5882 0.3581 -0.0142 0.0370 616 LYS A CA 4764 C C . LYS A 616 ? 1.6046 1.6389 1.5354 0.3290 -0.0186 0.0282 616 LYS A C 4765 O O . LYS A 616 ? 1.6712 1.7047 1.6208 0.3056 -0.0078 0.0399 616 LYS A O 4766 C CB . LYS A 616 ? 1.8033 1.9355 1.7327 0.3836 -0.0023 0.0471 616 LYS A CB 4767 C CG . LYS A 616 ? 1.9707 2.1763 1.9046 0.4141 0.0060 0.0631 616 LYS A CG 4768 C CD . LYS A 616 ? 1.9202 2.1887 1.8611 0.4289 0.0204 0.0844 616 LYS A CD 4769 C CE . LYS A 616 ? 1.8300 2.1921 1.7819 0.4557 0.0307 0.1107 616 LYS A CE 4770 N NZ . LYS A 616 ? 1.8126 2.2503 1.7789 0.4629 0.0435 0.1411 616 LYS A NZ 4771 N N . ILE A 617 ? 1.4913 1.4876 1.4016 0.3322 -0.0393 0.0089 617 ILE A N 4772 C CA . ILE A 617 ? 1.4281 1.3895 1.3361 0.3093 -0.0444 0.0048 617 ILE A CA 4773 C C . ILE A 617 ? 1.4863 1.4284 1.3743 0.3302 -0.0580 -0.0040 617 ILE A C 4774 O O . ILE A 617 ? 1.5499 1.4752 1.4200 0.3529 -0.0855 -0.0158 617 ILE A O 4775 C CB . ILE A 617 ? 1.3833 1.3191 1.2920 0.2848 -0.0628 0.0006 617 ILE A CB 4776 C CG1 . ILE A 617 ? 1.4052 1.3510 1.3325 0.2599 -0.0475 0.0093 617 ILE A CG1 4777 C CG2 . ILE A 617 ? 1.3670 1.2798 1.2704 0.2691 -0.0742 0.0003 617 ILE A CG2 4778 C CD1 . ILE A 617 ? 1.4047 1.3596 1.3449 0.2481 -0.0281 0.0160 617 ILE A CD1 4779 N N . TYR A 618 ? 1.4584 1.3980 1.3504 0.3234 -0.0438 0.0009 618 TYR A N 4780 C CA . TYR A 618 ? 1.3428 1.2608 1.2170 0.3433 -0.0538 -0.0045 618 TYR A CA 4781 C C . TYR A 618 ? 1.4642 1.3379 1.3315 0.3291 -0.0773 -0.0054 618 TYR A C 4782 O O . TYR A 618 ? 1.5853 1.4574 1.4661 0.2987 -0.0705 0.0012 618 TYR A O 4783 C CB . TYR A 618 ? 1.2914 1.2268 1.1768 0.3398 -0.0300 0.0035 618 TYR A CB 4784 C CG . TYR A 618 ? 1.3552 1.3456 1.2537 0.3508 -0.0123 0.0147 618 TYR A CG 4785 C CD1 . TYR A 618 ? 1.4821 1.5038 1.3661 0.3851 -0.0170 0.0121 618 TYR A CD1 4786 C CD2 . TYR A 618 ? 1.4105 1.4265 1.3385 0.3280 0.0038 0.0303 618 TYR A CD2 4787 C CE1 . TYR A 618 ? 1.5317 1.6181 1.4308 0.3949 -0.0007 0.0299 618 TYR A CE1 4788 C CE2 . TYR A 618 ? 1.4970 1.5698 1.4436 0.3343 0.0135 0.0505 618 TYR A CE2 4789 C CZ . TYR A 618 ? 1.5210 1.6335 1.4534 0.3669 0.0139 0.0530 618 TYR A CZ 4790 O OH . TYR A 618 ? 1.5584 1.7414 1.5122 0.3730 0.0240 0.0803 618 TYR A OH 4791 N N . ILE A 619 ? 1.4783 1.3205 1.3252 0.3540 -0.1087 -0.0116 619 ILE A N 4792 C CA . ILE A 619 ? 1.4726 1.2731 1.3165 0.3417 -0.1416 -0.0040 619 ILE A CA 4793 C C . ILE A 619 ? 1.5772 1.3590 1.4239 0.3304 -0.1292 0.0057 619 ILE A C 4794 O O . ILE A 619 ? 1.5285 1.3088 1.3684 0.3468 -0.1122 0.0008 619 ILE A O 4795 C CB . ILE A 619 ? 1.3499 1.1141 1.1731 0.3755 -0.1924 -0.0129 619 ILE A CB 4796 C CG1 . ILE A 619 ? 1.4642 1.2480 1.2845 0.3919 -0.2068 -0.0277 619 ILE A CG1 4797 C CG2 . ILE A 619 ? 1.5631 1.2869 1.3915 0.3571 -0.2372 0.0045 619 ILE A CG2 4798 C CD1 . ILE A 619 ? 1.5578 1.3030 1.3620 0.4232 -0.2702 -0.0402 619 ILE A CD1 4799 N N . GLY A 620 ? 1.6766 1.4495 1.5348 0.3017 -0.1385 0.0212 620 GLY A N 4800 C CA . GLY A 620 ? 1.7726 1.5263 1.6347 0.2911 -0.1320 0.0322 620 GLY A CA 4801 C C . GLY A 620 ? 1.8350 1.6227 1.7163 0.2633 -0.0966 0.0339 620 GLY A C 4802 O O . GLY A 620 ? 1.9783 1.7563 1.8659 0.2521 -0.0917 0.0426 620 GLY A O 4803 N N . ASP A 621 ? 1.8184 1.6440 1.7090 0.2546 -0.0756 0.0247 621 ASP A N 4804 C CA . ASP A 621 ? 1.9040 1.7603 1.8111 0.2349 -0.0499 0.0209 621 ASP A CA 4805 C C . ASP A 621 ? 1.7634 1.6537 1.6774 0.2233 -0.0441 0.0171 621 ASP A C 4806 O O . ASP A 621 ? 1.6531 1.5438 1.5628 0.2302 -0.0508 0.0151 621 ASP A O 4807 C CB . ASP A 621 ? 1.8729 1.7297 1.7886 0.2407 -0.0280 0.0097 621 ASP A CB 4808 C CG . ASP A 621 ? 1.7746 1.6493 1.6932 0.2519 -0.0198 0.0047 621 ASP A CG 4809 O OD1 . ASP A 621 ? 1.8123 1.6851 1.7182 0.2662 -0.0313 0.0062 621 ASP A OD1 4810 O OD2 . ASP A 621 ? 1.5203 1.4132 1.4566 0.2466 -0.0062 0.0012 621 ASP A OD2 4811 N N . ASP A 622 ? 1.7880 1.7070 1.7116 0.2082 -0.0329 0.0148 622 ASP A N 4812 C CA . ASP A 622 ? 1.9082 1.8560 1.8371 0.2004 -0.0259 0.0077 622 ASP A CA 4813 C C . ASP A 622 ? 1.8064 1.7506 1.7448 0.2093 -0.0137 -0.0038 622 ASP A C 4814 O O . ASP A 622 ? 1.7178 1.6500 1.6623 0.2168 -0.0079 -0.0067 622 ASP A O 4815 C CB . ASP A 622 ? 2.0675 2.0529 2.0006 0.1897 -0.0197 0.0048 622 ASP A CB 4816 C CG . ASP A 622 ? 2.1881 2.1740 2.1282 0.1944 -0.0099 -0.0047 622 ASP A CG 4817 O OD1 . ASP A 622 ? 2.2076 2.1702 2.1553 0.2021 -0.0043 -0.0153 622 ASP A OD1 4818 O OD2 . ASP A 622 ? 2.2347 2.2495 2.1749 0.1892 -0.0094 0.0006 622 ASP A OD2 4819 N N . ASN A 623 ? 1.8160 1.7716 1.7583 0.2060 -0.0130 -0.0061 623 ASN A N 4820 C CA . ASN A 623 ? 1.7416 1.6962 1.6971 0.2124 -0.0084 -0.0068 623 ASN A CA 4821 C C . ASN A 623 ? 1.5823 1.5441 1.5416 0.2059 -0.0115 -0.0067 623 ASN A C 4822 O O . ASN A 623 ? 1.5558 1.5189 1.5047 0.1982 -0.0166 -0.0040 623 ASN A O 4823 C CB . ASN A 623 ? 1.8801 1.8265 1.8320 0.2264 -0.0083 0.0023 623 ASN A CB 4824 C CG . ASN A 623 ? 1.6912 1.6267 1.6252 0.2310 -0.0204 0.0049 623 ASN A CG 4825 O OD1 . ASN A 623 ? 1.6304 1.5657 1.5593 0.2178 -0.0300 0.0053 623 ASN A OD1 4826 N ND2 . ASN A 623 ? 1.5462 1.4771 1.4719 0.2512 -0.0245 0.0069 623 ASN A ND2 4827 N N . PRO A 624 ? 1.6217 1.5854 1.5984 0.2073 -0.0137 -0.0074 624 PRO A N 4828 C CA . PRO A 624 ? 1.6890 1.6510 1.6690 0.2022 -0.0202 -0.0066 624 PRO A CA 4829 C C . PRO A 624 ? 1.6889 1.6446 1.6656 0.2003 -0.0194 0.0069 624 PRO A C 4830 O O . PRO A 624 ? 1.7912 1.7501 1.7753 0.2090 -0.0167 0.0195 624 PRO A O 4831 C CB . PRO A 624 ? 1.8008 1.7592 1.8054 0.2063 -0.0322 -0.0036 624 PRO A CB 4832 C CG . PRO A 624 ? 1.8486 1.8132 1.8658 0.2106 -0.0289 0.0061 624 PRO A CG 4833 C CD . PRO A 624 ? 1.7367 1.7012 1.7341 0.2119 -0.0170 -0.0051 624 PRO A CD 4834 N N . LEU A 625 ? 1.6142 1.5667 1.5805 0.1894 -0.0229 0.0040 625 LEU A N 4835 C CA . LEU A 625 ? 1.6017 1.5442 1.5674 0.1852 -0.0266 0.0133 625 LEU A CA 4836 C C . LEU A 625 ? 1.6260 1.5580 1.5951 0.1736 -0.0322 0.0133 625 LEU A C 4837 O O . LEU A 625 ? 1.6216 1.5603 1.5799 0.1626 -0.0352 0.0044 625 LEU A O 4838 C CB . LEU A 625 ? 1.5953 1.5373 1.5467 0.1798 -0.0344 0.0110 625 LEU A CB 4839 C CG . LEU A 625 ? 1.5926 1.5231 1.5436 0.1806 -0.0449 0.0153 625 LEU A CG 4840 C CD1 . LEU A 625 ? 1.6744 1.5950 1.6281 0.1589 -0.0533 0.0166 625 LEU A CD1 4841 C CD2 . LEU A 625 ? 1.5995 1.5351 1.5603 0.2001 -0.0362 0.0236 625 LEU A CD2 4842 N N . THR A 626 ? 1.6531 1.5723 1.6380 0.1766 -0.0352 0.0266 626 THR A N 4843 C CA . THR A 626 ? 1.7134 1.6124 1.7025 0.1681 -0.0446 0.0285 626 THR A CA 4844 C C . THR A 626 ? 1.6402 1.5219 1.6360 0.1600 -0.0468 0.0435 626 THR A C 4845 O O . THR A 626 ? 1.7018 1.5889 1.7128 0.1687 -0.0446 0.0618 626 THR A O 4846 C CB . THR A 626 ? 1.8385 1.7285 1.8459 0.1779 -0.0574 0.0344 626 THR A CB 4847 O OG1 . THR A 626 ? 1.7279 1.6338 1.7311 0.1868 -0.0580 0.0169 626 THR A OG1 4848 C CG2 . THR A 626 ? 1.9245 1.7857 1.9317 0.1737 -0.0737 0.0329 626 THR A CG2 4849 N N . LEU A 627 ? 1.5182 1.3855 1.5039 0.1431 -0.0516 0.0370 627 LEU A N 4850 C CA . LEU A 627 ? 1.4486 1.2935 1.4417 0.1319 -0.0564 0.0482 627 LEU A CA 4851 C C . LEU A 627 ? 1.4837 1.2954 1.4846 0.1252 -0.0659 0.0571 627 LEU A C 4852 O O . LEU A 627 ? 1.5126 1.3186 1.5018 0.1216 -0.0716 0.0443 627 LEU A O 4853 C CB . LEU A 627 ? 1.3989 1.2448 1.3803 0.1129 -0.0629 0.0376 627 LEU A CB 4854 C CG . LEU A 627 ? 1.4838 1.3531 1.4570 0.1194 -0.0650 0.0295 627 LEU A CG 4855 C CD1 . LEU A 627 ? 1.4319 1.2997 1.4008 0.0957 -0.0846 0.0246 627 LEU A CD1 4856 C CD2 . LEU A 627 ? 1.7764 1.6513 1.7565 0.1423 -0.0613 0.0350 627 LEU A CD2 4857 N N . ILE A 628 ? 1.4388 1.2315 1.4592 0.1263 -0.0697 0.0801 628 ILE A N 4858 C CA . ILE A 628 ? 1.3661 1.1166 1.3959 0.1190 -0.0844 0.0934 628 ILE A CA 4859 C C . ILE A 628 ? 1.4145 1.1364 1.4414 0.0967 -0.0863 0.0934 628 ILE A C 4860 O O . ILE A 628 ? 1.3893 1.1142 1.4271 0.0939 -0.0823 0.1039 628 ILE A O 4861 C CB . ILE A 628 ? 1.3922 1.1372 1.4521 0.1304 -0.0944 0.1283 628 ILE A CB 4862 C CG1 . ILE A 628 ? 1.7059 1.4858 1.7797 0.1367 -0.0806 0.1472 628 ILE A CG1 4863 C CG2 . ILE A 628 ? 1.3174 1.0772 1.3845 0.1465 -0.1053 0.1282 628 ILE A CG2 4864 C CD1 . ILE A 628 ? 1.7203 1.4869 1.8223 0.1340 -0.0892 0.1865 628 ILE A CD1 4865 N N . VAL A 629 ? 1.4917 1.1902 1.5037 0.0821 -0.0942 0.0799 629 VAL A N 4866 C CA . VAL A 629 ? 1.5538 1.2243 1.5640 0.0553 -0.0992 0.0790 629 VAL A CA 4867 C C . VAL A 629 ? 1.5766 1.1893 1.5982 0.0495 -0.1128 0.0979 629 VAL A C 4868 O O . VAL A 629 ? 1.5809 1.1713 1.5982 0.0618 -0.1252 0.0991 629 VAL A O 4869 C CB . VAL A 629 ? 1.4864 1.1767 1.4745 0.0372 -0.1009 0.0570 629 VAL A CB 4870 C CG1 . VAL A 629 ? 1.4661 1.2051 1.4489 0.0358 -0.0951 0.0463 629 VAL A CG1 4871 C CG2 . VAL A 629 ? 1.6907 1.3875 1.6614 0.0522 -0.1040 0.0452 629 VAL A CG2 4872 N N . LYS A 630 ? 1.5505 1.1358 1.5874 0.0331 -0.1148 0.1123 630 LYS A N 4873 C CA . LYS A 630 ? 1.4474 0.9706 1.4963 0.0226 -0.1290 0.1332 630 LYS A CA 4874 C C . LYS A 630 ? 1.4135 0.9070 1.4543 -0.0111 -0.1342 0.1205 630 LYS A C 4875 O O . LYS A 630 ? 1.4809 0.9771 1.5321 -0.0282 -0.1328 0.1191 630 LYS A O 4876 C CB . LYS A 630 ? 1.5409 1.0582 1.6207 0.0309 -0.1287 0.1683 630 LYS A CB 4877 C CG . LYS A 630 ? 1.6973 1.1476 1.7953 0.0188 -0.1457 0.1983 630 LYS A CG 4878 C CD . LYS A 630 ? 1.6912 1.1552 1.8236 0.0336 -0.1479 0.2434 630 LYS A CD 4879 C CE . LYS A 630 ? 1.8036 1.2071 1.9589 0.0171 -0.1618 0.2773 630 LYS A CE 4880 N NZ . LYS A 630 ? 1.6648 1.0639 1.8196 -0.0038 -0.1500 0.2615 630 LYS A NZ 4881 N N . ALA A 631 ? 1.3600 0.8275 1.3823 -0.0192 -0.1441 0.1103 631 ALA A N 4882 C CA . ALA A 631 ? 1.3812 0.8280 1.3953 -0.0544 -0.1509 0.1000 631 ALA A CA 4883 C C . ALA A 631 ? 1.5161 0.8843 1.5344 -0.0640 -0.1667 0.1161 631 ALA A C 4884 O O . ALA A 631 ? 1.6424 0.9859 1.6450 -0.0463 -0.1781 0.1141 631 ALA A O 4885 C CB . ALA A 631 ? 1.2977 0.7944 1.2843 -0.0580 -0.1487 0.0759 631 ALA A CB 4886 N N . GLN A 632 ? 1.5433 0.8693 1.5827 -0.0901 -0.1711 0.1305 632 GLN A N 4887 C CA . GLN A 632 ? 1.7170 0.9853 1.7619 -0.0980 -0.1782 0.1452 632 GLN A CA 4888 C C . GLN A 632 ? 1.7597 1.0453 1.8009 -0.1320 -0.1690 0.1271 632 GLN A C 4889 O O . GLN A 632 ? 1.7459 1.0544 1.7972 -0.1554 -0.1691 0.1179 632 GLN A O 4890 C CB . GLN A 632 ? 1.9147 1.2023 1.9828 -0.0808 -0.1623 0.1676 632 GLN A CB 4891 C CG . GLN A 632 ? 1.8960 1.2046 1.9851 -0.0892 -0.1559 0.1718 632 GLN A CG 4892 C CD . GLN A 632 ? 2.0242 1.3503 2.1331 -0.0712 -0.1452 0.1989 632 GLN A CD 4893 O OE1 . GLN A 632 ? 2.0971 1.4370 2.2284 -0.0545 -0.1494 0.2203 632 GLN A OE1 4894 N NE2 . GLN A 632 ? 2.0725 1.4014 2.1739 -0.0733 -0.1327 0.2008 632 GLN A NE2 4895 N N . ASN A 633 ? 1.7795 1.0574 1.8083 -0.1319 -0.1649 0.1219 633 ASN A N 4896 C CA . ASN A 633 ? 1.6849 0.9856 1.7145 -0.1579 -0.1532 0.1080 633 ASN A CA 4897 C C . ASN A 633 ? 1.5087 0.8170 1.5443 -0.1457 -0.1295 0.1123 633 ASN A C 4898 O O . ASN A 633 ? 1.4322 0.7216 1.4580 -0.1293 -0.1313 0.1168 633 ASN A O 4899 C CB . ASN A 633 ? 1.6587 0.9441 1.6646 -0.1737 -0.1722 0.0975 633 ASN A CB 4900 C CG . ASN A 633 ? 1.5209 0.8340 1.5311 -0.1958 -0.1601 0.0874 633 ASN A CG 4901 O OD1 . ASN A 633 ? 1.5179 0.8665 1.5482 -0.2061 -0.1422 0.0822 633 ASN A OD1 4902 N ND2 . ASN A 633 ? 1.2440 0.5366 1.2325 -0.1996 -0.1734 0.0835 633 ASN A ND2 4903 N N . GLN A 634 ? 1.3896 0.7233 1.4383 -0.1533 -0.1113 0.1095 634 GLN A N 4904 C CA . GLN A 634 ? 1.5668 0.9002 1.6230 -0.1509 -0.1151 0.1183 634 GLN A CA 4905 C C . GLN A 634 ? 1.6534 1.0018 1.7139 -0.1750 -0.1265 0.1063 634 GLN A C 4906 O O . GLN A 634 ? 1.6765 1.0466 1.7483 -0.1894 -0.1289 0.0985 634 GLN A O 4907 C CB . GLN A 634 ? 1.5060 0.8469 1.5780 -0.1420 -0.1117 0.1328 634 GLN A CB 4908 C CG . GLN A 634 ? 1.5719 0.9001 1.6465 -0.1185 -0.1146 0.1570 634 GLN A CG 4909 C CD . GLN A 634 ? 1.6734 0.9887 1.7321 -0.0993 -0.1071 0.1603 634 GLN A CD 4910 O OE1 . GLN A 634 ? 1.6848 1.0006 1.7479 -0.1039 -0.1152 0.1565 634 GLN A OE1 4911 N NE2 . GLN A 634 ? 1.7750 1.0759 1.8325 -0.0820 -0.1218 0.1737 634 GLN A NE2 4912 N N . GLY A 635 ? 1.8075 1.1430 1.8581 -0.1772 -0.1373 0.1061 635 GLY A N 4913 C CA . GLY A 635 ? 1.7305 1.0785 1.7807 -0.1985 -0.1492 0.0982 635 GLY A CA 4914 C C . GLY A 635 ? 1.7692 1.1013 1.7992 -0.2005 -0.1532 0.0930 635 GLY A C 4915 O O . GLY A 635 ? 1.6300 0.9379 1.6472 -0.1820 -0.1497 0.0945 635 GLY A O 4916 N N . GLU A 636 ? 1.7622 1.1073 1.7884 -0.2212 -0.1630 0.0874 636 GLU A N 4917 C CA . GLU A 636 ? 1.8665 1.1977 1.8724 -0.2255 -0.1672 0.0823 636 GLU A CA 4918 C C . GLU A 636 ? 1.8283 1.1664 1.8270 -0.2298 -0.1542 0.0714 636 GLU A C 4919 O O . GLU A 636 ? 1.7326 1.0953 1.7439 -0.2374 -0.1454 0.0676 636 GLU A O 4920 C CB . GLU A 636 ? 1.7589 1.1074 1.7636 -0.2492 -0.1813 0.0823 636 GLU A CB 4921 C CG . GLU A 636 ? 1.5393 0.8811 1.5529 -0.2447 -0.1947 0.0921 636 GLU A CG 4922 C CD . GLU A 636 ? 1.7817 1.1407 1.7946 -0.2664 -0.2103 0.0938 636 GLU A CD 4923 O OE1 . GLU A 636 ? 1.7208 1.0958 1.7236 -0.2857 -0.2124 0.0899 636 GLU A OE1 4924 O OE2 . GLU A 636 ? 1.7158 1.0741 1.7392 -0.2650 -0.2219 0.1007 636 GLU A OE2 4925 N N . GLY A 637 ? 1.6724 0.9847 1.6491 -0.2246 -0.1593 0.0665 637 GLY A N 4926 C CA . GLY A 637 ? 1.4451 0.7226 1.3865 -0.2360 -0.1971 0.0687 637 GLY A CA 4927 C C . GLY A 637 ? 1.6367 0.9570 1.5801 -0.2800 -0.2095 0.0702 637 GLY A C 4928 O O . GLY A 637 ? 1.7397 1.1121 1.7029 -0.3051 -0.2019 0.0694 637 GLY A O 4929 N N . ALA A 638 ? 1.6871 0.9907 1.6112 -0.2879 -0.2299 0.0729 638 ALA A N 4930 C CA . ALA A 638 ? 1.4292 0.7912 1.3595 -0.3346 -0.2432 0.0781 638 ALA A CA 4931 C C . ALA A 638 ? 1.3131 0.7596 1.2040 -0.3288 -0.2465 0.0705 638 ALA A C 4932 O O . ALA A 638 ? 1.2767 0.7545 1.1405 -0.2714 -0.2332 0.0554 638 ALA A O 4933 C CB . ALA A 638 ? 1.2508 0.6185 1.2017 -0.3221 -0.2369 0.0796 638 ALA A CB 4934 N N . TYR A 639 ? 1.4170 0.9320 1.3102 -0.3756 -0.2569 0.0796 639 TYR A N 4935 C CA . TYR A 639 ? 1.4713 1.1146 1.3327 -0.3595 -0.2494 0.0751 639 TYR A CA 4936 C C . TYR A 639 ? 1.4442 1.1953 1.3114 -0.3413 -0.2366 0.0762 639 TYR A C 4937 O O . TYR A 639 ? 1.4095 1.1814 1.3150 -0.3788 -0.2463 0.0920 639 TYR A O 4938 C CB . TYR A 639 ? 1.4888 1.1907 1.3608 -0.4232 -0.2673 0.0946 639 TYR A CB 4939 C CG . TYR A 639 ? 1.6496 1.2502 1.5139 -0.4456 -0.2807 0.0942 639 TYR A CG 4940 C CD1 . TYR A 639 ? 1.5350 1.0656 1.3561 -0.3908 -0.2751 0.0736 639 TYR A CD1 4941 C CD2 . TYR A 639 ? 1.7496 1.3389 1.6530 -0.4966 -0.2921 0.1110 639 TYR A CD2 4942 C CE1 . TYR A 639 ? 1.8114 1.2410 1.6250 -0.4107 -0.2904 0.0754 639 TYR A CE1 4943 C CE2 . TYR A 639 ? 1.6026 1.1429 1.5049 -0.4720 -0.2794 0.1038 639 TYR A CE2 4944 C CZ . TYR A 639 ? 1.7421 1.1891 1.6002 -0.4501 -0.2869 0.0912 639 TYR A CZ 4945 O OH . TYR A 639 ? 2.0208 1.4345 1.8847 -0.4242 -0.2734 0.0857 639 TYR A OH 4946 N N . GLU A 640 ? 1.4090 1.2246 1.2381 -0.2818 -0.2192 0.0579 640 GLU A N 4947 C CA . GLU A 640 ? 1.3670 1.2912 1.1969 -0.2610 -0.2057 0.0589 640 GLU A CA 4948 C C . GLU A 640 ? 1.3437 1.2214 1.2075 -0.2651 -0.2041 0.0635 640 GLU A C 4949 O O . GLU A 640 ? 1.3424 1.2854 1.2329 -0.2944 -0.2104 0.0813 640 GLU A O 4950 C CB . GLU A 640 ? 1.3333 1.3968 1.1745 -0.3058 -0.2137 0.0855 640 GLU A CB 4951 C CG . GLU A 640 ? 1.5749 1.7023 1.3838 -0.3061 -0.2153 0.0850 640 GLU A CG 4952 C CD . GLU A 640 ? 1.6456 1.9288 1.4712 -0.3537 -0.2254 0.1207 640 GLU A CD 4953 O OE1 . GLU A 640 ? 1.6674 1.9977 1.4818 -0.3791 -0.2343 0.1317 640 GLU A OE1 4954 O OE2 . GLU A 640 ? 1.7004 2.0610 1.5519 -0.3662 -0.2273 0.1413 640 GLU A OE2 4955 N N . ALA A 641 ? 1.3320 1.0995 1.1956 -0.2347 -0.1995 0.0502 641 ALA A N 4956 C CA . ALA A 641 ? 1.3663 1.0916 1.2587 -0.2328 -0.1965 0.0539 641 ALA A CA 4957 C C . ALA A 641 ? 1.4140 1.2158 1.2984 -0.1956 -0.1805 0.0464 641 ALA A C 4958 O O . ALA A 641 ? 1.5085 1.3408 1.3623 -0.1475 -0.1688 0.0288 641 ALA A O 4959 C CB . ALA A 641 ? 1.3809 0.9850 1.2766 -0.2092 -0.1963 0.0489 641 ALA A CB 4960 N N . GLU A 642 ? 1.3424 1.1712 1.2546 -0.2165 -0.1843 0.0581 642 GLU A N 4961 C CA . GLU A 642 ? 1.3374 1.2307 1.2455 -0.1864 -0.1711 0.0542 642 GLU A CA 4962 C C . GLU A 642 ? 1.3494 1.1995 1.2840 -0.1865 -0.1735 0.0571 642 GLU A C 4963 O O . GLU A 642 ? 1.3516 1.1738 1.3139 -0.2245 -0.1938 0.0682 642 GLU A O 4964 C CB . GLU A 642 ? 1.3405 1.3542 1.2503 -0.2104 -0.1776 0.0709 642 GLU A CB 4965 C CG . GLU A 642 ? 1.4190 1.5091 1.2965 -0.1955 -0.1690 0.0659 642 GLU A CG 4966 C CD . GLU A 642 ? 1.5838 1.8067 1.4700 -0.2260 -0.1779 0.0933 642 GLU A CD 4967 O OE1 . GLU A 642 ? 1.7155 1.9539 1.6379 -0.2703 -0.2007 0.1198 642 GLU A OE1 4968 O OE2 . GLU A 642 ? 1.6045 1.9202 1.4626 -0.2037 -0.1662 0.0900 642 GLU A OE2 4969 N N . LEU A 643 ? 1.3857 1.2326 1.3116 -0.1420 -0.1559 0.0456 643 LEU A N 4970 C CA . LEU A 643 ? 1.3672 1.1921 1.3131 -0.1354 -0.1558 0.0477 643 LEU A CA 4971 C C . LEU A 643 ? 1.3841 1.2875 1.3362 -0.1447 -0.1623 0.0561 643 LEU A C 4972 O O . LEU A 643 ? 1.4567 1.4257 1.3918 -0.1246 -0.1498 0.0534 643 LEU A O 4973 C CB . LEU A 643 ? 1.3622 1.1508 1.2999 -0.0877 -0.1374 0.0365 643 LEU A CB 4974 C CG . LEU A 643 ? 1.4090 1.1827 1.3643 -0.0758 -0.1344 0.0390 643 LEU A CG 4975 C CD1 . LEU A 643 ? 1.4044 1.1213 1.3827 -0.0982 -0.1478 0.0467 643 LEU A CD1 4976 C CD2 . LEU A 643 ? 1.4862 1.2443 1.4355 -0.0322 -0.1184 0.0329 643 LEU A CD2 4977 N N . ILE A 644 ? 1.3515 1.2469 1.3292 -0.1735 -0.1867 0.0667 644 ILE A N 4978 C CA . ILE A 644 ? 1.2773 1.2374 1.2660 -0.1857 -0.2044 0.0804 644 ILE A CA 4979 C C . ILE A 644 ? 1.3345 1.2704 1.3291 -0.1577 -0.2037 0.0728 644 ILE A C 4980 O O . ILE A 644 ? 1.3556 1.2392 1.3659 -0.1609 -0.2202 0.0676 644 ILE A O 4981 C CB . ILE A 644 ? 1.2401 1.2172 1.2567 -0.2409 -0.2480 0.1010 644 ILE A CB 4982 C CG1 . ILE A 644 ? 1.2900 1.2979 1.3009 -0.2714 -0.2485 0.1109 644 ILE A CG1 4983 C CG2 . ILE A 644 ? 1.2376 1.2808 1.2698 -0.2536 -0.2756 0.1225 644 ILE A CG2 4984 C CD1 . ILE A 644 ? 1.3382 1.4306 1.3217 -0.2501 -0.2223 0.1137 644 ILE A CD1 4985 N N . VAL A 645 ? 1.4014 1.3786 1.3823 -0.1282 -0.1852 0.0708 645 VAL A N 4986 C CA . VAL A 645 ? 1.3728 1.3331 1.3563 -0.1005 -0.1835 0.0645 645 VAL A CA 4987 C C . VAL A 645 ? 1.4236 1.4290 1.4200 -0.1169 -0.2142 0.0826 645 VAL A C 4988 O O . VAL A 645 ? 1.5847 1.6529 1.5746 -0.1156 -0.2076 0.0949 645 VAL A O 4989 C CB . VAL A 645 ? 1.3672 1.3334 1.3307 -0.0574 -0.1472 0.0511 645 VAL A CB 4990 C CG1 . VAL A 645 ? 1.4489 1.4020 1.4151 -0.0315 -0.1458 0.0466 645 VAL A CG1 4991 C CG2 . VAL A 645 ? 1.3831 1.3020 1.3385 -0.0409 -0.1276 0.0388 645 VAL A CG2 4992 N N . SER A 646 ? 1.3717 1.3453 1.3877 -0.1296 -0.2522 0.0849 646 SER A N 4993 C CA . SER A 646 ? 1.3974 1.4020 1.4295 -0.1439 -0.2942 0.1048 646 SER A CA 4994 C C . SER A 646 ? 1.5738 1.5584 1.5955 -0.1019 -0.2862 0.0929 646 SER A C 4995 O O . SER A 646 ? 1.7242 1.6578 1.7446 -0.0779 -0.2900 0.0729 646 SER A O 4996 C CB . SER A 646 ? 1.4482 1.4283 1.5096 -0.1803 -0.3540 0.1129 646 SER A CB 4997 O OG . SER A 646 ? 1.4606 1.3726 1.5227 -0.1589 -0.3591 0.0860 646 SER A OG 4998 N N . ILE A 647 ? 1.5986 1.6290 1.6127 -0.0922 -0.2748 0.1060 647 ILE A N 4999 C CA . ILE A 647 ? 1.6701 1.6844 1.6710 -0.0524 -0.2583 0.0949 647 ILE A CA 5000 C C . ILE A 647 ? 1.8043 1.8105 1.8184 -0.0533 -0.3091 0.1094 647 ILE A C 5001 O O . ILE A 647 ? 1.7318 1.7498 1.7692 -0.0875 -0.3616 0.1316 647 ILE A O 5002 C CB . ILE A 647 ? 1.4865 1.5483 1.4715 -0.0383 -0.2173 0.0978 647 ILE A CB 5003 C CG1 . ILE A 647 ? 1.6388 1.7744 1.6352 -0.0690 -0.2374 0.1315 647 ILE A CG1 5004 C CG2 . ILE A 647 ? 1.4299 1.4870 1.4002 -0.0272 -0.1758 0.0784 647 ILE A CG2 5005 C CD1 . ILE A 647 ? 1.7912 1.9877 1.7717 -0.0559 -0.1979 0.1316 647 ILE A CD1 5006 N N . PRO A 648 ? 1.8036 1.7873 1.8048 -0.0164 -0.2995 0.0984 648 PRO A N 5007 C CA . PRO A 648 ? 1.7819 1.7578 1.7930 -0.0144 -0.3498 0.1156 648 PRO A CA 5008 C C . PRO A 648 ? 1.7219 1.7502 1.7350 -0.0241 -0.3427 0.1456 648 PRO A C 5009 O O . PRO A 648 ? 1.6364 1.7130 1.6421 -0.0306 -0.2995 0.1490 648 PRO A O 5010 C CB . PRO A 648 ? 1.7556 1.6813 1.7484 0.0334 -0.3400 0.0868 648 PRO A CB 5011 C CG . PRO A 648 ? 1.7711 1.7051 1.7458 0.0528 -0.2724 0.0687 648 PRO A CG 5012 C CD . PRO A 648 ? 1.7311 1.6848 1.7122 0.0245 -0.2549 0.0702 648 PRO A CD 5013 N N . LEU A 649 ? 1.6374 1.6559 1.6605 -0.0220 -0.3883 0.1669 649 LEU A N 5014 C CA . LEU A 649 ? 1.6504 1.7182 1.6793 -0.0314 -0.3871 0.2016 649 LEU A CA 5015 C C . LEU A 649 ? 1.7037 1.7692 1.7073 0.0032 -0.3261 0.1807 649 LEU A C 5016 O O . LEU A 649 ? 1.6152 1.7311 1.6195 -0.0016 -0.3062 0.2008 649 LEU A O 5017 C CB . LEU A 649 ? 1.5072 1.5520 1.5560 -0.0371 -0.4607 0.2333 649 LEU A CB 5018 C CG . LEU A 649 ? 1.4905 1.5525 1.5762 -0.0807 -0.5394 0.2711 649 LEU A CG 5019 C CD1 . LEU A 649 ? 1.5059 1.5141 1.5955 -0.0800 -0.5719 0.2399 649 LEU A CD1 5020 C CD2 . LEU A 649 ? 1.5220 1.5702 1.6294 -0.0850 -0.6111 0.3127 649 LEU A CD2 5021 N N . GLN A 650 ? 1.7683 1.7809 1.7525 0.0374 -0.2993 0.1420 650 GLN A N 5022 C CA . GLN A 650 ? 1.7766 1.7780 1.7416 0.0690 -0.2524 0.1228 650 GLN A CA 5023 C C . GLN A 650 ? 1.9151 1.9416 1.8700 0.0734 -0.1963 0.1016 650 GLN A C 5024 O O . GLN A 650 ? 1.9907 2.0087 1.9341 0.0968 -0.1609 0.0843 650 GLN A O 5025 C CB . GLN A 650 ? 1.6527 1.5921 1.6046 0.1049 -0.2601 0.0984 650 GLN A CB 5026 C CG . GLN A 650 ? 1.6923 1.5941 1.6519 0.1077 -0.3278 0.1086 650 GLN A CG 5027 C CD . GLN A 650 ? 1.7769 1.6625 1.7447 0.1002 -0.3592 0.0963 650 GLN A CD 5028 O OE1 . GLN A 650 ? 1.8470 1.7205 1.8043 0.1178 -0.3303 0.0681 650 GLN A OE1 5029 N NE2 . GLN A 650 ? 1.8090 1.6960 1.7993 0.0720 -0.4226 0.1207 650 GLN A NE2 5030 N N . ALA A 651 ? 1.7951 1.8489 1.7559 0.0505 -0.1947 0.1038 651 ALA A N 5031 C CA . ALA A 651 ? 1.7700 1.8322 1.7212 0.0571 -0.1535 0.0819 651 ALA A CA 5032 C C . ALA A 651 ? 1.7255 1.8227 1.6672 0.0714 -0.1176 0.0741 651 ALA A C 5033 O O . ALA A 651 ? 1.7428 1.8140 1.6770 0.0962 -0.0927 0.0529 651 ALA A O 5034 C CB . ALA A 651 ? 1.9607 2.0483 1.9193 0.0276 -0.1642 0.0901 651 ALA A CB 5035 N N . ASP A 652 ? 1.7225 1.8845 1.6669 0.0558 -0.1185 0.0922 652 ASP A N 5036 C CA . ASP A 652 ? 1.9242 2.1307 1.8590 0.0721 -0.0883 0.0808 652 ASP A CA 5037 C C . ASP A 652 ? 1.8744 2.0643 1.7979 0.0895 -0.0642 0.0487 652 ASP A C 5038 O O . ASP A 652 ? 1.9958 2.1532 1.9155 0.1134 -0.0480 0.0267 652 ASP A O 5039 C CB . ASP A 652 ? 2.0588 2.2474 1.9926 0.0915 -0.0800 0.0780 652 ASP A CB 5040 C CG . ASP A 652 ? 2.0361 2.2854 1.9657 0.1023 -0.0604 0.0751 652 ASP A CG 5041 O OD1 . ASP A 652 ? 2.0109 2.3347 1.9405 0.0906 -0.0617 0.0899 652 ASP A OD1 5042 O OD2 . ASP A 652 ? 1.9931 2.2208 1.9199 0.1230 -0.0451 0.0580 652 ASP A OD2 5043 N N . PHE A 653 ? 1.7606 1.9716 1.6815 0.0755 -0.0674 0.0491 653 PHE A N 5044 C CA . PHE A 653 ? 1.7548 1.9418 1.6663 0.0901 -0.0539 0.0233 653 PHE A CA 5045 C C . PHE A 653 ? 1.7237 1.9506 1.6219 0.1167 -0.0380 0.0013 653 PHE A C 5046 O O . PHE A 653 ? 1.7445 2.0456 1.6371 0.1167 -0.0352 0.0086 653 PHE A O 5047 C CB . PHE A 653 ? 1.8651 2.0569 1.7774 0.0652 -0.0659 0.0320 653 PHE A CB 5048 C CG . PHE A 653 ? 1.7643 1.9532 1.6630 0.0794 -0.0562 0.0105 653 PHE A CG 5049 C CD1 . PHE A 653 ? 1.7217 1.8417 1.6216 0.0937 -0.0535 -0.0055 653 PHE A CD1 5050 C CD2 . PHE A 653 ? 1.7939 2.0528 1.6793 0.0802 -0.0536 0.0091 653 PHE A CD2 5051 C CE1 . PHE A 653 ? 1.7138 1.8219 1.6026 0.1082 -0.0535 -0.0226 653 PHE A CE1 5052 C CE2 . PHE A 653 ? 1.7624 2.0130 1.6317 0.0990 -0.0506 -0.0139 653 PHE A CE2 5053 C CZ . PHE A 653 ? 1.7060 1.8746 1.5775 0.1126 -0.0531 -0.0297 653 PHE A CZ 5054 N N . ILE A 654 ? 1.6832 1.8653 1.5785 0.1408 -0.0325 -0.0242 654 ILE A N 5055 C CA . ILE A 654 ? 1.7493 1.9584 1.6330 0.1709 -0.0285 -0.0517 654 ILE A CA 5056 C C . ILE A 654 ? 1.8100 1.9719 1.6902 0.1866 -0.0384 -0.0715 654 ILE A C 5057 O O . ILE A 654 ? 1.8477 1.9453 1.7410 0.1821 -0.0436 -0.0661 654 ILE A O 5058 C CB . ILE A 654 ? 1.9845 2.1882 1.8747 0.1909 -0.0233 -0.0642 654 ILE A CB 5059 C CG1 . ILE A 654 ? 1.8266 1.9568 1.7328 0.1917 -0.0263 -0.0635 654 ILE A CG1 5060 C CG2 . ILE A 654 ? 2.0331 2.2842 1.9258 0.1792 -0.0162 -0.0438 654 ILE A CG2 5061 C CD1 . ILE A 654 ? 1.6793 1.7790 1.5917 0.2166 -0.0379 -0.0878 654 ILE A CD1 5062 N N . GLY A 655 ? 1.8583 2.0566 1.7207 0.2068 -0.0437 -0.0920 655 GLY A N 5063 C CA . GLY A 655 ? 1.7997 1.9527 1.6571 0.2307 -0.0621 -0.1148 655 GLY A CA 5064 C C . GLY A 655 ? 1.8110 1.8918 1.6788 0.2131 -0.0713 -0.0997 655 GLY A C 5065 O O . GLY A 655 ? 1.7539 1.8340 1.6229 0.1828 -0.0643 -0.0783 655 GLY A O 5066 N N . VAL A 656 ? 1.9222 1.9432 1.8014 0.2313 -0.0916 -0.1084 656 VAL A N 5067 C CA . VAL A 656 ? 1.8498 1.8013 1.7426 0.2200 -0.1050 -0.0914 656 VAL A CA 5068 C C . VAL A 656 ? 1.8840 1.7877 1.7963 0.2429 -0.1335 -0.0964 656 VAL A C 5069 O O . VAL A 656 ? 1.9972 1.9197 1.9097 0.2675 -0.1455 -0.1188 656 VAL A O 5070 C CB . VAL A 656 ? 1.9006 1.8403 1.7752 0.2181 -0.1150 -0.0954 656 VAL A CB 5071 C CG1 . VAL A 656 ? 1.9526 1.9028 1.8265 0.1789 -0.0967 -0.0726 656 VAL A CG1 5072 C CG2 . VAL A 656 ? 1.9540 1.9455 1.7997 0.2497 -0.1234 -0.1280 656 VAL A CG2 5073 N N . VAL A 657 ? 1.7446 1.5894 1.6770 0.2337 -0.1488 -0.0731 657 VAL A N 5074 C CA . VAL A 657 ? 1.8722 1.6773 1.8332 0.2480 -0.1814 -0.0646 657 VAL A CA 5075 C C . VAL A 657 ? 1.8372 1.6009 1.7948 0.2751 -0.2280 -0.0800 657 VAL A C 5076 O O . VAL A 657 ? 1.6531 1.3724 1.6095 0.2700 -0.2420 -0.0664 657 VAL A O 5077 C CB . VAL A 657 ? 1.7431 1.5173 1.7340 0.2252 -0.1773 -0.0226 657 VAL A CB 5078 C CG1 . VAL A 657 ? 1.8306 1.5742 1.8572 0.2357 -0.2169 -0.0038 657 VAL A CG1 5079 C CG2 . VAL A 657 ? 1.6597 1.4718 1.6518 0.2072 -0.1392 -0.0125 657 VAL A CG2 5080 N N . ARG A 658 ? 1.9255 1.7006 1.8819 0.3059 -0.2562 -0.1101 658 ARG A N 5081 C CA . ARG A 658 ? 1.9646 1.7004 1.9166 0.3411 -0.3117 -0.1327 658 ARG A CA 5082 C C . ARG A 658 ? 2.0360 1.7073 2.0316 0.3417 -0.3659 -0.1033 658 ARG A C 5083 O O . ARG A 658 ? 2.0097 1.6248 2.0080 0.3605 -0.4165 -0.1032 658 ARG A O 5084 C CB . ARG A 658 ? 1.9729 1.7537 1.9053 0.3787 -0.3253 -0.1825 658 ARG A CB 5085 C CG . ARG A 658 ? 2.0526 1.9161 1.9534 0.3740 -0.2710 -0.2006 658 ARG A CG 5086 C CD . ARG A 658 ? 2.2198 2.1067 2.0839 0.3747 -0.2530 -0.2076 658 ARG A CD 5087 N NE . ARG A 658 ? 2.2983 2.2750 2.1384 0.3678 -0.2083 -0.2166 658 ARG A NE 5088 C CZ . ARG A 658 ? 2.3533 2.3790 2.1627 0.3669 -0.1904 -0.2219 658 ARG A CZ 5089 N NH1 . ARG A 658 ? 2.2813 2.2680 2.0760 0.3740 -0.2105 -0.2242 658 ARG A NH1 5090 N NH2 . ARG A 658 ? 2.3954 2.5105 2.1907 0.3572 -0.1550 -0.2208 658 ARG A NH2 5091 N N . ASN A 659 ? 1.9865 1.6686 2.0175 0.3210 -0.3586 -0.0749 659 ASN A N 5092 C CA . ASN A 659 ? 1.8629 1.5079 1.9414 0.3235 -0.4172 -0.0493 659 ASN A CA 5093 C C . ASN A 659 ? 1.8792 1.4728 1.9908 0.3056 -0.4450 0.0059 659 ASN A C 5094 O O . ASN A 659 ? 2.0215 1.5833 2.1760 0.3083 -0.5062 0.0332 659 ASN A O 5095 C CB . ASN A 659 ? 1.6853 1.3719 1.7903 0.3066 -0.3988 -0.0371 659 ASN A CB 5096 C CG . ASN A 659 ? 1.8929 1.6160 1.9924 0.2755 -0.3319 -0.0105 659 ASN A CG 5097 O OD1 . ASN A 659 ? 1.9753 1.6828 2.0831 0.2574 -0.3195 0.0261 659 ASN A OD1 5098 N ND2 . ASN A 659 ? 1.8456 1.6153 1.9312 0.2717 -0.2925 -0.0298 659 ASN A ND2 5099 N N . ASN A 660 ? 1.7042 1.2910 1.8004 0.2861 -0.4054 0.0257 660 ASN A N 5100 C CA . ASN A 660 ? 1.7628 1.3048 1.8911 0.2687 -0.4278 0.0807 660 ASN A CA 5101 C C . ASN A 660 ? 1.8419 1.3191 1.9511 0.2811 -0.4568 0.0750 660 ASN A C 5102 O O . ASN A 660 ? 1.8576 1.3401 1.9217 0.2889 -0.4285 0.0371 660 ASN A O 5103 C CB . ASN A 660 ? 1.7251 1.3021 1.8587 0.2366 -0.3683 0.1142 660 ASN A CB 5104 C CG . ASN A 660 ? 1.7595 1.3903 1.9228 0.2249 -0.3533 0.1371 660 ASN A CG 5105 O OD1 . ASN A 660 ? 1.9026 1.5357 2.0976 0.2318 -0.3964 0.1466 660 ASN A OD1 5106 N ND2 . ASN A 660 ? 1.7563 1.4299 1.9102 0.2078 -0.2970 0.1456 660 ASN A ND2 5107 N N . GLU A 661 ? 2.0663 1.4839 2.2120 0.2823 -0.5172 0.1164 661 GLU A N 5108 C CA . GLU A 661 ? 1.9911 1.3545 2.1193 0.2808 -0.5327 0.1163 661 GLU A CA 5109 C C . GLU A 661 ? 1.8757 1.2298 2.0060 0.2497 -0.4886 0.1539 661 GLU A C 5110 O O . GLU A 661 ? 2.1041 1.4222 2.2074 0.2461 -0.4799 0.1431 661 GLU A O 5111 C CB . GLU A 661 ? 2.0242 1.3823 2.1783 0.2631 -0.5727 0.1300 661 GLU A CB 5112 C CG . GLU A 661 ? 2.1054 1.4581 2.2512 0.2921 -0.6240 0.0837 661 GLU A CG 5113 C CD . GLU A 661 ? 2.2473 1.5735 2.4057 0.2770 -0.6681 0.0863 661 GLU A CD 5114 O OE1 . GLU A 661 ? 2.1493 1.4521 2.3036 0.2585 -0.6590 0.1052 661 GLU A OE1 5115 O OE2 . GLU A 661 ? 2.2805 1.6076 2.4535 0.2824 -0.7130 0.0677 661 GLU A OE2 5116 N N . ALA A 662 ? 1.7722 1.1632 1.9348 0.2274 -0.4619 0.1966 662 ALA A N 5117 C CA . ALA A 662 ? 1.9218 1.3145 2.0899 0.1991 -0.4204 0.2310 662 ALA A CA 5118 C C . ALA A 662 ? 1.9202 1.3227 2.0397 0.1925 -0.3678 0.1879 662 ALA A C 5119 O O . ALA A 662 ? 1.7868 1.1519 1.8973 0.1767 -0.3563 0.1975 662 ALA A O 5120 C CB . ALA A 662 ? 1.8408 1.2968 2.0441 0.1828 -0.3946 0.2718 662 ALA A CB 5121 N N . LEU A 663 ? 1.9358 1.3933 2.0269 0.2011 -0.3374 0.1427 663 LEU A N 5122 C CA . LEU A 663 ? 1.7737 1.2539 1.8211 0.1941 -0.2952 0.1028 663 LEU A CA 5123 C C . LEU A 663 ? 1.8766 1.3557 1.8897 0.2240 -0.3164 0.0546 663 LEU A C 5124 O O . LEU A 663 ? 1.6431 1.1544 1.6555 0.2458 -0.3279 0.0320 663 LEU A O 5125 C CB . LEU A 663 ? 1.8725 1.4238 1.9149 0.1796 -0.2442 0.0947 663 LEU A CB 5126 C CG . LEU A 663 ? 1.8419 1.4451 1.8891 0.1939 -0.2396 0.0799 663 LEU A CG 5127 C CD1 . LEU A 663 ? 1.8640 1.5069 1.8729 0.2047 -0.2205 0.0320 663 LEU A CD1 5128 C CD2 . LEU A 663 ? 1.6050 1.2507 1.6720 0.1788 -0.2085 0.1045 663 LEU A CD2 5129 N N . ALA A 664 ? 2.2070 1.6525 2.1915 0.2272 -0.3231 0.0378 664 ALA A N 5130 C CA . ALA A 664 ? 2.3084 1.7564 2.2591 0.2643 -0.3497 -0.0076 664 ALA A CA 5131 C C . ALA A 664 ? 2.1439 1.6667 2.0546 0.2610 -0.3047 -0.0443 664 ALA A C 5132 O O . ALA A 664 ? 1.9790 1.5038 1.8705 0.2398 -0.2825 -0.0442 664 ALA A O 5133 C CB . ALA A 664 ? 2.2311 1.5973 2.1728 0.2788 -0.3953 -0.0043 664 ALA A CB 5134 N N . ARG A 665 ? 2.1592 1.7456 2.0624 0.2796 -0.2949 -0.0710 665 ARG A N 5135 C CA . ARG A 665 ? 2.0441 1.7150 1.9136 0.2838 -0.2603 -0.1034 665 ARG A CA 5136 C C . ARG A 665 ? 1.9428 1.6461 1.8054 0.2409 -0.2158 -0.0868 665 ARG A C 5137 O O . ARG A 665 ? 1.9862 1.6636 1.8738 0.2082 -0.2009 -0.0547 665 ARG A O 5138 C CB . ARG A 665 ? 2.0457 1.7301 1.8768 0.3265 -0.2869 -0.1450 665 ARG A CB 5139 C CG . ARG A 665 ? 2.1700 1.7938 1.9844 0.3288 -0.3101 -0.1421 665 ARG A CG 5140 C CD . ARG A 665 ? 2.4701 2.1264 2.2394 0.3761 -0.3315 -0.1881 665 ARG A CD 5141 N NE . ARG A 665 ? 2.4983 2.2482 2.2372 0.3607 -0.2872 -0.1978 665 ARG A NE 5142 C CZ . ARG A 665 ? 2.3494 2.0939 2.0706 0.3383 -0.2768 -0.1883 665 ARG A CZ 5143 N NH1 . ARG A 665 ? 2.1378 1.7807 1.8661 0.3307 -0.3047 -0.1716 665 ARG A NH1 5144 N NH2 . ARG A 665 ? 2.2958 2.1382 1.9955 0.3211 -0.2415 -0.1915 665 ARG A NH2 5145 N N . LEU A 666 ? 1.9252 1.6909 1.7551 0.2436 -0.1999 -0.1086 666 LEU A N 5146 C CA . LEU A 666 ? 1.8846 1.6778 1.7046 0.2054 -0.1748 -0.0954 666 LEU A CA 5147 C C . LEU A 666 ? 1.8197 1.7126 1.6076 0.2190 -0.1614 -0.1194 666 LEU A C 5148 O O . LEU A 666 ? 1.8344 1.7720 1.6091 0.2580 -0.1671 -0.1464 666 LEU A O 5149 C CB . LEU A 666 ? 1.7360 1.5359 1.5825 0.1616 -0.1479 -0.0660 666 LEU A CB 5150 C CG . LEU A 666 ? 1.5227 1.2500 1.3886 0.1288 -0.1520 -0.0385 666 LEU A CG 5151 C CD1 . LEU A 666 ? 1.4951 1.2497 1.3755 0.0866 -0.1299 -0.0201 666 LEU A CD1 5152 C CD2 . LEU A 666 ? 1.4868 1.1760 1.3339 0.1280 -0.1696 -0.0435 666 LEU A CD2 5153 N N . SER A 667 ? 1.7421 1.6762 1.5204 0.1863 -0.1459 -0.1074 667 SER A N 5154 C CA . SER A 667 ? 1.7186 1.7693 1.4752 0.1891 -0.1292 -0.1161 667 SER A CA 5155 C C . SER A 667 ? 1.7306 1.8288 1.5101 0.1403 -0.1070 -0.0847 667 SER A C 5156 O O . SER A 667 ? 1.9004 1.9816 1.6928 0.0957 -0.1067 -0.0608 667 SER A O 5157 C CB . SER A 667 ? 1.8083 1.8885 1.5349 0.1929 -0.1370 -0.1249 667 SER A CB 5158 O OG . SER A 667 ? 1.9047 2.1160 1.6108 0.2011 -0.1218 -0.1303 667 SER A OG 5159 N N . CYS A 668 ? 1.7511 1.9044 1.5371 0.1492 -0.0939 -0.0852 668 CYS A N 5160 C CA . CYS A 668 ? 1.7123 1.8985 1.5218 0.1083 -0.0815 -0.0552 668 CYS A CA 5161 C C . CYS A 668 ? 1.7284 2.0293 1.5309 0.1144 -0.0696 -0.0509 668 CYS A C 5162 O O . CYS A 668 ? 1.8645 2.2010 1.6521 0.1562 -0.0650 -0.0753 668 CYS A O 5163 C CB . CYS A 668 ? 1.6186 1.7324 1.4528 0.1062 -0.0800 -0.0494 668 CYS A CB 5164 S SG . CYS A 668 ? 1.8168 1.8138 1.6690 0.0886 -0.0919 -0.0391 668 CYS A SG 5165 N N . ALA A 669 ? 1.5739 1.9327 1.3907 0.0715 -0.0694 -0.0174 669 ALA A N 5166 C CA . ALA A 669 ? 1.5248 1.9981 1.3420 0.0698 -0.0619 -0.0004 669 ALA A CA 5167 C C . ALA A 669 ? 1.5797 2.0588 1.4291 0.0237 -0.0718 0.0395 669 ALA A C 5168 O O . ALA A 669 ? 1.4898 1.9335 1.3571 -0.0174 -0.0888 0.0598 669 ALA A O 5169 C CB . ALA A 669 ? 1.4692 2.0504 1.2666 0.0701 -0.0613 0.0050 669 ALA A CB 5170 N N . PHE A 670 ? 1.7343 2.2530 1.5917 0.0324 -0.0661 0.0492 670 PHE A N 5171 C CA . PHE A 670 ? 1.7284 2.2529 1.6151 -0.0049 -0.0832 0.0875 670 PHE A CA 5172 C C . PHE A 670 ? 1.5993 2.2372 1.4986 -0.0413 -0.0994 0.1311 670 PHE A C 5173 O O . PHE A 670 ? 1.6727 2.4179 1.5582 -0.0247 -0.0867 0.1358 670 PHE A O 5174 C CB . PHE A 670 ? 1.7970 2.3167 1.6875 0.0182 -0.0738 0.0844 670 PHE A CB 5175 C CG . PHE A 670 ? 1.7606 2.2628 1.6789 -0.0124 -0.0973 0.1191 670 PHE A CG 5176 C CD1 . PHE A 670 ? 1.6410 2.2318 1.5776 -0.0408 -0.1172 0.1647 670 PHE A CD1 5177 C CD2 . PHE A 670 ? 1.8001 2.2013 1.7268 -0.0100 -0.1041 0.1079 670 PHE A CD2 5178 C CE1 . PHE A 670 ? 1.6493 2.2150 1.6125 -0.0662 -0.1496 0.1971 670 PHE A CE1 5179 C CE2 . PHE A 670 ? 1.8526 2.2337 1.8009 -0.0306 -0.1320 0.1347 670 PHE A CE2 5180 C CZ . PHE A 670 ? 1.7962 2.2530 1.7630 -0.0586 -0.1579 0.1785 670 PHE A CZ 5181 N N . LYS A 671 ? 1.4612 2.0819 1.3888 -0.0902 -0.1314 0.1643 671 LYS A N 5182 C CA . LYS A 671 ? 1.5496 2.2795 1.4991 -0.1330 -0.1573 0.2158 671 LYS A CA 5183 C C . LYS A 671 ? 1.5520 2.2474 1.5418 -0.1790 -0.2047 0.2542 671 LYS A C 5184 O O . LYS A 671 ? 1.4019 1.9898 1.4000 -0.1874 -0.2202 0.2372 671 LYS A O 5185 C CB . LYS A 671 ? 1.6105 2.3833 1.5503 -0.1512 -0.1578 0.2165 671 LYS A CB 5186 C CG . LYS A 671 ? 1.6748 2.5974 1.6317 -0.1872 -0.1763 0.2701 671 LYS A CG 5187 C CD . LYS A 671 ? 1.6164 2.6632 1.5525 -0.1477 -0.1472 0.2724 671 LYS A CD 5188 C CE . LYS A 671 ? 1.4984 2.7148 1.4516 -0.1815 -0.1632 0.3310 671 LYS A CE 5189 N NZ . LYS A 671 ? 1.3729 2.6249 1.3777 -0.2354 -0.2095 0.3989 671 LYS A NZ 5190 N N . THR A 672 ? 1.6996 2.4900 1.7155 -0.2061 -0.2320 0.3072 672 THR A N 5191 C CA . THR A 672 ? 1.6982 2.4713 1.7574 -0.2543 -0.2926 0.3517 672 THR A CA 5192 C C . THR A 672 ? 1.6959 2.6042 1.7854 -0.3037 -0.3269 0.4157 672 THR A C 5193 O O . THR A 672 ? 1.7856 2.8113 1.8780 -0.2989 -0.3183 0.4509 672 THR A O 5194 C CB . THR A 672 ? 1.6431 2.3769 1.7141 -0.2389 -0.3088 0.3626 672 THR A CB 5195 O OG1 . THR A 672 ? 1.6412 2.4023 1.7578 -0.2864 -0.3775 0.4216 672 THR A OG1 5196 C CG2 . THR A 672 ? 1.6119 2.4205 1.6638 -0.2024 -0.2685 0.3639 672 THR A CG2 5197 N N . GLU A 673 ? 1.6196 2.5172 1.7343 -0.3526 -0.3674 0.4335 673 GLU A N 5198 C CA . GLU A 673 ? 1.7103 2.7414 1.8579 -0.4059 -0.4037 0.4978 673 GLU A CA 5199 C C . GLU A 673 ? 1.7356 2.7085 1.9306 -0.4521 -0.4645 0.5376 673 GLU A C 5200 O O . GLU A 673 ? 1.5987 2.5989 1.8130 -0.4591 -0.4728 0.5796 673 GLU A O 5201 C CB . GLU A 673 ? 1.6541 2.7097 1.7850 -0.4204 -0.3845 0.4802 673 GLU A CB 5202 C CG . GLU A 673 ? 1.6603 2.7600 1.7364 -0.3639 -0.3133 0.4369 673 GLU A CG 5203 C CD . GLU A 673 ? 1.8104 2.9374 1.8687 -0.3769 -0.3006 0.4235 673 GLU A CD 5204 O OE1 . GLU A 673 ? 1.8890 2.9705 1.9751 -0.4284 -0.3398 0.4372 673 GLU A OE1 5205 O OE2 . GLU A 673 ? 1.8556 3.0474 1.8720 -0.3340 -0.2547 0.3974 673 GLU A OE2 5206 N N . ASN A 674 ? 1.7966 2.6520 1.9995 -0.4708 -0.4879 0.5121 674 ASN A N 5207 C CA . ASN A 674 ? 1.6933 2.4493 1.9219 -0.4923 -0.5249 0.5296 674 ASN A CA 5208 C C . ASN A 674 ? 1.5838 2.2166 1.8153 -0.4653 -0.5511 0.4952 674 ASN A C 5209 O O . ASN A 674 ? 1.3625 1.9126 1.5850 -0.4548 -0.5559 0.4501 674 ASN A O 5210 C CB . ASN A 674 ? 1.5879 2.2946 1.8189 -0.5238 -0.5337 0.5265 674 ASN A CB 5211 C CG . ASN A 674 ? 1.6198 2.4457 1.8451 -0.5510 -0.5105 0.5617 674 ASN A CG 5212 O OD1 . ASN A 674 ? 1.7308 2.6719 1.9602 -0.5549 -0.4968 0.6042 674 ASN A OD1 5213 N ND2 . ASN A 674 ? 1.5326 2.3329 1.7472 -0.5680 -0.5048 0.5443 674 ASN A ND2 5214 N N . GLN A 675 ? 1.6558 2.2792 1.8990 -0.4530 -0.5669 0.5171 675 GLN A N 5215 C CA . GLN A 675 ? 1.7165 2.2201 1.9654 -0.4306 -0.5997 0.4927 675 GLN A CA 5216 C C . GLN A 675 ? 1.6376 2.0873 1.8648 -0.3919 -0.5953 0.4413 675 GLN A C 5217 O O . GLN A 675 ? 1.6190 1.9818 1.8458 -0.3656 -0.6194 0.4197 675 GLN A O 5218 C CB . GLN A 675 ? 1.7891 2.2004 2.0513 -0.4498 -0.6299 0.4873 675 GLN A CB 5219 C CG . GLN A 675 ? 1.8421 2.2952 2.1234 -0.4891 -0.6396 0.5427 675 GLN A CG 5220 C CD . GLN A 675 ? 1.9034 2.2734 2.1910 -0.5060 -0.6649 0.5379 675 GLN A CD 5221 O OE1 . GLN A 675 ? 2.0301 2.2990 2.3221 -0.4878 -0.6945 0.5131 675 GLN A OE1 5222 N NE2 . GLN A 675 ? 1.6721 2.0881 1.9575 -0.5376 -0.6529 0.5614 675 GLN A NE2 5223 N N . THR A 676 ? 1.5807 2.0823 1.7876 -0.3870 -0.5658 0.4225 676 THR A N 5224 C CA . THR A 676 ? 1.5866 2.0007 1.7597 -0.3407 -0.5302 0.3626 676 THR A CA 5225 C C . THR A 676 ? 1.6841 2.1259 1.8126 -0.2967 -0.4437 0.3335 676 THR A C 5226 O O . THR A 676 ? 1.6915 2.2086 1.8087 -0.3057 -0.4101 0.3398 676 THR A O 5227 C CB . THR A 676 ? 1.4786 1.8192 1.6516 -0.3528 -0.5349 0.3268 676 THR A CB 5228 O OG1 . THR A 676 ? 1.3320 1.7368 1.5049 -0.3852 -0.5147 0.3389 676 THR A OG1 5229 C CG2 . THR A 676 ? 1.6100 1.8813 1.8147 -0.3729 -0.6014 0.3311 676 THR A CG2 5230 N N . ARG A 677 ? 1.7451 2.1258 1.8492 -0.2478 -0.4129 0.3003 677 ARG A N 5231 C CA . ARG A 677 ? 1.7490 2.1297 1.8136 -0.2032 -0.3393 0.2633 677 ARG A CA 5232 C C . ARG A 677 ? 1.7556 2.0617 1.8016 -0.1886 -0.3109 0.2178 677 ARG A C 5233 O O . ARG A 677 ? 1.7703 2.0018 1.8272 -0.1936 -0.3389 0.2040 677 ARG A O 5234 C CB . ARG A 677 ? 1.7415 2.0876 1.7927 -0.1620 -0.3230 0.2505 677 ARG A CB 5235 C CG . ARG A 677 ? 1.7882 2.2112 1.8508 -0.1670 -0.3342 0.2927 677 ARG A CG 5236 C CD . ARG A 677 ? 1.6802 2.0447 1.7359 -0.1337 -0.3348 0.2828 677 ARG A CD 5237 N NE . ARG A 677 ? 1.6276 1.9340 1.6512 -0.0892 -0.2801 0.2305 677 ARG A NE 5238 C CZ . ARG A 677 ? 1.6107 1.9450 1.6144 -0.0610 -0.2328 0.2157 677 ARG A CZ 5239 N NH1 . ARG A 677 ? 1.5609 1.9836 1.5700 -0.0684 -0.2280 0.2462 677 ARG A NH1 5240 N NH2 . ARG A 677 ? 1.6413 1.9201 1.6229 -0.0258 -0.1941 0.1725 677 ARG A NH2 5241 N N . GLN A 678 ? 1.7085 2.0345 1.7273 -0.1674 -0.2595 0.1948 678 GLN A N 5242 C CA . GLN A 678 ? 1.4863 1.7433 1.4894 -0.1540 -0.2349 0.1585 678 GLN A CA 5243 C C . GLN A 678 ? 1.4057 1.6873 1.3786 -0.1242 -0.1871 0.1355 678 GLN A C 5244 O O . GLN A 678 ? 1.4684 1.8350 1.4318 -0.1184 -0.1736 0.1465 678 GLN A O 5245 C CB . GLN A 678 ? 1.4854 1.7280 1.5083 -0.1985 -0.2679 0.1694 678 GLN A CB 5246 C CG . GLN A 678 ? 1.4866 1.8263 1.5208 -0.2385 -0.2841 0.2046 678 GLN A CG 5247 C CD . GLN A 678 ? 1.5372 1.8584 1.5990 -0.2899 -0.3276 0.2196 678 GLN A CD 5248 O OE1 . GLN A 678 ? 1.3405 1.5723 1.4113 -0.2925 -0.3442 0.1996 678 GLN A OE1 5249 N NE2 . GLN A 678 ? 1.6031 2.0148 1.6801 -0.3313 -0.3476 0.2560 678 GLN A NE2 5250 N N . VAL A 679 ? 1.4024 1.6111 1.3619 -0.1033 -0.1663 0.1046 679 VAL A N 5251 C CA . VAL A 679 ? 1.4415 1.6542 1.3745 -0.0716 -0.1328 0.0800 679 VAL A CA 5252 C C . VAL A 679 ? 1.4515 1.6281 1.3800 -0.0862 -0.1350 0.0723 679 VAL A C 5253 O O . VAL A 679 ? 1.4009 1.5027 1.3416 -0.0982 -0.1453 0.0687 679 VAL A O 5254 C CB . VAL A 679 ? 1.4120 1.5672 1.3352 -0.0290 -0.1105 0.0541 679 VAL A CB 5255 C CG1 . VAL A 679 ? 1.4253 1.5776 1.3257 0.0034 -0.0898 0.0293 679 VAL A CG1 5256 C CG2 . VAL A 679 ? 1.5091 1.6938 1.4350 -0.0143 -0.1072 0.0601 679 VAL A CG2 5257 N N . VAL A 680 ? 1.4554 1.6869 1.3653 -0.0825 -0.1258 0.0692 680 VAL A N 5258 C CA . VAL A 680 ? 1.3791 1.5791 1.2818 -0.0964 -0.1298 0.0634 680 VAL A CA 5259 C C . VAL A 680 ? 1.3873 1.5441 1.2630 -0.0512 -0.1114 0.0319 680 VAL A C 5260 O O . VAL A 680 ? 1.4576 1.6643 1.3116 -0.0141 -0.0980 0.0158 680 VAL A O 5261 C CB . VAL A 680 ? 1.3275 1.6228 1.2285 -0.1275 -0.1406 0.0853 680 VAL A CB 5262 C CG1 . VAL A 680 ? 1.3589 1.6146 1.2509 -0.1425 -0.1454 0.0782 680 VAL A CG1 5263 C CG2 . VAL A 680 ? 1.2642 1.6028 1.1995 -0.1769 -0.1712 0.1234 680 VAL A CG2 5264 N N . CYS A 681 ? 1.4421 1.5054 1.3215 -0.0537 -0.1161 0.0243 681 CYS A N 5265 C CA . CYS A 681 ? 1.6173 1.6270 1.4770 -0.0142 -0.1108 0.0008 681 CYS A CA 5266 C C . CYS A 681 ? 1.5998 1.5690 1.4508 -0.0298 -0.1220 0.0006 681 CYS A C 5267 O O . CYS A 681 ? 1.6308 1.5501 1.5016 -0.0680 -0.1323 0.0158 681 CYS A O 5268 C CB . CYS A 681 ? 1.6273 1.5564 1.5023 0.0041 -0.1086 -0.0025 681 CYS A CB 5269 S SG . CYS A 681 ? 1.9547 1.9207 1.8360 0.0288 -0.0954 -0.0062 681 CYS A SG 5270 N N . ASP A 682 ? 1.6110 1.5992 1.4317 0.0023 -0.1229 -0.0189 682 ASP A N 5271 C CA . ASP A 682 ? 1.6695 1.6184 1.4765 -0.0074 -0.1353 -0.0211 682 ASP A CA 5272 C C . ASP A 682 ? 1.6042 1.4282 1.4187 0.0059 -0.1476 -0.0242 682 ASP A C 5273 O O . ASP A 682 ? 1.6102 1.3992 1.4170 0.0505 -0.1537 -0.0399 682 ASP A O 5274 C CB . ASP A 682 ? 1.8607 1.8810 1.6283 0.0294 -0.1359 -0.0433 682 ASP A CB 5275 C CG . ASP A 682 ? 2.1423 2.1266 1.8915 0.0206 -0.1500 -0.0461 682 ASP A CG 5276 O OD1 . ASP A 682 ? 2.1638 2.1066 1.9342 -0.0314 -0.1557 -0.0234 682 ASP A OD1 5277 O OD2 . ASP A 682 ? 2.1953 2.1907 1.9085 0.0674 -0.1587 -0.0730 682 ASP A OD2 5278 N N . LEU A 683 ? 1.5029 1.2622 1.3361 -0.0349 -0.1556 -0.0061 683 LEU A N 5279 C CA . LEU A 683 ? 1.4904 1.1347 1.3362 -0.0294 -0.1683 0.0003 683 LEU A CA 5280 C C . LEU A 683 ? 1.4651 1.0583 1.2868 -0.0183 -0.1866 -0.0079 683 LEU A C 5281 O O . LEU A 683 ? 1.3689 0.8614 1.2009 -0.0183 -0.2025 0.0028 683 LEU A O 5282 C CB . LEU A 683 ? 1.4755 1.0750 1.3566 -0.0759 -0.1680 0.0235 683 LEU A CB 5283 C CG . LEU A 683 ? 1.4048 1.0438 1.3079 -0.0808 -0.1558 0.0294 683 LEU A CG 5284 C CD1 . LEU A 683 ? 1.5102 1.0993 1.4454 -0.1159 -0.1615 0.0461 683 LEU A CD1 5285 C CD2 . LEU A 683 ? 1.4222 1.0563 1.3237 -0.0342 -0.1488 0.0226 683 LEU A CD2 5286 N N . GLY A 684 ? 1.4650 1.1321 1.2544 -0.0074 -0.1857 -0.0246 684 GLY A N 5287 C CA . GLY A 684 ? 1.5878 1.2191 1.3468 0.0093 -0.2042 -0.0372 684 GLY A CA 5288 C C . GLY A 684 ? 1.6550 1.3086 1.4131 -0.0426 -0.2033 -0.0237 684 GLY A C 5289 O O . GLY A 684 ? 1.7290 1.3726 1.5203 -0.0983 -0.1988 -0.0001 684 GLY A O 5290 N N . ASN A 685 ? 1.6421 1.3282 1.3621 -0.0223 -0.2119 -0.0404 685 ASN A N 5291 C CA . ASN A 685 ? 1.5351 1.2661 1.2504 -0.0694 -0.2120 -0.0276 685 ASN A CA 5292 C C . ASN A 685 ? 1.5596 1.2199 1.2427 -0.0514 -0.2332 -0.0402 685 ASN A C 5293 O O . ASN A 685 ? 1.6929 1.4132 1.3315 -0.0043 -0.2382 -0.0656 685 ASN A O 5294 C CB . ASN A 685 ? 1.6109 1.5092 1.3107 -0.0685 -0.1962 -0.0289 685 ASN A CB 5295 C CG . ASN A 685 ? 1.6145 1.5790 1.3182 -0.1257 -0.1994 -0.0063 685 ASN A CG 5296 O OD1 . ASN A 685 ? 1.7026 1.5907 1.4330 -0.1808 -0.2112 0.0134 685 ASN A OD1 5297 N ND2 . ASN A 685 ? 1.5348 1.6485 1.2145 -0.1140 -0.1908 -0.0070 685 ASN A ND2 5298 N N . PRO A 686 ? 1.5315 1.0646 1.2356 -0.0857 -0.2477 -0.0232 686 PRO A N 5299 C CA . PRO A 686 ? 1.4913 0.9532 1.2461 -0.1384 -0.2446 0.0045 686 PRO A CA 5300 C C . PRO A 686 ? 1.4758 0.8655 1.2506 -0.1067 -0.2456 0.0066 686 PRO A C 5301 O O . PRO A 686 ? 1.5611 0.9137 1.3144 -0.0490 -0.2595 -0.0094 686 PRO A O 5302 C CB . PRO A 686 ? 1.4981 0.8529 1.2580 -0.1752 -0.2632 0.0175 686 PRO A CB 5303 C CG . PRO A 686 ? 1.5920 0.9767 1.3021 -0.1471 -0.2741 -0.0022 686 PRO A CG 5304 C CD . PRO A 686 ? 1.5870 1.0397 1.2617 -0.0723 -0.2713 -0.0317 686 PRO A CD 5305 N N . MET A 687 ? 1.4757 0.8494 1.2926 -0.1438 -0.2357 0.0268 687 MET A N 5306 C CA . MET A 687 ? 1.3434 0.6439 1.1851 -0.1236 -0.2377 0.0375 687 MET A CA 5307 C C . MET A 687 ? 1.5106 0.6876 1.3732 -0.1497 -0.2544 0.0593 687 MET A C 5308 O O . MET A 687 ? 1.4178 0.6050 1.3111 -0.1960 -0.2432 0.0712 687 MET A O 5309 C CB . MET A 687 ? 1.4166 0.7726 1.2891 -0.1417 -0.2186 0.0457 687 MET A CB 5310 C CG . MET A 687 ? 1.3606 0.6558 1.2618 -0.1259 -0.2181 0.0612 687 MET A CG 5311 S SD . MET A 687 ? 1.6700 1.0365 1.5996 -0.1403 -0.1979 0.0650 687 MET A SD 5312 C CE . MET A 687 ? 1.4985 0.8032 1.4539 -0.1100 -0.1981 0.0846 687 MET A CE 5313 N N . LYS A 688 ? 1.9642 1.0620 1.8182 -0.1110 -0.2741 0.0623 688 LYS A N 5314 C CA . LYS A 688 ? 1.7830 0.9150 1.6729 -0.1117 -0.2473 0.0721 688 LYS A CA 5315 C C . LYS A 688 ? 1.8285 1.0116 1.7682 -0.1146 -0.2091 0.0878 688 LYS A C 5316 O O . LYS A 688 ? 1.9439 1.1384 1.8944 -0.1182 -0.2052 0.0927 688 LYS A O 5317 C CB . LYS A 688 ? 1.4143 0.5067 1.2845 -0.0674 -0.2711 0.0670 688 LYS A CB 5318 C CG . LYS A 688 ? 1.6298 0.6547 1.4314 -0.0452 -0.3168 0.0413 688 LYS A CG 5319 C CD . LYS A 688 ? 1.7428 0.7441 1.5291 -0.0135 -0.3364 0.0337 688 LYS A CD 5320 C CE . LYS A 688 ? 1.8436 0.8409 1.6408 0.0358 -0.3556 0.0343 688 LYS A CE 5321 N NZ . LYS A 688 ? 2.0981 1.0744 1.8781 0.0632 -0.3821 0.0249 688 LYS A NZ 5322 N N . ALA A 689 ? 1.8229 1.0305 1.7846 -0.1112 -0.1832 0.0940 689 ALA A N 5323 C CA . ALA A 689 ? 1.5767 0.8174 1.5670 -0.1116 -0.1553 0.1060 689 ALA A CA 5324 C C . ALA A 689 ? 1.7719 1.0006 1.7663 -0.0826 -0.1626 0.1203 689 ALA A C 5325 O O . ALA A 689 ? 1.6256 0.8216 1.6041 -0.0603 -0.1947 0.1188 689 ALA A O 5326 C CB . ALA A 689 ? 1.3306 0.5724 1.3303 -0.1216 -0.1725 0.1145 689 ALA A CB 5327 N N . GLY A 690 ? 1.8355 1.0822 1.8505 -0.0836 -0.1568 0.1362 690 GLY A N 5328 C CA . GLY A 690 ? 1.7357 0.9810 1.7572 -0.0598 -0.1598 0.1523 690 GLY A CA 5329 C C . GLY A 690 ? 1.8575 1.0897 1.8724 -0.0557 -0.1754 0.1469 690 GLY A C 5330 O O . GLY A 690 ? 1.7107 0.9551 1.7294 -0.0750 -0.1662 0.1415 690 GLY A O 5331 N N . THR A 691 ? 1.9755 1.1816 1.9802 -0.0292 -0.2064 0.1468 691 THR A N 5332 C CA . THR A 691 ? 2.1450 1.3273 2.1324 -0.0182 -0.2303 0.1355 691 THR A CA 5333 C C . THR A 691 ? 2.0765 1.2791 2.0824 -0.0228 -0.2193 0.1477 691 THR A C 5334 O O . THR A 691 ? 1.9925 1.1972 1.9934 -0.0450 -0.2135 0.1388 691 THR A O 5335 C CB . THR A 691 ? 1.4273 0.5865 1.3837 -0.0385 -0.2382 0.1125 691 THR A CB 5336 O OG1 . THR A 691 ? 1.4943 0.6454 1.4400 -0.0430 -0.2392 0.1051 691 THR A OG1 5337 C CG2 . THR A 691 ? 1.3310 0.4607 1.2487 -0.0106 -0.2691 0.0919 691 THR A CG2 5338 N N . GLN A 692 ? 1.9674 1.1878 1.9956 -0.0040 -0.2197 0.1697 692 GLN A N 5339 C CA . GLN A 692 ? 1.8620 1.1009 1.9080 -0.0006 -0.2149 0.1839 692 GLN A CA 5340 C C . GLN A 692 ? 1.8040 1.0257 1.8396 0.0309 -0.2441 0.1772 692 GLN A C 5341 O O . GLN A 692 ? 1.8554 1.0794 1.8969 0.0568 -0.2643 0.1839 692 GLN A O 5342 C CB . GLN A 692 ? 2.0085 1.2811 2.0829 0.0029 -0.2019 0.2145 692 GLN A CB 5343 C CG . GLN A 692 ? 2.0483 1.3347 2.1255 -0.0186 -0.1765 0.2165 692 GLN A CG 5344 C CD . GLN A 692 ? 2.1552 1.4715 2.2545 -0.0128 -0.1693 0.2468 692 GLN A CD 5345 O OE1 . GLN A 692 ? 2.2345 1.5706 2.3533 0.0012 -0.1778 0.2693 692 GLN A OE1 5346 N NE2 . GLN A 692 ? 1.9897 1.3127 2.0864 -0.0226 -0.1552 0.2489 692 GLN A NE2 5347 N N . LEU A 693 ? 1.6332 0.9126 1.6486 0.0277 -0.2219 0.1466 693 LEU A N 5348 C CA . LEU A 693 ? 1.5118 0.8450 1.5085 0.0578 -0.2218 0.1202 693 LEU A CA 5349 C C . LEU A 693 ? 1.5754 0.9736 1.5882 0.0641 -0.2000 0.1245 693 LEU A C 5350 O O . LEU A 693 ? 1.5587 0.9910 1.5773 0.0440 -0.1749 0.1245 693 LEU A O 5351 C CB . LEU A 693 ? 1.3071 0.6819 1.2659 0.0533 -0.2097 0.0812 693 LEU A CB 5352 C CG . LEU A 693 ? 1.4767 0.8021 1.4110 0.0533 -0.2306 0.0702 693 LEU A CG 5353 C CD1 . LEU A 693 ? 1.5468 0.9424 1.4436 0.0601 -0.2194 0.0335 693 LEU A CD1 5354 C CD2 . LEU A 693 ? 1.8287 1.0832 1.7666 0.0873 -0.2725 0.0805 693 LEU A CD2 5355 N N . LEU A 694 ? 1.7133 1.1257 1.7336 0.0934 -0.2152 0.1270 694 LEU A N 5356 C CA . LEU A 694 ? 1.5498 1.0251 1.5816 0.1022 -0.1966 0.1278 694 LEU A CA 5357 C C . LEU A 694 ? 1.6247 1.1463 1.6296 0.1216 -0.1924 0.0891 694 LEU A C 5358 O O . LEU A 694 ? 1.8359 1.3385 1.8221 0.1405 -0.2155 0.0689 694 LEU A O 5359 C CB . LEU A 694 ? 1.5733 1.0381 1.6427 0.1154 -0.2187 0.1674 694 LEU A CB 5360 C CG . LEU A 694 ? 1.6506 1.0944 1.7538 0.0997 -0.2188 0.2148 694 LEU A CG 5361 C CD1 . LEU A 694 ? 1.4296 0.9104 1.5275 0.0809 -0.1803 0.2067 694 LEU A CD1 5362 C CD2 . LEU A 694 ? 1.7977 1.1584 1.9081 0.0918 -0.2498 0.2366 694 LEU A CD2 5363 N N . ALA A 695 ? 1.5893 1.1720 1.5921 0.1202 -0.1657 0.0788 695 ALA A N 5364 C CA . ALA A 695 ? 1.5377 1.1713 1.5168 0.1348 -0.1570 0.0454 695 ALA A CA 5365 C C . ALA A 695 ? 1.5558 1.2422 1.5408 0.1312 -0.1313 0.0454 695 ALA A C 5366 O O . ALA A 695 ? 1.6379 1.3251 1.6396 0.1189 -0.1196 0.0656 695 ALA A O 5367 C CB . ALA A 695 ? 1.4936 1.1436 1.4416 0.1241 -0.1494 0.0213 695 ALA A CB 5368 N N . GLY A 696 ? 1.5316 1.2628 1.5017 0.1449 -0.1241 0.0216 696 GLY A N 5369 C CA . GLY A 696 ? 1.4850 1.2594 1.4587 0.1434 -0.1033 0.0212 696 GLY A CA 5370 C C . GLY A 696 ? 1.4691 1.2941 1.4201 0.1468 -0.0916 -0.0037 696 GLY A C 5371 O O . GLY A 696 ? 1.4801 1.3183 1.4146 0.1611 -0.1004 -0.0240 696 GLY A O 5372 N N . LEU A 697 ? 1.5028 1.3590 1.4534 0.1368 -0.0748 -0.0010 697 LEU A N 5373 C CA . LEU A 697 ? 1.6833 1.5905 1.6172 0.1347 -0.0655 -0.0146 697 LEU A CA 5374 C C . LEU A 697 ? 1.7479 1.6740 1.6881 0.1434 -0.0557 -0.0135 697 LEU A C 5375 O O . LEU A 697 ? 1.6884 1.6009 1.6397 0.1396 -0.0520 -0.0005 697 LEU A O 5376 C CB . LEU A 697 ? 1.6940 1.6181 1.6212 0.1059 -0.0647 -0.0073 697 LEU A CB 5377 C CG . LEU A 697 ? 1.5007 1.4120 1.4203 0.0902 -0.0735 -0.0072 697 LEU A CG 5378 C CD1 . LEU A 697 ? 1.3408 1.1916 1.2755 0.0789 -0.0805 0.0062 697 LEU A CD1 5379 C CD2 . LEU A 697 ? 1.4209 1.3803 1.3336 0.0625 -0.0756 -0.0013 697 LEU A CD2 5380 N N . ARG A 698 ? 1.6911 1.6503 1.6232 0.1577 -0.0525 -0.0284 698 ARG A N 5381 C CA . ARG A 698 ? 1.6688 1.6400 1.6070 0.1659 -0.0445 -0.0282 698 ARG A CA 5382 C C . ARG A 698 ? 1.6283 1.6336 1.5577 0.1527 -0.0374 -0.0223 698 ARG A C 5383 O O . ARG A 698 ? 1.6320 1.6750 1.5504 0.1429 -0.0383 -0.0229 698 ARG A O 5384 C CB . ARG A 698 ? 1.8610 1.8426 1.8005 0.1884 -0.0499 -0.0472 698 ARG A CB 5385 C CG . ARG A 698 ? 1.8269 1.7712 1.7808 0.2017 -0.0702 -0.0494 698 ARG A CG 5386 C CD . ARG A 698 ? 1.7622 1.7106 1.7253 0.2226 -0.0850 -0.0672 698 ARG A CD 5387 N NE . ARG A 698 ? 1.8067 1.7161 1.7908 0.2329 -0.1163 -0.0628 698 ARG A NE 5388 C CZ . ARG A 698 ? 1.9393 1.8267 1.9517 0.2261 -0.1249 -0.0364 698 ARG A CZ 5389 N NH1 . ARG A 698 ? 1.9169 1.8179 1.9345 0.2138 -0.1011 -0.0183 698 ARG A NH1 5390 N NH2 . ARG A 698 ? 2.0280 1.8835 2.0643 0.2332 -0.1613 -0.0256 698 ARG A NH2 5391 N N . PHE A 699 ? 1.6586 1.6535 1.5943 0.1532 -0.0342 -0.0135 699 PHE A N 5392 C CA . PHE A 699 ? 1.7364 1.7517 1.6671 0.1426 -0.0373 -0.0039 699 PHE A CA 5393 C C . PHE A 699 ? 1.8662 1.8767 1.7992 0.1564 -0.0316 -0.0047 699 PHE A C 5394 O O . PHE A 699 ? 2.0086 1.9969 1.9493 0.1702 -0.0262 -0.0083 699 PHE A O 5395 C CB . PHE A 699 ? 1.8829 1.8786 1.8167 0.1274 -0.0512 0.0086 699 PHE A CB 5396 C CG . PHE A 699 ? 1.8550 1.8525 1.7887 0.1076 -0.0593 0.0117 699 PHE A CG 5397 C CD1 . PHE A 699 ? 1.7633 1.7305 1.7012 0.1104 -0.0559 0.0077 699 PHE A CD1 5398 C CD2 . PHE A 699 ? 1.8307 1.8612 1.7630 0.0837 -0.0735 0.0231 699 PHE A CD2 5399 C CE1 . PHE A 699 ? 1.6768 1.6388 1.6142 0.0910 -0.0639 0.0105 699 PHE A CE1 5400 C CE2 . PHE A 699 ? 1.7198 1.7533 1.6532 0.0623 -0.0820 0.0270 699 PHE A CE2 5401 C CZ . PHE A 699 ? 1.6919 1.6871 1.6262 0.0666 -0.0760 0.0183 699 PHE A CZ 5402 N N . SER A 700 ? 1.8299 1.8636 1.7584 0.1508 -0.0353 0.0028 700 SER A N 5403 C CA . SER A 700 ? 1.9691 1.9900 1.8986 0.1614 -0.0334 0.0050 700 SER A CA 5404 C C . SER A 700 ? 2.0371 2.0522 1.9643 0.1517 -0.0542 0.0236 700 SER A C 5405 O O . SER A 700 ? 1.9954 2.0426 1.9236 0.1354 -0.0663 0.0392 700 SER A O 5406 C CB . SER A 700 ? 1.9713 2.0191 1.9006 0.1683 -0.0229 -0.0036 700 SER A CB 5407 O OG . SER A 700 ? 1.9972 2.0924 1.9225 0.1562 -0.0273 0.0080 700 SER A OG 5408 N N . VAL A 701 ? 2.0220 2.0006 1.9476 0.1633 -0.0632 0.0237 701 VAL A N 5409 C CA . VAL A 701 ? 1.8878 1.8503 1.8114 0.1596 -0.0948 0.0375 701 VAL A CA 5410 C C . VAL A 701 ? 1.9275 1.8762 1.8475 0.1690 -0.1032 0.0459 701 VAL A C 5411 O O . VAL A 701 ? 1.8920 1.8197 1.8069 0.1890 -0.0890 0.0355 701 VAL A O 5412 C CB . VAL A 701 ? 1.7490 1.6809 1.6694 0.1739 -0.1076 0.0291 701 VAL A CB 5413 C CG1 . VAL A 701 ? 1.7276 1.6662 1.6545 0.1555 -0.1172 0.0298 701 VAL A CG1 5414 C CG2 . VAL A 701 ? 1.7860 1.7103 1.7042 0.1971 -0.0806 0.0159 701 VAL A CG2 5415 N N . HIS A 702 ? 1.9518 1.9149 1.8771 0.1522 -0.1289 0.0691 702 HIS A N 5416 C CA . HIS A 702 ? 1.9754 1.9205 1.9001 0.1577 -0.1456 0.0848 702 HIS A CA 5417 C C . HIS A 702 ? 2.0300 1.9291 1.9512 0.1682 -0.1921 0.0916 702 HIS A C 5418 O O . HIS A 702 ? 2.1458 2.0195 2.0673 0.1725 -0.2216 0.1095 702 HIS A O 5419 C CB . HIS A 702 ? 2.0995 2.0933 2.0360 0.1341 -0.1524 0.1137 702 HIS A CB 5420 C CG . HIS A 702 ? 2.2058 2.2531 2.1429 0.1296 -0.1135 0.1020 702 HIS A CG 5421 N ND1 . HIS A 702 ? 2.2496 2.3653 2.1950 0.1104 -0.1144 0.1233 702 HIS A ND1 5422 C CD2 . HIS A 702 ? 2.1652 2.2107 2.0964 0.1445 -0.0784 0.0714 702 HIS A CD2 5423 C CE1 . HIS A 702 ? 2.1849 2.3362 2.1249 0.1190 -0.0805 0.1002 702 HIS A CE1 5424 N NE2 . HIS A 702 ? 2.1430 2.2475 2.0761 0.1384 -0.0617 0.0689 702 HIS A NE2 5425 N N . GLN A 703 ? 2.0201 1.9084 1.9388 0.1734 -0.2025 0.0771 703 GLN A N 5426 C CA . GLN A 703 ? 2.0623 1.9105 1.9768 0.1892 -0.2507 0.0733 703 GLN A CA 5427 C C . GLN A 703 ? 2.1246 1.9610 2.0525 0.1725 -0.3134 0.1043 703 GLN A C 5428 O O . GLN A 703 ? 2.2142 2.0910 2.1602 0.1380 -0.3213 0.1333 703 GLN A O 5429 C CB . GLN A 703 ? 1.9928 1.8038 1.8872 0.2314 -0.2439 0.0513 703 GLN A CB 5430 C CG . GLN A 703 ? 2.0054 1.7907 1.8920 0.2441 -0.2456 0.0603 703 GLN A CG 5431 C CD . GLN A 703 ? 2.0641 1.8697 1.9499 0.2428 -0.1892 0.0533 703 GLN A CD 5432 O OE1 . GLN A 703 ? 2.1778 2.0072 2.0643 0.2452 -0.1525 0.0369 703 GLN A OE1 5433 N NE2 . GLN A 703 ? 2.0375 1.8318 1.9251 0.2378 -0.1875 0.0676 703 GLN A NE2 5434 N N . GLN A 704 ? 2.0522 1.8374 1.9718 0.1991 -0.3611 0.1004 704 GLN A N 5435 C CA . GLN A 704 ? 2.1004 1.8624 2.0361 0.1874 -0.4403 0.1262 704 GLN A CA 5436 C C . GLN A 704 ? 2.1746 1.8716 2.0909 0.2341 -0.4851 0.1056 704 GLN A C 5437 O O . GLN A 704 ? 2.2130 1.8973 2.1038 0.2710 -0.4463 0.0742 704 GLN A O 5438 C CB . GLN A 704 ? 1.9306 1.7149 1.8852 0.1598 -0.4677 0.1285 704 GLN A CB 5439 C CG . GLN A 704 ? 1.8415 1.6248 1.8262 0.1283 -0.5493 0.1688 704 GLN A CG 5440 C CD . GLN A 704 ? 1.9499 1.7904 1.9562 0.0876 -0.5399 0.2179 704 GLN A CD 5441 O OE1 . GLN A 704 ? 2.1813 2.0112 2.1903 0.0912 -0.5551 0.2451 704 GLN A OE1 5442 N NE2 . GLN A 704 ? 1.7294 1.6346 1.7506 0.0504 -0.5148 0.2302 704 GLN A NE2 5443 N N . SER A 705 ? 2.0167 1.6761 1.9456 0.2342 -0.5704 0.1241 705 SER A N 5444 C CA . SER A 705 ? 1.8890 1.4920 1.7985 0.2815 -0.6181 0.0921 705 SER A CA 5445 C C . SER A 705 ? 2.0330 1.6042 1.9106 0.3252 -0.5894 0.0726 705 SER A C 5446 O O . SER A 705 ? 2.0307 1.5831 1.9130 0.3117 -0.5920 0.0907 705 SER A O 5447 C CB . SER A 705 ? 1.8795 1.4917 1.7802 0.3025 -0.6159 0.0531 705 SER A CB 5448 O OG . SER A 705 ? 2.0989 1.7291 2.0306 0.2607 -0.6546 0.0686 705 SER A OG 5449 N N . GLU A 706 ? 2.0758 1.6579 1.9266 0.3648 -0.5452 0.0344 706 GLU A N 5450 C CA . GLU A 706 ? 1.9622 1.5198 1.7778 0.4220 -0.5332 0.0034 706 GLU A CA 5451 C C . GLU A 706 ? 1.7408 1.2896 1.5444 0.4474 -0.5682 -0.0350 706 GLU A C 5452 O O . GLU A 706 ? 1.8201 1.3685 1.5931 0.4921 -0.5544 -0.0676 706 GLU A O 5453 C CB . GLU A 706 ? 1.8513 1.3752 1.6617 0.4160 -0.5319 0.0185 706 GLU A CB 5454 C CG . GLU A 706 ? 1.9359 1.4697 1.7548 0.3932 -0.4883 0.0496 706 GLU A CG 5455 C CD . GLU A 706 ? 2.0179 1.5162 1.8411 0.3789 -0.4997 0.0720 706 GLU A CD 5456 O OE1 . GLU A 706 ? 1.9388 1.4129 1.7562 0.3832 -0.5253 0.0569 706 GLU A OE1 5457 O OE2 . GLU A 706 ? 1.9939 1.4942 1.8270 0.3591 -0.4774 0.1020 706 GLU A OE2 5458 N N . MET A 707 ? 1.6152 1.1625 1.4434 0.4158 -0.6108 -0.0317 707 MET A N 5459 C CA . MET A 707 ? 1.6589 1.2025 1.4783 0.4378 -0.6392 -0.0720 707 MET A CA 5460 C C . MET A 707 ? 1.7806 1.3624 1.6077 0.4446 -0.6263 -0.0802 707 MET A C 5461 O O . MET A 707 ? 1.9625 1.5487 1.7843 0.4642 -0.6446 -0.1135 707 MET A O 5462 C CB . MET A 707 ? 1.5862 1.0949 1.4293 0.3996 -0.6957 -0.0686 707 MET A CB 5463 C CG . MET A 707 ? 1.7401 1.2069 1.5733 0.4001 -0.7134 -0.0688 707 MET A CG 5464 S SD . MET A 707 ? 2.5435 1.9972 2.3206 0.4707 -0.7002 -0.1215 707 MET A SD 5465 C CE . MET A 707 ? 1.8707 1.2714 1.6458 0.4536 -0.7258 -0.1105 707 MET A CE 5466 N N . ASP A 708 ? 1.5906 1.2035 1.4308 0.4203 -0.5841 -0.0525 708 ASP A N 5467 C CA . ASP A 708 ? 1.6883 1.3461 1.5429 0.3936 -0.5418 -0.0584 708 ASP A CA 5468 C C . ASP A 708 ? 1.6944 1.3920 1.5276 0.4298 -0.4775 -0.0853 708 ASP A C 5469 O O . ASP A 708 ? 1.8450 1.5621 1.6645 0.4407 -0.4228 -0.0814 708 ASP A O 5470 C CB . ASP A 708 ? 1.6609 1.3490 1.5400 0.3307 -0.4976 -0.0228 708 ASP A CB 5471 C CG . ASP A 708 ? 1.7999 1.4851 1.7111 0.2830 -0.5507 0.0002 708 ASP A CG 5472 O OD1 . ASP A 708 ? 2.0091 1.6791 1.9281 0.2895 -0.6006 -0.0177 708 ASP A OD1 5473 O OD2 . ASP A 708 ? 1.7433 1.4471 1.6734 0.2388 -0.5443 0.0369 708 ASP A OD2 5474 N N . THR A 709 ? 1.5859 1.2987 1.4198 0.4468 -0.4883 -0.1097 709 THR A N 5475 C CA . THR A 709 ? 1.5986 1.3621 1.4197 0.4760 -0.4301 -0.1266 709 THR A CA 5476 C C . THR A 709 ? 1.5242 1.3247 1.3665 0.4286 -0.3640 -0.1049 709 THR A C 5477 O O . THR A 709 ? 1.3679 1.2087 1.2051 0.4368 -0.3044 -0.0989 709 THR A O 5478 C CB . THR A 709 ? 1.6979 1.4676 1.5115 0.5187 -0.4701 -0.1617 709 THR A CB 5479 O OG1 . THR A 709 ? 1.8350 1.5886 1.6770 0.4766 -0.5007 -0.1582 709 THR A OG1 5480 C CG2 . THR A 709 ? 1.6533 1.3834 1.4428 0.5748 -0.5444 -0.1892 709 THR A CG2 5481 N N . SER A 710 ? 1.6149 1.4021 1.4821 0.3793 -0.3805 -0.0917 710 SER A N 5482 C CA . SER A 710 ? 1.5528 1.3675 1.4378 0.3391 -0.3284 -0.0757 710 SER A CA 5483 C C . SER A 710 ? 1.5184 1.3231 1.4237 0.2815 -0.3337 -0.0498 710 SER A C 5484 O O . SER A 710 ? 1.7329 1.5134 1.6445 0.2674 -0.3837 -0.0401 710 SER A O 5485 C CB . SER A 710 ? 1.6941 1.5179 1.5877 0.3444 -0.3358 -0.0912 710 SER A CB 5486 O OG . SER A 710 ? 2.0087 1.8562 1.8836 0.4020 -0.3334 -0.1146 710 SER A OG 5487 N N . VAL A 711 ? 1.4840 1.3117 1.4001 0.2505 -0.2854 -0.0365 711 VAL A N 5488 C CA . VAL A 711 ? 1.5995 1.4311 1.5328 0.1996 -0.2877 -0.0150 711 VAL A CA 5489 C C . VAL A 711 ? 1.7138 1.5479 1.6620 0.1728 -0.2824 -0.0158 711 VAL A C 5490 O O . VAL A 711 ? 1.7014 1.5431 1.6477 0.1863 -0.2486 -0.0236 711 VAL A O 5491 C CB . VAL A 711 ? 1.4813 1.3361 1.4115 0.1875 -0.2396 0.0001 711 VAL A CB 5492 C CG1 . VAL A 711 ? 1.5332 1.3801 1.4541 0.2009 -0.2533 0.0069 711 VAL A CG1 5493 C CG2 . VAL A 711 ? 1.4083 1.2792 1.3331 0.2062 -0.1875 -0.0067 711 VAL A CG2 5494 N N . LYS A 712 ? 1.7258 1.5553 1.6913 0.1326 -0.3183 -0.0034 712 LYS A N 5495 C CA . LYS A 712 ? 1.5844 1.4062 1.5654 0.1057 -0.3273 -0.0061 712 LYS A CA 5496 C C . LYS A 712 ? 1.4887 1.3314 1.4776 0.0647 -0.2963 0.0122 712 LYS A C 5497 O O . LYS A 712 ? 1.4816 1.3479 1.4767 0.0361 -0.3070 0.0325 712 LYS A O 5498 C CB . LYS A 712 ? 1.7209 1.5204 1.7197 0.0891 -0.4024 -0.0078 712 LYS A CB 5499 C CG . LYS A 712 ? 1.7065 1.4971 1.7266 0.0496 -0.4193 -0.0064 712 LYS A CG 5500 C CD . LYS A 712 ? 1.7088 1.4823 1.7540 0.0228 -0.5030 -0.0009 712 LYS A CD 5501 C CE . LYS A 712 ? 1.6273 1.4221 1.6968 -0.0405 -0.5148 0.0279 712 LYS A CE 5502 N NZ . LYS A 712 ? 1.4587 1.3006 1.5218 -0.0576 -0.4797 0.0577 712 LYS A NZ 5503 N N . PHE A 713 ? 1.4481 1.2854 1.4367 0.0645 -0.2609 0.0064 713 PHE A N 5504 C CA . PHE A 713 ? 1.4014 1.2484 1.3955 0.0302 -0.2394 0.0185 713 PHE A CA 5505 C C . PHE A 713 ? 1.4312 1.2508 1.4404 0.0071 -0.2578 0.0144 713 PHE A C 5506 O O . PHE A 713 ? 1.5191 1.3166 1.5297 0.0286 -0.2530 0.0019 713 PHE A O 5507 C CB . PHE A 713 ? 1.4746 1.3303 1.4568 0.0487 -0.1861 0.0187 713 PHE A CB 5508 C CG . PHE A 713 ? 1.5164 1.4010 1.4870 0.0602 -0.1672 0.0234 713 PHE A CG 5509 C CD1 . PHE A 713 ? 1.4661 1.3519 1.4279 0.0940 -0.1572 0.0173 713 PHE A CD1 5510 C CD2 . PHE A 713 ? 1.6418 1.5565 1.6100 0.0386 -0.1592 0.0334 713 PHE A CD2 5511 C CE1 . PHE A 713 ? 1.5297 1.4371 1.4831 0.1022 -0.1409 0.0211 713 PHE A CE1 5512 C CE2 . PHE A 713 ? 1.7182 1.6620 1.6770 0.0510 -0.1424 0.0360 713 PHE A CE2 5513 C CZ . PHE A 713 ? 1.6165 1.5521 1.5692 0.0809 -0.1337 0.0298 713 PHE A CZ 5514 N N . ASP A 714 ? 1.4886 1.3150 1.5105 -0.0371 -0.2795 0.0271 714 ASP A N 5515 C CA . ASP A 714 ? 1.4815 1.2786 1.5197 -0.0660 -0.2975 0.0247 714 ASP A CA 5516 C C . ASP A 714 ? 1.4329 1.2358 1.4672 -0.0911 -0.2665 0.0356 714 ASP A C 5517 O O . ASP A 714 ? 1.3658 1.2091 1.3941 -0.1070 -0.2592 0.0491 714 ASP A O 5518 C CB . ASP A 714 ? 1.6049 1.3998 1.6666 -0.1009 -0.3634 0.0301 714 ASP A CB 5519 C CG . ASP A 714 ? 1.7688 1.5440 1.8346 -0.0712 -0.4066 0.0128 714 ASP A CG 5520 O OD1 . ASP A 714 ? 1.8260 1.6026 1.8724 -0.0238 -0.3814 0.0003 714 ASP A OD1 5521 O OD2 . ASP A 714 ? 1.8176 1.5765 1.9064 -0.0942 -0.4705 0.0112 714 ASP A OD2 5522 N N . LEU A 715 ? 1.5512 1.3159 1.5885 -0.0916 -0.2505 0.0304 715 LEU A N 5523 C CA . LEU A 715 ? 1.4912 1.2492 1.5216 -0.1073 -0.2240 0.0383 715 LEU A CA 5524 C C . LEU A 715 ? 1.3784 1.0966 1.4251 -0.1441 -0.2432 0.0405 715 LEU A C 5525 O O . LEU A 715 ? 1.4677 1.1482 1.5288 -0.1420 -0.2578 0.0326 715 LEU A O 5526 C CB . LEU A 715 ? 1.3726 1.1156 1.3904 -0.0696 -0.1832 0.0365 715 LEU A CB 5527 C CG . LEU A 715 ? 1.3779 1.1524 1.3826 -0.0320 -0.1628 0.0334 715 LEU A CG 5528 C CD1 . LEU A 715 ? 1.3001 1.0597 1.2999 -0.0048 -0.1322 0.0373 715 LEU A CD1 5529 C CD2 . LEU A 715 ? 1.6088 1.4304 1.6024 -0.0402 -0.1631 0.0364 715 LEU A CD2 5530 N N . GLN A 716 ? 1.2764 1.0066 1.3201 -0.1764 -0.2433 0.0505 716 GLN A N 5531 C CA . GLN A 716 ? 1.3391 1.0264 1.3952 -0.2121 -0.2559 0.0538 716 GLN A CA 5532 C C . GLN A 716 ? 1.3286 1.0316 1.3678 -0.2264 -0.2385 0.0620 716 GLN A C 5533 O O . GLN A 716 ? 1.3446 1.1054 1.3661 -0.2148 -0.2249 0.0652 716 GLN A O 5534 C CB . GLN A 716 ? 1.3053 0.9922 1.3895 -0.2560 -0.3080 0.0563 716 GLN A CB 5535 C CG . GLN A 716 ? 1.5028 1.2522 1.5923 -0.2948 -0.3321 0.0746 716 GLN A CG 5536 C CD . GLN A 716 ? 1.4764 1.2143 1.5994 -0.3515 -0.3870 0.0832 716 GLN A CD 5537 O OE1 . GLN A 716 ? 1.5002 1.1757 1.6398 -0.3619 -0.4036 0.0710 716 GLN A OE1 5538 N NE2 . GLN A 716 ? 1.3292 1.1319 1.4657 -0.3899 -0.4184 0.1071 716 GLN A NE2 5539 N N . ILE A 717 ? 1.3733 1.0251 1.4169 -0.2484 -0.2404 0.0643 717 ILE A N 5540 C CA . ILE A 717 ? 1.3556 1.0158 1.3806 -0.2598 -0.2294 0.0692 717 ILE A CA 5541 C C . ILE A 717 ? 1.2811 0.9605 1.3221 -0.3176 -0.2613 0.0805 717 ILE A C 5542 O O . ILE A 717 ? 1.4199 1.0630 1.4895 -0.3511 -0.2917 0.0821 717 ILE A O 5543 C CB . ILE A 717 ? 1.2032 0.7864 1.2198 -0.2420 -0.2119 0.0674 717 ILE A CB 5544 C CG1 . ILE A 717 ? 1.2487 0.8172 1.2592 -0.1909 -0.1888 0.0638 717 ILE A CG1 5545 C CG2 . ILE A 717 ? 1.1793 0.7690 1.1704 -0.2427 -0.2044 0.0675 717 ILE A CG2 5546 C CD1 . ILE A 717 ? 1.3492 0.8404 1.3631 -0.1761 -0.1816 0.0719 717 ILE A CD1 5547 N N . GLN A 718 ? 1.2075 0.9508 1.2317 -0.3288 -0.2572 0.0886 718 GLN A N 5548 C CA . GLN A 718 ? 1.3145 1.0904 1.3544 -0.3862 -0.2871 0.1054 718 GLN A CA 5549 C C . GLN A 718 ? 1.3422 1.1157 1.3556 -0.3877 -0.2710 0.1047 718 GLN A C 5550 O O . GLN A 718 ? 1.4062 1.1833 1.3856 -0.3402 -0.2408 0.0919 718 GLN A O 5551 C CB . GLN A 718 ? 1.2762 1.1596 1.3269 -0.4060 -0.3076 0.1254 718 GLN A CB 5552 C CG . GLN A 718 ? 1.2668 1.1495 1.3449 -0.4075 -0.3360 0.1277 718 GLN A CG 5553 C CD . GLN A 718 ? 1.3967 1.3827 1.4877 -0.4269 -0.3611 0.1548 718 GLN A CD 5554 O OE1 . GLN A 718 ? 1.5102 1.5041 1.6171 -0.4193 -0.3841 0.1584 718 GLN A OE1 5555 N NE2 . GLN A 718 ? 1.4126 1.4823 1.4967 -0.4506 -0.3589 0.1766 718 GLN A NE2 5556 N N . SER A 719 ? 1.1677 0.9339 1.1971 -0.4414 -0.2963 0.1173 719 SER A N 5557 C CA . SER A 719 ? 1.1772 0.9414 1.1800 -0.4446 -0.2854 0.1167 719 SER A CA 5558 C C . SER A 719 ? 1.0808 0.9034 1.1033 -0.5105 -0.3169 0.1405 719 SER A C 5559 O O . SER A 719 ? 1.3016 1.1668 1.3520 -0.5162 -0.3304 0.1524 719 SER A O 5560 C CB . SER A 719 ? 1.3580 0.9938 1.3549 -0.4320 -0.2770 0.1035 719 SER A CB 5561 O OG . SER A 719 ? 1.6841 1.2980 1.7137 -0.4207 -0.2713 0.0981 719 SER A OG 5562 N N . SER A 720 ? 1.1014 0.9351 1.0974 -0.5140 -0.3083 0.1407 720 SER A N 5563 C CA . SER A 720 ? 1.0797 0.9850 1.0865 -0.5574 -0.3261 0.1635 720 SER A CA 5564 C C . SER A 720 ? 1.1119 0.9403 1.1257 -0.5288 -0.3103 0.1515 720 SER A C 5565 O O . SER A 720 ? 1.0913 0.9618 1.1075 -0.5442 -0.3160 0.1653 720 SER A O 5566 C CB . SER A 720 ? 1.1193 1.1148 1.0844 -0.5464 -0.3121 0.1653 720 SER A CB 5567 O OG . SER A 720 ? 1.2873 1.3879 1.2333 -0.5010 -0.2913 0.1643 720 SER A OG 5568 N N . ASN A 721 ? 1.1727 0.9069 1.1924 -0.4857 -0.2887 0.1267 721 ASN A N 5569 C CA . ASN A 721 ? 1.4166 1.1113 1.4511 -0.4553 -0.2678 0.1112 721 ASN A CA 5570 C C . ASN A 721 ? 1.5759 1.3117 1.6384 -0.4541 -0.2751 0.1141 721 ASN A C 5571 O O . ASN A 721 ? 1.7280 1.4971 1.8018 -0.4624 -0.2931 0.1235 721 ASN A O 5572 C CB . ASN A 721 ? 1.3045 0.9270 1.3445 -0.4113 -0.2395 0.0887 721 ASN A CB 5573 C CG . ASN A 721 ? 1.5236 1.0872 1.5323 -0.4034 -0.2366 0.0873 721 ASN A CG 5574 O OD1 . ASN A 721 ? 1.6178 1.1893 1.5969 -0.4331 -0.2593 0.0983 721 ASN A OD1 5575 N ND2 . ASN A 721 ? 1.5987 1.1096 1.6115 -0.3641 -0.2101 0.0742 721 ASN A ND2 5576 N N . LEU A 722 ? 1.4200 1.1407 1.4787 -0.4522 -0.2802 0.1191 722 LEU A N 5577 C CA . LEU A 722 ? 1.3605 1.0956 1.4213 -0.4655 -0.3166 0.1428 722 LEU A CA 5578 C C . LEU A 722 ? 1.5655 1.2601 1.6367 -0.4418 -0.3254 0.1349 722 LEU A C 5579 O O . LEU A 722 ? 1.6719 1.3812 1.7541 -0.4463 -0.3528 0.1467 722 LEU A O 5580 C CB . LEU A 722 ? 1.3608 1.0882 1.4041 -0.4805 -0.3339 0.1616 722 LEU A CB 5581 C CG . LEU A 722 ? 1.3404 1.1158 1.3723 -0.5071 -0.3286 0.1720 722 LEU A CG 5582 C CD1 . LEU A 722 ? 1.2365 1.0039 1.2493 -0.5239 -0.3505 0.1943 722 LEU A CD1 5583 C CD2 . LEU A 722 ? 1.0696 0.9272 1.1140 -0.5309 -0.3383 0.1888 722 LEU A CD2 5584 N N . PHE A 723 ? 1.3495 0.9955 1.4184 -0.4163 -0.3042 0.1171 723 PHE A N 5585 C CA . PHE A 723 ? 1.5470 1.1637 1.6276 -0.3944 -0.3106 0.1095 723 PHE A CA 5586 C C . PHE A 723 ? 1.5700 1.1678 1.6564 -0.3714 -0.2794 0.0888 723 PHE A C 5587 O O . PHE A 723 ? 1.4277 1.0077 1.5047 -0.3629 -0.2513 0.0807 723 PHE A O 5588 C CB . PHE A 723 ? 1.6282 1.2123 1.7042 -0.3858 -0.3189 0.1137 723 PHE A CB 5589 C CG . PHE A 723 ? 1.6809 1.2770 1.7482 -0.4079 -0.3492 0.1359 723 PHE A CG 5590 C CD1 . PHE A 723 ? 1.7134 1.3186 1.7900 -0.4166 -0.3877 0.1529 723 PHE A CD1 5591 C CD2 . PHE A 723 ? 1.6039 1.1984 1.6528 -0.4195 -0.3418 0.1417 723 PHE A CD2 5592 C CE1 . PHE A 723 ? 1.7724 1.3846 1.8393 -0.4378 -0.4182 0.1786 723 PHE A CE1 5593 C CE2 . PHE A 723 ? 1.6893 1.2952 1.7277 -0.4415 -0.3699 0.1644 723 PHE A CE2 5594 C CZ . PHE A 723 ? 1.7515 1.3663 1.7983 -0.4513 -0.4081 0.1846 723 PHE A CZ 5595 N N . ASP A 724 ? 1.7125 1.3108 1.8131 -0.3607 -0.2876 0.0822 724 ASP A N 5596 C CA . ASP A 724 ? 1.5840 1.1663 1.6892 -0.3403 -0.2611 0.0657 724 ASP A CA 5597 C C . ASP A 724 ? 1.5083 1.1066 1.6088 -0.3461 -0.2382 0.0595 724 ASP A C 5598 O O . ASP A 724 ? 1.3854 0.9546 1.4786 -0.3305 -0.2121 0.0531 724 ASP A O 5599 C CB . ASP A 724 ? 1.4785 1.0207 1.5795 -0.3186 -0.2410 0.0623 724 ASP A CB 5600 C CG . ASP A 724 ? 1.7825 1.3153 1.8915 -0.3149 -0.2634 0.0678 724 ASP A CG 5601 O OD1 . ASP A 724 ? 1.8956 1.4411 2.0170 -0.3178 -0.2909 0.0682 724 ASP A OD1 5602 O OD2 . ASP A 724 ? 1.8286 1.3407 1.9327 -0.3081 -0.2565 0.0721 724 ASP A OD2 5603 N N . LYS A 725 ? 1.6069 1.2515 1.7119 -0.3693 -0.2545 0.0665 725 LYS A N 5604 C CA . LYS A 725 ? 1.3977 1.0548 1.4874 -0.3929 -0.2684 0.0822 725 LYS A CA 5605 C C . LYS A 725 ? 1.4383 1.0828 1.5258 -0.3906 -0.2790 0.0836 725 LYS A C 5606 O O . LYS A 725 ? 1.4987 1.1482 1.5702 -0.4081 -0.2868 0.0938 725 LYS A O 5607 C CB . LYS A 725 ? 1.2326 0.9549 1.3252 -0.4260 -0.2954 0.1027 725 LYS A CB 5608 C CG . LYS A 725 ? 1.2831 1.0389 1.3940 -0.4290 -0.3227 0.1099 725 LYS A CG 5609 C CD . LYS A 725 ? 1.4136 1.2396 1.5263 -0.4612 -0.3490 0.1394 725 LYS A CD 5610 C CE . LYS A 725 ? 1.2636 1.0990 1.3738 -0.4679 -0.3432 0.1444 725 LYS A CE 5611 N NZ . LYS A 725 ? 1.5214 1.4302 1.6239 -0.5050 -0.3619 0.1788 725 LYS A NZ 5612 N N . VAL A 726 ? 1.2410 0.8713 1.3427 -0.3707 -0.2819 0.0731 726 VAL A N 5613 C CA . VAL A 726 ? 1.0981 0.7169 1.2004 -0.3669 -0.2959 0.0736 726 VAL A CA 5614 C C . VAL A 726 ? 1.2701 0.8360 1.3745 -0.3340 -0.2787 0.0608 726 VAL A C 5615 O O . VAL A 726 ? 1.4058 0.9507 1.5108 -0.3161 -0.2534 0.0537 726 VAL A O 5616 C CB . VAL A 726 ? 1.0550 0.7191 1.1740 -0.3780 -0.3321 0.0789 726 VAL A CB 5617 C CG1 . VAL A 726 ? 1.0931 0.8235 1.2115 -0.4118 -0.3509 0.1015 726 VAL A CG1 5618 C CG2 . VAL A 726 ? 1.1623 0.8237 1.2958 -0.3617 -0.3381 0.0681 726 VAL A CG2 5619 N N . SER A 727 ? 1.4467 0.9977 1.5534 -0.3271 -0.2934 0.0600 727 SER A N 5620 C CA . SER A 727 ? 1.3493 0.8552 1.4604 -0.2962 -0.2833 0.0526 727 SER A CA 5621 C C . SER A 727 ? 1.4797 0.9980 1.6083 -0.2902 -0.3171 0.0409 727 SER A C 5622 O O . SER A 727 ? 1.2677 0.8248 1.4021 -0.3076 -0.3483 0.0420 727 SER A O 5623 C CB . SER A 727 ? 1.3210 0.7951 1.4150 -0.2753 -0.2653 0.0607 727 SER A CB 5624 O OG . SER A 727 ? 1.3330 0.8740 1.4153 -0.2531 -0.2618 0.0560 727 SER A OG 5625 N N . PRO A 728 ? 1.4719 0.9609 1.6098 -0.2638 -0.3150 0.0310 728 PRO A N 5626 C CA . PRO A 728 ? 1.2644 0.7549 1.4167 -0.2508 -0.3549 0.0139 728 PRO A CA 5627 C C . PRO A 728 ? 1.3618 0.8929 1.4950 -0.2211 -0.3426 0.0145 728 PRO A C 5628 O O . PRO A 728 ? 1.6709 1.2109 1.7839 -0.1906 -0.2966 0.0238 728 PRO A O 5629 C CB . PRO A 728 ? 1.4715 0.9261 1.6331 -0.2210 -0.3454 0.0058 728 PRO A CB 5630 C CG . PRO A 728 ? 1.4421 0.8717 1.5932 -0.2161 -0.2984 0.0279 728 PRO A CG 5631 C CD . PRO A 728 ? 1.4335 0.8914 1.5704 -0.2431 -0.2814 0.0357 728 PRO A CD 5632 N N . VAL A 729 ? 1.2683 0.8336 1.4064 -0.2244 -0.3806 0.0072 729 VAL A N 5633 C CA . VAL A 729 ? 1.2904 0.9052 1.4076 -0.1918 -0.3635 0.0096 729 VAL A CA 5634 C C . VAL A 729 ? 1.2941 0.9130 1.3985 -0.1323 -0.3390 -0.0036 729 VAL A C 5635 O O . VAL A 729 ? 1.4270 1.0344 1.5412 -0.1121 -0.3666 -0.0226 729 VAL A O 5636 C CB . VAL A 729 ? 1.1851 0.8307 1.3147 -0.2112 -0.4181 0.0108 729 VAL A CB 5637 C CG1 . VAL A 729 ? 1.1839 0.8747 1.2920 -0.1767 -0.3986 0.0152 729 VAL A CG1 5638 C CG2 . VAL A 729 ? 1.2227 0.8824 1.3690 -0.2734 -0.4442 0.0318 729 VAL A CG2 5639 N N . VAL A 730 ? 1.3153 0.9557 1.3985 -0.1032 -0.2902 0.0060 730 VAL A N 5640 C CA . VAL A 730 ? 1.3738 1.0292 1.4464 -0.0502 -0.2643 0.0003 730 VAL A CA 5641 C C . VAL A 730 ? 1.4317 1.1279 1.4874 -0.0244 -0.2612 -0.0031 730 VAL A C 5642 O O . VAL A 730 ? 1.4094 1.1252 1.4563 -0.0401 -0.2525 0.0071 730 VAL A O 5643 C CB . VAL A 730 ? 1.3705 1.0162 1.4387 -0.0366 -0.2177 0.0183 730 VAL A CB 5644 C CG1 . VAL A 730 ? 1.3980 1.0707 1.4624 0.0135 -0.1957 0.0194 730 VAL A CG1 5645 C CG2 . VAL A 730 ? 1.4238 1.0206 1.5088 -0.0664 -0.2224 0.0263 730 VAL A CG2 5646 N N . SER A 731 ? 1.5526 1.2640 1.6032 0.0173 -0.2694 -0.0178 731 SER A N 5647 C CA . SER A 731 ? 1.5270 1.2689 1.5613 0.0439 -0.2697 -0.0217 731 SER A CA 5648 C C . SER A 731 ? 1.4704 1.2387 1.4909 0.0912 -0.2288 -0.0198 731 SER A C 5649 O O . SER A 731 ? 1.5389 1.3130 1.5630 0.1183 -0.2202 -0.0237 731 SER A O 5650 C CB . SER A 731 ? 1.4778 1.2146 1.5165 0.0526 -0.3284 -0.0412 731 SER A CB 5651 O OG . SER A 731 ? 1.5635 1.2836 1.6210 0.0032 -0.3738 -0.0358 731 SER A OG 5652 N N . HIS A 732 ? 1.3877 1.1781 1.3947 0.0997 -0.2052 -0.0113 732 HIS A N 5653 C CA . HIS A 732 ? 1.4086 1.2281 1.4055 0.1396 -0.1720 -0.0070 732 HIS A CA 5654 C C . HIS A 732 ? 1.4528 1.2893 1.4339 0.1595 -0.1807 -0.0152 732 HIS A C 5655 O O . HIS A 732 ? 1.4018 1.2360 1.3799 0.1370 -0.1886 -0.0109 732 HIS A O 5656 C CB . HIS A 732 ? 1.4312 1.2543 1.4314 0.1303 -0.1335 0.0142 732 HIS A CB 5657 C CG . HIS A 732 ? 1.5615 1.4175 1.5571 0.1630 -0.1059 0.0235 732 HIS A CG 5658 N ND1 . HIS A 732 ? 1.5713 1.4344 1.5653 0.1587 -0.0851 0.0347 732 HIS A ND1 5659 C CD2 . HIS A 732 ? 1.7305 1.6191 1.7240 0.2006 -0.0990 0.0235 732 HIS A CD2 5660 C CE1 . HIS A 732 ? 1.6196 1.5140 1.6144 0.1870 -0.0686 0.0434 732 HIS A CE1 5661 N NE2 . HIS A 732 ? 1.7377 1.6522 1.7313 0.2127 -0.0744 0.0385 732 HIS A NE2 5662 N N . LYS A 733 ? 1.4716 1.3291 1.4427 0.2030 -0.1799 -0.0252 733 LYS A N 5663 C CA . LYS A 733 ? 1.3779 1.2449 1.3326 0.2256 -0.1892 -0.0328 733 LYS A CA 5664 C C . LYS A 733 ? 1.4285 1.3304 1.3749 0.2568 -0.1502 -0.0244 733 LYS A C 5665 O O . LYS A 733 ? 1.5111 1.4410 1.4622 0.2784 -0.1304 -0.0181 733 LYS A O 5666 C CB . LYS A 733 ? 1.3628 1.2182 1.3096 0.2527 -0.2392 -0.0571 733 LYS A CB 5667 C CG . LYS A 733 ? 1.4099 1.2900 1.3515 0.2983 -0.2374 -0.0724 733 LYS A CG 5668 C CD . LYS A 733 ? 1.5669 1.4344 1.4960 0.3347 -0.2941 -0.1033 733 LYS A CD 5669 C CE . LYS A 733 ? 1.7082 1.6149 1.6281 0.3889 -0.2901 -0.1218 733 LYS A CE 5670 N NZ . LYS A 733 ? 1.7235 1.6158 1.6288 0.4323 -0.3535 -0.1592 733 LYS A NZ 5671 N N . VAL A 734 ? 1.5116 1.4159 1.4489 0.2564 -0.1411 -0.0203 734 VAL A N 5672 C CA . VAL A 734 ? 1.6333 1.5686 1.5634 0.2851 -0.1136 -0.0145 734 VAL A CA 5673 C C . VAL A 734 ? 1.5866 1.5153 1.4964 0.3137 -0.1375 -0.0304 734 VAL A C 5674 O O . VAL A 734 ? 1.5973 1.4960 1.5031 0.2981 -0.1654 -0.0346 734 VAL A O 5675 C CB . VAL A 734 ? 1.7115 1.6516 1.6502 0.2627 -0.0836 0.0027 734 VAL A CB 5676 C CG1 . VAL A 734 ? 1.8259 1.7749 1.7840 0.2484 -0.0634 0.0207 734 VAL A CG1 5677 C CG2 . VAL A 734 ? 1.6045 1.5199 1.5410 0.2321 -0.0956 0.0006 734 VAL A CG2 5678 N N . ASP A 735 ? 1.5921 1.5522 1.4900 0.3564 -0.1298 -0.0361 735 ASP A N 5679 C CA . ASP A 735 ? 1.5382 1.4882 1.4129 0.3929 -0.1585 -0.0552 735 ASP A CA 5680 C C . ASP A 735 ? 1.4603 1.4015 1.3275 0.3890 -0.1452 -0.0469 735 ASP A C 5681 O O . ASP A 735 ? 1.4701 1.4359 1.3470 0.3776 -0.1071 -0.0299 735 ASP A O 5682 C CB . ASP A 735 ? 1.5738 1.5698 1.4346 0.4467 -0.1565 -0.0676 735 ASP A CB 5683 C CG . ASP A 735 ? 1.8199 1.8311 1.6902 0.4530 -0.1663 -0.0753 735 ASP A CG 5684 O OD1 . ASP A 735 ? 2.1003 2.0683 1.9775 0.4311 -0.2015 -0.0868 735 ASP A OD1 5685 O OD2 . ASP A 735 ? 1.8964 1.9667 1.7701 0.4778 -0.1404 -0.0665 735 ASP A OD2 5686 N N . LEU A 736 ? 1.3822 1.2849 1.2352 0.3973 -0.1823 -0.0574 736 LEU A N 5687 C CA . LEU A 736 ? 1.3109 1.2007 1.1544 0.4004 -0.1746 -0.0512 736 LEU A CA 5688 C C . LEU A 736 ? 1.4065 1.3289 1.2321 0.4464 -0.1582 -0.0586 736 LEU A C 5689 O O . LEU A 736 ? 1.5461 1.4854 1.3555 0.4894 -0.1774 -0.0770 736 LEU A O 5690 C CB . LEU A 736 ? 1.3776 1.2155 1.2129 0.3986 -0.2259 -0.0545 736 LEU A CB 5691 C CG . LEU A 736 ? 1.4328 1.2505 1.2874 0.3483 -0.2390 -0.0358 736 LEU A CG 5692 C CD1 . LEU A 736 ? 1.5243 1.3656 1.3916 0.3168 -0.1877 -0.0194 736 LEU A CD1 5693 C CD2 . LEU A 736 ? 1.4678 1.2839 1.3367 0.3279 -0.2656 -0.0383 736 LEU A CD2 5694 N N . ALA A 737 ? 1.4150 1.3516 1.2442 0.4384 -0.1249 -0.0450 737 ALA A N 5695 C CA . ALA A 737 ? 1.3993 1.3730 1.2140 0.4765 -0.1091 -0.0469 737 ALA A CA 5696 C C . ALA A 737 ? 1.4530 1.3910 1.2563 0.4772 -0.1128 -0.0458 737 ALA A C 5697 O O . ALA A 737 ? 1.4200 1.3194 1.2345 0.4412 -0.1135 -0.0367 737 ALA A O 5698 C CB . ALA A 737 ? 1.4406 1.4784 1.2780 0.4648 -0.0664 -0.0251 737 ALA A CB 5699 N N . VAL A 738 ? 1.4709 1.4253 1.2512 0.5201 -0.1154 -0.0547 738 VAL A N 5700 C CA . VAL A 738 ? 1.4057 1.3218 1.1732 0.5239 -0.1201 -0.0538 738 VAL A CA 5701 C C . VAL A 738 ? 1.4060 1.3708 1.1852 0.5171 -0.0790 -0.0374 738 VAL A C 5702 O O . VAL A 738 ? 1.4754 1.5053 1.2476 0.5484 -0.0651 -0.0361 738 VAL A O 5703 C CB . VAL A 738 ? 1.5295 1.4140 1.2591 0.5795 -0.1635 -0.0774 738 VAL A CB 5704 C CG1 . VAL A 738 ? 1.4785 1.3232 1.1947 0.5848 -0.1652 -0.0736 738 VAL A CG1 5705 C CG2 . VAL A 738 ? 1.7014 1.5282 1.4262 0.5808 -0.2180 -0.0896 738 VAL A CG2 5706 N N . LEU A 739 ? 1.3605 1.3000 1.1602 0.4755 -0.0628 -0.0234 739 LEU A N 5707 C CA . LEU A 739 ? 1.4393 1.4131 1.2549 0.4631 -0.0341 -0.0079 739 LEU A CA 5708 C C . LEU A 739 ? 1.4043 1.3172 1.2167 0.4477 -0.0395 -0.0085 739 LEU A C 5709 O O . LEU A 739 ? 1.3779 1.2488 1.2040 0.4141 -0.0423 -0.0059 739 LEU A O 5710 C CB . LEU A 739 ? 1.4393 1.4539 1.2946 0.4232 -0.0095 0.0117 739 LEU A CB 5711 C CG . LEU A 739 ? 1.4006 1.4562 1.2814 0.4064 0.0101 0.0318 739 LEU A CG 5712 C CD1 . LEU A 739 ? 1.4139 1.5469 1.2871 0.4411 0.0180 0.0431 739 LEU A CD1 5713 C CD2 . LEU A 739 ? 1.4855 1.5588 1.4077 0.3648 0.0195 0.0488 739 LEU A CD2 5714 N N . ALA A 740 ? 1.4001 1.3125 1.1939 0.4737 -0.0409 -0.0110 740 ALA A N 5715 C CA . ALA A 740 ? 1.4529 1.3035 1.2433 0.4604 -0.0465 -0.0101 740 ALA A CA 5716 C C . ALA A 740 ? 1.4960 1.3835 1.3004 0.4517 -0.0236 0.0019 740 ALA A C 5717 O O . ALA A 740 ? 1.5219 1.4537 1.3082 0.4865 -0.0209 0.0015 740 ALA A O 5718 C CB . ALA A 740 ? 1.3660 1.1535 1.1170 0.5003 -0.0839 -0.0251 740 ALA A CB 5719 N N . ALA A 741 ? 1.4153 1.2894 1.2528 0.4061 -0.0102 0.0123 741 ALA A N 5720 C CA . ALA A 741 ? 1.2857 1.1908 1.1445 0.3896 0.0043 0.0256 741 ALA A CA 5721 C C . ALA A 741 ? 1.2795 1.1151 1.1202 0.3933 -0.0053 0.0193 741 ALA A C 5722 O O . ALA A 741 ? 1.3399 1.1111 1.1895 0.3674 -0.0109 0.0162 741 ALA A O 5723 C CB . ALA A 741 ? 1.2376 1.1625 1.1448 0.3407 0.0146 0.0374 741 ALA A CB 5724 N N . VAL A 742 ? 1.2627 1.1157 1.0778 0.4275 -0.0075 0.0186 742 VAL A N 5725 C CA . VAL A 742 ? 1.2663 1.0468 1.0576 0.4387 -0.0207 0.0122 742 VAL A CA 5726 C C . VAL A 742 ? 1.2859 1.1026 1.0955 0.4218 -0.0060 0.0260 742 VAL A C 5727 O O . VAL A 742 ? 1.4333 1.3371 1.2413 0.4412 0.0043 0.0359 742 VAL A O 5728 C CB . VAL A 742 ? 1.3662 1.1195 1.1034 0.5013 -0.0467 -0.0049 742 VAL A CB 5729 C CG1 . VAL A 742 ? 1.2871 0.9405 1.0009 0.5098 -0.0694 -0.0097 742 VAL A CG1 5730 C CG2 . VAL A 742 ? 1.3398 1.0802 1.0653 0.5180 -0.0661 -0.0159 742 VAL A CG2 5731 N N . GLU A 743 ? 1.2457 1.0019 1.0758 0.3840 -0.0064 0.0290 743 GLU A N 5732 C CA . GLU A 743 ? 1.3451 1.1258 1.1969 0.3613 0.0019 0.0422 743 GLU A CA 5733 C C . GLU A 743 ? 1.3076 1.0022 1.1290 0.3756 -0.0105 0.0346 743 GLU A C 5734 O O . GLU A 743 ? 1.3792 0.9808 1.1816 0.3814 -0.0263 0.0244 743 GLU A O 5735 C CB . GLU A 743 ? 1.4645 1.2520 1.3752 0.2998 0.0074 0.0521 743 GLU A CB 5736 C CG . GLU A 743 ? 1.5359 1.2281 1.4552 0.2730 0.0002 0.0397 743 GLU A CG 5737 C CD . GLU A 743 ? 1.7268 1.4221 1.7013 0.2189 -0.0005 0.0438 743 GLU A CD 5738 O OE1 . GLU A 743 ? 1.9127 1.5449 1.8986 0.1972 -0.0050 0.0327 743 GLU A OE1 5739 O OE2 . GLU A 743 ? 1.6339 1.3990 1.6425 0.1988 -0.0008 0.0595 743 GLU A OE2 5740 N N . ILE A 744 ? 1.2143 0.9431 1.0323 0.3810 -0.0059 0.0436 744 ILE A N 5741 C CA . ILE A 744 ? 1.2488 0.8929 1.0440 0.3868 -0.0173 0.0389 744 ILE A CA 5742 C C . ILE A 744 ? 1.2785 0.9302 1.1224 0.3289 -0.0089 0.0544 744 ILE A C 5743 O O . ILE A 744 ? 1.2769 1.0274 1.1517 0.3103 0.0010 0.0730 744 ILE A O 5744 C CB . ILE A 744 ? 1.2625 0.9260 1.0010 0.4524 -0.0263 0.0309 744 ILE A CB 5745 C CG1 . ILE A 744 ? 1.2880 0.8510 1.0015 0.4586 -0.0419 0.0264 744 ILE A CG1 5746 C CG2 . ILE A 744 ? 1.2615 1.0674 1.0111 0.4614 -0.0074 0.0475 744 ILE A CG2 5747 C CD1 . ILE A 744 ? 1.4489 1.0119 1.0983 0.5327 -0.0594 0.0121 744 ILE A CD1 5748 N N . ARG A 745 ? 1.3120 0.8615 1.1675 0.2979 -0.0171 0.0495 745 ARG A N 5749 C CA . ARG A 745 ? 1.1237 0.6653 1.0281 0.2407 -0.0153 0.0594 745 ARG A CA 5750 C C . ARG A 745 ? 1.1470 0.5940 1.0282 0.2434 -0.0250 0.0571 745 ARG A C 5751 O O . ARG A 745 ? 1.3139 0.6788 1.1475 0.2828 -0.0372 0.0475 745 ARG A O 5752 C CB . ARG A 745 ? 1.0836 0.5969 1.0347 0.1934 -0.0167 0.0538 745 ARG A CB 5753 C CG . ARG A 745 ? 1.2486 0.8482 1.2257 0.1873 -0.0109 0.0562 745 ARG A CG 5754 C CD . ARG A 745 ? 1.2737 0.8463 1.2934 0.1465 -0.0160 0.0462 745 ARG A CD 5755 N NE . ARG A 745 ? 1.5485 1.0929 1.6127 0.0985 -0.0268 0.0468 745 ARG A NE 5756 C CZ . ARG A 745 ? 1.5943 1.2015 1.7108 0.0614 -0.0388 0.0584 745 ARG A CZ 5757 N NH1 . ARG A 745 ? 1.5732 1.2777 1.7041 0.0670 -0.0393 0.0748 745 ARG A NH1 5758 N NH2 . ARG A 745 ? 1.4815 1.0536 1.6395 0.0170 -0.0551 0.0562 745 ARG A NH2 5759 N N . GLY A 746 ? 1.1593 0.6140 1.0770 0.1999 -0.0249 0.0679 746 GLY A N 5760 C CA . GLY A 746 ? 1.1393 0.5038 1.0387 0.1973 -0.0338 0.0673 746 GLY A CA 5761 C C . GLY A 746 ? 1.1245 0.4683 1.0838 0.1282 -0.0381 0.0745 746 GLY A C 5762 O O . GLY A 746 ? 1.1774 0.6018 1.1920 0.0865 -0.0386 0.0840 746 GLY A O 5763 N N . VAL A 747 ? 1.0959 0.3461 1.0532 0.1132 -0.0426 0.0699 747 VAL A N 5764 C CA . VAL A 747 ? 1.1507 0.4241 1.1524 0.0471 -0.0276 0.0674 747 VAL A CA 5765 C C . VAL A 747 ? 1.2195 0.4978 1.2164 0.0437 -0.0037 0.0648 747 VAL A C 5766 O O . VAL A 747 ? 1.0186 0.3164 1.0297 0.0709 0.0013 0.0611 747 VAL A O 5767 C CB . VAL A 747 ? 1.1257 0.4166 1.1271 0.0172 -0.0064 0.0481 747 VAL A CB 5768 C CG1 . VAL A 747 ? 0.9864 0.3014 0.9867 0.0411 0.0213 0.0419 747 VAL A CG1 5769 C CG2 . VAL A 747 ? 1.1754 0.4939 1.1786 -0.0338 -0.0007 0.0368 747 VAL A CG2 5770 N N . SER A 748 ? 1.4874 0.7724 1.4844 0.0032 -0.0071 0.0668 748 SER A N 5771 C CA . SER A 748 ? 1.3535 0.6560 1.3449 -0.0013 0.0151 0.0612 748 SER A CA 5772 C C . SER A 748 ? 1.3196 0.6360 1.3120 -0.0391 0.0138 0.0440 748 SER A C 5773 O O . SER A 748 ? 1.3642 0.7008 1.3754 -0.0751 -0.0004 0.0390 748 SER A O 5774 C CB . SER A 748 ? 1.2637 0.5472 1.2604 -0.0149 -0.0133 0.0822 748 SER A CB 5775 O OG . SER A 748 ? 1.5595 0.8519 1.5511 -0.0125 0.0088 0.0756 748 SER A OG 5776 N N . SER A 749 ? 1.2305 0.5387 1.2258 -0.0280 0.0138 0.0403 749 SER A N 5777 C CA . SER A 749 ? 1.2164 0.5276 1.2180 -0.0524 0.0040 0.0315 749 SER A CA 5778 C C . SER A 749 ? 1.2937 0.5995 1.2987 -0.0561 -0.0027 0.0333 749 SER A C 5779 O O . SER A 749 ? 1.1151 0.4048 1.1152 -0.0361 -0.0033 0.0366 749 SER A O 5780 C CB . SER A 749 ? 1.2934 0.6007 1.2917 -0.0383 0.0073 0.0290 749 SER A CB 5781 O OG . SER A 749 ? 1.6424 0.9576 1.6499 -0.0582 -0.0024 0.0234 749 SER A OG 5782 N N . PRO A 750 ? 1.0243 0.3506 1.0447 -0.0826 -0.0147 0.0328 750 PRO A N 5783 C CA . PRO A 750 ? 1.1563 0.5187 1.2044 -0.1099 -0.0274 0.0324 750 PRO A CA 5784 C C . PRO A 750 ? 1.1733 0.5351 1.2164 -0.1110 -0.0223 0.0437 750 PRO A C 5785 O O . PRO A 750 ? 1.6066 0.9346 1.6212 -0.0837 -0.0063 0.0511 750 PRO A O 5786 C CB . PRO A 750 ? 1.3551 0.7478 1.4367 -0.1330 -0.0477 0.0312 750 PRO A CB 5787 C CG . PRO A 750 ? 1.2004 0.5640 1.2594 -0.1189 -0.0419 0.0317 750 PRO A CG 5788 C CD . PRO A 750 ? 0.9643 0.2885 0.9881 -0.0881 -0.0227 0.0349 750 PRO A CD 5789 N N . ASP A 751 ? 0.9455 0.3505 1.0255 -0.1392 -0.0377 0.0485 751 ASP A N 5790 C CA . ASP A 751 ? 1.1927 0.6107 1.2778 -0.1497 -0.0361 0.0674 751 ASP A CA 5791 C C . ASP A 751 ? 1.3904 0.8421 1.5052 -0.1762 -0.0524 0.0781 751 ASP A C 5792 O O . ASP A 751 ? 1.6522 1.1277 1.7838 -0.1928 -0.0590 0.1038 751 ASP A O 5793 C CB . ASP A 751 ? 1.2312 0.6940 1.3573 -0.1715 -0.0509 0.0751 751 ASP A CB 5794 C CG . ASP A 751 ? 1.4227 0.9372 1.5995 -0.1952 -0.0767 0.0634 751 ASP A CG 5795 O OD1 . ASP A 751 ? 1.6552 1.1736 1.8438 -0.1977 -0.0892 0.0568 751 ASP A OD1 5796 O OD2 . ASP A 751 ? 1.3486 0.8962 1.5555 -0.2068 -0.0885 0.0643 751 ASP A OD2 5797 N N . HIS A 752 ? 1.4487 0.9065 1.5773 -0.1806 -0.0660 0.0668 752 HIS A N 5798 C CA . HIS A 752 ? 1.2580 0.7451 1.4136 -0.2017 -0.0854 0.0764 752 HIS A CA 5799 C C . HIS A 752 ? 1.4731 0.9232 1.6016 -0.1858 -0.0791 0.0674 752 HIS A C 5800 O O . HIS A 752 ? 1.6626 1.0939 1.7805 -0.1716 -0.0755 0.0540 752 HIS A O 5801 C CB . HIS A 752 ? 1.0433 0.5848 1.2552 -0.2244 -0.1197 0.0789 752 HIS A CB 5802 C CG . HIS A 752 ? 1.5400 1.1395 1.7934 -0.2512 -0.1406 0.1009 752 HIS A CG 5803 N ND1 . HIS A 752 ? 1.6876 1.3275 1.9634 -0.2745 -0.1579 0.1259 752 HIS A ND1 5804 C CD2 . HIS A 752 ? 1.6754 1.3074 1.9546 -0.2599 -0.1498 0.1059 752 HIS A CD2 5805 C CE1 . HIS A 752 ? 1.5617 1.2634 1.8766 -0.2971 -0.1781 0.1491 752 HIS A CE1 5806 N NE2 . HIS A 752 ? 1.6872 1.3834 2.0054 -0.2883 -0.1738 0.1362 752 HIS A NE2 5807 N N . VAL A 753 ? 1.0083 0.4526 1.1283 -0.1902 -0.0786 0.0779 753 VAL A N 5808 C CA . VAL A 753 ? 1.0764 0.4999 1.1841 -0.1831 -0.0817 0.0720 753 VAL A CA 5809 C C . VAL A 753 ? 1.5415 1.0033 1.6810 -0.2102 -0.1053 0.0861 753 VAL A C 5810 O O . VAL A 753 ? 1.5116 0.9833 1.6493 -0.2213 -0.1029 0.1026 753 VAL A O 5811 C CB . VAL A 753 ? 1.0621 0.4277 1.1197 -0.1510 -0.0582 0.0697 753 VAL A CB 5812 C CG1 . VAL A 753 ? 1.1401 0.4925 1.1917 -0.1487 -0.0664 0.0661 753 VAL A CG1 5813 C CG2 . VAL A 753 ? 1.3216 0.6558 1.3547 -0.1211 -0.0414 0.0600 753 VAL A CG2 5814 N N . PHE A 754 ? 1.8110 1.2949 1.9797 -0.2197 -0.1287 0.0835 754 PHE A N 5815 C CA . PHE A 754 ? 1.5039 1.0235 1.7042 -0.2426 -0.1573 0.0998 754 PHE A CA 5816 C C . PHE A 754 ? 1.4940 0.9864 1.6704 -0.2375 -0.1534 0.0989 754 PHE A C 5817 O O . PHE A 754 ? 1.3762 0.8327 1.5279 -0.2181 -0.1414 0.0844 754 PHE A O 5818 C CB . PHE A 754 ? 1.1147 0.6625 1.3560 -0.2497 -0.1877 0.1005 754 PHE A CB 5819 C CG . PHE A 754 ? 0.8693 0.4470 1.1394 -0.2567 -0.1997 0.1048 754 PHE A CG 5820 C CD1 . PHE A 754 ? 1.4358 0.9982 1.6977 -0.2410 -0.1833 0.0869 754 PHE A CD1 5821 C CD2 . PHE A 754 ? 0.8692 0.4918 1.1742 -0.2798 -0.2302 0.1300 754 PHE A CD2 5822 C CE1 . PHE A 754 ? 1.4530 1.0411 1.7411 -0.2468 -0.1954 0.0897 754 PHE A CE1 5823 C CE2 . PHE A 754 ? 0.8603 0.5095 1.1920 -0.2856 -0.2447 0.1360 754 PHE A CE2 5824 C CZ . PHE A 754 ? 1.0321 0.6625 1.3557 -0.2684 -0.2265 0.1135 754 PHE A CZ 5825 N N . LEU A 755 ? 1.3223 0.8369 1.5082 -0.2568 -0.1664 0.1177 755 LEU A N 5826 C CA . LEU A 755 ? 1.4196 0.9081 1.5815 -0.2531 -0.1630 0.1180 755 LEU A CA 5827 C C . LEU A 755 ? 1.4827 1.0010 1.6748 -0.2720 -0.1972 0.1311 755 LEU A C 5828 O O . LEU A 755 ? 1.3506 0.9148 1.5800 -0.2933 -0.2258 0.1507 755 LEU A O 5829 C CB . LEU A 755 ? 1.4401 0.9203 1.5787 -0.2563 -0.1454 0.1309 755 LEU A CB 5830 C CG . LEU A 755 ? 1.5240 0.9523 1.6191 -0.2258 -0.1102 0.1208 755 LEU A CG 5831 C CD1 . LEU A 755 ? 1.4766 0.8823 1.5417 -0.2190 -0.0924 0.1389 755 LEU A CD1 5832 C CD2 . LEU A 755 ? 1.1122 0.4884 1.1765 -0.1930 -0.0991 0.0974 755 LEU A CD2 5833 N N . PRO A 756 ? 1.1278 0.6180 1.3024 -0.2631 -0.1973 0.1235 756 PRO A N 5834 C CA . PRO A 756 ? 1.1318 0.5686 1.2621 -0.2376 -0.1705 0.1060 756 PRO A CA 5835 C C . PRO A 756 ? 1.1616 0.5798 1.2867 -0.2181 -0.1614 0.0888 756 PRO A C 5836 O O . PRO A 756 ? 1.4498 0.8939 1.6057 -0.2232 -0.1735 0.0876 756 PRO A O 5837 C CB . PRO A 756 ? 1.4349 0.8627 1.5588 -0.2426 -0.1838 0.1107 756 PRO A CB 5838 C CG . PRO A 756 ? 1.6095 1.0776 1.7764 -0.2613 -0.2169 0.1223 756 PRO A CG 5839 C CD . PRO A 756 ? 0.9656 0.4751 1.1630 -0.2776 -0.2288 0.1362 756 PRO A CD 5840 N N . ILE A 757 ? 1.2878 0.6623 1.3752 -0.1957 -0.1435 0.0785 757 ILE A N 5841 C CA . ILE A 757 ? 1.6049 0.9648 1.6863 -0.1799 -0.1370 0.0676 757 ILE A CA 5842 C C . ILE A 757 ? 1.6879 1.0536 1.7841 -0.1838 -0.1537 0.0674 757 ILE A C 5843 O O . ILE A 757 ? 1.8040 1.1550 1.8873 -0.1842 -0.1606 0.0705 757 ILE A O 5844 C CB . ILE A 757 ? 1.7280 1.0414 1.7660 -0.1534 -0.1192 0.0621 757 ILE A CB 5845 C CG1 . ILE A 757 ? 1.5402 0.8432 1.5628 -0.1437 -0.1021 0.0634 757 ILE A CG1 5846 C CG2 . ILE A 757 ? 1.4445 0.7494 1.4805 -0.1415 -0.1174 0.0558 757 ILE A CG2 5847 C CD1 . ILE A 757 ? 1.4392 0.7654 1.4810 -0.1485 -0.0956 0.0607 757 ILE A CD1 5848 N N . PRO A 758 ? 1.7829 1.1690 1.9064 -0.1858 -0.1606 0.0640 758 PRO A N 5849 C CA . PRO A 758 ? 1.7780 1.1698 1.9188 -0.1877 -0.1758 0.0645 758 PRO A CA 5850 C C . PRO A 758 ? 1.3987 0.7563 1.5091 -0.1741 -0.1697 0.0620 758 PRO A C 5851 O O . PRO A 758 ? 1.3283 0.6642 1.4161 -0.1602 -0.1562 0.0578 758 PRO A O 5852 C CB . PRO A 758 ? 1.7889 1.2028 1.9595 -0.1873 -0.1789 0.0600 758 PRO A CB 5853 C CG . PRO A 758 ? 1.8240 1.2327 1.9803 -0.1808 -0.1601 0.0549 758 PRO A CG 5854 C CD . PRO A 758 ? 1.6584 1.0625 1.7987 -0.1856 -0.1552 0.0598 758 PRO A CD 5855 N N . ASN A 759 ? 1.6479 1.0008 1.7588 -0.1784 -0.1836 0.0663 759 ASN A N 5856 C CA . ASN A 759 ? 1.8238 1.1462 1.9093 -0.1677 -0.1853 0.0660 759 ASN A CA 5857 C C . ASN A 759 ? 1.8517 1.1360 1.8932 -0.1525 -0.1749 0.0644 759 ASN A C 5858 O O . ASN A 759 ? 1.6374 0.8997 1.6606 -0.1388 -0.1734 0.0629 759 ASN A O 5859 C CB . ASN A 759 ? 1.7255 1.0520 1.8252 -0.1623 -0.1866 0.0638 759 ASN A CB 5860 C CG . ASN A 759 ? 2.0074 1.3637 2.1479 -0.1726 -0.2013 0.0656 759 ASN A CG 5861 O OD1 . ASN A 759 ? 2.0140 1.3782 2.1656 -0.1814 -0.2161 0.0704 759 ASN A OD1 5862 N ND2 . ASN A 759 ? 1.9242 1.2959 2.0875 -0.1704 -0.1989 0.0622 759 ASN A ND2 5863 N N . TRP A 760 ? 2.1142 1.3903 2.1396 -0.1542 -0.1712 0.0660 760 TRP A N 5864 C CA . TRP A 760 ? 2.0911 1.3275 2.0734 -0.1357 -0.1648 0.0644 760 TRP A CA 5865 C C . TRP A 760 ? 1.8673 1.0804 1.8243 -0.1350 -0.1751 0.0674 760 TRP A C 5866 O O . TRP A 760 ? 1.7597 0.9918 1.7319 -0.1512 -0.1771 0.0718 760 TRP A O 5867 C CB . TRP A 760 ? 1.8802 1.1212 1.8601 -0.1318 -0.1473 0.0630 760 TRP A CB 5868 C CG . TRP A 760 ? 1.8267 1.0255 1.7621 -0.1076 -0.1436 0.0619 760 TRP A CG 5869 C CD1 . TRP A 760 ? 1.8445 1.0140 1.7512 -0.0833 -0.1452 0.0585 760 TRP A CD1 5870 C CD2 . TRP A 760 ? 1.8765 1.0561 1.7882 -0.1020 -0.1428 0.0647 760 TRP A CD2 5871 N NE1 . TRP A 760 ? 1.7097 0.8412 1.5723 -0.0592 -0.1491 0.0575 760 TRP A NE1 5872 C CE2 . TRP A 760 ? 1.7848 0.9207 1.6497 -0.0690 -0.1452 0.0612 760 TRP A CE2 5873 C CE3 . TRP A 760 ? 1.6666 0.8615 1.5903 -0.1207 -0.1435 0.0710 760 TRP A CE3 5874 C CZ2 . TRP A 760 ? 1.6066 0.7108 1.4330 -0.0487 -0.1468 0.0622 760 TRP A CZ2 5875 C CZ3 . TRP A 760 ? 1.6393 0.8051 1.5305 -0.1064 -0.1409 0.0742 760 TRP A CZ3 5876 C CH2 . TRP A 760 ? 1.5951 0.7143 1.4370 -0.0678 -0.1416 0.0693 760 TRP A CH2 5877 N N . GLU A 761 ? 1.5675 0.7383 1.4839 -0.1164 -0.1861 0.0658 761 GLU A N 5878 C CA . GLU A 761 ? 1.8340 0.9729 1.7149 -0.1103 -0.1975 0.0668 761 GLU A CA 5879 C C . GLU A 761 ? 1.9492 1.0402 1.7752 -0.0806 -0.2008 0.0622 761 GLU A C 5880 O O . GLU A 761 ? 2.0156 1.1020 1.8355 -0.0665 -0.1947 0.0593 761 GLU A O 5881 C CB . GLU A 761 ? 2.0714 1.1985 1.9466 -0.1142 -0.2194 0.0688 761 GLU A CB 5882 C CG . GLU A 761 ? 2.1589 1.2629 2.0168 -0.1007 -0.2347 0.0674 761 GLU A CG 5883 C CD . GLU A 761 ? 2.2675 1.3604 2.1219 -0.1059 -0.2581 0.0709 761 GLU A CD 5884 O OE1 . GLU A 761 ? 2.2174 1.2906 2.0584 -0.0975 -0.2762 0.0718 761 GLU A OE1 5885 O OE2 . GLU A 761 ? 2.2101 1.3144 2.0761 -0.1192 -0.2608 0.0737 761 GLU A OE2 5886 N N . HIS A 762 ? 2.0282 1.0815 1.8100 -0.0681 -0.2134 0.0610 762 HIS A N 5887 C CA . HIS A 762 ? 2.0134 1.0168 1.7325 -0.0327 -0.2213 0.0546 762 HIS A CA 5888 C C . HIS A 762 ? 1.9468 0.8953 1.6041 -0.0098 -0.2566 0.0483 762 HIS A C 5889 O O . HIS A 762 ? 2.2179 1.1441 1.8516 -0.0118 -0.2738 0.0481 762 HIS A O 5890 C CB . HIS A 762 ? 1.8766 0.8709 1.5791 -0.0266 -0.2110 0.0563 762 HIS A CB 5891 C CG . HIS A 762 ? 2.1370 1.0755 1.7630 0.0209 -0.2227 0.0474 762 HIS A CG 5892 N ND1 . HIS A 762 ? 2.2766 1.1790 1.8524 0.0423 -0.2309 0.0447 762 HIS A ND1 5893 C CD2 . HIS A 762 ? 2.1476 1.0601 1.7322 0.0571 -0.2306 0.0388 762 HIS A CD2 5894 C CE1 . HIS A 762 ? 2.2523 1.1089 1.7536 0.0959 -0.2443 0.0328 762 HIS A CE1 5895 N NE2 . HIS A 762 ? 2.2663 1.1289 1.7719 0.1049 -0.2457 0.0288 762 HIS A NE2 5896 N N . LYS A 763 ? 1.8599 0.7862 1.4902 0.0110 -0.2709 0.0432 763 LYS A N 5897 C CA . LYS A 763 ? 2.2742 1.1410 1.8349 0.0379 -0.3125 0.0352 763 LYS A CA 5898 C C . LYS A 763 ? 2.4063 1.2266 1.8927 0.0831 -0.3232 0.0225 763 LYS A C 5899 O O . LYS A 763 ? 2.6040 1.4373 2.0952 0.0977 -0.3060 0.0204 763 LYS A O 5900 C CB . LYS A 763 ? 2.3942 1.2634 1.9687 0.0340 -0.3298 0.0374 763 LYS A CB 5901 C CG . LYS A 763 ? 2.3333 1.2349 1.9615 0.0019 -0.3308 0.0474 763 LYS A CG 5902 C CD . LYS A 763 ? 2.4507 1.3100 2.0394 0.0058 -0.3718 0.0462 763 LYS A CD 5903 C CE . LYS A 763 ? 2.3452 1.2355 1.9858 -0.0204 -0.3764 0.0565 763 LYS A CE 5904 N NZ . LYS A 763 ? 2.3158 1.1640 1.9201 -0.0170 -0.4205 0.0563 763 LYS A NZ 5905 N N . GLU A 764 ? 2.3040 1.0703 1.7182 0.1097 -0.3531 0.0124 764 GLU A N 5906 C CA . GLU A 764 ? 2.5128 1.2367 1.8475 0.1628 -0.3636 -0.0032 764 GLU A CA 5907 C C . GLU A 764 ? 2.5230 1.2067 1.7968 0.2022 -0.4009 -0.0185 764 GLU A C 5908 O O . GLU A 764 ? 2.6778 1.3427 1.8956 0.2511 -0.4052 -0.0330 764 GLU A O 5909 C CB . GLU A 764 ? 2.6746 1.3543 1.9463 0.1835 -0.3836 -0.0117 764 GLU A CB 5910 C CG . GLU A 764 ? 2.7970 1.4295 2.0263 0.1827 -0.4326 -0.0177 764 GLU A CG 5911 C CD . GLU A 764 ? 2.9360 1.5255 2.1030 0.2027 -0.4505 -0.0264 764 GLU A CD 5912 O OE1 . GLU A 764 ? 3.0974 1.6341 2.2067 0.2158 -0.4991 -0.0368 764 GLU A OE1 5913 O OE2 . GLU A 764 ? 2.8048 1.4128 1.9814 0.2053 -0.4180 -0.0226 764 GLU A OE2 5914 N N . ASN A 765 ? 2.6695 1.8465 2.0042 0.2305 -0.9436 -0.1407 765 ASN A N 5915 C CA . ASN A 765 ? 2.6177 1.7702 2.0113 0.1849 -0.9650 -0.1517 765 ASN A CA 5916 C C . ASN A 765 ? 2.4080 1.7017 2.0137 0.1325 -0.9416 -0.1014 765 ASN A C 5917 O O . ASN A 765 ? 2.4493 1.7702 2.1583 0.0757 -1.0167 -0.0809 765 ASN A O 5918 C CB . ASN A 765 ? 2.8025 1.8398 2.1274 0.1598 -1.0929 -0.1819 765 ASN A CB 5919 C CG . ASN A 765 ? 3.0465 1.9312 2.1392 0.2228 -1.1157 -0.2390 765 ASN A CG 5920 O OD1 . ASN A 765 ? 3.1914 2.0534 2.2040 0.2542 -1.1369 -0.2420 765 ASN A OD1 5921 N ND2 . ASN A 765 ? 2.9478 1.7388 1.9453 0.2459 -1.0890 -0.2785 765 ASN A ND2 5922 N N . PRO A 766 ? 2.1036 1.4881 1.7723 0.1526 -0.8395 -0.0782 766 PRO A N 5923 C CA . PRO A 766 ? 1.9860 1.5132 1.8380 0.1222 -0.8057 -0.0302 766 PRO A CA 5924 C C . PRO A 766 ? 1.8137 1.3586 1.7495 0.0773 -0.7928 -0.0221 766 PRO A C 5925 O O . PRO A 766 ? 1.8511 1.3207 1.7098 0.0891 -0.7521 -0.0529 766 PRO A O 5926 C CB . PRO A 766 ? 1.9737 1.5462 1.8149 0.1701 -0.7068 -0.0222 766 PRO A CB 5927 C CG . PRO A 766 ? 1.8206 1.2826 1.5097 0.2021 -0.6668 -0.0625 766 PRO A CG 5928 C CD . PRO A 766 ? 1.9853 1.3336 1.5493 0.2047 -0.7491 -0.0972 766 PRO A CD 5929 N N . GLU A 767 ? 1.8181 1.4676 1.9119 0.0276 -0.8266 0.0238 767 GLU A N 5930 C CA . GLU A 767 ? 1.8562 1.5771 2.0579 -0.0015 -0.7761 0.0511 767 GLU A CA 5931 C C . GLU A 767 ? 1.7207 1.6165 2.0720 0.0061 -0.7316 0.1062 767 GLU A C 5932 O O . GLU A 767 ? 1.9606 1.9580 2.4345 -0.0263 -0.7836 0.1525 767 GLU A O 5933 C CB . GLU A 767 ? 2.1020 1.7822 2.3510 -0.0703 -0.8543 0.0620 767 GLU A CB 5934 C CG . GLU A 767 ? 2.2252 1.9604 2.5796 -0.1255 -0.9600 0.1036 767 GLU A CG 5935 C CD . GLU A 767 ? 2.4551 2.0923 2.6970 -0.1090 -1.0443 0.0686 767 GLU A CD 5936 O OE1 . GLU A 767 ? 2.6444 2.1420 2.7089 -0.0629 -1.0348 0.0079 767 GLU A OE1 5937 O OE2 . GLU A 767 ? 2.4428 2.1502 2.7742 -0.1394 -1.1194 0.1052 767 GLU A OE2 5938 N N . THR A 768 ? 1.5676 1.4978 1.9055 0.0535 -0.6379 0.1015 768 THR A N 5939 C CA . THR A 768 ? 1.4798 1.5568 1.9291 0.0805 -0.5913 0.1437 768 THR A CA 5940 C C . THR A 768 ? 1.3901 1.5043 1.8573 0.1043 -0.4989 0.1458 768 THR A C 5941 O O . THR A 768 ? 1.5873 1.8187 2.1705 0.0923 -0.4735 0.1877 768 THR A O 5942 C CB . THR A 768 ? 1.6129 1.6884 2.0125 0.1335 -0.5914 0.1358 768 THR A CB 5943 O OG1 . THR A 768 ? 1.7531 1.7313 2.0627 0.1221 -0.6676 0.1111 768 THR A OG1 5944 C CG2 . THR A 768 ? 1.5206 1.7551 2.0580 0.1489 -0.5951 0.1876 768 THR A CG2 5945 N N . GLU A 769 ? 1.3130 1.3275 1.6607 0.1387 -0.4526 0.1032 769 GLU A N 5946 C CA . GLU A 769 ? 1.2996 1.3212 1.6286 0.1767 -0.3708 0.0949 769 GLU A CA 5947 C C . GLU A 769 ? 1.3094 1.3680 1.6354 0.2323 -0.3487 0.1019 769 GLU A C 5948 O O . GLU A 769 ? 1.2776 1.3027 1.5543 0.2691 -0.2972 0.0868 769 GLU A O 5949 C CB . GLU A 769 ? 1.3104 1.4201 1.7348 0.1603 -0.3332 0.1235 769 GLU A CB 5950 C CG . GLU A 769 ? 1.2996 1.4119 1.6989 0.2019 -0.2575 0.1129 769 GLU A CG 5951 C CD . GLU A 769 ? 1.4202 1.6221 1.9028 0.1907 -0.2220 0.1433 769 GLU A CD 5952 O OE1 . GLU A 769 ? 1.4442 1.7033 1.9428 0.2370 -0.1718 0.1517 769 GLU A OE1 5953 O OE2 . GLU A 769 ? 1.5389 1.7467 2.0629 0.1383 -0.2466 0.1593 769 GLU A OE2 5954 N N . GLU A 770 ? 1.3564 1.4734 1.7306 0.2381 -0.3955 0.1247 770 GLU A N 5955 C CA . GLU A 770 ? 1.4703 1.5953 1.8207 0.2932 -0.3889 0.1270 770 GLU A CA 5956 C C . GLU A 770 ? 1.6584 1.6601 1.8810 0.3001 -0.4149 0.0979 770 GLU A C 5957 O O . GLU A 770 ? 1.7099 1.6614 1.8661 0.3403 -0.3887 0.0889 770 GLU A O 5958 C CB . GLU A 770 ? 1.6686 1.9229 2.1323 0.3037 -0.4261 0.1689 770 GLU A CB 5959 C CG . GLU A 770 ? 1.9301 2.2043 2.3810 0.3716 -0.4155 0.1748 770 GLU A CG 5960 C CD . GLU A 770 ? 1.9309 2.2562 2.4082 0.4263 -0.3482 0.1799 770 GLU A CD 5961 O OE1 . GLU A 770 ? 1.7661 2.1213 2.2742 0.4102 -0.3072 0.1814 770 GLU A OE1 5962 O OE2 . GLU A 770 ? 1.9138 2.2415 2.3728 0.4895 -0.3400 0.1813 770 GLU A OE2 5963 N N . ASP A 771 ? 1.7121 1.6619 1.8961 0.2618 -0.4697 0.0857 771 ASP A N 5964 C CA . ASP A 771 ? 1.8496 1.6945 1.9070 0.2732 -0.5001 0.0623 771 ASP A CA 5965 C C . ASP A 771 ? 1.7107 1.4536 1.6541 0.2792 -0.4538 0.0319 771 ASP A C 5966 O O . ASP A 771 ? 1.7291 1.3985 1.5644 0.3010 -0.4554 0.0210 771 ASP A O 5967 C CB . ASP A 771 ? 2.0855 1.9064 2.1319 0.2379 -0.5846 0.0573 771 ASP A CB 5968 C CG . ASP A 771 ? 2.2762 2.2036 2.4376 0.2300 -0.6407 0.0943 771 ASP A CG 5969 O OD1 . ASP A 771 ? 2.2683 2.3040 2.5303 0.2534 -0.6054 0.1249 771 ASP A OD1 5970 O OD2 . ASP A 771 ? 2.3845 2.2888 2.5349 0.2033 -0.7228 0.0932 771 ASP A OD2 5971 N N . VAL A 772 ? 1.5659 1.3128 1.5363 0.2609 -0.4123 0.0237 772 VAL A N 5972 C CA . VAL A 772 ? 1.5824 1.2523 1.4638 0.2678 -0.3654 0.0008 772 VAL A CA 5973 C C . VAL A 772 ? 1.5494 1.2187 1.4184 0.2999 -0.3134 0.0112 772 VAL A C 5974 O O . VAL A 772 ? 1.7981 1.4095 1.5810 0.3185 -0.3030 0.0104 772 VAL A O 5975 C CB . VAL A 772 ? 1.5106 1.1825 1.4257 0.2393 -0.3424 -0.0102 772 VAL A CB 5976 C CG1 . VAL A 772 ? 1.5694 1.1719 1.3973 0.2504 -0.2966 -0.0310 772 VAL A CG1 5977 C CG2 . VAL A 772 ? 1.4968 1.1553 1.4272 0.2030 -0.4047 -0.0172 772 VAL A CG2 5978 N N . GLY A 773 ? 1.2784 1.0094 1.2299 0.3071 -0.2838 0.0235 773 GLY A N 5979 C CA . GLY A 773 ? 1.2433 0.9593 1.1818 0.3385 -0.2462 0.0299 773 GLY A CA 5980 C C . GLY A 773 ? 1.1724 0.9440 1.1837 0.3469 -0.2119 0.0332 773 GLY A C 5981 O O . GLY A 773 ? 1.1487 0.9885 1.2320 0.3286 -0.2147 0.0390 773 GLY A O 5982 N N . PRO A 774 ? 1.1508 0.8888 1.1390 0.3747 -0.1828 0.0318 774 PRO A N 5983 C CA . PRO A 774 ? 1.2195 0.9961 1.2534 0.3947 -0.1517 0.0304 774 PRO A CA 5984 C C . PRO A 774 ? 1.1914 0.9722 1.2381 0.3615 -0.1246 0.0196 774 PRO A C 5985 O O . PRO A 774 ? 1.0898 0.8266 1.0987 0.3290 -0.1258 0.0100 774 PRO A O 5986 C CB . PRO A 774 ? 1.2375 0.9362 1.2144 0.4265 -0.1425 0.0259 774 PRO A CB 5987 C CG . PRO A 774 ? 1.2697 0.8917 1.1777 0.4009 -0.1517 0.0281 774 PRO A CG 5988 C CD . PRO A 774 ? 1.2757 0.9282 1.1857 0.3867 -0.1818 0.0338 774 PRO A CD 5989 N N . VAL A 775 ? 1.2973 1.1319 1.3912 0.3761 -0.0997 0.0221 775 VAL A N 5990 C CA . VAL A 775 ? 1.0660 0.9075 1.1738 0.3472 -0.0757 0.0156 775 VAL A CA 5991 C C . VAL A 775 ? 1.1591 0.9270 1.2122 0.3545 -0.0514 -0.0018 775 VAL A C 5992 O O . VAL A 775 ? 1.2249 0.9814 1.2652 0.3924 -0.0403 -0.0062 775 VAL A O 5993 C CB . VAL A 775 ? 0.9620 0.9071 1.1477 0.3567 -0.0595 0.0347 775 VAL A CB 5994 C CG1 . VAL A 775 ? 1.0173 0.9610 1.2109 0.3260 -0.0372 0.0312 775 VAL A CG1 5995 C CG2 . VAL A 775 ? 1.0209 1.0520 1.2803 0.3409 -0.0900 0.0618 775 VAL A CG2 5996 N N . VAL A 776 ? 1.2433 0.9600 1.2623 0.3208 -0.0473 -0.0111 776 VAL A N 5997 C CA . VAL A 776 ? 1.0365 0.6978 1.0207 0.3174 -0.0281 -0.0211 776 VAL A CA 5998 C C . VAL A 776 ? 1.2077 0.8971 1.2191 0.2997 -0.0081 -0.0263 776 VAL A C 5999 O O . VAL A 776 ? 1.3038 1.0160 1.3352 0.2733 -0.0118 -0.0249 776 VAL A O 6000 C CB . VAL A 776 ? 1.3421 0.9452 1.2779 0.2966 -0.0313 -0.0193 776 VAL A CB 6001 C CG1 . VAL A 776 ? 1.3796 0.9418 1.2989 0.2862 -0.0154 -0.0212 776 VAL A CG1 6002 C CG2 . VAL A 776 ? 1.5794 1.1519 1.4838 0.3127 -0.0521 -0.0076 776 VAL A CG2 6003 N N . GLN A 777 ? 1.3939 1.0719 1.3988 0.3160 0.0074 -0.0328 777 GLN A N 6004 C CA . GLN A 777 ? 1.1879 0.8966 1.2159 0.3056 0.0262 -0.0341 777 GLN A CA 6005 C C . GLN A 777 ? 1.1878 0.8415 1.1835 0.2978 0.0341 -0.0457 777 GLN A C 6006 O O . GLN A 777 ? 1.3484 0.9600 1.3133 0.3208 0.0291 -0.0538 777 GLN A O 6007 C CB . GLN A 777 ? 1.1510 0.9244 1.2073 0.3406 0.0387 -0.0256 777 GLN A CB 6008 C CG . GLN A 777 ? 1.1625 0.9891 1.2525 0.3275 0.0583 -0.0144 777 GLN A CG 6009 C CD . GLN A 777 ? 1.4304 1.3419 1.5506 0.3675 0.0772 0.0042 777 GLN A CD 6010 O OE1 . GLN A 777 ? 1.5800 1.5187 1.7034 0.4069 0.0741 0.0077 777 GLN A OE1 6011 N NE2 . GLN A 777 ? 1.4190 1.3780 1.5601 0.3621 0.0986 0.0198 777 GLN A NE2 6012 N N . HIS A 778 ? 1.0886 0.7382 1.0902 0.2672 0.0408 -0.0465 778 HIS A N 6013 C CA . HIS A 778 ? 1.0386 0.6539 1.0244 0.2576 0.0471 -0.0525 778 HIS A CA 6014 C C . HIS A 778 ? 1.0580 0.7023 1.0604 0.2578 0.0605 -0.0535 778 HIS A C 6015 O O . HIS A 778 ? 1.4005 1.0798 1.4301 0.2429 0.0652 -0.0464 778 HIS A O 6016 C CB . HIS A 778 ? 0.8679 0.4658 0.8473 0.2328 0.0489 -0.0490 778 HIS A CB 6017 C CG . HIS A 778 ? 1.0897 0.6597 1.0472 0.2314 0.0400 -0.0394 778 HIS A CG 6018 N ND1 . HIS A 778 ? 1.2802 0.8409 1.2297 0.2159 0.0465 -0.0270 778 HIS A ND1 6019 C CD2 . HIS A 778 ? 1.3356 0.8900 1.2786 0.2451 0.0259 -0.0347 778 HIS A CD2 6020 C CE1 . HIS A 778 ? 1.2049 0.7460 1.1356 0.2160 0.0379 -0.0115 778 HIS A CE1 6021 N NE2 . HIS A 778 ? 1.4226 0.9521 1.3461 0.2333 0.0228 -0.0180 778 HIS A NE2 6022 N N . ILE A 779 ? 0.9846 0.6067 0.9653 0.2742 0.0611 -0.0610 779 ILE A N 6023 C CA . ILE A 779 ? 1.0479 0.6938 1.0328 0.2783 0.0740 -0.0597 779 ILE A CA 6024 C C . ILE A 779 ? 1.1673 0.7720 1.1362 0.2643 0.0671 -0.0669 779 ILE A C 6025 O O . ILE A 779 ? 0.9627 0.5174 0.9041 0.2701 0.0488 -0.0756 779 ILE A O 6026 C CB . ILE A 779 ? 1.2069 0.8727 1.1697 0.3222 0.0816 -0.0617 779 ILE A CB 6027 C CG1 . ILE A 779 ? 1.3688 1.0791 1.3513 0.3439 0.0849 -0.0525 779 ILE A CG1 6028 C CG2 . ILE A 779 ? 1.0477 0.7596 1.0200 0.3253 0.1013 -0.0491 779 ILE A CG2 6029 C CD1 . ILE A 779 ? 1.3529 1.1325 1.3957 0.3159 0.0923 -0.0290 779 ILE A CD1 6030 N N . TYR A 780 ? 1.1534 0.7759 1.1422 0.2449 0.0759 -0.0608 780 TYR A N 6031 C CA . TYR A 780 ? 0.7754 0.3730 0.7586 0.2339 0.0692 -0.0638 780 TYR A CA 6032 C C . TYR A 780 ? 0.8968 0.5060 0.8684 0.2450 0.0753 -0.0621 780 TYR A C 6033 O O . TYR A 780 ? 0.8390 0.4860 0.8263 0.2444 0.0902 -0.0496 780 TYR A O 6034 C CB . TYR A 780 ? 0.8012 0.4056 0.8091 0.2116 0.0736 -0.0582 780 TYR A CB 6035 C CG . TYR A 780 ? 0.9992 0.5951 1.0093 0.2039 0.0705 -0.0548 780 TYR A CG 6036 C CD1 . TYR A 780 ? 1.0495 0.6308 1.0646 0.1938 0.0606 -0.0465 780 TYR A CD1 6037 C CD2 . TYR A 780 ? 1.0441 0.6495 1.0528 0.2045 0.0743 -0.0545 780 TYR A CD2 6038 C CE1 . TYR A 780 ? 1.0643 0.6471 1.0834 0.1853 0.0612 -0.0330 780 TYR A CE1 6039 C CE2 . TYR A 780 ? 1.3167 0.9154 1.3179 0.2012 0.0732 -0.0479 780 TYR A CE2 6040 C CZ . TYR A 780 ? 1.2541 0.8446 1.2606 0.1920 0.0700 -0.0348 780 TYR A CZ 6041 O OH . TYR A 780 ? 1.1668 0.7596 1.1680 0.1870 0.0723 -0.0182 780 TYR A OH 6042 N N . GLU A 781 ? 0.8848 0.4602 0.8284 0.2528 0.0596 -0.0707 781 GLU A N 6043 C CA . GLU A 781 ? 0.8399 0.4205 0.7577 0.2687 0.0630 -0.0694 781 GLU A CA 6044 C C . GLU A 781 ? 1.0017 0.5596 0.9223 0.2534 0.0452 -0.0700 781 GLU A C 6045 O O . GLU A 781 ? 1.4059 0.9257 1.3189 0.2467 0.0174 -0.0782 781 GLU A O 6046 C CB . GLU A 781 ? 0.9040 0.4620 0.7617 0.3103 0.0564 -0.0831 781 GLU A CB 6047 C CG . GLU A 781 ? 1.1332 0.6953 0.9475 0.3346 0.0607 -0.0812 781 GLU A CG 6048 C CD . GLU A 781 ? 1.4825 1.0133 1.2165 0.3892 0.0529 -0.1002 781 GLU A CD 6049 O OE1 . GLU A 781 ? 1.4957 1.0504 1.1864 0.4221 0.0693 -0.0933 781 GLU A OE1 6050 O OE2 . GLU A 781 ? 1.7556 1.2538 1.4746 0.3879 0.0283 -0.1165 781 GLU A OE2 6051 N N . LEU A 782 ? 0.8880 0.4696 0.8238 0.2463 0.0570 -0.0574 782 LEU A N 6052 C CA . LEU A 782 ? 0.8338 0.4021 0.7738 0.2382 0.0407 -0.0554 782 LEU A CA 6053 C C . LEU A 782 ? 1.0204 0.5774 0.9090 0.2613 0.0350 -0.0555 782 LEU A C 6054 O O . LEU A 782 ? 1.4398 1.0238 1.3210 0.2689 0.0561 -0.0394 782 LEU A O 6055 C CB . LEU A 782 ? 0.7980 0.3873 0.7784 0.2226 0.0526 -0.0427 782 LEU A CB 6056 C CG . LEU A 782 ? 0.8841 0.4695 0.8768 0.2202 0.0385 -0.0373 782 LEU A CG 6057 C CD1 . LEU A 782 ? 0.7999 0.3882 0.8217 0.2101 0.0201 -0.0391 782 LEU A CD1 6058 C CD2 . LEU A 782 ? 0.8184 0.4106 0.8330 0.2172 0.0498 -0.0278 782 LEU A CD2 6059 N N . ARG A 783 ? 0.9502 0.4649 0.8000 0.2716 0.0028 -0.0706 783 ARG A N 6060 C CA . ARG A 783 ? 1.2849 0.7789 1.0642 0.3031 -0.0064 -0.0759 783 ARG A CA 6061 C C . ARG A 783 ? 1.0328 0.5007 0.8056 0.2946 -0.0419 -0.0764 783 ARG A C 6062 O O . ARG A 783 ? 1.0378 0.4805 0.8369 0.2732 -0.0781 -0.0828 783 ARG A O 6063 C CB . ARG A 783 ? 1.4424 0.8913 1.1499 0.3390 -0.0220 -0.1003 783 ARG A CB 6064 C CG . ARG A 783 ? 1.1662 0.5961 0.7801 0.3870 -0.0248 -0.1079 783 ARG A CG 6065 C CD . ARG A 783 ? 1.2803 0.6842 0.8184 0.4400 -0.0216 -0.1294 783 ARG A CD 6066 N NE . ARG A 783 ? 1.4226 0.8146 0.8574 0.4982 -0.0181 -0.1361 783 ARG A NE 6067 C CZ . ARG A 783 ? 1.4205 0.8903 0.8412 0.5293 0.0339 -0.1083 783 ARG A CZ 6068 N NH1 . ARG A 783 ? 1.3178 0.8752 0.8273 0.5011 0.0786 -0.0731 783 ARG A NH1 6069 N NH2 . ARG A 783 ? 1.5721 1.0330 0.8884 0.5885 0.0386 -0.1122 783 ARG A NH2 6070 N N . ASN A 784 ? 1.0658 0.5457 0.8087 0.3094 -0.0330 -0.0637 784 ASN A N 6071 C CA . ASN A 784 ? 1.1313 0.5858 0.8563 0.3087 -0.0697 -0.0637 784 ASN A CA 6072 C C . ASN A 784 ? 1.2518 0.6525 0.8713 0.3477 -0.0985 -0.0842 784 ASN A C 6073 O O . ASN A 784 ? 1.3382 0.7505 0.8920 0.3843 -0.0716 -0.0783 784 ASN A O 6074 C CB . ASN A 784 ? 1.1030 0.5911 0.8498 0.3042 -0.0496 -0.0363 784 ASN A CB 6075 C CG . ASN A 784 ? 1.2347 0.6998 0.9618 0.3077 -0.0890 -0.0342 784 ASN A CG 6076 O OD1 . ASN A 784 ? 1.2771 0.7112 1.0022 0.3012 -0.1353 -0.0501 784 ASN A OD1 6077 N ND2 . ASN A 784 ? 1.3441 0.8228 1.0599 0.3150 -0.0762 -0.0105 784 ASN A ND2 6078 N N . ASN A 785 ? 1.2590 0.6007 0.8605 0.3407 -0.1560 -0.1057 785 ASN A N 6079 C CA . ASN A 785 ? 1.4478 0.7128 0.9341 0.3806 -0.1990 -0.1339 785 ASN A CA 6080 C C . ASN A 785 ? 1.6998 0.9419 1.1510 0.3841 -0.2399 -0.1307 785 ASN A C 6081 O O . ASN A 785 ? 1.9231 1.1503 1.2772 0.4288 -0.2335 -0.1338 785 ASN A O 6082 C CB . ASN A 785 ? 1.4396 0.6300 0.9136 0.3702 -0.2522 -0.1610 785 ASN A CB 6083 C CG . ASN A 785 ? 1.6747 0.8635 1.1321 0.3920 -0.2188 -0.1728 785 ASN A CG 6084 O OD1 . ASN A 785 ? 1.6115 0.8396 1.1550 0.3580 -0.1957 -0.1591 785 ASN A OD1 6085 N ND2 . ASN A 785 ? 1.6448 0.7922 0.9867 0.4555 -0.2145 -0.1972 785 ASN A ND2 6086 N N . GLY A 786 ? 1.8109 1.0577 1.3421 0.3396 -0.2813 -0.1206 786 GLY A N 6087 C CA . GLY A 786 ? 1.5802 0.8028 1.0896 0.3383 -0.3350 -0.1179 786 GLY A CA 6088 C C . GLY A 786 ? 1.5393 0.7947 1.0086 0.3666 -0.3002 -0.0990 786 GLY A C 6089 O O . GLY A 786 ? 1.8374 1.1522 1.3421 0.3674 -0.2355 -0.0766 786 GLY A O 6090 N N . PRO A 787 ? 1.6267 0.8375 1.0198 0.3876 -0.3492 -0.1053 787 PRO A N 6091 C CA . PRO A 787 ? 1.7068 0.9268 1.0198 0.4263 -0.3250 -0.0894 787 PRO A CA 6092 C C . PRO A 787 ? 1.5898 0.8874 0.9879 0.4072 -0.2707 -0.0475 787 PRO A C 6093 O O . PRO A 787 ? 1.6116 0.9377 0.9719 0.4293 -0.2173 -0.0256 787 PRO A O 6094 C CB . PRO A 787 ? 1.7400 0.9016 0.9973 0.4330 -0.4061 -0.1006 787 PRO A CB 6095 C CG . PRO A 787 ? 1.7004 0.8588 1.0645 0.3802 -0.4633 -0.1050 787 PRO A CG 6096 C CD . PRO A 787 ? 1.6654 0.8210 1.0633 0.3655 -0.4387 -0.1198 787 PRO A CD 6097 N N . SER A 788 ? 1.4554 0.7866 0.9672 0.3682 -0.2862 -0.0338 788 SER A N 6098 C CA . SER A 788 ? 1.4545 0.8389 1.0368 0.3566 -0.2463 -0.0002 788 SER A CA 6099 C C . SER A 788 ? 1.4136 0.8347 1.0443 0.3440 -0.1841 0.0068 788 SER A C 6100 O O . SER A 788 ? 1.3257 0.7501 0.9873 0.3301 -0.1780 -0.0117 788 SER A O 6101 C CB . SER A 788 ? 1.7758 1.1899 1.4596 0.3315 -0.2804 0.0101 788 SER A CB 6102 O OG . SER A 788 ? 2.0259 1.4105 1.6752 0.3383 -0.3469 0.0059 788 SER A OG 6103 N N . SER A 789 ? 1.3491 0.7920 0.9849 0.3466 -0.1441 0.0361 789 SER A N 6104 C CA . SER A 789 ? 1.3551 0.8280 1.0417 0.3298 -0.0957 0.0459 789 SER A CA 6105 C C . SER A 789 ? 1.2892 0.7786 1.0688 0.3085 -0.0957 0.0512 789 SER A C 6106 O O . SER A 789 ? 1.2370 0.7270 1.0468 0.3101 -0.1273 0.0519 789 SER A O 6107 C CB . SER A 789 ? 1.3497 0.8349 0.9951 0.3388 -0.0585 0.0806 789 SER A CB 6108 O OG . SER A 789 ? 1.3947 0.8650 1.0182 0.3458 -0.0737 0.1083 789 SER A OG 6109 N N . PHE A 790 ? 1.1900 0.6943 1.0119 0.2935 -0.0623 0.0549 790 PHE A N 6110 C CA . PHE A 790 ? 1.0836 0.5930 0.9716 0.2856 -0.0604 0.0577 790 PHE A CA 6111 C C . PHE A 790 ? 1.1315 0.6273 1.0251 0.2749 -0.0349 0.0754 790 PHE A C 6112 O O . PHE A 790 ? 1.2078 0.7137 1.0878 0.2637 -0.0118 0.0809 790 PHE A O 6113 C CB . PHE A 790 ? 1.0311 0.5674 0.9755 0.2770 -0.0611 0.0356 790 PHE A CB 6114 C CG . PHE A 790 ? 0.9666 0.5103 0.9118 0.2640 -0.0356 0.0229 790 PHE A CG 6115 C CD1 . PHE A 790 ? 1.0650 0.6084 1.0334 0.2562 -0.0112 0.0245 790 PHE A CD1 6116 C CD2 . PHE A 790 ? 1.0086 0.5512 0.9276 0.2622 -0.0429 0.0077 790 PHE A CD2 6117 C CE1 . PHE A 790 ? 0.8977 0.4510 0.8689 0.2451 0.0081 0.0144 790 PHE A CE1 6118 C CE2 . PHE A 790 ? 1.1131 0.6618 1.0334 0.2548 -0.0214 -0.0030 790 PHE A CE2 6119 C CZ . PHE A 790 ? 0.9073 0.4674 0.8574 0.2453 0.0053 0.0020 790 PHE A CZ 6120 N N . SER A 791 ? 1.3425 0.8126 1.2567 0.2797 -0.0446 0.0859 791 SER A N 6121 C CA . SER A 791 ? 1.1614 0.5962 1.0751 0.2661 -0.0371 0.1061 791 SER A CA 6122 C C . SER A 791 ? 1.0730 0.5031 1.0188 0.2553 -0.0252 0.0869 791 SER A C 6123 O O . SER A 791 ? 1.1125 0.5318 1.0581 0.2320 -0.0165 0.1010 791 SER A O 6124 C CB . SER A 791 ? 1.1996 0.5864 1.1086 0.2810 -0.0618 0.1223 791 SER A CB 6125 O OG . SER A 791 ? 1.5769 0.9736 1.5160 0.3088 -0.0746 0.0991 791 SER A OG 6126 N N . LYS A 792 ? 1.0184 0.4622 0.9929 0.2723 -0.0261 0.0593 792 LYS A N 6127 C CA . LYS A 792 ? 1.1292 0.5636 1.1204 0.2706 -0.0163 0.0399 792 LYS A CA 6128 C C . LYS A 792 ? 1.1997 0.6865 1.2195 0.2782 -0.0023 0.0176 792 LYS A C 6129 O O . LYS A 792 ? 1.2737 0.7973 1.3162 0.2925 -0.0080 0.0165 792 LYS A O 6130 C CB . LYS A 792 ? 1.0565 0.4321 1.0408 0.2942 -0.0335 0.0348 792 LYS A CB 6131 C CG . LYS A 792 ? 1.1423 0.4449 1.1010 0.2748 -0.0540 0.0578 792 LYS A CG 6132 C CD . LYS A 792 ? 1.4063 0.6514 1.3548 0.2938 -0.0744 0.0433 792 LYS A CD 6133 C CE . LYS A 792 ? 1.4763 0.6419 1.4038 0.2639 -0.1031 0.0693 792 LYS A CE 6134 N NZ . LYS A 792 ? 1.5525 0.6684 1.4620 0.2796 -0.1236 0.0490 792 LYS A NZ 6135 N N . ALA A 793 ? 1.1440 0.6361 1.1669 0.2656 0.0124 0.0054 793 ALA A N 6136 C CA . ALA A 793 ? 1.2483 0.7855 1.2962 0.2699 0.0260 -0.0093 793 ALA A CA 6137 C C . ALA A 793 ? 1.1743 0.6955 1.2146 0.2712 0.0367 -0.0241 793 ALA A C 6138 O O . ALA A 793 ? 1.0936 0.5719 1.1131 0.2578 0.0300 -0.0238 793 ALA A O 6139 C CB . ALA A 793 ? 0.8427 0.4101 0.8924 0.2504 0.0285 -0.0078 793 ALA A CB 6140 N N . MET A 794 ? 0.9346 0.4938 0.9931 0.2859 0.0504 -0.0326 794 MET A N 6141 C CA . MET A 794 ? 0.8656 0.4127 0.9066 0.2931 0.0607 -0.0474 794 MET A CA 6142 C C . MET A 794 ? 1.0445 0.6326 1.1014 0.2727 0.0742 -0.0457 794 MET A C 6143 O O . MET A 794 ? 0.9042 0.5365 0.9920 0.2640 0.0764 -0.0342 794 MET A O 6144 C CB . MET A 794 ? 0.8994 0.4621 0.9371 0.3337 0.0680 -0.0557 794 MET A CB 6145 C CG . MET A 794 ? 0.9823 0.5049 1.0023 0.3499 0.0482 -0.0612 794 MET A CG 6146 S SD . MET A 794 ? 1.4214 0.8548 1.3985 0.3232 0.0208 -0.0715 794 MET A SD 6147 C CE . MET A 794 ? 1.0280 0.4632 0.9744 0.3323 0.0289 -0.0938 794 MET A CE 6148 N N . LEU A 795 ? 0.9418 0.5082 0.9766 0.2639 0.0763 -0.0558 795 LEU A N 6149 C CA . LEU A 795 ? 0.8533 0.4488 0.8969 0.2481 0.0862 -0.0541 795 LEU A CA 6150 C C . LEU A 795 ? 1.1278 0.7157 1.1461 0.2631 0.0943 -0.0652 795 LEU A C 6151 O O . LEU A 795 ? 1.4390 0.9791 1.4246 0.2666 0.0814 -0.0790 795 LEU A O 6152 C CB . LEU A 795 ? 0.8959 0.4808 0.9365 0.2226 0.0791 -0.0516 795 LEU A CB 6153 C CG . LEU A 795 ? 0.8729 0.4796 0.9199 0.2110 0.0835 -0.0497 795 LEU A CG 6154 C CD1 . LEU A 795 ? 0.8421 0.4478 0.8834 0.2029 0.0782 -0.0456 795 LEU A CD1 6155 C CD2 . LEU A 795 ? 0.9666 0.5678 1.0007 0.2092 0.0868 -0.0564 795 LEU A CD2 6156 N N . HIS A 796 ? 0.9960 0.6290 1.0276 0.2704 0.1115 -0.0557 796 HIS A N 6157 C CA . HIS A 796 ? 1.0235 0.6566 1.0218 0.2911 0.1232 -0.0624 796 HIS A CA 6158 C C . HIS A 796 ? 1.0297 0.6784 1.0321 0.2688 0.1266 -0.0535 796 HIS A C 6159 O O . HIS A 796 ? 0.9706 0.6600 1.0086 0.2536 0.1333 -0.0315 796 HIS A O 6160 C CB . HIS A 796 ? 0.8555 0.5390 0.8596 0.3289 0.1471 -0.0504 796 HIS A CB 6161 C CG . HIS A 796 ? 0.9870 0.6452 0.9712 0.3665 0.1431 -0.0644 796 HIS A CG 6162 N ND1 . HIS A 796 ? 1.3974 1.0351 1.3259 0.4011 0.1407 -0.0841 796 HIS A ND1 6163 C CD2 . HIS A 796 ? 0.9673 0.6205 0.9774 0.3662 0.1318 -0.0614 796 HIS A CD2 6164 C CE1 . HIS A 796 ? 1.3101 0.9323 1.2362 0.4163 0.1272 -0.0923 796 HIS A CE1 6165 N NE2 . HIS A 796 ? 1.4047 1.0381 1.3815 0.3959 0.1221 -0.0779 796 HIS A NE2 6166 N N . LEU A 797 ? 0.9787 0.5896 0.9456 0.2657 0.1153 -0.0688 797 LEU A N 6167 C CA . LEU A 797 ? 0.8561 0.4760 0.8198 0.2515 0.1159 -0.0617 797 LEU A CA 6168 C C . LEU A 797 ? 1.0864 0.7113 1.0066 0.2776 0.1280 -0.0619 797 LEU A C 6169 O O . LEU A 797 ? 1.2243 0.8103 1.0934 0.3018 0.1189 -0.0835 797 LEU A O 6170 C CB . LEU A 797 ? 1.0855 0.6752 1.0457 0.2321 0.0944 -0.0724 797 LEU A CB 6171 C CG . LEU A 797 ? 1.0668 0.6606 1.0183 0.2251 0.0906 -0.0679 797 LEU A CG 6172 C CD1 . LEU A 797 ? 0.8831 0.5007 0.8598 0.2148 0.0991 -0.0493 797 LEU A CD1 6173 C CD2 . LEU A 797 ? 1.0398 0.6217 0.9997 0.2107 0.0703 -0.0736 797 LEU A CD2 6174 N N . GLN A 798 ? 0.9815 0.6487 0.9161 0.2734 0.1450 -0.0358 798 GLN A N 6175 C CA . GLN A 798 ? 0.9819 0.6620 0.8710 0.2977 0.1602 -0.0278 798 GLN A CA 6176 C C . GLN A 798 ? 1.1692 0.8263 1.0441 0.2780 0.1442 -0.0264 798 GLN A C 6177 O O . GLN A 798 ? 1.3355 1.0006 1.2494 0.2494 0.1379 -0.0089 798 GLN A O 6178 C CB . GLN A 798 ? 0.9302 0.6852 0.8498 0.3059 0.1921 0.0129 798 GLN A CB 6179 C CG . GLN A 798 ? 0.9815 0.7762 0.9267 0.3299 0.2091 0.0170 798 GLN A CG 6180 C CD . GLN A 798 ? 1.1510 1.0417 1.1294 0.3454 0.2452 0.0652 798 GLN A CD 6181 O OE1 . GLN A 798 ? 1.0887 1.0109 1.0512 0.3471 0.2620 0.0936 798 GLN A OE1 6182 N NE2 . GLN A 798 ? 1.3823 1.3278 1.4115 0.3566 0.2572 0.0805 798 GLN A NE2 6183 N N . TRP A 799 ? 1.2236 0.8446 1.0377 0.2966 0.1317 -0.0463 799 TRP A N 6184 C CA . TRP A 799 ? 1.1467 0.7470 0.9493 0.2811 0.1113 -0.0463 799 TRP A CA 6185 C C . TRP A 799 ? 1.3130 0.9144 1.0512 0.3064 0.1191 -0.0371 799 TRP A C 6186 O O . TRP A 799 ? 1.1805 0.7707 0.8561 0.3439 0.1263 -0.0510 799 TRP A O 6187 C CB . TRP A 799 ? 1.0332 0.5905 0.8331 0.2706 0.0766 -0.0747 799 TRP A CB 6188 C CG . TRP A 799 ? 1.1564 0.7088 0.9657 0.2545 0.0548 -0.0712 799 TRP A CG 6189 C CD1 . TRP A 799 ? 1.2834 0.8151 1.0466 0.2643 0.0342 -0.0766 799 TRP A CD1 6190 C CD2 . TRP A 799 ? 1.2729 0.8424 1.1366 0.2334 0.0497 -0.0620 799 TRP A CD2 6191 N NE1 . TRP A 799 ? 1.1062 0.6481 0.9024 0.2484 0.0171 -0.0685 799 TRP A NE1 6192 C CE2 . TRP A 799 ? 1.1636 0.7289 1.0189 0.2331 0.0284 -0.0603 799 TRP A CE2 6193 C CE3 . TRP A 799 ? 1.3554 0.9412 1.2659 0.2211 0.0595 -0.0564 799 TRP A CE3 6194 C CZ2 . TRP A 799 ? 1.1835 0.7661 1.0787 0.2262 0.0208 -0.0527 799 TRP A CZ2 6195 C CZ3 . TRP A 799 ? 1.1468 0.7414 1.0849 0.2158 0.0511 -0.0519 799 TRP A CZ3 6196 C CH2 . TRP A 799 ? 1.3215 0.9173 1.2535 0.2208 0.0341 -0.0498 799 TRP A CH2 6197 N N . PRO A 800 ? 1.3803 0.9892 1.1245 0.2912 0.1157 -0.0140 800 PRO A N 6198 C CA . PRO A 800 ? 1.4316 1.0419 1.1126 0.3125 0.1215 0.0016 800 PRO A CA 6199 C C . PRO A 800 ? 1.5562 1.1147 1.1767 0.3260 0.0853 -0.0302 800 PRO A C 6200 O O . PRO A 800 ? 1.5863 1.1315 1.2149 0.3105 0.0616 -0.0255 800 PRO A O 6201 C CB . PRO A 800 ? 1.3354 0.9602 1.0561 0.2839 0.1216 0.0396 800 PRO A CB 6202 C CG . PRO A 800 ? 1.2173 0.8215 0.9969 0.2566 0.0985 0.0230 800 PRO A CG 6203 C CD . PRO A 800 ? 1.1209 0.7328 0.9261 0.2577 0.1058 0.0008 800 PRO A CD 6204 N N . TYR A 801 ? 1.4163 0.9413 0.9760 0.3559 0.0752 -0.0621 801 TYR A N 6205 C CA . TYR A 801 ? 1.4964 0.9616 1.0009 0.3626 0.0272 -0.0935 801 TYR A CA 6206 C C . TYR A 801 ? 1.5403 0.9975 0.9715 0.3838 0.0207 -0.0819 801 TYR A C 6207 O O . TYR A 801 ? 1.4966 0.9393 0.9377 0.3653 -0.0135 -0.0813 801 TYR A O 6208 C CB . TYR A 801 ? 1.6841 1.0932 1.1262 0.3921 0.0080 -0.1324 801 TYR A CB 6209 C CG . TYR A 801 ? 1.8817 1.2185 1.2859 0.3837 -0.0577 -0.1639 801 TYR A CG 6210 C CD1 . TYR A 801 ? 1.9378 1.2820 1.4243 0.3348 -0.0916 -0.1587 801 TYR A CD1 6211 C CD2 . TYR A 801 ? 1.7531 1.0167 1.0389 0.4267 -0.0891 -0.1964 801 TYR A CD2 6212 C CE1 . TYR A 801 ? 1.9864 1.2782 1.4564 0.3193 -0.1564 -0.1778 801 TYR A CE1 6213 C CE2 . TYR A 801 ? 2.0933 1.2830 1.3479 0.4119 -0.1619 -0.2234 801 TYR A CE2 6214 C CZ . TYR A 801 ? 2.2268 1.4366 1.5830 0.3533 -0.1961 -0.2103 801 TYR A CZ 6215 O OH . TYR A 801 ? 2.2444 1.3943 1.5872 0.3312 -0.2728 -0.2276 801 TYR A OH 6216 N N . LYS A 802 ? 1.5108 0.9853 0.8694 0.4261 0.0555 -0.0686 802 LYS A N 6217 C CA . LYS A 802 ? 1.5662 1.0356 0.8414 0.4522 0.0542 -0.0527 802 LYS A CA 6218 C C . LYS A 802 ? 1.7105 1.2534 0.9858 0.4656 0.1133 0.0025 802 LYS A C 6219 O O . LYS A 802 ? 1.6000 1.1970 0.9225 0.4669 0.1547 0.0221 802 LYS A O 6220 C CB . LYS A 802 ? 1.6771 1.0786 0.8213 0.5048 0.0249 -0.0949 802 LYS A CB 6221 C CG . LYS A 802 ? 1.6927 1.0150 0.8296 0.4841 -0.0497 -0.1392 802 LYS A CG 6222 C CD . LYS A 802 ? 1.8869 1.1224 0.8784 0.5377 -0.0900 -0.1829 802 LYS A CD 6223 C CE . LYS A 802 ? 2.3250 1.5392 1.2596 0.5874 -0.0641 -0.2079 802 LYS A CE 6224 N NZ . LYS A 802 ? 2.2609 1.3713 1.0332 0.6511 -0.1085 -0.2576 802 LYS A NZ 6225 N N . TYR A 803 ? 1.8261 1.3747 1.0550 0.4720 0.1138 0.0334 803 TYR A N 6226 C CA . TYR A 803 ? 1.7981 1.4173 1.0136 0.4860 0.1666 0.0957 803 TYR A CA 6227 C C . TYR A 803 ? 1.8828 1.4830 0.9650 0.5360 0.1647 0.1011 803 TYR A C 6228 O O . TYR A 803 ? 1.8397 1.3921 0.8907 0.5256 0.1229 0.0949 803 TYR A O 6229 C CB . TYR A 803 ? 1.6861 1.3345 1.0006 0.4287 0.1696 0.1480 803 TYR A CB 6230 C CG . TYR A 803 ? 1.7292 1.4453 1.0373 0.4304 0.2132 0.2247 803 TYR A CG 6231 C CD1 . TYR A 803 ? 1.7706 1.5742 1.1165 0.4378 0.2666 0.2665 803 TYR A CD1 6232 C CD2 . TYR A 803 ? 1.7770 1.4761 1.0484 0.4227 0.1996 0.2623 803 TYR A CD2 6233 C CE1 . TYR A 803 ? 1.7954 1.6764 1.1497 0.4331 0.3068 0.3493 803 TYR A CE1 6234 C CE2 . TYR A 803 ? 1.8316 1.5943 1.1016 0.4183 0.2380 0.3427 803 TYR A CE2 6235 C CZ . TYR A 803 ? 1.8500 1.7079 1.1653 0.4211 0.2923 0.3887 803 TYR A CZ 6236 O OH . TYR A 803 ? 1.8472 1.7834 1.1744 0.4109 0.3309 0.4807 803 TYR A OH 6237 N N . ASN A 804 ? 1.9446 1.5866 0.9454 0.5958 0.2105 0.1138 804 ASN A N 6238 C CA . ASN A 804 ? 2.1656 1.7849 1.0130 0.6596 0.2112 0.1114 804 ASN A CA 6239 C C . ASN A 804 ? 2.2160 1.7177 0.9730 0.6778 0.1369 0.0358 804 ASN A C 6240 O O . ASN A 804 ? 2.3743 1.8325 1.0711 0.6776 0.0985 0.0357 804 ASN A O 6241 C CB . ASN A 804 ? 2.2524 1.9111 1.0953 0.6413 0.2266 0.1822 804 ASN A CB 6242 C CG . ASN A 804 ? 2.2435 2.0232 1.1435 0.6363 0.3003 0.2679 804 ASN A CG 6243 O OD1 . ASN A 804 ? 2.3445 2.1910 1.2406 0.6761 0.3498 0.2752 804 ASN A OD1 6244 N ND2 . ASN A 804 ? 2.1915 2.0007 1.1485 0.5874 0.3042 0.3373 804 ASN A ND2 6245 N N . ASN A 805 ? 2.2609 1.7110 1.0184 0.6876 0.1116 -0.0238 805 ASN A N 6246 C CA . ASN A 805 ? 2.4319 1.7650 1.0959 0.7091 0.0371 -0.0951 805 ASN A CA 6247 C C . ASN A 805 ? 2.3711 1.6535 1.1085 0.6432 -0.0349 -0.1137 805 ASN A C 6248 O O . ASN A 805 ? 2.6074 1.7985 1.2895 0.6475 -0.1055 -0.1653 805 ASN A O 6249 C CB . ASN A 805 ? 2.7664 2.0558 1.2441 0.7873 0.0291 -0.1079 805 ASN A CB 6250 C CG . ASN A 805 ? 2.9894 2.2734 1.3994 0.8569 0.0504 -0.1310 805 ASN A CG 6251 O OD1 . ASN A 805 ? 2.7761 2.0320 1.2311 0.8511 0.0357 -0.1643 805 ASN A OD1 6252 N ND2 . ASN A 805 ? 3.6437 2.9633 1.9731 0.9159 0.0805 -0.1052 805 ASN A ND2 6253 N N . ASN A 806 ? 2.1834 1.5232 1.0435 0.5848 -0.0214 -0.0704 806 ASN A N 6254 C CA . ASN A 806 ? 2.1329 1.4431 1.0696 0.5317 -0.0820 -0.0836 806 ASN A CA 6255 C C . ASN A 806 ? 1.9042 1.2652 0.9995 0.4728 -0.0648 -0.0639 806 ASN A C 6256 O O . ASN A 806 ? 1.7592 1.1800 0.9108 0.4618 -0.0106 -0.0251 806 ASN A O 6257 C CB . ASN A 806 ? 2.1597 1.4626 1.0494 0.5351 -0.1066 -0.0592 806 ASN A CB 6258 C CG . ASN A 806 ? 2.2178 1.5805 1.0843 0.5513 -0.0448 0.0017 806 ASN A CG 6259 O OD1 . ASN A 806 ? 2.3066 1.7310 1.2640 0.5248 0.0047 0.0403 806 ASN A OD1 6260 N ND2 . ASN A 806 ? 2.1533 1.4964 0.8961 0.5932 -0.0515 0.0144 806 ASN A ND2 6261 N N . THR A 807 ? 1.7828 1.1203 0.9464 0.4363 -0.1154 -0.0885 807 THR A N 6262 C CA . THR A 807 ? 1.6395 1.0127 0.9332 0.3919 -0.1055 -0.0843 807 THR A CA 6263 C C . THR A 807 ? 1.5946 1.0221 0.9708 0.3675 -0.0712 -0.0421 807 THR A C 6264 O O . THR A 807 ? 1.9575 1.3879 1.3259 0.3671 -0.0824 -0.0188 807 THR A O 6265 C CB . THR A 807 ? 1.6507 1.0023 0.9982 0.3608 -0.1683 -0.1073 807 THR A CB 6266 O OG1 . THR A 807 ? 1.7136 0.9955 0.9837 0.3765 -0.2152 -0.1466 807 THR A OG1 6267 C CG2 . THR A 807 ? 1.5941 0.9861 1.0620 0.3234 -0.1539 -0.1025 807 THR A CG2 6268 N N . LEU A 808 ? 1.4637 0.9237 0.9135 0.3485 -0.0363 -0.0340 808 LEU A N 6269 C CA . LEU A 808 ? 1.3795 0.8716 0.9049 0.3239 -0.0160 -0.0016 808 LEU A CA 6270 C C . LEU A 808 ? 1.3803 0.8800 0.9914 0.2988 -0.0379 -0.0159 808 LEU A C 6271 O O . LEU A 808 ? 1.5017 1.0027 1.1374 0.2951 -0.0628 -0.0096 808 LEU A O 6272 C CB . LEU A 808 ? 1.3610 0.8858 0.9104 0.3197 0.0322 0.0215 808 LEU A CB 6273 C CG . LEU A 808 ? 1.4304 0.9792 0.9230 0.3402 0.0671 0.0595 808 LEU A CG 6274 C CD1 . LEU A 808 ? 1.4038 1.0011 0.9426 0.3325 0.1100 0.0824 808 LEU A CD1 6275 C CD2 . LEU A 808 ? 1.5079 1.0519 0.9980 0.3287 0.0596 0.1008 808 LEU A CD2 6276 N N . LEU A 809 ? 1.4594 0.9697 1.1139 0.2868 -0.0262 -0.0321 809 LEU A N 6277 C CA . LEU A 809 ? 1.2225 0.7496 0.9514 0.2674 -0.0421 -0.0425 809 LEU A CA 6278 C C . LEU A 809 ? 1.3829 0.8960 1.1105 0.2605 -0.0693 -0.0680 809 LEU A C 6279 O O . LEU A 809 ? 1.5560 1.0551 1.2721 0.2613 -0.0566 -0.0813 809 LEU A O 6280 C CB . LEU A 809 ? 1.2103 0.7570 0.9927 0.2555 -0.0119 -0.0345 809 LEU A CB 6281 C CG . LEU A 809 ? 1.1630 0.7084 0.9587 0.2550 -0.0015 -0.0103 809 LEU A CG 6282 C CD1 . LEU A 809 ? 1.0908 0.6427 0.9283 0.2429 0.0180 -0.0076 809 LEU A CD1 6283 C CD2 . LEU A 809 ? 1.2864 0.8331 1.1006 0.2630 -0.0273 -0.0082 809 LEU A CD2 6284 N N . TYR A 810 ? 1.5708 1.0863 1.3142 0.2524 -0.1118 -0.0715 810 TYR A N 6285 C CA . TYR A 810 ? 1.5273 1.0206 1.2736 0.2368 -0.1529 -0.0895 810 TYR A CA 6286 C C . TYR A 810 ? 1.4295 0.9657 1.2687 0.2094 -0.1484 -0.0800 810 TYR A C 6287 O O . TYR A 810 ? 1.2425 0.8360 1.1506 0.2019 -0.1482 -0.0602 810 TYR A O 6288 C CB . TYR A 810 ? 1.3821 0.8648 1.1121 0.2344 -0.2086 -0.0903 810 TYR A CB 6289 C CG . TYR A 810 ? 1.4023 0.8521 1.1380 0.2101 -0.2682 -0.1045 810 TYR A CG 6290 C CD1 . TYR A 810 ? 1.3660 0.8694 1.2064 0.1735 -0.2930 -0.0841 810 TYR A CD1 6291 C CD2 . TYR A 810 ? 1.5437 0.9071 1.1772 0.2254 -0.3037 -0.1349 810 TYR A CD2 6292 C CE1 . TYR A 810 ? 1.4449 0.9159 1.3004 0.1411 -0.3563 -0.0883 810 TYR A CE1 6293 C CE2 . TYR A 810 ? 1.6667 0.9790 1.2992 0.1998 -0.3719 -0.1490 810 TYR A CE2 6294 C CZ . TYR A 810 ? 1.5757 0.9418 1.3258 0.1518 -0.4006 -0.1228 810 TYR A CZ 6295 O OH . TYR A 810 ? 1.6522 0.9660 1.4118 0.1163 -0.4763 -0.1281 810 TYR A OH 6296 N N . ILE A 811 ? 1.4219 0.9324 1.2585 0.2001 -0.1438 -0.0921 811 ILE A N 6297 C CA . ILE A 811 ? 1.2014 0.7519 1.1178 0.1752 -0.1351 -0.0781 811 ILE A CA 6298 C C . ILE A 811 ? 1.2429 0.8028 1.2087 0.1418 -0.1876 -0.0671 811 ILE A C 6299 O O . ILE A 811 ? 1.3195 0.8128 1.2438 0.1311 -0.2327 -0.0839 811 ILE A O 6300 C CB . ILE A 811 ? 1.1620 0.6816 1.0596 0.1780 -0.1102 -0.0902 811 ILE A CB 6301 C CG1 . ILE A 811 ? 1.1540 0.6801 1.0229 0.2035 -0.0615 -0.0915 811 ILE A CG1 6302 C CG2 . ILE A 811 ? 1.0575 0.6161 1.0305 0.1522 -0.1043 -0.0717 811 ILE A CG2 6303 C CD1 . ILE A 811 ? 0.9975 0.5076 0.8581 0.2091 -0.0367 -0.0993 811 ILE A CD1 6304 N N . LEU A 812 ? 1.1372 0.7800 1.1907 0.1275 -0.1846 -0.0364 812 LEU A N 6305 C CA . LEU A 812 ? 1.2795 0.9601 1.4078 0.0885 -0.2303 -0.0099 812 LEU A CA 6306 C C . LEU A 812 ? 1.2121 0.8929 1.3800 0.0596 -0.2262 0.0042 812 LEU A C 6307 O O . LEU A 812 ? 1.3086 0.9472 1.4865 0.0235 -0.2783 0.0093 812 LEU A O 6308 C CB . LEU A 812 ? 1.2750 1.0666 1.4899 0.0920 -0.2212 0.0258 812 LEU A CB 6309 C CG . LEU A 812 ? 1.2935 1.0977 1.4916 0.1150 -0.2392 0.0230 812 LEU A CG 6310 C CD1 . LEU A 812 ? 1.1623 1.0859 1.4537 0.1273 -0.2234 0.0605 812 LEU A CD1 6311 C CD2 . LEU A 812 ? 1.5176 1.2691 1.6887 0.0908 -0.3118 0.0142 812 LEU A CD2 6312 N N . HIS A 813 ? 1.1023 0.8219 1.2872 0.0755 -0.1697 0.0113 813 HIS A N 6313 C CA . HIS A 813 ? 1.1353 0.8774 1.3675 0.0512 -0.1591 0.0351 813 HIS A CA 6314 C C . HIS A 813 ? 1.0887 0.8281 1.2912 0.0801 -0.1021 0.0224 813 HIS A C 6315 O O . HIS A 813 ? 1.1235 0.8682 1.2943 0.1141 -0.0708 0.0062 813 HIS A O 6316 C CB . HIS A 813 ? 1.1918 1.0500 1.5307 0.0291 -0.1610 0.0882 813 HIS A CB 6317 C CG . HIS A 813 ? 1.4403 1.3264 1.8357 -0.0072 -0.1624 0.1263 813 HIS A CG 6318 N ND1 . HIS A 813 ? 1.7983 1.6056 2.1865 -0.0500 -0.2140 0.1277 813 HIS A ND1 6319 C CD2 . HIS A 813 ? 1.4226 1.4027 1.8765 -0.0046 -0.1206 0.1671 813 HIS A CD2 6320 C CE1 . HIS A 813 ? 1.7886 1.6410 2.2361 -0.0786 -0.2045 0.1722 813 HIS A CE1 6321 N NE2 . HIS A 813 ? 1.6496 1.6131 2.1370 -0.0507 -0.1450 0.1980 813 HIS A NE2 6322 N N . TYR A 814 ? 1.0469 0.7721 1.2590 0.0644 -0.0951 0.0319 814 TYR A N 6323 C CA . TYR A 814 ? 1.0224 0.7583 1.2185 0.0882 -0.0470 0.0271 814 TYR A CA 6324 C C . TYR A 814 ? 1.0158 0.7950 1.2619 0.0669 -0.0379 0.0643 814 TYR A C 6325 O O . TYR A 814 ? 1.1766 0.9281 1.4441 0.0303 -0.0721 0.0818 814 TYR A O 6326 C CB . TYR A 814 ? 0.9420 0.5949 1.0660 0.1058 -0.0405 -0.0103 814 TYR A CB 6327 C CG . TYR A 814 ? 1.0654 0.6449 1.1657 0.0885 -0.0716 -0.0188 814 TYR A CG 6328 C CD1 . TYR A 814 ? 1.0932 0.6628 1.2033 0.0807 -0.0622 -0.0072 814 TYR A CD1 6329 C CD2 . TYR A 814 ? 1.3189 0.8281 1.3750 0.0859 -0.1142 -0.0410 814 TYR A CD2 6330 C CE1 . TYR A 814 ? 1.0658 0.5554 1.1483 0.0698 -0.0955 -0.0160 814 TYR A CE1 6331 C CE2 . TYR A 814 ? 1.4901 0.9136 1.5098 0.0789 -0.1491 -0.0543 814 TYR A CE2 6332 C CZ . TYR A 814 ? 1.4303 0.8430 1.4659 0.0706 -0.1399 -0.0413 814 TYR A CZ 6333 O OH . TYR A 814 ? 1.6189 0.9344 1.6132 0.0680 -0.1792 -0.0552 814 TYR A OH 6334 N N . ASP A 815 ? 0.9350 0.7760 1.1931 0.0914 0.0046 0.0777 815 ASP A N 6335 C CA . ASP A 815 ? 1.0236 0.9194 1.3215 0.0795 0.0216 0.1185 815 ASP A CA 6336 C C . ASP A 815 ? 0.9493 0.8131 1.1978 0.1035 0.0510 0.1018 815 ASP A C 6337 O O . ASP A 815 ? 0.8713 0.6985 1.0698 0.1337 0.0647 0.0653 815 ASP A O 6338 C CB . ASP A 815 ? 1.0964 1.1118 1.4512 0.0949 0.0460 0.1581 815 ASP A CB 6339 C CG . ASP A 815 ? 1.2668 1.3385 1.6993 0.0580 0.0115 0.1952 815 ASP A CG 6340 O OD1 . ASP A 815 ? 1.5592 1.5930 2.0183 0.0072 -0.0305 0.2127 815 ASP A OD1 6341 O OD2 . ASP A 815 ? 1.1596 1.3087 1.6262 0.0801 0.0206 0.2073 815 ASP A OD2 6342 N N . ILE A 816 ? 0.9693 0.8474 1.2353 0.0864 0.0558 0.1334 816 ILE A N 6343 C CA . ILE A 816 ? 0.9239 0.7707 1.1441 0.1064 0.0765 0.1214 816 ILE A CA 6344 C C . ILE A 816 ? 0.9802 0.9092 1.2112 0.1260 0.1116 0.1589 816 ILE A C 6345 O O . ILE A 816 ? 1.1187 1.1316 1.4072 0.1109 0.1182 0.2086 816 ILE A O 6346 C CB . ILE A 816 ? 1.0515 0.8239 1.2616 0.0780 0.0497 0.1223 816 ILE A CB 6347 C CG1 . ILE A 816 ? 1.0861 0.7888 1.2920 0.0566 0.0080 0.0993 816 ILE A CG1 6348 C CG2 . ILE A 816 ? 0.9217 0.6470 1.0784 0.1045 0.0634 0.0944 816 ILE A CG2 6349 C CD1 . ILE A 816 ? 0.9596 0.6148 1.1144 0.0863 0.0118 0.0485 816 ILE A CD1 6350 N N . ASP A 817 ? 0.9964 0.9055 1.1708 0.1617 0.1325 0.1377 817 ASP A N 6351 C CA . ASP A 817 ? 1.0664 1.0373 1.2256 0.1896 0.1644 0.1678 817 ASP A CA 6352 C C . ASP A 817 ? 1.1897 1.1018 1.2967 0.1959 0.1623 0.1555 817 ASP A C 6353 O O . ASP A 817 ? 1.2913 1.1399 1.3514 0.2140 0.1531 0.1108 817 ASP A O 6354 C CB . ASP A 817 ? 1.1137 1.1235 1.2389 0.2454 0.1889 0.1499 817 ASP A CB 6355 C CG . ASP A 817 ? 1.4240 1.5436 1.5619 0.2762 0.2260 0.1983 817 ASP A CG 6356 O OD1 . ASP A 817 ? 1.6714 1.8244 1.8174 0.2630 0.2386 0.2407 817 ASP A OD1 6357 O OD2 . ASP A 817 ? 1.2758 1.4521 1.4144 0.3175 0.2440 0.1971 817 ASP A OD2 6358 N N . GLY A 818 ? 1.1439 1.0804 1.2646 0.1780 0.1676 0.2006 818 GLY A N 6359 C CA . GLY A 818 ? 1.1741 1.0564 1.2480 0.1832 0.1618 0.1944 818 GLY A CA 6360 C C . GLY A 818 ? 1.1424 0.9539 1.2388 0.1410 0.1277 0.1957 818 GLY A C 6361 O O . GLY A 818 ? 1.1817 0.9794 1.3232 0.1070 0.1058 0.2008 818 GLY A O 6362 N N . PRO A 819 ? 1.1601 0.9198 1.2186 0.1479 0.1186 0.1887 819 PRO A N 6363 C CA . PRO A 819 ? 1.1122 0.7992 1.1808 0.1198 0.0862 0.1918 819 PRO A CA 6364 C C . PRO A 819 ? 1.0236 0.6463 1.0904 0.1212 0.0636 0.1412 819 PRO A C 6365 O O . PRO A 819 ? 1.0649 0.6460 1.1034 0.1418 0.0568 0.1116 819 PRO A O 6366 C CB . PRO A 819 ? 1.1712 0.8362 1.1936 0.1409 0.0881 0.1963 819 PRO A CB 6367 C CG . PRO A 819 ? 1.2581 0.9486 1.2375 0.1816 0.1075 0.1646 819 PRO A CG 6368 C CD . PRO A 819 ? 1.4282 1.1880 1.4246 0.1886 0.1327 0.1738 819 PRO A CD 6369 N N . MET A 820 ? 1.0227 0.6447 1.1197 0.1020 0.0522 0.1352 820 MET A N 6370 C CA . MET A 820 ? 0.9542 0.5205 1.0391 0.1093 0.0345 0.0906 820 MET A CA 6371 C C . MET A 820 ? 0.9895 0.5237 1.0973 0.0794 0.0032 0.0952 820 MET A C 6372 O O . MET A 820 ? 1.2366 0.8196 1.3849 0.0534 0.0017 0.1263 820 MET A O 6373 C CB . MET A 820 ? 0.8910 0.4896 0.9640 0.1352 0.0562 0.0585 820 MET A CB 6374 C CG . MET A 820 ? 0.8596 0.4201 0.9212 0.1444 0.0458 0.0217 820 MET A CG 6375 S SD . MET A 820 ? 1.1852 0.7850 1.2423 0.1625 0.0661 -0.0005 820 MET A SD 6376 C CE . MET A 820 ? 1.3170 0.9234 1.3538 0.1838 0.0770 -0.0065 820 MET A CE 6377 N N . ASN A 821 ? 1.0270 0.4800 1.1063 0.0871 -0.0244 0.0648 821 ASN A N 6378 C CA . ASN A 821 ? 1.0912 0.4931 1.1692 0.0690 -0.0618 0.0541 821 ASN A CA 6379 C C . ASN A 821 ? 1.1086 0.4963 1.1505 0.1027 -0.0535 0.0067 821 ASN A C 6380 O O . ASN A 821 ? 1.3667 0.7635 1.3866 0.1366 -0.0281 -0.0147 821 ASN A O 6381 C CB . ASN A 821 ? 1.2386 0.5378 1.2948 0.0563 -0.1098 0.0580 821 ASN A CB 6382 C CG . ASN A 821 ? 1.4920 0.8023 1.5905 0.0119 -0.1252 0.1168 821 ASN A CG 6383 O OD1 . ASN A 821 ? 1.7111 1.1093 1.8636 -0.0169 -0.1084 0.1586 821 ASN A OD1 6384 N ND2 . ASN A 821 ? 2.0959 1.3207 2.1699 0.0095 -0.1564 0.1246 821 ASN A ND2 6385 N N . CYS A 822 ? 1.1214 0.4921 1.1598 0.0920 -0.0765 -0.0045 822 CYS A N 6386 C CA . CYS A 822 ? 1.0891 0.4479 1.0861 0.1252 -0.0677 -0.0437 822 CYS A CA 6387 C C . CYS A 822 ? 1.4587 0.7350 1.4131 0.1245 -0.1156 -0.0660 822 CYS A C 6388 O O . CYS A 822 ? 1.7270 0.9727 1.7027 0.0854 -0.1596 -0.0471 822 CYS A O 6389 C CB . CYS A 822 ? 1.0093 0.4504 1.0336 0.1251 -0.0364 -0.0389 822 CYS A CB 6390 S SG . CYS A 822 ? 1.5042 1.0148 1.5489 0.1397 0.0107 -0.0279 822 CYS A SG 6391 N N . THR A 823 ? 1.1284 0.3704 1.0208 0.1686 -0.1092 -0.1032 823 THR A N 6392 C CA . THR A 823 ? 1.3570 0.5225 1.1867 0.1798 -0.1515 -0.1308 823 THR A CA 6393 C C . THR A 823 ? 1.3803 0.5767 1.1673 0.2159 -0.1254 -0.1542 823 THR A C 6394 O O . THR A 823 ? 1.3248 0.5812 1.1143 0.2445 -0.0763 -0.1550 823 THR A O 6395 C CB . THR A 823 ? 1.4049 0.5196 1.1885 0.1991 -0.1680 -0.1450 823 THR A CB 6396 O OG1 . THR A 823 ? 1.4169 0.5080 1.2404 0.1665 -0.1865 -0.1174 823 THR A OG1 6397 C CG2 . THR A 823 ? 1.4522 0.4896 1.1672 0.2050 -0.2211 -0.1702 823 THR A CG2 6398 N N . SER A 824 ? 1.2761 0.4318 1.0274 0.2110 -0.1628 -0.1681 824 SER A N 6399 C CA . SER A 824 ? 1.2843 0.4601 0.9848 0.2457 -0.1432 -0.1865 824 SER A CA 6400 C C . SER A 824 ? 1.3973 0.5216 1.0054 0.2846 -0.1623 -0.2154 824 SER A C 6401 O O . SER A 824 ? 1.8327 0.8788 1.4057 0.2728 -0.2197 -0.2274 824 SER A O 6402 C CB . SER A 824 ? 1.4665 0.6501 1.1873 0.2179 -0.1689 -0.1792 824 SER A CB 6403 O OG . SER A 824 ? 1.4878 0.6797 1.1492 0.2531 -0.1539 -0.1953 824 SER A OG 6404 N N . ASP A 825 ? 1.3956 0.5634 0.9637 0.3323 -0.1173 -0.2228 825 ASP A N 6405 C CA . ASP A 825 ? 1.5261 0.6530 0.9973 0.3826 -0.1288 -0.2476 825 ASP A CA 6406 C C . ASP A 825 ? 1.6055 0.6725 1.0023 0.3892 -0.1738 -0.2673 825 ASP A C 6407 O O . ASP A 825 ? 1.7350 0.7377 1.0391 0.4248 -0.2070 -0.2913 825 ASP A O 6408 C CB . ASP A 825 ? 1.4893 0.6929 0.9463 0.4326 -0.0656 -0.2400 825 ASP A CB 6409 C CG . ASP A 825 ? 1.8655 1.1310 1.3347 0.4360 -0.0278 -0.2242 825 ASP A CG 6410 O OD1 . ASP A 825 ? 1.8388 1.0977 1.3441 0.3977 -0.0435 -0.2182 825 ASP A OD1 6411 O OD2 . ASP A 825 ? 1.6642 0.9869 1.1082 0.4791 0.0176 -0.2136 825 ASP A OD2 6412 N N . MET A 826 ? 1.9189 1.0039 1.3526 0.3587 -0.1782 -0.2571 826 MET A N 6413 C CA . MET A 826 ? 1.7431 0.7710 1.1184 0.3571 -0.2294 -0.2734 826 MET A CA 6414 C C . MET A 826 ? 1.6023 0.6024 1.0504 0.2930 -0.2830 -0.2616 826 MET A C 6415 O O . MET A 826 ? 1.4925 0.5446 1.0352 0.2599 -0.2583 -0.2359 826 MET A O 6416 C CB . MET A 826 ? 1.8352 0.9109 1.1789 0.3875 -0.1896 -0.2695 826 MET A CB 6417 C CG . MET A 826 ? 1.8933 1.0206 1.1866 0.4462 -0.1280 -0.2662 826 MET A CG 6418 S SD . MET A 826 ? 1.6936 0.8558 0.9238 0.4844 -0.0946 -0.2579 826 MET A SD 6419 C CE . MET A 826 ? 2.4295 1.4839 1.5363 0.5045 -0.1729 -0.2939 826 MET A CE 6420 N N . GLU A 827 ? 1.7799 0.7005 1.1855 0.2766 -0.3597 -0.2763 827 GLU A N 6421 C CA . GLU A 827 ? 1.7808 0.6814 1.2664 0.2097 -0.4209 -0.2570 827 GLU A CA 6422 C C . GLU A 827 ? 1.7875 0.7994 1.3587 0.1860 -0.3839 -0.2256 827 GLU A C 6423 O O . GLU A 827 ? 1.8541 0.8869 1.3797 0.2133 -0.3710 -0.2340 827 GLU A O 6424 C CB . GLU A 827 ? 1.8464 0.6571 1.2691 0.1977 -0.5124 -0.2744 827 GLU A CB 6425 C CG . GLU A 827 ? 2.0117 0.8181 1.5299 0.1220 -0.5835 -0.2461 827 GLU A CG 6426 C CD . GLU A 827 ? 2.4698 1.1936 1.9257 0.1109 -0.6786 -0.2606 827 GLU A CD 6427 O OE1 . GLU A 827 ? 2.5196 1.2008 2.0150 0.0613 -0.7476 -0.2406 827 GLU A OE1 6428 O OE2 . GLU A 827 ? 2.5842 1.2858 1.9506 0.1523 -0.6859 -0.2877 827 GLU A OE2 6429 N N . ILE A 828 ? 1.7153 0.8136 1.4099 0.1377 -0.3631 -0.1835 828 ILE A N 6430 C CA . ILE A 828 ? 1.6040 0.8225 1.3824 0.1209 -0.3247 -0.1503 828 ILE A CA 6431 C C . ILE A 828 ? 1.5846 0.8154 1.4038 0.0830 -0.3875 -0.1334 828 ILE A C 6432 O O . ILE A 828 ? 1.5676 0.7553 1.4169 0.0399 -0.4540 -0.1224 828 ILE A O 6433 C CB . ILE A 828 ? 1.3448 0.6550 1.2268 0.0962 -0.2757 -0.1131 828 ILE A CB 6434 C CG1 . ILE A 828 ? 1.8014 1.0924 1.7433 0.0467 -0.3190 -0.0880 828 ILE A CG1 6435 C CG2 . ILE A 828 ? 1.2229 0.5398 1.0733 0.1341 -0.2119 -0.1263 828 ILE A CG2 6436 C CD1 . ILE A 828 ? 1.6199 1.0219 1.6712 0.0184 -0.2793 -0.0401 828 ILE A CD1 6437 N N . ASN A 829 ? 1.5810 0.8701 1.4046 0.0974 -0.3705 -0.1275 829 ASN A N 6438 C CA . ASN A 829 ? 1.5586 0.8685 1.4181 0.0698 -0.4293 -0.1118 829 ASN A CA 6439 C C . ASN A 829 ? 1.6220 0.8085 1.4021 0.0607 -0.5204 -0.1409 829 ASN A C 6440 O O . ASN A 829 ? 1.6659 0.8386 1.5077 0.0074 -0.5887 -0.1196 829 ASN A O 6441 C CB . ASN A 829 ? 1.5373 0.9544 1.5428 0.0189 -0.4323 -0.0583 829 ASN A CB 6442 C CG . ASN A 829 ? 1.6197 1.0959 1.6855 -0.0039 -0.4798 -0.0324 829 ASN A CG 6443 O OD1 . ASN A 829 ? 1.6731 1.1285 1.6772 0.0243 -0.4932 -0.0525 829 ASN A OD1 6444 N ND2 . ASN A 829 ? 1.6937 1.2526 1.8846 -0.0546 -0.5053 0.0181 829 ASN A ND2 6445 N N . PRO A 830 ? 1.7474 0.8420 1.3865 0.1141 -0.5244 -0.1874 830 PRO A N 6446 C CA . PRO A 830 ? 1.8881 0.8433 1.4207 0.1199 -0.6147 -0.2254 830 PRO A CA 6447 C C . PRO A 830 ? 1.9400 0.8969 1.4896 0.0906 -0.6922 -0.2153 830 PRO A C 6448 O O . PRO A 830 ? 2.0416 0.8871 1.5359 0.0732 -0.7893 -0.2367 830 PRO A O 6449 C CB . PRO A 830 ? 2.0217 0.9119 1.3992 0.2001 -0.5757 -0.2712 830 PRO A CB 6450 C CG . PRO A 830 ? 1.9645 0.9733 1.3800 0.2205 -0.4895 -0.2465 830 PRO A CG 6451 C CD . PRO A 830 ? 1.7297 0.8484 1.2989 0.1733 -0.4483 -0.2025 830 PRO A CD 6452 N N . LEU A 831 ? 1.9609 1.0365 1.5833 0.0870 -0.6555 -0.1835 831 LEU A N 6453 C CA . LEU A 831 ? 2.0067 1.1011 1.6517 0.0657 -0.7233 -0.1701 831 LEU A CA 6454 C C . LEU A 831 ? 1.9619 1.1552 1.7796 -0.0067 -0.7603 -0.1138 831 LEU A C 6455 O O . LEU A 831 ? 1.8729 1.1084 1.7427 -0.0319 -0.8179 -0.0912 831 LEU A O 6456 C CB . LEU A 831 ? 1.9324 1.0957 1.5537 0.1086 -0.6687 -0.1648 831 LEU A CB 6457 C CG . LEU A 831 ? 2.0020 1.0860 1.4563 0.1783 -0.6365 -0.2071 831 LEU A CG 6458 C CD1 . LEU A 831 ? 1.9117 1.0806 1.3731 0.2096 -0.5665 -0.1860 831 LEU A CD1 6459 C CD2 . LEU A 831 ? 2.2943 1.2553 1.6166 0.1960 -0.7285 -0.2453 831 LEU A CD2 6460 N N . ARG A 832 ? 2.0472 1.2857 1.9543 -0.0373 -0.7252 -0.0867 832 ARG A N 6461 C CA . ARG A 832 ? 1.9309 1.2760 2.0052 -0.1046 -0.7495 -0.0237 832 ARG A CA 6462 C C . ARG A 832 ? 1.8225 1.3272 2.0066 -0.1033 -0.7179 0.0207 832 ARG A C 6463 O O . ARG A 832 ? 1.9778 1.5681 2.2838 -0.1526 -0.7681 0.0709 832 ARG A O 6464 C CB . ARG A 832 ? 1.9725 1.2325 2.0594 -0.1652 -0.8732 -0.0163 832 ARG A CB 6465 C CG . ARG A 832 ? 2.1434 1.2241 2.1107 -0.1612 -0.9183 -0.0637 832 ARG A CG 6466 C CD . ARG A 832 ? 2.2238 1.3212 2.2085 -0.1508 -0.8374 -0.0584 832 ARG A CD 6467 N NE . ARG A 832 ? 2.3888 1.3139 2.2499 -0.1328 -0.8744 -0.1074 832 ARG A NE 6468 C CZ . ARG A 832 ? 2.2606 1.1638 2.0877 -0.1019 -0.8088 -0.1225 832 ARG A CZ 6469 N NH1 . ARG A 832 ? 2.0713 1.1074 1.9744 -0.0900 -0.7071 -0.0941 832 ARG A NH1 6470 N NH2 . ARG A 832 ? 2.4003 1.1671 2.1158 -0.0743 -0.8385 -0.1616 832 ARG A NH2 6471 N N . ILE A 833 ? 1.6534 1.1982 1.7965 -0.0459 -0.6377 0.0051 833 ILE A N 6472 C CA . ILE A 833 ? 1.5548 1.2376 1.7872 -0.0309 -0.6009 0.0415 833 ILE A CA 6473 C C . ILE A 833 ? 1.5605 1.3738 1.9276 -0.0505 -0.5489 0.0927 833 ILE A C 6474 O O . ILE A 833 ? 1.8212 1.6251 2.1715 -0.0377 -0.4875 0.0844 833 ILE A O 6475 C CB . ILE A 833 ? 1.5249 1.1942 1.6682 0.0340 -0.5350 0.0119 833 ILE A CB 6476 C CG1 . ILE A 833 ? 1.6836 1.2279 1.6798 0.0603 -0.5757 -0.0347 833 ILE A CG1 6477 C CG2 . ILE A 833 ? 1.4746 1.2656 1.6985 0.0549 -0.5095 0.0458 833 ILE A CG2 6478 C CD1 . ILE A 833 ? 1.6862 1.2093 1.5898 0.1174 -0.5096 -0.0567 833 ILE A CD1 6479 N N . LYS A 834 ? 1.5713 1.5134 2.0711 -0.0778 -0.5727 0.1483 834 LYS A N 6480 C CA . LYS A 834 ? 1.7239 1.8057 2.3515 -0.0912 -0.5225 0.2047 834 LYS A CA 6481 C C . LYS A 834 ? 1.7166 1.9419 2.4141 -0.0448 -0.4728 0.2342 834 LYS A C 6482 O O . LYS A 834 ? 1.7049 1.9454 2.3969 -0.0245 -0.5029 0.2300 834 LYS A O 6483 C CB . LYS A 834 ? 1.8513 1.9818 2.5967 -0.1689 -0.5902 0.2618 834 LYS A CB 6484 C CG . LYS A 834 ? 1.8645 1.8534 2.5493 -0.2124 -0.6328 0.2393 834 LYS A CG 6485 C CD . LYS A 834 ? 1.6066 1.5732 2.2471 -0.1852 -0.5497 0.2226 834 LYS A CD 6486 C CE . LYS A 834 ? 1.6879 1.5074 2.2612 -0.2190 -0.5925 0.1976 834 LYS A CE 6487 N NZ . LYS A 834 ? 1.6158 1.4160 2.1468 -0.1905 -0.5150 0.1819 834 LYS A NZ 6488 N N . ILE A 835 ? 1.6911 2.0146 2.4445 -0.0222 -0.3988 0.2623 835 ILE A N 6489 C CA . ILE A 835 ? 1.5680 2.0214 2.3758 0.0351 -0.3466 0.2870 835 ILE A CA 6490 C C . ILE A 835 ? 1.5918 2.1968 2.5416 0.0140 -0.3882 0.3518 835 ILE A C 6491 O O . ILE A 835 ? 1.5711 2.2008 2.5240 0.0423 -0.4132 0.3484 835 ILE A O 6492 C CB . ILE A 835 ? 1.4135 1.9342 2.2401 0.0671 -0.2635 0.3030 835 ILE A CB 6493 C CG1 . ILE A 835 ? 1.0826 1.7280 1.9510 0.1388 -0.2139 0.3241 835 ILE A CG1 6494 C CG2 . ILE A 835 ? 1.3986 1.9944 2.3248 0.0082 -0.2702 0.3606 835 ILE A CG2 6495 C CD1 . ILE A 835 ? 1.0177 1.7245 1.8874 0.1820 -0.1359 0.3362 835 ILE A CD1 6496 N N . HIS A 870 ? 1.7992 1.6088 1.6332 0.0677 0.1675 0.6643 870 HIS A N 6497 C CA . HIS A 870 ? 1.7704 1.4543 1.6229 0.0404 0.1009 0.6200 870 HIS A CA 6498 C C . HIS A 870 ? 1.6379 1.3012 1.5044 0.0612 0.0947 0.5303 870 HIS A C 6499 O O . HIS A 870 ? 1.6152 1.2048 1.4394 0.0875 0.0690 0.4622 870 HIS A O 6500 C CB . HIS A 870 ? 1.9482 1.6013 1.8832 -0.0314 0.0590 0.6894 870 HIS A CB 6501 C CG . HIS A 870 ? 1.9291 1.4326 1.8517 -0.0491 -0.0145 0.6560 870 HIS A CG 6502 N ND1 . HIS A 870 ? 1.7538 1.1888 1.6943 -0.0465 -0.0499 0.5849 870 HIS A ND1 6503 C CD2 . HIS A 870 ? 1.9832 1.3905 1.8699 -0.0620 -0.0591 0.6843 870 HIS A CD2 6504 C CE1 . HIS A 870 ? 1.6809 0.9861 1.5929 -0.0511 -0.1109 0.5681 870 HIS A CE1 6505 N NE2 . HIS A 870 ? 1.9285 1.2105 1.8095 -0.0612 -0.1200 0.6265 870 HIS A NE2 6506 N N . THR A 871 ? 1.6863 1.4233 1.6163 0.0499 0.1190 0.5366 871 THR A N 6507 C CA . THR A 871 ? 1.5615 1.2848 1.5064 0.0673 0.1153 0.4609 871 THR A CA 6508 C C . THR A 871 ? 1.4392 1.2292 1.3397 0.1222 0.1651 0.4229 871 THR A C 6509 O O . THR A 871 ? 1.3589 1.2458 1.2641 0.1376 0.2118 0.4655 871 THR A O 6510 C CB . THR A 871 ? 1.4830 1.2306 1.5216 0.0231 0.1004 0.4836 871 THR A CB 6511 O OG1 . THR A 871 ? 1.8094 1.4709 1.8784 -0.0275 0.0409 0.5124 871 THR A OG1 6512 C CG2 . THR A 871 ? 1.2588 0.9894 1.3036 0.0440 0.0968 0.4078 871 THR A CG2 6513 N N . LEU A 872 ? 1.4280 1.1658 1.2844 0.1538 0.1528 0.3458 872 LEU A N 6514 C CA . LEU A 872 ? 1.3191 1.0922 1.1270 0.2030 0.1848 0.3031 872 LEU A CA 6515 C C . LEU A 872 ? 1.3951 1.1618 1.2408 0.2045 0.1794 0.2518 872 LEU A C 6516 O O . LEU A 872 ? 1.4271 1.1316 1.2722 0.2009 0.1483 0.2035 872 LEU A O 6517 C CB . LEU A 872 ? 1.3549 1.0752 1.0757 0.2370 0.1701 0.2627 872 LEU A CB 6518 C CG . LEU A 872 ? 1.4945 1.2172 1.1581 0.2453 0.1752 0.3091 872 LEU A CG 6519 C CD1 . LEU A 872 ? 1.5001 1.1653 1.0826 0.2769 0.1493 0.2636 872 LEU A CD1 6520 C CD2 . LEU A 872 ? 1.5896 1.4035 1.2278 0.2707 0.2287 0.3586 872 LEU A CD2 6521 N N . GLY A 873 ? 1.4873 1.3259 1.3656 0.2139 0.2120 0.2668 873 GLY A N 6522 C CA . GLY A 873 ? 1.5355 1.3711 1.4435 0.2197 0.2091 0.2231 873 GLY A CA 6523 C C . GLY A 873 ? 1.5980 1.4427 1.4401 0.2748 0.2324 0.1835 873 GLY A C 6524 O O . GLY A 873 ? 1.4841 1.3248 1.2498 0.3086 0.2441 0.1820 873 GLY A O 6525 N N . CYS A 874 ? 1.6632 1.5094 1.5255 0.2862 0.2339 0.1505 874 CYS A N 6526 C CA . CYS A 874 ? 1.3924 1.2326 1.1883 0.3408 0.2490 0.1128 874 CYS A CA 6527 C C . CYS A 874 ? 1.4339 1.3631 1.2128 0.3827 0.2980 0.1539 874 CYS A C 6528 O O . CYS A 874 ? 1.7624 1.6851 1.4544 0.4426 0.3147 0.1307 874 CYS A O 6529 C CB . CYS A 874 ? 1.0944 0.9086 0.9184 0.3408 0.2351 0.0734 874 CYS A CB 6530 S SG . CYS A 874 ? 2.0159 1.7638 1.7460 0.3954 0.2237 0.0120 874 CYS A SG 6531 N N . GLY A 875 ? 1.3258 1.3392 1.1871 0.3528 0.3183 0.2176 875 GLY A N 6532 C CA . GLY A 875 ? 1.3971 1.5202 1.2583 0.3850 0.3693 0.2775 875 GLY A CA 6533 C C . GLY A 875 ? 1.7038 1.8170 1.4981 0.3905 0.3759 0.3033 875 GLY A C 6534 O O . GLY A 875 ? 1.8538 1.8936 1.6450 0.3491 0.3378 0.2945 875 GLY A O 6535 N N . VAL A 876 ? 1.6715 1.8579 1.4049 0.4492 0.4245 0.3338 876 VAL A N 6536 C CA . VAL A 876 ? 1.9176 2.1037 1.5663 0.4697 0.4381 0.3614 876 VAL A CA 6537 C C . VAL A 876 ? 1.7948 1.8472 1.3579 0.4668 0.3874 0.2971 876 VAL A C 6538 O O . VAL A 876 ? 1.5292 1.5581 1.0582 0.4507 0.3760 0.3222 876 VAL A O 6539 C CB . VAL A 876 ? 1.7682 2.0318 1.4988 0.4114 0.4510 0.4602 876 VAL A CB 6540 C CG1 . VAL A 876 ? 1.8361 2.2481 1.6690 0.4077 0.4969 0.5336 876 VAL A CG1 6541 C CG2 . VAL A 876 ? 1.4091 1.5884 1.2077 0.3284 0.3919 0.4586 876 VAL A CG2 6542 N N . ALA A 877 ? 1.9246 1.8947 1.4566 0.4829 0.3557 0.2191 877 ALA A N 6543 C CA . ALA A 877 ? 1.6735 1.5308 1.1310 0.4848 0.3061 0.1591 877 ALA A CA 6544 C C . ALA A 877 ? 1.7778 1.5689 1.1855 0.5216 0.2841 0.0864 877 ALA A C 6545 O O . ALA A 877 ? 1.9221 1.7427 1.3726 0.5321 0.3006 0.0792 877 ALA A O 6546 C CB . ALA A 877 ? 1.4617 1.2720 0.9941 0.4150 0.2638 0.1588 877 ALA A CB 6547 N N . GLN A 878 ? 1.8289 1.5274 1.1487 0.5387 0.2411 0.0359 878 GLN A N 6548 C CA . GLN A 878 ? 1.7847 1.4019 1.0552 0.5650 0.2062 -0.0301 878 GLN A CA 6549 C C . GLN A 878 ? 1.5801 1.1810 0.9581 0.5094 0.1826 -0.0452 878 GLN A C 6550 O O . GLN A 878 ? 1.3895 0.9852 0.8365 0.4538 0.1608 -0.0350 878 GLN A O 6551 C CB . GLN A 878 ? 1.9985 1.5182 1.1672 0.5800 0.1517 -0.0735 878 GLN A CB 6552 C CG . GLN A 878 ? 1.9089 1.3302 1.0053 0.6122 0.1070 -0.1379 878 GLN A CG 6553 C CD . GLN A 878 ? 2.3319 1.7451 1.3075 0.6995 0.1316 -0.1543 878 GLN A CD 6554 O OE1 . GLN A 878 ? 2.5175 2.0127 1.4625 0.7395 0.1880 -0.1135 878 GLN A OE1 6555 N NE2 . GLN A 878 ? 2.4784 1.8163 1.4189 0.7069 0.0793 -0.1953 878 GLN A NE2 6556 N N . CYS A 879 ? 1.7942 1.3866 1.1793 0.5312 0.1876 -0.0686 879 CYS A N 6557 C CA . CYS A 879 ? 1.6920 1.2830 1.1765 0.4840 0.1743 -0.0740 879 CYS A CA 6558 C C . CYS A 879 ? 1.4684 0.9638 0.9302 0.4764 0.1215 -0.1246 879 CYS A C 6559 O O . CYS A 879 ? 1.4603 0.8903 0.8332 0.5229 0.1020 -0.1613 879 CYS A O 6560 C CB . CYS A 879 ? 1.5464 1.2096 1.0802 0.5032 0.2170 -0.0512 879 CYS A CB 6561 S SG . CYS A 879 ? 1.9834 1.6477 1.6294 0.4501 0.2016 -0.0539 879 CYS A SG 6562 N N . LEU A 880 ? 1.2644 0.7507 0.8050 0.4188 0.0963 -0.1234 880 LEU A N 6563 C CA . LEU A 880 ? 1.2568 0.6758 0.8066 0.3990 0.0516 -0.1543 880 LEU A CA 6564 C C . LEU A 880 ? 1.2270 0.6793 0.8607 0.3745 0.0677 -0.1420 880 LEU A C 6565 O O . LEU A 880 ? 1.0698 0.5698 0.7780 0.3372 0.0801 -0.1175 880 LEU A O 6566 C CB . LEU A 880 ? 1.4109 0.8041 0.9822 0.3572 0.0090 -0.1574 880 LEU A CB 6567 C CG . LEU A 880 ? 1.3628 0.6971 0.9534 0.3286 -0.0420 -0.1772 880 LEU A CG 6568 C CD1 . LEU A 880 ? 1.3742 0.6607 0.9288 0.3168 -0.0961 -0.1902 880 LEU A CD1 6569 C CD2 . LEU A 880 ? 1.1311 0.5135 0.8259 0.2829 -0.0329 -0.1544 880 LEU A CD2 6570 N N . LYS A 881 ? 1.4030 0.8248 1.0170 0.3986 0.0636 -0.1599 881 LYS A N 6571 C CA . LYS A 881 ? 1.1895 0.6442 0.8753 0.3797 0.0770 -0.1471 881 LYS A CA 6572 C C . LYS A 881 ? 1.1964 0.6067 0.9187 0.3373 0.0382 -0.1551 881 LYS A C 6573 O O . LYS A 881 ? 1.5055 0.8514 1.1913 0.3311 -0.0039 -0.1745 881 LYS A O 6574 C CB . LYS A 881 ? 1.4409 0.9156 1.1046 0.4185 0.0934 -0.1504 881 LYS A CB 6575 C CG . LYS A 881 ? 1.4785 1.0383 1.1985 0.4319 0.1407 -0.1193 881 LYS A CG 6576 C CD . LYS A 881 ? 1.1689 0.7579 0.8670 0.4775 0.1564 -0.1205 881 LYS A CD 6577 C CE . LYS A 881 ? 1.3878 0.9608 0.9900 0.5262 0.1588 -0.1343 881 LYS A CE 6578 N NZ . LYS A 881 ? 1.3979 1.0162 0.9834 0.5393 0.1914 -0.1112 881 LYS A NZ 6579 N N . ILE A 882 ? 1.1526 0.5974 0.9447 0.3087 0.0510 -0.1360 882 ILE A N 6580 C CA . ILE A 882 ? 1.1481 0.5670 0.9776 0.2741 0.0246 -0.1337 882 ILE A CA 6581 C C . ILE A 882 ? 1.1125 0.5543 0.9782 0.2753 0.0413 -0.1233 882 ILE A C 6582 O O . ILE A 882 ? 1.2842 0.7816 1.1909 0.2685 0.0673 -0.1059 882 ILE A O 6583 C CB . ILE A 882 ? 1.1483 0.6045 1.0283 0.2344 0.0208 -0.1158 882 ILE A CB 6584 C CG1 . ILE A 882 ? 1.0880 0.5278 0.9387 0.2321 -0.0009 -0.1234 882 ILE A CG1 6585 C CG2 . ILE A 882 ? 1.1406 0.5904 1.0629 0.2026 0.0018 -0.1031 882 ILE A CG2 6586 C CD1 . ILE A 882 ? 1.0581 0.5387 0.9600 0.2013 -0.0071 -0.1052 882 ILE A CD1 6587 N N . VAL A 883 ? 1.1271 0.5299 0.9804 0.2778 0.0203 -0.1315 883 VAL A N 6588 C CA . VAL A 883 ? 1.3134 0.7359 1.1957 0.2826 0.0313 -0.1221 883 VAL A CA 6589 C C . VAL A 883 ? 1.1525 0.5437 1.0627 0.2508 0.0114 -0.1081 883 VAL A C 6590 O O . VAL A 883 ? 1.2974 0.6332 1.1964 0.2298 -0.0221 -0.1085 883 VAL A O 6591 C CB . VAL A 883 ? 1.0684 0.4697 0.9115 0.3176 0.0256 -0.1372 883 VAL A CB 6592 C CG1 . VAL A 883 ? 1.1602 0.4772 0.9515 0.3131 -0.0173 -0.1554 883 VAL A CG1 6593 C CG2 . VAL A 883 ? 1.0537 0.4713 0.9281 0.3246 0.0318 -0.1265 883 VAL A CG2 6594 N N . CYS A 884 ? 1.0225 0.4471 0.9670 0.2474 0.0285 -0.0919 884 CYS A N 6595 C CA . CYS A 884 ? 1.0119 0.4311 0.9832 0.2170 0.0174 -0.0705 884 CYS A CA 6596 C C . CYS A 884 ? 1.0503 0.4604 1.0259 0.2292 0.0175 -0.0621 884 CYS A C 6597 O O . CYS A 884 ? 0.9635 0.4070 0.9463 0.2533 0.0354 -0.0655 884 CYS A O 6598 C CB . CYS A 884 ? 1.0218 0.5052 1.0269 0.1957 0.0367 -0.0547 884 CYS A CB 6599 S SG . CYS A 884 ? 1.4368 0.9377 1.4443 0.1821 0.0344 -0.0588 884 CYS A SG 6600 N N . GLN A 885 ? 1.0167 0.3859 0.9935 0.2094 -0.0056 -0.0452 885 GLN A N 6601 C CA . GLN A 885 ? 0.9892 0.3496 0.9695 0.2165 -0.0081 -0.0305 885 GLN A CA 6602 C C . GLN A 885 ? 1.1124 0.5229 1.1190 0.1893 0.0047 0.0000 885 GLN A C 6603 O O . GLN A 885 ? 1.0983 0.5203 1.1206 0.1588 0.0005 0.0217 885 GLN A O 6604 C CB . GLN A 885 ? 1.0978 0.3684 1.0519 0.2173 -0.0455 -0.0283 885 GLN A CB 6605 C CG . GLN A 885 ? 1.4881 0.7351 1.4116 0.2355 -0.0562 -0.0588 885 GLN A CG 6606 C CD . GLN A 885 ? 1.8663 1.0553 1.7726 0.2064 -0.0913 -0.0604 885 GLN A CD 6607 O OE1 . GLN A 885 ? 1.9938 1.1320 1.9087 0.1713 -0.1250 -0.0350 885 GLN A OE1 6608 N NE2 . GLN A 885 ? 1.5941 0.7926 1.4792 0.2175 -0.0879 -0.0851 885 GLN A NE2 6609 N N . VAL A 886 ? 1.1668 0.6113 1.1768 0.2037 0.0186 0.0035 886 VAL A N 6610 C CA . VAL A 886 ? 0.9004 0.3869 0.9147 0.1912 0.0309 0.0261 886 VAL A CA 6611 C C . VAL A 886 ? 1.0290 0.4948 1.0310 0.1916 0.0200 0.0515 886 VAL A C 6612 O O . VAL A 886 ? 0.9935 0.4319 0.9879 0.2117 0.0078 0.0443 886 VAL A O 6613 C CB . VAL A 886 ? 0.8577 0.3871 0.8721 0.2056 0.0452 0.0109 886 VAL A CB 6614 C CG1 . VAL A 886 ? 0.8559 0.4166 0.8546 0.2030 0.0557 0.0261 886 VAL A CG1 6615 C CG2 . VAL A 886 ? 1.0269 0.5705 1.0524 0.2063 0.0537 -0.0100 886 VAL A CG2 6616 N N . GLY A 887 ? 1.0125 0.4997 1.0137 0.1725 0.0263 0.0857 887 GLY A N 6617 C CA . GLY A 887 ? 1.0292 0.5013 1.0141 0.1704 0.0183 0.1190 887 GLY A CA 6618 C C . GLY A 887 ? 1.0228 0.5256 0.9778 0.1947 0.0289 0.1165 887 GLY A C 6619 O O . GLY A 887 ? 1.1851 0.6984 1.1373 0.2133 0.0291 0.0842 887 GLY A O 6620 N N . ARG A 888 ? 1.0827 0.5977 1.0129 0.1936 0.0334 0.1539 888 ARG A N 6621 C CA . ARG A 888 ? 1.1462 0.6775 1.0306 0.2211 0.0359 0.1504 888 ARG A CA 6622 C C . ARG A 888 ? 1.2437 0.8214 1.1039 0.2372 0.0577 0.1354 888 ARG A C 6623 O O . ARG A 888 ? 1.1594 0.7816 1.0200 0.2330 0.0829 0.1605 888 ARG A O 6624 C CB . ARG A 888 ? 1.1817 0.7088 1.0337 0.2208 0.0347 0.1979 888 ARG A CB 6625 C CG . ARG A 888 ? 1.2170 0.7427 1.0090 0.2533 0.0260 0.1915 888 ARG A CG 6626 C CD . ARG A 888 ? 1.4074 0.9453 1.1544 0.2572 0.0354 0.2452 888 ARG A CD 6627 N NE . ARG A 888 ? 1.4695 0.9972 1.1453 0.2922 0.0212 0.2367 888 ARG A NE 6628 C CZ . ARG A 888 ? 1.5695 1.0545 1.2307 0.2994 -0.0103 0.2418 888 ARG A CZ 6629 N NH1 . ARG A 888 ? 1.6070 1.0520 1.3162 0.2795 -0.0282 0.2536 888 ARG A NH1 6630 N NH2 . ARG A 888 ? 1.5491 1.0252 1.1418 0.3309 -0.0287 0.2335 888 ARG A NH2 6631 N N . LEU A 889 ? 1.0821 0.6495 0.9237 0.2566 0.0445 0.0974 889 LEU A N 6632 C CA . LEU A 889 ? 1.1583 0.7439 0.9598 0.2789 0.0529 0.0773 889 LEU A CA 6633 C C . LEU A 889 ? 1.3619 0.9245 1.0940 0.3081 0.0310 0.0675 889 LEU A C 6634 O O . LEU A 889 ? 1.3635 0.8965 1.1029 0.3066 -0.0022 0.0487 889 LEU A O 6635 C CB . LEU A 889 ? 1.0004 0.5794 0.8350 0.2717 0.0457 0.0414 889 LEU A CB 6636 C CG . LEU A 889 ? 0.9945 0.5973 0.8743 0.2535 0.0668 0.0433 889 LEU A CG 6637 C CD1 . LEU A 889 ? 1.1103 0.7042 1.0066 0.2522 0.0585 0.0108 889 LEU A CD1 6638 C CD2 . LEU A 889 ? 1.0842 0.7318 0.9468 0.2632 0.0952 0.0677 889 LEU A CD2 6639 N N . ASP A 890 ? 1.3896 0.9706 1.0536 0.3375 0.0485 0.0826 890 ASP A N 6640 C CA . ASP A 890 ? 1.3592 0.9087 0.9338 0.3740 0.0244 0.0688 890 ASP A CA 6641 C C . ASP A 890 ? 1.3457 0.8673 0.8699 0.4017 0.0088 0.0252 890 ASP A C 6642 O O . ASP A 890 ? 1.3093 0.8351 0.8800 0.3870 0.0136 0.0066 890 ASP A O 6643 C CB . ASP A 890 ? 1.5097 1.0904 1.0191 0.4010 0.0518 0.1105 890 ASP A CB 6644 C CG . ASP A 890 ? 1.5551 1.1528 1.1147 0.3683 0.0622 0.1605 890 ASP A CG 6645 O OD1 . ASP A 890 ? 1.5769 1.1361 1.1308 0.3631 0.0313 0.1633 890 ASP A OD1 6646 O OD2 . ASP A 890 ? 1.6253 1.2714 1.2320 0.3470 0.0958 0.1986 890 ASP A OD2 6647 N N . ARG A 891 ? 1.3781 0.8610 0.7995 0.4437 -0.0153 0.0084 891 ARG A N 6648 C CA . ARG A 891 ? 1.5326 0.9612 0.8857 0.4754 -0.0450 -0.0372 891 ARG A CA 6649 C C . ARG A 891 ? 1.8543 1.3149 1.2010 0.4994 -0.0053 -0.0426 891 ARG A C 6650 O O . ARG A 891 ? 1.3771 0.8222 0.7714 0.4800 -0.0150 -0.0646 891 ARG A O 6651 C CB . ARG A 891 ? 1.5727 0.9494 0.7917 0.5284 -0.0754 -0.0524 891 ARG A CB 6652 C CG . ARG A 891 ? 1.9631 1.3151 1.1805 0.5111 -0.1152 -0.0416 891 ARG A CG 6653 C CD . ARG A 891 ? 2.0676 1.3647 1.1371 0.5682 -0.1474 -0.0566 891 ARG A CD 6654 N NE . ARG A 891 ? 2.3889 1.5903 1.3876 0.5874 -0.2149 -0.1112 891 ARG A NE 6655 C CZ . ARG A 891 ? 2.6321 1.7897 1.5256 0.6435 -0.2152 -0.1446 891 ARG A CZ 6656 N NH1 . ARG A 891 ? 2.6089 1.8302 1.4636 0.6892 -0.1438 -0.1252 891 ARG A NH1 6657 N NH2 . ARG A 891 ? 2.7626 1.8122 1.5909 0.6552 -0.2903 -0.1947 891 ARG A NH2 6658 N N . GLY A 892 ? 2.0979 1.6115 1.3890 0.5432 0.0409 -0.0169 892 GLY A N 6659 C CA . GLY A 892 ? 2.1836 1.7362 1.4583 0.5806 0.0776 -0.0206 892 GLY A CA 6660 C C . GLY A 892 ? 1.9105 1.5270 1.3061 0.5358 0.1095 0.0005 892 GLY A C 6661 O O . GLY A 892 ? 1.9387 1.5909 1.3338 0.5638 0.1355 -0.0025 892 GLY A O 6662 N N . LYS A 893 ? 1.6504 1.2770 1.1430 0.4720 0.1041 0.0196 893 LYS A N 6663 C CA . LYS A 893 ? 1.6651 1.3483 1.2602 0.4314 0.1311 0.0431 893 LYS A CA 6664 C C . LYS A 893 ? 1.3793 1.0199 1.0395 0.3899 0.1027 0.0134 893 LYS A C 6665 O O . LYS A 893 ? 1.1094 0.6931 0.7659 0.3759 0.0650 -0.0102 893 LYS A O 6666 C CB . LYS A 893 ? 1.6157 1.3488 1.2648 0.3961 0.1524 0.0975 893 LYS A CB 6667 C CG . LYS A 893 ? 1.8418 1.6391 1.5817 0.3610 0.1782 0.1305 893 LYS A CG 6668 C CD . LYS A 893 ? 1.9008 1.7673 1.6292 0.3999 0.2123 0.1389 893 LYS A CD 6669 C CE . LYS A 893 ? 1.5912 1.5056 1.4147 0.3627 0.2217 0.1557 893 LYS A CE 6670 N NZ . LYS A 893 ? 1.6838 1.6364 1.5827 0.3087 0.2255 0.2108 893 LYS A NZ 6671 N N . SER A 894 ? 1.2444 0.9217 0.9654 0.3722 0.1214 0.0195 894 SER A N 6672 C CA . SER A 894 ? 1.0011 0.6512 0.7811 0.3363 0.1032 -0.0008 894 SER A CA 6673 C C . SER A 894 ? 0.9946 0.6916 0.8503 0.3019 0.1233 0.0259 894 SER A C 6674 O O . SER A 894 ? 1.1019 0.8530 0.9745 0.2990 0.1468 0.0637 894 SER A O 6675 C CB . SER A 894 ? 1.2590 0.8765 1.0108 0.3584 0.0895 -0.0346 894 SER A CB 6676 O OG . SER A 894 ? 1.5164 1.1811 1.2552 0.3909 0.1181 -0.0260 894 SER A OG 6677 N N . ALA A 895 ? 1.1628 0.8388 1.0622 0.2754 0.1106 0.0094 895 ALA A N 6678 C CA . ALA A 895 ? 0.9438 0.6450 0.9018 0.2449 0.1180 0.0263 895 ALA A CA 6679 C C . ALA A 895 ? 1.1132 0.8100 1.0876 0.2433 0.1144 0.0053 895 ALA A C 6680 O O . ALA A 895 ? 1.3743 1.0330 1.3368 0.2454 0.0995 -0.0201 895 ALA A O 6681 C CB . ALA A 895 ? 0.9256 0.5944 0.9084 0.2178 0.1030 0.0297 895 ALA A CB 6682 N N . ILE A 896 ? 1.0130 0.7532 1.0191 0.2373 0.1257 0.0217 896 ILE A N 6683 C CA . ILE A 896 ? 0.9888 0.7297 1.0027 0.2432 0.1227 0.0050 896 ILE A CA 6684 C C . ILE A 896 ? 0.9379 0.6869 0.9975 0.2125 0.1140 0.0127 896 ILE A C 6685 O O . ILE A 896 ? 1.1274 0.9069 1.2226 0.1907 0.1132 0.0409 896 ILE A O 6686 C CB . ILE A 896 ? 0.8492 0.6371 0.8473 0.2807 0.1402 0.0120 896 ILE A CB 6687 C CG1 . ILE A 896 ? 0.8545 0.6320 0.7907 0.3192 0.1474 0.0061 896 ILE A CG1 6688 C CG2 . ILE A 896 ? 1.0837 0.8508 1.0735 0.2950 0.1307 -0.0110 896 ILE A CG2 6689 C CD1 . ILE A 896 ? 0.9453 0.7796 0.8563 0.3692 0.1717 0.0177 896 ILE A CD1 6690 N N . LEU A 897 ? 0.9085 0.6261 0.9635 0.2100 0.1029 -0.0098 897 LEU A N 6691 C CA . LEU A 897 ? 0.9142 0.6302 0.9939 0.1895 0.0902 -0.0087 897 LEU A CA 6692 C C . LEU A 897 ? 1.0668 0.8029 1.1487 0.2038 0.0901 -0.0132 897 LEU A C 6693 O O . LEU A 897 ? 1.0832 0.7920 1.1377 0.2198 0.0896 -0.0309 897 LEU A O 6694 C CB . LEU A 897 ? 0.7664 0.4306 0.8300 0.1806 0.0789 -0.0278 897 LEU A CB 6695 C CG . LEU A 897 ? 0.7631 0.4088 0.8246 0.1719 0.0635 -0.0365 897 LEU A CG 6696 C CD1 . LEU A 897 ? 0.8154 0.4683 0.9033 0.1490 0.0432 -0.0206 897 LEU A CD1 6697 C CD2 . LEU A 897 ? 0.7612 0.3657 0.7953 0.1781 0.0615 -0.0536 897 LEU A CD2 6698 N N . TYR A 898 ? 0.9967 0.7814 1.1163 0.1958 0.0866 0.0076 898 TYR A N 6699 C CA . TYR A 898 ? 0.8396 0.6510 0.9676 0.2119 0.0837 0.0070 898 TYR A CA 6700 C C . TYR A 898 ? 0.8610 0.6489 0.9970 0.1891 0.0577 0.0011 898 TYR A C 6701 O O . TYR A 898 ? 1.0651 0.8663 1.2342 0.1609 0.0384 0.0173 898 TYR A O 6702 C CB . TYR A 898 ? 0.8298 0.7298 1.0010 0.2254 0.0974 0.0393 898 TYR A CB 6703 C CG . TYR A 898 ? 0.9650 0.8944 1.1157 0.2574 0.1256 0.0477 898 TYR A CG 6704 C CD1 . TYR A 898 ? 1.0741 1.0202 1.2359 0.2400 0.1351 0.0699 898 TYR A CD1 6705 C CD2 . TYR A 898 ? 0.8062 0.7387 0.9168 0.3094 0.1391 0.0331 898 TYR A CD2 6706 C CE1 . TYR A 898 ? 1.2812 1.2539 1.4122 0.2741 0.1609 0.0785 898 TYR A CE1 6707 C CE2 . TYR A 898 ? 0.8211 0.7711 0.8943 0.3477 0.1615 0.0361 898 TYR A CE2 6708 C CZ . TYR A 898 ? 1.1368 1.1113 1.2195 0.3303 0.1742 0.0595 898 TYR A CZ 6709 O OH . TYR A 898 ? 1.1790 1.1704 1.2128 0.3730 0.1965 0.0633 898 TYR A OH 6710 N N . VAL A 899 ? 0.8219 0.5702 0.9230 0.2007 0.0527 -0.0196 899 VAL A N 6711 C CA . VAL A 899 ? 0.8289 0.5518 0.9197 0.1882 0.0291 -0.0268 899 VAL A CA 6712 C C . VAL A 899 ? 0.9809 0.7323 1.0821 0.2027 0.0195 -0.0208 899 VAL A C 6713 O O . VAL A 899 ? 1.1753 0.9110 1.2504 0.2261 0.0276 -0.0284 899 VAL A O 6714 C CB . VAL A 899 ? 0.8536 0.5189 0.8945 0.1922 0.0323 -0.0467 899 VAL A CB 6715 C CG1 . VAL A 899 ? 0.9927 0.6309 1.0055 0.1889 0.0100 -0.0549 899 VAL A CG1 6716 C CG2 . VAL A 899 ? 0.8293 0.4726 0.8633 0.1849 0.0413 -0.0521 899 VAL A CG2 6717 N N . LYS A 900 ? 0.8935 0.6837 1.0353 0.1872 -0.0034 -0.0044 900 LYS A N 6718 C CA . LYS A 900 ? 0.9247 0.7474 1.0818 0.2017 -0.0179 0.0034 900 LYS A CA 6719 C C . LYS A 900 ? 0.9925 0.7629 1.1099 0.1914 -0.0497 -0.0111 900 LYS A C 6720 O O . LYS A 900 ? 1.1858 0.9351 1.3044 0.1646 -0.0803 -0.0126 900 LYS A O 6721 C CB . LYS A 900 ? 0.9739 0.8899 1.2108 0.1932 -0.0264 0.0381 900 LYS A CB 6722 C CG . LYS A 900 ? 1.0783 1.0424 1.3400 0.2154 -0.0404 0.0494 900 LYS A CG 6723 C CD . LYS A 900 ? 1.1315 1.2167 1.4849 0.2174 -0.0370 0.0924 900 LYS A CD 6724 C CE . LYS A 900 ? 1.3014 1.4169 1.7192 0.1609 -0.0760 0.1209 900 LYS A CE 6725 N NZ . LYS A 900 ? 1.2982 1.5535 1.8235 0.1582 -0.0750 0.1758 900 LYS A NZ 6726 N N . SER A 901 ? 0.9379 0.6792 1.0119 0.2146 -0.0459 -0.0211 901 SER A N 6727 C CA . SER A 901 ? 1.0124 0.7060 1.0341 0.2130 -0.0702 -0.0323 901 SER A CA 6728 C C . SER A 901 ? 1.0540 0.7644 1.0753 0.2324 -0.0865 -0.0230 901 SER A C 6729 O O . SER A 901 ? 1.0994 0.8459 1.1502 0.2544 -0.0737 -0.0125 901 SER A O 6730 C CB . SER A 901 ? 1.1262 0.7639 1.0848 0.2207 -0.0478 -0.0461 901 SER A CB 6731 O OG . SER A 901 ? 1.0363 0.6692 0.9854 0.2383 -0.0286 -0.0391 901 SER A OG 6732 N N . LEU A 902 ? 1.1190 0.7974 1.0977 0.2304 -0.1171 -0.0286 902 LEU A N 6733 C CA . LEU A 902 ? 1.1356 0.8212 1.1039 0.2499 -0.1369 -0.0191 902 LEU A CA 6734 C C . LEU A 902 ? 1.2928 0.9170 1.1772 0.2643 -0.1292 -0.0239 902 LEU A C 6735 O O . LEU A 902 ? 1.4238 1.0063 1.2498 0.2593 -0.1292 -0.0363 902 LEU A O 6736 C CB . LEU A 902 ? 1.1547 0.8639 1.1473 0.2356 -0.1882 -0.0136 902 LEU A CB 6737 C CG . LEU A 902 ? 1.1888 0.9810 1.2831 0.2163 -0.2009 0.0073 902 LEU A CG 6738 C CD1 . LEU A 902 ? 1.2167 1.0245 1.3362 0.1934 -0.2636 0.0165 902 LEU A CD1 6739 C CD2 . LEU A 902 ? 1.2577 1.1217 1.4072 0.2477 -0.1725 0.0267 902 LEU A CD2 6740 N N . LEU A 903 ? 1.3921 1.0107 1.2678 0.2857 -0.1226 -0.0110 903 LEU A N 6741 C CA . LEU A 903 ? 1.2303 0.7992 1.0336 0.2956 -0.1202 -0.0026 903 LEU A CA 6742 C C . LEU A 903 ? 1.3035 0.8610 1.0616 0.2996 -0.1578 -0.0050 903 LEU A C 6743 O O . LEU A 903 ? 1.3760 0.9628 1.1675 0.3046 -0.1923 -0.0012 903 LEU A O 6744 C CB . LEU A 903 ? 1.2262 0.7791 1.0313 0.3150 -0.1171 0.0150 903 LEU A CB 6745 C CG . LEU A 903 ? 1.3923 0.8939 1.1319 0.3171 -0.1113 0.0362 903 LEU A CG 6746 C CD1 . LEU A 903 ? 1.4678 0.9532 1.2028 0.2989 -0.0769 0.0428 903 LEU A CD1 6747 C CD2 . LEU A 903 ? 1.3562 0.8300 1.0916 0.3385 -0.1304 0.0543 903 LEU A CD2 6748 N N . TRP A 904 ? 1.3632 0.8816 1.0429 0.3019 -0.1528 -0.0101 904 TRP A N 6749 C CA . TRP A 904 ? 1.4445 0.9384 1.0599 0.3121 -0.1932 -0.0170 904 TRP A CA 6750 C C . TRP A 904 ? 1.5579 1.0335 1.1237 0.3323 -0.1943 0.0089 904 TRP A C 6751 O O . TRP A 904 ? 1.9465 1.4010 1.4571 0.3402 -0.1623 0.0264 904 TRP A O 6752 C CB . TRP A 904 ? 1.5607 1.0155 1.0972 0.3178 -0.1892 -0.0387 904 TRP A CB 6753 C CG . TRP A 904 ? 1.6359 1.0518 1.1027 0.3279 -0.2447 -0.0579 904 TRP A CG 6754 C CD1 . TRP A 904 ? 1.7732 1.1580 1.1476 0.3539 -0.2641 -0.0517 904 TRP A CD1 6755 C CD2 . TRP A 904 ? 1.6067 1.0018 1.0847 0.3107 -0.2953 -0.0852 904 TRP A CD2 6756 N NE1 . TRP A 904 ? 1.8205 1.1623 1.1411 0.3575 -0.3265 -0.0787 904 TRP A NE1 6757 C CE2 . TRP A 904 ? 1.7848 1.1289 1.1710 0.3281 -0.3499 -0.0990 904 TRP A CE2 6758 C CE3 . TRP A 904 ? 1.5559 0.9659 1.1106 0.2802 -0.3043 -0.0957 904 TRP A CE3 6759 C CZ2 . TRP A 904 ? 1.8504 1.1497 1.2207 0.3129 -0.4200 -0.1257 904 TRP A CZ2 6760 C CZ3 . TRP A 904 ? 1.7440 1.1151 1.2898 0.2620 -0.3699 -0.1159 904 TRP A CZ3 6761 C CH2 . TRP A 904 ? 1.8237 1.1360 1.2787 0.2769 -0.4306 -0.1321 904 TRP A CH2 6762 N N . THR A 905 ? 1.5548 1.0443 1.1447 0.3402 -0.2328 0.0168 905 THR A N 6763 C CA . THR A 905 ? 1.6215 1.0916 1.1791 0.3598 -0.2374 0.0450 905 THR A CA 6764 C C . THR A 905 ? 1.8548 1.2849 1.3016 0.3755 -0.2529 0.0518 905 THR A C 6765 O O . THR A 905 ? 2.1186 1.5231 1.5126 0.3874 -0.2382 0.0828 905 THR A O 6766 C CB . THR A 905 ? 1.5521 1.0563 1.1746 0.3722 -0.2738 0.0517 905 THR A CB 6767 O OG1 . THR A 905 ? 1.4280 0.9811 1.1461 0.3652 -0.2574 0.0438 905 THR A OG1 6768 C CG2 . THR A 905 ? 1.8135 1.2851 1.4067 0.3956 -0.2768 0.0809 905 THR A CG2 6769 N N . GLU A 906 ? 1.6756 1.0952 1.0819 0.3759 -0.2858 0.0245 906 GLU A N 6770 C CA . GLU A 906 ? 1.8196 1.1946 1.1029 0.3999 -0.3083 0.0227 906 GLU A CA 6771 C C . GLU A 906 ? 1.8972 1.2545 1.0973 0.4162 -0.2520 0.0414 906 GLU A C 6772 O O . GLU A 906 ? 2.0266 1.3616 1.1324 0.4410 -0.2511 0.0648 906 GLU A O 6773 C CB . GLU A 906 ? 1.9412 1.2904 1.1904 0.3970 -0.3583 -0.0178 906 GLU A CB 6774 C CG . GLU A 906 ? 2.1399 1.4290 1.2410 0.4305 -0.3897 -0.0293 906 GLU A CG 6775 C CD . GLU A 906 ? 2.3302 1.5684 1.3809 0.4299 -0.4403 -0.0761 906 GLU A CD 6776 O OE1 . GLU A 906 ? 2.5111 1.6883 1.4371 0.4590 -0.4866 -0.0942 906 GLU A OE1 6777 O OE2 . GLU A 906 ? 2.4076 1.6580 1.5360 0.4014 -0.4380 -0.0944 906 GLU A OE2 6778 N N . THR A 907 ? 1.8825 1.2588 1.1219 0.4029 -0.2044 0.0367 907 THR A N 6779 C CA . THR A 907 ? 2.0301 1.4108 1.2082 0.4178 -0.1488 0.0585 907 THR A CA 6780 C C . THR A 907 ? 1.8103 1.2075 1.0132 0.4072 -0.1161 0.1144 907 THR A C 6781 O O . THR A 907 ? 1.9766 1.3790 1.1087 0.4235 -0.0864 0.1525 907 THR A O 6782 C CB . THR A 907 ? 1.9953 1.3947 1.2130 0.4080 -0.1142 0.0365 907 THR A CB 6783 O OG1 . THR A 907 ? 2.1106 1.5352 1.4481 0.3735 -0.1085 0.0369 907 THR A OG1 6784 C CG2 . THR A 907 ? 1.9875 1.3509 1.1583 0.4215 -0.1512 -0.0149 907 THR A CG2 6785 N N . PHE A 908 ? 1.7067 1.1096 1.0057 0.3818 -0.1236 0.1221 908 PHE A N 6786 C CA . PHE A 908 ? 1.7580 1.1489 1.0712 0.3722 -0.1153 0.1718 908 PHE A CA 6787 C C . PHE A 908 ? 1.8573 1.2188 1.1147 0.3931 -0.1570 0.1855 908 PHE A C 6788 O O . PHE A 908 ? 2.2017 1.5582 1.4162 0.4120 -0.1917 0.1554 908 PHE A O 6789 C CB . PHE A 908 ? 1.5948 0.9825 1.0084 0.3500 -0.1188 0.1680 908 PHE A CB 6790 C CG . PHE A 908 ? 1.6795 1.0944 1.1508 0.3306 -0.0873 0.1480 908 PHE A CG 6791 C CD1 . PHE A 908 ? 1.6415 1.0661 1.1273 0.3106 -0.0505 0.1805 908 PHE A CD1 6792 C CD2 . PHE A 908 ? 1.7146 1.1495 1.2310 0.3296 -0.0975 0.1026 908 PHE A CD2 6793 C CE1 . PHE A 908 ? 1.4479 0.8984 0.9869 0.2945 -0.0258 0.1627 908 PHE A CE1 6794 C CE2 . PHE A 908 ? 1.4711 0.9274 1.0352 0.3134 -0.0703 0.0865 908 PHE A CE2 6795 C CZ . PHE A 908 ? 1.4228 0.8851 0.9957 0.2980 -0.0351 0.1138 908 PHE A CZ 6796 N N . MET A 909 ? 1.8176 1.1530 1.0727 0.3886 -0.1601 0.2326 909 MET A N 6797 C CA . MET A 909 ? 2.0914 1.3945 1.3190 0.4082 -0.2074 0.2434 909 MET A CA 6798 C C . MET A 909 ? 2.3606 1.6550 1.4750 0.4363 -0.2252 0.2506 909 MET A C 6799 O O . MET A 909 ? 2.5291 1.7966 1.6116 0.4541 -0.2668 0.2643 909 MET A O 6800 C CB . MET A 909 ? 1.8484 1.1648 1.1529 0.4144 -0.2454 0.1996 909 MET A CB 6801 C CG . MET A 909 ? 2.0023 1.2944 1.3176 0.4360 -0.2909 0.2131 909 MET A CG 6802 S SD . MET A 909 ? 2.3692 1.7122 1.7916 0.4472 -0.3215 0.1698 909 MET A SD 6803 C CE . MET A 909 ? 2.7274 2.0491 2.1395 0.4855 -0.3760 0.1926 909 MET A CE 6804 N N . ASN A 910 ? 2.2360 1.5487 1.2809 0.4469 -0.1963 0.2412 910 ASN A N 6805 C CA . ASN A 910 ? 2.4344 1.7289 1.3590 0.4826 -0.2231 0.2311 910 ASN A CA 6806 C C . ASN A 910 ? 2.7014 1.9912 1.5147 0.5043 -0.1939 0.2896 910 ASN A C 6807 O O . ASN A 910 ? 2.9728 2.2338 1.7432 0.5148 -0.2231 0.3236 910 ASN A O 6808 C CB . ASN A 910 ? 2.3920 1.6921 1.2817 0.4956 -0.2236 0.1743 910 ASN A CB 6809 C CG . ASN A 910 ? 2.3883 1.7232 1.2953 0.4885 -0.1579 0.1785 910 ASN A CG 6810 O OD1 . ASN A 910 ? 2.4308 1.7929 1.3449 0.4800 -0.1085 0.2324 910 ASN A OD1 6811 N ND2 . ASN A 910 ? 2.2482 1.5833 1.1664 0.4904 -0.1612 0.1259 910 ASN A ND2 6812 N N . LYS A 911 ? 2.4665 1.7907 1.2338 0.5143 -0.1356 0.3065 911 LYS A N 6813 C CA . LYS A 911 ? 2.6152 1.9557 1.2819 0.5370 -0.0987 0.3728 911 LYS A CA 6814 C C . LYS A 911 ? 2.5334 1.9365 1.2522 0.5132 -0.0269 0.4305 911 LYS A C 6815 O O . LYS A 911 ? 2.4201 1.8292 1.1829 0.4809 -0.0145 0.5013 911 LYS A O 6816 C CB . LYS A 911 ? 2.6976 2.0277 1.2075 0.5971 -0.1024 0.3436 911 LYS A CB 6817 C CG . LYS A 911 ? 2.6903 2.0485 1.0807 0.6318 -0.0579 0.4152 911 LYS A CG 6818 C CD . LYS A 911 ? 2.8377 2.1741 1.0966 0.6836 -0.0816 0.3691 911 LYS A CD 6819 C CE . LYS A 911 ? 2.8551 2.1251 1.0914 0.6814 -0.1642 0.3455 911 LYS A CE 6820 N NZ . LYS A 911 ? 2.9557 2.1971 1.0629 0.7286 -0.1920 0.3059 911 LYS A NZ 6821 N N . GLU A 912 ? 2.6879 2.1352 1.4041 0.5285 0.0148 0.4027 912 GLU A N 6822 C CA . GLU A 912 ? 2.7191 2.2421 1.4957 0.5078 0.0820 0.4569 912 GLU A CA 6823 C C . GLU A 912 ? 2.4693 1.9848 1.3992 0.4437 0.0704 0.4632 912 GLU A C 6824 O O . GLU A 912 ? 2.4526 2.0105 1.4515 0.4067 0.1034 0.5286 912 GLU A O 6825 C CB . GLU A 912 ? 2.7811 2.3497 1.5174 0.5487 0.1240 0.4180 912 GLU A CB 6826 C CG . GLU A 912 ? 2.8400 2.3601 1.6005 0.5522 0.0839 0.3226 912 GLU A CG 6827 C CD . GLU A 912 ? 2.9372 2.4811 1.6323 0.6026 0.1171 0.2829 912 GLU A CD 6828 O OE1 . GLU A 912 ? 2.8770 2.3787 1.5902 0.6035 0.0849 0.2108 912 GLU A OE1 6829 O OE2 . GLU A 912 ? 3.0115 2.6178 1.6360 0.6442 0.1753 0.3273 912 GLU A OE2 6830 N N . ASN A 913 ? 2.3274 1.7900 1.3081 0.4321 0.0203 0.3972 913 ASN A N 6831 C CA . ASN A 913 ? 2.2376 1.6748 1.3379 0.3844 -0.0015 0.3985 913 ASN A CA 6832 C C . ASN A 913 ? 2.3519 1.7234 1.4461 0.3856 -0.0601 0.3939 913 ASN A C 6833 O O . ASN A 913 ? 2.4967 1.8456 1.5785 0.4061 -0.0996 0.3375 913 ASN A O 6834 C CB . ASN A 913 ? 2.1188 1.5637 1.2943 0.3745 -0.0039 0.3321 913 ASN A CB 6835 C CG . ASN A 913 ? 1.9703 1.4716 1.1287 0.3907 0.0446 0.3193 913 ASN A CG 6836 O OD1 . ASN A 913 ? 1.9791 1.4793 1.0515 0.4325 0.0447 0.2828 913 ASN A OD1 6837 N ND2 . ASN A 913 ? 1.7843 1.3290 1.0216 0.3607 0.0803 0.3477 913 ASN A ND2 6838 N N . GLN A 914 ? 2.3582 1.6999 1.4653 0.3634 -0.0694 0.4567 914 GLN A N 6839 C CA . GLN A 914 ? 2.2619 1.5362 1.3691 0.3692 -0.1261 0.4542 914 GLN A CA 6840 C C . GLN A 914 ? 2.3113 1.5397 1.5107 0.3348 -0.1448 0.4660 914 GLN A C 6841 O O . GLN A 914 ? 2.3417 1.5544 1.6010 0.3387 -0.1673 0.4117 914 GLN A O 6842 C CB . GLN A 914 ? 2.4287 1.6804 1.4424 0.3847 -0.1360 0.5157 914 GLN A CB 6843 C CG . GLN A 914 ? 2.5223 1.7934 1.4223 0.4313 -0.1381 0.4924 914 GLN A CG 6844 C CD . GLN A 914 ? 2.7157 1.9602 1.5165 0.4500 -0.1516 0.5545 914 GLN A CD 6845 O OE1 . GLN A 914 ? 2.7389 1.9485 1.5619 0.4245 -0.1602 0.6191 914 GLN A OE1 6846 N NE2 . GLN A 914 ? 2.8084 2.0597 1.4921 0.4953 -0.1589 0.5358 914 GLN A NE2 6847 N N . ASN A 915 ? 2.3841 1.5897 1.5921 0.3018 -0.1377 0.5395 915 ASN A N 6848 C CA . ASN A 915 ? 2.2816 1.4306 1.5685 0.2659 -0.1603 0.5498 915 ASN A CA 6849 C C . ASN A 915 ? 2.2668 1.4634 1.6079 0.2195 -0.1201 0.5913 915 ASN A C 6850 O O . ASN A 915 ? 2.4586 1.6743 1.7889 0.1909 -0.1023 0.6737 915 ASN A O 6851 C CB . ASN A 915 ? 2.4012 1.4552 1.6654 0.2587 -0.2088 0.6021 915 ASN A CB 6852 C CG . ASN A 915 ? 2.3139 1.3361 1.5152 0.3078 -0.2455 0.5789 915 ASN A CG 6853 O OD1 . ASN A 915 ? 2.1715 1.2463 1.3114 0.3363 -0.2294 0.5672 915 ASN A OD1 6854 N ND2 . ASN A 915 ? 2.2194 1.1668 1.4447 0.3180 -0.2956 0.5666 915 ASN A ND2 6855 N N . HIS A 916 ? 2.1380 1.3608 1.5423 0.2114 -0.1068 0.5403 916 HIS A N 6856 C CA . HIS A 916 ? 2.2331 1.4935 1.7050 0.1654 -0.0809 0.5755 916 HIS A CA 6857 C C . HIS A 916 ? 2.1718 1.4207 1.7082 0.1613 -0.0898 0.5088 916 HIS A C 6858 O O . HIS A 916 ? 1.9887 1.2365 1.5165 0.1971 -0.0959 0.4372 916 HIS A O 6859 C CB . HIS A 916 ? 2.2411 1.6152 1.6937 0.1695 -0.0166 0.6095 916 HIS A CB 6860 C CG . HIS A 916 ? 2.5402 1.9566 2.0304 0.1214 0.0046 0.7099 916 HIS A CG 6861 N ND1 . HIS A 916 ? 2.6045 2.1119 2.0507 0.1324 0.0562 0.7756 916 HIS A ND1 6862 C CD2 . HIS A 916 ? 2.5892 1.9720 2.1586 0.0614 -0.0221 0.7606 916 HIS A CD2 6863 C CE1 . HIS A 916 ? 2.5625 2.1064 2.0722 0.0777 0.0654 0.8699 916 HIS A CE1 6864 N NE2 . HIS A 916 ? 2.6346 2.0984 2.2218 0.0295 0.0134 0.8623 916 HIS A NE2 6865 N N . SER A 917 ? 2.1776 1.4232 1.7803 0.1156 -0.0922 0.5377 917 SER A N 6866 C CA . SER A 917 ? 2.0434 1.2686 1.6995 0.1107 -0.1053 0.4805 917 SER A CA 6867 C C . SER A 917 ? 1.8738 1.2014 1.5634 0.1108 -0.0535 0.4600 917 SER A C 6868 O O . SER A 917 ? 1.8863 1.2804 1.6117 0.0798 -0.0237 0.5146 917 SER A O 6869 C CB . SER A 917 ? 2.2656 1.4083 1.9671 0.0627 -0.1524 0.5160 917 SER A CB 6870 O OG . SER A 917 ? 2.4208 1.6064 2.1563 0.0104 -0.1392 0.6065 917 SER A OG 6871 N N . TYR A 918 ? 1.8361 1.1795 1.5180 0.1463 -0.0443 0.3857 918 TYR A N 6872 C CA . TYR A 918 ? 1.6773 1.1008 1.3827 0.1524 -0.0021 0.3587 918 TYR A CA 6873 C C . TYR A 918 ? 1.5542 0.9569 1.3096 0.1470 -0.0162 0.3080 918 TYR A C 6874 O O . TYR A 918 ? 1.6257 0.9766 1.3738 0.1673 -0.0447 0.2622 918 TYR A O 6875 C CB . TYR A 918 ? 1.4768 0.9384 1.1227 0.1967 0.0201 0.3204 918 TYR A CB 6876 C CG . TYR A 918 ? 1.5507 1.0507 1.1336 0.2109 0.0459 0.3674 918 TYR A CG 6877 C CD1 . TYR A 918 ? 1.6425 1.2236 1.2270 0.2100 0.0945 0.4063 918 TYR A CD1 6878 C CD2 . TYR A 918 ? 1.7194 1.1804 1.2376 0.2314 0.0231 0.3752 918 TYR A CD2 6879 C CE1 . TYR A 918 ? 1.8410 1.4648 1.3571 0.2325 0.1239 0.4521 918 TYR A CE1 6880 C CE2 . TYR A 918 ? 2.0055 1.5000 1.4529 0.2492 0.0470 0.4194 918 TYR A CE2 6881 C CZ . TYR A 918 ? 2.0149 1.5914 1.4577 0.2515 0.0996 0.4579 918 TYR A CZ 6882 O OH . TYR A 918 ? 2.1324 1.7496 1.4944 0.2786 0.1290 0.5044 918 TYR A OH 6883 N N . SER A 919 ? 1.3771 0.8282 1.1826 0.1234 0.0054 0.3201 919 SER A N 6884 C CA . SER A 919 ? 1.3132 0.7501 1.1595 0.1193 -0.0054 0.2756 919 SER A CA 6885 C C . SER A 919 ? 1.3288 0.8348 1.1787 0.1413 0.0332 0.2383 919 SER A C 6886 O O . SER A 919 ? 1.4692 1.0440 1.3397 0.1345 0.0668 0.2645 919 SER A O 6887 C CB . SER A 919 ? 1.3303 0.7541 1.2345 0.0722 -0.0251 0.3158 919 SER A CB 6888 O OG . SER A 919 ? 1.2725 0.6988 1.2101 0.0711 -0.0286 0.2758 919 SER A OG 6889 N N . LEU A 920 ? 1.2759 0.7652 1.1090 0.1689 0.0265 0.1812 920 LEU A N 6890 C CA . LEU A 920 ? 1.1572 0.6928 0.9898 0.1873 0.0524 0.1452 920 LEU A CA 6891 C C . LEU A 920 ? 1.2251 0.7708 1.1080 0.1722 0.0550 0.1313 920 LEU A C 6892 O O . LEU A 920 ? 1.2496 0.7533 1.1496 0.1676 0.0300 0.1116 920 LEU A O 6893 C CB . LEU A 920 ? 1.1307 0.6496 0.9360 0.2139 0.0384 0.1008 920 LEU A CB 6894 C CG . LEU A 920 ? 1.3033 0.8086 1.0565 0.2306 0.0272 0.1112 920 LEU A CG 6895 C CD1 . LEU A 920 ? 1.3343 0.8340 1.0782 0.2508 0.0063 0.0721 920 LEU A CD1 6896 C CD2 . LEU A 920 ? 1.3571 0.8973 1.0644 0.2405 0.0549 0.1349 920 LEU A CD2 6897 N N . LYS A 921 ? 1.2530 0.8549 1.1528 0.1714 0.0850 0.1413 921 LYS A N 6898 C CA . LYS A 921 ? 1.0537 0.6725 1.0042 0.1553 0.0864 0.1380 921 LYS A CA 6899 C C . LYS A 921 ? 1.1959 0.8453 1.1421 0.1782 0.1079 0.1031 921 LYS A C 6900 O O . LYS A 921 ? 1.4425 1.1275 1.3598 0.2016 0.1340 0.1046 921 LYS A O 6901 C CB . LYS A 921 ? 1.0930 0.7575 1.0881 0.1270 0.0963 0.1964 921 LYS A CB 6902 C CG . LYS A 921 ? 1.2789 0.9875 1.3294 0.1156 0.1043 0.2001 921 LYS A CG 6903 C CD . LYS A 921 ? 1.4917 1.2496 1.6044 0.0776 0.1029 0.2685 921 LYS A CD 6904 C CE . LYS A 921 ? 1.5645 1.4028 1.7349 0.0773 0.1240 0.2827 921 LYS A CE 6905 N NZ . LYS A 921 ? 1.5575 1.4712 1.7006 0.1245 0.1773 0.2806 921 LYS A NZ 6906 N N . SER A 922 ? 1.2408 0.8689 1.2069 0.1754 0.0943 0.0719 922 SER A N 6907 C CA . SER A 922 ? 1.0636 0.7114 1.0316 0.1908 0.1084 0.0448 922 SER A CA 6908 C C . SER A 922 ? 1.1090 0.7691 1.1235 0.1750 0.1046 0.0499 922 SER A C 6909 O O . SER A 922 ? 1.0799 0.7082 1.1114 0.1568 0.0799 0.0518 922 SER A O 6910 C CB . SER A 922 ? 0.8671 0.4847 0.8141 0.2026 0.0952 0.0071 922 SER A CB 6911 O OG . SER A 922 ? 0.8963 0.4896 0.8624 0.1940 0.0767 -0.0027 922 SER A OG 6912 N N . SER A 923 ? 1.0743 0.7743 1.1021 0.1868 0.1248 0.0503 923 SER A N 6913 C CA . SER A 923 ? 0.9103 0.6299 0.9847 0.1738 0.1195 0.0582 923 SER A CA 6914 C C . SER A 923 ? 0.8848 0.5938 0.9502 0.1912 0.1217 0.0254 923 SER A C 6915 O O . SER A 923 ? 1.1406 0.8425 1.1713 0.2150 0.1330 0.0055 923 SER A O 6916 C CB . SER A 923 ? 0.9986 0.7912 1.1140 0.1715 0.1405 0.1017 923 SER A CB 6917 O OG . SER A 923 ? 1.0555 0.8844 1.1383 0.2100 0.1743 0.0989 923 SER A OG 6918 N N . ALA A 924 ? 0.8655 0.5646 0.9565 0.1785 0.1049 0.0210 924 ALA A N 6919 C CA . ALA A 924 ? 0.7460 0.4362 0.8317 0.1917 0.1054 -0.0013 924 ALA A CA 6920 C C . ALA A 924 ? 0.9576 0.6728 1.0837 0.1842 0.0971 0.0124 924 ALA A C 6921 O O . ALA A 924 ? 0.8443 0.5463 0.9884 0.1624 0.0724 0.0213 924 ALA A O 6922 C CB . ALA A 924 ? 0.9354 0.5829 0.9966 0.1897 0.0915 -0.0244 924 ALA A CB 6923 N N . SER A 925 ? 1.1631 0.9073 1.2986 0.2053 0.1120 0.0126 925 SER A N 6924 C CA . SER A 925 ? 0.9127 0.6890 1.0911 0.2029 0.1032 0.0272 925 SER A CA 6925 C C . SER A 925 ? 0.9021 0.6454 1.0587 0.2178 0.0967 0.0041 925 SER A C 6926 O O . SER A 925 ? 1.1069 0.8160 1.2243 0.2332 0.1043 -0.0166 925 SER A O 6927 C CB . SER A 925 ? 0.9518 0.8056 1.1692 0.2215 0.1273 0.0564 925 SER A CB 6928 O OG . SER A 925 ? 1.4155 1.2647 1.5925 0.2645 0.1511 0.0373 925 SER A OG 6929 N N . PHE A 926 ? 0.8140 0.5640 0.9957 0.2101 0.0772 0.0112 926 PHE A N 6930 C CA . PHE A 926 ? 0.9856 0.7062 1.1463 0.2238 0.0702 -0.0032 926 PHE A CA 6931 C C . PHE A 926 ? 0.9262 0.6875 1.1278 0.2355 0.0626 0.0131 926 PHE A C 6932 O O . PHE A 926 ? 0.9085 0.7160 1.1602 0.2200 0.0497 0.0367 926 PHE A O 6933 C CB . PHE A 926 ? 1.1711 0.8456 1.3000 0.2086 0.0503 -0.0150 926 PHE A CB 6934 C CG . PHE A 926 ? 1.1297 0.8049 1.2735 0.1946 0.0196 -0.0066 926 PHE A CG 6935 C CD1 . PHE A 926 ? 1.2029 0.8744 1.3453 0.2023 0.0029 -0.0045 926 PHE A CD1 6936 C CD2 . PHE A 926 ? 0.9450 0.6139 1.0986 0.1733 -0.0001 -0.0005 926 PHE A CD2 6937 C CE1 . PHE A 926 ? 1.1933 0.8572 1.3419 0.1896 -0.0344 0.0010 926 PHE A CE1 6938 C CE2 . PHE A 926 ? 1.0429 0.6953 1.2031 0.1582 -0.0412 0.0049 926 PHE A CE2 6939 C CZ . PHE A 926 ? 1.1413 0.7922 1.2978 0.1667 -0.0592 0.0042 926 PHE A CZ 6940 N N . ASN A 927 ? 1.1052 0.8475 1.2884 0.2613 0.0657 0.0038 927 ASN A N 6941 C CA . ASN A 927 ? 0.8484 0.6256 1.0661 0.2807 0.0573 0.0178 927 ASN A CA 6942 C C . ASN A 927 ? 0.8516 0.5732 1.0336 0.2868 0.0397 0.0074 927 ASN A C 6943 O O . ASN A 927 ? 0.8202 0.4878 0.9583 0.2958 0.0453 -0.0073 927 ASN A O 6944 C CB . ASN A 927 ? 0.8519 0.6720 1.0834 0.3233 0.0837 0.0228 927 ASN A CB 6945 C CG . ASN A 927 ? 1.2734 1.1616 1.5617 0.3468 0.0790 0.0465 927 ASN A CG 6946 O OD1 . ASN A 927 ? 1.5665 1.4502 1.8729 0.3332 0.0504 0.0536 927 ASN A OD1 6947 N ND2 . ASN A 927 ? 1.4137 1.3711 1.7281 0.3874 0.1076 0.0607 927 ASN A ND2 6948 N N . VAL A 928 ? 0.8065 0.5392 1.0068 0.2792 0.0138 0.0189 928 VAL A N 6949 C CA . VAL A 928 ? 0.9030 0.5873 1.0656 0.2855 -0.0031 0.0157 928 VAL A CA 6950 C C . VAL A 928 ? 0.9731 0.6700 1.1542 0.3213 -0.0059 0.0238 928 VAL A C 6951 O O . VAL A 928 ? 1.1324 0.8875 1.3653 0.3310 -0.0181 0.0405 928 VAL A O 6952 C CB . VAL A 928 ? 0.8934 0.5701 1.0458 0.2655 -0.0346 0.0205 928 VAL A CB 6953 C CG1 . VAL A 928 ? 0.9189 0.5519 1.0254 0.2765 -0.0481 0.0231 928 VAL A CG1 6954 C CG2 . VAL A 928 ? 0.8957 0.5502 1.0186 0.2419 -0.0340 0.0086 928 VAL A CG2 6955 N N . ILE A 929 ? 0.9582 0.5990 1.0993 0.3416 0.0008 0.0138 929 ILE A N 6956 C CA . ILE A 929 ? 1.1408 0.7767 1.2868 0.3863 -0.0028 0.0159 929 ILE A CA 6957 C C . ILE A 929 ? 0.9863 0.5819 1.1133 0.3944 -0.0303 0.0271 929 ILE A C 6958 O O . ILE A 929 ? 1.3384 0.9360 1.4755 0.4357 -0.0384 0.0314 929 ILE A O 6959 C CB . ILE A 929 ? 1.2818 0.8585 1.3845 0.4115 0.0092 -0.0041 929 ILE A CB 6960 C CG1 . ILE A 929 ? 1.3801 0.8751 1.4352 0.3770 -0.0053 -0.0075 929 ILE A CG1 6961 C CG2 . ILE A 929 ? 0.9532 0.5693 1.0652 0.4114 0.0366 -0.0143 929 ILE A CG2 6962 C CD1 . ILE A 929 ? 1.4220 0.8717 1.4468 0.3723 -0.0057 -0.0252 929 ILE A CD1 6963 N N . GLU A 930 ? 0.9873 0.5498 1.0829 0.3616 -0.0436 0.0339 930 GLU A N 6964 C CA . GLU A 930 ? 1.3256 0.8435 1.3908 0.3688 -0.0677 0.0494 930 GLU A CA 6965 C C . GLU A 930 ? 1.1975 0.7121 1.2322 0.3415 -0.0804 0.0610 930 GLU A C 6966 O O . GLU A 930 ? 1.3454 0.8712 1.3676 0.3165 -0.0687 0.0538 930 GLU A O 6967 C CB . GLU A 930 ? 1.3861 0.8197 1.4081 0.3730 -0.0695 0.0503 930 GLU A CB 6968 C CG . GLU A 930 ? 1.5272 0.9392 1.5540 0.4106 -0.0791 0.0462 930 GLU A CG 6969 C CD . GLU A 930 ? 1.6942 1.0237 1.6812 0.3949 -0.0907 0.0499 930 GLU A CD 6970 O OE1 . GLU A 930 ? 1.7057 0.9908 1.6644 0.3627 -0.0986 0.0701 930 GLU A OE1 6971 O OE2 . GLU A 930 ? 1.8389 1.1465 1.8206 0.4168 -0.0941 0.0357 930 GLU A OE2 6972 N N . PHE A 931 ? 1.1477 0.6424 1.1612 0.3536 -0.1052 0.0785 931 PHE A N 6973 C CA . PHE A 931 ? 1.1629 0.6469 1.1276 0.3397 -0.1191 0.0906 931 PHE A CA 6974 C C . PHE A 931 ? 1.4457 0.8758 1.3639 0.3483 -0.1310 0.1180 931 PHE A C 6975 O O . PHE A 931 ? 1.5082 0.9116 1.4408 0.3706 -0.1441 0.1254 931 PHE A O 6976 C CB . PHE A 931 ? 1.1179 0.6431 1.1022 0.3439 -0.1503 0.0872 931 PHE A CB 6977 C CG . PHE A 931 ? 1.0817 0.6559 1.1146 0.3276 -0.1466 0.0699 931 PHE A CG 6978 C CD1 . PHE A 931 ? 1.0262 0.6572 1.1377 0.3369 -0.1443 0.0711 931 PHE A CD1 6979 C CD2 . PHE A 931 ? 1.3511 0.9158 1.3487 0.3068 -0.1458 0.0565 931 PHE A CD2 6980 C CE1 . PHE A 931 ? 1.0768 0.7567 1.2371 0.3167 -0.1414 0.0656 931 PHE A CE1 6981 C CE2 . PHE A 931 ? 1.0539 0.6514 1.0941 0.2887 -0.1487 0.0447 931 PHE A CE2 6982 C CZ . PHE A 931 ? 1.0904 0.7468 1.2151 0.2891 -0.1469 0.0525 931 PHE A CZ 6983 N N . PRO A 932 ? 1.3525 0.7669 1.2114 0.3348 -0.1261 0.1362 932 PRO A N 6984 C CA . PRO A 932 ? 1.3888 0.7608 1.1982 0.3383 -0.1359 0.1735 932 PRO A CA 6985 C C . PRO A 932 ? 1.4382 0.8045 1.2321 0.3644 -0.1736 0.1820 932 PRO A C 6986 O O . PRO A 932 ? 1.9476 1.2737 1.7048 0.3727 -0.1881 0.2144 932 PRO A O 6987 C CB . PRO A 932 ? 1.3585 0.7461 1.1115 0.3242 -0.1128 0.1893 932 PRO A CB 6988 C CG . PRO A 932 ? 1.3120 0.7374 1.0675 0.3268 -0.1106 0.1526 932 PRO A CG 6989 C CD . PRO A 932 ? 1.2015 0.6421 1.0328 0.3204 -0.1084 0.1246 932 PRO A CD 6990 N N . TYR A 933 ? 1.3167 0.7246 1.1429 0.3741 -0.1932 0.1570 933 TYR A N 6991 C CA . TYR A 933 ? 1.3618 0.7781 1.1764 0.3934 -0.2365 0.1623 933 TYR A CA 6992 C C . TYR A 933 ? 1.4370 0.8612 1.3095 0.4203 -0.2601 0.1696 933 TYR A C 6993 O O . TYR A 933 ? 1.5627 1.0150 1.4542 0.4352 -0.2991 0.1723 933 TYR A O 6994 C CB . TYR A 933 ? 1.3822 0.8370 1.2070 0.3838 -0.2566 0.1368 933 TYR A CB 6995 C CG . TYR A 933 ? 1.5538 0.9915 1.3048 0.3719 -0.2385 0.1263 933 TYR A CG 6996 C CD1 . TYR A 933 ? 1.6123 1.0177 1.2636 0.3862 -0.2455 0.1416 933 TYR A CD1 6997 C CD2 . TYR A 933 ? 1.4636 0.9202 1.2393 0.3534 -0.2124 0.1031 933 TYR A CD2 6998 C CE1 . TYR A 933 ? 1.6109 1.0087 1.1886 0.3885 -0.2242 0.1326 933 TYR A CE1 6999 C CE2 . TYR A 933 ? 1.4887 0.9314 1.1951 0.3524 -0.1955 0.0929 933 TYR A CE2 7000 C CZ . TYR A 933 ? 1.5106 0.9266 1.1181 0.3731 -0.1999 0.1069 933 TYR A CZ 7001 O OH . TYR A 933 ? 1.5676 0.9778 1.1007 0.3847 -0.1787 0.0972 933 TYR A OH 7002 N N . LYS A 934 ? 1.5615 0.9592 1.4594 0.4301 -0.2404 0.1719 934 LYS A N 7003 C CA . LYS A 934 ? 1.7206 1.1289 1.6735 0.4684 -0.2545 0.1711 934 LYS A CA 7004 C C . LYS A 934 ? 1.8355 1.2432 1.7826 0.4974 -0.2983 0.1925 934 LYS A C 7005 O O . LYS A 934 ? 1.9755 1.3376 1.8539 0.4912 -0.3164 0.2150 934 LYS A O 7006 C CB . LYS A 934 ? 1.8223 1.1667 1.7632 0.4749 -0.2358 0.1716 934 LYS A CB 7007 C CG . LYS A 934 ? 1.7792 1.1347 1.7465 0.4631 -0.2009 0.1450 934 LYS A CG 7008 C CD . LYS A 934 ? 1.8204 1.1062 1.7408 0.4285 -0.1864 0.1533 934 LYS A CD 7009 C CE . LYS A 934 ? 2.0376 1.3088 1.9783 0.4262 -0.1667 0.1293 934 LYS A CE 7010 N NZ . LYS A 934 ? 2.0693 1.4133 2.0591 0.4436 -0.1455 0.0999 934 LYS A NZ 7011 N N . ASN A 935 ? 1.9394 1.4104 1.9621 0.5296 -0.3116 0.1887 935 ASN A N 7012 C CA . ASN A 935 ? 2.1027 1.6152 2.1520 0.5518 -0.3549 0.2063 935 ASN A CA 7013 C C . ASN A 935 ? 1.8955 1.4484 1.9444 0.5235 -0.3880 0.2050 935 ASN A C 7014 O O . ASN A 935 ? 1.9057 1.4489 1.9225 0.5288 -0.4335 0.2202 935 ASN A O 7015 C CB . ASN A 935 ? 2.1432 1.5884 2.1295 0.5611 -0.3697 0.2295 935 ASN A CB 7016 C CG . ASN A 935 ? 2.0631 1.4836 2.0679 0.5869 -0.3490 0.2290 935 ASN A CG 7017 O OD1 . ASN A 935 ? 2.1355 1.4889 2.1040 0.5717 -0.3236 0.2235 935 ASN A OD1 7018 N ND2 . ASN A 935 ? 1.9273 1.4017 1.9891 0.6265 -0.3642 0.2355 935 ASN A ND2 7019 N N . LEU A 936 ? 1.7126 1.3052 1.7909 0.4904 -0.3657 0.1850 936 LEU A N 7020 C CA . LEU A 936 ? 1.7602 1.3952 1.8557 0.4591 -0.3993 0.1787 936 LEU A CA 7021 C C . LEU A 936 ? 1.6438 1.3571 1.8332 0.4402 -0.3756 0.1689 936 LEU A C 7022 O O . LEU A 936 ? 1.3828 1.0885 1.5756 0.4408 -0.3247 0.1566 936 LEU A O 7023 C CB . LEU A 936 ? 1.7557 1.3198 1.7400 0.4337 -0.4005 0.1658 936 LEU A CB 7024 C CG . LEU A 936 ? 1.7747 1.3365 1.7267 0.4142 -0.4553 0.1563 936 LEU A CG 7025 C CD1 . LEU A 936 ? 1.9321 1.4896 1.8676 0.4355 -0.5168 0.1755 936 LEU A CD1 7026 C CD2 . LEU A 936 ? 1.6530 1.1475 1.4883 0.4032 -0.4390 0.1378 936 LEU A CD2 7027 N N . PRO A 937 ? 1.5980 1.3856 1.8639 0.4207 -0.4162 0.1785 937 PRO A N 7028 C CA . PRO A 937 ? 1.5189 1.3923 1.8836 0.3980 -0.3976 0.1817 937 PRO A CA 7029 C C . PRO A 937 ? 1.6124 1.4423 1.9316 0.3704 -0.3541 0.1558 937 PRO A C 7030 O O . PRO A 937 ? 1.7982 1.5455 2.0201 0.3541 -0.3591 0.1356 937 PRO A O 7031 C CB . PRO A 937 ? 1.5995 1.5180 2.0174 0.3632 -0.4677 0.1972 937 PRO A CB 7032 C CG . PRO A 937 ? 1.5538 1.4638 1.9560 0.3914 -0.5158 0.2125 937 PRO A CG 7033 C CD . PRO A 937 ? 1.5322 1.3363 1.8092 0.4211 -0.4872 0.1956 937 PRO A CD 7034 N N . ILE A 938 ? 1.6341 1.5255 2.0214 0.3715 -0.3105 0.1587 938 ILE A N 7035 C CA . ILE A 938 ? 1.4136 1.2659 1.7601 0.3555 -0.2634 0.1356 938 ILE A CA 7036 C C . ILE A 938 ? 1.3431 1.2463 1.7476 0.3150 -0.2640 0.1398 938 ILE A C 7037 O O . ILE A 938 ? 1.2895 1.1347 1.6384 0.2839 -0.2707 0.1202 938 ILE A O 7038 C CB . ILE A 938 ? 1.4407 1.2930 1.7874 0.3950 -0.2092 0.1300 938 ILE A CB 7039 C CG1 . ILE A 938 ? 1.5244 1.4718 1.9610 0.4378 -0.2054 0.1541 938 ILE A CG1 7040 C CG2 . ILE A 938 ? 1.4830 1.2352 1.7363 0.4139 -0.2040 0.1182 938 ILE A CG2 7041 C CD1 . ILE A 938 ? 1.4449 1.3800 1.8661 0.4884 -0.1584 0.1424 938 ILE A CD1 7042 N N . GLU A 939 ? 1.5078 1.5216 2.0230 0.3194 -0.2555 0.1691 939 GLU A N 7043 C CA . GLU A 939 ? 1.7922 1.8677 2.3727 0.2863 -0.2403 0.1835 939 GLU A CA 7044 C C . GLU A 939 ? 1.8837 1.9154 2.4073 0.2971 -0.1801 0.1570 939 GLU A C 7045 O O . GLU A 939 ? 1.9794 1.9968 2.4734 0.3419 -0.1419 0.1452 939 GLU A O 7046 C CB . GLU A 939 ? 1.8427 1.8855 2.4214 0.2278 -0.2991 0.1848 939 GLU A CB 7047 C CG . GLU A 939 ? 1.6829 1.8087 2.3628 0.1849 -0.3059 0.2198 939 GLU A CG 7048 C CD . GLU A 939 ? 1.7066 1.9746 2.5269 0.1833 -0.3254 0.2759 939 GLU A CD 7049 O OE1 . GLU A 939 ? 1.6958 1.9852 2.5311 0.2101 -0.3512 0.2832 939 GLU A OE1 7050 O OE2 . GLU A 939 ? 1.6560 2.0219 2.5758 0.1556 -0.3147 0.3182 939 GLU A OE2 7051 N N . ASP A 940 ? 1.6816 1.6819 2.1845 0.2578 -0.1787 0.1467 940 ASP A N 7052 C CA . ASP A 940 ? 1.6200 1.5889 2.0790 0.2642 -0.1272 0.1256 940 ASP A CA 7053 C C . ASP A 940 ? 1.5392 1.4687 1.9760 0.2196 -0.1394 0.1165 940 ASP A C 7054 O O . ASP A 940 ? 1.6094 1.5491 2.0821 0.1824 -0.1859 0.1325 940 ASP A O 7055 C CB . ASP A 940 ? 1.5861 1.6473 2.1086 0.2940 -0.0808 0.1463 940 ASP A CB 7056 C CG . ASP A 940 ? 1.5520 1.7174 2.1762 0.2620 -0.0883 0.1896 940 ASP A CG 7057 O OD1 . ASP A 940 ? 1.6192 1.8735 2.3315 0.2612 -0.1132 0.2271 940 ASP A OD1 7058 O OD2 . ASP A 940 ? 1.4620 1.6236 2.0830 0.2354 -0.0719 0.1912 940 ASP A OD2 7059 N N . ILE A 941 ? 1.1611 1.0404 1.5383 0.2239 -0.1031 0.0914 941 ILE A N 7060 C CA . ILE A 941 ? 0.9753 0.8083 1.3201 0.1916 -0.1114 0.0789 941 ILE A CA 7061 C C . ILE A 941 ? 0.9806 0.8298 1.3264 0.1961 -0.0641 0.0763 941 ILE A C 7062 O O . ILE A 941 ? 1.0562 0.8815 1.3601 0.2230 -0.0295 0.0576 941 ILE A O 7063 C CB . ILE A 941 ? 1.0437 0.7818 1.2904 0.1948 -0.1249 0.0465 941 ILE A CB 7064 C CG1 . ILE A 941 ? 1.0570 0.7719 1.2834 0.1979 -0.1717 0.0474 941 ILE A CG1 7065 C CG2 . ILE A 941 ? 1.2510 0.9408 1.4613 0.1720 -0.1365 0.0320 941 ILE A CG2 7066 C CD1 . ILE A 941 ? 1.2724 0.9176 1.4016 0.2186 -0.1677 0.0250 941 ILE A CD1 7067 N N . THR A 942 ? 1.0548 0.9389 1.4464 0.1672 -0.0686 0.0976 942 THR A N 7068 C CA . THR A 942 ? 0.9847 0.8881 1.3754 0.1711 -0.0269 0.1000 942 THR A CA 7069 C C . THR A 942 ? 1.1003 0.9872 1.5032 0.1292 -0.0495 0.1131 942 THR A C 7070 O O . THR A 942 ? 1.4577 1.3598 1.9108 0.0945 -0.0940 0.1393 942 THR A O 7071 C CB . THR A 942 ? 1.0435 1.0495 1.4971 0.1985 0.0107 0.1306 942 THR A CB 7072 O OG1 . THR A 942 ? 1.3494 1.3574 1.7878 0.2422 0.0224 0.1171 942 THR A OG1 7073 C CG2 . THR A 942 ? 1.0192 1.0342 1.4481 0.2127 0.0547 0.1275 942 THR A CG2 7074 N N . ASN A 943 ? 0.9691 0.8202 1.3271 0.1312 -0.0251 0.0969 943 ASN A N 7075 C CA . ASN A 943 ? 0.9801 0.8041 1.3398 0.0973 -0.0446 0.1083 943 ASN A CA 7076 C C . ASN A 943 ? 0.8793 0.6758 1.1876 0.1129 -0.0085 0.0887 943 ASN A C 7077 O O . ASN A 943 ? 0.8636 0.6482 1.1303 0.1442 0.0216 0.0623 943 ASN A O 7078 C CB . ASN A 943 ? 1.1565 0.8924 1.4758 0.0765 -0.1020 0.0886 943 ASN A CB 7079 C CG . ASN A 943 ? 1.3413 1.0671 1.7050 0.0296 -0.1510 0.1211 943 ASN A CG 7080 O OD1 . ASN A 943 ? 1.1413 0.8857 1.5290 0.0118 -0.1380 0.1460 943 ASN A OD1 7081 N ND2 . ASN A 943 ? 1.7995 1.4895 2.1714 0.0073 -0.2133 0.1235 943 ASN A ND2 7082 N N . SER A 944 ? 0.9292 0.7121 1.2421 0.0887 -0.0171 0.1048 944 SER A N 7083 C CA . SER A 944 ? 0.8972 0.6585 1.1649 0.1028 0.0126 0.0903 944 SER A CA 7084 C C . SER A 944 ? 0.9372 0.6375 1.1840 0.0780 -0.0175 0.0930 944 SER A C 7085 O O . SER A 944 ? 1.0664 0.7603 1.3517 0.0423 -0.0555 0.1231 944 SER A O 7086 C CB . SER A 944 ? 0.8432 0.6844 1.1397 0.1177 0.0569 0.1178 944 SER A CB 7087 O OG . SER A 944 ? 0.9994 0.9044 1.3663 0.0877 0.0495 0.1724 944 SER A OG 7088 N N . THR A 945 ? 0.8559 0.5094 1.0441 0.0967 -0.0052 0.0638 945 THR A N 7089 C CA . THR A 945 ? 0.9036 0.4972 1.0644 0.0843 -0.0295 0.0643 945 THR A CA 7090 C C . THR A 945 ? 0.9453 0.5537 1.0840 0.0997 0.0048 0.0640 945 THR A C 7091 O O . THR A 945 ? 0.9924 0.6301 1.1160 0.1246 0.0386 0.0472 945 THR A O 7092 C CB . THR A 945 ? 1.0463 0.5564 1.1463 0.1007 -0.0599 0.0250 945 THR A CB 7093 O OG1 . THR A 945 ? 1.3633 0.8073 1.4333 0.0953 -0.0882 0.0252 945 THR A OG1 7094 C CG2 . THR A 945 ? 0.8553 0.3747 0.9171 0.1367 -0.0257 -0.0072 945 THR A CG2 7095 N N . LEU A 946 ? 0.9889 0.5688 1.1222 0.0838 -0.0105 0.0836 946 LEU A N 7096 C CA . LEU A 946 ? 1.1323 0.7223 1.2396 0.0984 0.0159 0.0857 946 LEU A CA 7097 C C . LEU A 946 ? 1.2779 0.7933 1.3357 0.1108 -0.0070 0.0616 946 LEU A C 7098 O O . LEU A 946 ? 1.0542 0.5032 1.0992 0.1015 -0.0481 0.0581 946 LEU A O 7099 C CB . LEU A 946 ? 1.0908 0.7290 1.2335 0.0756 0.0268 0.1395 946 LEU A CB 7100 C CG . LEU A 946 ? 1.0624 0.6755 1.2451 0.0305 -0.0158 0.1827 946 LEU A CG 7101 C CD1 . LEU A 946 ? 1.2607 0.7919 1.4033 0.0238 -0.0460 0.1848 946 LEU A CD1 7102 C CD2 . LEU A 946 ? 1.0296 0.7405 1.2805 0.0061 0.0065 0.2473 946 LEU A CD2 7103 N N . VAL A 947 ? 1.2357 0.7596 1.2632 0.1356 0.0153 0.0444 947 VAL A N 7104 C CA . VAL A 947 ? 1.1830 0.6551 1.1711 0.1550 -0.0014 0.0247 947 VAL A CA 7105 C C . VAL A 947 ? 1.2806 0.7538 1.2550 0.1543 0.0033 0.0457 947 VAL A C 7106 O O . VAL A 947 ? 1.2370 0.7575 1.2102 0.1590 0.0311 0.0528 947 VAL A O 7107 C CB . VAL A 947 ? 1.0802 0.5680 1.0520 0.1845 0.0139 -0.0098 947 VAL A CB 7108 C CG1 . VAL A 947 ? 0.9569 0.4167 0.8991 0.2102 0.0028 -0.0225 947 VAL A CG1 7109 C CG2 . VAL A 947 ? 1.1041 0.5835 1.0772 0.1896 0.0073 -0.0272 947 VAL A CG2 7110 N N . THR A 948 ? 1.2553 0.6666 1.2095 0.1526 -0.0281 0.0541 948 THR A N 7111 C CA . THR A 948 ? 1.1705 0.5745 1.1092 0.1490 -0.0293 0.0814 948 THR A CA 7112 C C . THR A 948 ? 1.2988 0.6640 1.1989 0.1824 -0.0435 0.0589 948 THR A C 7113 O O . THR A 948 ? 1.4713 0.7863 1.3526 0.2045 -0.0671 0.0337 948 THR A O 7114 C CB . THR A 948 ? 1.2675 0.6320 1.2224 0.1116 -0.0589 0.1272 948 THR A CB 7115 O OG1 . THR A 948 ? 1.6163 0.9630 1.5478 0.1111 -0.0637 0.1558 948 THR A OG1 7116 C CG2 . THR A 948 ? 1.2879 0.5602 1.2292 0.1092 -0.1097 0.1101 948 THR A CG2 7117 N N . THR A 949 ? 1.2076 0.6004 1.0923 0.1916 -0.0291 0.0680 949 THR A N 7118 C CA . THR A 949 ? 1.1586 0.5240 1.0142 0.2208 -0.0458 0.0573 949 THR A CA 7119 C C . THR A 949 ? 1.2889 0.6283 1.1214 0.2095 -0.0572 0.0962 949 THR A C 7120 O O . THR A 949 ? 1.4664 0.8500 1.2907 0.2019 -0.0348 0.1162 949 THR A O 7121 C CB . THR A 949 ? 1.2476 0.6696 1.1051 0.2431 -0.0276 0.0328 949 THR A CB 7122 O OG1 . THR A 949 ? 1.3455 0.7934 1.2268 0.2517 -0.0176 0.0053 949 THR A OG1 7123 C CG2 . THR A 949 ? 1.2174 0.6249 1.0560 0.2725 -0.0476 0.0289 949 THR A CG2 7124 N N . ASN A 950 ? 1.3894 0.6511 1.2030 0.2125 -0.0942 0.1075 950 ASN A N 7125 C CA . ASN A 950 ? 1.3064 0.5340 1.0981 0.1976 -0.1100 0.1525 950 ASN A CA 7126 C C . ASN A 950 ? 1.4604 0.6710 1.2158 0.2350 -0.1237 0.1435 950 ASN A C 7127 O O . ASN A 950 ? 1.9183 1.0844 1.6604 0.2704 -0.1487 0.1156 950 ASN A O 7128 C CB . ASN A 950 ? 1.3668 0.5036 1.1595 0.1702 -0.1535 0.1799 950 ASN A CB 7129 C CG . ASN A 950 ? 1.6540 0.8130 1.4925 0.1270 -0.1482 0.1975 950 ASN A CG 7130 O OD1 . ASN A 950 ? 1.8702 1.1172 1.7380 0.1203 -0.1063 0.1944 950 ASN A OD1 7131 N ND2 . ASN A 950 ? 2.0323 1.1055 1.8761 0.0986 -0.1972 0.2169 950 ASN A ND2 7132 N N . VAL A 951 ? 1.3802 0.6298 1.1156 0.2328 -0.1076 0.1673 951 VAL A N 7133 C CA . VAL A 951 ? 1.3952 0.6264 1.0947 0.2635 -0.1272 0.1679 951 VAL A CA 7134 C C . VAL A 951 ? 1.5478 0.7190 1.2163 0.2457 -0.1497 0.2222 951 VAL A C 7135 O O . VAL A 951 ? 1.6395 0.8288 1.3119 0.2090 -0.1325 0.2677 951 VAL A O 7136 C CB . VAL A 951 ? 1.4563 0.7588 1.1411 0.2776 -0.1057 0.1547 951 VAL A CB 7137 C CG1 . VAL A 951 ? 1.5422 0.8974 1.2635 0.2882 -0.0909 0.1087 951 VAL A CG1 7138 C CG2 . VAL A 951 ? 1.6545 0.9927 1.3152 0.2553 -0.0763 0.1886 951 VAL A CG2 7139 N N . THR A 952 ? 1.7744 0.8782 1.4149 0.2733 -0.1883 0.2225 952 THR A N 7140 C CA . THR A 952 ? 1.7416 0.7651 1.3526 0.2548 -0.2205 0.2759 952 THR A CA 7141 C C . THR A 952 ? 1.8710 0.8581 1.4373 0.2932 -0.2493 0.2814 952 THR A C 7142 O O . THR A 952 ? 1.7832 0.7989 1.3501 0.3385 -0.2527 0.2395 952 THR A O 7143 C CB . THR A 952 ? 1.9369 0.8797 1.5675 0.2361 -0.2553 0.2733 952 THR A CB 7144 O OG1 . THR A 952 ? 2.0902 1.0475 1.7376 0.2727 -0.2559 0.2068 952 THR A OG1 7145 C CG2 . THR A 952 ? 1.9371 0.8825 1.6010 0.1809 -0.2459 0.3084 952 THR A CG2 7146 N N . TRP A 953 ? 1.9792 0.9167 1.5166 0.2712 -0.2691 0.3381 953 TRP A N 7147 C CA . TRP A 953 ? 1.9015 0.8180 1.4064 0.2993 -0.2945 0.3458 953 TRP A CA 7148 C C . TRP A 953 ? 2.1487 0.9915 1.6642 0.2893 -0.3312 0.3516 953 TRP A C 7149 O O . TRP A 953 ? 2.2998 1.1246 1.8192 0.3283 -0.3512 0.3053 953 TRP A O 7150 C CB . TRP A 953 ? 2.1331 1.0632 1.5820 0.2887 -0.2835 0.4066 953 TRP A CB 7151 C CG . TRP A 953 ? 2.0834 1.1154 1.5210 0.3065 -0.2451 0.3785 953 TRP A CG 7152 C CD1 . TRP A 953 ? 2.0618 1.1743 1.5172 0.2847 -0.1972 0.3724 953 TRP A CD1 7153 C CD2 . TRP A 953 ? 2.1979 1.2596 1.6052 0.3494 -0.2576 0.3506 953 TRP A CD2 7154 N NE1 . TRP A 953 ? 2.1323 1.3080 1.5610 0.3122 -0.1827 0.3391 953 TRP A NE1 7155 C CE2 . TRP A 953 ? 2.2034 1.3514 1.6062 0.3478 -0.2213 0.3266 953 TRP A CE2 7156 C CE3 . TRP A 953 ? 2.2279 1.2501 1.6129 0.3902 -0.3009 0.3445 953 TRP A CE3 7157 C CZ2 . TRP A 953 ? 2.1525 1.3399 1.5285 0.3786 -0.2337 0.2971 953 TRP A CZ2 7158 C CZ3 . TRP A 953 ? 2.1394 1.2182 1.5081 0.4208 -0.3083 0.3189 953 TRP A CZ3 7159 C CH2 . TRP A 953 ? 2.0920 1.2485 1.4560 0.4114 -0.2781 0.2956 953 TRP A CH2 7160 N N . GLY A 954 ? 2.3125 1.1158 1.8294 0.2386 -0.3395 0.4110 954 GLY A N 7161 C CA . GLY A 954 ? 2.3806 1.1007 1.8983 0.2242 -0.3804 0.4200 954 GLY A CA 7162 C C . GLY A 954 ? 2.2280 0.9219 1.7315 0.1807 -0.3886 0.5021 954 GLY A C 7163 O O . GLY A 954 ? 2.3209 0.9668 1.7931 0.1960 -0.4159 0.5183 954 GLY A O 7164 N N . GLY B 1 ? 1.8693 1.9773 2.9231 -0.5266 -0.0764 -0.0191 1 GLY B N 7165 C CA . GLY B 1 ? 1.9100 2.0686 3.0438 -0.5209 -0.0876 -0.0131 1 GLY B CA 7166 C C . GLY B 1 ? 1.9144 2.0811 3.0342 -0.5014 -0.1158 -0.0069 1 GLY B C 7167 O O . GLY B 1 ? 1.9071 2.0482 2.9620 -0.5005 -0.1392 -0.0091 1 GLY B O 7168 N N . PRO B 2 ? 1.9706 2.1734 3.1536 -0.4864 -0.1134 0.0006 2 PRO B N 7169 C CA . PRO B 2 ? 2.0606 2.2725 3.2396 -0.4671 -0.1398 0.0096 2 PRO B CA 7170 C C . PRO B 2 ? 2.1818 2.3529 3.2756 -0.4499 -0.1278 0.0104 2 PRO B C 7171 O O . PRO B 2 ? 2.2357 2.3942 3.2828 -0.4450 -0.1572 0.0143 2 PRO B O 7172 C CB . PRO B 2 ? 1.9697 2.2244 3.2418 -0.4544 -0.1268 0.0148 2 PRO B CB 7173 C CG . PRO B 2 ? 1.9223 2.1788 3.2194 -0.4622 -0.0802 0.0069 2 PRO B CG 7174 C CD . PRO B 2 ? 1.9488 2.1858 3.2141 -0.4875 -0.0836 0.0005 2 PRO B CD 7175 N N . ASN B 3 ? 2.1631 2.3150 3.2376 -0.4424 -0.0852 0.0070 3 ASN B N 7176 C CA . ASN B 3 ? 2.0794 2.1891 3.0709 -0.4294 -0.0699 0.0063 3 ASN B CA 7177 C C . ASN B 3 ? 1.9533 2.0598 2.9184 -0.4097 -0.0919 0.0140 3 ASN B C 7178 O O . ASN B 3 ? 1.9050 2.0408 2.9251 -0.3967 -0.0996 0.0215 3 ASN B O 7179 C CB . ASN B 3 ? 2.1492 2.2202 3.0706 -0.4445 -0.0741 -0.0013 3 ASN B CB 7180 C CG . ASN B 3 ? 2.2734 2.3020 3.1261 -0.4360 -0.0444 -0.0036 3 ASN B CG 7181 O OD1 . ASN B 3 ? 2.3186 2.3237 3.1137 -0.4233 -0.0520 -0.0026 3 ASN B OD1 7182 N ND2 . ASN B 3 ? 2.2858 2.3049 3.1446 -0.4444 -0.0110 -0.0057 3 ASN B ND2 7183 N N . ILE B 4 ? 1.8846 1.9551 2.7680 -0.4083 -0.1016 0.0121 4 ILE B N 7184 C CA . ILE B 4 ? 1.9151 1.9769 2.7606 -0.3924 -0.1207 0.0195 4 ILE B CA 7185 C C . ILE B 4 ? 2.0261 2.0761 2.8211 -0.4048 -0.1566 0.0174 4 ILE B C 7186 O O . ILE B 4 ? 2.0643 2.1332 2.8709 -0.4046 -0.1911 0.0261 4 ILE B O 7187 C CB . ILE B 4 ? 1.7732 1.8010 2.5613 -0.3760 -0.0916 0.0184 4 ILE B CB 7188 C CG1 . ILE B 4 ? 1.7255 1.7669 2.5605 -0.3630 -0.0577 0.0198 4 ILE B CG1 7189 C CG2 . ILE B 4 ? 1.5745 1.5904 2.3165 -0.3632 -0.1136 0.0254 4 ILE B CG2 7190 C CD1 . ILE B 4 ? 1.7110 1.7443 2.5513 -0.3739 -0.0212 0.0120 4 ILE B CD1 7191 N N . CYS B 5 ? 2.0441 2.0617 2.7815 -0.4158 -0.1480 0.0057 5 CYS B N 7192 C CA . CYS B 5 ? 2.0834 2.0884 2.7713 -0.4299 -0.1770 -0.0015 5 CYS B CA 7193 C C . CYS B 5 ? 2.1365 2.1751 2.8698 -0.4469 -0.2127 0.0004 5 CYS B C 7194 O O . CYS B 5 ? 2.1824 2.2260 2.8888 -0.4528 -0.2461 0.0027 5 CYS B O 7195 C CB . CYS B 5 ? 2.0327 2.0022 2.6753 -0.4413 -0.1595 -0.0170 5 CYS B CB 7196 S SG . CYS B 5 ? 2.5213 2.4482 3.1032 -0.4238 -0.1239 -0.0188 5 CYS B SG 7197 N N . THR B 6 ? 2.1748 2.2371 2.9760 -0.4560 -0.2057 -0.0002 6 THR B N 7198 C CA . THR B 6 ? 2.2015 2.2987 3.0559 -0.4725 -0.2390 0.0020 6 THR B CA 7199 C C . THR B 6 ? 2.1353 2.2626 3.0210 -0.4627 -0.2704 0.0187 6 THR B C 7200 O O . THR B 6 ? 2.1333 2.2655 2.9924 -0.4726 -0.3080 0.0218 6 THR B O 7201 C CB . THR B 6 ? 2.1708 2.2922 3.1033 -0.4812 -0.2214 0.0003 6 THR B CB 7202 O OG1 . THR B 6 ? 2.1668 2.2578 3.0710 -0.4896 -0.1903 -0.0117 6 THR B OG1 7203 C CG2 . THR B 6 ? 2.1513 2.3054 3.1337 -0.5015 -0.2573 0.0003 6 THR B CG2 7204 N N . THR B 7 ? 2.1156 2.2630 3.0586 -0.4443 -0.2553 0.0294 7 THR B N 7205 C CA . THR B 7 ? 2.1584 2.3320 3.1387 -0.4321 -0.2834 0.0467 7 THR B CA 7206 C C . THR B 7 ? 2.0058 2.1614 2.9600 -0.4070 -0.2627 0.0532 7 THR B C 7207 O O . THR B 7 ? 1.9490 2.0926 2.9072 -0.3961 -0.2218 0.0468 7 THR B O 7208 C CB . THR B 7 ? 2.2170 2.4368 3.3068 -0.4320 -0.2898 0.0536 7 THR B CB 7209 O OG1 . THR B 7 ? 2.2801 2.5022 3.4095 -0.4244 -0.2436 0.0456 7 THR B OG1 7210 C CG2 . THR B 7 ? 2.1362 2.3771 3.2536 -0.4577 -0.3195 0.0498 7 THR B CG2 7211 N N . ARG B 8 ? 1.9121 2.0678 2.8434 -0.3996 -0.2927 0.0670 8 ARG B N 7212 C CA . ARG B 8 ? 1.9157 2.0464 2.7962 -0.3806 -0.2829 0.0732 8 ARG B CA 7213 C C . ARG B 8 ? 2.0549 2.1482 2.8334 -0.3896 -0.2826 0.0637 8 ARG B C 7214 O O . ARG B 8 ? 1.9355 2.0066 2.6607 -0.3781 -0.2792 0.0680 8 ARG B O 7215 C CB . ARG B 8 ? 1.8674 1.9899 2.7700 -0.3602 -0.2377 0.0689 8 ARG B CB 7216 C CG . ARG B 8 ? 1.8583 2.0169 2.8627 -0.3484 -0.2318 0.0752 8 ARG B CG 7217 C CD . ARG B 8 ? 1.7910 1.9382 2.8045 -0.3312 -0.1838 0.0671 8 ARG B CD 7218 N NE . ARG B 8 ? 1.7903 1.9734 2.9040 -0.3238 -0.1694 0.0663 8 ARG B NE 7219 C CZ . ARG B 8 ? 1.7749 1.9744 2.9322 -0.3343 -0.1445 0.0551 8 ARG B CZ 7220 N NH1 . ARG B 8 ? 1.7207 1.9015 2.8301 -0.3524 -0.1332 0.0455 8 ARG B NH1 7221 N NH2 . ARG B 8 ? 1.7780 2.0124 3.0291 -0.3271 -0.1304 0.0533 8 ARG B NH2 7222 N N . GLY B 9 ? 2.2464 2.3334 3.0020 -0.4104 -0.2856 0.0497 9 GLY B N 7223 C CA . GLY B 9 ? 2.3238 2.3797 2.9916 -0.4218 -0.2894 0.0378 9 GLY B CA 7224 C C . GLY B 9 ? 2.3168 2.3870 2.9660 -0.4416 -0.3347 0.0413 9 GLY B C 7225 O O . GLY B 9 ? 2.4047 2.5013 3.0892 -0.4401 -0.3655 0.0595 9 GLY B O 7226 N N . VAL B 10 ? 2.1951 2.2476 2.7898 -0.4609 -0.3391 0.0237 10 VAL B N 7227 C CA . VAL B 10 ? 2.0274 2.0928 2.5997 -0.4847 -0.3799 0.0221 10 VAL B CA 7228 C C . VAL B 10 ? 1.9656 2.0351 2.4972 -0.4839 -0.4100 0.0385 10 VAL B C 7229 O O . VAL B 10 ? 1.9194 2.0181 2.4907 -0.4869 -0.4442 0.0582 10 VAL B O 7230 C CB . VAL B 10 ? 1.9480 2.0508 2.5988 -0.4977 -0.4044 0.0281 10 VAL B CB 7231 C CG1 . VAL B 10 ? 1.9611 2.0710 2.5805 -0.5271 -0.4409 0.0191 10 VAL B CG1 7232 C CG2 . VAL B 10 ? 1.9287 2.0323 2.6330 -0.4957 -0.3722 0.0174 10 VAL B CG2 7233 N N . SER B 11 ? 2.0209 2.0611 2.4756 -0.4801 -0.3972 0.0314 11 SER B N 7234 C CA . SER B 11 ? 2.0479 2.0886 2.4499 -0.4851 -0.4246 0.0441 11 SER B CA 7235 C C . SER B 11 ? 2.2278 2.2477 2.5452 -0.5057 -0.4263 0.0218 11 SER B C 7236 O O . SER B 11 ? 2.1784 2.2112 2.4720 -0.5304 -0.4588 0.0192 11 SER B O 7237 C CB . SER B 11 ? 1.8757 1.9032 2.2668 -0.4598 -0.4074 0.0588 11 SER B CB 7238 O OG . SER B 11 ? 1.8284 1.8572 2.1715 -0.4660 -0.4351 0.0739 11 SER B OG 7239 N N . SER B 12 ? 2.3499 2.3380 2.6239 -0.4958 -0.3908 0.0049 12 SER B N 7240 C CA . SER B 12 ? 2.3629 2.3289 2.5643 -0.5123 -0.3845 -0.0211 12 SER B CA 7241 C C . SER B 12 ? 2.2532 2.1901 2.4535 -0.5018 -0.3437 -0.0427 12 SER B C 7242 O O . SER B 12 ? 2.1995 2.1313 2.4406 -0.4810 -0.3197 -0.0343 12 SER B O 7243 C CB . SER B 12 ? 2.3519 2.3085 2.4835 -0.5126 -0.3903 -0.0157 12 SER B CB 7244 O OG . SER B 12 ? 2.3926 2.3293 2.4572 -0.5284 -0.3809 -0.0440 12 SER B OG 7245 N N . CYS B 13 ? 2.1722 2.0898 2.3264 -0.5170 -0.3364 -0.0704 13 CYS B N 7246 C CA . CYS B 13 ? 2.0260 1.9135 2.1785 -0.5091 -0.3014 -0.0909 13 CYS B CA 7247 C C . CYS B 13 ? 1.9924 1.8593 2.1304 -0.4833 -0.2726 -0.0831 13 CYS B C 7248 O O . CYS B 13 ? 1.9461 1.8008 2.1171 -0.4680 -0.2475 -0.0805 13 CYS B O 7249 C CB . CYS B 13 ? 1.9813 1.8506 2.0826 -0.5288 -0.3003 -0.1230 13 CYS B CB 7250 S SG . CYS B 13 ? 2.2756 2.1043 2.3741 -0.5189 -0.2605 -0.1476 13 CYS B SG 7251 N N . GLN B 14 ? 2.0626 1.9260 2.1497 -0.4802 -0.2768 -0.0788 14 GLN B N 7252 C CA . GLN B 14 ? 2.1385 1.9835 2.2087 -0.4571 -0.2524 -0.0711 14 GLN B CA 7253 C C . GLN B 14 ? 2.1622 2.0210 2.2832 -0.4374 -0.2506 -0.0436 14 GLN B C 7254 O O . GLN B 14 ? 2.1569 2.0001 2.2900 -0.4177 -0.2240 -0.0399 14 GLN B O 7255 C CB . GLN B 14 ? 2.1192 1.9605 2.1246 -0.4615 -0.2595 -0.0724 14 GLN B CB 7256 C CG . GLN B 14 ? 2.0348 1.8580 2.0211 -0.4391 -0.2363 -0.0647 14 GLN B CG 7257 C CD . GLN B 14 ? 2.0570 1.8749 1.9774 -0.4464 -0.2395 -0.0705 14 GLN B CD 7258 O OE1 . GLN B 14 ? 2.0480 1.8712 1.9308 -0.4689 -0.2532 -0.0864 14 GLN B OE1 7259 N NE2 . GLN B 14 ? 2.0922 1.9004 1.9977 -0.4287 -0.2263 -0.0584 14 GLN B NE2 7260 N N . GLN B 15 ? 2.1434 2.0318 2.2957 -0.4433 -0.2795 -0.0253 15 GLN B N 7261 C CA . GLN B 15 ? 2.1217 2.0261 2.3292 -0.4251 -0.2800 -0.0008 15 GLN B CA 7262 C C . GLN B 15 ? 1.8781 1.7866 2.1486 -0.4190 -0.2616 -0.0033 15 GLN B C 7263 O O . GLN B 15 ? 1.8277 1.7436 2.1434 -0.4014 -0.2494 0.0106 15 GLN B O 7264 C CB . GLN B 15 ? 2.1966 2.1317 2.4241 -0.4340 -0.3194 0.0201 15 GLN B CB 7265 C CG . GLN B 15 ? 2.3457 2.2785 2.5085 -0.4436 -0.3400 0.0259 15 GLN B CG 7266 C CD . GLN B 15 ? 2.3802 2.3416 2.5653 -0.4510 -0.3808 0.0519 15 GLN B CD 7267 O OE1 . GLN B 15 ? 2.3737 2.3549 2.6289 -0.4408 -0.3899 0.0689 15 GLN B OE1 7268 N NE2 . GLN B 15 ? 2.3693 2.3332 2.4958 -0.4697 -0.4059 0.0553 15 GLN B NE2 7269 N N . CYS B 16 ? 1.7740 1.6775 2.0474 -0.4346 -0.2587 -0.0219 16 CYS B N 7270 C CA . CYS B 16 ? 1.7513 1.6583 2.0814 -0.4330 -0.2415 -0.0247 16 CYS B CA 7271 C C . CYS B 16 ? 1.7578 1.6348 2.0768 -0.4182 -0.2031 -0.0313 16 CYS B C 7272 O O . CYS B 16 ? 1.7597 1.6408 2.1228 -0.4076 -0.1837 -0.0236 16 CYS B O 7273 C CB . CYS B 16 ? 1.7125 1.6240 2.0509 -0.4569 -0.2544 -0.0412 16 CYS B CB 7274 S SG . CYS B 16 ? 1.8808 1.7965 2.2877 -0.4589 -0.2338 -0.0441 16 CYS B SG 7275 N N . LEU B 17 ? 1.7107 1.5585 1.9714 -0.4187 -0.1926 -0.0459 17 LEU B N 7276 C CA . LEU B 17 ? 1.6240 1.4412 1.8704 -0.4062 -0.1601 -0.0519 17 LEU B CA 7277 C C . LEU B 17 ? 1.6144 1.4292 1.8608 -0.3838 -0.1449 -0.0357 17 LEU B C 7278 O O . LEU B 17 ? 1.6673 1.4665 1.9229 -0.3728 -0.1187 -0.0338 17 LEU B O 7279 C CB . LEU B 17 ? 1.6578 1.4464 1.8471 -0.4120 -0.1552 -0.0725 17 LEU B CB 7280 C CG . LEU B 17 ? 1.6275 1.4017 1.8188 -0.4291 -0.1538 -0.0938 17 LEU B CG 7281 C CD1 . LEU B 17 ? 1.5803 1.3797 1.7911 -0.4504 -0.1814 -0.0988 17 LEU B CD1 7282 C CD2 . LEU B 17 ? 1.6717 1.4169 1.8104 -0.4304 -0.1456 -0.1146 17 LEU B CD2 7283 N N . ALA B 18 ? 1.6481 1.4776 1.8833 -0.3785 -0.1625 -0.0236 18 ALA B N 7284 C CA . ALA B 18 ? 1.6670 1.4934 1.9001 -0.3579 -0.1509 -0.0091 18 ALA B CA 7285 C C . ALA B 18 ? 1.6637 1.5086 1.9603 -0.3473 -0.1416 0.0042 18 ALA B C 7286 O O . ALA B 18 ? 1.6213 1.4630 1.9241 -0.3299 -0.1278 0.0139 18 ALA B O 7287 C CB . ALA B 18 ? 1.6133 1.4495 1.8181 -0.3575 -0.1746 0.0011 18 ALA B CB 7288 N N . VAL B 19 ? 1.6616 1.5264 2.0067 -0.3585 -0.1481 0.0029 19 VAL B N 7289 C CA . VAL B 19 ? 1.7481 1.6345 2.1597 -0.3508 -0.1379 0.0127 19 VAL B CA 7290 C C . VAL B 19 ? 1.7846 1.6519 2.1991 -0.3434 -0.1008 0.0078 19 VAL B C 7291 O O . VAL B 19 ? 1.7979 1.6621 2.2193 -0.3272 -0.0823 0.0144 19 VAL B O 7292 C CB . VAL B 19 ? 1.8095 1.7251 2.2753 -0.3667 -0.1560 0.0124 19 VAL B CB 7293 C CG1 . VAL B 19 ? 1.7399 1.6792 2.2788 -0.3588 -0.1411 0.0201 19 VAL B CG1 7294 C CG2 . VAL B 19 ? 1.9808 1.9171 2.4444 -0.3755 -0.1959 0.0199 19 VAL B CG2 7295 N N . SER B 20 ? 1.7451 1.5985 2.1530 -0.3565 -0.0908 -0.0038 20 SER B N 7296 C CA . SER B 20 ? 1.7573 1.5919 2.1663 -0.3536 -0.0581 -0.0063 20 SER B CA 7297 C C . SER B 20 ? 1.8701 1.6707 2.2337 -0.3626 -0.0515 -0.0186 20 SER B C 7298 O O . SER B 20 ? 1.8577 1.6562 2.2098 -0.3764 -0.0698 -0.0287 20 SER B O 7299 C CB . SER B 20 ? 1.6454 1.5041 2.1189 -0.3616 -0.0483 -0.0039 20 SER B CB 7300 O OG . SER B 20 ? 1.5535 1.3933 2.0229 -0.3633 -0.0174 -0.0057 20 SER B OG 7301 N N . PRO B 21 ? 1.8669 1.6403 2.2055 -0.3550 -0.0262 -0.0183 21 PRO B N 7302 C CA . PRO B 21 ? 1.7304 1.4701 2.0366 -0.3628 -0.0181 -0.0279 21 PRO B CA 7303 C C . PRO B 21 ? 1.6906 1.4343 2.0283 -0.3825 -0.0216 -0.0339 21 PRO B C 7304 O O . PRO B 21 ? 1.7813 1.5050 2.0992 -0.3927 -0.0292 -0.0460 21 PRO B O 7305 C CB . PRO B 21 ? 1.7674 1.4871 2.0602 -0.3529 0.0097 -0.0205 21 PRO B CB 7306 C CG . PRO B 21 ? 1.8132 1.5472 2.1056 -0.3358 0.0121 -0.0120 21 PRO B CG 7307 C CD . PRO B 21 ? 1.8109 1.5825 2.1483 -0.3383 -0.0059 -0.0088 21 PRO B CD 7308 N N . MET B 22 ? 1.7177 1.4874 2.1070 -0.3879 -0.0154 -0.0268 22 MET B N 7309 C CA . MET B 22 ? 1.9179 1.6981 2.3441 -0.4076 -0.0223 -0.0318 22 MET B CA 7310 C C . MET B 22 ? 2.0029 1.8167 2.4572 -0.4133 -0.0511 -0.0338 22 MET B C 7311 O O . MET B 22 ? 2.0451 1.8908 2.5394 -0.4074 -0.0544 -0.0246 22 MET B O 7312 C CB . MET B 22 ? 1.8945 1.6849 2.3628 -0.4135 0.0017 -0.0236 22 MET B CB 7313 C CG . MET B 22 ? 1.8797 1.6970 2.3776 -0.4001 0.0152 -0.0135 22 MET B CG 7314 S SD . MET B 22 ? 2.3522 2.1875 2.9040 -0.4114 0.0447 -0.0076 22 MET B SD 7315 C CE . MET B 22 ? 1.9920 1.8520 2.5963 -0.4332 0.0231 -0.0132 22 MET B CE 7316 N N . CYS B 23 ? 1.9706 1.7765 2.4050 -0.4256 -0.0723 -0.0465 23 CYS B N 7317 C CA . CYS B 23 ? 1.8858 1.7187 2.3321 -0.4338 -0.1037 -0.0495 23 CYS B CA 7318 C C . CYS B 23 ? 1.8821 1.6960 2.2957 -0.4495 -0.1189 -0.0683 23 CYS B C 7319 O O . CYS B 23 ? 1.9682 1.7477 2.3462 -0.4485 -0.1058 -0.0781 23 CYS B O 7320 C CB . CYS B 23 ? 1.9509 1.7957 2.3761 -0.4184 -0.1160 -0.0409 23 CYS B CB 7321 S SG . CYS B 23 ? 2.1005 1.9877 2.5885 -0.4075 -0.1209 -0.0218 23 CYS B SG 7322 N N . ALA B 24 ? 1.8701 1.7064 2.2967 -0.4644 -0.1470 -0.0740 24 ALA B N 7323 C CA . ALA B 24 ? 1.9389 1.7592 2.3317 -0.4806 -0.1622 -0.0949 24 ALA B CA 7324 C C . ALA B 24 ? 2.0881 1.9367 2.4784 -0.4930 -0.1967 -0.0973 24 ALA B C 7325 O O . ALA B 24 ? 2.1128 1.9935 2.5347 -0.4891 -0.2108 -0.0808 24 ALA B O 7326 C CB . ALA B 24 ? 1.9317 1.7379 2.3507 -0.4968 -0.1545 -0.1060 24 ALA B CB 7327 N N . TRP B 25 ? 2.1244 1.9607 2.4785 -0.5089 -0.2107 -0.1184 25 TRP B N 7328 C CA . TRP B 25 ? 2.0364 1.8970 2.3792 -0.5253 -0.2446 -0.1228 25 TRP B CA 7329 C C . TRP B 25 ? 1.9057 1.7596 2.2522 -0.5501 -0.2554 -0.1463 25 TRP B C 7330 O O . TRP B 25 ? 1.8232 1.6511 2.1795 -0.5524 -0.2359 -0.1582 25 TRP B O 7331 C CB . TRP B 25 ? 1.9911 1.8446 2.2687 -0.5203 -0.2518 -0.1264 25 TRP B CB 7332 C CG . TRP B 25 ? 2.0934 1.9724 2.3515 -0.5378 -0.2875 -0.1268 25 TRP B CG 7333 C CD1 . TRP B 25 ? 2.1634 2.0364 2.3759 -0.5588 -0.3025 -0.1501 25 TRP B CD1 7334 C CD2 . TRP B 25 ? 2.2152 2.1292 2.4985 -0.5370 -0.3136 -0.1026 25 TRP B CD2 7335 N NE1 . TRP B 25 ? 2.2172 2.1196 2.4197 -0.5729 -0.3371 -0.1407 25 TRP B NE1 7336 C CE2 . TRP B 25 ? 2.2510 2.1784 2.4984 -0.5593 -0.3459 -0.1103 25 TRP B CE2 7337 C CE3 . TRP B 25 ? 2.2535 2.1887 2.5880 -0.5200 -0.3130 -0.0759 25 TRP B CE3 7338 C CZ2 . TRP B 25 ? 2.3120 2.2722 2.5727 -0.5652 -0.3801 -0.0889 25 TRP B CZ2 7339 C CZ3 . TRP B 25 ? 2.2474 2.2152 2.6008 -0.5241 -0.3459 -0.0566 25 TRP B CZ3 7340 C CH2 . TRP B 25 ? 2.2774 2.2570 2.5939 -0.5466 -0.3804 -0.0615 25 TRP B CH2 7341 N N . CYS B 26 ? 1.8728 1.7487 2.2116 -0.5697 -0.2873 -0.1525 26 CYS B N 7342 C CA . CYS B 26 ? 1.9837 1.8534 2.3231 -0.5949 -0.2991 -0.1774 26 CYS B CA 7343 C C . CYS B 26 ? 2.0781 1.9612 2.3729 -0.6157 -0.3306 -0.1910 26 CYS B C 7344 O O . CYS B 26 ? 2.1386 2.0502 2.4283 -0.6167 -0.3547 -0.1733 26 CYS B O 7345 C CB . CYS B 26 ? 2.0253 1.9155 2.4370 -0.6051 -0.3054 -0.1692 26 CYS B CB 7346 S SG . CYS B 26 ? 2.4032 2.2846 2.8245 -0.6369 -0.3193 -0.1992 26 CYS B SG 7347 N N . SER B 27 ? 2.1769 2.0384 2.4393 -0.6332 -0.3302 -0.2227 27 SER B N 7348 C CA . SER B 27 ? 2.2395 2.1156 2.4708 -0.6609 -0.3611 -0.2404 27 SER B CA 7349 C C . SER B 27 ? 2.3959 2.2656 2.6621 -0.6821 -0.3656 -0.2617 27 SER B C 7350 O O . SER B 27 ? 2.4396 2.2760 2.6962 -0.6844 -0.3457 -0.2874 27 SER B O 7351 C CB . SER B 27 ? 2.1206 1.9781 2.2742 -0.6651 -0.3561 -0.2636 27 SER B CB 7352 O OG . SER B 27 ? 2.0338 1.8525 2.1769 -0.6559 -0.3241 -0.2862 27 SER B OG 7353 N N . ASP B 28 ? 2.4574 2.3589 2.7671 -0.6976 -0.3931 -0.2509 28 ASP B N 7354 C CA . ASP B 28 ? 2.6223 2.5213 2.9821 -0.7147 -0.3956 -0.2637 28 ASP B CA 7355 C C . ASP B 28 ? 2.7142 2.6139 3.0480 -0.7473 -0.4205 -0.2947 28 ASP B C 7356 O O . ASP B 28 ? 2.7243 2.6239 3.0999 -0.7645 -0.4268 -0.3061 28 ASP B O 7357 C CB . ASP B 28 ? 2.7007 2.6348 3.1356 -0.7124 -0.4076 -0.2344 28 ASP B CB 7358 C CG . ASP B 28 ? 2.7242 2.6991 3.1581 -0.7169 -0.4431 -0.2135 28 ASP B CG 7359 O OD1 . ASP B 28 ? 2.7520 2.7262 3.1226 -0.7177 -0.4544 -0.2158 28 ASP B OD1 7360 O OD2 . ASP B 28 ? 2.6824 2.6902 3.1808 -0.7200 -0.4598 -0.1940 28 ASP B OD2 7361 N N . GLU B 29 ? 2.6591 2.5609 2.9240 -0.7573 -0.4347 -0.3079 29 GLU B N 7362 C CA . GLU B 29 ? 2.6497 2.5528 2.8771 -0.7902 -0.4579 -0.3400 29 GLU B CA 7363 C C . GLU B 29 ? 2.4842 2.4264 2.7452 -0.8136 -0.4993 -0.3280 29 GLU B C 7364 O O . GLU B 29 ? 2.5652 2.5160 2.7907 -0.8430 -0.5256 -0.3493 29 GLU B O 7365 C CB . GLU B 29 ? 2.7257 2.5919 2.9596 -0.7996 -0.4374 -0.3774 29 GLU B CB 7366 C CG . GLU B 29 ? 2.7348 2.5607 2.9483 -0.7764 -0.3977 -0.3892 29 GLU B CG 7367 C CD . GLU B 29 ? 2.7476 2.5414 3.0099 -0.7743 -0.3759 -0.4028 29 GLU B CD 7368 O OE1 . GLU B 29 ? 2.7407 2.5434 3.0658 -0.7684 -0.3742 -0.3790 29 GLU B OE1 7369 O OE2 . GLU B 29 ? 2.7576 2.5173 2.9970 -0.7792 -0.3603 -0.4374 29 GLU B OE2 7370 N N . ALA B 30 ? 2.3067 2.2735 2.6369 -0.8011 -0.5047 -0.2948 30 ALA B N 7371 C CA . ALA B 30 ? 2.3641 2.3707 2.7397 -0.8202 -0.5435 -0.2800 30 ALA B CA 7372 C C . ALA B 30 ? 2.4027 2.4433 2.8002 -0.8035 -0.5602 -0.2391 30 ALA B C 7373 O O . ALA B 30 ? 2.3210 2.3527 2.6940 -0.7787 -0.5413 -0.2243 30 ALA B O 7374 C CB . ALA B 30 ? 2.2642 2.2716 2.7193 -0.8249 -0.5359 -0.2818 30 ALA B CB 7375 N N . LEU B 31 ? 2.5400 2.6195 2.9875 -0.8170 -0.5964 -0.2211 31 LEU B N 7376 C CA . LEU B 31 ? 2.5930 2.7062 3.0737 -0.8011 -0.6150 -0.1821 31 LEU B CA 7377 C C . LEU B 31 ? 2.6319 2.7768 3.2169 -0.7954 -0.6214 -0.1601 31 LEU B C 7378 O O . LEU B 31 ? 2.6701 2.8527 3.2918 -0.8077 -0.6615 -0.1425 31 LEU B O 7379 C CB . LEU B 31 ? 2.6093 2.7457 3.0417 -0.8225 -0.6620 -0.1744 31 LEU B CB 7380 C CG . LEU B 31 ? 2.5810 2.7146 2.9551 -0.8073 -0.6632 -0.1557 31 LEU B CG 7381 C CD1 . LEU B 31 ? 2.6174 2.7736 2.9417 -0.8345 -0.7126 -0.1481 31 LEU B CD1 7382 C CD2 . LEU B 31 ? 2.4438 2.5921 2.8796 -0.7740 -0.6522 -0.1198 31 LEU B CD2 7383 N N . PRO B 32 ? 2.5237 2.6545 3.1580 -0.7777 -0.5822 -0.1607 32 PRO B N 7384 C CA . PRO B 32 ? 2.4385 2.6018 3.1710 -0.7680 -0.5821 -0.1372 32 PRO B CA 7385 C C . PRO B 32 ? 2.3909 2.5675 3.1410 -0.7373 -0.5731 -0.1069 32 PRO B C 7386 O O . PRO B 32 ? 2.3706 2.5289 3.1314 -0.7136 -0.5324 -0.1033 32 PRO B O 7387 C CB . PRO B 32 ? 2.2898 2.4284 3.0546 -0.7649 -0.5418 -0.1520 32 PRO B CB 7388 C CG . PRO B 32 ? 2.2221 2.3134 2.9095 -0.7547 -0.5111 -0.1704 32 PRO B CG 7389 C CD . PRO B 32 ? 2.3333 2.4194 2.9395 -0.7688 -0.5384 -0.1832 32 PRO B CD 7390 N N . LEU B 33 ? 2.3710 2.5775 3.1233 -0.7388 -0.6114 -0.0856 33 LEU B N 7391 C CA . LEU B 33 ? 2.3632 2.5762 3.1144 -0.7114 -0.6071 -0.0593 33 LEU B CA 7392 C C . LEU B 33 ? 2.3150 2.5329 3.1378 -0.6837 -0.5697 -0.0465 33 LEU B C 7393 O O . LEU B 33 ? 2.2601 2.4533 3.0528 -0.6605 -0.5360 -0.0445 33 LEU B O 7394 C CB . LEU B 33 ? 2.3826 2.6338 3.1547 -0.7191 -0.6588 -0.0339 33 LEU B CB 7395 C CG . LEU B 33 ? 2.3011 2.5592 3.0740 -0.6928 -0.6608 -0.0052 33 LEU B CG 7396 C CD1 . LEU B 33 ? 2.1908 2.4109 2.8643 -0.6842 -0.6405 -0.0135 33 LEU B CD1 7397 C CD2 . LEU B 33 ? 2.3080 2.6034 3.1070 -0.7035 -0.7168 0.0212 33 LEU B CD2 7398 N N . GLY B 34 ? 2.2216 2.4726 3.1377 -0.6874 -0.5760 -0.0383 34 GLY B N 7399 C CA . GLY B 34 ? 2.1183 2.3717 3.1010 -0.6702 -0.5347 -0.0356 34 GLY B CA 7400 C C . GLY B 34 ? 2.1298 2.3703 3.1027 -0.6379 -0.5024 -0.0226 34 GLY B C 7401 O O . GLY B 34 ? 2.1343 2.3899 3.1102 -0.6239 -0.5204 -0.0028 34 GLY B O 7402 N N . SER B 35 ? 2.2290 2.4408 3.1908 -0.6271 -0.4557 -0.0331 35 SER B N 7403 C CA . SER B 35 ? 2.3610 2.5445 3.2739 -0.6018 -0.4254 -0.0290 35 SER B CA 7404 C C . SER B 35 ? 2.2782 2.4150 3.1320 -0.6019 -0.3890 -0.0491 35 SER B C 7405 O O . SER B 35 ? 2.2150 2.3377 3.0801 -0.5856 -0.3502 -0.0468 35 SER B O 7406 C CB . SER B 35 ? 2.3787 2.5833 3.3607 -0.5777 -0.4019 -0.0114 35 SER B CB 7407 O OG . SER B 35 ? 2.3995 2.6111 3.4405 -0.5821 -0.3730 -0.0173 35 SER B OG 7408 N N . PRO B 36 ? 2.2113 2.3239 3.0034 -0.6209 -0.4014 -0.0692 36 PRO B N 7409 C CA . PRO B 36 ? 2.1741 2.2403 2.9081 -0.6151 -0.3675 -0.0856 36 PRO B CA 7410 C C . PRO B 36 ? 2.2039 2.2519 2.8843 -0.5912 -0.3537 -0.0774 36 PRO B C 7411 O O . PRO B 36 ? 2.3054 2.3319 2.9802 -0.5734 -0.3180 -0.0751 36 PRO B O 7412 C CB . PRO B 36 ? 2.1291 2.1774 2.8132 -0.6403 -0.3873 -0.1105 36 PRO B CB 7413 C CG . PRO B 36 ? 1.9969 2.0823 2.7296 -0.6626 -0.4244 -0.1083 36 PRO B CG 7414 C CD . PRO B 36 ? 2.0645 2.1885 2.8422 -0.6486 -0.4414 -0.0806 36 PRO B CD 7415 N N . ARG B 37 ? 2.1821 2.2393 2.8230 -0.5929 -0.3833 -0.0723 37 ARG B N 7416 C CA . ARG B 37 ? 2.0937 2.1454 2.6981 -0.5713 -0.3794 -0.0580 37 ARG B CA 7417 C C . ARG B 37 ? 2.0517 2.0647 2.6130 -0.5528 -0.3391 -0.0649 37 ARG B C 7418 O O . ARG B 37 ? 2.0004 1.9817 2.5144 -0.5603 -0.3264 -0.0859 37 ARG B O 7419 C CB . ARG B 37 ? 2.0119 2.0988 2.6849 -0.5559 -0.3870 -0.0316 37 ARG B CB 7420 C CG . ARG B 37 ? 2.1177 2.2444 2.8362 -0.5728 -0.4315 -0.0215 37 ARG B CG 7421 C CD . ARG B 37 ? 2.1236 2.2856 2.9195 -0.5562 -0.4393 0.0038 37 ARG B CD 7422 N NE . ARG B 37 ? 2.1686 2.3697 3.0172 -0.5730 -0.4830 0.0139 37 ARG B NE 7423 C CZ . ARG B 37 ? 2.1143 2.3293 2.9394 -0.5816 -0.5263 0.0268 37 ARG B CZ 7424 N NH1 . ARG B 37 ? 2.1215 2.3149 2.8706 -0.5754 -0.5296 0.0307 37 ARG B NH1 7425 N NH2 . ARG B 37 ? 2.0103 2.2613 2.8882 -0.5977 -0.5670 0.0369 37 ARG B NH2 7426 N N . CYS B 38 ? 2.1148 2.1311 2.6955 -0.5285 -0.3202 -0.0475 38 CYS B N 7427 C CA . CYS B 38 ? 2.1349 2.1183 2.6866 -0.5103 -0.2814 -0.0508 38 CYS B CA 7428 C C . CYS B 38 ? 2.1745 2.1637 2.7877 -0.5028 -0.2526 -0.0449 38 CYS B C 7429 O O . CYS B 38 ? 2.1843 2.2055 2.8596 -0.4964 -0.2562 -0.0299 38 CYS B O 7430 C CB . CYS B 38 ? 1.9920 1.9711 2.5100 -0.4895 -0.2794 -0.0372 38 CYS B CB 7431 S SG . CYS B 38 ? 1.9615 1.9140 2.4730 -0.4635 -0.2332 -0.0331 38 CYS B SG 7432 N N . ASP B 39 ? 2.1851 2.1439 2.7826 -0.5043 -0.2240 -0.0566 39 ASP B N 7433 C CA . ASP B 39 ? 2.1335 2.0963 2.7830 -0.5018 -0.1959 -0.0513 39 ASP B CA 7434 C C . ASP B 39 ? 2.1222 2.0440 2.7358 -0.4967 -0.1624 -0.0581 39 ASP B C 7435 O O . ASP B 39 ? 2.0716 1.9619 2.6243 -0.4933 -0.1608 -0.0678 39 ASP B O 7436 C CB . ASP B 39 ? 2.1918 2.1765 2.8971 -0.5241 -0.2085 -0.0562 39 ASP B CB 7437 C CG . ASP B 39 ? 2.2268 2.2453 3.0109 -0.5204 -0.1958 -0.0429 39 ASP B CG 7438 O OD1 . ASP B 39 ? 2.2102 2.2173 3.0056 -0.5138 -0.1610 -0.0398 39 ASP B OD1 7439 O OD2 . ASP B 39 ? 2.2750 2.3321 3.1106 -0.5251 -0.2208 -0.0357 39 ASP B OD2 7440 N N . LEU B 40 ? 2.0951 2.0185 2.7486 -0.4972 -0.1361 -0.0524 40 LEU B N 7441 C CA . LEU B 40 ? 1.9708 1.8565 2.5968 -0.4959 -0.1062 -0.0556 40 LEU B CA 7442 C C . LEU B 40 ? 1.8278 1.6895 2.4424 -0.5163 -0.1129 -0.0711 40 LEU B C 7443 O O . LEU B 40 ? 1.7863 1.6658 2.4270 -0.5336 -0.1359 -0.0788 40 LEU B O 7444 C CB . LEU B 40 ? 1.8704 1.7675 2.5411 -0.4934 -0.0761 -0.0437 40 LEU B CB 7445 C CG . LEU B 40 ? 1.7829 1.7036 2.4746 -0.4737 -0.0632 -0.0307 40 LEU B CG 7446 C CD1 . LEU B 40 ? 1.7952 1.6980 2.4299 -0.4538 -0.0669 -0.0292 40 LEU B CD1 7447 C CD2 . LEU B 40 ? 1.6985 1.6676 2.4578 -0.4760 -0.0815 -0.0254 40 LEU B CD2 7448 N N . LYS B 41 ? 1.7881 1.6087 2.3653 -0.5145 -0.0942 -0.0758 41 LYS B N 7449 C CA . LYS B 41 ? 1.8124 1.6053 2.3836 -0.5326 -0.0974 -0.0902 41 LYS B CA 7450 C C . LYS B 41 ? 1.9633 1.7739 2.5948 -0.5527 -0.0958 -0.0872 41 LYS B C 7451 O O . LYS B 41 ? 2.0953 1.9191 2.7485 -0.5700 -0.1183 -0.0984 41 LYS B O 7452 C CB . LYS B 41 ? 1.8174 1.5644 2.3501 -0.5254 -0.0753 -0.0904 41 LYS B CB 7453 C CG . LYS B 41 ? 1.7941 1.5138 2.2688 -0.5155 -0.0832 -0.1044 41 LYS B CG 7454 C CD . LYS B 41 ? 1.7439 1.4412 2.2109 -0.5325 -0.0973 -0.1269 41 LYS B CD 7455 C CE . LYS B 41 ? 1.7676 1.4324 2.2515 -0.5427 -0.0819 -0.1254 41 LYS B CE 7456 N NZ . LYS B 41 ? 1.7813 1.4199 2.2606 -0.5579 -0.0946 -0.1491 41 LYS B NZ 7457 N N . GLU B 42 ? 2.0414 1.8535 2.6988 -0.5515 -0.0689 -0.0725 42 GLU B N 7458 C CA . GLU B 42 ? 2.1715 1.9987 2.8857 -0.5715 -0.0614 -0.0680 42 GLU B CA 7459 C C . GLU B 42 ? 2.2208 2.0952 2.9908 -0.5818 -0.0835 -0.0699 42 GLU B C 7460 O O . GLU B 42 ? 2.2086 2.0917 3.0193 -0.6032 -0.0901 -0.0742 42 GLU B O 7461 C CB . GLU B 42 ? 2.1808 2.0109 2.9107 -0.5666 -0.0273 -0.0507 42 GLU B CB 7462 C CG . GLU B 42 ? 2.1374 1.9918 2.8659 -0.5444 -0.0177 -0.0412 42 GLU B CG 7463 C CD . GLU B 42 ? 2.1165 1.9741 2.8585 -0.5421 0.0180 -0.0274 42 GLU B CD 7464 O OE1 . GLU B 42 ? 2.1759 2.0354 2.9500 -0.5610 0.0328 -0.0231 42 GLU B OE1 7465 O OE2 . GLU B 42 ? 1.9620 1.8200 2.6810 -0.5227 0.0316 -0.0213 42 GLU B OE2 7466 N N . ASN B 43 ? 2.2055 2.1097 2.9791 -0.5671 -0.0966 -0.0658 43 ASN B N 7467 C CA . ASN B 43 ? 2.1608 2.1100 2.9864 -0.5752 -0.1227 -0.0658 43 ASN B CA 7468 C C . ASN B 43 ? 2.1430 2.0860 2.9466 -0.5898 -0.1572 -0.0823 43 ASN B C 7469 O O . ASN B 43 ? 2.2393 2.1954 3.0808 -0.6112 -0.1720 -0.0892 43 ASN B O 7470 C CB . ASN B 43 ? 1.9893 1.9693 2.8265 -0.5546 -0.1278 -0.0544 43 ASN B CB 7471 C CG . ASN B 43 ? 1.9518 1.9552 2.8392 -0.5461 -0.0983 -0.0412 43 ASN B CG 7472 O OD1 . ASN B 43 ? 1.9931 2.0354 2.9509 -0.5544 -0.1012 -0.0372 43 ASN B OD1 7473 N ND2 . ASN B 43 ? 1.9546 1.9355 2.8071 -0.5303 -0.0693 -0.0356 43 ASN B ND2 7474 N N . LEU B 44 ? 1.9318 1.8559 2.6737 -0.5791 -0.1693 -0.0894 44 LEU B N 7475 C CA . LEU B 44 ? 1.8901 1.8051 2.5990 -0.5930 -0.1989 -0.1079 44 LEU B CA 7476 C C . LEU B 44 ? 1.7909 1.6757 2.4983 -0.6131 -0.1951 -0.1248 44 LEU B C 7477 O O . LEU B 44 ? 1.7654 1.6518 2.4704 -0.6319 -0.2197 -0.1415 44 LEU B O 7478 C CB . LEU B 44 ? 2.0197 1.9131 2.6570 -0.5775 -0.2024 -0.1134 44 LEU B CB 7479 C CG . LEU B 44 ? 2.1139 2.0184 2.7171 -0.5853 -0.2368 -0.1244 44 LEU B CG 7480 C CD1 . LEU B 44 ? 1.9464 1.8399 2.4918 -0.5654 -0.2342 -0.1207 44 LEU B CD1 7481 C CD2 . LEU B 44 ? 2.0899 1.9715 2.6686 -0.6071 -0.2487 -0.1507 44 LEU B CD2 7482 N N . LEU B 45 ? 1.7214 1.5782 2.4308 -0.6102 -0.1651 -0.1199 45 LEU B N 7483 C CA . LEU B 45 ? 1.7301 1.5537 2.4413 -0.6280 -0.1598 -0.1329 45 LEU B CA 7484 C C . LEU B 45 ? 2.0353 1.8821 2.8070 -0.6531 -0.1726 -0.1358 45 LEU B C 7485 O O . LEU B 45 ? 2.2180 2.0504 2.9873 -0.6719 -0.1891 -0.1549 45 LEU B O 7486 C CB . LEU B 45 ? 1.6278 1.4191 2.3314 -0.6201 -0.1262 -0.1210 45 LEU B CB 7487 C CG . LEU B 45 ? 1.6753 1.4165 2.3216 -0.6110 -0.1179 -0.1312 45 LEU B CG 7488 C CD1 . LEU B 45 ? 1.5263 1.2679 2.1212 -0.5954 -0.1312 -0.1413 45 LEU B CD1 7489 C CD2 . LEU B 45 ? 1.6364 1.3544 2.2741 -0.5997 -0.0869 -0.1128 45 LEU B CD2 7490 N N . LYS B 46 ? 2.0958 1.9795 2.9241 -0.6539 -0.1645 -0.1184 46 LYS B N 7491 C CA . LYS B 46 ? 2.2493 2.1584 3.1423 -0.6777 -0.1740 -0.1193 46 LYS B CA 7492 C C . LYS B 46 ? 2.2371 2.1839 3.1489 -0.6861 -0.2119 -0.1267 46 LYS B C 7493 O O . LYS B 46 ? 2.3575 2.3292 3.3221 -0.7068 -0.2274 -0.1297 46 LYS B O 7494 C CB . LYS B 46 ? 2.2687 2.2042 3.2186 -0.6764 -0.1476 -0.0991 46 LYS B CB 7495 C CG . LYS B 46 ? 2.4128 2.3616 3.4260 -0.7030 -0.1460 -0.0992 46 LYS B CG 7496 C CD . LYS B 46 ? 2.4047 2.3149 3.4110 -0.7119 -0.1157 -0.0937 46 LYS B CD 7497 C CE . LYS B 46 ? 2.3265 2.1829 3.2816 -0.7178 -0.1239 -0.1097 46 LYS B CE 7498 N NZ . LYS B 46 ? 2.2498 2.0663 3.1989 -0.7256 -0.0971 -0.1009 46 LYS B NZ 7499 N N . ASP B 47 ? 2.0303 1.9809 2.8972 -0.6711 -0.2275 -0.1286 47 ASP B N 7500 C CA . ASP B 47 ? 1.9824 1.9621 2.8498 -0.6796 -0.2666 -0.1352 47 ASP B CA 7501 C C . ASP B 47 ? 1.9981 1.9475 2.8135 -0.6951 -0.2849 -0.1615 47 ASP B C 7502 O O . ASP B 47 ? 2.0241 1.9888 2.8179 -0.7034 -0.3168 -0.1706 47 ASP B O 7503 C CB . ASP B 47 ? 1.9552 1.9547 2.8007 -0.6573 -0.2747 -0.1219 47 ASP B CB 7504 C CG . ASP B 47 ? 1.9495 1.9833 2.8544 -0.6428 -0.2593 -0.0991 47 ASP B CG 7505 O OD1 . ASP B 47 ? 1.8610 1.9215 2.8356 -0.6552 -0.2572 -0.0942 47 ASP B OD1 7506 O OD2 . ASP B 47 ? 2.0872 2.1217 2.9711 -0.6194 -0.2484 -0.0874 47 ASP B OD2 7507 N N . ASN B 48 ? 2.0948 2.0007 2.8904 -0.6991 -0.2640 -0.1733 48 ASN B N 7508 C CA . ASN B 48 ? 2.0803 1.9488 2.8242 -0.7090 -0.2725 -0.2008 48 ASN B CA 7509 C C . ASN B 48 ? 2.0776 1.9334 2.7518 -0.6910 -0.2741 -0.2060 48 ASN B C 7510 O O . ASN B 48 ? 2.0413 1.8890 2.6974 -0.6676 -0.2525 -0.1908 48 ASN B O 7511 C CB . ASN B 48 ? 1.8470 1.7313 2.6065 -0.7372 -0.3059 -0.2201 48 ASN B CB 7512 C CG . ASN B 48 ? 1.7869 1.6846 2.6180 -0.7571 -0.3056 -0.2159 48 ASN B CG 7513 O OD1 . ASN B 48 ? 1.7252 1.6335 2.6009 -0.7500 -0.2836 -0.1947 48 ASN B OD1 7514 N ND2 . ASN B 48 ? 2.0220 1.9195 2.8638 -0.7836 -0.3292 -0.2372 48 ASN B ND2 7515 N N . CYS B 49 ? 2.1188 1.9733 2.7531 -0.7033 -0.2991 -0.2282 49 CYS B N 7516 C CA . CYS B 49 ? 2.1632 2.0066 2.7288 -0.6904 -0.3013 -0.2359 49 CYS B CA 7517 C C . CYS B 49 ? 2.2803 2.0800 2.8123 -0.6714 -0.2693 -0.2394 49 CYS B C 7518 O O . CYS B 49 ? 2.2388 2.0383 2.7517 -0.6483 -0.2543 -0.2223 49 CYS B O 7519 C CB . CYS B 49 ? 2.1480 2.0287 2.7124 -0.6758 -0.3128 -0.2114 49 CYS B CB 7520 S SG . CYS B 49 ? 2.7560 2.6277 3.2374 -0.6617 -0.3174 -0.2166 49 CYS B SG 7521 N N . ALA B 50 ? 2.3090 2.0715 2.8381 -0.6813 -0.2597 -0.2610 50 ALA B N 7522 C CA . ALA B 50 ? 2.2592 1.9787 2.7549 -0.6649 -0.2344 -0.2674 50 ALA B CA 7523 C C . ALA B 50 ? 2.4752 2.1594 2.9428 -0.6770 -0.2368 -0.3038 50 ALA B C 7524 O O . ALA B 50 ? 2.5305 2.1783 3.0148 -0.6785 -0.2217 -0.3113 50 ALA B O 7525 C CB . ALA B 50 ? 2.1015 1.8035 2.6356 -0.6566 -0.2089 -0.2467 50 ALA B CB 7526 N N . PRO B 51 ? 2.6164 2.3107 3.0419 -0.6867 -0.2556 -0.3269 51 PRO B N 7527 C CA . PRO B 51 ? 2.6385 2.2971 3.0284 -0.6913 -0.2499 -0.3626 51 PRO B CA 7528 C C . PRO B 51 ? 2.5458 2.1919 2.8859 -0.6680 -0.2337 -0.3617 51 PRO B C 7529 O O . PRO B 51 ? 2.5964 2.2464 2.8879 -0.6726 -0.2412 -0.3835 51 PRO B O 7530 C CB . PRO B 51 ? 2.6687 2.3481 3.0378 -0.7173 -0.2778 -0.3887 51 PRO B CB 7531 C CG . PRO B 51 ? 2.6742 2.3997 3.0383 -0.7155 -0.2967 -0.3624 51 PRO B CG 7532 C CD . PRO B 51 ? 2.6259 2.3629 3.0412 -0.6997 -0.2848 -0.3249 51 PRO B CD 7533 N N . GLU B 52 ? 2.4444 2.0773 2.7962 -0.6451 -0.2120 -0.3364 52 GLU B N 7534 C CA . GLU B 52 ? 2.3870 2.0130 2.6984 -0.6210 -0.1969 -0.3279 52 GLU B CA 7535 C C . GLU B 52 ? 2.2980 1.9643 2.5856 -0.6153 -0.2100 -0.3092 52 GLU B C 7536 O O . GLU B 52 ? 2.3178 1.9836 2.5722 -0.5965 -0.2002 -0.2996 52 GLU B O 7537 C CB . GLU B 52 ? 2.4913 2.0884 2.7627 -0.6203 -0.1896 -0.3623 52 GLU B CB 7538 C CG . GLU B 52 ? 2.6149 2.1682 2.9127 -0.6226 -0.1766 -0.3806 52 GLU B CG 7539 C CD . GLU B 52 ? 2.6857 2.2132 2.9502 -0.6212 -0.1687 -0.4175 52 GLU B CD 7540 O OE1 . GLU B 52 ? 2.7103 2.2551 2.9273 -0.6196 -0.1718 -0.4284 52 GLU B OE1 7541 O OE2 . GLU B 52 ? 2.6568 2.1467 2.9447 -0.6222 -0.1592 -0.4355 52 GLU B OE2 7542 N N . SER B 53 ? 2.3147 2.0150 2.6216 -0.6323 -0.2338 -0.3039 53 SER B N 7543 C CA . SER B 53 ? 2.3731 2.1128 2.6659 -0.6296 -0.2517 -0.2846 53 SER B CA 7544 C C . SER B 53 ? 2.4557 2.2032 2.7581 -0.6035 -0.2362 -0.2516 53 SER B C 7545 O O . SER B 53 ? 2.4279 2.1899 2.6976 -0.5925 -0.2407 -0.2408 53 SER B O 7546 C CB . SER B 53 ? 2.3200 2.0938 2.6520 -0.6504 -0.2786 -0.2785 53 SER B CB 7547 O OG . SER B 53 ? 2.3503 2.1618 2.6822 -0.6450 -0.2960 -0.2539 53 SER B OG 7548 N N . ILE B 54 ? 2.5151 2.2526 2.8614 -0.5952 -0.2180 -0.2358 54 ILE B N 7549 C CA . ILE B 54 ? 2.4700 2.2121 2.8257 -0.5717 -0.2001 -0.2074 54 ILE B CA 7550 C C . ILE B 54 ? 2.4008 2.1170 2.7069 -0.5525 -0.1831 -0.2112 54 ILE B C 7551 O O . ILE B 54 ? 2.4152 2.0963 2.7054 -0.5518 -0.1701 -0.2289 54 ILE B O 7552 C CB . ILE B 54 ? 2.4135 2.1457 2.8192 -0.5699 -0.1808 -0.1930 54 ILE B CB 7553 C CG1 . ILE B 54 ? 2.4055 2.0979 2.8133 -0.5800 -0.1711 -0.2129 54 ILE B CG1 7554 C CG2 . ILE B 54 ? 2.4073 2.1760 2.8689 -0.5828 -0.1942 -0.1804 54 ILE B CG2 7555 C CD1 . ILE B 54 ? 2.3953 2.0745 2.8468 -0.5812 -0.1527 -0.1973 54 ILE B CD1 7556 N N . GLU B 55 ? 2.2925 2.0262 2.5775 -0.5371 -0.1842 -0.1945 55 GLU B N 7557 C CA . GLU B 55 ? 2.3208 2.0330 2.5628 -0.5181 -0.1676 -0.1949 55 GLU B CA 7558 C C . GLU B 55 ? 2.3743 2.0859 2.6354 -0.4973 -0.1479 -0.1680 55 GLU B C 7559 O O . GLU B 55 ? 2.4107 2.1500 2.6845 -0.4893 -0.1533 -0.1478 55 GLU B O 7560 C CB . GLU B 55 ? 2.3465 2.0754 2.5418 -0.5181 -0.1833 -0.1988 55 GLU B CB 7561 C CG . GLU B 55 ? 2.3476 2.0516 2.4937 -0.5055 -0.1680 -0.2103 55 GLU B CG 7562 C CD . GLU B 55 ? 2.3730 2.0474 2.5039 -0.5159 -0.1615 -0.2430 55 GLU B CD 7563 O OE1 . GLU B 55 ? 2.4085 2.0869 2.5504 -0.5371 -0.1755 -0.2611 55 GLU B OE1 7564 O OE2 . GLU B 55 ? 2.2867 1.9338 2.3977 -0.5030 -0.1429 -0.2513 55 GLU B OE2 7565 N N . PHE B 56 ? 2.3138 1.9932 2.5774 -0.4892 -0.1257 -0.1682 56 PHE B N 7566 C CA . PHE B 56 ? 2.1537 1.8297 2.4329 -0.4729 -0.1054 -0.1445 56 PHE B CA 7567 C C . PHE B 56 ? 2.0329 1.6730 2.2799 -0.4580 -0.0867 -0.1470 56 PHE B C 7568 O O . PHE B 56 ? 2.1559 1.7676 2.4142 -0.4595 -0.0737 -0.1477 56 PHE B O 7569 C CB . PHE B 56 ? 2.0285 1.7064 2.3579 -0.4831 -0.0979 -0.1350 56 PHE B CB 7570 C CG . PHE B 56 ? 2.0050 1.6799 2.3482 -0.4699 -0.0751 -0.1124 56 PHE B CG 7571 C CD1 . PHE B 56 ? 2.0693 1.7706 2.4174 -0.4564 -0.0721 -0.0957 56 PHE B CD1 7572 C CD2 . PHE B 56 ? 2.0692 1.7143 2.4205 -0.4722 -0.0571 -0.1081 56 PHE B CD2 7573 C CE1 . PHE B 56 ? 2.1716 1.8706 2.5306 -0.4457 -0.0496 -0.0779 56 PHE B CE1 7574 C CE2 . PHE B 56 ? 2.1266 1.7695 2.4851 -0.4628 -0.0359 -0.0878 56 PHE B CE2 7575 C CZ . PHE B 56 ? 2.1839 1.8543 2.5454 -0.4497 -0.0311 -0.0742 56 PHE B CZ 7576 N N . PRO B 57 ? 1.7748 1.4161 1.9828 -0.4444 -0.0867 -0.1474 57 PRO B N 7577 C CA . PRO B 57 ? 1.7684 1.3786 1.9478 -0.4294 -0.0702 -0.1492 57 PRO B CA 7578 C C . PRO B 57 ? 1.8454 1.4464 2.0389 -0.4170 -0.0511 -0.1262 57 PRO B C 7579 O O . PRO B 57 ? 1.9730 1.5978 2.1805 -0.4111 -0.0487 -0.1080 57 PRO B O 7580 C CB . PRO B 57 ? 1.8378 1.4605 1.9772 -0.4199 -0.0764 -0.1518 57 PRO B CB 7581 C CG . PRO B 57 ? 1.8649 1.5254 2.0184 -0.4237 -0.0916 -0.1385 57 PRO B CG 7582 C CD . PRO B 57 ? 1.7089 1.3808 1.8995 -0.4429 -0.1030 -0.1441 57 PRO B CD 7583 N N . VAL B 58 ? 1.7316 1.2981 1.9226 -0.4140 -0.0382 -0.1273 58 VAL B N 7584 C CA . VAL B 58 ? 1.7119 1.2663 1.9086 -0.4047 -0.0203 -0.1059 58 VAL B CA 7585 C C . VAL B 58 ? 1.5458 1.0795 1.7067 -0.3870 -0.0116 -0.1044 58 VAL B C 7586 O O . VAL B 58 ? 1.6621 1.1772 1.8040 -0.3848 -0.0154 -0.1218 58 VAL B O 7587 C CB . VAL B 58 ? 1.7227 1.2530 1.9458 -0.4170 -0.0136 -0.1023 58 VAL B CB 7588 C CG1 . VAL B 58 ? 1.7877 1.2830 2.0027 -0.4202 -0.0178 -0.1213 58 VAL B CG1 7589 C CG2 . VAL B 58 ? 1.7698 1.2896 1.9937 -0.4107 0.0048 -0.0787 58 VAL B CG2 7590 N N . SER B 59 ? 1.4004 0.9388 1.5540 -0.3748 0.0005 -0.0851 59 SER B N 7591 C CA . SER B 59 ? 1.4815 1.0028 1.6026 -0.3582 0.0081 -0.0818 59 SER B CA 7592 C C . SER B 59 ? 1.6538 1.1362 1.7717 -0.3578 0.0155 -0.0804 59 SER B C 7593 O O . SER B 59 ? 1.7932 1.2638 1.9299 -0.3665 0.0221 -0.0688 59 SER B O 7594 C CB . SER B 59 ? 1.6572 1.1951 1.7730 -0.3467 0.0183 -0.0628 59 SER B CB 7595 O OG . SER B 59 ? 1.7107 1.2832 1.8347 -0.3462 0.0092 -0.0625 59 SER B OG 7596 N N . GLU B 60 ? 1.5654 1.0283 1.6611 -0.3483 0.0141 -0.0915 60 GLU B N 7597 C CA . GLU B 60 ? 1.5196 0.9448 1.6183 -0.3479 0.0165 -0.0930 60 GLU B CA 7598 C C . GLU B 60 ? 1.5225 0.9299 1.5985 -0.3326 0.0244 -0.0804 60 GLU B C 7599 O O . GLU B 60 ? 1.4031 0.8203 1.4559 -0.3202 0.0252 -0.0841 60 GLU B O 7600 C CB . GLU B 60 ? 1.4644 0.8776 1.5668 -0.3515 0.0074 -0.1208 60 GLU B CB 7601 C CG . GLU B 60 ? 1.6509 1.0729 1.7779 -0.3693 -0.0015 -0.1348 60 GLU B CG 7602 C CD . GLU B 60 ? 1.8364 1.2474 1.9643 -0.3736 -0.0089 -0.1660 60 GLU B CD 7603 O OE1 . GLU B 60 ? 1.7129 1.1252 1.8175 -0.3634 -0.0076 -0.1793 60 GLU B OE1 7604 O OE2 . GLU B 60 ? 1.9063 1.3077 2.0592 -0.3879 -0.0149 -0.1785 60 GLU B OE2 7605 N N . ALA B 61 ? 1.7066 1.0877 1.7891 -0.3354 0.0293 -0.0644 61 ALA B N 7606 C CA . ALA B 61 ? 1.6597 1.0200 1.7223 -0.3238 0.0343 -0.0506 61 ALA B CA 7607 C C . ALA B 61 ? 1.5594 0.8862 1.6283 -0.3194 0.0273 -0.0604 61 ALA B C 7608 O O . ALA B 61 ? 1.7937 1.0997 1.8513 -0.3114 0.0284 -0.0478 61 ALA B O 7609 C CB . ALA B 61 ? 1.9001 1.2528 1.9617 -0.3310 0.0434 -0.0245 61 ALA B CB 7610 N N . ARG B 62 ? 1.4413 0.7634 1.5303 -0.3250 0.0197 -0.0835 62 ARG B N 7611 C CA . ARG B 62 ? 1.4248 0.7127 1.5339 -0.3241 0.0130 -0.0942 62 ARG B CA 7612 C C . ARG B 62 ? 1.4181 0.6894 1.5159 -0.3078 0.0129 -0.0936 62 ARG B C 7613 O O . ARG B 62 ? 1.4289 0.7182 1.5067 -0.2968 0.0161 -0.1042 62 ARG B O 7614 C CB . ARG B 62 ? 1.4618 0.7546 1.5881 -0.3300 0.0073 -0.1269 62 ARG B CB 7615 C CG . ARG B 62 ? 1.7341 1.0525 1.8670 -0.3448 0.0055 -0.1324 62 ARG B CG 7616 C CD . ARG B 62 ? 1.7611 1.0888 1.8997 -0.3500 -0.0001 -0.1669 62 ARG B CD 7617 N NE . ARG B 62 ? 1.7734 1.0691 1.9423 -0.3549 -0.0048 -0.1845 62 ARG B NE 7618 C CZ . ARG B 62 ? 1.9181 1.2034 2.1155 -0.3706 -0.0104 -0.1889 62 ARG B CZ 7619 N NH1 . ARG B 62 ? 1.9603 1.2667 2.1598 -0.3832 -0.0116 -0.1768 62 ARG B NH1 7620 N NH2 . ARG B 62 ? 1.9459 1.1997 2.1734 -0.3738 -0.0150 -0.2059 62 ARG B NH2 7621 N N . VAL B 63 ? 1.3436 0.5803 1.4560 -0.3073 0.0079 -0.0801 63 VAL B N 7622 C CA . VAL B 63 ? 1.3190 0.5378 1.4286 -0.2925 0.0050 -0.0792 63 VAL B CA 7623 C C . VAL B 63 ? 1.3310 0.5386 1.4688 -0.2874 0.0002 -0.1108 63 VAL B C 7624 O O . VAL B 63 ? 1.5180 0.7086 1.6872 -0.2965 -0.0053 -0.1226 63 VAL B O 7625 C CB . VAL B 63 ? 1.3379 0.5241 1.4512 -0.2944 -0.0011 -0.0489 63 VAL B CB 7626 C CG1 . VAL B 63 ? 1.3291 0.5279 1.4110 -0.3004 0.0067 -0.0209 63 VAL B CG1 7627 C CG2 . VAL B 63 ? 1.9559 1.1122 2.1050 -0.3069 -0.0103 -0.0470 63 VAL B CG2 7628 N N . LEU B 64 ? 1.4220 0.6406 1.5493 -0.2739 0.0037 -0.1264 64 LEU B N 7629 C CA . LEU B 64 ? 1.4190 0.6287 1.5734 -0.2684 0.0024 -0.1586 64 LEU B CA 7630 C C . LEU B 64 ? 1.4108 0.5841 1.5973 -0.2600 -0.0065 -0.1509 64 LEU B C 7631 O O . LEU B 64 ? 1.8118 0.9642 2.0383 -0.2606 -0.0113 -0.1709 64 LEU B O 7632 C CB . LEU B 64 ? 1.5342 0.7728 1.6653 -0.2594 0.0112 -0.1794 64 LEU B CB 7633 C CG . LEU B 64 ? 1.6576 0.9296 1.7655 -0.2697 0.0164 -0.1942 64 LEU B CG 7634 C CD1 . LEU B 64 ? 1.7157 1.0138 1.7994 -0.2631 0.0241 -0.2141 64 LEU B CD1 7635 C CD2 . LEU B 64 ? 1.5639 0.8288 1.6980 -0.2834 0.0128 -0.2168 64 LEU B CD2 7636 N N . GLU B 65 ? 1.3379 0.5032 1.5083 -0.2524 -0.0095 -0.1225 65 GLU B N 7637 C CA . GLU B 65 ? 1.4047 0.5335 1.6039 -0.2473 -0.0222 -0.1065 65 GLU B CA 7638 C C . GLU B 65 ? 1.3911 0.5106 1.5621 -0.2491 -0.0270 -0.0659 65 GLU B C 7639 O O . GLU B 65 ? 1.4148 0.5571 1.5467 -0.2453 -0.0192 -0.0562 65 GLU B O 7640 C CB . GLU B 65 ? 1.4994 0.6251 1.7211 -0.2309 -0.0230 -0.1272 65 GLU B CB 7641 C CG . GLU B 65 ? 1.5315 0.6839 1.7175 -0.2201 -0.0146 -0.1256 65 GLU B CG 7642 C CD . GLU B 65 ? 1.7650 0.9108 1.9780 -0.2045 -0.0170 -0.1397 65 GLU B CD 7643 O OE1 . GLU B 65 ? 1.5098 0.6251 1.7551 -0.1997 -0.0311 -0.1257 65 GLU B OE1 7644 O OE2 . GLU B 65 ? 1.8995 1.0712 2.1027 -0.1980 -0.0054 -0.1640 65 GLU B OE2 7645 N N . ASP B 66 ? 1.6664 0.7519 1.8566 -0.2562 -0.0401 -0.0424 66 ASP B N 7646 C CA . ASP B 66 ? 1.7051 0.7768 1.8698 -0.2582 -0.0470 -0.0049 66 ASP B CA 7647 C C . ASP B 66 ? 1.4240 0.4714 1.6115 -0.2510 -0.0617 0.0091 66 ASP B C 7648 O O . ASP B 66 ? 1.4535 0.4864 1.6608 -0.2573 -0.0677 0.0153 66 ASP B O 7649 C CB . ASP B 66 ? 1.6497 0.7245 1.7867 -0.2766 -0.0419 0.0197 66 ASP B CB 7650 C CG . ASP B 66 ? 1.6066 0.6641 1.7736 -0.2905 -0.0466 0.0195 66 ASP B CG 7651 O OD1 . ASP B 66 ? 1.7915 0.8499 1.9908 -0.2858 -0.0473 -0.0092 66 ASP B OD1 7652 O OD2 . ASP B 66 ? 1.6869 0.7368 1.8392 -0.3051 -0.0465 0.0467 66 ASP B OD2 7653 N N . ARG B 67 ? 1.5154 0.5617 1.6992 -0.2374 -0.0675 0.0152 67 ARG B N 7654 C CA . ARG B 67 ? 1.4450 0.4739 1.6495 -0.2292 -0.0828 0.0311 67 ARG B CA 7655 C C . ARG B 67 ? 1.4630 0.4815 1.6334 -0.2398 -0.0895 0.0723 67 ARG B C 7656 O O . ARG B 67 ? 1.6662 0.6942 1.7953 -0.2469 -0.0820 0.0848 67 ARG B O 7657 C CB . ARG B 67 ? 1.7699 0.8052 1.9925 -0.2098 -0.0867 0.0162 67 ARG B CB 7658 C CG . ARG B 67 ? 1.6456 0.6933 1.9034 -0.1997 -0.0786 -0.0263 67 ARG B CG 7659 C CD . ARG B 67 ? 1.6391 0.6986 1.9093 -0.1825 -0.0780 -0.0414 67 ARG B CD 7660 N NE . ARG B 67 ? 1.6184 0.6900 1.8481 -0.1837 -0.0710 -0.0338 67 ARG B NE 7661 C CZ . ARG B 67 ? 1.5588 0.6440 1.7909 -0.1718 -0.0670 -0.0475 67 ARG B CZ 7662 N NH1 . ARG B 67 ? 1.6696 0.7603 1.9434 -0.1578 -0.0679 -0.0704 67 ARG B NH1 7663 N NH2 . ARG B 67 ? 1.6139 0.7131 1.8040 -0.1732 -0.0602 -0.0385 67 ARG B NH2 7664 N N . PRO B 68 ? 1.4996 0.4995 1.6864 -0.2416 -0.1040 0.0931 68 PRO B N 7665 C CA . PRO B 68 ? 1.6520 0.6435 1.8043 -0.2538 -0.1107 0.1322 68 PRO B CA 7666 C C . PRO B 68 ? 1.5978 0.5934 1.7262 -0.2455 -0.1180 0.1465 68 PRO B C 7667 O O . PRO B 68 ? 1.5079 0.5034 1.6639 -0.2287 -0.1274 0.1351 68 PRO B O 7668 C CB . PRO B 68 ? 1.5664 0.5364 1.7496 -0.2563 -0.1270 0.1470 68 PRO B CB 7669 C CG . PRO B 68 ? 1.5788 0.5467 1.8143 -0.2380 -0.1336 0.1185 68 PRO B CG 7670 C CD . PRO B 68 ? 1.5251 0.5115 1.7624 -0.2337 -0.1154 0.0820 68 PRO B CD 7671 N N . LEU B 69 ? 1.5715 0.5720 1.6502 -0.2579 -0.1133 0.1701 69 LEU B N 7672 C CA . LEU B 69 ? 1.5139 0.5170 1.5636 -0.2534 -0.1215 0.1868 69 LEU B CA 7673 C C . LEU B 69 ? 1.5481 0.5351 1.6213 -0.2476 -0.1457 0.2052 69 LEU B C 7674 O O . LEU B 69 ? 2.1666 1.1390 2.2443 -0.2584 -0.1554 0.2258 69 LEU B O 7675 C CB . LEU B 69 ? 1.5215 0.5306 1.5124 -0.2715 -0.1125 0.2103 69 LEU B CB 7676 C CG . LEU B 69 ? 1.4948 0.5197 1.4613 -0.2804 -0.0896 0.1967 69 LEU B CG 7677 C CD1 . LEU B 69 ? 1.5795 0.6088 1.4939 -0.3005 -0.0805 0.2214 69 LEU B CD1 7678 C CD2 . LEU B 69 ? 1.8564 0.8952 1.8153 -0.2671 -0.0818 0.1737 69 LEU B CD2 7679 N N . SER B 70 ? 1.5367 0.5265 1.6265 -0.2313 -0.1564 0.1985 70 SER B N 7680 C CA . SER B 70 ? 1.9039 0.8802 2.0237 -0.2245 -0.1818 0.2143 70 SER B CA 7681 C C . SER B 70 ? 1.9013 0.8707 1.9774 -0.2379 -0.1962 0.2521 70 SER B C 7682 O O . SER B 70 ? 1.5976 0.5741 1.6191 -0.2517 -0.1844 0.2636 70 SER B O 7683 C CB . SER B 70 ? 1.6156 0.5997 1.7732 -0.2029 -0.1885 0.1935 70 SER B CB 7684 O OG . SER B 70 ? 1.5266 0.5245 1.6486 -0.2003 -0.1817 0.1918 70 SER B OG 7685 N N . ASP B 71 ? 2.0079 0.9644 2.1090 -0.2342 -0.2225 0.2704 71 ASP B N 7686 C CA . ASP B 71 ? 1.9457 0.8935 2.0084 -0.2489 -0.2409 0.3076 71 ASP B CA 7687 C C . ASP B 71 ? 1.7717 0.7247 1.8317 -0.2389 -0.2579 0.3131 71 ASP B C 7688 O O . ASP B 71 ? 1.9889 0.9485 1.9952 -0.2482 -0.2556 0.3256 71 ASP B O 7689 C CB . ASP B 71 ? 2.0512 0.9789 2.1413 -0.2559 -0.2619 0.3289 71 ASP B CB 7690 C CG . ASP B 71 ? 2.0865 1.0081 2.1749 -0.2688 -0.2457 0.3266 71 ASP B CG 7691 O OD1 . ASP B 71 ? 1.9716 0.8988 2.0083 -0.2864 -0.2286 0.3359 71 ASP B OD1 7692 O OD2 . ASP B 71 ? 2.1649 1.0771 2.3054 -0.2614 -0.2494 0.3139 71 ASP B OD2 7693 N N . LYS B 72 ? 1.7138 0.6644 1.8334 -0.2209 -0.2754 0.3035 72 LYS B N 7694 C CA . LYS B 72 ? 2.0216 0.9808 2.1503 -0.2084 -0.2888 0.3017 72 LYS B CA 7695 C C . LYS B 72 ? 2.0626 1.0368 2.2321 -0.1876 -0.2723 0.2627 72 LYS B C 7696 O O . LYS B 72 ? 2.0421 1.0151 2.2653 -0.1768 -0.2683 0.2410 72 LYS B O 7697 C CB . LYS B 72 ? 2.0858 1.0334 2.2528 -0.2049 -0.3247 0.3236 72 LYS B CB 7698 C CG . LYS B 72 ? 2.1013 1.0357 2.2205 -0.2270 -0.3447 0.3642 72 LYS B CG 7699 C CD . LYS B 72 ? 2.1257 1.0588 2.2528 -0.2247 -0.3778 0.3845 72 LYS B CD 7700 C CE . LYS B 72 ? 2.2282 1.1474 2.3075 -0.2488 -0.4002 0.4250 72 LYS B CE 7701 N NZ . LYS B 72 ? 2.1925 1.0939 2.3032 -0.2553 -0.4151 0.4411 72 LYS B NZ 7702 N N . GLY B 73 ? 1.9089 0.8973 2.0512 -0.1833 -0.2625 0.2531 73 GLY B N 7703 C CA . GLY B 73 ? 1.7483 0.7524 1.9200 -0.1665 -0.2447 0.2168 73 GLY B CA 7704 C C . GLY B 73 ? 1.7829 0.7943 2.0057 -0.1486 -0.2606 0.2076 73 GLY B C 7705 O O . GLY B 73 ? 1.6624 0.6892 1.8985 -0.1367 -0.2473 0.1817 73 GLY B O 7706 N N . SER B 74 ? 1.8392 0.8404 2.0929 -0.1473 -0.2898 0.2289 74 SER B N 7707 C CA . SER B 74 ? 1.9767 0.9859 2.2849 -0.1310 -0.3080 0.2227 74 SER B CA 7708 C C . SER B 74 ? 1.7874 0.7947 2.1765 -0.1172 -0.3162 0.2071 74 SER B C 7709 O O . SER B 74 ? 1.6113 0.6032 2.0205 -0.1223 -0.3368 0.2276 74 SER B O 7710 C CB . SER B 74 ? 2.0381 1.0403 2.3252 -0.1393 -0.3391 0.2586 74 SER B CB 7711 O OG . SER B 74 ? 1.7785 0.7622 2.0610 -0.1521 -0.3595 0.2880 74 SER B OG 7712 N N . GLY B 75 ? 1.8442 0.8676 2.2792 -0.1007 -0.2996 0.1701 75 GLY B N 7713 C CA . GLY B 75 ? 1.8239 0.8503 2.3418 -0.0857 -0.3063 0.1505 75 GLY B CA 7714 C C . GLY B 75 ? 2.0955 1.1101 2.6316 -0.0890 -0.2983 0.1412 75 GLY B C 7715 O O . GLY B 75 ? 2.2320 1.2333 2.7180 -0.1047 -0.2921 0.1563 75 GLY B O 7716 N N . ASP B 76 ? 2.1939 1.2149 2.8051 -0.0744 -0.2980 0.1150 76 ASP B N 7717 C CA . ASP B 76 ? 2.1974 1.2081 2.8407 -0.0751 -0.2928 0.1020 76 ASP B CA 7718 C C . ASP B 76 ? 2.3559 1.3649 2.9478 -0.0862 -0.2640 0.0870 76 ASP B C 7719 O O . ASP B 76 ? 2.3355 1.3592 2.8923 -0.0863 -0.2414 0.0686 76 ASP B O 7720 C CB . ASP B 76 ? 2.1402 1.1275 2.7943 -0.0836 -0.3232 0.1392 76 ASP B CB 7721 C CG . ASP B 76 ? 2.3011 1.2806 3.0239 -0.0769 -0.3277 0.1239 76 ASP B CG 7722 O OD1 . ASP B 76 ? 2.2976 1.2839 3.0335 -0.0732 -0.3024 0.0886 76 ASP B OD1 7723 O OD2 . ASP B 76 ? 2.3125 1.2790 3.0763 -0.0762 -0.3574 0.1472 76 ASP B OD2 7724 N N . SER B 77 ? 2.2554 1.2462 2.8440 -0.0965 -0.2668 0.0969 77 SER B N 7725 C CA . SER B 77 ? 2.2479 1.2359 2.7972 -0.1081 -0.2427 0.0836 77 SER B CA 7726 C C . SER B 77 ? 2.2362 1.2455 2.7981 -0.0989 -0.2151 0.0378 77 SER B C 7727 O O . SER B 77 ? 2.2040 1.2248 2.8265 -0.0840 -0.2131 0.0095 77 SER B O 7728 C CB . SER B 77 ? 2.2297 1.2127 2.6980 -0.1257 -0.2379 0.1112 77 SER B CB 7729 O OG . SER B 77 ? 1.8884 0.8724 2.3233 -0.1364 -0.2143 0.0965 77 SER B OG 7730 N N . SER B 78 ? 2.0699 1.0855 2.5750 -0.1090 -0.1938 0.0306 78 SER B N 7731 C CA . SER B 78 ? 1.9511 0.9895 2.4476 -0.1028 -0.1704 -0.0034 78 SER B CA 7732 C C . SER B 78 ? 1.8217 0.8616 2.2459 -0.1172 -0.1568 0.0071 78 SER B C 7733 O O . SER B 78 ? 1.9476 0.9726 2.3387 -0.1318 -0.1601 0.0306 78 SER B O 7734 C CB . SER B 78 ? 1.9321 0.9803 2.4689 -0.0973 -0.1536 -0.0458 78 SER B CB 7735 O OG . SER B 78 ? 2.0827 1.1194 2.5992 -0.1109 -0.1470 -0.0461 78 SER B OG 7736 N N . GLN B 79 ? 1.7506 0.8090 2.1531 -0.1137 -0.1413 -0.0103 79 GLN B N 7737 C CA . GLN B 79 ? 1.9763 1.0396 2.3199 -0.1263 -0.1251 -0.0090 79 GLN B CA 7738 C C . GLN B 79 ? 2.0337 1.0823 2.3263 -0.1406 -0.1348 0.0318 79 GLN B C 7739 O O . GLN B 79 ? 2.0981 1.1363 2.3729 -0.1538 -0.1326 0.0423 79 GLN B O 7740 C CB . GLN B 79 ? 2.0730 1.1400 2.4200 -0.1330 -0.1086 -0.0358 79 GLN B CB 7741 C CG . GLN B 79 ? 2.1016 1.1891 2.4830 -0.1224 -0.0929 -0.0803 79 GLN B CG 7742 C CD . GLN B 79 ? 2.1578 1.2473 2.5507 -0.1290 -0.0810 -0.1069 79 GLN B CD 7743 O OE1 . GLN B 79 ? 1.8894 0.9616 2.2895 -0.1363 -0.0893 -0.0945 79 GLN B OE1 7744 N NE2 . GLN B 79 ? 2.2195 1.3308 2.6129 -0.1277 -0.0615 -0.1437 79 GLN B NE2 7745 N N . VAL B 80 ? 1.9826 1.0318 2.2534 -0.1387 -0.1451 0.0536 80 VAL B N 7746 C CA . VAL B 80 ? 1.8151 0.8519 2.0397 -0.1520 -0.1565 0.0930 80 VAL B CA 7747 C C . VAL B 80 ? 1.7735 0.8084 1.9480 -0.1696 -0.1422 0.1016 80 VAL B C 7748 O O . VAL B 80 ? 1.6601 0.6827 1.8099 -0.1830 -0.1496 0.1301 80 VAL B O 7749 C CB . VAL B 80 ? 1.5092 0.5528 1.7083 -0.1482 -0.1636 0.1062 80 VAL B CB 7750 C CG1 . VAL B 80 ? 1.4420 0.4744 1.5922 -0.1628 -0.1759 0.1452 80 VAL B CG1 7751 C CG2 . VAL B 80 ? 1.5255 0.5731 1.7781 -0.1313 -0.1784 0.0984 80 VAL B CG2 7752 N N . THR B 81 ? 1.6500 0.6983 1.8119 -0.1702 -0.1223 0.0770 81 THR B N 7753 C CA . THR B 81 ? 1.8235 0.8732 1.9483 -0.1859 -0.1080 0.0795 81 THR B CA 7754 C C . THR B 81 ? 1.6558 0.6993 1.7276 -0.2014 -0.1108 0.1145 81 THR B C 7755 O O . THR B 81 ? 1.5429 0.5756 1.6088 -0.2137 -0.1143 0.1332 81 THR B O 7756 C CB . THR B 81 ? 1.6578 0.7013 1.8120 -0.1914 -0.1038 0.0665 81 THR B CB 7757 O OG1 . THR B 81 ? 1.7424 0.7887 1.8624 -0.2075 -0.0916 0.0716 81 THR B OG1 7758 C CG2 . THR B 81 ? 1.6907 0.7156 1.8720 -0.1928 -0.1207 0.0852 81 THR B CG2 7759 N N . GLN B 82 ? 1.5739 0.6250 1.6061 -0.2014 -0.1084 0.1220 82 GLN B N 7760 C CA . GLN B 82 ? 1.7412 0.7901 1.7178 -0.2166 -0.1072 0.1503 82 GLN B CA 7761 C C . GLN B 82 ? 1.5579 0.6158 1.4968 -0.2288 -0.0865 0.1441 82 GLN B C 7762 O O . GLN B 82 ? 1.3985 0.4608 1.2896 -0.2408 -0.0791 0.1612 82 GLN B O 7763 C CB . GLN B 82 ? 1.6466 0.6986 1.5964 -0.2117 -0.1149 0.1610 82 GLN B CB 7764 C CG . GLN B 82 ? 1.7062 0.7734 1.6558 -0.1989 -0.1050 0.1362 82 GLN B CG 7765 C CD . GLN B 82 ? 1.8341 0.9012 1.7702 -0.1926 -0.1167 0.1460 82 GLN B CD 7766 O OE1 . GLN B 82 ? 1.8668 0.9246 1.7888 -0.1986 -0.1320 0.1715 82 GLN B OE1 7767 N NE2 . GLN B 82 ? 1.8682 0.9604 1.8099 -0.1785 -0.1059 0.1234 82 GLN B NE2 7768 N N . VAL B 83 ? 1.4087 0.4850 1.3721 -0.2221 -0.0728 0.1157 83 VAL B N 7769 C CA . VAL B 83 ? 1.3472 0.4478 1.2873 -0.2293 -0.0513 0.1064 83 VAL B CA 7770 C C . VAL B 83 ? 1.3574 0.4532 1.3340 -0.2339 -0.0500 0.0927 83 VAL B C 7771 O O . VAL B 83 ? 1.3566 0.4408 1.3774 -0.2256 -0.0594 0.0778 83 VAL B O 7772 C CB . VAL B 83 ? 1.4015 0.5371 1.3269 -0.2170 -0.0349 0.0836 83 VAL B CB 7773 C CG1 . VAL B 83 ? 1.2902 0.4508 1.1958 -0.2241 -0.0155 0.0760 83 VAL B CG1 7774 C CG2 . VAL B 83 ? 1.4759 0.6146 1.3694 -0.2122 -0.0371 0.0955 83 VAL B CG2 7775 N N . SER B 84 ? 1.3894 0.4952 1.3502 -0.2472 -0.0375 0.0956 84 SER B N 7776 C CA . SER B 84 ? 1.4262 0.5271 1.4189 -0.2544 -0.0367 0.0845 84 SER B CA 7777 C C . SER B 84 ? 1.3575 0.4777 1.3285 -0.2683 -0.0204 0.0874 84 SER B C 7778 O O . SER B 84 ? 1.3689 0.4892 1.3060 -0.2795 -0.0150 0.1095 84 SER B O 7779 C CB . SER B 84 ? 1.4095 0.4709 1.4302 -0.2628 -0.0561 0.1030 84 SER B CB 7780 O OG . SER B 84 ? 1.4137 0.4691 1.4632 -0.2722 -0.0547 0.0940 84 SER B OG 7781 N N . PRO B 85 ? 1.4083 0.5458 1.4001 -0.2685 -0.0125 0.0641 85 PRO B N 7782 C CA . PRO B 85 ? 1.3957 0.5353 1.4237 -0.2578 -0.0162 0.0344 85 PRO B CA 7783 C C . PRO B 85 ? 1.5639 0.7255 1.5832 -0.2408 -0.0111 0.0151 85 PRO B C 7784 O O . PRO B 85 ? 1.5772 0.7528 1.5633 -0.2366 -0.0051 0.0248 85 PRO B O 7785 C CB . PRO B 85 ? 1.3278 0.4851 1.3658 -0.2676 -0.0071 0.0193 85 PRO B CB 7786 C CG . PRO B 85 ? 1.3178 0.4960 1.3214 -0.2760 0.0055 0.0346 85 PRO B CG 7787 C CD . PRO B 85 ? 1.3721 0.5293 1.3530 -0.2816 0.0011 0.0654 85 PRO B CD 7788 N N . GLN B 86 ? 1.3911 0.5556 1.4403 -0.2325 -0.0124 -0.0129 86 GLN B N 7789 C CA . GLN B 86 ? 1.3040 0.4876 1.3487 -0.2180 -0.0075 -0.0319 86 GLN B CA 7790 C C . GLN B 86 ? 1.3780 0.5944 1.4130 -0.2187 0.0052 -0.0565 86 GLN B C 7791 O O . GLN B 86 ? 1.6863 0.9272 1.6914 -0.2147 0.0135 -0.0560 86 GLN B O 7792 C CB . GLN B 86 ? 1.2866 0.4512 1.3720 -0.2078 -0.0172 -0.0467 86 GLN B CB 7793 C CG . GLN B 86 ? 1.3845 0.5182 1.4802 -0.2051 -0.0333 -0.0208 86 GLN B CG 7794 C CD . GLN B 86 ? 1.3472 0.4490 1.4647 -0.2171 -0.0456 -0.0035 86 GLN B CD 7795 O OE1 . GLN B 86 ? 1.3510 0.4467 1.4984 -0.2221 -0.0452 -0.0202 86 GLN B OE1 7796 N NE2 . GLN B 86 ? 1.3727 0.4534 1.4738 -0.2232 -0.0569 0.0303 86 GLN B NE2 7797 N N . ARG B 87 ? 1.2642 0.4801 1.3248 -0.2244 0.0053 -0.0781 87 ARG B N 7798 C CA . ARG B 87 ? 1.2629 0.5092 1.3122 -0.2283 0.0147 -0.1000 87 ARG B CA 7799 C C . ARG B 87 ? 1.3588 0.6080 1.4123 -0.2434 0.0148 -0.0973 87 ARG B C 7800 O O . ARG B 87 ? 1.3981 0.6254 1.4811 -0.2506 0.0084 -0.1005 87 ARG B O 7801 C CB . ARG B 87 ? 1.3541 0.6047 1.4255 -0.2233 0.0168 -0.1345 87 ARG B CB 7802 C CG . ARG B 87 ? 1.6343 0.9151 1.6907 -0.2303 0.0246 -0.1576 87 ARG B CG 7803 C CD . ARG B 87 ? 1.6086 0.8972 1.6774 -0.2261 0.0300 -0.1921 87 ARG B CD 7804 N NE . ARG B 87 ? 1.8218 1.1232 1.8732 -0.2145 0.0355 -0.1915 87 ARG B NE 7805 C CZ . ARG B 87 ? 1.8616 1.1473 1.9339 -0.2028 0.0335 -0.1914 87 ARG B CZ 7806 N NH1 . ARG B 87 ? 1.7271 0.9825 1.8394 -0.2004 0.0251 -0.1910 87 ARG B NH1 7807 N NH2 . ARG B 87 ? 1.7360 1.0360 1.7918 -0.1937 0.0388 -0.1910 87 ARG B NH2 7808 N N . ILE B 88 ? 1.3991 0.6751 1.4266 -0.2482 0.0214 -0.0909 88 ILE B N 7809 C CA . ILE B 88 ? 1.5293 0.8149 1.5637 -0.2624 0.0218 -0.0919 88 ILE B CA 7810 C C . ILE B 88 ? 1.4300 0.7498 1.4502 -0.2644 0.0258 -0.1099 88 ILE B C 7811 O O . ILE B 88 ? 1.2448 0.5826 1.2422 -0.2557 0.0297 -0.1124 88 ILE B O 7812 C CB . ILE B 88 ? 1.3402 0.6250 1.3634 -0.2699 0.0247 -0.0624 88 ILE B CB 7813 C CG1 . ILE B 88 ? 1.3724 0.6903 1.3699 -0.2682 0.0327 -0.0566 88 ILE B CG1 7814 C CG2 . ILE B 88 ? 1.3705 0.6280 1.3883 -0.2657 0.0217 -0.0393 88 ILE B CG2 7815 C CD1 . ILE B 88 ? 1.4939 0.8153 1.4853 -0.2768 0.0387 -0.0331 88 ILE B CD1 7816 N N . ALA B 89 ? 1.3595 0.6876 1.3932 -0.2771 0.0233 -0.1214 89 ALA B N 7817 C CA . ALA B 89 ? 1.2699 0.6295 1.2907 -0.2819 0.0235 -0.1375 89 ALA B CA 7818 C C . ALA B 89 ? 1.3120 0.6938 1.3272 -0.2895 0.0240 -0.1205 89 ALA B C 7819 O O . ALA B 89 ? 1.3849 0.7632 1.4197 -0.3013 0.0215 -0.1162 89 ALA B O 7820 C CB . ALA B 89 ? 1.3582 0.7146 1.3975 -0.2917 0.0192 -0.1669 89 ALA B CB 7821 N N . LEU B 90 ? 1.4167 0.8214 1.4087 -0.2827 0.0272 -0.1111 90 LEU B N 7822 C CA . LEU B 90 ? 1.3793 0.8079 1.3710 -0.2878 0.0278 -0.0966 90 LEU B CA 7823 C C . LEU B 90 ? 1.4029 0.8588 1.3931 -0.2962 0.0199 -0.1117 90 LEU B C 7824 O O . LEU B 90 ? 1.4262 0.8939 1.3965 -0.2925 0.0175 -0.1235 90 LEU B O 7825 C CB . LEU B 90 ? 1.4058 0.8433 1.3775 -0.2760 0.0345 -0.0782 90 LEU B CB 7826 C CG . LEU B 90 ? 1.3785 0.8402 1.3556 -0.2791 0.0372 -0.0633 90 LEU B CG 7827 C CD1 . LEU B 90 ? 1.3249 0.7767 1.3223 -0.2884 0.0425 -0.0508 90 LEU B CD1 7828 C CD2 . LEU B 90 ? 1.3753 0.8456 1.3328 -0.2664 0.0434 -0.0506 90 LEU B CD2 7829 N N . ARG B 91 ? 1.3772 0.8435 1.3880 -0.3090 0.0153 -0.1106 91 ARG B N 7830 C CA . ARG B 91 ? 1.3668 0.8594 1.3780 -0.3194 0.0048 -0.1230 91 ARG B CA 7831 C C . ARG B 91 ? 1.5157 1.0334 1.5423 -0.3236 0.0026 -0.1057 91 ARG B C 7832 O O . ARG B 91 ? 1.6112 1.1250 1.6632 -0.3309 0.0055 -0.0973 91 ARG B O 7833 C CB . ARG B 91 ? 1.3348 0.8163 1.3623 -0.3333 -0.0016 -0.1450 91 ARG B CB 7834 C CG . ARG B 91 ? 1.4962 1.0027 1.5192 -0.3466 -0.0140 -0.1612 91 ARG B CG 7835 C CD . ARG B 91 ? 1.6723 1.1641 1.7110 -0.3604 -0.0187 -0.1861 91 ARG B CD 7836 N NE . ARG B 91 ? 1.8485 1.3645 1.8841 -0.3765 -0.0321 -0.2004 91 ARG B NE 7837 C CZ . ARG B 91 ? 2.0279 1.5367 2.0767 -0.3918 -0.0383 -0.2234 91 ARG B CZ 7838 N NH1 . ARG B 91 ? 2.0093 1.4863 2.0788 -0.3919 -0.0321 -0.2344 91 ARG B NH1 7839 N NH2 . ARG B 91 ? 2.1170 1.6496 2.1591 -0.4077 -0.0520 -0.2352 91 ARG B NH2 7840 N N . LEU B 92 ? 1.5117 1.0553 1.5256 -0.3193 -0.0025 -0.0999 92 LEU B N 7841 C CA . LEU B 92 ? 1.4398 1.0077 1.4735 -0.3197 -0.0037 -0.0826 92 LEU B CA 7842 C C . LEU B 92 ? 1.6026 1.2009 1.6431 -0.3295 -0.0209 -0.0866 92 LEU B C 7843 O O . LEU B 92 ? 1.5071 1.1149 1.5225 -0.3296 -0.0306 -0.0940 92 LEU B O 7844 C CB . LEU B 92 ? 1.3143 0.8850 1.3354 -0.3038 0.0055 -0.0662 92 LEU B CB 7845 C CG . LEU B 92 ? 1.3774 0.9224 1.3950 -0.2959 0.0218 -0.0568 92 LEU B CG 7846 C CD1 . LEU B 92 ? 1.2898 0.8379 1.2914 -0.2811 0.0298 -0.0439 92 LEU B CD1 7847 C CD2 . LEU B 92 ? 1.3922 0.9356 1.4390 -0.3051 0.0290 -0.0481 92 LEU B CD2 7848 N N . ARG B 93 ? 1.6284 1.2425 1.7033 -0.3391 -0.0251 -0.0809 93 ARG B N 7849 C CA . ARG B 93 ? 1.5537 1.1996 1.6428 -0.3479 -0.0432 -0.0797 93 ARG B CA 7850 C C . ARG B 93 ? 1.7156 1.3822 1.8141 -0.3356 -0.0426 -0.0603 93 ARG B C 7851 O O . ARG B 93 ? 1.6549 1.3115 1.7546 -0.3231 -0.0257 -0.0497 93 ARG B O 7852 C CB . ARG B 93 ? 1.6430 1.2977 1.7706 -0.3636 -0.0484 -0.0825 93 ARG B CB 7853 C CG . ARG B 93 ? 1.8037 1.4631 1.9679 -0.3608 -0.0341 -0.0666 93 ARG B CG 7854 C CD . ARG B 93 ? 1.8656 1.5408 2.0710 -0.3778 -0.0419 -0.0687 93 ARG B CD 7855 N NE . ARG B 93 ? 1.7855 1.4943 2.0067 -0.3838 -0.0636 -0.0676 93 ARG B NE 7856 C CZ . ARG B 93 ? 1.8043 1.5324 2.0607 -0.3996 -0.0765 -0.0707 93 ARG B CZ 7857 N NH1 . ARG B 93 ? 1.7501 1.4666 2.0294 -0.4112 -0.0684 -0.0756 93 ARG B NH1 7858 N NH2 . ARG B 93 ? 1.8651 1.6238 2.1347 -0.4046 -0.0990 -0.0676 93 ARG B NH2 7859 N N . PRO B 94 ? 1.7909 1.4853 1.8962 -0.3396 -0.0618 -0.0556 94 PRO B N 7860 C CA . PRO B 94 ? 1.6469 1.3593 1.7627 -0.3269 -0.0638 -0.0379 94 PRO B CA 7861 C C . PRO B 94 ? 1.4928 1.2104 1.6477 -0.3182 -0.0468 -0.0253 94 PRO B C 7862 O O . PRO B 94 ? 1.4824 1.2095 1.6745 -0.3270 -0.0442 -0.0254 94 PRO B O 7863 C CB . PRO B 94 ? 1.8065 1.5487 1.9363 -0.3378 -0.0911 -0.0345 94 PRO B CB 7864 C CG . PRO B 94 ? 1.9161 1.6580 2.0498 -0.3569 -0.1003 -0.0504 94 PRO B CG 7865 C CD . PRO B 94 ? 1.8705 1.5800 1.9719 -0.3566 -0.0845 -0.0665 94 PRO B CD 7866 N N . ASP B 95 ? 1.4187 1.1303 1.5640 -0.3021 -0.0345 -0.0159 95 ASP B N 7867 C CA . ASP B 95 ? 1.4378 1.1553 1.6150 -0.2930 -0.0164 -0.0056 95 ASP B CA 7868 C C . ASP B 95 ? 1.4782 1.1796 1.6637 -0.2988 0.0043 -0.0091 95 ASP B C 7869 O O . ASP B 95 ? 1.4211 1.1335 1.6407 -0.2984 0.0185 -0.0031 95 ASP B O 7870 C CB . ASP B 95 ? 1.5622 1.3142 1.7912 -0.2943 -0.0281 0.0029 95 ASP B CB 7871 C CG . ASP B 95 ? 1.7566 1.5228 1.9832 -0.2851 -0.0456 0.0124 95 ASP B CG 7872 O OD1 . ASP B 95 ? 1.6401 1.3918 1.8381 -0.2724 -0.0378 0.0159 95 ASP B OD1 7873 O OD2 . ASP B 95 ? 1.8670 1.6584 2.1209 -0.2913 -0.0685 0.0175 95 ASP B OD2 7874 N N . ASP B 96 ? 1.6184 1.2937 1.7738 -0.3048 0.0063 -0.0186 96 ASP B N 7875 C CA . ASP B 96 ? 1.5061 1.1626 1.6673 -0.3123 0.0225 -0.0197 96 ASP B CA 7876 C C . ASP B 96 ? 1.5891 1.2167 1.7174 -0.3025 0.0395 -0.0161 96 ASP B C 7877 O O . ASP B 96 ? 1.5950 1.2176 1.6972 -0.2897 0.0391 -0.0144 96 ASP B O 7878 C CB . ASP B 96 ? 1.4945 1.1397 1.6534 -0.3271 0.0117 -0.0324 96 ASP B CB 7879 C CG . ASP B 96 ? 1.6089 1.2441 1.7909 -0.3394 0.0234 -0.0308 96 ASP B CG 7880 O OD1 . ASP B 96 ? 1.5923 1.2214 1.7786 -0.3363 0.0426 -0.0202 96 ASP B OD1 7881 O OD2 . ASP B 96 ? 1.7417 1.3744 1.9362 -0.3535 0.0136 -0.0402 96 ASP B OD2 7882 N N . SER B 97 ? 1.6980 1.3063 1.8278 -0.3098 0.0530 -0.0138 97 SER B N 7883 C CA . SER B 97 ? 1.5102 1.0893 1.6090 -0.3034 0.0664 -0.0089 97 SER B CA 7884 C C . SER B 97 ? 1.6187 1.1710 1.7158 -0.3155 0.0702 -0.0091 97 SER B C 7885 O O . SER B 97 ? 1.6214 1.1804 1.7465 -0.3295 0.0713 -0.0086 97 SER B O 7886 C CB . SER B 97 ? 1.4956 1.0823 1.5978 -0.2969 0.0850 0.0022 97 SER B CB 7887 O OG . SER B 97 ? 1.6937 1.2940 1.8287 -0.3088 0.0966 0.0068 97 SER B OG 7888 N N . LYS B 98 ? 1.5315 1.0535 1.5985 -0.3104 0.0712 -0.0092 98 LYS B N 7889 C CA . LYS B 98 ? 1.4683 0.9605 1.5331 -0.3202 0.0748 -0.0051 98 LYS B CA 7890 C C . LYS B 98 ? 1.3585 0.8269 1.3929 -0.3125 0.0842 0.0059 98 LYS B C 7891 O O . LYS B 98 ? 1.3502 0.8222 1.3639 -0.2987 0.0855 0.0060 98 LYS B O 7892 C CB . LYS B 98 ? 1.5513 1.0266 1.6182 -0.3244 0.0600 -0.0197 98 LYS B CB 7893 C CG . LYS B 98 ? 1.4997 0.9829 1.5989 -0.3410 0.0539 -0.0259 98 LYS B CG 7894 C CD . LYS B 98 ? 1.6153 1.0889 1.7303 -0.3546 0.0653 -0.0111 98 LYS B CD 7895 C CE . LYS B 98 ? 1.7486 1.2348 1.8997 -0.3716 0.0598 -0.0167 98 LYS B CE 7896 N NZ . LYS B 98 ? 1.6832 1.2100 1.8551 -0.3712 0.0566 -0.0211 98 LYS B NZ 7897 N N . ASN B 99 ? 1.5906 1.0340 1.6221 -0.3226 0.0894 0.0164 99 ASN B N 7898 C CA . ASN B 99 ? 1.6556 1.0761 1.6573 -0.3184 0.0967 0.0294 99 ASN B CA 7899 C C . ASN B 99 ? 1.4915 0.8745 1.4863 -0.3225 0.0874 0.0332 99 ASN B C 7900 O O . ASN B 99 ? 1.6412 1.0129 1.6569 -0.3349 0.0820 0.0324 99 ASN B O 7901 C CB . ASN B 99 ? 1.8460 1.2744 1.8456 -0.3284 0.1153 0.0439 99 ASN B CB 7902 C CG . ASN B 99 ? 2.0229 1.4519 2.0482 -0.3481 0.1192 0.0491 99 ASN B CG 7903 O OD1 . ASN B 99 ? 1.9110 1.3529 1.9658 -0.3529 0.1110 0.0389 99 ASN B OD1 7904 N ND2 . ASN B 99 ? 2.5029 1.9179 2.5154 -0.3614 0.1316 0.0654 99 ASN B ND2 7905 N N . PHE B 100 ? 1.2617 0.6255 1.2305 -0.3119 0.0846 0.0375 100 PHE B N 7906 C CA . PHE B 100 ? 1.2588 0.5864 1.2242 -0.3135 0.0740 0.0426 100 PHE B CA 7907 C C . PHE B 100 ? 1.2889 0.5970 1.2237 -0.3130 0.0782 0.0619 100 PHE B C 7908 O O . PHE B 100 ? 1.2845 0.6075 1.1996 -0.3123 0.0911 0.0689 100 PHE B O 7909 C CB . PHE B 100 ? 1.2498 0.5719 1.2210 -0.3003 0.0612 0.0238 100 PHE B CB 7910 C CG . PHE B 100 ? 1.2728 0.6127 1.2246 -0.2842 0.0634 0.0161 100 PHE B CG 7911 C CD1 . PHE B 100 ? 1.3708 0.7421 1.3280 -0.2803 0.0650 0.0032 100 PHE B CD1 7912 C CD2 . PHE B 100 ? 1.3988 0.7238 1.3281 -0.2740 0.0621 0.0231 100 PHE B CD2 7913 C CE1 . PHE B 100 ? 1.2800 0.6660 1.2197 -0.2667 0.0660 -0.0018 100 PHE B CE1 7914 C CE2 . PHE B 100 ? 1.4096 0.7504 1.3224 -0.2602 0.0641 0.0165 100 PHE B CE2 7915 C CZ . PHE B 100 ? 1.3341 0.7048 1.2518 -0.2567 0.0664 0.0044 100 PHE B CZ 7916 N N . SER B 101 ? 1.5153 0.7900 1.4478 -0.3141 0.0663 0.0700 101 SER B N 7917 C CA . SER B 101 ? 1.3214 0.5748 1.2241 -0.3159 0.0661 0.0904 101 SER B CA 7918 C C . SER B 101 ? 1.3494 0.5832 1.2483 -0.3011 0.0516 0.0868 101 SER B C 7919 O O . SER B 101 ? 1.5479 0.7779 1.4715 -0.2927 0.0416 0.0701 101 SER B O 7920 C CB . SER B 101 ? 1.3886 0.6170 1.2916 -0.3363 0.0643 0.1119 101 SER B CB 7921 O OG . SER B 101 ? 1.7981 1.0462 1.7059 -0.3515 0.0799 0.1154 101 SER B OG 7922 N N . ILE B 102 ? 1.3793 0.6022 1.2480 -0.2987 0.0511 0.1014 102 ILE B N 7923 C CA . ILE B 102 ? 1.3160 0.5183 1.1833 -0.2866 0.0359 0.1019 102 ILE B CA 7924 C C . ILE B 102 ? 1.3484 0.5251 1.1876 -0.2959 0.0296 0.1285 102 ILE B C 7925 O O . ILE B 102 ? 1.5317 0.7162 1.3381 -0.3048 0.0419 0.1404 102 ILE B O 7926 C CB . ILE B 102 ? 1.2818 0.5055 1.1405 -0.2682 0.0394 0.0852 102 ILE B CB 7927 C CG1 . ILE B 102 ? 1.3335 0.5374 1.1930 -0.2566 0.0247 0.0864 102 ILE B CG1 7928 C CG2 . ILE B 102 ? 1.2956 0.5400 1.1226 -0.2691 0.0551 0.0904 102 ILE B CG2 7929 C CD1 . ILE B 102 ? 1.4566 0.6803 1.3093 -0.2399 0.0279 0.0705 102 ILE B CD1 7930 N N . GLN B 103 ? 1.3700 0.5158 1.2233 -0.2947 0.0102 0.1376 103 GLN B N 7931 C CA . GLN B 103 ? 1.4119 0.5311 1.2392 -0.3040 -0.0010 0.1650 103 GLN B CA 7932 C C . GLN B 103 ? 1.4476 0.5564 1.2770 -0.2877 -0.0163 0.1631 103 GLN B C 7933 O O . GLN B 103 ? 1.5311 0.6369 1.3973 -0.2736 -0.0258 0.1464 103 GLN B O 7934 C CB . GLN B 103 ? 1.6432 0.7307 1.4870 -0.3206 -0.0144 0.1849 103 GLN B CB 7935 C CG . GLN B 103 ? 1.7821 0.8777 1.6237 -0.3401 0.0002 0.1904 103 GLN B CG 7936 C CD . GLN B 103 ? 1.8498 0.9559 1.7352 -0.3362 0.0029 0.1681 103 GLN B CD 7937 O OE1 . GLN B 103 ? 1.6496 0.7831 1.5458 -0.3222 0.0119 0.1426 103 GLN B OE1 7938 N NE2 . GLN B 103 ? 2.0332 1.1166 1.9430 -0.3500 -0.0059 0.1783 103 GLN B NE2 7939 N N . VAL B 104 ? 1.5786 0.6831 1.3694 -0.2906 -0.0180 0.1788 104 VAL B N 7940 C CA . VAL B 104 ? 1.6048 0.7000 1.3964 -0.2769 -0.0335 0.1794 104 VAL B CA 7941 C C . VAL B 104 ? 1.4772 0.5453 1.2444 -0.2894 -0.0512 0.2103 104 VAL B C 7942 O O . VAL B 104 ? 1.4764 0.5455 1.2090 -0.3070 -0.0438 0.2281 104 VAL B O 7943 C CB . VAL B 104 ? 1.4348 0.5579 1.2040 -0.2644 -0.0199 0.1640 104 VAL B CB 7944 C CG1 . VAL B 104 ? 1.5055 0.6558 1.3015 -0.2506 -0.0074 0.1348 104 VAL B CG1 7945 C CG2 . VAL B 104 ? 1.5329 0.6668 1.2548 -0.2779 -0.0031 0.1742 104 VAL B CG2 7946 N N . ARG B 105 ? 1.4533 0.5121 1.2451 -0.2765 -0.0722 0.2134 105 ARG B N 7947 C CA . ARG B 105 ? 1.7641 0.8117 1.5442 -0.2826 -0.0909 0.2402 105 ARG B CA 7948 C C . ARG B 105 ? 1.7170 0.7628 1.4981 -0.2691 -0.1066 0.2402 105 ARG B C 7949 O O . ARG B 105 ? 1.6959 0.7436 1.5156 -0.2511 -0.1114 0.2212 105 ARG B O 7950 C CB . ARG B 105 ? 1.5160 0.5495 1.3384 -0.2838 -0.1062 0.2504 105 ARG B CB 7951 C CG . ARG B 105 ? 1.5619 0.5823 1.3705 -0.2927 -0.1272 0.2806 105 ARG B CG 7952 C CD . ARG B 105 ? 1.7674 0.7721 1.6294 -0.2862 -0.1469 0.2860 105 ARG B CD 7953 N NE . ARG B 105 ? 1.6992 0.7007 1.5835 -0.2936 -0.1368 0.2812 105 ARG B NE 7954 C CZ . ARG B 105 ? 1.6836 0.6764 1.5535 -0.3121 -0.1384 0.3034 105 ARG B CZ 7955 N NH1 . ARG B 105 ? 1.6284 0.6187 1.5221 -0.3181 -0.1288 0.2968 105 ARG B NH1 7956 N NH2 . ARG B 105 ? 1.8840 0.8709 1.7145 -0.3258 -0.1497 0.3318 105 ARG B NH2 7957 N N . GLN B 106 ? 1.5477 0.5906 1.2863 -0.2789 -0.1142 0.2608 106 GLN B N 7958 C CA . GLN B 106 ? 1.6115 0.6510 1.3527 -0.2688 -0.1336 0.2654 106 GLN B CA 7959 C C . GLN B 106 ? 1.5568 0.5820 1.3311 -0.2680 -0.1604 0.2843 106 GLN B C 7960 O O . GLN B 106 ? 1.5947 0.6114 1.3427 -0.2849 -0.1688 0.3090 106 GLN B O 7961 C CB . GLN B 106 ? 1.6684 0.7109 1.3462 -0.2810 -0.1301 0.2768 106 GLN B CB 7962 C CG . GLN B 106 ? 1.5772 0.6329 1.2255 -0.2789 -0.1050 0.2566 106 GLN B CG 7963 C CD . GLN B 106 ? 1.8626 0.9227 1.5314 -0.2595 -0.1099 0.2393 106 GLN B CD 7964 O OE1 . GLN B 106 ? 1.9339 0.9894 1.6476 -0.2461 -0.1295 0.2383 106 GLN B OE1 7965 N NE2 . GLN B 106 ? 1.7175 0.7941 1.3590 -0.2561 -0.0902 0.2234 106 GLN B NE2 7966 N N . VAL B 107 ? 1.5311 0.5538 1.3628 -0.2490 -0.1736 0.2722 107 VAL B N 7967 C CA . VAL B 107 ? 1.7700 0.7793 1.6456 -0.2467 -0.1943 0.2841 107 VAL B CA 7968 C C . VAL B 107 ? 1.8715 0.8730 1.7585 -0.2426 -0.2243 0.3022 107 VAL B C 7969 O O . VAL B 107 ? 1.9870 0.9930 1.9117 -0.2250 -0.2333 0.2887 107 VAL B O 7970 C CB . VAL B 107 ? 1.7413 0.7522 1.6813 -0.2294 -0.1891 0.2569 107 VAL B CB 7971 C CG1 . VAL B 107 ? 1.9931 0.9890 1.9789 -0.2278 -0.2081 0.2673 107 VAL B CG1 7972 C CG2 . VAL B 107 ? 1.5055 0.5247 1.4359 -0.2338 -0.1619 0.2378 107 VAL B CG2 7973 N N . GLU B 108 ? 1.9651 0.9559 1.8194 -0.2603 -0.2399 0.3328 108 GLU B N 7974 C CA . GLU B 108 ? 1.9434 0.9228 1.8157 -0.2602 -0.2738 0.3555 108 GLU B CA 7975 C C . GLU B 108 ? 2.1881 1.1739 2.0846 -0.2436 -0.2886 0.3470 108 GLU B C 7976 O O . GLU B 108 ? 2.3764 1.3710 2.2344 -0.2452 -0.2821 0.3431 108 GLU B O 7977 C CB . GLU B 108 ? 2.0798 1.0466 2.0095 -0.2552 -0.2873 0.3594 108 GLU B CB 7978 C CG . GLU B 108 ? 2.5344 1.4859 2.4638 -0.2661 -0.3210 0.3930 108 GLU B CG 7979 C CD . GLU B 108 ? 2.6908 1.6396 2.5423 -0.2921 -0.3231 0.4200 108 GLU B CD 7980 O OE1 . GLU B 108 ? 2.7853 1.7349 2.5975 -0.3081 -0.3015 0.4227 108 GLU B OE1 7981 O OE2 . GLU B 108 ? 2.6436 1.5904 2.4734 -0.2974 -0.3463 0.4374 108 GLU B OE2 7982 N N . ASP B 109 ? 1.9813 0.9630 1.9448 -0.2279 -0.3084 0.3435 109 ASP B N 7983 C CA . ASP B 109 ? 1.8575 0.8479 1.8603 -0.2094 -0.3198 0.3303 109 ASP B CA 7984 C C . ASP B 109 ? 1.7368 0.7404 1.7737 -0.1917 -0.2933 0.2928 109 ASP B C 7985 O O . ASP B 109 ? 1.7479 0.7499 1.8301 -0.1834 -0.2854 0.2766 109 ASP B O 7986 C CB . ASP B 109 ? 1.8743 0.8563 1.9377 -0.2012 -0.3531 0.3429 109 ASP B CB 7987 C CG . ASP B 109 ? 1.9917 0.9852 2.1079 -0.1808 -0.3637 0.3265 109 ASP B CG 7988 O OD1 . ASP B 109 ? 2.0283 1.0344 2.1237 -0.1760 -0.3500 0.3117 109 ASP B OD1 7989 O OD2 . ASP B 109 ? 1.9145 0.9051 2.0958 -0.1699 -0.3861 0.3285 109 ASP B OD2 7990 N N . TYR B 110 ? 1.6105 0.6267 1.6234 -0.1873 -0.2803 0.2788 110 TYR B N 7991 C CA . TYR B 110 ? 1.5792 0.6089 1.6168 -0.1728 -0.2558 0.2440 110 TYR B CA 7992 C C . TYR B 110 ? 1.6146 0.6552 1.6756 -0.1589 -0.2636 0.2330 110 TYR B C 7993 O O . TYR B 110 ? 1.8200 0.8600 1.8463 -0.1655 -0.2765 0.2498 110 TYR B O 7994 C CB . TYR B 110 ? 1.4790 0.5140 1.4592 -0.1835 -0.2276 0.2364 110 TYR B CB 7995 C CG . TYR B 110 ? 1.5550 0.6019 1.5573 -0.1723 -0.2027 0.2022 110 TYR B CG 7996 C CD1 . TYR B 110 ? 1.7763 0.8357 1.7696 -0.1644 -0.1918 0.1843 110 TYR B CD1 7997 C CD2 . TYR B 110 ? 1.5210 0.5659 1.5508 -0.1711 -0.1910 0.1880 110 TYR B CD2 7998 C CE1 . TYR B 110 ? 1.6810 0.7511 1.6911 -0.1562 -0.1705 0.1539 110 TYR B CE1 7999 C CE2 . TYR B 110 ? 1.3959 0.4518 1.4426 -0.1630 -0.1699 0.1566 110 TYR B CE2 8000 C CZ . TYR B 110 ? 1.5199 0.5886 1.5560 -0.1559 -0.1601 0.1400 110 TYR B CZ 8001 O OH . TYR B 110 ? 1.6390 0.7186 1.6893 -0.1497 -0.1407 0.1094 110 TYR B OH 8002 N N . PRO B 111 ? 1.5566 0.6079 1.6759 -0.1409 -0.2550 0.2036 111 PRO B N 8003 C CA . PRO B 111 ? 1.6763 0.7400 1.8264 -0.1274 -0.2616 0.1915 111 PRO B CA 8004 C C . PRO B 111 ? 1.7169 0.7876 1.8118 -0.1328 -0.2500 0.1899 111 PRO B C 8005 O O . PRO B 111 ? 1.5959 0.6692 1.6507 -0.1389 -0.2263 0.1797 111 PRO B O 8006 C CB . PRO B 111 ? 1.6841 0.7598 1.8967 -0.1108 -0.2451 0.1554 111 PRO B CB 8007 C CG . PRO B 111 ? 1.7062 0.7770 1.9013 -0.1176 -0.2246 0.1459 111 PRO B CG 8008 C CD . PRO B 111 ? 1.6850 0.7384 1.8445 -0.1335 -0.2383 0.1788 111 PRO B CD 8009 N N . VAL B 112 ? 1.7791 0.8523 1.8723 -0.1313 -0.2682 0.2007 112 VAL B N 8010 C CA . VAL B 112 ? 1.6874 0.7651 1.7274 -0.1374 -0.2602 0.2010 112 VAL B CA 8011 C C . VAL B 112 ? 1.5707 0.6607 1.6488 -0.1245 -0.2679 0.1887 112 VAL B C 8012 O O . VAL B 112 ? 1.5085 0.5976 1.6192 -0.1209 -0.2946 0.2020 112 VAL B O 8013 C CB . VAL B 112 ? 1.5420 0.6073 1.5159 -0.1566 -0.2752 0.2329 112 VAL B CB 8014 C CG1 . VAL B 112 ? 1.4299 0.4995 1.3560 -0.1616 -0.2703 0.2316 112 VAL B CG1 8015 C CG2 . VAL B 112 ? 1.5603 0.6166 1.4893 -0.1715 -0.2619 0.2427 112 VAL B CG2 8016 N N . ASP B 113 ? 1.4601 0.5621 1.5356 -0.1184 -0.2452 0.1638 113 ASP B N 8017 C CA . ASP B 113 ? 1.5221 0.6385 1.6259 -0.1085 -0.2489 0.1519 113 ASP B CA 8018 C C . ASP B 113 ? 1.4090 0.5382 1.4464 -0.1165 -0.2381 0.1549 113 ASP B C 8019 O O . ASP B 113 ? 1.3467 0.4878 1.3389 -0.1206 -0.2114 0.1443 113 ASP B O 8020 C CB . ASP B 113 ? 1.5447 0.6871 1.7033 -0.0924 -0.2253 0.1153 113 ASP B CB 8021 C CG . ASP B 113 ? 1.5437 0.6969 1.6759 -0.0941 -0.1939 0.0965 113 ASP B CG 8022 O OD1 . ASP B 113 ? 1.8698 1.0165 1.9392 -0.1063 -0.1862 0.1090 113 ASP B OD1 8023 O OD2 . ASP B 113 ? 1.3450 0.5144 1.5206 -0.0840 -0.1767 0.0681 113 ASP B OD2 8024 N N . ILE B 114 ? 1.4579 0.5842 1.4927 -0.1190 -0.2604 0.1693 114 ILE B N 8025 C CA . ILE B 114 ? 1.5139 0.6485 1.4874 -0.1279 -0.2540 0.1732 114 ILE B CA 8026 C C . ILE B 114 ? 1.3426 0.5008 1.3471 -0.1175 -0.2525 0.1574 114 ILE B C 8027 O O . ILE B 114 ? 1.3356 0.4921 1.3913 -0.1115 -0.2766 0.1626 114 ILE B O 8028 C CB . ILE B 114 ? 1.6218 0.7301 1.5467 -0.1458 -0.2817 0.2065 114 ILE B CB 8029 C CG1 . ILE B 114 ? 1.6462 0.7383 1.6228 -0.1437 -0.3206 0.2261 114 ILE B CG1 8030 C CG2 . ILE B 114 ? 1.5864 0.6763 1.4637 -0.1598 -0.2747 0.2201 114 ILE B CG2 8031 C CD1 . ILE B 114 ? 1.6891 0.7653 1.6216 -0.1613 -0.3454 0.2584 114 ILE B CD1 8032 N N . TYR B 115 ? 1.2788 0.4592 1.2551 -0.1158 -0.2244 0.1385 115 TYR B N 8033 C CA . TYR B 115 ? 1.2542 0.4589 1.2579 -0.1073 -0.2186 0.1221 115 TYR B CA 8034 C C . TYR B 115 ? 1.2631 0.4676 1.2149 -0.1173 -0.2235 0.1317 115 TYR B C 8035 O O . TYR B 115 ? 1.4062 0.6109 1.2995 -0.1252 -0.2059 0.1308 115 TYR B O 8036 C CB . TYR B 115 ? 1.2996 0.5307 1.3155 -0.0984 -0.1842 0.0929 115 TYR B CB 8037 C CG . TYR B 115 ? 1.3114 0.5690 1.3642 -0.0900 -0.1762 0.0746 115 TYR B CG 8038 C CD1 . TYR B 115 ? 1.4580 0.7262 1.5850 -0.0789 -0.1822 0.0622 115 TYR B CD1 8039 C CD2 . TYR B 115 ? 1.2045 0.4768 1.2207 -0.0937 -0.1617 0.0688 115 TYR B CD2 8040 C CE1 . TYR B 115 ? 1.4096 0.7042 1.5714 -0.0727 -0.1727 0.0446 115 TYR B CE1 8041 C CE2 . TYR B 115 ? 1.2155 0.5121 1.2649 -0.0878 -0.1539 0.0532 115 TYR B CE2 8042 C CZ . TYR B 115 ? 1.2746 0.5832 1.3958 -0.0779 -0.1587 0.0411 115 TYR B CZ 8043 O OH . TYR B 115 ? 1.3631 0.6979 1.5187 -0.0735 -0.1489 0.0249 115 TYR B OH 8044 N N . TYR B 116 ? 1.2753 0.4799 1.2521 -0.1169 -0.2477 0.1398 116 TYR B N 8045 C CA . TYR B 116 ? 1.3710 0.5736 1.3017 -0.1276 -0.2562 0.1489 116 TYR B CA 8046 C C . TYR B 116 ? 1.2792 0.5085 1.2143 -0.1217 -0.2337 0.1272 116 TYR B C 8047 O O . TYR B 116 ? 1.2940 0.5423 1.2867 -0.1115 -0.2339 0.1145 116 TYR B O 8048 C CB . TYR B 116 ? 1.4556 0.6453 1.4097 -0.1318 -0.2959 0.1695 116 TYR B CB 8049 C CG . TYR B 116 ? 1.4889 0.6624 1.3766 -0.1499 -0.3125 0.1885 116 TYR B CG 8050 C CD1 . TYR B 116 ? 1.4002 0.5462 1.2424 -0.1651 -0.3302 0.2130 116 TYR B CD1 8051 C CD2 . TYR B 116 ? 1.5936 0.7790 1.4627 -0.1534 -0.3101 0.1813 116 TYR B CD2 8052 C CE1 . TYR B 116 ? 1.4726 0.6044 1.2499 -0.1839 -0.3439 0.2284 116 TYR B CE1 8053 C CE2 . TYR B 116 ? 1.5695 0.7397 1.3768 -0.1710 -0.3245 0.1957 116 TYR B CE2 8054 C CZ . TYR B 116 ? 1.6133 0.7574 1.3735 -0.1865 -0.3409 0.2185 116 TYR B CZ 8055 O OH . TYR B 116 ? 1.7430 0.8728 1.4378 -0.2062 -0.3537 0.2310 116 TYR B OH 8056 N N . LEU B 117 ? 1.3862 0.6171 1.2626 -0.1290 -0.2141 0.1230 117 LEU B N 8057 C CA . LEU B 117 ? 1.4413 0.6943 1.3163 -0.1253 -0.1934 0.1052 117 LEU B CA 8058 C C . LEU B 117 ? 1.4169 0.6628 1.2505 -0.1365 -0.2043 0.1133 117 LEU B C 8059 O O . LEU B 117 ? 1.3382 0.5700 1.1123 -0.1473 -0.1999 0.1198 117 LEU B O 8060 C CB . LEU B 117 ? 1.4084 0.6705 1.2574 -0.1231 -0.1607 0.0914 117 LEU B CB 8061 C CG . LEU B 117 ? 1.4929 0.7793 1.3494 -0.1182 -0.1379 0.0730 117 LEU B CG 8062 C CD1 . LEU B 117 ? 1.3849 0.6915 1.3059 -0.1089 -0.1401 0.0615 117 LEU B CD1 8063 C CD2 . LEU B 117 ? 1.3916 0.6858 1.2289 -0.1159 -0.1103 0.0623 117 LEU B CD2 8064 N N . MET B 118 ? 1.3953 0.6520 1.2621 -0.1344 -0.2176 0.1112 118 MET B N 8065 C CA . MET B 118 ? 1.4986 0.7454 1.3331 -0.1463 -0.2364 0.1213 118 MET B CA 8066 C C . MET B 118 ? 1.5113 0.7752 1.3471 -0.1460 -0.2239 0.1075 118 MET B C 8067 O O . MET B 118 ? 1.2881 0.5745 1.1743 -0.1364 -0.2150 0.0946 118 MET B O 8068 C CB . MET B 118 ? 1.2906 0.5290 1.1602 -0.1483 -0.2740 0.1379 118 MET B CB 8069 C CG . MET B 118 ? 1.3274 0.5526 1.1590 -0.1635 -0.2985 0.1511 118 MET B CG 8070 S SD . MET B 118 ? 1.6165 0.8333 1.4952 -0.1659 -0.3467 0.1728 118 MET B SD 8071 C CE . MET B 118 ? 1.4531 0.6526 1.2633 -0.1883 -0.3698 0.1864 118 MET B CE 8072 N N . ASP B 119 ? 1.5120 0.7646 1.2916 -0.1578 -0.2229 0.1098 119 ASP B N 8073 C CA . ASP B 119 ? 1.3906 0.6536 1.1664 -0.1604 -0.2161 0.0996 119 ASP B CA 8074 C C . ASP B 119 ? 1.4463 0.7139 1.2594 -0.1628 -0.2448 0.1057 119 ASP B C 8075 O O . ASP B 119 ? 1.6144 0.8656 1.4134 -0.1720 -0.2738 0.1216 119 ASP B O 8076 C CB . ASP B 119 ? 1.4247 0.6708 1.1316 -0.1730 -0.2091 0.0997 119 ASP B CB 8077 C CG . ASP B 119 ? 1.6308 0.8851 1.3327 -0.1753 -0.1990 0.0877 119 ASP B CG 8078 O OD1 . ASP B 119 ? 2.0706 1.3431 1.8193 -0.1696 -0.2010 0.0820 119 ASP B OD1 8079 O OD2 . ASP B 119 ? 1.5081 0.7505 1.1607 -0.1836 -0.1886 0.0834 119 ASP B OD2 8080 N N . LEU B 120 ? 1.3373 0.6283 1.1998 -0.1553 -0.2376 0.0940 120 LEU B N 8081 C CA . LEU B 120 ? 1.4795 0.7787 1.3841 -0.1573 -0.2632 0.0980 120 LEU B CA 8082 C C . LEU B 120 ? 1.4585 0.7591 1.3430 -0.1672 -0.2649 0.0934 120 LEU B C 8083 O O . LEU B 120 ? 1.3421 0.6529 1.2650 -0.1692 -0.2840 0.0949 120 LEU B O 8084 C CB . LEU B 120 ? 1.4811 0.8069 1.4644 -0.1438 -0.2572 0.0881 120 LEU B CB 8085 C CG . LEU B 120 ? 1.5193 0.8402 1.5398 -0.1359 -0.2724 0.0964 120 LEU B CG 8086 C CD1 . LEU B 120 ? 1.6535 0.9995 1.7611 -0.1248 -0.2767 0.0876 120 LEU B CD1 8087 C CD2 . LEU B 120 ? 1.2808 0.5747 1.2718 -0.1462 -0.3079 0.1195 120 LEU B CD2 8088 N N . SER B 121 ? 1.3433 0.6347 1.1733 -0.1730 -0.2452 0.0870 121 SER B N 8089 C CA . SER B 121 ? 1.3789 0.6678 1.1878 -0.1831 -0.2471 0.0820 121 SER B CA 8090 C C . SER B 121 ? 1.6714 0.9423 1.4553 -0.1972 -0.2815 0.0947 121 SER B C 8091 O O . SER B 121 ? 1.6766 0.9319 1.4396 -0.2013 -0.2988 0.1083 121 SER B O 8092 C CB . SER B 121 ? 1.3226 0.6023 1.0803 -0.1859 -0.2200 0.0724 121 SER B CB 8093 O OG . SER B 121 ? 1.4333 0.6899 1.1333 -0.1935 -0.2219 0.0784 121 SER B OG 8094 N N . TYR B 122 ? 1.5502 0.8229 1.3354 -0.2061 -0.2922 0.0910 122 TYR B N 8095 C CA . TYR B 122 ? 1.4930 0.7554 1.2718 -0.2193 -0.3297 0.1029 122 TYR B CA 8096 C C . TYR B 122 ? 1.4646 0.6987 1.1743 -0.2338 -0.3452 0.1146 122 TYR B C 8097 O O . TYR B 122 ? 1.4652 0.6903 1.1726 -0.2434 -0.3800 0.1303 122 TYR B O 8098 C CB . TYR B 122 ? 1.4479 0.7147 1.2291 -0.2284 -0.3339 0.0939 122 TYR B CB 8099 C CG . TYR B 122 ? 1.6027 0.8755 1.4216 -0.2352 -0.3716 0.1039 122 TYR B CG 8100 C CD1 . TYR B 122 ? 1.6104 0.9106 1.5084 -0.2252 -0.3752 0.1015 122 TYR B CD1 8101 C CD2 . TYR B 122 ? 1.5495 0.8020 1.3258 -0.2526 -0.4038 0.1155 122 TYR B CD2 8102 C CE1 . TYR B 122 ? 1.4918 0.7995 1.4310 -0.2308 -0.4107 0.1107 122 TYR B CE1 8103 C CE2 . TYR B 122 ? 1.5358 0.7942 1.3484 -0.2594 -0.4415 0.1262 122 TYR B CE2 8104 C CZ . TYR B 122 ? 1.5217 0.8081 1.4186 -0.2476 -0.4452 0.1239 122 TYR B CZ 8105 O OH . TYR B 122 ? 1.6747 0.9688 1.6141 -0.2538 -0.4835 0.1345 122 TYR B OH 8106 N N . SER B 123 ? 1.4726 0.6937 1.1275 -0.2361 -0.3200 0.1075 123 SER B N 8107 C CA . SER B 123 ? 1.6111 0.8071 1.1965 -0.2517 -0.3289 0.1160 123 SER B CA 8108 C C . SER B 123 ? 2.0780 1.2675 1.6699 -0.2500 -0.3468 0.1358 123 SER B C 8109 O O . SER B 123 ? 2.2868 1.4560 1.8277 -0.2657 -0.3641 0.1491 123 SER B O 8110 C CB . SER B 123 ? 1.5864 0.7740 1.1229 -0.2523 -0.2936 0.1016 123 SER B CB 8111 O OG . SER B 123 ? 1.9333 1.0981 1.3993 -0.2704 -0.2990 0.1055 123 SER B OG 8112 N N . MET B 124 ? 1.8781 1.0845 1.5328 -0.2321 -0.3421 0.1373 124 MET B N 8113 C CA . MET B 124 ? 1.5993 0.8001 1.2714 -0.2278 -0.3568 0.1542 124 MET B CA 8114 C C . MET B 124 ? 1.6580 0.8632 1.3846 -0.2269 -0.3958 0.1699 124 MET B C 8115 O O . MET B 124 ? 1.9010 1.1020 1.6552 -0.2216 -0.4111 0.1843 124 MET B O 8116 C CB . MET B 124 ? 1.5931 0.8078 1.3004 -0.2090 -0.3269 0.1445 124 MET B CB 8117 C CG . MET B 124 ? 1.5896 0.8011 1.2500 -0.2086 -0.2902 0.1308 124 MET B CG 8118 S SD . MET B 124 ? 1.7857 0.9735 1.3842 -0.2184 -0.2865 0.1427 124 MET B SD 8119 C CE . MET B 124 ? 1.9150 1.0810 1.4371 -0.2436 -0.3017 0.1473 124 MET B CE 8120 N N . LYS B 125 ? 1.8654 1.0794 1.6122 -0.2317 -0.4122 0.1669 125 LYS B N 8121 C CA . LYS B 125 ? 1.7520 0.9725 1.5560 -0.2313 -0.4512 0.1812 125 LYS B CA 8122 C C . LYS B 125 ? 1.7570 0.9524 1.5255 -0.2465 -0.4888 0.2080 125 LYS B C 8123 O O . LYS B 125 ? 1.5787 0.7747 1.3981 -0.2411 -0.5172 0.2249 125 LYS B O 8124 C CB . LYS B 125 ? 1.7018 0.9342 1.5228 -0.2378 -0.4624 0.1733 125 LYS B CB 8125 C CG . LYS B 125 ? 1.7514 1.0000 1.6530 -0.2324 -0.4957 0.1827 125 LYS B CG 8126 C CD . LYS B 125 ? 1.5899 0.8524 1.5096 -0.2391 -0.5029 0.1728 125 LYS B CD 8127 C CE . LYS B 125 ? 1.4955 0.7788 1.5052 -0.2325 -0.5331 0.1799 125 LYS B CE 8128 N NZ . LYS B 125 ? 1.6175 0.8842 1.6266 -0.2424 -0.5820 0.2069 125 LYS B NZ 8129 N N . ASP B 126 ? 1.8786 1.0521 1.5602 -0.2662 -0.4884 0.2116 126 ASP B N 8130 C CA . ASP B 126 ? 1.6772 0.8251 1.3087 -0.2847 -0.5191 0.2371 126 ASP B CA 8131 C C . ASP B 126 ? 1.7976 0.9382 1.4415 -0.2754 -0.5134 0.2490 126 ASP B C 8132 O O . ASP B 126 ? 1.9719 1.0983 1.6221 -0.2818 -0.5472 0.2747 126 ASP B O 8133 C CB . ASP B 126 ? 1.6801 0.8088 1.2124 -0.3078 -0.5089 0.2322 126 ASP B CB 8134 C CG . ASP B 126 ? 1.7871 0.9180 1.2877 -0.3004 -0.4592 0.2101 126 ASP B CG 8135 O OD1 . ASP B 126 ? 1.8338 0.9845 1.3867 -0.2792 -0.4325 0.1939 126 ASP B OD1 8136 O OD2 . ASP B 126 ? 1.8231 0.9368 1.2475 -0.3166 -0.4469 0.2087 126 ASP B OD2 8137 N N . ASP B 127 ? 1.9475 1.0972 1.5961 -0.2607 -0.4715 0.2306 127 ASP B N 8138 C CA . ASP B 127 ? 1.8331 0.9757 1.4865 -0.2529 -0.4601 0.2379 127 ASP B CA 8139 C C . ASP B 127 ? 1.8326 0.9869 1.5770 -0.2338 -0.4747 0.2442 127 ASP B C 8140 O O . ASP B 127 ? 1.7534 0.8935 1.5085 -0.2344 -0.4931 0.2638 127 ASP B O 8141 C CB . ASP B 127 ? 1.6965 0.8468 1.3273 -0.2440 -0.4115 0.2150 127 ASP B CB 8142 C CG . ASP B 127 ? 1.8480 0.9879 1.3975 -0.2609 -0.3943 0.2055 127 ASP B CG 8143 O OD1 . ASP B 127 ? 2.0807 1.2266 1.6230 -0.2657 -0.3956 0.1944 127 ASP B OD1 8144 O OD2 . ASP B 127 ? 1.9358 1.0620 1.4311 -0.2696 -0.3787 0.2078 127 ASP B OD2 8145 N N . LEU B 128 ? 1.6984 0.8785 1.5094 -0.2178 -0.4657 0.2268 128 LEU B N 8146 C CA . LEU B 128 ? 1.5992 0.7947 1.5031 -0.1988 -0.4742 0.2266 128 LEU B CA 8147 C C . LEU B 128 ? 1.7971 0.9807 1.7347 -0.2045 -0.5246 0.2537 128 LEU B C 8148 O O . LEU B 128 ? 1.6818 0.8646 1.6791 -0.1928 -0.5374 0.2622 128 LEU B O 8149 C CB . LEU B 128 ? 1.4575 0.6845 1.4209 -0.1850 -0.4557 0.2027 128 LEU B CB 8150 C CG . LEU B 128 ? 1.5136 0.7617 1.5773 -0.1650 -0.4574 0.1957 128 LEU B CG 8151 C CD1 . LEU B 128 ? 1.6042 0.8506 1.6789 -0.1528 -0.4324 0.1887 128 LEU B CD1 8152 C CD2 . LEU B 128 ? 1.3754 0.6553 1.4887 -0.1562 -0.4387 0.1728 128 LEU B CD2 8153 N N . TRP B 129 ? 1.9037 1.0774 1.8036 -0.2230 -0.5542 0.2671 129 TRP B N 8154 C CA . TRP B 129 ? 1.9092 1.0714 1.8368 -0.2311 -0.6067 0.2954 129 TRP B CA 8155 C C . TRP B 129 ? 1.8559 0.9898 1.7563 -0.2394 -0.6270 0.3228 129 TRP B C 8156 O O . TRP B 129 ? 1.6434 0.7747 1.6111 -0.2292 -0.6517 0.3376 129 TRP B O 8157 C CB . TRP B 129 ? 1.7576 0.9133 1.6358 -0.2531 -0.6331 0.3038 129 TRP B CB 8158 C CG . TRP B 129 ? 1.8006 0.9423 1.6973 -0.2648 -0.6904 0.3360 129 TRP B CG 8159 C CD1 . TRP B 129 ? 2.0142 1.1267 1.8387 -0.2897 -0.7217 0.3643 129 TRP B CD1 8160 C CD2 . TRP B 129 ? 1.8689 1.0255 1.8649 -0.2529 -0.7243 0.3445 129 TRP B CD2 8161 N NE1 . TRP B 129 ? 2.1027 1.2097 1.9736 -0.2944 -0.7757 0.3920 129 TRP B NE1 8162 C CE2 . TRP B 129 ? 1.9708 1.1050 1.9506 -0.2711 -0.7785 0.3800 129 TRP B CE2 8163 C CE3 . TRP B 129 ? 1.7841 0.9719 1.8821 -0.2296 -0.7136 0.3251 129 TRP B CE3 8164 C CZ2 . TRP B 129 ? 2.0127 1.1542 2.0795 -0.2650 -0.8242 0.3974 129 TRP B CZ2 8165 C CZ3 . TRP B 129 ? 1.8239 1.0205 2.0092 -0.2236 -0.7558 0.3398 129 TRP B CZ3 8166 C CH2 . TRP B 129 ? 1.9579 1.1312 2.1295 -0.2404 -0.8115 0.3760 129 TRP B CH2 8167 N N . SER B 130 ? 1.9692 1.0820 1.7735 -0.2581 -0.6159 0.3291 130 SER B N 8168 C CA . SER B 130 ? 2.0307 1.1147 1.7957 -0.2718 -0.6365 0.3579 130 SER B CA 8169 C C . SER B 130 ? 1.8754 0.9583 1.6778 -0.2544 -0.6144 0.3543 130 SER B C 8170 O O . SER B 130 ? 1.9619 1.0216 1.7466 -0.2630 -0.6312 0.3785 130 SER B O 8171 C CB . SER B 130 ? 1.9164 0.9811 1.5660 -0.2987 -0.6264 0.3622 130 SER B CB 8172 O OG . SER B 130 ? 1.7292 0.8053 1.3457 -0.2923 -0.5748 0.3321 130 SER B OG 8173 N N . ILE B 131 ? 1.6895 0.7970 1.5422 -0.2316 -0.5772 0.3245 131 ILE B N 8174 C CA . ILE B 131 ? 1.5924 0.7016 1.4783 -0.2153 -0.5518 0.3157 131 ILE B CA 8175 C C . ILE B 131 ? 1.6205 0.7341 1.6090 -0.1977 -0.5765 0.3229 131 ILE B C 8176 O O . ILE B 131 ? 1.7565 0.8686 1.7833 -0.1845 -0.5630 0.3180 131 ILE B O 8177 C CB . ILE B 131 ? 1.5333 0.6668 1.4198 -0.2012 -0.5001 0.2801 131 ILE B CB 8178 C CG1 . ILE B 131 ? 1.5438 0.6672 1.3810 -0.2031 -0.4682 0.2754 131 ILE B CG1 8179 C CG2 . ILE B 131 ? 1.4839 0.6450 1.4676 -0.1768 -0.4893 0.2592 131 ILE B CG2 8180 C CD1 . ILE B 131 ? 1.4962 0.6408 1.3215 -0.1933 -0.4215 0.2443 131 ILE B CD1 8181 N N . GLN B 132 ? 1.6337 0.7519 1.6669 -0.1987 -0.6143 0.3346 132 GLN B N 8182 C CA . GLN B 132 ? 1.7097 0.8356 1.8510 -0.1814 -0.6399 0.3393 132 GLN B CA 8183 C C . GLN B 132 ? 1.9144 1.0205 2.0820 -0.1784 -0.6572 0.3593 132 GLN B C 8184 O O . GLN B 132 ? 1.8644 0.9857 2.1055 -0.1575 -0.6407 0.3425 132 GLN B O 8185 C CB . GLN B 132 ? 1.8825 1.0108 2.0512 -0.1894 -0.6862 0.3570 132 GLN B CB 8186 C CG . GLN B 132 ? 2.1476 1.2463 2.2312 -0.2185 -0.7238 0.3913 132 GLN B CG 8187 C CD . GLN B 132 ? 2.3001 1.4057 2.3942 -0.2290 -0.7617 0.4019 132 GLN B CD 8188 O OE1 . GLN B 132 ? 2.3358 1.4695 2.4997 -0.2145 -0.7577 0.3827 132 GLN B OE1 8189 N NE2 . GLN B 132 ? 2.3352 1.4156 2.3584 -0.2559 -0.7987 0.4325 132 GLN B NE2 8190 N N . ASN B 133 ? 1.9258 1.0141 2.0321 -0.1992 -0.6837 0.3883 133 ASN B N 8191 C CA . ASN B 133 ? 1.8258 0.9113 1.9532 -0.1986 -0.6980 0.4044 133 ASN B CA 8192 C C . ASN B 133 ? 1.9601 1.0330 2.0198 -0.2053 -0.6653 0.4019 133 ASN B C 8193 O O . ASN B 133 ? 1.9986 1.0662 2.0646 -0.2076 -0.6737 0.4155 133 ASN B O 8194 C CB . ASN B 133 ? 1.9553 1.0307 2.0645 -0.2191 -0.7498 0.4390 133 ASN B CB 8195 C CG . ASN B 133 ? 2.1207 1.2116 2.3181 -0.2100 -0.7871 0.4436 133 ASN B CG 8196 O OD1 . ASN B 133 ? 2.1065 1.1986 2.2911 -0.2167 -0.7999 0.4436 133 ASN B OD1 8197 N ND2 . ASN B 133 ? 2.1628 1.2659 2.4533 -0.1950 -0.8049 0.4468 133 ASN B ND2 8198 N N . LEU B 134 ? 2.0685 1.1369 2.0671 -0.2088 -0.6282 0.3841 134 LEU B N 8199 C CA . LEU B 134 ? 2.2160 1.2731 2.1454 -0.2176 -0.5971 0.3818 134 LEU B CA 8200 C C . LEU B 134 ? 2.0763 1.1446 2.0609 -0.1957 -0.5658 0.3606 134 LEU B C 8201 O O . LEU B 134 ? 2.1817 1.2432 2.1222 -0.2000 -0.5387 0.3564 134 LEU B O 8202 C CB . LEU B 134 ? 2.0244 1.0725 1.8684 -0.2307 -0.5701 0.3706 134 LEU B CB 8203 C CG . LEU B 134 ? 2.0065 1.0351 1.7508 -0.2614 -0.5854 0.3926 134 LEU B CG 8204 C CD1 . LEU B 134 ? 1.9293 0.9549 1.6833 -0.2731 -0.6349 0.4158 134 LEU B CD1 8205 C CD2 . LEU B 134 ? 2.0858 1.1169 1.7573 -0.2701 -0.5510 0.3722 134 LEU B CD2 8206 N N . GLY B 135 ? 1.7735 0.8596 1.8550 -0.1733 -0.5691 0.3460 135 GLY B N 8207 C CA . GLY B 135 ? 1.5608 0.6576 1.7016 -0.1537 -0.5447 0.3264 135 GLY B CA 8208 C C . GLY B 135 ? 1.6983 0.7882 1.8619 -0.1553 -0.5653 0.3458 135 GLY B C 8209 O O . GLY B 135 ? 1.6882 0.7734 1.8402 -0.1535 -0.5436 0.3407 135 GLY B O 8210 N N . THR B 136 ? 1.6449 0.7339 1.8422 -0.1596 -0.6086 0.3687 136 THR B N 8211 C CA . THR B 136 ? 1.6886 0.7701 1.9103 -0.1630 -0.6334 0.3899 136 THR B CA 8212 C C . THR B 136 ? 1.7966 0.8565 1.9203 -0.1901 -0.6404 0.4163 136 THR B C 8213 O O . THR B 136 ? 1.9918 1.0428 2.1135 -0.1947 -0.6440 0.4287 136 THR B O 8214 C CB . THR B 136 ? 1.8995 0.9883 2.1957 -0.1595 -0.6800 0.4061 136 THR B CB 8215 O OG1 . THR B 136 ? 1.9165 0.9981 2.1613 -0.1791 -0.7093 0.4271 136 THR B OG1 8216 C CG2 . THR B 136 ? 1.9634 1.0764 2.3634 -0.1330 -0.6714 0.3782 136 THR B CG2 8217 N N . LYS B 137 ? 2.0456 1.0975 2.0888 -0.2088 -0.6418 0.4239 137 LYS B N 8218 C CA . LYS B 137 ? 2.1887 1.2222 2.1324 -0.2364 -0.6428 0.4445 137 LYS B CA 8219 C C . LYS B 137 ? 1.9485 0.9784 1.8549 -0.2349 -0.5993 0.4298 137 LYS B C 8220 O O . LYS B 137 ? 1.9489 0.9670 1.8092 -0.2507 -0.5982 0.4454 137 LYS B O 8221 C CB . LYS B 137 ? 2.2531 1.2798 2.1199 -0.2561 -0.6489 0.4498 137 LYS B CB 8222 C CG . LYS B 137 ? 2.2614 1.2880 2.1471 -0.2653 -0.6971 0.4703 137 LYS B CG 8223 C CD . LYS B 137 ? 2.2139 1.2315 2.0144 -0.2873 -0.7007 0.4741 137 LYS B CD 8224 C CE . LYS B 137 ? 2.3286 1.3484 2.1562 -0.2941 -0.7476 0.4903 137 LYS B CE 8225 N NZ . LYS B 137 ? 2.2483 1.2596 1.9971 -0.3139 -0.7491 0.4898 137 LYS B NZ 8226 N N . LEU B 138 ? 1.6986 0.7396 1.6266 -0.2169 -0.5638 0.3996 138 LEU B N 8227 C CA . LEU B 138 ? 1.8446 0.8848 1.7463 -0.2136 -0.5224 0.3827 138 LEU B CA 8228 C C . LEU B 138 ? 1.9037 0.9457 1.8664 -0.2010 -0.5212 0.3817 138 LEU B C 8229 O O . LEU B 138 ? 1.8239 0.8594 1.7565 -0.2065 -0.5004 0.3814 138 LEU B O 8230 C CB . LEU B 138 ? 1.6133 0.6655 1.5246 -0.1989 -0.4881 0.3510 138 LEU B CB 8231 C CG . LEU B 138 ? 1.5802 0.6336 1.4651 -0.1955 -0.4449 0.3308 138 LEU B CG 8232 C CD1 . LEU B 138 ? 1.6131 0.6524 1.4055 -0.2192 -0.4349 0.3448 138 LEU B CD1 8233 C CD2 . LEU B 138 ? 1.6172 0.6822 1.5094 -0.1839 -0.4181 0.3025 138 LEU B CD2 8234 N N . ALA B 139 ? 1.8458 0.8970 1.8966 -0.1846 -0.5437 0.3805 139 ALA B N 8235 C CA . ALA B 139 ? 1.7368 0.7893 1.8538 -0.1720 -0.5457 0.3783 139 ALA B CA 8236 C C . ALA B 139 ? 1.7135 0.7486 1.7925 -0.1910 -0.5640 0.4080 139 ALA B C 8237 O O . ALA B 139 ? 1.7700 0.7998 1.8481 -0.1901 -0.5460 0.4046 139 ALA B O 8238 C CB . ALA B 139 ? 1.7610 0.8266 1.9780 -0.1539 -0.5712 0.3742 139 ALA B CB 8239 N N . THR B 140 ? 1.7632 0.7895 1.8098 -0.2097 -0.6000 0.4369 140 THR B N 8240 C CA . THR B 140 ? 1.8235 0.8335 1.8335 -0.2307 -0.6214 0.4674 140 THR B CA 8241 C C . THR B 140 ? 1.8746 0.8744 1.7926 -0.2495 -0.5917 0.4694 140 THR B C 8242 O O . THR B 140 ? 1.9401 0.9301 1.8462 -0.2582 -0.5897 0.4815 140 THR B O 8243 C CB . THR B 140 ? 1.8780 0.8816 1.8672 -0.2497 -0.6671 0.4970 140 THR B CB 8244 O OG1 . THR B 140 ? 2.0420 1.0440 1.9518 -0.2653 -0.6597 0.4962 140 THR B OG1 8245 C CG2 . THR B 140 ? 1.8701 0.8857 1.9557 -0.2317 -0.6982 0.4956 140 THR B CG2 8246 N N . GLN B 141 ? 1.8459 0.8484 1.7020 -0.2559 -0.5685 0.4570 141 GLN B N 8247 C CA . GLN B 141 ? 1.8368 0.8320 1.6071 -0.2741 -0.5390 0.4567 141 GLN B CA 8248 C C . GLN B 141 ? 1.9540 0.9534 1.7454 -0.2604 -0.5013 0.4356 141 GLN B C 8249 O O . GLN B 141 ? 1.7985 0.7901 1.5550 -0.2731 -0.4890 0.4440 141 GLN B O 8250 C CB . GLN B 141 ? 1.8114 0.8087 1.5167 -0.2834 -0.5241 0.4464 141 GLN B CB 8251 C CG . GLN B 141 ? 2.0414 1.0321 1.7080 -0.3029 -0.5595 0.4678 141 GLN B CG 8252 C CD . GLN B 141 ? 2.0683 1.0453 1.6733 -0.3324 -0.5766 0.4963 141 GLN B CD 8253 O OE1 . GLN B 141 ? 1.9400 0.9124 1.5037 -0.3429 -0.5524 0.4967 141 GLN B OE1 8254 N NE2 . GLN B 141 ? 1.9825 0.9536 1.5819 -0.3470 -0.6188 0.5201 141 GLN B NE2 8255 N N . MET B 142 ? 1.8259 0.8381 1.6745 -0.2358 -0.4833 0.4079 142 MET B N 8256 C CA . MET B 142 ? 1.8293 0.8465 1.7025 -0.2225 -0.4492 0.3855 142 MET B CA 8257 C C . MET B 142 ? 1.8001 0.8130 1.7349 -0.2146 -0.4618 0.3922 142 MET B C 8258 O O . MET B 142 ? 1.8387 0.8507 1.7822 -0.2105 -0.4382 0.3810 142 MET B O 8259 C CB . MET B 142 ? 1.7446 0.7772 1.6594 -0.2006 -0.4274 0.3532 142 MET B CB 8260 C CG . MET B 142 ? 1.6023 0.6382 1.4543 -0.2075 -0.4043 0.3414 142 MET B CG 8261 S SD . MET B 142 ? 1.9756 1.0048 1.7478 -0.2252 -0.3706 0.3409 142 MET B SD 8262 C CE . MET B 142 ? 1.7556 0.7922 1.5878 -0.2063 -0.3448 0.3173 142 MET B CE 8263 N N . ARG B 143 ? 1.7551 0.7650 1.7340 -0.2131 -0.5000 0.4103 143 ARG B N 8264 C CA . ARG B 143 ? 1.8411 0.8455 1.8815 -0.2065 -0.5165 0.4188 143 ARG B CA 8265 C C . ARG B 143 ? 1.7823 0.7717 1.7724 -0.2263 -0.5121 0.4379 143 ARG B C 8266 O O . ARG B 143 ? 1.9378 0.9229 1.9647 -0.2199 -0.5047 0.4338 143 ARG B O 8267 C CB . ARG B 143 ? 1.9429 0.9462 2.0318 -0.2055 -0.5624 0.4392 143 ARG B CB 8268 C CG . ARG B 143 ? 1.8947 0.8933 2.0593 -0.1963 -0.5820 0.4460 143 ARG B CG 8269 C CD . ARG B 143 ? 1.8332 0.8335 2.0519 -0.1945 -0.6281 0.4646 143 ARG B CD 8270 N NE . ARG B 143 ? 2.2331 1.2269 2.5213 -0.1885 -0.6497 0.4745 143 ARG B NE 8271 C CZ . ARG B 143 ? 2.2466 1.2402 2.5925 -0.1874 -0.6922 0.4928 143 ARG B CZ 8272 N NH1 . ARG B 143 ? 2.3401 1.3400 2.6818 -0.1923 -0.7182 0.5035 143 ARG B NH1 8273 N NH2 . ARG B 143 ? 2.0340 1.0210 2.4438 -0.1820 -0.7097 0.5004 143 ARG B NH2 8274 N N . LYS B 144 ? 1.8177 0.7994 1.7235 -0.2512 -0.5156 0.4576 144 LYS B N 8275 C CA . LYS B 144 ? 1.8588 0.8277 1.7100 -0.2735 -0.5111 0.4770 144 LYS B CA 8276 C C . LYS B 144 ? 1.8962 0.8680 1.7358 -0.2692 -0.4688 0.4561 144 LYS B C 8277 O O . LYS B 144 ? 2.1161 1.0799 1.9670 -0.2731 -0.4647 0.4627 144 LYS B O 8278 C CB . LYS B 144 ? 1.9022 0.8656 1.6619 -0.3017 -0.5185 0.4966 144 LYS B CB 8279 C CG . LYS B 144 ? 2.0661 1.0272 1.8296 -0.3084 -0.5604 0.5159 144 LYS B CG 8280 C CD . LYS B 144 ? 2.1860 1.1376 2.0010 -0.3101 -0.5996 0.5409 144 LYS B CD 8281 C CE . LYS B 144 ? 2.2535 1.2050 2.0840 -0.3146 -0.6433 0.5585 144 LYS B CE 8282 N NZ . LYS B 144 ? 2.0038 0.9703 1.8976 -0.2886 -0.6435 0.5356 144 LYS B NZ 8283 N N . LEU B 145 ? 1.9722 0.9553 1.7901 -0.2621 -0.4386 0.4313 145 LEU B N 8284 C CA . LEU B 145 ? 1.9963 0.9841 1.8026 -0.2585 -0.3991 0.4101 145 LEU B CA 8285 C C . LEU B 145 ? 1.8278 0.8221 1.7140 -0.2333 -0.3879 0.3853 145 LEU B C 8286 O O . LEU B 145 ? 1.7592 0.7521 1.6531 -0.2322 -0.3667 0.3756 145 LEU B O 8287 C CB . LEU B 145 ? 2.0478 1.0448 1.7990 -0.2620 -0.3725 0.3938 145 LEU B CB 8288 C CG . LEU B 145 ? 2.1022 1.0938 1.7691 -0.2878 -0.3780 0.4125 145 LEU B CG 8289 C CD1 . LEU B 145 ? 2.0655 1.0658 1.6850 -0.2891 -0.3485 0.3923 145 LEU B CD1 8290 C CD2 . LEU B 145 ? 1.8708 0.8526 1.4945 -0.3109 -0.3763 0.4333 145 LEU B CD2 8291 N N . THR B 146 ? 1.9155 0.9175 1.8610 -0.2142 -0.4016 0.3737 146 THR B N 8292 C CA . THR B 146 ? 1.8346 0.8453 1.8542 -0.1908 -0.3883 0.3455 146 THR B CA 8293 C C . THR B 146 ? 1.9489 0.9621 2.0487 -0.1750 -0.4175 0.3464 146 THR B C 8294 O O . THR B 146 ? 1.9874 1.0049 2.0944 -0.1735 -0.4394 0.3544 146 THR B O 8295 C CB . THR B 146 ? 1.9268 0.9524 1.9399 -0.1797 -0.3584 0.3148 146 THR B CB 8296 O OG1 . THR B 146 ? 2.0807 1.1054 2.0320 -0.1920 -0.3296 0.3105 146 THR B OG1 8297 C CG2 . THR B 146 ? 1.7648 0.8007 1.8537 -0.1572 -0.3462 0.2845 146 THR B CG2 8298 N N . SER B 147 ? 1.9110 0.9219 2.0731 -0.1638 -0.4177 0.3373 147 SER B N 8299 C CA . SER B 147 ? 1.9284 0.9433 2.1757 -0.1477 -0.4427 0.3346 147 SER B CA 8300 C C . SER B 147 ? 1.9778 1.0124 2.2789 -0.1257 -0.4269 0.2997 147 SER B C 8301 O O . SER B 147 ? 2.0390 1.0825 2.3974 -0.1142 -0.4479 0.2981 147 SER B O 8302 C CB . SER B 147 ? 1.8022 0.8067 2.0969 -0.1447 -0.4483 0.3365 147 SER B CB 8303 O OG . SER B 147 ? 1.8493 0.8589 2.1599 -0.1352 -0.4142 0.3054 147 SER B OG 8304 N N . ASN B 148 ? 1.8014 0.8438 2.0857 -0.1209 -0.3902 0.2717 148 ASN B N 8305 C CA . ASN B 148 ? 1.7446 0.8064 2.0753 -0.1023 -0.3719 0.2368 148 ASN B CA 8306 C C . ASN B 148 ? 1.7328 0.8032 2.0107 -0.1062 -0.3572 0.2307 148 ASN B C 8307 O O . ASN B 148 ? 1.5626 0.6322 1.7862 -0.1137 -0.3310 0.2227 148 ASN B O 8308 C CB . ASN B 148 ? 1.6426 0.7085 2.0011 -0.0937 -0.3424 0.2060 148 ASN B CB 8309 C CG . ASN B 148 ? 1.7414 0.8275 2.1703 -0.0736 -0.3297 0.1697 148 ASN B CG 8310 O OD1 . ASN B 148 ? 1.7844 0.8844 2.2199 -0.0675 -0.3281 0.1606 148 ASN B OD1 8311 N ND2 . ASN B 148 ? 1.4569 0.5453 1.9391 -0.0642 -0.3196 0.1478 148 ASN B ND2 8312 N N . LEU B 149 ? 1.6549 0.7343 1.9537 -0.1006 -0.3743 0.2334 149 LEU B N 8313 C CA . LEU B 149 ? 1.4653 0.5505 1.7137 -0.1058 -0.3657 0.2316 149 LEU B CA 8314 C C . LEU B 149 ? 1.4603 0.5658 1.7624 -0.0889 -0.3561 0.2032 149 LEU B C 8315 O O . LEU B 149 ? 1.4304 0.5457 1.8096 -0.0752 -0.3695 0.1950 149 LEU B O 8316 C CB . LEU B 149 ? 1.6303 0.7054 1.8358 -0.1209 -0.3971 0.2658 149 LEU B CB 8317 C CG . LEU B 149 ? 1.4920 0.5704 1.6422 -0.1286 -0.3929 0.2670 149 LEU B CG 8318 C CD1 . LEU B 149 ? 1.4829 0.5551 1.5524 -0.1419 -0.3647 0.2647 149 LEU B CD1 8319 C CD2 . LEU B 149 ? 1.5329 0.6037 1.6627 -0.1407 -0.4301 0.2973 149 LEU B CD2 8320 N N . ARG B 150 ? 1.5033 0.6159 1.7660 -0.0906 -0.3324 0.1879 150 ARG B N 8321 C CA . ARG B 150 ? 1.4881 0.6199 1.7920 -0.0778 -0.3218 0.1624 150 ARG B CA 8322 C C . ARG B 150 ? 1.4719 0.6031 1.7191 -0.0872 -0.3226 0.1705 150 ARG B C 8323 O O . ARG B 150 ? 1.5549 0.6761 1.7274 -0.1005 -0.3108 0.1786 150 ARG B O 8324 C CB . ARG B 150 ? 1.5205 0.6644 1.8444 -0.0689 -0.2862 0.1264 150 ARG B CB 8325 C CG . ARG B 150 ? 1.3990 0.5445 1.7789 -0.0598 -0.2816 0.1127 150 ARG B CG 8326 C CD . ARG B 150 ? 1.6512 0.8123 2.1220 -0.0438 -0.2936 0.0991 150 ARG B CD 8327 N NE . ARG B 150 ? 1.8756 1.0473 2.4023 -0.0326 -0.2736 0.0676 150 ARG B NE 8328 C CZ . ARG B 150 ? 1.7807 0.9702 2.3217 -0.0266 -0.2421 0.0315 150 ARG B CZ 8329 N NH1 . ARG B 150 ? 1.7181 0.9160 2.2240 -0.0302 -0.2276 0.0238 150 ARG B NH1 8330 N NH2 . ARG B 150 ? 1.5473 0.7464 2.1367 -0.0183 -0.2250 0.0026 150 ARG B NH2 8331 N N . ILE B 151 ? 1.5343 0.6768 1.8188 -0.0806 -0.3362 0.1676 151 ILE B N 8332 C CA . ILE B 151 ? 1.4991 0.6420 1.7361 -0.0887 -0.3355 0.1713 151 ILE B CA 8333 C C . ILE B 151 ? 1.4733 0.6508 1.7548 -0.0752 -0.3149 0.1401 151 ILE B C 8334 O O . ILE B 151 ? 1.5234 0.7118 1.8861 -0.0611 -0.3164 0.1235 151 ILE B O 8335 C CB . ILE B 151 ? 1.3977 0.5306 1.6155 -0.0990 -0.3727 0.2026 151 ILE B CB 8336 C CG1 . ILE B 151 ? 1.6122 0.7548 1.9167 -0.0870 -0.4010 0.2061 151 ILE B CG1 8337 C CG2 . ILE B 151 ? 1.6297 0.7419 1.7801 -0.1164 -0.3843 0.2310 151 ILE B CG2 8338 C CD1 . ILE B 151 ? 1.7020 0.8337 1.9896 -0.0987 -0.4422 0.2397 151 ILE B CD1 8339 N N . GLY B 152 ? 1.4827 0.6779 1.7115 -0.0803 -0.2946 0.1317 152 GLY B N 8340 C CA . GLY B 152 ? 1.6539 0.8822 1.9135 -0.0711 -0.2745 0.1052 152 GLY B CA 8341 C C . GLY B 152 ? 1.5980 0.8341 1.7986 -0.0808 -0.2713 0.1110 152 GLY B C 8342 O O . GLY B 152 ? 1.5013 0.7214 1.6293 -0.0936 -0.2723 0.1271 152 GLY B O 8343 N N . PHE B 153 ? 1.4939 0.7548 1.7272 -0.0752 -0.2663 0.0967 153 PHE B N 8344 C CA . PHE B 153 ? 1.2623 0.5296 1.4484 -0.0842 -0.2665 0.1020 153 PHE B CA 8345 C C . PHE B 153 ? 1.2336 0.5316 1.4207 -0.0801 -0.2328 0.0757 153 PHE B C 8346 O O . PHE B 153 ? 1.1772 0.4975 1.4220 -0.0697 -0.2173 0.0536 153 PHE B O 8347 C CB . PHE B 153 ? 1.3113 0.5750 1.5306 -0.0859 -0.3025 0.1180 153 PHE B CB 8348 C CG . PHE B 153 ? 1.4081 0.6703 1.5710 -0.0984 -0.3096 0.1282 153 PHE B CG 8349 C CD1 . PHE B 153 ? 1.5991 0.8346 1.6930 -0.1135 -0.3271 0.1521 153 PHE B CD1 8350 C CD2 . PHE B 153 ? 1.3147 0.6021 1.4937 -0.0963 -0.2983 0.1130 153 PHE B CD2 8351 C CE1 . PHE B 153 ? 1.7278 0.9614 1.7701 -0.1258 -0.3326 0.1585 153 PHE B CE1 8352 C CE2 . PHE B 153 ? 1.2506 0.5351 1.3802 -0.1081 -0.3052 0.1210 153 PHE B CE2 8353 C CZ . PHE B 153 ? 1.2846 0.5420 1.3460 -0.1225 -0.3222 0.1427 153 PHE B CZ 8354 N N . GLY B 154 ? 1.4065 0.7051 1.5293 -0.0894 -0.2216 0.0783 154 GLY B N 8355 C CA . GLY B 154 ? 1.3311 0.6556 1.4482 -0.0881 -0.1934 0.0584 154 GLY B CA 8356 C C . GLY B 154 ? 1.3635 0.6836 1.4272 -0.0988 -0.1974 0.0678 154 GLY B C 8357 O O . GLY B 154 ? 1.2742 0.5709 1.2873 -0.1083 -0.2124 0.0859 154 GLY B O 8358 N N . ALA B 155 ? 1.3687 0.7110 1.4427 -0.0984 -0.1830 0.0546 155 ALA B N 8359 C CA . ALA B 155 ? 1.2328 0.5714 1.2671 -0.1080 -0.1891 0.0617 155 ALA B CA 8360 C C . ALA B 155 ? 1.2003 0.5548 1.2097 -0.1098 -0.1595 0.0478 155 ALA B C 8361 O O . ALA B 155 ? 1.3361 0.7115 1.3717 -0.1038 -0.1366 0.0315 155 ALA B O 8362 C CB . ALA B 155 ? 1.2330 0.5790 1.3127 -0.1083 -0.2134 0.0659 155 ALA B CB 8363 N N . PHE B 156 ? 1.1857 0.5294 1.1443 -0.1190 -0.1607 0.0543 156 PHE B N 8364 C CA . PHE B 156 ? 1.3820 0.7368 1.3164 -0.1216 -0.1366 0.0443 156 PHE B CA 8365 C C . PHE B 156 ? 1.3993 0.7465 1.3077 -0.1310 -0.1475 0.0499 156 PHE B C 8366 O O . PHE B 156 ? 1.1904 0.5181 1.0756 -0.1378 -0.1702 0.0622 156 PHE B O 8367 C CB . PHE B 156 ? 1.1822 0.5282 1.0706 -0.1219 -0.1172 0.0433 156 PHE B CB 8368 C CG . PHE B 156 ? 1.3295 0.6495 1.1624 -0.1299 -0.1269 0.0557 156 PHE B CG 8369 C CD1 . PHE B 156 ? 1.3857 0.6876 1.2082 -0.1316 -0.1427 0.0674 156 PHE B CD1 8370 C CD2 . PHE B 156 ? 1.3441 0.6575 1.1361 -0.1369 -0.1195 0.0549 156 PHE B CD2 8371 C CE1 . PHE B 156 ? 1.4789 0.7585 1.2474 -0.1415 -0.1494 0.0780 156 PHE B CE1 8372 C CE2 . PHE B 156 ? 1.3651 0.6562 1.1066 -0.1453 -0.1256 0.0629 156 PHE B CE2 8373 C CZ . PHE B 156 ? 1.4308 0.7058 1.1586 -0.1484 -0.1397 0.0743 156 PHE B CZ 8374 N N . VAL B 157 ? 1.2766 0.6385 1.1880 -0.1328 -0.1319 0.0409 157 VAL B N 8375 C CA . VAL B 157 ? 1.3117 0.6648 1.1949 -0.1421 -0.1381 0.0438 157 VAL B CA 8376 C C . VAL B 157 ? 1.3224 0.6740 1.1692 -0.1440 -0.1142 0.0383 157 VAL B C 8377 O O . VAL B 157 ? 1.4060 0.7383 1.2058 -0.1479 -0.1124 0.0419 157 VAL B O 8378 C CB . VAL B 157 ? 1.2327 0.6033 1.1602 -0.1443 -0.1465 0.0401 157 VAL B CB 8379 C CG1 . VAL B 157 ? 1.4931 0.8523 1.3900 -0.1549 -0.1535 0.0424 157 VAL B CG1 8380 C CG2 . VAL B 157 ? 1.2717 0.6454 1.2438 -0.1414 -0.1721 0.0458 157 VAL B CG2 8381 N N . ASP B 158 ? 1.1427 0.5155 1.0134 -0.1417 -0.0956 0.0297 158 ASP B N 8382 C CA . ASP B 158 ? 1.1321 0.5053 0.9761 -0.1437 -0.0752 0.0264 158 ASP B CA 8383 C C . ASP B 158 ? 1.1226 0.5227 1.0006 -0.1428 -0.0584 0.0187 158 ASP B C 8384 O O . ASP B 158 ? 1.1257 0.5437 1.0472 -0.1410 -0.0616 0.0140 158 ASP B O 8385 C CB . ASP B 158 ? 1.1575 0.5151 0.9739 -0.1519 -0.0815 0.0290 158 ASP B CB 8386 C CG . ASP B 158 ? 1.2075 0.5541 0.9866 -0.1527 -0.0656 0.0282 158 ASP B CG 8387 O OD1 . ASP B 158 ? 1.1201 0.4777 0.9020 -0.1483 -0.0483 0.0262 158 ASP B OD1 8388 O OD2 . ASP B 158 ? 1.1955 0.5226 0.9440 -0.1581 -0.0709 0.0290 158 ASP B OD2 8389 N N . LYS B 159 ? 1.1140 0.5174 0.9731 -0.1450 -0.0405 0.0175 159 LYS B N 8390 C CA . LYS B 159 ? 1.1110 0.5394 0.9942 -0.1475 -0.0238 0.0118 159 LYS B CA 8391 C C . LYS B 159 ? 1.2485 0.6883 1.1607 -0.1543 -0.0289 0.0106 159 LYS B C 8392 O O . LYS B 159 ? 1.2131 0.6401 1.1101 -0.1602 -0.0356 0.0155 159 LYS B O 8393 C CB . LYS B 159 ? 1.1033 0.5295 0.9567 -0.1503 -0.0079 0.0147 159 LYS B CB 8394 C CG . LYS B 159 ? 1.0948 0.5182 0.9288 -0.1445 0.0006 0.0141 159 LYS B CG 8395 C CD . LYS B 159 ? 1.1390 0.5581 0.9455 -0.1472 0.0117 0.0192 159 LYS B CD 8396 C CE . LYS B 159 ? 1.1411 0.5669 0.9377 -0.1435 0.0224 0.0171 159 LYS B CE 8397 N NZ . LYS B 159 ? 1.2994 0.7152 1.0928 -0.1362 0.0156 0.0149 159 LYS B NZ 8398 N N . PRO B 160 ? 1.2326 0.6971 1.1895 -0.1539 -0.0251 0.0028 160 PRO B N 8399 C CA . PRO B 160 ? 1.1925 0.6724 1.1856 -0.1605 -0.0291 0.0004 160 PRO B CA 8400 C C . PRO B 160 ? 1.3459 0.8371 1.3328 -0.1708 -0.0124 0.0014 160 PRO B C 8401 O O . PRO B 160 ? 1.2987 0.8169 1.3162 -0.1758 0.0020 -0.0058 160 PRO B O 8402 C CB . PRO B 160 ? 1.1373 0.6420 1.1821 -0.1555 -0.0256 -0.0107 160 PRO B CB 8403 C CG . PRO B 160 ? 1.2096 0.7189 1.2402 -0.1506 -0.0085 -0.0164 160 PRO B CG 8404 C CD . PRO B 160 ? 1.1697 0.6500 1.1486 -0.1473 -0.0152 -0.0064 160 PRO B CD 8405 N N . VAL B 161 ? 1.2859 0.7563 1.2344 -0.1747 -0.0139 0.0101 161 VAL B N 8406 C CA . VAL B 161 ? 1.2280 0.7038 1.1683 -0.1849 -0.0013 0.0145 161 VAL B CA 8407 C C . VAL B 161 ? 1.1816 0.6295 1.0945 -0.1881 -0.0125 0.0225 161 VAL B C 8408 O O . VAL B 161 ? 1.1354 0.5608 1.0257 -0.1822 -0.0246 0.0234 161 VAL B O 8409 C CB . VAL B 161 ? 1.1621 0.6459 1.0815 -0.1853 0.0179 0.0155 161 VAL B CB 8410 C CG1 . VAL B 161 ? 1.1179 0.5770 0.9977 -0.1780 0.0143 0.0210 161 VAL B CG1 8411 C CG2 . VAL B 161 ? 1.7520 1.2469 1.6695 -0.1985 0.0306 0.0215 161 VAL B CG2 8412 N N . SER B 162 ? 1.1380 0.5870 1.0536 -0.1985 -0.0083 0.0274 162 SER B N 8413 C CA . SER B 162 ? 1.3232 0.7449 1.2155 -0.2017 -0.0169 0.0331 162 SER B CA 8414 C C . SER B 162 ? 1.2486 0.6535 1.1056 -0.1959 -0.0101 0.0376 162 SER B C 8415 O O . SER B 162 ? 1.1260 0.5439 0.9781 -0.1945 0.0031 0.0398 162 SER B O 8416 C CB . SER B 162 ? 1.4359 0.8624 1.3434 -0.2148 -0.0138 0.0383 162 SER B CB 8417 O OG . SER B 162 ? 1.8438 1.2874 1.7519 -0.2208 0.0037 0.0440 162 SER B OG 8418 N N . PRO B 163 ? 1.2390 0.6160 1.0723 -0.1933 -0.0188 0.0378 163 PRO B N 8419 C CA . PRO B 163 ? 1.3483 0.7069 1.1793 -0.1966 -0.0345 0.0338 163 PRO B CA 8420 C C . PRO B 163 ? 1.1605 0.5181 0.9917 -0.1924 -0.0485 0.0281 163 PRO B C 8421 O O . PRO B 163 ? 1.5541 0.9024 1.3884 -0.1977 -0.0637 0.0253 163 PRO B O 8422 C CB . PRO B 163 ? 1.3014 0.6324 1.1028 -0.1942 -0.0333 0.0338 163 PRO B CB 8423 C CG . PRO B 163 ? 1.3446 0.6792 1.1307 -0.1853 -0.0224 0.0359 163 PRO B CG 8424 C CD . PRO B 163 ? 1.1264 0.4888 0.9319 -0.1869 -0.0121 0.0406 163 PRO B CD 8425 N N . TYR B 164 ? 1.1406 0.5065 0.9684 -0.1840 -0.0450 0.0272 164 TYR B N 8426 C CA . TYR B 164 ? 1.2823 0.6421 1.1053 -0.1799 -0.0597 0.0248 164 TYR B CA 8427 C C . TYR B 164 ? 1.1556 0.5288 1.0139 -0.1837 -0.0748 0.0235 164 TYR B C 8428 O O . TYR B 164 ? 1.1700 0.5305 1.0215 -0.1864 -0.0940 0.0236 164 TYR B O 8429 C CB . TYR B 164 ? 1.3017 0.6685 1.1197 -0.1706 -0.0522 0.0248 164 TYR B CB 8430 C CG . TYR B 164 ? 1.2392 0.6011 1.0333 -0.1668 -0.0357 0.0265 164 TYR B CG 8431 C CD1 . TYR B 164 ? 1.3629 0.7015 1.1246 -0.1666 -0.0353 0.0265 164 TYR B CD1 8432 C CD2 . TYR B 164 ? 1.1737 0.5550 0.9792 -0.1642 -0.0207 0.0270 164 TYR B CD2 8433 C CE1 . TYR B 164 ? 1.5449 0.8803 1.2913 -0.1626 -0.0217 0.0284 164 TYR B CE1 8434 C CE2 . TYR B 164 ? 1.2040 0.5814 0.9891 -0.1615 -0.0085 0.0299 164 TYR B CE2 8435 C CZ . TYR B 164 ? 1.4685 0.8231 1.2266 -0.1600 -0.0098 0.0312 164 TYR B CZ 8436 O OH . TYR B 164 ? 1.4941 0.8460 1.2382 -0.1568 0.0008 0.0344 164 TYR B OH 8437 N N . MET B 165 ? 1.1501 0.5499 1.0464 -0.1848 -0.0661 0.0222 165 MET B N 8438 C CA . MET B 165 ? 1.1569 0.5746 1.0969 -0.1870 -0.0782 0.0197 165 MET B CA 8439 C C . MET B 165 ? 1.2756 0.6906 1.2282 -0.1979 -0.0889 0.0203 165 MET B C 8440 O O . MET B 165 ? 1.1920 0.5981 1.1289 -0.2044 -0.0810 0.0221 165 MET B O 8441 C CB . MET B 165 ? 1.1728 0.6225 1.1514 -0.1849 -0.0612 0.0148 165 MET B CB 8442 C CG . MET B 165 ? 1.2938 0.7650 1.3260 -0.1842 -0.0717 0.0099 165 MET B CG 8443 S SD . MET B 165 ? 1.2039 0.7143 1.2827 -0.1827 -0.0473 -0.0007 165 MET B SD 8444 C CE . MET B 165 ? 1.9265 1.4542 2.0706 -0.1784 -0.0667 -0.0064 165 MET B CE 8445 N N . TYR B 166 ? 1.2888 0.7109 1.2723 -0.2001 -0.1084 0.0194 166 TYR B N 8446 C CA . TYR B 166 ? 1.2206 0.6477 1.2277 -0.2112 -0.1172 0.0190 166 TYR B CA 8447 C C . TYR B 166 ? 1.2816 0.7415 1.3333 -0.2142 -0.0986 0.0159 166 TYR B C 8448 O O . TYR B 166 ? 1.2518 0.7363 1.3444 -0.2093 -0.0964 0.0114 166 TYR B O 8449 C CB . TYR B 166 ? 1.2017 0.6267 1.2288 -0.2135 -0.1465 0.0199 166 TYR B CB 8450 C CG . TYR B 166 ? 1.2198 0.6121 1.1996 -0.2181 -0.1661 0.0224 166 TYR B CG 8451 C CD1 . TYR B 166 ? 1.2879 0.6610 1.2270 -0.2119 -0.1699 0.0249 166 TYR B CD1 8452 C CD2 . TYR B 166 ? 1.2592 0.6402 1.2345 -0.2303 -0.1799 0.0212 166 TYR B CD2 8453 C CE1 . TYR B 166 ? 1.3570 0.7017 1.2499 -0.2184 -0.1854 0.0256 166 TYR B CE1 8454 C CE2 . TYR B 166 ? 1.4304 0.7820 1.3599 -0.2364 -0.1963 0.0208 166 TYR B CE2 8455 C CZ . TYR B 166 ? 1.3648 0.6989 1.2520 -0.2308 -0.1982 0.0227 166 TYR B CZ 8456 O OH . TYR B 166 ? 1.4819 0.7882 1.3205 -0.2389 -0.2121 0.0208 166 TYR B OH 8457 N N . ILE B 167 ? 1.3257 0.7853 1.3698 -0.2232 -0.0848 0.0180 167 ILE B N 8458 C CA . ILE B 167 ? 1.2357 0.7248 1.3112 -0.2293 -0.0637 0.0165 167 ILE B CA 8459 C C . ILE B 167 ? 1.3391 0.8436 1.4565 -0.2415 -0.0703 0.0155 167 ILE B C 8460 O O . ILE B 167 ? 1.3156 0.8484 1.4658 -0.2490 -0.0535 0.0132 167 ILE B O 8461 C CB . ILE B 167 ? 1.3782 0.8586 1.4188 -0.2333 -0.0440 0.0226 167 ILE B CB 8462 C CG1 . ILE B 167 ? 1.6496 1.1617 1.7117 -0.2391 -0.0197 0.0212 167 ILE B CG1 8463 C CG2 . ILE B 167 ? 1.3064 0.7643 1.3308 -0.2434 -0.0510 0.0286 167 ILE B CG2 8464 C CD1 . ILE B 167 ? 1.7404 1.2447 1.7696 -0.2456 -0.0038 0.0305 167 ILE B CD1 8465 N N . SER B 168 ? 1.3749 0.8621 1.4915 -0.2447 -0.0948 0.0164 168 SER B N 8466 C CA . SER B 168 ? 1.3454 0.8410 1.4952 -0.2580 -0.1035 0.0164 168 SER B CA 8467 C C . SER B 168 ? 1.3641 0.8376 1.5054 -0.2604 -0.1344 0.0164 168 SER B C 8468 O O . SER B 168 ? 1.3237 0.7685 1.4192 -0.2552 -0.1446 0.0174 168 SER B O 8469 C CB . SER B 168 ? 1.3754 0.8638 1.5096 -0.2699 -0.0881 0.0218 168 SER B CB 8470 O OG . SER B 168 ? 1.5701 1.0218 1.6528 -0.2682 -0.0927 0.0253 168 SER B OG 8471 N N . PRO B 169 ? 1.3910 0.8786 1.5758 -0.2698 -0.1494 0.0148 169 PRO B N 8472 C CA . PRO B 169 ? 1.3207 0.8436 1.5642 -0.2784 -0.1383 0.0125 169 PRO B CA 8473 C C . PRO B 169 ? 1.4636 1.0211 1.7518 -0.2690 -0.1268 0.0068 169 PRO B C 8474 O O . PRO B 169 ? 1.3564 0.9091 1.6385 -0.2559 -0.1363 0.0057 169 PRO B O 8475 C CB . PRO B 169 ? 1.2599 0.7818 1.5322 -0.2884 -0.1664 0.0119 169 PRO B CB 8476 C CG . PRO B 169 ? 1.2423 0.7395 1.4842 -0.2811 -0.1937 0.0130 169 PRO B CG 8477 C CD . PRO B 169 ? 1.3316 0.7997 1.5077 -0.2738 -0.1816 0.0149 169 PRO B CD 8478 N N . PRO B 170 ? 1.6864 1.2782 2.0191 -0.2764 -0.1054 0.0027 170 PRO B N 8479 C CA . PRO B 170 ? 1.6411 1.2683 2.0224 -0.2685 -0.0916 -0.0067 170 PRO B CA 8480 C C . PRO B 170 ? 1.6830 1.3193 2.1129 -0.2605 -0.1192 -0.0104 170 PRO B C 8481 O O . PRO B 170 ? 1.5163 1.1689 1.9761 -0.2482 -0.1162 -0.0172 170 PRO B O 8482 C CB . PRO B 170 ? 1.6143 1.2752 2.0351 -0.2834 -0.0669 -0.0108 170 PRO B CB 8483 C CG . PRO B 170 ? 1.6735 1.3183 2.0846 -0.2986 -0.0789 -0.0026 170 PRO B CG 8484 C CD . PRO B 170 ? 1.7850 1.3844 2.1269 -0.2939 -0.0925 0.0057 170 PRO B CD 8485 N N . GLU B 171 ? 1.8640 1.4887 2.3019 -0.2680 -0.1472 -0.0055 171 GLU B N 8486 C CA . GLU B 171 ? 1.8766 1.5045 2.3537 -0.2625 -0.1803 -0.0051 171 GLU B CA 8487 C C . GLU B 171 ? 1.7286 1.3336 2.1711 -0.2474 -0.1946 -0.0012 171 GLU B C 8488 O O . GLU B 171 ? 1.6547 1.2709 2.1396 -0.2379 -0.2117 -0.0021 171 GLU B O 8489 C CB . GLU B 171 ? 1.8356 1.4470 2.3075 -0.2756 -0.2093 0.0007 171 GLU B CB 8490 C CG . GLU B 171 ? 1.8746 1.5106 2.3916 -0.2915 -0.1994 -0.0026 171 GLU B CG 8491 C CD . GLU B 171 ? 2.0503 1.6630 2.5472 -0.3060 -0.2238 0.0026 171 GLU B CD 8492 O OE1 . GLU B 171 ? 2.0425 1.6764 2.5938 -0.3173 -0.2340 0.0008 171 GLU B OE1 8493 O OE2 . GLU B 171 ? 2.1072 1.6812 2.5357 -0.3068 -0.2319 0.0071 171 GLU B OE2 8494 N N . ALA B 172 ? 1.6513 1.2242 2.0199 -0.2455 -0.1878 0.0036 172 ALA B N 8495 C CA . ALA B 172 ? 1.5957 1.1489 1.9296 -0.2323 -0.1955 0.0071 172 ALA B CA 8496 C C . ALA B 172 ? 1.6903 1.2458 1.9977 -0.2243 -0.1629 0.0031 172 ALA B C 8497 O O . ALA B 172 ? 1.9162 1.4523 2.1691 -0.2275 -0.1485 0.0058 172 ALA B O 8498 C CB . ALA B 172 ? 1.5635 1.0769 1.8330 -0.2365 -0.2179 0.0152 172 ALA B CB 8499 N N . LEU B 173 ? 1.5028 1.0820 1.8520 -0.2139 -0.1528 -0.0039 173 LEU B N 8500 C CA . LEU B 173 ? 1.3691 0.9494 1.6952 -0.2049 -0.1275 -0.0084 173 LEU B CA 8501 C C . LEU B 173 ? 1.4858 1.0673 1.8386 -0.1909 -0.1416 -0.0099 173 LEU B C 8502 O O . LEU B 173 ? 1.8584 1.4155 2.1684 -0.1833 -0.1480 -0.0042 173 LEU B O 8503 C CB . LEU B 173 ? 1.5484 1.1614 1.9021 -0.2100 -0.0929 -0.0189 173 LEU B CB 8504 C CG . LEU B 173 ? 1.3531 0.9578 1.6624 -0.2226 -0.0747 -0.0140 173 LEU B CG 8505 C CD1 . LEU B 173 ? 1.2166 0.8555 1.5532 -0.2310 -0.0422 -0.0227 173 LEU B CD1 8506 C CD2 . LEU B 173 ? 1.3475 0.9206 1.5862 -0.2173 -0.0709 -0.0071 173 LEU B CD2 8507 N N . GLU B 174 ? 1.4467 1.0579 1.8751 -0.1879 -0.1460 -0.0177 174 GLU B N 8508 C CA . GLU B 174 ? 1.6347 1.2480 2.1052 -0.1751 -0.1658 -0.0180 174 GLU B CA 8509 C C . GLU B 174 ? 1.5602 1.1413 2.0011 -0.1752 -0.2057 -0.0014 174 GLU B C 8510 O O . GLU B 174 ? 1.6971 1.2682 2.1495 -0.1656 -0.2252 0.0040 174 GLU B O 8511 C CB . GLU B 174 ? 1.7948 1.4466 2.3597 -0.1736 -0.1661 -0.0294 174 GLU B CB 8512 C CG . GLU B 174 ? 1.9192 1.6067 2.5156 -0.1764 -0.1250 -0.0477 174 GLU B CG 8513 C CD . GLU B 174 ? 1.9702 1.6976 2.6611 -0.1776 -0.1237 -0.0602 174 GLU B CD 8514 O OE1 . GLU B 174 ? 1.8601 1.5870 2.5892 -0.1782 -0.1563 -0.0525 174 GLU B OE1 8515 O OE2 . GLU B 174 ? 1.9847 1.7449 2.7121 -0.1788 -0.0901 -0.0784 174 GLU B OE2 8516 N N . ASN B 175 ? 1.3572 0.9216 1.7598 -0.1876 -0.2181 0.0064 175 ASN B N 8517 C CA . ASN B 175 ? 1.3981 0.9305 1.7600 -0.1915 -0.2533 0.0207 175 ASN B CA 8518 C C . ASN B 175 ? 1.4301 0.9326 1.7092 -0.2005 -0.2465 0.0248 175 ASN B C 8519 O O . ASN B 175 ? 1.4459 0.9417 1.7119 -0.2127 -0.2557 0.0262 175 ASN B O 8520 C CB . ASN B 175 ? 1.3970 0.9394 1.8070 -0.1991 -0.2852 0.0251 175 ASN B CB 8521 C CG . ASN B 175 ? 1.5143 1.0256 1.8847 -0.2046 -0.3248 0.0403 175 ASN B CG 8522 O OD1 . ASN B 175 ? 1.3396 0.8267 1.6641 -0.1997 -0.3312 0.0480 175 ASN B OD1 8523 N ND2 . ASN B 175 ? 1.8682 1.3803 2.2544 -0.2164 -0.3518 0.0448 175 ASN B ND2 8524 N N . PRO B 176 ? 1.4903 0.9746 1.7165 -0.1943 -0.2306 0.0257 176 PRO B N 8525 C CA . PRO B 176 ? 1.3227 0.7799 1.4758 -0.2008 -0.2206 0.0275 176 PRO B CA 8526 C C . PRO B 176 ? 1.3002 0.7300 1.4136 -0.2115 -0.2498 0.0351 176 PRO B C 8527 O O . PRO B 176 ? 1.5775 0.9890 1.6451 -0.2198 -0.2433 0.0333 176 PRO B O 8528 C CB . PRO B 176 ? 1.2891 0.7343 1.4057 -0.1904 -0.2058 0.0284 176 PRO B CB 8529 C CG . PRO B 176 ? 1.2947 0.7503 1.4544 -0.1804 -0.2193 0.0306 176 PRO B CG 8530 C CD . PRO B 176 ? 1.3718 0.8594 1.6080 -0.1807 -0.2226 0.0245 176 PRO B CD 8531 N N . CYS B 177 ? 1.2668 0.6933 1.3977 -0.2119 -0.2821 0.0432 177 CYS B N 8532 C CA . CYS B 177 ? 1.4159 0.8197 1.5121 -0.2252 -0.3123 0.0500 177 CYS B CA 8533 C C . CYS B 177 ? 1.7252 1.1484 1.8779 -0.2331 -0.3323 0.0495 177 CYS B C 8534 O O . CYS B 177 ? 1.7960 1.2365 2.0060 -0.2289 -0.3529 0.0544 177 CYS B O 8535 C CB . CYS B 177 ? 1.3605 0.7441 1.4285 -0.2243 -0.3388 0.0625 177 CYS B CB 8536 S SG . CYS B 177 ? 2.3686 1.7725 2.5078 -0.2099 -0.3533 0.0699 177 CYS B SG 8537 N N . TYR B 178 ? 1.6832 1.1026 1.8217 -0.2448 -0.3269 0.0435 178 TYR B N 8538 C CA . TYR B 178 ? 1.3499 0.7901 1.5435 -0.2535 -0.3393 0.0410 178 TYR B CA 8539 C C . TYR B 178 ? 1.4121 0.8288 1.5669 -0.2704 -0.3662 0.0431 178 TYR B C 8540 O O . TYR B 178 ? 1.5892 1.0091 1.7686 -0.2775 -0.4009 0.0496 178 TYR B O 8541 C CB . TYR B 178 ? 1.3634 0.8242 1.5835 -0.2538 -0.3054 0.0311 178 TYR B CB 8542 C CG . TYR B 178 ? 1.6340 1.1249 1.9258 -0.2608 -0.3123 0.0279 178 TYR B CG 8543 C CD1 . TYR B 178 ? 1.7217 1.2477 2.0890 -0.2520 -0.3095 0.0256 178 TYR B CD1 8544 C CD2 . TYR B 178 ? 1.7794 1.2644 2.0666 -0.2765 -0.3203 0.0257 178 TYR B CD2 8545 C CE1 . TYR B 178 ? 1.7719 1.3282 2.2091 -0.2588 -0.3139 0.0215 178 TYR B CE1 8546 C CE2 . TYR B 178 ? 1.7886 1.3025 2.1436 -0.2840 -0.3261 0.0230 178 TYR B CE2 8547 C CZ . TYR B 178 ? 1.8319 1.3824 2.2622 -0.2751 -0.3224 0.0210 178 TYR B CZ 8548 O OH . TYR B 178 ? 1.9079 1.4897 2.4097 -0.2830 -0.3266 0.0171 178 TYR B OH 8549 N N . ASP B 179 ? 1.3876 0.7802 1.4826 -0.2771 -0.3503 0.0369 179 ASP B N 8550 C CA . ASP B 179 ? 1.6249 0.9911 1.6733 -0.2939 -0.3707 0.0348 179 ASP B CA 8551 C C . ASP B 179 ? 1.6567 1.0023 1.6634 -0.2989 -0.4023 0.0439 179 ASP B C 8552 O O . ASP B 179 ? 1.6216 0.9485 1.5938 -0.3151 -0.4262 0.0431 179 ASP B O 8553 C CB . ASP B 179 ? 1.7599 1.1029 1.7534 -0.2969 -0.3436 0.0250 179 ASP B CB 8554 C CG . ASP B 179 ? 1.6637 0.9975 1.6208 -0.2834 -0.3186 0.0255 179 ASP B CG 8555 O OD1 . ASP B 179 ? 1.5992 0.9108 1.5038 -0.2845 -0.3277 0.0281 179 ASP B OD1 8556 O OD2 . ASP B 179 ? 1.6321 0.9815 1.6122 -0.2731 -0.2899 0.0235 179 ASP B OD2 8557 N N . MET B 180 ? 1.7101 1.0588 1.7189 -0.2864 -0.4024 0.0526 180 MET B N 8558 C CA . MET B 180 ? 1.6545 0.9854 1.6287 -0.2913 -0.4333 0.0650 180 MET B CA 8559 C C . MET B 180 ? 1.7163 1.0634 1.7468 -0.2957 -0.4732 0.0763 180 MET B C 8560 O O . MET B 180 ? 1.7296 1.0627 1.7367 -0.3031 -0.5066 0.0896 180 MET B O 8561 C CB . MET B 180 ? 1.4685 0.7961 1.4287 -0.2766 -0.4187 0.0710 180 MET B CB 8562 C CG . MET B 180 ? 1.4479 0.7738 1.3862 -0.2667 -0.3753 0.0599 180 MET B CG 8563 S SD . MET B 180 ? 2.1019 1.3993 1.9625 -0.2642 -0.3642 0.0632 180 MET B SD 8564 C CE . MET B 180 ? 1.4263 0.7313 1.3199 -0.2556 -0.3892 0.0810 180 MET B CE 8565 N N . LYS B 181 ? 1.7210 1.0983 1.8269 -0.2918 -0.4695 0.0716 181 LYS B N 8566 C CA . LYS B 181 ? 1.7276 1.1259 1.9022 -0.2946 -0.5049 0.0803 181 LYS B CA 8567 C C . LYS B 181 ? 1.5943 0.9980 1.7995 -0.2826 -0.5239 0.0948 181 LYS B C 8568 O O . LYS B 181 ? 1.6044 1.0068 1.8286 -0.2890 -0.5659 0.1089 181 LYS B O 8569 C CB . LYS B 181 ? 1.7802 1.1616 1.9232 -0.3165 -0.5421 0.0842 181 LYS B CB 8570 C CG . LYS B 181 ? 1.8156 1.1835 1.9168 -0.3296 -0.5245 0.0690 181 LYS B CG 8571 C CD . LYS B 181 ? 1.9294 1.2890 2.0214 -0.3513 -0.5619 0.0701 181 LYS B CD 8572 C CE . LYS B 181 ? 2.0404 1.4342 2.2245 -0.3522 -0.5758 0.0704 181 LYS B CE 8573 N NZ . LYS B 181 ? 1.9894 1.4004 2.2072 -0.3478 -0.5372 0.0559 181 LYS B NZ 8574 N N . THR B 182 ? 1.5451 0.9539 1.7556 -0.2657 -0.4938 0.0916 182 THR B N 8575 C CA . THR B 182 ? 1.5002 0.9146 1.7466 -0.2521 -0.5060 0.1028 182 THR B CA 8576 C C . THR B 182 ? 1.4348 0.8732 1.7269 -0.2334 -0.4658 0.0906 182 THR B C 8577 O O . THR B 182 ? 1.5612 1.0129 1.8579 -0.2329 -0.4327 0.0760 182 THR B O 8578 C CB . THR B 182 ? 1.5560 0.9360 1.7256 -0.2558 -0.5188 0.1161 182 THR B CB 8579 O OG1 . THR B 182 ? 1.6992 1.0836 1.9103 -0.2434 -0.5345 0.1289 182 THR B OG1 8580 C CG2 . THR B 182 ? 1.6321 0.9960 1.7342 -0.2526 -0.4782 0.1055 182 THR B CG2 8581 N N . THR B 183 ? 1.3854 0.8285 1.7105 -0.2193 -0.4690 0.0965 183 THR B N 8582 C CA . THR B 183 ? 1.3270 0.7939 1.6980 -0.2026 -0.4323 0.0831 183 THR B CA 8583 C C . THR B 183 ? 1.3204 0.7695 1.6520 -0.1923 -0.4177 0.0861 183 THR B C 8584 O O . THR B 183 ? 1.3820 0.8149 1.7089 -0.1900 -0.4444 0.1011 183 THR B O 8585 C CB . THR B 183 ? 1.4655 0.9660 1.9442 -0.1923 -0.4436 0.0804 183 THR B CB 8586 O OG1 . THR B 183 ? 1.8148 1.3032 2.3136 -0.1880 -0.4817 0.0978 183 THR B OG1 8587 C CG2 . THR B 183 ? 1.3680 0.8906 1.8945 -0.2024 -0.4560 0.0763 183 THR B CG2 8588 N N . CYS B 184 ? 1.3831 0.8350 1.6868 -0.1873 -0.3763 0.0730 184 CYS B N 8589 C CA . CYS B 184 ? 1.3995 0.8420 1.6801 -0.1761 -0.3571 0.0723 184 CYS B CA 8590 C C . CYS B 184 ? 1.3680 0.8407 1.6966 -0.1648 -0.3192 0.0541 184 CYS B C 8591 O O . CYS B 184 ? 1.3157 0.8162 1.6965 -0.1661 -0.3099 0.0437 184 CYS B O 8592 C CB . CYS B 184 ? 1.3026 0.7146 1.4881 -0.1831 -0.3450 0.0752 184 CYS B CB 8593 S SG . CYS B 184 ? 1.5555 0.9701 1.7014 -0.1905 -0.3107 0.0612 184 CYS B SG 8594 N N . LEU B 185 ? 1.2351 0.7029 1.5452 -0.1552 -0.2971 0.0499 185 LEU B N 8595 C CA . LEU B 185 ? 1.2544 0.7507 1.6091 -0.1455 -0.2629 0.0322 185 LEU B CA 8596 C C . LEU B 185 ? 1.1970 0.6888 1.4929 -0.1480 -0.2273 0.0245 185 LEU B C 8597 O O . LEU B 185 ? 1.2028 0.6667 1.4288 -0.1520 -0.2289 0.0328 185 LEU B O 8598 C CB . LEU B 185 ? 1.3818 0.8810 1.7795 -0.1316 -0.2667 0.0310 185 LEU B CB 8599 C CG . LEU B 185 ? 1.3638 0.8348 1.7089 -0.1271 -0.2673 0.0396 185 LEU B CG 8600 C CD1 . LEU B 185 ? 1.2631 0.7464 1.6625 -0.1129 -0.2570 0.0297 185 LEU B CD1 8601 C CD2 . LEU B 185 ? 1.2866 0.7269 1.5974 -0.1335 -0.3067 0.0620 185 LEU B CD2 8602 N N . PRO B 186 ? 1.2666 0.7864 1.5916 -0.1466 -0.1955 0.0087 186 PRO B N 8603 C CA . PRO B 186 ? 1.3754 0.8934 1.6496 -0.1506 -0.1636 0.0030 186 PRO B CA 8604 C C . PRO B 186 ? 1.3761 0.8712 1.5962 -0.1449 -0.1563 0.0071 186 PRO B C 8605 O O . PRO B 186 ? 1.5401 1.0343 1.7806 -0.1352 -0.1603 0.0061 186 PRO B O 8606 C CB . PRO B 186 ? 1.3502 0.9047 1.6761 -0.1487 -0.1342 -0.0143 186 PRO B CB 8607 C CG . PRO B 186 ? 1.2845 0.8613 1.6854 -0.1484 -0.1501 -0.0180 186 PRO B CG 8608 C CD . PRO B 186 ? 1.3051 0.8612 1.7144 -0.1425 -0.1877 -0.0048 186 PRO B CD 8609 N N . MET B 187 ? 1.2931 0.7700 1.4488 -0.1508 -0.1460 0.0112 187 MET B N 8610 C CA . MET B 187 ? 1.3147 0.7699 1.4182 -0.1466 -0.1396 0.0155 187 MET B CA 8611 C C . MET B 187 ? 1.3096 0.7812 1.4267 -0.1390 -0.1132 0.0045 187 MET B C 8612 O O . MET B 187 ? 1.3339 0.8328 1.4868 -0.1398 -0.0940 -0.0072 187 MET B O 8613 C CB . MET B 187 ? 1.1646 0.5996 1.2046 -0.1545 -0.1330 0.0202 187 MET B CB 8614 C CG . MET B 187 ? 1.1562 0.6064 1.1946 -0.1593 -0.1076 0.0133 187 MET B CG 8615 S SD . MET B 187 ? 1.7328 1.1561 1.7022 -0.1656 -0.1004 0.0187 187 MET B SD 8616 C CE . MET B 187 ? 1.1495 0.5557 1.0810 -0.1570 -0.0963 0.0216 187 MET B CE 8617 N N . PHE B 188 ? 1.2034 0.6585 1.2909 -0.1333 -0.1121 0.0080 188 PHE B N 8618 C CA . PHE B 188 ? 1.3372 0.8044 1.4338 -0.1265 -0.0900 -0.0024 188 PHE B CA 8619 C C . PHE B 188 ? 1.3217 0.7678 1.3587 -0.1260 -0.0821 0.0032 188 PHE B C 8620 O O . PHE B 188 ? 1.4313 0.8521 1.4317 -0.1277 -0.0984 0.0150 188 PHE B O 8621 C CB . PHE B 188 ? 1.4395 0.9133 1.5895 -0.1171 -0.1009 -0.0068 188 PHE B CB 8622 C CG . PHE B 188 ? 1.3334 0.7835 1.4809 -0.1158 -0.1341 0.0086 188 PHE B CG 8623 C CD1 . PHE B 188 ? 1.2555 0.6796 1.3601 -0.1144 -0.1418 0.0191 188 PHE B CD1 8624 C CD2 . PHE B 188 ? 1.4161 0.8707 1.6035 -0.1174 -0.1583 0.0136 188 PHE B CD2 8625 C CE1 . PHE B 188 ? 1.1674 0.5693 1.2647 -0.1160 -0.1727 0.0351 188 PHE B CE1 8626 C CE2 . PHE B 188 ? 1.3449 0.7772 1.5263 -0.1184 -0.1914 0.0299 188 PHE B CE2 8627 C CZ . PHE B 188 ? 1.1908 0.5963 1.3249 -0.1183 -0.1984 0.0412 188 PHE B CZ 8628 N N . GLY B 189 ? 1.1856 0.6431 1.2124 -0.1250 -0.0572 -0.0053 189 GLY B N 8629 C CA . GLY B 189 ? 1.3018 0.7423 1.2786 -0.1242 -0.0495 -0.0006 189 GLY B CA 8630 C C . GLY B 189 ? 1.4328 0.8582 1.4091 -0.1175 -0.0608 0.0032 189 GLY B C 8631 O O . GLY B 189 ? 1.4698 0.8712 1.4095 -0.1190 -0.0732 0.0146 189 GLY B O 8632 N N . TYR B 190 ? 1.3851 0.8245 1.4034 -0.1111 -0.0561 -0.0070 190 TYR B N 8633 C CA . TYR B 190 ? 1.2307 0.6557 1.2591 -0.1047 -0.0691 -0.0033 190 TYR B CA 8634 C C . TYR B 190 ? 1.2676 0.7080 1.3642 -0.0978 -0.0748 -0.0133 190 TYR B C 8635 O O . TYR B 190 ? 1.1778 0.6433 1.3078 -0.0960 -0.0552 -0.0308 190 TYR B O 8636 C CB . TYR B 190 ? 1.1624 0.5826 1.1625 -0.1029 -0.0531 -0.0067 190 TYR B CB 8637 C CG . TYR B 190 ? 1.2791 0.6890 1.3009 -0.0963 -0.0626 -0.0064 190 TYR B CG 8638 C CD1 . TYR B 190 ? 1.1321 0.5172 1.1438 -0.0964 -0.0872 0.0100 190 TYR B CD1 8639 C CD2 . TYR B 190 ? 1.4234 0.8476 1.4748 -0.0913 -0.0471 -0.0226 190 TYR B CD2 8640 C CE1 . TYR B 190 ? 1.1459 0.5195 1.1786 -0.0914 -0.0973 0.0126 190 TYR B CE1 8641 C CE2 . TYR B 190 ? 1.1836 0.5963 1.2582 -0.0854 -0.0562 -0.0228 190 TYR B CE2 8642 C CZ . TYR B 190 ? 1.2122 0.5991 1.2785 -0.0852 -0.0818 -0.0041 190 TYR B CZ 8643 O OH . TYR B 190 ? 1.2461 0.6197 1.3367 -0.0801 -0.0923 -0.0020 190 TYR B OH 8644 N N . LYS B 191 ? 1.3039 0.7290 1.4214 -0.0945 -0.1016 -0.0024 191 LYS B N 8645 C CA . LYS B 191 ? 1.1760 0.6134 1.3658 -0.0868 -0.1115 -0.0102 191 LYS B CA 8646 C C . LYS B 191 ? 1.3010 0.7188 1.5030 -0.0805 -0.1262 -0.0036 191 LYS B C 8647 O O . LYS B 191 ? 1.4627 0.8544 1.6371 -0.0836 -0.1503 0.0166 191 LYS B O 8648 C CB . LYS B 191 ? 1.1760 0.6159 1.3949 -0.0891 -0.1353 -0.0017 191 LYS B CB 8649 C CG . LYS B 191 ? 1.1868 0.6460 1.4911 -0.0809 -0.1428 -0.0125 191 LYS B CG 8650 C CD . LYS B 191 ? 1.1938 0.6609 1.5273 -0.0847 -0.1633 -0.0058 191 LYS B CD 8651 C CE . LYS B 191 ? 1.1680 0.6049 1.4649 -0.0904 -0.1983 0.0199 191 LYS B CE 8652 N NZ . LYS B 191 ? 1.2131 0.6575 1.5405 -0.0948 -0.2216 0.0267 191 LYS B NZ 8653 N N . HIS B 192 ? 1.1515 0.5814 1.3929 -0.0731 -0.1111 -0.0211 192 HIS B N 8654 C CA . HIS B 192 ? 1.1495 0.5618 1.4144 -0.0664 -0.1247 -0.0170 192 HIS B CA 8655 C C . HIS B 192 ? 1.2331 0.6531 1.5808 -0.0578 -0.1428 -0.0214 192 HIS B C 8656 O O . HIS B 192 ? 1.3130 0.7602 1.7158 -0.0526 -0.1257 -0.0445 192 HIS B O 8657 C CB . HIS B 192 ? 1.2093 0.6274 1.4692 -0.0637 -0.0986 -0.0346 192 HIS B CB 8658 C CG . HIS B 192 ? 1.5869 0.9902 1.8849 -0.0561 -0.1100 -0.0353 192 HIS B CG 8659 N ND1 . HIS B 192 ? 1.5167 0.8890 1.8001 -0.0570 -0.1381 -0.0111 192 HIS B ND1 8660 C CD2 . HIS B 192 ? 1.4924 0.9067 1.8431 -0.0485 -0.0972 -0.0575 192 HIS B CD2 8661 C CE1 . HIS B 192 ? 1.4523 0.8159 1.7794 -0.0498 -0.1434 -0.0165 192 HIS B CE1 8662 N NE2 . HIS B 192 ? 1.3737 0.7623 1.7437 -0.0439 -0.1186 -0.0458 192 HIS B NE2 8663 N N . VAL B 193 ? 1.3760 0.7727 1.7336 -0.0572 -0.1777 0.0008 193 VAL B N 8664 C CA . VAL B 193 ? 1.6094 1.0117 2.0497 -0.0488 -0.2004 0.0004 193 VAL B CA 8665 C C . VAL B 193 ? 1.3288 0.7169 1.8148 -0.0395 -0.2096 -0.0013 193 VAL B C 8666 O O . VAL B 193 ? 1.4374 0.8443 1.9948 -0.0295 -0.1974 -0.0246 193 VAL B O 8667 C CB . VAL B 193 ? 1.4921 0.8794 1.9246 -0.0548 -0.2383 0.0272 193 VAL B CB 8668 C CG1 . VAL B 193 ? 1.2679 0.6225 1.6169 -0.0657 -0.2529 0.0530 193 VAL B CG1 8669 C CG2 . VAL B 193 ? 1.5229 0.9079 2.0401 -0.0459 -0.2697 0.0335 193 VAL B CG2 8670 N N . LEU B 194 ? 1.3908 0.7459 1.8373 -0.0436 -0.2300 0.0224 194 LEU B N 8671 C CA . LEU B 194 ? 1.5305 0.8676 2.0211 -0.0360 -0.2437 0.0252 194 LEU B CA 8672 C C . LEU B 194 ? 1.2761 0.6011 1.7227 -0.0381 -0.2226 0.0197 194 LEU B C 8673 O O . LEU B 194 ? 1.2570 0.5635 1.6280 -0.0484 -0.2239 0.0373 194 LEU B O 8674 C CB . LEU B 194 ? 1.5169 0.8236 2.0082 -0.0400 -0.2889 0.0598 194 LEU B CB 8675 C CG . LEU B 194 ? 1.3881 0.6707 1.9218 -0.0338 -0.3076 0.0684 194 LEU B CG 8676 C CD1 . LEU B 194 ? 1.4974 0.7991 2.1375 -0.0176 -0.3028 0.0428 194 LEU B CD1 8677 C CD2 . LEU B 194 ? 1.3778 0.6285 1.8981 -0.0418 -0.3536 0.1073 194 LEU B CD2 8678 N N . THR B 195 ? 1.2255 0.5620 1.7219 -0.0289 -0.2029 -0.0063 195 THR B N 8679 C CA . THR B 195 ? 1.3818 0.7069 1.8466 -0.0307 -0.1854 -0.0129 195 THR B CA 8680 C C . THR B 195 ? 1.6011 0.8895 2.0678 -0.0317 -0.2155 0.0128 195 THR B C 8681 O O . THR B 195 ? 1.5267 0.8022 2.0424 -0.0276 -0.2476 0.0286 195 THR B O 8682 C CB . THR B 195 ? 1.2023 0.5502 1.7205 -0.0221 -0.1560 -0.0503 195 THR B CB 8683 O OG1 . THR B 195 ? 1.2881 0.6227 1.7765 -0.0247 -0.1428 -0.0554 195 THR B OG1 8684 C CG2 . THR B 195 ? 1.2585 0.6084 1.8774 -0.0093 -0.1718 -0.0603 195 THR B CG2 8685 N N . LEU B 196 ? 1.4227 0.6947 1.8370 -0.0383 -0.2060 0.0182 196 LEU B N 8686 C CA . LEU B 196 ? 1.3264 0.5626 1.7291 -0.0430 -0.2323 0.0455 196 LEU B CA 8687 C C . LEU B 196 ? 1.3615 0.5851 1.8518 -0.0322 -0.2527 0.0435 196 LEU B C 8688 O O . LEU B 196 ? 1.4681 0.7039 2.0111 -0.0226 -0.2336 0.0142 196 LEU B O 8689 C CB . LEU B 196 ? 1.2370 0.4637 1.5809 -0.0508 -0.2124 0.0445 196 LEU B CB 8690 C CG . LEU B 196 ? 1.2232 0.4478 1.4755 -0.0640 -0.2040 0.0593 196 LEU B CG 8691 C CD1 . LEU B 196 ? 1.2095 0.4374 1.4211 -0.0681 -0.1760 0.0471 196 LEU B CD1 8692 C CD2 . LEU B 196 ? 1.2580 0.4523 1.4736 -0.0751 -0.2353 0.0959 196 LEU B CD2 8693 N N . THR B 197 ? 1.2798 0.4845 1.7821 -0.0344 -0.2901 0.0742 197 THR B N 8694 C CA . THR B 197 ? 1.3501 0.5589 1.9285 -0.0237 -0.3095 0.0758 197 THR B CA 8695 C C . THR B 197 ? 1.5077 0.6933 2.0567 -0.0330 -0.3414 0.1137 197 THR B C 8696 O O . THR B 197 ? 1.5676 0.7370 2.0431 -0.0477 -0.3529 0.1403 197 THR B O 8697 C CB . THR B 197 ? 1.4073 0.6358 2.0610 -0.0131 -0.3250 0.0693 197 THR B CB 8698 O OG1 . THR B 197 ? 1.4509 0.6830 2.1805 -0.0031 -0.3466 0.0730 197 THR B OG1 8699 C CG2 . THR B 197 ? 1.3498 0.5698 1.9636 -0.0232 -0.3517 0.0984 197 THR B CG2 8700 N N . ASP B 198 ? 1.3589 0.5437 1.9661 -0.0254 -0.3548 0.1151 198 ASP B N 8701 C CA . ASP B 198 ? 1.4061 0.5699 1.9938 -0.0347 -0.3858 0.1505 198 ASP B CA 8702 C C . ASP B 198 ? 1.4501 0.6155 2.0762 -0.0342 -0.4269 0.1746 198 ASP B C 8703 O O . ASP B 198 ? 1.5180 0.6680 2.1375 -0.0423 -0.4578 0.2051 198 ASP B O 8704 C CB . ASP B 198 ? 1.5981 0.7576 2.2269 -0.0286 -0.3811 0.1417 198 ASP B CB 8705 C CG . ASP B 198 ? 1.6881 0.8686 2.4225 -0.0099 -0.3805 0.1149 198 ASP B CG 8706 O OD1 . ASP B 198 ? 1.6932 0.8958 2.4626 -0.0006 -0.3654 0.0896 198 ASP B OD1 8707 O OD2 . ASP B 198 ? 1.7110 0.8868 2.4949 -0.0051 -0.3943 0.1186 198 ASP B OD2 8708 N N . GLN B 199 ? 1.4078 0.5924 2.0751 -0.0258 -0.4276 0.1610 199 GLN B N 8709 C CA . GLN B 199 ? 1.4753 0.6636 2.1811 -0.0258 -0.4670 0.1824 199 GLN B CA 8710 C C . GLN B 199 ? 1.5651 0.7453 2.1969 -0.0404 -0.4778 0.2025 199 GLN B C 8711 O O . GLN B 199 ? 1.4593 0.6509 2.0803 -0.0383 -0.4576 0.1842 199 GLN B O 8712 C CB . GLN B 199 ? 1.4112 0.6280 2.2222 -0.0071 -0.4638 0.1545 199 GLN B CB 8713 C CG . GLN B 199 ? 1.5204 0.7475 2.4095 0.0074 -0.4516 0.1304 199 GLN B CG 8714 C CD . GLN B 199 ? 1.8616 1.0727 2.7719 0.0043 -0.4855 0.1581 199 GLN B CD 8715 O OE1 . GLN B 199 ? 2.1227 1.3249 3.0293 -0.0039 -0.5255 0.1915 199 GLN B OE1 8716 N NE2 . GLN B 199 ? 1.8966 1.1036 2.8282 0.0094 -0.4705 0.1444 199 GLN B NE2 8717 N N . VAL B 200 ? 1.6302 0.7908 2.2110 -0.0567 -0.5097 0.2396 200 VAL B N 8718 C CA . VAL B 200 ? 1.5814 0.7316 2.0824 -0.0737 -0.5202 0.2593 200 VAL B CA 8719 C C . VAL B 200 ? 1.6540 0.8162 2.1988 -0.0713 -0.5490 0.2656 200 VAL B C 8720 O O . VAL B 200 ? 1.7249 0.8837 2.2179 -0.0818 -0.5522 0.2723 200 VAL B O 8721 C CB . VAL B 200 ? 1.7144 0.8399 2.1389 -0.0949 -0.5418 0.2951 200 VAL B CB 8722 C CG1 . VAL B 200 ? 1.6062 0.7208 1.9876 -0.0982 -0.5122 0.2886 200 VAL B CG1 8723 C CG2 . VAL B 200 ? 1.8079 0.9297 2.2823 -0.0966 -0.5862 0.3209 200 VAL B CG2 8724 N N . THR B 201 ? 1.6928 0.8693 2.3353 -0.0578 -0.5700 0.2627 201 THR B N 8725 C CA . THR B 201 ? 1.7220 0.9143 2.4225 -0.0530 -0.5953 0.2645 201 THR B CA 8726 C C . THR B 201 ? 1.6959 0.9089 2.4227 -0.0411 -0.5606 0.2292 201 THR B C 8727 O O . THR B 201 ? 1.7546 0.9745 2.4807 -0.0443 -0.5700 0.2306 201 THR B O 8728 C CB . THR B 201 ? 1.6480 0.8531 2.4562 -0.0408 -0.6247 0.2677 201 THR B CB 8729 O OG1 . THR B 201 ? 1.7198 0.9393 2.5943 -0.0223 -0.5939 0.2351 201 THR B OG1 8730 C CG2 . THR B 201 ? 1.8699 1.0538 2.6522 -0.0553 -0.6635 0.3057 201 THR B CG2 8731 N N . ARG B 202 ? 1.5267 0.7491 2.2744 -0.0291 -0.5206 0.1975 202 ARG B N 8732 C CA . ARG B 202 ? 1.6082 0.8506 2.3771 -0.0197 -0.4827 0.1612 202 ARG B CA 8733 C C . ARG B 202 ? 1.6610 0.8923 2.3366 -0.0341 -0.4690 0.1655 202 ARG B C 8734 O O . ARG B 202 ? 1.4576 0.7037 2.1454 -0.0311 -0.4494 0.1444 202 ARG B O 8735 C CB . ARG B 202 ? 1.5285 0.7790 2.3213 -0.0086 -0.4438 0.1293 202 ARG B CB 8736 C CG . ARG B 202 ? 1.6425 0.9147 2.4555 -0.0008 -0.4019 0.0895 202 ARG B CG 8737 C CD . ARG B 202 ? 1.6810 0.9804 2.5835 0.0100 -0.4080 0.0738 202 ARG B CD 8738 N NE . ARG B 202 ? 1.6989 1.0205 2.6141 0.0142 -0.3661 0.0361 202 ARG B NE 8739 C CZ . ARG B 202 ? 1.6240 0.9775 2.5739 0.0164 -0.3601 0.0229 202 ARG B CZ 8740 N NH1 . ARG B 202 ? 1.6906 1.0423 2.6786 0.0162 -0.3989 0.0447 202 ARG B NH1 8741 N NH2 . ARG B 202 ? 1.5522 0.9396 2.4977 0.0175 -0.3162 -0.0111 202 ARG B NH2 8742 N N . PHE B 203 ? 1.6013 0.8072 2.1856 -0.0510 -0.4795 0.1926 203 PHE B N 8743 C CA . PHE B 203 ? 1.4240 0.6172 1.9156 -0.0664 -0.4688 0.1987 203 PHE B CA 8744 C C . PHE B 203 ? 1.5519 0.7468 2.0396 -0.0745 -0.4983 0.2148 203 PHE B C 8745 O O . PHE B 203 ? 1.4055 0.6271 1.8865 -0.0735 -0.4785 0.1960 203 PHE B O 8746 C CB . PHE B 203 ? 1.5076 0.6755 1.9073 -0.0826 -0.4698 0.2211 203 PHE B CB 8747 C CG . PHE B 203 ? 1.4076 0.5670 1.7102 -0.0988 -0.4561 0.2254 203 PHE B CG 8748 C CD1 . PHE B 203 ? 1.4414 0.5886 1.6941 -0.1153 -0.4849 0.2507 203 PHE B CD1 8749 C CD2 . PHE B 203 ? 1.5092 0.6823 1.7683 -0.0975 -0.4118 0.2015 203 PHE B CD2 8750 C CE1 . PHE B 203 ? 1.5150 0.6637 1.6789 -0.1294 -0.4673 0.2493 203 PHE B CE1 8751 C CE2 . PHE B 203 ? 1.3711 0.5457 1.5447 -0.1107 -0.3960 0.2023 203 PHE B CE2 8752 C CZ . PHE B 203 ? 1.4043 0.5665 1.5313 -0.1263 -0.4226 0.2250 203 PHE B CZ 8753 N N . ASN B 204 ? 1.6721 0.8542 2.1566 -0.0833 -0.5410 0.2468 204 ASN B N 8754 C CA . ASN B 204 ? 1.5709 0.7507 2.0493 -0.0936 -0.5761 0.2663 204 ASN B CA 8755 C C . ASN B 204 ? 1.5126 0.7182 2.0818 -0.0792 -0.5773 0.2464 204 ASN B C 8756 O O . ASN B 204 ? 1.5100 0.7286 2.0624 -0.0867 -0.5859 0.2480 204 ASN B O 8757 C CB . ASN B 204 ? 1.7447 0.9130 2.2251 -0.1032 -0.6231 0.3012 204 ASN B CB 8758 C CG . ASN B 204 ? 1.8413 0.9865 2.2398 -0.1180 -0.6212 0.3203 204 ASN B CG 8759 O OD1 . ASN B 204 ? 1.8458 0.9866 2.2058 -0.1163 -0.5842 0.3052 204 ASN B OD1 8760 N ND2 . ASN B 204 ? 1.8289 0.9603 2.2015 -0.1339 -0.6613 0.3535 204 ASN B ND2 8761 N N . GLU B 205 ? 1.6338 0.8606 2.2957 -0.0591 -0.5626 0.2228 205 GLU B N 8762 C CA . GLU B 205 ? 1.7039 0.9610 2.4598 -0.0448 -0.5578 0.1993 205 GLU B CA 8763 C C . GLU B 205 ? 1.6569 0.9454 2.3760 -0.0459 -0.5128 0.1693 205 GLU B C 8764 O O . GLU B 205 ? 1.5402 0.8517 2.2824 -0.0469 -0.5167 0.1632 205 GLU B O 8765 C CB . GLU B 205 ? 1.5283 0.8048 2.3859 -0.0241 -0.5457 0.1764 205 GLU B CB 8766 C CG . GLU B 205 ? 1.7202 0.9956 2.6337 -0.0206 -0.5871 0.1991 205 GLU B CG 8767 C CD . GLU B 205 ? 1.8506 1.1466 2.8617 -0.0009 -0.5714 0.1732 205 GLU B CD 8768 O OE1 . GLU B 205 ? 1.6999 0.9960 2.7646 0.0026 -0.6028 0.1888 205 GLU B OE1 8769 O OE2 . GLU B 205 ? 1.9185 1.2304 2.9521 0.0096 -0.5277 0.1366 205 GLU B OE2 8770 N N . GLU B 206 ? 1.7400 1.0288 2.4033 -0.0464 -0.4717 0.1519 206 GLU B N 8771 C CA . GLU B 206 ? 1.6678 0.9841 2.2948 -0.0479 -0.4287 0.1250 206 GLU B CA 8772 C C . GLU B 206 ? 1.6487 0.9573 2.1855 -0.0656 -0.4352 0.1410 206 GLU B C 8773 O O . GLU B 206 ? 1.4964 0.8285 2.0238 -0.0680 -0.4166 0.1260 206 GLU B O 8774 C CB . GLU B 206 ? 1.5700 0.8877 2.1660 -0.0439 -0.3866 0.1038 206 GLU B CB 8775 C CG . GLU B 206 ? 1.7225 1.0552 2.4087 -0.0268 -0.3709 0.0781 206 GLU B CG 8776 C CD . GLU B 206 ? 1.8106 1.1803 2.5820 -0.0171 -0.3624 0.0543 206 GLU B CD 8777 O OE1 . GLU B 206 ? 1.7102 1.1060 2.4575 -0.0210 -0.3335 0.0364 206 GLU B OE1 8778 O OE2 . GLU B 206 ? 1.7541 1.1270 2.6188 -0.0060 -0.3851 0.0540 206 GLU B OE2 8779 N N . VAL B 207 ? 1.6597 0.9349 2.1302 -0.0790 -0.4606 0.1708 207 VAL B N 8780 C CA . VAL B 207 ? 1.5254 0.7905 1.9180 -0.0970 -0.4743 0.1876 207 VAL B CA 8781 C C . VAL B 207 ? 1.6367 0.9109 2.0827 -0.0985 -0.5116 0.1987 207 VAL B C 8782 O O . VAL B 207 ? 1.8210 1.0964 2.3505 -0.0885 -0.5381 0.2053 207 VAL B O 8783 C CB . VAL B 207 ? 1.5493 0.7771 1.8596 -0.1129 -0.4924 0.2162 207 VAL B CB 8784 C CG1 . VAL B 207 ? 1.8027 1.0206 2.0330 -0.1329 -0.5057 0.2306 207 VAL B CG1 8785 C CG2 . VAL B 207 ? 1.3753 0.5967 1.6404 -0.1111 -0.4554 0.2044 207 VAL B CG2 8786 N N . LYS B 208 ? 1.5653 0.8468 1.9683 -0.1102 -0.5130 0.1989 208 LYS B N 8787 C CA . LYS B 208 ? 1.8163 1.1087 2.2612 -0.1143 -0.5465 0.2077 208 LYS B CA 8788 C C . LYS B 208 ? 1.8709 1.2020 2.4133 -0.0981 -0.5293 0.1809 208 LYS B C 8789 O O . LYS B 208 ? 2.1137 1.4620 2.6912 -0.1010 -0.5459 0.1807 208 LYS B O 8790 C CB . LYS B 208 ? 1.8100 1.0789 2.2808 -0.1192 -0.6013 0.2411 208 LYS B CB 8791 C CG . LYS B 208 ? 1.8611 1.0918 2.2352 -0.1382 -0.6199 0.2697 208 LYS B CG 8792 C CD . LYS B 208 ? 2.0360 1.2445 2.4352 -0.1458 -0.6779 0.3055 208 LYS B CD 8793 C CE . LYS B 208 ? 2.0673 1.2842 2.4771 -0.1566 -0.7131 0.3164 208 LYS B CE 8794 N NZ . LYS B 208 ? 2.1557 1.3495 2.5835 -0.1666 -0.7735 0.3547 208 LYS B NZ 8795 N N . LYS B 209 ? 1.4998 0.8454 2.0848 -0.0825 -0.4954 0.1573 209 LYS B N 8796 C CA . LYS B 209 ? 1.4153 0.8002 2.0661 -0.0712 -0.4638 0.1256 209 LYS B CA 8797 C C . LYS B 209 ? 1.5061 0.8997 2.0805 -0.0803 -0.4270 0.1115 209 LYS B C 8798 O O . LYS B 209 ? 1.6178 1.0388 2.2140 -0.0812 -0.4112 0.0954 209 LYS B O 8799 C CB . LYS B 209 ? 1.3716 0.7687 2.0889 -0.0537 -0.4390 0.1034 209 LYS B CB 8800 C CG . LYS B 209 ? 1.4551 0.8541 2.2788 -0.0407 -0.4701 0.1085 209 LYS B CG 8801 C CD . LYS B 209 ? 1.4646 0.8840 2.3614 -0.0235 -0.4368 0.0766 209 LYS B CD 8802 C CE . LYS B 209 ? 1.6373 1.0580 2.6483 -0.0090 -0.4665 0.0791 209 LYS B CE 8803 N NZ . LYS B 209 ? 1.5698 0.9493 2.5664 -0.0098 -0.5028 0.1097 209 LYS B NZ 8804 N N . GLN B 210 ? 1.5873 0.9567 2.0741 -0.0875 -0.4144 0.1186 210 GLN B N 8805 C CA . GLN B 210 ? 1.6296 1.0010 2.0381 -0.0967 -0.3835 0.1091 210 GLN B CA 8806 C C . GLN B 210 ? 1.5305 0.8945 1.8940 -0.1122 -0.4049 0.1228 210 GLN B C 8807 O O . GLN B 210 ? 1.5699 0.9160 1.9294 -0.1200 -0.4455 0.1459 210 GLN B O 8808 C CB . GLN B 210 ? 1.5594 0.9065 1.8936 -0.0999 -0.3675 0.1140 210 GLN B CB 8809 C CG . GLN B 210 ? 1.3905 0.7462 1.7577 -0.0864 -0.3395 0.0962 210 GLN B CG 8810 C CD . GLN B 210 ? 1.4914 0.8791 1.8758 -0.0811 -0.2984 0.0671 210 GLN B CD 8811 O OE1 . GLN B 210 ? 1.6819 1.0774 2.0245 -0.0892 -0.2838 0.0626 210 GLN B OE1 8812 N NE2 . GLN B 210 ? 1.4382 0.8438 1.8841 -0.0686 -0.2797 0.0471 210 GLN B NE2 8813 N N . SER B 211 ? 1.5057 0.8828 1.8351 -0.1177 -0.3785 0.1086 211 SER B N 8814 C CA . SER B 211 ? 1.5800 0.9492 1.8623 -0.1331 -0.3943 0.1178 211 SER B CA 8815 C C . SER B 211 ? 1.5243 0.8890 1.7309 -0.1402 -0.3614 0.1076 211 SER B C 8816 O O . SER B 211 ? 1.5228 0.8924 1.7160 -0.1333 -0.3280 0.0947 211 SER B O 8817 C CB . SER B 211 ? 1.4592 0.8548 1.8100 -0.1326 -0.4068 0.1117 211 SER B CB 8818 O OG . SER B 211 ? 1.4692 0.8971 1.8918 -0.1191 -0.3790 0.0893 211 SER B OG 8819 N N . VAL B 212 ? 1.3375 0.6931 1.4980 -0.1544 -0.3723 0.1129 212 VAL B N 8820 C CA . VAL B 212 ? 1.3240 0.6676 1.4071 -0.1629 -0.3482 0.1069 212 VAL B CA 8821 C C . VAL B 212 ? 1.3854 0.7508 1.4815 -0.1634 -0.3235 0.0894 212 VAL B C 8822 O O . VAL B 212 ? 1.7595 1.1425 1.9040 -0.1652 -0.3357 0.0868 212 VAL B O 8823 C CB . VAL B 212 ? 1.5067 0.8215 1.5209 -0.1803 -0.3747 0.1229 212 VAL B CB 8824 C CG1 . VAL B 212 ? 1.4027 0.7147 1.3696 -0.1912 -0.3607 0.1130 212 VAL B CG1 8825 C CG2 . VAL B 212 ? 1.6068 0.8958 1.5661 -0.1831 -0.3755 0.1345 212 VAL B CG2 8826 N N . SER B 213 ? 1.2696 0.6340 1.3249 -0.1626 -0.2899 0.0787 213 SER B N 8827 C CA . SER B 213 ? 1.3287 0.7096 1.3881 -0.1651 -0.2667 0.0650 213 SER B CA 8828 C C . SER B 213 ? 1.3865 0.7463 1.3756 -0.1771 -0.2626 0.0656 213 SER B C 8829 O O . SER B 213 ? 1.4210 0.7552 1.3571 -0.1843 -0.2764 0.0749 213 SER B O 8830 C CB . SER B 213 ? 1.3374 0.7372 1.4146 -0.1548 -0.2305 0.0512 213 SER B CB 8831 O OG . SER B 213 ? 1.2413 0.6565 1.3222 -0.1591 -0.2099 0.0408 213 SER B OG 8832 N N . ARG B 214 ? 1.3243 0.6949 1.3141 -0.1802 -0.2430 0.0552 214 ARG B N 8833 C CA . ARG B 214 ? 1.4316 0.7828 1.3637 -0.1907 -0.2376 0.0531 214 ARG B CA 8834 C C . ARG B 214 ? 1.5007 0.8566 1.4165 -0.1868 -0.2028 0.0436 214 ARG B C 8835 O O . ARG B 214 ? 1.4892 0.8686 1.4441 -0.1805 -0.1844 0.0373 214 ARG B O 8836 C CB . ARG B 214 ? 1.4340 0.7876 1.3802 -0.2021 -0.2556 0.0524 214 ARG B CB 8837 C CG . ARG B 214 ? 1.3779 0.7067 1.2639 -0.2146 -0.2565 0.0499 214 ARG B CG 8838 C CD . ARG B 214 ? 1.5222 0.8565 1.4287 -0.2254 -0.2685 0.0461 214 ARG B CD 8839 N NE . ARG B 214 ? 1.3980 0.7069 1.2488 -0.2381 -0.2707 0.0414 214 ARG B NE 8840 C CZ . ARG B 214 ? 1.4297 0.7369 1.2865 -0.2495 -0.2797 0.0363 214 ARG B CZ 8841 N NH1 . ARG B 214 ? 1.4711 0.8019 1.3872 -0.2502 -0.2874 0.0367 214 ARG B NH1 8842 N NH2 . ARG B 214 ? 1.5900 0.8724 1.3954 -0.2607 -0.2802 0.0295 214 ARG B NH2 8843 N N . ASN B 215 ? 1.5065 0.8401 1.3649 -0.1917 -0.1946 0.0424 215 ASN B N 8844 C CA . ASN B 215 ? 1.3947 0.7286 1.2344 -0.1884 -0.1654 0.0356 215 ASN B CA 8845 C C . ASN B 215 ? 1.3974 0.7136 1.2035 -0.1986 -0.1647 0.0313 215 ASN B C 8846 O O . ASN B 215 ? 1.7356 1.0381 1.5257 -0.2085 -0.1856 0.0324 215 ASN B O 8847 C CB . ASN B 215 ? 1.3166 0.6413 1.1256 -0.1811 -0.1527 0.0373 215 ASN B CB 8848 C CG . ASN B 215 ? 1.3045 0.6362 1.1082 -0.1756 -0.1240 0.0318 215 ASN B CG 8849 O OD1 . ASN B 215 ? 1.2312 0.5500 0.9993 -0.1733 -0.1125 0.0314 215 ASN B OD1 8850 N ND2 . ASN B 215 ? 1.6233 0.9762 1.4628 -0.1748 -0.1129 0.0283 215 ASN B ND2 8851 N N . ARG B 216 ? 1.2226 0.5386 1.0197 -0.1971 -0.1420 0.0262 216 ARG B N 8852 C CA . ARG B 216 ? 1.2346 0.5323 1.0055 -0.2058 -0.1404 0.0207 216 ARG B CA 8853 C C . ARG B 216 ? 1.3440 0.6188 1.0651 -0.2051 -0.1300 0.0168 216 ARG B C 8854 O O . ARG B 216 ? 1.3702 0.6245 1.0572 -0.2136 -0.1404 0.0126 216 ARG B O 8855 C CB . ARG B 216 ? 1.2712 0.5807 1.0681 -0.2067 -0.1251 0.0185 216 ARG B CB 8856 C CG . ARG B 216 ? 1.7349 1.0233 1.5098 -0.2152 -0.1240 0.0126 216 ARG B CG 8857 C CD . ARG B 216 ? 1.7444 1.0433 1.5499 -0.2193 -0.1151 0.0133 216 ARG B CD 8858 N NE . ARG B 216 ? 1.5575 0.8627 1.3899 -0.2294 -0.1320 0.0125 216 ARG B NE 8859 C CZ . ARG B 216 ? 1.4401 0.7716 1.3177 -0.2309 -0.1315 0.0162 216 ARG B CZ 8860 N NH1 . ARG B 216 ? 1.5999 0.9531 1.4970 -0.2238 -0.1142 0.0198 216 ARG B NH1 8861 N NH2 . ARG B 216 ? 1.2387 0.5759 1.1424 -0.2406 -0.1477 0.0151 216 ARG B NH2 8862 N N . ASP B 217 ? 1.4457 0.7250 1.1633 -0.1960 -0.1092 0.0171 217 ASP B N 8863 C CA . ASP B 217 ? 1.3199 0.5806 0.9977 -0.1943 -0.0971 0.0126 217 ASP B CA 8864 C C . ASP B 217 ? 1.3016 0.5561 0.9535 -0.1926 -0.1025 0.0159 217 ASP B C 8865 O O . ASP B 217 ? 1.3063 0.5746 0.9765 -0.1864 -0.1053 0.0227 217 ASP B O 8866 C CB . ASP B 217 ? 1.2507 0.5189 0.9376 -0.1861 -0.0748 0.0128 217 ASP B CB 8867 C CG . ASP B 217 ? 1.2882 0.5748 0.9896 -0.1769 -0.0672 0.0187 217 ASP B CG 8868 O OD1 . ASP B 217 ? 1.5409 0.8403 1.2625 -0.1759 -0.0777 0.0224 217 ASP B OD1 8869 O OD2 . ASP B 217 ? 1.4525 0.7407 1.1475 -0.1707 -0.0512 0.0191 217 ASP B OD2 8870 N N . ALA B 218 ? 1.4974 0.7307 1.1070 -0.1991 -0.1026 0.0101 218 ALA B N 8871 C CA . ALA B 218 ? 1.4059 0.6297 0.9828 -0.2023 -0.1095 0.0139 218 ALA B CA 8872 C C . ALA B 218 ? 1.3318 0.5654 0.9147 -0.1918 -0.0986 0.0203 218 ALA B C 8873 O O . ALA B 218 ? 1.4881 0.7235 1.0711 -0.1920 -0.1115 0.0292 218 ALA B O 8874 C CB . ALA B 218 ? 1.3213 0.5227 0.8505 -0.2117 -0.1034 0.0033 218 ALA B CB 8875 N N . PRO B 219 ? 1.3291 0.5682 0.9177 -0.1833 -0.0765 0.0164 219 PRO B N 8876 C CA . PRO B 219 ? 1.3410 0.5898 0.9357 -0.1747 -0.0681 0.0221 219 PRO B CA 8877 C C . PRO B 219 ? 1.4942 0.7628 1.1293 -0.1684 -0.0752 0.0287 219 PRO B C 8878 O O . PRO B 219 ? 1.2098 0.4919 0.8748 -0.1663 -0.0724 0.0272 219 PRO B O 8879 C CB . PRO B 219 ? 1.3004 0.5523 0.8970 -0.1679 -0.0457 0.0168 219 PRO B CB 8880 C CG . PRO B 219 ? 1.5659 0.8031 1.1474 -0.1739 -0.0423 0.0075 219 PRO B CG 8881 C CD . PRO B 219 ? 1.7208 0.9563 1.3111 -0.1814 -0.0603 0.0081 219 PRO B CD 8882 N N . GLU B 220 ? 1.3282 0.5985 0.9657 -0.1663 -0.0834 0.0354 220 GLU B N 8883 C CA . GLU B 220 ? 1.3783 0.6668 1.0578 -0.1598 -0.0894 0.0392 220 GLU B CA 8884 C C . GLU B 220 ? 1.3683 0.6647 1.0536 -0.1515 -0.0758 0.0397 220 GLU B C 8885 O O . GLU B 220 ? 2.0039 1.2897 1.6699 -0.1523 -0.0794 0.0445 220 GLU B O 8886 C CB . GLU B 220 ? 1.3583 0.6413 1.0454 -0.1643 -0.1152 0.0470 220 GLU B CB 8887 C CG . GLU B 220 ? 1.3456 0.6151 1.0126 -0.1759 -0.1321 0.0476 220 GLU B CG 8888 C CD . GLU B 220 ? 1.4541 0.7369 1.1558 -0.1767 -0.1365 0.0435 220 GLU B CD 8889 O OE1 . GLU B 220 ? 1.7300 1.0090 1.4376 -0.1841 -0.1589 0.0472 220 GLU B OE1 8890 O OE2 . GLU B 220 ? 1.5520 0.8491 1.2744 -0.1713 -0.1186 0.0375 220 GLU B OE2 8891 N N . GLY B 221 ? 1.2056 0.5203 0.9154 -0.1453 -0.0606 0.0350 221 GLY B N 8892 C CA . GLY B 221 ? 1.4904 0.8125 1.2027 -0.1388 -0.0475 0.0341 221 GLY B CA 8893 C C . GLY B 221 ? 1.5539 0.8800 1.2889 -0.1350 -0.0576 0.0369 221 GLY B C 8894 O O . GLY B 221 ? 1.3607 0.7013 1.1338 -0.1323 -0.0627 0.0342 221 GLY B O 8895 N N . GLY B 222 ? 1.4366 0.7499 1.1509 -0.1351 -0.0597 0.0416 222 GLY B N 8896 C CA . GLY B 222 ? 1.1887 0.5025 0.9242 -0.1314 -0.0686 0.0451 222 GLY B CA 8897 C C . GLY B 222 ? 1.2688 0.5907 1.0072 -0.1259 -0.0516 0.0404 222 GLY B C 8898 O O . GLY B 222 ? 1.3771 0.7017 1.1377 -0.1218 -0.0547 0.0401 222 GLY B O 8899 N N . PHE B 223 ? 1.2451 0.5704 0.9630 -0.1263 -0.0348 0.0365 223 PHE B N 8900 C CA . PHE B 223 ? 1.1382 0.4715 0.8556 -0.1226 -0.0197 0.0327 223 PHE B CA 8901 C C . PHE B 223 ? 1.1782 0.5329 0.9312 -0.1180 -0.0131 0.0241 223 PHE B C 8902 O O . PHE B 223 ? 1.3012 0.6626 1.0635 -0.1151 -0.0060 0.0198 223 PHE B O 8903 C CB . PHE B 223 ? 1.1788 0.5115 0.8710 -0.1240 -0.0058 0.0316 223 PHE B CB 8904 C CG . PHE B 223 ? 1.0998 0.4133 0.7577 -0.1287 -0.0072 0.0362 223 PHE B CG 8905 C CD1 . PHE B 223 ? 1.1211 0.4192 0.7663 -0.1331 -0.0203 0.0426 223 PHE B CD1 8906 C CD2 . PHE B 223 ? 1.4611 0.7722 1.1006 -0.1295 0.0048 0.0339 223 PHE B CD2 8907 C CE1 . PHE B 223 ? 1.1441 0.4259 0.7538 -0.1401 -0.0194 0.0457 223 PHE B CE1 8908 C CE2 . PHE B 223 ? 1.2870 0.5824 0.8970 -0.1345 0.0067 0.0348 223 PHE B CE2 8909 C CZ . PHE B 223 ? 1.1546 0.4359 0.7470 -0.1407 -0.0044 0.0402 223 PHE B CZ 8910 N N . ASP B 224 ? 1.1673 0.5334 0.9402 -0.1187 -0.0145 0.0206 224 ASP B N 8911 C CA . ASP B 224 ? 1.2032 0.5908 1.0131 -0.1161 -0.0083 0.0108 224 ASP B CA 8912 C C . ASP B 224 ? 1.1946 0.5796 1.0333 -0.1115 -0.0187 0.0087 224 ASP B C 8913 O O . ASP B 224 ? 1.1737 0.5706 1.0343 -0.1082 -0.0102 -0.0009 224 ASP B O 8914 C CB . ASP B 224 ? 1.2257 0.6251 1.0538 -0.1190 -0.0094 0.0083 224 ASP B CB 8915 C CG . ASP B 224 ? 1.3180 0.7267 1.1301 -0.1236 0.0047 0.0078 224 ASP B CG 8916 O OD1 . ASP B 224 ? 1.2132 0.6160 0.9979 -0.1239 0.0122 0.0111 224 ASP B OD1 8917 O OD2 . ASP B 224 ? 1.4863 0.9084 1.3155 -0.1273 0.0076 0.0050 224 ASP B OD2 8918 N N . ALA B 225 ? 1.1644 0.5329 1.0030 -0.1121 -0.0381 0.0180 225 ALA B N 8919 C CA . ALA B 225 ? 1.2289 0.5915 1.0979 -0.1080 -0.0528 0.0197 225 ALA B CA 8920 C C . ALA B 225 ? 1.3876 0.7386 1.2432 -0.1067 -0.0505 0.0225 225 ALA B C 8921 O O . ALA B 225 ? 1.4557 0.8121 1.3431 -0.1018 -0.0489 0.0152 225 ALA B O 8922 C CB . ALA B 225 ? 1.3449 0.6915 1.2120 -0.1114 -0.0771 0.0323 225 ALA B CB 8923 N N . ILE B 226 ? 1.2362 0.5716 1.0467 -0.1117 -0.0493 0.0317 226 ILE B N 8924 C CA . ILE B 226 ? 1.1707 0.4951 0.9655 -0.1123 -0.0463 0.0354 226 ILE B CA 8925 C C . ILE B 226 ? 1.1678 0.5089 0.9776 -0.1081 -0.0283 0.0224 226 ILE B C 8926 O O . ILE B 226 ? 1.4408 0.7788 1.2666 -0.1058 -0.0290 0.0200 226 ILE B O 8927 C CB . ILE B 226 ? 1.1109 0.4214 0.8562 -0.1190 -0.0424 0.0439 226 ILE B CB 8928 C CG1 . ILE B 226 ? 1.2518 0.5441 0.9761 -0.1258 -0.0605 0.0560 226 ILE B CG1 8929 C CG2 . ILE B 226 ? 1.1959 0.4985 0.9283 -0.1204 -0.0368 0.0468 226 ILE B CG2 8930 C CD1 . ILE B 226 ? 1.2613 0.5401 0.9368 -0.1339 -0.0547 0.0614 226 ILE B CD1 8931 N N . MET B 227 ? 1.0847 0.4427 0.8886 -0.1084 -0.0132 0.0144 227 MET B N 8932 C CA . MET B 227 ? 1.0775 0.4529 0.8902 -0.1071 0.0032 0.0024 227 MET B CA 8933 C C . MET B 227 ? 1.1148 0.5025 0.9715 -0.1030 0.0038 -0.0107 227 MET B C 8934 O O . MET B 227 ? 1.4338 0.8252 1.3021 -0.1016 0.0101 -0.0194 227 MET B O 8935 C CB . MET B 227 ? 1.2518 0.6422 1.0498 -0.1100 0.0160 -0.0006 227 MET B CB 8936 C CG . MET B 227 ? 1.2323 0.6430 1.0381 -0.1112 0.0311 -0.0126 227 MET B CG 8937 S SD . MET B 227 ? 1.2242 0.6292 1.0164 -0.1114 0.0356 -0.0130 227 MET B SD 8938 C CE . MET B 227 ? 1.0571 0.4487 0.8104 -0.1135 0.0349 0.0016 227 MET B CE 8939 N N . GLN B 228 ? 1.1557 0.5503 1.0396 -0.1013 -0.0024 -0.0136 228 GLN B N 8940 C CA . GLN B 228 ? 1.2882 0.6979 1.2204 -0.0971 0.0006 -0.0290 228 GLN B CA 8941 C C . GLN B 228 ? 1.2842 0.6788 1.2448 -0.0919 -0.0133 -0.0275 228 GLN B C 8942 O O . GLN B 228 ? 1.1572 0.5591 1.1466 -0.0887 -0.0059 -0.0420 228 GLN B O 8943 C CB . GLN B 228 ? 1.1241 0.5466 1.0824 -0.0970 -0.0024 -0.0320 228 GLN B CB 8944 C CG . GLN B 228 ? 1.1622 0.6049 1.1052 -0.1029 0.0150 -0.0381 228 GLN B CG 8945 C CD . GLN B 228 ? 1.1623 0.6224 1.1031 -0.1057 0.0353 -0.0530 228 GLN B CD 8946 O OE1 . GLN B 228 ? 1.1079 0.5830 1.0849 -0.1040 0.0435 -0.0703 228 GLN B OE1 8947 N NE2 . GLN B 228 ? 1.1905 0.6491 1.0900 -0.1106 0.0432 -0.0471 228 GLN B NE2 8948 N N . ALA B 229 ? 1.3721 0.7447 1.3234 -0.0921 -0.0339 -0.0099 229 ALA B N 8949 C CA . ALA B 229 ? 1.3112 0.6662 1.2885 -0.0885 -0.0511 -0.0038 229 ALA B CA 8950 C C . ALA B 229 ? 1.2417 0.5885 1.2074 -0.0891 -0.0437 -0.0060 229 ALA B C 8951 O O . ALA B 229 ? 1.5688 0.9065 1.5672 -0.0854 -0.0518 -0.0081 229 ALA B O 8952 C CB . ALA B 229 ? 1.2437 0.5758 1.2008 -0.0923 -0.0749 0.0185 229 ALA B CB 8953 N N . THR B 230 ? 1.1771 0.5268 1.0995 -0.0941 -0.0292 -0.0053 230 THR B N 8954 C CA . THR B 230 ? 1.1860 0.5302 1.0954 -0.0959 -0.0216 -0.0071 230 THR B CA 8955 C C . THR B 230 ? 1.2744 0.6374 1.2105 -0.0935 -0.0054 -0.0295 230 THR B C 8956 O O . THR B 230 ? 1.7156 1.0718 1.6733 -0.0918 -0.0068 -0.0356 230 THR B O 8957 C CB . THR B 230 ? 1.1933 0.5357 1.0514 -0.1020 -0.0124 0.0013 230 THR B CB 8958 O OG1 . THR B 230 ? 1.2071 0.5308 1.0377 -0.1060 -0.0255 0.0196 230 THR B OG1 8959 C CG2 . THR B 230 ? 1.3191 0.6585 1.1673 -0.1045 -0.0045 -0.0011 230 THR B CG2 8960 N N . VAL B 231 ? 1.1023 0.4884 1.0360 -0.0946 0.0096 -0.0418 231 VAL B N 8961 C CA . VAL B 231 ? 1.1358 0.5419 1.0815 -0.0961 0.0275 -0.0630 231 VAL B CA 8962 C C . VAL B 231 ? 1.1289 0.5491 1.1264 -0.0918 0.0318 -0.0834 231 VAL B C 8963 O O . VAL B 231 ? 1.3256 0.7614 1.3370 -0.0938 0.0469 -0.1044 231 VAL B O 8964 C CB . VAL B 231 ? 1.1807 0.6049 1.0921 -0.1025 0.0422 -0.0646 231 VAL B CB 8965 C CG1 . VAL B 231 ? 1.3232 0.7349 1.1909 -0.1056 0.0388 -0.0465 231 VAL B CG1 8966 C CG2 . VAL B 231 ? 1.1207 0.5578 1.0405 -0.1027 0.0437 -0.0653 231 VAL B CG2 8967 N N . CYS B 232 ? 1.1138 0.5293 1.1409 -0.0865 0.0185 -0.0780 232 CYS B N 8968 C CA . CYS B 232 ? 1.2732 0.7035 1.3570 -0.0814 0.0218 -0.0969 232 CYS B CA 8969 C C . CYS B 232 ? 1.3605 0.7759 1.4910 -0.0742 0.0104 -0.1022 232 CYS B C 8970 O O . CYS B 232 ? 1.3709 0.7938 1.5580 -0.0678 0.0080 -0.1152 232 CYS B O 8971 C CB . CYS B 232 ? 1.4179 0.8532 1.5166 -0.0795 0.0123 -0.0889 232 CYS B CB 8972 S SG . CYS B 232 ? 1.1657 0.6263 1.2324 -0.0880 0.0310 -0.0927 232 CYS B SG 8973 N N . ASP B 233 ? 1.6260 1.0206 1.7358 -0.0755 0.0036 -0.0921 233 ASP B N 8974 C CA . ASP B 233 ? 1.5842 0.9551 1.7281 -0.0702 -0.0144 -0.0861 233 ASP B CA 8975 C C . ASP B 233 ? 1.3453 0.7234 1.5616 -0.0619 -0.0135 -0.1087 233 ASP B C 8976 O O . ASP B 233 ? 1.3431 0.7037 1.6012 -0.0554 -0.0347 -0.0994 233 ASP B O 8977 C CB . ASP B 233 ? 1.6021 0.9594 1.7173 -0.0750 -0.0111 -0.0830 233 ASP B CB 8978 C CG . ASP B 233 ? 1.6196 0.9987 1.7220 -0.0797 0.0140 -0.1067 233 ASP B CG 8979 O OD1 . ASP B 233 ? 1.3930 0.7972 1.5070 -0.0800 0.0294 -0.1253 233 ASP B OD1 8980 O OD2 . ASP B 233 ? 1.9704 1.3422 2.0508 -0.0844 0.0178 -0.1064 233 ASP B OD2 8981 N N . GLU B 234 ? 1.1926 0.5960 1.4246 -0.0630 0.0108 -0.1382 234 GLU B N 8982 C CA . GLU B 234 ? 1.2100 0.6255 1.5138 -0.0556 0.0165 -0.1645 234 GLU B CA 8983 C C . GLU B 234 ? 1.2224 0.6412 1.5679 -0.0485 0.0014 -0.1566 234 GLU B C 8984 O O . GLU B 234 ? 1.1818 0.5932 1.5929 -0.0392 -0.0119 -0.1616 234 GLU B O 8985 C CB . GLU B 234 ? 1.4920 0.9395 1.7945 -0.0615 0.0482 -0.1972 234 GLU B CB 8986 C CG . GLU B 234 ? 1.6462 1.1136 2.0220 -0.0552 0.0597 -0.2281 234 GLU B CG 8987 C CD . GLU B 234 ? 1.8470 1.3010 2.2790 -0.0480 0.0571 -0.2468 234 GLU B CD 8988 O OE1 . GLU B 234 ? 1.8887 1.3180 2.3001 -0.0490 0.0466 -0.2353 234 GLU B OE1 8989 O OE2 . GLU B 234 ? 1.8694 1.3379 2.3693 -0.0416 0.0663 -0.2741 234 GLU B OE2 8990 N N . LYS B 235 ? 1.4889 0.9183 1.7988 -0.0531 0.0020 -0.1437 235 LYS B N 8991 C CA . LYS B 235 ? 1.4703 0.9060 1.8157 -0.0484 -0.0115 -0.1367 235 LYS B CA 8992 C C . LYS B 235 ? 1.2600 0.6653 1.6109 -0.0443 -0.0464 -0.1064 235 LYS B C 8993 O O . LYS B 235 ? 1.3754 0.7777 1.7872 -0.0364 -0.0643 -0.1052 235 LYS B O 8994 C CB . LYS B 235 ? 1.4818 0.9366 1.7844 -0.0563 -0.0001 -0.1321 235 LYS B CB 8995 C CG . LYS B 235 ? 1.2461 0.7202 1.5954 -0.0531 -0.0026 -0.1376 235 LYS B CG 8996 C CD . LYS B 235 ? 1.3736 0.8772 1.7793 -0.0510 0.0218 -0.1730 235 LYS B CD 8997 C CE . LYS B 235 ? 1.2806 0.8049 1.7423 -0.0475 0.0192 -0.1794 235 LYS B CE 8998 N NZ . LYS B 235 ? 1.2572 0.8130 1.7758 -0.0464 0.0465 -0.2165 235 LYS B NZ 8999 N N . ILE B 236 ? 1.1373 0.5209 1.4254 -0.0507 -0.0564 -0.0818 236 ILE B N 9000 C CA . ILE B 236 ? 1.2369 0.5925 1.5174 -0.0508 -0.0885 -0.0514 236 ILE B CA 9001 C C . ILE B 236 ? 1.5180 0.8470 1.8227 -0.0476 -0.1046 -0.0438 236 ILE B C 9002 O O . ILE B 236 ? 1.5477 0.8526 1.8593 -0.0477 -0.1340 -0.0193 236 ILE B O 9003 C CB . ILE B 236 ? 1.2659 0.6110 1.4671 -0.0609 -0.0909 -0.0290 236 ILE B CB 9004 C CG1 . ILE B 236 ? 1.2006 0.5251 1.3587 -0.0662 -0.0898 -0.0186 236 ILE B CG1 9005 C CG2 . ILE B 236 ? 1.2353 0.6060 1.4057 -0.0652 -0.0671 -0.0408 236 ILE B CG2 9006 C CD1 . ILE B 236 ? 1.3198 0.6147 1.4498 -0.0717 -0.1165 0.0120 236 ILE B CD1 9007 N N . GLY B 237 ? 1.4689 0.8019 1.7861 -0.0460 -0.0864 -0.0645 237 GLY B N 9008 C CA . GLY B 237 ? 1.4857 0.7960 1.8401 -0.0419 -0.0992 -0.0631 237 GLY B CA 9009 C C . GLY B 237 ? 1.6329 0.9121 1.9419 -0.0494 -0.1142 -0.0363 237 GLY B C 9010 O O . GLY B 237 ? 1.8649 1.1182 2.2005 -0.0478 -0.1406 -0.0177 237 GLY B O 9011 N N . TRP B 238 ? 1.4010 0.6828 1.6442 -0.0583 -0.0978 -0.0337 238 TRP B N 9012 C CA . TRP B 238 ? 1.3019 0.5580 1.5043 -0.0665 -0.1066 -0.0125 238 TRP B CA 9013 C C . TRP B 238 ? 1.2805 0.5233 1.5221 -0.0639 -0.1070 -0.0229 238 TRP B C 9014 O O . TRP B 238 ? 1.2901 0.5499 1.5556 -0.0603 -0.0861 -0.0523 238 TRP B O 9015 C CB . TRP B 238 ? 1.3526 0.6187 1.4855 -0.0754 -0.0864 -0.0117 238 TRP B CB 9016 C CG . TRP B 238 ? 1.3537 0.6253 1.4391 -0.0801 -0.0878 0.0029 238 TRP B CG 9017 C CD1 . TRP B 238 ? 1.2154 0.5117 1.2798 -0.0803 -0.0696 -0.0091 238 TRP B CD1 9018 C CD2 . TRP B 238 ? 1.3290 0.5800 1.3804 -0.0869 -0.1084 0.0317 238 TRP B CD2 9019 N NE1 . TRP B 238 ? 1.2285 0.5201 1.2520 -0.0854 -0.0775 0.0093 238 TRP B NE1 9020 C CE2 . TRP B 238 ? 1.2375 0.5022 1.2507 -0.0899 -0.1005 0.0333 238 TRP B CE2 9021 C CE3 . TRP B 238 ? 1.3576 0.5796 1.4056 -0.0922 -0.1328 0.0565 238 TRP B CE3 9022 C CZ2 . TRP B 238 ? 1.1699 0.4206 1.1424 -0.0976 -0.1150 0.0558 238 TRP B CZ2 9023 C CZ3 . TRP B 238 ? 1.3923 0.6013 1.3957 -0.1013 -0.1474 0.0805 238 TRP B CZ3 9024 C CH2 . TRP B 238 ? 1.3309 0.5546 1.2972 -0.1037 -0.1379 0.0784 238 TRP B CH2 9025 N N . ARG B 239 ? 1.5063 0.7180 1.7525 -0.0673 -0.1307 0.0012 239 ARG B N 9026 C CA . ARG B 239 ? 1.6271 0.8215 1.9011 -0.0675 -0.1319 -0.0043 239 ARG B CA 9027 C C . ARG B 239 ? 1.6572 0.8550 1.8755 -0.0774 -0.1120 -0.0071 239 ARG B C 9028 O O . ARG B 239 ? 1.5470 0.7431 1.7042 -0.0865 -0.1109 0.0119 239 ARG B O 9029 C CB . ARG B 239 ? 1.4412 0.5996 1.7326 -0.0705 -0.1649 0.0266 239 ARG B CB 9030 C CG . ARG B 239 ? 1.3685 0.5277 1.7267 -0.0591 -0.1866 0.0292 239 ARG B CG 9031 C CD . ARG B 239 ? 1.3999 0.5395 1.7475 -0.0650 -0.2165 0.0664 239 ARG B CD 9032 N NE . ARG B 239 ? 1.6314 0.7747 2.0474 -0.0540 -0.2393 0.0702 239 ARG B NE 9033 C CZ . ARG B 239 ? 1.8065 0.9443 2.2693 -0.0492 -0.2493 0.0705 239 ARG B CZ 9034 N NH1 . ARG B 239 ? 1.8736 1.0011 2.3203 -0.0548 -0.2380 0.0670 239 ARG B NH1 9035 N NH2 . ARG B 239 ? 1.6596 0.8022 2.1880 -0.0389 -0.2717 0.0745 239 ARG B NH2 9036 N N . ASN B 240 ? 1.6935 0.8966 1.9348 -0.0760 -0.0965 -0.0316 240 ASN B N 9037 C CA . ASN B 240 ? 1.6277 0.8350 1.8222 -0.0856 -0.0795 -0.0346 240 ASN B CA 9038 C C . ASN B 240 ? 1.4609 0.6378 1.6412 -0.0948 -0.0944 -0.0099 240 ASN B C 9039 O O . ASN B 240 ? 1.4884 0.6663 1.6219 -0.1047 -0.0846 -0.0029 240 ASN B O 9040 C CB . ASN B 240 ? 1.4852 0.7114 1.7048 -0.0830 -0.0573 -0.0714 240 ASN B CB 9041 C CG . ASN B 240 ? 1.6327 0.8467 1.9265 -0.0748 -0.0646 -0.0889 240 ASN B CG 9042 O OD1 . ASN B 240 ? 1.9991 1.1865 2.3262 -0.0718 -0.0888 -0.0699 240 ASN B OD1 9043 N ND2 . ASN B 240 ? 1.4645 0.6976 1.7851 -0.0721 -0.0442 -0.1254 240 ASN B ND2 9044 N N . ASP B 241 ? 1.6467 0.7969 1.8699 -0.0921 -0.1186 0.0043 241 ASP B N 9045 C CA . ASP B 241 ? 1.4408 0.5596 1.6566 -0.1021 -0.1347 0.0291 241 ASP B CA 9046 C C . ASP B 241 ? 1.4294 0.5346 1.5990 -0.1113 -0.1529 0.0672 241 ASP B C 9047 O O . ASP B 241 ? 1.7692 0.8598 1.9238 -0.1202 -0.1636 0.0906 241 ASP B O 9048 C CB . ASP B 241 ? 1.6029 0.7183 1.8814 -0.0931 -0.1455 0.0232 241 ASP B CB 9049 C CG . ASP B 241 ? 1.7632 0.8843 2.0866 -0.0809 -0.1630 0.0266 241 ASP B CG 9050 O OD1 . ASP B 241 ? 1.4539 0.5678 1.7537 -0.0843 -0.1815 0.0551 241 ASP B OD1 9051 O OD2 . ASP B 241 ? 1.8225 0.9566 2.2060 -0.0684 -0.1579 -0.0004 241 ASP B OD2 9052 N N . ALA B 242 ? 1.6253 0.7416 1.7694 -0.1097 -0.1536 0.0720 242 ALA B N 9053 C CA . ALA B 242 ? 1.5988 0.6995 1.7088 -0.1178 -0.1751 0.1054 242 ALA B CA 9054 C C . ALA B 242 ? 1.3714 0.4839 1.4075 -0.1277 -0.1612 0.1135 242 ALA B C 9055 O O . ALA B 242 ? 1.4045 0.5424 1.4210 -0.1248 -0.1358 0.0928 242 ALA B O 9056 C CB . ALA B 242 ? 1.6211 0.7283 1.7715 -0.1067 -0.1926 0.1063 242 ALA B CB 9057 N N . SER B 243 ? 1.4233 0.5174 1.4188 -0.1400 -0.1782 0.1439 243 SER B N 9058 C CA . SER B 243 ? 1.6285 0.7326 1.5564 -0.1495 -0.1665 0.1514 243 SER B CA 9059 C C . SER B 243 ? 1.5156 0.6369 1.4433 -0.1412 -0.1675 0.1437 243 SER B C 9060 O O . SER B 243 ? 1.8376 0.9486 1.7872 -0.1389 -0.1917 0.1559 243 SER B O 9061 C CB . SER B 243 ? 1.7192 0.7973 1.6015 -0.1682 -0.1833 0.1849 243 SER B CB 9062 O OG . SER B 243 ? 1.6378 0.7254 1.4571 -0.1775 -0.1711 0.1893 243 SER B OG 9063 N N . HIS B 244 ? 1.2938 0.4410 1.1983 -0.1375 -0.1426 0.1247 244 HIS B N 9064 C CA . HIS B 244 ? 1.4495 0.6153 1.3575 -0.1295 -0.1403 0.1143 244 HIS B CA 9065 C C . HIS B 244 ? 1.5041 0.6683 1.3539 -0.1395 -0.1416 0.1285 244 HIS B C 9066 O O . HIS B 244 ? 1.6626 0.8339 1.4679 -0.1460 -0.1226 0.1262 244 HIS B O 9067 C CB . HIS B 244 ? 1.4255 0.6205 1.3458 -0.1199 -0.1136 0.0850 244 HIS B CB 9068 C CG . HIS B 244 ? 1.2819 0.4810 1.2530 -0.1119 -0.1077 0.0661 244 HIS B CG 9069 N ND1 . HIS B 244 ? 1.4899 0.7108 1.4629 -0.1085 -0.0834 0.0423 244 HIS B ND1 9070 C CD2 . HIS B 244 ? 1.3754 0.5594 1.3982 -0.1074 -0.1234 0.0668 244 HIS B CD2 9071 C CE1 . HIS B 244 ? 1.6746 0.8941 1.6952 -0.1029 -0.0830 0.0272 244 HIS B CE1 9072 N NE2 . HIS B 244 ? 1.7306 0.9275 1.7846 -0.1014 -0.1065 0.0410 244 HIS B NE2 9073 N N . LEU B 245 ? 1.2859 0.4413 1.1384 -0.1408 -0.1640 0.1420 245 LEU B N 9074 C CA . LEU B 245 ? 1.2978 0.4522 1.0967 -0.1507 -0.1658 0.1524 245 LEU B CA 9075 C C . LEU B 245 ? 1.4229 0.5950 1.2388 -0.1417 -0.1665 0.1405 245 LEU B C 9076 O O . LEU B 245 ? 1.4782 0.6504 1.3414 -0.1340 -0.1848 0.1410 245 LEU B O 9077 C CB . LEU B 245 ? 1.3458 0.4724 1.1182 -0.1656 -0.1934 0.1821 245 LEU B CB 9078 C CG . LEU B 245 ? 1.6929 0.7974 1.4537 -0.1769 -0.1994 0.1996 245 LEU B CG 9079 C CD1 . LEU B 245 ? 1.5853 0.6649 1.3029 -0.1959 -0.2242 0.2300 245 LEU B CD1 9080 C CD2 . LEU B 245 ? 1.7837 0.8977 1.5137 -0.1809 -0.1689 0.1886 245 LEU B CD2 9081 N N . LEU B 246 ? 1.4219 0.6093 1.2028 -0.1428 -0.1467 0.1299 246 LEU B N 9082 C CA . LEU B 246 ? 1.3640 0.5673 1.1544 -0.1368 -0.1462 0.1200 246 LEU B CA 9083 C C . LEU B 246 ? 1.3610 0.5551 1.0994 -0.1489 -0.1537 0.1322 246 LEU B C 9084 O O . LEU B 246 ? 1.3737 0.5698 1.0667 -0.1554 -0.1358 0.1289 246 LEU B O 9085 C CB . LEU B 246 ? 1.2203 0.4492 1.0175 -0.1282 -0.1178 0.0967 246 LEU B CB 9086 C CG . LEU B 246 ? 1.1852 0.4319 0.9910 -0.1232 -0.1139 0.0861 246 LEU B CG 9087 C CD1 . LEU B 246 ? 1.4071 0.6565 1.2659 -0.1164 -0.1332 0.0858 246 LEU B CD1 9088 C CD2 . LEU B 246 ? 1.1520 0.4221 0.9629 -0.1168 -0.0872 0.0661 246 LEU B CD2 9089 N N . VAL B 247 ? 1.2877 0.4722 1.0349 -0.1522 -0.1803 0.1450 247 VAL B N 9090 C CA . VAL B 247 ? 1.6111 0.7843 1.3065 -0.1663 -0.1907 0.1570 247 VAL B CA 9091 C C . VAL B 247 ? 1.6398 0.8292 1.3381 -0.1620 -0.1861 0.1443 247 VAL B C 9092 O O . VAL B 247 ? 1.4925 0.6922 1.2378 -0.1531 -0.1976 0.1400 247 VAL B O 9093 C CB . VAL B 247 ? 1.5250 0.6752 1.2182 -0.1768 -0.2264 0.1825 247 VAL B CB 9094 C CG1 . VAL B 247 ? 1.4563 0.6100 1.2217 -0.1641 -0.2474 0.1836 247 VAL B CG1 9095 C CG2 . VAL B 247 ? 1.8384 0.9809 1.4841 -0.1909 -0.2394 0.1912 247 VAL B CG2 9096 N N . PHE B 248 ? 1.5786 0.7700 1.2287 -0.1689 -0.1687 0.1379 248 PHE B N 9097 C CA . PHE B 248 ? 1.4422 0.6481 1.0919 -0.1654 -0.1598 0.1244 248 PHE B CA 9098 C C . PHE B 248 ? 1.4277 0.6203 1.0360 -0.1796 -0.1758 0.1334 248 PHE B C 9099 O O . PHE B 248 ? 1.4942 0.6740 1.0485 -0.1926 -0.1698 0.1374 248 PHE B O 9100 C CB . PHE B 248 ? 1.2752 0.4938 0.9081 -0.1613 -0.1278 0.1084 248 PHE B CB 9101 C CG . PHE B 248 ? 1.3849 0.6197 1.0275 -0.1557 -0.1170 0.0944 248 PHE B CG 9102 C CD1 . PHE B 248 ? 1.4351 0.6888 1.1272 -0.1441 -0.1147 0.0849 248 PHE B CD1 9103 C CD2 . PHE B 248 ? 1.3834 0.6145 0.9864 -0.1629 -0.1077 0.0899 248 PHE B CD2 9104 C CE1 . PHE B 248 ? 1.2255 0.4937 0.9253 -0.1409 -0.1046 0.0738 248 PHE B CE1 9105 C CE2 . PHE B 248 ? 1.2844 0.5284 0.8982 -0.1583 -0.0988 0.0784 248 PHE B CE2 9106 C CZ . PHE B 248 ? 1.4407 0.7031 1.1018 -0.1478 -0.0977 0.0717 248 PHE B CZ 9107 N N . THR B 249 ? 1.4093 0.6055 1.0434 -0.1781 -0.1958 0.1354 249 THR B N 9108 C CA . THR B 249 ? 1.6050 0.7884 1.2022 -0.1928 -0.2152 0.1443 249 THR B CA 9109 C C . THR B 249 ? 1.7048 0.9005 1.3033 -0.1910 -0.2073 0.1296 249 THR B C 9110 O O . THR B 249 ? 1.7000 0.9116 1.3477 -0.1809 -0.2118 0.1234 249 THR B O 9111 C CB . THR B 249 ? 1.3988 0.5720 1.0209 -0.1968 -0.2531 0.1636 249 THR B CB 9112 O OG1 . THR B 249 ? 1.4926 0.6839 1.1859 -0.1810 -0.2589 0.1568 249 THR B OG1 9113 C CG2 . THR B 249 ? 1.5040 0.6597 1.1176 -0.2022 -0.2645 0.1818 249 THR B CG2 9114 N N . THR B 250 ? 1.5027 0.6910 1.0484 -0.2015 -0.1946 0.1233 250 THR B N 9115 C CA . THR B 250 ? 1.3941 0.5890 0.9352 -0.2026 -0.1892 0.1106 250 THR B CA 9116 C C . THR B 250 ? 1.5074 0.6849 0.9838 -0.2206 -0.1891 0.1097 250 THR B C 9117 O O . THR B 250 ? 1.5172 0.6835 0.9518 -0.2291 -0.1788 0.1122 250 THR B O 9118 C CB . THR B 250 ? 1.4703 0.6832 1.0327 -0.1894 -0.1592 0.0931 250 THR B CB 9119 O OG1 . THR B 250 ? 1.5916 0.8076 1.1480 -0.1921 -0.1552 0.0825 250 THR B OG1 9120 C CG2 . THR B 250 ? 1.4402 0.6493 0.9716 -0.1896 -0.1342 0.0882 250 THR B CG2 9121 N N . ASP B 251 ? 1.5806 0.7564 1.0494 -0.2276 -0.2003 0.1051 251 ASP B N 9122 C CA . ASP B 251 ? 1.5469 0.7066 0.9548 -0.2457 -0.1996 0.1005 251 ASP B CA 9123 C C . ASP B 251 ? 1.5121 0.6760 0.9093 -0.2426 -0.1713 0.0789 251 ASP B C 9124 O O . ASP B 251 ? 1.6952 0.8465 1.0450 -0.2565 -0.1654 0.0700 251 ASP B O 9125 C CB . ASP B 251 ? 1.5555 0.7073 0.9556 -0.2587 -0.2322 0.1087 251 ASP B CB 9126 C CG . ASP B 251 ? 1.6359 0.8018 1.0791 -0.2502 -0.2353 0.0988 251 ASP B CG 9127 O OD1 . ASP B 251 ? 1.5259 0.7101 1.0225 -0.2327 -0.2243 0.0946 251 ASP B OD1 9128 O OD2 . ASP B 251 ? 2.0718 1.2308 1.4942 -0.2626 -0.2482 0.0947 251 ASP B OD2 9129 N N . ALA B 252 ? 1.3902 0.5713 0.8315 -0.2254 -0.1540 0.0701 252 ALA B N 9130 C CA . ALA B 252 ? 1.5904 0.7750 1.0302 -0.2219 -0.1318 0.0524 252 ALA B CA 9131 C C . ALA B 252 ? 1.3628 0.5576 0.8167 -0.2090 -0.1036 0.0454 252 ALA B C 9132 O O . ALA B 252 ? 1.3921 0.5911 0.8534 -0.2035 -0.0995 0.0528 252 ALA B O 9133 C CB . ALA B 252 ? 1.9504 1.1456 1.4288 -0.2170 -0.1409 0.0487 252 ALA B CB 9134 N N . LYS B 253 ? 1.5230 0.7213 0.9831 -0.2045 -0.0858 0.0317 253 LYS B N 9135 C CA . LYS B 253 ? 1.3900 0.5979 0.8647 -0.1931 -0.0612 0.0256 253 LYS B CA 9136 C C . LYS B 253 ? 1.3258 0.5529 0.8468 -0.1798 -0.0617 0.0318 253 LYS B C 9137 O O . LYS B 253 ? 1.5656 0.7987 1.1097 -0.1790 -0.0792 0.0392 253 LYS B O 9138 C CB . LYS B 253 ? 1.5343 0.7392 1.0080 -0.1922 -0.0460 0.0111 253 LYS B CB 9139 C CG . LYS B 253 ? 1.5484 0.7347 0.9784 -0.2060 -0.0433 0.0001 253 LYS B CG 9140 C CD . LYS B 253 ? 1.6524 0.8328 1.0888 -0.2084 -0.0434 -0.0117 253 LYS B CD 9141 C CE . LYS B 253 ? 1.6460 0.8337 1.1128 -0.1962 -0.0243 -0.0189 253 LYS B CE 9142 N NZ . LYS B 253 ? 1.7207 0.8996 1.1945 -0.1996 -0.0249 -0.0299 253 LYS B NZ 9143 N N . THR B 254 ? 1.3806 0.6182 0.9164 -0.1702 -0.0426 0.0282 254 THR B N 9144 C CA . THR B 254 ? 1.3198 0.5762 0.8944 -0.1597 -0.0407 0.0320 254 THR B CA 9145 C C . THR B 254 ? 1.2772 0.5446 0.8695 -0.1527 -0.0241 0.0263 254 THR B C 9146 O O . THR B 254 ? 1.4298 0.6909 1.0077 -0.1529 -0.0113 0.0204 254 THR B O 9147 C CB . THR B 254 ? 1.2053 0.4654 0.7816 -0.1559 -0.0382 0.0379 254 THR B CB 9148 O OG1 . THR B 254 ? 1.2320 0.5110 0.8450 -0.1465 -0.0338 0.0381 254 THR B OG1 9149 C CG2 . THR B 254 ? 1.1921 0.4469 0.7445 -0.1564 -0.0208 0.0341 254 THR B CG2 9150 N N . HIS B 255 ? 1.2468 0.5313 0.8720 -0.1473 -0.0247 0.0282 255 HIS B N 9151 C CA . HIS B 255 ? 1.4858 0.7822 1.1266 -0.1422 -0.0107 0.0261 255 HIS B CA 9152 C C . HIS B 255 ? 1.3196 0.6230 0.9594 -0.1367 0.0011 0.0270 255 HIS B C 9153 O O . HIS B 255 ? 1.4370 0.7433 1.0784 -0.1350 -0.0019 0.0295 255 HIS B O 9154 C CB . HIS B 255 ? 1.5251 0.8388 1.1977 -0.1412 -0.0137 0.0273 255 HIS B CB 9155 C CG . HIS B 255 ? 1.3559 0.6651 1.0337 -0.1468 -0.0207 0.0259 255 HIS B CG 9156 N ND1 . HIS B 255 ? 1.1727 0.4711 0.8398 -0.1493 -0.0152 0.0232 255 HIS B ND1 9157 C CD2 . HIS B 255 ? 1.1421 0.4561 0.8380 -0.1505 -0.0332 0.0265 255 HIS B CD2 9158 C CE1 . HIS B 255 ? 1.1548 0.4505 0.8307 -0.1550 -0.0240 0.0221 255 HIS B CE1 9159 N NE2 . HIS B 255 ? 1.1420 0.4480 0.8353 -0.1561 -0.0351 0.0243 255 HIS B NE2 9160 N N . ILE B 256 ? 1.1188 0.4244 0.7586 -0.1341 0.0132 0.0255 256 ILE B N 9161 C CA . ILE B 256 ? 1.0988 0.4119 0.7393 -0.1294 0.0238 0.0265 256 ILE B CA 9162 C C . ILE B 256 ? 1.0999 0.4291 0.7601 -0.1271 0.0292 0.0292 256 ILE B C 9163 O O . ILE B 256 ? 1.0768 0.4082 0.7469 -0.1296 0.0265 0.0304 256 ILE B O 9164 C CB . ILE B 256 ? 1.2530 0.5541 0.8761 -0.1294 0.0327 0.0227 256 ILE B CB 9165 C CG1 . ILE B 256 ? 1.1496 0.4458 0.7792 -0.1289 0.0368 0.0202 256 ILE B CG1 9166 C CG2 . ILE B 256 ? 1.1318 0.4166 0.7289 -0.1353 0.0282 0.0197 256 ILE B CG2 9167 C CD1 . ILE B 256 ? 1.1260 0.4110 0.7455 -0.1282 0.0468 0.0133 256 ILE B CD1 9168 N N . ALA B 257 ? 1.3512 0.6918 1.0160 -0.1239 0.0360 0.0309 257 ALA B N 9169 C CA . ALA B 257 ? 1.1106 0.4672 0.7891 -0.1242 0.0400 0.0347 257 ALA B CA 9170 C C . ALA B 257 ? 1.2198 0.5708 0.9010 -0.1252 0.0411 0.0386 257 ALA B C 9171 O O . ALA B 257 ? 1.1736 0.5099 0.8481 -0.1234 0.0427 0.0364 257 ALA B O 9172 C CB . ALA B 257 ? 1.0906 0.4578 0.7696 -0.1218 0.0458 0.0356 257 ALA B CB 9173 N N . LEU B 258 ? 1.3462 0.7086 1.0382 -0.1292 0.0407 0.0439 258 LEU B N 9174 C CA . LEU B 258 ? 1.1803 0.5381 0.8786 -0.1319 0.0397 0.0507 258 LEU B CA 9175 C C . LEU B 258 ? 1.2769 0.6216 0.9773 -0.1349 0.0346 0.0481 258 LEU B C 9176 O O . LEU B 258 ? 1.2807 0.6205 0.9890 -0.1383 0.0328 0.0537 258 LEU B O 9177 C CB . LEU B 258 ? 1.0760 0.4250 0.7750 -0.1270 0.0424 0.0533 258 LEU B CB 9178 C CG . LEU B 258 ? 1.0578 0.4206 0.7584 -0.1253 0.0453 0.0581 258 LEU B CG 9179 C CD1 . LEU B 258 ? 1.0634 0.4179 0.7718 -0.1198 0.0470 0.0601 258 LEU B CD1 9180 C CD2 . LEU B 258 ? 1.1662 0.5459 0.8705 -0.1324 0.0435 0.0676 258 LEU B CD2 9181 N N . ASP B 259 ? 1.3953 0.7337 1.0891 -0.1347 0.0306 0.0407 259 ASP B N 9182 C CA . ASP B 259 ? 1.1733 0.5015 0.8692 -0.1392 0.0237 0.0380 259 ASP B CA 9183 C C . ASP B 259 ? 1.2844 0.6279 0.9972 -0.1452 0.0217 0.0422 259 ASP B C 9184 O O . ASP B 259 ? 1.4662 0.8038 1.1863 -0.1504 0.0174 0.0434 259 ASP B O 9185 C CB . ASP B 259 ? 1.3079 0.6269 0.9917 -0.1391 0.0171 0.0310 259 ASP B CB 9186 C CG . ASP B 259 ? 1.2210 0.5211 0.8843 -0.1374 0.0194 0.0252 259 ASP B CG 9187 O OD1 . ASP B 259 ? 1.2646 0.5577 0.9290 -0.1353 0.0261 0.0245 259 ASP B OD1 9188 O OD2 . ASP B 259 ? 1.1208 0.4131 0.7681 -0.1390 0.0145 0.0214 259 ASP B OD2 9189 N N . GLY B 260 ? 1.1929 0.5565 0.9126 -0.1455 0.0261 0.0434 260 GLY B N 9190 C CA . GLY B 260 ? 1.0774 0.4593 0.8138 -0.1522 0.0275 0.0446 260 GLY B CA 9191 C C . GLY B 260 ? 1.1500 0.5364 0.8905 -0.1597 0.0309 0.0541 260 GLY B C 9192 O O . GLY B 260 ? 1.1599 0.5615 0.9130 -0.1678 0.0335 0.0557 260 GLY B O 9193 N N . ARG B 261 ? 1.0819 0.4554 0.8141 -0.1578 0.0308 0.0609 261 ARG B N 9194 C CA . ARG B 261 ? 1.1005 0.4746 0.8372 -0.1652 0.0311 0.0732 261 ARG B CA 9195 C C . ARG B 261 ? 1.2226 0.5886 0.9706 -0.1720 0.0262 0.0743 261 ARG B C 9196 O O . ARG B 261 ? 1.1123 0.4858 0.8678 -0.1821 0.0271 0.0840 261 ARG B O 9197 C CB . ARG B 261 ? 1.0906 0.4498 0.8232 -0.1598 0.0295 0.0796 261 ARG B CB 9198 C CG . ARG B 261 ? 1.0997 0.4634 0.8360 -0.1669 0.0282 0.0960 261 ARG B CG 9199 C CD . ARG B 261 ? 1.1072 0.4536 0.8484 -0.1595 0.0244 0.1011 261 ARG B CD 9200 N NE . ARG B 261 ? 1.2969 0.6503 1.0401 -0.1643 0.0210 0.1180 261 ARG B NE 9201 C CZ . ARG B 261 ? 1.2219 0.5675 0.9752 -0.1715 0.0142 0.1336 261 ARG B CZ 9202 N NH1 . ARG B 261 ? 1.2830 0.6136 1.0468 -0.1744 0.0114 0.1326 261 ARG B NH1 9203 N NH2 . ARG B 261 ? 1.2746 0.6269 1.0277 -0.1769 0.0087 0.1510 261 ARG B NH2 9204 N N . LEU B 262 ? 1.2836 0.6344 1.0316 -0.1680 0.0205 0.0648 262 LEU B N 9205 C CA . LEU B 262 ? 1.1290 0.4705 0.8876 -0.1746 0.0143 0.0642 262 LEU B CA 9206 C C . LEU B 262 ? 1.2185 0.5817 0.9922 -0.1829 0.0155 0.0640 262 LEU B C 9207 O O . LEU B 262 ? 1.4080 0.7729 1.1947 -0.1925 0.0141 0.0692 262 LEU B O 9208 C CB . LEU B 262 ? 1.1189 0.4405 0.8699 -0.1703 0.0072 0.0527 262 LEU B CB 9209 C CG . LEU B 262 ? 1.1955 0.4959 0.9319 -0.1627 0.0083 0.0477 262 LEU B CG 9210 C CD1 . LEU B 262 ? 1.1469 0.4261 0.8770 -0.1648 0.0014 0.0371 262 LEU B CD1 9211 C CD2 . LEU B 262 ? 1.1537 0.4482 0.8968 -0.1614 0.0123 0.0569 262 LEU B CD2 9212 N N . ALA B 263 ? 1.1122 0.4924 0.8874 -0.1793 0.0188 0.0573 263 ALA B N 9213 C CA . ALA B 263 ? 1.1185 0.5216 0.9140 -0.1857 0.0215 0.0538 263 ALA B CA 9214 C C . ALA B 263 ? 1.1327 0.5576 0.9306 -0.1944 0.0336 0.0605 263 ALA B C 9215 O O . ALA B 263 ? 1.1450 0.5928 0.9603 -0.2015 0.0402 0.0565 263 ALA B O 9216 C CB . ALA B 263 ? 1.1749 0.5861 0.9762 -0.1780 0.0194 0.0432 263 ALA B CB 9217 N N . GLY B 264 ? 1.1141 0.5326 0.8949 -0.1949 0.0363 0.0704 264 GLY B N 9218 C CA . GLY B 264 ? 1.1278 0.5650 0.9035 -0.2053 0.0457 0.0791 264 GLY B CA 9219 C C . GLY B 264 ? 1.1949 0.6502 0.9627 -0.2020 0.0541 0.0717 264 GLY B C 9220 O O . GLY B 264 ? 1.2371 0.7148 1.0031 -0.2125 0.0644 0.0724 264 GLY B O 9221 N N . ILE B 265 ? 1.1084 0.5541 0.8709 -0.1888 0.0505 0.0639 265 ILE B N 9222 C CA . ILE B 265 ? 1.1219 0.5818 0.8785 -0.1851 0.0574 0.0561 265 ILE B CA 9223 C C . ILE B 265 ? 1.1029 0.5543 0.8396 -0.1811 0.0560 0.0637 265 ILE B C 9224 O O . ILE B 265 ? 1.0898 0.5231 0.8214 -0.1707 0.0499 0.0629 265 ILE B O 9225 C CB . ILE B 265 ? 1.1185 0.5754 0.8862 -0.1744 0.0540 0.0427 265 ILE B CB 9226 C CG1 . ILE B 265 ? 1.1031 0.5655 0.8952 -0.1770 0.0511 0.0367 265 ILE B CG1 9227 C CG2 . ILE B 265 ? 1.1324 0.6051 0.9001 -0.1719 0.0619 0.0331 265 ILE B CG2 9228 C CD1 . ILE B 265 ? 1.1403 0.5969 0.9448 -0.1672 0.0430 0.0270 265 ILE B CD1 9229 N N . VAL B 266 ? 1.1126 0.5784 0.8384 -0.1906 0.0616 0.0709 266 VAL B N 9230 C CA . VAL B 266 ? 1.1108 0.5713 0.8210 -0.1884 0.0582 0.0800 266 VAL B CA 9231 C C . VAL B 266 ? 1.2255 0.7000 0.9272 -0.1865 0.0640 0.0709 266 VAL B C 9232 O O . VAL B 266 ? 1.2082 0.6808 0.8985 -0.1852 0.0607 0.0776 266 VAL B O 9233 C CB . VAL B 266 ? 1.2709 0.7346 0.9720 -0.2016 0.0560 0.0981 266 VAL B CB 9234 C CG1 . VAL B 266 ? 1.1492 0.5918 0.8602 -0.2006 0.0474 0.1087 266 VAL B CG1 9235 C CG2 . VAL B 266 ? 1.5632 1.0517 1.2602 -0.2179 0.0663 0.0965 266 VAL B CG2 9236 N N . GLN B 267 ? 1.1832 0.6720 0.8937 -0.1865 0.0719 0.0554 267 GLN B N 9237 C CA . GLN B 267 ? 1.2462 0.7480 0.9512 -0.1857 0.0781 0.0446 267 GLN B CA 9238 C C . GLN B 267 ? 1.2019 0.6898 0.9125 -0.1711 0.0735 0.0369 267 GLN B C 9239 O O . GLN B 267 ? 1.1334 0.6136 0.8587 -0.1639 0.0710 0.0297 267 GLN B O 9240 C CB . GLN B 267 ? 1.4146 0.9399 1.1302 -0.1938 0.0907 0.0297 267 GLN B CB 9241 C CG . GLN B 267 ? 1.2878 0.8268 0.9985 -0.1947 0.0983 0.0162 267 GLN B CG 9242 C CD . GLN B 267 ? 1.4648 1.0261 1.1929 -0.2006 0.1123 -0.0031 267 GLN B CD 9243 O OE1 . GLN B 267 ? 1.5335 1.0978 1.2846 -0.1995 0.1144 -0.0082 267 GLN B OE1 9244 N NE2 . GLN B 267 ? 1.5892 1.1667 1.3087 -0.2074 0.1221 -0.0153 267 GLN B NE2 9245 N N . PRO B 268 ? 1.2946 0.7799 0.9933 -0.1680 0.0715 0.0394 268 PRO B N 9246 C CA . PRO B 268 ? 1.0842 0.5566 0.7855 -0.1562 0.0679 0.0338 268 PRO B CA 9247 C C . PRO B 268 ? 1.0862 0.5657 0.8005 -0.1532 0.0725 0.0178 268 PRO B C 9248 O O . PRO B 268 ? 1.2681 0.7664 0.9868 -0.1604 0.0808 0.0085 268 PRO B O 9249 C CB . PRO B 268 ? 1.0858 0.5604 0.7742 -0.1572 0.0664 0.0400 268 PRO B CB 9250 C CG . PRO B 268 ? 1.0982 0.5801 0.7769 -0.1676 0.0647 0.0534 268 PRO B CG 9251 C CD . PRO B 268 ? 1.2476 0.7425 0.9295 -0.1771 0.0714 0.0489 268 PRO B CD 9252 N N . ASN B 269 ? 1.1292 0.5934 0.8502 -0.1435 0.0672 0.0146 269 ASN B N 9253 C CA . ASN B 269 ? 1.1216 0.5883 0.8591 -0.1395 0.0682 0.0018 269 ASN B CA 9254 C C . ASN B 269 ? 1.1712 0.6485 0.9061 -0.1414 0.0742 -0.0064 269 ASN B C 9255 O O . ASN B 269 ? 1.1706 0.6434 0.8911 -0.1408 0.0726 -0.0006 269 ASN B O 9256 C CB . ASN B 269 ? 1.0709 0.5162 0.8105 -0.1308 0.0587 0.0045 269 ASN B CB 9257 C CG . ASN B 269 ? 1.1198 0.5648 0.8827 -0.1269 0.0552 -0.0050 269 ASN B CG 9258 O OD1 . ASN B 269 ? 1.1685 0.6259 0.9464 -0.1275 0.0610 -0.0163 269 ASN B OD1 9259 N ND2 . ASN B 269 ? 1.5383 0.9687 1.3059 -0.1233 0.0448 -0.0007 269 ASN B ND2 9260 N N . ASP B 270 ? 1.2607 0.7532 1.0121 -0.1443 0.0815 -0.0211 270 ASP B N 9261 C CA . ASP B 270 ? 1.2014 0.7009 0.9546 -0.1453 0.0865 -0.0327 270 ASP B CA 9262 C C . ASP B 270 ? 1.3774 0.8644 1.1532 -0.1359 0.0812 -0.0401 270 ASP B C 9263 O O . ASP B 270 ? 1.6910 1.1736 1.4879 -0.1313 0.0769 -0.0422 270 ASP B O 9264 C CB . ASP B 270 ? 1.2064 0.7305 0.9624 -0.1560 0.0996 -0.0471 270 ASP B CB 9265 C CG . ASP B 270 ? 1.3777 0.9127 1.1600 -0.1568 0.1059 -0.0580 270 ASP B CG 9266 O OD1 . ASP B 270 ? 1.4963 1.0197 1.3012 -0.1476 0.0983 -0.0573 270 ASP B OD1 9267 O OD2 . ASP B 270 ? 1.5654 1.1219 1.3462 -0.1680 0.1185 -0.0674 270 ASP B OD2 9268 N N . GLY B 271 ? 1.2300 0.7108 1.0028 -0.1338 0.0798 -0.0428 271 GLY B N 9269 C CA . GLY B 271 ? 1.3214 0.7866 1.1130 -0.1260 0.0725 -0.0456 271 GLY B CA 9270 C C . GLY B 271 ? 1.3551 0.8291 1.1809 -0.1245 0.0768 -0.0639 271 GLY B C 9271 O O . GLY B 271 ? 1.8646 1.3267 1.7104 -0.1189 0.0707 -0.0679 271 GLY B O 9272 N N . GLN B 272 ? 1.2032 0.6980 1.0376 -0.1301 0.0876 -0.0753 272 GLN B N 9273 C CA . GLN B 272 ? 1.4208 0.9278 1.2917 -0.1294 0.0954 -0.0968 272 GLN B CA 9274 C C . GLN B 272 ? 1.3347 0.8359 1.2411 -0.1214 0.0870 -0.0965 272 GLN B C 9275 O O . GLN B 272 ? 1.2268 0.7156 1.1244 -0.1184 0.0756 -0.0796 272 GLN B O 9276 C CB . GLN B 272 ? 1.4125 0.9467 1.2764 -0.1411 0.1130 -0.1109 272 GLN B CB 9277 C CG . GLN B 272 ? 1.5029 1.0434 1.3283 -0.1510 0.1179 -0.1080 272 GLN B CG 9278 C CD . GLN B 272 ? 1.8303 1.3975 1.6433 -0.1657 0.1343 -0.1208 272 GLN B CD 9279 O OE1 . GLN B 272 ? 2.0467 1.6296 1.8840 -0.1685 0.1460 -0.1376 272 GLN B OE1 9280 N NE2 . GLN B 272 ? 1.8309 1.4041 1.6064 -0.1762 0.1352 -0.1126 272 GLN B NE2 9281 N N . CYS B 273 ? 1.5145 1.0255 1.4633 -0.1186 0.0926 -0.1162 273 CYS B N 9282 C CA . CYS B 273 ? 1.4737 0.9798 1.4649 -0.1103 0.0822 -0.1164 273 CYS B CA 9283 C C . CYS B 273 ? 1.4772 1.0083 1.4919 -0.1146 0.0944 -0.1287 273 CYS B C 9284 O O . CYS B 273 ? 1.6566 1.2087 1.6952 -0.1184 0.1114 -0.1522 273 CYS B O 9285 C CB . CYS B 273 ? 1.3865 0.8833 1.4201 -0.1021 0.0766 -0.1286 273 CYS B CB 9286 S SG . CYS B 273 ? 1.3879 0.8809 1.4846 -0.0916 0.0616 -0.1299 273 CYS B SG 9287 N N . HIS B 274 ? 1.4317 0.9610 1.4394 -0.1153 0.0866 -0.1139 274 HIS B N 9288 C CA . HIS B 274 ? 1.6000 1.1529 1.6290 -0.1208 0.0976 -0.1227 274 HIS B CA 9289 C C . HIS B 274 ? 1.5189 1.0729 1.6037 -0.1124 0.0869 -0.1268 274 HIS B C 9290 O O . HIS B 274 ? 1.7582 1.3323 1.8671 -0.1166 0.0948 -0.1339 274 HIS B O 9291 C CB . HIS B 274 ? 1.3695 0.9224 1.3572 -0.1290 0.0975 -0.1051 274 HIS B CB 9292 C CG . HIS B 274 ? 1.3375 0.8932 1.2774 -0.1380 0.1075 -0.1011 274 HIS B CG 9293 N ND1 . HIS B 274 ? 1.3046 0.8836 1.2380 -0.1488 0.1274 -0.1170 274 HIS B ND1 9294 C CD2 . HIS B 274 ? 1.3352 0.8739 1.2333 -0.1383 0.0996 -0.0833 274 HIS B CD2 9295 C CE1 . HIS B 274 ? 1.3403 0.9159 1.2291 -0.1557 0.1289 -0.1070 274 HIS B CE1 9296 N NE2 . HIS B 274 ? 1.3288 0.8804 1.1986 -0.1486 0.1124 -0.0869 274 HIS B NE2 9297 N N . VAL B 275 ? 1.2808 0.8137 1.3875 -0.1017 0.0680 -0.1210 275 VAL B N 9298 C CA . VAL B 275 ? 1.2879 0.8210 1.4525 -0.0935 0.0543 -0.1237 275 VAL B CA 9299 C C . VAL B 275 ? 1.3760 0.9315 1.5986 -0.0907 0.0704 -0.1529 275 VAL B C 9300 O O . VAL B 275 ? 1.5000 1.0519 1.7309 -0.0879 0.0765 -0.1659 275 VAL B O 9301 C CB . VAL B 275 ? 1.1178 0.6198 1.2868 -0.0846 0.0266 -0.1060 275 VAL B CB 9302 C CG1 . VAL B 275 ? 1.1176 0.6200 1.3471 -0.0770 0.0086 -0.1055 275 VAL B CG1 9303 C CG2 . VAL B 275 ? 1.1153 0.5959 1.2247 -0.0885 0.0142 -0.0807 275 VAL B CG2 9304 N N . GLY B 276 ? 1.4172 0.9963 1.6824 -0.0920 0.0778 -0.1645 276 GLY B N 9305 C CA . GLY B 276 ? 1.5599 1.1650 1.8821 -0.0909 0.0979 -0.1958 276 GLY B CA 9306 C C . GLY B 276 ? 1.4656 1.0688 1.8668 -0.0777 0.0820 -0.2025 276 GLY B C 9307 O O . GLY B 276 ? 1.4107 0.9873 1.8187 -0.0689 0.0528 -0.1818 276 GLY B O 9308 N N . SER B 277 ? 1.4914 1.1234 1.9533 -0.0771 0.1014 -0.2317 277 SER B N 9309 C CA . SER B 277 ? 1.5870 1.2210 2.1362 -0.0637 0.0884 -0.2419 277 SER B CA 9310 C C . SER B 277 ? 1.4270 1.0580 2.0003 -0.0601 0.0630 -0.2206 277 SER B C 9311 O O . SER B 277 ? 1.4648 1.0873 2.1005 -0.0483 0.0397 -0.2168 277 SER B O 9312 C CB . SER B 277 ? 1.5983 1.2683 2.2079 -0.0653 0.1197 -0.2817 277 SER B CB 9313 O OG . SER B 277 ? 1.4810 1.1820 2.0831 -0.0777 0.1402 -0.2883 277 SER B OG 9314 N N . ASP B 278 ? 1.2998 0.9371 1.8245 -0.0710 0.0661 -0.2061 278 ASP B N 9315 C CA . ASP B 278 ? 1.2563 0.8903 1.7953 -0.0701 0.0425 -0.1859 278 ASP B CA 9316 C C . ASP B 278 ? 1.2134 0.8086 1.7059 -0.0669 0.0093 -0.1530 278 ASP B C 9317 O O . ASP B 278 ? 1.1389 0.7255 1.6324 -0.0673 -0.0142 -0.1336 278 ASP B O 9318 C CB . ASP B 278 ? 1.4465 1.1030 1.9562 -0.0842 0.0605 -0.1856 278 ASP B CB 9319 C CG . ASP B 278 ? 1.7144 1.3589 2.1342 -0.0950 0.0702 -0.1726 278 ASP B CG 9320 O OD1 . ASP B 278 ? 1.8219 1.4553 2.2097 -0.0941 0.0779 -0.1767 278 ASP B OD1 9321 O OD2 . ASP B 278 ? 1.5714 1.2175 1.9559 -0.1044 0.0694 -0.1584 278 ASP B OD2 9322 N N . ASN B 279 ? 1.4093 0.9821 1.8598 -0.0652 0.0086 -0.1479 279 ASN B N 9323 C CA . ASN B 279 ? 1.3858 0.9222 1.7916 -0.0633 -0.0193 -0.1192 279 ASN B CA 9324 C C . ASN B 279 ? 1.2512 0.7785 1.5927 -0.0726 -0.0256 -0.0978 279 ASN B C 9325 O O . ASN B 279 ? 1.2316 0.7336 1.5489 -0.0723 -0.0520 -0.0746 279 ASN B O 9326 C CB . ASN B 279 ? 1.4174 0.9379 1.8780 -0.0532 -0.0523 -0.1079 279 ASN B CB 9327 C CG . ASN B 279 ? 1.4405 0.9619 1.9636 -0.0426 -0.0503 -0.1259 279 ASN B CG 9328 O OD1 . ASN B 279 ? 1.5413 1.0558 2.0430 -0.0424 -0.0362 -0.1352 279 ASN B OD1 9329 N ND2 . ASN B 279 ? 1.5838 1.1138 2.1883 -0.0338 -0.0649 -0.1317 279 ASN B ND2 9330 N N . HIS B 280 ? 1.3800 0.9273 1.6937 -0.0820 -0.0013 -0.1061 280 HIS B N 9331 C CA . HIS B 280 ? 1.2499 0.7885 1.5044 -0.0909 -0.0044 -0.0881 280 HIS B CA 9332 C C . HIS B 280 ? 1.2372 0.7746 1.4315 -0.0978 0.0164 -0.0892 280 HIS B C 9333 O O . HIS B 280 ? 1.2860 0.8386 1.4866 -0.0989 0.0379 -0.1073 280 HIS B O 9334 C CB . HIS B 280 ? 1.2688 0.8303 1.5469 -0.0974 0.0009 -0.0918 280 HIS B CB 9335 C CG . HIS B 280 ? 1.2678 0.8220 1.5799 -0.0940 -0.0277 -0.0797 280 HIS B CG 9336 N ND1 . HIS B 280 ? 1.3380 0.9168 1.7052 -0.0955 -0.0270 -0.0883 280 HIS B ND1 9337 C CD2 . HIS B 280 ? 1.3273 0.8531 1.6248 -0.0907 -0.0585 -0.0592 280 HIS B CD2 9338 C CE1 . HIS B 280 ? 1.3370 0.9026 1.7238 -0.0927 -0.0580 -0.0733 280 HIS B CE1 9339 N NE2 . HIS B 280 ? 1.2481 0.7811 1.5909 -0.0904 -0.0777 -0.0552 280 HIS B NE2 9340 N N . TYR B 281 ? 1.2161 0.7357 1.3535 -0.1029 0.0096 -0.0708 281 TYR B N 9341 C CA . TYR B 281 ? 1.2091 0.7264 1.2925 -0.1088 0.0257 -0.0690 281 TYR B CA 9342 C C . TYR B 281 ? 1.3126 0.8519 1.3860 -0.1194 0.0440 -0.0734 281 TYR B C 9343 O O . TYR B 281 ? 1.3704 0.9061 1.4318 -0.1241 0.0369 -0.0621 281 TYR B O 9344 C CB . TYR B 281 ? 1.1383 0.6260 1.1705 -0.1086 0.0106 -0.0484 281 TYR B CB 9345 C CG . TYR B 281 ? 1.1236 0.6080 1.1048 -0.1138 0.0244 -0.0448 281 TYR B CG 9346 C CD1 . TYR B 281 ? 1.2079 0.7073 1.1864 -0.1161 0.0435 -0.0578 281 TYR B CD1 9347 C CD2 . TYR B 281 ? 1.2333 0.6998 1.1708 -0.1169 0.0176 -0.0290 281 TYR B CD2 9348 C CE1 . TYR B 281 ? 1.2255 0.7224 1.1599 -0.1212 0.0529 -0.0526 281 TYR B CE1 9349 C CE2 . TYR B 281 ? 1.3305 0.7945 1.2285 -0.1207 0.0285 -0.0252 281 TYR B CE2 9350 C CZ . TYR B 281 ? 1.3048 0.7841 1.2018 -0.1228 0.0449 -0.0357 281 TYR B CZ 9351 O OH . TYR B 281 ? 1.3774 0.8547 1.2375 -0.1269 0.0528 -0.0302 281 TYR B OH 9352 N N . SER B 282 ? 1.1513 0.7127 1.2283 -0.1246 0.0673 -0.0899 282 SER B N 9353 C CA . SER B 282 ? 1.1745 0.7608 1.2488 -0.1369 0.0863 -0.0959 282 SER B CA 9354 C C . SER B 282 ? 1.2588 0.8368 1.2754 -0.1460 0.0897 -0.0801 282 SER B C 9355 O O . SER B 282 ? 1.7319 1.3181 1.7412 -0.1553 0.0937 -0.0738 282 SER B O 9356 C CB . SER B 282 ? 1.2616 0.8753 1.3581 -0.1415 0.1108 -0.1206 282 SER B CB 9357 O OG . SER B 282 ? 1.6068 1.2127 1.6726 -0.1409 0.1165 -0.1238 282 SER B OG 9358 N N . ALA B 283 ? 1.1432 0.7048 1.1223 -0.1434 0.0872 -0.0734 283 ALA B N 9359 C CA . ALA B 283 ? 1.2783 0.8320 1.2078 -0.1508 0.0897 -0.0590 283 ALA B CA 9360 C C . ALA B 283 ? 1.2898 0.8210 1.2022 -0.1484 0.0727 -0.0404 283 ALA B C 9361 O O . ALA B 283 ? 1.2793 0.8030 1.1583 -0.1538 0.0733 -0.0281 283 ALA B O 9362 C CB . ALA B 283 ? 1.4218 0.9669 1.3229 -0.1484 0.0920 -0.0588 283 ALA B CB 9363 N N . SER B 284 ? 1.2668 0.7874 1.2036 -0.1410 0.0570 -0.0389 284 SER B N 9364 C CA . SER B 284 ? 1.2243 0.7221 1.1440 -0.1393 0.0398 -0.0240 284 SER B CA 9365 C C . SER B 284 ? 1.1736 0.6734 1.0771 -0.1488 0.0435 -0.0157 284 SER B C 9366 O O . SER B 284 ? 1.2521 0.7322 1.1246 -0.1492 0.0368 -0.0041 284 SER B O 9367 C CB . SER B 284 ? 1.2435 0.7366 1.1978 -0.1339 0.0226 -0.0249 284 SER B CB 9368 O OG . SER B 284 ? 1.2474 0.7176 1.1800 -0.1341 0.0055 -0.0118 284 SER B OG 9369 N N . THR B 285 ? 1.1998 0.7231 1.1260 -0.1569 0.0548 -0.0222 285 THR B N 9370 C CA . THR B 285 ? 1.1236 0.6493 1.0366 -0.1678 0.0588 -0.0132 285 THR B CA 9371 C C . THR B 285 ? 1.2118 0.7406 1.0906 -0.1752 0.0714 -0.0073 285 THR B C 9372 O O . THR B 285 ? 1.1831 0.7009 1.0398 -0.1807 0.0688 0.0057 285 THR B O 9373 C CB . THR B 285 ? 1.1362 0.6874 1.0864 -0.1763 0.0671 -0.0211 285 THR B CB 9374 O OG1 . THR B 285 ? 1.2974 0.8754 1.2599 -0.1813 0.0872 -0.0349 285 THR B OG1 9375 C CG2 . THR B 285 ? 1.1371 0.6874 1.1273 -0.1693 0.0522 -0.0260 285 THR B CG2 9376 N N . THR B 286 ? 1.2961 0.8393 1.1722 -0.1759 0.0840 -0.0168 286 THR B N 9377 C CA . THR B 286 ? 1.1810 0.7314 1.0263 -0.1856 0.0952 -0.0113 286 THR B CA 9378 C C . THR B 286 ? 1.2761 0.8083 1.0906 -0.1789 0.0892 -0.0038 286 THR B C 9379 O O . THR B 286 ? 1.2225 0.7581 1.0114 -0.1864 0.0943 0.0036 286 THR B O 9380 C CB . THR B 286 ? 1.2003 0.7802 1.0564 -0.1942 0.1144 -0.0275 286 THR B CB 9381 O OG1 . THR B 286 ? 1.1707 0.7509 1.0404 -0.1837 0.1149 -0.0420 286 THR B OG1 9382 C CG2 . THR B 286 ? 1.2828 0.8845 1.1732 -0.2018 0.1235 -0.0367 286 THR B CG2 9383 N N . MET B 287 ? 1.1672 0.6807 0.9845 -0.1661 0.0776 -0.0045 287 MET B N 9384 C CA . MET B 287 ? 1.1822 0.6815 0.9755 -0.1600 0.0740 0.0000 287 MET B CA 9385 C C . MET B 287 ? 1.1751 0.6474 0.9580 -0.1514 0.0599 0.0090 287 MET B C 9386 O O . MET B 287 ? 1.1960 0.6594 0.9933 -0.1468 0.0506 0.0071 287 MET B O 9387 C CB . MET B 287 ? 1.5597 1.0669 1.3644 -0.1550 0.0787 -0.0140 287 MET B CB 9388 C CG . MET B 287 ? 1.8211 1.3172 1.6037 -0.1504 0.0765 -0.0106 287 MET B CG 9389 S SD . MET B 287 ? 1.2777 0.7857 1.0741 -0.1480 0.0843 -0.0283 287 MET B SD 9390 C CE . MET B 287 ? 1.1295 0.6683 0.9261 -0.1627 0.1024 -0.0390 287 MET B CE 9391 N N . ASP B 288 ? 1.0805 0.5408 0.8389 -0.1503 0.0583 0.0183 288 ASP B N 9392 C CA . ASP B 288 ? 1.0699 0.5060 0.8158 -0.1441 0.0487 0.0251 288 ASP B CA 9393 C C . ASP B 288 ? 1.0636 0.4884 0.8088 -0.1360 0.0431 0.0204 288 ASP B C 9394 O O . ASP B 288 ? 1.1644 0.5980 0.9175 -0.1339 0.0465 0.0133 288 ASP B O 9395 C CB . ASP B 288 ? 1.0665 0.4960 0.7934 -0.1451 0.0504 0.0348 288 ASP B CB 9396 C CG . ASP B 288 ? 1.1571 0.5637 0.8751 -0.1410 0.0436 0.0401 288 ASP B CG 9397 O OD1 . ASP B 288 ? 1.0694 0.4637 0.7882 -0.1377 0.0373 0.0360 288 ASP B OD1 9398 O OD2 . ASP B 288 ? 1.0639 0.4647 0.7747 -0.1417 0.0441 0.0479 288 ASP B OD2 9399 N N . TYR B 289 ? 1.0605 0.4649 0.7955 -0.1328 0.0345 0.0241 289 TYR B N 9400 C CA . TYR B 289 ? 1.0584 0.4492 0.7853 -0.1276 0.0289 0.0229 289 TYR B CA 9401 C C . TYR B 289 ? 1.1906 0.5825 0.9057 -0.1252 0.0360 0.0235 289 TYR B C 9402 O O . TYR B 289 ? 1.0494 0.4446 0.7564 -0.1266 0.0418 0.0275 289 TYR B O 9403 C CB . TYR B 289 ? 1.0627 0.4321 0.7735 -0.1279 0.0207 0.0265 289 TYR B CB 9404 C CG . TYR B 289 ? 1.1341 0.5012 0.8552 -0.1315 0.0120 0.0263 289 TYR B CG 9405 C CD1 . TYR B 289 ? 1.2384 0.6035 0.9717 -0.1312 0.0003 0.0248 289 TYR B CD1 9406 C CD2 . TYR B 289 ? 1.2961 0.6628 1.0174 -0.1356 0.0139 0.0286 289 TYR B CD2 9407 C CE1 . TYR B 289 ? 1.2041 0.5685 0.9495 -0.1351 -0.0092 0.0249 289 TYR B CE1 9408 C CE2 . TYR B 289 ? 1.2501 0.6152 0.9823 -0.1398 0.0056 0.0282 289 TYR B CE2 9409 C CZ . TYR B 289 ? 1.1642 0.5289 0.9084 -0.1396 -0.0059 0.0260 289 TYR B CZ 9410 O OH . TYR B 289 ? 1.2266 0.5910 0.9843 -0.1443 -0.0157 0.0257 289 TYR B OH 9411 N N . PRO B 290 ? 1.2539 0.6430 0.9704 -0.1221 0.0341 0.0204 290 PRO B N 9412 C CA . PRO B 290 ? 1.0471 0.4378 0.7551 -0.1205 0.0402 0.0203 290 PRO B CA 9413 C C . PRO B 290 ? 1.0502 0.4256 0.7382 -0.1194 0.0407 0.0255 290 PRO B C 9414 O O . PRO B 290 ? 1.2144 0.5741 0.8920 -0.1199 0.0351 0.0272 290 PRO B O 9415 C CB . PRO B 290 ? 1.0501 0.4401 0.7702 -0.1182 0.0364 0.0154 290 PRO B CB 9416 C CG . PRO B 290 ? 1.1098 0.4873 0.8339 -0.1178 0.0248 0.0178 290 PRO B CG 9417 C CD . PRO B 290 ? 1.0582 0.4410 0.7867 -0.1203 0.0243 0.0182 290 PRO B CD 9418 N N . SER B 291 ? 1.0466 0.4274 0.7300 -0.1189 0.0476 0.0270 291 SER B N 9419 C CA . SER B 291 ? 1.2218 0.5912 0.8924 -0.1176 0.0506 0.0296 291 SER B CA 9420 C C . SER B 291 ? 1.3542 0.7147 1.0172 -0.1176 0.0499 0.0285 291 SER B C 9421 O O . SER B 291 ? 1.0819 0.4466 0.7531 -0.1176 0.0470 0.0265 291 SER B O 9422 C CB . SER B 291 ? 1.0946 0.4744 0.7690 -0.1168 0.0564 0.0325 291 SER B CB 9423 O OG . SER B 291 ? 1.2069 0.5998 0.8870 -0.1177 0.0582 0.0306 291 SER B OG 9424 N N . LEU B 292 ? 1.4156 0.7636 1.0640 -0.1185 0.0530 0.0294 292 LEU B N 9425 C CA . LEU B 292 ? 1.3087 0.6479 0.9464 -0.1210 0.0536 0.0302 292 LEU B CA 9426 C C . LEU B 292 ? 1.1890 0.5397 0.8379 -0.1200 0.0575 0.0297 292 LEU B C 9427 O O . LEU B 292 ? 1.1487 0.4951 0.7976 -0.1219 0.0543 0.0306 292 LEU B O 9428 C CB . LEU B 292 ? 1.1842 0.5124 0.8044 -0.1237 0.0610 0.0291 292 LEU B CB 9429 C CG . LEU B 292 ? 1.2803 0.5935 0.8826 -0.1274 0.0580 0.0274 292 LEU B CG 9430 C CD1 . LEU B 292 ? 1.3304 0.6354 0.9163 -0.1311 0.0694 0.0228 292 LEU B CD1 9431 C CD2 . LEU B 292 ? 1.1140 0.4166 0.7054 -0.1321 0.0451 0.0315 292 LEU B CD2 9432 N N . GLY B 293 ? 1.3330 0.6975 0.9921 -0.1177 0.0628 0.0290 293 GLY B N 9433 C CA . GLY B 293 ? 1.4069 0.7838 1.0762 -0.1179 0.0654 0.0279 293 GLY B CA 9434 C C . GLY B 293 ? 1.3741 0.7577 1.0530 -0.1186 0.0606 0.0240 293 GLY B C 9435 O O . GLY B 293 ? 1.2718 0.6540 0.9548 -0.1199 0.0600 0.0220 293 GLY B O 9436 N N . LEU B 294 ? 1.4221 0.8129 1.1068 -0.1181 0.0582 0.0220 294 LEU B N 9437 C CA . LEU B 294 ? 1.2292 0.6290 0.9269 -0.1189 0.0564 0.0150 294 LEU B CA 9438 C C . LEU B 294 ? 1.1711 0.5578 0.8747 -0.1177 0.0500 0.0136 294 LEU B C 9439 O O . LEU B 294 ? 1.2766 0.6660 0.9940 -0.1177 0.0490 0.0075 294 LEU B O 9440 C CB . LEU B 294 ? 1.0637 0.4745 0.7666 -0.1202 0.0568 0.0130 294 LEU B CB 9441 C CG . LEU B 294 ? 1.1567 0.5813 0.8750 -0.1222 0.0589 0.0024 294 LEU B CG 9442 C CD1 . LEU B 294 ? 1.3224 0.7609 1.0388 -0.1262 0.0642 -0.0021 294 LEU B CD1 9443 C CD2 . LEU B 294 ? 1.3185 0.7533 1.0434 -0.1245 0.0604 -0.0001 294 LEU B CD2 9444 N N . MET B 295 ? 1.1033 0.4750 0.7971 -0.1173 0.0445 0.0195 295 MET B N 9445 C CA . MET B 295 ? 1.1420 0.4990 0.8387 -0.1176 0.0349 0.0220 295 MET B CA 9446 C C . MET B 295 ? 1.4115 0.7604 1.1041 -0.1198 0.0355 0.0247 295 MET B C 9447 O O . MET B 295 ? 1.5169 0.8611 1.2244 -0.1195 0.0294 0.0235 295 MET B O 9448 C CB . MET B 295 ? 1.1998 0.5421 0.8800 -0.1194 0.0282 0.0286 295 MET B CB 9449 C CG . MET B 295 ? 1.5322 0.8799 1.2222 -0.1180 0.0239 0.0264 295 MET B CG 9450 S SD . MET B 295 ? 1.4907 0.8194 1.1632 -0.1217 0.0118 0.0333 295 MET B SD 9451 C CE . MET B 295 ? 1.4184 0.7400 1.0610 -0.1247 0.0226 0.0344 295 MET B CE 9452 N N . THR B 296 ? 1.2586 0.6059 0.9343 -0.1221 0.0430 0.0280 296 THR B N 9453 C CA . THR B 296 ? 1.1743 0.5155 0.8456 -0.1258 0.0455 0.0310 296 THR B CA 9454 C C . THR B 296 ? 1.2791 0.6302 0.9709 -0.1249 0.0464 0.0245 296 THR B C 9455 O O . THR B 296 ? 1.3064 0.6482 1.0054 -0.1271 0.0416 0.0261 296 THR B O 9456 C CB . THR B 296 ? 1.1078 0.4518 0.7651 -0.1278 0.0563 0.0326 296 THR B CB 9457 O OG1 . THR B 296 ? 1.1147 0.4450 0.7503 -0.1312 0.0566 0.0370 296 THR B OG1 9458 C CG2 . THR B 296 ? 1.1976 0.5425 0.8578 -0.1317 0.0611 0.0336 296 THR B CG2 9459 N N . GLU B 297 ? 1.1756 0.5449 0.8761 -0.1228 0.0518 0.0174 297 GLU B N 9460 C CA . GLU B 297 ? 1.1867 0.5674 0.9031 -0.1237 0.0539 0.0087 297 GLU B CA 9461 C C . GLU B 297 ? 1.3264 0.7027 1.0629 -0.1221 0.0478 0.0017 297 GLU B C 9462 O O . GLU B 297 ? 1.6141 0.9853 1.3628 -0.1236 0.0459 -0.0016 297 GLU B O 9463 C CB . GLU B 297 ? 1.0894 0.4904 0.8061 -0.1241 0.0593 0.0035 297 GLU B CB 9464 C CG . GLU B 297 ? 1.1533 0.5677 0.8833 -0.1267 0.0614 -0.0086 297 GLU B CG 9465 C CD . GLU B 297 ? 1.5337 0.9679 1.2573 -0.1304 0.0655 -0.0110 297 GLU B CD 9466 O OE1 . GLU B 297 ? 1.6639 1.1101 1.3922 -0.1328 0.0679 -0.0205 297 GLU B OE1 9467 O OE2 . GLU B 297 ? 1.6135 1.0517 1.3285 -0.1315 0.0661 -0.0031 297 GLU B OE2 9468 N N . LYS B 298 ? 1.3604 0.7389 1.1044 -0.1190 0.0446 -0.0010 298 LYS B N 9469 C CA . LYS B 298 ? 1.1577 0.5348 0.9286 -0.1163 0.0395 -0.0096 298 LYS B CA 9470 C C . LYS B 298 ? 1.2501 0.6048 1.0270 -0.1155 0.0271 -0.0002 298 LYS B C 9471 O O . LYS B 298 ? 1.1633 0.5126 0.9670 -0.1135 0.0212 -0.0057 298 LYS B O 9472 C CB . LYS B 298 ? 1.0664 0.4548 0.8470 -0.1139 0.0404 -0.0151 298 LYS B CB 9473 C CG . LYS B 298 ? 1.0823 0.4934 0.8592 -0.1169 0.0518 -0.0246 298 LYS B CG 9474 C CD . LYS B 298 ? 1.2827 0.7029 1.0663 -0.1202 0.0581 -0.0363 298 LYS B CD 9475 C CE . LYS B 298 ? 1.4568 0.9001 1.2339 -0.1259 0.0681 -0.0458 298 LYS B CE 9476 N NZ . LYS B 298 ? 1.5813 1.0367 1.3781 -0.1260 0.0730 -0.0590 298 LYS B NZ 9477 N N . LEU B 299 ? 1.1622 0.5035 0.9145 -0.1180 0.0227 0.0137 299 LEU B N 9478 C CA . LEU B 299 ? 1.2877 0.6069 1.0378 -0.1205 0.0099 0.0256 299 LEU B CA 9479 C C . LEU B 299 ? 1.3643 0.6756 1.1171 -0.1245 0.0108 0.0277 299 LEU B C 9480 O O . LEU B 299 ? 1.6651 0.9608 1.4326 -0.1257 -0.0005 0.0332 299 LEU B O 9481 C CB . LEU B 299 ? 1.4720 0.7802 1.1890 -0.1250 0.0074 0.0380 299 LEU B CB 9482 C CG . LEU B 299 ? 1.4239 0.7143 1.1375 -0.1273 -0.0097 0.0493 299 LEU B CG 9483 C CD1 . LEU B 299 ? 1.2026 0.4991 0.9498 -0.1205 -0.0188 0.0429 299 LEU B CD1 9484 C CD2 . LEU B 299 ? 1.1795 0.4639 0.8578 -0.1323 -0.0086 0.0559 299 LEU B CD2 9485 N N . SER B 300 ? 1.3272 0.6494 1.0685 -0.1269 0.0233 0.0240 300 SER B N 9486 C CA . SER B 300 ? 1.1135 0.4314 0.8585 -0.1316 0.0258 0.0246 300 SER B CA 9487 C C . SER B 300 ? 1.0925 0.4158 0.8697 -0.1289 0.0249 0.0109 300 SER B C 9488 O O . SER B 300 ? 1.4953 0.8050 1.2874 -0.1314 0.0186 0.0131 300 SER B O 9489 C CB . SER B 300 ? 1.3639 0.6945 1.0917 -0.1348 0.0386 0.0240 300 SER B CB 9490 O OG . SER B 300 ? 1.7196 1.0493 1.4548 -0.1397 0.0413 0.0231 300 SER B OG 9491 N N . GLN B 301 ? 1.0853 0.4279 0.8728 -0.1249 0.0316 -0.0036 301 GLN B N 9492 C CA . GLN B 301 ? 1.1752 0.5262 0.9905 -0.1238 0.0342 -0.0210 301 GLN B CA 9493 C C . GLN B 301 ? 1.2695 0.6067 1.1178 -0.1195 0.0237 -0.0245 301 GLN B C 9494 O O . GLN B 301 ? 1.6041 0.9367 1.4774 -0.1200 0.0226 -0.0343 301 GLN B O 9495 C CB . GLN B 301 ? 1.3563 0.7315 1.1707 -0.1227 0.0441 -0.0350 301 GLN B CB 9496 C CG . GLN B 301 ? 1.5539 0.9441 1.3442 -0.1274 0.0524 -0.0335 301 GLN B CG 9497 C CD . GLN B 301 ? 1.7651 1.1780 1.5528 -0.1291 0.0602 -0.0455 301 GLN B CD 9498 O OE1 . GLN B 301 ? 1.8251 1.2447 1.6302 -0.1276 0.0626 -0.0586 301 GLN B OE1 9499 N NE2 . GLN B 301 ? 1.7022 1.1277 1.4695 -0.1330 0.0643 -0.0407 301 GLN B NE2 9500 N N . LYS B 302 ? 1.2522 0.5826 1.1040 -0.1154 0.0150 -0.0168 302 LYS B N 9501 C CA . LYS B 302 ? 1.2095 0.5282 1.0987 -0.1103 0.0028 -0.0191 302 LYS B CA 9502 C C . LYS B 302 ? 1.3492 0.6403 1.2358 -0.1133 -0.0140 0.0016 302 LYS B C 9503 O O . LYS B 302 ? 1.1354 0.4129 1.0530 -0.1096 -0.0287 0.0050 302 LYS B O 9504 C CB . LYS B 302 ? 1.1107 0.4391 1.0114 -0.1048 0.0006 -0.0226 302 LYS B CB 9505 C CG . LYS B 302 ? 1.1610 0.5161 1.0533 -0.1049 0.0172 -0.0376 302 LYS B CG 9506 C CD . LYS B 302 ? 1.1496 0.5199 1.0683 -0.1047 0.0286 -0.0615 302 LYS B CD 9507 C CE . LYS B 302 ? 1.2042 0.5838 1.1643 -0.0989 0.0290 -0.0767 302 LYS B CE 9508 N NZ . LYS B 302 ? 1.4329 0.8333 1.4109 -0.1009 0.0454 -0.1037 302 LYS B NZ 9509 N N . ASN B 303 ? 1.3970 0.6804 1.2477 -0.1209 -0.0118 0.0156 303 ASN B N 9510 C CA . ASN B 303 ? 1.3779 0.6359 1.2172 -0.1277 -0.0254 0.0365 303 ASN B CA 9511 C C . ASN B 303 ? 1.4003 0.6446 1.2362 -0.1272 -0.0425 0.0514 303 ASN B C 9512 O O . ASN B 303 ? 1.3100 0.5345 1.1660 -0.1281 -0.0606 0.0625 303 ASN B O 9513 C CB . ASN B 303 ? 1.4478 0.6912 1.3199 -0.1286 -0.0329 0.0350 303 ASN B CB 9514 C CG . ASN B 303 ? 1.4014 0.6550 1.2731 -0.1320 -0.0184 0.0228 303 ASN B CG 9515 O OD1 . ASN B 303 ? 1.3582 0.6080 1.2034 -0.1406 -0.0136 0.0329 303 ASN B OD1 9516 N ND2 . ASN B 303 ? 1.3375 0.6052 1.2393 -0.1265 -0.0111 0.0000 303 ASN B ND2 9517 N N . ILE B 304 ? 1.3975 0.6518 1.2092 -0.1263 -0.0383 0.0522 304 ILE B N 9518 C CA . ILE B 304 ? 1.3473 0.5905 1.1527 -0.1271 -0.0548 0.0653 304 ILE B CA 9519 C C . ILE B 304 ? 1.3242 0.5558 1.0788 -0.1381 -0.0555 0.0820 304 ILE B C 9520 O O . ILE B 304 ? 1.6294 0.8722 1.3555 -0.1404 -0.0389 0.0772 304 ILE B O 9521 C CB . ILE B 304 ? 1.4341 0.6958 1.2518 -0.1193 -0.0511 0.0532 304 ILE B CB 9522 C CG1 . ILE B 304 ? 1.2083 0.4856 1.0736 -0.1101 -0.0453 0.0329 304 ILE B CG1 9523 C CG2 . ILE B 304 ? 1.5071 0.7574 1.3233 -0.1205 -0.0707 0.0664 304 ILE B CG2 9524 C CD1 . ILE B 304 ? 1.2036 0.4677 1.1152 -0.1058 -0.0628 0.0345 304 ILE B CD1 9525 N N . ASN B 305 ? 1.2155 0.4248 0.9596 -0.1458 -0.0748 0.1013 305 ASN B N 9526 C CA . ASN B 305 ? 1.2778 0.4761 0.9705 -0.1586 -0.0756 0.1159 305 ASN B CA 9527 C C . ASN B 305 ? 1.6016 0.8010 1.2815 -0.1581 -0.0846 0.1179 305 ASN B C 9528 O O . ASN B 305 ? 1.7448 0.9342 1.4429 -0.1573 -0.1068 0.1270 305 ASN B O 9529 C CB . ASN B 305 ? 1.4369 0.6096 1.1158 -0.1714 -0.0916 0.1378 305 ASN B CB 9530 C CG . ASN B 305 ? 1.5890 0.7593 1.2767 -0.1744 -0.0820 0.1370 305 ASN B CG 9531 O OD1 . ASN B 305 ? 1.5484 0.7239 1.2067 -0.1818 -0.0641 0.1355 305 ASN B OD1 9532 N ND2 . ASN B 305 ? 1.6083 0.7707 1.3401 -0.1689 -0.0937 0.1371 305 ASN B ND2 9533 N N . LEU B 306 ? 1.5185 0.7299 1.1703 -0.1587 -0.0685 0.1094 306 LEU B N 9534 C CA . LEU B 306 ? 1.2342 0.4479 0.8744 -0.1584 -0.0749 0.1087 306 LEU B CA 9535 C C . LEU B 306 ? 1.2705 0.4662 0.8622 -0.1737 -0.0836 0.1233 306 LEU B C 9536 O O . LEU B 306 ? 1.4895 0.6826 1.0443 -0.1829 -0.0690 0.1239 306 LEU B O 9537 C CB . LEU B 306 ? 1.3886 0.6229 1.0265 -0.1514 -0.0542 0.0918 306 LEU B CB 9538 C CG . LEU B 306 ? 1.3079 0.5440 0.9314 -0.1523 -0.0582 0.0898 306 LEU B CG 9539 C CD1 . LEU B 306 ? 1.3593 0.5961 1.0171 -0.1468 -0.0778 0.0917 306 LEU B CD1 9540 C CD2 . LEU B 306 ? 1.1775 0.4316 0.7995 -0.1463 -0.0379 0.0753 306 LEU B CD2 9541 N N . ILE B 307 ? 1.2920 0.4765 0.8847 -0.1774 -0.1074 0.1343 307 ILE B N 9542 C CA . ILE B 307 ? 1.5320 0.6994 1.0753 -0.1941 -0.1185 0.1481 307 ILE B CA 9543 C C . ILE B 307 ? 1.5478 0.7212 1.0790 -0.1936 -0.1203 0.1404 307 ILE B C 9544 O O . ILE B 307 ? 1.3670 0.5491 0.9351 -0.1834 -0.1307 0.1359 307 ILE B O 9545 C CB . ILE B 307 ? 1.3750 0.5209 0.9215 -0.2029 -0.1494 0.1712 307 ILE B CB 9546 C CG1 . ILE B 307 ? 1.4916 0.6292 1.0541 -0.2037 -0.1490 0.1796 307 ILE B CG1 9547 C CG2 . ILE B 307 ? 1.5300 0.6584 1.0175 -0.2236 -0.1606 0.1860 307 ILE B CG2 9548 C CD1 . ILE B 307 ? 1.8590 1.0022 1.4879 -0.1874 -0.1580 0.1748 307 ILE B CD1 9549 N N . PHE B 308 ? 1.4478 0.6169 0.9294 -0.2053 -0.1092 0.1377 308 PHE B N 9550 C CA . PHE B 308 ? 1.3555 0.5270 0.8215 -0.2073 -0.1114 0.1302 308 PHE B CA 9551 C C . PHE B 308 ? 1.6212 0.7732 1.0493 -0.2250 -0.1356 0.1458 308 PHE B C 9552 O O . PHE B 308 ? 1.6472 0.7867 1.0244 -0.2420 -0.1312 0.1516 308 PHE B O 9553 C CB . PHE B 308 ? 1.3467 0.5262 0.7862 -0.2082 -0.0829 0.1135 308 PHE B CB 9554 C CG . PHE B 308 ? 1.6063 0.8064 1.0831 -0.1911 -0.0640 0.0980 308 PHE B CG 9555 C CD1 . PHE B 308 ? 1.7468 0.9588 1.2686 -0.1781 -0.0721 0.0946 308 PHE B CD1 9556 C CD2 . PHE B 308 ? 1.5400 0.7484 1.0072 -0.1892 -0.0383 0.0869 308 PHE B CD2 9557 C CE1 . PHE B 308 ? 1.6285 0.8594 1.1788 -0.1653 -0.0550 0.0815 308 PHE B CE1 9558 C CE2 . PHE B 308 ? 1.4752 0.7018 0.9743 -0.1753 -0.0238 0.0752 308 PHE B CE2 9559 C CZ . PHE B 308 ? 1.4751 0.7125 1.0126 -0.1642 -0.0323 0.0730 308 PHE B CZ 9560 N N . ALA B 309 ? 1.5324 0.6830 0.9853 -0.2221 -0.1612 0.1525 309 ALA B N 9561 C CA . ALA B 309 ? 1.5200 0.6536 0.9384 -0.2392 -0.1875 0.1673 309 ALA B CA 9562 C C . ALA B 309 ? 1.6850 0.8243 1.0898 -0.2408 -0.1849 0.1536 309 ALA B C 9563 O O . ALA B 309 ? 1.7010 0.8526 1.1482 -0.2285 -0.1914 0.1469 309 ALA B O 9564 C CB . ALA B 309 ? 1.4661 0.5929 0.9236 -0.2364 -0.2216 0.1859 309 ALA B CB 9565 N N . VAL B 310 ? 1.6284 0.7590 0.9750 -0.2567 -0.1741 0.1482 310 VAL B N 9566 C CA . VAL B 310 ? 1.4955 0.6308 0.8283 -0.2579 -0.1657 0.1311 310 VAL B CA 9567 C C . VAL B 310 ? 1.5852 0.7033 0.8533 -0.2821 -0.1753 0.1342 310 VAL B C 9568 O O . VAL B 310 ? 1.8187 0.9234 1.0426 -0.2990 -0.1773 0.1457 310 VAL B O 9569 C CB . VAL B 310 ? 1.4892 0.6376 0.8264 -0.2474 -0.1293 0.1094 310 VAL B CB 9570 C CG1 . VAL B 310 ? 1.4322 0.5993 0.8307 -0.2252 -0.1213 0.1042 310 VAL B CG1 9571 C CG2 . VAL B 310 ? 1.5919 0.7346 0.8918 -0.2568 -0.1087 0.1089 310 VAL B CG2 9572 N N . THR B 311 ? 1.5536 0.6723 0.8151 -0.2852 -0.1807 0.1236 311 THR B N 9573 C CA . THR B 311 ? 1.7013 0.8041 0.9019 -0.3092 -0.1919 0.1241 311 THR B CA 9574 C C . THR B 311 ? 1.8698 0.9683 1.0186 -0.3208 -0.1600 0.1064 311 THR B C 9575 O O . THR B 311 ? 1.7154 0.8251 0.8835 -0.3072 -0.1295 0.0898 311 THR B O 9576 C CB . THR B 311 ? 1.8411 0.9463 1.0546 -0.3090 -0.2074 0.1162 311 THR B CB 9577 O OG1 . THR B 311 ? 1.6603 0.7808 0.9119 -0.2905 -0.1834 0.0955 311 THR B OG1 9578 C CG2 . THR B 311 ? 1.7720 0.8789 1.0273 -0.3044 -0.2443 0.1362 311 THR B CG2 9579 N N . GLU B 312 ? 2.1161 1.1986 1.1999 -0.3468 -0.1678 0.1097 312 GLU B N 9580 C CA . GLU B 312 ? 2.2260 1.3037 1.2556 -0.3620 -0.1378 0.0939 312 GLU B CA 9581 C C . GLU B 312 ? 2.1288 1.2149 1.1681 -0.3527 -0.1078 0.0625 312 GLU B C 9582 O O . GLU B 312 ? 2.2273 1.3161 1.2485 -0.3551 -0.0756 0.0456 312 GLU B O 9583 C CB . GLU B 312 ? 2.3286 1.3879 1.2837 -0.3945 -0.1546 0.1021 312 GLU B CB 9584 C CG . GLU B 312 ? 2.5246 1.5774 1.4244 -0.4145 -0.1340 0.1036 312 GLU B CG 9585 C CD . GLU B 312 ? 2.5338 1.5934 1.4156 -0.4155 -0.0908 0.0708 312 GLU B CD 9586 O OE1 . GLU B 312 ? 2.5326 1.5986 1.4136 -0.4139 -0.0637 0.0672 312 GLU B OE1 9587 O OE2 . GLU B 312 ? 2.4632 1.5216 1.3347 -0.4178 -0.0842 0.0483 312 GLU B OE2 9588 N N . ASN B 313 ? 2.0844 1.1745 1.1556 -0.3422 -0.1185 0.0549 313 ASN B N 9589 C CA . ASN B 313 ? 2.1663 1.2623 1.2523 -0.3329 -0.0933 0.0274 313 ASN B CA 9590 C C . ASN B 313 ? 2.1701 1.2824 1.3089 -0.3081 -0.0691 0.0213 313 ASN B C 9591 O O . ASN B 313 ? 2.3434 1.4595 1.4815 -0.3042 -0.0392 0.0016 313 ASN B O 9592 C CB . ASN B 313 ? 1.9779 1.0730 1.0841 -0.3303 -0.1133 0.0230 313 ASN B CB 9593 C CG . ASN B 313 ? 1.7209 0.8264 0.8834 -0.3141 -0.1378 0.0420 313 ASN B CG 9594 O OD1 . ASN B 313 ? 1.6315 0.7515 0.8470 -0.2929 -0.1266 0.0379 313 ASN B OD1 9595 N ND2 . ASN B 313 ? 1.7770 0.8755 0.9289 -0.3250 -0.1714 0.0628 313 ASN B ND2 9596 N N . VAL B 314 ? 1.9270 1.0494 1.1128 -0.2921 -0.0827 0.0379 314 VAL B N 9597 C CA . VAL B 314 ? 1.7231 0.8620 0.9596 -0.2696 -0.0640 0.0337 314 VAL B CA 9598 C C . VAL B 314 ? 1.8334 0.9761 1.0691 -0.2676 -0.0534 0.0436 314 VAL B C 9599 O O . VAL B 314 ? 1.6777 0.8340 0.9523 -0.2508 -0.0396 0.0419 314 VAL B O 9600 C CB . VAL B 314 ? 1.6077 0.7578 0.8990 -0.2534 -0.0817 0.0419 314 VAL B CB 9601 C CG1 . VAL B 314 ? 1.7583 0.9103 1.0678 -0.2506 -0.1020 0.0636 314 VAL B CG1 9602 C CG2 . VAL B 314 ? 1.5785 0.7441 0.9139 -0.2341 -0.0608 0.0304 314 VAL B CG2 9603 N N . VAL B 315 ? 1.8586 0.9889 1.0482 -0.2865 -0.0603 0.0543 315 VAL B N 9604 C CA . VAL B 315 ? 1.8258 0.9577 1.0145 -0.2871 -0.0543 0.0669 315 VAL B CA 9605 C C . VAL B 315 ? 1.8169 0.9584 1.0075 -0.2822 -0.0188 0.0509 315 VAL B C 9606 O O . VAL B 315 ? 1.8469 0.9976 1.0645 -0.2720 -0.0105 0.0567 315 VAL B O 9607 C CB . VAL B 315 ? 1.8685 0.9833 1.0033 -0.3118 -0.0712 0.0847 315 VAL B CB 9608 C CG1 . VAL B 315 ? 2.0927 1.1988 1.1658 -0.3337 -0.0531 0.0700 315 VAL B CG1 9609 C CG2 . VAL B 315 ? 1.8916 1.0067 1.0354 -0.3111 -0.0714 0.1023 315 VAL B CG2 9610 N N . ASN B 316 ? 1.8013 0.9411 0.9674 -0.2891 0.0017 0.0297 316 ASN B N 9611 C CA . ASN B 316 ? 1.6984 0.8484 0.8729 -0.2838 0.0352 0.0128 316 ASN B CA 9612 C C . ASN B 316 ? 1.6751 0.8414 0.9104 -0.2585 0.0434 0.0075 316 ASN B C 9613 O O . ASN B 316 ? 1.6121 0.7900 0.8687 -0.2501 0.0631 0.0032 316 ASN B O 9614 C CB . ASN B 316 ? 1.7316 0.8756 0.8721 -0.2962 0.0548 -0.0114 316 ASN B CB 9615 C CG . ASN B 316 ? 1.9962 1.1288 1.0723 -0.3235 0.0594 -0.0103 316 ASN B CG 9616 O OD1 . ASN B 316 ? 2.3315 1.4572 1.3843 -0.3351 0.0414 0.0123 316 ASN B OD1 9617 N ND2 . ASN B 316 ? 2.0888 1.2191 1.1362 -0.3350 0.0840 -0.0349 316 ASN B ND2 9618 N N . LEU B 317 ? 1.5592 0.7269 0.8217 -0.2478 0.0276 0.0086 317 LEU B N 9619 C CA . LEU B 317 ? 1.4527 0.6352 0.7684 -0.2265 0.0328 0.0055 317 LEU B CA 9620 C C . LEU B 317 ? 1.4727 0.6658 0.8171 -0.2165 0.0276 0.0207 317 LEU B C 9621 O O . LEU B 317 ? 1.6831 0.8890 1.0547 -0.2054 0.0432 0.0168 317 LEU B O 9622 C CB . LEU B 317 ? 1.5550 0.7365 0.8897 -0.2207 0.0164 0.0046 317 LEU B CB 9623 C CG . LEU B 317 ? 1.4179 0.6147 0.8047 -0.2016 0.0167 0.0062 317 LEU B CG 9624 C CD1 . LEU B 317 ? 1.5792 0.7835 0.9851 -0.1924 0.0403 -0.0078 317 LEU B CD1 9625 C CD2 . LEU B 317 ? 1.3284 0.5241 0.7305 -0.1996 -0.0017 0.0082 317 LEU B CD2 9626 N N . TYR B 318 ? 1.5054 0.6927 0.8455 -0.2210 0.0047 0.0375 318 TYR B N 9627 C CA . TYR B 318 ? 1.5330 0.7285 0.9033 -0.2117 -0.0020 0.0503 318 TYR B CA 9628 C C . TYR B 318 ? 1.6234 0.8189 0.9796 -0.2176 0.0117 0.0539 318 TYR B C 9629 O O . TYR B 318 ? 1.3720 0.5773 0.7573 -0.2081 0.0151 0.0583 318 TYR B O 9630 C CB . TYR B 318 ? 1.3943 0.5824 0.7698 -0.2146 -0.0311 0.0664 318 TYR B CB 9631 C CG . TYR B 318 ? 1.5302 0.7249 0.9367 -0.2049 -0.0435 0.0635 318 TYR B CG 9632 C CD1 . TYR B 318 ? 1.5625 0.7729 1.0166 -0.1890 -0.0432 0.0632 318 TYR B CD1 9633 C CD2 . TYR B 318 ? 1.4814 0.6675 0.8690 -0.2131 -0.0544 0.0600 318 TYR B CD2 9634 C CE1 . TYR B 318 ? 1.4638 0.6821 0.9465 -0.1819 -0.0522 0.0602 318 TYR B CE1 9635 C CE2 . TYR B 318 ? 1.3842 0.5775 0.8026 -0.2052 -0.0650 0.0575 318 TYR B CE2 9636 C CZ . TYR B 318 ? 1.5239 0.7337 0.9901 -0.1897 -0.0632 0.0579 318 TYR B CZ 9637 O OH . TYR B 318 ? 1.8138 1.0324 1.3107 -0.1836 -0.0718 0.0551 318 TYR B OH 9638 N N . GLN B 319 ? 1.5190 0.7040 0.8301 -0.2346 0.0203 0.0513 319 GLN B N 9639 C CA . GLN B 319 ? 1.4828 0.6701 0.7803 -0.2417 0.0386 0.0515 319 GLN B CA 9640 C C . GLN B 319 ? 1.5418 0.7470 0.8759 -0.2263 0.0612 0.0381 319 GLN B C 9641 O O . GLN B 319 ? 1.5991 0.8134 0.9546 -0.2209 0.0671 0.0430 319 GLN B O 9642 C CB . GLN B 319 ? 1.5856 0.7620 0.8287 -0.2631 0.0503 0.0449 319 GLN B CB 9643 C CG . GLN B 319 ? 1.8787 1.0372 1.0775 -0.2836 0.0295 0.0633 319 GLN B CG 9644 C CD . GLN B 319 ? 2.1305 1.2802 1.2707 -0.3077 0.0447 0.0560 319 GLN B CD 9645 O OE1 . GLN B 319 ? 2.2329 1.3889 1.3667 -0.3082 0.0699 0.0334 319 GLN B OE1 9646 N NE2 . GLN B 319 ? 2.1840 1.3190 1.2816 -0.3287 0.0295 0.0748 319 GLN B NE2 9647 N N . ASN B 320 ? 1.6507 0.8603 0.9937 -0.2198 0.0718 0.0219 320 ASN B N 9648 C CA . ASN B 320 ? 1.5450 0.7703 0.9224 -0.2064 0.0915 0.0098 320 ASN B CA 9649 C C . ASN B 320 ? 1.4731 0.7111 0.8952 -0.1891 0.0827 0.0163 320 ASN B C 9650 O O . ASN B 320 ? 1.4199 0.6719 0.8697 -0.1801 0.0945 0.0133 320 ASN B O 9651 C CB . ASN B 320 ? 1.5275 0.7506 0.9026 -0.2053 0.1035 -0.0087 320 ASN B CB 9652 C CG . ASN B 320 ? 1.8735 1.0894 1.2104 -0.2216 0.1218 -0.0214 320 ASN B CG 9653 O OD1 . ASN B 320 ? 2.2842 1.5019 1.6044 -0.2313 0.1315 -0.0176 320 ASN B OD1 9654 N ND2 . ASN B 320 ? 2.0317 1.2395 1.3542 -0.2260 0.1276 -0.0374 320 ASN B ND2 9655 N N . TYR B 321 ? 1.5098 0.7442 0.9392 -0.1857 0.0620 0.0247 321 TYR B N 9656 C CA . TYR B 321 ? 1.5279 0.7748 0.9957 -0.1722 0.0542 0.0303 321 TYR B CA 9657 C C . TYR B 321 ? 1.4951 0.7450 0.9690 -0.1733 0.0523 0.0401 321 TYR B C 9658 O O . TYR B 321 ? 1.4559 0.7195 0.9584 -0.1640 0.0572 0.0396 321 TYR B O 9659 C CB . TYR B 321 ? 1.4314 0.6751 0.9081 -0.1695 0.0341 0.0354 321 TYR B CB 9660 C CG . TYR B 321 ? 1.4548 0.6999 0.9392 -0.1653 0.0357 0.0262 321 TYR B CG 9661 C CD1 . TYR B 321 ? 1.3566 0.6101 0.8563 -0.1582 0.0518 0.0166 321 TYR B CD1 9662 C CD2 . TYR B 321 ? 1.6872 0.9246 1.1663 -0.1687 0.0197 0.0281 321 TYR B CD2 9663 C CE1 . TYR B 321 ? 1.4981 0.7506 1.0069 -0.1548 0.0522 0.0096 321 TYR B CE1 9664 C CE2 . TYR B 321 ? 1.4359 0.6737 0.9233 -0.1659 0.0209 0.0201 321 TYR B CE2 9665 C CZ . TYR B 321 ? 1.5663 0.8107 1.0680 -0.1590 0.0373 0.0110 321 TYR B CZ 9666 O OH . TYR B 321 ? 1.5163 0.7589 1.0281 -0.1568 0.0374 0.0043 321 TYR B OH 9667 N N . SER B 322 ? 1.5014 0.7376 0.9469 -0.1860 0.0445 0.0494 322 SER B N 9668 C CA . SER B 322 ? 1.5295 0.7647 0.9798 -0.1889 0.0408 0.0602 322 SER B CA 9669 C C . SER B 322 ? 1.6189 0.8633 1.0709 -0.1903 0.0623 0.0546 322 SER B C 9670 O O . SER B 322 ? 1.4804 0.7315 0.9526 -0.1869 0.0632 0.0590 322 SER B O 9671 C CB . SER B 322 ? 1.4705 0.6865 0.8879 -0.2042 0.0253 0.0742 322 SER B CB 9672 O OG . SER B 322 ? 1.8734 1.0813 1.2484 -0.2195 0.0372 0.0707 322 SER B OG 9673 N N . GLU B 323 ? 1.5290 0.7744 0.9629 -0.1954 0.0799 0.0436 323 GLU B N 9674 C CA . GLU B 323 ? 1.3786 0.6353 0.8199 -0.1963 0.1018 0.0364 323 GLU B CA 9675 C C . GLU B 323 ? 1.4260 0.7014 0.9111 -0.1800 0.1065 0.0313 323 GLU B C 9676 O O . GLU B 323 ? 1.5353 0.8225 1.0366 -0.1789 0.1192 0.0288 323 GLU B O 9677 C CB . GLU B 323 ? 1.4974 0.7521 0.9155 -0.2042 0.1207 0.0224 323 GLU B CB 9678 C CG . GLU B 323 ? 1.9255 1.1636 1.2931 -0.2247 0.1200 0.0264 323 GLU B CG 9679 C CD . GLU B 323 ? 2.3396 1.5769 1.6843 -0.2334 0.1414 0.0082 323 GLU B CD 9680 O OE1 . GLU B 323 ? 2.4406 1.6915 1.8143 -0.2234 0.1597 -0.0067 323 GLU B OE1 9681 O OE2 . GLU B 323 ? 2.4681 1.6911 1.7668 -0.2507 0.1394 0.0085 323 GLU B OE2 9682 N N . LEU B 324 ? 1.6509 0.9296 1.1546 -0.1690 0.0959 0.0303 324 LEU B N 9683 C CA . LEU B 324 ? 1.4506 0.7463 0.9910 -0.1559 0.0972 0.0277 324 LEU B CA 9684 C C . LEU B 324 ? 1.4914 0.7905 1.0479 -0.1522 0.0838 0.0360 324 LEU B C 9685 O O . LEU B 324 ? 1.7102 1.0237 1.2931 -0.1440 0.0840 0.0344 324 LEU B O 9686 C CB . LEU B 324 ? 1.1588 0.4570 0.7101 -0.1478 0.0955 0.0216 324 LEU B CB 9687 C CG . LEU B 324 ? 1.2100 0.5054 0.7544 -0.1494 0.1100 0.0103 324 LEU B CG 9688 C CD1 . LEU B 324 ? 1.3443 0.6399 0.9023 -0.1417 0.1062 0.0058 324 LEU B CD1 9689 C CD2 . LEU B 324 ? 1.2988 0.6070 0.8615 -0.1474 0.1267 0.0050 324 LEU B CD2 9690 N N . ILE B 325 ? 1.3095 0.5951 0.8506 -0.1591 0.0716 0.0446 325 ILE B N 9691 C CA . ILE B 325 ? 1.4160 0.7026 0.9758 -0.1559 0.0592 0.0509 325 ILE B CA 9692 C C . ILE B 325 ? 1.6967 0.9711 1.2428 -0.1664 0.0557 0.0606 325 ILE B C 9693 O O . ILE B 325 ? 1.9260 1.1844 1.4560 -0.1732 0.0419 0.0698 325 ILE B O 9694 C CB . ILE B 325 ? 1.3239 0.6058 0.8908 -0.1517 0.0426 0.0531 325 ILE B CB 9695 C CG1 . ILE B 325 ? 1.3504 0.6414 0.9249 -0.1446 0.0460 0.0453 325 ILE B CG1 9696 C CG2 . ILE B 325 ? 1.2532 0.5400 0.8483 -0.1464 0.0333 0.0549 325 ILE B CG2 9697 C CD1 . ILE B 325 ? 1.2977 0.5857 0.8800 -0.1418 0.0313 0.0468 325 ILE B CD1 9698 N N . PRO B 326 ? 1.5498 0.8315 1.1032 -0.1687 0.0669 0.0597 326 PRO B N 9699 C CA . PRO B 326 ? 1.4531 0.7239 0.9935 -0.1806 0.0662 0.0695 326 PRO B CA 9700 C C . PRO B 326 ? 1.5364 0.7940 1.0860 -0.1813 0.0462 0.0801 326 PRO B C 9701 O O . PRO B 326 ? 1.5419 0.8061 1.1208 -0.1708 0.0385 0.0759 326 PRO B O 9702 C CB . PRO B 326 ? 1.6456 0.9322 1.2067 -0.1787 0.0800 0.0641 326 PRO B CB 9703 C CG . PRO B 326 ? 1.5118 0.8152 1.0846 -0.1694 0.0913 0.0524 326 PRO B CG 9704 C CD . PRO B 326 ? 1.4627 0.7642 1.0389 -0.1610 0.0798 0.0505 326 PRO B CD 9705 N N . GLY B 327 ? 1.6549 0.8938 1.1802 -0.1945 0.0380 0.0935 327 GLY B N 9706 C CA . GLY B 327 ? 1.8867 1.1103 1.4238 -0.1959 0.0169 0.1059 327 GLY B CA 9707 C C . GLY B 327 ? 1.9313 1.1424 1.4572 -0.1964 -0.0018 0.1127 327 GLY B C 9708 O O . GLY B 327 ? 1.9287 1.1239 1.4608 -0.1999 -0.0223 0.1260 327 GLY B O 9709 N N . THR B 328 ? 1.6420 0.8599 1.1543 -0.1932 0.0040 0.1039 328 THR B N 9710 C CA . THR B 328 ? 1.7344 0.9426 1.2367 -0.1943 -0.0134 0.1088 328 THR B CA 9711 C C . THR B 328 ? 1.8844 1.0771 1.3365 -0.2120 -0.0151 0.1177 328 THR B C 9712 O O . THR B 328 ? 2.0628 1.2602 1.4887 -0.2182 0.0044 0.1094 328 THR B O 9713 C CB . THR B 328 ? 1.5893 0.8122 1.1059 -0.1820 -0.0082 0.0945 328 THR B CB 9714 O OG1 . THR B 328 ? 1.7014 0.9330 1.1996 -0.1835 0.0131 0.0837 328 THR B OG1 9715 C CG2 . THR B 328 ? 1.4852 0.7236 1.0468 -0.1672 -0.0072 0.0861 328 THR B CG2 9716 N N . THR B 329 ? 1.6921 0.8667 1.1322 -0.2207 -0.0390 0.1340 329 THR B N 9717 C CA . THR B 329 ? 1.8437 1.0021 1.2313 -0.2406 -0.0444 0.1444 329 THR B CA 9718 C C . THR B 329 ? 1.8732 1.0264 1.2507 -0.2410 -0.0616 0.1448 329 THR B C 9719 O O . THR B 329 ? 1.8974 1.0545 1.3124 -0.2281 -0.0772 0.1445 329 THR B O 9720 C CB . THR B 329 ? 1.9530 1.0916 1.3259 -0.2557 -0.0614 0.1677 329 THR B CB 9721 O OG1 . THR B 329 ? 1.8563 0.9877 1.2688 -0.2466 -0.0884 0.1787 329 THR B OG1 9722 C CG2 . THR B 329 ? 2.1330 1.2759 1.5109 -0.2588 -0.0430 0.1675 329 THR B CG2 9723 N N . VAL B 330 ? 1.7185 0.8639 1.0460 -0.2569 -0.0578 0.1439 330 VAL B N 9724 C CA . VAL B 330 ? 1.5616 0.7012 0.8744 -0.2601 -0.0742 0.1435 330 VAL B CA 9725 C C . VAL B 330 ? 1.5657 0.6836 0.8308 -0.2833 -0.0959 0.1634 330 VAL B C 9726 O O . VAL B 330 ? 1.8062 0.9146 1.0374 -0.2998 -0.0906 0.1737 330 VAL B O 9727 C CB . VAL B 330 ? 1.5314 0.6804 0.8263 -0.2590 -0.0521 0.1215 330 VAL B CB 9728 C CG1 . VAL B 330 ? 1.5064 0.6759 0.8455 -0.2381 -0.0321 0.1047 330 VAL B CG1 9729 C CG2 . VAL B 330 ? 1.5759 0.7190 0.8177 -0.2783 -0.0326 0.1173 330 VAL B CG2 9730 N N . GLY B 331 ? 1.5771 0.6877 0.8392 -0.2859 -0.1211 0.1696 331 GLY B N 9731 C CA . GLY B 331 ? 1.6133 0.7033 0.8276 -0.3092 -0.1456 0.1895 331 GLY B CA 9732 C C . GLY B 331 ? 1.7395 0.8271 0.9392 -0.3134 -0.1614 0.1848 331 GLY B C 9733 O O . GLY B 331 ? 1.6710 0.7712 0.9124 -0.2956 -0.1627 0.1726 331 GLY B O 9734 N N . VAL B 332 ? 1.6757 0.7473 0.8145 -0.3387 -0.1739 0.1948 332 VAL B N 9735 C CA . VAL B 332 ? 1.7014 0.7695 0.8184 -0.3464 -0.1885 0.1890 332 VAL B CA 9736 C C . VAL B 332 ? 1.7194 0.7819 0.8716 -0.3418 -0.2299 0.2088 332 VAL B C 9737 O O . VAL B 332 ? 1.8145 0.8622 0.9601 -0.3528 -0.2576 0.2355 332 VAL B O 9738 C CB . VAL B 332 ? 1.9641 1.0175 0.9986 -0.3778 -0.1866 0.1907 332 VAL B CB 9739 C CG1 . VAL B 332 ? 2.1547 1.2037 1.1672 -0.3867 -0.2044 0.1843 332 VAL B CG1 9740 C CG2 . VAL B 332 ? 1.8725 0.9339 0.8787 -0.3816 -0.1431 0.1676 332 VAL B CG2 9741 N N . LEU B 333 ? 1.7184 0.7932 0.9114 -0.3257 -0.2341 0.1958 333 LEU B N 9742 C CA . LEU B 333 ? 1.7113 0.7851 0.9464 -0.3195 -0.2708 0.2103 333 LEU B CA 9743 C C . LEU B 333 ? 1.8979 0.9624 1.0926 -0.3381 -0.2932 0.2126 333 LEU B C 9744 O O . LEU B 333 ? 2.0314 1.1010 1.2031 -0.3408 -0.2757 0.1910 333 LEU B O 9745 C CB . LEU B 333 ? 1.6287 0.7240 0.9378 -0.2915 -0.2616 0.1948 333 LEU B CB 9746 C CG . LEU B 333 ? 1.6675 0.7673 1.0460 -0.2761 -0.2863 0.2085 333 LEU B CG 9747 C CD1 . LEU B 333 ? 1.6840 0.8069 1.1245 -0.2532 -0.2745 0.1893 333 LEU B CD1 9748 C CD2 . LEU B 333 ? 1.6656 0.7511 1.0401 -0.2895 -0.3299 0.2322 333 LEU B CD2 9749 N N . SER B 334 ? 2.0424 1.0925 1.2300 -0.3515 -0.3333 0.2391 334 SER B N 9750 C CA . SER B 334 ? 2.0970 1.1389 1.2518 -0.3694 -0.3608 0.2438 334 SER B CA 9751 C C . SER B 334 ? 2.0162 1.0753 1.2283 -0.3508 -0.3650 0.2284 334 SER B C 9752 O O . SER B 334 ? 2.0138 1.0889 1.2958 -0.3258 -0.3575 0.2227 334 SER B O 9753 C CB . SER B 334 ? 2.1422 1.1658 1.2860 -0.3863 -0.4071 0.2791 334 SER B CB 9754 O OG . SER B 334 ? 2.1168 1.1457 1.3399 -0.3656 -0.4273 0.2935 334 SER B OG 9755 N N . MET B 335 ? 1.9965 1.0527 1.1774 -0.3645 -0.3759 0.2208 335 MET B N 9756 C CA . MET B 335 ? 2.1026 1.1746 1.3326 -0.3502 -0.3785 0.2054 335 MET B CA 9757 C C . MET B 335 ? 1.8248 0.9057 1.1314 -0.3354 -0.4108 0.2220 335 MET B C 9758 O O . MET B 335 ? 1.7426 0.8430 1.1128 -0.3145 -0.4020 0.2088 335 MET B O 9759 C CB . MET B 335 ? 2.4530 1.5169 1.6317 -0.3715 -0.3897 0.1968 335 MET B CB 9760 C CG . MET B 335 ? 2.6062 1.6596 1.7067 -0.3893 -0.3596 0.1792 335 MET B CG 9761 S SD . MET B 335 ? 2.8825 1.9512 2.0052 -0.3669 -0.3043 0.1479 335 MET B SD 9762 C CE . MET B 335 ? 2.2870 1.3412 1.3174 -0.3927 -0.2771 0.1300 335 MET B CE 9763 N N . ASP B 336 ? 1.9705 1.0373 1.2720 -0.3472 -0.4481 0.2510 336 ASP B N 9764 C CA . ASP B 336 ? 1.9711 1.0446 1.3481 -0.3346 -0.4827 0.2682 336 ASP B CA 9765 C C . ASP B 336 ? 2.0475 1.1235 1.4765 -0.3164 -0.4774 0.2775 336 ASP B C 9766 O O . ASP B 336 ? 2.0220 1.1027 1.5192 -0.3047 -0.5041 0.2910 336 ASP B O 9767 C CB . ASP B 336 ? 1.9945 1.0505 1.3443 -0.3579 -0.5328 0.2963 336 ASP B CB 9768 C CG . ASP B 336 ? 2.1865 1.2175 1.4508 -0.3848 -0.5385 0.3148 336 ASP B CG 9769 O OD1 . ASP B 336 ? 2.3386 1.3650 1.5919 -0.3807 -0.5148 0.3160 336 ASP B OD1 9770 O OD2 . ASP B 336 ? 2.1135 1.1299 1.3203 -0.4116 -0.5666 0.3279 336 ASP B OD2 9771 N N . SER B 337 ? 2.1893 1.2623 1.5881 -0.3145 -0.4431 0.2693 337 SER B N 9772 C CA . SER B 337 ? 2.0594 1.1332 1.4987 -0.2995 -0.4341 0.2757 337 SER B CA 9773 C C . SER B 337 ? 2.0547 1.1087 1.5008 -0.3093 -0.4734 0.3095 337 SER B C 9774 O O . SER B 337 ? 2.0862 1.1434 1.6000 -0.2927 -0.4835 0.3172 337 SER B O 9775 C CB . SER B 337 ? 2.0452 1.1435 1.5719 -0.2706 -0.4209 0.2586 337 SER B CB 9776 O OG . SER B 337 ? 2.1945 1.3088 1.7137 -0.2607 -0.3791 0.2304 337 SER B OG 9777 N N . SER B 338 ? 1.9719 1.0048 1.3473 -0.3372 -0.4958 0.3294 338 SER B N 9778 C CA . SER B 338 ? 1.9319 0.9425 1.3013 -0.3509 -0.5332 0.3651 338 SER B CA 9779 C C . SER B 338 ? 2.0400 1.0386 1.3745 -0.3568 -0.5103 0.3709 338 SER B C 9780 O O . SER B 338 ? 2.3951 1.3760 1.7374 -0.3632 -0.5342 0.3989 338 SER B O 9781 C CB . SER B 338 ? 2.0391 1.0322 1.3428 -0.3817 -0.5690 0.3859 338 SER B CB 9782 O OG . SER B 338 ? 1.9823 0.9718 1.1970 -0.4019 -0.5413 0.3704 338 SER B OG 9783 N N . ASN B 339 ? 1.8508 0.8593 1.1504 -0.3545 -0.4643 0.3447 339 ASN B N 9784 C CA . ASN B 339 ? 1.9194 0.9189 1.1767 -0.3634 -0.4386 0.3471 339 ASN B CA 9785 C C . ASN B 339 ? 1.9014 0.9109 1.2217 -0.3385 -0.4168 0.3385 339 ASN B C 9786 O O . ASN B 339 ? 1.9081 0.9089 1.2062 -0.3449 -0.4019 0.3452 339 ASN B O 9787 C CB . ASN B 339 ? 1.9947 0.9998 1.1820 -0.3755 -0.4005 0.3228 339 ASN B CB 9788 C CG . ASN B 339 ? 2.3690 1.3649 1.5043 -0.3901 -0.3753 0.3262 339 ASN B CG 9789 O OD1 . ASN B 339 ? 2.5319 1.5407 1.6823 -0.3760 -0.3378 0.3062 339 ASN B OD1 9790 N ND2 . ASN B 339 ? 2.4075 1.3816 1.4812 -0.4198 -0.3964 0.3525 339 ASN B ND2 9791 N N . VAL B 340 ? 1.8021 0.8303 1.2002 -0.3117 -0.4151 0.3235 340 VAL B N 9792 C CA . VAL B 340 ? 1.7017 0.7430 1.1557 -0.2883 -0.3893 0.3086 340 VAL B CA 9793 C C . VAL B 340 ? 1.8059 0.8308 1.2861 -0.2884 -0.4053 0.3311 340 VAL B C 9794 O O . VAL B 340 ? 1.9425 0.9686 1.4228 -0.2837 -0.3795 0.3242 340 VAL B O 9795 C CB . VAL B 340 ? 1.7301 0.7948 1.2634 -0.2621 -0.3869 0.2893 340 VAL B CB 9796 C CG1 . VAL B 340 ? 1.8628 0.9480 1.3803 -0.2553 -0.3525 0.2594 340 VAL B CG1 9797 C CG2 . VAL B 340 ? 1.7378 0.7991 1.3074 -0.2629 -0.4295 0.3052 340 VAL B CG2 9798 N N . LEU B 341 ? 2.0221 1.0312 1.5269 -0.2939 -0.4491 0.3584 341 LEU B N 9799 C CA . LEU B 341 ? 1.8817 0.8891 1.4276 -0.2895 -0.4643 0.3748 341 LEU B CA 9800 C C . LEU B 341 ? 1.8443 0.8437 1.3283 -0.3076 -0.4472 0.3833 341 LEU B C 9801 O O . LEU B 341 ? 2.0609 1.0643 1.5746 -0.2988 -0.4346 0.3819 341 LEU B O 9802 C CB . LEU B 341 ? 2.3210 1.3261 1.8985 -0.2940 -0.5129 0.3995 341 LEU B CB 9803 C CG . LEU B 341 ? 2.6354 1.6268 2.1404 -0.3245 -0.5410 0.4242 341 LEU B CG 9804 C CD1 . LEU B 341 ? 2.6771 1.6622 2.1681 -0.3383 -0.5547 0.4472 341 LEU B CD1 9805 C CD2 . LEU B 341 ? 2.5786 1.5707 2.1126 -0.3253 -0.5819 0.4352 341 LEU B CD2 9806 N N . GLN B 342 ? 1.9277 0.9162 1.3258 -0.3336 -0.4451 0.3903 342 GLN B N 9807 C CA . GLN B 342 ? 1.8935 0.8764 1.2283 -0.3533 -0.4251 0.3956 342 GLN B CA 9808 C C . GLN B 342 ? 1.8099 0.7982 1.1302 -0.3454 -0.3779 0.3699 342 GLN B C 9809 O O . GLN B 342 ? 1.9329 0.9236 1.2476 -0.3471 -0.3570 0.3688 342 GLN B O 9810 C CB . GLN B 342 ? 1.9973 0.9687 1.2446 -0.3855 -0.4369 0.4086 342 GLN B CB 9811 C CG . GLN B 342 ? 2.0720 1.0397 1.2543 -0.4084 -0.4160 0.4138 342 GLN B CG 9812 C CD . GLN B 342 ? 2.2526 1.2213 1.4709 -0.4069 -0.4289 0.4326 342 GLN B CD 9813 O OE1 . GLN B 342 ? 2.2593 1.2260 1.5208 -0.4035 -0.4669 0.4522 342 GLN B OE1 9814 N NE2 . GLN B 342 ? 2.2359 1.2076 1.4396 -0.4096 -0.3976 0.4265 342 GLN B NE2 9815 N N . LEU B 343 ? 1.8448 0.8409 1.1650 -0.3357 -0.3610 0.3471 343 LEU B N 9816 C CA . LEU B 343 ? 1.8342 0.8504 1.1487 -0.3248 -0.3147 0.3164 343 LEU B CA 9817 C C . LEU B 343 ? 1.7314 0.7577 1.1108 -0.3020 -0.2994 0.3065 343 LEU B C 9818 O O . LEU B 343 ? 1.6798 0.7152 1.0487 -0.2993 -0.2662 0.2919 343 LEU B O 9819 C CB . LEU B 343 ? 1.9054 0.9407 1.2226 -0.3145 -0.3018 0.2906 343 LEU B CB 9820 C CG . LEU B 343 ? 1.9848 1.0389 1.2875 -0.3068 -0.2567 0.2606 343 LEU B CG 9821 C CD1 . LEU B 343 ? 2.2552 1.3003 1.4886 -0.3293 -0.2366 0.2634 343 LEU B CD1 9822 C CD2 . LEU B 343 ? 1.8391 0.9069 1.1393 -0.3007 -0.2494 0.2397 343 LEU B CD2 9823 N N . ILE B 344 ? 1.7785 0.8037 1.2266 -0.2861 -0.3238 0.3135 344 ILE B N 9824 C CA . ILE B 344 ? 1.6800 0.7133 1.1918 -0.2656 -0.3120 0.3034 344 ILE B CA 9825 C C . ILE B 344 ? 1.7512 0.7731 1.2507 -0.2759 -0.3097 0.3187 344 ILE B C 9826 O O . ILE B 344 ? 1.5976 0.6249 1.1006 -0.2709 -0.2815 0.3058 344 ILE B O 9827 C CB . ILE B 344 ? 1.7508 0.7859 1.3426 -0.2474 -0.3392 0.3062 344 ILE B CB 9828 C CG1 . ILE B 344 ? 1.5479 0.6051 1.1634 -0.2340 -0.3353 0.2857 344 ILE B CG1 9829 C CG2 . ILE B 344 ? 1.6704 0.7126 1.3244 -0.2291 -0.3266 0.2950 344 ILE B CG2 9830 C CD1 . ILE B 344 ? 1.5338 0.6165 1.1575 -0.2192 -0.2951 0.2538 344 ILE B CD1 9831 N N . VAL B 345 ? 1.6717 0.6852 1.1605 -0.2896 -0.3392 0.3445 345 VAL B N 9832 C CA . VAL B 345 ? 1.8381 0.8474 1.3189 -0.2997 -0.3391 0.3596 345 VAL B CA 9833 C C . VAL B 345 ? 1.8383 0.8464 1.2525 -0.3164 -0.3054 0.3533 345 VAL B C 9834 O O . VAL B 345 ? 2.0087 1.0199 1.4332 -0.3148 -0.2867 0.3501 345 VAL B O 9835 C CB . VAL B 345 ? 1.7586 0.7577 1.2254 -0.3166 -0.3775 0.3899 345 VAL B CB 9836 C CG1 . VAL B 345 ? 1.9092 0.9033 1.3680 -0.3280 -0.3766 0.4057 345 VAL B CG1 9837 C CG2 . VAL B 345 ? 1.7506 0.7520 1.2898 -0.2998 -0.4119 0.3961 345 VAL B CG2 9838 N N . ASP B 346 ? 1.7302 0.7341 1.0783 -0.3326 -0.2971 0.3503 346 ASP B N 9839 C CA . ASP B 346 ? 1.8920 0.8962 1.1777 -0.3487 -0.2628 0.3411 346 ASP B CA 9840 C C . ASP B 346 ? 1.8154 0.8300 1.1285 -0.3310 -0.2278 0.3156 346 ASP B C 9841 O O . ASP B 346 ? 1.9448 0.9633 1.2418 -0.3372 -0.2021 0.3107 346 ASP B O 9842 C CB . ASP B 346 ? 2.1235 1.1208 1.3389 -0.3675 -0.2597 0.3382 346 ASP B CB 9843 C CG . ASP B 346 ? 2.1581 1.1456 1.3384 -0.3886 -0.2946 0.3630 346 ASP B CG 9844 O OD1 . ASP B 346 ? 1.8669 0.8523 1.0553 -0.3966 -0.3118 0.3835 346 ASP B OD1 9845 O OD2 . ASP B 346 ? 2.1997 1.1809 1.3445 -0.3979 -0.3057 0.3622 346 ASP B OD2 9846 N N . ALA B 347 ? 1.6343 0.6637 0.9952 -0.3072 -0.2262 0.2963 347 ALA B N 9847 C CA . ALA B 347 ? 1.6381 0.6919 1.0320 -0.2869 -0.1935 0.2673 347 ALA B CA 9848 C C . ALA B 347 ? 1.6884 0.7409 1.1264 -0.2781 -0.1890 0.2687 347 ALA B C 9849 O O . ALA B 347 ? 1.5673 0.6324 1.0038 -0.2754 -0.1601 0.2544 347 ALA B O 9850 C CB . ALA B 347 ? 1.6707 0.7418 1.1064 -0.2654 -0.1956 0.2486 347 ALA B CB 9851 N N . TYR B 348 ? 1.8076 0.8449 1.2881 -0.2737 -0.2184 0.2855 348 TYR B N 9852 C CA . TYR B 348 ? 1.5853 0.6249 1.1148 -0.2641 -0.2161 0.2849 348 TYR B CA 9853 C C . TYR B 348 ? 1.6121 0.6480 1.1038 -0.2824 -0.2030 0.2957 348 TYR B C 9854 O O . TYR B 348 ? 1.7673 0.8081 1.2804 -0.2776 -0.1854 0.2871 348 TYR B O 9855 C CB . TYR B 348 ? 1.7630 0.7993 1.3503 -0.2544 -0.2493 0.2980 348 TYR B CB 9856 C CG . TYR B 348 ? 1.8721 0.9102 1.5151 -0.2436 -0.2474 0.2950 348 TYR B CG 9857 C CD1 . TYR B 348 ? 1.7729 0.8211 1.4607 -0.2254 -0.2290 0.2699 348 TYR B CD1 9858 C CD2 . TYR B 348 ? 1.6996 0.7287 1.3494 -0.2529 -0.2646 0.3168 348 TYR B CD2 9859 C CE1 . TYR B 348 ? 1.8235 0.8721 1.5607 -0.2169 -0.2271 0.2651 348 TYR B CE1 9860 C CE2 . TYR B 348 ? 1.7206 0.7496 1.4222 -0.2435 -0.2627 0.3130 348 TYR B CE2 9861 C CZ . TYR B 348 ? 1.7780 0.8166 1.5230 -0.2255 -0.2437 0.2863 348 TYR B CZ 9862 O OH . TYR B 348 ? 1.6484 0.6859 1.4432 -0.2173 -0.2414 0.2804 348 TYR B OH 9863 N N . GLY B 349 ? 1.6281 0.6557 1.0626 -0.3046 -0.2115 0.3140 349 GLY B N 9864 C CA . GLY B 349 ? 1.7857 0.8111 1.1778 -0.3254 -0.1976 0.3243 349 GLY B CA 9865 C C . GLY B 349 ? 1.8993 0.9337 1.2686 -0.3269 -0.1583 0.3036 349 GLY B C 9866 O O . GLY B 349 ? 1.8637 0.9023 1.2430 -0.3295 -0.1423 0.3022 349 GLY B O 9867 N N . LYS B 350 ? 1.8598 0.8987 1.2023 -0.3248 -0.1431 0.2871 350 LYS B N 9868 C CA . LYS B 350 ? 1.8861 0.9495 1.2224 -0.3191 -0.1049 0.2610 350 LYS B CA 9869 C C . LYS B 350 ? 1.9008 0.9791 1.2975 -0.2973 -0.0935 0.2448 350 LYS B C 9870 O O . LYS B 350 ? 1.7305 0.8185 1.1291 -0.2998 -0.0708 0.2374 350 LYS B O 9871 C CB . LYS B 350 ? 2.0164 1.0951 1.3348 -0.3120 -0.0937 0.2411 350 LYS B CB 9872 C CG . LYS B 350 ? 2.1218 1.1937 1.3704 -0.3358 -0.0885 0.2457 350 LYS B CG 9873 C CD . LYS B 350 ? 2.1379 1.2267 1.3774 -0.3264 -0.0725 0.2210 350 LYS B CD 9874 C CE . LYS B 350 ? 2.1845 1.2689 1.3552 -0.3502 -0.0603 0.2191 350 LYS B CE 9875 N NZ . LYS B 350 ? 2.1721 1.2719 1.3388 -0.3404 -0.0431 0.1930 350 LYS B NZ 9876 N N . ILE B 351 ? 1.8667 0.9480 1.3129 -0.2771 -0.1092 0.2386 351 ILE B N 9877 C CA . ILE B 351 ? 1.6686 0.7660 1.1699 -0.2565 -0.0985 0.2199 351 ILE B CA 9878 C C . ILE B 351 ? 1.5829 0.6706 1.1058 -0.2613 -0.0989 0.2285 351 ILE B C 9879 O O . ILE B 351 ? 1.8416 0.9449 1.3853 -0.2541 -0.0787 0.2127 351 ILE B O 9880 C CB . ILE B 351 ? 1.5488 0.6489 1.0983 -0.2373 -0.1170 0.2134 351 ILE B CB 9881 C CG1 . ILE B 351 ? 1.4582 0.5707 0.9899 -0.2320 -0.1137 0.2023 351 ILE B CG1 9882 C CG2 . ILE B 351 ? 1.5426 0.6583 1.1460 -0.2190 -0.1060 0.1936 351 ILE B CG2 9883 C CD1 . ILE B 351 ? 1.6497 0.7660 1.2256 -0.2160 -0.1318 0.1971 351 ILE B CD1 9884 N N . ARG B 352 ? 1.6665 0.7277 1.1845 -0.2746 -0.1233 0.2547 352 ARG B N 9885 C CA . ARG B 352 ? 1.7280 0.7831 1.2702 -0.2791 -0.1250 0.2636 352 ARG B CA 9886 C C . ARG B 352 ? 1.7291 0.7837 1.2221 -0.3021 -0.1088 0.2746 352 ARG B C 9887 O O . ARG B 352 ? 1.8933 0.9457 1.4000 -0.3092 -0.1087 0.2838 352 ARG B O 9888 C CB . ARG B 352 ? 1.5379 0.5833 1.1188 -0.2749 -0.1575 0.2813 352 ARG B CB 9889 C CG . ARG B 352 ? 1.5712 0.6194 1.2202 -0.2511 -0.1682 0.2664 352 ARG B CG 9890 C CD . ARG B 352 ? 1.9253 0.9853 1.5864 -0.2385 -0.1435 0.2378 352 ARG B CD 9891 N NE . ARG B 352 ? 2.2830 1.3464 2.0092 -0.2194 -0.1485 0.2212 352 ARG B NE 9892 C CZ . ARG B 352 ? 2.1878 1.2762 1.9363 -0.2041 -0.1281 0.1926 352 ARG B CZ 9893 N NH1 . ARG B 352 ? 2.0284 1.1386 1.7428 -0.2047 -0.1038 0.1798 352 ARG B NH1 9894 N NH2 . ARG B 352 ? 2.0288 1.1213 1.8347 -0.1889 -0.1319 0.1765 352 ARG B NH2 9895 N N . SER B 353 ? 1.8202 0.8771 1.2573 -0.3145 -0.0939 0.2722 353 SER B N 9896 C CA . SER B 353 ? 2.1281 1.1873 1.5170 -0.3373 -0.0737 0.2785 353 SER B CA 9897 C C . SER B 353 ? 2.1122 1.1927 1.5122 -0.3323 -0.0400 0.2564 353 SER B C 9898 O O . SER B 353 ? 2.1628 1.2460 1.5375 -0.3500 -0.0214 0.2603 353 SER B O 9899 C CB . SER B 353 ? 2.1952 1.2512 1.5206 -0.3534 -0.0705 0.2824 353 SER B CB 9900 O OG . SER B 353 ? 2.3065 1.3686 1.5871 -0.3739 -0.0422 0.2800 353 SER B OG 9901 N N . LYS B 354 ? 2.0000 1.1005 1.4411 -0.3079 -0.0324 0.2327 354 LYS B N 9902 C CA . LYS B 354 ? 1.9654 1.0923 1.4210 -0.3005 -0.0030 0.2106 354 LYS B CA 9903 C C . LYS B 354 ? 1.8835 1.0182 1.3958 -0.2841 -0.0047 0.1997 354 LYS B C 9904 O O . LYS B 354 ? 1.7602 0.8861 1.3060 -0.2715 -0.0248 0.2004 354 LYS B O 9905 C CB . LYS B 354 ? 1.6996 0.8475 1.1445 -0.2891 0.0125 0.1898 354 LYS B CB 9906 C CG . LYS B 354 ? 1.9611 1.1223 1.3698 -0.3021 0.0406 0.1821 354 LYS B CG 9907 C CD . LYS B 354 ? 2.0621 1.2453 1.4757 -0.2868 0.0566 0.1587 354 LYS B CD 9908 C CE . LYS B 354 ? 1.9052 1.1088 1.3691 -0.2665 0.0634 0.1422 354 LYS B CE 9909 N NZ . LYS B 354 ? 1.7896 1.0132 1.2593 -0.2528 0.0773 0.1224 354 LYS B NZ 9910 N N . VAL B 355 ? 1.6397 0.7917 1.1634 -0.2852 0.0170 0.1886 355 VAL B N 9911 C CA . VAL B 355 ? 1.3788 0.5426 0.9513 -0.2710 0.0189 0.1743 355 VAL B CA 9912 C C . VAL B 355 ? 1.3645 0.5588 0.9436 -0.2640 0.0442 0.1534 355 VAL B C 9913 O O . VAL B 355 ? 1.4960 0.6994 1.0566 -0.2764 0.0629 0.1541 355 VAL B O 9914 C CB . VAL B 355 ? 1.5169 0.6654 1.1075 -0.2825 0.0123 0.1869 355 VAL B CB 9915 C CG1 . VAL B 355 ? 1.3703 0.5366 1.0034 -0.2720 0.0215 0.1684 355 VAL B CG1 9916 C CG2 . VAL B 355 ? 1.6152 0.7341 1.2185 -0.2833 -0.0170 0.2046 355 VAL B CG2 9917 N N . GLU B 356 ? 1.3119 0.5226 0.9187 -0.2449 0.0445 0.1355 356 GLU B N 9918 C CA . GLU B 356 ? 1.5532 0.7920 1.1715 -0.2375 0.0640 0.1177 356 GLU B CA 9919 C C . GLU B 356 ? 1.6956 0.9467 1.3541 -0.2231 0.0595 0.1030 356 GLU B C 9920 O O . GLU B 356 ? 1.7908 1.0373 1.4630 -0.2120 0.0465 0.0985 356 GLU B O 9921 C CB . GLU B 356 ? 1.7041 0.9542 1.3006 -0.2314 0.0732 0.1100 356 GLU B CB 9922 C CG . GLU B 356 ? 1.7937 1.0716 1.4061 -0.2228 0.0907 0.0934 356 GLU B CG 9923 C CD . GLU B 356 ? 1.9604 1.2466 1.5520 -0.2192 0.1013 0.0869 356 GLU B CD 9924 O OE1 . GLU B 356 ? 2.1112 1.3821 1.6736 -0.2237 0.0953 0.0938 356 GLU B OE1 9925 O OE2 . GLU B 356 ? 1.8653 1.1726 1.4713 -0.2124 0.1145 0.0749 356 GLU B OE2 9926 N N . LEU B 357 ? 1.4241 0.6921 1.1012 -0.2246 0.0708 0.0948 357 LEU B N 9927 C CA . LEU B 357 ? 1.3470 0.6276 1.0577 -0.2144 0.0672 0.0802 357 LEU B CA 9928 C C . LEU B 357 ? 1.6127 0.9160 1.3266 -0.2012 0.0731 0.0661 357 LEU B C 9929 O O . LEU B 357 ? 1.6989 1.0157 1.4003 -0.2012 0.0855 0.0647 357 LEU B O 9930 C CB . LEU B 357 ? 1.2520 0.5412 0.9814 -0.2231 0.0744 0.0781 357 LEU B CB 9931 C CG . LEU B 357 ? 1.4997 0.7667 1.2327 -0.2371 0.0678 0.0917 357 LEU B CG 9932 C CD1 . LEU B 357 ? 1.3343 0.6141 1.0858 -0.2464 0.0774 0.0884 357 LEU B CD1 9933 C CD2 . LEU B 357 ? 1.5175 0.7648 1.2709 -0.2315 0.0490 0.0909 357 LEU B CD2 9934 N N . GLU B 358 ? 1.6131 0.9203 1.3452 -0.1909 0.0645 0.0553 358 GLU B N 9935 C CA . GLU B 358 ? 1.4149 0.7439 1.1513 -0.1806 0.0687 0.0429 358 GLU B CA 9936 C C . GLU B 358 ? 1.4255 0.7688 1.1866 -0.1793 0.0675 0.0299 358 GLU B C 9937 O O . GLU B 358 ? 1.3507 0.6840 1.1283 -0.1829 0.0610 0.0271 358 GLU B O 9938 C CB . GLU B 358 ? 1.3187 0.6426 1.0488 -0.1712 0.0613 0.0408 358 GLU B CB 9939 C CG . GLU B 358 ? 1.4570 0.7682 1.2057 -0.1678 0.0487 0.0368 358 GLU B CG 9940 C CD . GLU B 358 ? 1.8953 1.2081 1.6438 -0.1582 0.0435 0.0318 358 GLU B CD 9941 O OE1 . GLU B 358 ? 2.2551 1.5869 2.0035 -0.1525 0.0492 0.0221 358 GLU B OE1 9942 O OE2 . GLU B 358 ? 1.6515 0.9467 1.4011 -0.1570 0.0329 0.0387 358 GLU B OE2 9943 N N . VAL B 359 ? 1.4887 0.8548 1.2524 -0.1751 0.0728 0.0223 359 VAL B N 9944 C CA . VAL B 359 ? 1.2253 0.6073 1.0073 -0.1762 0.0709 0.0104 359 VAL B CA 9945 C C . VAL B 359 ? 1.2149 0.6092 0.9960 -0.1688 0.0677 -0.0003 359 VAL B C 9946 O O . VAL B 359 ? 1.8417 1.2441 1.6110 -0.1632 0.0702 0.0025 359 VAL B O 9947 C CB . VAL B 359 ? 1.1182 0.5190 0.9069 -0.1809 0.0778 0.0119 359 VAL B CB 9948 C CG1 . VAL B 359 ? 1.2127 0.6277 1.0193 -0.1850 0.0731 0.0008 359 VAL B CG1 9949 C CG2 . VAL B 359 ? 1.1151 0.5065 0.9025 -0.1895 0.0846 0.0225 359 VAL B CG2 9950 N N . ARG B 360 ? 1.1578 0.5533 0.9517 -0.1698 0.0629 -0.0133 360 ARG B N 9951 C CA . ARG B 360 ? 1.1829 0.5920 0.9746 -0.1659 0.0617 -0.0252 360 ARG B CA 9952 C C . ARG B 360 ? 1.4975 0.9251 1.2958 -0.1725 0.0608 -0.0371 360 ARG B C 9953 O O . ARG B 360 ? 1.8248 1.2492 1.6368 -0.1792 0.0591 -0.0425 360 ARG B O 9954 C CB . ARG B 360 ? 1.1048 0.5006 0.9050 -0.1616 0.0583 -0.0339 360 ARG B CB 9955 C CG . ARG B 360 ? 1.1927 0.5722 0.9854 -0.1554 0.0562 -0.0222 360 ARG B CG 9956 C CD . ARG B 360 ? 1.5168 0.8859 1.3256 -0.1507 0.0514 -0.0314 360 ARG B CD 9957 N NE . ARG B 360 ? 1.6722 1.0259 1.4751 -0.1457 0.0463 -0.0192 360 ARG B NE 9958 C CZ . ARG B 360 ? 1.6942 1.0348 1.5151 -0.1412 0.0391 -0.0220 360 ARG B CZ 9959 N NH1 . ARG B 360 ? 1.6406 0.9815 1.4890 -0.1404 0.0381 -0.0385 360 ARG B NH1 9960 N NH2 . ARG B 360 ? 1.4249 0.7524 1.2384 -0.1380 0.0324 -0.0091 360 ARG B NH2 9961 N N . ASP B 361 ? 1.4089 0.8555 1.1965 -0.1720 0.0608 -0.0400 361 ASP B N 9962 C CA . ASP B 361 ? 1.3908 0.8562 1.1785 -0.1800 0.0579 -0.0514 361 ASP B CA 9963 C C . ASP B 361 ? 1.2698 0.7435 1.0673 -0.1872 0.0550 -0.0475 361 ASP B C 9964 O O . ASP B 361 ? 1.2589 0.7423 1.0613 -0.1960 0.0512 -0.0590 361 ASP B O 9965 C CB . ASP B 361 ? 1.4870 0.9481 1.2823 -0.1834 0.0584 -0.0717 361 ASP B CB 9966 C CG . ASP B 361 ? 1.8511 1.3056 1.6440 -0.1761 0.0619 -0.0770 361 ASP B CG 9967 O OD1 . ASP B 361 ? 1.8638 1.3275 1.6413 -0.1728 0.0632 -0.0706 361 ASP B OD1 9968 O OD2 . ASP B 361 ? 2.0962 1.5360 1.9058 -0.1738 0.0625 -0.0872 361 ASP B OD2 9969 N N . LEU B 362 ? 1.1209 0.5922 0.9223 -0.1844 0.0574 -0.0325 362 LEU B N 9970 C CA . LEU B 362 ? 1.1255 0.6068 0.9412 -0.1909 0.0560 -0.0281 362 LEU B CA 9971 C C . LEU B 362 ? 1.2315 0.7376 1.0468 -0.1944 0.0491 -0.0270 362 LEU B C 9972 O O . LEU B 362 ? 1.6992 1.2131 1.5072 -0.1887 0.0485 -0.0181 362 LEU B O 9973 C CB . LEU B 362 ? 1.2209 0.6950 1.0413 -0.1875 0.0632 -0.0140 362 LEU B CB 9974 C CG . LEU B 362 ? 1.2600 0.7482 1.0996 -0.1934 0.0642 -0.0088 362 LEU B CG 9975 C CD1 . LEU B 362 ? 1.3395 0.8238 1.1934 -0.2036 0.0616 -0.0159 362 LEU B CD1 9976 C CD2 . LEU B 362 ? 1.4042 0.8877 1.2462 -0.1902 0.0749 0.0026 362 LEU B CD2 9977 N N . PRO B 363 ? 1.3251 0.8427 1.1488 -0.2046 0.0423 -0.0353 363 PRO B N 9978 C CA . PRO B 363 ? 1.6270 1.1685 1.4527 -0.2099 0.0324 -0.0313 363 PRO B CA 9979 C C . PRO B 363 ? 1.7806 1.3309 1.6257 -0.2055 0.0334 -0.0159 363 PRO B C 9980 O O . PRO B 363 ? 1.9514 1.4963 1.8143 -0.2065 0.0397 -0.0135 363 PRO B O 9981 C CB . PRO B 363 ? 1.5868 1.1350 1.4202 -0.2229 0.0257 -0.0443 363 PRO B CB 9982 C CG . PRO B 363 ? 1.4111 0.9384 1.2561 -0.2230 0.0335 -0.0506 363 PRO B CG 9983 C CD . PRO B 363 ? 1.4147 0.9229 1.2476 -0.2123 0.0419 -0.0488 363 PRO B CD 9984 N N . GLU B 364 ? 1.5261 1.0896 1.3695 -0.2015 0.0276 -0.0059 364 GLU B N 9985 C CA . GLU B 364 ? 1.6671 1.2385 1.5333 -0.1951 0.0299 0.0069 364 GLU B CA 9986 C C . GLU B 364 ? 1.7477 1.3365 1.6441 -0.2024 0.0238 0.0086 364 GLU B C 9987 O O . GLU B 364 ? 1.6029 1.1978 1.5258 -0.1983 0.0298 0.0155 364 GLU B O 9988 C CB . GLU B 364 ? 1.8366 1.4166 1.6976 -0.1891 0.0227 0.0172 364 GLU B CB 9989 C CG . GLU B 364 ? 1.9134 1.5151 1.7795 -0.1972 0.0040 0.0222 364 GLU B CG 9990 C CD . GLU B 364 ? 2.1367 1.7412 1.9778 -0.2098 -0.0037 0.0107 364 GLU B CD 9991 O OE1 . GLU B 364 ? 2.1643 1.7543 1.9828 -0.2095 0.0050 -0.0005 364 GLU B OE1 9992 O OE2 . GLU B 364 ? 2.2889 1.9109 2.1346 -0.2205 -0.0187 0.0118 364 GLU B OE2 9993 N N . GLU B 365 ? 1.7108 1.3083 1.6044 -0.2140 0.0126 0.0008 365 GLU B N 9994 C CA . GLU B 365 ? 1.6663 1.2815 1.5888 -0.2228 0.0042 0.0016 365 GLU B CA 9995 C C . GLU B 365 ? 1.6267 1.2343 1.5716 -0.2238 0.0176 -0.0003 365 GLU B C 9996 O O . GLU B 365 ? 1.4343 1.0576 1.4123 -0.2270 0.0161 0.0042 365 GLU B O 9997 C CB . GLU B 365 ? 1.7759 1.3985 1.6850 -0.2369 -0.0095 -0.0095 365 GLU B CB 9998 C CG . GLU B 365 ? 1.9403 1.5788 1.8326 -0.2415 -0.0267 -0.0043 365 GLU B CG 9999 C CD . GLU B 365 ? 2.1058 1.7660 2.0284 -0.2406 -0.0406 0.0119 365 GLU B CD 10000 O OE1 . GLU B 365 ? 2.1314 1.8004 2.0443 -0.2396 -0.0530 0.0230 365 GLU B OE1 10001 O OE2 . GLU B 365 ? 2.1038 1.7727 2.0627 -0.2414 -0.0395 0.0139 365 GLU B OE2 10002 N N . LEU B 366 ? 1.5719 1.1560 1.5003 -0.2218 0.0300 -0.0061 366 LEU B N 10003 C CA . LEU B 366 ? 1.6621 1.2362 1.6063 -0.2247 0.0426 -0.0055 366 LEU B CA 10004 C C . LEU B 366 ? 1.3933 0.9507 1.3267 -0.2154 0.0583 0.0011 366 LEU B C 10005 O O . LEU B 366 ? 1.2678 0.8127 1.1763 -0.2076 0.0594 0.0010 366 LEU B O 10006 C CB . LEU B 366 ? 1.8367 1.3959 1.7752 -0.2343 0.0412 -0.0168 366 LEU B CB 10007 C CG . LEU B 366 ? 1.7657 1.3043 1.6763 -0.2316 0.0410 -0.0262 366 LEU B CG 10008 C CD1 . LEU B 366 ? 1.6487 1.1610 1.5562 -0.2300 0.0519 -0.0240 366 LEU B CD1 10009 C CD2 . LEU B 366 ? 1.6843 1.2267 1.5928 -0.2419 0.0301 -0.0417 366 LEU B CD2 10010 N N . SER B 367 ? 1.3365 0.8946 1.2883 -0.2177 0.0706 0.0062 367 SER B N 10011 C CA . SER B 367 ? 1.6224 1.1660 1.5619 -0.2120 0.0864 0.0118 367 SER B CA 10012 C C . SER B 367 ? 1.6060 1.1289 1.5380 -0.2206 0.0954 0.0127 367 SER B C 10013 O O . SER B 367 ? 1.3263 0.8512 1.2744 -0.2313 0.0931 0.0105 367 SER B O 10014 C CB . SER B 367 ? 1.8076 1.3693 1.7721 -0.2081 0.0963 0.0168 367 SER B CB 10015 O OG . SER B 367 ? 1.7515 1.2994 1.6995 -0.2034 0.1120 0.0199 367 SER B OG 10016 N N . LEU B 368 ? 1.5790 1.0816 1.4864 -0.2169 0.1042 0.0171 368 LEU B N 10017 C CA . LEU B 368 ? 1.4548 0.9344 1.3502 -0.2256 0.1103 0.0215 368 LEU B CA 10018 C C . LEU B 368 ? 1.2846 0.7628 1.1760 -0.2299 0.1281 0.0291 368 LEU B C 10019 O O . LEU B 368 ? 1.3502 0.8252 1.2245 -0.2226 0.1351 0.0310 368 LEU B O 10020 C CB . LEU B 368 ? 1.3043 0.7589 1.1725 -0.2204 0.1032 0.0212 368 LEU B CB 10021 C CG . LEU B 368 ? 1.3733 0.8179 1.2449 -0.2226 0.0901 0.0131 368 LEU B CG 10022 C CD1 . LEU B 368 ? 1.3508 0.8176 1.2364 -0.2213 0.0809 0.0026 368 LEU B CD1 10023 C CD2 . LEU B 368 ? 1.5746 0.9979 1.4248 -0.2151 0.0850 0.0123 368 LEU B CD2 10024 N N . SER B 369 ? 1.2740 0.7547 1.1802 -0.2430 0.1364 0.0325 369 SER B N 10025 C CA . SER B 369 ? 1.3635 0.8410 1.2605 -0.2509 0.1555 0.0391 369 SER B CA 10026 C C . SER B 369 ? 1.4852 0.9306 1.3491 -0.2584 0.1542 0.0484 369 SER B C 10027 O O . SER B 369 ? 1.7331 1.1609 1.5911 -0.2571 0.1390 0.0488 369 SER B O 10028 C CB . SER B 369 ? 1.4969 0.9937 1.4257 -0.2635 0.1665 0.0391 369 SER B CB 10029 O OG . SER B 369 ? 1.6879 1.2130 1.6532 -0.2574 0.1604 0.0316 369 SER B OG 10030 N N . PHE B 370 ? 1.5949 1.0327 1.4384 -0.2674 0.1699 0.0557 370 PHE B N 10031 C CA . PHE B 370 ? 1.4754 0.8823 1.2859 -0.2769 0.1666 0.0680 370 PHE B CA 10032 C C . PHE B 370 ? 1.5733 0.9772 1.3689 -0.2957 0.1853 0.0773 370 PHE B C 10033 O O . PHE B 370 ? 1.6468 1.0684 1.4423 -0.2974 0.2047 0.0723 370 PHE B O 10034 C CB . PHE B 370 ? 1.3601 0.7513 1.1394 -0.2655 0.1597 0.0690 370 PHE B CB 10035 C CG . PHE B 370 ? 1.4053 0.7921 1.1921 -0.2510 0.1405 0.0626 370 PHE B CG 10036 C CD1 . PHE B 370 ? 1.5188 0.8831 1.3044 -0.2530 0.1249 0.0669 370 PHE B CD1 10037 C CD2 . PHE B 370 ? 1.4346 0.8395 1.2310 -0.2361 0.1386 0.0521 370 PHE B CD2 10038 C CE1 . PHE B 370 ? 1.3654 0.7277 1.1594 -0.2406 0.1103 0.0581 370 PHE B CE1 10039 C CE2 . PHE B 370 ? 1.3010 0.7033 1.1013 -0.2253 0.1231 0.0458 370 PHE B CE2 10040 C CZ . PHE B 370 ? 1.3483 0.7304 1.1474 -0.2275 0.1102 0.0474 370 PHE B CZ 10041 N N . ASN B 371 ? 1.4963 0.8770 1.2797 -0.3105 0.1795 0.0906 371 ASN B N 10042 C CA . ASN B 371 ? 1.5595 0.9293 1.3148 -0.3310 0.1938 0.1037 371 ASN B CA 10043 C C . ASN B 371 ? 1.6088 0.9423 1.3292 -0.3348 0.1767 0.1193 371 ASN B C 10044 O O . ASN B 371 ? 1.6030 0.9215 1.3344 -0.3250 0.1554 0.1197 371 ASN B O 10045 C CB . ASN B 371 ? 1.5483 0.9262 1.3267 -0.3496 0.2032 0.1086 371 ASN B CB 10046 C CG . ASN B 371 ? 1.4482 0.8642 1.2634 -0.3478 0.2218 0.0943 371 ASN B CG 10047 O OD1 . ASN B 371 ? 1.5061 0.9409 1.3257 -0.3346 0.2305 0.0823 371 ASN B OD1 10048 N ND2 . ASN B 371 ? 1.6904 1.1174 1.5354 -0.3612 0.2270 0.0959 371 ASN B ND2 10049 N N . ALA B 372 ? 1.7479 1.0677 1.4273 -0.3495 0.1853 0.1316 372 ALA B N 10050 C CA . ALA B 372 ? 1.7273 1.0130 1.3735 -0.3533 0.1663 0.1483 372 ALA B CA 10051 C C . ALA B 372 ? 1.8902 1.1553 1.5078 -0.3806 0.1687 0.1706 372 ALA B C 10052 O O . ALA B 372 ? 1.9862 1.2614 1.5803 -0.3977 0.1911 0.1727 372 ALA B O 10053 C CB . ALA B 372 ? 1.5748 0.8585 1.1896 -0.3431 0.1664 0.1439 372 ALA B CB 10054 N N . THR B 373 ? 1.6806 0.9165 1.3012 -0.3854 0.1457 0.1870 373 THR B N 10055 C CA . THR B 373 ? 1.5421 0.7523 1.1331 -0.4115 0.1417 0.2129 373 THR B CA 10056 C C . THR B 373 ? 1.5404 0.7198 1.0977 -0.4107 0.1188 0.2294 373 THR B C 10057 O O . THR B 373 ? 1.6715 0.8328 1.2508 -0.3968 0.0938 0.2318 373 THR B O 10058 C CB . THR B 373 ? 1.7570 0.9545 1.3818 -0.4209 0.1313 0.2226 373 THR B CB 10059 O OG1 . THR B 373 ? 1.9192 1.1472 1.5795 -0.4203 0.1502 0.2060 373 THR B OG1 10060 C CG2 . THR B 373 ? 2.0087 1.1805 1.6015 -0.4509 0.1287 0.2517 373 THR B CG2 10061 N N . CYS B 374 ? 1.6743 0.8488 1.1797 -0.4262 0.1274 0.2395 374 CYS B N 10062 C CA . CYS B 374 ? 1.5998 0.7484 1.0702 -0.4261 0.1056 0.2544 374 CYS B CA 10063 C C . CYS B 374 ? 2.0244 1.1601 1.4591 -0.4502 0.0976 0.2812 374 CYS B C 10064 O O . CYS B 374 ? 2.3176 1.4360 1.7641 -0.4477 0.0687 0.2995 374 CYS B O 10065 C CB . CYS B 374 ? 1.5840 0.7490 1.0280 -0.4155 0.1177 0.2378 374 CYS B CB 10066 S SG . CYS B 374 ? 2.0946 1.2951 1.5862 -0.3842 0.1312 0.2033 374 CYS B SG 10067 N N . LEU B 375 ? 2.0237 1.1732 1.4196 -0.4715 0.1237 0.2812 375 LEU B N 10068 C CA . LEU B 375 ? 2.0507 1.1957 1.4083 -0.4949 0.1191 0.3038 375 LEU B CA 10069 C C . LEU B 375 ? 1.9502 1.1011 1.3316 -0.5099 0.1265 0.3136 375 LEU B C 10070 O O . LEU B 375 ? 1.7598 0.9317 1.1475 -0.5199 0.1573 0.3008 375 LEU B O 10071 C CB . LEU B 375 ? 2.0759 1.2336 1.3760 -0.5116 0.1449 0.2962 375 LEU B CB 10072 C CG . LEU B 375 ? 2.2437 1.4025 1.4953 -0.5405 0.1490 0.3142 375 LEU B CG 10073 C CD1 . LEU B 375 ? 2.2289 1.3635 1.4663 -0.5422 0.1096 0.3419 375 LEU B CD1 10074 C CD2 . LEU B 375 ? 2.4875 1.6600 1.6865 -0.5531 0.1770 0.2983 375 LEU B CD2 10075 N N . ASN B 376 ? 1.8646 0.9971 1.2631 -0.5109 0.0979 0.3361 376 ASN B N 10076 C CA . ASN B 376 ? 2.0894 1.2217 1.5194 -0.5219 0.0981 0.3474 376 ASN B CA 10077 C C . ASN B 376 ? 2.2191 1.3679 1.6946 -0.5149 0.1184 0.3258 376 ASN B C 10078 O O . ASN B 376 ? 2.2406 1.3864 1.7504 -0.4928 0.1106 0.3100 376 ASN B O 10079 C CB . ASN B 376 ? 1.9384 1.0771 1.3273 -0.5524 0.1114 0.3649 376 ASN B CB 10080 C CG . ASN B 376 ? 2.0756 1.2368 1.4173 -0.5668 0.1455 0.3502 376 ASN B CG 10081 O OD1 . ASN B 376 ? 2.3052 1.4894 1.6616 -0.5706 0.1769 0.3313 376 ASN B OD1 10082 N ND2 . ASN B 376 ? 2.0603 1.2154 1.3467 -0.5758 0.1397 0.3579 376 ASN B ND2 10083 N N . ASN B 377 ? 2.0084 1.1755 1.4844 -0.5346 0.1442 0.3248 377 ASN B N 10084 C CA . ASN B 377 ? 1.8746 1.0586 1.3968 -0.5309 0.1620 0.3063 377 ASN B CA 10085 C C . ASN B 377 ? 2.1243 1.3347 1.6386 -0.5301 0.1962 0.2808 377 ASN B C 10086 O O . ASN B 377 ? 2.1774 1.4050 1.7302 -0.5281 0.2128 0.2645 377 ASN B O 10087 C CB . ASN B 377 ? 1.9207 1.1106 1.4608 -0.5518 0.1692 0.3195 377 ASN B CB 10088 C CG . ASN B 377 ? 2.2202 1.3830 1.7690 -0.5541 0.1375 0.3458 377 ASN B CG 10089 O OD1 . ASN B 377 ? 2.0852 1.2262 1.6478 -0.5354 0.1089 0.3493 377 ASN B OD1 10090 N ND2 . ASN B 377 ? 2.2832 1.4476 1.8265 -0.5771 0.1432 0.3639 377 ASN B ND2 10091 N N . GLU B 378 ? 2.1543 1.3679 1.6215 -0.5319 0.2064 0.2767 378 GLU B N 10092 C CA . GLU B 378 ? 1.9890 1.2270 1.4495 -0.5316 0.2408 0.2519 378 GLU B CA 10093 C C . GLU B 378 ? 2.0860 1.3367 1.5866 -0.4963 0.2329 0.2280 378 GLU B C 10094 O O . GLU B 378 ? 1.9619 1.1951 1.4534 -0.4790 0.2097 0.2295 378 GLU B O 10095 C CB . GLU B 378 ? 2.1121 1.3526 1.5116 -0.5432 0.2535 0.2524 378 GLU B CB 10096 C CG . GLU B 378 ? 2.2492 1.4970 1.6143 -0.5721 0.2649 0.2678 378 GLU B CG 10097 C CD . GLU B 378 ? 2.3813 1.6356 1.6857 -0.5853 0.2827 0.2619 378 GLU B CD 10098 O OE1 . GLU B 378 ? 2.4086 1.6687 1.6777 -0.6100 0.2922 0.2731 378 GLU B OE1 10099 O OE2 . GLU B 378 ? 2.1591 1.4124 1.4508 -0.5716 0.2872 0.2455 378 GLU B OE2 10100 N N . VAL B 379 ? 2.1925 1.4771 1.7399 -0.4855 0.2512 0.2060 379 VAL B N 10101 C CA . VAL B 379 ? 2.0157 1.3174 1.6043 -0.4531 0.2435 0.1838 379 VAL B CA 10102 C C . VAL B 379 ? 1.9889 1.3152 1.5687 -0.4409 0.2638 0.1624 379 VAL B C 10103 O O . VAL B 379 ? 2.1249 1.4701 1.6921 -0.4556 0.2930 0.1554 379 VAL B O 10104 C CB . VAL B 379 ? 1.9624 1.2861 1.6112 -0.4471 0.2463 0.1730 379 VAL B CB 10105 C CG1 . VAL B 379 ? 2.0230 1.3200 1.6888 -0.4515 0.2207 0.1890 379 VAL B CG1 10106 C CG2 . VAL B 379 ? 1.9508 1.3024 1.6106 -0.4668 0.2784 0.1679 379 VAL B CG2 10107 N N . ILE B 380 ? 1.9466 1.2722 1.5348 -0.4147 0.2488 0.1515 380 ILE B N 10108 C CA . ILE B 380 ? 1.8434 1.1891 1.4278 -0.4007 0.2641 0.1315 380 ILE B CA 10109 C C . ILE B 380 ? 1.8865 1.2531 1.5220 -0.3731 0.2568 0.1137 380 ILE B C 10110 O O . ILE B 380 ? 1.9569 1.3124 1.5938 -0.3544 0.2355 0.1123 380 ILE B O 10111 C CB . ILE B 380 ? 1.6169 0.9398 1.1514 -0.3983 0.2531 0.1371 380 ILE B CB 10112 C CG1 . ILE B 380 ? 1.7722 1.0735 1.2505 -0.4281 0.2576 0.1569 380 ILE B CG1 10113 C CG2 . ILE B 380 ? 1.6492 0.9917 1.1826 -0.3844 0.2694 0.1153 380 ILE B CG2 10114 C CD1 . ILE B 380 ? 2.0355 1.3019 1.4992 -0.4365 0.2276 0.1836 380 ILE B CD1 10115 N N . PRO B 381 ? 1.9225 1.3202 1.6007 -0.3717 0.2742 0.1005 381 PRO B N 10116 C CA . PRO B 381 ? 1.9076 1.3269 1.6360 -0.3494 0.2661 0.0862 381 PRO B CA 10117 C C . PRO B 381 ? 1.7733 1.1985 1.5003 -0.3272 0.2626 0.0733 381 PRO B C 10118 O O . PRO B 381 ? 1.9369 1.3608 1.6356 -0.3292 0.2766 0.0686 381 PRO B O 10119 C CB . PRO B 381 ? 1.8902 1.3425 1.6584 -0.3573 0.2899 0.0763 381 PRO B CB 10120 C CG . PRO B 381 ? 1.8891 1.3321 1.6330 -0.3856 0.3043 0.0894 381 PRO B CG 10121 C CD . PRO B 381 ? 1.9280 1.3426 1.6100 -0.3939 0.3021 0.1000 381 PRO B CD 10122 N N . GLY B 382 ? 1.5914 1.0224 1.3474 -0.3078 0.2441 0.0677 382 GLY B N 10123 C CA . GLY B 382 ? 1.6148 1.0527 1.3744 -0.2873 0.2394 0.0568 382 GLY B CA 10124 C C . GLY B 382 ? 1.5572 0.9682 1.2778 -0.2808 0.2235 0.0630 382 GLY B C 10125 O O . GLY B 382 ? 1.7755 1.1890 1.4998 -0.2636 0.2147 0.0560 382 GLY B O 10126 N N . LEU B 383 ? 1.3990 0.7843 1.0838 -0.2954 0.2186 0.0773 383 LEU B N 10127 C CA . LEU B 383 ? 1.6289 0.9888 1.2778 -0.2912 0.2030 0.0846 383 LEU B CA 10128 C C . LEU B 383 ? 1.5658 0.9081 1.2242 -0.2847 0.1769 0.0924 383 LEU B C 10129 O O . LEU B 383 ? 1.5332 0.8659 1.2000 -0.2954 0.1708 0.1019 383 LEU B O 10130 C CB . LEU B 383 ? 1.7013 1.0425 1.3026 -0.3117 0.2112 0.0965 383 LEU B CB 10131 C CG . LEU B 383 ? 1.9130 1.2324 1.4745 -0.3085 0.1987 0.1018 383 LEU B CG 10132 C CD1 . LEU B 383 ? 1.7000 1.0335 1.2681 -0.2904 0.2039 0.0848 383 LEU B CD1 10133 C CD2 . LEU B 383 ? 2.0059 1.3097 1.5173 -0.3323 0.2080 0.1135 383 LEU B CD2 10134 N N . LYS B 384 ? 1.6925 1.0315 1.3527 -0.2673 0.1626 0.0871 384 LYS B N 10135 C CA . LYS B 384 ? 1.4130 0.7368 1.0839 -0.2598 0.1399 0.0907 384 LYS B CA 10136 C C . LYS B 384 ? 1.6042 0.8993 1.2436 -0.2630 0.1255 0.1036 384 LYS B C 10137 O O . LYS B 384 ? 1.6321 0.9142 1.2819 -0.2550 0.1067 0.1053 384 LYS B O 10138 C CB . LYS B 384 ? 1.4085 0.7483 1.1034 -0.2403 0.1331 0.0766 384 LYS B CB 10139 C CG . LYS B 384 ? 1.9033 1.2471 1.5820 -0.2293 0.1357 0.0708 384 LYS B CG 10140 C CD . LYS B 384 ? 1.9266 1.2897 1.6302 -0.2133 0.1317 0.0585 384 LYS B CD 10141 C CE . LYS B 384 ? 1.8711 1.2602 1.6030 -0.2136 0.1433 0.0513 384 LYS B CE 10142 N NZ . LYS B 384 ? 1.8379 1.2452 1.5911 -0.1999 0.1371 0.0422 384 LYS B NZ 10143 N N . SER B 385 ? 1.6096 0.8962 1.2121 -0.2749 0.1341 0.1114 385 SER B N 10144 C CA . SER B 385 ? 1.5211 0.7815 1.0911 -0.2794 0.1187 0.1249 385 SER B CA 10145 C C . SER B 385 ? 1.6001 0.8420 1.1356 -0.3037 0.1210 0.1437 385 SER B C 10146 O O . SER B 385 ? 1.6613 0.9134 1.1920 -0.3179 0.1403 0.1439 385 SER B O 10147 C CB . SER B 385 ? 1.6631 0.9279 1.2124 -0.2703 0.1219 0.1165 385 SER B CB 10148 O OG . SER B 385 ? 1.9726 1.2531 1.5073 -0.2771 0.1462 0.1080 385 SER B OG 10149 N N . CYS B 386 ? 1.6830 0.8981 1.1955 -0.3092 0.1005 0.1603 386 CYS B N 10150 C CA . CYS B 386 ? 1.7668 0.9609 1.2399 -0.3341 0.0981 0.1820 386 CYS B CA 10151 C C . CYS B 386 ? 1.7619 0.9375 1.1942 -0.3383 0.0837 0.1924 386 CYS B C 10152 O O . CYS B 386 ? 1.6634 0.8334 1.1084 -0.3218 0.0656 0.1896 386 CYS B O 10153 C CB . CYS B 386 ? 1.4737 0.6477 0.9664 -0.3421 0.0808 0.1996 386 CYS B CB 10154 S SG . CYS B 386 ? 2.2608 1.4514 1.7839 -0.3510 0.1000 0.1948 386 CYS B SG 10155 N N . MET B 387 ? 1.6559 0.8228 1.0386 -0.3619 0.0919 0.2042 387 MET B N 10156 C CA . MET B 387 ? 1.6261 0.7777 0.9633 -0.3693 0.0803 0.2128 387 MET B CA 10157 C C . MET B 387 ? 1.7364 0.8614 1.0296 -0.3980 0.0676 0.2419 387 MET B C 10158 O O . MET B 387 ? 2.0267 1.1495 1.3163 -0.4156 0.0769 0.2524 387 MET B O 10159 C CB . MET B 387 ? 1.8861 1.0571 1.1967 -0.3701 0.1064 0.1924 387 MET B CB 10160 C CG . MET B 387 ? 2.1267 1.2865 1.3997 -0.3710 0.0944 0.1934 387 MET B CG 10161 S SD . MET B 387 ? 2.4376 1.6154 1.6715 -0.3800 0.1279 0.1706 387 MET B SD 10162 C CE . MET B 387 ? 1.9135 1.0881 1.1044 -0.4154 0.1483 0.1831 387 MET B CE 10163 N N . GLY B 388 ? 1.6701 0.7751 0.9301 -0.4039 0.0451 0.2560 388 GLY B N 10164 C CA . GLY B 388 ? 1.8205 0.9078 1.0383 -0.4293 0.0296 0.2827 388 GLY B CA 10165 C C . GLY B 388 ? 1.9988 1.0778 1.2561 -0.4257 0.0027 0.3029 388 GLY B C 10166 O O . GLY B 388 ? 2.0192 1.0984 1.2651 -0.4439 0.0040 0.3182 388 GLY B O 10167 N N . LEU B 389 ? 1.9718 1.0435 1.2771 -0.4025 -0.0205 0.3021 389 LEU B N 10168 C CA . LEU B 389 ? 2.0990 1.1621 1.4506 -0.3961 -0.0450 0.3175 389 LEU B CA 10169 C C . LEU B 389 ? 2.1580 1.2068 1.5171 -0.3903 -0.0821 0.3345 389 LEU B C 10170 O O . LEU B 389 ? 1.9612 1.0080 1.3103 -0.3816 -0.0908 0.3284 389 LEU B O 10171 C CB . LEU B 389 ? 1.8785 0.9465 1.2904 -0.3741 -0.0397 0.2998 389 LEU B CB 10172 C CG . LEU B 389 ? 1.8603 0.9434 1.2740 -0.3765 -0.0054 0.2808 389 LEU B CG 10173 C CD1 . LEU B 389 ? 1.6396 0.7253 1.1122 -0.3566 -0.0062 0.2656 389 LEU B CD1 10174 C CD2 . LEU B 389 ? 2.2943 1.3822 1.6851 -0.4007 0.0100 0.2923 389 LEU B CD2 10175 N N . LYS B 390 ? 2.1083 1.1469 1.4871 -0.3956 -0.1042 0.3560 390 LYS B N 10176 C CA . LYS B 390 ? 2.1206 1.1461 1.5214 -0.3875 -0.1411 0.3720 390 LYS B CA 10177 C C . LYS B 390 ? 2.1416 1.1625 1.6172 -0.3668 -0.1542 0.3687 390 LYS B C 10178 O O . LYS B 390 ? 1.9255 0.9493 1.4256 -0.3667 -0.1397 0.3633 390 LYS B O 10179 C CB . LYS B 390 ? 2.0066 1.0217 1.3677 -0.4116 -0.1600 0.4009 390 LYS B CB 10180 C CG . LYS B 390 ? 2.1582 1.1705 1.5241 -0.4265 -0.1548 0.4153 390 LYS B CG 10181 C CD . LYS B 390 ? 2.3514 1.3521 1.6797 -0.4499 -0.1776 0.4453 390 LYS B CD 10182 C CE . LYS B 390 ? 2.4219 1.4275 1.6727 -0.4718 -0.1683 0.4463 390 LYS B CE 10183 N NZ . LYS B 390 ? 2.3421 1.3366 1.5519 -0.4971 -0.1915 0.4753 390 LYS B NZ 10184 N N . ILE B 391 ? 2.1194 1.1337 1.6322 -0.3496 -0.1806 0.3701 391 ILE B N 10185 C CA . ILE B 391 ? 1.8953 0.9062 1.4820 -0.3283 -0.1917 0.3622 391 ILE B CA 10186 C C . ILE B 391 ? 1.9167 0.9181 1.5273 -0.3364 -0.1980 0.3772 391 ILE B C 10187 O O . ILE B 391 ? 2.2287 1.2199 1.8159 -0.3533 -0.2149 0.4031 391 ILE B O 10188 C CB . ILE B 391 ? 1.9046 0.9096 1.5259 -0.3128 -0.2222 0.3661 391 ILE B CB 10189 C CG1 . ILE B 391 ? 2.0492 1.0625 1.6466 -0.3061 -0.2174 0.3526 391 ILE B CG1 10190 C CG2 . ILE B 391 ? 1.7537 0.7572 1.4531 -0.2904 -0.2292 0.3525 391 ILE B CG2 10191 C CD1 . ILE B 391 ? 1.9844 0.9946 1.6194 -0.2907 -0.2458 0.3544 391 ILE B CD1 10192 N N . GLY B 392 ? 1.8652 0.8694 1.5213 -0.3252 -0.1849 0.3605 392 GLY B N 10193 C CA . GLY B 392 ? 2.0299 1.0248 1.7122 -0.3322 -0.1880 0.3712 392 GLY B CA 10194 C C . GLY B 392 ? 1.9518 0.9553 1.6104 -0.3466 -0.1585 0.3656 392 GLY B C 10195 O O . GLY B 392 ? 1.7880 0.7862 1.4740 -0.3506 -0.1555 0.3680 392 GLY B O 10196 N N . ASP B 393 ? 2.0215 1.0384 1.6313 -0.3547 -0.1363 0.3571 393 ASP B N 10197 C CA . ASP B 393 ? 1.9867 1.0148 1.5746 -0.3686 -0.1064 0.3499 393 ASP B CA 10198 C C . ASP B 393 ? 1.7668 0.8036 1.3980 -0.3529 -0.0906 0.3229 393 ASP B C 10199 O O . ASP B 393 ? 1.5957 0.6344 1.2554 -0.3324 -0.0954 0.3050 393 ASP B O 10200 C CB . ASP B 393 ? 1.8432 0.8830 1.3661 -0.3824 -0.0868 0.3477 393 ASP B CB 10201 C CG . ASP B 393 ? 2.1277 1.1606 1.5987 -0.4049 -0.0972 0.3735 393 ASP B CG 10202 O OD1 . ASP B 393 ? 2.2904 1.3123 1.7696 -0.4157 -0.1119 0.3948 393 ASP B OD1 10203 O OD2 . ASP B 393 ? 2.0907 1.1286 1.5114 -0.4128 -0.0908 0.3719 393 ASP B OD2 10204 N N . THR B 394 ? 1.7958 0.8385 1.4311 -0.3639 -0.0720 0.3197 394 THR B N 10205 C CA . THR B 394 ? 1.5898 0.6408 1.2631 -0.3528 -0.0579 0.2949 394 THR B CA 10206 C C . THR B 394 ? 1.7326 0.8007 1.3768 -0.3664 -0.0273 0.2858 394 THR B C 10207 O O . THR B 394 ? 1.8674 0.9383 1.4855 -0.3873 -0.0170 0.3004 394 THR B O 10208 C CB . THR B 394 ? 1.6845 0.7246 1.4107 -0.3503 -0.0686 0.2966 394 THR B CB 10209 O OG1 . THR B 394 ? 1.9320 0.9552 1.6821 -0.3418 -0.0965 0.3099 394 THR B OG1 10210 C CG2 . THR B 394 ? 1.5519 0.5985 1.3204 -0.3353 -0.0602 0.2676 394 THR B CG2 10211 N N . VAL B 395 ? 1.5391 0.6191 1.1890 -0.3550 -0.0123 0.2613 395 VAL B N 10212 C CA . VAL B 395 ? 1.7492 0.8465 1.3784 -0.3658 0.0174 0.2500 395 VAL B CA 10213 C C . VAL B 395 ? 1.6052 0.7200 1.2804 -0.3535 0.0265 0.2260 395 VAL B C 10214 O O . VAL B 395 ? 1.5006 0.6103 1.2138 -0.3365 0.0122 0.2142 395 VAL B O 10215 C CB . VAL B 395 ? 1.5125 0.6277 1.1053 -0.3599 0.0322 0.2391 395 VAL B CB 10216 C CG1 . VAL B 395 ? 1.5582 0.6597 1.0986 -0.3768 0.0270 0.2613 395 VAL B CG1 10217 C CG2 . VAL B 395 ? 1.4709 0.5936 1.0875 -0.3329 0.0222 0.2205 395 VAL B CG2 10218 N N . SER B 396 ? 1.5105 0.6496 1.1840 -0.3619 0.0505 0.2175 396 SER B N 10219 C CA . SER B 396 ? 1.4442 0.6051 1.1599 -0.3523 0.0588 0.1958 396 SER B CA 10220 C C . SER B 396 ? 1.8247 1.0232 1.5374 -0.3426 0.0812 0.1749 396 SER B C 10221 O O . SER B 396 ? 1.6013 0.8106 1.2806 -0.3489 0.0968 0.1777 396 SER B O 10222 C CB . SER B 396 ? 1.4686 0.6238 1.2003 -0.3723 0.0631 0.2056 396 SER B CB 10223 O OG . SER B 396 ? 1.5985 0.7823 1.3622 -0.3670 0.0765 0.1846 396 SER B OG 10224 N N . PHE B 397 ? 1.6635 0.8813 1.4121 -0.3280 0.0819 0.1536 397 PHE B N 10225 C CA . PHE B 397 ? 1.3716 0.6247 1.1260 -0.3189 0.0997 0.1351 397 PHE B CA 10226 C C . PHE B 397 ? 1.4433 0.7140 1.2372 -0.3195 0.1027 0.1222 397 PHE B C 10227 O O . PHE B 397 ? 1.6498 0.9101 1.4699 -0.3148 0.0880 0.1160 397 PHE B O 10228 C CB . PHE B 397 ? 1.4985 0.7602 1.2501 -0.2971 0.0942 0.1213 397 PHE B CB 10229 C CG . PHE B 397 ? 1.6219 0.8693 1.3363 -0.2956 0.0909 0.1316 397 PHE B CG 10230 C CD1 . PHE B 397 ? 1.6672 0.9285 1.3533 -0.2985 0.1080 0.1312 397 PHE B CD1 10231 C CD2 . PHE B 397 ? 1.5579 0.7788 1.2689 -0.2912 0.0703 0.1402 397 PHE B CD2 10232 C CE1 . PHE B 397 ? 1.5133 0.7615 1.1636 -0.2985 0.1042 0.1393 397 PHE B CE1 10233 C CE2 . PHE B 397 ? 1.6645 0.8731 1.3422 -0.2906 0.0650 0.1500 397 PHE B CE2 10234 C CZ . PHE B 397 ? 1.6479 0.8699 1.2930 -0.2948 0.0819 0.1496 397 PHE B CZ 10235 N N . SER B 398 ? 1.5395 0.8375 1.3399 -0.3256 0.1215 0.1170 398 SER B N 10236 C CA . SER B 398 ? 1.5021 0.8220 1.3410 -0.3248 0.1234 0.1033 398 SER B CA 10237 C C . SER B 398 ? 1.6282 0.9780 1.4765 -0.3076 0.1278 0.0856 398 SER B C 10238 O O . SER B 398 ? 1.7473 1.1115 1.5800 -0.3036 0.1410 0.0848 398 SER B O 10239 C CB . SER B 398 ? 1.4106 0.7417 1.2598 -0.3448 0.1391 0.1103 398 SER B CB 10240 O OG . SER B 398 ? 1.6395 0.9913 1.4733 -0.3476 0.1604 0.1102 398 SER B OG 10241 N N . ILE B 399 ? 1.4706 0.8287 1.3441 -0.2982 0.1162 0.0715 399 ILE B N 10242 C CA . ILE B 399 ? 1.2630 0.6463 1.1436 -0.2828 0.1159 0.0569 399 ILE B CA 10243 C C . ILE B 399 ? 1.3063 0.7152 1.2209 -0.2859 0.1152 0.0462 399 ILE B C 10244 O O . ILE B 399 ? 1.3150 0.7169 1.2486 -0.2948 0.1077 0.0438 399 ILE B O 10245 C CB . ILE B 399 ? 1.3557 0.7269 1.2282 -0.2684 0.1010 0.0489 399 ILE B CB 10246 C CG1 . ILE B 399 ? 1.4266 0.7686 1.2720 -0.2675 0.0969 0.0610 399 ILE B CG1 10247 C CG2 . ILE B 399 ? 1.5530 0.9478 1.4240 -0.2541 0.1018 0.0382 399 ILE B CG2 10248 C CD1 . ILE B 399 ? 1.4589 0.7879 1.3033 -0.2548 0.0825 0.0530 399 ILE B CD1 10249 N N . GLU B 400 ? 1.3036 0.7416 1.2281 -0.2789 0.1218 0.0401 400 GLU B N 10250 C CA . GLU B 400 ? 1.2986 0.7631 1.2561 -0.2809 0.1175 0.0307 400 GLU B CA 10251 C C . GLU B 400 ? 1.2518 0.7316 1.2092 -0.2666 0.1069 0.0203 400 GLU B C 10252 O O . GLU B 400 ? 1.3766 0.8611 1.3193 -0.2553 0.1109 0.0216 400 GLU B O 10253 C CB . GLU B 400 ? 1.3989 0.8879 1.3782 -0.2882 0.1335 0.0343 400 GLU B CB 10254 C CG . GLU B 400 ? 1.4368 0.9568 1.4540 -0.2889 0.1273 0.0259 400 GLU B CG 10255 C CD . GLU B 400 ? 1.6957 1.2417 1.7421 -0.2955 0.1439 0.0286 400 GLU B CD 10256 O OE1 . GLU B 400 ? 1.7728 1.3149 1.8274 -0.3109 0.1550 0.0343 400 GLU B OE1 10257 O OE2 . GLU B 400 ? 1.6166 1.1872 1.6802 -0.2856 0.1460 0.0250 400 GLU B OE2 10258 N N . ALA B 401 ? 1.1936 0.6806 1.1660 -0.2685 0.0931 0.0100 401 ALA B N 10259 C CA . ALA B 401 ? 1.3552 0.8578 1.3249 -0.2587 0.0821 0.0010 401 ALA B CA 10260 C C . ALA B 401 ? 1.5807 1.1136 1.5804 -0.2639 0.0757 -0.0029 401 ALA B C 10261 O O . ALA B 401 ? 1.5774 1.1132 1.5964 -0.2756 0.0703 -0.0077 401 ALA B O 10262 C CB . ALA B 401 ? 1.3734 0.8590 1.3291 -0.2570 0.0703 -0.0098 401 ALA B CB 10263 N N . LYS B 402 ? 1.5217 1.0765 1.5274 -0.2554 0.0751 -0.0004 402 LYS B N 10264 C CA . LYS B 402 ? 1.5260 1.1112 1.5641 -0.2593 0.0670 -0.0013 402 LYS B CA 10265 C C . LYS B 402 ? 1.5349 1.1343 1.5650 -0.2509 0.0526 -0.0029 402 LYS B C 10266 O O . LYS B 402 ? 1.6829 1.2762 1.6930 -0.2395 0.0559 0.0007 402 LYS B O 10267 C CB . LYS B 402 ? 1.7119 1.3136 1.7787 -0.2593 0.0818 0.0065 402 LYS B CB 10268 C CG . LYS B 402 ? 1.7040 1.3381 1.8144 -0.2642 0.0735 0.0062 402 LYS B CG 10269 C CD . LYS B 402 ? 1.6643 1.3177 1.8055 -0.2591 0.0886 0.0118 402 LYS B CD 10270 C CE . LYS B 402 ? 1.7567 1.3965 1.8919 -0.2647 0.1132 0.0144 402 LYS B CE 10271 N NZ . LYS B 402 ? 1.7413 1.3764 1.8874 -0.2817 0.1154 0.0136 402 LYS B NZ 10272 N N . VAL B 403 ? 1.6101 1.2285 1.6554 -0.2581 0.0359 -0.0073 403 VAL B N 10273 C CA . VAL B 403 ? 1.8171 1.4491 1.8516 -0.2537 0.0197 -0.0069 403 VAL B CA 10274 C C . VAL B 403 ? 1.8235 1.4856 1.8941 -0.2529 0.0101 0.0017 403 VAL B C 10275 O O . VAL B 403 ? 1.8416 1.5164 1.9494 -0.2557 0.0172 0.0052 403 VAL B O 10276 C CB . VAL B 403 ? 1.6998 1.3299 1.7157 -0.2642 0.0044 -0.0193 403 VAL B CB 10277 C CG1 . VAL B 403 ? 1.6112 1.2123 1.5990 -0.2638 0.0129 -0.0295 403 VAL B CG1 10278 C CG2 . VAL B 403 ? 1.6421 1.2872 1.6873 -0.2787 -0.0051 -0.0238 403 VAL B CG2 10279 N N . ARG B 404 ? 1.6762 1.3499 1.7373 -0.2499 -0.0065 0.0057 404 ARG B N 10280 C CA . ARG B 404 ? 1.7146 1.4167 1.8109 -0.2505 -0.0224 0.0152 404 ARG B CA 10281 C C . ARG B 404 ? 1.6138 1.3271 1.6946 -0.2626 -0.0475 0.0123 404 ARG B C 10282 O O . ARG B 404 ? 1.5533 1.2578 1.5939 -0.2628 -0.0540 0.0100 404 ARG B O 10283 C CB . ARG B 404 ? 1.7298 1.4360 1.8332 -0.2356 -0.0207 0.0269 404 ARG B CB 10284 C CG . ARG B 404 ? 1.7560 1.4549 1.8774 -0.2251 0.0042 0.0282 404 ARG B CG 10285 C CD . ARG B 404 ? 1.8070 1.5145 1.9483 -0.2114 0.0035 0.0381 404 ARG B CD 10286 N NE . ARG B 404 ? 1.9782 1.6757 2.0831 -0.2063 -0.0078 0.0428 404 ARG B NE 10287 C CZ . ARG B 404 ? 2.0888 1.7634 2.1563 -0.1995 0.0046 0.0401 404 ARG B CZ 10288 N NH1 . ARG B 404 ? 2.1160 1.7742 2.1750 -0.1971 0.0271 0.0335 404 ARG B NH1 10289 N NH2 . ARG B 404 ? 2.0400 1.7084 2.0781 -0.1963 -0.0061 0.0447 404 ARG B NH2 10290 N N . GLY B 405 ? 1.7449 1.4784 1.8569 -0.2742 -0.0613 0.0120 405 GLY B N 10291 C CA . GLY B 405 ? 1.9026 1.6455 1.9966 -0.2896 -0.0845 0.0064 405 GLY B CA 10292 C C . GLY B 405 ? 1.8748 1.5941 1.9274 -0.2966 -0.0756 -0.0117 405 GLY B C 10293 O O . GLY B 405 ? 1.9557 1.6596 2.0156 -0.2967 -0.0588 -0.0198 405 GLY B O 10294 N N . CYS B 406 ? 1.7278 1.4439 1.7382 -0.3023 -0.0862 -0.0176 406 CYS B N 10295 C CA . CYS B 406 ? 1.7455 1.4399 1.7187 -0.3073 -0.0767 -0.0369 406 CYS B CA 10296 C C . CYS B 406 ? 1.7141 1.4113 1.6426 -0.3138 -0.0878 -0.0416 406 CYS B C 10297 O O . CYS B 406 ? 1.8429 1.5603 1.7656 -0.3256 -0.1094 -0.0368 406 CYS B O 10298 C CB . CYS B 406 ? 1.8911 1.5834 1.8768 -0.3221 -0.0787 -0.0530 406 CYS B CB 10299 S SG . CYS B 406 ? 2.4737 2.1968 2.4773 -0.3416 -0.1077 -0.0519 406 CYS B SG 10300 N N . PRO B 407 ? 1.6468 1.3242 1.5434 -0.3073 -0.0732 -0.0507 407 PRO B N 10301 C CA . PRO B 407 ? 1.7039 1.3820 1.5560 -0.3133 -0.0776 -0.0575 407 PRO B CA 10302 C C . PRO B 407 ? 1.9771 1.6551 1.8051 -0.3318 -0.0817 -0.0823 407 PRO B C 10303 O O . PRO B 407 ? 2.0714 1.7402 1.9154 -0.3367 -0.0764 -0.0978 407 PRO B O 10304 C CB . PRO B 407 ? 1.5296 1.1859 1.3681 -0.2975 -0.0571 -0.0591 407 PRO B CB 10305 C CG . PRO B 407 ? 1.5492 1.1971 1.4222 -0.2829 -0.0460 -0.0468 407 PRO B CG 10306 C CD . PRO B 407 ? 1.6611 1.3159 1.5654 -0.2918 -0.0511 -0.0503 407 PRO B CD 10307 N N . GLN B 408 ? 1.9954 1.6835 1.7844 -0.3430 -0.0909 -0.0859 408 GLN B N 10308 C CA . GLN B 408 ? 2.0426 1.7299 1.7990 -0.3606 -0.0901 -0.1129 408 GLN B CA 10309 C C . GLN B 408 ? 2.0128 1.6822 1.7469 -0.3522 -0.0685 -0.1277 408 GLN B C 10310 O O . GLN B 408 ? 2.1691 1.8382 1.8731 -0.3646 -0.0634 -0.1510 408 GLN B O 10311 C CB . GLN B 408 ? 2.0654 1.7759 1.7885 -0.3810 -0.1120 -0.1087 408 GLN B CB 10312 C CG . GLN B 408 ? 2.1136 1.8435 1.8610 -0.3916 -0.1367 -0.0960 408 GLN B CG 10313 C CD . GLN B 408 ? 2.2411 1.9680 2.0064 -0.4029 -0.1369 -0.1183 408 GLN B CD 10314 O OE1 . GLN B 408 ? 2.3307 2.0427 2.0823 -0.4074 -0.1218 -0.1460 408 GLN B OE1 10315 N NE2 . GLN B 408 ? 2.1925 1.9338 1.9927 -0.4077 -0.1543 -0.1066 408 GLN B NE2 10316 N N . GLU B 409 ? 1.9218 1.5770 1.6726 -0.3316 -0.0556 -0.1147 409 GLU B N 10317 C CA . GLU B 409 ? 2.0363 1.6792 1.7682 -0.3208 -0.0397 -0.1180 409 GLU B CA 10318 C C . GLU B 409 ? 2.1256 1.7544 1.8462 -0.3237 -0.0237 -0.1480 409 GLU B C 10319 O O . GLU B 409 ? 2.2081 1.8286 1.9167 -0.3149 -0.0109 -0.1509 409 GLU B O 10320 C CB . GLU B 409 ? 2.0539 1.6823 1.8118 -0.2992 -0.0298 -0.1002 409 GLU B CB 10321 C CG . GLU B 409 ? 2.1172 1.7553 1.8732 -0.2909 -0.0370 -0.0736 409 GLU B CG 10322 C CD . GLU B 409 ? 2.1577 1.7815 1.9394 -0.2715 -0.0261 -0.0597 409 GLU B CD 10323 O OE1 . GLU B 409 ? 2.1206 1.7269 1.9176 -0.2657 -0.0139 -0.0688 409 GLU B OE1 10324 O OE2 . GLU B 409 ? 2.1395 1.7688 1.9256 -0.2631 -0.0300 -0.0397 409 GLU B OE2 10325 N N . LYS B 410 ? 1.9277 1.5529 1.6577 -0.3347 -0.0242 -0.1701 410 LYS B N 10326 C CA . LYS B 410 ? 1.9783 1.5892 1.7062 -0.3375 -0.0093 -0.2018 410 LYS B CA 10327 C C . LYS B 410 ? 1.9464 1.5310 1.7097 -0.3198 0.0029 -0.2012 410 LYS B C 10328 O O . LYS B 410 ? 1.9433 1.5122 1.7142 -0.3170 0.0153 -0.2233 410 LYS B O 10329 C CB . LYS B 410 ? 2.1275 1.7445 1.8207 -0.3412 0.0008 -0.2148 410 LYS B CB 10330 C CG . LYS B 410 ? 2.1585 1.8006 1.8099 -0.3628 -0.0108 -0.2166 410 LYS B CG 10331 C CD . LYS B 410 ? 2.0381 1.6870 1.6843 -0.3836 -0.0182 -0.2406 410 LYS B CD 10332 C CE . LYS B 410 ? 1.9420 1.6158 1.5406 -0.4078 -0.0310 -0.2420 410 LYS B CE 10333 N NZ . LYS B 410 ? 1.9001 1.5793 1.4618 -0.4135 -0.0159 -0.2555 410 LYS B NZ 10334 N N . GLU B 411 ? 1.9632 1.5439 1.7470 -0.3082 -0.0009 -0.1747 411 GLU B N 10335 C CA . GLU B 411 ? 2.0698 1.6279 1.8868 -0.2962 0.0059 -0.1683 411 GLU B CA 10336 C C . GLU B 411 ? 2.0696 1.6089 1.8899 -0.2787 0.0184 -0.1616 411 GLU B C 10337 O O . GLU B 411 ? 2.2511 1.7746 2.0925 -0.2691 0.0217 -0.1479 411 GLU B O 10338 C CB . GLU B 411 ? 2.1794 1.7239 2.0156 -0.3052 0.0074 -0.1924 411 GLU B CB 10339 C CG . GLU B 411 ? 2.1919 1.7122 2.0386 -0.2968 0.0206 -0.2101 411 GLU B CG 10340 C CD . GLU B 411 ? 2.2933 1.8098 2.1430 -0.3093 0.0231 -0.2447 411 GLU B CD 10341 O OE1 . GLU B 411 ? 2.4167 1.9216 2.2912 -0.3158 0.0195 -0.2534 411 GLU B OE1 10342 O OE2 . GLU B 411 ? 2.2619 1.7870 2.0897 -0.3134 0.0297 -0.2644 411 GLU B OE2 10343 N N . LYS B 412 ? 1.8686 1.4109 1.6672 -0.2759 0.0248 -0.1699 412 LYS B N 10344 C CA . LYS B 412 ? 1.9154 1.4436 1.7154 -0.2599 0.0345 -0.1618 412 LYS B CA 10345 C C . LYS B 412 ? 1.8516 1.3523 1.6809 -0.2505 0.0401 -0.1625 412 LYS B C 10346 O O . LYS B 412 ? 1.8882 1.3776 1.7355 -0.2561 0.0408 -0.1808 412 LYS B O 10347 C CB . LYS B 412 ? 1.8061 1.3424 1.5970 -0.2514 0.0311 -0.1336 412 LYS B CB 10348 C CG . LYS B 412 ? 1.9177 1.4797 1.6878 -0.2612 0.0203 -0.1253 412 LYS B CG 10349 C CD . LYS B 412 ? 2.0768 1.6515 1.8167 -0.2713 0.0218 -0.1412 412 LYS B CD 10350 C CE . LYS B 412 ? 2.0438 1.6133 1.7721 -0.2608 0.0319 -0.1380 412 LYS B CE 10351 N NZ . LYS B 412 ? 1.9090 1.4934 1.6070 -0.2727 0.0353 -0.1530 412 LYS B NZ 10352 N N . SER B 413 ? 1.7503 1.2399 1.5836 -0.2374 0.0428 -0.1418 413 SER B N 10353 C CA . SER B 413 ? 1.4543 0.9179 1.3102 -0.2294 0.0454 -0.1344 413 SER B CA 10354 C C . SER B 413 ? 1.4816 0.9396 1.3289 -0.2170 0.0483 -0.1124 413 SER B C 10355 O O . SER B 413 ? 1.8871 1.3585 1.7149 -0.2132 0.0496 -0.1078 413 SER B O 10356 C CB . SER B 413 ? 1.4507 0.8962 1.3238 -0.2273 0.0494 -0.1554 413 SER B CB 10357 O OG . SER B 413 ? 1.5970 1.0404 1.4630 -0.2172 0.0550 -0.1568 413 SER B OG 10358 N N . PHE B 414 ? 1.2844 0.7220 1.1446 -0.2120 0.0490 -0.0988 414 PHE B N 10359 C CA . PHE B 414 ? 1.3404 0.7704 1.1905 -0.2017 0.0519 -0.0804 414 PHE B CA 10360 C C . PHE B 414 ? 1.3793 0.7813 1.2425 -0.1977 0.0515 -0.0725 414 PHE B C 10361 O O . PHE B 414 ? 1.2646 0.6518 1.1477 -0.2024 0.0486 -0.0798 414 PHE B O 10362 C CB . PHE B 414 ? 1.3087 0.7521 1.1498 -0.2021 0.0526 -0.0624 414 PHE B CB 10363 C CG . PHE B 414 ? 1.3259 0.7626 1.1813 -0.2081 0.0531 -0.0524 414 PHE B CG 10364 C CD1 . PHE B 414 ? 1.4749 0.8949 1.3289 -0.2051 0.0573 -0.0367 414 PHE B CD1 10365 C CD2 . PHE B 414 ? 1.2850 0.7332 1.1536 -0.2185 0.0495 -0.0585 414 PHE B CD2 10366 C CE1 . PHE B 414 ? 1.2895 0.7046 1.1548 -0.2128 0.0596 -0.0273 414 PHE B CE1 10367 C CE2 . PHE B 414 ? 1.2415 0.6851 1.1252 -0.2252 0.0511 -0.0492 414 PHE B CE2 10368 C CZ . PHE B 414 ? 1.2020 0.6293 1.0838 -0.2226 0.0571 -0.0335 414 PHE B CZ 10369 N N . THR B 415 ? 1.4155 0.8094 1.2670 -0.1900 0.0532 -0.0569 415 THR B N 10370 C CA . THR B 415 ? 1.2434 0.6107 1.1027 -0.1866 0.0501 -0.0479 415 THR B CA 10371 C C . THR B 415 ? 1.4141 0.7729 1.2600 -0.1878 0.0521 -0.0253 415 THR B C 10372 O O . THR B 415 ? 1.5383 0.9086 1.3658 -0.1843 0.0569 -0.0173 415 THR B O 10373 C CB . THR B 415 ? 1.2393 0.6014 1.0976 -0.1768 0.0488 -0.0532 415 THR B CB 10374 O OG1 . THR B 415 ? 1.5853 0.9557 1.4574 -0.1768 0.0497 -0.0768 415 THR B OG1 10375 C CG2 . THR B 415 ? 1.2004 0.5349 1.0691 -0.1736 0.0421 -0.0419 415 THR B CG2 10376 N N . ILE B 416 ? 1.4474 0.7854 1.3028 -0.1939 0.0489 -0.0158 416 ILE B N 10377 C CA . ILE B 416 ? 1.3018 0.6277 1.1411 -0.1973 0.0510 0.0052 416 ILE B CA 10378 C C . ILE B 416 ? 1.3519 0.6505 1.1934 -0.1947 0.0416 0.0138 416 ILE B C 10379 O O . ILE B 416 ? 1.2916 0.5758 1.1571 -0.1945 0.0334 0.0066 416 ILE B O 10380 C CB . ILE B 416 ? 1.2289 0.5539 1.0739 -0.2099 0.0549 0.0135 416 ILE B CB 10381 C CG1 . ILE B 416 ? 1.3394 0.6929 1.1892 -0.2122 0.0615 0.0045 416 ILE B CG1 10382 C CG2 . ILE B 416 ? 1.1669 0.4814 0.9909 -0.2156 0.0599 0.0338 416 ILE B CG2 10383 C CD1 . ILE B 416 ? 1.3236 0.6804 1.1844 -0.2247 0.0660 0.0108 416 ILE B CD1 10384 N N . LYS B 417 ? 1.4696 0.7604 1.2880 -0.1934 0.0418 0.0290 417 LYS B N 10385 C CA . LYS B 417 ? 1.2519 0.5202 1.0709 -0.1896 0.0302 0.0373 417 LYS B CA 10386 C C . LYS B 417 ? 1.3570 0.6185 1.1438 -0.1919 0.0313 0.0550 417 LYS B C 10387 O O . LYS B 417 ? 1.6877 0.9661 1.4547 -0.1894 0.0414 0.0535 417 LYS B O 10388 C CB . LYS B 417 ? 1.4081 0.6835 1.2422 -0.1772 0.0265 0.0208 417 LYS B CB 10389 C CG . LYS B 417 ? 1.6740 0.9291 1.5173 -0.1717 0.0132 0.0275 417 LYS B CG 10390 C CD . LYS B 417 ? 1.4667 0.7337 1.3264 -0.1600 0.0130 0.0094 417 LYS B CD 10391 C CE . LYS B 417 ? 1.1467 0.4319 0.9798 -0.1553 0.0207 0.0097 417 LYS B CE 10392 N NZ . LYS B 417 ? 1.3859 0.6569 1.1962 -0.1566 0.0144 0.0296 417 LYS B NZ 10393 N N . PRO B 418 ? 1.4761 0.7117 1.2576 -0.1977 0.0199 0.0720 418 PRO B N 10394 C CA . PRO B 418 ? 1.4096 0.6360 1.1582 -0.2011 0.0178 0.0881 418 PRO B CA 10395 C C . PRO B 418 ? 1.4192 0.6495 1.1678 -0.1884 0.0117 0.0818 418 PRO B C 10396 O O . PRO B 418 ? 1.3838 0.6140 1.1621 -0.1790 0.0040 0.0705 418 PRO B O 10397 C CB . PRO B 418 ? 1.3500 0.5465 1.0980 -0.2123 0.0031 0.1084 418 PRO B CB 10398 C CG . PRO B 418 ? 1.3591 0.5470 1.1500 -0.2076 -0.0069 0.0995 418 PRO B CG 10399 C CD . PRO B 418 ? 1.4182 0.6308 1.2242 -0.2036 0.0074 0.0783 418 PRO B CD 10400 N N . VAL B 419 ? 1.4284 0.6626 1.1459 -0.1889 0.0162 0.0875 419 VAL B N 10401 C CA . VAL B 419 ? 1.3130 0.5522 1.0295 -0.1780 0.0113 0.0819 419 VAL B CA 10402 C C . VAL B 419 ? 1.2993 0.5166 1.0256 -0.1769 -0.0093 0.0925 419 VAL B C 10403 O O . VAL B 419 ? 1.5883 0.7838 1.3030 -0.1876 -0.0200 0.1109 419 VAL B O 10404 C CB . VAL B 419 ? 1.3810 0.6287 1.0625 -0.1797 0.0215 0.0844 419 VAL B CB 10405 C CG1 . VAL B 419 ? 1.3620 0.6336 1.0435 -0.1774 0.0397 0.0723 419 VAL B CG1 10406 C CG2 . VAL B 419 ? 1.6497 0.8798 1.2978 -0.1943 0.0200 0.1025 419 VAL B CG2 10407 N N . GLY B 420 ? 1.3764 0.6000 1.1256 -0.1648 -0.0153 0.0816 420 GLY B N 10408 C CA . GLY B 420 ? 1.5971 0.8034 1.3639 -0.1617 -0.0356 0.0899 420 GLY B CA 10409 C C . GLY B 420 ? 1.6187 0.8093 1.4247 -0.1613 -0.0478 0.0907 420 GLY B C 10410 O O . GLY B 420 ? 1.9696 1.1437 1.7982 -0.1586 -0.0671 0.0990 420 GLY B O 10411 N N . PHE B 421 ? 1.3951 0.5906 1.2123 -0.1639 -0.0376 0.0819 421 PHE B N 10412 C CA . PHE B 421 ? 1.4288 0.6083 1.2843 -0.1645 -0.0476 0.0808 421 PHE B CA 10413 C C . PHE B 421 ? 1.5260 0.7215 1.4207 -0.1539 -0.0399 0.0530 421 PHE B C 10414 O O . PHE B 421 ? 1.4860 0.7060 1.3707 -0.1513 -0.0232 0.0365 421 PHE B O 10415 C CB . PHE B 421 ? 1.4752 0.6445 1.3159 -0.1784 -0.0435 0.0925 421 PHE B CB 10416 C CG . PHE B 421 ? 1.7213 0.8636 1.5411 -0.1913 -0.0586 0.1214 421 PHE B CG 10417 C CD1 . PHE B 421 ? 1.8118 0.9416 1.6224 -0.1903 -0.0753 0.1359 421 PHE B CD1 10418 C CD2 . PHE B 421 ? 1.4591 0.5888 1.2681 -0.2062 -0.0570 0.1350 421 PHE B CD2 10419 C CE1 . PHE B 421 ? 1.8044 0.9090 1.5912 -0.2046 -0.0909 0.1642 421 PHE B CE1 10420 C CE2 . PHE B 421 ? 1.5391 0.6438 1.3245 -0.2209 -0.0707 0.1632 421 PHE B CE2 10421 C CZ . PHE B 421 ? 1.8446 0.9365 1.6172 -0.2205 -0.0883 0.1782 421 PHE B CZ 10422 N N . LYS B 422 ? 1.4377 0.6189 1.3778 -0.1487 -0.0526 0.0478 422 LYS B N 10423 C CA . LYS B 422 ? 1.3172 0.5116 1.2969 -0.1404 -0.0446 0.0189 422 LYS B CA 10424 C C . LYS B 422 ? 1.3817 0.5770 1.3649 -0.1479 -0.0355 0.0100 422 LYS B C 10425 O O . LYS B 422 ? 1.6167 0.8337 1.6025 -0.1462 -0.0208 -0.0131 422 LYS B O 10426 C CB . LYS B 422 ? 1.4257 0.6042 1.4593 -0.1318 -0.0606 0.0141 422 LYS B CB 10427 C CG . LYS B 422 ? 1.7332 0.9261 1.8100 -0.1235 -0.0500 -0.0198 422 LYS B CG 10428 C CD . LYS B 422 ? 1.9496 1.1745 2.0116 -0.1178 -0.0331 -0.0389 422 LYS B CD 10429 C CE . LYS B 422 ? 1.8840 1.1245 1.9856 -0.1120 -0.0212 -0.0738 422 LYS B CE 10430 N NZ . LYS B 422 ? 1.8287 1.0703 1.9314 -0.1193 -0.0120 -0.0884 422 LYS B NZ 10431 N N . ASP B 423 ? 1.4387 0.6102 1.4205 -0.1578 -0.0453 0.0293 423 ASP B N 10432 C CA . ASP B 423 ? 1.5070 0.6763 1.4962 -0.1663 -0.0391 0.0230 423 ASP B CA 10433 C C . ASP B 423 ? 1.4565 0.6492 1.4063 -0.1731 -0.0215 0.0214 423 ASP B C 10434 O O . ASP B 423 ? 1.2367 0.4371 1.1491 -0.1750 -0.0171 0.0348 423 ASP B O 10435 C CB . ASP B 423 ? 1.5325 0.6694 1.5295 -0.1768 -0.0548 0.0475 423 ASP B CB 10436 C CG . ASP B 423 ? 1.7196 0.8317 1.7659 -0.1699 -0.0745 0.0486 423 ASP B CG 10437 O OD1 . ASP B 423 ? 1.6088 0.7107 1.6544 -0.1656 -0.0887 0.0640 423 ASP B OD1 10438 O OD2 . ASP B 423 ? 1.7426 0.8456 1.8309 -0.1688 -0.0764 0.0332 423 ASP B OD2 10439 N N . SER B 424 ? 1.5367 0.7405 1.4977 -0.1769 -0.0122 0.0041 424 SER B N 10440 C CA . SER B 424 ? 1.6077 0.8362 1.5396 -0.1822 0.0027 0.0005 424 SER B CA 10441 C C . SER B 424 ? 1.3564 0.5873 1.3023 -0.1917 0.0068 -0.0087 424 SER B C 10442 O O . SER B 424 ? 1.2856 0.5027 1.2656 -0.1924 0.0007 -0.0201 424 SER B O 10443 C CB . SER B 424 ? 1.4426 0.6990 1.3660 -0.1732 0.0126 -0.0185 424 SER B CB 10444 O OG . SER B 424 ? 1.4488 0.7112 1.4024 -0.1691 0.0141 -0.0447 424 SER B OG 10445 N N . LEU B 425 ? 1.3037 0.5523 1.2260 -0.1989 0.0170 -0.0045 425 LEU B N 10446 C CA . LEU B 425 ? 1.2048 0.4614 1.1388 -0.2083 0.0214 -0.0139 425 LEU B CA 10447 C C . LEU B 425 ? 1.2504 0.5373 1.1803 -0.2050 0.0298 -0.0361 425 LEU B C 10448 O O . LEU B 425 ? 1.4937 0.8018 1.3995 -0.2035 0.0370 -0.0320 425 LEU B O 10449 C CB . LEU B 425 ? 1.3377 0.5948 1.2537 -0.2202 0.0263 0.0062 425 LEU B CB 10450 C CG . LEU B 425 ? 1.3353 0.6077 1.2605 -0.2305 0.0324 -0.0014 425 LEU B CG 10451 C CD1 . LEU B 425 ? 1.2309 0.4852 1.1892 -0.2372 0.0245 -0.0105 425 LEU B CD1 10452 C CD2 . LEU B 425 ? 1.2374 0.5153 1.1444 -0.2408 0.0405 0.0181 425 LEU B CD2 10453 N N . ILE B 426 ? 1.2804 0.5689 1.2343 -0.2049 0.0283 -0.0595 426 ILE B N 10454 C CA . ILE B 426 ? 1.2324 0.5488 1.1793 -0.2049 0.0349 -0.0809 426 ILE B CA 10455 C C . ILE B 426 ? 1.2238 0.5521 1.1739 -0.2171 0.0363 -0.0858 426 ILE B C 10456 O O . ILE B 426 ? 1.3921 0.7058 1.3659 -0.2246 0.0321 -0.0919 426 ILE B O 10457 C CB . ILE B 426 ? 1.2904 0.6060 1.2576 -0.1997 0.0349 -0.1077 426 ILE B CB 10458 C CG1 . ILE B 426 ? 1.4587 0.7727 1.4209 -0.1874 0.0353 -0.1050 426 ILE B CG1 10459 C CG2 . ILE B 426 ? 1.2821 0.6245 1.2404 -0.2054 0.0410 -0.1306 426 ILE B CG2 10460 C CD1 . ILE B 426 ? 1.6704 0.9890 1.6531 -0.1822 0.0387 -0.1330 426 ILE B CD1 10461 N N . VAL B 427 ? 1.1931 0.5475 1.1221 -0.2193 0.0409 -0.0827 427 VAL B N 10462 C CA . VAL B 427 ? 1.2431 0.6123 1.1764 -0.2307 0.0407 -0.0854 427 VAL B CA 10463 C C . VAL B 427 ? 1.3123 0.7061 1.2389 -0.2340 0.0405 -0.1065 427 VAL B C 10464 O O . VAL B 427 ? 1.5056 0.9193 1.4110 -0.2298 0.0427 -0.1047 427 VAL B O 10465 C CB . VAL B 427 ? 1.2384 0.6197 1.1587 -0.2327 0.0448 -0.0637 427 VAL B CB 10466 C CG1 . VAL B 427 ? 1.1981 0.5963 1.1298 -0.2446 0.0435 -0.0666 427 VAL B CG1 10467 C CG2 . VAL B 427 ? 1.2200 0.5782 1.1400 -0.2325 0.0464 -0.0428 427 VAL B CG2 10468 N N . GLN B 428 ? 1.5092 0.9009 1.4527 -0.2430 0.0373 -0.1263 428 GLN B N 10469 C CA . GLN B 428 ? 1.4098 0.8250 1.3435 -0.2503 0.0361 -0.1467 428 GLN B CA 10470 C C . GLN B 428 ? 1.5208 0.9559 1.4523 -0.2605 0.0316 -0.1377 428 GLN B C 10471 O O . GLN B 428 ? 1.8681 1.2959 1.8198 -0.2692 0.0285 -0.1355 428 GLN B O 10472 C CB . GLN B 428 ? 1.3105 0.7148 1.2630 -0.2565 0.0354 -0.1756 428 GLN B CB 10473 C CG . GLN B 428 ? 1.3018 0.6863 1.2669 -0.2457 0.0396 -0.1862 428 GLN B CG 10474 C CD . GLN B 428 ? 1.3519 0.7234 1.3440 -0.2512 0.0398 -0.2162 428 GLN B CD 10475 O OE1 . GLN B 428 ? 1.4965 0.8692 1.4984 -0.2637 0.0361 -0.2273 428 GLN B OE1 10476 N NE2 . GLN B 428 ? 1.4438 0.8031 1.4513 -0.2420 0.0443 -0.2307 428 GLN B NE2 10477 N N . VAL B 429 ? 1.3494 0.8099 1.2595 -0.2599 0.0303 -0.1318 429 VAL B N 10478 C CA . VAL B 429 ? 1.3684 0.8503 1.2809 -0.2679 0.0245 -0.1215 429 VAL B CA 10479 C C . VAL B 429 ? 1.4071 0.9065 1.3157 -0.2817 0.0160 -0.1409 429 VAL B C 10480 O O . VAL B 429 ? 1.4258 0.9296 1.3167 -0.2835 0.0164 -0.1585 429 VAL B O 10481 C CB . VAL B 429 ? 1.3879 0.8874 1.2843 -0.2598 0.0251 -0.1026 429 VAL B CB 10482 C CG1 . VAL B 429 ? 1.5902 1.1068 1.5019 -0.2651 0.0209 -0.0883 429 VAL B CG1 10483 C CG2 . VAL B 429 ? 1.4208 0.9030 1.3114 -0.2462 0.0339 -0.0894 429 VAL B CG2 10484 N N . THR B 430 ? 1.5649 1.0748 1.4898 -0.2929 0.0087 -0.1384 430 THR B N 10485 C CA . THR B 430 ? 1.4660 0.9945 1.3855 -0.3081 -0.0020 -0.1550 430 THR B CA 10486 C C . THR B 430 ? 1.5426 1.0945 1.4747 -0.3153 -0.0123 -0.1397 430 THR B C 10487 O O . THR B 430 ? 1.6309 1.1796 1.5869 -0.3127 -0.0091 -0.1237 430 THR B O 10488 C CB . THR B 430 ? 1.5416 1.0537 1.4768 -0.3187 -0.0023 -0.1794 430 THR B CB 10489 O OG1 . THR B 430 ? 1.8664 1.3530 1.8288 -0.3140 0.0036 -0.1708 430 THR B OG1 10490 C CG2 . THR B 430 ? 1.3263 0.8301 1.2445 -0.3176 0.0035 -0.2046 430 THR B CG2 10491 N N . PHE B 431 ? 1.6633 1.2395 1.5799 -0.3254 -0.0248 -0.1446 431 PHE B N 10492 C CA . PHE B 431 ? 1.6840 1.2850 1.6159 -0.3321 -0.0378 -0.1298 431 PHE B CA 10493 C C . PHE B 431 ? 1.6449 1.2603 1.5761 -0.3522 -0.0532 -0.1462 431 PHE B C 10494 O O . PHE B 431 ? 1.7805 1.4018 1.6811 -0.3611 -0.0587 -0.1624 431 PHE B O 10495 C CB . PHE B 431 ? 1.6582 1.2783 1.5742 -0.3244 -0.0433 -0.1115 431 PHE B CB 10496 C CG . PHE B 431 ? 1.5009 1.1080 1.4132 -0.3056 -0.0290 -0.0974 431 PHE B CG 10497 C CD1 . PHE B 431 ? 1.5223 1.1175 1.4057 -0.2984 -0.0211 -0.1044 431 PHE B CD1 10498 C CD2 . PHE B 431 ? 1.4862 1.0942 1.4240 -0.2964 -0.0230 -0.0783 431 PHE B CD2 10499 C CE1 . PHE B 431 ? 1.5535 1.1369 1.4333 -0.2822 -0.0096 -0.0916 431 PHE B CE1 10500 C CE2 . PHE B 431 ? 1.4316 1.0275 1.3629 -0.2809 -0.0102 -0.0669 431 PHE B CE2 10501 C CZ . PHE B 431 ? 1.4240 1.0072 1.3261 -0.2738 -0.0046 -0.0730 431 PHE B CZ 10502 N N . ASP B 432 ? 1.6616 1.2832 1.6255 -0.3609 -0.0597 -0.1429 432 ASP B N 10503 C CA . ASP B 432 ? 1.8671 1.5076 1.8326 -0.3806 -0.0781 -0.1540 432 ASP B CA 10504 C C . ASP B 432 ? 1.8695 1.5386 1.8581 -0.3822 -0.0926 -0.1314 432 ASP B C 10505 O O . ASP B 432 ? 1.7299 1.4018 1.7576 -0.3804 -0.0896 -0.1199 432 ASP B O 10506 C CB . ASP B 432 ? 1.8454 1.4703 1.8339 -0.3925 -0.0763 -0.1724 432 ASP B CB 10507 C CG . ASP B 432 ? 1.7677 1.3754 1.7918 -0.3838 -0.0631 -0.1593 432 ASP B CG 10508 O OD1 . ASP B 432 ? 1.6316 1.2361 1.6568 -0.3678 -0.0523 -0.1399 432 ASP B OD1 10509 O OD2 . ASP B 432 ? 1.8438 1.4408 1.8932 -0.3944 -0.0634 -0.1686 432 ASP B OD2 10510 N N . CYS B 433 ? 1.8700 1.5605 1.8356 -0.3862 -0.1083 -0.1249 433 CYS B N 10511 C CA . CYS B 433 ? 1.7884 1.5065 1.7781 -0.3860 -0.1247 -0.1020 433 CYS B CA 10512 C C . CYS B 433 ? 1.9104 1.6508 1.9085 -0.4076 -0.1495 -0.1078 433 CYS B C 10513 O O . CYS B 433 ? 1.9777 1.7431 2.0018 -0.4098 -0.1672 -0.0898 433 CYS B O 10514 C CB . CYS B 433 ? 1.8315 1.5584 1.7955 -0.3761 -0.1293 -0.0861 433 CYS B CB 10515 S SG . CYS B 433 ? 2.0906 1.7910 2.0367 -0.3533 -0.1021 -0.0829 433 CYS B SG 10516 N N . ASP B 434 ? 2.0326 1.7636 2.0107 -0.4237 -0.1513 -0.1336 434 ASP B N 10517 C CA . ASP B 434 ? 2.0839 1.8345 2.0601 -0.4472 -0.1759 -0.1428 434 ASP B CA 10518 C C . ASP B 434 ? 2.0709 1.8067 2.0591 -0.4609 -0.1713 -0.1690 434 ASP B C 10519 O O . ASP B 434 ? 2.1057 1.8137 2.0926 -0.4535 -0.1499 -0.1834 434 ASP B O 10520 C CB . ASP B 434 ? 2.1029 1.8633 2.0236 -0.4593 -0.1897 -0.1494 434 ASP B CB 10521 C CG . ASP B 434 ? 2.1597 1.8981 2.0393 -0.4503 -0.1681 -0.1633 434 ASP B CG 10522 O OD1 . ASP B 434 ? 2.1172 1.8304 2.0058 -0.4429 -0.1467 -0.1799 434 ASP B OD1 10523 O OD2 . ASP B 434 ? 2.1909 1.9375 2.0316 -0.4510 -0.1732 -0.1565 434 ASP B OD2 10524 N N . CYS B 435 ? 2.0355 1.7895 2.0375 -0.4812 -0.1929 -0.1745 435 CYS B N 10525 C CA . CYS B 435 ? 2.0694 1.8107 2.0871 -0.4963 -0.1913 -0.1992 435 CYS B CA 10526 C C . CYS B 435 ? 2.0766 1.8032 2.0474 -0.5098 -0.1882 -0.2328 435 CYS B C 10527 O O . CYS B 435 ? 2.2252 1.9544 2.1494 -0.5091 -0.1875 -0.2364 435 CYS B O 10528 C CB . CYS B 435 ? 2.1760 1.9434 2.2271 -0.5144 -0.2166 -0.1939 435 CYS B CB 10529 S SG . CYS B 435 ? 2.6924 2.4790 2.8115 -0.5009 -0.2172 -0.1600 435 CYS B SG 10530 N N . ALA B 436 ? 2.0292 1.7406 2.0143 -0.5228 -0.1855 -0.2583 436 ALA B N 10531 C CA . ALA B 436 ? 2.0877 1.7831 2.0364 -0.5357 -0.1795 -0.2954 436 ALA B CA 10532 C C . ALA B 436 ? 2.2336 1.9525 2.1461 -0.5628 -0.2037 -0.3103 436 ALA B C 10533 O O . ALA B 436 ? 2.2667 1.9816 2.1322 -0.5733 -0.1994 -0.3361 436 ALA B O 10534 C CB . ALA B 436 ? 2.0656 1.7325 2.0480 -0.5384 -0.1671 -0.3174 436 ALA B CB 10535 N N . CYS B 437 ? 2.2550 1.9994 2.1898 -0.5752 -0.2289 -0.2941 437 CYS B N 10536 C CA . CYS B 437 ? 2.1979 1.9640 2.1036 -0.6044 -0.2558 -0.3077 437 CYS B CA 10537 C C . CYS B 437 ? 2.2846 2.0709 2.1329 -0.6109 -0.2691 -0.2980 437 CYS B C 10538 O O . CYS B 437 ? 2.3284 2.1312 2.1396 -0.6373 -0.2906 -0.3106 437 CYS B O 10539 C CB . CYS B 437 ? 2.1152 1.9042 2.0682 -0.6149 -0.2810 -0.2902 437 CYS B CB 10540 S SG . CYS B 437 ? 3.1064 2.9231 3.0940 -0.5960 -0.2940 -0.2402 437 CYS B SG 10541 N N . GLN B 438 ? 2.2771 2.0614 2.1164 -0.5885 -0.2571 -0.2754 438 GLN B N 10542 C CA . GLN B 438 ? 2.3177 2.1200 2.1061 -0.5936 -0.2698 -0.2612 438 GLN B CA 10543 C C . GLN B 438 ? 2.3943 2.1887 2.1173 -0.6095 -0.2593 -0.2941 438 GLN B C 10544 O O . GLN B 438 ? 2.3776 2.1898 2.0492 -0.6259 -0.2750 -0.2894 438 GLN B O 10545 C CB . GLN B 438 ? 2.3149 2.1149 2.1152 -0.5649 -0.2580 -0.2296 438 GLN B CB 10546 C CG . GLN B 438 ? 2.3823 2.1975 2.2408 -0.5516 -0.2710 -0.1948 438 GLN B CG 10547 C CD . GLN B 438 ? 2.4159 2.2302 2.2808 -0.5258 -0.2611 -0.1657 438 GLN B CD 10548 O OE1 . GLN B 438 ? 2.4179 2.2466 2.3261 -0.5143 -0.2710 -0.1373 438 GLN B OE1 10549 N NE2 . GLN B 438 ? 2.3826 2.1806 2.2070 -0.5169 -0.2410 -0.1739 438 GLN B NE2 10550 N N . ALA B 439 ? 2.4433 2.2112 2.1699 -0.6054 -0.2326 -0.3274 439 ALA B N 10551 C CA . ALA B 439 ? 2.4112 2.1706 2.0841 -0.6188 -0.2174 -0.3639 439 ALA B CA 10552 C C . ALA B 439 ? 2.4302 2.2023 2.0700 -0.6544 -0.2358 -0.3924 439 ALA B C 10553 O O . ALA B 439 ? 2.5400 2.3101 2.1300 -0.6713 -0.2254 -0.4253 439 ALA B O 10554 C CB . ALA B 439 ? 2.3735 2.1000 2.0705 -0.6019 -0.1845 -0.3904 439 ALA B CB 10555 N N . GLN B 440 ? 2.3299 2.1164 1.9985 -0.6665 -0.2627 -0.3805 440 GLN B N 10556 C CA . GLN B 440 ? 2.3464 2.1437 1.9919 -0.7006 -0.2825 -0.4073 440 GLN B CA 10557 C C . GLN B 440 ? 2.5130 2.3415 2.1027 -0.7260 -0.3138 -0.3920 440 GLN B C 10558 O O . GLN B 440 ? 2.5770 2.4194 2.1466 -0.7564 -0.3372 -0.4071 440 GLN B O 10559 C CB . GLN B 440 ? 2.2535 2.0499 1.9617 -0.7027 -0.2962 -0.4043 440 GLN B CB 10560 C CG . GLN B 440 ? 2.2270 1.9899 1.9801 -0.6881 -0.2679 -0.4287 440 GLN B CG 10561 C CD . GLN B 440 ? 2.3411 2.1028 2.1581 -0.6899 -0.2800 -0.4216 440 GLN B CD 10562 O OE1 . GLN B 440 ? 2.3462 2.1335 2.1828 -0.6969 -0.3073 -0.3946 440 GLN B OE1 10563 N NE2 . GLN B 440 ? 2.3813 2.1133 2.2343 -0.6839 -0.2599 -0.4453 440 GLN B NE2 10564 N N . ALA B 441 ? 2.5608 2.3995 2.1265 -0.7144 -0.3157 -0.3608 441 ALA B N 10565 C CA . ALA B 441 ? 2.6736 2.5388 2.1801 -0.7381 -0.3438 -0.3436 441 ALA B CA 10566 C C . ALA B 441 ? 2.7802 2.6712 2.3060 -0.7556 -0.3875 -0.3190 441 ALA B C 10567 O O . ALA B 441 ? 2.6285 2.5279 2.2101 -0.7364 -0.4010 -0.2824 441 ALA B O 10568 C CB . ALA B 441 ? 2.7342 2.5988 2.1656 -0.7679 -0.3341 -0.3849 441 ALA B CB 10569 N N . GLU B 442 ? 3.0081 2.9126 2.4879 -0.7927 -0.4092 -0.3399 442 GLU B N 10570 C CA . GLU B 442 ? 3.0509 2.9833 2.5356 -0.8152 -0.4559 -0.3162 442 GLU B CA 10571 C C . GLU B 442 ? 3.0390 2.9917 2.5071 -0.8115 -0.4815 -0.2675 442 GLU B C 10572 O O . GLU B 442 ? 3.0534 3.0163 2.5817 -0.7919 -0.4982 -0.2294 442 GLU B O 10573 C CB . GLU B 442 ? 2.9569 2.8906 2.5277 -0.8028 -0.4659 -0.3069 442 GLU B CB 10574 C CG . GLU B 442 ? 2.9380 2.8461 2.5397 -0.7989 -0.4371 -0.3485 442 GLU B CG 10575 C CD . GLU B 442 ? 3.0035 2.9083 2.5511 -0.8343 -0.4382 -0.3958 442 GLU B CD 10576 O OE1 . GLU B 442 ? 3.0773 3.0054 2.5856 -0.8653 -0.4720 -0.3930 442 GLU B OE1 10577 O OE2 . GLU B 442 ? 3.0309 2.9095 2.5770 -0.8301 -0.4049 -0.4359 442 GLU B OE2 10578 N N . PRO B 443 ? 2.9921 2.9505 2.3795 -0.8313 -0.4838 -0.2694 443 PRO B N 10579 C CA . PRO B 443 ? 2.8949 2.8644 2.2624 -0.8234 -0.4981 -0.2254 443 PRO B CA 10580 C C . PRO B 443 ? 2.8438 2.8392 2.2409 -0.8290 -0.5479 -0.1781 443 PRO B C 10581 O O . PRO B 443 ? 2.7108 2.7075 2.1564 -0.8002 -0.5506 -0.1410 443 PRO B O 10582 C CB . PRO B 443 ? 2.9144 2.8870 2.1821 -0.8547 -0.4938 -0.2444 443 PRO B CB 10583 C CG . PRO B 443 ? 2.9087 2.8835 2.1495 -0.8826 -0.4943 -0.2868 443 PRO B CG 10584 C CD . PRO B 443 ? 2.9256 2.8819 2.2353 -0.8659 -0.4751 -0.3134 443 PRO B CD 10585 N N . ASN B 444 ? 2.9306 2.9463 2.3030 -0.8641 -0.5868 -0.1787 444 ASN B N 10586 C CA . ASN B 444 ? 2.8824 2.9225 2.3006 -0.8654 -0.6347 -0.1336 444 ASN B CA 10587 C C . ASN B 444 ? 2.7999 2.8578 2.2501 -0.8877 -0.6689 -0.1402 444 ASN B C 10588 O O . ASN B 444 ? 2.7447 2.8039 2.2788 -0.8677 -0.6678 -0.1362 444 ASN B O 10589 C CB . ASN B 444 ? 2.9333 2.9889 2.2896 -0.8854 -0.6673 -0.0983 444 ASN B CB 10590 C CG . ASN B 444 ? 2.9499 3.0050 2.2104 -0.9121 -0.6554 -0.1242 444 ASN B CG 10591 O OD1 . ASN B 444 ? 2.9108 2.9618 2.1548 -0.9235 -0.6389 -0.1653 444 ASN B OD1 10592 N ND2 . ASN B 444 ? 2.9553 3.0140 2.1567 -0.9193 -0.6606 -0.0994 444 ASN B ND2 10593 N N . SER B 445 ? 2.7844 2.8541 2.1762 -0.9142 -0.6846 -0.1500 445 SER B N 10594 C CA . SER B 445 ? 2.8262 2.9201 2.2484 -0.9279 -0.7265 -0.1340 445 SER B CA 10595 C C . SER B 445 ? 2.8971 2.9913 2.3961 -0.9228 -0.7257 -0.1543 445 SER B C 10596 O O . SER B 445 ? 2.8849 2.9910 2.4650 -0.9097 -0.7466 -0.1267 445 SER B O 10597 C CB . SER B 445 ? 2.8368 2.9385 2.1779 -0.9564 -0.7342 -0.1491 445 SER B CB 10598 O OG . SER B 445 ? 2.8452 2.9698 2.2127 -0.9706 -0.7762 -0.1328 445 SER B OG 10599 N N . HIS B 446 ? 2.9513 3.8091 1.8984 -0.9506 -0.1386 -0.3357 446 HIS B N 10600 C CA . HIS B 446 ? 2.8720 3.7050 1.9412 -0.8432 -0.1414 -0.3607 446 HIS B CA 10601 C C . HIS B 446 ? 2.9104 3.5959 1.9947 -0.8056 -0.1911 -0.2969 446 HIS B C 10602 O O . HIS B 446 ? 2.9058 3.5522 1.9243 -0.8466 -0.2236 -0.2698 446 HIS B O 10603 C CB . HIS B 446 ? 2.7210 3.5707 1.8840 -0.7738 -0.1148 -0.3871 446 HIS B CB 10604 C CG . HIS B 446 ? 2.7100 3.7165 1.8889 -0.7877 -0.0694 -0.4701 446 HIS B CG 10605 N ND1 . HIS B 446 ? 2.7033 3.8357 1.8148 -0.8667 -0.0482 -0.5174 446 HIS B ND1 10606 C CD2 . HIS B 446 ? 2.6706 3.7329 1.9269 -0.7329 -0.0433 -0.5206 446 HIS B CD2 10607 C CE1 . HIS B 446 ? 2.6776 3.9466 1.8333 -0.8584 -0.0096 -0.5991 446 HIS B CE1 10608 N NE2 . HIS B 446 ? 2.6542 3.8794 1.8979 -0.7747 -0.0090 -0.6017 446 HIS B NE2 10609 N N . ARG B 447 ? 2.8994 3.5078 2.0707 -0.7295 -0.1971 -0.2778 447 ARG B N 10610 C CA . ARG B 447 ? 2.9019 3.3908 2.1133 -0.6838 -0.2374 -0.2355 447 ARG B CA 10611 C C . ARG B 447 ? 2.9530 3.3308 2.0937 -0.7280 -0.2878 -0.1608 447 ARG B C 10612 O O . ARG B 447 ? 2.8813 3.1698 2.0424 -0.7028 -0.3300 -0.1313 447 ARG B O 10613 C CB . ARG B 447 ? 2.7968 3.2455 2.1166 -0.5987 -0.2239 -0.2440 447 ARG B CB 10614 C CG . ARG B 447 ? 2.7436 3.2813 2.1256 -0.5518 -0.1836 -0.3154 447 ARG B CG 10615 C CD . ARG B 447 ? 2.6862 3.1631 2.1550 -0.4767 -0.1762 -0.3164 447 ARG B CD 10616 N NE . ARG B 447 ? 2.6680 3.2138 2.1838 -0.4322 -0.1478 -0.3829 447 ARG B NE 10617 C CZ . ARG B 447 ? 2.6963 3.2554 2.2514 -0.3907 -0.1483 -0.4281 447 ARG B CZ 10618 N NH1 . ARG B 447 ? 2.7282 3.2446 2.2836 -0.3904 -0.1695 -0.4138 447 ARG B NH1 10619 N NH2 . ARG B 447 ? 2.6682 3.2795 2.2617 -0.3480 -0.1322 -0.4902 447 ARG B NH2 10620 N N . CYS B 448 ? 3.0941 3.4761 2.1519 -0.7938 -0.2872 -0.1344 448 CYS B N 10621 C CA . CYS B 448 ? 3.1631 3.4277 2.1419 -0.8386 -0.3430 -0.0634 448 CYS B CA 10622 C C . CYS B 448 ? 3.2001 3.4510 2.0509 -0.9223 -0.3777 -0.0436 448 CYS B C 10623 O O . CYS B 448 ? 3.2637 3.4105 2.0214 -0.9728 -0.4329 0.0148 448 CYS B O 10624 C CB . CYS B 448 ? 3.1898 3.4466 2.1335 -0.8716 -0.3309 -0.0390 448 CYS B CB 10625 S SG . CYS B 448 ? 3.6240 3.8614 2.7025 -0.7784 -0.3053 -0.0457 448 CYS B SG 10626 N N . ASN B 449 ? 3.1135 3.4657 1.9569 -0.9368 -0.3486 -0.0943 449 ASN B N 10627 C CA . ASN B 449 ? 3.1635 3.5186 1.8874 -1.0166 -0.3746 -0.0852 449 ASN B CA 10628 C C . ASN B 449 ? 3.2165 3.5620 1.7857 -1.1312 -0.3835 -0.0513 449 ASN B C 10629 O O . ASN B 449 ? 3.1203 3.5447 1.6784 -1.1628 -0.3373 -0.0728 449 ASN B O 10630 C CB . ASN B 449 ? 3.2217 3.4501 1.9424 -0.9910 -0.4448 -0.0430 449 ASN B CB 10631 C CG . ASN B 449 ? 3.1292 3.3742 1.9871 -0.8941 -0.4342 -0.0806 449 ASN B CG 10632 O OD1 . ASN B 449 ? 3.0130 3.3680 1.9375 -0.8620 -0.3805 -0.1412 449 ASN B OD1 10633 N ND2 . ASN B 449 ? 3.1917 3.3262 2.0915 -0.8484 -0.4886 -0.0489 449 ASN B ND2 10634 N N . ASN B 450 ? 3.3287 3.5721 1.7739 -1.1957 -0.4462 0.0008 450 ASN B N 10635 C CA . ASN B 450 ? 3.4119 3.6248 1.7045 -1.3084 -0.4548 0.0400 450 ASN B CA 10636 C C . ASN B 450 ? 3.4837 3.5676 1.7351 -1.3202 -0.4987 0.1043 450 ASN B C 10637 O O . ASN B 450 ? 3.3957 3.4275 1.7475 -1.2375 -0.5169 0.1137 450 ASN B O 10638 C CB . ASN B 450 ? 3.4376 3.5801 1.6393 -1.3585 -0.4942 0.0724 450 ASN B CB 10639 C CG . ASN B 450 ? 3.4579 3.7232 1.6131 -1.4360 -0.4281 0.0372 450 ASN B CG 10640 O OD1 . ASN B 450 ? 3.3878 3.7997 1.5908 -1.4466 -0.3533 -0.0179 450 ASN B OD1 10641 N ND2 . ASN B 450 ? 3.5119 3.7201 1.5796 -1.4898 -0.4577 0.0650 450 ASN B ND2 10642 N N . GLY B 451 ? 3.5694 3.5977 1.7119 -1.4081 -0.5022 0.1490 451 GLY B N 10643 C CA . GLY B 451 ? 3.6744 3.5864 1.7732 -1.4277 -0.5384 0.2061 451 GLY B CA 10644 C C . GLY B 451 ? 3.7104 3.7266 1.8816 -1.4033 -0.4781 0.1696 451 GLY B C 10645 O O . GLY B 451 ? 3.6890 3.6445 1.9086 -1.3477 -0.5090 0.1871 451 GLY B O 10646 N N . ASN B 452 ? 3.7525 3.9295 1.9368 -1.4441 -0.3936 0.1142 452 ASN B N 10647 C CA . ASN B 452 ? 3.6632 3.9683 1.9304 -1.4146 -0.3281 0.0611 452 ASN B CA 10648 C C . ASN B 452 ? 3.4768 3.8123 1.8757 -1.2992 -0.3276 0.0230 452 ASN B C 10649 O O . ASN B 452 ? 3.4654 3.8080 1.9253 -1.2444 -0.3364 0.0023 452 ASN B O 10650 C CB . ASN B 452 ? 3.7083 3.9433 1.9322 -1.4519 -0.3367 0.1069 452 ASN B CB 10651 C CG . ASN B 452 ? 3.8676 4.0620 1.9743 -1.5692 -0.3351 0.1450 452 ASN B CG 10652 O OD1 . ASN B 452 ? 3.8997 4.1840 1.9774 -1.6309 -0.2951 0.1143 452 ASN B OD1 10653 N ND2 . ASN B 452 ? 3.9343 3.9911 1.9750 -1.6036 -0.3808 0.2098 452 ASN B ND2 10654 N N . GLY B 453 ? 3.3267 3.6703 1.8150 -1.2439 -0.3030 0.0184 453 GLY B N 10655 C CA . GLY B 453 ? 3.1342 3.4819 1.7896 -1.1181 -0.2889 -0.0063 453 GLY B CA 10656 C C . GLY B 453 ? 3.0604 3.5103 1.8003 -1.0816 -0.2275 -0.0536 453 GLY B C 10657 O O . GLY B 453 ? 3.0353 3.5354 1.7107 -1.1495 -0.2024 -0.0577 453 GLY B O 10658 N N . THR B 454 ? 3.0247 3.5022 1.9030 -0.9777 -0.2058 -0.0911 454 THR B N 10659 C CA . THR B 454 ? 2.9541 3.5394 1.9209 -0.9308 -0.1499 -0.1520 454 THR B CA 10660 C C . THR B 454 ? 2.7871 3.3592 1.8839 -0.8198 -0.1452 -0.1802 454 THR B C 10661 O O . THR B 454 ? 2.8008 3.2673 1.9282 -0.7785 -0.1826 -0.1415 454 THR B O 10662 C CB . THR B 454 ? 2.6195 3.1736 1.5818 -0.9408 -0.1432 -0.1227 454 THR B CB 10663 O OG1 . THR B 454 ? 2.6109 3.2870 1.5159 -1.0142 -0.1010 -0.1635 454 THR B OG1 10664 C CG2 . THR B 454 ? 2.4847 3.0241 1.5752 -0.8383 -0.1270 -0.1387 454 THR B CG2 10665 N N . PHE B 455 ? 2.6701 3.3481 1.8399 -0.7745 -0.1025 -0.2514 455 PHE B N 10666 C CA . PHE B 455 ? 2.5595 3.2134 1.8401 -0.6743 -0.0987 -0.2772 455 PHE B CA 10667 C C . PHE B 455 ? 2.4001 3.1257 1.7418 -0.6327 -0.0630 -0.3291 455 PHE B C 10668 O O . PHE B 455 ? 2.4008 3.2538 1.7313 -0.6603 -0.0333 -0.3915 455 PHE B O 10669 C CB . PHE B 455 ? 2.7529 3.4477 2.0556 -0.6517 -0.1005 -0.3208 455 PHE B CB 10670 C CG . PHE B 455 ? 2.7454 3.4095 2.1473 -0.5573 -0.0988 -0.3496 455 PHE B CG 10671 C CD1 . PHE B 455 ? 2.6779 3.2209 2.1177 -0.5142 -0.1249 -0.3030 455 PHE B CD1 10672 C CD2 . PHE B 455 ? 2.6916 3.4463 2.1453 -0.5147 -0.0745 -0.4276 455 PHE B CD2 10673 C CE1 . PHE B 455 ? 2.5706 3.0796 2.0867 -0.4396 -0.1220 -0.3282 455 PHE B CE1 10674 C CE2 . PHE B 455 ? 2.5924 3.3002 2.1204 -0.4338 -0.0799 -0.4505 455 PHE B CE2 10675 C CZ . PHE B 455 ? 2.5477 3.1305 2.1011 -0.4009 -0.1013 -0.3981 455 PHE B CZ 10676 N N . GLU B 456 ? 2.3372 2.9848 1.7437 -0.5677 -0.0673 -0.3086 456 GLU B N 10677 C CA . GLU B 456 ? 2.3571 3.0551 1.8179 -0.5240 -0.0407 -0.3535 456 GLU B CA 10678 C C . GLU B 456 ? 2.3039 2.9217 1.8438 -0.4355 -0.0483 -0.3552 456 GLU B C 10679 O O . GLU B 456 ? 2.3753 2.8827 1.9288 -0.4179 -0.0671 -0.2991 456 GLU B O 10680 C CB . GLU B 456 ? 2.4397 3.1334 1.8666 -0.5651 -0.0317 -0.3199 456 GLU B CB 10681 C CG . GLU B 456 ? 2.3467 3.0920 1.8276 -0.5221 -0.0065 -0.3651 456 GLU B CG 10682 C CD . GLU B 456 ? 2.2789 3.0209 1.7252 -0.5662 0.0029 -0.3312 456 GLU B CD 10683 O OE1 . GLU B 456 ? 2.3128 3.0045 1.6881 -0.6314 -0.0135 -0.2710 456 GLU B OE1 10684 O OE2 . GLU B 456 ? 2.1722 2.9559 1.6593 -0.5352 0.0224 -0.3655 456 GLU B OE2 10685 N N . CYS B 457 ? 2.2652 2.9389 1.8536 -0.3832 -0.0362 -0.4241 457 CYS B N 10686 C CA . CYS B 457 ? 2.2994 2.8954 1.9470 -0.3056 -0.0437 -0.4316 457 CYS B CA 10687 C C . CYS B 457 ? 2.3032 2.7866 1.9653 -0.2814 -0.0646 -0.3905 457 CYS B C 10688 O O . CYS B 457 ? 2.2469 2.6391 1.9396 -0.2416 -0.0696 -0.3674 457 CYS B O 10689 C CB . CYS B 457 ? 2.2843 2.8415 1.9453 -0.2927 -0.0352 -0.4052 457 CYS B CB 10690 S SG . CYS B 457 ? 2.5279 3.2157 2.1906 -0.3040 -0.0102 -0.4676 457 CYS B SG 10691 N N . GLY B 458 ? 2.3286 2.8229 1.9676 -0.3091 -0.0757 -0.3851 458 GLY B N 10692 C CA . GLY B 458 ? 2.3459 2.7481 2.0022 -0.2895 -0.0950 -0.3550 458 GLY B CA 10693 C C . GLY B 458 ? 2.4500 2.7815 2.0883 -0.3233 -0.1116 -0.2854 458 GLY B C 10694 O O . GLY B 458 ? 2.4547 2.7076 2.1201 -0.3038 -0.1267 -0.2614 458 GLY B O 10695 N N . VAL B 459 ? 2.5711 2.9296 2.1630 -0.3753 -0.1120 -0.2570 459 VAL B N 10696 C CA . VAL B 459 ? 2.5960 2.8805 2.1648 -0.4068 -0.1388 -0.1935 459 VAL B CA 10697 C C . VAL B 459 ? 2.6491 2.9738 2.1338 -0.4820 -0.1491 -0.1732 459 VAL B C 10698 O O . VAL B 459 ? 2.6563 3.0758 2.1059 -0.5135 -0.1253 -0.2081 459 VAL B O 10699 C CB . VAL B 459 ? 2.5155 2.7370 2.1179 -0.3844 -0.1370 -0.1620 459 VAL B CB 10700 C CG1 . VAL B 459 ? 2.5923 2.8581 2.1550 -0.4210 -0.1233 -0.1542 459 VAL B CG1 10701 C CG2 . VAL B 459 ? 2.4859 2.6149 2.1021 -0.3866 -0.1715 -0.1132 459 VAL B CG2 10702 N N . CYS B 460 ? 2.6662 2.9172 2.1158 -0.5131 -0.1875 -0.1209 460 CYS B N 10703 C CA . CYS B 460 ? 2.7623 3.0227 2.1128 -0.5919 -0.2079 -0.0929 460 CYS B CA 10704 C C . CYS B 460 ? 2.8056 2.9851 2.1224 -0.6194 -0.2376 -0.0352 460 CYS B C 10705 O O . CYS B 460 ? 2.8393 2.9235 2.1824 -0.5971 -0.2779 0.0003 460 CYS B O 10706 C CB . CYS B 460 ? 2.7940 3.0300 2.1092 -0.6127 -0.2417 -0.0841 460 CYS B CB 10707 S SG . CYS B 460 ? 3.5543 3.7422 2.7336 -0.7093 -0.2901 -0.0299 460 CYS B SG 10708 N N . ARG B 461 ? 2.7858 3.0072 2.0477 -0.6677 -0.2192 -0.0313 461 ARG B N 10709 C CA . ARG B 461 ? 2.7313 2.8749 1.9399 -0.7076 -0.2517 0.0244 461 ARG B CA 10710 C C . ARG B 461 ? 2.7284 2.8797 1.8034 -0.8063 -0.2711 0.0461 461 ARG B C 10711 O O . ARG B 461 ? 2.6497 2.8960 1.6739 -0.8586 -0.2326 0.0186 461 ARG B O 10712 C CB . ARG B 461 ? 2.6227 2.7958 1.8647 -0.6925 -0.2173 0.0167 461 ARG B CB 10713 C CG . ARG B 461 ? 2.4683 2.6689 1.8229 -0.6074 -0.1821 -0.0226 461 ARG B CG 10714 C CD . ARG B 461 ? 2.4016 2.7014 1.7666 -0.6072 -0.1329 -0.0660 461 ARG B CD 10715 N NE . ARG B 461 ? 2.4591 2.7492 1.7763 -0.6537 -0.1332 -0.0363 461 ARG B NE 10716 C CZ . ARG B 461 ? 2.4296 2.8061 1.7436 -0.6684 -0.0948 -0.0699 461 ARG B CZ 10717 N NH1 . ARG B 461 ? 2.4190 2.8975 1.7780 -0.6354 -0.0576 -0.1379 461 ARG B NH1 10718 N NH2 . ARG B 461 ? 2.3883 2.7482 1.6554 -0.7148 -0.0974 -0.0392 461 ARG B NH2 10719 N N . CYS B 462 ? 2.8377 2.8877 1.8511 -0.8358 -0.3331 0.0930 462 CYS B N 10720 C CA . CYS B 462 ? 3.0388 3.0910 1.9141 -0.9319 -0.3540 0.1100 462 CYS B CA 10721 C C . CYS B 462 ? 3.2189 3.1337 1.9859 -0.9908 -0.4269 0.1796 462 CYS B C 10722 O O . CYS B 462 ? 3.2959 3.0965 2.0975 -0.9476 -0.4865 0.2123 462 CYS B O 10723 C CB . CYS B 462 ? 3.0915 3.1681 1.9693 -0.9228 -0.3619 0.0864 462 CYS B CB 10724 S SG . CYS B 462 ? 3.4996 3.4462 2.4392 -0.8556 -0.4323 0.1167 462 CYS B SG 10725 N N . GLY B 463 ? 3.3120 3.2391 1.9464 -1.0918 -0.4239 0.1973 463 GLY B N 10726 C CA . GLY B 463 ? 3.4303 3.2224 1.9205 -1.1704 -0.4998 0.2620 463 GLY B CA 10727 C C . GLY B 463 ? 3.4272 3.0883 1.9064 -1.1629 -0.5541 0.3151 463 GLY B C 10728 O O . GLY B 463 ? 3.3133 2.9667 1.9205 -1.0769 -0.5456 0.3067 463 GLY B O 10729 N N . PRO B 464 ? 3.5371 3.0903 1.8547 -1.2581 -0.6130 0.3696 464 PRO B N 10730 C CA . PRO B 464 ? 3.6199 3.0161 1.8888 -1.2684 -0.6887 0.4281 464 PRO B CA 10731 C C . PRO B 464 ? 3.6972 2.9417 1.9847 -1.2157 -0.7901 0.4595 464 PRO B C 10732 O O . PRO B 464 ? 3.7184 2.8451 1.8654 -1.2807 -0.8676 0.5011 464 PRO B O 10733 C CB . PRO B 464 ? 3.7273 3.0843 1.8170 -1.4009 -0.6956 0.4629 464 PRO B CB 10734 C CG . PRO B 464 ? 3.7105 3.2405 1.7889 -1.4515 -0.6025 0.4101 464 PRO B CG 10735 C CD . PRO B 464 ? 3.6161 3.2128 1.7720 -1.3793 -0.5977 0.3704 464 PRO B CD 10736 N N . GLY B 465 ? 3.6866 2.9354 2.1439 -1.1015 -0.7907 0.4354 465 GLY B N 10737 C CA . GLY B 465 ? 3.7975 2.9276 2.3030 -1.0401 -0.8805 0.4483 465 GLY B CA 10738 C C . GLY B 465 ? 3.7946 2.9947 2.3995 -0.9778 -0.8581 0.4047 465 GLY B C 10739 O O . GLY B 465 ? 3.8126 2.9646 2.5225 -0.8993 -0.9031 0.3918 465 GLY B O 10740 N N . TRP B 466 ? 3.7794 3.0998 2.3577 -1.0120 -0.7877 0.3758 466 TRP B N 10741 C CA . TRP B 466 ? 3.6347 3.0452 2.3288 -0.9447 -0.7463 0.3259 466 TRP B CA 10742 C C . TRP B 466 ? 3.4856 2.9857 2.3330 -0.8670 -0.6741 0.2869 466 TRP B C 10743 O O . TRP B 466 ? 3.5466 3.0944 2.3845 -0.8881 -0.6272 0.2866 466 TRP B O 10744 C CB . TRP B 466 ? 3.6095 3.1193 2.2278 -1.0043 -0.6985 0.3030 466 TRP B CB 10745 C CG . TRP B 466 ? 3.7654 3.1911 2.2682 -1.0551 -0.7703 0.3300 466 TRP B CG 10746 C CD1 . TRP B 466 ? 3.7828 3.1999 2.3342 -1.0111 -0.7972 0.3115 466 TRP B CD1 10747 C CD2 . TRP B 466 ? 4.0112 3.3422 2.3227 -1.1631 -0.8275 0.3810 466 TRP B CD2 10748 N NE1 . TRP B 466 ? 4.0079 3.3323 2.4139 -1.0804 -0.8691 0.3471 466 TRP B NE1 10749 C CE2 . TRP B 466 ? 4.1276 3.3926 2.3787 -1.1767 -0.8903 0.3917 466 TRP B CE2 10750 C CE3 . TRP B 466 ? 4.1401 3.4314 2.3183 -1.2543 -0.8329 0.4187 466 TRP B CE3 10751 C CZ2 . TRP B 466 ? 4.2638 3.4227 2.3625 -1.2616 -0.9379 0.4380 466 TRP B CZ2 10752 C CZ3 . TRP B 466 ? 4.3479 3.5361 2.3927 -1.3366 -0.8707 0.4624 466 TRP B CZ3 10753 C CH2 . TRP B 466 ? 4.3760 3.4967 2.3841 -1.3383 -0.9212 0.4721 466 TRP B CH2 10754 N N . LEU B 467 ? 3.3210 2.8385 2.3040 -0.7810 -0.6675 0.2539 467 LEU B N 10755 C CA . LEU B 467 ? 3.2537 2.8212 2.3709 -0.7100 -0.6160 0.2254 467 LEU B CA 10756 C C . LEU B 467 ? 3.1843 2.8533 2.4047 -0.6543 -0.5494 0.1719 467 LEU B C 10757 O O . LEU B 467 ? 3.1253 2.8876 2.3638 -0.6524 -0.4792 0.1449 467 LEU B O 10758 C CB . LEU B 467 ? 3.2582 2.7286 2.4522 -0.6562 -0.6781 0.2373 467 LEU B CB 10759 C CG . LEU B 467 ? 3.2469 2.6545 2.4253 -0.6661 -0.7033 0.2686 467 LEU B CG 10760 C CD1 . LEU B 467 ? 3.3414 2.6920 2.3555 -0.7587 -0.7379 0.3169 467 LEU B CD1 10761 C CD2 . LEU B 467 ? 3.3024 2.6168 2.5595 -0.6111 -0.7776 0.2697 467 LEU B CD2 10762 N N . GLY B 468 ? 3.1406 2.7873 2.4258 -0.6099 -0.5761 0.1542 468 GLY B N 10763 C CA . GLY B 468 ? 3.0100 2.7260 2.4044 -0.5501 -0.5230 0.1065 468 GLY B CA 10764 C C . GLY B 468 ? 2.9427 2.7578 2.3146 -0.5643 -0.4645 0.0739 468 GLY B C 10765 O O . GLY B 468 ? 2.9938 2.8423 2.2657 -0.6255 -0.4586 0.0827 468 GLY B O 10766 N N . SER B 469 ? 2.7768 2.6383 2.2404 -0.5100 -0.4226 0.0327 469 SER B N 10767 C CA . SER B 469 ? 2.7496 2.6978 2.2082 -0.5098 -0.3754 -0.0067 469 SER B CA 10768 C C . SER B 469 ? 2.9116 2.8644 2.2951 -0.5530 -0.4062 -0.0025 469 SER B C 10769 O O . SER B 469 ? 2.9057 2.9318 2.2299 -0.5908 -0.3791 -0.0209 469 SER B O 10770 C CB . SER B 469 ? 2.5749 2.5375 2.1357 -0.4459 -0.3452 -0.0454 469 SER B CB 10771 O OG . SER B 469 ? 2.5348 2.4411 2.1439 -0.4223 -0.3846 -0.0431 469 SER B OG 10772 N N . GLN B 470 ? 3.0786 2.9563 2.4677 -0.5469 -0.4647 0.0168 470 GLN B N 10773 C CA . GLN B 470 ? 3.2732 3.1255 2.5690 -0.5973 -0.5116 0.0354 470 GLN B CA 10774 C C . GLN B 470 ? 3.3298 3.0960 2.5364 -0.6463 -0.5688 0.0886 470 GLN B C 10775 O O . GLN B 470 ? 3.3969 3.0897 2.6486 -0.6170 -0.6054 0.1077 470 GLN B O 10776 C CB . GLN B 470 ? 3.2939 3.1123 2.6431 -0.5612 -0.5489 0.0206 470 GLN B CB 10777 C CG . GLN B 470 ? 3.3221 3.0461 2.7274 -0.5268 -0.6121 0.0369 470 GLN B CG 10778 C CD . GLN B 470 ? 3.2094 2.9378 2.7268 -0.4722 -0.5808 0.0201 470 GLN B CD 10779 O OE1 . GLN B 470 ? 3.1052 2.8988 2.6682 -0.4506 -0.5136 -0.0065 470 GLN B OE1 10780 N NE2 . GLN B 470 ? 3.2127 2.8690 2.7728 -0.4501 -0.6337 0.0327 470 GLN B NE2 10781 N N . CYS B 471 ? 3.2859 3.0618 2.3627 -0.7246 -0.5759 0.1096 471 CYS B N 10782 C CA . CYS B 471 ? 3.3214 3.0090 2.2918 -0.7834 -0.6284 0.1626 471 CYS B CA 10783 C C . CYS B 471 ? 3.3515 2.9117 2.2791 -0.7881 -0.7264 0.1962 471 CYS B C 10784 O O . CYS B 471 ? 3.2461 2.7987 2.1220 -0.8109 -0.7536 0.1937 471 CYS B O 10785 C CB . CYS B 471 ? 3.3445 3.0885 2.1800 -0.8773 -0.5992 0.1702 471 CYS B CB 10786 S SG . CYS B 471 ? 3.5604 3.4403 2.4393 -0.8758 -0.5005 0.1315 471 CYS B SG 10787 N N . GLU B 472 ? 3.4686 2.9290 2.4207 -0.7637 -0.7831 0.2236 472 GLU B N 10788 C CA . GLU B 472 ? 3.6158 2.9498 2.5523 -0.7502 -0.8864 0.2457 472 GLU B CA 10789 C C . GLU B 472 ? 3.6715 2.8899 2.5786 -0.7556 -0.9533 0.2851 472 GLU B C 10790 O O . GLU B 472 ? 3.6993 2.9309 2.5680 -0.7881 -0.9199 0.3044 472 GLU B O 10791 C CB . GLU B 472 ? 3.5725 2.9275 2.6625 -0.6621 -0.8897 0.2005 472 GLU B CB 10792 C CG . GLU B 472 ? 3.4701 2.8806 2.7072 -0.5944 -0.8335 0.1685 472 GLU B CG 10793 C CD . GLU B 472 ? 3.4377 2.8289 2.8105 -0.5196 -0.8667 0.1319 472 GLU B CD 10794 O OE1 . GLU B 472 ? 3.5416 2.8663 2.8986 -0.5147 -0.9445 0.1328 472 GLU B OE1 10795 O OE2 . GLU B 472 ? 3.2788 2.7227 2.7717 -0.4686 -0.8159 0.0992 472 GLU B OE2 10796 N N . CYS B 473 ? 3.6547 2.7612 2.5828 -0.7217 -1.0515 0.2924 473 CYS B N 10797 C CA . CYS B 473 ? 3.6683 2.6565 2.5900 -0.7105 -1.1299 0.3201 473 CYS B CA 10798 C C . CYS B 473 ? 3.6584 2.5576 2.3974 -0.8045 -1.1666 0.3816 473 CYS B C 10799 O O . CYS B 473 ? 3.6734 2.4894 2.2631 -0.8708 -1.2281 0.4161 473 CYS B O 10800 C CB . CYS B 473 ? 3.5616 2.6122 2.6338 -0.6448 -1.0744 0.2901 473 CYS B CB 10801 S SG . CYS B 473 ? 3.8182 2.9544 3.0992 -0.5428 -1.0400 0.2177 473 CYS B SG 10802 N N . SER B 474 ? 3.6666 2.5794 2.4149 -0.8125 -1.1305 0.3944 474 SER B N 10803 C CA . SER B 474 ? 3.9116 2.7384 2.4986 -0.8999 -1.1627 0.4504 474 SER B CA 10804 C C . SER B 474 ? 4.1205 2.7540 2.6275 -0.9080 -1.3037 0.4904 474 SER B C 10805 O O . SER B 474 ? 4.2896 2.8236 2.6454 -0.9863 -1.3346 0.5359 474 SER B O 10806 C CB . SER B 474 ? 4.0207 2.8941 2.4478 -1.0048 -1.1194 0.4701 474 SER B CB 10807 O OG . SER B 474 ? 4.1623 2.9638 2.4338 -1.0977 -1.1389 0.5200 474 SER B OG 10808 N N . GLU B 475 ? 4.0493 2.6413 2.6975 -0.8150 -1.3574 0.4626 475 GLU B N 10809 C CA . GLU B 475 ? 4.2188 2.6368 2.8428 -0.7954 -1.4793 0.4845 475 GLU B CA 10810 C C . GLU B 475 ? 4.2857 2.5855 2.8022 -0.8312 -1.5382 0.5092 475 GLU B C 10811 O O . GLU B 475 ? 4.4601 2.6187 2.8554 -0.8885 -1.5846 0.5538 475 GLU B O 10812 C CB . GLU B 475 ? 4.4040 2.7486 2.9603 -0.8375 -1.4829 0.5251 475 GLU B CB 10813 C CG . GLU B 475 ? 4.5161 2.7324 3.1457 -0.7737 -1.5762 0.5180 475 GLU B CG 10814 C CD . GLU B 475 ? 4.3575 2.6535 3.1911 -0.6623 -1.5891 0.4530 475 GLU B CD 10815 O OE1 . GLU B 475 ? 4.1450 2.5913 3.0796 -0.6380 -1.4930 0.4227 475 GLU B OE1 10816 O OE2 . GLU B 475 ? 4.4060 2.6224 3.3193 -0.5960 -1.6700 0.4231 475 GLU B OE2 10817 N N . GLU B 476 ? 4.1401 2.4982 2.7043 -0.7999 -1.5363 0.4766 476 GLU B N 10818 C CA . GLU B 476 ? 4.2801 2.5472 2.7607 -0.8236 -1.5883 0.4912 476 GLU B CA 10819 C C . GLU B 476 ? 4.3038 2.4575 2.8767 -0.7383 -1.6944 0.4643 476 GLU B C 10820 O O . GLU B 476 ? 4.3675 2.4568 2.9101 -0.7327 -1.7452 0.4611 476 GLU B O 10821 C CB . GLU B 476 ? 4.1125 2.5104 2.5995 -0.8338 -1.5274 0.4653 476 GLU B CB 10822 C CG . GLU B 476 ? 4.2396 2.5653 2.5910 -0.8958 -1.5517 0.4940 476 GLU B CG 10823 C CD . GLU B 476 ? 4.1123 2.5671 2.4916 -0.8916 -1.4996 0.4598 476 GLU B CD 10824 O OE1 . GLU B 476 ? 4.1304 2.5289 2.4445 -0.9111 -1.5356 0.4683 476 GLU B OE1 10825 O OE2 . GLU B 476 ? 3.9821 2.5895 2.4471 -0.8701 -1.4249 0.4228 476 GLU B OE2 10826 N N . ASP B 477 ? 4.2076 2.3381 2.8920 -0.6737 -1.7275 0.4417 477 ASP B N 10827 C CA . ASP B 477 ? 4.0641 2.2261 2.9378 -0.5627 -1.7699 0.3737 477 ASP B CA 10828 C C . ASP B 477 ? 3.9122 2.2682 2.8960 -0.5391 -1.6808 0.3293 477 ASP B C 10829 O O . ASP B 477 ? 3.7221 2.1636 2.7246 -0.5564 -1.6150 0.3330 477 ASP B O 10830 C CB . ASP B 477 ? 4.0465 2.1111 2.9295 -0.5242 -1.8558 0.3535 477 ASP B CB 10831 C CG . ASP B 477 ? 4.1644 2.0391 3.0172 -0.5064 -1.9616 0.3652 477 ASP B CG 10832 O OD1 . ASP B 477 ? 3.9855 1.8406 2.9048 -0.4743 -1.9757 0.3538 477 ASP B OD1 10833 O OD2 . ASP B 477 ? 4.2781 2.0202 3.0410 -0.5252 -2.0324 0.3827 477 ASP B OD2 10834 N N . TYR B 478 ? 3.9114 2.3328 2.9691 -0.5020 -1.6787 0.2850 478 TYR B N 10835 C CA . TYR B 478 ? 3.7233 2.3210 2.8944 -0.4805 -1.5802 0.2383 478 TYR B CA 10836 C C . TYR B 478 ? 3.5481 2.2186 2.8999 -0.4085 -1.5395 0.1887 478 TYR B C 10837 O O . TYR B 478 ? 3.3705 2.0997 2.7276 -0.4260 -1.4568 0.2039 478 TYR B O 10838 C CB . TYR B 478 ? 3.6891 2.3684 2.7560 -0.5570 -1.4666 0.2773 478 TYR B CB 10839 C CG . TYR B 478 ? 3.6689 2.4416 2.7173 -0.5780 -1.4017 0.2631 478 TYR B CG 10840 C CD1 . TYR B 478 ? 3.8746 2.5756 2.7698 -0.6393 -1.4566 0.2971 478 TYR B CD1 10841 C CD2 . TYR B 478 ? 3.4731 2.4001 2.6480 -0.5409 -1.2870 0.2166 478 TYR B CD2 10842 C CE1 . TYR B 478 ? 3.8541 2.6455 2.7348 -0.6584 -1.3971 0.2809 478 TYR B CE1 10843 C CE2 . TYR B 478 ? 3.4752 2.4837 2.6337 -0.5582 -1.2318 0.2014 478 TYR B CE2 10844 C CZ . TYR B 478 ? 3.6598 2.6057 2.6762 -0.6153 -1.2856 0.2319 478 TYR B CZ 10845 O OH . TYR B 478 ? 3.6521 2.6836 2.6557 -0.6317 -1.2312 0.2132 478 TYR B OH 10846 N N . ARG B 479 ? 3.5490 2.2105 3.0415 -0.3316 -1.6048 0.1281 479 ARG B N 10847 C CA . ARG B 479 ? 3.3973 2.1222 3.0611 -0.2662 -1.5792 0.0739 479 ARG B CA 10848 C C . ARG B 479 ? 3.3163 2.2027 3.1490 -0.2188 -1.4774 0.0029 479 ARG B C 10849 O O . ARG B 479 ? 3.2767 2.1907 3.2048 -0.1745 -1.5112 -0.0550 479 ARG B O 10850 C CB . ARG B 479 ? 3.4692 2.0884 3.1939 -0.2091 -1.7117 0.0412 479 ARG B CB 10851 C CG . ARG B 479 ? 3.6832 2.1198 3.2426 -0.2427 -1.7946 0.1075 479 ARG B CG 10852 C CD . ARG B 479 ? 3.8038 2.1505 3.4374 -0.1716 -1.8895 0.0620 479 ARG B CD 10853 N NE . ARG B 479 ? 3.7155 2.1356 3.5489 -0.0883 -1.8910 -0.0193 479 ARG B NE 10854 C CZ . ARG B 479 ? 3.6568 2.1832 3.6569 -0.0235 -1.8787 -0.1051 479 ARG B CZ 10855 N NH1 . ARG B 479 ? 3.6042 2.1699 3.5975 -0.0282 -1.8693 -0.1188 479 ARG B NH1 10856 N NH2 . ARG B 479 ? 3.5788 2.1769 3.7527 0.0429 -1.8719 -0.1802 479 ARG B NH2 10857 N N . PRO B 480 ? 3.3139 2.3020 3.1776 -0.2313 -1.3555 0.0068 480 PRO B N 10858 C CA . PRO B 480 ? 3.1897 2.3163 3.1941 -0.1979 -1.2471 -0.0478 480 PRO B CA 10859 C C . PRO B 480 ? 3.2352 2.3819 3.3743 -0.1483 -1.2572 -0.0946 480 PRO B C 10860 O O . PRO B 480 ? 3.2520 2.3750 3.3621 -0.1612 -1.2438 -0.0633 480 PRO B O 10861 C CB . PRO B 480 ? 3.0391 2.2208 2.9587 -0.2482 -1.1381 -0.0016 480 PRO B CB 10862 C CG . PRO B 480 ? 3.1497 2.2443 2.8912 -0.3111 -1.1829 0.0668 480 PRO B CG 10863 C CD . PRO B 480 ? 3.3324 2.2964 3.0472 -0.2998 -1.3114 0.0794 480 PRO B CD 10864 N N . SER B 481 ? 3.1898 2.3799 3.4739 -0.0940 -1.2864 -0.1724 481 SER B N 10865 C CA . SER B 481 ? 3.1168 2.3331 3.5416 -0.0445 -1.3091 -0.2325 481 SER B CA 10866 C C . SER B 481 ? 3.0828 2.4032 3.5705 -0.0494 -1.1852 -0.2453 481 SER B C 10867 O O . SER B 481 ? 3.0436 2.4352 3.6721 -0.0133 -1.1657 -0.3146 481 SER B O 10868 C CB . SER B 481 ? 2.9599 2.2192 3.5295 0.0096 -1.3630 -0.3250 481 SER B CB 10869 O OG . SER B 481 ? 2.8455 2.1143 3.5418 0.0578 -1.4134 -0.3869 481 SER B OG 10870 N N . GLN B 482 ? 3.1075 2.4355 3.4865 -0.0964 -1.1056 -0.1815 482 GLN B N 10871 C CA . GLN B 482 ? 2.9556 2.3823 3.3572 -0.1110 -0.9789 -0.1869 482 GLN B CA 10872 C C . GLN B 482 ? 2.8953 2.4063 3.4393 -0.0804 -0.9254 -0.2523 482 GLN B C 10873 O O . GLN B 482 ? 2.7683 2.3601 3.3568 -0.0846 -0.8429 -0.2835 482 GLN B O 10874 C CB . GLN B 482 ? 2.9019 2.3037 3.1826 -0.1538 -0.9316 -0.1142 482 GLN B CB 10875 C CG . GLN B 482 ? 2.9853 2.3034 3.1089 -0.1985 -0.9811 -0.0462 482 GLN B CG 10876 C CD . GLN B 482 ? 3.0124 2.2271 3.0665 -0.2124 -1.0592 -0.0023 482 GLN B CD 10877 O OE1 . GLN B 482 ? 2.9438 2.1459 3.0769 -0.1802 -1.0867 -0.0259 482 GLN B OE1 10878 N NE2 . GLN B 482 ? 3.0793 2.2186 2.9805 -0.2648 -1.0961 0.0597 482 GLN B NE2 10879 N N . GLN B 483 ? 2.9604 2.4516 3.5701 -0.0540 -0.9712 -0.2745 483 GLN B N 10880 C CA . GLN B 483 ? 2.8944 2.4738 3.6506 -0.0262 -0.9299 -0.3508 483 GLN B CA 10881 C C . GLN B 483 ? 2.8295 2.4800 3.5770 -0.0524 -0.8053 -0.3424 483 GLN B C 10882 O O . GLN B 483 ? 2.7986 2.4296 3.4837 -0.0703 -0.7678 -0.2934 483 GLN B O 10883 C CB . GLN B 483 ? 2.8679 2.5037 3.7410 0.0030 -0.9588 -0.4355 483 GLN B CB 10884 C CG . GLN B 483 ? 2.8355 2.4978 3.8534 0.0491 -1.0240 -0.5181 483 GLN B CG 10885 C CD . GLN B 483 ? 2.9710 2.5274 3.9706 0.0802 -1.1654 -0.5101 483 GLN B CD 10886 O OE1 . GLN B 483 ? 2.9848 2.5551 4.1043 0.1257 -1.2393 -0.5852 483 GLN B OE1 10887 N NE2 . GLN B 483 ? 3.0895 2.5380 3.9358 0.0537 -1.2069 -0.4230 483 GLN B NE2 10888 N N . ASP B 484 ? 2.7868 2.5151 3.5963 -0.0549 -0.7468 -0.3935 484 ASP B N 10889 C CA . ASP B 484 ? 2.6853 2.4690 3.4807 -0.0811 -0.6365 -0.3911 484 ASP B CA 10890 C C . ASP B 484 ? 2.6846 2.4266 3.3421 -0.1103 -0.5967 -0.3100 484 ASP B C 10891 O O . ASP B 484 ? 2.7379 2.4345 3.3100 -0.1209 -0.6326 -0.2673 484 ASP B O 10892 C CB . ASP B 484 ? 2.6307 2.4782 3.4777 -0.0881 -0.5957 -0.4455 484 ASP B CB 10893 C CG . ASP B 484 ? 2.6594 2.5280 3.6051 -0.0594 -0.6696 -0.5120 484 ASP B CG 10894 O OD1 . ASP B 484 ? 2.5354 2.4104 3.5688 -0.0302 -0.7260 -0.5546 484 ASP B OD1 10895 O OD2 . ASP B 484 ? 2.7312 2.6110 3.6701 -0.0635 -0.6747 -0.5255 484 ASP B OD2 10896 N N . GLU B 485 ? 2.5836 2.3442 3.2223 -0.1237 -0.5255 -0.2944 485 GLU B N 10897 C CA . GLU B 485 ? 2.5174 2.2566 3.0434 -0.1477 -0.4777 -0.2328 485 GLU B CA 10898 C C . GLU B 485 ? 2.4855 2.1656 2.9321 -0.1548 -0.5227 -0.1729 485 GLU B C 10899 O O . GLU B 485 ? 2.5387 2.2125 2.9069 -0.1737 -0.4821 -0.1304 485 GLU B O 10900 C CB . GLU B 485 ? 2.5930 2.3393 3.0587 -0.1633 -0.4546 -0.2222 485 GLU B CB 10901 C CG . GLU B 485 ? 2.5127 2.3079 3.0281 -0.1670 -0.3963 -0.2708 485 GLU B CG 10902 C CD . GLU B 485 ? 2.5082 2.3050 2.9640 -0.1797 -0.3805 -0.2607 485 GLU B CD 10903 O OE1 . GLU B 485 ? 2.5356 2.3113 2.9589 -0.1788 -0.4333 -0.2438 485 GLU B OE1 10904 O OE2 . GLU B 485 ? 2.5143 2.3275 2.9507 -0.1916 -0.3188 -0.2697 485 GLU B OE2 10905 N N . CYS B 486 ? 2.4995 2.1337 2.9631 -0.1414 -0.6091 -0.1722 486 CYS B N 10906 C CA . CYS B 486 ? 2.5010 2.0682 2.8882 -0.1537 -0.6567 -0.1175 486 CYS B CA 10907 C C . CYS B 486 ? 2.2935 1.8686 2.7368 -0.1393 -0.6426 -0.1279 486 CYS B C 10908 O O . CYS B 486 ? 2.1727 1.7099 2.5522 -0.1545 -0.6484 -0.0822 486 CYS B O 10909 C CB . CYS B 486 ? 2.6106 2.1046 2.9784 -0.1475 -0.7653 -0.1095 486 CYS B CB 10910 S SG . CYS B 486 ? 2.4770 1.8733 2.6808 -0.1919 -0.8188 -0.0245 486 CYS B SG 10911 N N . SER B 487 ? 2.2556 1.8850 2.8188 -0.1138 -0.6230 -0.1920 487 SER B N 10912 C CA . SER B 487 ? 2.0980 1.7527 2.7241 -0.1023 -0.5952 -0.2124 487 SER B CA 10913 C C . SER B 487 ? 2.1986 1.9343 2.9059 -0.1010 -0.5190 -0.2708 487 SER B C 10914 O O . SER B 487 ? 2.1896 1.9624 2.9529 -0.0959 -0.5199 -0.3189 487 SER B O 10915 C CB . SER B 487 ? 1.9311 1.5533 2.6295 -0.0722 -0.6839 -0.2398 487 SER B CB 10916 O OG . SER B 487 ? 1.8993 1.5566 2.6697 -0.0601 -0.6556 -0.2685 487 SER B OG 10917 N N . PRO B 488 ? 2.3283 2.0883 3.0361 -0.1099 -0.4540 -0.2675 488 PRO B N 10918 C CA . PRO B 488 ? 2.3833 2.2082 3.1499 -0.1192 -0.3824 -0.3198 488 PRO B CA 10919 C C . PRO B 488 ? 2.3704 2.2474 3.2698 -0.1013 -0.4035 -0.3963 488 PRO B C 10920 O O . PRO B 488 ? 2.4564 2.3119 3.4010 -0.0747 -0.4776 -0.4049 488 PRO B O 10921 C CB . PRO B 488 ? 2.3690 2.1858 3.0725 -0.1357 -0.3167 -0.2824 488 PRO B CB 10922 C CG . PRO B 488 ? 2.3187 2.0782 2.9292 -0.1363 -0.3477 -0.2120 488 PRO B CG 10923 C CD . PRO B 488 ? 2.3211 2.0471 2.9588 -0.1188 -0.4384 -0.2123 488 PRO B CD 10924 N N . ARG B 489 ? 2.2168 2.1590 3.1725 -0.1187 -0.3414 -0.4529 489 ARG B N 10925 C CA . ARG B 489 ? 2.1762 2.1910 3.2660 -0.1091 -0.3505 -0.5407 489 ARG B CA 10926 C C . ARG B 489 ? 2.2353 2.2545 3.4063 -0.0730 -0.4439 -0.5820 489 ARG B C 10927 O O . ARG B 489 ? 2.2579 2.2608 3.4812 -0.0412 -0.5117 -0.5942 489 ARG B O 10928 C CB . ARG B 489 ? 2.0320 2.0552 3.1519 -0.1034 -0.3405 -0.5441 489 ARG B CB 10929 C CG . ARG B 489 ? 1.8764 1.9943 3.1140 -0.1142 -0.3059 -0.6375 489 ARG B CG 10930 C CD . ARG B 489 ? 1.7963 1.9203 3.0421 -0.1166 -0.2797 -0.6321 489 ARG B CD 10931 N NE . ARG B 489 ? 1.7515 1.9728 3.0968 -0.1383 -0.2341 -0.7222 489 ARG B NE 10932 C CZ . ARG B 489 ? 1.6526 1.8999 3.0222 -0.1464 -0.2038 -0.7374 489 ARG B CZ 10933 N NH1 . ARG B 489 ? 1.6385 1.8194 2.9433 -0.1310 -0.2155 -0.6673 489 ARG B NH1 10934 N NH2 . ARG B 489 ? 1.5084 1.8529 2.9664 -0.1739 -0.1599 -0.8259 489 ARG B NH2 10935 N N . GLU B 490 ? 2.1711 2.2058 3.3490 -0.0770 -0.4516 -0.6041 490 GLU B N 10936 C CA . GLU B 490 ? 2.1366 2.1523 3.3581 -0.0432 -0.5465 -0.6259 490 GLU B CA 10937 C C . GLU B 490 ? 2.1769 2.2300 3.5349 -0.0037 -0.6187 -0.7041 490 GLU B C 10938 O O . GLU B 490 ? 2.2150 2.3585 3.6786 -0.0083 -0.5819 -0.7831 490 GLU B O 10939 C CB . GLU B 490 ? 2.0896 2.1451 3.3270 -0.0567 -0.5278 -0.6621 490 GLU B CB 10940 C CG . GLU B 490 ? 2.0807 2.2440 3.4179 -0.0801 -0.4630 -0.7540 490 GLU B CG 10941 C CD . GLU B 490 ? 2.2233 2.4262 3.5858 -0.0917 -0.4562 -0.7967 490 GLU B CD 10942 O OE1 . GLU B 490 ? 2.1885 2.4819 3.6287 -0.1183 -0.4046 -0.8763 490 GLU B OE1 10943 O OE2 . GLU B 490 ? 2.3018 2.4471 3.6034 -0.0784 -0.5013 -0.7523 490 GLU B OE2 10944 N N . GLY B 491 ? 2.1185 2.0983 3.4687 0.0327 -0.7251 -0.6836 491 GLY B N 10945 C CA . GLY B 491 ? 2.0245 2.0160 3.4929 0.0786 -0.8141 -0.7513 491 GLY B CA 10946 C C . GLY B 491 ? 1.9768 1.8851 3.3947 0.0923 -0.8595 -0.6940 491 GLY B C 10947 O O . GLY B 491 ? 1.9529 1.8391 3.4451 0.1340 -0.9519 -0.7341 491 GLY B O 10948 N N . GLN B 492 ? 2.0628 1.9245 3.3550 0.0580 -0.7977 -0.6035 492 GLN B N 10949 C CA . GLN B 492 ? 2.2433 2.0244 3.4703 0.0621 -0.8318 -0.5406 492 GLN B CA 10950 C C . GLN B 492 ? 2.3394 1.9963 3.4448 0.0608 -0.9148 -0.4619 492 GLN B C 10951 O O . GLN B 492 ? 2.3192 1.9574 3.3604 0.0449 -0.9131 -0.4356 492 GLN B O 10952 C CB . GLN B 492 ? 2.2047 2.0032 3.3607 0.0253 -0.7258 -0.4896 492 GLN B CB 10953 C CG . GLN B 492 ? 2.1489 2.0408 3.4088 0.0253 -0.6644 -0.5564 492 GLN B CG 10954 C CD . GLN B 492 ? 2.1148 2.0014 3.2961 -0.0051 -0.5799 -0.5004 492 GLN B CD 10955 O OE1 . GLN B 492 ? 2.1740 2.0117 3.2328 -0.0297 -0.5461 -0.4240 492 GLN B OE1 10956 N NE2 . GLN B 492 ? 2.0143 1.9549 3.2687 -0.0026 -0.5478 -0.5435 492 GLN B NE2 10957 N N . PRO B 493 ? 2.4453 2.0145 3.5130 0.0728 -0.9887 -0.4251 493 PRO B N 10958 C CA . PRO B 493 ? 2.5033 1.9425 3.4424 0.0618 -1.0749 -0.3504 493 PRO B CA 10959 C C . PRO B 493 ? 2.4500 1.8631 3.2365 0.0096 -1.0093 -0.2633 493 PRO B C 10960 O O . PRO B 493 ? 2.4503 1.9265 3.2181 -0.0147 -0.9029 -0.2475 493 PRO B O 10961 C CB . PRO B 493 ? 2.5006 1.8638 3.4257 0.0735 -1.1385 -0.3272 493 PRO B CB 10962 C CG . PRO B 493 ? 2.3692 1.8287 3.3845 0.0796 -1.0548 -0.3666 493 PRO B CG 10963 C CD . PRO B 493 ? 2.3866 1.9699 3.5290 0.0945 -1.0009 -0.4553 493 PRO B CD 10964 N N . VAL B 494 ? 2.3732 1.6918 3.0496 -0.0081 -1.0775 -0.2112 494 VAL B N 10965 C CA . VAL B 494 ? 2.2289 1.5344 2.7691 -0.0576 -1.0229 -0.1423 494 VAL B CA 10966 C C . VAL B 494 ? 2.2079 1.4759 2.6344 -0.0981 -0.9866 -0.0689 494 VAL B C 10967 O O . VAL B 494 ? 2.1802 1.3556 2.5484 -0.1066 -1.0584 -0.0326 494 VAL B O 10968 C CB . VAL B 494 ? 2.2821 1.5035 2.7390 -0.0690 -1.1090 -0.1160 494 VAL B CB 10969 C CG1 . VAL B 494 ? 2.1626 1.3538 2.4590 -0.1282 -1.0685 -0.0375 494 VAL B CG1 10970 C CG2 . VAL B 494 ? 2.1329 1.4169 2.6851 -0.0399 -1.1108 -0.1828 494 VAL B CG2 10971 N N . CYS B 495 ? 2.3292 1.6682 2.7255 -0.1228 -0.8777 -0.0515 495 CYS B N 10972 C CA . CYS B 495 ? 2.4543 1.7813 2.7511 -0.1611 -0.8292 0.0082 495 CYS B CA 10973 C C . CYS B 495 ? 2.4270 1.7343 2.7597 -0.1481 -0.8425 0.0090 495 CYS B C 10974 O O . CYS B 495 ? 2.4735 1.7355 2.7133 -0.1807 -0.8439 0.0625 495 CYS B O 10975 C CB . CYS B 495 ? 2.5990 1.8452 2.7423 -0.2101 -0.8742 0.0743 495 CYS B CB 10976 S SG . CYS B 495 ? 2.9824 2.2670 3.0620 -0.2364 -0.8357 0.0816 495 CYS B SG 10977 N N . SER B 496 ? 2.2769 1.6252 2.7458 -0.1036 -0.8494 -0.0547 496 SER B N 10978 C CA . SER B 496 ? 2.2354 1.5780 2.7565 -0.0863 -0.8586 -0.0651 496 SER B CA 10979 C C . SER B 496 ? 2.2636 1.4890 2.7421 -0.0836 -0.9762 -0.0386 496 SER B C 10980 O O . SER B 496 ? 2.1614 1.3662 2.6822 -0.0661 -1.0039 -0.0482 496 SER B O 10981 C CB . SER B 496 ? 2.0856 1.4626 2.5504 -0.1145 -0.7671 -0.0259 496 SER B CB 10982 O OG . SER B 496 ? 1.9827 1.4307 2.4311 -0.1287 -0.6766 -0.0286 496 SER B OG 10983 N N . GLN B 497 ? 2.4166 1.5609 2.8076 -0.1020 -1.0478 -0.0068 497 GLN B N 10984 C CA . GLN B 497 ? 2.4869 1.4910 2.7927 -0.1138 -1.1689 0.0325 497 GLN B CA 10985 C C . GLN B 497 ? 2.5400 1.4791 2.6921 -0.1752 -1.1563 0.1148 497 GLN B C 10986 O O . GLN B 497 ? 2.5923 1.4085 2.6248 -0.2095 -1.2430 0.1638 497 GLN B O 10987 C CB . GLN B 497 ? 2.3727 1.3423 2.7906 -0.0601 -1.2546 -0.0195 497 GLN B CB 10988 C CG . GLN B 497 ? 2.3631 1.3759 2.9267 -0.0010 -1.3025 -0.1076 497 GLN B CG 10989 C CD . GLN B 497 ? 2.3987 1.4582 3.1125 0.0505 -1.3190 -0.1789 497 GLN B CD 10990 O OE1 . GLN B 497 ? 2.2092 1.3070 2.9322 0.0409 -1.2547 -0.1666 497 GLN B OE1 10991 N NE2 . GLN B 497 ? 2.4461 1.5041 3.2787 0.1056 -1.4085 -0.2571 497 GLN B NE2 10992 N N . ARG B 498 ? 2.5810 1.6001 2.7290 -0.1934 -1.0502 0.1284 498 ARG B N 10993 C CA . ARG B 498 ? 2.6899 1.6785 2.6910 -0.2585 -1.0183 0.1981 498 ARG B CA 10994 C C . ARG B 498 ? 2.7443 1.7625 2.6686 -0.2930 -0.9816 0.2159 498 ARG B C 10995 O O . ARG B 498 ? 2.6338 1.7506 2.6283 -0.2703 -0.9083 0.1795 498 ARG B O 10996 C CB . ARG B 498 ? 2.6427 1.7110 2.6743 -0.2599 -0.9225 0.1983 498 ARG B CB 10997 C CG . ARG B 498 ? 2.6032 1.6578 2.7324 -0.2187 -0.9530 0.1697 498 ARG B CG 10998 C CD . ARG B 498 ? 2.5345 1.6810 2.7122 -0.2119 -0.8521 0.1590 498 ARG B CD 10999 N NE . ARG B 498 ? 2.4652 1.7199 2.7432 -0.1795 -0.7740 0.1069 498 ARG B NE 11000 C CZ . ARG B 498 ? 2.3383 1.6724 2.6654 -0.1690 -0.6875 0.0885 498 ARG B CZ 11001 N NH1 . ARG B 498 ? 2.1332 1.4594 2.4285 -0.1832 -0.6667 0.1154 498 ARG B NH1 11002 N NH2 . ARG B 498 ? 2.2709 1.6866 2.6723 -0.1475 -0.6242 0.0438 498 ARG B NH2 11003 N N . GLY B 499 ? 2.7989 1.7269 2.5771 -0.3497 -1.0371 0.2691 499 GLY B N 11004 C CA . GLY B 499 ? 2.8117 1.7566 2.5122 -0.3843 -1.0195 0.2834 499 GLY B CA 11005 C C . GLY B 499 ? 2.7927 1.6712 2.5238 -0.3532 -1.1148 0.2606 499 GLY B C 11006 O O . GLY B 499 ? 2.9410 1.7132 2.6710 -0.3384 -1.2175 0.2642 499 GLY B O 11007 N N . GLU B 500 ? 2.7038 1.6364 2.4529 -0.3459 -1.0876 0.2388 500 GLU B N 11008 C CA . GLU B 500 ? 2.7153 1.6205 2.5257 -0.3056 -1.1579 0.2006 500 GLU B CA 11009 C C . GLU B 500 ? 2.8115 1.8063 2.6142 -0.3178 -1.0826 0.1897 500 GLU B C 11010 O O . GLU B 500 ? 2.7933 1.8589 2.5505 -0.3510 -0.9904 0.2087 500 GLU B O 11011 C CB . GLU B 500 ? 2.8001 1.5488 2.5035 -0.3291 -1.2928 0.2360 500 GLU B CB 11012 C CG . GLU B 500 ? 2.8361 1.4953 2.6058 -0.2824 -1.3988 0.2131 500 GLU B CG 11013 C CD . GLU B 500 ? 3.0830 1.5605 2.7017 -0.3231 -1.5312 0.2673 500 GLU B CD 11014 O OE1 . GLU B 500 ? 3.2795 1.6905 2.8129 -0.3461 -1.5903 0.2845 500 GLU B OE1 11015 O OE2 . GLU B 500 ? 3.1314 1.5279 2.7038 -0.3387 -1.5737 0.2967 500 GLU B OE2 11016 N N . CYS B 501 ? 2.8375 1.8311 2.6864 -0.2898 -1.1229 0.1558 501 CYS B N 11017 C CA . CYS B 501 ? 2.8183 1.8945 2.6579 -0.3022 -1.0516 0.1456 501 CYS B CA 11018 C C . CYS B 501 ? 2.8932 1.8954 2.6229 -0.3367 -1.1209 0.1735 501 CYS B C 11019 O O . CYS B 501 ? 2.9424 1.8664 2.6929 -0.3104 -1.2222 0.1575 501 CYS B O 11020 C CB . CYS B 501 ? 2.7823 1.9537 2.7817 -0.2432 -1.0082 0.0734 501 CYS B CB 11021 S SG . CYS B 501 ? 3.5107 2.8037 3.5120 -0.2571 -0.8822 0.0611 501 CYS B SG 11022 N N . LEU B 502 ? 2.8652 1.8916 2.4766 -0.3962 -1.0705 0.2117 502 LEU B N 11023 C CA . LEU B 502 ? 2.9110 1.8853 2.4104 -0.4374 -1.1191 0.2363 502 LEU B CA 11024 C C . LEU B 502 ? 2.8784 1.9626 2.3703 -0.4536 -1.0266 0.2227 502 LEU B C 11025 O O . LEU B 502 ? 2.8339 2.0027 2.3161 -0.4730 -0.9334 0.2261 502 LEU B O 11026 C CB . LEU B 502 ? 3.0611 1.9252 2.3795 -0.5154 -1.1759 0.3045 502 LEU B CB 11027 C CG . LEU B 502 ? 3.1221 2.0325 2.3406 -0.5829 -1.0972 0.3421 502 LEU B CG 11028 C CD1 . LEU B 502 ? 3.1201 2.0741 2.2213 -0.6495 -1.0563 0.3597 502 LEU B CD1 11029 C CD2 . LEU B 502 ? 3.2339 2.0255 2.3492 -0.6272 -1.1643 0.3917 502 LEU B CD2 11030 N N . CYS B 503 ? 2.9147 1.9948 2.4160 -0.4414 -1.0590 0.2028 503 CYS B N 11031 C CA . CYS B 503 ? 2.7772 1.9494 2.2740 -0.4522 -0.9880 0.1853 503 CYS B CA 11032 C C . CYS B 503 ? 2.7639 2.0501 2.4021 -0.3998 -0.8962 0.1337 503 CYS B C 11033 O O . CYS B 503 ? 2.8692 2.2328 2.5220 -0.3990 -0.8345 0.1121 503 CYS B O 11034 C CB . CYS B 503 ? 2.7434 1.9386 2.0950 -0.5294 -0.9428 0.2268 503 CYS B CB 11035 S SG . CYS B 503 ? 3.4956 2.7723 2.8074 -0.5535 -0.8935 0.2094 503 CYS B SG 11036 N N . GLY B 504 ? 2.7253 2.0150 2.4611 -0.3592 -0.8912 0.1137 504 GLY B N 11037 C CA . GLY B 504 ? 2.7032 2.0846 2.5625 -0.3165 -0.8105 0.0674 504 GLY B CA 11038 C C . GLY B 504 ? 2.7569 2.1807 2.6029 -0.3292 -0.7364 0.0836 504 GLY B C 11039 O O . GLY B 504 ? 2.7160 2.1858 2.6577 -0.2948 -0.6888 0.0525 504 GLY B O 11040 N N . GLN B 505 ? 2.7677 2.1784 2.4931 -0.3819 -0.7267 0.1289 505 GLN B N 11041 C CA . GLN B 505 ? 2.5458 1.9828 2.2521 -0.3962 -0.6750 0.1463 505 GLN B CA 11042 C C . GLN B 505 ? 2.6539 2.0078 2.3525 -0.3974 -0.7397 0.1713 505 GLN B C 11043 O O . GLN B 505 ? 2.8127 2.0776 2.4746 -0.4054 -0.8297 0.1879 505 GLN B O 11044 C CB . GLN B 505 ? 2.5681 2.0405 2.1556 -0.4551 -0.6346 0.1740 505 GLN B CB 11045 C CG . GLN B 505 ? 2.5797 2.1440 2.1804 -0.4494 -0.5639 0.1433 505 GLN B CG 11046 C CD . GLN B 505 ? 2.7997 2.3553 2.3786 -0.4558 -0.5963 0.1346 505 GLN B CD 11047 O OE1 . GLN B 505 ? 3.0256 2.5035 2.5715 -0.4669 -0.6743 0.1532 505 GLN B OE1 11048 N NE2 . GLN B 505 ? 2.7354 2.3655 2.3310 -0.4472 -0.5414 0.1048 505 GLN B NE2 11049 N N . CYS B 506 ? 2.6086 1.9849 2.3399 -0.3879 -0.6997 0.1728 506 CYS B N 11050 C CA . CYS B 506 ? 2.4602 1.7582 2.1760 -0.3930 -0.7585 0.1983 506 CYS B CA 11051 C C . CYS B 506 ? 2.5089 1.7880 2.0959 -0.4576 -0.7474 0.2474 506 CYS B C 11052 O O . CYS B 506 ? 2.4915 1.8406 2.0781 -0.4662 -0.6715 0.2456 506 CYS B O 11053 C CB . CYS B 506 ? 2.2449 1.5743 2.0848 -0.3416 -0.7302 0.1654 506 CYS B CB 11054 S SG . CYS B 506 ? 2.9686 2.3314 2.9655 -0.2750 -0.7399 0.0975 506 CYS B SG 11055 N N . VAL B 507 ? 2.7532 1.9352 2.2266 -0.5060 -0.8258 0.2889 507 VAL B N 11056 C CA . VAL B 507 ? 2.9559 2.1067 2.2990 -0.5773 -0.8250 0.3358 507 VAL B CA 11057 C C . VAL B 507 ? 3.0362 2.0969 2.3889 -0.5676 -0.8858 0.3556 507 VAL B C 11058 O O . VAL B 507 ? 3.0863 2.0333 2.4219 -0.5601 -0.9870 0.3684 507 VAL B O 11059 C CB . VAL B 507 ? 3.0695 2.1597 2.2558 -0.6530 -0.8726 0.3738 507 VAL B CB 11060 C CG1 . VAL B 507 ? 3.1707 2.2281 2.2166 -0.7374 -0.8711 0.4196 507 VAL B CG1 11061 C CG2 . VAL B 507 ? 2.8999 2.0874 2.0816 -0.6614 -0.8114 0.3493 507 VAL B CG2 11062 N N . CYS B 508 ? 3.0327 2.1422 2.4141 -0.5651 -0.8280 0.3548 508 CYS B N 11063 C CA . CYS B 508 ? 3.0839 2.1261 2.5006 -0.5444 -0.8738 0.3641 508 CYS B CA 11064 C C . CYS B 508 ? 3.1866 2.1005 2.4567 -0.6125 -0.9558 0.4204 508 CYS B C 11065 O O . CYS B 508 ? 3.1618 2.0847 2.3066 -0.6891 -0.9256 0.4541 508 CYS B O 11066 C CB . CYS B 508 ? 2.9986 2.1307 2.4806 -0.5256 -0.7859 0.3480 508 CYS B CB 11067 S SG . CYS B 508 ? 2.7530 2.0143 2.3900 -0.4524 -0.6941 0.2858 508 CYS B SG 11068 N N . HIS B 509 ? 3.3203 2.1140 2.6054 -0.5862 -1.0626 0.4261 509 HIS B N 11069 C CA . HIS B 509 ? 3.5768 2.2229 2.7207 -0.6467 -1.1556 0.4804 509 HIS B CA 11070 C C . HIS B 509 ? 3.5966 2.2244 2.7759 -0.6349 -1.1540 0.4863 509 HIS B C 11071 O O . HIS B 509 ? 3.3352 2.0739 2.6357 -0.5879 -1.0720 0.4510 509 HIS B O 11072 C CB . HIS B 509 ? 3.6385 2.1449 2.7644 -0.6251 -1.2889 0.4835 509 HIS B CB 11073 C CG . HIS B 509 ? 3.4904 1.9638 2.7673 -0.5353 -1.3519 0.4398 509 HIS B CG 11074 N ND1 . HIS B 509 ? 3.3067 1.8909 2.7443 -0.4717 -1.2803 0.3921 509 HIS B ND1 11075 C CD2 . HIS B 509 ? 3.4715 1.8153 2.7631 -0.4994 -1.4837 0.4309 509 HIS B CD2 11076 C CE1 . HIS B 509 ? 3.2340 1.7689 2.7817 -0.4041 -1.3595 0.3532 509 HIS B CE1 11077 N NE2 . HIS B 509 ? 3.3416 1.7328 2.8097 -0.4152 -1.4855 0.3728 509 HIS B NE2 11078 N N . SER B 510 ? 3.9425 2.4235 3.0101 -0.6794 -1.2478 0.5314 510 SER B N 11079 C CA . SER B 510 ? 4.0595 2.5051 3.1458 -0.6744 -1.2590 0.5415 510 SER B CA 11080 C C . SER B 510 ? 3.8319 2.4026 2.9116 -0.7089 -1.1359 0.5449 510 SER B C 11081 O O . SER B 510 ? 3.7160 2.3587 2.9142 -0.6574 -1.0851 0.5157 510 SER B O 11082 C CB . SER B 510 ? 4.0325 2.4907 3.3055 -0.5695 -1.2896 0.4867 510 SER B CB 11083 O OG . SER B 510 ? 4.1799 2.5377 3.4778 -0.5291 -1.4043 0.4699 510 SER B OG 11084 N N . SER B 511 ? 3.7476 2.3475 2.6895 -0.7967 -1.0898 0.5758 511 SER B N 11085 C CA . SER B 511 ? 3.4819 2.2042 2.4133 -0.8324 -0.9793 0.5722 511 SER B CA 11086 C C . SER B 511 ? 3.4844 2.1224 2.2915 -0.9089 -1.0099 0.6184 511 SER B C 11087 O O . SER B 511 ? 3.6898 2.2443 2.3237 -1.0054 -1.0510 0.6631 511 SER B O 11088 C CB . SER B 511 ? 3.4556 2.2833 2.3237 -0.8830 -0.9033 0.5650 511 SER B CB 11089 O OG . SER B 511 ? 3.6312 2.3616 2.3289 -0.9705 -0.9653 0.6074 511 SER B OG 11090 N N . ASP B 512 ? 3.2151 1.8785 2.1090 -0.8691 -0.9861 0.6057 512 ASP B N 11091 C CA . ASP B 512 ? 3.2126 1.7989 2.0157 -0.9274 -1.0145 0.6435 512 ASP B CA 11092 C C . ASP B 512 ? 3.0521 1.6999 2.0071 -0.8502 -0.9755 0.6110 512 ASP B C 11093 O O . ASP B 512 ? 2.9049 1.6108 2.0161 -0.7569 -0.9584 0.5663 512 ASP B O 11094 C CB . ASP B 512 ? 3.4071 1.8471 2.1367 -0.9426 -1.1371 0.6545 512 ASP B CB 11095 C CG . ASP B 512 ? 3.6291 2.0348 2.2520 -1.0149 -1.1498 0.6688 512 ASP B CG 11096 O OD1 . ASP B 512 ? 3.5487 2.0317 2.1997 -1.0196 -1.0807 0.6656 512 ASP B OD1 11097 O OD2 . ASP B 512 ? 3.7088 2.0047 2.2189 -1.0697 -1.2308 0.6814 512 ASP B OD2 11098 N N . PHE B 513 ? 2.9745 1.6117 1.8812 -0.8924 -0.9608 0.6306 513 PHE B N 11099 C CA . PHE B 513 ? 2.8781 1.5773 1.9155 -0.8290 -0.9177 0.6026 513 PHE B CA 11100 C C . PHE B 513 ? 2.8795 1.7553 2.0415 -0.7724 -0.8028 0.5510 513 PHE B C 11101 O O . PHE B 513 ? 2.7314 1.6590 2.0392 -0.6893 -0.7776 0.5132 513 PHE B O 11102 C CB . PHE B 513 ? 2.8202 1.4192 1.9568 -0.7512 -1.0103 0.5908 513 PHE B CB 11103 C CG . PHE B 513 ? 2.8233 1.4799 2.0906 -0.6893 -0.9728 0.5604 513 PHE B CG 11104 C CD1 . PHE B 513 ? 2.9104 1.5631 2.1263 -0.7310 -0.9539 0.5805 513 PHE B CD1 11105 C CD2 . PHE B 513 ? 2.5339 1.2571 1.9744 -0.5916 -0.9541 0.5065 513 PHE B CD2 11106 C CE1 . PHE B 513 ? 2.7456 1.4436 2.0775 -0.6767 -0.9223 0.5554 513 PHE B CE1 11107 C CE2 . PHE B 513 ? 2.5468 1.3235 2.1004 -0.5404 -0.9187 0.4775 513 PHE B CE2 11108 C CZ . PHE B 513 ? 2.6092 1.3719 2.1095 -0.5804 -0.9039 0.5028 513 PHE B CZ 11109 N N . GLY B 514 ? 3.1088 2.0737 2.2062 -0.8219 -0.7362 0.5476 514 GLY B N 11110 C CA . GLY B 514 ? 3.0825 2.1952 2.2804 -0.7708 -0.6425 0.4995 514 GLY B CA 11111 C C . GLY B 514 ? 3.1380 2.2555 2.3350 -0.7588 -0.6555 0.4893 514 GLY B C 11112 O O . GLY B 514 ? 3.1686 2.1732 2.3069 -0.7766 -0.7412 0.5159 514 GLY B O 11113 N N . LYS B 515 ? 3.0601 2.3016 2.3192 -0.7277 -0.5757 0.4498 515 LYS B N 11114 C CA . LYS B 515 ? 3.1806 2.4389 2.4370 -0.7197 -0.5792 0.4374 515 LYS B CA 11115 C C . LYS B 515 ? 3.0385 2.3190 2.4401 -0.6258 -0.5743 0.3994 515 LYS B C 11116 O O . LYS B 515 ? 2.9278 2.2634 2.4338 -0.5701 -0.5289 0.3705 515 LYS B O 11117 C CB . LYS B 515 ? 3.1257 2.5041 2.3349 -0.7599 -0.4998 0.4167 515 LYS B CB 11118 C CG . LYS B 515 ? 2.9035 2.4068 2.2160 -0.7047 -0.4116 0.3695 515 LYS B CG 11119 C CD . LYS B 515 ? 2.7600 2.3776 2.0398 -0.7311 -0.3478 0.3384 515 LYS B CD 11120 C CE . LYS B 515 ? 2.5748 2.2972 1.9576 -0.6663 -0.2748 0.2888 515 LYS B CE 11121 N NZ . LYS B 515 ? 2.5436 2.3753 1.9042 -0.6829 -0.2218 0.2501 515 LYS B NZ 11122 N N . ILE B 516 ? 2.9026 2.1392 2.3049 -0.6136 -0.6219 0.3983 516 ILE B N 11123 C CA . ILE B 516 ? 2.6687 1.9333 2.2001 -0.5356 -0.6157 0.3579 516 ILE B CA 11124 C C . ILE B 516 ? 2.6034 1.9537 2.1374 -0.5330 -0.5589 0.3331 516 ILE B C 11125 O O . ILE B 516 ? 2.7011 2.0352 2.1454 -0.5794 -0.5795 0.3498 516 ILE B O 11126 C CB . ILE B 516 ? 2.6794 1.8368 2.2335 -0.5115 -0.7160 0.3626 516 ILE B CB 11127 C CG1 . ILE B 516 ? 2.6004 1.6671 2.1607 -0.5063 -0.7816 0.3807 516 ILE B CG1 11128 C CG2 . ILE B 516 ? 2.4868 1.6909 2.1768 -0.4383 -0.7018 0.3121 516 ILE B CG2 11129 C CD1 . ILE B 516 ? 2.4545 1.5779 2.1436 -0.4471 -0.7381 0.3460 516 ILE B CD1 11130 N N . THR B 517 ? 2.5249 1.9606 2.1561 -0.4810 -0.4906 0.2931 517 THR B N 11131 C CA . THR B 517 ? 2.4541 1.9680 2.0923 -0.4731 -0.4371 0.2659 517 THR B CA 11132 C C . THR B 517 ? 2.2991 1.8322 2.0523 -0.4075 -0.4236 0.2271 517 THR B C 11133 O O . THR B 517 ? 2.2798 1.7728 2.1089 -0.3712 -0.4570 0.2175 517 THR B O 11134 C CB . THR B 517 ? 2.4692 2.0764 2.0883 -0.4856 -0.3588 0.2506 517 THR B CB 11135 O OG1 . THR B 517 ? 2.4372 2.1128 2.0670 -0.4722 -0.3160 0.2195 517 THR B OG1 11136 C CG2 . THR B 517 ? 2.4388 2.0682 2.1400 -0.4402 -0.3228 0.2333 517 THR B CG2 11137 N N . GLY B 518 ? 2.2540 1.8508 2.0185 -0.3956 -0.3753 0.2007 518 GLY B N 11138 C CA . GLY B 518 ? 2.2412 1.8554 2.0987 -0.3451 -0.3590 0.1640 518 GLY B CA 11139 C C . GLY B 518 ? 2.3969 1.9847 2.2488 -0.3476 -0.4020 0.1604 518 GLY B C 11140 O O . GLY B 518 ? 2.5376 2.0679 2.3291 -0.3790 -0.4637 0.1889 518 GLY B O 11141 N N . LYS B 519 ? 2.3064 1.9296 2.2149 -0.3170 -0.3725 0.1257 519 LYS B N 11142 C CA . LYS B 519 ? 2.3285 1.9363 2.2388 -0.3164 -0.4073 0.1165 519 LYS B CA 11143 C C . LYS B 519 ? 2.2650 1.8201 2.2452 -0.2912 -0.4705 0.1053 519 LYS B C 11144 O O . LYS B 519 ? 2.2570 1.7681 2.2158 -0.2998 -0.5322 0.1125 519 LYS B O 11145 C CB . LYS B 519 ? 2.4173 2.0793 2.3634 -0.2944 -0.3543 0.0807 519 LYS B CB 11146 C CG . LYS B 519 ? 2.4982 2.2154 2.3987 -0.3042 -0.2931 0.0777 519 LYS B CG 11147 C CD . LYS B 519 ? 2.5549 2.2837 2.3544 -0.3524 -0.3039 0.1049 519 LYS B CD 11148 C CE . LYS B 519 ? 2.4537 2.2485 2.2227 -0.3581 -0.2461 0.0915 519 LYS B CE 11149 N NZ . LYS B 519 ? 2.4029 2.2010 2.2127 -0.3342 -0.2171 0.0876 519 LYS B NZ 11150 N N . TYR B 520 ? 2.2513 1.8139 2.3171 -0.2592 -0.4567 0.0825 520 TYR B N 11151 C CA . TYR B 520 ? 2.2781 1.8025 2.4229 -0.2324 -0.5174 0.0616 520 TYR B CA 11152 C C . TYR B 520 ? 2.3674 1.8321 2.4804 -0.2442 -0.5676 0.0943 520 TYR B C 11153 O O . TYR B 520 ? 2.3538 1.7832 2.5337 -0.2187 -0.6231 0.0758 520 TYR B O 11154 C CB . TYR B 520 ? 2.1993 1.7731 2.4586 -0.1962 -0.4745 0.0097 520 TYR B CB 11155 C CG . TYR B 520 ? 2.2635 1.8830 2.5535 -0.1885 -0.4344 -0.0250 520 TYR B CG 11156 C CD1 . TYR B 520 ? 2.2950 1.9530 2.5485 -0.1973 -0.3619 -0.0233 520 TYR B CD1 11157 C CD2 . TYR B 520 ? 2.2884 1.9089 2.6429 -0.1717 -0.4738 -0.0626 520 TYR B CD2 11158 C CE1 . TYR B 520 ? 2.2359 1.9241 2.5095 -0.1927 -0.3300 -0.0534 520 TYR B CE1 11159 C CE2 . TYR B 520 ? 2.2411 1.9020 2.6204 -0.1691 -0.4366 -0.0945 520 TYR B CE2 11160 C CZ . TYR B 520 ? 2.2437 1.9342 2.5787 -0.1813 -0.3648 -0.0874 520 TYR B CZ 11161 O OH . TYR B 520 ? 2.2560 1.9756 2.6083 -0.1810 -0.3322 -0.1177 520 TYR B OH 11162 N N . CYS B 521 ? 2.4257 1.8843 2.4398 -0.2832 -0.5472 0.1373 521 CYS B N 11163 C CA . CYS B 521 ? 2.4630 1.8644 2.4265 -0.3060 -0.5867 0.1739 521 CYS B CA 11164 C C . CYS B 521 ? 2.4758 1.8980 2.5204 -0.2750 -0.5595 0.1551 521 CYS B C 11165 O O . CYS B 521 ? 2.5046 1.8838 2.5229 -0.2876 -0.5879 0.1800 521 CYS B O 11166 C CB . CYS B 521 ? 2.4931 1.7953 2.4274 -0.3138 -0.6930 0.1916 521 CYS B CB 11167 S SG . CYS B 521 ? 2.1770 1.4348 1.9816 -0.3659 -0.7343 0.2264 521 CYS B SG 11168 N N . GLU B 522 ? 2.4780 1.9628 2.6153 -0.2389 -0.5055 0.1109 522 GLU B N 11169 C CA . GLU B 522 ? 2.4632 1.9745 2.6834 -0.2103 -0.4755 0.0849 522 GLU B CA 11170 C C . GLU B 522 ? 2.3431 1.8649 2.5144 -0.2278 -0.4343 0.1137 522 GLU B C 11171 O O . GLU B 522 ? 2.3295 1.8534 2.5530 -0.2103 -0.4284 0.1031 522 GLU B O 11172 C CB . GLU B 522 ? 2.4024 1.9780 2.6985 -0.1852 -0.4146 0.0371 522 GLU B CB 11173 C CG . GLU B 522 ? 2.3865 1.9914 2.7744 -0.1597 -0.3870 0.0005 522 GLU B CG 11174 C CD . GLU B 522 ? 2.3195 1.9790 2.7546 -0.1503 -0.3227 -0.0413 522 GLU B CD 11175 O OE1 . GLU B 522 ? 2.3223 1.9930 2.7246 -0.1587 -0.3044 -0.0423 522 GLU B OE1 11176 O OE2 . GLU B 522 ? 2.2713 1.9590 2.7704 -0.1384 -0.2912 -0.0733 522 GLU B OE2 11177 N N . CYS B 523 ? 2.2038 1.7381 2.2789 -0.2627 -0.4071 0.1449 523 CYS B N 11178 C CA . CYS B 523 ? 1.9960 1.5534 2.0304 -0.2785 -0.3646 0.1632 523 CYS B CA 11179 C C . CYS B 523 ? 2.1829 1.6936 2.1222 -0.3260 -0.4066 0.2082 523 CYS B C 11180 O O . CYS B 523 ? 2.2585 1.7116 2.1493 -0.3499 -0.4689 0.2291 523 CYS B O 11181 C CB . CYS B 523 ? 1.8385 1.4623 1.8446 -0.2807 -0.2931 0.1511 523 CYS B CB 11182 S SG . CYS B 523 ? 2.6633 2.3265 2.7560 -0.2357 -0.2398 0.1036 523 CYS B SG 11183 N N . ASP B 524 ? 2.3792 1.9122 2.2855 -0.3432 -0.3728 0.2221 524 ASP B N 11184 C CA . ASP B 524 ? 2.5125 1.9982 2.3332 -0.3925 -0.4099 0.2626 524 ASP B CA 11185 C C . ASP B 524 ? 2.4041 1.9327 2.2119 -0.4026 -0.3605 0.2658 524 ASP B C 11186 O O . ASP B 524 ? 2.3075 1.8992 2.1682 -0.3693 -0.3001 0.2374 524 ASP B O 11187 C CB . ASP B 524 ? 2.5679 1.9586 2.4093 -0.3850 -0.4947 0.2774 524 ASP B CB 11188 C CG . ASP B 524 ? 2.4463 1.8436 2.3977 -0.3338 -0.4887 0.2503 524 ASP B CG 11189 O OD1 . ASP B 524 ? 2.3529 1.8159 2.3809 -0.2956 -0.4306 0.2139 524 ASP B OD1 11190 O OD2 . ASP B 524 ? 2.4090 1.7421 2.3650 -0.3348 -0.5442 0.2646 524 ASP B OD2 11191 N N . ASP B 525 ? 2.5011 1.9875 2.2310 -0.4520 -0.3914 0.3007 525 ASP B N 11192 C CA . ASP B 525 ? 2.4215 1.9343 2.1401 -0.4652 -0.3593 0.3063 525 ASP B CA 11193 C C . ASP B 525 ? 2.4316 1.8605 2.1819 -0.4525 -0.4195 0.3233 525 ASP B C 11194 O O . ASP B 525 ? 2.6211 1.9770 2.3884 -0.4400 -0.4866 0.3292 525 ASP B O 11195 C CB . ASP B 525 ? 2.3865 1.9235 1.9871 -0.5403 -0.3445 0.3279 525 ASP B CB 11196 C CG . ASP B 525 ? 2.3483 1.9831 1.9291 -0.5485 -0.2842 0.2996 525 ASP B CG 11197 O OD1 . ASP B 525 ? 2.2052 1.8930 1.8643 -0.4918 -0.2421 0.2640 525 ASP B OD1 11198 O OD2 . ASP B 525 ? 2.4845 2.1416 1.9677 -0.6146 -0.2808 0.3103 525 ASP B OD2 11199 N N . PHE B 526 ? 2.2469 1.6932 2.0214 -0.4451 -0.3948 0.3219 526 PHE B N 11200 C CA . PHE B 526 ? 2.3423 1.7185 2.1487 -0.4332 -0.4461 0.3342 526 PHE B CA 11201 C C . PHE B 526 ? 2.2857 1.6544 2.2198 -0.3635 -0.4627 0.2993 526 PHE B C 11202 O O . PHE B 526 ? 2.3800 1.7085 2.3621 -0.3433 -0.4981 0.2968 526 PHE B O 11203 C CB . PHE B 526 ? 2.4510 1.7144 2.1573 -0.4888 -0.5337 0.3794 526 PHE B CB 11204 C CG . PHE B 526 ? 2.3906 1.5714 2.1116 -0.4704 -0.6153 0.3807 526 PHE B CG 11205 C CD1 . PHE B 526 ? 2.3308 1.4745 2.1606 -0.4096 -0.6634 0.3540 526 PHE B CD1 11206 C CD2 . PHE B 526 ? 2.4338 1.5730 2.0554 -0.5180 -0.6494 0.4058 526 PHE B CD2 11207 C CE1 . PHE B 526 ? 2.3269 1.4013 2.1762 -0.3898 -0.7423 0.3468 526 PHE B CE1 11208 C CE2 . PHE B 526 ? 2.3854 1.4456 2.0179 -0.4996 -0.7291 0.4053 526 PHE B CE2 11209 C CZ . PHE B 526 ? 2.3264 1.3544 2.0755 -0.4333 -0.7775 0.3743 526 PHE B CZ 11210 N N . SER B 527 ? 2.3123 1.7252 2.3026 -0.3295 -0.4353 0.2680 527 SER B N 11211 C CA . SER B 527 ? 2.3443 1.7647 2.4545 -0.2725 -0.4433 0.2268 527 SER B CA 11212 C C . SER B 527 ? 2.2554 1.7348 2.4354 -0.2411 -0.3813 0.1996 527 SER B C 11213 O O . SER B 527 ? 2.1732 1.6679 2.4506 -0.2015 -0.3803 0.1616 527 SER B O 11214 C CB . SER B 527 ? 2.3555 1.8040 2.4959 -0.2545 -0.4316 0.2009 527 SER B CB 11215 O OG . SER B 527 ? 2.3207 1.8226 2.4024 -0.2745 -0.3715 0.2069 527 SER B OG 11216 N N . CYS B 528 ? 2.2161 1.7315 2.3449 -0.2612 -0.3307 0.2150 528 CYS B N 11217 C CA . CYS B 528 ? 2.0363 1.6040 2.2153 -0.2337 -0.2707 0.1916 528 CYS B CA 11218 C C . CYS B 528 ? 1.9896 1.5318 2.2251 -0.2169 -0.2962 0.1868 528 CYS B C 11219 O O . CYS B 528 ? 2.0556 1.5356 2.2952 -0.2231 -0.3654 0.1997 528 CYS B O 11220 C CB . CYS B 528 ? 2.0272 1.6418 2.1368 -0.2571 -0.2174 0.2037 528 CYS B CB 11221 S SG . CYS B 528 ? 1.9163 1.5707 1.9613 -0.2765 -0.1888 0.2016 528 CYS B SG 11222 N N . VAL B 529 ? 1.9010 1.4864 2.1768 -0.1951 -0.2444 0.1669 529 VAL B N 11223 C CA . VAL B 529 ? 1.7988 1.3729 2.1386 -0.1754 -0.2595 0.1544 529 VAL B CA 11224 C C . VAL B 529 ? 1.9637 1.5256 2.2523 -0.1992 -0.2601 0.1847 529 VAL B C 11225 O O . VAL B 529 ? 1.9345 1.5044 2.1383 -0.2342 -0.2450 0.2118 529 VAL B O 11226 C CB . VAL B 529 ? 1.5140 1.1390 1.9244 -0.1428 -0.2038 0.1133 529 VAL B CB 11227 C CG1 . VAL B 529 ? 1.5683 1.2037 2.0470 -0.1230 -0.2117 0.0749 529 VAL B CG1 11228 C CG2 . VAL B 529 ? 1.4455 1.1113 1.8026 -0.1472 -0.1369 0.1169 529 VAL B CG2 11229 N N . ARG B 530 ? 1.9812 1.5303 2.3246 -0.1821 -0.2766 0.1749 530 ARG B N 11230 C CA . ARG B 530 ? 1.6950 1.2288 1.9977 -0.2040 -0.2811 0.2011 530 ARG B CA 11231 C C . ARG B 530 ? 1.5842 1.1594 1.9474 -0.1751 -0.2379 0.1760 530 ARG B C 11232 O O . ARG B 530 ? 1.5115 1.1102 1.9559 -0.1409 -0.2238 0.1382 530 ARG B O 11233 C CB . ARG B 530 ? 1.7269 1.1760 2.0169 -0.2206 -0.3672 0.2240 530 ARG B CB 11234 C CG . ARG B 530 ? 1.8639 1.2584 2.1444 -0.2246 -0.4304 0.2285 530 ARG B CG 11235 C CD . ARG B 530 ? 2.1374 1.4282 2.3830 -0.2450 -0.5258 0.2560 530 ARG B CD 11236 N NE . ARG B 530 ? 2.2487 1.4962 2.3611 -0.3107 -0.5374 0.3085 530 ARG B NE 11237 C CZ . ARG B 530 ? 2.2497 1.4601 2.2750 -0.3501 -0.5635 0.3354 530 ARG B CZ 11238 N NH1 . ARG B 530 ? 2.2921 1.5007 2.3538 -0.3249 -0.5829 0.3162 530 ARG B NH1 11239 N NH2 . ARG B 530 ? 2.2181 1.3972 2.1182 -0.4191 -0.5684 0.3787 530 ARG B NH2 11240 N N . TYR B 531 ? 1.7312 1.3179 2.0521 -0.1932 -0.2165 0.1943 531 TYR B N 11241 C CA . TYR B 531 ? 1.8681 1.4913 2.2352 -0.1686 -0.1764 0.1737 531 TYR B CA 11242 C C . TYR B 531 ? 1.9655 1.5498 2.3540 -0.1726 -0.2192 0.1840 531 TYR B C 11243 O O . TYR B 531 ? 2.0846 1.6603 2.5554 -0.1429 -0.2411 0.1575 531 TYR B O 11244 C CB . TYR B 531 ? 1.8775 1.5532 2.1897 -0.1776 -0.1151 0.1767 531 TYR B CB 11245 C CG . TYR B 531 ? 1.7649 1.4684 2.1016 -0.1611 -0.0823 0.1645 531 TYR B CG 11246 C CD1 . TYR B 531 ? 1.6517 1.3627 2.0629 -0.1266 -0.0691 0.1354 531 TYR B CD1 11247 C CD2 . TYR B 531 ? 1.6448 1.3733 1.9291 -0.1831 -0.0626 0.1776 531 TYR B CD2 11248 C CE1 . TYR B 531 ? 1.5605 1.2941 1.9887 -0.1131 -0.0403 0.1249 531 TYR B CE1 11249 C CE2 . TYR B 531 ? 1.6777 1.4316 1.9847 -0.1661 -0.0347 0.1649 531 TYR B CE2 11250 C CZ . TYR B 531 ? 1.7335 1.4856 2.1101 -0.1302 -0.0249 0.1410 531 TYR B CZ 11251 O OH . TYR B 531 ? 1.8113 1.5856 2.2058 -0.1148 0.0015 0.1289 531 TYR B OH 11252 N N . LYS B 532 ? 1.7224 1.2872 2.0370 -0.2119 -0.2303 0.2180 532 LYS B N 11253 C CA . LYS B 532 ? 1.7167 1.2303 2.0341 -0.2240 -0.2780 0.2338 532 LYS B CA 11254 C C . LYS B 532 ? 2.0205 1.4423 2.2947 -0.2532 -0.3621 0.2628 532 LYS B C 11255 O O . LYS B 532 ? 2.1898 1.5455 2.4406 -0.2738 -0.4163 0.2841 532 LYS B O 11256 C CB . LYS B 532 ? 1.6757 1.2169 1.9339 -0.2558 -0.2433 0.2516 532 LYS B CB 11257 C CG . LYS B 532 ? 1.5768 1.1887 1.8855 -0.2203 -0.1786 0.2215 532 LYS B CG 11258 C CD . LYS B 532 ? 1.6814 1.3231 1.9408 -0.2485 -0.1507 0.2331 532 LYS B CD 11259 C CE . LYS B 532 ? 1.7490 1.3339 2.0092 -0.2672 -0.1996 0.2522 532 LYS B CE 11260 N NZ . LYS B 532 ? 1.6185 1.2408 1.8391 -0.2941 -0.1673 0.2576 532 LYS B NZ 11261 N N . GLY B 533 ? 2.0520 1.4625 2.3103 -0.2556 -0.3768 0.2637 533 GLY B N 11262 C CA . GLY B 533 ? 2.1490 1.4677 2.3471 -0.2877 -0.4566 0.2940 533 GLY B CA 11263 C C . GLY B 533 ? 2.1551 1.4814 2.2380 -0.3445 -0.4354 0.3263 533 GLY B C 11264 O O . GLY B 533 ? 2.1008 1.3556 2.1142 -0.3798 -0.4928 0.3539 533 GLY B O 11265 N N . GLU B 534 ? 2.1741 1.5887 2.2369 -0.3532 -0.3550 0.3185 534 GLU B N 11266 C CA . GLU B 534 ? 2.1446 1.5955 2.1166 -0.4001 -0.3226 0.3328 534 GLU B CA 11267 C C . GLU B 534 ? 2.1101 1.6181 2.1236 -0.3630 -0.2822 0.3042 534 GLU B C 11268 O O . GLU B 534 ? 2.0819 1.6479 2.1658 -0.3159 -0.2325 0.2717 534 GLU B O 11269 C CB . GLU B 534 ? 1.9442 1.4629 1.8724 -0.4312 -0.2653 0.3320 534 GLU B CB 11270 C CG . GLU B 534 ? 2.0634 1.6193 1.8879 -0.4959 -0.2423 0.3440 534 GLU B CG 11271 C CD . GLU B 534 ? 2.0899 1.7144 1.8761 -0.5317 -0.1948 0.3362 534 GLU B CD 11272 O OE1 . GLU B 534 ? 1.9327 1.5801 1.7783 -0.4969 -0.1738 0.3207 534 GLU B OE1 11273 O OE2 . GLU B 534 ? 2.1172 1.7780 1.8153 -0.5968 -0.1781 0.3413 534 GLU B OE2 11274 N N . MET B 535 ? 2.0631 1.5472 2.0264 -0.3873 -0.3064 0.3174 535 MET B N 11275 C CA . MET B 535 ? 1.9613 1.4889 1.9597 -0.3554 -0.2761 0.2921 535 MET B CA 11276 C C . MET B 535 ? 1.8117 1.4341 1.8041 -0.3474 -0.1977 0.2683 535 MET B C 11277 O O . MET B 535 ? 1.8477 1.5082 1.7689 -0.3906 -0.1742 0.2760 535 MET B O 11278 C CB . MET B 535 ? 2.2135 1.6984 2.1461 -0.3904 -0.3177 0.3132 535 MET B CB 11279 C CG . MET B 535 ? 2.2007 1.7283 2.1657 -0.3606 -0.2887 0.2877 535 MET B CG 11280 S SD . MET B 535 ? 2.0118 1.4939 1.8932 -0.4049 -0.3356 0.3125 535 MET B SD 11281 C CE . MET B 535 ? 2.3514 1.7058 2.2260 -0.4146 -0.4406 0.3414 535 MET B CE 11282 N N . CYS B 536 ? 1.6818 1.3403 1.7472 -0.2942 -0.1607 0.2354 536 CYS B N 11283 C CA . CYS B 536 ? 1.7080 1.4396 1.7715 -0.2760 -0.0968 0.2086 536 CYS B CA 11284 C C . CYS B 536 ? 1.8002 1.5679 1.8571 -0.2792 -0.0675 0.2038 536 CYS B C 11285 O O . CYS B 536 ? 1.7806 1.6059 1.8350 -0.2617 -0.0219 0.1782 536 CYS B O 11286 C CB . CYS B 536 ? 1.6782 1.4466 1.6775 -0.3038 -0.0823 0.2070 536 CYS B CB 11287 S SG . CYS B 536 ? 1.9045 1.6553 1.9242 -0.2827 -0.0930 0.1970 536 CYS B SG 11288 N N . SER B 537 ? 1.8067 1.5358 1.8586 -0.3013 -0.0998 0.2267 537 SER B N 11289 C CA . SER B 537 ? 1.6302 1.3864 1.6678 -0.3159 -0.0809 0.2276 537 SER B CA 11290 C C . SER B 537 ? 1.6711 1.4701 1.6222 -0.3747 -0.0678 0.2348 537 SER B C 11291 O O . SER B 537 ? 1.6741 1.5052 1.6020 -0.3993 -0.0513 0.2331 537 SER B O 11292 C CB . SER B 537 ? 1.5344 1.3400 1.6238 -0.2667 -0.0316 0.1940 537 SER B CB 11293 O OG . SER B 537 ? 1.4065 1.1829 1.5666 -0.2214 -0.0354 0.1815 537 SER B OG 11294 N N . GLY B 538 ? 1.8299 1.6353 1.7343 -0.4002 -0.0735 0.2386 538 GLY B N 11295 C CA . GLY B 538 ? 1.9156 1.7767 1.7391 -0.4599 -0.0553 0.2357 538 GLY B CA 11296 C C . GLY B 538 ? 1.9880 1.9489 1.8316 -0.4298 0.0012 0.1871 538 GLY B C 11297 O O . GLY B 538 ? 2.0792 2.1136 1.8734 -0.4694 0.0253 0.1663 538 GLY B O 11298 N N . HIS B 539 ? 1.8545 1.8159 1.7690 -0.3609 0.0191 0.1651 539 HIS B N 11299 C CA . HIS B 539 ? 1.6786 1.7120 1.6135 -0.3216 0.0613 0.1183 539 HIS B CA 11300 C C . HIS B 539 ? 1.6461 1.6817 1.5835 -0.2974 0.0648 0.1028 539 HIS B C 11301 O O . HIS B 539 ? 1.7029 1.7793 1.6558 -0.2585 0.0899 0.0641 539 HIS B O 11302 C CB . HIS B 539 ? 1.6113 1.6326 1.6045 -0.2668 0.0762 0.1044 539 HIS B CB 11303 C CG . HIS B 539 ? 1.6158 1.6400 1.6119 -0.2854 0.0751 0.1153 539 HIS B CG 11304 N ND1 . HIS B 539 ? 1.6960 1.7687 1.6433 -0.3411 0.0803 0.1150 539 HIS B ND1 11305 C CD2 . HIS B 539 ? 1.6851 1.6716 1.7255 -0.2598 0.0700 0.1246 539 HIS B CD2 11306 C CE1 . HIS B 539 ? 1.7452 1.8050 1.7059 -0.3473 0.0772 0.1259 539 HIS B CE1 11307 N NE2 . HIS B 539 ? 1.7644 1.7725 1.7836 -0.2959 0.0701 0.1318 539 HIS B NE2 11308 N N . GLY B 540 ? 1.6520 1.6376 1.5729 -0.3187 0.0346 0.1315 540 GLY B N 11309 C CA . GLY B 540 ? 1.7654 1.7534 1.6855 -0.3016 0.0364 0.1182 540 GLY B CA 11310 C C . GLY B 540 ? 1.9180 1.8763 1.7932 -0.3470 0.0041 0.1464 540 GLY B C 11311 O O . GLY B 540 ? 1.7836 1.6861 1.6384 -0.3809 -0.0327 0.1833 540 GLY B O 11312 N N . GLN B 541 ? 2.2077 2.1974 2.0643 -0.3465 0.0131 0.1277 541 GLN B N 11313 C CA . GLN B 541 ? 2.3318 2.2943 2.1434 -0.3862 -0.0167 0.1507 541 GLN B CA 11314 C C . GLN B 541 ? 2.2945 2.1815 2.1507 -0.3538 -0.0470 0.1675 541 GLN B C 11315 O O . GLN B 541 ? 2.3305 2.2093 2.2457 -0.3015 -0.0310 0.1484 541 GLN B O 11316 C CB . GLN B 541 ? 2.3301 2.3661 2.1081 -0.3984 0.0069 0.1179 541 GLN B CB 11317 C CG . GLN B 541 ? 2.3749 2.5038 2.1090 -0.4402 0.0353 0.0905 541 GLN B CG 11318 C CD . GLN B 541 ? 2.3593 2.5719 2.0740 -0.4456 0.0576 0.0458 541 GLN B CD 11319 O OE1 . GLN B 541 ? 2.3167 2.5207 2.0627 -0.3998 0.0590 0.0282 541 GLN B OE1 11320 N NE2 . GLN B 541 ? 2.3747 2.6719 2.0368 -0.5051 0.0753 0.0235 541 GLN B NE2 11321 N N . CYS B 542 ? 2.2923 2.1231 2.1164 -0.3879 -0.0928 0.2000 542 CYS B N 11322 C CA . CYS B 542 ? 2.1800 1.9475 2.0522 -0.3584 -0.1269 0.2080 542 CYS B CA 11323 C C . CYS B 542 ? 2.1531 1.9290 2.0050 -0.3625 -0.1311 0.2003 542 CYS B C 11324 O O . CYS B 542 ? 2.1660 1.9284 1.9507 -0.4101 -0.1584 0.2207 542 CYS B O 11325 C CB . CYS B 542 ? 2.2772 1.9633 2.1392 -0.3818 -0.1886 0.2440 542 CYS B CB 11326 S SG . CYS B 542 ? 2.0356 1.6537 1.9654 -0.3451 -0.2404 0.2420 542 CYS B SG 11327 N N . SER B 543 ? 2.1000 1.8932 2.0037 -0.3165 -0.1052 0.1714 543 SER B N 11328 C CA . SER B 543 ? 2.0230 1.8228 1.9165 -0.3147 -0.1079 0.1608 543 SER B CA 11329 C C . SER B 543 ? 1.8650 1.6207 1.8258 -0.2791 -0.1258 0.1533 543 SER B C 11330 O O . SER B 543 ? 1.7377 1.4993 1.7508 -0.2414 -0.0973 0.1297 543 SER B O 11331 C CB . SER B 543 ? 1.9903 1.8569 1.8726 -0.2983 -0.0608 0.1258 543 SER B CB 11332 O OG . SER B 543 ? 2.0599 1.9301 1.9377 -0.2925 -0.0634 0.1133 543 SER B OG 11333 N N . CYS B 544 ? 1.8386 1.5503 1.7929 -0.2951 -0.1744 0.1703 544 CYS B N 11334 C CA . CYS B 544 ? 1.8315 1.5106 1.8538 -0.2656 -0.1976 0.1559 544 CYS B CA 11335 C C . CYS B 544 ? 1.8362 1.5050 1.9388 -0.2322 -0.1903 0.1391 544 CYS B C 11336 O O . CYS B 544 ? 1.8496 1.5367 2.0015 -0.2043 -0.1569 0.1093 544 CYS B O 11337 C CB . CYS B 544 ? 1.8378 1.5467 1.8684 -0.2493 -0.1676 0.1297 544 CYS B CB 11338 S SG . CYS B 544 ? 2.2972 1.9769 2.3989 -0.2268 -0.1980 0.1083 544 CYS B SG 11339 N N . GLY B 545 ? 1.8792 1.5166 1.9889 -0.2396 -0.2224 0.1571 545 GLY B N 11340 C CA . GLY B 545 ? 1.8437 1.4740 2.0326 -0.2104 -0.2220 0.1385 545 GLY B CA 11341 C C . GLY B 545 ? 1.7901 1.4590 1.9921 -0.1940 -0.1615 0.1237 545 GLY B C 11342 O O . GLY B 545 ? 1.7261 1.3945 1.9888 -0.1736 -0.1548 0.1066 545 GLY B O 11343 N N . ASP B 546 ? 1.8194 1.5221 1.9650 -0.2020 -0.1211 0.1261 546 ASP B N 11344 C CA . ASP B 546 ? 1.7950 1.5259 1.9443 -0.1832 -0.0707 0.1098 546 ASP B CA 11345 C C . ASP B 546 ? 1.7716 1.5316 1.8626 -0.2010 -0.0557 0.1237 546 ASP B C 11346 O O . ASP B 546 ? 1.8853 1.6580 1.9209 -0.2322 -0.0694 0.1392 546 ASP B O 11347 C CB . ASP B 546 ? 1.8061 1.5497 1.9530 -0.1657 -0.0369 0.0839 546 ASP B CB 11348 C CG . ASP B 546 ? 1.8852 1.6098 2.0895 -0.1549 -0.0449 0.0638 546 ASP B CG 11349 O OD1 . ASP B 546 ? 1.8965 1.6103 2.1604 -0.1477 -0.0575 0.0551 546 ASP B OD1 11350 O OD2 . ASP B 546 ? 1.8728 1.5988 2.0659 -0.1545 -0.0387 0.0518 546 ASP B OD2 11351 N N . CYS B 547 ? 1.6528 1.4274 1.7551 -0.1845 -0.0269 0.1143 547 CYS B N 11352 C CA . CYS B 547 ? 1.6314 1.4416 1.6905 -0.1998 -0.0125 0.1199 547 CYS B CA 11353 C C . CYS B 547 ? 1.6743 1.5287 1.7050 -0.1831 0.0240 0.0917 547 CYS B C 11354 O O . CYS B 547 ? 1.5257 1.3693 1.5754 -0.1498 0.0456 0.0706 547 CYS B O 11355 C CB . CYS B 547 ? 1.6322 1.4324 1.7217 -0.1918 -0.0105 0.1256 547 CYS B CB 11356 S SG . CYS B 547 ? 2.1783 1.9317 2.2796 -0.2197 -0.0644 0.1593 547 CYS B SG 11357 N N . LEU B 548 ? 1.7392 1.6417 1.7209 -0.2090 0.0272 0.0882 548 LEU B N 11358 C CA . LEU B 548 ? 1.8090 1.7657 1.7700 -0.1915 0.0551 0.0520 548 LEU B CA 11359 C C . LEU B 548 ? 1.7629 1.7643 1.7147 -0.2008 0.0687 0.0444 548 LEU B C 11360 O O . LEU B 548 ? 1.7588 1.7973 1.6768 -0.2461 0.0639 0.0545 548 LEU B O 11361 C CB . LEU B 548 ? 1.9286 1.9283 1.8504 -0.2132 0.0533 0.0385 548 LEU B CB 11362 C CG . LEU B 548 ? 1.9226 1.8839 1.8498 -0.2077 0.0387 0.0449 548 LEU B CG 11363 C CD1 . LEU B 548 ? 1.9907 2.0037 1.8771 -0.2299 0.0392 0.0276 548 LEU B CD1 11364 C CD2 . LEU B 548 ? 1.8497 1.7705 1.8081 -0.1608 0.0505 0.0265 548 LEU B CD2 11365 N N . CYS B 549 ? 1.6708 1.6668 1.6466 -0.1620 0.0853 0.0254 549 CYS B N 11366 C CA . CYS B 549 ? 1.5630 1.5909 1.5419 -0.1657 0.0960 0.0203 549 CYS B CA 11367 C C . CYS B 549 ? 1.5783 1.6959 1.5311 -0.1755 0.1118 -0.0189 549 CYS B C 11368 O O . CYS B 549 ? 1.6366 1.7874 1.5807 -0.1545 0.1174 -0.0563 549 CYS B O 11369 C CB . CYS B 549 ? 1.5548 1.5432 1.5651 -0.1209 0.1060 0.0116 549 CYS B CB 11370 S SG . CYS B 549 ? 1.7457 1.6509 1.7975 -0.1141 0.0941 0.0436 549 CYS B SG 11371 N N . ASP B 550 ? 1.6077 1.7671 1.5505 -0.2086 0.1175 -0.0149 550 ASP B N 11372 C CA . ASP B 550 ? 1.5506 1.8098 1.4786 -0.2208 0.1365 -0.0614 550 ASP B CA 11373 C C . ASP B 550 ? 1.5169 1.7912 1.4758 -0.1585 0.1468 -0.1068 550 ASP B C 11374 O O . ASP B 550 ? 1.4855 1.6871 1.4671 -0.1185 0.1418 -0.0918 550 ASP B O 11375 C CB . ASP B 550 ? 1.5388 1.8311 1.4447 -0.2783 0.1405 -0.0436 550 ASP B CB 11376 C CG . ASP B 550 ? 1.6513 1.9400 1.5028 -0.3508 0.1266 -0.0098 550 ASP B CG 11377 O OD1 . ASP B 550 ? 1.5971 1.7992 1.4416 -0.3666 0.0991 0.0432 550 ASP B OD1 11378 O OD2 . ASP B 550 ? 1.8164 2.1892 1.6306 -0.3932 0.1404 -0.0402 550 ASP B OD2 11379 N N . SER B 551 ? 1.5241 1.8932 1.4816 -0.1522 0.1585 -0.1666 551 SER B N 11380 C CA . SER B 551 ? 1.4905 1.8758 1.4740 -0.0908 0.1588 -0.2180 551 SER B CA 11381 C C . SER B 551 ? 1.5189 1.8635 1.5216 -0.0758 0.1616 -0.1968 551 SER B C 11382 O O . SER B 551 ? 1.6808 2.0435 1.6810 -0.1202 0.1704 -0.1694 551 SER B O 11383 C CB . SER B 551 ? 1.4370 1.9525 1.4262 -0.0954 0.1694 -0.2930 551 SER B CB 11384 O OG . SER B 551 ? 1.5375 2.0989 1.5117 -0.1091 0.1677 -0.3190 551 SER B OG 11385 N N . ASP B 552 ? 1.5068 1.7882 1.5214 -0.0163 0.1513 -0.2079 552 ASP B N 11386 C CA . ASP B 552 ? 1.4892 1.7261 1.5197 0.0037 0.1530 -0.1919 552 ASP B CA 11387 C C . ASP B 552 ? 1.4134 1.5804 1.4496 -0.0260 0.1548 -0.1256 552 ASP B C 11388 O O . ASP B 552 ? 1.4042 1.5624 1.4569 -0.0323 0.1600 -0.1080 552 ASP B O 11389 C CB . ASP B 552 ? 1.4632 1.7928 1.5096 -0.0054 0.1649 -0.2283 552 ASP B CB 11390 C CG . ASP B 552 ? 1.5811 2.0001 1.6342 0.0234 0.1608 -0.3070 552 ASP B CG 11391 O OD1 . ASP B 552 ? 1.7343 2.1095 1.7843 0.0811 0.1393 -0.3377 552 ASP B OD1 11392 O OD2 . ASP B 552 ? 1.5686 2.1011 1.6281 -0.0142 0.1765 -0.3419 552 ASP B OD2 11393 N N . TRP B 553 ? 1.4446 1.5650 1.4719 -0.0417 0.1475 -0.0945 553 TRP B N 11394 C CA . TRP B 553 ? 1.4681 1.5198 1.5105 -0.0594 0.1422 -0.0435 553 TRP B CA 11395 C C . TRP B 553 ? 1.4871 1.4690 1.5270 -0.0403 0.1353 -0.0344 553 TRP B C 11396 O O . TRP B 553 ? 1.5901 1.5809 1.6106 -0.0384 0.1308 -0.0483 553 TRP B O 11397 C CB . TRP B 553 ? 1.6482 1.7209 1.6835 -0.1158 0.1347 -0.0106 553 TRP B CB 11398 C CG . TRP B 553 ? 1.5456 1.6697 1.5771 -0.1470 0.1409 -0.0100 553 TRP B CG 11399 C CD1 . TRP B 553 ? 1.4680 1.6755 1.4720 -0.1834 0.1503 -0.0328 553 TRP B CD1 11400 C CD2 . TRP B 553 ? 1.5180 1.6168 1.5726 -0.1494 0.1394 0.0110 553 TRP B CD2 11401 N NE1 . TRP B 553 ? 1.4554 1.6877 1.4595 -0.2115 0.1554 -0.0253 553 TRP B NE1 11402 C CE2 . TRP B 553 ? 1.4388 1.6021 1.4746 -0.1884 0.1470 0.0030 553 TRP B CE2 11403 C CE3 . TRP B 553 ? 1.5371 1.5700 1.6269 -0.1254 0.1335 0.0317 553 TRP B CE3 11404 C CZ2 . TRP B 553 ? 1.4214 1.5770 1.4709 -0.2014 0.1462 0.0191 553 TRP B CZ2 11405 C CZ3 . TRP B 553 ? 1.4514 1.4817 1.5597 -0.1351 0.1323 0.0450 553 TRP B CZ3 11406 C CH2 . TRP B 553 ? 1.4367 1.5238 1.5241 -0.1713 0.1373 0.0405 553 TRP B CH2 11407 N N . THR B 554 ? 1.5022 1.4198 1.5618 -0.0293 0.1359 -0.0152 554 THR B N 11408 C CA . THR B 554 ? 1.5171 1.3721 1.5745 -0.0207 0.1334 -0.0090 554 THR B CA 11409 C C . THR B 554 ? 1.4609 1.2813 1.5584 -0.0380 0.1311 0.0186 554 THR B C 11410 O O . THR B 554 ? 1.4291 1.2653 1.5538 -0.0519 0.1271 0.0342 554 THR B O 11411 C CB . THR B 554 ? 1.4553 1.2598 1.4838 0.0154 0.1375 -0.0328 554 THR B CB 11412 O OG1 . THR B 554 ? 1.4262 1.2183 1.4640 0.0276 0.1447 -0.0334 554 THR B OG1 11413 C CG2 . THR B 554 ? 1.4735 1.3043 1.4674 0.0407 0.1289 -0.0690 554 THR B CG2 11414 N N . GLY B 555 ? 1.4329 1.2085 1.5358 -0.0375 0.1318 0.0193 555 GLY B N 11415 C CA . GLY B 555 ? 1.3624 1.1165 1.5136 -0.0512 0.1287 0.0315 555 GLY B CA 11416 C C . GLY B 555 ? 1.3694 1.1307 1.5447 -0.0725 0.1074 0.0456 555 GLY B C 11417 O O . GLY B 555 ? 1.4173 1.2029 1.5677 -0.0841 0.0953 0.0540 555 GLY B O 11418 N N . TYR B 556 ? 1.3399 1.0828 1.5641 -0.0787 0.1013 0.0435 556 TYR B N 11419 C CA . TYR B 556 ? 1.3538 1.0966 1.6082 -0.0937 0.0736 0.0513 556 TYR B CA 11420 C C . TYR B 556 ? 1.3891 1.1431 1.6466 -0.1093 0.0413 0.0767 556 TYR B C 11421 O O . TYR B 556 ? 1.3616 1.1150 1.6001 -0.1262 0.0165 0.0912 556 TYR B O 11422 C CB . TYR B 556 ? 1.4301 1.1621 1.7491 -0.0938 0.0720 0.0314 556 TYR B CB 11423 C CG . TYR B 556 ? 1.6925 1.4233 2.0500 -0.1027 0.0400 0.0288 556 TYR B CG 11424 C CD1 . TYR B 556 ? 1.7114 1.4402 2.1168 -0.1055 -0.0025 0.0363 556 TYR B CD1 11425 C CD2 . TYR B 556 ? 1.6815 1.4073 2.0261 -0.1069 0.0469 0.0168 556 TYR B CD2 11426 C CE1 . TYR B 556 ? 1.6240 1.3450 2.0641 -0.1094 -0.0406 0.0303 556 TYR B CE1 11427 C CE2 . TYR B 556 ? 1.6437 1.3701 2.0262 -0.1128 0.0153 0.0110 556 TYR B CE2 11428 C CZ . TYR B 556 ? 1.6428 1.3666 2.0736 -0.1125 -0.0299 0.0169 556 TYR B CZ 11429 O OH . TYR B 556 ? 1.6902 1.4080 2.1579 -0.1143 -0.0699 0.0078 556 TYR B OH 11430 N N . TYR B 557 ? 1.5777 1.3361 1.8514 -0.1074 0.0405 0.0828 557 TYR B N 11431 C CA . TYR B 557 ? 1.5942 1.3512 1.8621 -0.1279 0.0079 0.1083 557 TYR B CA 11432 C C . TYR B 557 ? 1.6089 1.3977 1.8154 -0.1423 0.0228 0.1185 557 TYR B C 11433 O O . TYR B 557 ? 1.7141 1.5038 1.8973 -0.1702 0.0011 0.1402 557 TYR B O 11434 C CB . TYR B 557 ? 1.5982 1.3426 1.9217 -0.1200 -0.0054 0.1063 557 TYR B CB 11435 C CG . TYR B 557 ? 1.5713 1.2990 1.9683 -0.1082 -0.0258 0.0858 557 TYR B CG 11436 C CD1 . TYR B 557 ? 1.5515 1.2514 1.9778 -0.1161 -0.0810 0.0942 557 TYR B CD1 11437 C CD2 . TYR B 557 ? 1.4760 1.2155 1.9105 -0.0917 0.0073 0.0534 557 TYR B CD2 11438 C CE1 . TYR B 557 ? 1.5224 1.2184 2.0277 -0.1010 -0.1035 0.0637 557 TYR B CE1 11439 C CE2 . TYR B 557 ? 1.4409 1.1823 1.9492 -0.0855 -0.0074 0.0237 557 TYR B CE2 11440 C CZ . TYR B 557 ? 1.4963 1.2218 2.0472 -0.0866 -0.0631 0.0254 557 TYR B CZ 11441 O OH . TYR B 557 ? 1.3847 1.1227 2.0205 -0.0760 -0.0815 -0.0154 557 TYR B OH 11442 N N . CYS B 558 ? 1.6543 1.4678 1.8334 -0.1251 0.0568 0.0984 558 CYS B N 11443 C CA . CYS B 558 ? 1.5915 1.4509 1.7242 -0.1316 0.0733 0.0915 558 CYS B CA 11444 C C . CYS B 558 ? 1.5676 1.4444 1.7067 -0.1357 0.0781 0.0953 558 CYS B C 11445 O O . CYS B 558 ? 1.6283 1.5499 1.7336 -0.1563 0.0840 0.0927 558 CYS B O 11446 C CB . CYS B 558 ? 1.5903 1.4739 1.6788 -0.1684 0.0581 0.1035 558 CYS B CB 11447 S SG . CYS B 558 ? 1.7118 1.5963 1.7802 -0.1611 0.0606 0.0898 558 CYS B SG 11448 N N . ASN B 559 ? 1.5166 1.3647 1.7004 -0.1193 0.0772 0.0972 559 ASN B N 11449 C CA . ASN B 559 ? 1.5117 1.3734 1.7060 -0.1202 0.0816 0.0997 559 ASN B CA 11450 C C . ASN B 559 ? 1.5573 1.4328 1.7518 -0.0862 0.1123 0.0734 559 ASN B C 11451 O O . ASN B 559 ? 1.6912 1.5788 1.8977 -0.0817 0.1187 0.0714 559 ASN B O 11452 C CB . ASN B 559 ? 1.5266 1.3506 1.7714 -0.1243 0.0555 0.1155 559 ASN B CB 11453 C CG . ASN B 559 ? 1.5768 1.3743 1.8721 -0.0984 0.0609 0.0988 559 ASN B CG 11454 O OD1 . ASN B 559 ? 1.5943 1.3889 1.8778 -0.0854 0.0798 0.0834 559 ASN B OD1 11455 N ND2 . ASN B 559 ? 1.6669 1.4467 2.0182 -0.0943 0.0435 0.0980 559 ASN B ND2 11456 N N . CYS B 560 ? 1.4642 1.3298 1.6402 -0.0628 0.1269 0.0535 560 CYS B N 11457 C CA . CYS B 560 ? 1.3925 1.2510 1.5546 -0.0301 0.1461 0.0291 560 CYS B CA 11458 C C . CYS B 560 ? 1.4795 1.3820 1.6031 -0.0171 0.1517 0.0032 560 CYS B C 11459 O O . CYS B 560 ? 1.5371 1.4527 1.6358 -0.0179 0.1481 -0.0075 560 CYS B O 11460 C CB . CYS B 560 ? 1.3347 1.1391 1.4904 -0.0146 0.1531 0.0206 560 CYS B CB 11461 S SG . CYS B 560 ? 1.9892 1.7560 2.1050 0.0198 0.1666 -0.0047 560 CYS B SG 11462 N N . THR B 561 ? 1.5699 1.5004 1.6942 -0.0034 0.1590 -0.0127 561 THR B N 11463 C CA . THR B 561 ? 1.6044 1.5891 1.7048 0.0138 0.1617 -0.0502 561 THR B CA 11464 C C . THR B 561 ? 1.5124 1.4559 1.5837 0.0588 0.1568 -0.0806 561 THR B C 11465 O O . THR B 561 ? 1.5083 1.3784 1.5702 0.0735 0.1566 -0.0710 561 THR B O 11466 C CB . THR B 561 ? 1.6462 1.6812 1.7617 0.0127 0.1690 -0.0625 561 THR B CB 11467 O OG1 . THR B 561 ? 1.7997 1.7855 1.9290 0.0361 0.1720 -0.0567 561 THR B OG1 11468 C CG2 . THR B 561 ? 1.7463 1.8180 1.8740 -0.0379 0.1687 -0.0350 561 THR B CG2 11469 N N . THR B 562 ? 1.4119 1.4016 1.4651 0.0772 0.1501 -0.1207 562 THR B N 11470 C CA . THR B 562 ? 1.4463 1.3939 1.4676 0.1253 0.1337 -0.1570 562 THR B CA 11471 C C . THR B 562 ? 1.4180 1.3963 1.4456 0.1566 0.1286 -0.1930 562 THR B C 11472 O O . THR B 562 ? 1.3425 1.2846 1.3426 0.2020 0.1060 -0.2294 562 THR B O 11473 C CB . THR B 562 ? 1.5797 1.5579 1.5837 0.1364 0.1206 -0.1904 562 THR B CB 11474 O OG1 . THR B 562 ? 1.5147 1.6081 1.5411 0.1266 0.1263 -0.2273 562 THR B OG1 11475 C CG2 . THR B 562 ? 1.5767 1.5317 1.5765 0.1039 0.1255 -0.1557 562 THR B CG2 11476 N N . ARG B 563 ? 1.3249 1.3645 1.3861 0.1319 0.1451 -0.1839 563 ARG B N 11477 C CA . ARG B 563 ? 1.3279 1.4185 1.4039 0.1552 0.1437 -0.2220 563 ARG B CA 11478 C C . ARG B 563 ? 1.3571 1.3669 1.4192 0.1881 0.1352 -0.2160 563 ARG B C 11479 O O . ARG B 563 ? 1.3358 1.2949 1.4038 0.1687 0.1471 -0.1728 563 ARG B O 11480 C CB . ARG B 563 ? 1.2729 1.4479 1.3818 0.1093 0.1649 -0.2101 563 ARG B CB 11481 C CG . ARG B 563 ? 1.3511 1.6096 1.4604 0.0662 0.1737 -0.2186 563 ARG B CG 11482 C CD . ARG B 563 ? 1.4013 1.7125 1.5238 0.0088 0.1904 -0.1937 563 ARG B CD 11483 N NE . ARG B 563 ? 1.3833 1.7382 1.5271 0.0205 0.1974 -0.2202 563 ARG B NE 11484 C CZ . ARG B 563 ? 1.3261 1.7214 1.4791 -0.0253 0.2104 -0.2037 563 ARG B CZ 11485 N NH1 . ARG B 563 ? 1.3560 1.7439 1.4922 -0.0859 0.2126 -0.1589 563 ARG B NH1 11486 N NH2 . ARG B 563 ? 1.2054 1.6417 1.3796 -0.0111 0.2169 -0.2320 563 ARG B NH2 11487 N N . THR B 564 ? 1.6094 1.6069 1.6521 0.2381 0.1110 -0.2637 564 THR B N 11488 C CA . THR B 564 ? 1.4980 1.4170 1.5163 0.2688 0.0980 -0.2625 564 THR B CA 11489 C C . THR B 564 ? 1.5339 1.5224 1.5876 0.2804 0.1028 -0.2896 564 THR B C 11490 O O . THR B 564 ? 1.5090 1.4420 1.5461 0.3037 0.0932 -0.2892 564 THR B O 11491 C CB . THR B 564 ? 1.3699 1.2021 1.3295 0.3195 0.0564 -0.2955 564 THR B CB 11492 O OG1 . THR B 564 ? 1.3212 1.2314 1.2994 0.3564 0.0327 -0.3630 564 THR B OG1 11493 C CG2 . THR B 564 ? 1.3893 1.1418 1.3068 0.3044 0.0521 -0.2670 564 THR B CG2 11494 N N . ASP B 565 ? 1.6308 1.7407 1.7284 0.2591 0.1184 -0.3141 565 ASP B N 11495 C CA . ASP B 565 ? 1.5947 1.7863 1.7270 0.2693 0.1225 -0.3528 565 ASP B CA 11496 C C . ASP B 565 ? 1.3786 1.5522 1.5287 0.2439 0.1436 -0.3088 565 ASP B C 11497 O O . ASP B 565 ? 1.4196 1.6120 1.5841 0.2664 0.1398 -0.3332 565 ASP B O 11498 C CB . ASP B 565 ? 1.5336 1.8658 1.7014 0.2393 0.1387 -0.3928 565 ASP B CB 11499 C CG . ASP B 565 ? 1.5857 1.9411 1.7566 0.1701 0.1664 -0.3404 565 ASP B CG 11500 O OD1 . ASP B 565 ? 1.4914 1.8664 1.6789 0.1290 0.1862 -0.3073 565 ASP B OD1 11501 O OD2 . ASP B 565 ? 1.7894 2.1380 1.9432 0.1576 0.1637 -0.3332 565 ASP B OD2 11502 N N . THR B 566 ? 1.3723 1.5105 1.5250 0.2000 0.1620 -0.2486 566 THR B N 11503 C CA . THR B 566 ? 1.2730 1.3895 1.4473 0.1783 0.1770 -0.2098 566 THR B CA 11504 C C . THR B 566 ? 1.2638 1.2742 1.4111 0.2057 0.1683 -0.1925 566 THR B C 11505 O O . THR B 566 ? 1.2196 1.2090 1.3843 0.1970 0.1783 -0.1701 566 THR B O 11506 C CB . THR B 566 ? 1.2500 1.3709 1.4429 0.1227 0.1918 -0.1592 566 THR B CB 11507 O OG1 . THR B 566 ? 1.3273 1.3877 1.4985 0.1187 0.1864 -0.1357 566 THR B OG1 11508 C CG2 . THR B 566 ? 1.2674 1.4859 1.4723 0.0821 0.2010 -0.1714 566 THR B CG2 11509 N N . CYS B 567 ? 1.2879 1.2296 1.3876 0.2345 0.1487 -0.2041 567 CYS B N 11510 C CA . CYS B 567 ? 1.3214 1.1548 1.3748 0.2534 0.1381 -0.1922 567 CYS B CA 11511 C C . CYS B 567 ? 1.5848 1.3977 1.6093 0.3033 0.1103 -0.2352 567 CYS B C 11512 O O . CYS B 567 ? 1.6229 1.3418 1.5970 0.3185 0.0967 -0.2287 567 CYS B O 11513 C CB . CYS B 567 ? 1.3529 1.1044 1.3556 0.2498 0.1282 -0.1778 567 CYS B CB 11514 S SG . CYS B 567 ? 1.4340 1.1976 1.4692 0.1965 0.1543 -0.1320 567 CYS B SG 11515 N N . MET B 568 ? 1.8132 1.7161 1.8677 0.3259 0.1004 -0.2829 568 MET B N 11516 C CA . MET B 568 ? 1.7496 1.6439 1.7853 0.3813 0.0653 -0.3369 568 MET B CA 11517 C C . MET B 568 ? 1.7060 1.6181 1.7654 0.3858 0.0744 -0.3377 568 MET B C 11518 O O . MET B 568 ? 1.6753 1.6810 1.7932 0.3565 0.1040 -0.3325 568 MET B O 11519 C CB . MET B 568 ? 1.6376 1.6398 1.7081 0.4040 0.0517 -0.4013 568 MET B CB 11520 C CG . MET B 568 ? 1.7298 1.6947 1.7686 0.4726 -0.0028 -0.4655 568 MET B CG 11521 S SD . MET B 568 ? 2.1108 1.9111 2.0549 0.4947 -0.0448 -0.4468 568 MET B SD 11522 C CE . MET B 568 ? 1.7722 1.6412 1.7444 0.4552 -0.0178 -0.4340 568 MET B CE 11523 N N . SER B 569 ? 1.8393 1.6545 1.8457 0.4196 0.0463 -0.3434 569 SER B N 11524 C CA . SER B 569 ? 1.7259 1.5481 1.7480 0.4275 0.0515 -0.3456 569 SER B CA 11525 C C . SER B 569 ? 1.7675 1.6639 1.8190 0.4759 0.0244 -0.4154 569 SER B C 11526 O O . SER B 569 ? 1.6464 1.5983 1.7105 0.4906 0.0038 -0.4554 569 SER B O 11527 C CB . SER B 569 ? 1.7414 1.4230 1.6853 0.4334 0.0351 -0.3183 569 SER B CB 11528 O OG . SER B 569 ? 1.7735 1.4637 1.7332 0.4386 0.0420 -0.3193 569 SER B OG 11529 N N . SER B 570 ? 1.6940 1.5993 1.7583 0.4788 0.0254 -0.4152 570 SER B N 11530 C CA . SER B 570 ? 1.5885 1.5731 1.6838 0.4929 0.0029 -0.4568 570 SER B CA 11531 C C . SER B 570 ? 1.6955 1.5999 1.7302 0.5306 -0.0595 -0.4770 570 SER B C 11532 O O . SER B 570 ? 1.7698 1.7395 1.8294 0.5507 -0.0915 -0.5219 570 SER B O 11533 C CB . SER B 570 ? 1.6123 1.6392 1.7457 0.4773 0.0278 -0.4460 570 SER B CB 11534 O OG . SER B 570 ? 1.7611 1.6758 1.8444 0.4816 0.0232 -0.4111 570 SER B OG 11535 N N . ASN B 571 ? 1.7326 1.4954 1.6853 0.5376 -0.0799 -0.4458 571 ASN B N 11536 C CA . ASN B 571 ? 1.7957 1.4648 1.6758 0.5697 -0.1452 -0.4594 571 ASN B CA 11537 C C . ASN B 571 ? 1.7638 1.4091 1.6168 0.5878 -0.1818 -0.4795 571 ASN B C 11538 O O . ASN B 571 ? 1.9316 1.5092 1.7292 0.6180 -0.2448 -0.4971 571 ASN B O 11539 C CB . ASN B 571 ? 1.9219 1.4416 1.7106 0.5604 -0.1528 -0.4162 571 ASN B CB 11540 C CG . ASN B 571 ? 2.0666 1.4966 1.8046 0.5337 -0.1282 -0.3766 571 ASN B CG 11541 O OD1 . ASN B 571 ? 2.2397 1.5717 1.9014 0.5390 -0.1639 -0.3708 571 ASN B OD1 11542 N ND2 . ASN B 571 ? 1.8816 1.3432 1.6602 0.5039 -0.0696 -0.3497 571 ASN B ND2 11543 N N . GLY B 572 ? 1.6711 1.3719 1.5621 0.5700 -0.1456 -0.4778 572 GLY B N 11544 C CA . GLY B 572 ? 1.8356 1.5293 1.7115 0.5847 -0.1746 -0.4993 572 GLY B CA 11545 C C . GLY B 572 ? 2.0167 1.5840 1.8185 0.5697 -0.1701 -0.4574 572 GLY B C 11546 O O . GLY B 572 ? 1.9558 1.5304 1.7572 0.5720 -0.1758 -0.4680 572 GLY B O 11547 N N . LEU B 573 ? 2.0717 1.5245 1.8088 0.5507 -0.1595 -0.4119 573 LEU B N 11548 C CA . LEU B 573 ? 2.0989 1.4290 1.7601 0.5255 -0.1498 -0.3703 573 LEU B CA 11549 C C . LEU B 573 ? 1.8674 1.2553 1.5830 0.4892 -0.0831 -0.3421 573 LEU B C 11550 O O . LEU B 573 ? 1.5690 1.0260 1.3411 0.4646 -0.0426 -0.3236 573 LEU B O 11551 C CB . LEU B 573 ? 2.0211 1.2030 1.5785 0.5092 -0.1676 -0.3350 573 LEU B CB 11552 C CG . LEU B 573 ? 1.9590 1.0347 1.4220 0.5315 -0.2421 -0.3443 573 LEU B CG 11553 C CD1 . LEU B 573 ? 1.9611 0.9029 1.3198 0.5070 -0.2525 -0.3096 573 LEU B CD1 11554 C CD2 . LEU B 573 ? 1.9989 1.0097 1.4102 0.5304 -0.2692 -0.3420 573 LEU B CD2 11555 N N . LEU B 574 ? 1.9131 1.2981 1.6247 0.4651 -0.0717 -0.3243 574 LEU B N 11556 C CA . LEU B 574 ? 1.9079 1.3654 1.6791 0.4081 -0.0127 -0.2806 574 LEU B CA 11557 C C . LEU B 574 ? 1.8423 1.2216 1.5759 0.3623 0.0152 -0.2294 574 LEU B C 11558 O O . LEU B 574 ? 2.0652 1.3167 1.7052 0.3526 -0.0039 -0.2143 574 LEU B O 11559 C CB . LEU B 574 ? 1.8987 1.3698 1.6723 0.3964 -0.0118 -0.2784 574 LEU B CB 11560 C CG . LEU B 574 ? 1.9484 1.2877 1.6314 0.3857 -0.0330 -0.2582 574 LEU B CG 11561 C CD1 . LEU B 574 ? 1.9249 1.3161 1.6411 0.3633 -0.0150 -0.2493 574 LEU B CD1 11562 C CD2 . LEU B 574 ? 1.9321 1.1636 1.5299 0.4390 -0.1011 -0.2969 574 LEU B CD2 11563 N N . CYS B 575 ? 1.5277 0.9856 1.3328 0.3321 0.0583 -0.2076 575 CYS B N 11564 C CA . CYS B 575 ? 1.4428 0.8577 1.2367 0.2893 0.0887 -0.1702 575 CYS B CA 11565 C C . CYS B 575 ? 1.5641 0.8746 1.2748 0.3007 0.0665 -0.1743 575 CYS B C 11566 O O . CYS B 575 ? 1.6219 0.8653 1.2873 0.2612 0.0843 -0.1492 575 CYS B O 11567 C CB . CYS B 575 ? 1.4644 0.8361 1.2354 0.2462 0.1069 -0.1409 575 CYS B CB 11568 S SG . CYS B 575 ? 1.8984 1.3803 1.7612 0.2249 0.1324 -0.1290 575 CYS B SG 11569 N N . SER B 576 ? 1.7489 1.0486 1.4386 0.3526 0.0262 -0.2103 576 SER B N 11570 C CA . SER B 576 ? 1.9272 1.1301 1.5385 0.3702 -0.0034 -0.2180 576 SER B CA 11571 C C . SER B 576 ? 2.1214 1.1606 1.5987 0.3465 -0.0274 -0.1981 576 SER B C 11572 O O . SER B 576 ? 2.1436 1.0925 1.5440 0.3337 -0.0374 -0.1890 576 SER B O 11573 C CB . SER B 576 ? 1.4903 0.7430 1.1511 0.3456 0.0356 -0.2018 576 SER B CB 11574 O OG . SER B 576 ? 1.3964 0.7917 1.1732 0.3554 0.0599 -0.2138 576 SER B OG 11575 N N . GLY B 577 ? 2.0292 1.0274 1.4721 0.3351 -0.0363 -0.1909 577 GLY B N 11576 C CA . GLY B 577 ? 2.0487 0.8929 1.3610 0.2999 -0.0543 -0.1691 577 GLY B CA 11577 C C . GLY B 577 ? 2.0808 0.9167 1.3834 0.2263 0.0011 -0.1334 577 GLY B C 11578 O O . GLY B 577 ? 2.1727 0.8895 1.3642 0.1805 -0.0028 -0.1152 577 GLY B O 11579 N N . ARG B 578 ? 1.8004 0.7642 1.2188 0.2127 0.0507 -0.1278 578 ARG B N 11580 C CA . ARG B 578 ? 1.7177 0.6985 1.1519 0.1504 0.1020 -0.1066 578 ARG B CA 11581 C C . ARG B 578 ? 1.7000 0.7547 1.2090 0.1126 0.1430 -0.0934 578 ARG B C 11582 O O . ARG B 578 ? 1.8492 0.9419 1.3966 0.0652 0.1852 -0.0856 578 ARG B O 11583 C CB . ARG B 578 ? 1.7731 0.8387 1.2871 0.1600 0.1244 -0.1124 578 ARG B CB 11584 C CG . ARG B 578 ? 1.9116 0.8955 1.3432 0.1823 0.0916 -0.1231 578 ARG B CG 11585 C CD . ARG B 578 ? 1.5934 0.6704 1.1129 0.1936 0.1149 -0.1304 578 ARG B CD 11586 N NE . ARG B 578 ? 1.6630 0.6557 1.0969 0.2053 0.0878 -0.1385 578 ARG B NE 11587 C CZ . ARG B 578 ? 1.6493 0.6991 1.1365 0.2340 0.0882 -0.1524 578 ARG B CZ 11588 N NH1 . ARG B 578 ? 1.5585 0.7466 1.1801 0.2504 0.1145 -0.1587 578 ARG B NH1 11589 N NH2 . ARG B 578 ? 1.8538 0.8159 1.2529 0.2435 0.0597 -0.1594 578 ARG B NH2 11590 N N . GLY B 579 ? 1.7386 0.8194 1.2735 0.1350 0.1287 -0.0961 579 GLY B N 11591 C CA . GLY B 579 ? 1.8741 1.0187 1.4757 0.1027 0.1609 -0.0844 579 GLY B CA 11592 C C . GLY B 579 ? 1.7358 0.8977 1.3501 0.1269 0.1411 -0.0881 579 GLY B C 11593 O O . GLY B 579 ? 1.5715 0.7257 1.1687 0.1756 0.1041 -0.1061 579 GLY B O 11594 N N . LYS B 580 ? 1.7607 0.9509 1.4087 0.0926 0.1650 -0.0763 580 LYS B N 11595 C CA . LYS B 580 ? 1.6096 0.8273 1.2785 0.1081 0.1524 -0.0780 580 LYS B CA 11596 C C . LYS B 580 ? 1.5380 0.8817 1.3170 0.1302 0.1604 -0.0810 580 LYS B C 11597 O O . LYS B 580 ? 1.5035 0.9138 1.3530 0.1213 0.1821 -0.0752 580 LYS B O 11598 C CB . LYS B 580 ? 1.6216 0.8210 1.2834 0.0606 0.1742 -0.0655 580 LYS B CB 11599 C CG . LYS B 580 ? 1.8688 0.9355 1.4037 0.0321 0.1615 -0.0632 580 LYS B CG 11600 C CD . LYS B 580 ? 2.1070 1.0954 1.5633 0.0729 0.1113 -0.0730 580 LYS B CD 11601 C CE . LYS B 580 ? 2.1304 0.9734 1.4517 0.0377 0.0936 -0.0665 580 LYS B CE 11602 N NZ . LYS B 580 ? 2.1206 0.9792 1.4573 -0.0153 0.1270 -0.0564 580 LYS B NZ 11603 N N . CYS B 581 ? 1.5760 0.9493 1.3640 0.1551 0.1414 -0.0915 581 CYS B N 11604 C CA . CYS B 581 ? 1.3711 0.8591 1.2471 0.1633 0.1497 -0.0937 581 CYS B CA 11605 C C . CYS B 581 ? 1.3594 0.8812 1.2702 0.1366 0.1616 -0.0784 581 CYS B C 11606 O O . CYS B 581 ? 1.5197 1.0116 1.3927 0.1429 0.1467 -0.0851 581 CYS B O 11607 C CB . CYS B 581 ? 1.3741 0.8955 1.2436 0.2089 0.1214 -0.1265 581 CYS B CB 11608 S SG . CYS B 581 ? 1.4338 1.0969 1.3925 0.2036 0.1346 -0.1327 581 CYS B SG 11609 N N . GLU B 582 ? 1.3255 0.9059 1.3082 0.1089 0.1835 -0.0598 582 GLU B N 11610 C CA . GLU B 582 ? 1.3415 0.9512 1.3605 0.0838 0.1897 -0.0455 582 GLU B CA 11611 C C . GLU B 582 ? 1.3002 0.9958 1.3868 0.0761 0.1903 -0.0357 582 GLU B C 11612 O O . GLU B 582 ? 1.3357 1.0604 1.4692 0.0669 0.1975 -0.0270 582 GLU B O 11613 C CB . GLU B 582 ? 1.4015 0.9807 1.4352 0.0502 0.2078 -0.0352 582 GLU B CB 11614 C CG . GLU B 582 ? 1.5044 0.9930 1.4579 0.0407 0.2105 -0.0424 582 GLU B CG 11615 C CD . GLU B 582 ? 1.7277 1.2062 1.7022 -0.0010 0.2344 -0.0418 582 GLU B CD 11616 O OE1 . GLU B 582 ? 1.5720 1.1147 1.6321 -0.0140 0.2431 -0.0390 582 GLU B OE1 11617 O OE2 . GLU B 582 ? 2.0733 1.4789 1.9765 -0.0230 0.2419 -0.0477 582 GLU B OE2 11618 N N . CYS B 583 ? 1.3684 1.0994 1.4528 0.0764 0.1807 -0.0379 583 CYS B N 11619 C CA . CYS B 583 ? 1.3260 1.1272 1.4537 0.0572 0.1786 -0.0259 583 CYS B CA 11620 C C . CYS B 583 ? 1.3066 1.1579 1.4534 0.0628 0.1807 -0.0331 583 CYS B C 11621 O O . CYS B 583 ? 1.3754 1.2587 1.5604 0.0389 0.1807 -0.0148 583 CYS B O 11622 C CB . CYS B 583 ? 1.3501 1.1462 1.5242 0.0274 0.1791 -0.0003 583 CYS B CB 11623 S SG . CYS B 583 ? 1.3968 1.1486 1.5589 0.0161 0.1783 0.0030 583 CYS B SG 11624 N N . GLY B 584 ? 1.3250 1.1787 1.4430 0.0946 0.1779 -0.0621 584 GLY B N 11625 C CA . GLY B 584 ? 1.3262 1.2350 1.4624 0.1021 0.1804 -0.0773 584 GLY B CA 11626 C C . GLY B 584 ? 1.3146 1.1966 1.4704 0.1060 0.1879 -0.0674 584 GLY B C 11627 O O . GLY B 584 ? 1.3359 1.2561 1.5063 0.1149 0.1901 -0.0807 584 GLY B O 11628 N N . SER B 585 ? 1.2648 1.0877 1.4229 0.0971 0.1932 -0.0486 585 SER B N 11629 C CA . SER B 585 ? 1.2116 1.0114 1.3889 0.0975 0.2023 -0.0436 585 SER B CA 11630 C C . SER B 585 ? 1.1852 0.9078 1.3087 0.1111 0.2042 -0.0532 585 SER B C 11631 O O . SER B 585 ? 1.2168 0.8939 1.3061 0.1037 0.2028 -0.0508 585 SER B O 11632 C CB . SER B 585 ? 1.3317 1.1400 1.5670 0.0673 0.2066 -0.0205 585 SER B CB 11633 O OG . SER B 585 ? 1.5249 1.3854 1.7951 0.0497 0.1976 -0.0073 585 SER B OG 11634 N N . CYS B 586 ? 1.2784 0.9812 1.3871 0.1270 0.2060 -0.0637 586 CYS B N 11635 C CA . CYS B 586 ? 1.2193 0.8371 1.2622 0.1308 0.2056 -0.0697 586 CYS B CA 11636 C C . CYS B 586 ? 1.2079 0.8072 1.2731 0.0948 0.2275 -0.0579 586 CYS B C 11637 O O . CYS B 586 ? 1.2340 0.8853 1.3728 0.0807 0.2385 -0.0513 586 CYS B O 11638 C CB . CYS B 586 ? 1.2262 0.8255 1.2392 0.1596 0.1959 -0.0867 586 CYS B CB 11639 S SG . CYS B 586 ? 1.5657 1.1887 1.5536 0.2084 0.1651 -0.1190 586 CYS B SG 11640 N N . VAL B 587 ? 1.2625 0.7879 1.2629 0.0779 0.2313 -0.0595 587 VAL B N 11641 C CA . VAL B 587 ? 1.3105 0.8218 1.3223 0.0394 0.2558 -0.0605 587 VAL B CA 11642 C C . VAL B 587 ? 1.3957 0.8232 1.3145 0.0321 0.2568 -0.0681 587 VAL B C 11643 O O . VAL B 587 ? 1.4145 0.7564 1.2358 0.0324 0.2411 -0.0681 587 VAL B O 11644 C CB . VAL B 587 ? 1.3593 0.8649 1.3777 0.0083 0.2652 -0.0584 587 VAL B CB 11645 C CG1 . VAL B 587 ? 1.7105 1.1556 1.6492 0.0190 0.2463 -0.0549 587 VAL B CG1 11646 C CG2 . VAL B 587 ? 1.6086 1.0940 1.6185 -0.0363 0.2921 -0.0715 587 VAL B CG2 11647 N N . CYS B 588 ? 1.3871 0.8331 1.3306 0.0246 0.2714 -0.0745 588 CYS B N 11648 C CA . CYS B 588 ? 1.5232 0.8912 1.3752 0.0195 0.2684 -0.0804 588 CYS B CA 11649 C C . CYS B 588 ? 1.5175 0.8142 1.2904 -0.0354 0.2867 -0.0842 588 CYS B C 11650 O O . CYS B 588 ? 1.4916 0.8368 1.3197 -0.0761 0.3179 -0.0946 588 CYS B O 11651 C CB . CYS B 588 ? 1.5188 0.9370 1.4266 0.0266 0.2800 -0.0876 588 CYS B CB 11652 S SG . CYS B 588 ? 1.5135 1.0151 1.5053 0.0793 0.2618 -0.0852 588 CYS B SG 11653 N N . ILE B 589 ? 1.5592 0.7395 1.2004 -0.0383 0.2640 -0.0799 589 ILE B N 11654 C CA . ILE B 589 ? 1.6989 0.7936 1.2376 -0.1004 0.2791 -0.0817 589 ILE B CA 11655 C C . ILE B 589 ? 1.8798 0.9363 1.3618 -0.1284 0.2910 -0.0888 589 ILE B C 11656 O O . ILE B 589 ? 1.9395 1.0319 1.4416 -0.1845 0.3311 -0.1035 589 ILE B O 11657 C CB . ILE B 589 ? 2.0553 1.0217 1.4614 -0.0994 0.2426 -0.0708 589 ILE B CB 11658 C CG1 . ILE B 589 ? 2.1883 1.0847 1.5313 -0.0377 0.1893 -0.0688 589 ILE B CG1 11659 C CG2 . ILE B 589 ? 1.8470 0.8543 1.3053 -0.0922 0.2427 -0.0673 589 ILE B CG2 11660 C CD1 . ILE B 589 ? 2.1850 0.9098 1.3515 -0.0558 0.1507 -0.0629 589 ILE B CD1 11661 N N . GLN B 590 ? 1.8818 0.8696 1.2943 -0.0900 0.2549 -0.0836 590 GLN B N 11662 C CA . GLN B 590 ? 2.0250 0.9601 1.3661 -0.1133 0.2584 -0.0881 590 GLN B CA 11663 C C . GLN B 590 ? 1.7905 0.8464 1.2488 -0.1336 0.3045 -0.1042 590 GLN B C 11664 O O . GLN B 590 ? 1.6615 0.8261 1.2516 -0.0920 0.3090 -0.1080 590 GLN B O 11665 C CB . GLN B 590 ? 2.0698 0.9454 1.3611 -0.0498 0.2077 -0.0857 590 GLN B CB 11666 C CG . GLN B 590 ? 2.2098 0.9851 1.3818 -0.0744 0.1959 -0.0860 590 GLN B CG 11667 C CD . GLN B 590 ? 2.3454 1.0709 1.4824 -0.0045 0.1410 -0.0904 590 GLN B CD 11668 O OE1 . GLN B 590 ? 2.2849 1.1050 1.5318 0.0573 0.1321 -0.1004 590 GLN B OE1 11669 N NE2 . GLN B 590 ? 2.4328 1.0073 1.4117 -0.0170 0.1013 -0.0857 590 GLN B NE2 11670 N N . PRO B 591 ? 1.8806 0.9161 1.2871 -0.2017 0.3371 -0.1167 591 PRO B N 11671 C CA . PRO B 591 ? 1.8307 0.9845 1.3501 -0.2278 0.3818 -0.1423 591 PRO B CA 11672 C C . PRO B 591 ? 1.7548 0.9650 1.3492 -0.1755 0.3721 -0.1445 591 PRO B C 11673 O O . PRO B 591 ? 1.8726 1.0061 1.3849 -0.1472 0.3413 -0.1332 591 PRO B O 11674 C CB . PRO B 591 ? 2.1430 1.2346 1.5475 -0.3129 0.4103 -0.1569 591 PRO B CB 11675 C CG . PRO B 591 ? 2.4382 1.3582 1.6562 -0.3165 0.3678 -0.1302 591 PRO B CG 11676 C CD . PRO B 591 ? 2.2039 1.0976 1.4321 -0.2625 0.3306 -0.1103 591 PRO B CD 11677 N N . GLY B 592 ? 1.6794 1.0188 1.4278 -0.1623 0.3939 -0.1609 592 GLY B N 11678 C CA . GLY B 592 ? 1.6792 1.0791 1.5063 -0.1211 0.3886 -0.1653 592 GLY B CA 11679 C C . GLY B 592 ? 1.5785 0.9740 1.4234 -0.0510 0.3501 -0.1443 592 GLY B C 11680 O O . GLY B 592 ? 1.8379 1.2494 1.7025 -0.0171 0.3386 -0.1456 592 GLY B O 11681 N N . SER B 593 ? 1.4012 0.7819 1.2408 -0.0316 0.3316 -0.1295 593 SER B N 11682 C CA . SER B 593 ? 1.3492 0.7455 1.2153 0.0287 0.2993 -0.1182 593 SER B CA 11683 C C . SER B 593 ? 1.3355 0.8269 1.3210 0.0404 0.3045 -0.1135 593 SER B C 11684 O O . SER B 593 ? 1.3251 0.8371 1.3421 0.0103 0.3201 -0.1143 593 SER B O 11685 C CB . SER B 593 ? 1.4351 0.7293 1.1854 0.0478 0.2643 -0.1092 593 SER B CB 11686 O OG . SER B 593 ? 1.4650 0.7420 1.2003 0.0241 0.2689 -0.1017 593 SER B OG 11687 N N . TYR B 594 ? 1.1848 0.7314 1.2313 0.0809 0.2894 -0.1104 594 TYR B N 11688 C CA . TYR B 594 ? 1.1121 0.7377 1.2564 0.0880 0.2883 -0.1024 594 TYR B CA 11689 C C . TYR B 594 ? 1.1225 0.7833 1.2848 0.1278 0.2673 -0.0999 594 TYR B C 11690 O O . TYR B 594 ? 1.3160 0.9448 1.4232 0.1558 0.2520 -0.1095 594 TYR B O 11691 C CB . TYR B 594 ? 1.0863 0.7785 1.3314 0.0680 0.3060 -0.1097 594 TYR B CB 11692 C CG . TYR B 594 ? 1.0217 0.7281 1.2822 0.0750 0.3126 -0.1218 594 TYR B CG 11693 C CD1 . TYR B 594 ? 1.0115 0.7601 1.3157 0.1043 0.2999 -0.1185 594 TYR B CD1 11694 C CD2 . TYR B 594 ? 1.0639 0.7439 1.2916 0.0472 0.3332 -0.1386 594 TYR B CD2 11695 C CE1 . TYR B 594 ? 0.9414 0.7035 1.2610 0.1115 0.3055 -0.1304 594 TYR B CE1 11696 C CE2 . TYR B 594 ? 1.0822 0.7763 1.3226 0.0528 0.3394 -0.1507 594 TYR B CE2 11697 C CZ . TYR B 594 ? 0.9825 0.7168 1.2714 0.0879 0.3245 -0.1460 594 TYR B CZ 11698 O OH . TYR B 594 ? 0.9629 0.7120 1.2662 0.0941 0.3303 -0.1590 594 TYR B OH 11699 N N . GLY B 595 ? 1.0126 0.7393 1.2501 0.1272 0.2647 -0.0906 595 GLY B N 11700 C CA . GLY B 595 ? 0.9876 0.7584 1.2397 0.1517 0.2496 -0.0915 595 GLY B CA 11701 C C . GLY B 595 ? 1.1570 0.9294 1.3888 0.1525 0.2391 -0.0857 595 GLY B C 11702 O O . GLY B 595 ? 1.2709 0.9964 1.4646 0.1411 0.2405 -0.0810 595 GLY B O 11703 N N . ASP B 596 ? 1.1910 1.0207 1.4463 0.1612 0.2303 -0.0885 596 ASP B N 11704 C CA . ASP B 596 ? 1.1883 1.0330 1.4287 0.1588 0.2218 -0.0868 596 ASP B CA 11705 C C . ASP B 596 ? 1.3339 1.1230 1.4995 0.1854 0.2082 -0.1049 596 ASP B C 11706 O O . ASP B 596 ? 1.5923 1.3495 1.7299 0.1775 0.2048 -0.0980 596 ASP B O 11707 C CB . ASP B 596 ? 1.2423 1.1660 1.5128 0.1568 0.2179 -0.0947 596 ASP B CB 11708 C CG . ASP B 596 ? 1.4012 1.3637 1.7319 0.1281 0.2232 -0.0749 596 ASP B CG 11709 O OD1 . ASP B 596 ? 1.3186 1.2550 1.6791 0.1092 0.2248 -0.0540 596 ASP B OD1 11710 O OD2 . ASP B 596 ? 1.4761 1.4951 1.8243 0.1237 0.2231 -0.0842 596 ASP B OD2 11711 N N . THR B 597 ? 1.4372 1.2107 1.5696 0.2186 0.1956 -0.1299 597 THR B N 11712 C CA . THR B 597 ? 1.3706 1.0757 1.4252 0.2503 0.1701 -0.1512 597 THR B CA 11713 C C . THR B 597 ? 1.5587 1.1597 1.5454 0.2457 0.1674 -0.1424 597 THR B C 11714 O O . THR B 597 ? 1.7360 1.2565 1.6419 0.2705 0.1386 -0.1577 597 THR B O 11715 C CB . THR B 597 ? 1.4351 1.1791 1.4880 0.2939 0.1470 -0.1926 597 THR B CB 11716 O OG1 . THR B 597 ? 1.6703 1.4249 1.7411 0.3022 0.1519 -0.1980 597 THR B OG1 11717 C CG2 . THR B 597 ? 1.3421 1.1958 1.4525 0.2880 0.1535 -0.2076 597 THR B CG2 11718 N N . CYS B 598 ? 1.4051 1.0074 1.4219 0.2123 0.1942 -0.1218 598 CYS B N 11719 C CA . CYS B 598 ? 1.3021 0.8228 1.2592 0.1958 0.1998 -0.1172 598 CYS B CA 11720 C C . CYS B 598 ? 1.3421 0.8315 1.2581 0.2281 0.1800 -0.1360 598 CYS B C 11721 O O . CYS B 598 ? 1.4289 0.8206 1.2531 0.2258 0.1661 -0.1378 598 CYS B O 11722 C CB . CYS B 598 ? 1.3442 0.7686 1.2108 0.1791 0.1906 -0.1108 598 CYS B CB 11723 S SG . CYS B 598 ? 1.4485 0.8984 1.3570 0.1339 0.2173 -0.0917 598 CYS B SG 11724 N N . GLU B 599 ? 1.3040 0.8739 1.2833 0.2541 0.1773 -0.1506 599 GLU B N 11725 C CA . GLU B 599 ? 1.5114 1.0667 1.4644 0.2914 0.1551 -0.1753 599 GLU B CA 11726 C C . GLU B 599 ? 1.4528 0.9889 1.4050 0.2737 0.1726 -0.1673 599 GLU B C 11727 O O . GLU B 599 ? 1.6455 1.1324 1.5454 0.2976 0.1517 -0.1829 599 GLU B O 11728 C CB . GLU B 599 ? 1.5148 1.1766 1.5407 0.3189 0.1506 -0.1997 599 GLU B CB 11729 C CG . GLU B 599 ? 1.3689 1.1229 1.4889 0.2923 0.1823 -0.1853 599 GLU B CG 11730 C CD . GLU B 599 ? 1.4611 1.2510 1.6277 0.2540 0.2027 -0.1575 599 GLU B CD 11731 O OE1 . GLU B 599 ? 1.5751 1.4197 1.8099 0.2297 0.2204 -0.1425 599 GLU B OE1 11732 O OE2 . GLU B 599 ? 1.4990 1.2570 1.6321 0.2491 0.1963 -0.1515 599 GLU B OE2 11733 N N . LYS B 600 ? 1.2678 0.8431 1.2793 0.2335 0.2072 -0.1473 600 LYS B N 11734 C CA . LYS B 600 ? 1.2235 0.8018 1.2532 0.2155 0.2268 -0.1462 600 LYS B CA 11735 C C . LYS B 600 ? 1.2796 0.7814 1.2425 0.1745 0.2416 -0.1381 600 LYS B C 11736 O O . LYS B 600 ? 1.4183 0.9314 1.4049 0.1398 0.2617 -0.1282 600 LYS B O 11737 C CB . LYS B 600 ? 1.0876 0.7645 1.2342 0.2000 0.2499 -0.1391 600 LYS B CB 11738 C CG . LYS B 600 ? 1.0377 0.7908 1.2413 0.2266 0.2394 -0.1470 600 LYS B CG 11739 C CD . LYS B 600 ? 1.3213 1.1486 1.6223 0.2078 0.2550 -0.1380 600 LYS B CD 11740 C CE . LYS B 600 ? 1.6038 1.4476 1.9500 0.1765 0.2630 -0.1184 600 LYS B CE 11741 N NZ . LYS B 600 ? 1.2674 1.1662 1.7023 0.1604 0.2663 -0.1110 600 LYS B NZ 11742 N N . CYS B 601 ? 1.3528 0.7760 1.2270 0.1755 0.2301 -0.1452 601 CYS B N 11743 C CA . CYS B 601 ? 1.3841 0.7322 1.1785 0.1255 0.2465 -0.1406 601 CYS B CA 11744 C C . CYS B 601 ? 1.4011 0.7176 1.1530 0.1187 0.2488 -0.1502 601 CYS B C 11745 O O . CYS B 601 ? 1.7542 0.9631 1.3845 0.1238 0.2198 -0.1510 601 CYS B O 11746 C CB . CYS B 601 ? 1.4744 0.7058 1.1424 0.1189 0.2196 -0.1329 601 CYS B CB 11747 S SG . CYS B 601 ? 1.8153 0.9570 1.3762 0.0389 0.2452 -0.1260 601 CYS B SG 11748 N N . PRO B 602 ? 1.3237 0.7280 1.1724 0.1072 0.2787 -0.1584 602 PRO B N 11749 C CA . PRO B 602 ? 1.4007 0.7928 1.2261 0.1027 0.2836 -0.1702 602 PRO B CA 11750 C C . PRO B 602 ? 1.4984 0.8056 1.2110 0.0442 0.2985 -0.1723 602 PRO B C 11751 O O . PRO B 602 ? 1.5258 0.7780 1.1644 0.0398 0.2896 -0.1781 602 PRO B O 11752 C CB . PRO B 602 ? 1.2240 0.7388 1.1948 0.0997 0.3129 -0.1800 602 PRO B CB 11753 C CG . PRO B 602 ? 1.3170 0.8803 1.3555 0.0762 0.3307 -0.1748 602 PRO B CG 11754 C CD . PRO B 602 ? 1.4679 0.9815 1.4510 0.0962 0.3054 -0.1587 602 PRO B CD 11755 N N . THR B 603 ? 1.5417 0.8398 1.2381 -0.0050 0.3216 -0.1694 603 THR B N 11756 C CA . THR B 603 ? 1.6859 0.9139 1.2741 -0.0754 0.3428 -0.1752 603 THR B CA 11757 C C . THR B 603 ? 2.0099 1.0852 1.4273 -0.0881 0.3080 -0.1563 603 THR B C 11758 O O . THR B 603 ? 2.3038 1.2984 1.6032 -0.1554 0.3209 -0.1563 603 THR B O 11759 C CB . THR B 603 ? 1.7672 1.0789 1.4350 -0.1304 0.3902 -0.1926 603 THR B CB 11760 O OG1 . THR B 603 ? 2.1017 1.3367 1.6443 -0.2068 0.4101 -0.1987 603 THR B OG1 11761 C CG2 . THR B 603 ? 1.8905 1.2443 1.6331 -0.1066 0.3837 -0.1817 603 THR B CG2 11762 N N . CYS B 604 ? 1.9561 0.9923 1.3589 -0.0265 0.2621 -0.1438 604 CYS B N 11763 C CA . CYS B 604 ? 1.9389 0.8228 1.1842 -0.0246 0.2151 -0.1297 604 CYS B CA 11764 C C . CYS B 604 ? 1.9992 0.7643 1.1124 -0.0180 0.1760 -0.1300 604 CYS B C 11765 O O . CYS B 604 ? 1.9230 0.7393 1.0893 0.0112 0.1768 -0.1417 604 CYS B O 11766 C CB . CYS B 604 ? 1.8913 0.7871 1.1786 0.0434 0.1767 -0.1267 604 CYS B CB 11767 S SG . CYS B 604 ? 2.9543 1.8785 2.2775 0.0178 0.1965 -0.1161 604 CYS B SG 11768 N N . PRO B 605 ? 2.3922 0.9900 1.3264 -0.0469 0.1377 -0.1167 605 PRO B N 11769 C CA . PRO B 605 ? 2.4355 0.8925 1.2190 -0.0452 0.0896 -0.1144 605 PRO B CA 11770 C C . PRO B 605 ? 2.3160 0.7691 1.1310 0.0527 0.0295 -0.1284 605 PRO B C 11771 O O . PRO B 605 ? 2.1613 0.6762 1.0664 0.1146 0.0111 -0.1375 605 PRO B O 11772 C CB . PRO B 605 ? 2.4630 0.7365 1.0543 -0.0921 0.0519 -0.0949 605 PRO B CB 11773 C CG . PRO B 605 ? 2.4066 0.7469 1.0490 -0.1495 0.1076 -0.0897 605 PRO B CG 11774 C CD . PRO B 605 ? 2.2852 0.8085 1.1393 -0.0914 0.1369 -0.1023 605 PRO B CD 11775 N N . ASP B 606 ? 2.3278 0.7122 1.0671 0.0632 -0.0006 -0.1343 606 ASP B N 11776 C CA . ASP B 606 ? 2.3120 0.6997 1.0839 0.1544 -0.0574 -0.1563 606 ASP B CA 11777 C C . ASP B 606 ? 2.6472 0.9052 1.3229 0.2084 -0.1420 -0.1626 606 ASP B C 11778 O O . ASP B 606 ? 2.8271 0.9651 1.3767 0.1667 -0.1653 -0.1408 606 ASP B O 11779 C CB . ASP B 606 ? 2.3994 0.7332 1.1017 0.1481 -0.0721 -0.1618 606 ASP B CB 11780 C CG . ASP B 606 ? 2.6996 0.8408 1.1831 0.0746 -0.0967 -0.1397 606 ASP B CG 11781 O OD1 . ASP B 606 ? 2.8750 0.8775 1.2301 0.0573 -0.1384 -0.1245 606 ASP B OD1 11782 O OD2 . ASP B 606 ? 2.7836 0.9086 1.2173 0.0299 -0.0752 -0.1379 606 ASP B OD2 11783 N N . ALA B 607 ? 1.4968 0.8272 2.0229 0.4351 0.0496 0.2754 607 ALA B N 11784 C CA . ALA B 607 ? 1.3889 0.7454 1.9190 0.4172 0.0417 0.2732 607 ALA B CA 11785 C C . ALA B 607 ? 1.7793 1.1578 2.3051 0.4134 0.0297 0.2402 607 ALA B C 11786 O O . ALA B 607 ? 1.5225 0.9400 2.0369 0.4041 0.0179 0.2389 607 ALA B O 11787 C CB . ALA B 607 ? 1.4076 0.7257 1.9500 0.3953 0.0518 0.2682 607 ALA B CB 11788 N N . CYS B 608 ? 1.7242 1.0796 2.2473 0.4159 0.0319 0.2107 608 CYS B N 11789 C CA . CYS B 608 ? 1.5807 0.9504 2.0963 0.4123 0.0205 0.1802 608 CYS B CA 11790 C C . CYS B 608 ? 1.3778 0.7931 1.8835 0.4248 0.0101 0.1934 608 CYS B C 11791 O O . CYS B 608 ? 1.2597 0.6975 1.7443 0.4135 -0.0033 0.1760 608 CYS B O 11792 C CB . CYS B 608 ? 1.6543 0.9923 2.1694 0.4142 0.0273 0.1515 608 CYS B CB 11793 S SG . CYS B 608 ? 2.1033 1.3867 2.6308 0.3951 0.0412 0.1307 608 CYS B SG 11794 N N . THR B 609 ? 1.4513 0.8857 1.9597 0.4434 0.0148 0.2208 609 THR B N 11795 C CA . THR B 609 ? 1.5066 0.9937 2.0048 0.4530 0.0067 0.2353 609 THR B CA 11796 C C . THR B 609 ? 1.5140 1.0392 1.9948 0.4381 -0.0010 0.2559 609 THR B C 11797 O O . THR B 609 ? 1.2301 0.7953 1.6847 0.4275 -0.0113 0.2515 609 THR B O 11798 C CB . THR B 609 ? 1.3047 0.8067 1.8181 0.4816 0.0143 0.2576 609 THR B CB 11799 O OG1 . THR B 609 ? 1.3299 0.8008 1.8483 0.4894 0.0215 0.2305 609 THR B OG1 11800 C CG2 . THR B 609 ? 1.4328 1.0018 1.9323 0.4867 0.0057 0.2687 609 THR B CG2 11801 N N . PHE B 610 ? 1.5601 1.0698 2.0523 0.4344 0.0055 0.2771 610 PHE B N 11802 C CA . PHE B 610 ? 1.5287 1.0735 2.0062 0.4184 0.0009 0.2969 610 PHE B CA 11803 C C . PHE B 610 ? 1.5060 1.0507 1.9668 0.3935 -0.0068 0.2689 610 PHE B C 11804 O O . PHE B 610 ? 1.3964 0.9759 1.8316 0.3827 -0.0160 0.2639 610 PHE B O 11805 C CB . PHE B 610 ? 1.7103 1.2359 2.2028 0.4199 0.0110 0.3278 610 PHE B CB 11806 C CG . PHE B 610 ? 1.8363 1.4032 2.3258 0.4321 0.0104 0.3698 610 PHE B CG 11807 C CD1 . PHE B 610 ? 1.9384 1.4972 2.4449 0.4628 0.0157 0.3934 610 PHE B CD1 11808 C CD2 . PHE B 610 ? 1.8412 1.4570 2.3111 0.4135 0.0045 0.3852 610 PHE B CD2 11809 C CE1 . PHE B 610 ? 1.9892 1.5923 2.4941 0.4765 0.0130 0.4337 610 PHE B CE1 11810 C CE2 . PHE B 610 ? 1.9934 1.6535 2.4594 0.4226 0.0029 0.4243 610 PHE B CE2 11811 C CZ . PHE B 610 ? 2.0582 1.7142 2.5423 0.4550 0.0060 0.4497 610 PHE B CZ 11812 N N . LYS B 611 ? 1.5391 1.0444 2.0138 0.3847 -0.0025 0.2500 611 LYS B N 11813 C CA . LYS B 611 ? 1.3452 0.8535 1.8107 0.3646 -0.0093 0.2251 611 LYS B CA 11814 C C . LYS B 611 ? 1.2710 0.7846 1.7150 0.3633 -0.0229 0.1953 611 LYS B C 11815 O O . LYS B 611 ? 1.5495 1.0702 1.9806 0.3513 -0.0310 0.1772 611 LYS B O 11816 C CB . LYS B 611 ? 1.3139 0.7853 1.8018 0.3555 -0.0012 0.2098 611 LYS B CB 11817 C CG . LYS B 611 ? 1.6275 1.0828 2.1304 0.3525 0.0133 0.2383 611 LYS B CG 11818 C CD . LYS B 611 ? 1.7264 1.2206 2.2175 0.3416 0.0126 0.2642 611 LYS B CD 11819 C CE . LYS B 611 ? 1.7649 1.2811 2.2506 0.3198 0.0078 0.2413 611 LYS B CE 11820 N NZ . LYS B 611 ? 1.7770 1.3336 2.2485 0.3072 0.0082 0.2631 611 LYS B NZ 11821 N N . LYS B 612 ? 1.3415 0.8506 1.7797 0.3759 -0.0251 0.1900 612 LYS B N 11822 C CA . LYS B 612 ? 1.3287 0.8395 1.7396 0.3720 -0.0380 0.1642 612 LYS B CA 11823 C C . LYS B 612 ? 1.3617 0.9088 1.7383 0.3638 -0.0452 0.1739 612 LYS B C 11824 O O . LYS B 612 ? 1.1945 0.7390 1.5401 0.3554 -0.0563 0.1547 612 LYS B O 11825 C CB . LYS B 612 ? 1.1971 0.6948 1.6099 0.3837 -0.0365 0.1536 612 LYS B CB 11826 C CG . LYS B 612 ? 1.1929 0.7255 1.5911 0.3914 -0.0362 0.1698 612 LYS B CG 11827 C CD . LYS B 612 ? 1.5172 1.0392 1.9186 0.4013 -0.0338 0.1535 612 LYS B CD 11828 C CE . LYS B 612 ? 1.6965 1.2617 2.0923 0.4116 -0.0309 0.1702 612 LYS B CE 11829 N NZ . LYS B 612 ? 1.5155 1.0737 1.9209 0.4231 -0.0255 0.1535 612 LYS B NZ 11830 N N . GLU B 613 ? 1.4903 1.0694 1.8699 0.3654 -0.0387 0.2044 613 GLU B N 11831 C CA . GLU B 613 ? 1.4772 1.0949 1.8241 0.3532 -0.0429 0.2146 613 GLU B CA 11832 C C . GLU B 613 ? 1.3308 0.9446 1.6646 0.3373 -0.0465 0.2037 613 GLU B C 11833 O O . GLU B 613 ? 1.3758 1.0011 1.6735 0.3251 -0.0522 0.1959 613 GLU B O 11834 C CB . GLU B 613 ? 1.5207 1.1790 1.8769 0.3580 -0.0355 0.2511 613 GLU B CB 11835 C CG . GLU B 613 ? 1.6778 1.3843 1.9993 0.3470 -0.0390 0.2602 613 GLU B CG 11836 C CD . GLU B 613 ? 1.8577 1.5707 2.1627 0.3520 -0.0431 0.2461 613 GLU B CD 11837 O OE1 . GLU B 613 ? 1.7764 1.5071 2.1032 0.3702 -0.0389 0.2590 613 GLU B OE1 11838 O OE2 . GLU B 613 ? 1.9860 1.6853 2.2551 0.3379 -0.0503 0.2218 613 GLU B OE2 11839 N N . CYS B 614 ? 1.3496 0.9460 1.7120 0.3369 -0.0417 0.2014 614 CYS B N 11840 C CA . CYS B 614 ? 1.3268 0.9245 1.6847 0.3240 -0.0436 0.1884 614 CYS B CA 11841 C C . CYS B 614 ? 1.3289 0.9010 1.6728 0.3255 -0.0556 0.1542 614 CYS B C 11842 O O . CYS B 614 ? 1.5099 1.0860 1.8289 0.3185 -0.0615 0.1421 614 CYS B O 11843 C CB . CYS B 614 ? 1.4360 1.0285 1.8290 0.3202 -0.0337 0.1955 614 CYS B CB 11844 S SG . CYS B 614 ? 2.0992 1.7227 2.4991 0.3133 -0.0214 0.2380 614 CYS B SG 11845 N N . VAL B 615 ? 1.2271 0.7717 1.5852 0.3352 -0.0593 0.1387 615 VAL B N 11846 C CA . VAL B 615 ? 1.2727 0.7947 1.6189 0.3375 -0.0726 0.1079 615 VAL B CA 11847 C C . VAL B 615 ? 1.3595 0.8758 1.6575 0.3363 -0.0836 0.1012 615 VAL B C 11848 O O . VAL B 615 ? 1.5354 1.0348 1.8107 0.3370 -0.0959 0.0809 615 VAL B O 11849 C CB . VAL B 615 ? 1.1629 0.6596 1.5333 0.3444 -0.0733 0.0926 615 VAL B CB 11850 C CG1 . VAL B 615 ? 1.3504 0.8461 1.7622 0.3422 -0.0590 0.1017 615 VAL B CG1 11851 C CG2 . VAL B 615 ? 1.1682 0.6554 1.5255 0.3504 -0.0734 0.0957 615 VAL B CG2 11852 N N . GLU B 616 ? 1.3290 0.8596 1.6100 0.3342 -0.0793 0.1182 616 GLU B N 11853 C CA . GLU B 616 ? 1.4140 0.9423 1.6441 0.3268 -0.0869 0.1133 616 GLU B CA 11854 C C . GLU B 616 ? 1.5304 1.0620 1.7288 0.3162 -0.0891 0.1113 616 GLU B C 11855 O O . GLU B 616 ? 1.5740 1.0767 1.7410 0.3160 -0.1002 0.0919 616 GLU B O 11856 C CB . GLU B 616 ? 1.5437 1.1010 1.7664 0.3243 -0.0794 0.1327 616 GLU B CB 11857 C CG . GLU B 616 ? 1.6285 1.1763 1.8653 0.3342 -0.0792 0.1262 616 GLU B CG 11858 C CD . GLU B 616 ? 1.6455 1.1624 1.8452 0.3291 -0.0916 0.1007 616 GLU B CD 11859 O OE1 . GLU B 616 ? 1.5413 1.0672 1.7007 0.3184 -0.0936 0.0996 616 GLU B OE1 11860 O OE2 . GLU B 616 ? 1.5351 1.0207 1.7439 0.3341 -0.0994 0.0819 616 GLU B OE2 11861 N N . CYS B 617 ? 1.4702 1.0353 1.6753 0.3079 -0.0784 0.1316 617 CYS B N 11862 C CA . CYS B 617 ? 1.6165 1.1878 1.7899 0.2949 -0.0770 0.1296 617 CYS B CA 11863 C C . CYS B 617 ? 1.3552 0.9086 1.5422 0.3008 -0.0810 0.1104 617 CYS B C 11864 O O . CYS B 617 ? 1.3875 0.9213 1.5398 0.2981 -0.0862 0.0952 617 CYS B O 11865 C CB . CYS B 617 ? 1.8030 1.4207 1.9831 0.2824 -0.0640 0.1565 617 CYS B CB 11866 S SG . CYS B 617 ? 1.6033 1.2411 1.8368 0.2843 -0.0540 0.1692 617 CYS B SG 11867 N N . LYS B 618 ? 1.2610 0.8211 1.4974 0.3086 -0.0777 0.1102 618 LYS B N 11868 C CA . LYS B 618 ? 1.2622 0.8199 1.5178 0.3125 -0.0795 0.0919 618 LYS B CA 11869 C C . LYS B 618 ? 1.2650 0.7890 1.5101 0.3269 -0.0959 0.0644 618 LYS B C 11870 O O . LYS B 618 ? 1.3875 0.9048 1.6240 0.3324 -0.1015 0.0468 618 LYS B O 11871 C CB . LYS B 618 ? 1.1854 0.7621 1.4935 0.3118 -0.0700 0.0988 618 LYS B CB 11872 C CG . LYS B 618 ? 1.2478 0.8578 1.5649 0.2973 -0.0549 0.1261 618 LYS B CG 11873 C CD . LYS B 618 ? 1.2657 0.8959 1.5673 0.2851 -0.0498 0.1208 618 LYS B CD 11874 C CE . LYS B 618 ? 1.5078 1.1413 1.8378 0.2883 -0.0502 0.0963 618 LYS B CE 11875 N NZ . LYS B 618 ? 1.5450 1.2006 1.8633 0.2771 -0.0429 0.0885 618 LYS B NZ 11876 N N . LYS B 619 ? 1.1796 0.6836 1.4249 0.3339 -0.1038 0.0606 619 LYS B N 11877 C CA . LYS B 619 ? 1.1890 0.6634 1.4233 0.3464 -0.1210 0.0368 619 LYS B CA 11878 C C . LYS B 619 ? 1.3978 0.8399 1.5723 0.3448 -0.1314 0.0341 619 LYS B C 11879 O O . LYS B 619 ? 1.9656 1.3828 2.1060 0.3506 -0.1419 0.0213 619 LYS B O 11880 C CB . LYS B 619 ? 1.1886 0.6602 1.4589 0.3516 -0.1232 0.0301 619 LYS B CB 11881 C CG . LYS B 619 ? 1.1681 0.6650 1.4923 0.3495 -0.1122 0.0303 619 LYS B CG 11882 C CD . LYS B 619 ? 1.3189 0.8295 1.6575 0.3553 -0.1181 0.0109 619 LYS B CD 11883 C CE . LYS B 619 ? 1.5227 1.0204 1.8641 0.3681 -0.1361 -0.0142 619 LYS B CE 11884 N NZ . LYS B 619 ? 1.3423 0.8621 1.7034 0.3775 -0.1426 -0.0344 619 LYS B NZ 11885 N N . PHE B 620 ? 1.2256 0.6669 1.3860 0.3369 -0.1280 0.0456 620 PHE B N 11886 C CA . PHE B 620 ? 1.3452 0.7571 1.4466 0.3305 -0.1368 0.0416 620 PHE B CA 11887 C C . PHE B 620 ? 1.4230 0.8393 1.4789 0.3145 -0.1291 0.0525 620 PHE B C 11888 O O . PHE B 620 ? 1.3212 0.7117 1.3209 0.3041 -0.1343 0.0491 620 PHE B O 11889 C CB . PHE B 620 ? 1.2427 0.6565 1.3485 0.3274 -0.1358 0.0444 620 PHE B CB 11890 C CG . PHE B 620 ? 1.2378 0.6371 1.3710 0.3384 -0.1450 0.0284 620 PHE B CG 11891 C CD1 . PHE B 620 ? 1.2557 0.6198 1.3542 0.3416 -0.1629 0.0109 620 PHE B CD1 11892 C CD2 . PHE B 620 ? 1.4373 0.8564 1.6277 0.3438 -0.1356 0.0312 620 PHE B CD2 11893 C CE1 . PHE B 620 ? 1.3625 0.7191 1.4851 0.3491 -0.1718 -0.0043 620 PHE B CE1 11894 C CE2 . PHE B 620 ? 1.4483 0.8554 1.6614 0.3497 -0.1424 0.0143 620 PHE B CE2 11895 C CZ . PHE B 620 ? 1.2674 0.6473 1.4479 0.3520 -0.1608 -0.0038 620 PHE B CZ 11896 N N . ASP B 621 ? 1.4203 0.8693 1.4975 0.3093 -0.1161 0.0650 621 ASP B N 11897 C CA . ASP B 621 ? 1.4793 0.9358 1.5148 0.2918 -0.1077 0.0727 621 ASP B CA 11898 C C . ASP B 621 ? 1.4872 0.9542 1.4836 0.2736 -0.1034 0.0838 621 ASP B C 11899 O O . ASP B 621 ? 1.6395 1.0828 1.5753 0.2584 -0.1045 0.0781 621 ASP B O 11900 C CB . ASP B 621 ? 1.7401 1.1520 1.7320 0.2952 -0.1159 0.0540 621 ASP B CB 11901 C CG . ASP B 621 ? 1.7879 1.2078 1.7473 0.2778 -0.1035 0.0582 621 ASP B CG 11902 O OD1 . ASP B 621 ? 1.7620 1.2269 1.7554 0.2710 -0.0904 0.0706 621 ASP B OD1 11903 O OD2 . ASP B 621 ? 1.6809 1.0598 1.5775 0.2688 -0.1060 0.0491 621 ASP B OD2 11904 N N . ARG B 622 ? 1.5885 1.0911 1.6187 0.2750 -0.0977 0.0987 622 ARG B N 11905 C CA . ARG B 622 ? 1.5099 1.0328 1.5111 0.2605 -0.0941 0.1069 622 ARG B CA 11906 C C . ARG B 622 ? 1.5817 1.1562 1.6312 0.2669 -0.0847 0.1282 622 ARG B C 11907 O O . ARG B 622 ? 1.3625 0.9523 1.4620 0.2792 -0.0798 0.1394 622 ARG B O 11908 C CB . ARG B 622 ? 1.5613 1.0449 1.5303 0.2609 -0.1057 0.0892 622 ARG B CB 11909 C CG . ARG B 622 ? 1.6544 1.1263 1.6699 0.2814 -0.1121 0.0816 622 ARG B CG 11910 C CD . ARG B 622 ? 1.7367 1.1648 1.7137 0.2794 -0.1256 0.0619 622 ARG B CD 11911 N NE . ARG B 622 ? 1.6441 1.0651 1.6636 0.2951 -0.1303 0.0530 622 ARG B NE 11912 C CZ . ARG B 622 ? 1.6673 1.0544 1.6641 0.2951 -0.1427 0.0357 622 ARG B CZ 11913 N NH1 . ARG B 622 ? 1.7959 1.1482 1.7256 0.2816 -0.1525 0.0272 622 ARG B NH1 11914 N NH2 . ARG B 622 ? 1.6464 1.0318 1.6837 0.3065 -0.1448 0.0269 622 ARG B NH2 11915 N N . GLY B 623 ? 1.8976 1.4979 1.9299 0.2585 -0.0821 0.1334 623 GLY B N 11916 C CA . GLY B 623 ? 1.9377 1.5876 2.0127 0.2686 -0.0741 0.1535 623 GLY B CA 11917 C C . GLY B 623 ? 1.8306 1.5325 1.9152 0.2612 -0.0646 0.1790 623 GLY B C 11918 O O . GLY B 623 ? 1.8819 1.5865 1.9318 0.2420 -0.0626 0.1786 623 GLY B O 11919 N N . ALA B 624 ? 1.7122 1.4538 1.8422 0.2766 -0.0587 0.2014 624 ALA B N 11920 C CA . ALA B 624 ? 1.5903 1.3840 1.7322 0.2716 -0.0514 0.2296 624 ALA B CA 11921 C C . ALA B 624 ? 1.5481 1.3209 1.7102 0.2726 -0.0492 0.2340 624 ALA B C 11922 O O . ALA B 624 ? 1.7189 1.4419 1.8876 0.2787 -0.0536 0.2141 624 ALA B O 11923 C CB . ALA B 624 ? 1.6334 1.4705 1.8167 0.2922 -0.0473 0.2539 624 ALA B CB 11924 N N . LEU B 625 ? 1.4750 1.2911 1.6452 0.2650 -0.0426 0.2592 625 LEU B N 11925 C CA . LEU B 625 ? 1.5017 1.3084 1.6897 0.2613 -0.0384 0.2652 625 LEU B CA 11926 C C . LEU B 625 ? 1.6064 1.3849 1.7585 0.2430 -0.0392 0.2401 625 LEU B C 11927 O O . LEU B 625 ? 1.4984 1.2775 1.6582 0.2350 -0.0343 0.2409 625 LEU B O 11928 C CB . LEU B 625 ? 1.5424 1.3128 1.7787 0.2837 -0.0385 0.2647 625 LEU B CB 11929 C CG . LEU B 625 ? 1.5420 1.3142 1.8058 0.2809 -0.0318 0.2789 625 LEU B CG 11930 C CD1 . LEU B 625 ? 1.5111 1.3319 1.7863 0.2807 -0.0261 0.3178 625 LEU B CD1 11931 C CD2 . LEU B 625 ? 1.3582 1.0852 1.6599 0.2971 -0.0317 0.2682 625 LEU B CD2 11932 N N . HIS B 626 ? 1.8648 1.6177 1.9760 0.2364 -0.0450 0.2176 626 HIS B N 11933 C CA . HIS B 626 ? 1.9005 1.6181 1.9703 0.2224 -0.0464 0.1937 626 HIS B CA 11934 C C . HIS B 626 ? 1.9174 1.6679 1.9395 0.1928 -0.0384 0.1993 626 HIS B C 11935 O O . HIS B 626 ? 2.1072 1.8635 2.1196 0.1788 -0.0311 0.1979 626 HIS B O 11936 C CB . HIS B 626 ? 1.9184 1.5829 1.9614 0.2295 -0.0573 0.1681 626 HIS B CB 11937 C CG . HIS B 626 ? 1.8759 1.4942 1.8753 0.2213 -0.0605 0.1444 626 HIS B CG 11938 N ND1 . HIS B 626 ? 1.7794 1.3485 1.7339 0.2205 -0.0700 0.1244 626 HIS B ND1 11939 C CD2 . HIS B 626 ? 1.8339 1.4453 1.8266 0.2148 -0.0551 0.1375 626 HIS B CD2 11940 C CE1 . HIS B 626 ? 1.7361 1.2660 1.6573 0.2167 -0.0710 0.1077 626 HIS B CE1 11941 N NE2 . HIS B 626 ? 1.7706 1.3270 1.7161 0.2138 -0.0615 0.1138 626 HIS B NE2 11942 N N . ASP B 627 ? 1.8339 1.6085 1.8256 0.1812 -0.0386 0.2035 627 ASP B N 11943 C CA . ASP B 627 ? 1.8779 1.6854 1.8173 0.1482 -0.0306 0.2058 627 ASP B CA 11944 C C . ASP B 627 ? 1.8428 1.7148 1.7979 0.1347 -0.0209 0.2312 627 ASP B C 11945 O O . ASP B 627 ? 1.9667 1.8656 1.8788 0.1037 -0.0124 0.2311 627 ASP B O 11946 C CB . ASP B 627 ? 1.8834 1.7167 1.7954 0.1386 -0.0325 0.2062 627 ASP B CB 11947 C CG . ASP B 627 ? 1.8681 1.7230 1.8319 0.1671 -0.0384 0.2189 627 ASP B CG 11948 O OD1 . ASP B 627 ? 1.8078 1.6218 1.8107 0.1936 -0.0442 0.2138 627 ASP B OD1 11949 O OD2 . ASP B 627 ? 2.0283 1.9430 1.9938 0.1629 -0.0364 0.2327 627 ASP B OD2 11950 N N . GLU B 628 ? 1.7296 1.6241 1.7420 0.1555 -0.0217 0.2530 628 GLU B N 11951 C CA . GLU B 628 ? 1.7116 1.6610 1.7386 0.1434 -0.0139 0.2788 628 GLU B CA 11952 C C . GLU B 628 ? 1.7813 1.7027 1.8098 0.1350 -0.0077 0.2667 628 GLU B C 11953 O O . GLU B 628 ? 1.9169 1.8782 1.9520 0.1199 0.0001 0.2837 628 GLU B O 11954 C CB . GLU B 628 ? 1.6770 1.6583 1.7593 0.1686 -0.0170 0.3102 628 GLU B CB 11955 C CG . GLU B 628 ? 1.6557 1.6833 1.7423 0.1782 -0.0212 0.3265 628 GLU B CG 11956 C CD . GLU B 628 ? 1.7592 1.7440 1.8564 0.2012 -0.0284 0.3080 628 GLU B CD 11957 O OE1 . GLU B 628 ? 1.8033 1.7225 1.8974 0.2066 -0.0314 0.2822 628 GLU B OE1 11958 O OE2 . GLU B 628 ? 1.7828 1.8034 1.8921 0.2140 -0.0311 0.3188 628 GLU B OE2 11959 N N . ASN B 629 ? 1.7922 1.6485 1.8154 0.1456 -0.0117 0.2371 629 ASN B N 11960 C CA . ASN B 629 ? 1.9147 1.7433 1.9448 0.1436 -0.0068 0.2201 629 ASN B CA 11961 C C . ASN B 629 ? 1.7687 1.6179 1.8537 0.1539 -0.0041 0.2382 629 ASN B C 11962 O O . ASN B 629 ? 1.7901 1.6435 1.8828 0.1436 0.0038 0.2319 629 ASN B O 11963 C CB . ASN B 629 ? 2.0068 1.8497 1.9893 0.1109 0.0052 0.2113 629 ASN B CB 11964 C CG . ASN B 629 ? 2.0512 1.8524 1.9726 0.0996 0.0042 0.1870 629 ASN B CG 11965 O OD1 . ASN B 629 ? 2.0782 1.9064 1.9542 0.0717 0.0108 0.1913 629 ASN B OD1 11966 N ND2 . ASN B 629 ? 2.0466 1.7815 1.9638 0.1199 -0.0042 0.1617 629 ASN B ND2 11967 N N . THR B 630 ? 1.7056 1.5658 1.8266 0.1732 -0.0097 0.2597 630 THR B N 11968 C CA . THR B 630 ? 1.7103 1.5764 1.8798 0.1844 -0.0074 0.2772 630 THR B CA 11969 C C . THR B 630 ? 1.6997 1.5128 1.8996 0.2078 -0.0138 0.2558 630 THR B C 11970 O O . THR B 630 ? 1.4646 1.2715 1.7040 0.2178 -0.0120 0.2657 630 THR B O 11971 C CB . THR B 630 ? 1.5530 1.4570 1.7430 0.1937 -0.0086 0.3151 630 THR B CB 11972 O OG1 . THR B 630 ? 1.5197 1.3988 1.7240 0.2190 -0.0168 0.3116 630 THR B OG1 11973 C CG2 . THR B 630 ? 1.4784 1.4424 1.6351 0.1723 -0.0055 0.3343 630 THR B CG2 11974 N N . CYS B 631 ? 1.9001 1.6748 2.0776 0.2144 -0.0212 0.2269 631 CYS B N 11975 C CA . CYS B 631 ? 2.0105 1.7390 2.2112 0.2365 -0.0300 0.2058 631 CYS B CA 11976 C C . CYS B 631 ? 1.9591 1.6815 2.1998 0.2401 -0.0260 0.1991 631 CYS B C 11977 O O . CYS B 631 ? 2.0571 1.7634 2.3332 0.2544 -0.0280 0.2005 631 CYS B O 11978 C CB . CYS B 631 ? 2.1714 1.8605 2.3347 0.2388 -0.0385 0.1755 631 CYS B CB 11979 S SG . CYS B 631 ? 3.2834 2.9233 3.4681 0.2649 -0.0523 0.1535 631 CYS B SG 11980 N N . ASN B 632 ? 1.8640 1.6003 2.0982 0.2251 -0.0187 0.1898 632 ASN B N 11981 C CA . ASN B 632 ? 1.8573 1.6061 2.1297 0.2209 -0.0110 0.1918 632 ASN B CA 11982 C C . ASN B 632 ? 1.6980 1.4916 1.9647 0.1971 0.0013 0.2175 632 ASN B C 11983 O O . ASN B 632 ? 1.7501 1.5626 1.9983 0.1789 0.0089 0.2074 632 ASN B O 11984 C CB . ASN B 632 ? 2.0696 1.8034 2.3495 0.2245 -0.0122 0.1561 632 ASN B CB 11985 C CG . ASN B 632 ? 2.0109 1.7576 2.3343 0.2205 -0.0052 0.1521 632 ASN B CG 11986 O OD1 . ASN B 632 ? 1.9553 1.7232 2.2941 0.2075 0.0040 0.1777 632 ASN B OD1 11987 N ND2 . ASN B 632 ? 1.9409 1.6758 2.2822 0.2311 -0.0096 0.1198 632 ASN B ND2 11988 N N . ARG B 633 ? 1.7220 1.5310 2.0035 0.1983 0.0032 0.2512 633 ARG B N 11989 C CA . ARG B 633 ? 1.8273 1.6688 2.1203 0.1810 0.0133 0.2790 633 ARG B CA 11990 C C . ARG B 633 ? 1.7512 1.5708 2.0767 0.1979 0.0118 0.2991 633 ARG B C 11991 O O . ARG B 633 ? 1.6909 1.4969 2.0425 0.1943 0.0177 0.2972 633 ARG B O 11992 C CB . ARG B 633 ? 1.9032 1.7912 2.1658 0.1635 0.0166 0.3066 633 ARG B CB 11993 C CG . ARG B 633 ? 1.9272 1.8484 2.1996 0.1471 0.0248 0.3413 633 ARG B CG 11994 C CD . ARG B 633 ? 1.9550 1.9237 2.1978 0.1144 0.0338 0.3447 633 ARG B CD 11995 N NE . ARG B 633 ? 1.9128 1.8725 2.1511 0.1011 0.0412 0.3059 633 ARG B NE 11996 C CZ . ARG B 633 ? 1.8529 1.8465 2.0677 0.0717 0.0521 0.2989 633 ARG B CZ 11997 N NH1 . ARG B 633 ? 1.8677 1.9090 2.0595 0.0494 0.0562 0.3293 633 ARG B NH1 11998 N NH2 . ARG B 633 ? 1.8062 1.7884 2.0209 0.0651 0.0591 0.2610 633 ARG B NH2 11999 N N . TYR B 634 ? 1.7626 1.5791 2.0837 0.2154 0.0050 0.3167 634 TYR B N 12000 C CA . TYR B 634 ? 1.8074 1.5988 2.1549 0.2364 0.0038 0.3358 634 TYR B CA 12001 C C . TYR B 634 ? 1.8247 1.5672 2.1978 0.2491 0.0022 0.3076 634 TYR B C 12002 O O . TYR B 634 ? 1.9601 1.6757 2.3575 0.2576 0.0066 0.3191 634 TYR B O 12003 C CB . TYR B 634 ? 1.7031 1.5068 2.0400 0.2541 -0.0034 0.3512 634 TYR B CB 12004 C CG . TYR B 634 ? 1.7904 1.6509 2.1052 0.2427 -0.0026 0.3821 634 TYR B CG 12005 C CD1 . TYR B 634 ? 1.9341 1.8237 2.2466 0.2234 0.0043 0.4068 634 TYR B CD1 12006 C CD2 . TYR B 634 ? 1.8143 1.7036 2.1088 0.2484 -0.0087 0.3859 634 TYR B CD2 12007 C CE1 . TYR B 634 ? 1.9433 1.8906 2.2345 0.2112 0.0041 0.4356 634 TYR B CE1 12008 C CE2 . TYR B 634 ? 1.9625 1.9122 2.2370 0.2360 -0.0083 0.4132 634 TYR B CE2 12009 C CZ . TYR B 634 ? 1.9120 1.8911 2.1852 0.2180 -0.0024 0.4385 634 TYR B CZ 12010 O OH . TYR B 634 ? 1.7760 1.8207 2.0283 0.2040 -0.0029 0.4662 634 TYR B OH 12011 N N . CYS B 635 ? 1.6506 1.3801 2.0160 0.2500 -0.0038 0.2712 635 CYS B N 12012 C CA . CYS B 635 ? 1.6932 1.3856 2.0826 0.2593 -0.0062 0.2434 635 CYS B CA 12013 C C . CYS B 635 ? 1.6954 1.3975 2.0962 0.2427 -0.0006 0.2232 635 CYS B C 12014 O O . CYS B 635 ? 1.8007 1.5141 2.1870 0.2384 -0.0042 0.1996 635 CYS B O 12015 C CB . CYS B 635 ? 1.5696 1.2407 1.9450 0.2739 -0.0187 0.2161 635 CYS B CB 12016 S SG . CYS B 635 ? 1.3581 1.0215 1.7202 0.2917 -0.0249 0.2307 635 CYS B SG 12017 N N . ARG B 636 ? 1.6934 1.3900 2.1190 0.2334 0.0091 0.2316 636 ARG B N 12018 C CA . ARG B 636 ? 1.7104 1.4199 2.1520 0.2163 0.0158 0.2092 636 ARG B CA 12019 C C . ARG B 636 ? 1.7107 1.3940 2.1792 0.2238 0.0132 0.1805 636 ARG B C 12020 O O . ARG B 636 ? 1.8306 1.5288 2.3168 0.2118 0.0174 0.1563 636 ARG B O 12021 C CB . ARG B 636 ? 1.9016 1.6282 2.3473 0.1927 0.0299 0.2359 636 ARG B CB 12022 C CG . ARG B 636 ? 1.8863 1.6526 2.3058 0.1777 0.0333 0.2563 636 ARG B CG 12023 C CD . ARG B 636 ? 1.9420 1.7223 2.3612 0.1547 0.0455 0.2887 636 ARG B CD 12024 N NE . ARG B 636 ? 2.0439 1.8006 2.4616 0.1676 0.0445 0.3283 636 ARG B NE 12025 C CZ . ARG B 636 ? 2.0202 1.7975 2.4182 0.1733 0.0405 0.3617 636 ARG B CZ 12026 N NH1 . ARG B 636 ? 2.0187 1.8391 2.3933 0.1625 0.0383 0.3596 636 ARG B NH1 12027 N NH2 . ARG B 636 ? 1.9613 1.7173 2.3623 0.1901 0.0391 0.3964 636 ARG B NH2 12028 N N . ASP B 637 ? 1.6842 1.3336 2.1558 0.2425 0.0067 0.1817 637 ASP B N 12029 C CA . ASP B 637 ? 1.5963 1.2200 2.0916 0.2470 0.0054 0.1573 637 ASP B CA 12030 C C . ASP B 637 ? 1.5742 1.2094 2.0726 0.2540 -0.0067 0.1180 637 ASP B C 12031 O O . ASP B 637 ? 1.5978 1.2334 2.0743 0.2677 -0.0189 0.1107 637 ASP B O 12032 C CB . ASP B 637 ? 1.7203 1.3055 2.2155 0.2648 0.0027 0.1678 637 ASP B CB 12033 C CG . ASP B 637 ? 1.8583 1.4282 2.3526 0.2644 0.0138 0.2072 637 ASP B CG 12034 O OD1 . ASP B 637 ? 1.7844 1.3262 2.2947 0.2569 0.0252 0.2125 637 ASP B OD1 12035 O OD2 . ASP B 637 ? 1.9615 1.5474 2.4376 0.2716 0.0112 0.2330 637 ASP B OD2 12036 N N . GLU B 638 ? 1.5983 1.2434 2.1224 0.2441 -0.0034 0.0931 638 GLU B N 12037 C CA . GLU B 638 ? 1.4927 1.1518 2.0249 0.2544 -0.0165 0.0558 638 GLU B CA 12038 C C . GLU B 638 ? 1.5484 1.1755 2.0753 0.2733 -0.0299 0.0458 638 GLU B C 12039 O O . GLU B 638 ? 1.7666 1.3677 2.3048 0.2705 -0.0246 0.0499 638 GLU B O 12040 C CB . GLU B 638 ? 1.5457 1.2322 2.1100 0.2378 -0.0092 0.0312 638 GLU B CB 12041 C CG . GLU B 638 ? 1.7951 1.5247 2.3646 0.2210 0.0006 0.0279 638 GLU B CG 12042 C CD . GLU B 638 ? 1.9459 1.7001 2.5059 0.2376 -0.0112 0.0068 638 GLU B CD 12043 O OE1 . GLU B 638 ? 1.8613 1.6456 2.4173 0.2267 -0.0027 0.0073 638 GLU B OE1 12044 O OE2 . GLU B 638 ? 1.9496 1.6903 2.5039 0.2612 -0.0283 -0.0105 638 GLU B OE2 12045 N N . ILE B 639 ? 1.3769 1.0025 1.8831 0.2910 -0.0464 0.0324 639 ILE B N 12046 C CA . ILE B 639 ? 1.2559 0.8526 1.7508 0.3067 -0.0604 0.0226 639 ILE B CA 12047 C C . ILE B 639 ? 1.2820 0.8905 1.7815 0.3189 -0.0772 -0.0106 639 ILE B C 12048 O O . ILE B 639 ? 1.3632 0.9906 1.8545 0.3259 -0.0833 -0.0211 639 ILE B O 12049 C CB . ILE B 639 ? 1.2624 0.8388 1.7188 0.3167 -0.0665 0.0409 639 ILE B CB 12050 C CG1 . ILE B 639 ? 1.2791 0.8546 1.7329 0.3078 -0.0515 0.0753 639 ILE B CG1 12051 C CG2 . ILE B 639 ? 1.4403 0.9873 1.8837 0.3288 -0.0792 0.0308 639 ILE B CG2 12052 C CD1 . ILE B 639 ? 1.2112 0.7773 1.6302 0.3150 -0.0561 0.0927 639 ILE B CD1 12053 N N . GLU B 640 ? 1.2222 0.8203 1.7345 0.3219 -0.0844 -0.0274 640 GLU B N 12054 C CA . GLU B 640 ? 1.2135 0.8262 1.7303 0.3352 -0.1031 -0.0572 640 GLU B CA 12055 C C . GLU B 640 ? 1.3330 0.9162 1.8335 0.3444 -0.1175 -0.0646 640 GLU B C 12056 O O . GLU B 640 ? 1.6123 1.1812 2.1254 0.3338 -0.1099 -0.0641 640 GLU B O 12057 C CB . GLU B 640 ? 1.3314 0.9848 1.8904 0.3233 -0.0973 -0.0793 640 GLU B CB 12058 C CG . GLU B 640 ? 1.5757 1.2676 2.1504 0.3153 -0.0864 -0.0806 640 GLU B CG 12059 C CD . GLU B 640 ? 1.7208 1.4248 2.2779 0.3369 -0.0999 -0.0900 640 GLU B CD 12060 O OE1 . GLU B 640 ? 1.5676 1.2625 2.1114 0.3591 -0.1207 -0.1048 640 GLU B OE1 12061 O OE2 . GLU B 640 ? 1.7720 1.4917 2.3258 0.3313 -0.0892 -0.0824 640 GLU B OE2 12062 N N . SER B 641 ? 1.3359 0.9070 1.8054 0.3630 -0.1375 -0.0719 641 SER B N 12063 C CA . SER B 641 ? 1.2816 0.8261 1.7296 0.3703 -0.1533 -0.0798 641 SER B CA 12064 C C . SER B 641 ? 1.1915 0.7611 1.6676 0.3707 -0.1637 -0.1067 641 SER B C 12065 O O . SER B 641 ? 1.4989 1.1016 1.9898 0.3816 -0.1743 -0.1238 641 SER B O 12066 C CB . SER B 641 ? 1.3876 0.9063 1.7867 0.3875 -0.1715 -0.0775 641 SER B CB 12067 O OG . SER B 641 ? 1.7381 1.2756 2.1378 0.4027 -0.1809 -0.0890 641 SER B OG 12068 N N . VAL B 642 ? 1.1973 0.7546 1.6812 0.3587 -0.1600 -0.1116 642 VAL B N 12069 C CA . VAL B 642 ? 1.3169 0.9020 1.8284 0.3521 -0.1663 -0.1374 642 VAL B CA 12070 C C . VAL B 642 ? 1.2605 0.8218 1.7544 0.3484 -0.1758 -0.1460 642 VAL B C 12071 O O . VAL B 642 ? 1.3089 0.8311 1.7740 0.3482 -0.1731 -0.1319 642 VAL B O 12072 C CB . VAL B 642 ? 1.2890 0.8948 1.8418 0.3281 -0.1424 -0.1413 642 VAL B CB 12073 C CG1 . VAL B 642 ? 1.3729 1.0180 1.9487 0.3278 -0.1358 -0.1423 642 VAL B CG1 12074 C CG2 . VAL B 642 ? 1.2052 0.7697 1.7527 0.3150 -0.1202 -0.1189 642 VAL B CG2 12075 N N . LYS B 643 ? 1.2286 0.8196 1.7405 0.3439 -0.1865 -0.1708 643 LYS B N 12076 C CA . LYS B 643 ? 1.2445 0.8212 1.7487 0.3313 -0.1896 -0.1832 643 LYS B CA 12077 C C . LYS B 643 ? 1.5697 1.1377 2.1018 0.3048 -0.1604 -0.1843 643 LYS B C 12078 O O . LYS B 643 ? 1.6795 1.2414 2.2262 0.2998 -0.1404 -0.1687 643 LYS B O 12079 C CB . LYS B 643 ? 1.2563 0.8741 1.7685 0.3347 -0.2127 -0.2093 643 LYS B CB 12080 C CG . LYS B 643 ? 1.4492 1.0912 1.9509 0.3642 -0.2392 -0.2114 643 LYS B CG 12081 C CD . LYS B 643 ? 1.3996 1.0918 1.9167 0.3675 -0.2612 -0.2373 643 LYS B CD 12082 C CE . LYS B 643 ? 1.3863 1.1085 1.9011 0.4013 -0.2869 -0.2411 643 LYS B CE 12083 N NZ . LYS B 643 ? 1.4555 1.2379 1.9911 0.4061 -0.3087 -0.2660 643 LYS B NZ 12084 N N . GLU B 644 ? 1.6760 1.2398 2.2120 0.2871 -0.1573 -0.2023 644 GLU B N 12085 C CA . GLU B 644 ? 1.7612 1.3171 2.3242 0.2600 -0.1293 -0.2091 644 GLU B CA 12086 C C . GLU B 644 ? 1.7392 1.2463 2.2982 0.2589 -0.1046 -0.1832 644 GLU B C 12087 O O . GLU B 644 ? 1.8919 1.3607 2.4308 0.2620 -0.1006 -0.1760 644 GLU B O 12088 C CB . GLU B 644 ? 2.1127 1.7177 2.7112 0.2474 -0.1234 -0.2227 644 GLU B CB 12089 C CG . GLU B 644 ? 2.1842 1.8420 2.7970 0.2375 -0.1392 -0.2551 644 GLU B CG 12090 C CD . GLU B 644 ? 2.0761 1.7166 2.6876 0.2099 -0.1277 -0.2739 644 GLU B CD 12091 O OE1 . GLU B 644 ? 2.1073 1.7023 2.7209 0.1916 -0.0994 -0.2670 644 GLU B OE1 12092 O OE2 . GLU B 644 ? 1.9949 1.6660 2.6016 0.2068 -0.1469 -0.2954 644 GLU B OE2 12093 N N . LEU B 645 ? 1.5306 1.0433 2.1089 0.2545 -0.0885 -0.1697 645 LEU B N 12094 C CA . LEU B 645 ? 1.5443 1.0161 2.1289 0.2451 -0.0605 -0.1498 645 LEU B CA 12095 C C . LEU B 645 ? 1.4196 0.8732 2.0177 0.2182 -0.0418 -0.1703 645 LEU B C 12096 O O . LEU B 645 ? 1.5190 0.9311 2.1074 0.2156 -0.0313 -0.1713 645 LEU B O 12097 C CB . LEU B 645 ? 1.2858 0.7179 1.8463 0.2635 -0.0589 -0.1252 645 LEU B CB 12098 C CG . LEU B 645 ? 1.4547 0.8582 2.0178 0.2680 -0.0386 -0.0933 645 LEU B CG 12099 C CD1 . LEU B 645 ? 1.3724 0.7559 1.9113 0.2884 -0.0434 -0.0737 645 LEU B CD1 12100 C CD2 . LEU B 645 ? 1.7299 1.0966 2.3089 0.2500 -0.0116 -0.0946 645 LEU B CD2 12101 N N . LYS B 646 ? 1.4833 0.9721 2.1036 0.1968 -0.0373 -0.1893 646 LYS B N 12102 C CA . LYS B 646 ? 1.7959 1.2769 2.4281 0.1644 -0.0195 -0.2140 646 LYS B CA 12103 C C . LYS B 646 ? 1.9774 1.3904 2.6063 0.1521 0.0123 -0.1989 646 LYS B C 12104 O O . LYS B 646 ? 1.9439 1.3304 2.5703 0.1634 0.0226 -0.1683 646 LYS B O 12105 C CB . LYS B 646 ? 1.8872 1.4260 2.5437 0.1427 -0.0190 -0.2341 646 LYS B CB 12106 C CG . LYS B 646 ? 1.7891 1.3985 2.4527 0.1565 -0.0505 -0.2537 646 LYS B CG 12107 C CD . LYS B 646 ? 1.7041 1.3755 2.3931 0.1503 -0.0522 -0.2618 646 LYS B CD 12108 C CE . LYS B 646 ? 1.6222 1.3620 2.3192 0.1717 -0.0848 -0.2799 646 LYS B CE 12109 N NZ . LYS B 646 ? 1.6708 1.4736 2.3940 0.1731 -0.0873 -0.2872 646 LYS B NZ 12110 N N . ASP B 647 ? 2.0538 1.4383 2.6814 0.1292 0.0276 -0.2206 647 ASP B N 12111 C CA . ASP B 647 ? 2.1094 1.4193 2.7306 0.1209 0.0580 -0.2099 647 ASP B CA 12112 C C . ASP B 647 ? 2.1954 1.4789 2.8227 0.1063 0.0815 -0.1913 647 ASP B C 12113 O O . ASP B 647 ? 2.2053 1.4225 2.8245 0.1110 0.1033 -0.1700 647 ASP B O 12114 C CB . ASP B 647 ? 2.1062 1.3952 2.7242 0.0927 0.0717 -0.2437 647 ASP B CB 12115 C CG . ASP B 647 ? 2.0054 1.3153 2.6129 0.1036 0.0503 -0.2613 647 ASP B CG 12116 O OD1 . ASP B 647 ? 1.7853 1.0941 2.3818 0.1355 0.0339 -0.2419 647 ASP B OD1 12117 O OD2 . ASP B 647 ? 2.0149 1.3437 2.6224 0.0776 0.0500 -0.2948 647 ASP B OD2 12118 N N . THR B 648 ? 2.1253 1.4604 2.7660 0.0891 0.0771 -0.1989 648 THR B N 12119 C CA . THR B 648 ? 2.2548 1.5671 2.8973 0.0704 0.0994 -0.1819 648 THR B CA 12120 C C . THR B 648 ? 2.1731 1.5090 2.8173 0.0943 0.0879 -0.1495 648 THR B C 12121 O O . THR B 648 ? 1.9980 1.4010 2.6542 0.0969 0.0701 -0.1575 648 THR B O 12122 C CB . THR B 648 ? 2.3004 1.6541 2.9555 0.0272 0.1084 -0.2133 648 THR B CB 12123 O OG1 . THR B 648 ? 2.2643 1.6209 2.9216 0.0130 0.1210 -0.1952 648 THR B OG1 12124 C CG2 . THR B 648 ? 2.2272 1.6716 2.8994 0.0309 0.0796 -0.2423 648 THR B CG2 12125 N N . GLY B 649 ? 2.3353 1.6160 2.9670 0.1125 0.0987 -0.1133 649 GLY B N 12126 C CA . GLY B 649 ? 2.3811 1.6774 3.0107 0.1302 0.0924 -0.0798 649 GLY B CA 12127 C C . GLY B 649 ? 2.4085 1.6641 3.0317 0.1109 0.1169 -0.0557 649 GLY B C 12128 O O . GLY B 649 ? 2.5737 1.8320 3.1913 0.1239 0.1151 -0.0229 649 GLY B O 12129 N N . LYS B 650 ? 2.2402 1.4559 2.8602 0.0779 0.1400 -0.0715 650 LYS B N 12130 C CA . LYS B 650 ? 2.2379 1.3913 2.8428 0.0594 0.1663 -0.0464 650 LYS B CA 12131 C C . LYS B 650 ? 2.1344 1.2271 2.7262 0.0960 0.1697 -0.0060 650 LYS B C 12132 O O . LYS B 650 ? 2.0563 1.1076 2.6456 0.1140 0.1729 -0.0106 650 LYS B O 12133 C CB . LYS B 650 ? 2.2348 1.4309 2.8415 0.0389 0.1672 -0.0356 650 LYS B CB 12134 C CG . LYS B 650 ? 2.2364 1.4888 2.8564 -0.0030 0.1706 -0.0754 650 LYS B CG 12135 C CD . LYS B 650 ? 2.1436 1.4873 2.7876 0.0118 0.1422 -0.1036 650 LYS B CD 12136 C CE . LYS B 650 ? 2.1456 1.5562 2.8071 -0.0266 0.1447 -0.1428 650 LYS B CE 12137 N NZ . LYS B 650 ? 2.1018 1.5364 2.7628 -0.0525 0.1566 -0.1325 650 LYS B NZ 12138 N N . ASP B 651 ? 2.1115 1.2044 2.6958 0.1069 0.1687 0.0326 651 ASP B N 12139 C CA . ASP B 651 ? 2.0724 1.1287 2.6481 0.1461 0.1665 0.0720 651 ASP B CA 12140 C C . ASP B 651 ? 2.0953 1.2160 2.6800 0.1773 0.1390 0.0751 651 ASP B C 12141 O O . ASP B 651 ? 2.1808 1.3581 2.7680 0.1751 0.1261 0.0824 651 ASP B O 12142 C CB . ASP B 651 ? 2.2024 1.2267 2.7620 0.1423 0.1783 0.1151 651 ASP B CB 12143 C CG . ASP B 651 ? 2.5254 1.4585 3.0667 0.1223 0.2071 0.1224 651 ASP B CG 12144 O OD1 . ASP B 651 ? 2.5922 1.4758 3.1335 0.1243 0.2185 0.1019 651 ASP B OD1 12145 O OD2 . ASP B 651 ? 2.6830 1.5907 3.2069 0.1032 0.2191 0.1485 651 ASP B OD2 12146 N N . ALA B 652 ? 2.0056 1.1154 2.5925 0.2043 0.1316 0.0684 652 ALA B N 12147 C CA . ALA B 652 ? 1.7086 0.8733 2.2983 0.2297 0.1067 0.0678 652 ALA B CA 12148 C C . ALA B 652 ? 1.5494 0.6884 2.1364 0.2607 0.1046 0.0726 652 ALA B C 12149 O O . ALA B 652 ? 1.6712 0.7505 2.2576 0.2650 0.1225 0.0737 652 ALA B O 12150 C CB . ALA B 652 ? 1.4815 0.7009 2.0799 0.2150 0.0905 0.0286 652 ALA B CB 12151 N N . VAL B 653 ? 1.4730 0.6570 2.0569 0.2811 0.0836 0.0736 653 VAL B N 12152 C CA . VAL B 653 ? 1.4680 0.6410 2.0485 0.3079 0.0798 0.0751 653 VAL B CA 12153 C C . VAL B 653 ? 1.5111 0.7290 2.0853 0.3106 0.0575 0.0496 653 VAL B C 12154 O O . VAL B 653 ? 1.4297 0.6939 1.9973 0.3100 0.0405 0.0526 653 VAL B O 12155 C CB . VAL B 653 ? 1.4673 0.6437 2.0431 0.3357 0.0793 0.1166 653 VAL B CB 12156 C CG1 . VAL B 653 ? 1.7415 0.8723 2.3038 0.3457 0.0961 0.1298 653 VAL B CG1 12157 C CG2 . VAL B 653 ? 1.4546 0.6598 2.0263 0.3271 0.0757 0.1433 653 VAL B CG2 12158 N N . ASN B 654 ? 1.5747 0.7755 2.1481 0.3126 0.0582 0.0245 654 ASN B N 12159 C CA . ASN B 654 ? 1.3866 0.6221 1.9478 0.3160 0.0369 0.0034 654 ASN B CA 12160 C C . ASN B 654 ? 1.3727 0.6155 1.9225 0.3412 0.0318 0.0203 654 ASN B C 12161 O O . ASN B 654 ? 1.6539 0.8743 2.1977 0.3503 0.0443 0.0221 654 ASN B O 12162 C CB . ASN B 654 ? 1.4034 0.6239 1.9663 0.2999 0.0389 -0.0347 654 ASN B CB 12163 C CG . ASN B 654 ? 1.4339 0.6590 2.0080 0.2721 0.0428 -0.0549 654 ASN B CG 12164 O OD1 . ASN B 654 ? 1.5781 0.7799 2.1574 0.2539 0.0542 -0.0808 654 ASN B OD1 12165 N ND2 . ASN B 654 ? 1.3928 0.6515 1.9706 0.2668 0.0346 -0.0450 654 ASN B ND2 12166 N N . CYS B 655 ? 1.3329 0.6168 1.8668 0.3478 0.0133 0.0306 655 CYS B N 12167 C CA . CYS B 655 ? 1.3220 0.6220 1.8423 0.3672 0.0086 0.0476 655 CYS B CA 12168 C C . CYS B 655 ? 1.3731 0.6927 1.8688 0.3651 -0.0096 0.0261 655 CYS B C 12169 O O . CYS B 655 ? 1.3112 0.6454 1.7944 0.3535 -0.0254 0.0097 655 CYS B O 12170 C CB . CYS B 655 ? 1.3003 0.6290 1.8159 0.3741 0.0048 0.0807 655 CYS B CB 12171 S SG . CYS B 655 ? 1.4770 0.7838 2.0118 0.3736 0.0239 0.1106 655 CYS B SG 12172 N N . THR B 656 ? 1.4952 0.8155 1.9828 0.3768 -0.0071 0.0261 656 THR B N 12173 C CA . THR B 656 ? 1.2841 0.6205 1.7421 0.3723 -0.0228 0.0078 656 THR B CA 12174 C C . THR B 656 ? 1.2715 0.6358 1.7133 0.3846 -0.0247 0.0266 656 THR B C 12175 O O . THR B 656 ? 1.6528 1.0186 2.1128 0.4008 -0.0104 0.0428 656 THR B O 12176 C CB . THR B 656 ? 1.3065 0.6193 1.7661 0.3656 -0.0173 -0.0226 656 THR B CB 12177 O OG1 . THR B 656 ? 2.0150 1.3101 2.4963 0.3802 0.0039 -0.0165 656 THR B OG1 12178 C CG2 . THR B 656 ? 1.3193 0.6124 1.7912 0.3490 -0.0169 -0.0444 656 THR B CG2 12179 N N . TYR B 657 ? 1.2507 0.6376 1.6572 0.3769 -0.0422 0.0242 657 TYR B N 12180 C CA . TYR B 657 ? 1.2407 0.6582 1.6254 0.3820 -0.0443 0.0376 657 TYR B CA 12181 C C . TYR B 657 ? 1.2344 0.6571 1.5718 0.3668 -0.0621 0.0205 657 TYR B C 12182 O O . TYR B 657 ? 1.2351 0.6403 1.5569 0.3566 -0.0754 0.0050 657 TYR B O 12183 C CB . TYR B 657 ? 1.2263 0.6705 1.6152 0.3885 -0.0426 0.0697 657 TYR B CB 12184 C CG . TYR B 657 ? 1.2094 0.6614 1.5719 0.3760 -0.0570 0.0716 657 TYR B CG 12185 C CD1 . TYR B 657 ? 1.3064 0.7426 1.6832 0.3713 -0.0597 0.0669 657 TYR B CD1 12186 C CD2 . TYR B 657 ? 1.4826 0.9584 1.8053 0.3682 -0.0665 0.0765 657 TYR B CD2 12187 C CE1 . TYR B 657 ? 1.2078 0.6525 1.5632 0.3631 -0.0718 0.0665 657 TYR B CE1 12188 C CE2 . TYR B 657 ? 1.5196 0.9960 1.8163 0.3582 -0.0778 0.0767 657 TYR B CE2 12189 C CZ . TYR B 657 ? 1.2576 0.7189 1.5725 0.3578 -0.0806 0.0716 657 TYR B CZ 12190 O OH . TYR B 657 ? 1.3273 0.7907 1.6191 0.3511 -0.0908 0.0699 657 TYR B OH 12191 N N . LYS B 658 ? 1.3238 0.7710 1.6368 0.3653 -0.0623 0.0235 658 LYS B N 12192 C CA . LYS B 658 ? 1.2766 0.7238 1.5365 0.3478 -0.0774 0.0090 658 LYS B CA 12193 C C . LYS B 658 ? 1.2952 0.7674 1.5222 0.3415 -0.0833 0.0274 658 LYS B C 12194 O O . LYS B 658 ? 1.3521 0.8609 1.5844 0.3461 -0.0742 0.0440 658 LYS B O 12195 C CB . LYS B 658 ? 1.3138 0.7687 1.5627 0.3428 -0.0720 -0.0084 658 LYS B CB 12196 C CG . LYS B 658 ? 1.3797 0.8342 1.5670 0.3209 -0.0859 -0.0214 658 LYS B CG 12197 C CD . LYS B 658 ? 1.4881 0.9514 1.6661 0.3126 -0.0792 -0.0423 658 LYS B CD 12198 C CE . LYS B 658 ? 1.6980 1.1312 1.8998 0.3136 -0.0762 -0.0649 658 LYS B CE 12199 N NZ . LYS B 658 ? 1.8274 1.2686 2.0163 0.3020 -0.0694 -0.0888 658 LYS B NZ 12200 N N . ASN B 659 ? 1.3317 0.7853 1.5246 0.3313 -0.0982 0.0238 659 ASN B N 12201 C CA . ASN B 659 ? 1.4447 0.9139 1.6001 0.3219 -0.1027 0.0377 659 ASN B CA 12202 C C . ASN B 659 ? 1.6087 1.0863 1.7105 0.3038 -0.1060 0.0299 659 ASN B C 12203 O O . ASN B 659 ? 1.7346 1.2082 1.8301 0.2991 -0.1053 0.0136 659 ASN B O 12204 C CB . ASN B 659 ? 1.3756 0.8170 1.5115 0.3194 -0.1160 0.0341 659 ASN B CB 12205 C CG . ASN B 659 ? 1.3797 0.7821 1.4911 0.3154 -0.1319 0.0105 659 ASN B CG 12206 O OD1 . ASN B 659 ? 1.4101 0.8035 1.4976 0.3064 -0.1350 -0.0031 659 ASN B OD1 12207 N ND2 . ASN B 659 ? 1.2675 0.6509 1.3852 0.3221 -0.1423 0.0052 659 ASN B ND2 12208 N N . GLU B 660 ? 1.5636 1.0525 1.6243 0.2905 -0.1083 0.0399 660 GLU B N 12209 C CA . GLU B 660 ? 1.6352 1.1356 1.6403 0.2680 -0.1090 0.0338 660 GLU B CA 12210 C C . GLU B 660 ? 1.6124 1.0629 1.5616 0.2523 -0.1238 0.0123 660 GLU B C 12211 O O . GLU B 660 ? 1.6077 1.0594 1.5056 0.2300 -0.1247 0.0035 660 GLU B O 12212 C CB . GLU B 660 ? 1.7670 1.2906 1.7396 0.2542 -0.1059 0.0496 660 GLU B CB 12213 C CG . GLU B 660 ? 2.0484 1.5432 2.0140 0.2576 -0.1122 0.0561 660 GLU B CG 12214 C CD . GLU B 660 ? 2.1938 1.7167 2.2210 0.2767 -0.1036 0.0752 660 GLU B CD 12215 O OE1 . GLU B 660 ? 2.0243 1.5625 2.1053 0.2942 -0.0971 0.0791 660 GLU B OE1 12216 O OE2 . GLU B 660 ? 2.2680 1.7951 2.2869 0.2728 -0.1022 0.0859 660 GLU B OE2 12217 N N . ASP B 661 ? 1.6690 1.0781 1.6270 0.2631 -0.1357 0.0042 661 ASP B N 12218 C CA . ASP B 661 ? 1.6874 1.0482 1.5960 0.2527 -0.1526 -0.0138 661 ASP B CA 12219 C C . ASP B 661 ? 1.7605 1.1201 1.6911 0.2538 -0.1524 -0.0311 661 ASP B C 12220 O O . ASP B 661 ? 1.8947 1.2181 1.7924 0.2465 -0.1671 -0.0462 661 ASP B O 12221 C CB . ASP B 661 ? 1.6693 0.9921 1.5742 0.2653 -0.1674 -0.0143 661 ASP B CB 12222 C CG . ASP B 661 ? 1.8014 1.1140 1.6693 0.2603 -0.1683 -0.0026 661 ASP B CG 12223 O OD1 . ASP B 661 ? 1.7502 1.0649 1.5667 0.2388 -0.1637 0.0006 661 ASP B OD1 12224 O OD2 . ASP B 661 ? 1.8176 1.1217 1.7068 0.2758 -0.1722 0.0015 661 ASP B OD2 12225 N N . ASP B 662 ? 1.5577 0.9558 1.5433 0.2638 -0.1356 -0.0284 662 ASP B N 12226 C CA . ASP B 662 ? 1.5254 0.9256 1.5387 0.2656 -0.1300 -0.0459 662 ASP B CA 12227 C C . ASP B 662 ? 1.4625 0.8325 1.5021 0.2757 -0.1390 -0.0566 662 ASP B C 12228 O O . ASP B 662 ? 1.4872 0.8429 1.5226 0.2683 -0.1427 -0.0765 662 ASP B O 12229 C CB . ASP B 662 ? 1.6675 1.0621 1.6254 0.2406 -0.1340 -0.0635 662 ASP B CB 12230 C CG . ASP B 662 ? 1.9555 1.3902 1.8899 0.2271 -0.1230 -0.0568 662 ASP B CG 12231 O OD1 . ASP B 662 ? 2.0327 1.5125 2.0151 0.2420 -0.1071 -0.0448 662 ASP B OD1 12232 O OD2 . ASP B 662 ? 2.0191 1.4411 1.8854 0.2008 -0.1303 -0.0631 662 ASP B OD2 12233 N N . CYS B 663 ? 1.4310 0.7964 1.4978 0.2905 -0.1419 -0.0447 663 CYS B N 12234 C CA . CYS B 663 ? 1.3492 0.6962 1.4459 0.2996 -0.1494 -0.0547 663 CYS B CA 12235 C C . CYS B 663 ? 1.2969 0.6614 1.4612 0.3147 -0.1319 -0.0467 663 CYS B C 12236 O O . CYS B 663 ? 1.3230 0.7096 1.5073 0.3226 -0.1195 -0.0268 663 CYS B O 12237 C CB . CYS B 663 ? 1.3287 0.6553 1.3999 0.3035 -0.1680 -0.0514 663 CYS B CB 12238 S SG . CYS B 663 ? 1.5464 0.8337 1.5359 0.2890 -0.1925 -0.0629 663 CYS B SG 12239 N N . VAL B 664 ? 1.2831 0.6366 1.4790 0.3167 -0.1309 -0.0619 664 VAL B N 12240 C CA . VAL B 664 ? 1.2673 0.6274 1.5214 0.3274 -0.1130 -0.0563 664 VAL B CA 12241 C C . VAL B 664 ? 1.3222 0.6827 1.5983 0.3332 -0.1183 -0.0506 664 VAL B C 12242 O O . VAL B 664 ? 1.2636 0.6158 1.5378 0.3296 -0.1315 -0.0666 664 VAL B O 12243 C CB . VAL B 664 ? 1.2834 0.6309 1.5609 0.3223 -0.1034 -0.0782 664 VAL B CB 12244 C CG1 . VAL B 664 ? 1.3078 0.6520 1.6391 0.3317 -0.0833 -0.0717 664 VAL B CG1 12245 C CG2 . VAL B 664 ? 1.3051 0.6569 1.5648 0.3167 -0.0957 -0.0867 664 VAL B CG2 12246 N N . VAL B 665 ? 1.5103 0.8854 1.8073 0.3418 -0.1080 -0.0280 665 VAL B N 12247 C CA . VAL B 665 ? 1.2298 0.6106 1.5498 0.3453 -0.1094 -0.0221 665 VAL B CA 12248 C C . VAL B 665 ? 1.3422 0.7192 1.7115 0.3469 -0.0909 -0.0208 665 VAL B C 12249 O O . VAL B 665 ? 1.2385 0.6123 1.6252 0.3523 -0.0740 -0.0096 665 VAL B O 12250 C CB . VAL B 665 ? 1.2147 0.6135 1.5227 0.3492 -0.1090 0.0015 665 VAL B CB 12251 C CG1 . VAL B 665 ? 1.2053 0.6133 1.5372 0.3510 -0.1092 0.0049 665 VAL B CG1 12252 C CG2 . VAL B 665 ? 1.2204 0.6151 1.4734 0.3445 -0.1245 -0.0006 665 VAL B CG2 12253 N N . ARG B 666 ? 1.4789 0.8557 1.8688 0.3423 -0.0940 -0.0330 666 ARG B N 12254 C CA . ARG B 666 ? 1.3405 0.7084 1.7708 0.3381 -0.0760 -0.0351 666 ARG B CA 12255 C C . ARG B 666 ? 1.3876 0.7718 1.8379 0.3358 -0.0740 -0.0264 666 ARG B C 12256 O O . ARG B 666 ? 1.3180 0.7191 1.7632 0.3337 -0.0891 -0.0388 666 ARG B O 12257 C CB . ARG B 666 ? 1.2632 0.6186 1.7002 0.3268 -0.0780 -0.0651 666 ARG B CB 12258 C CG . ARG B 666 ? 1.8312 1.1663 2.3020 0.3186 -0.0554 -0.0707 666 ARG B CG 12259 C CD . ARG B 666 ? 1.7798 1.1063 2.2515 0.3036 -0.0576 -0.1031 666 ARG B CD 12260 N NE . ARG B 666 ? 1.7911 1.1114 2.2350 0.3048 -0.0661 -0.1137 666 ARG B NE 12261 C CZ . ARG B 666 ? 1.8645 1.1622 2.3112 0.3037 -0.0499 -0.1203 666 ARG B CZ 12262 N NH1 . ARG B 666 ? 1.6887 0.9616 2.1640 0.3042 -0.0246 -0.1162 666 ARG B NH1 12263 N NH2 . ARG B 666 ? 1.7827 1.0805 2.2017 0.3018 -0.0582 -0.1317 666 ARG B NH2 12264 N N . PHE B 667 ? 1.3307 0.7111 1.8027 0.3370 -0.0557 -0.0049 667 PHE B N 12265 C CA . PHE B 667 ? 1.2338 0.6308 1.7232 0.3308 -0.0515 0.0036 667 PHE B CA 12266 C C . PHE B 667 ? 1.2585 0.6350 1.7764 0.3228 -0.0289 0.0127 667 PHE B C 12267 O O . PHE B 667 ? 1.2839 0.6302 1.8077 0.3268 -0.0156 0.0169 667 PHE B O 12268 C CB . PHE B 667 ? 1.2141 0.6332 1.6871 0.3378 -0.0557 0.0280 667 PHE B CB 12269 C CG . PHE B 667 ? 1.2188 0.6329 1.6906 0.3463 -0.0432 0.0580 667 PHE B CG 12270 C CD1 . PHE B 667 ? 1.4169 0.8291 1.9083 0.3441 -0.0275 0.0813 667 PHE B CD1 12271 C CD2 . PHE B 667 ? 1.2146 0.6293 1.6642 0.3560 -0.0479 0.0632 667 PHE B CD2 12272 C CE1 . PHE B 667 ? 1.2997 0.7110 1.7904 0.3555 -0.0183 0.1110 667 PHE B CE1 12273 C CE2 . PHE B 667 ? 1.2330 0.6531 1.6847 0.3661 -0.0375 0.0902 667 PHE B CE2 12274 C CZ . PHE B 667 ? 1.3041 0.7229 1.7772 0.3678 -0.0236 0.1150 667 PHE B CZ 12275 N N . GLN B 668 ? 1.2586 0.6497 1.7920 0.3110 -0.0240 0.0147 668 GLN B N 12276 C CA . GLN B 668 ? 1.2895 0.6574 1.8440 0.2980 -0.0025 0.0223 668 GLN B CA 12277 C C . GLN B 668 ? 1.5354 0.9178 2.0927 0.2943 0.0049 0.0502 668 GLN B C 12278 O O . GLN B 668 ? 1.5568 0.9759 2.1069 0.2948 -0.0064 0.0521 668 GLN B O 12279 C CB . GLN B 668 ? 1.3022 0.6738 1.8729 0.2771 -0.0004 -0.0097 668 GLN B CB 12280 C CG . GLN B 668 ? 1.3543 0.6901 1.9403 0.2585 0.0240 -0.0083 668 GLN B CG 12281 C CD . GLN B 668 ? 1.5395 0.8921 2.1404 0.2323 0.0261 -0.0413 668 GLN B CD 12282 O OE1 . GLN B 668 ? 1.5202 0.9215 2.1260 0.2294 0.0098 -0.0590 668 GLN B OE1 12283 N NE2 . GLN B 668 ? 1.9061 1.2191 2.5138 0.2133 0.0466 -0.0508 668 GLN B NE2 12284 N N . TYR B 669 ? 1.4693 0.8200 2.0346 0.2901 0.0244 0.0718 669 TYR B N 12285 C CA . TYR B 669 ? 1.5072 0.8677 2.0725 0.2830 0.0327 0.1004 669 TYR B CA 12286 C C . TYR B 669 ? 1.6796 1.0163 2.2577 0.2575 0.0511 0.0961 669 TYR B C 12287 O O . TYR B 669 ? 1.7554 1.0423 2.3370 0.2551 0.0663 0.0968 669 TYR B O 12288 C CB . TYR B 669 ? 1.7002 1.0455 2.2562 0.3030 0.0376 0.1389 669 TYR B CB 12289 C CG . TYR B 669 ? 2.0393 1.3872 2.5933 0.2949 0.0477 0.1727 669 TYR B CG 12290 C CD1 . TYR B 669 ? 2.1003 1.4950 2.6447 0.2904 0.0393 0.1853 669 TYR B CD1 12291 C CD2 . TYR B 669 ? 2.2091 1.5088 2.7670 0.2906 0.0662 0.1922 669 TYR B CD2 12292 C CE1 . TYR B 669 ? 2.1569 1.5568 2.6968 0.2801 0.0483 0.2163 669 TYR B CE1 12293 C CE2 . TYR B 669 ? 2.2763 1.5758 2.8276 0.2818 0.0744 0.2255 669 TYR B CE2 12294 C CZ . TYR B 669 ? 2.2717 1.6245 2.8145 0.2758 0.0649 0.2374 669 TYR B CZ 12295 O OH . TYR B 669 ? 2.2866 1.6421 2.8205 0.2641 0.0729 0.2706 669 TYR B OH 12296 N N . TYR B 670 ? 1.6739 1.0452 2.2572 0.2372 0.0512 0.0902 670 TYR B N 12297 C CA . TYR B 670 ? 1.6774 1.0350 2.2709 0.2066 0.0682 0.0791 670 TYR B CA 12298 C C . TYR B 670 ? 1.7338 1.1235 2.3267 0.1870 0.0734 0.0924 670 TYR B C 12299 O O . TYR B 670 ? 1.8013 1.2408 2.3932 0.1927 0.0605 0.0913 670 TYR B O 12300 C CB . TYR B 670 ? 1.7314 1.1095 2.3392 0.1935 0.0623 0.0343 670 TYR B CB 12301 C CG . TYR B 670 ? 1.9662 1.3602 2.5865 0.1577 0.0750 0.0140 670 TYR B CG 12302 C CD1 . TYR B 670 ? 2.1169 1.4605 2.7331 0.1334 0.0991 0.0217 670 TYR B CD1 12303 C CD2 . TYR B 670 ? 2.0645 1.5238 2.6997 0.1481 0.0635 -0.0146 670 TYR B CD2 12304 C CE1 . TYR B 670 ? 2.2064 1.5666 2.8307 0.0954 0.1122 0.0011 670 TYR B CE1 12305 C CE2 . TYR B 670 ? 2.1466 1.6304 2.7953 0.1138 0.0756 -0.0361 670 TYR B CE2 12306 C CZ . TYR B 670 ? 2.2902 1.7253 2.9323 0.0850 0.1003 -0.0287 670 TYR B CZ 12307 O OH . TYR B 670 ? 2.3955 1.8568 3.0477 0.0458 0.1138 -0.0517 670 TYR B OH 12308 N N . GLU B 671 ? 1.8921 1.2500 2.4826 0.1622 0.0937 0.1044 671 GLU B N 12309 C CA . GLU B 671 ? 2.0302 1.4158 2.6170 0.1380 0.1013 0.1172 671 GLU B CA 12310 C C . GLU B 671 ? 1.9719 1.3434 2.5627 0.0976 0.1208 0.1002 671 GLU B C 12311 O O . GLU B 671 ? 1.9102 1.2332 2.5008 0.0885 0.1324 0.0884 671 GLU B O 12312 C CB . GLU B 671 ? 2.0377 1.3983 2.6050 0.1485 0.1062 0.1668 671 GLU B CB 12313 C CG . GLU B 671 ? 2.0366 1.3225 2.5909 0.1397 0.1263 0.1922 671 GLU B CG 12314 C CD . GLU B 671 ? 2.1115 1.3411 2.6680 0.1627 0.1287 0.1878 671 GLU B CD 12315 O OE1 . GLU B 671 ? 2.1483 1.3109 2.6966 0.1515 0.1475 0.1941 671 GLU B OE1 12316 O OE2 . GLU B 671 ? 2.0188 1.2684 2.5828 0.1904 0.1131 0.1772 671 GLU B OE2 12317 N N . ASP B 672 ? 1.9951 1.4101 2.5876 0.0708 0.1258 0.0972 672 ASP B N 12318 C CA . ASP B 672 ? 2.0871 1.4970 2.6802 0.0265 0.1456 0.0811 672 ASP B CA 12319 C C . ASP B 672 ? 2.2129 1.5938 2.7818 0.0038 0.1621 0.1191 672 ASP B C 12320 O O . ASP B 672 ? 2.1780 1.6047 2.7439 -0.0010 0.1582 0.1318 672 ASP B O 12321 C CB . ASP B 672 ? 2.0548 1.5481 2.6724 0.0082 0.1394 0.0385 672 ASP B CB 12322 C CG . ASP B 672 ? 2.1169 1.6320 2.7561 0.0194 0.1272 -0.0023 672 ASP B CG 12323 O OD1 . ASP B 672 ? 2.1862 1.6467 2.8201 0.0216 0.1327 -0.0051 672 ASP B OD1 12324 O OD2 . ASP B 672 ? 2.0673 1.6535 2.7275 0.0263 0.1122 -0.0315 672 ASP B OD2 12325 N N . SER B 673 ? 2.4010 1.7034 2.9500 -0.0110 0.1810 0.1367 673 SER B N 12326 C CA . SER B 673 ? 2.5077 1.7673 3.0269 -0.0324 0.1970 0.1768 673 SER B CA 12327 C C . SER B 673 ? 2.5457 1.8155 3.0537 -0.0021 0.1843 0.2214 673 SER B C 12328 O O . SER B 673 ? 2.4872 1.7432 2.9989 0.0400 0.1712 0.2364 673 SER B O 12329 C CB . SER B 673 ? 2.5021 1.8052 3.0194 -0.0840 0.2101 0.1580 673 SER B CB 12330 O OG . SER B 673 ? 2.4870 1.7846 3.0127 -0.1165 0.2234 0.1171 673 SER B OG 12331 N N . SER B 674 ? 2.6221 1.9208 3.1157 -0.0264 0.1889 0.2410 674 SER B N 12332 C CA . SER B 674 ? 2.5622 1.8850 3.0444 -0.0047 0.1771 0.2803 674 SER B CA 12333 C C . SER B 674 ? 2.4639 1.8757 2.9681 0.0065 0.1598 0.2546 674 SER B C 12334 O O . SER B 674 ? 2.4957 1.9407 2.9916 0.0201 0.1499 0.2789 674 SER B O 12335 C CB . SER B 674 ? 2.5625 1.8725 3.0140 -0.0384 0.1903 0.3155 674 SER B CB 12336 O OG . SER B 674 ? 2.5305 1.8950 2.9874 -0.0834 0.1996 0.2850 674 SER B OG 12337 N N . GLY B 675 ? 2.3281 1.7772 2.8584 0.0006 0.1565 0.2053 675 GLY B N 12338 C CA . GLY B 675 ? 2.1546 1.6809 2.7048 0.0123 0.1411 0.1772 675 GLY B CA 12339 C C . GLY B 675 ? 2.1229 1.6506 2.6770 0.0579 0.1210 0.1817 675 GLY B C 12340 O O . GLY B 675 ? 2.1484 1.6274 2.6901 0.0817 0.1186 0.2120 675 GLY B O 12341 N N . LYS B 676 ? 2.0736 1.6572 2.6440 0.0700 0.1071 0.1503 676 LYS B N 12342 C CA . LYS B 676 ? 2.0126 1.6032 2.5808 0.1079 0.0881 0.1523 676 LYS B CA 12343 C C . LYS B 676 ? 1.9085 1.4546 2.4820 0.1325 0.0811 0.1446 676 LYS B C 12344 O O . LYS B 676 ? 1.8556 1.3786 2.4410 0.1208 0.0882 0.1236 676 LYS B O 12345 C CB . LYS B 676 ? 2.0109 1.6637 2.5917 0.1129 0.0764 0.1179 676 LYS B CB 12346 C CG . LYS B 676 ? 1.9878 1.6703 2.5952 0.0970 0.0788 0.0734 676 LYS B CG 12347 C CD . LYS B 676 ? 1.9299 1.6775 2.5499 0.1015 0.0700 0.0436 676 LYS B CD 12348 C CE . LYS B 676 ? 1.9535 1.7429 2.6035 0.0846 0.0734 0.0004 676 LYS B CE 12349 N NZ . LYS B 676 ? 1.9369 1.7915 2.6019 0.0923 0.0660 -0.0290 676 LYS B NZ 12350 N N . SER B 677 ? 1.8364 1.3737 2.3992 0.1634 0.0682 0.1601 677 SER B N 12351 C CA . SER B 677 ? 1.8696 1.3719 2.4357 0.1875 0.0605 0.1511 677 SER B CA 12352 C C . SER B 677 ? 1.8561 1.3908 2.4239 0.2068 0.0409 0.1239 677 SER B C 12353 O O . SER B 677 ? 1.7979 1.3648 2.3537 0.2144 0.0321 0.1301 677 SER B O 12354 C CB . SER B 677 ? 1.8648 1.3279 2.4160 0.2082 0.0622 0.1901 677 SER B CB 12355 O OG . SER B 677 ? 1.8702 1.3660 2.4061 0.2207 0.0527 0.2119 677 SER B OG 12356 N N . ILE B 678 ? 1.7344 1.2576 2.3136 0.2131 0.0344 0.0942 678 ILE B N 12357 C CA . ILE B 678 ? 1.5017 1.0513 2.0802 0.2299 0.0149 0.0671 678 ILE B CA 12358 C C . ILE B 678 ? 1.4390 0.9564 2.0079 0.2519 0.0050 0.0653 678 ILE B C 12359 O O . ILE B 678 ? 1.4852 0.9644 2.0599 0.2504 0.0136 0.0662 678 ILE B O 12360 C CB . ILE B 678 ? 1.3077 0.8894 1.9087 0.2170 0.0119 0.0275 678 ILE B CB 12361 C CG1 . ILE B 678 ? 1.3271 0.9302 1.9251 0.2386 -0.0105 0.0017 678 ILE B CG1 12362 C CG2 . ILE B 678 ? 1.3071 0.8607 1.9227 0.2001 0.0237 0.0148 678 ILE B CG2 12363 C CD1 . ILE B 678 ? 1.4193 1.0653 2.0412 0.2315 -0.0166 -0.0359 678 ILE B CD1 12364 N N . LEU B 679 ? 1.3417 0.8723 1.8930 0.2704 -0.0117 0.0622 679 LEU B N 12365 C CA . LEU B 679 ? 1.2348 0.7411 1.7733 0.2882 -0.0225 0.0565 679 LEU B CA 12366 C C . LEU B 679 ? 1.2418 0.7602 1.7819 0.2932 -0.0393 0.0212 679 LEU B C 12367 O O . LEU B 679 ? 1.2619 0.8068 1.7931 0.2995 -0.0521 0.0102 679 LEU B O 12368 C CB . LEU B 679 ? 1.1947 0.7036 1.7053 0.3028 -0.0294 0.0785 679 LEU B CB 12369 C CG . LEU B 679 ? 1.3788 0.8819 1.8849 0.3032 -0.0168 0.1162 679 LEU B CG 12370 C CD1 . LEU B 679 ? 1.1887 0.7054 1.6662 0.3149 -0.0256 0.1313 679 LEU B CD1 12371 C CD2 . LEU B 679 ? 1.6632 1.1272 2.1826 0.3072 -0.0048 0.1259 679 LEU B CD2 12372 N N . TYR B 680 ? 1.2231 0.7211 1.7730 0.2908 -0.0391 0.0037 680 TYR B N 12373 C CA . TYR B 680 ? 1.2050 0.7140 1.7526 0.2970 -0.0574 -0.0268 680 TYR B CA 12374 C C . TYR B 680 ? 1.2123 0.6968 1.7319 0.3126 -0.0693 -0.0240 680 TYR B C 12375 O O . TYR B 680 ? 1.3256 0.7804 1.8448 0.3118 -0.0609 -0.0196 680 TYR B O 12376 C CB . TYR B 680 ? 1.3219 0.8304 1.8941 0.2806 -0.0511 -0.0513 680 TYR B CB 12377 C CG . TYR B 680 ? 1.3964 0.9349 1.9948 0.2606 -0.0397 -0.0601 680 TYR B CG 12378 C CD1 . TYR B 680 ? 1.3619 0.9497 1.9732 0.2611 -0.0523 -0.0839 680 TYR B CD1 12379 C CD2 . TYR B 680 ? 1.5446 1.0622 2.1537 0.2411 -0.0161 -0.0451 680 TYR B CD2 12380 C CE1 . TYR B 680 ? 1.4281 1.0508 2.0647 0.2404 -0.0408 -0.0949 680 TYR B CE1 12381 C CE2 . TYR B 680 ? 1.5683 1.1132 2.1972 0.2178 -0.0045 -0.0542 680 TYR B CE2 12382 C CZ . TYR B 680 ? 1.6267 1.2279 2.2706 0.2163 -0.0165 -0.0803 680 TYR B CZ 12383 O OH . TYR B 680 ? 1.9104 1.5462 2.5752 0.1910 -0.0038 -0.0921 680 TYR B OH 12384 N N . VAL B 681 ? 1.3412 0.8361 1.8354 0.3257 -0.0876 -0.0276 681 VAL B N 12385 C CA . VAL B 681 ? 1.3785 0.8510 1.8398 0.3363 -0.0996 -0.0267 681 VAL B CA 12386 C C . VAL B 681 ? 1.2519 0.7244 1.7063 0.3398 -0.1184 -0.0545 681 VAL B C 12387 O O . VAL B 681 ? 1.2331 0.7286 1.6923 0.3445 -0.1313 -0.0701 681 VAL B O 12388 C CB . VAL B 681 ? 1.1806 0.6557 1.6074 0.3453 -0.1072 -0.0113 681 VAL B CB 12389 C CG1 . VAL B 681 ? 1.1877 0.6403 1.5751 0.3521 -0.1208 -0.0148 681 VAL B CG1 12390 C CG2 . VAL B 681 ? 1.1745 0.6542 1.6048 0.3411 -0.0900 0.0181 681 VAL B CG2 12391 N N . VAL B 682 ? 1.2488 0.6980 1.6920 0.3380 -0.1202 -0.0610 682 VAL B N 12392 C CA . VAL B 682 ? 1.2532 0.7028 1.6857 0.3390 -0.1389 -0.0857 682 VAL B CA 12393 C C . VAL B 682 ? 1.2231 0.6642 1.6109 0.3524 -0.1608 -0.0842 682 VAL B C 12394 O O . VAL B 682 ? 1.2956 0.7150 1.6511 0.3538 -0.1603 -0.0711 682 VAL B O 12395 C CB . VAL B 682 ? 1.2356 0.6628 1.6684 0.3291 -0.1319 -0.0952 682 VAL B CB 12396 C CG1 . VAL B 682 ? 1.2490 0.6775 1.6616 0.3288 -0.1538 -0.1181 682 VAL B CG1 12397 C CG2 . VAL B 682 ? 1.2440 0.6711 1.7166 0.3144 -0.1100 -0.1006 682 VAL B CG2 12398 N N . GLU B 683 ? 1.3535 0.8116 1.7382 0.3621 -0.1798 -0.0982 683 GLU B N 12399 C CA . GLU B 683 ? 1.2416 0.6828 1.5795 0.3764 -0.2015 -0.0974 683 GLU B CA 12400 C C . GLU B 683 ? 1.4200 0.8371 1.7255 0.3727 -0.2153 -0.1064 683 GLU B C 12401 O O . GLU B 683 ? 1.5303 0.9539 1.8562 0.3616 -0.2119 -0.1198 683 GLU B O 12402 C CB . GLU B 683 ? 1.2468 0.7122 1.5932 0.3926 -0.2181 -0.1102 683 GLU B CB 12403 C CG . GLU B 683 ? 1.2572 0.7469 1.6239 0.3941 -0.2331 -0.1339 683 GLU B CG 12404 C CD . GLU B 683 ? 1.5743 1.0843 1.9380 0.4176 -0.2562 -0.1456 683 GLU B CD 12405 O OE1 . GLU B 683 ? 1.2700 0.7783 1.6257 0.4314 -0.2556 -0.1381 683 GLU B OE1 12406 O OE2 . GLU B 683 ? 1.5378 1.0669 1.9069 0.4229 -0.2749 -0.1630 683 GLU B OE2 12407 N N . GLU B 684 ? 1.4219 0.8095 1.6736 0.3793 -0.2298 -0.0999 684 GLU B N 12408 C CA . GLU B 684 ? 1.6843 1.0456 1.8952 0.3727 -0.2430 -0.1064 684 GLU B CA 12409 C C . GLU B 684 ? 1.6240 0.9818 1.8476 0.3545 -0.2242 -0.1068 684 GLU B C 12410 O O . GLU B 684 ? 1.3831 0.7497 1.6276 0.3454 -0.2234 -0.1229 684 GLU B O 12411 C CB . GLU B 684 ? 1.5504 0.9226 1.7621 0.3796 -0.2665 -0.1257 684 GLU B CB 12412 C CG . GLU B 684 ? 1.6396 0.9767 1.7873 0.3840 -0.2917 -0.1262 684 GLU B CG 12413 C CD . GLU B 684 ? 2.1155 1.4685 2.2646 0.3937 -0.3175 -0.1426 684 GLU B CD 12414 O OE1 . GLU B 684 ? 2.1630 1.5571 2.3626 0.3889 -0.3131 -0.1574 684 GLU B OE1 12415 O OE2 . GLU B 684 ? 2.3623 1.6868 2.4599 0.4055 -0.3423 -0.1402 684 GLU B OE2 12416 N N . PRO B 685 ? 1.2886 0.6362 1.5004 0.3496 -0.2083 -0.0900 685 PRO B N 12417 C CA . PRO B 685 ? 1.2843 0.6287 1.5060 0.3373 -0.1900 -0.0891 685 PRO B CA 12418 C C . PRO B 685 ? 1.3092 0.6359 1.4959 0.3260 -0.2002 -0.1039 685 PRO B C 12419 O O . PRO B 685 ? 1.7871 1.1019 1.9389 0.3270 -0.2231 -0.1127 685 PRO B O 12420 C CB . PRO B 685 ? 1.2733 0.6167 1.4784 0.3381 -0.1783 -0.0672 685 PRO B CB 12421 C CG . PRO B 685 ? 1.2634 0.6156 1.4714 0.3483 -0.1820 -0.0565 685 PRO B CG 12422 C CD . PRO B 685 ? 1.2817 0.6258 1.4736 0.3560 -0.2053 -0.0714 685 PRO B CD 12423 N N . GLU B 686 ? 1.4434 0.7686 1.6385 0.3159 -0.1831 -0.1063 686 GLU B N 12424 C CA . GLU B 686 ? 1.5033 0.8155 1.6667 0.3014 -0.1890 -0.1222 686 GLU B CA 12425 C C . GLU B 686 ? 1.3410 0.6429 1.4560 0.2947 -0.1885 -0.1128 686 GLU B C 12426 O O . GLU B 686 ? 1.3478 0.6616 1.4768 0.2961 -0.1698 -0.1012 686 GLU B O 12427 C CB . GLU B 686 ? 1.4027 0.7202 1.6059 0.2929 -0.1688 -0.1370 686 GLU B CB 12428 C CG . GLU B 686 ? 1.6036 0.9305 1.8468 0.2917 -0.1690 -0.1512 686 GLU B CG 12429 C CD . GLU B 686 ? 1.9892 1.3134 2.2706 0.2821 -0.1443 -0.1649 686 GLU B CD 12430 O OE1 . GLU B 686 ? 2.0116 1.3290 2.3021 0.2848 -0.1242 -0.1575 686 GLU B OE1 12431 O OE2 . GLU B 686 ? 2.0894 1.4189 2.3913 0.2721 -0.1446 -0.1838 686 GLU B OE2 12432 N N . CYS B 687 ? 1.3795 0.6604 1.4355 0.2866 -0.2097 -0.1174 687 CYS B N 12433 C CA . CYS B 687 ? 1.4174 0.6855 1.4171 0.2747 -0.2107 -0.1104 687 CYS B CA 12434 C C . CYS B 687 ? 1.4800 0.7357 1.4400 0.2533 -0.2168 -0.1281 687 CYS B C 12435 O O . CYS B 687 ? 1.5265 0.7767 1.4889 0.2494 -0.2283 -0.1436 687 CYS B O 12436 C CB . CYS B 687 ? 1.4259 0.6700 1.3776 0.2807 -0.2287 -0.0977 687 CYS B CB 12437 S SG . CYS B 687 ? 1.8920 1.1532 1.8831 0.3011 -0.2196 -0.0783 687 CYS B SG 12438 N N . PRO B 688 ? 1.5976 0.8539 1.5205 0.2370 -0.2085 -0.1271 688 PRO B N 12439 C CA . PRO B 688 ? 1.7211 0.9670 1.6000 0.2125 -0.2133 -0.1448 688 PRO B CA 12440 C C . PRO B 688 ? 1.8885 1.0964 1.7053 0.2047 -0.2429 -0.1477 688 PRO B C 12441 O O . PRO B 688 ? 2.0836 1.2646 1.8579 0.2103 -0.2574 -0.1332 688 PRO B O 12442 C CB . PRO B 688 ? 1.9044 1.1614 1.7498 0.1973 -0.2005 -0.1394 688 PRO B CB 12443 C CG . PRO B 688 ? 1.8345 1.0952 1.6847 0.2121 -0.1980 -0.1165 688 PRO B CG 12444 C CD . PRO B 688 ? 1.6440 0.9171 1.5642 0.2380 -0.1937 -0.1108 688 PRO B CD 12445 N N . LYS B 689 ? 1.8700 1.0747 1.6803 0.1922 -0.2514 -0.1662 689 LYS B N 12446 C CA . LYS B 689 ? 1.9500 1.1224 1.7058 0.1877 -0.2818 -0.1680 689 LYS B CA 12447 C C . LYS B 689 ? 2.1006 1.2375 1.7666 0.1637 -0.2924 -0.1643 689 LYS B C 12448 O O . LYS B 689 ? 1.9928 1.1407 1.6419 0.1416 -0.2751 -0.1705 689 LYS B O 12449 C CB . LYS B 689 ? 2.0094 1.1960 1.7866 0.1782 -0.2868 -0.1893 689 LYS B CB 12450 C CG . LYS B 689 ? 2.1784 1.3487 1.9313 0.1868 -0.3192 -0.1885 689 LYS B CG 12451 C CD . LYS B 689 ? 2.2062 1.4041 1.9951 0.1776 -0.3200 -0.2105 689 LYS B CD 12452 C CE . LYS B 689 ? 2.2439 1.4389 2.0181 0.1900 -0.3532 -0.2090 689 LYS B CE 12453 N NZ . LYS B 689 ? 2.0210 1.2507 1.8326 0.1781 -0.3529 -0.2316 689 LYS B NZ 12454 N N . GLY B 690 ? 2.2406 1.3348 1.8479 0.1683 -0.3206 -0.1544 690 GLY B N 12455 C CA . GLY B 690 ? 2.0810 1.1290 1.5933 0.1448 -0.3323 -0.1486 690 GLY B CA 12456 C C . GLY B 690 ? 2.1005 1.1423 1.5679 0.1125 -0.3395 -0.1649 690 GLY B C 12457 O O . GLY B 690 ? 2.1561 1.1667 1.5455 0.0837 -0.3427 -0.1641 690 GLY B O 12458 N N . SER C 1 ? 2.4998 1.9643 2.8378 -0.9787 0.1824 -0.5045 1417 SER C N 12459 C CA . SER C 1 ? 2.5768 2.0364 3.0191 -0.9760 0.2246 -0.4782 1417 SER C CA 12460 C C . SER C 1 ? 2.5470 2.2689 3.0703 -0.8969 0.1367 -0.5654 1417 SER C C 12461 O O . SER C 1 ? 2.4957 2.0853 2.9662 -0.8149 0.0987 -0.6200 1417 SER C O 12462 C CB . SER C 1 ? 2.4031 1.9713 2.9885 -1.0800 0.3075 -0.3819 1417 SER C CB 12463 O OG . SER C 1 ? 2.2673 1.8421 2.9476 -1.0465 0.3323 -0.3553 1417 SER C OG 12464 N N . ASP C 2 ? 2.5094 2.6035 3.1590 -0.9194 0.1026 -0.5770 1418 ASP C N 12465 C CA . ASP C 2 ? 2.3628 2.7471 3.1029 -0.8436 0.0191 -0.6541 1418 ASP C CA 12466 C C . ASP C 2 ? 2.4824 2.9129 3.1122 -0.7494 -0.0954 -0.7697 1418 ASP C C 12467 O O . ASP C 2 ? 2.3303 2.9782 3.0114 -0.6712 -0.1801 -0.8464 1418 ASP C O 12468 C CB . ASP C 2 ? 2.1366 2.9051 3.0352 -0.8957 0.0256 -0.6252 1418 ASP C CB 12469 C CG . ASP C 2 ? 2.1127 2.9795 2.9939 -0.9736 0.0402 -0.5941 1418 ASP C CG 12470 O OD1 . ASP C 2 ? 2.2939 3.0125 3.0444 -0.9572 0.0071 -0.6317 1418 ASP C OD1 12471 O OD2 . ASP C 2 ? 1.9373 3.0250 2.9369 -1.0483 0.0823 -0.5335 1418 ASP C OD2 12472 N N . VAL C 3 ? 2.7671 2.9896 3.2415 -0.7505 -0.1035 -0.7866 1419 VAL C N 12473 C CA . VAL C 3 ? 2.8702 3.1378 3.2312 -0.6669 -0.2144 -0.9026 1419 VAL C CA 12474 C C . VAL C 3 ? 2.9967 2.8529 3.1469 -0.6136 -0.2219 -0.9326 1419 VAL C C 12475 O O . VAL C 3 ? 3.2062 2.7745 3.2811 -0.6631 -0.1379 -0.8569 1419 VAL C O 12476 C CB . VAL C 3 ? 2.9590 3.4645 3.3483 -0.7120 -0.2400 -0.9177 1419 VAL C CB 12477 C CG1 . VAL C 3 ? 3.0610 3.3634 3.4096 -0.8030 -0.1535 -0.8258 1419 VAL C CG1 12478 C CG2 . VAL C 3 ? 3.0032 3.5609 3.2807 -0.6245 -0.3583 -1.0487 1419 VAL C CG2 12479 N N . PRO C 4 ? 2.8733 2.6968 2.9210 -0.5076 -0.3247 -1.0437 1420 PRO C N 12480 C CA . PRO C 4 ? 3.0320 2.4811 2.8560 -0.4446 -0.3473 -1.0887 1420 PRO C CA 12481 C C . PRO C 4 ? 3.1540 2.5477 2.8618 -0.4525 -0.3693 -1.1197 1420 PRO C C 12482 O O . PRO C 4 ? 3.0516 2.7541 2.8513 -0.4802 -0.4086 -1.1485 1420 PRO C O 12483 C CB . PRO C 4 ? 3.0123 2.5292 2.7867 -0.3314 -0.4701 -1.2097 1420 PRO C CB 12484 C CG . PRO C 4 ? 2.7491 2.7302 2.7005 -0.3314 -0.5330 -1.2501 1420 PRO C CG 12485 C CD . PRO C 4 ? 2.6450 2.7616 2.7794 -0.4348 -0.4238 -1.1286 1420 PRO C CD 12486 N N . ARG C 5 ? 3.3794 2.3841 2.8910 -0.4239 -0.3448 -1.1149 1421 ARG C N 12487 C CA . ARG C 5 ? 3.4000 2.3137 2.8056 -0.4297 -0.3572 -1.1334 1421 ARG C CA 12488 C C . ARG C 5 ? 3.6842 2.3442 2.8511 -0.3177 -0.4434 -1.2469 1421 ARG C C 12489 O O . ARG C 5 ? 3.7395 2.1605 2.7921 -0.2573 -0.4187 -1.2343 1421 ARG C O 12490 C CB . ARG C 5 ? 3.3690 2.0424 2.7592 -0.5090 -0.2351 -1.0042 1421 ARG C CB 12491 C CG . ARG C 5 ? 3.1715 2.0342 2.7726 -0.6194 -0.1433 -0.8884 1421 ARG C CG 12492 C CD . ARG C 5 ? 3.2657 1.8935 2.8388 -0.6942 -0.0363 -0.7711 1421 ARG C CD 12493 N NE . ARG C 5 ? 3.5146 1.7105 2.9054 -0.6476 0.0146 -0.7451 1421 ARG C NE 12494 C CZ . ARG C 5 ? 3.7235 1.6273 2.9162 -0.5971 0.0051 -0.7639 1421 ARG C CZ 12495 N NH1 . ARG C 5 ? 3.6421 1.6387 2.8038 -0.5864 -0.0597 -0.8148 1421 ARG C NH1 12496 N NH2 . ARG C 5 ? 3.8143 1.5136 2.9470 -0.5089 0.0450 -0.6904 1421 ARG C NH2 12497 N N . ASP C 6 ? 2.5452 2.8365 1.5038 -0.2478 -0.3398 0.4715 1422 ASP C N 12498 C CA . ASP C 6 ? 2.8226 2.9281 1.6631 -0.3050 -0.4610 0.5177 1422 ASP C CA 12499 C C . ASP C 6 ? 2.7201 2.9263 1.6919 -0.3249 -0.4295 0.5429 1422 ASP C C 12500 O O . ASP C 6 ? 2.9276 2.9990 1.6863 -0.3230 -0.4055 0.5496 1422 ASP C O 12501 C CB . ASP C 6 ? 3.2562 3.0492 1.6826 -0.2965 -0.4852 0.5100 1422 ASP C CB 12502 C CG . ASP C 6 ? 3.3031 3.0875 1.5525 -0.2255 -0.3243 0.4633 1422 ASP C CG 12503 O OD1 . ASP C 6 ? 3.3670 3.1379 1.5423 -0.2302 -0.2766 0.4706 1422 ASP C OD1 12504 O OD2 . ASP C 6 ? 3.2554 3.0462 1.4396 -0.1649 -0.2465 0.4225 1422 ASP C OD2 12505 N N . LEU C 7 ? 2.3028 2.7361 1.6193 -0.3475 -0.4282 0.5560 1423 LEU C N 12506 C CA . LEU C 7 ? 2.1771 2.6836 1.6303 -0.3706 -0.4105 0.5845 1423 LEU C CA 12507 C C . LEU C 7 ? 2.2604 2.5800 1.6404 -0.4245 -0.5732 0.6528 1423 LEU C C 12508 O O . LEU C 7 ? 2.1476 2.4379 1.6098 -0.4606 -0.7015 0.6846 1423 LEU C O 12509 C CB . LEU C 7 ? 1.8534 2.6474 1.6940 -0.3801 -0.3503 0.5730 1423 LEU C CB 12510 C CG . LEU C 7 ? 1.6993 2.5817 1.8262 -0.4257 -0.4595 0.6073 1423 LEU C CG 12511 C CD1 . LEU C 7 ? 1.2596 2.4181 1.7325 -0.4327 -0.3581 0.5822 1423 LEU C CD1 12512 C CD2 . LEU C 7 ? 1.7303 2.5699 1.8311 -0.4366 -0.5516 0.6045 1423 LEU C CD2 12513 N N . GLU C 8 ? 2.3387 2.5316 1.5527 -0.4348 -0.5716 0.6796 1424 GLU C N 12514 C CA . GLU C 8 ? 2.6873 2.6940 1.8022 -0.4899 -0.7283 0.7534 1424 GLU C CA 12515 C C . GLU C 8 ? 2.7070 2.7366 1.9065 -0.5058 -0.7136 0.7964 1424 GLU C C 12516 O O . GLU C 8 ? 2.6366 2.6882 1.7495 -0.4810 -0.5895 0.7663 1424 GLU C O 12517 C CB . GLU C 8 ? 3.1026 2.8260 1.8001 -0.5036 -0.7819 0.7529 1424 GLU C CB 12518 C CG . GLU C 8 ? 3.1088 2.7586 1.6933 -0.4954 -0.8164 0.7187 1424 GLU C CG 12519 C CD . GLU C 8 ? 3.4604 2.8238 1.6779 -0.5043 -0.8444 0.6950 1424 GLU C CD 12520 O OE1 . GLU C 8 ? 3.6008 2.8264 1.6961 -0.5375 -0.8836 0.7187 1424 GLU C OE1 12521 O OE2 . GLU C 8 ? 3.5219 2.8107 1.6089 -0.4738 -0.8114 0.6423 1424 GLU C OE2 12522 N N . VAL C 9 ? 2.7707 2.7977 2.1452 -0.5472 -0.8411 0.8703 1425 VAL C N 12523 C CA . VAL C 9 ? 2.7139 2.7350 2.1720 -0.5639 -0.8495 0.9257 1425 VAL C CA 12524 C C . VAL C 9 ? 3.0756 2.8630 2.1606 -0.5857 -0.8670 0.9486 1425 VAL C C 12525 O O . VAL C 9 ? 3.4316 3.0178 2.2481 -0.6202 -0.9732 0.9727 1425 VAL C O 12526 C CB . VAL C 9 ? 2.7285 2.7709 2.4314 -0.6010 -1.0026 1.0134 1425 VAL C CB 12527 C CG1 . VAL C 9 ? 2.7792 2.8245 2.5998 -0.6081 -0.9985 1.0717 1425 VAL C CG1 12528 C CG2 . VAL C 9 ? 2.3513 2.6167 2.4059 -0.5866 -0.9905 0.9871 1425 VAL C CG2 12529 N N . VAL C 10 ? 2.9394 2.7504 1.9976 -0.5735 -0.7604 0.9390 1426 VAL C N 12530 C CA . VAL C 10 ? 3.2402 2.8465 1.9425 -0.5967 -0.7566 0.9527 1426 VAL C CA 12531 C C . VAL C 10 ? 3.4635 2.9624 2.1743 -0.6469 -0.8673 1.0513 1426 VAL C C 12532 O O . VAL C 10 ? 3.7328 3.0387 2.2429 -0.6935 -0.9939 1.0988 1426 VAL C O 12533 C CB . VAL C 10 ? 3.1396 2.8255 1.7549 -0.5581 -0.5657 0.8808 1426 VAL C CB 12534 C CG1 . VAL C 10 ? 3.5318 3.0067 1.7722 -0.5873 -0.5601 0.8931 1426 VAL C CG1 12535 C CG2 . VAL C 10 ? 2.9235 2.7221 1.5337 -0.5048 -0.4576 0.7935 1426 VAL C CG2 12536 N N . ALA C 11 ? 3.3026 2.9311 2.2638 -0.6348 -0.8071 1.0690 1427 ALA C N 12537 C CA . ALA C 11 ? 3.5021 3.0325 2.4832 -0.6740 -0.8946 1.1645 1427 ALA C CA 12538 C C . ALA C 11 ? 3.5483 3.1316 2.8379 -0.6860 -1.0381 1.2490 1427 ALA C C 12539 O O . ALA C 11 ? 3.2342 3.0132 2.8749 -0.6517 -0.9894 1.2292 1427 ALA C O 12540 C CB . ALA C 11 ? 3.2940 2.9097 2.3624 -0.6574 -0.7521 1.1432 1427 ALA C CB 12541 N N . ALA C 12 ? 3.8740 3.2941 3.0427 -0.7353 -1.2032 1.3311 1428 ALA C N 12542 C CA . ALA C 12 ? 3.8391 3.3184 3.3146 -0.7443 -1.3241 1.3996 1428 ALA C CA 12543 C C . ALA C 12 ? 3.8658 3.3553 3.5029 -0.7403 -1.3190 1.4796 1428 ALA C C 12544 O O . ALA C 12 ? 4.1172 3.4635 3.5462 -0.7688 -1.3245 1.4991 1428 ALA C O 12545 C CB . ALA C 12 ? 4.0110 3.3526 3.3438 -0.7948 -1.4453 1.4006 1428 ALA C CB 12546 N N . THR C 13 ? 3.5905 3.2535 3.6150 -0.7022 -1.2929 1.5073 1429 THR C N 12547 C CA . THR C 13 ? 3.4292 3.1314 3.6393 -0.6803 -1.2126 1.5308 1429 THR C CA 12548 C C . THR C 13 ? 3.0156 2.9291 3.6867 -0.6344 -1.1712 1.5203 1429 THR C C 12549 O O . THR C 13 ? 2.7155 2.7732 3.5220 -0.6159 -1.1408 1.4551 1429 THR C O 12550 C CB . THR C 13 ? 3.2210 2.9227 3.2390 -0.6698 -1.0219 1.4345 1429 THR C CB 12551 O OG1 . THR C 13 ? 3.5117 3.0131 3.1072 -0.7137 -1.0567 1.4478 1429 THR C OG1 12552 C CG2 . THR C 13 ? 3.1075 2.8549 3.3179 -0.6528 -0.9215 1.4459 1429 THR C CG2 12553 N N . PRO C 14 ? 3.0013 2.9278 3.9127 -0.6174 -1.1672 1.5844 1430 PRO C N 12554 C CA . PRO C 14 ? 2.8041 2.9226 4.1355 -0.5712 -1.0727 1.5518 1430 PRO C CA 12555 C C . PRO C 14 ? 2.8223 3.0725 4.1601 -0.5536 -0.8606 1.4132 1430 PRO C C 12556 O O . PRO C 14 ? 2.9284 3.1422 3.9685 -0.5692 -0.8001 1.3457 1430 PRO C O 12557 C CB . PRO C 14 ? 2.8368 2.8757 4.3143 -0.5610 -1.0958 1.6475 1430 PRO C CB 12558 C CG . PRO C 14 ? 3.1151 2.9285 4.2143 -0.6071 -1.1780 1.7156 1430 PRO C CG 12559 C CD . PRO C 14 ? 3.2163 2.9681 4.0395 -0.6445 -1.2855 1.7108 1430 PRO C CD 12560 N N . THR C 15 ? 2.7595 3.1642 4.4331 -0.5240 -0.7473 1.3725 1431 THR C N 12561 C CA . THR C 15 ? 2.6246 3.1884 4.3443 -0.5174 -0.5567 1.2437 1431 THR C CA 12562 C C . THR C 15 ? 2.7798 3.2627 4.1933 -0.5374 -0.4409 1.1968 1431 THR C C 12563 O O . THR C 15 ? 3.0606 3.3719 4.2962 -0.5535 -0.4858 1.2631 1431 THR C O 12564 C CB . THR C 15 ? 2.4143 3.1282 4.5284 -0.4947 -0.4486 1.2138 1431 THR C CB 12565 O OG1 . THR C 15 ? 2.1636 3.0457 4.3133 -0.5020 -0.2754 1.0902 1431 THR C OG1 12566 C CG2 . THR C 15 ? 2.5394 3.1402 4.6994 -0.4906 -0.4098 1.2664 1431 THR C CG2 12567 N N . SER C 16 ? 2.9813 2.0175 2.3020 -0.4908 -0.4528 0.6625 1432 SER C N 12568 C CA . SER C 16 ? 2.8809 1.8403 2.0882 -0.4846 -0.4243 0.6087 1432 SER C CA 12569 C C . SER C 16 ? 2.8617 1.6866 1.9553 -0.5112 -0.4592 0.6069 1432 SER C C 12570 O O . SER C 16 ? 2.9188 1.6525 1.8933 -0.5217 -0.4512 0.5663 1432 SER C O 12571 C CB . SER C 16 ? 2.9479 1.9071 2.1226 -0.4994 -0.4036 0.5700 1432 SER C CB 12572 O OG . SER C 16 ? 2.8699 1.9425 2.1460 -0.4715 -0.3893 0.5703 1432 SER C OG 12573 N N . LEU C 17 ? 2.7959 1.6480 1.9526 -0.5032 -0.4924 0.6347 1433 LEU C N 12574 C CA . LEU C 17 ? 2.8588 1.6101 1.9351 -0.5110 -0.5361 0.6238 1433 LEU C CA 12575 C C . LEU C 17 ? 2.8058 1.4908 1.7817 -0.4835 -0.5136 0.5965 1433 LEU C C 12576 O O . LEU C 17 ? 2.6232 1.4182 1.6703 -0.4408 -0.4532 0.5690 1433 LEU C O 12577 C CB . LEU C 17 ? 2.8062 1.6286 2.0046 -0.5102 -0.5818 0.6683 1433 LEU C CB 12578 C CG . LEU C 17 ? 2.5356 1.4921 1.8633 -0.4727 -0.5555 0.7089 1433 LEU C CG 12579 C CD1 . LEU C 17 ? 2.3715 1.3014 1.6740 -0.4540 -0.5734 0.7060 1433 LEU C CD1 12580 C CD2 . LEU C 17 ? 2.4397 1.5109 1.9161 -0.4736 -0.5720 0.7625 1433 LEU C CD2 12581 N N . LEU C 18 ? 2.8734 1.4292 1.7201 -0.4861 -0.5503 0.5706 1434 LEU C N 12582 C CA . LEU C 18 ? 2.8042 1.3396 1.5753 -0.4428 -0.5126 0.5067 1434 LEU C CA 12583 C C . LEU C 18 ? 2.9286 1.3877 1.6591 -0.4408 -0.5834 0.5200 1434 LEU C C 12584 O O . LEU C 18 ? 3.1292 1.5152 1.8374 -0.4663 -0.6633 0.5462 1434 LEU C O 12585 C CB . LEU C 18 ? 2.8564 1.3061 1.4785 -0.4309 -0.4773 0.4489 1434 LEU C CB 12586 C CG . LEU C 18 ? 2.8675 1.3307 1.4292 -0.3776 -0.4103 0.3778 1434 LEU C CG 12587 C CD1 . LEU C 18 ? 2.9172 1.3990 1.4330 -0.3642 -0.3427 0.3478 1434 LEU C CD1 12588 C CD2 . LEU C 18 ? 2.9633 1.2877 1.3752 -0.3599 -0.4602 0.3523 1434 LEU C CD2 12589 N N . ILE C 19 ? 2.9043 1.4248 1.6655 -0.4026 -0.5482 0.4800 1435 ILE C N 12590 C CA . ILE C 19 ? 3.0254 1.4839 1.7519 -0.3988 -0.6169 0.4833 1435 ILE C CA 12591 C C . ILE C 19 ? 2.9364 1.3608 1.5630 -0.3553 -0.5725 0.3949 1435 ILE C C 12592 O O . ILE C 19 ? 2.8132 1.3068 1.4532 -0.3251 -0.4773 0.3433 1435 ILE C O 12593 C CB . ILE C 19 ? 2.8759 1.4606 1.7722 -0.4007 -0.6353 0.5406 1435 ILE C CB 12594 C CG1 . ILE C 19 ? 2.6397 1.3679 1.6305 -0.3576 -0.5341 0.4943 1435 ILE C CG1 12595 C CG2 . ILE C 19 ? 2.8539 1.5205 1.8835 -0.4293 -0.6641 0.6186 1435 ILE C CG2 12596 C CD1 . ILE C 19 ? 2.3819 1.2367 1.5267 -0.3467 -0.5423 0.5464 1435 ILE C CD1 12597 N N . SER C 20 ? 2.9890 1.3031 1.5183 -0.3511 -0.6488 0.3825 1436 SER C N 12598 C CA . SER C 20 ? 3.0590 1.3331 1.4858 -0.3075 -0.6148 0.3002 1436 SER C CA 12599 C C . SER C 20 ? 3.1585 1.4025 1.5903 -0.3075 -0.6966 0.2993 1436 SER C C 12600 O O . SER C 20 ? 3.2662 1.4158 1.6659 -0.3339 -0.8167 0.3510 1436 SER C O 12601 C CB . SER C 20 ? 3.2128 1.3361 1.4310 -0.2835 -0.6181 0.2600 1436 SER C CB 12602 O OG . SER C 20 ? 3.2955 1.3892 1.4137 -0.2329 -0.5764 0.1848 1436 SER C OG 12603 N N . TRP C 21 ? 3.1317 1.4518 1.6089 -0.2803 -0.6386 0.2438 1437 TRP C N 12604 C CA . TRP C 21 ? 3.1560 1.4541 1.6357 -0.2795 -0.7101 0.2294 1437 TRP C CA 12605 C C . TRP C 21 ? 3.2551 1.4619 1.5757 -0.2353 -0.6870 0.1378 1437 TRP C C 12606 O O . TRP C 21 ? 3.2367 1.4104 1.4572 -0.2033 -0.6101 0.0970 1437 TRP C O 12607 C CB . TRP C 21 ? 3.0877 1.5505 1.7607 -0.2860 -0.6702 0.2440 1437 TRP C CB 12608 C CG . TRP C 21 ? 3.0773 1.6445 1.8157 -0.2576 -0.5357 0.1979 1437 TRP C CG 12609 C CD1 . TRP C 21 ? 3.1238 1.7092 1.8505 -0.2269 -0.4664 0.1217 1437 TRP C CD1 12610 C CD2 . TRP C 21 ? 3.0345 1.6917 1.8616 -0.2567 -0.4659 0.2293 1437 TRP C CD2 12611 N NE1 . TRP C 21 ? 3.0247 1.6994 1.8311 -0.2077 -0.3632 0.1095 1437 TRP C NE1 12612 C CE2 . TRP C 21 ? 2.9895 1.7093 1.8541 -0.2234 -0.3642 0.1721 1437 TRP C CE2 12613 C CE3 . TRP C 21 ? 3.0551 1.7406 1.9344 -0.2808 -0.4864 0.3019 1437 TRP C CE3 12614 C CZ2 . TRP C 21 ? 2.8435 1.6465 1.7900 -0.2105 -0.2933 0.1849 1437 TRP C CZ2 12615 C CZ3 . TRP C 21 ? 2.8776 1.6540 1.8352 -0.2677 -0.4084 0.3084 1437 TRP C CZ3 12616 C CH2 . TRP C 21 ? 2.7583 1.5898 1.7462 -0.2314 -0.3180 0.2501 1437 TRP C CH2 12617 N N . ASP C 22 ? 3.3398 1.5122 1.6400 -0.2313 -0.7542 0.1099 1438 ASP C N 12618 C CA . ASP C 22 ? 3.4853 1.5506 1.6119 -0.1846 -0.7505 0.0268 1438 ASP C CA 12619 C C . ASP C 22 ? 3.5244 1.6506 1.7068 -0.1730 -0.7227 -0.0345 1438 ASP C C 12620 O O . ASP C 22 ? 3.7204 1.8611 1.9714 -0.1999 -0.8120 -0.0193 1438 ASP C O 12621 C CB . ASP C 22 ? 3.6292 1.5058 1.5797 -0.1786 -0.8989 0.0386 1438 ASP C CB 12622 C CG . ASP C 22 ? 3.7808 1.5263 1.5105 -0.1127 -0.8927 -0.0445 1438 ASP C CG 12623 O OD1 . ASP C 22 ? 3.7291 1.5005 1.5075 -0.0905 -0.8992 -0.0820 1438 ASP C OD1 12624 O OD2 . ASP C 22 ? 3.9013 1.5645 1.4815 -0.0739 -0.8508 -0.0572 1438 ASP C OD2 12625 N N . ALA C 23 ? 3.4555 1.6205 1.6184 -0.1356 -0.5999 -0.0964 1439 ALA C N 12626 C CA . ALA C 23 ? 3.5695 1.7256 1.6963 -0.1070 -0.5722 -0.1741 1439 ALA C CA 12627 C C . ALA C 23 ? 3.4744 1.6667 1.6984 -0.1383 -0.6471 -0.1860 1439 ALA C C 12628 O O . ALA C 23 ? 3.6314 1.7760 1.8116 -0.1212 -0.7219 -0.1958 1439 ALA C O 12629 C CB . ALA C 23 ? 3.9085 1.9083 1.7959 -0.0519 -0.6041 -0.2217 1439 ALA C CB 12630 N N . PRO C 24 ? 3.0346 1.3674 1.4582 -0.1704 -0.6046 -0.1610 1440 PRO C N 12631 C CA . PRO C 24 ? 2.9109 1.2894 1.4274 -0.1938 -0.6522 -0.1843 1440 PRO C CA 12632 C C . PRO C 24 ? 2.9182 1.3213 1.4261 -0.1524 -0.5779 -0.2558 1440 PRO C C 12633 O O . PRO C 24 ? 2.7874 1.1991 1.2789 -0.1282 -0.4669 -0.2962 1440 PRO C O 12634 C CB . PRO C 24 ? 2.6709 1.2038 1.3935 -0.2146 -0.5831 -0.1446 1440 PRO C CB 12635 C CG . PRO C 24 ? 2.8359 1.3937 1.5758 -0.2155 -0.5576 -0.0760 1440 PRO C CG 12636 C CD . PRO C 24 ? 2.9675 1.4152 1.5320 -0.1841 -0.5296 -0.1061 1440 PRO C CD 12637 N N . ALA C 25 ? 3.0361 1.4701 1.5827 -0.1430 -0.6330 -0.2572 1441 ALA C N 12638 C CA . ALA C 25 ? 3.0589 1.5320 1.6084 -0.1047 -0.5708 -0.3126 1441 ALA C CA 12639 C C . ALA C 25 ? 2.8751 1.4763 1.5797 -0.1154 -0.4693 -0.3478 1441 ALA C C 12640 O O . ALA C 25 ? 2.8993 1.5357 1.6133 -0.0884 -0.3942 -0.3912 1441 ALA C O 12641 C CB . ALA C 25 ? 3.0607 1.5328 1.6227 -0.0963 -0.6597 -0.3007 1441 ALA C CB 12642 N N . VAL C 26 ? 2.6333 1.3028 1.4646 -0.1528 -0.4708 -0.3237 1442 VAL C N 12643 C CA . VAL C 26 ? 2.4359 1.2178 1.4194 -0.1576 -0.3782 -0.3513 1442 VAL C CA 12644 C C . VAL C 26 ? 2.4760 1.2202 1.4262 -0.1393 -0.2819 -0.3666 1442 VAL C C 12645 O O . VAL C 26 ? 2.6531 1.2903 1.4590 -0.1270 -0.2839 -0.3564 1442 VAL C O 12646 C CB . VAL C 26 ? 2.5237 1.3840 1.6443 -0.1928 -0.4126 -0.3161 1442 VAL C CB 12647 C CG1 . VAL C 26 ? 2.3827 1.1909 1.4866 -0.2083 -0.4079 -0.2842 1442 VAL C CG1 12648 C CG2 . VAL C 26 ? 2.3295 1.3238 1.6152 -0.1913 -0.3402 -0.3469 1442 VAL C CG2 12649 N N . THR C 27 ? 2.2490 1.0823 1.3377 -0.1348 -0.2001 -0.3848 1443 THR C N 12650 C CA . THR C 27 ? 2.4062 1.2128 1.4930 -0.1152 -0.1142 -0.3847 1443 THR C CA 12651 C C . THR C 27 ? 2.3633 1.1555 1.4906 -0.1311 -0.1146 -0.3509 1443 THR C C 12652 O O . THR C 27 ? 2.3355 1.2065 1.5916 -0.1433 -0.1243 -0.3426 1443 THR C O 12653 C CB . THR C 27 ? 2.3341 1.2402 1.5619 -0.0965 -0.0439 -0.4083 1443 THR C CB 12654 O OG1 . THR C 27 ? 2.2121 1.1325 1.4083 -0.0829 -0.0485 -0.4385 1443 THR C OG1 12655 C CG2 . THR C 27 ? 1.9907 0.8587 1.2094 -0.0742 0.0324 -0.3934 1443 THR C CG2 12656 N N . VAL C 28 ? 2.2200 1.2683 1.2431 -0.3892 -0.5171 0.0148 1444 VAL C N 12657 C CA . VAL C 28 ? 1.9973 1.0254 1.0339 -0.4161 -0.5395 0.0596 1444 VAL C CA 12658 C C . VAL C 28 ? 2.1164 1.1168 1.1308 -0.4157 -0.5078 0.0675 1444 VAL C C 12659 O O . VAL C 28 ? 2.2157 1.2031 1.1707 -0.4138 -0.4972 0.0616 1444 VAL C O 12660 C CB . VAL C 28 ? 2.1273 1.1626 1.1459 -0.4438 -0.5984 0.0952 1444 VAL C CB 12661 C CG1 . VAL C 28 ? 2.2895 1.3468 1.3523 -0.4512 -0.6328 0.1011 1444 VAL C CG1 12662 C CG2 . VAL C 28 ? 2.2165 1.2587 1.1685 -0.4368 -0.6013 0.0816 1444 VAL C CG2 12663 N N . ARG C 29 ? 2.2225 1.2212 1.2901 -0.4150 -0.4887 0.0797 1445 ARG C N 12664 C CA . ARG C 29 ? 2.0595 1.0350 1.1280 -0.4110 -0.4532 0.0874 1445 ARG C CA 12665 C C . ARG C 29 ? 2.0850 1.0498 1.1570 -0.4379 -0.4849 0.1393 1445 ARG C C 12666 O O . ARG C 29 ? 2.0248 0.9941 1.0710 -0.4205 -0.4558 0.1559 1445 ARG C O 12667 C CB . ARG C 29 ? 1.9337 0.9470 1.0959 -0.3859 -0.4072 0.0811 1445 ARG C CB 12668 C CG . ARG C 29 ? 1.9746 0.9918 1.1775 -0.3641 -0.3521 0.0871 1445 ARG C CG 12669 C CD . ARG C 29 ? 1.7886 0.8668 1.1038 -0.3377 -0.3102 0.0819 1445 ARG C CD 12670 N NE . ARG C 29 ? 1.4201 0.5214 0.7870 -0.3023 -0.2463 0.0756 1445 ARG C NE 12671 C CZ . ARG C 29 ? 1.7768 0.9338 1.2472 -0.2758 -0.2033 0.0728 1445 ARG C CZ 12672 N NH1 . ARG C 29 ? 1.9362 1.1195 1.4576 -0.2419 -0.1494 0.0679 1445 ARG C NH1 12673 N NH2 . ARG C 29 ? 1.5896 0.7778 1.1131 -0.2841 -0.2153 0.0757 1445 ARG C NH2 12674 N N . TYR C 30 ? 2.2083 1.2133 1.3482 -0.4516 -0.5212 0.1772 1446 TYR C N 12675 C CA . TYR C 30 ? 2.1780 1.2353 1.3787 -0.4430 -0.5267 0.2401 1446 TYR C CA 12676 C C . TYR C 30 ? 2.0373 1.1325 1.2645 -0.4658 -0.5912 0.2667 1446 TYR C C 12677 O O . TYR C 30 ? 2.2574 1.3416 1.4756 -0.4889 -0.6264 0.2410 1446 TYR C O 12678 C CB . TYR C 30 ? 2.1980 1.2763 1.5052 -0.4236 -0.4784 0.2657 1446 TYR C CB 12679 C CG . TYR C 30 ? 2.1463 1.2010 1.4435 -0.3950 -0.4176 0.2618 1446 TYR C CG 12680 C CD1 . TYR C 30 ? 2.2531 1.3027 1.4863 -0.3848 -0.4124 0.2757 1446 TYR C CD1 12681 C CD2 . TYR C 30 ? 1.9309 1.0061 1.2985 -0.3667 -0.3590 0.2343 1446 TYR C CD2 12682 C CE1 . TYR C 30 ? 2.1606 1.1891 1.3861 -0.3610 -0.3581 0.2741 1446 TYR C CE1 12683 C CE2 . TYR C 30 ? 1.9905 1.0695 1.3658 -0.3324 -0.3009 0.2235 1446 TYR C CE2 12684 C CZ . TYR C 30 ? 2.0017 1.0533 1.3071 -0.3320 -0.3017 0.2434 1446 TYR C CZ 12685 O OH . TYR C 30 ? 2.0092 1.0684 1.3273 -0.2999 -0.2456 0.2330 1446 TYR C OH 12686 N N . TYR C 31 ? 1.9463 1.0836 1.2064 -0.4596 -0.6093 0.3182 1447 TYR C N 12687 C CA . TYR C 31 ? 1.9512 1.1314 1.2573 -0.4776 -0.6665 0.3493 1447 TYR C CA 12688 C C . TYR C 31 ? 1.9100 1.1441 1.3342 -0.4640 -0.6527 0.3982 1447 TYR C C 12689 O O . TYR C 31 ? 2.2078 1.4493 1.6484 -0.4399 -0.6233 0.4244 1447 TYR C O 12690 C CB . TYR C 31 ? 2.3737 1.5540 1.5998 -0.4849 -0.7173 0.3618 1447 TYR C CB 12691 C CG . TYR C 31 ? 2.4497 1.5878 1.5658 -0.5000 -0.7444 0.3122 1447 TYR C CG 12692 C CD1 . TYR C 31 ? 2.3315 1.4709 1.4669 -0.5168 -0.7722 0.2864 1447 TYR C CD1 12693 C CD2 . TYR C 31 ? 2.4433 1.5507 1.4643 -0.4889 -0.7205 0.2861 1447 TYR C CD2 12694 C CE1 . TYR C 31 ? 2.3028 1.4200 1.3869 -0.5082 -0.7597 0.2384 1447 TYR C CE1 12695 C CE2 . TYR C 31 ? 2.3323 1.4236 1.3048 -0.4859 -0.7116 0.2320 1447 TYR C CE2 12696 C CZ . TYR C 31 ? 2.3410 1.4383 1.3482 -0.4916 -0.7304 0.2108 1447 TYR C CZ 12697 O OH . TYR C 31 ? 2.2593 1.3507 1.2306 -0.4772 -0.7177 0.1650 1447 TYR C OH 12698 N N . ARG C 32 ? 1.7621 1.0355 1.2691 -0.4800 -0.6757 0.4092 1448 ARG C N 12699 C CA . ARG C 32 ? 1.7424 1.0756 1.3703 -0.4678 -0.6640 0.4489 1448 ARG C CA 12700 C C . ARG C 32 ? 1.9680 1.3522 1.6390 -0.4814 -0.7248 0.4842 1448 ARG C C 12701 O O . ARG C 32 ? 2.1187 1.5153 1.7981 -0.5094 -0.7648 0.4758 1448 ARG C O 12702 C CB . ARG C 32 ? 1.6378 0.9844 1.3423 -0.4733 -0.6293 0.4317 1448 ARG C CB 12703 C CG . ARG C 32 ? 1.5862 1.0051 1.4219 -0.4642 -0.6204 0.4663 1448 ARG C CG 12704 C CD . ARG C 32 ? 1.5122 0.9387 1.4104 -0.4669 -0.5757 0.4461 1448 ARG C CD 12705 N NE . ARG C 32 ? 1.6868 1.1927 1.7074 -0.4716 -0.5807 0.4718 1448 ARG C NE 12706 C CZ . ARG C 32 ? 1.7485 1.2876 1.8060 -0.5060 -0.6104 0.4695 1448 ARG C CZ 12707 N NH1 . ARG C 32 ? 1.6155 1.1092 1.5959 -0.5379 -0.6412 0.4435 1448 ARG C NH1 12708 N NH2 . ARG C 32 ? 1.8570 1.4762 2.0294 -0.5091 -0.6107 0.4921 1448 ARG C NH2 12709 N N . ILE C 33 ? 1.8538 1.2646 1.5523 -0.4618 -0.7342 0.5236 1449 ILE C N 12710 C CA . ILE C 33 ? 1.9722 1.4272 1.7088 -0.4708 -0.7939 0.5574 1449 ILE C CA 12711 C C . ILE C 33 ? 1.8147 1.3413 1.6914 -0.4605 -0.7883 0.5856 1449 ILE C C 12712 O O . ILE C 33 ? 1.7906 1.3306 1.7196 -0.4325 -0.7488 0.5990 1449 ILE C O 12713 C CB . ILE C 33 ? 1.8876 1.3226 1.5548 -0.4584 -0.8204 0.5831 1449 ILE C CB 12714 C CG1 . ILE C 33 ? 2.0073 1.3816 1.5345 -0.4701 -0.8302 0.5537 1449 ILE C CG1 12715 C CG2 . ILE C 33 ? 1.9301 1.4086 1.6439 -0.4652 -0.8830 0.6182 1449 ILE C CG2 12716 C CD1 . ILE C 33 ? 1.9354 1.2636 1.3976 -0.4531 -0.7725 0.5332 1449 ILE C CD1 12717 N N . THR C 34 ? 1.8214 1.3959 1.7600 -0.4830 -0.8292 0.5932 1450 THR C N 12718 C CA . THR C 34 ? 1.8547 1.5078 1.9305 -0.4764 -0.8275 0.6157 1450 THR C CA 12719 C C . THR C 34 ? 2.0030 1.7009 2.1188 -0.4857 -0.8935 0.6444 1450 THR C C 12720 O O . THR C 34 ? 2.1526 1.8414 2.2273 -0.5139 -0.9403 0.6384 1450 THR C O 12721 C CB . THR C 34 ? 1.8184 1.5018 1.9571 -0.4980 -0.8028 0.5938 1450 THR C CB 12722 O OG1 . THR C 34 ? 1.9110 1.5488 2.0138 -0.4883 -0.7428 0.5657 1450 THR C OG1 12723 C CG2 . THR C 34 ? 1.7486 1.5226 2.0312 -0.4905 -0.7972 0.6146 1450 THR C CG2 12724 N N . TYR C 35 ? 1.8311 1.5751 2.0275 -0.4609 -0.9005 0.6743 1451 TYR C N 12725 C CA . TYR C 35 ? 1.8875 1.6723 2.1259 -0.4663 -0.9647 0.7008 1451 TYR C CA 12726 C C . TYR C 35 ? 1.9868 1.8546 2.3682 -0.4469 -0.9669 0.7217 1451 TYR C C 12727 O O . TYR C 35 ? 2.1705 2.0464 2.5930 -0.4146 -0.9326 0.7297 1451 TYR C O 12728 C CB . TYR C 35 ? 2.0529 1.7829 2.1926 -0.4554 -1.0000 0.7191 1451 TYR C CB 12729 C CG . TYR C 35 ? 2.0553 1.7646 2.1894 -0.4201 -0.9694 0.7360 1451 TYR C CG 12730 C CD1 . TYR C 35 ? 2.0744 1.7274 2.1319 -0.4101 -0.9169 0.7195 1451 TYR C CD1 12731 C CD2 . TYR C 35 ? 1.8875 1.6322 2.0942 -0.3970 -0.9963 0.7676 1451 TYR C CD2 12732 C CE1 . TYR C 35 ? 2.0350 1.6681 2.0880 -0.3798 -0.8909 0.7368 1451 TYR C CE1 12733 C CE2 . TYR C 35 ? 1.8867 1.6088 2.0881 -0.3661 -0.9736 0.7845 1451 TYR C CE2 12734 C CZ . TYR C 35 ? 2.0055 1.6720 2.1295 -0.3585 -0.9205 0.7704 1451 TYR C CZ 12735 O OH . TYR C 35 ? 2.0373 1.6802 2.1563 -0.3296 -0.8998 0.7890 1451 TYR C OH 12736 N N . GLY C 36 ? 1.7944 1.7257 2.2541 -0.4661 -1.0082 0.7285 1452 GLY C N 12737 C CA . GLY C 36 ? 1.9264 1.9249 2.4940 -0.4470 -1.0400 0.7527 1452 GLY C CA 12738 C C . GLY C 36 ? 1.9282 1.9931 2.5713 -0.4725 -1.0919 0.7583 1452 GLY C C 12739 O O . GLY C 36 ? 1.8936 1.9875 2.5609 -0.5046 -1.0854 0.7424 1452 GLY C O 12740 N N . GLU C 37 ? 1.9940 2.0813 2.6751 -0.4581 -1.1451 0.7816 1453 GLU C N 12741 C CA . GLU C 37 ? 2.2564 2.4027 3.0168 -0.4699 -1.1784 0.7810 1453 GLU C CA 12742 C C . GLU C 37 ? 2.2211 2.3672 2.9553 -0.5117 -1.1887 0.7649 1453 GLU C C 12743 O O . GLU C 37 ? 2.1795 2.2529 2.7975 -0.5300 -1.1914 0.7550 1453 GLU C O 12744 C CB . GLU C 37 ? 2.3226 2.5707 3.2393 -0.4519 -1.1600 0.7810 1453 GLU C CB 12745 C CG . GLU C 37 ? 2.4299 2.6874 3.3917 -0.4126 -1.1818 0.7951 1453 GLU C CG 12746 C CD . GLU C 37 ? 2.4174 2.7408 3.4931 -0.3797 -1.1470 0.7929 1453 GLU C CD 12747 O OE1 . GLU C 37 ? 2.4048 2.6934 3.4648 -0.3446 -1.1448 0.8042 1453 GLU C OE1 12748 O OE2 . GLU C 37 ? 2.4051 2.8127 3.5820 -0.3888 -1.1188 0.7776 1453 GLU C OE2 12749 N N . THR C 38 ? 2.0467 2.0925 3.2975 -0.3231 -0.7090 0.0633 1454 THR C N 12750 C CA . THR C 38 ? 2.0551 2.1419 3.4417 -0.3738 -0.6852 0.0628 1454 THR C CA 12751 C C . THR C 38 ? 2.0341 2.2177 3.5685 -0.4075 -0.5968 0.0816 1454 THR C C 12752 O O . THR C 38 ? 1.9476 2.1208 3.4470 -0.4411 -0.5183 0.1276 1454 THR C O 12753 C CB . THR C 38 ? 2.1630 2.2730 3.6769 -0.3685 -0.7751 0.0046 1454 THR C CB 12754 O OG1 . THR C 38 ? 2.2531 2.4325 3.8688 -0.3302 -0.8182 -0.0365 1454 THR C OG1 12755 C CG2 . THR C 38 ? 2.1704 2.1752 3.5334 -0.3438 -0.8538 -0.0105 1454 THR C CG2 12756 N N . GLY C 39 ? 2.0875 2.3647 3.7845 -0.3944 -0.6106 0.0448 1455 GLY C N 12757 C CA . GLY C 39 ? 2.0304 2.4109 3.9059 -0.4293 -0.5317 0.0523 1455 GLY C CA 12758 C C . GLY C 39 ? 2.0150 2.4594 3.9043 -0.4080 -0.4670 0.0642 1455 GLY C C 12759 O O . GLY C 39 ? 1.9681 2.4916 3.9833 -0.4376 -0.3857 0.0782 1455 GLY C O 12760 N N . GLY C 40 ? 2.0866 2.4931 3.8465 -0.3566 -0.4991 0.0586 1456 GLY C N 12761 C CA . GLY C 40 ? 2.1159 2.5767 3.8845 -0.3300 -0.4467 0.0620 1456 GLY C CA 12762 C C . GLY C 40 ? 2.1475 2.5884 3.8094 -0.3512 -0.3476 0.1168 1456 GLY C C 12763 O O . GLY C 40 ? 2.1291 2.5288 3.7417 -0.3905 -0.3127 0.1536 1456 GLY C O 12764 N N . ASN C 41 ? 2.2158 2.6838 3.8404 -0.3212 -0.3055 0.1195 1457 ASN C N 12765 C CA . ASN C 41 ? 2.3295 2.7686 3.8231 -0.3288 -0.2257 0.1645 1457 ASN C CA 12766 C C . ASN C 41 ? 2.4242 2.7486 3.7233 -0.3294 -0.2575 0.1891 1457 ASN C C 12767 O O . ASN C 41 ? 2.4557 2.7454 3.6555 -0.3496 -0.2053 0.2291 1457 ASN C O 12768 C CB . ASN C 41 ? 2.3826 2.8593 3.8572 -0.2872 -0.1945 0.1507 1457 ASN C CB 12769 C CG . ASN C 41 ? 2.4197 2.8416 3.8140 -0.2375 -0.2743 0.1197 1457 ASN C CG 12770 O OD1 . ASN C 41 ? 2.4381 2.8937 3.9337 -0.2098 -0.3339 0.0787 1457 ASN C OD1 12771 N ND2 . ASN C 41 ? 2.3898 2.7246 3.6033 -0.2250 -0.2761 0.1388 1457 ASN C ND2 12772 N N . SER C 42 ? 2.4907 2.7587 3.7387 -0.3034 -0.3439 0.1632 1458 SER C N 12773 C CA . SER C 42 ? 2.4808 2.6416 3.5646 -0.3020 -0.3856 0.1777 1458 SER C CA 12774 C C . SER C 42 ? 2.3850 2.4916 3.3079 -0.2850 -0.3570 0.1976 1458 SER C C 12775 O O . SER C 42 ? 2.3429 2.4840 3.2539 -0.2895 -0.2889 0.2153 1458 SER C O 12776 C CB . SER C 42 ? 2.4819 2.6173 3.5612 -0.3467 -0.3705 0.2044 1458 SER C CB 12777 O OG . SER C 42 ? 2.4956 2.5351 3.4296 -0.3440 -0.4108 0.2136 1458 SER C OG 12778 N N . PRO C 43 ? 2.3312 2.3497 3.1287 -0.2652 -0.4093 0.1929 1459 PRO C N 12779 C CA . PRO C 43 ? 2.3433 2.2912 2.9849 -0.2549 -0.3969 0.2076 1459 PRO C CA 12780 C C . PRO C 43 ? 2.3089 2.1940 2.8443 -0.2823 -0.3912 0.2347 1459 PRO C C 12781 O O . PRO C 43 ? 2.4537 2.2634 2.9038 -0.2733 -0.4369 0.2307 1459 PRO C O 12782 C CB . PRO C 43 ? 2.3560 2.2464 2.9513 -0.2148 -0.4609 0.1828 1459 PRO C CB 12783 C CG . PRO C 43 ? 2.3315 2.2367 3.0173 -0.2080 -0.5240 0.1600 1459 PRO C CG 12784 C CD . PRO C 43 ? 2.3164 2.2989 3.1286 -0.2465 -0.4923 0.1662 1459 PRO C CD 12785 N N . VAL C 44 ? 2.0667 1.9783 2.6035 -0.3111 -0.3375 0.2614 1460 VAL C N 12786 C CA . VAL C 44 ? 1.9166 1.7731 2.3619 -0.3325 -0.3354 0.2839 1460 VAL C CA 12787 C C . VAL C 44 ? 1.9139 1.7007 2.2249 -0.3194 -0.3478 0.2827 1460 VAL C C 12788 O O . VAL C 44 ? 2.1089 1.9008 2.3779 -0.3075 -0.3214 0.2804 1460 VAL C O 12789 C CB . VAL C 44 ? 1.7908 1.6806 2.2398 -0.3558 -0.2730 0.3148 1460 VAL C CB 12790 C CG1 . VAL C 44 ? 1.6239 1.5500 2.1873 -0.3814 -0.2633 0.3243 1460 VAL C CG1 12791 C CG2 . VAL C 44 ? 1.7969 1.7340 2.2427 -0.3416 -0.2220 0.3170 1460 VAL C CG2 12792 N N . GLN C 45 ? 1.8958 1.6167 2.1430 -0.3223 -0.3862 0.2819 1461 GLN C N 12793 C CA . GLN C 45 ? 2.0397 1.6894 2.1677 -0.3139 -0.3951 0.2812 1461 GLN C CA 12794 C C . GLN C 45 ? 2.0391 1.6496 2.1022 -0.3340 -0.3923 0.2959 1461 GLN C C 12795 O O . GLN C 45 ? 1.9754 1.5803 2.0670 -0.3433 -0.4140 0.2972 1461 GLN C O 12796 C CB . GLN C 45 ? 2.0939 1.6884 2.1936 -0.2864 -0.4465 0.2628 1461 GLN C CB 12797 C CG . GLN C 45 ? 2.1320 1.6411 2.1077 -0.2799 -0.4491 0.2661 1461 GLN C CG 12798 C CD . GLN C 45 ? 2.2635 1.7636 2.2197 -0.2636 -0.4327 0.2579 1461 GLN C CD 12799 O OE1 . GLN C 45 ? 2.2325 1.7016 2.1224 -0.2741 -0.4047 0.2624 1461 GLN C OE1 12800 N NE2 . GLN C 45 ? 2.3097 1.8376 2.3309 -0.2372 -0.4519 0.2418 1461 GLN C NE2 12801 N N . GLU C 46 ? 2.0042 1.5900 1.9875 -0.3399 -0.3670 0.3025 1462 GLU C N 12802 C CA . GLU C 46 ? 1.8577 1.4193 1.7901 -0.3567 -0.3585 0.3140 1462 GLU C CA 12803 C C . GLU C 46 ? 1.8783 1.3937 1.7213 -0.3587 -0.3469 0.3106 1462 GLU C C 12804 O O . GLU C 46 ? 2.0217 1.5295 1.8442 -0.3518 -0.3365 0.3018 1462 GLU C O 12805 C CB . GLU C 46 ? 1.8278 1.4441 1.7969 -0.3704 -0.3237 0.3309 1462 GLU C CB 12806 C CG . GLU C 46 ? 1.9556 1.6090 1.9104 -0.3660 -0.2877 0.3315 1462 GLU C CG 12807 C CD . GLU C 46 ? 2.0302 1.7307 2.0084 -0.3720 -0.2546 0.3519 1462 GLU C CD 12808 O OE1 . GLU C 46 ? 1.9808 1.7011 2.0222 -0.3795 -0.2508 0.3661 1462 GLU C OE1 12809 O OE2 . GLU C 46 ? 2.0073 1.7215 1.9399 -0.3684 -0.2331 0.3533 1462 GLU C OE2 12810 N N . PHE C 47 ? 1.7608 1.2457 1.5579 -0.3690 -0.3468 0.3153 1463 PHE C N 12811 C CA . PHE C 47 ? 1.8736 1.3275 1.6037 -0.3769 -0.3268 0.3117 1463 PHE C CA 12812 C C . PHE C 47 ? 1.9159 1.3748 1.6309 -0.3881 -0.3170 0.3172 1463 PHE C C 12813 O O . PHE C 47 ? 1.8052 1.2800 1.5537 -0.3887 -0.3280 0.3252 1463 PHE C O 12814 C CB . PHE C 47 ? 1.9217 1.2977 1.5855 -0.3689 -0.3410 0.3064 1463 PHE C CB 12815 C CG . PHE C 47 ? 1.9877 1.3154 1.6203 -0.3591 -0.3737 0.3081 1463 PHE C CG 12816 C CD1 . PHE C 47 ? 2.0359 1.3598 1.7013 -0.3409 -0.4140 0.3033 1463 PHE C CD1 12817 C CD2 . PHE C 47 ? 1.9144 1.2033 1.4871 -0.3654 -0.3659 0.3097 1463 PHE C CD2 12818 C CE1 . PHE C 47 ? 2.0020 1.2811 1.6361 -0.3284 -0.4518 0.2982 1463 PHE C CE1 12819 C CE2 . PHE C 47 ? 1.9781 1.2187 1.5112 -0.3521 -0.3980 0.3070 1463 PHE C CE2 12820 C CZ . PHE C 47 ? 2.0256 1.2595 1.5867 -0.3331 -0.4440 0.3002 1463 PHE C CZ 12821 N N . THR C 48 ? 2.0348 1.4793 1.7066 -0.3970 -0.2958 0.3109 1464 THR C N 12822 C CA . THR C 48 ? 1.9271 1.3866 1.5926 -0.4037 -0.2842 0.3117 1464 THR C CA 12823 C C . THR C 48 ? 1.9502 1.3540 1.5559 -0.4075 -0.2784 0.3056 1464 THR C C 12824 O O . THR C 48 ? 2.1132 1.4753 1.6781 -0.4119 -0.2664 0.3009 1464 THR C O 12825 C CB . THR C 48 ? 1.8439 1.3595 1.5291 -0.4087 -0.2606 0.3046 1464 THR C CB 12826 O OG1 . THR C 48 ? 1.7720 1.3336 1.4961 -0.4011 -0.2611 0.3120 1464 THR C OG1 12827 C CG2 . THR C 48 ? 1.7168 1.2532 1.4031 -0.4088 -0.2542 0.3041 1464 THR C CG2 12828 N N . VAL C 49 ? 1.8027 1.2004 1.4003 -0.4048 -0.2837 0.3066 1465 VAL C N 12829 C CA . VAL C 49 ? 1.8211 1.1702 1.3588 -0.4051 -0.2727 0.2998 1465 VAL C CA 12830 C C . VAL C 49 ? 1.8609 1.2475 1.4165 -0.4076 -0.2544 0.2924 1465 VAL C C 12831 O O . VAL C 49 ? 1.7226 1.1445 1.3194 -0.4013 -0.2671 0.2973 1465 VAL C O 12832 C CB . VAL C 49 ? 1.9121 1.2018 1.4086 -0.3902 -0.3057 0.3013 1465 VAL C CB 12833 C CG1 . VAL C 49 ? 1.9502 1.1969 1.3829 -0.3851 -0.2935 0.2932 1465 VAL C CG1 12834 C CG2 . VAL C 49 ? 1.9368 1.1794 1.3996 -0.3817 -0.3242 0.3048 1465 VAL C CG2 12835 N N . PRO C 50 ? 1.8565 1.2340 1.3842 -0.4158 -0.2225 0.2808 1466 PRO C N 12836 C CA . PRO C 50 ? 1.9178 1.3353 1.4691 -0.4140 -0.2060 0.2684 1466 PRO C CA 12837 C C . PRO C 50 ? 2.0871 1.4809 1.6221 -0.3968 -0.2263 0.2694 1466 PRO C C 12838 O O . PRO C 50 ? 2.2238 1.5577 1.7101 -0.3891 -0.2449 0.2731 1466 PRO C O 12839 C CB . PRO C 50 ? 1.8465 1.2468 1.3696 -0.4285 -0.1636 0.2553 1466 PRO C CB 12840 C CG . PRO C 50 ? 1.8902 1.2146 1.3475 -0.4326 -0.1616 0.2675 1466 PRO C CG 12841 C CD . PRO C 50 ? 1.8836 1.2158 1.3652 -0.4279 -0.1958 0.2787 1466 PRO C CD 12842 N N . GLY C 51 ? 2.0800 1.5171 1.6541 -0.3877 -0.2265 0.2633 1467 GLY C N 12843 C CA . GLY C 51 ? 2.0471 1.4599 1.6140 -0.3705 -0.2465 0.2622 1467 GLY C CA 12844 C C . GLY C 51 ? 2.0955 1.4586 1.6015 -0.3629 -0.2336 0.2467 1467 GLY C C 12845 O O . GLY C 51 ? 2.2189 1.5463 1.7057 -0.3471 -0.2547 0.2411 1467 GLY C O 12846 N N . SER C 52 ? 2.0981 1.4549 1.5719 -0.3741 -0.1963 0.2389 1468 SER C N 12847 C CA . SER C 52 ? 2.2136 1.5213 1.6177 -0.3664 -0.1719 0.2266 1468 SER C CA 12848 C C . SER C 52 ? 2.3361 1.5587 1.6518 -0.3599 -0.1906 0.2360 1468 SER C C 12849 O O . SER C 52 ? 2.4643 1.6307 1.7014 -0.3449 -0.1818 0.2271 1468 SER C O 12850 C CB . SER C 52 ? 2.2983 1.6342 1.7104 -0.3838 -0.1148 0.2160 1468 SER C CB 12851 O OG . SER C 52 ? 2.5013 1.7944 1.8468 -0.3753 -0.0805 0.2051 1468 SER C OG 12852 N N . LYS C 53 ? 2.2843 1.4978 1.6098 -0.3668 -0.2179 0.2517 1469 LYS C N 12853 C CA . LYS C 53 ? 2.3855 1.5231 1.6340 -0.3557 -0.2442 0.2587 1469 LYS C CA 12854 C C . LYS C 53 ? 2.3370 1.4647 1.6096 -0.3413 -0.3038 0.2557 1469 LYS C C 12855 O O . LYS C 53 ? 2.3144 1.4923 1.6713 -0.3500 -0.3225 0.2626 1469 LYS C O 12856 C CB . LYS C 53 ? 2.5599 1.6880 1.8039 -0.3695 -0.2352 0.2743 1469 LYS C CB 12857 C CG . LYS C 53 ? 2.5933 1.7038 1.7992 -0.3861 -0.1765 0.2774 1469 LYS C CG 12858 C CD . LYS C 53 ? 2.4690 1.5621 1.6757 -0.3988 -0.1727 0.2914 1469 LYS C CD 12859 C CE . LYS C 53 ? 2.5688 1.6280 1.7366 -0.4190 -0.1120 0.2959 1469 LYS C CE 12860 N NZ . LYS C 53 ? 2.6328 1.5946 1.6745 -0.4035 -0.0924 0.3057 1469 LYS C NZ 12861 N N . SER C 54 ? 2.4558 1.5175 1.6539 -0.3192 -0.3318 0.2439 1470 SER C N 12862 C CA . SER C 54 ? 2.4638 1.5130 1.6917 -0.3068 -0.3915 0.2328 1470 SER C CA 12863 C C . SER C 54 ? 2.5315 1.5486 1.7427 -0.2981 -0.4352 0.2358 1470 SER C C 12864 O O . SER C 54 ? 2.5468 1.5576 1.7942 -0.2892 -0.4884 0.2220 1470 SER C O 12865 C CB . SER C 54 ? 2.5338 1.5336 1.6998 -0.2836 -0.4071 0.2079 1470 SER C CB 12866 O OG . SER C 54 ? 2.5942 1.5791 1.7974 -0.2742 -0.4682 0.1913 1470 SER C OG 12867 N N . THR C 55 ? 2.7498 1.8774 2.1989 -0.0283 -0.4461 0.8634 1471 THR C N 12868 C CA . THR C 55 ? 2.6415 1.7329 2.0837 -0.0094 -0.4886 0.8361 1471 THR C CA 12869 C C . THR C 55 ? 2.5465 1.6550 2.0730 -0.0379 -0.5051 0.8191 1471 THR C C 12870 O O . THR C 55 ? 2.3791 1.5218 1.9670 -0.0699 -0.4812 0.8350 1471 THR C O 12871 C CB . THR C 55 ? 2.6042 1.6282 1.9679 0.0327 -0.4869 0.8752 1471 THR C CB 12872 O OG1 . THR C 55 ? 2.6596 1.6777 2.0390 0.0261 -0.4435 0.9201 1471 THR C OG1 12873 C CG2 . THR C 55 ? 2.6367 1.6424 1.9135 0.0661 -0.4808 0.8801 1471 THR C CG2 12874 N N . ALA C 56 ? 2.5999 1.6872 2.1291 -0.0257 -0.5455 0.7855 1472 ALA C N 12875 C CA . ALA C 56 ? 2.6574 1.7561 2.2625 -0.0514 -0.5643 0.7664 1472 ALA C CA 12876 C C . ALA C 56 ? 2.7346 1.7868 2.3105 -0.0227 -0.5999 0.7524 1472 ALA C C 12877 O O . ALA C 56 ? 2.8081 1.8319 2.3113 0.0164 -0.6178 0.7437 1472 ALA C O 12878 C CB . ALA C 56 ? 2.5528 1.7100 2.2299 -0.0846 -0.5785 0.7195 1472 ALA C CB 12879 N N . THR C 57 ? 2.6270 1.6749 2.2595 -0.0412 -0.6086 0.7494 1473 THR C N 12880 C CA . THR C 57 ? 2.5423 1.5486 2.1511 -0.0147 -0.6385 0.7392 1473 THR C CA 12881 C C . THR C 57 ? 2.4135 1.4443 2.1007 -0.0471 -0.6683 0.6986 1473 THR C C 12882 O O . THR C 57 ? 2.3212 1.3970 2.0858 -0.0900 -0.6596 0.6875 1473 THR C O 12883 C CB . THR C 57 ? 2.5280 1.4825 2.1102 0.0064 -0.6090 0.7912 1473 THR C CB 12884 O OG1 . THR C 57 ? 2.5624 1.5044 2.1017 0.0190 -0.5700 0.8350 1473 THR C OG1 12885 C CG2 . THR C 57 ? 2.6087 1.5141 2.1226 0.0577 -0.6334 0.7899 1473 THR C CG2 12886 N N . ILE C 58 ? 2.5545 1.5580 2.2203 -0.0244 -0.7035 0.6769 1474 ILE C N 12887 C CA . ILE C 58 ? 2.6017 1.6231 2.3336 -0.0513 -0.7364 0.6366 1474 ILE C CA 12888 C C . ILE C 58 ? 2.7886 1.7681 2.5128 -0.0352 -0.7481 0.6467 1474 ILE C C 12889 O O . ILE C 58 ? 2.7920 1.7343 2.4410 0.0125 -0.7592 0.6542 1474 ILE C O 12890 C CB . ILE C 58 ? 2.4741 1.5173 2.1970 -0.0444 -0.7768 0.5801 1474 ILE C CB 12891 C CG1 . ILE C 58 ? 2.2534 1.3453 2.0140 -0.0722 -0.7620 0.5634 1474 ILE C CG1 12892 C CG2 . ILE C 58 ? 2.4612 1.5050 2.2303 -0.0578 -0.8165 0.5417 1474 ILE C CG2 12893 C CD1 . ILE C 58 ? 2.2167 1.3282 1.9779 -0.0677 -0.7923 0.5063 1474 ILE C CD1 12894 N N . SER C 59 ? 2.8567 1.8446 2.6582 -0.0732 -0.7435 0.6466 1475 SER C N 12895 C CA . SER C 59 ? 2.8729 1.8226 2.6753 -0.0630 -0.7514 0.6544 1475 SER C CA 12896 C C . SER C 59 ? 2.8555 1.8221 2.7036 -0.0829 -0.7975 0.6063 1475 SER C C 12897 O O . SER C 59 ? 2.9587 1.9619 2.8895 -0.1294 -0.8015 0.5862 1475 SER C O 12898 C CB . SER C 59 ? 2.8256 1.7640 2.6810 -0.0904 -0.7058 0.6929 1475 SER C CB 12899 O OG . SER C 59 ? 2.7754 1.6765 2.6367 -0.0833 -0.7081 0.7001 1475 SER C OG 12900 N N . GLY C 60 ? 2.6798 1.6216 2.4734 -0.0455 -0.8323 0.5874 1476 GLY C N 12901 C CA . GLY C 60 ? 2.6106 1.5634 2.4407 -0.0601 -0.8776 0.5416 1476 GLY C CA 12902 C C . GLY C 60 ? 2.6851 1.6293 2.4460 -0.0150 -0.9189 0.5079 1476 GLY C C 12903 O O . GLY C 60 ? 2.7486 1.6691 2.4270 0.0347 -0.9128 0.5271 1476 GLY C O 12904 N N . LEU C 61 ? 2.7320 1.6973 2.5292 -0.0314 -0.9604 0.4559 1477 LEU C N 12905 C CA . LEU C 61 ? 2.7093 1.6784 2.4579 0.0033 -1.0031 0.4095 1477 LEU C CA 12906 C C . LEU C 61 ? 2.6643 1.6023 2.3286 0.0599 -1.0138 0.4238 1477 LEU C C 12907 O O . LEU C 61 ? 2.5089 1.4180 2.1734 0.0644 -1.0065 0.4526 1477 LEU C O 12908 C CB . LEU C 61 ? 2.6051 1.6015 2.3286 0.0128 -1.0004 0.3846 1477 LEU C CB 12909 C CG . LEU C 61 ? 2.5993 1.5995 2.2937 0.0177 -0.9569 0.4233 1477 LEU C CG 12910 C CD1 . LEU C 61 ? 2.6500 1.6235 2.2464 0.0744 -0.9480 0.4513 1477 LEU C CD1 12911 C CD2 . LEU C 61 ? 2.3066 1.3428 2.0221 0.0007 -0.9531 0.3901 1477 LEU C CD2 12912 N N . LYS C 62 ? 2.7951 1.7415 2.3876 0.1047 -1.0286 0.4026 1478 LYS C N 12913 C CA . LYS C 62 ? 3.0156 1.9448 2.5248 0.1658 -1.0454 0.4052 1478 LYS C CA 12914 C C . LYS C 62 ? 3.0970 2.0181 2.5212 0.2155 -1.0211 0.4346 1478 LYS C C 12915 O O . LYS C 62 ? 3.0426 1.9702 2.4739 0.1990 -0.9929 0.4512 1478 LYS C O 12916 C CB . LYS C 62 ? 3.0503 2.0056 2.5532 0.1794 -1.0989 0.3365 1478 LYS C CB 12917 C CG . LYS C 62 ? 2.9041 1.8543 2.4624 0.1524 -1.1280 0.3152 1478 LYS C CG 12918 C CD . LYS C 62 ? 2.7097 1.6843 2.2505 0.1750 -1.1795 0.2482 1478 LYS C CD 12919 C CE . LYS C 62 ? 2.5540 1.5189 2.1424 0.1525 -1.2093 0.2308 1478 LYS C CE 12920 N NZ . LYS C 62 ? 2.4914 1.4813 2.0638 0.1752 -1.2593 0.1635 1478 LYS C NZ 12921 N N . PRO C 63 ? 3.2097 2.1176 2.5511 0.2794 -1.0310 0.4425 1479 PRO C N 12922 C CA . PRO C 63 ? 3.3065 2.2138 2.5644 0.3315 -1.0166 0.4585 1479 PRO C CA 12923 C C . PRO C 63 ? 3.3239 2.2733 2.5773 0.3277 -1.0413 0.4007 1479 PRO C C 12924 O O . PRO C 63 ? 3.3848 2.3370 2.6055 0.3381 -1.0191 0.4148 1479 PRO C O 12925 C CB . PRO C 63 ? 3.4055 2.3001 2.5820 0.4030 -1.0301 0.4668 1479 PRO C CB 12926 C CG . PRO C 63 ? 3.4074 2.3072 2.6251 0.3855 -1.0629 0.4374 1479 PRO C CG 12927 C CD . PRO C 63 ? 3.2863 2.1750 2.6030 0.3102 -1.0455 0.4502 1479 PRO C CD 12928 N N . GLY C 64 ? 3.2507 2.2304 2.5390 0.3122 -1.0842 0.3359 1480 GLY C N 12929 C CA . GLY C 64 ? 3.1127 2.1307 2.4194 0.2964 -1.1018 0.2753 1480 GLY C CA 12930 C C . GLY C 64 ? 2.9651 2.0010 2.3509 0.2532 -1.1339 0.2205 1480 GLY C C 12931 O O . GLY C 64 ? 2.8858 1.9128 2.2843 0.2559 -1.1584 0.2149 1480 GLY C O 12932 N N . VAL C 65 ? 2.8673 1.9269 2.3032 0.2169 -1.1315 0.1804 1481 VAL C N 12933 C CA . VAL C 65 ? 2.8561 1.9269 2.3785 0.1699 -1.1509 0.1362 1481 VAL C CA 12934 C C . VAL C 65 ? 2.7868 1.8805 2.3465 0.1418 -1.1313 0.1043 1481 VAL C C 12935 O O . VAL C 65 ? 2.7869 1.8822 2.3133 0.1492 -1.0979 0.1317 1481 VAL C O 12936 C CB . VAL C 65 ? 2.4503 1.4960 2.0341 0.1291 -1.1384 0.1810 1481 VAL C CB 12937 C CG1 . VAL C 65 ? 2.4076 1.4450 2.0067 0.1046 -1.0896 0.2369 1481 VAL C CG1 12938 C CG2 . VAL C 65 ? 2.3369 1.3916 2.0067 0.0864 -1.1629 0.1359 1481 VAL C CG2 12939 N N . ASP C 66 ? 2.7591 1.8681 2.3861 0.1119 -1.1486 0.0480 1482 ASP C N 12940 C CA . ASP C 66 ? 2.7265 1.8549 2.3936 0.0869 -1.1239 0.0167 1482 ASP C CA 12941 C C . ASP C 66 ? 2.5056 1.6289 2.2464 0.0392 -1.0955 0.0492 1482 ASP C C 12942 O O . ASP C 66 ? 2.4753 1.5937 2.2801 0.0122 -1.1132 0.0361 1482 ASP C O 12943 C CB . ASP C 66 ? 2.7391 1.8875 2.4378 0.0869 -1.1525 -0.0685 1482 ASP C CB 12944 C CG . ASP C 66 ? 2.7113 1.8748 2.3435 0.1345 -1.1865 -0.1082 1482 ASP C CG 12945 O OD1 . ASP C 66 ? 2.6933 1.8559 2.2483 0.1714 -1.1791 -0.0735 1482 ASP C OD1 12946 O OD2 . ASP C 66 ? 2.5734 1.7516 2.2311 0.1372 -1.2201 -0.1752 1482 ASP C OD2 12947 N N . TYR C 67 ? 2.5358 2.1136 3.3135 -0.7832 -1.4789 1.1220 1483 TYR C N 12948 C CA . TYR C 67 ? 2.3965 1.9694 3.1859 -0.7214 -1.4262 1.0567 1483 TYR C CA 12949 C C . TYR C 67 ? 2.4268 1.9680 3.0629 -0.7348 -1.4014 0.9828 1483 TYR C C 12950 O O . TYR C 67 ? 2.4857 1.9992 3.0075 -0.7857 -1.4159 0.9851 1483 TYR C O 12951 C CB . TYR C 67 ? 2.4942 1.9967 3.2206 -0.7095 -1.4155 1.0440 1483 TYR C CB 12952 C CG . TYR C 67 ? 2.5156 2.0435 3.4342 -0.6389 -1.3794 1.0719 1483 TYR C CG 12953 C CD1 . TYR C 67 ? 2.5321 2.1218 3.6258 -0.6280 -1.4007 1.1433 1483 TYR C CD1 12954 C CD2 . TYR C 67 ? 2.4266 1.9313 3.3483 -0.5896 -1.2822 0.9866 1483 TYR C CD2 12955 C CE1 . TYR C 67 ? 2.4629 2.0683 3.7377 -0.5625 -1.3555 1.1630 1483 TYR C CE1 12956 C CE2 . TYR C 67 ? 2.3356 1.8570 3.4254 -0.5321 -1.2255 0.9940 1483 TYR C CE2 12957 C CZ . TYR C 67 ? 2.3630 1.9200 3.6339 -0.5158 -1.2715 1.0963 1483 TYR C CZ 12958 O OH . TYR C 67 ? 2.1884 1.7538 3.6337 -0.4575 -1.2077 1.1015 1483 TYR C OH 12959 N N . THR C 68 ? 2.3705 1.9181 3.0103 -0.6882 -1.3601 0.9155 1484 THR C N 12960 C CA . THR C 68 ? 2.4136 1.9356 2.9180 -0.6957 -1.3248 0.8309 1484 THR C CA 12961 C C . THR C 68 ? 2.3082 1.7773 2.7251 -0.6705 -1.2512 0.7406 1484 THR C C 12962 O O . THR C 68 ? 2.2427 1.7354 2.7612 -0.6172 -1.1888 0.7128 1484 THR C O 12963 C CB . THR C 68 ? 2.2372 1.8347 2.8501 -0.6592 -1.2952 0.8106 1484 THR C CB 12964 O OG1 . THR C 68 ? 2.2347 1.8673 2.9125 -0.6777 -1.3240 0.8780 1484 THR C OG1 12965 C CG2 . THR C 68 ? 2.0784 1.6384 2.5451 -0.6625 -1.2561 0.7290 1484 THR C CG2 12966 N N . ILE C 69 ? 2.2316 1.6291 2.4625 -0.7108 -1.2522 0.6918 1485 ILE C N 12967 C CA . ILE C 69 ? 2.1617 1.5097 2.3045 -0.6931 -1.1848 0.6062 1485 ILE C CA 12968 C C . ILE C 69 ? 2.3096 1.6437 2.3569 -0.6876 -1.1515 0.5262 1485 ILE C C 12969 O O . ILE C 69 ? 2.5510 1.8511 2.4896 -0.7200 -1.1718 0.5297 1485 ILE C O 12970 C CB . ILE C 69 ? 2.3295 1.5921 2.3370 -0.7475 -1.2061 0.6147 1485 ILE C CB 12971 C CG1 . ILE C 69 ? 2.4418 1.7089 2.5382 -0.7544 -1.2458 0.7028 1485 ILE C CG1 12972 C CG2 . ILE C 69 ? 2.2543 1.4738 2.1810 -0.7298 -1.1315 0.5209 1485 ILE C CG2 12973 C CD1 . ILE C 69 ? 2.5577 1.8268 2.6428 -0.8140 -1.3443 0.8017 1485 ILE C CD1 12974 N N . THR C 70 ? 2.1795 1.5376 2.2628 -0.6345 -1.0811 0.4558 1486 THR C N 12975 C CA . THR C 70 ? 2.0529 1.4021 2.0613 -0.6214 -1.0500 0.3832 1486 THR C CA 12976 C C . THR C 70 ? 2.1110 1.4264 2.0496 -0.6066 -0.9922 0.3038 1486 THR C C 12977 O O . THR C 70 ? 2.1673 1.4939 2.1566 -0.5853 -0.9549 0.2916 1486 THR C O 12978 C CB . THR C 70 ? 2.0010 1.4229 2.1170 -0.5744 -1.0241 0.3715 1486 THR C CB 12979 O OG1 . THR C 70 ? 1.9799 1.4458 2.2018 -0.5300 -0.9684 0.3507 1486 THR C OG1 12980 C CG2 . THR C 70 ? 2.1122 1.5743 2.3066 -0.5901 -1.0759 0.4446 1486 THR C CG2 12981 N N . VAL C 71 ? 2.0653 1.3397 1.8937 -0.6182 -0.9825 0.2490 1487 VAL C N 12982 C CA . VAL C 71 ? 2.0715 1.3211 1.8408 -0.6051 -0.9288 0.1701 1487 VAL C CA 12983 C C . VAL C 71 ? 2.1065 1.3796 1.8718 -0.5672 -0.8994 0.1102 1487 VAL C C 12984 O O . VAL C 71 ? 2.1948 1.4449 1.9046 -0.5734 -0.9131 0.1103 1487 VAL C O 12985 C CB . VAL C 71 ? 2.1502 1.3212 1.7824 -0.6517 -0.9255 0.1568 1487 VAL C CB 12986 C CG1 . VAL C 71 ? 2.1329 1.2887 1.7174 -0.6354 -0.8640 0.0690 1487 VAL C CG1 12987 C CG2 . VAL C 71 ? 2.3156 1.4566 1.9399 -0.6943 -0.9587 0.2165 1487 VAL C CG2 12988 N N . TYR C 72 ? 2.1208 1.4437 1.9449 -0.5225 -0.8491 0.0630 1488 TYR C N 12989 C CA . TYR C 72 ? 1.8684 1.2219 1.6965 -0.4853 -0.8252 0.0112 1488 TYR C CA 12990 C C . TYR C 72 ? 1.8883 1.2176 1.6550 -0.4813 -0.7880 -0.0620 1488 TYR C C 12991 O O . TYR C 72 ? 2.0414 1.3604 1.7966 -0.4922 -0.7590 -0.0858 1488 TYR C O 12992 C CB . TYR C 72 ? 1.7822 1.2161 1.7163 -0.4444 -0.7961 0.0073 1488 TYR C CB 12993 C CG . TYR C 72 ? 1.7578 1.2244 1.7683 -0.4442 -0.8226 0.0694 1488 TYR C CG 12994 C CD1 . TYR C 72 ? 1.8300 1.3039 1.9064 -0.4567 -0.8316 0.1213 1488 TYR C CD1 12995 C CD2 . TYR C 72 ? 1.7360 1.2265 1.7590 -0.4316 -0.8373 0.0768 1488 TYR C CD2 12996 C CE1 . TYR C 72 ? 1.8966 1.4081 2.0608 -0.4550 -0.8524 0.1758 1488 TYR C CE1 12997 C CE2 . TYR C 72 ? 1.7378 1.2611 1.8342 -0.4352 -0.8561 0.1284 1488 TYR C CE2 12998 C CZ . TYR C 72 ? 1.8976 1.4353 2.0705 -0.4460 -0.8623 0.1762 1488 TYR C CZ 12999 O OH . TYR C 72 ? 2.0801 1.6578 2.3434 -0.4482 -0.8779 0.2257 1488 TYR C OH 13000 N N . ALA C 73 ? 1.8960 1.2155 1.6289 -0.4658 -0.7877 -0.0971 1489 ALA C N 13001 C CA . ALA C 73 ? 1.9089 1.2192 1.6090 -0.4538 -0.7504 -0.1690 1489 ALA C CA 13002 C C . ALA C 73 ? 2.0217 1.4142 1.7948 -0.4039 -0.7223 -0.2053 1489 ALA C C 13003 O O . ALA C 73 ? 2.0508 1.4852 1.8692 -0.3799 -0.7388 -0.1808 1489 ALA C O 13004 C CB . ALA C 73 ? 1.9763 1.2236 1.6053 -0.4651 -0.7611 -0.1862 1489 ALA C CB 13005 N N . VAL C 74 ? 1.9598 1.3761 1.7394 -0.3944 -0.6803 -0.2639 1490 VAL C N 13006 C CA . VAL C 74 ? 1.7517 1.2531 1.5967 -0.3563 -0.6545 -0.2983 1490 VAL C CA 13007 C C . VAL C 74 ? 1.9574 1.4747 1.8006 -0.3310 -0.6423 -0.3549 1490 VAL C C 13008 O O . VAL C 74 ? 1.8889 1.3854 1.7067 -0.3421 -0.6130 -0.4040 1490 VAL C O 13009 C CB . VAL C 74 ? 1.7215 1.2586 1.5969 -0.3642 -0.6121 -0.3199 1490 VAL C CB 13010 C CG1 . VAL C 74 ? 1.8677 1.4957 1.8038 -0.3345 -0.5865 -0.3536 1490 VAL C CG1 13011 C CG2 . VAL C 74 ? 1.7196 1.2381 1.6137 -0.3844 -0.6228 -0.2610 1490 VAL C CG2 13012 N N . THR C 75 ? 2.0816 1.6360 1.9562 -0.2979 -0.6646 -0.3461 1491 THR C N 13013 C CA . THR C 75 ? 1.9841 1.5630 1.8782 -0.2657 -0.6611 -0.3891 1491 THR C CA 13014 C C . THR C 75 ? 1.8379 1.4969 1.7784 -0.2539 -0.6228 -0.4438 1491 THR C C 13015 O O . THR C 75 ? 1.7760 1.4987 1.7493 -0.2546 -0.6113 -0.4390 1491 THR C O 13016 C CB . THR C 75 ? 1.9726 1.5758 1.8903 -0.2346 -0.6998 -0.3566 1491 THR C CB 13017 O OG1 . THR C 75 ? 2.2665 1.7937 2.1380 -0.2491 -0.7328 -0.3090 1491 THR C OG1 13018 C CG2 . THR C 75 ? 1.7804 1.4092 1.7311 -0.1967 -0.7022 -0.3931 1491 THR C CG2 13019 N N . PRO C 76 ? 1.7243 0.8956 0.8623 0.0888 -0.2527 -0.0678 1492 PRO C N 13020 C CA . PRO C 76 ? 1.7365 0.9722 0.8465 0.1207 -0.2129 -0.0517 1492 PRO C CA 13021 C C . PRO C 76 ? 1.7727 0.9705 0.8666 0.1500 -0.1591 -0.0598 1492 PRO C C 13022 O O . PRO C 76 ? 1.7748 0.9830 0.7784 0.1905 -0.1347 -0.0727 1492 PRO C O 13023 C CB . PRO C 76 ? 1.6140 0.8827 0.6047 0.1502 -0.2333 -0.0697 1492 PRO C CB 13024 C CG . PRO C 76 ? 1.7266 0.9033 0.6505 0.1598 -0.2640 -0.1157 1492 PRO C CG 13025 C CD . PRO C 76 ? 1.7293 0.8555 0.7566 0.1072 -0.2917 -0.1072 1492 PRO C CD 13026 N N . ARG C 77 ? 1.7084 0.8751 0.8890 0.1313 -0.1408 -0.0496 1493 ARG C N 13027 C CA . ARG C 77 ? 1.6058 0.7437 0.7832 0.1565 -0.0891 -0.0520 1493 ARG C CA 13028 C C . ARG C 77 ? 1.5707 0.7520 0.8714 0.1423 -0.0648 -0.0216 1493 ARG C C 13029 O O . ARG C 77 ? 1.5245 0.7209 0.9112 0.1074 -0.0902 -0.0064 1493 ARG C O 13030 C CB . ARG C 77 ? 1.6100 0.6457 0.7367 0.1567 -0.0976 -0.0785 1493 ARG C CB 13031 C CG . ARG C 77 ? 1.7262 0.7099 0.7206 0.1840 -0.1307 -0.1195 1493 ARG C CG 13032 C CD . ARG C 77 ? 2.0354 0.9016 0.9654 0.1979 -0.1389 -0.1491 1493 ARG C CD 13033 N NE . ARG C 77 ? 2.0004 0.8596 0.8794 0.2434 -0.0851 -0.1562 1493 ARG C NE 13034 C CZ . ARG C 77 ? 2.1513 0.9534 1.0067 0.2549 -0.0837 -0.1651 1493 ARG C CZ 13035 N NH1 . ARG C 77 ? 2.1827 0.8753 1.0192 0.2313 -0.1383 -0.1824 1493 ARG C NH1 13036 N NH2 . ARG C 77 ? 2.3199 1.1909 1.1920 0.2810 -0.0356 -0.1475 1493 ARG C NH2 13037 N N . GLY C 78 ? 1.5504 0.7599 0.8574 0.1745 -0.0177 -0.0141 1494 GLY C N 13038 C CA . GLY C 78 ? 1.3252 0.5862 0.7382 0.1768 0.0036 0.0087 1494 GLY C CA 13039 C C . GLY C 78 ? 1.3566 0.6788 0.8286 0.1675 -0.0295 0.0261 1494 GLY C C 13040 O O . GLY C 78 ? 1.3553 0.6880 0.7811 0.1603 -0.0598 0.0275 1494 GLY C O 13041 N N . ASP C 79 ? 1.3739 0.7423 0.9469 0.1704 -0.0276 0.0408 1495 ASP C N 13042 C CA . ASP C 79 ? 1.2058 0.6220 0.8357 0.1697 -0.0655 0.0541 1495 ASP C CA 13043 C C . ASP C 79 ? 1.3696 0.7888 1.0229 0.1279 -0.1167 0.0590 1495 ASP C C 13044 O O . ASP C 79 ? 1.4711 0.8866 1.0815 0.1125 -0.1520 0.0622 1495 ASP C O 13045 C CB . ASP C 79 ? 1.1538 0.6225 0.8766 0.2002 -0.0511 0.0605 1495 ASP C CB 13046 C CG . ASP C 79 ? 1.3776 0.8830 1.1567 0.2076 -0.1005 0.0688 1495 ASP C CG 13047 O OD1 . ASP C 79 ? 1.3884 0.8760 1.1266 0.1988 -0.1342 0.0754 1495 ASP C OD1 13048 O OD2 . ASP C 79 ? 1.2131 0.7705 1.0767 0.2237 -0.1090 0.0710 1495 ASP C OD2 13049 N N . TRP C 80 ? 1.4468 0.8823 1.1694 0.1082 -0.1213 0.0639 1496 TRP C N 13050 C CA . TRP C 80 ? 1.4342 0.8686 1.1777 0.0654 -0.1686 0.0675 1496 TRP C CA 13051 C C . TRP C 80 ? 1.5374 0.9417 1.2909 0.0341 -0.1633 0.0677 1496 TRP C C 13052 O O . TRP C 80 ? 1.5817 1.0275 1.4098 0.0329 -0.1429 0.0842 1496 TRP C O 13053 C CB . TRP C 80 ? 1.3988 0.9006 1.2376 0.0659 -0.2014 0.0819 1496 TRP C CB 13054 C CG . TRP C 80 ? 1.6068 1.1090 1.4540 0.0266 -0.2558 0.0855 1496 TRP C CG 13055 C CD1 . TRP C 80 ? 1.6688 1.1873 1.5676 -0.0097 -0.2781 0.0921 1496 TRP C CD1 13056 C CD2 . TRP C 80 ? 1.6616 1.1546 1.4659 0.0172 -0.2968 0.0871 1496 TRP C CD2 13057 N NE1 . TRP C 80 ? 1.6362 1.1505 1.5243 -0.0370 -0.3291 0.0919 1496 TRP C NE1 13058 C CE2 . TRP C 80 ? 1.6929 1.1942 1.5231 -0.0207 -0.3406 0.0900 1496 TRP C CE2 13059 C CE3 . TRP C 80 ? 1.6215 1.1080 1.3707 0.0335 -0.3031 0.0925 1496 TRP C CE3 13060 C CZ2 . TRP C 80 ? 1.6759 1.1798 1.4766 -0.0384 -0.3874 0.0956 1496 TRP C CZ2 13061 C CZ3 . TRP C 80 ? 1.5387 1.0338 1.2618 0.0110 -0.3514 0.1046 1496 TRP C CZ3 13062 C CH2 . TRP C 80 ? 1.4963 1.0000 1.2440 -0.0226 -0.3916 0.1048 1496 TRP C CH2 13063 N N . ASN C 81 ? 1.6180 0.9543 1.2959 0.0098 -0.1874 0.0517 1497 ASN C N 13064 C CA . ASN C 81 ? 1.7642 1.0474 1.4409 -0.0245 -0.1987 0.0512 1497 ASN C CA 13065 C C . ASN C 81 ? 1.9235 1.1723 1.5786 -0.0628 -0.2588 0.0412 1497 ASN C C 13066 O O . ASN C 81 ? 1.8666 1.0893 1.4399 -0.0519 -0.2808 0.0190 1497 ASN C O 13067 C CB . ASN C 81 ? 1.7107 0.9138 1.2959 -0.0039 -0.1696 0.0317 1497 ASN C CB 13068 C CG . ASN C 81 ? 1.8688 1.0808 1.5071 -0.0040 -0.1300 0.0533 1497 ASN C CG 13069 O OD1 . ASN C 81 ? 2.1934 1.3486 1.8305 -0.0358 -0.1452 0.0606 1497 ASN C OD1 13070 N ND2 . ASN C 81 ? 1.6540 0.9384 1.3398 0.0312 -0.0844 0.0659 1497 ASN C ND2 13071 N N . GLU C 82 ? 2.0212 1.2816 1.7514 -0.1075 -0.2867 0.0607 1498 GLU C N 13072 C CA . GLU C 82 ? 1.9657 1.1964 1.6862 -0.1466 -0.3482 0.0524 1498 GLU C CA 13073 C C . GLU C 82 ? 2.0612 1.1958 1.7503 -0.1827 -0.3800 0.0464 1498 GLU C C 13074 O O . GLU C 82 ? 2.1418 1.2615 1.8630 -0.1954 -0.3587 0.0674 1498 GLU C O 13075 C CB . GLU C 82 ? 1.7858 1.1108 1.6204 -0.1733 -0.3700 0.0808 1498 GLU C CB 13076 C CG . GLU C 82 ? 1.6982 1.0958 1.5548 -0.1390 -0.3608 0.0825 1498 GLU C CG 13077 C CD . GLU C 82 ? 1.7387 1.2278 1.7047 -0.1553 -0.3848 0.1063 1498 GLU C CD 13078 O OE1 . GLU C 82 ? 1.9245 1.4360 1.9532 -0.1960 -0.4043 0.1252 1498 GLU C OE1 13079 O OE2 . GLU C 82 ? 1.6974 1.2366 1.6863 -0.1274 -0.3889 0.1081 1498 GLU C OE2 13080 N N . GLY C 83 ? 2.0118 1.0795 1.6355 -0.1980 -0.4367 0.0187 1499 GLY C N 13081 C CA . GLY C 83 ? 2.2057 1.1609 1.7878 -0.2301 -0.4858 0.0062 1499 GLY C CA 13082 C C . GLY C 83 ? 2.2713 1.2519 1.9690 -0.2968 -0.5124 0.0522 1499 GLY C C 13083 O O . GLY C 83 ? 2.2092 1.3087 2.0175 -0.3123 -0.4920 0.0897 1499 GLY C O 13084 N N . SER C 84 ? 2.2303 1.1014 1.9010 -0.3352 -0.5637 0.0508 1500 SER C N 13085 C CA . SER C 84 ? 2.1218 1.0165 1.9016 -0.4083 -0.5950 0.1052 1500 SER C CA 13086 C C . SER C 84 ? 2.1610 1.0929 1.9949 -0.4537 -0.6535 0.1132 1500 SER C C 13087 O O . SER C 84 ? 2.1760 1.1996 2.1298 -0.5066 -0.6619 0.1674 1500 SER C O 13088 C CB . SER C 84 ? 2.4844 1.2337 2.2149 -0.4398 -0.6410 0.1066 1500 SER C CB 13089 O OG . SER C 84 ? 2.8205 1.4252 2.4228 -0.4199 -0.7050 0.0443 1500 SER C OG 13090 N N . LYS C 85 ? 2.3630 1.2377 2.1088 -0.4302 -0.6928 0.0613 1501 LYS C N 13091 C CA . LYS C 85 ? 2.5897 1.4690 2.3663 -0.4740 -0.7611 0.0611 1501 LYS C CA 13092 C C . LYS C 85 ? 2.5216 1.4836 2.2905 -0.4408 -0.7520 0.0394 1501 LYS C C 13093 O O . LYS C 85 ? 2.5815 1.4888 2.2418 -0.4014 -0.7730 -0.0108 1501 LYS C O 13094 C CB . LYS C 85 ? 2.7956 1.5077 2.4711 -0.4882 -0.8458 0.0195 1501 LYS C CB 13095 C CG . LYS C 85 ? 2.8538 1.4666 2.5455 -0.5377 -0.8806 0.0486 1501 LYS C CG 13096 C CD . LYS C 85 ? 2.9181 1.3884 2.4653 -0.4824 -0.9038 -0.0072 1501 LYS C CD 13097 C CE . LYS C 85 ? 2.9311 1.3425 2.3874 -0.4516 -0.9677 -0.0628 1501 LYS C CE 13098 N NZ . LYS C 85 ? 2.9289 1.2190 2.2417 -0.3834 -0.9890 -0.1202 1501 LYS C NZ 13099 N N . PRO C 86 ? 2.2914 1.3921 2.1742 -0.4536 -0.7235 0.0790 1502 PRO C N 13100 C CA . PRO C 86 ? 2.0485 1.2248 1.9420 -0.4363 -0.7308 0.0684 1502 PRO C CA 13101 C C . PRO C 86 ? 2.2520 1.4072 2.1580 -0.4830 -0.8075 0.0628 1502 PRO C C 13102 O O . PRO C 86 ? 2.4429 1.5641 2.3953 -0.5404 -0.8495 0.0855 1502 PRO C O 13103 C CB . PRO C 86 ? 1.8243 1.1427 1.8379 -0.4318 -0.6825 0.1122 1502 PRO C CB 13104 C CG . PRO C 86 ? 1.8260 1.1651 1.9197 -0.4742 -0.6747 0.1560 1502 PRO C CG 13105 C CD . PRO C 86 ? 2.0592 1.2611 2.0614 -0.4746 -0.6802 0.1354 1502 PRO C CD 13106 N N . ILE C 87 ? 2.2006 1.3788 2.0679 -0.4618 -0.8286 0.0374 1503 ILE C N 13107 C CA . ILE C 87 ? 2.2434 1.4000 2.1101 -0.4985 -0.9023 0.0255 1503 ILE C CA 13108 C C . ILE C 87 ? 2.0296 1.3106 1.9872 -0.5100 -0.9046 0.0515 1503 ILE C C 13109 O O . ILE C 87 ? 1.9547 1.3096 1.9219 -0.4706 -0.8633 0.0569 1503 ILE C O 13110 C CB . ILE C 87 ? 2.4227 1.4908 2.1466 -0.4603 -0.9402 -0.0336 1503 ILE C CB 13111 C CG1 . ILE C 87 ? 2.6823 1.6258 2.3057 -0.4356 -0.9403 -0.0660 1503 ILE C CG1 13112 C CG2 . ILE C 87 ? 2.3932 1.4275 2.1104 -0.4957 -1.0225 -0.0508 1503 ILE C CG2 13113 C CD1 . ILE C 87 ? 2.7264 1.5676 2.3734 -0.4922 -0.9965 -0.0575 1503 ILE C CD1 13114 N N . SER C 88 ? 2.0923 1.3921 2.1158 -0.5644 -0.9585 0.0684 1504 SER C N 13115 C CA . SER C 88 ? 2.1210 1.5397 2.2342 -0.5760 -0.9661 0.0932 1504 SER C CA 13116 C C . SER C 88 ? 2.3391 1.7427 2.4423 -0.6024 -1.0274 0.0807 1504 SER C C 13117 O O . SER C 88 ? 2.5569 1.8711 2.6137 -0.6198 -1.0610 0.0657 1504 SER C O 13118 C CB . SER C 88 ? 2.0236 1.5515 2.2721 -0.6043 -0.9387 0.1480 1504 SER C CB 13119 O OG . SER C 88 ? 2.0500 1.6956 2.3822 -0.6080 -0.9499 0.1683 1504 SER C OG 13120 N N . ILE C 89 ? 2.2323 1.7256 2.3744 -0.5911 -1.0297 0.0883 1505 ILE C N 13121 C CA . ILE C 89 ? 2.3127 1.8188 2.4603 -0.6064 -1.0671 0.0841 1505 ILE C CA 13122 C C . ILE C 89 ? 2.2418 1.8782 2.4888 -0.6078 -1.0581 0.1153 1505 ILE C C 13123 O O . ILE C 89 ? 1.8861 1.5825 2.1568 -0.5769 -1.0301 0.1239 1505 ILE C O 13124 C CB . ILE C 89 ? 2.4299 1.8725 2.4560 -0.5690 -1.0886 0.0367 1505 ILE C CB 13125 C CG1 . ILE C 89 ? 2.5103 1.9502 2.5386 -0.5879 -1.1324 0.0285 1505 ILE C CG1 13126 C CG2 . ILE C 89 ? 2.0418 1.5447 2.0429 -0.5259 -1.0627 0.0342 1505 ILE C CG2 13127 C CD1 . ILE C 89 ? 2.4126 1.7859 2.4613 -0.6326 -1.1675 0.0356 1505 ILE C CD1 13128 N N . ASN C 90 ? 2.2279 1.9052 2.5308 -0.6403 -1.0850 0.1318 1506 ASN C N 13129 C CA . ASN C 90 ? 2.0174 1.8177 2.4089 -0.6369 -1.0800 0.1576 1506 ASN C CA 13130 C C . ASN C 90 ? 2.1294 1.9326 2.4761 -0.6147 -1.0988 0.1353 1506 ASN C C 13131 O O . ASN C 90 ? 2.2441 1.9663 2.4965 -0.6051 -1.1182 0.1017 1506 ASN C O 13132 C CB . ASN C 90 ? 1.9893 1.8617 2.4831 -0.6869 -1.0941 0.1976 1506 ASN C CB 13133 C CG . ASN C 90 ? 1.9687 1.8634 2.5200 -0.7134 -1.0742 0.2315 1506 ASN C CG 13134 O OD1 . ASN C 90 ? 1.9545 1.8552 2.5040 -0.6866 -1.0422 0.2306 1506 ASN C OD1 13135 N ND2 . ASN C 90 ? 2.0114 1.9225 2.6156 -0.7676 -1.0945 0.2660 1506 ASN C ND2 13136 N N . TYR C 91 ? 2.2285 2.1321 2.6444 -0.6041 -1.0950 0.1546 1507 TYR C N 13137 C CA . TYR C 91 ? 2.3352 2.2577 2.7252 -0.5858 -1.1110 0.1420 1507 TYR C CA 13138 C C . TYR C 91 ? 2.2351 2.2703 2.7153 -0.5727 -1.1052 0.1670 1507 TYR C C 13139 O O . TYR C 91 ? 2.0580 2.1328 2.5643 -0.5384 -1.0826 0.1767 1507 TYR C O 13140 C CB . TYR C 91 ? 2.1627 2.0374 2.4574 -0.5450 -1.1007 0.1190 1507 TYR C CB 13141 C CG . TYR C 91 ? 2.0923 2.0060 2.3735 -0.5255 -1.1119 0.1176 1507 TYR C CG 13142 C CD1 . TYR C 91 ? 2.1499 2.0660 2.4235 -0.5445 -1.1433 0.1065 1507 TYR C CD1 13143 C CD2 . TYR C 91 ? 1.9044 1.8490 2.1809 -0.4891 -1.0937 0.1294 1507 TYR C CD2 13144 C CE1 . TYR C 91 ? 2.2611 2.2170 2.5243 -0.5279 -1.1531 0.1071 1507 TYR C CE1 13145 C CE2 . TYR C 91 ? 1.9797 1.9568 2.2453 -0.4749 -1.1052 0.1335 1507 TYR C CE2 13146 C CZ . TYR C 91 ? 2.3407 2.3271 2.6003 -0.4943 -1.1334 0.1222 1507 TYR C CZ 13147 O OH . TYR C 91 ? 2.5286 2.5513 2.7786 -0.4810 -1.1447 0.1277 1507 TYR C OH # 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 ? ? ? A . n A 1 869 ILE 869 869 ? ? ? 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 ? ? ? A . n A 1 956 GLN 956 956 ? ? ? 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 1417 SER SER C . n C 3 2 ASP 2 1418 1418 ASP ASP C . n C 3 3 VAL 3 1419 1419 VAL VAL C . n C 3 4 PRO 4 1420 1420 PRO PRO C . n C 3 5 ARG 5 1421 1421 ARG ARG C . n C 3 6 ASP 6 1422 1422 ASP ASP C . n C 3 7 LEU 7 1423 1423 LEU LEU C . n C 3 8 GLU 8 1424 1424 GLU GLU C . n C 3 9 VAL 9 1425 1425 VAL VAL C . n C 3 10 VAL 10 1426 1426 VAL VAL C . n C 3 11 ALA 11 1427 1427 ALA ALA C . n C 3 12 ALA 12 1428 1428 ALA ALA C . n C 3 13 THR 13 1429 1429 THR THR C . n C 3 14 PRO 14 1430 1430 PRO PRO C . n C 3 15 THR 15 1431 1431 THR THR C . n C 3 16 SER 16 1432 1432 SER SER C . n C 3 17 LEU 17 1433 1433 LEU LEU C . n C 3 18 LEU 18 1434 1434 LEU LEU C . n C 3 19 ILE 19 1435 1435 ILE ILE C . n C 3 20 SER 20 1436 1436 SER SER C . n C 3 21 TRP 21 1437 1437 TRP TRP C . n C 3 22 ASP 22 1438 1438 ASP ASP C . n C 3 23 ALA 23 1439 1439 ALA ALA C . n C 3 24 PRO 24 1440 1440 PRO PRO C . n C 3 25 ALA 25 1441 1441 ALA ALA C . n C 3 26 VAL 26 1442 1442 VAL VAL C . n C 3 27 THR 27 1443 1443 THR THR C . n C 3 28 VAL 28 1444 1444 VAL VAL C . n C 3 29 ARG 29 1445 1445 ARG ARG C . n C 3 30 TYR 30 1446 1446 TYR TYR C . n C 3 31 TYR 31 1447 1447 TYR TYR C . n C 3 32 ARG 32 1448 1448 ARG ARG C . n C 3 33 ILE 33 1449 1449 ILE ILE C . n C 3 34 THR 34 1450 1450 THR THR C . n C 3 35 TYR 35 1451 1451 TYR TYR C . n C 3 36 GLY 36 1452 1452 GLY GLY C . n C 3 37 GLU 37 1453 1453 GLU GLU C . n C 3 38 THR 38 1454 1454 THR THR C . n C 3 39 GLY 39 1455 1455 GLY GLY C . n C 3 40 GLY 40 1456 1456 GLY GLY C . n C 3 41 ASN 41 1457 1457 ASN ASN C . n C 3 42 SER 42 1458 1458 SER SER C . n C 3 43 PRO 43 1459 1459 PRO PRO C . n C 3 44 VAL 44 1460 1460 VAL VAL C . n C 3 45 GLN 45 1461 1461 GLN GLN C . n C 3 46 GLU 46 1462 1462 GLU GLU C . n C 3 47 PHE 47 1463 1463 PHE PHE C . n C 3 48 THR 48 1464 1464 THR THR C . n C 3 49 VAL 49 1465 1465 VAL VAL C . n C 3 50 PRO 50 1466 1466 PRO PRO C . n C 3 51 GLY 51 1467 1467 GLY GLY C . n C 3 52 SER 52 1468 1468 SER SER C . n C 3 53 LYS 53 1469 1469 LYS LYS C . n C 3 54 SER 54 1470 1470 SER SER C . n C 3 55 THR 55 1471 1471 THR THR C . n C 3 56 ALA 56 1472 1472 ALA ALA C . n C 3 57 THR 57 1473 1473 THR THR C . n C 3 58 ILE 58 1474 1474 ILE ILE C . n C 3 59 SER 59 1475 1475 SER SER C . n C 3 60 GLY 60 1476 1476 GLY GLY C . n C 3 61 LEU 61 1477 1477 LEU LEU C . n C 3 62 LYS 62 1478 1478 LYS LYS C . n C 3 63 PRO 63 1479 1479 PRO PRO C . n C 3 64 GLY 64 1480 1480 GLY GLY C . n C 3 65 VAL 65 1481 1481 VAL VAL C . n C 3 66 ASP 66 1482 1482 ASP ASP C . n C 3 67 TYR 67 1483 1483 TYR TYR C . n C 3 68 THR 68 1484 1484 THR THR C . n C 3 69 ILE 69 1485 1485 ILE ILE C . n C 3 70 THR 70 1486 1486 THR THR C . n C 3 71 VAL 71 1487 1487 VAL VAL C . n C 3 72 TYR 72 1488 1488 TYR TYR C . n C 3 73 ALA 73 1489 1489 ALA ALA C . n C 3 74 VAL 74 1490 1490 VAL VAL C . n C 3 75 THR 75 1491 1491 THR THR C . n C 3 76 PRO 76 1492 1492 PRO PRO 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 GLU 82 1498 1498 GLU GLU C . n C 3 83 GLY 83 1499 1499 GLY GLY C . n C 3 84 SER 84 1500 1500 SER SER C . n C 3 85 LYS 85 1501 1501 LYS LYS C . n C 3 86 PRO 86 1502 1502 PRO PRO C . n C 3 87 ILE 87 1503 1503 ILE ILE C . n C 3 88 SER 88 1504 1504 SER SER C . n C 3 89 ILE 89 1505 1505 ILE ILE C . n C 3 90 ASN 90 1506 1506 ASN ASN C . n C 3 91 TYR 91 1507 1507 TYR TYR 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 4 NAG 1 1003 1003 NAG NAG A . G 4 NAG 1 1004 1004 NAG NAG A . H 4 NAG 2 1005 1005 NAG NAG A . I 5 BMA 3 1006 1006 BMA BMA A . J 6 MAN 4 1007 1007 MAN MAN A . K 5 BMA 5 1008 1008 BMA BMA A . L 6 MAN 6 1009 1009 MAN MAN A . M 4 NAG 1 1010 1010 NAG NAG A . N 4 NAG 2 1011 1011 NAG NAG A . O 4 NAG 1 1012 1012 NAG NAG A . P 4 NAG 1 1013 1013 NAG NAG A . Q 4 NAG 1 1014 1014 NAG NAG A . R 4 NAG 2 1015 1015 NAG NAG A . S 4 NAG 1 1016 1016 NAG NAG A . T 4 NAG 1 1017 1017 NAG NAG A . U 7 MN 1 1018 1018 MN MN A . V 7 MN 1 1019 1019 MN MN A . W 7 MN 1 1020 1020 MN MN A . X 7 MN 1 1021 1021 MN MN A . Y 7 MN 1 1022 1022 MN MN A . Z 8 NA 1 1023 1023 NA NA A . AA 9 GOL 1 1024 715 GOL GOL A . BA 4 NAG 1 701 701 NAG NAG B . CA 4 NAG 1 702 702 NAG NAG B . DA 4 NAG 1 703 703 NAG NAG B . EA 4 NAG 2 704 704 NAG NAG B . FA 4 NAG 1 705 705 NAG NAG B . GA 4 NAG 2 706 706 NAG NAG B . HA 5 BMA 3 707 707 BMA BMA B . IA 7 MN 1 708 708 MN MN B . JA 7 MN 1 709 709 MN MN B . KA 7 MN 1 710 710 MN MN B . LA 8 NA 1 711 711 NA NA B . MA 10 CL 1 712 712 CL CL B . NA 10 CL 1 713 713 CL CL B . OA 9 GOL 1 1601 714 GOL GOL C . PA 11 HOH 1 1101 1101 HOH HOH A . PA 11 HOH 2 1102 804 HOH HOH A . QA 11 HOH 1 801 801 HOH HOH B . QA 11 HOH 2 802 802 HOH HOH B . RA 11 HOH 1 1701 803 HOH HOH C . RA 11 HOH 2 1702 1601 HOH HOH C . RA 11 HOH 3 1703 1602 HOH HOH C . RA 11 HOH 4 1704 1603 HOH HOH C . RA 11 HOH 5 1705 1604 HOH HOH C . # 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 458 A ASN 458 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 266 A ASN 266 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 320 B ASN 320 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 821 A ASN 821 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 559 B ASN 559 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 585 A ASN 585 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 943 A ASN 943 ? ASN 'GLYCOSYLATION SITE' 8 A ASN 805 A ASN 805 ? ASN 'GLYCOSYLATION SITE' 9 A ASN 950 A ASN 950 ? ASN 'GLYCOSYLATION SITE' 10 A ASN 44 A ASN 44 ? ASN 'GLYCOSYLATION SITE' 11 A ASN 260 A ASN 260 ? ASN 'GLYCOSYLATION SITE' 12 B ASN 371 B ASN 371 ? ASN 'GLYCOSYLATION SITE' 13 B ASN 99 B ASN 99 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _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 # _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 O ? B PRO 219 ? B PRO 219 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 111.4 ? 2 O ? B PRO 219 ? B PRO 219 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 100.4 ? 3 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 147.4 ? 4 O ? B PRO 219 ? B PRO 219 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 83.4 ? 5 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 101.0 ? 6 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 89.6 ? 7 O ? B PRO 219 ? B PRO 219 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 O ? B ASP 217 ? B ASP 217 ? 1_555 99.2 ? 8 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 O ? B ASP 217 ? B ASP 217 ? 1_555 70.1 ? 9 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 O ? B ASP 217 ? B ASP 217 ? 1_555 98.3 ? 10 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 O ? B ASP 217 ? B ASP 217 ? 1_555 171.0 ? 11 O ? B PRO 219 ? B PRO 219 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 166.3 ? 12 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 82.3 ? 13 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 66.0 ? 14 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 94.5 ? 15 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? KA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 85.0 ? 16 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 162.3 ? 17 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD2 ? A ASP 234 ? A ASP 234 ? 1_555 130.0 ? 18 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD2 ? A ASP 234 ? A ASP 234 ? 1_555 61.9 ? 19 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 83.1 ? 20 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 88.6 ? 21 OD2 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 75.6 ? 22 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASP 230 ? A ASP 230 ? 1_555 99.2 ? 23 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASP 230 ? A ASP 230 ? 1_555 64.4 ? 24 OD2 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASP 230 ? A ASP 230 ? 1_555 122.9 ? 25 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD1 ? A ASP 230 ? A ASP 230 ? 1_555 85.4 ? 26 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 61.3 ? 27 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 134.9 ? 28 OD2 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 97.7 ? 29 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 127.1 ? 30 OD1 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 134.8 ? 31 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 98.9 ? 32 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 84.6 ? 33 OD2 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 114.4 ? 34 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 162.8 ? 35 OD1 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 77.4 ? 36 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? U MN . ? A MN 1018 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 67.3 ? 37 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 147.1 ? 38 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 106.6 ? 39 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 101.6 ? 40 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 94.1 ? 41 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 85.5 ? 42 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 59.8 ? 43 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 85.3 ? 44 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 77.5 ? 45 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 152.0 ? 46 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 146.3 ? 47 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 69.5 ? 48 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 78.3 ? 49 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 137.8 ? 50 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 78.2 ? 51 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 70.0 ? 52 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 ND2 ? A ASN 417 ? A ASN 417 ? 1_555 109.6 ? 53 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 ND2 ? A ASN 417 ? A ASN 417 ? 1_555 83.8 ? 54 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 ND2 ? A ASN 417 ? A ASN 417 ? 1_555 95.7 ? 55 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 ND2 ? A ASN 417 ? A ASN 417 ? 1_555 150.5 ? 56 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 ND2 ? A ASN 417 ? A ASN 417 ? 1_555 56.3 ? 57 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? X MN . ? A MN 1021 ? 1_555 ND2 ? A ASN 417 ? A ASN 417 ? 1_555 125.8 ? 58 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 284 ? A ASP 284 ? 1_555 78.9 ? 59 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 79.9 ? 60 OD1 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 145.7 ? 61 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 107.6 ? 62 OD1 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 101.1 ? 63 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 60.7 ? 64 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 157.3 ? 65 OD1 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 78.4 ? 66 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 120.2 ? 67 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 77.2 ? 68 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 110.5 ? 69 OD1 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 71.9 ? 70 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 141.5 ? 71 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 138.7 ? 72 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 MN ? V MN . ? A MN 1019 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 61.5 ? 73 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 121.9 ? 74 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 127.1 ? 75 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 61.3 ? 76 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 61.4 ? 77 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 171.7 ? 78 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 124.0 ? 79 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 76.3 ? 80 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 68.9 ? 81 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 130.0 ? 82 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 105.9 ? 83 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 68.4 ? 84 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 58.5 ? 85 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 76.2 ? 86 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 127.5 ? 87 O ? A VAL 601 ? A VAL 601 ? 1_555 MN ? Y MN . ? A MN 1022 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 74.5 ? 88 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 81.9 ? 89 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 136.0 ? 90 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 141.3 ? 91 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD1 ? A ASP 351 ? A ASP 351 ? 1_555 84.5 ? 92 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD1 ? A ASP 351 ? A ASP 351 ? 1_555 65.8 ? 93 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD1 ? A ASP 351 ? A ASP 351 ? 1_555 116.6 ? 94 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 82.7 ? 95 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 152.3 ? 96 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 60.7 ? 97 OD1 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 90.0 ? 98 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 60.1 ? 99 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 91.3 ? 100 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 101.2 ? 101 OD1 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 140.9 ? 102 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? W MN . ? A MN 1020 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 100.6 ? 103 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 61.8 ? 104 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 90.2 ? 105 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 60.8 ? 106 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 98.4 ? 107 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 72.3 ? 108 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 120.4 ? 109 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? B MET 335 ? B MET 335 ? 1_555 76.1 ? 110 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? B MET 335 ? B MET 335 ? 1_555 105.5 ? 111 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? B MET 335 ? B MET 335 ? 1_555 61.3 ? 112 O ? B SER 123 ? B SER 123 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? B MET 335 ? B MET 335 ? 1_555 174.4 ? 113 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? RA HOH . ? C HOH 1702 ? 1_555 165.3 ? 114 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? RA HOH . ? C HOH 1702 ? 1_555 116.6 ? 115 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? RA HOH . ? C HOH 1702 ? 1_555 77.2 ? 116 O ? B SER 123 ? B SER 123 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? RA HOH . ? C HOH 1702 ? 1_555 94.6 ? 117 O ? B MET 335 ? B MET 335 ? 1_555 MN ? JA MN . ? B MN 709 ? 1_555 O ? RA HOH . ? C HOH 1702 ? 1_555 90.9 ? 118 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 84.8 ? 119 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 OG ? B SER 121 ? B SER 121 ? 1_555 112.1 ? 120 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 OG ? B SER 121 ? B SER 121 ? 1_555 91.5 ? 121 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? QA HOH . ? B HOH 801 ? 1_555 133.0 ? 122 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? QA HOH . ? B HOH 801 ? 1_555 139.7 ? 123 OG ? B SER 121 ? B SER 121 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? QA HOH . ? B HOH 801 ? 1_555 86.1 ? 124 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? QA HOH . ? B HOH 802 ? 1_555 104.4 ? 125 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? QA HOH . ? B HOH 802 ? 1_555 90.4 ? 126 OG ? B SER 121 ? B SER 121 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? QA HOH . ? B HOH 802 ? 1_555 143.5 ? 127 O ? QA HOH . ? B HOH 801 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? QA HOH . ? B HOH 802 ? 1_555 69.6 ? 128 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? RA HOH . ? C HOH 1701 ? 1_555 150.3 ? 129 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? RA HOH . ? C HOH 1701 ? 1_555 68.0 ? 130 OG ? B SER 121 ? B SER 121 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? RA HOH . ? C HOH 1701 ? 1_555 81.7 ? 131 O ? QA HOH . ? B HOH 801 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? RA HOH . ? C HOH 1701 ? 1_555 71.9 ? 132 O ? QA HOH . ? B HOH 802 ? 1_555 MN ? IA MN . ? B MN 708 ? 1_555 O ? RA HOH . ? C HOH 1701 ? 1_555 65.4 ? 133 O ? A SER 546 ? A SER 546 ? 1_555 NA ? Z NA . ? A NA 1023 ? 1_555 OD1 ? A ASP 544 ? A ASP 544 ? 1_555 116.3 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 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 5.9361 54.9650 23.0087 0.9032 0.3867 0.6384 -0.2360 -0.0663 0.0306 4.4039 3.3991 1.8917 1.2493 0.3367 -0.2429 -0.2103 0.1497 0.3250 -0.0678 0.1581 0.2350 -0.2280 0.0061 0.0465 'X-RAY DIFFRACTION' 2 ? refined -30.0330 47.6911 -1.0324 1.0543 0.8600 1.0424 -0.3840 -0.2154 0.1496 9.2294 0.1651 1.6332 0.9412 3.6584 0.2101 -0.2528 1.1745 0.3171 -0.3495 0.1632 0.2744 -0.1425 0.2098 0.0793 'X-RAY DIFFRACTION' 3 ? refined -46.2994 40.2253 32.1507 1.0067 0.9424 0.9532 0.1417 -0.0567 0.0132 4.3943 1.2775 2.0962 -1.0335 6.2627 -2.1352 -0.5364 0.1314 0.0030 -0.0160 0.3229 0.1578 -0.0698 0.4330 0.2441 'X-RAY DIFFRACTION' 4 ? refined -26.5433 38.1154 72.6980 0.7948 0.3909 0.7571 0.2088 0.0716 -0.0638 6.4173 7.4691 9.7268 -3.3485 4.6699 -4.0745 -0.1940 -0.4610 0.1057 0.6832 0.1767 -0.1089 -0.2419 -0.0371 0.0137 'X-RAY DIFFRACTION' 5 ? refined -2.2408 16.4092 28.8328 1.1142 0.4112 0.8758 -0.1409 0.0202 0.0309 3.0075 2.8476 1.1096 1.4753 0.4265 0.2578 0.1739 -0.0064 -0.7187 0.3978 -0.0397 -0.2968 0.2635 -0.0933 -0.1334 'X-RAY DIFFRACTION' 6 ? refined -37.5583 23.0103 17.3090 1.2437 0.9998 1.2807 -0.2329 -0.0902 0.1339 3.4038 4.4471 6.5570 2.8889 3.8530 5.3107 -0.9108 1.0631 0.6323 -1.0498 0.3825 1.0178 -0.6057 0.7911 0.5277 'X-RAY DIFFRACTION' 7 ? refined -10.2860 14.0472 66.8141 1.1781 0.6523 1.6100 0.3420 -0.0614 0.0759 2.5428 1.3913 5.2053 1.5631 -0.7818 0.9840 0.1355 0.3131 0.9065 0.1143 0.3313 -0.3557 -0.2785 0.0452 -0.4648 'X-RAY DIFFRACTION' 8 ? refined 25.9548 50.2673 56.8835 2.5798 2.2110 2.6981 -0.7070 -0.1116 -0.8229 2.0000 5.7287 2.0000 -6.0184 4.2069 3.5282 0.6966 3.4896 -0.0052 3.8705 1.4597 0.6597 1.4407 4.1719 -2.1560 'X-RAY DIFFRACTION' 9 ? refined 34.9844 37.0235 67.1646 2.5315 2.5887 2.1525 -0.5726 -0.8025 0.9854 6.0885 6.5054 9.5827 6.2329 -1.6829 -2.7888 -0.0494 -1.4343 -2.2800 6.3087 -1.4479 -3.8570 -1.1339 -0.0847 1.4970 'X-RAY DIFFRACTION' 10 ? refined 26.4411 41.4329 61.3633 2.6751 1.1880 1.3055 -0.2345 -0.4745 0.1536 2.0004 6.7362 2.0002 -4.1836 7.8561 -6.5809 -1.1365 -0.7191 0.2373 3.2975 -1.0419 -1.1710 -1.5351 0.1284 2.1768 'X-RAY DIFFRACTION' 11 ? refined 28.9315 37.0120 52.6908 1.7494 1.1313 1.4198 -0.4677 -0.7099 0.4928 2.0001 2.0004 2.0005 0.3278 2.9486 1.3996 -0.3431 -1.2828 -0.4983 1.6237 -0.4708 -1.7683 -0.3990 1.2388 0.8136 'X-RAY DIFFRACTION' 12 ? refined 32.7624 33.9459 53.2167 1.6927 1.1859 1.6216 -0.3604 -0.4268 0.3079 5.8757 9.0172 5.5359 -2.9606 -0.1336 2.6219 -0.1804 0.2445 0.5158 1.0254 0.2808 -1.6808 0.3212 0.5983 -0.0998 'X-RAY DIFFRACTION' 13 ? refined 38.7149 30.3575 61.8406 2.4554 1.4459 2.0378 0.0655 -0.9032 0.4779 2.0000 0.6981 1.3081 -2.4862 -3.6345 0.9515 -0.7898 -1.3752 -0.7782 1.8803 1.4064 0.1091 0.6017 0.0675 -0.6159 'X-RAY DIFFRACTION' 14 ? refined 32.7753 39.9769 53.3488 1.9349 1.2896 1.9154 -0.5568 -0.9316 0.2395 5.2994 7.5297 5.0513 5.5757 -2.2573 0.2331 0.3394 -0.4987 -1.1404 1.8570 -1.7231 -1.5573 -0.3596 0.5666 1.3814 'X-RAY DIFFRACTION' 15 ? refined 28.6498 43.4839 50.4637 1.6790 0.9664 1.4787 -0.2635 -0.5514 0.0494 7.1836 0.9602 8.9261 -2.6135 6.6047 -2.2361 -0.1053 -0.5733 0.9591 1.1894 -0.4838 -2.0933 -1.8782 0.9110 0.5917 # 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 342 ) ; 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 343 through 598 ) ; 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 599 through 764 ) ; 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 765 through 954 ) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 1 through 445 ) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 446 through 606 ) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 607 through 690 ) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1417 through 1421 ) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1422 through 1431 ) ; 'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1432 through 1443 ) ; 'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1444 through 1453 ) ; 'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1454 through 1470 ) ; 'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1471 through 1482 ) ; 'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1483 through 1491 ) ; 'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1492 through 1507 ) ; # 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 SER A 63 ? ? 83.34 -3.24 2 1 ASP A 73 ? ? -95.56 -63.46 3 1 ALA A 74 ? ? 67.96 -2.17 4 1 LYS A 89 ? ? 71.49 -13.64 5 1 GLN A 102 ? ? 54.56 -118.18 6 1 THR A 116 ? ? 69.82 -11.25 7 1 GLU A 117 ? ? 66.89 -4.04 8 1 MET A 118 ? ? -105.38 -74.66 9 1 PRO A 124 ? ? -67.13 74.06 10 1 ILE A 147 ? ? -101.12 -71.31 11 1 LYS A 259 ? ? -109.22 -71.40 12 1 ALA A 273 ? ? 65.90 -3.73 13 1 PHE A 334 ? ? -128.68 -62.68 14 1 ARG A 398 ? ? 60.21 -135.63 15 1 ALA A 411 ? ? 74.32 -3.12 16 1 PHE A 427 ? ? 73.02 -17.48 17 1 THR A 460 ? ? -128.41 -66.32 18 1 LYS A 505 ? ? 44.76 -133.29 19 1 ALA A 507 ? ? 174.39 176.02 20 1 ARG A 510 ? ? 73.47 -16.32 21 1 ARG A 529 ? ? 44.85 -136.01 22 1 ALA A 540 ? ? 34.85 72.79 23 1 PHE A 548 ? ? -121.51 -58.44 24 1 ARG A 549 ? ? 87.26 -7.18 25 1 LYS A 551 ? ? -98.50 -158.21 26 1 LEU A 552 ? ? 62.83 -93.80 27 1 THR A 553 ? ? -38.42 126.35 28 1 TYR A 565 ? ? -55.76 -74.87 29 1 ARG A 566 ? ? 46.71 -110.41 30 1 THR A 572 ? ? 62.30 73.40 31 1 THR A 582 ? ? -177.21 137.94 32 1 ASN A 623 ? ? -175.41 144.76 33 1 ALA A 651 ? ? -57.15 -70.73 34 1 ASP A 652 ? ? 56.64 70.43 35 1 ARG A 665 ? ? 42.96 -147.89 36 1 LEU A 666 ? ? 169.92 174.04 37 1 GLU A 673 ? ? -115.75 -71.65 38 1 GLN A 675 ? ? 62.89 -7.75 39 1 GLN A 703 ? ? 49.47 -143.98 40 1 GLN A 704 ? ? 175.89 178.22 41 1 SER A 705 ? ? 58.58 -101.04 42 1 GLU A 706 ? ? 94.04 -7.38 43 1 THR A 768 ? ? -140.89 -60.26 44 1 GLU A 769 ? ? 85.95 -16.00 45 1 ASN A 805 ? ? 74.62 -2.57 46 1 LEU A 808 ? ? -100.94 -74.34 47 1 MET A 909 ? ? 67.65 -2.77 48 1 ASN A 910 ? ? -99.29 -78.42 49 1 LYS A 911 ? ? -133.79 -69.41 50 1 GLN A 914 ? ? -119.12 -77.48 51 1 GLU A 939 ? ? 63.76 -132.86 52 1 TRP A 953 ? ? -114.60 -71.77 53 1 ASN B 3 ? ? 47.89 -134.93 54 1 ILE B 4 ? ? -127.98 -59.67 55 1 ARG B 8 ? ? 87.16 -7.28 56 1 VAL B 10 ? ? 59.17 71.25 57 1 SER B 11 ? ? -124.17 -70.76 58 1 GLU B 29 ? ? 68.15 -11.11 59 1 SER B 35 ? ? -142.26 57.85 60 1 ARG B 37 ? ? 41.87 -128.85 61 1 ASN B 48 ? ? 64.10 -132.52 62 1 ALA B 50 ? ? -140.25 59.79 63 1 PRO B 51 ? ? -93.38 58.07 64 1 GLU B 52 ? ? 68.59 -1.74 65 1 ASP B 71 ? ? -108.15 -61.63 66 1 ASP B 76 ? ? 50.72 -143.65 67 1 SER B 77 ? ? 42.86 -137.09 68 1 GLN B 79 ? ? 52.68 75.88 69 1 THR B 81 ? ? 43.48 74.24 70 1 SER B 84 ? ? -173.48 137.87 71 1 GLN B 86 ? ? -107.39 -61.19 72 1 GLU B 108 ? ? 40.13 -122.80 73 1 VAL B 157 ? ? -123.11 -73.50 74 1 LEU B 173 ? ? -134.91 -62.57 75 1 TYR B 178 ? ? -122.64 -60.59 76 1 VAL B 193 ? ? -99.10 -62.61 77 1 LYS B 208 ? ? 75.05 -15.53 78 1 ARG B 216 ? ? -100.57 -61.39 79 1 LEU B 258 ? ? 80.18 -7.03 80 1 CYS B 374 ? ? -120.71 -63.21 81 1 ASN B 376 ? ? 41.77 -124.20 82 1 CYS B 406 ? ? -176.14 134.96 83 1 GLU B 409 ? ? -56.77 -4.55 84 1 LYS B 410 ? ? 83.99 3.73 85 1 GLU B 411 ? ? 86.13 -17.25 86 1 LYS B 412 ? ? 45.30 -138.99 87 1 SER B 413 ? ? 174.10 164.41 88 1 LYS B 417 ? ? -174.57 139.21 89 1 ALA B 441 ? ? 59.75 -113.70 90 1 GLU B 442 ? ? 61.18 71.39 91 1 ASN B 444 ? ? -138.46 -76.33 92 1 SER B 445 ? ? -56.99 -75.50 93 1 HIS B 446 ? ? 45.01 -122.69 94 1 ASN B 449 ? ? 56.31 -138.37 95 1 ASN B 452 ? ? 54.27 -141.94 96 1 LEU B 467 ? ? -128.84 -70.23 97 1 CYS B 473 ? ? 58.54 -115.30 98 1 ASP B 477 ? ? 71.06 -116.41 99 1 TYR B 478 ? ? 62.28 78.37 100 1 SER B 481 ? ? -72.02 27.85 101 1 GLN B 482 ? ? -33.91 -39.11 102 1 GLN B 483 ? ? 55.43 -111.74 103 1 GLU B 485 ? ? 74.20 -14.47 104 1 ARG B 489 ? ? 45.21 72.56 105 1 SER B 496 ? ? 69.93 -2.03 106 1 GLN B 497 ? ? 77.45 -19.21 107 1 GLU B 500 ? ? 179.94 -178.66 108 1 CYS B 503 ? ? 68.36 -0.37 109 1 ASP B 512 ? ? 178.34 162.10 110 1 ASP B 524 ? ? 175.81 -177.28 111 1 PHE B 526 ? ? 73.05 -6.32 112 1 TYR B 531 ? ? -110.37 -73.21 113 1 CYS B 536 ? ? 66.47 -0.37 114 1 SER B 537 ? ? 76.54 -2.38 115 1 ILE B 589 ? ? -90.95 -60.08 116 1 LYS B 619 ? ? -100.28 -61.95 117 1 LEU B 625 ? ? 66.51 -9.02 118 1 ARG B 633 ? ? -141.08 -64.19 119 1 GLU B 644 ? ? 59.77 -105.51 120 1 LEU B 645 ? ? 67.20 70.36 121 1 LYS B 650 ? ? 55.43 -116.88 122 1 SER B 673 ? ? 53.31 -132.00 123 1 GLU B 684 ? ? 52.35 73.68 124 1 PRO B 685 ? ? -61.61 -178.52 125 1 VAL C 1426 ? ? -100.29 -65.18 126 1 PRO C 1430 ? ? -59.71 -170.08 127 1 SER C 1432 ? ? 70.72 39.24 128 1 ALA C 1439 ? ? 35.31 69.77 129 1 GLU C 1453 ? ? 37.20 -143.22 130 1 THR C 1454 ? ? -137.79 -73.08 131 1 SER C 1458 ? ? 70.06 147.45 132 1 PRO C 1459 ? ? -115.28 65.50 133 1 VAL C 1460 ? ? -30.41 145.38 134 1 LEU C 1477 ? ? 45.27 -134.53 135 1 VAL C 1481 ? ? 176.48 161.90 136 1 ASP C 1495 ? ? -75.06 -71.52 # loop_ _pdbx_validate_peptide_omega.id _pdbx_validate_peptide_omega.PDB_model_num _pdbx_validate_peptide_omega.auth_comp_id_1 _pdbx_validate_peptide_omega.auth_asym_id_1 _pdbx_validate_peptide_omega.auth_seq_id_1 _pdbx_validate_peptide_omega.PDB_ins_code_1 _pdbx_validate_peptide_omega.label_alt_id_1 _pdbx_validate_peptide_omega.auth_comp_id_2 _pdbx_validate_peptide_omega.auth_asym_id_2 _pdbx_validate_peptide_omega.auth_seq_id_2 _pdbx_validate_peptide_omega.PDB_ins_code_2 _pdbx_validate_peptide_omega.label_alt_id_2 _pdbx_validate_peptide_omega.omega 1 1 ILE A 539 ? ? ALA A 540 ? ? 123.54 2 1 GLU B 476 ? ? ASP B 477 ? ? -135.33 3 1 SER B 481 ? ? GLN B 482 ? ? -146.93 4 1 ASN B 632 ? ? ARG B 633 ? ? 149.44 5 1 TYR C 1451 ? ? GLY C 1452 ? ? 149.44 # 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 ASP 868 ? A ASP 868 34 1 Y 1 A ILE 869 ? A ILE 869 35 1 Y 1 A ILE 955 ? A ILE 955 36 1 Y 1 A GLN 956 ? A GLN 956 37 1 Y 1 A PRO 957 ? A PRO 957 38 1 Y 1 A ALA 958 ? A ALA 958 39 1 Y 1 A PRO 959 ? A PRO 959 40 1 Y 1 B PRO 691 ? B PRO 691 41 1 Y 1 B ASP 692 ? B ASP 692 42 1 Y 1 C ARG 1508 ? C ARG 92 43 1 Y 1 C THR 1509 ? C THR 93 44 1 Y 1 C GLY 1510 ? C GLY 94 45 1 Y 1 C LYS 1511 ? C LYS 95 46 1 Y 1 C LYS 1512 ? C LYS 96 47 1 Y 1 C GLY 1513 ? C GLY 97 48 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 'SODIUM ION' NA 9 GLYCEROL GOL 10 'CHLORIDE ION' CL 11 water HOH #