data_4MMX # _entry.id 4MMX # _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 4MMX RCSB RCSB082111 WWPDB D_1000082111 # 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 4MMY . unspecified PDB 4MMZ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MMX _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 4MMX _cell.length_a 129.859 _cell.length_b 129.859 _cell.length_c 305.831 _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 4MMX _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 10349.573 1 ? ? 'Fibronectin type-III domain 10 (UNP residues 1448-1540)' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 23 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 6 ? ? ? ? 6 non-polymer man ALPHA-D-MANNOSE 180.156 4 ? ? ? ? 7 non-polymer syn 'MANGANESE (II) ION' 54.938 8 ? ? ? ? 8 water nat water 18.015 2 ? ? ? ? # 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 ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDS PASSKPISINYRTGKKGK ; ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDS PASSKPISINYRTGKKGK ; 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 GLY n 3 77 ARG n 3 78 GLY n 3 79 ASP n 3 80 SER n 3 81 PRO n 3 82 ALA n 3 83 SER 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 ? 'Fibronectin, FN, FN1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? plasmid ? ? ? pET ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP ITAV_HUMAN P06756 1 ;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSM PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME YRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYE AELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSS NLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWP YKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCL KIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAP ; 31 ? 2 UNP ITB3_HUMAN P05106 2 ;GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQV TQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKP VSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRN DASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQN YSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIE AKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRP SQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNC TTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIE SVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPD ; 27 ? 3 UNP FINC_HUMAN P02751 3 ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDS PASSKPISINYRT ; 1448 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4MMX A 1 ? 959 ? P06756 31 ? 989 ? 1 959 2 2 4MMX B 1 ? 692 ? P05106 27 ? 718 ? 1 692 3 3 4MMX 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 4MMX GLY C 94 ? UNP P02751 ? ? 'EXPRESSION TAG' 1510 1 3 4MMX LYS C 95 ? UNP P02751 ? ? 'EXPRESSION TAG' 1511 2 3 4MMX LYS C 96 ? UNP P02751 ? ? 'EXPRESSION TAG' 1512 3 3 4MMX GLY C 97 ? UNP P02751 ? ? 'EXPRESSION TAG' 1513 4 3 4MMX LYS C 98 ? UNP P02751 ? ? 'EXPRESSION TAG' 1514 5 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MN non-polymer . 'MANGANESE (II) ION' ? 'Mn 2' 54.938 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4MMX _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.85 _exptl_crystal.density_percent_sol 68.05 _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 2012-10-13 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'sagitally focused Si(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.97921 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 19-ID' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 19-ID _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.97921 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MMX _reflns.observed_criterion_sigma_I 5.3 _reflns.observed_criterion_sigma_F 5.3 _reflns.d_resolution_low 75.49 _reflns.d_resolution_high 3.32 _reflns.number_obs 39593 _reflns.number_all 67157 _reflns.percent_possible_obs 88 _reflns.pdbx_Rmerge_I_obs 0.109 _reflns.pdbx_Rsym_value 0.109 _reflns.pdbx_netI_over_sigmaI 13.9 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.2 _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 3.32 _reflns_shell.d_res_low 3.41 _reflns_shell.percent_possible_all 88.0 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.676 _reflns_shell.meanI_over_sigI_obs 3.3 _reflns_shell.pdbx_redundancy 6.4 _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 4MMX _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 39586 _refine.ls_number_reflns_all 39661 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.38 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 42.506 _refine.ls_d_res_high 3.320 _refine.ls_percent_reflns_obs 88.00 _refine.ls_R_factor_obs 0.2105 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2082 _refine.ls_R_factor_R_free 0.2586 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.91 _refine.ls_number_reflns_R_free 1942 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.42 _refine.pdbx_overall_phase_error 25.86 _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 13184 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 440 _refine_hist.number_atoms_solvent 2 _refine_hist.number_atoms_total 13626 _refine_hist.d_res_high 3.320 _refine_hist.d_res_low 42.506 # 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 0.010 ? ? 14004 'X-RAY DIFFRACTION' ? f_angle_d 0.864 ? ? 18917 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 12.476 ? ? 5175 'X-RAY DIFFRACTION' ? f_chiral_restr 0.035 ? ? 2172 'X-RAY DIFFRACTION' ? f_plane_restr 0.004 ? ? 2445 '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' . 3.3200 3.4030 3003 0.2820 100.00 0.3442 . . 147 . . . . 'X-RAY DIFFRACTION' . 3.4030 3.4950 1356 0.2925 46.00 0.3324 . . 85 . . . . 'X-RAY DIFFRACTION' . 3.4950 3.5978 2984 0.2592 100.00 0.3379 . . 166 . . . . 'X-RAY DIFFRACTION' . 3.5978 3.7138 1222 0.2532 40.00 0.3559 . . 47 . . . . 'X-RAY DIFFRACTION' . 3.7138 3.8465 3018 0.2494 100.00 0.2879 . . 127 . . . . 'X-RAY DIFFRACTION' . 3.8465 4.0004 1431 0.2311 47.00 0.3271 . . 82 . . . . 'X-RAY DIFFRACTION' . 4.0004 4.1823 3046 0.2132 100.00 0.2318 . . 152 . . . . 'X-RAY DIFFRACTION' . 4.1823 4.4026 3033 0.1915 100.00 0.2255 . . 138 . . . . 'X-RAY DIFFRACTION' . 4.4026 4.6781 3029 0.1674 100.00 0.2187 . . 173 . . . . 'X-RAY DIFFRACTION' . 4.6781 5.0388 3027 0.1677 100.00 0.2214 . . 175 . . . . 'X-RAY DIFFRACTION' . 5.0388 5.5449 3037 0.1891 100.00 0.2432 . . 184 . . . . 'X-RAY DIFFRACTION' . 5.5449 6.3449 3077 0.2188 100.00 0.2768 . . 159 . . . . 'X-RAY DIFFRACTION' . 6.3449 7.9853 3125 0.2272 100.00 0.2866 . . 168 . . . . 'X-RAY DIFFRACTION' . 7.9853 42.5099 3256 0.1941 99.00 0.2317 . . 139 . . . . # _struct.entry_id 4MMX _struct.title 'Integrin AlphaVBeta3 ectodomain bound to the 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 4MMX _struct_keywords.pdbx_keywords 'CELL ADHESION' _struct_keywords.text ;integrin, A domain, hybrid domain, PSI, EGF repeats, beta TA thigh, beta propeller, RGD motif, fibronectin, vitronectin, CELL ADHESION ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 5 ? G N N 6 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 4 ? L N N 5 ? M N N 6 ? N N N 5 ? O N N 6 ? P N N 4 ? Q N N 4 ? R N N 5 ? S N N 6 ? T N N 4 ? U N N 4 ? V N N 4 ? W N N 4 ? X N N 4 ? Y N N 4 ? Z N N 4 ? AA N N 4 ? BA N N 4 ? CA N N 5 ? DA N N 7 ? EA N N 7 ? FA N N 7 ? GA N N 7 ? HA N N 7 ? IA N N 4 ? JA N N 4 ? KA N N 4 ? LA N N 4 ? MA N N 4 ? NA N N 4 ? OA N N 5 ? PA N N 7 ? QA N N 7 ? RA N N 7 ? SA N N 8 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLY A 175 ? GLN A 180 ? GLY A 175 GLN A 180 1 ? 6 HELX_P HELX_P2 2 VAL A 188 ? LYS A 194 ? VAL A 188 LYS A 194 1 ? 7 HELX_P HELX_P3 3 GLN A 214 ? ASP A 218 ? GLN A 214 ASP A 218 5 ? 5 HELX_P HELX_P4 4 GLY A 366 ? LYS A 370 ? GLY A 366 LYS A 370 5 ? 5 HELX_P HELX_P5 5 ASP A 544 ? PHE A 548 ? ASP A 544 PHE A 548 5 ? 5 HELX_P HELX_P6 6 THR A 768 ? VAL A 772 ? THR A 768 VAL A 772 5 ? 5 HELX_P HELX_P7 7 ARG B 8 ? SER B 12 ? ARG B 8 SER B 12 5 ? 5 HELX_P HELX_P8 8 CYS B 13 ? ALA B 18 ? CYS B 13 ALA B 18 1 ? 6 HELX_P HELX_P9 9 GLU B 42 ? ASP B 47 ? GLU B 42 ASP B 47 1 ? 6 HELX_P HELX_P10 10 SER B 121 ? LYS B 125 ? SER B 121 LYS B 125 5 ? 5 HELX_P HELX_P11 11 ASP B 127 ? ILE B 131 ? ASP B 127 ILE B 131 5 ? 5 HELX_P HELX_P12 12 LEU B 134 ? ARG B 143 ? LEU B 134 ARG B 143 1 ? 10 HELX_P HELX_P13 13 PRO B 170 ? ASN B 175 ? PRO B 170 ASN B 175 1 ? 6 HELX_P HELX_P14 14 TYR B 178 ? THR B 182 ? TYR B 178 THR B 182 5 ? 5 HELX_P HELX_P15 15 VAL B 200 ? LYS B 209 ? VAL B 200 LYS B 209 1 ? 10 HELX_P HELX_P16 16 GLY B 222 ? CYS B 232 ? GLY B 222 CYS B 232 1 ? 11 HELX_P HELX_P17 17 CYS B 232 ? GLY B 237 ? CYS B 232 GLY B 237 1 ? 6 HELX_P HELX_P18 18 LEU B 258 ? LEU B 262 ? LEU B 258 LEU B 262 5 ? 5 HELX_P HELX_P19 19 SER B 291 ? LYS B 302 ? SER B 291 LYS B 302 1 ? 12 HELX_P HELX_P20 20 VAL B 314 ? ILE B 325 ? VAL B 314 ILE B 325 1 ? 12 HELX_P HELX_P21 21 SER B 338 ? ARG B 352 ? SER B 338 ARG B 352 1 ? 15 HELX_P HELX_P22 22 CYS B 435 ? ALA B 439 ? CYS B 435 ALA B 439 5 ? 5 HELX_P HELX_P23 23 GLU B 534 ? GLY B 538 ? GLU B 534 GLY B 538 5 ? 5 HELX_P HELX_P24 24 THR B 564 ? MET B 568 ? THR B 564 MET B 568 5 ? 5 HELX_P HELX_P25 25 LEU B 573 ? GLY B 577 ? LEU B 573 GLY B 577 5 ? 5 HELX_P HELX_P26 26 ALA B 607 ? LYS B 619 ? ALA B 607 LYS B 619 1 ? 13 HELX_P HELX_P27 27 THR B 630 ? CYS B 635 ? THR B 630 CYS B 635 1 ? 6 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 59 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 59 A CYS 67 1_555 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? A CYS 108 SG ? ? ? 1_555 A CYS 128 SG ? ? A CYS 108 A CYS 128 1_555 ? ? ? ? ? ? ? 2.030 ? disulf3 disulf ? ? A CYS 142 SG ? ? ? 1_555 A CYS 155 SG ? ? A CYS 142 A CYS 155 1_555 ? ? ? ? ? ? ? 2.029 ? disulf4 disulf ? ? A CYS 461 SG ? ? ? 1_555 A CYS 472 SG ? ? A CYS 461 A CYS 472 1_555 ? ? ? ? ? ? ? 2.028 ? disulf5 disulf ? ? A CYS 478 SG ? ? ? 1_555 A CYS 535 SG ? ? A CYS 478 A CYS 535 1_555 ? ? ? ? ? ? ? 2.031 ? disulf6 disulf ? ? A CYS 596 SG ? ? ? 1_555 A CYS 602 SG ? ? A CYS 596 A CYS 602 1_555 ? ? ? ? ? ? ? 2.032 ? disulf7 disulf ? ? A CYS 668 SG ? ? ? 1_555 A CYS 681 SG ? ? A CYS 668 A CYS 681 1_555 ? ? ? ? ? ? ? 2.031 ? disulf8 disulf ? ? A CYS 822 SG ? ? ? 1_555 A CYS 884 SG ? ? A CYS 822 A CYS 884 1_555 ? ? ? ? ? ? ? 2.030 ? disulf9 disulf ? ? A CYS 874 SG ? ? ? 1_555 A CYS 879 SG ? ? A CYS 874 A CYS 879 1_555 ? ? ? ? ? ? ? 2.031 ? disulf10 disulf ? ? B CYS 5 SG ? ? ? 1_555 B CYS 23 SG ? ? B CYS 5 B CYS 23 1_555 ? ? ? ? ? ? ? 2.029 ? disulf11 disulf ? ? B CYS 13 SG ? ? ? 1_555 B CYS 435 SG ? ? B CYS 13 B CYS 435 1_555 ? ? ? ? ? ? ? 2.032 ? disulf12 disulf ? ? B CYS 16 SG ? ? ? 1_555 B CYS 38 SG ? ? B CYS 16 B CYS 38 1_555 ? ? ? ? ? ? ? 2.030 ? disulf13 disulf ? ? B CYS 26 SG ? ? ? 1_555 B CYS 49 SG ? ? B CYS 26 B CYS 49 1_555 ? ? ? ? ? ? ? 2.030 ? disulf14 disulf ? ? B CYS 177 SG ? ? ? 1_555 B CYS 184 SG ? ? B CYS 177 B CYS 184 1_555 ? ? ? ? ? ? ? 2.032 ? disulf15 disulf ? ? B CYS 232 SG ? ? ? 1_555 B CYS 273 SG ? ? B CYS 232 B CYS 273 1_555 ? ? ? ? ? ? ? 2.031 ? disulf16 disulf ? ? B CYS 374 SG ? ? ? 1_555 B CYS 386 SG ? ? B CYS 374 B CYS 386 1_555 ? ? ? ? ? ? ? 2.031 ? disulf17 disulf ? ? B CYS 406 SG ? ? ? 1_555 B CYS 433 SG ? ? B CYS 406 B CYS 433 1_555 ? ? ? ? ? ? ? 2.032 ? disulf18 disulf ? ? B CYS 437 SG ? ? ? 1_555 B CYS 457 SG ? ? B CYS 437 B CYS 457 1_555 ? ? ? ? ? ? ? 2.032 ? disulf19 disulf ? ? B CYS 448 SG ? ? ? 1_555 B CYS 460 SG ? ? B CYS 448 B CYS 460 1_555 ? ? ? ? ? ? ? 2.031 ? disulf20 disulf ? ? B CYS 462 SG ? ? ? 1_555 B CYS 471 SG ? ? B CYS 462 B CYS 471 1_555 ? ? ? ? ? ? ? 2.032 ? disulf21 disulf ? ? B CYS 473 SG ? ? ? 1_555 B CYS 503 SG ? ? B CYS 473 B CYS 503 1_555 ? ? ? ? ? ? ? 2.034 ? disulf22 disulf ? ? B CYS 486 SG ? ? ? 1_555 B CYS 501 SG ? ? B CYS 486 B CYS 501 1_555 ? ? ? ? ? ? ? 2.035 ? disulf23 disulf ? ? B CYS 495 SG ? ? ? 1_555 B CYS 506 SG ? ? B CYS 495 B CYS 506 1_555 ? ? ? ? ? ? ? 2.031 ? disulf24 disulf ? ? B CYS 508 SG ? ? ? 1_555 B CYS 521 SG ? ? B CYS 508 B CYS 521 1_555 ? ? ? ? ? ? ? 2.037 ? disulf25 disulf ? ? B CYS 523 SG ? ? ? 1_555 B CYS 544 SG ? ? B CYS 523 B CYS 544 1_555 ? ? ? ? ? ? ? 2.032 ? disulf26 disulf ? ? B CYS 528 SG ? ? ? 1_555 B CYS 542 SG ? ? B CYS 528 B CYS 542 1_555 ? ? ? ? ? ? ? 2.033 ? disulf27 disulf ? ? B CYS 536 SG ? ? ? 1_555 B CYS 547 SG ? ? B CYS 536 B CYS 547 1_555 ? ? ? ? ? ? ? 2.032 ? disulf28 disulf ? ? B CYS 549 SG ? ? ? 1_555 B CYS 558 SG ? ? B CYS 549 B CYS 558 1_555 ? ? ? ? ? ? ? 2.031 ? disulf29 disulf ? ? B CYS 560 SG ? ? ? 1_555 B CYS 583 SG ? ? B CYS 560 B CYS 583 1_555 ? ? ? ? ? ? ? 2.032 ? disulf30 disulf ? ? B CYS 567 SG ? ? ? 1_555 B CYS 581 SG ? ? B CYS 567 B CYS 581 1_555 ? ? ? ? ? ? ? 2.031 ? disulf31 disulf ? ? B CYS 575 SG ? ? ? 1_555 B CYS 586 SG ? ? B CYS 575 B CYS 586 1_555 ? ? ? ? ? ? ? 2.032 ? disulf32 disulf ? ? B CYS 588 SG ? ? ? 1_555 B CYS 598 SG ? ? B CYS 588 B CYS 598 1_555 ? ? ? ? ? ? ? 2.031 ? disulf33 disulf ? ? B CYS 601 SG ? ? ? 1_555 B CYS 604 SG ? ? B CYS 601 B CYS 604 1_555 ? ? ? ? ? ? ? 2.032 ? disulf34 disulf ? ? B CYS 608 SG ? ? ? 1_555 B CYS 655 SG ? ? B CYS 608 B CYS 655 1_555 ? ? ? ? ? ? ? 2.033 ? disulf35 disulf ? ? B CYS 614 SG ? ? ? 1_555 B CYS 635 SG ? ? B CYS 614 B CYS 635 1_555 ? ? ? ? ? ? ? 2.032 ? disulf36 disulf ? ? B CYS 617 SG ? ? ? 1_555 B CYS 631 SG ? ? B CYS 617 B CYS 631 1_555 ? ? ? ? ? ? ? 2.031 ? disulf37 disulf ? ? B CYS 663 SG ? ? ? 1_555 B CYS 687 SG ? ? B CYS 663 B CYS 687 1_555 ? ? ? ? ? ? ? 2.031 ? covale1 covale ? ? A ASN 266 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 266 A NAG 1007 1_555 ? ? ? ? ? ? ? 1.434 ? covale2 covale ? ? B ASN 371 ND2 ? ? ? 1_555 KA NAG . C1 ? ? B ASN 371 B NAG 703 1_555 ? ? ? ? ? ? ? 1.435 ? covale3 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 1007 A NAG 1008 1_555 ? ? ? ? ? ? ? 1.436 ? covale4 covale ? ? A ASN 943 ND2 ? ? ? 1_555 Y NAG . C1 ? ? A ASN 943 A NAG 1022 1_555 ? ? ? ? ? ? ? 1.437 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1001 A NAG 1002 1_555 ? ? ? ? ? ? ? 1.438 ? covale6 covale ? ? A ASN 260 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 260 A NAG 1005 1_555 ? ? ? ? ? ? ? 1.438 ? covale7 covale ? ? A ASN 585 ND2 ? ? ? 1_555 U NAG . C1 ? ? A ASN 585 A NAG 1018 1_555 ? ? ? ? ? ? ? 1.438 ? covale8 covale ? ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 1002 A BMA 1003 1_555 ? ? ? ? ? ? ? 1.438 ? covale9 covale ? ? A ASN 458 ND2 ? ? ? 1_555 P NAG . C1 ? ? A ASN 458 A NAG 1013 1_555 ? ? ? ? ? ? ? 1.438 ? covale10 covale ? ? K NAG . O4 ? ? ? 1_555 L BMA . C1 ? ? A NAG 1008 A BMA 1009 1_555 ? ? ? ? ? ? ? 1.438 ? covale11 covale ? ? B ASN 320 ND2 ? ? ? 1_555 JA NAG . C1 ? ? B ASN 320 B NAG 702 1_555 ? ? ? ? ? ? ? 1.439 ? covale12 covale ? ? P NAG . O4 ? ? ? 1_555 Q NAG . C1 ? ? A NAG 1013 A NAG 1014 1_555 ? ? ? ? ? ? ? 1.439 ? covale13 covale ? ? L BMA . O3 ? ? ? 1_555 M MAN . C1 ? ? A BMA 1009 A MAN 1010 1_555 ? ? ? ? ? ? ? 1.439 ? covale14 covale ? ? KA NAG . O4 ? ? ? 1_555 LA NAG . C1 ? ? B NAG 703 B NAG 704 1_555 ? ? ? ? ? ? ? 1.440 ? covale15 covale ? ? A ASN 950 ND2 ? ? ? 1_555 AA NAG . C1 ? ? A ASN 950 A NAG 1024 1_555 ? ? ? ? ? ? ? 1.440 ? covale16 covale ? ? B ASN 559 ND2 ? ? ? 1_555 MA NAG . C1 ? ? B ASN 559 B NAG 705 1_555 ? ? ? ? ? ? ? 1.440 ? covale17 covale ? ? AA NAG . O4 ? ? ? 1_555 BA NAG . C1 ? ? A NAG 1024 A NAG 1025 1_555 ? ? ? ? ? ? ? 1.440 ? covale18 covale ? ? R BMA . O3 ? ? ? 1_555 S MAN . C1 ? ? A BMA 1015 A MAN 1016 1_555 ? ? ? ? ? ? ? 1.440 ? covale19 covale ? ? A ASN 821 ND2 ? ? ? 1_555 X NAG . C1 ? ? A ASN 821 A NAG 1021 1_555 ? ? ? ? ? ? ? 1.440 ? covale20 covale ? ? A ASN 44 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 44 A NAG 1001 1_555 ? ? ? ? ? ? ? 1.441 ? covale21 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 1005 A NAG 1006 1_555 ? ? ? ? ? ? ? 1.441 ? covale22 covale ? ? Q NAG . O4 ? ? ? 1_555 R BMA . C1 ? ? A NAG 1014 A BMA 1015 1_555 ? ? ? ? ? ? ? 1.441 ? covale23 covale ? ? A ASN 524 ND2 ? ? ? 1_555 T NAG . C1 ? ? A ASN 524 A NAG 1017 1_555 ? ? ? ? ? ? ? 1.441 ? covale24 covale ? ? B ASN 99 ND2 ? ? ? 1_555 IA NAG . C1 ? ? B ASN 99 B NAG 701 1_555 ? ? ? ? ? ? ? 1.441 ? covale25 covale ? ? U NAG . O4 ? ? ? 1_555 V NAG . C1 ? ? A NAG 1018 A NAG 1019 1_555 ? ? ? ? ? ? ? 1.442 ? covale26 covale ? ? BA NAG . O4 ? ? ? 1_555 CA BMA . C1 ? ? A NAG 1025 A BMA 1026 1_555 ? ? ? ? ? ? ? 1.443 ? covale27 covale ? ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 1003 A MAN 1004 1_555 ? ? ? ? ? ? ? 1.443 ? covale28 covale ? ? Y NAG . O4 ? ? ? 1_555 Z NAG . C1 ? ? A NAG 1022 A NAG 1023 1_555 ? ? ? ? ? ? ? 1.443 ? covale29 covale ? ? NA NAG . O4 ? ? ? 1_555 OA BMA . C1 ? ? B NAG 706 B BMA 707 1_555 ? ? ? ? ? ? ? 1.444 ? covale30 covale ? ? MA NAG . O4 ? ? ? 1_555 NA NAG . C1 ? ? B NAG 705 B NAG 706 1_555 ? ? ? ? ? ? ? 1.445 ? covale31 covale ? ? A ASN 674 ND2 ? ? ? 1_555 W NAG . C1 ? ? A ASN 674 A NAG 1020 1_555 ? ? ? ? ? ? ? 1.447 ? covale32 covale ? ? L BMA . O6 ? ? ? 1_555 N BMA . C1 ? ? A BMA 1009 A BMA 1011 1_555 ? ? ? ? ? ? ? 1.447 ? covale33 covale ? ? N BMA . O4 ? ? ? 1_555 O MAN . C1 ? ? A BMA 1011 A MAN 1012 1_555 ? ? ? ? ? ? ? 1.452 ? metalc1 metalc ? ? A TYR 290 O ? ? ? 1_555 EA MN . MN ? ? A TYR 290 A MN 1028 1_555 ? ? ? ? ? ? ? 2.053 ? metalc2 metalc ? ? A TYR 419 O ? ? ? 1_555 GA MN . MN ? ? A TYR 419 A MN 1030 1_555 ? ? ? ? ? ? ? 2.077 ? metalc3 metalc ? ? B ASP 217 O ? ? ? 1_555 RA MN . MN ? ? B ASP 217 B MN 710 1_555 ? ? ? ? ? ? ? 2.123 ? metalc4 metalc ? ? A ASN 232 OD1 ? ? ? 1_555 DA MN . MN ? ? A ASN 232 A MN 1027 1_555 ? ? ? ? ? ? ? 2.127 ? metalc5 metalc ? ? B ASP 217 OD1 ? ? ? 1_555 RA MN . MN ? ? B ASP 217 B MN 710 1_555 ? ? ? ? ? ? ? 2.131 ? metalc6 metalc ? ? B GLU 220 OE1 ? ? ? 1_555 PA MN . MN ? ? B GLU 220 B MN 708 1_555 ? ? ? ? ? ? ? 2.133 ? metalc7 metalc ? ? C ASP 79 OD1 ? ? ? 1_555 PA MN . MN ? ? C ASP 1495 B MN 708 1_555 ? ? ? ? ? ? ? 2.141 ? metalc8 metalc ? ? B ASP 126 OD1 ? ? ? 1_555 QA MN . MN ? ? B ASP 126 B MN 709 1_555 ? ? ? ? ? ? ? 2.144 ? metalc9 metalc ? ? B ASP 127 OD1 ? ? ? 1_555 QA MN . MN ? ? B ASP 127 B MN 709 1_555 ? ? ? ? ? ? ? 2.147 ? metalc10 metalc ? ? B ASP 251 OD1 ? ? ? 1_555 QA MN . MN ? ? B ASP 251 B MN 709 1_555 ? ? ? ? ? ? ? 2.149 ? metalc11 metalc ? ? A ASP 413 OD1 ? ? ? 1_555 GA MN . MN ? ? A ASP 413 A MN 1030 1_555 ? ? ? ? ? ? ? 2.149 ? metalc12 metalc ? ? A ASP 284 OD2 ? ? ? 1_555 EA MN . MN ? ? A ASP 284 A MN 1028 1_555 ? ? ? ? ? ? ? 2.150 ? metalc13 metalc ? ? B ASP 251 OD2 ? ? ? 1_555 QA MN . MN ? ? B ASP 251 B MN 709 1_555 ? ? ? ? ? ? ? 2.153 ? metalc14 metalc ? ? A ASP 599 OD1 ? ? ? 1_555 HA MN . MN ? ? A ASP 599 A MN 1031 1_555 ? ? ? ? ? ? ? 2.155 ? metalc15 metalc ? ? A ASP 353 OD2 ? ? ? 1_555 FA MN . MN ? ? A ASP 353 A MN 1029 1_555 ? ? ? ? ? ? ? 2.155 ? metalc16 metalc ? ? A ASP 349 OD1 ? ? ? 1_555 FA MN . MN ? ? A ASP 349 A MN 1029 1_555 ? ? ? ? ? ? ? 2.155 ? metalc17 metalc ? ? A ASP 234 OD1 ? ? ? 1_555 DA MN . MN ? ? A ASP 234 A MN 1027 1_555 ? ? ? ? ? ? ? 2.156 ? metalc18 metalc ? ? A ASP 599 OD2 ? ? ? 1_555 HA MN . MN ? ? A ASP 599 A MN 1031 1_555 ? ? ? ? ? ? ? 2.156 ? metalc19 metalc ? ? A GLU 636 OE1 ? ? ? 1_555 HA MN . MN ? ? A GLU 636 A MN 1031 1_555 ? ? ? ? ? ? ? 2.157 ? metalc20 metalc ? ? A GLU 636 OE2 ? ? ? 1_555 HA MN . MN ? ? A GLU 636 A MN 1031 1_555 ? ? ? ? ? ? ? 2.157 ? metalc21 metalc ? ? B ASP 126 OD2 ? ? ? 1_555 QA MN . MN ? ? B ASP 126 B MN 709 1_555 ? ? ? ? ? ? ? 2.158 ? metalc22 metalc ? ? A ASP 357 OD1 ? ? ? 1_555 FA MN . MN ? ? A ASP 357 A MN 1029 1_555 ? ? ? ? ? ? ? 2.160 ? metalc23 metalc ? ? A ASP 351 OD2 ? ? ? 1_555 FA MN . MN ? ? A ASP 351 A MN 1029 1_555 ? ? ? ? ? ? ? 2.161 ? metalc24 metalc ? ? A ASP 353 OD1 ? ? ? 1_555 FA MN . MN ? ? A ASP 353 A MN 1029 1_555 ? ? ? ? ? ? ? 2.162 ? metalc25 metalc ? ? A ASP 238 OD2 ? ? ? 1_555 DA MN . MN ? ? A ASP 238 A MN 1027 1_555 ? ? ? ? ? ? ? 2.162 ? metalc26 metalc ? ? B SER 123 OG ? ? ? 1_555 PA MN . MN ? ? B SER 123 B MN 708 1_555 ? ? ? ? ? ? ? 2.163 ? metalc27 metalc ? ? A ASP 238 OD1 ? ? ? 1_555 DA MN . MN ? ? A ASP 238 A MN 1027 1_555 ? ? ? ? ? ? ? 2.165 ? metalc28 metalc ? ? A ASP 357 OD2 ? ? ? 1_555 FA MN . MN ? ? A ASP 357 A MN 1029 1_555 ? ? ? ? ? ? ? 2.166 ? metalc29 metalc ? ? A ASP 421 OD2 ? ? ? 1_555 GA MN . MN ? ? A ASP 421 A MN 1030 1_555 ? ? ? ? ? ? ? 2.166 ? metalc30 metalc ? ? A ASP 421 OD1 ? ? ? 1_555 GA MN . MN ? ? A ASP 421 A MN 1030 1_555 ? ? ? ? ? ? ? 2.166 ? metalc31 metalc ? ? A ASP 292 OD1 ? ? ? 1_555 EA MN . MN ? ? A ASP 292 A MN 1028 1_555 ? ? ? ? ? ? ? 2.168 ? metalc32 metalc ? ? A ASN 286 OD1 ? ? ? 1_555 EA MN . MN ? ? A ASN 286 A MN 1028 1_555 ? ? ? ? ? ? ? 2.171 ? metalc33 metalc ? ? B GLU 220 OE2 ? ? ? 1_555 RA MN . MN ? ? B GLU 220 B MN 710 1_555 ? ? ? ? ? ? ? 2.171 ? metalc34 metalc ? ? B SER 121 OG ? ? ? 1_555 PA MN . MN ? ? B SER 121 B MN 708 1_555 ? ? ? ? ? ? ? 2.173 ? metalc35 metalc ? ? B SER 123 O ? ? ? 1_555 QA MN . MN ? ? B SER 123 B MN 709 1_555 ? ? ? ? ? ? ? 2.174 ? metalc36 metalc ? ? A ASP 292 OD2 ? ? ? 1_555 EA MN . MN ? ? A ASP 292 A MN 1028 1_555 ? ? ? ? ? ? ? 2.174 ? metalc37 metalc ? ? A ASP 415 OD2 ? ? ? 1_555 GA MN . MN ? ? A ASP 415 A MN 1030 1_555 ? ? ? ? ? ? ? 2.176 ? metalc38 metalc ? ? B ASP 158 OD2 ? ? ? 1_555 RA MN . MN ? ? B ASP 158 B MN 710 1_555 ? ? ? ? ? ? ? 2.177 ? metalc39 metalc ? ? B ASN 215 OD1 ? ? ? 1_555 RA MN . MN ? ? B ASN 215 B MN 710 1_555 ? ? ? ? ? ? ? 2.179 ? metalc40 metalc ? ? A ASP 288 OD1 ? ? ? 1_555 EA MN . MN ? ? A ASP 288 A MN 1028 1_555 ? ? ? ? ? ? ? 2.180 ? metalc41 metalc ? ? A ASP 230 OD2 ? ? ? 1_555 DA MN . MN ? ? A ASP 230 A MN 1027 1_555 ? ? ? ? ? ? ? 2.183 ? metalc42 metalc ? ? A ASN 417 OD1 ? ? ? 1_555 GA MN . MN ? ? A ASN 417 A MN 1030 1_555 ? ? ? ? ? ? ? 2.188 ? metalc43 metalc ? ? A CYS 596 O ? ? ? 1_555 HA MN . MN ? ? A CYS 596 A MN 1031 1_555 ? ? ? ? ? ? ? 2.199 ? metalc44 metalc ? ? A VAL 601 O ? ? ? 1_555 HA MN . MN ? ? A VAL 601 A MN 1031 1_555 ? ? ? ? ? ? ? 2.264 ? metalc45 metalc ? ? A ILE 236 O ? ? ? 1_555 DA MN . MN ? ? A ILE 236 A MN 1027 1_555 ? ? ? ? ? ? ? 2.286 ? metalc46 metalc ? ? A PHE 355 O ? ? ? 1_555 FA MN . MN ? ? A PHE 355 A MN 1029 1_555 ? ? ? ? ? ? ? 2.381 ? metalc47 metalc ? ? B PRO 219 O ? ? ? 1_555 RA MN . MN ? ? B PRO 219 B MN 710 1_555 ? ? ? ? ? ? ? 2.407 ? metalc48 metalc ? ? PA MN . MN ? ? ? 1_555 SA HOH . O ? ? B MN 708 B HOH 802 1_555 ? ? ? ? ? ? ? 2.189 ? metalc49 metalc ? ? PA MN . MN ? ? ? 1_555 SA HOH . O ? ? B MN 708 B HOH 801 1_555 ? ? ? ? ? ? ? 2.195 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 685 A . ? ASN 685 A PRO 686 A ? PRO 686 A 1 -0.21 2 SER 749 A . ? SER 749 A PRO 750 A ? PRO 750 A 1 -0.98 3 LEU 755 A . ? LEU 755 A PRO 756 A ? PRO 756 A 1 -0.51 4 SER 84 B . ? SER 84 B PRO 85 B ? PRO 85 B 1 -0.65 # 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 ? 4 ? N ? 6 ? O ? 4 ? P ? 6 ? Q ? 4 ? R ? 6 ? S ? 4 ? T ? 6 ? U ? 2 ? V ? 2 ? W ? 2 ? X ? 4 ? Y ? 3 ? Z ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel H 1 2 ? anti-parallel I 1 2 ? anti-parallel I 2 3 ? anti-parallel I 3 4 ? anti-parallel J 1 2 ? anti-parallel K 1 2 ? anti-parallel K 2 3 ? anti-parallel K 3 4 ? anti-parallel L 1 2 ? parallel L 2 3 ? anti-parallel L 3 4 ? anti-parallel L 4 5 ? anti-parallel M 1 2 ? anti-parallel M 2 3 ? anti-parallel M 3 4 ? anti-parallel N 1 2 ? parallel N 2 3 ? anti-parallel N 3 4 ? anti-parallel N 4 5 ? anti-parallel N 5 6 ? anti-parallel O 1 2 ? anti-parallel O 2 3 ? anti-parallel O 3 4 ? anti-parallel P 1 2 ? parallel P 2 3 ? anti-parallel P 3 4 ? anti-parallel P 4 5 ? anti-parallel P 5 6 ? anti-parallel Q 1 2 ? anti-parallel Q 2 3 ? anti-parallel Q 3 4 ? parallel R 1 2 ? anti-parallel R 2 3 ? 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 ? anti-parallel T 1 2 ? anti-parallel T 2 3 ? parallel T 3 4 ? parallel T 4 5 ? parallel T 5 6 ? parallel U 1 2 ? anti-parallel V 1 2 ? anti-parallel W 1 2 ? anti-parallel X 1 2 ? parallel X 2 3 ? anti-parallel X 3 4 ? anti-parallel Y 1 2 ? anti-parallel Y 2 3 ? anti-parallel Z 1 2 ? anti-parallel Z 2 3 ? anti-parallel Z 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 LEU A 3 ? SER A 12 ? LEU A 3 SER A 12 A 2 ARG A 431 ? ALA A 437 ? ARG A 431 ALA A 437 A 3 ASP A 421 ? ALA A 426 ? ASP A 421 ALA A 426 A 4 SER A 407 ? THR A 412 ? SER A 407 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 ? ILE A 70 ? CYS A 67 ILE A 70 C 1 ASP A 79 ? ALA A 81 ? ASP A 79 ALA A 81 C 2 ASP A 84 ? PRO A 85 ? ASP A 84 PRO A 85 D 1 VAL A 98 ? LYS A 101 ? VAL A 98 LYS A 101 D 2 LYS A 104 ? ALA A 109 ? LYS A 104 ALA A 109 D 3 THR A 127 ? ASP A 132 ? THR A 127 ASP A 132 D 4 LYS A 135 ? TYR A 139 ? LYS A 135 TYR A 139 E 1 SER A 160 ? PHE A 163 ? SER A 160 PHE A 163 E 2 ARG A 168 ? GLY A 173 ? ARG A 168 GLY A 173 E 3 GLN A 182 ? GLN A 187 ? GLN A 182 GLN A 187 E 4 LEU A 208 ? ALA A 209 ? LEU A 208 ALA A 209 F 1 SER A 225 ? GLY A 229 ? SER A 225 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 ? GLY A 348 ? ALA A 343 GLY A 348 I 2 ASP A 357 ? ALA A 362 ? ASP A 357 ALA A 362 I 3 ILE A 372 ? PHE A 376 ? ILE A 372 PHE A 376 I 4 GLN A 389 ? 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 THR A 442 ? VAL A 449 ? THR A 442 VAL A 449 K 2 SER A 471 ? ASP A 482 ? SER A 471 ASP A 482 K 3 GLN A 534 ? LEU A 542 ? GLN A 534 LEU A 542 K 4 ALA A 511 ? PHE A 513 ? ALA A 511 PHE A 513 L 1 ILE A 453 ? LEU A 454 ? ILE A 453 LEU A 454 L 2 ASN A 585 ? ILE A 592 ? ASN A 585 ILE A 592 L 3 ILE A 555 ? TYR A 561 ? ILE A 555 TYR A 561 L 4 LEU A 491 ? LEU A 498 ? LEU A 491 LEU A 498 L 5 SER A 520 ? ILE A 527 ? SER A 520 ILE A 527 M 1 LEU A 606 ? ASP A 611 ? LEU A 606 ASP A 611 M 2 ASN A 623 ? ASN A 633 ? ASN A 623 ASN A 633 M 3 THR A 691 ? VAL A 701 ? THR A 691 VAL A 701 M 4 ASP A 652 ? VAL A 656 ? ASP A 652 VAL A 656 N 1 LYS A 616 ? TYR A 618 ? LYS A 616 TYR A 618 N 2 VAL A 730 ? ALA A 737 ? VAL A 730 ALA A 737 N 3 SER A 710 ? GLN A 718 ? SER A 710 GLN A 718 N 4 ALA A 641 ? SER A 646 ? ALA A 641 SER A 646 N 5 THR A 676 ? GLY A 684 ? THR A 676 GLY A 684 N 6 CYS A 668 ? GLU A 673 ? CYS A 668 GLU A 673 O 1 VAL A 742 ? SER A 749 ? VAL A 742 SER A 749 O 2 VAL A 775 ? ASN A 784 ? VAL A 775 ASN A 784 O 3 SER A 894 ? LEU A 903 ? SER A 894 LEU A 903 O 4 LEU A 809 ? ASP A 817 ? LEU A 809 ASP A 817 P 1 HIS A 752 ? LEU A 755 ? HIS A 752 LEU A 755 P 2 ILE A 941 ? TRP A 953 ? ILE A 941 TRP A 953 P 3 SER A 917 ? GLU A 930 ? SER A 917 GLU A 930 P 4 PHE A 790 ? TYR A 803 ? PHE A 790 TYR A 803 P 5 GLN A 878 ? LEU A 889 ? GLN A 878 LEU A 889 P 6 MET A 820 ? SER A 824 ? MET A 820 SER A 824 Q 1 ASN A 806 ? THR A 807 ? ASN A 806 THR A 807 Q 2 PHE A 790 ? TYR A 803 ? PHE A 790 TYR A 803 Q 3 SER A 917 ? GLU A 930 ? SER A 917 GLU A 930 Q 4 ILE A 869 ? LEU A 872 ? ILE A 869 LEU A 872 R 1 GLU B 60 ? GLU B 65 ? GLU B 60 GLU B 65 R 2 ARG B 87 ? LEU B 92 ? ARG B 87 LEU B 92 R 3 LEU B 425 ? PHE B 431 ? LEU B 425 PHE B 431 R 4 LYS B 412 ? PRO B 418 ? LYS B 412 PRO B 418 R 5 VAL B 355 ? ARG B 360 ? VAL B 355 ARG B 360 R 6 SER B 385 ? CYS B 386 ? SER B 385 CYS B 386 S 1 VAL B 83 ? SER B 84 ? VAL B 83 SER B 84 S 2 SER B 97 ? ARG B 105 ? SER B 97 ARG B 105 S 3 THR B 394 ? VAL B 403 ? THR B 394 VAL B 403 S 4 LEU B 366 ? THR B 373 ? LEU B 366 THR B 373 T 1 LYS B 191 ? THR B 197 ? LYS B 191 THR B 197 T 2 ARG B 150 ? PHE B 156 ? ARG B 150 PHE B 156 T 3 VAL B 112 ? ASP B 119 ? VAL B 112 ASP B 119 T 4 SER B 243 ? THR B 250 ? SER B 243 THR B 250 T 5 ILE B 304 ? THR B 311 ? ILE B 304 THR B 311 T 6 THR B 329 ? LEU B 333 ? THR B 329 LEU B 333 U 1 GLY B 540 ? SER B 543 ? GLY B 540 SER B 543 U 2 ASP B 546 ? CYS B 549 ? ASP B 546 CYS B 549 V 1 TRP B 553 ? THR B 554 ? TRP B 553 THR B 554 V 2 CYS B 560 ? THR B 561 ? CYS B 560 THR B 561 W 1 GLY B 579 ? GLU B 582 ? GLY B 579 GLU B 582 W 2 SER B 585 ? CYS B 588 ? SER B 585 CYS B 588 X 1 ILE B 639 ? VAL B 642 ? ILE B 639 VAL B 642 X 2 LEU B 679 ? VAL B 682 ? LEU B 679 VAL B 682 X 3 VAL B 664 ? TYR B 670 ? VAL B 664 TYR B 670 X 4 ALA B 652 ? LYS B 658 ? ALA B 652 LYS B 658 Y 1 GLU C 8 ? VAL C 9 ? GLU C 1424 VAL C 1425 Y 2 LEU C 17 ? SER C 20 ? LEU C 1433 SER C 1436 Y 3 THR C 55 ? ILE C 58 ? THR C 1471 ILE C 1474 Z 1 GLN C 45 ? PRO C 50 ? GLN C 1461 PRO C 1466 Z 2 TYR C 30 ? GLY C 36 ? TYR C 1446 GLY C 1452 Z 3 TYR C 67 ? VAL C 74 ? TYR C 1483 VAL C 1490 Z 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 ARG A 431 ? O ARG A 431 N ALA A 426 ? N ALA A 426 A 3 4 O ASP A 421 ? O ASP A 421 N THR A 412 ? N THR A 412 B 1 2 N PHE A 26 ? N PHE A 26 O PHE A 35 ? O PHE A 35 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 GLY A 348 ? N GLY A 348 O ASP A 357 ? O ASP A 357 I 2 3 N ILE A 360 ? N ILE A 360 O TYR A 374 ? O TYR A 374 I 3 4 N VAL A 373 ? N VAL A 373 O LEU A 391 ? O LEU A 391 J 1 2 N ARG A 379 ? N ARG A 379 O GLY A 382 ? O GLY A 382 K 1 2 N GLU A 448 ? N GLU A 448 O ARG A 476 ? O ARG A 476 K 2 3 N SER A 471 ? N SER A 471 O LEU A 542 ? O LEU A 542 K 3 4 O TYR A 541 ? O TYR A 541 N LEU A 512 ? N LEU A 512 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 PHE A 493 ? N PHE A 493 O MET A 525 ? O MET A 525 M 1 2 N SER A 609 ? N SER A 609 O LYS A 630 ? O LYS A 630 M 2 3 N LEU A 625 ? N LEU A 625 O PHE A 699 ? O PHE A 699 M 3 4 O ARG A 698 ? O ARG A 698 N ILE A 654 ? N ILE A 654 N 1 2 N ILE A 617 ? N ILE A 617 O ALA A 737 ? O ALA A 737 N 2 3 O VAL A 730 ? O VAL A 730 N LEU A 715 ? N LEU A 715 N 3 4 O GLN A 716 ? O GLN A 716 N ILE A 644 ? N ILE A 644 N 4 5 N VAL A 645 ? N VAL A 645 O VAL A 679 ? O VAL A 679 N 5 6 O VAL A 680 ? O VAL A 680 N ALA A 669 ? N ALA A 669 O 1 2 N ARG A 745 ? N ARG A 745 O GLU A 781 ? O GLU A 781 O 2 3 N LEU A 782 ? N LEU A 782 O ALA A 895 ? O ALA A 895 O 3 4 O LEU A 902 ? O LEU A 902 N TYR A 810 ? N TYR A 810 P 1 2 N LEU A 755 ? N LEU A 755 O THR A 952 ? O THR A 952 P 2 3 O THR A 949 ? O THR A 949 N LEU A 920 ? N LEU A 920 P 3 4 O SER A 925 ? O SER A 925 N HIS A 796 ? N HIS A 796 P 4 5 N LEU A 795 ? N LEU A 795 O CYS A 884 ? O CYS A 884 P 5 6 O GLN A 885 ? O GLN A 885 N ASN A 821 ? N ASN A 821 Q 1 2 O ASN A 806 ? O ASN A 806 N TYR A 803 ? N TYR A 803 Q 2 3 N HIS A 796 ? N HIS A 796 O SER A 925 ? O SER A 925 Q 3 4 O SER A 917 ? O SER A 917 N HIS A 870 ? N HIS A 870 R 1 2 N GLU B 60 ? N GLU B 60 O ARG B 91 ? O ARG B 91 R 2 3 N LEU B 90 ? N LEU B 90 O GLN B 428 ? O GLN B 428 R 3 4 O LEU B 425 ? O LEU B 425 N ILE B 416 ? N ILE B 416 R 4 5 O LYS B 417 ? O LYS B 417 N GLU B 358 ? N GLU B 358 R 5 6 N VAL B 355 ? N VAL B 355 O CYS B 386 ? O CYS B 386 S 1 2 N SER B 84 ? N SER B 84 O GLN B 103 ? O GLN B 103 S 2 3 N PHE B 100 ? N PHE B 100 O ILE B 399 ? O ILE B 399 S 3 4 O SER B 396 ? O SER B 396 N THR B 373 ? N THR B 373 T 1 2 O LYS B 191 ? O LYS B 191 N ALA B 155 ? N ALA B 155 T 2 3 O GLY B 154 ? O GLY B 154 N TYR B 116 ? N TYR B 116 T 3 4 N ASP B 113 ? N ASP B 113 O SER B 243 ? O SER B 243 T 4 5 N PHE B 248 ? N PHE B 248 O ILE B 307 ? O ILE B 307 T 5 6 N PHE B 308 ? N PHE B 308 O THR B 329 ? O THR B 329 U 1 2 N SER B 543 ? N SER B 543 O ASP B 546 ? O ASP B 546 V 1 2 N THR B 554 ? N THR B 554 O CYS B 560 ? O CYS B 560 W 1 2 N LYS B 580 ? N LYS B 580 O VAL B 587 ? O VAL B 587 X 1 2 N GLU B 640 ? N GLU B 640 O LEU B 679 ? O LEU B 679 X 2 3 O TYR B 680 ? O TYR B 680 N GLN B 668 ? N GLN B 668 X 3 4 O VAL B 665 ? O VAL B 665 N TYR B 657 ? N TYR B 657 Y 1 2 N GLU C 8 ? N GLU C 1424 O SER C 20 ? O SER C 1436 Y 2 3 N ILE C 19 ? N ILE C 1435 O ALA C 56 ? O ALA C 1472 Z 1 2 O VAL C 49 ? O VAL C 1465 N TYR C 31 ? N TYR C 1447 Z 2 3 N ARG C 32 ? N ARG C 1448 O TYR C 72 ? O TYR C 1488 Z 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 1027' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1028' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1029' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1030' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MN A 1031' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN B 708' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MN B 709' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN B 710' AC9 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 44 RESIDUES 1001 TO 1004' BC1 Software ? ? ? ? 4 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 260 RESIDUES 1005 TO 1006' BC2 Software ? ? ? ? 11 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 266 RESIDUES 1007 TO 1012' BC3 Software ? ? ? ? 9 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 458 RESIDUES 1013 TO 1016' BC4 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A1017 BOUND TO ASN A 524' BC5 Software ? ? ? ? 3 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 585 RESIDUES 1018 TO 1019' BC6 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A1020 BOUND TO ASN A 674' BC7 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A1021 BOUND TO ASN A 821' BC8 Software ? ? ? ? 1 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 943 RESIDUES 1022 TO 1023' BC9 Software ? ? ? ? 3 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 950 RESIDUES 1024 TO 1026' CC1 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG B 701 BOUND TO ASN B 99' CC2 Software ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG B 702 BOUND TO ASN B 320' CC3 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 371 RESIDUES 703 TO 704' CC4 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 559 RESIDUES 705 TO 707' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 ASP A 230 ? ASP A 230 . ? 1_555 ? 2 AC1 5 ASN A 232 ? ASN A 232 . ? 1_555 ? 3 AC1 5 ASP A 234 ? ASP A 234 . ? 1_555 ? 4 AC1 5 ILE A 236 ? ILE A 236 . ? 1_555 ? 5 AC1 5 ASP A 238 ? ASP A 238 . ? 1_555 ? 6 AC2 5 ASP A 284 ? ASP A 284 . ? 1_555 ? 7 AC2 5 ASN A 286 ? ASN A 286 . ? 1_555 ? 8 AC2 5 ASP A 288 ? ASP A 288 . ? 1_555 ? 9 AC2 5 TYR A 290 ? TYR A 290 . ? 1_555 ? 10 AC2 5 ASP A 292 ? ASP A 292 . ? 1_555 ? 11 AC3 5 ASP A 349 ? ASP A 349 . ? 1_555 ? 12 AC3 5 ASP A 351 ? ASP A 351 . ? 1_555 ? 13 AC3 5 ASP A 353 ? ASP A 353 . ? 1_555 ? 14 AC3 5 PHE A 355 ? PHE A 355 . ? 1_555 ? 15 AC3 5 ASP A 357 ? ASP A 357 . ? 1_555 ? 16 AC4 5 ASP A 413 ? ASP A 413 . ? 1_555 ? 17 AC4 5 ASP A 415 ? ASP A 415 . ? 1_555 ? 18 AC4 5 ASN A 417 ? ASN A 417 . ? 1_555 ? 19 AC4 5 TYR A 419 ? TYR A 419 . ? 1_555 ? 20 AC4 5 ASP A 421 ? ASP A 421 . ? 1_555 ? 21 AC5 4 CYS A 596 ? CYS A 596 . ? 1_555 ? 22 AC5 4 ASP A 599 ? ASP A 599 . ? 1_555 ? 23 AC5 4 VAL A 601 ? VAL A 601 . ? 1_555 ? 24 AC5 4 GLU A 636 ? GLU A 636 . ? 1_555 ? 25 AC6 6 SER B 121 ? SER B 121 . ? 1_555 ? 26 AC6 6 SER B 123 ? SER B 123 . ? 1_555 ? 27 AC6 6 GLU B 220 ? GLU B 220 . ? 1_555 ? 28 AC6 6 HOH SA . ? HOH B 801 . ? 1_555 ? 29 AC6 6 HOH SA . ? HOH B 802 . ? 1_555 ? 30 AC6 6 ASP C 79 ? ASP C 1495 . ? 1_555 ? 31 AC7 4 SER B 123 ? SER B 123 . ? 1_555 ? 32 AC7 4 ASP B 126 ? ASP B 126 . ? 1_555 ? 33 AC7 4 ASP B 127 ? ASP B 127 . ? 1_555 ? 34 AC7 4 ASP B 251 ? ASP B 251 . ? 1_555 ? 35 AC8 5 ASP B 158 ? ASP B 158 . ? 1_555 ? 36 AC8 5 ASN B 215 ? ASN B 215 . ? 1_555 ? 37 AC8 5 ASP B 217 ? ASP B 217 . ? 1_555 ? 38 AC8 5 PRO B 219 ? PRO B 219 . ? 1_555 ? 39 AC8 5 GLU B 220 ? GLU B 220 . ? 1_555 ? 40 AC9 5 GLU A 15 ? GLU A 15 . ? 1_555 ? 41 AC9 5 GLY A 16 ? GLY A 16 . ? 1_555 ? 42 AC9 5 SER A 17 ? SER A 17 . ? 1_555 ? 43 AC9 5 ASN A 44 ? ASN A 44 . ? 1_555 ? 44 AC9 5 GLU A 52 ? GLU A 52 . ? 1_555 ? 45 BC1 4 ASP A 257 ? ASP A 257 . ? 1_555 ? 46 BC1 4 LYS A 259 ? LYS A 259 . ? 1_555 ? 47 BC1 4 ASN A 260 ? ASN A 260 . ? 1_555 ? 48 BC1 4 SER A 262 ? SER A 262 . ? 1_555 ? 49 BC2 11 ALA A 213 ? ALA A 213 . ? 1_555 ? 50 BC2 11 GLN A 214 ? GLN A 214 . ? 1_555 ? 51 BC2 11 PHE A 217 ? PHE A 217 . ? 1_555 ? 52 BC2 11 TYR A 254 ? TYR A 254 . ? 1_555 ? 53 BC2 11 SER A 263 ? SER A 263 . ? 1_555 ? 54 BC2 11 LEU A 264 ? LEU A 264 . ? 1_555 ? 55 BC2 11 ASN A 266 ? ASN A 266 . ? 1_555 ? 56 BC2 11 ASN A 935 ? ASN A 935 . ? 5_665 ? 57 BC2 11 VAL C 28 ? VAL C 1444 . ? 1_555 ? 58 BC2 11 ARG C 29 ? ARG C 1445 . ? 1_555 ? 59 BC2 11 SER C 52 ? SER C 1468 . ? 1_555 ? 60 BC3 9 GLU A 448 ? GLU A 448 . ? 1_555 ? 61 BC3 9 TYR A 450 ? TYR A 450 . ? 1_555 ? 62 BC3 9 ASN A 458 ? ASN A 458 . ? 1_555 ? 63 BC3 9 THR A 460 ? THR A 460 . ? 1_555 ? 64 BC3 9 CYS A 461 ? CYS A 461 . ? 1_555 ? 65 BC3 9 CYS A 472 ? CYS A 472 . ? 1_555 ? 66 BC3 9 ASN A 474 ? ASN A 474 . ? 1_555 ? 67 BC3 9 ARG A 476 ? ARG A 476 . ? 1_555 ? 68 BC3 9 ASN B 48 ? ASN B 48 . ? 4_565 ? 69 BC4 2 GLN A 494 ? GLN A 494 . ? 1_555 ? 70 BC4 2 ASN A 524 ? ASN A 524 . ? 1_555 ? 71 BC5 3 PHE A 558 ? PHE A 558 . ? 1_555 ? 72 BC5 3 ALA A 584 ? ALA A 584 . ? 1_555 ? 73 BC5 3 ASN A 585 ? ASN A 585 . ? 1_555 ? 74 BC6 1 ASN A 674 ? ASN A 674 . ? 1_555 ? 75 BC7 2 PRO A 819 ? PRO A 819 . ? 1_555 ? 76 BC7 2 ASN A 821 ? ASN A 821 . ? 1_555 ? 77 BC8 1 ASN A 943 ? ASN A 943 . ? 1_555 ? 78 BC9 3 ILE A 869 ? ILE A 869 . ? 1_555 ? 79 BC9 3 THR A 948 ? THR A 948 . ? 1_555 ? 80 BC9 3 ASN A 950 ? ASN A 950 . ? 1_555 ? 81 CC1 2 ASN B 99 ? ASN B 99 . ? 1_555 ? 82 CC1 2 NAG KA . ? NAG B 703 . ? 1_555 ? 83 CC2 4 ARG A 248 ? ARG A 248 . ? 1_555 ? 84 CC2 4 ASN B 316 ? ASN B 316 . ? 1_555 ? 85 CC2 4 LEU B 317 ? LEU B 317 . ? 1_555 ? 86 CC2 4 ASN B 320 ? ASN B 320 . ? 1_555 ? 87 CC3 5 ASN B 371 ? ASN B 371 . ? 1_555 ? 88 CC3 5 SER B 398 ? SER B 398 . ? 1_555 ? 89 CC3 5 ILE B 399 ? ILE B 399 . ? 1_555 ? 90 CC3 5 GLU B 400 ? GLU B 400 . ? 1_555 ? 91 CC3 5 NAG IA . ? NAG B 701 . ? 1_555 ? 92 CC4 5 ASP A 621 ? ASP A 621 . ? 1_555 ? 93 CC4 5 PRO A 624 ? PRO A 624 . ? 1_555 ? 94 CC4 5 TYR B 531 ? TYR B 531 . ? 1_555 ? 95 CC4 5 TYR B 557 ? TYR B 557 . ? 1_555 ? 96 CC4 5 ASN B 559 ? ASN B 559 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MMX _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 4MMX _atom_sites.fract_transf_matrix[1][1] 0.007701 _atom_sites.fract_transf_matrix[1][2] 0.004446 _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] 0.008892 _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] 0.003270 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C MN N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PHE A 1 1 ? -17.475 49.743 8.391 1.00 70.49 ? 1 PHE A N 1 ATOM 2 C CA . PHE A 1 1 ? -17.988 48.933 7.293 1.00 81.66 ? 1 PHE A CA 1 ATOM 3 C C . PHE A 1 1 ? -17.682 49.579 5.947 1.00 82.15 ? 1 PHE A C 1 ATOM 4 O O . PHE A 1 1 ? -17.834 48.953 4.897 1.00 78.29 ? 1 PHE A O 1 ATOM 5 C CB . PHE A 1 1 ? -19.497 48.716 7.444 1.00 84.06 ? 1 PHE A CB 1 ATOM 6 C CG . PHE A 1 1 ? -20.304 49.982 7.380 1.00 79.41 ? 1 PHE A CG 1 ATOM 7 C CD1 . PHE A 1 1 ? -20.903 50.378 6.195 1.00 81.25 ? 1 PHE A CD1 1 ATOM 8 C CD2 . PHE A 1 1 ? -20.466 50.775 8.504 1.00 83.75 ? 1 PHE A CD2 1 ATOM 9 C CE1 . PHE A 1 1 ? -21.647 51.540 6.132 1.00 83.33 ? 1 PHE A CE1 1 ATOM 10 C CE2 . PHE A 1 1 ? -21.208 51.940 8.447 1.00 89.80 ? 1 PHE A CE2 1 ATOM 11 C CZ . PHE A 1 1 ? -21.800 52.322 7.259 1.00 89.20 ? 1 PHE A CZ 1 ATOM 12 N N . ASN A 1 2 ? -17.248 50.834 5.987 1.00 84.79 ? 2 ASN A N 1 ATOM 13 C CA . ASN A 1 2 ? -17.029 51.614 4.775 1.00 94.14 ? 2 ASN A CA 1 ATOM 14 C C . ASN A 1 2 ? -15.592 51.596 4.257 1.00 87.99 ? 2 ASN A C 1 ATOM 15 O O . ASN A 1 2 ? -15.269 52.302 3.305 1.00 89.60 ? 2 ASN A O 1 ATOM 16 C CB . ASN A 1 2 ? -17.467 53.060 5.005 1.00 97.83 ? 2 ASN A CB 1 ATOM 17 C CG . ASN A 1 2 ? -17.081 53.575 6.374 1.00 92.16 ? 2 ASN A CG 1 ATOM 18 O OD1 . ASN A 1 2 ? -17.116 52.838 7.360 1.00 88.13 ? 2 ASN A OD1 1 ATOM 19 N ND2 . ASN A 1 2 ? -16.711 54.848 6.443 1.00 88.94 ? 2 ASN A ND2 1 ATOM 20 N N . LEU A 1 3 ? -14.725 50.812 4.887 1.00 75.71 ? 3 LEU A N 1 ATOM 21 C CA . LEU A 1 3 ? -13.356 50.681 4.399 1.00 73.23 ? 3 LEU A CA 1 ATOM 22 C C . LEU A 1 3 ? -13.321 49.837 3.127 1.00 76.18 ? 3 LEU A C 1 ATOM 23 O O . LEU A 1 3 ? -13.997 48.813 3.035 1.00 88.03 ? 3 LEU A O 1 ATOM 24 C CB . LEU A 1 3 ? -12.453 50.074 5.473 1.00 69.44 ? 3 LEU A CB 1 ATOM 25 C CG . LEU A 1 3 ? -12.187 50.970 6.685 1.00 66.63 ? 3 LEU A CG 1 ATOM 26 C CD1 . LEU A 1 3 ? -11.277 50.278 7.688 1.00 63.29 ? 3 LEU A CD1 1 ATOM 27 C CD2 . LEU A 1 3 ? -11.593 52.300 6.246 1.00 67.33 ? 3 LEU A CD2 1 ATOM 28 N N . ASP A 1 4 ? -12.535 50.275 2.149 1.00 77.86 ? 4 ASP A N 1 ATOM 29 C CA . ASP A 1 4 ? -12.463 49.601 0.855 1.00 81.27 ? 4 ASP A CA 1 ATOM 30 C C . ASP A 1 4 ? -11.313 48.599 0.816 1.00 84.81 ? 4 ASP A C 1 ATOM 31 O O . ASP A 1 4 ? -10.144 48.982 0.819 1.00 78.90 ? 4 ASP A O 1 ATOM 32 C CB . ASP A 1 4 ? -12.307 50.632 -0.265 1.00 88.45 ? 4 ASP A CB 1 ATOM 33 C CG . ASP A 1 4 ? -12.065 49.995 -1.617 1.00 101.06 ? 4 ASP A CG 1 ATOM 34 O OD1 . ASP A 1 4 ? -10.886 49.764 -1.963 1.00 98.49 ? 4 ASP A OD1 1 ATOM 35 O OD2 . ASP A 1 4 ? -13.051 49.731 -2.336 1.00 117.98 ? 4 ASP A OD2 1 ATOM 36 N N . VAL A 1 5 ? -11.653 47.313 0.778 1.00 95.23 ? 5 VAL A N 1 ATOM 37 C CA . VAL A 1 5 ? -10.649 46.255 0.839 1.00 93.16 ? 5 VAL A CA 1 ATOM 38 C C . VAL A 1 5 ? -10.269 45.680 -0.529 1.00 91.84 ? 5 VAL A C 1 ATOM 39 O O . VAL A 1 5 ? -9.370 44.844 -0.624 1.00 92.34 ? 5 VAL A O 1 ATOM 40 C CB . VAL A 1 5 ? -11.132 45.098 1.741 1.00 89.39 ? 5 VAL A CB 1 ATOM 41 C CG1 . VAL A 1 5 ? -9.949 44.404 2.402 1.00 89.73 ? 5 VAL A CG1 1 ATOM 42 C CG2 . VAL A 1 5 ? -12.090 45.619 2.798 1.00 85.61 ? 5 VAL A CG2 1 ATOM 43 N N . ASP A 1 6 ? -10.936 46.124 -1.590 1.00 98.49 ? 6 ASP A N 1 ATOM 44 C CA . ASP A 1 6 ? -10.678 45.546 -2.908 1.00 114.43 ? 6 ASP A CA 1 ATOM 45 C C . ASP A 1 6 ? -9.416 46.130 -3.543 1.00 111.43 ? 6 ASP A C 1 ATOM 46 O O . ASP A 1 6 ? -8.662 45.417 -4.205 1.00 121.39 ? 6 ASP A O 1 ATOM 47 C CB . ASP A 1 6 ? -11.890 45.733 -3.835 1.00 131.86 ? 6 ASP A CB 1 ATOM 48 C CG . ASP A 1 6 ? -11.829 47.017 -4.645 1.00 146.97 ? 6 ASP A CG 1 ATOM 49 O OD1 . ASP A 1 6 ? -11.558 48.087 -4.061 1.00 159.33 ? 6 ASP A OD1 1 ATOM 50 O OD2 . ASP A 1 6 ? -12.051 46.955 -5.872 1.00 141.45 ? 6 ASP A OD2 1 ATOM 51 N N . SER A 1 7 ? -9.184 47.423 -3.334 1.00 99.81 ? 7 SER A N 1 ATOM 52 C CA . SER A 1 7 ? -8.026 48.087 -3.923 1.00 103.47 ? 7 SER A CA 1 ATOM 53 C C . SER A 1 7 ? -7.397 49.116 -2.986 1.00 109.71 ? 7 SER A C 1 ATOM 54 O O . SER A 1 7 ? -7.560 50.320 -3.184 1.00 115.00 ? 7 SER A O 1 ATOM 55 C CB . SER A 1 7 ? -8.419 48.760 -5.240 1.00 106.02 ? 7 SER A CB 1 ATOM 56 O OG . SER A 1 7 ? -7.296 49.358 -5.862 1.00 117.54 ? 7 SER A OG 1 ATOM 57 N N . PRO A 1 8 ? -6.673 48.645 -1.960 1.00 102.20 ? 8 PRO A N 1 ATOM 58 C CA . PRO A 1 8 ? -5.968 49.556 -1.055 1.00 90.62 ? 8 PRO A CA 1 ATOM 59 C C . PRO A 1 8 ? -4.612 49.973 -1.616 1.00 92.00 ? 8 PRO A C 1 ATOM 60 O O . PRO A 1 8 ? -4.282 49.620 -2.748 1.00 92.42 ? 8 PRO A O 1 ATOM 61 C CB . PRO A 1 8 ? -5.803 48.720 0.211 1.00 77.37 ? 8 PRO A CB 1 ATOM 62 C CG . PRO A 1 8 ? -5.660 47.329 -0.303 1.00 93.38 ? 8 PRO A CG 1 ATOM 63 C CD . PRO A 1 8 ? -6.527 47.238 -1.541 1.00 97.17 ? 8 PRO A CD 1 ATOM 64 N N . ALA A 1 9 ? -3.838 50.713 -0.829 1.00 86.86 ? 9 ALA A N 1 ATOM 65 C CA . ALA A 1 9 ? -2.501 51.123 -1.240 1.00 93.22 ? 9 ALA A CA 1 ATOM 66 C C . ALA A 1 9 ? -1.443 50.329 -0.481 1.00 87.14 ? 9 ALA A C 1 ATOM 67 O O . ALA A 1 9 ? -1.366 50.397 0.745 1.00 83.78 ? 9 ALA A O 1 ATOM 68 C CB . ALA A 1 9 ? -2.309 52.614 -1.019 1.00 105.10 ? 9 ALA A CB 1 ATOM 69 N N . GLU A 1 10 ? -0.630 49.577 -1.216 1.00 86.18 ? 10 GLU A N 1 ATOM 70 C CA . GLU A 1 10 ? 0.384 48.728 -0.600 1.00 84.88 ? 10 GLU A CA 1 ATOM 71 C C . GLU A 1 10 ? 1.786 49.309 -0.755 1.00 89.48 ? 10 GLU A C 1 ATOM 72 O O . GLU A 1 10 ? 2.259 49.535 -1.869 1.00 94.19 ? 10 GLU A O 1 ATOM 73 C CB . GLU A 1 10 ? 0.328 47.319 -1.195 1.00 81.95 ? 10 GLU A CB 1 ATOM 74 C CG . GLU A 1 10 ? -0.977 46.589 -0.916 1.00 91.82 ? 10 GLU A CG 1 ATOM 75 C CD . GLU A 1 10 ? -1.059 45.244 -1.612 1.00 113.26 ? 10 GLU A CD 1 ATOM 76 O OE1 . GLU A 1 10 ? -0.073 44.852 -2.270 1.00 136.19 ? 10 GLU A OE1 1 ATOM 77 O OE2 . GLU A 1 10 ? -2.113 44.581 -1.502 1.00 106.43 ? 10 GLU A OE2 1 ATOM 78 N N . TYR A 1 11 ? 2.442 49.550 0.375 1.00 74.76 ? 11 TYR A N 1 ATOM 79 C CA . TYR A 1 11 ? 3.810 50.055 0.388 1.00 74.87 ? 11 TYR A CA 1 ATOM 80 C C . TYR A 1 11 ? 4.748 49.006 0.976 1.00 73.46 ? 11 TYR A C 1 ATOM 81 O O . TYR A 1 11 ? 4.411 48.349 1.960 1.00 70.61 ? 11 TYR A O 1 ATOM 82 C CB . TYR A 1 11 ? 3.900 51.355 1.189 1.00 82.06 ? 11 TYR A CB 1 ATOM 83 C CG . TYR A 1 11 ? 3.041 52.478 0.648 1.00 74.04 ? 11 TYR A CG 1 ATOM 84 C CD1 . TYR A 1 11 ? 1.712 52.608 1.030 1.00 72.87 ? 11 TYR A CD1 1 ATOM 85 C CD2 . TYR A 1 11 ? 3.562 53.411 -0.238 1.00 82.33 ? 11 TYR A CD2 1 ATOM 86 C CE1 . TYR A 1 11 ? 0.925 53.634 0.540 1.00 74.64 ? 11 TYR A CE1 1 ATOM 87 C CE2 . TYR A 1 11 ? 2.784 54.441 -0.732 1.00 89.97 ? 11 TYR A CE2 1 ATOM 88 C CZ . TYR A 1 11 ? 1.466 54.547 -0.341 1.00 98.56 ? 11 TYR A CZ 1 ATOM 89 O OH . TYR A 1 11 ? 0.688 55.571 -0.832 1.00 106.66 ? 11 TYR A OH 1 ATOM 90 N N . SER A 1 12 ? 5.924 48.851 0.377 1.00 75.75 ? 12 SER A N 1 ATOM 91 C CA . SER A 1 12 ? 6.865 47.826 0.815 1.00 75.13 ? 12 SER A CA 1 ATOM 92 C C . SER A 1 12 ? 8.286 48.357 0.953 1.00 82.77 ? 12 SER A C 1 ATOM 93 O O . SER A 1 12 ? 8.823 48.969 0.029 1.00 96.79 ? 12 SER A O 1 ATOM 94 C CB . SER A 1 12 ? 6.853 46.645 -0.157 1.00 79.16 ? 12 SER A CB 1 ATOM 95 O OG . SER A 1 12 ? 7.309 47.039 -1.440 1.00 84.11 ? 12 SER A OG 1 ATOM 96 N N . GLY A 1 13 ? 8.892 48.113 2.110 1.00 72.25 ? 13 GLY A N 1 ATOM 97 C CA . GLY A 1 13 ? 10.278 48.474 2.340 1.00 72.40 ? 13 GLY A CA 1 ATOM 98 C C . GLY A 1 13 ? 11.183 47.276 2.130 1.00 88.89 ? 13 GLY A C 1 ATOM 99 O O . GLY A 1 13 ? 10.711 46.203 1.754 1.00 106.10 ? 13 GLY A O 1 ATOM 100 N N . PRO A 1 14 ? 12.491 47.449 2.371 1.00 81.23 ? 14 PRO A N 1 ATOM 101 C CA . PRO A 1 14 ? 13.451 46.349 2.226 1.00 87.90 ? 14 PRO A CA 1 ATOM 102 C C . PRO A 1 14 ? 13.186 45.240 3.240 1.00 85.91 ? 14 PRO A C 1 ATOM 103 O O . PRO A 1 14 ? 12.865 45.537 4.389 1.00 82.37 ? 14 PRO A O 1 ATOM 104 C CB . PRO A 1 14 ? 14.801 47.023 2.481 1.00 76.90 ? 14 PRO A CB 1 ATOM 105 C CG . PRO A 1 14 ? 14.475 48.209 3.325 1.00 73.49 ? 14 PRO A CG 1 ATOM 106 C CD . PRO A 1 14 ? 13.135 48.686 2.846 1.00 73.30 ? 14 PRO A CD 1 ATOM 107 N N . GLU A 1 15 ? 13.315 43.986 2.819 1.00 85.14 ? 15 GLU A N 1 ATOM 108 C CA . GLU A 1 15 ? 13.018 42.856 3.693 1.00 81.06 ? 15 GLU A CA 1 ATOM 109 C C . GLU A 1 15 ? 14.008 42.765 4.851 1.00 79.00 ? 15 GLU A C 1 ATOM 110 O O . GLU A 1 15 ? 15.198 43.038 4.689 1.00 74.03 ? 15 GLU A O 1 ATOM 111 C CB . GLU A 1 15 ? 13.012 41.546 2.900 1.00 84.37 ? 15 GLU A CB 1 ATOM 112 C CG . GLU A 1 15 ? 14.312 41.234 2.174 1.00 97.99 ? 15 GLU A CG 1 ATOM 113 C CD . GLU A 1 15 ? 14.262 39.909 1.436 1.00 117.16 ? 15 GLU A CD 1 ATOM 114 O OE1 . GLU A 1 15 ? 13.342 39.109 1.712 1.00 126.41 ? 15 GLU A OE1 1 ATOM 115 O OE2 . GLU A 1 15 ? 15.138 39.667 0.579 1.00 122.25 ? 15 GLU A OE2 1 ATOM 116 N N . GLY A 1 16 ? 13.503 42.388 6.021 1.00 76.70 ? 16 GLY A N 1 ATOM 117 C CA . GLY A 1 16 ? 14.328 42.253 7.207 1.00 69.13 ? 16 GLY A CA 1 ATOM 118 C C . GLY A 1 16 ? 14.490 43.555 7.966 1.00 64.43 ? 16 GLY A C 1 ATOM 119 O O . GLY A 1 16 ? 15.180 43.607 8.983 1.00 67.15 ? 16 GLY A O 1 ATOM 120 N N . SER A 1 17 ? 13.854 44.612 7.469 1.00 64.39 ? 17 SER A N 1 ATOM 121 C CA . SER A 1 17 ? 13.970 45.933 8.077 1.00 64.30 ? 17 SER A CA 1 ATOM 122 C C . SER A 1 17 ? 12.834 46.219 9.051 1.00 62.33 ? 17 SER A C 1 ATOM 123 O O . SER A 1 17 ? 12.794 47.284 9.671 1.00 61.39 ? 17 SER A O 1 ATOM 124 C CB . SER A 1 17 ? 14.000 47.013 6.994 1.00 64.95 ? 17 SER A CB 1 ATOM 125 O OG . SER A 1 17 ? 12.795 47.021 6.249 1.00 64.46 ? 17 SER A OG 1 ATOM 126 N N . TYR A 1 18 ? 11.920 45.260 9.179 1.00 61.59 ? 18 TYR A N 1 ATOM 127 C CA . TYR A 1 18 ? 10.695 45.430 9.959 1.00 67.07 ? 18 TYR A CA 1 ATOM 128 C C . TYR A 1 18 ? 9.927 46.661 9.489 1.00 67.40 ? 18 TYR A C 1 ATOM 129 O O . TYR A 1 18 ? 9.372 47.402 10.299 1.00 63.21 ? 18 TYR A O 1 ATOM 130 C CB . TYR A 1 18 ? 10.990 45.542 11.460 1.00 68.52 ? 18 TYR A CB 1 ATOM 131 C CG . TYR A 1 18 ? 11.475 44.269 12.120 1.00 59.37 ? 18 TYR A CG 1 ATOM 132 C CD1 . TYR A 1 18 ? 11.673 44.216 13.493 1.00 57.47 ? 18 TYR A CD1 1 ATOM 133 C CD2 . TYR A 1 18 ? 11.740 43.125 11.377 1.00 67.21 ? 18 TYR A CD2 1 ATOM 134 C CE1 . TYR A 1 18 ? 12.115 43.063 14.108 1.00 62.46 ? 18 TYR A CE1 1 ATOM 135 C CE2 . TYR A 1 18 ? 12.188 41.966 11.984 1.00 83.15 ? 18 TYR A CE2 1 ATOM 136 C CZ . TYR A 1 18 ? 12.372 41.942 13.350 1.00 76.82 ? 18 TYR A CZ 1 ATOM 137 O OH . TYR A 1 18 ? 12.816 40.795 13.965 1.00 88.31 ? 18 TYR A OH 1 ATOM 138 N N . PHE A 1 19 ? 9.918 46.880 8.177 1.00 67.32 ? 19 PHE A N 1 ATOM 139 C CA . PHE A 1 19 ? 9.185 47.991 7.584 1.00 58.70 ? 19 PHE A CA 1 ATOM 140 C C . PHE A 1 19 ? 7.705 47.866 7.922 1.00 56.55 ? 19 PHE A C 1 ATOM 141 O O . PHE A 1 19 ? 7.083 46.841 7.652 1.00 57.25 ? 19 PHE A O 1 ATOM 142 C CB . PHE A 1 19 ? 9.403 48.017 6.067 1.00 69.56 ? 19 PHE A CB 1 ATOM 143 C CG . PHE A 1 19 ? 8.649 49.105 5.353 1.00 73.08 ? 19 PHE A CG 1 ATOM 144 C CD1 . PHE A 1 19 ? 7.389 48.862 4.827 1.00 87.72 ? 19 PHE A CD1 1 ATOM 145 C CD2 . PHE A 1 19 ? 9.209 50.361 5.184 1.00 68.88 ? 19 PHE A CD2 1 ATOM 146 C CE1 . PHE A 1 19 ? 6.697 49.855 4.160 1.00 81.65 ? 19 PHE A CE1 1 ATOM 147 C CE2 . PHE A 1 19 ? 8.522 51.358 4.516 1.00 73.56 ? 19 PHE A CE2 1 ATOM 148 C CZ . PHE A 1 19 ? 7.264 51.104 4.003 1.00 72.13 ? 19 PHE A CZ 1 ATOM 149 N N . GLY A 1 20 ? 7.144 48.913 8.516 1.00 54.73 ? 20 GLY A N 1 ATOM 150 C CA . GLY A 1 20 ? 5.756 48.883 8.936 1.00 58.54 ? 20 GLY A CA 1 ATOM 151 C C . GLY A 1 20 ? 5.593 48.579 10.412 1.00 53.33 ? 20 GLY A C 1 ATOM 152 O O . GLY A 1 20 ? 4.487 48.305 10.876 1.00 66.08 ? 20 GLY A O 1 ATOM 153 N N . PHE A 1 21 ? 6.695 48.624 11.153 1.00 49.34 ? 21 PHE A N 1 ATOM 154 C CA . PHE A 1 21 ? 6.653 48.378 12.590 1.00 51.14 ? 21 PHE A CA 1 ATOM 155 C C . PHE A 1 21 ? 5.981 49.542 13.309 1.00 45.33 ? 21 PHE A C 1 ATOM 156 O O . PHE A 1 21 ? 5.414 49.379 14.390 1.00 43.59 ? 21 PHE A O 1 ATOM 157 C CB . PHE A 1 21 ? 8.060 48.154 13.145 1.00 47.08 ? 21 PHE A CB 1 ATOM 158 C CG . PHE A 1 21 ? 8.080 47.729 14.584 1.00 45.60 ? 21 PHE A CG 1 ATOM 159 C CD1 . PHE A 1 21 ? 7.873 46.405 14.929 1.00 44.27 ? 21 PHE A CD1 1 ATOM 160 C CD2 . PHE A 1 21 ? 8.305 48.652 15.592 1.00 42.99 ? 21 PHE A CD2 1 ATOM 161 C CE1 . PHE A 1 21 ? 7.888 46.010 16.251 1.00 42.66 ? 21 PHE A CE1 1 ATOM 162 C CE2 . PHE A 1 21 ? 8.321 48.262 16.917 1.00 55.38 ? 21 PHE A CE2 1 ATOM 163 C CZ . PHE A 1 21 ? 8.112 46.937 17.246 1.00 45.79 ? 21 PHE A CZ 1 ATOM 164 N N . ALA A 1 22 ? 6.059 50.719 12.699 1.00 50.17 ? 22 ALA A N 1 ATOM 165 C CA . ALA A 1 22 ? 5.401 51.908 13.223 1.00 56.93 ? 22 ALA A CA 1 ATOM 166 C C . ALA A 1 22 ? 4.854 52.738 12.071 1.00 66.39 ? 22 ALA A C 1 ATOM 167 O O . ALA A 1 22 ? 5.527 52.924 11.056 1.00 90.57 ? 22 ALA A O 1 ATOM 168 C CB . ALA A 1 22 ? 6.362 52.727 14.066 1.00 75.21 ? 22 ALA A CB 1 ATOM 169 N N . VAL A 1 23 ? 3.630 53.231 12.225 1.00 59.68 ? 23 VAL A N 1 ATOM 170 C CA . VAL A 1 23 ? 2.989 54.012 11.175 1.00 58.25 ? 23 VAL A CA 1 ATOM 171 C C . VAL A 1 23 ? 2.310 55.259 11.725 1.00 65.43 ? 23 VAL A C 1 ATOM 172 O O . VAL A 1 23 ? 1.854 55.278 12.868 1.00 75.15 ? 23 VAL A O 1 ATOM 173 C CB . VAL A 1 23 ? 1.940 53.179 10.410 1.00 51.44 ? 23 VAL A CB 1 ATOM 174 C CG1 . VAL A 1 23 ? 2.617 52.126 9.547 1.00 59.23 ? 23 VAL A CG1 1 ATOM 175 C CG2 . VAL A 1 23 ? 0.958 52.540 11.380 1.00 48.73 ? 23 VAL A CG2 1 ATOM 176 N N . ASP A 1 24 ? 2.250 56.298 10.898 1.00 62.08 ? 24 ASP A N 1 ATOM 177 C CA . ASP A 1 24 ? 1.514 57.509 11.235 1.00 64.99 ? 24 ASP A CA 1 ATOM 178 C C . ASP A 1 24 ? 1.273 58.336 9.977 1.00 60.48 ? 24 ASP A C 1 ATOM 179 O O . ASP A 1 24 ? 1.744 57.989 8.895 1.00 67.02 ? 24 ASP A O 1 ATOM 180 C CB . ASP A 1 24 ? 2.273 58.332 12.281 1.00 80.64 ? 24 ASP A CB 1 ATOM 181 C CG . ASP A 1 24 ? 1.364 59.260 13.069 1.00 99.77 ? 24 ASP A CG 1 ATOM 182 O OD1 . ASP A 1 24 ? 0.412 59.810 12.478 1.00 105.83 ? 24 ASP A OD1 1 ATOM 183 O OD2 . ASP A 1 24 ? 1.599 59.434 14.284 1.00 104.53 ? 24 ASP A OD2 1 ATOM 184 N N . PHE A 1 25 ? 0.546 59.437 10.128 1.00 68.97 ? 25 PHE A N 1 ATOM 185 C CA . PHE A 1 25 ? 0.290 60.343 9.018 1.00 70.23 ? 25 PHE A CA 1 ATOM 186 C C . PHE A 1 25 ? 1.190 61.565 9.100 1.00 78.65 ? 25 PHE A C 1 ATOM 187 O O . PHE A 1 25 ? 1.449 62.086 10.185 1.00 80.45 ? 25 PHE A O 1 ATOM 188 C CB . PHE A 1 25 ? -1.175 60.785 9.000 1.00 62.61 ? 25 PHE A CB 1 ATOM 189 C CG . PHE A 1 25 ? -2.136 59.700 8.614 1.00 69.26 ? 25 PHE A CG 1 ATOM 190 C CD1 . PHE A 1 25 ? -2.737 58.912 9.581 1.00 89.31 ? 25 PHE A CD1 1 ATOM 191 C CD2 . PHE A 1 25 ? -2.448 59.475 7.283 1.00 63.77 ? 25 PHE A CD2 1 ATOM 192 C CE1 . PHE A 1 25 ? -3.629 57.917 9.228 1.00 90.13 ? 25 PHE A CE1 1 ATOM 193 C CE2 . PHE A 1 25 ? -3.338 58.481 6.924 1.00 64.31 ? 25 PHE A CE2 1 ATOM 194 C CZ . PHE A 1 25 ? -3.929 57.701 7.898 1.00 71.54 ? 25 PHE A CZ 1 ATOM 195 N N . PHE A 1 26 ? 1.669 62.017 7.948 1.00 85.07 ? 26 PHE A N 1 ATOM 196 C CA . PHE A 1 26 ? 2.389 63.279 7.874 1.00 79.71 ? 26 PHE A CA 1 ATOM 197 C C . PHE A 1 26 ? 1.557 64.292 7.103 1.00 82.65 ? 26 PHE A C 1 ATOM 198 O O . PHE A 1 26 ? 1.383 64.173 5.889 1.00 89.40 ? 26 PHE A O 1 ATOM 199 C CB . PHE A 1 26 ? 3.755 63.093 7.215 1.00 66.85 ? 26 PHE A CB 1 ATOM 200 C CG . PHE A 1 26 ? 4.530 64.369 7.059 1.00 75.59 ? 26 PHE A CG 1 ATOM 201 C CD1 . PHE A 1 26 ? 4.706 64.940 5.810 1.00 85.66 ? 26 PHE A CD1 1 ATOM 202 C CD2 . PHE A 1 26 ? 5.076 65.002 8.162 1.00 70.51 ? 26 PHE A CD2 1 ATOM 203 C CE1 . PHE A 1 26 ? 5.419 66.115 5.664 1.00 87.43 ? 26 PHE A CE1 1 ATOM 204 C CE2 . PHE A 1 26 ? 5.789 66.178 8.023 1.00 70.09 ? 26 PHE A CE2 1 ATOM 205 C CZ . PHE A 1 26 ? 5.960 66.735 6.772 1.00 82.90 ? 26 PHE A CZ 1 ATOM 206 N N . VAL A 1 27 ? 1.040 65.287 7.814 1.00 78.48 ? 27 VAL A N 1 ATOM 207 C CA . VAL A 1 27 ? 0.221 66.318 7.193 1.00 88.54 ? 27 VAL A CA 1 ATOM 208 C C . VAL A 1 27 ? 0.830 67.693 7.492 1.00 81.97 ? 27 VAL A C 1 ATOM 209 O O . VAL A 1 27 ? 0.525 68.327 8.504 1.00 76.69 ? 27 VAL A O 1 ATOM 210 C CB . VAL A 1 27 ? -1.260 66.221 7.664 1.00 87.89 ? 27 VAL A CB 1 ATOM 211 C CG1 . VAL A 1 27 ? -1.354 66.033 9.181 1.00 78.13 ? 27 VAL A CG1 1 ATOM 212 C CG2 . VAL A 1 27 ? -2.081 67.415 7.177 1.00 99.01 ? 27 VAL A CG2 1 ATOM 213 N N . PRO A 1 28 ? 1.729 68.144 6.606 1.00 74.90 ? 28 PRO A N 1 ATOM 214 C CA . PRO A 1 28 ? 2.460 69.402 6.783 1.00 76.77 ? 28 PRO A CA 1 ATOM 215 C C . PRO A 1 28 ? 1.575 70.625 6.579 1.00 80.02 ? 28 PRO A C 1 ATOM 216 O O . PRO A 1 28 ? 0.622 70.578 5.802 1.00 92.83 ? 28 PRO A O 1 ATOM 217 C CB . PRO A 1 28 ? 3.544 69.329 5.706 1.00 89.78 ? 28 PRO A CB 1 ATOM 218 C CG . PRO A 1 28 ? 2.939 68.487 4.640 1.00 103.55 ? 28 PRO A CG 1 ATOM 219 C CD . PRO A 1 28 ? 2.105 67.461 5.355 1.00 76.32 ? 28 PRO A CD 1 ATOM 220 N N . SER A 1 29 ? 1.895 71.708 7.278 1.00 80.85 ? 29 SER A N 1 ATOM 221 C CA . SER A 1 29 ? 1.145 72.951 7.156 1.00 92.57 ? 29 SER A CA 1 ATOM 222 C C . SER A 1 29 ? 1.666 73.793 5.996 1.00 99.29 ? 29 SER A C 1 ATOM 223 O O . SER A 1 29 ? 1.033 74.767 5.589 1.00 98.38 ? 29 SER A O 1 ATOM 224 C CB . SER A 1 29 ? 1.218 73.745 8.461 1.00 83.67 ? 29 SER A CB 1 ATOM 225 O OG . SER A 1 29 ? 2.561 73.902 8.884 1.00 82.76 ? 29 SER A OG 1 ATOM 226 N N . ALA A 1 30 ? 2.821 73.406 5.465 1.00 99.55 ? 30 ALA A N 1 ATOM 227 C CA . ALA A 1 30 ? 3.451 74.145 4.378 1.00 92.59 ? 30 ALA A CA 1 ATOM 228 C C . ALA A 1 30 ? 3.064 73.580 3.015 1.00 94.64 ? 30 ALA A C 1 ATOM 229 O O . ALA A 1 30 ? 3.483 74.096 1.979 1.00 98.50 ? 30 ALA A O 1 ATOM 230 C CB . ALA A 1 30 ? 4.963 74.133 4.542 1.00 108.21 ? 30 ALA A CB 1 ATOM 231 N N . SER A 1 31 ? 2.261 72.521 3.019 1.00 115.99 ? 31 SER A N 1 ATOM 232 C CA . SER A 1 31 ? 1.868 71.863 1.779 1.00 108.43 ? 31 SER A CA 1 ATOM 233 C C . SER A 1 31 ? 0.465 71.271 1.858 1.00 105.05 ? 31 SER A C 1 ATOM 234 O O . SER A 1 31 ? 0.017 70.843 2.922 1.00 106.78 ? 31 SER A O 1 ATOM 235 C CB . SER A 1 31 ? 2.874 70.766 1.422 1.00 100.92 ? 31 SER A CB 1 ATOM 236 O OG . SER A 1 31 ? 2.463 70.052 0.269 1.00 97.05 ? 31 SER A OG 1 ATOM 237 N N . SER A 1 32 ? -0.222 71.248 0.720 1.00 98.73 ? 32 SER A N 1 ATOM 238 C CA . SER A 1 32 ? -1.551 70.658 0.637 1.00 96.11 ? 32 SER A CA 1 ATOM 239 C C . SER A 1 32 ? -1.455 69.144 0.494 1.00 94.09 ? 32 SER A C 1 ATOM 240 O O . SER A 1 32 ? -2.440 68.427 0.669 1.00 94.31 ? 32 SER A O 1 ATOM 241 C CB . SER A 1 32 ? -2.333 71.254 -0.534 1.00 101.20 ? 32 SER A CB 1 ATOM 242 O OG . SER A 1 32 ? -1.638 71.074 -1.756 1.00 105.95 ? 32 SER A OG 1 ATOM 243 N N . ARG A 1 33 ? -0.258 68.665 0.171 1.00 93.04 ? 33 ARG A N 1 ATOM 244 C CA . ARG A 1 33 ? -0.007 67.235 0.045 1.00 90.87 ? 33 ARG A CA 1 ATOM 245 C C . ARG A 1 33 ? 0.074 66.552 1.406 1.00 95.04 ? 33 ARG A C 1 ATOM 246 O O . ARG A 1 33 ? 0.353 67.192 2.421 1.00 93.61 ? 33 ARG A O 1 ATOM 247 C CB . ARG A 1 33 ? 1.285 66.986 -0.738 1.00 93.35 ? 33 ARG A CB 1 ATOM 248 C CG . ARG A 1 33 ? 1.132 67.090 -2.245 1.00 103.50 ? 33 ARG A CG 1 ATOM 249 C CD . ARG A 1 33 ? 0.163 66.041 -2.762 1.00 118.18 ? 33 ARG A CD 1 ATOM 250 N NE . ARG A 1 33 ? 0.458 64.720 -2.215 1.00 129.90 ? 33 ARG A NE 1 ATOM 251 C CZ . ARG A 1 33 ? -0.242 63.624 -2.486 1.00 134.29 ? 33 ARG A CZ 1 ATOM 252 N NH1 . ARG A 1 33 ? -1.284 63.684 -3.304 1.00 131.04 ? 33 ARG A NH1 1 ATOM 253 N NH2 . ARG A 1 33 ? 0.100 62.466 -1.938 1.00 135.31 ? 33 ARG A NH2 1 ATOM 254 N N . MET A 1 34 ? -0.176 65.246 1.417 1.00 96.31 ? 34 MET A N 1 ATOM 255 C CA . MET A 1 34 ? -0.066 64.444 2.630 1.00 86.49 ? 34 MET A CA 1 ATOM 256 C C . MET A 1 34 ? 0.798 63.218 2.361 1.00 84.44 ? 34 MET A C 1 ATOM 257 O O . MET A 1 34 ? 0.904 62.766 1.221 1.00 99.73 ? 34 MET A O 1 ATOM 258 C CB . MET A 1 34 ? -1.449 64.026 3.131 1.00 83.03 ? 34 MET A CB 1 ATOM 259 C CG . MET A 1 34 ? -2.373 65.194 3.437 1.00 97.02 ? 34 MET A CG 1 ATOM 260 S SD . MET A 1 34 ? -4.032 64.676 3.914 1.00 94.95 ? 34 MET A SD 1 ATOM 261 C CE . MET A 1 34 ? -4.831 66.264 4.132 1.00 101.65 ? 34 MET A CE 1 ATOM 262 N N . PHE A 1 35 ? 1.417 62.681 3.407 1.00 73.85 ? 35 PHE A N 1 ATOM 263 C CA . PHE A 1 35 ? 2.335 61.559 3.245 1.00 72.74 ? 35 PHE A CA 1 ATOM 264 C C . PHE A 1 35 ? 2.137 60.483 4.306 1.00 73.92 ? 35 PHE A C 1 ATOM 265 O O . PHE A 1 35 ? 1.516 60.720 5.342 1.00 80.89 ? 35 PHE A O 1 ATOM 266 C CB . PHE A 1 35 ? 3.784 62.051 3.279 1.00 77.51 ? 35 PHE A CB 1 ATOM 267 C CG . PHE A 1 35 ? 4.121 63.028 2.190 1.00 82.20 ? 35 PHE A CG 1 ATOM 268 C CD1 . PHE A 1 35 ? 3.971 64.390 2.393 1.00 78.56 ? 35 PHE A CD1 1 ATOM 269 C CD2 . PHE A 1 35 ? 4.591 62.586 0.965 1.00 87.04 ? 35 PHE A CD2 1 ATOM 270 C CE1 . PHE A 1 35 ? 4.281 65.292 1.394 1.00 105.19 ? 35 PHE A CE1 1 ATOM 271 C CE2 . PHE A 1 35 ? 4.903 63.484 -0.038 1.00 102.02 ? 35 PHE A CE2 1 ATOM 272 C CZ . PHE A 1 35 ? 4.748 64.839 0.177 1.00 113.90 ? 35 PHE A CZ 1 ATOM 273 N N . LEU A 1 36 ? 2.675 59.298 4.036 1.00 71.33 ? 36 LEU A N 1 ATOM 274 C CA . LEU A 1 36 ? 2.637 58.198 4.992 1.00 69.45 ? 36 LEU A CA 1 ATOM 275 C C . LEU A 1 36 ? 3.995 58.032 5.660 1.00 78.03 ? 36 LEU A C 1 ATOM 276 O O . LEU A 1 36 ? 5.014 57.891 4.985 1.00 95.09 ? 36 LEU A O 1 ATOM 277 C CB . LEU A 1 36 ? 2.229 56.887 4.311 1.00 70.33 ? 36 LEU A CB 1 ATOM 278 C CG . LEU A 1 36 ? 0.834 56.769 3.691 1.00 86.10 ? 36 LEU A CG 1 ATOM 279 C CD1 . LEU A 1 36 ? 0.807 57.338 2.281 1.00 119.37 ? 36 LEU A CD1 1 ATOM 280 C CD2 . LEU A 1 36 ? 0.368 55.320 3.695 1.00 71.27 ? 36 LEU A CD2 1 ATOM 281 N N . LEU A 1 37 ? 4.007 58.056 6.988 1.00 60.19 ? 37 LEU A N 1 ATOM 282 C CA . LEU A 1 37 ? 5.233 57.818 7.738 1.00 66.85 ? 37 LEU A CA 1 ATOM 283 C C . LEU A 1 37 ? 5.304 56.366 8.188 1.00 67.19 ? 37 LEU A C 1 ATOM 284 O O . LEU A 1 37 ? 4.417 55.877 8.888 1.00 59.71 ? 37 LEU A O 1 ATOM 285 C CB . LEU A 1 37 ? 5.325 58.753 8.943 1.00 67.00 ? 37 LEU A CB 1 ATOM 286 C CG . LEU A 1 37 ? 5.460 60.239 8.615 1.00 58.83 ? 37 LEU A CG 1 ATOM 287 C CD1 . LEU A 1 37 ? 5.717 61.047 9.875 1.00 57.27 ? 37 LEU A CD1 1 ATOM 288 C CD2 . LEU A 1 37 ? 6.564 60.462 7.595 1.00 61.35 ? 37 LEU A CD2 1 ATOM 289 N N . VAL A 1 38 ? 6.361 55.677 7.773 1.00 57.22 ? 38 VAL A N 1 ATOM 290 C CA . VAL A 1 38 ? 6.533 54.272 8.111 1.00 55.90 ? 38 VAL A CA 1 ATOM 291 C C . VAL A 1 38 ? 7.899 54.022 8.743 1.00 60.48 ? 38 VAL A C 1 ATOM 292 O O . VAL A 1 38 ? 8.933 54.325 8.146 1.00 57.67 ? 38 VAL A O 1 ATOM 293 C CB . VAL A 1 38 ? 6.383 53.371 6.872 1.00 63.15 ? 38 VAL A CB 1 ATOM 294 C CG1 . VAL A 1 38 ? 6.365 51.918 7.286 1.00 57.58 ? 38 VAL A CG1 1 ATOM 295 C CG2 . VAL A 1 38 ? 5.116 53.720 6.104 1.00 62.86 ? 38 VAL A CG2 1 ATOM 296 N N . GLY A 1 39 ? 7.899 53.475 9.954 1.00 52.31 ? 39 GLY A N 1 ATOM 297 C CA . GLY A 1 39 ? 9.138 53.153 10.639 1.00 53.64 ? 39 GLY A CA 1 ATOM 298 C C . GLY A 1 39 ? 9.717 51.816 10.215 1.00 64.34 ? 39 GLY A C 1 ATOM 299 O O . GLY A 1 39 ? 8.982 50.860 9.963 1.00 74.92 ? 39 GLY A O 1 ATOM 300 N N . ALA A 1 40 ? 11.043 51.752 10.142 1.00 55.91 ? 40 ALA A N 1 ATOM 301 C CA . ALA A 1 40 ? 11.749 50.524 9.789 1.00 54.52 ? 40 ALA A CA 1 ATOM 302 C C . ALA A 1 40 ? 13.021 50.397 10.619 1.00 57.49 ? 40 ALA A C 1 ATOM 303 O O . ALA A 1 40 ? 14.113 50.693 10.135 1.00 67.72 ? 40 ALA A O 1 ATOM 304 C CB . ALA A 1 40 ? 12.072 50.500 8.304 1.00 57.94 ? 40 ALA A CB 1 ATOM 305 N N . PRO A 1 41 ? 12.880 49.954 11.877 1.00 54.59 ? 41 PRO A N 1 ATOM 306 C CA . PRO A 1 41 ? 13.955 49.986 12.877 1.00 58.65 ? 41 PRO A CA 1 ATOM 307 C C . PRO A 1 41 ? 15.159 49.095 12.564 1.00 58.14 ? 41 PRO A C 1 ATOM 308 O O . PRO A 1 41 ? 16.241 49.346 13.095 1.00 65.88 ? 41 PRO A O 1 ATOM 309 C CB . PRO A 1 41 ? 13.253 49.503 14.150 1.00 59.78 ? 41 PRO A CB 1 ATOM 310 C CG . PRO A 1 41 ? 12.135 48.657 13.660 1.00 68.78 ? 41 PRO A CG 1 ATOM 311 C CD . PRO A 1 41 ? 11.658 49.321 12.403 1.00 66.21 ? 41 PRO A CD 1 ATOM 312 N N . LYS A 1 42 ? 14.977 48.063 11.748 1.00 55.48 ? 42 LYS A N 1 ATOM 313 C CA . LYS A 1 42 ? 16.084 47.169 11.415 1.00 60.23 ? 42 LYS A CA 1 ATOM 314 C C . LYS A 1 42 ? 16.742 47.499 10.074 1.00 67.55 ? 42 LYS A C 1 ATOM 315 O O . LYS A 1 42 ? 17.642 46.786 9.629 1.00 78.46 ? 42 LYS A O 1 ATOM 316 C CB . LYS A 1 42 ? 15.612 45.715 11.425 1.00 63.20 ? 42 LYS A CB 1 ATOM 317 C CG . LYS A 1 42 ? 15.079 45.259 12.774 1.00 63.02 ? 42 LYS A CG 1 ATOM 318 C CD . LYS A 1 42 ? 15.293 43.770 12.987 1.00 72.38 ? 42 LYS A CD 1 ATOM 319 C CE . LYS A 1 42 ? 16.759 43.448 13.207 1.00 96.15 ? 42 LYS A CE 1 ATOM 320 N NZ . LYS A 1 42 ? 16.983 41.994 13.436 1.00 115.82 ? 42 LYS A NZ 1 ATOM 321 N N . ALA A 1 43 ? 16.287 48.569 9.430 1.00 68.04 ? 43 ALA A N 1 ATOM 322 C CA . ALA A 1 43 ? 16.817 48.962 8.126 1.00 68.96 ? 43 ALA A CA 1 ATOM 323 C C . ALA A 1 43 ? 18.270 49.424 8.204 1.00 80.29 ? 43 ALA A C 1 ATOM 324 O O . ALA A 1 43 ? 18.690 50.020 9.196 1.00 86.66 ? 43 ALA A O 1 ATOM 325 C CB . ALA A 1 43 ? 15.954 50.056 7.517 1.00 63.58 ? 43 ALA A CB 1 ATOM 326 N N . ASN A 1 44 ? 19.032 49.143 7.150 1.00 85.65 ? 44 ASN A N 1 ATOM 327 C CA . ASN A 1 44 ? 20.417 49.594 7.056 1.00 81.68 ? 44 ASN A CA 1 ATOM 328 C C . ASN A 1 44 ? 20.514 51.051 6.619 1.00 78.73 ? 44 ASN A C 1 ATOM 329 O O . ASN A 1 44 ? 19.676 51.536 5.860 1.00 87.05 ? 44 ASN A O 1 ATOM 330 C CB . ASN A 1 44 ? 21.208 48.710 6.090 1.00 86.79 ? 44 ASN A CB 1 ATOM 331 C CG . ASN A 1 44 ? 21.802 47.496 6.771 1.00 90.20 ? 44 ASN A CG 1 ATOM 332 O OD1 . ASN A 1 44 ? 22.698 47.620 7.605 1.00 88.00 ? 44 ASN A OD1 1 ATOM 333 N ND2 . ASN A 1 44 ? 21.313 46.314 6.417 1.00 123.35 ? 44 ASN A ND2 1 ATOM 334 N N . THR A 1 45 ? 21.543 51.742 7.097 1.00 74.64 ? 45 THR A N 1 ATOM 335 C CA . THR A 1 45 ? 21.710 53.161 6.802 1.00 72.89 ? 45 THR A CA 1 ATOM 336 C C . THR A 1 45 ? 23.057 53.468 6.160 1.00 86.34 ? 45 THR A C 1 ATOM 337 O O . THR A 1 45 ? 23.987 52.663 6.213 1.00 86.49 ? 45 THR A O 1 ATOM 338 C CB . THR A 1 45 ? 21.572 54.021 8.072 1.00 73.45 ? 45 THR A CB 1 ATOM 339 O OG1 . THR A 1 45 ? 22.549 53.613 9.038 1.00 69.47 ? 45 THR A OG1 1 ATOM 340 C CG2 . THR A 1 45 ? 20.186 53.873 8.667 1.00 75.60 ? 45 THR A CG2 1 ATOM 341 N N . THR A 1 46 ? 23.146 54.648 5.554 1.00 92.16 ? 46 THR A N 1 ATOM 342 C CA . THR A 1 46 ? 24.386 55.127 4.958 1.00 82.44 ? 46 THR A CA 1 ATOM 343 C C . THR A 1 46 ? 25.344 55.631 6.035 1.00 88.74 ? 46 THR A C 1 ATOM 344 O O . THR A 1 46 ? 26.488 55.985 5.746 1.00 91.42 ? 46 THR A O 1 ATOM 345 C CB . THR A 1 46 ? 24.122 56.253 3.942 1.00 85.05 ? 46 THR A CB 1 ATOM 346 O OG1 . THR A 1 46 ? 25.365 56.702 3.386 1.00 131.86 ? 46 THR A OG1 1 ATOM 347 C CG2 . THR A 1 46 ? 23.420 57.423 4.616 1.00 82.39 ? 46 THR A CG2 1 ATOM 348 N N . GLN A 1 47 ? 24.859 55.670 7.273 1.00 80.92 ? 47 GLN A N 1 ATOM 349 C CA . GLN A 1 47 ? 25.658 56.093 8.418 1.00 76.29 ? 47 GLN A CA 1 ATOM 350 C C . GLN A 1 47 ? 26.909 55.233 8.567 1.00 83.65 ? 47 GLN A C 1 ATOM 351 O O . GLN A 1 47 ? 26.819 54.005 8.606 1.00 84.61 ? 47 GLN A O 1 ATOM 352 C CB . GLN A 1 47 ? 24.825 56.030 9.699 1.00 71.91 ? 47 GLN A CB 1 ATOM 353 C CG . GLN A 1 47 ? 23.492 56.755 9.615 1.00 70.07 ? 47 GLN A CG 1 ATOM 354 C CD . GLN A 1 47 ? 22.690 56.651 10.897 1.00 66.09 ? 47 GLN A CD 1 ATOM 355 O OE1 . GLN A 1 47 ? 21.645 56.001 10.940 1.00 78.06 ? 47 GLN A OE1 1 ATOM 356 N NE2 . GLN A 1 47 ? 23.174 57.297 11.952 1.00 77.10 ? 47 GLN A NE2 1 ATOM 357 N N . PRO A 1 48 ? 28.083 55.880 8.647 1.00 85.02 ? 48 PRO A N 1 ATOM 358 C CA . PRO A 1 48 ? 29.377 55.194 8.743 1.00 82.84 ? 48 PRO A CA 1 ATOM 359 C C . PRO A 1 48 ? 29.476 54.252 9.941 1.00 87.52 ? 48 PRO A C 1 ATOM 360 O O . PRO A 1 48 ? 29.183 54.651 11.068 1.00 82.96 ? 48 PRO A O 1 ATOM 361 C CB . PRO A 1 48 ? 30.374 56.349 8.884 1.00 84.95 ? 48 PRO A CB 1 ATOM 362 C CG . PRO A 1 48 ? 29.692 57.513 8.254 1.00 85.30 ? 48 PRO A CG 1 ATOM 363 C CD . PRO A 1 48 ? 28.239 57.343 8.580 1.00 85.33 ? 48 PRO A CD 1 ATOM 364 N N . GLY A 1 49 ? 29.895 53.016 9.686 1.00 89.46 ? 49 GLY A N 1 ATOM 365 C CA . GLY A 1 49 ? 30.091 52.030 10.734 1.00 85.50 ? 49 GLY A CA 1 ATOM 366 C C . GLY A 1 49 ? 28.842 51.672 11.516 1.00 82.27 ? 49 GLY A C 1 ATOM 367 O O . GLY A 1 49 ? 28.930 51.200 12.650 1.00 86.22 ? 49 GLY A O 1 ATOM 368 N N . ILE A 1 50 ? 27.676 51.888 10.915 1.00 78.94 ? 50 ILE A N 1 ATOM 369 C CA . ILE A 1 50 ? 26.412 51.604 11.587 1.00 78.33 ? 50 ILE A CA 1 ATOM 370 C C . ILE A 1 50 ? 25.622 50.517 10.866 1.00 84.30 ? 50 ILE A C 1 ATOM 371 O O . ILE A 1 50 ? 25.220 50.687 9.715 1.00 92.67 ? 50 ILE A O 1 ATOM 372 C CB . ILE A 1 50 ? 25.536 52.866 11.700 1.00 79.49 ? 50 ILE A CB 1 ATOM 373 C CG1 . ILE A 1 50 ? 26.312 53.996 12.379 1.00 87.91 ? 50 ILE A CG1 1 ATOM 374 C CG2 . ILE A 1 50 ? 24.254 52.559 12.460 1.00 64.94 ? 50 ILE A CG2 1 ATOM 375 C CD1 . ILE A 1 50 ? 26.891 53.616 13.722 1.00 85.93 ? 50 ILE A CD1 1 ATOM 376 N N . VAL A 1 51 ? 25.402 49.401 11.554 1.00 79.79 ? 51 VAL A N 1 ATOM 377 C CA . VAL A 1 51 ? 24.656 48.284 10.988 1.00 76.27 ? 51 VAL A CA 1 ATOM 378 C C . VAL A 1 51 ? 23.235 48.230 11.549 1.00 78.10 ? 51 VAL A C 1 ATOM 379 O O . VAL A 1 51 ? 23.038 48.238 12.766 1.00 70.46 ? 51 VAL A O 1 ATOM 380 C CB . VAL A 1 51 ? 25.374 46.940 11.250 1.00 73.87 ? 51 VAL A CB 1 ATOM 381 C CG1 . VAL A 1 51 ? 25.865 46.861 12.690 1.00 81.39 ? 51 VAL A CG1 1 ATOM 382 C CG2 . VAL A 1 51 ? 24.464 45.766 10.912 1.00 74.07 ? 51 VAL A CG2 1 ATOM 383 N N . GLU A 1 52 ? 22.256 48.186 10.647 1.00 80.26 ? 52 GLU A N 1 ATOM 384 C CA . GLU A 1 52 ? 20.838 48.147 11.006 1.00 69.64 ? 52 GLU A CA 1 ATOM 385 C C . GLU A 1 52 ? 20.453 49.275 11.957 1.00 65.41 ? 52 GLU A C 1 ATOM 386 O O . GLU A 1 52 ? 19.789 49.048 12.969 1.00 62.88 ? 52 GLU A O 1 ATOM 387 C CB . GLU A 1 52 ? 20.476 46.797 11.628 1.00 74.24 ? 52 GLU A CB 1 ATOM 388 C CG . GLU A 1 52 ? 20.542 45.631 10.657 1.00 92.94 ? 52 GLU A CG 1 ATOM 389 C CD . GLU A 1 52 ? 19.953 44.360 11.235 1.00 107.96 ? 52 GLU A CD 1 ATOM 390 O OE1 . GLU A 1 52 ? 19.719 44.317 12.461 1.00 112.31 ? 52 GLU A OE1 1 ATOM 391 O OE2 . GLU A 1 52 ? 19.718 43.406 10.463 1.00 108.31 ? 52 GLU A OE2 1 ATOM 392 N N . GLY A 1 53 ? 20.873 50.491 11.624 1.00 64.40 ? 53 GLY A N 1 ATOM 393 C CA . GLY A 1 53 ? 20.589 51.650 12.448 1.00 61.45 ? 53 GLY A CA 1 ATOM 394 C C . GLY A 1 53 ? 19.117 52.010 12.477 1.00 60.50 ? 53 GLY A C 1 ATOM 395 O O . GLY A 1 53 ? 18.655 52.689 13.393 1.00 56.48 ? 53 GLY A O 1 ATOM 396 N N . GLY A 1 54 ? 18.377 51.551 11.472 1.00 66.39 ? 54 GLY A N 1 ATOM 397 C CA . GLY A 1 54 ? 16.961 51.850 11.366 1.00 59.27 ? 54 GLY A CA 1 ATOM 398 C C . GLY A 1 54 ? 16.726 53.192 10.707 1.00 64.63 ? 54 GLY A C 1 ATOM 399 O O . GLY A 1 54 ? 17.658 53.981 10.559 1.00 97.97 ? 54 GLY A O 1 ATOM 400 N N . GLN A 1 55 ? 15.476 53.466 10.345 1.00 57.63 ? 55 GLN A N 1 ATOM 401 C CA . GLN A 1 55 ? 15.135 54.694 9.633 1.00 65.98 ? 55 GLN A CA 1 ATOM 402 C C . GLN A 1 55 ? 13.634 54.845 9.434 1.00 67.76 ? 55 GLN A C 1 ATOM 403 O O . GLN A 1 55 ? 12.870 53.891 9.582 1.00 78.85 ? 55 GLN A O 1 ATOM 404 C CB . GLN A 1 55 ? 15.826 54.739 8.265 1.00 65.12 ? 55 GLN A CB 1 ATOM 405 C CG . GLN A 1 55 ? 15.264 53.759 7.247 1.00 63.44 ? 55 GLN A CG 1 ATOM 406 C CD . GLN A 1 55 ? 15.886 53.925 5.873 1.00 78.16 ? 55 GLN A CD 1 ATOM 407 O OE1 . GLN A 1 55 ? 16.955 54.518 5.731 1.00 86.56 ? 55 GLN A OE1 1 ATOM 408 N NE2 . GLN A 1 55 ? 15.213 53.407 4.851 1.00 71.41 ? 55 GLN A NE2 1 ATOM 409 N N . VAL A 1 56 ? 13.227 56.064 9.097 1.00 66.96 ? 56 VAL A N 1 ATOM 410 C CA . VAL A 1 56 ? 11.828 56.384 8.853 1.00 62.25 ? 56 VAL A CA 1 ATOM 411 C C . VAL A 1 56 ? 11.663 56.870 7.421 1.00 79.96 ? 56 VAL A C 1 ATOM 412 O O . VAL A 1 56 ? 12.428 57.715 6.954 1.00 95.13 ? 56 VAL A O 1 ATOM 413 C CB . VAL A 1 56 ? 11.318 57.460 9.828 1.00 56.18 ? 56 VAL A CB 1 ATOM 414 C CG1 . VAL A 1 56 ? 9.842 57.742 9.592 1.00 56.02 ? 56 VAL A CG1 1 ATOM 415 C CG2 . VAL A 1 56 ? 11.564 57.027 11.262 1.00 53.35 ? 56 VAL A CG2 1 ATOM 416 N N . LEU A 1 57 ? 10.666 56.339 6.722 1.00 61.81 ? 57 LEU A N 1 ATOM 417 C CA . LEU A 1 57 ? 10.478 56.674 5.317 1.00 71.17 ? 57 LEU A CA 1 ATOM 418 C C . LEU A 1 57 ? 9.247 57.543 5.091 1.00 77.02 ? 57 LEU A C 1 ATOM 419 O O . LEU A 1 57 ? 8.247 57.428 5.800 1.00 80.75 ? 57 LEU A O 1 ATOM 420 C CB . LEU A 1 57 ? 10.376 55.401 4.470 1.00 67.17 ? 57 LEU A CB 1 ATOM 421 C CG . LEU A 1 57 ? 11.640 54.545 4.336 1.00 67.71 ? 57 LEU A CG 1 ATOM 422 C CD1 . LEU A 1 57 ? 11.782 53.572 5.498 1.00 66.02 ? 57 LEU A CD1 1 ATOM 423 C CD2 . LEU A 1 57 ? 11.650 53.806 3.007 1.00 79.73 ? 57 LEU A CD2 1 ATOM 424 N N . LYS A 1 58 ? 9.339 58.420 4.097 1.00 68.90 ? 58 LYS A N 1 ATOM 425 C CA . LYS A 1 58 ? 8.217 59.253 3.688 1.00 70.12 ? 58 LYS A CA 1 ATOM 426 C C . LYS A 1 58 ? 7.592 58.673 2.426 1.00 72.86 ? 58 LYS A C 1 ATOM 427 O O . LYS A 1 58 ? 8.211 58.680 1.362 1.00 86.17 ? 58 LYS A O 1 ATOM 428 C CB . LYS A 1 58 ? 8.670 60.695 3.447 1.00 72.26 ? 58 LYS A CB 1 ATOM 429 C CG . LYS A 1 58 ? 7.546 61.645 3.064 1.00 85.41 ? 58 LYS A CG 1 ATOM 430 C CD . LYS A 1 58 ? 8.064 62.901 2.367 1.00 93.22 ? 58 LYS A CD 1 ATOM 431 C CE . LYS A 1 58 ? 8.958 63.742 3.270 1.00 98.84 ? 58 LYS A CE 1 ATOM 432 N NZ . LYS A 1 58 ? 10.403 63.395 3.141 1.00 100.23 ? 58 LYS A NZ 1 ATOM 433 N N . CYS A 1 59 ? 6.370 58.167 2.544 1.00 72.66 ? 59 CYS A N 1 ATOM 434 C CA . CYS A 1 59 ? 5.703 57.532 1.412 1.00 84.11 ? 59 CYS A CA 1 ATOM 435 C C . CYS A 1 59 ? 4.690 58.461 0.749 1.00 81.09 ? 59 CYS A C 1 ATOM 436 O O . CYS A 1 59 ? 3.774 58.966 1.397 1.00 77.65 ? 59 CYS A O 1 ATOM 437 C CB . CYS A 1 59 ? 5.019 56.237 1.855 1.00 91.98 ? 59 CYS A CB 1 ATOM 438 S SG . CYS A 1 59 ? 6.166 54.905 2.284 1.00 107.28 ? 59 CYS A SG 1 ATOM 439 N N . ASP A 1 60 ? 4.867 58.677 -0.551 1.00 89.02 ? 60 ASP A N 1 ATOM 440 C CA . ASP A 1 60 ? 4.002 59.567 -1.315 1.00 101.22 ? 60 ASP A CA 1 ATOM 441 C C . ASP A 1 60 ? 2.741 58.844 -1.782 1.00 110.64 ? 60 ASP A C 1 ATOM 442 O O . ASP A 1 60 ? 2.817 57.803 -2.433 1.00 133.09 ? 60 ASP A O 1 ATOM 443 C CB . ASP A 1 60 ? 4.758 60.141 -2.514 1.00 111.34 ? 60 ASP A CB 1 ATOM 444 C CG . ASP A 1 60 ? 3.977 61.222 -3.232 1.00 121.13 ? 60 ASP A CG 1 ATOM 445 O OD1 . ASP A 1 60 ? 4.131 61.349 -4.465 1.00 131.10 ? 60 ASP A OD1 1 ATOM 446 O OD2 . ASP A 1 60 ? 3.212 61.948 -2.564 1.00 118.64 ? 60 ASP A OD2 1 ATOM 447 N N . TRP A 1 61 ? 1.584 59.403 -1.442 1.00 96.60 ? 61 TRP A N 1 ATOM 448 C CA . TRP A 1 61 ? 0.306 58.789 -1.781 1.00 95.87 ? 61 TRP A CA 1 ATOM 449 C C . TRP A 1 61 ? -0.118 59.050 -3.224 1.00 107.23 ? 61 TRP A C 1 ATOM 450 O O . TRP A 1 61 ? -0.890 58.277 -3.795 1.00 112.83 ? 61 TRP A O 1 ATOM 451 C CB . TRP A 1 61 ? -0.788 59.282 -0.831 1.00 89.75 ? 61 TRP A CB 1 ATOM 452 C CG . TRP A 1 61 ? -2.132 58.690 -1.121 1.00 86.51 ? 61 TRP A CG 1 ATOM 453 C CD1 . TRP A 1 61 ? -2.570 57.446 -0.775 1.00 82.21 ? 61 TRP A CD1 1 ATOM 454 C CD2 . TRP A 1 61 ? -3.212 59.314 -1.825 1.00 91.78 ? 61 TRP A CD2 1 ATOM 455 N NE1 . TRP A 1 61 ? -3.857 57.256 -1.217 1.00 83.43 ? 61 TRP A NE1 1 ATOM 456 C CE2 . TRP A 1 61 ? -4.274 58.389 -1.865 1.00 89.89 ? 61 TRP A CE2 1 ATOM 457 C CE3 . TRP A 1 61 ? -3.385 60.566 -2.425 1.00 115.63 ? 61 TRP A CE3 1 ATOM 458 C CZ2 . TRP A 1 61 ? -5.491 58.676 -2.480 1.00 108.19 ? 61 TRP A CZ2 1 ATOM 459 C CZ3 . TRP A 1 61 ? -4.594 60.848 -3.035 1.00 129.31 ? 61 TRP A CZ3 1 ATOM 460 C CH2 . TRP A 1 61 ? -5.631 59.907 -3.058 1.00 122.41 ? 61 TRP A CH2 1 ATOM 461 N N . SER A 1 62 ? 0.388 60.136 -3.805 1.00 115.61 ? 62 SER A N 1 ATOM 462 C CA . SER A 1 62 ? -0.052 60.600 -5.122 1.00 131.16 ? 62 SER A CA 1 ATOM 463 C C . SER A 1 62 ? 0.014 59.510 -6.188 1.00 151.76 ? 62 SER A C 1 ATOM 464 O O . SER A 1 62 ? -0.993 59.192 -6.821 1.00 152.60 ? 62 SER A O 1 ATOM 465 C CB . SER A 1 62 ? 0.788 61.799 -5.566 1.00 129.66 ? 62 SER A CB 1 ATOM 466 O OG . SER A 1 62 ? 2.126 61.413 -5.826 1.00 129.57 ? 62 SER A OG 1 ATOM 467 N N . SER A 1 63 ? 1.198 58.936 -6.372 1.00 164.39 ? 63 SER A N 1 ATOM 468 C CA . SER A 1 63 ? 1.382 57.838 -7.315 1.00 166.49 ? 63 SER A CA 1 ATOM 469 C C . SER A 1 63 ? 2.702 57.119 -7.072 1.00 164.40 ? 63 SER A C 1 ATOM 470 O O . SER A 1 63 ? 3.476 57.504 -6.194 1.00 162.63 ? 63 SER A O 1 ATOM 471 C CB . SER A 1 63 ? 1.326 58.345 -8.759 1.00 165.26 ? 63 SER A CB 1 ATOM 472 O OG . SER A 1 63 ? 0.017 58.759 -9.109 1.00 159.52 ? 63 SER A OG 1 ATOM 473 N N . THR A 1 64 ? 2.929 56.056 -7.842 1.00 161.56 ? 64 THR A N 1 ATOM 474 C CA . THR A 1 64 ? 4.172 55.275 -7.839 1.00 156.68 ? 64 THR A CA 1 ATOM 475 C C . THR A 1 64 ? 4.414 54.528 -6.525 1.00 138.88 ? 64 THR A C 1 ATOM 476 O O . THR A 1 64 ? 5.263 53.637 -6.466 1.00 137.93 ? 64 THR A O 1 ATOM 477 C CB . THR A 1 64 ? 5.412 56.156 -8.139 1.00 123.40 ? 64 THR A CB 1 ATOM 478 O OG1 . THR A 1 64 ? 5.651 57.053 -7.046 1.00 131.05 ? 64 THR A OG1 1 ATOM 479 C CG2 . THR A 1 64 ? 5.214 56.953 -9.421 1.00 119.46 ? 64 THR A CG2 1 ATOM 480 N N . ARG A 1 65 ? 3.656 54.885 -5.489 1.00 121.26 ? 65 ARG A N 1 ATOM 481 C CA . ARG A 1 65 ? 3.790 54.302 -4.155 1.00 111.66 ? 65 ARG A CA 1 ATOM 482 C C . ARG A 1 65 ? 5.242 54.270 -3.687 1.00 113.75 ? 65 ARG A C 1 ATOM 483 O O . ARG A 1 65 ? 5.668 53.334 -3.011 1.00 130.62 ? 65 ARG A O 1 ATOM 484 C CB . ARG A 1 65 ? 3.193 52.894 -4.127 1.00 118.38 ? 65 ARG A CB 1 ATOM 485 C CG . ARG A 1 65 ? 1.737 52.844 -4.561 1.00 131.57 ? 65 ARG A CG 1 ATOM 486 C CD . ARG A 1 65 ? 0.890 53.816 -3.754 1.00 132.77 ? 65 ARG A CD 1 ATOM 487 N NE . ARG A 1 65 ? 0.032 54.633 -4.608 1.00 140.46 ? 65 ARG A NE 1 ATOM 488 C CZ . ARG A 1 65 ? -1.209 54.308 -4.953 1.00 134.89 ? 65 ARG A CZ 1 ATOM 489 N NH1 . ARG A 1 65 ? -1.747 53.178 -4.516 1.00 125.35 ? 65 ARG A NH1 1 ATOM 490 N NH2 . ARG A 1 65 ? -1.914 55.114 -5.735 1.00 132.28 ? 65 ARG A NH2 1 ATOM 491 N N . ARG A 1 66 ? 5.996 55.302 -4.050 1.00 106.31 ? 66 ARG A N 1 ATOM 492 C CA . ARG A 1 66 ? 7.423 55.347 -3.763 1.00 104.02 ? 66 ARG A CA 1 ATOM 493 C C . ARG A 1 66 ? 7.694 55.881 -2.363 1.00 97.90 ? 66 ARG A C 1 ATOM 494 O O . ARG A 1 66 ? 7.081 56.856 -1.928 1.00 100.39 ? 66 ARG A O 1 ATOM 495 C CB . ARG A 1 66 ? 8.147 56.204 -4.803 1.00 116.23 ? 66 ARG A CB 1 ATOM 496 C CG . ARG A 1 66 ? 9.662 56.150 -4.712 1.00 124.79 ? 66 ARG A CG 1 ATOM 497 C CD . ARG A 1 66 ? 10.301 56.953 -5.830 1.00 129.09 ? 66 ARG A CD 1 ATOM 498 N NE . ARG A 1 66 ? 9.833 56.520 -7.144 1.00 132.27 ? 66 ARG A NE 1 ATOM 499 C CZ . ARG A 1 66 ? 10.205 57.079 -8.291 1.00 135.02 ? 66 ARG A CZ 1 ATOM 500 N NH1 . ARG A 1 66 ? 11.055 58.097 -8.290 1.00 136.78 ? 66 ARG A NH1 1 ATOM 501 N NH2 . ARG A 1 66 ? 9.728 56.620 -9.439 1.00 136.57 ? 66 ARG A NH2 1 ATOM 502 N N . CYS A 1 67 ? 8.616 55.231 -1.662 1.00 94.40 ? 67 CYS A N 1 ATOM 503 C CA . CYS A 1 67 ? 8.980 55.638 -0.313 1.00 92.88 ? 67 CYS A CA 1 ATOM 504 C C . CYS A 1 67 ? 10.430 56.102 -0.253 1.00 100.30 ? 67 CYS A C 1 ATOM 505 O O . CYS A 1 67 ? 11.326 55.434 -0.769 1.00 108.37 ? 67 CYS A O 1 ATOM 506 C CB . CYS A 1 67 ? 8.756 54.490 0.672 1.00 85.19 ? 67 CYS A CB 1 ATOM 507 S SG . CYS A 1 67 ? 7.050 53.900 0.756 1.00 141.25 ? 67 CYS A SG 1 ATOM 508 N N . GLN A 1 68 ? 10.655 57.249 0.379 1.00 93.85 ? 68 GLN A N 1 ATOM 509 C CA . GLN A 1 68 ? 12.007 57.760 0.557 1.00 100.13 ? 68 GLN A CA 1 ATOM 510 C C . GLN A 1 68 ? 12.289 57.987 2.037 1.00 96.22 ? 68 GLN A C 1 ATOM 511 O O . GLN A 1 68 ? 11.426 58.471 2.769 1.00 98.47 ? 68 GLN A O 1 ATOM 512 C CB . GLN A 1 68 ? 12.200 59.062 -0.226 1.00 109.07 ? 68 GLN A CB 1 ATOM 513 C CG . GLN A 1 68 ? 11.947 58.938 -1.721 1.00 120.13 ? 68 GLN A CG 1 ATOM 514 C CD . GLN A 1 68 ? 13.015 58.128 -2.431 1.00 132.19 ? 68 GLN A CD 1 ATOM 515 O OE1 . GLN A 1 68 ? 14.118 57.945 -1.916 1.00 141.82 ? 68 GLN A OE1 1 ATOM 516 N NE2 . GLN A 1 68 ? 12.692 57.640 -3.623 1.00 128.99 ? 68 GLN A NE2 1 ATOM 517 N N . PRO A 1 69 ? 13.506 57.643 2.479 1.00 90.52 ? 69 PRO A N 1 ATOM 518 C CA . PRO A 1 69 ? 13.894 57.791 3.885 1.00 74.31 ? 69 PRO A CA 1 ATOM 519 C C . PRO A 1 69 ? 14.040 59.249 4.300 1.00 75.13 ? 69 PRO A C 1 ATOM 520 O O . PRO A 1 69 ? 14.633 60.040 3.567 1.00 89.82 ? 69 PRO A O 1 ATOM 521 C CB . PRO A 1 69 ? 15.249 57.073 3.956 1.00 73.35 ? 69 PRO A CB 1 ATOM 522 C CG . PRO A 1 69 ? 15.296 56.201 2.742 1.00 84.01 ? 69 PRO A CG 1 ATOM 523 C CD . PRO A 1 69 ? 14.542 56.952 1.695 1.00 97.91 ? 69 PRO A CD 1 ATOM 524 N N . ILE A 1 70 ? 13.502 59.596 5.464 1.00 75.03 ? 70 ILE A N 1 ATOM 525 C CA . ILE A 1 70 ? 13.707 60.923 6.028 1.00 78.12 ? 70 ILE A CA 1 ATOM 526 C C . ILE A 1 70 ? 15.045 60.947 6.752 1.00 82.74 ? 70 ILE A C 1 ATOM 527 O O . ILE A 1 70 ? 15.309 60.103 7.607 1.00 100.86 ? 70 ILE A O 1 ATOM 528 C CB . ILE A 1 70 ? 12.582 61.317 7.001 1.00 71.80 ? 70 ILE A CB 1 ATOM 529 C CG1 . ILE A 1 70 ? 11.221 61.215 6.310 1.00 67.84 ? 70 ILE A CG1 1 ATOM 530 C CG2 . ILE A 1 70 ? 12.807 62.723 7.535 1.00 66.78 ? 70 ILE A CG2 1 ATOM 531 C CD1 . ILE A 1 70 ? 10.057 61.556 7.210 1.00 64.56 ? 70 ILE A CD1 1 ATOM 532 N N . GLU A 1 71 ? 15.889 61.913 6.411 1.00 80.60 ? 71 GLU A N 1 ATOM 533 C CA . GLU A 1 71 ? 17.239 61.949 6.955 1.00 94.70 ? 71 GLU A CA 1 ATOM 534 C C . GLU A 1 71 ? 17.290 62.709 8.274 1.00 93.21 ? 71 GLU A C 1 ATOM 535 O O . GLU A 1 71 ? 17.005 63.906 8.329 1.00 103.63 ? 71 GLU A O 1 ATOM 536 C CB . GLU A 1 71 ? 18.205 62.576 5.948 1.00 115.88 ? 71 GLU A CB 1 ATOM 537 C CG . GLU A 1 71 ? 19.663 62.263 6.225 1.00 135.58 ? 71 GLU A CG 1 ATOM 538 C CD . GLU A 1 71 ? 19.949 60.772 6.205 1.00 145.82 ? 71 GLU A CD 1 ATOM 539 O OE1 . GLU A 1 71 ? 20.214 60.231 5.111 1.00 158.72 ? 71 GLU A OE1 1 ATOM 540 O OE2 . GLU A 1 71 ? 19.910 60.142 7.283 1.00 135.33 ? 71 GLU A OE2 1 ATOM 541 N N . PHE A 1 72 ? 17.659 62.001 9.336 1.00 75.55 ? 72 PHE A N 1 ATOM 542 C CA . PHE A 1 72 ? 17.761 62.595 10.662 1.00 71.51 ? 72 PHE A CA 1 ATOM 543 C C . PHE A 1 72 ? 19.217 62.757 11.085 1.00 77.49 ? 72 PHE A C 1 ATOM 544 O O . PHE A 1 72 ? 19.716 63.875 11.209 1.00 103.66 ? 72 PHE A O 1 ATOM 545 C CB . PHE A 1 72 ? 17.013 61.746 11.693 1.00 79.30 ? 72 PHE A CB 1 ATOM 546 C CG . PHE A 1 72 ? 15.518 61.775 11.539 1.00 77.80 ? 72 PHE A CG 1 ATOM 547 C CD1 . PHE A 1 72 ? 14.879 60.898 10.679 1.00 81.42 ? 72 PHE A CD1 1 ATOM 548 C CD2 . PHE A 1 72 ? 14.752 62.672 12.264 1.00 68.59 ? 72 PHE A CD2 1 ATOM 549 C CE1 . PHE A 1 72 ? 13.504 60.920 10.540 1.00 75.06 ? 72 PHE A CE1 1 ATOM 550 C CE2 . PHE A 1 72 ? 13.377 62.698 12.130 1.00 60.15 ? 72 PHE A CE2 1 ATOM 551 C CZ . PHE A 1 72 ? 12.753 61.821 11.267 1.00 62.57 ? 72 PHE A CZ 1 ATOM 552 N N . ASP A 1 73 ? 19.893 61.633 11.300 1.00 71.53 ? 73 ASP A N 1 ATOM 553 C CA . ASP A 1 73 ? 21.260 61.642 11.809 1.00 75.73 ? 73 ASP A CA 1 ATOM 554 C C . ASP A 1 73 ? 22.286 61.634 10.678 1.00 85.11 ? 73 ASP A C 1 ATOM 555 O O . ASP A 1 73 ? 23.055 62.585 10.529 1.00 95.12 ? 73 ASP A O 1 ATOM 556 C CB . ASP A 1 73 ? 21.486 60.444 12.736 1.00 83.10 ? 73 ASP A CB 1 ATOM 557 C CG . ASP A 1 73 ? 22.709 60.608 13.621 1.00 102.29 ? 73 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 73 ? 22.580 60.427 14.850 1.00 128.72 ? 73 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 73 ? 23.800 60.910 13.093 1.00 96.62 ? 73 ASP A OD2 1 ATOM 560 N N . ALA A 1 74 ? 22.312 60.538 9.920 1.00 85.99 ? 74 ALA A N 1 ATOM 561 C CA . ALA A 1 74 ? 23.187 60.373 8.753 1.00 90.12 ? 74 ALA A CA 1 ATOM 562 C C . ALA A 1 74 ? 24.675 60.303 9.104 1.00 80.92 ? 74 ALA A C 1 ATOM 563 O O . ALA A 1 74 ? 25.509 60.080 8.228 1.00 78.49 ? 74 ALA A O 1 ATOM 564 C CB . ALA A 1 74 ? 22.944 61.493 7.741 1.00 80.35 ? 74 ALA A CB 1 ATOM 565 N N . THR A 1 75 ? 25.008 60.491 10.377 1.00 73.28 ? 75 THR A N 1 ATOM 566 C CA . THR A 1 75 ? 26.404 60.495 10.804 1.00 87.05 ? 75 THR A CA 1 ATOM 567 C C . THR A 1 75 ? 26.798 59.201 11.510 1.00 84.91 ? 75 THR A C 1 ATOM 568 O O . THR A 1 75 ? 25.996 58.277 11.637 1.00 71.06 ? 75 THR A O 1 ATOM 569 C CB . THR A 1 75 ? 26.699 61.678 11.745 1.00 90.66 ? 75 THR A CB 1 ATOM 570 O OG1 . THR A 1 75 ? 25.905 61.559 12.932 1.00 70.95 ? 75 THR A OG1 1 ATOM 571 C CG2 . THR A 1 75 ? 26.384 62.997 11.059 1.00 99.66 ? 75 THR A CG2 1 ATOM 572 N N . GLY A 1 76 ? 28.040 59.154 11.984 1.00 88.18 ? 76 GLY A N 1 ATOM 573 C CA . GLY A 1 76 ? 28.540 58.020 12.740 1.00 77.77 ? 76 GLY A CA 1 ATOM 574 C C . GLY A 1 76 ? 28.058 58.161 14.167 1.00 70.41 ? 76 GLY A C 1 ATOM 575 O O . GLY A 1 76 ? 27.010 58.762 14.402 1.00 68.38 ? 76 GLY A O 1 ATOM 576 N N . ASN A 1 77 ? 28.786 57.609 15.132 1.00 70.06 ? 77 ASN A N 1 ATOM 577 C CA . ASN A 1 77 ? 28.312 57.742 16.498 1.00 94.53 ? 77 ASN A CA 1 ATOM 578 C C . ASN A 1 77 ? 28.862 58.983 17.187 1.00 92.00 ? 77 ASN A C 1 ATOM 579 O O . ASN A 1 77 ? 28.228 60.038 17.159 1.00 111.15 ? 77 ASN A O 1 ATOM 580 C CB . ASN A 1 77 ? 28.705 56.507 17.310 1.00 82.60 ? 77 ASN A CB 1 ATOM 581 C CG . ASN A 1 77 ? 28.417 55.208 16.584 1.00 87.06 ? 77 ASN A CG 1 ATOM 582 O OD1 . ASN A 1 77 ? 27.372 54.590 16.787 1.00 69.44 ? 77 ASN A OD1 1 ATOM 583 N ND2 . ASN A 1 77 ? 29.352 54.780 15.742 1.00 109.76 ? 77 ASN A ND2 1 ATOM 584 N N . ARG A 1 78 ? 30.075 58.860 17.724 1.00 71.80 ? 78 ARG A N 1 ATOM 585 C CA . ARG A 1 78 ? 30.785 59.938 18.418 1.00 78.79 ? 78 ARG A CA 1 ATOM 586 C C . ARG A 1 78 ? 32.028 59.353 19.081 1.00 87.56 ? 78 ARG A C 1 ATOM 587 O O . ARG A 1 78 ? 32.216 58.137 19.080 1.00 105.60 ? 78 ARG A O 1 ATOM 588 C CB . ARG A 1 78 ? 29.899 60.634 19.455 1.00 77.46 ? 78 ARG A CB 1 ATOM 589 C CG . ARG A 1 78 ? 29.671 62.109 19.149 1.00 77.25 ? 78 ARG A CG 1 ATOM 590 C CD . ARG A 1 78 ? 28.405 62.645 19.795 1.00 70.59 ? 78 ARG A CD 1 ATOM 591 N NE . ARG A 1 78 ? 27.202 62.295 19.045 1.00 68.53 ? 78 ARG A NE 1 ATOM 592 C CZ . ARG A 1 78 ? 25.993 62.786 19.303 1.00 85.34 ? 78 ARG A CZ 1 ATOM 593 N NH1 . ARG A 1 78 ? 25.825 63.652 20.293 1.00 63.67 ? 78 ARG A NH1 1 ATOM 594 N NH2 . ARG A 1 78 ? 24.952 62.414 18.570 1.00 104.52 ? 78 ARG A NH2 1 ATOM 595 N N . ASP A 1 79 ? 32.868 60.206 19.658 1.00 79.46 ? 79 ASP A N 1 ATOM 596 C CA . ASP A 1 79 ? 34.060 59.728 20.354 1.00 83.08 ? 79 ASP A CA 1 ATOM 597 C C . ASP A 1 79 ? 34.252 60.370 21.728 1.00 82.43 ? 79 ASP A C 1 ATOM 598 O O . ASP A 1 79 ? 34.262 61.594 21.860 1.00 108.15 ? 79 ASP A O 1 ATOM 599 C CB . ASP A 1 79 ? 35.311 59.966 19.504 1.00 115.22 ? 79 ASP A CB 1 ATOM 600 C CG . ASP A 1 79 ? 35.477 58.934 18.404 1.00 123.45 ? 79 ASP A CG 1 ATOM 601 O OD1 . ASP A 1 79 ? 36.563 58.322 18.326 1.00 139.83 ? 79 ASP A OD1 1 ATOM 602 O OD2 . ASP A 1 79 ? 34.533 58.739 17.611 1.00 111.64 ? 79 ASP A OD2 1 ATOM 603 N N . TYR A 1 80 ? 34.386 59.526 22.746 1.00 80.42 ? 80 TYR A N 1 ATOM 604 C CA . TYR A 1 80 ? 34.752 59.964 24.090 1.00 75.52 ? 80 TYR A CA 1 ATOM 605 C C . TYR A 1 80 ? 36.266 60.154 24.206 1.00 79.72 ? 80 TYR A C 1 ATOM 606 O O . TYR A 1 80 ? 36.741 61.020 24.941 1.00 80.84 ? 80 TYR A O 1 ATOM 607 C CB . TYR A 1 80 ? 34.250 58.953 25.126 1.00 78.79 ? 80 TYR A CB 1 ATOM 608 C CG . TYR A 1 80 ? 34.619 59.268 26.558 1.00 73.83 ? 80 TYR A CG 1 ATOM 609 C CD1 . TYR A 1 80 ? 33.911 60.214 27.288 1.00 82.08 ? 80 TYR A CD1 1 ATOM 610 C CD2 . TYR A 1 80 ? 35.661 58.601 27.189 1.00 75.79 ? 80 TYR A CD2 1 ATOM 611 C CE1 . TYR A 1 80 ? 34.240 60.498 28.600 1.00 86.85 ? 80 TYR A CE1 1 ATOM 612 C CE2 . TYR A 1 80 ? 35.997 58.877 28.500 1.00 95.19 ? 80 TYR A CE2 1 ATOM 613 C CZ . TYR A 1 80 ? 35.284 59.826 29.201 1.00 95.78 ? 80 TYR A CZ 1 ATOM 614 O OH . TYR A 1 80 ? 35.616 60.104 30.507 1.00 108.77 ? 80 TYR A OH 1 ATOM 615 N N . ALA A 1 81 ? 37.013 59.336 23.470 1.00 82.48 ? 81 ALA A N 1 ATOM 616 C CA . ALA A 1 81 ? 38.476 59.361 23.483 1.00 89.11 ? 81 ALA A CA 1 ATOM 617 C C . ALA A 1 81 ? 39.012 58.905 22.128 1.00 101.60 ? 81 ALA A C 1 ATOM 618 O O . ALA A 1 81 ? 38.257 58.858 21.156 1.00 100.22 ? 81 ALA A O 1 ATOM 619 C CB . ALA A 1 81 ? 39.024 58.492 24.601 1.00 94.10 ? 81 ALA A CB 1 ATOM 620 N N . LYS A 1 82 ? 40.311 58.606 22.063 1.00 112.59 ? 82 LYS A N 1 ATOM 621 C CA . LYS A 1 82 ? 40.959 58.183 20.817 1.00 117.86 ? 82 LYS A CA 1 ATOM 622 C C . LYS A 1 82 ? 40.154 57.098 20.105 1.00 125.59 ? 82 LYS A C 1 ATOM 623 O O . LYS A 1 82 ? 39.556 57.363 19.062 1.00 144.02 ? 82 LYS A O 1 ATOM 624 C CB . LYS A 1 82 ? 42.384 57.698 21.090 1.00 121.84 ? 82 LYS A CB 1 ATOM 625 C CG . LYS A 1 82 ? 43.330 58.809 21.521 1.00 129.06 ? 82 LYS A CG 1 ATOM 626 C CD . LYS A 1 82 ? 44.779 58.352 21.518 1.00 130.41 ? 82 LYS A CD 1 ATOM 627 C CE . LYS A 1 82 ? 45.715 59.508 21.834 1.00 131.73 ? 82 LYS A CE 1 ATOM 628 N NZ . LYS A 1 82 ? 47.147 59.107 21.762 1.00 138.62 ? 82 LYS A NZ 1 ATOM 629 N N . ASP A 1 83 ? 40.130 55.884 20.647 1.00 109.37 ? 83 ASP A N 1 ATOM 630 C CA . ASP A 1 83 ? 39.018 55.001 20.329 1.00 101.53 ? 83 ASP A CA 1 ATOM 631 C C . ASP A 1 83 ? 38.242 54.724 21.607 1.00 93.41 ? 83 ASP A C 1 ATOM 632 O O . ASP A 1 83 ? 38.609 53.855 22.397 1.00 102.17 ? 83 ASP A O 1 ATOM 633 C CB . ASP A 1 83 ? 39.512 53.694 19.704 1.00 111.91 ? 83 ASP A CB 1 ATOM 634 C CG . ASP A 1 83 ? 40.290 53.918 18.422 1.00 142.03 ? 83 ASP A CG 1 ATOM 635 O OD1 . ASP A 1 83 ? 39.930 54.837 17.658 1.00 158.51 ? 83 ASP A OD1 1 ATOM 636 O OD2 . ASP A 1 83 ? 41.264 53.173 18.180 1.00 146.98 ? 83 ASP A OD2 1 ATOM 637 N N . ASP A 1 84 ? 37.160 55.468 21.794 1.00 85.83 ? 84 ASP A N 1 ATOM 638 C CA . ASP A 1 84 ? 36.221 55.235 22.880 1.00 79.98 ? 84 ASP A CA 1 ATOM 639 C C . ASP A 1 84 ? 34.840 55.709 22.457 1.00 75.45 ? 84 ASP A C 1 ATOM 640 O O . ASP A 1 84 ? 34.452 56.824 22.803 1.00 81.81 ? 84 ASP A O 1 ATOM 641 C CB . ASP A 1 84 ? 36.669 55.938 24.160 1.00 82.17 ? 84 ASP A CB 1 ATOM 642 C CG . ASP A 1 84 ? 36.156 55.252 25.412 1.00 98.28 ? 84 ASP A CG 1 ATOM 643 O OD1 . ASP A 1 84 ? 35.045 54.681 25.369 1.00 117.80 ? 84 ASP A OD1 1 ATOM 644 O OD2 . ASP A 1 84 ? 36.867 55.278 26.439 1.00 97.44 ? 84 ASP A OD2 1 ATOM 645 N N . PRO A 1 85 ? 34.110 54.894 21.681 1.00 73.29 ? 85 PRO A N 1 ATOM 646 C CA . PRO A 1 85 ? 32.817 55.342 21.149 1.00 71.57 ? 85 PRO A CA 1 ATOM 647 C C . PRO A 1 85 ? 31.896 55.887 22.240 1.00 69.23 ? 85 PRO A C 1 ATOM 648 O O . PRO A 1 85 ? 31.693 55.242 23.267 1.00 76.82 ? 85 PRO A O 1 ATOM 649 C CB . PRO A 1 85 ? 32.233 54.069 20.520 1.00 76.47 ? 85 PRO A CB 1 ATOM 650 C CG . PRO A 1 85 ? 33.048 52.935 21.081 1.00 80.76 ? 85 PRO A CG 1 ATOM 651 C CD . PRO A 1 85 ? 34.405 53.499 21.322 1.00 83.89 ? 85 PRO A CD 1 ATOM 652 N N . LEU A 1 86 ? 31.363 57.083 22.010 1.00 71.02 ? 86 LEU A N 1 ATOM 653 C CA . LEU A 1 86 ? 30.560 57.778 23.009 1.00 70.96 ? 86 LEU A CA 1 ATOM 654 C C . LEU A 1 86 ? 29.095 57.377 22.910 1.00 71.70 ? 86 LEU A C 1 ATOM 655 O O . LEU A 1 86 ? 28.295 57.673 23.794 1.00 73.84 ? 86 LEU A O 1 ATOM 656 C CB . LEU A 1 86 ? 30.714 59.292 22.847 1.00 85.37 ? 86 LEU A CB 1 ATOM 657 C CG . LEU A 1 86 ? 30.022 60.219 23.847 1.00 84.07 ? 86 LEU A CG 1 ATOM 658 C CD1 . LEU A 1 86 ? 30.258 59.754 25.274 1.00 90.10 ? 86 LEU A CD1 1 ATOM 659 C CD2 . LEU A 1 86 ? 30.533 61.628 23.661 1.00 112.38 ? 86 LEU A CD2 1 ATOM 660 N N . GLU A 1 87 ? 28.749 56.711 21.818 1.00 68.91 ? 87 GLU A N 1 ATOM 661 C CA . GLU A 1 87 ? 27.404 56.185 21.640 1.00 62.76 ? 87 GLU A CA 1 ATOM 662 C C . GLU A 1 87 ? 27.414 55.058 20.619 1.00 67.38 ? 87 GLU A C 1 ATOM 663 O O . GLU A 1 87 ? 28.389 54.880 19.892 1.00 62.30 ? 87 GLU A O 1 ATOM 664 C CB . GLU A 1 87 ? 26.436 57.290 21.221 1.00 58.42 ? 87 GLU A CB 1 ATOM 665 C CG . GLU A 1 87 ? 26.897 58.141 20.054 1.00 60.72 ? 87 GLU A CG 1 ATOM 666 C CD . GLU A 1 87 ? 25.905 59.238 19.722 1.00 64.83 ? 87 GLU A CD 1 ATOM 667 O OE1 . GLU A 1 87 ? 25.957 59.775 18.598 1.00 61.64 ? 87 GLU A OE1 1 ATOM 668 O OE2 . GLU A 1 87 ? 25.067 59.562 20.589 1.00 74.25 ? 87 GLU A OE2 1 ATOM 669 N N . PHE A 1 88 ? 26.343 54.275 20.591 1.00 69.51 ? 88 PHE A N 1 ATOM 670 C CA . PHE A 1 88 ? 26.253 53.170 19.649 1.00 58.20 ? 88 PHE A CA 1 ATOM 671 C C . PHE A 1 88 ? 24.926 53.189 18.897 1.00 63.57 ? 88 PHE A C 1 ATOM 672 O O . PHE A 1 88 ? 23.863 52.988 19.484 1.00 81.49 ? 88 PHE A O 1 ATOM 673 C CB . PHE A 1 88 ? 26.444 51.846 20.388 1.00 57.81 ? 88 PHE A CB 1 ATOM 674 C CG . PHE A 1 88 ? 27.597 51.859 21.352 1.00 59.14 ? 88 PHE A CG 1 ATOM 675 C CD1 . PHE A 1 88 ? 28.879 51.561 20.923 1.00 62.09 ? 88 PHE A CD1 1 ATOM 676 C CD2 . PHE A 1 88 ? 27.401 52.186 22.684 1.00 57.76 ? 88 PHE A CD2 1 ATOM 677 C CE1 . PHE A 1 88 ? 29.941 51.579 21.805 1.00 63.55 ? 88 PHE A CE1 1 ATOM 678 C CE2 . PHE A 1 88 ? 28.461 52.207 23.572 1.00 59.27 ? 88 PHE A CE2 1 ATOM 679 C CZ . PHE A 1 88 ? 29.732 51.903 23.131 1.00 62.13 ? 88 PHE A CZ 1 ATOM 680 N N . LYS A 1 89 ? 25.000 53.431 17.592 1.00 62.53 ? 89 LYS A N 1 ATOM 681 C CA . LYS A 1 89 ? 23.813 53.506 16.750 1.00 59.05 ? 89 LYS A CA 1 ATOM 682 C C . LYS A 1 89 ? 23.480 52.150 16.140 1.00 59.44 ? 89 LYS A C 1 ATOM 683 O O . LYS A 1 89 ? 22.443 51.987 15.501 1.00 69.52 ? 89 LYS A O 1 ATOM 684 C CB . LYS A 1 89 ? 24.008 54.539 15.638 1.00 79.90 ? 89 LYS A CB 1 ATOM 685 C CG . LYS A 1 89 ? 24.443 55.916 16.114 1.00 88.99 ? 89 LYS A CG 1 ATOM 686 C CD . LYS A 1 89 ? 23.261 56.753 16.567 1.00 99.18 ? 89 LYS A CD 1 ATOM 687 C CE . LYS A 1 89 ? 23.701 58.150 16.966 1.00 108.14 ? 89 LYS A CE 1 ATOM 688 N NZ . LYS A 1 89 ? 24.467 58.822 15.879 1.00 93.04 ? 89 LYS A NZ 1 ATOM 689 N N . SER A 1 90 ? 24.368 51.180 16.333 1.00 68.89 ? 90 SER A N 1 ATOM 690 C CA . SER A 1 90 ? 24.185 49.857 15.748 1.00 73.41 ? 90 SER A CA 1 ATOM 691 C C . SER A 1 90 ? 23.028 49.117 16.407 1.00 69.56 ? 90 SER A C 1 ATOM 692 O O . SER A 1 90 ? 23.006 48.944 17.626 1.00 66.59 ? 90 SER A O 1 ATOM 693 C CB . SER A 1 90 ? 25.470 49.036 15.868 1.00 76.35 ? 90 SER A CB 1 ATOM 694 O OG . SER A 1 90 ? 26.538 49.657 15.174 1.00 82.11 ? 90 SER A OG 1 ATOM 695 N N . HIS A 1 91 ? 22.075 48.683 15.584 1.00 70.58 ? 91 HIS A N 1 ATOM 696 C CA . HIS A 1 91 ? 20.880 47.981 16.048 1.00 66.16 ? 91 HIS A CA 1 ATOM 697 C C . HIS A 1 91 ? 20.137 48.784 17.111 1.00 59.28 ? 91 HIS A C 1 ATOM 698 O O . HIS A 1 91 ? 19.608 48.223 18.071 1.00 52.69 ? 91 HIS A O 1 ATOM 699 C CB . HIS A 1 91 ? 21.247 46.597 16.590 1.00 59.21 ? 91 HIS A CB 1 ATOM 700 C CG . HIS A 1 91 ? 22.056 45.772 15.638 1.00 62.42 ? 91 HIS A CG 1 ATOM 701 N ND1 . HIS A 1 91 ? 21.483 44.949 14.693 1.00 65.07 ? 91 HIS A ND1 1 ATOM 702 C CD2 . HIS A 1 91 ? 23.395 45.645 15.485 1.00 73.79 ? 91 HIS A CD2 1 ATOM 703 C CE1 . HIS A 1 91 ? 22.434 44.349 13.999 1.00 70.08 ? 91 HIS A CE1 1 ATOM 704 N NE2 . HIS A 1 91 ? 23.604 44.754 14.460 1.00 75.83 ? 91 HIS A NE2 1 ATOM 705 N N . GLN A 1 92 ? 20.096 50.101 16.929 1.00 53.64 ? 92 GLN A N 1 ATOM 706 C CA . GLN A 1 92 ? 19.485 50.994 17.906 1.00 53.08 ? 92 GLN A CA 1 ATOM 707 C C . GLN A 1 92 ? 17.972 51.051 17.747 1.00 52.57 ? 92 GLN A C 1 ATOM 708 O O . GLN A 1 92 ? 17.284 51.684 18.550 1.00 55.38 ? 92 GLN A O 1 ATOM 709 C CB . GLN A 1 92 ? 20.071 52.402 17.785 1.00 54.31 ? 92 GLN A CB 1 ATOM 710 C CG . GLN A 1 92 ? 19.689 53.127 16.506 1.00 51.66 ? 92 GLN A CG 1 ATOM 711 C CD . GLN A 1 92 ? 20.290 54.515 16.429 1.00 67.94 ? 92 GLN A CD 1 ATOM 712 O OE1 . GLN A 1 92 ? 20.717 55.074 17.438 1.00 61.76 ? 92 GLN A OE1 1 ATOM 713 N NE2 . GLN A 1 92 ? 20.331 55.078 15.227 1.00 95.77 ? 92 GLN A NE2 1 ATOM 714 N N . TRP A 1 93 ? 17.466 50.392 16.706 1.00 53.19 ? 93 TRP A N 1 ATOM 715 C CA . TRP A 1 93 ? 16.035 50.356 16.418 1.00 58.16 ? 93 TRP A CA 1 ATOM 716 C C . TRP A 1 93 ? 15.448 51.752 16.246 1.00 59.96 ? 93 TRP A C 1 ATOM 717 O O . TRP A 1 93 ? 14.429 52.080 16.853 1.00 61.25 ? 93 TRP A O 1 ATOM 718 C CB . TRP A 1 93 ? 15.280 49.615 17.526 1.00 54.55 ? 93 TRP A CB 1 ATOM 719 C CG . TRP A 1 93 ? 15.261 48.128 17.371 1.00 48.63 ? 93 TRP A CG 1 ATOM 720 C CD1 . TRP A 1 93 ? 16.336 47.288 17.372 1.00 68.13 ? 93 TRP A CD1 1 ATOM 721 C CD2 . TRP A 1 93 ? 14.104 47.299 17.212 1.00 47.73 ? 93 TRP A CD2 1 ATOM 722 N NE1 . TRP A 1 93 ? 15.920 45.988 17.215 1.00 71.19 ? 93 TRP A NE1 1 ATOM 723 C CE2 . TRP A 1 93 ? 14.554 45.968 17.115 1.00 56.06 ? 93 TRP A CE2 1 ATOM 724 C CE3 . TRP A 1 93 ? 12.731 47.554 17.139 1.00 48.89 ? 93 TRP A CE3 1 ATOM 725 C CZ2 . TRP A 1 93 ? 13.680 44.896 16.947 1.00 58.26 ? 93 TRP A CZ2 1 ATOM 726 C CZ3 . TRP A 1 93 ? 11.866 46.489 16.973 1.00 45.99 ? 93 TRP A CZ3 1 ATOM 727 C CH2 . TRP A 1 93 ? 12.343 45.176 16.879 1.00 48.19 ? 93 TRP A CH2 1 ATOM 728 N N . PHE A 1 94 ? 16.089 52.578 15.425 1.00 65.57 ? 94 PHE A N 1 ATOM 729 C CA . PHE A 1 94 ? 15.565 53.912 15.164 1.00 73.10 ? 94 PHE A CA 1 ATOM 730 C C . PHE A 1 94 ? 14.384 53.846 14.207 1.00 75.23 ? 94 PHE A C 1 ATOM 731 O O . PHE A 1 94 ? 14.496 53.320 13.099 1.00 81.28 ? 94 PHE A O 1 ATOM 732 C CB . PHE A 1 94 ? 16.647 54.831 14.600 1.00 67.72 ? 94 PHE A CB 1 ATOM 733 C CG . PHE A 1 94 ? 16.120 56.150 14.115 1.00 58.75 ? 94 PHE A CG 1 ATOM 734 C CD1 . PHE A 1 94 ? 15.708 57.119 15.015 1.00 51.84 ? 94 PHE A CD1 1 ATOM 735 C CD2 . PHE A 1 94 ? 16.028 56.418 12.759 1.00 60.19 ? 94 PHE A CD2 1 ATOM 736 C CE1 . PHE A 1 94 ? 15.219 58.332 14.572 1.00 61.02 ? 94 PHE A CE1 1 ATOM 737 C CE2 . PHE A 1 94 ? 15.538 57.629 12.310 1.00 55.01 ? 94 PHE A CE2 1 ATOM 738 C CZ . PHE A 1 94 ? 15.134 58.587 13.218 1.00 58.66 ? 94 PHE A CZ 1 ATOM 739 N N . GLY A 1 95 ? 13.254 54.395 14.639 1.00 63.10 ? 95 GLY A N 1 ATOM 740 C CA . GLY A 1 95 ? 12.030 54.324 13.866 1.00 64.96 ? 95 GLY A CA 1 ATOM 741 C C . GLY A 1 95 ? 11.056 53.330 14.464 1.00 57.81 ? 95 GLY A C 1 ATOM 742 O O . GLY A 1 95 ? 9.976 53.097 13.919 1.00 55.17 ? 95 GLY A O 1 ATOM 743 N N . ALA A 1 96 ? 11.442 52.740 15.592 1.00 51.34 ? 96 ALA A N 1 ATOM 744 C CA . ALA A 1 96 ? 10.586 51.795 16.299 1.00 51.08 ? 96 ALA A CA 1 ATOM 745 C C . ALA A 1 96 ? 9.311 52.477 16.784 1.00 59.31 ? 96 ALA A C 1 ATOM 746 O O . ALA A 1 96 ? 8.277 51.832 16.957 1.00 92.43 ? 96 ALA A O 1 ATOM 747 C CB . ALA A 1 96 ? 11.333 51.171 17.467 1.00 59.00 ? 96 ALA A CB 1 ATOM 748 N N . SER A 1 97 ? 9.396 53.784 17.010 1.00 42.23 ? 97 SER A N 1 ATOM 749 C CA . SER A 1 97 ? 8.230 54.584 17.361 1.00 51.70 ? 97 SER A CA 1 ATOM 750 C C . SER A 1 97 ? 8.237 55.898 16.586 1.00 51.99 ? 97 SER A C 1 ATOM 751 O O . SER A 1 97 ? 9.193 56.670 16.666 1.00 62.82 ? 97 SER A O 1 ATOM 752 C CB . SER A 1 97 ? 8.190 54.855 18.867 1.00 61.85 ? 97 SER A CB 1 ATOM 753 O OG . SER A 1 97 ? 9.305 55.626 19.278 1.00 74.50 ? 97 SER A OG 1 ATOM 754 N N . VAL A 1 98 ? 7.169 56.147 15.834 1.00 49.19 ? 98 VAL A N 1 ATOM 755 C CA . VAL A 1 98 ? 7.072 57.347 15.009 1.00 45.86 ? 98 VAL A CA 1 ATOM 756 C C . VAL A 1 98 ? 5.741 58.064 15.211 1.00 50.54 ? 98 VAL A C 1 ATOM 757 O O . VAL A 1 98 ? 4.675 57.471 15.046 1.00 58.17 ? 98 VAL A O 1 ATOM 758 C CB . VAL A 1 98 ? 7.234 57.015 13.512 1.00 47.74 ? 98 VAL A CB 1 ATOM 759 C CG1 . VAL A 1 98 ? 7.017 58.259 12.664 1.00 49.95 ? 98 VAL A CG1 1 ATOM 760 C CG2 . VAL A 1 98 ? 8.604 56.413 13.244 1.00 81.67 ? 98 VAL A CG2 1 ATOM 761 N N . ARG A 1 99 ? 5.810 59.341 15.572 1.00 47.62 ? 99 ARG A N 1 ATOM 762 C CA . ARG A 1 99 ? 4.613 60.155 15.748 1.00 50.54 ? 99 ARG A CA 1 ATOM 763 C C . ARG A 1 99 ? 4.788 61.503 15.058 1.00 51.49 ? 99 ARG A C 1 ATOM 764 O O . ARG A 1 99 ? 5.892 62.044 15.009 1.00 57.14 ? 99 ARG A O 1 ATOM 765 C CB . ARG A 1 99 ? 4.307 60.353 17.234 1.00 58.27 ? 99 ARG A CB 1 ATOM 766 C CG . ARG A 1 99 ? 2.883 60.805 17.524 1.00 72.53 ? 99 ARG A CG 1 ATOM 767 C CD . ARG A 1 99 ? 2.019 59.650 18.009 1.00 84.64 ? 99 ARG A CD 1 ATOM 768 N NE . ARG A 1 99 ? 1.940 58.562 17.038 1.00 100.91 ? 99 ARG A NE 1 ATOM 769 C CZ . ARG A 1 99 ? 1.281 57.427 17.243 1.00 106.69 ? 99 ARG A CZ 1 ATOM 770 N NH1 . ARG A 1 99 ? 0.642 57.227 18.388 1.00 108.27 ? 99 ARG A NH1 1 ATOM 771 N NH2 . ARG A 1 99 ? 1.260 56.490 16.305 1.00 101.48 ? 99 ARG A NH2 1 ATOM 772 N N . SER A 1 100 ? 3.697 62.042 14.523 1.00 52.56 ? 100 SER A N 1 ATOM 773 C CA . SER A 1 100 ? 3.755 63.305 13.797 1.00 55.33 ? 100 SER A CA 1 ATOM 774 C C . SER A 1 100 ? 2.585 64.223 14.127 1.00 65.55 ? 100 SER A C 1 ATOM 775 O O . SER A 1 100 ? 1.424 63.826 14.032 1.00 99.71 ? 100 SER A O 1 ATOM 776 C CB . SER A 1 100 ? 3.794 63.048 12.290 1.00 59.90 ? 100 SER A CB 1 ATOM 777 O OG . SER A 1 100 ? 3.554 64.240 11.564 1.00 88.77 ? 100 SER A OG 1 ATOM 778 N N . LYS A 1 101 ? 2.901 65.455 14.511 1.00 58.77 ? 101 LYS A N 1 ATOM 779 C CA . LYS A 1 101 ? 1.884 66.479 14.711 1.00 69.90 ? 101 LYS A CA 1 ATOM 780 C C . LYS A 1 101 ? 2.153 67.663 13.792 1.00 76.01 ? 101 LYS A C 1 ATOM 781 O O . LYS A 1 101 ? 3.184 68.328 13.914 1.00 73.45 ? 101 LYS A O 1 ATOM 782 C CB . LYS A 1 101 ? 1.844 66.942 16.168 1.00 81.19 ? 101 LYS A CB 1 ATOM 783 C CG . LYS A 1 101 ? 0.873 68.089 16.409 1.00 92.48 ? 101 LYS A CG 1 ATOM 784 C CD . LYS A 1 101 ? 0.872 68.537 17.859 1.00 86.95 ? 101 LYS A CD 1 ATOM 785 C CE . LYS A 1 101 ? -0.071 69.712 18.064 1.00 89.56 ? 101 LYS A CE 1 ATOM 786 N NZ . LYS A 1 101 ? -1.461 69.388 17.639 1.00 104.20 ? 101 LYS A NZ 1 ATOM 787 N N . GLN A 1 102 ? 1.221 67.913 12.876 1.00 81.05 ? 102 GLN A N 1 ATOM 788 C CA . GLN A 1 102 ? 1.347 68.990 11.899 1.00 78.93 ? 102 GLN A CA 1 ATOM 789 C C . GLN A 1 102 ? 2.641 68.859 11.097 1.00 78.94 ? 102 GLN A C 1 ATOM 790 O O . GLN A 1 102 ? 2.854 67.859 10.412 1.00 92.77 ? 102 GLN A O 1 ATOM 791 C CB . GLN A 1 102 ? 1.273 70.353 12.594 1.00 78.66 ? 102 GLN A CB 1 ATOM 792 C CG . GLN A 1 102 ? -0.070 70.627 13.255 1.00 88.93 ? 102 GLN A CG 1 ATOM 793 C CD . GLN A 1 102 ? -0.022 71.789 14.228 1.00 118.74 ? 102 GLN A CD 1 ATOM 794 O OE1 . GLN A 1 102 ? 0.872 71.872 15.071 1.00 134.80 ? 102 GLN A OE1 1 ATOM 795 N NE2 . GLN A 1 102 ? -0.987 72.695 14.117 1.00 126.18 ? 102 GLN A NE2 1 ATOM 796 N N . ASP A 1 103 ? 3.502 69.866 11.186 1.00 72.91 ? 103 ASP A N 1 ATOM 797 C CA . ASP A 1 103 ? 4.750 69.867 10.432 1.00 74.13 ? 103 ASP A CA 1 ATOM 798 C C . ASP A 1 103 ? 5.892 69.238 11.234 1.00 67.63 ? 103 ASP A C 1 ATOM 799 O O . ASP A 1 103 ? 6.991 69.040 10.716 1.00 68.14 ? 103 ASP A O 1 ATOM 800 C CB . ASP A 1 103 ? 5.112 71.294 10.012 1.00 82.71 ? 103 ASP A CB 1 ATOM 801 C CG . ASP A 1 103 ? 5.815 71.350 8.667 1.00 100.92 ? 103 ASP A CG 1 ATOM 802 O OD1 . ASP A 1 103 ? 6.690 70.498 8.407 1.00 101.64 ? 103 ASP A OD1 1 ATOM 803 O OD2 . ASP A 1 103 ? 5.487 72.249 7.864 1.00 106.72 ? 103 ASP A OD2 1 ATOM 804 N N . LYS A 1 104 ? 5.624 68.921 12.498 1.00 65.05 ? 104 LYS A N 1 ATOM 805 C CA . LYS A 1 104 ? 6.626 68.307 13.365 1.00 62.60 ? 104 LYS A CA 1 ATOM 806 C C . LYS A 1 104 ? 6.554 66.784 13.300 1.00 87.75 ? 104 LYS A C 1 ATOM 807 O O . LYS A 1 104 ? 5.464 66.211 13.280 1.00 100.03 ? 104 LYS A O 1 ATOM 808 C CB . LYS A 1 104 ? 6.440 68.766 14.814 1.00 61.60 ? 104 LYS A CB 1 ATOM 809 C CG . LYS A 1 104 ? 6.229 70.262 14.990 1.00 69.43 ? 104 LYS A CG 1 ATOM 810 C CD . LYS A 1 104 ? 7.506 71.048 14.750 1.00 66.45 ? 104 LYS A CD 1 ATOM 811 C CE . LYS A 1 104 ? 7.270 72.540 14.929 1.00 69.62 ? 104 LYS A CE 1 ATOM 812 N NZ . LYS A 1 104 ? 8.482 73.343 14.608 1.00 71.98 ? 104 LYS A NZ 1 ATOM 813 N N . ILE A 1 105 ? 7.711 66.129 13.262 1.00 74.64 ? 105 ILE A N 1 ATOM 814 C CA . ILE A 1 105 ? 7.761 64.671 13.359 1.00 63.21 ? 105 ILE A CA 1 ATOM 815 C C . ILE A 1 105 ? 8.782 64.236 14.408 1.00 61.16 ? 105 ILE A C 1 ATOM 816 O O . ILE A 1 105 ? 9.814 64.883 14.593 1.00 74.62 ? 105 ILE A O 1 ATOM 817 C CB . ILE A 1 105 ? 8.100 64.003 12.005 1.00 65.04 ? 105 ILE A CB 1 ATOM 818 C CG1 . ILE A 1 105 ? 9.493 64.408 11.520 1.00 92.57 ? 105 ILE A CG1 1 ATOM 819 C CG2 . ILE A 1 105 ? 7.054 64.346 10.961 1.00 66.69 ? 105 ILE A CG2 1 ATOM 820 C CD1 . ILE A 1 105 ? 9.899 63.735 10.226 1.00 113.30 ? 105 ILE A CD1 1 ATOM 821 N N . LEU A 1 106 ? 8.479 63.144 15.101 1.00 56.17 ? 106 LEU A N 1 ATOM 822 C CA . LEU A 1 106 ? 9.350 62.645 16.157 1.00 52.05 ? 106 LEU A CA 1 ATOM 823 C C . LEU A 1 106 ? 9.590 61.145 16.028 1.00 55.59 ? 106 LEU A C 1 ATOM 824 O O . LEU A 1 106 ? 8.657 60.347 16.119 1.00 60.64 ? 106 LEU A O 1 ATOM 825 C CB . LEU A 1 106 ? 8.755 62.960 17.530 1.00 49.29 ? 106 LEU A CB 1 ATOM 826 C CG . LEU A 1 106 ? 9.538 62.429 18.731 1.00 47.71 ? 106 LEU A CG 1 ATOM 827 C CD1 . LEU A 1 106 ? 10.936 63.025 18.763 1.00 77.28 ? 106 LEU A CD1 1 ATOM 828 C CD2 . LEU A 1 106 ? 8.798 62.719 20.027 1.00 46.92 ? 106 LEU A CD2 1 ATOM 829 N N . ALA A 1 107 ? 10.847 60.769 15.820 1.00 54.18 ? 107 ALA A N 1 ATOM 830 C CA . ALA A 1 107 ? 11.223 59.365 15.712 1.00 51.56 ? 107 ALA A CA 1 ATOM 831 C C . ALA A 1 107 ? 12.253 59.018 16.779 1.00 51.27 ? 107 ALA A C 1 ATOM 832 O O . ALA A 1 107 ? 13.096 59.844 17.123 1.00 57.64 ? 107 ALA A O 1 ATOM 833 C CB . ALA A 1 107 ? 11.762 59.062 14.327 1.00 50.04 ? 107 ALA A CB 1 ATOM 834 N N . CYS A 1 108 ? 12.186 57.796 17.299 1.00 45.54 ? 108 CYS A N 1 ATOM 835 C CA . CYS A 1 108 ? 13.033 57.410 18.423 1.00 44.65 ? 108 CYS A CA 1 ATOM 836 C C . CYS A 1 108 ? 13.774 56.094 18.204 1.00 51.73 ? 108 CYS A C 1 ATOM 837 O O . CYS A 1 108 ? 13.345 55.243 17.424 1.00 53.43 ? 108 CYS A O 1 ATOM 838 C CB . CYS A 1 108 ? 12.194 57.316 19.698 1.00 42.93 ? 108 CYS A CB 1 ATOM 839 S SG . CYS A 1 108 ? 11.311 58.835 20.119 1.00 66.32 ? 108 CYS A SG 1 ATOM 840 N N . ALA A 1 109 ? 14.892 55.942 18.908 1.00 57.14 ? 109 ALA A N 1 ATOM 841 C CA . ALA A 1 109 ? 15.691 54.723 18.865 1.00 57.20 ? 109 ALA A CA 1 ATOM 842 C C . ALA A 1 109 ? 15.829 54.139 20.267 1.00 56.07 ? 109 ALA A C 1 ATOM 843 O O . ALA A 1 109 ? 16.811 54.404 20.959 1.00 63.24 ? 109 ALA A O 1 ATOM 844 C CB . ALA A 1 109 ? 17.059 55.004 18.268 1.00 48.30 ? 109 ALA A CB 1 ATOM 845 N N . PRO A 1 110 ? 14.840 53.339 20.690 1.00 44.29 ? 110 PRO A N 1 ATOM 846 C CA . PRO A 1 110 ? 14.774 52.805 22.056 1.00 42.97 ? 110 PRO A CA 1 ATOM 847 C C . PRO A 1 110 ? 15.971 51.937 22.444 1.00 57.19 ? 110 PRO A C 1 ATOM 848 O O . PRO A 1 110 ? 16.265 51.818 23.632 1.00 79.22 ? 110 PRO A O 1 ATOM 849 C CB . PRO A 1 110 ? 13.487 51.970 22.041 1.00 40.88 ? 110 PRO A CB 1 ATOM 850 C CG . PRO A 1 110 ? 12.676 52.541 20.927 1.00 54.99 ? 110 PRO A CG 1 ATOM 851 C CD . PRO A 1 110 ? 13.672 52.940 19.887 1.00 41.64 ? 110 PRO A CD 1 ATOM 852 N N . LEU A 1 111 ? 16.643 51.336 21.468 1.00 50.46 ? 111 LEU A N 1 ATOM 853 C CA . LEU A 1 111 ? 17.778 50.461 21.759 1.00 44.18 ? 111 LEU A CA 1 ATOM 854 C C . LEU A 1 111 ? 19.131 51.169 21.652 1.00 45.52 ? 111 LEU A C 1 ATOM 855 O O . LEU A 1 111 ? 20.179 50.533 21.755 1.00 46.81 ? 111 LEU A O 1 ATOM 856 C CB . LEU A 1 111 ? 17.750 49.233 20.848 1.00 44.66 ? 111 LEU A CB 1 ATOM 857 C CG . LEU A 1 111 ? 17.151 47.996 21.529 1.00 60.15 ? 111 LEU A CG 1 ATOM 858 C CD1 . LEU A 1 111 ? 15.711 48.245 21.957 1.00 41.89 ? 111 LEU A CD1 1 ATOM 859 C CD2 . LEU A 1 111 ? 17.242 46.768 20.637 1.00 77.56 ? 111 LEU A CD2 1 ATOM 860 N N . TYR A 1 112 ? 19.100 52.478 21.424 1.00 45.74 ? 112 TYR A N 1 ATOM 861 C CA . TYR A 1 112 ? 20.309 53.302 21.413 1.00 47.41 ? 112 TYR A CA 1 ATOM 862 C C . TYR A 1 112 ? 21.076 53.187 22.733 1.00 47.94 ? 112 TYR A C 1 ATOM 863 O O . TYR A 1 112 ? 20.481 53.260 23.806 1.00 46.46 ? 112 TYR A O 1 ATOM 864 C CB . TYR A 1 112 ? 19.930 54.759 21.126 1.00 47.55 ? 112 TYR A CB 1 ATOM 865 C CG . TYR A 1 112 ? 20.986 55.791 21.448 1.00 49.10 ? 112 TYR A CG 1 ATOM 866 C CD1 . TYR A 1 112 ? 21.948 56.146 20.511 1.00 81.80 ? 112 TYR A CD1 1 ATOM 867 C CD2 . TYR A 1 112 ? 20.997 56.439 22.676 1.00 48.67 ? 112 TYR A CD2 1 ATOM 868 C CE1 . TYR A 1 112 ? 22.905 57.101 20.799 1.00 52.94 ? 112 TYR A CE1 1 ATOM 869 C CE2 . TYR A 1 112 ? 21.950 57.391 22.973 1.00 72.52 ? 112 TYR A CE2 1 ATOM 870 C CZ . TYR A 1 112 ? 22.901 57.720 22.032 1.00 52.42 ? 112 TYR A CZ 1 ATOM 871 O OH . TYR A 1 112 ? 23.846 58.672 22.333 1.00 54.29 ? 112 TYR A OH 1 ATOM 872 N N . HIS A 1 113 ? 22.396 53.023 22.649 1.00 51.93 ? 113 HIS A N 1 ATOM 873 C CA . HIS A 1 113 ? 23.231 52.787 23.831 1.00 70.85 ? 113 HIS A CA 1 ATOM 874 C C . HIS A 1 113 ? 24.255 53.904 24.046 1.00 51.71 ? 113 HIS A C 1 ATOM 875 O O . HIS A 1 113 ? 24.573 54.642 23.115 1.00 52.89 ? 113 HIS A O 1 ATOM 876 C CB . HIS A 1 113 ? 23.940 51.436 23.719 1.00 80.67 ? 113 HIS A CB 1 ATOM 877 C CG . HIS A 1 113 ? 23.070 50.267 24.061 1.00 63.29 ? 113 HIS A CG 1 ATOM 878 N ND1 . HIS A 1 113 ? 22.120 49.765 23.197 1.00 59.18 ? 113 HIS A ND1 1 ATOM 879 C CD2 . HIS A 1 113 ? 23.004 49.504 25.177 1.00 57.90 ? 113 HIS A CD2 1 ATOM 880 C CE1 . HIS A 1 113 ? 21.509 48.741 23.765 1.00 64.71 ? 113 HIS A CE1 1 ATOM 881 N NE2 . HIS A 1 113 ? 22.026 48.562 24.967 1.00 64.82 ? 113 HIS A NE2 1 ATOM 882 N N . TRP A 1 114 ? 24.772 54.023 25.269 1.00 52.11 ? 114 TRP A N 1 ATOM 883 C CA . TRP A 1 114 ? 25.492 55.239 25.656 1.00 59.52 ? 114 TRP A CA 1 ATOM 884 C C . TRP A 1 114 ? 26.969 55.102 26.077 1.00 68.92 ? 114 TRP A C 1 ATOM 885 O O . TRP A 1 114 ? 27.824 55.663 25.398 1.00 79.30 ? 114 TRP A O 1 ATOM 886 C CB . TRP A 1 114 ? 24.726 55.936 26.781 1.00 57.74 ? 114 TRP A CB 1 ATOM 887 C CG . TRP A 1 114 ? 25.151 57.355 26.975 1.00 67.83 ? 114 TRP A CG 1 ATOM 888 C CD1 . TRP A 1 114 ? 25.953 58.091 26.149 1.00 81.11 ? 114 TRP A CD1 1 ATOM 889 C CD2 . TRP A 1 114 ? 24.803 58.213 28.063 1.00 83.17 ? 114 TRP A CD2 1 ATOM 890 N NE1 . TRP A 1 114 ? 26.128 59.352 26.659 1.00 86.21 ? 114 TRP A NE1 1 ATOM 891 C CE2 . TRP A 1 114 ? 25.432 59.454 27.834 1.00 88.12 ? 114 TRP A CE2 1 ATOM 892 C CE3 . TRP A 1 114 ? 24.024 58.053 29.212 1.00 96.89 ? 114 TRP A CE3 1 ATOM 893 C CZ2 . TRP A 1 114 ? 25.307 60.527 28.711 1.00 94.88 ? 114 TRP A CZ2 1 ATOM 894 C CZ3 . TRP A 1 114 ? 23.900 59.117 30.077 1.00 111.39 ? 114 TRP A CZ3 1 ATOM 895 C CH2 . TRP A 1 114 ? 24.536 60.340 29.823 1.00 106.21 ? 114 TRP A CH2 1 ATOM 896 N N . ARG A 1 115 ? 27.242 54.399 27.186 1.00 68.29 ? 115 ARG A N 1 ATOM 897 C CA . ARG A 1 115 ? 28.560 54.337 27.877 1.00 75.68 ? 115 ARG A CA 1 ATOM 898 C C . ARG A 1 115 ? 28.723 55.505 28.858 1.00 68.67 ? 115 ARG A C 1 ATOM 899 O O . ARG A 1 115 ? 29.626 55.524 29.696 1.00 66.97 ? 115 ARG A O 1 ATOM 900 C CB . ARG A 1 115 ? 29.735 54.320 26.877 1.00 88.91 ? 115 ARG A CB 1 ATOM 901 C CG . ARG A 1 115 ? 31.135 54.242 27.478 1.00 92.86 ? 115 ARG A CG 1 ATOM 902 C CD . ARG A 1 115 ? 32.011 55.386 26.981 1.00 73.17 ? 115 ARG A CD 1 ATOM 903 N NE . ARG A 1 115 ? 33.379 55.300 27.488 1.00 72.26 ? 115 ARG A NE 1 ATOM 904 C CZ . ARG A 1 115 ? 33.810 55.913 28.586 1.00 71.96 ? 115 ARG A CZ 1 ATOM 905 N NH1 . ARG A 1 115 ? 32.982 56.662 29.301 1.00 87.69 ? 115 ARG A NH1 1 ATOM 906 N NH2 . ARG A 1 115 ? 35.072 55.778 28.970 1.00 72.94 ? 115 ARG A NH2 1 ATOM 907 N N . THR A 1 116 ? 27.801 56.452 28.760 1.00 78.78 ? 116 THR A N 1 ATOM 908 C CA . THR A 1 116 ? 27.812 57.712 29.502 1.00 95.67 ? 116 THR A CA 1 ATOM 909 C C . THR A 1 116 ? 29.131 58.478 29.399 1.00 94.93 ? 116 THR A C 1 ATOM 910 O O . THR A 1 116 ? 29.860 58.347 28.416 1.00 110.80 ? 116 THR A O 1 ATOM 911 C CB . THR A 1 116 ? 27.516 57.472 31.000 1.00 90.08 ? 116 THR A CB 1 ATOM 912 O OG1 . THR A 1 116 ? 28.691 56.966 31.646 1.00 76.26 ? 116 THR A OG1 1 ATOM 913 C CG2 . THR A 1 116 ? 26.380 56.473 31.173 1.00 77.83 ? 116 THR A CG2 1 ATOM 914 N N . GLU A 1 117 ? 29.437 59.272 30.424 1.00 73.82 ? 117 GLU A N 1 ATOM 915 C CA . GLU A 1 117 ? 30.706 59.994 30.490 1.00 74.02 ? 117 GLU A CA 1 ATOM 916 C C . GLU A 1 117 ? 31.699 59.505 31.547 1.00 83.31 ? 117 GLU A C 1 ATOM 917 O O . GLU A 1 117 ? 32.815 60.017 31.630 1.00 89.23 ? 117 GLU A O 1 ATOM 918 C CB . GLU A 1 117 ? 30.434 61.485 30.684 1.00 75.45 ? 117 GLU A CB 1 ATOM 919 C CG . GLU A 1 117 ? 30.576 62.274 29.391 1.00 77.59 ? 117 GLU A CG 1 ATOM 920 C CD . GLU A 1 117 ? 29.611 63.435 29.295 1.00 99.05 ? 117 GLU A CD 1 ATOM 921 O OE1 . GLU A 1 117 ? 28.620 63.452 30.054 1.00 110.63 ? 117 GLU A OE1 1 ATOM 922 O OE2 . GLU A 1 117 ? 29.845 64.331 28.457 1.00 100.70 ? 117 GLU A OE2 1 ATOM 923 N N . MET A 1 118 ? 31.303 58.528 32.355 1.00 81.97 ? 118 MET A N 1 ATOM 924 C CA . MET A 1 118 ? 32.089 58.190 33.539 1.00 77.28 ? 118 MET A CA 1 ATOM 925 C C . MET A 1 118 ? 32.963 56.962 33.333 1.00 86.36 ? 118 MET A C 1 ATOM 926 O O . MET A 1 118 ? 34.178 57.076 33.171 1.00 93.41 ? 118 MET A O 1 ATOM 927 C CB . MET A 1 118 ? 31.165 57.977 34.741 1.00 68.53 ? 118 MET A CB 1 ATOM 928 C CG . MET A 1 118 ? 30.702 59.270 35.398 1.00 76.01 ? 118 MET A CG 1 ATOM 929 S SD . MET A 1 118 ? 28.923 59.338 35.686 1.00 82.52 ? 118 MET A SD 1 ATOM 930 C CE . MET A 1 118 ? 28.313 59.443 34.006 1.00 99.78 ? 118 MET A CE 1 ATOM 931 N N . LYS A 1 119 ? 32.343 55.790 33.331 1.00 68.08 ? 119 LYS A N 1 ATOM 932 C CA . LYS A 1 119 ? 33.070 54.551 33.102 1.00 70.51 ? 119 LYS A CA 1 ATOM 933 C C . LYS A 1 119 ? 32.587 53.906 31.815 1.00 72.53 ? 119 LYS A C 1 ATOM 934 O O . LYS A 1 119 ? 31.461 54.147 31.382 1.00 90.60 ? 119 LYS A O 1 ATOM 935 C CB . LYS A 1 119 ? 32.899 53.593 34.282 1.00 71.65 ? 119 LYS A CB 1 ATOM 936 C CG . LYS A 1 119 ? 31.456 53.380 34.707 1.00 81.62 ? 119 LYS A CG 1 ATOM 937 C CD . LYS A 1 119 ? 31.366 52.425 35.887 1.00 96.81 ? 119 LYS A CD 1 ATOM 938 C CE . LYS A 1 119 ? 29.952 52.358 36.442 1.00 92.54 ? 119 LYS A CE 1 ATOM 939 N NZ . LYS A 1 119 ? 28.970 51.906 35.419 1.00 76.16 ? 119 LYS A NZ 1 ATOM 940 N N . GLN A 1 120 ? 33.446 53.101 31.196 1.00 72.50 ? 120 GLN A N 1 ATOM 941 C CA . GLN A 1 120 ? 33.069 52.388 29.984 1.00 72.35 ? 120 GLN A CA 1 ATOM 942 C C . GLN A 1 120 ? 31.874 51.491 30.276 1.00 70.65 ? 120 GLN A C 1 ATOM 943 O O . GLN A 1 120 ? 31.791 50.890 31.347 1.00 78.89 ? 120 GLN A O 1 ATOM 944 C CB . GLN A 1 120 ? 34.243 51.574 29.439 1.00 77.31 ? 120 GLN A CB 1 ATOM 945 C CG . GLN A 1 120 ? 33.967 50.915 28.097 1.00 88.15 ? 120 GLN A CG 1 ATOM 946 C CD . GLN A 1 120 ? 35.233 50.469 27.394 1.00 113.17 ? 120 GLN A CD 1 ATOM 947 O OE1 . GLN A 1 120 ? 36.312 51.015 27.626 1.00 115.93 ? 120 GLN A OE1 1 ATOM 948 N NE2 . GLN A 1 120 ? 35.108 49.470 26.527 1.00 122.81 ? 120 GLN A NE2 1 ATOM 949 N N . GLU A 1 121 ? 30.958 51.405 29.317 1.00 69.26 ? 121 GLU A N 1 ATOM 950 C CA . GLU A 1 121 ? 29.675 50.742 29.516 1.00 74.30 ? 121 GLU A CA 1 ATOM 951 C C . GLU A 1 121 ? 28.897 50.752 28.207 1.00 74.18 ? 121 GLU A C 1 ATOM 952 O O . GLU A 1 121 ? 29.329 51.358 27.232 1.00 82.24 ? 121 GLU A O 1 ATOM 953 C CB . GLU A 1 121 ? 28.867 51.447 30.614 1.00 72.48 ? 121 GLU A CB 1 ATOM 954 C CG . GLU A 1 121 ? 27.826 50.581 31.306 1.00 93.45 ? 121 GLU A CG 1 ATOM 955 C CD . GLU A 1 121 ? 28.425 49.694 32.380 1.00 118.24 ? 121 GLU A CD 1 ATOM 956 O OE1 . GLU A 1 121 ? 27.781 48.691 32.752 1.00 126.92 ? 121 GLU A OE1 1 ATOM 957 O OE2 . GLU A 1 121 ? 29.536 50.005 32.857 1.00 124.29 ? 121 GLU A OE2 1 ATOM 958 N N . ARG A 1 122 ? 27.781 50.035 28.163 1.00 61.01 ? 122 ARG A N 1 ATOM 959 C CA . ARG A 1 122 ? 26.775 50.277 27.138 1.00 57.22 ? 122 ARG A CA 1 ATOM 960 C C . ARG A 1 122 ? 25.412 50.311 27.812 1.00 69.73 ? 122 ARG A C 1 ATOM 961 O O . ARG A 1 122 ? 24.926 49.288 28.295 1.00 99.20 ? 122 ARG A O 1 ATOM 962 C CB . ARG A 1 122 ? 26.821 49.203 26.050 1.00 57.84 ? 122 ARG A CB 1 ATOM 963 C CG . ARG A 1 122 ? 28.142 49.129 25.299 1.00 61.57 ? 122 ARG A CG 1 ATOM 964 C CD . ARG A 1 122 ? 28.213 47.891 24.422 1.00 71.78 ? 122 ARG A CD 1 ATOM 965 N NE . ARG A 1 122 ? 27.295 47.960 23.288 1.00 72.59 ? 122 ARG A NE 1 ATOM 966 C CZ . ARG A 1 122 ? 27.674 48.185 22.035 1.00 69.05 ? 122 ARG A CZ 1 ATOM 967 N NH1 . ARG A 1 122 ? 28.958 48.358 21.750 1.00 63.97 ? 122 ARG A NH1 1 ATOM 968 N NH2 . ARG A 1 122 ? 26.771 48.230 21.064 1.00 70.01 ? 122 ARG A NH2 1 ATOM 969 N N . GLU A 1 123 ? 24.794 51.485 27.844 1.00 63.20 ? 123 GLU A N 1 ATOM 970 C CA . GLU A 1 123 ? 23.505 51.639 28.506 1.00 58.72 ? 123 GLU A CA 1 ATOM 971 C C . GLU A 1 123 ? 22.418 52.098 27.545 1.00 56.03 ? 123 GLU A C 1 ATOM 972 O O . GLU A 1 123 ? 22.497 53.192 26.987 1.00 57.29 ? 123 GLU A O 1 ATOM 973 C CB . GLU A 1 123 ? 23.627 52.603 29.685 1.00 51.89 ? 123 GLU A CB 1 ATOM 974 C CG . GLU A 1 123 ? 24.466 52.032 30.817 1.00 55.00 ? 123 GLU A CG 1 ATOM 975 C CD . GLU A 1 123 ? 24.526 52.935 32.029 1.00 70.04 ? 123 GLU A CD 1 ATOM 976 O OE1 . GLU A 1 123 ? 25.280 52.606 32.969 1.00 58.05 ? 123 GLU A OE1 1 ATOM 977 O OE2 . GLU A 1 123 ? 23.826 53.968 32.044 1.00 88.74 ? 123 GLU A OE2 1 ATOM 978 N N . PRO A 1 124 ? 21.395 51.255 27.352 1.00 50.38 ? 124 PRO A N 1 ATOM 979 C CA . PRO A 1 124 ? 20.284 51.568 26.450 1.00 51.61 ? 124 PRO A CA 1 ATOM 980 C C . PRO A 1 124 ? 19.411 52.706 26.974 1.00 60.63 ? 124 PRO A C 1 ATOM 981 O O . PRO A 1 124 ? 18.268 52.467 27.357 1.00 56.01 ? 124 PRO A O 1 ATOM 982 C CB . PRO A 1 124 ? 19.498 50.257 26.400 1.00 43.97 ? 124 PRO A CB 1 ATOM 983 C CG . PRO A 1 124 ? 19.779 49.611 27.708 1.00 44.27 ? 124 PRO A CG 1 ATOM 984 C CD . PRO A 1 124 ? 21.199 49.970 28.045 1.00 46.92 ? 124 PRO A CD 1 ATOM 985 N N . VAL A 1 125 ? 19.947 53.923 26.999 1.00 44.96 ? 125 VAL A N 1 ATOM 986 C CA . VAL A 1 125 ? 19.165 55.079 27.417 1.00 44.51 ? 125 VAL A CA 1 ATOM 987 C C . VAL A 1 125 ? 18.100 55.399 26.377 1.00 46.52 ? 125 VAL A C 1 ATOM 988 O O . VAL A 1 125 ? 17.019 55.885 26.709 1.00 47.54 ? 125 VAL A O 1 ATOM 989 C CB . VAL A 1 125 ? 20.047 56.330 27.641 1.00 46.18 ? 125 VAL A CB 1 ATOM 990 C CG1 . VAL A 1 125 ? 20.907 56.168 28.881 1.00 64.09 ? 125 VAL A CG1 1 ATOM 991 C CG2 . VAL A 1 125 ? 20.910 56.613 26.420 1.00 74.81 ? 125 VAL A CG2 1 ATOM 992 N N . GLY A 1 126 ? 18.411 55.113 25.117 1.00 43.96 ? 126 GLY A N 1 ATOM 993 C CA . GLY A 1 126 ? 17.531 55.454 24.018 1.00 45.39 ? 126 GLY A CA 1 ATOM 994 C C . GLY A 1 126 ? 17.642 56.924 23.669 1.00 48.70 ? 126 GLY A C 1 ATOM 995 O O . GLY A 1 126 ? 18.110 57.730 24.474 1.00 56.12 ? 126 GLY A O 1 ATOM 996 N N . THR A 1 127 ? 17.210 57.278 22.465 1.00 50.93 ? 127 THR A N 1 ATOM 997 C CA . THR A 1 127 ? 17.249 58.663 22.020 1.00 46.30 ? 127 THR A CA 1 ATOM 998 C C . THR A 1 127 ? 16.206 58.900 20.941 1.00 54.22 ? 127 THR A C 1 ATOM 999 O O . THR A 1 127 ? 15.712 57.955 20.326 1.00 50.95 ? 127 THR A O 1 ATOM 1000 C CB . THR A 1 127 ? 18.636 59.051 21.474 1.00 67.92 ? 127 THR A CB 1 ATOM 1001 O OG1 . THR A 1 127 ? 18.664 60.455 21.188 1.00 68.12 ? 127 THR A OG1 1 ATOM 1002 C CG2 . THR A 1 127 ? 18.946 58.272 20.203 1.00 49.02 ? 127 THR A CG2 1 ATOM 1003 N N . CYS A 1 128 ? 15.867 60.163 20.716 1.00 47.23 ? 128 CYS A N 1 ATOM 1004 C CA . CYS A 1 128 ? 14.918 60.503 19.668 1.00 47.59 ? 128 CYS A CA 1 ATOM 1005 C C . CYS A 1 128 ? 15.444 61.628 18.793 1.00 75.22 ? 128 CYS A C 1 ATOM 1006 O O . CYS A 1 128 ? 16.513 62.182 19.047 1.00 97.00 ? 128 CYS A O 1 ATOM 1007 C CB . CYS A 1 128 ? 13.572 60.898 20.274 1.00 46.60 ? 128 CYS A CB 1 ATOM 1008 S SG . CYS A 1 128 ? 12.803 59.602 21.262 1.00 84.41 ? 128 CYS A SG 1 ATOM 1009 N N . PHE A 1 129 ? 14.684 61.957 17.756 1.00 62.35 ? 129 PHE A N 1 ATOM 1010 C CA . PHE A 1 129 ? 15.015 63.075 16.888 1.00 56.18 ? 129 PHE A CA 1 ATOM 1011 C C . PHE A 1 129 ? 13.754 63.825 16.486 1.00 53.81 ? 129 PHE A C 1 ATOM 1012 O O . PHE A 1 129 ? 12.795 63.228 15.998 1.00 52.99 ? 129 PHE A O 1 ATOM 1013 C CB . PHE A 1 129 ? 15.770 62.593 15.647 1.00 55.82 ? 129 PHE A CB 1 ATOM 1014 C CG . PHE A 1 129 ? 17.192 62.189 15.921 1.00 61.58 ? 129 PHE A CG 1 ATOM 1015 C CD1 . PHE A 1 129 ? 17.501 60.888 16.280 1.00 60.98 ? 129 PHE A CD1 1 ATOM 1016 C CD2 . PHE A 1 129 ? 18.219 63.113 15.819 1.00 57.52 ? 129 PHE A CD2 1 ATOM 1017 C CE1 . PHE A 1 129 ? 18.808 60.515 16.533 1.00 56.98 ? 129 PHE A CE1 1 ATOM 1018 C CE2 . PHE A 1 129 ? 19.527 62.747 16.070 1.00 58.21 ? 129 PHE A CE2 1 ATOM 1019 C CZ . PHE A 1 129 ? 19.822 61.446 16.428 1.00 56.86 ? 129 PHE A CZ 1 ATOM 1020 N N . LEU A 1 130 ? 13.760 65.135 16.698 1.00 64.13 ? 130 LEU A N 1 ATOM 1021 C CA . LEU A 1 130 ? 12.647 65.979 16.288 1.00 64.49 ? 130 LEU A CA 1 ATOM 1022 C C . LEU A 1 130 ? 13.100 66.866 15.137 1.00 76.23 ? 130 LEU A C 1 ATOM 1023 O O . LEU A 1 130 ? 14.136 67.526 15.220 1.00 95.51 ? 130 LEU A O 1 ATOM 1024 C CB . LEU A 1 130 ? 12.138 66.822 17.461 1.00 56.46 ? 130 LEU A CB 1 ATOM 1025 C CG . LEU A 1 130 ? 10.649 67.189 17.505 1.00 56.45 ? 130 LEU A CG 1 ATOM 1026 C CD1 . LEU A 1 130 ? 10.310 67.852 18.831 1.00 56.39 ? 130 LEU A CD1 1 ATOM 1027 C CD2 . LEU A 1 130 ? 10.244 68.089 16.345 1.00 61.40 ? 130 LEU A CD2 1 ATOM 1028 N N . GLN A 1 131 ? 12.323 66.872 14.061 1.00 60.66 ? 131 GLN A N 1 ATOM 1029 C CA . GLN A 1 131 ? 12.674 67.636 12.873 1.00 82.05 ? 131 GLN A CA 1 ATOM 1030 C C . GLN A 1 131 ? 11.474 68.376 12.305 1.00 73.46 ? 131 GLN A C 1 ATOM 1031 O O . GLN A 1 131 ? 10.439 67.765 12.038 1.00 70.10 ? 131 GLN A O 1 ATOM 1032 C CB . GLN A 1 131 ? 13.261 66.712 11.803 1.00 84.92 ? 131 GLN A CB 1 ATOM 1033 C CG . GLN A 1 131 ? 13.282 67.315 10.407 1.00 90.46 ? 131 GLN A CG 1 ATOM 1034 C CD . GLN A 1 131 ? 13.629 66.299 9.337 1.00 87.46 ? 131 GLN A CD 1 ATOM 1035 O OE1 . GLN A 1 131 ? 14.109 65.205 9.636 1.00 77.98 ? 131 GLN A OE1 1 ATOM 1036 N NE2 . GLN A 1 131 ? 13.382 66.653 8.081 1.00 101.40 ? 131 GLN A NE2 1 ATOM 1037 N N . ASP A 1 132 ? 11.597 69.688 12.125 1.00 75.91 ? 132 ASP A N 1 ATOM 1038 C CA . ASP A 1 132 ? 10.580 70.394 11.362 1.00 82.12 ? 132 ASP A CA 1 ATOM 1039 C C . ASP A 1 132 ? 11.149 70.950 10.061 1.00 85.99 ? 132 ASP A C 1 ATOM 1040 O O . ASP A 1 132 ? 11.770 72.013 10.036 1.00 90.82 ? 132 ASP A O 1 ATOM 1041 C CB . ASP A 1 132 ? 9.993 71.527 12.205 1.00 85.87 ? 132 ASP A CB 1 ATOM 1042 C CG . ASP A 1 132 ? 8.995 72.367 11.441 1.00 114.57 ? 132 ASP A CG 1 ATOM 1043 O OD1 . ASP A 1 132 ? 9.405 73.378 10.831 1.00 123.66 ? 132 ASP A OD1 1 ATOM 1044 O OD2 . ASP A 1 132 ? 7.797 72.022 11.457 1.00 131.96 ? 132 ASP A OD2 1 ATOM 1045 N N . GLY A 1 133 ? 10.937 70.202 8.984 1.00 91.15 ? 133 GLY A N 1 ATOM 1046 C CA . GLY A 1 133 ? 11.055 70.660 7.610 1.00 100.78 ? 133 GLY A CA 1 ATOM 1047 C C . GLY A 1 133 ? 12.471 70.923 7.131 1.00 106.75 ? 133 GLY A C 1 ATOM 1048 O O . GLY A 1 133 ? 12.787 70.740 5.956 1.00 121.26 ? 133 GLY A O 1 ATOM 1049 N N . THR A 1 134 ? 13.327 71.349 8.056 1.00 102.78 ? 134 THR A N 1 ATOM 1050 C CA . THR A 1 134 ? 14.745 71.554 7.790 1.00 112.41 ? 134 THR A CA 1 ATOM 1051 C C . THR A 1 134 ? 15.601 71.083 8.963 1.00 110.60 ? 134 THR A C 1 ATOM 1052 O O . THR A 1 134 ? 16.361 70.120 8.865 1.00 123.02 ? 134 THR A O 1 ATOM 1053 C CB . THR A 1 134 ? 15.053 73.037 7.481 1.00 113.34 ? 134 THR A CB 1 ATOM 1054 O OG1 . THR A 1 134 ? 16.374 73.359 7.935 1.00 114.58 ? 134 THR A OG1 1 ATOM 1055 C CG2 . THR A 1 134 ? 14.046 73.956 8.163 1.00 107.47 ? 134 THR A CG2 1 ATOM 1056 N N . LYS A 1 135 ? 15.453 71.800 10.075 1.00 89.53 ? 135 LYS A N 1 ATOM 1057 C CA . LYS A 1 135 ? 16.274 71.632 11.266 1.00 89.93 ? 135 LYS A CA 1 ATOM 1058 C C . LYS A 1 135 ? 15.949 70.343 12.010 1.00 88.05 ? 135 LYS A C 1 ATOM 1059 O O . LYS A 1 135 ? 14.784 69.981 12.167 1.00 75.14 ? 135 LYS A O 1 ATOM 1060 C CB . LYS A 1 135 ? 16.085 72.839 12.191 1.00 91.30 ? 135 LYS A CB 1 ATOM 1061 C CG . LYS A 1 135 ? 17.096 72.964 13.318 1.00 98.17 ? 135 LYS A CG 1 ATOM 1062 C CD . LYS A 1 135 ? 16.899 74.281 14.058 1.00 105.94 ? 135 LYS A CD 1 ATOM 1063 C CE . LYS A 1 135 ? 18.007 74.541 15.066 1.00 109.05 ? 135 LYS A CE 1 ATOM 1064 N NZ . LYS A 1 135 ? 17.961 73.597 16.214 1.00 75.34 ? 135 LYS A NZ 1 ATOM 1065 N N . THR A 1 136 ? 16.990 69.656 12.468 1.00 90.79 ? 136 THR A N 1 ATOM 1066 C CA . THR A 1 136 ? 16.824 68.403 13.192 1.00 67.73 ? 136 THR A CA 1 ATOM 1067 C C . THR A 1 136 ? 17.556 68.442 14.528 1.00 80.98 ? 136 THR A C 1 ATOM 1068 O O . THR A 1 136 ? 18.769 68.647 14.575 1.00 95.84 ? 136 THR A O 1 ATOM 1069 C CB . THR A 1 136 ? 17.335 67.206 12.370 1.00 68.23 ? 136 THR A CB 1 ATOM 1070 O OG1 . THR A 1 136 ? 16.672 67.177 11.100 1.00 68.98 ? 136 THR A OG1 1 ATOM 1071 C CG2 . THR A 1 136 ? 17.073 65.903 13.108 1.00 64.01 ? 136 THR A CG2 1 ATOM 1072 N N . VAL A 1 137 ? 16.813 68.249 15.612 1.00 64.57 ? 137 VAL A N 1 ATOM 1073 C CA . VAL A 1 137 ? 17.397 68.235 16.947 1.00 63.04 ? 137 VAL A CA 1 ATOM 1074 C C . VAL A 1 137 ? 17.305 66.844 17.563 1.00 64.47 ? 137 VAL A C 1 ATOM 1075 O O . VAL A 1 137 ? 16.403 66.071 17.242 1.00 80.15 ? 137 VAL A O 1 ATOM 1076 C CB . VAL A 1 137 ? 16.711 69.253 17.879 1.00 63.38 ? 137 VAL A CB 1 ATOM 1077 C CG1 . VAL A 1 137 ? 16.867 70.659 17.331 1.00 66.81 ? 137 VAL A CG1 1 ATOM 1078 C CG2 . VAL A 1 137 ? 15.239 68.910 18.057 1.00 61.45 ? 137 VAL A CG2 1 ATOM 1079 N N . GLU A 1 138 ? 18.251 66.524 18.439 1.00 63.28 ? 138 GLU A N 1 ATOM 1080 C CA . GLU A 1 138 ? 18.237 65.243 19.132 1.00 72.77 ? 138 GLU A CA 1 ATOM 1081 C C . GLU A 1 138 ? 17.591 65.389 20.504 1.00 77.27 ? 138 GLU A C 1 ATOM 1082 O O . GLU A 1 138 ? 17.886 66.327 21.245 1.00 83.98 ? 138 GLU A O 1 ATOM 1083 C CB . GLU A 1 138 ? 19.653 64.681 19.269 1.00 72.23 ? 138 GLU A CB 1 ATOM 1084 C CG . GLU A 1 138 ? 19.700 63.280 19.860 1.00 62.79 ? 138 GLU A CG 1 ATOM 1085 C CD . GLU A 1 138 ? 21.109 62.730 19.952 1.00 80.52 ? 138 GLU A CD 1 ATOM 1086 O OE1 . GLU A 1 138 ? 22.068 63.522 19.831 1.00 103.01 ? 138 GLU A OE1 1 ATOM 1087 O OE2 . GLU A 1 138 ? 21.259 61.505 20.141 1.00 69.99 ? 138 GLU A OE2 1 ATOM 1088 N N . TYR A 1 139 ? 16.706 64.455 20.835 1.00 65.04 ? 139 TYR A N 1 ATOM 1089 C CA . TYR A 1 139 ? 15.983 64.496 22.098 1.00 51.78 ? 139 TYR A CA 1 ATOM 1090 C C . TYR A 1 139 ? 16.191 63.195 22.867 1.00 62.34 ? 139 TYR A C 1 ATOM 1091 O O . TYR A 1 139 ? 15.733 62.134 22.443 1.00 71.48 ? 139 TYR A O 1 ATOM 1092 C CB . TYR A 1 139 ? 14.496 64.749 21.836 1.00 51.22 ? 139 TYR A CB 1 ATOM 1093 C CG . TYR A 1 139 ? 13.641 64.900 23.073 1.00 65.29 ? 139 TYR A CG 1 ATOM 1094 C CD1 . TYR A 1 139 ? 13.874 65.922 23.984 1.00 67.98 ? 139 TYR A CD1 1 ATOM 1095 C CD2 . TYR A 1 139 ? 12.581 64.037 23.314 1.00 67.12 ? 139 TYR A CD2 1 ATOM 1096 C CE1 . TYR A 1 139 ? 13.087 66.067 25.111 1.00 62.68 ? 139 TYR A CE1 1 ATOM 1097 C CE2 . TYR A 1 139 ? 11.787 64.176 24.434 1.00 55.88 ? 139 TYR A CE2 1 ATOM 1098 C CZ . TYR A 1 139 ? 12.042 65.193 25.327 1.00 49.66 ? 139 TYR A CZ 1 ATOM 1099 O OH . TYR A 1 139 ? 11.254 65.326 26.445 1.00 58.54 ? 139 TYR A OH 1 ATOM 1100 N N . ALA A 1 140 ? 16.890 63.282 23.995 1.00 50.09 ? 140 ALA A N 1 ATOM 1101 C CA . ALA A 1 140 ? 17.214 62.101 24.789 1.00 51.34 ? 140 ALA A CA 1 ATOM 1102 C C . ALA A 1 140 ? 17.158 62.389 26.287 1.00 48.82 ? 140 ALA A C 1 ATOM 1103 O O . ALA A 1 140 ? 18.199 62.531 26.930 1.00 49.93 ? 140 ALA A O 1 ATOM 1104 C CB . ALA A 1 140 ? 18.588 61.573 24.405 1.00 49.45 ? 140 ALA A CB 1 ATOM 1105 N N . PRO A 1 141 ? 15.942 62.462 26.851 1.00 54.19 ? 141 PRO A N 1 ATOM 1106 C CA . PRO A 1 141 ? 15.755 62.783 28.271 1.00 55.44 ? 141 PRO A CA 1 ATOM 1107 C C . PRO A 1 141 ? 16.373 61.743 29.199 1.00 61.47 ? 141 PRO A C 1 ATOM 1108 O O . PRO A 1 141 ? 16.917 62.099 30.243 1.00 75.29 ? 141 PRO A O 1 ATOM 1109 C CB . PRO A 1 141 ? 14.231 62.804 28.434 1.00 50.32 ? 141 PRO A CB 1 ATOM 1110 C CG . PRO A 1 141 ? 13.690 62.938 27.065 1.00 51.02 ? 141 PRO A CG 1 ATOM 1111 C CD . PRO A 1 141 ? 14.659 62.256 26.161 1.00 55.22 ? 141 PRO A CD 1 ATOM 1112 N N . CYS A 1 142 ? 16.287 60.473 28.818 1.00 59.21 ? 142 CYS A N 1 ATOM 1113 C CA . CYS A 1 142 ? 16.833 59.394 29.634 1.00 68.75 ? 142 CYS A CA 1 ATOM 1114 C C . CYS A 1 142 ? 18.356 59.400 29.632 1.00 66.58 ? 142 CYS A C 1 ATOM 1115 O O . CYS A 1 142 ? 18.990 58.706 30.429 1.00 79.16 ? 142 CYS A O 1 ATOM 1116 C CB . CYS A 1 142 ? 16.315 58.039 29.149 1.00 84.45 ? 142 CYS A CB 1 ATOM 1117 S SG . CYS A 1 142 ? 14.952 57.380 30.130 1.00 44.83 ? 142 CYS A SG 1 ATOM 1118 N N . ARG A 1 143 ? 18.942 60.190 28.741 1.00 51.21 ? 143 ARG A N 1 ATOM 1119 C CA . ARG A 1 143 ? 20.389 60.316 28.685 1.00 52.95 ? 143 ARG A CA 1 ATOM 1120 C C . ARG A 1 143 ? 20.813 61.492 29.554 1.00 66.50 ? 143 ARG A C 1 ATOM 1121 O O . ARG A 1 143 ? 20.585 62.649 29.202 1.00 90.65 ? 143 ARG A O 1 ATOM 1122 C CB . ARG A 1 143 ? 20.851 60.504 27.239 1.00 51.35 ? 143 ARG A CB 1 ATOM 1123 C CG . ARG A 1 143 ? 22.345 60.661 27.074 1.00 52.46 ? 143 ARG A CG 1 ATOM 1124 C CD . ARG A 1 143 ? 22.743 60.705 25.608 1.00 65.58 ? 143 ARG A CD 1 ATOM 1125 N NE . ARG A 1 143 ? 22.316 61.940 24.958 1.00 54.04 ? 143 ARG A NE 1 ATOM 1126 C CZ . ARG A 1 143 ? 22.331 62.133 23.644 1.00 61.24 ? 143 ARG A CZ 1 ATOM 1127 N NH1 . ARG A 1 143 ? 22.743 61.167 22.835 1.00 54.59 ? 143 ARG A NH1 1 ATOM 1128 N NH2 . ARG A 1 143 ? 21.927 63.290 23.136 1.00 81.71 ? 143 ARG A NH2 1 ATOM 1129 N N . SER A 1 144 ? 21.445 61.188 30.683 1.00 66.10 ? 144 SER A N 1 ATOM 1130 C CA . SER A 1 144 ? 21.713 62.197 31.701 1.00 84.06 ? 144 SER A CA 1 ATOM 1131 C C . SER A 1 144 ? 22.769 61.751 32.707 1.00 76.88 ? 144 SER A C 1 ATOM 1132 O O . SER A 1 144 ? 23.366 60.686 32.571 1.00 72.65 ? 144 SER A O 1 ATOM 1133 C CB . SER A 1 144 ? 20.422 62.551 32.440 1.00 96.59 ? 144 SER A CB 1 ATOM 1134 O OG . SER A 1 144 ? 19.853 61.400 33.039 1.00 87.66 ? 144 SER A OG 1 ATOM 1135 N N . GLN A 1 145 ? 22.972 62.560 33.740 1.00 66.96 ? 145 GLN A N 1 ATOM 1136 C CA . GLN A 1 145 ? 23.987 62.266 34.742 1.00 71.84 ? 145 GLN A CA 1 ATOM 1137 C C . GLN A 1 145 ? 23.470 61.254 35.762 1.00 78.69 ? 145 GLN A C 1 ATOM 1138 O O . GLN A 1 145 ? 24.192 60.849 36.672 1.00 100.84 ? 145 GLN A O 1 ATOM 1139 C CB . GLN A 1 145 ? 24.435 63.551 35.439 1.00 98.35 ? 145 GLN A CB 1 ATOM 1140 C CG . GLN A 1 145 ? 24.902 64.648 34.488 1.00 113.20 ? 145 GLN A CG 1 ATOM 1141 C CD . GLN A 1 145 ? 26.163 64.280 33.722 1.00 111.69 ? 145 GLN A CD 1 ATOM 1142 O OE1 . GLN A 1 145 ? 26.879 63.347 34.088 1.00 126.18 ? 145 GLN A OE1 1 ATOM 1143 N NE2 . GLN A 1 145 ? 26.439 65.017 32.653 1.00 93.30 ? 145 GLN A NE2 1 ATOM 1144 N N . ASP A 1 146 ? 22.212 60.854 35.600 1.00 72.93 ? 146 ASP A N 1 ATOM 1145 C CA . ASP A 1 146 ? 21.637 59.767 36.382 1.00 75.86 ? 146 ASP A CA 1 ATOM 1146 C C . ASP A 1 146 ? 21.797 58.474 35.588 1.00 70.81 ? 146 ASP A C 1 ATOM 1147 O O . ASP A 1 146 ? 21.182 58.311 34.534 1.00 86.77 ? 146 ASP A O 1 ATOM 1148 C CB . ASP A 1 146 ? 20.164 60.041 36.689 1.00 87.48 ? 146 ASP A CB 1 ATOM 1149 C CG . ASP A 1 146 ? 19.675 59.295 37.914 1.00 97.89 ? 146 ASP A CG 1 ATOM 1150 O OD1 . ASP A 1 146 ? 20.412 58.421 38.416 1.00 112.00 ? 146 ASP A OD1 1 ATOM 1151 O OD2 . ASP A 1 146 ? 18.549 59.582 38.373 1.00 89.73 ? 146 ASP A OD2 1 ATOM 1152 N N . ILE A 1 147 ? 22.616 57.554 36.091 1.00 65.74 ? 147 ILE A N 1 ATOM 1153 C CA . ILE A 1 147 ? 23.065 56.429 35.275 1.00 72.54 ? 147 ILE A CA 1 ATOM 1154 C C . ILE A 1 147 ? 22.827 55.035 35.860 1.00 76.24 ? 147 ILE A C 1 ATOM 1155 O O . ILE A 1 147 ? 22.161 54.862 36.881 1.00 80.19 ? 147 ILE A O 1 ATOM 1156 C CB . ILE A 1 147 ? 24.573 56.543 34.960 1.00 60.36 ? 147 ILE A CB 1 ATOM 1157 C CG1 . ILE A 1 147 ? 25.399 56.458 36.244 1.00 62.81 ? 147 ILE A CG1 1 ATOM 1158 C CG2 . ILE A 1 147 ? 24.869 57.834 34.210 1.00 60.99 ? 147 ILE A CG2 1 ATOM 1159 C CD1 . ILE A 1 147 ? 26.888 56.366 36.000 1.00 60.11 ? 147 ILE A CD1 1 ATOM 1160 N N . ASP A 1 148 ? 23.396 54.055 35.162 1.00 61.44 ? 148 ASP A N 1 ATOM 1161 C CA . ASP A 1 148 ? 23.259 52.622 35.426 1.00 68.82 ? 148 ASP A CA 1 ATOM 1162 C C . ASP A 1 148 ? 21.808 52.148 35.450 1.00 79.92 ? 148 ASP A C 1 ATOM 1163 O O . ASP A 1 148 ? 20.968 52.665 34.715 1.00 91.79 ? 148 ASP A O 1 ATOM 1164 C CB . ASP A 1 148 ? 23.940 52.267 36.752 1.00 68.14 ? 148 ASP A CB 1 ATOM 1165 C CG . ASP A 1 148 ? 25.374 52.762 36.823 1.00 67.70 ? 148 ASP A CG 1 ATOM 1166 O OD1 . ASP A 1 148 ? 26.017 52.881 35.758 1.00 71.67 ? 148 ASP A OD1 1 ATOM 1167 O OD2 . ASP A 1 148 ? 25.858 53.029 37.942 1.00 66.02 ? 148 ASP A OD2 1 ATOM 1168 N N . ALA A 1 149 ? 21.513 51.175 36.307 1.00 68.96 ? 149 ALA A N 1 ATOM 1169 C CA . ALA A 1 149 ? 20.157 50.643 36.403 1.00 58.32 ? 149 ALA A CA 1 ATOM 1170 C C . ALA A 1 149 ? 19.350 51.368 37.466 1.00 62.40 ? 149 ALA A C 1 ATOM 1171 O O . ALA A 1 149 ? 18.121 51.303 37.483 1.00 78.28 ? 149 ALA A O 1 ATOM 1172 C CB . ALA A 1 149 ? 20.194 49.153 36.690 1.00 58.97 ? 149 ALA A CB 1 ATOM 1173 N N . ASP A 1 150 ? 20.051 52.084 38.337 1.00 65.72 ? 150 ASP A N 1 ATOM 1174 C CA . ASP A 1 150 ? 19.410 52.803 39.426 1.00 69.20 ? 150 ASP A CA 1 ATOM 1175 C C . ASP A 1 150 ? 18.784 54.066 38.862 1.00 67.27 ? 150 ASP A C 1 ATOM 1176 O O . ASP A 1 150 ? 17.734 54.519 39.317 1.00 66.45 ? 150 ASP A O 1 ATOM 1177 C CB . ASP A 1 150 ? 20.423 53.136 40.524 1.00 81.01 ? 150 ASP A CB 1 ATOM 1178 C CG . ASP A 1 150 ? 19.769 53.390 41.868 1.00 113.40 ? 150 ASP A CG 1 ATOM 1179 O OD1 . ASP A 1 150 ? 18.551 53.663 41.901 1.00 135.44 ? 150 ASP A OD1 1 ATOM 1180 O OD2 . ASP A 1 150 ? 20.477 53.318 42.896 1.00 114.91 ? 150 ASP A OD2 1 ATOM 1181 N N . GLY A 1 151 ? 19.444 54.617 37.850 1.00 82.05 ? 151 GLY A N 1 ATOM 1182 C CA . GLY A 1 151 ? 18.983 55.816 37.181 1.00 81.80 ? 151 GLY A CA 1 ATOM 1183 C C . GLY A 1 151 ? 18.265 55.526 35.879 1.00 73.71 ? 151 GLY A C 1 ATOM 1184 O O . GLY A 1 151 ? 17.582 54.511 35.738 1.00 81.49 ? 151 GLY A O 1 ATOM 1185 N N . GLN A 1 152 ? 18.425 56.436 34.925 1.00 61.92 ? 152 GLN A N 1 ATOM 1186 C CA . GLN A 1 152 ? 17.741 56.361 33.641 1.00 67.70 ? 152 GLN A CA 1 ATOM 1187 C C . GLN A 1 152 ? 18.568 55.640 32.578 1.00 58.90 ? 152 GLN A C 1 ATOM 1188 O O . GLN A 1 152 ? 18.189 55.611 31.408 1.00 67.27 ? 152 GLN A O 1 ATOM 1189 C CB . GLN A 1 152 ? 17.384 57.768 33.161 1.00 84.36 ? 152 GLN A CB 1 ATOM 1190 C CG . GLN A 1 152 ? 16.444 58.512 34.096 1.00 88.10 ? 152 GLN A CG 1 ATOM 1191 C CD . GLN A 1 152 ? 16.499 60.014 33.906 1.00 94.23 ? 152 GLN A CD 1 ATOM 1192 O OE1 . GLN A 1 152 ? 17.524 60.563 33.503 1.00 98.81 ? 152 GLN A OE1 1 ATOM 1193 N NE2 . GLN A 1 152 ? 15.392 60.687 34.198 1.00 100.88 ? 152 GLN A NE2 1 ATOM 1194 N N . GLY A 1 153 ? 19.705 55.082 32.983 1.00 53.33 ? 153 GLY A N 1 ATOM 1195 C CA . GLY A 1 153 ? 20.610 54.416 32.061 1.00 53.16 ? 153 GLY A CA 1 ATOM 1196 C C . GLY A 1 153 ? 19.980 53.355 31.175 1.00 50.91 ? 153 GLY A C 1 ATOM 1197 O O . GLY A 1 153 ? 20.295 53.256 29.989 1.00 53.34 ? 153 GLY A O 1 ATOM 1198 N N . PHE A 1 154 ? 19.101 52.545 31.751 1.00 48.05 ? 154 PHE A N 1 ATOM 1199 C CA . PHE A 1 154 ? 18.439 51.480 31.003 1.00 47.00 ? 154 PHE A CA 1 ATOM 1200 C C . PHE A 1 154 ? 17.048 51.848 30.504 1.00 56.07 ? 154 PHE A C 1 ATOM 1201 O O . PHE A 1 154 ? 16.337 50.997 29.968 1.00 61.34 ? 154 PHE A O 1 ATOM 1202 C CB . PHE A 1 154 ? 18.374 50.214 31.850 1.00 47.71 ? 154 PHE A CB 1 ATOM 1203 C CG . PHE A 1 154 ? 19.667 49.474 31.889 1.00 50.17 ? 154 PHE A CG 1 ATOM 1204 C CD1 . PHE A 1 154 ? 20.670 49.856 32.760 1.00 53.13 ? 154 PHE A CD1 1 ATOM 1205 C CD2 . PHE A 1 154 ? 19.897 48.420 31.026 1.00 52.52 ? 154 PHE A CD2 1 ATOM 1206 C CE1 . PHE A 1 154 ? 21.869 49.185 32.783 1.00 63.80 ? 154 PHE A CE1 1 ATOM 1207 C CE2 . PHE A 1 154 ? 21.093 47.746 31.047 1.00 57.30 ? 154 PHE A CE2 1 ATOM 1208 C CZ . PHE A 1 154 ? 22.080 48.131 31.924 1.00 63.47 ? 154 PHE A CZ 1 ATOM 1209 N N . CYS A 1 155 ? 16.669 53.109 30.692 1.00 63.85 ? 155 CYS A N 1 ATOM 1210 C CA . CYS A 1 155 ? 15.317 53.585 30.396 1.00 63.65 ? 155 CYS A CA 1 ATOM 1211 C C . CYS A 1 155 ? 14.774 53.164 29.036 1.00 63.00 ? 155 CYS A C 1 ATOM 1212 O O . CYS A 1 155 ? 13.608 52.780 28.928 1.00 44.72 ? 155 CYS A O 1 ATOM 1213 C CB . CYS A 1 155 ? 15.266 55.108 30.489 1.00 46.17 ? 155 CYS A CB 1 ATOM 1214 S SG . CYS A 1 155 ? 13.674 55.809 30.007 1.00 149.18 ? 155 CYS A SG 1 ATOM 1215 N N . GLN A 1 156 ? 15.621 53.235 28.012 1.00 64.46 ? 156 GLN A N 1 ATOM 1216 C CA . GLN A 1 156 ? 15.197 53.023 26.631 1.00 59.91 ? 156 GLN A CA 1 ATOM 1217 C C . GLN A 1 156 ? 14.072 53.989 26.283 1.00 67.88 ? 156 GLN A C 1 ATOM 1218 O O . GLN A 1 156 ? 13.054 53.594 25.714 1.00 78.46 ? 156 GLN A O 1 ATOM 1219 C CB . GLN A 1 156 ? 14.749 51.575 26.400 1.00 42.65 ? 156 GLN A CB 1 ATOM 1220 C CG . GLN A 1 156 ? 15.809 50.532 26.706 1.00 43.63 ? 156 GLN A CG 1 ATOM 1221 C CD . GLN A 1 156 ? 15.372 49.132 26.324 1.00 47.75 ? 156 GLN A CD 1 ATOM 1222 O OE1 . GLN A 1 156 ? 15.491 48.195 27.114 1.00 53.47 ? 156 GLN A OE1 1 ATOM 1223 N NE2 . GLN A 1 156 ? 14.868 48.982 25.106 1.00 46.87 ? 156 GLN A NE2 1 ATOM 1224 N N . GLY A 1 157 ? 14.263 55.255 26.647 1.00 55.01 ? 157 GLY A N 1 ATOM 1225 C CA . GLY A 1 157 ? 13.282 56.291 26.380 1.00 46.67 ? 157 GLY A CA 1 ATOM 1226 C C . GLY A 1 157 ? 12.994 56.427 24.899 1.00 55.04 ? 157 GLY A C 1 ATOM 1227 O O . GLY A 1 157 ? 13.903 56.362 24.071 1.00 56.88 ? 157 GLY A O 1 ATOM 1228 N N . GLY A 1 158 ? 11.722 56.615 24.564 1.00 53.77 ? 158 GLY A N 1 ATOM 1229 C CA . GLY A 1 158 ? 11.304 56.678 23.177 1.00 47.68 ? 158 GLY A CA 1 ATOM 1230 C C . GLY A 1 158 ? 10.618 55.393 22.757 1.00 46.87 ? 158 GLY A C 1 ATOM 1231 O O . GLY A 1 158 ? 10.229 55.233 21.600 1.00 53.13 ? 158 GLY A O 1 ATOM 1232 N N . PHE A 1 159 ? 10.478 54.475 23.709 1.00 40.59 ? 159 PHE A N 1 ATOM 1233 C CA . PHE A 1 159 ? 9.787 53.210 23.484 1.00 43.10 ? 159 PHE A CA 1 ATOM 1234 C C . PHE A 1 159 ? 8.355 53.468 23.020 1.00 40.19 ? 159 PHE A C 1 ATOM 1235 O O . PHE A 1 159 ? 7.836 52.770 22.148 1.00 37.08 ? 159 PHE A O 1 ATOM 1236 C CB . PHE A 1 159 ? 9.799 52.369 24.763 1.00 55.96 ? 159 PHE A CB 1 ATOM 1237 C CG . PHE A 1 159 ? 9.451 50.921 24.551 1.00 50.21 ? 159 PHE A CG 1 ATOM 1238 C CD1 . PHE A 1 159 ? 10.366 50.050 23.984 1.00 44.19 ? 159 PHE A CD1 1 ATOM 1239 C CD2 . PHE A 1 159 ? 8.217 50.427 24.942 1.00 52.51 ? 159 PHE A CD2 1 ATOM 1240 C CE1 . PHE A 1 159 ? 10.053 48.717 23.796 1.00 53.53 ? 159 PHE A CE1 1 ATOM 1241 C CE2 . PHE A 1 159 ? 7.897 49.094 24.757 1.00 52.18 ? 159 PHE A CE2 1 ATOM 1242 C CZ . PHE A 1 159 ? 8.817 48.239 24.183 1.00 57.01 ? 159 PHE A CZ 1 ATOM 1243 N N . SER A 1 160 ? 7.728 54.479 23.613 1.00 43.86 ? 160 SER A N 1 ATOM 1244 C CA . SER A 1 160 ? 6.404 54.929 23.199 1.00 48.18 ? 160 SER A CA 1 ATOM 1245 C C . SER A 1 160 ? 6.304 56.448 23.316 1.00 59.33 ? 160 SER A C 1 ATOM 1246 O O . SER A 1 160 ? 6.724 57.026 24.320 1.00 85.82 ? 160 SER A O 1 ATOM 1247 C CB . SER A 1 160 ? 5.319 54.254 24.039 1.00 52.25 ? 160 SER A CB 1 ATOM 1248 O OG . SER A 1 160 ? 5.489 54.541 25.417 1.00 40.97 ? 160 SER A OG 1 ATOM 1249 N N . ILE A 1 161 ? 5.747 57.094 22.294 1.00 42.44 ? 161 ILE A N 1 ATOM 1250 C CA . ILE A 1 161 ? 5.667 58.554 22.266 1.00 43.82 ? 161 ILE A CA 1 ATOM 1251 C C . ILE A 1 161 ? 4.317 59.066 21.773 1.00 44.82 ? 161 ILE A C 1 ATOM 1252 O O . ILE A 1 161 ? 3.593 58.360 21.071 1.00 62.55 ? 161 ILE A O 1 ATOM 1253 C CB . ILE A 1 161 ? 6.767 59.160 21.373 1.00 50.94 ? 161 ILE A CB 1 ATOM 1254 C CG1 . ILE A 1 161 ? 6.760 58.492 19.996 1.00 53.11 ? 161 ILE A CG1 1 ATOM 1255 C CG2 . ILE A 1 161 ? 8.132 59.020 22.028 1.00 59.77 ? 161 ILE A CG2 1 ATOM 1256 C CD1 . ILE A 1 161 ? 7.815 59.027 19.052 1.00 71.52 ? 161 ILE A CD1 1 ATOM 1257 N N . ASP A 1 162 ? 3.985 60.299 22.148 1.00 47.92 ? 162 ASP A N 1 ATOM 1258 C CA . ASP A 1 162 ? 2.755 60.937 21.690 1.00 58.27 ? 162 ASP A CA 1 ATOM 1259 C C . ASP A 1 162 ? 2.835 62.463 21.789 1.00 63.98 ? 162 ASP A C 1 ATOM 1260 O O . ASP A 1 162 ? 3.668 63.007 22.515 1.00 62.27 ? 162 ASP A O 1 ATOM 1261 C CB . ASP A 1 162 ? 1.558 60.423 22.494 1.00 58.26 ? 162 ASP A CB 1 ATOM 1262 C CG . ASP A 1 162 ? 0.323 60.223 21.636 1.00 72.23 ? 162 ASP A CG 1 ATOM 1263 O OD1 . ASP A 1 162 ? 0.172 60.945 20.628 1.00 85.61 ? 162 ASP A OD1 1 ATOM 1264 O OD2 . ASP A 1 162 ? -0.496 59.341 21.968 1.00 80.06 ? 162 ASP A OD2 1 ATOM 1265 N N . PHE A 1 163 ? 1.959 63.144 21.054 1.00 60.32 ? 163 PHE A N 1 ATOM 1266 C CA . PHE A 1 163 ? 1.863 64.601 21.096 1.00 55.81 ? 163 PHE A CA 1 ATOM 1267 C C . PHE A 1 163 ? 0.565 65.036 21.766 1.00 62.77 ? 163 PHE A C 1 ATOM 1268 O O . PHE A 1 163 ? -0.437 64.327 21.704 1.00 72.27 ? 163 PHE A O 1 ATOM 1269 C CB . PHE A 1 163 ? 1.924 65.201 19.688 1.00 57.18 ? 163 PHE A CB 1 ATOM 1270 C CG . PHE A 1 163 ? 3.287 65.173 19.061 1.00 51.42 ? 163 PHE A CG 1 ATOM 1271 C CD1 . PHE A 1 163 ? 3.594 64.245 18.081 1.00 50.60 ? 163 PHE A CD1 1 ATOM 1272 C CD2 . PHE A 1 163 ? 4.256 66.088 19.436 1.00 72.93 ? 163 PHE A CD2 1 ATOM 1273 C CE1 . PHE A 1 163 ? 4.844 64.222 17.494 1.00 66.28 ? 163 PHE A CE1 1 ATOM 1274 C CE2 . PHE A 1 163 ? 5.508 66.071 18.852 1.00 74.14 ? 163 PHE A CE2 1 ATOM 1275 C CZ . PHE A 1 163 ? 5.803 65.135 17.881 1.00 71.71 ? 163 PHE A CZ 1 ATOM 1276 N N . THR A 1 164 ? 0.582 66.202 22.403 1.00 52.71 ? 164 THR A N 1 ATOM 1277 C CA . THR A 1 164 ? -0.646 66.789 22.923 1.00 62.77 ? 164 THR A CA 1 ATOM 1278 C C . THR A 1 164 ? -1.103 67.927 22.014 1.00 65.06 ? 164 THR A C 1 ATOM 1279 O O . THR A 1 164 ? -0.417 68.273 21.052 1.00 74.74 ? 164 THR A O 1 ATOM 1280 C CB . THR A 1 164 ? -0.465 67.313 24.359 1.00 61.82 ? 164 THR A CB 1 ATOM 1281 O OG1 . THR A 1 164 ? 0.456 68.412 24.360 1.00 59.15 ? 164 THR A OG1 1 ATOM 1282 C CG2 . THR A 1 164 ? 0.062 66.211 25.264 1.00 53.33 ? 164 THR A CG2 1 ATOM 1283 N N . LYS A 1 165 ? -2.254 68.516 22.326 1.00 59.39 ? 165 LYS A N 1 ATOM 1284 C CA . LYS A 1 165 ? -2.776 69.626 21.536 1.00 63.23 ? 165 LYS A CA 1 ATOM 1285 C C . LYS A 1 165 ? -2.008 70.906 21.834 1.00 79.72 ? 165 LYS A C 1 ATOM 1286 O O . LYS A 1 165 ? -2.061 71.870 21.071 1.00 88.59 ? 165 LYS A O 1 ATOM 1287 C CB . LYS A 1 165 ? -4.268 69.831 21.808 1.00 67.20 ? 165 LYS A CB 1 ATOM 1288 C CG . LYS A 1 165 ? -5.167 68.833 21.100 1.00 86.72 ? 165 LYS A CG 1 ATOM 1289 C CD . LYS A 1 165 ? -5.011 68.942 19.591 1.00 108.36 ? 165 LYS A CD 1 ATOM 1290 C CE . LYS A 1 165 ? -5.907 67.951 18.865 1.00 112.94 ? 165 LYS A CE 1 ATOM 1291 N NZ . LYS A 1 165 ? -5.553 66.539 19.181 1.00 104.74 ? 165 LYS A NZ 1 ATOM 1292 N N . ALA A 1 166 ? -1.284 70.896 22.947 1.00 84.52 ? 166 ALA A N 1 ATOM 1293 C CA . ALA A 1 166 ? -0.511 72.049 23.388 1.00 87.14 ? 166 ALA A CA 1 ATOM 1294 C C . ALA A 1 166 ? 0.896 72.010 22.804 1.00 78.63 ? 166 ALA A C 1 ATOM 1295 O O . ALA A 1 166 ? 1.746 72.824 23.168 1.00 77.77 ? 166 ALA A O 1 ATOM 1296 C CB . ALA A 1 166 ? -0.456 72.101 24.906 1.00 95.77 ? 166 ALA A CB 1 ATOM 1297 N N . ASP A 1 167 ? 1.129 71.051 21.910 1.00 75.06 ? 167 ASP A N 1 ATOM 1298 C CA . ASP A 1 167 ? 2.452 70.791 21.346 1.00 81.26 ? 167 ASP A CA 1 ATOM 1299 C C . ASP A 1 167 ? 3.446 70.470 22.453 1.00 71.22 ? 167 ASP A C 1 ATOM 1300 O O . ASP A 1 167 ? 4.497 71.099 22.571 1.00 85.16 ? 167 ASP A O 1 ATOM 1301 C CB . ASP A 1 167 ? 2.941 71.975 20.508 1.00 108.69 ? 167 ASP A CB 1 ATOM 1302 C CG . ASP A 1 167 ? 2.234 72.072 19.171 1.00 129.75 ? 167 ASP A CG 1 ATOM 1303 O OD1 . ASP A 1 167 ? 2.749 71.507 18.184 1.00 131.54 ? 167 ASP A OD1 1 ATOM 1304 O OD2 . ASP A 1 167 ? 1.162 72.710 19.107 1.00 140.80 ? 167 ASP A OD2 1 ATOM 1305 N N . ARG A 1 168 ? 3.081 69.494 23.276 1.00 60.14 ? 168 ARG A N 1 ATOM 1306 C CA . ARG A 1 168 ? 3.957 68.978 24.316 1.00 59.09 ? 168 ARG A CA 1 ATOM 1307 C C . ARG A 1 168 ? 4.178 67.486 24.085 1.00 59.00 ? 168 ARG A C 1 ATOM 1308 O O . ARG A 1 168 ? 3.222 66.732 23.899 1.00 70.13 ? 168 ARG A O 1 ATOM 1309 C CB . ARG A 1 168 ? 3.361 69.234 25.702 1.00 57.27 ? 168 ARG A CB 1 ATOM 1310 C CG . ARG A 1 168 ? 4.167 68.644 26.844 1.00 55.94 ? 168 ARG A CG 1 ATOM 1311 C CD . ARG A 1 168 ? 3.445 68.801 28.174 1.00 64.12 ? 168 ARG A CD 1 ATOM 1312 N NE . ARG A 1 168 ? 3.550 70.154 28.710 1.00 75.61 ? 168 ARG A NE 1 ATOM 1313 C CZ . ARG A 1 168 ? 4.511 70.556 29.534 1.00 77.20 ? 168 ARG A CZ 1 ATOM 1314 N NH1 . ARG A 1 168 ? 5.456 69.707 29.916 1.00 77.21 ? 168 ARG A NH1 1 ATOM 1315 N NH2 . ARG A 1 168 ? 4.531 71.806 29.977 1.00 79.21 ? 168 ARG A NH2 1 ATOM 1316 N N . VAL A 1 169 ? 5.438 67.066 24.080 1.00 52.82 ? 169 VAL A N 1 ATOM 1317 C CA . VAL A 1 169 ? 5.774 65.672 23.812 1.00 49.75 ? 169 VAL A CA 1 ATOM 1318 C C . VAL A 1 169 ? 5.657 64.806 25.059 1.00 48.18 ? 169 VAL A C 1 ATOM 1319 O O . VAL A 1 169 ? 6.263 65.102 26.085 1.00 48.65 ? 169 VAL A O 1 ATOM 1320 C CB . VAL A 1 169 ? 7.204 65.537 23.250 1.00 52.95 ? 169 VAL A CB 1 ATOM 1321 C CG1 . VAL A 1 169 ? 7.658 64.084 23.278 1.00 47.21 ? 169 VAL A CG1 1 ATOM 1322 C CG2 . VAL A 1 169 ? 7.275 66.096 21.841 1.00 50.97 ? 169 VAL A CG2 1 ATOM 1323 N N . LEU A 1 170 ? 4.872 63.738 24.964 1.00 46.59 ? 170 LEU A N 1 ATOM 1324 C CA . LEU A 1 170 ? 4.815 62.739 26.024 1.00 52.26 ? 170 LEU A CA 1 ATOM 1325 C C . LEU A 1 170 ? 5.652 61.526 25.635 1.00 59.67 ? 170 LEU A C 1 ATOM 1326 O O . LEU A 1 170 ? 5.353 60.841 24.657 1.00 70.12 ? 170 LEU A O 1 ATOM 1327 C CB . LEU A 1 170 ? 3.373 62.319 26.309 1.00 44.88 ? 170 LEU A CB 1 ATOM 1328 C CG . LEU A 1 170 ? 3.234 61.183 27.325 1.00 43.54 ? 170 LEU A CG 1 ATOM 1329 C CD1 . LEU A 1 170 ? 3.814 61.595 28.670 1.00 53.91 ? 170 LEU A CD1 1 ATOM 1330 C CD2 . LEU A 1 170 ? 1.783 60.749 27.469 1.00 44.52 ? 170 LEU A CD2 1 ATOM 1331 N N . LEU A 1 171 ? 6.700 61.265 26.408 1.00 58.97 ? 171 LEU A N 1 ATOM 1332 C CA . LEU A 1 171 ? 7.632 60.188 26.097 1.00 49.64 ? 171 LEU A CA 1 ATOM 1333 C C . LEU A 1 171 ? 7.887 59.311 27.312 1.00 51.02 ? 171 LEU A C 1 ATOM 1334 O O . LEU A 1 171 ? 8.415 59.778 28.322 1.00 54.65 ? 171 LEU A O 1 ATOM 1335 C CB . LEU A 1 171 ? 8.952 60.766 25.577 1.00 61.43 ? 171 LEU A CB 1 ATOM 1336 C CG . LEU A 1 171 ? 10.113 59.830 25.230 1.00 69.17 ? 171 LEU A CG 1 ATOM 1337 C CD1 . LEU A 1 171 ? 10.904 60.426 24.086 1.00 91.93 ? 171 LEU A CD1 1 ATOM 1338 C CD2 . LEU A 1 171 ? 11.033 59.592 26.422 1.00 48.51 ? 171 LEU A CD2 1 ATOM 1339 N N . GLY A 1 172 ? 7.506 58.043 27.220 1.00 47.67 ? 172 GLY A N 1 ATOM 1340 C CA . GLY A 1 172 ? 7.831 57.098 28.268 1.00 53.90 ? 172 GLY A CA 1 ATOM 1341 C C . GLY A 1 172 ? 8.939 56.135 27.890 1.00 50.16 ? 172 GLY A C 1 ATOM 1342 O O . GLY A 1 172 ? 9.313 56.023 26.722 1.00 38.14 ? 172 GLY A O 1 ATOM 1343 N N . GLY A 1 173 ? 9.462 55.434 28.890 1.00 41.83 ? 173 GLY A N 1 ATOM 1344 C CA . GLY A 1 173 ? 10.280 54.262 28.648 1.00 49.33 ? 173 GLY A CA 1 ATOM 1345 C C . GLY A 1 173 ? 10.227 53.341 29.850 1.00 59.60 ? 173 GLY A C 1 ATOM 1346 O O . GLY A 1 173 ? 10.097 53.800 30.984 1.00 73.97 ? 173 GLY A O 1 ATOM 1347 N N . PRO A 1 174 ? 10.357 52.032 29.603 1.00 49.79 ? 174 PRO A N 1 ATOM 1348 C CA . PRO A 1 174 ? 10.217 50.968 30.606 1.00 41.83 ? 174 PRO A CA 1 ATOM 1349 C C . PRO A 1 174 ? 11.380 50.817 31.588 1.00 46.80 ? 174 PRO A C 1 ATOM 1350 O O . PRO A 1 174 ? 11.152 50.381 32.712 1.00 64.34 ? 174 PRO A O 1 ATOM 1351 C CB . PRO A 1 174 ? 10.085 49.707 29.748 1.00 43.72 ? 174 PRO A CB 1 ATOM 1352 C CG . PRO A 1 174 ? 10.799 50.038 28.490 1.00 47.74 ? 174 PRO A CG 1 ATOM 1353 C CD . PRO A 1 174 ? 10.545 51.490 28.247 1.00 50.13 ? 174 PRO A CD 1 ATOM 1354 N N . GLY A 1 175 ? 12.593 51.173 31.178 1.00 43.17 ? 175 GLY A N 1 ATOM 1355 C CA . GLY A 1 175 ? 13.782 50.753 31.900 1.00 45.16 ? 175 GLY A CA 1 ATOM 1356 C C . GLY A 1 175 ? 14.291 51.616 33.040 1.00 47.12 ? 175 GLY A C 1 ATOM 1357 O O . GLY A 1 175 ? 15.240 51.233 33.724 1.00 51.30 ? 175 GLY A O 1 ATOM 1358 N N . SER A 1 176 ? 13.680 52.778 33.249 1.00 47.84 ? 176 SER A N 1 ATOM 1359 C CA . SER A 1 176 ? 14.132 53.686 34.301 1.00 54.53 ? 176 SER A CA 1 ATOM 1360 C C . SER A 1 176 ? 13.977 53.081 35.693 1.00 56.93 ? 176 SER A C 1 ATOM 1361 O O . SER A 1 176 ? 12.961 52.454 35.997 1.00 59.30 ? 176 SER A O 1 ATOM 1362 C CB . SER A 1 176 ? 13.374 55.011 34.233 1.00 66.03 ? 176 SER A CB 1 ATOM 1363 O OG . SER A 1 176 ? 13.868 55.837 33.194 1.00 69.05 ? 176 SER A OG 1 ATOM 1364 N N . PHE A 1 177 ? 14.999 53.281 36.522 1.00 55.71 ? 177 PHE A N 1 ATOM 1365 C CA . PHE A 1 177 ? 14.995 52.852 37.920 1.00 56.93 ? 177 PHE A CA 1 ATOM 1366 C C . PHE A 1 177 ? 14.693 51.366 38.066 1.00 60.03 ? 177 PHE A C 1 ATOM 1367 O O . PHE A 1 177 ? 13.676 50.987 38.647 1.00 65.10 ? 177 PHE A O 1 ATOM 1368 C CB . PHE A 1 177 ? 13.983 53.673 38.721 1.00 55.43 ? 177 PHE A CB 1 ATOM 1369 C CG . PHE A 1 177 ? 13.889 55.103 38.282 1.00 54.24 ? 177 PHE A CG 1 ATOM 1370 C CD1 . PHE A 1 177 ? 12.746 55.574 37.660 1.00 54.31 ? 177 PHE A CD1 1 ATOM 1371 C CD2 . PHE A 1 177 ? 14.951 55.970 38.471 1.00 55.62 ? 177 PHE A CD2 1 ATOM 1372 C CE1 . PHE A 1 177 ? 12.658 56.888 37.247 1.00 62.57 ? 177 PHE A CE1 1 ATOM 1373 C CE2 . PHE A 1 177 ? 14.870 57.285 38.061 1.00 63.87 ? 177 PHE A CE2 1 ATOM 1374 C CZ . PHE A 1 177 ? 13.721 57.744 37.447 1.00 69.54 ? 177 PHE A CZ 1 ATOM 1375 N N . TYR A 1 178 ? 15.593 50.538 37.546 1.00 58.25 ? 178 TYR A N 1 ATOM 1376 C CA . TYR A 1 178 ? 15.421 49.088 37.543 1.00 60.46 ? 178 TYR A CA 1 ATOM 1377 C C . TYR A 1 178 ? 14.066 48.684 36.971 1.00 60.40 ? 178 TYR A C 1 ATOM 1378 O O . TYR A 1 178 ? 13.320 47.912 37.577 1.00 51.39 ? 178 TYR A O 1 ATOM 1379 C CB . TYR A 1 178 ? 15.600 48.521 38.949 1.00 58.57 ? 178 TYR A CB 1 ATOM 1380 C CG . TYR A 1 178 ? 17.043 48.248 39.298 1.00 61.56 ? 178 TYR A CG 1 ATOM 1381 C CD1 . TYR A 1 178 ? 17.611 47.006 39.050 1.00 62.63 ? 178 TYR A CD1 1 ATOM 1382 C CD2 . TYR A 1 178 ? 17.842 49.231 39.869 1.00 67.45 ? 178 TYR A CD2 1 ATOM 1383 C CE1 . TYR A 1 178 ? 18.930 46.747 39.365 1.00 67.68 ? 178 TYR A CE1 1 ATOM 1384 C CE2 . TYR A 1 178 ? 19.162 48.980 40.193 1.00 67.40 ? 178 TYR A CE2 1 ATOM 1385 C CZ . TYR A 1 178 ? 19.700 47.736 39.937 1.00 68.23 ? 178 TYR A CZ 1 ATOM 1386 O OH . TYR A 1 178 ? 21.014 47.477 40.252 1.00 75.00 ? 178 TYR A OH 1 ATOM 1387 N N . TRP A 1 179 ? 13.770 49.230 35.796 1.00 69.32 ? 179 TRP A N 1 ATOM 1388 C CA . TRP A 1 179 ? 12.581 48.889 35.022 1.00 60.10 ? 179 TRP A CA 1 ATOM 1389 C C . TRP A 1 179 ? 11.272 49.171 35.753 1.00 59.07 ? 179 TRP A C 1 ATOM 1390 O O . TRP A 1 179 ? 10.264 48.504 35.518 1.00 59.15 ? 179 TRP A O 1 ATOM 1391 C CB . TRP A 1 179 ? 12.646 47.425 34.583 1.00 45.25 ? 179 TRP A CB 1 ATOM 1392 C CG . TRP A 1 179 ? 13.771 47.191 33.628 1.00 44.09 ? 179 TRP A CG 1 ATOM 1393 C CD1 . TRP A 1 179 ? 13.730 47.301 32.269 1.00 41.97 ? 179 TRP A CD1 1 ATOM 1394 C CD2 . TRP A 1 179 ? 15.119 46.841 33.961 1.00 44.45 ? 179 TRP A CD2 1 ATOM 1395 N NE1 . TRP A 1 179 ? 14.966 47.028 31.735 1.00 42.35 ? 179 TRP A NE1 1 ATOM 1396 C CE2 . TRP A 1 179 ? 15.836 46.742 32.754 1.00 44.52 ? 179 TRP A CE2 1 ATOM 1397 C CE3 . TRP A 1 179 ? 15.787 46.590 35.163 1.00 44.05 ? 179 TRP A CE3 1 ATOM 1398 C CZ2 . TRP A 1 179 ? 17.187 46.406 32.715 1.00 46.49 ? 179 TRP A CZ2 1 ATOM 1399 C CZ3 . TRP A 1 179 ? 17.127 46.261 35.123 1.00 45.36 ? 179 TRP A CZ3 1 ATOM 1400 C CH2 . TRP A 1 179 ? 17.813 46.170 33.908 1.00 45.56 ? 179 TRP A CH2 1 ATOM 1401 N N . GLN A 1 180 ? 11.288 50.171 36.629 1.00 53.13 ? 180 GLN A N 1 ATOM 1402 C CA . GLN A 1 180 ? 10.050 50.717 37.165 1.00 47.78 ? 180 GLN A CA 1 ATOM 1403 C C . GLN A 1 180 ? 9.294 51.391 36.033 1.00 46.07 ? 180 GLN A C 1 ATOM 1404 O O . GLN A 1 180 ? 8.068 51.328 35.959 1.00 46.06 ? 180 GLN A O 1 ATOM 1405 C CB . GLN A 1 180 ? 10.318 51.722 38.287 1.00 46.53 ? 180 GLN A CB 1 ATOM 1406 C CG . GLN A 1 180 ? 10.678 51.106 39.622 1.00 47.90 ? 180 GLN A CG 1 ATOM 1407 C CD . GLN A 1 180 ? 10.840 52.150 40.710 1.00 50.73 ? 180 GLN A CD 1 ATOM 1408 O OE1 . GLN A 1 180 ? 10.502 53.318 40.519 1.00 51.29 ? 180 GLN A OE1 1 ATOM 1409 N NE2 . GLN A 1 180 ? 11.360 51.733 41.858 1.00 51.79 ? 180 GLN A NE2 1 ATOM 1410 N N . GLY A 1 181 ? 10.049 52.032 35.148 1.00 44.89 ? 181 GLY A N 1 ATOM 1411 C CA . GLY A 1 181 ? 9.478 52.792 34.056 1.00 43.91 ? 181 GLY A CA 1 ATOM 1412 C C . GLY A 1 181 ? 9.402 54.264 34.405 1.00 54.45 ? 181 GLY A C 1 ATOM 1413 O O . GLY A 1 181 ? 9.441 54.635 35.578 1.00 74.52 ? 181 GLY A O 1 ATOM 1414 N N . GLN A 1 182 ? 9.308 55.109 33.386 1.00 59.53 ? 182 GLN A N 1 ATOM 1415 C CA . GLN A 1 182 ? 9.213 56.545 33.604 1.00 56.36 ? 182 GLN A CA 1 ATOM 1416 C C . GLN A 1 182 ? 8.458 57.227 32.472 1.00 57.00 ? 182 GLN A C 1 ATOM 1417 O O . GLN A 1 182 ? 8.539 56.806 31.320 1.00 43.75 ? 182 GLN A O 1 ATOM 1418 C CB . GLN A 1 182 ? 10.612 57.151 33.743 1.00 46.47 ? 182 GLN A CB 1 ATOM 1419 C CG . GLN A 1 182 ? 10.636 58.631 34.078 1.00 48.23 ? 182 GLN A CG 1 ATOM 1420 C CD . GLN A 1 182 ? 12.043 59.193 34.112 1.00 65.57 ? 182 GLN A CD 1 ATOM 1421 O OE1 . GLN A 1 182 ? 12.979 58.582 33.596 1.00 57.51 ? 182 GLN A OE1 1 ATOM 1422 N NE2 . GLN A 1 182 ? 12.199 60.361 34.724 1.00 89.33 ? 182 GLN A NE2 1 ATOM 1423 N N . LEU A 1 183 ? 7.721 58.279 32.808 1.00 60.13 ? 183 LEU A N 1 ATOM 1424 C CA . LEU A 1 183 ? 7.116 59.138 31.802 1.00 44.63 ? 183 LEU A CA 1 ATOM 1425 C C . LEU A 1 183 ? 7.766 60.510 31.867 1.00 52.00 ? 183 LEU A C 1 ATOM 1426 O O . LEU A 1 183 ? 7.823 61.122 32.930 1.00 67.96 ? 183 LEU A O 1 ATOM 1427 C CB . LEU A 1 183 ? 5.608 59.260 32.009 1.00 43.00 ? 183 LEU A CB 1 ATOM 1428 C CG . LEU A 1 183 ? 4.773 57.984 31.969 1.00 41.72 ? 183 LEU A CG 1 ATOM 1429 C CD1 . LEU A 1 183 ? 3.299 58.347 31.944 1.00 42.85 ? 183 LEU A CD1 1 ATOM 1430 C CD2 . LEU A 1 183 ? 5.146 57.131 30.769 1.00 45.73 ? 183 LEU A CD2 1 ATOM 1431 N N . ILE A 1 184 ? 8.266 60.984 30.732 1.00 45.92 ? 184 ILE A N 1 ATOM 1432 C CA . ILE A 1 184 ? 8.896 62.295 30.671 1.00 54.53 ? 184 ILE A CA 1 ATOM 1433 C C . ILE A 1 184 ? 8.216 63.150 29.611 1.00 59.13 ? 184 ILE A C 1 ATOM 1434 O O . ILE A 1 184 ? 7.980 62.694 28.493 1.00 69.66 ? 184 ILE A O 1 ATOM 1435 C CB . ILE A 1 184 ? 10.402 62.187 30.365 1.00 45.88 ? 184 ILE A CB 1 ATOM 1436 C CG1 . ILE A 1 184 ? 11.066 61.189 31.316 1.00 45.31 ? 184 ILE A CG1 1 ATOM 1437 C CG2 . ILE A 1 184 ? 11.067 63.553 30.465 1.00 67.02 ? 184 ILE A CG2 1 ATOM 1438 C CD1 . ILE A 1 184 ? 12.538 60.976 31.055 1.00 67.13 ? 184 ILE A CD1 1 ATOM 1439 N N . SER A 1 185 ? 7.895 64.389 29.965 1.00 60.63 ? 185 SER A N 1 ATOM 1440 C CA . SER A 1 185 ? 7.185 65.265 29.046 1.00 61.82 ? 185 SER A CA 1 ATOM 1441 C C . SER A 1 185 ? 7.833 66.641 28.939 1.00 64.65 ? 185 SER A C 1 ATOM 1442 O O . SER A 1 185 ? 8.224 67.238 29.943 1.00 68.17 ? 185 SER A O 1 ATOM 1443 C CB . SER A 1 185 ? 5.726 65.409 29.475 1.00 64.13 ? 185 SER A CB 1 ATOM 1444 O OG . SER A 1 185 ? 4.964 66.029 28.457 1.00 62.44 ? 185 SER A OG 1 ATOM 1445 N N . ASP A 1 186 ? 7.938 67.140 27.711 1.00 53.20 ? 186 ASP A N 1 ATOM 1446 C CA . ASP A 1 186 ? 8.564 68.431 27.457 1.00 57.98 ? 186 ASP A CA 1 ATOM 1447 C C . ASP A 1 186 ? 7.827 69.226 26.388 1.00 61.55 ? 186 ASP A C 1 ATOM 1448 O O . ASP A 1 186 ? 7.175 68.657 25.513 1.00 56.13 ? 186 ASP A O 1 ATOM 1449 C CB . ASP A 1 186 ? 10.023 68.244 27.037 1.00 62.48 ? 186 ASP A CB 1 ATOM 1450 C CG . ASP A 1 186 ? 10.905 67.796 28.180 1.00 79.62 ? 186 ASP A CG 1 ATOM 1451 O OD1 . ASP A 1 186 ? 11.405 68.670 28.915 1.00 91.92 ? 186 ASP A OD1 1 ATOM 1452 O OD2 . ASP A 1 186 ? 11.102 66.573 28.343 1.00 87.74 ? 186 ASP A OD2 1 ATOM 1453 N N . GLN A 1 187 ? 7.941 70.547 26.466 1.00 66.39 ? 187 GLN A N 1 ATOM 1454 C CA . GLN A 1 187 ? 7.394 71.426 25.443 1.00 62.07 ? 187 GLN A CA 1 ATOM 1455 C C . GLN A 1 187 ? 8.224 71.304 24.170 1.00 61.32 ? 187 GLN A C 1 ATOM 1456 O O . GLN A 1 187 ? 9.452 71.357 24.223 1.00 61.10 ? 187 GLN A O 1 ATOM 1457 C CB . GLN A 1 187 ? 7.374 72.875 25.932 1.00 67.11 ? 187 GLN A CB 1 ATOM 1458 C CG . GLN A 1 187 ? 6.708 73.067 27.285 1.00 75.62 ? 187 GLN A CG 1 ATOM 1459 C CD . GLN A 1 187 ? 6.878 74.474 27.824 1.00 83.42 ? 187 GLN A CD 1 ATOM 1460 O OE1 . GLN A 1 187 ? 7.579 75.297 27.234 1.00 92.84 ? 187 GLN A OE1 1 ATOM 1461 N NE2 . GLN A 1 187 ? 6.234 74.758 28.950 1.00 85.49 ? 187 GLN A NE2 1 ATOM 1462 N N . VAL A 1 188 ? 7.553 71.134 23.034 1.00 60.72 ? 188 VAL A N 1 ATOM 1463 C CA . VAL A 1 188 ? 8.236 70.982 21.751 1.00 60.76 ? 188 VAL A CA 1 ATOM 1464 C C . VAL A 1 188 ? 9.146 72.169 21.458 1.00 66.85 ? 188 VAL A C 1 ATOM 1465 O O . VAL A 1 188 ? 10.316 71.997 21.115 1.00 63.59 ? 188 VAL A O 1 ATOM 1466 C CB . VAL A 1 188 ? 7.231 70.819 20.593 1.00 60.91 ? 188 VAL A CB 1 ATOM 1467 C CG1 . VAL A 1 188 ? 7.939 70.928 19.250 1.00 61.96 ? 188 VAL A CG1 1 ATOM 1468 C CG2 . VAL A 1 188 ? 6.502 69.491 20.706 1.00 68.89 ? 188 VAL A CG2 1 ATOM 1469 N N . ALA A 1 189 ? 8.602 73.373 21.606 1.00 67.81 ? 189 ALA A N 1 ATOM 1470 C CA . ALA A 1 189 ? 9.364 74.597 21.392 1.00 89.68 ? 189 ALA A CA 1 ATOM 1471 C C . ALA A 1 189 ? 10.558 74.674 22.339 1.00 84.14 ? 189 ALA A C 1 ATOM 1472 O O . ALA A 1 189 ? 11.601 75.227 21.994 1.00 97.47 ? 189 ALA A O 1 ATOM 1473 C CB . ALA A 1 189 ? 8.469 75.813 21.564 1.00 116.05 ? 189 ALA A CB 1 ATOM 1474 N N . GLU A 1 190 ? 10.396 74.113 23.532 1.00 73.13 ? 190 GLU A N 1 ATOM 1475 C CA . GLU A 1 190 ? 11.459 74.104 24.528 1.00 71.24 ? 190 GLU A CA 1 ATOM 1476 C C . GLU A 1 190 ? 12.553 73.110 24.146 1.00 65.97 ? 190 GLU A C 1 ATOM 1477 O O . GLU A 1 190 ? 13.728 73.331 24.432 1.00 66.99 ? 190 GLU A O 1 ATOM 1478 C CB . GLU A 1 190 ? 10.891 73.769 25.910 1.00 73.81 ? 190 GLU A CB 1 ATOM 1479 C CG . GLU A 1 190 ? 11.344 74.704 27.023 1.00 89.50 ? 190 GLU A CG 1 ATOM 1480 C CD . GLU A 1 190 ? 12.675 74.299 27.624 1.00 110.18 ? 190 GLU A CD 1 ATOM 1481 O OE1 . GLU A 1 190 ? 13.341 75.163 28.232 1.00 111.98 ? 190 GLU A OE1 1 ATOM 1482 O OE2 . GLU A 1 190 ? 13.049 73.115 27.496 1.00 127.49 ? 190 GLU A OE2 1 ATOM 1483 N N . ILE A 1 191 ? 12.159 72.018 23.495 1.00 63.32 ? 191 ILE A N 1 ATOM 1484 C CA . ILE A 1 191 ? 13.108 70.996 23.058 1.00 61.50 ? 191 ILE A CA 1 ATOM 1485 C C . ILE A 1 191 ? 14.080 71.542 22.016 1.00 63.51 ? 191 ILE A C 1 ATOM 1486 O O . ILE A 1 191 ? 15.293 71.362 22.130 1.00 90.12 ? 191 ILE A O 1 ATOM 1487 C CB . ILE A 1 191 ? 12.387 69.763 22.470 1.00 64.30 ? 191 ILE A CB 1 ATOM 1488 C CG1 . ILE A 1 191 ? 11.542 69.070 23.541 1.00 68.45 ? 191 ILE A CG1 1 ATOM 1489 C CG2 . ILE A 1 191 ? 13.392 68.783 21.883 1.00 57.49 ? 191 ILE A CG2 1 ATOM 1490 C CD1 . ILE A 1 191 ? 10.764 67.876 23.026 1.00 65.34 ? 191 ILE A CD1 1 ATOM 1491 N N . VAL A 1 192 ? 13.541 72.212 21.003 1.00 65.23 ? 192 VAL A N 1 ATOM 1492 C CA . VAL A 1 192 ? 14.355 72.731 19.909 1.00 67.48 ? 192 VAL A CA 1 ATOM 1493 C C . VAL A 1 192 ? 15.183 73.946 20.340 1.00 82.69 ? 192 VAL A C 1 ATOM 1494 O O . VAL A 1 192 ? 16.349 74.076 19.961 1.00 82.48 ? 192 VAL A O 1 ATOM 1495 C CB . VAL A 1 192 ? 13.473 73.098 18.685 1.00 68.77 ? 192 VAL A CB 1 ATOM 1496 C CG1 . VAL A 1 192 ? 12.256 73.905 19.114 1.00 77.97 ? 192 VAL A CG1 1 ATOM 1497 C CG2 . VAL A 1 192 ? 14.280 73.840 17.629 1.00 76.56 ? 192 VAL A CG2 1 ATOM 1498 N N . SER A 1 193 ? 14.591 74.818 21.150 1.00 71.97 ? 193 SER A N 1 ATOM 1499 C CA . SER A 1 193 ? 15.261 76.046 21.568 1.00 89.85 ? 193 SER A CA 1 ATOM 1500 C C . SER A 1 193 ? 16.417 75.782 22.532 1.00 89.14 ? 193 SER A C 1 ATOM 1501 O O . SER A 1 193 ? 17.390 76.536 22.565 1.00 97.70 ? 193 SER A O 1 ATOM 1502 C CB . SER A 1 193 ? 14.259 77.006 22.216 1.00 77.21 ? 193 SER A CB 1 ATOM 1503 O OG . SER A 1 193 ? 13.706 76.448 23.396 1.00 75.12 ? 193 SER A OG 1 ATOM 1504 N N . LYS A 1 194 ? 16.307 74.712 23.312 1.00 80.46 ? 194 LYS A N 1 ATOM 1505 C CA . LYS A 1 194 ? 17.317 74.393 24.316 1.00 76.24 ? 194 LYS A CA 1 ATOM 1506 C C . LYS A 1 194 ? 18.381 73.426 23.808 1.00 75.77 ? 194 LYS A C 1 ATOM 1507 O O . LYS A 1 194 ? 19.279 73.043 24.557 1.00 79.17 ? 194 LYS A O 1 ATOM 1508 C CB . LYS A 1 194 ? 16.657 73.800 25.564 1.00 69.58 ? 194 LYS A CB 1 ATOM 1509 C CG . LYS A 1 194 ? 16.176 74.824 26.579 1.00 72.67 ? 194 LYS A CG 1 ATOM 1510 C CD . LYS A 1 194 ? 17.342 75.452 27.325 1.00 82.68 ? 194 LYS A CD 1 ATOM 1511 C CE . LYS A 1 194 ? 16.858 76.264 28.516 1.00 97.27 ? 194 LYS A CE 1 ATOM 1512 N NZ . LYS A 1 194 ? 15.909 77.336 28.108 1.00 110.37 ? 194 LYS A NZ 1 ATOM 1513 N N . TYR A 1 195 ? 18.295 73.035 22.541 1.00 69.55 ? 195 TYR A N 1 ATOM 1514 C CA . TYR A 1 195 ? 19.197 72.008 22.031 1.00 69.92 ? 195 TYR A CA 1 ATOM 1515 C C . TYR A 1 195 ? 20.584 72.552 21.712 1.00 70.98 ? 195 TYR A C 1 ATOM 1516 O O . TYR A 1 195 ? 20.744 73.423 20.858 1.00 91.45 ? 195 TYR A O 1 ATOM 1517 C CB . TYR A 1 195 ? 18.611 71.347 20.782 1.00 66.95 ? 195 TYR A CB 1 ATOM 1518 C CG . TYR A 1 195 ? 19.594 70.439 20.079 1.00 66.49 ? 195 TYR A CG 1 ATOM 1519 C CD1 . TYR A 1 195 ? 20.171 70.808 18.871 1.00 68.79 ? 195 TYR A CD1 1 ATOM 1520 C CD2 . TYR A 1 195 ? 19.960 69.221 20.635 1.00 80.67 ? 195 TYR A CD2 1 ATOM 1521 C CE1 . TYR A 1 195 ? 21.076 69.983 18.230 1.00 68.75 ? 195 TYR A CE1 1 ATOM 1522 C CE2 . TYR A 1 195 ? 20.864 68.390 20.003 1.00 82.80 ? 195 TYR A CE2 1 ATOM 1523 C CZ . TYR A 1 195 ? 21.419 68.776 18.801 1.00 85.99 ? 195 TYR A CZ 1 ATOM 1524 O OH . TYR A 1 195 ? 22.320 67.950 18.169 1.00 89.39 ? 195 TYR A OH 1 ATOM 1525 N N . ASP A 1 196 ? 21.584 72.023 22.410 1.00 70.58 ? 196 ASP A N 1 ATOM 1526 C CA . ASP A 1 196 ? 22.981 72.341 22.143 1.00 73.06 ? 196 ASP A CA 1 ATOM 1527 C C . ASP A 1 196 ? 23.744 71.084 21.728 1.00 81.36 ? 196 ASP A C 1 ATOM 1528 O O . ASP A 1 196 ? 23.856 70.140 22.510 1.00 87.19 ? 196 ASP A O 1 ATOM 1529 C CB . ASP A 1 196 ? 23.634 72.983 23.367 1.00 74.79 ? 196 ASP A CB 1 ATOM 1530 C CG . ASP A 1 196 ? 25.023 73.511 23.074 1.00 98.06 ? 196 ASP A CG 1 ATOM 1531 O OD1 . ASP A 1 196 ? 26.000 72.764 23.286 1.00 114.20 ? 196 ASP A OD1 1 ATOM 1532 O OD2 . ASP A 1 196 ? 25.136 74.672 22.628 1.00 106.50 ? 196 ASP A OD2 1 ATOM 1533 N N . PRO A 1 197 ? 24.271 71.069 20.494 1.00 73.08 ? 197 PRO A N 1 ATOM 1534 C CA . PRO A 1 197 ? 24.970 69.901 19.943 1.00 72.24 ? 197 PRO A CA 1 ATOM 1535 C C . PRO A 1 197 ? 26.231 69.531 20.722 1.00 87.79 ? 197 PRO A C 1 ATOM 1536 O O . PRO A 1 197 ? 26.714 68.403 20.609 1.00 95.25 ? 197 PRO A O 1 ATOM 1537 C CB . PRO A 1 197 ? 25.324 70.347 18.521 1.00 74.86 ? 197 PRO A CB 1 ATOM 1538 C CG . PRO A 1 197 ? 25.378 71.831 18.598 1.00 96.79 ? 197 PRO A CG 1 ATOM 1539 C CD . PRO A 1 197 ? 24.309 72.218 19.575 1.00 86.12 ? 197 PRO A CD 1 ATOM 1540 N N . ASN A 1 198 ? 26.754 70.472 21.499 1.00 74.95 ? 198 ASN A N 1 ATOM 1541 C CA . ASN A 1 198 ? 27.947 70.231 22.301 1.00 75.99 ? 198 ASN A CA 1 ATOM 1542 C C . ASN A 1 198 ? 27.613 69.783 23.722 1.00 73.94 ? 198 ASN A C 1 ATOM 1543 O O . ASN A 1 198 ? 28.500 69.654 24.562 1.00 87.88 ? 198 ASN A O 1 ATOM 1544 C CB . ASN A 1 198 ? 28.823 71.484 22.340 1.00 81.76 ? 198 ASN A CB 1 ATOM 1545 C CG . ASN A 1 198 ? 29.351 71.866 20.972 1.00 95.13 ? 198 ASN A CG 1 ATOM 1546 O OD1 . ASN A 1 198 ? 29.522 71.014 20.100 1.00 107.76 ? 198 ASN A OD1 1 ATOM 1547 N ND2 . ASN A 1 198 ? 29.613 73.153 20.776 1.00 96.18 ? 198 ASN A ND2 1 ATOM 1548 N N . VAL A 1 199 ? 26.331 69.569 23.995 1.00 71.39 ? 199 VAL A N 1 ATOM 1549 C CA . VAL A 1 199 ? 25.905 69.106 25.312 1.00 75.38 ? 199 VAL A CA 1 ATOM 1550 C C . VAL A 1 199 ? 25.050 67.844 25.205 1.00 66.09 ? 199 VAL A C 1 ATOM 1551 O O . VAL A 1 199 ? 23.954 67.870 24.644 1.00 71.81 ? 199 VAL A O 1 ATOM 1552 C CB . VAL A 1 199 ? 25.119 70.196 26.064 1.00 89.17 ? 199 VAL A CB 1 ATOM 1553 C CG1 . VAL A 1 199 ? 24.555 69.642 27.357 1.00 103.77 ? 199 VAL A CG1 1 ATOM 1554 C CG2 . VAL A 1 199 ? 26.012 71.398 26.340 1.00 83.19 ? 199 VAL A CG2 1 ATOM 1555 N N . TYR A 1 200 ? 25.561 66.743 25.750 1.00 77.50 ? 200 TYR A N 1 ATOM 1556 C CA . TYR A 1 200 ? 24.911 65.441 25.624 1.00 74.41 ? 200 TYR A CA 1 ATOM 1557 C C . TYR A 1 200 ? 23.750 65.264 26.599 1.00 78.10 ? 200 TYR A C 1 ATOM 1558 O O . TYR A 1 200 ? 22.755 64.616 26.275 1.00 75.23 ? 200 TYR A O 1 ATOM 1559 C CB . TYR A 1 200 ? 25.937 64.323 25.819 1.00 65.42 ? 200 TYR A CB 1 ATOM 1560 C CG . TYR A 1 200 ? 27.139 64.461 24.916 1.00 65.48 ? 200 TYR A CG 1 ATOM 1561 C CD1 . TYR A 1 200 ? 27.014 64.324 23.540 1.00 64.43 ? 200 TYR A CD1 1 ATOM 1562 C CD2 . TYR A 1 200 ? 28.398 64.733 25.436 1.00 77.74 ? 200 TYR A CD2 1 ATOM 1563 C CE1 . TYR A 1 200 ? 28.107 64.455 22.708 1.00 66.90 ? 200 TYR A CE1 1 ATOM 1564 C CE2 . TYR A 1 200 ? 29.499 64.864 24.611 1.00 69.13 ? 200 TYR A CE2 1 ATOM 1565 C CZ . TYR A 1 200 ? 29.346 64.725 23.246 1.00 71.16 ? 200 TYR A CZ 1 ATOM 1566 O OH . TYR A 1 200 ? 30.437 64.850 22.416 1.00 72.32 ? 200 TYR A OH 1 ATOM 1567 N N . SER A 1 201 ? 23.882 65.832 27.793 1.00 76.05 ? 201 SER A N 1 ATOM 1568 C CA . SER A 1 201 ? 22.793 65.807 28.762 1.00 67.54 ? 201 SER A CA 1 ATOM 1569 C C . SER A 1 201 ? 22.191 67.199 28.893 1.00 74.26 ? 201 SER A C 1 ATOM 1570 O O . SER A 1 201 ? 22.798 68.094 29.476 1.00 86.93 ? 201 SER A O 1 ATOM 1571 C CB . SER A 1 201 ? 23.287 65.310 30.122 1.00 65.31 ? 201 SER A CB 1 ATOM 1572 O OG . SER A 1 201 ? 23.893 64.034 30.009 1.00 69.60 ? 201 SER A OG 1 ATOM 1573 N N . ILE A 1 202 ? 20.983 67.369 28.366 1.00 82.38 ? 202 ILE A N 1 ATOM 1574 C CA . ILE A 1 202 ? 20.375 68.691 28.278 1.00 80.24 ? 202 ILE A CA 1 ATOM 1575 C C . ILE A 1 202 ? 19.241 68.880 29.276 1.00 76.28 ? 202 ILE A C 1 ATOM 1576 O O . ILE A 1 202 ? 18.249 68.152 29.255 1.00 75.34 ? 202 ILE A O 1 ATOM 1577 C CB . ILE A 1 202 ? 19.841 68.961 26.859 1.00 73.35 ? 202 ILE A CB 1 ATOM 1578 C CG1 . ILE A 1 202 ? 20.985 68.905 25.845 1.00 69.08 ? 202 ILE A CG1 1 ATOM 1579 C CG2 . ILE A 1 202 ? 19.137 70.308 26.801 1.00 71.61 ? 202 ILE A CG2 1 ATOM 1580 C CD1 . ILE A 1 202 ? 20.540 69.063 24.408 1.00 79.80 ? 202 ILE A CD1 1 ATOM 1581 N N . LYS A 1 203 ? 19.397 69.870 30.149 1.00 85.20 ? 203 LYS A N 1 ATOM 1582 C CA . LYS A 1 203 ? 18.365 70.209 31.118 1.00 86.40 ? 203 LYS A CA 1 ATOM 1583 C C . LYS A 1 203 ? 17.277 71.053 30.464 1.00 81.22 ? 203 LYS A C 1 ATOM 1584 O O . LYS A 1 203 ? 17.545 72.137 29.944 1.00 93.34 ? 203 LYS A O 1 ATOM 1585 C CB . LYS A 1 203 ? 18.978 70.947 32.311 1.00 100.71 ? 203 LYS A CB 1 ATOM 1586 C CG . LYS A 1 203 ? 20.045 71.963 31.929 1.00 101.93 ? 203 LYS A CG 1 ATOM 1587 C CD . LYS A 1 203 ? 20.742 72.533 33.154 1.00 99.50 ? 203 LYS A CD 1 ATOM 1588 C CE . LYS A 1 203 ? 21.879 73.462 32.756 1.00 99.66 ? 203 LYS A CE 1 ATOM 1589 N NZ . LYS A 1 203 ? 22.592 74.016 33.940 1.00 91.06 ? 203 LYS A NZ 1 ATOM 1590 N N . TYR A 1 204 ? 16.049 70.547 30.488 1.00 75.37 ? 204 TYR A N 1 ATOM 1591 C CA . TYR A 1 204 ? 14.923 71.252 29.892 1.00 83.91 ? 204 TYR A CA 1 ATOM 1592 C C . TYR A 1 204 ? 14.037 71.879 30.960 1.00 91.90 ? 204 TYR A C 1 ATOM 1593 O O . TYR A 1 204 ? 13.671 71.226 31.938 1.00 105.17 ? 204 TYR A O 1 ATOM 1594 C CB . TYR A 1 204 ? 14.089 70.308 29.023 1.00 73.88 ? 204 TYR A CB 1 ATOM 1595 C CG . TYR A 1 204 ? 14.806 69.766 27.808 1.00 63.35 ? 204 TYR A CG 1 ATOM 1596 C CD1 . TYR A 1 204 ? 15.380 68.501 27.824 1.00 65.94 ? 204 TYR A CD1 1 ATOM 1597 C CD2 . TYR A 1 204 ? 14.900 70.514 26.642 1.00 63.79 ? 204 TYR A CD2 1 ATOM 1598 C CE1 . TYR A 1 204 ? 16.033 67.999 26.714 1.00 71.20 ? 204 TYR A CE1 1 ATOM 1599 C CE2 . TYR A 1 204 ? 15.552 70.020 25.527 1.00 71.78 ? 204 TYR A CE2 1 ATOM 1600 C CZ . TYR A 1 204 ? 16.116 68.763 25.569 1.00 76.37 ? 204 TYR A CZ 1 ATOM 1601 O OH . TYR A 1 204 ? 16.765 68.267 24.461 1.00 79.62 ? 204 TYR A OH 1 ATOM 1602 N N . ASN A 1 205 ? 13.694 73.148 30.770 1.00 71.98 ? 205 ASN A N 1 ATOM 1603 C CA . ASN A 1 205 ? 12.758 73.818 31.660 1.00 74.68 ? 205 ASN A CA 1 ATOM 1604 C C . ASN A 1 205 ? 11.332 73.363 31.377 1.00 71.83 ? 205 ASN A C 1 ATOM 1605 O O . ASN A 1 205 ? 11.013 72.965 30.255 1.00 77.80 ? 205 ASN A O 1 ATOM 1606 C CB . ASN A 1 205 ? 12.875 75.336 31.522 1.00 86.50 ? 205 ASN A CB 1 ATOM 1607 C CG . ASN A 1 205 ? 14.202 75.865 32.029 1.00 94.15 ? 205 ASN A CG 1 ATOM 1608 O OD1 . ASN A 1 205 ? 14.737 75.377 33.025 1.00 95.20 ? 205 ASN A OD1 1 ATOM 1609 N ND2 . ASN A 1 205 ? 14.741 76.866 31.344 1.00 106.82 ? 205 ASN A ND2 1 ATOM 1610 N N . ASN A 1 206 ? 10.486 73.423 32.403 1.00 73.06 ? 206 ASN A N 1 ATOM 1611 C CA . ASN A 1 206 ? 9.100 72.968 32.317 1.00 81.21 ? 206 ASN A CA 1 ATOM 1612 C C . ASN A 1 206 ? 8.997 71.504 31.897 1.00 79.34 ? 206 ASN A C 1 ATOM 1613 O O . ASN A 1 206 ? 8.123 71.137 31.112 1.00 75.85 ? 206 ASN A O 1 ATOM 1614 C CB . ASN A 1 206 ? 8.300 73.840 31.345 1.00 79.54 ? 206 ASN A CB 1 ATOM 1615 C CG . ASN A 1 206 ? 8.590 75.318 31.511 1.00 95.90 ? 206 ASN A CG 1 ATOM 1616 O OD1 . ASN A 1 206 ? 8.025 75.981 32.380 1.00 118.27 ? 206 ASN A OD1 1 ATOM 1617 N ND2 . ASN A 1 206 ? 9.473 75.844 30.669 1.00 94.31 ? 206 ASN A ND2 1 ATOM 1618 N N . GLN A 1 207 ? 9.896 70.673 32.415 1.00 69.41 ? 207 GLN A N 1 ATOM 1619 C CA . GLN A 1 207 ? 9.847 69.243 32.135 1.00 67.14 ? 207 GLN A CA 1 ATOM 1620 C C . GLN A 1 207 ? 9.024 68.510 33.185 1.00 68.33 ? 207 GLN A C 1 ATOM 1621 O O . GLN A 1 207 ? 9.242 68.671 34.386 1.00 74.48 ? 207 GLN A O 1 ATOM 1622 C CB . GLN A 1 207 ? 11.255 68.645 32.069 1.00 75.72 ? 207 GLN A CB 1 ATOM 1623 C CG . GLN A 1 207 ? 11.258 67.139 31.823 1.00 77.87 ? 207 GLN A CG 1 ATOM 1624 C CD . GLN A 1 207 ? 12.646 66.578 31.581 1.00 71.71 ? 207 GLN A CD 1 ATOM 1625 O OE1 . GLN A 1 207 ? 13.251 65.981 32.471 1.00 72.68 ? 207 GLN A OE1 1 ATOM 1626 N NE2 . GLN A 1 207 ? 13.153 66.757 30.366 1.00 71.48 ? 207 GLN A NE2 1 ATOM 1627 N N . LEU A 1 208 ? 8.075 67.706 32.722 1.00 56.99 ? 208 LEU A N 1 ATOM 1628 C CA . LEU A 1 208 ? 7.257 66.894 33.610 1.00 57.26 ? 208 LEU A CA 1 ATOM 1629 C C . LEU A 1 208 ? 7.692 65.437 33.534 1.00 67.23 ? 208 LEU A C 1 ATOM 1630 O O . LEU A 1 208 ? 7.552 64.792 32.495 1.00 79.39 ? 208 LEU A O 1 ATOM 1631 C CB . LEU A 1 208 ? 5.777 67.025 33.251 1.00 56.13 ? 208 LEU A CB 1 ATOM 1632 C CG . LEU A 1 208 ? 5.197 68.440 33.271 1.00 59.21 ? 208 LEU A CG 1 ATOM 1633 C CD1 . LEU A 1 208 ? 3.794 68.441 32.693 1.00 59.16 ? 208 LEU A CD1 1 ATOM 1634 C CD2 . LEU A 1 208 ? 5.196 69.000 34.684 1.00 61.96 ? 208 LEU A CD2 1 ATOM 1635 N N . ALA A 1 209 ? 8.225 64.921 34.636 1.00 68.33 ? 209 ALA A N 1 ATOM 1636 C CA . ALA A 1 209 ? 8.712 63.549 34.662 1.00 62.72 ? 209 ALA A CA 1 ATOM 1637 C C . ALA A 1 209 ? 8.399 62.859 35.983 1.00 62.14 ? 209 ALA A C 1 ATOM 1638 O O . ALA A 1 209 ? 8.414 63.486 37.043 1.00 69.32 ? 209 ALA A O 1 ATOM 1639 C CB . ALA A 1 209 ? 10.209 63.518 34.393 1.00 59.47 ? 209 ALA A CB 1 ATOM 1640 N N . THR A 1 210 ? 8.112 61.563 35.910 1.00 52.59 ? 210 THR A N 1 ATOM 1641 C CA . THR A 1 210 ? 7.894 60.763 37.107 1.00 55.28 ? 210 THR A CA 1 ATOM 1642 C C . THR A 1 210 ? 9.234 60.443 37.755 1.00 56.63 ? 210 THR A C 1 ATOM 1643 O O . THR A 1 210 ? 10.245 60.303 37.067 1.00 69.12 ? 210 THR A O 1 ATOM 1644 C CB . THR A 1 210 ? 7.149 59.451 36.795 1.00 54.96 ? 210 THR A CB 1 ATOM 1645 O OG1 . THR A 1 210 ? 8.032 58.540 36.129 1.00 53.20 ? 210 THR A OG1 1 ATOM 1646 C CG2 . THR A 1 210 ? 5.939 59.719 35.916 1.00 55.29 ? 210 THR A CG2 1 ATOM 1647 N N . ARG A 1 211 ? 9.241 60.331 39.077 1.00 59.29 ? 211 ARG A N 1 ATOM 1648 C CA . ARG A 1 211 ? 10.471 60.044 39.804 1.00 70.20 ? 211 ARG A CA 1 ATOM 1649 C C . ARG A 1 211 ? 10.596 58.555 40.101 1.00 64.51 ? 211 ARG A C 1 ATOM 1650 O O . ARG A 1 211 ? 9.715 57.768 39.757 1.00 73.28 ? 211 ARG A O 1 ATOM 1651 C CB . ARG A 1 211 ? 10.520 60.846 41.106 1.00 91.46 ? 211 ARG A CB 1 ATOM 1652 C CG . ARG A 1 211 ? 10.463 62.351 40.908 1.00 97.21 ? 211 ARG A CG 1 ATOM 1653 C CD . ARG A 1 211 ? 10.394 63.081 42.238 1.00 99.54 ? 211 ARG A CD 1 ATOM 1654 N NE . ARG A 1 211 ? 9.171 62.766 42.971 1.00 107.06 ? 211 ARG A NE 1 ATOM 1655 C CZ . ARG A 1 211 ? 8.865 63.268 44.163 1.00 121.33 ? 211 ARG A CZ 1 ATOM 1656 N NH1 . ARG A 1 211 ? 9.695 64.111 44.761 1.00 129.11 ? 211 ARG A NH1 1 ATOM 1657 N NH2 . ARG A 1 211 ? 7.730 62.927 44.757 1.00 123.44 ? 211 ARG A NH2 1 ATOM 1658 N N . THR A 1 212 ? 11.696 58.174 40.741 1.00 57.92 ? 212 THR A N 1 ATOM 1659 C CA . THR A 1 212 ? 11.879 56.795 41.168 1.00 57.86 ? 212 THR A CA 1 ATOM 1660 C C . THR A 1 212 ? 10.940 56.490 42.328 1.00 62.05 ? 212 THR A C 1 ATOM 1661 O O . THR A 1 212 ? 10.474 57.399 43.015 1.00 72.33 ? 212 THR A O 1 ATOM 1662 C CB . THR A 1 212 ? 13.333 56.514 41.591 1.00 63.58 ? 212 THR A CB 1 ATOM 1663 O OG1 . THR A 1 212 ? 13.453 55.155 42.030 1.00 66.80 ? 212 THR A OG1 1 ATOM 1664 C CG2 . THR A 1 212 ? 13.749 57.445 42.719 1.00 75.63 ? 212 THR A CG2 1 ATOM 1665 N N . ALA A 1 213 ? 10.654 55.211 42.536 1.00 61.03 ? 213 ALA A N 1 ATOM 1666 C CA . ALA A 1 213 ? 9.767 54.797 43.614 1.00 60.65 ? 213 ALA A CA 1 ATOM 1667 C C . ALA A 1 213 ? 10.417 53.705 44.447 1.00 60.30 ? 213 ALA A C 1 ATOM 1668 O O . ALA A 1 213 ? 11.586 53.375 44.245 1.00 56.06 ? 213 ALA A O 1 ATOM 1669 C CB . ALA A 1 213 ? 8.438 54.320 43.056 1.00 60.20 ? 213 ALA A CB 1 ATOM 1670 N N . GLN A 1 214 ? 9.658 53.154 45.389 1.00 61.84 ? 214 GLN A N 1 ATOM 1671 C CA . GLN A 1 214 ? 10.135 52.039 46.197 1.00 62.64 ? 214 GLN A CA 1 ATOM 1672 C C . GLN A 1 214 ? 10.448 50.848 45.299 1.00 73.39 ? 214 GLN A C 1 ATOM 1673 O O . GLN A 1 214 ? 9.839 50.684 44.241 1.00 70.60 ? 214 GLN A O 1 ATOM 1674 C CB . GLN A 1 214 ? 9.105 51.648 47.260 1.00 70.53 ? 214 GLN A CB 1 ATOM 1675 C CG . GLN A 1 214 ? 8.837 52.714 48.314 1.00 78.17 ? 214 GLN A CG 1 ATOM 1676 C CD . GLN A 1 214 ? 7.826 53.753 47.864 1.00 74.76 ? 214 GLN A CD 1 ATOM 1677 O OE1 . GLN A 1 214 ? 7.448 53.804 46.694 1.00 68.57 ? 214 GLN A OE1 1 ATOM 1678 N NE2 . GLN A 1 214 ? 7.377 54.584 48.798 1.00 79.65 ? 214 GLN A NE2 1 ATOM 1679 N N . ALA A 1 215 ? 11.398 50.021 45.725 1.00 78.00 ? 215 ALA A N 1 ATOM 1680 C CA . ALA A 1 215 ? 11.844 48.884 44.924 1.00 59.94 ? 215 ALA A CA 1 ATOM 1681 C C . ALA A 1 215 ? 10.731 47.865 44.695 1.00 57.75 ? 215 ALA A C 1 ATOM 1682 O O . ALA A 1 215 ? 10.844 46.998 43.830 1.00 66.21 ? 215 ALA A O 1 ATOM 1683 C CB . ALA A 1 215 ? 13.037 48.216 45.581 1.00 62.88 ? 215 ALA A CB 1 ATOM 1684 N N . ILE A 1 216 ? 9.657 47.975 45.470 1.00 58.30 ? 216 ILE A N 1 ATOM 1685 C CA . ILE A 1 216 ? 8.488 47.121 45.301 1.00 58.39 ? 216 ILE A CA 1 ATOM 1686 C C . ILE A 1 216 ? 7.891 47.308 43.908 1.00 57.86 ? 216 ILE A C 1 ATOM 1687 O O . ILE A 1 216 ? 7.275 46.398 43.353 1.00 66.46 ? 216 ILE A O 1 ATOM 1688 C CB . ILE A 1 216 ? 7.413 47.424 46.364 1.00 61.62 ? 216 ILE A CB 1 ATOM 1689 C CG1 . ILE A 1 216 ? 8.057 47.605 47.742 1.00 87.93 ? 216 ILE A CG1 1 ATOM 1690 C CG2 . ILE A 1 216 ? 6.356 46.328 46.394 1.00 60.25 ? 216 ILE A CG2 1 ATOM 1691 C CD1 . ILE A 1 216 ? 8.805 46.384 48.240 1.00 98.83 ? 216 ILE A CD1 1 ATOM 1692 N N . PHE A 1 217 ? 8.095 48.495 43.345 1.00 69.09 ? 217 PHE A N 1 ATOM 1693 C CA . PHE A 1 217 ? 7.545 48.846 42.040 1.00 63.76 ? 217 PHE A CA 1 ATOM 1694 C C . PHE A 1 217 ? 8.493 48.509 40.890 1.00 59.13 ? 217 PHE A C 1 ATOM 1695 O O . PHE A 1 217 ? 8.211 48.835 39.736 1.00 59.18 ? 217 PHE A O 1 ATOM 1696 C CB . PHE A 1 217 ? 7.193 50.334 42.002 1.00 55.10 ? 217 PHE A CB 1 ATOM 1697 C CG . PHE A 1 217 ? 6.119 50.728 42.976 1.00 60.13 ? 217 PHE A CG 1 ATOM 1698 C CD1 . PHE A 1 217 ? 4.782 50.623 42.632 1.00 55.28 ? 217 PHE A CD1 1 ATOM 1699 C CD2 . PHE A 1 217 ? 6.447 51.204 44.235 1.00 73.58 ? 217 PHE A CD2 1 ATOM 1700 C CE1 . PHE A 1 217 ? 3.791 50.985 43.525 1.00 57.04 ? 217 PHE A CE1 1 ATOM 1701 C CE2 . PHE A 1 217 ? 5.460 51.568 45.133 1.00 77.37 ? 217 PHE A CE2 1 ATOM 1702 C CZ . PHE A 1 217 ? 4.130 51.459 44.777 1.00 63.25 ? 217 PHE A CZ 1 ATOM 1703 N N . ASP A 1 218 ? 9.615 47.868 41.204 1.00 56.12 ? 218 ASP A N 1 ATOM 1704 C CA . ASP A 1 218 ? 10.586 47.485 40.180 1.00 56.71 ? 218 ASP A CA 1 ATOM 1705 C C . ASP A 1 218 ? 9.993 46.506 39.174 1.00 62.95 ? 218 ASP A C 1 ATOM 1706 O O . ASP A 1 218 ? 9.063 45.763 39.491 1.00 84.92 ? 218 ASP A O 1 ATOM 1707 C CB . ASP A 1 218 ? 11.834 46.867 40.813 1.00 59.96 ? 218 ASP A CB 1 ATOM 1708 C CG . ASP A 1 218 ? 12.719 47.894 41.482 1.00 68.42 ? 218 ASP A CG 1 ATOM 1709 O OD1 . ASP A 1 218 ? 13.395 47.536 42.466 1.00 65.28 ? 218 ASP A OD1 1 ATOM 1710 O OD2 . ASP A 1 218 ? 12.745 49.055 41.023 1.00 86.24 ? 218 ASP A OD2 1 ATOM 1711 N N . ASP A 1 219 ? 10.541 46.528 37.960 1.00 53.61 ? 219 ASP A N 1 ATOM 1712 C CA . ASP A 1 219 ? 10.129 45.634 36.880 1.00 52.82 ? 219 ASP A CA 1 ATOM 1713 C C . ASP A 1 219 ? 8.649 45.792 36.549 1.00 59.34 ? 219 ASP A C 1 ATOM 1714 O O . ASP A 1 219 ? 7.985 44.827 36.178 1.00 73.92 ? 219 ASP A O 1 ATOM 1715 C CB . ASP A 1 219 ? 10.434 44.176 37.238 1.00 56.31 ? 219 ASP A CB 1 ATOM 1716 C CG . ASP A 1 219 ? 11.835 43.993 37.786 1.00 66.12 ? 219 ASP A CG 1 ATOM 1717 O OD1 . ASP A 1 219 ? 12.786 43.917 36.981 1.00 73.80 ? 219 ASP A OD1 1 ATOM 1718 O OD2 . ASP A 1 219 ? 11.986 43.930 39.024 1.00 75.05 ? 219 ASP A OD2 1 ATOM 1719 N N . SER A 1 220 ? 8.135 47.009 36.701 1.00 50.61 ? 220 SER A N 1 ATOM 1720 C CA . SER A 1 220 ? 6.751 47.305 36.346 1.00 49.46 ? 220 SER A CA 1 ATOM 1721 C C . SER A 1 220 ? 6.597 47.547 34.846 1.00 54.29 ? 220 SER A C 1 ATOM 1722 O O . SER A 1 220 ? 5.547 47.256 34.272 1.00 71.44 ? 220 SER A O 1 ATOM 1723 C CB . SER A 1 220 ? 6.244 48.518 37.128 1.00 50.27 ? 220 SER A CB 1 ATOM 1724 O OG . SER A 1 220 ? 6.125 48.222 38.509 1.00 51.37 ? 220 SER A OG 1 ATOM 1725 N N . TYR A 1 221 ? 7.659 48.058 34.224 1.00 52.80 ? 221 TYR A N 1 ATOM 1726 C CA . TYR A 1 221 ? 7.662 48.453 32.812 1.00 47.53 ? 221 TYR A CA 1 ATOM 1727 C C . TYR A 1 221 ? 6.673 49.579 32.506 1.00 51.48 ? 221 TYR A C 1 ATOM 1728 O O . TYR A 1 221 ? 5.887 49.476 31.565 1.00 62.55 ? 221 TYR A O 1 ATOM 1729 C CB . TYR A 1 221 ? 7.355 47.258 31.897 1.00 41.81 ? 221 TYR A CB 1 ATOM 1730 C CG . TYR A 1 221 ? 8.463 46.236 31.771 1.00 41.68 ? 221 TYR A CG 1 ATOM 1731 C CD1 . TYR A 1 221 ? 8.326 45.144 30.923 1.00 41.65 ? 221 TYR A CD1 1 ATOM 1732 C CD2 . TYR A 1 221 ? 9.641 46.356 32.497 1.00 56.32 ? 221 TYR A CD2 1 ATOM 1733 C CE1 . TYR A 1 221 ? 9.330 44.204 30.798 1.00 62.10 ? 221 TYR A CE1 1 ATOM 1734 C CE2 . TYR A 1 221 ? 10.651 45.417 32.380 1.00 66.16 ? 221 TYR A CE2 1 ATOM 1735 C CZ . TYR A 1 221 ? 10.489 44.343 31.528 1.00 66.68 ? 221 TYR A CZ 1 ATOM 1736 O OH . TYR A 1 221 ? 11.490 43.405 31.404 1.00 63.44 ? 221 TYR A OH 1 ATOM 1737 N N . LEU A 1 222 ? 6.710 50.647 33.298 1.00 51.49 ? 222 LEU A N 1 ATOM 1738 C CA . LEU A 1 222 ? 5.902 51.831 33.007 1.00 53.94 ? 222 LEU A CA 1 ATOM 1739 C C . LEU A 1 222 ? 6.394 52.510 31.736 1.00 53.66 ? 222 LEU A C 1 ATOM 1740 O O . LEU A 1 222 ? 7.596 52.620 31.510 1.00 62.18 ? 222 LEU A O 1 ATOM 1741 C CB . LEU A 1 222 ? 5.931 52.818 34.178 1.00 51.72 ? 222 LEU A CB 1 ATOM 1742 C CG . LEU A 1 222 ? 5.392 54.228 33.910 1.00 50.36 ? 222 LEU A CG 1 ATOM 1743 C CD1 . LEU A 1 222 ? 3.903 54.195 33.593 1.00 51.66 ? 222 LEU A CD1 1 ATOM 1744 C CD2 . LEU A 1 222 ? 5.674 55.156 35.082 1.00 51.70 ? 222 LEU A CD2 1 ATOM 1745 N N . GLY A 1 223 ? 5.463 52.961 30.904 1.00 48.62 ? 223 GLY A N 1 ATOM 1746 C CA . GLY A 1 223 ? 5.821 53.634 29.671 1.00 51.74 ? 223 GLY A CA 1 ATOM 1747 C C . GLY A 1 223 ? 6.002 52.660 28.525 1.00 49.46 ? 223 GLY A C 1 ATOM 1748 O O . GLY A 1 223 ? 6.602 52.994 27.503 1.00 46.89 ? 223 GLY A O 1 ATOM 1749 N N . TYR A 1 224 ? 5.489 51.448 28.705 1.00 50.72 ? 224 TYR A N 1 ATOM 1750 C CA . TYR A 1 224 ? 5.501 50.441 27.653 1.00 40.39 ? 224 TYR A CA 1 ATOM 1751 C C . TYR A 1 224 ? 4.677 50.942 26.474 1.00 38.12 ? 224 TYR A C 1 ATOM 1752 O O . TYR A 1 224 ? 5.034 50.738 25.314 1.00 46.34 ? 224 TYR A O 1 ATOM 1753 C CB . TYR A 1 224 ? 4.948 49.115 28.176 1.00 46.67 ? 224 TYR A CB 1 ATOM 1754 C CG . TYR A 1 224 ? 5.283 47.910 27.329 1.00 49.71 ? 224 TYR A CG 1 ATOM 1755 C CD1 . TYR A 1 224 ? 6.294 47.036 27.704 1.00 52.66 ? 224 TYR A CD1 1 ATOM 1756 C CD2 . TYR A 1 224 ? 4.583 47.640 26.160 1.00 39.77 ? 224 TYR A CD2 1 ATOM 1757 C CE1 . TYR A 1 224 ? 6.601 45.930 26.938 1.00 44.49 ? 224 TYR A CE1 1 ATOM 1758 C CE2 . TYR A 1 224 ? 4.886 46.538 25.388 1.00 37.76 ? 224 TYR A CE2 1 ATOM 1759 C CZ . TYR A 1 224 ? 5.894 45.687 25.781 1.00 40.04 ? 224 TYR A CZ 1 ATOM 1760 O OH . TYR A 1 224 ? 6.197 44.586 25.015 1.00 55.52 ? 224 TYR A OH 1 ATOM 1761 N N . SER A 1 225 ? 3.570 51.604 26.794 1.00 39.02 ? 225 SER A N 1 ATOM 1762 C CA . SER A 1 225 ? 2.711 52.229 25.799 1.00 54.11 ? 225 SER A CA 1 ATOM 1763 C C . SER A 1 225 ? 2.079 53.478 26.400 1.00 57.67 ? 225 SER A C 1 ATOM 1764 O O . SER A 1 225 ? 1.805 53.519 27.599 1.00 58.94 ? 225 SER A O 1 ATOM 1765 C CB . SER A 1 225 ? 1.632 51.258 25.320 1.00 70.37 ? 225 SER A CB 1 ATOM 1766 O OG . SER A 1 225 ? 0.798 50.856 26.393 1.00 71.60 ? 225 SER A OG 1 ATOM 1767 N N . VAL A 1 226 ? 1.856 54.496 25.574 1.00 62.23 ? 226 VAL A N 1 ATOM 1768 C CA . VAL A 1 226 ? 1.279 55.747 26.058 1.00 48.01 ? 226 VAL A CA 1 ATOM 1769 C C . VAL A 1 226 ? 0.199 56.293 25.130 1.00 46.54 ? 226 VAL A C 1 ATOM 1770 O O . VAL A 1 226 ? 0.132 55.938 23.953 1.00 44.34 ? 226 VAL A O 1 ATOM 1771 C CB . VAL A 1 226 ? 2.358 56.837 26.242 1.00 41.37 ? 226 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 226 ? 3.312 56.468 27.367 1.00 51.75 ? 226 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 226 ? 3.110 57.066 24.940 1.00 43.78 ? 226 VAL A CG2 1 ATOM 1774 N N . ALA A 1 227 ? -0.646 57.159 25.680 1.00 44.99 ? 227 ALA A N 1 ATOM 1775 C CA . ALA A 1 227 ? -1.682 57.842 24.916 1.00 46.63 ? 227 ALA A CA 1 ATOM 1776 C C . ALA A 1 227 ? -2.069 59.132 25.629 1.00 53.46 ? 227 ALA A C 1 ATOM 1777 O O . ALA A 1 227 ? -1.799 59.291 26.820 1.00 68.46 ? 227 ALA A O 1 ATOM 1778 C CB . ALA A 1 227 ? -2.895 56.946 24.728 1.00 51.41 ? 227 ALA A CB 1 ATOM 1779 N N . VAL A 1 228 ? -2.699 60.052 24.906 1.00 55.09 ? 228 VAL A N 1 ATOM 1780 C CA . VAL A 1 228 ? -3.061 61.343 25.484 1.00 52.08 ? 228 VAL A CA 1 ATOM 1781 C C . VAL A 1 228 ? -4.563 61.618 25.399 1.00 55.81 ? 228 VAL A C 1 ATOM 1782 O O . VAL A 1 228 ? -5.240 61.170 24.475 1.00 59.23 ? 228 VAL A O 1 ATOM 1783 C CB . VAL A 1 228 ? -2.299 62.493 24.798 1.00 51.09 ? 228 VAL A CB 1 ATOM 1784 C CG1 . VAL A 1 228 ? -0.812 62.406 25.111 1.00 47.52 ? 228 VAL A CG1 1 ATOM 1785 C CG2 . VAL A 1 228 ? -2.536 62.465 23.296 1.00 71.74 ? 228 VAL A CG2 1 ATOM 1786 N N . GLY A 1 229 ? -5.068 62.358 26.382 1.00 57.57 ? 229 GLY A N 1 ATOM 1787 C CA . GLY A 1 229 ? -6.470 62.733 26.452 1.00 62.47 ? 229 GLY A CA 1 ATOM 1788 C C . GLY A 1 229 ? -6.708 63.514 27.729 1.00 68.41 ? 229 GLY A C 1 ATOM 1789 O O . GLY A 1 229 ? -5.891 63.455 28.642 1.00 79.93 ? 229 GLY A O 1 ATOM 1790 N N . ASP A 1 230 ? -7.815 64.245 27.810 1.00 72.42 ? 230 ASP A N 1 ATOM 1791 C CA . ASP A 1 230 ? -8.048 65.082 28.985 1.00 76.86 ? 230 ASP A CA 1 ATOM 1792 C C . ASP A 1 230 ? -9.202 64.618 29.880 1.00 79.72 ? 230 ASP A C 1 ATOM 1793 O O . ASP A 1 230 ? -10.371 64.692 29.498 1.00 90.16 ? 230 ASP A O 1 ATOM 1794 C CB . ASP A 1 230 ? -8.293 66.521 28.563 1.00 90.77 ? 230 ASP A CB 1 ATOM 1795 C CG . ASP A 1 230 ? -8.700 67.380 29.719 1.00 94.76 ? 230 ASP A CG 1 ATOM 1796 O OD1 . ASP A 1 230 ? -9.921 67.598 29.881 1.00 92.73 ? 230 ASP A OD1 1 ATOM 1797 O OD2 . ASP A 1 230 ? -7.803 67.808 30.481 1.00 97.82 ? 230 ASP A OD2 1 ATOM 1798 N N . PHE A 1 231 ? -8.848 64.123 31.065 1.00 77.51 ? 231 PHE A N 1 ATOM 1799 C CA . PHE A 1 231 ? -9.819 63.581 32.020 1.00 81.23 ? 231 PHE A CA 1 ATOM 1800 C C . PHE A 1 231 ? -10.195 64.482 33.211 1.00 89.06 ? 231 PHE A C 1 ATOM 1801 O O . PHE A 1 231 ? -11.020 64.095 34.045 1.00 100.41 ? 231 PHE A O 1 ATOM 1802 C CB . PHE A 1 231 ? -9.295 62.236 32.515 1.00 78.40 ? 231 PHE A CB 1 ATOM 1803 C CG . PHE A 1 231 ? -8.921 61.314 31.397 1.00 75.03 ? 231 PHE A CG 1 ATOM 1804 C CD1 . PHE A 1 231 ? -9.852 60.438 30.862 1.00 75.73 ? 231 PHE A CD1 1 ATOM 1805 C CD2 . PHE A 1 231 ? -7.644 61.348 30.855 1.00 70.95 ? 231 PHE A CD2 1 ATOM 1806 C CE1 . PHE A 1 231 ? -9.510 59.599 29.821 1.00 73.55 ? 231 PHE A CE1 1 ATOM 1807 C CE2 . PHE A 1 231 ? -7.295 60.519 29.813 1.00 71.58 ? 231 PHE A CE2 1 ATOM 1808 C CZ . PHE A 1 231 ? -8.228 59.638 29.296 1.00 70.62 ? 231 PHE A CZ 1 ATOM 1809 N N . ASN A 1 232 ? -9.582 65.659 33.314 1.00 89.99 ? 232 ASN A N 1 ATOM 1810 C CA . ASN A 1 232 ? -10.001 66.630 34.325 1.00 88.79 ? 232 ASN A CA 1 ATOM 1811 C C . ASN A 1 232 ? -10.650 67.853 33.689 1.00 90.28 ? 232 ASN A C 1 ATOM 1812 O O . ASN A 1 232 ? -10.782 67.922 32.469 1.00 90.04 ? 232 ASN A O 1 ATOM 1813 C CB . ASN A 1 232 ? -8.822 67.058 35.199 1.00 85.81 ? 232 ASN A CB 1 ATOM 1814 C CG . ASN A 1 232 ? -7.571 67.285 34.403 1.00 82.02 ? 232 ASN A CG 1 ATOM 1815 O OD1 . ASN A 1 232 ? -7.567 67.100 33.193 1.00 82.14 ? 232 ASN A OD1 1 ATOM 1816 N ND2 . ASN A 1 232 ? -6.499 67.686 35.070 1.00 79.25 ? 232 ASN A ND2 1 ATOM 1817 N N . GLY A 1 233 ? -11.058 68.811 34.517 1.00 103.87 ? 233 GLY A N 1 ATOM 1818 C CA . GLY A 1 233 ? -11.789 69.969 34.032 1.00 123.25 ? 233 GLY A CA 1 ATOM 1819 C C . GLY A 1 233 ? -11.092 70.753 32.934 1.00 118.86 ? 233 GLY A C 1 ATOM 1820 O O . GLY A 1 233 ? -11.731 71.179 31.971 1.00 110.21 ? 233 GLY A O 1 ATOM 1821 N N . ASP A 1 234 ? -9.776 70.904 33.064 1.00 112.65 ? 234 ASP A N 1 ATOM 1822 C CA . ASP A 1 234 ? -8.989 71.746 32.164 1.00 96.69 ? 234 ASP A CA 1 ATOM 1823 C C . ASP A 1 234 ? -9.009 71.240 30.723 1.00 85.38 ? 234 ASP A C 1 ATOM 1824 O O . ASP A 1 234 ? -9.261 70.071 30.479 1.00 82.82 ? 234 ASP A O 1 ATOM 1825 C CB . ASP A 1 234 ? -7.547 71.843 32.669 1.00 99.49 ? 234 ASP A CB 1 ATOM 1826 C CG . ASP A 1 234 ? -6.937 70.483 32.984 1.00 103.94 ? 234 ASP A CG 1 ATOM 1827 O OD1 . ASP A 1 234 ? -7.188 69.505 32.244 1.00 104.51 ? 234 ASP A OD1 1 ATOM 1828 O OD2 . ASP A 1 234 ? -6.193 70.387 33.983 1.00 104.38 ? 234 ASP A OD2 1 ATOM 1829 N N . GLY A 1 235 ? -8.758 72.128 29.768 1.00 85.34 ? 235 GLY A N 1 ATOM 1830 C CA . GLY A 1 235 ? -8.754 71.742 28.368 1.00 85.95 ? 235 GLY A CA 1 ATOM 1831 C C . GLY A 1 235 ? -7.517 70.957 27.974 1.00 81.64 ? 235 GLY A C 1 ATOM 1832 O O . GLY A 1 235 ? -7.475 70.329 26.916 1.00 79.68 ? 235 GLY A O 1 ATOM 1833 N N . ILE A 1 236 ? -6.510 70.988 28.839 1.00 83.76 ? 236 ILE A N 1 ATOM 1834 C CA . ILE A 1 236 ? -5.214 70.391 28.540 1.00 85.01 ? 236 ILE A CA 1 ATOM 1835 C C . ILE A 1 236 ? -5.227 68.870 28.669 1.00 75.05 ? 236 ILE A C 1 ATOM 1836 O O . ILE A 1 236 ? -5.775 68.320 29.626 1.00 74.99 ? 236 ILE A O 1 ATOM 1837 C CB . ILE A 1 236 ? -4.119 70.964 29.460 1.00 93.15 ? 236 ILE A CB 1 ATOM 1838 C CG1 . ILE A 1 236 ? -4.150 72.494 29.426 1.00 93.04 ? 236 ILE A CG1 1 ATOM 1839 C CG2 . ILE A 1 236 ? -2.749 70.444 29.055 1.00 96.68 ? 236 ILE A CG2 1 ATOM 1840 C CD1 . ILE A 1 236 ? -3.079 73.146 30.271 1.00 97.32 ? 236 ILE A CD1 1 ATOM 1841 N N . ASP A 1 237 ? -4.619 68.202 27.692 1.00 76.87 ? 237 ASP A N 1 ATOM 1842 C CA . ASP A 1 237 ? -4.511 66.748 27.688 1.00 75.03 ? 237 ASP A CA 1 ATOM 1843 C C . ASP A 1 237 ? -3.748 66.237 28.905 1.00 72.68 ? 237 ASP A C 1 ATOM 1844 O O . ASP A 1 237 ? -2.825 66.890 29.393 1.00 79.96 ? 237 ASP A O 1 ATOM 1845 C CB . ASP A 1 237 ? -3.822 66.265 26.408 1.00 80.75 ? 237 ASP A CB 1 ATOM 1846 C CG . ASP A 1 237 ? -4.606 66.608 25.157 1.00 104.67 ? 237 ASP A CG 1 ATOM 1847 O OD1 . ASP A 1 237 ? -4.424 65.916 24.133 1.00 101.04 ? 237 ASP A OD1 1 ATOM 1848 O OD2 . ASP A 1 237 ? -5.405 67.567 25.198 1.00 125.31 ? 237 ASP A OD2 1 ATOM 1849 N N . ASP A 1 238 ? -4.140 65.063 29.386 1.00 68.69 ? 238 ASP A N 1 ATOM 1850 C CA . ASP A 1 238 ? -3.479 64.436 30.521 1.00 67.64 ? 238 ASP A CA 1 ATOM 1851 C C . ASP A 1 238 ? -2.836 63.126 30.074 1.00 64.53 ? 238 ASP A C 1 ATOM 1852 O O . ASP A 1 238 ? -3.261 62.524 29.089 1.00 66.76 ? 238 ASP A O 1 ATOM 1853 C CB . ASP A 1 238 ? -4.473 64.202 31.661 1.00 71.54 ? 238 ASP A CB 1 ATOM 1854 C CG . ASP A 1 238 ? -5.237 65.464 32.035 1.00 88.93 ? 238 ASP A CG 1 ATOM 1855 O OD1 . ASP A 1 238 ? -4.656 66.342 32.705 1.00 98.11 ? 238 ASP A OD1 1 ATOM 1856 O OD2 . ASP A 1 238 ? -6.421 65.583 31.660 1.00 98.92 ? 238 ASP A OD2 1 ATOM 1857 N N . PHE A 1 239 ? -1.807 62.692 30.795 1.00 71.23 ? 239 PHE A N 1 ATOM 1858 C CA . PHE A 1 239 ? -0.994 61.560 30.359 1.00 63.02 ? 239 PHE A CA 1 ATOM 1859 C C . PHE A 1 239 ? -1.589 60.213 30.759 1.00 58.24 ? 239 PHE A C 1 ATOM 1860 O O . PHE A 1 239 ? -2.043 60.033 31.888 1.00 60.49 ? 239 PHE A O 1 ATOM 1861 C CB . PHE A 1 239 ? 0.423 61.692 30.919 1.00 59.96 ? 239 PHE A CB 1 ATOM 1862 C CG . PHE A 1 239 ? 1.083 62.998 30.581 1.00 57.97 ? 239 PHE A CG 1 ATOM 1863 C CD1 . PHE A 1 239 ? 1.926 63.620 31.486 1.00 67.65 ? 239 PHE A CD1 1 ATOM 1864 C CD2 . PHE A 1 239 ? 0.857 63.605 29.356 1.00 56.87 ? 239 PHE A CD2 1 ATOM 1865 C CE1 . PHE A 1 239 ? 2.531 64.822 31.176 1.00 86.13 ? 239 PHE A CE1 1 ATOM 1866 C CE2 . PHE A 1 239 ? 1.459 64.804 29.040 1.00 67.32 ? 239 PHE A CE2 1 ATOM 1867 C CZ . PHE A 1 239 ? 2.295 65.415 29.951 1.00 86.55 ? 239 PHE A CZ 1 ATOM 1868 N N . VAL A 1 240 ? -1.584 59.273 29.817 1.00 54.75 ? 240 VAL A N 1 ATOM 1869 C CA . VAL A 1 240 ? -2.083 57.921 30.053 1.00 53.78 ? 240 VAL A CA 1 ATOM 1870 C C . VAL A 1 240 ? -1.074 56.886 29.572 1.00 57.67 ? 240 VAL A C 1 ATOM 1871 O O . VAL A 1 240 ? -0.716 56.861 28.395 1.00 67.32 ? 240 VAL A O 1 ATOM 1872 C CB . VAL A 1 240 ? -3.427 57.678 29.341 1.00 53.45 ? 240 VAL A CB 1 ATOM 1873 C CG1 . VAL A 1 240 ? -3.833 56.216 29.453 1.00 52.36 ? 240 VAL A CG1 1 ATOM 1874 C CG2 . VAL A 1 240 ? -4.499 58.576 29.918 1.00 60.75 ? 240 VAL A CG2 1 ATOM 1875 N N . SER A 1 241 ? -0.617 56.030 30.481 1.00 53.42 ? 241 SER A N 1 ATOM 1876 C CA . SER A 1 241 ? 0.375 55.023 30.128 1.00 48.02 ? 241 SER A CA 1 ATOM 1877 C C . SER A 1 241 ? 0.051 53.652 30.707 1.00 46.19 ? 241 SER A C 1 ATOM 1878 O O . SER A 1 241 ? -0.240 53.518 31.896 1.00 44.39 ? 241 SER A O 1 ATOM 1879 C CB . SER A 1 241 ? 1.764 55.458 30.596 1.00 49.52 ? 241 SER A CB 1 ATOM 1880 O OG . SER A 1 241 ? 2.739 54.480 30.280 1.00 63.62 ? 241 SER A OG 1 ATOM 1881 N N . GLY A 1 242 ? 0.103 52.637 29.852 1.00 45.00 ? 242 GLY A N 1 ATOM 1882 C CA . GLY A 1 242 ? -0.034 51.265 30.297 1.00 58.63 ? 242 GLY A CA 1 ATOM 1883 C C . GLY A 1 242 ? 1.256 50.790 30.937 1.00 67.01 ? 242 GLY A C 1 ATOM 1884 O O . GLY A 1 242 ? 2.349 51.136 30.486 1.00 77.09 ? 242 GLY A O 1 ATOM 1885 N N . VAL A 1 243 ? 1.129 50.007 32.002 1.00 55.21 ? 243 VAL A N 1 ATOM 1886 C CA . VAL A 1 243 ? 2.290 49.459 32.689 1.00 46.45 ? 243 VAL A CA 1 ATOM 1887 C C . VAL A 1 243 ? 2.012 47.976 32.980 1.00 42.79 ? 243 VAL A C 1 ATOM 1888 O O . VAL A 1 243 ? 1.521 47.608 34.050 1.00 42.80 ? 243 VAL A O 1 ATOM 1889 C CB . VAL A 1 243 ? 2.624 50.292 33.966 1.00 75.26 ? 243 VAL A CB 1 ATOM 1890 C CG1 . VAL A 1 243 ? 1.381 50.572 34.802 1.00 68.45 ? 243 VAL A CG1 1 ATOM 1891 C CG2 . VAL A 1 243 ? 3.723 49.648 34.784 1.00 88.97 ? 243 VAL A CG2 1 ATOM 1892 N N . PRO A 1 244 ? 2.324 47.119 31.994 1.00 43.08 ? 244 PRO A N 1 ATOM 1893 C CA . PRO A 1 244 ? 1.888 45.719 31.878 1.00 46.44 ? 244 PRO A CA 1 ATOM 1894 C C . PRO A 1 244 ? 2.415 44.771 32.951 1.00 42.25 ? 244 PRO A C 1 ATOM 1895 O O . PRO A 1 244 ? 1.730 43.806 33.290 1.00 40.83 ? 244 PRO A O 1 ATOM 1896 C CB . PRO A 1 244 ? 2.428 45.307 30.506 1.00 44.65 ? 244 PRO A CB 1 ATOM 1897 C CG . PRO A 1 244 ? 3.606 46.184 30.292 1.00 37.11 ? 244 PRO A CG 1 ATOM 1898 C CD . PRO A 1 244 ? 3.223 47.502 30.892 1.00 37.78 ? 244 PRO A CD 1 ATOM 1899 N N . ARG A 1 245 ? 3.614 45.020 33.462 1.00 45.24 ? 245 ARG A N 1 ATOM 1900 C CA . ARG A 1 245 ? 4.199 44.128 34.454 1.00 42.58 ? 245 ARG A CA 1 ATOM 1901 C C . ARG A 1 245 ? 3.921 44.588 35.880 1.00 53.96 ? 245 ARG A C 1 ATOM 1902 O O . ARG A 1 245 ? 4.403 43.983 36.836 1.00 82.17 ? 245 ARG A O 1 ATOM 1903 C CB . ARG A 1 245 ? 5.706 43.995 34.237 1.00 40.83 ? 245 ARG A CB 1 ATOM 1904 C CG . ARG A 1 245 ? 6.103 42.967 33.193 1.00 40.92 ? 245 ARG A CG 1 ATOM 1905 C CD . ARG A 1 245 ? 7.544 42.535 33.396 1.00 49.04 ? 245 ARG A CD 1 ATOM 1906 N NE . ARG A 1 245 ? 7.785 42.113 34.773 1.00 48.03 ? 245 ARG A NE 1 ATOM 1907 C CZ . ARG A 1 245 ? 7.717 40.854 35.194 1.00 50.96 ? 245 ARG A CZ 1 ATOM 1908 N NH1 . ARG A 1 245 ? 7.422 39.882 34.342 1.00 59.13 ? 245 ARG A NH1 1 ATOM 1909 N NH2 . ARG A 1 245 ? 7.948 40.567 36.468 1.00 59.12 ? 245 ARG A NH2 1 ATOM 1910 N N . ALA A 1 246 ? 3.144 45.657 36.023 1.00 49.98 ? 246 ALA A N 1 ATOM 1911 C CA . ALA A 1 246 ? 2.842 46.190 37.347 1.00 62.73 ? 246 ALA A CA 1 ATOM 1912 C C . ALA A 1 246 ? 1.847 45.311 38.089 1.00 64.51 ? 246 ALA A C 1 ATOM 1913 O O . ALA A 1 246 ? 1.332 44.339 37.535 1.00 54.42 ? 246 ALA A O 1 ATOM 1914 C CB . ALA A 1 246 ? 2.304 47.603 37.240 1.00 64.84 ? 246 ALA A CB 1 ATOM 1915 N N . ALA A 1 247 ? 1.571 45.688 39.337 1.00 73.52 ? 247 ALA A N 1 ATOM 1916 C CA . ALA A 1 247 ? 0.634 44.977 40.204 1.00 69.20 ? 247 ALA A CA 1 ATOM 1917 C C . ALA A 1 247 ? 0.825 43.470 40.141 1.00 70.76 ? 247 ALA A C 1 ATOM 1918 O O . ALA A 1 247 ? -0.063 42.760 39.677 1.00 70.84 ? 247 ALA A O 1 ATOM 1919 C CB . ALA A 1 247 ? -0.796 45.336 39.837 1.00 65.03 ? 247 ALA A CB 1 ATOM 1920 N N . ARG A 1 248 ? 1.990 43.002 40.590 1.00 72.37 ? 248 ARG A N 1 ATOM 1921 C CA . ARG A 1 248 ? 2.367 41.582 40.584 1.00 61.63 ? 248 ARG A CA 1 ATOM 1922 C C . ARG A 1 248 ? 1.984 40.900 39.265 1.00 58.12 ? 248 ARG A C 1 ATOM 1923 O O . ARG A 1 248 ? 1.391 39.822 39.262 1.00 77.67 ? 248 ARG A O 1 ATOM 1924 C CB . ARG A 1 248 ? 1.766 40.836 41.794 1.00 66.73 ? 248 ARG A CB 1 ATOM 1925 C CG . ARG A 1 248 ? 0.246 40.810 41.903 1.00 93.60 ? 248 ARG A CG 1 ATOM 1926 C CD . ARG A 1 248 ? -0.225 40.003 43.091 1.00 114.43 ? 248 ARG A CD 1 ATOM 1927 N NE . ARG A 1 248 ? -1.652 39.702 43.012 1.00 124.84 ? 248 ARG A NE 1 ATOM 1928 C CZ . ARG A 1 248 ? -2.162 38.659 42.364 1.00 113.07 ? 248 ARG A CZ 1 ATOM 1929 N NH1 . ARG A 1 248 ? -1.362 37.813 41.730 1.00 108.37 ? 248 ARG A NH1 1 ATOM 1930 N NH2 . ARG A 1 248 ? -3.474 38.465 42.345 1.00 98.11 ? 248 ARG A NH2 1 ATOM 1931 N N . THR A 1 249 ? 2.321 41.575 38.164 1.00 52.47 ? 249 THR A N 1 ATOM 1932 C CA . THR A 1 249 ? 2.152 41.115 36.776 1.00 49.17 ? 249 THR A CA 1 ATOM 1933 C C . THR A 1 249 ? 0.696 41.158 36.273 1.00 51.10 ? 249 THR A C 1 ATOM 1934 O O . THR A 1 249 ? 0.439 40.898 35.093 1.00 51.81 ? 249 THR A O 1 ATOM 1935 C CB . THR A 1 249 ? 2.756 39.687 36.569 1.00 51.52 ? 249 THR A CB 1 ATOM 1936 O OG1 . THR A 1 249 ? 3.490 39.651 35.339 1.00 67.02 ? 249 THR A OG1 1 ATOM 1937 C CG2 . THR A 1 249 ? 1.690 38.603 36.545 1.00 51.59 ? 249 THR A CG2 1 ATOM 1938 N N . LEU A 1 250 ? -0.246 41.520 37.145 1.00 48.85 ? 250 LEU A N 1 ATOM 1939 C CA . LEU A 1 250 ? -1.636 41.739 36.725 1.00 48.46 ? 250 LEU A CA 1 ATOM 1940 C C . LEU A 1 250 ? -1.726 42.766 35.603 1.00 53.31 ? 250 LEU A C 1 ATOM 1941 O O . LEU A 1 250 ? -2.547 42.645 34.694 1.00 55.97 ? 250 LEU A O 1 ATOM 1942 C CB . LEU A 1 250 ? -2.505 42.208 37.896 1.00 48.08 ? 250 LEU A CB 1 ATOM 1943 C CG . LEU A 1 250 ? -3.239 41.168 38.743 1.00 55.19 ? 250 LEU A CG 1 ATOM 1944 C CD1 . LEU A 1 250 ? -2.248 40.273 39.436 1.00 78.99 ? 250 LEU A CD1 1 ATOM 1945 C CD2 . LEU A 1 250 ? -4.147 41.845 39.759 1.00 50.91 ? 250 LEU A CD2 1 ATOM 1946 N N . GLY A 1 251 ? -0.874 43.781 35.684 1.00 56.48 ? 251 GLY A N 1 ATOM 1947 C CA . GLY A 1 251 ? -0.859 44.856 34.713 1.00 52.97 ? 251 GLY A CA 1 ATOM 1948 C C . GLY A 1 251 ? -1.688 46.033 35.180 1.00 48.18 ? 251 GLY A C 1 ATOM 1949 O O . GLY A 1 251 ? -2.714 45.863 35.839 1.00 55.82 ? 251 GLY A O 1 ATOM 1950 N N . MET A 1 252 ? -1.246 47.232 34.825 1.00 47.51 ? 252 MET A N 1 ATOM 1951 C CA . MET A 1 252 ? -1.927 48.448 35.244 1.00 49.89 ? 252 MET A CA 1 ATOM 1952 C C . MET A 1 252 ? -1.871 49.526 34.169 1.00 50.26 ? 252 MET A C 1 ATOM 1953 O O . MET A 1 252 ? -1.097 49.434 33.216 1.00 46.99 ? 252 MET A O 1 ATOM 1954 C CB . MET A 1 252 ? -1.324 48.984 36.546 1.00 50.46 ? 252 MET A CB 1 ATOM 1955 C CG . MET A 1 252 ? -1.906 48.386 37.817 1.00 50.42 ? 252 MET A CG 1 ATOM 1956 S SD . MET A 1 252 ? -1.317 49.246 39.290 1.00 59.15 ? 252 MET A SD 1 ATOM 1957 C CE . MET A 1 252 ? -2.359 48.527 40.558 1.00 92.68 ? 252 MET A CE 1 ATOM 1958 N N . VAL A 1 253 ? -2.714 50.540 34.324 1.00 52.77 ? 253 VAL A N 1 ATOM 1959 C CA . VAL A 1 253 ? -2.678 51.710 33.458 1.00 54.18 ? 253 VAL A CA 1 ATOM 1960 C C . VAL A 1 253 ? -2.722 52.977 34.301 1.00 64.24 ? 253 VAL A C 1 ATOM 1961 O O . VAL A 1 253 ? -3.700 53.232 35.005 1.00 84.79 ? 253 VAL A O 1 ATOM 1962 C CB . VAL A 1 253 ? -3.845 51.716 32.455 1.00 53.43 ? 253 VAL A CB 1 ATOM 1963 C CG1 . VAL A 1 253 ? -3.896 53.039 31.708 1.00 54.16 ? 253 VAL A CG1 1 ATOM 1964 C CG2 . VAL A 1 253 ? -3.710 50.558 31.484 1.00 49.03 ? 253 VAL A CG2 1 ATOM 1965 N N . TYR A 1 254 ? -1.658 53.768 34.228 1.00 59.37 ? 254 TYR A N 1 ATOM 1966 C CA . TYR A 1 254 ? -1.564 54.986 35.021 1.00 60.24 ? 254 TYR A CA 1 ATOM 1967 C C . TYR A 1 254 ? -2.051 56.199 34.240 1.00 65.24 ? 254 TYR A C 1 ATOM 1968 O O . TYR A 1 254 ? -1.807 56.320 33.039 1.00 58.51 ? 254 TYR A O 1 ATOM 1969 C CB . TYR A 1 254 ? -0.125 55.215 35.489 1.00 58.42 ? 254 TYR A CB 1 ATOM 1970 C CG . TYR A 1 254 ? 0.392 54.166 36.449 1.00 60.56 ? 254 TYR A CG 1 ATOM 1971 C CD1 . TYR A 1 254 ? -0.482 53.371 37.180 1.00 60.71 ? 254 TYR A CD1 1 ATOM 1972 C CD2 . TYR A 1 254 ? 1.755 53.974 36.625 1.00 70.86 ? 254 TYR A CD2 1 ATOM 1973 C CE1 . TYR A 1 254 ? -0.011 52.412 38.058 1.00 61.62 ? 254 TYR A CE1 1 ATOM 1974 C CE2 . TYR A 1 254 ? 2.236 53.018 37.501 1.00 65.35 ? 254 TYR A CE2 1 ATOM 1975 C CZ . TYR A 1 254 ? 1.349 52.241 38.214 1.00 61.61 ? 254 TYR A CZ 1 ATOM 1976 O OH . TYR A 1 254 ? 1.825 51.289 39.086 1.00 64.09 ? 254 TYR A OH 1 ATOM 1977 N N . ILE A 1 255 ? -2.748 57.093 34.932 1.00 73.87 ? 255 ILE A N 1 ATOM 1978 C CA . ILE A 1 255 ? -3.172 58.356 34.344 1.00 61.22 ? 255 ILE A CA 1 ATOM 1979 C C . ILE A 1 255 ? -2.640 59.517 35.173 1.00 61.22 ? 255 ILE A C 1 ATOM 1980 O O . ILE A 1 255 ? -2.950 59.638 36.357 1.00 64.03 ? 255 ILE A O 1 ATOM 1981 C CB . ILE A 1 255 ? -4.704 58.456 34.240 1.00 61.99 ? 255 ILE A CB 1 ATOM 1982 C CG1 . ILE A 1 255 ? -5.240 57.406 33.265 1.00 59.47 ? 255 ILE A CG1 1 ATOM 1983 C CG2 . ILE A 1 255 ? -5.115 59.851 33.797 1.00 63.08 ? 255 ILE A CG2 1 ATOM 1984 C CD1 . ILE A 1 255 ? -6.724 57.526 32.989 1.00 61.32 ? 255 ILE A CD1 1 ATOM 1985 N N . TYR A 1 256 ? -1.828 60.363 34.548 1.00 59.37 ? 256 TYR A N 1 ATOM 1986 C CA . TYR A 1 256 ? -1.244 61.507 35.238 1.00 65.60 ? 256 TYR A CA 1 ATOM 1987 C C . TYR A 1 256 ? -1.799 62.820 34.701 1.00 71.93 ? 256 TYR A C 1 ATOM 1988 O O . TYR A 1 256 ? -2.181 62.912 33.535 1.00 87.46 ? 256 TYR A O 1 ATOM 1989 C CB . TYR A 1 256 ? 0.281 61.497 35.108 1.00 68.79 ? 256 TYR A CB 1 ATOM 1990 C CG . TYR A 1 256 ? 0.953 60.285 35.714 1.00 69.54 ? 256 TYR A CG 1 ATOM 1991 C CD1 . TYR A 1 256 ? 1.636 59.375 34.918 1.00 64.79 ? 256 TYR A CD1 1 ATOM 1992 C CD2 . TYR A 1 256 ? 0.903 60.050 37.080 1.00 75.92 ? 256 TYR A CD2 1 ATOM 1993 C CE1 . TYR A 1 256 ? 2.254 58.268 35.468 1.00 57.90 ? 256 TYR A CE1 1 ATOM 1994 C CE2 . TYR A 1 256 ? 1.518 58.947 37.640 1.00 72.26 ? 256 TYR A CE2 1 ATOM 1995 C CZ . TYR A 1 256 ? 2.191 58.059 36.829 1.00 64.52 ? 256 TYR A CZ 1 ATOM 1996 O OH . TYR A 1 256 ? 2.804 56.958 37.383 1.00 71.86 ? 256 TYR A OH 1 ATOM 1997 N N . ASP A 1 257 ? -1.841 63.831 35.562 1.00 68.48 ? 257 ASP A N 1 ATOM 1998 C CA . ASP A 1 257 ? -2.299 65.160 35.176 1.00 70.75 ? 257 ASP A CA 1 ATOM 1999 C C . ASP A 1 257 ? -1.353 65.767 34.143 1.00 68.24 ? 257 ASP A C 1 ATOM 2000 O O . ASP A 1 257 ? -0.160 65.464 34.127 1.00 72.21 ? 257 ASP A O 1 ATOM 2001 C CB . ASP A 1 257 ? -2.403 66.065 36.409 1.00 79.46 ? 257 ASP A CB 1 ATOM 2002 C CG . ASP A 1 257 ? -3.200 67.332 36.148 1.00 98.21 ? 257 ASP A CG 1 ATOM 2003 O OD1 . ASP A 1 257 ? -4.086 67.650 36.969 1.00 114.39 ? 257 ASP A OD1 1 ATOM 2004 O OD2 . ASP A 1 257 ? -2.939 68.017 35.137 1.00 100.76 ? 257 ASP A OD2 1 ATOM 2005 N N . GLY A 1 258 ? -1.893 66.620 33.279 1.00 69.48 ? 258 GLY A N 1 ATOM 2006 C CA . GLY A 1 258 ? -1.096 67.287 32.267 1.00 66.31 ? 258 GLY A CA 1 ATOM 2007 C C . GLY A 1 258 ? -0.383 68.504 32.822 1.00 74.95 ? 258 GLY A C 1 ATOM 2008 O O . GLY A 1 258 ? 0.629 68.945 32.279 1.00 78.35 ? 258 GLY A O 1 ATOM 2009 N N . LYS A 1 259 ? -0.912 69.044 33.916 1.00 80.50 ? 259 LYS A N 1 ATOM 2010 C CA . LYS A 1 259 ? -0.317 70.203 34.569 1.00 83.03 ? 259 LYS A CA 1 ATOM 2011 C C . LYS A 1 259 ? 0.957 69.784 35.288 1.00 81.85 ? 259 LYS A C 1 ATOM 2012 O O . LYS A 1 259 ? 2.058 70.192 34.919 1.00 84.08 ? 259 LYS A O 1 ATOM 2013 C CB . LYS A 1 259 ? -1.300 70.832 35.559 1.00 92.48 ? 259 LYS A CB 1 ATOM 2014 C CG . LYS A 1 259 ? -2.596 71.327 34.939 1.00 94.32 ? 259 LYS A CG 1 ATOM 2015 C CD . LYS A 1 259 ? -2.400 72.652 34.224 1.00 99.58 ? 259 LYS A CD 1 ATOM 2016 C CE . LYS A 1 259 ? -3.736 73.279 33.858 1.00 106.37 ? 259 LYS A CE 1 ATOM 2017 N NZ . LYS A 1 259 ? -3.573 74.645 33.287 1.00 109.97 ? 259 LYS A NZ 1 ATOM 2018 N N . ASN A 1 260 ? 0.794 68.965 36.319 1.00 82.68 ? 260 ASN A N 1 ATOM 2019 C CA . ASN A 1 260 ? 1.923 68.346 36.996 1.00 87.81 ? 260 ASN A CA 1 ATOM 2020 C C . ASN A 1 260 ? 1.774 66.832 36.989 1.00 83.23 ? 260 ASN A C 1 ATOM 2021 O O . ASN A 1 260 ? 0.699 66.307 36.713 1.00 92.86 ? 260 ASN A O 1 ATOM 2022 C CB . ASN A 1 260 ? 2.068 68.868 38.426 1.00 100.20 ? 260 ASN A CB 1 ATOM 2023 C CG . ASN A 1 260 ? 0.764 69.377 39.001 1.00 126.85 ? 260 ASN A CG 1 ATOM 2024 O OD1 . ASN A 1 260 ? 0.281 70.443 38.617 1.00 121.45 ? 260 ASN A OD1 1 ATOM 2025 N ND2 . ASN A 1 260 ? 0.190 68.621 39.934 1.00 159.84 ? 260 ASN A ND2 1 ATOM 2026 N N . MET A 1 261 ? 2.860 66.134 37.294 1.00 75.65 ? 261 MET A N 1 ATOM 2027 C CA . MET A 1 261 ? 2.928 64.690 37.103 1.00 70.55 ? 261 MET A CA 1 ATOM 2028 C C . MET A 1 261 ? 2.069 63.892 38.083 1.00 70.08 ? 261 MET A C 1 ATOM 2029 O O . MET A 1 261 ? 2.037 62.666 38.014 1.00 72.26 ? 261 MET A O 1 ATOM 2030 C CB . MET A 1 261 ? 4.379 64.218 37.187 1.00 100.03 ? 261 MET A CB 1 ATOM 2031 C CG . MET A 1 261 ? 4.716 63.175 36.140 1.00 105.54 ? 261 MET A CG 1 ATOM 2032 S SD . MET A 1 261 ? 3.887 63.552 34.583 1.00 93.07 ? 261 MET A SD 1 ATOM 2033 C CE . MET A 1 261 ? 4.602 62.320 33.504 1.00 48.54 ? 261 MET A CE 1 ATOM 2034 N N . SER A 1 262 ? 1.402 64.586 39.002 1.00 83.67 ? 262 SER A N 1 ATOM 2035 C CA . SER A 1 262 ? 0.565 63.944 40.015 1.00 93.53 ? 262 SER A CA 1 ATOM 2036 C C . SER A 1 262 ? -0.425 62.945 39.415 1.00 82.04 ? 262 SER A C 1 ATOM 2037 O O . SER A 1 262 ? -1.035 63.202 38.377 1.00 69.52 ? 262 SER A O 1 ATOM 2038 C CB . SER A 1 262 ? -0.202 65.000 40.813 1.00 92.79 ? 262 SER A CB 1 ATOM 2039 O OG . SER A 1 262 ? -1.175 65.639 40.005 1.00 77.60 ? 262 SER A OG 1 ATOM 2040 N N . SER A 1 263 ? -0.567 61.801 40.078 1.00 74.48 ? 263 SER A N 1 ATOM 2041 C CA . SER A 1 263 ? -1.439 60.730 39.608 1.00 67.48 ? 263 SER A CA 1 ATOM 2042 C C . SER A 1 263 ? -2.906 61.145 39.614 1.00 68.26 ? 263 SER A C 1 ATOM 2043 O O . SER A 1 263 ? -3.330 61.953 40.440 1.00 70.66 ? 263 SER A O 1 ATOM 2044 C CB . SER A 1 263 ? -1.249 59.477 40.466 1.00 68.34 ? 263 SER A CB 1 ATOM 2045 O OG . SER A 1 263 ? -2.109 58.433 40.044 1.00 75.10 ? 263 SER A OG 1 ATOM 2046 N N . LEU A 1 264 ? -3.676 60.584 38.686 1.00 67.43 ? 264 LEU A N 1 ATOM 2047 C CA . LEU A 1 264 ? -5.099 60.886 38.584 1.00 69.13 ? 264 LEU A CA 1 ATOM 2048 C C . LEU A 1 264 ? -5.951 59.637 38.787 1.00 71.14 ? 264 LEU A C 1 ATOM 2049 O O . LEU A 1 264 ? -6.643 59.509 39.795 1.00 80.32 ? 264 LEU A O 1 ATOM 2050 C CB . LEU A 1 264 ? -5.415 61.526 37.231 1.00 67.98 ? 264 LEU A CB 1 ATOM 2051 C CG . LEU A 1 264 ? -5.708 63.028 37.245 1.00 70.42 ? 264 LEU A CG 1 ATOM 2052 C CD1 . LEU A 1 264 ? -4.663 63.774 38.057 1.00 81.42 ? 264 LEU A CD1 1 ATOM 2053 C CD2 . LEU A 1 264 ? -5.773 63.575 35.827 1.00 69.62 ? 264 LEU A CD2 1 ATOM 2054 N N . TYR A 1 265 ? -5.897 58.718 37.828 1.00 71.10 ? 265 TYR A N 1 ATOM 2055 C CA . TYR A 1 265 ? -6.690 57.496 37.904 1.00 74.28 ? 265 TYR A CA 1 ATOM 2056 C C . TYR A 1 265 ? -5.855 56.250 37.628 1.00 77.35 ? 265 TYR A C 1 ATOM 2057 O O . TYR A 1 265 ? -4.775 56.327 37.040 1.00 69.76 ? 265 TYR A O 1 ATOM 2058 C CB . TYR A 1 265 ? -7.864 57.562 36.925 1.00 78.36 ? 265 TYR A CB 1 ATOM 2059 C CG . TYR A 1 265 ? -8.808 58.716 37.177 1.00 89.83 ? 265 TYR A CG 1 ATOM 2060 C CD1 . TYR A 1 265 ? -9.789 58.635 38.157 1.00 98.48 ? 265 TYR A CD1 1 ATOM 2061 C CD2 . TYR A 1 265 ? -8.721 59.885 36.432 1.00 91.64 ? 265 TYR A CD2 1 ATOM 2062 C CE1 . TYR A 1 265 ? -10.654 59.688 38.390 1.00 100.67 ? 265 TYR A CE1 1 ATOM 2063 C CE2 . TYR A 1 265 ? -9.582 60.942 36.658 1.00 93.69 ? 265 TYR A CE2 1 ATOM 2064 C CZ . TYR A 1 265 ? -10.546 60.838 37.638 1.00 104.30 ? 265 TYR A CZ 1 ATOM 2065 O OH . TYR A 1 265 ? -11.406 61.888 37.866 1.00 123.65 ? 265 TYR A OH 1 ATOM 2066 N N . ASN A 1 266 ? -6.370 55.101 38.056 1.00 82.57 ? 266 ASN A N 1 ATOM 2067 C CA . ASN A 1 266 ? -5.683 53.827 37.880 1.00 71.15 ? 266 ASN A CA 1 ATOM 2068 C C . ASN A 1 266 ? -6.574 52.742 37.292 1.00 68.43 ? 266 ASN A C 1 ATOM 2069 O O . ASN A 1 266 ? -7.779 52.711 37.534 1.00 80.28 ? 266 ASN A O 1 ATOM 2070 C CB . ASN A 1 266 ? -5.123 53.334 39.213 1.00 73.39 ? 266 ASN A CB 1 ATOM 2071 C CG . ASN A 1 266 ? -3.771 53.925 39.534 1.00 75.43 ? 266 ASN A CG 1 ATOM 2072 O OD1 . ASN A 1 266 ? -3.098 54.484 38.669 1.00 73.21 ? 266 ASN A OD1 1 ATOM 2073 N ND2 . ASN A 1 266 ? -3.361 53.795 40.788 1.00 87.75 ? 266 ASN A ND2 1 ATOM 2074 N N . PHE A 1 267 ? -5.964 51.850 36.522 1.00 64.38 ? 267 PHE A N 1 ATOM 2075 C CA . PHE A 1 267 ? -6.648 50.664 36.027 1.00 63.42 ? 267 PHE A CA 1 ATOM 2076 C C . PHE A 1 267 ? -5.798 49.441 36.340 1.00 82.12 ? 267 PHE A C 1 ATOM 2077 O O . PHE A 1 267 ? -4.575 49.534 36.397 1.00 72.82 ? 267 PHE A O 1 ATOM 2078 C CB . PHE A 1 267 ? -6.915 50.774 34.525 1.00 61.98 ? 267 PHE A CB 1 ATOM 2079 C CG . PHE A 1 267 ? -7.852 51.888 34.160 1.00 66.06 ? 267 PHE A CG 1 ATOM 2080 C CD1 . PHE A 1 267 ? -7.369 53.160 33.901 1.00 67.10 ? 267 PHE A CD1 1 ATOM 2081 C CD2 . PHE A 1 267 ? -9.216 51.665 34.081 1.00 80.56 ? 267 PHE A CD2 1 ATOM 2082 C CE1 . PHE A 1 267 ? -8.230 54.189 33.567 1.00 70.45 ? 267 PHE A CE1 1 ATOM 2083 C CE2 . PHE A 1 267 ? -10.082 52.690 33.747 1.00 76.85 ? 267 PHE A CE2 1 ATOM 2084 C CZ . PHE A 1 267 ? -9.588 53.954 33.490 1.00 72.80 ? 267 PHE A CZ 1 ATOM 2085 N N . THR A 1 268 ? -6.444 48.301 36.557 1.00 89.90 ? 268 THR A N 1 ATOM 2086 C CA . THR A 1 268 ? -5.729 47.082 36.915 1.00 68.28 ? 268 THR A CA 1 ATOM 2087 C C . THR A 1 268 ? -6.307 45.872 36.190 1.00 58.13 ? 268 THR A C 1 ATOM 2088 O O . THR A 1 268 ? -7.524 45.722 36.091 1.00 59.93 ? 268 THR A O 1 ATOM 2089 C CB . THR A 1 268 ? -5.772 46.833 38.438 1.00 56.86 ? 268 THR A CB 1 ATOM 2090 O OG1 . THR A 1 268 ? -5.307 47.998 39.131 1.00 55.25 ? 268 THR A OG1 1 ATOM 2091 C CG2 . THR A 1 268 ? -4.902 45.643 38.817 1.00 54.88 ? 268 THR A CG2 1 ATOM 2092 N N . GLY A 1 269 ? -5.429 45.018 35.674 1.00 58.21 ? 269 GLY A N 1 ATOM 2093 C CA . GLY A 1 269 ? -5.856 43.788 35.036 1.00 77.76 ? 269 GLY A CA 1 ATOM 2094 C C . GLY A 1 269 ? -6.414 42.811 36.052 1.00 81.00 ? 269 GLY A C 1 ATOM 2095 O O . GLY A 1 269 ? -6.009 42.816 37.214 1.00 91.75 ? 269 GLY A O 1 ATOM 2096 N N . GLU A 1 270 ? -7.353 41.976 35.618 1.00 65.78 ? 270 GLU A N 1 ATOM 2097 C CA . GLU A 1 270 ? -7.961 40.991 36.504 1.00 70.39 ? 270 GLU A CA 1 ATOM 2098 C C . GLU A 1 270 ? -7.281 39.630 36.390 1.00 65.14 ? 270 GLU A C 1 ATOM 2099 O O . GLU A 1 270 ? -7.617 38.698 37.119 1.00 79.62 ? 270 GLU A O 1 ATOM 2100 C CB . GLU A 1 270 ? -9.454 40.853 36.201 1.00 89.42 ? 270 GLU A CB 1 ATOM 2101 C CG . GLU A 1 270 ? -9.763 40.513 34.753 1.00 111.48 ? 270 GLU A CG 1 ATOM 2102 C CD . GLU A 1 270 ? -11.238 40.251 34.519 1.00 123.03 ? 270 GLU A CD 1 ATOM 2103 O OE1 . GLU A 1 270 ? -11.957 39.984 35.505 1.00 130.42 ? 270 GLU A OE1 1 ATOM 2104 O OE2 . GLU A 1 270 ? -11.678 40.315 33.352 1.00 117.06 ? 270 GLU A OE2 1 ATOM 2105 N N . GLN A 1 271 ? -6.320 39.523 35.478 1.00 57.84 ? 271 GLN A N 1 ATOM 2106 C CA . GLN A 1 271 ? -5.616 38.263 35.265 1.00 65.52 ? 271 GLN A CA 1 ATOM 2107 C C . GLN A 1 271 ? -4.114 38.472 35.113 1.00 73.28 ? 271 GLN A C 1 ATOM 2108 O O . GLN A 1 271 ? -3.669 39.370 34.397 1.00 83.44 ? 271 GLN A O 1 ATOM 2109 C CB . GLN A 1 271 ? -6.165 37.540 34.034 1.00 63.43 ? 271 GLN A CB 1 ATOM 2110 C CG . GLN A 1 271 ? -5.440 36.240 33.711 1.00 52.52 ? 271 GLN A CG 1 ATOM 2111 C CD . GLN A 1 271 ? -5.941 35.587 32.438 1.00 48.88 ? 271 GLN A CD 1 ATOM 2112 O OE1 . GLN A 1 271 ? -5.159 35.266 31.543 1.00 48.11 ? 271 GLN A OE1 1 ATOM 2113 N NE2 . GLN A 1 271 ? -7.250 35.381 32.353 1.00 50.14 ? 271 GLN A NE2 1 ATOM 2114 N N . MET A 1 272 ? -3.342 37.630 35.792 1.00 71.04 ? 272 MET A N 1 ATOM 2115 C CA . MET A 1 272 ? -1.887 37.683 35.733 1.00 57.26 ? 272 MET A CA 1 ATOM 2116 C C . MET A 1 272 ? -1.362 37.331 34.344 1.00 52.49 ? 272 MET A C 1 ATOM 2117 O O . MET A 1 272 ? -2.003 36.582 33.605 1.00 62.78 ? 272 MET A O 1 ATOM 2118 C CB . MET A 1 272 ? -1.286 36.735 36.772 1.00 57.82 ? 272 MET A CB 1 ATOM 2119 C CG . MET A 1 272 ? -1.670 37.067 38.199 1.00 50.57 ? 272 MET A CG 1 ATOM 2120 S SD . MET A 1 272 ? -0.943 35.961 39.419 1.00 132.61 ? 272 MET A SD 1 ATOM 2121 C CE . MET A 1 272 ? 0.800 36.137 39.053 1.00 64.14 ? 272 MET A CE 1 ATOM 2122 N N . ALA A 1 273 ? -0.213 37.906 33.991 1.00 44.81 ? 273 ALA A N 1 ATOM 2123 C CA . ALA A 1 273 ? 0.525 37.565 32.771 1.00 45.13 ? 273 ALA A CA 1 ATOM 2124 C C . ALA A 1 273 ? -0.209 37.948 31.485 1.00 44.13 ? 273 ALA A C 1 ATOM 2125 O O . ALA A 1 273 ? 0.324 37.781 30.389 1.00 43.45 ? 273 ALA A O 1 ATOM 2126 C CB . ALA A 1 273 ? 0.867 36.077 32.756 1.00 47.12 ? 273 ALA A CB 1 ATOM 2127 N N . ALA A 1 274 ? -1.428 38.460 31.623 1.00 49.64 ? 274 ALA A N 1 ATOM 2128 C CA . ALA A 1 274 ? -2.240 38.855 30.476 1.00 48.34 ? 274 ALA A CA 1 ATOM 2129 C C . ALA A 1 274 ? -1.666 40.079 29.767 1.00 47.41 ? 274 ALA A C 1 ATOM 2130 O O . ALA A 1 274 ? -2.113 40.440 28.676 1.00 39.97 ? 274 ALA A O 1 ATOM 2131 C CB . ALA A 1 274 ? -3.668 39.126 30.917 1.00 52.54 ? 274 ALA A CB 1 ATOM 2132 N N . TYR A 1 275 ? -0.678 40.706 30.402 1.00 43.75 ? 275 TYR A N 1 ATOM 2133 C CA . TYR A 1 275 ? -0.025 41.907 29.889 1.00 44.28 ? 275 TYR A CA 1 ATOM 2134 C C . TYR A 1 275 ? -1.027 43.033 29.668 1.00 43.69 ? 275 TYR A C 1 ATOM 2135 O O . TYR A 1 275 ? -1.033 43.684 28.622 1.00 40.43 ? 275 TYR A O 1 ATOM 2136 C CB . TYR A 1 275 ? 0.736 41.605 28.596 1.00 54.24 ? 275 TYR A CB 1 ATOM 2137 C CG . TYR A 1 275 ? 2.165 42.091 28.630 1.00 53.72 ? 275 TYR A CG 1 ATOM 2138 C CD1 . TYR A 1 275 ? 3.077 41.542 29.518 1.00 52.67 ? 275 TYR A CD1 1 ATOM 2139 C CD2 . TYR A 1 275 ? 2.601 43.100 27.782 1.00 48.62 ? 275 TYR A CD2 1 ATOM 2140 C CE1 . TYR A 1 275 ? 4.381 41.979 29.564 1.00 40.81 ? 275 TYR A CE1 1 ATOM 2141 C CE2 . TYR A 1 275 ? 3.910 43.545 27.819 1.00 48.02 ? 275 TYR A CE2 1 ATOM 2142 C CZ . TYR A 1 275 ? 4.795 42.979 28.714 1.00 43.92 ? 275 TYR A CZ 1 ATOM 2143 O OH . TYR A 1 275 ? 6.100 43.411 28.761 1.00 50.71 ? 275 TYR A OH 1 ATOM 2144 N N . PHE A 1 276 ? -1.880 43.242 30.666 1.00 55.34 ? 276 PHE A N 1 ATOM 2145 C CA . PHE A 1 276 ? -2.826 44.347 30.669 1.00 54.97 ? 276 PHE A CA 1 ATOM 2146 C C . PHE A 1 276 ? -2.074 45.667 30.545 1.00 49.03 ? 276 PHE A C 1 ATOM 2147 O O . PHE A 1 276 ? -1.212 45.975 31.364 1.00 60.15 ? 276 PHE A O 1 ATOM 2148 C CB . PHE A 1 276 ? -3.657 44.304 31.955 1.00 58.77 ? 276 PHE A CB 1 ATOM 2149 C CG . PHE A 1 276 ? -4.662 45.412 32.085 1.00 50.72 ? 276 PHE A CG 1 ATOM 2150 C CD1 . PHE A 1 276 ? -5.927 45.288 31.534 1.00 61.38 ? 276 PHE A CD1 1 ATOM 2151 C CD2 . PHE A 1 276 ? -4.356 46.562 32.794 1.00 51.92 ? 276 PHE A CD2 1 ATOM 2152 C CE1 . PHE A 1 276 ? -6.859 46.299 31.669 1.00 65.00 ? 276 PHE A CE1 1 ATOM 2153 C CE2 . PHE A 1 276 ? -5.281 47.577 32.931 1.00 55.76 ? 276 PHE A CE2 1 ATOM 2154 C CZ . PHE A 1 276 ? -6.536 47.445 32.370 1.00 58.62 ? 276 PHE A CZ 1 ATOM 2155 N N . GLY A 1 277 ? -2.411 46.453 29.529 1.00 61.19 ? 277 GLY A N 1 ATOM 2156 C CA . GLY A 1 277 ? -1.708 47.698 29.279 1.00 65.11 ? 277 GLY A CA 1 ATOM 2157 C C . GLY A 1 277 ? -0.604 47.596 28.239 1.00 53.17 ? 277 GLY A C 1 ATOM 2158 O O . GLY A 1 277 ? 0.270 48.461 28.172 1.00 41.09 ? 277 GLY A O 1 ATOM 2159 N N . PHE A 1 278 ? -0.632 46.536 27.435 1.00 66.85 ? 278 PHE A N 1 ATOM 2160 C CA . PHE A 1 278 ? 0.316 46.387 26.333 1.00 55.33 ? 278 PHE A CA 1 ATOM 2161 C C . PHE A 1 278 ? 0.092 47.483 25.300 1.00 45.51 ? 278 PHE A C 1 ATOM 2162 O O . PHE A 1 278 ? 1.022 47.915 24.620 1.00 53.57 ? 278 PHE A O 1 ATOM 2163 C CB . PHE A 1 278 ? 0.184 45.009 25.676 1.00 47.93 ? 278 PHE A CB 1 ATOM 2164 C CG . PHE A 1 278 ? 1.037 44.836 24.445 1.00 41.79 ? 278 PHE A CG 1 ATOM 2165 C CD1 . PHE A 1 278 ? 2.367 44.467 24.554 1.00 53.56 ? 278 PHE A CD1 1 ATOM 2166 C CD2 . PHE A 1 278 ? 0.505 45.034 23.180 1.00 39.47 ? 278 PHE A CD2 1 ATOM 2167 C CE1 . PHE A 1 278 ? 3.154 44.305 23.425 1.00 56.01 ? 278 PHE A CE1 1 ATOM 2168 C CE2 . PHE A 1 278 ? 1.287 44.875 22.048 1.00 41.29 ? 278 PHE A CE2 1 ATOM 2169 C CZ . PHE A 1 278 ? 2.613 44.510 22.171 1.00 37.06 ? 278 PHE A CZ 1 ATOM 2170 N N . SER A 1 279 ? -1.156 47.922 25.189 1.00 38.78 ? 279 SER A N 1 ATOM 2171 C CA . SER A 1 279 ? -1.522 48.985 24.266 1.00 46.31 ? 279 SER A CA 1 ATOM 2172 C C . SER A 1 279 ? -2.648 49.823 24.857 1.00 47.72 ? 279 SER A C 1 ATOM 2173 O O . SER A 1 279 ? -3.537 49.298 25.528 1.00 57.72 ? 279 SER A O 1 ATOM 2174 C CB . SER A 1 279 ? -1.940 48.406 22.914 1.00 63.49 ? 279 SER A CB 1 ATOM 2175 O OG . SER A 1 279 ? -3.033 47.516 23.060 1.00 69.00 ? 279 SER A OG 1 ATOM 2176 N N . VAL A 1 280 ? -2.605 51.126 24.607 1.00 47.08 ? 280 VAL A N 1 ATOM 2177 C CA . VAL A 1 280 ? -3.606 52.040 25.143 1.00 43.98 ? 280 VAL A CA 1 ATOM 2178 C C . VAL A 1 280 ? -4.072 53.035 24.087 1.00 46.42 ? 280 VAL A C 1 ATOM 2179 O O . VAL A 1 280 ? -3.352 53.324 23.132 1.00 62.88 ? 280 VAL A O 1 ATOM 2180 C CB . VAL A 1 280 ? -3.065 52.814 26.360 1.00 43.63 ? 280 VAL A CB 1 ATOM 2181 C CG1 . VAL A 1 280 ? -2.947 51.897 27.569 1.00 43.01 ? 280 VAL A CG1 1 ATOM 2182 C CG2 . VAL A 1 280 ? -1.725 53.450 26.027 1.00 49.59 ? 280 VAL A CG2 1 ATOM 2183 N N . ALA A 1 281 ? -5.283 53.551 24.263 1.00 49.10 ? 281 ALA A N 1 ATOM 2184 C CA . ALA A 1 281 ? -5.839 54.533 23.340 1.00 58.08 ? 281 ALA A CA 1 ATOM 2185 C C . ALA A 1 281 ? -6.845 55.433 24.048 1.00 60.84 ? 281 ALA A C 1 ATOM 2186 O O . ALA A 1 281 ? -7.436 55.046 25.057 1.00 64.69 ? 281 ALA A O 1 ATOM 2187 C CB . ALA A 1 281 ? -6.490 53.840 22.154 1.00 69.00 ? 281 ALA A CB 1 ATOM 2188 N N . ALA A 1 282 ? -7.034 56.636 23.516 1.00 58.01 ? 282 ALA A N 1 ATOM 2189 C CA . ALA A 1 282 ? -7.988 57.579 24.084 1.00 59.71 ? 282 ALA A CA 1 ATOM 2190 C C . ALA A 1 282 ? -8.816 58.244 22.992 1.00 67.19 ? 282 ALA A C 1 ATOM 2191 O O . ALA A 1 282 ? -8.273 58.852 22.071 1.00 89.92 ? 282 ALA A O 1 ATOM 2192 C CB . ALA A 1 282 ? -7.267 58.627 24.915 1.00 60.21 ? 282 ALA A CB 1 ATOM 2193 N N . THR A 1 283 ? -10.134 58.113 23.099 1.00 64.77 ? 283 THR A N 1 ATOM 2194 C CA . THR A 1 283 ? -11.063 58.736 22.163 1.00 68.92 ? 283 THR A CA 1 ATOM 2195 C C . THR A 1 283 ? -12.404 58.923 22.852 1.00 85.43 ? 283 THR A C 1 ATOM 2196 O O . THR A 1 283 ? -12.686 58.256 23.845 1.00 108.51 ? 283 THR A O 1 ATOM 2197 C CB . THR A 1 283 ? -11.269 57.885 20.890 1.00 67.55 ? 283 THR A CB 1 ATOM 2198 O OG1 . THR A 1 283 ? -10.065 57.176 20.574 1.00 80.09 ? 283 THR A OG1 1 ATOM 2199 C CG2 . THR A 1 283 ? -11.671 58.760 19.709 1.00 80.44 ? 283 THR A CG2 1 ATOM 2200 N N . ASP A 1 284 ? -13.234 59.822 22.336 1.00 74.62 ? 284 ASP A N 1 ATOM 2201 C CA . ASP A 1 284 ? -14.610 59.877 22.802 1.00 76.27 ? 284 ASP A CA 1 ATOM 2202 C C . ASP A 1 284 ? -15.460 59.038 21.859 1.00 74.03 ? 284 ASP A C 1 ATOM 2203 O O . ASP A 1 284 ? -15.720 59.433 20.724 1.00 73.78 ? 284 ASP A O 1 ATOM 2204 C CB . ASP A 1 284 ? -15.115 61.317 22.859 1.00 86.31 ? 284 ASP A CB 1 ATOM 2205 C CG . ASP A 1 284 ? -16.523 61.416 23.405 1.00 98.83 ? 284 ASP A CG 1 ATOM 2206 O OD1 . ASP A 1 284 ? -17.261 62.329 22.982 1.00 123.15 ? 284 ASP A OD1 1 ATOM 2207 O OD2 . ASP A 1 284 ? -16.892 60.580 24.257 1.00 83.65 ? 284 ASP A OD2 1 ATOM 2208 N N . ILE A 1 285 ? -15.888 57.874 22.338 1.00 72.21 ? 285 ILE A N 1 ATOM 2209 C CA . ILE A 1 285 ? -16.609 56.931 21.494 1.00 70.63 ? 285 ILE A CA 1 ATOM 2210 C C . ILE A 1 285 ? -18.122 57.137 21.546 1.00 73.03 ? 285 ILE A C 1 ATOM 2211 O O . ILE A 1 285 ? -18.850 56.654 20.679 1.00 86.47 ? 285 ILE A O 1 ATOM 2212 C CB . ILE A 1 285 ? -16.277 55.472 21.896 1.00 69.70 ? 285 ILE A CB 1 ATOM 2213 C CG1 . ILE A 1 285 ? -16.303 54.549 20.675 1.00 68.88 ? 285 ILE A CG1 1 ATOM 2214 C CG2 . ILE A 1 285 ? -17.205 54.980 22.998 1.00 83.60 ? 285 ILE A CG2 1 ATOM 2215 C CD1 . ILE A 1 285 ? -15.088 54.687 19.786 1.00 65.84 ? 285 ILE A CD1 1 ATOM 2216 N N . ASN A 1 286 ? -18.591 57.857 22.560 1.00 74.01 ? 286 ASN A N 1 ATOM 2217 C CA . ASN A 1 286 ? -20.022 58.089 22.731 1.00 76.72 ? 286 ASN A CA 1 ATOM 2218 C C . ASN A 1 286 ? -20.483 59.454 22.231 1.00 80.88 ? 286 ASN A C 1 ATOM 2219 O O . ASN A 1 286 ? -21.670 59.775 22.298 1.00 95.41 ? 286 ASN A O 1 ATOM 2220 C CB . ASN A 1 286 ? -20.412 57.907 24.201 1.00 79.03 ? 286 ASN A CB 1 ATOM 2221 C CG . ASN A 1 286 ? -19.386 58.482 25.153 1.00 79.87 ? 286 ASN A CG 1 ATOM 2222 O OD1 . ASN A 1 286 ? -18.312 58.919 24.740 1.00 79.20 ? 286 ASN A OD1 1 ATOM 2223 N ND2 . ASN A 1 286 ? -19.706 58.469 26.443 1.00 81.53 ? 286 ASN A ND2 1 ATOM 2224 N N . GLY A 1 287 ? -19.545 60.255 21.736 1.00 75.39 ? 287 GLY A N 1 ATOM 2225 C CA . GLY A 1 287 ? -19.859 61.593 21.267 1.00 77.50 ? 287 GLY A CA 1 ATOM 2226 C C . GLY A 1 287 ? -20.318 62.500 22.393 1.00 79.99 ? 287 GLY A C 1 ATOM 2227 O O . GLY A 1 287 ? -21.020 63.486 22.165 1.00 78.82 ? 287 GLY A O 1 ATOM 2228 N N . ASP A 1 288 ? -19.917 62.161 23.615 1.00 87.16 ? 288 ASP A N 1 ATOM 2229 C CA . ASP A 1 288 ? -20.324 62.907 24.800 1.00 85.48 ? 288 ASP A CA 1 ATOM 2230 C C . ASP A 1 288 ? -19.302 63.978 25.172 1.00 82.25 ? 288 ASP A C 1 ATOM 2231 O O . ASP A 1 288 ? -19.413 64.606 26.227 1.00 85.31 ? 288 ASP A O 1 ATOM 2232 C CB . ASP A 1 288 ? -20.548 61.960 25.982 1.00 80.63 ? 288 ASP A CB 1 ATOM 2233 C CG . ASP A 1 288 ? -19.249 61.483 26.608 1.00 78.69 ? 288 ASP A CG 1 ATOM 2234 O OD1 . ASP A 1 288 ? -18.387 60.934 25.885 1.00 77.77 ? 288 ASP A OD1 1 ATOM 2235 O OD2 . ASP A 1 288 ? -19.096 61.655 27.835 1.00 80.16 ? 288 ASP A OD2 1 ATOM 2236 N N . ASP A 1 289 ? -18.295 64.142 24.312 1.00 77.86 ? 289 ASP A N 1 ATOM 2237 C CA . ASP A 1 289 ? -17.227 65.138 24.463 1.00 79.59 ? 289 ASP A CA 1 ATOM 2238 C C . ASP A 1 289 ? -16.235 64.780 25.571 1.00 78.35 ? 289 ASP A C 1 ATOM 2239 O O . ASP A 1 289 ? -15.245 65.482 25.771 1.00 81.01 ? 289 ASP A O 1 ATOM 2240 C CB . ASP A 1 289 ? -17.807 66.538 24.708 1.00 102.36 ? 289 ASP A CB 1 ATOM 2241 C CG . ASP A 1 289 ? -18.572 67.068 23.510 1.00 119.54 ? 289 ASP A CG 1 ATOM 2242 O OD1 . ASP A 1 289 ? -19.618 67.723 23.710 1.00 115.49 ? 289 ASP A OD1 1 ATOM 2243 O OD2 . ASP A 1 289 ? -18.126 66.831 22.367 1.00 130.13 ? 289 ASP A OD2 1 ATOM 2244 N N . TYR A 1 290 ? -16.500 63.692 26.287 1.00 78.09 ? 290 TYR A N 1 ATOM 2245 C CA . TYR A 1 290 ? -15.550 63.181 27.271 1.00 76.28 ? 290 TYR A CA 1 ATOM 2246 C C . TYR A 1 290 ? -14.771 62.003 26.695 1.00 73.73 ? 290 TYR A C 1 ATOM 2247 O O . TYR A 1 290 ? -15.360 61.026 26.231 1.00 73.08 ? 290 TYR A O 1 ATOM 2248 C CB . TYR A 1 290 ? -16.265 62.764 28.558 1.00 77.94 ? 290 TYR A CB 1 ATOM 2249 C CG . TYR A 1 290 ? -16.775 63.920 29.391 1.00 81.00 ? 290 TYR A CG 1 ATOM 2250 C CD1 . TYR A 1 290 ? -17.856 63.759 30.248 1.00 84.05 ? 290 TYR A CD1 1 ATOM 2251 C CD2 . TYR A 1 290 ? -16.172 65.169 29.326 1.00 82.27 ? 290 TYR A CD2 1 ATOM 2252 C CE1 . TYR A 1 290 ? -18.326 64.811 31.014 1.00 86.71 ? 290 TYR A CE1 1 ATOM 2253 C CE2 . TYR A 1 290 ? -16.634 66.227 30.088 1.00 92.68 ? 290 TYR A CE2 1 ATOM 2254 C CZ . TYR A 1 290 ? -17.711 66.042 30.930 1.00 94.49 ? 290 TYR A CZ 1 ATOM 2255 O OH . TYR A 1 290 ? -18.174 67.092 31.690 1.00 104.63 ? 290 TYR A OH 1 ATOM 2256 N N . ALA A 1 291 ? -13.445 62.104 26.724 1.00 71.97 ? 291 ALA A N 1 ATOM 2257 C CA . ALA A 1 291 ? -12.578 61.068 26.173 1.00 64.93 ? 291 ALA A CA 1 ATOM 2258 C C . ALA A 1 291 ? -12.675 59.774 26.974 1.00 69.19 ? 291 ALA A C 1 ATOM 2259 O O . ALA A 1 291 ? -12.750 59.799 28.201 1.00 66.60 ? 291 ALA A O 1 ATOM 2260 C CB . ALA A 1 291 ? -11.139 61.553 26.128 1.00 64.84 ? 291 ALA A CB 1 ATOM 2261 N N . ASP A 1 292 ? -12.665 58.644 26.274 1.00 68.64 ? 292 ASP A N 1 ATOM 2262 C CA . ASP A 1 292 ? -12.815 57.343 26.916 1.00 70.16 ? 292 ASP A CA 1 ATOM 2263 C C . ASP A 1 292 ? -11.567 56.481 26.707 1.00 68.99 ? 292 ASP A C 1 ATOM 2264 O O . ASP A 1 292 ? -10.851 56.640 25.717 1.00 64.62 ? 292 ASP A O 1 ATOM 2265 C CB . ASP A 1 292 ? -14.062 56.636 26.382 1.00 72.47 ? 292 ASP A CB 1 ATOM 2266 C CG . ASP A 1 292 ? -15.258 57.572 26.267 1.00 86.64 ? 292 ASP A CG 1 ATOM 2267 O OD1 . ASP A 1 292 ? -15.617 57.951 25.134 1.00 90.54 ? 292 ASP A OD1 1 ATOM 2268 O OD2 . ASP A 1 292 ? -15.837 57.941 27.310 1.00 104.03 ? 292 ASP A OD2 1 ATOM 2269 N N . VAL A 1 293 ? -11.316 55.567 27.641 1.00 73.30 ? 293 VAL A N 1 ATOM 2270 C CA . VAL A 1 293 ? -10.063 54.813 27.669 1.00 65.02 ? 293 VAL A CA 1 ATOM 2271 C C . VAL A 1 293 ? -10.187 53.408 27.078 1.00 63.46 ? 293 VAL A C 1 ATOM 2272 O O . VAL A 1 293 ? -11.141 52.685 27.364 1.00 68.92 ? 293 VAL A O 1 ATOM 2273 C CB . VAL A 1 293 ? -9.528 54.695 29.112 1.00 66.37 ? 293 VAL A CB 1 ATOM 2274 C CG1 . VAL A 1 293 ? -8.144 54.067 29.125 1.00 63.12 ? 293 VAL A CG1 1 ATOM 2275 C CG2 . VAL A 1 293 ? -9.496 56.061 29.776 1.00 68.95 ? 293 VAL A CG2 1 ATOM 2276 N N . PHE A 1 294 ? -9.211 53.033 26.254 1.00 60.61 ? 294 PHE A N 1 ATOM 2277 C CA . PHE A 1 294 ? -9.153 51.698 25.666 1.00 68.33 ? 294 PHE A CA 1 ATOM 2278 C C . PHE A 1 294 ? -7.843 51.010 26.043 1.00 69.75 ? 294 PHE A C 1 ATOM 2279 O O . PHE A 1 294 ? -6.762 51.519 25.749 1.00 86.07 ? 294 PHE A O 1 ATOM 2280 C CB . PHE A 1 294 ? -9.294 51.769 24.144 1.00 67.41 ? 294 PHE A CB 1 ATOM 2281 C CG . PHE A 1 294 ? -10.610 52.329 23.681 1.00 62.19 ? 294 PHE A CG 1 ATOM 2282 C CD1 . PHE A 1 294 ? -10.814 53.697 23.620 1.00 63.67 ? 294 PHE A CD1 1 ATOM 2283 C CD2 . PHE A 1 294 ? -11.641 51.485 23.300 1.00 62.69 ? 294 PHE A CD2 1 ATOM 2284 C CE1 . PHE A 1 294 ? -12.022 54.215 23.195 1.00 74.65 ? 294 PHE A CE1 1 ATOM 2285 C CE2 . PHE A 1 294 ? -12.851 51.997 22.871 1.00 66.97 ? 294 PHE A CE2 1 ATOM 2286 C CZ . PHE A 1 294 ? -13.042 53.364 22.819 1.00 74.27 ? 294 PHE A CZ 1 ATOM 2287 N N . ILE A 1 295 ? -7.940 49.854 26.693 1.00 55.73 ? 295 ILE A N 1 ATOM 2288 C CA . ILE A 1 295 ? -6.754 49.161 27.189 1.00 51.91 ? 295 ILE A CA 1 ATOM 2289 C C . ILE A 1 295 ? -6.627 47.739 26.652 1.00 50.77 ? 295 ILE A C 1 ATOM 2290 O O . ILE A 1 295 ? -7.505 46.903 26.868 1.00 62.33 ? 295 ILE A O 1 ATOM 2291 C CB . ILE A 1 295 ? -6.750 49.096 28.723 1.00 52.66 ? 295 ILE A CB 1 ATOM 2292 C CG1 . ILE A 1 295 ? -6.912 50.497 29.316 1.00 53.96 ? 295 ILE A CG1 1 ATOM 2293 C CG2 . ILE A 1 295 ? -5.472 48.435 29.209 1.00 50.33 ? 295 ILE A CG2 1 ATOM 2294 C CD1 . ILE A 1 295 ? -7.278 50.504 30.783 1.00 55.36 ? 295 ILE A CD1 1 ATOM 2295 N N . GLY A 1 296 ? -5.529 47.468 25.954 1.00 48.22 ? 296 GLY A N 1 ATOM 2296 C CA . GLY A 1 296 ? -5.291 46.149 25.401 1.00 48.60 ? 296 GLY A CA 1 ATOM 2297 C C . GLY A 1 296 ? -4.664 45.162 26.368 1.00 72.66 ? 296 GLY A C 1 ATOM 2298 O O . GLY A 1 296 ? -3.804 45.517 27.174 1.00 82.11 ? 296 GLY A O 1 ATOM 2299 N N . ALA A 1 297 ? -5.100 43.910 26.271 1.00 81.45 ? 297 ALA A N 1 ATOM 2300 C CA . ALA A 1 297 ? -4.509 42.806 27.019 1.00 59.67 ? 297 ALA A CA 1 ATOM 2301 C C . ALA A 1 297 ? -4.503 41.564 26.135 1.00 54.53 ? 297 ALA A C 1 ATOM 2302 O O . ALA A 1 297 ? -5.315 40.658 26.323 1.00 53.68 ? 297 ALA A O 1 ATOM 2303 C CB . ALA A 1 297 ? -5.273 42.552 28.307 1.00 46.46 ? 297 ALA A CB 1 ATOM 2304 N N . PRO A 1 298 ? -3.582 41.522 25.162 1.00 51.73 ? 298 PRO A N 1 ATOM 2305 C CA . PRO A 1 298 ? -3.571 40.502 24.106 1.00 47.12 ? 298 PRO A CA 1 ATOM 2306 C C . PRO A 1 298 ? -3.330 39.083 24.617 1.00 55.62 ? 298 PRO A C 1 ATOM 2307 O O . PRO A 1 298 ? -3.651 38.120 23.921 1.00 83.87 ? 298 PRO A O 1 ATOM 2308 C CB . PRO A 1 298 ? -2.419 40.951 23.203 1.00 51.98 ? 298 PRO A CB 1 ATOM 2309 C CG . PRO A 1 298 ? -1.519 41.724 24.104 1.00 38.80 ? 298 PRO A CG 1 ATOM 2310 C CD . PRO A 1 298 ? -2.429 42.435 25.059 1.00 38.56 ? 298 PRO A CD 1 ATOM 2311 N N . LEU A 1 299 ? -2.760 38.957 25.809 1.00 42.72 ? 299 LEU A N 1 ATOM 2312 C CA . LEU A 1 299 ? -2.448 37.645 26.366 1.00 44.01 ? 299 LEU A CA 1 ATOM 2313 C C . LEU A 1 299 ? -3.522 37.137 27.325 1.00 58.65 ? 299 LEU A C 1 ATOM 2314 O O . LEU A 1 299 ? -3.367 36.076 27.930 1.00 67.09 ? 299 LEU A O 1 ATOM 2315 C CB . LEU A 1 299 ? -1.092 37.683 27.070 1.00 44.58 ? 299 LEU A CB 1 ATOM 2316 C CG . LEU A 1 299 ? 0.125 37.257 26.245 1.00 45.77 ? 299 LEU A CG 1 ATOM 2317 C CD1 . LEU A 1 299 ? -0.016 37.650 24.780 1.00 41.82 ? 299 LEU A CD1 1 ATOM 2318 C CD2 . LEU A 1 299 ? 1.380 37.868 26.840 1.00 70.53 ? 299 LEU A CD2 1 ATOM 2319 N N . PHE A 1 300 ? -4.603 37.898 27.469 1.00 65.27 ? 300 PHE A N 1 ATOM 2320 C CA . PHE A 1 300 ? -5.673 37.537 28.395 1.00 44.60 ? 300 PHE A CA 1 ATOM 2321 C C . PHE A 1 300 ? -6.351 36.231 28.008 1.00 46.43 ? 300 PHE A C 1 ATOM 2322 O O . PHE A 1 300 ? -6.576 35.959 26.829 1.00 51.54 ? 300 PHE A O 1 ATOM 2323 C CB . PHE A 1 300 ? -6.717 38.652 28.475 1.00 53.29 ? 300 PHE A CB 1 ATOM 2324 C CG . PHE A 1 300 ? -7.854 38.352 29.414 1.00 54.56 ? 300 PHE A CG 1 ATOM 2325 C CD1 . PHE A 1 300 ? -7.761 38.675 30.758 1.00 49.07 ? 300 PHE A CD1 1 ATOM 2326 C CD2 . PHE A 1 300 ? -9.015 37.748 28.955 1.00 58.54 ? 300 PHE A CD2 1 ATOM 2327 C CE1 . PHE A 1 300 ? -8.803 38.401 31.624 1.00 57.43 ? 300 PHE A CE1 1 ATOM 2328 C CE2 . PHE A 1 300 ? -10.059 37.472 29.816 1.00 54.53 ? 300 PHE A CE2 1 ATOM 2329 C CZ . PHE A 1 300 ? -9.953 37.800 31.152 1.00 58.79 ? 300 PHE A CZ 1 ATOM 2330 N N . MET A 1 301 ? -6.686 35.435 29.017 1.00 47.88 ? 301 MET A N 1 ATOM 2331 C CA . MET A 1 301 ? -7.358 34.165 28.794 1.00 49.98 ? 301 MET A CA 1 ATOM 2332 C C . MET A 1 301 ? -8.770 34.165 29.365 1.00 54.81 ? 301 MET A C 1 ATOM 2333 O O . MET A 1 301 ? -8.960 34.288 30.575 1.00 57.28 ? 301 MET A O 1 ATOM 2334 C CB . MET A 1 301 ? -6.552 33.018 29.408 1.00 51.15 ? 301 MET A CB 1 ATOM 2335 C CG . MET A 1 301 ? -5.123 32.920 28.903 1.00 50.17 ? 301 MET A CG 1 ATOM 2336 S SD . MET A 1 301 ? -4.265 31.450 29.502 1.00 109.97 ? 301 MET A SD 1 ATOM 2337 C CE . MET A 1 301 ? -4.372 31.688 31.273 1.00 52.57 ? 301 MET A CE 1 ATOM 2338 N N . ASP A 1 302 ? -9.759 34.038 28.486 1.00 64.45 ? 302 ASP A N 1 ATOM 2339 C CA . ASP A 1 302 ? -11.136 33.833 28.915 1.00 61.06 ? 302 ASP A CA 1 ATOM 2340 C C . ASP A 1 302 ? -11.413 32.335 28.972 1.00 59.32 ? 302 ASP A C 1 ATOM 2341 O O . ASP A 1 302 ? -10.495 31.526 28.843 1.00 57.75 ? 302 ASP A O 1 ATOM 2342 C CB . ASP A 1 302 ? -12.121 34.537 27.976 1.00 72.38 ? 302 ASP A CB 1 ATOM 2343 C CG . ASP A 1 302 ? -12.236 33.856 26.623 1.00 83.16 ? 302 ASP A CG 1 ATOM 2344 O OD1 . ASP A 1 302 ? -11.247 33.244 26.168 1.00 105.36 ? 302 ASP A OD1 1 ATOM 2345 O OD2 . ASP A 1 302 ? -13.323 33.938 26.012 1.00 72.11 ? 302 ASP A OD2 1 ATOM 2346 N N . ARG A 1 303 ? -12.672 31.963 29.163 1.00 58.70 ? 303 ARG A N 1 ATOM 2347 C CA . ARG A 1 303 ? -13.027 30.550 29.200 1.00 61.82 ? 303 ARG A CA 1 ATOM 2348 C C . ARG A 1 303 ? -14.057 30.202 28.133 1.00 67.86 ? 303 ARG A C 1 ATOM 2349 O O . ARG A 1 303 ? -15.071 30.884 27.985 1.00 72.62 ? 303 ARG A O 1 ATOM 2350 C CB . ARG A 1 303 ? -13.540 30.166 30.589 1.00 69.66 ? 303 ARG A CB 1 ATOM 2351 C CG . ARG A 1 303 ? -12.474 30.271 31.668 1.00 66.08 ? 303 ARG A CG 1 ATOM 2352 C CD . ARG A 1 303 ? -12.966 29.773 33.015 1.00 69.35 ? 303 ARG A CD 1 ATOM 2353 N NE . ARG A 1 303 ? -11.930 29.893 34.036 1.00 73.80 ? 303 ARG A NE 1 ATOM 2354 C CZ . ARG A 1 303 ? -11.033 28.949 34.305 1.00 82.35 ? 303 ARG A CZ 1 ATOM 2355 N NH1 . ARG A 1 303 ? -11.046 27.807 33.632 1.00 86.04 ? 303 ARG A NH1 1 ATOM 2356 N NH2 . ARG A 1 303 ? -10.123 29.147 35.250 1.00 89.72 ? 303 ARG A NH2 1 ATOM 2357 N N . GLY A 1 304 ? -13.784 29.134 27.390 1.00 74.70 ? 304 GLY A N 1 ATOM 2358 C CA . GLY A 1 304 ? -14.660 28.698 26.319 1.00 73.18 ? 304 GLY A CA 1 ATOM 2359 C C . GLY A 1 304 ? -15.931 28.048 26.829 1.00 69.13 ? 304 GLY A C 1 ATOM 2360 O O . GLY A 1 304 ? -16.226 28.089 28.023 1.00 80.55 ? 304 GLY A O 1 ATOM 2361 N N . SER A 1 305 ? -16.684 27.444 25.916 1.00 72.61 ? 305 SER A N 1 ATOM 2362 C CA . SER A 1 305 ? -17.958 26.820 26.254 1.00 77.35 ? 305 SER A CA 1 ATOM 2363 C C . SER A 1 305 ? -17.786 25.668 27.241 1.00 79.19 ? 305 SER A C 1 ATOM 2364 O O . SER A 1 305 ? -18.649 25.431 28.085 1.00 80.95 ? 305 SER A O 1 ATOM 2365 C CB . SER A 1 305 ? -18.659 26.324 24.988 1.00 89.43 ? 305 SER A CB 1 ATOM 2366 O OG . SER A 1 305 ? -17.843 25.407 24.281 1.00 107.48 ? 305 SER A OG 1 ATOM 2367 N N . ASP A 1 306 ? -16.666 24.960 27.134 1.00 85.90 ? 306 ASP A N 1 ATOM 2368 C CA . ASP A 1 306 ? -16.391 23.835 28.020 1.00 99.95 ? 306 ASP A CA 1 ATOM 2369 C C . ASP A 1 306 ? -15.771 24.297 29.337 1.00 96.82 ? 306 ASP A C 1 ATOM 2370 O O . ASP A 1 306 ? -15.586 23.501 30.258 1.00 105.79 ? 306 ASP A O 1 ATOM 2371 C CB . ASP A 1 306 ? -15.475 22.822 27.330 1.00 108.14 ? 306 ASP A CB 1 ATOM 2372 C CG . ASP A 1 306 ? -14.214 23.457 26.781 1.00 111.92 ? 306 ASP A CG 1 ATOM 2373 O OD1 . ASP A 1 306 ? -14.221 24.681 26.534 1.00 110.22 ? 306 ASP A OD1 1 ATOM 2374 O OD2 . ASP A 1 306 ? -13.217 22.729 26.591 1.00 117.46 ? 306 ASP A OD2 1 ATOM 2375 N N . GLY A 1 307 ? -15.451 25.584 29.420 1.00 79.71 ? 307 GLY A N 1 ATOM 2376 C CA . GLY A 1 307 ? -14.940 26.164 30.649 1.00 78.95 ? 307 GLY A CA 1 ATOM 2377 C C . GLY A 1 307 ? -13.427 26.164 30.753 1.00 77.04 ? 307 GLY A C 1 ATOM 2378 O O . GLY A 1 307 ? -12.866 26.676 31.722 1.00 77.12 ? 307 GLY A O 1 ATOM 2379 N N . LYS A 1 308 ? -12.763 25.588 29.756 1.00 86.47 ? 308 LYS A N 1 ATOM 2380 C CA . LYS A 1 308 ? -11.306 25.533 29.742 1.00 82.93 ? 308 LYS A CA 1 ATOM 2381 C C . LYS A 1 308 ? -10.709 26.917 29.523 1.00 75.75 ? 308 LYS A C 1 ATOM 2382 O O . LYS A 1 308 ? -11.357 27.801 28.964 1.00 71.84 ? 308 LYS A O 1 ATOM 2383 C CB . LYS A 1 308 ? -10.811 24.582 28.652 1.00 89.86 ? 308 LYS A CB 1 ATOM 2384 C CG . LYS A 1 308 ? -11.051 25.096 27.242 1.00 111.54 ? 308 LYS A CG 1 ATOM 2385 C CD . LYS A 1 308 ? -10.368 24.226 26.202 1.00 123.13 ? 308 LYS A CD 1 ATOM 2386 C CE . LYS A 1 308 ? -10.580 24.780 24.803 1.00 110.09 ? 308 LYS A CE 1 ATOM 2387 N NZ . LYS A 1 308 ? -10.069 26.174 24.681 1.00 87.17 ? 308 LYS A NZ 1 ATOM 2388 N N . LEU A 1 309 ? -9.469 27.100 29.963 1.00 75.09 ? 309 LEU A N 1 ATOM 2389 C CA . LEU A 1 309 ? -8.763 28.353 29.731 1.00 66.55 ? 309 LEU A CA 1 ATOM 2390 C C . LEU A 1 309 ? -8.190 28.393 28.320 1.00 70.53 ? 309 LEU A C 1 ATOM 2391 O O . LEU A 1 309 ? -7.608 27.419 27.844 1.00 80.71 ? 309 LEU A O 1 ATOM 2392 C CB . LEU A 1 309 ? -7.649 28.549 30.760 1.00 65.83 ? 309 LEU A CB 1 ATOM 2393 C CG . LEU A 1 309 ? -8.084 29.079 32.127 1.00 60.19 ? 309 LEU A CG 1 ATOM 2394 C CD1 . LEU A 1 309 ? -6.902 29.153 33.077 1.00 59.76 ? 309 LEU A CD1 1 ATOM 2395 C CD2 . LEU A 1 309 ? -8.737 30.442 31.979 1.00 58.28 ? 309 LEU A CD2 1 ATOM 2396 N N . GLN A 1 310 ? -8.373 29.527 27.655 1.00 71.44 ? 310 GLN A N 1 ATOM 2397 C CA . GLN A 1 310 ? -7.836 29.740 26.319 1.00 79.20 ? 310 GLN A CA 1 ATOM 2398 C C . GLN A 1 310 ? -7.497 31.212 26.149 1.00 72.81 ? 310 GLN A C 1 ATOM 2399 O O . GLN A 1 310 ? -8.220 32.076 26.643 1.00 88.92 ? 310 GLN A O 1 ATOM 2400 C CB . GLN A 1 310 ? -8.838 29.290 25.253 1.00 87.85 ? 310 GLN A CB 1 ATOM 2401 C CG . GLN A 1 310 ? -10.182 30.003 25.327 1.00 73.65 ? 310 GLN A CG 1 ATOM 2402 C CD . GLN A 1 310 ? -11.176 29.486 24.307 1.00 76.14 ? 310 GLN A CD 1 ATOM 2403 O OE1 . GLN A 1 310 ? -11.013 28.396 23.761 1.00 83.68 ? 310 GLN A OE1 1 ATOM 2404 N NE2 . GLN A 1 310 ? -12.215 30.271 24.044 1.00 74.33 ? 310 GLN A NE2 1 ATOM 2405 N N . GLU A 1 311 ? -6.409 31.511 25.448 1.00 59.83 ? 311 GLU A N 1 ATOM 2406 C CA . GLU A 1 311 ? -6.019 32.902 25.283 1.00 59.54 ? 311 GLU A CA 1 ATOM 2407 C C . GLU A 1 311 ? -6.594 33.460 23.990 1.00 63.03 ? 311 GLU A C 1 ATOM 2408 O O . GLU A 1 311 ? -6.126 33.139 22.899 1.00 76.66 ? 311 GLU A O 1 ATOM 2409 C CB . GLU A 1 311 ? -4.491 33.020 25.285 1.00 67.58 ? 311 GLU A CB 1 ATOM 2410 C CG . GLU A 1 311 ? -3.943 34.340 24.768 1.00 88.16 ? 311 GLU A CG 1 ATOM 2411 C CD . GLU A 1 311 ? -2.507 34.220 24.293 1.00 101.69 ? 311 GLU A CD 1 ATOM 2412 O OE1 . GLU A 1 311 ? -2.024 35.147 23.609 1.00 125.65 ? 311 GLU A OE1 1 ATOM 2413 O OE2 . GLU A 1 311 ? -1.861 33.196 24.600 1.00 83.16 ? 311 GLU A OE2 1 ATOM 2414 N N . VAL A 1 312 ? -7.630 34.284 24.119 1.00 54.61 ? 312 VAL A N 1 ATOM 2415 C CA . VAL A 1 312 ? -8.164 35.026 22.986 1.00 52.59 ? 312 VAL A CA 1 ATOM 2416 C C . VAL A 1 312 ? -7.750 36.497 22.993 1.00 48.35 ? 312 VAL A C 1 ATOM 2417 O O . VAL A 1 312 ? -8.020 37.224 22.041 1.00 47.70 ? 312 VAL A O 1 ATOM 2418 C CB . VAL A 1 312 ? -9.700 34.941 22.945 1.00 57.48 ? 312 VAL A CB 1 ATOM 2419 C CG1 . VAL A 1 312 ? -10.144 33.488 22.881 1.00 66.65 ? 312 VAL A CG1 1 ATOM 2420 C CG2 . VAL A 1 312 ? -10.301 35.631 24.156 1.00 64.71 ? 312 VAL A CG2 1 ATOM 2421 N N . GLY A 1 313 ? -7.086 36.928 24.061 1.00 47.01 ? 313 GLY A N 1 ATOM 2422 C CA . GLY A 1 313 ? -6.810 38.342 24.262 1.00 58.05 ? 313 GLY A CA 1 ATOM 2423 C C . GLY A 1 313 ? -8.046 39.093 24.732 1.00 56.63 ? 313 GLY A C 1 ATOM 2424 O O . GLY A 1 313 ? -9.165 38.603 24.587 1.00 58.03 ? 313 GLY A O 1 ATOM 2425 N N . GLN A 1 314 ? -7.855 40.283 25.297 1.00 55.98 ? 314 GLN A N 1 ATOM 2426 C CA . GLN A 1 314 ? -8.983 41.076 25.784 1.00 60.16 ? 314 GLN A CA 1 ATOM 2427 C C . GLN A 1 314 ? -8.719 42.579 25.707 1.00 59.90 ? 314 GLN A C 1 ATOM 2428 O O . GLN A 1 314 ? -7.599 43.034 25.935 1.00 70.57 ? 314 GLN A O 1 ATOM 2429 C CB . GLN A 1 314 ? -9.319 40.685 27.224 1.00 62.09 ? 314 GLN A CB 1 ATOM 2430 C CG . GLN A 1 314 ? -10.604 41.284 27.770 1.00 66.15 ? 314 GLN A CG 1 ATOM 2431 C CD . GLN A 1 314 ? -10.789 41.004 29.249 1.00 64.93 ? 314 GLN A CD 1 ATOM 2432 O OE1 . GLN A 1 314 ? -11.703 40.282 29.647 1.00 56.93 ? 314 GLN A OE1 1 ATOM 2433 N NE2 . GLN A 1 314 ? -9.919 41.578 30.073 1.00 70.84 ? 314 GLN A NE2 1 ATOM 2434 N N . VAL A 1 315 ? -9.761 43.344 25.396 1.00 50.73 ? 315 VAL A N 1 ATOM 2435 C CA . VAL A 1 315 ? -9.662 44.799 25.342 1.00 52.70 ? 315 VAL A CA 1 ATOM 2436 C C . VAL A 1 315 ? -10.623 45.452 26.333 1.00 61.45 ? 315 VAL A C 1 ATOM 2437 O O . VAL A 1 315 ? -11.814 45.140 26.352 1.00 68.29 ? 315 VAL A O 1 ATOM 2438 C CB . VAL A 1 315 ? -9.953 45.334 23.928 1.00 52.83 ? 315 VAL A CB 1 ATOM 2439 C CG1 . VAL A 1 315 ? -9.989 46.855 23.929 1.00 53.64 ? 315 VAL A CG1 1 ATOM 2440 C CG2 . VAL A 1 315 ? -8.914 44.822 22.945 1.00 57.74 ? 315 VAL A CG2 1 ATOM 2441 N N . SER A 1 316 ? -10.098 46.358 27.153 1.00 58.51 ? 316 SER A N 1 ATOM 2442 C CA . SER A 1 316 ? -10.900 47.044 28.160 1.00 57.77 ? 316 SER A CA 1 ATOM 2443 C C . SER A 1 316 ? -11.399 48.398 27.658 1.00 59.57 ? 316 SER A C 1 ATOM 2444 O O . SER A 1 316 ? -10.618 49.218 27.178 1.00 65.02 ? 316 SER A O 1 ATOM 2445 C CB . SER A 1 316 ? -10.090 47.226 29.446 1.00 58.44 ? 316 SER A CB 1 ATOM 2446 O OG . SER A 1 316 ? -10.855 47.866 30.452 1.00 71.59 ? 316 SER A OG 1 ATOM 2447 N N . VAL A 1 317 ? -12.705 48.622 27.771 1.00 60.33 ? 317 VAL A N 1 ATOM 2448 C CA . VAL A 1 317 ? -13.315 49.878 27.344 1.00 62.48 ? 317 VAL A CA 1 ATOM 2449 C C . VAL A 1 317 ? -13.902 50.638 28.532 1.00 68.14 ? 317 VAL A C 1 ATOM 2450 O O . VAL A 1 317 ? -14.876 50.196 29.141 1.00 88.02 ? 317 VAL A O 1 ATOM 2451 C CB . VAL A 1 317 ? -14.419 49.639 26.297 1.00 61.38 ? 317 VAL A CB 1 ATOM 2452 C CG1 . VAL A 1 317 ? -15.189 50.923 26.025 1.00 64.56 ? 317 VAL A CG1 1 ATOM 2453 C CG2 . VAL A 1 317 ? -13.818 49.088 25.015 1.00 57.12 ? 317 VAL A CG2 1 ATOM 2454 N N . SER A 1 318 ? -13.308 51.783 28.855 1.00 68.46 ? 318 SER A N 1 ATOM 2455 C CA . SER A 1 318 ? -13.743 52.569 30.005 1.00 72.65 ? 318 SER A CA 1 ATOM 2456 C C . SER A 1 318 ? -14.317 53.921 29.587 1.00 74.35 ? 318 SER A C 1 ATOM 2457 O O . SER A 1 318 ? -13.600 54.782 29.078 1.00 73.03 ? 318 SER A O 1 ATOM 2458 C CB . SER A 1 318 ? -12.580 52.774 30.977 1.00 72.86 ? 318 SER A CB 1 ATOM 2459 O OG . SER A 1 318 ? -12.046 51.531 31.399 1.00 70.10 ? 318 SER A OG 1 ATOM 2460 N N . LEU A 1 319 ? -15.614 54.099 29.816 1.00 75.76 ? 319 LEU A N 1 ATOM 2461 C CA . LEU A 1 319 ? -16.300 55.336 29.457 1.00 76.84 ? 319 LEU A CA 1 ATOM 2462 C C . LEU A 1 319 ? -16.217 56.365 30.581 1.00 79.49 ? 319 LEU A C 1 ATOM 2463 O O . LEU A 1 319 ? -16.642 56.100 31.705 1.00 81.06 ? 319 LEU A O 1 ATOM 2464 C CB . LEU A 1 319 ? -17.770 55.062 29.117 1.00 76.37 ? 319 LEU A CB 1 ATOM 2465 C CG . LEU A 1 319 ? -18.115 54.294 27.836 1.00 73.89 ? 319 LEU A CG 1 ATOM 2466 C CD1 . LEU A 1 319 ? -17.336 54.843 26.653 1.00 70.17 ? 319 LEU A CD1 1 ATOM 2467 C CD2 . LEU A 1 319 ? -17.897 52.792 27.987 1.00 90.68 ? 319 LEU A CD2 1 ATOM 2468 N N . GLN A 1 320 ? -15.673 57.538 30.273 1.00 80.46 ? 320 GLN A N 1 ATOM 2469 C CA . GLN A 1 320 ? -15.604 58.619 31.250 1.00 83.03 ? 320 GLN A CA 1 ATOM 2470 C C . GLN A 1 320 ? -16.950 59.323 31.366 1.00 86.79 ? 320 GLN A C 1 ATOM 2471 O O . GLN A 1 320 ? -17.579 59.650 30.360 1.00 86.32 ? 320 GLN A O 1 ATOM 2472 C CB . GLN A 1 320 ? -14.517 59.628 30.877 1.00 82.09 ? 320 GLN A CB 1 ATOM 2473 C CG . GLN A 1 320 ? -14.397 60.789 31.855 1.00 84.63 ? 320 GLN A CG 1 ATOM 2474 C CD . GLN A 1 320 ? -13.414 61.849 31.396 1.00 86.46 ? 320 GLN A CD 1 ATOM 2475 O OE1 . GLN A 1 320 ? -12.800 61.727 30.337 1.00 93.04 ? 320 GLN A OE1 1 ATOM 2476 N NE2 . GLN A 1 320 ? -13.263 62.899 32.194 1.00 87.25 ? 320 GLN A NE2 1 ATOM 2477 N N . ARG A 1 321 ? -17.386 59.557 32.599 1.00 95.40 ? 321 ARG A N 1 ATOM 2478 C CA . ARG A 1 321 ? -18.657 60.222 32.846 1.00 104.14 ? 321 ARG A CA 1 ATOM 2479 C C . ARG A 1 321 ? -18.439 61.590 33.480 1.00 111.38 ? 321 ARG A C 1 ATOM 2480 O O . ARG A 1 321 ? -17.301 62.026 33.658 1.00 103.03 ? 321 ARG A O 1 ATOM 2481 C CB . ARG A 1 321 ? -19.551 59.360 33.740 1.00 103.94 ? 321 ARG A CB 1 ATOM 2482 C CG . ARG A 1 321 ? -20.909 59.044 33.135 1.00 104.02 ? 321 ARG A CG 1 ATOM 2483 C CD . ARG A 1 321 ? -20.763 58.268 31.836 1.00 100.96 ? 321 ARG A CD 1 ATOM 2484 N NE . ARG A 1 321 ? -22.053 58.006 31.205 1.00 104.69 ? 321 ARG A NE 1 ATOM 2485 C CZ . ARG A 1 321 ? -22.205 57.340 30.065 1.00 113.72 ? 321 ARG A CZ 1 ATOM 2486 N NH1 . ARG A 1 321 ? -21.144 56.866 29.426 1.00 119.07 ? 321 ARG A NH1 1 ATOM 2487 N NH2 . ARG A 1 321 ? -23.417 57.148 29.562 1.00 118.95 ? 321 ARG A NH2 1 ATOM 2488 N N . ALA A 1 322 ? -19.539 62.264 33.803 1.00 120.91 ? 322 ALA A N 1 ATOM 2489 C CA . ALA A 1 322 ? -19.501 63.577 34.440 1.00 125.17 ? 322 ALA A CA 1 ATOM 2490 C C . ALA A 1 322 ? -18.657 63.571 35.711 1.00 122.21 ? 322 ALA A C 1 ATOM 2491 O O . ALA A 1 322 ? -17.646 64.269 35.798 1.00 115.57 ? 322 ALA A O 1 ATOM 2492 C CB . ALA A 1 322 ? -20.913 64.053 34.748 1.00 135.33 ? 322 ALA A CB 1 ATOM 2493 N N . SER A 1 323 ? -19.088 62.784 36.693 1.00 128.56 ? 323 SER A N 1 ATOM 2494 C CA . SER A 1 323 ? -18.421 62.700 37.991 1.00 126.84 ? 323 SER A CA 1 ATOM 2495 C C . SER A 1 323 ? -16.943 62.329 37.886 1.00 126.27 ? 323 SER A C 1 ATOM 2496 O O . SER A 1 323 ? -16.140 62.706 38.739 1.00 123.40 ? 323 SER A O 1 ATOM 2497 C CB . SER A 1 323 ? -19.138 61.685 38.883 1.00 121.58 ? 323 SER A CB 1 ATOM 2498 O OG . SER A 1 323 ? -19.067 60.382 38.329 1.00 117.40 ? 323 SER A OG 1 ATOM 2499 N N . GLY A 1 324 ? -16.586 61.592 36.839 1.00 134.17 ? 324 GLY A N 1 ATOM 2500 C CA . GLY A 1 324 ? -15.217 61.149 36.659 1.00 135.81 ? 324 GLY A CA 1 ATOM 2501 C C . GLY A 1 324 ? -15.049 59.665 36.924 1.00 129.79 ? 324 GLY A C 1 ATOM 2502 O O . GLY A 1 324 ? -13.978 59.102 36.698 1.00 114.49 ? 324 GLY A O 1 ATOM 2503 N N . ASP A 1 325 ? -16.113 59.030 37.404 1.00 130.65 ? 325 ASP A N 1 ATOM 2504 C CA . ASP A 1 325 ? -16.088 57.597 37.669 1.00 114.82 ? 325 ASP A CA 1 ATOM 2505 C C . ASP A 1 325 ? -16.378 56.827 36.388 1.00 105.02 ? 325 ASP A C 1 ATOM 2506 O O . ASP A 1 325 ? -17.447 56.969 35.794 1.00 124.31 ? 325 ASP A O 1 ATOM 2507 C CB . ASP A 1 325 ? -17.103 57.227 38.753 1.00 123.81 ? 325 ASP A CB 1 ATOM 2508 C CG . ASP A 1 325 ? -16.822 57.917 40.074 1.00 138.55 ? 325 ASP A CG 1 ATOM 2509 O OD1 . ASP A 1 325 ? -15.634 58.141 40.390 1.00 145.44 ? 325 ASP A OD1 1 ATOM 2510 O OD2 . ASP A 1 325 ? -17.790 58.235 40.796 1.00 137.95 ? 325 ASP A OD2 1 ATOM 2511 N N . PHE A 1 326 ? -15.419 56.009 35.970 1.00 98.04 ? 326 PHE A N 1 ATOM 2512 C CA . PHE A 1 326 ? -15.521 55.289 34.708 1.00 93.44 ? 326 PHE A CA 1 ATOM 2513 C C . PHE A 1 326 ? -16.548 54.165 34.756 1.00 91.09 ? 326 PHE A C 1 ATOM 2514 O O . PHE A 1 326 ? -16.670 53.462 35.759 1.00 96.30 ? 326 PHE A O 1 ATOM 2515 C CB . PHE A 1 326 ? -14.160 54.714 34.311 1.00 89.45 ? 326 PHE A CB 1 ATOM 2516 C CG . PHE A 1 326 ? -13.134 55.756 33.972 1.00 88.89 ? 326 PHE A CG 1 ATOM 2517 C CD1 . PHE A 1 326 ? -12.970 56.184 32.665 1.00 88.83 ? 326 PHE A CD1 1 ATOM 2518 C CD2 . PHE A 1 326 ? -12.330 56.304 34.957 1.00 91.59 ? 326 PHE A CD2 1 ATOM 2519 C CE1 . PHE A 1 326 ? -12.026 57.141 32.347 1.00 89.01 ? 326 PHE A CE1 1 ATOM 2520 C CE2 . PHE A 1 326 ? -11.384 57.262 34.645 1.00 91.74 ? 326 PHE A CE2 1 ATOM 2521 C CZ . PHE A 1 326 ? -11.232 57.681 33.339 1.00 89.70 ? 326 PHE A CZ 1 ATOM 2522 N N . GLN A 1 327 ? -17.289 54.009 33.664 1.00 91.32 ? 327 GLN A N 1 ATOM 2523 C CA . GLN A 1 327 ? -18.135 52.841 33.475 1.00 93.11 ? 327 GLN A CA 1 ATOM 2524 C C . GLN A 1 327 ? -17.445 51.936 32.463 1.00 87.98 ? 327 GLN A C 1 ATOM 2525 O O . GLN A 1 327 ? -17.379 52.257 31.277 1.00 85.13 ? 327 GLN A O 1 ATOM 2526 C CB . GLN A 1 327 ? -19.532 53.241 32.996 1.00 106.32 ? 327 GLN A CB 1 ATOM 2527 C CG . GLN A 1 327 ? -20.173 54.357 33.811 1.00 123.97 ? 327 GLN A CG 1 ATOM 2528 C CD . GLN A 1 327 ? -20.357 53.989 35.272 1.00 130.22 ? 327 GLN A CD 1 ATOM 2529 O OE1 . GLN A 1 327 ? -20.601 52.830 35.608 1.00 132.99 ? 327 GLN A OE1 1 ATOM 2530 N NE2 . GLN A 1 327 ? -20.237 54.979 36.150 1.00 126.31 ? 327 GLN A NE2 1 ATOM 2531 N N . THR A 1 328 ? -16.931 50.805 32.935 1.00 90.92 ? 328 THR A N 1 ATOM 2532 C CA . THR A 1 328 ? -16.042 49.984 32.121 1.00 78.15 ? 328 THR A CA 1 ATOM 2533 C C . THR A 1 328 ? -16.695 48.696 31.629 1.00 75.92 ? 328 THR A C 1 ATOM 2534 O O . THR A 1 328 ? -17.325 47.968 32.396 1.00 78.66 ? 328 THR A O 1 ATOM 2535 C CB . THR A 1 328 ? -14.757 49.627 32.898 1.00 75.00 ? 328 THR A CB 1 ATOM 2536 O OG1 . THR A 1 328 ? -14.093 50.830 33.303 1.00 75.90 ? 328 THR A OG1 1 ATOM 2537 C CG2 . THR A 1 328 ? -13.814 48.804 32.034 1.00 72.73 ? 328 THR A CG2 1 ATOM 2538 N N . THR A 1 329 ? -16.535 48.431 30.336 1.00 74.65 ? 329 THR A N 1 ATOM 2539 C CA . THR A 1 329 ? -16.993 47.191 29.725 1.00 73.97 ? 329 THR A CA 1 ATOM 2540 C C . THR A 1 329 ? -15.824 46.480 29.048 1.00 84.97 ? 329 THR A C 1 ATOM 2541 O O . THR A 1 329 ? -14.875 47.123 28.598 1.00 96.94 ? 329 THR A O 1 ATOM 2542 C CB . THR A 1 329 ? -18.108 47.446 28.697 1.00 76.51 ? 329 THR A CB 1 ATOM 2543 O OG1 . THR A 1 329 ? -18.296 46.275 27.893 1.00 105.69 ? 329 THR A OG1 1 ATOM 2544 C CG2 . THR A 1 329 ? -17.742 48.616 27.795 1.00 77.26 ? 329 THR A CG2 1 ATOM 2545 N N . LYS A 1 330 ? -15.890 45.154 28.981 1.00 76.05 ? 330 LYS A N 1 ATOM 2546 C CA . LYS A 1 330 ? -14.824 44.372 28.364 1.00 66.67 ? 330 LYS A CA 1 ATOM 2547 C C . LYS A 1 330 ? -15.319 43.596 27.149 1.00 70.32 ? 330 LYS A C 1 ATOM 2548 O O . LYS A 1 330 ? -16.452 43.118 27.127 1.00 86.12 ? 330 LYS A O 1 ATOM 2549 C CB . LYS A 1 330 ? -14.213 43.399 29.375 1.00 61.94 ? 330 LYS A CB 1 ATOM 2550 C CG . LYS A 1 330 ? -13.551 44.052 30.577 1.00 66.53 ? 330 LYS A CG 1 ATOM 2551 C CD . LYS A 1 330 ? -12.839 43.009 31.430 1.00 72.76 ? 330 LYS A CD 1 ATOM 2552 C CE . LYS A 1 330 ? -12.223 43.620 32.678 1.00 77.78 ? 330 LYS A CE 1 ATOM 2553 N NZ . LYS A 1 330 ? -13.257 44.131 33.618 1.00 87.98 ? 330 LYS A NZ 1 ATOM 2554 N N . LEU A 1 331 ? -14.463 43.477 26.139 1.00 64.95 ? 331 LEU A N 1 ATOM 2555 C CA . LEU A 1 331 ? -14.743 42.604 25.005 1.00 68.30 ? 331 LEU A CA 1 ATOM 2556 C C . LEU A 1 331 ? -13.556 41.679 24.760 1.00 73.22 ? 331 LEU A C 1 ATOM 2557 O O . LEU A 1 331 ? -12.412 42.027 25.054 1.00 75.46 ? 331 LEU A O 1 ATOM 2558 C CB . LEU A 1 331 ? -15.067 43.410 23.744 1.00 57.82 ? 331 LEU A CB 1 ATOM 2559 C CG . LEU A 1 331 ? -13.991 44.324 23.159 1.00 68.00 ? 331 LEU A CG 1 ATOM 2560 C CD1 . LEU A 1 331 ? -14.058 44.302 21.642 1.00 55.63 ? 331 LEU A CD1 1 ATOM 2561 C CD2 . LEU A 1 331 ? -14.168 45.738 23.674 1.00 89.27 ? 331 LEU A CD2 1 ATOM 2562 N N . ASN A 1 332 ? -13.836 40.503 24.210 1.00 72.46 ? 332 ASN A N 1 ATOM 2563 C CA . ASN A 1 332 ? -12.838 39.448 24.091 1.00 71.21 ? 332 ASN A CA 1 ATOM 2564 C C . ASN A 1 332 ? -12.510 39.114 22.645 1.00 79.89 ? 332 ASN A C 1 ATOM 2565 O O . ASN A 1 332 ? -13.288 39.404 21.736 1.00 92.50 ? 332 ASN A O 1 ATOM 2566 C CB . ASN A 1 332 ? -13.316 38.183 24.808 1.00 59.48 ? 332 ASN A CB 1 ATOM 2567 C CG . ASN A 1 332 ? -13.450 38.374 26.304 1.00 60.31 ? 332 ASN A CG 1 ATOM 2568 O OD1 . ASN A 1 332 ? -13.175 39.452 26.832 1.00 60.20 ? 332 ASN A OD1 1 ATOM 2569 N ND2 . ASN A 1 332 ? -13.881 37.326 26.997 1.00 61.97 ? 332 ASN A ND2 1 ATOM 2570 N N . GLY A 1 333 ? -11.347 38.506 22.438 1.00 56.94 ? 333 GLY A N 1 ATOM 2571 C CA . GLY A 1 333 ? -10.939 38.073 21.117 1.00 72.39 ? 333 GLY A CA 1 ATOM 2572 C C . GLY A 1 333 ? -11.757 36.893 20.629 1.00 81.01 ? 333 GLY A C 1 ATOM 2573 O O . GLY A 1 333 ? -12.728 36.486 21.267 1.00 88.81 ? 333 GLY A O 1 ATOM 2574 N N . PHE A 1 334 ? -11.359 36.339 19.491 1.00 81.60 ? 334 PHE A N 1 ATOM 2575 C CA . PHE A 1 334 ? -12.122 35.275 18.855 1.00 71.58 ? 334 PHE A CA 1 ATOM 2576 C C . PHE A 1 334 ? -11.251 34.043 18.628 1.00 72.00 ? 334 PHE A C 1 ATOM 2577 O O . PHE A 1 334 ? -11.516 32.975 19.180 1.00 89.62 ? 334 PHE A O 1 ATOM 2578 C CB . PHE A 1 334 ? -12.717 35.774 17.539 1.00 76.78 ? 334 PHE A CB 1 ATOM 2579 C CG . PHE A 1 334 ? -13.341 37.139 17.643 1.00 73.04 ? 334 PHE A CG 1 ATOM 2580 C CD1 . PHE A 1 334 ? -12.628 38.271 17.281 1.00 57.67 ? 334 PHE A CD1 1 ATOM 2581 C CD2 . PHE A 1 334 ? -14.633 37.293 18.117 1.00 68.60 ? 334 PHE A CD2 1 ATOM 2582 C CE1 . PHE A 1 334 ? -13.194 39.528 17.380 1.00 57.00 ? 334 PHE A CE1 1 ATOM 2583 C CE2 . PHE A 1 334 ? -15.205 38.548 18.219 1.00 62.05 ? 334 PHE A CE2 1 ATOM 2584 C CZ . PHE A 1 334 ? -14.484 39.667 17.850 1.00 57.56 ? 334 PHE A CZ 1 ATOM 2585 N N . GLU A 1 335 ? -10.216 34.195 17.808 1.00 63.92 ? 335 GLU A N 1 ATOM 2586 C CA . GLU A 1 335 ? -9.251 33.124 17.595 1.00 70.20 ? 335 GLU A CA 1 ATOM 2587 C C . GLU A 1 335 ? -8.254 33.058 18.749 1.00 63.42 ? 335 GLU A C 1 ATOM 2588 O O . GLU A 1 335 ? -7.871 34.086 19.307 1.00 59.29 ? 335 GLU A O 1 ATOM 2589 C CB . GLU A 1 335 ? -8.514 33.320 16.270 1.00 70.86 ? 335 GLU A CB 1 ATOM 2590 C CG . GLU A 1 335 ? -9.414 33.254 15.048 1.00 81.70 ? 335 GLU A CG 1 ATOM 2591 C CD . GLU A 1 335 ? -8.638 33.318 13.748 1.00 93.75 ? 335 GLU A CD 1 ATOM 2592 O OE1 . GLU A 1 335 ? -9.137 32.795 12.729 1.00 102.20 ? 335 GLU A OE1 1 ATOM 2593 O OE2 . GLU A 1 335 ? -7.528 33.892 13.743 1.00 93.54 ? 335 GLU A OE2 1 ATOM 2594 N N . VAL A 1 336 ? -7.843 31.846 19.111 1.00 62.56 ? 336 VAL A N 1 ATOM 2595 C CA . VAL A 1 336 ? -6.866 31.665 20.179 1.00 62.85 ? 336 VAL A CA 1 ATOM 2596 C C . VAL A 1 336 ? -5.467 32.038 19.698 1.00 70.51 ? 336 VAL A C 1 ATOM 2597 O O . VAL A 1 336 ? -5.149 31.874 18.519 1.00 79.22 ? 336 VAL A O 1 ATOM 2598 C CB . VAL A 1 336 ? -6.858 30.218 20.706 1.00 64.21 ? 336 VAL A CB 1 ATOM 2599 C CG1 . VAL A 1 336 ? -8.150 29.919 21.450 1.00 81.63 ? 336 VAL A CG1 1 ATOM 2600 C CG2 . VAL A 1 336 ? -6.649 29.234 19.566 1.00 89.63 ? 336 VAL A CG2 1 ATOM 2601 N N . PHE A 1 337 ? -4.658 32.575 20.612 1.00 77.67 ? 337 PHE A N 1 ATOM 2602 C CA . PHE A 1 337 ? -3.276 32.983 20.331 1.00 72.33 ? 337 PHE A CA 1 ATOM 2603 C C . PHE A 1 337 ? -3.200 34.166 19.364 1.00 74.61 ? 337 PHE A C 1 ATOM 2604 O O . PHE A 1 337 ? -2.113 34.648 19.046 1.00 98.68 ? 337 PHE A O 1 ATOM 2605 C CB . PHE A 1 337 ? -2.458 31.804 19.794 1.00 72.95 ? 337 PHE A CB 1 ATOM 2606 C CG . PHE A 1 337 ? -2.173 30.747 20.823 1.00 73.79 ? 337 PHE A CG 1 ATOM 2607 C CD1 . PHE A 1 337 ? -2.026 31.085 22.158 1.00 73.37 ? 337 PHE A CD1 1 ATOM 2608 C CD2 . PHE A 1 337 ? -2.056 29.417 20.457 1.00 63.13 ? 337 PHE A CD2 1 ATOM 2609 C CE1 . PHE A 1 337 ? -1.764 30.116 23.110 1.00 61.40 ? 337 PHE A CE1 1 ATOM 2610 C CE2 . PHE A 1 337 ? -1.794 28.443 21.403 1.00 64.54 ? 337 PHE A CE2 1 ATOM 2611 C CZ . PHE A 1 337 ? -1.648 28.793 22.731 1.00 63.65 ? 337 PHE A CZ 1 ATOM 2612 N N . ALA A 1 338 ? -4.357 34.620 18.892 1.00 56.98 ? 338 ALA A N 1 ATOM 2613 C CA . ALA A 1 338 ? -4.437 35.733 17.953 1.00 56.05 ? 338 ALA A CA 1 ATOM 2614 C C . ALA A 1 338 ? -3.941 37.041 18.562 1.00 76.71 ? 338 ALA A C 1 ATOM 2615 O O . ALA A 1 338 ? -3.568 37.963 17.835 1.00 71.50 ? 338 ALA A O 1 ATOM 2616 C CB . ALA A 1 338 ? -5.865 35.897 17.461 1.00 56.68 ? 338 ALA A CB 1 ATOM 2617 N N . ARG A 1 339 ? -3.946 37.111 19.892 1.00 86.82 ? 339 ARG A N 1 ATOM 2618 C CA . ARG A 1 339 ? -3.521 38.305 20.622 1.00 74.65 ? 339 ARG A CA 1 ATOM 2619 C C . ARG A 1 339 ? -4.340 39.521 20.193 1.00 65.37 ? 339 ARG A C 1 ATOM 2620 O O . ARG A 1 339 ? -3.843 40.422 19.516 1.00 67.02 ? 339 ARG A O 1 ATOM 2621 C CB . ARG A 1 339 ? -2.024 38.551 20.426 1.00 52.39 ? 339 ARG A CB 1 ATOM 2622 C CG . ARG A 1 339 ? -1.155 37.458 21.026 1.00 51.77 ? 339 ARG A CG 1 ATOM 2623 C CD . ARG A 1 339 ? 0.317 37.703 20.768 1.00 50.87 ? 339 ARG A CD 1 ATOM 2624 N NE . ARG A 1 339 ? 1.157 36.727 21.456 1.00 51.19 ? 339 ARG A NE 1 ATOM 2625 C CZ . ARG A 1 339 ? 2.482 36.680 21.359 1.00 64.32 ? 339 ARG A CZ 1 ATOM 2626 N NH1 . ARG A 1 339 ? 3.124 37.553 20.596 1.00 56.76 ? 339 ARG A NH1 1 ATOM 2627 N NH2 . ARG A 1 339 ? 3.164 35.758 22.024 1.00 77.44 ? 339 ARG A NH2 1 ATOM 2628 N N . PHE A 1 340 ? -5.605 39.520 20.599 1.00 54.33 ? 340 PHE A N 1 ATOM 2629 C CA . PHE A 1 340 ? -6.597 40.491 20.151 1.00 52.48 ? 340 PHE A CA 1 ATOM 2630 C C . PHE A 1 340 ? -6.295 41.938 20.537 1.00 72.12 ? 340 PHE A C 1 ATOM 2631 O O . PHE A 1 340 ? -6.529 42.851 19.750 1.00 86.92 ? 340 PHE A O 1 ATOM 2632 C CB . PHE A 1 340 ? -7.970 40.093 20.699 1.00 58.43 ? 340 PHE A CB 1 ATOM 2633 C CG . PHE A 1 340 ? -9.069 41.050 20.349 1.00 53.55 ? 340 PHE A CG 1 ATOM 2634 C CD1 . PHE A 1 340 ? -9.342 41.361 19.028 1.00 57.72 ? 340 PHE A CD1 1 ATOM 2635 C CD2 . PHE A 1 340 ? -9.847 41.622 21.342 1.00 56.14 ? 340 PHE A CD2 1 ATOM 2636 C CE1 . PHE A 1 340 ? -10.359 42.238 18.705 1.00 63.18 ? 340 PHE A CE1 1 ATOM 2637 C CE2 . PHE A 1 340 ? -10.866 42.497 21.026 1.00 72.28 ? 340 PHE A CE2 1 ATOM 2638 C CZ . PHE A 1 340 ? -11.122 42.806 19.706 1.00 68.70 ? 340 PHE A CZ 1 ATOM 2639 N N . GLY A 1 341 ? -5.778 42.148 21.742 1.00 58.18 ? 341 GLY A N 1 ATOM 2640 C CA . GLY A 1 341 ? -5.563 43.494 22.245 1.00 55.07 ? 341 GLY A CA 1 ATOM 2641 C C . GLY A 1 341 ? -4.204 44.079 21.907 1.00 66.21 ? 341 GLY A C 1 ATOM 2642 O O . GLY A 1 341 ? -3.743 45.011 22.568 1.00 88.66 ? 341 GLY A O 1 ATOM 2643 N N . SER A 1 342 ? -3.568 43.538 20.873 1.00 49.24 ? 342 SER A N 1 ATOM 2644 C CA . SER A 1 342 ? -2.210 43.929 20.506 1.00 66.22 ? 342 SER A CA 1 ATOM 2645 C C . SER A 1 342 ? -2.092 45.401 20.113 1.00 69.12 ? 342 SER A C 1 ATOM 2646 O O . SER A 1 342 ? -1.202 46.105 20.589 1.00 98.79 ? 342 SER A O 1 ATOM 2647 C CB . SER A 1 342 ? -1.705 43.051 19.362 1.00 72.33 ? 342 SER A CB 1 ATOM 2648 O OG . SER A 1 342 ? -1.733 41.681 19.722 1.00 73.35 ? 342 SER A OG 1 ATOM 2649 N N . ALA A 1 343 ? -2.980 45.862 19.239 1.00 56.96 ? 343 ALA A N 1 ATOM 2650 C CA . ALA A 1 343 ? -2.942 47.250 18.789 1.00 48.91 ? 343 ALA A CA 1 ATOM 2651 C C . ALA A 1 343 ? -4.334 47.875 18.762 1.00 64.38 ? 343 ALA A C 1 ATOM 2652 O O . ALA A 1 343 ? -5.243 47.362 18.111 1.00 65.87 ? 343 ALA A O 1 ATOM 2653 C CB . ALA A 1 343 ? -2.295 47.342 17.415 1.00 49.19 ? 343 ALA A CB 1 ATOM 2654 N N . ILE A 1 344 ? -4.491 48.984 19.478 1.00 55.74 ? 344 ILE A N 1 ATOM 2655 C CA . ILE A 1 344 ? -5.755 49.711 19.501 1.00 50.58 ? 344 ILE A CA 1 ATOM 2656 C C . ILE A 1 344 ? -5.593 51.091 18.870 1.00 51.13 ? 344 ILE A C 1 ATOM 2657 O O . ILE A 1 344 ? -4.951 51.970 19.443 1.00 96.08 ? 344 ILE A O 1 ATOM 2658 C CB . ILE A 1 344 ? -6.285 49.868 20.938 1.00 52.79 ? 344 ILE A CB 1 ATOM 2659 C CG1 . ILE A 1 344 ? -6.336 48.512 21.642 1.00 50.42 ? 344 ILE A CG1 1 ATOM 2660 C CG2 . ILE A 1 344 ? -7.654 50.517 20.931 1.00 51.81 ? 344 ILE A CG2 1 ATOM 2661 C CD1 . ILE A 1 344 ? -6.852 48.585 23.061 1.00 54.82 ? 344 ILE A CD1 1 ATOM 2662 N N . ALA A 1 345 ? -6.175 51.276 17.690 1.00 51.86 ? 345 ALA A N 1 ATOM 2663 C CA . ALA A 1 345 ? -6.033 52.533 16.960 1.00 88.79 ? 345 ALA A CA 1 ATOM 2664 C C . ALA A 1 345 ? -7.358 53.258 16.756 1.00 73.51 ? 345 ALA A C 1 ATOM 2665 O O . ALA A 1 345 ? -8.256 52.738 16.092 1.00 66.07 ? 345 ALA A O 1 ATOM 2666 C CB . ALA A 1 345 ? -5.373 52.283 15.619 1.00 89.48 ? 345 ALA A CB 1 ATOM 2667 N N . PRO A 1 346 ? -7.492 54.459 17.339 1.00 54.57 ? 346 PRO A N 1 ATOM 2668 C CA . PRO A 1 346 ? -8.649 55.290 16.997 1.00 55.94 ? 346 PRO A CA 1 ATOM 2669 C C . PRO A 1 346 ? -8.601 55.690 15.527 1.00 72.76 ? 346 PRO A C 1 ATOM 2670 O O . PRO A 1 346 ? -7.594 56.241 15.081 1.00 70.71 ? 346 PRO A O 1 ATOM 2671 C CB . PRO A 1 346 ? -8.489 56.516 17.904 1.00 59.50 ? 346 PRO A CB 1 ATOM 2672 C CG . PRO A 1 346 ? -7.511 56.102 18.966 1.00 60.49 ? 346 PRO A CG 1 ATOM 2673 C CD . PRO A 1 346 ? -6.606 55.109 18.317 1.00 62.72 ? 346 PRO A CD 1 ATOM 2674 N N . LEU A 1 347 ? -9.669 55.416 14.788 1.00 71.01 ? 347 LEU A N 1 ATOM 2675 C CA . LEU A 1 347 ? -9.738 55.797 13.381 1.00 69.88 ? 347 LEU A CA 1 ATOM 2676 C C . LEU A 1 347 ? -10.559 57.069 13.166 1.00 60.26 ? 347 LEU A C 1 ATOM 2677 O O . LEU A 1 347 ? -10.766 57.497 12.030 1.00 61.33 ? 347 LEU A O 1 ATOM 2678 C CB . LEU A 1 347 ? -10.295 54.640 12.549 1.00 58.16 ? 347 LEU A CB 1 ATOM 2679 C CG . LEU A 1 347 ? -11.483 53.871 13.126 1.00 65.18 ? 347 LEU A CG 1 ATOM 2680 C CD1 . LEU A 1 347 ? -12.775 54.560 12.756 1.00 93.78 ? 347 LEU A CD1 1 ATOM 2681 C CD2 . LEU A 1 347 ? -11.484 52.432 12.641 1.00 57.05 ? 347 LEU A CD2 1 ATOM 2682 N N . GLY A 1 348 ? -11.034 57.661 14.258 1.00 60.42 ? 348 GLY A N 1 ATOM 2683 C CA . GLY A 1 348 ? -11.900 58.825 14.181 1.00 62.20 ? 348 GLY A CA 1 ATOM 2684 C C . GLY A 1 348 ? -13.341 58.400 13.983 1.00 71.17 ? 348 GLY A C 1 ATOM 2685 O O . GLY A 1 348 ? -13.758 57.363 14.497 1.00 81.90 ? 348 GLY A O 1 ATOM 2686 N N . ASP A 1 349 ? -14.111 59.197 13.249 1.00 68.11 ? 349 ASP A N 1 ATOM 2687 C CA . ASP A 1 349 ? -15.462 58.790 12.884 1.00 84.49 ? 349 ASP A CA 1 ATOM 2688 C C . ASP A 1 349 ? -15.462 58.310 11.438 1.00 84.14 ? 349 ASP A C 1 ATOM 2689 O O . ASP A 1 349 ? -15.363 59.107 10.505 1.00 88.70 ? 349 ASP A O 1 ATOM 2690 C CB . ASP A 1 349 ? -16.453 59.939 13.077 1.00 92.24 ? 349 ASP A CB 1 ATOM 2691 C CG . ASP A 1 349 ? -17.895 59.501 12.904 1.00 89.34 ? 349 ASP A CG 1 ATOM 2692 O OD1 . ASP A 1 349 ? -18.153 58.278 12.897 1.00 94.78 ? 349 ASP A OD1 1 ATOM 2693 O OD2 . ASP A 1 349 ? -18.772 60.383 12.788 1.00 78.11 ? 349 ASP A OD2 1 ATOM 2694 N N . LEU A 1 350 ? -15.593 57.000 11.264 1.00 75.52 ? 350 LEU A N 1 ATOM 2695 C CA . LEU A 1 350 ? -15.408 56.374 9.960 1.00 69.09 ? 350 LEU A CA 1 ATOM 2696 C C . LEU A 1 350 ? -16.614 56.551 9.046 1.00 75.89 ? 350 LEU A C 1 ATOM 2697 O O . LEU A 1 350 ? -16.471 56.915 7.880 1.00 92.11 ? 350 LEU A O 1 ATOM 2698 C CB . LEU A 1 350 ? -15.103 54.885 10.136 1.00 66.92 ? 350 LEU A CB 1 ATOM 2699 C CG . LEU A 1 350 ? -14.556 54.124 8.930 1.00 61.64 ? 350 LEU A CG 1 ATOM 2700 C CD1 . LEU A 1 350 ? -13.457 54.921 8.254 1.00 62.51 ? 350 LEU A CD1 1 ATOM 2701 C CD2 . LEU A 1 350 ? -14.036 52.765 9.365 1.00 60.23 ? 350 LEU A CD2 1 ATOM 2702 N N . ASP A 1 351 ? -17.801 56.288 9.581 1.00 77.21 ? 351 ASP A N 1 ATOM 2703 C CA . ASP A 1 351 ? -19.020 56.328 8.784 1.00 84.12 ? 351 ASP A CA 1 ATOM 2704 C C . ASP A 1 351 ? -19.724 57.679 8.877 1.00 94.38 ? 351 ASP A C 1 ATOM 2705 O O . ASP A 1 351 ? -20.814 57.854 8.330 1.00 114.23 ? 351 ASP A O 1 ATOM 2706 C CB . ASP A 1 351 ? -19.967 55.205 9.211 1.00 79.20 ? 351 ASP A CB 1 ATOM 2707 C CG . ASP A 1 351 ? -20.280 55.233 10.695 1.00 73.98 ? 351 ASP A CG 1 ATOM 2708 O OD1 . ASP A 1 351 ? -21.338 54.694 11.082 1.00 74.99 ? 351 ASP A OD1 1 ATOM 2709 O OD2 . ASP A 1 351 ? -19.474 55.791 11.472 1.00 69.18 ? 351 ASP A OD2 1 ATOM 2710 N N . GLN A 1 352 ? -19.093 58.621 9.574 1.00 78.61 ? 352 GLN A N 1 ATOM 2711 C CA . GLN A 1 352 ? -19.659 59.950 9.805 1.00 77.68 ? 352 GLN A CA 1 ATOM 2712 C C . GLN A 1 352 ? -21.026 59.857 10.474 1.00 81.52 ? 352 GLN A C 1 ATOM 2713 O O . GLN A 1 352 ? -21.929 60.641 10.179 1.00 83.03 ? 352 GLN A O 1 ATOM 2714 C CB . GLN A 1 352 ? -19.762 60.737 8.495 1.00 80.06 ? 352 GLN A CB 1 ATOM 2715 C CG . GLN A 1 352 ? -18.420 61.134 7.905 1.00 97.20 ? 352 GLN A CG 1 ATOM 2716 C CD . GLN A 1 352 ? -17.663 62.118 8.774 1.00 102.20 ? 352 GLN A CD 1 ATOM 2717 O OE1 . GLN A 1 352 ? -18.253 63.008 9.387 1.00 109.28 ? 352 GLN A OE1 1 ATOM 2718 N NE2 . GLN A 1 352 ? -16.346 61.959 8.835 1.00 96.38 ? 352 GLN A NE2 1 ATOM 2719 N N . ASP A 1 353 ? -21.166 58.894 11.380 1.00 86.82 ? 353 ASP A N 1 ATOM 2720 C CA . ASP A 1 353 ? -22.419 58.676 12.093 1.00 86.75 ? 353 ASP A CA 1 ATOM 2721 C C . ASP A 1 353 ? -22.627 59.710 13.196 1.00 94.10 ? 353 ASP A C 1 ATOM 2722 O O . ASP A 1 353 ? -23.692 59.772 13.809 1.00 112.91 ? 353 ASP A O 1 ATOM 2723 C CB . ASP A 1 353 ? -22.460 57.262 12.684 1.00 80.93 ? 353 ASP A CB 1 ATOM 2724 C CG . ASP A 1 353 ? -21.181 56.895 13.425 1.00 86.86 ? 353 ASP A CG 1 ATOM 2725 O OD1 . ASP A 1 353 ? -20.426 57.806 13.820 1.00 110.60 ? 353 ASP A OD1 1 ATOM 2726 O OD2 . ASP A 1 353 ? -20.931 55.687 13.617 1.00 77.84 ? 353 ASP A OD2 1 ATOM 2727 N N . GLY A 1 354 ? -21.601 60.517 13.444 1.00 82.73 ? 354 GLY A N 1 ATOM 2728 C CA . GLY A 1 354 ? -21.649 61.505 14.505 1.00 84.04 ? 354 GLY A CA 1 ATOM 2729 C C . GLY A 1 354 ? -20.898 61.022 15.729 1.00 84.59 ? 354 GLY A C 1 ATOM 2730 O O . GLY A 1 354 ? -20.565 61.805 16.618 1.00 88.72 ? 354 GLY A O 1 ATOM 2731 N N . PHE A 1 355 ? -20.634 59.720 15.771 1.00 83.12 ? 355 PHE A N 1 ATOM 2732 C CA . PHE A 1 355 ? -19.884 59.124 16.869 1.00 75.10 ? 355 PHE A CA 1 ATOM 2733 C C . PHE A 1 355 ? -18.596 58.491 16.356 1.00 74.96 ? 355 PHE A C 1 ATOM 2734 O O . PHE A 1 355 ? -18.600 57.783 15.347 1.00 76.06 ? 355 PHE A O 1 ATOM 2735 C CB . PHE A 1 355 ? -20.730 58.079 17.598 1.00 72.70 ? 355 PHE A CB 1 ATOM 2736 C CG . PHE A 1 355 ? -22.066 58.590 18.053 1.00 75.38 ? 355 PHE A CG 1 ATOM 2737 C CD1 . PHE A 1 355 ? -22.175 59.354 19.203 1.00 79.12 ? 355 PHE A CD1 1 ATOM 2738 C CD2 . PHE A 1 355 ? -23.214 58.300 17.336 1.00 77.02 ? 355 PHE A CD2 1 ATOM 2739 C CE1 . PHE A 1 355 ? -23.405 59.824 19.626 1.00 82.62 ? 355 PHE A CE1 1 ATOM 2740 C CE2 . PHE A 1 355 ? -24.446 58.766 17.753 1.00 89.66 ? 355 PHE A CE2 1 ATOM 2741 C CZ . PHE A 1 355 ? -24.541 59.529 18.900 1.00 89.42 ? 355 PHE A CZ 1 ATOM 2742 N N . ASN A 1 356 ? -17.497 58.751 17.057 1.00 75.49 ? 356 ASN A N 1 ATOM 2743 C CA . ASN A 1 356 ? -16.197 58.215 16.672 1.00 69.04 ? 356 ASN A CA 1 ATOM 2744 C C . ASN A 1 356 ? -16.164 56.696 16.748 1.00 65.40 ? 356 ASN A C 1 ATOM 2745 O O . ASN A 1 356 ? -16.902 56.085 17.520 1.00 73.08 ? 356 ASN A O 1 ATOM 2746 C CB . ASN A 1 356 ? -15.095 58.805 17.551 1.00 70.52 ? 356 ASN A CB 1 ATOM 2747 C CG . ASN A 1 356 ? -14.930 60.296 17.352 1.00 86.62 ? 356 ASN A CG 1 ATOM 2748 O OD1 . ASN A 1 356 ? -14.160 60.738 16.500 1.00 92.67 ? 356 ASN A OD1 1 ATOM 2749 N ND2 . ASN A 1 356 ? -15.658 61.083 18.137 1.00 105.08 ? 356 ASN A ND2 1 ATOM 2750 N N . ASP A 1 357 ? -15.307 56.093 15.933 1.00 62.97 ? 357 ASP A N 1 ATOM 2751 C CA . ASP A 1 357 ? -15.189 54.643 15.879 1.00 62.26 ? 357 ASP A CA 1 ATOM 2752 C C . ASP A 1 357 ? -13.723 54.250 16.060 1.00 60.25 ? 357 ASP A C 1 ATOM 2753 O O . ASP A 1 357 ? -12.836 55.096 15.962 1.00 62.66 ? 357 ASP A O 1 ATOM 2754 C CB . ASP A 1 357 ? -15.754 54.113 14.558 1.00 63.33 ? 357 ASP A CB 1 ATOM 2755 C CG . ASP A 1 357 ? -16.969 54.902 14.084 1.00 71.98 ? 357 ASP A CG 1 ATOM 2756 O OD1 . ASP A 1 357 ? -18.067 54.709 14.645 1.00 88.95 ? 357 ASP A OD1 1 ATOM 2757 O OD2 . ASP A 1 357 ? -16.829 55.719 13.150 1.00 67.99 ? 357 ASP A OD2 1 ATOM 2758 N N . ILE A 1 358 ? -13.468 52.975 16.336 1.00 58.97 ? 358 ILE A N 1 ATOM 2759 C CA . ILE A 1 358 ? -12.120 52.539 16.689 1.00 56.22 ? 358 ILE A CA 1 ATOM 2760 C C . ILE A 1 358 ? -11.771 51.184 16.067 1.00 62.05 ? 358 ILE A C 1 ATOM 2761 O O . ILE A 1 358 ? -12.658 50.401 15.724 1.00 62.55 ? 358 ILE A O 1 ATOM 2762 C CB . ILE A 1 358 ? -11.960 52.471 18.229 1.00 56.47 ? 358 ILE A CB 1 ATOM 2763 C CG1 . ILE A 1 358 ? -10.490 52.576 18.639 1.00 62.22 ? 358 ILE A CG1 1 ATOM 2764 C CG2 . ILE A 1 358 ? -12.612 51.213 18.790 1.00 56.62 ? 358 ILE A CG2 1 ATOM 2765 C CD1 . ILE A 1 358 ? -10.297 52.773 20.125 1.00 72.59 ? 358 ILE A CD1 1 ATOM 2766 N N . ALA A 1 359 ? -10.476 50.918 15.913 1.00 54.40 ? 359 ALA A N 1 ATOM 2767 C CA . ALA A 1 359 ? -10.012 49.666 15.320 1.00 53.95 ? 359 ALA A CA 1 ATOM 2768 C C . ALA A 1 359 ? -9.112 48.882 16.272 1.00 77.02 ? 359 ALA A C 1 ATOM 2769 O O . ALA A 1 359 ? -8.219 49.444 16.906 1.00 78.38 ? 359 ALA A O 1 ATOM 2770 C CB . ALA A 1 359 ? -9.279 49.939 14.017 1.00 54.31 ? 359 ALA A CB 1 ATOM 2771 N N . ILE A 1 360 ? -9.357 47.578 16.359 1.00 71.89 ? 360 ILE A N 1 ATOM 2772 C CA . ILE A 1 360 ? -8.554 46.685 17.188 1.00 58.68 ? 360 ILE A CA 1 ATOM 2773 C C . ILE A 1 360 ? -8.021 45.537 16.331 1.00 61.05 ? 360 ILE A C 1 ATOM 2774 O O . ILE A 1 360 ? -8.755 44.976 15.517 1.00 59.38 ? 360 ILE A O 1 ATOM 2775 C CB . ILE A 1 360 ? -9.370 46.128 18.370 1.00 52.34 ? 360 ILE A CB 1 ATOM 2776 C CG1 . ILE A 1 360 ? -10.027 47.269 19.150 1.00 52.61 ? 360 ILE A CG1 1 ATOM 2777 C CG2 . ILE A 1 360 ? -8.490 45.303 19.288 1.00 54.22 ? 360 ILE A CG2 1 ATOM 2778 C CD1 . ILE A 1 360 ? -10.867 46.808 20.318 1.00 53.08 ? 360 ILE A CD1 1 ATOM 2779 N N . ALA A 1 361 ? -6.749 45.190 16.509 1.00 51.69 ? 361 ALA A N 1 ATOM 2780 C CA . ALA A 1 361 ? -6.098 44.232 15.618 1.00 52.01 ? 361 ALA A CA 1 ATOM 2781 C C . ALA A 1 361 ? -5.553 42.997 16.331 1.00 66.44 ? 361 ALA A C 1 ATOM 2782 O O . ALA A 1 361 ? -5.044 43.082 17.447 1.00 70.47 ? 361 ALA A O 1 ATOM 2783 C CB . ALA A 1 361 ? -4.975 44.920 14.856 1.00 71.33 ? 361 ALA A CB 1 ATOM 2784 N N . ALA A 1 362 ? -5.656 41.853 15.660 1.00 66.12 ? 362 ALA A N 1 ATOM 2785 C CA . ALA A 1 362 ? -5.060 40.609 16.134 1.00 55.82 ? 362 ALA A CA 1 ATOM 2786 C C . ALA A 1 362 ? -4.068 40.093 15.094 1.00 53.44 ? 362 ALA A C 1 ATOM 2787 O O . ALA A 1 362 ? -4.426 39.290 14.232 1.00 54.69 ? 362 ALA A O 1 ATOM 2788 C CB . ALA A 1 362 ? -6.131 39.572 16.419 1.00 53.91 ? 362 ALA A CB 1 ATOM 2789 N N . PRO A 1 363 ? -2.812 40.559 15.182 1.00 52.64 ? 363 PRO A N 1 ATOM 2790 C CA . PRO A 1 363 ? -1.744 40.374 14.190 1.00 53.12 ? 363 PRO A CA 1 ATOM 2791 C C . PRO A 1 363 ? -1.411 38.920 13.891 1.00 68.83 ? 363 PRO A C 1 ATOM 2792 O O . PRO A 1 363 ? -0.973 38.602 12.787 1.00 72.86 ? 363 PRO A O 1 ATOM 2793 C CB . PRO A 1 363 ? -0.539 41.067 14.840 1.00 55.71 ? 363 PRO A CB 1 ATOM 2794 C CG . PRO A 1 363 ? -1.125 42.007 15.832 1.00 63.64 ? 363 PRO A CG 1 ATOM 2795 C CD . PRO A 1 363 ? -2.341 41.318 16.351 1.00 51.31 ? 363 PRO A CD 1 ATOM 2796 N N . TYR A 1 364 ? -1.572 38.056 14.882 1.00 65.20 ? 364 TYR A N 1 ATOM 2797 C CA . TYR A 1 364 ? -1.276 36.642 14.708 1.00 59.18 ? 364 TYR A CA 1 ATOM 2798 C C . TYR A 1 364 ? -2.539 35.829 14.441 1.00 57.38 ? 364 TYR A C 1 ATOM 2799 O O . TYR A 1 364 ? -2.492 34.603 14.348 1.00 79.08 ? 364 TYR A O 1 ATOM 2800 C CB . TYR A 1 364 ? -0.513 36.135 15.927 1.00 60.82 ? 364 TYR A CB 1 ATOM 2801 C CG . TYR A 1 364 ? 0.661 37.036 16.231 1.00 59.87 ? 364 TYR A CG 1 ATOM 2802 C CD1 . TYR A 1 364 ? 0.639 37.899 17.317 1.00 60.35 ? 364 TYR A CD1 1 ATOM 2803 C CD2 . TYR A 1 364 ? 1.769 37.064 15.395 1.00 61.72 ? 364 TYR A CD2 1 ATOM 2804 C CE1 . TYR A 1 364 ? 1.705 38.740 17.583 1.00 59.92 ? 364 TYR A CE1 1 ATOM 2805 C CE2 . TYR A 1 364 ? 2.836 37.901 15.650 1.00 79.62 ? 364 TYR A CE2 1 ATOM 2806 C CZ . TYR A 1 364 ? 2.801 38.737 16.745 1.00 73.11 ? 364 TYR A CZ 1 ATOM 2807 O OH . TYR A 1 364 ? 3.865 39.571 17.002 1.00 78.91 ? 364 TYR A OH 1 ATOM 2808 N N . GLY A 1 365 ? -3.668 36.522 14.326 1.00 58.39 ? 365 GLY A N 1 ATOM 2809 C CA . GLY A 1 365 ? -4.931 35.881 14.009 1.00 63.28 ? 365 GLY A CA 1 ATOM 2810 C C . GLY A 1 365 ? -5.160 35.736 12.517 1.00 69.37 ? 365 GLY A C 1 ATOM 2811 O O . GLY A 1 365 ? -4.224 35.830 11.724 1.00 78.75 ? 365 GLY A O 1 ATOM 2812 N N . GLY A 1 366 ? -6.412 35.500 12.134 1.00 73.35 ? 366 GLY A N 1 ATOM 2813 C CA . GLY A 1 366 ? -6.772 35.364 10.734 1.00 85.49 ? 366 GLY A CA 1 ATOM 2814 C C . GLY A 1 366 ? -6.467 33.990 10.169 1.00 104.36 ? 366 GLY A C 1 ATOM 2815 O O . GLY A 1 366 ? -6.360 33.012 10.910 1.00 103.77 ? 366 GLY A O 1 ATOM 2816 N N . GLU A 1 367 ? -6.327 33.915 8.849 1.00 115.30 ? 367 GLU A N 1 ATOM 2817 C CA . GLU A 1 367 ? -6.000 32.659 8.184 1.00 105.57 ? 367 GLU A CA 1 ATOM 2818 C C . GLU A 1 367 ? -4.508 32.368 8.280 1.00 104.58 ? 367 GLU A C 1 ATOM 2819 O O . GLU A 1 367 ? -3.692 33.115 7.744 1.00 105.78 ? 367 GLU A O 1 ATOM 2820 C CB . GLU A 1 367 ? -6.429 32.705 6.716 1.00 106.54 ? 367 GLU A CB 1 ATOM 2821 C CG . GLU A 1 367 ? -5.786 31.637 5.844 1.00 123.23 ? 367 GLU A CG 1 ATOM 2822 C CD . GLU A 1 367 ? -5.711 32.047 4.385 1.00 133.37 ? 367 GLU A CD 1 ATOM 2823 O OE1 . GLU A 1 367 ? -6.344 33.058 4.016 1.00 133.12 ? 367 GLU A OE1 1 ATOM 2824 O OE2 . GLU A 1 367 ? -5.012 31.362 3.609 1.00 138.76 ? 367 GLU A OE2 1 ATOM 2825 N N . ASP A 1 368 ? -4.171 31.265 8.942 1.00 108.36 ? 368 ASP A N 1 ATOM 2826 C CA . ASP A 1 368 ? -2.785 30.848 9.155 1.00 105.78 ? 368 ASP A CA 1 ATOM 2827 C C . ASP A 1 368 ? -1.863 31.998 9.559 1.00 89.52 ? 368 ASP A C 1 ATOM 2828 O O . ASP A 1 368 ? -0.914 32.321 8.843 1.00 89.62 ? 368 ASP A O 1 ATOM 2829 C CB . ASP A 1 368 ? -2.241 30.170 7.895 1.00 116.75 ? 368 ASP A CB 1 ATOM 2830 C CG . ASP A 1 368 ? -2.936 28.857 7.595 1.00 138.22 ? 368 ASP A CG 1 ATOM 2831 O OD1 . ASP A 1 368 ? -2.280 27.950 7.040 1.00 151.76 ? 368 ASP A OD1 1 ATOM 2832 O OD2 . ASP A 1 368 ? -4.136 28.730 7.916 1.00 143.24 ? 368 ASP A OD2 1 ATOM 2833 N N . LYS A 1 369 ? -2.157 32.608 10.704 1.00 84.55 ? 369 LYS A N 1 ATOM 2834 C CA . LYS A 1 369 ? -1.307 33.638 11.302 1.00 90.70 ? 369 LYS A CA 1 ATOM 2835 C C . LYS A 1 369 ? -0.995 34.806 10.360 1.00 85.87 ? 369 LYS A C 1 ATOM 2836 O O . LYS A 1 369 ? 0.058 35.434 10.476 1.00 109.51 ? 369 LYS A O 1 ATOM 2837 C CB . LYS A 1 369 ? 0.001 33.008 11.791 1.00 112.13 ? 369 LYS A CB 1 ATOM 2838 C CG . LYS A 1 369 ? 0.480 33.517 13.142 1.00 121.45 ? 369 LYS A CG 1 ATOM 2839 C CD . LYS A 1 369 ? 1.714 32.754 13.603 1.00 117.70 ? 369 LYS A CD 1 ATOM 2840 C CE . LYS A 1 369 ? 2.109 33.131 15.023 1.00 105.11 ? 369 LYS A CE 1 ATOM 2841 N NZ . LYS A 1 369 ? 1.081 32.726 16.020 1.00 100.39 ? 369 LYS A NZ 1 ATOM 2842 N N . LYS A 1 370 ? -1.905 35.096 9.435 1.00 73.86 ? 370 LYS A N 1 ATOM 2843 C CA . LYS A 1 370 ? -1.707 36.199 8.496 1.00 73.87 ? 370 LYS A CA 1 ATOM 2844 C C . LYS A 1 370 ? -2.026 37.551 9.123 1.00 70.13 ? 370 LYS A C 1 ATOM 2845 O O . LYS A 1 370 ? -1.505 38.579 8.695 1.00 72.31 ? 370 LYS A O 1 ATOM 2846 C CB . LYS A 1 370 ? -2.560 36.004 7.240 1.00 75.33 ? 370 LYS A CB 1 ATOM 2847 C CG . LYS A 1 370 ? -1.878 35.209 6.139 1.00 77.09 ? 370 LYS A CG 1 ATOM 2848 C CD . LYS A 1 370 ? -2.724 35.193 4.874 1.00 88.06 ? 370 LYS A CD 1 ATOM 2849 C CE . LYS A 1 370 ? -2.014 34.469 3.741 1.00 98.95 ? 370 LYS A CE 1 ATOM 2850 N NZ . LYS A 1 370 ? -2.817 34.480 2.486 1.00 104.77 ? 370 LYS A NZ 1 ATOM 2851 N N . GLY A 1 371 ? -2.885 37.543 10.137 1.00 66.43 ? 371 GLY A N 1 ATOM 2852 C CA . GLY A 1 371 ? -3.282 38.766 10.808 1.00 61.23 ? 371 GLY A CA 1 ATOM 2853 C C . GLY A 1 371 ? -4.678 39.224 10.440 1.00 66.63 ? 371 GLY A C 1 ATOM 2854 O O . GLY A 1 371 ? -5.171 38.939 9.349 1.00 88.43 ? 371 GLY A O 1 ATOM 2855 N N . ILE A 1 372 ? -5.316 39.939 11.360 1.00 56.73 ? 372 ILE A N 1 ATOM 2856 C CA . ILE A 1 372 ? -6.678 40.407 11.150 1.00 56.89 ? 372 ILE A CA 1 ATOM 2857 C C . ILE A 1 372 ? -6.931 41.695 11.938 1.00 55.60 ? 372 ILE A C 1 ATOM 2858 O O . ILE A 1 372 ? -6.372 41.891 13.018 1.00 54.54 ? 372 ILE A O 1 ATOM 2859 C CB . ILE A 1 372 ? -7.699 39.313 11.546 1.00 57.58 ? 372 ILE A CB 1 ATOM 2860 C CG1 . ILE A 1 372 ? -9.112 39.679 11.092 1.00 58.05 ? 372 ILE A CG1 1 ATOM 2861 C CG2 . ILE A 1 372 ? -7.651 39.037 13.044 1.00 96.63 ? 372 ILE A CG2 1 ATOM 2862 C CD1 . ILE A 1 372 ? -10.120 38.584 11.355 1.00 82.11 ? 372 ILE A CD1 1 ATOM 2863 N N . VAL A 1 373 ? -7.758 42.578 11.386 1.00 55.85 ? 373 VAL A N 1 ATOM 2864 C CA . VAL A 1 373 ? -8.071 43.847 12.037 1.00 55.01 ? 373 VAL A CA 1 ATOM 2865 C C . VAL A 1 373 ? -9.577 44.077 12.126 1.00 63.28 ? 373 VAL A C 1 ATOM 2866 O O . VAL A 1 373 ? -10.254 44.214 11.106 1.00 66.24 ? 373 VAL A O 1 ATOM 2867 C CB . VAL A 1 373 ? -7.428 45.038 11.297 1.00 55.12 ? 373 VAL A CB 1 ATOM 2868 C CG1 . VAL A 1 373 ? -7.877 46.352 11.916 1.00 59.78 ? 373 VAL A CG1 1 ATOM 2869 C CG2 . VAL A 1 373 ? -5.912 44.925 11.316 1.00 54.72 ? 373 VAL A CG2 1 ATOM 2870 N N . TYR A 1 374 ? -10.095 44.123 13.349 1.00 54.77 ? 374 TYR A N 1 ATOM 2871 C CA . TYR A 1 374 ? -11.516 44.366 13.572 1.00 55.14 ? 374 TYR A CA 1 ATOM 2872 C C . TYR A 1 374 ? -11.774 45.845 13.828 1.00 55.09 ? 374 TYR A C 1 ATOM 2873 O O . TYR A 1 374 ? -11.055 46.480 14.598 1.00 57.21 ? 374 TYR A O 1 ATOM 2874 C CB . TYR A 1 374 ? -12.032 43.543 14.755 1.00 55.07 ? 374 TYR A CB 1 ATOM 2875 C CG . TYR A 1 374 ? -11.698 42.070 14.693 1.00 55.50 ? 374 TYR A CG 1 ATOM 2876 C CD1 . TYR A 1 374 ? -12.539 41.172 14.050 1.00 62.64 ? 374 TYR A CD1 1 ATOM 2877 C CD2 . TYR A 1 374 ? -10.545 41.576 15.289 1.00 55.02 ? 374 TYR A CD2 1 ATOM 2878 C CE1 . TYR A 1 374 ? -12.237 39.825 13.996 1.00 67.37 ? 374 TYR A CE1 1 ATOM 2879 C CE2 . TYR A 1 374 ? -10.235 40.232 15.239 1.00 63.57 ? 374 TYR A CE2 1 ATOM 2880 C CZ . TYR A 1 374 ? -11.083 39.361 14.592 1.00 63.22 ? 374 TYR A CZ 1 ATOM 2881 O OH . TYR A 1 374 ? -10.776 38.020 14.544 1.00 61.38 ? 374 TYR A OH 1 ATOM 2882 N N . ILE A 1 375 ? -12.801 46.392 13.185 1.00 57.58 ? 375 ILE A N 1 ATOM 2883 C CA . ILE A 1 375 ? -13.189 47.774 13.435 1.00 57.38 ? 375 ILE A CA 1 ATOM 2884 C C . ILE A 1 375 ? -14.549 47.816 14.129 1.00 56.40 ? 375 ILE A C 1 ATOM 2885 O O . ILE A 1 375 ? -15.408 46.967 13.891 1.00 59.53 ? 375 ILE A O 1 ATOM 2886 C CB . ILE A 1 375 ? -13.228 48.610 12.135 1.00 61.04 ? 375 ILE A CB 1 ATOM 2887 C CG1 . ILE A 1 375 ? -14.414 48.217 11.254 1.00 82.24 ? 375 ILE A CG1 1 ATOM 2888 C CG2 . ILE A 1 375 ? -11.920 48.462 11.369 1.00 59.34 ? 375 ILE A CG2 1 ATOM 2889 C CD1 . ILE A 1 375 ? -14.651 49.175 10.109 1.00 103.91 ? 375 ILE A CD1 1 ATOM 2890 N N . PHE A 1 376 ? -14.730 48.801 15.002 1.00 56.03 ? 376 PHE A N 1 ATOM 2891 C CA . PHE A 1 376 ? -15.934 48.882 15.818 1.00 57.89 ? 376 PHE A CA 1 ATOM 2892 C C . PHE A 1 376 ? -16.533 50.282 15.800 1.00 66.61 ? 376 PHE A C 1 ATOM 2893 O O . PHE A 1 376 ? -15.875 51.253 16.173 1.00 74.57 ? 376 PHE A O 1 ATOM 2894 C CB . PHE A 1 376 ? -15.630 48.470 17.261 1.00 62.20 ? 376 PHE A CB 1 ATOM 2895 C CG . PHE A 1 376 ? -15.074 47.080 17.393 1.00 67.28 ? 376 PHE A CG 1 ATOM 2896 C CD1 . PHE A 1 376 ? -13.708 46.856 17.320 1.00 60.23 ? 376 PHE A CD1 1 ATOM 2897 C CD2 . PHE A 1 376 ? -15.915 45.999 17.599 1.00 75.73 ? 376 PHE A CD2 1 ATOM 2898 C CE1 . PHE A 1 376 ? -13.193 45.581 17.444 1.00 55.12 ? 376 PHE A CE1 1 ATOM 2899 C CE2 . PHE A 1 376 ? -15.405 44.720 17.723 1.00 67.69 ? 376 PHE A CE2 1 ATOM 2900 C CZ . PHE A 1 376 ? -14.042 44.511 17.646 1.00 56.93 ? 376 PHE A CZ 1 ATOM 2901 N N . ASN A 1 377 ? -17.786 50.381 15.368 1.00 62.60 ? 377 ASN A N 1 ATOM 2902 C CA . ASN A 1 377 ? -18.486 51.657 15.362 1.00 66.98 ? 377 ASN A CA 1 ATOM 2903 C C . ASN A 1 377 ? -18.975 52.043 16.753 1.00 69.66 ? 377 ASN A C 1 ATOM 2904 O O . ASN A 1 377 ? -19.496 51.208 17.493 1.00 80.36 ? 377 ASN A O 1 ATOM 2905 C CB . ASN A 1 377 ? -19.667 51.620 14.390 1.00 83.19 ? 377 ASN A CB 1 ATOM 2906 C CG . ASN A 1 377 ? -19.228 51.567 12.940 1.00 97.34 ? 377 ASN A CG 1 ATOM 2907 O OD1 . ASN A 1 377 ? -18.159 51.046 12.622 1.00 102.78 ? 377 ASN A OD1 1 ATOM 2908 N ND2 . ASN A 1 377 ? -20.051 52.114 12.053 1.00 101.70 ? 377 ASN A ND2 1 ATOM 2909 N N . GLY A 1 378 ? -18.799 53.311 17.106 1.00 67.45 ? 378 GLY A N 1 ATOM 2910 C CA . GLY A 1 378 ? -19.288 53.821 18.372 1.00 71.66 ? 378 GLY A CA 1 ATOM 2911 C C . GLY A 1 378 ? -20.660 54.446 18.215 1.00 75.90 ? 378 GLY A C 1 ATOM 2912 O O . GLY A 1 378 ? -21.063 54.804 17.108 1.00 83.64 ? 378 GLY A O 1 ATOM 2913 N N . ARG A 1 379 ? -21.381 54.574 19.323 1.00 78.87 ? 379 ARG A N 1 ATOM 2914 C CA . ARG A 1 379 ? -22.710 55.174 19.303 1.00 82.42 ? 379 ARG A CA 1 ATOM 2915 C C . ARG A 1 379 ? -23.014 55.870 20.626 1.00 85.44 ? 379 ARG A C 1 ATOM 2916 O O . ARG A 1 379 ? -22.153 55.956 21.501 1.00 84.80 ? 379 ARG A O 1 ATOM 2917 C CB . ARG A 1 379 ? -23.773 54.114 19.000 1.00 84.13 ? 379 ARG A CB 1 ATOM 2918 C CG . ARG A 1 379 ? -23.807 52.968 19.995 1.00 93.16 ? 379 ARG A CG 1 ATOM 2919 C CD . ARG A 1 379 ? -24.699 51.834 19.516 1.00 109.20 ? 379 ARG A CD 1 ATOM 2920 N NE . ARG A 1 379 ? -24.719 50.720 20.461 1.00 110.18 ? 379 ARG A NE 1 ATOM 2921 C CZ . ARG A 1 379 ? -25.320 49.557 20.233 1.00 105.72 ? 379 ARG A CZ 1 ATOM 2922 N NH1 . ARG A 1 379 ? -25.951 49.347 19.086 1.00 98.98 ? 379 ARG A NH1 1 ATOM 2923 N NH2 . ARG A 1 379 ? -25.286 48.600 21.152 1.00 106.55 ? 379 ARG A NH2 1 ATOM 2924 N N . SER A 1 380 ? -24.240 56.364 20.763 1.00 88.97 ? 380 SER A N 1 ATOM 2925 C CA . SER A 1 380 ? -24.651 57.099 21.955 1.00 95.01 ? 380 SER A CA 1 ATOM 2926 C C . SER A 1 380 ? -24.587 56.235 23.211 1.00 94.93 ? 380 SER A C 1 ATOM 2927 O O . SER A 1 380 ? -24.287 56.724 24.300 1.00 97.69 ? 380 SER A O 1 ATOM 2928 C CB . SER A 1 380 ? -26.067 57.650 21.775 1.00 104.10 ? 380 SER A CB 1 ATOM 2929 O OG . SER A 1 380 ? -26.988 56.605 21.513 1.00 110.31 ? 380 SER A OG 1 ATOM 2930 N N . THR A 1 381 ? -24.862 54.945 23.047 1.00 93.97 ? 381 THR A N 1 ATOM 2931 C CA . THR A 1 381 ? -24.854 53.996 24.156 1.00 94.85 ? 381 THR A CA 1 ATOM 2932 C C . THR A 1 381 ? -23.435 53.680 24.622 1.00 92.03 ? 381 THR A C 1 ATOM 2933 O O . THR A 1 381 ? -23.239 52.940 25.587 1.00 90.90 ? 381 THR A O 1 ATOM 2934 C CB . THR A 1 381 ? -25.557 52.679 23.775 1.00 102.17 ? 381 THR A CB 1 ATOM 2935 O OG1 . THR A 1 381 ? -24.711 51.913 22.909 1.00 107.71 ? 381 THR A OG1 1 ATOM 2936 C CG2 . THR A 1 381 ? -26.879 52.962 23.076 1.00 101.96 ? 381 THR A CG2 1 ATOM 2937 N N . GLY A 1 382 ? -22.449 54.240 23.930 1.00 93.68 ? 382 GLY A N 1 ATOM 2938 C CA . GLY A 1 382 ? -21.061 53.874 24.137 1.00 91.79 ? 382 GLY A CA 1 ATOM 2939 C C . GLY A 1 382 ? -20.620 53.012 22.973 1.00 91.41 ? 382 GLY A C 1 ATOM 2940 O O . GLY A 1 382 ? -21.328 52.923 21.971 1.00 104.13 ? 382 GLY A O 1 ATOM 2941 N N . LEU A 1 383 ? -19.457 52.382 23.085 1.00 83.91 ? 383 LEU A N 1 ATOM 2942 C CA . LEU A 1 383 ? -18.975 51.548 21.994 1.00 77.58 ? 383 LEU A CA 1 ATOM 2943 C C . LEU A 1 383 ? -19.827 50.296 21.849 1.00 75.31 ? 383 LEU A C 1 ATOM 2944 O O . LEU A 1 383 ? -19.963 49.511 22.787 1.00 76.23 ? 383 LEU A O 1 ATOM 2945 C CB . LEU A 1 383 ? -17.513 51.155 22.207 1.00 73.96 ? 383 LEU A CB 1 ATOM 2946 C CG . LEU A 1 383 ? -16.997 50.113 21.211 1.00 69.68 ? 383 LEU A CG 1 ATOM 2947 C CD1 . LEU A 1 383 ? -17.039 50.660 19.792 1.00 69.29 ? 383 LEU A CD1 1 ATOM 2948 C CD2 . LEU A 1 383 ? -15.594 49.650 21.573 1.00 66.95 ? 383 LEU A CD2 1 ATOM 2949 N N . ASN A 1 384 ? -20.393 50.115 20.662 1.00 81.71 ? 384 ASN A N 1 ATOM 2950 C CA . ASN A 1 384 ? -21.117 48.897 20.335 1.00 83.87 ? 384 ASN A CA 1 ATOM 2951 C C . ASN A 1 384 ? -20.123 47.796 20.014 1.00 70.34 ? 384 ASN A C 1 ATOM 2952 O O . ASN A 1 384 ? -19.251 47.979 19.164 1.00 63.23 ? 384 ASN A O 1 ATOM 2953 C CB . ASN A 1 384 ? -22.063 49.132 19.157 1.00 83.25 ? 384 ASN A CB 1 ATOM 2954 C CG . ASN A 1 384 ? -22.349 47.867 18.377 1.00 72.35 ? 384 ASN A CG 1 ATOM 2955 O OD1 . ASN A 1 384 ? -21.685 47.577 17.382 1.00 70.69 ? 384 ASN A OD1 1 ATOM 2956 N ND2 . ASN A 1 384 ? -23.341 47.105 18.823 1.00 74.52 ? 384 ASN A ND2 1 ATOM 2957 N N . ALA A 1 385 ? -20.245 46.651 20.677 1.00 65.74 ? 385 ALA A N 1 ATOM 2958 C CA . ALA A 1 385 ? -19.235 45.620 20.501 1.00 62.87 ? 385 ALA A CA 1 ATOM 2959 C C . ALA A 1 385 ? -19.700 44.542 19.536 1.00 62.22 ? 385 ALA A C 1 ATOM 2960 O O . ALA A 1 385 ? -20.509 43.680 19.878 1.00 99.70 ? 385 ALA A O 1 ATOM 2961 C CB . ALA A 1 385 ? -18.869 45.006 21.841 1.00 59.04 ? 385 ALA A CB 1 ATOM 2962 N N . VAL A 1 386 ? -19.139 44.619 18.334 1.00 61.30 ? 386 VAL A N 1 ATOM 2963 C CA . VAL A 1 386 ? -19.260 43.637 17.263 1.00 61.92 ? 386 VAL A CA 1 ATOM 2964 C C . VAL A 1 386 ? -18.549 44.276 16.077 1.00 63.77 ? 386 VAL A C 1 ATOM 2965 O O . VAL A 1 386 ? -18.710 45.473 15.832 1.00 68.66 ? 386 VAL A O 1 ATOM 2966 C CB . VAL A 1 386 ? -20.732 43.278 16.906 1.00 70.65 ? 386 VAL A CB 1 ATOM 2967 C CG1 . VAL A 1 386 ? -21.549 44.524 16.597 1.00 85.48 ? 386 VAL A CG1 1 ATOM 2968 C CG2 . VAL A 1 386 ? -20.785 42.294 15.745 1.00 68.25 ? 386 VAL A CG2 1 ATOM 2969 N N . PRO A 1 387 ? -17.737 43.500 15.348 1.00 62.09 ? 387 PRO A N 1 ATOM 2970 C CA . PRO A 1 387 ? -17.080 44.126 14.198 1.00 70.09 ? 387 PRO A CA 1 ATOM 2971 C C . PRO A 1 387 ? -18.084 44.528 13.123 1.00 68.79 ? 387 PRO A C 1 ATOM 2972 O O . PRO A 1 387 ? -18.921 43.717 12.729 1.00 90.36 ? 387 PRO A O 1 ATOM 2973 C CB . PRO A 1 387 ? -16.139 43.029 13.692 1.00 89.08 ? 387 PRO A CB 1 ATOM 2974 C CG . PRO A 1 387 ? -15.900 42.157 14.882 1.00 81.39 ? 387 PRO A CG 1 ATOM 2975 C CD . PRO A 1 387 ? -17.189 42.166 15.647 1.00 70.11 ? 387 PRO A CD 1 ATOM 2976 N N . SER A 1 388 ? -17.995 45.769 12.657 1.00 61.18 ? 388 SER A N 1 ATOM 2977 C CA . SER A 1 388 ? -18.850 46.234 11.573 1.00 63.73 ? 388 SER A CA 1 ATOM 2978 C C . SER A 1 388 ? -18.162 45.934 10.253 1.00 73.99 ? 388 SER A C 1 ATOM 2979 O O . SER A 1 388 ? -18.716 46.168 9.180 1.00 98.27 ? 388 SER A O 1 ATOM 2980 C CB . SER A 1 388 ? -19.148 47.729 11.703 1.00 63.71 ? 388 SER A CB 1 ATOM 2981 O OG . SER A 1 388 ? -17.977 48.503 11.513 1.00 68.63 ? 388 SER A OG 1 ATOM 2982 N N . GLN A 1 389 ? -16.958 45.378 10.357 1.00 70.29 ? 389 GLN A N 1 ATOM 2983 C CA . GLN A 1 389 ? -16.140 45.020 9.207 1.00 76.54 ? 389 GLN A CA 1 ATOM 2984 C C . GLN A 1 389 ? -14.877 44.321 9.694 1.00 74.85 ? 389 GLN A C 1 ATOM 2985 O O . GLN A 1 389 ? -14.479 44.469 10.850 1.00 62.99 ? 389 GLN A O 1 ATOM 2986 C CB . GLN A 1 389 ? -15.776 46.262 8.383 1.00 62.80 ? 389 GLN A CB 1 ATOM 2987 C CG . GLN A 1 389 ? -15.125 45.977 7.037 1.00 66.39 ? 389 GLN A CG 1 ATOM 2988 C CD . GLN A 1 389 ? -14.711 47.240 6.309 1.00 62.83 ? 389 GLN A CD 1 ATOM 2989 O OE1 . GLN A 1 389 ? -14.907 48.349 6.805 1.00 61.75 ? 389 GLN A OE1 1 ATOM 2990 N NE2 . GLN A 1 389 ? -14.134 47.078 5.125 1.00 64.79 ? 389 GLN A NE2 1 ATOM 2991 N N . ILE A 1 390 ? -14.244 43.573 8.799 1.00 71.56 ? 390 ILE A N 1 ATOM 2992 C CA . ILE A 1 390 ? -13.062 42.796 9.133 1.00 63.36 ? 390 ILE A CA 1 ATOM 2993 C C . ILE A 1 390 ? -11.989 42.994 8.073 1.00 77.37 ? 390 ILE A C 1 ATOM 2994 O O . ILE A 1 390 ? -12.232 42.784 6.884 1.00 103.56 ? 390 ILE A O 1 ATOM 2995 C CB . ILE A 1 390 ? -13.389 41.291 9.261 1.00 62.55 ? 390 ILE A CB 1 ATOM 2996 C CG1 . ILE A 1 390 ? -14.052 40.991 10.609 1.00 72.98 ? 390 ILE A CG1 1 ATOM 2997 C CG2 . ILE A 1 390 ? -12.134 40.454 9.100 1.00 61.67 ? 390 ILE A CG2 1 ATOM 2998 C CD1 . ILE A 1 390 ? -15.561 41.110 10.597 1.00 92.01 ? 390 ILE A CD1 1 ATOM 2999 N N . LEU A 1 391 ? -10.804 43.410 8.505 1.00 66.87 ? 391 LEU A N 1 ATOM 3000 C CA . LEU A 1 391 ? -9.685 43.563 7.589 1.00 67.51 ? 391 LEU A CA 1 ATOM 3001 C C . LEU A 1 391 ? -8.739 42.380 7.727 1.00 67.54 ? 391 LEU A C 1 ATOM 3002 O O . LEU A 1 391 ? -8.054 42.233 8.739 1.00 66.07 ? 391 LEU A O 1 ATOM 3003 C CB . LEU A 1 391 ? -8.944 44.875 7.850 1.00 66.46 ? 391 LEU A CB 1 ATOM 3004 C CG . LEU A 1 391 ? -9.797 46.141 7.748 1.00 74.27 ? 391 LEU A CG 1 ATOM 3005 C CD1 . LEU A 1 391 ? -8.941 47.382 7.936 1.00 92.67 ? 391 LEU A CD1 1 ATOM 3006 C CD2 . LEU A 1 391 ? -10.534 46.186 6.418 1.00 73.39 ? 391 LEU A CD2 1 ATOM 3007 N N . GLU A 1 392 ? -8.709 41.535 6.704 1.00 71.16 ? 392 GLU A N 1 ATOM 3008 C CA . GLU A 1 392 ? -7.848 40.364 6.714 1.00 76.13 ? 392 GLU A CA 1 ATOM 3009 C C . GLU A 1 392 ? -6.675 40.579 5.772 1.00 79.05 ? 392 GLU A C 1 ATOM 3010 O O . GLU A 1 392 ? -6.837 40.571 4.553 1.00 85.75 ? 392 GLU A O 1 ATOM 3011 C CB . GLU A 1 392 ? -8.638 39.116 6.314 1.00 103.27 ? 392 GLU A CB 1 ATOM 3012 C CG . GLU A 1 392 ? -7.854 37.817 6.392 1.00 125.96 ? 392 GLU A CG 1 ATOM 3013 C CD . GLU A 1 392 ? -8.681 36.615 5.970 1.00 133.79 ? 392 GLU A CD 1 ATOM 3014 O OE1 . GLU A 1 392 ? -8.202 35.473 6.130 1.00 134.28 ? 392 GLU A OE1 1 ATOM 3015 O OE2 . GLU A 1 392 ? -9.812 36.815 5.478 1.00 129.93 ? 392 GLU A OE2 1 ATOM 3016 N N . GLY A 1 393 ? -5.493 40.774 6.344 1.00 80.33 ? 393 GLY A N 1 ATOM 3017 C CA . GLY A 1 393 ? -4.298 40.969 5.548 1.00 90.65 ? 393 GLY A CA 1 ATOM 3018 C C . GLY A 1 393 ? -3.879 39.674 4.888 1.00 90.00 ? 393 GLY A C 1 ATOM 3019 O O . GLY A 1 393 ? -3.799 38.637 5.547 1.00 97.71 ? 393 GLY A O 1 ATOM 3020 N N . GLN A 1 394 ? -3.617 39.723 3.587 1.00 94.29 ? 394 GLN A N 1 ATOM 3021 C CA . GLN A 1 394 ? -3.136 38.541 2.888 1.00 112.72 ? 394 GLN A CA 1 ATOM 3022 C C . GLN A 1 394 ? -1.688 38.719 2.460 1.00 100.90 ? 394 GLN A C 1 ATOM 3023 O O . GLN A 1 394 ? -1.395 39.442 1.509 1.00 98.19 ? 394 GLN A O 1 ATOM 3024 C CB . GLN A 1 394 ? -4.005 38.239 1.664 1.00 133.94 ? 394 GLN A CB 1 ATOM 3025 C CG . GLN A 1 394 ? -5.492 38.117 1.954 1.00 139.88 ? 394 GLN A CG 1 ATOM 3026 C CD . GLN A 1 394 ? -6.247 39.404 1.683 1.00 132.44 ? 394 GLN A CD 1 ATOM 3027 O OE1 . GLN A 1 394 ? -5.648 40.464 1.503 1.00 115.90 ? 394 GLN A OE1 1 ATOM 3028 N NE2 . GLN A 1 394 ? -7.572 39.315 1.646 1.00 133.67 ? 394 GLN A NE2 1 ATOM 3029 N N . TRP A 1 395 ? -0.792 38.035 3.163 1.00 92.33 ? 395 TRP A N 1 ATOM 3030 C CA . TRP A 1 395 ? 0.624 38.010 2.821 1.00 89.92 ? 395 TRP A CA 1 ATOM 3031 C C . TRP A 1 395 ? 1.234 36.711 3.328 1.00 90.73 ? 395 TRP A C 1 ATOM 3032 O O . TRP A 1 395 ? 0.809 36.179 4.354 1.00 88.19 ? 395 TRP A O 1 ATOM 3033 C CB . TRP A 1 395 ? 1.359 39.218 3.409 1.00 87.19 ? 395 TRP A CB 1 ATOM 3034 C CG . TRP A 1 395 ? 0.991 40.516 2.759 1.00 87.44 ? 395 TRP A CG 1 ATOM 3035 C CD1 . TRP A 1 395 ? 0.188 41.492 3.272 1.00 86.89 ? 395 TRP A CD1 1 ATOM 3036 C CD2 . TRP A 1 395 ? 1.394 40.970 1.460 1.00 94.22 ? 395 TRP A CD2 1 ATOM 3037 N NE1 . TRP A 1 395 ? 0.074 42.530 2.379 1.00 87.40 ? 395 TRP A NE1 1 ATOM 3038 C CE2 . TRP A 1 395 ? 0.804 42.233 1.258 1.00 89.10 ? 395 TRP A CE2 1 ATOM 3039 C CE3 . TRP A 1 395 ? 2.199 40.432 0.451 1.00 116.91 ? 395 TRP A CE3 1 ATOM 3040 C CZ2 . TRP A 1 395 ? 0.994 42.968 0.089 1.00 110.54 ? 395 TRP A CZ2 1 ATOM 3041 C CZ3 . TRP A 1 395 ? 2.387 41.163 -0.709 1.00 124.83 ? 395 TRP A CZ3 1 ATOM 3042 C CH2 . TRP A 1 395 ? 1.787 42.417 -0.880 1.00 123.64 ? 395 TRP A CH2 1 ATOM 3043 N N . ALA A 1 396 ? 2.233 36.203 2.616 1.00 101.25 ? 396 ALA A N 1 ATOM 3044 C CA . ALA A 1 396 ? 2.855 34.941 2.992 1.00 105.55 ? 396 ALA A CA 1 ATOM 3045 C C . ALA A 1 396 ? 3.736 35.113 4.223 1.00 84.97 ? 396 ALA A C 1 ATOM 3046 O O . ALA A 1 396 ? 3.879 36.215 4.748 1.00 82.93 ? 396 ALA A O 1 ATOM 3047 C CB . ALA A 1 396 ? 3.665 34.383 1.833 1.00 125.60 ? 396 ALA A CB 1 ATOM 3048 N N . ALA A 1 397 ? 4.324 34.013 4.679 1.00 85.66 ? 397 ALA A N 1 ATOM 3049 C CA . ALA A 1 397 ? 5.216 34.042 5.829 1.00 88.67 ? 397 ALA A CA 1 ATOM 3050 C C . ALA A 1 397 ? 6.595 33.532 5.436 1.00 114.82 ? 397 ALA A C 1 ATOM 3051 O O . ALA A 1 397 ? 6.747 32.383 5.018 1.00 137.42 ? 397 ALA A O 1 ATOM 3052 C CB . ALA A 1 397 ? 4.644 33.215 6.970 1.00 84.22 ? 397 ALA A CB 1 ATOM 3053 N N . ARG A 1 398 ? 7.599 34.392 5.567 1.00 106.69 ? 398 ARG A N 1 ATOM 3054 C CA . ARG A 1 398 ? 8.958 34.044 5.173 1.00 99.27 ? 398 ARG A CA 1 ATOM 3055 C C . ARG A 1 398 ? 9.776 33.551 6.360 1.00 91.48 ? 398 ARG A C 1 ATOM 3056 O O . ARG A 1 398 ? 10.160 32.383 6.419 1.00 106.59 ? 398 ARG A O 1 ATOM 3057 C CB . ARG A 1 398 ? 9.640 35.246 4.518 1.00 100.82 ? 398 ARG A CB 1 ATOM 3058 C CG . ARG A 1 398 ? 9.017 35.642 3.190 1.00 112.37 ? 398 ARG A CG 1 ATOM 3059 C CD . ARG A 1 398 ? 9.540 36.976 2.687 1.00 121.77 ? 398 ARG A CD 1 ATOM 3060 N NE . ARG A 1 398 ? 9.027 37.283 1.355 1.00 136.79 ? 398 ARG A NE 1 ATOM 3061 C CZ . ARG A 1 398 ? 7.836 37.823 1.116 1.00 124.90 ? 398 ARG A CZ 1 ATOM 3062 N NH1 . ARG A 1 398 ? 7.026 38.121 2.123 1.00 112.71 ? 398 ARG A NH1 1 ATOM 3063 N NH2 . ARG A 1 398 ? 7.454 38.064 -0.131 1.00 112.93 ? 398 ARG A NH2 1 ATOM 3064 N N . SER A 1 399 ? 10.036 34.446 7.306 1.00 84.34 ? 399 SER A N 1 ATOM 3065 C CA . SER A 1 399 ? 10.823 34.112 8.487 1.00 96.70 ? 399 SER A CA 1 ATOM 3066 C C . SER A 1 399 ? 9.946 34.046 9.730 1.00 97.60 ? 399 SER A C 1 ATOM 3067 O O . SER A 1 399 ? 9.809 32.995 10.355 1.00 88.39 ? 399 SER A O 1 ATOM 3068 C CB . SER A 1 399 ? 11.945 35.130 8.691 1.00 104.58 ? 399 SER A CB 1 ATOM 3069 O OG . SER A 1 399 ? 12.668 34.859 9.880 1.00 112.05 ? 399 SER A OG 1 ATOM 3070 N N . MET A 1 400 ? 9.348 35.180 10.077 1.00 97.81 ? 400 MET A N 1 ATOM 3071 C CA . MET A 1 400 ? 8.551 35.296 11.288 1.00 82.19 ? 400 MET A CA 1 ATOM 3072 C C . MET A 1 400 ? 7.106 35.606 10.896 1.00 73.94 ? 400 MET A C 1 ATOM 3073 O O . MET A 1 400 ? 6.822 35.764 9.708 1.00 77.84 ? 400 MET A O 1 ATOM 3074 C CB . MET A 1 400 ? 9.139 36.385 12.192 1.00 71.52 ? 400 MET A CB 1 ATOM 3075 C CG . MET A 1 400 ? 9.031 37.788 11.626 1.00 64.47 ? 400 MET A CG 1 ATOM 3076 S SD . MET A 1 400 ? 9.992 38.968 12.588 1.00 134.13 ? 400 MET A SD 1 ATOM 3077 C CE . MET A 1 400 ? 11.616 38.221 12.483 1.00 113.97 ? 400 MET A CE 1 ATOM 3078 N N . PRO A 1 401 ? 6.183 35.681 11.877 1.00 65.40 ? 401 PRO A N 1 ATOM 3079 C CA . PRO A 1 401 ? 4.804 35.986 11.479 1.00 65.25 ? 401 PRO A CA 1 ATOM 3080 C C . PRO A 1 401 ? 4.663 37.310 10.742 1.00 73.56 ? 401 PRO A C 1 ATOM 3081 O O . PRO A 1 401 ? 5.173 38.330 11.205 1.00 86.63 ? 401 PRO A O 1 ATOM 3082 C CB . PRO A 1 401 ? 4.061 36.038 12.815 1.00 62.58 ? 401 PRO A CB 1 ATOM 3083 C CG . PRO A 1 401 ? 4.813 35.116 13.685 1.00 70.85 ? 401 PRO A CG 1 ATOM 3084 C CD . PRO A 1 401 ? 6.255 35.245 13.286 1.00 73.25 ? 401 PRO A CD 1 ATOM 3085 N N . PRO A 1 402 ? 3.975 37.290 9.593 1.00 75.77 ? 402 PRO A N 1 ATOM 3086 C CA . PRO A 1 402 ? 3.653 38.528 8.883 1.00 79.97 ? 402 PRO A CA 1 ATOM 3087 C C . PRO A 1 402 ? 2.585 39.275 9.657 1.00 84.08 ? 402 PRO A C 1 ATOM 3088 O O . PRO A 1 402 ? 1.413 39.225 9.284 1.00 109.33 ? 402 PRO A O 1 ATOM 3089 C CB . PRO A 1 402 ? 3.129 38.036 7.533 1.00 78.63 ? 402 PRO A CB 1 ATOM 3090 C CG . PRO A 1 402 ? 2.574 36.683 7.825 1.00 79.56 ? 402 PRO A CG 1 ATOM 3091 C CD . PRO A 1 402 ? 3.449 36.100 8.902 1.00 77.39 ? 402 PRO A CD 1 ATOM 3092 N N . SER A 1 403 ? 2.985 39.956 10.726 1.00 66.12 ? 403 SER A N 1 ATOM 3093 C CA . SER A 1 403 ? 2.006 40.486 11.658 1.00 63.44 ? 403 SER A CA 1 ATOM 3094 C C . SER A 1 403 ? 1.217 41.592 10.989 1.00 63.04 ? 403 SER A C 1 ATOM 3095 O O . SER A 1 403 ? 1.770 42.617 10.610 1.00 75.81 ? 403 SER A O 1 ATOM 3096 C CB . SER A 1 403 ? 2.692 41.015 12.920 1.00 78.60 ? 403 SER A CB 1 ATOM 3097 O OG . SER A 1 403 ? 3.578 40.055 13.470 1.00 52.58 ? 403 SER A OG 1 ATOM 3098 N N . PHE A 1 404 ? -0.090 41.389 10.883 1.00 63.06 ? 404 PHE A N 1 ATOM 3099 C CA . PHE A 1 404 ? -0.961 42.366 10.252 1.00 59.64 ? 404 PHE A CA 1 ATOM 3100 C C . PHE A 1 404 ? -1.738 43.064 11.346 1.00 61.50 ? 404 PHE A C 1 ATOM 3101 O O . PHE A 1 404 ? -2.551 42.452 12.033 1.00 91.33 ? 404 PHE A O 1 ATOM 3102 C CB . PHE A 1 404 ? -1.899 41.709 9.244 1.00 60.75 ? 404 PHE A CB 1 ATOM 3103 C CG . PHE A 1 404 ? -2.744 42.686 8.485 1.00 60.99 ? 404 PHE A CG 1 ATOM 3104 C CD1 . PHE A 1 404 ? -2.215 43.393 7.418 1.00 63.05 ? 404 PHE A CD1 1 ATOM 3105 C CD2 . PHE A 1 404 ? -4.065 42.901 8.838 1.00 59.50 ? 404 PHE A CD2 1 ATOM 3106 C CE1 . PHE A 1 404 ? -2.989 44.295 6.718 1.00 64.51 ? 404 PHE A CE1 1 ATOM 3107 C CE2 . PHE A 1 404 ? -4.843 43.802 8.140 1.00 60.86 ? 404 PHE A CE2 1 ATOM 3108 C CZ . PHE A 1 404 ? -4.305 44.499 7.079 1.00 63.61 ? 404 PHE A CZ 1 ATOM 3109 N N . GLY A 1 405 ? -1.496 44.356 11.491 1.00 57.47 ? 405 GLY A N 1 ATOM 3110 C CA . GLY A 1 405 ? -1.811 45.030 12.729 1.00 65.19 ? 405 GLY A CA 1 ATOM 3111 C C . GLY A 1 405 ? -0.500 45.092 13.481 1.00 74.93 ? 405 GLY A C 1 ATOM 3112 O O . GLY A 1 405 ? 0.559 44.973 12.862 1.00 103.95 ? 405 GLY A O 1 ATOM 3113 N N . TYR A 1 406 ? -0.578 45.307 14.795 1.00 53.92 ? 406 TYR A N 1 ATOM 3114 C CA . TYR A 1 406 ? 0.576 45.525 15.677 1.00 49.21 ? 406 TYR A CA 1 ATOM 3115 C C . TYR A 1 406 ? 1.123 46.934 15.442 1.00 57.53 ? 406 TYR A C 1 ATOM 3116 O O . TYR A 1 406 ? 1.848 47.480 16.271 1.00 73.69 ? 406 TYR A O 1 ATOM 3117 C CB . TYR A 1 406 ? 1.666 44.462 15.457 1.00 49.23 ? 406 TYR A CB 1 ATOM 3118 C CG . TYR A 1 406 ? 2.712 44.369 16.546 1.00 48.08 ? 406 TYR A CG 1 ATOM 3119 C CD1 . TYR A 1 406 ? 2.550 43.500 17.615 1.00 47.68 ? 406 TYR A CD1 1 ATOM 3120 C CD2 . TYR A 1 406 ? 3.870 45.135 16.495 1.00 47.54 ? 406 TYR A CD2 1 ATOM 3121 C CE1 . TYR A 1 406 ? 3.504 43.404 18.610 1.00 62.57 ? 406 TYR A CE1 1 ATOM 3122 C CE2 . TYR A 1 406 ? 4.830 45.046 17.486 1.00 54.20 ? 406 TYR A CE2 1 ATOM 3123 C CZ . TYR A 1 406 ? 4.642 44.179 18.542 1.00 64.79 ? 406 TYR A CZ 1 ATOM 3124 O OH . TYR A 1 406 ? 5.594 44.085 19.532 1.00 73.07 ? 406 TYR A OH 1 ATOM 3125 N N . SER A 1 407 ? 0.753 47.515 14.304 1.00 50.14 ? 407 SER A N 1 ATOM 3126 C CA . SER A 1 407 ? 0.954 48.930 14.027 1.00 50.49 ? 407 SER A CA 1 ATOM 3127 C C . SER A 1 407 ? -0.231 49.469 13.227 1.00 68.32 ? 407 SER A C 1 ATOM 3128 O O . SER A 1 407 ? -0.544 48.946 12.156 1.00 52.63 ? 407 SER A O 1 ATOM 3129 C CB . SER A 1 407 ? 2.262 49.148 13.268 1.00 81.33 ? 407 SER A CB 1 ATOM 3130 O OG . SER A 1 407 ? 2.352 48.273 12.157 1.00 82.64 ? 407 SER A OG 1 ATOM 3131 N N . MET A 1 408 ? -0.873 50.519 13.733 1.00 72.40 ? 408 MET A N 1 ATOM 3132 C CA . MET A 1 408 ? -2.004 51.143 13.046 1.00 52.89 ? 408 MET A CA 1 ATOM 3133 C C . MET A 1 408 ? -2.098 52.632 13.369 1.00 57.38 ? 408 MET A C 1 ATOM 3134 O O . MET A 1 408 ? -1.806 53.046 14.490 1.00 67.43 ? 408 MET A O 1 ATOM 3135 C CB . MET A 1 408 ? -3.325 50.463 13.425 1.00 52.73 ? 408 MET A CB 1 ATOM 3136 C CG . MET A 1 408 ? -3.541 49.065 12.869 1.00 63.72 ? 408 MET A CG 1 ATOM 3137 S SD . MET A 1 408 ? -5.145 48.389 13.336 1.00 62.54 ? 408 MET A SD 1 ATOM 3138 C CE . MET A 1 408 ? -5.104 48.616 15.112 1.00 57.50 ? 408 MET A CE 1 ATOM 3139 N N . LYS A 1 409 ? -2.496 53.434 12.384 1.00 61.00 ? 409 LYS A N 1 ATOM 3140 C CA . LYS A 1 409 ? -2.839 54.833 12.634 1.00 62.86 ? 409 LYS A CA 1 ATOM 3141 C C . LYS A 1 409 ? -4.068 55.255 11.831 1.00 57.13 ? 409 LYS A C 1 ATOM 3142 O O . LYS A 1 409 ? -4.091 55.131 10.607 1.00 58.17 ? 409 LYS A O 1 ATOM 3143 C CB . LYS A 1 409 ? -1.660 55.752 12.308 1.00 58.83 ? 409 LYS A CB 1 ATOM 3144 C CG . LYS A 1 409 ? -1.883 57.200 12.726 1.00 68.96 ? 409 LYS A CG 1 ATOM 3145 C CD . LYS A 1 409 ? -2.200 57.297 14.212 1.00 96.56 ? 409 LYS A CD 1 ATOM 3146 C CE . LYS A 1 409 ? -2.537 58.722 14.625 1.00 116.99 ? 409 LYS A CE 1 ATOM 3147 N NZ . LYS A 1 409 ? -1.382 59.649 14.470 1.00 116.11 ? 409 LYS A NZ 1 ATOM 3148 N N . GLY A 1 410 ? -5.092 55.739 12.527 1.00 59.83 ? 410 GLY A N 1 ATOM 3149 C CA . GLY A 1 410 ? -6.298 56.227 11.880 1.00 74.26 ? 410 GLY A CA 1 ATOM 3150 C C . GLY A 1 410 ? -6.485 57.732 11.967 1.00 77.82 ? 410 GLY A C 1 ATOM 3151 O O . GLY A 1 410 ? -5.521 58.483 12.115 1.00 86.59 ? 410 GLY A O 1 ATOM 3152 N N . ALA A 1 411 ? -7.742 58.158 11.850 1.00 68.78 ? 411 ALA A N 1 ATOM 3153 C CA . ALA A 1 411 ? -8.167 59.531 12.136 1.00 68.08 ? 411 ALA A CA 1 ATOM 3154 C C . ALA A 1 411 ? -7.537 60.601 11.243 1.00 75.55 ? 411 ALA A C 1 ATOM 3155 O O . ALA A 1 411 ? -7.283 61.717 11.695 1.00 92.79 ? 411 ALA A O 1 ATOM 3156 C CB . ALA A 1 411 ? -7.896 59.861 13.601 1.00 75.74 ? 411 ALA A CB 1 ATOM 3157 N N . THR A 1 412 ? -7.289 60.266 9.981 1.00 65.15 ? 412 THR A N 1 ATOM 3158 C CA . THR A 1 412 ? -6.814 61.254 9.016 1.00 70.67 ? 412 THR A CA 1 ATOM 3159 C C . THR A 1 412 ? -7.377 60.948 7.631 1.00 77.91 ? 412 THR A C 1 ATOM 3160 O O . THR A 1 412 ? -7.437 59.788 7.226 1.00 94.02 ? 412 THR A O 1 ATOM 3161 C CB . THR A 1 412 ? -5.274 61.293 8.954 1.00 67.10 ? 412 THR A CB 1 ATOM 3162 O OG1 . THR A 1 412 ? -4.743 61.472 10.273 1.00 93.72 ? 412 THR A OG1 1 ATOM 3163 C CG2 . THR A 1 412 ? -4.799 62.432 8.065 1.00 69.69 ? 412 THR A CG2 1 ATOM 3164 N N . ASP A 1 413 ? -7.786 61.984 6.904 1.00 75.94 ? 413 ASP A N 1 ATOM 3165 C CA . ASP A 1 413 ? -8.328 61.785 5.567 1.00 72.28 ? 413 ASP A CA 1 ATOM 3166 C C . ASP A 1 413 ? -7.267 62.128 4.529 1.00 74.02 ? 413 ASP A C 1 ATOM 3167 O O . ASP A 1 413 ? -6.980 63.298 4.279 1.00 123.40 ? 413 ASP A O 1 ATOM 3168 C CB . ASP A 1 413 ? -9.582 62.643 5.373 1.00 85.30 ? 413 ASP A CB 1 ATOM 3169 C CG . ASP A 1 413 ? -10.248 62.419 4.031 1.00 97.06 ? 413 ASP A CG 1 ATOM 3170 O OD1 . ASP A 1 413 ? -9.972 61.385 3.386 1.00 121.24 ? 413 ASP A OD1 1 ATOM 3171 O OD2 . ASP A 1 413 ? -11.062 63.276 3.628 1.00 78.12 ? 413 ASP A OD2 1 ATOM 3172 N N . ILE A 1 414 ? -6.696 61.092 3.923 1.00 73.29 ? 414 ILE A N 1 ATOM 3173 C CA . ILE A 1 414 ? -5.584 61.257 2.994 1.00 74.86 ? 414 ILE A CA 1 ATOM 3174 C C . ILE A 1 414 ? -6.040 61.585 1.570 1.00 77.60 ? 414 ILE A C 1 ATOM 3175 O O . ILE A 1 414 ? -5.363 62.318 0.850 1.00 79.93 ? 414 ILE A O 1 ATOM 3176 C CB . ILE A 1 414 ? -4.678 59.996 2.988 1.00 85.24 ? 414 ILE A CB 1 ATOM 3177 C CG1 . ILE A 1 414 ? -3.365 60.275 2.254 1.00 74.70 ? 414 ILE A CG1 1 ATOM 3178 C CG2 . ILE A 1 414 ? -5.404 58.786 2.409 1.00 84.39 ? 414 ILE A CG2 1 ATOM 3179 C CD1 . ILE A 1 414 ? -2.317 59.211 2.472 1.00 73.01 ? 414 ILE A CD1 1 ATOM 3180 N N . ASP A 1 415 ? -7.189 61.049 1.168 1.00 92.15 ? 415 ASP A N 1 ATOM 3181 C CA . ASP A 1 415 ? -7.685 61.252 -0.188 1.00 79.99 ? 415 ASP A CA 1 ATOM 3182 C C . ASP A 1 415 ? -8.637 62.438 -0.261 1.00 81.84 ? 415 ASP A C 1 ATOM 3183 O O . ASP A 1 415 ? -9.189 62.734 -1.322 1.00 112.46 ? 415 ASP A O 1 ATOM 3184 C CB . ASP A 1 415 ? -8.377 59.988 -0.710 1.00 79.10 ? 415 ASP A CB 1 ATOM 3185 C CG . ASP A 1 415 ? -9.341 59.383 0.297 1.00 81.69 ? 415 ASP A CG 1 ATOM 3186 O OD1 . ASP A 1 415 ? -9.842 58.269 0.034 1.00 75.62 ? 415 ASP A OD1 1 ATOM 3187 O OD2 . ASP A 1 415 ? -9.594 60.006 1.351 1.00 97.08 ? 415 ASP A OD2 1 ATOM 3188 N N . LYS A 1 416 ? -8.819 63.106 0.874 1.00 81.03 ? 416 LYS A N 1 ATOM 3189 C CA . LYS A 1 416 ? -9.714 64.254 0.983 1.00 84.22 ? 416 LYS A CA 1 ATOM 3190 C C . LYS A 1 416 ? -11.121 63.913 0.500 1.00 83.77 ? 416 LYS A C 1 ATOM 3191 O O . LYS A 1 416 ? -11.807 64.749 -0.088 1.00 87.02 ? 416 LYS A O 1 ATOM 3192 C CB . LYS A 1 416 ? -9.155 65.448 0.204 1.00 87.93 ? 416 LYS A CB 1 ATOM 3193 C CG . LYS A 1 416 ? -7.808 65.931 0.717 1.00 88.94 ? 416 LYS A CG 1 ATOM 3194 C CD . LYS A 1 416 ? -7.321 67.151 -0.045 1.00 105.53 ? 416 LYS A CD 1 ATOM 3195 C CE . LYS A 1 416 ? -5.986 67.637 0.499 1.00 111.73 ? 416 LYS A CE 1 ATOM 3196 N NZ . LYS A 1 416 ? -5.494 68.845 -0.219 1.00 109.69 ? 416 LYS A NZ 1 ATOM 3197 N N . ASN A 1 417 ? -11.544 62.679 0.758 1.00 92.39 ? 417 ASN A N 1 ATOM 3198 C CA . ASN A 1 417 ? -12.873 62.233 0.364 1.00 92.68 ? 417 ASN A CA 1 ATOM 3199 C C . ASN A 1 417 ? -13.918 62.583 1.415 1.00 87.94 ? 417 ASN A C 1 ATOM 3200 O O . ASN A 1 417 ? -15.096 62.260 1.267 1.00 96.62 ? 417 ASN A O 1 ATOM 3201 C CB . ASN A 1 417 ? -12.885 60.723 0.089 1.00 84.82 ? 417 ASN A CB 1 ATOM 3202 C CG . ASN A 1 417 ? -12.413 59.899 1.276 1.00 89.40 ? 417 ASN A CG 1 ATOM 3203 O OD1 . ASN A 1 417 ? -12.080 60.432 2.335 1.00 109.56 ? 417 ASN A OD1 1 ATOM 3204 N ND2 . ASN A 1 417 ? -12.384 58.583 1.099 1.00 82.19 ? 417 ASN A ND2 1 ATOM 3205 N N . GLY A 1 418 ? -13.475 63.246 2.478 1.00 79.10 ? 418 GLY A N 1 ATOM 3206 C CA . GLY A 1 418 ? -14.362 63.639 3.555 1.00 84.19 ? 418 GLY A CA 1 ATOM 3207 C C . GLY A 1 418 ? -14.506 62.540 4.586 1.00 84.24 ? 418 GLY A C 1 ATOM 3208 O O . GLY A 1 418 ? -15.254 62.674 5.554 1.00 79.68 ? 418 GLY A O 1 ATOM 3209 N N . TYR A 1 419 ? -13.787 61.443 4.374 1.00 73.98 ? 419 TYR A N 1 ATOM 3210 C CA . TYR A 1 419 ? -13.820 60.328 5.307 1.00 71.36 ? 419 TYR A CA 1 ATOM 3211 C C . TYR A 1 419 ? -12.415 59.922 5.737 1.00 70.10 ? 419 TYR A C 1 ATOM 3212 O O . TYR A 1 419 ? -11.494 59.877 4.916 1.00 70.82 ? 419 TYR A O 1 ATOM 3213 C CB . TYR A 1 419 ? -14.545 59.136 4.682 1.00 85.92 ? 419 TYR A CB 1 ATOM 3214 C CG . TYR A 1 419 ? -16.032 59.345 4.514 1.00 94.59 ? 419 TYR A CG 1 ATOM 3215 C CD1 . TYR A 1 419 ? -16.532 60.113 3.471 1.00 96.29 ? 419 TYR A CD1 1 ATOM 3216 C CD2 . TYR A 1 419 ? -16.936 58.771 5.397 1.00 91.85 ? 419 TYR A CD2 1 ATOM 3217 C CE1 . TYR A 1 419 ? -17.887 60.308 3.317 1.00 84.99 ? 419 TYR A CE1 1 ATOM 3218 C CE2 . TYR A 1 419 ? -18.295 58.957 5.248 1.00 77.91 ? 419 TYR A CE2 1 ATOM 3219 C CZ . TYR A 1 419 ? -18.764 59.729 4.208 1.00 77.80 ? 419 TYR A CZ 1 ATOM 3220 O OH . TYR A 1 419 ? -20.118 59.918 4.055 1.00 82.53 ? 419 TYR A OH 1 ATOM 3221 N N . PRO A 1 420 ? -12.255 59.606 7.031 1.00 74.55 ? 420 PRO A N 1 ATOM 3222 C CA . PRO A 1 420 ? -10.976 59.172 7.598 1.00 66.92 ? 420 PRO A CA 1 ATOM 3223 C C . PRO A 1 420 ? -10.537 57.839 7.017 1.00 65.84 ? 420 PRO A C 1 ATOM 3224 O O . PRO A 1 420 ? -11.369 56.961 6.803 1.00 65.29 ? 420 PRO A O 1 ATOM 3225 C CB . PRO A 1 420 ? -11.276 59.042 9.096 1.00 65.46 ? 420 PRO A CB 1 ATOM 3226 C CG . PRO A 1 420 ? -12.490 59.876 9.320 1.00 75.41 ? 420 PRO A CG 1 ATOM 3227 C CD . PRO A 1 420 ? -13.293 59.742 8.066 1.00 78.00 ? 420 PRO A CD 1 ATOM 3228 N N . ASP A 1 421 ? -9.242 57.689 6.770 1.00 65.70 ? 421 ASP A N 1 ATOM 3229 C CA . ASP A 1 421 ? -8.722 56.457 6.198 1.00 65.00 ? 421 ASP A CA 1 ATOM 3230 C C . ASP A 1 421 ? -7.822 55.761 7.217 1.00 63.38 ? 421 ASP A C 1 ATOM 3231 O O . ASP A 1 421 ? -7.615 56.277 8.315 1.00 69.61 ? 421 ASP A O 1 ATOM 3232 C CB . ASP A 1 421 ? -7.982 56.760 4.896 1.00 73.52 ? 421 ASP A CB 1 ATOM 3233 C CG . ASP A 1 421 ? -8.762 57.709 3.995 1.00 90.69 ? 421 ASP A CG 1 ATOM 3234 O OD1 . ASP A 1 421 ? -9.709 57.255 3.319 1.00 86.02 ? 421 ASP A OD1 1 ATOM 3235 O OD2 . ASP A 1 421 ? -8.439 58.915 3.970 1.00 105.89 ? 421 ASP A OD2 1 ATOM 3236 N N . LEU A 1 422 ? -7.291 54.594 6.867 1.00 62.38 ? 422 LEU A N 1 ATOM 3237 C CA . LEU A 1 422 ? -6.582 53.780 7.851 1.00 60.54 ? 422 LEU A CA 1 ATOM 3238 C C . LEU A 1 422 ? -5.306 53.130 7.322 1.00 60.52 ? 422 LEU A C 1 ATOM 3239 O O . LEU A 1 422 ? -5.290 52.559 6.231 1.00 61.70 ? 422 LEU A O 1 ATOM 3240 C CB . LEU A 1 422 ? -7.514 52.695 8.395 1.00 59.43 ? 422 LEU A CB 1 ATOM 3241 C CG . LEU A 1 422 ? -6.917 51.762 9.450 1.00 57.74 ? 422 LEU A CG 1 ATOM 3242 C CD1 . LEU A 1 422 ? -6.461 52.556 10.664 1.00 56.92 ? 422 LEU A CD1 1 ATOM 3243 C CD2 . LEU A 1 422 ? -7.916 50.689 9.850 1.00 57.12 ? 422 LEU A CD2 1 ATOM 3244 N N . ILE A 1 423 ? -4.242 53.215 8.115 1.00 61.25 ? 423 ILE A N 1 ATOM 3245 C CA . ILE A 1 423 ? -2.975 52.572 7.788 1.00 67.37 ? 423 ILE A CA 1 ATOM 3246 C C . ILE A 1 423 ? -2.710 51.382 8.703 1.00 78.82 ? 423 ILE A C 1 ATOM 3247 O O . ILE A 1 423 ? -2.730 51.514 9.926 1.00 93.44 ? 423 ILE A O 1 ATOM 3248 C CB . ILE A 1 423 ? -1.792 53.551 7.903 1.00 62.10 ? 423 ILE A CB 1 ATOM 3249 C CG1 . ILE A 1 423 ? -2.043 54.800 7.060 1.00 63.84 ? 423 ILE A CG1 1 ATOM 3250 C CG2 . ILE A 1 423 ? -0.497 52.871 7.485 1.00 59.58 ? 423 ILE A CG2 1 ATOM 3251 C CD1 . ILE A 1 423 ? -0.926 55.817 7.136 1.00 79.37 ? 423 ILE A CD1 1 ATOM 3252 N N . VAL A 1 424 ? -2.467 50.219 8.107 1.00 71.77 ? 424 VAL A N 1 ATOM 3253 C CA . VAL A 1 424 ? -2.109 49.028 8.868 1.00 57.21 ? 424 VAL A CA 1 ATOM 3254 C C . VAL A 1 424 ? -0.741 48.516 8.435 1.00 65.72 ? 424 VAL A C 1 ATOM 3255 O O . VAL A 1 424 ? -0.573 48.060 7.304 1.00 98.15 ? 424 VAL A O 1 ATOM 3256 C CB . VAL A 1 424 ? -3.147 47.905 8.692 1.00 57.44 ? 424 VAL A CB 1 ATOM 3257 C CG1 . VAL A 1 424 ? -2.739 46.680 9.493 1.00 55.65 ? 424 VAL A CG1 1 ATOM 3258 C CG2 . VAL A 1 424 ? -4.528 48.386 9.108 1.00 56.50 ? 424 VAL A CG2 1 ATOM 3259 N N . GLY A 1 425 ? 0.239 48.604 9.327 1.00 55.52 ? 425 GLY A N 1 ATOM 3260 C CA . GLY A 1 425 ? 1.578 48.142 9.012 1.00 58.95 ? 425 GLY A CA 1 ATOM 3261 C C . GLY A 1 425 ? 1.792 46.667 9.284 1.00 58.91 ? 425 GLY A C 1 ATOM 3262 O O . GLY A 1 425 ? 1.252 46.117 10.245 1.00 54.18 ? 425 GLY A O 1 ATOM 3263 N N . ALA A 1 426 ? 2.592 46.026 8.437 1.00 65.79 ? 426 ALA A N 1 ATOM 3264 C CA . ALA A 1 426 ? 3.003 44.647 8.664 1.00 59.92 ? 426 ALA A CA 1 ATOM 3265 C C . ALA A 1 426 ? 4.515 44.520 8.537 1.00 62.94 ? 426 ALA A C 1 ATOM 3266 O O . ALA A 1 426 ? 5.061 44.625 7.441 1.00 88.64 ? 426 ALA A O 1 ATOM 3267 C CB . ALA A 1 426 ? 2.306 43.715 7.686 1.00 59.86 ? 426 ALA A CB 1 ATOM 3268 N N . PHE A 1 427 ? 5.187 44.263 9.654 1.00 58.31 ? 427 PHE A N 1 ATOM 3269 C CA . PHE A 1 427 ? 6.645 44.229 9.657 1.00 58.96 ? 427 PHE A CA 1 ATOM 3270 C C . PHE A 1 427 ? 7.178 42.823 9.413 1.00 64.69 ? 427 PHE A C 1 ATOM 3271 O O . PHE A 1 427 ? 8.380 42.630 9.234 1.00 65.19 ? 427 PHE A O 1 ATOM 3272 C CB . PHE A 1 427 ? 7.194 44.790 10.973 1.00 55.50 ? 427 PHE A CB 1 ATOM 3273 C CG . PHE A 1 427 ? 6.805 43.998 12.187 1.00 57.82 ? 427 PHE A CG 1 ATOM 3274 C CD1 . PHE A 1 427 ? 7.688 43.091 12.750 1.00 54.51 ? 427 PHE A CD1 1 ATOM 3275 C CD2 . PHE A 1 427 ? 5.564 44.169 12.776 1.00 71.82 ? 427 PHE A CD2 1 ATOM 3276 C CE1 . PHE A 1 427 ? 7.335 42.366 13.869 1.00 52.88 ? 427 PHE A CE1 1 ATOM 3277 C CE2 . PHE A 1 427 ? 5.207 43.444 13.895 1.00 74.32 ? 427 PHE A CE2 1 ATOM 3278 C CZ . PHE A 1 427 ? 6.094 42.542 14.443 1.00 65.46 ? 427 PHE A CZ 1 ATOM 3279 N N . GLY A 1 428 ? 6.279 41.845 9.404 1.00 76.96 ? 428 GLY A N 1 ATOM 3280 C CA . GLY A 1 428 ? 6.656 40.482 9.083 1.00 80.63 ? 428 GLY A CA 1 ATOM 3281 C C . GLY A 1 428 ? 7.059 40.379 7.626 1.00 87.46 ? 428 GLY A C 1 ATOM 3282 O O . GLY A 1 428 ? 8.097 39.809 7.295 1.00 97.81 ? 428 GLY A O 1 ATOM 3283 N N . VAL A 1 429 ? 6.227 40.938 6.754 1.00 81.68 ? 429 VAL A N 1 ATOM 3284 C CA . VAL A 1 429 ? 6.521 40.979 5.326 1.00 91.64 ? 429 VAL A CA 1 ATOM 3285 C C . VAL A 1 429 ? 7.182 42.297 4.936 1.00 104.30 ? 429 VAL A C 1 ATOM 3286 O O . VAL A 1 429 ? 7.445 42.541 3.757 1.00 102.35 ? 429 VAL A O 1 ATOM 3287 C CB . VAL A 1 429 ? 5.249 40.786 4.483 1.00 86.94 ? 429 VAL A CB 1 ATOM 3288 C CG1 . VAL A 1 429 ? 4.782 39.345 4.561 1.00 94.03 ? 429 VAL A CG1 1 ATOM 3289 C CG2 . VAL A 1 429 ? 4.156 41.739 4.944 1.00 82.48 ? 429 VAL A CG2 1 ATOM 3290 N N . ASP A 1 430 ? 7.443 43.135 5.938 1.00 103.46 ? 430 ASP A N 1 ATOM 3291 C CA . ASP A 1 430 ? 8.020 44.463 5.735 1.00 82.62 ? 430 ASP A CA 1 ATOM 3292 C C . ASP A 1 430 ? 7.171 45.291 4.775 1.00 73.27 ? 430 ASP A C 1 ATOM 3293 O O . ASP A 1 430 ? 7.668 45.813 3.777 1.00 76.84 ? 430 ASP A O 1 ATOM 3294 C CB . ASP A 1 430 ? 9.460 44.359 5.224 1.00 73.04 ? 430 ASP A CB 1 ATOM 3295 C CG . ASP A 1 430 ? 10.373 43.649 6.204 1.00 96.94 ? 430 ASP A CG 1 ATOM 3296 O OD1 . ASP A 1 430 ? 11.529 44.090 6.372 1.00 108.87 ? 430 ASP A OD1 1 ATOM 3297 O OD2 . ASP A 1 430 ? 9.934 42.649 6.809 1.00 108.73 ? 430 ASP A OD2 1 ATOM 3298 N N . ARG A 1 431 ? 5.883 45.396 5.085 1.00 65.46 ? 431 ARG A N 1 ATOM 3299 C CA . ARG A 1 431 ? 4.943 46.122 4.240 1.00 66.46 ? 431 ARG A CA 1 ATOM 3300 C C . ARG A 1 431 ? 3.978 46.980 5.051 1.00 63.37 ? 431 ARG A C 1 ATOM 3301 O O . ARG A 1 431 ? 3.813 46.788 6.254 1.00 59.51 ? 431 ARG A O 1 ATOM 3302 C CB . ARG A 1 431 ? 4.154 45.144 3.368 1.00 72.08 ? 431 ARG A CB 1 ATOM 3303 C CG . ARG A 1 431 ? 4.951 44.565 2.216 1.00 83.50 ? 431 ARG A CG 1 ATOM 3304 C CD . ARG A 1 431 ? 4.181 43.468 1.509 1.00 84.31 ? 431 ARG A CD 1 ATOM 3305 N NE . ARG A 1 431 ? 4.743 43.173 0.195 1.00 88.51 ? 431 ARG A NE 1 ATOM 3306 C CZ . ARG A 1 431 ? 5.782 42.370 -0.011 1.00 100.05 ? 431 ARG A CZ 1 ATOM 3307 N NH1 . ARG A 1 431 ? 6.380 41.779 1.014 1.00 102.92 ? 431 ARG A NH1 1 ATOM 3308 N NH2 . ARG A 1 431 ? 6.224 42.161 -1.243 1.00 108.79 ? 431 ARG A NH2 1 ATOM 3309 N N . ALA A 1 432 ? 3.343 47.932 4.377 1.00 65.93 ? 432 ALA A N 1 ATOM 3310 C CA . ALA A 1 432 ? 2.340 48.783 5.004 1.00 67.94 ? 432 ALA A CA 1 ATOM 3311 C C . ALA A 1 432 ? 1.181 49.012 4.042 1.00 68.58 ? 432 ALA A C 1 ATOM 3312 O O . ALA A 1 432 ? 1.390 49.350 2.877 1.00 67.96 ? 432 ALA A O 1 ATOM 3313 C CB . ALA A 1 432 ? 2.953 50.106 5.430 1.00 79.03 ? 432 ALA A CB 1 ATOM 3314 N N . ILE A 1 433 ? -0.041 48.828 4.531 1.00 63.22 ? 433 ILE A N 1 ATOM 3315 C CA . ILE A 1 433 ? -1.219 48.951 3.681 1.00 63.73 ? 433 ILE A CA 1 ATOM 3316 C C . ILE A 1 433 ? -2.097 50.127 4.100 1.00 63.35 ? 433 ILE A C 1 ATOM 3317 O O . ILE A 1 433 ? -2.330 50.353 5.287 1.00 61.62 ? 433 ILE A O 1 ATOM 3318 C CB . ILE A 1 433 ? -2.057 47.658 3.697 1.00 75.04 ? 433 ILE A CB 1 ATOM 3319 C CG1 . ILE A 1 433 ? -1.159 46.441 3.467 1.00 76.62 ? 433 ILE A CG1 1 ATOM 3320 C CG2 . ILE A 1 433 ? -3.155 47.716 2.645 1.00 71.74 ? 433 ILE A CG2 1 ATOM 3321 C CD1 . ILE A 1 433 ? -1.912 45.132 3.396 1.00 101.06 ? 433 ILE A CD1 1 ATOM 3322 N N . LEU A 1 434 ? -2.576 50.875 3.111 1.00 65.19 ? 434 LEU A N 1 ATOM 3323 C CA . LEU A 1 434 ? -3.445 52.019 3.352 1.00 65.29 ? 434 LEU A CA 1 ATOM 3324 C C . LEU A 1 434 ? -4.844 51.744 2.811 1.00 80.90 ? 434 LEU A C 1 ATOM 3325 O O . LEU A 1 434 ? -5.040 51.628 1.601 1.00 97.36 ? 434 LEU A O 1 ATOM 3326 C CB . LEU A 1 434 ? -2.850 53.281 2.714 1.00 67.81 ? 434 LEU A CB 1 ATOM 3327 C CG . LEU A 1 434 ? -3.553 54.641 2.824 1.00 84.55 ? 434 LEU A CG 1 ATOM 3328 C CD1 . LEU A 1 434 ? -4.521 54.869 1.669 1.00 94.77 ? 434 LEU A CD1 1 ATOM 3329 C CD2 . LEU A 1 434 ? -4.262 54.805 4.161 1.00 84.83 ? 434 LEU A CD2 1 ATOM 3330 N N . TYR A 1 435 ? -5.813 51.636 3.714 1.00 70.10 ? 435 TYR A N 1 ATOM 3331 C CA . TYR A 1 435 ? -7.203 51.433 3.326 1.00 69.43 ? 435 TYR A CA 1 ATOM 3332 C C . TYR A 1 435 ? -7.946 52.763 3.304 1.00 69.88 ? 435 TYR A C 1 ATOM 3333 O O . TYR A 1 435 ? -7.766 53.595 4.192 1.00 83.09 ? 435 TYR A O 1 ATOM 3334 C CB . TYR A 1 435 ? -7.894 50.456 4.278 1.00 68.88 ? 435 TYR A CB 1 ATOM 3335 C CG . TYR A 1 435 ? -7.274 49.078 4.299 1.00 78.25 ? 435 TYR A CG 1 ATOM 3336 C CD1 . TYR A 1 435 ? -6.275 48.758 5.210 1.00 76.04 ? 435 TYR A CD1 1 ATOM 3337 C CD2 . TYR A 1 435 ? -7.685 48.097 3.406 1.00 78.84 ? 435 TYR A CD2 1 ATOM 3338 C CE1 . TYR A 1 435 ? -5.704 47.499 5.231 1.00 66.16 ? 435 TYR A CE1 1 ATOM 3339 C CE2 . TYR A 1 435 ? -7.120 46.835 3.421 1.00 72.99 ? 435 TYR A CE2 1 ATOM 3340 C CZ . TYR A 1 435 ? -6.131 46.542 4.335 1.00 68.85 ? 435 TYR A CZ 1 ATOM 3341 O OH . TYR A 1 435 ? -5.567 45.287 4.350 1.00 68.47 ? 435 TYR A OH 1 ATOM 3342 N N . ARG A 1 436 ? -8.778 52.960 2.286 1.00 71.00 ? 436 ARG A N 1 ATOM 3343 C CA . ARG A 1 436 ? -9.529 54.203 2.146 1.00 71.97 ? 436 ARG A CA 1 ATOM 3344 C C . ARG A 1 436 ? -11.013 53.998 2.426 1.00 74.41 ? 436 ARG A C 1 ATOM 3345 O O . ARG A 1 436 ? -11.607 53.012 1.992 1.00 92.83 ? 436 ARG A O 1 ATOM 3346 C CB . ARG A 1 436 ? -9.342 54.788 0.746 1.00 75.15 ? 436 ARG A CB 1 ATOM 3347 C CG . ARG A 1 436 ? -7.897 55.054 0.368 1.00 76.42 ? 436 ARG A CG 1 ATOM 3348 C CD . ARG A 1 436 ? -7.814 55.760 -0.971 1.00 78.06 ? 436 ARG A CD 1 ATOM 3349 N NE . ARG A 1 436 ? -8.536 55.032 -2.009 1.00 80.62 ? 436 ARG A NE 1 ATOM 3350 C CZ . ARG A 1 436 ? -8.860 55.544 -3.191 1.00 92.21 ? 436 ARG A CZ 1 ATOM 3351 N NH1 . ARG A 1 436 ? -8.531 56.793 -3.487 1.00 98.33 ? 436 ARG A NH1 1 ATOM 3352 N NH2 . ARG A 1 436 ? -9.520 54.808 -4.075 1.00 100.71 ? 436 ARG A NH2 1 ATOM 3353 N N . ALA A 1 437 ? -11.606 54.938 3.155 1.00 68.63 ? 437 ALA A N 1 ATOM 3354 C CA . ALA A 1 437 ? -13.025 54.875 3.482 1.00 69.19 ? 437 ALA A CA 1 ATOM 3355 C C . ALA A 1 437 ? -13.896 55.225 2.279 1.00 87.80 ? 437 ALA A C 1 ATOM 3356 O O . ALA A 1 437 ? -13.435 55.849 1.324 1.00 104.43 ? 437 ALA A O 1 ATOM 3357 C CB . ALA A 1 437 ? -13.340 55.794 4.641 1.00 66.83 ? 437 ALA A CB 1 ATOM 3358 N N . ARG A 1 438 ? -15.159 54.819 2.342 1.00 80.57 ? 438 ARG A N 1 ATOM 3359 C CA . ARG A 1 438 ? -16.104 55.041 1.254 1.00 74.37 ? 438 ARG A CA 1 ATOM 3360 C C . ARG A 1 438 ? -17.211 56.002 1.704 1.00 73.40 ? 438 ARG A C 1 ATOM 3361 O O . ARG A 1 438 ? -17.509 56.085 2.892 1.00 80.32 ? 438 ARG A O 1 ATOM 3362 C CB . ARG A 1 438 ? -16.674 53.698 0.785 1.00 74.57 ? 438 ARG A CB 1 ATOM 3363 C CG . ARG A 1 438 ? -15.605 52.771 0.212 1.00 76.94 ? 438 ARG A CG 1 ATOM 3364 C CD . ARG A 1 438 ? -15.980 51.301 0.343 1.00 92.45 ? 438 ARG A CD 1 ATOM 3365 N NE . ARG A 1 438 ? -17.087 50.927 -0.532 1.00 93.45 ? 438 ARG A NE 1 ATOM 3366 C CZ . ARG A 1 438 ? -17.570 49.694 -0.639 1.00 84.59 ? 438 ARG A CZ 1 ATOM 3367 N NH1 . ARG A 1 438 ? -17.043 48.709 0.076 1.00 83.02 ? 438 ARG A NH1 1 ATOM 3368 N NH2 . ARG A 1 438 ? -18.580 49.445 -1.461 1.00 83.34 ? 438 ARG A NH2 1 ATOM 3369 N N . PRO A 1 439 ? -17.804 56.746 0.753 1.00 74.93 ? 439 PRO A N 1 ATOM 3370 C CA . PRO A 1 439 ? -18.748 57.845 1.015 1.00 77.57 ? 439 PRO A CA 1 ATOM 3371 C C . PRO A 1 439 ? -20.005 57.529 1.844 1.00 76.42 ? 439 PRO A C 1 ATOM 3372 O O . PRO A 1 439 ? -20.617 58.478 2.332 1.00 96.13 ? 439 PRO A O 1 ATOM 3373 C CB . PRO A 1 439 ? -19.155 58.278 -0.395 1.00 103.83 ? 439 PRO A CB 1 ATOM 3374 C CG . PRO A 1 439 ? -17.951 58.005 -1.210 1.00 103.02 ? 439 PRO A CG 1 ATOM 3375 C CD . PRO A 1 439 ? -17.391 56.722 -0.662 1.00 87.62 ? 439 PRO A CD 1 ATOM 3376 N N . VAL A 1 440 ? -20.394 56.262 1.978 1.00 75.61 ? 440 VAL A N 1 ATOM 3377 C CA . VAL A 1 440 ? -21.551 55.887 2.806 1.00 76.55 ? 440 VAL A CA 1 ATOM 3378 C C . VAL A 1 440 ? -22.841 56.605 2.388 1.00 88.92 ? 440 VAL A C 1 ATOM 3379 O O . VAL A 1 440 ? -23.287 57.540 3.055 1.00 92.56 ? 440 VAL A O 1 ATOM 3380 C CB . VAL A 1 440 ? -21.303 56.158 4.313 1.00 105.01 ? 440 VAL A CB 1 ATOM 3381 C CG1 . VAL A 1 440 ? -22.401 55.519 5.159 1.00 89.44 ? 440 VAL A CG1 1 ATOM 3382 C CG2 . VAL A 1 440 ? -19.958 55.618 4.738 1.00 122.23 ? 440 VAL A CG2 1 ATOM 3383 N N . ILE A 1 441 ? -23.413 56.195 1.261 1.00 95.41 ? 441 ILE A N 1 ATOM 3384 C CA . ILE A 1 441 ? -24.686 56.751 0.810 1.00 91.99 ? 441 ILE A CA 1 ATOM 3385 C C . ILE A 1 441 ? -25.868 56.143 1.564 1.00 88.13 ? 441 ILE A C 1 ATOM 3386 O O . ILE A 1 441 ? -25.990 54.923 1.659 1.00 86.81 ? 441 ILE A O 1 ATOM 3387 C CB . ILE A 1 441 ? -24.894 56.525 -0.700 1.00 88.57 ? 441 ILE A CB 1 ATOM 3388 C CG1 . ILE A 1 441 ? -23.705 57.071 -1.491 1.00 103.13 ? 441 ILE A CG1 1 ATOM 3389 C CG2 . ILE A 1 441 ? -26.193 57.169 -1.164 1.00 86.18 ? 441 ILE A CG2 1 ATOM 3390 C CD1 . ILE A 1 441 ? -23.809 56.840 -2.980 1.00 111.01 ? 441 ILE A CD1 1 ATOM 3391 N N . THR A 1 442 ? -26.738 56.993 2.101 1.00 85.49 ? 442 THR A N 1 ATOM 3392 C CA . THR A 1 442 ? -27.947 56.520 2.770 1.00 83.61 ? 442 THR A CA 1 ATOM 3393 C C . THR A 1 442 ? -29.166 56.745 1.883 1.00 86.08 ? 442 THR A C 1 ATOM 3394 O O . THR A 1 442 ? -29.574 57.883 1.649 1.00 87.23 ? 442 THR A O 1 ATOM 3395 C CB . THR A 1 442 ? -28.166 57.221 4.124 1.00 88.70 ? 442 THR A CB 1 ATOM 3396 O OG1 . THR A 1 442 ? -28.402 58.618 3.911 1.00 108.39 ? 442 THR A OG1 1 ATOM 3397 C CG2 . THR A 1 442 ? -26.950 57.045 5.019 1.00 86.81 ? 442 THR A CG2 1 ATOM 3398 N N . VAL A 1 443 ? -29.748 55.654 1.394 1.00 89.74 ? 443 VAL A N 1 ATOM 3399 C CA . VAL A 1 443 ? -30.869 55.735 0.465 1.00 87.82 ? 443 VAL A CA 1 ATOM 3400 C C . VAL A 1 443 ? -32.210 55.502 1.159 1.00 87.04 ? 443 VAL A C 1 ATOM 3401 O O . VAL A 1 443 ? -32.408 54.495 1.839 1.00 95.41 ? 443 VAL A O 1 ATOM 3402 C CB . VAL A 1 443 ? -30.708 54.724 -0.694 1.00 96.50 ? 443 VAL A CB 1 ATOM 3403 C CG1 . VAL A 1 443 ? -30.267 53.366 -0.168 1.00 110.97 ? 443 VAL A CG1 1 ATOM 3404 C CG2 . VAL A 1 443 ? -31.998 54.608 -1.495 1.00 95.97 ? 443 VAL A CG2 1 ATOM 3405 N N . ASN A 1 444 ? -33.124 56.451 0.989 1.00 89.30 ? 444 ASN A N 1 ATOM 3406 C CA . ASN A 1 444 ? -34.466 56.331 1.541 1.00 96.05 ? 444 ASN A CA 1 ATOM 3407 C C . ASN A 1 444 ? -35.470 56.013 0.440 1.00 95.50 ? 444 ASN A C 1 ATOM 3408 O O . ASN A 1 444 ? -35.686 56.814 -0.467 1.00 91.54 ? 444 ASN A O 1 ATOM 3409 C CB . ASN A 1 444 ? -34.864 57.616 2.271 1.00 114.30 ? 444 ASN A CB 1 ATOM 3410 C CG . ASN A 1 444 ? -36.012 57.407 3.242 1.00 123.74 ? 444 ASN A CG 1 ATOM 3411 O OD1 . ASN A 1 444 ? -36.794 56.465 3.109 1.00 123.39 ? 444 ASN A OD1 1 ATOM 3412 N ND2 . ASN A 1 444 ? -36.119 58.291 4.227 1.00 126.50 ? 444 ASN A ND2 1 ATOM 3413 N N . ALA A 1 445 ? -36.084 54.839 0.522 1.00 107.45 ? 445 ALA A N 1 ATOM 3414 C CA . ALA A 1 445 ? -37.020 54.405 -0.506 1.00 106.15 ? 445 ALA A CA 1 ATOM 3415 C C . ALA A 1 445 ? -38.421 54.245 0.062 1.00 88.37 ? 445 ALA A C 1 ATOM 3416 O O . ALA A 1 445 ? -38.599 54.051 1.264 1.00 86.13 ? 445 ALA A O 1 ATOM 3417 C CB . ALA A 1 445 ? -36.551 53.101 -1.131 1.00 109.82 ? 445 ALA A CB 1 ATOM 3418 N N . GLY A 1 446 ? -39.416 54.325 -0.812 1.00 88.71 ? 446 GLY A N 1 ATOM 3419 C CA . GLY A 1 446 ? -40.791 54.139 -0.398 1.00 105.62 ? 446 GLY A CA 1 ATOM 3420 C C . GLY A 1 446 ? -41.643 53.600 -1.527 1.00 108.18 ? 446 GLY A C 1 ATOM 3421 O O . GLY A 1 446 ? -41.343 53.801 -2.704 1.00 90.88 ? 446 GLY A O 1 ATOM 3422 N N . LEU A 1 447 ? -42.719 52.917 -1.160 1.00 111.95 ? 447 LEU A N 1 ATOM 3423 C CA . LEU A 1 447 ? -43.592 52.280 -2.133 1.00 98.07 ? 447 LEU A CA 1 ATOM 3424 C C . LEU A 1 447 ? -45.049 52.497 -1.768 1.00 98.94 ? 447 LEU A C 1 ATOM 3425 O O . LEU A 1 447 ? -45.473 52.153 -0.668 1.00 94.79 ? 447 LEU A O 1 ATOM 3426 C CB . LEU A 1 447 ? -43.287 50.785 -2.223 1.00 85.79 ? 447 LEU A CB 1 ATOM 3427 C CG . LEU A 1 447 ? -44.194 49.947 -3.122 1.00 86.99 ? 447 LEU A CG 1 ATOM 3428 C CD1 . LEU A 1 447 ? -44.069 50.384 -4.571 1.00 80.38 ? 447 LEU A CD1 1 ATOM 3429 C CD2 . LEU A 1 447 ? -43.866 48.471 -2.973 1.00 88.27 ? 447 LEU A CD2 1 ATOM 3430 N N . GLU A 1 448 ? -45.826 53.006 -2.715 1.00 101.69 ? 448 GLU A N 1 ATOM 3431 C CA . GLU A 1 448 ? -47.257 53.158 -2.533 1.00 101.04 ? 448 GLU A CA 1 ATOM 3432 C C . GLU A 1 448 ? -47.975 52.488 -3.674 1.00 103.85 ? 448 GLU A C 1 ATOM 3433 O O . GLU A 1 448 ? -47.677 52.742 -4.828 1.00 102.93 ? 448 GLU A O 1 ATOM 3434 C CB . GLU A 1 448 ? -47.653 54.626 -2.492 1.00 110.97 ? 448 GLU A CB 1 ATOM 3435 C CG . GLU A 1 448 ? -48.874 54.909 -1.630 1.00 121.92 ? 448 GLU A CG 1 ATOM 3436 C CD . GLU A 1 448 ? -49.558 56.218 -1.974 1.00 132.73 ? 448 GLU A CD 1 ATOM 3437 O OE1 . GLU A 1 448 ? -49.026 56.959 -2.815 1.00 143.58 ? 448 GLU A OE1 1 ATOM 3438 O OE2 . GLU A 1 448 ? -50.629 56.510 -1.406 1.00 124.95 ? 448 GLU A OE2 1 ATOM 3439 N N . VAL A 1 449 ? -48.922 51.629 -3.331 1.00 116.45 ? 449 VAL A N 1 ATOM 3440 C CA . VAL A 1 449 ? -49.713 50.889 -4.292 1.00 120.90 ? 449 VAL A CA 1 ATOM 3441 C C . VAL A 1 449 ? -51.077 51.491 -4.297 1.00 129.75 ? 449 VAL A C 1 ATOM 3442 O O . VAL A 1 449 ? -51.648 51.733 -3.245 1.00 126.37 ? 449 VAL A O 1 ATOM 3443 C CB . VAL A 1 449 ? -49.972 49.485 -3.810 1.00 122.81 ? 449 VAL A CB 1 ATOM 3444 C CG1 . VAL A 1 449 ? -51.133 49.528 -2.843 1.00 121.64 ? 449 VAL A CG1 1 ATOM 3445 C CG2 . VAL A 1 449 ? -50.327 48.611 -4.985 1.00 122.46 ? 449 VAL A CG2 1 ATOM 3446 N N . TYR A 1 450 ? -51.640 51.826 -5.464 1.00 145.33 ? 450 TYR A N 1 ATOM 3447 C CA . TYR A 1 450 ? -52.926 52.578 -5.530 1.00 149.13 ? 450 TYR A CA 1 ATOM 3448 C C . TYR A 1 450 ? -54.167 51.720 -5.219 1.00 154.23 ? 450 TYR A C 1 ATOM 3449 O O . TYR A 1 450 ? -54.007 50.521 -4.988 1.00 161.35 ? 450 TYR A O 1 ATOM 3450 C CB . TYR A 1 450 ? -53.083 53.251 -6.896 1.00 144.12 ? 450 TYR A CB 1 ATOM 3451 C CG . TYR A 1 450 ? -52.689 54.711 -6.908 1.00 143.70 ? 450 TYR A CG 1 ATOM 3452 C CD1 . TYR A 1 450 ? -53.028 55.532 -7.975 1.00 144.48 ? 450 TYR A CD1 1 ATOM 3453 C CD2 . TYR A 1 450 ? -51.978 55.267 -5.853 1.00 150.04 ? 450 TYR A CD2 1 ATOM 3454 C CE1 . TYR A 1 450 ? -52.670 56.867 -7.991 1.00 150.93 ? 450 TYR A CE1 1 ATOM 3455 C CE2 . TYR A 1 450 ? -51.615 56.601 -5.860 1.00 161.22 ? 450 TYR A CE2 1 ATOM 3456 C CZ . TYR A 1 450 ? -51.964 57.396 -6.931 1.00 164.85 ? 450 TYR A CZ 1 ATOM 3457 O OH . TYR A 1 450 ? -51.605 58.724 -6.942 1.00 173.86 ? 450 TYR A OH 1 ATOM 3458 N N . PRO A 1 451 ? -55.368 52.272 -5.160 1.00 137.12 ? 451 PRO A N 1 ATOM 3459 C CA . PRO A 1 451 ? -56.515 51.423 -4.803 1.00 129.02 ? 451 PRO A CA 1 ATOM 3460 C C . PRO A 1 451 ? -56.092 50.017 -4.319 1.00 122.53 ? 451 PRO A C 1 ATOM 3461 O O . PRO A 1 451 ? -56.444 49.019 -4.949 1.00 144.35 ? 451 PRO A O 1 ATOM 3462 C CB . PRO A 1 451 ? -57.289 51.316 -6.117 1.00 133.49 ? 451 PRO A CB 1 ATOM 3463 C CG . PRO A 1 451 ? -56.947 52.567 -6.852 1.00 135.14 ? 451 PRO A CG 1 ATOM 3464 C CD . PRO A 1 451 ? -55.521 52.875 -6.496 1.00 136.16 ? 451 PRO A CD 1 ATOM 3465 N N . SER A 1 452 ? -55.351 49.959 -3.212 1.00 106.48 ? 452 SER A N 1 ATOM 3466 C CA . SER A 1 452 ? -54.893 48.723 -2.578 1.00 98.05 ? 452 SER A CA 1 ATOM 3467 C C . SER A 1 452 ? -55.930 47.591 -2.473 1.00 112.22 ? 452 SER A C 1 ATOM 3468 O O . SER A 1 452 ? -55.551 46.430 -2.320 1.00 122.85 ? 452 SER A O 1 ATOM 3469 C CB . SER A 1 452 ? -54.319 49.025 -1.191 1.00 97.52 ? 452 SER A CB 1 ATOM 3470 O OG . SER A 1 452 ? -55.109 48.436 -0.172 1.00 111.84 ? 452 SER A OG 1 ATOM 3471 N N . ILE A 1 453 ? -57.222 47.910 -2.542 1.00 107.17 ? 453 ILE A N 1 ATOM 3472 C CA . ILE A 1 453 ? -58.243 46.890 -2.334 1.00 87.33 ? 453 ILE A CA 1 ATOM 3473 C C . ILE A 1 453 ? -58.938 46.621 -3.652 1.00 85.01 ? 453 ILE A C 1 ATOM 3474 O O . ILE A 1 453 ? -59.777 47.414 -4.080 1.00 82.94 ? 453 ILE A O 1 ATOM 3475 C CB . ILE A 1 453 ? -59.284 47.334 -1.291 1.00 89.23 ? 453 ILE A CB 1 ATOM 3476 C CG1 . ILE A 1 453 ? -59.000 46.675 0.060 1.00 87.65 ? 453 ILE A CG1 1 ATOM 3477 C CG2 . ILE A 1 453 ? -60.690 47.000 -1.766 1.00 107.48 ? 453 ILE A CG2 1 ATOM 3478 C CD1 . ILE A 1 453 ? -59.956 47.092 1.156 1.00 90.06 ? 453 ILE A CD1 1 ATOM 3479 N N . LEU A 1 454 ? -58.591 45.523 -4.318 1.00 83.93 ? 454 LEU A N 1 ATOM 3480 C CA . LEU A 1 454 ? -59.113 45.362 -5.657 1.00 85.19 ? 454 LEU A CA 1 ATOM 3481 C C . LEU A 1 454 ? -60.530 44.844 -5.732 1.00 94.09 ? 454 LEU A C 1 ATOM 3482 O O . LEU A 1 454 ? -60.880 43.884 -5.076 1.00 109.67 ? 454 LEU A O 1 ATOM 3483 C CB . LEU A 1 454 ? -58.212 44.431 -6.434 1.00 82.33 ? 454 LEU A CB 1 ATOM 3484 C CG . LEU A 1 454 ? -56.794 44.708 -6.014 1.00 83.24 ? 454 LEU A CG 1 ATOM 3485 C CD1 . LEU A 1 454 ? -55.846 44.488 -7.164 1.00 85.19 ? 454 LEU A CD1 1 ATOM 3486 C CD2 . LEU A 1 454 ? -56.783 46.151 -5.588 1.00 84.55 ? 454 LEU A CD2 1 ATOM 3487 N N . ASN A 1 455 ? -61.336 45.487 -6.560 1.00 88.07 ? 455 ASN A N 1 ATOM 3488 C CA . ASN A 1 455 ? -62.653 44.988 -6.911 1.00 89.47 ? 455 ASN A CA 1 ATOM 3489 C C . ASN A 1 455 ? -62.587 44.157 -8.184 1.00 91.91 ? 455 ASN A C 1 ATOM 3490 O O . ASN A 1 455 ? -62.241 44.664 -9.252 1.00 94.74 ? 455 ASN A O 1 ATOM 3491 C CB . ASN A 1 455 ? -63.645 46.138 -7.076 1.00 89.84 ? 455 ASN A CB 1 ATOM 3492 C CG . ASN A 1 455 ? -65.044 45.653 -7.392 1.00 90.14 ? 455 ASN A CG 1 ATOM 3493 O OD1 . ASN A 1 455 ? -65.420 45.527 -8.556 1.00 101.78 ? 455 ASN A OD1 1 ATOM 3494 N ND2 . ASN A 1 455 ? -65.821 45.370 -6.353 1.00 92.21 ? 455 ASN A ND2 1 ATOM 3495 N N . GLN A 1 456 ? -62.911 42.875 -8.053 1.00 93.96 ? 456 GLN A N 1 ATOM 3496 C CA . GLN A 1 456 ? -62.877 41.939 -9.172 1.00 97.84 ? 456 GLN A CA 1 ATOM 3497 C C . GLN A 1 456 ? -63.723 42.407 -10.349 1.00 100.74 ? 456 GLN A C 1 ATOM 3498 O O . GLN A 1 456 ? -63.349 42.218 -11.507 1.00 100.91 ? 456 GLN A O 1 ATOM 3499 C CB . GLN A 1 456 ? -63.356 40.556 -8.719 1.00 98.41 ? 456 GLN A CB 1 ATOM 3500 C CG . GLN A 1 456 ? -62.335 39.750 -7.933 1.00 97.36 ? 456 GLN A CG 1 ATOM 3501 C CD . GLN A 1 456 ? -61.368 38.997 -8.829 1.00 104.70 ? 456 GLN A CD 1 ATOM 3502 O OE1 . GLN A 1 456 ? -60.910 39.517 -9.846 1.00 123.58 ? 456 GLN A OE1 1 ATOM 3503 N NE2 . GLN A 1 456 ? -61.061 37.760 -8.458 1.00 96.33 ? 456 GLN A NE2 1 ATOM 3504 N N . ASP A 1 457 ? -64.862 43.021 -10.047 1.00 107.66 ? 457 ASP A N 1 ATOM 3505 C CA . ASP A 1 457 ? -65.825 43.383 -11.079 1.00 113.20 ? 457 ASP A CA 1 ATOM 3506 C C . ASP A 1 457 ? -65.647 44.812 -11.584 1.00 125.28 ? 457 ASP A C 1 ATOM 3507 O O . ASP A 1 457 ? -66.437 45.286 -12.400 1.00 135.02 ? 457 ASP A O 1 ATOM 3508 C CB . ASP A 1 457 ? -67.252 43.191 -10.563 1.00 110.71 ? 457 ASP A CB 1 ATOM 3509 C CG . ASP A 1 457 ? -68.221 42.819 -11.668 1.00 128.14 ? 457 ASP A CG 1 ATOM 3510 O OD1 . ASP A 1 457 ? -68.769 43.734 -12.318 1.00 137.50 ? 457 ASP A OD1 1 ATOM 3511 O OD2 . ASP A 1 457 ? -68.431 41.608 -11.890 1.00 132.15 ? 457 ASP A OD2 1 ATOM 3512 N N . ASN A 1 458 ? -64.611 45.499 -11.111 1.00 124.07 ? 458 ASN A N 1 ATOM 3513 C CA . ASN A 1 458 ? -64.342 46.842 -11.609 1.00 125.25 ? 458 ASN A CA 1 ATOM 3514 C C . ASN A 1 458 ? -63.236 46.766 -12.649 1.00 126.71 ? 458 ASN A C 1 ATOM 3515 O O . ASN A 1 458 ? -62.057 46.644 -12.330 1.00 138.22 ? 458 ASN A O 1 ATOM 3516 C CB . ASN A 1 458 ? -63.961 47.774 -10.457 1.00 130.46 ? 458 ASN A CB 1 ATOM 3517 C CG . ASN A 1 458 ? -63.438 49.119 -10.928 1.00 137.62 ? 458 ASN A CG 1 ATOM 3518 O OD1 . ASN A 1 458 ? -63.793 49.607 -12.003 1.00 133.78 ? 458 ASN A OD1 1 ATOM 3519 N ND2 . ASN A 1 458 ? -62.584 49.728 -10.112 1.00 156.04 ? 458 ASN A ND2 1 ATOM 3520 N N . LYS A 1 459 ? -63.662 46.875 -13.901 1.00 121.90 ? 459 LYS A N 1 ATOM 3521 C CA . LYS A 1 459 ? -62.858 46.572 -15.082 1.00 121.87 ? 459 LYS A CA 1 ATOM 3522 C C . LYS A 1 459 ? -62.257 47.807 -15.741 1.00 133.59 ? 459 LYS A C 1 ATOM 3523 O O . LYS A 1 459 ? -61.788 47.735 -16.879 1.00 133.54 ? 459 LYS A O 1 ATOM 3524 C CB . LYS A 1 459 ? -63.698 45.776 -16.076 1.00 119.52 ? 459 LYS A CB 1 ATOM 3525 C CG . LYS A 1 459 ? -64.047 44.395 -15.545 1.00 115.48 ? 459 LYS A CG 1 ATOM 3526 C CD . LYS A 1 459 ? -65.113 43.704 -16.355 1.00 121.93 ? 459 LYS A CD 1 ATOM 3527 C CE . LYS A 1 459 ? -65.580 42.447 -15.648 1.00 113.95 ? 459 LYS A CE 1 ATOM 3528 N NZ . LYS A 1 459 ? -66.687 41.777 -16.376 1.00 110.20 ? 459 LYS A NZ 1 ATOM 3529 N N . THR A 1 460 ? -62.308 48.933 -15.032 1.00 139.69 ? 460 THR A N 1 ATOM 3530 C CA . THR A 1 460 ? -62.189 50.276 -15.606 1.00 137.19 ? 460 THR A CA 1 ATOM 3531 C C . THR A 1 460 ? -61.133 50.461 -16.687 1.00 133.14 ? 460 THR A C 1 ATOM 3532 O O . THR A 1 460 ? -61.473 50.735 -17.839 1.00 143.64 ? 460 THR A O 1 ATOM 3533 C CB . THR A 1 460 ? -61.885 51.316 -14.499 1.00 135.17 ? 460 THR A CB 1 ATOM 3534 O OG1 . THR A 1 460 ? -62.910 51.280 -13.496 1.00 138.21 ? 460 THR A OG1 1 ATOM 3535 C CG2 . THR A 1 460 ? -61.816 52.709 -15.093 1.00 133.33 ? 460 THR A CG2 1 ATOM 3536 N N . CYS A 1 461 ? -59.864 50.325 -16.320 1.00 129.03 ? 461 CYS A N 1 ATOM 3537 C CA . CYS A 1 461 ? -58.773 50.578 -17.251 1.00 135.25 ? 461 CYS A CA 1 ATOM 3538 C C . CYS A 1 461 ? -58.212 49.297 -17.847 1.00 139.40 ? 461 CYS A C 1 ATOM 3539 O O . CYS A 1 461 ? -57.614 48.476 -17.146 1.00 150.42 ? 461 CYS A O 1 ATOM 3540 C CB . CYS A 1 461 ? -57.658 51.354 -16.548 1.00 142.21 ? 461 CYS A CB 1 ATOM 3541 S SG . CYS A 1 461 ? -57.938 51.516 -14.774 1.00 244.82 ? 461 CYS A SG 1 ATOM 3542 N N . SER A 1 462 ? -58.412 49.144 -19.149 1.00 137.90 ? 462 SER A N 1 ATOM 3543 C CA . SER A 1 462 ? -57.797 48.074 -19.902 1.00 142.09 ? 462 SER A CA 1 ATOM 3544 C C . SER A 1 462 ? -57.270 48.613 -21.218 1.00 145.50 ? 462 SER A C 1 ATOM 3545 O O . SER A 1 462 ? -58.018 49.193 -22.003 1.00 148.84 ? 462 SER A O 1 ATOM 3546 C CB . SER A 1 462 ? -58.794 46.940 -20.163 1.00 150.30 ? 462 SER A CB 1 ATOM 3547 O OG . SER A 1 462 ? -59.809 47.338 -21.065 1.00 163.57 ? 462 SER A OG 1 ATOM 3548 N N . LEU A 1 463 ? -55.975 48.429 -21.448 1.00 156.21 ? 463 LEU A N 1 ATOM 3549 C CA . LEU A 1 463 ? -55.417 48.552 -22.786 1.00 165.09 ? 463 LEU A CA 1 ATOM 3550 C C . LEU A 1 463 ? -54.417 47.423 -23.049 1.00 164.21 ? 463 LEU A C 1 ATOM 3551 O O . LEU A 1 463 ? -53.262 47.695 -23.379 1.00 164.02 ? 463 LEU A O 1 ATOM 3552 C CB . LEU A 1 463 ? -54.735 49.910 -22.960 1.00 161.75 ? 463 LEU A CB 1 ATOM 3553 C CG . LEU A 1 463 ? -55.036 50.736 -24.214 1.00 157.51 ? 463 LEU A CG 1 ATOM 3554 C CD1 . LEU A 1 463 ? -54.123 51.951 -24.263 1.00 161.57 ? 463 LEU A CD1 1 ATOM 3555 C CD2 . LEU A 1 463 ? -54.911 49.913 -25.492 1.00 150.74 ? 463 LEU A CD2 1 ATOM 3556 N N . PRO A 1 464 ? -54.850 46.148 -22.920 1.00 155.38 ? 464 PRO A N 1 ATOM 3557 C CA . PRO A 1 464 ? -53.908 45.064 -23.212 1.00 151.46 ? 464 PRO A CA 1 ATOM 3558 C C . PRO A 1 464 ? -53.986 44.513 -24.642 1.00 154.93 ? 464 PRO A C 1 ATOM 3559 O O . PRO A 1 464 ? -54.582 43.450 -24.831 1.00 164.45 ? 464 PRO A O 1 ATOM 3560 C CB . PRO A 1 464 ? -54.313 43.987 -22.201 1.00 151.62 ? 464 PRO A CB 1 ATOM 3561 C CG . PRO A 1 464 ? -55.798 44.157 -22.075 1.00 150.67 ? 464 PRO A CG 1 ATOM 3562 C CD . PRO A 1 464 ? -56.120 45.608 -22.394 1.00 150.79 ? 464 PRO A CD 1 ATOM 3563 N N . GLY A 1 465 ? -53.403 45.190 -25.629 1.00 152.62 ? 465 GLY A N 1 ATOM 3564 C CA . GLY A 1 465 ? -53.295 44.566 -26.939 1.00 158.63 ? 465 GLY A CA 1 ATOM 3565 C C . GLY A 1 465 ? -54.605 44.375 -27.685 1.00 158.05 ? 465 GLY A C 1 ATOM 3566 O O . GLY A 1 465 ? -55.044 43.235 -27.849 1.00 151.26 ? 465 GLY A O 1 ATOM 3567 N N . THR A 1 466 ? -55.242 45.479 -28.089 1.00 160.80 ? 466 THR A N 1 ATOM 3568 C CA . THR A 1 466 ? -56.637 45.490 -28.554 1.00 162.15 ? 466 THR A CA 1 ATOM 3569 C C . THR A 1 466 ? -57.551 45.112 -27.388 1.00 160.94 ? 466 THR A C 1 ATOM 3570 O O . THR A 1 466 ? -58.052 43.990 -27.279 1.00 157.78 ? 466 THR A O 1 ATOM 3571 C CB . THR A 1 466 ? -56.879 44.558 -29.764 1.00 156.25 ? 466 THR A CB 1 ATOM 3572 O OG1 . THR A 1 466 ? -55.858 44.763 -30.749 1.00 150.32 ? 466 THR A OG1 1 ATOM 3573 C CG2 . THR A 1 466 ? -58.233 44.842 -30.386 1.00 153.49 ? 466 THR A CG2 1 ATOM 3574 N N . ALA A 1 467 ? -57.709 46.106 -26.516 1.00 159.76 ? 467 ALA A N 1 ATOM 3575 C CA . ALA A 1 467 ? -58.233 46.014 -25.158 1.00 152.70 ? 467 ALA A CA 1 ATOM 3576 C C . ALA A 1 467 ? -59.568 45.315 -24.958 1.00 146.43 ? 467 ALA A C 1 ATOM 3577 O O . ALA A 1 467 ? -60.499 45.472 -25.746 1.00 139.77 ? 467 ALA A O 1 ATOM 3578 C CB . ALA A 1 467 ? -58.330 47.418 -24.592 1.00 152.14 ? 467 ALA A CB 1 ATOM 3579 N N . LEU A 1 468 ? -59.621 44.531 -23.884 1.00 145.63 ? 468 LEU A N 1 ATOM 3580 C CA . LEU A 1 468 ? -60.860 44.039 -23.293 1.00 135.80 ? 468 LEU A CA 1 ATOM 3581 C C . LEU A 1 468 ? -60.851 44.393 -21.809 1.00 128.86 ? 468 LEU A C 1 ATOM 3582 O O . LEU A 1 468 ? -59.829 44.230 -21.144 1.00 133.78 ? 468 LEU A O 1 ATOM 3583 C CB . LEU A 1 468 ? -61.005 42.531 -23.480 1.00 136.41 ? 468 LEU A CB 1 ATOM 3584 C CG . LEU A 1 468 ? -60.969 42.008 -24.914 1.00 145.24 ? 468 LEU A CG 1 ATOM 3585 C CD1 . LEU A 1 468 ? -61.081 40.495 -24.910 1.00 153.17 ? 468 LEU A CD1 1 ATOM 3586 C CD2 . LEU A 1 468 ? -62.081 42.632 -25.738 1.00 137.51 ? 468 LEU A CD2 1 ATOM 3587 N N . LYS A 1 469 ? -61.991 44.844 -21.291 1.00 131.18 ? 469 LYS A N 1 ATOM 3588 C CA . LYS A 1 469 ? -62.082 45.391 -19.934 1.00 134.81 ? 469 LYS A CA 1 ATOM 3589 C C . LYS A 1 469 ? -61.475 44.483 -18.855 1.00 127.21 ? 469 LYS A C 1 ATOM 3590 O O . LYS A 1 469 ? -61.788 43.295 -18.780 1.00 131.53 ? 469 LYS A O 1 ATOM 3591 C CB . LYS A 1 469 ? -63.547 45.686 -19.593 1.00 143.04 ? 469 LYS A CB 1 ATOM 3592 C CG . LYS A 1 469 ? -64.111 46.939 -20.250 1.00 140.02 ? 469 LYS A CG 1 ATOM 3593 C CD . LYS A 1 469 ? -63.417 48.193 -19.737 1.00 129.94 ? 469 LYS A CD 1 ATOM 3594 C CE . LYS A 1 469 ? -64.021 49.455 -20.335 1.00 124.64 ? 469 LYS A CE 1 ATOM 3595 N NZ . LYS A 1 469 ? -63.371 50.689 -19.809 1.00 120.31 ? 469 LYS A NZ 1 ATOM 3596 N N . VAL A 1 470 ? -60.604 45.060 -18.026 1.00 118.77 ? 470 VAL A N 1 ATOM 3597 C CA . VAL A 1 470 ? -59.917 44.315 -16.969 1.00 116.91 ? 470 VAL A CA 1 ATOM 3598 C C . VAL A 1 470 ? -59.645 45.198 -15.744 1.00 114.04 ? 470 VAL A C 1 ATOM 3599 O O . VAL A 1 470 ? -59.449 46.408 -15.867 1.00 115.51 ? 470 VAL A O 1 ATOM 3600 C CB . VAL A 1 470 ? -58.580 43.712 -17.479 1.00 99.46 ? 470 VAL A CB 1 ATOM 3601 C CG1 . VAL A 1 470 ? -57.526 44.797 -17.678 1.00 93.99 ? 470 VAL A CG1 1 ATOM 3602 C CG2 . VAL A 1 470 ? -58.072 42.633 -16.528 1.00 92.68 ? 470 VAL A CG2 1 ATOM 3603 N N . SER A 1 471 ? -59.644 44.583 -14.564 1.00 113.07 ? 471 SER A N 1 ATOM 3604 C CA . SER A 1 471 ? -59.398 45.294 -13.311 1.00 112.36 ? 471 SER A CA 1 ATOM 3605 C C . SER A 1 471 ? -57.935 45.688 -13.159 1.00 116.42 ? 471 SER A C 1 ATOM 3606 O O . SER A 1 471 ? -57.048 44.844 -13.255 1.00 117.63 ? 471 SER A O 1 ATOM 3607 C CB . SER A 1 471 ? -59.825 44.436 -12.118 1.00 108.04 ? 471 SER A CB 1 ATOM 3608 O OG . SER A 1 471 ? -59.596 45.113 -10.895 1.00 103.21 ? 471 SER A OG 1 ATOM 3609 N N . CYS A 1 472 ? -57.687 46.969 -12.902 1.00 117.55 ? 472 CYS A N 1 ATOM 3610 C CA . CYS A 1 472 ? -56.321 47.476 -12.823 1.00 112.22 ? 472 CYS A CA 1 ATOM 3611 C C . CYS A 1 472 ? -56.065 48.307 -11.571 1.00 114.73 ? 472 CYS A C 1 ATOM 3612 O O . CYS A 1 472 ? -56.996 48.726 -10.885 1.00 113.62 ? 472 CYS A O 1 ATOM 3613 C CB . CYS A 1 472 ? -55.998 48.313 -14.062 1.00 105.34 ? 472 CYS A CB 1 ATOM 3614 S SG . CYS A 1 472 ? -57.006 49.801 -14.224 1.00 233.84 ? 472 CYS A SG 1 ATOM 3615 N N . PHE A 1 473 ? -54.786 48.531 -11.286 1.00 115.57 ? 473 PHE A N 1 ATOM 3616 C CA . PHE A 1 473 ? -54.357 49.410 -10.205 1.00 108.69 ? 473 PHE A CA 1 ATOM 3617 C C . PHE A 1 473 ? -52.953 49.925 -10.509 1.00 113.20 ? 473 PHE A C 1 ATOM 3618 O O . PHE A 1 473 ? -52.249 49.356 -11.344 1.00 115.41 ? 473 PHE A O 1 ATOM 3619 C CB . PHE A 1 473 ? -54.391 48.685 -8.856 1.00 103.79 ? 473 PHE A CB 1 ATOM 3620 C CG . PHE A 1 473 ? -53.496 47.478 -8.789 1.00 101.67 ? 473 PHE A CG 1 ATOM 3621 C CD1 . PHE A 1 473 ? -52.204 47.581 -8.300 1.00 101.70 ? 473 PHE A CD1 1 ATOM 3622 C CD2 . PHE A 1 473 ? -53.950 46.238 -9.209 1.00 99.78 ? 473 PHE A CD2 1 ATOM 3623 C CE1 . PHE A 1 473 ? -51.381 46.473 -8.235 1.00 100.85 ? 473 PHE A CE1 1 ATOM 3624 C CE2 . PHE A 1 473 ? -53.133 45.126 -9.146 1.00 96.27 ? 473 PHE A CE2 1 ATOM 3625 C CZ . PHE A 1 473 ? -51.846 45.244 -8.658 1.00 94.23 ? 473 PHE A CZ 1 ATOM 3626 N N . ASN A 1 474 ? -52.548 50.999 -9.839 1.00 118.00 ? 474 ASN A N 1 ATOM 3627 C CA . ASN A 1 474 ? -51.253 51.613 -10.114 1.00 124.14 ? 474 ASN A CA 1 ATOM 3628 C C . ASN A 1 474 ? -50.232 51.360 -9.009 1.00 120.99 ? 474 ASN A C 1 ATOM 3629 O O . ASN A 1 474 ? -50.576 51.323 -7.828 1.00 127.70 ? 474 ASN A O 1 ATOM 3630 C CB . ASN A 1 474 ? -51.413 53.120 -10.325 1.00 130.98 ? 474 ASN A CB 1 ATOM 3631 C CG . ASN A 1 474 ? -52.849 53.523 -10.603 1.00 154.16 ? 474 ASN A CG 1 ATOM 3632 O OD1 . ASN A 1 474 ? -53.790 52.887 -10.129 1.00 169.76 ? 474 ASN A OD1 1 ATOM 3633 N ND2 . ASN A 1 474 ? -53.024 54.590 -11.374 1.00 153.87 ? 474 ASN A ND2 1 ATOM 3634 N N . VAL A 1 475 ? -48.974 51.186 -9.403 1.00 118.73 ? 475 VAL A N 1 ATOM 3635 C CA . VAL A 1 475 ? -47.890 50.996 -8.447 1.00 116.00 ? 475 VAL A CA 1 ATOM 3636 C C . VAL A 1 475 ? -46.908 52.163 -8.503 1.00 126.30 ? 475 VAL A C 1 ATOM 3637 O O . VAL A 1 475 ? -46.203 52.347 -9.496 1.00 138.01 ? 475 VAL A O 1 ATOM 3638 C CB . VAL A 1 475 ? -47.133 49.680 -8.701 1.00 113.56 ? 475 VAL A CB 1 ATOM 3639 C CG1 . VAL A 1 475 ? -45.967 49.543 -7.733 1.00 111.49 ? 475 VAL A CG1 1 ATOM 3640 C CG2 . VAL A 1 475 ? -48.077 48.495 -8.579 1.00 113.09 ? 475 VAL A CG2 1 ATOM 3641 N N . ARG A 1 476 ? -46.869 52.947 -7.430 1.00 128.33 ? 476 ARG A N 1 ATOM 3642 C CA . ARG A 1 476 ? -46.008 54.123 -7.362 1.00 128.97 ? 476 ARG A CA 1 ATOM 3643 C C . ARG A 1 476 ? -44.902 53.927 -6.329 1.00 123.47 ? 476 ARG A C 1 ATOM 3644 O O . ARG A 1 476 ? -45.158 53.468 -5.216 1.00 130.75 ? 476 ARG A O 1 ATOM 3645 C CB . ARG A 1 476 ? -46.837 55.365 -7.029 1.00 124.28 ? 476 ARG A CB 1 ATOM 3646 C CG . ARG A 1 476 ? -46.045 56.659 -6.957 1.00 110.22 ? 476 ARG A CG 1 ATOM 3647 C CD . ARG A 1 476 ? -46.944 57.816 -6.548 1.00 109.15 ? 476 ARG A CD 1 ATOM 3648 N NE . ARG A 1 476 ? -46.194 59.049 -6.333 1.00 117.79 ? 476 ARG A NE 1 ATOM 3649 C CZ . ARG A 1 476 ? -45.977 59.966 -7.270 1.00 129.13 ? 476 ARG A CZ 1 ATOM 3650 N NH1 . ARG A 1 476 ? -46.455 59.790 -8.495 1.00 137.10 ? 476 ARG A NH1 1 ATOM 3651 N NH2 . ARG A 1 476 ? -45.284 61.059 -6.983 1.00 125.51 ? 476 ARG A NH2 1 ATOM 3652 N N . PHE A 1 477 ? -43.674 54.275 -6.702 1.00 111.66 ? 477 PHE A N 1 ATOM 3653 C CA . PHE A 1 477 ? -42.526 54.073 -5.823 1.00 110.22 ? 477 PHE A CA 1 ATOM 3654 C C . PHE A 1 477 ? -41.535 55.232 -5.896 1.00 108.91 ? 477 PHE A C 1 ATOM 3655 O O . PHE A 1 477 ? -41.154 55.666 -6.980 1.00 112.29 ? 477 PHE A O 1 ATOM 3656 C CB . PHE A 1 477 ? -41.826 52.753 -6.162 1.00 107.22 ? 477 PHE A CB 1 ATOM 3657 C CG . PHE A 1 477 ? -41.373 52.645 -7.595 1.00 99.48 ? 477 PHE A CG 1 ATOM 3658 C CD1 . PHE A 1 477 ? -40.051 52.880 -7.936 1.00 98.66 ? 477 PHE A CD1 1 ATOM 3659 C CD2 . PHE A 1 477 ? -42.264 52.291 -8.596 1.00 98.70 ? 477 PHE A CD2 1 ATOM 3660 C CE1 . PHE A 1 477 ? -39.630 52.775 -9.249 1.00 98.70 ? 477 PHE A CE1 1 ATOM 3661 C CE2 . PHE A 1 477 ? -41.848 52.187 -9.910 1.00 99.38 ? 477 PHE A CE2 1 ATOM 3662 C CZ . PHE A 1 477 ? -40.530 52.429 -10.236 1.00 99.32 ? 477 PHE A CZ 1 ATOM 3663 N N . CYS A 1 478 ? -41.112 55.719 -4.732 1.00 109.07 ? 478 CYS A N 1 ATOM 3664 C CA . CYS A 1 478 ? -40.226 56.878 -4.654 1.00 122.95 ? 478 CYS A CA 1 ATOM 3665 C C . CYS A 1 478 ? -38.833 56.495 -4.160 1.00 122.60 ? 478 CYS A C 1 ATOM 3666 O O . CYS A 1 478 ? -38.673 55.536 -3.405 1.00 116.13 ? 478 CYS A O 1 ATOM 3667 C CB . CYS A 1 478 ? -40.828 57.946 -3.740 1.00 132.04 ? 478 CYS A CB 1 ATOM 3668 S SG . CYS A 1 478 ? -42.462 58.530 -4.248 1.00 190.43 ? 478 CYS A SG 1 ATOM 3669 N N . LEU A 1 479 ? -37.826 57.250 -4.592 1.00 121.29 ? 479 LEU A N 1 ATOM 3670 C CA . LEU A 1 479 ? -36.442 56.946 -4.245 1.00 113.24 ? 479 LEU A CA 1 ATOM 3671 C C . LEU A 1 479 ? -35.657 58.193 -3.832 1.00 110.28 ? 479 LEU A C 1 ATOM 3672 O O . LEU A 1 479 ? -35.501 59.127 -4.618 1.00 110.33 ? 479 LEU A O 1 ATOM 3673 C CB . LEU A 1 479 ? -35.753 56.259 -5.425 1.00 113.58 ? 479 LEU A CB 1 ATOM 3674 C CG . LEU A 1 479 ? -34.508 55.424 -5.131 1.00 114.17 ? 479 LEU A CG 1 ATOM 3675 C CD1 . LEU A 1 479 ? -34.834 54.322 -4.140 1.00 90.54 ? 479 LEU A CD1 1 ATOM 3676 C CD2 . LEU A 1 479 ? -33.959 54.838 -6.418 1.00 101.98 ? 479 LEU A CD2 1 ATOM 3677 N N . LYS A 1 480 ? -35.159 58.197 -2.598 1.00 115.08 ? 480 LYS A N 1 ATOM 3678 C CA . LYS A 1 480 ? -34.352 59.304 -2.087 1.00 119.15 ? 480 LYS A CA 1 ATOM 3679 C C . LYS A 1 480 ? -32.912 58.867 -1.851 1.00 120.51 ? 480 LYS A C 1 ATOM 3680 O O . LYS A 1 480 ? -32.666 57.805 -1.284 1.00 124.73 ? 480 LYS A O 1 ATOM 3681 C CB . LYS A 1 480 ? -34.943 59.849 -0.785 1.00 127.81 ? 480 LYS A CB 1 ATOM 3682 C CG . LYS A 1 480 ? -34.132 60.967 -0.146 1.00 138.14 ? 480 LYS A CG 1 ATOM 3683 C CD . LYS A 1 480 ? -34.597 61.241 1.276 1.00 138.43 ? 480 LYS A CD 1 ATOM 3684 C CE . LYS A 1 480 ? -36.073 61.600 1.320 1.00 131.17 ? 480 LYS A CE 1 ATOM 3685 N NZ . LYS A 1 480 ? -36.548 61.829 2.712 1.00 121.41 ? 480 LYS A NZ 1 ATOM 3686 N N . ALA A 1 481 ? -31.963 59.693 -2.279 1.00 116.82 ? 481 ALA A N 1 ATOM 3687 C CA . ALA A 1 481 ? -30.552 59.383 -2.089 1.00 112.57 ? 481 ALA A CA 1 ATOM 3688 C C . ALA A 1 481 ? -29.769 60.602 -1.611 1.00 116.84 ? 481 ALA A C 1 ATOM 3689 O O . ALA A 1 481 ? -29.765 61.644 -2.266 1.00 128.73 ? 481 ALA A O 1 ATOM 3690 C CB . ALA A 1 481 ? -29.954 58.844 -3.378 1.00 115.49 ? 481 ALA A CB 1 ATOM 3691 N N . ASP A 1 482 ? -29.106 60.465 -0.467 1.00 113.41 ? 482 ASP A N 1 ATOM 3692 C CA . ASP A 1 482 ? -28.274 61.535 0.070 1.00 126.88 ? 482 ASP A CA 1 ATOM 3693 C C . ASP A 1 482 ? -27.149 60.964 0.927 1.00 118.51 ? 482 ASP A C 1 ATOM 3694 O O . ASP A 1 482 ? -27.258 59.855 1.451 1.00 113.02 ? 482 ASP A O 1 ATOM 3695 C CB . ASP A 1 482 ? -29.117 62.518 0.886 1.00 140.33 ? 482 ASP A CB 1 ATOM 3696 C CG . ASP A 1 482 ? -28.382 63.813 1.179 1.00 141.83 ? 482 ASP A CG 1 ATOM 3697 O OD1 . ASP A 1 482 ? -27.726 63.902 2.239 1.00 147.18 ? 482 ASP A OD1 1 ATOM 3698 O OD2 . ASP A 1 482 ? -28.458 64.741 0.347 1.00 129.25 ? 482 ASP A OD2 1 ATOM 3699 N N . GLY A 1 483 ? -26.069 61.726 1.066 1.00 118.05 ? 483 GLY A N 1 ATOM 3700 C CA . GLY A 1 483 ? -24.920 61.286 1.835 1.00 114.81 ? 483 GLY A CA 1 ATOM 3701 C C . GLY A 1 483 ? -24.050 62.437 2.303 1.00 119.10 ? 483 GLY A C 1 ATOM 3702 O O . GLY A 1 483 ? -24.409 63.604 2.148 1.00 127.60 ? 483 GLY A O 1 ATOM 3703 N N . LYS A 1 484 ? -22.900 62.101 2.877 1.00 108.86 ? 484 LYS A N 1 ATOM 3704 C CA . LYS A 1 484 ? -21.964 63.101 3.377 1.00 94.71 ? 484 LYS A CA 1 ATOM 3705 C C . LYS A 1 484 ? -20.603 62.940 2.712 1.00 90.12 ? 484 LYS A C 1 ATOM 3706 O O . LYS A 1 484 ? -20.318 61.907 2.107 1.00 88.17 ? 484 LYS A O 1 ATOM 3707 C CB . LYS A 1 484 ? -21.823 62.999 4.897 1.00 93.42 ? 484 LYS A CB 1 ATOM 3708 C CG . LYS A 1 484 ? -23.106 63.273 5.663 1.00 100.09 ? 484 LYS A CG 1 ATOM 3709 C CD . LYS A 1 484 ? -22.877 63.183 7.163 1.00 106.68 ? 484 LYS A CD 1 ATOM 3710 C CE . LYS A 1 484 ? -21.837 64.192 7.621 1.00 117.81 ? 484 LYS A CE 1 ATOM 3711 N NZ . LYS A 1 484 ? -21.541 64.064 9.075 1.00 120.95 ? 484 LYS A NZ 1 ATOM 3712 N N . GLY A 1 485 ? -19.768 63.968 2.818 1.00 89.29 ? 485 GLY A N 1 ATOM 3713 C CA . GLY A 1 485 ? -18.468 63.957 2.174 1.00 89.47 ? 485 GLY A CA 1 ATOM 3714 C C . GLY A 1 485 ? -18.622 64.113 0.675 1.00 89.72 ? 485 GLY A C 1 ATOM 3715 O O . GLY A 1 485 ? -19.714 64.407 0.190 1.00 91.87 ? 485 GLY A O 1 ATOM 3716 N N . VAL A 1 486 ? -17.536 63.919 -0.066 1.00 91.17 ? 486 VAL A N 1 ATOM 3717 C CA . VAL A 1 486 ? -17.603 64.053 -1.514 1.00 101.10 ? 486 VAL A CA 1 ATOM 3718 C C . VAL A 1 486 ? -18.214 62.798 -2.135 1.00 102.79 ? 486 VAL A C 1 ATOM 3719 O O . VAL A 1 486 ? -17.965 61.676 -1.686 1.00 102.62 ? 486 VAL A O 1 ATOM 3720 C CB . VAL A 1 486 ? -16.214 64.334 -2.137 1.00 102.83 ? 486 VAL A CB 1 ATOM 3721 C CG1 . VAL A 1 486 ? -15.569 65.539 -1.468 1.00 106.27 ? 486 VAL A CG1 1 ATOM 3722 C CG2 . VAL A 1 486 ? -15.309 63.121 -2.037 1.00 97.09 ? 486 VAL A CG2 1 ATOM 3723 N N . LEU A 1 487 ? -19.023 63.013 -3.167 1.00 110.84 ? 487 LEU A N 1 ATOM 3724 C CA . LEU A 1 487 ? -19.747 61.950 -3.857 1.00 117.98 ? 487 LEU A CA 1 ATOM 3725 C C . LEU A 1 487 ? -20.508 62.579 -5.019 1.00 130.66 ? 487 LEU A C 1 ATOM 3726 O O . LEU A 1 487 ? -21.005 63.699 -4.897 1.00 140.63 ? 487 LEU A O 1 ATOM 3727 C CB . LEU A 1 487 ? -20.702 61.205 -2.910 1.00 102.36 ? 487 LEU A CB 1 ATOM 3728 C CG . LEU A 1 487 ? -22.055 61.791 -2.488 1.00 100.60 ? 487 LEU A CG 1 ATOM 3729 C CD1 . LEU A 1 487 ? -22.772 60.817 -1.563 1.00 95.30 ? 487 LEU A CD1 1 ATOM 3730 C CD2 . LEU A 1 487 ? -21.919 63.151 -1.820 1.00 103.97 ? 487 LEU A CD2 1 ATOM 3731 N N . PRO A 1 488 ? -20.590 61.864 -6.152 1.00 125.67 ? 488 PRO A N 1 ATOM 3732 C CA . PRO A 1 488 ? -21.147 62.395 -7.402 1.00 125.86 ? 488 PRO A CA 1 ATOM 3733 C C . PRO A 1 488 ? -22.526 63.025 -7.251 1.00 116.40 ? 488 PRO A C 1 ATOM 3734 O O . PRO A 1 488 ? -23.315 62.614 -6.400 1.00 110.02 ? 488 PRO A O 1 ATOM 3735 C CB . PRO A 1 488 ? -21.214 61.159 -8.297 1.00 124.19 ? 488 PRO A CB 1 ATOM 3736 C CG . PRO A 1 488 ? -20.074 60.342 -7.838 1.00 121.75 ? 488 PRO A CG 1 ATOM 3737 C CD . PRO A 1 488 ? -20.047 60.508 -6.342 1.00 118.90 ? 488 PRO A CD 1 ATOM 3738 N N . ARG A 1 489 ? -22.785 64.033 -8.079 1.00 113.21 ? 489 ARG A N 1 ATOM 3739 C CA . ARG A 1 489 ? -24.027 64.792 -8.035 1.00 120.61 ? 489 ARG A CA 1 ATOM 3740 C C . ARG A 1 489 ? -25.242 63.886 -8.172 1.00 118.41 ? 489 ARG A C 1 ATOM 3741 O O . ARG A 1 489 ? -26.241 64.067 -7.479 1.00 111.38 ? 489 ARG A O 1 ATOM 3742 C CB . ARG A 1 489 ? -24.044 65.855 -9.138 1.00 136.66 ? 489 ARG A CB 1 ATOM 3743 C CG . ARG A 1 489 ? -22.753 66.653 -9.273 1.00 146.99 ? 489 ARG A CG 1 ATOM 3744 C CD . ARG A 1 489 ? -21.844 66.073 -10.352 1.00 156.50 ? 489 ARG A CD 1 ATOM 3745 N NE . ARG A 1 489 ? -22.461 66.127 -11.674 1.00 164.07 ? 489 ARG A NE 1 ATOM 3746 C CZ . ARG A 1 489 ? -21.899 65.652 -12.782 1.00 159.11 ? 489 ARG A CZ 1 ATOM 3747 N NH1 . ARG A 1 489 ? -20.704 65.081 -12.730 1.00 156.91 ? 489 ARG A NH1 1 ATOM 3748 N NH2 . ARG A 1 489 ? -22.535 65.745 -13.942 1.00 152.31 ? 489 ARG A NH2 1 ATOM 3749 N N . LYS A 1 490 ? -25.149 62.906 -9.065 1.00 119.04 ? 490 LYS A N 1 ATOM 3750 C CA . LYS A 1 490 ? -26.266 62.007 -9.325 1.00 114.47 ? 490 LYS A CA 1 ATOM 3751 C C . LYS A 1 490 ? -25.857 60.538 -9.257 1.00 114.59 ? 490 LYS A C 1 ATOM 3752 O O . LYS A 1 490 ? -24.748 60.170 -9.643 1.00 121.08 ? 490 LYS A O 1 ATOM 3753 C CB . LYS A 1 490 ? -26.886 62.319 -10.688 1.00 122.64 ? 490 LYS A CB 1 ATOM 3754 C CG . LYS A 1 490 ? -27.531 63.694 -10.764 1.00 131.17 ? 490 LYS A CG 1 ATOM 3755 C CD . LYS A 1 490 ? -28.097 63.974 -12.144 1.00 145.10 ? 490 LYS A CD 1 ATOM 3756 C CE . LYS A 1 490 ? -28.742 65.349 -12.199 1.00 150.24 ? 490 LYS A CE 1 ATOM 3757 N NZ . LYS A 1 490 ? -27.785 66.425 -11.820 1.00 143.36 ? 490 LYS A NZ 1 ATOM 3758 N N . LEU A 1 491 ? -26.771 59.706 -8.766 1.00 116.34 ? 491 LEU A N 1 ATOM 3759 C CA . LEU A 1 491 ? -26.516 58.280 -8.593 1.00 115.41 ? 491 LEU A CA 1 ATOM 3760 C C . LEU A 1 491 ? -27.440 57.454 -9.481 1.00 121.72 ? 491 LEU A C 1 ATOM 3761 O O . LEU A 1 491 ? -28.525 57.903 -9.839 1.00 122.03 ? 491 LEU A O 1 ATOM 3762 C CB . LEU A 1 491 ? -26.702 57.882 -7.129 1.00 105.75 ? 491 LEU A CB 1 ATOM 3763 C CG . LEU A 1 491 ? -26.075 58.824 -6.100 1.00 109.22 ? 491 LEU A CG 1 ATOM 3764 C CD1 . LEU A 1 491 ? -26.539 58.468 -4.699 1.00 105.60 ? 491 LEU A CD1 1 ATOM 3765 C CD2 . LEU A 1 491 ? -24.557 58.791 -6.192 1.00 115.88 ? 491 LEU A CD2 1 ATOM 3766 N N . ASN A 1 492 ? -27.010 56.245 -9.831 1.00 121.10 ? 492 ASN A N 1 ATOM 3767 C CA . ASN A 1 492 ? -27.806 55.379 -10.696 1.00 121.15 ? 492 ASN A CA 1 ATOM 3768 C C . ASN A 1 492 ? -28.259 54.098 -10.000 1.00 131.24 ? 492 ASN A C 1 ATOM 3769 O O . ASN A 1 492 ? -27.441 53.254 -9.636 1.00 131.71 ? 492 ASN A O 1 ATOM 3770 C CB . ASN A 1 492 ? -27.021 55.034 -11.962 1.00 115.50 ? 492 ASN A CB 1 ATOM 3771 C CG . ASN A 1 492 ? -26.822 56.233 -12.868 1.00 121.49 ? 492 ASN A CG 1 ATOM 3772 O OD1 . ASN A 1 492 ? -27.596 56.456 -13.800 1.00 117.84 ? 492 ASN A OD1 1 ATOM 3773 N ND2 . ASN A 1 492 ? -25.784 57.015 -12.597 1.00 131.35 ? 492 ASN A ND2 1 ATOM 3774 N N . PHE A 1 493 ? -29.571 53.960 -9.832 1.00 133.58 ? 493 PHE A N 1 ATOM 3775 C CA . PHE A 1 493 ? -30.156 52.794 -9.175 1.00 119.45 ? 493 PHE A CA 1 ATOM 3776 C C . PHE A 1 493 ? -30.826 51.857 -10.174 1.00 120.80 ? 493 PHE A C 1 ATOM 3777 O O . PHE A 1 493 ? -31.360 52.298 -11.192 1.00 120.99 ? 493 PHE A O 1 ATOM 3778 C CB . PHE A 1 493 ? -31.181 53.226 -8.124 1.00 110.67 ? 493 PHE A CB 1 ATOM 3779 C CG . PHE A 1 493 ? -30.579 53.858 -6.902 1.00 106.68 ? 493 PHE A CG 1 ATOM 3780 C CD1 . PHE A 1 493 ? -30.191 55.188 -6.910 1.00 118.41 ? 493 PHE A CD1 1 ATOM 3781 C CD2 . PHE A 1 493 ? -30.420 53.127 -5.736 1.00 103.58 ? 493 PHE A CD2 1 ATOM 3782 C CE1 . PHE A 1 493 ? -29.644 55.772 -5.783 1.00 124.06 ? 493 PHE A CE1 1 ATOM 3783 C CE2 . PHE A 1 493 ? -29.874 53.705 -4.606 1.00 100.98 ? 493 PHE A CE2 1 ATOM 3784 C CZ . PHE A 1 493 ? -29.485 55.029 -4.629 1.00 113.49 ? 493 PHE A CZ 1 ATOM 3785 N N . GLN A 1 494 ? -30.791 50.562 -9.877 1.00 120.84 ? 494 GLN A N 1 ATOM 3786 C CA . GLN A 1 494 ? -31.538 49.578 -10.653 1.00 125.31 ? 494 GLN A CA 1 ATOM 3787 C C . GLN A 1 494 ? -32.667 49.003 -9.804 1.00 120.41 ? 494 GLN A C 1 ATOM 3788 O O . GLN A 1 494 ? -32.423 48.271 -8.846 1.00 115.60 ? 494 GLN A O 1 ATOM 3789 C CB . GLN A 1 494 ? -30.618 48.460 -11.148 1.00 132.12 ? 494 GLN A CB 1 ATOM 3790 C CG . GLN A 1 494 ? -29.503 48.931 -12.067 1.00 142.01 ? 494 GLN A CG 1 ATOM 3791 C CD . GLN A 1 494 ? -30.016 49.414 -13.410 1.00 147.54 ? 494 GLN A CD 1 ATOM 3792 O OE1 . GLN A 1 494 ? -29.408 50.277 -14.044 1.00 148.21 ? 494 GLN A OE1 1 ATOM 3793 N NE2 . GLN A 1 494 ? -31.134 48.853 -13.855 1.00 146.01 ? 494 GLN A NE2 1 ATOM 3794 N N . VAL A 1 495 ? -33.903 49.339 -10.161 1.00 120.91 ? 495 VAL A N 1 ATOM 3795 C CA . VAL A 1 495 ? -35.063 48.936 -9.375 1.00 114.46 ? 495 VAL A CA 1 ATOM 3796 C C . VAL A 1 495 ? -35.727 47.687 -9.949 1.00 111.17 ? 495 VAL A C 1 ATOM 3797 O O . VAL A 1 495 ? -35.865 47.550 -11.164 1.00 116.18 ? 495 VAL A O 1 ATOM 3798 C CB . VAL A 1 495 ? -36.103 50.072 -9.294 1.00 107.42 ? 495 VAL A CB 1 ATOM 3799 C CG1 . VAL A 1 495 ? -37.205 49.723 -8.303 1.00 103.79 ? 495 VAL A CG1 1 ATOM 3800 C CG2 . VAL A 1 495 ? -35.429 51.376 -8.900 1.00 106.09 ? 495 VAL A CG2 1 ATOM 3801 N N . GLU A 1 496 ? -36.131 46.778 -9.067 1.00 105.20 ? 496 GLU A N 1 ATOM 3802 C CA . GLU A 1 496 ? -36.815 45.557 -9.475 1.00 105.93 ? 496 GLU A CA 1 ATOM 3803 C C . GLU A 1 496 ? -38.155 45.420 -8.756 1.00 107.75 ? 496 GLU A C 1 ATOM 3804 O O . GLU A 1 496 ? -38.216 45.464 -7.527 1.00 116.49 ? 496 GLU A O 1 ATOM 3805 C CB . GLU A 1 496 ? -35.940 44.333 -9.199 1.00 107.95 ? 496 GLU A CB 1 ATOM 3806 C CG . GLU A 1 496 ? -36.504 43.033 -9.744 1.00 121.31 ? 496 GLU A CG 1 ATOM 3807 C CD . GLU A 1 496 ? -36.521 42.998 -11.259 1.00 136.31 ? 496 GLU A CD 1 ATOM 3808 O OE1 . GLU A 1 496 ? -37.443 42.381 -11.833 1.00 144.39 ? 496 GLU A OE1 1 ATOM 3809 O OE2 . GLU A 1 496 ? -35.608 43.585 -11.877 1.00 136.69 ? 496 GLU A OE2 1 ATOM 3810 N N . LEU A 1 497 ? -39.226 45.254 -9.526 1.00 101.79 ? 497 LEU A N 1 ATOM 3811 C CA . LEU A 1 497 ? -40.566 45.129 -8.959 1.00 97.52 ? 497 LEU A CA 1 ATOM 3812 C C . LEU A 1 497 ? -41.121 43.718 -9.128 1.00 100.01 ? 497 LEU A C 1 ATOM 3813 O O . LEU A 1 497 ? -41.069 43.146 -10.216 1.00 102.60 ? 497 LEU A O 1 ATOM 3814 C CB . LEU A 1 497 ? -41.515 46.144 -9.600 1.00 96.82 ? 497 LEU A CB 1 ATOM 3815 C CG . LEU A 1 497 ? -41.276 47.614 -9.252 1.00 95.29 ? 497 LEU A CG 1 ATOM 3816 C CD1 . LEU A 1 497 ? -42.231 48.510 -10.025 1.00 96.42 ? 497 LEU A CD1 1 ATOM 3817 C CD2 . LEU A 1 497 ? -41.426 47.836 -7.757 1.00 93.24 ? 497 LEU A CD2 1 ATOM 3818 N N . LEU A 1 498 ? -41.651 43.163 -8.042 1.00 97.70 ? 498 LEU A N 1 ATOM 3819 C CA . LEU A 1 498 ? -42.243 41.830 -8.067 1.00 103.10 ? 498 LEU A CA 1 ATOM 3820 C C . LEU A 1 498 ? -43.672 41.864 -7.536 1.00 102.05 ? 498 LEU A C 1 ATOM 3821 O O . LEU A 1 498 ? -43.932 42.407 -6.462 1.00 106.21 ? 498 LEU A O 1 ATOM 3822 C CB . LEU A 1 498 ? -41.405 40.842 -7.248 1.00 114.34 ? 498 LEU A CB 1 ATOM 3823 C CG . LEU A 1 498 ? -40.029 40.420 -7.776 1.00 115.50 ? 498 LEU A CG 1 ATOM 3824 C CD1 . LEU A 1 498 ? -40.092 40.091 -9.260 1.00 107.57 ? 498 LEU A CD1 1 ATOM 3825 C CD2 . LEU A 1 498 ? -38.960 41.470 -7.491 1.00 115.67 ? 498 LEU A CD2 1 ATOM 3826 N N . LEU A 1 499 ? -44.596 41.281 -8.292 1.00 100.57 ? 499 LEU A N 1 ATOM 3827 C CA . LEU A 1 499 ? -46.001 41.262 -7.902 1.00 105.15 ? 499 LEU A CA 1 ATOM 3828 C C . LEU A 1 499 ? -46.382 39.943 -7.238 1.00 110.46 ? 499 LEU A C 1 ATOM 3829 O O . LEU A 1 499 ? -46.083 38.869 -7.761 1.00 102.94 ? 499 LEU A O 1 ATOM 3830 C CB . LEU A 1 499 ? -46.897 41.512 -9.117 1.00 102.85 ? 499 LEU A CB 1 ATOM 3831 C CG . LEU A 1 499 ? -46.810 42.899 -9.757 1.00 103.20 ? 499 LEU A CG 1 ATOM 3832 C CD1 . LEU A 1 499 ? -47.706 42.982 -10.983 1.00 106.45 ? 499 LEU A CD1 1 ATOM 3833 C CD2 . LEU A 1 499 ? -47.177 43.975 -8.747 1.00 102.97 ? 499 LEU A CD2 1 ATOM 3834 N N . ASP A 1 500 ? -47.047 40.042 -6.088 1.00 115.78 ? 500 ASP A N 1 ATOM 3835 C CA . ASP A 1 500 ? -47.536 38.877 -5.353 1.00 109.67 ? 500 ASP A CA 1 ATOM 3836 C C . ASP A 1 500 ? -46.410 37.901 -5.010 1.00 106.19 ? 500 ASP A C 1 ATOM 3837 O O . ASP A 1 500 ? -46.467 36.723 -5.364 1.00 102.86 ? 500 ASP A O 1 ATOM 3838 C CB . ASP A 1 500 ? -48.630 38.167 -6.154 1.00 103.08 ? 500 ASP A CB 1 ATOM 3839 C CG . ASP A 1 500 ? -49.606 37.421 -5.272 1.00 108.98 ? 500 ASP A CG 1 ATOM 3840 O OD1 . ASP A 1 500 ? -50.405 36.629 -5.813 1.00 104.88 ? 500 ASP A OD1 1 ATOM 3841 O OD2 . ASP A 1 500 ? -49.577 37.624 -4.040 1.00 115.33 ? 500 ASP A OD2 1 ATOM 3842 N N . LYS A 1 501 ? -45.385 38.410 -4.330 1.00 103.37 ? 501 LYS A N 1 ATOM 3843 C CA . LYS A 1 501 ? -44.196 37.631 -3.985 1.00 104.56 ? 501 LYS A CA 1 ATOM 3844 C C . LYS A 1 501 ? -44.512 36.357 -3.197 1.00 105.13 ? 501 LYS A C 1 ATOM 3845 O O . LYS A 1 501 ? -43.788 35.365 -3.302 1.00 118.96 ? 501 LYS A O 1 ATOM 3846 C CB . LYS A 1 501 ? -43.215 38.498 -3.189 1.00 107.38 ? 501 LYS A CB 1 ATOM 3847 C CG . LYS A 1 501 ? -41.911 37.797 -2.832 1.00 113.86 ? 501 LYS A CG 1 ATOM 3848 C CD . LYS A 1 501 ? -41.010 38.680 -1.988 1.00 116.23 ? 501 LYS A CD 1 ATOM 3849 C CE . LYS A 1 501 ? -39.780 37.919 -1.517 1.00 118.59 ? 501 LYS A CE 1 ATOM 3850 N NZ . LYS A 1 501 ? -38.980 37.388 -2.655 1.00 123.20 ? 501 LYS A NZ 1 ATOM 3851 N N . LEU A 1 502 ? -45.585 36.386 -2.411 1.00 98.43 ? 502 LEU A N 1 ATOM 3852 C CA . LEU A 1 502 ? -46.011 35.213 -1.650 1.00 99.82 ? 502 LEU A CA 1 ATOM 3853 C C . LEU A 1 502 ? -46.246 34.019 -2.572 1.00 111.48 ? 502 LEU A C 1 ATOM 3854 O O . LEU A 1 502 ? -45.879 32.888 -2.253 1.00 123.06 ? 502 LEU A O 1 ATOM 3855 C CB . LEU A 1 502 ? -47.279 35.519 -0.850 1.00 95.97 ? 502 LEU A CB 1 ATOM 3856 C CG . LEU A 1 502 ? -47.136 36.481 0.331 1.00 92.94 ? 502 LEU A CG 1 ATOM 3857 C CD1 . LEU A 1 502 ? -48.473 36.674 1.031 1.00 92.51 ? 502 LEU A CD1 1 ATOM 3858 C CD2 . LEU A 1 502 ? -46.087 35.974 1.307 1.00 91.47 ? 502 LEU A CD2 1 ATOM 3859 N N . LYS A 1 503 ? -46.860 34.292 -3.718 1.00 115.99 ? 503 LYS A N 1 ATOM 3860 C CA . LYS A 1 503 ? -47.080 33.292 -4.756 1.00 122.77 ? 503 LYS A CA 1 ATOM 3861 C C . LYS A 1 503 ? -45.846 33.138 -5.634 1.00 138.32 ? 503 LYS A C 1 ATOM 3862 O O . LYS A 1 503 ? -44.748 33.554 -5.256 1.00 128.55 ? 503 LYS A O 1 ATOM 3863 C CB . LYS A 1 503 ? -48.291 33.657 -5.615 1.00 116.49 ? 503 LYS A CB 1 ATOM 3864 C CG . LYS A 1 503 ? -49.604 33.696 -4.852 1.00 112.82 ? 503 LYS A CG 1 ATOM 3865 C CD . LYS A 1 503 ? -49.965 32.332 -4.289 1.00 121.98 ? 503 LYS A CD 1 ATOM 3866 C CE . LYS A 1 503 ? -51.318 32.367 -3.596 1.00 121.77 ? 503 LYS A CE 1 ATOM 3867 N NZ . LYS A 1 503 ? -51.685 31.044 -3.022 1.00 126.30 ? 503 LYS A NZ 1 ATOM 3868 N N . GLN A 1 504 ? -46.039 32.483 -6.779 1.00 155.44 ? 504 GLN A N 1 ATOM 3869 C CA . GLN A 1 504 ? -45.009 32.284 -7.803 1.00 157.66 ? 504 GLN A CA 1 ATOM 3870 C C . GLN A 1 504 ? -43.988 31.245 -7.386 1.00 152.01 ? 504 GLN A C 1 ATOM 3871 O O . GLN A 1 504 ? -43.109 30.874 -8.166 1.00 148.71 ? 504 GLN A O 1 ATOM 3872 C CB . GLN A 1 504 ? -44.300 33.593 -8.147 1.00 152.19 ? 504 GLN A CB 1 ATOM 3873 C CG . GLN A 1 504 ? -45.231 34.690 -8.596 1.00 145.56 ? 504 GLN A CG 1 ATOM 3874 C CD . GLN A 1 504 ? -44.491 35.853 -9.211 1.00 151.99 ? 504 GLN A CD 1 ATOM 3875 O OE1 . GLN A 1 504 ? -43.312 35.745 -9.547 1.00 158.46 ? 504 GLN A OE1 1 ATOM 3876 N NE2 . GLN A 1 504 ? -45.179 36.977 -9.362 1.00 153.54 ? 504 GLN A NE2 1 ATOM 3877 N N . LYS A 1 505 ? -44.111 30.776 -6.153 1.00 143.98 ? 505 LYS A N 1 ATOM 3878 C CA . LYS A 1 505 ? -43.314 29.661 -5.699 1.00 133.46 ? 505 LYS A CA 1 ATOM 3879 C C . LYS A 1 505 ? -44.150 28.402 -5.843 1.00 136.18 ? 505 LYS A C 1 ATOM 3880 O O . LYS A 1 505 ? -45.057 28.157 -5.044 1.00 140.50 ? 505 LYS A O 1 ATOM 3881 C CB . LYS A 1 505 ? -42.894 29.877 -4.252 1.00 122.32 ? 505 LYS A CB 1 ATOM 3882 C CG . LYS A 1 505 ? -41.892 30.997 -4.032 1.00 116.51 ? 505 LYS A CG 1 ATOM 3883 C CD . LYS A 1 505 ? -40.480 30.539 -4.370 1.00 122.20 ? 505 LYS A CD 1 ATOM 3884 C CE . LYS A 1 505 ? -39.431 31.549 -3.911 1.00 109.74 ? 505 LYS A CE 1 ATOM 3885 N NZ . LYS A 1 505 ? -38.033 31.126 -4.237 1.00 106.76 ? 505 LYS A NZ 1 ATOM 3886 N N . GLY A 1 506 ? -43.816 27.598 -6.848 1.00 135.47 ? 506 GLY A N 1 ATOM 3887 C CA . GLY A 1 506 ? -44.613 26.444 -7.222 1.00 134.89 ? 506 GLY A CA 1 ATOM 3888 C C . GLY A 1 506 ? -46.098 26.756 -7.304 1.00 136.17 ? 506 GLY A C 1 ATOM 3889 O O . GLY A 1 506 ? -46.923 25.914 -6.954 1.00 139.42 ? 506 GLY A O 1 ATOM 3890 N N . ALA A 1 507 ? -46.441 27.954 -7.772 1.00 138.63 ? 507 ALA A N 1 ATOM 3891 C CA . ALA A 1 507 ? -47.810 28.451 -7.657 1.00 141.85 ? 507 ALA A CA 1 ATOM 3892 C C . ALA A 1 507 ? -48.196 29.415 -8.776 1.00 140.69 ? 507 ALA A C 1 ATOM 3893 O O . ALA A 1 507 ? -47.341 29.921 -9.504 1.00 148.98 ? 507 ALA A O 1 ATOM 3894 C CB . ALA A 1 507 ? -48.005 29.120 -6.304 1.00 134.16 ? 507 ALA A CB 1 ATOM 3895 N N . ILE A 1 508 ? -49.497 29.657 -8.901 1.00 126.29 ? 508 ILE A N 1 ATOM 3896 C CA . ILE A 1 508 ? -50.046 30.536 -9.930 1.00 129.49 ? 508 ILE A CA 1 ATOM 3897 C C . ILE A 1 508 ? -49.663 32.003 -9.702 1.00 138.32 ? 508 ILE A C 1 ATOM 3898 O O . ILE A 1 508 ? -49.593 32.469 -8.564 1.00 138.64 ? 508 ILE A O 1 ATOM 3899 C CB . ILE A 1 508 ? -51.591 30.401 -9.994 1.00 144.13 ? 508 ILE A CB 1 ATOM 3900 C CG1 . ILE A 1 508 ? -52.185 31.298 -11.084 1.00 136.33 ? 508 ILE A CG1 1 ATOM 3901 C CG2 . ILE A 1 508 ? -52.219 30.700 -8.638 1.00 142.24 ? 508 ILE A CG2 1 ATOM 3902 C CD1 . ILE A 1 508 ? -51.696 30.974 -12.478 1.00 134.89 ? 508 ILE A CD1 1 ATOM 3903 N N . ARG A 1 509 ? -49.405 32.717 -10.795 1.00 144.84 ? 509 ARG A N 1 ATOM 3904 C CA . ARG A 1 509 ? -49.100 34.144 -10.747 1.00 138.47 ? 509 ARG A CA 1 ATOM 3905 C C . ARG A 1 509 ? -50.396 34.939 -10.879 1.00 125.77 ? 509 ARG A C 1 ATOM 3906 O O . ARG A 1 509 ? -51.067 34.878 -11.909 1.00 131.11 ? 509 ARG A O 1 ATOM 3907 C CB . ARG A 1 509 ? -48.115 34.535 -11.855 1.00 147.22 ? 509 ARG A CB 1 ATOM 3908 C CG . ARG A 1 509 ? -46.719 33.927 -11.720 1.00 155.13 ? 509 ARG A CG 1 ATOM 3909 C CD . ARG A 1 509 ? -46.659 32.492 -12.229 1.00 163.55 ? 509 ARG A CD 1 ATOM 3910 N NE . ARG A 1 509 ? -45.418 31.824 -11.846 1.00 164.41 ? 509 ARG A NE 1 ATOM 3911 C CZ . ARG A 1 509 ? -45.170 30.535 -12.055 1.00 159.73 ? 509 ARG A CZ 1 ATOM 3912 N NH1 . ARG A 1 509 ? -46.079 29.770 -12.645 1.00 156.01 ? 509 ARG A NH1 1 ATOM 3913 N NH2 . ARG A 1 509 ? -44.014 30.009 -11.674 1.00 156.10 ? 509 ARG A NH2 1 ATOM 3914 N N . ARG A 1 510 ? -50.745 35.681 -9.834 1.00 116.89 ? 510 ARG A N 1 ATOM 3915 C CA . ARG A 1 510 ? -52.077 36.269 -9.728 1.00 111.41 ? 510 ARG A CA 1 ATOM 3916 C C . ARG A 1 510 ? -52.200 37.724 -10.188 1.00 108.20 ? 510 ARG A C 1 ATOM 3917 O O . ARG A 1 510 ? -53.300 38.275 -10.198 1.00 107.50 ? 510 ARG A O 1 ATOM 3918 C CB . ARG A 1 510 ? -52.558 36.156 -8.281 1.00 108.69 ? 510 ARG A CB 1 ATOM 3919 C CG . ARG A 1 510 ? -52.759 34.723 -7.819 1.00 111.30 ? 510 ARG A CG 1 ATOM 3920 C CD . ARG A 1 510 ? -52.798 34.634 -6.308 1.00 118.23 ? 510 ARG A CD 1 ATOM 3921 N NE . ARG A 1 510 ? -53.628 35.680 -5.721 1.00 123.06 ? 510 ARG A NE 1 ATOM 3922 C CZ . ARG A 1 510 ? -53.534 36.082 -4.459 1.00 128.72 ? 510 ARG A CZ 1 ATOM 3923 N NH1 . ARG A 1 510 ? -52.641 35.526 -3.652 1.00 128.76 ? 510 ARG A NH1 1 ATOM 3924 N NH2 . ARG A 1 510 ? -54.328 37.041 -4.004 1.00 132.60 ? 510 ARG A NH2 1 ATOM 3925 N N . ALA A 1 511 ? -51.090 38.347 -10.571 1.00 105.04 ? 511 ALA A N 1 ATOM 3926 C CA . ALA A 1 511 ? -51.137 39.735 -11.027 1.00 101.38 ? 511 ALA A CA 1 ATOM 3927 C C . ALA A 1 511 ? -50.061 40.040 -12.065 1.00 99.40 ? 511 ALA A C 1 ATOM 3928 O O . ALA A 1 511 ? -48.937 39.550 -11.968 1.00 100.13 ? 511 ALA A O 1 ATOM 3929 C CB . ALA A 1 511 ? -51.008 40.683 -9.845 1.00 89.12 ? 511 ALA A CB 1 ATOM 3930 N N . LEU A 1 512 ? -50.412 40.865 -13.047 1.00 98.63 ? 512 LEU A N 1 ATOM 3931 C CA . LEU A 1 512 ? -49.496 41.223 -14.126 1.00 111.34 ? 512 LEU A CA 1 ATOM 3932 C C . LEU A 1 512 ? -49.519 42.724 -14.402 1.00 104.82 ? 512 LEU A C 1 ATOM 3933 O O . LEU A 1 512 ? -50.509 43.399 -14.121 1.00 100.09 ? 512 LEU A O 1 ATOM 3934 C CB . LEU A 1 512 ? -49.851 40.462 -15.407 1.00 118.98 ? 512 LEU A CB 1 ATOM 3935 C CG . LEU A 1 512 ? -50.005 38.941 -15.330 1.00 113.02 ? 512 LEU A CG 1 ATOM 3936 C CD1 . LEU A 1 512 ? -50.453 38.380 -16.669 1.00 107.74 ? 512 LEU A CD1 1 ATOM 3937 C CD2 . LEU A 1 512 ? -48.708 38.291 -14.891 1.00 118.05 ? 512 LEU A CD2 1 ATOM 3938 N N . PHE A 1 513 ? -48.426 43.243 -14.955 1.00 103.60 ? 513 PHE A N 1 ATOM 3939 C CA . PHE A 1 513 ? -48.387 44.635 -15.391 1.00 106.62 ? 513 PHE A CA 1 ATOM 3940 C C . PHE A 1 513 ? -49.149 44.779 -16.704 1.00 118.49 ? 513 PHE A C 1 ATOM 3941 O O . PHE A 1 513 ? -49.207 43.841 -17.498 1.00 121.20 ? 513 PHE A O 1 ATOM 3942 C CB . PHE A 1 513 ? -46.944 45.122 -15.545 1.00 106.37 ? 513 PHE A CB 1 ATOM 3943 C CG . PHE A 1 513 ? -46.216 45.285 -14.238 1.00 113.74 ? 513 PHE A CG 1 ATOM 3944 C CD1 . PHE A 1 513 ? -45.287 44.346 -13.823 1.00 117.15 ? 513 PHE A CD1 1 ATOM 3945 C CD2 . PHE A 1 513 ? -46.464 46.378 -13.425 1.00 110.07 ? 513 PHE A CD2 1 ATOM 3946 C CE1 . PHE A 1 513 ? -44.619 44.493 -12.622 1.00 102.56 ? 513 PHE A CE1 1 ATOM 3947 C CE2 . PHE A 1 513 ? -45.799 46.531 -12.222 1.00 101.89 ? 513 PHE A CE2 1 ATOM 3948 C CZ . PHE A 1 513 ? -44.875 45.587 -11.821 1.00 100.94 ? 513 PHE A CZ 1 ATOM 3949 N N . LEU A 1 514 ? -49.731 45.954 -16.928 1.00 128.97 ? 514 LEU A N 1 ATOM 3950 C CA . LEU A 1 514 ? -50.611 46.166 -18.075 1.00 128.57 ? 514 LEU A CA 1 ATOM 3951 C C . LEU A 1 514 ? -49.878 46.053 -19.408 1.00 120.10 ? 514 LEU A C 1 ATOM 3952 O O . LEU A 1 514 ? -50.262 45.264 -20.271 1.00 118.91 ? 514 LEU A O 1 ATOM 3953 C CB . LEU A 1 514 ? -51.296 47.532 -17.971 1.00 126.76 ? 514 LEU A CB 1 ATOM 3954 C CG . LEU A 1 514 ? -52.416 47.830 -18.969 1.00 127.06 ? 514 LEU A CG 1 ATOM 3955 C CD1 . LEU A 1 514 ? -53.610 48.444 -18.256 1.00 118.84 ? 514 LEU A CD1 1 ATOM 3956 C CD2 . LEU A 1 514 ? -51.924 48.751 -20.074 1.00 138.27 ? 514 LEU A CD2 1 ATOM 3957 N N . TYR A 1 515 ? -48.822 46.841 -19.570 1.00 121.75 ? 515 TYR A N 1 ATOM 3958 C CA . TYR A 1 515 ? -48.080 46.866 -20.824 1.00 126.75 ? 515 TYR A CA 1 ATOM 3959 C C . TYR A 1 515 ? -47.130 45.679 -20.948 1.00 127.02 ? 515 TYR A C 1 ATOM 3960 O O . TYR A 1 515 ? -46.978 45.105 -22.026 1.00 128.22 ? 515 TYR A O 1 ATOM 3961 C CB . TYR A 1 515 ? -47.302 48.177 -20.951 1.00 134.57 ? 515 TYR A CB 1 ATOM 3962 C CG . TYR A 1 515 ? -48.178 49.407 -20.899 1.00 142.55 ? 515 TYR A CG 1 ATOM 3963 C CD1 . TYR A 1 515 ? -48.401 50.076 -19.701 1.00 146.49 ? 515 TYR A CD1 1 ATOM 3964 C CD2 . TYR A 1 515 ? -48.788 49.898 -22.046 1.00 145.70 ? 515 TYR A CD2 1 ATOM 3965 C CE1 . TYR A 1 515 ? -49.203 51.200 -19.649 1.00 153.81 ? 515 TYR A CE1 1 ATOM 3966 C CE2 . TYR A 1 515 ? -49.592 51.021 -22.004 1.00 151.65 ? 515 TYR A CE2 1 ATOM 3967 C CZ . TYR A 1 515 ? -49.796 51.668 -20.803 1.00 159.22 ? 515 TYR A CZ 1 ATOM 3968 O OH . TYR A 1 515 ? -50.596 52.787 -20.757 1.00 165.92 ? 515 TYR A OH 1 ATOM 3969 N N . SER A 1 516 ? -46.499 45.312 -19.838 1.00 137.49 ? 516 SER A N 1 ATOM 3970 C CA . SER A 1 516 ? -45.486 44.262 -19.843 1.00 137.10 ? 516 SER A CA 1 ATOM 3971 C C . SER A 1 516 ? -46.085 42.860 -19.906 1.00 125.73 ? 516 SER A C 1 ATOM 3972 O O . SER A 1 516 ? -45.438 41.931 -20.393 1.00 124.26 ? 516 SER A O 1 ATOM 3973 C CB . SER A 1 516 ? -44.594 44.384 -18.604 1.00 134.37 ? 516 SER A CB 1 ATOM 3974 O OG . SER A 1 516 ? -43.917 45.628 -18.582 1.00 130.35 ? 516 SER A OG 1 ATOM 3975 N N . ARG A 1 517 ? -47.313 42.715 -19.410 1.00 123.28 ? 517 ARG A N 1 ATOM 3976 C CA . ARG A 1 517 ? -47.970 41.412 -19.289 1.00 126.55 ? 517 ARG A CA 1 ATOM 3977 C C . ARG A 1 517 ? -47.120 40.445 -18.469 1.00 128.51 ? 517 ARG A C 1 ATOM 3978 O O . ARG A 1 517 ? -47.154 39.234 -18.687 1.00 131.49 ? 517 ARG A O 1 ATOM 3979 C CB . ARG A 1 517 ? -48.262 40.810 -20.667 1.00 125.17 ? 517 ARG A CB 1 ATOM 3980 C CG . ARG A 1 517 ? -49.305 41.554 -21.482 1.00 128.25 ? 517 ARG A CG 1 ATOM 3981 C CD . ARG A 1 517 ? -49.473 40.910 -22.850 1.00 139.86 ? 517 ARG A CD 1 ATOM 3982 N NE . ARG A 1 517 ? -50.541 41.526 -23.631 1.00 138.93 ? 517 ARG A NE 1 ATOM 3983 C CZ . ARG A 1 517 ? -51.787 41.066 -23.685 1.00 120.11 ? 517 ARG A CZ 1 ATOM 3984 N NH1 . ARG A 1 517 ? -52.127 39.982 -23.001 1.00 116.18 ? 517 ARG A NH1 1 ATOM 3985 N NH2 . ARG A 1 517 ? -52.694 41.689 -24.424 1.00 117.13 ? 517 ARG A NH2 1 ATOM 3986 N N . SER A 1 518 ? -46.362 40.990 -17.524 1.00 124.58 ? 518 SER A N 1 ATOM 3987 C CA . SER A 1 518 ? -45.418 40.204 -16.740 1.00 117.88 ? 518 SER A CA 1 ATOM 3988 C C . SER A 1 518 ? -45.578 40.484 -15.250 1.00 108.82 ? 518 SER A C 1 ATOM 3989 O O . SER A 1 518 ? -45.984 41.578 -14.864 1.00 106.44 ? 518 SER A O 1 ATOM 3990 C CB . SER A 1 518 ? -43.984 40.505 -17.189 1.00 115.85 ? 518 SER A CB 1 ATOM 3991 O OG . SER A 1 518 ? -43.035 39.765 -16.440 1.00 112.36 ? 518 SER A OG 1 ATOM 3992 N N . PRO A 1 519 ? -45.276 39.486 -14.406 1.00 108.44 ? 519 PRO A N 1 ATOM 3993 C CA . PRO A 1 519 ? -45.292 39.690 -12.954 1.00 109.74 ? 519 PRO A CA 1 ATOM 3994 C C . PRO A 1 519 ? -44.169 40.612 -12.483 1.00 119.57 ? 519 PRO A C 1 ATOM 3995 O O . PRO A 1 519 ? -44.256 41.178 -11.394 1.00 122.35 ? 519 PRO A O 1 ATOM 3996 C CB . PRO A 1 519 ? -45.097 38.275 -12.395 1.00 111.07 ? 519 PRO A CB 1 ATOM 3997 C CG . PRO A 1 519 ? -45.474 37.358 -13.509 1.00 114.33 ? 519 PRO A CG 1 ATOM 3998 C CD . PRO A 1 519 ? -45.075 38.071 -14.759 1.00 113.71 ? 519 PRO A CD 1 ATOM 3999 N N . SER A 1 520 ? -43.129 40.755 -13.299 1.00 124.44 ? 520 SER A N 1 ATOM 4000 C CA . SER A 1 520 ? -41.960 41.539 -12.917 1.00 117.57 ? 520 SER A CA 1 ATOM 4001 C C . SER A 1 520 ? -41.647 42.654 -13.911 1.00 112.95 ? 520 SER A C 1 ATOM 4002 O O . SER A 1 520 ? -41.883 42.517 -15.112 1.00 119.18 ? 520 SER A O 1 ATOM 4003 C CB . SER A 1 520 ? -40.740 40.629 -12.768 1.00 122.63 ? 520 SER A CB 1 ATOM 4004 O OG . SER A 1 520 ? -40.427 39.989 -13.993 1.00 133.63 ? 520 SER A OG 1 ATOM 4005 N N . HIS A 1 521 ? -41.112 43.757 -13.397 1.00 113.18 ? 521 HIS A N 1 ATOM 4006 C CA . HIS A 1 521 ? -40.691 44.877 -14.230 1.00 123.72 ? 521 HIS A CA 1 ATOM 4007 C C . HIS A 1 521 ? -39.500 45.589 -13.596 1.00 119.09 ? 521 HIS A C 1 ATOM 4008 O O . HIS A 1 521 ? -39.410 45.694 -12.373 1.00 115.13 ? 521 HIS A O 1 ATOM 4009 C CB . HIS A 1 521 ? -41.846 45.858 -14.443 1.00 129.83 ? 521 HIS A CB 1 ATOM 4010 C CG . HIS A 1 521 ? -41.540 46.947 -15.424 1.00 127.46 ? 521 HIS A CG 1 ATOM 4011 N ND1 . HIS A 1 521 ? -40.853 48.091 -15.077 1.00 121.99 ? 521 HIS A ND1 1 ATOM 4012 C CD2 . HIS A 1 521 ? -41.831 47.068 -16.741 1.00 129.84 ? 521 HIS A CD2 1 ATOM 4013 C CE1 . HIS A 1 521 ? -40.732 48.868 -16.139 1.00 128.37 ? 521 HIS A CE1 1 ATOM 4014 N NE2 . HIS A 1 521 ? -41.317 48.270 -17.161 1.00 136.14 ? 521 HIS A NE2 1 ATOM 4015 N N . SER A 1 522 ? -38.588 46.075 -14.432 1.00 119.07 ? 522 SER A N 1 ATOM 4016 C CA . SER A 1 522 ? -37.401 46.769 -13.945 1.00 120.10 ? 522 SER A CA 1 ATOM 4017 C C . SER A 1 522 ? -37.155 48.063 -14.713 1.00 134.55 ? 522 SER A C 1 ATOM 4018 O O . SER A 1 522 ? -37.489 48.169 -15.893 1.00 155.26 ? 522 SER A O 1 ATOM 4019 C CB . SER A 1 522 ? -36.174 45.862 -14.044 1.00 118.50 ? 522 SER A CB 1 ATOM 4020 O OG . SER A 1 522 ? -35.957 45.441 -15.379 1.00 123.94 ? 522 SER A OG 1 ATOM 4021 N N . LYS A 1 523 ? -36.570 49.047 -14.036 1.00 127.31 ? 523 LYS A N 1 ATOM 4022 C CA . LYS A 1 523 ? -36.286 50.336 -14.655 1.00 131.76 ? 523 LYS A CA 1 ATOM 4023 C C . LYS A 1 523 ? -35.040 50.981 -14.053 1.00 133.29 ? 523 LYS A C 1 ATOM 4024 O O . LYS A 1 523 ? -34.778 50.849 -12.857 1.00 126.87 ? 523 LYS A O 1 ATOM 4025 C CB . LYS A 1 523 ? -37.488 51.272 -14.509 1.00 135.51 ? 523 LYS A CB 1 ATOM 4026 C CG . LYS A 1 523 ? -37.368 52.574 -15.284 1.00 138.74 ? 523 LYS A CG 1 ATOM 4027 C CD . LYS A 1 523 ? -37.203 52.316 -16.773 1.00 137.62 ? 523 LYS A CD 1 ATOM 4028 C CE . LYS A 1 523 ? -37.120 53.617 -17.553 1.00 137.88 ? 523 LYS A CE 1 ATOM 4029 N NZ . LYS A 1 523 ? -38.347 54.444 -17.382 1.00 133.44 ? 523 LYS A NZ 1 ATOM 4030 N N . ASN A 1 524 ? -34.276 51.675 -14.890 1.00 148.42 ? 524 ASN A N 1 ATOM 4031 C CA . ASN A 1 524 ? -33.093 52.397 -14.437 1.00 152.34 ? 524 ASN A CA 1 ATOM 4032 C C . ASN A 1 524 ? -33.456 53.799 -13.953 1.00 142.12 ? 524 ASN A C 1 ATOM 4033 O O . ASN A 1 524 ? -34.161 54.537 -14.641 1.00 145.97 ? 524 ASN A O 1 ATOM 4034 C CB . ASN A 1 524 ? -32.055 52.470 -15.559 1.00 163.86 ? 524 ASN A CB 1 ATOM 4035 C CG . ASN A 1 524 ? -31.608 51.097 -16.029 1.00 178.56 ? 524 ASN A CG 1 ATOM 4036 O OD1 . ASN A 1 524 ? -32.202 50.083 -15.665 1.00 166.29 ? 524 ASN A OD1 1 ATOM 4037 N ND2 . ASN A 1 524 ? -30.559 51.059 -16.844 1.00 209.28 ? 524 ASN A ND2 1 ATOM 4038 N N . MET A 1 525 ? -32.973 54.161 -12.768 1.00 129.13 ? 525 MET A N 1 ATOM 4039 C CA . MET A 1 525 ? -33.326 55.440 -12.157 1.00 127.72 ? 525 MET A CA 1 ATOM 4040 C C . MET A 1 525 ? -32.110 56.292 -11.811 1.00 136.54 ? 525 MET A C 1 ATOM 4041 O O . MET A 1 525 ? -30.992 55.788 -11.709 1.00 143.53 ? 525 MET A O 1 ATOM 4042 C CB . MET A 1 525 ? -34.158 55.210 -10.894 1.00 123.85 ? 525 MET A CB 1 ATOM 4043 C CG . MET A 1 525 ? -35.652 55.384 -11.089 1.00 124.31 ? 525 MET A CG 1 ATOM 4044 S SD . MET A 1 525 ? -36.551 55.288 -9.530 1.00 114.16 ? 525 MET A SD 1 ATOM 4045 C CE . MET A 1 525 ? -38.165 55.875 -10.036 1.00 179.60 ? 525 MET A CE 1 ATOM 4046 N N . THR A 1 526 ? -32.341 57.591 -11.637 1.00 135.62 ? 526 THR A N 1 ATOM 4047 C CA . THR A 1 526 ? -31.288 58.512 -11.226 1.00 127.45 ? 526 THR A CA 1 ATOM 4048 C C . THR A 1 526 ? -31.798 59.548 -10.222 1.00 121.76 ? 526 THR A C 1 ATOM 4049 O O . THR A 1 526 ? -32.780 60.241 -10.482 1.00 125.02 ? 526 THR A O 1 ATOM 4050 C CB . THR A 1 526 ? -30.681 59.240 -12.440 1.00 123.31 ? 526 THR A CB 1 ATOM 4051 O OG1 . THR A 1 526 ? -30.117 58.279 -13.342 1.00 118.64 ? 526 THR A OG1 1 ATOM 4052 C CG2 . THR A 1 526 ? -29.595 60.207 -11.997 1.00 125.32 ? 526 THR A CG2 1 ATOM 4053 N N . ILE A 1 527 ? -31.123 59.651 -9.080 1.00 112.70 ? 527 ILE A N 1 ATOM 4054 C CA . ILE A 1 527 ? -31.462 60.649 -8.068 1.00 118.46 ? 527 ILE A CA 1 ATOM 4055 C C . ILE A 1 527 ? -30.272 61.592 -7.895 1.00 122.56 ? 527 ILE A C 1 ATOM 4056 O O . ILE A 1 527 ? -29.237 61.393 -8.526 1.00 132.57 ? 527 ILE A O 1 ATOM 4057 C CB . ILE A 1 527 ? -31.823 59.992 -6.714 1.00 116.95 ? 527 ILE A CB 1 ATOM 4058 C CG1 . ILE A 1 527 ? -32.441 58.609 -6.931 1.00 110.48 ? 527 ILE A CG1 1 ATOM 4059 C CG2 . ILE A 1 527 ? -32.773 60.875 -5.912 1.00 125.26 ? 527 ILE A CG2 1 ATOM 4060 C CD1 . ILE A 1 527 ? -33.839 58.645 -7.517 1.00 118.11 ? 527 ILE A CD1 1 ATOM 4061 N N . SER A 1 528 ? -30.409 62.616 -7.056 1.00 116.16 ? 528 SER A N 1 ATOM 4062 C CA . SER A 1 528 ? -29.289 63.514 -6.784 1.00 127.62 ? 528 SER A CA 1 ATOM 4063 C C . SER A 1 528 ? -29.073 63.766 -5.290 1.00 122.71 ? 528 SER A C 1 ATOM 4064 O O . SER A 1 528 ? -28.077 63.326 -4.716 1.00 109.44 ? 528 SER A O 1 ATOM 4065 C CB . SER A 1 528 ? -29.487 64.848 -7.507 1.00 143.99 ? 528 SER A CB 1 ATOM 4066 O OG . SER A 1 528 ? -30.404 65.674 -6.814 1.00 153.08 ? 528 SER A OG 1 ATOM 4067 N N . ARG A 1 529 ? -30.012 64.476 -4.670 1.00 126.34 ? 529 ARG A N 1 ATOM 4068 C CA . ARG A 1 529 ? -29.875 64.889 -3.275 1.00 125.45 ? 529 ARG A CA 1 ATOM 4069 C C . ARG A 1 529 ? -31.052 64.386 -2.437 1.00 142.50 ? 529 ARG A C 1 ATOM 4070 O O . ARG A 1 529 ? -31.909 63.658 -2.935 1.00 152.06 ? 529 ARG A O 1 ATOM 4071 C CB . ARG A 1 529 ? -29.763 66.416 -3.185 1.00 124.51 ? 529 ARG A CB 1 ATOM 4072 C CG . ARG A 1 529 ? -28.915 66.922 -2.024 1.00 135.38 ? 529 ARG A CG 1 ATOM 4073 C CD . ARG A 1 529 ? -28.869 68.443 -1.979 1.00 140.53 ? 529 ARG A CD 1 ATOM 4074 N NE . ARG A 1 529 ? -28.181 69.011 -3.135 1.00 137.25 ? 529 ARG A NE 1 ATOM 4075 C CZ . ARG A 1 529 ? -27.943 70.308 -3.300 1.00 136.91 ? 529 ARG A CZ 1 ATOM 4076 N NH1 . ARG A 1 529 ? -28.337 71.179 -2.380 1.00 141.85 ? 529 ARG A NH1 1 ATOM 4077 N NH2 . ARG A 1 529 ? -27.310 70.736 -4.383 1.00 134.52 ? 529 ARG A NH2 1 ATOM 4078 N N . GLY A 1 530 ? -31.082 64.764 -1.162 1.00 146.83 ? 530 GLY A N 1 ATOM 4079 C CA . GLY A 1 530 ? -32.150 64.354 -0.265 1.00 144.57 ? 530 GLY A CA 1 ATOM 4080 C C . GLY A 1 530 ? -33.416 65.173 -0.437 1.00 138.80 ? 530 GLY A C 1 ATOM 4081 O O . GLY A 1 530 ? -33.359 66.354 -0.777 1.00 131.74 ? 530 GLY A O 1 ATOM 4082 N N . GLY A 1 531 ? -34.563 64.541 -0.201 1.00 139.77 ? 531 GLY A N 1 ATOM 4083 C CA . GLY A 1 531 ? -35.851 65.195 -0.367 1.00 150.44 ? 531 GLY A CA 1 ATOM 4084 C C . GLY A 1 531 ? -36.203 65.378 -1.831 1.00 160.15 ? 531 GLY A C 1 ATOM 4085 O O . GLY A 1 531 ? -37.179 66.043 -2.178 1.00 162.43 ? 531 GLY A O 1 ATOM 4086 N N . LEU A 1 532 ? -35.394 64.770 -2.690 1.00 163.51 ? 532 LEU A N 1 ATOM 4087 C CA . LEU A 1 532 ? -35.512 64.905 -4.136 1.00 162.57 ? 532 LEU A CA 1 ATOM 4088 C C . LEU A 1 532 ? -36.352 63.789 -4.753 1.00 157.24 ? 532 LEU A C 1 ATOM 4089 O O . LEU A 1 532 ? -36.385 63.653 -5.976 1.00 152.22 ? 532 LEU A O 1 ATOM 4090 C CB . LEU A 1 532 ? -34.127 64.935 -4.785 1.00 159.06 ? 532 LEU A CB 1 ATOM 4091 C CG . LEU A 1 532 ? -34.030 65.644 -6.140 1.00 160.83 ? 532 LEU A CG 1 ATOM 4092 C CD1 . LEU A 1 532 ? -33.267 66.955 -6.017 1.00 162.96 ? 532 LEU A CD1 1 ATOM 4093 C CD2 . LEU A 1 532 ? -33.404 64.734 -7.188 1.00 160.27 ? 532 LEU A CD2 1 ATOM 4094 N N . MET A 1 533 ? -37.020 62.998 -3.911 1.00 148.11 ? 533 MET A N 1 ATOM 4095 C CA . MET A 1 533 ? -37.507 61.672 -4.299 1.00 131.19 ? 533 MET A CA 1 ATOM 4096 C C . MET A 1 533 ? -38.221 61.658 -5.643 1.00 126.96 ? 533 MET A C 1 ATOM 4097 O O . MET A 1 533 ? -39.139 62.439 -5.892 1.00 140.51 ? 533 MET A O 1 ATOM 4098 C CB . MET A 1 533 ? -38.465 61.117 -3.240 1.00 130.56 ? 533 MET A CB 1 ATOM 4099 C CG . MET A 1 533 ? -37.967 61.196 -1.814 1.00 134.71 ? 533 MET A CG 1 ATOM 4100 S SD . MET A 1 533 ? -38.761 59.977 -0.746 1.00 169.79 ? 533 MET A SD 1 ATOM 4101 C CE . MET A 1 533 ? -40.488 60.392 -0.971 1.00 95.36 ? 533 MET A CE 1 ATOM 4102 N N . GLN A 1 534 ? -37.776 60.747 -6.501 1.00 121.53 ? 534 GLN A N 1 ATOM 4103 C CA . GLN A 1 534 ? -38.275 60.641 -7.861 1.00 126.03 ? 534 GLN A CA 1 ATOM 4104 C C . GLN A 1 534 ? -39.076 59.363 -8.026 1.00 131.69 ? 534 GLN A C 1 ATOM 4105 O O . GLN A 1 534 ? -38.571 58.267 -7.780 1.00 137.40 ? 534 GLN A O 1 ATOM 4106 C CB . GLN A 1 534 ? -37.116 60.677 -8.859 1.00 121.09 ? 534 GLN A CB 1 ATOM 4107 C CG . GLN A 1 534 ? -37.486 60.235 -10.262 1.00 125.34 ? 534 GLN A CG 1 ATOM 4108 C CD . GLN A 1 534 ? -36.312 60.306 -11.216 1.00 131.59 ? 534 GLN A CD 1 ATOM 4109 O OE1 . GLN A 1 534 ? -35.373 61.074 -11.004 1.00 131.71 ? 534 GLN A OE1 1 ATOM 4110 N NE2 . GLN A 1 534 ? -36.355 59.501 -12.271 1.00 132.24 ? 534 GLN A NE2 1 ATOM 4111 N N . CYS A 1 535 ? -40.330 59.505 -8.436 1.00 125.99 ? 535 CYS A N 1 ATOM 4112 C CA . CYS A 1 535 ? -41.208 58.354 -8.567 1.00 121.60 ? 535 CYS A CA 1 ATOM 4113 C C . CYS A 1 535 ? -41.419 57.949 -10.020 1.00 119.97 ? 535 CYS A C 1 ATOM 4114 O O . CYS A 1 535 ? -40.927 58.600 -10.941 1.00 125.26 ? 535 CYS A O 1 ATOM 4115 C CB . CYS A 1 535 ? -42.557 58.645 -7.909 1.00 126.15 ? 535 CYS A CB 1 ATOM 4116 S SG . CYS A 1 535 ? -42.443 59.158 -6.179 1.00 174.74 ? 535 CYS A SG 1 ATOM 4117 N N . GLU A 1 536 ? -42.161 56.864 -10.205 1.00 119.88 ? 536 GLU A N 1 ATOM 4118 C CA . GLU A 1 536 ? -42.581 56.412 -11.524 1.00 130.23 ? 536 GLU A CA 1 ATOM 4119 C C . GLU A 1 536 ? -43.948 55.757 -11.408 1.00 127.74 ? 536 GLU A C 1 ATOM 4120 O O . GLU A 1 536 ? -44.248 55.099 -10.410 1.00 115.26 ? 536 GLU A O 1 ATOM 4121 C CB . GLU A 1 536 ? -41.570 55.439 -12.133 1.00 133.42 ? 536 GLU A CB 1 ATOM 4122 C CG . GLU A 1 536 ? -40.430 56.114 -12.879 1.00 134.92 ? 536 GLU A CG 1 ATOM 4123 C CD . GLU A 1 536 ? -39.670 55.156 -13.775 1.00 144.48 ? 536 GLU A CD 1 ATOM 4124 O OE1 . GLU A 1 536 ? -40.088 53.984 -13.886 1.00 160.22 ? 536 GLU A OE1 1 ATOM 4125 O OE2 . GLU A 1 536 ? -38.656 55.576 -14.371 1.00 138.79 ? 536 GLU A OE2 1 ATOM 4126 N N . GLU A 1 537 ? -44.778 55.940 -12.427 1.00 133.57 ? 537 GLU A N 1 ATOM 4127 C CA . GLU A 1 537 ? -46.141 55.436 -12.382 1.00 128.55 ? 537 GLU A CA 1 ATOM 4128 C C . GLU A 1 537 ? -46.329 54.252 -13.323 1.00 124.93 ? 537 GLU A C 1 ATOM 4129 O O . GLU A 1 537 ? -46.299 54.404 -14.544 1.00 141.23 ? 537 GLU A O 1 ATOM 4130 C CB . GLU A 1 537 ? -47.130 56.550 -12.730 1.00 134.67 ? 537 GLU A CB 1 ATOM 4131 C CG . GLU A 1 537 ? -48.538 56.316 -12.211 1.00 139.19 ? 537 GLU A CG 1 ATOM 4132 C CD . GLU A 1 537 ? -48.621 56.381 -10.697 1.00 135.29 ? 537 GLU A CD 1 ATOM 4133 O OE1 . GLU A 1 537 ? -47.715 56.971 -10.070 1.00 123.13 ? 537 GLU A OE1 1 ATOM 4134 O OE2 . GLU A 1 537 ? -49.594 55.841 -10.132 1.00 138.10 ? 537 GLU A OE2 1 ATOM 4135 N N . LEU A 1 538 ? -46.518 53.073 -12.743 1.00 114.80 ? 538 LEU A N 1 ATOM 4136 C CA . LEU A 1 538 ? -46.791 51.871 -13.520 1.00 117.50 ? 538 LEU A CA 1 ATOM 4137 C C . LEU A 1 538 ? -48.203 51.373 -13.246 1.00 125.94 ? 538 LEU A C 1 ATOM 4138 O O . LEU A 1 538 ? -48.726 51.539 -12.144 1.00 129.20 ? 538 LEU A O 1 ATOM 4139 C CB . LEU A 1 538 ? -45.775 50.770 -13.204 1.00 110.10 ? 538 LEU A CB 1 ATOM 4140 C CG . LEU A 1 538 ? -44.478 50.744 -14.017 1.00 112.21 ? 538 LEU A CG 1 ATOM 4141 C CD1 . LEU A 1 538 ? -43.604 51.954 -13.714 1.00 121.41 ? 538 LEU A CD1 1 ATOM 4142 C CD2 . LEU A 1 538 ? -43.717 49.450 -13.766 1.00 109.52 ? 538 LEU A CD2 1 ATOM 4143 N N . ILE A 1 539 ? -48.818 50.766 -14.253 1.00 117.58 ? 539 ILE A N 1 ATOM 4144 C CA . ILE A 1 539 ? -50.160 50.224 -14.104 1.00 106.49 ? 539 ILE A CA 1 ATOM 4145 C C . ILE A 1 539 ? -50.136 48.706 -14.233 1.00 102.44 ? 539 ILE A C 1 ATOM 4146 O O . ILE A 1 539 ? -49.771 48.168 -15.277 1.00 109.52 ? 539 ILE A O 1 ATOM 4147 C CB . ILE A 1 539 ? -51.140 50.810 -15.143 1.00 116.76 ? 539 ILE A CB 1 ATOM 4148 C CG1 . ILE A 1 539 ? -51.257 52.329 -14.988 1.00 123.16 ? 539 ILE A CG1 1 ATOM 4149 C CG2 . ILE A 1 539 ? -52.509 50.161 -15.006 1.00 116.21 ? 539 ILE A CG2 1 ATOM 4150 C CD1 . ILE A 1 539 ? -50.279 53.123 -15.835 1.00 127.10 ? 539 ILE A CD1 1 ATOM 4151 N N . ALA A 1 540 ? -50.513 48.022 -13.159 1.00 99.76 ? 540 ALA A N 1 ATOM 4152 C CA . ALA A 1 540 ? -50.595 46.568 -13.167 1.00 99.74 ? 540 ALA A CA 1 ATOM 4153 C C . ALA A 1 540 ? -52.040 46.134 -12.987 1.00 99.07 ? 540 ALA A C 1 ATOM 4154 O O . ALA A 1 540 ? -52.709 46.562 -12.047 1.00 105.58 ? 540 ALA A O 1 ATOM 4155 C CB . ALA A 1 540 ? -49.719 45.975 -12.078 1.00 101.37 ? 540 ALA A CB 1 ATOM 4156 N N . TYR A 1 541 ? -52.526 45.287 -13.887 1.00 99.14 ? 541 TYR A N 1 ATOM 4157 C CA . TYR A 1 541 ? -53.913 44.849 -13.817 1.00 97.78 ? 541 TYR A CA 1 ATOM 4158 C C . TYR A 1 541 ? -54.056 43.555 -13.030 1.00 94.82 ? 541 TYR A C 1 ATOM 4159 O O . TYR A 1 541 ? -53.072 42.980 -12.564 1.00 94.12 ? 541 TYR A O 1 ATOM 4160 C CB . TYR A 1 541 ? -54.499 44.676 -15.222 1.00 106.59 ? 541 TYR A CB 1 ATOM 4161 C CG . TYR A 1 541 ? -53.874 43.565 -16.038 1.00 113.97 ? 541 TYR A CG 1 ATOM 4162 C CD1 . TYR A 1 541 ? -52.733 43.794 -16.791 1.00 119.19 ? 541 TYR A CD1 1 ATOM 4163 C CD2 . TYR A 1 541 ? -54.434 42.293 -16.068 1.00 112.09 ? 541 TYR A CD2 1 ATOM 4164 C CE1 . TYR A 1 541 ? -52.159 42.789 -17.545 1.00 115.67 ? 541 TYR A CE1 1 ATOM 4165 C CE2 . TYR A 1 541 ? -53.865 41.280 -16.819 1.00 110.17 ? 541 TYR A CE2 1 ATOM 4166 C CZ . TYR A 1 541 ? -52.727 41.535 -17.555 1.00 110.53 ? 541 TYR A CZ 1 ATOM 4167 O OH . TYR A 1 541 ? -52.154 40.536 -18.307 1.00 109.75 ? 541 TYR A OH 1 ATOM 4168 N N . LEU A 1 542 ? -55.298 43.106 -12.888 1.00 94.63 ? 542 LEU A N 1 ATOM 4169 C CA . LEU A 1 542 ? -55.598 41.861 -12.198 1.00 91.98 ? 542 LEU A CA 1 ATOM 4170 C C . LEU A 1 542 ? -56.240 40.893 -13.181 1.00 93.41 ? 542 LEU A C 1 ATOM 4171 O O . LEU A 1 542 ? -57.213 41.239 -13.848 1.00 89.25 ? 542 LEU A O 1 ATOM 4172 C CB . LEU A 1 542 ? -56.521 42.116 -11.005 1.00 89.17 ? 542 LEU A CB 1 ATOM 4173 C CG . LEU A 1 542 ? -56.674 40.990 -9.984 1.00 88.17 ? 542 LEU A CG 1 ATOM 4174 C CD1 . LEU A 1 542 ? -55.332 40.668 -9.350 1.00 87.84 ? 542 LEU A CD1 1 ATOM 4175 C CD2 . LEU A 1 542 ? -57.693 41.370 -8.921 1.00 86.95 ? 542 LEU A CD2 1 ATOM 4176 N N . ARG A 1 543 ? -55.699 39.682 -13.269 1.00 94.90 ? 543 ARG A N 1 ATOM 4177 C CA . ARG A 1 543 ? -56.173 38.714 -14.253 1.00 100.19 ? 543 ARG A CA 1 ATOM 4178 C C . ARG A 1 543 ? -57.621 38.319 -13.982 1.00 113.12 ? 543 ARG A C 1 ATOM 4179 O O . ARG A 1 543 ? -58.115 38.468 -12.864 1.00 113.49 ? 543 ARG A O 1 ATOM 4180 C CB . ARG A 1 543 ? -55.279 37.472 -14.268 1.00 101.08 ? 543 ARG A CB 1 ATOM 4181 C CG . ARG A 1 543 ? -55.273 36.680 -12.974 1.00 116.49 ? 543 ARG A CG 1 ATOM 4182 C CD . ARG A 1 543 ? -54.501 35.373 -13.123 1.00 123.65 ? 543 ARG A CD 1 ATOM 4183 N NE . ARG A 1 543 ? -53.087 35.587 -13.421 1.00 119.00 ? 543 ARG A NE 1 ATOM 4184 C CZ . ARG A 1 543 ? -52.550 35.482 -14.634 1.00 110.82 ? 543 ARG A CZ 1 ATOM 4185 N NH1 . ARG A 1 543 ? -53.309 35.165 -15.674 1.00 107.92 ? 543 ARG A NH1 1 ATOM 4186 N NH2 . ARG A 1 543 ? -51.252 35.694 -14.806 1.00 108.66 ? 543 ARG A NH2 1 ATOM 4187 N N . ASP A 1 544 ? -58.292 37.827 -15.020 1.00 121.69 ? 544 ASP A N 1 ATOM 4188 C CA . ASP A 1 544 ? -59.719 37.529 -14.963 1.00 110.52 ? 544 ASP A CA 1 ATOM 4189 C C . ASP A 1 544 ? -60.063 36.558 -13.837 1.00 107.56 ? 544 ASP A C 1 ATOM 4190 O O . ASP A 1 544 ? -59.264 35.689 -13.485 1.00 106.51 ? 544 ASP A O 1 ATOM 4191 C CB . ASP A 1 544 ? -60.195 36.965 -16.304 1.00 112.64 ? 544 ASP A CB 1 ATOM 4192 C CG . ASP A 1 544 ? -61.703 36.836 -16.381 1.00 129.70 ? 544 ASP A CG 1 ATOM 4193 O OD1 . ASP A 1 544 ? -62.363 37.809 -16.804 1.00 140.28 ? 544 ASP A OD1 1 ATOM 4194 O OD2 . ASP A 1 544 ? -62.229 35.762 -16.020 1.00 134.13 ? 544 ASP A OD2 1 ATOM 4195 N N . GLU A 1 545 ? -61.256 36.730 -13.276 1.00 108.82 ? 545 GLU A N 1 ATOM 4196 C CA . GLU A 1 545 ? -61.725 35.949 -12.135 1.00 112.23 ? 545 GLU A CA 1 ATOM 4197 C C . GLU A 1 545 ? -61.650 34.443 -12.371 1.00 110.96 ? 545 GLU A C 1 ATOM 4198 O O . GLU A 1 545 ? -61.428 33.670 -11.439 1.00 109.38 ? 545 GLU A O 1 ATOM 4199 C CB . GLU A 1 545 ? -63.166 36.341 -11.800 1.00 128.76 ? 545 GLU A CB 1 ATOM 4200 C CG . GLU A 1 545 ? -63.439 37.834 -11.897 1.00 137.17 ? 545 GLU A CG 1 ATOM 4201 C CD . GLU A 1 545 ? -64.921 38.155 -11.922 1.00 131.45 ? 545 GLU A CD 1 ATOM 4202 O OE1 . GLU A 1 545 ? -65.277 39.307 -12.248 1.00 116.01 ? 545 GLU A OE1 1 ATOM 4203 O OE2 . GLU A 1 545 ? -65.731 37.254 -11.619 1.00 133.77 ? 545 GLU A OE2 1 ATOM 4204 N N . SER A 1 546 ? -61.834 34.034 -13.622 1.00 117.42 ? 546 SER A N 1 ATOM 4205 C CA . SER A 1 546 ? -61.890 32.619 -13.968 1.00 127.03 ? 546 SER A CA 1 ATOM 4206 C C . SER A 1 546 ? -60.517 32.037 -14.294 1.00 118.17 ? 546 SER A C 1 ATOM 4207 O O . SER A 1 546 ? -60.375 30.826 -14.458 1.00 114.73 ? 546 SER A O 1 ATOM 4208 C CB . SER A 1 546 ? -62.835 32.405 -15.151 1.00 138.09 ? 546 SER A CB 1 ATOM 4209 O OG . SER A 1 546 ? -64.117 32.944 -14.882 1.00 141.74 ? 546 SER A OG 1 ATOM 4210 N N . GLU A 1 547 ? -59.508 32.897 -14.385 1.00 115.00 ? 547 GLU A N 1 ATOM 4211 C CA . GLU A 1 547 ? -58.162 32.451 -14.733 1.00 116.83 ? 547 GLU A CA 1 ATOM 4212 C C . GLU A 1 547 ? -57.477 31.737 -13.573 1.00 112.64 ? 547 GLU A C 1 ATOM 4213 O O . GLU A 1 547 ? -56.436 31.106 -13.753 1.00 111.31 ? 547 GLU A O 1 ATOM 4214 C CB . GLU A 1 547 ? -57.302 33.631 -15.190 1.00 119.61 ? 547 GLU A CB 1 ATOM 4215 C CG . GLU A 1 547 ? -57.754 34.267 -16.492 1.00 125.67 ? 547 GLU A CG 1 ATOM 4216 C CD . GLU A 1 547 ? -56.774 35.306 -17.000 1.00 128.89 ? 547 GLU A CD 1 ATOM 4217 O OE1 . GLU A 1 547 ? -55.586 35.239 -16.621 1.00 125.41 ? 547 GLU A OE1 1 ATOM 4218 O OE2 . GLU A 1 547 ? -57.192 36.190 -17.778 1.00 134.25 ? 547 GLU A OE2 1 ATOM 4219 N N . PHE A 1 548 ? -58.062 31.841 -12.384 1.00 113.95 ? 548 PHE A N 1 ATOM 4220 C CA . PHE A 1 548 ? -57.475 31.227 -11.197 1.00 116.56 ? 548 PHE A CA 1 ATOM 4221 C C . PHE A 1 548 ? -58.489 31.027 -10.070 1.00 126.32 ? 548 PHE A C 1 ATOM 4222 O O . PHE A 1 548 ? -59.669 31.346 -10.210 1.00 127.77 ? 548 PHE A O 1 ATOM 4223 C CB . PHE A 1 548 ? -56.273 32.050 -10.694 1.00 108.27 ? 548 PHE A CB 1 ATOM 4224 C CG . PHE A 1 548 ? -56.620 33.424 -10.158 1.00 112.99 ? 548 PHE A CG 1 ATOM 4225 C CD1 . PHE A 1 548 ? -55.904 33.953 -9.096 1.00 111.62 ? 548 PHE A CD1 1 ATOM 4226 C CD2 . PHE A 1 548 ? -57.623 34.199 -10.724 1.00 117.12 ? 548 PHE A CD2 1 ATOM 4227 C CE1 . PHE A 1 548 ? -56.191 35.212 -8.599 1.00 99.11 ? 548 PHE A CE1 1 ATOM 4228 C CE2 . PHE A 1 548 ? -57.915 35.457 -10.229 1.00 108.24 ? 548 PHE A CE2 1 ATOM 4229 C CZ . PHE A 1 548 ? -57.200 35.962 -9.164 1.00 98.69 ? 548 PHE A CZ 1 ATOM 4230 N N . ARG A 1 549 ? -58.001 30.498 -8.953 1.00 129.59 ? 549 ARG A N 1 ATOM 4231 C CA . ARG A 1 549 ? -58.834 30.110 -7.819 1.00 131.08 ? 549 ARG A CA 1 ATOM 4232 C C . ARG A 1 549 ? -59.014 31.291 -6.868 1.00 135.17 ? 549 ARG A C 1 ATOM 4233 O O . ARG A 1 549 ? -59.580 31.157 -5.782 1.00 131.04 ? 549 ARG A O 1 ATOM 4234 C CB . ARG A 1 549 ? -58.203 28.917 -7.093 1.00 131.61 ? 549 ARG A CB 1 ATOM 4235 C CG . ARG A 1 549 ? -59.140 28.127 -6.192 1.00 133.21 ? 549 ARG A CG 1 ATOM 4236 C CD . ARG A 1 549 ? -58.405 26.961 -5.549 1.00 142.28 ? 549 ARG A CD 1 ATOM 4237 N NE . ARG A 1 549 ? -57.189 27.395 -4.866 1.00 155.32 ? 549 ARG A NE 1 ATOM 4238 C CZ . ARG A 1 549 ? -56.313 26.571 -4.299 1.00 156.91 ? 549 ARG A CZ 1 ATOM 4239 N NH1 . ARG A 1 549 ? -56.514 25.261 -4.331 1.00 165.41 ? 549 ARG A NH1 1 ATOM 4240 N NH2 . ARG A 1 549 ? -55.234 27.058 -3.701 1.00 138.42 ? 549 ARG A NH2 1 ATOM 4241 N N . ASP A 1 550 ? -58.517 32.445 -7.304 1.00 149.15 ? 550 ASP A N 1 ATOM 4242 C CA . ASP A 1 550 ? -58.389 33.643 -6.481 1.00 147.39 ? 550 ASP A CA 1 ATOM 4243 C C . ASP A 1 550 ? -57.578 33.325 -5.235 1.00 122.67 ? 550 ASP A C 1 ATOM 4244 O O . ASP A 1 550 ? -56.670 32.498 -5.293 1.00 113.81 ? 550 ASP A O 1 ATOM 4245 C CB . ASP A 1 550 ? -59.763 34.199 -6.094 1.00 154.99 ? 550 ASP A CB 1 ATOM 4246 C CG . ASP A 1 550 ? -60.702 34.313 -7.279 1.00 156.97 ? 550 ASP A CG 1 ATOM 4247 O OD1 . ASP A 1 550 ? -60.221 34.592 -8.396 1.00 161.24 ? 550 ASP A OD1 1 ATOM 4248 O OD2 . ASP A 1 550 ? -61.922 34.122 -7.093 1.00 153.21 ? 550 ASP A OD2 1 ATOM 4249 N N . LYS A 1 551 ? -57.956 33.942 -4.115 1.00 109.89 ? 551 LYS A N 1 ATOM 4250 C CA . LYS A 1 551 ? -57.308 33.755 -2.814 1.00 110.12 ? 551 LYS A CA 1 ATOM 4251 C C . LYS A 1 551 ? -57.888 34.706 -1.774 1.00 106.48 ? 551 LYS A C 1 ATOM 4252 O O . LYS A 1 551 ? -58.560 35.680 -2.113 1.00 98.67 ? 551 LYS A O 1 ATOM 4253 C CB . LYS A 1 551 ? -55.792 33.987 -2.888 1.00 115.19 ? 551 LYS A CB 1 ATOM 4254 C CG . LYS A 1 551 ? -54.944 32.721 -2.891 1.00 115.22 ? 551 LYS A CG 1 ATOM 4255 C CD . LYS A 1 551 ? -55.596 31.611 -2.087 1.00 124.96 ? 551 LYS A CD 1 ATOM 4256 C CE . LYS A 1 551 ? -55.465 30.280 -2.806 1.00 131.62 ? 551 LYS A CE 1 ATOM 4257 N NZ . LYS A 1 551 ? -56.071 30.329 -4.166 1.00 128.96 ? 551 LYS A NZ 1 ATOM 4258 N N . LEU A 1 552 ? -57.626 34.411 -0.506 1.00 106.35 ? 552 LEU A N 1 ATOM 4259 C CA . LEU A 1 552 ? -57.713 35.418 0.542 1.00 90.97 ? 552 LEU A CA 1 ATOM 4260 C C . LEU A 1 552 ? -56.311 35.955 0.784 1.00 87.08 ? 552 LEU A C 1 ATOM 4261 O O . LEU A 1 552 ? -56.101 36.861 1.591 1.00 85.77 ? 552 LEU A O 1 ATOM 4262 C CB . LEU A 1 552 ? -58.306 34.844 1.829 1.00 90.47 ? 552 LEU A CB 1 ATOM 4263 C CG . LEU A 1 552 ? -59.831 34.866 1.933 1.00 106.75 ? 552 LEU A CG 1 ATOM 4264 C CD1 . LEU A 1 552 ? -60.282 34.350 3.291 1.00 115.31 ? 552 LEU A CD1 1 ATOM 4265 C CD2 . LEU A 1 552 ? -60.359 36.271 1.687 1.00 109.31 ? 552 LEU A CD2 1 ATOM 4266 N N . THR A 1 553 ? -55.354 35.378 0.064 1.00 84.89 ? 553 THR A N 1 ATOM 4267 C CA . THR A 1 553 ? -53.950 35.742 0.186 1.00 83.12 ? 553 THR A CA 1 ATOM 4268 C C . THR A 1 553 ? -53.680 37.097 -0.455 1.00 80.75 ? 553 THR A C 1 ATOM 4269 O O . THR A 1 553 ? -53.939 37.288 -1.643 1.00 81.69 ? 553 THR A O 1 ATOM 4270 C CB . THR A 1 553 ? -53.038 34.685 -0.464 1.00 88.69 ? 553 THR A CB 1 ATOM 4271 O OG1 . THR A 1 553 ? -53.419 33.378 -0.015 1.00 96.75 ? 553 THR A OG1 1 ATOM 4272 C CG2 . THR A 1 553 ? -51.581 34.940 -0.111 1.00 86.93 ? 553 THR A CG2 1 ATOM 4273 N N . PRO A 1 554 ? -53.160 38.045 0.337 1.00 79.99 ? 554 PRO A N 1 ATOM 4274 C CA . PRO A 1 554 ? -52.852 39.394 -0.148 1.00 77.96 ? 554 PRO A CA 1 ATOM 4275 C C . PRO A 1 554 ? -51.820 39.384 -1.268 1.00 82.01 ? 554 PRO A C 1 ATOM 4276 O O . PRO A 1 554 ? -51.000 38.469 -1.346 1.00 77.79 ? 554 PRO A O 1 ATOM 4277 C CB . PRO A 1 554 ? -52.294 40.097 1.095 1.00 77.52 ? 554 PRO A CB 1 ATOM 4278 C CG . PRO A 1 554 ? -52.821 39.313 2.247 1.00 80.28 ? 554 PRO A CG 1 ATOM 4279 C CD . PRO A 1 554 ? -52.876 37.898 1.773 1.00 80.79 ? 554 PRO A CD 1 ATOM 4280 N N . ILE A 1 555 ? -51.870 40.394 -2.129 1.00 82.90 ? 555 ILE A N 1 ATOM 4281 C CA . ILE A 1 555 ? -50.882 40.539 -3.187 1.00 84.16 ? 555 ILE A CA 1 ATOM 4282 C C . ILE A 1 555 ? -49.768 41.464 -2.717 1.00 83.71 ? 555 ILE A C 1 ATOM 4283 O O . ILE A 1 555 ? -49.981 42.661 -2.528 1.00 86.01 ? 555 ILE A O 1 ATOM 4284 C CB . ILE A 1 555 ? -51.511 41.091 -4.479 1.00 84.84 ? 555 ILE A CB 1 ATOM 4285 C CG1 . ILE A 1 555 ? -52.641 40.174 -4.951 1.00 80.23 ? 555 ILE A CG1 1 ATOM 4286 C CG2 . ILE A 1 555 ? -50.457 41.249 -5.563 1.00 85.80 ? 555 ILE A CG2 1 ATOM 4287 C CD1 . ILE A 1 555 ? -53.341 40.659 -6.199 1.00 81.28 ? 555 ILE A CD1 1 ATOM 4288 N N . THR A 1 556 ? -48.578 40.904 -2.531 1.00 84.15 ? 556 THR A N 1 ATOM 4289 C CA . THR A 1 556 ? -47.451 41.666 -2.009 1.00 85.60 ? 556 THR A CA 1 ATOM 4290 C C . THR A 1 556 ? -46.604 42.247 -3.134 1.00 92.65 ? 556 THR A C 1 ATOM 4291 O O . THR A 1 556 ? -45.984 41.511 -3.901 1.00 95.53 ? 556 THR A O 1 ATOM 4292 C CB . THR A 1 556 ? -46.554 40.800 -1.102 1.00 90.95 ? 556 THR A CB 1 ATOM 4293 O OG1 . THR A 1 556 ? -45.998 39.722 -1.865 1.00 114.12 ? 556 THR A OG1 1 ATOM 4294 C CG2 . THR A 1 556 ? -47.355 40.231 0.056 1.00 84.62 ? 556 THR A CG2 1 ATOM 4295 N N . ILE A 1 557 ? -46.583 43.572 -3.229 1.00 91.83 ? 557 ILE A N 1 ATOM 4296 C CA . ILE A 1 557 ? -45.749 44.251 -4.213 1.00 93.31 ? 557 ILE A CA 1 ATOM 4297 C C . ILE A 1 557 ? -44.351 44.444 -3.637 1.00 77.82 ? 557 ILE A C 1 ATOM 4298 O O . ILE A 1 557 ? -44.179 45.082 -2.599 1.00 76.90 ? 557 ILE A O 1 ATOM 4299 C CB . ILE A 1 557 ? -46.335 45.614 -4.633 1.00 96.04 ? 557 ILE A CB 1 ATOM 4300 C CG1 . ILE A 1 557 ? -47.680 45.431 -5.343 1.00 80.10 ? 557 ILE A CG1 1 ATOM 4301 C CG2 . ILE A 1 557 ? -45.367 46.347 -5.545 1.00 98.18 ? 557 ILE A CG2 1 ATOM 4302 C CD1 . ILE A 1 557 ? -48.884 45.438 -4.422 1.00 79.48 ? 557 ILE A CD1 1 ATOM 4303 N N . PHE A 1 558 ? -43.356 43.887 -4.318 1.00 87.66 ? 558 PHE A N 1 ATOM 4304 C CA . PHE A 1 558 ? -41.996 43.835 -3.794 1.00 86.71 ? 558 PHE A CA 1 ATOM 4305 C C . PHE A 1 558 ? -41.030 44.695 -4.605 1.00 102.91 ? 558 PHE A C 1 ATOM 4306 O O . PHE A 1 558 ? -40.738 44.388 -5.760 1.00 121.99 ? 558 PHE A O 1 ATOM 4307 C CB . PHE A 1 558 ? -41.513 42.382 -3.766 1.00 87.60 ? 558 PHE A CB 1 ATOM 4308 C CG . PHE A 1 558 ? -40.158 42.197 -3.146 1.00 84.89 ? 558 PHE A CG 1 ATOM 4309 C CD1 . PHE A 1 558 ? -40.019 42.104 -1.772 1.00 83.88 ? 558 PHE A CD1 1 ATOM 4310 C CD2 . PHE A 1 558 ? -39.027 42.096 -3.938 1.00 86.60 ? 558 PHE A CD2 1 ATOM 4311 C CE1 . PHE A 1 558 ? -38.775 41.925 -1.198 1.00 87.62 ? 558 PHE A CE1 1 ATOM 4312 C CE2 . PHE A 1 558 ? -37.780 41.918 -3.370 1.00 92.47 ? 558 PHE A CE2 1 ATOM 4313 C CZ . PHE A 1 558 ? -37.654 41.832 -1.999 1.00 96.51 ? 558 PHE A CZ 1 ATOM 4314 N N . MET A 1 559 ? -40.536 45.769 -3.997 1.00 99.74 ? 559 MET A N 1 ATOM 4315 C CA . MET A 1 559 ? -39.553 46.629 -4.650 1.00 95.88 ? 559 MET A CA 1 ATOM 4316 C C . MET A 1 559 ? -38.150 46.375 -4.119 1.00 97.19 ? 559 MET A C 1 ATOM 4317 O O . MET A 1 559 ? -37.936 46.345 -2.912 1.00 94.94 ? 559 MET A O 1 ATOM 4318 C CB . MET A 1 559 ? -39.905 48.107 -4.466 1.00 95.29 ? 559 MET A CB 1 ATOM 4319 C CG . MET A 1 559 ? -38.800 49.044 -4.940 1.00 95.86 ? 559 MET A CG 1 ATOM 4320 S SD . MET A 1 559 ? -39.226 50.794 -4.905 1.00 98.77 ? 559 MET A SD 1 ATOM 4321 C CE . MET A 1 559 ? -39.505 51.053 -3.158 1.00 92.13 ? 559 MET A CE 1 ATOM 4322 N N . GLU A 1 560 ? -37.197 46.202 -5.030 1.00 106.28 ? 560 GLU A N 1 ATOM 4323 C CA . GLU A 1 560 ? -35.802 46.002 -4.659 1.00 105.89 ? 560 GLU A CA 1 ATOM 4324 C C . GLU A 1 560 ? -34.897 46.887 -5.514 1.00 107.38 ? 560 GLU A C 1 ATOM 4325 O O . GLU A 1 560 ? -35.090 46.993 -6.725 1.00 114.67 ? 560 GLU A O 1 ATOM 4326 C CB . GLU A 1 560 ? -35.416 44.529 -4.813 1.00 110.71 ? 560 GLU A CB 1 ATOM 4327 C CG . GLU A 1 560 ? -34.065 44.164 -4.223 1.00 128.20 ? 560 GLU A CG 1 ATOM 4328 C CD . GLU A 1 560 ? -33.780 42.677 -4.308 1.00 139.01 ? 560 GLU A CD 1 ATOM 4329 O OE1 . GLU A 1 560 ? -34.398 42.001 -5.158 1.00 135.39 ? 560 GLU A OE1 1 ATOM 4330 O OE2 . GLU A 1 560 ? -32.946 42.182 -3.522 1.00 145.41 ? 560 GLU A OE2 1 ATOM 4331 N N . TYR A 1 561 ? -33.915 47.525 -4.883 1.00 105.76 ? 561 TYR A N 1 ATOM 4332 C CA . TYR A 1 561 ? -33.007 48.418 -5.599 1.00 109.11 ? 561 TYR A CA 1 ATOM 4333 C C . TYR A 1 561 ? -31.558 47.943 -5.510 1.00 114.21 ? 561 TYR A C 1 ATOM 4334 O O . TYR A 1 561 ? -31.193 47.189 -4.609 1.00 115.81 ? 561 TYR A O 1 ATOM 4335 C CB . TYR A 1 561 ? -33.134 49.852 -5.073 1.00 107.65 ? 561 TYR A CB 1 ATOM 4336 C CG . TYR A 1 561 ? -33.328 49.966 -3.578 1.00 109.81 ? 561 TYR A CG 1 ATOM 4337 C CD1 . TYR A 1 561 ? -32.241 50.106 -2.725 1.00 114.24 ? 561 TYR A CD1 1 ATOM 4338 C CD2 . TYR A 1 561 ? -34.600 49.951 -3.019 1.00 111.38 ? 561 TYR A CD2 1 ATOM 4339 C CE1 . TYR A 1 561 ? -32.414 50.217 -1.358 1.00 119.67 ? 561 TYR A CE1 1 ATOM 4340 C CE2 . TYR A 1 561 ? -34.783 50.059 -1.655 1.00 114.39 ? 561 TYR A CE2 1 ATOM 4341 C CZ . TYR A 1 561 ? -33.688 50.193 -0.829 1.00 122.37 ? 561 TYR A CZ 1 ATOM 4342 O OH . TYR A 1 561 ? -33.868 50.302 0.530 1.00 129.67 ? 561 TYR A OH 1 ATOM 4343 N N . ARG A 1 562 ? -30.738 48.399 -6.453 1.00 118.43 ? 562 ARG A N 1 ATOM 4344 C CA . ARG A 1 562 ? -29.396 47.856 -6.649 1.00 123.13 ? 562 ARG A CA 1 ATOM 4345 C C . ARG A 1 562 ? -28.294 48.893 -6.435 1.00 128.97 ? 562 ARG A C 1 ATOM 4346 O O . ARG A 1 562 ? -27.430 48.713 -5.575 1.00 136.44 ? 562 ARG A O 1 ATOM 4347 C CB . ARG A 1 562 ? -29.271 47.253 -8.049 1.00 128.34 ? 562 ARG A CB 1 ATOM 4348 C CG . ARG A 1 562 ? -28.071 46.339 -8.225 1.00 128.17 ? 562 ARG A CG 1 ATOM 4349 C CD . ARG A 1 562 ? -28.141 45.158 -7.269 1.00 133.11 ? 562 ARG A CD 1 ATOM 4350 N NE . ARG A 1 562 ? -29.378 44.399 -7.429 1.00 141.42 ? 562 ARG A NE 1 ATOM 4351 C CZ . ARG A 1 562 ? -29.706 43.339 -6.697 1.00 140.76 ? 562 ARG A CZ 1 ATOM 4352 N NH1 . ARG A 1 562 ? -28.887 42.907 -5.748 1.00 141.25 ? 562 ARG A NH1 1 ATOM 4353 N NH2 . ARG A 1 562 ? -30.854 42.711 -6.913 1.00 136.20 ? 562 ARG A NH2 1 ATOM 4354 N N . LEU A 1 563 ? -28.323 49.957 -7.238 1.00 128.31 ? 563 LEU A N 1 ATOM 4355 C CA . LEU A 1 563 ? -27.281 50.989 -7.244 1.00 132.43 ? 563 LEU A CA 1 ATOM 4356 C C . LEU A 1 563 ? -25.916 50.424 -7.644 1.00 134.38 ? 563 LEU A C 1 ATOM 4357 O O . LEU A 1 563 ? -25.026 50.258 -6.808 1.00 125.26 ? 563 LEU A O 1 ATOM 4358 C CB . LEU A 1 563 ? -27.191 51.683 -5.877 1.00 134.05 ? 563 LEU A CB 1 ATOM 4359 C CG . LEU A 1 563 ? -26.234 52.870 -5.709 1.00 135.35 ? 563 LEU A CG 1 ATOM 4360 C CD1 . LEU A 1 563 ? -26.614 54.024 -6.622 1.00 141.68 ? 563 LEU A CD1 1 ATOM 4361 C CD2 . LEU A 1 563 ? -26.185 53.323 -4.257 1.00 130.52 ? 563 LEU A CD2 1 ATOM 4362 N N . ASP A 1 564 ? -25.778 50.096 -8.927 1.00 141.75 ? 564 ASP A N 1 ATOM 4363 C CA . ASP A 1 564 ? -24.488 49.716 -9.494 1.00 134.50 ? 564 ASP A CA 1 ATOM 4364 C C . ASP A 1 564 ? -23.487 50.847 -9.286 1.00 132.42 ? 564 ASP A C 1 ATOM 4365 O O . ASP A 1 564 ? -23.853 52.021 -9.338 1.00 128.19 ? 564 ASP A O 1 ATOM 4366 C CB . ASP A 1 564 ? -24.623 49.388 -10.981 1.00 130.36 ? 564 ASP A CB 1 ATOM 4367 C CG . ASP A 1 564 ? -25.634 48.290 -11.246 1.00 140.40 ? 564 ASP A CG 1 ATOM 4368 O OD1 . ASP A 1 564 ? -25.804 47.414 -10.373 1.00 147.23 ? 564 ASP A OD1 1 ATOM 4369 O OD2 . ASP A 1 564 ? -26.259 48.304 -12.327 1.00 142.75 ? 564 ASP A OD2 1 ATOM 4370 N N . TYR A 1 565 ? -22.225 50.499 -9.056 1.00 132.95 ? 565 TYR A N 1 ATOM 4371 C CA . TYR A 1 565 ? -21.249 51.496 -8.633 1.00 122.41 ? 565 TYR A CA 1 ATOM 4372 C C . TYR A 1 565 ? -20.304 51.959 -9.740 1.00 118.45 ? 565 TYR A C 1 ATOM 4373 O O . TYR A 1 565 ? -19.415 51.223 -10.169 1.00 117.66 ? 565 TYR A O 1 ATOM 4374 C CB . TYR A 1 565 ? -20.428 50.950 -7.463 1.00 122.73 ? 565 TYR A CB 1 ATOM 4375 C CG . TYR A 1 565 ? -21.259 50.320 -6.369 1.00 122.86 ? 565 TYR A CG 1 ATOM 4376 C CD1 . TYR A 1 565 ? -22.012 51.104 -5.504 1.00 126.77 ? 565 TYR A CD1 1 ATOM 4377 C CD2 . TYR A 1 565 ? -21.285 48.943 -6.195 1.00 118.34 ? 565 TYR A CD2 1 ATOM 4378 C CE1 . TYR A 1 565 ? -22.773 50.532 -4.502 1.00 126.24 ? 565 TYR A CE1 1 ATOM 4379 C CE2 . TYR A 1 565 ? -22.042 48.362 -5.194 1.00 117.87 ? 565 TYR A CE2 1 ATOM 4380 C CZ . TYR A 1 565 ? -22.783 49.162 -4.350 1.00 118.74 ? 565 TYR A CZ 1 ATOM 4381 O OH . TYR A 1 565 ? -23.538 48.590 -3.352 1.00 112.22 ? 565 TYR A OH 1 ATOM 4382 N N . ARG A 1 566 ? -20.509 53.193 -10.188 1.00 118.66 ? 566 ARG A N 1 ATOM 4383 C CA . ARG A 1 566 ? -19.550 53.903 -11.027 1.00 124.96 ? 566 ARG A CA 1 ATOM 4384 C C . ARG A 1 566 ? -19.440 55.319 -10.479 1.00 129.26 ? 566 ARG A C 1 ATOM 4385 O O . ARG A 1 566 ? -20.406 56.079 -10.531 1.00 123.71 ? 566 ARG A O 1 ATOM 4386 C CB . ARG A 1 566 ? -19.986 53.910 -12.492 1.00 138.23 ? 566 ARG A CB 1 ATOM 4387 C CG . ARG A 1 566 ? -19.899 52.553 -13.173 1.00 145.90 ? 566 ARG A CG 1 ATOM 4388 C CD . ARG A 1 566 ? -18.465 52.047 -13.213 1.00 150.32 ? 566 ARG A CD 1 ATOM 4389 N NE . ARG A 1 566 ? -18.351 50.767 -13.906 1.00 154.47 ? 566 ARG A NE 1 ATOM 4390 C CZ . ARG A 1 566 ? -18.400 49.583 -13.305 1.00 147.09 ? 566 ARG A CZ 1 ATOM 4391 N NH1 . ARG A 1 566 ? -18.562 49.511 -11.990 1.00 139.11 ? 566 ARG A NH1 1 ATOM 4392 N NH2 . ARG A 1 566 ? -18.287 48.470 -14.017 1.00 143.58 ? 566 ARG A NH2 1 ATOM 4393 N N . THR A 1 567 ? -18.250 55.689 -10.010 1.00 135.72 ? 567 THR A N 1 ATOM 4394 C CA . THR A 1 567 ? -18.100 56.787 -9.056 1.00 126.54 ? 567 THR A CA 1 ATOM 4395 C C . THR A 1 567 ? -16.635 57.109 -8.775 1.00 127.39 ? 567 THR A C 1 ATOM 4396 O O . THR A 1 567 ? -15.741 56.379 -9.205 1.00 132.62 ? 567 THR A O 1 ATOM 4397 C CB . THR A 1 567 ? -18.763 56.442 -7.700 1.00 119.02 ? 567 THR A CB 1 ATOM 4398 O OG1 . THR A 1 567 ? -18.729 55.022 -7.510 1.00 129.67 ? 567 THR A OG1 1 ATOM 4399 C CG2 . THR A 1 567 ? -20.208 56.915 -7.631 1.00 111.01 ? 567 THR A CG2 1 ATOM 4400 N N . ALA A 1 568 ? -16.406 58.207 -8.054 1.00 131.01 ? 568 ALA A N 1 ATOM 4401 C CA . ALA A 1 568 ? -15.079 58.552 -7.537 1.00 132.91 ? 568 ALA A CA 1 ATOM 4402 C C . ALA A 1 568 ? -14.023 58.672 -8.632 1.00 129.55 ? 568 ALA A C 1 ATOM 4403 O O . ALA A 1 568 ? -13.177 57.788 -8.778 1.00 124.23 ? 568 ALA A O 1 ATOM 4404 C CB . ALA A 1 568 ? -14.642 57.536 -6.501 1.00 136.00 ? 568 ALA A CB 1 ATOM 4405 N N . ALA A 1 569 ? -14.089 59.759 -9.396 1.00 142.54 ? 569 ALA A N 1 ATOM 4406 C CA . ALA A 1 569 ? -13.226 59.967 -10.559 1.00 150.76 ? 569 ALA A CA 1 ATOM 4407 C C . ALA A 1 569 ? -11.743 59.753 -10.255 1.00 150.56 ? 569 ALA A C 1 ATOM 4408 O O . ALA A 1 569 ? -11.216 60.255 -9.261 1.00 138.50 ? 569 ALA A O 1 ATOM 4409 C CB . ALA A 1 569 ? -13.444 61.363 -11.123 1.00 151.53 ? 569 ALA A CB 1 ATOM 4410 N N . ASP A 1 570 ? -11.094 58.999 -11.138 1.00 158.44 ? 570 ASP A N 1 ATOM 4411 C CA . ASP A 1 570 ? -9.712 58.550 -10.981 1.00 158.96 ? 570 ASP A CA 1 ATOM 4412 C C . ASP A 1 570 ? -9.478 57.859 -9.641 1.00 157.91 ? 570 ASP A C 1 ATOM 4413 O O . ASP A 1 570 ? -10.364 57.170 -9.132 1.00 147.90 ? 570 ASP A O 1 ATOM 4414 C CB . ASP A 1 570 ? -8.745 59.727 -11.133 1.00 157.96 ? 570 ASP A CB 1 ATOM 4415 C CG . ASP A 1 570 ? -8.801 60.354 -12.511 1.00 163.37 ? 570 ASP A CG 1 ATOM 4416 O OD1 . ASP A 1 570 ? -9.099 59.630 -13.484 1.00 165.79 ? 570 ASP A OD1 1 ATOM 4417 O OD2 . ASP A 1 570 ? -8.547 61.572 -12.622 1.00 164.03 ? 570 ASP A OD2 1 ATOM 4418 N N . THR A 1 571 ? -8.298 58.092 -9.067 1.00 168.86 ? 571 THR A N 1 ATOM 4419 C CA . THR A 1 571 ? -7.859 57.441 -7.832 1.00 171.39 ? 571 THR A CA 1 ATOM 4420 C C . THR A 1 571 ? -8.240 55.965 -7.812 1.00 167.13 ? 571 THR A C 1 ATOM 4421 O O . THR A 1 571 ? -8.995 55.538 -6.936 1.00 163.01 ? 571 THR A O 1 ATOM 4422 C CB . THR A 1 571 ? -8.457 58.124 -6.585 1.00 168.09 ? 571 THR A CB 1 ATOM 4423 O OG1 . THR A 1 571 ? -9.884 57.982 -6.594 1.00 153.27 ? 571 THR A OG1 1 ATOM 4424 C CG2 . THR A 1 571 ? -8.096 59.601 -6.559 1.00 176.77 ? 571 THR A CG2 1 ATOM 4425 N N . THR A 1 572 ? -7.706 55.196 -8.762 1.00 168.66 ? 572 THR A N 1 ATOM 4426 C CA . THR A 1 572 ? -8.192 53.839 -9.009 1.00 170.78 ? 572 THR A CA 1 ATOM 4427 C C . THR A 1 572 ? -9.704 53.947 -9.184 1.00 160.01 ? 572 THR A C 1 ATOM 4428 O O . THR A 1 572 ? -10.186 54.532 -10.154 1.00 160.07 ? 572 THR A O 1 ATOM 4429 C CB . THR A 1 572 ? -7.831 52.856 -7.873 1.00 171.69 ? 572 THR A CB 1 ATOM 4430 O OG1 . THR A 1 572 ? -6.503 53.126 -7.407 1.00 178.15 ? 572 THR A OG1 1 ATOM 4431 C CG2 . THR A 1 572 ? -7.908 51.414 -8.365 1.00 160.62 ? 572 THR A CG2 1 ATOM 4432 N N . GLY A 1 573 ? -10.445 53.374 -8.244 1.00 144.42 ? 573 GLY A N 1 ATOM 4433 C CA . GLY A 1 573 ? -11.860 53.656 -8.122 1.00 133.01 ? 573 GLY A CA 1 ATOM 4434 C C . GLY A 1 573 ? -12.279 53.482 -6.677 1.00 131.83 ? 573 GLY A C 1 ATOM 4435 O O . GLY A 1 573 ? -11.660 52.723 -5.932 1.00 147.80 ? 573 GLY A O 1 ATOM 4436 N N . LEU A 1 574 ? -13.331 54.187 -6.276 1.00 117.49 ? 574 LEU A N 1 ATOM 4437 C CA . LEU A 1 574 ? -13.829 54.087 -4.912 1.00 113.16 ? 574 LEU A CA 1 ATOM 4438 C C . LEU A 1 574 ? -15.343 53.940 -4.925 1.00 110.73 ? 574 LEU A C 1 ATOM 4439 O O . LEU A 1 574 ? -16.062 54.846 -5.347 1.00 112.15 ? 574 LEU A O 1 ATOM 4440 C CB . LEU A 1 574 ? -13.410 55.308 -4.090 1.00 108.63 ? 574 LEU A CB 1 ATOM 4441 C CG . LEU A 1 574 ? -13.614 55.244 -2.576 1.00 104.68 ? 574 LEU A CG 1 ATOM 4442 C CD1 . LEU A 1 574 ? -12.730 54.168 -1.965 1.00 90.52 ? 574 LEU A CD1 1 ATOM 4443 C CD2 . LEU A 1 574 ? -13.335 56.596 -1.940 1.00 102.45 ? 574 LEU A CD2 1 ATOM 4444 N N . GLN A 1 575 ? -15.822 52.797 -4.451 1.00 111.17 ? 575 GLN A N 1 ATOM 4445 C CA . GLN A 1 575 ? -17.242 52.483 -4.498 1.00 118.23 ? 575 GLN A CA 1 ATOM 4446 C C . GLN A 1 575 ? -17.945 52.912 -3.219 1.00 121.45 ? 575 GLN A C 1 ATOM 4447 O O . GLN A 1 575 ? -17.679 52.362 -2.154 1.00 136.83 ? 575 GLN A O 1 ATOM 4448 C CB . GLN A 1 575 ? -17.449 50.983 -4.723 1.00 121.04 ? 575 GLN A CB 1 ATOM 4449 C CG . GLN A 1 575 ? -16.539 50.365 -5.776 1.00 118.36 ? 575 GLN A CG 1 ATOM 4450 C CD . GLN A 1 575 ? -17.028 50.598 -7.192 1.00 120.95 ? 575 GLN A CD 1 ATOM 4451 O OE1 . GLN A 1 575 ? -17.255 51.734 -7.608 1.00 132.38 ? 575 GLN A OE1 1 ATOM 4452 N NE2 . GLN A 1 575 ? -17.199 49.515 -7.942 1.00 115.21 ? 575 GLN A NE2 1 ATOM 4453 N N . PRO A 1 576 ? -18.843 53.902 -3.315 1.00 103.02 ? 576 PRO A N 1 ATOM 4454 C CA . PRO A 1 576 ? -19.653 54.259 -2.149 1.00 96.55 ? 576 PRO A CA 1 ATOM 4455 C C . PRO A 1 576 ? -20.548 53.093 -1.755 1.00 103.49 ? 576 PRO A C 1 ATOM 4456 O O . PRO A 1 576 ? -21.124 52.447 -2.629 1.00 120.97 ? 576 PRO A O 1 ATOM 4457 C CB . PRO A 1 576 ? -20.483 55.451 -2.640 1.00 93.65 ? 576 PRO A CB 1 ATOM 4458 C CG . PRO A 1 576 ? -19.765 55.958 -3.846 1.00 98.75 ? 576 PRO A CG 1 ATOM 4459 C CD . PRO A 1 576 ? -19.144 54.754 -4.474 1.00 109.21 ? 576 PRO A CD 1 ATOM 4460 N N . ILE A 1 577 ? -20.655 52.823 -0.461 1.00 88.23 ? 577 ILE A N 1 ATOM 4461 C CA . ILE A 1 577 ? -21.468 51.713 0.012 1.00 86.14 ? 577 ILE A CA 1 ATOM 4462 C C . ILE A 1 577 ? -22.690 52.259 0.740 1.00 84.91 ? 577 ILE A C 1 ATOM 4463 O O . ILE A 1 577 ? -22.656 53.365 1.276 1.00 79.28 ? 577 ILE A O 1 ATOM 4464 C CB . ILE A 1 577 ? -20.662 50.769 0.937 1.00 82.78 ? 577 ILE A CB 1 ATOM 4465 C CG1 . ILE A 1 577 ? -21.410 49.450 1.156 1.00 91.74 ? 577 ILE A CG1 1 ATOM 4466 C CG2 . ILE A 1 577 ? -20.334 51.451 2.260 1.00 68.04 ? 577 ILE A CG2 1 ATOM 4467 C CD1 . ILE A 1 577 ? -21.788 48.739 -0.127 1.00 83.91 ? 577 ILE A CD1 1 ATOM 4468 N N . LEU A 1 578 ? -23.775 51.493 0.743 1.00 85.58 ? 578 LEU A N 1 ATOM 4469 C CA . LEU A 1 578 ? -25.009 51.937 1.376 1.00 85.01 ? 578 LEU A CA 1 ATOM 4470 C C . LEU A 1 578 ? -24.845 51.948 2.892 1.00 94.12 ? 578 LEU A C 1 ATOM 4471 O O . LEU A 1 578 ? -23.788 51.586 3.411 1.00 114.26 ? 578 LEU A O 1 ATOM 4472 C CB . LEU A 1 578 ? -26.185 51.040 0.974 1.00 83.65 ? 578 LEU A CB 1 ATOM 4473 C CG . LEU A 1 578 ? -26.778 51.171 -0.434 1.00 82.00 ? 578 LEU A CG 1 ATOM 4474 C CD1 . LEU A 1 578 ? -25.844 50.628 -1.509 1.00 83.22 ? 578 LEU A CD1 1 ATOM 4475 C CD2 . LEU A 1 578 ? -28.128 50.472 -0.500 1.00 87.11 ? 578 LEU A CD2 1 ATOM 4476 N N . ASN A 1 579 ? -25.891 52.359 3.600 1.00 85.27 ? 579 ASN A N 1 ATOM 4477 C CA . ASN A 1 579 ? -25.822 52.476 5.051 1.00 86.52 ? 579 ASN A CA 1 ATOM 4478 C C . ASN A 1 579 ? -25.623 51.111 5.698 1.00 87.07 ? 579 ASN A C 1 ATOM 4479 O O . ASN A 1 579 ? -25.954 50.084 5.105 1.00 86.17 ? 579 ASN A O 1 ATOM 4480 C CB . ASN A 1 579 ? -27.085 53.144 5.597 1.00 101.57 ? 579 ASN A CB 1 ATOM 4481 C CG . ASN A 1 579 ? -26.874 53.762 6.967 1.00 111.81 ? 579 ASN A CG 1 ATOM 4482 O OD1 . ASN A 1 579 ? -25.978 53.363 7.711 1.00 116.99 ? 579 ASN A OD1 1 ATOM 4483 N ND2 . ASN A 1 579 ? -27.702 54.743 7.306 1.00 112.86 ? 579 ASN A ND2 1 ATOM 4484 N N . GLN A 1 580 ? -25.065 51.110 6.906 1.00 102.74 ? 580 GLN A N 1 ATOM 4485 C CA . GLN A 1 580 ? -24.798 49.876 7.637 1.00 106.07 ? 580 GLN A CA 1 ATOM 4486 C C . GLN A 1 580 ? -26.068 49.046 7.768 1.00 107.51 ? 580 GLN A C 1 ATOM 4487 O O . GLN A 1 580 ? -26.169 47.958 7.201 1.00 96.15 ? 580 GLN A O 1 ATOM 4488 C CB . GLN A 1 580 ? -24.219 50.184 9.017 1.00 100.68 ? 580 GLN A CB 1 ATOM 4489 C CG . GLN A 1 580 ? -23.707 48.964 9.763 1.00 100.56 ? 580 GLN A CG 1 ATOM 4490 C CD . GLN A 1 580 ? -22.991 49.331 11.046 1.00 114.32 ? 580 GLN A CD 1 ATOM 4491 O OE1 . GLN A 1 580 ? -22.879 50.507 11.393 1.00 109.47 ? 580 GLN A OE1 1 ATOM 4492 N NE2 . GLN A 1 580 ? -22.499 48.324 11.758 1.00 126.06 ? 580 GLN A NE2 1 ATOM 4493 N N . PHE A 1 581 ? -27.039 49.567 8.509 1.00 119.07 ? 581 PHE A N 1 ATOM 4494 C CA . PHE A 1 581 ? -28.349 48.939 8.564 1.00 127.28 ? 581 PHE A CA 1 ATOM 4495 C C . PHE A 1 581 ? -29.331 49.720 7.702 1.00 123.59 ? 581 PHE A C 1 ATOM 4496 O O . PHE A 1 581 ? -29.755 50.819 8.060 1.00 109.11 ? 581 PHE A O 1 ATOM 4497 C CB . PHE A 1 581 ? -28.850 48.851 10.006 1.00 129.62 ? 581 PHE A CB 1 ATOM 4498 C CG . PHE A 1 581 ? -27.988 48.001 10.894 1.00 124.16 ? 581 PHE A CG 1 ATOM 4499 C CD1 . PHE A 1 581 ? -26.967 48.567 11.640 1.00 119.35 ? 581 PHE A CD1 1 ATOM 4500 C CD2 . PHE A 1 581 ? -28.195 46.634 10.979 1.00 118.28 ? 581 PHE A CD2 1 ATOM 4501 C CE1 . PHE A 1 581 ? -26.171 47.786 12.456 1.00 112.62 ? 581 PHE A CE1 1 ATOM 4502 C CE2 . PHE A 1 581 ? -27.402 45.848 11.793 1.00 122.63 ? 581 PHE A CE2 1 ATOM 4503 C CZ . PHE A 1 581 ? -26.389 46.425 12.533 1.00 119.33 ? 581 PHE A CZ 1 ATOM 4504 N N . THR A 1 582 ? -29.683 49.142 6.560 1.00 128.64 ? 582 THR A N 1 ATOM 4505 C CA . THR A 1 582 ? -30.651 49.744 5.656 1.00 124.49 ? 582 THR A CA 1 ATOM 4506 C C . THR A 1 582 ? -31.444 48.654 4.945 1.00 117.66 ? 582 THR A C 1 ATOM 4507 O O . THR A 1 582 ? -30.916 47.574 4.675 1.00 114.37 ? 582 THR A O 1 ATOM 4508 C CB . THR A 1 582 ? -29.966 50.658 4.614 1.00 120.33 ? 582 THR A CB 1 ATOM 4509 O OG1 . THR A 1 582 ? -30.949 51.191 3.717 1.00 122.42 ? 582 THR A OG1 1 ATOM 4510 C CG2 . THR A 1 582 ? -28.927 49.885 3.815 1.00 112.91 ? 582 THR A CG2 1 ATOM 4511 N N . PRO A 1 583 ? -32.722 48.927 4.652 1.00 108.95 ? 583 PRO A N 1 ATOM 4512 C CA . PRO A 1 583 ? -33.508 47.975 3.865 1.00 108.63 ? 583 PRO A CA 1 ATOM 4513 C C . PRO A 1 583 ? -32.972 47.850 2.443 1.00 110.76 ? 583 PRO A C 1 ATOM 4514 O O . PRO A 1 583 ? -32.710 48.862 1.796 1.00 110.07 ? 583 PRO A O 1 ATOM 4515 C CB . PRO A 1 583 ? -34.913 48.586 3.870 1.00 111.55 ? 583 PRO A CB 1 ATOM 4516 C CG . PRO A 1 583 ? -34.939 49.470 5.074 1.00 111.96 ? 583 PRO A CG 1 ATOM 4517 C CD . PRO A 1 583 ? -33.551 50.020 5.187 1.00 110.52 ? 583 PRO A CD 1 ATOM 4518 N N . ALA A 1 584 ? -32.808 46.620 1.969 1.00 125.41 ? 584 ALA A N 1 ATOM 4519 C CA . ALA A 1 584 ? -32.387 46.383 0.595 1.00 127.81 ? 584 ALA A CA 1 ATOM 4520 C C . ALA A 1 584 ? -33.617 46.291 -0.295 1.00 119.70 ? 584 ALA A C 1 ATOM 4521 O O . ALA A 1 584 ? -33.512 46.068 -1.502 1.00 111.39 ? 584 ALA A O 1 ATOM 4522 C CB . ALA A 1 584 ? -31.554 45.117 0.496 1.00 133.09 ? 584 ALA A CB 1 ATOM 4523 N N . ASN A 1 585 ? -34.778 46.492 0.322 1.00 120.11 ? 585 ASN A N 1 ATOM 4524 C CA . ASN A 1 585 ? -36.066 46.321 -0.335 1.00 109.96 ? 585 ASN A CA 1 ATOM 4525 C C . ASN A 1 585 ? -37.211 46.705 0.591 1.00 102.48 ? 585 ASN A C 1 ATOM 4526 O O . ASN A 1 585 ? -37.025 46.835 1.801 1.00 103.29 ? 585 ASN A O 1 ATOM 4527 C CB . ASN A 1 585 ? -36.247 44.872 -0.794 1.00 114.59 ? 585 ASN A CB 1 ATOM 4528 C CG . ASN A 1 585 ? -36.295 43.896 0.364 1.00 118.04 ? 585 ASN A CG 1 ATOM 4529 O OD1 . ASN A 1 585 ? -37.330 43.730 1.009 1.00 116.31 ? 585 ASN A OD1 1 ATOM 4530 N ND2 . ASN A 1 585 ? -35.173 43.242 0.632 1.00 144.03 ? 585 ASN A ND2 1 ATOM 4531 N N . ILE A 1 586 ? -38.397 46.887 0.020 1.00 96.32 ? 586 ILE A N 1 ATOM 4532 C CA . ILE A 1 586 ? -39.591 47.139 0.816 1.00 90.37 ? 586 ILE A CA 1 ATOM 4533 C C . ILE A 1 586 ? -40.795 46.468 0.162 1.00 87.28 ? 586 ILE A C 1 ATOM 4534 O O . ILE A 1 586 ? -40.816 46.250 -1.050 1.00 87.11 ? 586 ILE A O 1 ATOM 4535 C CB . ILE A 1 586 ? -39.857 48.652 0.995 1.00 96.77 ? 586 ILE A CB 1 ATOM 4536 C CG1 . ILE A 1 586 ? -40.751 48.903 2.212 1.00 109.18 ? 586 ILE A CG1 1 ATOM 4537 C CG2 . ILE A 1 586 ? -40.473 49.248 -0.258 1.00 89.08 ? 586 ILE A CG2 1 ATOM 4538 C CD1 . ILE A 1 586 ? -40.186 48.364 3.509 1.00 106.23 ? 586 ILE A CD1 1 ATOM 4539 N N . SER A 1 587 ? -41.788 46.125 0.975 1.00 92.34 ? 587 SER A N 1 ATOM 4540 C CA . SER A 1 587 ? -42.977 45.449 0.480 1.00 94.40 ? 587 SER A CA 1 ATOM 4541 C C . SER A 1 587 ? -44.246 46.182 0.895 1.00 102.22 ? 587 SER A C 1 ATOM 4542 O O . SER A 1 587 ? -44.272 46.877 1.910 1.00 111.51 ? 587 SER A O 1 ATOM 4543 C CB . SER A 1 587 ? -43.021 44.005 0.986 1.00 92.85 ? 587 SER A CB 1 ATOM 4544 O OG . SER A 1 587 ? -41.864 43.288 0.594 1.00 97.17 ? 587 SER A OG 1 ATOM 4545 N N . ARG A 1 588 ? -45.294 46.028 0.094 1.00 97.79 ? 588 ARG A N 1 ATOM 4546 C CA . ARG A 1 588 ? -46.608 46.543 0.446 1.00 86.41 ? 588 ARG A CA 1 ATOM 4547 C C . ARG A 1 588 ? -47.675 45.637 -0.150 1.00 83.54 ? 588 ARG A C 1 ATOM 4548 O O . ARG A 1 588 ? -47.510 45.113 -1.252 1.00 83.38 ? 588 ARG A O 1 ATOM 4549 C CB . ARG A 1 588 ? -46.782 47.982 -0.037 1.00 87.35 ? 588 ARG A CB 1 ATOM 4550 C CG . ARG A 1 588 ? -47.905 48.725 0.665 1.00 97.37 ? 588 ARG A CG 1 ATOM 4551 C CD . ARG A 1 588 ? -47.685 50.224 0.607 1.00 110.81 ? 588 ARG A CD 1 ATOM 4552 N NE . ARG A 1 588 ? -46.291 50.573 0.868 1.00 116.01 ? 588 ARG A NE 1 ATOM 4553 C CZ . ARG A 1 588 ? -45.749 50.647 2.080 1.00 109.42 ? 588 ARG A CZ 1 ATOM 4554 N NH1 . ARG A 1 588 ? -46.481 50.393 3.156 1.00 97.44 ? 588 ARG A NH1 1 ATOM 4555 N NH2 . ARG A 1 588 ? -44.470 50.971 2.215 1.00 111.10 ? 588 ARG A NH2 1 ATOM 4556 N N . GLN A 1 589 ? -48.769 45.451 0.580 1.00 82.79 ? 589 GLN A N 1 ATOM 4557 C CA . GLN A 1 589 ? -49.764 44.459 0.197 1.00 82.74 ? 589 GLN A CA 1 ATOM 4558 C C . GLN A 1 589 ? -51.065 45.068 -0.307 1.00 83.03 ? 589 GLN A C 1 ATOM 4559 O O . GLN A 1 589 ? -51.553 46.064 0.226 1.00 78.63 ? 589 GLN A O 1 ATOM 4560 C CB . GLN A 1 589 ? -50.060 43.533 1.378 1.00 82.80 ? 589 GLN A CB 1 ATOM 4561 C CG . GLN A 1 589 ? -48.826 42.879 1.971 1.00 93.41 ? 589 GLN A CG 1 ATOM 4562 C CD . GLN A 1 589 ? -49.165 41.824 3.004 1.00 99.47 ? 589 GLN A CD 1 ATOM 4563 O OE1 . GLN A 1 589 ? -50.336 41.580 3.297 1.00 92.35 ? 589 GLN A OE1 1 ATOM 4564 N NE2 . GLN A 1 589 ? -48.140 41.190 3.560 1.00 106.89 ? 589 GLN A NE2 1 ATOM 4565 N N . ALA A 1 590 ? -51.618 44.451 -1.346 1.00 82.93 ? 590 ALA A N 1 ATOM 4566 C CA . ALA A 1 590 ? -52.951 44.779 -1.826 1.00 82.66 ? 590 ALA A CA 1 ATOM 4567 C C . ALA A 1 590 ? -53.855 43.575 -1.607 1.00 81.18 ? 590 ALA A C 1 ATOM 4568 O O . ALA A 1 590 ? -53.394 42.434 -1.640 1.00 80.98 ? 590 ALA A O 1 ATOM 4569 C CB . ALA A 1 590 ? -52.918 45.173 -3.292 1.00 83.50 ? 590 ALA A CB 1 ATOM 4570 N N . HIS A 1 591 ? -55.138 43.825 -1.375 1.00 80.72 ? 591 HIS A N 1 ATOM 4571 C CA . HIS A 1 591 ? -56.076 42.742 -1.107 1.00 80.44 ? 591 HIS A CA 1 ATOM 4572 C C . HIS A 1 591 ? -57.230 42.746 -2.101 1.00 84.49 ? 591 HIS A C 1 ATOM 4573 O O . HIS A 1 591 ? -57.631 43.797 -2.597 1.00 91.19 ? 591 HIS A O 1 ATOM 4574 C CB . HIS A 1 591 ? -56.616 42.843 0.321 1.00 75.60 ? 591 HIS A CB 1 ATOM 4575 C CG . HIS A 1 591 ? -55.552 42.824 1.374 1.00 75.91 ? 591 HIS A CG 1 ATOM 4576 N ND1 . HIS A 1 591 ? -54.713 43.893 1.605 1.00 88.44 ? 591 HIS A ND1 1 ATOM 4577 C CD2 . HIS A 1 591 ? -55.194 41.867 2.263 1.00 76.62 ? 591 HIS A CD2 1 ATOM 4578 C CE1 . HIS A 1 591 ? -53.882 43.595 2.588 1.00 90.14 ? 591 HIS A CE1 1 ATOM 4579 N NE2 . HIS A 1 591 ? -54.153 42.371 3.005 1.00 86.02 ? 591 HIS A NE2 1 ATOM 4580 N N . ILE A 1 592 ? -57.756 41.562 -2.394 1.00 81.52 ? 592 ILE A N 1 ATOM 4581 C CA . ILE A 1 592 ? -58.924 41.437 -3.255 1.00 84.32 ? 592 ILE A CA 1 ATOM 4582 C C . ILE A 1 592 ? -60.183 41.579 -2.409 1.00 83.60 ? 592 ILE A C 1 ATOM 4583 O O . ILE A 1 592 ? -60.268 41.016 -1.318 1.00 82.08 ? 592 ILE A O 1 ATOM 4584 C CB . ILE A 1 592 ? -58.938 40.091 -4.003 1.00 87.54 ? 592 ILE A CB 1 ATOM 4585 C CG1 . ILE A 1 592 ? -57.609 39.876 -4.729 1.00 88.57 ? 592 ILE A CG1 1 ATOM 4586 C CG2 . ILE A 1 592 ? -60.100 40.033 -4.982 1.00 92.29 ? 592 ILE A CG2 1 ATOM 4587 C CD1 . ILE A 1 592 ? -57.530 38.570 -5.488 1.00 99.69 ? 592 ILE A CD1 1 ATOM 4588 N N . LEU A 1 593 ? -61.157 42.335 -2.908 1.00 85.07 ? 593 LEU A N 1 ATOM 4589 C CA . LEU A 1 593 ? -62.359 42.619 -2.134 1.00 84.94 ? 593 LEU A CA 1 ATOM 4590 C C . LEU A 1 593 ? -63.218 41.369 -1.994 1.00 87.21 ? 593 LEU A C 1 ATOM 4591 O O . LEU A 1 593 ? -63.655 40.789 -2.988 1.00 90.61 ? 593 LEU A O 1 ATOM 4592 C CB . LEU A 1 593 ? -63.157 43.749 -2.794 1.00 86.71 ? 593 LEU A CB 1 ATOM 4593 C CG . LEU A 1 593 ? -64.338 44.372 -2.044 1.00 92.77 ? 593 LEU A CG 1 ATOM 4594 C CD1 . LEU A 1 593 ? -64.460 45.841 -2.410 1.00 98.00 ? 593 LEU A CD1 1 ATOM 4595 C CD2 . LEU A 1 593 ? -65.640 43.646 -2.352 1.00 90.59 ? 593 LEU A CD2 1 ATOM 4596 N N . LEU A 1 594 ? -63.455 40.961 -0.752 1.00 89.94 ? 594 LEU A N 1 ATOM 4597 C CA . LEU A 1 594 ? -64.303 39.810 -0.469 1.00 88.17 ? 594 LEU A CA 1 ATOM 4598 C C . LEU A 1 594 ? -65.097 40.012 0.820 1.00 96.51 ? 594 LEU A C 1 ATOM 4599 O O . LEU A 1 594 ? -64.529 40.374 1.851 1.00 96.28 ? 594 LEU A O 1 ATOM 4600 C CB . LEU A 1 594 ? -63.453 38.539 -0.386 1.00 88.24 ? 594 LEU A CB 1 ATOM 4601 C CG . LEU A 1 594 ? -64.167 37.207 -0.161 1.00 91.41 ? 594 LEU A CG 1 ATOM 4602 C CD1 . LEU A 1 594 ? -63.597 36.142 -1.082 1.00 94.12 ? 594 LEU A CD1 1 ATOM 4603 C CD2 . LEU A 1 594 ? -64.037 36.775 1.289 1.00 116.01 ? 594 LEU A CD2 1 ATOM 4604 N N . ASP A 1 595 ? -66.403 39.761 0.752 1.00 106.75 ? 595 ASP A N 1 ATOM 4605 C CA . ASP A 1 595 ? -67.295 39.849 1.910 1.00 102.60 ? 595 ASP A CA 1 ATOM 4606 C C . ASP A 1 595 ? -67.148 41.148 2.702 1.00 98.36 ? 595 ASP A C 1 ATOM 4607 O O . ASP A 1 595 ? -67.015 41.124 3.926 1.00 85.84 ? 595 ASP A O 1 ATOM 4608 C CB . ASP A 1 595 ? -67.068 38.655 2.842 1.00 95.70 ? 595 ASP A CB 1 ATOM 4609 C CG . ASP A 1 595 ? -67.564 37.351 2.249 1.00 101.03 ? 595 ASP A CG 1 ATOM 4610 O OD1 . ASP A 1 595 ? -66.955 36.298 2.530 1.00 94.88 ? 595 ASP A OD1 1 ATOM 4611 O OD2 . ASP A 1 595 ? -68.564 37.379 1.502 1.00 106.62 ? 595 ASP A OD2 1 ATOM 4612 N N . CYS A 1 596 ? -67.163 42.276 2.001 1.00 97.65 ? 596 CYS A N 1 ATOM 4613 C CA . CYS A 1 596 ? -67.081 43.577 2.655 1.00 102.91 ? 596 CYS A CA 1 ATOM 4614 C C . CYS A 1 596 ? -68.464 44.190 2.866 1.00 97.84 ? 596 CYS A C 1 ATOM 4615 O O . CYS A 1 596 ? -68.587 45.306 3.372 1.00 91.47 ? 596 CYS A O 1 ATOM 4616 C CB . CYS A 1 596 ? -66.198 44.529 1.847 1.00 113.60 ? 596 CYS A CB 1 ATOM 4617 S SG . CYS A 1 596 ? -64.436 44.126 1.905 1.00 199.00 ? 596 CYS A SG 1 ATOM 4618 N N . GLY A 1 597 ? -69.500 43.456 2.475 1.00 101.62 ? 597 GLY A N 1 ATOM 4619 C CA . GLY A 1 597 ? -70.866 43.922 2.630 1.00 109.58 ? 597 GLY A CA 1 ATOM 4620 C C . GLY A 1 597 ? -71.347 44.718 1.433 1.00 111.92 ? 597 GLY A C 1 ATOM 4621 O O . GLY A 1 597 ? -70.617 44.887 0.456 1.00 113.59 ? 597 GLY A O 1 ATOM 4622 N N . GLU A 1 598 ? -72.580 45.212 1.510 1.00 109.90 ? 598 GLU A N 1 ATOM 4623 C CA . GLU A 1 598 ? -73.166 45.987 0.421 1.00 118.22 ? 598 GLU A CA 1 ATOM 4624 C C . GLU A 1 598 ? -72.483 47.341 0.261 1.00 117.96 ? 598 GLU A C 1 ATOM 4625 O O . GLU A 1 598 ? -72.581 47.976 -0.789 1.00 121.43 ? 598 GLU A O 1 ATOM 4626 C CB . GLU A 1 598 ? -74.667 46.182 0.648 1.00 128.51 ? 598 GLU A CB 1 ATOM 4627 C CG . GLU A 1 598 ? -75.475 44.896 0.603 1.00 139.55 ? 598 GLU A CG 1 ATOM 4628 C CD . GLU A 1 598 ? -76.969 45.143 0.671 1.00 145.86 ? 598 GLU A CD 1 ATOM 4629 O OE1 . GLU A 1 598 ? -77.372 46.304 0.899 1.00 157.11 ? 598 GLU A OE1 1 ATOM 4630 O OE2 . GLU A 1 598 ? -77.742 44.178 0.491 1.00 134.90 ? 598 GLU A OE2 1 ATOM 4631 N N . ASP A 1 599 ? -71.790 47.777 1.308 1.00 108.88 ? 599 ASP A N 1 ATOM 4632 C CA . ASP A 1 599 ? -71.068 49.044 1.278 1.00 107.83 ? 599 ASP A CA 1 ATOM 4633 C C . ASP A 1 599 ? -69.771 48.923 0.483 1.00 116.96 ? 599 ASP A C 1 ATOM 4634 O O . ASP A 1 599 ? -69.110 49.925 0.206 1.00 123.86 ? 599 ASP A O 1 ATOM 4635 C CB . ASP A 1 599 ? -70.773 49.523 2.702 1.00 106.31 ? 599 ASP A CB 1 ATOM 4636 C CG . ASP A 1 599 ? -70.048 48.479 3.532 1.00 114.57 ? 599 ASP A CG 1 ATOM 4637 O OD1 . ASP A 1 599 ? -70.141 47.279 3.196 1.00 130.32 ? 599 ASP A OD1 1 ATOM 4638 O OD2 . ASP A 1 599 ? -69.391 48.855 4.525 1.00 107.53 ? 599 ASP A OD2 1 ATOM 4639 N N . ASN A 1 600 ? -69.416 47.688 0.131 1.00 120.19 ? 600 ASN A N 1 ATOM 4640 C CA . ASN A 1 600 ? -68.198 47.384 -0.622 1.00 110.75 ? 600 ASN A CA 1 ATOM 4641 C C . ASN A 1 600 ? -66.934 47.859 0.087 1.00 98.45 ? 600 ASN A C 1 ATOM 4642 O O . ASN A 1 600 ? -65.905 48.093 -0.545 1.00 93.62 ? 600 ASN A O 1 ATOM 4643 C CB . ASN A 1 600 ? -68.267 47.991 -2.027 1.00 106.88 ? 600 ASN A CB 1 ATOM 4644 C CG . ASN A 1 600 ? -69.251 47.270 -2.926 1.00 121.71 ? 600 ASN A CG 1 ATOM 4645 O OD1 . ASN A 1 600 ? -69.429 46.056 -2.822 1.00 131.61 ? 600 ASN A OD1 1 ATOM 4646 N ND2 . ASN A 1 600 ? -69.896 48.014 -3.816 1.00 133.09 ? 600 ASN A ND2 1 ATOM 4647 N N . VAL A 1 601 ? -67.021 47.997 1.405 1.00 93.09 ? 601 VAL A N 1 ATOM 4648 C CA . VAL A 1 601 ? -65.872 48.365 2.220 1.00 89.45 ? 601 VAL A CA 1 ATOM 4649 C C . VAL A 1 601 ? -65.953 47.633 3.555 1.00 88.14 ? 601 VAL A C 1 ATOM 4650 O O . VAL A 1 601 ? -67.020 47.553 4.166 1.00 82.89 ? 601 VAL A O 1 ATOM 4651 C CB . VAL A 1 601 ? -65.794 49.895 2.441 1.00 90.24 ? 601 VAL A CB 1 ATOM 4652 C CG1 . VAL A 1 601 ? -67.146 50.452 2.862 1.00 99.57 ? 601 VAL A CG1 1 ATOM 4653 C CG2 . VAL A 1 601 ? -64.714 50.245 3.456 1.00 88.14 ? 601 VAL A CG2 1 ATOM 4654 N N . CYS A 1 602 ? -64.827 47.084 3.999 1.00 84.00 ? 602 CYS A N 1 ATOM 4655 C CA . CYS A 1 602 ? -64.802 46.313 5.234 1.00 81.84 ? 602 CYS A CA 1 ATOM 4656 C C . CYS A 1 602 ? -64.553 47.206 6.444 1.00 82.89 ? 602 CYS A C 1 ATOM 4657 O O . CYS A 1 602 ? -63.518 47.864 6.545 1.00 90.19 ? 602 CYS A O 1 ATOM 4658 C CB . CYS A 1 602 ? -63.744 45.212 5.152 1.00 85.73 ? 602 CYS A CB 1 ATOM 4659 S SG . CYS A 1 602 ? -64.097 43.952 3.901 1.00 80.09 ? 602 CYS A SG 1 ATOM 4660 N N . LYS A 1 603 ? -65.517 47.220 7.359 1.00 83.23 ? 603 LYS A N 1 ATOM 4661 C CA . LYS A 1 603 ? -65.432 48.035 8.565 1.00 85.15 ? 603 LYS A CA 1 ATOM 4662 C C . LYS A 1 603 ? -65.519 47.149 9.802 1.00 89.76 ? 603 LYS A C 1 ATOM 4663 O O . LYS A 1 603 ? -66.606 46.915 10.331 1.00 99.84 ? 603 LYS A O 1 ATOM 4664 C CB . LYS A 1 603 ? -66.540 49.090 8.581 1.00 93.93 ? 603 LYS A CB 1 ATOM 4665 C CG . LYS A 1 603 ? -66.590 49.948 7.326 1.00 100.04 ? 603 LYS A CG 1 ATOM 4666 C CD . LYS A 1 603 ? -67.717 50.968 7.384 1.00 107.23 ? 603 LYS A CD 1 ATOM 4667 C CE . LYS A 1 603 ? -67.467 52.015 8.456 1.00 109.38 ? 603 LYS A CE 1 ATOM 4668 N NZ . LYS A 1 603 ? -68.518 53.070 8.452 1.00 112.55 ? 603 LYS A NZ 1 ATOM 4669 N N . PRO A 1 604 ? -64.363 46.650 10.263 1.00 85.87 ? 604 PRO A N 1 ATOM 4670 C CA . PRO A 1 604 ? -64.270 45.692 11.369 1.00 87.31 ? 604 PRO A CA 1 ATOM 4671 C C . PRO A 1 604 ? -64.592 46.287 12.734 1.00 98.16 ? 604 PRO A C 1 ATOM 4672 O O . PRO A 1 604 ? -64.280 47.448 12.997 1.00 106.39 ? 604 PRO A O 1 ATOM 4673 C CB . PRO A 1 604 ? -62.806 45.251 11.320 1.00 83.17 ? 604 PRO A CB 1 ATOM 4674 C CG . PRO A 1 604 ? -62.092 46.410 10.730 1.00 82.44 ? 604 PRO A CG 1 ATOM 4675 C CD . PRO A 1 604 ? -63.037 46.996 9.722 1.00 84.52 ? 604 PRO A CD 1 ATOM 4676 N N . LYS A 1 605 ? -65.215 45.487 13.592 1.00 103.89 ? 605 LYS A N 1 ATOM 4677 C CA . LYS A 1 605 ? -65.364 45.846 14.993 1.00 108.07 ? 605 LYS A CA 1 ATOM 4678 C C . LYS A 1 605 ? -64.337 45.073 15.804 1.00 103.06 ? 605 LYS A C 1 ATOM 4679 O O . LYS A 1 605 ? -64.455 43.862 15.983 1.00 106.59 ? 605 LYS A O 1 ATOM 4680 C CB . LYS A 1 605 ? -66.777 45.551 15.497 1.00 115.99 ? 605 LYS A CB 1 ATOM 4681 C CG . LYS A 1 605 ? -67.825 46.553 15.047 1.00 127.62 ? 605 LYS A CG 1 ATOM 4682 C CD . LYS A 1 605 ? -69.167 46.317 15.734 1.00 136.78 ? 605 LYS A CD 1 ATOM 4683 C CE . LYS A 1 605 ? -69.140 46.718 17.208 1.00 133.86 ? 605 LYS A CE 1 ATOM 4684 N NZ . LYS A 1 605 ? -68.570 45.670 18.104 1.00 124.87 ? 605 LYS A NZ 1 ATOM 4685 N N . LEU A 1 606 ? -63.332 45.782 16.300 1.00 90.64 ? 606 LEU A N 1 ATOM 4686 C CA . LEU A 1 606 ? -62.230 45.144 17.001 1.00 87.13 ? 606 LEU A CA 1 ATOM 4687 C C . LEU A 1 606 ? -62.285 45.448 18.491 1.00 89.68 ? 606 LEU A C 1 ATOM 4688 O O . LEU A 1 606 ? -62.490 46.592 18.893 1.00 93.41 ? 606 LEU A O 1 ATOM 4689 C CB . LEU A 1 606 ? -60.893 45.599 16.414 1.00 88.37 ? 606 LEU A CB 1 ATOM 4690 C CG . LEU A 1 606 ? -60.723 45.407 14.905 1.00 84.66 ? 606 LEU A CG 1 ATOM 4691 C CD1 . LEU A 1 606 ? -59.435 46.055 14.421 1.00 79.33 ? 606 LEU A CD1 1 ATOM 4692 C CD2 . LEU A 1 606 ? -60.750 43.930 14.547 1.00 86.20 ? 606 LEU A CD2 1 ATOM 4693 N N . GLU A 1 607 ? -62.120 44.413 19.306 1.00 91.39 ? 607 GLU A N 1 ATOM 4694 C CA . GLU A 1 607 ? -62.073 44.582 20.752 1.00 90.42 ? 607 GLU A CA 1 ATOM 4695 C C . GLU A 1 607 ? -61.073 43.618 21.377 1.00 80.66 ? 607 GLU A C 1 ATOM 4696 O O . GLU A 1 607 ? -61.020 42.440 21.020 1.00 76.57 ? 607 GLU A O 1 ATOM 4697 C CB . GLU A 1 607 ? -63.464 44.390 21.362 1.00 98.63 ? 607 GLU A CB 1 ATOM 4698 C CG . GLU A 1 607 ? -64.179 43.126 20.919 1.00 114.07 ? 607 GLU A CG 1 ATOM 4699 C CD . GLU A 1 607 ? -65.634 43.108 21.344 1.00 120.29 ? 607 GLU A CD 1 ATOM 4700 O OE1 . GLU A 1 607 ? -66.336 42.123 21.032 1.00 119.51 ? 607 GLU A OE1 1 ATOM 4701 O OE2 . GLU A 1 607 ? -66.077 44.082 21.987 1.00 121.89 ? 607 GLU A OE2 1 ATOM 4702 N N . VAL A 1 608 ? -60.276 44.129 22.309 1.00 83.34 ? 608 VAL A N 1 ATOM 4703 C CA . VAL A 1 608 ? -59.250 43.329 22.962 1.00 80.50 ? 608 VAL A CA 1 ATOM 4704 C C . VAL A 1 608 ? -59.483 43.265 24.469 1.00 83.45 ? 608 VAL A C 1 ATOM 4705 O O . VAL A 1 608 ? -59.622 44.291 25.134 1.00 84.63 ? 608 VAL A O 1 ATOM 4706 C CB . VAL A 1 608 ? -57.836 43.886 22.671 1.00 77.64 ? 608 VAL A CB 1 ATOM 4707 C CG1 . VAL A 1 608 ? -57.822 45.406 22.767 1.00 77.92 ? 608 VAL A CG1 1 ATOM 4708 C CG2 . VAL A 1 608 ? -56.808 43.265 23.605 1.00 83.94 ? 608 VAL A CG2 1 ATOM 4709 N N . SER A 1 609 ? -59.533 42.048 25.001 1.00 85.92 ? 609 SER A N 1 ATOM 4710 C CA . SER A 1 609 ? -59.744 41.844 26.428 1.00 92.36 ? 609 SER A CA 1 ATOM 4711 C C . SER A 1 609 ? -58.513 41.207 27.058 1.00 94.90 ? 609 SER A C 1 ATOM 4712 O O . SER A 1 609 ? -57.742 40.530 26.381 1.00 91.87 ? 609 SER A O 1 ATOM 4713 C CB . SER A 1 609 ? -60.979 40.974 26.673 1.00 95.80 ? 609 SER A CB 1 ATOM 4714 O OG . SER A 1 609 ? -61.176 40.746 28.057 1.00 101.58 ? 609 SER A OG 1 ATOM 4715 N N . VAL A 1 610 ? -58.328 41.432 28.355 1.00 101.92 ? 610 VAL A N 1 ATOM 4716 C CA . VAL A 1 610 ? -57.157 40.919 29.054 1.00 100.80 ? 610 VAL A CA 1 ATOM 4717 C C . VAL A 1 610 ? -57.494 40.556 30.501 1.00 108.96 ? 610 VAL A C 1 ATOM 4718 O O . VAL A 1 610 ? -58.256 41.259 31.165 1.00 115.22 ? 610 VAL A O 1 ATOM 4719 C CB . VAL A 1 610 ? -56.001 41.948 29.017 1.00 98.21 ? 610 VAL A CB 1 ATOM 4720 C CG1 . VAL A 1 610 ? -56.476 43.308 29.513 1.00 104.07 ? 610 VAL A CG1 1 ATOM 4721 C CG2 . VAL A 1 610 ? -54.796 41.458 29.811 1.00 97.45 ? 610 VAL A CG2 1 ATOM 4722 N N . ASP A 1 611 ? -56.930 39.451 30.982 1.00 114.53 ? 611 ASP A N 1 ATOM 4723 C CA . ASP A 1 611 ? -57.169 39.006 32.350 1.00 129.13 ? 611 ASP A CA 1 ATOM 4724 C C . ASP A 1 611 ? -55.907 39.171 33.192 1.00 137.67 ? 611 ASP A C 1 ATOM 4725 O O . ASP A 1 611 ? -54.790 39.099 32.679 1.00 136.40 ? 611 ASP A O 1 ATOM 4726 C CB . ASP A 1 611 ? -57.640 37.550 32.372 1.00 139.68 ? 611 ASP A CB 1 ATOM 4727 C CG . ASP A 1 611 ? -58.417 37.207 33.631 1.00 142.20 ? 611 ASP A CG 1 ATOM 4728 O OD1 . ASP A 1 611 ? -58.164 37.833 34.682 1.00 135.56 ? 611 ASP A OD1 1 ATOM 4729 O OD2 . ASP A 1 611 ? -59.285 36.311 33.569 1.00 145.80 ? 611 ASP A OD2 1 ATOM 4730 N N . SER A 1 612 ? -56.100 39.390 34.488 1.00 148.05 ? 612 SER A N 1 ATOM 4731 C CA . SER A 1 612 ? -55.009 39.743 35.391 1.00 153.21 ? 612 SER A CA 1 ATOM 4732 C C . SER A 1 612 ? -53.989 38.629 35.606 1.00 154.36 ? 612 SER A C 1 ATOM 4733 O O . SER A 1 612 ? -52.797 38.903 35.756 1.00 151.90 ? 612 SER A O 1 ATOM 4734 C CB . SER A 1 612 ? -55.576 40.175 36.746 1.00 150.17 ? 612 SER A CB 1 ATOM 4735 O OG . SER A 1 612 ? -56.290 39.115 37.358 1.00 147.98 ? 612 SER A OG 1 ATOM 4736 N N . ASP A 1 613 ? -54.461 37.383 35.617 1.00 150.79 ? 613 ASP A N 1 ATOM 4737 C CA . ASP A 1 613 ? -53.632 36.233 35.980 1.00 147.97 ? 613 ASP A CA 1 ATOM 4738 C C . ASP A 1 613 ? -53.033 36.463 37.366 1.00 145.45 ? 613 ASP A C 1 ATOM 4739 O O . ASP A 1 613 ? -53.767 36.575 38.348 1.00 143.93 ? 613 ASP A O 1 ATOM 4740 C CB . ASP A 1 613 ? -52.534 35.988 34.940 1.00 148.84 ? 613 ASP A CB 1 ATOM 4741 C CG . ASP A 1 613 ? -51.967 34.581 35.005 1.00 154.71 ? 613 ASP A CG 1 ATOM 4742 O OD1 . ASP A 1 613 ? -52.070 33.940 36.072 1.00 154.70 ? 613 ASP A OD1 1 ATOM 4743 O OD2 . ASP A 1 613 ? -51.414 34.117 33.986 1.00 155.98 ? 613 ASP A OD2 1 ATOM 4744 N N . GLN A 1 614 ? -51.707 36.530 37.448 1.00 143.90 ? 614 GLN A N 1 ATOM 4745 C CA . GLN A 1 614 ? -51.056 36.861 38.710 1.00 139.03 ? 614 GLN A CA 1 ATOM 4746 C C . GLN A 1 614 ? -51.412 38.286 39.117 1.00 131.85 ? 614 GLN A C 1 ATOM 4747 O O . GLN A 1 614 ? -51.203 39.230 38.355 1.00 128.64 ? 614 GLN A O 1 ATOM 4748 C CB . GLN A 1 614 ? -49.536 36.706 38.609 1.00 139.95 ? 614 GLN A CB 1 ATOM 4749 C CG . GLN A 1 614 ? -49.052 35.271 38.472 1.00 142.76 ? 614 GLN A CG 1 ATOM 4750 C CD . GLN A 1 614 ? -48.711 34.901 37.043 1.00 135.42 ? 614 GLN A CD 1 ATOM 4751 O OE1 . GLN A 1 614 ? -49.020 35.638 36.107 1.00 129.73 ? 614 GLN A OE1 1 ATOM 4752 N NE2 . GLN A 1 614 ? -48.062 33.755 36.868 1.00 131.19 ? 614 GLN A NE2 1 ATOM 4753 N N . LYS A 1 615 ? -51.950 38.435 40.322 1.00 132.16 ? 615 LYS A N 1 ATOM 4754 C CA . LYS A 1 615 ? -52.368 39.739 40.821 1.00 129.36 ? 615 LYS A CA 1 ATOM 4755 C C . LYS A 1 615 ? -51.183 40.543 41.346 1.00 128.76 ? 615 LYS A C 1 ATOM 4756 O O . LYS A 1 615 ? -51.206 41.774 41.343 1.00 130.38 ? 615 LYS A O 1 ATOM 4757 C CB . LYS A 1 615 ? -53.419 39.577 41.921 1.00 127.01 ? 615 LYS A CB 1 ATOM 4758 C CG . LYS A 1 615 ? -54.694 38.881 41.466 1.00 128.35 ? 615 LYS A CG 1 ATOM 4759 C CD . LYS A 1 615 ? -55.492 39.742 40.497 1.00 123.92 ? 615 LYS A CD 1 ATOM 4760 C CE . LYS A 1 615 ? -56.576 40.541 41.210 1.00 124.62 ? 615 LYS A CE 1 ATOM 4761 N NZ . LYS A 1 615 ? -56.033 41.495 42.215 1.00 125.64 ? 615 LYS A NZ 1 ATOM 4762 N N . LYS A 1 616 ? -50.149 39.838 41.793 1.00 118.40 ? 616 LYS A N 1 ATOM 4763 C CA . LYS A 1 616 ? -49.018 40.477 42.454 1.00 109.89 ? 616 LYS A CA 1 ATOM 4764 C C . LYS A 1 616 ? -47.686 40.157 41.781 1.00 102.59 ? 616 LYS A C 1 ATOM 4765 O O . LYS A 1 616 ? -47.483 39.051 41.280 1.00 100.98 ? 616 LYS A O 1 ATOM 4766 C CB . LYS A 1 616 ? -48.963 40.051 43.923 1.00 117.29 ? 616 LYS A CB 1 ATOM 4767 C CG . LYS A 1 616 ? -50.306 40.101 44.635 1.00 120.29 ? 616 LYS A CG 1 ATOM 4768 C CD . LYS A 1 616 ? -50.246 39.399 45.982 1.00 122.11 ? 616 LYS A CD 1 ATOM 4769 C CE . LYS A 1 616 ? -51.618 39.343 46.634 1.00 120.80 ? 616 LYS A CE 1 ATOM 4770 N NZ . LYS A 1 616 ? -51.585 38.624 47.937 1.00 122.80 ? 616 LYS A NZ 1 ATOM 4771 N N . ILE A 1 617 ? -46.787 41.136 41.771 1.00 99.37 ? 617 ILE A N 1 ATOM 4772 C CA . ILE A 1 617 ? -45.408 40.917 41.345 1.00 96.44 ? 617 ILE A CA 1 ATOM 4773 C C . ILE A 1 617 ? -44.456 41.609 42.318 1.00 99.84 ? 617 ILE A C 1 ATOM 4774 O O . ILE A 1 617 ? -44.564 42.810 42.563 1.00 99.52 ? 617 ILE A O 1 ATOM 4775 C CB . ILE A 1 617 ? -45.152 41.420 39.909 1.00 92.97 ? 617 ILE A CB 1 ATOM 4776 C CG1 . ILE A 1 617 ? -45.749 42.812 39.702 1.00 99.81 ? 617 ILE A CG1 1 ATOM 4777 C CG2 . ILE A 1 617 ? -45.734 40.449 38.895 1.00 90.47 ? 617 ILE A CG2 1 ATOM 4778 C CD1 . ILE A 1 617 ? -45.435 43.408 38.349 1.00 114.13 ? 617 ILE A CD1 1 ATOM 4779 N N . TYR A 1 618 ? -43.530 40.841 42.881 1.00 100.51 ? 618 TYR A N 1 ATOM 4780 C CA . TYR A 1 618 ? -42.663 41.346 43.939 1.00 97.71 ? 618 TYR A CA 1 ATOM 4781 C C . TYR A 1 618 ? -41.494 42.171 43.398 1.00 96.52 ? 618 TYR A C 1 ATOM 4782 O O . TYR A 1 618 ? -41.042 41.970 42.271 1.00 102.43 ? 618 TYR A O 1 ATOM 4783 C CB . TYR A 1 618 ? -42.170 40.180 44.793 1.00 105.51 ? 618 TYR A CB 1 ATOM 4784 C CG . TYR A 1 618 ? -43.318 39.354 45.332 1.00 112.48 ? 618 TYR A CG 1 ATOM 4785 C CD1 . TYR A 1 618 ? -43.601 38.096 44.815 1.00 117.98 ? 618 TYR A CD1 1 ATOM 4786 C CD2 . TYR A 1 618 ? -44.143 39.850 46.332 1.00 115.04 ? 618 TYR A CD2 1 ATOM 4787 C CE1 . TYR A 1 618 ? -44.660 37.346 45.297 1.00 119.70 ? 618 TYR A CE1 1 ATOM 4788 C CE2 . TYR A 1 618 ? -45.203 39.109 46.821 1.00 114.72 ? 618 TYR A CE2 1 ATOM 4789 C CZ . TYR A 1 618 ? -45.457 37.858 46.300 1.00 115.10 ? 618 TYR A CZ 1 ATOM 4790 O OH . TYR A 1 618 ? -46.512 37.118 46.784 1.00 112.70 ? 618 TYR A OH 1 ATOM 4791 N N . ILE A 1 619 ? -41.020 43.103 44.221 1.00 98.08 ? 619 ILE A N 1 ATOM 4792 C CA . ILE A 1 619 ? -40.100 44.154 43.789 1.00 100.07 ? 619 ILE A CA 1 ATOM 4793 C C . ILE A 1 619 ? -38.735 43.679 43.291 1.00 110.67 ? 619 ILE A C 1 ATOM 4794 O O . ILE A 1 619 ? -38.356 43.951 42.152 1.00 129.67 ? 619 ILE A O 1 ATOM 4795 C CB . ILE A 1 619 ? -39.852 45.158 44.933 1.00 104.11 ? 619 ILE A CB 1 ATOM 4796 C CG1 . ILE A 1 619 ? -41.174 45.765 45.407 1.00 103.68 ? 619 ILE A CG1 1 ATOM 4797 C CG2 . ILE A 1 619 ? -38.891 46.248 44.487 1.00 113.55 ? 619 ILE A CG2 1 ATOM 4798 C CD1 . ILE A 1 619 ? -41.889 46.571 44.347 1.00 99.58 ? 619 ILE A CD1 1 ATOM 4799 N N . GLY A 1 620 ? -37.998 42.974 44.142 1.00 108.03 ? 620 GLY A N 1 ATOM 4800 C CA . GLY A 1 620 ? -36.606 42.674 43.859 1.00 114.18 ? 620 GLY A CA 1 ATOM 4801 C C . GLY A 1 620 ? -36.355 41.512 42.919 1.00 117.73 ? 620 GLY A C 1 ATOM 4802 O O . GLY A 1 620 ? -35.263 41.383 42.364 1.00 117.15 ? 620 GLY A O 1 ATOM 4803 N N . ASP A 1 621 ? -37.361 40.667 42.732 1.00 124.07 ? 621 ASP A N 1 ATOM 4804 C CA . ASP A 1 621 ? -37.190 39.452 41.946 1.00 123.17 ? 621 ASP A CA 1 ATOM 4805 C C . ASP A 1 621 ? -37.514 39.672 40.473 1.00 108.92 ? 621 ASP A C 1 ATOM 4806 O O . ASP A 1 621 ? -37.930 40.758 40.070 1.00 105.63 ? 621 ASP A O 1 ATOM 4807 C CB . ASP A 1 621 ? -38.077 38.338 42.510 1.00 131.51 ? 621 ASP A CB 1 ATOM 4808 C CG . ASP A 1 621 ? -37.551 36.952 42.197 1.00 148.80 ? 621 ASP A CG 1 ATOM 4809 O OD1 . ASP A 1 621 ? -36.316 36.770 42.197 1.00 158.46 ? 621 ASP A OD1 1 ATOM 4810 O OD2 . ASP A 1 621 ? -38.374 36.045 41.951 1.00 153.00 ? 621 ASP A OD2 1 ATOM 4811 N N . ASP A 1 622 ? -37.316 38.627 39.678 1.00 110.85 ? 622 ASP A N 1 ATOM 4812 C CA . ASP A 1 622 ? -37.806 38.588 38.309 1.00 121.62 ? 622 ASP A CA 1 ATOM 4813 C C . ASP A 1 622 ? -39.014 37.665 38.295 1.00 120.48 ? 622 ASP A C 1 ATOM 4814 O O . ASP A 1 622 ? -38.944 36.540 38.791 1.00 117.98 ? 622 ASP A O 1 ATOM 4815 C CB . ASP A 1 622 ? -36.727 38.101 37.342 1.00 133.63 ? 622 ASP A CB 1 ATOM 4816 C CG . ASP A 1 622 ? -35.504 38.997 37.334 1.00 133.77 ? 622 ASP A CG 1 ATOM 4817 O OD1 . ASP A 1 622 ? -35.651 40.210 37.597 1.00 133.99 ? 622 ASP A OD1 1 ATOM 4818 O OD2 . ASP A 1 622 ? -34.395 38.490 37.063 1.00 127.19 ? 622 ASP A OD2 1 ATOM 4819 N N . ASN A 1 623 ? -40.121 38.131 37.730 1.00 117.16 ? 623 ASN A N 1 ATOM 4820 C CA . ASN A 1 623 ? -41.380 37.417 37.881 1.00 117.38 ? 623 ASN A CA 1 ATOM 4821 C C . ASN A 1 623 ? -41.948 36.910 36.562 1.00 113.05 ? 623 ASN A C 1 ATOM 4822 O O . ASN A 1 623 ? -41.824 37.570 35.531 1.00 112.20 ? 623 ASN A O 1 ATOM 4823 C CB . ASN A 1 623 ? -42.406 38.319 38.572 1.00 125.68 ? 623 ASN A CB 1 ATOM 4824 C CG . ASN A 1 623 ? -41.885 38.903 39.872 1.00 127.80 ? 623 ASN A CG 1 ATOM 4825 O OD1 . ASN A 1 623 ? -41.879 40.120 40.062 1.00 119.97 ? 623 ASN A OD1 1 ATOM 4826 N ND2 . ASN A 1 623 ? -41.440 38.036 40.775 1.00 132.41 ? 623 ASN A ND2 1 ATOM 4827 N N . PRO A 1 624 ? -42.576 35.725 36.599 1.00 115.45 ? 624 PRO A N 1 ATOM 4828 C CA . PRO A 1 624 ? -43.212 35.116 35.429 1.00 127.19 ? 624 PRO A CA 1 ATOM 4829 C C . PRO A 1 624 ? -44.596 35.699 35.166 1.00 131.82 ? 624 PRO A C 1 ATOM 4830 O O . PRO A 1 624 ? -45.601 35.014 35.354 1.00 145.25 ? 624 PRO A O 1 ATOM 4831 C CB . PRO A 1 624 ? -43.303 33.640 35.814 1.00 135.45 ? 624 PRO A CB 1 ATOM 4832 C CG . PRO A 1 624 ? -43.437 33.663 37.297 1.00 132.15 ? 624 PRO A CG 1 ATOM 4833 C CD . PRO A 1 624 ? -42.617 34.834 37.773 1.00 120.69 ? 624 PRO A CD 1 ATOM 4834 N N . LEU A 1 625 ? -44.640 36.954 34.735 1.00 120.73 ? 625 LEU A N 1 ATOM 4835 C CA . LEU A 1 625 ? -45.907 37.622 34.472 1.00 111.51 ? 625 LEU A CA 1 ATOM 4836 C C . LEU A 1 625 ? -46.478 37.191 33.127 1.00 103.37 ? 625 LEU A C 1 ATOM 4837 O O . LEU A 1 625 ? -45.843 37.365 32.088 1.00 102.59 ? 625 LEU A O 1 ATOM 4838 C CB . LEU A 1 625 ? -45.732 39.141 34.509 1.00 109.34 ? 625 LEU A CB 1 ATOM 4839 C CG . LEU A 1 625 ? -46.995 39.969 34.269 1.00 107.12 ? 625 LEU A CG 1 ATOM 4840 C CD1 . LEU A 1 625 ? -48.047 39.665 35.325 1.00 108.42 ? 625 LEU A CD1 1 ATOM 4841 C CD2 . LEU A 1 625 ? -46.667 41.454 34.245 1.00 111.03 ? 625 LEU A CD2 1 ATOM 4842 N N . THR A 1 626 ? -47.681 36.630 33.156 1.00 99.22 ? 626 THR A N 1 ATOM 4843 C CA . THR A 1 626 ? -48.341 36.171 31.941 1.00 95.27 ? 626 THR A CA 1 ATOM 4844 C C . THR A 1 626 ? -49.670 36.892 31.747 1.00 100.89 ? 626 THR A C 1 ATOM 4845 O O . THR A 1 626 ? -50.474 36.988 32.674 1.00 112.11 ? 626 THR A O 1 ATOM 4846 C CB . THR A 1 626 ? -48.587 34.651 31.968 1.00 94.46 ? 626 THR A CB 1 ATOM 4847 O OG1 . THR A 1 626 ? -47.369 33.972 32.294 1.00 105.93 ? 626 THR A OG1 1 ATOM 4848 C CG2 . THR A 1 626 ? -49.088 34.166 30.615 1.00 92.34 ? 626 THR A CG2 1 ATOM 4849 N N . LEU A 1 627 ? -49.893 37.402 30.541 1.00 91.77 ? 627 LEU A N 1 ATOM 4850 C CA . LEU A 1 627 ? -51.127 38.111 30.233 1.00 89.78 ? 627 LEU A CA 1 ATOM 4851 C C . LEU A 1 627 ? -51.943 37.370 29.181 1.00 87.90 ? 627 LEU A C 1 ATOM 4852 O O . LEU A 1 627 ? -51.482 37.158 28.059 1.00 92.63 ? 627 LEU A O 1 ATOM 4853 C CB . LEU A 1 627 ? -50.824 39.533 29.758 1.00 88.35 ? 627 LEU A CB 1 ATOM 4854 C CG . LEU A 1 627 ? -50.086 40.427 30.757 1.00 95.41 ? 627 LEU A CG 1 ATOM 4855 C CD1 . LEU A 1 627 ? -49.971 41.850 30.229 1.00 87.24 ? 627 LEU A CD1 1 ATOM 4856 C CD2 . LEU A 1 627 ? -50.780 40.406 32.111 1.00 119.13 ? 627 LEU A CD2 1 ATOM 4857 N N . ILE A 1 628 ? -53.155 36.972 29.553 1.00 88.01 ? 628 ILE A N 1 ATOM 4858 C CA . ILE A 1 628 ? -54.058 36.297 28.630 1.00 88.67 ? 628 ILE A CA 1 ATOM 4859 C C . ILE A 1 628 ? -54.899 37.321 27.879 1.00 100.00 ? 628 ILE A C 1 ATOM 4860 O O . ILE A 1 628 ? -55.623 38.105 28.491 1.00 111.84 ? 628 ILE A O 1 ATOM 4861 C CB . ILE A 1 628 ? -54.985 35.311 29.363 1.00 91.48 ? 628 ILE A CB 1 ATOM 4862 C CG1 . ILE A 1 628 ? -54.162 34.315 30.183 1.00 91.29 ? 628 ILE A CG1 1 ATOM 4863 C CG2 . ILE A 1 628 ? -55.882 34.586 28.372 1.00 98.84 ? 628 ILE A CG2 1 ATOM 4864 C CD1 . ILE A 1 628 ? -53.183 33.509 29.359 1.00 90.31 ? 628 ILE A CD1 1 ATOM 4865 N N . VAL A 1 629 ? -54.801 37.314 26.553 1.00 97.76 ? 629 VAL A N 1 ATOM 4866 C CA . VAL A 1 629 ? -55.508 38.300 25.744 1.00 93.43 ? 629 VAL A CA 1 ATOM 4867 C C . VAL A 1 629 ? -56.638 37.681 24.926 1.00 92.26 ? 629 VAL A C 1 ATOM 4868 O O . VAL A 1 629 ? -56.525 36.563 24.423 1.00 90.67 ? 629 VAL A O 1 ATOM 4869 C CB . VAL A 1 629 ? -54.544 39.042 24.790 1.00 90.37 ? 629 VAL A CB 1 ATOM 4870 C CG1 . VAL A 1 629 ? -53.535 39.854 25.586 1.00 95.06 ? 629 VAL A CG1 1 ATOM 4871 C CG2 . VAL A 1 629 ? -53.835 38.065 23.867 1.00 87.28 ? 629 VAL A CG2 1 ATOM 4872 N N . LYS A 1 630 ? -57.737 38.420 24.814 1.00 97.31 ? 630 LYS A N 1 ATOM 4873 C CA . LYS A 1 630 ? -58.873 38.002 24.005 1.00 99.65 ? 630 LYS A CA 1 ATOM 4874 C C . LYS A 1 630 ? -59.041 38.957 22.829 1.00 109.03 ? 630 LYS A C 1 ATOM 4875 O O . LYS A 1 630 ? -59.437 40.107 23.009 1.00 116.03 ? 630 LYS A O 1 ATOM 4876 C CB . LYS A 1 630 ? -60.148 37.963 24.850 1.00 96.49 ? 630 LYS A CB 1 ATOM 4877 C CG . LYS A 1 630 ? -61.373 37.415 24.136 1.00 97.04 ? 630 LYS A CG 1 ATOM 4878 C CD . LYS A 1 630 ? -61.366 35.896 24.111 1.00 104.85 ? 630 LYS A CD 1 ATOM 4879 C CE . LYS A 1 630 ? -62.691 35.341 23.615 1.00 111.75 ? 630 LYS A CE 1 ATOM 4880 N NZ . LYS A 1 630 ? -62.727 33.853 23.678 1.00 105.47 ? 630 LYS A NZ 1 ATOM 4881 N N . ALA A 1 631 ? -58.741 38.477 21.627 1.00 108.66 ? 631 ALA A N 1 ATOM 4882 C CA . ALA A 1 631 ? -58.845 39.305 20.431 1.00 105.75 ? 631 ALA A CA 1 ATOM 4883 C C . ALA A 1 631 ? -60.072 38.920 19.616 1.00 117.09 ? 631 ALA A C 1 ATOM 4884 O O . ALA A 1 631 ? -60.170 37.799 19.119 1.00 132.61 ? 631 ALA A O 1 ATOM 4885 C CB . ALA A 1 631 ? -57.587 39.184 19.587 1.00 97.18 ? 631 ALA A CB 1 ATOM 4886 N N . GLN A 1 632 ? -61.007 39.855 19.482 1.00 106.39 ? 632 GLN A N 1 ATOM 4887 C CA . GLN A 1 632 ? -62.251 39.586 18.772 1.00 97.27 ? 632 GLN A CA 1 ATOM 4888 C C . GLN A 1 632 ? -62.490 40.559 17.626 1.00 99.38 ? 632 GLN A C 1 ATOM 4889 O O . GLN A 1 632 ? -62.321 41.768 17.780 1.00 116.23 ? 632 GLN A O 1 ATOM 4890 C CB . GLN A 1 632 ? -63.439 39.642 19.736 1.00 97.98 ? 632 GLN A CB 1 ATOM 4891 C CG . GLN A 1 632 ? -63.343 38.698 20.919 1.00 99.91 ? 632 GLN A CG 1 ATOM 4892 C CD . GLN A 1 632 ? -64.555 38.789 21.826 1.00 116.13 ? 632 GLN A CD 1 ATOM 4893 O OE1 . GLN A 1 632 ? -65.565 39.398 21.472 1.00 110.84 ? 632 GLN A OE1 1 ATOM 4894 N NE2 . GLN A 1 632 ? -64.461 38.183 23.004 1.00 133.43 ? 632 GLN A NE2 1 ATOM 4895 N N . ASN A 1 633 ? -62.882 40.024 16.474 1.00 91.44 ? 633 ASN A N 1 ATOM 4896 C CA . ASN A 1 633 ? -63.396 40.853 15.395 1.00 90.34 ? 633 ASN A CA 1 ATOM 4897 C C . ASN A 1 633 ? -64.867 40.537 15.164 1.00 92.34 ? 633 ASN A C 1 ATOM 4898 O O . ASN A 1 633 ? -65.209 39.476 14.643 1.00 93.99 ? 633 ASN A O 1 ATOM 4899 C CB . ASN A 1 633 ? -62.596 40.643 14.109 1.00 90.56 ? 633 ASN A CB 1 ATOM 4900 C CG . ASN A 1 633 ? -63.037 41.569 12.991 1.00 93.62 ? 633 ASN A CG 1 ATOM 4901 O OD1 . ASN A 1 633 ? -63.658 42.604 13.235 1.00 93.68 ? 633 ASN A OD1 1 ATOM 4902 N ND2 . ASN A 1 633 ? -62.717 41.201 11.756 1.00 95.08 ? 633 ASN A ND2 1 ATOM 4903 N N . GLN A 1 634 ? -65.736 41.461 15.558 1.00 94.91 ? 634 GLN A N 1 ATOM 4904 C CA . GLN A 1 634 ? -67.172 41.256 15.424 1.00 104.77 ? 634 GLN A CA 1 ATOM 4905 C C . GLN A 1 634 ? -67.709 41.917 14.161 1.00 106.19 ? 634 GLN A C 1 ATOM 4906 O O . GLN A 1 634 ? -68.895 41.815 13.851 1.00 119.16 ? 634 GLN A O 1 ATOM 4907 C CB . GLN A 1 634 ? -67.906 41.790 16.656 1.00 112.41 ? 634 GLN A CB 1 ATOM 4908 C CG . GLN A 1 634 ? -67.374 41.247 17.976 1.00 110.38 ? 634 GLN A CG 1 ATOM 4909 C CD . GLN A 1 634 ? -67.434 39.732 18.058 1.00 111.26 ? 634 GLN A CD 1 ATOM 4910 O OE1 . GLN A 1 634 ? -66.538 39.095 18.611 1.00 105.50 ? 634 GLN A OE1 1 ATOM 4911 N NE2 . GLN A 1 634 ? -68.498 39.149 17.516 1.00 115.34 ? 634 GLN A NE2 1 ATOM 4912 N N . GLY A 1 635 ? -66.827 42.596 13.436 1.00 97.44 ? 635 GLY A N 1 ATOM 4913 C CA . GLY A 1 635 ? -67.205 43.257 12.203 1.00 107.00 ? 635 GLY A CA 1 ATOM 4914 C C . GLY A 1 635 ? -66.674 42.538 10.980 1.00 111.99 ? 635 GLY A C 1 ATOM 4915 O O . GLY A 1 635 ? -66.241 41.390 11.063 1.00 105.80 ? 635 GLY A O 1 ATOM 4916 N N . GLU A 1 636 ? -66.701 43.223 9.843 1.00 114.06 ? 636 GLU A N 1 ATOM 4917 C CA . GLU A 1 636 ? -66.216 42.664 8.587 1.00 103.57 ? 636 GLU A CA 1 ATOM 4918 C C . GLU A 1 636 ? -64.701 42.473 8.642 1.00 90.31 ? 636 GLU A C 1 ATOM 4919 O O . GLU A 1 636 ? -64.033 43.055 9.493 1.00 86.77 ? 636 GLU A O 1 ATOM 4920 C CB . GLU A 1 636 ? -66.621 43.567 7.418 1.00 102.07 ? 636 GLU A CB 1 ATOM 4921 C CG . GLU A 1 636 ? -68.127 43.815 7.352 1.00 117.58 ? 636 GLU A CG 1 ATOM 4922 C CD . GLU A 1 636 ? -68.534 44.785 6.256 1.00 133.54 ? 636 GLU A CD 1 ATOM 4923 O OE1 . GLU A 1 636 ? -69.712 45.200 6.235 1.00 131.72 ? 636 GLU A OE1 1 ATOM 4924 O OE2 . GLU A 1 636 ? -67.683 45.132 5.414 1.00 144.25 ? 636 GLU A OE2 1 ATOM 4925 N N . GLY A 1 637 ? -64.171 41.637 7.753 1.00 84.60 ? 637 GLY A N 1 ATOM 4926 C CA . GLY A 1 637 ? -62.763 41.270 7.771 1.00 84.24 ? 637 GLY A CA 1 ATOM 4927 C C . GLY A 1 637 ? -61.778 42.426 7.828 1.00 82.24 ? 637 GLY A C 1 ATOM 4928 O O . GLY A 1 637 ? -61.893 43.393 7.076 1.00 81.55 ? 637 GLY A O 1 ATOM 4929 N N . ALA A 1 638 ? -60.803 42.318 8.726 1.00 74.68 ? 638 ALA A N 1 ATOM 4930 C CA . ALA A 1 638 ? -59.801 43.363 8.910 1.00 73.45 ? 638 ALA A CA 1 ATOM 4931 C C . ALA A 1 638 ? -58.458 42.963 8.308 1.00 74.19 ? 638 ALA A C 1 ATOM 4932 O O . ALA A 1 638 ? -57.852 41.976 8.723 1.00 74.53 ? 638 ALA A O 1 ATOM 4933 C CB . ALA A 1 638 ? -59.641 43.685 10.386 1.00 72.26 ? 638 ALA A CB 1 ATOM 4934 N N . TYR A 1 639 ? -57.994 43.742 7.335 1.00 82.54 ? 639 TYR A N 1 ATOM 4935 C CA . TYR A 1 639 ? -56.733 43.459 6.657 1.00 81.16 ? 639 TYR A CA 1 ATOM 4936 C C . TYR A 1 639 ? -55.528 43.738 7.549 1.00 74.51 ? 639 TYR A C 1 ATOM 4937 O O . TYR A 1 639 ? -55.492 44.746 8.254 1.00 72.41 ? 639 TYR A O 1 ATOM 4938 C CB . TYR A 1 639 ? -56.613 44.286 5.375 1.00 82.57 ? 639 TYR A CB 1 ATOM 4939 C CG . TYR A 1 639 ? -57.824 44.225 4.475 1.00 86.67 ? 639 TYR A CG 1 ATOM 4940 C CD1 . TYR A 1 639 ? -58.041 43.137 3.642 1.00 90.63 ? 639 TYR A CD1 1 ATOM 4941 C CD2 . TYR A 1 639 ? -58.745 45.263 4.450 1.00 88.37 ? 639 TYR A CD2 1 ATOM 4942 C CE1 . TYR A 1 639 ? -59.146 43.081 2.814 1.00 98.83 ? 639 TYR A CE1 1 ATOM 4943 C CE2 . TYR A 1 639 ? -59.852 45.217 3.627 1.00 88.43 ? 639 TYR A CE2 1 ATOM 4944 C CZ . TYR A 1 639 ? -60.047 44.124 2.811 1.00 92.65 ? 639 TYR A CZ 1 ATOM 4945 O OH . TYR A 1 639 ? -61.149 44.074 1.988 1.00 97.53 ? 639 TYR A OH 1 ATOM 4946 N N . GLU A 1 640 ? -54.548 42.839 7.500 1.00 78.01 ? 640 GLU A N 1 ATOM 4947 C CA . GLU A 1 640 ? -53.279 43.001 8.210 1.00 83.44 ? 640 GLU A CA 1 ATOM 4948 C C . GLU A 1 640 ? -53.467 43.328 9.688 1.00 86.88 ? 640 GLU A C 1 ATOM 4949 O O . GLU A 1 640 ? -52.829 44.239 10.216 1.00 86.71 ? 640 GLU A O 1 ATOM 4950 C CB . GLU A 1 640 ? -52.435 44.089 7.543 1.00 83.80 ? 640 GLU A CB 1 ATOM 4951 C CG . GLU A 1 640 ? -52.160 43.845 6.069 1.00 94.99 ? 640 GLU A CG 1 ATOM 4952 C CD . GLU A 1 640 ? -51.268 44.907 5.458 1.00 106.22 ? 640 GLU A CD 1 ATOM 4953 O OE1 . GLU A 1 640 ? -51.149 44.942 4.215 1.00 114.63 ? 640 GLU A OE1 1 ATOM 4954 O OE2 . GLU A 1 640 ? -50.683 45.705 6.221 1.00 105.00 ? 640 GLU A OE2 1 ATOM 4955 N N . ALA A 1 641 ? -54.346 42.583 10.349 1.00 90.23 ? 641 ALA A N 1 ATOM 4956 C CA . ALA A 1 641 ? -54.622 42.805 11.762 1.00 89.04 ? 641 ALA A CA 1 ATOM 4957 C C . ALA A 1 641 ? -53.404 42.477 12.617 1.00 75.13 ? 641 ALA A C 1 ATOM 4958 O O . ALA A 1 641 ? -52.756 41.449 12.424 1.00 75.22 ? 641 ALA A O 1 ATOM 4959 C CB . ALA A 1 641 ? -55.815 41.978 12.205 1.00 104.24 ? 641 ALA A CB 1 ATOM 4960 N N . GLU A 1 642 ? -53.097 43.362 13.558 1.00 75.78 ? 642 GLU A N 1 ATOM 4961 C CA . GLU A 1 642 ? -51.972 43.157 14.461 1.00 78.34 ? 642 GLU A CA 1 ATOM 4962 C C . GLU A 1 642 ? -52.325 43.554 15.889 1.00 79.37 ? 642 GLU A C 1 ATOM 4963 O O . GLU A 1 642 ? -53.004 44.555 16.117 1.00 75.91 ? 642 GLU A O 1 ATOM 4964 C CB . GLU A 1 642 ? -50.748 43.945 13.988 1.00 83.25 ? 642 GLU A CB 1 ATOM 4965 C CG . GLU A 1 642 ? -50.059 43.357 12.767 1.00 102.52 ? 642 GLU A CG 1 ATOM 4966 C CD . GLU A 1 642 ? -48.842 44.156 12.344 1.00 119.85 ? 642 GLU A CD 1 ATOM 4967 O OE1 . GLU A 1 642 ? -48.719 45.325 12.768 1.00 120.85 ? 642 GLU A OE1 1 ATOM 4968 O OE2 . GLU A 1 642 ? -48.006 43.614 11.590 1.00 126.92 ? 642 GLU A OE2 1 ATOM 4969 N N . LEU A 1 643 ? -51.866 42.755 16.846 1.00 85.82 ? 643 LEU A N 1 ATOM 4970 C CA . LEU A 1 643 ? -52.055 43.066 18.257 1.00 80.99 ? 643 LEU A CA 1 ATOM 4971 C C . LEU A 1 643 ? -50.865 43.853 18.787 1.00 71.52 ? 643 LEU A C 1 ATOM 4972 O O . LEU A 1 643 ? -49.743 43.349 18.819 1.00 71.71 ? 643 LEU A O 1 ATOM 4973 C CB . LEU A 1 643 ? -52.248 41.789 19.074 1.00 78.00 ? 643 LEU A CB 1 ATOM 4974 C CG . LEU A 1 643 ? -52.265 41.984 20.592 1.00 81.43 ? 643 LEU A CG 1 ATOM 4975 C CD1 . LEU A 1 643 ? -53.434 42.863 21.013 1.00 85.69 ? 643 LEU A CD1 1 ATOM 4976 C CD2 . LEU A 1 643 ? -52.307 40.645 21.312 1.00 81.75 ? 643 LEU A CD2 1 ATOM 4977 N N . ILE A 1 644 ? -51.113 45.089 19.203 1.00 70.42 ? 644 ILE A N 1 ATOM 4978 C CA . ILE A 1 644 ? -50.047 45.948 19.699 1.00 73.48 ? 644 ILE A CA 1 ATOM 4979 C C . ILE A 1 644 ? -49.979 45.927 21.221 1.00 84.28 ? 644 ILE A C 1 ATOM 4980 O O . ILE A 1 644 ? -50.895 46.385 21.903 1.00 94.34 ? 644 ILE A O 1 ATOM 4981 C CB . ILE A 1 644 ? -50.225 47.399 19.221 1.00 77.26 ? 644 ILE A CB 1 ATOM 4982 C CG1 . ILE A 1 644 ? -50.368 47.443 17.699 1.00 78.38 ? 644 ILE A CG1 1 ATOM 4983 C CG2 . ILE A 1 644 ? -49.056 48.258 19.679 1.00 81.59 ? 644 ILE A CG2 1 ATOM 4984 C CD1 . ILE A 1 644 ? -49.204 46.824 16.958 1.00 72.29 ? 644 ILE A CD1 1 ATOM 4985 N N . VAL A 1 645 ? -48.883 45.389 21.745 1.00 84.26 ? 645 VAL A N 1 ATOM 4986 C CA . VAL A 1 645 ? -48.664 45.323 23.183 1.00 80.79 ? 645 VAL A CA 1 ATOM 4987 C C . VAL A 1 645 ? -47.562 46.288 23.597 1.00 90.51 ? 645 VAL A C 1 ATOM 4988 O O . VAL A 1 645 ? -46.397 46.091 23.253 1.00 99.32 ? 645 VAL A O 1 ATOM 4989 C CB . VAL A 1 645 ? -48.285 43.901 23.633 1.00 79.87 ? 645 VAL A CB 1 ATOM 4990 C CG1 . VAL A 1 645 ? -48.023 43.870 25.130 1.00 84.89 ? 645 VAL A CG1 1 ATOM 4991 C CG2 . VAL A 1 645 ? -49.377 42.914 23.251 1.00 80.34 ? 645 VAL A CG2 1 ATOM 4992 N N . SER A 1 646 ? -47.928 47.327 24.340 1.00 94.12 ? 646 SER A N 1 ATOM 4993 C CA . SER A 1 646 ? -46.960 48.332 24.761 1.00 99.73 ? 646 SER A CA 1 ATOM 4994 C C . SER A 1 646 ? -46.381 47.994 26.129 1.00 118.23 ? 646 SER A C 1 ATOM 4995 O O . SER A 1 646 ? -47.083 48.041 27.139 1.00 134.45 ? 646 SER A O 1 ATOM 4996 C CB . SER A 1 646 ? -47.607 49.719 24.793 1.00 89.31 ? 646 SER A CB 1 ATOM 4997 O OG . SER A 1 646 ? -48.152 50.057 23.530 1.00 86.72 ? 646 SER A OG 1 ATOM 4998 N N . ILE A 1 647 ? -45.096 47.655 26.156 1.00 116.86 ? 647 ILE A N 1 ATOM 4999 C CA . ILE A 1 647 ? -44.423 47.322 27.405 1.00 118.19 ? 647 ILE A CA 1 ATOM 5000 C C . ILE A 1 647 ? -43.463 48.435 27.820 1.00 133.43 ? 647 ILE A C 1 ATOM 5001 O O . ILE A 1 647 ? -42.408 48.622 27.213 1.00 147.17 ? 647 ILE A O 1 ATOM 5002 C CB . ILE A 1 647 ? -43.662 45.984 27.296 1.00 112.78 ? 647 ILE A CB 1 ATOM 5003 C CG1 . ILE A 1 647 ? -42.907 45.891 25.968 1.00 114.84 ? 647 ILE A CG1 1 ATOM 5004 C CG2 . ILE A 1 647 ? -44.629 44.822 27.393 1.00 110.49 ? 647 ILE A CG2 1 ATOM 5005 C CD1 . ILE A 1 647 ? -42.093 44.627 25.824 1.00 114.64 ? 647 ILE A CD1 1 ATOM 5006 N N . PRO A 1 648 ? -43.838 49.192 28.860 1.00 135.14 ? 648 PRO A N 1 ATOM 5007 C CA . PRO A 1 648 ? -43.019 50.318 29.311 1.00 141.40 ? 648 PRO A CA 1 ATOM 5008 C C . PRO A 1 648 ? -41.776 49.898 30.090 1.00 131.90 ? 648 PRO A C 1 ATOM 5009 O O . PRO A 1 648 ? -41.837 48.966 30.893 1.00 121.75 ? 648 PRO A O 1 ATOM 5010 C CB . PRO A 1 648 ? -43.977 51.097 30.213 1.00 150.80 ? 648 PRO A CB 1 ATOM 5011 C CG . PRO A 1 648 ? -44.868 50.048 30.774 1.00 143.93 ? 648 PRO A CG 1 ATOM 5012 C CD . PRO A 1 648 ? -45.057 49.036 29.672 1.00 134.57 ? 648 PRO A CD 1 ATOM 5013 N N . LEU A 1 649 ? -40.669 50.592 29.840 1.00 134.18 ? 649 LEU A N 1 ATOM 5014 C CA . LEU A 1 649 ? -39.500 50.566 30.716 1.00 132.23 ? 649 LEU A CA 1 ATOM 5015 C C . LEU A 1 649 ? -38.965 49.172 31.042 1.00 125.82 ? 649 LEU A C 1 ATOM 5016 O O . LEU A 1 649 ? -38.542 48.428 30.157 1.00 121.83 ? 649 LEU A O 1 ATOM 5017 C CB . LEU A 1 649 ? -39.838 51.298 32.016 1.00 135.37 ? 649 LEU A CB 1 ATOM 5018 C CG . LEU A 1 649 ? -40.532 52.647 31.815 1.00 132.60 ? 649 LEU A CG 1 ATOM 5019 C CD1 . LEU A 1 649 ? -41.410 52.987 33.006 1.00 138.59 ? 649 LEU A CD1 1 ATOM 5020 C CD2 . LEU A 1 649 ? -39.510 53.745 31.565 1.00 128.31 ? 649 LEU A CD2 1 ATOM 5021 N N . GLN A 1 650 ? -38.991 48.842 32.331 1.00 128.45 ? 650 GLN A N 1 ATOM 5022 C CA . GLN A 1 650 ? -38.400 47.618 32.868 1.00 122.93 ? 650 GLN A CA 1 ATOM 5023 C C . GLN A 1 650 ? -38.924 46.331 32.234 1.00 120.14 ? 650 GLN A C 1 ATOM 5024 O O . GLN A 1 650 ? -38.235 45.311 32.232 1.00 117.14 ? 650 GLN A O 1 ATOM 5025 C CB . GLN A 1 650 ? -38.624 47.562 34.383 1.00 118.89 ? 650 GLN A CB 1 ATOM 5026 C CG . GLN A 1 650 ? -39.403 48.746 34.949 1.00 122.76 ? 650 GLN A CG 1 ATOM 5027 C CD . GLN A 1 650 ? -40.892 48.673 34.664 1.00 106.93 ? 650 GLN A CD 1 ATOM 5028 O OE1 . GLN A 1 650 ? -41.423 47.612 34.337 1.00 100.48 ? 650 GLN A OE1 1 ATOM 5029 N NE2 . GLN A 1 650 ? -41.573 49.807 34.784 1.00 101.27 ? 650 GLN A NE2 1 ATOM 5030 N N . ALA A 1 651 ? -40.141 46.378 31.704 1.00 120.70 ? 651 ALA A N 1 ATOM 5031 C CA . ALA A 1 651 ? -40.755 45.195 31.110 1.00 111.13 ? 651 ALA A CA 1 ATOM 5032 C C . ALA A 1 651 ? -40.051 44.780 29.822 1.00 104.76 ? 651 ALA A C 1 ATOM 5033 O O . ALA A 1 651 ? -39.821 45.602 28.937 1.00 104.25 ? 651 ALA A O 1 ATOM 5034 C CB . ALA A 1 651 ? -42.232 45.446 30.845 1.00 111.45 ? 651 ALA A CB 1 ATOM 5035 N N . ASP A 1 652 ? -39.707 43.499 29.726 1.00 105.94 ? 652 ASP A N 1 ATOM 5036 C CA . ASP A 1 652 ? -39.123 42.954 28.505 1.00 113.79 ? 652 ASP A CA 1 ATOM 5037 C C . ASP A 1 652 ? -39.812 41.648 28.120 1.00 114.33 ? 652 ASP A C 1 ATOM 5038 O O . ASP A 1 652 ? -40.172 40.843 28.979 1.00 106.79 ? 652 ASP A O 1 ATOM 5039 C CB . ASP A 1 652 ? -37.615 42.741 28.667 1.00 125.80 ? 652 ASP A CB 1 ATOM 5040 C CG . ASP A 1 652 ? -37.276 41.763 29.773 1.00 133.53 ? 652 ASP A CG 1 ATOM 5041 O OD1 . ASP A 1 652 ? -38.050 41.673 30.747 1.00 137.04 ? 652 ASP A OD1 1 ATOM 5042 O OD2 . ASP A 1 652 ? -36.231 41.086 29.669 1.00 133.44 ? 652 ASP A OD2 1 ATOM 5043 N N . PHE A 1 653 ? -39.994 41.450 26.818 1.00 119.99 ? 653 PHE A N 1 ATOM 5044 C CA . PHE A 1 653 ? -40.736 40.306 26.298 1.00 112.54 ? 653 PHE A CA 1 ATOM 5045 C C . PHE A 1 653 ? -39.951 39.004 26.423 1.00 111.47 ? 653 PHE A C 1 ATOM 5046 O O . PHE A 1 653 ? -38.739 38.975 26.212 1.00 120.00 ? 653 PHE A O 1 ATOM 5047 C CB . PHE A 1 653 ? -41.114 40.557 24.836 1.00 106.24 ? 653 PHE A CB 1 ATOM 5048 C CG . PHE A 1 653 ? -41.961 39.477 24.228 1.00 102.76 ? 653 PHE A CG 1 ATOM 5049 C CD1 . PHE A 1 653 ? -43.298 39.352 24.568 1.00 100.20 ? 653 PHE A CD1 1 ATOM 5050 C CD2 . PHE A 1 653 ? -41.427 38.599 23.300 1.00 110.20 ? 653 PHE A CD2 1 ATOM 5051 C CE1 . PHE A 1 653 ? -44.082 38.364 24.005 1.00 102.42 ? 653 PHE A CE1 1 ATOM 5052 C CE2 . PHE A 1 653 ? -42.206 37.610 22.732 1.00 112.15 ? 653 PHE A CE2 1 ATOM 5053 C CZ . PHE A 1 653 ? -43.536 37.493 23.085 1.00 105.61 ? 653 PHE A CZ 1 ATOM 5054 N N . ILE A 1 654 ? -40.651 37.928 26.773 1.00 105.85 ? 654 ILE A N 1 ATOM 5055 C CA . ILE A 1 654 ? -40.035 36.609 26.865 1.00 111.26 ? 654 ILE A CA 1 ATOM 5056 C C . ILE A 1 654 ? -40.441 35.739 25.679 1.00 115.84 ? 654 ILE A C 1 ATOM 5057 O O . ILE A 1 654 ? -39.602 35.364 24.859 1.00 123.10 ? 654 ILE A O 1 ATOM 5058 C CB . ILE A 1 654 ? -40.413 35.889 28.174 1.00 115.33 ? 654 ILE A CB 1 ATOM 5059 C CG1 . ILE A 1 654 ? -39.896 36.672 29.382 1.00 122.21 ? 654 ILE A CG1 1 ATOM 5060 C CG2 . ILE A 1 654 ? -39.857 34.472 28.184 1.00 113.01 ? 654 ILE A CG2 1 ATOM 5061 C CD1 . ILE A 1 654 ? -40.103 35.963 30.704 1.00 123.65 ? 654 ILE A CD1 1 ATOM 5062 N N . GLY A 1 655 ? -41.729 35.423 25.590 1.00 116.14 ? 655 GLY A N 1 ATOM 5063 C CA . GLY A 1 655 ? -42.229 34.594 24.510 1.00 121.17 ? 655 GLY A CA 1 ATOM 5064 C C . GLY A 1 655 ? -43.732 34.392 24.540 1.00 109.82 ? 655 GLY A C 1 ATOM 5065 O O . GLY A 1 655 ? -44.461 35.131 25.202 1.00 100.24 ? 655 GLY A O 1 ATOM 5066 N N . VAL A 1 656 ? -44.192 33.381 23.810 1.00 106.94 ? 656 VAL A N 1 ATOM 5067 C CA . VAL A 1 656 ? -45.606 33.031 23.760 1.00 106.98 ? 656 VAL A CA 1 ATOM 5068 C C . VAL A 1 656 ? -45.761 31.609 24.291 1.00 115.08 ? 656 VAL A C 1 ATOM 5069 O O . VAL A 1 656 ? -44.794 30.848 24.315 1.00 127.47 ? 656 VAL A O 1 ATOM 5070 C CB . VAL A 1 656 ? -46.170 33.135 22.327 1.00 105.65 ? 656 VAL A CB 1 ATOM 5071 C CG1 . VAL A 1 656 ? -47.688 33.241 22.352 1.00 106.23 ? 656 VAL A CG1 1 ATOM 5072 C CG2 . VAL A 1 656 ? -45.575 34.338 21.612 1.00 110.95 ? 656 VAL A CG2 1 ATOM 5073 N N . VAL A 1 657 ? -46.967 31.244 24.716 1.00 115.94 ? 657 VAL A N 1 ATOM 5074 C CA . VAL A 1 657 ? -47.168 29.945 25.346 1.00 129.11 ? 657 VAL A CA 1 ATOM 5075 C C . VAL A 1 657 ? -47.557 28.875 24.329 1.00 129.76 ? 657 VAL A C 1 ATOM 5076 O O . VAL A 1 657 ? -48.664 28.869 23.790 1.00 128.01 ? 657 VAL A O 1 ATOM 5077 C CB . VAL A 1 657 ? -48.249 30.025 26.440 1.00 123.45 ? 657 VAL A CB 1 ATOM 5078 C CG1 . VAL A 1 657 ? -47.654 30.538 27.738 1.00 116.52 ? 657 VAL A CG1 1 ATOM 5079 C CG2 . VAL A 1 657 ? -49.387 30.922 25.990 1.00 118.82 ? 657 VAL A CG2 1 ATOM 5080 N N . ARG A 1 658 ? -46.620 27.969 24.072 1.00 123.23 ? 658 ARG A N 1 ATOM 5081 C CA . ARG A 1 658 ? -46.838 26.853 23.162 1.00 129.11 ? 658 ARG A CA 1 ATOM 5082 C C . ARG A 1 658 ? -47.520 25.674 23.854 1.00 136.53 ? 658 ARG A C 1 ATOM 5083 O O . ARG A 1 658 ? -48.294 24.942 23.236 1.00 140.20 ? 658 ARG A O 1 ATOM 5084 C CB . ARG A 1 658 ? -45.507 26.415 22.548 1.00 137.54 ? 658 ARG A CB 1 ATOM 5085 C CG . ARG A 1 658 ? -44.724 27.567 21.931 1.00 137.83 ? 658 ARG A CG 1 ATOM 5086 C CD . ARG A 1 658 ? -43.406 27.105 21.332 1.00 148.50 ? 658 ARG A CD 1 ATOM 5087 N NE . ARG A 1 658 ? -42.631 28.225 20.804 1.00 141.64 ? 658 ARG A NE 1 ATOM 5088 C CZ . ARG A 1 658 ? -42.744 28.695 19.566 1.00 131.07 ? 658 ARG A CZ 1 ATOM 5089 N NH1 . ARG A 1 658 ? -43.603 28.144 18.720 1.00 130.06 ? 658 ARG A NH1 1 ATOM 5090 N NH2 . ARG A 1 658 ? -41.997 29.718 19.173 1.00 122.56 ? 658 ARG A NH2 1 ATOM 5091 N N . ASN A 1 659 ? -47.223 25.501 25.138 1.00 137.07 ? 659 ASN A N 1 ATOM 5092 C CA . ASN A 1 659 ? -47.654 24.325 25.889 1.00 134.24 ? 659 ASN A CA 1 ATOM 5093 C C . ASN A 1 659 ? -49.167 24.203 26.057 1.00 129.82 ? 659 ASN A C 1 ATOM 5094 O O . ASN A 1 659 ? -49.702 23.095 26.096 1.00 130.70 ? 659 ASN A O 1 ATOM 5095 C CB . ASN A 1 659 ? -46.992 24.317 27.269 1.00 126.37 ? 659 ASN A CB 1 ATOM 5096 C CG . ASN A 1 659 ? -47.365 25.528 28.103 1.00 113.79 ? 659 ASN A CG 1 ATOM 5097 O OD1 . ASN A 1 659 ? -47.552 26.625 27.577 1.00 110.88 ? 659 ASN A OD1 1 ATOM 5098 N ND2 . ASN A 1 659 ? -47.479 25.333 29.412 1.00 113.25 ? 659 ASN A ND2 1 ATOM 5099 N N . ASN A 1 660 ? -49.855 25.335 26.157 1.00 123.36 ? 660 ASN A N 1 ATOM 5100 C CA . ASN A 1 660 ? -51.295 25.321 26.389 1.00 122.97 ? 660 ASN A CA 1 ATOM 5101 C C . ASN A 1 660 ? -52.083 25.059 25.109 1.00 117.90 ? 660 ASN A C 1 ATOM 5102 O O . ASN A 1 660 ? -51.823 25.666 24.070 1.00 111.43 ? 660 ASN A O 1 ATOM 5103 C CB . ASN A 1 660 ? -51.747 26.639 27.023 1.00 124.79 ? 660 ASN A CB 1 ATOM 5104 C CG . ASN A 1 660 ? -53.119 26.539 27.671 1.00 120.87 ? 660 ASN A CG 1 ATOM 5105 O OD1 . ASN A 1 660 ? -54.009 25.848 27.174 1.00 110.06 ? 660 ASN A OD1 1 ATOM 5106 N ND2 . ASN A 1 660 ? -53.294 27.231 28.791 1.00 123.86 ? 660 ASN A ND2 1 ATOM 5107 N N . GLU A 1 661 ? -53.048 24.149 25.199 1.00 123.24 ? 661 GLU A N 1 ATOM 5108 C CA . GLU A 1 661 ? -53.918 23.823 24.076 1.00 129.78 ? 661 GLU A CA 1 ATOM 5109 C C . GLU A 1 661 ? -55.001 24.884 23.905 1.00 120.17 ? 661 GLU A C 1 ATOM 5110 O O . GLU A 1 661 ? -55.421 25.187 22.787 1.00 114.42 ? 661 GLU A O 1 ATOM 5111 C CB . GLU A 1 661 ? -54.552 22.444 24.277 1.00 138.13 ? 661 GLU A CB 1 ATOM 5112 C CG . GLU A 1 661 ? -55.507 22.016 23.171 1.00 145.15 ? 661 GLU A CG 1 ATOM 5113 C CD . GLU A 1 661 ? -54.794 21.684 21.874 1.00 155.40 ? 661 GLU A CD 1 ATOM 5114 O OE1 . GLU A 1 661 ? -53.574 21.420 21.912 1.00 160.89 ? 661 GLU A OE1 1 ATOM 5115 O OE2 . GLU A 1 661 ? -55.456 21.686 20.814 1.00 157.26 ? 661 GLU A OE2 1 ATOM 5116 N N . ALA A 1 662 ? -55.442 25.450 25.024 1.00 112.16 ? 662 ALA A N 1 ATOM 5117 C CA . ALA A 1 662 ? -56.493 26.463 25.021 1.00 109.83 ? 662 ALA A CA 1 ATOM 5118 C C . ALA A 1 662 ? -55.977 27.815 24.538 1.00 115.44 ? 662 ALA A C 1 ATOM 5119 O O . ALA A 1 662 ? -56.748 28.761 24.377 1.00 114.72 ? 662 ALA A O 1 ATOM 5120 C CB . ALA A 1 662 ? -57.099 26.597 26.410 1.00 110.39 ? 662 ALA A CB 1 ATOM 5121 N N . LEU A 1 663 ? -54.671 27.901 24.304 1.00 115.96 ? 663 LEU A N 1 ATOM 5122 C CA . LEU A 1 663 ? -54.045 29.161 23.924 1.00 105.61 ? 663 LEU A CA 1 ATOM 5123 C C . LEU A 1 663 ? -53.376 29.068 22.556 1.00 106.80 ? 663 LEU A C 1 ATOM 5124 O O . LEU A 1 663 ? -53.123 27.975 22.049 1.00 106.27 ? 663 LEU A O 1 ATOM 5125 C CB . LEU A 1 663 ? -53.035 29.594 24.988 1.00 97.08 ? 663 LEU A CB 1 ATOM 5126 C CG . LEU A 1 663 ? -53.679 29.988 26.320 1.00 91.68 ? 663 LEU A CG 1 ATOM 5127 C CD1 . LEU A 1 663 ? -52.635 30.365 27.357 1.00 90.52 ? 663 LEU A CD1 1 ATOM 5128 C CD2 . LEU A 1 663 ? -54.667 31.127 26.115 1.00 89.73 ? 663 LEU A CD2 1 ATOM 5129 N N . ALA A 1 664 ? -53.093 30.225 21.966 1.00 109.70 ? 664 ALA A N 1 ATOM 5130 C CA . ALA A 1 664 ? -52.662 30.300 20.575 1.00 104.03 ? 664 ALA A CA 1 ATOM 5131 C C . ALA A 1 664 ? -51.150 30.439 20.433 1.00 103.22 ? 664 ALA A C 1 ATOM 5132 O O . ALA A 1 664 ? -50.481 31.042 21.272 1.00 102.68 ? 664 ALA A O 1 ATOM 5133 C CB . ALA A 1 664 ? -53.363 31.453 19.873 1.00 98.83 ? 664 ALA A CB 1 ATOM 5134 N N . ARG A 1 665 ? -50.630 29.871 19.350 1.00 112.49 ? 665 ARG A N 1 ATOM 5135 C CA . ARG A 1 665 ? -49.198 29.809 19.080 1.00 124.53 ? 665 ARG A CA 1 ATOM 5136 C C . ARG A 1 665 ? -48.723 31.050 18.323 1.00 112.09 ? 665 ARG A C 1 ATOM 5137 O O . ARG A 1 665 ? -47.584 31.101 17.858 1.00 113.46 ? 665 ARG A O 1 ATOM 5138 C CB . ARG A 1 665 ? -48.861 28.544 18.285 1.00 142.02 ? 665 ARG A CB 1 ATOM 5139 C CG . ARG A 1 665 ? -47.413 28.086 18.402 1.00 146.99 ? 665 ARG A CG 1 ATOM 5140 C CD . ARG A 1 665 ? -47.069 27.061 17.334 1.00 156.87 ? 665 ARG A CD 1 ATOM 5141 N NE . ARG A 1 665 ? -47.247 27.598 15.987 1.00 164.33 ? 665 ARG A NE 1 ATOM 5142 C CZ . ARG A 1 665 ? -46.299 28.231 15.304 1.00 156.61 ? 665 ARG A CZ 1 ATOM 5143 N NH1 . ARG A 1 665 ? -45.099 28.410 15.838 1.00 155.90 ? 665 ARG A NH1 1 ATOM 5144 N NH2 . ARG A 1 665 ? -46.551 28.687 14.084 1.00 144.60 ? 665 ARG A NH2 1 ATOM 5145 N N . LEU A 1 666 ? -49.607 32.040 18.206 1.00 106.29 ? 666 LEU A N 1 ATOM 5146 C CA . LEU A 1 666 ? -49.418 33.184 17.311 1.00 108.32 ? 666 LEU A CA 1 ATOM 5147 C C . LEU A 1 666 ? -48.038 33.822 17.422 1.00 107.80 ? 666 LEU A C 1 ATOM 5148 O O . LEU A 1 666 ? -47.560 34.122 18.516 1.00 104.77 ? 666 LEU A O 1 ATOM 5149 C CB . LEU A 1 666 ? -50.481 34.249 17.595 1.00 107.32 ? 666 LEU A CB 1 ATOM 5150 C CG . LEU A 1 666 ? -51.948 33.843 17.457 1.00 115.08 ? 666 LEU A CG 1 ATOM 5151 C CD1 . LEU A 1 666 ? -52.852 34.937 18.002 1.00 98.59 ? 666 LEU A CD1 1 ATOM 5152 C CD2 . LEU A 1 666 ? -52.285 33.539 16.006 1.00 127.45 ? 666 LEU A CD2 1 ATOM 5153 N N . SER A 1 667 ? -47.405 34.016 16.269 1.00 115.66 ? 667 SER A N 1 ATOM 5154 C CA . SER A 1 667 ? -46.045 34.532 16.208 1.00 114.45 ? 667 SER A CA 1 ATOM 5155 C C . SER A 1 667 ? -45.982 36.006 16.591 1.00 102.43 ? 667 SER A C 1 ATOM 5156 O O . SER A 1 667 ? -46.664 36.845 16.001 1.00 92.23 ? 667 SER A O 1 ATOM 5157 C CB . SER A 1 667 ? -45.464 34.333 14.806 1.00 113.19 ? 667 SER A CB 1 ATOM 5158 O OG . SER A 1 667 ? -46.224 35.030 13.834 1.00 108.78 ? 667 SER A OG 1 ATOM 5159 N N . CYS A 1 668 ? -45.151 36.312 17.580 1.00 96.60 ? 668 CYS A N 1 ATOM 5160 C CA . CYS A 1 668 ? -44.976 37.682 18.035 1.00 93.29 ? 668 CYS A CA 1 ATOM 5161 C C . CYS A 1 668 ? -43.515 38.098 17.929 1.00 97.28 ? 668 CYS A C 1 ATOM 5162 O O . CYS A 1 668 ? -42.616 37.261 17.997 1.00 109.27 ? 668 CYS A O 1 ATOM 5163 C CB . CYS A 1 668 ? -45.468 37.840 19.474 1.00 89.23 ? 668 CYS A CB 1 ATOM 5164 S SG . CYS A 1 668 ? -47.223 37.476 19.704 1.00 146.27 ? 668 CYS A SG 1 ATOM 5165 N N . ALA A 1 669 ? -43.286 39.394 17.758 1.00 98.57 ? 669 ALA A N 1 ATOM 5166 C CA . ALA A 1 669 ? -41.932 39.917 17.646 1.00 103.01 ? 669 ALA A CA 1 ATOM 5167 C C . ALA A 1 669 ? -41.751 41.147 18.526 1.00 106.57 ? 669 ALA A C 1 ATOM 5168 O O . ALA A 1 669 ? -42.682 41.930 18.715 1.00 100.91 ? 669 ALA A O 1 ATOM 5169 C CB . ALA A 1 669 ? -41.609 40.248 16.197 1.00 105.47 ? 669 ALA A CB 1 ATOM 5170 N N . PHE A 1 670 ? -40.547 41.309 19.062 1.00 116.76 ? 670 PHE A N 1 ATOM 5171 C CA . PHE A 1 670 ? -40.230 42.461 19.895 1.00 113.53 ? 670 PHE A CA 1 ATOM 5172 C C . PHE A 1 670 ? -39.616 43.565 19.043 1.00 114.64 ? 670 PHE A C 1 ATOM 5173 O O . PHE A 1 670 ? -38.506 43.423 18.531 1.00 122.10 ? 670 PHE A O 1 ATOM 5174 C CB . PHE A 1 670 ? -39.284 42.057 21.027 1.00 112.64 ? 670 PHE A CB 1 ATOM 5175 C CG . PHE A 1 670 ? -38.877 43.196 21.916 1.00 118.38 ? 670 PHE A CG 1 ATOM 5176 C CD1 . PHE A 1 670 ? -39.811 43.842 22.708 1.00 114.53 ? 670 PHE A CD1 1 ATOM 5177 C CD2 . PHE A 1 670 ? -37.557 43.610 21.970 1.00 135.40 ? 670 PHE A CD2 1 ATOM 5178 C CE1 . PHE A 1 670 ? -39.437 44.888 23.530 1.00 128.10 ? 670 PHE A CE1 1 ATOM 5179 C CE2 . PHE A 1 670 ? -37.177 44.653 22.792 1.00 142.27 ? 670 PHE A CE2 1 ATOM 5180 C CZ . PHE A 1 670 ? -38.119 45.293 23.573 1.00 140.04 ? 670 PHE A CZ 1 ATOM 5181 N N . LYS A 1 671 ? -40.346 44.665 18.896 1.00 113.01 ? 671 LYS A N 1 ATOM 5182 C CA . LYS A 1 671 ? -39.936 45.739 18.000 1.00 119.83 ? 671 LYS A CA 1 ATOM 5183 C C . LYS A 1 671 ? -39.707 47.050 18.744 1.00 126.85 ? 671 LYS A C 1 ATOM 5184 O O . LYS A 1 671 ? -40.564 47.506 19.502 1.00 120.05 ? 671 LYS A O 1 ATOM 5185 C CB . LYS A 1 671 ? -40.984 45.938 16.903 1.00 122.73 ? 671 LYS A CB 1 ATOM 5186 C CG . LYS A 1 671 ? -40.593 46.950 15.841 1.00 131.11 ? 671 LYS A CG 1 ATOM 5187 C CD . LYS A 1 671 ? -41.692 47.106 14.802 1.00 125.28 ? 671 LYS A CD 1 ATOM 5188 C CE . LYS A 1 671 ? -41.269 48.050 13.689 1.00 123.84 ? 671 LYS A CE 1 ATOM 5189 N NZ . LYS A 1 671 ? -40.884 49.388 14.216 1.00 126.45 ? 671 LYS A NZ 1 ATOM 5190 N N . THR A 1 672 ? -38.542 47.648 18.523 1.00 138.73 ? 672 THR A N 1 ATOM 5191 C CA . THR A 1 672 ? -38.207 48.934 19.121 1.00 143.87 ? 672 THR A CA 1 ATOM 5192 C C . THR A 1 672 ? -37.839 49.948 18.046 1.00 150.30 ? 672 THR A C 1 ATOM 5193 O O . THR A 1 672 ? -36.934 49.707 17.248 1.00 156.21 ? 672 THR A O 1 ATOM 5194 C CB . THR A 1 672 ? -37.037 48.816 20.115 1.00 145.59 ? 672 THR A CB 1 ATOM 5195 O OG1 . THR A 1 672 ? -35.866 48.361 19.426 1.00 154.22 ? 672 THR A OG1 1 ATOM 5196 C CG2 . THR A 1 672 ? -37.375 47.841 21.227 1.00 136.09 ? 672 THR A CG2 1 ATOM 5197 N N . GLU A 1 673 ? -38.525 51.089 18.056 1.00 147.87 ? 673 GLU A N 1 ATOM 5198 C CA . GLU A 1 673 ? -38.303 52.153 17.079 1.00 145.98 ? 673 GLU A CA 1 ATOM 5199 C C . GLU A 1 673 ? -39.158 53.373 17.399 1.00 146.06 ? 673 GLU A C 1 ATOM 5200 O O . GLU A 1 673 ? -40.150 53.273 18.122 1.00 135.89 ? 673 GLU A O 1 ATOM 5201 C CB . GLU A 1 673 ? -38.612 51.665 15.660 1.00 139.38 ? 673 GLU A CB 1 ATOM 5202 C CG . GLU A 1 673 ? -37.394 51.576 14.754 1.00 146.22 ? 673 GLU A CG 1 ATOM 5203 C CD . GLU A 1 673 ? -37.654 50.757 13.505 1.00 144.75 ? 673 GLU A CD 1 ATOM 5204 O OE1 . GLU A 1 673 ? -38.726 50.122 13.422 1.00 136.21 ? 673 GLU A OE1 1 ATOM 5205 O OE2 . GLU A 1 673 ? -36.786 50.747 12.607 1.00 150.26 ? 673 GLU A OE2 1 ATOM 5206 N N . ASN A 1 674 ? -38.770 54.513 16.832 1.00 157.98 ? 674 ASN A N 1 ATOM 5207 C CA . ASN A 1 674 ? -39.393 55.803 17.122 1.00 158.04 ? 674 ASN A CA 1 ATOM 5208 C C . ASN A 1 674 ? -39.567 56.044 18.621 1.00 151.47 ? 674 ASN A C 1 ATOM 5209 O O . ASN A 1 674 ? -40.613 56.518 19.067 1.00 148.59 ? 674 ASN A O 1 ATOM 5210 C CB . ASN A 1 674 ? -40.740 55.923 16.405 1.00 152.51 ? 674 ASN A CB 1 ATOM 5211 C CG . ASN A 1 674 ? -40.744 57.029 15.366 1.00 173.70 ? 674 ASN A CG 1 ATOM 5212 O OD1 . ASN A 1 674 ? -39.700 57.370 14.809 1.00 165.90 ? 674 ASN A OD1 1 ATOM 5213 N ND2 . ASN A 1 674 ? -41.915 57.597 15.102 1.00 207.58 ? 674 ASN A ND2 1 ATOM 5214 N N . GLN A 1 675 ? -38.529 55.701 19.381 1.00 142.76 ? 675 GLN A N 1 ATOM 5215 C CA . GLN A 1 675 ? -38.500 55.866 20.834 1.00 139.52 ? 675 GLN A CA 1 ATOM 5216 C C . GLN A 1 675 ? -39.653 55.127 21.516 1.00 142.85 ? 675 GLN A C 1 ATOM 5217 O O . GLN A 1 675 ? -40.125 55.534 22.577 1.00 149.48 ? 675 GLN A O 1 ATOM 5218 C CB . GLN A 1 675 ? -38.528 57.354 21.204 1.00 139.04 ? 675 GLN A CB 1 ATOM 5219 C CG . GLN A 1 675 ? -37.883 57.678 22.545 1.00 145.98 ? 675 GLN A CG 1 ATOM 5220 C CD . GLN A 1 675 ? -37.918 59.159 22.867 1.00 153.72 ? 675 GLN A CD 1 ATOM 5221 O OE1 . GLN A 1 675 ? -38.448 59.961 22.098 1.00 164.33 ? 675 GLN A OE1 1 ATOM 5222 N NE2 . GLN A 1 675 ? -37.349 59.530 24.008 1.00 144.28 ? 675 GLN A NE2 1 ATOM 5223 N N . THR A 1 676 ? -40.104 54.039 20.900 1.00 137.90 ? 676 THR A N 1 ATOM 5224 C CA . THR A 1 676 ? -41.182 53.238 21.467 1.00 128.44 ? 676 THR A CA 1 ATOM 5225 C C . THR A 1 676 ? -40.888 51.744 21.382 1.00 123.81 ? 676 THR A C 1 ATOM 5226 O O . THR A 1 676 ? -40.726 51.194 20.293 1.00 125.79 ? 676 THR A O 1 ATOM 5227 C CB . THR A 1 676 ? -42.523 53.523 20.765 1.00 123.33 ? 676 THR A CB 1 ATOM 5228 O OG1 . THR A 1 676 ? -42.896 54.890 20.979 1.00 131.03 ? 676 THR A OG1 1 ATOM 5229 C CG2 . THR A 1 676 ? -43.614 52.615 21.312 1.00 111.82 ? 676 THR A CG2 1 ATOM 5230 N N . ARG A 1 677 ? -40.823 51.094 22.539 1.00 122.40 ? 677 ARG A N 1 ATOM 5231 C CA . ARG A 1 677 ? -40.650 49.648 22.598 1.00 125.21 ? 677 ARG A CA 1 ATOM 5232 C C . ARG A 1 677 ? -42.000 48.982 22.837 1.00 114.00 ? 677 ARG A C 1 ATOM 5233 O O . ARG A 1 677 ? -42.823 49.496 23.597 1.00 108.45 ? 677 ARG A O 1 ATOM 5234 C CB . ARG A 1 677 ? -39.648 49.265 23.690 1.00 132.82 ? 677 ARG A CB 1 ATOM 5235 C CG . ARG A 1 677 ? -40.007 49.759 25.082 1.00 126.50 ? 677 ARG A CG 1 ATOM 5236 C CD . ARG A 1 677 ? -38.798 49.722 26.005 1.00 114.86 ? 677 ARG A CD 1 ATOM 5237 N NE . ARG A 1 677 ? -38.157 48.410 26.023 1.00 112.61 ? 677 ARG A NE 1 ATOM 5238 C CZ . ARG A 1 677 ? -38.435 47.455 26.903 1.00 115.58 ? 677 ARG A CZ 1 ATOM 5239 N NH1 . ARG A 1 677 ? -39.345 47.662 27.845 1.00 113.74 ? 677 ARG A NH1 1 ATOM 5240 N NH2 . ARG A 1 677 ? -37.802 46.291 26.843 1.00 114.58 ? 677 ARG A NH2 1 ATOM 5241 N N . GLN A 1 678 ? -42.215 47.832 22.204 1.00 106.92 ? 678 GLN A N 1 ATOM 5242 C CA . GLN A 1 678 ? -43.527 47.190 22.197 1.00 97.64 ? 678 GLN A CA 1 ATOM 5243 C C . GLN A 1 678 ? -43.506 45.833 21.500 1.00 91.12 ? 678 GLN A C 1 ATOM 5244 O O . GLN A 1 678 ? -42.513 45.455 20.877 1.00 95.88 ? 678 GLN A O 1 ATOM 5245 C CB . GLN A 1 678 ? -44.556 48.096 21.513 1.00 104.39 ? 678 GLN A CB 1 ATOM 5246 C CG . GLN A 1 678 ? -44.183 48.493 20.092 1.00 110.03 ? 678 GLN A CG 1 ATOM 5247 C CD . GLN A 1 678 ? -45.149 49.496 19.492 1.00 109.87 ? 678 GLN A CD 1 ATOM 5248 O OE1 . GLN A 1 678 ? -46.025 50.020 20.180 1.00 110.29 ? 678 GLN A OE1 1 ATOM 5249 N NE2 . GLN A 1 678 ? -44.993 49.768 18.201 1.00 108.45 ? 678 GLN A NE2 1 ATOM 5250 N N . VAL A 1 679 ? -44.614 45.106 21.613 1.00 87.19 ? 679 VAL A N 1 ATOM 5251 C CA . VAL A 1 679 ? -44.734 43.775 21.027 1.00 86.54 ? 679 VAL A CA 1 ATOM 5252 C C . VAL A 1 679 ? -45.833 43.733 19.970 1.00 86.42 ? 679 VAL A C 1 ATOM 5253 O O . VAL A 1 679 ? -46.959 44.165 20.218 1.00 93.43 ? 679 VAL A O 1 ATOM 5254 C CB . VAL A 1 679 ? -45.033 42.712 22.105 1.00 85.89 ? 679 VAL A CB 1 ATOM 5255 C CG1 . VAL A 1 679 ? -45.154 41.333 21.478 1.00 86.55 ? 679 VAL A CG1 1 ATOM 5256 C CG2 . VAL A 1 679 ? -43.955 42.723 23.176 1.00 94.33 ? 679 VAL A CG2 1 ATOM 5257 N N . VAL A 1 680 ? -45.503 43.215 18.791 1.00 84.92 ? 680 VAL A N 1 ATOM 5258 C CA . VAL A 1 680 ? -46.481 43.074 17.719 1.00 83.98 ? 680 VAL A CA 1 ATOM 5259 C C . VAL A 1 680 ? -46.805 41.602 17.472 1.00 88.78 ? 680 VAL A C 1 ATOM 5260 O O . VAL A 1 680 ? -45.929 40.742 17.557 1.00 101.58 ? 680 VAL A O 1 ATOM 5261 C CB . VAL A 1 680 ? -45.986 43.723 16.409 1.00 87.54 ? 680 VAL A CB 1 ATOM 5262 C CG1 . VAL A 1 680 ? -45.935 45.235 16.555 1.00 92.06 ? 680 VAL A CG1 1 ATOM 5263 C CG2 . VAL A 1 680 ? -44.621 43.176 16.018 1.00 99.28 ? 680 VAL A CG2 1 ATOM 5264 N N . CYS A 1 681 ? -48.069 41.318 17.177 1.00 87.46 ? 681 CYS A N 1 ATOM 5265 C CA . CYS A 1 681 ? -48.518 39.947 16.956 1.00 85.68 ? 681 CYS A CA 1 ATOM 5266 C C . CYS A 1 681 ? -49.513 39.876 15.804 1.00 89.65 ? 681 CYS A C 1 ATOM 5267 O O . CYS A 1 681 ? -50.422 40.698 15.713 1.00 104.41 ? 681 CYS A O 1 ATOM 5268 C CB . CYS A 1 681 ? -49.151 39.376 18.227 1.00 83.60 ? 681 CYS A CB 1 ATOM 5269 S SG . CYS A 1 681 ? -48.056 39.328 19.664 1.00 132.22 ? 681 CYS A SG 1 ATOM 5270 N N . ASP A 1 682 ? -49.348 38.885 14.933 1.00 84.34 ? 682 ASP A N 1 ATOM 5271 C CA . ASP A 1 682 ? -50.224 38.746 13.774 1.00 84.73 ? 682 ASP A CA 1 ATOM 5272 C C . ASP A 1 682 ? -51.551 38.095 14.145 1.00 81.06 ? 682 ASP A C 1 ATOM 5273 O O . ASP A 1 682 ? -51.590 36.961 14.622 1.00 81.35 ? 682 ASP A O 1 ATOM 5274 C CB . ASP A 1 682 ? -49.534 37.935 12.675 1.00 89.94 ? 682 ASP A CB 1 ATOM 5275 C CG . ASP A 1 682 ? -48.433 38.711 11.981 1.00 106.70 ? 682 ASP A CG 1 ATOM 5276 O OD1 . ASP A 1 682 ? -47.853 39.619 12.613 1.00 114.32 ? 682 ASP A OD1 1 ATOM 5277 O OD2 . ASP A 1 682 ? -48.147 38.413 10.802 1.00 111.29 ? 682 ASP A OD2 1 ATOM 5278 N N . LEU A 1 683 ? -52.638 38.826 13.921 1.00 81.76 ? 683 LEU A N 1 ATOM 5279 C CA . LEU A 1 683 ? -53.981 38.319 14.173 1.00 83.16 ? 683 LEU A CA 1 ATOM 5280 C C . LEU A 1 683 ? -54.585 37.749 12.894 1.00 82.68 ? 683 LEU A C 1 ATOM 5281 O O . LEU A 1 683 ? -55.752 37.358 12.862 1.00 81.96 ? 683 LEU A O 1 ATOM 5282 C CB . LEU A 1 683 ? -54.873 39.418 14.750 1.00 88.09 ? 683 LEU A CB 1 ATOM 5283 C CG . LEU A 1 683 ? -54.384 40.022 16.070 1.00 81.05 ? 683 LEU A CG 1 ATOM 5284 C CD1 . LEU A 1 683 ? -55.452 40.907 16.686 1.00 80.41 ? 683 LEU A CD1 1 ATOM 5285 C CD2 . LEU A 1 683 ? -53.961 38.930 17.043 1.00 73.35 ? 683 LEU A CD2 1 ATOM 5286 N N . GLY A 1 684 ? -53.774 37.712 11.841 1.00 83.03 ? 684 GLY A N 1 ATOM 5287 C CA . GLY A 1 684 ? -54.190 37.188 10.553 1.00 87.46 ? 684 GLY A CA 1 ATOM 5288 C C . GLY A 1 684 ? -54.418 38.271 9.516 1.00 86.20 ? 684 GLY A C 1 ATOM 5289 O O . GLY A 1 684 ? -54.785 39.399 9.843 1.00 93.36 ? 684 GLY A O 1 ATOM 5290 N N . ASN A 1 685 ? -54.196 37.913 8.256 1.00 84.11 ? 685 ASN A N 1 ATOM 5291 C CA . ASN A 1 685 ? -54.259 38.861 7.150 1.00 78.46 ? 685 ASN A CA 1 ATOM 5292 C C . ASN A 1 685 ? -55.030 38.312 5.953 1.00 91.95 ? 685 ASN A C 1 ATOM 5293 O O . ASN A 1 685 ? -54.448 37.641 5.100 1.00 104.98 ? 685 ASN A O 1 ATOM 5294 C CB . ASN A 1 685 ? -52.848 39.266 6.722 1.00 79.00 ? 685 ASN A CB 1 ATOM 5295 C CG . ASN A 1 685 ? -52.846 40.390 5.704 1.00 80.39 ? 685 ASN A CG 1 ATOM 5296 O OD1 . ASN A 1 685 ? -53.855 41.068 5.507 1.00 83.58 ? 685 ASN A OD1 1 ATOM 5297 N ND2 . ASN A 1 685 ? -51.705 40.599 5.058 1.00 86.75 ? 685 ASN A ND2 1 ATOM 5298 N N . PRO A 1 686 ? -56.341 38.590 5.878 1.00 88.73 ? 686 PRO A N 1 ATOM 5299 C CA . PRO A 1 686 ? -57.162 39.366 6.813 1.00 77.65 ? 686 PRO A CA 1 ATOM 5300 C C . PRO A 1 686 ? -57.569 38.596 8.064 1.00 74.25 ? 686 PRO A C 1 ATOM 5301 O O . PRO A 1 686 ? -57.468 37.370 8.099 1.00 74.32 ? 686 PRO A O 1 ATOM 5302 C CB . PRO A 1 686 ? -58.393 39.713 5.978 1.00 80.95 ? 686 PRO A CB 1 ATOM 5303 C CG . PRO A 1 686 ? -58.540 38.551 5.070 1.00 93.13 ? 686 PRO A CG 1 ATOM 5304 C CD . PRO A 1 686 ? -57.137 38.107 4.735 1.00 96.81 ? 686 PRO A CD 1 ATOM 5305 N N . MET A 1 687 ? -58.026 39.322 9.079 1.00 75.33 ? 687 MET A N 1 ATOM 5306 C CA . MET A 1 687 ? -58.659 38.702 10.233 1.00 71.68 ? 687 MET A CA 1 ATOM 5307 C C . MET A 1 687 ? -60.160 38.652 9.977 1.00 80.75 ? 687 MET A C 1 ATOM 5308 O O . MET A 1 687 ? -60.831 39.683 9.961 1.00 94.65 ? 687 MET A O 1 ATOM 5309 C CB . MET A 1 687 ? -58.346 39.483 11.510 1.00 71.65 ? 687 MET A CB 1 ATOM 5310 C CG . MET A 1 687 ? -59.019 38.950 12.764 1.00 88.38 ? 687 MET A CG 1 ATOM 5311 S SD . MET A 1 687 ? -58.614 39.949 14.211 1.00 79.15 ? 687 MET A SD 1 ATOM 5312 C CE . MET A 1 687 ? -59.536 39.101 15.491 1.00 72.99 ? 687 MET A CE 1 ATOM 5313 N N . LYS A 1 688 ? -60.679 37.444 9.781 1.00 80.83 ? 688 LYS A N 1 ATOM 5314 C CA . LYS A 1 688 ? -62.055 37.256 9.332 1.00 79.38 ? 688 LYS A CA 1 ATOM 5315 C C . LYS A 1 688 ? -63.076 37.546 10.428 1.00 92.02 ? 688 LYS A C 1 ATOM 5316 O O . LYS A 1 688 ? -62.743 37.567 11.611 1.00 115.29 ? 688 LYS A O 1 ATOM 5317 C CB . LYS A 1 688 ? -62.246 35.834 8.801 1.00 79.06 ? 688 LYS A CB 1 ATOM 5318 C CG . LYS A 1 688 ? -61.360 35.505 7.609 1.00 78.82 ? 688 LYS A CG 1 ATOM 5319 C CD . LYS A 1 688 ? -61.628 34.105 7.083 1.00 86.78 ? 688 LYS A CD 1 ATOM 5320 C CE . LYS A 1 688 ? -63.057 33.967 6.584 1.00 94.96 ? 688 LYS A CE 1 ATOM 5321 N NZ . LYS A 1 688 ? -63.340 32.592 6.086 1.00 100.77 ? 688 LYS A NZ 1 ATOM 5322 N N . ALA A 1 689 ? -64.316 37.785 10.013 1.00 92.61 ? 689 ALA A N 1 ATOM 5323 C CA . ALA A 1 689 ? -65.403 38.109 10.932 1.00 100.33 ? 689 ALA A CA 1 ATOM 5324 C C . ALA A 1 689 ? -65.650 37.004 11.954 1.00 106.43 ? 689 ALA A C 1 ATOM 5325 O O . ALA A 1 689 ? -65.494 35.820 11.654 1.00 111.48 ? 689 ALA A O 1 ATOM 5326 C CB . ALA A 1 689 ? -66.677 38.389 10.151 1.00 105.84 ? 689 ALA A CB 1 ATOM 5327 N N . GLY A 1 690 ? -66.033 37.401 13.163 1.00 105.97 ? 690 GLY A N 1 ATOM 5328 C CA . GLY A 1 690 ? -66.367 36.456 14.214 1.00 109.84 ? 690 GLY A CA 1 ATOM 5329 C C . GLY A 1 690 ? -65.167 35.747 14.811 1.00 110.52 ? 690 GLY A C 1 ATOM 5330 O O . GLY A 1 690 ? -65.319 34.825 15.612 1.00 121.33 ? 690 GLY A O 1 ATOM 5331 N N . THR A 1 691 ? -63.970 36.178 14.424 1.00 97.65 ? 691 THR A N 1 ATOM 5332 C CA . THR A 1 691 ? -62.743 35.562 14.914 1.00 93.89 ? 691 THR A CA 1 ATOM 5333 C C . THR A 1 691 ? -62.478 35.926 16.369 1.00 97.14 ? 691 THR A C 1 ATOM 5334 O O . THR A 1 691 ? -62.443 37.102 16.727 1.00 110.78 ? 691 THR A O 1 ATOM 5335 C CB . THR A 1 691 ? -61.525 35.977 14.068 1.00 90.60 ? 691 THR A CB 1 ATOM 5336 O OG1 . THR A 1 691 ? -61.749 35.623 12.697 1.00 94.97 ? 691 THR A OG1 1 ATOM 5337 C CG2 . THR A 1 691 ? -60.266 35.286 14.567 1.00 96.00 ? 691 THR A CG2 1 ATOM 5338 N N . GLN A 1 692 ? -62.295 34.909 17.203 1.00 94.46 ? 692 GLN A N 1 ATOM 5339 C CA . GLN A 1 692 ? -61.946 35.111 18.604 1.00 91.64 ? 692 GLN A CA 1 ATOM 5340 C C . GLN A 1 692 ? -60.707 34.296 18.951 1.00 92.76 ? 692 GLN A C 1 ATOM 5341 O O . GLN A 1 692 ? -60.664 33.090 18.711 1.00 106.16 ? 692 GLN A O 1 ATOM 5342 C CB . GLN A 1 692 ? -63.111 34.726 19.518 1.00 109.87 ? 692 GLN A CB 1 ATOM 5343 C CG . GLN A 1 692 ? -64.385 35.520 19.274 1.00 119.72 ? 692 GLN A CG 1 ATOM 5344 C CD . GLN A 1 692 ? -65.499 35.139 20.229 1.00 117.18 ? 692 GLN A CD 1 ATOM 5345 O OE1 . GLN A 1 692 ? -65.269 34.462 21.231 1.00 107.97 ? 692 GLN A OE1 1 ATOM 5346 N NE2 . GLN A 1 692 ? -66.716 35.573 19.922 1.00 119.40 ? 692 GLN A NE2 1 ATOM 5347 N N . LEU A 1 693 ? -59.699 34.956 19.513 1.00 94.17 ? 693 LEU A N 1 ATOM 5348 C CA . LEU A 1 693 ? -58.437 34.290 19.814 1.00 98.07 ? 693 LEU A CA 1 ATOM 5349 C C . LEU A 1 693 ? -58.007 34.458 21.268 1.00 97.30 ? 693 LEU A C 1 ATOM 5350 O O . LEU A 1 693 ? -58.297 35.471 21.905 1.00 92.44 ? 693 LEU A O 1 ATOM 5351 C CB . LEU A 1 693 ? -57.333 34.807 18.888 1.00 86.08 ? 693 LEU A CB 1 ATOM 5352 C CG . LEU A 1 693 ? -57.491 34.486 17.401 1.00 85.09 ? 693 LEU A CG 1 ATOM 5353 C CD1 . LEU A 1 693 ? -56.299 35.000 16.611 1.00 84.42 ? 693 LEU A CD1 1 ATOM 5354 C CD2 . LEU A 1 693 ? -57.670 32.990 17.193 1.00 90.55 ? 693 LEU A CD2 1 ATOM 5355 N N . LEU A 1 694 ? -57.313 33.448 21.781 1.00 97.19 ? 694 LEU A N 1 ATOM 5356 C CA . LEU A 1 694 ? -56.765 33.479 23.131 1.00 106.92 ? 694 LEU A CA 1 ATOM 5357 C C . LEU A 1 694 ? -55.310 33.027 23.123 1.00 111.21 ? 694 LEU A C 1 ATOM 5358 O O . LEU A 1 694 ? -54.998 31.927 22.671 1.00 128.72 ? 694 LEU A O 1 ATOM 5359 C CB . LEU A 1 694 ? -57.585 32.592 24.071 1.00 117.34 ? 694 LEU A CB 1 ATOM 5360 C CG . LEU A 1 694 ? -58.861 33.187 24.666 1.00 113.55 ? 694 LEU A CG 1 ATOM 5361 C CD1 . LEU A 1 694 ? -59.682 32.108 25.353 1.00 115.38 ? 694 LEU A CD1 1 ATOM 5362 C CD2 . LEU A 1 694 ? -58.516 34.296 25.645 1.00 101.02 ? 694 LEU A CD2 1 ATOM 5363 N N . ALA A 1 695 ? -54.421 33.885 23.612 1.00 95.70 ? 695 ALA A N 1 ATOM 5364 C CA . ALA A 1 695 ? -53.005 33.549 23.706 1.00 95.07 ? 695 ALA A CA 1 ATOM 5365 C C . ALA A 1 695 ? -52.359 34.262 24.888 1.00 92.59 ? 695 ALA A C 1 ATOM 5366 O O . ALA A 1 695 ? -52.700 35.402 25.194 1.00 92.82 ? 695 ALA A O 1 ATOM 5367 C CB . ALA A 1 695 ? -52.286 33.904 22.415 1.00 94.66 ? 695 ALA A CB 1 ATOM 5368 N N . GLY A 1 696 ? -51.430 33.585 25.553 1.00 95.00 ? 696 GLY A N 1 ATOM 5369 C CA . GLY A 1 696 ? -50.723 34.182 26.671 1.00 98.82 ? 696 GLY A CA 1 ATOM 5370 C C . GLY A 1 696 ? -49.416 34.827 26.256 1.00 92.20 ? 696 GLY A C 1 ATOM 5371 O O . GLY A 1 696 ? -48.806 34.433 25.262 1.00 85.26 ? 696 GLY A O 1 ATOM 5372 N N . LEU A 1 697 ? -48.983 35.819 27.026 1.00 95.01 ? 697 LEU A N 1 ATOM 5373 C CA . LEU A 1 697 ? -47.721 36.499 26.764 1.00 95.95 ? 697 LEU A CA 1 ATOM 5374 C C . LEU A 1 697 ? -46.905 36.624 28.044 1.00 98.75 ? 697 LEU A C 1 ATOM 5375 O O . LEU A 1 697 ? -47.323 37.284 28.995 1.00 95.62 ? 697 LEU A O 1 ATOM 5376 C CB . LEU A 1 697 ? -47.969 37.881 26.154 1.00 85.19 ? 697 LEU A CB 1 ATOM 5377 C CG . LEU A 1 697 ? -48.591 37.897 24.756 1.00 83.10 ? 697 LEU A CG 1 ATOM 5378 C CD1 . LEU A 1 697 ? -48.812 39.322 24.276 1.00 81.21 ? 697 LEU A CD1 1 ATOM 5379 C CD2 . LEU A 1 697 ? -47.717 37.129 23.776 1.00 84.27 ? 697 LEU A CD2 1 ATOM 5380 N N . ARG A 1 698 ? -45.738 35.987 28.064 1.00 97.77 ? 698 ARG A N 1 ATOM 5381 C CA . ARG A 1 698 ? -44.888 36.000 29.247 1.00 99.49 ? 698 ARG A CA 1 ATOM 5382 C C . ARG A 1 698 ? -43.886 37.147 29.218 1.00 103.74 ? 698 ARG A C 1 ATOM 5383 O O . ARG A 1 698 ? -43.279 37.433 28.186 1.00 107.95 ? 698 ARG A O 1 ATOM 5384 C CB . ARG A 1 698 ? -44.151 34.667 29.395 1.00 100.74 ? 698 ARG A CB 1 ATOM 5385 C CG . ARG A 1 698 ? -44.951 33.600 30.124 1.00 107.33 ? 698 ARG A CG 1 ATOM 5386 C CD . ARG A 1 698 ? -44.076 32.420 30.514 1.00 111.29 ? 698 ARG A CD 1 ATOM 5387 N NE . ARG A 1 698 ? -43.924 31.459 29.426 1.00 107.55 ? 698 ARG A NE 1 ATOM 5388 C CZ . ARG A 1 698 ? -44.626 30.336 29.323 1.00 101.42 ? 698 ARG A CZ 1 ATOM 5389 N NH1 . ARG A 1 698 ? -45.530 30.032 30.245 1.00 98.66 ? 698 ARG A NH1 1 ATOM 5390 N NH2 . ARG A 1 698 ? -44.426 29.516 28.300 1.00 101.91 ? 698 ARG A NH2 1 ATOM 5391 N N . PHE A 1 699 ? -43.725 37.804 30.362 1.00 109.56 ? 699 PHE A N 1 ATOM 5392 C CA . PHE A 1 699 ? -42.755 38.881 30.502 1.00 113.93 ? 699 PHE A CA 1 ATOM 5393 C C . PHE A 1 699 ? -41.947 38.711 31.781 1.00 110.87 ? 699 PHE A C 1 ATOM 5394 O O . PHE A 1 699 ? -42.178 37.783 32.557 1.00 112.22 ? 699 PHE A O 1 ATOM 5395 C CB . PHE A 1 699 ? -43.450 40.244 30.510 1.00 117.43 ? 699 PHE A CB 1 ATOM 5396 C CG . PHE A 1 699 ? -44.303 40.501 29.304 1.00 109.76 ? 699 PHE A CG 1 ATOM 5397 C CD1 . PHE A 1 699 ? -43.761 41.072 28.165 1.00 107.64 ? 699 PHE A CD1 1 ATOM 5398 C CD2 . PHE A 1 699 ? -45.650 40.180 29.311 1.00 111.69 ? 699 PHE A CD2 1 ATOM 5399 C CE1 . PHE A 1 699 ? -44.546 41.313 27.055 1.00 121.05 ? 699 PHE A CE1 1 ATOM 5400 C CE2 . PHE A 1 699 ? -46.439 40.418 28.204 1.00 118.87 ? 699 PHE A CE2 1 ATOM 5401 C CZ . PHE A 1 699 ? -45.886 40.985 27.074 1.00 126.05 ? 699 PHE A CZ 1 ATOM 5402 N N . SER A 1 700 ? -40.999 39.616 31.993 1.00 107.54 ? 700 SER A N 1 ATOM 5403 C CA . SER A 1 700 ? -40.244 39.658 33.237 1.00 115.69 ? 700 SER A CA 1 ATOM 5404 C C . SER A 1 700 ? -40.131 41.100 33.713 1.00 116.48 ? 700 SER A C 1 ATOM 5405 O O . SER A 1 700 ? -39.586 41.953 33.013 1.00 120.04 ? 700 SER A O 1 ATOM 5406 C CB . SER A 1 700 ? -38.857 39.038 33.056 1.00 124.19 ? 700 SER A CB 1 ATOM 5407 O OG . SER A 1 700 ? -38.182 38.928 34.298 1.00 129.48 ? 700 SER A OG 1 ATOM 5408 N N . VAL A 1 701 ? -40.655 41.374 34.901 1.00 113.47 ? 701 VAL A N 1 ATOM 5409 C CA . VAL A 1 701 ? -40.624 42.722 35.449 1.00 115.79 ? 701 VAL A CA 1 ATOM 5410 C C . VAL A 1 701 ? -39.618 42.810 36.589 1.00 126.96 ? 701 VAL A C 1 ATOM 5411 O O . VAL A 1 701 ? -39.612 41.966 37.485 1.00 126.79 ? 701 VAL A O 1 ATOM 5412 C CB . VAL A 1 701 ? -42.011 43.158 35.957 1.00 114.33 ? 701 VAL A CB 1 ATOM 5413 C CG1 . VAL A 1 701 ? -41.985 44.618 36.384 1.00 123.88 ? 701 VAL A CG1 1 ATOM 5414 C CG2 . VAL A 1 701 ? -43.061 42.933 34.882 1.00 112.03 ? 701 VAL A CG2 1 ATOM 5415 N N . HIS A 1 702 ? -38.762 43.826 36.552 1.00 134.78 ? 702 HIS A N 1 ATOM 5416 C CA . HIS A 1 702 ? -37.788 44.013 37.617 1.00 145.40 ? 702 HIS A CA 1 ATOM 5417 C C . HIS A 1 702 ? -38.186 45.192 38.496 1.00 138.88 ? 702 HIS A C 1 ATOM 5418 O O . HIS A 1 702 ? -38.757 45.002 39.571 1.00 133.03 ? 702 HIS A O 1 ATOM 5419 C CB . HIS A 1 702 ? -36.391 44.241 37.035 1.00 156.47 ? 702 HIS A CB 1 ATOM 5420 C CG . HIS A 1 702 ? -36.076 43.373 35.856 1.00 155.29 ? 702 HIS A CG 1 ATOM 5421 N ND1 . HIS A 1 702 ? -36.534 42.079 35.738 1.00 151.49 ? 702 HIS A ND1 1 ATOM 5422 C CD2 . HIS A 1 702 ? -35.352 43.619 34.738 1.00 152.99 ? 702 HIS A CD2 1 ATOM 5423 C CE1 . HIS A 1 702 ? -36.103 41.564 34.600 1.00 148.85 ? 702 HIS A CE1 1 ATOM 5424 N NE2 . HIS A 1 702 ? -35.384 42.478 33.975 1.00 148.16 ? 702 HIS A NE2 1 ATOM 5425 N N . GLN A 1 703 ? -37.919 46.400 38.000 1.00 140.17 ? 703 GLN A N 1 ATOM 5426 C CA . GLN A 1 703 ? -38.265 47.651 38.677 1.00 144.58 ? 703 GLN A CA 1 ATOM 5427 C C . GLN A 1 703 ? -37.734 48.853 37.903 1.00 149.99 ? 703 GLN A C 1 ATOM 5428 O O . GLN A 1 703 ? -36.860 48.717 37.046 1.00 157.97 ? 703 GLN A O 1 ATOM 5429 C CB . GLN A 1 703 ? -37.711 47.689 40.105 1.00 149.07 ? 703 GLN A CB 1 ATOM 5430 C CG . GLN A 1 703 ? -36.202 47.534 40.194 1.00 151.75 ? 703 GLN A CG 1 ATOM 5431 C CD . GLN A 1 703 ? -35.701 47.546 41.625 1.00 155.58 ? 703 GLN A CD 1 ATOM 5432 O OE1 . GLN A 1 703 ? -36.469 47.766 42.562 1.00 154.78 ? 703 GLN A OE1 1 ATOM 5433 N NE2 . GLN A 1 703 ? -34.407 47.307 41.801 1.00 160.88 ? 703 GLN A NE2 1 ATOM 5434 N N . GLN A 1 704 ? -38.270 50.028 38.211 1.00 146.90 ? 704 GLN A N 1 ATOM 5435 C CA . GLN A 1 704 ? -37.701 51.285 37.742 1.00 147.74 ? 704 GLN A CA 1 ATOM 5436 C C . GLN A 1 704 ? -37.598 52.232 38.927 1.00 144.49 ? 704 GLN A C 1 ATOM 5437 O O . GLN A 1 704 ? -38.619 52.638 39.484 1.00 140.56 ? 704 GLN A O 1 ATOM 5438 C CB . GLN A 1 704 ? -38.552 51.906 36.634 1.00 148.07 ? 704 GLN A CB 1 ATOM 5439 C CG . GLN A 1 704 ? -37.950 53.170 36.043 1.00 158.85 ? 704 GLN A CG 1 ATOM 5440 C CD . GLN A 1 704 ? -38.993 54.087 35.440 1.00 157.09 ? 704 GLN A CD 1 ATOM 5441 O OE1 . GLN A 1 704 ? -40.178 53.991 35.757 1.00 154.22 ? 704 GLN A OE1 1 ATOM 5442 N NE2 . GLN A 1 704 ? -38.556 54.988 34.567 1.00 155.29 ? 704 GLN A NE2 1 ATOM 5443 N N . SER A 1 705 ? -36.370 52.591 39.295 1.00 147.17 ? 705 SER A N 1 ATOM 5444 C CA . SER A 1 705 ? -36.113 53.305 40.543 1.00 154.76 ? 705 SER A CA 1 ATOM 5445 C C . SER A 1 705 ? -36.799 52.563 41.686 1.00 159.81 ? 705 SER A C 1 ATOM 5446 O O . SER A 1 705 ? -36.618 51.355 41.842 1.00 161.65 ? 705 SER A O 1 ATOM 5447 C CB . SER A 1 705 ? -36.597 54.755 40.463 1.00 151.45 ? 705 SER A CB 1 ATOM 5448 O OG . SER A 1 705 ? -36.342 55.446 41.674 1.00 153.60 ? 705 SER A OG 1 ATOM 5449 N N . GLU A 1 706 ? -37.597 53.279 42.473 1.00 155.05 ? 706 GLU A N 1 ATOM 5450 C CA . GLU A 1 706 ? -38.414 52.644 43.502 1.00 141.72 ? 706 GLU A CA 1 ATOM 5451 C C . GLU A 1 706 ? -39.777 53.321 43.614 1.00 141.76 ? 706 GLU A C 1 ATOM 5452 O O . GLU A 1 706 ? -40.032 54.326 42.950 1.00 139.95 ? 706 GLU A O 1 ATOM 5453 C CB . GLU A 1 706 ? -37.700 52.673 44.857 1.00 140.14 ? 706 GLU A CB 1 ATOM 5454 C CG . GLU A 1 706 ? -36.511 51.728 44.961 1.00 138.44 ? 706 GLU A CG 1 ATOM 5455 C CD . GLU A 1 706 ? -35.813 51.808 46.303 1.00 154.84 ? 706 GLU A CD 1 ATOM 5456 O OE1 . GLU A 1 706 ? -36.300 52.545 47.185 1.00 170.20 ? 706 GLU A OE1 1 ATOM 5457 O OE2 . GLU A 1 706 ? -34.776 51.133 46.474 1.00 155.11 ? 706 GLU A OE2 1 ATOM 5458 N N . MET A 1 707 ? -40.631 52.758 44.470 1.00 147.02 ? 707 MET A N 1 ATOM 5459 C CA . MET A 1 707 ? -42.005 53.218 44.721 1.00 144.36 ? 707 MET A CA 1 ATOM 5460 C C . MET A 1 707 ? -42.751 53.656 43.453 1.00 139.95 ? 707 MET A C 1 ATOM 5461 O O . MET A 1 707 ? -43.149 54.813 43.311 1.00 150.20 ? 707 MET A O 1 ATOM 5462 C CB . MET A 1 707 ? -42.019 54.343 45.775 1.00 141.54 ? 707 MET A CB 1 ATOM 5463 C CG . MET A 1 707 ? -41.202 55.593 45.463 1.00 137.98 ? 707 MET A CG 1 ATOM 5464 S SD . MET A 1 707 ? -41.082 56.712 46.866 1.00 180.21 ? 707 MET A SD 1 ATOM 5465 C CE . MET A 1 707 ? -40.020 55.760 47.945 1.00 126.32 ? 707 MET A CE 1 ATOM 5466 N N . ASP A 1 708 ? -42.953 52.712 42.540 1.00 128.01 ? 708 ASP A N 1 ATOM 5467 C CA . ASP A 1 708 ? -43.700 52.976 41.315 1.00 127.11 ? 708 ASP A CA 1 ATOM 5468 C C . ASP A 1 708 ? -45.156 52.544 41.438 1.00 125.34 ? 708 ASP A C 1 ATOM 5469 O O . ASP A 1 708 ? -45.915 52.636 40.471 1.00 129.39 ? 708 ASP A O 1 ATOM 5470 C CB . ASP A 1 708 ? -43.048 52.271 40.124 1.00 128.37 ? 708 ASP A CB 1 ATOM 5471 C CG . ASP A 1 708 ? -41.750 52.925 39.702 1.00 127.82 ? 708 ASP A CG 1 ATOM 5472 O OD1 . ASP A 1 708 ? -41.045 53.463 40.578 1.00 122.05 ? 708 ASP A OD1 1 ATOM 5473 O OD2 . ASP A 1 708 ? -41.437 52.907 38.493 1.00 130.58 ? 708 ASP A OD2 1 ATOM 5474 N N . THR A 1 709 ? -45.531 52.074 42.626 1.00 122.13 ? 709 THR A N 1 ATOM 5475 C CA . THR A 1 709 ? -46.847 51.484 42.862 1.00 125.35 ? 709 THR A CA 1 ATOM 5476 C C . THR A 1 709 ? -47.061 50.331 41.882 1.00 129.71 ? 709 THR A C 1 ATOM 5477 O O . THR A 1 709 ? -46.338 49.339 41.927 1.00 143.30 ? 709 THR A O 1 ATOM 5478 C CB . THR A 1 709 ? -47.984 52.523 42.735 1.00 133.61 ? 709 THR A CB 1 ATOM 5479 O OG1 . THR A 1 709 ? -47.542 53.784 43.253 1.00 150.29 ? 709 THR A OG1 1 ATOM 5480 C CG2 . THR A 1 709 ? -49.219 52.068 43.507 1.00 130.53 ? 709 THR A CG2 1 ATOM 5481 N N . SER A 1 710 ? -48.047 50.459 41.000 1.00 117.50 ? 710 SER A N 1 ATOM 5482 C CA . SER A 1 710 ? -48.330 49.415 40.021 1.00 114.93 ? 710 SER A CA 1 ATOM 5483 C C . SER A 1 710 ? -47.561 49.626 38.716 1.00 110.55 ? 710 SER A C 1 ATOM 5484 O O . SER A 1 710 ? -46.818 50.596 38.571 1.00 110.79 ? 710 SER A O 1 ATOM 5485 C CB . SER A 1 710 ? -49.831 49.353 39.738 1.00 116.59 ? 710 SER A CB 1 ATOM 5486 O OG . SER A 1 710 ? -50.325 50.626 39.359 1.00 118.26 ? 710 SER A OG 1 ATOM 5487 N N . VAL A 1 711 ? -47.746 48.707 37.772 1.00 108.15 ? 711 VAL A N 1 ATOM 5488 C CA . VAL A 1 711 ? -47.137 48.817 36.450 1.00 108.94 ? 711 VAL A CA 1 ATOM 5489 C C . VAL A 1 711 ? -48.220 48.667 35.379 1.00 121.07 ? 711 VAL A C 1 ATOM 5490 O O . VAL A 1 711 ? -49.110 47.826 35.501 1.00 124.47 ? 711 VAL A O 1 ATOM 5491 C CB . VAL A 1 711 ? -46.018 47.765 36.248 1.00 101.39 ? 711 VAL A CB 1 ATOM 5492 C CG1 . VAL A 1 711 ? -46.545 46.358 36.482 1.00 98.98 ? 711 VAL A CG1 1 ATOM 5493 C CG2 . VAL A 1 711 ? -45.395 47.892 34.864 1.00 107.00 ? 711 VAL A CG2 1 ATOM 5494 N N . LYS A 1 712 ? -48.150 49.492 34.338 1.00 119.78 ? 712 LYS A N 1 ATOM 5495 C CA . LYS A 1 712 ? -49.238 49.595 33.369 1.00 118.07 ? 712 LYS A CA 1 ATOM 5496 C C . LYS A 1 712 ? -48.887 49.053 31.982 1.00 115.67 ? 712 LYS A C 1 ATOM 5497 O O . LYS A 1 712 ? -47.879 49.433 31.392 1.00 111.80 ? 712 LYS A O 1 ATOM 5498 C CB . LYS A 1 712 ? -49.681 51.055 33.250 1.00 119.66 ? 712 LYS A CB 1 ATOM 5499 C CG . LYS A 1 712 ? -50.757 51.308 32.210 1.00 119.09 ? 712 LYS A CG 1 ATOM 5500 C CD . LYS A 1 712 ? -51.104 52.787 32.138 1.00 122.66 ? 712 LYS A CD 1 ATOM 5501 C CE . LYS A 1 712 ? -52.128 53.065 31.052 1.00 123.55 ? 712 LYS A CE 1 ATOM 5502 N NZ . LYS A 1 712 ? -52.477 54.510 30.979 1.00 124.48 ? 712 LYS A NZ 1 ATOM 5503 N N . PHE A 1 713 ? -49.736 48.164 31.471 1.00 110.95 ? 713 PHE A N 1 ATOM 5504 C CA . PHE A 1 713 ? -49.605 47.649 30.110 1.00 99.69 ? 713 PHE A CA 1 ATOM 5505 C C . PHE A 1 713 ? -50.699 48.231 29.218 1.00 102.10 ? 713 PHE A C 1 ATOM 5506 O O . PHE A 1 713 ? -51.809 48.483 29.681 1.00 114.55 ? 713 PHE A O 1 ATOM 5507 C CB . PHE A 1 713 ? -49.678 46.120 30.095 1.00 98.17 ? 713 PHE A CB 1 ATOM 5508 C CG . PHE A 1 713 ? -48.457 45.444 30.653 1.00 103.64 ? 713 PHE A CG 1 ATOM 5509 C CD1 . PHE A 1 713 ? -48.241 45.388 32.020 1.00 124.08 ? 713 PHE A CD1 1 ATOM 5510 C CD2 . PHE A 1 713 ? -47.534 44.847 29.810 1.00 98.18 ? 713 PHE A CD2 1 ATOM 5511 C CE1 . PHE A 1 713 ? -47.120 44.761 32.535 1.00 129.55 ? 713 PHE A CE1 1 ATOM 5512 C CE2 . PHE A 1 713 ? -46.414 44.217 30.319 1.00 105.57 ? 713 PHE A CE2 1 ATOM 5513 C CZ . PHE A 1 713 ? -46.206 44.175 31.683 1.00 117.66 ? 713 PHE A CZ 1 ATOM 5514 N N . ASP A 1 714 ? -50.388 48.445 27.943 1.00 94.97 ? 714 ASP A N 1 ATOM 5515 C CA . ASP A 1 714 ? -51.368 48.986 27.004 1.00 92.41 ? 714 ASP A CA 1 ATOM 5516 C C . ASP A 1 714 ? -51.606 48.042 25.828 1.00 86.98 ? 714 ASP A C 1 ATOM 5517 O O . ASP A 1 714 ? -50.675 47.684 25.107 1.00 84.42 ? 714 ASP A O 1 ATOM 5518 C CB . ASP A 1 714 ? -50.920 50.357 26.492 1.00 98.40 ? 714 ASP A CB 1 ATOM 5519 C CG . ASP A 1 714 ? -50.897 51.407 27.585 1.00 115.77 ? 714 ASP A CG 1 ATOM 5520 O OD1 . ASP A 1 714 ? -49.805 51.681 28.126 1.00 132.00 ? 714 ASP A OD1 1 ATOM 5521 O OD2 . ASP A 1 714 ? -51.972 51.958 27.905 1.00 110.96 ? 714 ASP A OD2 1 ATOM 5522 N N . LEU A 1 715 ? -52.863 47.650 25.637 1.00 92.91 ? 715 LEU A N 1 ATOM 5523 C CA . LEU A 1 715 ? -53.223 46.710 24.581 1.00 86.96 ? 715 LEU A CA 1 ATOM 5524 C C . LEU A 1 715 ? -54.190 47.322 23.572 1.00 84.41 ? 715 LEU A C 1 ATOM 5525 O O . LEU A 1 715 ? -55.226 47.871 23.946 1.00 83.45 ? 715 LEU A O 1 ATOM 5526 C CB . LEU A 1 715 ? -53.842 45.447 25.182 1.00 82.20 ? 715 LEU A CB 1 ATOM 5527 C CG . LEU A 1 715 ? -53.002 44.702 26.218 1.00 81.21 ? 715 LEU A CG 1 ATOM 5528 C CD1 . LEU A 1 715 ? -53.690 43.415 26.635 1.00 81.77 ? 715 LEU A CD1 1 ATOM 5529 C CD2 . LEU A 1 715 ? -51.616 44.417 25.673 1.00 79.23 ? 715 LEU A CD2 1 ATOM 5530 N N . GLN A 1 716 ? -53.847 47.219 22.292 1.00 84.61 ? 716 GLN A N 1 ATOM 5531 C CA . GLN A 1 716 ? -54.723 47.698 21.230 1.00 86.43 ? 716 GLN A CA 1 ATOM 5532 C C . GLN A 1 716 ? -54.576 46.865 19.961 1.00 89.94 ? 716 GLN A C 1 ATOM 5533 O O . GLN A 1 716 ? -53.478 46.429 19.612 1.00 99.65 ? 716 GLN A O 1 ATOM 5534 C CB . GLN A 1 716 ? -54.436 49.169 20.918 1.00 86.35 ? 716 GLN A CB 1 ATOM 5535 C CG . GLN A 1 716 ? -55.450 49.809 19.980 1.00 87.88 ? 716 GLN A CG 1 ATOM 5536 C CD . GLN A 1 716 ? -54.903 51.029 19.268 1.00 91.17 ? 716 GLN A CD 1 ATOM 5537 O OE1 . GLN A 1 716 ? -53.690 51.219 19.179 1.00 91.85 ? 716 GLN A OE1 1 ATOM 5538 N NE2 . GLN A 1 716 ? -55.798 51.864 18.754 1.00 92.04 ? 716 GLN A NE2 1 ATOM 5539 N N . ILE A 1 717 ? -55.693 46.650 19.275 1.00 79.77 ? 717 ILE A N 1 ATOM 5540 C CA . ILE A 1 717 ? -55.694 45.985 17.979 1.00 71.74 ? 717 ILE A CA 1 ATOM 5541 C C . ILE A 1 717 ? -55.816 47.026 16.873 1.00 73.10 ? 717 ILE A C 1 ATOM 5542 O O . ILE A 1 717 ? -56.646 47.930 16.960 1.00 91.34 ? 717 ILE A O 1 ATOM 5543 C CB . ILE A 1 717 ? -56.852 44.975 17.859 1.00 70.22 ? 717 ILE A CB 1 ATOM 5544 C CG1 . ILE A 1 717 ? -56.831 43.989 19.028 1.00 71.45 ? 717 ILE A CG1 1 ATOM 5545 C CG2 . ILE A 1 717 ? -56.790 44.246 16.526 1.00 68.91 ? 717 ILE A CG2 1 ATOM 5546 C CD1 . ILE A 1 717 ? -58.020 43.053 19.052 1.00 81.91 ? 717 ILE A CD1 1 ATOM 5547 N N . GLN A 1 718 ? -54.991 46.909 15.838 1.00 68.76 ? 718 GLN A N 1 ATOM 5548 C CA . GLN A 1 718 ? -55.063 47.842 14.719 1.00 69.74 ? 718 GLN A CA 1 ATOM 5549 C C . GLN A 1 718 ? -54.902 47.130 13.378 1.00 81.09 ? 718 GLN A C 1 ATOM 5550 O O . GLN A 1 718 ? -54.248 46.091 13.285 1.00 84.21 ? 718 GLN A O 1 ATOM 5551 C CB . GLN A 1 718 ? -54.010 48.942 14.869 1.00 70.28 ? 718 GLN A CB 1 ATOM 5552 C CG . GLN A 1 718 ? -52.574 48.455 14.881 1.00 77.47 ? 718 GLN A CG 1 ATOM 5553 C CD . GLN A 1 718 ? -51.596 49.562 15.223 1.00 84.89 ? 718 GLN A CD 1 ATOM 5554 O OE1 . GLN A 1 718 ? -51.922 50.482 15.974 1.00 85.07 ? 718 GLN A OE1 1 ATOM 5555 N NE2 . GLN A 1 718 ? -50.392 49.482 14.669 1.00 88.18 ? 718 GLN A NE2 1 ATOM 5556 N N . SER A 1 719 ? -55.514 47.699 12.344 1.00 88.17 ? 719 SER A N 1 ATOM 5557 C CA . SER A 1 719 ? -55.513 47.100 11.014 1.00 84.32 ? 719 SER A CA 1 ATOM 5558 C C . SER A 1 719 ? -55.327 48.156 9.928 1.00 82.29 ? 719 SER A C 1 ATOM 5559 O O . SER A 1 719 ? -55.403 49.355 10.194 1.00 83.35 ? 719 SER A O 1 ATOM 5560 C CB . SER A 1 719 ? -56.808 46.322 10.778 1.00 85.90 ? 719 SER A CB 1 ATOM 5561 O OG . SER A 1 719 ? -57.940 47.161 10.923 1.00 89.22 ? 719 SER A OG 1 ATOM 5562 N N . SER A 1 720 ? -55.086 47.699 8.703 1.00 82.27 ? 720 SER A N 1 ATOM 5563 C CA . SER A 1 720 ? -54.797 48.592 7.585 1.00 80.26 ? 720 SER A CA 1 ATOM 5564 C C . SER A 1 720 ? -56.062 49.039 6.856 1.00 80.23 ? 720 SER A C 1 ATOM 5565 O O . SER A 1 720 ? -55.984 49.694 5.817 1.00 82.80 ? 720 SER A O 1 ATOM 5566 C CB . SER A 1 720 ? -53.843 47.919 6.596 1.00 82.38 ? 720 SER A CB 1 ATOM 5567 O OG . SER A 1 720 ? -54.477 46.847 5.921 1.00 85.90 ? 720 SER A OG 1 ATOM 5568 N N . ASN A 1 721 ? -57.222 48.673 7.393 1.00 79.64 ? 721 ASN A N 1 ATOM 5569 C CA . ASN A 1 721 ? -58.494 49.070 6.796 1.00 92.20 ? 721 ASN A CA 1 ATOM 5570 C C . ASN A 1 721 ? -58.666 50.586 6.815 1.00 106.67 ? 721 ASN A C 1 ATOM 5571 O O . ASN A 1 721 ? -58.052 51.279 7.623 1.00 117.51 ? 721 ASN A O 1 ATOM 5572 C CB . ASN A 1 721 ? -59.665 48.404 7.521 1.00 86.68 ? 721 ASN A CB 1 ATOM 5573 C CG . ASN A 1 721 ? -59.623 46.891 7.430 1.00 91.20 ? 721 ASN A CG 1 ATOM 5574 O OD1 . ASN A 1 721 ? -58.550 46.291 7.379 1.00 108.37 ? 721 ASN A OD1 1 ATOM 5575 N ND2 . ASN A 1 721 ? -60.795 46.267 7.405 1.00 82.75 ? 721 ASN A ND2 1 ATOM 5576 N N . LEU A 1 722 ? -59.494 51.098 5.911 1.00 101.34 ? 722 LEU A N 1 ATOM 5577 C CA . LEU A 1 722 ? -59.683 52.538 5.788 1.00 92.01 ? 722 LEU A CA 1 ATOM 5578 C C . LEU A 1 722 ? -60.573 53.087 6.899 1.00 93.93 ? 722 LEU A C 1 ATOM 5579 O O . LEU A 1 722 ? -60.439 54.244 7.295 1.00 109.81 ? 722 LEU A O 1 ATOM 5580 C CB . LEU A 1 722 ? -60.277 52.890 4.420 1.00 97.58 ? 722 LEU A CB 1 ATOM 5581 C CG . LEU A 1 722 ? -59.415 52.621 3.181 1.00 108.99 ? 722 LEU A CG 1 ATOM 5582 C CD1 . LEU A 1 722 ? -59.552 51.180 2.702 1.00 127.69 ? 722 LEU A CD1 1 ATOM 5583 C CD2 . LEU A 1 722 ? -59.756 53.596 2.064 1.00 98.33 ? 722 LEU A CD2 1 ATOM 5584 N N . PHE A 1 723 ? -61.479 52.253 7.400 1.00 92.51 ? 723 PHE A N 1 ATOM 5585 C CA . PHE A 1 723 ? -62.406 52.677 8.443 1.00 93.99 ? 723 PHE A CA 1 ATOM 5586 C C . PHE A 1 723 ? -62.521 51.641 9.554 1.00 92.43 ? 723 PHE A C 1 ATOM 5587 O O . PHE A 1 723 ? -62.441 50.438 9.299 1.00 90.84 ? 723 PHE A O 1 ATOM 5588 C CB . PHE A 1 723 ? -63.785 52.959 7.847 1.00 96.84 ? 723 PHE A CB 1 ATOM 5589 C CG . PHE A 1 723 ? -63.787 54.062 6.829 1.00 101.54 ? 723 PHE A CG 1 ATOM 5590 C CD1 . PHE A 1 723 ? -63.869 55.386 7.226 1.00 113.52 ? 723 PHE A CD1 1 ATOM 5591 C CD2 . PHE A 1 723 ? -63.704 53.775 5.477 1.00 97.71 ? 723 PHE A CD2 1 ATOM 5592 C CE1 . PHE A 1 723 ? -63.869 56.404 6.292 1.00 121.92 ? 723 PHE A CE1 1 ATOM 5593 C CE2 . PHE A 1 723 ? -63.704 54.789 4.538 1.00 101.85 ? 723 PHE A CE2 1 ATOM 5594 C CZ . PHE A 1 723 ? -63.787 56.106 4.947 1.00 119.49 ? 723 PHE A CZ 1 ATOM 5595 N N . ASP A 1 724 ? -62.715 52.124 10.781 1.00 93.77 ? 724 ASP A N 1 ATOM 5596 C CA . ASP A 1 724 ? -62.819 51.273 11.965 1.00 94.48 ? 724 ASP A CA 1 ATOM 5597 C C . ASP A 1 724 ? -61.612 50.345 12.067 1.00 90.87 ? 724 ASP A C 1 ATOM 5598 O O . ASP A 1 724 ? -61.731 49.183 12.453 1.00 87.17 ? 724 ASP A O 1 ATOM 5599 C CB . ASP A 1 724 ? -64.119 50.466 11.933 1.00 105.16 ? 724 ASP A CB 1 ATOM 5600 C CG . ASP A 1 724 ? -65.341 51.339 11.715 1.00 118.31 ? 724 ASP A CG 1 ATOM 5601 O OD1 . ASP A 1 724 ? -66.445 50.936 12.138 1.00 134.09 ? 724 ASP A OD1 1 ATOM 5602 O OD2 . ASP A 1 724 ? -65.196 52.428 11.120 1.00 105.36 ? 724 ASP A OD2 1 ATOM 5603 N N . LYS A 1 725 ? -60.448 50.887 11.723 1.00 98.38 ? 725 LYS A N 1 ATOM 5604 C CA . LYS A 1 725 ? -59.226 50.105 11.577 1.00 93.51 ? 725 LYS A CA 1 ATOM 5605 C C . LYS A 1 725 ? -58.575 49.730 12.902 1.00 76.83 ? 725 LYS A C 1 ATOM 5606 O O . LYS A 1 725 ? -57.607 48.971 12.926 1.00 72.96 ? 725 LYS A O 1 ATOM 5607 C CB . LYS A 1 725 ? -58.222 50.877 10.723 1.00 95.44 ? 725 LYS A CB 1 ATOM 5608 C CG . LYS A 1 725 ? -57.944 52.285 11.223 1.00 96.65 ? 725 LYS A CG 1 ATOM 5609 C CD . LYS A 1 725 ? -57.100 53.070 10.233 1.00 98.75 ? 725 LYS A CD 1 ATOM 5610 C CE . LYS A 1 725 ? -56.918 54.510 10.685 1.00 115.02 ? 725 LYS A CE 1 ATOM 5611 N NZ . LYS A 1 725 ? -56.151 55.313 9.693 1.00 125.66 ? 725 LYS A NZ 1 ATOM 5612 N N . VAL A 1 726 ? -59.094 50.266 14.000 1.00 77.83 ? 726 VAL A N 1 ATOM 5613 C CA . VAL A 1 726 ? -58.501 50.015 15.307 1.00 76.98 ? 726 VAL A CA 1 ATOM 5614 C C . VAL A 1 726 ? -59.527 49.567 16.340 1.00 78.67 ? 726 VAL A C 1 ATOM 5615 O O . VAL A 1 726 ? -60.727 49.790 16.183 1.00 81.97 ? 726 VAL A O 1 ATOM 5616 C CB . VAL A 1 726 ? -57.783 51.268 15.849 1.00 82.10 ? 726 VAL A CB 1 ATOM 5617 C CG1 . VAL A 1 726 ? -56.591 51.623 14.974 1.00 93.34 ? 726 VAL A CG1 1 ATOM 5618 C CG2 . VAL A 1 726 ? -58.753 52.436 15.945 1.00 89.76 ? 726 VAL A CG2 1 ATOM 5619 N N . SER A 1 727 ? -59.037 48.925 17.395 1.00 78.25 ? 727 SER A N 1 ATOM 5620 C CA . SER A 1 727 ? -59.859 48.590 18.548 1.00 82.20 ? 727 SER A CA 1 ATOM 5621 C C . SER A 1 727 ? -59.763 49.745 19.539 1.00 87.74 ? 727 SER A C 1 ATOM 5622 O O . SER A 1 727 ? -59.023 50.698 19.298 1.00 86.22 ? 727 SER A O 1 ATOM 5623 C CB . SER A 1 727 ? -59.387 47.279 19.184 1.00 83.47 ? 727 SER A CB 1 ATOM 5624 O OG . SER A 1 727 ? -58.116 47.434 19.791 1.00 98.89 ? 727 SER A OG 1 ATOM 5625 N N . PRO A 1 728 ? -60.504 49.678 20.657 1.00 95.20 ? 728 PRO A N 1 ATOM 5626 C CA . PRO A 1 728 ? -60.201 50.692 21.670 1.00 90.86 ? 728 PRO A CA 1 ATOM 5627 C C . PRO A 1 728 ? -58.875 50.396 22.359 1.00 91.44 ? 728 PRO A C 1 ATOM 5628 O O . PRO A 1 728 ? -58.238 49.386 22.059 1.00 94.96 ? 728 PRO A O 1 ATOM 5629 C CB . PRO A 1 728 ? -61.373 50.576 22.650 1.00 95.33 ? 728 PRO A CB 1 ATOM 5630 C CG . PRO A 1 728 ? -61.894 49.190 22.455 1.00 97.62 ? 728 PRO A CG 1 ATOM 5631 C CD . PRO A 1 728 ? -61.721 48.915 20.992 1.00 103.33 ? 728 PRO A CD 1 ATOM 5632 N N . VAL A 1 729 ? -58.465 51.264 23.276 1.00 95.89 ? 729 VAL A N 1 ATOM 5633 C CA . VAL A 1 729 ? -57.240 51.033 24.027 1.00 88.70 ? 729 VAL A CA 1 ATOM 5634 C C . VAL A 1 729 ? -57.571 50.492 25.412 1.00 90.78 ? 729 VAL A C 1 ATOM 5635 O O . VAL A 1 729 ? -58.131 51.197 26.252 1.00 108.28 ? 729 VAL A O 1 ATOM 5636 C CB . VAL A 1 729 ? -56.396 52.317 24.151 1.00 86.99 ? 729 VAL A CB 1 ATOM 5637 C CG1 . VAL A 1 729 ? -55.439 52.437 22.976 1.00 84.00 ? 729 VAL A CG1 1 ATOM 5638 C CG2 . VAL A 1 729 ? -57.296 53.542 24.247 1.00 91.27 ? 729 VAL A CG2 1 ATOM 5639 N N . VAL A 1 730 ? -57.232 49.229 25.640 1.00 145.35 ? 730 VAL A N 1 ATOM 5640 C CA . VAL A 1 730 ? -57.507 48.586 26.916 1.00 142.94 ? 730 VAL A CA 1 ATOM 5641 C C . VAL A 1 730 ? -56.223 48.397 27.710 1.00 136.59 ? 730 VAL A C 1 ATOM 5642 O O . VAL A 1 730 ? -55.357 47.607 27.334 1.00 133.22 ? 730 VAL A O 1 ATOM 5643 C CB . VAL A 1 730 ? -58.196 47.224 26.724 1.00 141.84 ? 730 VAL A CB 1 ATOM 5644 C CG1 . VAL A 1 730 ? -58.421 46.550 28.069 1.00 139.05 ? 730 VAL A CG1 1 ATOM 5645 C CG2 . VAL A 1 730 ? -59.512 47.402 25.984 1.00 149.85 ? 730 VAL A CG2 1 ATOM 5646 N N . SER A 1 731 ? -56.107 49.132 28.810 1.00 129.78 ? 731 SER A N 1 ATOM 5647 C CA . SER A 1 731 ? -54.918 49.068 29.647 1.00 123.76 ? 731 SER A CA 1 ATOM 5648 C C . SER A 1 731 ? -55.148 48.182 30.865 1.00 120.46 ? 731 SER A C 1 ATOM 5649 O O . SER A 1 731 ? -56.216 48.213 31.477 1.00 122.84 ? 731 SER A O 1 ATOM 5650 C CB . SER A 1 731 ? -54.495 50.470 30.088 1.00 128.28 ? 731 SER A CB 1 ATOM 5651 O OG . SER A 1 731 ? -55.505 51.087 30.866 1.00 142.95 ? 731 SER A OG 1 ATOM 5652 N N . HIS A 1 732 ? -54.138 47.391 31.207 1.00 118.00 ? 732 HIS A N 1 ATOM 5653 C CA . HIS A 1 732 ? -54.216 46.494 32.351 1.00 118.17 ? 732 HIS A CA 1 ATOM 5654 C C . HIS A 1 732 ? -53.009 46.670 33.263 1.00 118.46 ? 732 HIS A C 1 ATOM 5655 O O . HIS A 1 732 ? -51.869 46.695 32.799 1.00 117.88 ? 732 HIS A O 1 ATOM 5656 C CB . HIS A 1 732 ? -54.316 45.041 31.886 1.00 120.60 ? 732 HIS A CB 1 ATOM 5657 C CG . HIS A 1 732 ? -54.059 44.043 32.970 1.00 115.70 ? 732 HIS A CG 1 ATOM 5658 N ND1 . HIS A 1 732 ? -54.746 44.048 34.165 1.00 125.68 ? 732 HIS A ND1 1 ATOM 5659 C CD2 . HIS A 1 732 ? -53.188 43.009 33.041 1.00 114.97 ? 732 HIS A CD2 1 ATOM 5660 C CE1 . HIS A 1 732 ? -54.309 43.060 34.925 1.00 124.70 ? 732 HIS A CE1 1 ATOM 5661 N NE2 . HIS A 1 732 ? -53.364 42.414 34.266 1.00 124.19 ? 732 HIS A NE2 1 ATOM 5662 N N . LYS A 1 733 ? -53.263 46.791 34.562 1.00 117.07 ? 733 LYS A N 1 ATOM 5663 C CA . LYS A 1 733 ? -52.184 46.974 35.523 1.00 110.99 ? 733 LYS A CA 1 ATOM 5664 C C . LYS A 1 733 ? -52.159 45.862 36.565 1.00 110.85 ? 733 LYS A C 1 ATOM 5665 O O . LYS A 1 733 ? -53.178 45.228 36.841 1.00 115.80 ? 733 LYS A O 1 ATOM 5666 C CB . LYS A 1 733 ? -52.306 48.332 36.221 1.00 109.13 ? 733 LYS A CB 1 ATOM 5667 C CG . LYS A 1 733 ? -53.306 48.360 37.366 1.00 110.48 ? 733 LYS A CG 1 ATOM 5668 C CD . LYS A 1 733 ? -53.182 49.642 38.174 1.00 114.64 ? 733 LYS A CD 1 ATOM 5669 C CE . LYS A 1 733 ? -54.047 49.597 39.423 1.00 122.14 ? 733 LYS A CE 1 ATOM 5670 N NZ . LYS A 1 733 ? -55.494 49.474 39.096 1.00 133.05 ? 733 LYS A NZ 1 ATOM 5671 N N . VAL A 1 734 ? -50.982 45.628 37.133 1.00 109.76 ? 734 VAL A N 1 ATOM 5672 C CA . VAL A 1 734 ? -50.831 44.681 38.230 1.00 111.68 ? 734 VAL A CA 1 ATOM 5673 C C . VAL A 1 734 ? -50.012 45.317 39.349 1.00 108.59 ? 734 VAL A C 1 ATOM 5674 O O . VAL A 1 734 ? -48.982 45.945 39.102 1.00 106.42 ? 734 VAL A O 1 ATOM 5675 C CB . VAL A 1 734 ? -50.167 43.367 37.768 1.00 117.08 ? 734 VAL A CB 1 ATOM 5676 C CG1 . VAL A 1 734 ? -51.167 42.506 37.009 1.00 121.48 ? 734 VAL A CG1 1 ATOM 5677 C CG2 . VAL A 1 734 ? -48.942 43.652 36.914 1.00 116.05 ? 734 VAL A CG2 1 ATOM 5678 N N . ASP A 1 735 ? -50.485 45.161 40.580 1.00 109.46 ? 735 ASP A N 1 ATOM 5679 C CA . ASP A 1 735 ? -49.869 45.816 41.726 1.00 109.60 ? 735 ASP A CA 1 ATOM 5680 C C . ASP A 1 735 ? -48.541 45.176 42.112 1.00 112.40 ? 735 ASP A C 1 ATOM 5681 O O . ASP A 1 735 ? -48.414 43.951 42.137 1.00 118.23 ? 735 ASP A O 1 ATOM 5682 C CB . ASP A 1 735 ? -50.822 45.794 42.922 1.00 116.82 ? 735 ASP A CB 1 ATOM 5683 C CG . ASP A 1 735 ? -52.139 46.483 42.629 1.00 131.43 ? 735 ASP A CG 1 ATOM 5684 O OD1 . ASP A 1 735 ? -52.138 47.466 41.858 1.00 141.13 ? 735 ASP A OD1 1 ATOM 5685 O OD2 . ASP A 1 735 ? -53.176 46.040 43.166 1.00 135.55 ? 735 ASP A OD2 1 ATOM 5686 N N . LEU A 1 736 ? -47.553 46.014 42.410 1.00 105.64 ? 736 LEU A N 1 ATOM 5687 C CA . LEU A 1 736 ? -46.265 45.534 42.895 1.00 95.33 ? 736 LEU A CA 1 ATOM 5688 C C . LEU A 1 736 ? -46.327 45.326 44.402 1.00 94.23 ? 736 LEU A C 1 ATOM 5689 O O . LEU A 1 736 ? -46.739 46.216 45.145 1.00 99.89 ? 736 LEU A O 1 ATOM 5690 C CB . LEU A 1 736 ? -45.141 46.512 42.538 1.00 91.79 ? 736 LEU A CB 1 ATOM 5691 C CG . LEU A 1 736 ? -44.523 46.453 41.136 1.00 94.34 ? 736 LEU A CG 1 ATOM 5692 C CD1 . LEU A 1 736 ? -45.530 46.800 40.048 1.00 113.72 ? 736 LEU A CD1 1 ATOM 5693 C CD2 . LEU A 1 736 ? -43.311 47.371 41.052 1.00 91.55 ? 736 LEU A CD2 1 ATOM 5694 N N . ALA A 1 737 ? -45.915 44.145 44.849 1.00 95.05 ? 737 ALA A N 1 ATOM 5695 C CA . ALA A 1 737 ? -45.975 43.801 46.263 1.00 89.60 ? 737 ALA A CA 1 ATOM 5696 C C . ALA A 1 737 ? -44.582 43.748 46.876 1.00 81.98 ? 737 ALA A C 1 ATOM 5697 O O . ALA A 1 737 ? -43.605 43.435 46.197 1.00 80.46 ? 737 ALA A O 1 ATOM 5698 C CB . ALA A 1 737 ? -46.689 42.471 46.455 1.00 90.65 ? 737 ALA A CB 1 ATOM 5699 N N . VAL A 1 738 ? -44.498 44.068 48.162 1.00 79.44 ? 738 VAL A N 1 ATOM 5700 C CA . VAL A 1 738 ? -43.235 44.005 48.883 1.00 75.06 ? 738 VAL A CA 1 ATOM 5701 C C . VAL A 1 738 ? -43.169 42.744 49.735 1.00 73.91 ? 738 VAL A C 1 ATOM 5702 O O . VAL A 1 738 ? -43.902 42.607 50.714 1.00 75.55 ? 738 VAL A O 1 ATOM 5703 C CB . VAL A 1 738 ? -43.034 45.239 49.785 1.00 64.41 ? 738 VAL A CB 1 ATOM 5704 C CG1 . VAL A 1 738 ? -41.775 45.087 50.624 1.00 61.50 ? 738 VAL A CG1 1 ATOM 5705 C CG2 . VAL A 1 738 ? -42.972 46.503 48.948 1.00 64.98 ? 738 VAL A CG2 1 ATOM 5706 N N . LEU A 1 739 ? -42.298 41.817 49.351 1.00 72.82 ? 739 LEU A N 1 ATOM 5707 C CA . LEU A 1 739 ? -42.083 40.610 50.136 1.00 77.20 ? 739 LEU A CA 1 ATOM 5708 C C . LEU A 1 739 ? -40.594 40.350 50.314 1.00 73.29 ? 739 LEU A C 1 ATOM 5709 O O . LEU A 1 739 ? -39.875 40.093 49.348 1.00 68.10 ? 739 LEU A O 1 ATOM 5710 C CB . LEU A 1 739 ? -42.761 39.406 49.475 1.00 91.43 ? 739 LEU A CB 1 ATOM 5711 C CG . LEU A 1 739 ? -42.750 38.066 50.218 1.00 86.17 ? 739 LEU A CG 1 ATOM 5712 C CD1 . LEU A 1 739 ? -44.061 37.331 49.992 1.00 85.79 ? 739 LEU A CD1 1 ATOM 5713 C CD2 . LEU A 1 739 ? -41.579 37.196 49.779 1.00 84.68 ? 739 LEU A CD2 1 ATOM 5714 N N . ALA A 1 740 ? -40.137 40.416 51.559 1.00 77.81 ? 740 ALA A N 1 ATOM 5715 C CA . ALA A 1 740 ? -38.756 40.098 51.883 1.00 79.55 ? 740 ALA A CA 1 ATOM 5716 C C . ALA A 1 740 ? -38.717 39.100 53.029 1.00 70.90 ? 740 ALA A C 1 ATOM 5717 O O . ALA A 1 740 ? -39.122 39.413 54.148 1.00 58.79 ? 740 ALA A O 1 ATOM 5718 C CB . ALA A 1 740 ? -37.984 41.359 52.240 1.00 80.60 ? 740 ALA A CB 1 ATOM 5719 N N . ALA A 1 741 ? -38.222 37.899 52.755 1.00 69.16 ? 741 ALA A N 1 ATOM 5720 C CA . ALA A 1 741 ? -38.171 36.866 53.778 1.00 66.05 ? 741 ALA A CA 1 ATOM 5721 C C . ALA A 1 741 ? -36.922 37.055 54.619 1.00 63.35 ? 741 ALA A C 1 ATOM 5722 O O . ALA A 1 741 ? -35.801 36.953 54.122 1.00 66.74 ? 741 ALA A O 1 ATOM 5723 C CB . ALA A 1 741 ? -38.194 35.483 53.148 1.00 66.79 ? 741 ALA A CB 1 ATOM 5724 N N . VAL A 1 742 ? -37.121 37.331 55.902 1.00 60.48 ? 742 VAL A N 1 ATOM 5725 C CA . VAL A 1 742 ? -36.007 37.615 56.792 1.00 60.56 ? 742 VAL A CA 1 ATOM 5726 C C . VAL A 1 742 ? -35.942 36.591 57.913 1.00 65.41 ? 742 VAL A C 1 ATOM 5727 O O . VAL A 1 742 ? -36.865 36.476 58.719 1.00 71.28 ? 742 VAL A O 1 ATOM 5728 C CB . VAL A 1 742 ? -36.109 39.026 57.397 1.00 56.75 ? 742 VAL A CB 1 ATOM 5729 C CG1 . VAL A 1 742 ? -34.777 39.435 57.998 1.00 50.87 ? 742 VAL A CG1 1 ATOM 5730 C CG2 . VAL A 1 742 ? -36.540 40.027 56.339 1.00 52.68 ? 742 VAL A CG2 1 ATOM 5731 N N . GLU A 1 743 ? -34.844 35.846 57.954 1.00 66.47 ? 743 GLU A N 1 ATOM 5732 C CA . GLU A 1 743 ? -34.637 34.850 58.994 1.00 70.23 ? 743 GLU A CA 1 ATOM 5733 C C . GLU A 1 743 ? -33.515 35.289 59.921 1.00 69.58 ? 743 GLU A C 1 ATOM 5734 O O . GLU A 1 743 ? -32.603 36.009 59.512 1.00 60.09 ? 743 GLU A O 1 ATOM 5735 C CB . GLU A 1 743 ? -34.313 33.485 58.384 1.00 70.03 ? 743 GLU A CB 1 ATOM 5736 C CG . GLU A 1 743 ? -33.009 33.449 57.604 1.00 75.86 ? 743 GLU A CG 1 ATOM 5737 C CD . GLU A 1 743 ? -32.614 32.046 57.193 1.00 98.96 ? 743 GLU A CD 1 ATOM 5738 O OE1 . GLU A 1 743 ? -33.378 31.102 57.488 1.00 104.59 ? 743 GLU A OE1 1 ATOM 5739 O OE2 . GLU A 1 743 ? -31.539 31.886 56.578 1.00 118.27 ? 743 GLU A OE2 1 ATOM 5740 N N . ILE A 1 744 ? -33.593 34.865 61.175 1.00 68.42 ? 744 ILE A N 1 ATOM 5741 C CA . ILE A 1 744 ? -32.539 35.154 62.133 1.00 61.79 ? 744 ILE A CA 1 ATOM 5742 C C . ILE A 1 744 ? -31.965 33.848 62.674 1.00 66.55 ? 744 ILE A C 1 ATOM 5743 O O . ILE A 1 744 ? -32.680 33.023 63.245 1.00 80.55 ? 744 ILE A O 1 ATOM 5744 C CB . ILE A 1 744 ? -33.048 36.050 63.285 1.00 58.12 ? 744 ILE A CB 1 ATOM 5745 C CG1 . ILE A 1 744 ? -31.974 36.202 64.362 1.00 52.42 ? 744 ILE A CG1 1 ATOM 5746 C CG2 . ILE A 1 744 ? -34.350 35.509 63.871 1.00 67.96 ? 744 ILE A CG2 1 ATOM 5747 C CD1 . ILE A 1 744 ? -32.393 37.087 65.510 1.00 52.61 ? 744 ILE A CD1 1 ATOM 5748 N N . ARG A 1 745 ? -30.667 33.656 62.468 1.00 66.16 ? 745 ARG A N 1 ATOM 5749 C CA . ARG A 1 745 ? -30.010 32.414 62.851 1.00 65.81 ? 745 ARG A CA 1 ATOM 5750 C C . ARG A 1 745 ? -28.931 32.657 63.894 1.00 69.65 ? 745 ARG A C 1 ATOM 5751 O O . ARG A 1 745 ? -28.401 33.762 64.007 1.00 71.59 ? 745 ARG A O 1 ATOM 5752 C CB . ARG A 1 745 ? -29.403 31.732 61.626 1.00 55.18 ? 745 ARG A CB 1 ATOM 5753 C CG . ARG A 1 745 ? -30.406 31.381 60.544 1.00 58.94 ? 745 ARG A CG 1 ATOM 5754 C CD . ARG A 1 745 ? -29.730 30.623 59.419 1.00 67.05 ? 745 ARG A CD 1 ATOM 5755 N NE . ARG A 1 745 ? -28.833 29.597 59.942 1.00 90.57 ? 745 ARG A NE 1 ATOM 5756 C CZ . ARG A 1 745 ? -29.221 28.378 60.300 1.00 103.38 ? 745 ARG A CZ 1 ATOM 5757 N NH1 . ARG A 1 745 ? -30.494 28.025 60.189 1.00 107.85 ? 745 ARG A NH1 1 ATOM 5758 N NH2 . ARG A 1 745 ? -28.334 27.512 60.770 1.00 101.04 ? 745 ARG A NH2 1 ATOM 5759 N N . GLY A 1 746 ? -28.605 31.618 64.655 1.00 63.44 ? 746 GLY A N 1 ATOM 5760 C CA . GLY A 1 746 ? -27.554 31.723 65.646 1.00 52.43 ? 746 GLY A CA 1 ATOM 5761 C C . GLY A 1 746 ? -26.884 30.404 65.971 1.00 65.96 ? 746 GLY A C 1 ATOM 5762 O O . GLY A 1 746 ? -27.482 29.338 65.826 1.00 84.42 ? 746 GLY A O 1 ATOM 5763 N N . VAL A 1 747 ? -25.638 30.486 66.428 1.00 54.06 ? 747 VAL A N 1 ATOM 5764 C CA . VAL A 1 747 ? -24.862 29.309 66.806 1.00 55.89 ? 747 VAL A CA 1 ATOM 5765 C C . VAL A 1 747 ? -23.969 29.615 68.003 1.00 62.38 ? 747 VAL A C 1 ATOM 5766 O O . VAL A 1 747 ? -23.704 30.777 68.308 1.00 64.12 ? 747 VAL A O 1 ATOM 5767 C CB . VAL A 1 747 ? -23.975 28.801 65.648 1.00 57.32 ? 747 VAL A CB 1 ATOM 5768 C CG1 . VAL A 1 747 ? -24.816 28.147 64.559 1.00 95.16 ? 747 VAL A CG1 1 ATOM 5769 C CG2 . VAL A 1 747 ? -23.133 29.937 65.085 1.00 58.64 ? 747 VAL A CG2 1 ATOM 5770 N N . SER A 1 748 ? -23.507 28.566 68.674 1.00 69.59 ? 748 SER A N 1 ATOM 5771 C CA . SER A 1 748 ? -22.593 28.718 69.799 1.00 63.67 ? 748 SER A CA 1 ATOM 5772 C C . SER A 1 748 ? -21.366 27.833 69.621 1.00 71.00 ? 748 SER A C 1 ATOM 5773 O O . SER A 1 748 ? -21.488 26.628 69.407 1.00 76.63 ? 748 SER A O 1 ATOM 5774 C CB . SER A 1 748 ? -23.294 28.381 71.116 1.00 62.15 ? 748 SER A CB 1 ATOM 5775 O OG . SER A 1 748 ? -22.416 28.547 72.217 1.00 80.96 ? 748 SER A OG 1 ATOM 5776 N N . SER A 1 749 ? -20.187 28.440 69.693 1.00 59.24 ? 749 SER A N 1 ATOM 5777 C CA . SER A 1 749 ? -18.937 27.695 69.604 1.00 61.81 ? 749 SER A CA 1 ATOM 5778 C C . SER A 1 749 ? -18.150 27.795 70.908 1.00 71.21 ? 749 SER A C 1 ATOM 5779 O O . SER A 1 749 ? -17.662 28.869 71.259 1.00 84.97 ? 749 SER A O 1 ATOM 5780 C CB . SER A 1 749 ? -18.091 28.203 68.436 1.00 67.59 ? 749 SER A CB 1 ATOM 5781 O OG . SER A 1 749 ? -17.722 29.558 68.626 1.00 104.21 ? 749 SER A OG 1 ATOM 5782 N N . PRO A 1 750 ? -18.020 26.671 71.630 1.00 70.71 ? 750 PRO A N 1 ATOM 5783 C CA . PRO A 1 750 ? -18.591 25.368 71.272 1.00 73.70 ? 750 PRO A CA 1 ATOM 5784 C C . PRO A 1 750 ? -20.054 25.232 71.687 1.00 76.39 ? 750 PRO A C 1 ATOM 5785 O O . PRO A 1 750 ? -20.616 26.149 72.286 1.00 70.39 ? 750 PRO A O 1 ATOM 5786 C CB . PRO A 1 750 ? -17.719 24.371 72.055 1.00 79.78 ? 750 PRO A CB 1 ATOM 5787 C CG . PRO A 1 750 ? -16.600 25.187 72.669 1.00 72.12 ? 750 PRO A CG 1 ATOM 5788 C CD . PRO A 1 750 ? -17.141 26.568 72.803 1.00 65.02 ? 750 PRO A CD 1 ATOM 5789 N N . ASP A 1 751 ? -20.656 24.091 71.366 1.00 90.76 ? 751 ASP A N 1 ATOM 5790 C CA . ASP A 1 751 ? -22.027 23.806 71.769 1.00 84.73 ? 751 ASP A CA 1 ATOM 5791 C C . ASP A 1 751 ? -22.080 23.486 73.254 1.00 84.15 ? 751 ASP A C 1 ATOM 5792 O O . ASP A 1 751 ? -23.075 23.753 73.927 1.00 94.83 ? 751 ASP A O 1 ATOM 5793 C CB . ASP A 1 751 ? -22.600 22.637 70.964 1.00 91.19 ? 751 ASP A CB 1 ATOM 5794 C CG . ASP A 1 751 ? -22.615 22.905 69.474 1.00 115.82 ? 751 ASP A CG 1 ATOM 5795 O OD1 . ASP A 1 751 ? -22.926 24.047 69.076 1.00 127.09 ? 751 ASP A OD1 1 ATOM 5796 O OD2 . ASP A 1 751 ? -22.313 21.972 68.700 1.00 124.81 ? 751 ASP A OD2 1 ATOM 5797 N N . HIS A 1 752 ? -20.993 22.911 73.756 1.00 78.50 ? 752 HIS A N 1 ATOM 5798 C CA . HIS A 1 752 ? -20.937 22.454 75.136 1.00 80.89 ? 752 HIS A CA 1 ATOM 5799 C C . HIS A 1 752 ? -19.566 22.672 75.765 1.00 80.25 ? 752 HIS A C 1 ATOM 5800 O O . HIS A 1 752 ? -18.558 22.784 75.068 1.00 95.88 ? 752 HIS A O 1 ATOM 5801 C CB . HIS A 1 752 ? -21.313 20.973 75.210 1.00 98.69 ? 752 HIS A CB 1 ATOM 5802 C CG . HIS A 1 752 ? -20.721 20.146 74.111 1.00 122.04 ? 752 HIS A CG 1 ATOM 5803 N ND1 . HIS A 1 752 ? -19.376 20.160 73.810 1.00 124.26 ? 752 HIS A ND1 1 ATOM 5804 C CD2 . HIS A 1 752 ? -21.293 19.284 73.237 1.00 138.27 ? 752 HIS A CD2 1 ATOM 5805 C CE1 . HIS A 1 752 ? -19.144 19.340 72.800 1.00 130.82 ? 752 HIS A CE1 1 ATOM 5806 N NE2 . HIS A 1 752 ? -20.291 18.796 72.434 1.00 141.18 ? 752 HIS A NE2 1 ATOM 5807 N N . VAL A 1 753 ? -19.542 22.738 77.092 1.00 76.97 ? 753 VAL A N 1 ATOM 5808 C CA . VAL A 1 753 ? -18.298 22.839 77.843 1.00 77.55 ? 753 VAL A CA 1 ATOM 5809 C C . VAL A 1 753 ? -18.275 21.777 78.936 1.00 88.75 ? 753 VAL A C 1 ATOM 5810 O O . VAL A 1 753 ? -19.173 21.722 79.776 1.00 85.03 ? 753 VAL A O 1 ATOM 5811 C CB . VAL A 1 753 ? -18.118 24.234 78.473 1.00 76.25 ? 753 VAL A CB 1 ATOM 5812 C CG1 . VAL A 1 753 ? -16.906 24.249 79.391 1.00 77.94 ? 753 VAL A CG1 1 ATOM 5813 C CG2 . VAL A 1 753 ? -17.988 25.295 77.390 1.00 68.34 ? 753 VAL A CG2 1 ATOM 5814 N N . PHE A 1 754 ? -17.248 20.933 78.921 1.00 98.87 ? 754 PHE A N 1 ATOM 5815 C CA . PHE A 1 754 ? -17.169 19.817 79.858 1.00 93.81 ? 754 PHE A CA 1 ATOM 5816 C C . PHE A 1 754 ? -16.364 20.161 81.106 1.00 91.84 ? 754 PHE A C 1 ATOM 5817 O O . PHE A 1 754 ? -15.154 20.376 81.037 1.00 95.41 ? 754 PHE A O 1 ATOM 5818 C CB . PHE A 1 754 ? -16.558 18.592 79.174 1.00 85.86 ? 754 PHE A CB 1 ATOM 5819 C CG . PHE A 1 754 ? -17.411 18.022 78.078 1.00 86.49 ? 754 PHE A CG 1 ATOM 5820 C CD1 . PHE A 1 754 ? -17.259 18.449 76.769 1.00 103.74 ? 754 PHE A CD1 1 ATOM 5821 C CD2 . PHE A 1 754 ? -18.365 17.058 78.356 1.00 93.41 ? 754 PHE A CD2 1 ATOM 5822 C CE1 . PHE A 1 754 ? -18.043 17.926 75.759 1.00 99.77 ? 754 PHE A CE1 1 ATOM 5823 C CE2 . PHE A 1 754 ? -19.152 16.530 77.350 1.00 99.96 ? 754 PHE A CE2 1 ATOM 5824 C CZ . PHE A 1 754 ? -18.991 16.965 76.050 1.00 98.11 ? 754 PHE A CZ 1 ATOM 5825 N N . LEU A 1 755 ? -17.048 20.215 82.244 1.00 88.80 ? 755 LEU A N 1 ATOM 5826 C CA . LEU A 1 755 ? -16.387 20.382 83.533 1.00 90.36 ? 755 LEU A CA 1 ATOM 5827 C C . LEU A 1 755 ? -16.054 19.013 84.120 1.00 96.75 ? 755 LEU A C 1 ATOM 5828 O O . LEU A 1 755 ? -16.797 18.055 83.910 1.00 107.24 ? 755 LEU A O 1 ATOM 5829 C CB . LEU A 1 755 ? -17.268 21.182 84.494 1.00 96.52 ? 755 LEU A CB 1 ATOM 5830 C CG . LEU A 1 755 ? -17.576 22.619 84.070 1.00 100.11 ? 755 LEU A CG 1 ATOM 5831 C CD1 . LEU A 1 755 ? -18.363 23.344 85.152 1.00 104.36 ? 755 LEU A CD1 1 ATOM 5832 C CD2 . LEU A 1 755 ? -16.293 23.367 83.737 1.00 98.63 ? 755 LEU A CD2 1 ATOM 5833 N N . PRO A 1 756 ? -14.932 18.908 84.854 1.00 96.52 ? 756 PRO A N 1 ATOM 5834 C CA . PRO A 1 756 ? -13.937 19.937 85.183 1.00 97.47 ? 756 PRO A CA 1 ATOM 5835 C C . PRO A 1 756 ? -13.117 20.377 83.974 1.00 106.52 ? 756 PRO A C 1 ATOM 5836 O O . PRO A 1 756 ? -13.145 19.709 82.940 1.00 112.75 ? 756 PRO A O 1 ATOM 5837 C CB . PRO A 1 756 ? -13.050 19.245 86.220 1.00 104.24 ? 756 PRO A CB 1 ATOM 5838 C CG . PRO A 1 756 ? -13.153 17.806 85.885 1.00 117.40 ? 756 PRO A CG 1 ATOM 5839 C CD . PRO A 1 756 ? -14.568 17.600 85.428 1.00 111.08 ? 756 PRO A CD 1 ATOM 5840 N N . ILE A 1 757 ? -12.389 21.480 84.109 1.00 109.96 ? 757 ILE A N 1 ATOM 5841 C CA . ILE A 1 757 ? -11.689 22.071 82.977 1.00 104.27 ? 757 ILE A CA 1 ATOM 5842 C C . ILE A 1 757 ? -10.180 22.006 83.216 1.00 99.75 ? 757 ILE A C 1 ATOM 5843 O O . ILE A 1 757 ? -9.715 22.232 84.334 1.00 103.66 ? 757 ILE A O 1 ATOM 5844 C CB . ILE A 1 757 ? -12.158 23.540 82.767 1.00 107.82 ? 757 ILE A CB 1 ATOM 5845 C CG1 . ILE A 1 757 ? -11.207 24.330 81.864 1.00 112.38 ? 757 ILE A CG1 1 ATOM 5846 C CG2 . ILE A 1 757 ? -12.314 24.247 84.105 1.00 109.53 ? 757 ILE A CG2 1 ATOM 5847 C CD1 . ILE A 1 757 ? -11.672 24.434 80.427 1.00 116.73 ? 757 ILE A CD1 1 ATOM 5848 N N . PRO A 1 758 ? -9.410 21.697 82.157 1.00 102.68 ? 758 PRO A N 1 ATOM 5849 C CA . PRO A 1 758 ? -7.957 21.505 82.257 1.00 119.94 ? 758 PRO A CA 1 ATOM 5850 C C . PRO A 1 758 ? -7.200 22.757 82.684 1.00 125.77 ? 758 PRO A C 1 ATOM 5851 O O . PRO A 1 758 ? -7.492 23.851 82.200 1.00 116.07 ? 758 PRO A O 1 ATOM 5852 C CB . PRO A 1 758 ? -7.557 21.093 80.832 1.00 127.45 ? 758 PRO A CB 1 ATOM 5853 C CG . PRO A 1 758 ? -8.712 21.486 79.965 1.00 117.54 ? 758 PRO A CG 1 ATOM 5854 C CD . PRO A 1 758 ? -9.913 21.312 80.829 1.00 102.81 ? 758 PRO A CD 1 ATOM 5855 N N . ASN A 1 759 ? -6.231 22.570 83.577 1.00 138.30 ? 759 ASN A N 1 ATOM 5856 C CA . ASN A 1 759 ? -5.418 23.657 84.114 1.00 133.39 ? 759 ASN A CA 1 ATOM 5857 C C . ASN A 1 759 ? -6.263 24.825 84.603 1.00 126.02 ? 759 ASN A C 1 ATOM 5858 O O . ASN A 1 759 ? -6.178 25.932 84.070 1.00 124.14 ? 759 ASN A O 1 ATOM 5859 C CB . ASN A 1 759 ? -4.415 24.140 83.064 1.00 130.05 ? 759 ASN A CB 1 ATOM 5860 C CG . ASN A 1 759 ? -3.418 23.067 82.673 1.00 137.97 ? 759 ASN A CG 1 ATOM 5861 O OD1 . ASN A 1 759 ? -3.087 22.190 83.472 1.00 138.13 ? 759 ASN A OD1 1 ATOM 5862 N ND2 . ASN A 1 759 ? -2.933 23.131 81.439 1.00 142.76 ? 759 ASN A ND2 1 ATOM 5863 N N . TRP A 1 760 ? -7.078 24.571 85.620 1.00 126.53 ? 760 TRP A N 1 ATOM 5864 C CA . TRP A 1 760 ? -7.934 25.607 86.180 1.00 132.80 ? 760 TRP A CA 1 ATOM 5865 C C . TRP A 1 760 ? -7.528 25.962 87.602 1.00 132.58 ? 760 TRP A C 1 ATOM 5866 O O . TRP A 1 760 ? -7.624 25.140 88.513 1.00 125.71 ? 760 TRP A O 1 ATOM 5867 C CB . TRP A 1 760 ? -9.400 25.175 86.152 1.00 134.97 ? 760 TRP A CB 1 ATOM 5868 C CG . TRP A 1 760 ? -10.266 25.988 87.068 1.00 132.82 ? 760 TRP A CG 1 ATOM 5869 C CD1 . TRP A 1 760 ? -10.983 25.533 88.136 1.00 132.91 ? 760 TRP A CD1 1 ATOM 5870 C CD2 . TRP A 1 760 ? -10.487 27.403 87.010 1.00 121.57 ? 760 TRP A CD2 1 ATOM 5871 N NE1 . TRP A 1 760 ? -11.646 26.574 88.740 1.00 124.85 ? 760 TRP A NE1 1 ATOM 5872 C CE2 . TRP A 1 760 ? -11.356 27.733 88.069 1.00 121.56 ? 760 TRP A CE2 1 ATOM 5873 C CE3 . TRP A 1 760 ? -10.038 28.422 86.164 1.00 114.94 ? 760 TRP A CE3 1 ATOM 5874 C CZ2 . TRP A 1 760 ? -11.785 29.038 88.303 1.00 123.91 ? 760 TRP A CZ2 1 ATOM 5875 C CZ3 . TRP A 1 760 ? -10.464 29.716 86.398 1.00 120.18 ? 760 TRP A CZ3 1 ATOM 5876 C CH2 . TRP A 1 760 ? -11.329 30.013 87.458 1.00 127.17 ? 760 TRP A CH2 1 ATOM 5877 N N . GLU A 1 761 ? -7.073 27.196 87.781 1.00 133.91 ? 761 GLU A N 1 ATOM 5878 C CA . GLU A 1 761 ? -6.727 27.703 89.099 1.00 137.23 ? 761 GLU A CA 1 ATOM 5879 C C . GLU A 1 761 ? -7.462 29.010 89.363 1.00 133.91 ? 761 GLU A C 1 ATOM 5880 O O . GLU A 1 761 ? -7.239 30.009 88.679 1.00 122.37 ? 761 GLU A O 1 ATOM 5881 C CB . GLU A 1 761 ? -5.216 27.901 89.225 1.00 141.08 ? 761 GLU A CB 1 ATOM 5882 C CG . GLU A 1 761 ? -4.416 26.612 89.135 1.00 144.38 ? 761 GLU A CG 1 ATOM 5883 C CD . GLU A 1 761 ? -2.923 26.841 89.253 1.00 149.43 ? 761 GLU A CD 1 ATOM 5884 O OE1 . GLU A 1 761 ? -2.179 25.849 89.399 1.00 154.37 ? 761 GLU A OE1 1 ATOM 5885 O OE2 . GLU A 1 761 ? -2.494 28.013 89.198 1.00 147.42 ? 761 GLU A OE2 1 ATOM 5886 N N . HIS A 1 762 ? -8.344 28.992 90.356 1.00 137.33 ? 762 HIS A N 1 ATOM 5887 C CA . HIS A 1 762 ? -9.126 30.170 90.706 1.00 124.57 ? 762 HIS A CA 1 ATOM 5888 C C . HIS A 1 762 ? -8.251 31.254 91.321 1.00 126.74 ? 762 HIS A C 1 ATOM 5889 O O . HIS A 1 762 ? -7.534 31.014 92.292 1.00 137.57 ? 762 HIS A O 1 ATOM 5890 C CB . HIS A 1 762 ? -10.253 29.796 91.670 1.00 121.09 ? 762 HIS A CB 1 ATOM 5891 C CG . HIS A 1 762 ? -10.666 30.913 92.578 1.00 128.48 ? 762 HIS A CG 1 ATOM 5892 N ND1 . HIS A 1 762 ? -11.169 32.107 92.109 1.00 129.54 ? 762 HIS A ND1 1 ATOM 5893 C CD2 . HIS A 1 762 ? -10.644 31.017 93.927 1.00 138.38 ? 762 HIS A CD2 1 ATOM 5894 C CE1 . HIS A 1 762 ? -11.440 32.899 93.132 1.00 134.30 ? 762 HIS A CE1 1 ATOM 5895 N NE2 . HIS A 1 762 ? -11.132 32.261 94.246 1.00 139.50 ? 762 HIS A NE2 1 ATOM 5896 N N . LYS A 1 763 ? -8.316 32.450 90.746 1.00 122.20 ? 763 LYS A N 1 ATOM 5897 C CA . LYS A 1 763 ? -7.565 33.587 91.259 1.00 128.57 ? 763 LYS A CA 1 ATOM 5898 C C . LYS A 1 763 ? -8.518 34.591 91.897 1.00 135.29 ? 763 LYS A C 1 ATOM 5899 O O . LYS A 1 763 ? -9.605 34.841 91.373 1.00 134.85 ? 763 LYS A O 1 ATOM 5900 C CB . LYS A 1 763 ? -6.754 34.246 90.142 1.00 128.51 ? 763 LYS A CB 1 ATOM 5901 C CG . LYS A 1 763 ? -5.652 35.170 90.633 1.00 139.27 ? 763 LYS A CG 1 ATOM 5902 C CD . LYS A 1 763 ? -4.823 35.702 89.475 1.00 136.55 ? 763 LYS A CD 1 ATOM 5903 C CE . LYS A 1 763 ? -3.613 36.477 89.969 1.00 134.06 ? 763 LYS A CE 1 ATOM 5904 N NZ . LYS A 1 763 ? -2.684 35.615 90.751 1.00 136.90 ? 763 LYS A NZ 1 ATOM 5905 N N . GLU A 1 764 ? -8.110 35.155 93.030 1.00 137.18 ? 764 GLU A N 1 ATOM 5906 C CA . GLU A 1 764 ? -8.935 36.116 93.757 1.00 132.62 ? 764 GLU A CA 1 ATOM 5907 C C . GLU A 1 764 ? -9.272 37.324 92.891 1.00 130.84 ? 764 GLU A C 1 ATOM 5908 O O . GLU A 1 764 ? -10.395 37.828 92.918 1.00 130.72 ? 764 GLU A O 1 ATOM 5909 C CB . GLU A 1 764 ? -8.230 36.572 95.036 1.00 134.37 ? 764 GLU A CB 1 ATOM 5910 C CG . GLU A 1 764 ? -7.890 35.448 96.000 1.00 142.45 ? 764 GLU A CG 1 ATOM 5911 C CD . GLU A 1 764 ? -7.286 35.957 97.294 1.00 158.13 ? 764 GLU A CD 1 ATOM 5912 O OE1 . GLU A 1 764 ? -7.288 37.188 97.508 1.00 159.42 ? 764 GLU A OE1 1 ATOM 5913 O OE2 . GLU A 1 764 ? -6.808 35.129 98.098 1.00 164.89 ? 764 GLU A OE2 1 ATOM 5914 N N . ASN A 1 765 ? -8.290 37.781 92.124 1.00 130.57 ? 765 ASN A N 1 ATOM 5915 C CA . ASN A 1 765 ? -8.477 38.911 91.225 1.00 134.50 ? 765 ASN A CA 1 ATOM 5916 C C . ASN A 1 765 ? -8.091 38.539 89.796 1.00 137.18 ? 765 ASN A C 1 ATOM 5917 O O . ASN A 1 765 ? -6.927 38.663 89.414 1.00 143.38 ? 765 ASN A O 1 ATOM 5918 C CB . ASN A 1 765 ? -7.661 40.114 91.703 1.00 141.87 ? 765 ASN A CB 1 ATOM 5919 C CG . ASN A 1 765 ? -8.037 41.395 90.986 1.00 140.98 ? 765 ASN A CG 1 ATOM 5920 O OD1 . ASN A 1 765 ? -9.093 41.483 90.359 1.00 138.69 ? 765 ASN A OD1 1 ATOM 5921 N ND2 . ASN A 1 765 ? -7.173 42.400 91.079 1.00 141.52 ? 765 ASN A ND2 1 ATOM 5922 N N . PRO A 1 766 ? -9.073 38.070 89.008 1.00 133.33 ? 766 PRO A N 1 ATOM 5923 C CA . PRO A 1 766 ? -8.878 37.595 87.632 1.00 121.22 ? 766 PRO A CA 1 ATOM 5924 C C . PRO A 1 766 ? -8.154 38.603 86.743 1.00 119.30 ? 766 PRO A C 1 ATOM 5925 O O . PRO A 1 766 ? -8.316 39.811 86.914 1.00 120.94 ? 766 PRO A O 1 ATOM 5926 C CB . PRO A 1 766 ? -10.309 37.369 87.138 1.00 116.66 ? 766 PRO A CB 1 ATOM 5927 C CG . PRO A 1 766 ? -11.081 37.071 88.372 1.00 124.26 ? 766 PRO A CG 1 ATOM 5928 C CD . PRO A 1 766 ? -10.477 37.940 89.438 1.00 134.46 ? 766 PRO A CD 1 ATOM 5929 N N . GLU A 1 767 ? -7.365 38.097 85.801 1.00 118.23 ? 767 GLU A N 1 ATOM 5930 C CA . GLU A 1 767 ? -6.551 38.943 84.936 1.00 120.56 ? 767 GLU A CA 1 ATOM 5931 C C . GLU A 1 767 ? -6.799 38.644 83.460 1.00 117.78 ? 767 GLU A C 1 ATOM 5932 O O . GLU A 1 767 ? -7.267 39.505 82.714 1.00 120.83 ? 767 GLU A O 1 ATOM 5933 C CB . GLU A 1 767 ? -5.067 38.768 85.264 1.00 131.45 ? 767 GLU A CB 1 ATOM 5934 C CG . GLU A 1 767 ? -4.697 39.146 86.689 1.00 132.88 ? 767 GLU A CG 1 ATOM 5935 C CD . GLU A 1 767 ? -3.227 38.931 86.988 1.00 138.91 ? 767 GLU A CD 1 ATOM 5936 O OE1 . GLU A 1 767 ? -2.828 39.090 88.161 1.00 138.82 ? 767 GLU A OE1 1 ATOM 5937 O OE2 . GLU A 1 767 ? -2.470 38.604 86.050 1.00 144.20 ? 767 GLU A OE2 1 ATOM 5938 N N . THR A 1 768 ? -6.478 37.424 83.043 1.00 116.84 ? 768 THR A N 1 ATOM 5939 C CA . THR A 1 768 ? -6.617 37.030 81.646 1.00 117.19 ? 768 THR A CA 1 ATOM 5940 C C . THR A 1 768 ? -7.722 35.990 81.477 1.00 112.31 ? 768 THR A C 1 ATOM 5941 O O . THR A 1 768 ? -8.380 35.612 82.446 1.00 110.50 ? 768 THR A O 1 ATOM 5942 C CB . THR A 1 768 ? -5.298 36.459 81.089 1.00 130.62 ? 768 THR A CB 1 ATOM 5943 O OG1 . THR A 1 768 ? -4.207 36.861 81.926 1.00 139.24 ? 768 THR A OG1 1 ATOM 5944 C CG2 . THR A 1 768 ? -5.055 36.949 79.667 1.00 131.43 ? 768 THR A CG2 1 ATOM 5945 N N . GLU A 1 769 ? -7.922 35.537 80.242 1.00 110.54 ? 769 GLU A N 1 ATOM 5946 C CA . GLU A 1 769 ? -8.911 34.506 79.945 1.00 107.17 ? 769 GLU A CA 1 ATOM 5947 C C . GLU A 1 769 ? -8.576 33.213 80.676 1.00 107.57 ? 769 GLU A C 1 ATOM 5948 O O . GLU A 1 769 ? -9.464 32.447 81.049 1.00 105.92 ? 769 GLU A O 1 ATOM 5949 C CB . GLU A 1 769 ? -8.993 34.247 78.439 1.00 104.97 ? 769 GLU A CB 1 ATOM 5950 C CG . GLU A 1 769 ? -9.359 35.463 77.605 1.00 105.50 ? 769 GLU A CG 1 ATOM 5951 C CD . GLU A 1 769 ? -9.563 35.122 76.141 1.00 115.10 ? 769 GLU A CD 1 ATOM 5952 O OE1 . GLU A 1 769 ? -9.307 33.961 75.759 1.00 125.15 ? 769 GLU A OE1 1 ATOM 5953 O OE2 . GLU A 1 769 ? -9.981 36.015 75.373 1.00 114.12 ? 769 GLU A OE2 1 ATOM 5954 N N . GLU A 1 770 ? -7.282 32.981 80.872 1.00 113.26 ? 770 GLU A N 1 ATOM 5955 C CA . GLU A 1 770 ? -6.801 31.807 81.585 1.00 119.00 ? 770 GLU A CA 1 ATOM 5956 C C . GLU A 1 770 ? -7.276 31.819 83.035 1.00 121.25 ? 770 GLU A C 1 ATOM 5957 O O . GLU A 1 770 ? -7.496 30.768 83.637 1.00 134.55 ? 770 GLU A O 1 ATOM 5958 C CB . GLU A 1 770 ? -5.272 31.745 81.530 1.00 128.72 ? 770 GLU A CB 1 ATOM 5959 C CG . GLU A 1 770 ? -4.674 30.448 82.047 1.00 132.39 ? 770 GLU A CG 1 ATOM 5960 C CD . GLU A 1 770 ? -4.901 29.283 81.103 1.00 129.47 ? 770 GLU A CD 1 ATOM 5961 O OE1 . GLU A 1 770 ? -5.247 29.525 79.927 1.00 114.89 ? 770 GLU A OE1 1 ATOM 5962 O OE2 . GLU A 1 770 ? -4.733 28.125 81.537 1.00 139.63 ? 770 GLU A OE2 1 ATOM 5963 N N . ASP A 1 771 ? -7.441 33.018 83.583 1.00 113.07 ? 771 ASP A N 1 ATOM 5964 C CA . ASP A 1 771 ? -7.841 33.183 84.976 1.00 115.79 ? 771 ASP A CA 1 ATOM 5965 C C . ASP A 1 771 ? -9.358 33.167 85.142 1.00 116.90 ? 771 ASP A C 1 ATOM 5966 O O . ASP A 1 771 ? -9.866 33.132 86.263 1.00 117.67 ? 771 ASP A O 1 ATOM 5967 C CB . ASP A 1 771 ? -7.273 34.488 85.538 1.00 130.98 ? 771 ASP A CB 1 ATOM 5968 C CG . ASP A 1 771 ? -5.771 34.594 85.361 1.00 145.75 ? 771 ASP A CG 1 ATOM 5969 O OD1 . ASP A 1 771 ? -5.034 34.254 86.310 1.00 155.36 ? 771 ASP A OD1 1 ATOM 5970 O OD2 . ASP A 1 771 ? -5.328 35.017 84.273 1.00 141.65 ? 771 ASP A OD2 1 ATOM 5971 N N . VAL A 1 772 ? -10.077 33.192 84.024 1.00 116.89 ? 772 VAL A N 1 ATOM 5972 C CA . VAL A 1 772 ? -11.535 33.238 84.055 1.00 100.85 ? 772 VAL A CA 1 ATOM 5973 C C . VAL A 1 772 ? -12.152 31.911 83.622 1.00 92.75 ? 772 VAL A C 1 ATOM 5974 O O . VAL A 1 772 ? -12.812 31.235 84.411 1.00 94.23 ? 772 VAL A O 1 ATOM 5975 C CB . VAL A 1 772 ? -12.081 34.363 83.155 1.00 93.89 ? 772 VAL A CB 1 ATOM 5976 C CG1 . VAL A 1 772 ? -13.602 34.368 83.173 1.00 94.72 ? 772 VAL A CG1 1 ATOM 5977 C CG2 . VAL A 1 772 ? -11.533 35.709 83.600 1.00 96.41 ? 772 VAL A CG2 1 ATOM 5978 N N . GLY A 1 773 ? -11.937 31.547 82.362 1.00 88.12 ? 773 GLY A N 1 ATOM 5979 C CA . GLY A 1 773 ? -12.470 30.310 81.821 1.00 84.31 ? 773 GLY A CA 1 ATOM 5980 C C . GLY A 1 773 ? -12.316 30.240 80.314 1.00 82.34 ? 773 GLY A C 1 ATOM 5981 O O . GLY A 1 773 ? -11.732 31.137 79.708 1.00 82.85 ? 773 GLY A O 1 ATOM 5982 N N . PRO A 1 774 ? -12.840 29.169 79.699 1.00 80.20 ? 774 PRO A N 1 ATOM 5983 C CA . PRO A 1 774 ? -12.764 28.989 78.244 1.00 79.97 ? 774 PRO A CA 1 ATOM 5984 C C . PRO A 1 774 ? -13.560 30.046 77.481 1.00 78.26 ? 774 PRO A C 1 ATOM 5985 O O . PRO A 1 774 ? -14.222 30.882 78.095 1.00 77.97 ? 774 PRO A O 1 ATOM 5986 C CB . PRO A 1 774 ? -13.361 27.594 78.032 1.00 79.00 ? 774 PRO A CB 1 ATOM 5987 C CG . PRO A 1 774 ? -14.230 27.369 79.222 1.00 79.54 ? 774 PRO A CG 1 ATOM 5988 C CD . PRO A 1 774 ? -13.534 28.051 80.359 1.00 73.95 ? 774 PRO A CD 1 ATOM 5989 N N . VAL A 1 775 ? -13.506 29.994 76.154 1.00 78.31 ? 775 VAL A N 1 ATOM 5990 C CA . VAL A 1 775 ? -14.143 31.014 75.330 1.00 76.10 ? 775 VAL A CA 1 ATOM 5991 C C . VAL A 1 775 ? -15.410 30.500 74.657 1.00 74.71 ? 775 VAL A C 1 ATOM 5992 O O . VAL A 1 775 ? -15.350 29.663 73.757 1.00 89.08 ? 775 VAL A O 1 ATOM 5993 C CB . VAL A 1 775 ? -13.184 31.535 74.241 1.00 82.90 ? 775 VAL A CB 1 ATOM 5994 C CG1 . VAL A 1 775 ? -13.817 32.697 73.490 1.00 76.23 ? 775 VAL A CG1 1 ATOM 5995 C CG2 . VAL A 1 775 ? -11.856 31.950 74.853 1.00 97.80 ? 775 VAL A CG2 1 ATOM 5996 N N . VAL A 1 776 ? -16.555 31.011 75.096 1.00 70.21 ? 776 VAL A N 1 ATOM 5997 C CA . VAL A 1 776 ? -17.826 30.689 74.460 1.00 69.98 ? 776 VAL A CA 1 ATOM 5998 C C . VAL A 1 776 ? -18.232 31.829 73.536 1.00 75.75 ? 776 VAL A C 1 ATOM 5999 O O . VAL A 1 776 ? -18.297 32.985 73.955 1.00 70.03 ? 776 VAL A O 1 ATOM 6000 C CB . VAL A 1 776 ? -18.938 30.436 75.493 1.00 69.22 ? 776 VAL A CB 1 ATOM 6001 C CG1 . VAL A 1 776 ? -20.253 30.128 74.791 1.00 64.91 ? 776 VAL A CG1 1 ATOM 6002 C CG2 . VAL A 1 776 ? -18.547 29.299 76.423 1.00 71.05 ? 776 VAL A CG2 1 ATOM 6003 N N . GLN A 1 777 ? -18.498 31.503 72.276 1.00 75.53 ? 777 GLN A N 1 ATOM 6004 C CA . GLN A 1 777 ? -18.788 32.524 71.280 1.00 72.24 ? 777 GLN A CA 1 ATOM 6005 C C . GLN A 1 777 ? -20.137 32.301 70.602 1.00 72.22 ? 777 GLN A C 1 ATOM 6006 O O . GLN A 1 777 ? -20.347 31.292 69.929 1.00 78.52 ? 777 GLN A O 1 ATOM 6007 C CB . GLN A 1 777 ? -17.673 32.566 70.233 1.00 69.20 ? 777 GLN A CB 1 ATOM 6008 C CG . GLN A 1 777 ? -17.692 33.800 69.351 1.00 85.26 ? 777 GLN A CG 1 ATOM 6009 C CD . GLN A 1 777 ? -16.500 33.867 68.416 1.00 104.53 ? 777 GLN A CD 1 ATOM 6010 O OE1 . GLN A 1 777 ? -15.757 32.896 68.267 1.00 100.30 ? 777 GLN A OE1 1 ATOM 6011 N NE2 . GLN A 1 777 ? -16.309 35.018 67.783 1.00 117.05 ? 777 GLN A NE2 1 ATOM 6012 N N . HIS A 1 778 ? -21.050 33.250 70.790 1.00 60.90 ? 778 HIS A N 1 ATOM 6013 C CA . HIS A 1 778 ? -22.350 33.207 70.132 1.00 55.68 ? 778 HIS A CA 1 ATOM 6014 C C . HIS A 1 778 ? -22.348 34.074 68.880 1.00 65.85 ? 778 HIS A C 1 ATOM 6015 O O . HIS A 1 778 ? -21.957 35.240 68.923 1.00 77.26 ? 778 HIS A O 1 ATOM 6016 C CB . HIS A 1 778 ? -23.458 33.666 71.084 1.00 55.09 ? 778 HIS A CB 1 ATOM 6017 C CG . HIS A 1 778 ? -23.777 32.681 72.164 1.00 61.33 ? 778 HIS A CG 1 ATOM 6018 N ND1 . HIS A 1 778 ? -24.939 32.737 72.902 1.00 61.59 ? 778 HIS A ND1 1 ATOM 6019 C CD2 . HIS A 1 778 ? -23.085 31.614 72.632 1.00 72.95 ? 778 HIS A CD2 1 ATOM 6020 C CE1 . HIS A 1 778 ? -24.951 31.748 73.777 1.00 68.53 ? 778 HIS A CE1 1 ATOM 6021 N NE2 . HIS A 1 778 ? -23.838 31.052 73.634 1.00 75.90 ? 778 HIS A NE2 1 ATOM 6022 N N . ILE A 1 779 ? -22.782 33.499 67.763 1.00 71.39 ? 779 ILE A N 1 ATOM 6023 C CA . ILE A 1 779 ? -22.858 34.236 66.508 1.00 51.56 ? 779 ILE A CA 1 ATOM 6024 C C . ILE A 1 779 ? -24.303 34.356 66.050 1.00 50.65 ? 779 ILE A C 1 ATOM 6025 O O . ILE A 1 779 ? -24.982 33.350 65.867 1.00 52.88 ? 779 ILE A O 1 ATOM 6026 C CB . ILE A 1 779 ? -22.038 33.558 65.395 1.00 65.95 ? 779 ILE A CB 1 ATOM 6027 C CG1 . ILE A 1 779 ? -20.680 33.094 65.927 1.00 86.62 ? 779 ILE A CG1 1 ATOM 6028 C CG2 . ILE A 1 779 ? -21.881 34.493 64.204 1.00 52.99 ? 779 ILE A CG2 1 ATOM 6029 C CD1 . ILE A 1 779 ? -19.822 34.210 66.474 1.00 102.18 ? 779 ILE A CD1 1 ATOM 6030 N N . TYR A 1 780 ? -24.772 35.585 65.866 1.00 64.63 ? 780 TYR A N 1 ATOM 6031 C CA . TYR A 1 780 ? -26.133 35.811 65.395 1.00 49.54 ? 780 TYR A CA 1 ATOM 6032 C C . TYR A 1 780 ? -26.145 36.429 64.003 1.00 50.19 ? 780 TYR A C 1 ATOM 6033 O O . TYR A 1 780 ? -25.471 37.427 63.748 1.00 49.70 ? 780 TYR A O 1 ATOM 6034 C CB . TYR A 1 780 ? -26.900 36.704 66.370 1.00 49.14 ? 780 TYR A CB 1 ATOM 6035 C CG . TYR A 1 780 ? -27.271 36.013 67.661 1.00 56.02 ? 780 TYR A CG 1 ATOM 6036 C CD1 . TYR A 1 780 ? -26.545 36.233 68.823 1.00 65.58 ? 780 TYR A CD1 1 ATOM 6037 C CD2 . TYR A 1 780 ? -28.342 35.133 67.713 1.00 59.03 ? 780 TYR A CD2 1 ATOM 6038 C CE1 . TYR A 1 780 ? -26.880 35.599 70.004 1.00 81.29 ? 780 TYR A CE1 1 ATOM 6039 C CE2 . TYR A 1 780 ? -28.685 34.496 68.889 1.00 62.88 ? 780 TYR A CE2 1 ATOM 6040 C CZ . TYR A 1 780 ? -27.953 34.733 70.031 1.00 82.71 ? 780 TYR A CZ 1 ATOM 6041 O OH . TYR A 1 780 ? -28.292 34.098 71.203 1.00 96.48 ? 780 TYR A OH 1 ATOM 6042 N N . GLU A 1 781 ? -26.916 35.827 63.105 1.00 49.37 ? 781 GLU A N 1 ATOM 6043 C CA . GLU A 1 781 ? -27.025 36.324 61.741 1.00 52.90 ? 781 GLU A CA 1 ATOM 6044 C C . GLU A 1 781 ? -28.448 36.736 61.393 1.00 65.08 ? 781 GLU A C 1 ATOM 6045 O O . GLU A 1 781 ? -29.381 35.939 61.494 1.00 71.89 ? 781 GLU A O 1 ATOM 6046 C CB . GLU A 1 781 ? -26.543 35.273 60.742 1.00 52.40 ? 781 GLU A CB 1 ATOM 6047 C CG . GLU A 1 781 ? -26.909 35.604 59.306 1.00 66.20 ? 781 GLU A CG 1 ATOM 6048 C CD . GLU A 1 781 ? -26.346 34.612 58.312 1.00 94.41 ? 781 GLU A CD 1 ATOM 6049 O OE1 . GLU A 1 781 ? -26.185 33.426 58.673 1.00 111.29 ? 781 GLU A OE1 1 ATOM 6050 O OE2 . GLU A 1 781 ? -26.062 35.023 57.168 1.00 98.54 ? 781 GLU A OE2 1 ATOM 6051 N N . LEU A 1 782 ? -28.605 37.990 60.984 1.00 48.87 ? 782 LEU A N 1 ATOM 6052 C CA . LEU A 1 782 ? -29.876 38.472 60.466 1.00 48.79 ? 782 LEU A CA 1 ATOM 6053 C C . LEU A 1 782 ? -29.773 38.594 58.953 1.00 60.45 ? 782 LEU A C 1 ATOM 6054 O O . LEU A 1 782 ? -29.068 39.464 58.442 1.00 84.17 ? 782 LEU A O 1 ATOM 6055 C CB . LEU A 1 782 ? -30.245 39.816 61.093 1.00 64.00 ? 782 LEU A CB 1 ATOM 6056 C CG . LEU A 1 782 ? -31.592 40.404 60.673 1.00 53.28 ? 782 LEU A CG 1 ATOM 6057 C CD1 . LEU A 1 782 ? -32.716 39.459 61.057 1.00 53.54 ? 782 LEU A CD1 1 ATOM 6058 C CD2 . LEU A 1 782 ? -31.799 41.774 61.298 1.00 48.88 ? 782 LEU A CD2 1 ATOM 6059 N N . ARG A 1 783 ? -30.473 37.722 58.235 1.00 52.25 ? 783 ARG A N 1 ATOM 6060 C CA . ARG A 1 783 ? -30.335 37.671 56.786 1.00 56.30 ? 783 ARG A CA 1 ATOM 6061 C C . ARG A 1 783 ? -31.637 37.966 56.054 1.00 61.53 ? 783 ARG A C 1 ATOM 6062 O O . ARG A 1 783 ? -32.690 37.421 56.384 1.00 58.39 ? 783 ARG A O 1 ATOM 6063 C CB . ARG A 1 783 ? -29.797 36.303 56.353 1.00 58.92 ? 783 ARG A CB 1 ATOM 6064 C CG . ARG A 1 783 ? -29.503 36.201 54.863 1.00 64.92 ? 783 ARG A CG 1 ATOM 6065 C CD . ARG A 1 783 ? -28.611 35.011 54.545 1.00 80.43 ? 783 ARG A CD 1 ATOM 6066 N NE . ARG A 1 783 ? -28.241 34.976 53.133 1.00 86.27 ? 783 ARG A NE 1 ATOM 6067 C CZ . ARG A 1 783 ? -27.212 35.639 52.614 1.00 86.42 ? 783 ARG A CZ 1 ATOM 6068 N NH1 . ARG A 1 783 ? -26.445 36.391 53.391 1.00 58.63 ? 783 ARG A NH1 1 ATOM 6069 N NH2 . ARG A 1 783 ? -26.950 35.550 51.317 1.00 91.08 ? 783 ARG A NH2 1 ATOM 6070 N N . ASN A 1 784 ? -31.551 38.841 55.058 1.00 62.73 ? 784 ASN A N 1 ATOM 6071 C CA . ASN A 1 784 ? -32.672 39.113 54.172 1.00 60.75 ? 784 ASN A CA 1 ATOM 6072 C C . ASN A 1 784 ? -32.600 38.195 52.959 1.00 66.83 ? 784 ASN A C 1 ATOM 6073 O O . ASN A 1 784 ? -31.601 38.178 52.246 1.00 72.95 ? 784 ASN A O 1 ATOM 6074 C CB . ASN A 1 784 ? -32.677 40.581 53.741 1.00 65.47 ? 784 ASN A CB 1 ATOM 6075 C CG . ASN A 1 784 ? -33.878 40.937 52.888 1.00 76.03 ? 784 ASN A CG 1 ATOM 6076 O OD1 . ASN A 1 784 ? -34.853 40.188 52.820 1.00 81.36 ? 784 ASN A OD1 1 ATOM 6077 N ND2 . ASN A 1 784 ? -33.817 42.091 52.234 1.00 82.44 ? 784 ASN A ND2 1 ATOM 6078 N N . ASN A 1 785 ? -33.656 37.421 52.742 1.00 68.35 ? 785 ASN A N 1 ATOM 6079 C CA . ASN A 1 785 ? -33.696 36.462 51.644 1.00 79.38 ? 785 ASN A CA 1 ATOM 6080 C C . ASN A 1 785 ? -34.618 36.912 50.521 1.00 96.53 ? 785 ASN A C 1 ATOM 6081 O O . ASN A 1 785 ? -34.180 37.090 49.384 1.00 105.07 ? 785 ASN A O 1 ATOM 6082 C CB . ASN A 1 785 ? -34.123 35.082 52.147 1.00 82.11 ? 785 ASN A CB 1 ATOM 6083 C CG . ASN A 1 785 ? -33.017 34.370 52.898 1.00 90.77 ? 785 ASN A CG 1 ATOM 6084 O OD1 . ASN A 1 785 ? -33.168 34.026 54.070 1.00 96.96 ? 785 ASN A OD1 1 ATOM 6085 N ND2 . ASN A 1 785 ? -31.894 34.146 52.224 1.00 93.72 ? 785 ASN A ND2 1 ATOM 6086 N N . GLY A 1 786 ? -35.896 37.084 50.849 1.00 101.07 ? 786 GLY A N 1 ATOM 6087 C CA . GLY A 1 786 ? -36.919 37.375 49.860 1.00 89.68 ? 786 GLY A CA 1 ATOM 6088 C C . GLY A 1 786 ? -36.619 38.598 49.017 1.00 85.15 ? 786 GLY A C 1 ATOM 6089 O O . GLY A 1 786 ? -35.821 39.449 49.411 1.00 94.58 ? 786 GLY A O 1 ATOM 6090 N N . PRO A 1 787 ? -37.269 38.686 47.847 1.00 80.21 ? 787 PRO A N 1 ATOM 6091 C CA . PRO A 1 787 ? -36.967 39.628 46.762 1.00 82.50 ? 787 PRO A CA 1 ATOM 6092 C C . PRO A 1 787 ? -36.805 41.074 47.214 1.00 76.95 ? 787 PRO A C 1 ATOM 6093 O O . PRO A 1 787 ? -35.863 41.744 46.791 1.00 83.55 ? 787 PRO A O 1 ATOM 6094 C CB . PRO A 1 787 ? -38.185 39.495 45.846 1.00 91.25 ? 787 PRO A CB 1 ATOM 6095 C CG . PRO A 1 787 ? -38.668 38.111 46.075 1.00 89.23 ? 787 PRO A CG 1 ATOM 6096 C CD . PRO A 1 787 ? -38.427 37.833 47.527 1.00 80.14 ? 787 PRO A CD 1 ATOM 6097 N N . SER A 1 788 ? -37.697 41.540 48.079 1.00 71.46 ? 788 SER A N 1 ATOM 6098 C CA . SER A 1 788 ? -37.683 42.936 48.491 1.00 70.46 ? 788 SER A CA 1 ATOM 6099 C C . SER A 1 788 ? -36.530 43.231 49.442 1.00 67.03 ? 788 SER A C 1 ATOM 6100 O O . SER A 1 788 ? -35.767 42.338 49.809 1.00 76.51 ? 788 SER A O 1 ATOM 6101 C CB . SER A 1 788 ? -39.011 43.306 49.149 1.00 79.33 ? 788 SER A CB 1 ATOM 6102 O OG . SER A 1 788 ? -40.101 42.999 48.297 1.00 89.12 ? 788 SER A OG 1 ATOM 6103 N N . SER A 1 789 ? -36.415 44.492 49.839 1.00 67.20 ? 789 SER A N 1 ATOM 6104 C CA . SER A 1 789 ? -35.364 44.924 50.750 1.00 68.36 ? 789 SER A CA 1 ATOM 6105 C C . SER A 1 789 ? -35.959 45.830 51.816 1.00 68.80 ? 789 SER A C 1 ATOM 6106 O O . SER A 1 789 ? -36.944 46.521 51.560 1.00 79.62 ? 789 SER A O 1 ATOM 6107 C CB . SER A 1 789 ? -34.256 45.653 49.989 1.00 74.22 ? 789 SER A CB 1 ATOM 6108 O OG . SER A 1 789 ? -33.850 44.916 48.850 1.00 92.29 ? 789 SER A OG 1 ATOM 6109 N N . PHE A 1 790 ? -35.377 45.829 53.011 1.00 60.84 ? 790 PHE A N 1 ATOM 6110 C CA . PHE A 1 790 ? -35.867 46.710 54.066 1.00 64.22 ? 790 PHE A CA 1 ATOM 6111 C C . PHE A 1 790 ? -34.839 47.777 54.432 1.00 61.00 ? 790 PHE A C 1 ATOM 6112 O O . PHE A 1 790 ? -33.638 47.514 54.483 1.00 59.18 ? 790 PHE A O 1 ATOM 6113 C CB . PHE A 1 790 ? -36.279 45.906 55.306 1.00 63.77 ? 790 PHE A CB 1 ATOM 6114 C CG . PHE A 1 790 ? -35.165 45.115 55.935 1.00 67.37 ? 790 PHE A CG 1 ATOM 6115 C CD1 . PHE A 1 790 ? -34.401 45.656 56.956 1.00 75.81 ? 790 PHE A CD1 1 ATOM 6116 C CD2 . PHE A 1 790 ? -34.906 43.816 55.529 1.00 70.01 ? 790 PHE A CD2 1 ATOM 6117 C CE1 . PHE A 1 790 ? -33.385 44.926 57.543 1.00 63.54 ? 790 PHE A CE1 1 ATOM 6118 C CE2 . PHE A 1 790 ? -33.892 43.081 56.114 1.00 68.20 ? 790 PHE A CE2 1 ATOM 6119 C CZ . PHE A 1 790 ? -33.134 43.636 57.124 1.00 57.75 ? 790 PHE A CZ 1 ATOM 6120 N N . SER A 1 791 ? -35.332 48.988 54.671 1.00 60.82 ? 791 SER A N 1 ATOM 6121 C CA . SER A 1 791 ? -34.478 50.144 54.921 1.00 61.88 ? 791 SER A CA 1 ATOM 6122 C C . SER A 1 791 ? -33.952 50.205 56.352 1.00 60.05 ? 791 SER A C 1 ATOM 6123 O O . SER A 1 791 ? -32.817 50.616 56.576 1.00 62.13 ? 791 SER A O 1 ATOM 6124 C CB . SER A 1 791 ? -35.234 51.433 54.595 1.00 71.91 ? 791 SER A CB 1 ATOM 6125 O OG . SER A 1 791 ? -36.434 51.519 55.342 1.00 93.06 ? 791 SER A OG 1 ATOM 6126 N N . LYS A 1 792 ? -34.781 49.811 57.316 1.00 62.08 ? 792 LYS A N 1 ATOM 6127 C CA . LYS A 1 792 ? -34.388 49.837 58.725 1.00 63.12 ? 792 LYS A CA 1 ATOM 6128 C C . LYS A 1 792 ? -35.022 48.697 59.518 1.00 59.31 ? 792 LYS A C 1 ATOM 6129 O O . LYS A 1 792 ? -36.155 48.296 59.249 1.00 61.58 ? 792 LYS A O 1 ATOM 6130 C CB . LYS A 1 792 ? -34.759 51.178 59.366 1.00 60.26 ? 792 LYS A CB 1 ATOM 6131 C CG . LYS A 1 792 ? -33.779 52.306 59.081 1.00 70.51 ? 792 LYS A CG 1 ATOM 6132 C CD . LYS A 1 792 ? -34.130 53.562 59.862 1.00 81.95 ? 792 LYS A CD 1 ATOM 6133 C CE . LYS A 1 792 ? -33.123 54.673 59.601 1.00 85.20 ? 792 LYS A CE 1 ATOM 6134 N NZ . LYS A 1 792 ? -33.437 55.909 60.371 1.00 78.24 ? 792 LYS A NZ 1 ATOM 6135 N N . ALA A 1 793 ? -34.287 48.184 60.499 1.00 55.22 ? 793 ALA A N 1 ATOM 6136 C CA . ALA A 1 793 ? -34.790 47.115 61.354 1.00 55.17 ? 793 ALA A CA 1 ATOM 6137 C C . ALA A 1 793 ? -34.098 47.112 62.713 1.00 60.84 ? 793 ALA A C 1 ATOM 6138 O O . ALA A 1 793 ? -33.009 47.663 62.869 1.00 64.53 ? 793 ALA A O 1 ATOM 6139 C CB . ALA A 1 793 ? -34.619 45.769 60.674 1.00 53.93 ? 793 ALA A CB 1 ATOM 6140 N N . MET A 1 794 ? -34.736 46.480 63.692 1.00 58.79 ? 794 MET A N 1 ATOM 6141 C CA . MET A 1 794 ? -34.197 46.424 65.045 1.00 58.50 ? 794 MET A CA 1 ATOM 6142 C C . MET A 1 794 ? -33.781 45.007 65.421 1.00 69.83 ? 794 MET A C 1 ATOM 6143 O O . MET A 1 794 ? -34.344 44.031 64.929 1.00 71.79 ? 794 MET A O 1 ATOM 6144 C CB . MET A 1 794 ? -35.220 46.958 66.048 1.00 56.84 ? 794 MET A CB 1 ATOM 6145 C CG . MET A 1 794 ? -35.555 48.425 65.852 1.00 66.79 ? 794 MET A CG 1 ATOM 6146 S SD . MET A 1 794 ? -34.107 49.484 66.028 1.00 71.77 ? 794 MET A SD 1 ATOM 6147 C CE . MET A 1 794 ? -33.738 49.264 67.766 1.00 65.03 ? 794 MET A CE 1 ATOM 6148 N N . LEU A 1 795 ? -32.784 44.906 66.293 1.00 73.70 ? 795 LEU A N 1 ATOM 6149 C CA . LEU A 1 795 ? -32.284 43.615 66.747 1.00 55.57 ? 795 LEU A CA 1 ATOM 6150 C C . LEU A 1 795 ? -32.101 43.623 68.260 1.00 67.46 ? 795 LEU A C 1 ATOM 6151 O O . LEU A 1 795 ? -31.397 44.474 68.804 1.00 91.03 ? 795 LEU A O 1 ATOM 6152 C CB . LEU A 1 795 ? -30.964 43.275 66.052 1.00 50.58 ? 795 LEU A CB 1 ATOM 6153 C CG . LEU A 1 795 ? -30.441 41.848 66.219 1.00 49.54 ? 795 LEU A CG 1 ATOM 6154 C CD1 . LEU A 1 795 ? -31.389 40.857 65.566 1.00 64.36 ? 795 LEU A CD1 1 ATOM 6155 C CD2 . LEU A 1 795 ? -29.044 41.717 65.637 1.00 49.78 ? 795 LEU A CD2 1 ATOM 6156 N N . HIS A 1 796 ? -32.741 42.677 68.937 1.00 60.57 ? 796 HIS A N 1 ATOM 6157 C CA . HIS A 1 796 ? -32.666 42.604 70.391 1.00 64.26 ? 796 HIS A CA 1 ATOM 6158 C C . HIS A 1 796 ? -32.000 41.317 70.857 1.00 69.87 ? 796 HIS A C 1 ATOM 6159 O O . HIS A 1 796 ? -32.434 40.221 70.510 1.00 74.15 ? 796 HIS A O 1 ATOM 6160 C CB . HIS A 1 796 ? -34.061 42.719 71.005 1.00 58.54 ? 796 HIS A CB 1 ATOM 6161 C CG . HIS A 1 796 ? -34.706 44.050 70.785 1.00 67.62 ? 796 HIS A CG 1 ATOM 6162 N ND1 . HIS A 1 796 ? -34.645 45.069 71.711 1.00 71.93 ? 796 HIS A ND1 1 ATOM 6163 C CD2 . HIS A 1 796 ? -35.421 44.532 69.741 1.00 70.04 ? 796 HIS A CD2 1 ATOM 6164 C CE1 . HIS A 1 796 ? -35.298 46.120 71.248 1.00 61.99 ? 796 HIS A CE1 1 ATOM 6165 N NE2 . HIS A 1 796 ? -35.778 45.821 70.055 1.00 70.80 ? 796 HIS A NE2 1 ATOM 6166 N N . LEU A 1 797 ? -30.940 41.462 71.644 1.00 56.99 ? 797 LEU A N 1 ATOM 6167 C CA . LEU A 1 797 ? -30.244 40.316 72.209 1.00 54.20 ? 797 LEU A CA 1 ATOM 6168 C C . LEU A 1 797 ? -30.454 40.253 73.716 1.00 61.31 ? 797 LEU A C 1 ATOM 6169 O O . LEU A 1 797 ? -30.307 41.257 74.412 1.00 71.76 ? 797 LEU A O 1 ATOM 6170 C CB . LEU A 1 797 ? -28.749 40.381 71.887 1.00 52.66 ? 797 LEU A CB 1 ATOM 6171 C CG . LEU A 1 797 ? -27.858 39.344 72.574 1.00 55.15 ? 797 LEU A CG 1 ATOM 6172 C CD1 . LEU A 1 797 ? -28.297 37.935 72.215 1.00 64.52 ? 797 LEU A CD1 1 ATOM 6173 C CD2 . LEU A 1 797 ? -26.398 39.561 72.212 1.00 52.26 ? 797 LEU A CD2 1 ATOM 6174 N N . GLN A 1 798 ? -30.806 39.073 74.214 1.00 56.13 ? 798 GLN A N 1 ATOM 6175 C CA . GLN A 1 798 ? -30.941 38.868 75.649 1.00 64.07 ? 798 GLN A CA 1 ATOM 6176 C C . GLN A 1 798 ? -29.865 37.909 76.145 1.00 74.45 ? 798 GLN A C 1 ATOM 6177 O O . GLN A 1 798 ? -29.902 36.713 75.855 1.00 97.75 ? 798 GLN A O 1 ATOM 6178 C CB . GLN A 1 798 ? -32.333 38.336 75.992 1.00 65.76 ? 798 GLN A CB 1 ATOM 6179 C CG . GLN A 1 798 ? -33.467 39.223 75.508 1.00 64.37 ? 798 GLN A CG 1 ATOM 6180 C CD . GLN A 1 798 ? -34.798 38.871 76.145 1.00 68.34 ? 798 GLN A CD 1 ATOM 6181 O OE1 . GLN A 1 798 ? -34.859 38.077 77.084 1.00 68.51 ? 798 GLN A OE1 1 ATOM 6182 N NE2 . GLN A 1 798 ? -35.872 39.464 75.638 1.00 83.44 ? 798 GLN A NE2 1 ATOM 6183 N N . TRP A 1 799 ? -28.903 38.445 76.889 1.00 66.39 ? 799 TRP A N 1 ATOM 6184 C CA . TRP A 1 799 ? -27.784 37.655 77.387 1.00 68.38 ? 799 TRP A CA 1 ATOM 6185 C C . TRP A 1 799 ? -27.942 37.309 78.865 1.00 82.34 ? 799 TRP A C 1 ATOM 6186 O O . TRP A 1 799 ? -28.212 38.187 79.685 1.00 91.97 ? 799 TRP A O 1 ATOM 6187 C CB . TRP A 1 799 ? -26.467 38.398 77.161 1.00 66.25 ? 799 TRP A CB 1 ATOM 6188 C CG . TRP A 1 799 ? -25.268 37.510 77.221 1.00 70.20 ? 799 TRP A CG 1 ATOM 6189 C CD1 . TRP A 1 799 ? -24.491 37.254 78.312 1.00 73.61 ? 799 TRP A CD1 1 ATOM 6190 C CD2 . TRP A 1 799 ? -24.707 36.754 76.141 1.00 72.76 ? 799 TRP A CD2 1 ATOM 6191 N NE1 . TRP A 1 799 ? -23.479 36.387 77.978 1.00 70.66 ? 799 TRP A NE1 1 ATOM 6192 C CE2 . TRP A 1 799 ? -23.590 36.065 76.651 1.00 70.27 ? 799 TRP A CE2 1 ATOM 6193 C CE3 . TRP A 1 799 ? -25.041 36.594 74.793 1.00 76.22 ? 799 TRP A CE3 1 ATOM 6194 C CZ2 . TRP A 1 799 ? -22.804 35.228 75.861 1.00 75.21 ? 799 TRP A CZ2 1 ATOM 6195 C CZ3 . TRP A 1 799 ? -24.260 35.763 74.010 1.00 80.35 ? 799 TRP A CZ3 1 ATOM 6196 C CH2 . TRP A 1 799 ? -23.155 35.091 74.546 1.00 80.47 ? 799 TRP A CH2 1 ATOM 6197 N N . PRO A 1 800 ? -27.776 36.023 79.209 1.00 83.87 ? 800 PRO A N 1 ATOM 6198 C CA . PRO A 1 800 ? -27.826 35.561 80.601 1.00 83.25 ? 800 PRO A CA 1 ATOM 6199 C C . PRO A 1 800 ? -26.615 36.042 81.395 1.00 87.25 ? 800 PRO A C 1 ATOM 6200 O O . PRO A 1 800 ? -25.687 35.266 81.625 1.00 92.44 ? 800 PRO A O 1 ATOM 6201 C CB . PRO A 1 800 ? -27.818 34.032 80.473 1.00 80.36 ? 800 PRO A CB 1 ATOM 6202 C CG . PRO A 1 800 ? -28.135 33.746 79.039 1.00 76.91 ? 800 PRO A CG 1 ATOM 6203 C CD . PRO A 1 800 ? -27.602 34.906 78.267 1.00 80.39 ? 800 PRO A CD 1 ATOM 6204 N N . TYR A 1 801 ? -26.630 37.308 81.799 1.00 87.33 ? 801 TYR A N 1 ATOM 6205 C CA . TYR A 1 801 ? -25.482 37.928 82.454 1.00 86.51 ? 801 TYR A CA 1 ATOM 6206 C C . TYR A 1 801 ? -25.096 37.257 83.769 1.00 89.59 ? 801 TYR A C 1 ATOM 6207 O O . TYR A 1 801 ? -23.971 36.781 83.922 1.00 94.32 ? 801 TYR A O 1 ATOM 6208 C CB . TYR A 1 801 ? -25.761 39.412 82.700 1.00 88.32 ? 801 TYR A CB 1 ATOM 6209 C CG . TYR A 1 801 ? -24.643 40.135 83.415 1.00 93.93 ? 801 TYR A CG 1 ATOM 6210 C CD1 . TYR A 1 801 ? -23.369 40.199 82.864 1.00 95.50 ? 801 TYR A CD1 1 ATOM 6211 C CD2 . TYR A 1 801 ? -24.862 40.762 84.634 1.00 104.85 ? 801 TYR A CD2 1 ATOM 6212 C CE1 . TYR A 1 801 ? -22.343 40.860 83.512 1.00 112.63 ? 801 TYR A CE1 1 ATOM 6213 C CE2 . TYR A 1 801 ? -23.842 41.426 85.290 1.00 124.63 ? 801 TYR A CE2 1 ATOM 6214 C CZ . TYR A 1 801 ? -22.585 41.472 84.724 1.00 133.20 ? 801 TYR A CZ 1 ATOM 6215 O OH . TYR A 1 801 ? -21.567 42.133 85.372 1.00 144.94 ? 801 TYR A OH 1 ATOM 6216 N N . LYS A 1 802 ? -26.028 37.217 84.715 1.00 89.05 ? 802 LYS A N 1 ATOM 6217 C CA . LYS A 1 802 ? -25.748 36.641 86.026 1.00 90.01 ? 802 LYS A CA 1 ATOM 6218 C C . LYS A 1 802 ? -26.905 35.808 86.560 1.00 90.86 ? 802 LYS A C 1 ATOM 6219 O O . LYS A 1 802 ? -28.060 36.013 86.189 1.00 100.38 ? 802 LYS A O 1 ATOM 6220 C CB . LYS A 1 802 ? -25.409 37.740 87.037 1.00 92.42 ? 802 LYS A CB 1 ATOM 6221 C CG . LYS A 1 802 ? -23.989 38.270 86.945 1.00 103.13 ? 802 LYS A CG 1 ATOM 6222 C CD . LYS A 1 802 ? -23.661 39.178 88.121 1.00 109.94 ? 802 LYS A CD 1 ATOM 6223 C CE . LYS A 1 802 ? -22.198 39.595 88.109 1.00 105.40 ? 802 LYS A CE 1 ATOM 6224 N NZ . LYS A 1 802 ? -21.842 40.424 89.294 1.00 109.45 ? 802 LYS A NZ 1 ATOM 6225 N N . TYR A 1 803 ? -26.573 34.865 87.434 1.00 91.88 ? 803 TYR A N 1 ATOM 6226 C CA . TYR A 1 803 ? -27.569 34.074 88.143 1.00 91.74 ? 803 TYR A CA 1 ATOM 6227 C C . TYR A 1 803 ? -27.217 34.038 89.625 1.00 92.95 ? 803 TYR A C 1 ATOM 6228 O O . TYR A 1 803 ? -26.178 33.499 90.004 1.00 93.69 ? 803 TYR A O 1 ATOM 6229 C CB . TYR A 1 803 ? -27.646 32.659 87.565 1.00 91.43 ? 803 TYR A CB 1 ATOM 6230 C CG . TYR A 1 803 ? -28.606 31.741 88.288 1.00 97.24 ? 803 TYR A CG 1 ATOM 6231 C CD1 . TYR A 1 803 ? -28.146 30.624 88.974 1.00 97.71 ? 803 TYR A CD1 1 ATOM 6232 C CD2 . TYR A 1 803 ? -29.972 31.992 88.287 1.00 110.31 ? 803 TYR A CD2 1 ATOM 6233 C CE1 . TYR A 1 803 ? -29.019 29.781 89.635 1.00 100.93 ? 803 TYR A CE1 1 ATOM 6234 C CE2 . TYR A 1 803 ? -30.853 31.156 88.947 1.00 110.16 ? 803 TYR A CE2 1 ATOM 6235 C CZ . TYR A 1 803 ? -30.371 30.052 89.619 1.00 104.60 ? 803 TYR A CZ 1 ATOM 6236 O OH . TYR A 1 803 ? -31.244 29.217 90.277 1.00 109.59 ? 803 TYR A OH 1 ATOM 6237 N N . ASN A 1 804 ? -28.086 34.615 90.450 1.00 94.24 ? 804 ASN A N 1 ATOM 6238 C CA . ASN A 1 804 ? -27.848 34.733 91.888 1.00 98.57 ? 804 ASN A CA 1 ATOM 6239 C C . ASN A 1 804 ? -26.524 35.424 92.213 1.00 97.78 ? 804 ASN A C 1 ATOM 6240 O O . ASN A 1 804 ? -25.678 34.862 92.911 1.00 107.47 ? 804 ASN A O 1 ATOM 6241 C CB . ASN A 1 804 ? -27.900 33.357 92.559 1.00 110.66 ? 804 ASN A CB 1 ATOM 6242 C CG . ASN A 1 804 ? -29.274 32.720 92.475 1.00 120.92 ? 804 ASN A CG 1 ATOM 6243 O OD1 . ASN A 1 804 ? -30.264 33.390 92.178 1.00 125.53 ? 804 ASN A OD1 1 ATOM 6244 N ND2 . ASN A 1 804 ? -29.342 31.422 92.744 1.00 125.01 ? 804 ASN A ND2 1 ATOM 6245 N N . ASN A 1 805 ? -26.351 36.626 91.665 1.00 95.88 ? 805 ASN A N 1 ATOM 6246 C CA . ASN A 1 805 ? -25.235 37.523 91.985 1.00 102.01 ? 805 ASN A CA 1 ATOM 6247 C C . ASN A 1 805 ? -23.865 37.083 91.459 1.00 110.88 ? 805 ASN A C 1 ATOM 6248 O O . ASN A 1 805 ? -22.882 37.806 91.621 1.00 120.53 ? 805 ASN A O 1 ATOM 6249 C CB . ASN A 1 805 ? -25.146 37.740 93.501 1.00 112.73 ? 805 ASN A CB 1 ATOM 6250 C CG . ASN A 1 805 ? -26.406 38.355 94.077 1.00 114.68 ? 805 ASN A CG 1 ATOM 6251 O OD1 . ASN A 1 805 ? -27.148 39.047 93.380 1.00 103.60 ? 805 ASN A OD1 1 ATOM 6252 N ND2 . ASN A 1 805 ? -26.654 38.107 95.358 1.00 118.09 ? 805 ASN A ND2 1 ATOM 6253 N N . ASN A 1 806 ? -23.791 35.910 90.837 1.00 108.64 ? 806 ASN A N 1 ATOM 6254 C CA . ASN A 1 806 ? -22.534 35.461 90.241 1.00 93.74 ? 806 ASN A CA 1 ATOM 6255 C C . ASN A 1 806 ? -22.632 35.296 88.723 1.00 88.57 ? 806 ASN A C 1 ATOM 6256 O O . ASN A 1 806 ? -23.657 34.865 88.196 1.00 85.31 ? 806 ASN A O 1 ATOM 6257 C CB . ASN A 1 806 ? -22.064 34.154 90.888 1.00 93.84 ? 806 ASN A CB 1 ATOM 6258 C CG . ASN A 1 806 ? -23.186 33.397 91.570 1.00 96.13 ? 806 ASN A CG 1 ATOM 6259 O OD1 . ASN A 1 806 ? -23.799 32.509 90.979 1.00 95.11 ? 806 ASN A OD1 1 ATOM 6260 N ND2 . ASN A 1 806 ? -23.454 33.739 92.825 1.00 100.99 ? 806 ASN A ND2 1 ATOM 6261 N N . THR A 1 807 ? -21.548 35.642 88.034 1.00 88.00 ? 807 THR A N 1 ATOM 6262 C CA . THR A 1 807 ? -21.523 35.709 86.574 1.00 86.10 ? 807 THR A CA 1 ATOM 6263 C C . THR A 1 807 ? -21.623 34.339 85.905 1.00 86.10 ? 807 THR A C 1 ATOM 6264 O O . THR A 1 807 ? -21.040 33.365 86.377 1.00 94.46 ? 807 THR A O 1 ATOM 6265 C CB . THR A 1 807 ? -20.236 36.405 86.079 1.00 86.14 ? 807 THR A CB 1 ATOM 6266 O OG1 . THR A 1 807 ? -19.959 37.548 86.898 1.00 87.67 ? 807 THR A OG1 1 ATOM 6267 C CG2 . THR A 1 807 ? -20.381 36.844 84.628 1.00 85.80 ? 807 THR A CG2 1 ATOM 6268 N N . LEU A 1 808 ? -22.360 34.276 84.799 1.00 84.87 ? 808 LEU A N 1 ATOM 6269 C CA . LEU A 1 808 ? -22.471 33.050 84.016 1.00 82.73 ? 808 LEU A CA 1 ATOM 6270 C C . LEU A 1 808 ? -21.565 33.114 82.792 1.00 87.77 ? 808 LEU A C 1 ATOM 6271 O O . LEU A 1 808 ? -20.523 32.461 82.741 1.00 108.97 ? 808 LEU A O 1 ATOM 6272 C CB . LEU A 1 808 ? -23.919 32.815 83.582 1.00 80.79 ? 808 LEU A CB 1 ATOM 6273 C CG . LEU A 1 808 ? -24.930 32.487 84.681 1.00 83.59 ? 808 LEU A CG 1 ATOM 6274 C CD1 . LEU A 1 808 ? -26.325 32.345 84.096 1.00 82.47 ? 808 LEU A CD1 1 ATOM 6275 C CD2 . LEU A 1 808 ? -24.522 31.220 85.411 1.00 87.72 ? 808 LEU A CD2 1 ATOM 6276 N N . LEU A 1 809 ? -21.971 33.910 81.809 1.00 78.34 ? 809 LEU A N 1 ATOM 6277 C CA . LEU A 1 809 ? -21.152 34.154 80.630 1.00 76.65 ? 809 LEU A CA 1 ATOM 6278 C C . LEU A 1 809 ? -20.665 35.595 80.630 1.00 85.44 ? 809 LEU A C 1 ATOM 6279 O O . LEU A 1 809 ? -21.454 36.528 80.491 1.00 98.81 ? 809 LEU A O 1 ATOM 6280 C CB . LEU A 1 809 ? -21.931 33.855 79.349 1.00 73.96 ? 809 LEU A CB 1 ATOM 6281 C CG . LEU A 1 809 ? -22.151 32.380 79.014 1.00 79.25 ? 809 LEU A CG 1 ATOM 6282 C CD1 . LEU A 1 809 ? -23.059 32.229 77.804 1.00 88.47 ? 809 LEU A CD1 1 ATOM 6283 C CD2 . LEU A 1 809 ? -20.820 31.682 78.777 1.00 76.77 ? 809 LEU A CD2 1 ATOM 6284 N N . TYR A 1 810 ? -19.358 35.769 80.789 1.00 79.36 ? 810 TYR A N 1 ATOM 6285 C CA . TYR A 1 810 ? -18.772 37.098 80.877 1.00 80.93 ? 810 TYR A CA 1 ATOM 6286 C C . TYR A 1 810 ? -18.371 37.595 79.494 1.00 78.85 ? 810 TYR A C 1 ATOM 6287 O O . TYR A 1 810 ? -17.470 37.044 78.863 1.00 78.20 ? 810 TYR A O 1 ATOM 6288 C CB . TYR A 1 810 ? -17.566 37.076 81.818 1.00 77.19 ? 810 TYR A CB 1 ATOM 6289 C CG . TYR A 1 810 ? -16.910 38.419 82.038 1.00 80.56 ? 810 TYR A CG 1 ATOM 6290 C CD1 . TYR A 1 810 ? -17.395 39.305 82.990 1.00 83.24 ? 810 TYR A CD1 1 ATOM 6291 C CD2 . TYR A 1 810 ? -15.792 38.791 81.308 1.00 81.63 ? 810 TYR A CD2 1 ATOM 6292 C CE1 . TYR A 1 810 ? -16.790 40.531 83.197 1.00 90.96 ? 810 TYR A CE1 1 ATOM 6293 C CE2 . TYR A 1 810 ? -15.182 40.009 81.506 1.00 85.05 ? 810 TYR A CE2 1 ATOM 6294 C CZ . TYR A 1 810 ? -15.683 40.876 82.450 1.00 92.00 ? 810 TYR A CZ 1 ATOM 6295 O OH . TYR A 1 810 ? -15.069 42.090 82.647 1.00 95.39 ? 810 TYR A OH 1 ATOM 6296 N N . ILE A 1 811 ? -19.047 38.642 79.032 1.00 82.66 ? 811 ILE A N 1 ATOM 6297 C CA . ILE A 1 811 ? -18.809 39.183 77.699 1.00 78.75 ? 811 ILE A CA 1 ATOM 6298 C C . ILE A 1 811 ? -17.587 40.095 77.687 1.00 83.74 ? 811 ILE A C 1 ATOM 6299 O O . ILE A 1 811 ? -17.459 40.991 78.521 1.00 86.79 ? 811 ILE A O 1 ATOM 6300 C CB . ILE A 1 811 ? -20.035 39.961 77.180 1.00 68.19 ? 811 ILE A CB 1 ATOM 6301 C CG1 . ILE A 1 811 ? -21.261 39.047 77.123 1.00 64.61 ? 811 ILE A CG1 1 ATOM 6302 C CG2 . ILE A 1 811 ? -19.754 40.556 75.809 1.00 66.09 ? 811 ILE A CG2 1 ATOM 6303 C CD1 . ILE A 1 811 ? -22.495 39.711 76.551 1.00 60.53 ? 811 ILE A CD1 1 ATOM 6304 N N . LEU A 1 812 ? -16.690 39.854 76.736 1.00 80.38 ? 812 LEU A N 1 ATOM 6305 C CA . LEU A 1 812 ? -15.471 40.644 76.605 1.00 78.85 ? 812 LEU A CA 1 ATOM 6306 C C . LEU A 1 812 ? -15.637 41.725 75.553 1.00 94.96 ? 812 LEU A C 1 ATOM 6307 O O . LEU A 1 812 ? -15.697 42.915 75.864 1.00 99.44 ? 812 LEU A O 1 ATOM 6308 C CB . LEU A 1 812 ? -14.282 39.752 76.239 1.00 86.25 ? 812 LEU A CB 1 ATOM 6309 C CG . LEU A 1 812 ? -13.506 39.059 77.360 1.00 90.00 ? 812 LEU A CG 1 ATOM 6310 C CD1 . LEU A 1 812 ? -14.434 38.245 78.230 1.00 88.19 ? 812 LEU A CD1 1 ATOM 6311 C CD2 . LEU A 1 812 ? -12.413 38.177 76.776 1.00 94.48 ? 812 LEU A CD2 1 ATOM 6312 N N . HIS A 1 813 ? -15.710 41.292 74.301 1.00 91.30 ? 813 HIS A N 1 ATOM 6313 C CA . HIS A 1 813 ? -15.812 42.202 73.173 1.00 92.30 ? 813 HIS A CA 1 ATOM 6314 C C . HIS A 1 813 ? -16.728 41.622 72.106 1.00 86.92 ? 813 HIS A C 1 ATOM 6315 O O . HIS A 1 813 ? -16.710 40.419 71.848 1.00 90.16 ? 813 HIS A O 1 ATOM 6316 C CB . HIS A 1 813 ? -14.426 42.485 72.591 1.00 103.88 ? 813 HIS A CB 1 ATOM 6317 C CG . HIS A 1 813 ? -14.446 43.356 71.374 1.00 109.92 ? 813 HIS A CG 1 ATOM 6318 N ND1 . HIS A 1 813 ? -14.990 44.622 71.373 1.00 122.81 ? 813 HIS A ND1 1 ATOM 6319 C CD2 . HIS A 1 813 ? -13.983 43.144 70.119 1.00 106.47 ? 813 HIS A CD2 1 ATOM 6320 C CE1 . HIS A 1 813 ? -14.865 45.152 70.169 1.00 129.16 ? 813 HIS A CE1 1 ATOM 6321 N NE2 . HIS A 1 813 ? -14.257 44.276 69.390 1.00 120.61 ? 813 HIS A NE2 1 ATOM 6322 N N . TYR A 1 814 ? -17.536 42.480 71.493 1.00 84.05 ? 814 TYR A N 1 ATOM 6323 C CA . TYR A 1 814 ? -18.401 42.053 70.403 1.00 78.82 ? 814 TYR A CA 1 ATOM 6324 C C . TYR A 1 814 ? -18.140 42.898 69.164 1.00 79.92 ? 814 TYR A C 1 ATOM 6325 O O . TYR A 1 814 ? -17.969 44.114 69.256 1.00 82.82 ? 814 TYR A O 1 ATOM 6326 C CB . TYR A 1 814 ? -19.876 42.135 70.812 1.00 73.24 ? 814 TYR A CB 1 ATOM 6327 C CG . TYR A 1 814 ? -20.395 43.542 71.029 1.00 78.50 ? 814 TYR A CG 1 ATOM 6328 C CD1 . TYR A 1 814 ? -20.235 44.182 72.251 1.00 82.07 ? 814 TYR A CD1 1 ATOM 6329 C CD2 . TYR A 1 814 ? -21.056 44.224 70.014 1.00 82.80 ? 814 TYR A CD2 1 ATOM 6330 C CE1 . TYR A 1 814 ? -20.712 45.466 72.454 1.00 83.70 ? 814 TYR A CE1 1 ATOM 6331 C CE2 . TYR A 1 814 ? -21.533 45.506 70.208 1.00 78.69 ? 814 TYR A CE2 1 ATOM 6332 C CZ . TYR A 1 814 ? -21.360 46.122 71.428 1.00 76.95 ? 814 TYR A CZ 1 ATOM 6333 O OH . TYR A 1 814 ? -21.835 47.399 71.624 1.00 74.79 ? 814 TYR A OH 1 ATOM 6334 N N . ASP A 1 815 ? -18.101 42.252 68.004 1.00 79.00 ? 815 ASP A N 1 ATOM 6335 C CA . ASP A 1 815 ? -17.879 42.971 66.758 1.00 87.36 ? 815 ASP A CA 1 ATOM 6336 C C . ASP A 1 815 ? -19.109 42.899 65.864 1.00 79.05 ? 815 ASP A C 1 ATOM 6337 O O . ASP A 1 815 ? -20.082 42.218 66.184 1.00 73.23 ? 815 ASP A O 1 ATOM 6338 C CB . ASP A 1 815 ? -16.657 42.414 66.027 1.00 100.44 ? 815 ASP A CB 1 ATOM 6339 C CG . ASP A 1 815 ? -15.377 42.588 66.821 1.00 109.97 ? 815 ASP A CG 1 ATOM 6340 O OD1 . ASP A 1 815 ? -14.733 43.650 66.687 1.00 117.76 ? 815 ASP A OD1 1 ATOM 6341 O OD2 . ASP A 1 815 ? -15.015 41.664 67.580 1.00 105.32 ? 815 ASP A OD2 1 ATOM 6342 N N . ILE A 1 816 ? -19.053 43.597 64.734 1.00 77.94 ? 816 ILE A N 1 ATOM 6343 C CA . ILE A 1 816 ? -20.204 43.717 63.848 1.00 74.10 ? 816 ILE A CA 1 ATOM 6344 C C . ILE A 1 816 ? -19.800 43.606 62.384 1.00 77.03 ? 816 ILE A C 1 ATOM 6345 O O . ILE A 1 816 ? -18.896 44.304 61.925 1.00 86.62 ? 816 ILE A O 1 ATOM 6346 C CB . ILE A 1 816 ? -20.938 45.062 64.054 1.00 67.54 ? 816 ILE A CB 1 ATOM 6347 C CG1 . ILE A 1 816 ? -21.450 45.192 65.490 1.00 71.74 ? 816 ILE A CG1 1 ATOM 6348 C CG2 . ILE A 1 816 ? -22.089 45.200 63.071 1.00 65.74 ? 816 ILE A CG2 1 ATOM 6349 C CD1 . ILE A 1 816 ? -21.949 46.577 65.831 1.00 85.28 ? 816 ILE A CD1 1 ATOM 6350 N N . ASP A 1 817 ? -20.475 42.725 61.653 1.00 72.73 ? 817 ASP A N 1 ATOM 6351 C CA . ASP A 1 817 ? -20.287 42.628 60.212 1.00 74.61 ? 817 ASP A CA 1 ATOM 6352 C C . ASP A 1 817 ? -21.533 43.124 59.489 1.00 72.26 ? 817 ASP A C 1 ATOM 6353 O O . ASP A 1 817 ? -22.632 42.612 59.703 1.00 68.04 ? 817 ASP A O 1 ATOM 6354 C CB . ASP A 1 817 ? -19.966 41.191 59.798 1.00 83.67 ? 817 ASP A CB 1 ATOM 6355 C CG . ASP A 1 817 ? -18.554 41.041 59.266 1.00 101.13 ? 817 ASP A CG 1 ATOM 6356 O OD1 . ASP A 1 817 ? -17.937 39.980 59.501 1.00 91.00 ? 817 ASP A OD1 1 ATOM 6357 O OD2 . ASP A 1 817 ? -18.060 41.985 58.614 1.00 122.75 ? 817 ASP A OD2 1 ATOM 6358 N N . GLY A 1 818 ? -21.358 44.127 58.637 1.00 75.30 ? 818 GLY A N 1 ATOM 6359 C CA . GLY A 1 818 ? -22.469 44.693 57.895 1.00 73.41 ? 818 GLY A CA 1 ATOM 6360 C C . GLY A 1 818 ? -22.945 46.016 58.463 1.00 73.57 ? 818 GLY A C 1 ATOM 6361 O O . GLY A 1 818 ? -22.322 46.567 59.371 1.00 74.20 ? 818 GLY A O 1 ATOM 6362 N N . PRO A 1 819 ? -24.062 46.532 57.928 1.00 78.05 ? 819 PRO A N 1 ATOM 6363 C CA . PRO A 1 819 ? -24.630 47.826 58.318 1.00 74.78 ? 819 PRO A CA 1 ATOM 6364 C C . PRO A 1 819 ? -25.425 47.753 59.617 1.00 68.76 ? 819 PRO A C 1 ATOM 6365 O O . PRO A 1 819 ? -26.656 47.732 59.587 1.00 65.89 ? 819 PRO A O 1 ATOM 6366 C CB . PRO A 1 819 ? -25.544 48.167 57.141 1.00 74.41 ? 819 PRO A CB 1 ATOM 6367 C CG . PRO A 1 819 ? -25.996 46.837 56.641 1.00 67.52 ? 819 PRO A CG 1 ATOM 6368 C CD . PRO A 1 819 ? -24.850 45.883 56.865 1.00 78.13 ? 819 PRO A CD 1 ATOM 6369 N N . MET A 1 820 ? -24.729 47.711 60.747 1.00 69.86 ? 820 MET A N 1 ATOM 6370 C CA . MET A 1 820 ? -25.402 47.652 62.036 1.00 67.30 ? 820 MET A CA 1 ATOM 6371 C C . MET A 1 820 ? -24.624 48.389 63.124 1.00 70.82 ? 820 MET A C 1 ATOM 6372 O O . MET A 1 820 ? -23.398 48.303 63.193 1.00 74.81 ? 820 MET A O 1 ATOM 6373 C CB . MET A 1 820 ? -25.622 46.192 62.445 1.00 57.03 ? 820 MET A CB 1 ATOM 6374 C CG . MET A 1 820 ? -26.512 46.004 63.662 1.00 53.85 ? 820 MET A CG 1 ATOM 6375 S SD . MET A 1 820 ? -26.442 44.327 64.324 1.00 96.10 ? 820 MET A SD 1 ATOM 6376 C CE . MET A 1 820 ? -27.068 43.372 62.948 1.00 50.54 ? 820 MET A CE 1 ATOM 6377 N N . ASN A 1 821 ? -25.349 49.114 63.968 1.00 70.13 ? 821 ASN A N 1 ATOM 6378 C CA . ASN A 1 821 ? -24.778 49.709 65.168 1.00 73.25 ? 821 ASN A CA 1 ATOM 6379 C C . ASN A 1 821 ? -25.381 49.024 66.386 1.00 69.05 ? 821 ASN A C 1 ATOM 6380 O O . ASN A 1 821 ? -26.570 48.715 66.395 1.00 66.15 ? 821 ASN A O 1 ATOM 6381 C CB . ASN A 1 821 ? -25.037 51.218 65.221 1.00 86.30 ? 821 ASN A CB 1 ATOM 6382 C CG . ASN A 1 821 ? -24.247 51.990 64.177 1.00 105.92 ? 821 ASN A CG 1 ATOM 6383 O OD1 . ASN A 1 821 ? -23.261 51.495 63.632 1.00 105.18 ? 821 ASN A OD1 1 ATOM 6384 N ND2 . ASN A 1 821 ? -24.679 53.218 63.901 1.00 136.52 ? 821 ASN A ND2 1 ATOM 6385 N N . CYS A 1 822 ? -24.569 48.778 67.408 1.00 70.28 ? 822 CYS A N 1 ATOM 6386 C CA . CYS A 1 822 ? -25.052 48.067 68.587 1.00 64.67 ? 822 CYS A CA 1 ATOM 6387 C C . CYS A 1 822 ? -24.749 48.812 69.881 1.00 66.37 ? 822 CYS A C 1 ATOM 6388 O O . CYS A 1 822 ? -23.779 49.566 69.968 1.00 71.80 ? 822 CYS A O 1 ATOM 6389 C CB . CYS A 1 822 ? -24.450 46.662 68.643 1.00 63.78 ? 822 CYS A CB 1 ATOM 6390 S SG . CYS A 1 822 ? -25.008 45.564 67.322 1.00 106.87 ? 822 CYS A SG 1 ATOM 6391 N N . THR A 1 823 ? -25.590 48.587 70.885 1.00 71.16 ? 823 THR A N 1 ATOM 6392 C CA . THR A 1 823 ? -25.450 49.244 72.178 1.00 74.80 ? 823 THR A CA 1 ATOM 6393 C C . THR A 1 823 ? -25.756 48.268 73.309 1.00 76.12 ? 823 THR A C 1 ATOM 6394 O O . THR A 1 823 ? -26.723 47.509 73.240 1.00 75.61 ? 823 THR A O 1 ATOM 6395 C CB . THR A 1 823 ? -26.382 50.467 72.293 1.00 68.79 ? 823 THR A CB 1 ATOM 6396 O OG1 . THR A 1 823 ? -26.221 51.308 71.144 1.00 96.06 ? 823 THR A OG1 1 ATOM 6397 C CG2 . THR A 1 823 ? -26.073 51.265 73.552 1.00 72.82 ? 823 THR A CG2 1 ATOM 6398 N N . SER A 1 824 ? -24.927 48.286 74.347 1.00 67.09 ? 824 SER A N 1 ATOM 6399 C CA . SER A 1 824 ? -25.130 47.418 75.501 1.00 66.88 ? 824 SER A CA 1 ATOM 6400 C C . SER A 1 824 ? -25.633 48.218 76.697 1.00 75.07 ? 824 SER A C 1 ATOM 6401 O O . SER A 1 824 ? -25.064 49.252 77.043 1.00 88.88 ? 824 SER A O 1 ATOM 6402 C CB . SER A 1 824 ? -23.834 46.689 75.858 1.00 74.23 ? 824 SER A CB 1 ATOM 6403 O OG . SER A 1 824 ? -24.009 45.868 76.999 1.00 89.20 ? 824 SER A OG 1 ATOM 6404 N N . ASP A 1 825 ? -26.701 47.734 77.326 1.00 73.82 ? 825 ASP A N 1 ATOM 6405 C CA . ASP A 1 825 ? -27.281 48.416 78.479 1.00 82.09 ? 825 ASP A CA 1 ATOM 6406 C C . ASP A 1 825 ? -26.354 48.326 79.687 1.00 85.19 ? 825 ASP A C 1 ATOM 6407 O O . ASP A 1 825 ? -26.419 49.152 80.598 1.00 92.12 ? 825 ASP A O 1 ATOM 6408 C CB . ASP A 1 825 ? -28.657 47.834 78.816 1.00 87.79 ? 825 ASP A CB 1 ATOM 6409 C CG . ASP A 1 825 ? -28.589 46.386 79.266 1.00 98.17 ? 825 ASP A CG 1 ATOM 6410 O OD1 . ASP A 1 825 ? -27.600 45.699 78.936 1.00 111.01 ? 825 ASP A OD1 1 ATOM 6411 O OD2 . ASP A 1 825 ? -29.532 45.933 79.948 1.00 97.63 ? 825 ASP A OD2 1 ATOM 6412 N N . MET A 1 826 ? -25.493 47.314 79.688 1.00 75.83 ? 826 MET A N 1 ATOM 6413 C CA . MET A 1 826 ? -24.469 47.176 80.715 1.00 79.50 ? 826 MET A CA 1 ATOM 6414 C C . MET A 1 826 ? -23.089 47.270 80.080 1.00 82.11 ? 826 MET A C 1 ATOM 6415 O O . MET A 1 826 ? -22.892 46.835 78.946 1.00 83.95 ? 826 MET A O 1 ATOM 6416 C CB . MET A 1 826 ? -24.618 45.850 81.463 1.00 79.59 ? 826 MET A CB 1 ATOM 6417 C CG . MET A 1 826 ? -26.007 45.601 82.023 1.00 95.28 ? 826 MET A CG 1 ATOM 6418 S SD . MET A 1 826 ? -26.063 44.152 83.094 1.00 95.73 ? 826 MET A SD 1 ATOM 6419 C CE . MET A 1 826 ? -25.013 44.691 84.441 1.00 102.06 ? 826 MET A CE 1 ATOM 6420 N N . GLU A 1 827 ? -22.136 47.841 80.810 1.00 93.39 ? 827 GLU A N 1 ATOM 6421 C CA . GLU A 1 827 ? -20.781 47.995 80.296 1.00 97.11 ? 827 GLU A CA 1 ATOM 6422 C C . GLU A 1 827 ? -20.118 46.643 80.070 1.00 91.85 ? 827 GLU A C 1 ATOM 6423 O O . GLU A 1 827 ? -20.050 45.816 80.980 1.00 96.88 ? 827 GLU A O 1 ATOM 6424 C CB . GLU A 1 827 ? -19.930 48.831 81.254 1.00 108.91 ? 827 GLU A CB 1 ATOM 6425 C CG . GLU A 1 827 ? -18.466 48.924 80.851 1.00 115.30 ? 827 GLU A CG 1 ATOM 6426 C CD . GLU A 1 827 ? -17.598 49.545 81.928 1.00 129.35 ? 827 GLU A CD 1 ATOM 6427 O OE1 . GLU A 1 827 ? -16.396 49.769 81.668 1.00 136.99 ? 827 GLU A OE1 1 ATOM 6428 O OE2 . GLU A 1 827 ? -18.114 49.806 83.035 1.00 135.70 ? 827 GLU A OE2 1 ATOM 6429 N N . ILE A 1 828 ? -19.628 46.423 78.855 1.00 87.03 ? 828 ILE A N 1 ATOM 6430 C CA . ILE A 1 828 ? -18.879 45.211 78.556 1.00 84.53 ? 828 ILE A CA 1 ATOM 6431 C C . ILE A 1 828 ? -17.472 45.338 79.125 1.00 90.54 ? 828 ILE A C 1 ATOM 6432 O O . ILE A 1 828 ? -16.873 46.415 79.088 1.00 101.73 ? 828 ILE A O 1 ATOM 6433 C CB . ILE A 1 828 ? -18.815 44.929 77.042 1.00 81.04 ? 828 ILE A CB 1 ATOM 6434 C CG1 . ILE A 1 828 ? -18.274 46.145 76.288 1.00 102.57 ? 828 ILE A CG1 1 ATOM 6435 C CG2 . ILE A 1 828 ? -20.191 44.549 76.515 1.00 72.82 ? 828 ILE A CG2 1 ATOM 6436 C CD1 . ILE A 1 828 ? -18.069 45.905 74.808 1.00 101.55 ? 828 ILE A CD1 1 ATOM 6437 N N . ASN A 1 829 ? -16.960 44.234 79.661 1.00 91.87 ? 829 ASN A N 1 ATOM 6438 C CA . ASN A 1 829 ? -15.656 44.210 80.319 1.00 99.21 ? 829 ASN A CA 1 ATOM 6439 C C . ASN A 1 829 ? -15.498 45.261 81.421 1.00 105.11 ? 829 ASN A C 1 ATOM 6440 O O . ASN A 1 829 ? -14.705 46.191 81.276 1.00 125.41 ? 829 ASN A O 1 ATOM 6441 C CB . ASN A 1 829 ? -14.539 44.388 79.286 1.00 101.52 ? 829 ASN A CB 1 ATOM 6442 C CG . ASN A 1 829 ? -13.892 43.076 78.893 1.00 104.55 ? 829 ASN A CG 1 ATOM 6443 O OD1 . ASN A 1 829 ? -13.890 42.117 79.663 1.00 99.66 ? 829 ASN A OD1 1 ATOM 6444 N ND2 . ASN A 1 829 ? -13.331 43.029 77.690 1.00 115.29 ? 829 ASN A ND2 1 ATOM 6445 N N . PRO A 1 830 ? -16.256 45.124 82.524 1.00 103.50 ? 830 PRO A N 1 ATOM 6446 C CA . PRO A 1 830 ? -16.051 46.033 83.658 1.00 117.95 ? 830 PRO A CA 1 ATOM 6447 C C . PRO A 1 830 ? -14.690 45.824 84.322 1.00 122.41 ? 830 PRO A C 1 ATOM 6448 O O . PRO A 1 830 ? -14.076 46.780 84.796 1.00 127.66 ? 830 PRO A O 1 ATOM 6449 C CB . PRO A 1 830 ? -17.191 45.666 84.615 1.00 119.29 ? 830 PRO A CB 1 ATOM 6450 C CG . PRO A 1 830 ? -17.560 44.270 84.249 1.00 107.23 ? 830 PRO A CG 1 ATOM 6451 C CD . PRO A 1 830 ? -17.367 44.187 82.766 1.00 99.66 ? 830 PRO A CD 1 ATOM 6452 N N . LEU A 1 831 ? -14.234 44.576 84.350 1.00 114.83 ? 831 LEU A N 1 ATOM 6453 C CA . LEU A 1 831 ? -12.933 44.228 84.909 1.00 117.52 ? 831 LEU A CA 1 ATOM 6454 C C . LEU A 1 831 ? -11.891 44.214 83.798 1.00 120.59 ? 831 LEU A C 1 ATOM 6455 O O . LEU A 1 831 ? -10.724 43.883 84.014 1.00 124.15 ? 831 LEU A O 1 ATOM 6456 C CB . LEU A 1 831 ? -12.997 42.866 85.601 1.00 114.04 ? 831 LEU A CB 1 ATOM 6457 C CG . LEU A 1 831 ? -14.297 42.577 86.356 1.00 110.95 ? 831 LEU A CG 1 ATOM 6458 C CD1 . LEU A 1 831 ? -14.323 41.143 86.862 1.00 108.81 ? 831 LEU A CD1 1 ATOM 6459 C CD2 . LEU A 1 831 ? -14.482 43.556 87.505 1.00 134.75 ? 831 LEU A CD2 1 ATOM 6460 N N . ARG A 1 832 ? -12.349 44.587 82.608 1.00 128.80 ? 832 ARG A N 1 ATOM 6461 C CA . ARG A 1 832 ? -11.610 44.459 81.356 1.00 132.45 ? 832 ARG A CA 1 ATOM 6462 C C . ARG A 1 832 ? -11.099 43.037 81.137 1.00 130.58 ? 832 ARG A C 1 ATOM 6463 O O . ARG A 1 832 ? -11.739 42.072 81.563 1.00 138.21 ? 832 ARG A O 1 ATOM 6464 C CB . ARG A 1 832 ? -10.438 45.447 81.314 1.00 131.37 ? 832 ARG A CB 1 ATOM 6465 C CG . ARG A 1 832 ? -10.841 46.915 81.382 1.00 131.45 ? 832 ARG A CG 1 ATOM 6466 C CD . ARG A 1 832 ? -10.836 47.438 82.812 1.00 135.71 ? 832 ARG A CD 1 ATOM 6467 N NE . ARG A 1 832 ? -11.204 48.849 82.879 1.00 151.55 ? 832 ARG A NE 1 ATOM 6468 C CZ . ARG A 1 832 ? -11.156 49.583 83.986 1.00 154.38 ? 832 ARG A CZ 1 ATOM 6469 N NH1 . ARG A 1 832 ? -10.750 49.043 85.127 1.00 150.54 ? 832 ARG A NH1 1 ATOM 6470 N NH2 . ARG A 1 832 ? -11.511 50.860 83.951 1.00 153.69 ? 832 ARG A NH2 1 ATOM 6471 N N . ILE A 1 833 ? -9.918 42.930 80.530 1.00 120.58 ? 833 ILE A N 1 ATOM 6472 C CA . ILE A 1 833 ? -9.363 41.656 80.074 1.00 119.12 ? 833 ILE A CA 1 ATOM 6473 C C . ILE A 1 833 ? -8.097 41.956 79.265 1.00 122.70 ? 833 ILE A C 1 ATOM 6474 O O . ILE A 1 833 ? -7.830 43.116 78.954 1.00 124.41 ? 833 ILE A O 1 ATOM 6475 C CB . ILE A 1 833 ? -10.401 40.853 79.220 1.00 140.63 ? 833 ILE A CB 1 ATOM 6476 C CG1 . ILE A 1 833 ? -10.544 39.409 79.725 1.00 141.42 ? 833 ILE A CG1 1 ATOM 6477 C CG2 . ILE A 1 833 ? -10.125 40.960 77.714 1.00 142.82 ? 833 ILE A CG2 1 ATOM 6478 C CD1 . ILE A 1 833 ? -9.296 38.572 79.623 1.00 152.67 ? 833 ILE A CD1 1 ATOM 6479 N N . LYS A 1 834 ? -7.313 40.934 78.931 1.00 124.45 ? 834 LYS A N 1 ATOM 6480 C CA . LYS A 1 834 ? -6.242 41.112 77.956 1.00 132.05 ? 834 LYS A CA 1 ATOM 6481 C C . LYS A 1 834 ? -6.660 40.563 76.592 1.00 137.87 ? 834 LYS A C 1 ATOM 6482 O O . LYS A 1 834 ? -7.022 41.328 75.697 1.00 130.67 ? 834 LYS A O 1 ATOM 6483 C CB . LYS A 1 834 ? -4.957 40.431 78.428 1.00 135.80 ? 834 LYS A CB 1 ATOM 6484 C CG . LYS A 1 834 ? -4.159 41.244 79.432 1.00 140.29 ? 834 LYS A CG 1 ATOM 6485 C CD . LYS A 1 834 ? -3.710 42.565 78.827 1.00 133.93 ? 834 LYS A CD 1 ATOM 6486 C CE . LYS A 1 834 ? -2.861 43.361 79.803 1.00 133.57 ? 834 LYS A CE 1 ATOM 6487 N NZ . LYS A 1 834 ? -3.609 43.694 81.046 1.00 131.48 ? 834 LYS A NZ 1 ATOM 6488 N N . ILE A 1 835 ? -6.636 39.238 76.458 1.00 145.32 ? 835 ILE A N 1 ATOM 6489 C CA . ILE A 1 835 ? -7.058 38.559 75.233 1.00 140.05 ? 835 ILE A CA 1 ATOM 6490 C C . ILE A 1 835 ? -7.036 37.045 75.420 1.00 133.12 ? 835 ILE A C 1 ATOM 6491 O O . ILE A 1 835 ? -6.331 36.525 76.286 1.00 129.27 ? 835 ILE A O 1 ATOM 6492 C CB . ILE A 1 835 ? -6.168 38.920 74.023 1.00 140.26 ? 835 ILE A CB 1 ATOM 6493 C CG1 . ILE A 1 835 ? -6.728 38.290 72.746 1.00 126.00 ? 835 ILE A CG1 1 ATOM 6494 C CG2 . ILE A 1 835 ? -4.731 38.482 74.261 1.00 149.68 ? 835 ILE A CG2 1 ATOM 6495 C CD1 . ILE A 1 835 ? -5.929 38.611 71.502 1.00 127.33 ? 835 ILE A CD1 1 ATOM 6496 N N . ASP A 1 868 ? -31.715 15.067 84.738 1.00 148.76 ? 868 ASP A N 1 ATOM 6497 C CA . ASP A 1 868 ? -32.458 16.270 84.382 1.00 150.74 ? 868 ASP A CA 1 ATOM 6498 C C . ASP A 1 868 ? -31.520 17.455 84.176 1.00 141.94 ? 868 ASP A C 1 ATOM 6499 O O . ASP A 1 868 ? -30.468 17.543 84.809 1.00 140.48 ? 868 ASP A O 1 ATOM 6500 C CB . ASP A 1 868 ? -33.494 16.599 85.459 1.00 164.56 ? 868 ASP A CB 1 ATOM 6501 C CG . ASP A 1 868 ? -32.865 16.859 86.814 1.00 176.58 ? 868 ASP A CG 1 ATOM 6502 O OD1 . ASP A 1 868 ? -31.809 16.258 87.107 1.00 179.62 ? 868 ASP A OD1 1 ATOM 6503 O OD2 . ASP A 1 868 ? -33.426 17.664 87.586 1.00 181.34 ? 868 ASP A OD2 1 ATOM 6504 N N . ILE A 1 869 ? -31.909 18.363 83.287 1.00 137.73 ? 869 ILE A N 1 ATOM 6505 C CA . ILE A 1 869 ? -31.091 19.530 82.974 1.00 129.83 ? 869 ILE A CA 1 ATOM 6506 C C . ILE A 1 869 ? -31.833 20.829 83.288 1.00 133.13 ? 869 ILE A C 1 ATOM 6507 O O . ILE A 1 869 ? -33.007 20.985 82.951 1.00 141.90 ? 869 ILE A O 1 ATOM 6508 C CB . ILE A 1 869 ? -30.649 19.520 81.490 1.00 120.71 ? 869 ILE A CB 1 ATOM 6509 C CG1 . ILE A 1 869 ? -29.908 20.810 81.135 1.00 106.37 ? 869 ILE A CG1 1 ATOM 6510 C CG2 . ILE A 1 869 ? -31.843 19.308 80.569 1.00 132.40 ? 869 ILE A CG2 1 ATOM 6511 C CD1 . ILE A 1 869 ? -29.236 20.775 79.785 1.00 100.06 ? 869 ILE A CD1 1 ATOM 6512 N N . HIS A 1 870 ? -31.143 21.754 83.949 1.00 123.59 ? 870 HIS A N 1 ATOM 6513 C CA . HIS A 1 870 ? -31.741 23.029 84.330 1.00 120.36 ? 870 HIS A CA 1 ATOM 6514 C C . HIS A 1 870 ? -31.393 24.123 83.324 1.00 107.53 ? 870 HIS A C 1 ATOM 6515 O O . HIS A 1 870 ? -30.221 24.423 83.097 1.00 101.26 ? 870 HIS A O 1 ATOM 6516 C CB . HIS A 1 870 ? -31.285 23.435 85.732 1.00 129.61 ? 870 HIS A CB 1 ATOM 6517 C CG . HIS A 1 870 ? -32.097 24.538 86.336 1.00 142.20 ? 870 HIS A CG 1 ATOM 6518 N ND1 . HIS A 1 870 ? -31.755 25.151 87.522 1.00 145.13 ? 870 HIS A ND1 1 ATOM 6519 C CD2 . HIS A 1 870 ? -33.239 25.136 85.920 1.00 139.06 ? 870 HIS A CD2 1 ATOM 6520 C CE1 . HIS A 1 870 ? -32.649 26.080 87.810 1.00 136.03 ? 870 HIS A CE1 1 ATOM 6521 N NE2 . HIS A 1 870 ? -33.560 26.091 86.854 1.00 131.49 ? 870 HIS A NE2 1 ATOM 6522 N N . THR A 1 871 ? -32.421 24.717 82.727 1.00 107.09 ? 871 THR A N 1 ATOM 6523 C CA . THR A 1 871 ? -32.236 25.756 81.721 1.00 97.87 ? 871 THR A CA 1 ATOM 6524 C C . THR A 1 871 ? -32.135 27.139 82.354 1.00 94.98 ? 871 THR A C 1 ATOM 6525 O O . THR A 1 871 ? -32.966 27.513 83.181 1.00 98.67 ? 871 THR A O 1 ATOM 6526 C CB . THR A 1 871 ? -33.391 25.760 80.700 1.00 98.60 ? 871 THR A CB 1 ATOM 6527 O OG1 . THR A 1 871 ? -33.554 24.447 80.150 1.00 113.81 ? 871 THR A OG1 1 ATOM 6528 C CG2 . THR A 1 871 ? -33.114 26.749 79.577 1.00 91.53 ? 871 THR A CG2 1 ATOM 6529 N N . LEU A 1 872 ? -31.115 27.897 81.965 1.00 89.61 ? 872 LEU A N 1 ATOM 6530 C CA . LEU A 1 872 ? -30.982 29.272 82.429 1.00 89.26 ? 872 LEU A CA 1 ATOM 6531 C C . LEU A 1 872 ? -31.172 30.252 81.278 1.00 97.52 ? 872 LEU A C 1 ATOM 6532 O O . LEU A 1 872 ? -30.307 30.388 80.412 1.00 94.37 ? 872 LEU A O 1 ATOM 6533 C CB . LEU A 1 872 ? -29.619 29.490 83.088 1.00 85.62 ? 872 LEU A CB 1 ATOM 6534 C CG . LEU A 1 872 ? -29.357 28.714 84.380 1.00 88.37 ? 872 LEU A CG 1 ATOM 6535 C CD1 . LEU A 1 872 ? -27.977 29.038 84.932 1.00 84.47 ? 872 LEU A CD1 1 ATOM 6536 C CD2 . LEU A 1 872 ? -30.435 29.014 85.409 1.00 93.87 ? 872 LEU A CD2 1 ATOM 6537 N N . GLY A 1 873 ? -32.308 30.940 81.283 1.00 103.76 ? 873 GLY A N 1 ATOM 6538 C CA . GLY A 1 873 ? -32.608 31.932 80.270 1.00 96.58 ? 873 GLY A CA 1 ATOM 6539 C C . GLY A 1 873 ? -32.489 33.333 80.830 1.00 101.08 ? 873 GLY A C 1 ATOM 6540 O O . GLY A 1 873 ? -32.162 33.514 82.003 1.00 97.61 ? 873 GLY A O 1 ATOM 6541 N N . CYS A 1 874 ? -32.760 34.330 79.994 1.00 107.83 ? 874 CYS A N 1 ATOM 6542 C CA . CYS A 1 874 ? -32.714 35.718 80.432 1.00 106.17 ? 874 CYS A CA 1 ATOM 6543 C C . CYS A 1 874 ? -33.917 36.036 81.315 1.00 107.20 ? 874 CYS A C 1 ATOM 6544 O O . CYS A 1 874 ? -33.924 37.031 82.038 1.00 113.03 ? 874 CYS A O 1 ATOM 6545 C CB . CYS A 1 874 ? -32.668 36.661 79.229 1.00 100.02 ? 874 CYS A CB 1 ATOM 6546 S SG . CYS A 1 874 ? -32.313 38.384 79.642 1.00 180.05 ? 874 CYS A SG 1 ATOM 6547 N N . GLY A 1 875 ? -34.933 35.182 81.249 1.00 105.25 ? 875 GLY A N 1 ATOM 6548 C CA . GLY A 1 875 ? -36.128 35.351 82.054 1.00 109.95 ? 875 GLY A CA 1 ATOM 6549 C C . GLY A 1 875 ? -35.935 34.930 83.499 1.00 111.01 ? 875 GLY A C 1 ATOM 6550 O O . GLY A 1 875 ? -36.402 35.604 84.417 1.00 118.39 ? 875 GLY A O 1 ATOM 6551 N N . VAL A 1 876 ? -35.244 33.812 83.702 1.00 110.82 ? 876 VAL A N 1 ATOM 6552 C CA . VAL A 1 876 ? -35.033 33.278 85.044 1.00 117.06 ? 876 VAL A CA 1 ATOM 6553 C C . VAL A 1 876 ? -33.706 33.738 85.644 1.00 110.27 ? 876 VAL A C 1 ATOM 6554 O O . VAL A 1 876 ? -33.346 33.336 86.751 1.00 97.68 ? 876 VAL A O 1 ATOM 6555 C CB . VAL A 1 876 ? -35.077 31.738 85.051 1.00 121.63 ? 876 VAL A CB 1 ATOM 6556 C CG1 . VAL A 1 876 ? -36.432 31.244 84.567 1.00 129.96 ? 876 VAL A CG1 1 ATOM 6557 C CG2 . VAL A 1 876 ? -33.958 31.171 84.194 1.00 117.88 ? 876 VAL A CG2 1 ATOM 6558 N N . ALA A 1 877 ? -32.981 34.575 84.909 1.00 106.67 ? 877 ALA A N 1 ATOM 6559 C CA . ALA A 1 877 ? -31.710 35.107 85.387 1.00 95.64 ? 877 ALA A CA 1 ATOM 6560 C C . ALA A 1 877 ? -31.604 36.604 85.112 1.00 92.99 ? 877 ALA A C 1 ATOM 6561 O O . ALA A 1 877 ? -32.521 37.206 84.555 1.00 98.44 ? 877 ALA A O 1 ATOM 6562 C CB . ALA A 1 877 ? -30.550 34.366 84.744 1.00 93.57 ? 877 ALA A CB 1 ATOM 6563 N N . GLN A 1 878 ? -30.484 37.201 85.507 1.00 92.23 ? 878 GLN A N 1 ATOM 6564 C CA . GLN A 1 878 ? -30.250 38.619 85.261 1.00 96.83 ? 878 GLN A CA 1 ATOM 6565 C C . GLN A 1 878 ? -29.863 38.838 83.803 1.00 87.58 ? 878 GLN A C 1 ATOM 6566 O O . GLN A 1 878 ? -28.933 38.208 83.298 1.00 82.74 ? 878 GLN A O 1 ATOM 6567 C CB . GLN A 1 878 ? -29.165 39.162 86.192 1.00 111.50 ? 878 GLN A CB 1 ATOM 6568 C CG . GLN A 1 878 ? -28.983 40.669 86.114 1.00 126.15 ? 878 GLN A CG 1 ATOM 6569 C CD . GLN A 1 878 ? -27.960 41.185 87.106 1.00 136.42 ? 878 GLN A CD 1 ATOM 6570 O OE1 . GLN A 1 878 ? -27.128 40.430 87.607 1.00 127.86 ? 878 GLN A OE1 1 ATOM 6571 N NE2 . GLN A 1 878 ? -28.022 42.479 87.399 1.00 149.20 ? 878 GLN A NE2 1 ATOM 6572 N N . CYS A 1 879 ? -30.576 39.734 83.130 1.00 89.53 ? 879 CYS A N 1 ATOM 6573 C CA . CYS A 1 879 ? -30.420 39.899 81.689 1.00 87.64 ? 879 CYS A CA 1 ATOM 6574 C C . CYS A 1 879 ? -29.565 41.100 81.297 1.00 82.91 ? 879 CYS A C 1 ATOM 6575 O O . CYS A 1 879 ? -29.855 42.236 81.674 1.00 74.32 ? 879 CYS A O 1 ATOM 6576 C CB . CYS A 1 879 ? -31.794 40.019 81.026 1.00 89.54 ? 879 CYS A CB 1 ATOM 6577 S SG . CYS A 1 879 ? -31.737 40.289 79.239 1.00 183.73 ? 879 CYS A SG 1 ATOM 6578 N N . LEU A 1 880 ? -28.507 40.834 80.537 1.00 88.16 ? 880 LEU A N 1 ATOM 6579 C CA . LEU A 1 880 ? -27.742 41.888 79.883 1.00 78.93 ? 880 LEU A CA 1 ATOM 6580 C C . LEU A 1 880 ? -28.246 42.014 78.452 1.00 76.40 ? 880 LEU A C 1 ATOM 6581 O O . LEU A 1 880 ? -28.060 41.112 77.637 1.00 76.12 ? 880 LEU A O 1 ATOM 6582 C CB . LEU A 1 880 ? -26.240 41.583 79.913 1.00 76.16 ? 880 LEU A CB 1 ATOM 6583 C CG . LEU A 1 880 ? -25.257 42.620 79.360 1.00 79.37 ? 880 LEU A CG 1 ATOM 6584 C CD1 . LEU A 1 880 ? -23.947 42.555 80.126 1.00 100.28 ? 880 LEU A CD1 1 ATOM 6585 C CD2 . LEU A 1 880 ? -25.001 42.407 77.874 1.00 70.04 ? 880 LEU A CD2 1 ATOM 6586 N N . LYS A 1 881 ? -28.884 43.138 78.149 1.00 75.28 ? 881 LYS A N 1 ATOM 6587 C CA . LYS A 1 881 ? -29.543 43.310 76.863 1.00 64.55 ? 881 LYS A CA 1 ATOM 6588 C C . LYS A 1 881 ? -28.685 44.090 75.876 1.00 61.77 ? 881 LYS A C 1 ATOM 6589 O O . LYS A 1 881 ? -28.061 45.088 76.233 1.00 82.63 ? 881 LYS A O 1 ATOM 6590 C CB . LYS A 1 881 ? -30.884 44.016 77.057 1.00 78.13 ? 881 LYS A CB 1 ATOM 6591 C CG . LYS A 1 881 ? -31.795 43.995 75.844 1.00 91.72 ? 881 LYS A CG 1 ATOM 6592 C CD . LYS A 1 881 ? -33.056 44.814 76.090 1.00 94.62 ? 881 LYS A CD 1 ATOM 6593 C CE . LYS A 1 881 ? -33.780 44.375 77.357 1.00 81.05 ? 881 LYS A CE 1 ATOM 6594 N NZ . LYS A 1 881 ? -33.385 45.142 78.575 1.00 85.35 ? 881 LYS A NZ 1 ATOM 6595 N N . ILE A 1 882 ? -28.652 43.625 74.632 1.00 59.12 ? 882 ILE A N 1 ATOM 6596 C CA . ILE A 1 882 ? -27.962 44.344 73.570 1.00 58.36 ? 882 ILE A CA 1 ATOM 6597 C C . ILE A 1 882 ? -28.939 44.710 72.459 1.00 60.02 ? 882 ILE A C 1 ATOM 6598 O O . ILE A 1 882 ? -29.482 43.838 71.782 1.00 55.71 ? 882 ILE A O 1 ATOM 6599 C CB . ILE A 1 882 ? -26.800 43.525 72.984 1.00 56.49 ? 882 ILE A CB 1 ATOM 6600 C CG1 . ILE A 1 882 ? -25.765 43.221 74.069 1.00 57.60 ? 882 ILE A CG1 1 ATOM 6601 C CG2 . ILE A 1 882 ? -26.155 44.272 71.828 1.00 65.84 ? 882 ILE A CG2 1 ATOM 6602 C CD1 . ILE A 1 882 ? -24.510 42.556 73.550 1.00 56.50 ? 882 ILE A CD1 1 ATOM 6603 N N . VAL A 1 883 ? -29.166 46.008 72.289 1.00 59.29 ? 883 VAL A N 1 ATOM 6604 C CA . VAL A 1 883 ? -30.082 46.505 71.270 1.00 66.98 ? 883 VAL A CA 1 ATOM 6605 C C . VAL A 1 883 ? -29.306 47.064 70.085 1.00 75.81 ? 883 VAL A C 1 ATOM 6606 O O . VAL A 1 883 ? -28.436 47.918 70.252 1.00 90.06 ? 883 VAL A O 1 ATOM 6607 C CB . VAL A 1 883 ? -31.016 47.592 71.834 1.00 72.79 ? 883 VAL A CB 1 ATOM 6608 C CG1 . VAL A 1 883 ? -31.783 48.272 70.714 1.00 70.12 ? 883 VAL A CG1 1 ATOM 6609 C CG2 . VAL A 1 883 ? -31.969 46.994 72.858 1.00 87.37 ? 883 VAL A CG2 1 ATOM 6610 N N . CYS A 1 884 ? -29.622 46.581 68.888 1.00 56.39 ? 884 CYS A N 1 ATOM 6611 C CA . CYS A 1 884 ? -28.888 46.987 67.698 1.00 58.32 ? 884 CYS A CA 1 ATOM 6612 C C . CYS A 1 884 ? -29.773 47.650 66.650 1.00 66.17 ? 884 CYS A C 1 ATOM 6613 O O . CYS A 1 884 ? -30.907 47.232 66.419 1.00 65.36 ? 884 CYS A O 1 ATOM 6614 C CB . CYS A 1 884 ? -28.177 45.782 67.083 1.00 53.92 ? 884 CYS A CB 1 ATOM 6615 S SG . CYS A 1 884 ? -26.834 45.129 68.095 1.00 58.54 ? 884 CYS A SG 1 ATOM 6616 N N . GLN A 1 885 ? -29.237 48.692 66.021 1.00 74.97 ? 885 GLN A N 1 ATOM 6617 C CA . GLN A 1 885 ? -29.916 49.365 64.923 1.00 58.39 ? 885 GLN A CA 1 ATOM 6618 C C . GLN A 1 885 ? -29.412 48.822 63.590 1.00 58.08 ? 885 GLN A C 1 ATOM 6619 O O . GLN A 1 885 ? -28.222 48.907 63.286 1.00 70.82 ? 885 GLN A O 1 ATOM 6620 C CB . GLN A 1 885 ? -29.704 50.880 64.991 1.00 61.75 ? 885 GLN A CB 1 ATOM 6621 C CG . GLN A 1 885 ? -30.253 51.546 66.247 1.00 70.66 ? 885 GLN A CG 1 ATOM 6622 C CD . GLN A 1 885 ? -29.271 51.528 67.406 1.00 90.75 ? 885 GLN A CD 1 ATOM 6623 O OE1 . GLN A 1 885 ? -28.152 51.030 67.282 1.00 94.65 ? 885 GLN A OE1 1 ATOM 6624 N NE2 . GLN A 1 885 ? -29.687 52.078 68.541 1.00 100.54 ? 885 GLN A NE2 1 ATOM 6625 N N . VAL A 1 886 ? -30.320 48.255 62.804 1.00 55.70 ? 886 VAL A N 1 ATOM 6626 C CA . VAL A 1 886 ? -29.969 47.700 61.502 1.00 57.74 ? 886 VAL A CA 1 ATOM 6627 C C . VAL A 1 886 ? -30.608 48.522 60.390 1.00 71.26 ? 886 VAL A C 1 ATOM 6628 O O . VAL A 1 886 ? -31.701 49.063 60.562 1.00 87.21 ? 886 VAL A O 1 ATOM 6629 C CB . VAL A 1 886 ? -30.419 46.230 61.375 1.00 53.78 ? 886 VAL A CB 1 ATOM 6630 C CG1 . VAL A 1 886 ? -29.768 45.571 60.168 1.00 53.49 ? 886 VAL A CG1 1 ATOM 6631 C CG2 . VAL A 1 886 ? -30.082 45.466 62.641 1.00 82.58 ? 886 VAL A CG2 1 ATOM 6632 N N . GLY A 1 887 ? -29.928 48.622 59.253 1.00 66.23 ? 887 GLY A N 1 ATOM 6633 C CA . GLY A 1 887 ? -30.489 49.329 58.120 1.00 71.95 ? 887 GLY A CA 1 ATOM 6634 C C . GLY A 1 887 ? -29.972 48.882 56.767 1.00 90.32 ? 887 GLY A C 1 ATOM 6635 O O . GLY A 1 887 ? -28.857 48.376 56.650 1.00 112.65 ? 887 GLY A O 1 ATOM 6636 N N . ARG A 1 888 ? -30.800 49.096 55.747 1.00 87.52 ? 888 ARG A N 1 ATOM 6637 C CA . ARG A 1 888 ? -30.478 48.789 54.353 1.00 79.62 ? 888 ARG A CA 1 ATOM 6638 C C . ARG A 1 888 ? -29.831 47.417 54.146 1.00 73.91 ? 888 ARG A C 1 ATOM 6639 O O . ARG A 1 888 ? -28.644 47.320 53.834 1.00 84.28 ? 888 ARG A O 1 ATOM 6640 C CB . ARG A 1 888 ? -29.569 49.878 53.774 1.00 88.48 ? 888 ARG A CB 1 ATOM 6641 C CG . ARG A 1 888 ? -29.499 49.879 52.251 1.00 97.03 ? 888 ARG A CG 1 ATOM 6642 C CD . ARG A 1 888 ? -30.877 50.060 51.631 1.00 96.89 ? 888 ARG A CD 1 ATOM 6643 N NE . ARG A 1 888 ? -30.851 49.891 50.181 1.00 98.97 ? 888 ARG A NE 1 ATOM 6644 C CZ . ARG A 1 888 ? -31.903 50.063 49.388 1.00 90.99 ? 888 ARG A CZ 1 ATOM 6645 N NH1 . ARG A 1 888 ? -33.074 50.415 49.901 1.00 84.85 ? 888 ARG A NH1 1 ATOM 6646 N NH2 . ARG A 1 888 ? -31.786 49.886 48.079 1.00 90.83 ? 888 ARG A NH2 1 ATOM 6647 N N . LEU A 1 889 ? -30.611 46.359 54.339 1.00 65.88 ? 889 LEU A N 1 ATOM 6648 C CA . LEU A 1 889 ? -30.174 45.024 53.952 1.00 62.75 ? 889 LEU A CA 1 ATOM 6649 C C . LEU A 1 889 ? -30.907 44.599 52.688 1.00 65.37 ? 889 LEU A C 1 ATOM 6650 O O . LEU A 1 889 ? -32.109 44.338 52.714 1.00 73.01 ? 889 LEU A O 1 ATOM 6651 C CB . LEU A 1 889 ? -30.416 44.010 55.070 1.00 58.83 ? 889 LEU A CB 1 ATOM 6652 C CG . LEU A 1 889 ? -29.393 43.965 56.206 1.00 61.38 ? 889 LEU A CG 1 ATOM 6653 C CD1 . LEU A 1 889 ? -29.678 42.795 57.137 1.00 57.58 ? 889 LEU A CD1 1 ATOM 6654 C CD2 . LEU A 1 889 ? -27.982 43.878 55.649 1.00 71.69 ? 889 LEU A CD2 1 ATOM 6655 N N . ASP A 1 890 ? -30.174 44.527 51.583 1.00 66.49 ? 890 ASP A N 1 ATOM 6656 C CA . ASP A 1 890 ? -30.772 44.202 50.296 1.00 69.02 ? 890 ASP A CA 1 ATOM 6657 C C . ASP A 1 890 ? -30.959 42.700 50.133 1.00 71.35 ? 890 ASP A C 1 ATOM 6658 O O . ASP A 1 890 ? -30.804 41.938 51.088 1.00 69.34 ? 890 ASP A O 1 ATOM 6659 C CB . ASP A 1 890 ? -29.921 44.759 49.154 1.00 72.23 ? 890 ASP A CB 1 ATOM 6660 C CG . ASP A 1 890 ? -30.011 46.269 49.045 1.00 73.87 ? 890 ASP A CG 1 ATOM 6661 O OD1 . ASP A 1 890 ? -31.064 46.829 49.417 1.00 69.91 ? 890 ASP A OD1 1 ATOM 6662 O OD2 . ASP A 1 890 ? -29.033 46.896 48.587 1.00 86.02 ? 890 ASP A OD2 1 ATOM 6663 N N . ARG A 1 891 ? -31.309 42.293 48.916 1.00 77.76 ? 891 ARG A N 1 ATOM 6664 C CA . ARG A 1 891 ? -31.574 40.895 48.588 1.00 79.28 ? 891 ARG A CA 1 ATOM 6665 C C . ARG A 1 891 ? -30.477 39.951 49.074 1.00 80.91 ? 891 ARG A C 1 ATOM 6666 O O . ARG A 1 891 ? -30.727 39.074 49.895 1.00 91.84 ? 891 ARG A O 1 ATOM 6667 C CB . ARG A 1 891 ? -31.765 40.738 47.078 1.00 90.99 ? 891 ARG A CB 1 ATOM 6668 C CG . ARG A 1 891 ? -32.020 39.309 46.629 1.00 105.03 ? 891 ARG A CG 1 ATOM 6669 C CD . ARG A 1 891 ? -32.381 39.238 45.151 1.00 123.41 ? 891 ARG A CD 1 ATOM 6670 N NE . ARG A 1 891 ? -31.337 39.791 44.291 1.00 130.93 ? 891 ARG A NE 1 ATOM 6671 C CZ . ARG A 1 891 ? -31.400 40.985 43.709 1.00 127.22 ? 891 ARG A CZ 1 ATOM 6672 N NH1 . ARG A 1 891 ? -32.462 41.758 43.890 1.00 131.55 ? 891 ARG A NH1 1 ATOM 6673 N NH2 . ARG A 1 891 ? -30.402 41.405 42.944 1.00 116.43 ? 891 ARG A NH2 1 ATOM 6674 N N . GLY A 1 892 ? -29.267 40.125 48.557 1.00 76.63 ? 892 GLY A N 1 ATOM 6675 C CA . GLY A 1 892 ? -28.166 39.242 48.900 1.00 88.13 ? 892 GLY A CA 1 ATOM 6676 C C . GLY A 1 892 ? -27.562 39.431 50.282 1.00 87.71 ? 892 GLY A C 1 ATOM 6677 O O . GLY A 1 892 ? -27.327 38.458 50.998 1.00 91.12 ? 892 GLY A O 1 ATOM 6678 N N . LYS A 1 893 ? -27.315 40.681 50.661 1.00 79.18 ? 893 LYS A N 1 ATOM 6679 C CA . LYS A 1 893 ? -26.540 40.985 51.864 1.00 79.45 ? 893 LYS A CA 1 ATOM 6680 C C . LYS A 1 893 ? -27.264 40.640 53.169 1.00 71.55 ? 893 LYS A C 1 ATOM 6681 O O . LYS A 1 893 ? -28.492 40.584 53.221 1.00 68.36 ? 893 LYS A O 1 ATOM 6682 C CB . LYS A 1 893 ? -26.148 42.467 51.867 1.00 100.24 ? 893 LYS A CB 1 ATOM 6683 C CG . LYS A 1 893 ? -25.009 42.813 52.818 1.00 123.15 ? 893 LYS A CG 1 ATOM 6684 C CD . LYS A 1 893 ? -24.585 44.266 52.689 1.00 135.37 ? 893 LYS A CD 1 ATOM 6685 C CE . LYS A 1 893 ? -23.511 44.616 53.708 1.00 136.59 ? 893 LYS A CE 1 ATOM 6686 N NZ . LYS A 1 893 ? -22.309 43.744 53.582 1.00 133.90 ? 893 LYS A NZ 1 ATOM 6687 N N . SER A 1 894 ? -26.477 40.402 54.216 1.00 74.64 ? 894 SER A N 1 ATOM 6688 C CA . SER A 1 894 ? -26.990 40.131 55.555 1.00 71.18 ? 894 SER A CA 1 ATOM 6689 C C . SER A 1 894 ? -26.132 40.833 56.609 1.00 72.33 ? 894 SER A C 1 ATOM 6690 O O . SER A 1 894 ? -25.051 41.335 56.302 1.00 85.92 ? 894 SER A O 1 ATOM 6691 C CB . SER A 1 894 ? -27.031 38.627 55.824 1.00 77.54 ? 894 SER A CB 1 ATOM 6692 O OG . SER A 1 894 ? -25.741 38.051 55.721 1.00 91.51 ? 894 SER A OG 1 ATOM 6693 N N . ALA A 1 895 ? -26.617 40.869 57.847 1.00 59.91 ? 895 ALA A N 1 ATOM 6694 C CA . ALA A 1 895 ? -25.888 41.516 58.936 1.00 60.49 ? 895 ALA A CA 1 ATOM 6695 C C . ALA A 1 895 ? -25.568 40.533 60.062 1.00 67.62 ? 895 ALA A C 1 ATOM 6696 O O . ALA A 1 895 ? -26.413 39.728 60.453 1.00 79.94 ? 895 ALA A O 1 ATOM 6697 C CB . ALA A 1 895 ? -26.681 42.692 59.470 1.00 60.22 ? 895 ALA A CB 1 ATOM 6698 N N . ILE A 1 896 ? -24.346 40.609 60.585 1.00 67.41 ? 896 ILE A N 1 ATOM 6699 C CA . ILE A 1 896 ? -23.870 39.648 61.578 1.00 62.17 ? 896 ILE A CA 1 ATOM 6700 C C . ILE A 1 896 ? -23.472 40.316 62.895 1.00 67.95 ? 896 ILE A C 1 ATOM 6701 O O . ILE A 1 896 ? -23.021 41.461 62.910 1.00 77.10 ? 896 ILE A O 1 ATOM 6702 C CB . ILE A 1 896 ? -22.652 38.852 61.050 1.00 57.02 ? 896 ILE A CB 1 ATOM 6703 C CG1 . ILE A 1 896 ? -22.812 38.534 59.562 1.00 57.67 ? 896 ILE A CG1 1 ATOM 6704 C CG2 . ILE A 1 896 ? -22.451 37.573 61.850 1.00 60.29 ? 896 ILE A CG2 1 ATOM 6705 C CD1 . ILE A 1 896 ? -23.898 37.529 59.267 1.00 65.84 ? 896 ILE A CD1 1 ATOM 6706 N N . LEU A 1 897 ? -23.641 39.589 63.997 1.00 63.27 ? 897 LEU A N 1 ATOM 6707 C CA . LEU A 1 897 ? -23.157 40.030 65.301 1.00 58.94 ? 897 LEU A CA 1 ATOM 6708 C C . LEU A 1 897 ? -22.364 38.921 65.986 1.00 74.00 ? 897 LEU A C 1 ATOM 6709 O O . LEU A 1 897 ? -22.907 37.864 66.305 1.00 86.18 ? 897 LEU A O 1 ATOM 6710 C CB . LEU A 1 897 ? -24.320 40.469 66.194 1.00 56.62 ? 897 LEU A CB 1 ATOM 6711 C CG . LEU A 1 897 ? -23.971 40.739 67.661 1.00 50.97 ? 897 LEU A CG 1 ATOM 6712 C CD1 . LEU A 1 897 ? -22.924 41.837 67.779 1.00 54.65 ? 897 LEU A CD1 1 ATOM 6713 C CD2 . LEU A 1 897 ? -25.216 41.095 68.460 1.00 50.78 ? 897 LEU A CD2 1 ATOM 6714 N N . TYR A 1 898 ? -21.077 39.171 66.211 1.00 69.66 ? 898 TYR A N 1 ATOM 6715 C CA . TYR A 1 898 ? -20.215 38.202 66.878 1.00 60.14 ? 898 TYR A CA 1 ATOM 6716 C C . TYR A 1 898 ? -20.046 38.560 68.349 1.00 60.52 ? 898 TYR A C 1 ATOM 6717 O O . TYR A 1 898 ? -19.568 39.644 68.676 1.00 64.11 ? 898 TYR A O 1 ATOM 6718 C CB . TYR A 1 898 ? -18.845 38.134 66.199 1.00 63.90 ? 898 TYR A CB 1 ATOM 6719 C CG . TYR A 1 898 ? -18.898 37.935 64.701 1.00 64.00 ? 898 TYR A CG 1 ATOM 6720 C CD1 . TYR A 1 898 ? -18.771 39.011 63.833 1.00 73.64 ? 898 TYR A CD1 1 ATOM 6721 C CD2 . TYR A 1 898 ? -19.067 36.670 64.154 1.00 61.66 ? 898 TYR A CD2 1 ATOM 6722 C CE1 . TYR A 1 898 ? -18.816 38.833 62.463 1.00 79.15 ? 898 TYR A CE1 1 ATOM 6723 C CE2 . TYR A 1 898 ? -19.114 36.482 62.786 1.00 61.93 ? 898 TYR A CE2 1 ATOM 6724 C CZ . TYR A 1 898 ? -18.987 37.567 61.946 1.00 71.38 ? 898 TYR A CZ 1 ATOM 6725 O OH . TYR A 1 898 ? -19.032 37.384 60.583 1.00 83.97 ? 898 TYR A OH 1 ATOM 6726 N N . VAL A 1 899 ? -20.439 37.650 69.234 1.00 57.86 ? 899 VAL A N 1 ATOM 6727 C CA . VAL A 1 899 ? -20.300 37.880 70.668 1.00 56.63 ? 899 VAL A CA 1 ATOM 6728 C C . VAL A 1 899 ? -19.287 36.920 71.281 1.00 63.85 ? 899 VAL A C 1 ATOM 6729 O O . VAL A 1 899 ? -19.538 35.720 71.383 1.00 68.50 ? 899 VAL A O 1 ATOM 6730 C CB . VAL A 1 899 ? -21.647 37.726 71.399 1.00 54.05 ? 899 VAL A CB 1 ATOM 6731 C CG1 . VAL A 1 899 ? -21.465 37.929 72.896 1.00 58.72 ? 899 VAL A CG1 1 ATOM 6732 C CG2 . VAL A 1 899 ? -22.666 38.706 70.843 1.00 52.58 ? 899 VAL A CG2 1 ATOM 6733 N N . LYS A 1 900 ? -18.142 37.457 71.692 1.00 66.87 ? 900 LYS A N 1 ATOM 6734 C CA . LYS A 1 900 ? -17.105 36.653 72.327 1.00 67.90 ? 900 LYS A CA 1 ATOM 6735 C C . LYS A 1 900 ? -17.184 36.781 73.842 1.00 69.00 ? 900 LYS A C 1 ATOM 6736 O O . LYS A 1 900 ? -17.060 37.877 74.388 1.00 71.09 ? 900 LYS A O 1 ATOM 6737 C CB . LYS A 1 900 ? -15.718 37.067 71.834 1.00 71.99 ? 900 LYS A CB 1 ATOM 6738 C CG . LYS A 1 900 ? -14.577 36.321 72.508 1.00 75.77 ? 900 LYS A CG 1 ATOM 6739 C CD . LYS A 1 900 ? -13.229 36.764 71.965 1.00 80.32 ? 900 LYS A CD 1 ATOM 6740 C CE . LYS A 1 900 ? -12.091 36.016 72.641 1.00 82.84 ? 900 LYS A CE 1 ATOM 6741 N NZ . LYS A 1 900 ? -10.766 36.416 72.093 1.00 92.81 ? 900 LYS A NZ 1 ATOM 6742 N N . SER A 1 901 ? -17.391 35.656 74.518 1.00 67.37 ? 901 SER A N 1 ATOM 6743 C CA . SER A 1 901 ? -17.537 35.667 75.966 1.00 69.49 ? 901 SER A CA 1 ATOM 6744 C C . SER A 1 901 ? -16.690 34.592 76.631 1.00 72.07 ? 901 SER A C 1 ATOM 6745 O O . SER A 1 901 ? -16.295 33.613 75.999 1.00 73.77 ? 901 SER A O 1 ATOM 6746 C CB . SER A 1 901 ? -19.004 35.477 76.356 1.00 66.23 ? 901 SER A CB 1 ATOM 6747 O OG . SER A 1 901 ? -19.434 34.155 76.085 1.00 62.75 ? 901 SER A OG 1 ATOM 6748 N N . LEU A 1 902 ? -16.414 34.788 77.915 1.00 74.62 ? 902 LEU A N 1 ATOM 6749 C CA . LEU A 1 902 ? -15.728 33.785 78.713 1.00 76.51 ? 902 LEU A CA 1 ATOM 6750 C C . LEU A 1 902 ? -16.696 33.155 79.699 1.00 85.86 ? 902 LEU A C 1 ATOM 6751 O O . LEU A 1 902 ? -17.437 33.858 80.386 1.00 97.26 ? 902 LEU A O 1 ATOM 6752 C CB . LEU A 1 902 ? -14.546 34.397 79.465 1.00 80.29 ? 902 LEU A CB 1 ATOM 6753 C CG . LEU A 1 902 ? -13.365 34.903 78.640 1.00 87.97 ? 902 LEU A CG 1 ATOM 6754 C CD1 . LEU A 1 902 ? -12.358 35.583 79.550 1.00 95.74 ? 902 LEU A CD1 1 ATOM 6755 C CD2 . LEU A 1 902 ? -12.718 33.770 77.869 1.00 99.86 ? 902 LEU A CD2 1 ATOM 6756 N N . LEU A 1 903 ? -16.698 31.829 79.762 1.00 83.26 ? 903 LEU A N 1 ATOM 6757 C CA . LEU A 1 903 ? -17.457 31.136 80.789 1.00 79.23 ? 903 LEU A CA 1 ATOM 6758 C C . LEU A 1 903 ? -16.821 31.448 82.134 1.00 84.29 ? 903 LEU A C 1 ATOM 6759 O O . LEU A 1 903 ? -15.599 31.400 82.272 1.00 101.99 ? 903 LEU A O 1 ATOM 6760 C CB . LEU A 1 903 ? -17.487 29.626 80.533 1.00 78.10 ? 903 LEU A CB 1 ATOM 6761 C CG . LEU A 1 903 ? -18.239 28.753 81.543 1.00 79.35 ? 903 LEU A CG 1 ATOM 6762 C CD1 . LEU A 1 903 ? -18.978 27.634 80.829 1.00 80.75 ? 903 LEU A CD1 1 ATOM 6763 C CD2 . LEU A 1 903 ? -17.292 28.174 82.587 1.00 85.26 ? 903 LEU A CD2 1 ATOM 6764 N N . TRP A 1 904 ? -17.643 31.765 83.126 1.00 84.00 ? 904 TRP A N 1 ATOM 6765 C CA . TRP A 1 904 ? -17.110 32.086 84.439 1.00 86.85 ? 904 TRP A CA 1 ATOM 6766 C C . TRP A 1 904 ? -17.056 30.806 85.257 1.00 92.49 ? 904 TRP A C 1 ATOM 6767 O O . TRP A 1 904 ? -18.085 30.284 85.679 1.00 104.46 ? 904 TRP A O 1 ATOM 6768 C CB . TRP A 1 904 ? -17.973 33.143 85.130 1.00 86.44 ? 904 TRP A CB 1 ATOM 6769 C CG . TRP A 1 904 ? -17.268 33.884 86.222 1.00 89.05 ? 904 TRP A CG 1 ATOM 6770 C CD1 . TRP A 1 904 ? -17.128 33.493 87.521 1.00 98.70 ? 904 TRP A CD1 1 ATOM 6771 C CD2 . TRP A 1 904 ? -16.613 35.153 86.111 1.00 90.04 ? 904 TRP A CD2 1 ATOM 6772 N NE1 . TRP A 1 904 ? -16.423 34.438 88.226 1.00 104.90 ? 904 TRP A NE1 1 ATOM 6773 C CE2 . TRP A 1 904 ? -16.094 35.467 87.383 1.00 97.29 ? 904 TRP A CE2 1 ATOM 6774 C CE3 . TRP A 1 904 ? -16.412 36.052 85.060 1.00 88.65 ? 904 TRP A CE3 1 ATOM 6775 C CZ2 . TRP A 1 904 ? -15.388 36.642 87.632 1.00 95.50 ? 904 TRP A CZ2 1 ATOM 6776 C CZ3 . TRP A 1 904 ? -15.711 37.218 85.308 1.00 90.80 ? 904 TRP A CZ3 1 ATOM 6777 C CH2 . TRP A 1 904 ? -15.207 37.503 86.584 1.00 93.67 ? 904 TRP A CH2 1 ATOM 6778 N N . THR A 1 905 ? -15.844 30.316 85.492 1.00 92.62 ? 905 THR A N 1 ATOM 6779 C CA . THR A 1 905 ? -15.651 29.023 86.135 1.00 94.62 ? 905 THR A CA 1 ATOM 6780 C C . THR A 1 905 ? -15.825 29.137 87.642 1.00 97.50 ? 905 THR A C 1 ATOM 6781 O O . THR A 1 905 ? -16.292 28.206 88.299 1.00 98.24 ? 905 THR A O 1 ATOM 6782 C CB . THR A 1 905 ? -14.258 28.444 85.821 1.00 95.45 ? 905 THR A CB 1 ATOM 6783 O OG1 . THR A 1 905 ? -13.962 28.629 84.431 1.00 92.20 ? 905 THR A OG1 1 ATOM 6784 C CG2 . THR A 1 905 ? -14.204 26.962 86.158 1.00 103.02 ? 905 THR A CG2 1 ATOM 6785 N N . GLU A 1 906 ? -15.451 30.295 88.178 1.00 101.02 ? 906 GLU A N 1 ATOM 6786 C CA . GLU A 1 906 ? -15.523 30.560 89.610 1.00 111.52 ? 906 GLU A CA 1 ATOM 6787 C C . GLU A 1 906 ? -16.951 30.440 90.142 1.00 115.23 ? 906 GLU A C 1 ATOM 6788 O O . GLU A 1 906 ? -17.163 30.138 91.317 1.00 131.08 ? 906 GLU A O 1 ATOM 6789 C CB . GLU A 1 906 ? -14.960 31.952 89.907 1.00 120.96 ? 906 GLU A CB 1 ATOM 6790 C CG . GLU A 1 906 ? -14.843 32.291 91.382 1.00 134.12 ? 906 GLU A CG 1 ATOM 6791 C CD . GLU A 1 906 ? -14.236 33.660 91.613 1.00 145.69 ? 906 GLU A CD 1 ATOM 6792 O OE1 . GLU A 1 906 ? -14.257 34.133 92.769 1.00 151.00 ? 906 GLU A OE1 1 ATOM 6793 O OE2 . GLU A 1 906 ? -13.735 34.263 90.640 1.00 149.58 ? 906 GLU A OE2 1 ATOM 6794 N N . THR A 1 907 ? -17.926 30.668 89.268 1.00 105.91 ? 907 THR A N 1 ATOM 6795 C CA . THR A 1 907 ? -19.333 30.587 89.642 1.00 105.92 ? 907 THR A CA 1 ATOM 6796 C C . THR A 1 907 ? -19.781 29.144 89.860 1.00 106.81 ? 907 THR A C 1 ATOM 6797 O O . THR A 1 907 ? -20.505 28.846 90.812 1.00 125.25 ? 907 THR A O 1 ATOM 6798 C CB . THR A 1 907 ? -20.231 31.237 88.573 1.00 109.87 ? 907 THR A CB 1 ATOM 6799 O OG1 . THR A 1 907 ? -19.939 32.638 88.490 1.00 115.99 ? 907 THR A OG1 1 ATOM 6800 C CG2 . THR A 1 907 ? -21.701 31.055 88.917 1.00 111.58 ? 907 THR A CG2 1 ATOM 6801 N N . PHE A 1 908 ? -19.340 28.247 88.985 1.00 103.19 ? 908 PHE A N 1 ATOM 6802 C CA . PHE A 1 908 ? -19.736 26.846 89.069 1.00 107.26 ? 908 PHE A CA 1 ATOM 6803 C C . PHE A 1 908 ? -19.026 26.143 90.226 1.00 129.91 ? 908 PHE A C 1 ATOM 6804 O O . PHE A 1 908 ? -18.284 26.777 90.978 1.00 148.81 ? 908 PHE A O 1 ATOM 6805 C CB . PHE A 1 908 ? -19.464 26.138 87.741 1.00 101.07 ? 908 PHE A CB 1 ATOM 6806 C CG . PHE A 1 908 ? -20.209 26.737 86.580 1.00 115.52 ? 908 PHE A CG 1 ATOM 6807 C CD1 . PHE A 1 908 ? -21.526 26.386 86.327 1.00 118.09 ? 908 PHE A CD1 1 ATOM 6808 C CD2 . PHE A 1 908 ? -19.599 27.663 85.751 1.00 111.33 ? 908 PHE A CD2 1 ATOM 6809 C CE1 . PHE A 1 908 ? -22.216 26.943 85.264 1.00 96.71 ? 908 PHE A CE1 1 ATOM 6810 C CE2 . PHE A 1 908 ? -20.284 28.224 84.687 1.00 93.11 ? 908 PHE A CE2 1 ATOM 6811 C CZ . PHE A 1 908 ? -21.594 27.863 84.444 1.00 92.34 ? 908 PHE A CZ 1 ATOM 6812 N N . MET A 1 909 ? -19.260 24.837 90.357 1.00 126.37 ? 909 MET A N 1 ATOM 6813 C CA . MET A 1 909 ? -18.886 24.075 91.551 1.00 128.00 ? 909 MET A CA 1 ATOM 6814 C C . MET A 1 909 ? -19.579 24.671 92.777 1.00 133.55 ? 909 MET A C 1 ATOM 6815 O O . MET A 1 909 ? -20.783 24.904 92.751 1.00 126.99 ? 909 MET A O 1 ATOM 6816 C CB . MET A 1 909 ? -17.366 24.043 91.757 1.00 129.06 ? 909 MET A CB 1 ATOM 6817 C CG . MET A 1 909 ? -16.583 23.353 90.648 1.00 136.90 ? 909 MET A CG 1 ATOM 6818 S SD . MET A 1 909 ? -16.300 24.405 89.212 1.00 109.61 ? 909 MET A SD 1 ATOM 6819 C CE . MET A 1 909 ? -15.223 23.360 88.234 1.00 87.68 ? 909 MET A CE 1 ATOM 6820 N N . ASN A 1 910 ? -18.819 24.894 93.846 1.00 149.93 ? 910 ASN A N 1 ATOM 6821 C CA . ASN A 1 910 ? -19.298 25.606 95.035 1.00 152.10 ? 910 ASN A CA 1 ATOM 6822 C C . ASN A 1 910 ? -20.640 25.123 95.594 1.00 144.71 ? 910 ASN A C 1 ATOM 6823 O O . ASN A 1 910 ? -20.891 23.923 95.706 1.00 140.07 ? 910 ASN A O 1 ATOM 6824 C CB . ASN A 1 910 ? -19.408 27.103 94.731 1.00 141.07 ? 910 ASN A CB 1 ATOM 6825 C CG . ASN A 1 910 ? -18.223 27.630 93.948 1.00 132.59 ? 910 ASN A CG 1 ATOM 6826 O OD1 . ASN A 1 910 ? -17.159 27.014 93.920 1.00 138.80 ? 910 ASN A OD1 1 ATOM 6827 N ND2 . ASN A 1 910 ? -18.403 28.779 93.307 1.00 122.42 ? 910 ASN A ND2 1 ATOM 6828 N N . LYS A 1 911 ? -21.492 26.085 95.940 1.00 140.12 ? 911 LYS A N 1 ATOM 6829 C CA . LYS A 1 911 ? -22.857 25.822 96.389 1.00 149.31 ? 911 LYS A CA 1 ATOM 6830 C C . LYS A 1 911 ? -23.807 25.897 95.201 1.00 148.12 ? 911 LYS A C 1 ATOM 6831 O O . LYS A 1 911 ? -25.028 25.826 95.348 1.00 148.35 ? 911 LYS A O 1 ATOM 6832 C CB . LYS A 1 911 ? -23.276 26.810 97.478 1.00 157.11 ? 911 LYS A CB 1 ATOM 6833 C CG . LYS A 1 911 ? -22.493 26.669 98.773 1.00 158.92 ? 911 LYS A CG 1 ATOM 6834 C CD . LYS A 1 911 ? -23.044 27.580 99.858 1.00 159.27 ? 911 LYS A CD 1 ATOM 6835 C CE . LYS A 1 911 ? -22.316 27.366 101.176 1.00 159.33 ? 911 LYS A CE 1 ATOM 6836 N NZ . LYS A 1 911 ? -22.874 28.213 102.266 1.00 157.46 ? 911 LYS A NZ 1 ATOM 6837 N N . GLU A 1 912 ? -23.217 26.043 94.020 1.00 150.44 ? 912 GLU A N 1 ATOM 6838 C CA . GLU A 1 912 ? -23.934 26.131 92.752 1.00 157.45 ? 912 GLU A CA 1 ATOM 6839 C C . GLU A 1 912 ? -24.552 24.785 92.364 1.00 161.97 ? 912 GLU A C 1 ATOM 6840 O O . GLU A 1 912 ? -25.137 24.660 91.286 1.00 154.52 ? 912 GLU A O 1 ATOM 6841 C CB . GLU A 1 912 ? -23.003 26.640 91.644 1.00 148.58 ? 912 GLU A CB 1 ATOM 6842 C CG . GLU A 1 912 ? -23.710 27.200 90.417 1.00 136.93 ? 912 GLU A CG 1 ATOM 6843 C CD . GLU A 1 912 ? -24.678 28.315 90.759 1.00 141.19 ? 912 GLU A CD 1 ATOM 6844 O OE1 . GLU A 1 912 ? -25.775 28.352 90.163 1.00 138.76 ? 912 GLU A OE1 1 ATOM 6845 O OE2 . GLU A 1 912 ? -24.342 29.156 91.619 1.00 150.30 ? 912 GLU A OE2 1 ATOM 6846 N N . ASN A 1 913 ? -24.399 23.785 93.235 1.00 172.38 ? 913 ASN A N 1 ATOM 6847 C CA . ASN A 1 913 ? -24.727 22.395 92.916 1.00 178.39 ? 913 ASN A CA 1 ATOM 6848 C C . ASN A 1 913 ? -23.813 21.878 91.820 1.00 168.22 ? 913 ASN A C 1 ATOM 6849 O O . ASN A 1 913 ? -24.199 21.800 90.653 1.00 162.05 ? 913 ASN A O 1 ATOM 6850 C CB . ASN A 1 913 ? -26.199 22.232 92.516 1.00 181.77 ? 913 ASN A CB 1 ATOM 6851 C CG . ASN A 1 913 ? -27.146 22.434 93.681 1.00 180.48 ? 913 ASN A CG 1 ATOM 6852 O OD1 . ASN A 1 913 ? -27.958 23.360 93.683 1.00 179.67 ? 913 ASN A OD1 1 ATOM 6853 N ND2 . ASN A 1 913 ? -27.051 21.562 94.678 1.00 177.65 ? 913 ASN A ND2 1 ATOM 6854 N N . GLN A 1 914 ? -22.588 21.554 92.235 1.00 158.91 ? 914 GLN A N 1 ATOM 6855 C CA . GLN A 1 914 ? -21.472 21.201 91.362 1.00 147.10 ? 914 GLN A CA 1 ATOM 6856 C C . GLN A 1 914 ? -21.901 20.307 90.212 1.00 146.66 ? 914 GLN A C 1 ATOM 6857 O O . GLN A 1 914 ? -21.785 20.699 89.052 1.00 144.95 ? 914 GLN A O 1 ATOM 6858 C CB . GLN A 1 914 ? -20.370 20.509 92.168 1.00 146.37 ? 914 GLN A CB 1 ATOM 6859 C CG . GLN A 1 914 ? -19.986 21.236 93.446 1.00 146.81 ? 914 GLN A CG 1 ATOM 6860 C CD . GLN A 1 914 ? -18.855 20.554 94.190 1.00 153.65 ? 914 GLN A CD 1 ATOM 6861 O OE1 . GLN A 1 914 ? -18.502 19.412 93.895 1.00 158.99 ? 914 GLN A OE1 1 ATOM 6862 N NE2 . GLN A 1 914 ? -18.279 21.254 95.159 1.00 154.28 ? 914 GLN A NE2 1 ATOM 6863 N N . ASN A 1 915 ? -22.410 19.117 90.510 1.00 155.66 ? 915 ASN A N 1 ATOM 6864 C CA . ASN A 1 915 ? -22.923 18.303 89.424 1.00 160.25 ? 915 ASN A CA 1 ATOM 6865 C C . ASN A 1 915 ? -24.398 18.603 89.207 1.00 157.49 ? 915 ASN A C 1 ATOM 6866 O O . ASN A 1 915 ? -25.266 18.162 89.961 1.00 166.40 ? 915 ASN A O 1 ATOM 6867 C CB . ASN A 1 915 ? -22.720 16.816 89.723 1.00 169.86 ? 915 ASN A CB 1 ATOM 6868 C CG . ASN A 1 915 ? -23.477 15.918 88.762 1.00 172.48 ? 915 ASN A CG 1 ATOM 6869 O OD1 . ASN A 1 915 ? -23.567 16.200 87.567 1.00 173.48 ? 915 ASN A OD1 1 ATOM 6870 N ND2 . ASN A 1 915 ? -24.033 14.831 89.285 1.00 171.45 ? 915 ASN A ND2 1 ATOM 6871 N N . HIS A 1 916 ? -24.653 19.369 88.153 1.00 144.94 ? 916 HIS A N 1 ATOM 6872 C CA . HIS A 1 916 ? -25.986 19.622 87.631 1.00 135.81 ? 916 HIS A CA 1 ATOM 6873 C C . HIS A 1 916 ? -25.832 20.046 86.178 1.00 127.68 ? 916 HIS A C 1 ATOM 6874 O O . HIS A 1 916 ? -24.830 20.661 85.816 1.00 120.28 ? 916 HIS A O 1 ATOM 6875 C CB . HIS A 1 916 ? -26.718 20.688 88.448 1.00 130.35 ? 916 HIS A CB 1 ATOM 6876 C CG . HIS A 1 916 ? -27.736 20.127 89.393 1.00 139.06 ? 916 HIS A CG 1 ATOM 6877 N ND1 . HIS A 1 916 ? -28.376 20.895 90.341 1.00 141.26 ? 916 HIS A ND1 1 ATOM 6878 C CD2 . HIS A 1 916 ? -28.228 18.873 89.529 1.00 148.55 ? 916 HIS A CD2 1 ATOM 6879 C CE1 . HIS A 1 916 ? -29.216 20.138 91.024 1.00 148.60 ? 916 HIS A CE1 1 ATOM 6880 N NE2 . HIS A 1 916 ? -29.146 18.907 90.551 1.00 151.48 ? 916 HIS A NE2 1 ATOM 6881 N N . SER A 1 917 ? -26.815 19.734 85.344 1.00 131.61 ? 917 SER A N 1 ATOM 6882 C CA . SER A 1 917 ? -26.726 20.106 83.940 1.00 122.99 ? 917 SER A CA 1 ATOM 6883 C C . SER A 1 917 ? -27.326 21.489 83.705 1.00 110.09 ? 917 SER A C 1 ATOM 6884 O O . SER A 1 917 ? -28.520 21.704 83.914 1.00 108.49 ? 917 SER A O 1 ATOM 6885 C CB . SER A 1 917 ? -27.421 19.063 83.065 1.00 131.19 ? 917 SER A CB 1 ATOM 6886 O OG . SER A 1 917 ? -26.805 17.793 83.202 1.00 129.34 ? 917 SER A OG 1 ATOM 6887 N N . TYR A 1 918 ? -26.482 22.423 83.276 1.00 108.63 ? 918 TYR A N 1 ATOM 6888 C CA . TYR A 1 918 ? -26.912 23.788 82.992 1.00 95.74 ? 918 TYR A CA 1 ATOM 6889 C C . TYR A 1 918 ? -26.839 24.092 81.500 1.00 89.62 ? 918 TYR A C 1 ATOM 6890 O O . TYR A 1 918 ? -25.831 23.817 80.851 1.00 89.41 ? 918 TYR A O 1 ATOM 6891 C CB . TYR A 1 918 ? -26.054 24.799 83.760 1.00 90.52 ? 918 TYR A CB 1 ATOM 6892 C CG . TYR A 1 918 ? -26.303 24.846 85.252 1.00 94.74 ? 918 TYR A CG 1 ATOM 6893 C CD1 . TYR A 1 918 ? -27.515 24.435 85.792 1.00 106.67 ? 918 TYR A CD1 1 ATOM 6894 C CD2 . TYR A 1 918 ? -25.324 25.311 86.121 1.00 95.79 ? 918 TYR A CD2 1 ATOM 6895 C CE1 . TYR A 1 918 ? -27.742 24.482 87.158 1.00 117.30 ? 918 TYR A CE1 1 ATOM 6896 C CE2 . TYR A 1 918 ? -25.541 25.362 87.485 1.00 106.93 ? 918 TYR A CE2 1 ATOM 6897 C CZ . TYR A 1 918 ? -26.751 24.947 87.999 1.00 113.32 ? 918 TYR A CZ 1 ATOM 6898 O OH . TYR A 1 918 ? -26.966 24.997 89.358 1.00 109.79 ? 918 TYR A OH 1 ATOM 6899 N N . SER A 1 919 ? -27.912 24.659 80.960 1.00 87.32 ? 919 SER A N 1 ATOM 6900 C CA . SER A 1 919 ? -27.912 25.119 79.578 1.00 82.70 ? 919 SER A CA 1 ATOM 6901 C C . SER A 1 919 ? -28.107 26.628 79.548 1.00 79.45 ? 919 SER A C 1 ATOM 6902 O O . SER A 1 919 ? -29.092 27.144 80.074 1.00 85.57 ? 919 SER A O 1 ATOM 6903 C CB . SER A 1 919 ? -29.005 24.424 78.764 1.00 91.49 ? 919 SER A CB 1 ATOM 6904 O OG . SER A 1 919 ? -30.288 24.927 79.095 1.00 103.26 ? 919 SER A OG 1 ATOM 6905 N N . LEU A 1 920 ? -27.165 27.332 78.931 1.00 74.70 ? 920 LEU A N 1 ATOM 6906 C CA . LEU A 1 920 ? -27.201 28.788 78.907 1.00 73.88 ? 920 LEU A CA 1 ATOM 6907 C C . LEU A 1 920 ? -27.912 29.285 77.655 1.00 84.99 ? 920 LEU A C 1 ATOM 6908 O O . LEU A 1 920 ? -27.410 29.138 76.541 1.00 91.78 ? 920 LEU A O 1 ATOM 6909 C CB . LEU A 1 920 ? -25.782 29.349 78.989 1.00 70.13 ? 920 LEU A CB 1 ATOM 6910 C CG . LEU A 1 920 ? -24.987 28.786 80.171 1.00 70.51 ? 920 LEU A CG 1 ATOM 6911 C CD1 . LEU A 1 920 ? -23.558 29.297 80.175 1.00 68.88 ? 920 LEU A CD1 1 ATOM 6912 C CD2 . LEU A 1 920 ? -25.680 29.115 81.485 1.00 74.05 ? 920 LEU A CD2 1 ATOM 6913 N N . LYS A 1 921 ? -29.081 29.885 77.853 1.00 80.69 ? 921 LYS A N 1 ATOM 6914 C CA . LYS A 1 921 ? -29.961 30.252 76.751 1.00 74.06 ? 921 LYS A CA 1 ATOM 6915 C C . LYS A 1 921 ? -29.970 31.752 76.481 1.00 74.73 ? 921 LYS A C 1 ATOM 6916 O O . LYS A 1 921 ? -30.458 32.538 77.293 1.00 93.23 ? 921 LYS A O 1 ATOM 6917 C CB . LYS A 1 921 ? -31.385 29.766 77.039 1.00 79.55 ? 921 LYS A CB 1 ATOM 6918 C CG . LYS A 1 921 ? -32.457 30.376 76.152 1.00 87.19 ? 921 LYS A CG 1 ATOM 6919 C CD . LYS A 1 921 ? -33.844 29.957 76.610 1.00 95.81 ? 921 LYS A CD 1 ATOM 6920 C CE . LYS A 1 921 ? -34.918 30.851 76.014 1.00 101.19 ? 921 LYS A CE 1 ATOM 6921 N NZ . LYS A 1 921 ? -34.797 32.256 76.497 1.00 99.49 ? 921 LYS A NZ 1 ATOM 6922 N N . SER A 1 922 ? -29.429 32.142 75.331 1.00 67.55 ? 922 SER A N 1 ATOM 6923 C CA . SER A 1 922 ? -29.470 33.533 74.901 1.00 70.61 ? 922 SER A CA 1 ATOM 6924 C C . SER A 1 922 ? -30.502 33.705 73.791 1.00 64.78 ? 922 SER A C 1 ATOM 6925 O O . SER A 1 922 ? -30.552 32.914 72.849 1.00 62.63 ? 922 SER A O 1 ATOM 6926 C CB . SER A 1 922 ? -28.092 33.998 74.428 1.00 77.85 ? 922 SER A CB 1 ATOM 6927 O OG . SER A 1 922 ? -27.631 33.214 73.342 1.00 82.90 ? 922 SER A OG 1 ATOM 6928 N N . SER A 1 923 ? -31.328 34.739 73.911 1.00 63.51 ? 923 SER A N 1 ATOM 6929 C CA . SER A 1 923 ? -32.396 34.983 72.949 1.00 63.97 ? 923 SER A CA 1 ATOM 6930 C C . SER A 1 923 ? -32.067 36.155 72.033 1.00 59.84 ? 923 SER A C 1 ATOM 6931 O O . SER A 1 923 ? -31.439 37.125 72.454 1.00 59.61 ? 923 SER A O 1 ATOM 6932 C CB . SER A 1 923 ? -33.717 35.244 73.675 1.00 78.43 ? 923 SER A CB 1 ATOM 6933 O OG . SER A 1 923 ? -34.746 35.583 72.762 1.00 91.25 ? 923 SER A OG 1 ATOM 6934 N N . ALA A 1 924 ? -32.494 36.060 70.778 1.00 59.07 ? 924 ALA A N 1 ATOM 6935 C CA . ALA A 1 924 ? -32.309 37.152 69.831 1.00 60.66 ? 924 ALA A CA 1 ATOM 6936 C C . ALA A 1 924 ? -33.578 37.414 69.032 1.00 57.01 ? 924 ALA A C 1 ATOM 6937 O O . ALA A 1 924 ? -34.072 36.538 68.323 1.00 52.94 ? 924 ALA A O 1 ATOM 6938 C CB . ALA A 1 924 ? -31.155 36.857 68.901 1.00 71.32 ? 924 ALA A CB 1 ATOM 6939 N N . SER A 1 925 ? -34.098 38.631 69.148 1.00 61.91 ? 925 SER A N 1 ATOM 6940 C CA . SER A 1 925 ? -35.306 39.020 68.436 1.00 65.77 ? 925 SER A CA 1 ATOM 6941 C C . SER A 1 925 ? -34.981 40.055 67.369 1.00 62.56 ? 925 SER A C 1 ATOM 6942 O O . SER A 1 925 ? -34.050 40.845 67.525 1.00 75.24 ? 925 SER A O 1 ATOM 6943 C CB . SER A 1 925 ? -36.348 39.578 69.408 1.00 75.38 ? 925 SER A CB 1 ATOM 6944 O OG . SER A 1 925 ? -36.542 38.706 70.507 1.00 85.28 ? 925 SER A OG 1 ATOM 6945 N N . PHE A 1 926 ? -35.746 40.047 66.283 1.00 55.82 ? 926 PHE A N 1 ATOM 6946 C CA . PHE A 1 926 ? -35.586 41.058 65.246 1.00 66.10 ? 926 PHE A CA 1 ATOM 6947 C C . PHE A 1 926 ? -36.943 41.550 64.760 1.00 68.90 ? 926 PHE A C 1 ATOM 6948 O O . PHE A 1 926 ? -37.906 40.788 64.692 1.00 78.65 ? 926 PHE A O 1 ATOM 6949 C CB . PHE A 1 926 ? -34.764 40.514 64.071 1.00 65.17 ? 926 PHE A CB 1 ATOM 6950 C CG . PHE A 1 926 ? -35.593 39.910 62.971 1.00 61.32 ? 926 PHE A CG 1 ATOM 6951 C CD1 . PHE A 1 926 ? -35.946 40.659 61.858 1.00 54.31 ? 926 PHE A CD1 1 ATOM 6952 C CD2 . PHE A 1 926 ? -36.011 38.594 63.045 1.00 67.69 ? 926 PHE A CD2 1 ATOM 6953 C CE1 . PHE A 1 926 ? -36.707 40.107 60.848 1.00 58.10 ? 926 PHE A CE1 1 ATOM 6954 C CE2 . PHE A 1 926 ? -36.770 38.036 62.034 1.00 60.85 ? 926 PHE A CE2 1 ATOM 6955 C CZ . PHE A 1 926 ? -37.118 38.793 60.935 1.00 57.97 ? 926 PHE A CZ 1 ATOM 6956 N N . ASN A 1 927 ? -37.008 42.834 64.427 1.00 59.58 ? 927 ASN A N 1 ATOM 6957 C CA . ASN A 1 927 ? -38.227 43.427 63.898 1.00 57.25 ? 927 ASN A CA 1 ATOM 6958 C C . ASN A 1 927 ? -37.899 44.419 62.788 1.00 56.66 ? 927 ASN A C 1 ATOM 6959 O O . ASN A 1 927 ? -37.034 45.278 62.954 1.00 56.59 ? 927 ASN A O 1 ATOM 6960 C CB . ASN A 1 927 ? -39.014 44.112 65.016 1.00 61.71 ? 927 ASN A CB 1 ATOM 6961 C CG . ASN A 1 927 ? -40.393 44.558 64.573 1.00 88.98 ? 927 ASN A CG 1 ATOM 6962 O OD1 . ASN A 1 927 ? -40.885 44.145 63.523 1.00 112.36 ? 927 ASN A OD1 1 ATOM 6963 N ND2 . ASN A 1 927 ? -41.029 45.400 65.378 1.00 97.58 ? 927 ASN A ND2 1 ATOM 6964 N N . VAL A 1 928 ? -38.591 44.300 61.660 1.00 58.16 ? 928 VAL A N 1 ATOM 6965 C CA . VAL A 1 928 ? -38.352 45.188 60.528 1.00 60.46 ? 928 VAL A CA 1 ATOM 6966 C C . VAL A 1 928 ? -39.293 46.384 60.599 1.00 69.18 ? 928 VAL A C 1 ATOM 6967 O O . VAL A 1 928 ? -40.506 46.246 60.437 1.00 78.93 ? 928 VAL A O 1 ATOM 6968 C CB . VAL A 1 928 ? -38.540 44.458 59.186 1.00 54.32 ? 928 VAL A CB 1 ATOM 6969 C CG1 . VAL A 1 928 ? -38.504 45.447 58.038 1.00 67.74 ? 928 VAL A CG1 1 ATOM 6970 C CG2 . VAL A 1 928 ? -37.473 43.387 59.011 1.00 52.76 ? 928 VAL A CG2 1 ATOM 6971 N N . ILE A 1 929 ? -38.724 47.558 60.854 1.00 57.60 ? 929 ILE A N 1 ATOM 6972 C CA . ILE A 1 929 ? -39.523 48.744 61.138 1.00 73.17 ? 929 ILE A CA 1 ATOM 6973 C C . ILE A 1 929 ? -39.758 49.684 59.956 1.00 80.45 ? 929 ILE A C 1 ATOM 6974 O O . ILE A 1 929 ? -40.530 50.636 60.073 1.00 95.93 ? 929 ILE A O 1 ATOM 6975 C CB . ILE A 1 929 ? -38.871 49.568 62.261 1.00 69.59 ? 929 ILE A CB 1 ATOM 6976 C CG1 . ILE A 1 929 ? -37.586 50.225 61.754 1.00 77.57 ? 929 ILE A CG1 1 ATOM 6977 C CG2 . ILE A 1 929 ? -38.580 48.686 63.463 1.00 60.47 ? 929 ILE A CG2 1 ATOM 6978 C CD1 . ILE A 1 929 ? -36.896 51.096 62.779 1.00 101.67 ? 929 ILE A CD1 1 ATOM 6979 N N . GLU A 1 930 ? -39.113 49.427 58.821 1.00 65.65 ? 930 GLU A N 1 ATOM 6980 C CA . GLU A 1 930 ? -39.232 50.348 57.691 1.00 67.82 ? 930 GLU A CA 1 ATOM 6981 C C . GLU A 1 930 ? -38.860 49.714 56.349 1.00 71.39 ? 930 GLU A C 1 ATOM 6982 O O . GLU A 1 930 ? -38.160 48.704 56.297 1.00 63.60 ? 930 GLU A O 1 ATOM 6983 C CB . GLU A 1 930 ? -38.366 51.588 57.944 1.00 78.28 ? 930 GLU A CB 1 ATOM 6984 C CG . GLU A 1 930 ? -38.800 52.830 57.179 1.00 98.31 ? 930 GLU A CG 1 ATOM 6985 C CD . GLU A 1 930 ? -38.123 54.090 57.682 1.00 121.89 ? 930 GLU A CD 1 ATOM 6986 O OE1 . GLU A 1 930 ? -37.760 54.946 56.848 1.00 130.24 ? 930 GLU A OE1 1 ATOM 6987 O OE2 . GLU A 1 930 ? -37.960 54.228 58.913 1.00 131.56 ? 930 GLU A OE2 1 ATOM 6988 N N . PHE A 1 931 ? -39.334 50.328 55.268 1.00 82.28 ? 931 PHE A N 1 ATOM 6989 C CA . PHE A 1 931 ? -39.023 49.887 53.912 1.00 80.07 ? 931 PHE A CA 1 ATOM 6990 C C . PHE A 1 931 ? -38.717 51.091 53.020 1.00 87.93 ? 931 PHE A C 1 ATOM 6991 O O . PHE A 1 931 ? -39.279 52.168 53.216 1.00 104.85 ? 931 PHE A O 1 ATOM 6992 C CB . PHE A 1 931 ? -40.182 49.075 53.328 1.00 74.33 ? 931 PHE A CB 1 ATOM 6993 C CG . PHE A 1 931 ? -40.447 47.788 54.053 1.00 63.72 ? 931 PHE A CG 1 ATOM 6994 C CD1 . PHE A 1 931 ? -39.816 46.617 53.667 1.00 58.20 ? 931 PHE A CD1 1 ATOM 6995 C CD2 . PHE A 1 931 ? -41.330 47.747 55.119 1.00 69.33 ? 931 PHE A CD2 1 ATOM 6996 C CE1 . PHE A 1 931 ? -40.059 45.430 54.331 1.00 65.09 ? 931 PHE A CE1 1 ATOM 6997 C CE2 . PHE A 1 931 ? -41.577 46.564 55.788 1.00 71.39 ? 931 PHE A CE2 1 ATOM 6998 C CZ . PHE A 1 931 ? -40.942 45.404 55.393 1.00 71.13 ? 931 PHE A CZ 1 ATOM 6999 N N . PRO A 1 932 ? -37.817 50.912 52.040 1.00 74.81 ? 932 PRO A N 1 ATOM 7000 C CA . PRO A 1 932 ? -37.433 51.992 51.123 1.00 80.31 ? 932 PRO A CA 1 ATOM 7001 C C . PRO A 1 932 ? -38.549 52.406 50.166 1.00 91.12 ? 932 PRO A C 1 ATOM 7002 O O . PRO A 1 932 ? -38.576 53.555 49.731 1.00 101.53 ? 932 PRO A O 1 ATOM 7003 C CB . PRO A 1 932 ? -36.257 51.390 50.348 1.00 76.62 ? 932 PRO A CB 1 ATOM 7004 C CG . PRO A 1 932 ? -36.479 49.922 50.417 1.00 74.41 ? 932 PRO A CG 1 ATOM 7005 C CD . PRO A 1 932 ? -37.063 49.676 51.774 1.00 70.24 ? 932 PRO A CD 1 ATOM 7006 N N . TYR A 1 933 ? -39.451 51.484 49.845 1.00 87.65 ? 933 TYR A N 1 ATOM 7007 C CA . TYR A 1 933 ? -40.532 51.774 48.908 1.00 91.12 ? 933 TYR A CA 1 ATOM 7008 C C . TYR A 1 933 ? -41.755 52.326 49.632 1.00 100.73 ? 933 TYR A C 1 ATOM 7009 O O . TYR A 1 933 ? -42.346 51.641 50.467 1.00 112.62 ? 933 TYR A O 1 ATOM 7010 C CB . TYR A 1 933 ? -40.921 50.518 48.123 1.00 87.73 ? 933 TYR A CB 1 ATOM 7011 C CG . TYR A 1 933 ? -39.853 49.447 48.080 1.00 87.94 ? 933 TYR A CG 1 ATOM 7012 C CD1 . TYR A 1 933 ? -38.859 49.468 47.111 1.00 96.79 ? 933 TYR A CD1 1 ATOM 7013 C CD2 . TYR A 1 933 ? -39.846 48.409 49.003 1.00 81.44 ? 933 TYR A CD2 1 ATOM 7014 C CE1 . TYR A 1 933 ? -37.883 48.488 47.066 1.00 80.83 ? 933 TYR A CE1 1 ATOM 7015 C CE2 . TYR A 1 933 ? -38.875 47.425 48.966 1.00 83.69 ? 933 TYR A CE2 1 ATOM 7016 C CZ . TYR A 1 933 ? -37.897 47.469 47.995 1.00 77.59 ? 933 TYR A CZ 1 ATOM 7017 O OH . TYR A 1 933 ? -36.929 46.492 47.954 1.00 75.01 ? 933 TYR A OH 1 ATOM 7018 N N . LYS A 1 934 ? -42.137 53.559 49.314 1.00 105.33 ? 934 LYS A N 1 ATOM 7019 C CA . LYS A 1 934 ? -43.318 54.149 49.933 1.00 111.24 ? 934 LYS A CA 1 ATOM 7020 C C . LYS A 1 934 ? -44.541 54.011 49.032 1.00 109.45 ? 934 LYS A C 1 ATOM 7021 O O . LYS A 1 934 ? -44.436 53.553 47.894 1.00 104.44 ? 934 LYS A O 1 ATOM 7022 C CB . LYS A 1 934 ? -43.073 55.623 50.264 1.00 117.67 ? 934 LYS A CB 1 ATOM 7023 C CG . LYS A 1 934 ? -41.807 55.879 51.068 1.00 118.52 ? 934 LYS A CG 1 ATOM 7024 C CD . LYS A 1 934 ? -41.764 55.038 52.333 1.00 115.45 ? 934 LYS A CD 1 ATOM 7025 C CE . LYS A 1 934 ? -40.458 55.248 53.083 1.00 108.69 ? 934 LYS A CE 1 ATOM 7026 N NZ . LYS A 1 934 ? -40.367 54.395 54.300 1.00 105.42 ? 934 LYS A NZ 1 ATOM 7027 N N . ASN A 1 935 ? -45.695 54.414 49.559 1.00 116.77 ? 935 ASN A N 1 ATOM 7028 C CA . ASN A 1 935 ? -46.987 54.286 48.883 1.00 127.73 ? 935 ASN A CA 1 ATOM 7029 C C . ASN A 1 935 ? -47.289 52.840 48.487 1.00 123.86 ? 935 ASN A C 1 ATOM 7030 O O . ASN A 1 935 ? -48.115 52.582 47.612 1.00 120.66 ? 935 ASN A O 1 ATOM 7031 C CB . ASN A 1 935 ? -47.044 55.192 47.650 1.00 129.64 ? 935 ASN A CB 1 ATOM 7032 C CG . ASN A 1 935 ? -46.969 56.664 48.006 1.00 129.24 ? 935 ASN A CG 1 ATOM 7033 O OD1 . ASN A 1 935 ? -45.885 57.239 48.095 1.00 134.92 ? 935 ASN A OD1 1 ATOM 7034 N ND2 . ASN A 1 935 ? -48.127 57.283 48.211 1.00 118.27 ? 935 ASN A ND2 1 ATOM 7035 N N . LEU A 1 936 ? -46.605 51.906 49.140 1.00 113.23 ? 936 LEU A N 1 ATOM 7036 C CA . LEU A 1 936 ? -46.847 50.478 48.977 1.00 109.51 ? 936 LEU A CA 1 ATOM 7037 C C . LEU A 1 936 ? -47.248 49.861 50.310 1.00 110.97 ? 936 LEU A C 1 ATOM 7038 O O . LEU A 1 936 ? -46.484 49.935 51.272 1.00 110.22 ? 936 LEU A O 1 ATOM 7039 C CB . LEU A 1 936 ? -45.615 49.772 48.405 1.00 107.08 ? 936 LEU A CB 1 ATOM 7040 C CG . LEU A 1 936 ? -45.562 49.640 46.879 1.00 114.67 ? 936 LEU A CG 1 ATOM 7041 C CD1 . LEU A 1 936 ? -45.413 50.995 46.205 1.00 119.22 ? 936 LEU A CD1 1 ATOM 7042 C CD2 . LEU A 1 936 ? -44.445 48.703 46.448 1.00 129.97 ? 936 LEU A CD2 1 ATOM 7043 N N . PRO A 1 937 ? -48.456 49.281 50.382 1.00 126.11 ? 937 PRO A N 1 ATOM 7044 C CA . PRO A 1 937 ? -48.912 48.624 51.613 1.00 131.23 ? 937 PRO A CA 1 ATOM 7045 C C . PRO A 1 937 ? -47.901 47.593 52.111 1.00 133.21 ? 937 PRO A C 1 ATOM 7046 O O . PRO A 1 937 ? -47.458 46.740 51.341 1.00 127.15 ? 937 PRO A O 1 ATOM 7047 C CB . PRO A 1 937 ? -50.219 47.950 51.187 1.00 135.54 ? 937 PRO A CB 1 ATOM 7048 C CG . PRO A 1 937 ? -50.702 48.769 50.039 1.00 141.91 ? 937 PRO A CG 1 ATOM 7049 C CD . PRO A 1 937 ? -49.466 49.215 49.312 1.00 138.45 ? 937 PRO A CD 1 ATOM 7050 N N . ILE A 1 938 ? -47.547 47.679 53.389 1.00 137.24 ? 938 ILE A N 1 ATOM 7051 C CA . ILE A 1 938 ? -46.486 46.851 53.949 1.00 123.34 ? 938 ILE A CA 1 ATOM 7052 C C . ILE A 1 938 ? -46.950 46.054 55.161 1.00 113.21 ? 938 ILE A C 1 ATOM 7053 O O . ILE A 1 938 ? -47.943 46.396 55.802 1.00 117.44 ? 938 ILE A O 1 ATOM 7054 C CB . ILE A 1 938 ? -45.272 47.706 54.361 1.00 116.33 ? 938 ILE A CB 1 ATOM 7055 C CG1 . ILE A 1 938 ? -45.729 48.899 55.206 1.00 104.98 ? 938 ILE A CG1 1 ATOM 7056 C CG2 . ILE A 1 938 ? -44.513 48.183 53.134 1.00 117.49 ? 938 ILE A CG2 1 ATOM 7057 C CD1 . ILE A 1 938 ? -44.605 49.818 55.631 1.00 99.02 ? 938 ILE A CD1 1 ATOM 7058 N N . GLU A 1 939 ? -46.220 44.987 55.466 1.00 106.10 ? 939 GLU A N 1 ATOM 7059 C CA . GLU A 1 939 ? -46.509 44.161 56.631 1.00 119.11 ? 939 GLU A CA 1 ATOM 7060 C C . GLU A 1 939 ? -45.253 43.988 57.478 1.00 117.43 ? 939 GLU A C 1 ATOM 7061 O O . GLU A 1 939 ? -44.167 43.754 56.948 1.00 110.39 ? 939 GLU A O 1 ATOM 7062 C CB . GLU A 1 939 ? -47.058 42.799 56.202 1.00 130.35 ? 939 GLU A CB 1 ATOM 7063 C CG . GLU A 1 939 ? -48.322 42.881 55.361 1.00 141.25 ? 939 GLU A CG 1 ATOM 7064 C CD . GLU A 1 939 ? -48.804 41.521 54.896 1.00 144.44 ? 939 GLU A CD 1 ATOM 7065 O OE1 . GLU A 1 939 ? -48.197 40.505 55.294 1.00 143.35 ? 939 GLU A OE1 1 ATOM 7066 O OE2 . GLU A 1 939 ? -49.790 41.469 54.132 1.00 144.64 ? 939 GLU A OE2 1 ATOM 7067 N N . ASP A 1 940 ? -45.407 44.109 58.792 1.00 117.79 ? 940 ASP A N 1 ATOM 7068 C CA . ASP A 1 940 ? -44.276 44.001 59.708 1.00 104.49 ? 940 ASP A CA 1 ATOM 7069 C C . ASP A 1 940 ? -43.686 42.596 59.718 1.00 86.62 ? 940 ASP A C 1 ATOM 7070 O O . ASP A 1 940 ? -44.412 41.603 59.663 1.00 88.94 ? 940 ASP A O 1 ATOM 7071 C CB . ASP A 1 940 ? -44.693 44.402 61.124 1.00 110.43 ? 940 ASP A CB 1 ATOM 7072 C CG . ASP A 1 940 ? -44.852 45.901 61.282 1.00 127.61 ? 940 ASP A CG 1 ATOM 7073 O OD1 . ASP A 1 940 ? -44.068 46.651 60.661 1.00 122.28 ? 940 ASP A OD1 1 ATOM 7074 O OD2 . ASP A 1 940 ? -45.759 46.331 62.025 1.00 147.53 ? 940 ASP A OD2 1 ATOM 7075 N N . ILE A 1 941 ? -42.361 42.525 59.786 1.00 80.91 ? 941 ILE A N 1 ATOM 7076 C CA . ILE A 1 941 ? -41.656 41.250 59.810 1.00 78.77 ? 941 ILE A CA 1 ATOM 7077 C C . ILE A 1 941 ? -40.944 41.063 61.143 1.00 78.76 ? 941 ILE A C 1 ATOM 7078 O O . ILE A 1 941 ? -40.076 41.855 61.512 1.00 86.52 ? 941 ILE A O 1 ATOM 7079 C CB . ILE A 1 941 ? -40.636 41.149 58.664 1.00 73.85 ? 941 ILE A CB 1 ATOM 7080 C CG1 . ILE A 1 941 ? -41.318 41.427 57.324 1.00 75.27 ? 941 ILE A CG1 1 ATOM 7081 C CG2 . ILE A 1 941 ? -39.973 39.780 58.662 1.00 72.63 ? 941 ILE A CG2 1 ATOM 7082 C CD1 . ILE A 1 941 ? -40.360 41.556 56.166 1.00 72.44 ? 941 ILE A CD1 1 ATOM 7083 N N . THR A 1 942 ? -41.319 40.012 61.863 1.00 81.26 ? 942 THR A N 1 ATOM 7084 C CA . THR A 1 942 ? -40.772 39.757 63.188 1.00 83.00 ? 942 THR A CA 1 ATOM 7085 C C . THR A 1 942 ? -40.607 38.258 63.413 1.00 97.06 ? 942 THR A C 1 ATOM 7086 O O . THR A 1 942 ? -41.404 37.461 62.916 1.00 123.80 ? 942 THR A O 1 ATOM 7087 C CB . THR A 1 942 ? -41.678 40.350 64.292 1.00 98.01 ? 942 THR A CB 1 ATOM 7088 O OG1 . THR A 1 942 ? -42.053 41.687 63.940 1.00 112.02 ? 942 THR A OG1 1 ATOM 7089 C CG2 . THR A 1 942 ? -40.965 40.366 65.636 1.00 100.01 ? 942 THR A CG2 1 ATOM 7090 N N . ASN A 1 943 ? -39.584 37.889 64.180 1.00 90.99 ? 943 ASN A N 1 ATOM 7091 C CA . ASN A 1 943 ? -39.308 36.495 64.509 1.00 95.41 ? 943 ASN A CA 1 ATOM 7092 C C . ASN A 1 943 ? -38.148 36.398 65.488 1.00 86.91 ? 943 ASN A C 1 ATOM 7093 O O . ASN A 1 943 ? -37.377 37.343 65.647 1.00 84.83 ? 943 ASN A O 1 ATOM 7094 C CB . ASN A 1 943 ? -38.992 35.687 63.248 1.00 102.53 ? 943 ASN A CB 1 ATOM 7095 C CG . ASN A 1 943 ? -39.519 34.270 63.318 1.00 114.40 ? 943 ASN A CG 1 ATOM 7096 O OD1 . ASN A 1 943 ? -39.406 33.601 64.345 1.00 117.28 ? 943 ASN A OD1 1 ATOM 7097 N ND2 . ASN A 1 943 ? -40.105 33.807 62.222 1.00 136.61 ? 943 ASN A ND2 1 ATOM 7098 N N . SER A 1 944 ? -38.024 35.246 66.138 1.00 82.08 ? 944 SER A N 1 ATOM 7099 C CA . SER A 1 944 ? -37.031 35.076 67.188 1.00 79.30 ? 944 SER A CA 1 ATOM 7100 C C . SER A 1 944 ? -36.282 33.759 67.052 1.00 84.58 ? 944 SER A C 1 ATOM 7101 O O . SER A 1 944 ? -36.738 32.836 66.378 1.00 107.38 ? 944 SER A O 1 ATOM 7102 C CB . SER A 1 944 ? -37.697 35.154 68.564 1.00 83.18 ? 944 SER A CB 1 ATOM 7103 O OG . SER A 1 944 ? -38.424 36.361 68.710 1.00 108.53 ? 944 SER A OG 1 ATOM 7104 N N . THR A 1 945 ? -35.125 33.685 67.698 1.00 68.35 ? 945 THR A N 1 ATOM 7105 C CA . THR A 1 945 ? -34.347 32.456 67.750 1.00 66.75 ? 945 THR A CA 1 ATOM 7106 C C . THR A 1 945 ? -33.521 32.442 69.029 1.00 64.97 ? 945 THR A C 1 ATOM 7107 O O . THR A 1 945 ? -33.213 33.494 69.591 1.00 64.18 ? 945 THR A O 1 ATOM 7108 C CB . THR A 1 945 ? -33.425 32.306 66.523 1.00 62.21 ? 945 THR A CB 1 ATOM 7109 O OG1 . THR A 1 945 ? -32.842 30.997 66.516 1.00 89.33 ? 945 THR A OG1 1 ATOM 7110 C CG2 . THR A 1 945 ? -32.320 33.349 66.549 1.00 57.53 ? 945 THR A CG2 1 ATOM 7111 N N . LEU A 1 946 ? -33.173 31.249 69.495 1.00 73.43 ? 946 LEU A N 1 ATOM 7112 C CA . LEU A 1 946 ? -32.404 31.119 70.725 1.00 67.92 ? 946 LEU A CA 1 ATOM 7113 C C . LEU A 1 946 ? -31.129 30.318 70.494 1.00 58.92 ? 946 LEU A C 1 ATOM 7114 O O . LEU A 1 946 ? -31.081 29.433 69.640 1.00 58.99 ? 946 LEU A O 1 ATOM 7115 C CB . LEU A 1 946 ? -33.246 30.467 71.829 1.00 73.84 ? 946 LEU A CB 1 ATOM 7116 C CG . LEU A 1 946 ? -33.537 28.964 71.774 1.00 81.69 ? 946 LEU A CG 1 ATOM 7117 C CD1 . LEU A 1 946 ? -34.062 28.487 73.120 1.00 86.02 ? 946 LEU A CD1 1 ATOM 7118 C CD2 . LEU A 1 946 ? -34.526 28.615 70.670 1.00 91.73 ? 946 LEU A CD2 1 ATOM 7119 N N . VAL A 1 947 ? -30.094 30.646 71.259 1.00 57.56 ? 947 VAL A N 1 ATOM 7120 C CA . VAL A 1 947 ? -28.819 29.948 71.173 1.00 59.21 ? 947 VAL A CA 1 ATOM 7121 C C . VAL A 1 947 ? -28.422 29.416 72.543 1.00 66.52 ? 947 VAL A C 1 ATOM 7122 O O . VAL A 1 947 ? -28.344 30.170 73.514 1.00 83.34 ? 947 VAL A O 1 ATOM 7123 C CB . VAL A 1 947 ? -27.712 30.864 70.627 1.00 54.61 ? 947 VAL A CB 1 ATOM 7124 C CG1 . VAL A 1 947 ? -26.344 30.248 70.859 1.00 55.12 ? 947 VAL A CG1 1 ATOM 7125 C CG2 . VAL A 1 947 ? -27.938 31.127 69.153 1.00 53.71 ? 947 VAL A CG2 1 ATOM 7126 N N . THR A 1 948 ? -28.177 28.113 72.617 1.00 64.04 ? 948 THR A N 1 ATOM 7127 C CA . THR A 1 948 ? -27.906 27.466 73.891 1.00 63.14 ? 948 THR A CA 1 ATOM 7128 C C . THR A 1 948 ? -26.470 26.962 74.002 1.00 64.84 ? 948 THR A C 1 ATOM 7129 O O . THR A 1 948 ? -25.922 26.386 73.062 1.00 64.34 ? 948 THR A O 1 ATOM 7130 C CB . THR A 1 948 ? -28.875 26.288 74.129 1.00 71.87 ? 948 THR A CB 1 ATOM 7131 O OG1 . THR A 1 948 ? -28.456 25.543 75.279 1.00 94.01 ? 948 THR A OG1 1 ATOM 7132 C CG2 . THR A 1 948 ? -28.914 25.366 72.915 1.00 70.88 ? 948 THR A CG2 1 ATOM 7133 N N . THR A 1 949 ? -25.862 27.201 75.160 1.00 71.10 ? 949 THR A N 1 ATOM 7134 C CA . THR A 1 949 ? -24.554 26.642 75.477 1.00 71.38 ? 949 THR A CA 1 ATOM 7135 C C . THR A 1 949 ? -24.675 25.766 76.718 1.00 83.36 ? 949 THR A C 1 ATOM 7136 O O . THR A 1 949 ? -24.905 26.265 77.819 1.00 98.41 ? 949 THR A O 1 ATOM 7137 C CB . THR A 1 949 ? -23.503 27.741 75.719 1.00 63.11 ? 949 THR A CB 1 ATOM 7138 O OG1 . THR A 1 949 ? -23.429 28.597 74.572 1.00 68.43 ? 949 THR A OG1 1 ATOM 7139 C CG2 . THR A 1 949 ? -22.138 27.123 75.973 1.00 62.70 ? 949 THR A CG2 1 ATOM 7140 N N . ASN A 1 950 ? -24.516 24.459 76.538 1.00 79.22 ? 950 ASN A N 1 ATOM 7141 C CA . ASN A 1 950 ? -24.742 23.515 77.626 1.00 86.54 ? 950 ASN A CA 1 ATOM 7142 C C . ASN A 1 950 ? -23.458 23.117 78.344 1.00 85.44 ? 950 ASN A C 1 ATOM 7143 O O . ASN A 1 950 ? -22.609 22.432 77.780 1.00 102.69 ? 950 ASN A O 1 ATOM 7144 C CB . ASN A 1 950 ? -25.441 22.259 77.100 1.00 94.12 ? 950 ASN A CB 1 ATOM 7145 C CG . ASN A 1 950 ? -26.760 22.565 76.416 1.00 99.58 ? 950 ASN A CG 1 ATOM 7146 O OD1 . ASN A 1 950 ? -26.937 23.630 75.825 1.00 96.27 ? 950 ASN A OD1 1 ATOM 7147 N ND2 . ASN A 1 950 ? -27.695 21.625 76.495 1.00 121.07 ? 950 ASN A ND2 1 ATOM 7148 N N . VAL A 1 951 ? -23.327 23.539 79.596 1.00 82.43 ? 951 VAL A N 1 ATOM 7149 C CA . VAL A 1 951 ? -22.183 23.150 80.410 1.00 80.10 ? 951 VAL A CA 1 ATOM 7150 C C . VAL A 1 951 ? -22.555 21.964 81.300 1.00 82.01 ? 951 VAL A C 1 ATOM 7151 O O . VAL A 1 951 ? -23.509 22.030 82.076 1.00 83.58 ? 951 VAL A O 1 ATOM 7152 C CB . VAL A 1 951 ? -21.672 24.327 81.270 1.00 74.53 ? 951 VAL A CB 1 ATOM 7153 C CG1 . VAL A 1 951 ? -22.835 25.101 81.875 1.00 84.30 ? 951 VAL A CG1 1 ATOM 7154 C CG2 . VAL A 1 951 ? -20.718 23.831 82.345 1.00 79.24 ? 951 VAL A CG2 1 ATOM 7155 N N . THR A 1 952 ? -21.803 20.876 81.174 1.00 83.31 ? 952 THR A N 1 ATOM 7156 C CA . THR A 1 952 ? -22.135 19.637 81.868 1.00 88.45 ? 952 THR A CA 1 ATOM 7157 C C . THR A 1 952 ? -20.911 18.972 82.493 1.00 98.42 ? 952 THR A C 1 ATOM 7158 O O . THR A 1 952 ? -19.795 19.483 82.398 1.00 102.81 ? 952 THR A O 1 ATOM 7159 C CB . THR A 1 952 ? -22.813 18.636 80.915 1.00 93.82 ? 952 THR A CB 1 ATOM 7160 O OG1 . THR A 1 952 ? -22.988 17.379 81.581 1.00 121.00 ? 952 THR A OG1 1 ATOM 7161 C CG2 . THR A 1 952 ? -21.964 18.431 79.668 1.00 87.42 ? 952 THR A CG2 1 ATOM 7162 N N . TRP A 1 953 ? -21.134 17.828 83.133 1.00 107.73 ? 953 TRP A N 1 ATOM 7163 C CA . TRP A 1 953 ? -20.062 17.083 83.784 1.00 113.30 ? 953 TRP A CA 1 ATOM 7164 C C . TRP A 1 953 ? -19.873 15.706 83.156 1.00 113.91 ? 953 TRP A C 1 ATOM 7165 O O . TRP A 1 953 ? -20.813 14.915 83.077 1.00 111.56 ? 953 TRP A O 1 ATOM 7166 C CB . TRP A 1 953 ? -20.346 16.935 85.281 1.00 120.85 ? 953 TRP A CB 1 ATOM 7167 C CG . TRP A 1 953 ? -20.234 18.216 86.044 1.00 119.53 ? 953 TRP A CG 1 ATOM 7168 C CD1 . TRP A 1 953 ? -21.172 19.203 86.132 1.00 109.76 ? 953 TRP A CD1 1 ATOM 7169 C CD2 . TRP A 1 953 ? -19.120 18.650 86.833 1.00 121.51 ? 953 TRP A CD2 1 ATOM 7170 N NE1 . TRP A 1 953 ? -20.710 20.225 86.925 1.00 106.08 ? 953 TRP A NE1 1 ATOM 7171 C CE2 . TRP A 1 953 ? -19.452 19.910 87.367 1.00 106.28 ? 953 TRP A CE2 1 ATOM 7172 C CE3 . TRP A 1 953 ? -17.873 18.095 87.139 1.00 129.99 ? 953 TRP A CE3 1 ATOM 7173 C CZ2 . TRP A 1 953 ? -18.585 20.625 88.191 1.00 106.17 ? 953 TRP A CZ2 1 ATOM 7174 C CZ3 . TRP A 1 953 ? -17.013 18.807 87.956 1.00 127.12 ? 953 TRP A CZ3 1 ATOM 7175 C CH2 . TRP A 1 953 ? -17.372 20.058 88.472 1.00 115.96 ? 953 TRP A CH2 1 ATOM 7176 N N . GLY A 1 954 ? -18.652 15.427 82.712 1.00 116.39 ? 954 GLY A N 1 ATOM 7177 C CA . GLY A 1 954 ? -18.331 14.139 82.125 1.00 124.84 ? 954 GLY A CA 1 ATOM 7178 C C . GLY A 1 954 ? -18.160 13.064 83.180 1.00 134.52 ? 954 GLY A C 1 ATOM 7179 O O . GLY A 1 954 ? -18.315 11.875 82.902 1.00 129.96 ? 954 GLY A O 1 ATOM 7180 N N . ILE A 1 955 ? -17.839 13.487 84.398 1.00 144.10 ? 955 ILE A N 1 ATOM 7181 C CA . ILE A 1 955 ? -17.663 12.560 85.510 1.00 151.69 ? 955 ILE A CA 1 ATOM 7182 C C . ILE A 1 955 ? -18.420 13.033 86.748 1.00 156.01 ? 955 ILE A C 1 ATOM 7183 O O . ILE A 1 955 ? -18.325 14.195 87.144 1.00 144.74 ? 955 ILE A O 1 ATOM 7184 C CB . ILE A 1 955 ? -16.171 12.374 85.859 1.00 144.47 ? 955 ILE A CB 1 ATOM 7185 C CG1 . ILE A 1 955 ? -15.457 13.726 85.903 1.00 139.05 ? 955 ILE A CG1 1 ATOM 7186 C CG2 . ILE A 1 955 ? -15.499 11.463 84.844 1.00 134.38 ? 955 ILE A CG2 1 ATOM 7187 C CD1 . ILE A 1 955 ? -13.981 13.628 86.224 1.00 136.87 ? 955 ILE A CD1 1 ATOM 7188 N N . GLN A 1 956 ? -19.179 12.124 87.352 1.00 163.49 ? 956 GLN A N 1 ATOM 7189 C CA . GLN A 1 956 ? -19.962 12.446 88.539 1.00 151.43 ? 956 GLN A CA 1 ATOM 7190 C C . GLN A 1 956 ? -19.418 11.729 89.771 1.00 144.22 ? 956 GLN A C 1 ATOM 7191 O O . GLN A 1 956 ? -20.151 11.025 90.465 1.00 144.01 ? 956 GLN A O 1 ATOM 7192 C CB . GLN A 1 956 ? -21.435 12.083 88.330 1.00 150.89 ? 956 GLN A CB 1 ATOM 7193 C CG . GLN A 1 956 ? -22.164 12.946 87.307 1.00 143.23 ? 956 GLN A CG 1 ATOM 7194 C CD . GLN A 1 956 ? -21.877 12.540 85.874 1.00 138.86 ? 956 GLN A CD 1 ATOM 7195 O OE1 . GLN A 1 956 ? -21.240 11.518 85.621 1.00 147.49 ? 956 GLN A OE1 1 ATOM 7196 N NE2 . GLN A 1 956 ? -22.352 13.342 84.927 1.00 126.80 ? 956 GLN A NE2 1 ATOM 7197 N N . GLY B 2 1 ? -51.491 6.052 15.322 1.00 148.69 ? 1 GLY B N 1 ATOM 7198 C CA . GLY B 2 1 ? -51.971 7.250 14.658 1.00 151.56 ? 1 GLY B CA 1 ATOM 7199 C C . GLY B 2 1 ? -50.840 8.113 14.134 1.00 158.69 ? 1 GLY B C 1 ATOM 7200 O O . GLY B 2 1 ? -49.702 7.654 14.036 1.00 155.97 ? 1 GLY B O 1 ATOM 7201 N N . PRO B 2 2 ? -51.150 9.372 13.787 1.00 162.55 ? 2 PRO B N 1 ATOM 7202 C CA . PRO B 2 2 ? -50.158 10.327 13.281 1.00 153.80 ? 2 PRO B CA 1 ATOM 7203 C C . PRO B 2 2 ? -49.048 10.600 14.292 1.00 144.21 ? 2 PRO B C 1 ATOM 7204 O O . PRO B 2 2 ? -49.332 10.868 15.459 1.00 138.45 ? 2 PRO B O 1 ATOM 7205 C CB . PRO B 2 2 ? -50.984 11.593 13.027 1.00 150.57 ? 2 PRO B CB 1 ATOM 7206 C CG . PRO B 2 2 ? -52.388 11.111 12.873 1.00 150.53 ? 2 PRO B CG 1 ATOM 7207 C CD . PRO B 2 2 ? -52.507 9.945 13.803 1.00 159.70 ? 2 PRO B CD 1 ATOM 7208 N N . ASN B 2 3 ? -47.800 10.530 13.842 1.00 145.67 ? 3 ASN B N 1 ATOM 7209 C CA . ASN B 2 3 ? -46.660 10.790 14.712 1.00 143.27 ? 3 ASN B CA 1 ATOM 7210 C C . ASN B 2 3 ? -45.708 11.819 14.112 1.00 130.46 ? 3 ASN B C 1 ATOM 7211 O O . ASN B 2 3 ? -45.989 12.400 13.065 1.00 121.57 ? 3 ASN B O 1 ATOM 7212 C CB . ASN B 2 3 ? -45.909 9.489 15.018 1.00 143.69 ? 3 ASN B CB 1 ATOM 7213 C CG . ASN B 2 3 ? -45.499 8.733 13.764 1.00 140.20 ? 3 ASN B CG 1 ATOM 7214 O OD1 . ASN B 2 3 ? -45.341 9.315 12.691 1.00 134.96 ? 3 ASN B OD1 1 ATOM 7215 N ND2 . ASN B 2 3 ? -45.322 7.424 13.899 1.00 143.23 ? 3 ASN B ND2 1 ATOM 7216 N N . ILE B 2 4 ? -44.582 12.035 14.784 1.00 123.76 ? 4 ILE B N 1 ATOM 7217 C CA . ILE B 2 4 ? -43.581 12.992 14.326 1.00 112.35 ? 4 ILE B CA 1 ATOM 7218 C C . ILE B 2 4 ? -42.976 12.555 12.990 1.00 103.08 ? 4 ILE B C 1 ATOM 7219 O O . ILE B 2 4 ? -42.528 13.384 12.198 1.00 109.84 ? 4 ILE B O 1 ATOM 7220 C CB . ILE B 2 4 ? -42.462 13.174 15.384 1.00 113.57 ? 4 ILE B CB 1 ATOM 7221 C CG1 . ILE B 2 4 ? -41.511 14.306 14.990 1.00 110.77 ? 4 ILE B CG1 1 ATOM 7222 C CG2 . ILE B 2 4 ? -41.707 11.869 15.609 1.00 120.90 ? 4 ILE B CG2 1 ATOM 7223 C CD1 . ILE B 2 4 ? -40.374 14.516 15.966 1.00 118.31 ? 4 ILE B CD1 1 ATOM 7224 N N . CYS B 2 5 ? -42.990 11.250 12.736 1.00 185.03 ? 5 CYS B N 1 ATOM 7225 C CA . CYS B 2 5 ? -42.408 10.694 11.520 1.00 170.73 ? 5 CYS B CA 1 ATOM 7226 C C . CYS B 2 5 ? -43.280 10.930 10.291 1.00 166.73 ? 5 CYS B C 1 ATOM 7227 O O . CYS B 2 5 ? -42.786 11.335 9.238 1.00 163.22 ? 5 CYS B O 1 ATOM 7228 C CB . CYS B 2 5 ? -42.162 9.195 11.694 1.00 161.61 ? 5 CYS B CB 1 ATOM 7229 S SG . CYS B 2 5 ? -40.846 8.781 12.856 1.00 144.69 ? 5 CYS B SG 1 ATOM 7230 N N . THR B 2 6 ? -44.577 10.676 10.428 1.00 162.97 ? 6 THR B N 1 ATOM 7231 C CA . THR B 2 6 ? -45.500 10.773 9.303 1.00 158.25 ? 6 THR B CA 1 ATOM 7232 C C . THR B 2 6 ? -45.894 12.215 8.992 1.00 158.94 ? 6 THR B C 1 ATOM 7233 O O . THR B 2 6 ? -46.550 12.480 7.986 1.00 167.22 ? 6 THR B O 1 ATOM 7234 C CB . THR B 2 6 ? -46.782 9.957 9.560 1.00 159.00 ? 6 THR B CB 1 ATOM 7235 O OG1 . THR B 2 6 ? -47.448 10.461 10.724 1.00 160.90 ? 6 THR B OG1 1 ATOM 7236 C CG2 . THR B 2 6 ? -46.447 8.489 9.769 1.00 162.57 ? 6 THR B CG2 1 ATOM 7237 N N . THR B 2 7 ? -45.515 13.140 9.866 1.00 151.50 ? 7 THR B N 1 ATOM 7238 C CA . THR B 2 7 ? -45.834 14.549 9.660 1.00 150.57 ? 7 THR B CA 1 ATOM 7239 C C . THR B 2 7 ? -44.689 15.354 9.045 1.00 147.55 ? 7 THR B C 1 ATOM 7240 O O . THR B 2 7 ? -44.846 16.542 8.768 1.00 156.67 ? 7 THR B O 1 ATOM 7241 C CB . THR B 2 7 ? -46.246 15.222 10.983 1.00 152.29 ? 7 THR B CB 1 ATOM 7242 O OG1 . THR B 2 7 ? -45.256 14.956 11.984 1.00 150.56 ? 7 THR B OG1 1 ATOM 7243 C CG2 . THR B 2 7 ? -47.591 14.693 11.454 1.00 157.38 ? 7 THR B CG2 1 ATOM 7244 N N . ARG B 2 8 ? -43.539 14.718 8.837 1.00 143.72 ? 8 ARG B N 1 ATOM 7245 C CA . ARG B 2 8 ? -42.367 15.443 8.349 1.00 142.01 ? 8 ARG B CA 1 ATOM 7246 C C . ARG B 2 8 ? -41.655 14.787 7.166 1.00 141.76 ? 8 ARG B C 1 ATOM 7247 O O . ARG B 2 8 ? -41.664 15.317 6.055 1.00 142.14 ? 8 ARG B O 1 ATOM 7248 C CB . ARG B 2 8 ? -41.368 15.640 9.493 1.00 135.00 ? 8 ARG B CB 1 ATOM 7249 C CG . ARG B 2 8 ? -41.749 16.748 10.461 1.00 139.02 ? 8 ARG B CG 1 ATOM 7250 C CD . ARG B 2 8 ? -40.799 16.802 11.646 1.00 142.11 ? 8 ARG B CD 1 ATOM 7251 N NE . ARG B 2 8 ? -41.035 17.974 12.485 1.00 144.01 ? 8 ARG B NE 1 ATOM 7252 C CZ . ARG B 2 8 ? -41.976 18.048 13.420 1.00 144.15 ? 8 ARG B CZ 1 ATOM 7253 N NH1 . ARG B 2 8 ? -42.782 17.018 13.637 1.00 145.70 ? 8 ARG B NH1 1 ATOM 7254 N NH2 . ARG B 2 8 ? -42.117 19.155 14.136 1.00 145.22 ? 8 ARG B NH2 1 ATOM 7255 N N . GLY B 2 9 ? -41.040 13.635 7.412 1.00 136.68 ? 9 GLY B N 1 ATOM 7256 C CA . GLY B 2 9 ? -40.122 13.038 6.458 1.00 134.52 ? 9 GLY B CA 1 ATOM 7257 C C . GLY B 2 9 ? -40.737 12.211 5.345 1.00 136.23 ? 9 GLY B C 1 ATOM 7258 O O . GLY B 2 9 ? -40.046 11.412 4.713 1.00 142.65 ? 9 GLY B O 1 ATOM 7259 N N . VAL B 2 10 ? -42.030 12.393 5.099 1.00 136.03 ? 10 VAL B N 1 ATOM 7260 C CA . VAL B 2 10 ? -42.714 11.665 4.034 1.00 139.79 ? 10 VAL B CA 1 ATOM 7261 C C . VAL B 2 10 ? -42.191 12.088 2.659 1.00 141.10 ? 10 VAL B C 1 ATOM 7262 O O . VAL B 2 10 ? -42.401 11.397 1.661 1.00 143.36 ? 10 VAL B O 1 ATOM 7263 C CB . VAL B 2 10 ? -44.238 11.885 4.096 1.00 147.26 ? 10 VAL B CB 1 ATOM 7264 C CG1 . VAL B 2 10 ? -44.971 10.818 3.295 1.00 149.21 ? 10 VAL B CG1 1 ATOM 7265 C CG2 . VAL B 2 10 ? -44.704 11.866 5.535 1.00 150.04 ? 10 VAL B CG2 1 ATOM 7266 N N . SER B 2 11 ? -41.501 13.223 2.622 1.00 142.88 ? 11 SER B N 1 ATOM 7267 C CA . SER B 2 11 ? -40.955 13.761 1.381 1.00 144.38 ? 11 SER B CA 1 ATOM 7268 C C . SER B 2 11 ? -39.938 12.826 0.727 1.00 146.28 ? 11 SER B C 1 ATOM 7269 O O . SER B 2 11 ? -39.950 12.645 -0.490 1.00 149.62 ? 11 SER B O 1 ATOM 7270 C CB . SER B 2 11 ? -40.312 15.126 1.640 1.00 141.64 ? 11 SER B CB 1 ATOM 7271 O OG . SER B 2 11 ? -39.330 15.042 2.659 1.00 137.62 ? 11 SER B OG 1 ATOM 7272 N N . SER B 2 12 ? -39.061 12.234 1.533 1.00 149.67 ? 12 SER B N 1 ATOM 7273 C CA . SER B 2 12 ? -38.005 11.379 0.998 1.00 151.20 ? 12 SER B CA 1 ATOM 7274 C C . SER B 2 12 ? -37.592 10.267 1.959 1.00 152.79 ? 12 SER B C 1 ATOM 7275 O O . SER B 2 12 ? -38.212 10.068 3.003 1.00 152.31 ? 12 SER B O 1 ATOM 7276 C CB . SER B 2 12 ? -36.780 12.223 0.636 1.00 145.63 ? 12 SER B CB 1 ATOM 7277 O OG . SER B 2 12 ? -35.705 11.405 0.208 1.00 145.70 ? 12 SER B OG 1 ATOM 7278 N N . CYS B 2 13 ? -36.540 9.544 1.588 1.00 153.44 ? 13 CYS B N 1 ATOM 7279 C CA . CYS B 2 13 ? -35.985 8.483 2.422 1.00 147.44 ? 13 CYS B CA 1 ATOM 7280 C C . CYS B 2 13 ? -34.964 9.042 3.405 1.00 137.57 ? 13 CYS B C 1 ATOM 7281 O O . CYS B 2 13 ? -35.148 8.959 4.620 1.00 129.90 ? 13 CYS B O 1 ATOM 7282 C CB . CYS B 2 13 ? -35.338 7.398 1.560 1.00 151.20 ? 13 CYS B CB 1 ATOM 7283 S SG . CYS B 2 13 ? -34.333 6.217 2.492 1.00 164.90 ? 13 CYS B SG 1 ATOM 7284 N N . GLN B 2 14 ? -33.880 9.591 2.865 1.00 134.02 ? 14 GLN B N 1 ATOM 7285 C CA . GLN B 2 14 ? -32.822 10.195 3.669 1.00 133.59 ? 14 GLN B CA 1 ATOM 7286 C C . GLN B 2 14 ? -33.372 11.275 4.595 1.00 131.50 ? 14 GLN B C 1 ATOM 7287 O O . GLN B 2 14 ? -32.923 11.419 5.733 1.00 133.34 ? 14 GLN B O 1 ATOM 7288 C CB . GLN B 2 14 ? -31.737 10.781 2.762 1.00 137.68 ? 14 GLN B CB 1 ATOM 7289 C CG . GLN B 2 14 ? -30.579 11.424 3.507 1.00 135.41 ? 14 GLN B CG 1 ATOM 7290 C CD . GLN B 2 14 ? -29.549 12.027 2.572 1.00 138.27 ? 14 GLN B CD 1 ATOM 7291 O OE1 . GLN B 2 14 ? -29.727 12.032 1.353 1.00 139.16 ? 14 GLN B OE1 1 ATOM 7292 N NE2 . GLN B 2 14 ? -28.463 12.540 3.139 1.00 144.53 ? 14 GLN B NE2 1 ATOM 7293 N N . GLN B 2 15 ? -34.350 12.028 4.103 1.00 129.29 ? 15 GLN B N 1 ATOM 7294 C CA . GLN B 2 15 ? -34.983 13.074 4.897 1.00 129.75 ? 15 GLN B CA 1 ATOM 7295 C C . GLN B 2 15 ? -35.851 12.481 6.002 1.00 124.87 ? 15 GLN B C 1 ATOM 7296 O O . GLN B 2 15 ? -36.086 13.120 7.027 1.00 122.07 ? 15 GLN B O 1 ATOM 7297 C CB . GLN B 2 15 ? -35.820 13.993 4.005 1.00 141.27 ? 15 GLN B CB 1 ATOM 7298 C CG . GLN B 2 15 ? -35.001 14.805 3.015 1.00 151.25 ? 15 GLN B CG 1 ATOM 7299 C CD . GLN B 2 15 ? -35.847 15.777 2.217 1.00 158.60 ? 15 GLN B CD 1 ATOM 7300 O OE1 . GLN B 2 15 ? -37.074 15.776 2.315 1.00 166.89 ? 15 GLN B OE1 1 ATOM 7301 N NE2 . GLN B 2 15 ? -35.193 16.616 1.422 1.00 154.15 ? 15 GLN B NE2 1 ATOM 7302 N N . CYS B 2 16 ? -36.328 11.258 5.789 1.00 124.55 ? 16 CYS B N 1 ATOM 7303 C CA . CYS B 2 16 ? -37.106 10.560 6.806 1.00 120.29 ? 16 CYS B CA 1 ATOM 7304 C C . CYS B 2 16 ? -36.188 9.999 7.882 1.00 114.02 ? 16 CYS B C 1 ATOM 7305 O O . CYS B 2 16 ? -36.576 9.891 9.047 1.00 109.57 ? 16 CYS B O 1 ATOM 7306 C CB . CYS B 2 16 ? -37.936 9.436 6.185 1.00 120.33 ? 16 CYS B CB 1 ATOM 7307 S SG . CYS B 2 16 ? -38.858 8.445 7.385 1.00 101.16 ? 16 CYS B SG 1 ATOM 7308 N N . LEU B 2 17 ? -34.969 9.643 7.486 1.00 117.14 ? 17 LEU B N 1 ATOM 7309 C CA . LEU B 2 17 ? -33.996 9.104 8.426 1.00 114.25 ? 17 LEU B CA 1 ATOM 7310 C C . LEU B 2 17 ? -33.649 10.134 9.491 1.00 105.60 ? 17 LEU B C 1 ATOM 7311 O O . LEU B 2 17 ? -33.375 9.775 10.637 1.00 100.99 ? 17 LEU B O 1 ATOM 7312 C CB . LEU B 2 17 ? -32.735 8.632 7.700 1.00 108.65 ? 17 LEU B CB 1 ATOM 7313 C CG . LEU B 2 17 ? -32.604 7.107 7.641 1.00 98.87 ? 17 LEU B CG 1 ATOM 7314 C CD1 . LEU B 2 17 ? -33.820 6.492 6.965 1.00 106.23 ? 17 LEU B CD1 1 ATOM 7315 C CD2 . LEU B 2 17 ? -31.326 6.685 6.938 1.00 99.78 ? 17 LEU B CD2 1 ATOM 7316 N N . ALA B 2 18 ? -33.661 11.414 9.128 1.00 105.40 ? 18 ALA B N 1 ATOM 7317 C CA . ALA B 2 18 ? -33.602 12.434 10.161 1.00 107.95 ? 18 ALA B CA 1 ATOM 7318 C C . ALA B 2 18 ? -34.963 13.088 10.339 1.00 110.30 ? 18 ALA B C 1 ATOM 7319 O O . ALA B 2 18 ? -35.344 13.988 9.592 1.00 113.85 ? 18 ALA B O 1 ATOM 7320 C CB . ALA B 2 18 ? -32.559 13.482 9.814 1.00 112.37 ? 18 ALA B CB 1 ATOM 7321 N N . VAL B 2 19 ? -35.680 12.621 11.354 1.00 110.17 ? 19 VAL B N 1 ATOM 7322 C CA . VAL B 2 19 ? -36.807 13.317 11.951 1.00 124.09 ? 19 VAL B CA 1 ATOM 7323 C C . VAL B 2 19 ? -36.621 13.153 13.449 1.00 126.83 ? 19 VAL B C 1 ATOM 7324 O O . VAL B 2 19 ? -36.369 14.104 14.188 1.00 136.72 ? 19 VAL B O 1 ATOM 7325 C CB . VAL B 2 19 ? -38.167 12.747 11.506 1.00 141.51 ? 19 VAL B CB 1 ATOM 7326 C CG1 . VAL B 2 19 ? -39.295 13.424 12.263 1.00 144.34 ? 19 VAL B CG1 1 ATOM 7327 C CG2 . VAL B 2 19 ? -38.357 12.907 10.004 1.00 152.60 ? 19 VAL B CG2 1 ATOM 7328 N N . SER B 2 20 ? -36.755 11.897 13.861 1.00 119.72 ? 20 SER B N 1 ATOM 7329 C CA . SER B 2 20 ? -36.442 11.429 15.200 1.00 118.80 ? 20 SER B CA 1 ATOM 7330 C C . SER B 2 20 ? -35.718 10.095 15.039 1.00 110.59 ? 20 SER B C 1 ATOM 7331 O O . SER B 2 20 ? -35.973 9.369 14.078 1.00 108.82 ? 20 SER B O 1 ATOM 7332 C CB . SER B 2 20 ? -37.714 11.279 16.039 1.00 125.31 ? 20 SER B CB 1 ATOM 7333 O OG . SER B 2 20 ? -37.431 10.781 17.335 1.00 125.22 ? 20 SER B OG 1 ATOM 7334 N N . PRO B 2 21 ? -34.803 9.769 15.964 1.00 107.73 ? 21 PRO B N 1 ATOM 7335 C CA . PRO B 2 21 ? -34.066 8.501 15.884 1.00 105.06 ? 21 PRO B CA 1 ATOM 7336 C C . PRO B 2 21 ? -34.966 7.265 15.910 1.00 109.17 ? 21 PRO B C 1 ATOM 7337 O O . PRO B 2 21 ? -34.521 6.176 15.549 1.00 112.87 ? 21 PRO B O 1 ATOM 7338 C CB . PRO B 2 21 ? -33.166 8.538 17.125 1.00 103.46 ? 21 PRO B CB 1 ATOM 7339 C CG . PRO B 2 21 ? -33.752 9.591 18.013 1.00 112.73 ? 21 PRO B CG 1 ATOM 7340 C CD . PRO B 2 21 ? -34.338 10.600 17.085 1.00 112.16 ? 21 PRO B CD 1 ATOM 7341 N N . MET B 2 22 ? -36.212 7.438 16.337 1.00 115.88 ? 22 MET B N 1 ATOM 7342 C CA . MET B 2 22 ? -37.164 6.336 16.402 1.00 130.61 ? 22 MET B CA 1 ATOM 7343 C C . MET B 2 22 ? -37.752 6.003 15.031 1.00 132.56 ? 22 MET B C 1 ATOM 7344 O O . MET B 2 22 ? -38.288 4.914 14.828 1.00 140.11 ? 22 MET B O 1 ATOM 7345 C CB . MET B 2 22 ? -38.289 6.669 17.384 1.00 138.79 ? 22 MET B CB 1 ATOM 7346 C CG . MET B 2 22 ? -39.059 7.934 17.035 1.00 138.68 ? 22 MET B CG 1 ATOM 7347 S SD . MET B 2 22 ? -40.296 8.367 18.273 1.00 159.95 ? 22 MET B SD 1 ATOM 7348 C CE . MET B 2 22 ? -39.261 8.610 19.714 1.00 173.15 ? 22 MET B CE 1 ATOM 7349 N N . CYS B 2 23 ? -37.644 6.942 14.096 1.00 125.53 ? 23 CYS B N 1 ATOM 7350 C CA . CYS B 2 23 ? -38.251 6.793 12.775 1.00 127.90 ? 23 CYS B CA 1 ATOM 7351 C C . CYS B 2 23 ? -37.601 5.689 11.944 1.00 124.15 ? 23 CYS B C 1 ATOM 7352 O O . CYS B 2 23 ? -36.444 5.331 12.163 1.00 122.51 ? 23 CYS B O 1 ATOM 7353 C CB . CYS B 2 23 ? -38.181 8.116 12.010 1.00 128.26 ? 23 CYS B CB 1 ATOM 7354 S SG . CYS B 2 23 ? -38.952 9.510 12.860 1.00 202.27 ? 23 CYS B SG 1 ATOM 7355 N N . ALA B 2 24 ? -38.359 5.157 10.990 1.00 126.98 ? 24 ALA B N 1 ATOM 7356 C CA . ALA B 2 24 ? -37.853 4.142 10.071 1.00 129.03 ? 24 ALA B CA 1 ATOM 7357 C C . ALA B 2 24 ? -38.320 4.432 8.647 1.00 137.17 ? 24 ALA B C 1 ATOM 7358 O O . ALA B 2 24 ? -39.033 5.406 8.408 1.00 140.66 ? 24 ALA B O 1 ATOM 7359 C CB . ALA B 2 24 ? -38.298 2.758 10.509 1.00 123.36 ? 24 ALA B CB 1 ATOM 7360 N N . TRP B 2 25 ? -37.923 3.583 7.704 1.00 138.35 ? 25 TRP B N 1 ATOM 7361 C CA . TRP B 2 25 ? -38.244 3.807 6.298 1.00 140.98 ? 25 TRP B CA 1 ATOM 7362 C C . TRP B 2 25 ? -38.660 2.520 5.584 1.00 147.90 ? 25 TRP B C 1 ATOM 7363 O O . TRP B 2 25 ? -38.272 1.427 5.994 1.00 151.97 ? 25 TRP B O 1 ATOM 7364 C CB . TRP B 2 25 ? -37.050 4.439 5.580 1.00 137.42 ? 25 TRP B CB 1 ATOM 7365 C CG . TRP B 2 25 ? -37.298 4.646 4.131 1.00 140.70 ? 25 TRP B CG 1 ATOM 7366 C CD1 . TRP B 2 25 ? -36.737 3.958 3.096 1.00 146.34 ? 25 TRP B CD1 1 ATOM 7367 C CD2 . TRP B 2 25 ? -38.209 5.580 3.549 1.00 146.72 ? 25 TRP B CD2 1 ATOM 7368 N NE1 . TRP B 2 25 ? -37.229 4.423 1.901 1.00 153.54 ? 25 TRP B NE1 1 ATOM 7369 C CE2 . TRP B 2 25 ? -38.136 5.418 2.153 1.00 152.63 ? 25 TRP B CE2 1 ATOM 7370 C CE3 . TRP B 2 25 ? -39.074 6.546 4.072 1.00 149.03 ? 25 TRP B CE3 1 ATOM 7371 C CZ2 . TRP B 2 25 ? -38.894 6.183 1.274 1.00 154.59 ? 25 TRP B CZ2 1 ATOM 7372 C CZ3 . TRP B 2 25 ? -39.826 7.306 3.197 1.00 147.82 ? 25 TRP B CZ3 1 ATOM 7373 C CH2 . TRP B 2 25 ? -39.730 7.121 1.814 1.00 149.64 ? 25 TRP B CH2 1 ATOM 7374 N N . CYS B 2 26 ? -39.440 2.652 4.513 1.00 148.18 ? 26 CYS B N 1 ATOM 7375 C CA . CYS B 2 26 ? -39.938 1.483 3.794 1.00 150.33 ? 26 CYS B CA 1 ATOM 7376 C C . CYS B 2 26 ? -39.592 1.468 2.302 1.00 152.47 ? 26 CYS B C 1 ATOM 7377 O O . CYS B 2 26 ? -40.073 2.288 1.520 1.00 156.41 ? 26 CYS B O 1 ATOM 7378 C CB . CYS B 2 26 ? -41.455 1.376 3.962 1.00 153.21 ? 26 CYS B CB 1 ATOM 7379 S SG . CYS B 2 26 ? -42.007 -0.182 4.694 1.00 193.33 ? 26 CYS B SG 1 ATOM 7380 N N . SER B 2 27 ? -38.749 0.508 1.936 1.00 151.99 ? 27 SER B N 1 ATOM 7381 C CA . SER B 2 27 ? -38.463 0.135 0.553 1.00 159.53 ? 27 SER B CA 1 ATOM 7382 C C . SER B 2 27 ? -39.460 -0.942 0.138 1.00 168.57 ? 27 SER B C 1 ATOM 7383 O O . SER B 2 27 ? -40.524 -1.057 0.751 1.00 173.47 ? 27 SER B O 1 ATOM 7384 C CB . SER B 2 27 ? -37.025 -0.355 0.394 1.00 167.15 ? 27 SER B CB 1 ATOM 7385 O OG . SER B 2 27 ? -36.099 0.653 0.753 1.00 172.70 ? 27 SER B OG 1 ATOM 7386 N N . ASP B 2 28 ? -39.140 -1.695 -0.916 1.00 171.66 ? 28 ASP B N 1 ATOM 7387 C CA . ASP B 2 28 ? -39.998 -2.795 -1.367 1.00 170.44 ? 28 ASP B CA 1 ATOM 7388 C C . ASP B 2 28 ? -41.349 -2.297 -1.874 1.00 170.83 ? 28 ASP B C 1 ATOM 7389 O O . ASP B 2 28 ? -42.358 -2.347 -1.171 1.00 169.91 ? 28 ASP B O 1 ATOM 7390 C CB . ASP B 2 28 ? -40.194 -3.825 -0.245 1.00 170.72 ? 28 ASP B CB 1 ATOM 7391 C CG . ASP B 2 28 ? -41.041 -5.007 -0.676 1.00 181.68 ? 28 ASP B CG 1 ATOM 7392 O OD1 . ASP B 2 28 ? -40.992 -5.375 -1.868 1.00 190.16 ? 28 ASP B OD1 1 ATOM 7393 O OD2 . ASP B 2 28 ? -41.756 -5.568 0.181 1.00 183.03 ? 28 ASP B OD2 1 ATOM 7394 N N . GLU B 2 29 ? -41.334 -1.801 -3.109 1.00 175.39 ? 29 GLU B N 1 ATOM 7395 C CA . GLU B 2 29 ? -42.454 -1.095 -3.729 1.00 172.81 ? 29 GLU B CA 1 ATOM 7396 C C . GLU B 2 29 ? -43.769 -1.876 -3.751 1.00 166.06 ? 29 GLU B C 1 ATOM 7397 O O . GLU B 2 29 ? -44.805 -1.320 -4.111 1.00 162.08 ? 29 GLU B O 1 ATOM 7398 C CB . GLU B 2 29 ? -42.094 -0.709 -5.170 1.00 174.35 ? 29 GLU B CB 1 ATOM 7399 C CG . GLU B 2 29 ? -40.641 -0.303 -5.390 1.00 169.21 ? 29 GLU B CG 1 ATOM 7400 C CD . GLU B 2 29 ? -39.741 -1.482 -5.720 1.00 167.32 ? 29 GLU B CD 1 ATOM 7401 O OE1 . GLU B 2 29 ? -39.768 -2.484 -4.975 1.00 167.57 ? 29 GLU B OE1 1 ATOM 7402 O OE2 . GLU B 2 29 ? -39.008 -1.408 -6.729 1.00 168.48 ? 29 GLU B OE2 1 ATOM 7403 N N . ALA B 2 30 ? -43.724 -3.160 -3.403 1.00 164.01 ? 30 ALA B N 1 ATOM 7404 C CA . ALA B 2 30 ? -44.933 -3.977 -3.318 1.00 166.93 ? 30 ALA B CA 1 ATOM 7405 C C . ALA B 2 30 ? -46.001 -3.303 -2.457 1.00 172.53 ? 30 ALA B C 1 ATOM 7406 O O . ALA B 2 30 ? -45.727 -2.873 -1.335 1.00 161.01 ? 30 ALA B O 1 ATOM 7407 C CB . ALA B 2 30 ? -44.601 -5.354 -2.764 1.00 166.16 ? 30 ALA B CB 1 ATOM 7408 N N . LEU B 2 31 ? -47.215 -3.219 -3.001 1.00 188.91 ? 31 LEU B N 1 ATOM 7409 C CA . LEU B 2 31 ? -48.340 -2.541 -2.354 1.00 182.23 ? 31 LEU B CA 1 ATOM 7410 C C . LEU B 2 31 ? -48.009 -1.106 -1.939 1.00 167.24 ? 31 LEU B C 1 ATOM 7411 O O . LEU B 2 31 ? -47.851 -0.821 -0.752 1.00 158.30 ? 31 LEU B O 1 ATOM 7412 C CB . LEU B 2 31 ? -48.814 -3.341 -1.138 1.00 175.65 ? 31 LEU B CB 1 ATOM 7413 C CG . LEU B 2 31 ? -49.363 -4.736 -1.441 1.00 165.09 ? 31 LEU B CG 1 ATOM 7414 C CD1 . LEU B 2 31 ? -49.745 -5.458 -0.159 1.00 163.05 ? 31 LEU B CD1 1 ATOM 7415 C CD2 . LEU B 2 31 ? -50.552 -4.646 -2.386 1.00 166.54 ? 31 LEU B CD2 1 ATOM 7416 N N . PRO B 2 32 ? -47.901 -0.196 -2.923 1.00 171.03 ? 32 PRO B N 1 ATOM 7417 C CA . PRO B 2 32 ? -47.550 1.202 -2.649 1.00 173.54 ? 32 PRO B CA 1 ATOM 7418 C C . PRO B 2 32 ? -48.699 2.000 -2.037 1.00 182.20 ? 32 PRO B C 1 ATOM 7419 O O . PRO B 2 32 ? -49.803 1.479 -1.874 1.00 184.03 ? 32 PRO B O 1 ATOM 7420 C CB . PRO B 2 32 ? -47.196 1.762 -4.036 1.00 173.86 ? 32 PRO B CB 1 ATOM 7421 C CG . PRO B 2 32 ? -47.150 0.578 -4.963 1.00 179.68 ? 32 PRO B CG 1 ATOM 7422 C CD . PRO B 2 32 ? -48.057 -0.442 -4.365 1.00 179.29 ? 32 PRO B CD 1 ATOM 7423 N N . LEU B 2 33 ? -48.418 3.261 -1.719 1.00 185.51 ? 33 LEU B N 1 ATOM 7424 C CA . LEU B 2 33 ? -49.374 4.181 -1.102 1.00 184.25 ? 33 LEU B CA 1 ATOM 7425 C C . LEU B 2 33 ? -50.044 3.580 0.129 1.00 191.33 ? 33 LEU B C 1 ATOM 7426 O O . LEU B 2 33 ? -49.415 2.859 0.903 1.00 195.55 ? 33 LEU B O 1 ATOM 7427 C CB . LEU B 2 33 ? -50.447 4.605 -2.113 1.00 180.37 ? 33 LEU B CB 1 ATOM 7428 C CG . LEU B 2 33 ? -50.084 5.612 -3.210 1.00 174.26 ? 33 LEU B CG 1 ATOM 7429 C CD1 . LEU B 2 33 ? -49.288 4.961 -4.334 1.00 173.60 ? 33 LEU B CD1 1 ATOM 7430 C CD2 . LEU B 2 33 ? -51.339 6.280 -3.756 1.00 175.09 ? 33 LEU B CD2 1 ATOM 7431 N N . GLY B 2 34 ? -51.328 3.885 0.298 1.00 195.75 ? 34 GLY B N 1 ATOM 7432 C CA . GLY B 2 34 ? -52.151 3.297 1.342 1.00 200.99 ? 34 GLY B CA 1 ATOM 7433 C C . GLY B 2 34 ? -51.699 3.573 2.766 1.00 202.23 ? 34 GLY B C 1 ATOM 7434 O O . GLY B 2 34 ? -52.339 3.120 3.717 1.00 200.69 ? 34 GLY B O 1 ATOM 7435 N N . SER B 2 35 ? -50.625 4.349 2.906 1.00 203.41 ? 35 SER B N 1 ATOM 7436 C CA . SER B 2 35 ? -49.955 4.569 4.187 1.00 198.81 ? 35 SER B CA 1 ATOM 7437 C C . SER B 2 35 ? -48.696 5.406 3.984 1.00 192.25 ? 35 SER B C 1 ATOM 7438 O O . SER B 2 35 ? -48.127 5.419 2.893 1.00 193.15 ? 35 SER B O 1 ATOM 7439 C CB . SER B 2 35 ? -49.584 3.239 4.851 1.00 195.12 ? 35 SER B CB 1 ATOM 7440 O OG . SER B 2 35 ? -48.674 2.506 4.049 1.00 188.81 ? 35 SER B OG 1 ATOM 7441 N N . PRO B 2 36 ? -48.256 6.113 5.036 1.00 185.11 ? 36 PRO B N 1 ATOM 7442 C CA . PRO B 2 36 ? -46.977 6.827 4.971 1.00 179.80 ? 36 PRO B CA 1 ATOM 7443 C C . PRO B 2 36 ? -45.792 5.863 4.968 1.00 172.10 ? 36 PRO B C 1 ATOM 7444 O O . PRO B 2 36 ? -45.832 4.844 5.656 1.00 174.25 ? 36 PRO B O 1 ATOM 7445 C CB . PRO B 2 36 ? -46.981 7.683 6.244 1.00 181.66 ? 36 PRO B CB 1 ATOM 7446 C CG . PRO B 2 36 ? -48.413 7.734 6.680 1.00 185.97 ? 36 PRO B CG 1 ATOM 7447 C CD . PRO B 2 36 ? -48.995 6.421 6.271 1.00 187.50 ? 36 PRO B CD 1 ATOM 7448 N N . ARG B 2 37 ? -44.757 6.183 4.198 1.00 163.84 ? 37 ARG B N 1 ATOM 7449 C CA . ARG B 2 37 ? -43.562 5.348 4.137 1.00 160.70 ? 37 ARG B CA 1 ATOM 7450 C C . ARG B 2 37 ? -42.566 5.717 5.232 1.00 160.95 ? 37 ARG B C 1 ATOM 7451 O O . ARG B 2 37 ? -41.602 4.992 5.479 1.00 163.20 ? 37 ARG B O 1 ATOM 7452 C CB . ARG B 2 37 ? -42.891 5.470 2.766 1.00 155.83 ? 37 ARG B CB 1 ATOM 7453 C CG . ARG B 2 37 ? -43.735 4.984 1.600 1.00 159.72 ? 37 ARG B CG 1 ATOM 7454 C CD . ARG B 2 37 ? -43.018 5.212 0.278 1.00 166.19 ? 37 ARG B CD 1 ATOM 7455 N NE . ARG B 2 37 ? -43.779 4.705 -0.861 1.00 176.15 ? 37 ARG B NE 1 ATOM 7456 C CZ . ARG B 2 37 ? -43.585 3.515 -1.419 1.00 175.86 ? 37 ARG B CZ 1 ATOM 7457 N NH1 . ARG B 2 37 ? -42.651 2.701 -0.946 1.00 173.11 ? 37 ARG B NH1 1 ATOM 7458 N NH2 . ARG B 2 37 ? -44.325 3.138 -2.453 1.00 175.67 ? 37 ARG B NH2 1 ATOM 7459 N N . CYS B 2 38 ? -42.809 6.847 5.886 1.00 153.39 ? 38 CYS B N 1 ATOM 7460 C CA . CYS B 2 38 ? -41.862 7.399 6.848 1.00 143.08 ? 38 CYS B CA 1 ATOM 7461 C C . CYS B 2 38 ? -42.150 6.972 8.287 1.00 141.69 ? 38 CYS B C 1 ATOM 7462 O O . CYS B 2 38 ? -41.487 7.432 9.214 1.00 140.92 ? 38 CYS B O 1 ATOM 7463 C CB . CYS B 2 38 ? -41.848 8.927 6.757 1.00 144.75 ? 38 CYS B CB 1 ATOM 7464 S SG . CYS B 2 38 ? -40.431 9.716 7.564 1.00 196.71 ? 38 CYS B SG 1 ATOM 7465 N N . ASP B 2 39 ? -43.119 6.082 8.481 1.00 148.11 ? 39 ASP B N 1 ATOM 7466 C CA . ASP B 2 39 ? -43.542 5.736 9.835 1.00 147.83 ? 39 ASP B CA 1 ATOM 7467 C C . ASP B 2 39 ? -42.444 4.943 10.544 1.00 145.48 ? 39 ASP B C 1 ATOM 7468 O O . ASP B 2 39 ? -41.413 4.635 9.946 1.00 144.68 ? 39 ASP B O 1 ATOM 7469 C CB . ASP B 2 39 ? -44.851 4.943 9.801 1.00 145.18 ? 39 ASP B CB 1 ATOM 7470 C CG . ASP B 2 39 ? -45.682 5.135 11.055 1.00 148.88 ? 39 ASP B CG 1 ATOM 7471 O OD1 . ASP B 2 39 ? -45.277 5.937 11.922 1.00 158.23 ? 39 ASP B OD1 1 ATOM 7472 O OD2 . ASP B 2 39 ? -46.750 4.498 11.165 1.00 152.12 ? 39 ASP B OD2 1 ATOM 7473 N N . LEU B 2 40 ? -42.658 4.609 11.813 1.00 141.28 ? 40 LEU B N 1 ATOM 7474 C CA . LEU B 2 40 ? -41.562 4.095 12.629 1.00 142.16 ? 40 LEU B CA 1 ATOM 7475 C C . LEU B 2 40 ? -41.751 2.674 13.145 1.00 144.88 ? 40 LEU B C 1 ATOM 7476 O O . LEU B 2 40 ? -42.812 2.075 12.979 1.00 152.30 ? 40 LEU B O 1 ATOM 7477 C CB . LEU B 2 40 ? -41.333 5.035 13.820 1.00 147.20 ? 40 LEU B CB 1 ATOM 7478 C CG . LEU B 2 40 ? -42.555 5.532 14.608 1.00 147.90 ? 40 LEU B CG 1 ATOM 7479 C CD1 . LEU B 2 40 ? -43.156 4.456 15.507 1.00 145.37 ? 40 LEU B CD1 1 ATOM 7480 C CD2 . LEU B 2 40 ? -42.203 6.763 15.428 1.00 155.22 ? 40 LEU B CD2 1 ATOM 7481 N N . LYS B 2 41 ? -40.699 2.164 13.785 1.00 138.54 ? 41 LYS B N 1 ATOM 7482 C CA . LYS B 2 41 ? -40.728 0.924 14.560 1.00 138.05 ? 41 LYS B CA 1 ATOM 7483 C C . LYS B 2 41 ? -41.461 -0.233 13.885 1.00 139.31 ? 41 LYS B C 1 ATOM 7484 O O . LYS B 2 41 ? -41.135 -0.623 12.763 1.00 138.04 ? 41 LYS B O 1 ATOM 7485 C CB . LYS B 2 41 ? -41.341 1.194 15.935 1.00 147.90 ? 41 LYS B CB 1 ATOM 7486 C CG . LYS B 2 41 ? -40.527 2.161 16.779 1.00 150.19 ? 41 LYS B CG 1 ATOM 7487 C CD . LYS B 2 41 ? -41.115 2.331 18.168 1.00 155.42 ? 41 LYS B CD 1 ATOM 7488 C CE . LYS B 2 41 ? -40.263 3.268 19.010 1.00 153.50 ? 41 LYS B CE 1 ATOM 7489 N NZ . LYS B 2 41 ? -40.791 3.412 20.394 1.00 158.23 ? 41 LYS B NZ 1 ATOM 7490 N N . GLU B 2 42 ? -42.453 -0.772 14.585 1.00 147.17 ? 42 GLU B N 1 ATOM 7491 C CA . GLU B 2 42 ? -43.199 -1.931 14.111 1.00 154.64 ? 42 GLU B CA 1 ATOM 7492 C C . GLU B 2 42 ? -44.432 -1.536 13.303 1.00 152.32 ? 42 GLU B C 1 ATOM 7493 O O . GLU B 2 42 ? -45.206 -2.396 12.885 1.00 151.98 ? 42 GLU B O 1 ATOM 7494 C CB . GLU B 2 42 ? -43.618 -2.816 15.289 1.00 165.98 ? 42 GLU B CB 1 ATOM 7495 C CG . GLU B 2 42 ? -44.751 -2.247 16.134 1.00 175.80 ? 42 GLU B CG 1 ATOM 7496 C CD . GLU B 2 42 ? -44.330 -1.043 16.955 1.00 175.97 ? 42 GLU B CD 1 ATOM 7497 O OE1 . GLU B 2 42 ? -43.166 -1.010 17.409 1.00 169.14 ? 42 GLU B OE1 1 ATOM 7498 O OE2 . GLU B 2 42 ? -45.160 -0.129 17.143 1.00 179.88 ? 42 GLU B OE2 1 ATOM 7499 N N . ASN B 2 43 ? -44.621 -0.237 13.093 1.00 153.94 ? 43 ASN B N 1 ATOM 7500 C CA . ASN B 2 43 ? -45.761 0.238 12.317 1.00 157.30 ? 43 ASN B CA 1 ATOM 7501 C C . ASN B 2 43 ? -45.627 -0.132 10.844 1.00 153.31 ? 43 ASN B C 1 ATOM 7502 O O . ASN B 2 43 ? -46.626 -0.340 10.155 1.00 156.49 ? 43 ASN B O 1 ATOM 7503 C CB . ASN B 2 43 ? -45.924 1.750 12.468 1.00 161.96 ? 43 ASN B CB 1 ATOM 7504 C CG . ASN B 2 43 ? -46.291 2.157 13.881 1.00 168.27 ? 43 ASN B CG 1 ATOM 7505 O OD1 . ASN B 2 43 ? -46.789 1.347 14.663 1.00 173.85 ? 43 ASN B OD1 1 ATOM 7506 N ND2 . ASN B 2 43 ? -46.053 3.420 14.213 1.00 165.43 ? 43 ASN B ND2 1 ATOM 7507 N N . LEU B 2 44 ? -44.390 -0.209 10.364 1.00 149.67 ? 44 LEU B N 1 ATOM 7508 C CA . LEU B 2 44 ? -44.134 -0.695 9.015 1.00 154.73 ? 44 LEU B CA 1 ATOM 7509 C C . LEU B 2 44 ? -44.070 -2.216 9.036 1.00 164.96 ? 44 LEU B C 1 ATOM 7510 O O . LEU B 2 44 ? -44.119 -2.864 7.993 1.00 168.54 ? 44 LEU B O 1 ATOM 7511 C CB . LEU B 2 44 ? -42.834 -0.117 8.450 1.00 151.04 ? 44 LEU B CB 1 ATOM 7512 C CG . LEU B 2 44 ? -42.517 1.346 8.760 1.00 149.25 ? 44 LEU B CG 1 ATOM 7513 C CD1 . LEU B 2 44 ? -41.615 1.429 9.976 1.00 155.62 ? 44 LEU B CD1 1 ATOM 7514 C CD2 . LEU B 2 44 ? -41.877 2.035 7.566 1.00 141.93 ? 44 LEU B CD2 1 ATOM 7515 N N . LEU B 2 45 ? -43.938 -2.774 10.237 1.00 161.68 ? 45 LEU B N 1 ATOM 7516 C CA . LEU B 2 45 ? -43.984 -4.218 10.429 1.00 158.39 ? 45 LEU B CA 1 ATOM 7517 C C . LEU B 2 45 ? -45.434 -4.695 10.462 1.00 168.82 ? 45 LEU B C 1 ATOM 7518 O O . LEU B 2 45 ? -45.718 -5.866 10.207 1.00 180.30 ? 45 LEU B O 1 ATOM 7519 C CB . LEU B 2 45 ? -43.254 -4.618 11.713 1.00 154.49 ? 45 LEU B CB 1 ATOM 7520 C CG . LEU B 2 45 ? -43.015 -6.110 11.950 1.00 165.88 ? 45 LEU B CG 1 ATOM 7521 C CD1 . LEU B 2 45 ? -42.153 -6.697 10.844 1.00 170.48 ? 45 LEU B CD1 1 ATOM 7522 C CD2 . LEU B 2 45 ? -42.378 -6.341 13.311 1.00 165.82 ? 45 LEU B CD2 1 ATOM 7523 N N . LYS B 2 46 ? -46.344 -3.779 10.790 1.00 171.67 ? 46 LYS B N 1 ATOM 7524 C CA . LYS B 2 46 ? -47.779 -4.044 10.712 1.00 186.22 ? 46 LYS B CA 1 ATOM 7525 C C . LYS B 2 46 ? -48.143 -4.483 9.298 1.00 191.63 ? 46 LYS B C 1 ATOM 7526 O O . LYS B 2 46 ? -48.605 -5.604 9.086 1.00 201.92 ? 46 LYS B O 1 ATOM 7527 C CB . LYS B 2 46 ? -48.585 -2.812 11.127 1.00 190.32 ? 46 LYS B CB 1 ATOM 7528 C CG . LYS B 2 46 ? -48.443 -2.460 12.600 1.00 191.29 ? 46 LYS B CG 1 ATOM 7529 C CD . LYS B 2 46 ? -49.291 -1.257 12.979 1.00 190.80 ? 46 LYS B CD 1 ATOM 7530 C CE . LYS B 2 46 ? -49.167 -0.948 14.463 1.00 188.45 ? 46 LYS B CE 1 ATOM 7531 N NZ . LYS B 2 46 ? -49.985 0.231 14.861 1.00 187.90 ? 46 LYS B NZ 1 ATOM 7532 N N . ASP B 2 47 ? -47.937 -3.589 8.335 1.00 182.30 ? 47 ASP B N 1 ATOM 7533 C CA . ASP B 2 47 ? -47.943 -3.975 6.930 1.00 181.52 ? 47 ASP B CA 1 ATOM 7534 C C . ASP B 2 47 ? -46.788 -4.949 6.743 1.00 183.14 ? 47 ASP B C 1 ATOM 7535 O O . ASP B 2 47 ? -45.833 -4.906 7.515 1.00 179.45 ? 47 ASP B O 1 ATOM 7536 C CB . ASP B 2 47 ? -47.790 -2.756 6.019 1.00 172.54 ? 47 ASP B CB 1 ATOM 7537 C CG . ASP B 2 47 ? -48.435 -1.511 6.597 1.00 171.17 ? 47 ASP B CG 1 ATOM 7538 O OD1 . ASP B 2 47 ? -49.341 -1.647 7.446 1.00 172.30 ? 47 ASP B OD1 1 ATOM 7539 O OD2 . ASP B 2 47 ? -48.033 -0.396 6.205 1.00 171.65 ? 47 ASP B OD2 1 ATOM 7540 N N . ASN B 2 48 ? -46.869 -5.835 5.753 1.00 185.41 ? 48 ASN B N 1 ATOM 7541 C CA . ASN B 2 48 ? -45.848 -6.873 5.608 1.00 183.09 ? 48 ASN B CA 1 ATOM 7542 C C . ASN B 2 48 ? -44.446 -6.276 5.521 1.00 182.63 ? 48 ASN B C 1 ATOM 7543 O O . ASN B 2 48 ? -43.684 -6.353 6.485 1.00 182.93 ? 48 ASN B O 1 ATOM 7544 C CB . ASN B 2 48 ? -46.131 -7.729 4.373 1.00 177.06 ? 48 ASN B CB 1 ATOM 7545 C CG . ASN B 2 48 ? -47.461 -8.451 4.457 1.00 175.16 ? 48 ASN B CG 1 ATOM 7546 O OD1 . ASN B 2 48 ? -48.318 -8.104 5.271 1.00 171.82 ? 48 ASN B OD1 1 ATOM 7547 N ND2 . ASN B 2 48 ? -47.640 -9.461 3.615 1.00 181.68 ? 48 ASN B ND2 1 ATOM 7548 N N . CYS B 2 49 ? -44.120 -5.700 4.366 1.00 178.74 ? 49 CYS B N 1 ATOM 7549 C CA . CYS B 2 49 ? -43.045 -4.714 4.218 1.00 170.77 ? 49 CYS B CA 1 ATOM 7550 C C . CYS B 2 49 ? -41.769 -5.015 5.008 1.00 175.66 ? 49 CYS B C 1 ATOM 7551 O O . CYS B 2 49 ? -41.152 -4.102 5.557 1.00 174.89 ? 49 CYS B O 1 ATOM 7552 C CB . CYS B 2 49 ? -43.567 -3.327 4.609 1.00 161.82 ? 49 CYS B CB 1 ATOM 7553 S SG . CYS B 2 49 ? -42.636 -1.943 3.904 1.00 182.87 ? 49 CYS B SG 1 ATOM 7554 N N . ALA B 2 50 ? -41.369 -6.280 5.079 1.00 181.91 ? 50 ALA B N 1 ATOM 7555 C CA . ALA B 2 50 ? -40.182 -6.616 5.863 1.00 180.95 ? 50 ALA B CA 1 ATOM 7556 C C . ALA B 2 50 ? -39.173 -7.529 5.160 1.00 191.87 ? 50 ALA B C 1 ATOM 7557 O O . ALA B 2 50 ? -38.876 -8.616 5.655 1.00 195.07 ? 50 ALA B O 1 ATOM 7558 C CB . ALA B 2 50 ? -40.607 -7.249 7.182 1.00 183.94 ? 50 ALA B CB 1 ATOM 7559 N N . PRO B 2 51 ? -38.636 -7.093 4.007 1.00 197.34 ? 51 PRO B N 1 ATOM 7560 C CA . PRO B 2 51 ? -37.427 -7.729 3.483 1.00 199.05 ? 51 PRO B CA 1 ATOM 7561 C C . PRO B 2 51 ? -36.206 -7.077 4.115 1.00 189.86 ? 51 PRO B C 1 ATOM 7562 O O . PRO B 2 51 ? -36.356 -6.324 5.075 1.00 179.67 ? 51 PRO B O 1 ATOM 7563 C CB . PRO B 2 51 ? -37.491 -7.445 1.974 1.00 200.37 ? 51 PRO B CB 1 ATOM 7564 C CG . PRO B 2 51 ? -38.808 -6.728 1.741 1.00 198.87 ? 51 PRO B CG 1 ATOM 7565 C CD . PRO B 2 51 ? -39.159 -6.107 3.049 1.00 195.10 ? 51 PRO B CD 1 ATOM 7566 N N . GLU B 2 52 ? -35.018 -7.365 3.593 1.00 192.80 ? 52 GLU B N 1 ATOM 7567 C CA . GLU B 2 52 ? -33.834 -6.574 3.920 1.00 187.18 ? 52 GLU B CA 1 ATOM 7568 C C . GLU B 2 52 ? -34.077 -5.108 3.542 1.00 183.47 ? 52 GLU B C 1 ATOM 7569 O O . GLU B 2 52 ? -33.417 -4.198 4.047 1.00 179.80 ? 52 GLU B O 1 ATOM 7570 C CB . GLU B 2 52 ? -32.602 -7.131 3.196 1.00 188.60 ? 52 GLU B CB 1 ATOM 7571 C CG . GLU B 2 52 ? -31.320 -6.327 3.384 1.00 184.98 ? 52 GLU B CG 1 ATOM 7572 C CD . GLU B 2 52 ? -30.875 -6.253 4.832 1.00 185.55 ? 52 GLU B CD 1 ATOM 7573 O OE1 . GLU B 2 52 ? -31.119 -7.220 5.584 1.00 189.23 ? 52 GLU B OE1 1 ATOM 7574 O OE2 . GLU B 2 52 ? -30.280 -5.225 5.219 1.00 182.69 ? 52 GLU B OE2 1 ATOM 7575 N N . SER B 2 53 ? -35.052 -4.901 2.661 1.00 185.20 ? 53 SER B N 1 ATOM 7576 C CA . SER B 2 53 ? -35.452 -3.582 2.180 1.00 183.36 ? 53 SER B CA 1 ATOM 7577 C C . SER B 2 53 ? -35.781 -2.580 3.290 1.00 188.39 ? 53 SER B C 1 ATOM 7578 O O . SER B 2 53 ? -35.634 -1.373 3.097 1.00 189.93 ? 53 SER B O 1 ATOM 7579 C CB . SER B 2 53 ? -36.662 -3.724 1.254 1.00 179.87 ? 53 SER B CB 1 ATOM 7580 O OG . SER B 2 53 ? -36.383 -4.599 0.175 1.00 185.26 ? 53 SER B OG 1 ATOM 7581 N N . ILE B 2 54 ? -36.232 -3.074 4.440 1.00 186.97 ? 54 ILE B N 1 ATOM 7582 C CA . ILE B 2 54 ? -36.597 -2.198 5.552 1.00 171.24 ? 54 ILE B CA 1 ATOM 7583 C C . ILE B 2 54 ? -35.386 -1.389 6.027 1.00 150.01 ? 54 ILE B C 1 ATOM 7584 O O . ILE B 2 54 ? -34.299 -1.932 6.232 1.00 146.54 ? 54 ILE B O 1 ATOM 7585 C CB . ILE B 2 54 ? -37.204 -2.999 6.738 1.00 131.86 ? 54 ILE B CB 1 ATOM 7586 C CG1 . ILE B 2 54 ? -37.659 -2.057 7.856 1.00 120.30 ? 54 ILE B CG1 1 ATOM 7587 C CG2 . ILE B 2 54 ? -36.227 -4.041 7.270 1.00 133.05 ? 54 ILE B CG2 1 ATOM 7588 C CD1 . ILE B 2 54 ? -38.921 -1.290 7.532 1.00 117.98 ? 54 ILE B CD1 1 ATOM 7589 N N . GLU B 2 55 ? -35.571 -0.081 6.169 1.00 143.61 ? 55 GLU B N 1 ATOM 7590 C CA . GLU B 2 55 ? -34.482 0.796 6.586 1.00 144.46 ? 55 GLU B CA 1 ATOM 7591 C C . GLU B 2 55 ? -34.689 1.327 7.999 1.00 136.64 ? 55 GLU B C 1 ATOM 7592 O O . GLU B 2 55 ? -35.550 2.174 8.235 1.00 125.38 ? 55 GLU B O 1 ATOM 7593 C CB . GLU B 2 55 ? -34.338 1.967 5.610 1.00 145.87 ? 55 GLU B CB 1 ATOM 7594 C CG . GLU B 2 55 ? -33.724 1.601 4.268 1.00 149.28 ? 55 GLU B CG 1 ATOM 7595 C CD . GLU B 2 55 ? -32.211 1.514 4.322 1.00 146.71 ? 55 GLU B CD 1 ATOM 7596 O OE1 . GLU B 2 55 ? -31.631 1.835 5.381 1.00 136.56 ? 55 GLU B OE1 1 ATOM 7597 O OE2 . GLU B 2 55 ? -31.600 1.129 3.302 1.00 151.43 ? 55 GLU B OE2 1 ATOM 7598 N N . PHE B 2 56 ? -33.892 0.824 8.937 1.00 135.51 ? 56 PHE B N 1 ATOM 7599 C CA . PHE B 2 56 ? -33.906 1.333 10.303 1.00 123.86 ? 56 PHE B CA 1 ATOM 7600 C C . PHE B 2 56 ? -32.506 1.328 10.908 1.00 116.15 ? 56 PHE B C 1 ATOM 7601 O O . PHE B 2 56 ? -32.165 0.430 11.680 1.00 113.28 ? 56 PHE B O 1 ATOM 7602 C CB . PHE B 2 56 ? -34.861 0.518 11.176 1.00 122.94 ? 56 PHE B CB 1 ATOM 7603 C CG . PHE B 2 56 ? -35.014 1.058 12.570 1.00 113.81 ? 56 PHE B CG 1 ATOM 7604 C CD1 . PHE B 2 56 ? -35.573 2.307 12.783 1.00 112.72 ? 56 PHE B CD1 1 ATOM 7605 C CD2 . PHE B 2 56 ? -34.602 0.318 13.665 1.00 118.06 ? 56 PHE B CD2 1 ATOM 7606 C CE1 . PHE B 2 56 ? -35.716 2.809 14.062 1.00 119.97 ? 56 PHE B CE1 1 ATOM 7607 C CE2 . PHE B 2 56 ? -34.743 0.815 14.948 1.00 130.25 ? 56 PHE B CE2 1 ATOM 7608 C CZ . PHE B 2 56 ? -35.301 2.062 15.146 1.00 131.91 ? 56 PHE B CZ 1 ATOM 7609 N N . PRO B 2 57 ? -31.681 2.323 10.546 1.00 111.36 ? 57 PRO B N 1 ATOM 7610 C CA . PRO B 2 57 ? -30.337 2.438 11.120 1.00 104.70 ? 57 PRO B CA 1 ATOM 7611 C C . PRO B 2 57 ? -30.382 2.637 12.632 1.00 101.68 ? 57 PRO B C 1 ATOM 7612 O O . PRO B 2 57 ? -31.111 3.502 13.119 1.00 98.04 ? 57 PRO B O 1 ATOM 7613 C CB . PRO B 2 57 ? -29.758 3.673 10.422 1.00 102.85 ? 57 PRO B CB 1 ATOM 7614 C CG . PRO B 2 57 ? -30.557 3.813 9.168 1.00 107.47 ? 57 PRO B CG 1 ATOM 7615 C CD . PRO B 2 57 ? -31.936 3.359 9.531 1.00 110.25 ? 57 PRO B CD 1 ATOM 7616 N N . VAL B 2 58 ? -29.607 1.842 13.361 1.00 96.79 ? 58 VAL B N 1 ATOM 7617 C CA . VAL B 2 58 ? -29.578 1.923 14.815 1.00 92.28 ? 58 VAL B CA 1 ATOM 7618 C C . VAL B 2 58 ? -28.207 2.386 15.303 1.00 92.85 ? 58 VAL B C 1 ATOM 7619 O O . VAL B 2 58 ? -27.180 1.814 14.937 1.00 101.92 ? 58 VAL B O 1 ATOM 7620 C CB . VAL B 2 58 ? -29.937 0.565 15.461 1.00 95.47 ? 58 VAL B CB 1 ATOM 7621 C CG1 . VAL B 2 58 ? -29.234 -0.580 14.740 1.00 90.52 ? 58 VAL B CG1 1 ATOM 7622 C CG2 . VAL B 2 58 ? -29.608 0.567 16.948 1.00 107.85 ? 58 VAL B CG2 1 ATOM 7623 N N . SER B 2 59 ? -28.198 3.436 16.120 1.00 85.89 ? 59 SER B N 1 ATOM 7624 C CA . SER B 2 59 ? -26.954 3.982 16.646 1.00 93.42 ? 59 SER B CA 1 ATOM 7625 C C . SER B 2 59 ? -26.257 2.980 17.558 1.00 88.65 ? 59 SER B C 1 ATOM 7626 O O . SER B 2 59 ? -26.868 2.428 18.473 1.00 83.42 ? 59 SER B O 1 ATOM 7627 C CB . SER B 2 59 ? -27.213 5.287 17.400 1.00 109.48 ? 59 SER B CB 1 ATOM 7628 O OG . SER B 2 59 ? -27.688 6.295 16.525 1.00 117.15 ? 59 SER B OG 1 ATOM 7629 N N . GLU B 2 60 ? -24.975 2.749 17.298 1.00 95.39 ? 60 GLU B N 1 ATOM 7630 C CA . GLU B 2 60 ? -24.208 1.768 18.052 1.00 91.23 ? 60 GLU B CA 1 ATOM 7631 C C . GLU B 2 60 ? -22.967 2.369 18.698 1.00 93.25 ? 60 GLU B C 1 ATOM 7632 O O . GLU B 2 60 ? -22.347 3.285 18.157 1.00 77.40 ? 60 GLU B O 1 ATOM 7633 C CB . GLU B 2 60 ? -23.789 0.607 17.147 1.00 90.07 ? 60 GLU B CB 1 ATOM 7634 C CG . GLU B 2 60 ? -24.936 -0.174 16.538 1.00 110.80 ? 60 GLU B CG 1 ATOM 7635 C CD . GLU B 2 60 ? -24.454 -1.284 15.624 1.00 129.36 ? 60 GLU B CD 1 ATOM 7636 O OE1 . GLU B 2 60 ? -23.235 -1.343 15.355 1.00 119.46 ? 60 GLU B OE1 1 ATOM 7637 O OE2 . GLU B 2 60 ? -25.290 -2.098 15.177 1.00 146.33 ? 60 GLU B OE2 1 ATOM 7638 N N . ALA B 2 61 ? -22.619 1.847 19.868 1.00 95.79 ? 61 ALA B N 1 ATOM 7639 C CA . ALA B 2 61 ? -21.319 2.097 20.467 1.00 77.04 ? 61 ALA B CA 1 ATOM 7640 C C . ALA B 2 61 ? -20.707 0.753 20.833 1.00 80.77 ? 61 ALA B C 1 ATOM 7641 O O . ALA B 2 61 ? -21.198 0.064 21.726 1.00 90.44 ? 61 ALA B O 1 ATOM 7642 C CB . ALA B 2 61 ? -21.442 2.991 21.688 1.00 75.96 ? 61 ALA B CB 1 ATOM 7643 N N . ARG B 2 62 ? -19.635 0.381 20.144 1.00 79.21 ? 62 ARG B N 1 ATOM 7644 C CA . ARG B 2 62 ? -19.046 -0.939 20.328 1.00 80.98 ? 62 ARG B CA 1 ATOM 7645 C C . ARG B 2 62 ? -17.588 -0.849 20.748 1.00 87.37 ? 62 ARG B C 1 ATOM 7646 O O . ARG B 2 62 ? -16.807 -0.098 20.164 1.00 88.94 ? 62 ARG B O 1 ATOM 7647 C CB . ARG B 2 62 ? -19.169 -1.766 19.047 1.00 83.48 ? 62 ARG B CB 1 ATOM 7648 C CG . ARG B 2 62 ? -20.588 -1.893 18.519 1.00 104.06 ? 62 ARG B CG 1 ATOM 7649 C CD . ARG B 2 62 ? -20.733 -3.115 17.627 1.00 116.08 ? 62 ARG B CD 1 ATOM 7650 N NE . ARG B 2 62 ? -19.706 -3.165 16.591 1.00 117.35 ? 62 ARG B NE 1 ATOM 7651 C CZ . ARG B 2 62 ? -19.545 -4.181 15.749 1.00 125.91 ? 62 ARG B CZ 1 ATOM 7652 N NH1 . ARG B 2 62 ? -20.345 -5.236 15.820 1.00 125.28 ? 62 ARG B NH1 1 ATOM 7653 N NH2 . ARG B 2 62 ? -18.584 -4.143 14.837 1.00 132.55 ? 62 ARG B NH2 1 ATOM 7654 N N . VAL B 2 63 ? -17.227 -1.624 21.764 1.00 81.39 ? 63 VAL B N 1 ATOM 7655 C CA . VAL B 2 63 ? -15.853 -1.650 22.237 1.00 81.59 ? 63 VAL B CA 1 ATOM 7656 C C . VAL B 2 63 ? -14.982 -2.461 21.289 1.00 84.22 ? 63 VAL B C 1 ATOM 7657 O O . VAL B 2 63 ? -15.231 -3.643 21.054 1.00 95.48 ? 63 VAL B O 1 ATOM 7658 C CB . VAL B 2 63 ? -15.752 -2.241 23.654 1.00 81.55 ? 63 VAL B CB 1 ATOM 7659 C CG1 . VAL B 2 63 ? -14.298 -2.425 24.044 1.00 82.18 ? 63 VAL B CG1 1 ATOM 7660 C CG2 . VAL B 2 63 ? -16.471 -1.348 24.653 1.00 80.59 ? 63 VAL B CG2 1 ATOM 7661 N N . LEU B 2 64 ? -13.957 -1.813 20.748 1.00 84.58 ? 64 LEU B N 1 ATOM 7662 C CA . LEU B 2 64 ? -13.018 -2.471 19.851 1.00 87.71 ? 64 LEU B CA 1 ATOM 7663 C C . LEU B 2 64 ? -11.899 -3.122 20.651 1.00 88.82 ? 64 LEU B C 1 ATOM 7664 O O . LEU B 2 64 ? -11.727 -4.338 20.622 1.00 114.83 ? 64 LEU B O 1 ATOM 7665 C CB . LEU B 2 64 ? -12.448 -1.475 18.840 1.00 91.57 ? 64 LEU B CB 1 ATOM 7666 C CG . LEU B 2 64 ? -13.441 -0.972 17.791 1.00 89.24 ? 64 LEU B CG 1 ATOM 7667 C CD1 . LEU B 2 64 ? -12.810 0.093 16.908 1.00 103.41 ? 64 LEU B CD1 1 ATOM 7668 C CD2 . LEU B 2 64 ? -13.954 -2.132 16.952 1.00 90.98 ? 64 LEU B CD2 1 ATOM 7669 N N . GLU B 2 65 ? -11.131 -2.302 21.357 1.00 87.37 ? 65 GLU B N 1 ATOM 7670 C CA . GLU B 2 65 ? -10.039 -2.805 22.175 1.00 88.31 ? 65 GLU B CA 1 ATOM 7671 C C . GLU B 2 65 ? -10.217 -2.440 23.644 1.00 85.77 ? 65 GLU B C 1 ATOM 7672 O O . GLU B 2 65 ? -10.160 -1.266 24.008 1.00 90.18 ? 65 GLU B O 1 ATOM 7673 C CB . GLU B 2 65 ? -8.704 -2.263 21.663 1.00 99.41 ? 65 GLU B CB 1 ATOM 7674 C CG . GLU B 2 65 ? -7.533 -2.515 22.597 1.00 107.77 ? 65 GLU B CG 1 ATOM 7675 C CD . GLU B 2 65 ? -6.234 -1.942 22.066 1.00 114.08 ? 65 GLU B CD 1 ATOM 7676 O OE1 . GLU B 2 65 ? -5.177 -2.184 22.687 1.00 104.22 ? 65 GLU B OE1 1 ATOM 7677 O OE2 . GLU B 2 65 ? -6.269 -1.250 21.027 1.00 124.46 ? 65 GLU B OE2 1 ATOM 7678 N N . ASP B 2 66 ? -10.439 -3.444 24.487 1.00 95.67 ? 66 ASP B N 1 ATOM 7679 C CA . ASP B 2 66 ? -10.426 -3.216 25.926 1.00 94.85 ? 66 ASP B CA 1 ATOM 7680 C C . ASP B 2 66 ? -9.496 -4.193 26.635 1.00 86.62 ? 66 ASP B C 1 ATOM 7681 O O . ASP B 2 66 ? -9.770 -5.388 26.719 1.00 88.32 ? 66 ASP B O 1 ATOM 7682 C CB . ASP B 2 66 ? -11.841 -3.316 26.508 1.00 93.44 ? 66 ASP B CB 1 ATOM 7683 C CG . ASP B 2 66 ? -12.526 -4.625 26.172 1.00 94.58 ? 66 ASP B CG 1 ATOM 7684 O OD1 . ASP B 2 66 ? -12.176 -5.235 25.141 1.00 118.42 ? 66 ASP B OD1 1 ATOM 7685 O OD2 . ASP B 2 66 ? -13.418 -5.043 26.941 1.00 88.03 ? 66 ASP B OD2 1 ATOM 7686 N N . ARG B 2 67 ? -8.391 -3.668 27.148 1.00 87.76 ? 67 ARG B N 1 ATOM 7687 C CA . ARG B 2 67 ? -7.491 -4.443 27.987 1.00 89.23 ? 67 ARG B CA 1 ATOM 7688 C C . ARG B 2 67 ? -7.884 -4.256 29.445 1.00 86.82 ? 67 ARG B C 1 ATOM 7689 O O . ARG B 2 67 ? -8.359 -3.186 29.825 1.00 92.62 ? 67 ARG B O 1 ATOM 7690 C CB . ARG B 2 67 ? -6.039 -4.024 27.755 1.00 99.17 ? 67 ARG B CB 1 ATOM 7691 C CG . ARG B 2 67 ? -5.527 -4.312 26.353 1.00 95.59 ? 67 ARG B CG 1 ATOM 7692 C CD . ARG B 2 67 ? -4.193 -3.630 26.109 1.00 92.82 ? 67 ARG B CD 1 ATOM 7693 N NE . ARG B 2 67 ? -4.319 -2.176 26.134 1.00 90.86 ? 67 ARG B NE 1 ATOM 7694 C CZ . ARG B 2 67 ? -3.291 -1.334 26.100 1.00 110.95 ? 67 ARG B CZ 1 ATOM 7695 N NH1 . ARG B 2 67 ? -2.052 -1.801 26.046 1.00 125.96 ? 67 ARG B NH1 1 ATOM 7696 N NH2 . ARG B 2 67 ? -3.503 -0.026 26.125 1.00 103.37 ? 67 ARG B NH2 1 ATOM 7697 N N . PRO B 2 68 ? -7.697 -5.297 30.268 1.00 91.16 ? 68 PRO B N 1 ATOM 7698 C CA . PRO B 2 68 ? -7.980 -5.148 31.699 1.00 90.53 ? 68 PRO B CA 1 ATOM 7699 C C . PRO B 2 68 ? -7.032 -4.147 32.351 1.00 86.42 ? 68 PRO B C 1 ATOM 7700 O O . PRO B 2 68 ? -5.890 -4.009 31.908 1.00 87.17 ? 68 PRO B O 1 ATOM 7701 C CB . PRO B 2 68 ? -7.760 -6.560 32.250 1.00 93.98 ? 68 PRO B CB 1 ATOM 7702 C CG . PRO B 2 68 ? -6.833 -7.205 31.275 1.00 95.84 ? 68 PRO B CG 1 ATOM 7703 C CD . PRO B 2 68 ? -7.212 -6.647 29.936 1.00 94.07 ? 68 PRO B CD 1 ATOM 7704 N N . LEU B 2 69 ? -7.506 -3.452 33.379 1.00 85.44 ? 69 LEU B N 1 ATOM 7705 C CA . LEU B 2 69 ? -6.681 -2.489 34.097 1.00 85.20 ? 69 LEU B CA 1 ATOM 7706 C C . LEU B 2 69 ? -5.495 -3.185 34.748 1.00 86.90 ? 69 LEU B C 1 ATOM 7707 O O . LEU B 2 69 ? -5.629 -4.286 35.280 1.00 114.68 ? 69 LEU B O 1 ATOM 7708 C CB . LEU B 2 69 ? -7.505 -1.755 35.155 1.00 84.72 ? 69 LEU B CB 1 ATOM 7709 C CG . LEU B 2 69 ? -8.736 -1.000 34.654 1.00 84.64 ? 69 LEU B CG 1 ATOM 7710 C CD1 . LEU B 2 69 ? -9.597 -0.555 35.822 1.00 93.05 ? 69 LEU B CD1 1 ATOM 7711 C CD2 . LEU B 2 69 ? -8.322 0.192 33.806 1.00 85.48 ? 69 LEU B CD2 1 ATOM 7712 N N . SER B 2 70 ? -4.333 -2.544 34.703 1.00 87.28 ? 70 SER B N 1 ATOM 7713 C CA . SER B 2 70 ? -3.136 -3.123 35.296 1.00 89.06 ? 70 SER B CA 1 ATOM 7714 C C . SER B 2 70 ? -3.182 -3.036 36.817 1.00 89.51 ? 70 SER B C 1 ATOM 7715 O O . SER B 2 70 ? -4.128 -2.501 37.395 1.00 95.72 ? 70 SER B O 1 ATOM 7716 C CB . SER B 2 70 ? -1.881 -2.427 34.766 1.00 95.27 ? 70 SER B CB 1 ATOM 7717 O OG . SER B 2 70 ? -1.747 -2.613 33.368 1.00 104.30 ? 70 SER B OG 1 ATOM 7718 N N . ASP B 2 71 ? -2.148 -3.569 37.456 1.00 91.20 ? 71 ASP B N 1 ATOM 7719 C CA . ASP B 2 71 ? -2.033 -3.543 38.908 1.00 93.35 ? 71 ASP B CA 1 ATOM 7720 C C . ASP B 2 71 ? -0.751 -2.827 39.312 1.00 95.96 ? 71 ASP B C 1 ATOM 7721 O O . ASP B 2 71 ? -0.787 -1.798 39.987 1.00 110.78 ? 71 ASP B O 1 ATOM 7722 C CB . ASP B 2 71 ? -2.071 -4.961 39.483 1.00 105.83 ? 71 ASP B CB 1 ATOM 7723 C CG . ASP B 2 71 ? -1.428 -5.983 38.565 1.00 132.15 ? 71 ASP B CG 1 ATOM 7724 O OD1 . ASP B 2 71 ? -1.474 -5.791 37.332 1.00 138.67 ? 71 ASP B OD1 1 ATOM 7725 O OD2 . ASP B 2 71 ? -0.882 -6.983 39.077 1.00 146.04 ? 71 ASP B OD2 1 ATOM 7726 N N . LYS B 2 72 ? 0.381 -3.382 38.895 1.00 99.19 ? 72 LYS B N 1 ATOM 7727 C CA . LYS B 2 72 ? 1.683 -2.794 39.184 1.00 123.29 ? 72 LYS B CA 1 ATOM 7728 C C . LYS B 2 72 ? 2.347 -2.309 37.897 1.00 131.09 ? 72 LYS B C 1 ATOM 7729 O O . LYS B 2 72 ? 2.034 -2.787 36.807 1.00 134.08 ? 72 LYS B O 1 ATOM 7730 C CB . LYS B 2 72 ? 2.584 -3.799 39.909 1.00 125.07 ? 72 LYS B CB 1 ATOM 7731 C CG . LYS B 2 72 ? 2.497 -3.740 41.432 1.00 123.27 ? 72 LYS B CG 1 ATOM 7732 C CD . LYS B 2 72 ? 1.098 -4.062 41.939 1.00 120.26 ? 72 LYS B CD 1 ATOM 7733 C CE . LYS B 2 72 ? 1.000 -3.891 43.447 1.00 114.77 ? 72 LYS B CE 1 ATOM 7734 N NZ . LYS B 2 72 ? -0.374 -4.169 43.950 1.00 102.00 ? 72 LYS B NZ 1 ATOM 7735 N N . GLY B 2 73 ? 3.261 -1.353 38.031 1.00 124.85 ? 73 GLY B N 1 ATOM 7736 C CA . GLY B 2 73 ? 3.856 -0.691 36.883 1.00 134.45 ? 73 GLY B CA 1 ATOM 7737 C C . GLY B 2 73 ? 5.088 -1.368 36.313 1.00 143.03 ? 73 GLY B C 1 ATOM 7738 O O . GLY B 2 73 ? 5.900 -0.727 35.645 1.00 149.43 ? 73 GLY B O 1 ATOM 7739 N N . SER B 2 74 ? 5.233 -2.664 36.573 1.00 155.77 ? 74 SER B N 1 ATOM 7740 C CA . SER B 2 74 ? 6.372 -3.423 36.064 1.00 153.81 ? 74 SER B CA 1 ATOM 7741 C C . SER B 2 74 ? 6.254 -3.667 34.560 1.00 155.43 ? 74 SER B C 1 ATOM 7742 O O . SER B 2 74 ? 5.310 -3.207 33.918 1.00 152.39 ? 74 SER B O 1 ATOM 7743 C CB . SER B 2 74 ? 6.502 -4.756 36.804 1.00 145.45 ? 74 SER B CB 1 ATOM 7744 O OG . SER B 2 74 ? 5.363 -5.571 36.597 1.00 144.24 ? 74 SER B OG 1 ATOM 7745 N N . GLY B 2 75 ? 7.217 -4.396 34.004 1.00 157.00 ? 75 GLY B N 1 ATOM 7746 C CA . GLY B 2 75 ? 7.277 -4.611 32.568 1.00 155.21 ? 75 GLY B CA 1 ATOM 7747 C C . GLY B 2 75 ? 6.712 -5.934 32.087 1.00 152.01 ? 75 GLY B C 1 ATOM 7748 O O . GLY B 2 75 ? 6.673 -6.194 30.884 1.00 155.50 ? 75 GLY B O 1 ATOM 7749 N N . ASP B 2 76 ? 6.275 -6.775 33.019 1.00 134.12 ? 76 ASP B N 1 ATOM 7750 C CA . ASP B 2 76 ? 5.712 -8.076 32.667 1.00 139.66 ? 76 ASP B CA 1 ATOM 7751 C C . ASP B 2 76 ? 4.197 -8.012 32.485 1.00 144.94 ? 76 ASP B C 1 ATOM 7752 O O . ASP B 2 76 ? 3.547 -9.033 32.259 1.00 136.15 ? 76 ASP B O 1 ATOM 7753 C CB . ASP B 2 76 ? 6.071 -9.122 33.724 1.00 147.31 ? 76 ASP B CB 1 ATOM 7754 C CG . ASP B 2 76 ? 7.500 -9.612 33.595 1.00 148.18 ? 76 ASP B CG 1 ATOM 7755 O OD1 . ASP B 2 76 ? 7.754 -10.797 33.897 1.00 143.85 ? 76 ASP B OD1 1 ATOM 7756 O OD2 . ASP B 2 76 ? 8.370 -8.813 33.187 1.00 145.56 ? 76 ASP B OD2 1 ATOM 7757 N N . SER B 2 77 ? 3.643 -6.808 32.581 1.00 158.65 ? 77 SER B N 1 ATOM 7758 C CA . SER B 2 77 ? 2.211 -6.599 32.387 1.00 156.28 ? 77 SER B CA 1 ATOM 7759 C C . SER B 2 77 ? 1.854 -6.695 30.908 1.00 158.65 ? 77 SER B C 1 ATOM 7760 O O . SER B 2 77 ? 2.695 -7.066 30.089 1.00 156.03 ? 77 SER B O 1 ATOM 7761 C CB . SER B 2 77 ? 1.783 -5.243 32.950 1.00 141.24 ? 77 SER B CB 1 ATOM 7762 O OG . SER B 2 77 ? 2.498 -4.187 32.332 1.00 137.23 ? 77 SER B OG 1 ATOM 7763 N N . SER B 2 78 ? 0.602 -6.384 30.575 1.00 161.28 ? 78 SER B N 1 ATOM 7764 C CA . SER B 2 78 ? 0.154 -6.401 29.185 1.00 161.40 ? 78 SER B CA 1 ATOM 7765 C C . SER B 2 78 ? 1.063 -5.510 28.348 1.00 155.58 ? 78 SER B C 1 ATOM 7766 O O . SER B 2 78 ? 1.898 -5.996 27.585 1.00 164.03 ? 78 SER B O 1 ATOM 7767 C CB . SER B 2 78 ? -1.296 -5.926 29.089 1.00 160.30 ? 78 SER B CB 1 ATOM 7768 O OG . SER B 2 78 ? -2.123 -6.624 30.004 1.00 163.19 ? 78 SER B OG 1 ATOM 7769 N N . GLN B 2 79 ? 0.889 -4.202 28.495 1.00 136.76 ? 79 GLN B N 1 ATOM 7770 C CA . GLN B 2 79 ? 1.972 -3.255 28.289 1.00 135.25 ? 79 GLN B CA 1 ATOM 7771 C C . GLN B 2 79 ? 2.022 -2.440 29.570 1.00 134.72 ? 79 GLN B C 1 ATOM 7772 O O . GLN B 2 79 ? 2.860 -2.663 30.443 1.00 150.72 ? 79 GLN B O 1 ATOM 7773 C CB . GLN B 2 79 ? 1.723 -2.362 27.071 1.00 136.07 ? 79 GLN B CB 1 ATOM 7774 C CG . GLN B 2 79 ? 1.037 -3.055 25.901 1.00 141.40 ? 79 GLN B CG 1 ATOM 7775 C CD . GLN B 2 79 ? 1.927 -4.065 25.205 1.00 158.50 ? 79 GLN B CD 1 ATOM 7776 O OE1 . GLN B 2 79 ? 3.145 -4.069 25.386 1.00 170.02 ? 79 GLN B OE1 1 ATOM 7777 N NE2 . GLN B 2 79 ? 1.321 -4.929 24.399 1.00 158.61 ? 79 GLN B NE2 1 ATOM 7778 N N . VAL B 2 80 ? 1.094 -1.493 29.650 1.00 113.52 ? 80 VAL B N 1 ATOM 7779 C CA . VAL B 2 80 ? 0.555 -0.960 30.893 1.00 100.05 ? 80 VAL B CA 1 ATOM 7780 C C . VAL B 2 80 ? -0.840 -0.457 30.526 1.00 91.86 ? 80 VAL B C 1 ATOM 7781 O O . VAL B 2 80 ? -1.014 0.118 29.451 1.00 101.17 ? 80 VAL B O 1 ATOM 7782 C CB . VAL B 2 80 ? 1.435 0.166 31.490 1.00 103.95 ? 80 VAL B CB 1 ATOM 7783 C CG1 . VAL B 2 80 ? 0.582 1.296 32.053 1.00 116.79 ? 80 VAL B CG1 1 ATOM 7784 C CG2 . VAL B 2 80 ? 2.362 -0.391 32.563 1.00 100.22 ? 80 VAL B CG2 1 ATOM 7785 N N . THR B 2 81 ? -1.835 -0.662 31.383 1.00 80.40 ? 81 THR B N 1 ATOM 7786 C CA . THR B 2 81 ? -3.159 -0.125 31.082 1.00 72.19 ? 81 THR B CA 1 ATOM 7787 C C . THR B 2 81 ? -3.789 0.577 32.278 1.00 69.44 ? 81 THR B C 1 ATOM 7788 O O . THR B 2 81 ? -4.139 -0.061 33.271 1.00 86.86 ? 81 THR B O 1 ATOM 7789 C CB . THR B 2 81 ? -4.115 -1.232 30.600 1.00 75.83 ? 81 THR B CB 1 ATOM 7790 O OG1 . THR B 2 81 ? -3.550 -1.891 29.459 1.00 88.14 ? 81 THR B OG1 1 ATOM 7791 C CG2 . THR B 2 81 ? -5.465 -0.643 30.222 1.00 75.90 ? 81 THR B CG2 1 ATOM 7792 N N . GLN B 2 82 ? -3.930 1.894 32.175 1.00 66.62 ? 82 GLN B N 1 ATOM 7793 C CA . GLN B 2 82 ? -4.633 2.670 33.188 1.00 65.00 ? 82 GLN B CA 1 ATOM 7794 C C . GLN B 2 82 ? -6.062 3.041 32.780 1.00 63.47 ? 82 GLN B C 1 ATOM 7795 O O . GLN B 2 82 ? -6.796 3.634 33.570 1.00 62.40 ? 82 GLN B O 1 ATOM 7796 C CB . GLN B 2 82 ? -3.834 3.931 33.523 1.00 78.03 ? 82 GLN B CB 1 ATOM 7797 C CG . GLN B 2 82 ? -2.517 3.641 34.232 1.00 78.76 ? 82 GLN B CG 1 ATOM 7798 C CD . GLN B 2 82 ? -1.677 4.884 34.450 1.00 85.92 ? 82 GLN B CD 1 ATOM 7799 O OE1 . GLN B 2 82 ? -1.297 5.201 35.578 1.00 97.26 ? 82 GLN B OE1 1 ATOM 7800 N NE2 . GLN B 2 82 ? -1.376 5.592 33.368 1.00 86.22 ? 82 GLN B NE2 1 ATOM 7801 N N . VAL B 2 83 ? -6.455 2.700 31.554 1.00 63.62 ? 83 VAL B N 1 ATOM 7802 C CA . VAL B 2 83 ? -7.782 3.070 31.057 1.00 67.62 ? 83 VAL B CA 1 ATOM 7803 C C . VAL B 2 83 ? -8.498 1.936 30.316 1.00 64.38 ? 83 VAL B C 1 ATOM 7804 O O . VAL B 2 83 ? -8.032 1.466 29.279 1.00 71.00 ? 83 VAL B O 1 ATOM 7805 C CB . VAL B 2 83 ? -7.705 4.292 30.113 1.00 60.02 ? 83 VAL B CB 1 ATOM 7806 C CG1 . VAL B 2 83 ? -9.055 4.548 29.465 1.00 59.22 ? 83 VAL B CG1 1 ATOM 7807 C CG2 . VAL B 2 83 ? -7.231 5.528 30.864 1.00 58.06 ? 83 VAL B CG2 1 ATOM 7808 N N . SER B 2 84 ? -9.631 1.505 30.863 1.00 65.02 ? 84 SER B N 1 ATOM 7809 C CA . SER B 2 84 ? -10.507 0.524 30.220 1.00 69.44 ? 84 SER B CA 1 ATOM 7810 C C . SER B 2 84 ? -11.857 1.135 29.846 1.00 74.17 ? 84 SER B C 1 ATOM 7811 O O . SER B 2 84 ? -12.544 1.685 30.707 1.00 81.86 ? 84 SER B O 1 ATOM 7812 C CB . SER B 2 84 ? -10.719 -0.688 31.129 1.00 69.02 ? 84 SER B CB 1 ATOM 7813 O OG . SER B 2 84 ? -9.547 -1.479 31.203 1.00 78.28 ? 84 SER B OG 1 ATOM 7814 N N . PRO B 2 85 ? -12.248 1.049 28.564 1.00 65.41 ? 85 PRO B N 1 ATOM 7815 C CA . PRO B 2 85 ? -11.557 0.451 27.416 1.00 69.26 ? 85 PRO B CA 1 ATOM 7816 C C . PRO B 2 85 ? -10.573 1.401 26.738 1.00 80.09 ? 85 PRO B C 1 ATOM 7817 O O . PRO B 2 85 ? -10.290 2.479 27.259 1.00 89.09 ? 85 PRO B O 1 ATOM 7818 C CB . PRO B 2 85 ? -12.705 0.105 26.469 1.00 67.73 ? 85 PRO B CB 1 ATOM 7819 C CG . PRO B 2 85 ? -13.719 1.145 26.744 1.00 65.62 ? 85 PRO B CG 1 ATOM 7820 C CD . PRO B 2 85 ? -13.623 1.452 28.217 1.00 64.72 ? 85 PRO B CD 1 ATOM 7821 N N . GLN B 2 86 ? -10.057 0.989 25.584 1.00 66.60 ? 86 GLN B N 1 ATOM 7822 C CA . GLN B 2 86 ? -9.118 1.802 24.818 1.00 65.53 ? 86 GLN B CA 1 ATOM 7823 C C . GLN B 2 86 ? -9.755 2.351 23.542 1.00 71.10 ? 86 GLN B C 1 ATOM 7824 O O . GLN B 2 86 ? -9.848 3.563 23.360 1.00 89.41 ? 86 GLN B O 1 ATOM 7825 C CB . GLN B 2 86 ? -7.861 0.999 24.477 1.00 67.76 ? 86 GLN B CB 1 ATOM 7826 C CG . GLN B 2 86 ? -6.997 0.654 25.682 1.00 68.24 ? 86 GLN B CG 1 ATOM 7827 C CD . GLN B 2 86 ? -7.551 -0.502 26.492 1.00 73.67 ? 86 GLN B CD 1 ATOM 7828 O OE1 . GLN B 2 86 ? -7.592 -1.639 26.023 1.00 84.72 ? 86 GLN B OE1 1 ATOM 7829 N NE2 . GLN B 2 86 ? -7.984 -0.216 27.714 1.00 68.98 ? 86 GLN B NE2 1 ATOM 7830 N N . ARG B 2 87 ? -10.169 1.461 22.645 1.00 67.34 ? 87 ARG B N 1 ATOM 7831 C CA . ARG B 2 87 ? -10.798 1.887 21.398 1.00 67.36 ? 87 ARG B CA 1 ATOM 7832 C C . ARG B 2 87 ? -12.297 1.591 21.380 1.00 67.83 ? 87 ARG B C 1 ATOM 7833 O O . ARG B 2 87 ? -12.726 0.492 21.730 1.00 79.39 ? 87 ARG B O 1 ATOM 7834 C CB . ARG B 2 87 ? -10.123 1.216 20.201 1.00 81.53 ? 87 ARG B CB 1 ATOM 7835 C CG . ARG B 2 87 ? -8.620 1.420 20.140 1.00 94.21 ? 87 ARG B CG 1 ATOM 7836 C CD . ARG B 2 87 ? -8.081 1.119 18.753 1.00 101.99 ? 87 ARG B CD 1 ATOM 7837 N NE . ARG B 2 87 ? -8.651 2.014 17.751 1.00 109.73 ? 87 ARG B NE 1 ATOM 7838 C CZ . ARG B 2 87 ? -8.195 3.237 17.497 1.00 103.14 ? 87 ARG B CZ 1 ATOM 7839 N NH1 . ARG B 2 87 ? -7.159 3.714 18.173 1.00 81.46 ? 87 ARG B NH1 1 ATOM 7840 N NH2 . ARG B 2 87 ? -8.777 3.983 16.568 1.00 110.96 ? 87 ARG B NH2 1 ATOM 7841 N N . ILE B 2 88 ? -13.087 2.579 20.969 1.00 66.23 ? 88 ILE B N 1 ATOM 7842 C CA . ILE B 2 88 ? -14.532 2.412 20.844 1.00 74.32 ? 88 ILE B CA 1 ATOM 7843 C C . ILE B 2 88 ? -15.033 2.913 19.492 1.00 69.12 ? 88 ILE B C 1 ATOM 7844 O O . ILE B 2 88 ? -14.741 4.039 19.092 1.00 65.48 ? 88 ILE B O 1 ATOM 7845 C CB . ILE B 2 88 ? -15.297 3.158 21.960 1.00 74.66 ? 88 ILE B CB 1 ATOM 7846 C CG1 . ILE B 2 88 ? -14.945 2.588 23.335 1.00 77.34 ? 88 ILE B CG1 1 ATOM 7847 C CG2 . ILE B 2 88 ? -16.800 3.074 21.729 1.00 65.34 ? 88 ILE B CG2 1 ATOM 7848 C CD1 . ILE B 2 88 ? -15.691 3.254 24.473 1.00 75.66 ? 88 ILE B CD1 1 ATOM 7849 N N . ALA B 2 89 ? -15.787 2.072 18.793 1.00 69.72 ? 89 ALA B N 1 ATOM 7850 C CA . ALA B 2 89 ? -16.419 2.475 17.544 1.00 70.59 ? 89 ALA B CA 1 ATOM 7851 C C . ALA B 2 89 ? -17.796 3.067 17.824 1.00 70.71 ? 89 ALA B C 1 ATOM 7852 O O . ALA B 2 89 ? -18.612 2.460 18.517 1.00 70.19 ? 89 ALA B O 1 ATOM 7853 C CB . ALA B 2 89 ? -16.527 1.295 16.593 1.00 85.22 ? 89 ALA B CB 1 ATOM 7854 N N . LEU B 2 90 ? -18.050 4.256 17.286 1.00 70.39 ? 90 LEU B N 1 ATOM 7855 C CA . LEU B 2 90 ? -19.317 4.937 17.519 1.00 70.44 ? 90 LEU B CA 1 ATOM 7856 C C . LEU B 2 90 ? -20.054 5.204 16.211 1.00 71.66 ? 90 LEU B C 1 ATOM 7857 O O . LEU B 2 90 ? -19.565 5.932 15.348 1.00 79.18 ? 90 LEU B O 1 ATOM 7858 C CB . LEU B 2 90 ? -19.089 6.253 18.267 1.00 69.17 ? 90 LEU B CB 1 ATOM 7859 C CG . LEU B 2 90 ? -19.981 6.542 19.479 1.00 69.85 ? 90 LEU B CG 1 ATOM 7860 C CD1 . LEU B 2 90 ? -19.750 7.959 19.987 1.00 65.84 ? 90 LEU B CD1 1 ATOM 7861 C CD2 . LEU B 2 90 ? -21.452 6.316 19.157 1.00 75.38 ? 90 LEU B CD2 1 ATOM 7862 N N . ARG B 2 91 ? -21.232 4.607 16.072 1.00 74.75 ? 91 ARG B N 1 ATOM 7863 C CA . ARG B 2 91 ? -22.087 4.862 14.921 1.00 80.81 ? 91 ARG B CA 1 ATOM 7864 C C . ARG B 2 91 ? -23.311 5.650 15.363 1.00 80.44 ? 91 ARG B C 1 ATOM 7865 O O . ARG B 2 91 ? -23.967 5.293 16.341 1.00 78.95 ? 91 ARG B O 1 ATOM 7866 C CB . ARG B 2 91 ? -22.502 3.554 14.247 1.00 100.88 ? 91 ARG B CB 1 ATOM 7867 C CG . ARG B 2 91 ? -21.334 2.733 13.730 1.00 105.11 ? 91 ARG B CG 1 ATOM 7868 C CD . ARG B 2 91 ? -21.812 1.484 13.011 1.00 103.15 ? 91 ARG B CD 1 ATOM 7869 N NE . ARG B 2 91 ? -22.600 1.804 11.825 1.00 111.05 ? 91 ARG B NE 1 ATOM 7870 C CZ . ARG B 2 91 ? -23.134 0.894 11.017 1.00 127.19 ? 91 ARG B CZ 1 ATOM 7871 N NH1 . ARG B 2 91 ? -22.965 -0.397 11.268 1.00 126.84 ? 91 ARG B NH1 1 ATOM 7872 N NH2 . ARG B 2 91 ? -23.837 1.273 9.958 1.00 138.61 ? 91 ARG B NH2 1 ATOM 7873 N N . LEU B 2 92 ? -23.612 6.727 14.647 1.00 81.78 ? 92 LEU B N 1 ATOM 7874 C CA . LEU B 2 92 ? -24.698 7.612 15.044 1.00 80.42 ? 92 LEU B CA 1 ATOM 7875 C C . LEU B 2 92 ? -25.598 8.009 13.881 1.00 84.58 ? 92 LEU B C 1 ATOM 7876 O O . LEU B 2 92 ? -25.124 8.453 12.836 1.00 85.00 ? 92 LEU B O 1 ATOM 7877 C CB . LEU B 2 92 ? -24.134 8.870 15.709 1.00 76.91 ? 92 LEU B CB 1 ATOM 7878 C CG . LEU B 2 92 ? -23.568 8.686 17.118 1.00 76.15 ? 92 LEU B CG 1 ATOM 7879 C CD1 . LEU B 2 92 ? -22.845 9.940 17.582 1.00 72.14 ? 92 LEU B CD1 1 ATOM 7880 C CD2 . LEU B 2 92 ? -24.681 8.317 18.087 1.00 92.15 ? 92 LEU B CD2 1 ATOM 7881 N N . ARG B 2 93 ? -26.901 7.834 14.075 1.00 89.70 ? 93 ARG B N 1 ATOM 7882 C CA . ARG B 2 93 ? -27.892 8.365 13.152 1.00 95.74 ? 93 ARG B CA 1 ATOM 7883 C C . ARG B 2 93 ? -28.215 9.790 13.597 1.00 115.72 ? 93 ARG B C 1 ATOM 7884 O O . ARG B 2 93 ? -28.048 10.118 14.772 1.00 126.63 ? 93 ARG B O 1 ATOM 7885 C CB . ARG B 2 93 ? -29.145 7.481 13.123 1.00 93.36 ? 93 ARG B CB 1 ATOM 7886 C CG . ARG B 2 93 ? -29.966 7.504 14.397 1.00 100.17 ? 93 ARG B CG 1 ATOM 7887 C CD . ARG B 2 93 ? -31.215 6.651 14.258 1.00 104.51 ? 93 ARG B CD 1 ATOM 7888 N NE . ARG B 2 93 ? -32.063 7.101 13.157 1.00 100.19 ? 93 ARG B NE 1 ATOM 7889 C CZ . ARG B 2 93 ? -33.171 6.480 12.767 1.00 106.86 ? 93 ARG B CZ 1 ATOM 7890 N NH1 . ARG B 2 93 ? -33.568 5.377 13.388 1.00 104.75 ? 93 ARG B NH1 1 ATOM 7891 N NH2 . ARG B 2 93 ? -33.882 6.959 11.755 1.00 115.88 ? 93 ARG B NH2 1 ATOM 7892 N N . PRO B 2 94 ? -28.660 10.647 12.660 1.00 120.46 ? 94 PRO B N 1 ATOM 7893 C CA . PRO B 2 94 ? -28.889 12.070 12.944 1.00 117.39 ? 94 PRO B CA 1 ATOM 7894 C C . PRO B 2 94 ? -29.801 12.332 14.142 1.00 108.79 ? 94 PRO B C 1 ATOM 7895 O O . PRO B 2 94 ? -30.833 11.675 14.290 1.00 113.57 ? 94 PRO B O 1 ATOM 7896 C CB . PRO B 2 94 ? -29.537 12.585 11.651 1.00 120.83 ? 94 PRO B CB 1 ATOM 7897 C CG . PRO B 2 94 ? -29.985 11.357 10.916 1.00 121.63 ? 94 PRO B CG 1 ATOM 7898 C CD . PRO B 2 94 ? -28.986 10.318 11.264 1.00 120.69 ? 94 PRO B CD 1 ATOM 7899 N N . ASP B 2 95 ? -29.400 13.286 14.980 1.00 95.27 ? 95 ASP B N 1 ATOM 7900 C CA . ASP B 2 95 ? -30.149 13.679 16.173 1.00 102.69 ? 95 ASP B CA 1 ATOM 7901 C C . ASP B 2 95 ? -30.406 12.505 17.112 1.00 107.17 ? 95 ASP B C 1 ATOM 7902 O O . ASP B 2 95 ? -31.506 12.350 17.642 1.00 119.81 ? 95 ASP B O 1 ATOM 7903 C CB . ASP B 2 95 ? -31.476 14.336 15.782 1.00 116.64 ? 95 ASP B CB 1 ATOM 7904 C CG . ASP B 2 95 ? -31.282 15.661 15.071 1.00 122.88 ? 95 ASP B CG 1 ATOM 7905 O OD1 . ASP B 2 95 ? -32.034 15.941 14.114 1.00 128.22 ? 95 ASP B OD1 1 ATOM 7906 O OD2 . ASP B 2 95 ? -30.378 16.424 15.472 1.00 114.21 ? 95 ASP B OD2 1 ATOM 7907 N N . ASP B 2 96 ? -29.382 11.682 17.317 1.00 96.77 ? 96 ASP B N 1 ATOM 7908 C CA . ASP B 2 96 ? -29.482 10.552 18.233 1.00 96.66 ? 96 ASP B CA 1 ATOM 7909 C C . ASP B 2 96 ? -28.245 10.471 19.118 1.00 94.04 ? 96 ASP B C 1 ATOM 7910 O O . ASP B 2 96 ? -27.200 11.034 18.791 1.00 98.96 ? 96 ASP B O 1 ATOM 7911 C CB . ASP B 2 96 ? -29.670 9.245 17.462 1.00 98.71 ? 96 ASP B CB 1 ATOM 7912 C CG . ASP B 2 96 ? -30.055 8.086 18.361 1.00 104.38 ? 96 ASP B CG 1 ATOM 7913 O OD1 . ASP B 2 96 ? -30.471 8.338 19.512 1.00 100.99 ? 96 ASP B OD1 1 ATOM 7914 O OD2 . ASP B 2 96 ? -29.954 6.924 17.915 1.00 116.27 ? 96 ASP B OD2 1 ATOM 7915 N N . SER B 2 97 ? -28.368 9.766 20.237 1.00 82.11 ? 97 SER B N 1 ATOM 7916 C CA . SER B 2 97 ? -27.277 9.666 21.194 1.00 76.04 ? 97 SER B CA 1 ATOM 7917 C C . SER B 2 97 ? -27.166 8.280 21.810 1.00 74.47 ? 97 SER B C 1 ATOM 7918 O O . SER B 2 97 ? -28.170 7.667 22.171 1.00 96.03 ? 97 SER B O 1 ATOM 7919 C CB . SER B 2 97 ? -27.454 10.699 22.305 1.00 93.55 ? 97 SER B CB 1 ATOM 7920 O OG . SER B 2 97 ? -26.373 10.647 23.219 1.00 113.40 ? 97 SER B OG 1 ATOM 7921 N N . LYS B 2 98 ? -25.936 7.793 21.930 1.00 73.86 ? 98 LYS B N 1 ATOM 7922 C CA . LYS B 2 98 ? -25.672 6.565 22.666 1.00 87.44 ? 98 LYS B CA 1 ATOM 7923 C C . LYS B 2 98 ? -24.574 6.827 23.690 1.00 91.83 ? 98 LYS B C 1 ATOM 7924 O O . LYS B 2 98 ? -23.697 7.662 23.470 1.00 77.34 ? 98 LYS B O 1 ATOM 7925 C CB . LYS B 2 98 ? -25.280 5.429 21.721 1.00 79.75 ? 98 LYS B CB 1 ATOM 7926 C CG . LYS B 2 98 ? -25.326 4.056 22.369 1.00 79.22 ? 98 LYS B CG 1 ATOM 7927 C CD . LYS B 2 98 ? -25.322 2.950 21.332 1.00 100.54 ? 98 LYS B CD 1 ATOM 7928 C CE . LYS B 2 98 ? -25.380 1.580 21.989 1.00 125.31 ? 98 LYS B CE 1 ATOM 7929 N NZ . LYS B 2 98 ? -25.394 0.480 20.985 1.00 131.65 ? 98 LYS B NZ 1 ATOM 7930 N N . ASN B 2 99 ? -24.629 6.118 24.812 1.00 99.86 ? 99 ASN B N 1 ATOM 7931 C CA . ASN B 2 99 ? -23.710 6.371 25.911 1.00 92.60 ? 99 ASN B CA 1 ATOM 7932 C C . ASN B 2 99 ? -22.780 5.199 26.199 1.00 75.43 ? 99 ASN B C 1 ATOM 7933 O O . ASN B 2 99 ? -23.112 4.046 25.925 1.00 75.60 ? 99 ASN B O 1 ATOM 7934 C CB . ASN B 2 99 ? -24.494 6.728 27.174 1.00 104.17 ? 99 ASN B CB 1 ATOM 7935 C CG . ASN B 2 99 ? -25.522 5.676 27.535 1.00 117.62 ? 99 ASN B CG 1 ATOM 7936 O OD1 . ASN B 2 99 ? -26.086 5.019 26.660 1.00 100.53 ? 99 ASN B OD1 1 ATOM 7937 N ND2 . ASN B 2 99 ? -25.771 5.511 28.828 1.00 151.40 ? 99 ASN B ND2 1 ATOM 7938 N N . PHE B 2 100 ? -21.613 5.507 26.755 1.00 68.40 ? 100 PHE B N 1 ATOM 7939 C CA . PHE B 2 100 ? -20.642 4.487 27.127 1.00 66.39 ? 100 PHE B CA 1 ATOM 7940 C C . PHE B 2 100 ? -19.972 4.833 28.454 1.00 67.02 ? 100 PHE B C 1 ATOM 7941 O O . PHE B 2 100 ? -20.270 5.862 29.063 1.00 60.43 ? 100 PHE B O 1 ATOM 7942 C CB . PHE B 2 100 ? -19.590 4.315 26.027 1.00 67.27 ? 100 PHE B CB 1 ATOM 7943 C CG . PHE B 2 100 ? -18.944 5.602 25.594 1.00 67.26 ? 100 PHE B CG 1 ATOM 7944 C CD1 . PHE B 2 100 ? -17.819 6.083 26.243 1.00 83.26 ? 100 PHE B CD1 1 ATOM 7945 C CD2 . PHE B 2 100 ? -19.458 6.326 24.530 1.00 69.71 ? 100 PHE B CD2 1 ATOM 7946 C CE1 . PHE B 2 100 ? -17.223 7.265 25.844 1.00 82.73 ? 100 PHE B CE1 1 ATOM 7947 C CE2 . PHE B 2 100 ? -18.867 7.509 24.127 1.00 72.04 ? 100 PHE B CE2 1 ATOM 7948 C CZ . PHE B 2 100 ? -17.748 7.979 24.784 1.00 73.63 ? 100 PHE B CZ 1 ATOM 7949 N N . SER B 2 101 ? -19.065 3.969 28.897 1.00 82.59 ? 101 SER B N 1 ATOM 7950 C CA . SER B 2 101 ? -18.396 4.147 30.181 1.00 80.27 ? 101 SER B CA 1 ATOM 7951 C C . SER B 2 101 ? -16.887 3.962 30.059 1.00 73.43 ? 101 SER B C 1 ATOM 7952 O O . SER B 2 101 ? -16.407 3.297 29.142 1.00 94.37 ? 101 SER B O 1 ATOM 7953 C CB . SER B 2 101 ? -18.960 3.169 31.213 1.00 94.91 ? 101 SER B CB 1 ATOM 7954 O OG . SER B 2 101 ? -18.255 3.255 32.439 1.00 101.66 ? 101 SER B OG 1 ATOM 7955 N N . ILE B 2 102 ? -16.145 4.558 30.986 1.00 60.88 ? 102 ILE B N 1 ATOM 7956 C CA . ILE B 2 102 ? -14.691 4.441 30.994 1.00 61.98 ? 102 ILE B CA 1 ATOM 7957 C C . ILE B 2 102 ? -14.139 4.366 32.419 1.00 62.23 ? 102 ILE B C 1 ATOM 7958 O O . ILE B 2 102 ? -14.541 5.134 33.293 1.00 60.42 ? 102 ILE B O 1 ATOM 7959 C CB . ILE B 2 102 ? -14.037 5.623 30.240 1.00 58.61 ? 102 ILE B CB 1 ATOM 7960 C CG1 . ILE B 2 102 ? -12.520 5.633 30.438 1.00 69.75 ? 102 ILE B CG1 1 ATOM 7961 C CG2 . ILE B 2 102 ? -14.641 6.945 30.684 1.00 55.83 ? 102 ILE B CG2 1 ATOM 7962 C CD1 . ILE B 2 102 ? -11.838 6.840 29.830 1.00 84.42 ? 102 ILE B CD1 1 ATOM 7963 N N . GLN B 2 103 ? -13.221 3.430 32.648 1.00 61.66 ? 103 GLN B N 1 ATOM 7964 C CA . GLN B 2 103 ? -12.553 3.306 33.939 1.00 67.52 ? 103 GLN B CA 1 ATOM 7965 C C . GLN B 2 103 ? -11.131 3.847 33.871 1.00 70.55 ? 103 GLN B C 1 ATOM 7966 O O . GLN B 2 103 ? -10.415 3.616 32.897 1.00 81.88 ? 103 GLN B O 1 ATOM 7967 C CB . GLN B 2 103 ? -12.531 1.847 34.405 1.00 71.12 ? 103 GLN B CB 1 ATOM 7968 C CG . GLN B 2 103 ? -13.742 1.422 35.224 1.00 80.98 ? 103 GLN B CG 1 ATOM 7969 C CD . GLN B 2 103 ? -14.991 1.241 34.385 1.00 99.14 ? 103 GLN B CD 1 ATOM 7970 O OE1 . GLN B 2 103 ? -14.939 1.271 33.155 1.00 113.48 ? 103 GLN B OE1 1 ATOM 7971 N NE2 . GLN B 2 103 ? -16.125 1.047 35.048 1.00 97.97 ? 103 GLN B NE2 1 ATOM 7972 N N . VAL B 2 104 ? -10.730 4.574 34.908 1.00 68.84 ? 104 VAL B N 1 ATOM 7973 C CA . VAL B 2 104 ? -9.377 5.112 35.000 1.00 72.43 ? 104 VAL B CA 1 ATOM 7974 C C . VAL B 2 104 ? -8.766 4.733 36.344 1.00 61.64 ? 104 VAL B C 1 ATOM 7975 O O . VAL B 2 104 ? -9.416 4.852 37.381 1.00 62.20 ? 104 VAL B O 1 ATOM 7976 C CB . VAL B 2 104 ? -9.356 6.646 34.838 1.00 77.41 ? 104 VAL B CB 1 ATOM 7977 C CG1 . VAL B 2 104 ? -7.924 7.163 34.833 1.00 77.07 ? 104 VAL B CG1 1 ATOM 7978 C CG2 . VAL B 2 104 ? -10.076 7.059 33.563 1.00 87.32 ? 104 VAL B CG2 1 ATOM 7979 N N . ARG B 2 105 ? -7.519 4.272 36.325 1.00 62.67 ? 105 ARG B N 1 ATOM 7980 C CA . ARG B 2 105 ? -6.870 3.819 37.549 1.00 68.54 ? 105 ARG B CA 1 ATOM 7981 C C . ARG B 2 105 ? -5.454 4.357 37.712 1.00 81.09 ? 105 ARG B C 1 ATOM 7982 O O . ARG B 2 105 ? -4.631 4.264 36.801 1.00 86.63 ? 105 ARG B O 1 ATOM 7983 C CB . ARG B 2 105 ? -6.840 2.289 37.596 1.00 69.80 ? 105 ARG B CB 1 ATOM 7984 C CG . ARG B 2 105 ? -6.014 1.723 38.741 1.00 69.80 ? 105 ARG B CG 1 ATOM 7985 C CD . ARG B 2 105 ? -6.060 0.205 38.764 1.00 72.72 ? 105 ARG B CD 1 ATOM 7986 N NE . ARG B 2 105 ? -7.408 -0.296 39.017 1.00 81.43 ? 105 ARG B NE 1 ATOM 7987 C CZ . ARG B 2 105 ? -7.726 -1.584 39.083 1.00 75.90 ? 105 ARG B CZ 1 ATOM 7988 N NH1 . ARG B 2 105 ? -6.791 -2.509 38.914 1.00 78.06 ? 105 ARG B NH1 1 ATOM 7989 N NH2 . ARG B 2 105 ? -8.979 -1.948 39.318 1.00 76.45 ? 105 ARG B NH2 1 ATOM 7990 N N . GLN B 2 106 ? -5.179 4.918 38.885 1.00 81.05 ? 106 GLN B N 1 ATOM 7991 C CA . GLN B 2 106 ? -3.818 5.269 39.260 1.00 66.21 ? 106 GLN B CA 1 ATOM 7992 C C . GLN B 2 106 ? -3.127 3.986 39.699 1.00 68.07 ? 106 GLN B C 1 ATOM 7993 O O . GLN B 2 106 ? -3.566 3.341 40.647 1.00 94.21 ? 106 GLN B O 1 ATOM 7994 C CB . GLN B 2 106 ? -3.806 6.303 40.388 1.00 69.49 ? 106 GLN B CB 1 ATOM 7995 C CG . GLN B 2 106 ? -4.680 7.526 40.145 1.00 66.85 ? 106 GLN B CG 1 ATOM 7996 C CD . GLN B 2 106 ? -3.937 8.641 39.440 1.00 83.91 ? 106 GLN B CD 1 ATOM 7997 O OE1 . GLN B 2 106 ? -2.900 8.414 38.822 1.00 113.31 ? 106 GLN B OE1 1 ATOM 7998 N NE2 . GLN B 2 106 ? -4.460 9.858 39.539 1.00 75.10 ? 106 GLN B NE2 1 ATOM 7999 N N . VAL B 2 107 ? -2.053 3.609 39.016 1.00 68.72 ? 107 VAL B N 1 ATOM 8000 C CA . VAL B 2 107 ? -1.416 2.324 39.290 1.00 72.10 ? 107 VAL B CA 1 ATOM 8001 C C . VAL B 2 107 ? -0.154 2.470 40.132 1.00 81.64 ? 107 VAL B C 1 ATOM 8002 O O . VAL B 2 107 ? 0.587 3.445 40.005 1.00 94.13 ? 107 VAL B O 1 ATOM 8003 C CB . VAL B 2 107 ? -1.073 1.578 37.988 1.00 72.42 ? 107 VAL B CB 1 ATOM 8004 C CG1 . VAL B 2 107 ? -2.335 1.024 37.348 1.00 78.48 ? 107 VAL B CG1 1 ATOM 8005 C CG2 . VAL B 2 107 ? -0.344 2.495 37.028 1.00 76.34 ? 107 VAL B CG2 1 ATOM 8006 N N . GLU B 2 108 ? 0.075 1.489 40.999 1.00 80.57 ? 108 GLU B N 1 ATOM 8007 C CA . GLU B 2 108 ? 1.212 1.510 41.910 1.00 93.48 ? 108 GLU B CA 1 ATOM 8008 C C . GLU B 2 108 ? 2.519 1.195 41.189 1.00 104.28 ? 108 GLU B C 1 ATOM 8009 O O . GLU B 2 108 ? 2.523 0.523 40.156 1.00 103.71 ? 108 GLU B O 1 ATOM 8010 C CB . GLU B 2 108 ? 0.993 0.519 43.055 1.00 95.35 ? 108 GLU B CB 1 ATOM 8011 C CG . GLU B 2 108 ? -0.300 0.740 43.825 1.00 96.26 ? 108 GLU B CG 1 ATOM 8012 C CD . GLU B 2 108 ? -0.442 -0.194 45.011 1.00 117.45 ? 108 GLU B CD 1 ATOM 8013 O OE1 . GLU B 2 108 ? 0.587 -0.726 45.477 1.00 129.24 ? 108 GLU B OE1 1 ATOM 8014 O OE2 . GLU B 2 108 ? -1.583 -0.397 45.475 1.00 125.71 ? 108 GLU B OE2 1 ATOM 8015 N N . ASP B 2 109 ? 3.620 1.691 41.751 1.00 106.68 ? 109 ASP B N 1 ATOM 8016 C CA . ASP B 2 109 ? 4.960 1.512 41.192 1.00 94.10 ? 109 ASP B CA 1 ATOM 8017 C C . ASP B 2 109 ? 5.038 2.005 39.747 1.00 89.73 ? 109 ASP B C 1 ATOM 8018 O O . ASP B 2 109 ? 5.772 1.455 38.925 1.00 94.02 ? 109 ASP B O 1 ATOM 8019 C CB . ASP B 2 109 ? 5.390 0.045 41.282 1.00 94.74 ? 109 ASP B CB 1 ATOM 8020 C CG . ASP B 2 109 ? 6.890 -0.133 41.140 1.00 122.33 ? 109 ASP B CG 1 ATOM 8021 O OD1 . ASP B 2 109 ? 7.623 0.203 42.093 1.00 132.65 ? 109 ASP B OD1 1 ATOM 8022 O OD2 . ASP B 2 109 ? 7.335 -0.612 40.076 1.00 139.20 ? 109 ASP B OD2 1 ATOM 8023 N N . TYR B 2 110 ? 4.273 3.048 39.446 1.00 79.52 ? 110 TYR B N 1 ATOM 8024 C CA . TYR B 2 110 ? 4.298 3.662 38.127 1.00 75.63 ? 110 TYR B CA 1 ATOM 8025 C C . TYR B 2 110 ? 5.572 4.486 37.982 1.00 83.63 ? 110 TYR B C 1 ATOM 8026 O O . TYR B 2 110 ? 5.813 5.394 38.778 1.00 87.00 ? 110 TYR B O 1 ATOM 8027 C CB . TYR B 2 110 ? 3.057 4.531 37.920 1.00 76.41 ? 110 TYR B CB 1 ATOM 8028 C CG . TYR B 2 110 ? 2.745 4.865 36.478 1.00 79.22 ? 110 TYR B CG 1 ATOM 8029 C CD1 . TYR B 2 110 ? 2.452 3.864 35.560 1.00 73.61 ? 110 TYR B CD1 1 ATOM 8030 C CD2 . TYR B 2 110 ? 2.717 6.182 36.041 1.00 84.49 ? 110 TYR B CD2 1 ATOM 8031 C CE1 . TYR B 2 110 ? 2.154 4.165 34.244 1.00 73.25 ? 110 TYR B CE1 1 ATOM 8032 C CE2 . TYR B 2 110 ? 2.420 6.493 34.727 1.00 86.44 ? 110 TYR B CE2 1 ATOM 8033 C CZ . TYR B 2 110 ? 2.140 5.481 33.834 1.00 83.05 ? 110 TYR B CZ 1 ATOM 8034 O OH . TYR B 2 110 ? 1.843 5.786 32.526 1.00 89.71 ? 110 TYR B OH 1 ATOM 8035 N N . PRO B 2 111 ? 6.394 4.164 36.970 1.00 82.49 ? 111 PRO B N 1 ATOM 8036 C CA . PRO B 2 111 ? 7.696 4.808 36.746 1.00 83.42 ? 111 PRO B CA 1 ATOM 8037 C C . PRO B 2 111 ? 7.599 6.331 36.696 1.00 85.88 ? 111 PRO B C 1 ATOM 8038 O O . PRO B 2 111 ? 6.639 6.870 36.147 1.00 82.05 ? 111 PRO B O 1 ATOM 8039 C CB . PRO B 2 111 ? 8.145 4.240 35.392 1.00 75.47 ? 111 PRO B CB 1 ATOM 8040 C CG . PRO B 2 111 ? 6.906 3.677 34.767 1.00 74.47 ? 111 PRO B CG 1 ATOM 8041 C CD . PRO B 2 111 ? 6.071 3.199 35.907 1.00 76.71 ? 111 PRO B CD 1 ATOM 8042 N N . VAL B 2 112 ? 8.584 7.010 37.275 1.00 84.65 ? 112 VAL B N 1 ATOM 8043 C CA . VAL B 2 112 ? 8.547 8.464 37.384 1.00 72.57 ? 112 VAL B CA 1 ATOM 8044 C C . VAL B 2 112 ? 9.790 9.122 36.793 1.00 76.07 ? 112 VAL B C 1 ATOM 8045 O O . VAL B 2 112 ? 10.916 8.781 37.153 1.00 77.24 ? 112 VAL B O 1 ATOM 8046 C CB . VAL B 2 112 ? 8.403 8.908 38.854 1.00 69.34 ? 112 VAL B CB 1 ATOM 8047 C CG1 . VAL B 2 112 ? 8.473 10.424 38.963 1.00 82.67 ? 112 VAL B CG1 1 ATOM 8048 C CG2 . VAL B 2 112 ? 7.104 8.384 39.446 1.00 69.23 ? 112 VAL B CG2 1 ATOM 8049 N N . ASP B 2 113 ? 9.576 10.065 35.882 1.00 80.73 ? 113 ASP B N 1 ATOM 8050 C CA . ASP B 2 113 ? 10.668 10.854 35.324 1.00 80.39 ? 113 ASP B CA 1 ATOM 8051 C C . ASP B 2 113 ? 10.686 12.246 35.945 1.00 80.70 ? 113 ASP B C 1 ATOM 8052 O O . ASP B 2 113 ? 9.675 12.948 35.942 1.00 84.17 ? 113 ASP B O 1 ATOM 8053 C CB . ASP B 2 113 ? 10.543 10.958 33.804 1.00 77.33 ? 113 ASP B CB 1 ATOM 8054 C CG . ASP B 2 113 ? 10.688 9.619 33.114 1.00 99.09 ? 113 ASP B CG 1 ATOM 8055 O OD1 . ASP B 2 113 ? 9.963 9.379 32.125 1.00 114.95 ? 113 ASP B OD1 1 ATOM 8056 O OD2 . ASP B 2 113 ? 11.527 8.807 33.558 1.00 100.86 ? 113 ASP B OD2 1 ATOM 8057 N N . ILE B 2 114 ? 11.836 12.638 36.481 1.00 79.25 ? 114 ILE B N 1 ATOM 8058 C CA . ILE B 2 114 ? 11.977 13.949 37.103 1.00 77.60 ? 114 ILE B CA 1 ATOM 8059 C C . ILE B 2 114 ? 13.099 14.755 36.460 1.00 67.97 ? 114 ILE B C 1 ATOM 8060 O O . ILE B 2 114 ? 14.268 14.380 36.542 1.00 69.80 ? 114 ILE B O 1 ATOM 8061 C CB . ILE B 2 114 ? 12.255 13.834 38.614 1.00 66.27 ? 114 ILE B CB 1 ATOM 8062 C CG1 . ILE B 2 114 ? 11.116 13.094 39.316 1.00 78.58 ? 114 ILE B CG1 1 ATOM 8063 C CG2 . ILE B 2 114 ? 12.452 15.213 39.224 1.00 65.13 ? 114 ILE B CG2 1 ATOM 8064 C CD1 . ILE B 2 114 ? 11.311 12.953 40.811 1.00 68.80 ? 114 ILE B CD1 1 ATOM 8065 N N . TYR B 2 115 ? 12.740 15.862 35.819 1.00 62.76 ? 115 TYR B N 1 ATOM 8066 C CA . TYR B 2 115 ? 13.738 16.756 35.248 1.00 64.60 ? 115 TYR B CA 1 ATOM 8067 C C . TYR B 2 115 ? 13.755 18.075 36.009 1.00 62.97 ? 115 TYR B C 1 ATOM 8068 O O . TYR B 2 115 ? 12.719 18.715 36.184 1.00 60.79 ? 115 TYR B O 1 ATOM 8069 C CB . TYR B 2 115 ? 13.471 17.001 33.763 1.00 70.49 ? 115 TYR B CB 1 ATOM 8070 C CG . TYR B 2 115 ? 14.628 17.663 33.050 1.00 80.64 ? 115 TYR B CG 1 ATOM 8071 C CD1 . TYR B 2 115 ? 15.697 16.911 32.579 1.00 95.64 ? 115 TYR B CD1 1 ATOM 8072 C CD2 . TYR B 2 115 ? 14.658 19.038 32.855 1.00 67.66 ? 115 TYR B CD2 1 ATOM 8073 C CE1 . TYR B 2 115 ? 16.760 17.508 31.930 1.00 92.10 ? 115 TYR B CE1 1 ATOM 8074 C CE2 . TYR B 2 115 ? 15.719 19.644 32.206 1.00 72.10 ? 115 TYR B CE2 1 ATOM 8075 C CZ . TYR B 2 115 ? 16.766 18.874 31.746 1.00 79.96 ? 115 TYR B CZ 1 ATOM 8076 O OH . TYR B 2 115 ? 17.824 19.469 31.099 1.00 74.26 ? 115 TYR B OH 1 ATOM 8077 N N . TYR B 2 116 ? 14.939 18.473 36.461 1.00 65.46 ? 116 TYR B N 1 ATOM 8078 C CA . TYR B 2 116 ? 15.080 19.675 37.271 1.00 66.88 ? 116 TYR B CA 1 ATOM 8079 C C . TYR B 2 116 ? 15.448 20.895 36.434 1.00 83.99 ? 116 TYR B C 1 ATOM 8080 O O . TYR B 2 116 ? 16.387 20.856 35.640 1.00 95.20 ? 116 TYR B O 1 ATOM 8081 C CB . TYR B 2 116 ? 16.136 19.461 38.357 1.00 68.79 ? 116 TYR B CB 1 ATOM 8082 C CG . TYR B 2 116 ? 15.626 19.668 39.764 1.00 69.68 ? 116 TYR B CG 1 ATOM 8083 C CD1 . TYR B 2 116 ? 15.371 18.587 40.596 1.00 73.97 ? 116 TYR B CD1 1 ATOM 8084 C CD2 . TYR B 2 116 ? 15.399 20.945 40.259 1.00 76.73 ? 116 TYR B CD2 1 ATOM 8085 C CE1 . TYR B 2 116 ? 14.901 18.771 41.883 1.00 89.39 ? 116 TYR B CE1 1 ATOM 8086 C CE2 . TYR B 2 116 ? 14.931 21.139 41.545 1.00 85.95 ? 116 TYR B CE2 1 ATOM 8087 C CZ . TYR B 2 116 ? 14.684 20.049 42.352 1.00 92.36 ? 116 TYR B CZ 1 ATOM 8088 O OH . TYR B 2 116 ? 14.218 20.237 43.633 1.00 96.03 ? 116 TYR B OH 1 ATOM 8089 N N . LEU B 2 117 ? 14.696 21.975 36.613 1.00 83.66 ? 117 LEU B N 1 ATOM 8090 C CA . LEU B 2 117 ? 15.057 23.260 36.032 1.00 64.45 ? 117 LEU B CA 1 ATOM 8091 C C . LEU B 2 117 ? 15.499 24.200 37.142 1.00 67.56 ? 117 LEU B C 1 ATOM 8092 O O . LEU B 2 117 ? 14.694 24.619 37.974 1.00 62.67 ? 117 LEU B O 1 ATOM 8093 C CB . LEU B 2 117 ? 13.891 23.860 35.249 1.00 59.94 ? 117 LEU B CB 1 ATOM 8094 C CG . LEU B 2 117 ? 13.558 23.162 33.931 1.00 60.58 ? 117 LEU B CG 1 ATOM 8095 C CD1 . LEU B 2 117 ? 12.430 23.884 33.222 1.00 63.17 ? 117 LEU B CD1 1 ATOM 8096 C CD2 . LEU B 2 117 ? 14.788 23.081 33.041 1.00 62.22 ? 117 LEU B CD2 1 ATOM 8097 N N . MET B 2 118 ? 16.787 24.521 37.151 1.00 77.10 ? 118 MET B N 1 ATOM 8098 C CA . MET B 2 118 ? 17.374 25.299 38.232 1.00 81.02 ? 118 MET B CA 1 ATOM 8099 C C . MET B 2 118 ? 17.806 26.685 37.767 1.00 83.70 ? 118 MET B C 1 ATOM 8100 O O . MET B 2 118 ? 18.370 26.843 36.684 1.00 85.27 ? 118 MET B O 1 ATOM 8101 C CB . MET B 2 118 ? 18.563 24.545 38.828 1.00 79.52 ? 118 MET B CB 1 ATOM 8102 C CG . MET B 2 118 ? 19.506 23.974 37.782 1.00 87.33 ? 118 MET B CG 1 ATOM 8103 S SD . MET B 2 118 ? 20.700 22.812 38.464 1.00 154.45 ? 118 MET B SD 1 ATOM 8104 C CE . MET B 2 118 ? 19.608 21.579 39.171 1.00 74.12 ? 118 MET B CE 1 ATOM 8105 N N . ASP B 2 119 ? 17.535 27.685 38.597 1.00 77.63 ? 119 ASP B N 1 ATOM 8106 C CA . ASP B 2 119 ? 17.929 29.055 38.302 1.00 67.81 ? 119 ASP B CA 1 ATOM 8107 C C . ASP B 2 119 ? 19.361 29.279 38.774 1.00 79.73 ? 119 ASP B C 1 ATOM 8108 O O . ASP B 2 119 ? 19.657 29.170 39.961 1.00 85.27 ? 119 ASP B O 1 ATOM 8109 C CB . ASP B 2 119 ? 16.966 30.040 38.971 1.00 66.02 ? 119 ASP B CB 1 ATOM 8110 C CG . ASP B 2 119 ? 17.305 31.487 38.673 1.00 82.54 ? 119 ASP B CG 1 ATOM 8111 O OD1 . ASP B 2 119 ? 16.872 32.367 39.447 1.00 77.85 ? 119 ASP B OD1 1 ATOM 8112 O OD2 . ASP B 2 119 ? 17.999 31.748 37.669 1.00 107.23 ? 119 ASP B OD2 1 ATOM 8113 N N . LEU B 2 120 ? 20.252 29.567 37.832 1.00 82.81 ? 120 LEU B N 1 ATOM 8114 C CA . LEU B 2 120 ? 21.667 29.746 38.144 1.00 87.25 ? 120 LEU B CA 1 ATOM 8115 C C . LEU B 2 120 ? 22.064 31.213 38.302 1.00 77.25 ? 120 LEU B C 1 ATOM 8116 O O . LEU B 2 120 ? 23.245 31.528 38.446 1.00 76.78 ? 120 LEU B O 1 ATOM 8117 C CB . LEU B 2 120 ? 22.534 29.071 37.080 1.00 90.35 ? 120 LEU B CB 1 ATOM 8118 C CG . LEU B 2 120 ? 23.092 27.707 37.505 1.00 69.84 ? 120 LEU B CG 1 ATOM 8119 C CD1 . LEU B 2 120 ? 21.979 26.766 37.944 1.00 65.38 ? 120 LEU B CD1 1 ATOM 8120 C CD2 . LEU B 2 120 ? 23.920 27.082 36.393 1.00 71.57 ? 120 LEU B CD2 1 ATOM 8121 N N . SER B 2 121 ? 21.081 32.107 38.257 1.00 65.03 ? 121 SER B N 1 ATOM 8122 C CA . SER B 2 121 ? 21.341 33.536 38.413 1.00 65.42 ? 121 SER B CA 1 ATOM 8123 C C . SER B 2 121 ? 21.896 33.851 39.801 1.00 66.69 ? 121 SER B C 1 ATOM 8124 O O . SER B 2 121 ? 21.717 33.076 40.741 1.00 75.91 ? 121 SER B O 1 ATOM 8125 C CB . SER B 2 121 ? 20.069 34.345 38.160 1.00 62.99 ? 121 SER B CB 1 ATOM 8126 O OG . SER B 2 121 ? 19.095 34.099 39.159 1.00 65.70 ? 121 SER B OG 1 ATOM 8127 N N . TYR B 2 122 ? 22.572 34.991 39.914 1.00 66.89 ? 122 TYR B N 1 ATOM 8128 C CA . TYR B 2 122 ? 23.305 35.365 41.124 1.00 70.91 ? 122 TYR B CA 1 ATOM 8129 C C . TYR B 2 122 ? 22.451 35.391 42.390 1.00 81.78 ? 122 TYR B C 1 ATOM 8130 O O . TYR B 2 122 ? 22.967 35.229 43.496 1.00 86.33 ? 122 TYR B O 1 ATOM 8131 C CB . TYR B 2 122 ? 23.964 36.733 40.929 1.00 70.45 ? 122 TYR B CB 1 ATOM 8132 C CG . TYR B 2 122 ? 25.005 37.060 41.974 1.00 84.19 ? 122 TYR B CG 1 ATOM 8133 C CD1 . TYR B 2 122 ? 26.281 36.517 41.901 1.00 98.65 ? 122 TYR B CD1 1 ATOM 8134 C CD2 . TYR B 2 122 ? 24.715 37.912 43.032 1.00 85.96 ? 122 TYR B CD2 1 ATOM 8135 C CE1 . TYR B 2 122 ? 27.239 36.811 42.853 1.00 97.16 ? 122 TYR B CE1 1 ATOM 8136 C CE2 . TYR B 2 122 ? 25.668 38.212 43.990 1.00 95.79 ? 122 TYR B CE2 1 ATOM 8137 C CZ . TYR B 2 122 ? 26.928 37.658 43.894 1.00 90.15 ? 122 TYR B CZ 1 ATOM 8138 O OH . TYR B 2 122 ? 27.882 37.951 44.843 1.00 81.45 ? 122 TYR B OH 1 ATOM 8139 N N . SER B 2 123 ? 21.148 35.592 42.228 1.00 80.37 ? 123 SER B N 1 ATOM 8140 C CA . SER B 2 123 ? 20.237 35.640 43.367 1.00 71.57 ? 123 SER B CA 1 ATOM 8141 C C . SER B 2 123 ? 20.067 34.264 44.011 1.00 69.56 ? 123 SER B C 1 ATOM 8142 O O . SER B 2 123 ? 19.562 34.148 45.128 1.00 68.22 ? 123 SER B O 1 ATOM 8143 C CB . SER B 2 123 ? 18.877 36.188 42.932 1.00 63.38 ? 123 SER B CB 1 ATOM 8144 O OG . SER B 2 123 ? 18.296 35.369 41.933 1.00 59.31 ? 123 SER B OG 1 ATOM 8145 N N . MET B 2 124 ? 20.492 33.227 43.297 1.00 67.49 ? 124 MET B N 1 ATOM 8146 C CA . MET B 2 124 ? 20.313 31.852 43.746 1.00 75.35 ? 124 MET B CA 1 ATOM 8147 C C . MET B 2 124 ? 21.532 31.264 44.454 1.00 93.15 ? 124 MET B C 1 ATOM 8148 O O . MET B 2 124 ? 21.516 30.097 44.847 1.00 121.97 ? 124 MET B O 1 ATOM 8149 C CB . MET B 2 124 ? 19.939 30.968 42.558 1.00 73.01 ? 124 MET B CB 1 ATOM 8150 C CG . MET B 2 124 ? 18.506 31.142 42.089 1.00 66.23 ? 124 MET B CG 1 ATOM 8151 S SD . MET B 2 124 ? 17.342 30.207 43.098 1.00 70.35 ? 124 MET B SD 1 ATOM 8152 C CE . MET B 2 124 ? 17.909 28.534 42.803 1.00 134.59 ? 124 MET B CE 1 ATOM 8153 N N . LYS B 2 125 ? 22.587 32.058 44.612 1.00 76.76 ? 125 LYS B N 1 ATOM 8154 C CA . LYS B 2 125 ? 23.793 31.578 45.281 1.00 84.24 ? 125 LYS B CA 1 ATOM 8155 C C . LYS B 2 125 ? 23.506 31.267 46.747 1.00 89.68 ? 125 LYS B C 1 ATOM 8156 O O . LYS B 2 125 ? 24.122 30.380 47.340 1.00 88.53 ? 125 LYS B O 1 ATOM 8157 C CB . LYS B 2 125 ? 24.926 32.601 45.165 1.00 89.27 ? 125 LYS B CB 1 ATOM 8158 C CG . LYS B 2 125 ? 26.273 32.078 45.647 1.00 106.01 ? 125 LYS B CG 1 ATOM 8159 C CD . LYS B 2 125 ? 27.414 33.009 45.264 1.00 115.70 ? 125 LYS B CD 1 ATOM 8160 C CE . LYS B 2 125 ? 27.330 34.334 46.001 1.00 116.71 ? 125 LYS B CE 1 ATOM 8161 N NZ . LYS B 2 125 ? 28.471 35.224 45.652 1.00 116.06 ? 125 LYS B NZ 1 ATOM 8162 N N . ASP B 2 126 ? 22.559 32.000 47.320 1.00 97.16 ? 126 ASP B N 1 ATOM 8163 C CA . ASP B 2 126 ? 22.141 31.784 48.698 1.00 95.42 ? 126 ASP B CA 1 ATOM 8164 C C . ASP B 2 126 ? 21.254 30.548 48.821 1.00 84.93 ? 126 ASP B C 1 ATOM 8165 O O . ASP B 2 126 ? 21.195 29.920 49.876 1.00 86.23 ? 126 ASP B O 1 ATOM 8166 C CB . ASP B 2 126 ? 21.402 33.015 49.224 1.00 102.94 ? 126 ASP B CB 1 ATOM 8167 C CG . ASP B 2 126 ? 20.221 33.399 48.353 1.00 107.37 ? 126 ASP B CG 1 ATOM 8168 O OD1 . ASP B 2 126 ? 20.442 33.739 47.172 1.00 102.31 ? 126 ASP B OD1 1 ATOM 8169 O OD2 . ASP B 2 126 ? 19.075 33.367 48.848 1.00 114.05 ? 126 ASP B OD2 1 ATOM 8170 N N . ASP B 2 127 ? 20.562 30.213 47.737 1.00 82.43 ? 127 ASP B N 1 ATOM 8171 C CA . ASP B 2 127 ? 19.635 29.085 47.723 1.00 83.17 ? 127 ASP B CA 1 ATOM 8172 C C . ASP B 2 127 ? 20.274 27.817 47.165 1.00 92.38 ? 127 ASP B C 1 ATOM 8173 O O . ASP B 2 127 ? 19.615 26.785 47.041 1.00 96.20 ? 127 ASP B O 1 ATOM 8174 C CB . ASP B 2 127 ? 18.390 29.434 46.905 1.00 84.52 ? 127 ASP B CB 1 ATOM 8175 C CG . ASP B 2 127 ? 17.874 30.829 47.195 1.00 104.08 ? 127 ASP B CG 1 ATOM 8176 O OD1 . ASP B 2 127 ? 18.277 31.771 46.480 1.00 92.75 ? 127 ASP B OD1 1 ATOM 8177 O OD2 . ASP B 2 127 ? 17.068 30.984 48.135 1.00 130.33 ? 127 ASP B OD2 1 ATOM 8178 N N . LEU B 2 128 ? 21.558 27.898 46.832 1.00 95.76 ? 128 LEU B N 1 ATOM 8179 C CA . LEU B 2 128 ? 22.241 26.815 46.131 1.00 98.13 ? 128 LEU B CA 1 ATOM 8180 C C . LEU B 2 128 ? 22.499 25.594 47.018 1.00 95.20 ? 128 LEU B C 1 ATOM 8181 O O . LEU B 2 128 ? 22.965 24.561 46.541 1.00 84.33 ? 128 LEU B O 1 ATOM 8182 C CB . LEU B 2 128 ? 23.562 27.322 45.549 1.00 106.17 ? 128 LEU B CB 1 ATOM 8183 C CG . LEU B 2 128 ? 24.018 26.656 44.250 1.00 102.52 ? 128 LEU B CG 1 ATOM 8184 C CD1 . LEU B 2 128 ? 22.960 26.826 43.171 1.00 81.80 ? 128 LEU B CD1 1 ATOM 8185 C CD2 . LEU B 2 128 ? 25.351 27.226 43.791 1.00 113.79 ? 128 LEU B CD2 1 ATOM 8186 N N . TRP B 2 129 ? 22.201 25.719 48.307 1.00 97.75 ? 129 TRP B N 1 ATOM 8187 C CA . TRP B 2 129 ? 22.353 24.612 49.246 1.00 93.76 ? 129 TRP B CA 1 ATOM 8188 C C . TRP B 2 129 ? 21.426 23.449 48.907 1.00 93.45 ? 129 TRP B C 1 ATOM 8189 O O . TRP B 2 129 ? 21.708 22.299 49.244 1.00 95.14 ? 129 TRP B O 1 ATOM 8190 C CB . TRP B 2 129 ? 22.077 25.089 50.672 1.00 104.00 ? 129 TRP B CB 1 ATOM 8191 C CG . TRP B 2 129 ? 20.772 25.807 50.794 1.00 112.13 ? 129 TRP B CG 1 ATOM 8192 C CD1 . TRP B 2 129 ? 20.564 27.147 50.672 1.00 135.74 ? 129 TRP B CD1 1 ATOM 8193 C CD2 . TRP B 2 129 ? 19.489 25.222 51.045 1.00 105.78 ? 129 TRP B CD2 1 ATOM 8194 N NE1 . TRP B 2 129 ? 19.232 27.438 50.836 1.00 139.94 ? 129 TRP B NE1 1 ATOM 8195 C CE2 . TRP B 2 129 ? 18.550 26.272 51.067 1.00 120.01 ? 129 TRP B CE2 1 ATOM 8196 C CE3 . TRP B 2 129 ? 19.043 23.915 51.258 1.00 107.52 ? 129 TRP B CE3 1 ATOM 8197 C CZ2 . TRP B 2 129 ? 17.192 26.055 51.291 1.00 115.33 ? 129 TRP B CZ2 1 ATOM 8198 C CZ3 . TRP B 2 129 ? 17.695 23.701 51.480 1.00 112.34 ? 129 TRP B CZ3 1 ATOM 8199 C CH2 . TRP B 2 129 ? 16.786 24.766 51.496 1.00 116.21 ? 129 TRP B CH2 1 ATOM 8200 N N . SER B 2 130 ? 20.319 23.757 48.239 1.00 92.80 ? 130 SER B N 1 ATOM 8201 C CA . SER B 2 130 ? 19.296 22.762 47.940 1.00 106.32 ? 130 SER B CA 1 ATOM 8202 C C . SER B 2 130 ? 19.706 21.814 46.818 1.00 111.26 ? 130 SER B C 1 ATOM 8203 O O . SER B 2 130 ? 19.199 20.695 46.729 1.00 97.62 ? 130 SER B O 1 ATOM 8204 C CB . SER B 2 130 ? 17.981 23.454 47.577 1.00 101.17 ? 130 SER B CB 1 ATOM 8205 O OG . SER B 2 130 ? 18.155 24.329 46.476 1.00 88.64 ? 130 SER B OG 1 ATOM 8206 N N . ILE B 2 131 ? 20.618 22.260 45.961 1.00 123.33 ? 131 ILE B N 1 ATOM 8207 C CA . ILE B 2 131 ? 21.052 21.442 44.835 1.00 117.87 ? 131 ILE B CA 1 ATOM 8208 C C . ILE B 2 131 ? 21.979 20.329 45.316 1.00 116.82 ? 131 ILE B C 1 ATOM 8209 O O . ILE B 2 131 ? 22.064 19.272 44.695 1.00 114.67 ? 131 ILE B O 1 ATOM 8210 C CB . ILE B 2 131 ? 21.759 22.284 43.747 1.00 123.69 ? 131 ILE B CB 1 ATOM 8211 C CG1 . ILE B 2 131 ? 21.685 21.579 42.393 1.00 113.07 ? 131 ILE B CG1 1 ATOM 8212 C CG2 . ILE B 2 131 ? 23.206 22.583 44.124 1.00 141.83 ? 131 ILE B CG2 1 ATOM 8213 C CD1 . ILE B 2 131 ? 22.591 22.185 41.349 1.00 112.72 ? 131 ILE B CD1 1 ATOM 8214 N N . GLN B 2 132 ? 22.650 20.562 46.440 1.00 113.52 ? 132 GLN B N 1 ATOM 8215 C CA . GLN B 2 132 ? 23.516 19.555 47.037 1.00 106.76 ? 132 GLN B CA 1 ATOM 8216 C C . GLN B 2 132 ? 22.640 18.409 47.496 1.00 104.63 ? 132 GLN B C 1 ATOM 8217 O O . GLN B 2 132 ? 21.430 18.599 47.657 1.00 102.33 ? 132 GLN B O 1 ATOM 8218 C CB . GLN B 2 132 ? 24.312 20.132 48.205 1.00 110.48 ? 132 GLN B CB 1 ATOM 8219 C CG . GLN B 2 132 ? 25.040 21.421 47.873 1.00 122.17 ? 132 GLN B CG 1 ATOM 8220 C CD . GLN B 2 132 ? 26.016 21.261 46.726 1.00 127.44 ? 132 GLN B CD 1 ATOM 8221 O OE1 . GLN B 2 132 ? 26.629 20.206 46.557 1.00 142.19 ? 132 GLN B OE1 1 ATOM 8222 N NE2 . GLN B 2 132 ? 26.163 22.310 45.926 1.00 114.69 ? 132 GLN B NE2 1 ATOM 8223 N N . ASN B 2 133 ? 23.235 17.236 47.716 1.00 116.34 ? 133 ASN B N 1 ATOM 8224 C CA . ASN B 2 133 ? 22.439 16.040 47.969 1.00 122.86 ? 133 ASN B CA 1 ATOM 8225 C C . ASN B 2 133 ? 21.537 15.827 46.757 1.00 113.30 ? 133 ASN B C 1 ATOM 8226 O O . ASN B 2 133 ? 22.031 15.426 45.701 1.00 109.53 ? 133 ASN B O 1 ATOM 8227 C CB . ASN B 2 133 ? 21.654 16.159 49.278 1.00 132.29 ? 133 ASN B CB 1 ATOM 8228 C CG . ASN B 2 133 ? 22.543 16.027 50.505 1.00 133.03 ? 133 ASN B CG 1 ATOM 8229 O OD1 . ASN B 2 133 ? 22.292 15.195 51.377 1.00 120.71 ? 133 ASN B OD1 1 ATOM 8230 N ND2 . ASN B 2 133 ? 23.592 16.845 50.573 1.00 138.24 ? 133 ASN B ND2 1 ATOM 8231 N N . LEU B 2 134 ? 20.234 16.060 46.905 1.00 115.81 ? 134 LEU B N 1 ATOM 8232 C CA . LEU B 2 134 ? 19.306 15.905 45.783 1.00 115.13 ? 134 LEU B CA 1 ATOM 8233 C C . LEU B 2 134 ? 19.325 14.461 45.301 1.00 113.77 ? 134 LEU B C 1 ATOM 8234 O O . LEU B 2 134 ? 18.891 13.587 46.029 1.00 106.15 ? 134 LEU B O 1 ATOM 8235 C CB . LEU B 2 134 ? 19.646 16.873 44.644 1.00 105.00 ? 134 LEU B CB 1 ATOM 8236 C CG . LEU B 2 134 ? 18.525 17.198 43.659 1.00 91.71 ? 134 LEU B CG 1 ATOM 8237 C CD1 . LEU B 2 134 ? 17.281 17.649 44.404 1.00 89.38 ? 134 LEU B CD1 1 ATOM 8238 C CD2 . LEU B 2 134 ? 18.975 18.266 42.675 1.00 82.88 ? 134 LEU B CD2 1 ATOM 8239 N N . GLY B 2 135 ? 19.833 14.203 44.099 1.00 115.92 ? 135 GLY B N 1 ATOM 8240 C CA . GLY B 2 135 ? 19.723 12.884 43.489 1.00 118.20 ? 135 GLY B CA 1 ATOM 8241 C C . GLY B 2 135 ? 20.020 11.701 44.409 1.00 115.85 ? 135 GLY B C 1 ATOM 8242 O O . GLY B 2 135 ? 19.453 10.629 44.230 1.00 112.33 ? 135 GLY B O 1 ATOM 8243 N N . THR B 2 136 ? 20.892 11.892 45.392 1.00 125.28 ? 136 THR B N 1 ATOM 8244 C CA . THR B 2 136 ? 21.037 10.920 46.462 1.00 130.20 ? 136 THR B CA 1 ATOM 8245 C C . THR B 2 136 ? 19.786 10.917 47.345 1.00 138.85 ? 136 THR B C 1 ATOM 8246 O O . THR B 2 136 ? 19.225 9.861 47.628 1.00 145.46 ? 136 THR B O 1 ATOM 8247 C CB . THR B 2 136 ? 22.276 11.217 47.332 1.00 129.78 ? 136 THR B CB 1 ATOM 8248 O OG1 . THR B 2 136 ? 23.464 11.068 46.547 1.00 139.20 ? 136 THR B OG1 1 ATOM 8249 C CG2 . THR B 2 136 ? 22.342 10.275 48.514 1.00 126.36 ? 136 THR B CG2 1 ATOM 8250 N N . LYS B 2 137 ? 19.375 12.116 47.769 1.00 142.30 ? 137 LYS B N 1 ATOM 8251 C CA . LYS B 2 137 ? 18.195 12.335 48.616 1.00 140.73 ? 137 LYS B CA 1 ATOM 8252 C C . LYS B 2 137 ? 16.877 12.325 47.839 1.00 132.22 ? 137 LYS B C 1 ATOM 8253 O O . LYS B 2 137 ? 15.832 11.953 48.377 1.00 146.03 ? 137 LYS B O 1 ATOM 8254 C CB . LYS B 2 137 ? 18.339 13.666 49.370 1.00 141.10 ? 137 LYS B CB 1 ATOM 8255 C CG . LYS B 2 137 ? 19.494 13.716 50.368 1.00 143.54 ? 137 LYS B CG 1 ATOM 8256 C CD . LYS B 2 137 ? 19.142 12.986 51.641 1.00 135.28 ? 137 LYS B CD 1 ATOM 8257 C CE . LYS B 2 137 ? 20.346 12.787 52.525 1.00 138.09 ? 137 LYS B CE 1 ATOM 8258 N NZ . LYS B 2 137 ? 21.190 11.687 52.018 1.00 140.41 ? 137 LYS B NZ 1 ATOM 8259 N N . LEU B 2 138 ? 16.942 12.735 46.577 1.00 115.14 ? 138 LEU B N 1 ATOM 8260 C CA . LEU B 2 138 ? 15.805 12.791 45.672 1.00 110.61 ? 138 LEU B CA 1 ATOM 8261 C C . LEU B 2 138 ? 15.186 11.424 45.535 1.00 118.20 ? 138 LEU B C 1 ATOM 8262 O O . LEU B 2 138 ? 13.993 11.240 45.740 1.00 111.85 ? 138 LEU B O 1 ATOM 8263 C CB . LEU B 2 138 ? 16.252 13.286 44.294 1.00 102.25 ? 138 LEU B CB 1 ATOM 8264 C CG . LEU B 2 138 ? 15.464 14.374 43.545 1.00 95.95 ? 138 LEU B CG 1 ATOM 8265 C CD1 . LEU B 2 138 ? 15.561 14.255 42.012 1.00 92.28 ? 138 LEU B CD1 1 ATOM 8266 C CD2 . LEU B 2 138 ? 14.011 14.473 43.995 1.00 104.54 ? 138 LEU B CD2 1 ATOM 8267 N N . ALA B 2 139 ? 16.038 10.465 45.198 1.00 129.10 ? 139 ALA B N 1 ATOM 8268 C CA . ALA B 2 139 ? 15.694 9.062 45.184 1.00 127.63 ? 139 ALA B CA 1 ATOM 8269 C C . ALA B 2 139 ? 15.024 8.583 46.469 1.00 127.86 ? 139 ALA B C 1 ATOM 8270 O O . ALA B 2 139 ? 13.899 8.101 46.416 1.00 137.73 ? 139 ALA B O 1 ATOM 8271 C CB . ALA B 2 139 ? 16.919 8.270 44.926 1.00 132.91 ? 139 ALA B CB 1 ATOM 8272 N N . THR B 2 140 ? 15.713 8.719 47.615 1.00 126.06 ? 140 THR B N 1 ATOM 8273 C CA . THR B 2 140 ? 15.333 8.014 48.862 1.00 137.03 ? 140 THR B CA 1 ATOM 8274 C C . THR B 2 140 ? 13.862 8.102 49.158 1.00 137.15 ? 140 THR B C 1 ATOM 8275 O O . THR B 2 140 ? 13.220 7.097 49.425 1.00 141.52 ? 140 THR B O 1 ATOM 8276 C CB . THR B 2 140 ? 16.038 8.533 50.193 1.00 155.57 ? 140 THR B CB 1 ATOM 8277 O OG1 . THR B 2 140 ? 15.392 9.710 50.703 1.00 150.19 ? 140 THR B OG1 1 ATOM 8278 C CG2 . THR B 2 140 ? 17.536 8.741 50.058 1.00 159.33 ? 140 THR B CG2 1 ATOM 8279 N N . GLN B 2 141 ? 13.330 9.312 49.116 1.00 132.68 ? 141 GLN B N 1 ATOM 8280 C CA . GLN B 2 141 ? 11.944 9.537 49.454 1.00 131.77 ? 141 GLN B CA 1 ATOM 8281 C C . GLN B 2 141 ? 11.041 9.218 48.268 1.00 127.71 ? 141 GLN B C 1 ATOM 8282 O O . GLN B 2 141 ? 9.819 9.132 48.411 1.00 129.84 ? 141 GLN B O 1 ATOM 8283 C CB . GLN B 2 141 ? 11.756 10.972 49.947 1.00 130.39 ? 141 GLN B CB 1 ATOM 8284 C CG . GLN B 2 141 ? 11.901 11.034 51.455 1.00 139.80 ? 141 GLN B CG 1 ATOM 8285 C CD . GLN B 2 141 ? 11.376 9.764 52.114 1.00 150.25 ? 141 GLN B CD 1 ATOM 8286 O OE1 . GLN B 2 141 ? 10.191 9.452 52.012 1.00 160.91 ? 141 GLN B OE1 1 ATOM 8287 N NE2 . GLN B 2 141 ? 12.271 8.997 52.740 1.00 143.66 ? 141 GLN B NE2 1 ATOM 8288 N N . MET B 2 142 ? 11.634 8.998 47.100 1.00 119.06 ? 142 MET B N 1 ATOM 8289 C CA . MET B 2 142 ? 10.840 8.528 45.973 1.00 108.38 ? 142 MET B CA 1 ATOM 8290 C C . MET B 2 142 ? 10.783 7.003 45.878 1.00 105.01 ? 142 MET B C 1 ATOM 8291 O O . MET B 2 142 ? 9.985 6.465 45.116 1.00 102.19 ? 142 MET B O 1 ATOM 8292 C CB . MET B 2 142 ? 11.386 9.097 44.668 1.00 105.72 ? 142 MET B CB 1 ATOM 8293 C CG . MET B 2 142 ? 11.158 10.580 44.488 1.00 103.69 ? 142 MET B CG 1 ATOM 8294 S SD . MET B 2 142 ? 9.481 10.919 43.946 1.00 96.49 ? 142 MET B SD 1 ATOM 8295 C CE . MET B 2 142 ? 9.427 9.872 42.497 1.00 101.39 ? 142 MET B CE 1 ATOM 8296 N N . ARG B 2 143 ? 11.614 6.308 46.649 1.00 111.72 ? 143 ARG B N 1 ATOM 8297 C CA . ARG B 2 143 ? 11.682 4.850 46.550 1.00 114.64 ? 143 ARG B CA 1 ATOM 8298 C C . ARG B 2 143 ? 10.402 4.212 47.074 1.00 117.24 ? 143 ARG B C 1 ATOM 8299 O O . ARG B 2 143 ? 10.022 3.117 46.654 1.00 129.72 ? 143 ARG B O 1 ATOM 8300 C CB . ARG B 2 143 ? 12.894 4.305 47.314 1.00 122.88 ? 143 ARG B CB 1 ATOM 8301 C CG . ARG B 2 143 ? 13.088 2.794 47.200 1.00 130.91 ? 143 ARG B CG 1 ATOM 8302 C CD . ARG B 2 143 ? 14.305 2.315 47.986 1.00 131.72 ? 143 ARG B CD 1 ATOM 8303 N NE . ARG B 2 143 ? 15.545 2.923 47.509 1.00 129.34 ? 143 ARG B NE 1 ATOM 8304 C CZ . ARG B 2 143 ? 16.196 3.896 48.141 1.00 124.53 ? 143 ARG B CZ 1 ATOM 8305 N NH1 . ARG B 2 143 ? 15.731 4.373 49.287 1.00 127.88 ? 143 ARG B NH1 1 ATOM 8306 N NH2 . ARG B 2 143 ? 17.315 4.390 47.628 1.00 117.84 ? 143 ARG B NH2 1 ATOM 8307 N N . LYS B 2 144 ? 9.742 4.914 47.990 1.00 115.39 ? 144 LYS B N 1 ATOM 8308 C CA . LYS B 2 144 ? 8.485 4.462 48.570 1.00 124.90 ? 144 LYS B CA 1 ATOM 8309 C C . LYS B 2 144 ? 7.418 4.242 47.508 1.00 120.13 ? 144 LYS B C 1 ATOM 8310 O O . LYS B 2 144 ? 6.847 3.157 47.401 1.00 133.50 ? 144 LYS B O 1 ATOM 8311 C CB . LYS B 2 144 ? 7.977 5.478 49.593 1.00 133.76 ? 144 LYS B CB 1 ATOM 8312 C CG . LYS B 2 144 ? 8.995 5.879 50.640 1.00 146.75 ? 144 LYS B CG 1 ATOM 8313 C CD . LYS B 2 144 ? 8.370 6.820 51.651 1.00 148.75 ? 144 LYS B CD 1 ATOM 8314 C CE . LYS B 2 144 ? 7.571 7.912 50.957 1.00 136.70 ? 144 LYS B CE 1 ATOM 8315 N NZ . LYS B 2 144 ? 7.209 9.009 51.892 1.00 129.19 ? 144 LYS B NZ 1 ATOM 8316 N N . LEU B 2 145 ? 7.151 5.283 46.727 1.00 96.48 ? 145 LEU B N 1 ATOM 8317 C CA . LEU B 2 145 ? 6.093 5.229 45.728 1.00 91.22 ? 145 LEU B CA 1 ATOM 8318 C C . LEU B 2 145 ? 6.516 4.509 44.452 1.00 91.27 ? 145 LEU B C 1 ATOM 8319 O O . LEU B 2 145 ? 5.756 3.710 43.907 1.00 104.44 ? 145 LEU B O 1 ATOM 8320 C CB . LEU B 2 145 ? 5.616 6.642 45.388 1.00 86.35 ? 145 LEU B CB 1 ATOM 8321 C CG . LEU B 2 145 ? 5.062 7.462 46.554 1.00 85.97 ? 145 LEU B CG 1 ATOM 8322 C CD1 . LEU B 2 145 ? 4.501 8.788 46.065 1.00 76.58 ? 145 LEU B CD1 1 ATOM 8323 C CD2 . LEU B 2 145 ? 4.006 6.673 47.309 1.00 96.18 ? 145 LEU B CD2 1 ATOM 8324 N N . THR B 2 146 ? 7.724 4.791 43.973 1.00 88.43 ? 146 THR B N 1 ATOM 8325 C CA . THR B 2 146 ? 8.140 4.285 42.670 1.00 88.09 ? 146 THR B CA 1 ATOM 8326 C C . THR B 2 146 ? 9.561 3.723 42.627 1.00 104.04 ? 146 THR B C 1 ATOM 8327 O O . THR B 2 146 ? 10.534 4.435 42.881 1.00 118.94 ? 146 THR B O 1 ATOM 8328 C CB . THR B 2 146 ? 8.020 5.394 41.602 1.00 99.20 ? 146 THR B CB 1 ATOM 8329 O OG1 . THR B 2 146 ? 6.636 5.672 41.357 1.00 127.16 ? 146 THR B OG1 1 ATOM 8330 C CG2 . THR B 2 146 ? 8.677 4.971 40.302 1.00 81.91 ? 146 THR B CG2 1 ATOM 8331 N N . SER B 2 147 ? 9.666 2.434 42.318 1.00 105.48 ? 147 SER B N 1 ATOM 8332 C CA . SER B 2 147 ? 10.930 1.836 41.905 1.00 109.09 ? 147 SER B CA 1 ATOM 8333 C C . SER B 2 147 ? 11.138 2.116 40.420 1.00 119.67 ? 147 SER B C 1 ATOM 8334 O O . SER B 2 147 ? 10.167 2.317 39.691 1.00 117.00 ? 147 SER B O 1 ATOM 8335 C CB . SER B 2 147 ? 10.948 0.332 42.181 1.00 112.21 ? 147 SER B CB 1 ATOM 8336 O OG . SER B 2 147 ? 9.992 -0.345 41.385 1.00 110.32 ? 147 SER B OG 1 ATOM 8337 N N . ASN B 2 148 ? 12.393 2.119 39.978 1.00 138.18 ? 148 ASN B N 1 ATOM 8338 C CA . ASN B 2 148 ? 12.736 2.438 38.590 1.00 138.83 ? 148 ASN B CA 1 ATOM 8339 C C . ASN B 2 148 ? 12.282 3.844 38.193 1.00 117.60 ? 148 ASN B C 1 ATOM 8340 O O . ASN B 2 148 ? 11.330 4.016 37.430 1.00 101.85 ? 148 ASN B O 1 ATOM 8341 C CB . ASN B 2 148 ? 12.141 1.397 37.630 1.00 141.72 ? 148 ASN B CB 1 ATOM 8342 C CG . ASN B 2 148 ? 12.497 1.665 36.177 1.00 132.03 ? 148 ASN B CG 1 ATOM 8343 O OD1 . ASN B 2 148 ? 13.519 2.283 35.877 1.00 133.72 ? 148 ASN B OD1 1 ATOM 8344 N ND2 . ASN B 2 148 ? 11.646 1.204 35.267 1.00 121.20 ? 148 ASN B ND2 1 ATOM 8345 N N . LEU B 2 149 ? 12.958 4.847 38.744 1.00 111.74 ? 149 LEU B N 1 ATOM 8346 C CA . LEU B 2 149 ? 12.739 6.231 38.347 1.00 107.86 ? 149 LEU B CA 1 ATOM 8347 C C . LEU B 2 149 ? 14.037 6.799 37.777 1.00 102.79 ? 149 LEU B C 1 ATOM 8348 O O . LEU B 2 149 ? 15.122 6.316 38.099 1.00 108.49 ? 149 LEU B O 1 ATOM 8349 C CB . LEU B 2 149 ? 12.251 7.068 39.531 1.00 104.79 ? 149 LEU B CB 1 ATOM 8350 C CG . LEU B 2 149 ? 13.311 7.761 40.388 1.00 90.31 ? 149 LEU B CG 1 ATOM 8351 C CD1 . LEU B 2 149 ? 13.360 9.238 40.057 1.00 86.01 ? 149 LEU B CD1 1 ATOM 8352 C CD2 . LEU B 2 149 ? 13.037 7.553 41.865 1.00 91.47 ? 149 LEU B CD2 1 ATOM 8353 N N . ARG B 2 150 ? 13.927 7.814 36.925 1.00 88.64 ? 150 ARG B N 1 ATOM 8354 C CA . ARG B 2 150 ? 15.106 8.404 36.297 1.00 92.80 ? 150 ARG B CA 1 ATOM 8355 C C . ARG B 2 150 ? 15.129 9.919 36.441 1.00 96.70 ? 150 ARG B C 1 ATOM 8356 O O . ARG B 2 150 ? 14.154 10.600 36.120 1.00 104.86 ? 150 ARG B O 1 ATOM 8357 C CB . ARG B 2 150 ? 15.177 8.026 34.818 1.00 97.60 ? 150 ARG B CB 1 ATOM 8358 C CG . ARG B 2 150 ? 15.047 6.539 34.552 1.00 110.87 ? 150 ARG B CG 1 ATOM 8359 C CD . ARG B 2 150 ? 15.665 6.156 33.219 1.00 121.33 ? 150 ARG B CD 1 ATOM 8360 N NE . ARG B 2 150 ? 15.150 6.955 32.111 1.00 132.34 ? 150 ARG B NE 1 ATOM 8361 C CZ . ARG B 2 150 ? 15.514 6.790 30.844 1.00 130.21 ? 150 ARG B CZ 1 ATOM 8362 N NH1 . ARG B 2 150 ? 16.394 5.850 30.523 1.00 136.43 ? 150 ARG B NH1 1 ATOM 8363 N NH2 . ARG B 2 150 ? 14.999 7.561 29.896 1.00 113.39 ? 150 ARG B NH2 1 ATOM 8364 N N . ILE B 2 151 ? 16.245 10.438 36.939 1.00 95.16 ? 151 ILE B N 1 ATOM 8365 C CA . ILE B 2 151 ? 16.380 11.869 37.164 1.00 99.45 ? 151 ILE B CA 1 ATOM 8366 C C . ILE B 2 151 ? 17.318 12.538 36.158 1.00 101.65 ? 151 ILE B C 1 ATOM 8367 O O . ILE B 2 151 ? 17.942 11.872 35.334 1.00 93.85 ? 151 ILE B O 1 ATOM 8368 C CB . ILE B 2 151 ? 16.878 12.144 38.589 1.00 87.28 ? 151 ILE B CB 1 ATOM 8369 C CG1 . ILE B 2 151 ? 18.221 11.455 38.815 1.00 80.85 ? 151 ILE B CG1 1 ATOM 8370 C CG2 . ILE B 2 151 ? 15.871 11.640 39.605 1.00 86.53 ? 151 ILE B CG2 1 ATOM 8371 C CD1 . ILE B 2 151 ? 18.723 11.575 40.222 1.00 83.13 ? 151 ILE B CD1 1 ATOM 8372 N N . GLY B 2 152 ? 17.434 13.858 36.262 1.00 109.86 ? 152 GLY B N 1 ATOM 8373 C CA . GLY B 2 152 ? 18.225 14.651 35.336 1.00 106.77 ? 152 GLY B CA 1 ATOM 8374 C C . GLY B 2 152 ? 17.893 16.119 35.521 1.00 84.65 ? 152 GLY B C 1 ATOM 8375 O O . GLY B 2 152 ? 16.906 16.450 36.177 1.00 75.81 ? 152 GLY B O 1 ATOM 8376 N N . PHE B 2 153 ? 18.702 17.004 34.949 1.00 79.37 ? 153 PHE B N 1 ATOM 8377 C CA . PHE B 2 153 ? 18.499 18.430 35.176 1.00 79.04 ? 153 PHE B CA 1 ATOM 8378 C C . PHE B 2 153 ? 19.060 19.326 34.077 1.00 78.07 ? 153 PHE B C 1 ATOM 8379 O O . PHE B 2 153 ? 19.877 18.905 33.258 1.00 81.14 ? 153 PHE B O 1 ATOM 8380 C CB . PHE B 2 153 ? 19.109 18.836 36.521 1.00 84.41 ? 153 PHE B CB 1 ATOM 8381 C CG . PHE B 2 153 ? 20.611 18.857 36.531 1.00 88.92 ? 153 PHE B CG 1 ATOM 8382 C CD1 . PHE B 2 153 ? 21.301 20.051 36.399 1.00 85.61 ? 153 PHE B CD1 1 ATOM 8383 C CD2 . PHE B 2 153 ? 21.334 17.685 36.680 1.00 104.00 ? 153 PHE B CD2 1 ATOM 8384 C CE1 . PHE B 2 153 ? 22.681 20.077 36.411 1.00 106.47 ? 153 PHE B CE1 1 ATOM 8385 C CE2 . PHE B 2 153 ? 22.716 17.704 36.692 1.00 114.76 ? 153 PHE B CE2 1 ATOM 8386 C CZ . PHE B 2 153 ? 23.390 18.902 36.560 1.00 119.07 ? 153 PHE B CZ 1 ATOM 8387 N N . GLY B 2 154 ? 18.599 20.573 34.081 1.00 74.32 ? 154 GLY B N 1 ATOM 8388 C CA . GLY B 2 154 ? 19.085 21.600 33.182 1.00 72.46 ? 154 GLY B CA 1 ATOM 8389 C C . GLY B 2 154 ? 19.001 22.941 33.885 1.00 72.54 ? 154 GLY B C 1 ATOM 8390 O O . GLY B 2 154 ? 18.321 23.067 34.903 1.00 74.07 ? 154 GLY B O 1 ATOM 8391 N N . ALA B 2 155 ? 19.687 23.945 33.352 1.00 68.91 ? 155 ALA B N 1 ATOM 8392 C CA . ALA B 2 155 ? 19.748 25.241 34.016 1.00 67.50 ? 155 ALA B CA 1 ATOM 8393 C C . ALA B 2 155 ? 19.369 26.392 33.091 1.00 68.37 ? 155 ALA B C 1 ATOM 8394 O O . ALA B 2 155 ? 19.436 26.274 31.867 1.00 67.28 ? 155 ALA B O 1 ATOM 8395 C CB . ALA B 2 155 ? 21.136 25.467 34.589 1.00 64.87 ? 155 ALA B CB 1 ATOM 8396 N N . PHE B 2 156 ? 18.972 27.506 33.696 1.00 64.83 ? 156 PHE B N 1 ATOM 8397 C CA . PHE B 2 156 ? 18.622 28.714 32.960 1.00 62.67 ? 156 PHE B CA 1 ATOM 8398 C C . PHE B 2 156 ? 19.090 29.941 33.730 1.00 73.67 ? 156 PHE B C 1 ATOM 8399 O O . PHE B 2 156 ? 19.162 29.917 34.959 1.00 80.98 ? 156 PHE B O 1 ATOM 8400 C CB . PHE B 2 156 ? 17.112 28.787 32.719 1.00 59.86 ? 156 PHE B CB 1 ATOM 8401 C CG . PHE B 2 156 ? 16.299 28.870 33.984 1.00 62.81 ? 156 PHE B CG 1 ATOM 8402 C CD1 . PHE B 2 156 ? 16.017 30.097 34.567 1.00 57.43 ? 156 PHE B CD1 1 ATOM 8403 C CD2 . PHE B 2 156 ? 15.815 27.722 34.588 1.00 76.77 ? 156 PHE B CD2 1 ATOM 8404 C CE1 . PHE B 2 156 ? 15.276 30.175 35.729 1.00 54.39 ? 156 PHE B CE1 1 ATOM 8405 C CE2 . PHE B 2 156 ? 15.069 27.795 35.749 1.00 73.23 ? 156 PHE B CE2 1 ATOM 8406 C CZ . PHE B 2 156 ? 14.799 29.023 36.320 1.00 54.21 ? 156 PHE B CZ 1 ATOM 8407 N N . VAL B 2 157 ? 19.409 31.011 33.012 1.00 66.10 ? 157 VAL B N 1 ATOM 8408 C CA . VAL B 2 157 ? 19.721 32.281 33.656 1.00 60.32 ? 157 VAL B CA 1 ATOM 8409 C C . VAL B 2 157 ? 18.778 33.360 33.140 1.00 54.67 ? 157 VAL B C 1 ATOM 8410 O O . VAL B 2 157 ? 17.865 33.779 33.845 1.00 52.47 ? 157 VAL B O 1 ATOM 8411 C CB . VAL B 2 157 ? 21.181 32.706 33.418 1.00 62.41 ? 157 VAL B CB 1 ATOM 8412 C CG1 . VAL B 2 157 ? 21.454 34.053 34.071 1.00 65.23 ? 157 VAL B CG1 1 ATOM 8413 C CG2 . VAL B 2 157 ? 22.133 31.650 33.957 1.00 61.62 ? 157 VAL B CG2 1 ATOM 8414 N N . ASP B 2 158 ? 19.005 33.795 31.904 1.00 57.39 ? 158 ASP B N 1 ATOM 8415 C CA . ASP B 2 158 ? 18.140 34.761 31.234 1.00 55.35 ? 158 ASP B CA 1 ATOM 8416 C C . ASP B 2 158 ? 18.533 34.840 29.763 1.00 54.36 ? 158 ASP B C 1 ATOM 8417 O O . ASP B 2 158 ? 19.416 34.115 29.313 1.00 57.12 ? 158 ASP B O 1 ATOM 8418 C CB . ASP B 2 158 ? 18.233 36.142 31.891 1.00 62.33 ? 158 ASP B CB 1 ATOM 8419 C CG . ASP B 2 158 ? 16.937 36.927 31.788 1.00 57.89 ? 158 ASP B CG 1 ATOM 8420 O OD1 . ASP B 2 158 ? 16.153 36.660 30.850 1.00 48.48 ? 158 ASP B OD1 1 ATOM 8421 O OD2 . ASP B 2 158 ? 16.704 37.808 32.648 1.00 58.14 ? 158 ASP B OD2 1 ATOM 8422 N N . LYS B 2 159 ? 17.881 35.719 29.014 1.00 52.34 ? 159 LYS B N 1 ATOM 8423 C CA . LYS B 2 159 ? 18.221 35.896 27.610 1.00 53.13 ? 159 LYS B CA 1 ATOM 8424 C C . LYS B 2 159 ? 19.536 36.669 27.468 1.00 57.91 ? 159 LYS B C 1 ATOM 8425 O O . LYS B 2 159 ? 19.655 37.798 27.943 1.00 65.70 ? 159 LYS B O 1 ATOM 8426 C CB . LYS B 2 159 ? 17.085 36.611 26.873 1.00 49.76 ? 159 LYS B CB 1 ATOM 8427 C CG . LYS B 2 159 ? 15.830 35.767 26.680 1.00 47.94 ? 159 LYS B CG 1 ATOM 8428 C CD . LYS B 2 159 ? 14.780 36.525 25.880 1.00 51.39 ? 159 LYS B CD 1 ATOM 8429 C CE . LYS B 2 159 ? 13.552 35.669 25.610 1.00 50.52 ? 159 LYS B CE 1 ATOM 8430 N NZ . LYS B 2 159 ? 13.885 34.444 24.835 1.00 67.16 ? 159 LYS B NZ 1 ATOM 8431 N N . PRO B 2 160 ? 20.535 36.047 26.818 1.00 59.65 ? 160 PRO B N 1 ATOM 8432 C CA . PRO B 2 160 ? 21.870 36.615 26.584 1.00 64.11 ? 160 PRO B CA 1 ATOM 8433 C C . PRO B 2 160 ? 21.875 37.662 25.455 1.00 75.54 ? 160 PRO B C 1 ATOM 8434 O O . PRO B 2 160 ? 22.379 37.401 24.365 1.00 97.12 ? 160 PRO B O 1 ATOM 8435 C CB . PRO B 2 160 ? 22.699 35.387 26.198 1.00 62.12 ? 160 PRO B CB 1 ATOM 8436 C CG . PRO B 2 160 ? 21.719 34.485 25.527 1.00 65.64 ? 160 PRO B CG 1 ATOM 8437 C CD . PRO B 2 160 ? 20.410 34.691 26.251 1.00 60.32 ? 160 PRO B CD 1 ATOM 8438 N N . VAL B 2 161 ? 21.296 38.806 25.775 1.00 67.70 ? 161 VAL B N 1 ATOM 8439 C CA . VAL B 2 161 ? 21.247 39.937 24.901 1.00 68.42 ? 161 VAL B CA 1 ATOM 8440 C C . VAL B 2 161 ? 21.004 41.139 25.765 1.00 88.84 ? 161 VAL B C 1 ATOM 8441 O O . VAL B 2 161 ? 21.389 41.141 26.896 1.00 100.41 ? 161 VAL B O 1 ATOM 8442 C CB . VAL B 2 161 ? 20.111 39.803 23.939 1.00 63.70 ? 161 VAL B CB 1 ATOM 8443 C CG1 . VAL B 2 161 ? 20.139 38.420 23.366 1.00 70.22 ? 161 VAL B CG1 1 ATOM 8444 C CG2 . VAL B 2 161 ? 18.824 40.023 24.675 1.00 73.54 ? 161 VAL B CG2 1 ATOM 8445 N N . SER B 2 162 ? 20.370 42.152 25.179 1.00 96.46 ? 162 SER B N 1 ATOM 8446 C CA . SER B 2 162 ? 20.128 43.448 25.810 1.00 83.11 ? 162 SER B CA 1 ATOM 8447 C C . SER B 2 162 ? 20.079 43.423 27.337 1.00 62.66 ? 162 SER B C 1 ATOM 8448 O O . SER B 2 162 ? 20.372 42.406 27.965 1.00 66.48 ? 162 SER B O 1 ATOM 8449 C CB . SER B 2 162 ? 18.843 44.069 25.254 1.00 86.92 ? 162 SER B CB 1 ATOM 8450 O OG . SER B 2 162 ? 18.900 44.182 23.843 1.00 94.63 ? 162 SER B OG 1 ATOM 8451 N N . PRO B 2 163 ? 19.708 44.561 27.921 1.00 59.23 ? 163 PRO B N 1 ATOM 8452 C CA . PRO B 2 163 ? 19.660 44.704 29.380 1.00 57.81 ? 163 PRO B CA 1 ATOM 8453 C C . PRO B 2 163 ? 19.947 43.385 30.081 1.00 55.39 ? 163 PRO B C 1 ATOM 8454 O O . PRO B 2 163 ? 21.018 43.220 30.665 1.00 64.79 ? 163 PRO B O 1 ATOM 8455 C CB . PRO B 2 163 ? 18.214 45.148 29.650 1.00 53.98 ? 163 PRO B CB 1 ATOM 8456 C CG . PRO B 2 163 ? 17.471 44.931 28.371 1.00 51.05 ? 163 PRO B CG 1 ATOM 8457 C CD . PRO B 2 163 ? 18.490 45.085 27.286 1.00 52.71 ? 163 PRO B CD 1 ATOM 8458 N N . TYR B 2 164 ? 18.999 42.457 30.021 1.00 53.02 ? 164 TYR B N 1 ATOM 8459 C CA . TYR B 2 164 ? 19.186 41.190 30.618 1.00 52.68 ? 164 TYR B CA 1 ATOM 8460 C C . TYR B 2 164 ? 20.633 40.914 30.949 1.00 56.67 ? 164 TYR B C 1 ATOM 8461 O O . TYR B 2 164 ? 20.941 40.633 32.084 1.00 72.29 ? 164 TYR B O 1 ATOM 8462 C CB . TYR B 2 164 ? 18.586 40.183 29.683 1.00 53.87 ? 164 TYR B CB 1 ATOM 8463 C CG . TYR B 2 164 ? 17.180 40.561 29.344 1.00 48.24 ? 164 TYR B CG 1 ATOM 8464 C CD1 . TYR B 2 164 ? 16.663 40.338 28.110 1.00 46.50 ? 164 TYR B CD1 1 ATOM 8465 C CD2 . TYR B 2 164 ? 16.385 41.157 30.264 1.00 47.11 ? 164 TYR B CD2 1 ATOM 8466 C CE1 . TYR B 2 164 ? 15.380 40.679 27.806 1.00 43.80 ? 164 TYR B CE1 1 ATOM 8467 C CE2 . TYR B 2 164 ? 15.104 41.505 29.962 1.00 51.52 ? 164 TYR B CE2 1 ATOM 8468 C CZ . TYR B 2 164 ? 14.616 41.260 28.726 1.00 46.69 ? 164 TYR B CZ 1 ATOM 8469 O OH . TYR B 2 164 ? 13.341 41.610 28.425 1.00 52.00 ? 164 TYR B OH 1 ATOM 8470 N N . MET B 2 165 ? 21.528 40.994 29.978 1.00 58.76 ? 165 MET B N 1 ATOM 8471 C CA . MET B 2 165 ? 22.919 40.624 30.226 1.00 67.70 ? 165 MET B CA 1 ATOM 8472 C C . MET B 2 165 ? 23.824 41.845 30.320 1.00 67.74 ? 165 MET B C 1 ATOM 8473 O O . MET B 2 165 ? 23.386 42.968 30.070 1.00 71.73 ? 165 MET B O 1 ATOM 8474 C CB . MET B 2 165 ? 23.408 39.680 29.122 1.00 75.79 ? 165 MET B CB 1 ATOM 8475 C CG . MET B 2 165 ? 24.249 40.309 28.038 1.00 88.09 ? 165 MET B CG 1 ATOM 8476 S SD . MET B 2 165 ? 25.564 39.181 27.545 1.00 110.76 ? 165 MET B SD 1 ATOM 8477 C CE . MET B 2 165 ? 25.072 38.801 25.868 1.00 74.81 ? 165 MET B CE 1 ATOM 8478 N N . TYR B 2 166 ? 25.091 41.612 30.656 1.00 70.01 ? 166 TYR B N 1 ATOM 8479 C CA . TYR B 2 166 ? 26.081 42.674 30.745 1.00 71.73 ? 166 TYR B CA 1 ATOM 8480 C C . TYR B 2 166 ? 26.848 42.825 29.434 1.00 80.53 ? 166 TYR B C 1 ATOM 8481 O O . TYR B 2 166 ? 27.641 41.963 29.057 1.00 79.17 ? 166 TYR B O 1 ATOM 8482 C CB . TYR B 2 166 ? 27.056 42.399 31.894 1.00 70.33 ? 166 TYR B CB 1 ATOM 8483 C CG . TYR B 2 166 ? 26.476 42.639 33.272 1.00 68.76 ? 166 TYR B CG 1 ATOM 8484 C CD1 . TYR B 2 166 ? 26.747 43.812 33.964 1.00 64.19 ? 166 TYR B CD1 1 ATOM 8485 C CD2 . TYR B 2 166 ? 25.659 41.695 33.881 1.00 72.62 ? 166 TYR B CD2 1 ATOM 8486 C CE1 . TYR B 2 166 ? 26.221 44.039 35.223 1.00 61.37 ? 166 TYR B CE1 1 ATOM 8487 C CE2 . TYR B 2 166 ? 25.127 41.914 35.140 1.00 69.35 ? 166 TYR B CE2 1 ATOM 8488 C CZ . TYR B 2 166 ? 25.412 43.087 35.805 1.00 60.47 ? 166 TYR B CZ 1 ATOM 8489 O OH . TYR B 2 166 ? 24.887 43.311 37.057 1.00 60.81 ? 166 TYR B OH 1 ATOM 8490 N N . ILE B 2 167 ? 26.595 43.933 28.747 1.00 90.23 ? 167 ILE B N 1 ATOM 8491 C CA . ILE B 2 167 ? 27.326 44.298 27.541 1.00 87.59 ? 167 ILE B CA 1 ATOM 8492 C C . ILE B 2 167 ? 28.460 45.247 27.910 1.00 105.63 ? 167 ILE B C 1 ATOM 8493 O O . ILE B 2 167 ? 29.130 45.805 27.042 1.00 116.46 ? 167 ILE B O 1 ATOM 8494 C CB . ILE B 2 167 ? 26.408 44.939 26.488 1.00 85.69 ? 167 ILE B CB 1 ATOM 8495 C CG1 . ILE B 2 167 ? 25.402 45.875 27.158 1.00 97.12 ? 167 ILE B CG1 1 ATOM 8496 C CG2 . ILE B 2 167 ? 25.678 43.862 25.700 1.00 86.55 ? 167 ILE B CG2 1 ATOM 8497 C CD1 . ILE B 2 167 ? 24.361 46.427 26.210 1.00 105.91 ? 167 ILE B CD1 1 ATOM 8498 N N . SER B 2 168 ? 28.651 45.420 29.216 1.00 114.01 ? 168 SER B N 1 ATOM 8499 C CA . SER B 2 168 ? 29.654 46.312 29.797 1.00 104.93 ? 168 SER B CA 1 ATOM 8500 C C . SER B 2 168 ? 31.076 45.869 29.383 1.00 94.81 ? 168 SER B C 1 ATOM 8501 O O . SER B 2 168 ? 31.200 44.919 28.611 1.00 108.19 ? 168 SER B O 1 ATOM 8502 C CB . SER B 2 168 ? 29.468 46.326 31.320 1.00 110.48 ? 168 SER B CB 1 ATOM 8503 O OG . SER B 2 168 ? 29.909 45.115 31.902 1.00 117.29 ? 168 SER B OG 1 ATOM 8504 N N . PRO B 2 169 ? 32.148 46.544 29.875 1.00 90.73 ? 169 PRO B N 1 ATOM 8505 C CA . PRO B 2 169 ? 33.494 46.225 29.373 1.00 92.90 ? 169 PRO B CA 1 ATOM 8506 C C . PRO B 2 169 ? 33.820 44.732 29.270 1.00 91.07 ? 169 PRO B C 1 ATOM 8507 O O . PRO B 2 169 ? 33.406 43.954 30.127 1.00 90.14 ? 169 PRO B O 1 ATOM 8508 C CB . PRO B 2 169 ? 34.417 46.893 30.411 1.00 101.69 ? 169 PRO B CB 1 ATOM 8509 C CG . PRO B 2 169 ? 33.507 47.676 31.349 1.00 107.98 ? 169 PRO B CG 1 ATOM 8510 C CD . PRO B 2 169 ? 32.199 47.795 30.650 1.00 107.04 ? 169 PRO B CD 1 ATOM 8511 N N . PRO B 2 170 ? 34.565 44.351 28.216 1.00 95.94 ? 170 PRO B N 1 ATOM 8512 C CA . PRO B 2 170 ? 34.743 42.983 27.710 1.00 107.77 ? 170 PRO B CA 1 ATOM 8513 C C . PRO B 2 170 ? 35.045 41.918 28.763 1.00 112.67 ? 170 PRO B C 1 ATOM 8514 O O . PRO B 2 170 ? 34.649 40.768 28.572 1.00 107.38 ? 170 PRO B O 1 ATOM 8515 C CB . PRO B 2 170 ? 35.929 43.129 26.756 1.00 115.09 ? 170 PRO B CB 1 ATOM 8516 C CG . PRO B 2 170 ? 35.798 44.508 26.235 1.00 107.58 ? 170 PRO B CG 1 ATOM 8517 C CD . PRO B 2 170 ? 35.296 45.330 27.391 1.00 96.94 ? 170 PRO B CD 1 ATOM 8518 N N . GLU B 2 171 ? 35.726 42.280 29.844 1.00 119.15 ? 171 GLU B N 1 ATOM 8519 C CA . GLU B 2 171 ? 36.043 41.304 30.881 1.00 118.40 ? 171 GLU B CA 1 ATOM 8520 C C . GLU B 2 171 ? 34.778 40.860 31.613 1.00 107.85 ? 171 GLU B C 1 ATOM 8521 O O . GLU B 2 171 ? 34.780 39.848 32.313 1.00 117.34 ? 171 GLU B O 1 ATOM 8522 C CB . GLU B 2 171 ? 37.059 41.871 31.875 1.00 127.53 ? 171 GLU B CB 1 ATOM 8523 C CG . GLU B 2 171 ? 36.449 42.681 33.005 1.00 140.39 ? 171 GLU B CG 1 ATOM 8524 C CD . GLU B 2 171 ? 35.879 44.004 32.540 1.00 159.08 ? 171 GLU B CD 1 ATOM 8525 O OE1 . GLU B 2 171 ? 36.355 44.530 31.513 1.00 159.27 ? 171 GLU B OE1 1 ATOM 8526 O OE2 . GLU B 2 171 ? 34.953 44.517 33.203 1.00 171.67 ? 171 GLU B OE2 1 ATOM 8527 N N . ALA B 2 172 ? 33.699 41.620 31.445 1.00 100.21 ? 172 ALA B N 1 ATOM 8528 C CA . ALA B 2 172 ? 32.418 41.271 32.046 1.00 98.56 ? 172 ALA B CA 1 ATOM 8529 C C . ALA B 2 172 ? 31.613 40.338 31.146 1.00 92.81 ? 172 ALA B C 1 ATOM 8530 O O . ALA B 2 172 ? 30.614 39.761 31.572 1.00 89.71 ? 172 ALA B O 1 ATOM 8531 C CB . ALA B 2 172 ? 31.620 42.521 32.358 1.00 95.63 ? 172 ALA B CB 1 ATOM 8532 N N . LEU B 2 173 ? 32.046 40.196 29.899 1.00 91.33 ? 173 LEU B N 1 ATOM 8533 C CA . LEU B 2 173 ? 31.422 39.242 28.990 1.00 89.75 ? 173 LEU B CA 1 ATOM 8534 C C . LEU B 2 173 ? 31.765 37.823 29.422 1.00 98.21 ? 173 LEU B C 1 ATOM 8535 O O . LEU B 2 173 ? 30.883 36.982 29.595 1.00 98.69 ? 173 LEU B O 1 ATOM 8536 C CB . LEU B 2 173 ? 31.870 39.486 27.549 1.00 93.22 ? 173 LEU B CB 1 ATOM 8537 C CG . LEU B 2 173 ? 31.327 40.749 26.878 1.00 102.07 ? 173 LEU B CG 1 ATOM 8538 C CD1 . LEU B 2 173 ? 31.960 40.944 25.510 1.00 110.91 ? 173 LEU B CD1 1 ATOM 8539 C CD2 . LEU B 2 173 ? 29.812 40.679 26.765 1.00 98.36 ? 173 LEU B CD2 1 ATOM 8540 N N . GLU B 2 174 ? 33.057 37.570 29.601 1.00 105.48 ? 174 GLU B N 1 ATOM 8541 C CA . GLU B 2 174 ? 33.529 36.274 30.068 1.00 104.06 ? 174 GLU B CA 1 ATOM 8542 C C . GLU B 2 174 ? 33.225 36.098 31.552 1.00 91.85 ? 174 GLU B C 1 ATOM 8543 O O . GLU B 2 174 ? 32.917 34.997 32.009 1.00 90.68 ? 174 GLU B O 1 ATOM 8544 C CB . GLU B 2 174 ? 35.031 36.125 29.809 1.00 112.60 ? 174 GLU B CB 1 ATOM 8545 C CG . GLU B 2 174 ? 35.612 34.790 30.246 1.00 123.71 ? 174 GLU B CG 1 ATOM 8546 C CD . GLU B 2 174 ? 34.998 33.616 29.508 1.00 128.73 ? 174 GLU B CD 1 ATOM 8547 O OE1 . GLU B 2 174 ? 34.614 33.784 28.331 1.00 125.64 ? 174 GLU B OE1 1 ATOM 8548 O OE2 . GLU B 2 174 ? 34.897 32.525 30.107 1.00 131.74 ? 174 GLU B OE2 1 ATOM 8549 N N . ASN B 2 175 ? 33.310 37.195 32.296 1.00 88.74 ? 175 ASN B N 1 ATOM 8550 C CA . ASN B 2 175 ? 33.055 37.172 33.731 1.00 87.23 ? 175 ASN B CA 1 ATOM 8551 C C . ASN B 2 175 ? 32.112 38.292 34.160 1.00 83.16 ? 175 ASN B C 1 ATOM 8552 O O . ASN B 2 175 ? 32.562 39.380 34.516 1.00 81.05 ? 175 ASN B O 1 ATOM 8553 C CB . ASN B 2 175 ? 34.372 37.271 34.504 1.00 95.25 ? 175 ASN B CB 1 ATOM 8554 C CG . ASN B 2 175 ? 34.174 37.227 36.007 1.00 106.48 ? 175 ASN B CG 1 ATOM 8555 O OD1 . ASN B 2 175 ? 33.177 36.703 36.501 1.00 95.73 ? 175 ASN B OD1 1 ATOM 8556 N ND2 . ASN B 2 175 ? 35.127 37.788 36.744 1.00 126.99 ? 175 ASN B ND2 1 ATOM 8557 N N . PRO B 2 176 ? 30.796 38.016 34.149 1.00 79.56 ? 176 PRO B N 1 ATOM 8558 C CA . PRO B 2 176 ? 29.731 38.967 34.495 1.00 75.51 ? 176 PRO B CA 1 ATOM 8559 C C . PRO B 2 176 ? 29.962 39.660 35.832 1.00 75.24 ? 176 PRO B C 1 ATOM 8560 O O . PRO B 2 176 ? 29.407 40.732 36.074 1.00 75.16 ? 176 PRO B O 1 ATOM 8561 C CB . PRO B 2 176 ? 28.484 38.085 34.549 1.00 71.73 ? 176 PRO B CB 1 ATOM 8562 C CG . PRO B 2 176 ? 28.771 37.005 33.580 1.00 73.69 ? 176 PRO B CG 1 ATOM 8563 C CD . PRO B 2 176 ? 30.243 36.718 33.727 1.00 85.77 ? 176 PRO B CD 1 ATOM 8564 N N . CYS B 2 177 ? 30.772 39.050 36.689 1.00 74.15 ? 177 CYS B N 1 ATOM 8565 C CA . CYS B 2 177 ? 31.172 39.704 37.920 1.00 76.02 ? 177 CYS B CA 1 ATOM 8566 C C . CYS B 2 177 ? 32.573 40.286 37.763 1.00 105.21 ? 177 CYS B C 1 ATOM 8567 O O . CYS B 2 177 ? 33.565 39.563 37.714 1.00 112.95 ? 177 CYS B O 1 ATOM 8568 C CB . CYS B 2 177 ? 31.126 38.724 39.094 1.00 77.07 ? 177 CYS B CB 1 ATOM 8569 S SG . CYS B 2 177 ? 29.552 37.854 39.286 1.00 101.18 ? 177 CYS B SG 1 ATOM 8570 N N . TYR B 2 178 ? 32.629 41.608 37.669 1.00 101.62 ? 178 TYR B N 1 ATOM 8571 C CA . TYR B 2 178 ? 33.870 42.363 37.737 1.00 101.56 ? 178 TYR B CA 1 ATOM 8572 C C . TYR B 2 178 ? 33.677 43.305 38.906 1.00 114.57 ? 178 TYR B C 1 ATOM 8573 O O . TYR B 2 178 ? 34.436 43.296 39.874 1.00 139.53 ? 178 TYR B O 1 ATOM 8574 C CB . TYR B 2 178 ? 34.167 43.117 36.441 1.00 101.40 ? 178 TYR B CB 1 ATOM 8575 C CG . TYR B 2 178 ? 35.547 43.737 36.418 1.00 121.54 ? 178 TYR B CG 1 ATOM 8576 C CD1 . TYR B 2 178 ? 36.685 42.942 36.463 1.00 134.08 ? 178 TYR B CD1 1 ATOM 8577 C CD2 . TYR B 2 178 ? 35.714 45.115 36.355 1.00 121.35 ? 178 TYR B CD2 1 ATOM 8578 C CE1 . TYR B 2 178 ? 37.950 43.498 36.444 1.00 139.57 ? 178 TYR B CE1 1 ATOM 8579 C CE2 . TYR B 2 178 ? 36.977 45.682 36.336 1.00 125.21 ? 178 TYR B CE2 1 ATOM 8580 C CZ . TYR B 2 178 ? 38.091 44.868 36.381 1.00 135.42 ? 178 TYR B CZ 1 ATOM 8581 O OH . TYR B 2 178 ? 39.350 45.423 36.363 1.00 138.04 ? 178 TYR B OH 1 ATOM 8582 N N . ASP B 2 179 ? 32.643 44.130 38.782 1.00 98.31 ? 179 ASP B N 1 ATOM 8583 C CA . ASP B 2 179 ? 32.071 44.836 39.916 1.00 101.25 ? 179 ASP B CA 1 ATOM 8584 C C . ASP B 2 179 ? 31.715 43.811 40.992 1.00 113.69 ? 179 ASP B C 1 ATOM 8585 O O . ASP B 2 179 ? 31.400 42.664 40.666 1.00 116.41 ? 179 ASP B O 1 ATOM 8586 C CB . ASP B 2 179 ? 30.836 45.631 39.481 1.00 96.97 ? 179 ASP B CB 1 ATOM 8587 C CG . ASP B 2 179 ? 30.027 46.151 40.652 1.00 116.50 ? 179 ASP B CG 1 ATOM 8588 O OD1 . ASP B 2 179 ? 28.781 46.134 40.566 1.00 108.36 ? 179 ASP B OD1 1 ATOM 8589 O OD2 . ASP B 2 179 ? 30.634 46.582 41.655 1.00 137.68 ? 179 ASP B OD2 1 ATOM 8590 N N . MET B 2 180 ? 31.808 44.237 42.255 1.00 120.65 ? 180 MET B N 1 ATOM 8591 C CA . MET B 2 180 ? 31.610 43.411 43.459 1.00 122.23 ? 180 MET B CA 1 ATOM 8592 C C . MET B 2 180 ? 32.882 42.641 43.816 1.00 127.88 ? 180 MET B C 1 ATOM 8593 O O . MET B 2 180 ? 32.915 41.921 44.815 1.00 138.01 ? 180 MET B O 1 ATOM 8594 C CB . MET B 2 180 ? 30.428 42.440 43.317 1.00 110.69 ? 180 MET B CB 1 ATOM 8595 C CG . MET B 2 180 ? 29.096 43.107 43.006 1.00 102.30 ? 180 MET B CG 1 ATOM 8596 S SD . MET B 2 180 ? 27.765 41.917 42.756 1.00 120.49 ? 180 MET B SD 1 ATOM 8597 C CE . MET B 2 180 ? 27.637 41.206 44.394 1.00 79.01 ? 180 MET B CE 1 ATOM 8598 N N . LYS B 2 181 ? 33.914 42.788 42.986 1.00 120.67 ? 181 LYS B N 1 ATOM 8599 C CA . LYS B 2 181 ? 35.234 42.210 43.247 1.00 131.78 ? 181 LYS B CA 1 ATOM 8600 C C . LYS B 2 181 ? 35.190 40.691 43.390 1.00 131.10 ? 181 LYS B C 1 ATOM 8601 O O . LYS B 2 181 ? 35.931 40.110 44.185 1.00 137.15 ? 181 LYS B O 1 ATOM 8602 C CB . LYS B 2 181 ? 35.851 42.831 44.506 1.00 137.54 ? 181 LYS B CB 1 ATOM 8603 C CG . LYS B 2 181 ? 36.085 44.331 44.420 1.00 133.85 ? 181 LYS B CG 1 ATOM 8604 C CD . LYS B 2 181 ? 37.160 44.668 43.400 1.00 134.92 ? 181 LYS B CD 1 ATOM 8605 C CE . LYS B 2 181 ? 37.450 46.160 43.379 1.00 137.60 ? 181 LYS B CE 1 ATOM 8606 N NZ . LYS B 2 181 ? 37.922 46.653 44.702 1.00 142.75 ? 181 LYS B NZ 1 ATOM 8607 N N . THR B 2 182 ? 34.319 40.054 42.617 1.00 115.22 ? 182 THR B N 1 ATOM 8608 C CA . THR B 2 182 ? 34.175 38.604 42.641 1.00 111.02 ? 182 THR B CA 1 ATOM 8609 C C . THR B 2 182 ? 34.163 38.056 41.220 1.00 105.86 ? 182 THR B C 1 ATOM 8610 O O . THR B 2 182 ? 34.079 38.818 40.261 1.00 105.98 ? 182 THR B O 1 ATOM 8611 C CB . THR B 2 182 ? 32.890 38.170 43.368 1.00 120.47 ? 182 THR B CB 1 ATOM 8612 O OG1 . THR B 2 182 ? 31.768 38.875 42.822 1.00 130.34 ? 182 THR B OG1 1 ATOM 8613 C CG2 . THR B 2 182 ? 32.992 38.467 44.857 1.00 122.35 ? 182 THR B CG2 1 ATOM 8614 N N . THR B 2 183 ? 34.269 36.738 41.086 1.00 102.27 ? 183 THR B N 1 ATOM 8615 C CA . THR B 2 183 ? 34.234 36.105 39.771 1.00 99.71 ? 183 THR B CA 1 ATOM 8616 C C . THR B 2 183 ? 33.127 35.060 39.683 1.00 95.52 ? 183 THR B C 1 ATOM 8617 O O . THR B 2 183 ? 33.038 34.167 40.525 1.00 98.94 ? 183 THR B O 1 ATOM 8618 C CB . THR B 2 183 ? 35.578 35.435 39.428 1.00 103.50 ? 183 THR B CB 1 ATOM 8619 O OG1 . THR B 2 183 ? 35.859 34.404 40.382 1.00 118.55 ? 183 THR B OG1 1 ATOM 8620 C CG2 . THR B 2 183 ? 36.706 36.457 39.441 1.00 106.04 ? 183 THR B CG2 1 ATOM 8621 N N . CYS B 2 184 ? 32.286 35.179 38.661 1.00 94.70 ? 184 CYS B N 1 ATOM 8622 C CA . CYS B 2 184 ? 31.228 34.202 38.422 1.00 88.53 ? 184 CYS B CA 1 ATOM 8623 C C . CYS B 2 184 ? 31.228 33.747 36.965 1.00 83.04 ? 184 CYS B C 1 ATOM 8624 O O . CYS B 2 184 ? 32.089 34.142 36.180 1.00 91.24 ? 184 CYS B O 1 ATOM 8625 C CB . CYS B 2 184 ? 29.861 34.778 38.802 1.00 85.42 ? 184 CYS B CB 1 ATOM 8626 S SG . CYS B 2 184 ? 29.422 36.318 37.962 1.00 102.35 ? 184 CYS B SG 1 ATOM 8627 N N . LEU B 2 185 ? 30.256 32.915 36.610 1.00 78.91 ? 185 LEU B N 1 ATOM 8628 C CA . LEU B 2 185 ? 30.199 32.318 35.280 1.00 79.77 ? 185 LEU B CA 1 ATOM 8629 C C . LEU B 2 185 ? 29.449 33.205 34.287 1.00 76.66 ? 185 LEU B C 1 ATOM 8630 O O . LEU B 2 185 ? 28.593 33.993 34.684 1.00 92.61 ? 185 LEU B O 1 ATOM 8631 C CB . LEU B 2 185 ? 29.540 30.935 35.350 1.00 81.22 ? 185 LEU B CB 1 ATOM 8632 C CG . LEU B 2 185 ? 30.412 29.734 35.735 1.00 87.21 ? 185 LEU B CG 1 ATOM 8633 C CD1 . LEU B 2 185 ? 31.549 29.551 34.740 1.00 99.12 ? 185 LEU B CD1 1 ATOM 8634 C CD2 . LEU B 2 185 ? 30.952 29.852 37.155 1.00 90.45 ? 185 LEU B CD2 1 ATOM 8635 N N . PRO B 2 186 ? 29.780 33.085 32.989 1.00 77.50 ? 186 PRO B N 1 ATOM 8636 C CA . PRO B 2 186 ? 29.052 33.801 31.935 1.00 74.80 ? 186 PRO B CA 1 ATOM 8637 C C . PRO B 2 186 ? 27.628 33.278 31.773 1.00 72.30 ? 186 PRO B C 1 ATOM 8638 O O . PRO B 2 186 ? 27.417 32.065 31.760 1.00 79.19 ? 186 PRO B O 1 ATOM 8639 C CB . PRO B 2 186 ? 29.886 33.527 30.680 1.00 78.47 ? 186 PRO B CB 1 ATOM 8640 C CG . PRO B 2 186 ? 30.607 32.260 30.978 1.00 86.32 ? 186 PRO B CG 1 ATOM 8641 C CD . PRO B 2 186 ? 30.911 32.313 32.444 1.00 85.50 ? 186 PRO B CD 1 ATOM 8642 N N . MET B 2 187 ? 26.667 34.187 31.653 1.00 69.26 ? 187 MET B N 1 ATOM 8643 C CA . MET B 2 187 ? 25.259 33.805 31.616 1.00 67.85 ? 187 MET B CA 1 ATOM 8644 C C . MET B 2 187 ? 24.828 33.206 30.286 1.00 68.51 ? 187 MET B C 1 ATOM 8645 O O . MET B 2 187 ? 25.492 33.367 29.262 1.00 65.07 ? 187 MET B O 1 ATOM 8646 C CB . MET B 2 187 ? 24.370 34.998 31.955 1.00 75.31 ? 187 MET B CB 1 ATOM 8647 C CG . MET B 2 187 ? 24.373 36.109 30.935 1.00 76.04 ? 187 MET B CG 1 ATOM 8648 S SD . MET B 2 187 ? 22.928 37.146 31.195 1.00 68.69 ? 187 MET B SD 1 ATOM 8649 C CE . MET B 2 187 ? 21.655 36.138 30.448 1.00 54.48 ? 187 MET B CE 1 ATOM 8650 N N . PHE B 2 188 ? 23.701 32.505 30.328 1.00 67.42 ? 188 PHE B N 1 ATOM 8651 C CA . PHE B 2 188 ? 23.187 31.779 29.180 1.00 66.90 ? 188 PHE B CA 1 ATOM 8652 C C . PHE B 2 188 ? 21.667 31.694 29.235 1.00 64.43 ? 188 PHE B C 1 ATOM 8653 O O . PHE B 2 188 ? 21.047 32.152 30.194 1.00 62.93 ? 188 PHE B O 1 ATOM 8654 C CB . PHE B 2 188 ? 23.794 30.378 29.142 1.00 69.50 ? 188 PHE B CB 1 ATOM 8655 C CG . PHE B 2 188 ? 23.913 29.738 30.499 1.00 69.12 ? 188 PHE B CG 1 ATOM 8656 C CD1 . PHE B 2 188 ? 22.833 29.085 31.069 1.00 64.66 ? 188 PHE B CD1 1 ATOM 8657 C CD2 . PHE B 2 188 ? 25.101 29.798 31.208 1.00 87.21 ? 188 PHE B CD2 1 ATOM 8658 C CE1 . PHE B 2 188 ? 22.935 28.501 32.316 1.00 64.42 ? 188 PHE B CE1 1 ATOM 8659 C CE2 . PHE B 2 188 ? 25.210 29.214 32.458 1.00 89.85 ? 188 PHE B CE2 1 ATOM 8660 C CZ . PHE B 2 188 ? 24.124 28.565 33.011 1.00 71.37 ? 188 PHE B CZ 1 ATOM 8661 N N . GLY B 2 189 ? 21.074 31.085 28.215 1.00 65.30 ? 189 GLY B N 1 ATOM 8662 C CA . GLY B 2 189 ? 19.645 30.833 28.195 1.00 62.36 ? 189 GLY B CA 1 ATOM 8663 C C . GLY B 2 189 ? 19.398 29.521 28.908 1.00 64.29 ? 189 GLY B C 1 ATOM 8664 O O . GLY B 2 189 ? 20.103 29.195 29.859 1.00 73.59 ? 189 GLY B O 1 ATOM 8665 N N . TYR B 2 190 ? 18.384 28.775 28.488 1.00 70.05 ? 190 TYR B N 1 ATOM 8666 C CA . TYR B 2 190 ? 18.232 27.422 29.001 1.00 62.01 ? 190 TYR B CA 1 ATOM 8667 C C . TYR B 2 190 ? 19.411 26.569 28.549 1.00 63.09 ? 190 TYR B C 1 ATOM 8668 O O . TYR B 2 190 ? 19.812 26.616 27.386 1.00 63.94 ? 190 TYR B O 1 ATOM 8669 C CB . TYR B 2 190 ? 16.922 26.788 28.541 1.00 59.18 ? 190 TYR B CB 1 ATOM 8670 C CG . TYR B 2 190 ? 16.905 25.289 28.732 1.00 59.35 ? 190 TYR B CG 1 ATOM 8671 C CD1 . TYR B 2 190 ? 16.974 24.732 30.003 1.00 64.60 ? 190 TYR B CD1 1 ATOM 8672 C CD2 . TYR B 2 190 ? 16.834 24.430 27.644 1.00 61.32 ? 190 TYR B CD2 1 ATOM 8673 C CE1 . TYR B 2 190 ? 16.968 23.364 30.184 1.00 72.96 ? 190 TYR B CE1 1 ATOM 8674 C CE2 . TYR B 2 190 ? 16.826 23.059 27.816 1.00 62.22 ? 190 TYR B CE2 1 ATOM 8675 C CZ . TYR B 2 190 ? 16.892 22.533 29.089 1.00 71.47 ? 190 TYR B CZ 1 ATOM 8676 O OH . TYR B 2 190 ? 16.885 21.170 29.269 1.00 85.37 ? 190 TYR B OH 1 ATOM 8677 N N . LYS B 2 191 ? 19.968 25.795 29.474 1.00 68.78 ? 191 LYS B N 1 ATOM 8678 C CA . LYS B 2 191 ? 21.083 24.913 29.158 1.00 82.31 ? 191 LYS B CA 1 ATOM 8679 C C . LYS B 2 191 ? 20.828 23.500 29.671 1.00 87.03 ? 191 LYS B C 1 ATOM 8680 O O . LYS B 2 191 ? 20.716 23.279 30.876 1.00 89.28 ? 191 LYS B O 1 ATOM 8681 C CB . LYS B 2 191 ? 22.386 25.457 29.750 1.00 77.94 ? 191 LYS B CB 1 ATOM 8682 C CG . LYS B 2 191 ? 23.592 24.559 29.517 1.00 76.62 ? 191 LYS B CG 1 ATOM 8683 C CD . LYS B 2 191 ? 24.827 25.075 30.241 1.00 80.03 ? 191 LYS B CD 1 ATOM 8684 C CE . LYS B 2 191 ? 25.233 26.451 29.742 1.00 84.66 ? 191 LYS B CE 1 ATOM 8685 N NZ . LYS B 2 191 ? 26.495 26.922 30.379 1.00 92.41 ? 191 LYS B NZ 1 ATOM 8686 N N . HIS B 2 192 ? 20.738 22.546 28.751 1.00 76.84 ? 192 HIS B N 1 ATOM 8687 C CA . HIS B 2 192 ? 20.584 21.148 29.128 1.00 72.53 ? 192 HIS B CA 1 ATOM 8688 C C . HIS B 2 192 ? 21.909 20.604 29.642 1.00 79.30 ? 192 HIS B C 1 ATOM 8689 O O . HIS B 2 192 ? 22.950 20.795 29.016 1.00 79.87 ? 192 HIS B O 1 ATOM 8690 C CB . HIS B 2 192 ? 20.090 20.311 27.948 1.00 73.47 ? 192 HIS B CB 1 ATOM 8691 C CG . HIS B 2 192 ? 19.990 18.849 28.249 1.00 83.21 ? 192 HIS B CG 1 ATOM 8692 N ND1 . HIS B 2 192 ? 19.354 18.362 29.371 1.00 84.04 ? 192 HIS B ND1 1 ATOM 8693 C CD2 . HIS B 2 192 ? 20.448 17.766 27.577 1.00 94.80 ? 192 HIS B CD2 1 ATOM 8694 C CE1 . HIS B 2 192 ? 19.422 17.043 29.377 1.00 93.12 ? 192 HIS B CE1 1 ATOM 8695 N NE2 . HIS B 2 192 ? 20.081 16.656 28.299 1.00 99.84 ? 192 HIS B NE2 1 ATOM 8696 N N . VAL B 2 193 ? 21.867 19.928 30.785 1.00 87.61 ? 193 VAL B N 1 ATOM 8697 C CA . VAL B 2 193 ? 23.082 19.406 31.395 1.00 91.97 ? 193 VAL B CA 1 ATOM 8698 C C . VAL B 2 193 ? 23.101 17.883 31.397 1.00 93.62 ? 193 VAL B C 1 ATOM 8699 O O . VAL B 2 193 ? 23.929 17.263 30.730 1.00 110.29 ? 193 VAL B O 1 ATOM 8700 C CB . VAL B 2 193 ? 23.249 19.907 32.839 1.00 73.45 ? 193 VAL B CB 1 ATOM 8701 C CG1 . VAL B 2 193 ? 24.620 19.522 33.370 1.00 78.56 ? 193 VAL B CG1 1 ATOM 8702 C CG2 . VAL B 2 193 ? 23.057 21.413 32.902 1.00 70.87 ? 193 VAL B CG2 1 ATOM 8703 N N . LEU B 2 194 ? 22.185 17.283 32.150 1.00 82.07 ? 194 LEU B N 1 ATOM 8704 C CA . LEU B 2 194 ? 22.149 15.833 32.290 1.00 81.28 ? 194 LEU B CA 1 ATOM 8705 C C . LEU B 2 194 ? 20.825 15.242 31.818 1.00 77.70 ? 194 LEU B C 1 ATOM 8706 O O . LEU B 2 194 ? 19.769 15.528 32.381 1.00 75.40 ? 194 LEU B O 1 ATOM 8707 C CB . LEU B 2 194 ? 22.406 15.434 33.744 1.00 83.33 ? 194 LEU B CB 1 ATOM 8708 C CG . LEU B 2 194 ? 22.490 13.933 34.027 1.00 92.92 ? 194 LEU B CG 1 ATOM 8709 C CD1 . LEU B 2 194 ? 23.660 13.312 33.280 1.00 98.53 ? 194 LEU B CD1 1 ATOM 8710 C CD2 . LEU B 2 194 ? 22.602 13.674 35.520 1.00 93.01 ? 194 LEU B CD2 1 ATOM 8711 N N . THR B 2 195 ? 20.896 14.417 30.778 1.00 79.90 ? 195 THR B N 1 ATOM 8712 C CA . THR B 2 195 ? 19.732 13.693 30.281 1.00 82.69 ? 195 THR B CA 1 ATOM 8713 C C . THR B 2 195 ? 19.276 12.694 31.342 1.00 90.71 ? 195 THR B C 1 ATOM 8714 O O . THR B 2 195 ? 20.082 12.254 32.163 1.00 92.83 ? 195 THR B O 1 ATOM 8715 C CB . THR B 2 195 ? 20.050 12.961 28.959 1.00 82.82 ? 195 THR B CB 1 ATOM 8716 O OG1 . THR B 2 195 ? 20.782 13.836 28.091 1.00 82.79 ? 195 THR B OG1 1 ATOM 8717 C CG2 . THR B 2 195 ? 18.776 12.512 28.258 1.00 82.66 ? 195 THR B CG2 1 ATOM 8718 N N . LEU B 2 196 ? 17.990 12.352 31.338 1.00 88.65 ? 196 LEU B N 1 ATOM 8719 C CA . LEU B 2 196 ? 17.443 11.425 32.325 1.00 81.94 ? 196 LEU B CA 1 ATOM 8720 C C . LEU B 2 196 ? 18.169 10.082 32.295 1.00 85.66 ? 196 LEU B C 1 ATOM 8721 O O . LEU B 2 196 ? 18.243 9.432 31.252 1.00 88.71 ? 196 LEU B O 1 ATOM 8722 C CB . LEU B 2 196 ? 15.944 11.213 32.091 1.00 79.47 ? 196 LEU B CB 1 ATOM 8723 C CG . LEU B 2 196 ? 15.032 12.439 32.188 1.00 76.10 ? 196 LEU B CG 1 ATOM 8724 C CD1 . LEU B 2 196 ? 13.598 12.067 31.847 1.00 75.96 ? 196 LEU B CD1 1 ATOM 8725 C CD2 . LEU B 2 196 ? 15.107 13.069 33.569 1.00 74.27 ? 196 LEU B CD2 1 ATOM 8726 N N . THR B 2 197 ? 18.695 9.667 33.445 1.00 86.55 ? 197 THR B N 1 ATOM 8727 C CA . THR B 2 197 ? 19.437 8.410 33.545 1.00 100.40 ? 197 THR B CA 1 ATOM 8728 C C . THR B 2 197 ? 19.128 7.664 34.839 1.00 101.56 ? 197 THR B C 1 ATOM 8729 O O . THR B 2 197 ? 18.366 8.140 35.681 1.00 88.57 ? 197 THR B O 1 ATOM 8730 C CB . THR B 2 197 ? 20.965 8.634 33.474 1.00 117.14 ? 197 THR B CB 1 ATOM 8731 O OG1 . THR B 2 197 ? 21.366 9.560 34.491 1.00 122.31 ? 197 THR B OG1 1 ATOM 8732 C CG2 . THR B 2 197 ? 21.383 9.165 32.110 1.00 126.87 ? 197 THR B CG2 1 ATOM 8733 N N . ASP B 2 198 ? 19.728 6.486 34.982 1.00 114.53 ? 198 ASP B N 1 ATOM 8734 C CA . ASP B 2 198 ? 19.539 5.651 36.164 1.00 106.10 ? 198 ASP B CA 1 ATOM 8735 C C . ASP B 2 198 ? 20.425 6.071 37.336 1.00 109.51 ? 198 ASP B C 1 ATOM 8736 O O . ASP B 2 198 ? 19.977 6.102 38.483 1.00 100.74 ? 198 ASP B O 1 ATOM 8737 C CB . ASP B 2 198 ? 19.811 4.185 35.820 1.00 103.69 ? 198 ASP B CB 1 ATOM 8738 C CG . ASP B 2 198 ? 19.235 3.786 34.477 1.00 111.12 ? 198 ASP B CG 1 ATOM 8739 O OD1 . ASP B 2 198 ? 18.312 4.476 33.997 1.00 110.34 ? 198 ASP B OD1 1 ATOM 8740 O OD2 . ASP B 2 198 ? 19.705 2.782 33.901 1.00 120.02 ? 198 ASP B OD2 1 ATOM 8741 N N . GLN B 2 199 ? 21.682 6.391 37.041 1.00 120.74 ? 199 GLN B N 1 ATOM 8742 C CA . GLN B 2 199 ? 22.685 6.613 38.079 1.00 122.27 ? 199 GLN B CA 1 ATOM 8743 C C . GLN B 2 199 ? 22.458 7.904 38.859 1.00 108.10 ? 199 GLN B C 1 ATOM 8744 O O . GLN B 2 199 ? 22.377 8.987 38.280 1.00 95.55 ? 199 GLN B O 1 ATOM 8745 C CB . GLN B 2 199 ? 24.091 6.633 37.471 1.00 126.58 ? 199 GLN B CB 1 ATOM 8746 C CG . GLN B 2 199 ? 24.354 5.547 36.439 1.00 125.32 ? 199 GLN B CG 1 ATOM 8747 C CD . GLN B 2 199 ? 23.990 5.983 35.033 1.00 124.70 ? 199 GLN B CD 1 ATOM 8748 O OE1 . GLN B 2 199 ? 23.496 7.091 34.824 1.00 117.18 ? 199 GLN B OE1 1 ATOM 8749 N NE2 . GLN B 2 199 ? 24.238 5.114 34.061 1.00 129.90 ? 199 GLN B NE2 1 ATOM 8750 N N . VAL B 2 200 ? 22.356 7.776 40.179 1.00 110.28 ? 200 VAL B N 1 ATOM 8751 C CA . VAL B 2 200 ? 22.261 8.933 41.059 1.00 109.26 ? 200 VAL B CA 1 ATOM 8752 C C . VAL B 2 200 ? 23.644 9.528 41.320 1.00 108.75 ? 200 VAL B C 1 ATOM 8753 O O . VAL B 2 200 ? 23.773 10.712 41.630 1.00 110.43 ? 200 VAL B O 1 ATOM 8754 C CB . VAL B 2 200 ? 21.591 8.572 42.401 1.00 106.76 ? 200 VAL B CB 1 ATOM 8755 C CG1 . VAL B 2 200 ? 20.147 8.148 42.173 1.00 92.84 ? 200 VAL B CG1 1 ATOM 8756 C CG2 . VAL B 2 200 ? 22.368 7.472 43.111 1.00 119.77 ? 200 VAL B CG2 1 ATOM 8757 N N . THR B 2 201 ? 24.675 8.697 41.191 1.00 102.77 ? 201 THR B N 1 ATOM 8758 C CA . THR B 2 201 ? 26.051 9.140 41.392 1.00 109.01 ? 201 THR B CA 1 ATOM 8759 C C . THR B 2 201 ? 26.482 10.067 40.262 1.00 117.53 ? 201 THR B C 1 ATOM 8760 O O . THR B 2 201 ? 27.146 11.077 40.491 1.00 118.57 ? 201 THR B O 1 ATOM 8761 C CB . THR B 2 201 ? 27.024 7.951 41.476 1.00 112.57 ? 201 THR B CB 1 ATOM 8762 O OG1 . THR B 2 201 ? 26.941 7.176 40.273 1.00 110.40 ? 201 THR B OG1 1 ATOM 8763 C CG2 . THR B 2 201 ? 26.683 7.068 42.666 1.00 120.40 ? 201 THR B CG2 1 ATOM 8764 N N . ARG B 2 202 ? 26.094 9.709 39.041 1.00 119.11 ? 202 ARG B N 1 ATOM 8765 C CA . ARG B 2 202 ? 26.323 10.547 37.870 1.00 109.81 ? 202 ARG B CA 1 ATOM 8766 C C . ARG B 2 202 ? 25.606 11.885 38.032 1.00 99.81 ? 202 ARG B C 1 ATOM 8767 O O . ARG B 2 202 ? 26.045 12.912 37.513 1.00 103.59 ? 202 ARG B O 1 ATOM 8768 C CB . ARG B 2 202 ? 25.849 9.823 36.604 1.00 110.18 ? 202 ARG B CB 1 ATOM 8769 C CG . ARG B 2 202 ? 25.775 10.685 35.353 1.00 116.07 ? 202 ARG B CG 1 ATOM 8770 C CD . ARG B 2 202 ? 27.140 11.207 34.944 1.00 128.29 ? 202 ARG B CD 1 ATOM 8771 N NE . ARG B 2 202 ? 27.049 12.123 33.811 1.00 135.45 ? 202 ARG B NE 1 ATOM 8772 C CZ . ARG B 2 202 ? 28.076 12.804 33.315 1.00 140.60 ? 202 ARG B CZ 1 ATOM 8773 N NH1 . ARG B 2 202 ? 29.281 12.676 33.854 1.00 143.33 ? 202 ARG B NH1 1 ATOM 8774 N NH2 . ARG B 2 202 ? 27.899 13.616 32.282 1.00 138.06 ? 202 ARG B NH2 1 ATOM 8775 N N . PHE B 2 203 ? 24.510 11.863 38.783 1.00 94.16 ? 203 PHE B N 1 ATOM 8776 C CA . PHE B 2 203 ? 23.705 13.053 39.018 1.00 96.01 ? 203 PHE B CA 1 ATOM 8777 C C . PHE B 2 203 ? 24.380 13.999 40.007 1.00 102.33 ? 203 PHE B C 1 ATOM 8778 O O . PHE B 2 203 ? 24.720 15.130 39.659 1.00 94.33 ? 203 PHE B O 1 ATOM 8779 C CB . PHE B 2 203 ? 22.317 12.656 39.525 1.00 91.70 ? 203 PHE B CB 1 ATOM 8780 C CG . PHE B 2 203 ? 21.366 13.809 39.661 1.00 84.52 ? 203 PHE B CG 1 ATOM 8781 C CD1 . PHE B 2 203 ? 20.584 14.207 38.590 1.00 83.57 ? 203 PHE B CD1 1 ATOM 8782 C CD2 . PHE B 2 203 ? 21.247 14.488 40.860 1.00 79.94 ? 203 PHE B CD2 1 ATOM 8783 C CE1 . PHE B 2 203 ? 19.704 15.265 38.714 1.00 87.18 ? 203 PHE B CE1 1 ATOM 8784 C CE2 . PHE B 2 203 ? 20.371 15.544 40.989 1.00 80.57 ? 203 PHE B CE2 1 ATOM 8785 C CZ . PHE B 2 203 ? 19.598 15.934 39.915 1.00 86.78 ? 203 PHE B CZ 1 ATOM 8786 N N . ASN B 2 204 ? 24.556 13.531 41.241 1.00 109.70 ? 204 ASN B N 1 ATOM 8787 C CA . ASN B 2 204 ? 25.170 14.328 42.303 1.00 107.81 ? 204 ASN B CA 1 ATOM 8788 C C . ASN B 2 204 ? 26.524 14.908 41.908 1.00 110.10 ? 204 ASN B C 1 ATOM 8789 O O . ASN B 2 204 ? 26.838 16.052 42.237 1.00 106.00 ? 204 ASN B O 1 ATOM 8790 C CB . ASN B 2 204 ? 25.329 13.487 43.572 1.00 105.09 ? 204 ASN B CB 1 ATOM 8791 C CG . ASN B 2 204 ? 24.011 12.938 44.080 1.00 117.82 ? 204 ASN B CG 1 ATOM 8792 O OD1 . ASN B 2 204 ? 23.871 11.736 44.303 1.00 133.50 ? 204 ASN B OD1 1 ATOM 8793 N ND2 . ASN B 2 204 ? 23.036 13.820 44.265 1.00 117.80 ? 204 ASN B ND2 1 ATOM 8794 N N . GLU B 2 205 ? 27.320 14.111 41.202 1.00 118.31 ? 205 GLU B N 1 ATOM 8795 C CA . GLU B 2 205 ? 28.636 14.543 40.745 1.00 125.82 ? 205 GLU B CA 1 ATOM 8796 C C . GLU B 2 205 ? 28.527 15.721 39.781 1.00 123.08 ? 205 GLU B C 1 ATOM 8797 O O . GLU B 2 205 ? 29.236 16.718 39.922 1.00 128.12 ? 205 GLU B O 1 ATOM 8798 C CB . GLU B 2 205 ? 29.377 13.377 40.081 1.00 132.66 ? 205 GLU B CB 1 ATOM 8799 C CG . GLU B 2 205 ? 30.705 13.746 39.432 1.00 145.11 ? 205 GLU B CG 1 ATOM 8800 C CD . GLU B 2 205 ? 30.560 14.117 37.967 1.00 146.69 ? 205 GLU B CD 1 ATOM 8801 O OE1 . GLU B 2 205 ? 29.468 13.898 37.403 1.00 138.67 ? 205 GLU B OE1 1 ATOM 8802 O OE2 . GLU B 2 205 ? 31.537 14.631 37.383 1.00 152.84 ? 205 GLU B OE2 1 ATOM 8803 N N . GLU B 2 206 ? 27.633 15.601 38.805 1.00 113.76 ? 206 GLU B N 1 ATOM 8804 C CA . GLU B 2 206 ? 27.449 16.637 37.796 1.00 108.49 ? 206 GLU B CA 1 ATOM 8805 C C . GLU B 2 206 ? 26.736 17.856 38.377 1.00 97.08 ? 206 GLU B C 1 ATOM 8806 O O . GLU B 2 206 ? 26.858 18.967 37.860 1.00 99.06 ? 206 GLU B O 1 ATOM 8807 C CB . GLU B 2 206 ? 26.664 16.083 36.604 1.00 114.79 ? 206 GLU B CB 1 ATOM 8808 C CG . GLU B 2 206 ? 26.615 17.009 35.398 1.00 126.82 ? 206 GLU B CG 1 ATOM 8809 C CD . GLU B 2 206 ? 27.981 17.230 34.778 1.00 137.25 ? 206 GLU B CD 1 ATOM 8810 O OE1 . GLU B 2 206 ? 28.809 16.294 34.808 1.00 138.65 ? 206 GLU B OE1 1 ATOM 8811 O OE2 . GLU B 2 206 ? 28.229 18.341 34.263 1.00 137.75 ? 206 GLU B OE2 1 ATOM 8812 N N . VAL B 2 207 ? 25.998 17.640 39.460 1.00 91.88 ? 207 VAL B N 1 ATOM 8813 C CA . VAL B 2 207 ? 25.213 18.700 40.082 1.00 88.37 ? 207 VAL B CA 1 ATOM 8814 C C . VAL B 2 207 ? 26.081 19.650 40.912 1.00 92.52 ? 207 VAL B C 1 ATOM 8815 O O . VAL B 2 207 ? 25.870 20.864 40.896 1.00 87.77 ? 207 VAL B O 1 ATOM 8816 C CB . VAL B 2 207 ? 24.088 18.100 40.962 1.00 85.88 ? 207 VAL B CB 1 ATOM 8817 C CG1 . VAL B 2 207 ? 23.972 18.825 42.290 1.00 86.70 ? 207 VAL B CG1 1 ATOM 8818 C CG2 . VAL B 2 207 ? 22.763 18.125 40.216 1.00 76.00 ? 207 VAL B CG2 1 ATOM 8819 N N . LYS B 2 208 ? 27.065 19.100 41.618 1.00 102.77 ? 208 LYS B N 1 ATOM 8820 C CA . LYS B 2 208 ? 27.923 19.905 42.482 1.00 97.59 ? 208 LYS B CA 1 ATOM 8821 C C . LYS B 2 208 ? 28.787 20.859 41.662 1.00 94.44 ? 208 LYS B C 1 ATOM 8822 O O . LYS B 2 208 ? 29.206 21.911 42.147 1.00 100.01 ? 208 LYS B O 1 ATOM 8823 C CB . LYS B 2 208 ? 28.808 19.006 43.350 1.00 104.66 ? 208 LYS B CB 1 ATOM 8824 C CG . LYS B 2 208 ? 29.519 19.738 44.477 1.00 112.11 ? 208 LYS B CG 1 ATOM 8825 C CD . LYS B 2 208 ? 30.484 18.825 45.216 1.00 110.86 ? 208 LYS B CD 1 ATOM 8826 C CE . LYS B 2 208 ? 31.614 18.366 44.309 1.00 105.23 ? 208 LYS B CE 1 ATOM 8827 N NZ . LYS B 2 208 ? 32.605 17.527 45.037 1.00 105.56 ? 208 LYS B NZ 1 ATOM 8828 N N . LYS B 2 209 ? 29.041 20.485 40.412 1.00 92.34 ? 209 LYS B N 1 ATOM 8829 C CA . LYS B 2 209 ? 29.858 21.287 39.509 1.00 94.31 ? 209 LYS B CA 1 ATOM 8830 C C . LYS B 2 209 ? 29.203 22.624 39.174 1.00 99.18 ? 209 LYS B C 1 ATOM 8831 O O . LYS B 2 209 ? 29.884 23.586 38.820 1.00 118.09 ? 209 LYS B O 1 ATOM 8832 C CB . LYS B 2 209 ? 30.135 20.511 38.219 1.00 98.81 ? 209 LYS B CB 1 ATOM 8833 C CG . LYS B 2 209 ? 30.845 19.184 38.432 1.00 104.86 ? 209 LYS B CG 1 ATOM 8834 C CD . LYS B 2 209 ? 30.884 18.362 37.152 1.00 101.36 ? 209 LYS B CD 1 ATOM 8835 C CE . LYS B 2 209 ? 31.613 19.096 36.038 1.00 100.59 ? 209 LYS B CE 1 ATOM 8836 N NZ . LYS B 2 209 ? 31.679 18.283 34.792 1.00 97.85 ? 209 LYS B NZ 1 ATOM 8837 N N . GLN B 2 210 ? 27.880 22.677 39.290 1.00 88.97 ? 210 GLN B N 1 ATOM 8838 C CA . GLN B 2 210 ? 27.119 23.860 38.903 1.00 85.76 ? 210 GLN B CA 1 ATOM 8839 C C . GLN B 2 210 ? 27.404 25.060 39.802 1.00 85.64 ? 210 GLN B C 1 ATOM 8840 O O . GLN B 2 210 ? 27.406 24.947 41.027 1.00 85.18 ? 210 GLN B O 1 ATOM 8841 C CB . GLN B 2 210 ? 25.620 23.550 38.911 1.00 81.22 ? 210 GLN B CB 1 ATOM 8842 C CG . GLN B 2 210 ? 25.229 22.372 38.033 1.00 86.18 ? 210 GLN B CG 1 ATOM 8843 C CD . GLN B 2 210 ? 25.594 22.581 36.576 1.00 88.20 ? 210 GLN B CD 1 ATOM 8844 O OE1 . GLN B 2 210 ? 25.544 23.700 36.065 1.00 95.64 ? 210 GLN B OE1 1 ATOM 8845 N NE2 . GLN B 2 210 ? 25.968 21.500 35.900 1.00 82.81 ? 210 GLN B NE2 1 ATOM 8846 N N . SER B 2 211 ? 27.643 26.208 39.176 1.00 90.43 ? 211 SER B N 1 ATOM 8847 C CA . SER B 2 211 ? 27.894 27.449 39.900 1.00 89.22 ? 211 SER B CA 1 ATOM 8848 C C . SER B 2 211 ? 26.941 28.541 39.423 1.00 82.57 ? 211 SER B C 1 ATOM 8849 O O . SER B 2 211 ? 26.101 28.301 38.556 1.00 89.66 ? 211 SER B O 1 ATOM 8850 C CB . SER B 2 211 ? 29.347 27.889 39.725 1.00 103.02 ? 211 SER B CB 1 ATOM 8851 O OG . SER B 2 211 ? 30.241 26.859 40.112 1.00 117.39 ? 211 SER B OG 1 ATOM 8852 N N . VAL B 2 212 ? 27.078 29.741 39.976 1.00 79.58 ? 212 VAL B N 1 ATOM 8853 C CA . VAL B 2 212 ? 26.130 30.815 39.690 1.00 75.20 ? 212 VAL B CA 1 ATOM 8854 C C . VAL B 2 212 ? 26.649 31.825 38.671 1.00 74.65 ? 212 VAL B C 1 ATOM 8855 O O . VAL B 2 212 ? 27.846 32.107 38.603 1.00 88.95 ? 212 VAL B O 1 ATOM 8856 C CB . VAL B 2 212 ? 25.739 31.576 40.973 1.00 75.63 ? 212 VAL B CB 1 ATOM 8857 C CG1 . VAL B 2 212 ? 24.890 30.695 41.873 1.00 87.27 ? 212 VAL B CG1 1 ATOM 8858 C CG2 . VAL B 2 212 ? 26.978 32.066 41.705 1.00 95.75 ? 212 VAL B CG2 1 ATOM 8859 N N . SER B 2 213 ? 25.728 32.354 37.873 1.00 69.85 ? 213 SER B N 1 ATOM 8860 C CA . SER B 2 213 ? 26.042 33.391 36.899 1.00 68.68 ? 213 SER B CA 1 ATOM 8861 C C . SER B 2 213 ? 25.338 34.688 37.290 1.00 75.33 ? 213 SER B C 1 ATOM 8862 O O . SER B 2 213 ? 24.721 34.761 38.349 1.00 97.45 ? 213 SER B O 1 ATOM 8863 C CB . SER B 2 213 ? 25.632 32.961 35.494 1.00 66.39 ? 213 SER B CB 1 ATOM 8864 O OG . SER B 2 213 ? 26.212 33.818 34.531 1.00 66.66 ? 213 SER B OG 1 ATOM 8865 N N . ARG B 2 214 ? 25.430 35.713 36.448 1.00 66.42 ? 214 ARG B N 1 ATOM 8866 C CA . ARG B 2 214 ? 24.852 37.007 36.798 1.00 66.94 ? 214 ARG B CA 1 ATOM 8867 C C . ARG B 2 214 ? 24.203 37.750 35.634 1.00 63.68 ? 214 ARG B C 1 ATOM 8868 O O . ARG B 2 214 ? 24.714 37.758 34.514 1.00 64.12 ? 214 ARG B O 1 ATOM 8869 C CB . ARG B 2 214 ? 25.924 37.902 37.422 1.00 89.67 ? 214 ARG B CB 1 ATOM 8870 C CG . ARG B 2 214 ? 25.424 39.273 37.847 1.00 86.95 ? 214 ARG B CG 1 ATOM 8871 C CD . ARG B 2 214 ? 26.563 40.143 38.341 1.00 80.44 ? 214 ARG B CD 1 ATOM 8872 N NE . ARG B 2 214 ? 26.104 41.455 38.786 1.00 67.86 ? 214 ARG B NE 1 ATOM 8873 C CZ . ARG B 2 214 ? 26.888 42.357 39.365 1.00 69.88 ? 214 ARG B CZ 1 ATOM 8874 N NH1 . ARG B 2 214 ? 28.169 42.084 39.570 1.00 92.46 ? 214 ARG B NH1 1 ATOM 8875 N NH2 . ARG B 2 214 ? 26.395 43.528 39.742 1.00 74.04 ? 214 ARG B NH2 1 ATOM 8876 N N . ASN B 2 215 ? 23.064 38.374 35.925 1.00 61.89 ? 215 ASN B N 1 ATOM 8877 C CA . ASN B 2 215 ? 22.403 39.295 35.004 1.00 61.01 ? 215 ASN B CA 1 ATOM 8878 C C . ASN B 2 215 ? 21.737 40.406 35.818 1.00 60.68 ? 215 ASN B C 1 ATOM 8879 O O . ASN B 2 215 ? 21.510 40.229 37.011 1.00 77.19 ? 215 ASN B O 1 ATOM 8880 C CB . ASN B 2 215 ? 21.391 38.555 34.122 1.00 58.22 ? 215 ASN B CB 1 ATOM 8881 C CG . ASN B 2 215 ? 20.101 38.230 34.842 1.00 61.65 ? 215 ASN B CG 1 ATOM 8882 O OD1 . ASN B 2 215 ? 19.018 38.615 34.399 1.00 52.85 ? 215 ASN B OD1 1 ATOM 8883 N ND2 . ASN B 2 215 ? 20.204 37.490 35.937 1.00 77.96 ? 215 ASN B ND2 1 ATOM 8884 N N . ARG B 2 216 ? 21.465 41.561 35.213 1.00 59.49 ? 216 ARG B N 1 ATOM 8885 C CA . ARG B 2 216 ? 20.918 42.683 35.990 1.00 60.69 ? 216 ARG B CA 1 ATOM 8886 C C . ARG B 2 216 ? 19.400 42.741 36.132 1.00 62.64 ? 216 ARG B C 1 ATOM 8887 O O . ARG B 2 216 ? 18.887 43.434 37.006 1.00 72.61 ? 216 ARG B O 1 ATOM 8888 C CB . ARG B 2 216 ? 21.373 44.008 35.393 1.00 69.76 ? 216 ARG B CB 1 ATOM 8889 C CG . ARG B 2 216 ? 20.939 44.220 33.977 1.00 78.10 ? 216 ARG B CG 1 ATOM 8890 C CD . ARG B 2 216 ? 22.163 44.522 33.156 1.00 94.84 ? 216 ARG B CD 1 ATOM 8891 N NE . ARG B 2 216 ? 23.033 45.472 33.827 1.00 86.77 ? 216 ARG B NE 1 ATOM 8892 C CZ . ARG B 2 216 ? 24.064 46.062 33.238 1.00 68.81 ? 216 ARG B CZ 1 ATOM 8893 N NH1 . ARG B 2 216 ? 24.330 45.808 31.962 1.00 63.51 ? 216 ARG B NH1 1 ATOM 8894 N NH2 . ARG B 2 216 ? 24.815 46.919 33.914 1.00 68.31 ? 216 ARG B NH2 1 ATOM 8895 N N . ASP B 2 217 ? 18.683 42.028 35.275 1.00 60.87 ? 217 ASP B N 1 ATOM 8896 C CA . ASP B 2 217 ? 17.227 42.122 35.240 1.00 55.41 ? 217 ASP B CA 1 ATOM 8897 C C . ASP B 2 217 ? 16.610 41.105 36.196 1.00 53.40 ? 217 ASP B C 1 ATOM 8898 O O . ASP B 2 217 ? 16.915 39.923 36.111 1.00 54.53 ? 217 ASP B O 1 ATOM 8899 C CB . ASP B 2 217 ? 16.729 41.913 33.809 1.00 61.35 ? 217 ASP B CB 1 ATOM 8900 C CG . ASP B 2 217 ? 15.543 40.994 33.739 1.00 82.37 ? 217 ASP B CG 1 ATOM 8901 O OD1 . ASP B 2 217 ? 15.742 39.763 33.756 1.00 80.54 ? 217 ASP B OD1 1 ATOM 8902 O OD2 . ASP B 2 217 ? 14.409 41.499 33.651 1.00 97.70 ? 217 ASP B OD2 1 ATOM 8903 N N . ALA B 2 218 ? 15.758 41.560 37.114 1.00 64.61 ? 218 ALA B N 1 ATOM 8904 C CA . ALA B 2 218 ? 15.317 40.701 38.219 1.00 62.29 ? 218 ALA B CA 1 ATOM 8905 C C . ALA B 2 218 ? 14.517 39.468 37.776 1.00 49.40 ? 218 ALA B C 1 ATOM 8906 O O . ALA B 2 218 ? 14.812 38.357 38.227 1.00 61.75 ? 218 ALA B O 1 ATOM 8907 C CB . ALA B 2 218 ? 14.511 41.509 39.243 1.00 61.39 ? 218 ALA B CB 1 ATOM 8908 N N . PRO B 2 219 ? 13.492 39.643 36.919 1.00 46.52 ? 219 PRO B N 1 ATOM 8909 C CA . PRO B 2 219 ? 12.873 38.400 36.451 1.00 52.05 ? 219 PRO B CA 1 ATOM 8910 C C . PRO B 2 219 ? 13.843 37.609 35.584 1.00 47.49 ? 219 PRO B C 1 ATOM 8911 O O . PRO B 2 219 ? 14.491 38.186 34.715 1.00 46.43 ? 219 PRO B O 1 ATOM 8912 C CB . PRO B 2 219 ? 11.652 38.882 35.653 1.00 71.17 ? 219 PRO B CB 1 ATOM 8913 C CG . PRO B 2 219 ? 11.964 40.271 35.271 1.00 74.49 ? 219 PRO B CG 1 ATOM 8914 C CD . PRO B 2 219 ? 12.851 40.834 36.335 1.00 67.57 ? 219 PRO B CD 1 ATOM 8915 N N . GLU B 2 220 ? 13.949 36.311 35.844 1.00 52.41 ? 220 GLU B N 1 ATOM 8916 C CA . GLU B 2 220 ? 14.974 35.492 35.217 1.00 49.77 ? 220 GLU B CA 1 ATOM 8917 C C . GLU B 2 220 ? 14.499 34.801 33.942 1.00 53.66 ? 220 GLU B C 1 ATOM 8918 O O . GLU B 2 220 ? 15.305 34.282 33.169 1.00 60.23 ? 220 GLU B O 1 ATOM 8919 C CB . GLU B 2 220 ? 15.482 34.455 36.219 1.00 50.72 ? 220 GLU B CB 1 ATOM 8920 C CG . GLU B 2 220 ? 16.899 34.706 36.713 1.00 59.38 ? 220 GLU B CG 1 ATOM 8921 C CD . GLU B 2 220 ? 17.153 36.154 37.096 1.00 51.14 ? 220 GLU B CD 1 ATOM 8922 O OE1 . GLU B 2 220 ? 16.826 36.530 38.239 1.00 50.53 ? 220 GLU B OE1 1 ATOM 8923 O OE2 . GLU B 2 220 ? 17.684 36.915 36.255 1.00 52.44 ? 220 GLU B OE2 1 ATOM 8924 N N . GLY B 2 221 ? 13.192 34.830 33.704 1.00 55.90 ? 221 GLY B N 1 ATOM 8925 C CA . GLY B 2 221 ? 12.628 34.228 32.509 1.00 82.23 ? 221 GLY B CA 1 ATOM 8926 C C . GLY B 2 221 ? 12.933 32.748 32.374 1.00 85.05 ? 221 GLY B C 1 ATOM 8927 O O . GLY B 2 221 ? 13.509 32.313 31.375 1.00 57.25 ? 221 GLY B O 1 ATOM 8928 N N . GLY B 2 222 ? 12.563 31.975 33.389 1.00 87.54 ? 222 GLY B N 1 ATOM 8929 C CA . GLY B 2 222 ? 12.769 30.540 33.364 1.00 71.27 ? 222 GLY B CA 1 ATOM 8930 C C . GLY B 2 222 ? 11.770 29.827 32.478 1.00 62.99 ? 222 GLY B C 1 ATOM 8931 O O . GLY B 2 222 ? 11.940 28.651 32.161 1.00 66.59 ? 222 GLY B O 1 ATOM 8932 N N . PHE B 2 223 ? 10.724 30.546 32.078 1.00 61.14 ? 223 PHE B N 1 ATOM 8933 C CA . PHE B 2 223 ? 9.689 29.991 31.212 1.00 48.90 ? 223 PHE B CA 1 ATOM 8934 C C . PHE B 2 223 ? 10.280 29.488 29.900 1.00 49.85 ? 223 PHE B C 1 ATOM 8935 O O . PHE B 2 223 ? 9.767 28.543 29.301 1.00 59.58 ? 223 PHE B O 1 ATOM 8936 C CB . PHE B 2 223 ? 8.601 31.031 30.933 1.00 58.47 ? 223 PHE B CB 1 ATOM 8937 C CG . PHE B 2 223 ? 7.678 31.275 32.096 1.00 63.16 ? 223 PHE B CG 1 ATOM 8938 C CD1 . PHE B 2 223 ? 7.820 30.565 33.277 1.00 63.82 ? 223 PHE B CD1 1 ATOM 8939 C CD2 . PHE B 2 223 ? 6.659 32.208 32.001 1.00 61.78 ? 223 PHE B CD2 1 ATOM 8940 C CE1 . PHE B 2 223 ? 6.970 30.788 34.343 1.00 48.03 ? 223 PHE B CE1 1 ATOM 8941 C CE2 . PHE B 2 223 ? 5.804 32.433 33.063 1.00 55.73 ? 223 PHE B CE2 1 ATOM 8942 C CZ . PHE B 2 223 ? 5.961 31.721 34.236 1.00 47.63 ? 223 PHE B CZ 1 ATOM 8943 N N . ASP B 2 224 ? 11.356 30.133 29.461 1.00 49.69 ? 224 ASP B N 1 ATOM 8944 C CA . ASP B 2 224 ? 12.097 29.694 28.285 1.00 56.37 ? 224 ASP B CA 1 ATOM 8945 C C . ASP B 2 224 ? 12.568 28.256 28.453 1.00 65.43 ? 224 ASP B C 1 ATOM 8946 O O . ASP B 2 224 ? 12.477 27.446 27.529 1.00 80.36 ? 224 ASP B O 1 ATOM 8947 C CB . ASP B 2 224 ? 13.295 30.611 28.034 1.00 72.19 ? 224 ASP B CB 1 ATOM 8948 C CG . ASP B 2 224 ? 13.132 31.458 26.789 1.00 65.59 ? 224 ASP B CG 1 ATOM 8949 O OD1 . ASP B 2 224 ? 11.999 31.550 26.273 1.00 60.00 ? 224 ASP B OD1 1 ATOM 8950 O OD2 . ASP B 2 224 ? 14.140 32.035 26.329 1.00 52.76 ? 224 ASP B OD2 1 ATOM 8951 N N . ALA B 2 225 ? 13.068 27.948 29.645 1.00 62.73 ? 225 ALA B N 1 ATOM 8952 C CA . ALA B 2 225 ? 13.557 26.611 29.960 1.00 54.00 ? 225 ALA B CA 1 ATOM 8953 C C . ALA B 2 225 ? 12.414 25.604 30.020 1.00 54.55 ? 225 ALA B C 1 ATOM 8954 O O . ALA B 2 225 ? 12.533 24.491 29.507 1.00 56.21 ? 225 ALA B O 1 ATOM 8955 C CB . ALA B 2 225 ? 14.319 26.624 31.275 1.00 54.01 ? 225 ALA B CB 1 ATOM 8956 N N . ILE B 2 226 ? 11.313 26.002 30.652 1.00 53.40 ? 226 ILE B N 1 ATOM 8957 C CA . ILE B 2 226 ? 10.136 25.146 30.772 1.00 58.30 ? 226 ILE B CA 1 ATOM 8958 C C . ILE B 2 226 ? 9.613 24.739 29.400 1.00 55.11 ? 226 ILE B C 1 ATOM 8959 O O . ILE B 2 226 ? 9.293 23.573 29.166 1.00 56.71 ? 226 ILE B O 1 ATOM 8960 C CB . ILE B 2 226 ? 9.005 25.842 31.556 1.00 52.81 ? 226 ILE B CB 1 ATOM 8961 C CG1 . ILE B 2 226 ? 9.471 26.199 32.969 1.00 54.60 ? 226 ILE B CG1 1 ATOM 8962 C CG2 . ILE B 2 226 ? 7.770 24.958 31.617 1.00 53.81 ? 226 ILE B CG2 1 ATOM 8963 C CD1 . ILE B 2 226 ? 8.388 26.812 33.830 1.00 60.35 ? 226 ILE B CD1 1 ATOM 8964 N N . MET B 2 227 ? 9.541 25.709 28.496 1.00 54.45 ? 227 MET B N 1 ATOM 8965 C CA . MET B 2 227 ? 9.047 25.468 27.147 1.00 60.47 ? 227 MET B CA 1 ATOM 8966 C C . MET B 2 227 ? 9.917 24.464 26.395 1.00 60.17 ? 227 MET B C 1 ATOM 8967 O O . MET B 2 227 ? 9.402 23.568 25.730 1.00 59.36 ? 227 MET B O 1 ATOM 8968 C CB . MET B 2 227 ? 8.969 26.782 26.366 1.00 61.70 ? 227 MET B CB 1 ATOM 8969 C CG . MET B 2 227 ? 8.559 26.612 24.913 1.00 65.74 ? 227 MET B CG 1 ATOM 8970 S SD . MET B 2 227 ? 7.048 25.644 24.725 1.00 65.16 ? 227 MET B SD 1 ATOM 8971 C CE . MET B 2 227 ? 5.863 26.688 25.570 1.00 100.27 ? 227 MET B CE 1 ATOM 8972 N N . GLN B 2 228 ? 11.232 24.609 26.515 1.00 68.08 ? 228 GLN B N 1 ATOM 8973 C CA . GLN B 2 228 ? 12.163 23.753 25.784 1.00 59.68 ? 228 GLN B CA 1 ATOM 8974 C C . GLN B 2 228 ? 12.234 22.339 26.353 1.00 89.48 ? 228 GLN B C 1 ATOM 8975 O O . GLN B 2 228 ? 12.269 21.365 25.601 1.00 84.36 ? 228 GLN B O 1 ATOM 8976 C CB . GLN B 2 228 ? 13.558 24.379 25.770 1.00 59.48 ? 228 GLN B CB 1 ATOM 8977 C CG . GLN B 2 228 ? 13.668 25.590 24.863 1.00 65.24 ? 228 GLN B CG 1 ATOM 8978 C CD . GLN B 2 228 ? 13.238 25.284 23.442 1.00 64.84 ? 228 GLN B CD 1 ATOM 8979 O OE1 . GLN B 2 228 ? 13.611 24.256 22.876 1.00 62.60 ? 228 GLN B OE1 1 ATOM 8980 N NE2 . GLN B 2 228 ? 12.440 26.172 22.860 1.00 77.69 ? 228 GLN B NE2 1 ATOM 8981 N N . ALA B 2 229 ? 12.257 22.229 27.677 1.00 88.70 ? 229 ALA B N 1 ATOM 8982 C CA . ALA B 2 229 ? 12.318 20.926 28.332 1.00 61.83 ? 229 ALA B CA 1 ATOM 8983 C C . ALA B 2 229 ? 11.060 20.115 28.044 1.00 62.84 ? 229 ALA B C 1 ATOM 8984 O O . ALA B 2 229 ? 11.084 18.885 28.064 1.00 64.83 ? 229 ALA B O 1 ATOM 8985 C CB . ALA B 2 229 ? 12.510 21.092 29.831 1.00 71.60 ? 229 ALA B CB 1 ATOM 8986 N N . THR B 2 230 ? 9.962 20.815 27.782 1.00 62.43 ? 230 THR B N 1 ATOM 8987 C CA . THR B 2 230 ? 8.696 20.171 27.459 1.00 62.86 ? 230 THR B CA 1 ATOM 8988 C C . THR B 2 230 ? 8.648 19.684 26.013 1.00 65.00 ? 230 THR B C 1 ATOM 8989 O O . THR B 2 230 ? 8.245 18.552 25.745 1.00 89.24 ? 230 THR B O 1 ATOM 8990 C CB . THR B 2 230 ? 7.511 21.125 27.705 1.00 61.26 ? 230 THR B CB 1 ATOM 8991 O OG1 . THR B 2 230 ? 7.522 21.557 29.070 1.00 59.59 ? 230 THR B OG1 1 ATOM 8992 C CG2 . THR B 2 230 ? 6.193 20.429 27.409 1.00 65.89 ? 230 THR B CG2 1 ATOM 8993 N N . VAL B 2 231 ? 9.067 20.538 25.084 1.00 64.58 ? 231 VAL B N 1 ATOM 8994 C CA . VAL B 2 231 ? 8.926 20.241 23.661 1.00 66.69 ? 231 VAL B CA 1 ATOM 8995 C C . VAL B 2 231 ? 10.085 19.433 23.086 1.00 68.86 ? 231 VAL B C 1 ATOM 8996 O O . VAL B 2 231 ? 9.980 18.900 21.982 1.00 85.62 ? 231 VAL B O 1 ATOM 8997 C CB . VAL B 2 231 ? 8.785 21.529 22.832 1.00 90.70 ? 231 VAL B CB 1 ATOM 8998 C CG1 . VAL B 2 231 ? 7.620 22.355 23.340 1.00 84.41 ? 231 VAL B CG1 1 ATOM 8999 C CG2 . VAL B 2 231 ? 10.075 22.329 22.874 1.00 96.15 ? 231 VAL B CG2 1 ATOM 9000 N N . CYS B 2 232 ? 11.186 19.336 23.823 1.00 68.35 ? 232 CYS B N 1 ATOM 9001 C CA . CYS B 2 232 ? 12.297 18.515 23.363 1.00 82.76 ? 232 CYS B CA 1 ATOM 9002 C C . CYS B 2 232 ? 12.276 17.189 24.108 1.00 89.91 ? 232 CYS B C 1 ATOM 9003 O O . CYS B 2 232 ? 12.629 17.117 25.283 1.00 113.36 ? 232 CYS B O 1 ATOM 9004 C CB . CYS B 2 232 ? 13.633 19.231 23.573 1.00 81.94 ? 232 CYS B CB 1 ATOM 9005 S SG . CYS B 2 232 ? 13.758 20.847 22.766 1.00 71.58 ? 232 CYS B SG 1 ATOM 9006 N N . ASP B 2 233 ? 11.862 16.138 23.409 1.00 81.01 ? 233 ASP B N 1 ATOM 9007 C CA . ASP B 2 233 ? 11.707 14.826 24.020 1.00 90.99 ? 233 ASP B CA 1 ATOM 9008 C C . ASP B 2 233 ? 13.022 14.057 24.089 1.00 93.88 ? 233 ASP B C 1 ATOM 9009 O O . ASP B 2 233 ? 13.340 13.442 25.107 1.00 98.13 ? 233 ASP B O 1 ATOM 9010 C CB . ASP B 2 233 ? 10.662 14.014 23.254 1.00 109.18 ? 233 ASP B CB 1 ATOM 9011 C CG . ASP B 2 233 ? 9.347 14.757 23.102 1.00 114.06 ? 233 ASP B CG 1 ATOM 9012 O OD1 . ASP B 2 233 ? 9.084 15.674 23.909 1.00 85.94 ? 233 ASP B OD1 1 ATOM 9013 O OD2 . ASP B 2 233 ? 8.578 14.425 22.175 1.00 133.91 ? 233 ASP B OD2 1 ATOM 9014 N N . GLU B 2 234 ? 13.786 14.104 23.003 1.00 98.57 ? 234 GLU B N 1 ATOM 9015 C CA . GLU B 2 234 ? 15.005 13.313 22.887 1.00 109.24 ? 234 GLU B CA 1 ATOM 9016 C C . GLU B 2 234 ? 16.116 13.838 23.788 1.00 112.38 ? 234 GLU B C 1 ATOM 9017 O O . GLU B 2 234 ? 16.780 13.065 24.479 1.00 122.17 ? 234 GLU B O 1 ATOM 9018 C CB . GLU B 2 234 ? 15.486 13.281 21.432 1.00 121.45 ? 234 GLU B CB 1 ATOM 9019 C CG . GLU B 2 234 ? 14.621 12.445 20.493 1.00 132.37 ? 234 GLU B CG 1 ATOM 9020 C CD . GLU B 2 234 ? 13.302 13.112 20.148 1.00 143.57 ? 234 GLU B CD 1 ATOM 9021 O OE1 . GLU B 2 234 ? 13.135 14.309 20.463 1.00 146.76 ? 234 GLU B OE1 1 ATOM 9022 O OE2 . GLU B 2 234 ? 12.430 12.437 19.561 1.00 147.46 ? 234 GLU B OE2 1 ATOM 9023 N N . LYS B 2 235 ? 16.314 15.152 23.778 1.00 108.69 ? 235 LYS B N 1 ATOM 9024 C CA . LYS B 2 235 ? 17.383 15.767 24.555 1.00 106.47 ? 235 LYS B CA 1 ATOM 9025 C C . LYS B 2 235 ? 17.154 15.590 26.054 1.00 108.36 ? 235 LYS B C 1 ATOM 9026 O O . LYS B 2 235 ? 18.095 15.348 26.809 1.00 124.82 ? 235 LYS B O 1 ATOM 9027 C CB . LYS B 2 235 ? 17.510 17.252 24.210 1.00 91.39 ? 235 LYS B CB 1 ATOM 9028 C CG . LYS B 2 235 ? 18.927 17.679 23.864 1.00 91.41 ? 235 LYS B CG 1 ATOM 9029 C CD . LYS B 2 235 ? 19.476 16.851 22.712 1.00 104.90 ? 235 LYS B CD 1 ATOM 9030 C CE . LYS B 2 235 ? 20.926 17.196 22.418 1.00 104.28 ? 235 LYS B CE 1 ATOM 9031 N NZ . LYS B 2 235 ? 21.474 16.374 21.304 1.00 104.40 ? 235 LYS B NZ 1 ATOM 9032 N N . ILE B 2 236 ? 15.900 15.710 26.479 1.00 87.93 ? 236 ILE B N 1 ATOM 9033 C CA . ILE B 2 236 ? 15.550 15.529 27.883 1.00 84.76 ? 236 ILE B CA 1 ATOM 9034 C C . ILE B 2 236 ? 15.478 14.049 28.242 1.00 85.56 ? 236 ILE B C 1 ATOM 9035 O O . ILE B 2 236 ? 15.953 13.633 29.299 1.00 87.57 ? 236 ILE B O 1 ATOM 9036 C CB . ILE B 2 236 ? 14.207 16.198 28.224 1.00 81.50 ? 236 ILE B CB 1 ATOM 9037 C CG1 . ILE B 2 236 ? 14.267 17.695 27.918 1.00 95.09 ? 236 ILE B CG1 1 ATOM 9038 C CG2 . ILE B 2 236 ? 13.854 15.973 29.685 1.00 79.32 ? 236 ILE B CG2 1 ATOM 9039 C CD1 . ILE B 2 236 ? 15.376 18.417 28.636 1.00 98.53 ? 236 ILE B CD1 1 ATOM 9040 N N . GLY B 2 237 ? 14.889 13.255 27.355 1.00 97.63 ? 237 GLY B N 1 ATOM 9041 C CA . GLY B 2 237 ? 14.778 11.827 27.582 1.00 110.51 ? 237 GLY B CA 1 ATOM 9042 C C . GLY B 2 237 ? 13.502 11.396 28.281 1.00 104.78 ? 237 GLY B C 1 ATOM 9043 O O . GLY B 2 237 ? 13.481 10.356 28.939 1.00 101.04 ? 237 GLY B O 1 ATOM 9044 N N . TRP B 2 238 ? 12.448 12.200 28.155 1.00 97.03 ? 238 TRP B N 1 ATOM 9045 C CA . TRP B 2 238 ? 11.144 11.841 28.708 1.00 82.60 ? 238 TRP B CA 1 ATOM 9046 C C . TRP B 2 238 ? 10.700 10.485 28.178 1.00 85.39 ? 238 TRP B C 1 ATOM 9047 O O . TRP B 2 238 ? 10.679 10.261 26.968 1.00 82.64 ? 238 TRP B O 1 ATOM 9048 C CB . TRP B 2 238 ? 10.085 12.894 28.365 1.00 86.46 ? 238 TRP B CB 1 ATOM 9049 C CG . TRP B 2 238 ? 10.250 14.215 29.056 1.00 79.88 ? 238 TRP B CG 1 ATOM 9050 C CD1 . TRP B 2 238 ? 10.531 15.415 28.470 1.00 74.93 ? 238 TRP B CD1 1 ATOM 9051 C CD2 . TRP B 2 238 ? 10.128 14.474 30.460 1.00 78.98 ? 238 TRP B CD2 1 ATOM 9052 N NE1 . TRP B 2 238 ? 10.594 16.403 29.421 1.00 69.47 ? 238 TRP B NE1 1 ATOM 9053 C CE2 . TRP B 2 238 ? 10.353 15.852 30.652 1.00 67.97 ? 238 TRP B CE2 1 ATOM 9054 C CE3 . TRP B 2 238 ? 9.854 13.675 31.574 1.00 89.15 ? 238 TRP B CE3 1 ATOM 9055 C CZ2 . TRP B 2 238 ? 10.313 16.447 31.911 1.00 66.18 ? 238 TRP B CZ2 1 ATOM 9056 C CZ3 . TRP B 2 238 ? 9.815 14.269 32.824 1.00 93.89 ? 238 TRP B CZ3 1 ATOM 9057 C CH2 . TRP B 2 238 ? 10.043 15.641 32.982 1.00 67.01 ? 238 TRP B CH2 1 ATOM 9058 N N . ARG B 2 239 ? 10.348 9.579 29.084 1.00 90.80 ? 239 ARG B N 1 ATOM 9059 C CA . ARG B 2 239 ? 9.886 8.257 28.685 1.00 94.25 ? 239 ARG B CA 1 ATOM 9060 C C . ARG B 2 239 ? 8.387 8.265 28.419 1.00 85.26 ? 239 ARG B C 1 ATOM 9061 O O . ARG B 2 239 ? 7.721 9.286 28.582 1.00 105.40 ? 239 ARG B O 1 ATOM 9062 C CB . ARG B 2 239 ? 10.221 7.219 29.759 1.00 90.85 ? 239 ARG B CB 1 ATOM 9063 C CG . ARG B 2 239 ? 11.709 7.013 29.985 1.00 96.90 ? 239 ARG B CG 1 ATOM 9064 C CD . ARG B 2 239 ? 11.970 5.975 31.067 1.00 89.16 ? 239 ARG B CD 1 ATOM 9065 N NE . ARG B 2 239 ? 11.534 6.429 32.384 1.00 86.84 ? 239 ARG B NE 1 ATOM 9066 C CZ . ARG B 2 239 ? 11.661 5.717 33.499 1.00 92.08 ? 239 ARG B CZ 1 ATOM 9067 N NH1 . ARG B 2 239 ? 12.213 4.512 33.460 1.00 93.71 ? 239 ARG B NH1 1 ATOM 9068 N NH2 . ARG B 2 239 ? 11.237 6.210 34.655 1.00 85.85 ? 239 ARG B NH2 1 ATOM 9069 N N . ASN B 2 240 ? 7.863 7.117 28.009 1.00 88.43 ? 240 ASN B N 1 ATOM 9070 C CA . ASN B 2 240 ? 6.430 6.954 27.821 1.00 102.13 ? 240 ASN B CA 1 ATOM 9071 C C . ASN B 2 240 ? 5.889 5.939 28.817 1.00 114.01 ? 240 ASN B C 1 ATOM 9072 O O . ASN B 2 240 ? 6.624 5.062 29.275 1.00 113.94 ? 240 ASN B O 1 ATOM 9073 C CB . ASN B 2 240 ? 6.114 6.531 26.386 1.00 106.81 ? 240 ASN B CB 1 ATOM 9074 C CG . ASN B 2 240 ? 7.012 5.413 25.896 1.00 117.84 ? 240 ASN B CG 1 ATOM 9075 O OD1 . ASN B 2 240 ? 8.184 5.337 26.264 1.00 122.69 ? 240 ASN B OD1 1 ATOM 9076 N ND2 . ASN B 2 240 ? 6.465 4.539 25.059 1.00 119.38 ? 240 ASN B ND2 1 ATOM 9077 N N . ASP B 2 241 ? 4.607 6.070 29.150 1.00 122.42 ? 241 ASP B N 1 ATOM 9078 C CA . ASP B 2 241 ? 3.981 5.276 30.205 1.00 115.59 ? 241 ASP B CA 1 ATOM 9079 C C . ASP B 2 241 ? 4.739 5.446 31.517 1.00 106.07 ? 241 ASP B C 1 ATOM 9080 O O . ASP B 2 241 ? 4.976 4.483 32.247 1.00 91.20 ? 241 ASP B O 1 ATOM 9081 C CB . ASP B 2 241 ? 3.904 3.799 29.812 1.00 110.03 ? 241 ASP B CB 1 ATOM 9082 C CG . ASP B 2 241 ? 2.964 3.557 28.648 1.00 110.13 ? 241 ASP B CG 1 ATOM 9083 O OD1 . ASP B 2 241 ? 3.429 3.593 27.490 1.00 104.57 ? 241 ASP B OD1 1 ATOM 9084 O OD2 . ASP B 2 241 ? 1.759 3.337 28.893 1.00 116.58 ? 241 ASP B OD2 1 ATOM 9085 N N . ALA B 2 242 ? 5.119 6.688 31.799 1.00 99.31 ? 242 ALA B N 1 ATOM 9086 C CA . ALA B 2 242 ? 5.803 7.037 33.036 1.00 95.20 ? 242 ALA B CA 1 ATOM 9087 C C . ALA B 2 242 ? 5.418 8.452 33.448 1.00 80.96 ? 242 ALA B C 1 ATOM 9088 O O . ALA B 2 242 ? 5.196 9.310 32.595 1.00 79.72 ? 242 ALA B O 1 ATOM 9089 C CB . ALA B 2 242 ? 7.309 6.917 32.870 1.00 84.49 ? 242 ALA B CB 1 ATOM 9090 N N . SER B 2 243 ? 5.331 8.692 34.752 1.00 79.75 ? 243 SER B N 1 ATOM 9091 C CA . SER B 2 243 ? 4.967 10.013 35.251 1.00 84.54 ? 243 SER B CA 1 ATOM 9092 C C . SER B 2 243 ? 6.050 11.036 34.930 1.00 87.80 ? 243 SER B C 1 ATOM 9093 O O . SER B 2 243 ? 7.222 10.838 35.252 1.00 88.65 ? 243 SER B O 1 ATOM 9094 C CB . SER B 2 243 ? 4.712 9.972 36.758 1.00 76.54 ? 243 SER B CB 1 ATOM 9095 O OG . SER B 2 243 ? 3.492 9.313 37.049 1.00 78.28 ? 243 SER B OG 1 ATOM 9096 N N . HIS B 2 244 ? 5.647 12.130 34.294 1.00 82.00 ? 244 HIS B N 1 ATOM 9097 C CA . HIS B 2 244 ? 6.581 13.175 33.904 1.00 72.80 ? 244 HIS B CA 1 ATOM 9098 C C . HIS B 2 244 ? 6.513 14.349 34.869 1.00 69.90 ? 244 HIS B C 1 ATOM 9099 O O . HIS B 2 244 ? 5.507 15.054 34.935 1.00 69.54 ? 244 HIS B O 1 ATOM 9100 C CB . HIS B 2 244 ? 6.292 13.648 32.479 1.00 78.06 ? 244 HIS B CB 1 ATOM 9101 C CG . HIS B 2 244 ? 6.293 12.547 31.466 1.00 85.70 ? 244 HIS B CG 1 ATOM 9102 N ND1 . HIS B 2 244 ? 5.460 12.546 30.368 1.00 90.41 ? 244 HIS B ND1 1 ATOM 9103 C CD2 . HIS B 2 244 ? 7.028 11.413 31.384 1.00 87.26 ? 244 HIS B CD2 1 ATOM 9104 C CE1 . HIS B 2 244 ? 5.680 11.456 29.654 1.00 90.86 ? 244 HIS B CE1 1 ATOM 9105 N NE2 . HIS B 2 244 ? 6.625 10.752 30.248 1.00 93.48 ? 244 HIS B NE2 1 ATOM 9106 N N . LEU B 2 245 ? 7.590 14.552 35.619 1.00 70.59 ? 245 LEU B N 1 ATOM 9107 C CA . LEU B 2 245 ? 7.650 15.645 36.578 1.00 65.73 ? 245 LEU B CA 1 ATOM 9108 C C . LEU B 2 245 ? 8.713 16.662 36.190 1.00 79.28 ? 245 LEU B C 1 ATOM 9109 O O . LEU B 2 245 ? 9.900 16.343 36.132 1.00 91.74 ? 245 LEU B O 1 ATOM 9110 C CB . LEU B 2 245 ? 7.926 15.112 37.986 1.00 66.53 ? 245 LEU B CB 1 ATOM 9111 C CG . LEU B 2 245 ? 6.835 14.241 38.611 1.00 68.02 ? 245 LEU B CG 1 ATOM 9112 C CD1 . LEU B 2 245 ? 7.197 13.882 40.043 1.00 78.56 ? 245 LEU B CD1 1 ATOM 9113 C CD2 . LEU B 2 245 ? 5.488 14.943 38.554 1.00 67.07 ? 245 LEU B CD2 1 ATOM 9114 N N . LEU B 2 246 ? 8.278 17.886 35.915 1.00 76.45 ? 246 LEU B N 1 ATOM 9115 C CA . LEU B 2 246 ? 9.205 18.978 35.664 1.00 60.76 ? 246 LEU B CA 1 ATOM 9116 C C . LEU B 2 246 ? 9.176 19.941 36.844 1.00 59.35 ? 246 LEU B C 1 ATOM 9117 O O . LEU B 2 246 ? 8.202 20.666 37.041 1.00 62.48 ? 246 LEU B O 1 ATOM 9118 C CB . LEU B 2 246 ? 8.853 19.704 34.364 1.00 59.87 ? 246 LEU B CB 1 ATOM 9119 C CG . LEU B 2 246 ? 9.804 20.820 33.930 1.00 58.53 ? 246 LEU B CG 1 ATOM 9120 C CD1 . LEU B 2 246 ? 11.209 20.275 33.735 1.00 59.74 ? 246 LEU B CD1 1 ATOM 9121 C CD2 . LEU B 2 246 ? 9.304 21.490 32.659 1.00 65.79 ? 246 LEU B CD2 1 ATOM 9122 N N . VAL B 2 247 ? 10.249 19.946 37.626 1.00 59.63 ? 247 VAL B N 1 ATOM 9123 C CA . VAL B 2 247 ? 10.306 20.772 38.824 1.00 62.74 ? 247 VAL B CA 1 ATOM 9124 C C . VAL B 2 247 ? 11.079 22.060 38.552 1.00 78.53 ? 247 VAL B C 1 ATOM 9125 O O . VAL B 2 247 ? 12.181 22.038 38.002 1.00 84.63 ? 247 VAL B O 1 ATOM 9126 C CB . VAL B 2 247 ? 10.937 20.003 40.005 1.00 67.08 ? 247 VAL B CB 1 ATOM 9127 C CG1 . VAL B 2 247 ? 12.151 19.219 39.543 1.00 61.79 ? 247 VAL B CG1 1 ATOM 9128 C CG2 . VAL B 2 247 ? 11.289 20.951 41.146 1.00 87.86 ? 247 VAL B CG2 1 ATOM 9129 N N . PHE B 2 248 ? 10.479 23.181 38.936 1.00 78.63 ? 248 PHE B N 1 ATOM 9130 C CA . PHE B 2 248 ? 11.006 24.502 38.622 1.00 56.20 ? 248 PHE B CA 1 ATOM 9131 C C . PHE B 2 248 ? 11.424 25.242 39.890 1.00 61.03 ? 248 PHE B C 1 ATOM 9132 O O . PHE B 2 248 ? 10.636 25.369 40.827 1.00 87.08 ? 248 PHE B O 1 ATOM 9133 C CB . PHE B 2 248 ? 9.953 25.304 37.853 1.00 56.09 ? 248 PHE B CB 1 ATOM 9134 C CG . PHE B 2 248 ? 10.432 26.637 37.364 1.00 58.69 ? 248 PHE B CG 1 ATOM 9135 C CD1 . PHE B 2 248 ? 11.132 26.742 36.174 1.00 70.65 ? 248 PHE B CD1 1 ATOM 9136 C CD2 . PHE B 2 248 ? 10.161 27.791 38.080 1.00 65.73 ? 248 PHE B CD2 1 ATOM 9137 C CE1 . PHE B 2 248 ? 11.566 27.969 35.715 1.00 83.04 ? 248 PHE B CE1 1 ATOM 9138 C CE2 . PHE B 2 248 ? 10.593 29.021 37.627 1.00 72.61 ? 248 PHE B CE2 1 ATOM 9139 C CZ . PHE B 2 248 ? 11.296 29.111 36.443 1.00 86.42 ? 248 PHE B CZ 1 ATOM 9140 N N . THR B 2 249 ? 12.663 25.724 39.920 1.00 55.58 ? 249 THR B N 1 ATOM 9141 C CA . THR B 2 249 ? 13.161 26.462 41.078 1.00 62.20 ? 249 THR B CA 1 ATOM 9142 C C . THR B 2 249 ? 13.729 27.823 40.692 1.00 67.44 ? 249 THR B C 1 ATOM 9143 O O . THR B 2 249 ? 14.485 27.941 39.728 1.00 90.28 ? 249 THR B O 1 ATOM 9144 C CB . THR B 2 249 ? 14.251 25.674 41.834 1.00 74.26 ? 249 THR B CB 1 ATOM 9145 O OG1 . THR B 2 249 ? 15.360 25.425 40.961 1.00 87.89 ? 249 THR B OG1 1 ATOM 9146 C CG2 . THR B 2 249 ? 13.701 24.352 42.347 1.00 82.71 ? 249 THR B CG2 1 ATOM 9147 N N . THR B 2 250 ? 13.358 28.849 41.452 1.00 55.02 ? 250 THR B N 1 ATOM 9148 C CA . THR B 2 250 ? 13.879 30.191 41.229 1.00 54.16 ? 250 THR B CA 1 ATOM 9149 C C . THR B 2 250 ? 13.868 31.019 42.510 1.00 56.20 ? 250 THR B C 1 ATOM 9150 O O . THR B 2 250 ? 13.071 30.775 43.417 1.00 53.90 ? 250 THR B O 1 ATOM 9151 C CB . THR B 2 250 ? 13.078 30.935 40.149 1.00 61.02 ? 250 THR B CB 1 ATOM 9152 O OG1 . THR B 2 250 ? 13.545 32.287 40.052 1.00 67.09 ? 250 THR B OG1 1 ATOM 9153 C CG2 . THR B 2 250 ? 11.604 30.939 40.497 1.00 68.66 ? 250 THR B CG2 1 ATOM 9154 N N . ASP B 2 251 ? 14.764 31.997 42.572 1.00 80.22 ? 251 ASP B N 1 ATOM 9155 C CA . ASP B 2 251 ? 14.873 32.883 43.724 1.00 69.23 ? 251 ASP B CA 1 ATOM 9156 C C . ASP B 2 251 ? 13.809 33.974 43.683 1.00 59.71 ? 251 ASP B C 1 ATOM 9157 O O . ASP B 2 251 ? 13.313 34.416 44.720 1.00 54.05 ? 251 ASP B O 1 ATOM 9158 C CB . ASP B 2 251 ? 16.267 33.515 43.774 1.00 63.16 ? 251 ASP B CB 1 ATOM 9159 C CG . ASP B 2 251 ? 16.704 33.862 45.183 1.00 96.05 ? 251 ASP B CG 1 ATOM 9160 O OD1 . ASP B 2 251 ? 17.248 34.969 45.383 1.00 107.43 ? 251 ASP B OD1 1 ATOM 9161 O OD2 . ASP B 2 251 ? 16.515 33.024 46.088 1.00 110.01 ? 251 ASP B OD2 1 ATOM 9162 N N . ALA B 2 252 ? 13.452 34.389 42.473 1.00 54.90 ? 252 ALA B N 1 ATOM 9163 C CA . ALA B 2 252 ? 12.634 35.580 42.275 1.00 62.69 ? 252 ALA B CA 1 ATOM 9164 C C . ALA B 2 252 ? 11.585 35.381 41.187 1.00 59.12 ? 252 ALA B C 1 ATOM 9165 O O . ALA B 2 252 ? 11.353 34.264 40.727 1.00 60.22 ? 252 ALA B O 1 ATOM 9166 C CB . ALA B 2 252 ? 13.518 36.772 41.940 1.00 74.18 ? 252 ALA B CB 1 ATOM 9167 N N . LYS B 2 253 ? 10.952 36.480 40.788 1.00 54.42 ? 253 LYS B N 1 ATOM 9168 C CA . LYS B 2 253 ? 9.884 36.445 39.797 1.00 53.40 ? 253 LYS B CA 1 ATOM 9169 C C . LYS B 2 253 ? 10.422 36.113 38.409 1.00 50.20 ? 253 LYS B C 1 ATOM 9170 O O . LYS B 2 253 ? 11.624 35.919 38.229 1.00 50.73 ? 253 LYS B O 1 ATOM 9171 C CB . LYS B 2 253 ? 9.148 37.785 39.771 1.00 57.30 ? 253 LYS B CB 1 ATOM 9172 C CG . LYS B 2 253 ? 10.071 38.993 39.740 1.00 62.54 ? 253 LYS B CG 1 ATOM 9173 C CD . LYS B 2 253 ? 9.300 40.283 39.964 1.00 72.96 ? 253 LYS B CD 1 ATOM 9174 C CE . LYS B 2 253 ? 10.239 41.473 40.061 1.00 76.75 ? 253 LYS B CE 1 ATOM 9175 N NZ . LYS B 2 253 ? 9.507 42.749 40.293 1.00 73.73 ? 253 LYS B NZ 1 ATOM 9176 N N . THR B 2 254 ? 9.528 36.052 37.428 1.00 49.61 ? 254 THR B N 1 ATOM 9177 C CA . THR B 2 254 ? 9.906 35.594 36.097 1.00 54.71 ? 254 THR B CA 1 ATOM 9178 C C . THR B 2 254 ? 9.372 36.465 34.971 1.00 53.66 ? 254 THR B C 1 ATOM 9179 O O . THR B 2 254 ? 8.368 37.162 35.124 1.00 61.98 ? 254 THR B O 1 ATOM 9180 C CB . THR B 2 254 ? 9.421 34.156 35.846 1.00 63.30 ? 254 THR B CB 1 ATOM 9181 O OG1 . THR B 2 254 ? 9.597 33.830 34.461 1.00 65.50 ? 254 THR B OG1 1 ATOM 9182 C CG2 . THR B 2 254 ? 7.949 34.024 36.201 1.00 46.34 ? 254 THR B CG2 1 ATOM 9183 N N . HIS B 2 255 ? 10.062 36.413 33.836 1.00 48.12 ? 255 HIS B N 1 ATOM 9184 C CA . HIS B 2 255 ? 9.591 37.051 32.618 1.00 49.24 ? 255 HIS B CA 1 ATOM 9185 C C . HIS B 2 255 ? 8.376 36.326 32.068 1.00 51.69 ? 255 HIS B C 1 ATOM 9186 O O . HIS B 2 255 ? 8.323 35.096 32.059 1.00 53.98 ? 255 HIS B O 1 ATOM 9187 C CB . HIS B 2 255 ? 10.688 37.078 31.554 1.00 51.50 ? 255 HIS B CB 1 ATOM 9188 C CG . HIS B 2 255 ? 11.675 38.187 31.728 1.00 51.83 ? 255 HIS B CG 1 ATOM 9189 N ND1 . HIS B 2 255 ? 11.333 39.514 31.587 1.00 73.11 ? 255 HIS B ND1 1 ATOM 9190 C CD2 . HIS B 2 255 ? 12.998 38.166 32.014 1.00 46.35 ? 255 HIS B CD2 1 ATOM 9191 C CE1 . HIS B 2 255 ? 12.402 40.265 31.787 1.00 75.08 ? 255 HIS B CE1 1 ATOM 9192 N NE2 . HIS B 2 255 ? 13.425 39.471 32.048 1.00 56.69 ? 255 HIS B NE2 1 ATOM 9193 N N . ILE B 2 256 ? 7.398 37.098 31.615 1.00 51.83 ? 256 ILE B N 1 ATOM 9194 C CA . ILE B 2 256 ? 6.271 36.552 30.880 1.00 52.98 ? 256 ILE B CA 1 ATOM 9195 C C . ILE B 2 256 ? 6.439 36.904 29.408 1.00 50.27 ? 256 ILE B C 1 ATOM 9196 O O . ILE B 2 256 ? 7.447 37.497 29.022 1.00 44.87 ? 256 ILE B O 1 ATOM 9197 C CB . ILE B 2 256 ? 4.936 37.087 31.411 1.00 59.38 ? 256 ILE B CB 1 ATOM 9198 C CG1 . ILE B 2 256 ? 4.941 38.616 31.403 1.00 44.93 ? 256 ILE B CG1 1 ATOM 9199 C CG2 . ILE B 2 256 ? 4.684 36.567 32.819 1.00 45.66 ? 256 ILE B CG2 1 ATOM 9200 C CD1 . ILE B 2 256 ? 3.743 39.231 32.083 1.00 45.43 ? 256 ILE B CD1 1 ATOM 9201 N N . ALA B 2 257 ? 5.465 36.534 28.585 1.00 52.83 ? 257 ALA B N 1 ATOM 9202 C CA . ALA B 2 257 ? 5.520 36.863 27.167 1.00 46.52 ? 257 ALA B CA 1 ATOM 9203 C C . ALA B 2 257 ? 5.370 38.368 26.959 1.00 48.57 ? 257 ALA B C 1 ATOM 9204 O O . ALA B 2 257 ? 4.869 39.073 27.838 1.00 47.52 ? 257 ALA B O 1 ATOM 9205 C CB . ALA B 2 257 ? 4.450 36.106 26.403 1.00 50.37 ? 257 ALA B CB 1 ATOM 9206 N N . LEU B 2 258 ? 5.833 38.839 25.800 1.00 46.26 ? 258 LEU B N 1 ATOM 9207 C CA . LEU B 2 258 ? 5.817 40.254 25.405 1.00 56.61 ? 258 LEU B CA 1 ATOM 9208 C C . LEU B 2 258 ? 6.835 41.106 26.171 1.00 58.09 ? 258 LEU B C 1 ATOM 9209 O O . LEU B 2 258 ? 6.997 42.292 25.880 1.00 55.62 ? 258 LEU B O 1 ATOM 9210 C CB . LEU B 2 258 ? 4.415 40.856 25.559 1.00 46.48 ? 258 LEU B CB 1 ATOM 9211 C CG . LEU B 2 258 ? 3.315 40.268 24.674 1.00 54.50 ? 258 LEU B CG 1 ATOM 9212 C CD1 . LEU B 2 258 ? 1.992 40.967 24.934 1.00 61.39 ? 258 LEU B CD1 1 ATOM 9213 C CD2 . LEU B 2 258 ? 3.696 40.366 23.206 1.00 55.29 ? 258 LEU B CD2 1 ATOM 9214 N N . ASP B 2 259 ? 7.519 40.506 27.141 1.00 51.97 ? 259 ASP B N 1 ATOM 9215 C CA . ASP B 2 259 ? 8.579 41.203 27.866 1.00 44.31 ? 259 ASP B CA 1 ATOM 9216 C C . ASP B 2 259 ? 9.799 41.420 26.979 1.00 44.15 ? 259 ASP B C 1 ATOM 9217 O O . ASP B 2 259 ? 10.542 42.386 27.153 1.00 51.84 ? 259 ASP B O 1 ATOM 9218 C CB . ASP B 2 259 ? 8.989 40.424 29.119 1.00 54.92 ? 259 ASP B CB 1 ATOM 9219 C CG . ASP B 2 259 ? 8.047 40.651 30.282 1.00 66.39 ? 259 ASP B CG 1 ATOM 9220 O OD1 . ASP B 2 259 ? 7.329 41.672 30.275 1.00 71.34 ? 259 ASP B OD1 1 ATOM 9221 O OD2 . ASP B 2 259 ? 8.032 39.813 31.209 1.00 74.69 ? 259 ASP B OD2 1 ATOM 9222 N N . GLY B 2 260 ? 9.995 40.517 26.025 1.00 44.86 ? 260 GLY B N 1 ATOM 9223 C CA . GLY B 2 260 ? 11.173 40.534 25.177 1.00 46.52 ? 260 GLY B CA 1 ATOM 9224 C C . GLY B 2 260 ? 11.244 41.692 24.201 1.00 46.56 ? 260 GLY B C 1 ATOM 9225 O O . GLY B 2 260 ? 12.274 41.899 23.559 1.00 56.54 ? 260 GLY B O 1 ATOM 9226 N N . ARG B 2 261 ? 10.158 42.450 24.086 1.00 47.55 ? 261 ARG B N 1 ATOM 9227 C CA . ARG B 2 261 ? 10.117 43.582 23.165 1.00 46.97 ? 261 ARG B CA 1 ATOM 9228 C C . ARG B 2 261 ? 11.156 44.632 23.545 1.00 48.71 ? 261 ARG B C 1 ATOM 9229 O O . ARG B 2 261 ? 11.724 45.298 22.678 1.00 55.22 ? 261 ARG B O 1 ATOM 9230 C CB . ARG B 2 261 ? 8.722 44.205 23.136 1.00 50.85 ? 261 ARG B CB 1 ATOM 9231 C CG . ARG B 2 261 ? 8.572 45.319 22.116 1.00 46.39 ? 261 ARG B CG 1 ATOM 9232 C CD . ARG B 2 261 ? 7.162 45.878 22.092 1.00 46.74 ? 261 ARG B CD 1 ATOM 9233 N NE . ARG B 2 261 ? 7.039 46.970 21.131 1.00 53.31 ? 261 ARG B NE 1 ATOM 9234 C CZ . ARG B 2 261 ? 5.920 47.649 20.907 1.00 60.46 ? 261 ARG B CZ 1 ATOM 9235 N NH1 . ARG B 2 261 ? 4.816 47.350 21.578 1.00 76.89 ? 261 ARG B NH1 1 ATOM 9236 N NH2 . ARG B 2 261 ? 5.904 48.627 20.013 1.00 59.11 ? 261 ARG B NH2 1 ATOM 9237 N N . LEU B 2 262 ? 11.401 44.769 24.844 1.00 52.37 ? 262 LEU B N 1 ATOM 9238 C CA . LEU B 2 262 ? 12.440 45.663 25.344 1.00 57.88 ? 262 LEU B CA 1 ATOM 9239 C C . LEU B 2 262 ? 13.800 45.253 24.796 1.00 63.48 ? 262 LEU B C 1 ATOM 9240 O O . LEU B 2 262 ? 14.618 46.098 24.434 1.00 83.36 ? 262 LEU B O 1 ATOM 9241 C CB . LEU B 2 262 ? 12.468 45.663 26.873 1.00 44.36 ? 262 LEU B CB 1 ATOM 9242 C CG . LEU B 2 262 ? 11.549 46.637 27.616 1.00 44.41 ? 262 LEU B CG 1 ATOM 9243 C CD1 . LEU B 2 262 ? 10.086 46.422 27.259 1.00 43.87 ? 262 LEU B CD1 1 ATOM 9244 C CD2 . LEU B 2 262 ? 11.757 46.515 29.118 1.00 56.46 ? 262 LEU B CD2 1 ATOM 9245 N N . ALA B 2 263 ? 14.026 43.944 24.727 1.00 49.34 ? 263 ALA B N 1 ATOM 9246 C CA . ALA B 2 263 ? 15.266 43.398 24.189 1.00 48.30 ? 263 ALA B CA 1 ATOM 9247 C C . ALA B 2 263 ? 15.321 43.532 22.672 1.00 48.73 ? 263 ALA B C 1 ATOM 9248 O O . ALA B 2 263 ? 16.339 43.229 22.051 1.00 52.19 ? 263 ALA B O 1 ATOM 9249 C CB . ALA B 2 263 ? 15.423 41.942 24.594 1.00 54.19 ? 263 ALA B CB 1 ATOM 9250 N N . GLY B 2 264 ? 14.222 43.984 22.079 1.00 47.55 ? 264 GLY B N 1 ATOM 9251 C CA . GLY B 2 264 ? 14.127 44.081 20.636 1.00 73.91 ? 264 GLY B CA 1 ATOM 9252 C C . GLY B 2 264 ? 13.684 42.764 20.033 1.00 56.23 ? 264 GLY B C 1 ATOM 9253 O O . GLY B 2 264 ? 14.037 42.435 18.900 1.00 54.16 ? 264 GLY B O 1 ATOM 9254 N N . ILE B 2 265 ? 12.911 42.002 20.800 1.00 55.40 ? 265 ILE B N 1 ATOM 9255 C CA . ILE B 2 265 ? 12.427 40.711 20.335 1.00 54.98 ? 265 ILE B CA 1 ATOM 9256 C C . ILE B 2 265 ? 10.922 40.741 20.084 1.00 54.09 ? 265 ILE B C 1 ATOM 9257 O O . ILE B 2 265 ? 10.124 40.754 21.021 1.00 52.69 ? 265 ILE B O 1 ATOM 9258 C CB . ILE B 2 265 ? 12.741 39.607 21.350 1.00 51.52 ? 265 ILE B CB 1 ATOM 9259 C CG1 . ILE B 2 265 ? 14.211 39.670 21.773 1.00 49.20 ? 265 ILE B CG1 1 ATOM 9260 C CG2 . ILE B 2 265 ? 12.405 38.264 20.768 1.00 50.13 ? 265 ILE B CG2 1 ATOM 9261 C CD1 . ILE B 2 265 ? 14.570 38.693 22.872 1.00 48.98 ? 265 ILE B CD1 1 ATOM 9262 N N . VAL B 2 266 ? 10.547 40.751 18.810 1.00 56.15 ? 266 VAL B N 1 ATOM 9263 C CA . VAL B 2 266 ? 9.143 40.810 18.417 1.00 57.43 ? 266 VAL B CA 1 ATOM 9264 C C . VAL B 2 266 ? 8.544 39.466 18.008 1.00 59.80 ? 266 VAL B C 1 ATOM 9265 O O . VAL B 2 266 ? 7.350 39.381 17.724 1.00 61.20 ? 266 VAL B O 1 ATOM 9266 C CB . VAL B 2 266 ? 8.954 41.788 17.254 1.00 65.92 ? 266 VAL B CB 1 ATOM 9267 C CG1 . VAL B 2 266 ? 9.339 43.192 17.686 1.00 55.72 ? 266 VAL B CG1 1 ATOM 9268 C CG2 . VAL B 2 266 ? 9.789 41.344 16.068 1.00 81.62 ? 266 VAL B CG2 1 ATOM 9269 N N . GLN B 2 267 ? 9.364 38.420 17.975 1.00 65.78 ? 267 GLN B N 1 ATOM 9270 C CA . GLN B 2 267 ? 8.904 37.130 17.467 1.00 74.55 ? 267 GLN B CA 1 ATOM 9271 C C . GLN B 2 267 ? 8.312 36.265 18.571 1.00 65.96 ? 267 GLN B C 1 ATOM 9272 O O . GLN B 2 267 ? 8.991 35.948 19.548 1.00 72.66 ? 267 GLN B O 1 ATOM 9273 C CB . GLN B 2 267 ? 10.045 36.378 16.778 1.00 79.49 ? 267 GLN B CB 1 ATOM 9274 C CG . GLN B 2 267 ? 9.595 35.095 16.092 1.00 72.56 ? 267 GLN B CG 1 ATOM 9275 C CD . GLN B 2 267 ? 10.746 34.319 15.484 1.00 93.30 ? 267 GLN B CD 1 ATOM 9276 O OE1 . GLN B 2 267 ? 11.636 33.849 16.193 1.00 112.10 ? 267 GLN B OE1 1 ATOM 9277 N NE2 . GLN B 2 267 ? 10.733 34.178 14.163 1.00 99.83 ? 267 GLN B NE2 1 ATOM 9278 N N . PRO B 2 268 ? 7.039 35.874 18.413 1.00 61.88 ? 268 PRO B N 1 ATOM 9279 C CA . PRO B 2 268 ? 6.346 35.056 19.411 1.00 61.88 ? 268 PRO B CA 1 ATOM 9280 C C . PRO B 2 268 ? 6.971 33.674 19.521 1.00 62.85 ? 268 PRO B C 1 ATOM 9281 O O . PRO B 2 268 ? 7.517 33.176 18.537 1.00 72.10 ? 268 PRO B O 1 ATOM 9282 C CB . PRO B 2 268 ? 4.913 34.960 18.868 1.00 55.70 ? 268 PRO B CB 1 ATOM 9283 C CG . PRO B 2 268 ? 4.815 36.007 17.805 1.00 56.88 ? 268 PRO B CG 1 ATOM 9284 C CD . PRO B 2 268 ? 6.189 36.149 17.244 1.00 64.46 ? 268 PRO B CD 1 ATOM 9285 N N . ASN B 2 269 ? 6.895 33.070 20.701 1.00 60.40 ? 269 ASN B N 1 ATOM 9286 C CA . ASN B 2 269 ? 7.407 31.722 20.892 1.00 58.91 ? 269 ASN B CA 1 ATOM 9287 C C . ASN B 2 269 ? 6.634 30.740 20.020 1.00 61.36 ? 269 ASN B C 1 ATOM 9288 O O . ASN B 2 269 ? 5.405 30.693 20.064 1.00 62.73 ? 269 ASN B O 1 ATOM 9289 C CB . ASN B 2 269 ? 7.321 31.320 22.366 1.00 61.19 ? 269 ASN B CB 1 ATOM 9290 C CG . ASN B 2 269 ? 8.224 30.150 22.708 1.00 64.78 ? 269 ASN B CG 1 ATOM 9291 O OD1 . ASN B 2 269 ? 8.266 29.149 21.993 1.00 79.87 ? 269 ASN B OD1 1 ATOM 9292 N ND2 . ASN B 2 269 ? 8.962 30.277 23.805 1.00 55.93 ? 269 ASN B ND2 1 ATOM 9293 N N . ASP B 2 270 ? 7.357 29.965 19.220 1.00 63.65 ? 270 ASP B N 1 ATOM 9294 C CA . ASP B 2 270 ? 6.727 29.030 18.296 1.00 76.65 ? 270 ASP B CA 1 ATOM 9295 C C . ASP B 2 270 ? 6.462 27.683 18.962 1.00 78.16 ? 270 ASP B C 1 ATOM 9296 O O . ASP B 2 270 ? 5.766 26.831 18.409 1.00 87.33 ? 270 ASP B O 1 ATOM 9297 C CB . ASP B 2 270 ? 7.594 28.847 17.048 1.00 84.28 ? 270 ASP B CB 1 ATOM 9298 C CG . ASP B 2 270 ? 8.989 28.350 17.373 1.00 81.16 ? 270 ASP B CG 1 ATOM 9299 O OD1 . ASP B 2 270 ? 9.391 28.420 18.553 1.00 82.65 ? 270 ASP B OD1 1 ATOM 9300 O OD2 . ASP B 2 270 ? 9.688 27.897 16.442 1.00 77.58 ? 270 ASP B OD2 1 ATOM 9301 N N . GLY B 2 271 ? 7.021 27.499 20.154 1.00 71.36 ? 271 GLY B N 1 ATOM 9302 C CA . GLY B 2 271 ? 6.802 26.287 20.921 1.00 68.62 ? 271 GLY B CA 1 ATOM 9303 C C . GLY B 2 271 ? 7.447 25.058 20.311 1.00 70.74 ? 271 GLY B C 1 ATOM 9304 O O . GLY B 2 271 ? 7.015 23.933 20.564 1.00 79.33 ? 271 GLY B O 1 ATOM 9305 N N . GLN B 2 272 ? 8.481 25.269 19.504 1.00 71.82 ? 272 GLN B N 1 ATOM 9306 C CA . GLN B 2 272 ? 9.218 24.162 18.908 1.00 77.10 ? 272 GLN B CA 1 ATOM 9307 C C . GLN B 2 272 ? 10.484 23.888 19.711 1.00 89.38 ? 272 GLN B C 1 ATOM 9308 O O . GLN B 2 272 ? 10.763 24.582 20.688 1.00 102.76 ? 272 GLN B O 1 ATOM 9309 C CB . GLN B 2 272 ? 9.565 24.466 17.449 1.00 77.88 ? 272 GLN B CB 1 ATOM 9310 C CG . GLN B 2 272 ? 8.373 24.894 16.608 1.00 82.32 ? 272 GLN B CG 1 ATOM 9311 C CD . GLN B 2 272 ? 7.257 23.868 16.609 1.00 110.09 ? 272 GLN B CD 1 ATOM 9312 O OE1 . GLN B 2 272 ? 6.084 24.210 16.760 1.00 127.01 ? 272 GLN B OE1 1 ATOM 9313 N NE2 . GLN B 2 272 ? 7.616 22.601 16.432 1.00 114.67 ? 272 GLN B NE2 1 ATOM 9314 N N . CYS B 2 273 ? 11.252 22.884 19.299 1.00 79.89 ? 273 CYS B N 1 ATOM 9315 C CA . CYS B 2 273 ? 12.488 22.556 20.000 1.00 76.92 ? 273 CYS B CA 1 ATOM 9316 C C . CYS B 2 273 ? 13.696 23.101 19.253 1.00 84.27 ? 273 CYS B C 1 ATOM 9317 O O . CYS B 2 273 ? 14.074 22.590 18.199 1.00 99.69 ? 273 CYS B O 1 ATOM 9318 C CB . CYS B 2 273 ? 12.622 21.044 20.179 1.00 78.55 ? 273 CYS B CB 1 ATOM 9319 S SG . CYS B 2 273 ? 14.229 20.516 20.818 1.00 97.82 ? 273 CYS B SG 1 ATOM 9320 N N . HIS B 2 274 ? 14.294 24.146 19.811 1.00 81.51 ? 274 HIS B N 1 ATOM 9321 C CA . HIS B 2 274 ? 15.456 24.783 19.208 1.00 81.98 ? 274 HIS B CA 1 ATOM 9322 C C . HIS B 2 274 ? 16.770 24.340 19.848 1.00 91.80 ? 274 HIS B C 1 ATOM 9323 O O . HIS B 2 274 ? 17.841 24.814 19.471 1.00 105.41 ? 274 HIS B O 1 ATOM 9324 C CB . HIS B 2 274 ? 15.306 26.301 19.283 1.00 84.74 ? 274 HIS B CB 1 ATOM 9325 C CG . HIS B 2 274 ? 14.040 26.804 18.662 1.00 85.92 ? 274 HIS B CG 1 ATOM 9326 N ND1 . HIS B 2 274 ? 13.847 26.846 17.298 1.00 86.44 ? 274 HIS B ND1 1 ATOM 9327 C CD2 . HIS B 2 274 ? 12.897 27.271 19.219 1.00 90.01 ? 274 HIS B CD2 1 ATOM 9328 C CE1 . HIS B 2 274 ? 12.643 27.325 17.041 1.00 94.64 ? 274 HIS B CE1 1 ATOM 9329 N NE2 . HIS B 2 274 ? 12.046 27.591 18.189 1.00 94.56 ? 274 HIS B NE2 1 ATOM 9330 N N . VAL B 2 275 ? 16.685 23.436 20.821 1.00 88.59 ? 275 VAL B N 1 ATOM 9331 C CA . VAL B 2 275 ? 17.879 22.937 21.494 1.00 82.21 ? 275 VAL B CA 1 ATOM 9332 C C . VAL B 2 275 ? 18.690 22.050 20.558 1.00 85.00 ? 275 VAL B C 1 ATOM 9333 O O . VAL B 2 275 ? 18.180 21.067 20.021 1.00 87.91 ? 275 VAL B O 1 ATOM 9334 C CB . VAL B 2 275 ? 17.527 22.145 22.767 1.00 81.38 ? 275 VAL B CB 1 ATOM 9335 C CG1 . VAL B 2 275 ? 18.793 21.652 23.451 1.00 70.36 ? 275 VAL B CG1 1 ATOM 9336 C CG2 . VAL B 2 275 ? 16.706 23.002 23.715 1.00 65.78 ? 275 VAL B CG2 1 ATOM 9337 N N . GLY B 2 276 ? 19.958 22.400 20.368 1.00 87.56 ? 276 GLY B N 1 ATOM 9338 C CA . GLY B 2 276 ? 20.821 21.669 19.458 1.00 98.61 ? 276 GLY B CA 1 ATOM 9339 C C . GLY B 2 276 ? 21.647 20.609 20.157 1.00 107.58 ? 276 GLY B C 1 ATOM 9340 O O . GLY B 2 276 ? 21.355 20.227 21.290 1.00 121.73 ? 276 GLY B O 1 ATOM 9341 N N . SER B 2 277 ? 22.685 20.133 19.476 1.00 98.89 ? 277 SER B N 1 ATOM 9342 C CA . SER B 2 277 ? 23.573 19.121 20.035 1.00 101.22 ? 277 SER B CA 1 ATOM 9343 C C . SER B 2 277 ? 24.486 19.723 21.098 1.00 97.40 ? 277 SER B C 1 ATOM 9344 O O . SER B 2 277 ? 25.072 19.007 21.909 1.00 106.73 ? 277 SER B O 1 ATOM 9345 C CB . SER B 2 277 ? 24.408 18.473 18.929 1.00 110.58 ? 277 SER B CB 1 ATOM 9346 O OG . SER B 2 277 ? 25.176 19.444 18.238 1.00 108.15 ? 277 SER B OG 1 ATOM 9347 N N . ASP B 2 278 ? 24.596 21.047 21.086 1.00 90.65 ? 278 ASP B N 1 ATOM 9348 C CA . ASP B 2 278 ? 25.436 21.764 22.037 1.00 91.43 ? 278 ASP B CA 1 ATOM 9349 C C . ASP B 2 278 ? 24.682 22.051 23.333 1.00 91.56 ? 278 ASP B C 1 ATOM 9350 O O . ASP B 2 278 ? 25.215 22.691 24.241 1.00 87.97 ? 278 ASP B O 1 ATOM 9351 C CB . ASP B 2 278 ? 25.946 23.066 21.418 1.00 100.28 ? 278 ASP B CB 1 ATOM 9352 C CG . ASP B 2 278 ? 24.829 23.909 20.834 1.00 102.36 ? 278 ASP B CG 1 ATOM 9353 O OD1 . ASP B 2 278 ? 24.397 24.870 21.502 1.00 87.75 ? 278 ASP B OD1 1 ATOM 9354 O OD2 . ASP B 2 278 ? 24.382 23.609 19.707 1.00 117.53 ? 278 ASP B OD2 1 ATOM 9355 N N . ASN B 2 279 ? 23.438 21.581 23.397 1.00 106.96 ? 279 ASN B N 1 ATOM 9356 C CA . ASN B 2 279 ? 22.593 21.708 24.583 1.00 99.29 ? 279 ASN B CA 1 ATOM 9357 C C . ASN B 2 279 ? 22.348 23.155 25.001 1.00 96.00 ? 279 ASN B C 1 ATOM 9358 O O . ASN B 2 279 ? 22.399 23.486 26.186 1.00 95.77 ? 279 ASN B O 1 ATOM 9359 C CB . ASN B 2 279 ? 23.198 20.928 25.753 1.00 91.37 ? 279 ASN B CB 1 ATOM 9360 C CG . ASN B 2 279 ? 23.331 19.447 25.460 1.00 95.35 ? 279 ASN B CG 1 ATOM 9361 O OD1 . ASN B 2 279 ? 22.519 18.871 24.737 1.00 92.17 ? 279 ASN B OD1 1 ATOM 9362 N ND2 . ASN B 2 279 ? 24.359 18.823 26.022 1.00 103.25 ? 279 ASN B ND2 1 ATOM 9363 N N . HIS B 2 280 ? 22.078 24.012 24.022 1.00 94.51 ? 280 HIS B N 1 ATOM 9364 C CA . HIS B 2 280 ? 21.748 25.407 24.289 1.00 88.55 ? 280 HIS B CA 1 ATOM 9365 C C . HIS B 2 280 ? 20.482 25.817 23.550 1.00 80.28 ? 280 HIS B C 1 ATOM 9366 O O . HIS B 2 280 ? 20.163 25.270 22.494 1.00 88.84 ? 280 HIS B O 1 ATOM 9367 C CB . HIS B 2 280 ? 22.902 26.328 23.883 1.00 99.69 ? 280 HIS B CB 1 ATOM 9368 C CG . HIS B 2 280 ? 24.085 26.258 24.797 1.00 118.00 ? 280 HIS B CG 1 ATOM 9369 N ND1 . HIS B 2 280 ? 25.372 26.500 24.366 1.00 130.78 ? 280 HIS B ND1 1 ATOM 9370 C CD2 . HIS B 2 280 ? 24.176 25.987 26.120 1.00 123.92 ? 280 HIS B CD2 1 ATOM 9371 C CE1 . HIS B 2 280 ? 26.205 26.373 25.382 1.00 135.82 ? 280 HIS B CE1 1 ATOM 9372 N NE2 . HIS B 2 280 ? 25.506 26.062 26.459 1.00 132.16 ? 280 HIS B NE2 1 ATOM 9373 N N . TYR B 2 281 ? 19.765 26.788 24.106 1.00 73.30 ? 281 TYR B N 1 ATOM 9374 C CA . TYR B 2 281 ? 18.597 27.338 23.437 1.00 73.60 ? 281 TYR B CA 1 ATOM 9375 C C . TYR B 2 281 ? 19.091 28.314 22.376 1.00 78.63 ? 281 TYR B C 1 ATOM 9376 O O . TYR B 2 281 ? 19.707 29.331 22.696 1.00 96.10 ? 281 TYR B O 1 ATOM 9377 C CB . TYR B 2 281 ? 17.678 28.030 24.449 1.00 74.55 ? 281 TYR B CB 1 ATOM 9378 C CG . TYR B 2 281 ? 16.331 28.475 23.916 1.00 72.16 ? 281 TYR B CG 1 ATOM 9379 C CD1 . TYR B 2 281 ? 15.873 28.064 22.670 1.00 80.64 ? 281 TYR B CD1 1 ATOM 9380 C CD2 . TYR B 2 281 ? 15.517 29.313 24.666 1.00 62.88 ? 281 TYR B CD2 1 ATOM 9381 C CE1 . TYR B 2 281 ? 14.642 28.477 22.190 1.00 67.10 ? 281 TYR B CE1 1 ATOM 9382 C CE2 . TYR B 2 281 ? 14.289 29.729 24.194 1.00 61.87 ? 281 TYR B CE2 1 ATOM 9383 C CZ . TYR B 2 281 ? 13.856 29.310 22.957 1.00 63.82 ? 281 TYR B CZ 1 ATOM 9384 O OH . TYR B 2 281 ? 12.631 29.726 22.489 1.00 67.46 ? 281 TYR B OH 1 ATOM 9385 N N . SER B 2 282 ? 18.812 28.006 21.114 1.00 73.51 ? 282 SER B N 1 ATOM 9386 C CA . SER B 2 282 ? 19.332 28.796 20.004 1.00 76.40 ? 282 SER B CA 1 ATOM 9387 C C . SER B 2 282 ? 18.505 30.054 19.785 1.00 86.12 ? 282 SER B C 1 ATOM 9388 O O . SER B 2 282 ? 19.035 31.107 19.430 1.00 100.39 ? 282 SER B O 1 ATOM 9389 C CB . SER B 2 282 ? 19.362 27.966 18.720 1.00 79.90 ? 282 SER B CB 1 ATOM 9390 O OG . SER B 2 282 ? 18.056 27.779 18.205 1.00 75.49 ? 282 SER B OG 1 ATOM 9391 N N . ALA B 2 283 ? 17.201 29.932 20.006 1.00 78.72 ? 283 ALA B N 1 ATOM 9392 C CA . ALA B 2 283 ? 16.271 31.019 19.740 1.00 78.12 ? 283 ALA B CA 1 ATOM 9393 C C . ALA B 2 283 ? 16.086 31.917 20.958 1.00 68.62 ? 283 ALA B C 1 ATOM 9394 O O . ALA B 2 283 ? 15.268 32.837 20.936 1.00 74.94 ? 283 ALA B O 1 ATOM 9395 C CB . ALA B 2 283 ? 14.932 30.462 19.286 1.00 81.74 ? 283 ALA B CB 1 ATOM 9396 N N . SER B 2 284 ? 16.842 31.636 22.017 1.00 66.38 ? 284 SER B N 1 ATOM 9397 C CA . SER B 2 284 ? 16.778 32.409 23.256 1.00 65.24 ? 284 SER B CA 1 ATOM 9398 C C . SER B 2 284 ? 16.919 33.904 22.994 1.00 64.53 ? 284 SER B C 1 ATOM 9399 O O . SER B 2 284 ? 16.238 34.723 23.611 1.00 60.66 ? 284 SER B O 1 ATOM 9400 C CB . SER B 2 284 ? 17.860 31.944 24.231 1.00 75.82 ? 284 SER B CB 1 ATOM 9401 O OG . SER B 2 284 ? 17.835 32.708 25.425 1.00 79.88 ? 284 SER B OG 1 ATOM 9402 N N . THR B 2 285 ? 17.820 34.250 22.082 1.00 69.47 ? 285 THR B N 1 ATOM 9403 C CA . THR B 2 285 ? 18.000 35.632 21.666 1.00 64.25 ? 285 THR B CA 1 ATOM 9404 C C . THR B 2 285 ? 16.970 36.063 20.620 1.00 65.17 ? 285 THR B C 1 ATOM 9405 O O . THR B 2 285 ? 16.543 37.217 20.598 1.00 65.49 ? 285 THR B O 1 ATOM 9406 C CB . THR B 2 285 ? 19.411 35.861 21.095 1.00 65.89 ? 285 THR B CB 1 ATOM 9407 O OG1 . THR B 2 285 ? 19.536 35.195 19.832 1.00 84.86 ? 285 THR B OG1 1 ATOM 9408 C CG2 . THR B 2 285 ? 20.465 35.332 22.056 1.00 65.78 ? 285 THR B CG2 1 ATOM 9409 N N . THR B 2 286 ? 16.580 35.131 19.754 1.00 66.64 ? 286 THR B N 1 ATOM 9410 C CA . THR B 2 286 ? 15.790 35.468 18.571 1.00 68.06 ? 286 THR B CA 1 ATOM 9411 C C . THR B 2 286 ? 14.270 35.467 18.750 1.00 66.81 ? 286 THR B C 1 ATOM 9412 O O . THR B 2 286 ? 13.554 36.009 17.908 1.00 73.87 ? 286 THR B O 1 ATOM 9413 C CB . THR B 2 286 ? 16.111 34.504 17.413 1.00 74.43 ? 286 THR B CB 1 ATOM 9414 O OG1 . THR B 2 286 ? 15.428 33.262 17.617 1.00 70.24 ? 286 THR B OG1 1 ATOM 9415 C CG2 . THR B 2 286 ? 17.608 34.254 17.325 1.00 78.29 ? 286 THR B CG2 1 ATOM 9416 N N . MET B 2 287 ? 13.767 34.874 19.828 1.00 64.90 ? 287 MET B N 1 ATOM 9417 C CA . MET B 2 287 ? 12.318 34.833 20.024 1.00 65.65 ? 287 MET B CA 1 ATOM 9418 C C . MET B 2 287 ? 11.916 35.047 21.480 1.00 62.45 ? 287 MET B C 1 ATOM 9419 O O . MET B 2 287 ? 12.697 34.808 22.401 1.00 60.26 ? 287 MET B O 1 ATOM 9420 C CB . MET B 2 287 ? 11.735 33.518 19.505 1.00 71.07 ? 287 MET B CB 1 ATOM 9421 C CG . MET B 2 287 ? 11.976 32.312 20.388 1.00 80.54 ? 287 MET B CG 1 ATOM 9422 S SD . MET B 2 287 ? 11.045 30.891 19.786 1.00 80.63 ? 287 MET B SD 1 ATOM 9423 C CE . MET B 2 287 ? 11.461 30.936 18.043 1.00 67.97 ? 287 MET B CE 1 ATOM 9424 N N . ASP B 2 288 ? 10.679 35.497 21.666 1.00 60.41 ? 288 ASP B N 1 ATOM 9425 C CA . ASP B 2 288 ? 10.204 35.987 22.955 1.00 60.24 ? 288 ASP B CA 1 ATOM 9426 C C . ASP B 2 288 ? 9.960 34.866 23.960 1.00 59.98 ? 288 ASP B C 1 ATOM 9427 O O . ASP B 2 288 ? 10.121 33.686 23.648 1.00 61.64 ? 288 ASP B O 1 ATOM 9428 C CB . ASP B 2 288 ? 8.918 36.796 22.753 1.00 60.74 ? 288 ASP B CB 1 ATOM 9429 C CG . ASP B 2 288 ? 8.684 37.817 23.851 1.00 63.06 ? 288 ASP B CG 1 ATOM 9430 O OD1 . ASP B 2 288 ? 9.120 37.577 24.997 1.00 72.61 ? 288 ASP B OD1 1 ATOM 9431 O OD2 . ASP B 2 288 ? 8.061 38.861 23.565 1.00 58.58 ? 288 ASP B OD2 1 ATOM 9432 N N . TYR B 2 289 ? 9.570 35.253 25.171 1.00 55.97 ? 289 TYR B N 1 ATOM 9433 C CA . TYR B 2 289 ? 9.221 34.301 26.215 1.00 54.13 ? 289 TYR B CA 1 ATOM 9434 C C . TYR B 2 289 ? 7.879 33.653 25.896 1.00 64.78 ? 289 TYR B C 1 ATOM 9435 O O . TYR B 2 289 ? 6.997 34.299 25.331 1.00 78.74 ? 289 TYR B O 1 ATOM 9436 C CB . TYR B 2 289 ? 9.168 34.992 27.580 1.00 51.61 ? 289 TYR B CB 1 ATOM 9437 C CG . TYR B 2 289 ? 10.473 35.631 28.003 1.00 52.67 ? 289 TYR B CG 1 ATOM 9438 C CD1 . TYR B 2 289 ? 10.720 36.977 27.766 1.00 52.70 ? 289 TYR B CD1 1 ATOM 9439 C CD2 . TYR B 2 289 ? 11.456 34.888 28.644 1.00 52.74 ? 289 TYR B CD2 1 ATOM 9440 C CE1 . TYR B 2 289 ? 11.911 37.565 28.154 1.00 53.10 ? 289 TYR B CE1 1 ATOM 9441 C CE2 . TYR B 2 289 ? 12.649 35.466 29.036 1.00 52.35 ? 289 TYR B CE2 1 ATOM 9442 C CZ . TYR B 2 289 ? 12.872 36.805 28.789 1.00 54.95 ? 289 TYR B CZ 1 ATOM 9443 O OH . TYR B 2 289 ? 14.059 37.385 29.176 1.00 52.08 ? 289 TYR B OH 1 ATOM 9444 N N . PRO B 2 290 ? 7.723 32.369 26.251 1.00 64.27 ? 290 PRO B N 1 ATOM 9445 C CA . PRO B 2 290 ? 6.469 31.656 25.989 1.00 60.42 ? 290 PRO B CA 1 ATOM 9446 C C . PRO B 2 290 ? 5.320 32.171 26.849 1.00 60.38 ? 290 PRO B C 1 ATOM 9447 O O . PRO B 2 290 ? 5.498 32.387 28.049 1.00 61.32 ? 290 PRO B O 1 ATOM 9448 C CB . PRO B 2 290 ? 6.810 30.208 26.347 1.00 55.42 ? 290 PRO B CB 1 ATOM 9449 C CG . PRO B 2 290 ? 7.897 30.323 27.355 1.00 53.15 ? 290 PRO B CG 1 ATOM 9450 C CD . PRO B 2 290 ? 8.708 31.518 26.941 1.00 56.06 ? 290 PRO B CD 1 ATOM 9451 N N . SER B 2 291 ? 4.155 32.366 26.240 1.00 55.03 ? 291 SER B N 1 ATOM 9452 C CA . SER B 2 291 ? 2.977 32.789 26.985 1.00 59.52 ? 291 SER B CA 1 ATOM 9453 C C . SER B 2 291 ? 2.459 31.632 27.830 1.00 78.84 ? 291 SER B C 1 ATOM 9454 O O . SER B 2 291 ? 2.756 30.470 27.548 1.00 78.14 ? 291 SER B O 1 ATOM 9455 C CB . SER B 2 291 ? 1.885 33.292 26.039 1.00 53.86 ? 291 SER B CB 1 ATOM 9456 O OG . SER B 2 291 ? 1.450 32.265 25.166 1.00 52.41 ? 291 SER B OG 1 ATOM 9457 N N . LEU B 2 292 ? 1.698 31.957 28.870 1.00 83.74 ? 292 LEU B N 1 ATOM 9458 C CA . LEU B 2 292 ? 1.129 30.944 29.755 1.00 67.26 ? 292 LEU B CA 1 ATOM 9459 C C . LEU B 2 292 ? 0.268 29.954 28.981 1.00 63.06 ? 292 LEU B C 1 ATOM 9460 O O . LEU B 2 292 ? 0.307 28.751 29.238 1.00 57.00 ? 292 LEU B O 1 ATOM 9461 C CB . LEU B 2 292 ? 0.306 31.601 30.864 1.00 56.15 ? 292 LEU B CB 1 ATOM 9462 C CG . LEU B 2 292 ? 1.006 31.834 32.205 1.00 53.45 ? 292 LEU B CG 1 ATOM 9463 C CD1 . LEU B 2 292 ? 2.277 32.647 32.028 1.00 75.29 ? 292 LEU B CD1 1 ATOM 9464 C CD2 . LEU B 2 292 ? 0.064 32.517 33.183 1.00 54.78 ? 292 LEU B CD2 1 ATOM 9465 N N . GLY B 2 293 ? -0.503 30.472 28.029 1.00 68.28 ? 293 GLY B N 1 ATOM 9466 C CA . GLY B 2 293 ? -1.347 29.645 27.188 1.00 66.52 ? 293 GLY B CA 1 ATOM 9467 C C . GLY B 2 293 ? -0.563 28.590 26.434 1.00 58.09 ? 293 GLY B C 1 ATOM 9468 O O . GLY B 2 293 ? -0.881 27.403 26.506 1.00 57.23 ? 293 GLY B O 1 ATOM 9469 N N . LEU B 2 294 ? 0.469 29.021 25.713 1.00 58.85 ? 294 LEU B N 1 ATOM 9470 C CA . LEU B 2 294 ? 1.302 28.100 24.948 1.00 60.33 ? 294 LEU B CA 1 ATOM 9471 C C . LEU B 2 294 ? 2.033 27.128 25.868 1.00 60.48 ? 294 LEU B C 1 ATOM 9472 O O . LEU B 2 294 ? 2.253 25.970 25.511 1.00 61.15 ? 294 LEU B O 1 ATOM 9473 C CB . LEU B 2 294 ? 2.309 28.864 24.087 1.00 54.87 ? 294 LEU B CB 1 ATOM 9474 C CG . LEU B 2 294 ? 3.153 27.983 23.162 1.00 56.76 ? 294 LEU B CG 1 ATOM 9475 C CD1 . LEU B 2 294 ? 2.280 27.338 22.097 1.00 58.18 ? 294 LEU B CD1 1 ATOM 9476 C CD2 . LEU B 2 294 ? 4.292 28.769 22.531 1.00 79.70 ? 294 LEU B CD2 1 ATOM 9477 N N . MET B 2 295 ? 2.410 27.602 27.052 1.00 60.14 ? 295 MET B N 1 ATOM 9478 C CA . MET B 2 295 ? 3.022 26.731 28.047 1.00 62.26 ? 295 MET B CA 1 ATOM 9479 C C . MET B 2 295 ? 2.013 25.697 28.524 1.00 60.94 ? 295 MET B C 1 ATOM 9480 O O . MET B 2 295 ? 2.333 24.517 28.634 1.00 59.19 ? 295 MET B O 1 ATOM 9481 C CB . MET B 2 295 ? 3.557 27.532 29.234 1.00 63.04 ? 295 MET B CB 1 ATOM 9482 C CG . MET B 2 295 ? 4.847 28.283 28.956 1.00 63.86 ? 295 MET B CG 1 ATOM 9483 S SD . MET B 2 295 ? 5.657 28.814 30.477 1.00 73.46 ? 295 MET B SD 1 ATOM 9484 C CE . MET B 2 295 ? 4.305 29.652 31.300 1.00 69.89 ? 295 MET B CE 1 ATOM 9485 N N . THR B 2 296 ? 0.794 26.150 28.798 1.00 73.08 ? 296 THR B N 1 ATOM 9486 C CA . THR B 2 296 ? -0.284 25.266 29.230 1.00 71.89 ? 296 THR B CA 1 ATOM 9487 C C . THR B 2 296 ? -0.587 24.206 28.176 1.00 64.15 ? 296 THR B C 1 ATOM 9488 O O . THR B 2 296 ? -0.688 23.019 28.490 1.00 63.63 ? 296 THR B O 1 ATOM 9489 C CB . THR B 2 296 ? -1.573 26.058 29.536 1.00 63.55 ? 296 THR B CB 1 ATOM 9490 O OG1 . THR B 2 296 ? -1.388 26.835 30.725 1.00 56.59 ? 296 THR B OG1 1 ATOM 9491 C CG2 . THR B 2 296 ? -2.750 25.115 29.736 1.00 69.86 ? 296 THR B CG2 1 ATOM 9492 N N . GLU B 2 297 ? -0.721 24.643 26.928 1.00 59.56 ? 297 GLU B N 1 ATOM 9493 C CA . GLU B 2 297 ? -1.040 23.743 25.825 1.00 63.34 ? 297 GLU B CA 1 ATOM 9494 C C . GLU B 2 297 ? 0.007 22.647 25.662 1.00 73.71 ? 297 GLU B C 1 ATOM 9495 O O . GLU B 2 297 ? -0.314 21.462 25.713 1.00 100.51 ? 297 GLU B O 1 ATOM 9496 C CB . GLU B 2 297 ? -1.171 24.523 24.515 1.00 66.27 ? 297 GLU B CB 1 ATOM 9497 C CG . GLU B 2 297 ? -1.486 23.648 23.310 1.00 70.67 ? 297 GLU B CG 1 ATOM 9498 C CD . GLU B 2 297 ? -1.387 24.400 21.996 1.00 88.60 ? 297 GLU B CD 1 ATOM 9499 O OE1 . GLU B 2 297 ? -0.435 25.191 21.831 1.00 86.47 ? 297 GLU B OE1 1 ATOM 9500 O OE2 . GLU B 2 297 ? -2.265 24.202 21.130 1.00 107.47 ? 297 GLU B OE2 1 ATOM 9501 N N . LYS B 2 298 ? 1.259 23.052 25.476 1.00 67.22 ? 298 LYS B N 1 ATOM 9502 C CA . LYS B 2 298 ? 2.343 22.109 25.223 1.00 65.42 ? 298 LYS B CA 1 ATOM 9503 C C . LYS B 2 298 ? 2.630 21.209 26.423 1.00 64.20 ? 298 LYS B C 1 ATOM 9504 O O . LYS B 2 298 ? 3.113 20.088 26.263 1.00 57.61 ? 298 LYS B O 1 ATOM 9505 C CB . LYS B 2 298 ? 3.615 22.859 24.822 1.00 64.89 ? 298 LYS B CB 1 ATOM 9506 C CG . LYS B 2 298 ? 4.054 22.616 23.388 1.00 59.61 ? 298 LYS B CG 1 ATOM 9507 C CD . LYS B 2 298 ? 3.050 23.161 22.387 1.00 70.82 ? 298 LYS B CD 1 ATOM 9508 C CE . LYS B 2 298 ? 3.530 22.947 20.960 1.00 83.10 ? 298 LYS B CE 1 ATOM 9509 N NZ . LYS B 2 298 ? 2.623 23.576 19.961 1.00 90.66 ? 298 LYS B NZ 1 ATOM 9510 N N . LEU B 2 299 ? 2.332 21.702 27.621 1.00 62.53 ? 299 LEU B N 1 ATOM 9511 C CA . LEU B 2 299 ? 2.572 20.943 28.844 1.00 62.37 ? 299 LEU B CA 1 ATOM 9512 C C . LEU B 2 299 ? 1.706 19.690 28.900 1.00 63.93 ? 299 LEU B C 1 ATOM 9513 O O . LEU B 2 299 ? 2.172 18.617 29.284 1.00 63.93 ? 299 LEU B O 1 ATOM 9514 C CB . LEU B 2 299 ? 2.311 21.814 30.075 1.00 60.97 ? 299 LEU B CB 1 ATOM 9515 C CG . LEU B 2 299 ? 3.384 21.830 31.164 1.00 53.59 ? 299 LEU B CG 1 ATOM 9516 C CD1 . LEU B 2 299 ? 4.751 22.063 30.555 1.00 54.50 ? 299 LEU B CD1 1 ATOM 9517 C CD2 . LEU B 2 299 ? 3.075 22.904 32.193 1.00 52.43 ? 299 LEU B CD2 1 ATOM 9518 N N . SER B 2 300 ? 0.442 19.833 28.512 1.00 61.83 ? 300 SER B N 1 ATOM 9519 C CA . SER B 2 300 ? -0.503 18.724 28.557 1.00 69.17 ? 300 SER B CA 1 ATOM 9520 C C . SER B 2 300 ? -0.316 17.770 27.381 1.00 70.60 ? 300 SER B C 1 ATOM 9521 O O . SER B 2 300 ? -0.578 16.573 27.500 1.00 87.60 ? 300 SER B O 1 ATOM 9522 C CB . SER B 2 300 ? -1.940 19.246 28.576 1.00 77.11 ? 300 SER B CB 1 ATOM 9523 O OG . SER B 2 300 ? -2.287 19.828 27.332 1.00 91.14 ? 300 SER B OG 1 ATOM 9524 N N . GLN B 2 301 ? 0.133 18.304 26.248 1.00 66.67 ? 301 GLN B N 1 ATOM 9525 C CA . GLN B 2 301 ? 0.352 17.494 25.054 1.00 72.02 ? 301 GLN B CA 1 ATOM 9526 C C . GLN B 2 301 ? 1.421 16.432 25.292 1.00 76.14 ? 301 GLN B C 1 ATOM 9527 O O . GLN B 2 301 ? 1.327 15.317 24.779 1.00 81.83 ? 301 GLN B O 1 ATOM 9528 C CB . GLN B 2 301 ? 0.750 18.375 23.866 1.00 77.84 ? 301 GLN B CB 1 ATOM 9529 C CG . GLN B 2 301 ? -0.332 19.339 23.403 1.00 102.58 ? 301 GLN B CG 1 ATOM 9530 C CD . GLN B 2 301 ? -1.572 18.633 22.889 1.00 128.75 ? 301 GLN B CD 1 ATOM 9531 O OE1 . GLN B 2 301 ? -1.508 17.493 22.428 1.00 140.24 ? 301 GLN B OE1 1 ATOM 9532 N NE2 . GLN B 2 301 ? -2.712 19.311 22.966 1.00 129.85 ? 301 GLN B NE2 1 ATOM 9533 N N . LYS B 2 302 ? 2.436 16.789 26.071 1.00 73.95 ? 302 LYS B N 1 ATOM 9534 C CA . LYS B 2 302 ? 3.526 15.873 26.382 1.00 68.58 ? 302 LYS B CA 1 ATOM 9535 C C . LYS B 2 302 ? 3.282 15.137 27.697 1.00 69.27 ? 302 LYS B C 1 ATOM 9536 O O . LYS B 2 302 ? 4.130 14.364 28.146 1.00 78.17 ? 302 LYS B O 1 ATOM 9537 C CB . LYS B 2 302 ? 4.854 16.628 26.443 1.00 63.35 ? 302 LYS B CB 1 ATOM 9538 C CG . LYS B 2 302 ? 5.255 17.292 25.135 1.00 62.50 ? 302 LYS B CG 1 ATOM 9539 C CD . LYS B 2 302 ? 5.541 16.262 24.055 1.00 65.61 ? 302 LYS B CD 1 ATOM 9540 C CE . LYS B 2 302 ? 6.072 16.921 22.791 1.00 81.78 ? 302 LYS B CE 1 ATOM 9541 N NZ . LYS B 2 302 ? 6.462 15.920 21.760 1.00 94.44 ? 302 LYS B NZ 1 ATOM 9542 N N . ASN B 2 303 ? 2.123 15.387 28.304 1.00 64.70 ? 303 ASN B N 1 ATOM 9543 C CA . ASN B 2 303 ? 1.760 14.801 29.594 1.00 65.35 ? 303 ASN B CA 1 ATOM 9544 C C . ASN B 2 303 ? 2.825 15.050 30.655 1.00 67.14 ? 303 ASN B C 1 ATOM 9545 O O . ASN B 2 303 ? 3.215 14.140 31.387 1.00 67.85 ? 303 ASN B O 1 ATOM 9546 C CB . ASN B 2 303 ? 1.502 13.299 29.453 1.00 68.40 ? 303 ASN B CB 1 ATOM 9547 C CG . ASN B 2 303 ? 0.256 12.995 28.646 1.00 69.36 ? 303 ASN B CG 1 ATOM 9548 O OD1 . ASN B 2 303 ? 0.322 12.349 27.600 1.00 73.89 ? 303 ASN B OD1 1 ATOM 9549 N ND2 . ASN B 2 303 ? -0.890 13.461 29.128 1.00 72.95 ? 303 ASN B ND2 1 ATOM 9550 N N . ILE B 2 304 ? 3.293 16.291 30.726 1.00 70.46 ? 304 ILE B N 1 ATOM 9551 C CA . ILE B 2 304 ? 4.320 16.672 31.683 1.00 69.80 ? 304 ILE B CA 1 ATOM 9552 C C . ILE B 2 304 ? 3.732 17.519 32.805 1.00 63.48 ? 304 ILE B C 1 ATOM 9553 O O . ILE B 2 304 ? 3.037 18.504 32.554 1.00 59.31 ? 304 ILE B O 1 ATOM 9554 C CB . ILE B 2 304 ? 5.463 17.448 30.999 1.00 67.82 ? 304 ILE B CB 1 ATOM 9555 C CG1 . ILE B 2 304 ? 6.152 16.564 29.958 1.00 78.35 ? 304 ILE B CG1 1 ATOM 9556 C CG2 . ILE B 2 304 ? 6.467 17.946 32.027 1.00 64.31 ? 304 ILE B CG2 1 ATOM 9557 C CD1 . ILE B 2 304 ? 7.308 17.237 29.254 1.00 83.97 ? 304 ILE B CD1 1 ATOM 9558 N N . ASN B 2 305 ? 4.005 17.123 34.044 1.00 63.33 ? 305 ASN B N 1 ATOM 9559 C CA . ASN B 2 305 ? 3.549 17.877 35.204 1.00 69.57 ? 305 ASN B CA 1 ATOM 9560 C C . ASN B 2 305 ? 4.593 18.882 35.671 1.00 75.99 ? 305 ASN B C 1 ATOM 9561 O O . ASN B 2 305 ? 5.756 18.534 35.877 1.00 82.70 ? 305 ASN B O 1 ATOM 9562 C CB . ASN B 2 305 ? 3.183 16.930 36.345 1.00 65.98 ? 305 ASN B CB 1 ATOM 9563 C CG . ASN B 2 305 ? 1.878 16.206 36.100 1.00 73.51 ? 305 ASN B CG 1 ATOM 9564 O OD1 . ASN B 2 305 ? 1.849 14.984 35.951 1.00 87.76 ? 305 ASN B OD1 1 ATOM 9565 N ND2 . ASN B 2 305 ? 0.785 16.958 36.062 1.00 79.47 ? 305 ASN B ND2 1 ATOM 9566 N N . LEU B 2 306 ? 4.170 20.131 35.833 1.00 64.15 ? 306 LEU B N 1 ATOM 9567 C CA . LEU B 2 306 ? 5.072 21.193 36.257 1.00 62.45 ? 306 LEU B CA 1 ATOM 9568 C C . LEU B 2 306 ? 4.971 21.428 37.760 1.00 66.84 ? 306 LEU B C 1 ATOM 9569 O O . LEU B 2 306 ? 3.876 21.551 38.307 1.00 67.23 ? 306 LEU B O 1 ATOM 9570 C CB . LEU B 2 306 ? 4.770 22.484 35.496 1.00 59.93 ? 306 LEU B CB 1 ATOM 9571 C CG . LEU B 2 306 ? 5.714 23.661 35.744 1.00 58.44 ? 306 LEU B CG 1 ATOM 9572 C CD1 . LEU B 2 306 ? 7.137 23.288 35.365 1.00 58.77 ? 306 LEU B CD1 1 ATOM 9573 C CD2 . LEU B 2 306 ? 5.255 24.885 34.969 1.00 60.29 ? 306 LEU B CD2 1 ATOM 9574 N N . ILE B 2 307 ? 6.122 21.483 38.423 1.00 67.96 ? 307 ILE B N 1 ATOM 9575 C CA . ILE B 2 307 ? 6.169 21.711 39.862 1.00 65.57 ? 307 ILE B CA 1 ATOM 9576 C C . ILE B 2 307 ? 6.988 22.954 40.186 1.00 71.39 ? 307 ILE B C 1 ATOM 9577 O O . ILE B 2 307 ? 8.118 23.099 39.722 1.00 79.24 ? 307 ILE B O 1 ATOM 9578 C CB . ILE B 2 307 ? 6.771 20.506 40.617 1.00 65.73 ? 307 ILE B CB 1 ATOM 9579 C CG1 . ILE B 2 307 ? 6.030 19.214 40.265 1.00 86.34 ? 307 ILE B CG1 1 ATOM 9580 C CG2 . ILE B 2 307 ? 6.739 20.747 42.118 1.00 65.85 ? 307 ILE B CG2 1 ATOM 9581 C CD1 . ILE B 2 307 ? 6.688 18.405 39.166 1.00 104.83 ? 307 ILE B CD1 1 ATOM 9582 N N . PHE B 2 308 ? 6.412 23.849 40.981 1.00 69.93 ? 308 PHE B N 1 ATOM 9583 C CA . PHE B 2 308 ? 7.113 25.056 41.401 1.00 67.26 ? 308 PHE B CA 1 ATOM 9584 C C . PHE B 2 308 ? 7.689 24.907 42.804 1.00 71.45 ? 308 PHE B C 1 ATOM 9585 O O . PHE B 2 308 ? 6.949 24.818 43.781 1.00 88.25 ? 308 PHE B O 1 ATOM 9586 C CB . PHE B 2 308 ? 6.179 26.267 41.354 1.00 72.67 ? 308 PHE B CB 1 ATOM 9587 C CG . PHE B 2 308 ? 5.822 26.710 39.964 1.00 78.93 ? 308 PHE B CG 1 ATOM 9588 C CD1 . PHE B 2 308 ? 6.589 27.658 39.308 1.00 74.15 ? 308 PHE B CD1 1 ATOM 9589 C CD2 . PHE B 2 308 ? 4.715 26.187 39.318 1.00 85.87 ? 308 PHE B CD2 1 ATOM 9590 C CE1 . PHE B 2 308 ? 6.263 28.072 38.031 1.00 65.73 ? 308 PHE B CE1 1 ATOM 9591 C CE2 . PHE B 2 308 ? 4.383 26.597 38.040 1.00 80.81 ? 308 PHE B CE2 1 ATOM 9592 C CZ . PHE B 2 308 ? 5.159 27.541 37.397 1.00 68.46 ? 308 PHE B CZ 1 ATOM 9593 N N . ALA B 2 309 ? 9.014 24.878 42.900 1.00 70.20 ? 309 ALA B N 1 ATOM 9594 C CA . ALA B 2 309 ? 9.676 24.916 44.196 1.00 77.23 ? 309 ALA B CA 1 ATOM 9595 C C . ALA B 2 309 ? 10.438 26.227 44.318 1.00 79.48 ? 309 ALA B C 1 ATOM 9596 O O . ALA B 2 309 ? 11.465 26.414 43.674 1.00 80.08 ? 309 ALA B O 1 ATOM 9597 C CB . ALA B 2 309 ? 10.610 23.729 44.361 1.00 68.70 ? 309 ALA B CB 1 ATOM 9598 N N . VAL B 2 310 ? 9.940 27.132 45.153 1.00 75.08 ? 310 VAL B N 1 ATOM 9599 C CA . VAL B 2 310 ? 10.498 28.478 45.205 1.00 70.25 ? 310 VAL B CA 1 ATOM 9600 C C . VAL B 2 310 ? 10.715 28.975 46.629 1.00 75.14 ? 310 VAL B C 1 ATOM 9601 O O . VAL B 2 310 ? 10.373 28.296 47.597 1.00 86.96 ? 310 VAL B O 1 ATOM 9602 C CB . VAL B 2 310 ? 9.590 29.480 44.467 1.00 67.92 ? 310 VAL B CB 1 ATOM 9603 C CG1 . VAL B 2 310 ? 9.568 29.190 42.973 1.00 64.59 ? 310 VAL B CG1 1 ATOM 9604 C CG2 . VAL B 2 310 ? 8.186 29.439 45.042 1.00 69.34 ? 310 VAL B CG2 1 ATOM 9605 N N . THR B 2 311 ? 11.272 30.176 46.744 1.00 76.92 ? 311 THR B N 1 ATOM 9606 C CA . THR B 2 311 ? 11.574 30.768 48.040 1.00 81.83 ? 311 THR B CA 1 ATOM 9607 C C . THR B 2 311 ? 10.303 31.315 48.680 1.00 85.59 ? 311 THR B C 1 ATOM 9608 O O . THR B 2 311 ? 9.382 31.729 47.976 1.00 85.14 ? 311 THR B O 1 ATOM 9609 C CB . THR B 2 311 ? 12.615 31.896 47.916 1.00 90.69 ? 311 THR B CB 1 ATOM 9610 O OG1 . THR B 2 311 ? 13.452 31.655 46.779 1.00 78.36 ? 311 THR B OG1 1 ATOM 9611 C CG2 . THR B 2 311 ? 13.472 31.972 49.172 1.00 116.40 ? 311 THR B CG2 1 ATOM 9612 N N . GLU B 2 312 ? 10.270 31.321 50.011 1.00 90.66 ? 312 GLU B N 1 ATOM 9613 C CA . GLU B 2 312 ? 9.079 31.692 50.778 1.00 97.27 ? 312 GLU B CA 1 ATOM 9614 C C . GLU B 2 312 ? 8.485 33.037 50.363 1.00 101.18 ? 312 GLU B C 1 ATOM 9615 O O . GLU B 2 312 ? 7.265 33.203 50.334 1.00 115.12 ? 312 GLU B O 1 ATOM 9616 C CB . GLU B 2 312 ? 9.406 31.717 52.274 1.00 107.07 ? 312 GLU B CB 1 ATOM 9617 C CG . GLU B 2 312 ? 8.215 32.032 53.166 1.00 125.75 ? 312 GLU B CG 1 ATOM 9618 C CD . GLU B 2 312 ? 8.585 32.099 54.635 1.00 152.36 ? 312 GLU B CD 1 ATOM 9619 O OE1 . GLU B 2 312 ? 9.781 31.937 54.958 1.00 156.65 ? 312 GLU B OE1 1 ATOM 9620 O OE2 . GLU B 2 312 ? 7.679 32.314 55.468 1.00 165.58 ? 312 GLU B OE2 1 ATOM 9621 N N . ASN B 2 313 ? 9.353 33.988 50.037 1.00 92.26 ? 313 ASN B N 1 ATOM 9622 C CA . ASN B 2 313 ? 8.919 35.320 49.635 1.00 89.39 ? 313 ASN B CA 1 ATOM 9623 C C . ASN B 2 313 ? 8.117 35.314 48.336 1.00 85.60 ? 313 ASN B C 1 ATOM 9624 O O . ASN B 2 313 ? 7.098 35.996 48.219 1.00 86.65 ? 313 ASN B O 1 ATOM 9625 C CB . ASN B 2 313 ? 10.131 36.243 49.487 1.00 87.13 ? 313 ASN B CB 1 ATOM 9626 C CG . ASN B 2 313 ? 11.174 35.688 48.534 1.00 81.63 ? 313 ASN B CG 1 ATOM 9627 O OD1 . ASN B 2 313 ? 11.050 35.819 47.316 1.00 76.73 ? 313 ASN B OD1 1 ATOM 9628 N ND2 . ASN B 2 313 ? 12.208 35.065 49.085 1.00 82.07 ? 313 ASN B ND2 1 ATOM 9629 N N . VAL B 2 314 ? 8.587 34.540 47.365 1.00 80.86 ? 314 VAL B N 1 ATOM 9630 C CA . VAL B 2 314 ? 8.006 34.534 46.030 1.00 76.69 ? 314 VAL B CA 1 ATOM 9631 C C . VAL B 2 314 ? 6.995 33.392 45.852 1.00 76.47 ? 314 VAL B C 1 ATOM 9632 O O . VAL B 2 314 ? 6.444 33.200 44.765 1.00 74.42 ? 314 VAL B O 1 ATOM 9633 C CB . VAL B 2 314 ? 9.122 34.444 44.959 1.00 71.89 ? 314 VAL B CB 1 ATOM 9634 C CG1 . VAL B 2 314 ? 9.608 33.015 44.803 1.00 78.05 ? 314 VAL B CG1 1 ATOM 9635 C CG2 . VAL B 2 314 ? 8.656 35.019 43.630 1.00 83.20 ? 314 VAL B CG2 1 ATOM 9636 N N . VAL B 2 315 ? 6.748 32.644 46.926 1.00 78.38 ? 315 VAL B N 1 ATOM 9637 C CA . VAL B 2 315 ? 5.818 31.512 46.888 1.00 77.18 ? 315 VAL B CA 1 ATOM 9638 C C . VAL B 2 315 ? 4.417 31.912 46.430 1.00 82.89 ? 315 VAL B C 1 ATOM 9639 O O . VAL B 2 315 ? 3.881 31.325 45.490 1.00 93.96 ? 315 VAL B O 1 ATOM 9640 C CB . VAL B 2 315 ? 5.709 30.817 48.267 1.00 78.85 ? 315 VAL B CB 1 ATOM 9641 C CG1 . VAL B 2 315 ? 4.416 30.016 48.371 1.00 78.17 ? 315 VAL B CG1 1 ATOM 9642 C CG2 . VAL B 2 315 ? 6.902 29.911 48.500 1.00 99.19 ? 315 VAL B CG2 1 ATOM 9643 N N . ASN B 2 316 ? 3.835 32.913 47.088 1.00 79.75 ? 316 ASN B N 1 ATOM 9644 C CA . ASN B 2 316 ? 2.473 33.344 46.785 1.00 78.48 ? 316 ASN B CA 1 ATOM 9645 C C . ASN B 2 316 ? 2.309 33.766 45.328 1.00 77.40 ? 316 ASN B C 1 ATOM 9646 O O . ASN B 2 316 ? 1.242 33.590 44.738 1.00 79.04 ? 316 ASN B O 1 ATOM 9647 C CB . ASN B 2 316 ? 2.058 34.491 47.708 1.00 81.15 ? 316 ASN B CB 1 ATOM 9648 C CG . ASN B 2 316 ? 1.955 34.065 49.158 1.00 93.33 ? 316 ASN B CG 1 ATOM 9649 O OD1 . ASN B 2 316 ? 2.904 34.209 49.929 1.00 105.33 ? 316 ASN B OD1 1 ATOM 9650 N ND2 . ASN B 2 316 ? 0.797 33.538 49.540 1.00 101.44 ? 316 ASN B ND2 1 ATOM 9651 N N . LEU B 2 317 ? 3.370 34.331 44.760 1.00 71.52 ? 317 LEU B N 1 ATOM 9652 C CA . LEU B 2 317 ? 3.391 34.681 43.346 1.00 67.37 ? 317 LEU B CA 1 ATOM 9653 C C . LEU B 2 317 ? 3.150 33.459 42.466 1.00 64.33 ? 317 LEU B C 1 ATOM 9654 O O . LEU B 2 317 ? 2.130 33.365 41.783 1.00 73.57 ? 317 LEU B O 1 ATOM 9655 C CB . LEU B 2 317 ? 4.721 35.334 42.972 1.00 66.51 ? 317 LEU B CB 1 ATOM 9656 C CG . LEU B 2 317 ? 4.840 35.717 41.497 1.00 57.79 ? 317 LEU B CG 1 ATOM 9657 C CD1 . LEU B 2 317 ? 3.792 36.757 41.136 1.00 57.59 ? 317 LEU B CD1 1 ATOM 9658 C CD2 . LEU B 2 317 ? 6.232 36.221 41.175 1.00 56.74 ? 317 LEU B CD2 1 ATOM 9659 N N . TYR B 2 318 ? 4.097 32.525 42.489 1.00 62.11 ? 318 TYR B N 1 ATOM 9660 C CA . TYR B 2 318 ? 4.010 31.319 41.673 1.00 60.48 ? 318 TYR B CA 1 ATOM 9661 C C . TYR B 2 318 ? 2.823 30.453 42.073 1.00 62.44 ? 318 TYR B C 1 ATOM 9662 O O . TYR B 2 318 ? 2.309 29.680 41.263 1.00 59.16 ? 318 TYR B O 1 ATOM 9663 C CB . TYR B 2 318 ? 5.311 30.520 41.766 1.00 61.08 ? 318 TYR B CB 1 ATOM 9664 C CG . TYR B 2 318 ? 6.467 31.195 41.069 1.00 60.98 ? 318 TYR B CG 1 ATOM 9665 C CD1 . TYR B 2 318 ? 7.372 31.974 41.774 1.00 62.94 ? 318 TYR B CD1 1 ATOM 9666 C CD2 . TYR B 2 318 ? 6.640 31.069 39.697 1.00 61.27 ? 318 TYR B CD2 1 ATOM 9667 C CE1 . TYR B 2 318 ? 8.426 32.599 41.134 1.00 65.46 ? 318 TYR B CE1 1 ATOM 9668 C CE2 . TYR B 2 318 ? 7.690 31.689 39.049 1.00 58.53 ? 318 TYR B CE2 1 ATOM 9669 C CZ . TYR B 2 318 ? 8.578 32.455 39.772 1.00 59.47 ? 318 TYR B CZ 1 ATOM 9670 O OH . TYR B 2 318 ? 9.624 33.075 39.129 1.00 58.28 ? 318 TYR B OH 1 ATOM 9671 N N . GLN B 2 319 ? 2.390 30.588 43.322 1.00 74.02 ? 319 GLN B N 1 ATOM 9672 C CA . GLN B 2 319 ? 1.175 29.929 43.781 1.00 84.90 ? 319 GLN B CA 1 ATOM 9673 C C . GLN B 2 319 ? -0.015 30.479 43.007 1.00 79.09 ? 319 GLN B C 1 ATOM 9674 O O . GLN B 2 319 ? -0.921 29.738 42.623 1.00 73.75 ? 319 GLN B O 1 ATOM 9675 C CB . GLN B 2 319 ? 0.981 30.130 45.283 1.00 91.68 ? 319 GLN B CB 1 ATOM 9676 C CG . GLN B 2 319 ? -0.108 29.271 45.896 1.00 99.40 ? 319 GLN B CG 1 ATOM 9677 C CD . GLN B 2 319 ? -0.220 29.465 47.395 1.00 110.68 ? 319 GLN B CD 1 ATOM 9678 O OE1 . GLN B 2 319 ? 0.176 30.502 47.929 1.00 113.92 ? 319 GLN B OE1 1 ATOM 9679 N NE2 . GLN B 2 319 ? -0.755 28.464 48.084 1.00 113.76 ? 319 GLN B NE2 1 ATOM 9680 N N . ASN B 2 320 ? 0.003 31.787 42.773 1.00 78.68 ? 320 ASN B N 1 ATOM 9681 C CA . ASN B 2 320 ? -1.032 32.440 41.986 1.00 81.66 ? 320 ASN B CA 1 ATOM 9682 C C . ASN B 2 320 ? -0.860 32.176 40.493 1.00 76.90 ? 320 ASN B C 1 ATOM 9683 O O . ASN B 2 320 ? -1.841 32.080 39.755 1.00 80.17 ? 320 ASN B O 1 ATOM 9684 C CB . ASN B 2 320 ? -1.037 33.942 42.260 1.00 86.22 ? 320 ASN B CB 1 ATOM 9685 C CG . ASN B 2 320 ? -1.888 34.313 43.456 1.00 93.85 ? 320 ASN B CG 1 ATOM 9686 O OD1 . ASN B 2 320 ? -2.749 33.543 43.881 1.00 97.14 ? 320 ASN B OD1 1 ATOM 9687 N ND2 . ASN B 2 320 ? -1.654 35.499 44.003 1.00 106.25 ? 320 ASN B ND2 1 ATOM 9688 N N . TYR B 2 321 ? 0.391 32.063 40.054 1.00 72.67 ? 321 TYR B N 1 ATOM 9689 C CA . TYR B 2 321 ? 0.689 31.690 38.675 1.00 66.87 ? 321 TYR B CA 1 ATOM 9690 C C . TYR B 2 321 ? 0.147 30.301 38.365 1.00 68.63 ? 321 TYR B C 1 ATOM 9691 O O . TYR B 2 321 ? -0.427 30.068 37.301 1.00 76.11 ? 321 TYR B O 1 ATOM 9692 C CB . TYR B 2 321 ? 2.196 31.721 38.411 1.00 71.60 ? 321 TYR B CB 1 ATOM 9693 C CG . TYR B 2 321 ? 2.721 33.038 37.886 1.00 63.50 ? 321 TYR B CG 1 ATOM 9694 C CD1 . TYR B 2 321 ? 2.287 33.547 36.669 1.00 56.64 ? 321 TYR B CD1 1 ATOM 9695 C CD2 . TYR B 2 321 ? 3.671 33.760 38.595 1.00 67.12 ? 321 TYR B CD2 1 ATOM 9696 C CE1 . TYR B 2 321 ? 2.771 34.747 36.183 1.00 59.97 ? 321 TYR B CE1 1 ATOM 9697 C CE2 . TYR B 2 321 ? 4.163 34.957 38.116 1.00 64.98 ? 321 TYR B CE2 1 ATOM 9698 C CZ . TYR B 2 321 ? 3.709 35.447 36.911 1.00 65.68 ? 321 TYR B CZ 1 ATOM 9699 O OH . TYR B 2 321 ? 4.200 36.642 36.435 1.00 67.28 ? 321 TYR B OH 1 ATOM 9700 N N . SER B 2 322 ? 0.336 29.385 39.311 1.00 68.79 ? 322 SER B N 1 ATOM 9701 C CA . SER B 2 322 ? -0.054 27.989 39.142 1.00 69.98 ? 322 SER B CA 1 ATOM 9702 C C . SER B 2 322 ? -1.548 27.822 38.894 1.00 70.79 ? 322 SER B C 1 ATOM 9703 O O . SER B 2 322 ? -1.969 26.887 38.214 1.00 73.82 ? 322 SER B O 1 ATOM 9704 C CB . SER B 2 322 ? 0.355 27.176 40.371 1.00 80.24 ? 322 SER B CB 1 ATOM 9705 O OG . SER B 2 322 ? -0.218 27.717 41.548 1.00 97.75 ? 322 SER B OG 1 ATOM 9706 N N . GLU B 2 323 ? -2.346 28.729 39.449 1.00 69.83 ? 323 GLU B N 1 ATOM 9707 C CA . GLU B 2 323 ? -3.793 28.680 39.278 1.00 70.25 ? 323 GLU B CA 1 ATOM 9708 C C . GLU B 2 323 ? -4.183 28.867 37.814 1.00 74.29 ? 323 GLU B C 1 ATOM 9709 O O . GLU B 2 323 ? -5.217 28.369 37.368 1.00 78.48 ? 323 GLU B O 1 ATOM 9710 C CB . GLU B 2 323 ? -4.471 29.743 40.146 1.00 74.31 ? 323 GLU B CB 1 ATOM 9711 C CG . GLU B 2 323 ? -4.202 29.587 41.636 1.00 80.76 ? 323 GLU B CG 1 ATOM 9712 C CD . GLU B 2 323 ? -4.944 30.609 42.477 1.00 106.42 ? 323 GLU B CD 1 ATOM 9713 O OE1 . GLU B 2 323 ? -5.726 31.399 41.906 1.00 117.97 ? 323 GLU B OE1 1 ATOM 9714 O OE2 . GLU B 2 323 ? -4.745 30.622 43.710 1.00 111.01 ? 323 GLU B OE2 1 ATOM 9715 N N . LEU B 2 324 ? -3.347 29.585 37.070 1.00 72.28 ? 324 LEU B N 1 ATOM 9716 C CA . LEU B 2 324 ? -3.596 29.831 35.654 1.00 63.04 ? 324 LEU B CA 1 ATOM 9717 C C . LEU B 2 324 ? -3.132 28.665 34.786 1.00 66.74 ? 324 LEU B C 1 ATOM 9718 O O . LEU B 2 324 ? -3.518 28.554 33.623 1.00 79.07 ? 324 LEU B O 1 ATOM 9719 C CB . LEU B 2 324 ? -2.912 31.124 35.213 1.00 55.38 ? 324 LEU B CB 1 ATOM 9720 C CG . LEU B 2 324 ? -3.512 32.388 35.831 1.00 56.13 ? 324 LEU B CG 1 ATOM 9721 C CD1 . LEU B 2 324 ? -2.764 33.628 35.372 1.00 84.58 ? 324 LEU B CD1 1 ATOM 9722 C CD2 . LEU B 2 324 ? -4.989 32.488 35.486 1.00 56.20 ? 324 LEU B CD2 1 ATOM 9723 N N . ILE B 2 325 ? -2.306 27.797 35.359 1.00 58.32 ? 325 ILE B N 1 ATOM 9724 C CA . ILE B 2 325 ? -1.865 26.593 34.667 1.00 59.68 ? 325 ILE B CA 1 ATOM 9725 C C . ILE B 2 325 ? -2.295 25.373 35.472 1.00 85.51 ? 325 ILE B C 1 ATOM 9726 O O . ILE B 2 325 ? -1.528 24.858 36.285 1.00 110.41 ? 325 ILE B O 1 ATOM 9727 C CB . ILE B 2 325 ? -0.336 26.568 34.460 1.00 56.96 ? 325 ILE B CB 1 ATOM 9728 C CG1 . ILE B 2 325 ? 0.155 27.902 33.896 1.00 56.05 ? 325 ILE B CG1 1 ATOM 9729 C CG2 . ILE B 2 325 ? 0.060 25.424 33.538 1.00 59.77 ? 325 ILE B CG2 1 ATOM 9730 C CD1 . ILE B 2 325 ? 1.650 27.949 33.658 1.00 49.62 ? 325 ILE B CD1 1 ATOM 9731 N N . PRO B 2 326 ? -3.537 24.913 35.250 1.00 75.83 ? 326 PRO B N 1 ATOM 9732 C CA . PRO B 2 326 ? -4.132 23.806 36.007 1.00 74.26 ? 326 PRO B CA 1 ATOM 9733 C C . PRO B 2 326 ? -3.308 22.526 35.919 1.00 81.97 ? 326 PRO B C 1 ATOM 9734 O O . PRO B 2 326 ? -2.829 22.173 34.842 1.00 85.55 ? 326 PRO B O 1 ATOM 9735 C CB . PRO B 2 326 ? -5.502 23.622 35.344 1.00 75.77 ? 326 PRO B CB 1 ATOM 9736 C CG . PRO B 2 326 ? -5.359 24.230 33.989 1.00 72.88 ? 326 PRO B CG 1 ATOM 9737 C CD . PRO B 2 326 ? -4.427 25.383 34.175 1.00 71.64 ? 326 PRO B CD 1 ATOM 9738 N N . GLY B 2 327 ? -3.144 21.848 37.050 1.00 89.17 ? 327 GLY B N 1 ATOM 9739 C CA . GLY B 2 327 ? -2.366 20.624 37.101 1.00 101.69 ? 327 GLY B CA 1 ATOM 9740 C C . GLY B 2 327 ? -0.953 20.859 37.596 1.00 98.30 ? 327 GLY B C 1 ATOM 9741 O O . GLY B 2 327 ? -0.125 19.947 37.593 1.00 94.78 ? 327 GLY B O 1 ATOM 9742 N N . THR B 2 328 ? -0.675 22.086 38.024 1.00 88.31 ? 328 THR B N 1 ATOM 9743 C CA . THR B 2 328 ? 0.647 22.440 38.527 1.00 76.79 ? 328 THR B CA 1 ATOM 9744 C C . THR B 2 328 ? 0.582 22.839 39.997 1.00 75.70 ? 328 THR B C 1 ATOM 9745 O O . THR B 2 328 ? -0.321 23.565 40.412 1.00 84.14 ? 328 THR B O 1 ATOM 9746 C CB . THR B 2 328 ? 1.273 23.590 37.718 1.00 70.15 ? 328 THR B CB 1 ATOM 9747 O OG1 . THR B 2 328 ? 0.499 24.782 37.899 1.00 70.09 ? 328 THR B OG1 1 ATOM 9748 C CG2 . THR B 2 328 ? 1.314 23.238 36.240 1.00 67.79 ? 328 THR B CG2 1 ATOM 9749 N N . THR B 2 329 ? 1.547 22.366 40.779 1.00 69.29 ? 329 THR B N 1 ATOM 9750 C CA . THR B 2 329 ? 1.572 22.642 42.210 1.00 76.73 ? 329 THR B CA 1 ATOM 9751 C C . THR B 2 329 ? 2.808 23.441 42.609 1.00 78.86 ? 329 THR B C 1 ATOM 9752 O O . THR B 2 329 ? 3.824 23.430 41.913 1.00 78.30 ? 329 THR B O 1 ATOM 9753 C CB . THR B 2 329 ? 1.528 21.343 43.037 1.00 79.18 ? 329 THR B CB 1 ATOM 9754 O OG1 . THR B 2 329 ? 2.624 20.498 42.664 1.00 84.49 ? 329 THR B OG1 1 ATOM 9755 C CG2 . THR B 2 329 ? 0.220 20.604 42.801 1.00 84.35 ? 329 THR B CG2 1 ATOM 9756 N N . VAL B 2 330 ? 2.705 24.139 43.735 1.00 76.35 ? 330 VAL B N 1 ATOM 9757 C CA . VAL B 2 330 ? 3.800 24.951 44.248 1.00 66.69 ? 330 VAL B CA 1 ATOM 9758 C C . VAL B 2 330 ? 4.184 24.470 45.644 1.00 67.32 ? 330 VAL B C 1 ATOM 9759 O O . VAL B 2 330 ? 3.344 23.951 46.378 1.00 65.84 ? 330 VAL B O 1 ATOM 9760 C CB . VAL B 2 330 ? 3.416 26.448 44.284 1.00 66.77 ? 330 VAL B CB 1 ATOM 9761 C CG1 . VAL B 2 330 ? 4.612 27.316 44.648 1.00 67.16 ? 330 VAL B CG1 1 ATOM 9762 C CG2 . VAL B 2 330 ? 2.855 26.873 42.943 1.00 71.01 ? 330 VAL B CG2 1 ATOM 9763 N N . GLY B 2 331 ? 5.451 24.640 46.010 1.00 64.95 ? 331 GLY B N 1 ATOM 9764 C CA . GLY B 2 331 ? 5.916 24.243 47.325 1.00 78.37 ? 331 GLY B CA 1 ATOM 9765 C C . GLY B 2 331 ? 7.039 25.131 47.821 1.00 78.85 ? 331 GLY B C 1 ATOM 9766 O O . GLY B 2 331 ? 7.736 25.771 47.034 1.00 84.26 ? 331 GLY B O 1 ATOM 9767 N N . VAL B 2 332 ? 7.221 25.155 49.137 1.00 76.38 ? 332 VAL B N 1 ATOM 9768 C CA . VAL B 2 332 ? 8.157 26.079 49.766 1.00 77.02 ? 332 VAL B CA 1 ATOM 9769 C C . VAL B 2 332 ? 9.558 25.488 49.876 1.00 82.80 ? 332 VAL B C 1 ATOM 9770 O O . VAL B 2 332 ? 9.732 24.341 50.287 1.00 96.69 ? 332 VAL B O 1 ATOM 9771 C CB . VAL B 2 332 ? 7.670 26.490 51.171 1.00 83.46 ? 332 VAL B CB 1 ATOM 9772 C CG1 . VAL B 2 332 ? 8.600 27.531 51.779 1.00 80.23 ? 332 VAL B CG1 1 ATOM 9773 C CG2 . VAL B 2 332 ? 6.247 27.021 51.102 1.00 88.11 ? 332 VAL B CG2 1 ATOM 9774 N N . LEU B 2 333 ? 10.554 26.282 49.498 1.00 79.03 ? 333 LEU B N 1 ATOM 9775 C CA . LEU B 2 333 ? 11.950 25.886 49.616 1.00 79.66 ? 333 LEU B CA 1 ATOM 9776 C C . LEU B 2 333 ? 12.582 26.586 50.816 1.00 97.83 ? 333 LEU B C 1 ATOM 9777 O O . LEU B 2 333 ? 12.792 27.798 50.791 1.00 128.25 ? 333 LEU B O 1 ATOM 9778 C CB . LEU B 2 333 ? 12.710 26.229 48.332 1.00 74.30 ? 333 LEU B CB 1 ATOM 9779 C CG . LEU B 2 333 ? 13.912 25.373 47.936 1.00 73.43 ? 333 LEU B CG 1 ATOM 9780 C CD1 . LEU B 2 333 ? 13.456 24.003 47.461 1.00 74.00 ? 333 LEU B CD1 1 ATOM 9781 C CD2 . LEU B 2 333 ? 14.729 26.072 46.862 1.00 71.55 ? 333 LEU B CD2 1 ATOM 9782 N N . SER B 2 334 ? 12.888 25.830 51.866 1.00 92.01 ? 334 SER B N 1 ATOM 9783 C CA . SER B 2 334 ? 13.429 26.421 53.090 1.00 105.26 ? 334 SER B CA 1 ATOM 9784 C C . SER B 2 334 ? 14.364 25.465 53.823 1.00 118.68 ? 334 SER B C 1 ATOM 9785 O O . SER B 2 334 ? 14.243 24.257 53.691 1.00 125.76 ? 334 SER B O 1 ATOM 9786 C CB . SER B 2 334 ? 12.293 26.848 54.019 1.00 114.76 ? 334 SER B CB 1 ATOM 9787 O OG . SER B 2 334 ? 12.803 27.427 55.207 1.00 131.47 ? 334 SER B OG 1 ATOM 9788 N N . MET B 2 335 ? 15.288 26.005 54.610 1.00 123.57 ? 335 MET B N 1 ATOM 9789 C CA . MET B 2 335 ? 16.263 25.167 55.306 1.00 120.79 ? 335 MET B CA 1 ATOM 9790 C C . MET B 2 335 ? 15.669 24.475 56.529 1.00 127.20 ? 335 MET B C 1 ATOM 9791 O O . MET B 2 335 ? 16.303 23.609 57.134 1.00 142.70 ? 335 MET B O 1 ATOM 9792 C CB . MET B 2 335 ? 17.476 25.997 55.722 1.00 123.44 ? 335 MET B CB 1 ATOM 9793 C CG . MET B 2 335 ? 18.155 26.708 54.568 1.00 120.49 ? 335 MET B CG 1 ATOM 9794 S SD . MET B 2 335 ? 19.814 27.266 54.989 1.00 137.66 ? 335 MET B SD 1 ATOM 9795 C CE . MET B 2 335 ? 20.611 25.700 55.337 1.00 101.29 ? 335 MET B CE 1 ATOM 9796 N N . ASP B 2 336 ? 14.448 24.855 56.886 1.00 131.33 ? 336 ASP B N 1 ATOM 9797 C CA . ASP B 2 336 ? 13.778 24.289 58.050 1.00 155.57 ? 336 ASP B CA 1 ATOM 9798 C C . ASP B 2 336 ? 12.438 23.689 57.634 1.00 161.39 ? 336 ASP B C 1 ATOM 9799 O O . ASP B 2 336 ? 11.969 23.925 56.520 1.00 157.96 ? 336 ASP B O 1 ATOM 9800 C CB . ASP B 2 336 ? 13.589 25.347 59.140 1.00 166.26 ? 336 ASP B CB 1 ATOM 9801 C CG . ASP B 2 336 ? 13.617 24.755 60.540 1.00 175.38 ? 336 ASP B CG 1 ATOM 9802 O OD1 . ASP B 2 336 ? 14.719 24.408 61.018 1.00 178.18 ? 336 ASP B OD1 1 ATOM 9803 O OD2 . ASP B 2 336 ? 12.542 24.642 61.165 1.00 175.47 ? 336 ASP B OD2 1 ATOM 9804 N N . SER B 2 337 ? 11.844 22.910 58.537 1.00 163.91 ? 337 SER B N 1 ATOM 9805 C CA . SER B 2 337 ? 10.649 22.098 58.283 1.00 159.39 ? 337 SER B CA 1 ATOM 9806 C C . SER B 2 337 ? 10.899 20.997 57.243 1.00 161.24 ? 337 SER B C 1 ATOM 9807 O O . SER B 2 337 ? 11.916 20.299 57.309 1.00 160.85 ? 337 SER B O 1 ATOM 9808 C CB . SER B 2 337 ? 9.469 22.982 57.852 1.00 152.51 ? 337 SER B CB 1 ATOM 9809 O OG . SER B 2 337 ? 9.676 23.549 56.568 1.00 145.29 ? 337 SER B OG 1 ATOM 9810 N N . SER B 2 338 ? 9.980 20.849 56.290 1.00 165.50 ? 338 SER B N 1 ATOM 9811 C CA . SER B 2 338 ? 9.993 19.715 55.360 1.00 161.54 ? 338 SER B CA 1 ATOM 9812 C C . SER B 2 338 ? 11.069 19.812 54.276 1.00 160.79 ? 338 SER B C 1 ATOM 9813 O O . SER B 2 338 ? 11.936 18.952 54.181 1.00 163.93 ? 338 SER B O 1 ATOM 9814 C CB . SER B 2 338 ? 8.616 19.567 54.710 1.00 145.41 ? 338 SER B CB 1 ATOM 9815 O OG . SER B 2 338 ? 8.276 20.739 53.998 1.00 136.60 ? 338 SER B OG 1 ATOM 9816 N N . ASN B 2 339 ? 10.968 20.852 53.453 1.00 146.96 ? 339 ASN B N 1 ATOM 9817 C CA . ASN B 2 339 ? 11.877 21.165 52.333 1.00 140.17 ? 339 ASN B CA 1 ATOM 9818 C C . ASN B 2 339 ? 11.985 20.018 51.305 1.00 144.88 ? 339 ASN B C 1 ATOM 9819 O O . ASN B 2 339 ? 11.049 19.228 51.261 1.00 147.64 ? 339 ASN B O 1 ATOM 9820 C CB . ASN B 2 339 ? 13.218 21.567 52.963 1.00 147.24 ? 339 ASN B CB 1 ATOM 9821 C CG . ASN B 2 339 ? 14.336 21.774 51.974 1.00 155.21 ? 339 ASN B CG 1 ATOM 9822 O OD1 . ASN B 2 339 ? 14.138 22.295 50.878 1.00 154.68 ? 339 ASN B OD1 1 ATOM 9823 N ND2 . ASN B 2 339 ? 15.537 21.338 52.362 1.00 158.40 ? 339 ASN B ND2 1 ATOM 9824 N N . VAL B 2 340 ? 13.119 19.792 50.623 1.00 150.96 ? 340 VAL B N 1 ATOM 9825 C CA . VAL B 2 340 ? 13.103 19.127 49.291 1.00 152.09 ? 340 VAL B CA 1 ATOM 9826 C C . VAL B 2 340 ? 12.642 17.692 49.345 1.00 154.16 ? 340 VAL B C 1 ATOM 9827 O O . VAL B 2 340 ? 12.018 17.182 48.414 1.00 162.06 ? 340 VAL B O 1 ATOM 9828 C CB . VAL B 2 340 ? 14.507 19.085 48.587 1.00 121.64 ? 340 VAL B CB 1 ATOM 9829 C CG1 . VAL B 2 340 ? 14.375 18.634 47.134 1.00 118.60 ? 340 VAL B CG1 1 ATOM 9830 C CG2 . VAL B 2 340 ? 15.232 20.444 48.643 1.00 119.19 ? 340 VAL B CG2 1 ATOM 9831 N N . LEU B 2 341 ? 12.989 17.051 50.450 1.00 139.66 ? 341 LEU B N 1 ATOM 9832 C CA . LEU B 2 341 ? 12.751 15.641 50.689 1.00 134.96 ? 341 LEU B CA 1 ATOM 9833 C C . LEU B 2 341 ? 11.297 15.208 50.646 1.00 133.46 ? 341 LEU B C 1 ATOM 9834 O O . LEU B 2 341 ? 10.848 14.563 49.688 1.00 130.97 ? 341 LEU B O 1 ATOM 9835 C CB . LEU B 2 341 ? 13.307 15.270 52.056 1.00 142.07 ? 341 LEU B CB 1 ATOM 9836 C CG . LEU B 2 341 ? 14.779 15.345 52.443 1.00 140.34 ? 341 LEU B CG 1 ATOM 9837 C CD1 . LEU B 2 341 ? 15.446 16.680 52.134 1.00 131.24 ? 341 LEU B CD1 1 ATOM 9838 C CD2 . LEU B 2 341 ? 14.841 15.060 53.928 1.00 145.67 ? 341 LEU B CD2 1 ATOM 9839 N N . GLN B 2 342 ? 10.560 15.577 51.691 1.00 142.45 ? 342 GLN B N 1 ATOM 9840 C CA . GLN B 2 342 ? 9.167 15.196 51.796 1.00 140.01 ? 342 GLN B CA 1 ATOM 9841 C C . GLN B 2 342 ? 8.355 16.220 51.013 1.00 116.73 ? 342 GLN B C 1 ATOM 9842 O O . GLN B 2 342 ? 7.153 16.035 50.832 1.00 111.94 ? 342 GLN B O 1 ATOM 9843 C CB . GLN B 2 342 ? 8.694 15.094 53.268 1.00 150.06 ? 342 GLN B CB 1 ATOM 9844 C CG . GLN B 2 342 ? 8.155 13.693 53.667 1.00 124.40 ? 342 GLN B CG 1 ATOM 9845 C CD . GLN B 2 342 ? 6.658 13.657 54.030 1.00 135.16 ? 342 GLN B CD 1 ATOM 9846 O OE1 . GLN B 2 342 ? 6.075 14.653 54.466 1.00 140.43 ? 342 GLN B OE1 1 ATOM 9847 N NE2 . GLN B 2 342 ? 6.042 12.491 53.855 1.00 137.39 ? 342 GLN B NE2 1 ATOM 9848 N N . LEU B 2 343 ? 9.017 17.277 50.520 1.00 102.23 ? 343 LEU B N 1 ATOM 9849 C CA . LEU B 2 343 ? 8.398 18.155 49.514 1.00 118.26 ? 343 LEU B CA 1 ATOM 9850 C C . LEU B 2 343 ? 7.968 17.399 48.262 1.00 129.56 ? 343 LEU B C 1 ATOM 9851 O O . LEU B 2 343 ? 6.774 17.157 48.146 1.00 138.68 ? 343 LEU B O 1 ATOM 9852 C CB . LEU B 2 343 ? 9.302 19.329 49.099 1.00 109.50 ? 343 LEU B CB 1 ATOM 9853 C CG . LEU B 2 343 ? 9.271 20.022 47.716 1.00 89.31 ? 343 LEU B CG 1 ATOM 9854 C CD1 . LEU B 2 343 ? 7.924 20.593 47.289 1.00 82.58 ? 343 LEU B CD1 1 ATOM 9855 C CD2 . LEU B 2 343 ? 10.357 21.115 47.643 1.00 84.45 ? 343 LEU B CD2 1 ATOM 9856 N N . ILE B 2 344 ? 8.884 16.970 47.383 1.00 125.19 ? 344 ILE B N 1 ATOM 9857 C CA . ILE B 2 344 ? 8.481 16.548 46.047 1.00 114.55 ? 344 ILE B CA 1 ATOM 9858 C C . ILE B 2 344 ? 7.393 15.480 46.111 1.00 108.49 ? 344 ILE B C 1 ATOM 9859 O O . ILE B 2 344 ? 6.380 15.608 45.435 1.00 105.08 ? 344 ILE B O 1 ATOM 9860 C CB . ILE B 2 344 ? 9.624 15.968 45.232 1.00 107.84 ? 344 ILE B CB 1 ATOM 9861 C CG1 . ILE B 2 344 ? 10.466 17.056 44.515 1.00 76.21 ? 344 ILE B CG1 1 ATOM 9862 C CG2 . ILE B 2 344 ? 9.049 15.011 44.197 1.00 77.42 ? 344 ILE B CG2 1 ATOM 9863 C CD1 . ILE B 2 344 ? 10.807 16.706 43.025 1.00 79.66 ? 344 ILE B CD1 1 ATOM 9864 N N . VAL B 2 345 ? 7.573 14.457 46.947 1.00 85.41 ? 345 VAL B N 1 ATOM 9865 C CA . VAL B 2 345 ? 6.639 13.337 47.025 1.00 85.98 ? 345 VAL B CA 1 ATOM 9866 C C . VAL B 2 345 ? 5.218 13.834 47.334 1.00 93.75 ? 345 VAL B C 1 ATOM 9867 O O . VAL B 2 345 ? 4.239 13.337 46.770 1.00 112.15 ? 345 VAL B O 1 ATOM 9868 C CB . VAL B 2 345 ? 7.127 12.343 48.084 1.00 102.66 ? 345 VAL B CB 1 ATOM 9869 C CG1 . VAL B 2 345 ? 6.130 11.225 48.299 1.00 123.53 ? 345 VAL B CG1 1 ATOM 9870 C CG2 . VAL B 2 345 ? 8.466 11.772 47.658 1.00 102.63 ? 345 VAL B CG2 1 ATOM 9871 N N . ASP B 2 346 ? 5.116 14.840 48.205 1.00 85.28 ? 346 ASP B N 1 ATOM 9872 C CA . ASP B 2 346 ? 3.843 15.525 48.436 1.00 88.32 ? 346 ASP B CA 1 ATOM 9873 C C . ASP B 2 346 ? 3.301 16.193 47.160 1.00 84.61 ? 346 ASP B C 1 ATOM 9874 O O . ASP B 2 346 ? 2.093 16.181 46.915 1.00 101.11 ? 346 ASP B O 1 ATOM 9875 C CB . ASP B 2 346 ? 3.982 16.571 49.553 1.00 102.63 ? 346 ASP B CB 1 ATOM 9876 C CG . ASP B 2 346 ? 4.343 15.956 50.892 1.00 119.49 ? 346 ASP B CG 1 ATOM 9877 O OD1 . ASP B 2 346 ? 4.675 16.720 51.821 1.00 128.09 ? 346 ASP B OD1 1 ATOM 9878 O OD2 . ASP B 2 346 ? 4.326 14.710 51.014 1.00 123.61 ? 346 ASP B OD2 1 ATOM 9879 N N . ALA B 2 347 ? 4.178 16.762 46.339 1.00 78.13 ? 347 ALA B N 1 ATOM 9880 C CA . ALA B 2 347 ? 3.713 17.381 45.099 1.00 83.87 ? 347 ALA B CA 1 ATOM 9881 C C . ALA B 2 347 ? 3.230 16.303 44.133 1.00 90.03 ? 347 ALA B C 1 ATOM 9882 O O . ALA B 2 347 ? 2.172 16.441 43.520 1.00 88.33 ? 347 ALA B O 1 ATOM 9883 C CB . ALA B 2 347 ? 4.804 18.228 44.467 1.00 86.85 ? 347 ALA B CB 1 ATOM 9884 N N . TYR B 2 348 ? 4.002 15.224 44.018 1.00 86.29 ? 348 TYR B N 1 ATOM 9885 C CA . TYR B 2 348 ? 3.616 14.085 43.190 1.00 73.29 ? 348 TYR B CA 1 ATOM 9886 C C . TYR B 2 348 ? 2.331 13.463 43.719 1.00 79.90 ? 348 TYR B C 1 ATOM 9887 O O . TYR B 2 348 ? 1.530 12.921 42.957 1.00 92.96 ? 348 TYR B O 1 ATOM 9888 C CB . TYR B 2 348 ? 4.737 13.044 43.147 1.00 73.82 ? 348 TYR B CB 1 ATOM 9889 C CG . TYR B 2 348 ? 4.422 11.817 42.315 1.00 76.52 ? 348 TYR B CG 1 ATOM 9890 C CD1 . TYR B 2 348 ? 4.298 11.902 40.934 1.00 75.77 ? 348 TYR B CD1 1 ATOM 9891 C CD2 . TYR B 2 348 ? 4.263 10.571 42.910 1.00 82.06 ? 348 TYR B CD2 1 ATOM 9892 C CE1 . TYR B 2 348 ? 4.015 10.783 40.170 1.00 75.01 ? 348 TYR B CE1 1 ATOM 9893 C CE2 . TYR B 2 348 ? 3.981 9.446 42.153 1.00 85.50 ? 348 TYR B CE2 1 ATOM 9894 C CZ . TYR B 2 348 ? 3.859 9.559 40.784 1.00 82.11 ? 348 TYR B CZ 1 ATOM 9895 O OH . TYR B 2 348 ? 3.578 8.443 40.028 1.00 88.83 ? 348 TYR B OH 1 ATOM 9896 N N . GLY B 2 349 ? 2.141 13.548 45.032 1.00 84.06 ? 349 GLY B N 1 ATOM 9897 C CA . GLY B 2 349 ? 0.922 13.076 45.659 1.00 90.30 ? 349 GLY B CA 1 ATOM 9898 C C . GLY B 2 349 ? -0.278 13.892 45.220 1.00 95.08 ? 349 GLY B C 1 ATOM 9899 O O . GLY B 2 349 ? -1.319 13.337 44.875 1.00 110.66 ? 349 GLY B O 1 ATOM 9900 N N . LYS B 2 350 ? -0.125 15.214 45.231 1.00 83.14 ? 350 LYS B N 1 ATOM 9901 C CA . LYS B 2 350 ? -1.186 16.122 44.807 1.00 78.66 ? 350 LYS B CA 1 ATOM 9902 C C . LYS B 2 350 ? -1.592 15.877 43.359 1.00 76.11 ? 350 LYS B C 1 ATOM 9903 O O . LYS B 2 350 ? -2.779 15.842 43.036 1.00 76.24 ? 350 LYS B O 1 ATOM 9904 C CB . LYS B 2 350 ? -0.750 17.579 44.980 1.00 78.83 ? 350 LYS B CB 1 ATOM 9905 C CG . LYS B 2 350 ? -0.563 18.012 46.423 1.00 92.06 ? 350 LYS B CG 1 ATOM 9906 C CD . LYS B 2 350 ? -0.151 19.473 46.510 1.00 87.64 ? 350 LYS B CD 1 ATOM 9907 C CE . LYS B 2 350 ? 0.085 19.894 47.952 1.00 78.83 ? 350 LYS B CE 1 ATOM 9908 N NZ . LYS B 2 350 ? 0.523 21.313 48.053 1.00 77.98 ? 350 LYS B NZ 1 ATOM 9909 N N . ILE B 2 351 ? -0.596 15.714 42.493 1.00 75.15 ? 351 ILE B N 1 ATOM 9910 C CA . ILE B 2 351 ? -0.836 15.472 41.075 1.00 83.16 ? 351 ILE B CA 1 ATOM 9911 C C . ILE B 2 351 ? -1.664 14.209 40.860 1.00 92.09 ? 351 ILE B C 1 ATOM 9912 O O . ILE B 2 351 ? -2.594 14.191 40.052 1.00 112.65 ? 351 ILE B O 1 ATOM 9913 C CB . ILE B 2 351 ? 0.487 15.343 40.296 1.00 84.48 ? 351 ILE B CB 1 ATOM 9914 C CG1 . ILE B 2 351 ? 1.335 16.606 40.462 1.00 78.52 ? 351 ILE B CG1 1 ATOM 9915 C CG2 . ILE B 2 351 ? 0.214 15.066 38.828 1.00 91.12 ? 351 ILE B CG2 1 ATOM 9916 C CD1 . ILE B 2 351 ? 0.635 17.875 40.036 1.00 96.12 ? 351 ILE B CD1 1 ATOM 9917 N N . ARG B 2 352 ? -1.327 13.158 41.599 1.00 76.43 ? 352 ARG B N 1 ATOM 9918 C CA . ARG B 2 352 ? -2.020 11.883 41.482 1.00 76.22 ? 352 ARG B CA 1 ATOM 9919 C C . ARG B 2 352 ? -3.269 11.842 42.360 1.00 87.73 ? 352 ARG B C 1 ATOM 9920 O O . ARG B 2 352 ? -3.975 10.834 42.400 1.00 104.10 ? 352 ARG B O 1 ATOM 9921 C CB . ARG B 2 352 ? -1.081 10.732 41.850 1.00 81.17 ? 352 ARG B CB 1 ATOM 9922 C CG . ARG B 2 352 ? 0.133 10.582 40.940 1.00 76.18 ? 352 ARG B CG 1 ATOM 9923 C CD . ARG B 2 352 ? -0.249 10.015 39.581 1.00 76.72 ? 352 ARG B CD 1 ATOM 9924 N NE . ARG B 2 352 ? -0.465 11.056 38.580 1.00 78.93 ? 352 ARG B NE 1 ATOM 9925 C CZ . ARG B 2 352 ? 0.411 11.372 37.633 1.00 94.22 ? 352 ARG B CZ 1 ATOM 9926 N NH1 . ARG B 2 352 ? 0.134 12.332 36.760 1.00 95.34 ? 352 ARG B NH1 1 ATOM 9927 N NH2 . ARG B 2 352 ? 1.565 10.724 37.553 1.00 98.46 ? 352 ARG B NH2 1 ATOM 9928 N N . SER B 2 353 ? -3.538 12.940 43.061 1.00 80.40 ? 353 SER B N 1 ATOM 9929 C CA . SER B 2 353 ? -4.697 13.019 43.948 1.00 84.33 ? 353 SER B CA 1 ATOM 9930 C C . SER B 2 353 ? -5.954 13.454 43.205 1.00 88.00 ? 353 SER B C 1 ATOM 9931 O O . SER B 2 353 ? -7.036 13.526 43.788 1.00 93.89 ? 353 SER B O 1 ATOM 9932 C CB . SER B 2 353 ? -4.425 13.985 45.103 1.00 91.32 ? 353 SER B CB 1 ATOM 9933 O OG . SER B 2 353 ? -3.318 13.559 45.877 1.00 115.17 ? 353 SER B OG 1 ATOM 9934 N N . LYS B 2 354 ? -5.808 13.743 41.917 1.00 83.23 ? 354 LYS B N 1 ATOM 9935 C CA . LYS B 2 354 ? -6.923 14.225 41.112 1.00 74.02 ? 354 LYS B CA 1 ATOM 9936 C C . LYS B 2 354 ? -6.955 13.537 39.752 1.00 81.87 ? 354 LYS B C 1 ATOM 9937 O O . LYS B 2 354 ? -5.912 13.301 39.141 1.00 95.88 ? 354 LYS B O 1 ATOM 9938 C CB . LYS B 2 354 ? -6.832 15.744 40.939 1.00 73.15 ? 354 LYS B CB 1 ATOM 9939 C CG . LYS B 2 354 ? -8.039 16.384 40.273 1.00 85.30 ? 354 LYS B CG 1 ATOM 9940 C CD . LYS B 2 354 ? -7.863 17.892 40.162 1.00 86.70 ? 354 LYS B CD 1 ATOM 9941 C CE . LYS B 2 354 ? -9.093 18.555 39.564 1.00 81.02 ? 354 LYS B CE 1 ATOM 9942 N NZ . LYS B 2 354 ? -9.390 18.047 38.196 1.00 77.87 ? 354 LYS B NZ 1 ATOM 9943 N N . VAL B 2 355 ? -8.155 13.205 39.287 1.00 74.36 ? 355 VAL B N 1 ATOM 9944 C CA . VAL B 2 355 ? -8.327 12.608 37.967 1.00 73.67 ? 355 VAL B CA 1 ATOM 9945 C C . VAL B 2 355 ? -9.371 13.370 37.160 1.00 82.05 ? 355 VAL B C 1 ATOM 9946 O O . VAL B 2 355 ? -10.543 13.412 37.529 1.00 91.52 ? 355 VAL B O 1 ATOM 9947 C CB . VAL B 2 355 ? -8.739 11.126 38.059 1.00 71.42 ? 355 VAL B CB 1 ATOM 9948 C CG1 . VAL B 2 355 ? -9.139 10.599 36.689 1.00 70.19 ? 355 VAL B CG1 1 ATOM 9949 C CG2 . VAL B 2 355 ? -7.608 10.298 38.638 1.00 71.86 ? 355 VAL B CG2 1 ATOM 9950 N N . GLU B 2 356 ? -8.936 13.973 36.058 1.00 77.81 ? 356 GLU B N 1 ATOM 9951 C CA . GLU B 2 356 ? -9.836 14.711 35.181 1.00 77.72 ? 356 GLU B CA 1 ATOM 9952 C C . GLU B 2 356 ? -9.611 14.305 33.730 1.00 81.87 ? 356 GLU B C 1 ATOM 9953 O O . GLU B 2 356 ? -8.475 14.118 33.297 1.00 94.95 ? 356 GLU B O 1 ATOM 9954 C CB . GLU B 2 356 ? -9.639 16.219 35.350 1.00 93.84 ? 356 GLU B CB 1 ATOM 9955 C CG . GLU B 2 356 ? -10.614 17.070 34.550 1.00 113.85 ? 356 GLU B CG 1 ATOM 9956 C CD . GLU B 2 356 ? -10.506 18.546 34.879 1.00 118.10 ? 356 GLU B CD 1 ATOM 9957 O OE1 . GLU B 2 356 ? -9.503 18.945 35.508 1.00 104.56 ? 356 GLU B OE1 1 ATOM 9958 O OE2 . GLU B 2 356 ? -11.427 19.306 34.513 1.00 125.13 ? 356 GLU B OE2 1 ATOM 9959 N N . LEU B 2 357 ? -10.701 14.165 32.983 1.00 72.08 ? 357 LEU B N 1 ATOM 9960 C CA . LEU B 2 357 ? -10.619 13.743 31.591 1.00 69.25 ? 357 LEU B CA 1 ATOM 9961 C C . LEU B 2 357 ? -10.521 14.938 30.649 1.00 66.86 ? 357 LEU B C 1 ATOM 9962 O O . LEU B 2 357 ? -11.309 15.878 30.740 1.00 73.48 ? 357 LEU B O 1 ATOM 9963 C CB . LEU B 2 357 ? -11.833 12.888 31.222 1.00 69.64 ? 357 LEU B CB 1 ATOM 9964 C CG . LEU B 2 357 ? -12.130 11.697 32.135 1.00 73.05 ? 357 LEU B CG 1 ATOM 9965 C CD1 . LEU B 2 357 ? -13.395 10.985 31.684 1.00 69.88 ? 357 LEU B CD1 1 ATOM 9966 C CD2 . LEU B 2 357 ? -10.952 10.737 32.171 1.00 80.20 ? 357 LEU B CD2 1 ATOM 9967 N N . GLU B 2 358 ? -9.544 14.898 29.749 1.00 65.94 ? 358 GLU B N 1 ATOM 9968 C CA . GLU B 2 358 ? -9.411 15.925 28.722 1.00 67.30 ? 358 GLU B CA 1 ATOM 9969 C C . GLU B 2 358 ? -9.774 15.352 27.356 1.00 65.03 ? 358 GLU B C 1 ATOM 9970 O O . GLU B 2 358 ? -9.498 14.187 27.070 1.00 77.71 ? 358 GLU B O 1 ATOM 9971 C CB . GLU B 2 358 ? -7.992 16.501 28.706 1.00 89.32 ? 358 GLU B CB 1 ATOM 9972 C CG . GLU B 2 358 ? -6.888 15.461 28.614 1.00 106.45 ? 358 GLU B CG 1 ATOM 9973 C CD . GLU B 2 358 ? -5.507 16.085 28.516 1.00 109.89 ? 358 GLU B CD 1 ATOM 9974 O OE1 . GLU B 2 358 ? -4.513 15.387 28.810 1.00 110.48 ? 358 GLU B OE1 1 ATOM 9975 O OE2 . GLU B 2 358 ? -5.416 17.273 28.141 1.00 106.96 ? 358 GLU B OE2 1 ATOM 9976 N N . VAL B 2 359 ? -10.396 16.174 26.518 1.00 62.02 ? 359 VAL B N 1 ATOM 9977 C CA . VAL B 2 359 ? -10.889 15.715 25.224 1.00 62.97 ? 359 VAL B CA 1 ATOM 9978 C C . VAL B 2 359 ? -10.166 16.384 24.060 1.00 64.84 ? 359 VAL B C 1 ATOM 9979 O O . VAL B 2 359 ? -10.241 17.600 23.888 1.00 95.90 ? 359 VAL B O 1 ATOM 9980 C CB . VAL B 2 359 ? -12.398 15.973 25.082 1.00 62.17 ? 359 VAL B CB 1 ATOM 9981 C CG1 . VAL B 2 359 ? -12.906 15.409 23.768 1.00 74.88 ? 359 VAL B CG1 1 ATOM 9982 C CG2 . VAL B 2 359 ? -13.152 15.364 26.252 1.00 57.58 ? 359 VAL B CG2 1 ATOM 9983 N N . ARG B 2 360 ? -9.472 15.582 23.259 1.00 66.36 ? 360 ARG B N 1 ATOM 9984 C CA . ARG B 2 360 ? -8.747 16.097 22.103 1.00 70.69 ? 360 ARG B CA 1 ATOM 9985 C C . ARG B 2 360 ? -9.455 15.760 20.794 1.00 73.89 ? 360 ARG B C 1 ATOM 9986 O O . ARG B 2 360 ? -10.018 14.675 20.645 1.00 88.54 ? 360 ARG B O 1 ATOM 9987 C CB . ARG B 2 360 ? -7.321 15.545 22.073 1.00 76.22 ? 360 ARG B CB 1 ATOM 9988 C CG . ARG B 2 360 ? -6.476 15.919 23.279 1.00 89.78 ? 360 ARG B CG 1 ATOM 9989 C CD . ARG B 2 360 ? -5.084 15.314 23.178 1.00 97.68 ? 360 ARG B CD 1 ATOM 9990 N NE . ARG B 2 360 ? -4.291 15.552 24.380 1.00 97.09 ? 360 ARG B NE 1 ATOM 9991 C CZ . ARG B 2 360 ? -3.083 15.039 24.591 1.00 100.14 ? 360 ARG B CZ 1 ATOM 9992 N NH1 . ARG B 2 360 ? -2.525 14.254 23.679 1.00 97.80 ? 360 ARG B NH1 1 ATOM 9993 N NH2 . ARG B 2 360 ? -2.433 15.309 25.715 1.00 102.84 ? 360 ARG B NH2 1 ATOM 9994 N N . ASP B 2 361 ? -9.422 16.705 19.858 1.00 78.86 ? 361 ASP B N 1 ATOM 9995 C CA . ASP B 2 361 ? -9.939 16.513 18.503 1.00 82.78 ? 361 ASP B CA 1 ATOM 9996 C C . ASP B 2 361 ? -11.415 16.119 18.455 1.00 73.83 ? 361 ASP B C 1 ATOM 9997 O O . ASP B 2 361 ? -11.824 15.337 17.597 1.00 74.11 ? 361 ASP B O 1 ATOM 9998 C CB . ASP B 2 361 ? -9.105 15.460 17.767 1.00 94.81 ? 361 ASP B CB 1 ATOM 9999 C CG . ASP B 2 361 ? -7.642 15.845 17.662 1.00 106.21 ? 361 ASP B CG 1 ATOM 10000 O OD1 . ASP B 2 361 ? -6.779 14.957 17.823 1.00 108.54 ? 361 ASP B OD1 1 ATOM 10001 O OD2 . ASP B 2 361 ? -7.355 17.036 17.419 1.00 111.56 ? 361 ASP B OD2 1 ATOM 10002 N N . LEU B 2 362 ? -12.212 16.666 19.368 1.00 71.14 ? 362 LEU B N 1 ATOM 10003 C CA . LEU B 2 362 ? -13.648 16.408 19.374 1.00 72.04 ? 362 LEU B CA 1 ATOM 10004 C C . LEU B 2 362 ? -14.346 17.186 18.265 1.00 76.08 ? 362 LEU B C 1 ATOM 10005 O O . LEU B 2 362 ? -14.288 18.415 18.238 1.00 94.91 ? 362 LEU B O 1 ATOM 10006 C CB . LEU B 2 362 ? -14.259 16.771 20.728 1.00 70.76 ? 362 LEU B CB 1 ATOM 10007 C CG . LEU B 2 362 ? -15.768 16.551 20.867 1.00 72.21 ? 362 LEU B CG 1 ATOM 10008 C CD1 . LEU B 2 362 ? -16.112 15.072 20.767 1.00 78.42 ? 362 LEU B CD1 1 ATOM 10009 C CD2 . LEU B 2 362 ? -16.283 17.137 22.172 1.00 84.77 ? 362 LEU B CD2 1 ATOM 10010 N N . PRO B 2 363 ? -15.007 16.468 17.343 1.00 79.23 ? 363 PRO B N 1 ATOM 10011 C CA . PRO B 2 363 ? -15.735 17.095 16.233 1.00 93.35 ? 363 PRO B CA 1 ATOM 10012 C C . PRO B 2 363 ? -16.830 18.046 16.715 1.00 101.62 ? 363 PRO B C 1 ATOM 10013 O O . PRO B 2 363 ? -17.420 17.828 17.774 1.00 100.52 ? 363 PRO B O 1 ATOM 10014 C CB . PRO B 2 363 ? -16.336 15.899 15.487 1.00 91.00 ? 363 PRO B CB 1 ATOM 10015 C CG . PRO B 2 363 ? -15.455 14.750 15.845 1.00 83.29 ? 363 PRO B CG 1 ATOM 10016 C CD . PRO B 2 363 ? -15.035 14.998 17.261 1.00 79.86 ? 363 PRO B CD 1 ATOM 10017 N N . GLU B 2 364 ? -17.088 19.090 15.933 1.00 105.06 ? 364 GLU B N 1 ATOM 10018 C CA . GLU B 2 364 ? -18.021 20.148 16.311 1.00 105.15 ? 364 GLU B CA 1 ATOM 10019 C C . GLU B 2 364 ? -19.459 19.662 16.463 1.00 100.23 ? 364 GLU B C 1 ATOM 10020 O O . GLU B 2 364 ? -20.218 20.183 17.281 1.00 102.80 ? 364 GLU B O 1 ATOM 10021 C CB . GLU B 2 364 ? -17.982 21.273 15.274 1.00 110.58 ? 364 GLU B CB 1 ATOM 10022 C CG . GLU B 2 364 ? -16.602 21.859 15.020 1.00 119.76 ? 364 GLU B CG 1 ATOM 10023 C CD . GLU B 2 364 ? -16.203 22.892 16.054 1.00 124.23 ? 364 GLU B CD 1 ATOM 10024 O OE1 . GLU B 2 364 ? -16.096 24.083 15.692 1.00 118.69 ? 364 GLU B OE1 1 ATOM 10025 O OE2 . GLU B 2 364 ? -15.992 22.517 17.227 1.00 129.19 ? 364 GLU B OE2 1 ATOM 10026 N N . GLU B 2 365 ? -19.826 18.660 15.674 1.00 94.90 ? 365 GLU B N 1 ATOM 10027 C CA . GLU B 2 365 ? -21.224 18.270 15.526 1.00 105.37 ? 365 GLU B CA 1 ATOM 10028 C C . GLU B 2 365 ? -21.791 17.506 16.721 1.00 96.65 ? 365 GLU B C 1 ATOM 10029 O O . GLU B 2 365 ? -23.009 17.393 16.861 1.00 95.09 ? 365 GLU B O 1 ATOM 10030 C CB . GLU B 2 365 ? -21.398 17.432 14.255 1.00 128.06 ? 365 GLU B CB 1 ATOM 10031 C CG . GLU B 2 365 ? -21.171 18.203 12.958 1.00 149.28 ? 365 GLU B CG 1 ATOM 10032 C CD . GLU B 2 365 ? -19.702 18.445 12.654 1.00 152.99 ? 365 GLU B CD 1 ATOM 10033 O OE1 . GLU B 2 365 ? -18.842 17.971 13.427 1.00 156.07 ? 365 GLU B OE1 1 ATOM 10034 O OE2 . GLU B 2 365 ? -19.406 19.109 11.638 1.00 146.71 ? 365 GLU B OE2 1 ATOM 10035 N N . LEU B 2 366 ? -20.923 16.982 17.580 1.00 90.71 ? 366 LEU B N 1 ATOM 10036 C CA . LEU B 2 366 ? -21.394 16.220 18.733 1.00 91.39 ? 366 LEU B CA 1 ATOM 10037 C C . LEU B 2 366 ? -20.802 16.723 20.049 1.00 84.59 ? 366 LEU B C 1 ATOM 10038 O O . LEU B 2 366 ? -19.745 17.354 20.070 1.00 80.68 ? 366 LEU B O 1 ATOM 10039 C CB . LEU B 2 366 ? -21.087 14.728 18.559 1.00 89.23 ? 366 LEU B CB 1 ATOM 10040 C CG . LEU B 2 366 ? -19.692 14.191 18.886 1.00 87.83 ? 366 LEU B CG 1 ATOM 10041 C CD1 . LEU B 2 366 ? -19.705 12.670 18.875 1.00 93.15 ? 366 LEU B CD1 1 ATOM 10042 C CD2 . LEU B 2 366 ? -18.657 14.715 17.912 1.00 84.39 ? 366 LEU B CD2 1 ATOM 10043 N N . SER B 2 367 ? -21.501 16.436 21.144 1.00 79.82 ? 367 SER B N 1 ATOM 10044 C CA . SER B 2 367 ? -21.097 16.894 22.469 1.00 90.18 ? 367 SER B CA 1 ATOM 10045 C C . SER B 2 367 ? -21.042 15.740 23.466 1.00 88.17 ? 367 SER B C 1 ATOM 10046 O O . SER B 2 367 ? -21.584 14.664 23.214 1.00 93.94 ? 367 SER B O 1 ATOM 10047 C CB . SER B 2 367 ? -22.055 17.974 22.972 1.00 114.67 ? 367 SER B CB 1 ATOM 10048 O OG . SER B 2 367 ? -23.393 17.509 22.969 1.00 128.09 ? 367 SER B OG 1 ATOM 10049 N N . LEU B 2 368 ? -20.391 15.972 24.602 1.00 86.55 ? 368 LEU B N 1 ATOM 10050 C CA . LEU B 2 368 ? -20.199 14.922 25.595 1.00 81.73 ? 368 LEU B CA 1 ATOM 10051 C C . LEU B 2 368 ? -20.744 15.301 26.971 1.00 82.53 ? 368 LEU B C 1 ATOM 10052 O O . LEU B 2 368 ? -20.577 16.431 27.430 1.00 86.42 ? 368 LEU B O 1 ATOM 10053 C CB . LEU B 2 368 ? -18.713 14.570 25.705 1.00 69.04 ? 368 LEU B CB 1 ATOM 10054 C CG . LEU B 2 368 ? -18.038 14.102 24.415 1.00 67.57 ? 368 LEU B CG 1 ATOM 10055 C CD1 . LEU B 2 368 ? -16.570 13.787 24.655 1.00 65.85 ? 368 LEU B CD1 1 ATOM 10056 C CD2 . LEU B 2 368 ? -18.762 12.896 23.839 1.00 68.85 ? 368 LEU B CD2 1 ATOM 10057 N N . SER B 2 369 ? -21.398 14.342 27.620 1.00 79.39 ? 369 SER B N 1 ATOM 10058 C CA . SER B 2 369 ? -21.899 14.521 28.978 1.00 84.70 ? 369 SER B CA 1 ATOM 10059 C C . SER B 2 369 ? -21.144 13.594 29.924 1.00 86.66 ? 369 SER B C 1 ATOM 10060 O O . SER B 2 369 ? -20.736 12.504 29.530 1.00 99.47 ? 369 SER B O 1 ATOM 10061 C CB . SER B 2 369 ? -23.402 14.242 29.043 1.00 87.43 ? 369 SER B CB 1 ATOM 10062 O OG . SER B 2 369 ? -24.104 15.005 28.077 1.00 83.49 ? 369 SER B OG 1 ATOM 10063 N N . PHE B 2 370 ? -20.951 14.023 31.167 1.00 74.59 ? 370 PHE B N 1 ATOM 10064 C CA . PHE B 2 370 ? -20.166 13.235 32.112 1.00 72.08 ? 370 PHE B CA 1 ATOM 10065 C C . PHE B 2 370 ? -20.798 13.126 33.496 1.00 82.44 ? 370 PHE B C 1 ATOM 10066 O O . PHE B 2 370 ? -21.007 14.132 34.170 1.00 94.29 ? 370 PHE B O 1 ATOM 10067 C CB . PHE B 2 370 ? -18.762 13.829 32.256 1.00 68.59 ? 370 PHE B CB 1 ATOM 10068 C CG . PHE B 2 370 ? -18.018 13.960 30.959 1.00 67.58 ? 370 PHE B CG 1 ATOM 10069 C CD1 . PHE B 2 370 ? -18.086 15.130 30.221 1.00 81.24 ? 370 PHE B CD1 1 ATOM 10070 C CD2 . PHE B 2 370 ? -17.243 12.917 30.481 1.00 72.52 ? 370 PHE B CD2 1 ATOM 10071 C CE1 . PHE B 2 370 ? -17.401 15.255 29.028 1.00 84.30 ? 370 PHE B CE1 1 ATOM 10072 C CE2 . PHE B 2 370 ? -16.555 13.037 29.289 1.00 78.73 ? 370 PHE B CE2 1 ATOM 10073 C CZ . PHE B 2 370 ? -16.634 14.207 28.562 1.00 81.60 ? 370 PHE B CZ 1 ATOM 10074 N N . ASN B 2 371 ? -21.096 11.902 33.917 1.00 81.87 ? 371 ASN B N 1 ATOM 10075 C CA . ASN B 2 371 ? -21.380 11.632 35.321 1.00 88.29 ? 371 ASN B CA 1 ATOM 10076 C C . ASN B 2 371 ? -20.180 10.910 35.922 1.00 97.05 ? 371 ASN B C 1 ATOM 10077 O O . ASN B 2 371 ? -19.708 9.919 35.365 1.00 106.90 ? 371 ASN B O 1 ATOM 10078 C CB . ASN B 2 371 ? -22.641 10.787 35.501 1.00 94.93 ? 371 ASN B CB 1 ATOM 10079 C CG . ASN B 2 371 ? -23.822 11.295 34.696 1.00 105.62 ? 371 ASN B CG 1 ATOM 10080 O OD1 . ASN B 2 371 ? -23.686 12.154 33.826 1.00 105.94 ? 371 ASN B OD1 1 ATOM 10081 N ND2 . ASN B 2 371 ? -24.998 10.748 34.990 1.00 132.11 ? 371 ASN B ND2 1 ATOM 10082 N N . ALA B 2 372 ? -19.685 11.401 37.053 1.00 92.59 ? 372 ALA B N 1 ATOM 10083 C CA . ALA B 2 372 ? -18.483 10.830 37.651 1.00 88.29 ? 372 ALA B CA 1 ATOM 10084 C C . ALA B 2 372 ? -18.795 9.916 38.829 1.00 101.84 ? 372 ALA B C 1 ATOM 10085 O O . ALA B 2 372 ? -19.417 10.331 39.806 1.00 117.57 ? 372 ALA B O 1 ATOM 10086 C CB . ALA B 2 372 ? -17.538 11.935 38.090 1.00 81.05 ? 372 ALA B CB 1 ATOM 10087 N N . THR B 2 373 ? -18.353 8.667 38.726 1.00 95.45 ? 373 THR B N 1 ATOM 10088 C CA . THR B 2 373 ? -18.418 7.738 39.845 1.00 78.51 ? 373 THR B CA 1 ATOM 10089 C C . THR B 2 373 ? -17.033 7.617 40.467 1.00 74.32 ? 373 THR B C 1 ATOM 10090 O O . THR B 2 373 ? -16.119 7.051 39.867 1.00 76.23 ? 373 THR B O 1 ATOM 10091 C CB . THR B 2 373 ? -18.918 6.349 39.414 1.00 83.34 ? 373 THR B CB 1 ATOM 10092 O OG1 . THR B 2 373 ? -20.271 6.449 38.953 1.00 90.24 ? 373 THR B OG1 1 ATOM 10093 C CG2 . THR B 2 373 ? -18.859 5.378 40.582 1.00 87.55 ? 373 THR B CG2 1 ATOM 10094 N N . CYS B 2 374 ? -16.885 8.155 41.671 1.00 73.01 ? 374 CYS B N 1 ATOM 10095 C CA . CYS B 2 374 ? -15.590 8.189 42.338 1.00 72.44 ? 374 CYS B CA 1 ATOM 10096 C C . CYS B 2 374 ? -15.582 7.295 43.570 1.00 95.03 ? 374 CYS B C 1 ATOM 10097 O O . CYS B 2 374 ? -14.828 6.324 43.638 1.00 122.04 ? 374 CYS B O 1 ATOM 10098 C CB . CYS B 2 374 ? -15.224 9.623 42.722 1.00 71.78 ? 374 CYS B CB 1 ATOM 10099 S SG . CYS B 2 374 ? -15.253 10.791 41.342 1.00 105.85 ? 374 CYS B SG 1 ATOM 10100 N N . LEU B 2 375 ? -16.420 7.629 44.546 1.00 86.18 ? 375 LEU B N 1 ATOM 10101 C CA . LEU B 2 375 ? -16.477 6.872 45.789 1.00 84.71 ? 375 LEU B CA 1 ATOM 10102 C C . LEU B 2 375 ? -17.682 5.935 45.839 1.00 84.20 ? 375 LEU B C 1 ATOM 10103 O O . LEU B 2 375 ? -18.819 6.388 45.959 1.00 85.14 ? 375 LEU B O 1 ATOM 10104 C CB . LEU B 2 375 ? -16.514 7.830 46.978 1.00 80.53 ? 375 LEU B CB 1 ATOM 10105 C CG . LEU B 2 375 ? -16.658 7.201 48.361 1.00 93.22 ? 375 LEU B CG 1 ATOM 10106 C CD1 . LEU B 2 375 ? -15.469 6.306 48.669 1.00 111.00 ? 375 LEU B CD1 1 ATOM 10107 C CD2 . LEU B 2 375 ? -16.809 8.288 49.407 1.00 92.03 ? 375 LEU B CD2 1 ATOM 10108 N N . ASN B 2 376 ? -17.406 4.635 45.721 1.00 84.42 ? 376 ASN B N 1 ATOM 10109 C CA . ASN B 2 376 ? -18.381 3.541 45.853 1.00 85.94 ? 376 ASN B CA 1 ATOM 10110 C C . ASN B 2 376 ? -19.770 3.829 45.276 1.00 87.33 ? 376 ASN B C 1 ATOM 10111 O O . ASN B 2 376 ? -20.759 3.888 46.008 1.00 89.21 ? 376 ASN B O 1 ATOM 10112 C CB . ASN B 2 376 ? -18.504 3.086 47.322 1.00 94.67 ? 376 ASN B CB 1 ATOM 10113 C CG . ASN B 2 376 ? -18.710 4.232 48.301 1.00 102.00 ? 376 ASN B CG 1 ATOM 10114 O OD1 . ASN B 2 376 ? -19.582 5.079 48.123 1.00 119.99 ? 376 ASN B OD1 1 ATOM 10115 N ND2 . ASN B 2 376 ? -17.911 4.244 49.361 1.00 92.58 ? 376 ASN B ND2 1 ATOM 10116 N N . ASN B 2 377 ? -19.829 3.990 43.956 1.00 91.52 ? 377 ASN B N 1 ATOM 10117 C CA . ASN B 2 377 ? -21.085 4.186 43.233 1.00 98.42 ? 377 ASN B CA 1 ATOM 10118 C C . ASN B 2 377 ? -21.892 5.391 43.718 1.00 103.60 ? 377 ASN B C 1 ATOM 10119 O O . ASN B 2 377 ? -23.087 5.277 43.989 1.00 105.76 ? 377 ASN B O 1 ATOM 10120 C CB . ASN B 2 377 ? -21.947 2.923 43.326 1.00 99.05 ? 377 ASN B CB 1 ATOM 10121 C CG . ASN B 2 377 ? -21.134 1.651 43.181 1.00 105.68 ? 377 ASN B CG 1 ATOM 10122 O OD1 . ASN B 2 377 ? -21.044 0.850 44.112 1.00 105.65 ? 377 ASN B OD1 1 ATOM 10123 N ND2 . ASN B 2 377 ? -20.535 1.459 42.012 1.00 111.39 ? 377 ASN B ND2 1 ATOM 10124 N N . GLU B 2 378 ? -21.235 6.543 43.827 1.00 101.09 ? 378 GLU B N 1 ATOM 10125 C CA . GLU B 2 378 ? -21.902 7.765 44.267 1.00 107.14 ? 378 GLU B CA 1 ATOM 10126 C C . GLU B 2 378 ? -22.575 8.497 43.108 1.00 117.71 ? 378 GLU B C 1 ATOM 10127 O O . GLU B 2 378 ? -23.387 9.397 43.325 1.00 137.07 ? 378 GLU B O 1 ATOM 10128 C CB . GLU B 2 378 ? -20.908 8.695 44.962 1.00 112.07 ? 378 GLU B CB 1 ATOM 10129 C CG . GLU B 2 378 ? -19.763 9.150 44.075 1.00 111.99 ? 378 GLU B CG 1 ATOM 10130 C CD . GLU B 2 378 ? -18.828 10.109 44.782 1.00 133.26 ? 378 GLU B CD 1 ATOM 10131 O OE1 . GLU B 2 378 ? -19.008 10.330 45.998 1.00 144.05 ? 378 GLU B OE1 1 ATOM 10132 O OE2 . GLU B 2 378 ? -17.914 10.644 44.121 1.00 145.15 ? 378 GLU B OE2 1 ATOM 10133 N N . VAL B 2 379 ? -22.204 8.112 41.886 1.00 109.77 ? 379 VAL B N 1 ATOM 10134 C CA . VAL B 2 379 ? -22.788 8.599 40.623 1.00 95.72 ? 379 VAL B CA 1 ATOM 10135 C C . VAL B 2 379 ? -23.040 10.115 40.573 1.00 86.17 ? 379 VAL B C 1 ATOM 10136 O O . VAL B 2 379 ? -24.124 10.564 40.200 1.00 84.02 ? 379 VAL B O 1 ATOM 10137 C CB . VAL B 2 379 ? -24.114 7.837 40.256 1.00 107.80 ? 379 VAL B CB 1 ATOM 10138 C CG1 . VAL B 2 379 ? -23.814 6.375 39.946 1.00 104.77 ? 379 VAL B CG1 1 ATOM 10139 C CG2 . VAL B 2 379 ? -25.198 7.949 41.334 1.00 102.56 ? 379 VAL B CG2 1 ATOM 10140 N N . ILE B 2 380 ? -22.025 10.899 40.930 1.00 85.17 ? 380 ILE B N 1 ATOM 10141 C CA . ILE B 2 380 ? -22.122 12.356 40.857 1.00 84.87 ? 380 ILE B CA 1 ATOM 10142 C C . ILE B 2 380 ? -22.172 12.838 39.406 1.00 92.61 ? 380 ILE B C 1 ATOM 10143 O O . ILE B 2 380 ? -21.215 12.657 38.652 1.00 96.99 ? 380 ILE B O 1 ATOM 10144 C CB . ILE B 2 380 ? -20.944 13.039 41.577 1.00 85.66 ? 380 ILE B CB 1 ATOM 10145 C CG1 . ILE B 2 380 ? -21.032 12.802 43.086 1.00 106.11 ? 380 ILE B CG1 1 ATOM 10146 C CG2 . ILE B 2 380 ? -20.927 14.531 41.279 1.00 81.47 ? 380 ILE B CG2 1 ATOM 10147 C CD1 . ILE B 2 380 ? -19.965 13.522 43.885 1.00 116.79 ? 380 ILE B CD1 1 ATOM 10148 N N . PRO B 2 381 ? -23.297 13.458 39.015 1.00 93.37 ? 381 PRO B N 1 ATOM 10149 C CA . PRO B 2 381 ? -23.565 13.898 37.641 1.00 90.35 ? 381 PRO B CA 1 ATOM 10150 C C . PRO B 2 381 ? -22.870 15.203 37.259 1.00 87.79 ? 381 PRO B C 1 ATOM 10151 O O . PRO B 2 381 ? -22.493 15.984 38.132 1.00 91.50 ? 381 PRO B O 1 ATOM 10152 C CB . PRO B 2 381 ? -25.081 14.082 37.635 1.00 94.79 ? 381 PRO B CB 1 ATOM 10153 C CG . PRO B 2 381 ? -25.384 14.529 39.021 1.00 98.99 ? 381 PRO B CG 1 ATOM 10154 C CD . PRO B 2 381 ? -24.413 13.795 39.919 1.00 98.98 ? 381 PRO B CD 1 ATOM 10155 N N . GLY B 2 382 ? -22.703 15.424 35.958 1.00 85.48 ? 382 GLY B N 1 ATOM 10156 C CA . GLY B 2 382 ? -22.225 16.696 35.445 1.00 87.17 ? 382 GLY B CA 1 ATOM 10157 C C . GLY B 2 382 ? -20.735 16.943 35.584 1.00 80.69 ? 382 GLY B C 1 ATOM 10158 O O . GLY B 2 382 ? -20.224 17.946 35.089 1.00 92.68 ? 382 GLY B O 1 ATOM 10159 N N . LEU B 2 383 ? -20.032 16.032 36.249 1.00 71.84 ? 383 LEU B N 1 ATOM 10160 C CA . LEU B 2 383 ? -18.617 16.240 36.534 1.00 72.78 ? 383 LEU B CA 1 ATOM 10161 C C . LEU B 2 383 ? -17.721 15.252 35.790 1.00 75.56 ? 383 LEU B C 1 ATOM 10162 O O . LEU B 2 383 ? -17.955 14.046 35.813 1.00 78.97 ? 383 LEU B O 1 ATOM 10163 C CB . LEU B 2 383 ? -18.367 16.143 38.040 1.00 74.74 ? 383 LEU B CB 1 ATOM 10164 C CG . LEU B 2 383 ? -17.003 16.637 38.520 1.00 89.64 ? 383 LEU B CG 1 ATOM 10165 C CD1 . LEU B 2 383 ? -16.715 18.019 37.957 1.00 100.51 ? 383 LEU B CD1 1 ATOM 10166 C CD2 . LEU B 2 383 ? -16.948 16.653 40.040 1.00 99.34 ? 383 LEU B CD2 1 ATOM 10167 N N . LYS B 2 384 ? -16.702 15.777 35.116 1.00 72.56 ? 384 LYS B N 1 ATOM 10168 C CA . LYS B 2 384 ? -15.752 14.946 34.386 1.00 68.55 ? 384 LYS B CA 1 ATOM 10169 C C . LYS B 2 384 ? -14.489 14.674 35.202 1.00 73.58 ? 384 LYS B C 1 ATOM 10170 O O . LYS B 2 384 ? -13.547 14.055 34.707 1.00 81.52 ? 384 LYS B O 1 ATOM 10171 C CB . LYS B 2 384 ? -15.383 15.598 33.051 1.00 68.56 ? 384 LYS B CB 1 ATOM 10172 C CG . LYS B 2 384 ? -14.517 16.839 33.179 1.00 89.88 ? 384 LYS B CG 1 ATOM 10173 C CD . LYS B 2 384 ? -14.326 17.520 31.833 1.00 94.18 ? 384 LYS B CD 1 ATOM 10174 C CE . LYS B 2 384 ? -15.652 18.016 31.278 1.00 104.37 ? 384 LYS B CE 1 ATOM 10175 N NZ . LYS B 2 384 ? -15.478 18.781 30.013 1.00 112.36 ? 384 LYS B NZ 1 ATOM 10176 N N . SER B 2 385 ? -14.463 15.148 36.444 1.00 74.25 ? 385 SER B N 1 ATOM 10177 C CA . SER B 2 385 ? -13.279 14.998 37.286 1.00 79.87 ? 385 SER B CA 1 ATOM 10178 C C . SER B 2 385 ? -13.583 14.377 38.649 1.00 77.66 ? 385 SER B C 1 ATOM 10179 O O . SER B 2 385 ? -14.715 14.422 39.128 1.00 72.58 ? 385 SER B O 1 ATOM 10180 C CB . SER B 2 385 ? -12.597 16.355 37.479 1.00 92.68 ? 385 SER B CB 1 ATOM 10181 O OG . SER B 2 385 ? -13.519 17.335 37.921 1.00 106.93 ? 385 SER B OG 1 ATOM 10182 N N . CYS B 2 386 ? -12.557 13.794 39.265 1.00 82.61 ? 386 CYS B N 1 ATOM 10183 C CA . CYS B 2 386 ? -12.680 13.193 40.591 1.00 74.88 ? 386 CYS B CA 1 ATOM 10184 C C . CYS B 2 386 ? -11.490 13.566 41.473 1.00 71.43 ? 386 CYS B C 1 ATOM 10185 O O . CYS B 2 386 ? -10.339 13.324 41.109 1.00 69.59 ? 386 CYS B O 1 ATOM 10186 C CB . CYS B 2 386 ? -12.798 11.671 40.486 1.00 67.48 ? 386 CYS B CB 1 ATOM 10187 S SG . CYS B 2 386 ? -14.260 11.091 39.596 1.00 137.18 ? 386 CYS B SG 1 ATOM 10188 N N . MET B 2 387 ? -11.771 14.152 42.633 1.00 72.53 ? 387 MET B N 1 ATOM 10189 C CA . MET B 2 387 ? -10.717 14.593 43.542 1.00 74.33 ? 387 MET B CA 1 ATOM 10190 C C . MET B 2 387 ? -10.568 13.673 44.752 1.00 75.45 ? 387 MET B C 1 ATOM 10191 O O . MET B 2 387 ? -11.304 12.699 44.901 1.00 77.58 ? 387 MET B O 1 ATOM 10192 C CB . MET B 2 387 ? -10.990 16.019 44.021 1.00 75.39 ? 387 MET B CB 1 ATOM 10193 C CG . MET B 2 387 ? -12.258 16.154 44.848 1.00 77.41 ? 387 MET B CG 1 ATOM 10194 S SD . MET B 2 387 ? -12.277 17.654 45.845 1.00 144.12 ? 387 MET B SD 1 ATOM 10195 C CE . MET B 2 387 ? -10.825 17.396 46.860 1.00 72.72 ? 387 MET B CE 1 ATOM 10196 N N . GLY B 2 388 ? -9.613 14.007 45.617 1.00 76.26 ? 388 GLY B N 1 ATOM 10197 C CA . GLY B 2 388 ? -9.388 13.280 46.855 1.00 82.52 ? 388 GLY B CA 1 ATOM 10198 C C . GLY B 2 388 ? -9.020 11.824 46.656 1.00 95.38 ? 388 GLY B C 1 ATOM 10199 O O . GLY B 2 388 ? -9.603 10.939 47.279 1.00 103.80 ? 388 GLY B O 1 ATOM 10200 N N . LEU B 2 389 ? -8.034 11.571 45.803 1.00 96.97 ? 389 LEU B N 1 ATOM 10201 C CA . LEU B 2 389 ? -7.681 10.202 45.450 1.00 94.98 ? 389 LEU B CA 1 ATOM 10202 C C . LEU B 2 389 ? -6.271 9.823 45.884 1.00 91.29 ? 389 LEU B C 1 ATOM 10203 O O . LEU B 2 389 ? -5.409 10.680 46.075 1.00 79.83 ? 389 LEU B O 1 ATOM 10204 C CB . LEU B 2 389 ? -7.828 9.992 43.942 1.00 86.08 ? 389 LEU B CB 1 ATOM 10205 C CG . LEU B 2 389 ? -9.232 10.204 43.376 1.00 79.36 ? 389 LEU B CG 1 ATOM 10206 C CD1 . LEU B 2 389 ? -9.254 9.953 41.879 1.00 72.69 ? 389 LEU B CD1 1 ATOM 10207 C CD2 . LEU B 2 389 ? -10.231 9.307 44.084 1.00 89.28 ? 389 LEU B CD2 1 ATOM 10208 N N . LYS B 2 390 ? -6.053 8.522 46.045 1.00 95.64 ? 390 LYS B N 1 ATOM 10209 C CA . LYS B 2 390 ? -4.737 7.983 46.355 1.00 95.41 ? 390 LYS B CA 1 ATOM 10210 C C . LYS B 2 390 ? -4.314 7.028 45.247 1.00 100.38 ? 390 LYS B C 1 ATOM 10211 O O . LYS B 2 390 ? -5.155 6.529 44.499 1.00 110.89 ? 390 LYS B O 1 ATOM 10212 C CB . LYS B 2 390 ? -4.746 7.264 47.706 1.00 92.90 ? 390 LYS B CB 1 ATOM 10213 C CG . LYS B 2 390 ? -5.238 8.115 48.866 1.00 97.53 ? 390 LYS B CG 1 ATOM 10214 C CD . LYS B 2 390 ? -5.348 7.292 50.141 1.00 112.93 ? 390 LYS B CD 1 ATOM 10215 C CE . LYS B 2 390 ? -5.890 8.123 51.294 1.00 116.94 ? 390 LYS B CE 1 ATOM 10216 N NZ . LYS B 2 390 ? -6.063 7.310 52.531 1.00 111.03 ? 390 LYS B NZ 1 ATOM 10217 N N . ILE B 2 391 ? -3.013 6.784 45.132 1.00 92.56 ? 391 ILE B N 1 ATOM 10218 C CA . ILE B 2 391 ? -2.502 5.845 44.140 1.00 87.49 ? 391 ILE B CA 1 ATOM 10219 C C . ILE B 2 391 ? -3.014 4.439 44.440 1.00 88.39 ? 391 ILE B C 1 ATOM 10220 O O . ILE B 2 391 ? -2.895 3.954 45.565 1.00 96.80 ? 391 ILE B O 1 ATOM 10221 C CB . ILE B 2 391 ? -0.957 5.837 44.093 1.00 88.85 ? 391 ILE B CB 1 ATOM 10222 C CG1 . ILE B 2 391 ? -0.425 7.129 43.465 1.00 89.29 ? 391 ILE B CG1 1 ATOM 10223 C CG2 . ILE B 2 391 ? -0.449 4.639 43.306 1.00 88.52 ? 391 ILE B CG2 1 ATOM 10224 C CD1 . ILE B 2 391 ? -0.283 8.285 44.433 1.00 95.95 ? 391 ILE B CD1 1 ATOM 10225 N N . GLY B 2 392 ? -3.584 3.789 43.430 1.00 84.64 ? 392 GLY B N 1 ATOM 10226 C CA . GLY B 2 392 ? -4.169 2.473 43.603 1.00 105.56 ? 392 GLY B CA 1 ATOM 10227 C C . GLY B 2 392 ? -5.683 2.507 43.541 1.00 109.93 ? 392 GLY B C 1 ATOM 10228 O O . GLY B 2 392 ? -6.333 1.468 43.423 1.00 117.55 ? 392 GLY B O 1 ATOM 10229 N N . ASP B 2 393 ? -6.246 3.708 43.625 1.00 96.47 ? 393 ASP B N 1 ATOM 10230 C CA . ASP B 2 393 ? -7.689 3.886 43.509 1.00 98.63 ? 393 ASP B CA 1 ATOM 10231 C C . ASP B 2 393 ? -8.132 3.868 42.049 1.00 93.06 ? 393 ASP B C 1 ATOM 10232 O O . ASP B 2 393 ? -7.357 4.194 41.150 1.00 78.59 ? 393 ASP B O 1 ATOM 10233 C CB . ASP B 2 393 ? -8.126 5.191 44.178 1.00 105.01 ? 393 ASP B CB 1 ATOM 10234 C CG . ASP B 2 393 ? -7.984 5.147 45.687 1.00 107.16 ? 393 ASP B CG 1 ATOM 10235 O OD1 . ASP B 2 393 ? -8.129 4.051 46.268 1.00 106.25 ? 393 ASP B OD1 1 ATOM 10236 O OD2 . ASP B 2 393 ? -7.730 6.209 46.294 1.00 103.96 ? 393 ASP B OD2 1 ATOM 10237 N N . THR B 2 394 ? -9.384 3.483 41.824 1.00 94.28 ? 394 THR B N 1 ATOM 10238 C CA . THR B 2 394 ? -9.939 3.419 40.478 1.00 75.66 ? 394 THR B CA 1 ATOM 10239 C C . THR B 2 394 ? -11.274 4.151 40.411 1.00 73.95 ? 394 THR B C 1 ATOM 10240 O O . THR B 2 394 ? -12.147 3.942 41.253 1.00 92.01 ? 394 THR B O 1 ATOM 10241 C CB . THR B 2 394 ? -10.134 1.962 40.019 1.00 78.60 ? 394 THR B CB 1 ATOM 10242 O OG1 . THR B 2 394 ? -8.917 1.230 40.210 1.00 102.01 ? 394 THR B OG1 1 ATOM 10243 C CG2 . THR B 2 394 ? -10.528 1.910 38.552 1.00 74.23 ? 394 THR B CG2 1 ATOM 10244 N N . VAL B 2 395 ? -11.431 5.010 39.408 1.00 70.98 ? 395 VAL B N 1 ATOM 10245 C CA . VAL B 2 395 ? -12.666 5.767 39.244 1.00 78.77 ? 395 VAL B CA 1 ATOM 10246 C C . VAL B 2 395 ? -13.339 5.454 37.912 1.00 73.99 ? 395 VAL B C 1 ATOM 10247 O O . VAL B 2 395 ? -12.696 4.980 36.975 1.00 67.25 ? 395 VAL B O 1 ATOM 10248 C CB . VAL B 2 395 ? -12.419 7.285 39.339 1.00 75.77 ? 395 VAL B CB 1 ATOM 10249 C CG1 . VAL B 2 395 ? -12.007 7.668 40.752 1.00 73.84 ? 395 VAL B CG1 1 ATOM 10250 C CG2 . VAL B 2 395 ? -11.366 7.719 38.329 1.00 69.86 ? 395 VAL B CG2 1 ATOM 10251 N N . SER B 2 396 ? -14.640 5.717 37.840 1.00 67.66 ? 396 SER B N 1 ATOM 10252 C CA . SER B 2 396 ? -15.412 5.442 36.636 1.00 68.12 ? 396 SER B CA 1 ATOM 10253 C C . SER B 2 396 ? -16.099 6.697 36.110 1.00 74.38 ? 396 SER B C 1 ATOM 10254 O O . SER B 2 396 ? -16.480 7.579 36.878 1.00 77.16 ? 396 SER B O 1 ATOM 10255 C CB . SER B 2 396 ? -16.452 4.354 36.909 1.00 69.13 ? 396 SER B CB 1 ATOM 10256 O OG . SER B 2 396 ? -17.286 4.153 35.781 1.00 79.55 ? 396 SER B OG 1 ATOM 10257 N N . PHE B 2 397 ? -16.251 6.767 34.792 1.00 75.65 ? 397 PHE B N 1 ATOM 10258 C CA . PHE B 2 397 ? -16.950 7.874 34.152 1.00 71.67 ? 397 PHE B CA 1 ATOM 10259 C C . PHE B 2 397 ? -17.936 7.360 33.112 1.00 78.07 ? 397 PHE B C 1 ATOM 10260 O O . PHE B 2 397 ? -17.558 6.633 32.194 1.00 82.20 ? 397 PHE B O 1 ATOM 10261 C CB . PHE B 2 397 ? -15.963 8.835 33.484 1.00 71.87 ? 397 PHE B CB 1 ATOM 10262 C CG . PHE B 2 397 ? -15.037 9.526 34.441 1.00 67.61 ? 397 PHE B CG 1 ATOM 10263 C CD1 . PHE B 2 397 ? -13.763 9.033 34.671 1.00 72.52 ? 397 PHE B CD1 1 ATOM 10264 C CD2 . PHE B 2 397 ? -15.433 10.678 35.098 1.00 67.86 ? 397 PHE B CD2 1 ATOM 10265 C CE1 . PHE B 2 397 ? -12.906 9.672 35.546 1.00 82.16 ? 397 PHE B CE1 1 ATOM 10266 C CE2 . PHE B 2 397 ? -14.581 11.321 35.974 1.00 79.70 ? 397 PHE B CE2 1 ATOM 10267 C CZ . PHE B 2 397 ? -13.315 10.817 36.198 1.00 87.58 ? 397 PHE B CZ 1 ATOM 10268 N N . SER B 2 398 ? -19.202 7.734 33.258 1.00 88.08 ? 398 SER B N 1 ATOM 10269 C CA . SER B 2 398 ? -20.192 7.442 32.232 1.00 84.20 ? 398 SER B CA 1 ATOM 10270 C C . SER B 2 398 ? -20.283 8.632 31.283 1.00 82.67 ? 398 SER B C 1 ATOM 10271 O O . SER B 2 398 ? -20.385 9.779 31.719 1.00 70.93 ? 398 SER B O 1 ATOM 10272 C CB . SER B 2 398 ? -21.555 7.129 32.852 1.00 81.65 ? 398 SER B CB 1 ATOM 10273 O OG . SER B 2 398 ? -22.022 8.209 33.640 1.00 92.20 ? 398 SER B OG 1 ATOM 10274 N N . ILE B 2 399 ? -20.229 8.354 29.985 1.00 79.91 ? 399 ILE B N 1 ATOM 10275 C CA . ILE B 2 399 ? -20.188 9.411 28.981 1.00 65.51 ? 399 ILE B CA 1 ATOM 10276 C C . ILE B 2 399 ? -21.304 9.265 27.953 1.00 65.65 ? 399 ILE B C 1 ATOM 10277 O O . ILE B 2 399 ? -21.523 8.182 27.413 1.00 73.27 ? 399 ILE B O 1 ATOM 10278 C CB . ILE B 2 399 ? -18.832 9.429 28.248 1.00 64.98 ? 399 ILE B CB 1 ATOM 10279 C CG1 . ILE B 2 399 ? -17.685 9.557 29.251 1.00 65.83 ? 399 ILE B CG1 1 ATOM 10280 C CG2 . ILE B 2 399 ? -18.785 10.561 27.233 1.00 66.52 ? 399 ILE B CG2 1 ATOM 10281 C CD1 . ILE B 2 399 ? -16.316 9.525 28.618 1.00 80.84 ? 399 ILE B CD1 1 ATOM 10282 N N . GLU B 2 400 ? -22.008 10.361 27.691 1.00 69.94 ? 400 GLU B N 1 ATOM 10283 C CA . GLU B 2 400 ? -23.046 10.381 26.669 1.00 75.81 ? 400 GLU B CA 1 ATOM 10284 C C . GLU B 2 400 ? -22.581 11.191 25.465 1.00 70.01 ? 400 GLU B C 1 ATOM 10285 O O . GLU B 2 400 ? -22.061 12.296 25.616 1.00 67.67 ? 400 GLU B O 1 ATOM 10286 C CB . GLU B 2 400 ? -24.346 10.965 27.226 1.00 88.47 ? 400 GLU B CB 1 ATOM 10287 C CG . GLU B 2 400 ? -25.534 10.838 26.287 1.00 87.98 ? 400 GLU B CG 1 ATOM 10288 C CD . GLU B 2 400 ? -26.715 11.683 26.723 1.00 100.07 ? 400 GLU B CD 1 ATOM 10289 O OE1 . GLU B 2 400 ? -27.863 11.316 26.395 1.00 99.83 ? 400 GLU B OE1 1 ATOM 10290 O OE2 . GLU B 2 400 ? -26.496 12.718 27.387 1.00 111.84 ? 400 GLU B OE2 1 ATOM 10291 N N . ALA B 2 401 ? -22.766 10.639 24.272 1.00 74.86 ? 401 ALA B N 1 ATOM 10292 C CA . ALA B 2 401 ? -22.361 11.321 23.048 1.00 79.93 ? 401 ALA B CA 1 ATOM 10293 C C . ALA B 2 401 ? -23.561 11.579 22.143 1.00 88.28 ? 401 ALA B C 1 ATOM 10294 O O . ALA B 2 401 ? -24.171 10.643 21.627 1.00 92.95 ? 401 ALA B O 1 ATOM 10295 C CB . ALA B 2 401 ? -21.306 10.510 22.314 1.00 76.43 ? 401 ALA B CB 1 ATOM 10296 N N . LYS B 2 402 ? -23.893 12.851 21.952 1.00 84.69 ? 402 LYS B N 1 ATOM 10297 C CA . LYS B 2 402 ? -25.025 13.225 21.112 1.00 85.63 ? 402 LYS B CA 1 ATOM 10298 C C . LYS B 2 402 ? -24.595 14.138 19.974 1.00 86.11 ? 402 LYS B C 1 ATOM 10299 O O . LYS B 2 402 ? -23.988 15.182 20.203 1.00 88.91 ? 402 LYS B O 1 ATOM 10300 C CB . LYS B 2 402 ? -26.112 13.911 21.941 1.00 98.83 ? 402 LYS B CB 1 ATOM 10301 C CG . LYS B 2 402 ? -27.405 14.144 21.176 1.00 118.06 ? 402 LYS B CG 1 ATOM 10302 C CD . LYS B 2 402 ? -28.486 14.723 22.071 1.00 132.16 ? 402 LYS B CD 1 ATOM 10303 C CE . LYS B 2 402 ? -29.816 14.806 21.339 1.00 143.28 ? 402 LYS B CE 1 ATOM 10304 N NZ . LYS B 2 402 ? -29.718 15.626 20.100 1.00 148.54 ? 402 LYS B NZ 1 ATOM 10305 N N . VAL B 2 403 ? -24.920 13.743 18.748 1.00 84.97 ? 403 VAL B N 1 ATOM 10306 C CA . VAL B 2 403 ? -24.587 14.539 17.575 1.00 86.24 ? 403 VAL B CA 1 ATOM 10307 C C . VAL B 2 403 ? -25.823 15.274 17.057 1.00 93.03 ? 403 VAL B C 1 ATOM 10308 O O . VAL B 2 403 ? -26.928 14.729 17.058 1.00 100.72 ? 403 VAL B O 1 ATOM 10309 C CB . VAL B 2 403 ? -23.982 13.660 16.451 1.00 96.14 ? 403 VAL B CB 1 ATOM 10310 C CG1 . VAL B 2 403 ? -24.941 12.544 16.056 1.00 93.91 ? 403 VAL B CG1 1 ATOM 10311 C CG2 . VAL B 2 403 ? -23.603 14.507 15.243 1.00 106.57 ? 403 VAL B CG2 1 ATOM 10312 N N . ARG B 2 404 ? -25.637 16.521 16.636 1.00 89.70 ? 404 ARG B N 1 ATOM 10313 C CA . ARG B 2 404 ? -26.720 17.282 16.028 1.00 93.90 ? 404 ARG B CA 1 ATOM 10314 C C . ARG B 2 404 ? -26.660 17.119 14.515 1.00 96.66 ? 404 ARG B C 1 ATOM 10315 O O . ARG B 2 404 ? -25.741 17.618 13.865 1.00 96.65 ? 404 ARG B O 1 ATOM 10316 C CB . ARG B 2 404 ? -26.634 18.759 16.418 1.00 95.55 ? 404 ARG B CB 1 ATOM 10317 C CG . ARG B 2 404 ? -27.799 19.600 15.921 1.00 110.04 ? 404 ARG B CG 1 ATOM 10318 C CD . ARG B 2 404 ? -27.742 21.024 16.457 1.00 109.83 ? 404 ARG B CD 1 ATOM 10319 N NE . ARG B 2 404 ? -26.612 21.778 15.923 1.00 114.90 ? 404 ARG B NE 1 ATOM 10320 C CZ . ARG B 2 404 ? -25.488 22.021 16.591 1.00 115.78 ? 404 ARG B CZ 1 ATOM 10321 N NH1 . ARG B 2 404 ? -25.339 21.569 17.828 1.00 119.42 ? 404 ARG B NH1 1 ATOM 10322 N NH2 . ARG B 2 404 ? -24.514 22.718 16.021 1.00 110.15 ? 404 ARG B NH2 1 ATOM 10323 N N . GLY B 2 405 ? -27.649 16.424 13.961 1.00 101.43 ? 405 GLY B N 1 ATOM 10324 C CA . GLY B 2 405 ? -27.628 16.051 12.559 1.00 114.98 ? 405 GLY B CA 1 ATOM 10325 C C . GLY B 2 405 ? -26.417 15.186 12.268 1.00 130.34 ? 405 GLY B C 1 ATOM 10326 O O . GLY B 2 405 ? -26.096 14.284 13.042 1.00 151.13 ? 405 GLY B O 1 ATOM 10327 N N . CYS B 2 406 ? -25.741 15.484 11.161 1.00 122.03 ? 406 CYS B N 1 ATOM 10328 C CA . CYS B 2 406 ? -24.480 14.845 10.785 1.00 125.20 ? 406 CYS B CA 1 ATOM 10329 C C . CYS B 2 406 ? -23.975 15.474 9.495 1.00 128.35 ? 406 CYS B C 1 ATOM 10330 O O . CYS B 2 406 ? -24.743 15.657 8.551 1.00 136.19 ? 406 CYS B O 1 ATOM 10331 C CB . CYS B 2 406 ? -24.651 13.334 10.603 1.00 139.97 ? 406 CYS B CB 1 ATOM 10332 S SG . CYS B 2 406 ? -26.033 12.861 9.538 1.00 148.09 ? 406 CYS B SG 1 ATOM 10333 N N . PRO B 2 407 ? -22.676 15.804 9.445 1.00 125.76 ? 407 PRO B N 1 ATOM 10334 C CA . PRO B 2 407 ? -22.174 16.521 8.270 1.00 152.18 ? 407 PRO B CA 1 ATOM 10335 C C . PRO B 2 407 ? -21.690 15.607 7.150 1.00 153.79 ? 407 PRO B C 1 ATOM 10336 O O . PRO B 2 407 ? -20.624 15.882 6.597 1.00 146.96 ? 407 PRO B O 1 ATOM 10337 C CB . PRO B 2 407 ? -21.003 17.313 8.845 1.00 152.89 ? 407 PRO B CB 1 ATOM 10338 C CG . PRO B 2 407 ? -20.447 16.386 9.894 1.00 136.87 ? 407 PRO B CG 1 ATOM 10339 C CD . PRO B 2 407 ? -21.632 15.631 10.471 1.00 117.64 ? 407 PRO B CD 1 ATOM 10340 N N . GLN B 2 408 ? -22.475 14.586 6.809 1.00 149.32 ? 408 GLN B N 1 ATOM 10341 C CA . GLN B 2 408 ? -22.149 13.639 5.739 1.00 149.92 ? 408 GLN B CA 1 ATOM 10342 C C . GLN B 2 408 ? -20.657 13.306 5.713 1.00 160.51 ? 408 GLN B C 1 ATOM 10343 O O . GLN B 2 408 ? -19.951 13.645 4.763 1.00 168.94 ? 408 GLN B O 1 ATOM 10344 C CB . GLN B 2 408 ? -22.601 14.182 4.381 1.00 148.13 ? 408 GLN B CB 1 ATOM 10345 C CG . GLN B 2 408 ? -22.561 13.153 3.253 1.00 155.23 ? 408 GLN B CG 1 ATOM 10346 C CD . GLN B 2 408 ? -23.168 11.820 3.653 1.00 151.59 ? 408 GLN B CD 1 ATOM 10347 O OE1 . GLN B 2 408 ? -24.259 11.765 4.220 1.00 153.78 ? 408 GLN B OE1 1 ATOM 10348 N NE2 . GLN B 2 408 ? -22.456 10.737 3.363 1.00 143.51 ? 408 GLN B NE2 1 ATOM 10349 N N . GLU B 2 409 ? -20.172 12.665 6.769 1.00 159.11 ? 409 GLU B N 1 ATOM 10350 C CA . GLU B 2 409 ? -18.746 12.400 6.882 1.00 155.70 ? 409 GLU B CA 1 ATOM 10351 C C . GLU B 2 409 ? -18.448 10.938 6.575 1.00 160.54 ? 409 GLU B C 1 ATOM 10352 O O . GLU B 2 409 ? -19.361 10.144 6.346 1.00 157.87 ? 409 GLU B O 1 ATOM 10353 C CB . GLU B 2 409 ? -18.249 12.772 8.285 1.00 146.03 ? 409 GLU B CB 1 ATOM 10354 C CG . GLU B 2 409 ? -16.770 13.138 8.372 1.00 143.55 ? 409 GLU B CG 1 ATOM 10355 C CD . GLU B 2 409 ? -16.433 14.417 7.631 1.00 155.00 ? 409 GLU B CD 1 ATOM 10356 O OE1 . GLU B 2 409 ? -17.342 15.249 7.424 1.00 157.88 ? 409 GLU B OE1 1 ATOM 10357 O OE2 . GLU B 2 409 ? -15.254 14.591 7.255 1.00 164.92 ? 409 GLU B OE2 1 ATOM 10358 N N . LYS B 2 410 ? -17.167 10.589 6.570 1.00 164.29 ? 410 LYS B N 1 ATOM 10359 C CA . LYS B 2 410 ? -16.754 9.202 6.441 1.00 168.84 ? 410 LYS B CA 1 ATOM 10360 C C . LYS B 2 410 ? -16.408 8.672 7.824 1.00 158.39 ? 410 LYS B C 1 ATOM 10361 O O . LYS B 2 410 ? -17.131 7.849 8.386 1.00 160.93 ? 410 LYS B O 1 ATOM 10362 C CB . LYS B 2 410 ? -15.560 9.070 5.494 1.00 171.18 ? 410 LYS B CB 1 ATOM 10363 C CG . LYS B 2 410 ? -15.838 9.538 4.075 1.00 169.14 ? 410 LYS B CG 1 ATOM 10364 C CD . LYS B 2 410 ? -16.952 8.725 3.435 1.00 161.29 ? 410 LYS B CD 1 ATOM 10365 C CE . LYS B 2 410 ? -17.214 9.171 2.006 1.00 166.74 ? 410 LYS B CE 1 ATOM 10366 N NZ . LYS B 2 410 ? -17.647 10.594 1.938 1.00 166.87 ? 410 LYS B NZ 1 ATOM 10367 N N . GLU B 2 411 ? -15.299 9.159 8.369 1.00 136.99 ? 411 GLU B N 1 ATOM 10368 C CA . GLU B 2 411 ? -14.913 8.830 9.732 1.00 123.99 ? 411 GLU B CA 1 ATOM 10369 C C . GLU B 2 411 ? -14.125 9.965 10.375 1.00 113.26 ? 411 GLU B C 1 ATOM 10370 O O . GLU B 2 411 ? -13.317 10.623 9.720 1.00 114.54 ? 411 GLU B O 1 ATOM 10371 C CB . GLU B 2 411 ? -14.090 7.539 9.759 1.00 138.25 ? 411 GLU B CB 1 ATOM 10372 C CG . GLU B 2 411 ? -13.645 7.111 11.150 1.00 137.75 ? 411 GLU B CG 1 ATOM 10373 C CD . GLU B 2 411 ? -12.803 5.851 11.133 1.00 140.38 ? 411 GLU B CD 1 ATOM 10374 O OE1 . GLU B 2 411 ? -12.313 5.450 12.210 1.00 141.00 ? 411 GLU B OE1 1 ATOM 10375 O OE2 . GLU B 2 411 ? -12.633 5.262 10.046 1.00 140.91 ? 411 GLU B OE2 1 ATOM 10376 N N . LYS B 2 412 ? -14.370 10.189 11.660 1.00 105.01 ? 412 LYS B N 1 ATOM 10377 C CA . LYS B 2 412 ? -13.537 11.077 12.457 1.00 103.27 ? 412 LYS B CA 1 ATOM 10378 C C . LYS B 2 412 ? -13.109 10.346 13.720 1.00 97.20 ? 412 LYS B C 1 ATOM 10379 O O . LYS B 2 412 ? -13.530 9.215 13.963 1.00 100.42 ? 412 LYS B O 1 ATOM 10380 C CB . LYS B 2 412 ? -14.282 12.366 12.812 1.00 108.32 ? 412 LYS B CB 1 ATOM 10381 C CG . LYS B 2 412 ? -14.359 13.383 11.684 1.00 115.68 ? 412 LYS B CG 1 ATOM 10382 C CD . LYS B 2 412 ? -12.972 13.845 11.263 1.00 116.06 ? 412 LYS B CD 1 ATOM 10383 C CE . LYS B 2 412 ? -13.044 15.085 10.385 1.00 113.06 ? 412 LYS B CE 1 ATOM 10384 N NZ . LYS B 2 412 ? -13.575 16.259 11.132 1.00 106.61 ? 412 LYS B NZ 1 ATOM 10385 N N . SER B 2 413 ? -12.274 10.990 14.525 1.00 88.79 ? 413 SER B N 1 ATOM 10386 C CA . SER B 2 413 ? -11.835 10.397 15.779 1.00 81.89 ? 413 SER B CA 1 ATOM 10387 C C . SER B 2 413 ? -11.514 11.465 16.814 1.00 83.91 ? 413 SER B C 1 ATOM 10388 O O . SER B 2 413 ? -10.989 12.527 16.482 1.00 95.83 ? 413 SER B O 1 ATOM 10389 C CB . SER B 2 413 ? -10.613 9.504 15.551 1.00 81.71 ? 413 SER B CB 1 ATOM 10390 O OG . SER B 2 413 ? -10.920 8.430 14.680 1.00 93.73 ? 413 SER B OG 1 ATOM 10391 N N . PHE B 2 414 ? -11.834 11.176 18.070 1.00 75.51 ? 414 PHE B N 1 ATOM 10392 C CA . PHE B 2 414 ? -11.431 12.037 19.172 1.00 70.09 ? 414 PHE B CA 1 ATOM 10393 C C . PHE B 2 414 ? -10.923 11.181 20.321 1.00 72.56 ? 414 PHE B C 1 ATOM 10394 O O . PHE B 2 414 ? -11.272 10.005 20.434 1.00 77.62 ? 414 PHE B O 1 ATOM 10395 C CB . PHE B 2 414 ? -12.584 12.938 19.626 1.00 67.79 ? 414 PHE B CB 1 ATOM 10396 C CG . PHE B 2 414 ? -13.762 12.196 20.190 1.00 65.93 ? 414 PHE B CG 1 ATOM 10397 C CD1 . PHE B 2 414 ? -13.870 11.973 21.553 1.00 64.17 ? 414 PHE B CD1 1 ATOM 10398 C CD2 . PHE B 2 414 ? -14.771 11.740 19.361 1.00 67.70 ? 414 PHE B CD2 1 ATOM 10399 C CE1 . PHE B 2 414 ? -14.956 11.297 22.076 1.00 69.90 ? 414 PHE B CE1 1 ATOM 10400 C CE2 . PHE B 2 414 ? -15.860 11.065 19.878 1.00 67.44 ? 414 PHE B CE2 1 ATOM 10401 C CZ . PHE B 2 414 ? -15.952 10.844 21.236 1.00 65.64 ? 414 PHE B CZ 1 ATOM 10402 N N . THR B 2 415 ? -10.093 11.773 21.170 1.00 65.67 ? 415 THR B N 1 ATOM 10403 C CA . THR B 2 415 ? -9.456 11.027 22.244 1.00 63.69 ? 415 THR B CA 1 ATOM 10404 C C . THR B 2 415 ? -9.871 11.534 23.619 1.00 61.59 ? 415 THR B C 1 ATOM 10405 O O . THR B 2 415 ? -9.786 12.727 23.906 1.00 62.53 ? 415 THR B O 1 ATOM 10406 C CB . THR B 2 415 ? -7.923 11.089 22.128 1.00 64.04 ? 415 THR B CB 1 ATOM 10407 O OG1 . THR B 2 415 ? -7.517 10.561 20.859 1.00 66.34 ? 415 THR B OG1 1 ATOM 10408 C CG2 . THR B 2 415 ? -7.274 10.283 23.236 1.00 79.69 ? 415 THR B CG2 1 ATOM 10409 N N . ILE B 2 416 ? -10.329 10.614 24.460 1.00 66.41 ? 416 ILE B N 1 ATOM 10410 C CA . ILE B 2 416 ? -10.632 10.921 25.850 1.00 66.15 ? 416 ILE B CA 1 ATOM 10411 C C . ILE B 2 416 ? -9.568 10.302 26.746 1.00 66.48 ? 416 ILE B C 1 ATOM 10412 O O . ILE B 2 416 ? -9.358 9.089 26.724 1.00 73.63 ? 416 ILE B O 1 ATOM 10413 C CB . ILE B 2 416 ? -12.021 10.402 26.261 1.00 71.18 ? 416 ILE B CB 1 ATOM 10414 C CG1 . ILE B 2 416 ? -13.096 10.962 25.328 1.00 73.51 ? 416 ILE B CG1 1 ATOM 10415 C CG2 . ILE B 2 416 ? -12.319 10.765 27.709 1.00 73.51 ? 416 ILE B CG2 1 ATOM 10416 C CD1 . ILE B 2 416 ? -14.482 10.425 25.600 1.00 60.66 ? 416 ILE B CD1 1 ATOM 10417 N N . LYS B 2 417 ? -8.888 11.136 27.525 1.00 59.33 ? 417 LYS B N 1 ATOM 10418 C CA . LYS B 2 417 ? -7.809 10.659 28.380 1.00 61.22 ? 417 LYS B CA 1 ATOM 10419 C C . LYS B 2 417 ? -7.741 11.424 29.696 1.00 60.70 ? 417 LYS B C 1 ATOM 10420 O O . LYS B 2 417 ? -8.164 12.577 29.769 1.00 63.43 ? 417 LYS B O 1 ATOM 10421 C CB . LYS B 2 417 ? -6.466 10.769 27.653 1.00 63.62 ? 417 LYS B CB 1 ATOM 10422 C CG . LYS B 2 417 ? -6.088 12.187 27.265 1.00 63.38 ? 417 LYS B CG 1 ATOM 10423 C CD . LYS B 2 417 ? -4.582 12.388 27.307 1.00 65.04 ? 417 LYS B CD 1 ATOM 10424 C CE . LYS B 2 417 ? -3.861 11.370 26.440 1.00 90.91 ? 417 LYS B CE 1 ATOM 10425 N NZ . LYS B 2 417 ? -2.383 11.534 26.510 1.00 114.22 ? 417 LYS B NZ 1 ATOM 10426 N N . PRO B 2 418 ? -7.213 10.776 30.745 1.00 61.09 ? 418 PRO B N 1 ATOM 10427 C CA . PRO B 2 418 ? -6.909 11.490 31.988 1.00 64.44 ? 418 PRO B CA 1 ATOM 10428 C C . PRO B 2 418 ? -5.718 12.428 31.795 1.00 72.33 ? 418 PRO B C 1 ATOM 10429 O O . PRO B 2 418 ? -4.776 12.081 31.081 1.00 73.43 ? 418 PRO B O 1 ATOM 10430 C CB . PRO B 2 418 ? -6.580 10.364 32.972 1.00 61.32 ? 418 PRO B CB 1 ATOM 10431 C CG . PRO B 2 418 ? -6.117 9.239 32.110 1.00 61.45 ? 418 PRO B CG 1 ATOM 10432 C CD . PRO B 2 418 ? -6.930 9.334 30.852 1.00 60.70 ? 418 PRO B CD 1 ATOM 10433 N N . VAL B 2 419 ? -5.764 13.599 32.421 1.00 70.16 ? 419 VAL B N 1 ATOM 10434 C CA . VAL B 2 419 ? -4.719 14.600 32.237 1.00 70.78 ? 419 VAL B CA 1 ATOM 10435 C C . VAL B 2 419 ? -3.404 14.167 32.878 1.00 74.47 ? 419 VAL B C 1 ATOM 10436 O O . VAL B 2 419 ? -3.355 13.852 34.067 1.00 74.47 ? 419 VAL B O 1 ATOM 10437 C CB . VAL B 2 419 ? -5.139 15.962 32.822 1.00 73.82 ? 419 VAL B CB 1 ATOM 10438 C CG1 . VAL B 2 419 ? -4.040 16.993 32.615 1.00 85.73 ? 419 VAL B CG1 1 ATOM 10439 C CG2 . VAL B 2 419 ? -6.441 16.431 32.192 1.00 70.26 ? 419 VAL B CG2 1 ATOM 10440 N N . GLY B 2 420 ? -2.340 14.154 32.082 1.00 87.40 ? 420 GLY B N 1 ATOM 10441 C CA . GLY B 2 420 ? -1.019 13.815 32.580 1.00 97.13 ? 420 GLY B CA 1 ATOM 10442 C C . GLY B 2 420 ? -0.666 12.348 32.428 1.00 96.77 ? 420 GLY B C 1 ATOM 10443 O O . GLY B 2 420 ? 0.267 11.861 33.065 1.00 98.35 ? 420 GLY B O 1 ATOM 10444 N N . PHE B 2 421 ? -1.410 11.643 31.582 1.00 94.83 ? 421 PHE B N 1 ATOM 10445 C CA . PHE B 2 421 ? -1.164 10.224 31.346 1.00 89.83 ? 421 PHE B CA 1 ATOM 10446 C C . PHE B 2 421 ? -1.203 9.879 29.862 1.00 82.46 ? 421 PHE B C 1 ATOM 10447 O O . PHE B 2 421 ? -1.915 10.513 29.084 1.00 92.01 ? 421 PHE B O 1 ATOM 10448 C CB . PHE B 2 421 ? -2.181 9.371 32.104 1.00 89.36 ? 421 PHE B CB 1 ATOM 10449 C CG . PHE B 2 421 ? -1.833 9.157 33.548 1.00 87.60 ? 421 PHE B CG 1 ATOM 10450 C CD1 . PHE B 2 421 ? -0.516 8.973 33.937 1.00 84.88 ? 421 PHE B CD1 1 ATOM 10451 C CD2 . PHE B 2 421 ? -2.821 9.143 34.516 1.00 81.09 ? 421 PHE B CD2 1 ATOM 10452 C CE1 . PHE B 2 421 ? -0.193 8.777 35.266 1.00 81.05 ? 421 PHE B CE1 1 ATOM 10453 C CE2 . PHE B 2 421 ? -2.504 8.948 35.845 1.00 87.21 ? 421 PHE B CE2 1 ATOM 10454 C CZ . PHE B 2 421 ? -1.188 8.764 36.220 1.00 88.21 ? 421 PHE B CZ 1 ATOM 10455 N N . LYS B 2 422 ? -0.430 8.868 29.479 1.00 76.65 ? 422 LYS B N 1 ATOM 10456 C CA . LYS B 2 422 ? -0.373 8.429 28.091 1.00 78.54 ? 422 LYS B CA 1 ATOM 10457 C C . LYS B 2 422 ? -1.587 7.578 27.732 1.00 89.74 ? 422 LYS B C 1 ATOM 10458 O O . LYS B 2 422 ? -2.122 7.683 26.627 1.00 95.38 ? 422 LYS B O 1 ATOM 10459 C CB . LYS B 2 422 ? 0.915 7.646 27.830 1.00 87.75 ? 422 LYS B CB 1 ATOM 10460 C CG . LYS B 2 422 ? 1.137 7.286 26.371 1.00 97.57 ? 422 LYS B CG 1 ATOM 10461 C CD . LYS B 2 422 ? 2.428 6.506 26.184 1.00 104.48 ? 422 LYS B CD 1 ATOM 10462 C CE . LYS B 2 422 ? 2.688 6.214 24.716 1.00 105.97 ? 422 LYS B CE 1 ATOM 10463 N NZ . LYS B 2 422 ? 2.830 7.464 23.919 1.00 96.12 ? 422 LYS B NZ 1 ATOM 10464 N N . ASP B 2 423 ? -2.012 6.736 28.671 1.00 97.59 ? 423 ASP B N 1 ATOM 10465 C CA . ASP B 2 423 ? -3.155 5.849 28.465 1.00 93.30 ? 423 ASP B CA 1 ATOM 10466 C C . ASP B 2 423 ? -4.414 6.641 28.127 1.00 85.33 ? 423 ASP B C 1 ATOM 10467 O O . ASP B 2 423 ? -4.757 7.602 28.815 1.00 74.34 ? 423 ASP B O 1 ATOM 10468 C CB . ASP B 2 423 ? -3.391 4.984 29.704 1.00 92.67 ? 423 ASP B CB 1 ATOM 10469 C CG . ASP B 2 423 ? -2.219 4.071 30.007 1.00 98.47 ? 423 ASP B CG 1 ATOM 10470 O OD1 . ASP B 2 423 ? -2.168 2.960 29.437 1.00 96.76 ? 423 ASP B OD1 1 ATOM 10471 O OD2 . ASP B 2 423 ? -1.350 4.462 30.814 1.00 101.45 ? 423 ASP B OD2 1 ATOM 10472 N N . SER B 2 424 ? -5.101 6.229 27.067 1.00 91.75 ? 424 SER B N 1 ATOM 10473 C CA . SER B 2 424 ? -6.201 7.022 26.533 1.00 94.08 ? 424 SER B CA 1 ATOM 10474 C C . SER B 2 424 ? -7.316 6.187 25.910 1.00 80.49 ? 424 SER B C 1 ATOM 10475 O O . SER B 2 424 ? -7.124 5.018 25.572 1.00 66.03 ? 424 SER B O 1 ATOM 10476 C CB . SER B 2 424 ? -5.664 8.008 25.494 1.00 98.76 ? 424 SER B CB 1 ATOM 10477 O OG . SER B 2 424 ? -4.927 7.336 24.487 1.00 91.78 ? 424 SER B OG 1 ATOM 10478 N N . LEU B 2 425 ? -8.482 6.808 25.762 1.00 74.80 ? 425 LEU B N 1 ATOM 10479 C CA . LEU B 2 425 ? -9.624 6.182 25.107 1.00 66.77 ? 425 LEU B CA 1 ATOM 10480 C C . LEU B 2 425 ? -9.878 6.826 23.747 1.00 81.22 ? 425 LEU B C 1 ATOM 10481 O O . LEU B 2 425 ? -10.282 7.986 23.667 1.00 101.53 ? 425 LEU B O 1 ATOM 10482 C CB . LEU B 2 425 ? -10.875 6.291 25.981 1.00 64.90 ? 425 LEU B CB 1 ATOM 10483 C CG . LEU B 2 425 ? -12.194 5.817 25.364 1.00 62.28 ? 425 LEU B CG 1 ATOM 10484 C CD1 . LEU B 2 425 ? -12.245 4.302 25.277 1.00 58.89 ? 425 LEU B CD1 1 ATOM 10485 C CD2 . LEU B 2 425 ? -13.381 6.351 26.149 1.00 69.39 ? 425 LEU B CD2 1 ATOM 10486 N N . ILE B 2 426 ? -9.639 6.069 22.681 1.00 80.86 ? 426 ILE B N 1 ATOM 10487 C CA . ILE B 2 426 ? -9.841 6.569 21.325 1.00 84.61 ? 426 ILE B CA 1 ATOM 10488 C C . ILE B 2 426 ? -11.220 6.171 20.808 1.00 82.56 ? 426 ILE B C 1 ATOM 10489 O O . ILE B 2 426 ? -11.594 5.000 20.856 1.00 89.77 ? 426 ILE B O 1 ATOM 10490 C CB . ILE B 2 426 ? -8.760 6.046 20.352 1.00 69.55 ? 426 ILE B CB 1 ATOM 10491 C CG1 . ILE B 2 426 ? -7.367 6.521 20.775 1.00 70.21 ? 426 ILE B CG1 1 ATOM 10492 C CG2 . ILE B 2 426 ? -9.057 6.496 18.930 1.00 73.37 ? 426 ILE B CG2 1 ATOM 10493 C CD1 . ILE B 2 426 ? -6.640 5.574 21.712 1.00 69.32 ? 426 ILE B CD1 1 ATOM 10494 N N . VAL B 2 427 ? -11.975 7.148 20.316 1.00 72.83 ? 427 VAL B N 1 ATOM 10495 C CA . VAL B 2 427 ? -13.318 6.886 19.814 1.00 67.93 ? 427 VAL B CA 1 ATOM 10496 C C . VAL B 2 427 ? -13.443 7.194 18.326 1.00 79.71 ? 427 VAL B C 1 ATOM 10497 O O . VAL B 2 427 ? -13.322 8.346 17.907 1.00 97.60 ? 427 VAL B O 1 ATOM 10498 C CB . VAL B 2 427 ? -14.374 7.702 20.580 1.00 65.55 ? 427 VAL B CB 1 ATOM 10499 C CG1 . VAL B 2 427 ? -15.757 7.451 19.999 1.00 65.87 ? 427 VAL B CG1 1 ATOM 10500 C CG2 . VAL B 2 427 ? -14.340 7.355 22.059 1.00 66.69 ? 427 VAL B CG2 1 ATOM 10501 N N . GLN B 2 428 ? -13.684 6.154 17.534 1.00 79.34 ? 428 GLN B N 1 ATOM 10502 C CA . GLN B 2 428 ? -13.896 6.305 16.099 1.00 77.59 ? 428 GLN B CA 1 ATOM 10503 C C . GLN B 2 428 ? -15.343 6.694 15.825 1.00 78.85 ? 428 GLN B C 1 ATOM 10504 O O . GLN B 2 428 ? -16.268 6.004 16.253 1.00 94.87 ? 428 GLN B O 1 ATOM 10505 C CB . GLN B 2 428 ? -13.544 5.011 15.365 1.00 83.69 ? 428 GLN B CB 1 ATOM 10506 C CG . GLN B 2 428 ? -12.155 4.480 15.678 1.00 93.73 ? 428 GLN B CG 1 ATOM 10507 C CD . GLN B 2 428 ? -11.927 3.084 15.130 1.00 102.48 ? 428 GLN B CD 1 ATOM 10508 O OE1 . GLN B 2 428 ? -10.914 2.448 15.424 1.00 91.58 ? 428 GLN B OE1 1 ATOM 10509 N NE2 . GLN B 2 428 ? -12.871 2.600 14.332 1.00 113.77 ? 428 GLN B NE2 1 ATOM 10510 N N . VAL B 2 429 ? -15.539 7.797 15.111 1.00 81.49 ? 429 VAL B N 1 ATOM 10511 C CA . VAL B 2 429 ? -16.883 8.312 14.877 1.00 83.92 ? 429 VAL B CA 1 ATOM 10512 C C . VAL B 2 429 ? -17.333 8.128 13.432 1.00 90.37 ? 429 VAL B C 1 ATOM 10513 O O . VAL B 2 429 ? -16.688 8.609 12.501 1.00 97.18 ? 429 VAL B O 1 ATOM 10514 C CB . VAL B 2 429 ? -16.978 9.802 15.234 1.00 94.17 ? 429 VAL B CB 1 ATOM 10515 C CG1 . VAL B 2 429 ? -18.432 10.235 15.287 1.00 95.32 ? 429 VAL B CG1 1 ATOM 10516 C CG2 . VAL B 2 429 ? -16.298 10.066 16.562 1.00 106.35 ? 429 VAL B CG2 1 ATOM 10517 N N . THR B 2 430 ? -18.449 7.428 13.258 1.00 90.35 ? 430 THR B N 1 ATOM 10518 C CA . THR B 2 430 ? -19.034 7.221 11.940 1.00 97.99 ? 430 THR B CA 1 ATOM 10519 C C . THR B 2 430 ? -20.513 7.586 11.978 1.00 98.39 ? 430 THR B C 1 ATOM 10520 O O . THR B 2 430 ? -21.211 7.270 12.941 1.00 94.11 ? 430 THR B O 1 ATOM 10521 C CB . THR B 2 430 ? -18.869 5.764 11.465 1.00 104.20 ? 430 THR B CB 1 ATOM 10522 O OG1 . THR B 2 430 ? -17.502 5.361 11.615 1.00 106.76 ? 430 THR B OG1 1 ATOM 10523 C CG2 . THR B 2 430 ? -19.277 5.624 10.005 1.00 113.65 ? 430 THR B CG2 1 ATOM 10524 N N . PHE B 2 431 ? -20.989 8.256 10.935 1.00 104.03 ? 431 PHE B N 1 ATOM 10525 C CA . PHE B 2 431 ? -22.380 8.688 10.890 1.00 103.92 ? 431 PHE B CA 1 ATOM 10526 C C . PHE B 2 431 ? -23.184 7.949 9.826 1.00 112.15 ? 431 PHE B C 1 ATOM 10527 O O . PHE B 2 431 ? -22.769 7.853 8.671 1.00 126.83 ? 431 PHE B O 1 ATOM 10528 C CB . PHE B 2 431 ? -22.460 10.195 10.640 1.00 102.91 ? 431 PHE B CB 1 ATOM 10529 C CG . PHE B 2 431 ? -21.743 11.019 11.669 1.00 96.68 ? 431 PHE B CG 1 ATOM 10530 C CD1 . PHE B 2 431 ? -20.545 11.643 11.364 1.00 100.84 ? 431 PHE B CD1 1 ATOM 10531 C CD2 . PHE B 2 431 ? -22.265 11.167 12.943 1.00 91.00 ? 431 PHE B CD2 1 ATOM 10532 C CE1 . PHE B 2 431 ? -19.884 12.404 12.309 1.00 100.98 ? 431 PHE B CE1 1 ATOM 10533 C CE2 . PHE B 2 431 ? -21.607 11.924 13.892 1.00 87.53 ? 431 PHE B CE2 1 ATOM 10534 C CZ . PHE B 2 431 ? -20.416 12.545 13.574 1.00 92.24 ? 431 PHE B CZ 1 ATOM 10535 N N . ASP B 2 432 ? -24.338 7.425 10.228 1.00 107.71 ? 432 ASP B N 1 ATOM 10536 C CA . ASP B 2 432 ? -25.280 6.840 9.284 1.00 114.22 ? 432 ASP B CA 1 ATOM 10537 C C . ASP B 2 432 ? -26.315 7.885 8.890 1.00 116.56 ? 432 ASP B C 1 ATOM 10538 O O . ASP B 2 432 ? -27.129 8.300 9.711 1.00 111.34 ? 432 ASP B O 1 ATOM 10539 C CB . ASP B 2 432 ? -25.964 5.609 9.882 1.00 114.99 ? 432 ASP B CB 1 ATOM 10540 C CG . ASP B 2 432 ? -25.049 4.403 9.940 1.00 120.18 ? 432 ASP B CG 1 ATOM 10541 O OD1 . ASP B 2 432 ? -24.315 4.257 10.941 1.00 120.40 ? 432 ASP B OD1 1 ATOM 10542 O OD2 . ASP B 2 432 ? -25.065 3.598 8.985 1.00 120.89 ? 432 ASP B OD2 1 ATOM 10543 N N . CYS B 2 433 ? -26.276 8.307 7.631 1.00 126.22 ? 433 CYS B N 1 ATOM 10544 C CA . CYS B 2 433 ? -27.170 9.353 7.150 1.00 131.95 ? 433 CYS B CA 1 ATOM 10545 C C . CYS B 2 433 ? -27.954 8.894 5.926 1.00 138.63 ? 433 CYS B C 1 ATOM 10546 O O . CYS B 2 433 ? -29.179 8.801 5.963 1.00 143.34 ? 433 CYS B O 1 ATOM 10547 C CB . CYS B 2 433 ? -26.381 10.622 6.825 1.00 136.43 ? 433 CYS B CB 1 ATOM 10548 S SG . CYS B 2 433 ? -25.552 11.367 8.248 1.00 185.13 ? 433 CYS B SG 1 ATOM 10549 N N . ASP B 2 434 ? -27.240 8.620 4.840 1.00 147.48 ? 434 ASP B N 1 ATOM 10550 C CA . ASP B 2 434 ? -27.868 8.175 3.602 1.00 157.39 ? 434 ASP B CA 1 ATOM 10551 C C . ASP B 2 434 ? -28.356 6.734 3.704 1.00 154.47 ? 434 ASP B C 1 ATOM 10552 O O . ASP B 2 434 ? -27.751 5.911 4.391 1.00 147.69 ? 434 ASP B O 1 ATOM 10553 C CB . ASP B 2 434 ? -26.892 8.315 2.432 1.00 165.60 ? 434 ASP B CB 1 ATOM 10554 C CG . ASP B 2 434 ? -26.470 9.750 2.195 1.00 165.47 ? 434 ASP B CG 1 ATOM 10555 O OD1 . ASP B 2 434 ? -26.552 10.558 3.144 1.00 157.83 ? 434 ASP B OD1 1 ATOM 10556 O OD2 . ASP B 2 434 ? -26.054 10.071 1.062 1.00 170.83 ? 434 ASP B OD2 1 ATOM 10557 N N . CYS B 2 435 ? -29.456 6.436 3.019 1.00 160.37 ? 435 CYS B N 1 ATOM 10558 C CA . CYS B 2 435 ? -29.993 5.081 2.984 1.00 165.13 ? 435 CYS B CA 1 ATOM 10559 C C . CYS B 2 435 ? -29.123 4.179 2.115 1.00 170.98 ? 435 CYS B C 1 ATOM 10560 O O . CYS B 2 435 ? -28.386 4.657 1.253 1.00 171.73 ? 435 CYS B O 1 ATOM 10561 C CB . CYS B 2 435 ? -31.433 5.082 2.465 1.00 170.22 ? 435 CYS B CB 1 ATOM 10562 S SG . CYS B 2 435 ? -32.625 5.906 3.547 1.00 143.81 ? 435 CYS B SG 1 ATOM 10563 N N . ALA B 2 436 ? -29.214 2.874 2.347 1.00 172.22 ? 436 ALA B N 1 ATOM 10564 C CA . ALA B 2 436 ? -28.422 1.908 1.596 1.00 171.04 ? 436 ALA B CA 1 ATOM 10565 C C . ALA B 2 436 ? -28.934 1.757 0.167 1.00 175.36 ? 436 ALA B C 1 ATOM 10566 O O . ALA B 2 436 ? -28.163 1.482 -0.752 1.00 180.41 ? 436 ALA B O 1 ATOM 10567 C CB . ALA B 2 436 ? -28.424 0.561 2.303 1.00 166.20 ? 436 ALA B CB 1 ATOM 10568 N N . CYS B 2 437 ? -30.238 1.942 -0.015 1.00 173.36 ? 437 CYS B N 1 ATOM 10569 C CA . CYS B 2 437 ? -30.858 1.781 -1.326 1.00 178.04 ? 437 CYS B CA 1 ATOM 10570 C C . CYS B 2 437 ? -30.743 3.047 -2.170 1.00 175.11 ? 437 CYS B C 1 ATOM 10571 O O . CYS B 2 437 ? -31.156 3.068 -3.330 1.00 187.16 ? 437 CYS B O 1 ATOM 10572 C CB . CYS B 2 437 ? -32.329 1.386 -1.174 1.00 183.09 ? 437 CYS B CB 1 ATOM 10573 S SG . CYS B 2 437 ? -33.334 2.571 -0.249 1.00 154.86 ? 437 CYS B SG 1 ATOM 10574 N N . GLN B 2 438 ? -30.177 4.097 -1.585 1.00 163.43 ? 438 GLN B N 1 ATOM 10575 C CA . GLN B 2 438 ? -30.021 5.370 -2.279 1.00 165.03 ? 438 GLN B CA 1 ATOM 10576 C C . GLN B 2 438 ? -28.987 5.269 -3.397 1.00 172.24 ? 438 GLN B C 1 ATOM 10577 O O . GLN B 2 438 ? -29.097 5.942 -4.422 1.00 179.75 ? 438 GLN B O 1 ATOM 10578 C CB . GLN B 2 438 ? -29.627 6.469 -1.289 1.00 164.40 ? 438 GLN B CB 1 ATOM 10579 C CG . GLN B 2 438 ? -29.534 7.860 -1.896 1.00 171.03 ? 438 GLN B CG 1 ATOM 10580 C CD . GLN B 2 438 ? -29.266 8.932 -0.857 1.00 166.44 ? 438 GLN B CD 1 ATOM 10581 O OE1 . GLN B 2 438 ? -29.350 8.681 0.345 1.00 155.13 ? 438 GLN B OE1 1 ATOM 10582 N NE2 . GLN B 2 438 ? -28.940 10.134 -1.317 1.00 171.74 ? 438 GLN B NE2 1 ATOM 10583 N N . ALA B 2 439 ? -27.986 4.418 -3.197 1.00 176.18 ? 439 ALA B N 1 ATOM 10584 C CA . ALA B 2 439 ? -26.928 4.232 -4.183 1.00 183.96 ? 439 ALA B CA 1 ATOM 10585 C C . ALA B 2 439 ? -27.409 3.398 -5.368 1.00 188.12 ? 439 ALA B C 1 ATOM 10586 O O . ALA B 2 439 ? -26.822 3.443 -6.449 1.00 195.99 ? 439 ALA B O 1 ATOM 10587 C CB . ALA B 2 439 ? -25.713 3.582 -3.539 1.00 186.23 ? 439 ALA B CB 1 ATOM 10588 N N . GLN B 2 440 ? -28.481 2.640 -5.158 1.00 190.39 ? 440 GLN B N 1 ATOM 10589 C CA . GLN B 2 440 ? -29.029 1.774 -6.198 1.00 191.42 ? 440 GLN B CA 1 ATOM 10590 C C . GLN B 2 440 ? -29.744 2.569 -7.287 1.00 194.63 ? 440 GLN B C 1 ATOM 10591 O O . GLN B 2 440 ? -30.040 2.039 -8.358 1.00 203.10 ? 440 GLN B O 1 ATOM 10592 C CB . GLN B 2 440 ? -29.992 0.753 -5.589 1.00 184.80 ? 440 GLN B CB 1 ATOM 10593 C CG . GLN B 2 440 ? -29.343 -0.223 -4.623 1.00 180.38 ? 440 GLN B CG 1 ATOM 10594 C CD . GLN B 2 440 ? -30.330 -1.232 -4.069 1.00 180.46 ? 440 GLN B CD 1 ATOM 10595 O OE1 . GLN B 2 440 ? -31.541 -1.095 -4.246 1.00 179.66 ? 440 GLN B OE1 1 ATOM 10596 N NE2 . GLN B 2 440 ? -29.816 -2.256 -3.398 1.00 182.29 ? 440 GLN B NE2 1 ATOM 10597 N N . ALA B 2 441 ? -30.021 3.838 -7.006 1.00 189.24 ? 441 ALA B N 1 ATOM 10598 C CA . ALA B 2 441 ? -30.739 4.694 -7.942 1.00 194.60 ? 441 ALA B CA 1 ATOM 10599 C C . ALA B 2 441 ? -29.921 4.970 -9.201 1.00 208.81 ? 441 ALA B C 1 ATOM 10600 O O . ALA B 2 441 ? -28.752 5.347 -9.123 1.00 208.17 ? 441 ALA B O 1 ATOM 10601 C CB . ALA B 2 441 ? -31.125 6.001 -7.267 1.00 184.91 ? 441 ALA B CB 1 ATOM 10602 N N . GLU B 2 442 ? -30.545 4.778 -10.360 1.00 221.19 ? 442 GLU B N 1 ATOM 10603 C CA . GLU B 2 442 ? -29.898 5.059 -11.638 1.00 229.37 ? 442 GLU B CA 1 ATOM 10604 C C . GLU B 2 442 ? -30.247 6.474 -12.087 1.00 235.16 ? 442 GLU B C 1 ATOM 10605 O O . GLU B 2 442 ? -31.360 6.723 -12.546 1.00 234.36 ? 442 GLU B O 1 ATOM 10606 C CB . GLU B 2 442 ? -30.319 4.033 -12.690 1.00 226.92 ? 442 GLU B CB 1 ATOM 10607 C CG . GLU B 2 442 ? -30.028 2.595 -12.287 1.00 222.47 ? 442 GLU B CG 1 ATOM 10608 C CD . GLU B 2 442 ? -30.601 1.587 -13.261 1.00 228.71 ? 442 GLU B CD 1 ATOM 10609 O OE1 . GLU B 2 442 ? -31.255 2.007 -14.238 1.00 232.79 ? 442 GLU B OE1 1 ATOM 10610 O OE2 . GLU B 2 442 ? -30.400 0.373 -13.047 1.00 232.30 ? 442 GLU B OE2 1 ATOM 10611 N N . PRO B 2 443 ? -29.266 7.387 -12.003 1.00 238.34 ? 443 PRO B N 1 ATOM 10612 C CA . PRO B 2 443 ? -29.397 8.852 -11.974 1.00 234.69 ? 443 PRO B CA 1 ATOM 10613 C C . PRO B 2 443 ? -30.256 9.503 -13.063 1.00 238.51 ? 443 PRO B C 1 ATOM 10614 O O . PRO B 2 443 ? -30.791 10.584 -12.814 1.00 239.29 ? 443 PRO B O 1 ATOM 10615 C CB . PRO B 2 443 ? -27.943 9.331 -12.109 1.00 232.15 ? 443 PRO B CB 1 ATOM 10616 C CG . PRO B 2 443 ? -27.190 8.164 -12.653 1.00 238.22 ? 443 PRO B CG 1 ATOM 10617 C CD . PRO B 2 443 ? -27.855 6.974 -12.054 1.00 240.02 ? 443 PRO B CD 1 ATOM 10618 N N . ASN B 2 444 ? -30.394 8.883 -14.230 1.00 239.28 ? 444 ASN B N 1 ATOM 10619 C CA . ASN B 2 444 ? -30.988 9.585 -15.366 1.00 235.05 ? 444 ASN B CA 1 ATOM 10620 C C . ASN B 2 444 ? -32.508 9.769 -15.287 1.00 225.97 ? 444 ASN B C 1 ATOM 10621 O O . ASN B 2 444 ? -33.168 9.271 -14.375 1.00 217.06 ? 444 ASN B O 1 ATOM 10622 C CB . ASN B 2 444 ? -30.631 8.856 -16.665 1.00 242.71 ? 444 ASN B CB 1 ATOM 10623 C CG . ASN B 2 444 ? -30.559 9.791 -17.858 1.00 248.45 ? 444 ASN B CG 1 ATOM 10624 O OD1 . ASN B 2 444 ? -31.547 9.993 -18.564 1.00 253.36 ? 444 ASN B OD1 1 ATOM 10625 N ND2 . ASN B 2 444 ? -29.386 10.370 -18.085 1.00 249.10 ? 444 ASN B ND2 1 ATOM 10626 N N . SER B 2 445 ? -33.040 10.492 -16.269 1.00 231.69 ? 445 SER B N 1 ATOM 10627 C CA . SER B 2 445 ? -34.464 10.806 -16.384 1.00 232.15 ? 445 SER B CA 1 ATOM 10628 C C . SER B 2 445 ? -35.302 9.624 -16.865 1.00 236.35 ? 445 SER B C 1 ATOM 10629 O O . SER B 2 445 ? -34.754 8.618 -17.320 1.00 245.90 ? 445 SER B O 1 ATOM 10630 C CB . SER B 2 445 ? -34.665 11.998 -17.323 1.00 235.08 ? 445 SER B CB 1 ATOM 10631 O OG . SER B 2 445 ? -34.051 13.165 -16.803 1.00 229.96 ? 445 SER B OG 1 ATOM 10632 N N . HIS B 2 446 ? -36.621 9.747 -16.692 1.00 227.57 ? 446 HIS B N 1 ATOM 10633 C CA . HIS B 2 446 ? -37.633 8.825 -17.231 1.00 224.08 ? 446 HIS B CA 1 ATOM 10634 C C . HIS B 2 446 ? -37.831 7.596 -16.353 1.00 219.87 ? 446 HIS B C 1 ATOM 10635 O O . HIS B 2 446 ? -38.664 6.739 -16.652 1.00 221.38 ? 446 HIS B O 1 ATOM 10636 C CB . HIS B 2 446 ? -37.294 8.388 -18.664 1.00 227.50 ? 446 HIS B CB 1 ATOM 10637 C CG . HIS B 2 446 ? -37.392 9.488 -19.674 1.00 229.68 ? 446 HIS B CG 1 ATOM 10638 N ND1 . HIS B 2 446 ? -38.341 9.497 -20.674 1.00 234.03 ? 446 HIS B ND1 1 ATOM 10639 C CD2 . HIS B 2 446 ? -36.662 10.617 -19.838 1.00 227.94 ? 446 HIS B CD2 1 ATOM 10640 C CE1 . HIS B 2 446 ? -38.190 10.583 -21.411 1.00 233.28 ? 446 HIS B CE1 1 ATOM 10641 N NE2 . HIS B 2 446 ? -37.179 11.279 -20.925 1.00 230.81 ? 446 HIS B NE2 1 ATOM 10642 N N . ARG B 2 447 ? -37.061 7.509 -15.275 1.00 214.24 ? 447 ARG B N 1 ATOM 10643 C CA . ARG B 2 447 ? -37.136 6.368 -14.370 1.00 207.52 ? 447 ARG B CA 1 ATOM 10644 C C . ARG B 2 447 ? -38.510 6.232 -13.708 1.00 205.46 ? 447 ARG B C 1 ATOM 10645 O O . ARG B 2 447 ? -38.915 5.129 -13.338 1.00 205.52 ? 447 ARG B O 1 ATOM 10646 C CB . ARG B 2 447 ? -36.049 6.473 -13.297 1.00 196.06 ? 447 ARG B CB 1 ATOM 10647 C CG . ARG B 2 447 ? -35.907 5.230 -12.432 1.00 193.83 ? 447 ARG B CG 1 ATOM 10648 C CD . ARG B 2 447 ? -35.582 4.009 -13.279 1.00 199.30 ? 447 ARG B CD 1 ATOM 10649 N NE . ARG B 2 447 ? -35.614 2.775 -12.500 1.00 198.25 ? 447 ARG B NE 1 ATOM 10650 C CZ . ARG B 2 447 ? -36.671 1.973 -12.415 1.00 198.29 ? 447 ARG B CZ 1 ATOM 10651 N NH1 . ARG B 2 447 ? -37.788 2.273 -13.064 1.00 199.22 ? 447 ARG B NH1 1 ATOM 10652 N NH2 . ARG B 2 447 ? -36.611 0.870 -11.682 1.00 198.46 ? 447 ARG B NH2 1 ATOM 10653 N N . CYS B 2 448 ? -39.233 7.340 -13.567 1.00 203.82 ? 448 CYS B N 1 ATOM 10654 C CA . CYS B 2 448 ? -40.510 7.298 -12.860 1.00 204.83 ? 448 CYS B CA 1 ATOM 10655 C C . CYS B 2 448 ? -41.732 7.362 -13.778 1.00 211.30 ? 448 CYS B C 1 ATOM 10656 O O . CYS B 2 448 ? -42.344 6.333 -14.064 1.00 212.49 ? 448 CYS B O 1 ATOM 10657 C CB . CYS B 2 448 ? -40.580 8.444 -11.847 1.00 199.43 ? 448 CYS B CB 1 ATOM 10658 S SG . CYS B 2 448 ? -42.186 8.628 -11.039 1.00 215.80 ? 448 CYS B SG 1 ATOM 10659 N N . ASN B 2 449 ? -42.077 8.558 -14.250 1.00 216.27 ? 449 ASN B N 1 ATOM 10660 C CA . ASN B 2 449 ? -43.251 8.726 -15.108 1.00 222.63 ? 449 ASN B CA 1 ATOM 10661 C C . ASN B 2 449 ? -43.139 9.893 -16.085 1.00 223.57 ? 449 ASN B C 1 ATOM 10662 O O . ASN B 2 449 ? -42.631 10.959 -15.735 1.00 217.58 ? 449 ASN B O 1 ATOM 10663 C CB . ASN B 2 449 ? -44.510 8.911 -14.253 1.00 222.08 ? 449 ASN B CB 1 ATOM 10664 C CG . ASN B 2 449 ? -44.990 7.616 -13.627 1.00 223.12 ? 449 ASN B CG 1 ATOM 10665 O OD1 . ASN B 2 449 ? -45.765 6.872 -14.228 1.00 228.06 ? 449 ASN B OD1 1 ATOM 10666 N ND2 . ASN B 2 449 ? -44.533 7.341 -12.411 1.00 216.55 ? 449 ASN B ND2 1 ATOM 10667 N N . ASN B 2 450 ? -43.623 9.676 -17.307 1.00 238.20 ? 450 ASN B N 1 ATOM 10668 C CA . ASN B 2 450 ? -43.743 10.718 -18.330 1.00 246.08 ? 450 ASN B CA 1 ATOM 10669 C C . ASN B 2 450 ? -42.413 11.410 -18.624 1.00 243.87 ? 450 ASN B C 1 ATOM 10670 O O . ASN B 2 450 ? -42.380 12.533 -19.129 1.00 246.41 ? 450 ASN B O 1 ATOM 10671 C CB . ASN B 2 450 ? -44.793 11.753 -17.908 1.00 243.88 ? 450 ASN B CB 1 ATOM 10672 C CG . ASN B 2 450 ? -45.322 12.565 -19.079 1.00 240.22 ? 450 ASN B CG 1 ATOM 10673 O OD1 . ASN B 2 450 ? -44.913 13.707 -19.294 1.00 236.07 ? 450 ASN B OD1 1 ATOM 10674 N ND2 . ASN B 2 450 ? -46.237 11.978 -19.841 1.00 241.41 ? 450 ASN B ND2 1 ATOM 10675 N N . GLY B 2 451 ? -41.314 10.732 -18.310 1.00 238.57 ? 451 GLY B N 1 ATOM 10676 C CA . GLY B 2 451 ? -39.994 11.315 -18.452 1.00 233.66 ? 451 GLY B CA 1 ATOM 10677 C C . GLY B 2 451 ? -39.790 12.491 -17.516 1.00 220.09 ? 451 GLY B C 1 ATOM 10678 O O . GLY B 2 451 ? -40.692 12.849 -16.758 1.00 210.12 ? 451 GLY B O 1 ATOM 10679 N N . ASN B 2 452 ? -38.603 13.091 -17.580 1.00 217.64 ? 452 ASN B N 1 ATOM 10680 C CA . ASN B 2 452 ? -38.287 14.325 -16.858 1.00 206.77 ? 452 ASN B CA 1 ATOM 10681 C C . ASN B 2 452 ? -38.768 14.347 -15.408 1.00 198.50 ? 452 ASN B C 1 ATOM 10682 O O . ASN B 2 452 ? -39.644 15.136 -15.054 1.00 195.11 ? 452 ASN B O 1 ATOM 10683 C CB . ASN B 2 452 ? -38.881 15.521 -17.604 1.00 205.36 ? 452 ASN B CB 1 ATOM 10684 C CG . ASN B 2 452 ? -38.796 15.370 -19.110 1.00 209.50 ? 452 ASN B CG 1 ATOM 10685 O OD1 . ASN B 2 452 ? -39.814 15.364 -19.803 1.00 208.27 ? 452 ASN B OD1 1 ATOM 10686 N ND2 . ASN B 2 452 ? -37.579 15.245 -19.625 1.00 213.92 ? 452 ASN B ND2 1 ATOM 10687 N N . GLY B 2 453 ? -38.200 13.484 -14.573 1.00 197.01 ? 453 GLY B N 1 ATOM 10688 C CA . GLY B 2 453 ? -38.629 13.393 -13.189 1.00 192.58 ? 453 GLY B CA 1 ATOM 10689 C C . GLY B 2 453 ? -37.561 12.879 -12.245 1.00 191.45 ? 453 GLY B C 1 ATOM 10690 O O . GLY B 2 453 ? -36.444 12.572 -12.662 1.00 190.36 ? 453 GLY B O 1 ATOM 10691 N N . THR B 2 454 ? -37.910 12.782 -10.966 1.00 192.84 ? 454 THR B N 1 ATOM 10692 C CA . THR B 2 454 ? -36.977 12.309 -9.951 1.00 193.10 ? 454 THR B CA 1 ATOM 10693 C C . THR B 2 454 ? -37.430 10.958 -9.405 1.00 195.74 ? 454 THR B C 1 ATOM 10694 O O . THR B 2 454 ? -38.444 10.411 -9.843 1.00 195.88 ? 454 THR B O 1 ATOM 10695 C CB . THR B 2 454 ? -36.837 13.317 -8.792 1.00 181.47 ? 454 THR B CB 1 ATOM 10696 O OG1 . THR B 2 454 ? -37.274 14.611 -9.223 1.00 181.98 ? 454 THR B OG1 1 ATOM 10697 C CG2 . THR B 2 454 ? -35.390 13.400 -8.321 1.00 176.02 ? 454 THR B CG2 1 ATOM 10698 N N . PHE B 2 455 ? -36.681 10.439 -8.436 1.00 193.82 ? 455 PHE B N 1 ATOM 10699 C CA . PHE B 2 455 ? -36.832 9.062 -7.980 1.00 194.49 ? 455 PHE B CA 1 ATOM 10700 C C . PHE B 2 455 ? -35.878 8.772 -6.829 1.00 198.15 ? 455 PHE B C 1 ATOM 10701 O O . PHE B 2 455 ? -34.926 9.519 -6.599 1.00 206.42 ? 455 PHE B O 1 ATOM 10702 C CB . PHE B 2 455 ? -36.550 8.090 -9.126 1.00 199.06 ? 455 PHE B CB 1 ATOM 10703 C CG . PHE B 2 455 ? -35.194 8.276 -9.737 1.00 201.63 ? 455 PHE B CG 1 ATOM 10704 C CD1 . PHE B 2 455 ? -34.104 7.563 -9.268 1.00 197.69 ? 455 PHE B CD1 1 ATOM 10705 C CD2 . PHE B 2 455 ? -35.002 9.189 -10.759 1.00 209.27 ? 455 PHE B CD2 1 ATOM 10706 C CE1 . PHE B 2 455 ? -32.856 7.748 -9.818 1.00 200.78 ? 455 PHE B CE1 1 ATOM 10707 C CE2 . PHE B 2 455 ? -33.757 9.378 -11.309 1.00 209.24 ? 455 PHE B CE2 1 ATOM 10708 C CZ . PHE B 2 455 ? -32.685 8.660 -10.836 1.00 203.79 ? 455 PHE B CZ 1 ATOM 10709 N N . GLU B 2 456 ? -36.134 7.678 -6.120 1.00 198.14 ? 456 GLU B N 1 ATOM 10710 C CA . GLU B 2 456 ? -35.230 7.185 -5.087 1.00 197.07 ? 456 GLU B CA 1 ATOM 10711 C C . GLU B 2 456 ? -35.648 5.771 -4.707 1.00 195.31 ? 456 GLU B C 1 ATOM 10712 O O . GLU B 2 456 ? -36.537 5.195 -5.336 1.00 200.02 ? 456 GLU B O 1 ATOM 10713 C CB . GLU B 2 456 ? -35.232 8.100 -3.861 1.00 189.22 ? 456 GLU B CB 1 ATOM 10714 C CG . GLU B 2 456 ? -33.894 8.171 -3.140 1.00 182.60 ? 456 GLU B CG 1 ATOM 10715 C CD . GLU B 2 456 ? -33.916 9.121 -1.961 1.00 182.05 ? 456 GLU B CD 1 ATOM 10716 O OE1 . GLU B 2 456 ? -35.022 9.483 -1.508 1.00 179.59 ? 456 GLU B OE1 1 ATOM 10717 O OE2 . GLU B 2 456 ? -32.827 9.508 -1.489 1.00 188.72 ? 456 GLU B OE2 1 ATOM 10718 N N . CYS B 2 457 ? -35.004 5.205 -3.691 1.00 187.34 ? 457 CYS B N 1 ATOM 10719 C CA . CYS B 2 457 ? -35.400 3.895 -3.197 1.00 189.09 ? 457 CYS B CA 1 ATOM 10720 C C . CYS B 2 457 ? -36.822 3.977 -2.651 1.00 184.46 ? 457 CYS B C 1 ATOM 10721 O O . CYS B 2 457 ? -37.097 4.754 -1.736 1.00 176.68 ? 457 CYS B O 1 ATOM 10722 C CB . CYS B 2 457 ? -34.428 3.413 -2.117 1.00 191.39 ? 457 CYS B CB 1 ATOM 10723 S SG . CYS B 2 457 ? -34.809 1.796 -1.412 1.00 260.72 ? 457 CYS B SG 1 ATOM 10724 N N . GLY B 2 458 ? -37.710 3.156 -3.206 1.00 190.32 ? 458 GLY B N 1 ATOM 10725 C CA . GLY B 2 458 ? -39.122 3.184 -2.862 1.00 190.97 ? 458 GLY B CA 1 ATOM 10726 C C . GLY B 2 458 ? -39.750 4.569 -2.893 1.00 190.59 ? 458 GLY B C 1 ATOM 10727 O O . GLY B 2 458 ? -40.603 4.883 -2.064 1.00 189.65 ? 458 GLY B O 1 ATOM 10728 N N . VAL B 2 459 ? -39.334 5.398 -3.848 1.00 192.64 ? 459 VAL B N 1 ATOM 10729 C CA . VAL B 2 459 ? -39.787 6.787 -3.902 1.00 192.01 ? 459 VAL B CA 1 ATOM 10730 C C . VAL B 2 459 ? -40.024 7.288 -5.325 1.00 196.94 ? 459 VAL B C 1 ATOM 10731 O O . VAL B 2 459 ? -39.209 7.061 -6.221 1.00 197.93 ? 459 VAL B O 1 ATOM 10732 C CB . VAL B 2 459 ? -38.768 7.726 -3.203 1.00 216.29 ? 459 VAL B CB 1 ATOM 10733 C CG1 . VAL B 2 459 ? -38.817 9.138 -3.781 1.00 214.48 ? 459 VAL B CG1 1 ATOM 10734 C CG2 . VAL B 2 459 ? -39.012 7.758 -1.711 1.00 211.10 ? 459 VAL B CG2 1 ATOM 10735 N N . CYS B 2 460 ? -41.152 7.965 -5.524 1.00 200.93 ? 460 CYS B N 1 ATOM 10736 C CA . CYS B 2 460 ? -41.407 8.688 -6.764 1.00 212.11 ? 460 CYS B CA 1 ATOM 10737 C C . CYS B 2 460 ? -41.918 10.096 -6.470 1.00 218.53 ? 460 CYS B C 1 ATOM 10738 O O . CYS B 2 460 ? -43.002 10.269 -5.912 1.00 222.89 ? 460 CYS B O 1 ATOM 10739 C CB . CYS B 2 460 ? -42.412 7.933 -7.634 1.00 216.57 ? 460 CYS B CB 1 ATOM 10740 S SG . CYS B 2 460 ? -42.888 8.810 -9.142 1.00 212.65 ? 460 CYS B SG 1 ATOM 10741 N N . ARG B 2 461 ? -41.131 11.097 -6.848 1.00 217.43 ? 461 ARG B N 1 ATOM 10742 C CA . ARG B 2 461 ? -41.529 12.493 -6.700 1.00 210.92 ? 461 ARG B CA 1 ATOM 10743 C C . ARG B 2 461 ? -41.083 13.290 -7.920 1.00 213.77 ? 461 ARG B C 1 ATOM 10744 O O . ARG B 2 461 ? -39.922 13.226 -8.313 1.00 218.47 ? 461 ARG B O 1 ATOM 10745 C CB . ARG B 2 461 ? -40.940 13.096 -5.422 1.00 200.10 ? 461 ARG B CB 1 ATOM 10746 C CG . ARG B 2 461 ? -41.338 14.545 -5.180 1.00 199.41 ? 461 ARG B CG 1 ATOM 10747 C CD . ARG B 2 461 ? -40.748 15.077 -3.882 1.00 198.32 ? 461 ARG B CD 1 ATOM 10748 N NE . ARG B 2 461 ? -41.139 16.462 -3.632 1.00 199.56 ? 461 ARG B NE 1 ATOM 10749 C CZ . ARG B 2 461 ? -40.763 17.166 -2.570 1.00 196.25 ? 461 ARG B CZ 1 ATOM 10750 N NH1 . ARG B 2 461 ? -39.982 16.617 -1.650 1.00 191.40 ? 461 ARG B NH1 1 ATOM 10751 N NH2 . ARG B 2 461 ? -41.168 18.421 -2.427 1.00 195.98 ? 461 ARG B NH2 1 ATOM 10752 N N . CYS B 2 462 ? -42.003 14.038 -8.519 1.00 209.18 ? 462 CYS B N 1 ATOM 10753 C CA . CYS B 2 462 ? -41.687 14.784 -9.733 1.00 210.28 ? 462 CYS B CA 1 ATOM 10754 C C . CYS B 2 462 ? -40.845 16.021 -9.428 1.00 208.58 ? 462 CYS B C 1 ATOM 10755 O O . CYS B 2 462 ? -40.534 16.303 -8.271 1.00 201.77 ? 462 CYS B O 1 ATOM 10756 C CB . CYS B 2 462 ? -42.969 15.183 -10.465 1.00 206.53 ? 462 CYS B CB 1 ATOM 10757 S SG . CYS B 2 462 ? -42.972 14.766 -12.227 1.00 259.81 ? 462 CYS B SG 1 ATOM 10758 N N . GLY B 2 463 ? -40.484 16.757 -10.475 1.00 217.88 ? 463 GLY B N 1 ATOM 10759 C CA . GLY B 2 463 ? -39.619 17.914 -10.334 1.00 215.84 ? 463 GLY B CA 1 ATOM 10760 C C . GLY B 2 463 ? -40.366 19.203 -10.051 1.00 214.40 ? 463 GLY B C 1 ATOM 10761 O O . GLY B 2 463 ? -41.558 19.179 -9.745 1.00 215.14 ? 463 GLY B O 1 ATOM 10762 N N . PRO B 2 464 ? -39.663 20.342 -10.152 1.00 210.88 ? 464 PRO B N 1 ATOM 10763 C CA . PRO B 2 464 ? -40.247 21.663 -9.893 1.00 208.91 ? 464 PRO B CA 1 ATOM 10764 C C . PRO B 2 464 ? -41.316 22.030 -10.916 1.00 211.34 ? 464 PRO B C 1 ATOM 10765 O O . PRO B 2 464 ? -41.099 21.880 -12.118 1.00 217.40 ? 464 PRO B O 1 ATOM 10766 C CB . PRO B 2 464 ? -39.043 22.604 -9.997 1.00 213.31 ? 464 PRO B CB 1 ATOM 10767 C CG . PRO B 2 464 ? -38.086 21.890 -10.887 1.00 216.37 ? 464 PRO B CG 1 ATOM 10768 C CD . PRO B 2 464 ? -38.252 20.434 -10.567 1.00 211.84 ? 464 PRO B CD 1 ATOM 10769 N N . GLY B 2 465 ? -42.461 22.504 -10.435 1.00 210.96 ? 465 GLY B N 1 ATOM 10770 C CA . GLY B 2 465 ? -43.572 22.844 -11.304 1.00 217.83 ? 465 GLY B CA 1 ATOM 10771 C C . GLY B 2 465 ? -44.391 21.625 -11.684 1.00 216.04 ? 465 GLY B C 1 ATOM 10772 O O . GLY B 2 465 ? -45.515 21.747 -12.171 1.00 214.62 ? 465 GLY B O 1 ATOM 10773 N N . TRP B 2 466 ? -43.824 20.443 -11.456 1.00 217.65 ? 466 TRP B N 1 ATOM 10774 C CA . TRP B 2 466 ? -44.510 19.190 -11.748 1.00 218.81 ? 466 TRP B CA 1 ATOM 10775 C C . TRP B 2 466 ? -45.021 18.556 -10.461 1.00 217.43 ? 466 TRP B C 1 ATOM 10776 O O . TRP B 2 466 ? -46.221 18.378 -10.305 1.00 220.95 ? 466 TRP B O 1 ATOM 10777 C CB . TRP B 2 466 ? -43.589 18.231 -12.498 1.00 214.76 ? 466 TRP B CB 1 ATOM 10778 C CG . TRP B 2 466 ? -44.221 17.675 -13.733 1.00 215.62 ? 466 TRP B CG 1 ATOM 10779 C CD1 . TRP B 2 466 ? -45.543 17.395 -13.922 1.00 212.31 ? 466 TRP B CD1 1 ATOM 10780 C CD2 . TRP B 2 466 ? -43.563 17.356 -14.964 1.00 219.81 ? 466 TRP B CD2 1 ATOM 10781 N NE1 . TRP B 2 466 ? -45.747 16.909 -15.190 1.00 215.84 ? 466 TRP B NE1 1 ATOM 10782 C CE2 . TRP B 2 466 ? -44.548 16.876 -15.851 1.00 220.83 ? 466 TRP B CE2 1 ATOM 10783 C CE3 . TRP B 2 466 ? -42.237 17.425 -15.401 1.00 220.45 ? 466 TRP B CE3 1 ATOM 10784 C CZ2 . TRP B 2 466 ? -44.247 16.466 -17.148 1.00 225.97 ? 466 TRP B CZ2 1 ATOM 10785 C CZ3 . TRP B 2 466 ? -41.942 17.018 -16.689 1.00 226.45 ? 466 TRP B CZ3 1 ATOM 10786 C CH2 . TRP B 2 466 ? -42.942 16.545 -17.547 1.00 229.02 ? 466 TRP B CH2 1 ATOM 10787 N N . LEU B 2 467 ? -44.100 18.175 -9.578 1.00 211.91 ? 467 LEU B N 1 ATOM 10788 C CA . LEU B 2 467 ? -44.401 17.929 -8.165 1.00 205.63 ? 467 LEU B CA 1 ATOM 10789 C C . LEU B 2 467 ? -45.682 17.136 -7.893 1.00 204.95 ? 467 LEU B C 1 ATOM 10790 O O . LEU B 2 467 ? -46.688 17.697 -7.454 1.00 205.59 ? 467 LEU B O 1 ATOM 10791 C CB . LEU B 2 467 ? -44.475 19.263 -7.435 1.00 208.24 ? 467 LEU B CB 1 ATOM 10792 C CG . LEU B 2 467 ? -44.457 19.210 -5.914 1.00 205.90 ? 467 LEU B CG 1 ATOM 10793 C CD1 . LEU B 2 467 ? -43.128 18.702 -5.389 1.00 199.35 ? 467 LEU B CD1 1 ATOM 10794 C CD2 . LEU B 2 467 ? -44.698 20.592 -5.461 1.00 210.65 ? 467 LEU B CD2 1 ATOM 10795 N N . GLY B 2 468 ? -45.656 15.839 -8.171 1.00 204.14 ? 468 GLY B N 1 ATOM 10796 C CA . GLY B 2 468 ? -46.841 15.021 -8.003 1.00 205.54 ? 468 GLY B CA 1 ATOM 10797 C C . GLY B 2 468 ? -46.531 13.596 -7.598 1.00 203.26 ? 468 GLY B C 1 ATOM 10798 O O . GLY B 2 468 ? -45.365 13.204 -7.517 1.00 200.89 ? 468 GLY B O 1 ATOM 10799 N N . SER B 2 469 ? -47.586 12.834 -7.315 1.00 202.78 ? 469 SER B N 1 ATOM 10800 C CA . SER B 2 469 ? -47.465 11.418 -6.987 1.00 197.34 ? 469 SER B CA 1 ATOM 10801 C C . SER B 2 469 ? -46.669 10.698 -8.066 1.00 196.53 ? 469 SER B C 1 ATOM 10802 O O . SER B 2 469 ? -45.799 9.880 -7.768 1.00 191.39 ? 469 SER B O 1 ATOM 10803 C CB . SER B 2 469 ? -48.845 10.783 -6.824 1.00 199.35 ? 469 SER B CB 1 ATOM 10804 O OG . SER B 2 469 ? -49.565 11.398 -5.770 1.00 198.14 ? 469 SER B OG 1 ATOM 10805 N N . GLN B 2 470 ? -46.971 11.009 -9.323 1.00 204.68 ? 470 GLN B N 1 ATOM 10806 C CA . GLN B 2 470 ? -46.089 10.628 -10.414 1.00 212.17 ? 470 GLN B CA 1 ATOM 10807 C C . GLN B 2 470 ? -45.647 11.895 -11.134 1.00 217.37 ? 470 GLN B C 1 ATOM 10808 O O . GLN B 2 470 ? -44.546 12.387 -10.895 1.00 215.93 ? 470 GLN B O 1 ATOM 10809 C CB . GLN B 2 470 ? -46.788 9.667 -11.380 1.00 219.20 ? 470 GLN B CB 1 ATOM 10810 C CG . GLN B 2 470 ? -47.242 8.353 -10.754 1.00 217.15 ? 470 GLN B CG 1 ATOM 10811 C CD . GLN B 2 470 ? -48.522 8.490 -9.951 1.00 212.38 ? 470 GLN B CD 1 ATOM 10812 O OE1 . GLN B 2 470 ? -49.166 9.539 -9.961 1.00 210.34 ? 470 GLN B OE1 1 ATOM 10813 N NE2 . GLN B 2 470 ? -48.897 7.427 -9.249 1.00 211.23 ? 470 GLN B NE2 1 ATOM 10814 N N . CYS B 2 471 ? -46.502 12.427 -12.005 1.00 224.31 ? 471 CYS B N 1 ATOM 10815 C CA . CYS B 2 471 ? -46.363 13.806 -12.469 1.00 229.78 ? 471 CYS B CA 1 ATOM 10816 C C . CYS B 2 471 ? -47.712 14.510 -12.642 1.00 230.84 ? 471 CYS B C 1 ATOM 10817 O O . CYS B 2 471 ? -48.492 14.114 -13.509 1.00 236.09 ? 471 CYS B O 1 ATOM 10818 C CB . CYS B 2 471 ? -45.591 13.848 -13.792 1.00 238.06 ? 471 CYS B CB 1 ATOM 10819 S SG . CYS B 2 471 ? -43.807 13.582 -13.652 1.00 259.96 ? 471 CYS B SG 1 ATOM 10820 N N . GLU B 2 472 ? -47.961 15.546 -11.835 1.00 230.51 ? 472 GLU B N 1 ATOM 10821 C CA . GLU B 2 472 ? -48.978 16.582 -12.091 1.00 230.01 ? 472 GLU B CA 1 ATOM 10822 C C . GLU B 2 472 ? -49.076 17.554 -10.915 1.00 228.66 ? 472 GLU B C 1 ATOM 10823 O O . GLU B 2 472 ? -48.712 17.210 -9.789 1.00 226.04 ? 472 GLU B O 1 ATOM 10824 C CB . GLU B 2 472 ? -50.361 15.979 -12.365 1.00 228.74 ? 472 GLU B CB 1 ATOM 10825 C CG . GLU B 2 472 ? -50.853 16.230 -13.785 1.00 240.02 ? 472 GLU B CG 1 ATOM 10826 C CD . GLU B 2 472 ? -52.088 15.425 -14.135 1.00 246.07 ? 472 GLU B CD 1 ATOM 10827 O OE1 . GLU B 2 472 ? -52.600 14.704 -13.253 1.00 244.05 ? 472 GLU B OE1 1 ATOM 10828 O OE2 . GLU B 2 472 ? -52.547 15.513 -15.293 1.00 250.90 ? 472 GLU B OE2 1 ATOM 10829 N N . CYS B 2 473 ? -49.592 18.754 -11.178 1.00 230.64 ? 473 CYS B N 1 ATOM 10830 C CA . CYS B 2 473 ? -49.743 19.786 -10.148 1.00 224.72 ? 473 CYS B CA 1 ATOM 10831 C C . CYS B 2 473 ? -50.564 20.983 -10.612 1.00 219.37 ? 473 CYS B C 1 ATOM 10832 O O . CYS B 2 473 ? -51.224 20.953 -11.650 1.00 219.67 ? 473 CYS B O 1 ATOM 10833 C CB . CYS B 2 473 ? -48.390 20.288 -9.650 1.00 227.41 ? 473 CYS B CB 1 ATOM 10834 S SG . CYS B 2 473 ? -48.480 21.086 -8.027 1.00 266.34 ? 473 CYS B SG 1 ATOM 10835 N N . SER B 2 474 ? -50.499 22.038 -9.804 1.00 218.29 ? 474 SER B N 1 ATOM 10836 C CA . SER B 2 474 ? -51.103 23.330 -10.109 1.00 218.19 ? 474 SER B CA 1 ATOM 10837 C C . SER B 2 474 ? -50.473 23.933 -11.361 1.00 217.51 ? 474 SER B C 1 ATOM 10838 O O . SER B 2 474 ? -49.403 23.495 -11.787 1.00 215.69 ? 474 SER B O 1 ATOM 10839 C CB . SER B 2 474 ? -50.947 24.288 -8.928 1.00 213.53 ? 474 SER B CB 1 ATOM 10840 O OG . SER B 2 474 ? -49.580 24.544 -8.660 1.00 202.78 ? 474 SER B OG 1 ATOM 10841 N N . GLU B 2 475 ? -51.153 24.949 -11.903 1.00 217.28 ? 475 GLU B N 1 ATOM 10842 C CA . GLU B 2 475 ? -51.132 25.401 -13.307 1.00 220.71 ? 475 GLU B CA 1 ATOM 10843 C C . GLU B 2 475 ? -52.217 24.616 -14.030 1.00 225.15 ? 475 GLU B C 1 ATOM 10844 O O . GLU B 2 475 ? -52.553 24.889 -15.182 1.00 233.63 ? 475 GLU B O 1 ATOM 10845 C CB . GLU B 2 475 ? -49.773 25.221 -13.994 1.00 219.85 ? 475 GLU B CB 1 ATOM 10846 C CG . GLU B 2 475 ? -48.660 26.085 -13.422 1.00 216.91 ? 475 GLU B CG 1 ATOM 10847 C CD . GLU B 2 475 ? -47.292 25.679 -13.932 1.00 217.72 ? 475 GLU B CD 1 ATOM 10848 O OE1 . GLU B 2 475 ? -47.226 24.885 -14.894 1.00 220.23 ? 475 GLU B OE1 1 ATOM 10849 O OE2 . GLU B 2 475 ? -46.282 26.147 -13.367 1.00 215.96 ? 475 GLU B OE2 1 ATOM 10850 N N . GLU B 2 476 ? -52.754 23.631 -13.320 1.00 220.90 ? 476 GLU B N 1 ATOM 10851 C CA . GLU B 2 476 ? -54.052 23.050 -13.616 1.00 227.31 ? 476 GLU B CA 1 ATOM 10852 C C . GLU B 2 476 ? -54.839 23.046 -12.316 1.00 226.47 ? 476 GLU B C 1 ATOM 10853 O O . GLU B 2 476 ? -55.816 23.780 -12.159 1.00 231.23 ? 476 GLU B O 1 ATOM 10854 C CB . GLU B 2 476 ? -53.927 21.632 -14.174 1.00 226.70 ? 476 GLU B CB 1 ATOM 10855 C CG . GLU B 2 476 ? -53.619 21.559 -15.657 1.00 229.83 ? 476 GLU B CG 1 ATOM 10856 C CD . GLU B 2 476 ? -53.797 20.159 -16.211 1.00 225.80 ? 476 GLU B CD 1 ATOM 10857 O OE1 . GLU B 2 476 ? -54.030 19.228 -15.411 1.00 219.15 ? 476 GLU B OE1 1 ATOM 10858 O OE2 . GLU B 2 476 ? -53.709 19.989 -17.445 1.00 230.08 ? 476 GLU B OE2 1 ATOM 10859 N N . ASP B 2 477 ? -54.400 22.189 -11.396 1.00 220.33 ? 477 ASP B N 1 ATOM 10860 C CA . ASP B 2 477 ? -54.899 22.121 -10.023 1.00 217.24 ? 477 ASP B CA 1 ATOM 10861 C C . ASP B 2 477 ? -56.362 21.684 -9.938 1.00 223.09 ? 477 ASP B C 1 ATOM 10862 O O . ASP B 2 477 ? -56.843 21.357 -8.857 1.00 216.50 ? 477 ASP B O 1 ATOM 10863 C CB . ASP B 2 477 ? -54.714 23.470 -9.318 1.00 215.20 ? 477 ASP B CB 1 ATOM 10864 C CG . ASP B 2 477 ? -54.845 23.366 -7.810 1.00 213.43 ? 477 ASP B CG 1 ATOM 10865 O OD1 . ASP B 2 477 ? -54.571 22.278 -7.261 1.00 213.29 ? 477 ASP B OD1 1 ATOM 10866 O OD2 . ASP B 2 477 ? -55.218 24.374 -7.173 1.00 216.02 ? 477 ASP B OD2 1 ATOM 10867 N N . TYR B 2 478 ? -57.046 21.665 -11.083 1.00 237.63 ? 478 TYR B N 1 ATOM 10868 C CA . TYR B 2 478 ? -58.440 21.234 -11.198 1.00 244.75 ? 478 TYR B CA 1 ATOM 10869 C C . TYR B 2 478 ? -59.314 21.846 -10.110 1.00 238.73 ? 478 TYR B C 1 ATOM 10870 O O . TYR B 2 478 ? -59.208 23.031 -9.795 1.00 236.80 ? 478 TYR B O 1 ATOM 10871 C CB . TYR B 2 478 ? -58.546 19.704 -11.137 1.00 251.01 ? 478 TYR B CB 1 ATOM 10872 C CG . TYR B 2 478 ? -57.250 18.965 -11.389 1.00 254.87 ? 478 TYR B CG 1 ATOM 10873 C CD1 . TYR B 2 478 ? -56.785 18.756 -12.680 1.00 260.86 ? 478 TYR B CD1 1 ATOM 10874 C CD2 . TYR B 2 478 ? -56.499 18.462 -10.333 1.00 249.82 ? 478 TYR B CD2 1 ATOM 10875 C CE1 . TYR B 2 478 ? -55.603 18.078 -12.912 1.00 260.88 ? 478 TYR B CE1 1 ATOM 10876 C CE2 . TYR B 2 478 ? -55.317 17.785 -10.555 1.00 248.18 ? 478 TYR B CE2 1 ATOM 10877 C CZ . TYR B 2 478 ? -54.874 17.595 -11.845 1.00 255.33 ? 478 TYR B CZ 1 ATOM 10878 O OH . TYR B 2 478 ? -53.697 16.919 -12.067 1.00 256.13 ? 478 TYR B OH 1 ATOM 10879 N N . ARG B 2 479 ? -60.176 21.011 -9.542 1.00 235.86 ? 479 ARG B N 1 ATOM 10880 C CA . ARG B 2 479 ? -60.750 21.262 -8.232 1.00 228.26 ? 479 ARG B CA 1 ATOM 10881 C C . ARG B 2 479 ? -59.713 20.754 -7.242 1.00 225.81 ? 479 ARG B C 1 ATOM 10882 O O . ARG B 2 479 ? -58.799 20.035 -7.645 1.00 226.24 ? 479 ARG B O 1 ATOM 10883 C CB . ARG B 2 479 ? -62.092 20.544 -8.060 1.00 219.44 ? 479 ARG B CB 1 ATOM 10884 C CG . ARG B 2 479 ? -63.135 20.898 -9.103 1.00 213.75 ? 479 ARG B CG 1 ATOM 10885 C CD . ARG B 2 479 ? -64.480 20.290 -8.746 1.00 206.68 ? 479 ARG B CD 1 ATOM 10886 N NE . ARG B 2 479 ? -65.483 20.522 -9.780 1.00 208.87 ? 479 ARG B NE 1 ATOM 10887 C CZ . ARG B 2 479 ? -66.771 20.223 -9.649 1.00 214.61 ? 479 ARG B CZ 1 ATOM 10888 N NH1 . ARG B 2 479 ? -67.215 19.684 -8.521 1.00 211.72 ? 479 ARG B NH1 1 ATOM 10889 N NH2 . ARG B 2 479 ? -67.615 20.466 -10.641 1.00 222.67 ? 479 ARG B NH2 1 ATOM 10890 N N . PRO B 2 480 ? -59.836 21.115 -5.952 1.00 226.15 ? 480 PRO B N 1 ATOM 10891 C CA . PRO B 2 480 ? -58.905 20.591 -4.945 1.00 224.72 ? 480 PRO B CA 1 ATOM 10892 C C . PRO B 2 480 ? -58.698 19.077 -5.049 1.00 232.68 ? 480 PRO B C 1 ATOM 10893 O O . PRO B 2 480 ? -57.631 18.586 -4.674 1.00 226.83 ? 480 PRO B O 1 ATOM 10894 C CB . PRO B 2 480 ? -59.580 20.954 -3.612 1.00 220.59 ? 480 PRO B CB 1 ATOM 10895 C CG . PRO B 2 480 ? -60.837 21.737 -3.969 1.00 223.77 ? 480 PRO B CG 1 ATOM 10896 C CD . PRO B 2 480 ? -60.693 22.169 -5.388 1.00 228.03 ? 480 PRO B CD 1 ATOM 10897 N N . SER B 2 481 ? -59.728 18.367 -5.514 1.00 246.99 ? 481 SER B N 1 ATOM 10898 C CA . SER B 2 481 ? -59.697 16.927 -5.803 1.00 246.43 ? 481 SER B CA 1 ATOM 10899 C C . SER B 2 481 ? -59.699 16.115 -4.514 1.00 237.74 ? 481 SER B C 1 ATOM 10900 O O . SER B 2 481 ? -59.994 14.920 -4.518 1.00 234.98 ? 481 SER B O 1 ATOM 10901 C CB . SER B 2 481 ? -58.482 16.560 -6.665 1.00 246.19 ? 481 SER B CB 1 ATOM 10902 O OG . SER B 2 481 ? -58.397 15.160 -6.861 1.00 245.15 ? 481 SER B OG 1 ATOM 10903 N N . GLN B 2 482 ? -59.384 16.807 -3.425 1.00 231.72 ? 482 GLN B N 1 ATOM 10904 C CA . GLN B 2 482 ? -59.414 16.309 -2.059 1.00 219.93 ? 482 GLN B CA 1 ATOM 10905 C C . GLN B 2 482 ? -58.875 17.435 -1.195 1.00 206.26 ? 482 GLN B C 1 ATOM 10906 O O . GLN B 2 482 ? -58.218 18.348 -1.699 1.00 199.33 ? 482 GLN B O 1 ATOM 10907 C CB . GLN B 2 482 ? -58.572 15.042 -1.877 1.00 212.81 ? 482 GLN B CB 1 ATOM 10908 C CG . GLN B 2 482 ? -59.382 13.765 -1.681 1.00 207.72 ? 482 GLN B CG 1 ATOM 10909 C CD . GLN B 2 482 ? -60.158 13.750 -0.376 1.00 201.84 ? 482 GLN B CD 1 ATOM 10910 O OE1 . GLN B 2 482 ? -59.831 14.475 0.564 1.00 201.89 ? 482 GLN B OE1 1 ATOM 10911 N NE2 . GLN B 2 482 ? -61.193 12.921 -0.314 1.00 196.46 ? 482 GLN B NE2 1 ATOM 10912 N N . GLN B 2 483 ? -59.141 17.377 0.101 1.00 199.02 ? 483 GLN B N 1 ATOM 10913 C CA . GLN B 2 483 ? -58.483 18.281 1.027 1.00 185.97 ? 483 GLN B CA 1 ATOM 10914 C C . GLN B 2 483 ? -57.098 17.720 1.304 1.00 181.48 ? 483 GLN B C 1 ATOM 10915 O O . GLN B 2 483 ? -56.201 18.429 1.762 1.00 180.48 ? 483 GLN B O 1 ATOM 10916 C CB . GLN B 2 483 ? -59.293 18.428 2.313 1.00 182.17 ? 483 GLN B CB 1 ATOM 10917 C CG . GLN B 2 483 ? -59.676 17.101 2.943 1.00 183.35 ? 483 GLN B CG 1 ATOM 10918 C CD . GLN B 2 483 ? -60.891 17.212 3.837 1.00 179.90 ? 483 GLN B CD 1 ATOM 10919 O OE1 . GLN B 2 483 ? -61.315 18.310 4.196 1.00 180.77 ? 483 GLN B OE1 1 ATOM 10920 N NE2 . GLN B 2 483 ? -61.466 16.070 4.196 1.00 171.83 ? 483 GLN B NE2 1 ATOM 10921 N N . ASP B 2 484 ? -56.955 16.425 1.021 1.00 188.19 ? 484 ASP B N 1 ATOM 10922 C CA . ASP B 2 484 ? -55.733 15.659 1.258 1.00 190.25 ? 484 ASP B CA 1 ATOM 10923 C C . ASP B 2 484 ? -55.374 15.710 2.737 1.00 182.25 ? 484 ASP B C 1 ATOM 10924 O O . ASP B 2 484 ? -54.238 15.430 3.125 1.00 179.58 ? 484 ASP B O 1 ATOM 10925 C CB . ASP B 2 484 ? -54.582 16.194 0.396 1.00 196.32 ? 484 ASP B CB 1 ATOM 10926 C CG . ASP B 2 484 ? -53.402 15.242 0.337 1.00 198.18 ? 484 ASP B CG 1 ATOM 10927 O OD1 . ASP B 2 484 ? -53.624 14.014 0.363 1.00 203.60 ? 484 ASP B OD1 1 ATOM 10928 O OD2 . ASP B 2 484 ? -52.252 15.725 0.267 1.00 192.49 ? 484 ASP B OD2 1 ATOM 10929 N N . GLU B 2 485 ? -56.379 16.026 3.552 1.00 177.57 ? 485 GLU B N 1 ATOM 10930 C CA . GLU B 2 485 ? -56.208 16.299 4.973 1.00 175.75 ? 485 GLU B CA 1 ATOM 10931 C C . GLU B 2 485 ? -54.945 17.120 5.214 1.00 176.52 ? 485 GLU B C 1 ATOM 10932 O O . GLU B 2 485 ? -54.016 16.665 5.881 1.00 173.30 ? 485 GLU B O 1 ATOM 10933 C CB . GLU B 2 485 ? -56.177 14.996 5.772 1.00 176.83 ? 485 GLU B CB 1 ATOM 10934 C CG . GLU B 2 485 ? -57.480 14.212 5.692 1.00 185.18 ? 485 GLU B CG 1 ATOM 10935 C CD . GLU B 2 485 ? -57.566 13.104 6.722 1.00 185.71 ? 485 GLU B CD 1 ATOM 10936 O OE1 . GLU B 2 485 ? -56.684 13.039 7.604 1.00 185.71 ? 485 GLU B OE1 1 ATOM 10937 O OE2 . GLU B 2 485 ? -58.519 12.299 6.652 1.00 182.58 ? 485 GLU B OE2 1 ATOM 10938 N N . CYS B 2 486 ? -54.921 18.332 4.665 1.00 176.19 ? 486 CYS B N 1 ATOM 10939 C CA . CYS B 2 486 ? -53.785 19.230 4.836 1.00 163.54 ? 486 CYS B CA 1 ATOM 10940 C C . CYS B 2 486 ? -53.702 19.669 6.293 1.00 157.90 ? 486 CYS B C 1 ATOM 10941 O O . CYS B 2 486 ? -52.678 20.169 6.752 1.00 156.51 ? 486 CYS B O 1 ATOM 10942 C CB . CYS B 2 486 ? -53.900 20.442 3.905 1.00 166.76 ? 486 CYS B CB 1 ATOM 10943 S SG . CYS B 2 486 ? -53.375 20.149 2.191 1.00 133.61 ? 486 CYS B SG 1 ATOM 10944 N N . SER B 2 487 ? -54.800 19.473 7.011 1.00 158.28 ? 487 SER B N 1 ATOM 10945 C CA . SER B 2 487 ? -54.837 19.660 8.452 1.00 166.01 ? 487 SER B CA 1 ATOM 10946 C C . SER B 2 487 ? -55.126 18.309 9.101 1.00 174.17 ? 487 SER B C 1 ATOM 10947 O O . SER B 2 487 ? -55.716 17.437 8.463 1.00 176.04 ? 487 SER B O 1 ATOM 10948 C CB . SER B 2 487 ? -55.896 20.696 8.833 1.00 167.15 ? 487 SER B CB 1 ATOM 10949 O OG . SER B 2 487 ? -55.602 21.959 8.261 1.00 163.98 ? 487 SER B OG 1 ATOM 10950 N N . PRO B 2 488 ? -54.698 18.122 10.363 1.00 171.30 ? 488 PRO B N 1 ATOM 10951 C CA . PRO B 2 488 ? -54.936 16.862 11.081 1.00 168.43 ? 488 PRO B CA 1 ATOM 10952 C C . PRO B 2 488 ? -56.409 16.454 11.090 1.00 171.21 ? 488 PRO B C 1 ATOM 10953 O O . PRO B 2 488 ? -56.722 15.264 11.125 1.00 176.30 ? 488 PRO B O 1 ATOM 10954 C CB . PRO B 2 488 ? -54.441 17.163 12.504 1.00 161.68 ? 488 PRO B CB 1 ATOM 10955 C CG . PRO B 2 488 ? -54.315 18.658 12.576 1.00 159.83 ? 488 PRO B CG 1 ATOM 10956 C CD . PRO B 2 488 ? -53.958 19.086 11.194 1.00 162.30 ? 488 PRO B CD 1 ATOM 10957 N N . ARG B 2 489 ? -57.297 17.442 11.056 1.00 167.53 ? 489 ARG B N 1 ATOM 10958 C CA . ARG B 2 489 ? -58.726 17.193 10.920 1.00 168.13 ? 489 ARG B CA 1 ATOM 10959 C C . ARG B 2 489 ? -59.294 18.050 9.793 1.00 164.60 ? 489 ARG B C 1 ATOM 10960 O O . ARG B 2 489 ? -58.764 19.119 9.492 1.00 161.78 ? 489 ARG B O 1 ATOM 10961 C CB . ARG B 2 489 ? -59.451 17.475 12.237 1.00 164.72 ? 489 ARG B CB 1 ATOM 10962 C CG . ARG B 2 489 ? -59.049 18.781 12.897 1.00 152.03 ? 489 ARG B CG 1 ATOM 10963 C CD . ARG B 2 489 ? -59.698 18.933 14.263 1.00 154.87 ? 489 ARG B CD 1 ATOM 10964 N NE . ARG B 2 489 ? -59.265 20.151 14.940 1.00 159.99 ? 489 ARG B NE 1 ATOM 10965 C CZ . ARG B 2 489 ? -59.660 20.510 16.157 1.00 160.90 ? 489 ARG B CZ 1 ATOM 10966 N NH1 . ARG B 2 489 ? -60.501 19.742 16.837 1.00 163.33 ? 489 ARG B NH1 1 ATOM 10967 N NH2 . ARG B 2 489 ? -59.215 21.637 16.695 1.00 158.35 ? 489 ARG B NH2 1 ATOM 10968 N N . GLU B 2 490 ? -60.370 17.579 9.170 1.00 161.10 ? 490 GLU B N 1 ATOM 10969 C CA . GLU B 2 490 ? -60.944 18.268 8.019 1.00 165.58 ? 490 GLU B CA 1 ATOM 10970 C C . GLU B 2 490 ? -61.720 19.519 8.422 1.00 172.97 ? 490 GLU B C 1 ATOM 10971 O O . GLU B 2 490 ? -62.159 20.288 7.567 1.00 174.31 ? 490 GLU B O 1 ATOM 10972 C CB . GLU B 2 490 ? -61.858 17.330 7.229 1.00 168.81 ? 490 GLU B CB 1 ATOM 10973 C CG . GLU B 2 490 ? -63.203 17.069 7.882 1.00 173.60 ? 490 GLU B CG 1 ATOM 10974 C CD . GLU B 2 490 ? -64.208 16.483 6.911 1.00 177.68 ? 490 GLU B CD 1 ATOM 10975 O OE1 . GLU B 2 490 ? -63.869 16.344 5.717 1.00 180.87 ? 490 GLU B OE1 1 ATOM 10976 O OE2 . GLU B 2 490 ? -65.338 16.166 7.339 1.00 176.46 ? 490 GLU B OE2 1 ATOM 10977 N N . GLY B 2 491 ? -61.889 19.718 9.725 1.00 174.56 ? 491 GLY B N 1 ATOM 10978 C CA . GLY B 2 491 ? -62.594 20.880 10.234 1.00 170.85 ? 491 GLY B CA 1 ATOM 10979 C C . GLY B 2 491 ? -61.677 22.073 10.428 1.00 170.27 ? 491 GLY B C 1 ATOM 10980 O O . GLY B 2 491 ? -62.014 23.018 11.141 1.00 176.32 ? 491 GLY B O 1 ATOM 10981 N N . GLN B 2 492 ? -60.513 22.025 9.790 1.00 168.59 ? 492 GLN B N 1 ATOM 10982 C CA . GLN B 2 492 ? -59.532 23.099 9.884 1.00 171.64 ? 492 GLN B CA 1 ATOM 10983 C C . GLN B 2 492 ? -59.173 23.623 8.492 1.00 174.54 ? 492 GLN B C 1 ATOM 10984 O O . GLN B 2 492 ? -59.299 22.897 7.505 1.00 164.48 ? 492 GLN B O 1 ATOM 10985 C CB . GLN B 2 492 ? -58.280 22.609 10.620 1.00 163.57 ? 492 GLN B CB 1 ATOM 10986 C CG . GLN B 2 492 ? -58.515 22.259 12.082 1.00 160.11 ? 492 GLN B CG 1 ATOM 10987 C CD . GLN B 2 492 ? -58.883 23.466 12.923 1.00 163.24 ? 492 GLN B CD 1 ATOM 10988 O OE1 . GLN B 2 492 ? -58.538 24.600 12.590 1.00 161.59 ? 492 GLN B OE1 1 ATOM 10989 N NE2 . GLN B 2 492 ? -59.590 23.227 14.022 1.00 166.42 ? 492 GLN B NE2 1 ATOM 10990 N N . PRO B 2 493 ? -58.727 24.889 8.407 1.00 175.92 ? 493 PRO B N 1 ATOM 10991 C CA . PRO B 2 493 ? -58.399 25.519 7.121 1.00 175.00 ? 493 PRO B CA 1 ATOM 10992 C C . PRO B 2 493 ? -57.179 24.913 6.426 1.00 170.21 ? 493 PRO B C 1 ATOM 10993 O O . PRO B 2 493 ? -56.649 23.894 6.870 1.00 167.66 ? 493 PRO B O 1 ATOM 10994 C CB . PRO B 2 493 ? -58.126 26.977 7.508 1.00 166.81 ? 493 PRO B CB 1 ATOM 10995 C CG . PRO B 2 493 ? -57.738 26.922 8.942 1.00 157.72 ? 493 PRO B CG 1 ATOM 10996 C CD . PRO B 2 493 ? -58.582 25.835 9.528 1.00 164.30 ? 493 PRO B CD 1 ATOM 10997 N N . VAL B 2 494 ? -56.754 25.549 5.336 1.00 166.60 ? 494 VAL B N 1 ATOM 10998 C CA . VAL B 2 494 ? -55.613 25.095 4.544 1.00 161.13 ? 494 VAL B CA 1 ATOM 10999 C C . VAL B 2 494 ? -54.359 24.996 5.407 1.00 154.25 ? 494 VAL B C 1 ATOM 11000 O O . VAL B 2 494 ? -54.217 25.737 6.381 1.00 163.00 ? 494 VAL B O 1 ATOM 11001 C CB . VAL B 2 494 ? -55.347 26.038 3.356 1.00 169.17 ? 494 VAL B CB 1 ATOM 11002 C CG1 . VAL B 2 494 ? -55.455 25.281 2.046 1.00 169.60 ? 494 VAL B CG1 1 ATOM 11003 C CG2 . VAL B 2 494 ? -56.322 27.206 3.378 1.00 175.07 ? 494 VAL B CG2 1 ATOM 11004 N N . CYS B 2 495 ? -53.461 24.078 5.052 1.00 147.46 ? 495 CYS B N 1 ATOM 11005 C CA . CYS B 2 495 ? -52.362 23.699 5.939 1.00 153.29 ? 495 CYS B CA 1 ATOM 11006 C C . CYS B 2 495 ? -51.486 24.871 6.369 1.00 143.94 ? 495 CYS B C 1 ATOM 11007 O O . CYS B 2 495 ? -50.871 25.539 5.540 1.00 143.45 ? 495 CYS B O 1 ATOM 11008 C CB . CYS B 2 495 ? -51.485 22.639 5.262 1.00 166.54 ? 495 CYS B CB 1 ATOM 11009 S SG . CYS B 2 495 ? -50.869 23.075 3.617 1.00 215.01 ? 495 CYS B SG 1 ATOM 11010 N N . SER B 2 496 ? -51.427 25.081 7.683 1.00 137.16 ? 496 SER B N 1 ATOM 11011 C CA . SER B 2 496 ? -50.570 26.082 8.317 1.00 136.73 ? 496 SER B CA 1 ATOM 11012 C C . SER B 2 496 ? -50.604 27.451 7.635 1.00 139.11 ? 496 SER B C 1 ATOM 11013 O O . SER B 2 496 ? -49.600 28.163 7.639 1.00 148.17 ? 496 SER B O 1 ATOM 11014 C CB . SER B 2 496 ? -49.127 25.572 8.368 1.00 138.99 ? 496 SER B CB 1 ATOM 11015 O OG . SER B 2 496 ? -49.060 24.304 8.997 1.00 132.48 ? 496 SER B OG 1 ATOM 11016 N N . GLN B 2 497 ? -51.762 27.824 7.087 1.00 141.87 ? 497 GLN B N 1 ATOM 11017 C CA . GLN B 2 497 ? -51.889 29.018 6.246 1.00 154.85 ? 497 GLN B CA 1 ATOM 11018 C C . GLN B 2 497 ? -50.781 29.026 5.221 1.00 165.13 ? 497 GLN B C 1 ATOM 11019 O O . GLN B 2 497 ? -50.625 28.040 4.506 1.00 167.69 ? 497 GLN B O 1 ATOM 11020 C CB . GLN B 2 497 ? -51.838 30.297 7.074 1.00 152.59 ? 497 GLN B CB 1 ATOM 11021 C CG . GLN B 2 497 ? -52.703 30.261 8.303 1.00 146.84 ? 497 GLN B CG 1 ATOM 11022 C CD . GLN B 2 497 ? -54.172 30.127 7.978 1.00 149.80 ? 497 GLN B CD 1 ATOM 11023 O OE1 . GLN B 2 497 ? -54.616 30.454 6.876 1.00 152.61 ? 497 GLN B OE1 1 ATOM 11024 N NE2 . GLN B 2 497 ? -54.941 29.643 8.943 1.00 152.97 ? 497 GLN B NE2 1 ATOM 11025 N N . ARG B 2 498 ? -50.036 30.135 5.152 1.00 170.81 ? 498 ARG B N 1 ATOM 11026 C CA . ARG B 2 498 ? -48.716 30.128 4.529 1.00 174.31 ? 498 ARG B CA 1 ATOM 11027 C C . ARG B 2 498 ? -48.775 29.494 3.146 1.00 190.40 ? 498 ARG B C 1 ATOM 11028 O O . ARG B 2 498 ? -48.577 28.313 3.035 1.00 184.25 ? 498 ARG B O 1 ATOM 11029 C CB . ARG B 2 498 ? -47.705 29.392 5.429 1.00 163.15 ? 498 ARG B CB 1 ATOM 11030 C CG . ARG B 2 498 ? -46.376 30.110 5.646 1.00 163.34 ? 498 ARG B CG 1 ATOM 11031 C CD . ARG B 2 498 ? -45.517 29.393 6.689 1.00 156.74 ? 498 ARG B CD 1 ATOM 11032 N NE . ARG B 2 498 ? -46.167 29.328 7.999 1.00 148.31 ? 498 ARG B NE 1 ATOM 11033 C CZ . ARG B 2 498 ? -45.583 28.883 9.109 1.00 134.15 ? 498 ARG B CZ 1 ATOM 11034 N NH1 . ARG B 2 498 ? -44.326 28.462 9.082 1.00 128.79 ? 498 ARG B NH1 1 ATOM 11035 N NH2 . ARG B 2 498 ? -46.255 28.863 10.253 1.00 131.22 ? 498 ARG B NH2 1 ATOM 11036 N N . GLY B 2 499 ? -49.235 30.212 2.134 1.00 209.16 ? 499 GLY B N 1 ATOM 11037 C CA . GLY B 2 499 ? -49.181 29.679 0.782 1.00 217.63 ? 499 GLY B CA 1 ATOM 11038 C C . GLY B 2 499 ? -50.164 28.548 0.519 1.00 210.61 ? 499 GLY B C 1 ATOM 11039 O O . GLY B 2 499 ? -50.031 27.810 -0.459 1.00 207.41 ? 499 GLY B O 1 ATOM 11040 N N . GLU B 2 500 ? -51.151 28.425 1.404 1.00 206.84 ? 500 GLU B N 1 ATOM 11041 C CA . GLU B 2 500 ? -52.264 27.480 1.273 1.00 210.36 ? 500 GLU B CA 1 ATOM 11042 C C . GLU B 2 500 ? -51.825 26.031 1.050 1.00 210.06 ? 500 GLU B C 1 ATOM 11043 O O . GLU B 2 500 ? -50.845 25.576 1.635 1.00 203.08 ? 500 GLU B O 1 ATOM 11044 C CB . GLU B 2 500 ? -53.184 27.914 0.125 1.00 218.88 ? 500 GLU B CB 1 ATOM 11045 C CG . GLU B 2 500 ? -53.312 29.424 -0.054 1.00 220.01 ? 500 GLU B CG 1 ATOM 11046 C CD . GLU B 2 500 ? -53.769 30.137 1.204 1.00 213.08 ? 500 GLU B CD 1 ATOM 11047 O OE1 . GLU B 2 500 ? -54.623 29.586 1.929 1.00 215.17 ? 500 GLU B OE1 1 ATOM 11048 O OE2 . GLU B 2 500 ? -53.270 31.251 1.468 1.00 205.92 ? 500 GLU B OE2 1 ATOM 11049 N N . CYS B 2 501 ? -52.555 25.323 0.192 1.00 219.59 ? 501 CYS B N 1 ATOM 11050 C CA . CYS B 2 501 ? -52.256 23.931 -0.140 1.00 213.71 ? 501 CYS B CA 1 ATOM 11051 C C . CYS B 2 501 ? -52.545 23.694 -1.619 1.00 208.67 ? 501 CYS B C 1 ATOM 11052 O O . CYS B 2 501 ? -53.605 24.077 -2.117 1.00 209.10 ? 501 CYS B O 1 ATOM 11053 C CB . CYS B 2 501 ? -53.075 22.975 0.736 1.00 212.37 ? 501 CYS B CB 1 ATOM 11054 S SG . CYS B 2 501 ? -52.598 21.227 0.650 1.00 216.50 ? 501 CYS B SG 1 ATOM 11055 N N . LEU B 2 502 ? -51.607 23.068 -2.323 1.00 200.22 ? 502 LEU B N 1 ATOM 11056 C CA . LEU B 2 502 ? -51.731 22.904 -3.769 1.00 194.97 ? 502 LEU B CA 1 ATOM 11057 C C . LEU B 2 502 ? -51.516 21.467 -4.234 1.00 193.59 ? 502 LEU B C 1 ATOM 11058 O O . LEU B 2 502 ? -50.446 20.899 -4.019 1.00 194.51 ? 502 LEU B O 1 ATOM 11059 C CB . LEU B 2 502 ? -50.738 23.819 -4.497 1.00 198.71 ? 502 LEU B CB 1 ATOM 11060 C CG . LEU B 2 502 ? -51.091 25.293 -4.728 1.00 209.40 ? 502 LEU B CG 1 ATOM 11061 C CD1 . LEU B 2 502 ? -51.058 26.101 -3.439 1.00 211.93 ? 502 LEU B CD1 1 ATOM 11062 C CD2 . LEU B 2 502 ? -50.151 25.900 -5.756 1.00 213.31 ? 502 LEU B CD2 1 ATOM 11063 N N . CYS B 2 503 ? -52.543 20.900 -4.870 1.00 195.28 ? 503 CYS B N 1 ATOM 11064 C CA . CYS B 2 503 ? -52.468 19.610 -5.569 1.00 188.29 ? 503 CYS B CA 1 ATOM 11065 C C . CYS B 2 503 ? -51.702 18.532 -4.805 1.00 179.20 ? 503 CYS B C 1 ATOM 11066 O O . CYS B 2 503 ? -50.587 18.172 -5.179 1.00 179.07 ? 503 CYS B O 1 ATOM 11067 C CB . CYS B 2 503 ? -51.860 19.790 -6.973 1.00 190.62 ? 503 CYS B CB 1 ATOM 11068 S SG . CYS B 2 503 ? -50.194 20.519 -7.090 1.00 262.81 ? 503 CYS B SG 1 ATOM 11069 N N . GLY B 2 504 ? -52.300 18.005 -3.741 1.00 180.29 ? 504 GLY B N 1 ATOM 11070 C CA . GLY B 2 504 ? -51.571 17.088 -2.888 1.00 178.96 ? 504 GLY B CA 1 ATOM 11071 C C . GLY B 2 504 ? -50.496 17.818 -2.109 1.00 173.00 ? 504 GLY B C 1 ATOM 11072 O O . GLY B 2 504 ? -50.807 18.710 -1.318 1.00 161.22 ? 504 GLY B O 1 ATOM 11073 N N . GLN B 2 505 ? -49.241 17.426 -2.324 1.00 168.22 ? 505 GLN B N 1 ATOM 11074 C CA . GLN B 2 505 ? -48.109 17.909 -1.535 1.00 168.02 ? 505 GLN B CA 1 ATOM 11075 C C . GLN B 2 505 ? -48.097 19.424 -1.384 1.00 165.68 ? 505 GLN B C 1 ATOM 11076 O O . GLN B 2 505 ? -48.216 20.169 -2.359 1.00 169.07 ? 505 GLN B O 1 ATOM 11077 C CB . GLN B 2 505 ? -46.798 17.449 -2.170 1.00 173.96 ? 505 GLN B CB 1 ATOM 11078 C CG . GLN B 2 505 ? -46.712 15.949 -2.368 1.00 177.73 ? 505 GLN B CG 1 ATOM 11079 C CD . GLN B 2 505 ? -45.484 15.534 -3.153 1.00 183.65 ? 505 GLN B CD 1 ATOM 11080 O OE1 . GLN B 2 505 ? -44.738 16.377 -3.651 1.00 187.86 ? 505 GLN B OE1 1 ATOM 11081 N NE2 . GLN B 2 505 ? -45.268 14.229 -3.267 1.00 184.47 ? 505 GLN B NE2 1 ATOM 11082 N N . CYS B 2 506 ? -47.957 19.865 -0.140 1.00 160.90 ? 506 CYS B N 1 ATOM 11083 C CA . CYS B 2 506 ? -48.147 21.264 0.204 1.00 163.09 ? 506 CYS B CA 1 ATOM 11084 C C . CYS B 2 506 ? -46.931 22.098 -0.117 1.00 170.41 ? 506 CYS B C 1 ATOM 11085 O O . CYS B 2 506 ? -45.852 21.852 0.408 1.00 171.90 ? 506 CYS B O 1 ATOM 11086 C CB . CYS B 2 506 ? -48.481 21.408 1.690 1.00 157.06 ? 506 CYS B CB 1 ATOM 11087 S SG . CYS B 2 506 ? -49.605 22.772 2.056 1.00 136.61 ? 506 CYS B SG 1 ATOM 11088 N N . VAL B 2 507 ? -47.091 23.099 -0.972 1.00 178.99 ? 507 VAL B N 1 ATOM 11089 C CA . VAL B 2 507 ? -45.959 23.975 -1.244 1.00 181.36 ? 507 VAL B CA 1 ATOM 11090 C C . VAL B 2 507 ? -46.231 25.333 -0.576 1.00 183.02 ? 507 VAL B C 1 ATOM 11091 O O . VAL B 2 507 ? -47.128 26.083 -0.974 1.00 179.00 ? 507 VAL B O 1 ATOM 11092 C CB . VAL B 2 507 ? -45.696 24.066 -2.779 1.00 181.19 ? 507 VAL B CB 1 ATOM 11093 C CG1 . VAL B 2 507 ? -45.987 22.730 -3.399 1.00 186.43 ? 507 VAL B CG1 1 ATOM 11094 C CG2 . VAL B 2 507 ? -46.546 25.097 -3.482 1.00 184.81 ? 507 VAL B CG2 1 ATOM 11095 N N . CYS B 2 508 ? -45.534 25.606 0.524 1.00 186.66 ? 508 CYS B N 1 ATOM 11096 C CA . CYS B 2 508 ? -45.542 26.953 1.059 1.00 189.60 ? 508 CYS B CA 1 ATOM 11097 C C . CYS B 2 508 ? -44.171 27.458 1.442 1.00 190.52 ? 508 CYS B C 1 ATOM 11098 O O . CYS B 2 508 ? -43.836 27.476 2.628 1.00 196.02 ? 508 CYS B O 1 ATOM 11099 C CB . CYS B 2 508 ? -46.370 26.933 2.321 1.00 185.81 ? 508 CYS B CB 1 ATOM 11100 S SG . CYS B 2 508 ? -46.025 25.479 3.370 1.00 150.29 ? 508 CYS B SG 1 ATOM 11101 N N . HIS B 2 509 ? -43.443 28.058 0.521 1.00 190.69 ? 509 HIS B N 1 ATOM 11102 C CA . HIS B 2 509 ? -42.081 28.407 0.884 1.00 191.80 ? 509 HIS B CA 1 ATOM 11103 C C . HIS B 2 509 ? -42.070 29.823 1.431 1.00 192.77 ? 509 HIS B C 1 ATOM 11104 O O . HIS B 2 509 ? -41.491 30.083 2.481 1.00 187.03 ? 509 HIS B O 1 ATOM 11105 C CB . HIS B 2 509 ? -41.107 28.244 -0.287 1.00 200.55 ? 509 HIS B CB 1 ATOM 11106 C CG . HIS B 2 509 ? -41.655 27.492 -1.468 1.00 209.24 ? 509 HIS B CG 1 ATOM 11107 N ND1 . HIS B 2 509 ? -42.690 26.580 -1.400 1.00 210.97 ? 509 HIS B ND1 1 ATOM 11108 C CD2 . HIS B 2 509 ? -41.266 27.513 -2.763 1.00 217.08 ? 509 HIS B CD2 1 ATOM 11109 C CE1 . HIS B 2 509 ? -42.931 26.096 -2.606 1.00 218.31 ? 509 HIS B CE1 1 ATOM 11110 N NE2 . HIS B 2 509 ? -42.076 26.643 -3.450 1.00 222.39 ? 509 HIS B NE2 1 ATOM 11111 N N . SER B 2 510 ? -42.711 30.723 0.686 1.00 199.10 ? 510 SER B N 1 ATOM 11112 C CA . SER B 2 510 ? -42.871 32.140 1.030 1.00 198.04 ? 510 SER B CA 1 ATOM 11113 C C . SER B 2 510 ? -41.549 32.916 1.075 1.00 192.94 ? 510 SER B C 1 ATOM 11114 O O . SER B 2 510 ? -41.552 34.147 1.071 1.00 198.39 ? 510 SER B O 1 ATOM 11115 C CB . SER B 2 510 ? -43.603 32.284 2.366 1.00 193.78 ? 510 SER B CB 1 ATOM 11116 O OG . SER B 2 510 ? -43.860 33.646 2.660 1.00 194.55 ? 510 SER B OG 1 ATOM 11117 N N . SER B 2 511 ? -40.429 32.194 1.123 1.00 184.64 ? 511 SER B N 1 ATOM 11118 C CA . SER B 2 511 ? -39.095 32.771 0.944 1.00 189.41 ? 511 SER B CA 1 ATOM 11119 C C . SER B 2 511 ? -38.671 33.775 2.024 1.00 188.86 ? 511 SER B C 1 ATOM 11120 O O . SER B 2 511 ? -37.549 34.279 1.985 1.00 185.67 ? 511 SER B O 1 ATOM 11121 C CB . SER B 2 511 ? -38.991 33.437 -0.433 1.00 194.03 ? 511 SER B CB 1 ATOM 11122 O OG . SER B 2 511 ? -39.727 34.647 -0.475 1.00 192.55 ? 511 SER B OG 1 ATOM 11123 N N . ASP B 2 512 ? -39.552 34.080 2.975 1.00 186.42 ? 512 ASP B N 1 ATOM 11124 C CA . ASP B 2 512 ? -39.284 35.179 3.901 1.00 179.23 ? 512 ASP B CA 1 ATOM 11125 C C . ASP B 2 512 ? -38.335 34.801 5.042 1.00 168.05 ? 512 ASP B C 1 ATOM 11126 O O . ASP B 2 512 ? -38.659 33.964 5.885 1.00 158.10 ? 512 ASP B O 1 ATOM 11127 C CB . ASP B 2 512 ? -40.601 35.704 4.483 1.00 175.33 ? 512 ASP B CB 1 ATOM 11128 C CG . ASP B 2 512 ? -41.404 34.623 5.185 1.00 156.09 ? 512 ASP B CG 1 ATOM 11129 O OD1 . ASP B 2 512 ? -41.919 34.886 6.292 1.00 148.45 ? 512 ASP B OD1 1 ATOM 11130 O OD2 . ASP B 2 512 ? -41.516 33.509 4.632 1.00 153.72 ? 512 ASP B OD2 1 ATOM 11131 N N . PHE B 2 513 ? -37.165 35.443 5.038 1.00 166.19 ? 513 PHE B N 1 ATOM 11132 C CA . PHE B 2 513 ? -36.141 35.364 6.091 1.00 149.04 ? 513 PHE B CA 1 ATOM 11133 C C . PHE B 2 513 ? -36.005 33.980 6.727 1.00 142.79 ? 513 PHE B C 1 ATOM 11134 O O . PHE B 2 513 ? -36.195 33.820 7.932 1.00 136.40 ? 513 PHE B O 1 ATOM 11135 C CB . PHE B 2 513 ? -36.388 36.423 7.183 1.00 141.22 ? 513 PHE B CB 1 ATOM 11136 C CG . PHE B 2 513 ? -37.824 36.552 7.623 1.00 143.10 ? 513 PHE B CG 1 ATOM 11137 C CD1 . PHE B 2 513 ? -38.318 35.786 8.667 1.00 133.81 ? 513 PHE B CD1 1 ATOM 11138 C CD2 . PHE B 2 513 ? -38.669 37.467 7.016 1.00 155.64 ? 513 PHE B CD2 1 ATOM 11139 C CE1 . PHE B 2 513 ? -39.631 35.912 9.079 1.00 133.01 ? 513 PHE B CE1 1 ATOM 11140 C CE2 . PHE B 2 513 ? -39.984 37.598 7.424 1.00 155.99 ? 513 PHE B CE2 1 ATOM 11141 C CZ . PHE B 2 513 ? -40.465 36.819 8.457 1.00 145.03 ? 513 PHE B CZ 1 ATOM 11142 N N . GLY B 2 514 ? -35.657 32.985 5.920 1.00 153.43 ? 514 GLY B N 1 ATOM 11143 C CA . GLY B 2 514 ? -35.489 31.637 6.429 1.00 152.40 ? 514 GLY B CA 1 ATOM 11144 C C . GLY B 2 514 ? -35.944 30.587 5.436 1.00 153.19 ? 514 GLY B C 1 ATOM 11145 O O . GLY B 2 514 ? -36.169 30.881 4.262 1.00 152.56 ? 514 GLY B O 1 ATOM 11146 N N . LYS B 2 515 ? -36.087 29.357 5.916 1.00 153.15 ? 515 LYS B N 1 ATOM 11147 C CA . LYS B 2 515 ? -36.666 28.285 5.116 1.00 154.12 ? 515 LYS B CA 1 ATOM 11148 C C . LYS B 2 515 ? -37.817 27.630 5.875 1.00 157.73 ? 515 LYS B C 1 ATOM 11149 O O . LYS B 2 515 ? -37.691 27.300 7.055 1.00 156.43 ? 515 LYS B O 1 ATOM 11150 C CB . LYS B 2 515 ? -35.604 27.247 4.740 1.00 151.69 ? 515 LYS B CB 1 ATOM 11151 C CG . LYS B 2 515 ? -34.846 26.654 5.918 1.00 151.11 ? 515 LYS B CG 1 ATOM 11152 C CD . LYS B 2 515 ? -33.881 25.574 5.458 1.00 154.33 ? 515 LYS B CD 1 ATOM 11153 C CE . LYS B 2 515 ? -33.152 24.945 6.634 1.00 152.12 ? 515 LYS B CE 1 ATOM 11154 N NZ . LYS B 2 515 ? -32.218 23.872 6.196 1.00 149.25 ? 515 LYS B NZ 1 ATOM 11155 N N . ILE B 2 516 ? -38.944 27.457 5.194 1.00 160.08 ? 516 ILE B N 1 ATOM 11156 C CA . ILE B 2 516 ? -40.129 26.877 5.813 1.00 145.78 ? 516 ILE B CA 1 ATOM 11157 C C . ILE B 2 516 ? -40.417 25.497 5.236 1.00 143.10 ? 516 ILE B C 1 ATOM 11158 O O . ILE B 2 516 ? -40.464 25.326 4.018 1.00 149.80 ? 516 ILE B O 1 ATOM 11159 C CB . ILE B 2 516 ? -41.361 27.778 5.618 1.00 141.79 ? 516 ILE B CB 1 ATOM 11160 C CG1 . ILE B 2 516 ? -41.027 29.220 6.004 1.00 152.84 ? 516 ILE B CG1 1 ATOM 11161 C CG2 . ILE B 2 516 ? -42.540 27.255 6.424 1.00 136.69 ? 516 ILE B CG2 1 ATOM 11162 C CD1 . ILE B 2 516 ? -42.152 30.198 5.766 1.00 161.56 ? 516 ILE B CD1 1 ATOM 11163 N N . THR B 2 517 ? -40.606 24.513 6.108 1.00 134.89 ? 517 THR B N 1 ATOM 11164 C CA . THR B 2 517 ? -40.877 23.158 5.647 1.00 137.75 ? 517 THR B CA 1 ATOM 11165 C C . THR B 2 517 ? -41.883 22.414 6.518 1.00 134.90 ? 517 THR B C 1 ATOM 11166 O O . THR B 2 517 ? -42.327 22.912 7.553 1.00 128.96 ? 517 THR B O 1 ATOM 11167 C CB . THR B 2 517 ? -39.580 22.328 5.588 1.00 143.27 ? 517 THR B CB 1 ATOM 11168 O OG1 . THR B 2 517 ? -39.894 20.970 5.256 1.00 147.16 ? 517 THR B OG1 1 ATOM 11169 C CG2 . THR B 2 517 ? -38.867 22.362 6.932 1.00 141.45 ? 517 THR B CG2 1 ATOM 11170 N N . GLY B 2 518 ? -42.239 21.215 6.071 1.00 135.81 ? 518 GLY B N 1 ATOM 11171 C CA . GLY B 2 518 ? -43.125 20.327 6.799 1.00 128.11 ? 518 GLY B CA 1 ATOM 11172 C C . GLY B 2 518 ? -43.937 19.542 5.789 1.00 125.41 ? 518 GLY B C 1 ATOM 11173 O O . GLY B 2 518 ? -43.751 19.710 4.584 1.00 128.99 ? 518 GLY B O 1 ATOM 11174 N N . LYS B 2 519 ? -44.839 18.689 6.261 1.00 122.37 ? 519 LYS B N 1 ATOM 11175 C CA . LYS B 2 519 ? -45.833 18.108 5.369 1.00 125.03 ? 519 LYS B CA 1 ATOM 11176 C C . LYS B 2 519 ? -46.960 19.113 5.190 1.00 126.29 ? 519 LYS B C 1 ATOM 11177 O O . LYS B 2 519 ? -47.436 19.351 4.080 1.00 129.22 ? 519 LYS B O 1 ATOM 11178 C CB . LYS B 2 519 ? -46.371 16.786 5.916 1.00 124.89 ? 519 LYS B CB 1 ATOM 11179 C CG . LYS B 2 519 ? -47.405 16.128 5.015 1.00 123.45 ? 519 LYS B CG 1 ATOM 11180 C CD . LYS B 2 519 ? -47.843 14.779 5.557 1.00 120.05 ? 519 LYS B CD 1 ATOM 11181 C CE . LYS B 2 519 ? -48.805 14.093 4.601 1.00 124.13 ? 519 LYS B CE 1 ATOM 11182 N NZ . LYS B 2 519 ? -49.188 12.734 5.075 1.00 132.57 ? 519 LYS B NZ 1 ATOM 11183 N N . TYR B 2 520 ? -47.377 19.698 6.307 1.00 125.18 ? 520 TYR B N 1 ATOM 11184 C CA . TYR B 2 520 ? -48.380 20.752 6.312 1.00 128.01 ? 520 TYR B CA 1 ATOM 11185 C C . TYR B 2 520 ? -47.697 22.112 6.383 1.00 130.61 ? 520 TYR B C 1 ATOM 11186 O O . TYR B 2 520 ? -48.363 23.145 6.461 1.00 132.25 ? 520 TYR B O 1 ATOM 11187 C CB . TYR B 2 520 ? -49.347 20.574 7.485 1.00 116.33 ? 520 TYR B CB 1 ATOM 11188 C CG . TYR B 2 520 ? -49.945 19.187 7.589 1.00 127.79 ? 520 TYR B CG 1 ATOM 11189 C CD1 . TYR B 2 520 ? -50.300 18.655 8.822 1.00 130.41 ? 520 TYR B CD1 1 ATOM 11190 C CD2 . TYR B 2 520 ? -50.163 18.411 6.455 1.00 137.14 ? 520 TYR B CD2 1 ATOM 11191 C CE1 . TYR B 2 520 ? -50.847 17.390 8.925 1.00 126.85 ? 520 TYR B CE1 1 ATOM 11192 C CE2 . TYR B 2 520 ? -50.709 17.145 6.549 1.00 131.64 ? 520 TYR B CE2 1 ATOM 11193 C CZ . TYR B 2 520 ? -51.050 16.640 7.785 1.00 121.30 ? 520 TYR B CZ 1 ATOM 11194 O OH . TYR B 2 520 ? -51.595 15.381 7.883 1.00 116.39 ? 520 TYR B OH 1 ATOM 11195 N N . CYS B 2 521 ? -46.365 22.089 6.369 1.00 135.62 ? 521 CYS B N 1 ATOM 11196 C CA . CYS B 2 521 ? -45.537 23.287 6.503 1.00 138.34 ? 521 CYS B CA 1 ATOM 11197 C C . CYS B 2 521 ? -45.750 23.946 7.865 1.00 139.31 ? 521 CYS B C 1 ATOM 11198 O O . CYS B 2 521 ? -45.860 25.168 7.963 1.00 135.58 ? 521 CYS B O 1 ATOM 11199 C CB . CYS B 2 521 ? -45.831 24.285 5.374 1.00 135.98 ? 521 CYS B CB 1 ATOM 11200 S SG . CYS B 2 521 ? -44.402 24.791 4.391 1.00 166.16 ? 521 CYS B SG 1 ATOM 11201 N N . GLU B 2 522 ? -45.801 23.128 8.913 1.00 138.62 ? 522 GLU B N 1 ATOM 11202 C CA . GLU B 2 522 ? -46.014 23.624 10.270 1.00 133.82 ? 522 GLU B CA 1 ATOM 11203 C C . GLU B 2 522 ? -44.700 24.006 10.944 1.00 129.14 ? 522 GLU B C 1 ATOM 11204 O O . GLU B 2 522 ? -44.696 24.615 12.014 1.00 125.30 ? 522 GLU B O 1 ATOM 11205 C CB . GLU B 2 522 ? -46.746 22.579 11.119 1.00 139.50 ? 522 GLU B CB 1 ATOM 11206 C CG . GLU B 2 522 ? -45.947 21.308 11.396 1.00 145.16 ? 522 GLU B CG 1 ATOM 11207 C CD . GLU B 2 522 ? -45.955 20.335 10.230 1.00 145.38 ? 522 GLU B CD 1 ATOM 11208 O OE1 . GLU B 2 522 ? -46.587 20.643 9.198 1.00 154.75 ? 522 GLU B OE1 1 ATOM 11209 O OE2 . GLU B 2 522 ? -45.331 19.259 10.347 1.00 133.13 ? 522 GLU B OE2 1 ATOM 11210 N N . CYS B 2 523 ? -43.586 23.646 10.316 1.00 133.53 ? 523 CYS B N 1 ATOM 11211 C CA . CYS B 2 523 ? -42.270 23.957 10.863 1.00 135.69 ? 523 CYS B CA 1 ATOM 11212 C C . CYS B 2 523 ? -41.732 25.260 10.284 1.00 146.14 ? 523 CYS B C 1 ATOM 11213 O O . CYS B 2 523 ? -41.430 25.346 9.093 1.00 150.90 ? 523 CYS B O 1 ATOM 11214 C CB . CYS B 2 523 ? -41.290 22.814 10.593 1.00 138.28 ? 523 CYS B CB 1 ATOM 11215 S SG . CYS B 2 523 ? -41.707 21.266 11.428 1.00 144.59 ? 523 CYS B SG 1 ATOM 11216 N N . ASP B 2 524 ? -41.613 26.271 11.138 1.00 151.93 ? 524 ASP B N 1 ATOM 11217 C CA . ASP B 2 524 ? -41.160 27.591 10.714 1.00 149.07 ? 524 ASP B CA 1 ATOM 11218 C C . ASP B 2 524 ? -39.646 27.655 10.535 1.00 146.01 ? 524 ASP B C 1 ATOM 11219 O O . ASP B 2 524 ? -39.160 28.227 9.561 1.00 154.35 ? 524 ASP B O 1 ATOM 11220 C CB . ASP B 2 524 ? -41.615 28.649 11.722 1.00 140.73 ? 524 ASP B CB 1 ATOM 11221 C CG . ASP B 2 524 ? -41.442 28.198 13.161 1.00 134.79 ? 524 ASP B CG 1 ATOM 11222 O OD1 . ASP B 2 524 ? -40.475 27.460 13.444 1.00 129.55 ? 524 ASP B OD1 1 ATOM 11223 O OD2 . ASP B 2 524 ? -42.276 28.577 14.009 1.00 136.39 ? 524 ASP B OD2 1 ATOM 11224 N N . ASP B 2 525 ? -38.921 27.068 11.488 1.00 134.40 ? 525 ASP B N 1 ATOM 11225 C CA . ASP B 2 525 ? -37.452 27.028 11.510 1.00 134.00 ? 525 ASP B CA 1 ATOM 11226 C C . ASP B 2 525 ? -36.817 28.394 11.812 1.00 129.41 ? 525 ASP B C 1 ATOM 11227 O O . ASP B 2 525 ? -35.630 28.470 12.134 1.00 127.42 ? 525 ASP B O 1 ATOM 11228 C CB . ASP B 2 525 ? -36.908 26.466 10.187 1.00 144.55 ? 525 ASP B CB 1 ATOM 11229 C CG . ASP B 2 525 ? -35.394 26.359 10.170 1.00 142.55 ? 525 ASP B CG 1 ATOM 11230 O OD1 . ASP B 2 525 ? -34.862 25.328 10.634 1.00 140.67 ? 525 ASP B OD1 1 ATOM 11231 O OD2 . ASP B 2 525 ? -34.737 27.306 9.689 1.00 138.54 ? 525 ASP B OD2 1 ATOM 11232 N N . PHE B 2 526 ? -37.601 29.468 11.745 1.00 130.03 ? 526 PHE B N 1 ATOM 11233 C CA . PHE B 2 526 ? -37.114 30.769 12.201 1.00 124.85 ? 526 PHE B CA 1 ATOM 11234 C C . PHE B 2 526 ? -37.810 31.159 13.504 1.00 122.61 ? 526 PHE B C 1 ATOM 11235 O O . PHE B 2 526 ? -37.148 31.352 14.523 1.00 120.79 ? 526 PHE B O 1 ATOM 11236 C CB . PHE B 2 526 ? -37.274 31.865 11.127 1.00 127.07 ? 526 PHE B CB 1 ATOM 11237 C CG . PHE B 2 526 ? -38.634 31.929 10.483 1.00 137.39 ? 526 PHE B CG 1 ATOM 11238 C CD1 . PHE B 2 526 ? -39.604 32.801 10.953 1.00 140.77 ? 526 PHE B CD1 1 ATOM 11239 C CD2 . PHE B 2 526 ? -38.922 31.159 9.371 1.00 139.17 ? 526 PHE B CD2 1 ATOM 11240 C CE1 . PHE B 2 526 ? -40.847 32.869 10.353 1.00 139.22 ? 526 PHE B CE1 1 ATOM 11241 C CE2 . PHE B 2 526 ? -40.162 31.224 8.766 1.00 137.72 ? 526 PHE B CE2 1 ATOM 11242 C CZ . PHE B 2 526 ? -41.125 32.081 9.256 1.00 138.30 ? 526 PHE B CZ 1 ATOM 11243 N N . SER B 2 527 ? -39.133 31.289 13.470 1.00 128.77 ? 527 SER B N 1 ATOM 11244 C CA . SER B 2 527 ? -39.898 31.609 14.670 1.00 132.20 ? 527 SER B CA 1 ATOM 11245 C C . SER B 2 527 ? -39.651 30.565 15.752 1.00 122.04 ? 527 SER B C 1 ATOM 11246 O O . SER B 2 527 ? -39.842 29.370 15.534 1.00 119.73 ? 527 SER B O 1 ATOM 11247 C CB . SER B 2 527 ? -41.392 31.699 14.349 1.00 143.14 ? 527 SER B CB 1 ATOM 11248 O OG . SER B 2 527 ? -42.148 31.975 15.515 1.00 148.73 ? 527 SER B OG 1 ATOM 11249 N N . CYS B 2 528 ? -39.227 31.029 16.922 1.00 125.84 ? 528 CYS B N 1 ATOM 11250 C CA . CYS B 2 528 ? -38.844 30.133 18.004 1.00 127.85 ? 528 CYS B CA 1 ATOM 11251 C C . CYS B 2 528 ? -38.954 30.845 19.346 1.00 140.72 ? 528 CYS B C 1 ATOM 11252 O O . CYS B 2 528 ? -39.474 31.958 19.427 1.00 157.32 ? 528 CYS B O 1 ATOM 11253 C CB . CYS B 2 528 ? -37.420 29.616 17.790 1.00 119.16 ? 528 CYS B CB 1 ATOM 11254 S SG . CYS B 2 528 ? -37.192 27.854 18.127 1.00 142.63 ? 528 CYS B SG 1 ATOM 11255 N N . VAL B 2 529 ? -38.464 30.199 20.398 1.00 131.80 ? 529 VAL B N 1 ATOM 11256 C CA . VAL B 2 529 ? -38.481 30.791 21.729 1.00 123.07 ? 529 VAL B CA 1 ATOM 11257 C C . VAL B 2 529 ? -37.188 31.567 21.981 1.00 120.39 ? 529 VAL B C 1 ATOM 11258 O O . VAL B 2 529 ? -36.104 31.135 21.586 1.00 120.13 ? 529 VAL B O 1 ATOM 11259 C CB . VAL B 2 529 ? -38.684 29.711 22.822 1.00 110.53 ? 529 VAL B CB 1 ATOM 11260 C CG1 . VAL B 2 529 ? -37.608 28.639 22.732 1.00 114.01 ? 529 VAL B CG1 1 ATOM 11261 C CG2 . VAL B 2 529 ? -38.716 30.338 24.206 1.00 95.55 ? 529 VAL B CG2 1 ATOM 11262 N N . ARG B 2 530 ? -37.311 32.727 22.618 1.00 124.50 ? 530 ARG B N 1 ATOM 11263 C CA . ARG B 2 530 ? -36.156 33.566 22.915 1.00 118.69 ? 530 ARG B CA 1 ATOM 11264 C C . ARG B 2 530 ? -36.025 33.802 24.417 1.00 116.00 ? 530 ARG B C 1 ATOM 11265 O O . ARG B 2 530 ? -37.022 33.804 25.139 1.00 120.93 ? 530 ARG B O 1 ATOM 11266 C CB . ARG B 2 530 ? -36.262 34.901 22.177 1.00 120.24 ? 530 ARG B CB 1 ATOM 11267 C CG . ARG B 2 530 ? -36.483 34.766 20.677 1.00 119.28 ? 530 ARG B CG 1 ATOM 11268 C CD . ARG B 2 530 ? -36.375 36.106 19.961 1.00 119.76 ? 530 ARG B CD 1 ATOM 11269 N NE . ARG B 2 530 ? -37.370 37.070 20.422 1.00 134.76 ? 530 ARG B NE 1 ATOM 11270 C CZ . ARG B 2 530 ? -37.117 38.056 21.278 1.00 151.92 ? 530 ARG B CZ 1 ATOM 11271 N NH1 . ARG B 2 530 ? -35.896 38.213 21.769 1.00 148.49 ? 530 ARG B NH1 1 ATOM 11272 N NH2 . ARG B 2 530 ? -38.085 38.885 21.641 1.00 165.86 ? 530 ARG B NH2 1 ATOM 11273 N N . TYR B 2 531 ? -34.796 34.003 24.884 1.00 115.29 ? 531 TYR B N 1 ATOM 11274 C CA . TYR B 2 531 ? -34.558 34.242 26.303 1.00 125.98 ? 531 TYR B CA 1 ATOM 11275 C C . TYR B 2 531 ? -34.311 35.723 26.573 1.00 140.53 ? 531 TYR B C 1 ATOM 11276 O O . TYR B 2 531 ? -35.202 36.426 27.052 1.00 150.52 ? 531 TYR B O 1 ATOM 11277 C CB . TYR B 2 531 ? -33.375 33.397 26.788 1.00 114.16 ? 531 TYR B CB 1 ATOM 11278 C CG . TYR B 2 531 ? -32.840 33.772 28.153 1.00 107.87 ? 531 TYR B CG 1 ATOM 11279 C CD1 . TYR B 2 531 ? -33.652 33.729 29.278 1.00 113.94 ? 531 TYR B CD1 1 ATOM 11280 C CD2 . TYR B 2 531 ? -31.513 34.149 28.317 1.00 107.29 ? 531 TYR B CD2 1 ATOM 11281 C CE1 . TYR B 2 531 ? -33.162 34.067 30.526 1.00 122.37 ? 531 TYR B CE1 1 ATOM 11282 C CE2 . TYR B 2 531 ? -31.013 34.485 29.561 1.00 115.87 ? 531 TYR B CE2 1 ATOM 11283 C CZ . TYR B 2 531 ? -31.842 34.443 30.661 1.00 121.67 ? 531 TYR B CZ 1 ATOM 11284 O OH . TYR B 2 531 ? -31.348 34.778 31.902 1.00 115.86 ? 531 TYR B OH 1 ATOM 11285 N N . LYS B 2 532 ? -33.109 36.200 26.266 1.00 130.97 ? 532 LYS B N 1 ATOM 11286 C CA . LYS B 2 532 ? -32.842 37.633 26.300 1.00 119.01 ? 532 LYS B CA 1 ATOM 11287 C C . LYS B 2 532 ? -32.311 38.121 24.957 1.00 117.40 ? 532 LYS B C 1 ATOM 11288 O O . LYS B 2 532 ? -31.173 37.829 24.591 1.00 114.76 ? 532 LYS B O 1 ATOM 11289 C CB . LYS B 2 532 ? -31.843 37.966 27.411 1.00 110.72 ? 532 LYS B CB 1 ATOM 11290 C CG . LYS B 2 532 ? -32.335 37.646 28.814 1.00 108.17 ? 532 LYS B CG 1 ATOM 11291 C CD . LYS B 2 532 ? -33.246 38.736 29.356 1.00 114.26 ? 532 LYS B CD 1 ATOM 11292 C CE . LYS B 2 532 ? -32.470 40.017 29.624 1.00 126.94 ? 532 LYS B CE 1 ATOM 11293 N NZ . LYS B 2 532 ? -33.323 41.064 30.251 1.00 134.29 ? 532 LYS B NZ 1 ATOM 11294 N N . GLY B 2 533 ? -33.135 38.863 24.225 1.00 125.07 ? 533 GLY B N 1 ATOM 11295 C CA . GLY B 2 533 ? -32.687 39.556 23.029 1.00 135.87 ? 533 GLY B CA 1 ATOM 11296 C C . GLY B 2 533 ? -32.319 38.671 21.851 1.00 135.31 ? 533 GLY B C 1 ATOM 11297 O O . GLY B 2 533 ? -32.077 39.169 20.751 1.00 152.12 ? 533 GLY B O 1 ATOM 11298 N N . GLU B 2 534 ? -32.283 37.360 22.070 1.00 116.00 ? 534 GLU B N 1 ATOM 11299 C CA . GLU B 2 534 ? -31.794 36.428 21.059 1.00 113.50 ? 534 GLU B CA 1 ATOM 11300 C C . GLU B 2 534 ? -32.575 35.120 21.047 1.00 122.85 ? 534 GLU B C 1 ATOM 11301 O O . GLU B 2 534 ? -33.093 34.685 22.075 1.00 127.86 ? 534 GLU B O 1 ATOM 11302 C CB . GLU B 2 534 ? -30.308 36.129 21.282 1.00 113.02 ? 534 GLU B CB 1 ATOM 11303 C CG . GLU B 2 534 ? -29.367 37.265 20.914 1.00 120.85 ? 534 GLU B CG 1 ATOM 11304 C CD . GLU B 2 534 ? -27.917 36.937 21.214 1.00 115.25 ? 534 GLU B CD 1 ATOM 11305 O OE1 . GLU B 2 534 ? -27.630 36.476 22.339 1.00 113.67 ? 534 GLU B OE1 1 ATOM 11306 O OE2 . GLU B 2 534 ? -27.065 37.135 20.323 1.00 111.60 ? 534 GLU B OE2 1 ATOM 11307 N N . MET B 2 535 ? -32.642 34.494 19.876 1.00 127.29 ? 535 MET B N 1 ATOM 11308 C CA . MET B 2 535 ? -33.317 33.212 19.722 1.00 122.06 ? 535 MET B CA 1 ATOM 11309 C C . MET B 2 535 ? -32.461 32.074 20.268 1.00 108.79 ? 535 MET B C 1 ATOM 11310 O O . MET B 2 535 ? -31.311 31.905 19.858 1.00 107.32 ? 535 MET B O 1 ATOM 11311 C CB . MET B 2 535 ? -33.653 32.961 18.252 1.00 126.31 ? 535 MET B CB 1 ATOM 11312 C CG . MET B 2 535 ? -34.329 31.630 17.988 1.00 118.72 ? 535 MET B CG 1 ATOM 11313 S SD . MET B 2 535 ? -34.527 31.306 16.228 1.00 106.59 ? 535 MET B SD 1 ATOM 11314 C CE . MET B 2 535 ? -32.821 31.339 15.683 1.00 129.11 ? 535 MET B CE 1 ATOM 11315 N N . CYS B 2 536 ? -33.030 31.307 21.196 1.00 104.84 ? 536 CYS B N 1 ATOM 11316 C CA . CYS B 2 536 ? -32.331 30.208 21.865 1.00 104.26 ? 536 CYS B CA 1 ATOM 11317 C C . CYS B 2 536 ? -31.056 30.691 22.553 1.00 102.34 ? 536 CYS B C 1 ATOM 11318 O O . CYS B 2 536 ? -30.100 29.931 22.708 1.00 103.98 ? 536 CYS B O 1 ATOM 11319 C CB . CYS B 2 536 ? -32.003 29.087 20.873 1.00 105.42 ? 536 CYS B CB 1 ATOM 11320 S SG . CYS B 2 536 ? -33.445 28.223 20.208 1.00 93.69 ? 536 CYS B SG 1 ATOM 11321 N N . SER B 2 537 ? -31.059 31.962 22.949 1.00 108.45 ? 537 SER B N 1 ATOM 11322 C CA . SER B 2 537 ? -29.923 32.610 23.605 1.00 103.53 ? 537 SER B CA 1 ATOM 11323 C C . SER B 2 537 ? -28.668 32.581 22.735 1.00 98.02 ? 537 SER B C 1 ATOM 11324 O O . SER B 2 537 ? -27.551 32.684 23.241 1.00 96.24 ? 537 SER B O 1 ATOM 11325 C CB . SER B 2 537 ? -29.634 31.950 24.957 1.00 96.47 ? 537 SER B CB 1 ATOM 11326 O OG . SER B 2 537 ? -30.819 31.807 25.719 1.00 92.74 ? 537 SER B OG 1 ATOM 11327 N N . GLY B 2 538 ? -28.857 32.438 21.425 1.00 105.59 ? 538 GLY B N 1 ATOM 11328 C CA . GLY B 2 538 ? -27.748 32.390 20.487 1.00 111.67 ? 538 GLY B CA 1 ATOM 11329 C C . GLY B 2 538 ? -26.945 31.104 20.569 1.00 103.58 ? 538 GLY B C 1 ATOM 11330 O O . GLY B 2 538 ? -26.046 30.867 19.762 1.00 105.79 ? 538 GLY B O 1 ATOM 11331 N N . HIS B 2 539 ? -27.271 30.275 21.555 1.00 102.22 ? 539 HIS B N 1 ATOM 11332 C CA . HIS B 2 539 ? -26.526 29.054 21.834 1.00 103.94 ? 539 HIS B CA 1 ATOM 11333 C C . HIS B 2 539 ? -27.152 27.804 21.220 1.00 108.09 ? 539 HIS B C 1 ATOM 11334 O O . HIS B 2 539 ? -26.691 26.693 21.471 1.00 108.56 ? 539 HIS B O 1 ATOM 11335 C CB . HIS B 2 539 ? -26.379 28.872 23.344 1.00 101.28 ? 539 HIS B CB 1 ATOM 11336 C CG . HIS B 2 539 ? -25.545 29.930 23.996 1.00 99.91 ? 539 HIS B CG 1 ATOM 11337 N ND1 . HIS B 2 539 ? -24.645 30.703 23.295 1.00 99.99 ? 539 HIS B ND1 1 ATOM 11338 C CD2 . HIS B 2 539 ? -25.478 30.347 25.282 1.00 101.73 ? 539 HIS B CD2 1 ATOM 11339 C CE1 . HIS B 2 539 ? -24.056 31.549 24.122 1.00 102.91 ? 539 HIS B CE1 1 ATOM 11340 N NE2 . HIS B 2 539 ? -24.544 31.354 25.333 1.00 105.35 ? 539 HIS B NE2 1 ATOM 11341 N N . GLY B 2 540 ? -28.214 27.976 20.440 1.00 112.45 ? 540 GLY B N 1 ATOM 11342 C CA . GLY B 2 540 ? -28.870 26.836 19.827 1.00 117.90 ? 540 GLY B CA 1 ATOM 11343 C C . GLY B 2 540 ? -29.565 27.137 18.515 1.00 125.90 ? 540 GLY B C 1 ATOM 11344 O O . GLY B 2 540 ? -29.887 28.287 18.216 1.00 127.80 ? 540 GLY B O 1 ATOM 11345 N N . GLN B 2 541 ? -29.796 26.090 17.728 1.00 130.28 ? 541 GLN B N 1 ATOM 11346 C CA . GLN B 2 541 ? -30.521 26.215 16.471 1.00 135.50 ? 541 GLN B CA 1 ATOM 11347 C C . GLN B 2 541 ? -32.021 26.145 16.726 1.00 137.87 ? 541 GLN B C 1 ATOM 11348 O O . GLN B 2 541 ? -32.455 25.991 17.867 1.00 145.55 ? 541 GLN B O 1 ATOM 11349 C CB . GLN B 2 541 ? -30.099 25.120 15.490 1.00 134.19 ? 541 GLN B CB 1 ATOM 11350 C CG . GLN B 2 541 ? -28.616 25.114 15.160 1.00 135.81 ? 541 GLN B CG 1 ATOM 11351 C CD . GLN B 2 541 ? -28.229 23.963 14.251 1.00 138.14 ? 541 GLN B CD 1 ATOM 11352 O OE1 . GLN B 2 541 ? -29.044 23.088 13.957 1.00 136.34 ? 541 GLN B OE1 1 ATOM 11353 N NE2 . GLN B 2 541 ? -26.980 23.958 13.801 1.00 144.20 ? 541 GLN B NE2 1 ATOM 11354 N N . CYS B 2 542 ? -32.812 26.257 15.664 1.00 128.46 ? 542 CYS B N 1 ATOM 11355 C CA . CYS B 2 542 ? -34.261 26.180 15.798 1.00 122.79 ? 542 CYS B CA 1 ATOM 11356 C C . CYS B 2 542 ? -34.867 25.243 14.759 1.00 124.40 ? 542 CYS B C 1 ATOM 11357 O O . CYS B 2 542 ? -34.781 25.496 13.557 1.00 127.75 ? 542 CYS B O 1 ATOM 11358 C CB . CYS B 2 542 ? -34.883 27.573 15.679 1.00 125.46 ? 542 CYS B CB 1 ATOM 11359 S SG . CYS B 2 542 ? -36.616 27.662 16.187 1.00 130.34 ? 542 CYS B SG 1 ATOM 11360 N N . SER B 2 543 ? -35.477 24.160 15.230 1.00 122.40 ? 543 SER B N 1 ATOM 11361 C CA . SER B 2 543 ? -36.144 23.213 14.345 1.00 115.45 ? 543 SER B CA 1 ATOM 11362 C C . SER B 2 543 ? -37.620 23.072 14.698 1.00 110.46 ? 543 SER B C 1 ATOM 11363 O O . SER B 2 543 ? -37.961 22.538 15.754 1.00 107.81 ? 543 SER B O 1 ATOM 11364 C CB . SER B 2 543 ? -35.458 21.847 14.406 1.00 114.96 ? 543 SER B CB 1 ATOM 11365 O OG . SER B 2 543 ? -34.116 21.928 13.960 1.00 118.26 ? 543 SER B OG 1 ATOM 11366 N N . CYS B 2 544 ? -38.481 23.550 13.803 1.00 117.98 ? 544 CYS B N 1 ATOM 11367 C CA . CYS B 2 544 ? -39.931 23.442 13.955 1.00 122.85 ? 544 CYS B CA 1 ATOM 11368 C C . CYS B 2 544 ? -40.417 23.970 15.304 1.00 113.79 ? 544 CYS B C 1 ATOM 11369 O O . CYS B 2 544 ? -41.255 23.350 15.959 1.00 110.78 ? 544 CYS B O 1 ATOM 11370 C CB . CYS B 2 544 ? -40.375 21.987 13.769 1.00 121.62 ? 544 CYS B CB 1 ATOM 11371 S SG . CYS B 2 544 ? -42.122 21.777 13.350 1.00 164.79 ? 544 CYS B SG 1 ATOM 11372 N N . GLY B 2 545 ? -39.880 25.114 15.716 1.00 107.44 ? 545 GLY B N 1 ATOM 11373 C CA . GLY B 2 545 ? -40.278 25.735 16.966 1.00 112.67 ? 545 GLY B CA 1 ATOM 11374 C C . GLY B 2 545 ? -39.566 25.166 18.179 1.00 110.05 ? 545 GLY B C 1 ATOM 11375 O O . GLY B 2 545 ? -39.845 25.560 19.312 1.00 112.18 ? 545 GLY B O 1 ATOM 11376 N N . ASP B 2 546 ? -38.644 24.239 17.944 1.00 103.86 ? 546 ASP B N 1 ATOM 11377 C CA . ASP B 2 546 ? -37.883 23.630 19.029 1.00 103.10 ? 546 ASP B CA 1 ATOM 11378 C C . ASP B 2 546 ? -36.405 23.984 18.913 1.00 101.48 ? 546 ASP B C 1 ATOM 11379 O O . ASP B 2 546 ? -35.902 24.226 17.817 1.00 104.83 ? 546 ASP B O 1 ATOM 11380 C CB . ASP B 2 546 ? -38.066 22.111 19.029 1.00 107.97 ? 546 ASP B CB 1 ATOM 11381 C CG . ASP B 2 546 ? -39.511 21.700 19.234 1.00 118.75 ? 546 ASP B CG 1 ATOM 11382 O OD1 . ASP B 2 546 ? -39.948 20.719 18.596 1.00 130.93 ? 546 ASP B OD1 1 ATOM 11383 O OD2 . ASP B 2 546 ? -40.211 22.359 20.032 1.00 117.44 ? 546 ASP B OD2 1 ATOM 11384 N N . CYS B 2 547 ? -35.713 24.013 20.047 1.00 97.63 ? 547 CYS B N 1 ATOM 11385 C CA . CYS B 2 547 ? -34.315 24.426 20.074 1.00 95.73 ? 547 CYS B CA 1 ATOM 11386 C C . CYS B 2 547 ? -33.360 23.253 20.255 1.00 96.93 ? 547 CYS B C 1 ATOM 11387 O O . CYS B 2 547 ? -33.496 22.464 21.190 1.00 96.55 ? 547 CYS B O 1 ATOM 11388 C CB . CYS B 2 547 ? -34.087 25.451 21.188 1.00 93.16 ? 547 CYS B CB 1 ATOM 11389 S SG . CYS B 2 547 ? -34.923 27.031 20.931 1.00 136.81 ? 547 CYS B SG 1 ATOM 11390 N N . LEU B 2 548 ? -32.393 23.146 19.351 1.00 99.21 ? 548 LEU B N 1 ATOM 11391 C CA . LEU B 2 548 ? -31.330 22.159 19.479 1.00 102.64 ? 548 LEU B CA 1 ATOM 11392 C C . LEU B 2 548 ? -30.052 22.861 19.918 1.00 102.39 ? 548 LEU B C 1 ATOM 11393 O O . LEU B 2 548 ? -29.437 23.596 19.145 1.00 101.97 ? 548 LEU B O 1 ATOM 11394 C CB . LEU B 2 548 ? -31.120 21.413 18.160 1.00 107.15 ? 548 LEU B CB 1 ATOM 11395 C CG . LEU B 2 548 ? -32.364 20.720 17.599 1.00 106.13 ? 548 LEU B CG 1 ATOM 11396 C CD1 . LEU B 2 548 ? -32.042 19.983 16.308 1.00 111.29 ? 548 LEU B CD1 1 ATOM 11397 C CD2 . LEU B 2 548 ? -32.962 19.773 18.629 1.00 98.81 ? 548 LEU B CD2 1 ATOM 11398 N N . CYS B 2 549 ? -29.654 22.622 21.163 1.00 100.83 ? 549 CYS B N 1 ATOM 11399 C CA . CYS B 2 549 ? -28.586 23.394 21.788 1.00 100.66 ? 549 CYS B CA 1 ATOM 11400 C C . CYS B 2 549 ? -27.193 22.992 21.318 1.00 104.54 ? 549 CYS B C 1 ATOM 11401 O O . CYS B 2 549 ? -26.913 21.814 21.093 1.00 103.51 ? 549 CYS B O 1 ATOM 11402 C CB . CYS B 2 549 ? -28.669 23.261 23.310 1.00 97.64 ? 549 CYS B CB 1 ATOM 11403 S SG . CYS B 2 549 ? -30.206 23.880 24.032 1.00 105.41 ? 549 CYS B SG 1 ATOM 11404 N N . ASP B 2 550 ? -26.325 23.988 21.176 1.00 105.32 ? 550 ASP B N 1 ATOM 11405 C CA . ASP B 2 550 ? -24.922 23.757 20.856 1.00 105.57 ? 550 ASP B CA 1 ATOM 11406 C C . ASP B 2 550 ? -24.223 23.100 22.039 1.00 98.66 ? 550 ASP B C 1 ATOM 11407 O O . ASP B 2 550 ? -24.737 23.118 23.158 1.00 99.37 ? 550 ASP B O 1 ATOM 11408 C CB . ASP B 2 550 ? -24.219 25.063 20.481 1.00 106.37 ? 550 ASP B CB 1 ATOM 11409 C CG . ASP B 2 550 ? -24.832 25.726 19.263 1.00 107.90 ? 550 ASP B CG 1 ATOM 11410 O OD1 . ASP B 2 550 ? -25.376 25.005 18.401 1.00 113.43 ? 550 ASP B OD1 1 ATOM 11411 O OD2 . ASP B 2 550 ? -24.770 26.970 19.168 1.00 106.30 ? 550 ASP B OD2 1 ATOM 11412 N N . SER B 2 551 ? -23.059 22.514 21.777 1.00 95.81 ? 551 SER B N 1 ATOM 11413 C CA . SER B 2 551 ? -22.303 21.782 22.789 1.00 92.87 ? 551 SER B CA 1 ATOM 11414 C C . SER B 2 551 ? -22.068 22.610 24.050 1.00 92.83 ? 551 SER B C 1 ATOM 11415 O O . SER B 2 551 ? -21.879 23.825 23.978 1.00 99.68 ? 551 SER B O 1 ATOM 11416 C CB . SER B 2 551 ? -20.962 21.323 22.213 1.00 92.69 ? 551 SER B CB 1 ATOM 11417 O OG . SER B 2 551 ? -21.153 20.517 21.064 1.00 101.97 ? 551 SER B OG 1 ATOM 11418 N N . ASP B 2 552 ? -22.111 21.934 25.196 1.00 92.53 ? 552 ASP B N 1 ATOM 11419 C CA . ASP B 2 552 ? -21.949 22.549 26.515 1.00 91.83 ? 552 ASP B CA 1 ATOM 11420 C C . ASP B 2 552 ? -23.075 23.527 26.846 1.00 94.11 ? 552 ASP B C 1 ATOM 11421 O O . ASP B 2 552 ? -22.886 24.461 27.624 1.00 94.54 ? 552 ASP B O 1 ATOM 11422 C CB . ASP B 2 552 ? -20.594 23.258 26.623 1.00 97.23 ? 552 ASP B CB 1 ATOM 11423 C CG . ASP B 2 552 ? -19.427 22.327 26.364 1.00 109.18 ? 552 ASP B CG 1 ATOM 11424 O OD1 . ASP B 2 552 ? -18.960 22.263 25.207 1.00 101.51 ? 552 ASP B OD1 1 ATOM 11425 O OD2 . ASP B 2 552 ? -18.976 21.658 27.317 1.00 127.44 ? 552 ASP B OD2 1 ATOM 11426 N N . TRP B 2 553 ? -24.246 23.304 26.258 1.00 96.88 ? 553 TRP B N 1 ATOM 11427 C CA . TRP B 2 553 ? -25.430 24.094 26.581 1.00 100.55 ? 553 TRP B CA 1 ATOM 11428 C C . TRP B 2 553 ? -26.676 23.214 26.604 1.00 103.06 ? 553 TRP B C 1 ATOM 11429 O O . TRP B 2 553 ? -26.854 22.355 25.742 1.00 109.33 ? 553 TRP B O 1 ATOM 11430 C CB . TRP B 2 553 ? -25.612 25.239 25.582 1.00 98.15 ? 553 TRP B CB 1 ATOM 11431 C CG . TRP B 2 553 ? -24.530 26.273 25.648 1.00 96.32 ? 553 TRP B CG 1 ATOM 11432 C CD1 . TRP B 2 553 ? -23.444 26.376 24.829 1.00 109.99 ? 553 TRP B CD1 1 ATOM 11433 C CD2 . TRP B 2 553 ? -24.425 27.348 26.590 1.00 94.60 ? 553 TRP B CD2 1 ATOM 11434 N NE1 . TRP B 2 553 ? -22.672 27.450 25.199 1.00 108.05 ? 553 TRP B NE1 1 ATOM 11435 C CE2 . TRP B 2 553 ? -23.252 28.063 26.278 1.00 94.13 ? 553 TRP B CE2 1 ATOM 11436 C CE3 . TRP B 2 553 ? -25.210 27.776 27.665 1.00 98.37 ? 553 TRP B CE3 1 ATOM 11437 C CZ2 . TRP B 2 553 ? -22.843 29.181 27.003 1.00 92.36 ? 553 TRP B CZ2 1 ATOM 11438 C CZ3 . TRP B 2 553 ? -24.804 28.887 28.383 1.00 92.84 ? 553 TRP B CZ3 1 ATOM 11439 C CH2 . TRP B 2 553 ? -23.632 29.577 28.049 1.00 91.83 ? 553 TRP B CH2 1 ATOM 11440 N N . THR B 2 554 ? -27.529 23.425 27.602 1.00 95.54 ? 554 THR B N 1 ATOM 11441 C CA . THR B 2 554 ? -28.769 22.665 27.727 1.00 93.18 ? 554 THR B CA 1 ATOM 11442 C C . THR B 2 554 ? -29.934 23.570 28.111 1.00 90.74 ? 554 THR B C 1 ATOM 11443 O O . THR B 2 554 ? -29.757 24.771 28.309 1.00 104.34 ? 554 THR B O 1 ATOM 11444 C CB . THR B 2 554 ? -28.644 21.542 28.775 1.00 92.26 ? 554 THR B CB 1 ATOM 11445 O OG1 . THR B 2 554 ? -28.152 22.089 30.005 1.00 91.83 ? 554 THR B OG1 1 ATOM 11446 C CG2 . THR B 2 554 ? -27.694 20.455 28.294 1.00 92.54 ? 554 THR B CG2 1 ATOM 11447 N N . GLY B 2 555 ? -31.122 22.986 28.221 1.00 89.58 ? 555 GLY B N 1 ATOM 11448 C CA . GLY B 2 555 ? -32.304 23.730 28.617 1.00 92.67 ? 555 GLY B CA 1 ATOM 11449 C C . GLY B 2 555 ? -33.222 24.078 27.462 1.00 91.68 ? 555 GLY B C 1 ATOM 11450 O O . GLY B 2 555 ? -32.821 24.037 26.299 1.00 88.04 ? 555 GLY B O 1 ATOM 11451 N N . TYR B 2 556 ? -34.463 24.424 27.790 1.00 91.66 ? 556 TYR B N 1 ATOM 11452 C CA . TYR B 2 556 ? -35.454 24.812 26.793 1.00 92.04 ? 556 TYR B CA 1 ATOM 11453 C C . TYR B 2 556 ? -35.072 26.134 26.135 1.00 91.25 ? 556 TYR B C 1 ATOM 11454 O O . TYR B 2 556 ? -35.223 26.306 24.925 1.00 90.71 ? 556 TYR B O 1 ATOM 11455 C CB . TYR B 2 556 ? -36.840 24.913 27.436 1.00 94.93 ? 556 TYR B CB 1 ATOM 11456 C CG . TYR B 2 556 ? -37.957 25.266 26.480 1.00 100.68 ? 556 TYR B CG 1 ATOM 11457 C CD1 . TYR B 2 556 ? -38.456 26.561 26.412 1.00 105.50 ? 556 TYR B CD1 1 ATOM 11458 C CD2 . TYR B 2 556 ? -38.519 24.304 25.651 1.00 104.18 ? 556 TYR B CD2 1 ATOM 11459 C CE1 . TYR B 2 556 ? -39.480 26.888 25.543 1.00 110.26 ? 556 TYR B CE1 1 ATOM 11460 C CE2 . TYR B 2 556 ? -39.543 24.621 24.778 1.00 103.51 ? 556 TYR B CE2 1 ATOM 11461 C CZ . TYR B 2 556 ? -40.020 25.915 24.728 1.00 107.85 ? 556 TYR B CZ 1 ATOM 11462 O OH . TYR B 2 556 ? -41.039 26.237 23.861 1.00 112.57 ? 556 TYR B OH 1 ATOM 11463 N N . TYR B 2 557 ? -34.573 27.064 26.943 1.00 92.35 ? 557 TYR B N 1 ATOM 11464 C CA . TYR B 2 557 ? -34.124 28.360 26.448 1.00 94.16 ? 557 TYR B CA 1 ATOM 11465 C C . TYR B 2 557 ? -32.647 28.312 26.074 1.00 99.02 ? 557 TYR B C 1 ATOM 11466 O O . TYR B 2 557 ? -32.091 29.294 25.576 1.00 107.57 ? 557 TYR B O 1 ATOM 11467 C CB . TYR B 2 557 ? -34.365 29.450 27.495 1.00 102.20 ? 557 TYR B CB 1 ATOM 11468 C CG . TYR B 2 557 ? -35.824 29.758 27.750 1.00 108.81 ? 557 TYR B CG 1 ATOM 11469 C CD1 . TYR B 2 557 ? -36.416 30.895 27.216 1.00 107.91 ? 557 TYR B CD1 1 ATOM 11470 C CD2 . TYR B 2 557 ? -36.609 28.915 28.526 1.00 113.26 ? 557 TYR B CD2 1 ATOM 11471 C CE1 . TYR B 2 557 ? -37.747 31.183 27.448 1.00 116.61 ? 557 TYR B CE1 1 ATOM 11472 C CE2 . TYR B 2 557 ? -37.941 29.194 28.761 1.00 110.73 ? 557 TYR B CE2 1 ATOM 11473 C CZ . TYR B 2 557 ? -38.505 30.329 28.219 1.00 118.76 ? 557 TYR B CZ 1 ATOM 11474 O OH . TYR B 2 557 ? -39.832 30.611 28.452 1.00 127.93 ? 557 TYR B OH 1 ATOM 11475 N N . CYS B 2 558 ? -32.023 27.164 26.331 1.00 95.54 ? 558 CYS B N 1 ATOM 11476 C CA . CYS B 2 558 ? -30.603 26.941 26.059 1.00 94.81 ? 558 CYS B CA 1 ATOM 11477 C C . CYS B 2 558 ? -29.699 27.922 26.805 1.00 96.63 ? 558 CYS B C 1 ATOM 11478 O O . CYS B 2 558 ? -28.590 28.213 26.358 1.00 98.14 ? 558 CYS B O 1 ATOM 11479 C CB . CYS B 2 558 ? -30.322 27.017 24.554 1.00 94.41 ? 558 CYS B CB 1 ATOM 11480 S SG . CYS B 2 558 ? -31.046 25.674 23.585 1.00 152.99 ? 558 CYS B SG 1 ATOM 11481 N N . ASN B 2 559 ? -30.174 28.434 27.937 1.00 98.76 ? 559 ASN B N 1 ATOM 11482 C CA . ASN B 2 559 ? -29.371 29.341 28.749 1.00 102.16 ? 559 ASN B CA 1 ATOM 11483 C C . ASN B 2 559 ? -28.658 28.629 29.900 1.00 100.75 ? 559 ASN B C 1 ATOM 11484 O O . ASN B 2 559 ? -27.975 29.264 30.704 1.00 103.21 ? 559 ASN B O 1 ATOM 11485 C CB . ASN B 2 559 ? -30.235 30.488 29.289 1.00 107.31 ? 559 ASN B CB 1 ATOM 11486 C CG . ASN B 2 559 ? -31.358 30.013 30.196 1.00 113.53 ? 559 ASN B CG 1 ATOM 11487 O OD1 . ASN B 2 559 ? -31.556 28.815 30.394 1.00 113.60 ? 559 ASN B OD1 1 ATOM 11488 N ND2 . ASN B 2 559 ? -32.100 30.964 30.756 1.00 120.25 ? 559 ASN B ND2 1 ATOM 11489 N N . CYS B 2 560 ? -28.818 27.310 29.975 1.00 98.07 ? 560 CYS B N 1 ATOM 11490 C CA . CYS B 2 560 ? -28.201 26.522 31.039 1.00 97.33 ? 560 CYS B CA 1 ATOM 11491 C C . CYS B 2 560 ? -26.841 25.978 30.606 1.00 99.12 ? 560 CYS B C 1 ATOM 11492 O O . CYS B 2 560 ? -26.658 25.587 29.454 1.00 111.47 ? 560 CYS B O 1 ATOM 11493 C CB . CYS B 2 560 ? -29.120 25.373 31.458 1.00 90.97 ? 560 CYS B CB 1 ATOM 11494 S SG . CYS B 2 560 ? -28.529 24.428 32.881 1.00 111.89 ? 560 CYS B SG 1 ATOM 11495 N N . THR B 2 561 ? -25.892 25.951 31.537 1.00 97.91 ? 561 THR B N 1 ATOM 11496 C CA . THR B 2 561 ? -24.511 25.602 31.215 1.00 97.45 ? 561 THR B CA 1 ATOM 11497 C C . THR B 2 561 ? -24.072 24.278 31.840 1.00 95.87 ? 561 THR B C 1 ATOM 11498 O O . THR B 2 561 ? -24.489 23.930 32.944 1.00 95.32 ? 561 THR B O 1 ATOM 11499 C CB . THR B 2 561 ? -23.544 26.709 31.675 1.00 97.18 ? 561 THR B CB 1 ATOM 11500 O OG1 . THR B 2 561 ? -24.147 27.992 31.464 1.00 112.87 ? 561 THR B OG1 1 ATOM 11501 C CG2 . THR B 2 561 ? -22.234 26.634 30.907 1.00 96.28 ? 561 THR B CG2 1 ATOM 11502 N N . THR B 2 562 ? -23.228 23.546 31.118 1.00 98.33 ? 562 THR B N 1 ATOM 11503 C CA . THR B 2 562 ? -22.675 22.284 31.598 1.00 94.53 ? 562 THR B CA 1 ATOM 11504 C C . THR B 2 562 ? -21.508 22.517 32.557 1.00 90.03 ? 562 THR B C 1 ATOM 11505 O O . THR B 2 562 ? -21.181 21.655 33.374 1.00 86.37 ? 562 THR B O 1 ATOM 11506 C CB . THR B 2 562 ? -22.197 21.403 30.423 1.00 102.14 ? 562 THR B CB 1 ATOM 11507 O OG1 . THR B 2 562 ? -23.167 21.437 29.369 1.00 102.87 ? 562 THR B OG1 1 ATOM 11508 C CG2 . THR B 2 562 ? -21.988 19.961 30.870 1.00 114.14 ? 562 THR B CG2 1 ATOM 11509 N N . ARG B 2 563 ? -20.888 23.690 32.451 1.00 88.46 ? 563 ARG B N 1 ATOM 11510 C CA . ARG B 2 563 ? -19.680 24.009 33.210 1.00 85.78 ? 563 ARG B CA 1 ATOM 11511 C C . ARG B 2 563 ? -19.861 23.894 34.721 1.00 89.59 ? 563 ARG B C 1 ATOM 11512 O O . ARG B 2 563 ? -20.747 24.522 35.302 1.00 90.51 ? 563 ARG B O 1 ATOM 11513 C CB . ARG B 2 563 ? -19.207 25.423 32.867 1.00 86.92 ? 563 ARG B CB 1 ATOM 11514 C CG . ARG B 2 563 ? -18.764 25.609 31.428 1.00 92.53 ? 563 ARG B CG 1 ATOM 11515 C CD . ARG B 2 563 ? -18.600 27.083 31.098 1.00 90.00 ? 563 ARG B CD 1 ATOM 11516 N NE . ARG B 2 563 ? -17.699 27.758 32.029 1.00 87.67 ? 563 ARG B NE 1 ATOM 11517 C CZ . ARG B 2 563 ? -17.463 29.066 32.023 1.00 88.70 ? 563 ARG B CZ 1 ATOM 11518 N NH1 . ARG B 2 563 ? -18.065 29.846 31.135 1.00 89.92 ? 563 ARG B NH1 1 ATOM 11519 N NH2 . ARG B 2 563 ? -16.628 29.595 32.906 1.00 87.98 ? 563 ARG B NH2 1 ATOM 11520 N N . THR B 2 564 ? -19.018 23.080 35.348 1.00 94.00 ? 564 THR B N 1 ATOM 11521 C CA . THR B 2 564 ? -18.973 22.980 36.802 1.00 89.14 ? 564 THR B CA 1 ATOM 11522 C C . THR B 2 564 ? -17.831 23.802 37.394 1.00 88.10 ? 564 THR B C 1 ATOM 11523 O O . THR B 2 564 ? -17.673 23.868 38.613 1.00 95.77 ? 564 THR B O 1 ATOM 11524 C CB . THR B 2 564 ? -18.822 21.518 37.259 1.00 88.05 ? 564 THR B CB 1 ATOM 11525 O OG1 . THR B 2 564 ? -17.644 20.951 36.672 1.00 94.82 ? 564 THR B OG1 1 ATOM 11526 C CG2 . THR B 2 564 ? -20.034 20.702 36.840 1.00 81.88 ? 564 THR B CG2 1 ATOM 11527 N N . ASP B 2 565 ? -17.039 24.428 36.527 1.00 90.43 ? 565 ASP B N 1 ATOM 11528 C CA . ASP B 2 565 ? -15.809 25.092 36.952 1.00 100.23 ? 565 ASP B CA 1 ATOM 11529 C C . ASP B 2 565 ? -16.067 26.314 37.831 1.00 98.91 ? 565 ASP B C 1 ATOM 11530 O O . ASP B 2 565 ? -15.322 26.574 38.776 1.00 108.29 ? 565 ASP B O 1 ATOM 11531 C CB . ASP B 2 565 ? -14.973 25.496 35.732 1.00 109.60 ? 565 ASP B CB 1 ATOM 11532 C CG . ASP B 2 565 ? -15.661 26.537 34.869 1.00 109.39 ? 565 ASP B CG 1 ATOM 11533 O OD1 . ASP B 2 565 ? -16.908 26.553 34.835 1.00 112.11 ? 565 ASP B OD1 1 ATOM 11534 O OD2 . ASP B 2 565 ? -14.952 27.340 34.227 1.00 107.46 ? 565 ASP B OD2 1 ATOM 11535 N N . THR B 2 566 ? -17.123 27.060 37.522 1.00 94.11 ? 566 THR B N 1 ATOM 11536 C CA . THR B 2 566 ? -17.462 28.250 38.292 1.00 99.21 ? 566 THR B CA 1 ATOM 11537 C C . THR B 2 566 ? -18.179 27.870 39.583 1.00 97.73 ? 566 THR B C 1 ATOM 11538 O O . THR B 2 566 ? -18.422 28.716 40.444 1.00 101.04 ? 566 THR B O 1 ATOM 11539 C CB . THR B 2 566 ? -18.343 29.218 37.483 1.00 86.00 ? 566 THR B CB 1 ATOM 11540 O OG1 . THR B 2 566 ? -19.591 28.586 37.171 1.00 85.93 ? 566 THR B OG1 1 ATOM 11541 C CG2 . THR B 2 566 ? -17.646 29.617 36.192 1.00 87.19 ? 566 THR B CG2 1 ATOM 11542 N N . CYS B 2 567 ? -18.519 26.591 39.706 1.00 99.93 ? 567 CYS B N 1 ATOM 11543 C CA . CYS B 2 567 ? -19.152 26.075 40.912 1.00 104.91 ? 567 CYS B CA 1 ATOM 11544 C C . CYS B 2 567 ? -18.111 25.568 41.905 1.00 109.44 ? 567 CYS B C 1 ATOM 11545 O O . CYS B 2 567 ? -18.437 25.236 43.045 1.00 114.12 ? 567 CYS B O 1 ATOM 11546 C CB . CYS B 2 567 ? -20.133 24.955 40.561 1.00 101.70 ? 567 CYS B CB 1 ATOM 11547 S SG . CYS B 2 567 ? -21.500 25.469 39.499 1.00 127.17 ? 567 CYS B SG 1 ATOM 11548 N N . MET B 2 568 ? -16.858 25.515 41.465 1.00 103.10 ? 568 MET B N 1 ATOM 11549 C CA . MET B 2 568 ? -15.777 24.987 42.289 1.00 98.36 ? 568 MET B CA 1 ATOM 11550 C C . MET B 2 568 ? -15.334 25.998 43.341 1.00 106.09 ? 568 MET B C 1 ATOM 11551 O O . MET B 2 568 ? -15.222 27.191 43.061 1.00 107.92 ? 568 MET B O 1 ATOM 11552 C CB . MET B 2 568 ? -14.589 24.584 41.414 1.00 102.41 ? 568 MET B CB 1 ATOM 11553 C CG . MET B 2 568 ? -13.946 23.267 41.812 1.00 110.47 ? 568 MET B CG 1 ATOM 11554 S SD . MET B 2 568 ? -15.041 21.860 41.545 1.00 159.79 ? 568 MET B SD 1 ATOM 11555 C CE . MET B 2 568 ? -15.237 21.916 39.765 1.00 90.57 ? 568 MET B CE 1 ATOM 11556 N N . SER B 2 569 ? -15.080 25.511 44.552 1.00 113.26 ? 569 SER B N 1 ATOM 11557 C CA . SER B 2 569 ? -14.684 26.373 45.661 1.00 108.22 ? 569 SER B CA 1 ATOM 11558 C C . SER B 2 569 ? -13.168 26.495 45.776 1.00 103.48 ? 569 SER B C 1 ATOM 11559 O O . SER B 2 569 ? -12.428 26.021 44.914 1.00 102.31 ? 569 SER B O 1 ATOM 11560 C CB . SER B 2 569 ? -15.264 25.848 46.975 1.00 110.77 ? 569 SER B CB 1 ATOM 11561 O OG . SER B 2 569 ? -14.857 26.650 48.070 1.00 112.54 ? 569 SER B OG 1 ATOM 11562 N N . SER B 2 570 ? -12.716 27.135 46.849 1.00 107.84 ? 570 SER B N 1 ATOM 11563 C CA . SER B 2 570 ? -11.290 27.310 47.099 1.00 106.39 ? 570 SER B CA 1 ATOM 11564 C C . SER B 2 570 ? -10.637 25.984 47.470 1.00 106.15 ? 570 SER B C 1 ATOM 11565 O O . SER B 2 570 ? -9.498 25.712 47.089 1.00 108.81 ? 570 SER B O 1 ATOM 11566 C CB . SER B 2 570 ? -11.063 28.337 48.210 1.00 117.29 ? 570 SER B CB 1 ATOM 11567 O OG . SER B 2 570 ? -11.685 29.572 47.901 1.00 120.30 ? 570 SER B OG 1 ATOM 11568 N N . ASN B 2 571 ? -11.369 25.162 48.215 1.00 112.88 ? 571 ASN B N 1 ATOM 11569 C CA . ASN B 2 571 ? -10.875 23.860 48.644 1.00 116.67 ? 571 ASN B CA 1 ATOM 11570 C C . ASN B 2 571 ? -10.844 22.844 47.505 1.00 117.92 ? 571 ASN B C 1 ATOM 11571 O O . ASN B 2 571 ? -10.147 21.833 47.583 1.00 126.08 ? 571 ASN B O 1 ATOM 11572 C CB . ASN B 2 571 ? -11.728 23.328 49.795 1.00 119.90 ? 571 ASN B CB 1 ATOM 11573 C CG . ASN B 2 571 ? -13.213 23.489 49.540 1.00 123.73 ? 571 ASN B CG 1 ATOM 11574 O OD1 . ASN B 2 571 ? -13.826 22.680 48.845 1.00 132.24 ? 571 ASN B OD1 1 ATOM 11575 N ND2 . ASN B 2 571 ? -13.800 24.539 50.103 1.00 112.97 ? 571 ASN B ND2 1 ATOM 11576 N N . GLY B 2 572 ? -11.604 23.118 46.450 1.00 112.63 ? 572 GLY B N 1 ATOM 11577 C CA . GLY B 2 572 ? -11.635 22.251 45.287 1.00 109.01 ? 572 GLY B CA 1 ATOM 11578 C C . GLY B 2 572 ? -12.908 21.436 45.177 1.00 105.91 ? 572 GLY B C 1 ATOM 11579 O O . GLY B 2 572 ? -13.207 20.879 44.121 1.00 111.71 ? 572 GLY B O 1 ATOM 11580 N N . LEU B 2 573 ? -13.663 21.366 46.269 1.00 91.29 ? 573 LEU B N 1 ATOM 11581 C CA . LEU B 2 573 ? -14.942 20.666 46.265 1.00 92.05 ? 573 LEU B CA 1 ATOM 11582 C C . LEU B 2 573 ? -16.044 21.617 45.813 1.00 85.41 ? 573 LEU B C 1 ATOM 11583 O O . LEU B 2 573 ? -16.129 22.746 46.294 1.00 85.91 ? 573 LEU B O 1 ATOM 11584 C CB . LEU B 2 573 ? -15.253 20.097 47.652 1.00 97.30 ? 573 LEU B CB 1 ATOM 11585 C CG . LEU B 2 573 ? -16.488 19.205 47.777 1.00 99.74 ? 573 LEU B CG 1 ATOM 11586 C CD1 . LEU B 2 573 ? -16.370 17.995 46.864 1.00 102.39 ? 573 LEU B CD1 1 ATOM 11587 C CD2 . LEU B 2 573 ? -16.687 18.771 49.221 1.00 94.61 ? 573 LEU B CD2 1 ATOM 11588 N N . LEU B 2 574 ? -16.879 21.161 44.883 1.00 85.61 ? 574 LEU B N 1 ATOM 11589 C CA . LEU B 2 574 ? -17.913 22.013 44.302 1.00 95.76 ? 574 LEU B CA 1 ATOM 11590 C C . LEU B 2 574 ? -18.930 22.457 45.352 1.00 103.81 ? 574 LEU B C 1 ATOM 11591 O O . LEU B 2 574 ? -19.422 21.649 46.142 1.00 115.46 ? 574 LEU B O 1 ATOM 11592 C CB . LEU B 2 574 ? -18.619 21.300 43.139 1.00 99.02 ? 574 LEU B CB 1 ATOM 11593 C CG . LEU B 2 574 ? -19.672 20.215 43.397 1.00 108.25 ? 574 LEU B CG 1 ATOM 11594 C CD1 . LEU B 2 574 ? -20.409 19.881 42.109 1.00 98.80 ? 574 LEU B CD1 1 ATOM 11595 C CD2 . LEU B 2 574 ? -19.058 18.960 44.001 1.00 122.76 ? 574 LEU B CD2 1 ATOM 11596 N N . CYS B 2 575 ? -19.203 23.760 45.367 1.00 94.13 ? 575 CYS B N 1 ATOM 11597 C CA . CYS B 2 575 ? -20.147 24.375 46.299 1.00 94.24 ? 575 CYS B CA 1 ATOM 11598 C C . CYS B 2 575 ? -19.761 24.134 47.758 1.00 94.95 ? 575 CYS B C 1 ATOM 11599 O O . CYS B 2 575 ? -20.612 24.183 48.647 1.00 114.87 ? 575 CYS B O 1 ATOM 11600 C CB . CYS B 2 575 ? -21.567 23.862 46.040 1.00 102.81 ? 575 CYS B CB 1 ATOM 11601 S SG . CYS B 2 575 ? -22.196 24.220 44.383 1.00 131.37 ? 575 CYS B SG 1 ATOM 11602 N N . SER B 2 576 ? -18.476 23.871 47.987 1.00 87.98 ? 576 SER B N 1 ATOM 11603 C CA . SER B 2 576 ? -17.924 23.661 49.326 1.00 93.64 ? 576 SER B CA 1 ATOM 11604 C C . SER B 2 576 ? -18.622 22.529 50.076 1.00 98.88 ? 576 SER B C 1 ATOM 11605 O O . SER B 2 576 ? -18.615 22.494 51.307 1.00 98.03 ? 576 SER B O 1 ATOM 11606 C CB . SER B 2 576 ? -18.001 24.952 50.145 1.00 96.63 ? 576 SER B CB 1 ATOM 11607 O OG . SER B 2 576 ? -17.295 26.003 49.510 1.00 99.41 ? 576 SER B OG 1 ATOM 11608 N N . GLY B 2 577 ? -19.228 21.607 49.333 1.00 103.99 ? 577 GLY B N 1 ATOM 11609 C CA . GLY B 2 577 ? -19.956 20.501 49.928 1.00 104.37 ? 577 GLY B CA 1 ATOM 11610 C C . GLY B 2 577 ? -21.274 20.919 50.557 1.00 102.45 ? 577 GLY B C 1 ATOM 11611 O O . GLY B 2 577 ? -22.043 20.078 51.021 1.00 109.29 ? 577 GLY B O 1 ATOM 11612 N N . ARG B 2 578 ? -21.535 22.223 50.568 1.00 101.32 ? 578 ARG B N 1 ATOM 11613 C CA . ARG B 2 578 ? -22.719 22.769 51.220 1.00 107.26 ? 578 ARG B CA 1 ATOM 11614 C C . ARG B 2 578 ? -23.889 22.934 50.255 1.00 107.03 ? 578 ARG B C 1 ATOM 11615 O O . ARG B 2 578 ? -24.942 23.441 50.635 1.00 111.22 ? 578 ARG B O 1 ATOM 11616 C CB . ARG B 2 578 ? -22.400 24.122 51.864 1.00 105.34 ? 578 ARG B CB 1 ATOM 11617 C CG . ARG B 2 578 ? -21.183 24.129 52.776 1.00 97.86 ? 578 ARG B CG 1 ATOM 11618 C CD . ARG B 2 578 ? -21.035 25.484 53.457 1.00 99.35 ? 578 ARG B CD 1 ATOM 11619 N NE . ARG B 2 578 ? -19.802 25.595 54.229 1.00 100.46 ? 578 ARG B NE 1 ATOM 11620 C CZ . ARG B 2 578 ? -19.665 25.184 55.486 1.00 104.34 ? 578 ARG B CZ 1 ATOM 11621 N NH1 . ARG B 2 578 ? -20.687 24.622 56.118 1.00 107.65 ? 578 ARG B NH1 1 ATOM 11622 N NH2 . ARG B 2 578 ? -18.505 25.330 56.110 1.00 105.24 ? 578 ARG B NH2 1 ATOM 11623 N N . GLY B 2 579 ? -23.703 22.520 49.006 1.00 104.32 ? 579 GLY B N 1 ATOM 11624 C CA . GLY B 2 579 ? -24.747 22.671 48.007 1.00 107.27 ? 579 GLY B CA 1 ATOM 11625 C C . GLY B 2 579 ? -24.499 21.910 46.719 1.00 112.14 ? 579 GLY B C 1 ATOM 11626 O O . GLY B 2 579 ? -23.548 21.136 46.614 1.00 121.02 ? 579 GLY B O 1 ATOM 11627 N N . LYS B 2 580 ? -25.364 22.138 45.735 1.00 105.17 ? 580 LYS B N 1 ATOM 11628 C CA . LYS B 2 580 ? -25.269 21.457 44.449 1.00 102.35 ? 580 LYS B CA 1 ATOM 11629 C C . LYS B 2 580 ? -25.200 22.459 43.298 1.00 94.83 ? 580 LYS B C 1 ATOM 11630 O O . LYS B 2 580 ? -25.855 23.500 43.328 1.00 92.95 ? 580 LYS B O 1 ATOM 11631 C CB . LYS B 2 580 ? -26.458 20.510 44.259 1.00 112.85 ? 580 LYS B CB 1 ATOM 11632 C CG . LYS B 2 580 ? -26.441 19.729 42.953 1.00 123.63 ? 580 LYS B CG 1 ATOM 11633 C CD . LYS B 2 580 ? -25.166 18.911 42.811 1.00 123.30 ? 580 LYS B CD 1 ATOM 11634 C CE . LYS B 2 580 ? -25.114 18.201 41.468 1.00 117.78 ? 580 LYS B CE 1 ATOM 11635 N NZ . LYS B 2 580 ? -23.850 17.434 41.291 1.00 112.38 ? 580 LYS B NZ 1 ATOM 11636 N N . CYS B 2 581 ? -24.401 22.134 42.286 1.00 90.31 ? 581 CYS B N 1 ATOM 11637 C CA . CYS B 2 581 ? -24.197 23.018 41.144 1.00 86.80 ? 581 CYS B CA 1 ATOM 11638 C C . CYS B 2 581 ? -25.281 22.854 40.081 1.00 87.65 ? 581 CYS B C 1 ATOM 11639 O O . CYS B 2 581 ? -25.503 21.755 39.571 1.00 87.56 ? 581 CYS B O 1 ATOM 11640 C CB . CYS B 2 581 ? -22.821 22.766 40.523 1.00 89.21 ? 581 CYS B CB 1 ATOM 11641 S SG . CYS B 2 581 ? -22.470 23.744 39.044 1.00 114.85 ? 581 CYS B SG 1 ATOM 11642 N N . GLU B 2 582 ? -25.952 23.954 39.750 1.00 89.94 ? 582 GLU B N 1 ATOM 11643 C CA . GLU B 2 582 ? -26.958 23.952 38.693 1.00 93.21 ? 582 GLU B CA 1 ATOM 11644 C C . GLU B 2 582 ? -26.784 25.146 37.756 1.00 87.51 ? 582 GLU B C 1 ATOM 11645 O O . GLU B 2 582 ? -26.849 26.298 38.187 1.00 87.76 ? 582 GLU B O 1 ATOM 11646 C CB . GLU B 2 582 ? -28.369 23.953 39.287 1.00 98.67 ? 582 GLU B CB 1 ATOM 11647 C CG . GLU B 2 582 ? -28.764 22.649 39.965 1.00 114.56 ? 582 GLU B CG 1 ATOM 11648 C CD . GLU B 2 582 ? -30.226 22.618 40.371 1.00 125.65 ? 582 GLU B CD 1 ATOM 11649 O OE1 . GLU B 2 582 ? -30.901 23.663 40.250 1.00 122.20 ? 582 GLU B OE1 1 ATOM 11650 O OE2 . GLU B 2 582 ? -30.702 21.548 40.807 1.00 134.31 ? 582 GLU B OE2 1 ATOM 11651 N N . CYS B 2 583 ? -26.562 24.851 36.477 1.00 87.64 ? 583 CYS B N 1 ATOM 11652 C CA . CYS B 2 583 ? -26.408 25.866 35.433 1.00 88.78 ? 583 CYS B CA 1 ATOM 11653 C C . CYS B 2 583 ? -25.281 26.859 35.716 1.00 88.57 ? 583 CYS B C 1 ATOM 11654 O O . CYS B 2 583 ? -25.441 28.062 35.514 1.00 90.15 ? 583 CYS B O 1 ATOM 11655 C CB . CYS B 2 583 ? -27.724 26.623 35.227 1.00 90.56 ? 583 CYS B CB 1 ATOM 11656 S SG . CYS B 2 583 ? -29.024 25.656 34.423 1.00 107.34 ? 583 CYS B SG 1 ATOM 11657 N N . GLY B 2 584 ? -24.145 26.350 36.180 1.00 86.80 ? 584 GLY B N 1 ATOM 11658 C CA . GLY B 2 584 ? -22.965 27.173 36.374 1.00 86.79 ? 584 GLY B CA 1 ATOM 11659 C C . GLY B 2 584 ? -22.961 27.983 37.657 1.00 87.91 ? 584 GLY B C 1 ATOM 11660 O O . GLY B 2 584 ? -21.959 28.609 37.999 1.00 92.58 ? 584 GLY B O 1 ATOM 11661 N N . SER B 2 585 ? -24.083 27.973 38.370 1.00 86.95 ? 585 SER B N 1 ATOM 11662 C CA . SER B 2 585 ? -24.190 28.697 39.630 1.00 87.70 ? 585 SER B CA 1 ATOM 11663 C C . SER B 2 585 ? -24.625 27.765 40.754 1.00 86.70 ? 585 SER B C 1 ATOM 11664 O O . SER B 2 585 ? -25.614 27.043 40.624 1.00 87.16 ? 585 SER B O 1 ATOM 11665 C CB . SER B 2 585 ? -25.171 29.865 39.501 1.00 103.85 ? 585 SER B CB 1 ATOM 11666 O OG . SER B 2 585 ? -24.707 30.821 38.564 1.00 109.77 ? 585 SER B OG 1 ATOM 11667 N N . CYS B 2 586 ? -23.882 27.783 41.856 1.00 84.63 ? 586 CYS B N 1 ATOM 11668 C CA . CYS B 2 586 ? -24.185 26.924 42.995 1.00 84.62 ? 586 CYS B CA 1 ATOM 11669 C C . CYS B 2 586 ? -25.497 27.303 43.667 1.00 86.56 ? 586 CYS B C 1 ATOM 11670 O O . CYS B 2 586 ? -25.752 28.475 43.943 1.00 92.99 ? 586 CYS B O 1 ATOM 11671 C CB . CYS B 2 586 ? -23.054 26.974 44.024 1.00 83.49 ? 586 CYS B CB 1 ATOM 11672 S SG . CYS B 2 586 ? -21.599 25.997 43.599 1.00 105.78 ? 586 CYS B SG 1 ATOM 11673 N N . VAL B 2 587 ? -26.328 26.299 43.923 1.00 88.13 ? 587 VAL B N 1 ATOM 11674 C CA . VAL B 2 587 ? -27.533 26.487 44.716 1.00 90.58 ? 587 VAL B CA 1 ATOM 11675 C C . VAL B 2 587 ? -27.303 25.870 46.088 1.00 106.15 ? 587 VAL B C 1 ATOM 11676 O O . VAL B 2 587 ? -27.230 24.649 46.224 1.00 113.23 ? 587 VAL B O 1 ATOM 11677 C CB . VAL B 2 587 ? -28.765 25.852 44.050 1.00 92.61 ? 587 VAL B CB 1 ATOM 11678 C CG1 . VAL B 2 587 ? -29.999 26.056 44.914 1.00 96.17 ? 587 VAL B CG1 1 ATOM 11679 C CG2 . VAL B 2 587 ? -28.975 26.437 42.663 1.00 100.77 ? 587 VAL B CG2 1 ATOM 11680 N N . CYS B 2 588 ? -27.188 26.718 47.103 1.00 108.16 ? 588 CYS B N 1 ATOM 11681 C CA . CYS B 2 588 ? -26.805 26.260 48.431 1.00 111.96 ? 588 CYS B CA 1 ATOM 11682 C C . CYS B 2 588 ? -27.946 25.554 49.148 1.00 119.22 ? 588 CYS B C 1 ATOM 11683 O O . CYS B 2 588 ? -29.020 26.125 49.335 1.00 121.91 ? 588 CYS B O 1 ATOM 11684 C CB . CYS B 2 588 ? -26.316 27.437 49.280 1.00 111.70 ? 588 CYS B CB 1 ATOM 11685 S SG . CYS B 2 588 ? -24.823 28.245 48.663 1.00 115.11 ? 588 CYS B SG 1 ATOM 11686 N N . ILE B 2 589 ? -27.711 24.306 49.544 1.00 92.73 ? 589 ILE B N 1 ATOM 11687 C CA . ILE B 2 589 ? -28.632 23.626 50.441 1.00 92.29 ? 589 ILE B CA 1 ATOM 11688 C C . ILE B 2 589 ? -27.917 23.238 51.732 1.00 86.52 ? 589 ILE B C 1 ATOM 11689 O O . ILE B 2 589 ? -27.141 22.282 51.769 1.00 93.20 ? 589 ILE B O 1 ATOM 11690 C CB . ILE B 2 589 ? -29.244 22.372 49.783 1.00 92.07 ? 589 ILE B CB 1 ATOM 11691 C CG1 . ILE B 2 589 ? -28.220 21.688 48.872 1.00 88.68 ? 589 ILE B CG1 1 ATOM 11692 C CG2 . ILE B 2 589 ? -30.477 22.744 48.978 1.00 95.89 ? 589 ILE B CG2 1 ATOM 11693 C CD1 . ILE B 2 589 ? -27.800 20.310 49.341 1.00 92.25 ? 589 ILE B CD1 1 ATOM 11694 N N . GLN B 2 590 ? -28.237 23.975 52.792 1.00 75.13 ? 590 GLN B N 1 ATOM 11695 C CA . GLN B 2 590 ? -27.655 23.812 54.122 1.00 83.23 ? 590 GLN B CA 1 ATOM 11696 C C . GLN B 2 590 ? -28.164 24.969 54.968 1.00 90.62 ? 590 GLN B C 1 ATOM 11697 O O . GLN B 2 590 ? -28.400 26.057 54.441 1.00 104.33 ? 590 GLN B O 1 ATOM 11698 C CB . GLN B 2 590 ? -26.122 23.811 54.090 1.00 86.19 ? 590 GLN B CB 1 ATOM 11699 C CG . GLN B 2 590 ? -25.480 22.829 55.062 1.00 91.21 ? 590 GLN B CG 1 ATOM 11700 C CD . GLN B 2 590 ? -24.046 23.184 55.397 1.00 105.42 ? 590 GLN B CD 1 ATOM 11701 O OE1 . GLN B 2 590 ? -23.537 24.219 54.972 1.00 124.21 ? 590 GLN B OE1 1 ATOM 11702 N NE2 . GLN B 2 590 ? -23.387 22.326 56.169 1.00 101.03 ? 590 GLN B NE2 1 ATOM 11703 N N . PRO B 2 591 ? -28.345 24.749 56.277 1.00 94.93 ? 591 PRO B N 1 ATOM 11704 C CA . PRO B 2 591 ? -28.744 25.879 57.120 1.00 106.96 ? 591 PRO B CA 1 ATOM 11705 C C . PRO B 2 591 ? -27.686 26.982 57.145 1.00 102.49 ? 591 PRO B C 1 ATOM 11706 O O . PRO B 2 591 ? -26.512 26.702 57.390 1.00 97.21 ? 591 PRO B O 1 ATOM 11707 C CB . PRO B 2 591 ? -28.910 25.243 58.506 1.00 124.86 ? 591 PRO B CB 1 ATOM 11708 C CG . PRO B 2 591 ? -28.123 23.971 58.447 1.00 123.50 ? 591 PRO B CG 1 ATOM 11709 C CD . PRO B 2 591 ? -28.269 23.492 57.038 1.00 109.40 ? 591 PRO B CD 1 ATOM 11710 N N . GLY B 2 592 ? -28.111 28.217 56.889 1.00 99.93 ? 592 GLY B N 1 ATOM 11711 C CA . GLY B 2 592 ? -27.234 29.375 56.945 1.00 101.83 ? 592 GLY B CA 1 ATOM 11712 C C . GLY B 2 592 ? -25.985 29.308 56.083 1.00 91.50 ? 592 GLY B C 1 ATOM 11713 O O . GLY B 2 592 ? -24.880 29.550 56.569 1.00 100.95 ? 592 GLY B O 1 ATOM 11714 N N . SER B 2 593 ? -26.154 28.986 54.805 1.00 72.96 ? 593 SER B N 1 ATOM 11715 C CA . SER B 2 593 ? -25.028 28.951 53.876 1.00 71.27 ? 593 SER B CA 1 ATOM 11716 C C . SER B 2 593 ? -25.345 29.736 52.608 1.00 65.66 ? 593 SER B C 1 ATOM 11717 O O . SER B 2 593 ? -26.449 29.645 52.072 1.00 78.59 ? 593 SER B O 1 ATOM 11718 C CB . SER B 2 593 ? -24.661 27.508 53.525 1.00 74.47 ? 593 SER B CB 1 ATOM 11719 O OG . SER B 2 593 ? -25.718 26.865 52.833 1.00 80.87 ? 593 SER B OG 1 ATOM 11720 N N . TYR B 2 594 ? -24.369 30.503 52.132 1.00 64.11 ? 594 TYR B N 1 ATOM 11721 C CA . TYR B 2 594 ? -24.557 31.334 50.949 1.00 59.84 ? 594 TYR B CA 1 ATOM 11722 C C . TYR B 2 594 ? -23.226 31.727 50.318 1.00 62.94 ? 594 TYR B C 1 ATOM 11723 O O . TYR B 2 594 ? -22.160 31.340 50.796 1.00 66.12 ? 594 TYR B O 1 ATOM 11724 C CB . TYR B 2 594 ? -25.362 32.588 51.300 1.00 58.68 ? 594 TYR B CB 1 ATOM 11725 C CG . TYR B 2 594 ? -24.793 33.388 52.450 1.00 58.57 ? 594 TYR B CG 1 ATOM 11726 C CD1 . TYR B 2 594 ? -23.946 34.464 52.222 1.00 61.69 ? 594 TYR B CD1 1 ATOM 11727 C CD2 . TYR B 2 594 ? -25.109 33.070 53.764 1.00 60.11 ? 594 TYR B CD2 1 ATOM 11728 C CE1 . TYR B 2 594 ? -23.426 35.198 53.271 1.00 66.00 ? 594 TYR B CE1 1 ATOM 11729 C CE2 . TYR B 2 594 ? -24.593 33.796 54.817 1.00 64.30 ? 594 TYR B CE2 1 ATOM 11730 C CZ . TYR B 2 594 ? -23.754 34.860 54.567 1.00 66.93 ? 594 TYR B CZ 1 ATOM 11731 O OH . TYR B 2 594 ? -23.241 35.587 55.617 1.00 69.64 ? 594 TYR B OH 1 ATOM 11732 N N . GLY B 2 595 ? -23.298 32.508 49.245 1.00 62.86 ? 595 GLY B N 1 ATOM 11733 C CA . GLY B 2 595 ? -22.118 32.875 48.486 1.00 72.59 ? 595 GLY B CA 1 ATOM 11734 C C . GLY B 2 595 ? -22.082 32.137 47.163 1.00 66.93 ? 595 GLY B C 1 ATOM 11735 O O . GLY B 2 595 ? -22.840 31.189 46.956 1.00 65.72 ? 595 GLY B O 1 ATOM 11736 N N . ASP B 2 596 ? -21.202 32.572 46.266 1.00 65.01 ? 596 ASP B N 1 ATOM 11737 C CA . ASP B 2 596 ? -21.090 31.966 44.943 1.00 67.62 ? 596 ASP B CA 1 ATOM 11738 C C . ASP B 2 596 ? -20.680 30.500 45.031 1.00 79.20 ? 596 ASP B C 1 ATOM 11739 O O . ASP B 2 596 ? -21.311 29.631 44.431 1.00 89.13 ? 596 ASP B O 1 ATOM 11740 C CB . ASP B 2 596 ? -20.085 32.739 44.085 1.00 75.77 ? 596 ASP B CB 1 ATOM 11741 C CG . ASP B 2 596 ? -20.467 34.196 43.911 1.00 88.45 ? 596 ASP B CG 1 ATOM 11742 O OD1 . ASP B 2 596 ? -21.667 34.518 44.046 1.00 103.03 ? 596 ASP B OD1 1 ATOM 11743 O OD2 . ASP B 2 596 ? -19.569 35.019 43.636 1.00 89.61 ? 596 ASP B OD2 1 ATOM 11744 N N . THR B 2 597 ? -19.615 30.236 45.780 1.00 86.89 ? 597 THR B N 1 ATOM 11745 C CA . THR B 2 597 ? -19.117 28.879 45.972 1.00 93.87 ? 597 THR B CA 1 ATOM 11746 C C . THR B 2 597 ? -19.682 28.252 47.243 1.00 95.62 ? 597 THR B C 1 ATOM 11747 O O . THR B 2 597 ? -19.263 27.164 47.639 1.00 113.90 ? 597 THR B O 1 ATOM 11748 C CB . THR B 2 597 ? -17.579 28.846 46.033 1.00 109.83 ? 597 THR B CB 1 ATOM 11749 O OG1 . THR B 2 597 ? -17.126 29.605 47.160 1.00 127.68 ? 597 THR B OG1 1 ATOM 11750 C CG2 . THR B 2 597 ? -16.983 29.429 44.761 1.00 109.26 ? 597 THR B CG2 1 ATOM 11751 N N . CYS B 2 598 ? -20.608 28.963 47.886 1.00 76.69 ? 598 CYS B N 1 ATOM 11752 C CA . CYS B 2 598 ? -21.203 28.543 49.157 1.00 76.46 ? 598 CYS B CA 1 ATOM 11753 C C . CYS B 2 598 ? -20.138 28.433 50.241 1.00 76.60 ? 598 CYS B C 1 ATOM 11754 O O . CYS B 2 598 ? -20.218 27.582 51.126 1.00 77.86 ? 598 CYS B O 1 ATOM 11755 C CB . CYS B 2 598 ? -21.948 27.212 49.008 1.00 72.38 ? 598 CYS B CB 1 ATOM 11756 S SG . CYS B 2 598 ? -23.291 27.228 47.800 1.00 115.41 ? 598 CYS B SG 1 ATOM 11757 N N . GLU B 2 599 ? -19.142 29.309 50.162 1.00 79.19 ? 599 GLU B N 1 ATOM 11758 C CA . GLU B 2 599 ? -18.024 29.304 51.098 1.00 82.00 ? 599 GLU B CA 1 ATOM 11759 C C . GLU B 2 599 ? -18.391 29.970 52.420 1.00 92.71 ? 599 GLU B C 1 ATOM 11760 O O . GLU B 2 599 ? -17.728 29.757 53.436 1.00 103.66 ? 599 GLU B O 1 ATOM 11761 C CB . GLU B 2 599 ? -16.812 30.007 50.479 1.00 78.89 ? 599 GLU B CB 1 ATOM 11762 C CG . GLU B 2 599 ? -16.957 31.521 50.330 1.00 81.08 ? 599 GLU B CG 1 ATOM 11763 C CD . GLU B 2 599 ? -17.955 31.929 49.256 1.00 95.86 ? 599 GLU B CD 1 ATOM 11764 O OE1 . GLU B 2 599 ? -18.283 33.131 49.177 1.00 113.38 ? 599 GLU B OE1 1 ATOM 11765 O OE2 . GLU B 2 599 ? -18.409 31.051 48.492 1.00 92.41 ? 599 GLU B OE2 1 ATOM 11766 N N . LYS B 2 600 ? -19.448 30.775 52.403 1.00 87.65 ? 600 LYS B N 1 ATOM 11767 C CA . LYS B 2 600 ? -19.856 31.520 53.587 1.00 77.74 ? 600 LYS B CA 1 ATOM 11768 C C . LYS B 2 600 ? -20.896 30.773 54.416 1.00 78.14 ? 600 LYS B C 1 ATOM 11769 O O . LYS B 2 600 ? -22.014 30.530 53.961 1.00 76.77 ? 600 LYS B O 1 ATOM 11770 C CB . LYS B 2 600 ? -20.403 32.892 53.191 1.00 75.53 ? 600 LYS B CB 1 ATOM 11771 C CG . LYS B 2 600 ? -19.363 33.831 52.605 1.00 77.67 ? 600 LYS B CG 1 ATOM 11772 C CD . LYS B 2 600 ? -19.962 35.199 52.331 1.00 82.27 ? 600 LYS B CD 1 ATOM 11773 C CE . LYS B 2 600 ? -18.909 36.181 51.848 1.00 87.89 ? 600 LYS B CE 1 ATOM 11774 N NZ . LYS B 2 600 ? -19.475 37.546 51.665 1.00 88.60 ? 600 LYS B NZ 1 ATOM 11775 N N . CYS B 2 601 ? -20.512 30.409 55.634 1.00 81.97 ? 601 CYS B N 1 ATOM 11776 C CA . CYS B 2 601 ? -21.433 29.817 56.596 1.00 80.70 ? 601 CYS B CA 1 ATOM 11777 C C . CYS B 2 601 ? -21.125 30.340 57.996 1.00 83.55 ? 601 CYS B C 1 ATOM 11778 O O . CYS B 2 601 ? -20.485 29.654 58.792 1.00 102.86 ? 601 CYS B O 1 ATOM 11779 C CB . CYS B 2 601 ? -21.349 28.289 56.563 1.00 79.63 ? 601 CYS B CB 1 ATOM 11780 S SG . CYS B 2 601 ? -22.468 27.443 57.710 1.00 97.88 ? 601 CYS B SG 1 ATOM 11781 N N . PRO B 2 602 ? -21.563 31.573 58.293 1.00 83.65 ? 602 PRO B N 1 ATOM 11782 C CA . PRO B 2 602 ? -21.312 32.163 59.612 1.00 75.88 ? 602 PRO B CA 1 ATOM 11783 C C . PRO B 2 602 ? -21.996 31.384 60.731 1.00 78.81 ? 602 PRO B C 1 ATOM 11784 O O . PRO B 2 602 ? -21.388 31.152 61.776 1.00 77.91 ? 602 PRO B O 1 ATOM 11785 C CB . PRO B 2 602 ? -21.898 33.573 59.485 1.00 88.14 ? 602 PRO B CB 1 ATOM 11786 C CG . PRO B 2 602 ? -22.902 33.472 58.391 1.00 89.95 ? 602 PRO B CG 1 ATOM 11787 C CD . PRO B 2 602 ? -22.349 32.467 57.427 1.00 91.36 ? 602 PRO B CD 1 ATOM 11788 N N . THR B 2 603 ? -23.243 30.981 60.507 1.00 77.70 ? 603 THR B N 1 ATOM 11789 C CA . THR B 2 603 ? -23.968 30.187 61.490 1.00 80.59 ? 603 THR B CA 1 ATOM 11790 C C . THR B 2 603 ? -24.178 28.767 60.985 1.00 97.32 ? 603 THR B C 1 ATOM 11791 O O . THR B 2 603 ? -25.009 28.524 60.108 1.00 130.24 ? 603 THR B O 1 ATOM 11792 C CB . THR B 2 603 ? -25.335 30.811 61.826 1.00 78.74 ? 603 THR B CB 1 ATOM 11793 O OG1 . THR B 2 603 ? -26.133 30.889 60.638 1.00 71.63 ? 603 THR B OG1 1 ATOM 11794 C CG2 . THR B 2 603 ? -25.156 32.206 62.403 1.00 96.49 ? 603 THR B CG2 1 ATOM 11795 N N . CYS B 2 604 ? -23.436 27.837 61.578 1.00 88.81 ? 604 CYS B N 1 ATOM 11796 C CA . CYS B 2 604 ? -23.452 26.425 61.213 1.00 89.98 ? 604 CYS B CA 1 ATOM 11797 C C . CYS B 2 604 ? -22.463 25.715 62.131 1.00 91.79 ? 604 CYS B C 1 ATOM 11798 O O . CYS B 2 604 ? -21.611 26.374 62.729 1.00 93.13 ? 604 CYS B O 1 ATOM 11799 C CB . CYS B 2 604 ? -23.084 26.221 59.736 1.00 88.31 ? 604 CYS B CB 1 ATOM 11800 S SG . CYS B 2 604 ? -21.409 26.719 59.286 1.00 178.33 ? 604 CYS B SG 1 ATOM 11801 N N . PRO B 2 605 ? -22.580 24.381 62.266 1.00 95.44 ? 605 PRO B N 1 ATOM 11802 C CA . PRO B 2 605 ? -21.628 23.635 63.098 1.00 92.11 ? 605 PRO B CA 1 ATOM 11803 C C . PRO B 2 605 ? -20.182 23.950 62.730 1.00 91.64 ? 605 PRO B C 1 ATOM 11804 O O . PRO B 2 605 ? -19.835 23.977 61.549 1.00 90.13 ? 605 PRO B O 1 ATOM 11805 C CB . PRO B 2 605 ? -21.969 22.166 62.800 1.00 107.18 ? 605 PRO B CB 1 ATOM 11806 C CG . PRO B 2 605 ? -22.881 22.194 61.600 1.00 111.26 ? 605 PRO B CG 1 ATOM 11807 C CD . PRO B 2 605 ? -23.605 23.493 61.696 1.00 110.46 ? 605 PRO B CD 1 ATOM 11808 N N . ASP B 2 606 ? -19.357 24.204 63.740 1.00 93.67 ? 606 ASP B N 1 ATOM 11809 C CA . ASP B 2 606 ? -18.001 24.682 63.509 1.00 109.23 ? 606 ASP B CA 1 ATOM 11810 C C . ASP B 2 606 ? -16.946 23.689 63.976 1.00 105.89 ? 606 ASP B C 1 ATOM 11811 O O . ASP B 2 606 ? -17.148 22.970 64.955 1.00 105.07 ? 606 ASP B O 1 ATOM 11812 C CB . ASP B 2 606 ? -17.786 26.022 64.218 1.00 126.91 ? 606 ASP B CB 1 ATOM 11813 C CG . ASP B 2 606 ? -17.566 25.862 65.712 1.00 133.73 ? 606 ASP B CG 1 ATOM 11814 O OD1 . ASP B 2 606 ? -16.595 26.448 66.235 1.00 150.37 ? 606 ASP B OD1 1 ATOM 11815 O OD2 . ASP B 2 606 ? -18.359 25.148 66.362 1.00 117.89 ? 606 ASP B OD2 1 ATOM 11816 N N . ALA B 2 607 ? -15.827 23.658 63.256 1.00 102.40 ? 607 ALA B N 1 ATOM 11817 C CA . ALA B 2 607 ? -14.632 22.936 63.685 1.00 103.30 ? 607 ALA B CA 1 ATOM 11818 C C . ALA B 2 607 ? -14.900 21.477 64.042 1.00 101.49 ? 607 ALA B C 1 ATOM 11819 O O . ALA B 2 607 ? -15.293 20.677 63.192 1.00 101.40 ? 607 ALA B O 1 ATOM 11820 C CB . ALA B 2 607 ? -13.992 23.652 64.867 1.00 108.06 ? 607 ALA B CB 1 ATOM 11821 N N . CYS B 2 608 ? -14.676 21.157 65.314 1.00 109.45 ? 608 CYS B N 1 ATOM 11822 C CA . CYS B 2 608 ? -14.750 19.794 65.835 1.00 115.88 ? 608 CYS B CA 1 ATOM 11823 C C . CYS B 2 608 ? -16.008 19.027 65.438 1.00 97.53 ? 608 CYS B C 1 ATOM 11824 O O . CYS B 2 608 ? -15.935 17.835 65.152 1.00 101.76 ? 608 CYS B O 1 ATOM 11825 C CB . CYS B 2 608 ? -14.636 19.823 67.359 1.00 130.58 ? 608 CYS B CB 1 ATOM 11826 S SG . CYS B 2 608 ? -15.279 21.329 68.128 1.00 160.87 ? 608 CYS B SG 1 ATOM 11827 N N . THR B 2 609 ? -17.151 19.709 65.424 1.00 99.02 ? 609 THR B N 1 ATOM 11828 C CA . THR B 2 609 ? -18.424 19.081 65.073 1.00 102.88 ? 609 THR B CA 1 ATOM 11829 C C . THR B 2 609 ? -18.340 18.332 63.745 1.00 101.72 ? 609 THR B C 1 ATOM 11830 O O . THR B 2 609 ? -18.965 17.286 63.569 1.00 104.26 ? 609 THR B O 1 ATOM 11831 C CB . THR B 2 609 ? -19.556 20.117 64.991 1.00 108.98 ? 609 THR B CB 1 ATOM 11832 O OG1 . THR B 2 609 ? -19.200 21.139 64.053 1.00 130.98 ? 609 THR B OG1 1 ATOM 11833 C CG2 . THR B 2 609 ? -19.798 20.748 66.354 1.00 113.54 ? 609 THR B CG2 1 ATOM 11834 N N . PHE B 2 610 ? -17.565 18.878 62.814 1.00 99.30 ? 610 PHE B N 1 ATOM 11835 C CA . PHE B 2 610 ? -17.270 18.192 61.563 1.00 106.82 ? 610 PHE B CA 1 ATOM 11836 C C . PHE B 2 610 ? -16.206 17.116 61.764 1.00 98.61 ? 610 PHE B C 1 ATOM 11837 O O . PHE B 2 610 ? -16.337 15.996 61.269 1.00 94.77 ? 610 PHE B O 1 ATOM 11838 C CB . PHE B 2 610 ? -16.805 19.191 60.499 1.00 121.65 ? 610 PHE B CB 1 ATOM 11839 C CG . PHE B 2 610 ? -17.899 20.078 59.978 1.00 120.55 ? 610 PHE B CG 1 ATOM 11840 C CD1 . PHE B 2 610 ? -19.213 19.641 59.956 1.00 115.80 ? 610 PHE B CD1 1 ATOM 11841 C CD2 . PHE B 2 610 ? -17.613 21.350 59.508 1.00 125.36 ? 610 PHE B CD2 1 ATOM 11842 C CE1 . PHE B 2 610 ? -20.221 20.456 59.475 1.00 122.03 ? 610 PHE B CE1 1 ATOM 11843 C CE2 . PHE B 2 610 ? -18.617 22.169 59.026 1.00 130.10 ? 610 PHE B CE2 1 ATOM 11844 C CZ . PHE B 2 610 ? -19.923 21.721 59.010 1.00 129.23 ? 610 PHE B CZ 1 ATOM 11845 N N . LYS B 2 611 ? -15.150 17.470 62.491 1.00 92.85 ? 611 LYS B N 1 ATOM 11846 C CA . LYS B 2 611 ? -13.981 16.607 62.630 1.00 88.09 ? 611 LYS B CA 1 ATOM 11847 C C . LYS B 2 611 ? -14.111 15.526 63.704 1.00 88.77 ? 611 LYS B C 1 ATOM 11848 O O . LYS B 2 611 ? -13.381 14.536 63.673 1.00 87.66 ? 611 LYS B O 1 ATOM 11849 C CB . LYS B 2 611 ? -12.743 17.462 62.908 1.00 84.93 ? 611 LYS B CB 1 ATOM 11850 C CG . LYS B 2 611 ? -12.452 18.468 61.807 1.00 84.70 ? 611 LYS B CG 1 ATOM 11851 C CD . LYS B 2 611 ? -11.127 19.178 62.018 1.00 85.45 ? 611 LYS B CD 1 ATOM 11852 C CE . LYS B 2 611 ? -10.814 20.087 60.841 1.00 91.89 ? 611 LYS B CE 1 ATOM 11853 N NZ . LYS B 2 611 ? -9.493 20.755 60.981 1.00 109.57 ? 611 LYS B NZ 1 ATOM 11854 N N . LYS B 2 612 ? -15.029 15.704 64.651 1.00 102.58 ? 612 LYS B N 1 ATOM 11855 C CA . LYS B 2 612 ? -15.228 14.692 65.688 1.00 96.91 ? 612 LYS B CA 1 ATOM 11856 C C . LYS B 2 612 ? -15.853 13.446 65.076 1.00 97.59 ? 612 LYS B C 1 ATOM 11857 O O . LYS B 2 612 ? -15.752 12.352 65.626 1.00 111.53 ? 612 LYS B O 1 ATOM 11858 C CB . LYS B 2 612 ? -16.102 15.219 66.828 1.00 96.03 ? 612 LYS B CB 1 ATOM 11859 C CG . LYS B 2 612 ? -17.587 15.264 66.511 1.00 102.85 ? 612 LYS B CG 1 ATOM 11860 C CD . LYS B 2 612 ? -18.399 15.671 67.728 1.00 108.46 ? 612 LYS B CD 1 ATOM 11861 C CE . LYS B 2 612 ? -19.885 15.681 67.416 1.00 103.04 ? 612 LYS B CE 1 ATOM 11862 N NZ . LYS B 2 612 ? -20.693 16.125 68.584 1.00 99.22 ? 612 LYS B NZ 1 ATOM 11863 N N . GLU B 2 613 ? -16.504 13.625 63.932 1.00 93.17 ? 613 GLU B N 1 ATOM 11864 C CA . GLU B 2 613 ? -17.051 12.505 63.183 1.00 94.32 ? 613 GLU B CA 1 ATOM 11865 C C . GLU B 2 613 ? -15.916 11.741 62.511 1.00 91.79 ? 613 GLU B C 1 ATOM 11866 O O . GLU B 2 613 ? -16.022 10.542 62.256 1.00 97.43 ? 613 GLU B O 1 ATOM 11867 C CB . GLU B 2 613 ? -18.064 12.995 62.145 1.00 96.18 ? 613 GLU B CB 1 ATOM 11868 C CG . GLU B 2 613 ? -18.782 11.886 61.394 1.00 105.46 ? 613 GLU B CG 1 ATOM 11869 C CD . GLU B 2 613 ? -19.771 12.417 60.373 1.00 112.08 ? 613 GLU B CD 1 ATOM 11870 O OE1 . GLU B 2 613 ? -20.013 13.642 60.357 1.00 113.86 ? 613 GLU B OE1 1 ATOM 11871 O OE2 . GLU B 2 613 ? -20.304 11.608 59.584 1.00 115.99 ? 613 GLU B OE2 1 ATOM 11872 N N . CYS B 2 614 ? -14.823 12.447 62.240 1.00 90.95 ? 614 CYS B N 1 ATOM 11873 C CA . CYS B 2 614 ? -13.681 11.862 61.548 1.00 86.07 ? 614 CYS B CA 1 ATOM 11874 C C . CYS B 2 614 ? -12.820 11.012 62.483 1.00 85.24 ? 614 CYS B C 1 ATOM 11875 O O . CYS B 2 614 ? -12.324 9.957 62.086 1.00 89.10 ? 614 CYS B O 1 ATOM 11876 C CB . CYS B 2 614 ? -12.833 12.962 60.903 1.00 75.66 ? 614 CYS B CB 1 ATOM 11877 S SG . CYS B 2 614 ? -11.873 12.424 59.467 1.00 112.67 ? 614 CYS B SG 1 ATOM 11878 N N . VAL B 2 615 ? -12.643 11.467 63.721 1.00 73.36 ? 615 VAL B N 1 ATOM 11879 C CA . VAL B 2 615 ? -11.822 10.733 64.682 1.00 72.07 ? 615 VAL B CA 1 ATOM 11880 C C . VAL B 2 615 ? -12.514 9.453 65.142 1.00 81.39 ? 615 VAL B C 1 ATOM 11881 O O . VAL B 2 615 ? -11.856 8.447 65.407 1.00 95.57 ? 615 VAL B O 1 ATOM 11882 C CB . VAL B 2 615 ? -11.466 11.593 65.916 1.00 70.91 ? 615 VAL B CB 1 ATOM 11883 C CG1 . VAL B 2 615 ? -10.511 12.703 65.527 1.00 71.27 ? 615 VAL B CG1 1 ATOM 11884 C CG2 . VAL B 2 615 ? -12.713 12.166 66.559 1.00 74.18 ? 615 VAL B CG2 1 ATOM 11885 N N . GLU B 2 616 ? -13.840 9.494 65.236 1.00 80.05 ? 616 GLU B N 1 ATOM 11886 C CA . GLU B 2 616 ? -14.619 8.299 65.536 1.00 82.33 ? 616 GLU B CA 1 ATOM 11887 C C . GLU B 2 616 ? -14.464 7.313 64.389 1.00 91.22 ? 616 GLU B C 1 ATOM 11888 O O . GLU B 2 616 ? -14.299 6.111 64.598 1.00 94.49 ? 616 GLU B O 1 ATOM 11889 C CB . GLU B 2 616 ? -16.094 8.645 65.751 1.00 80.73 ? 616 GLU B CB 1 ATOM 11890 C CG . GLU B 2 616 ? -16.359 9.519 66.964 1.00 80.23 ? 616 GLU B CG 1 ATOM 11891 C CD . GLU B 2 616 ? -16.124 8.789 68.271 1.00 79.85 ? 616 GLU B CD 1 ATOM 11892 O OE1 . GLU B 2 616 ? -16.849 7.809 68.542 1.00 81.49 ? 616 GLU B OE1 1 ATOM 11893 O OE2 . GLU B 2 616 ? -15.213 9.193 69.024 1.00 76.92 ? 616 GLU B OE2 1 ATOM 11894 N N . CYS B 2 617 ? -14.524 7.845 63.173 1.00 97.86 ? 617 CYS B N 1 ATOM 11895 C CA . CYS B 2 617 ? -14.286 7.069 61.966 1.00 91.57 ? 617 CYS B CA 1 ATOM 11896 C C . CYS B 2 617 ? -12.899 6.432 61.970 1.00 86.35 ? 617 CYS B C 1 ATOM 11897 O O . CYS B 2 617 ? -12.766 5.211 62.057 1.00 76.63 ? 617 CYS B O 1 ATOM 11898 C CB . CYS B 2 617 ? -14.455 7.956 60.730 1.00 83.09 ? 617 CYS B CB 1 ATOM 11899 S SG . CYS B 2 617 ? -13.968 7.190 59.169 1.00 104.75 ? 617 CYS B SG 1 ATOM 11900 N N . LYS B 2 618 ? -11.869 7.267 61.878 1.00 92.39 ? 618 LYS B N 1 ATOM 11901 C CA . LYS B 2 618 ? -10.497 6.785 61.747 1.00 90.39 ? 618 LYS B CA 1 ATOM 11902 C C . LYS B 2 618 ? -9.950 6.070 62.983 1.00 87.09 ? 618 LYS B C 1 ATOM 11903 O O . LYS B 2 618 ? -9.534 4.915 62.901 1.00 100.64 ? 618 LYS B O 1 ATOM 11904 C CB . LYS B 2 618 ? -9.570 7.952 61.394 1.00 83.16 ? 618 LYS B CB 1 ATOM 11905 C CG . LYS B 2 618 ? -9.480 8.252 59.907 1.00 85.65 ? 618 LYS B CG 1 ATOM 11906 C CD . LYS B 2 618 ? -8.773 7.126 59.167 1.00 98.36 ? 618 LYS B CD 1 ATOM 11907 C CE . LYS B 2 618 ? -8.581 7.460 57.697 1.00 101.07 ? 618 LYS B CE 1 ATOM 11908 N NZ . LYS B 2 618 ? -7.853 6.380 56.976 1.00 100.16 ? 618 LYS B NZ 1 ATOM 11909 N N . LYS B 2 619 ? -9.945 6.756 64.122 1.00 76.34 ? 619 LYS B N 1 ATOM 11910 C CA . LYS B 2 619 ? -9.266 6.235 65.307 1.00 73.39 ? 619 LYS B CA 1 ATOM 11911 C C . LYS B 2 619 ? -10.067 5.215 66.115 1.00 93.73 ? 619 LYS B C 1 ATOM 11912 O O . LYS B 2 619 ? -9.517 4.208 66.557 1.00 123.45 ? 619 LYS B O 1 ATOM 11913 C CB . LYS B 2 619 ? -8.844 7.389 66.217 1.00 68.74 ? 619 LYS B CB 1 ATOM 11914 C CG . LYS B 2 619 ? -7.574 8.080 65.751 1.00 70.07 ? 619 LYS B CG 1 ATOM 11915 C CD . LYS B 2 619 ? -6.528 7.052 65.338 1.00 90.71 ? 619 LYS B CD 1 ATOM 11916 C CE . LYS B 2 619 ? -5.234 7.703 64.881 1.00 93.44 ? 619 LYS B CE 1 ATOM 11917 N NZ . LYS B 2 619 ? -4.556 8.429 65.988 1.00 108.36 ? 619 LYS B NZ 1 ATOM 11918 N N . PHE B 2 620 ? -11.355 5.469 66.318 1.00 78.97 ? 620 PHE B N 1 ATOM 11919 C CA . PHE B 2 620 ? -12.163 4.572 67.138 1.00 75.20 ? 620 PHE B CA 1 ATOM 11920 C C . PHE B 2 620 ? -12.918 3.539 66.312 1.00 78.47 ? 620 PHE B C 1 ATOM 11921 O O . PHE B 2 620 ? -13.596 2.673 66.868 1.00 81.21 ? 620 PHE B O 1 ATOM 11922 C CB . PHE B 2 620 ? -13.148 5.372 67.990 1.00 77.21 ? 620 PHE B CB 1 ATOM 11923 C CG . PHE B 2 620 ? -12.509 6.070 69.153 1.00 79.34 ? 620 PHE B CG 1 ATOM 11924 C CD1 . PHE B 2 620 ? -12.364 7.446 69.160 1.00 88.37 ? 620 PHE B CD1 1 ATOM 11925 C CD2 . PHE B 2 620 ? -12.046 5.345 70.239 1.00 83.39 ? 620 PHE B CD2 1 ATOM 11926 C CE1 . PHE B 2 620 ? -11.774 8.088 70.232 1.00 102.83 ? 620 PHE B CE1 1 ATOM 11927 C CE2 . PHE B 2 620 ? -11.454 5.981 71.312 1.00 95.18 ? 620 PHE B CE2 1 ATOM 11928 C CZ . PHE B 2 620 ? -11.317 7.354 71.309 1.00 106.72 ? 620 PHE B CZ 1 ATOM 11929 N N . ASP B 2 621 ? -12.796 3.638 64.990 1.00 86.05 ? 621 ASP B N 1 ATOM 11930 C CA . ASP B 2 621 ? -13.475 2.736 64.061 1.00 89.58 ? 621 ASP B CA 1 ATOM 11931 C C . ASP B 2 621 ? -14.980 2.721 64.319 1.00 90.90 ? 621 ASP B C 1 ATOM 11932 O O . ASP B 2 621 ? -15.659 1.728 64.060 1.00 92.85 ? 621 ASP B O 1 ATOM 11933 C CB . ASP B 2 621 ? -12.900 1.319 64.165 1.00 95.04 ? 621 ASP B CB 1 ATOM 11934 C CG . ASP B 2 621 ? -13.235 0.461 62.958 1.00 96.92 ? 621 ASP B CG 1 ATOM 11935 O OD1 . ASP B 2 621 ? -13.572 -0.727 63.146 1.00 85.41 ? 621 ASP B OD1 1 ATOM 11936 O OD2 . ASP B 2 621 ? -13.160 0.977 61.823 1.00 108.72 ? 621 ASP B OD2 1 ATOM 11937 N N . ARG B 2 622 ? -15.498 3.834 64.828 1.00 97.05 ? 622 ARG B N 1 ATOM 11938 C CA . ARG B 2 622 ? -16.910 3.927 65.165 1.00 104.55 ? 622 ARG B CA 1 ATOM 11939 C C . ARG B 2 622 ? -17.660 4.673 64.073 1.00 113.95 ? 622 ARG B C 1 ATOM 11940 O O . ARG B 2 622 ? -17.130 5.591 63.448 1.00 111.06 ? 622 ARG B O 1 ATOM 11941 C CB . ARG B 2 622 ? -17.102 4.593 66.528 1.00 104.60 ? 622 ARG B CB 1 ATOM 11942 C CG . ARG B 2 622 ? -16.892 3.627 67.687 1.00 101.82 ? 622 ARG B CG 1 ATOM 11943 C CD . ARG B 2 622 ? -17.180 4.261 69.035 1.00 99.57 ? 622 ARG B CD 1 ATOM 11944 N NE . ARG B 2 622 ? -16.159 5.230 69.416 1.00 105.27 ? 622 ARG B NE 1 ATOM 11945 C CZ . ARG B 2 622 ? -16.013 5.714 70.645 1.00 106.90 ? 622 ARG B CZ 1 ATOM 11946 N NH1 . ARG B 2 622 ? -16.821 5.313 71.617 1.00 102.82 ? 622 ARG B NH1 1 ATOM 11947 N NH2 . ARG B 2 622 ? -15.056 6.594 70.902 1.00 104.07 ? 622 ARG B NH2 1 ATOM 11948 N N . GLY B 2 623 ? -18.904 4.265 63.857 1.00 125.38 ? 623 GLY B N 1 ATOM 11949 C CA . GLY B 2 623 ? -19.600 4.549 62.620 1.00 134.07 ? 623 GLY B CA 1 ATOM 11950 C C . GLY B 2 623 ? -20.145 5.938 62.356 1.00 131.29 ? 623 GLY B C 1 ATOM 11951 O O . GLY B 2 623 ? -19.720 6.931 62.948 1.00 136.61 ? 623 GLY B O 1 ATOM 11952 N N . ALA B 2 624 ? -21.075 5.955 61.405 1.00 123.28 ? 624 ALA B N 1 ATOM 11953 C CA . ALA B 2 624 ? -21.784 7.117 60.864 1.00 118.53 ? 624 ALA B CA 1 ATOM 11954 C C . ALA B 2 624 ? -20.922 7.946 59.915 1.00 110.60 ? 624 ALA B C 1 ATOM 11955 O O . ALA B 2 624 ? -21.458 8.661 59.069 1.00 111.15 ? 624 ALA B O 1 ATOM 11956 C CB . ALA B 2 624 ? -22.323 7.997 61.992 1.00 120.65 ? 624 ALA B CB 1 ATOM 11957 N N . LEU B 2 625 ? -19.600 7.863 60.035 1.00 102.38 ? 625 LEU B N 1 ATOM 11958 C CA . LEU B 2 625 ? -18.734 8.134 58.894 1.00 101.29 ? 625 LEU B CA 1 ATOM 11959 C C . LEU B 2 625 ? -18.127 6.831 58.380 1.00 98.75 ? 625 LEU B C 1 ATOM 11960 O O . LEU B 2 625 ? -17.532 6.784 57.303 1.00 95.43 ? 625 LEU B O 1 ATOM 11961 C CB . LEU B 2 625 ? -17.638 9.131 59.271 1.00 102.40 ? 625 LEU B CB 1 ATOM 11962 C CG . LEU B 2 625 ? -16.977 9.877 58.110 1.00 89.16 ? 625 LEU B CG 1 ATOM 11963 C CD1 . LEU B 2 625 ? -18.024 10.614 57.289 1.00 83.26 ? 625 LEU B CD1 1 ATOM 11964 C CD2 . LEU B 2 625 ? -15.918 10.841 58.622 1.00 82.99 ? 625 LEU B CD2 1 ATOM 11965 N N . HIS B 2 626 ? -18.295 5.772 59.167 1.00 101.45 ? 626 HIS B N 1 ATOM 11966 C CA . HIS B 2 626 ? -17.687 4.478 58.880 1.00 99.98 ? 626 HIS B CA 1 ATOM 11967 C C . HIS B 2 626 ? -18.688 3.520 58.237 1.00 108.08 ? 626 HIS B C 1 ATOM 11968 O O . HIS B 2 626 ? -18.328 2.443 57.759 1.00 130.58 ? 626 HIS B O 1 ATOM 11969 C CB . HIS B 2 626 ? -17.106 3.900 60.182 1.00 99.62 ? 626 HIS B CB 1 ATOM 11970 C CG . HIS B 2 626 ? -16.880 2.421 60.161 1.00 104.51 ? 626 HIS B CG 1 ATOM 11971 N ND1 . HIS B 2 626 ? -16.044 1.805 59.254 1.00 119.61 ? 626 HIS B ND1 1 ATOM 11972 C CD2 . HIS B 2 626 ? -17.379 1.434 60.942 1.00 99.87 ? 626 HIS B CD2 1 ATOM 11973 C CE1 . HIS B 2 626 ? -16.040 0.503 59.476 1.00 115.72 ? 626 HIS B CE1 1 ATOM 11974 N NE2 . HIS B 2 626 ? -16.842 0.251 60.495 1.00 104.89 ? 626 HIS B NE2 1 ATOM 11975 N N . ASP B 2 627 ? -19.944 3.946 58.182 1.00 104.54 ? 627 ASP B N 1 ATOM 11976 C CA . ASP B 2 627 ? -21.011 3.101 57.662 1.00 115.34 ? 627 ASP B CA 1 ATOM 11977 C C . ASP B 2 627 ? -21.052 3.123 56.140 1.00 119.88 ? 627 ASP B C 1 ATOM 11978 O O . ASP B 2 627 ? -21.346 2.114 55.500 1.00 130.15 ? 627 ASP B O 1 ATOM 11979 C CB . ASP B 2 627 ? -22.360 3.538 58.235 1.00 112.33 ? 627 ASP B CB 1 ATOM 11980 C CG . ASP B 2 627 ? -22.392 3.488 59.750 1.00 111.30 ? 627 ASP B CG 1 ATOM 11981 O OD1 . ASP B 2 627 ? -21.567 2.757 60.338 1.00 120.13 ? 627 ASP B OD1 1 ATOM 11982 O OD2 . ASP B 2 627 ? -23.242 4.176 60.353 1.00 105.04 ? 627 ASP B OD2 1 ATOM 11983 N N . GLU B 2 628 ? -20.752 4.284 55.568 1.00 105.14 ? 628 GLU B N 1 ATOM 11984 C CA . GLU B 2 628 ? -20.801 4.464 54.123 1.00 107.08 ? 628 GLU B CA 1 ATOM 11985 C C . GLU B 2 628 ? -19.434 4.228 53.489 1.00 112.46 ? 628 GLU B C 1 ATOM 11986 O O . GLU B 2 628 ? -19.258 4.437 52.287 1.00 128.15 ? 628 GLU B O 1 ATOM 11987 C CB . GLU B 2 628 ? -21.312 5.864 53.773 1.00 111.75 ? 628 GLU B CB 1 ATOM 11988 C CG . GLU B 2 628 ? -22.703 6.187 54.303 1.00 124.91 ? 628 GLU B CG 1 ATOM 11989 C CD . GLU B 2 628 ? -22.695 6.634 55.755 1.00 127.44 ? 628 GLU B CD 1 ATOM 11990 O OE1 . GLU B 2 628 ? -21.613 6.624 56.379 1.00 128.36 ? 628 GLU B OE1 1 ATOM 11991 O OE2 . GLU B 2 628 ? -23.773 6.998 56.270 1.00 123.97 ? 628 GLU B OE2 1 ATOM 11992 N N . ASN B 2 629 ? -18.472 3.813 54.312 1.00 103.80 ? 629 ASN B N 1 ATOM 11993 C CA . ASN B 2 629 ? -17.111 3.516 53.864 1.00 102.51 ? 629 ASN B CA 1 ATOM 11994 C C . ASN B 2 629 ? -16.442 4.744 53.249 1.00 99.16 ? 629 ASN B C 1 ATOM 11995 O O . ASN B 2 629 ? -15.554 4.628 52.404 1.00 99.48 ? 629 ASN B O 1 ATOM 11996 C CB . ASN B 2 629 ? -17.118 2.350 52.868 1.00 106.90 ? 629 ASN B CB 1 ATOM 11997 C CG . ASN B 2 629 ? -15.799 1.600 52.833 1.00 110.72 ? 629 ASN B CG 1 ATOM 11998 O OD1 . ASN B 2 629 ? -14.941 1.864 51.992 1.00 119.97 ? 629 ASN B OD1 1 ATOM 11999 N ND2 . ASN B 2 629 ? -15.635 0.652 53.750 1.00 105.68 ? 629 ASN B ND2 1 ATOM 12000 N N . THR B 2 630 ? -16.878 5.920 53.687 1.00 96.79 ? 630 THR B N 1 ATOM 12001 C CA . THR B 2 630 ? -16.368 7.184 53.170 1.00 100.66 ? 630 THR B CA 1 ATOM 12002 C C . THR B 2 630 ? -15.224 7.722 54.022 1.00 110.15 ? 630 THR B C 1 ATOM 12003 O O . THR B 2 630 ? -14.735 8.827 53.788 1.00 110.06 ? 630 THR B O 1 ATOM 12004 C CB . THR B 2 630 ? -17.475 8.252 53.101 1.00 95.46 ? 630 THR B CB 1 ATOM 12005 O OG1 . THR B 2 630 ? -17.869 8.623 54.428 1.00 90.70 ? 630 THR B OG1 1 ATOM 12006 C CG2 . THR B 2 630 ? -18.681 7.722 52.350 1.00 99.97 ? 630 THR B CG2 1 ATOM 12007 N N . CYS B 2 631 ? -14.815 6.941 55.018 1.00 114.07 ? 631 CYS B N 1 ATOM 12008 C CA . CYS B 2 631 ? -13.787 7.356 55.968 1.00 113.72 ? 631 CYS B CA 1 ATOM 12009 C C . CYS B 2 631 ? -12.485 7.779 55.290 1.00 110.66 ? 631 CYS B C 1 ATOM 12010 O O . CYS B 2 631 ? -12.098 8.946 55.350 1.00 111.33 ? 631 CYS B O 1 ATOM 12011 C CB . CYS B 2 631 ? -13.506 6.229 56.964 1.00 125.17 ? 631 CYS B CB 1 ATOM 12012 S SG . CYS B 2 631 ? -12.265 6.631 58.213 1.00 183.28 ? 631 CYS B SG 1 ATOM 12013 N N . ASN B 2 632 ? -11.817 6.827 54.645 1.00 113.26 ? 632 ASN B N 1 ATOM 12014 C CA . ASN B 2 632 ? -10.533 7.088 54.003 1.00 118.44 ? 632 ASN B CA 1 ATOM 12015 C C . ASN B 2 632 ? -10.623 8.109 52.871 1.00 124.95 ? 632 ASN B C 1 ATOM 12016 O O . ASN B 2 632 ? -9.679 8.861 52.629 1.00 131.50 ? 632 ASN B O 1 ATOM 12017 C CB . ASN B 2 632 ? -9.935 5.784 53.469 1.00 125.30 ? 632 ASN B CB 1 ATOM 12018 C CG . ASN B 2 632 ? -9.492 4.849 54.577 1.00 134.09 ? 632 ASN B CG 1 ATOM 12019 O OD1 . ASN B 2 632 ? -9.930 4.972 55.721 1.00 137.05 ? 632 ASN B OD1 1 ATOM 12020 N ND2 . ASN B 2 632 ? -8.616 3.908 54.242 1.00 137.68 ? 632 ASN B ND2 1 ATOM 12021 N N . ARG B 2 633 ? -11.759 8.131 52.182 1.00 123.88 ? 633 ARG B N 1 ATOM 12022 C CA . ARG B 2 633 ? -11.938 9.018 51.038 1.00 122.00 ? 633 ARG B CA 1 ATOM 12023 C C . ARG B 2 633 ? -12.190 10.469 51.439 1.00 118.98 ? 633 ARG B C 1 ATOM 12024 O O . ARG B 2 633 ? -11.562 11.382 50.905 1.00 122.43 ? 633 ARG B O 1 ATOM 12025 C CB . ARG B 2 633 ? -13.091 8.525 50.163 1.00 122.81 ? 633 ARG B CB 1 ATOM 12026 C CG . ARG B 2 633 ? -13.476 9.483 49.046 1.00 122.77 ? 633 ARG B CG 1 ATOM 12027 C CD . ARG B 2 633 ? -12.345 9.669 48.055 1.00 127.31 ? 633 ARG B CD 1 ATOM 12028 N NE . ARG B 2 633 ? -11.971 8.415 47.408 1.00 115.48 ? 633 ARG B NE 1 ATOM 12029 C CZ . ARG B 2 633 ? -12.523 7.961 46.288 1.00 117.16 ? 633 ARG B CZ 1 ATOM 12030 N NH1 . ARG B 2 633 ? -13.475 8.659 45.686 1.00 116.49 ? 633 ARG B NH1 1 ATOM 12031 N NH2 . ARG B 2 633 ? -12.121 6.809 45.769 1.00 120.56 ? 633 ARG B NH2 1 ATOM 12032 N N . TYR B 2 634 ? -13.102 10.679 52.383 1.00 114.52 ? 634 TYR B N 1 ATOM 12033 C CA . TYR B 2 634 ? -13.509 12.034 52.744 1.00 115.00 ? 634 TYR B CA 1 ATOM 12034 C C . TYR B 2 634 ? -12.438 12.752 53.554 1.00 126.48 ? 634 TYR B C 1 ATOM 12035 O O . TYR B 2 634 ? -11.838 13.715 53.075 1.00 150.01 ? 634 TYR B O 1 ATOM 12036 C CB . TYR B 2 634 ? -14.830 12.015 53.516 1.00 106.53 ? 634 TYR B CB 1 ATOM 12037 C CG . TYR B 2 634 ? -16.052 12.037 52.624 1.00 106.34 ? 634 TYR B CG 1 ATOM 12038 C CD1 . TYR B 2 634 ? -15.935 12.283 51.262 1.00 109.51 ? 634 TYR B CD1 1 ATOM 12039 C CD2 . TYR B 2 634 ? -17.322 11.825 53.144 1.00 110.12 ? 634 TYR B CD2 1 ATOM 12040 C CE1 . TYR B 2 634 ? -17.046 12.308 50.441 1.00 110.45 ? 634 TYR B CE1 1 ATOM 12041 C CE2 . TYR B 2 634 ? -18.441 11.848 52.330 1.00 114.62 ? 634 TYR B CE2 1 ATOM 12042 C CZ . TYR B 2 634 ? -18.296 12.090 50.980 1.00 111.49 ? 634 TYR B CZ 1 ATOM 12043 O OH . TYR B 2 634 ? -19.404 12.115 50.165 1.00 109.52 ? 634 TYR B OH 1 ATOM 12044 N N . CYS B 2 635 ? -12.191 12.291 54.775 1.00 116.14 ? 635 CYS B N 1 ATOM 12045 C CA . CYS B 2 635 ? -11.170 12.922 55.599 1.00 122.62 ? 635 CYS B CA 1 ATOM 12046 C C . CYS B 2 635 ? -9.832 12.208 55.445 1.00 130.32 ? 635 CYS B C 1 ATOM 12047 O O . CYS B 2 635 ? -9.657 11.077 55.898 1.00 130.14 ? 635 CYS B O 1 ATOM 12048 C CB . CYS B 2 635 ? -11.599 12.951 57.070 1.00 128.52 ? 635 CYS B CB 1 ATOM 12049 S SG . CYS B 2 635 ? -12.140 11.365 57.753 1.00 83.29 ? 635 CYS B SG 1 ATOM 12050 N N . ARG B 2 636 ? -8.891 12.883 54.794 1.00 139.54 ? 636 ARG B N 1 ATOM 12051 C CA . ARG B 2 636 ? -7.542 12.362 54.623 1.00 143.93 ? 636 ARG B CA 1 ATOM 12052 C C . ARG B 2 636 ? -6.636 12.938 55.705 1.00 144.94 ? 636 ARG B C 1 ATOM 12053 O O . ARG B 2 636 ? -5.426 12.707 55.709 1.00 147.95 ? 636 ARG B O 1 ATOM 12054 C CB . ARG B 2 636 ? -7.001 12.691 53.228 1.00 147.87 ? 636 ARG B CB 1 ATOM 12055 C CG . ARG B 2 636 ? -5.872 11.778 52.770 1.00 152.99 ? 636 ARG B CG 1 ATOM 12056 C CD . ARG B 2 636 ? -5.306 12.212 51.428 1.00 165.17 ? 636 ARG B CD 1 ATOM 12057 N NE . ARG B 2 636 ? -4.181 11.376 51.021 1.00 178.94 ? 636 ARG B NE 1 ATOM 12058 C CZ . ARG B 2 636 ? -3.461 11.574 49.921 1.00 182.24 ? 636 ARG B CZ 1 ATOM 12059 N NH1 . ARG B 2 636 ? -3.747 12.585 49.112 1.00 184.28 ? 636 ARG B NH1 1 ATOM 12060 N NH2 . ARG B 2 636 ? -2.454 10.761 49.630 1.00 179.11 ? 636 ARG B NH2 1 ATOM 12061 N N . ASP B 2 637 ? -7.238 13.702 56.612 1.00 142.45 ? 637 ASP B N 1 ATOM 12062 C CA . ASP B 2 637 ? -6.511 14.344 57.700 1.00 144.82 ? 637 ASP B CA 1 ATOM 12063 C C . ASP B 2 637 ? -5.733 13.321 58.518 1.00 147.33 ? 637 ASP B C 1 ATOM 12064 O O . ASP B 2 637 ? -6.302 12.341 59.000 1.00 161.58 ? 637 ASP B O 1 ATOM 12065 C CB . ASP B 2 637 ? -7.477 15.108 58.608 1.00 149.04 ? 637 ASP B CB 1 ATOM 12066 C CG . ASP B 2 637 ? -8.560 15.832 57.831 1.00 160.53 ? 637 ASP B CG 1 ATOM 12067 O OD1 . ASP B 2 637 ? -8.348 16.116 56.633 1.00 169.42 ? 637 ASP B OD1 1 ATOM 12068 O OD2 . ASP B 2 637 ? -9.625 16.117 58.419 1.00 159.99 ? 637 ASP B OD2 1 ATOM 12069 N N . GLU B 2 638 ? -4.433 13.549 58.673 1.00 141.17 ? 638 GLU B N 1 ATOM 12070 C CA . GLU B 2 638 ? -3.600 12.622 59.427 1.00 140.62 ? 638 GLU B CA 1 ATOM 12071 C C . GLU B 2 638 ? -3.809 12.819 60.924 1.00 128.13 ? 638 GLU B C 1 ATOM 12072 O O . GLU B 2 638 ? -3.783 13.943 61.428 1.00 124.47 ? 638 GLU B O 1 ATOM 12073 C CB . GLU B 2 638 ? -2.121 12.785 59.060 1.00 150.21 ? 638 GLU B CB 1 ATOM 12074 C CG . GLU B 2 638 ? -1.541 14.171 59.293 1.00 153.05 ? 638 GLU B CG 1 ATOM 12075 C CD . GLU B 2 638 ? -0.036 14.203 59.106 1.00 156.61 ? 638 GLU B CD 1 ATOM 12076 O OE1 . GLU B 2 638 ? 0.531 13.176 58.678 1.00 160.47 ? 638 GLU B OE1 1 ATOM 12077 O OE2 . GLU B 2 638 ? 0.580 15.252 59.389 1.00 156.76 ? 638 GLU B OE2 1 ATOM 12078 N N . ILE B 2 639 ? -4.037 11.716 61.627 1.00 122.00 ? 639 ILE B N 1 ATOM 12079 C CA . ILE B 2 639 ? -4.288 11.769 63.059 1.00 110.16 ? 639 ILE B CA 1 ATOM 12080 C C . ILE B 2 639 ? -3.171 11.087 63.837 1.00 113.79 ? 639 ILE B C 1 ATOM 12081 O O . ILE B 2 639 ? -3.007 9.868 63.774 1.00 122.03 ? 639 ILE B O 1 ATOM 12082 C CB . ILE B 2 639 ? -5.631 11.111 63.418 1.00 101.74 ? 639 ILE B CB 1 ATOM 12083 C CG1 . ILE B 2 639 ? -6.749 11.673 62.538 1.00 98.89 ? 639 ILE B CG1 1 ATOM 12084 C CG2 . ILE B 2 639 ? -5.946 11.317 64.890 1.00 101.92 ? 639 ILE B CG2 1 ATOM 12085 C CD1 . ILE B 2 639 ? -8.103 11.057 62.802 1.00 94.31 ? 639 ILE B CD1 1 ATOM 12086 N N . GLU B 2 640 ? -2.401 11.885 64.567 1.00 113.13 ? 640 GLU B N 1 ATOM 12087 C CA . GLU B 2 640 ? -1.335 11.361 65.408 1.00 115.21 ? 640 GLU B CA 1 ATOM 12088 C C . GLU B 2 640 ? -1.736 11.461 66.873 1.00 106.70 ? 640 GLU B C 1 ATOM 12089 O O . GLU B 2 640 ? -1.872 12.558 67.412 1.00 113.95 ? 640 GLU B O 1 ATOM 12090 C CB . GLU B 2 640 ? -0.029 12.118 65.161 1.00 130.10 ? 640 GLU B CB 1 ATOM 12091 C CG . GLU B 2 640 ? 1.129 11.661 66.034 1.00 141.02 ? 640 GLU B CG 1 ATOM 12092 C CD . GLU B 2 640 ? 2.364 12.522 65.856 1.00 146.08 ? 640 GLU B CD 1 ATOM 12093 O OE1 . GLU B 2 640 ? 2.304 13.497 65.078 1.00 145.13 ? 640 GLU B OE1 1 ATOM 12094 O OE2 . GLU B 2 640 ? 3.396 12.225 66.496 1.00 147.80 ? 640 GLU B OE2 1 ATOM 12095 N N . SER B 2 641 ? -1.929 10.312 67.512 1.00 103.95 ? 641 SER B N 1 ATOM 12096 C CA . SER B 2 641 ? -2.315 10.294 68.915 1.00 104.40 ? 641 SER B CA 1 ATOM 12097 C C . SER B 2 641 ? -1.160 10.774 69.782 1.00 113.17 ? 641 SER B C 1 ATOM 12098 O O . SER B 2 641 ? -0.062 10.219 69.738 1.00 124.82 ? 641 SER B O 1 ATOM 12099 C CB . SER B 2 641 ? -2.753 8.891 69.339 1.00 107.73 ? 641 SER B CB 1 ATOM 12100 O OG . SER B 2 641 ? -3.123 8.864 70.707 1.00 106.65 ? 641 SER B OG 1 ATOM 12101 N N . VAL B 2 642 ? -1.417 11.810 70.572 1.00 116.15 ? 642 VAL B N 1 ATOM 12102 C CA . VAL B 2 642 ? -0.394 12.393 71.427 1.00 120.26 ? 642 VAL B CA 1 ATOM 12103 C C . VAL B 2 642 ? -0.602 11.907 72.857 1.00 116.16 ? 642 VAL B C 1 ATOM 12104 O O . VAL B 2 642 ? -1.735 11.694 73.290 1.00 119.43 ? 642 VAL B O 1 ATOM 12105 C CB . VAL B 2 642 ? -0.418 13.939 71.361 1.00 118.35 ? 642 VAL B CB 1 ATOM 12106 C CG1 . VAL B 2 642 ? -1.763 14.482 71.828 1.00 110.57 ? 642 VAL B CG1 1 ATOM 12107 C CG2 . VAL B 2 642 ? 0.728 14.539 72.167 1.00 119.65 ? 642 VAL B CG2 1 ATOM 12108 N N . LYS B 2 643 ? 0.492 11.717 73.588 1.00 132.93 ? 643 LYS B N 1 ATOM 12109 C CA . LYS B 2 643 ? 0.400 11.167 74.930 1.00 145.26 ? 643 LYS B CA 1 ATOM 12110 C C . LYS B 2 643 ? 0.286 12.276 75.964 1.00 138.88 ? 643 LYS B C 1 ATOM 12111 O O . LYS B 2 643 ? 1.245 13.008 76.213 1.00 142.69 ? 643 LYS B O 1 ATOM 12112 C CB . LYS B 2 643 ? 1.622 10.291 75.225 1.00 156.57 ? 643 LYS B CB 1 ATOM 12113 C CG . LYS B 2 643 ? 1.788 9.895 76.685 1.00 151.00 ? 643 LYS B CG 1 ATOM 12114 C CD . LYS B 2 643 ? 3.050 9.070 76.884 1.00 143.95 ? 643 LYS B CD 1 ATOM 12115 C CE . LYS B 2 643 ? 3.247 8.696 78.343 1.00 137.49 ? 643 LYS B CE 1 ATOM 12116 N NZ . LYS B 2 643 ? 4.506 7.928 78.550 1.00 137.57 ? 643 LYS B NZ 1 ATOM 12117 N N . GLU B 2 644 ? -0.909 12.407 76.536 1.00 140.62 ? 644 GLU B N 1 ATOM 12118 C CA . GLU B 2 644 ? -1.166 13.282 77.681 1.00 151.36 ? 644 GLU B CA 1 ATOM 12119 C C . GLU B 2 644 ? -0.932 14.767 77.392 1.00 151.18 ? 644 GLU B C 1 ATOM 12120 O O . GLU B 2 644 ? -1.236 15.619 78.227 1.00 157.23 ? 644 GLU B O 1 ATOM 12121 C CB . GLU B 2 644 ? -0.309 12.850 78.877 1.00 169.89 ? 644 GLU B CB 1 ATOM 12122 C CG . GLU B 2 644 ? -0.441 11.377 79.240 1.00 178.88 ? 644 GLU B CG 1 ATOM 12123 C CD . GLU B 2 644 ? -1.846 10.998 79.669 1.00 176.46 ? 644 GLU B CD 1 ATOM 12124 O OE1 . GLU B 2 644 ? -2.567 11.868 80.201 1.00 176.33 ? 644 GLU B OE1 1 ATOM 12125 O OE2 . GLU B 2 644 ? -2.231 9.826 79.473 1.00 169.62 ? 644 GLU B OE2 1 ATOM 12126 N N . LEU B 2 645 ? -0.403 15.076 76.213 1.00 143.82 ? 645 LEU B N 1 ATOM 12127 C CA . LEU B 2 645 ? 0.114 16.411 75.946 1.00 144.36 ? 645 LEU B CA 1 ATOM 12128 C C . LEU B 2 645 ? -0.703 17.232 74.956 1.00 140.80 ? 645 LEU B C 1 ATOM 12129 O O . LEU B 2 645 ? -0.749 16.932 73.764 1.00 141.32 ? 645 LEU B O 1 ATOM 12130 C CB . LEU B 2 645 ? 1.555 16.318 75.438 1.00 153.66 ? 645 LEU B CB 1 ATOM 12131 C CG . LEU B 2 645 ? 2.630 15.984 76.473 1.00 155.51 ? 645 LEU B CG 1 ATOM 12132 C CD1 . LEU B 2 645 ? 3.996 15.881 75.811 1.00 154.29 ? 645 LEU B CD1 1 ATOM 12133 C CD2 . LEU B 2 645 ? 2.644 17.027 77.579 1.00 150.39 ? 645 LEU B CD2 1 ATOM 12134 N N . LYS B 2 646 ? -1.344 18.274 75.471 1.00 138.57 ? 646 LYS B N 1 ATOM 12135 C CA . LYS B 2 646 ? -1.799 19.375 74.640 1.00 134.73 ? 646 LYS B CA 1 ATOM 12136 C C . LYS B 2 646 ? -0.794 20.497 74.858 1.00 141.75 ? 646 LYS B C 1 ATOM 12137 O O . LYS B 2 646 ? -0.614 20.968 75.981 1.00 142.94 ? 646 LYS B O 1 ATOM 12138 C CB . LYS B 2 646 ? -3.222 19.803 74.996 1.00 128.70 ? 646 LYS B CB 1 ATOM 12139 C CG . LYS B 2 646 ? -4.257 18.719 74.751 1.00 123.87 ? 646 LYS B CG 1 ATOM 12140 C CD . LYS B 2 646 ? -5.671 19.218 74.994 1.00 136.23 ? 646 LYS B CD 1 ATOM 12141 C CE . LYS B 2 646 ? -6.067 20.279 73.980 1.00 154.88 ? 646 LYS B CE 1 ATOM 12142 N NZ . LYS B 2 646 ? -7.464 20.748 74.193 1.00 160.23 ? 646 LYS B NZ 1 ATOM 12143 N N . ASP B 2 647 ? -0.140 20.919 73.782 1.00 153.15 ? 647 ASP B N 1 ATOM 12144 C CA . ASP B 2 647 ? 1.084 21.708 73.886 1.00 162.51 ? 647 ASP B CA 1 ATOM 12145 C C . ASP B 2 647 ? 0.845 23.126 74.395 1.00 166.03 ? 647 ASP B C 1 ATOM 12146 O O . ASP B 2 647 ? -0.281 23.499 74.726 1.00 160.92 ? 647 ASP B O 1 ATOM 12147 C CB . ASP B 2 647 ? 1.781 21.761 72.526 1.00 162.55 ? 647 ASP B CB 1 ATOM 12148 C CG . ASP B 2 647 ? 1.604 20.481 71.732 1.00 157.66 ? 647 ASP B CG 1 ATOM 12149 O OD1 . ASP B 2 647 ? 2.349 19.511 71.985 1.00 157.43 ? 647 ASP B OD1 1 ATOM 12150 O OD2 . ASP B 2 647 ? 0.716 20.445 70.854 1.00 152.63 ? 647 ASP B OD2 1 ATOM 12151 N N . THR B 2 648 ? 1.923 23.905 74.458 1.00 173.67 ? 648 THR B N 1 ATOM 12152 C CA . THR B 2 648 ? 1.867 25.297 74.902 1.00 177.82 ? 648 THR B CA 1 ATOM 12153 C C . THR B 2 648 ? 0.868 26.103 74.081 1.00 173.43 ? 648 THR B C 1 ATOM 12154 O O . THR B 2 648 ? 0.341 27.116 74.540 1.00 173.69 ? 648 THR B O 1 ATOM 12155 C CB . THR B 2 648 ? 3.249 25.972 74.813 1.00 184.29 ? 648 THR B CB 1 ATOM 12156 O OG1 . THR B 2 648 ? 3.112 27.377 75.055 1.00 190.33 ? 648 THR B OG1 1 ATOM 12157 C CG2 . THR B 2 648 ? 3.861 25.760 73.436 1.00 184.68 ? 648 THR B CG2 1 ATOM 12158 N N . GLY B 2 649 ? 0.613 25.639 72.864 1.00 168.96 ? 649 GLY B N 1 ATOM 12159 C CA . GLY B 2 649 ? -0.402 26.227 72.018 1.00 171.92 ? 649 GLY B CA 1 ATOM 12160 C C . GLY B 2 649 ? 0.136 27.113 70.917 1.00 178.84 ? 649 GLY B C 1 ATOM 12161 O O . GLY B 2 649 ? 1.169 27.766 71.056 1.00 184.08 ? 649 GLY B O 1 ATOM 12162 N N . LYS B 2 650 ? -0.609 27.134 69.820 1.00 173.08 ? 650 LYS B N 1 ATOM 12163 C CA . LYS B 2 650 ? -0.333 27.946 68.643 1.00 164.04 ? 650 LYS B CA 1 ATOM 12164 C C . LYS B 2 650 ? -1.712 28.362 68.174 1.00 154.55 ? 650 LYS B C 1 ATOM 12165 O O . LYS B 2 650 ? -2.675 28.212 68.928 1.00 151.82 ? 650 LYS B O 1 ATOM 12166 C CB . LYS B 2 650 ? 0.414 27.166 67.555 1.00 165.13 ? 650 LYS B CB 1 ATOM 12167 C CG . LYS B 2 650 ? 1.641 26.395 68.028 1.00 170.34 ? 650 LYS B CG 1 ATOM 12168 C CD . LYS B 2 650 ? 2.779 27.321 68.421 1.00 174.84 ? 650 LYS B CD 1 ATOM 12169 C CE . LYS B 2 650 ? 3.912 26.542 69.071 1.00 174.64 ? 650 LYS B CE 1 ATOM 12170 N NZ . LYS B 2 650 ? 4.999 27.436 69.557 1.00 179.55 ? 650 LYS B NZ 1 ATOM 12171 N N . ASP B 2 651 ? -1.833 28.907 66.968 1.00 154.48 ? 651 ASP B N 1 ATOM 12172 C CA . ASP B 2 651 ? -3.170 29.064 66.420 1.00 154.32 ? 651 ASP B CA 1 ATOM 12173 C C . ASP B 2 651 ? -3.766 27.662 66.350 1.00 157.04 ? 651 ASP B C 1 ATOM 12174 O O . ASP B 2 651 ? -3.226 26.777 65.685 1.00 157.10 ? 651 ASP B O 1 ATOM 12175 C CB . ASP B 2 651 ? -3.141 29.736 65.046 1.00 153.58 ? 651 ASP B CB 1 ATOM 12176 C CG . ASP B 2 651 ? -2.201 29.047 64.078 1.00 157.69 ? 651 ASP B CG 1 ATOM 12177 O OD1 . ASP B 2 651 ? -2.546 28.947 62.881 1.00 157.21 ? 651 ASP B OD1 1 ATOM 12178 O OD2 . ASP B 2 651 ? -1.118 28.602 64.513 1.00 160.29 ? 651 ASP B OD2 1 ATOM 12179 N N . ALA B 2 652 ? -4.878 27.462 67.047 1.00 155.90 ? 652 ALA B N 1 ATOM 12180 C CA . ALA B 2 652 ? -5.427 26.123 67.217 1.00 146.23 ? 652 ALA B CA 1 ATOM 12181 C C . ALA B 2 652 ? -6.887 26.157 67.634 1.00 146.68 ? 652 ALA B C 1 ATOM 12182 O O . ALA B 2 652 ? -7.387 27.176 68.110 1.00 161.21 ? 652 ALA B O 1 ATOM 12183 C CB . ALA B 2 652 ? -4.607 25.344 68.237 1.00 133.61 ? 652 ALA B CB 1 ATOM 12184 N N . VAL B 2 653 ? -7.566 25.030 67.458 1.00 128.66 ? 653 VAL B N 1 ATOM 12185 C CA . VAL B 2 653 ? -8.925 24.876 67.950 1.00 124.23 ? 653 VAL B CA 1 ATOM 12186 C C . VAL B 2 653 ? -9.004 23.662 68.868 1.00 128.97 ? 653 VAL B C 1 ATOM 12187 O O . VAL B 2 653 ? -8.815 22.528 68.429 1.00 129.82 ? 653 VAL B O 1 ATOM 12188 C CB . VAL B 2 653 ? -9.934 24.722 66.801 1.00 123.51 ? 653 VAL B CB 1 ATOM 12189 C CG1 . VAL B 2 653 ? -11.340 24.546 67.351 1.00 125.21 ? 653 VAL B CG1 1 ATOM 12190 C CG2 . VAL B 2 653 ? -9.867 25.926 65.875 1.00 135.01 ? 653 VAL B CG2 1 ATOM 12191 N N . ASN B 2 654 ? -9.285 23.906 70.143 1.00 135.65 ? 654 ASN B N 1 ATOM 12192 C CA . ASN B 2 654 ? -9.367 22.828 71.119 1.00 122.54 ? 654 ASN B CA 1 ATOM 12193 C C . ASN B 2 654 ? -10.796 22.318 71.231 1.00 109.27 ? 654 ASN B C 1 ATOM 12194 O O . ASN B 2 654 ? -11.682 23.025 71.709 1.00 130.33 ? 654 ASN B O 1 ATOM 12195 C CB . ASN B 2 654 ? -8.866 23.298 72.485 1.00 134.54 ? 654 ASN B CB 1 ATOM 12196 C CG . ASN B 2 654 ? -7.522 23.996 72.405 1.00 141.56 ? 654 ASN B CG 1 ATOM 12197 O OD1 . ASN B 2 654 ? -6.472 23.361 72.495 1.00 135.52 ? 654 ASN B OD1 1 ATOM 12198 N ND2 . ASN B 2 654 ? -7.550 25.313 72.238 1.00 142.55 ? 654 ASN B ND2 1 ATOM 12199 N N . CYS B 2 655 ? -11.013 21.085 70.790 1.00 98.17 ? 655 CYS B N 1 ATOM 12200 C CA . CYS B 2 655 ? -12.354 20.518 70.763 1.00 99.24 ? 655 CYS B CA 1 ATOM 12201 C C . CYS B 2 655 ? -12.478 19.279 71.639 1.00 92.96 ? 655 CYS B C 1 ATOM 12202 O O . CYS B 2 655 ? -11.609 18.407 71.635 1.00 103.30 ? 655 CYS B O 1 ATOM 12203 C CB . CYS B 2 655 ? -12.757 20.177 69.329 1.00 97.49 ? 655 CYS B CB 1 ATOM 12204 S SG . CYS B 2 655 ? -13.274 21.593 68.332 1.00 149.46 ? 655 CYS B SG 1 ATOM 12205 N N . THR B 2 656 ? -13.570 19.217 72.392 1.00 86.03 ? 656 THR B N 1 ATOM 12206 C CA . THR B 2 656 ? -13.875 18.061 73.223 1.00 83.95 ? 656 THR B CA 1 ATOM 12207 C C . THR B 2 656 ? -15.299 17.595 72.950 1.00 77.94 ? 656 THR B C 1 ATOM 12208 O O . THR B 2 656 ? -16.102 18.339 72.385 1.00 78.00 ? 656 THR B O 1 ATOM 12209 C CB . THR B 2 656 ? -13.718 18.375 74.722 1.00 79.40 ? 656 THR B CB 1 ATOM 12210 O OG1 . THR B 2 656 ? -14.695 19.348 75.113 1.00 79.79 ? 656 THR B OG1 1 ATOM 12211 C CG2 . THR B 2 656 ? -12.325 18.913 75.016 1.00 80.33 ? 656 THR B CG2 1 ATOM 12212 N N . TYR B 2 657 ? -15.612 16.375 73.379 1.00 77.65 ? 657 TYR B N 1 ATOM 12213 C CA . TYR B 2 657 ? -16.926 15.779 73.155 1.00 77.23 ? 657 TYR B CA 1 ATOM 12214 C C . TYR B 2 657 ? -17.025 14.427 73.848 1.00 77.43 ? 657 TYR B C 1 ATOM 12215 O O . TYR B 2 657 ? -16.014 13.837 74.228 1.00 77.87 ? 657 TYR B O 1 ATOM 12216 C CB . TYR B 2 657 ? -17.208 15.611 71.657 1.00 84.11 ? 657 TYR B CB 1 ATOM 12217 C CG . TYR B 2 657 ? -16.439 14.481 71.009 1.00 76.32 ? 657 TYR B CG 1 ATOM 12218 C CD1 . TYR B 2 657 ? -17.033 13.243 70.798 1.00 89.16 ? 657 TYR B CD1 1 ATOM 12219 C CD2 . TYR B 2 657 ? -15.121 14.651 70.609 1.00 76.60 ? 657 TYR B CD2 1 ATOM 12220 C CE1 . TYR B 2 657 ? -16.336 12.207 70.209 1.00 100.31 ? 657 TYR B CE1 1 ATOM 12221 C CE2 . TYR B 2 657 ? -14.415 13.620 70.017 1.00 92.31 ? 657 TYR B CE2 1 ATOM 12222 C CZ . TYR B 2 657 ? -15.028 12.400 69.821 1.00 97.40 ? 657 TYR B CZ 1 ATOM 12223 O OH . TYR B 2 657 ? -14.332 11.368 69.234 1.00 77.24 ? 657 TYR B OH 1 ATOM 12224 N N . LYS B 2 658 ? -18.250 13.938 74.001 1.00 77.48 ? 658 LYS B N 1 ATOM 12225 C CA . LYS B 2 658 ? -18.486 12.660 74.657 1.00 78.86 ? 658 LYS B CA 1 ATOM 12226 C C . LYS B 2 658 ? -18.874 11.603 73.628 1.00 78.48 ? 658 LYS B C 1 ATOM 12227 O O . LYS B 2 658 ? -19.711 11.851 72.760 1.00 77.15 ? 658 LYS B O 1 ATOM 12228 C CB . LYS B 2 658 ? -19.575 12.799 75.722 1.00 83.56 ? 658 LYS B CB 1 ATOM 12229 C CG . LYS B 2 658 ? -19.504 11.754 76.820 1.00 91.03 ? 658 LYS B CG 1 ATOM 12230 C CD . LYS B 2 658 ? -20.632 11.920 77.825 1.00 97.94 ? 658 LYS B CD 1 ATOM 12231 C CE . LYS B 2 658 ? -21.986 11.669 77.182 1.00 106.48 ? 658 LYS B CE 1 ATOM 12232 N NZ . LYS B 2 658 ? -23.092 11.717 78.178 1.00 115.68 ? 658 LYS B NZ 1 ATOM 12233 N N . ASN B 2 659 ? -18.261 10.428 73.726 1.00 78.32 ? 659 ASN B N 1 ATOM 12234 C CA . ASN B 2 659 ? -18.513 9.355 72.770 1.00 79.98 ? 659 ASN B CA 1 ATOM 12235 C C . ASN B 2 659 ? -19.629 8.415 73.215 1.00 84.48 ? 659 ASN B C 1 ATOM 12236 O O . ASN B 2 659 ? -20.303 8.665 74.214 1.00 87.10 ? 659 ASN B O 1 ATOM 12237 C CB . ASN B 2 659 ? -17.230 8.556 72.520 1.00 91.61 ? 659 ASN B CB 1 ATOM 12238 C CG . ASN B 2 659 ? -16.611 8.018 73.801 1.00 108.31 ? 659 ASN B CG 1 ATOM 12239 O OD1 . ASN B 2 659 ? -17.246 7.996 74.856 1.00 119.75 ? 659 ASN B OD1 1 ATOM 12240 N ND2 . ASN B 2 659 ? -15.361 7.579 73.712 1.00 104.88 ? 659 ASN B ND2 1 ATOM 12241 N N . GLU B 2 660 ? -19.811 7.332 72.465 1.00 85.92 ? 660 GLU B N 1 ATOM 12242 C CA . GLU B 2 660 ? -20.808 6.317 72.792 1.00 90.04 ? 660 GLU B CA 1 ATOM 12243 C C . GLU B 2 660 ? -20.511 5.666 74.137 1.00 91.99 ? 660 GLU B C 1 ATOM 12244 O O . GLU B 2 660 ? -21.409 5.156 74.806 1.00 110.21 ? 660 GLU B O 1 ATOM 12245 C CB . GLU B 2 660 ? -20.860 5.245 71.701 1.00 93.75 ? 660 GLU B CB 1 ATOM 12246 C CG . GLU B 2 660 ? -21.110 5.778 70.301 1.00 106.88 ? 660 GLU B CG 1 ATOM 12247 C CD . GLU B 2 660 ? -20.991 4.697 69.242 1.00 120.17 ? 660 GLU B CD 1 ATOM 12248 O OE1 . GLU B 2 660 ? -20.651 3.549 69.599 1.00 128.64 ? 660 GLU B OE1 1 ATOM 12249 O OE2 . GLU B 2 660 ? -21.234 4.996 68.054 1.00 118.85 ? 660 GLU B OE2 1 ATOM 12250 N N . ASP B 2 661 ? -19.241 5.695 74.528 1.00 91.32 ? 661 ASP B N 1 ATOM 12251 C CA . ASP B 2 661 ? -18.789 5.063 75.760 1.00 102.20 ? 661 ASP B CA 1 ATOM 12252 C C . ASP B 2 661 ? -18.876 6.024 76.941 1.00 105.63 ? 661 ASP B C 1 ATOM 12253 O O . ASP B 2 661 ? -18.420 5.707 78.040 1.00 119.98 ? 661 ASP B O 1 ATOM 12254 C CB . ASP B 2 661 ? -17.356 4.552 75.601 1.00 109.03 ? 661 ASP B CB 1 ATOM 12255 C CG . ASP B 2 661 ? -17.210 3.583 74.444 1.00 114.31 ? 661 ASP B CG 1 ATOM 12256 O OD1 . ASP B 2 661 ? -18.207 2.916 74.097 1.00 112.92 ? 661 ASP B OD1 1 ATOM 12257 O OD2 . ASP B 2 661 ? -16.099 3.489 73.882 1.00 119.32 ? 661 ASP B OD2 1 ATOM 12258 N N . ASP B 2 662 ? -19.443 7.202 76.689 1.00 92.35 ? 662 ASP B N 1 ATOM 12259 C CA . ASP B 2 662 ? -19.611 8.243 77.701 1.00 90.52 ? 662 ASP B CA 1 ATOM 12260 C C . ASP B 2 662 ? -18.264 8.720 78.231 1.00 85.25 ? 662 ASP B C 1 ATOM 12261 O O . ASP B 2 662 ? -18.144 9.118 79.390 1.00 85.84 ? 662 ASP B O 1 ATOM 12262 C CB . ASP B 2 662 ? -20.493 7.750 78.852 1.00 96.90 ? 662 ASP B CB 1 ATOM 12263 C CG . ASP B 2 662 ? -21.888 7.371 78.395 1.00 113.21 ? 662 ASP B CG 1 ATOM 12264 O OD1 . ASP B 2 662 ? -22.429 8.056 77.502 1.00 122.31 ? 662 ASP B OD1 1 ATOM 12265 O OD2 . ASP B 2 662 ? -22.442 6.386 78.927 1.00 120.29 ? 662 ASP B OD2 1 ATOM 12266 N N . CYS B 2 663 ? -17.253 8.677 77.370 1.00 82.85 ? 663 CYS B N 1 ATOM 12267 C CA . CYS B 2 663 ? -15.925 9.167 77.711 1.00 83.15 ? 663 CYS B CA 1 ATOM 12268 C C . CYS B 2 663 ? -15.644 10.465 76.963 1.00 81.47 ? 663 CYS B C 1 ATOM 12269 O O . CYS B 2 663 ? -16.056 10.627 75.814 1.00 80.24 ? 663 CYS B O 1 ATOM 12270 C CB . CYS B 2 663 ? -14.860 8.119 77.383 1.00 90.52 ? 663 CYS B CB 1 ATOM 12271 S SG . CYS B 2 663 ? -15.107 6.523 78.200 1.00 98.24 ? 663 CYS B SG 1 ATOM 12272 N N . VAL B 2 664 ? -14.939 11.387 77.610 1.00 81.70 ? 664 VAL B N 1 ATOM 12273 C CA . VAL B 2 664 ? -14.697 12.697 77.015 1.00 93.88 ? 664 VAL B CA 1 ATOM 12274 C C . VAL B 2 664 ? -13.389 12.724 76.236 1.00 80.60 ? 664 VAL B C 1 ATOM 12275 O O . VAL B 2 664 ? -12.306 12.664 76.815 1.00 81.75 ? 664 VAL B O 1 ATOM 12276 C CB . VAL B 2 664 ? -14.664 13.806 78.085 1.00 81.06 ? 664 VAL B CB 1 ATOM 12277 C CG1 . VAL B 2 664 ? -14.343 15.149 77.445 1.00 80.36 ? 664 VAL B CG1 1 ATOM 12278 C CG2 . VAL B 2 664 ? -15.989 13.867 78.828 1.00 81.35 ? 664 VAL B CG2 1 ATOM 12279 N N . VAL B 2 665 ? -13.504 12.837 74.917 1.00 79.58 ? 665 VAL B N 1 ATOM 12280 C CA . VAL B 2 665 ? -12.343 12.862 74.038 1.00 81.81 ? 665 VAL B CA 1 ATOM 12281 C C . VAL B 2 665 ? -11.885 14.290 73.775 1.00 81.01 ? 665 VAL B C 1 ATOM 12282 O O . VAL B 2 665 ? -12.642 15.105 73.252 1.00 79.90 ? 665 VAL B O 1 ATOM 12283 C CB . VAL B 2 665 ? -12.641 12.177 72.692 1.00 79.22 ? 665 VAL B CB 1 ATOM 12284 C CG1 . VAL B 2 665 ? -11.441 12.283 71.763 1.00 79.76 ? 665 VAL B CG1 1 ATOM 12285 C CG2 . VAL B 2 665 ? -13.034 10.725 72.910 1.00 106.81 ? 665 VAL B CG2 1 ATOM 12286 N N . ARG B 2 666 ? -10.644 14.588 74.140 1.00 88.77 ? 666 ARG B N 1 ATOM 12287 C CA . ARG B 2 666 ? -10.084 15.914 73.916 1.00 89.73 ? 666 ARG B CA 1 ATOM 12288 C C . ARG B 2 666 ? -9.065 15.874 72.786 1.00 85.36 ? 666 ARG B C 1 ATOM 12289 O O . ARG B 2 666 ? -8.200 14.999 72.754 1.00 91.39 ? 666 ARG B O 1 ATOM 12290 C CB . ARG B 2 666 ? -9.435 16.451 75.193 1.00 102.21 ? 666 ARG B CB 1 ATOM 12291 C CG . ARG B 2 666 ? -10.162 16.061 76.471 1.00 108.62 ? 666 ARG B CG 1 ATOM 12292 C CD . ARG B 2 666 ? -9.631 16.833 77.667 1.00 110.06 ? 666 ARG B CD 1 ATOM 12293 N NE . ARG B 2 666 ? -10.089 18.219 77.661 1.00 116.07 ? 666 ARG B NE 1 ATOM 12294 C CZ . ARG B 2 666 ? -11.156 18.655 78.322 1.00 115.45 ? 666 ARG B CZ 1 ATOM 12295 N NH1 . ARG B 2 666 ? -11.877 17.812 79.049 1.00 109.50 ? 666 ARG B NH1 1 ATOM 12296 N NH2 . ARG B 2 666 ? -11.503 19.933 78.258 1.00 111.15 ? 666 ARG B NH2 1 ATOM 12297 N N . PHE B 2 667 ? -9.172 16.816 71.855 1.00 81.38 ? 667 PHE B N 1 ATOM 12298 C CA . PHE B 2 667 ? -8.224 16.892 70.752 1.00 82.64 ? 667 PHE B CA 1 ATOM 12299 C C . PHE B 2 667 ? -8.064 18.323 70.255 1.00 82.41 ? 667 PHE B C 1 ATOM 12300 O O . PHE B 2 667 ? -8.589 19.260 70.857 1.00 112.09 ? 667 PHE B O 1 ATOM 12301 C CB . PHE B 2 667 ? -8.655 15.972 69.603 1.00 84.43 ? 667 PHE B CB 1 ATOM 12302 C CG . PHE B 2 667 ? -9.929 16.390 68.920 1.00 80.03 ? 667 PHE B CG 1 ATOM 12303 C CD1 . PHE B 2 667 ? -9.894 17.156 67.766 1.00 80.32 ? 667 PHE B CD1 1 ATOM 12304 C CD2 . PHE B 2 667 ? -11.161 15.998 69.418 1.00 87.99 ? 667 PHE B CD2 1 ATOM 12305 C CE1 . PHE B 2 667 ? -11.059 17.535 67.130 1.00 79.53 ? 667 PHE B CE1 1 ATOM 12306 C CE2 . PHE B 2 667 ? -12.332 16.375 68.785 1.00 86.35 ? 667 PHE B CE2 1 ATOM 12307 C CZ . PHE B 2 667 ? -12.280 17.143 67.639 1.00 78.41 ? 667 PHE B CZ 1 ATOM 12308 N N . GLN B 2 668 ? -7.354 18.474 69.141 1.00 83.31 ? 668 GLN B N 1 ATOM 12309 C CA . GLN B 2 668 ? -7.054 19.779 68.563 1.00 98.23 ? 668 GLN B CA 1 ATOM 12310 C C . GLN B 2 668 ? -6.321 19.610 67.242 1.00 97.03 ? 668 GLN B C 1 ATOM 12311 O O . GLN B 2 668 ? -5.763 18.550 66.964 1.00 105.13 ? 668 GLN B O 1 ATOM 12312 C CB . GLN B 2 668 ? -6.200 20.619 69.517 1.00 110.23 ? 668 GLN B CB 1 ATOM 12313 C CG . GLN B 2 668 ? -4.858 19.984 69.854 1.00 108.45 ? 668 GLN B CG 1 ATOM 12314 C CD . GLN B 2 668 ? -3.959 20.901 70.660 1.00 109.41 ? 668 GLN B CD 1 ATOM 12315 O OE1 . GLN B 2 668 ? -4.180 22.111 70.720 1.00 113.41 ? 668 GLN B OE1 1 ATOM 12316 N NE2 . GLN B 2 668 ? -2.937 20.327 71.285 1.00 104.15 ? 668 GLN B NE2 1 ATOM 12317 N N . TYR B 2 669 ? -6.308 20.666 66.436 1.00 100.23 ? 669 TYR B N 1 ATOM 12318 C CA . TYR B 2 669 ? -5.654 20.616 65.137 1.00 110.04 ? 669 TYR B CA 1 ATOM 12319 C C . TYR B 2 669 ? -4.943 21.922 64.817 1.00 127.42 ? 669 TYR B C 1 ATOM 12320 O O . TYR B 2 669 ? -5.450 23.007 65.102 1.00 126.88 ? 669 TYR B O 1 ATOM 12321 C CB . TYR B 2 669 ? -6.666 20.285 64.035 1.00 104.11 ? 669 TYR B CB 1 ATOM 12322 C CG . TYR B 2 669 ? -7.826 21.252 63.932 1.00 101.23 ? 669 TYR B CG 1 ATOM 12323 C CD1 . TYR B 2 669 ? -7.752 22.374 63.117 1.00 123.62 ? 669 TYR B CD1 1 ATOM 12324 C CD2 . TYR B 2 669 ? -9.000 21.035 64.642 1.00 96.04 ? 669 TYR B CD2 1 ATOM 12325 C CE1 . TYR B 2 669 ? -8.809 23.257 63.018 1.00 131.31 ? 669 TYR B CE1 1 ATOM 12326 C CE2 . TYR B 2 669 ? -10.064 21.912 64.548 1.00 97.54 ? 669 TYR B CE2 1 ATOM 12327 C CZ . TYR B 2 669 ? -9.963 23.021 63.735 1.00 117.67 ? 669 TYR B CZ 1 ATOM 12328 O OH . TYR B 2 669 ? -11.017 23.899 63.636 1.00 118.02 ? 669 TYR B OH 1 ATOM 12329 N N . TYR B 2 670 ? -3.758 21.808 64.230 1.00 137.63 ? 670 TYR B N 1 ATOM 12330 C CA . TYR B 2 670 ? -3.024 22.973 63.766 1.00 141.90 ? 670 TYR B CA 1 ATOM 12331 C C . TYR B 2 670 ? -3.577 23.452 62.433 1.00 144.86 ? 670 TYR B C 1 ATOM 12332 O O . TYR B 2 670 ? -4.033 22.652 61.616 1.00 141.32 ? 670 TYR B O 1 ATOM 12333 C CB . TYR B 2 670 ? -1.533 22.657 63.628 1.00 144.90 ? 670 TYR B CB 1 ATOM 12334 C CG . TYR B 2 670 ? -0.754 22.771 64.917 1.00 149.06 ? 670 TYR B CG 1 ATOM 12335 C CD1 . TYR B 2 670 ? -1.218 23.557 65.963 1.00 154.70 ? 670 TYR B CD1 1 ATOM 12336 C CD2 . TYR B 2 670 ? 0.449 22.099 65.084 1.00 153.28 ? 670 TYR B CD2 1 ATOM 12337 C CE1 . TYR B 2 670 ? -0.507 23.667 67.143 1.00 160.01 ? 670 TYR B CE1 1 ATOM 12338 C CE2 . TYR B 2 670 ? 1.168 22.203 66.260 1.00 159.30 ? 670 TYR B CE2 1 ATOM 12339 C CZ . TYR B 2 670 ? 0.685 22.988 67.285 1.00 159.26 ? 670 TYR B CZ 1 ATOM 12340 O OH . TYR B 2 670 ? 1.397 23.095 68.458 1.00 153.91 ? 670 TYR B OH 1 ATOM 12341 N N . GLU B 2 671 ? -3.533 24.761 62.214 1.00 156.29 ? 671 GLU B N 1 ATOM 12342 C CA . GLU B 2 671 ? -3.892 25.316 60.919 1.00 161.99 ? 671 GLU B CA 1 ATOM 12343 C C . GLU B 2 671 ? -2.682 25.157 60.002 1.00 163.05 ? 671 GLU B C 1 ATOM 12344 O O . GLU B 2 671 ? -1.716 24.483 60.361 1.00 162.14 ? 671 GLU B O 1 ATOM 12345 C CB . GLU B 2 671 ? -4.324 26.780 61.044 1.00 165.94 ? 671 GLU B CB 1 ATOM 12346 C CG . GLU B 2 671 ? -5.220 27.273 59.910 1.00 166.18 ? 671 GLU B CG 1 ATOM 12347 C CD . GLU B 2 671 ? -6.311 26.281 59.551 1.00 162.34 ? 671 GLU B CD 1 ATOM 12348 O OE1 . GLU B 2 671 ? -7.102 25.912 60.444 1.00 158.68 ? 671 GLU B OE1 1 ATOM 12349 O OE2 . GLU B 2 671 ? -6.373 25.866 58.374 1.00 161.34 ? 671 GLU B OE2 1 ATOM 12350 N N . ASP B 2 672 ? -2.731 25.761 58.822 0.50 168.69 ? 672 ASP B N 1 ATOM 12351 C CA . ASP B 2 672 ? -1.695 25.533 57.827 0.50 176.89 ? 672 ASP B CA 1 ATOM 12352 C C . ASP B 2 672 ? -0.309 26.013 58.261 0.50 191.75 ? 672 ASP B C 1 ATOM 12353 O O . ASP B 2 672 ? -0.111 27.188 58.571 0.50 195.98 ? 672 ASP B O 1 ATOM 12354 C CB . ASP B 2 672 ? -2.088 26.216 56.513 1.00 175.54 ? 672 ASP B CB 1 ATOM 12355 C CG . ASP B 2 672 ? -2.400 27.689 56.690 1.00 177.89 ? 672 ASP B CG 1 ATOM 12356 O OD1 . ASP B 2 672 ? -2.841 28.076 57.792 1.00 180.20 ? 672 ASP B OD1 1 ATOM 12357 O OD2 . ASP B 2 672 ? -2.204 28.459 55.726 1.00 176.48 ? 672 ASP B OD2 1 ATOM 12358 N N . SER B 2 673 ? 0.641 25.084 58.288 1.00 204.52 ? 673 SER B N 1 ATOM 12359 C CA . SER B 2 673 ? 2.059 25.416 58.245 1.00 224.09 ? 673 SER B CA 1 ATOM 12360 C C . SER B 2 673 ? 2.584 24.805 56.957 1.00 240.11 ? 673 SER B C 1 ATOM 12361 O O . SER B 2 673 ? 2.744 23.586 56.876 1.00 244.29 ? 673 SER B O 1 ATOM 12362 C CB . SER B 2 673 ? 2.799 24.871 59.467 1.00 230.52 ? 673 SER B CB 1 ATOM 12363 O OG . SER B 2 673 ? 4.203 24.973 59.304 1.00 237.24 ? 673 SER B OG 1 ATOM 12364 N N . SER B 2 674 ? 2.829 25.650 55.953 1.00 250.80 ? 674 SER B N 1 ATOM 12365 C CA . SER B 2 674 ? 3.028 25.218 54.559 1.00 252.48 ? 674 SER B CA 1 ATOM 12366 C C . SER B 2 674 ? 1.746 24.557 54.024 1.00 243.05 ? 674 SER B C 1 ATOM 12367 O O . SER B 2 674 ? 1.647 24.208 52.849 1.00 244.90 ? 674 SER B O 1 ATOM 12368 C CB . SER B 2 674 ? 4.228 24.272 54.420 1.00 256.97 ? 674 SER B CB 1 ATOM 12369 O OG . SER B 2 674 ? 3.975 23.019 55.031 1.00 256.64 ? 674 SER B OG 1 ATOM 12370 N N . GLY B 2 675 ? 0.776 24.405 54.921 1.00 232.70 ? 675 GLY B N 1 ATOM 12371 C CA . GLY B 2 675 ? -0.497 23.749 54.696 1.00 224.40 ? 675 GLY B CA 1 ATOM 12372 C C . GLY B 2 675 ? -0.456 22.294 55.116 1.00 219.44 ? 675 GLY B C 1 ATOM 12373 O O . GLY B 2 675 ? 0.522 21.595 54.844 1.00 229.96 ? 675 GLY B O 1 ATOM 12374 N N . LYS B 2 676 ? -1.545 21.849 55.746 1.00 205.06 ? 676 LYS B N 1 ATOM 12375 C CA . LYS B 2 676 ? -1.790 20.453 56.128 1.00 192.84 ? 676 LYS B CA 1 ATOM 12376 C C . LYS B 2 676 ? -3.048 20.354 56.990 1.00 184.14 ? 676 LYS B C 1 ATOM 12377 O O . LYS B 2 676 ? -3.535 21.353 57.520 1.00 185.15 ? 676 LYS B O 1 ATOM 12378 C CB . LYS B 2 676 ? -0.601 19.834 56.876 1.00 188.53 ? 676 LYS B CB 1 ATOM 12379 C CG . LYS B 2 676 ? -0.051 20.651 58.029 1.00 188.46 ? 676 LYS B CG 1 ATOM 12380 C CD . LYS B 2 676 ? 1.202 19.990 58.588 1.00 186.89 ? 676 LYS B CD 1 ATOM 12381 C CE . LYS B 2 676 ? 2.207 19.698 57.483 1.00 184.08 ? 676 LYS B CE 1 ATOM 12382 N NZ . LYS B 2 676 ? 3.387 18.936 57.976 1.00 184.39 ? 676 LYS B NZ 1 ATOM 12383 N N . SER B 2 677 ? -3.562 19.137 57.124 1.00 177.41 ? 677 SER B N 1 ATOM 12384 C CA . SER B 2 677 ? -4.758 18.858 57.915 1.00 171.94 ? 677 SER B CA 1 ATOM 12385 C C . SER B 2 677 ? -4.454 18.374 59.336 1.00 168.04 ? 677 SER B C 1 ATOM 12386 O O . SER B 2 677 ? -5.365 17.949 60.048 1.00 179.41 ? 677 SER B O 1 ATOM 12387 C CB . SER B 2 677 ? -5.634 17.832 57.197 1.00 173.15 ? 677 SER B CB 1 ATOM 12388 O OG . SER B 2 677 ? -6.192 18.378 56.015 1.00 170.94 ? 677 SER B OG 1 ATOM 12389 N N . ILE B 2 678 ? -3.183 18.437 59.735 1.00 157.17 ? 678 ILE B N 1 ATOM 12390 C CA . ILE B 2 678 ? -2.670 17.721 60.910 1.00 146.28 ? 678 ILE B CA 1 ATOM 12391 C C . ILE B 2 678 ? -3.528 17.872 62.172 1.00 131.59 ? 678 ILE B C 1 ATOM 12392 O O . ILE B 2 678 ? -3.953 18.970 62.534 1.00 130.47 ? 678 ILE B O 1 ATOM 12393 C CB . ILE B 2 678 ? -1.223 18.178 61.237 1.00 155.25 ? 678 ILE B CB 1 ATOM 12394 C CG1 . ILE B 2 678 ? -0.703 17.497 62.506 1.00 153.07 ? 678 ILE B CG1 1 ATOM 12395 C CG2 . ILE B 2 678 ? -1.151 19.692 61.376 1.00 160.43 ? 678 ILE B CG2 1 ATOM 12396 C CD1 . ILE B 2 678 ? -0.560 15.994 62.387 1.00 152.64 ? 678 ILE B CD1 1 ATOM 12397 N N . LEU B 2 679 ? -3.784 16.739 62.820 1.00 120.13 ? 679 LEU B N 1 ATOM 12398 C CA . LEU B 2 679 ? -4.718 16.654 63.936 1.00 107.13 ? 679 LEU B CA 1 ATOM 12399 C C . LEU B 2 679 ? -4.144 15.831 65.089 1.00 101.76 ? 679 LEU B C 1 ATOM 12400 O O . LEU B 2 679 ? -3.641 14.727 64.881 1.00 104.41 ? 679 LEU B O 1 ATOM 12401 C CB . LEU B 2 679 ? -6.036 16.042 63.456 1.00 100.12 ? 679 LEU B CB 1 ATOM 12402 C CG . LEU B 2 679 ? -7.127 15.720 64.474 1.00 93.57 ? 679 LEU B CG 1 ATOM 12403 C CD1 . LEU B 2 679 ? -7.757 16.989 65.005 1.00 107.34 ? 679 LEU B CD1 1 ATOM 12404 C CD2 . LEU B 2 679 ? -8.176 14.831 63.837 1.00 90.38 ? 679 LEU B CD2 1 ATOM 12405 N N . TYR B 2 680 ? -4.226 16.369 66.303 1.00 96.49 ? 680 TYR B N 1 ATOM 12406 C CA . TYR B 2 680 ? -3.702 15.685 67.483 1.00 94.66 ? 680 TYR B CA 1 ATOM 12407 C C . TYR B 2 680 ? -4.813 15.263 68.440 1.00 89.40 ? 680 TYR B C 1 ATOM 12408 O O . TYR B 2 680 ? -5.540 16.105 68.965 1.00 100.39 ? 680 TYR B O 1 ATOM 12409 C CB . TYR B 2 680 ? -2.703 16.577 68.223 1.00 101.57 ? 680 TYR B CB 1 ATOM 12410 C CG . TYR B 2 680 ? -1.474 16.938 67.421 1.00 111.17 ? 680 TYR B CG 1 ATOM 12411 C CD1 . TYR B 2 680 ? -0.398 16.065 67.332 1.00 118.68 ? 680 TYR B CD1 1 ATOM 12412 C CD2 . TYR B 2 680 ? -1.385 18.157 66.761 1.00 113.65 ? 680 TYR B CD2 1 ATOM 12413 C CE1 . TYR B 2 680 ? 0.729 16.392 66.603 1.00 130.30 ? 680 TYR B CE1 1 ATOM 12414 C CE2 . TYR B 2 680 ? -0.262 18.494 66.030 1.00 121.56 ? 680 TYR B CE2 1 ATOM 12415 C CZ . TYR B 2 680 ? 0.792 17.607 65.954 1.00 135.04 ? 680 TYR B CZ 1 ATOM 12416 O OH . TYR B 2 680 ? 1.914 17.937 65.228 1.00 151.35 ? 680 TYR B OH 1 ATOM 12417 N N . VAL B 2 681 ? -4.934 13.959 68.671 1.00 96.83 ? 681 VAL B N 1 ATOM 12418 C CA . VAL B 2 681 ? -5.925 13.431 69.604 1.00 85.43 ? 681 VAL B CA 1 ATOM 12419 C C . VAL B 2 681 ? -5.261 12.893 70.866 1.00 90.86 ? 681 VAL B C 1 ATOM 12420 O O . VAL B 2 681 ? -4.388 12.028 70.796 1.00 114.21 ? 681 VAL B O 1 ATOM 12421 C CB . VAL B 2 681 ? -6.766 12.311 68.962 1.00 84.65 ? 681 VAL B CB 1 ATOM 12422 C CG1 . VAL B 2 681 ? -7.638 11.631 70.009 1.00 83.95 ? 681 VAL B CG1 1 ATOM 12423 C CG2 . VAL B 2 681 ? -7.615 12.868 67.832 1.00 97.57 ? 681 VAL B CG2 1 ATOM 12424 N N . VAL B 2 682 ? -5.677 13.410 72.018 1.00 86.25 ? 682 VAL B N 1 ATOM 12425 C CA . VAL B 2 682 ? -5.128 12.968 73.294 1.00 87.77 ? 682 VAL B CA 1 ATOM 12426 C C . VAL B 2 682 ? -5.522 11.528 73.591 1.00 95.15 ? 682 VAL B C 1 ATOM 12427 O O . VAL B 2 682 ? -6.703 11.183 73.573 1.00 94.45 ? 682 VAL B O 1 ATOM 12428 C CB . VAL B 2 682 ? -5.602 13.865 74.454 1.00 91.33 ? 682 VAL B CB 1 ATOM 12429 C CG1 . VAL B 2 682 ? -5.000 13.397 75.771 1.00 88.85 ? 682 VAL B CG1 1 ATOM 12430 C CG2 . VAL B 2 682 ? -5.238 15.311 74.184 1.00 98.24 ? 682 VAL B CG2 1 ATOM 12431 N N . GLU B 2 683 ? -4.527 10.689 73.861 1.00 102.06 ? 683 GLU B N 1 ATOM 12432 C CA . GLU B 2 683 ? -4.787 9.312 74.254 1.00 94.48 ? 683 GLU B CA 1 ATOM 12433 C C . GLU B 2 683 ? -5.356 9.281 75.663 1.00 102.56 ? 683 GLU B C 1 ATOM 12434 O O . GLU B 2 683 ? -5.195 10.237 76.421 1.00 122.81 ? 683 GLU B O 1 ATOM 12435 C CB . GLU B 2 683 ? -3.515 8.470 74.188 1.00 98.46 ? 683 GLU B CB 1 ATOM 12436 C CG . GLU B 2 683 ? -2.477 8.838 75.235 1.00 109.72 ? 683 GLU B CG 1 ATOM 12437 C CD . GLU B 2 683 ? -1.655 7.646 75.682 1.00 129.48 ? 683 GLU B CD 1 ATOM 12438 O OE1 . GLU B 2 683 ? -0.425 7.791 75.836 1.00 118.54 ? 683 GLU B OE1 1 ATOM 12439 O OE2 . GLU B 2 683 ? -2.241 6.561 75.881 1.00 154.95 ? 683 GLU B OE2 1 ATOM 12440 N N . GLU B 2 684 ? -6.020 8.180 76.003 1.00 101.06 ? 684 GLU B N 1 ATOM 12441 C CA . GLU B 2 684 ? -6.586 7.989 77.336 1.00 109.22 ? 684 GLU B CA 1 ATOM 12442 C C . GLU B 2 684 ? -7.535 9.124 77.734 1.00 108.06 ? 684 GLU B C 1 ATOM 12443 O O . GLU B 2 684 ? -7.200 9.949 78.585 1.00 90.85 ? 684 GLU B O 1 ATOM 12444 C CB . GLU B 2 684 ? -5.465 7.853 78.373 1.00 107.47 ? 684 GLU B CB 1 ATOM 12445 C CG . GLU B 2 684 ? -5.922 7.360 79.736 1.00 112.02 ? 684 GLU B CG 1 ATOM 12446 C CD . GLU B 2 684 ? -6.435 5.936 79.697 1.00 124.00 ? 684 GLU B CD 1 ATOM 12447 O OE1 . GLU B 2 684 ? -5.623 5.010 79.900 1.00 126.14 ? 684 GLU B OE1 1 ATOM 12448 O OE2 . GLU B 2 684 ? -7.647 5.744 79.464 1.00 128.89 ? 684 GLU B OE2 1 ATOM 12449 N N . PRO B 2 685 ? -8.717 9.182 77.101 1.00 88.45 ? 685 PRO B N 1 ATOM 12450 C CA . PRO B 2 685 ? -9.722 10.184 77.474 1.00 86.50 ? 685 PRO B CA 1 ATOM 12451 C C . PRO B 2 685 ? -10.254 9.983 78.894 1.00 88.36 ? 685 PRO B C 1 ATOM 12452 O O . PRO B 2 685 ? -9.872 9.026 79.567 1.00 90.80 ? 685 PRO B O 1 ATOM 12453 C CB . PRO B 2 685 ? -10.831 9.967 76.439 1.00 84.70 ? 685 PRO B CB 1 ATOM 12454 C CG . PRO B 2 685 ? -10.638 8.576 75.951 1.00 85.99 ? 685 PRO B CG 1 ATOM 12455 C CD . PRO B 2 685 ? -9.161 8.357 75.966 1.00 87.96 ? 685 PRO B CD 1 ATOM 12456 N N . GLU B 2 686 ? -11.136 10.874 79.336 1.00 88.53 ? 686 GLU B N 1 ATOM 12457 C CA . GLU B 2 686 ? -11.684 10.798 80.687 1.00 93.63 ? 686 GLU B CA 1 ATOM 12458 C C . GLU B 2 686 ? -12.941 9.936 80.735 1.00 90.27 ? 686 GLU B C 1 ATOM 12459 O O . GLU B 2 686 ? -13.886 10.159 79.981 1.00 89.11 ? 686 GLU B O 1 ATOM 12460 C CB . GLU B 2 686 ? -11.996 12.197 81.227 1.00 109.08 ? 686 GLU B CB 1 ATOM 12461 C CG . GLU B 2 686 ? -10.777 13.084 81.446 1.00 124.68 ? 686 GLU B CG 1 ATOM 12462 C CD . GLU B 2 686 ? -10.456 13.952 80.245 1.00 138.02 ? 686 GLU B CD 1 ATOM 12463 O OE1 . GLU B 2 686 ? -9.838 15.021 80.433 1.00 131.17 ? 686 GLU B OE1 1 ATOM 12464 O OE2 . GLU B 2 686 ? -10.820 13.569 79.113 1.00 152.61 ? 686 GLU B OE2 1 ATOM 12465 N N . CYS B 2 687 ? -12.944 8.957 81.633 1.00 90.57 ? 687 CYS B N 1 ATOM 12466 C CA . CYS B 2 687 ? -14.078 8.055 81.796 1.00 90.57 ? 687 CYS B CA 1 ATOM 12467 C C . CYS B 2 687 ? -14.417 7.896 83.278 1.00 93.77 ? 687 CYS B C 1 ATOM 12468 O O . CYS B 2 687 ? -13.587 8.198 84.135 1.00 96.45 ? 687 CYS B O 1 ATOM 12469 C CB . CYS B 2 687 ? -13.771 6.695 81.165 1.00 91.26 ? 687 CYS B CB 1 ATOM 12470 S SG . CYS B 2 687 ? -13.471 6.742 79.384 1.00 136.30 ? 687 CYS B SG 1 ATOM 12471 N N . PRO B 2 688 ? -15.639 7.427 83.588 1.00 94.98 ? 688 PRO B N 1 ATOM 12472 C CA . PRO B 2 688 ? -16.002 7.206 84.994 1.00 108.61 ? 688 PRO B CA 1 ATOM 12473 C C . PRO B 2 688 ? -15.152 6.129 85.671 1.00 108.59 ? 688 PRO B C 1 ATOM 12474 O O . PRO B 2 688 ? -14.301 5.512 85.029 1.00 110.35 ? 688 PRO B O 1 ATOM 12475 C CB . PRO B 2 688 ? -17.472 6.769 84.915 1.00 114.25 ? 688 PRO B CB 1 ATOM 12476 C CG . PRO B 2 688 ? -17.678 6.333 83.498 1.00 103.91 ? 688 PRO B CG 1 ATOM 12477 C CD . PRO B 2 688 ? -16.785 7.213 82.688 1.00 92.67 ? 688 PRO B CD 1 ATOM 12478 N N . LYS B 2 689 ? -15.394 5.903 86.958 1.00 108.75 ? 689 LYS B N 1 ATOM 12479 C CA . LYS B 2 689 ? -14.558 5.001 87.743 1.00 122.66 ? 689 LYS B CA 1 ATOM 12480 C C . LYS B 2 689 ? -15.328 3.779 88.234 1.00 128.19 ? 689 LYS B C 1 ATOM 12481 O O . LYS B 2 689 ? -16.504 3.604 87.918 1.00 132.78 ? 689 LYS B O 1 ATOM 12482 C CB . LYS B 2 689 ? -13.952 5.747 88.933 1.00 123.14 ? 689 LYS B CB 1 ATOM 12483 C CG . LYS B 2 689 ? -13.274 7.055 88.561 1.00 115.26 ? 689 LYS B CG 1 ATOM 12484 C CD . LYS B 2 689 ? -12.198 6.842 87.508 1.00 118.66 ? 689 LYS B CD 1 ATOM 12485 C CE . LYS B 2 689 ? -11.534 8.155 87.126 1.00 123.37 ? 689 LYS B CE 1 ATOM 12486 N NZ . LYS B 2 689 ? -10.882 8.806 88.295 1.00 128.92 ? 689 LYS B NZ 1 ATOM 12487 N N . GLY B 2 690 ? -14.653 2.934 89.007 1.00 121.06 ? 690 GLY B N 1 ATOM 12488 C CA . GLY B 2 690 ? -15.266 1.736 89.548 1.00 125.92 ? 690 GLY B CA 1 ATOM 12489 C C . GLY B 2 690 ? -14.311 0.941 90.418 1.00 129.71 ? 690 GLY B C 1 ATOM 12490 O O . GLY B 2 690 ? -14.703 0.394 91.448 1.00 128.81 ? 690 GLY B O 1 ATOM 12491 N N . SER C 3 1 ? 32.370 47.072 52.148 1.00 208.80 ? 1417 SER C N 1 ATOM 12492 C CA . SER C 3 1 ? 31.586 47.806 51.163 1.00 205.74 ? 1417 SER C CA 1 ATOM 12493 C C . SER C 3 1 ? 30.223 48.200 51.731 1.00 206.84 ? 1417 SER C C 1 ATOM 12494 O O . SER C 3 1 ? 30.039 49.321 52.206 1.00 206.39 ? 1417 SER C O 1 ATOM 12495 C CB . SER C 3 1 ? 31.409 46.972 49.891 1.00 197.43 ? 1417 SER C CB 1 ATOM 12496 O OG . SER C 3 1 ? 32.663 46.619 49.331 1.00 194.85 ? 1417 SER C OG 1 ATOM 12497 N N . ASP C 3 2 ? 29.277 47.265 51.682 1.00 206.85 ? 1418 ASP C N 1 ATOM 12498 C CA . ASP C 3 2 ? 27.922 47.484 52.184 1.00 204.08 ? 1418 ASP C CA 1 ATOM 12499 C C . ASP C 3 2 ? 27.511 46.389 53.165 1.00 199.22 ? 1418 ASP C C 1 ATOM 12500 O O . ASP C 3 2 ? 27.527 45.204 52.823 1.00 199.39 ? 1418 ASP C O 1 ATOM 12501 C CB . ASP C 3 2 ? 26.928 47.548 51.024 1.00 201.62 ? 1418 ASP C CB 1 ATOM 12502 C CG . ASP C 3 2 ? 27.092 46.396 50.053 1.00 197.60 ? 1418 ASP C CG 1 ATOM 12503 O OD1 . ASP C 3 2 ? 27.908 46.518 49.116 1.00 201.40 ? 1418 ASP C OD1 1 ATOM 12504 O OD2 . ASP C 3 2 ? 26.408 45.366 50.229 1.00 188.61 ? 1418 ASP C OD2 1 ATOM 12505 N N . VAL C 3 3 ? 27.102 46.799 54.381 1.00 194.80 ? 1419 VAL C N 1 ATOM 12506 C CA . VAL C 3 3 ? 26.582 45.891 55.438 1.00 195.06 ? 1419 VAL C CA 1 ATOM 12507 C C . VAL C 3 3 ? 26.288 46.546 56.823 1.00 197.47 ? 1419 VAL C C 1 ATOM 12508 O O . VAL C 3 3 ? 26.750 47.654 57.092 1.00 199.16 ? 1419 VAL C O 1 ATOM 12509 C CB . VAL C 3 3 ? 27.518 44.685 55.649 1.00 187.42 ? 1419 VAL C CB 1 ATOM 12510 C CG1 . VAL C 3 3 ? 28.300 44.841 56.945 1.00 191.34 ? 1419 VAL C CG1 1 ATOM 12511 C CG2 . VAL C 3 3 ? 26.722 43.389 55.652 1.00 180.63 ? 1419 VAL C CG2 1 ATOM 12512 N N . PRO C 3 4 ? 25.526 45.853 57.689 1.00 195.17 ? 1420 PRO C N 1 ATOM 12513 C CA . PRO C 3 4 ? 25.216 46.308 59.054 1.00 193.37 ? 1420 PRO C CA 1 ATOM 12514 C C . PRO C 3 4 ? 26.446 46.277 59.969 1.00 197.29 ? 1420 PRO C C 1 ATOM 12515 O O . PRO C 3 4 ? 27.513 46.703 59.533 1.00 198.79 ? 1420 PRO C O 1 ATOM 12516 C CB . PRO C 3 4 ? 24.140 45.331 59.523 1.00 191.94 ? 1420 PRO C CB 1 ATOM 12517 C CG . PRO C 3 4 ? 24.370 44.126 58.704 1.00 193.41 ? 1420 PRO C CG 1 ATOM 12518 C CD . PRO C 3 4 ? 24.704 44.675 57.360 1.00 190.69 ? 1420 PRO C CD 1 ATOM 12519 N N . ARG C 3 5 ? 26.182 45.814 61.191 1.00 198.27 ? 1421 ARG C N 1 ATOM 12520 C CA . ARG C 3 5 ? 27.095 45.742 62.347 1.00 199.02 ? 1421 ARG C CA 1 ATOM 12521 C C . ARG C 3 5 ? 27.243 47.103 63.074 1.00 198.89 ? 1421 ARG C C 1 ATOM 12522 O O . ARG C 3 5 ? 26.273 47.846 63.093 1.00 195.98 ? 1421 ARG C O 1 ATOM 12523 C CB . ARG C 3 5 ? 28.457 45.121 61.830 1.00 217.27 ? 1421 ARG C CB 1 ATOM 12524 C CG . ARG C 3 5 ? 29.847 45.457 62.445 1.00 216.79 ? 1421 ARG C CG 1 ATOM 12525 C CD . ARG C 3 5 ? 31.056 45.313 61.469 1.00 219.91 ? 1421 ARG C CD 1 ATOM 12526 N NE . ARG C 3 5 ? 32.154 46.256 61.754 1.00 219.96 ? 1421 ARG C NE 1 ATOM 12527 C CZ . ARG C 3 5 ? 33.157 46.556 60.923 1.00 217.45 ? 1421 ARG C CZ 1 ATOM 12528 N NH1 . ARG C 3 5 ? 33.249 45.982 59.729 1.00 214.75 ? 1421 ARG C NH1 1 ATOM 12529 N NH2 . ARG C 3 5 ? 34.072 47.443 61.294 1.00 216.93 ? 1421 ARG C NH2 1 ATOM 12530 N N . ASP C 3 6 ? 28.402 47.424 63.646 1.00 209.89 ? 1422 ASP C N 1 ATOM 12531 C CA . ASP C 3 6 ? 28.567 48.380 64.755 1.00 220.39 ? 1422 ASP C CA 1 ATOM 12532 C C . ASP C 3 6 ? 27.388 48.295 65.728 1.00 219.92 ? 1422 ASP C C 1 ATOM 12533 O O . ASP C 3 6 ? 26.668 49.274 65.968 1.00 225.64 ? 1422 ASP C O 1 ATOM 12534 C CB . ASP C 3 6 ? 28.789 49.800 64.255 1.00 225.11 ? 1422 ASP C CB 1 ATOM 12535 C CG . ASP C 3 6 ? 30.233 50.035 63.851 1.00 227.64 ? 1422 ASP C CG 1 ATOM 12536 O OD1 . ASP C 3 6 ? 30.586 49.667 62.717 1.00 232.12 ? 1422 ASP C OD1 1 ATOM 12537 O OD2 . ASP C 3 6 ? 31.025 50.556 64.667 1.00 226.30 ? 1422 ASP C OD2 1 ATOM 12538 N N . LEU C 3 7 ? 27.256 47.112 66.321 1.00 210.89 ? 1423 LEU C N 1 ATOM 12539 C CA . LEU C 3 7 ? 26.062 46.715 67.044 1.00 202.31 ? 1423 LEU C CA 1 ATOM 12540 C C . LEU C 3 7 ? 26.203 46.953 68.539 1.00 204.82 ? 1423 LEU C C 1 ATOM 12541 O O . LEU C 3 7 ? 27.016 46.321 69.217 1.00 205.13 ? 1423 LEU C O 1 ATOM 12542 C CB . LEU C 3 7 ? 25.746 45.244 66.758 1.00 194.02 ? 1423 LEU C CB 1 ATOM 12543 C CG . LEU C 3 7 ? 26.816 44.364 66.099 1.00 196.79 ? 1423 LEU C CG 1 ATOM 12544 C CD1 . LEU C 3 7 ? 27.928 44.006 67.075 1.00 197.91 ? 1423 LEU C CD1 1 ATOM 12545 C CD2 . LEU C 3 7 ? 26.183 43.107 65.519 1.00 200.68 ? 1423 LEU C CD2 1 ATOM 12546 N N . GLU C 3 8 ? 25.403 47.886 69.038 1.00 204.29 ? 1424 GLU C N 1 ATOM 12547 C CA . GLU C 3 8 ? 25.449 48.265 70.436 1.00 205.87 ? 1424 GLU C CA 1 ATOM 12548 C C . GLU C 3 8 ? 24.247 47.722 71.192 1.00 205.24 ? 1424 GLU C C 1 ATOM 12549 O O . GLU C 3 8 ? 23.369 47.076 70.618 1.00 200.01 ? 1424 GLU C O 1 ATOM 12550 C CB . GLU C 3 8 ? 25.502 49.787 70.565 1.00 204.85 ? 1424 GLU C CB 1 ATOM 12551 C CG . GLU C 3 8 ? 26.515 50.453 69.649 1.00 203.87 ? 1424 GLU C CG 1 ATOM 12552 C CD . GLU C 3 8 ? 26.359 51.959 69.614 1.00 200.16 ? 1424 GLU C CD 1 ATOM 12553 O OE1 . GLU C 3 8 ? 25.522 52.486 70.376 1.00 194.88 ? 1424 GLU C OE1 1 ATOM 12554 O OE2 . GLU C 3 8 ? 27.069 52.616 68.824 1.00 200.92 ? 1424 GLU C OE2 1 ATOM 12555 N N . VAL C 3 9 ? 24.228 47.995 72.490 1.00 208.04 ? 1425 VAL C N 1 ATOM 12556 C CA . VAL C 3 9 ? 23.068 47.754 73.333 1.00 201.29 ? 1425 VAL C CA 1 ATOM 12557 C C . VAL C 3 9 ? 22.869 48.994 74.194 1.00 193.02 ? 1425 VAL C C 1 ATOM 12558 O O . VAL C 3 9 ? 23.742 49.349 74.986 1.00 190.63 ? 1425 VAL C O 1 ATOM 12559 C CB . VAL C 3 9 ? 23.243 46.508 74.220 1.00 197.95 ? 1425 VAL C CB 1 ATOM 12560 C CG1 . VAL C 3 9 ? 22.160 46.457 75.282 1.00 197.00 ? 1425 VAL C CG1 1 ATOM 12561 C CG2 . VAL C 3 9 ? 23.235 45.241 73.373 1.00 189.60 ? 1425 VAL C CG2 1 ATOM 12562 N N . VAL C 3 10 ? 21.726 49.655 74.042 1.00 320.24 ? 1426 VAL C N 1 ATOM 12563 C CA . VAL C 3 10 ? 21.537 50.966 74.656 1.00 328.13 ? 1426 VAL C CA 1 ATOM 12564 C C . VAL C 3 10 ? 20.651 50.932 75.899 1.00 333.61 ? 1426 VAL C C 1 ATOM 12565 O O . VAL C 3 10 ? 21.145 51.041 77.021 1.00 339.49 ? 1426 VAL C O 1 ATOM 12566 C CB . VAL C 3 10 ? 20.936 51.964 73.649 1.00 328.04 ? 1426 VAL C CB 1 ATOM 12567 C CG1 . VAL C 3 10 ? 20.863 53.355 74.261 1.00 334.03 ? 1426 VAL C CG1 1 ATOM 12568 C CG2 . VAL C 3 10 ? 21.759 51.985 72.371 1.00 322.35 ? 1426 VAL C CG2 1 ATOM 12569 N N . ALA C 3 11 ? 19.345 50.781 75.702 1.00 331.14 ? 1427 ALA C N 1 ATOM 12570 C CA . ALA C 3 11 ? 18.408 50.816 76.820 1.00 336.27 ? 1427 ALA C CA 1 ATOM 12571 C C . ALA C 3 11 ? 18.223 49.434 77.429 1.00 336.15 ? 1427 ALA C C 1 ATOM 12572 O O . ALA C 3 11 ? 18.043 48.447 76.715 1.00 331.28 ? 1427 ALA C O 1 ATOM 12573 C CB . ALA C 3 11 ? 17.069 51.384 76.377 1.00 338.98 ? 1427 ALA C CB 1 ATOM 12574 N N . ALA C 3 12 ? 18.267 49.372 78.755 1.00 344.97 ? 1428 ALA C N 1 ATOM 12575 C CA . ALA C 3 12 ? 18.130 48.108 79.465 1.00 341.44 ? 1428 ALA C CA 1 ATOM 12576 C C . ALA C 3 12 ? 17.115 48.211 80.598 1.00 344.23 ? 1428 ALA C C 1 ATOM 12577 O O . ALA C 3 12 ? 17.229 49.064 81.478 1.00 346.57 ? 1428 ALA C O 1 ATOM 12578 C CB . ALA C 3 12 ? 19.479 47.655 80.002 1.00 337.33 ? 1428 ALA C CB 1 ATOM 12579 N N . THR C 3 13 ? 16.122 47.330 80.563 1.00 343.93 ? 1429 THR C N 1 ATOM 12580 C CA . THR C 3 13 ? 15.112 47.248 81.607 1.00 347.82 ? 1429 THR C CA 1 ATOM 12581 C C . THR C 3 13 ? 15.183 45.846 82.213 1.00 346.11 ? 1429 THR C C 1 ATOM 12582 O O . THR C 3 13 ? 15.996 45.034 81.768 1.00 342.65 ? 1429 THR C O 1 ATOM 12583 C CB . THR C 3 13 ? 13.700 47.541 81.044 1.00 345.85 ? 1429 THR C CB 1 ATOM 12584 O OG1 . THR C 3 13 ? 13.379 46.586 80.025 1.00 338.73 ? 1429 THR C OG1 1 ATOM 12585 C CG2 . THR C 3 13 ? 13.638 48.943 80.458 1.00 347.38 ? 1429 THR C CG2 1 ATOM 12586 N N . PRO C 3 14 ? 14.360 45.555 83.239 1.00 346.70 ? 1430 PRO C N 1 ATOM 12587 C CA . PRO C 3 14 ? 14.283 44.160 83.690 1.00 343.46 ? 1430 PRO C CA 1 ATOM 12588 C C . PRO C 3 14 ? 13.939 43.174 82.570 1.00 336.86 ? 1430 PRO C C 1 ATOM 12589 O O . PRO C 3 14 ? 14.256 41.990 82.683 1.00 336.40 ? 1430 PRO C O 1 ATOM 12590 C CB . PRO C 3 14 ? 13.173 44.202 84.738 1.00 345.65 ? 1430 PRO C CB 1 ATOM 12591 C CG . PRO C 3 14 ? 13.313 45.552 85.340 1.00 349.09 ? 1430 PRO C CG 1 ATOM 12592 C CD . PRO C 3 14 ? 13.745 46.471 84.220 1.00 348.64 ? 1430 PRO C CD 1 ATOM 12593 N N . THR C 3 15 ? 13.304 43.660 81.506 1.00 332.24 ? 1431 THR C N 1 ATOM 12594 C CA . THR C 3 15 ? 12.982 42.825 80.354 1.00 331.97 ? 1431 THR C CA 1 ATOM 12595 C C . THR C 3 15 ? 13.227 43.556 79.034 1.00 325.61 ? 1431 THR C C 1 ATOM 12596 O O . THR C 3 15 ? 13.768 44.662 79.015 1.00 328.59 ? 1431 THR C O 1 ATOM 12597 C CB . THR C 3 15 ? 11.518 42.344 80.393 1.00 316.79 ? 1431 THR C CB 1 ATOM 12598 O OG1 . THR C 3 15 ? 10.655 43.451 80.681 1.00 321.27 ? 1431 THR C OG1 1 ATOM 12599 C CG2 . THR C 3 15 ? 11.335 41.275 81.460 1.00 317.40 ? 1431 THR C CG2 1 ATOM 12600 N N . SER C 3 16 ? 12.825 42.914 77.940 1.00 320.90 ? 1432 SER C N 1 ATOM 12601 C CA . SER C 3 16 ? 13.009 43.422 76.580 1.00 318.45 ? 1432 SER C CA 1 ATOM 12602 C C . SER C 3 16 ? 14.466 43.756 76.262 1.00 319.73 ? 1432 SER C C 1 ATOM 12603 O O . SER C 3 16 ? 15.376 43.071 76.732 1.00 319.27 ? 1432 SER C O 1 ATOM 12604 C CB . SER C 3 16 ? 12.134 44.659 76.355 1.00 318.45 ? 1432 SER C CB 1 ATOM 12605 O OG . SER C 3 16 ? 12.355 45.216 75.071 1.00 313.00 ? 1432 SER C OG 1 ATOM 12606 N N . LEU C 3 17 ? 14.668 44.834 75.502 1.00 321.44 ? 1433 LEU C N 1 ATOM 12607 C CA . LEU C 3 17 ? 15.990 45.262 75.034 1.00 320.34 ? 1433 LEU C CA 1 ATOM 12608 C C . LEU C 3 17 ? 15.892 46.466 74.097 1.00 323.68 ? 1433 LEU C C 1 ATOM 12609 O O . LEU C 3 17 ? 14.804 46.842 73.663 1.00 320.08 ? 1433 LEU C O 1 ATOM 12610 C CB . LEU C 3 17 ? 16.716 44.126 74.305 1.00 310.47 ? 1433 LEU C CB 1 ATOM 12611 C CG . LEU C 3 17 ? 17.988 43.586 74.964 1.00 307.66 ? 1433 LEU C CG 1 ATOM 12612 C CD1 . LEU C 3 17 ? 18.656 42.547 74.076 1.00 300.66 ? 1433 LEU C CD1 1 ATOM 12613 C CD2 . LEU C 3 17 ? 18.949 44.718 75.289 1.00 311.40 ? 1433 LEU C CD2 1 ATOM 12614 N N . LEU C 3 18 ? 17.041 47.064 73.793 1.00 219.81 ? 1434 LEU C N 1 ATOM 12615 C CA . LEU C 3 18 ? 17.138 48.072 72.742 1.00 214.34 ? 1434 LEU C CA 1 ATOM 12616 C C . LEU C 3 18 ? 18.433 47.870 71.961 1.00 210.46 ? 1434 LEU C C 1 ATOM 12617 O O . LEU C 3 18 ? 19.510 47.775 72.550 1.00 217.51 ? 1434 LEU C O 1 ATOM 12618 C CB . LEU C 3 18 ? 17.084 49.486 73.322 1.00 215.74 ? 1434 LEU C CB 1 ATOM 12619 C CG . LEU C 3 18 ? 16.807 50.604 72.312 1.00 202.44 ? 1434 LEU C CG 1 ATOM 12620 C CD1 . LEU C 3 18 ? 15.323 50.674 71.984 1.00 194.11 ? 1434 LEU C CD1 1 ATOM 12621 C CD2 . LEU C 3 18 ? 17.314 51.949 72.810 1.00 207.88 ? 1434 LEU C CD2 1 ATOM 12622 N N . ILE C 3 19 ? 18.330 47.804 70.637 1.00 199.21 ? 1435 ILE C N 1 ATOM 12623 C CA . ILE C 3 19 ? 19.502 47.562 69.803 1.00 197.33 ? 1435 ILE C CA 1 ATOM 12624 C C . ILE C 3 19 ? 19.742 48.706 68.817 1.00 193.11 ? 1435 ILE C C 1 ATOM 12625 O O . ILE C 3 19 ? 18.811 49.211 68.190 1.00 189.39 ? 1435 ILE C O 1 ATOM 12626 C CB . ILE C 3 19 ? 19.372 46.224 69.031 1.00 200.36 ? 1435 ILE C CB 1 ATOM 12627 C CG1 . ILE C 3 19 ? 20.588 45.996 68.128 1.00 203.66 ? 1435 ILE C CG1 1 ATOM 12628 C CG2 . ILE C 3 19 ? 18.077 46.177 68.230 1.00 198.73 ? 1435 ILE C CG2 1 ATOM 12629 C CD1 . ILE C 3 19 ? 20.546 44.691 67.363 1.00 201.24 ? 1435 ILE C CD1 1 ATOM 12630 N N . SER C 3 20 ? 21.000 49.122 68.703 1.00 192.45 ? 1436 SER C N 1 ATOM 12631 C CA . SER C 3 20 ? 21.380 50.175 67.770 1.00 191.91 ? 1436 SER C CA 1 ATOM 12632 C C . SER C 3 20 ? 22.583 49.747 66.938 1.00 194.21 ? 1436 SER C C 1 ATOM 12633 O O . SER C 3 20 ? 23.473 49.054 67.429 1.00 201.83 ? 1436 SER C O 1 ATOM 12634 C CB . SER C 3 20 ? 21.689 51.472 68.519 1.00 195.27 ? 1436 SER C CB 1 ATOM 12635 O OG . SER C 3 20 ? 20.556 51.926 69.237 1.00 197.60 ? 1436 SER C OG 1 ATOM 12636 N N . TRP C 3 21 ? 22.606 50.163 65.677 1.00 185.91 ? 1437 TRP C N 1 ATOM 12637 C CA . TRP C 3 21 ? 23.696 49.804 64.780 1.00 182.27 ? 1437 TRP C CA 1 ATOM 12638 C C . TRP C 3 21 ? 24.038 50.947 63.831 1.00 181.13 ? 1437 TRP C C 1 ATOM 12639 O O . TRP C 3 21 ? 23.414 52.007 63.871 1.00 183.53 ? 1437 TRP C O 1 ATOM 12640 C CB . TRP C 3 21 ? 23.336 48.547 63.986 1.00 177.38 ? 1437 TRP C CB 1 ATOM 12641 C CG . TRP C 3 21 ? 22.090 48.686 63.160 1.00 171.42 ? 1437 TRP C CG 1 ATOM 12642 C CD1 . TRP C 3 21 ? 22.012 49.060 61.849 1.00 167.19 ? 1437 TRP C CD1 1 ATOM 12643 C CD2 . TRP C 3 21 ? 20.743 48.453 63.591 1.00 168.98 ? 1437 TRP C CD2 1 ATOM 12644 N NE1 . TRP C 3 21 ? 20.701 49.074 61.438 1.00 162.94 ? 1437 TRP C NE1 1 ATOM 12645 C CE2 . TRP C 3 21 ? 19.902 48.705 62.488 1.00 157.71 ? 1437 TRP C CE2 1 ATOM 12646 C CE3 . TRP C 3 21 ? 20.166 48.055 64.801 1.00 166.24 ? 1437 TRP C CE3 1 ATOM 12647 C CZ2 . TRP C 3 21 ? 18.516 48.574 62.560 1.00 150.24 ? 1437 TRP C CZ2 1 ATOM 12648 C CZ3 . TRP C 3 21 ? 18.789 47.925 64.870 1.00 159.90 ? 1437 TRP C CZ3 1 ATOM 12649 C CH2 . TRP C 3 21 ? 17.980 48.184 63.756 1.00 150.56 ? 1437 TRP C CH2 1 ATOM 12650 N N . ASP C 3 22 ? 25.032 50.725 62.977 1.00 179.64 ? 1438 ASP C N 1 ATOM 12651 C CA . ASP C 3 22 ? 25.427 51.727 61.994 1.00 175.64 ? 1438 ASP C CA 1 ATOM 12652 C C . ASP C 3 22 ? 24.894 51.371 60.614 1.00 167.60 ? 1438 ASP C C 1 ATOM 12653 O O . ASP C 3 22 ? 24.792 50.197 60.258 1.00 166.60 ? 1438 ASP C O 1 ATOM 12654 C CB . ASP C 3 22 ? 26.948 51.878 61.947 1.00 181.11 ? 1438 ASP C CB 1 ATOM 12655 C CG . ASP C 3 22 ? 27.501 52.583 63.170 1.00 185.44 ? 1438 ASP C CG 1 ATOM 12656 O OD1 . ASP C 3 22 ? 26.903 52.447 64.258 1.00 181.23 ? 1438 ASP C OD1 1 ATOM 12657 O OD2 . ASP C 3 22 ? 28.542 53.263 63.046 1.00 193.79 ? 1438 ASP C OD2 1 ATOM 12658 N N . ALA C 3 23 ? 24.551 52.398 59.846 1.00 165.43 ? 1439 ALA C N 1 ATOM 12659 C CA . ALA C 3 23 ? 23.981 52.216 58.518 1.00 165.35 ? 1439 ALA C CA 1 ATOM 12660 C C . ALA C 3 23 ? 24.954 51.528 57.562 1.00 164.28 ? 1439 ALA C C 1 ATOM 12661 O O . ALA C 3 23 ? 26.165 51.734 57.645 1.00 169.83 ? 1439 ALA C O 1 ATOM 12662 C CB . ALA C 3 23 ? 23.545 53.558 57.951 1.00 165.86 ? 1439 ALA C CB 1 ATOM 12663 N N . PRO C 3 24 ? 24.416 50.703 56.650 1.00 164.01 ? 1440 PRO C N 1 ATOM 12664 C CA . PRO C 3 24 ? 25.149 50.003 55.587 1.00 166.43 ? 1440 PRO C CA 1 ATOM 12665 C C . PRO C 3 24 ? 25.875 50.939 54.620 1.00 162.33 ? 1440 PRO C C 1 ATOM 12666 O O . PRO C 3 24 ? 26.659 50.449 53.804 1.00 166.68 ? 1440 PRO C O 1 ATOM 12667 C CB . PRO C 3 24 ? 24.048 49.224 54.864 1.00 171.02 ? 1440 PRO C CB 1 ATOM 12668 C CG . PRO C 3 24 ? 23.024 48.990 55.912 1.00 171.07 ? 1440 PRO C CG 1 ATOM 12669 C CD . PRO C 3 24 ? 23.015 50.253 56.722 1.00 168.25 ? 1440 PRO C CD 1 ATOM 12670 N N . ALA C 3 25 ? 25.558 52.234 54.688 1.00 154.98 ? 1441 ALA C N 1 ATOM 12671 C CA . ALA C 3 25 ? 26.174 53.301 53.887 1.00 154.15 ? 1441 ALA C CA 1 ATOM 12672 C C . ALA C 3 25 ? 25.584 53.364 52.481 1.00 156.31 ? 1441 ALA C C 1 ATOM 12673 O O . ALA C 3 25 ? 25.931 54.240 51.690 1.00 156.46 ? 1441 ALA C O 1 ATOM 12674 C CB . ALA C 3 25 ? 27.697 53.150 53.826 1.00 149.65 ? 1441 ALA C CB 1 ATOM 12675 N N . VAL C 3 26 ? 24.688 52.430 52.178 1.00 154.76 ? 1442 VAL C N 1 ATOM 12676 C CA . VAL C 3 26 ? 23.951 52.446 50.921 1.00 151.34 ? 1442 VAL C CA 1 ATOM 12677 C C . VAL C 3 26 ? 22.464 52.533 51.248 1.00 142.26 ? 1442 VAL C C 1 ATOM 12678 O O . VAL C 3 26 ? 22.063 52.247 52.376 1.00 149.33 ? 1442 VAL C O 1 ATOM 12679 C CB . VAL C 3 26 ? 24.243 51.195 50.065 1.00 159.47 ? 1442 VAL C CB 1 ATOM 12680 C CG1 . VAL C 3 26 ? 23.886 51.445 48.606 1.00 151.15 ? 1442 VAL C CG1 1 ATOM 12681 C CG2 . VAL C 3 26 ? 25.705 50.807 50.182 1.00 166.79 ? 1442 VAL C CG2 1 ATOM 12682 N N . THR C 3 27 ? 21.655 52.949 50.277 1.00 140.11 ? 1443 THR C N 1 ATOM 12683 C CA . THR C 3 27 ? 20.215 53.086 50.476 1.00 144.88 ? 1443 THR C CA 1 ATOM 12684 C C . THR C 3 27 ? 19.585 51.782 50.957 1.00 147.96 ? 1443 THR C C 1 ATOM 12685 O O . THR C 3 27 ? 19.780 50.727 50.355 1.00 153.43 ? 1443 THR C O 1 ATOM 12686 C CB . THR C 3 27 ? 19.509 53.535 49.183 1.00 145.17 ? 1443 THR C CB 1 ATOM 12687 O OG1 . THR C 3 27 ? 19.740 52.568 48.150 1.00 150.45 ? 1443 THR C OG1 1 ATOM 12688 C CG2 . THR C 3 27 ? 20.036 54.889 48.731 1.00 144.88 ? 1443 THR C CG2 1 ATOM 12689 N N . VAL C 3 28 ? 18.836 51.866 52.052 1.00 144.30 ? 1444 VAL C N 1 ATOM 12690 C CA . VAL C 3 28 ? 18.222 50.691 52.659 1.00 145.07 ? 1444 VAL C CA 1 ATOM 12691 C C . VAL C 3 28 ? 16.703 50.811 52.692 1.00 132.73 ? 1444 VAL C C 1 ATOM 12692 O O . VAL C 3 28 ? 16.163 51.826 53.131 1.00 127.41 ? 1444 VAL C O 1 ATOM 12693 C CB . VAL C 3 28 ? 18.736 50.469 54.095 1.00 149.67 ? 1444 VAL C CB 1 ATOM 12694 C CG1 . VAL C 3 28 ? 18.073 49.254 54.718 1.00 148.27 ? 1444 VAL C CG1 1 ATOM 12695 C CG2 . VAL C 3 28 ? 20.243 50.311 54.098 1.00 152.12 ? 1444 VAL C CG2 1 ATOM 12696 N N . ARG C 3 29 ? 16.017 49.773 52.225 1.00 126.70 ? 1445 ARG C N 1 ATOM 12697 C CA . ARG C 3 29 ? 14.561 49.751 52.262 1.00 119.71 ? 1445 ARG C CA 1 ATOM 12698 C C . ARG C 3 29 ? 14.057 49.613 53.694 1.00 133.82 ? 1445 ARG C C 1 ATOM 12699 O O . ARG C 3 29 ? 13.246 50.416 54.156 1.00 145.05 ? 1445 ARG C O 1 ATOM 12700 C CB . ARG C 3 29 ? 14.015 48.611 51.401 1.00 112.66 ? 1445 ARG C CB 1 ATOM 12701 C CG . ARG C 3 29 ? 14.376 48.719 49.933 1.00 107.94 ? 1445 ARG C CG 1 ATOM 12702 C CD . ARG C 3 29 ? 13.423 47.908 49.074 1.00 100.52 ? 1445 ARG C CD 1 ATOM 12703 N NE . ARG C 3 29 ? 13.545 46.471 49.300 1.00 93.36 ? 1445 ARG C NE 1 ATOM 12704 C CZ . ARG C 3 29 ? 14.373 45.678 48.627 1.00 97.08 ? 1445 ARG C CZ 1 ATOM 12705 N NH1 . ARG C 3 29 ? 15.160 46.183 47.687 1.00 95.28 ? 1445 ARG C NH1 1 ATOM 12706 N NH2 . ARG C 3 29 ? 14.416 44.381 48.896 1.00 110.70 ? 1445 ARG C NH2 1 ATOM 12707 N N . TYR C 3 30 ? 14.553 48.594 54.390 1.00 138.39 ? 1446 TYR C N 1 ATOM 12708 C CA . TYR C 3 30 ? 14.169 48.337 55.774 1.00 138.75 ? 1446 TYR C CA 1 ATOM 12709 C C . TYR C 3 30 ? 15.141 47.355 56.425 1.00 141.73 ? 1446 TYR C C 1 ATOM 12710 O O . TYR C 3 30 ? 16.136 46.964 55.818 1.00 146.69 ? 1446 TYR C O 1 ATOM 12711 C CB . TYR C 3 30 ? 12.732 47.805 55.848 1.00 136.49 ? 1446 TYR C CB 1 ATOM 12712 C CG . TYR C 3 30 ? 12.491 46.506 55.108 1.00 133.51 ? 1446 TYR C CG 1 ATOM 12713 C CD1 . TYR C 3 30 ? 12.315 46.490 53.729 1.00 119.77 ? 1446 TYR C CD1 1 ATOM 12714 C CD2 . TYR C 3 30 ? 12.418 45.299 55.791 1.00 148.04 ? 1446 TYR C CD2 1 ATOM 12715 C CE1 . TYR C 3 30 ? 12.089 45.306 53.051 1.00 120.63 ? 1446 TYR C CE1 1 ATOM 12716 C CE2 . TYR C 3 30 ? 12.190 44.111 55.121 1.00 149.45 ? 1446 TYR C CE2 1 ATOM 12717 C CZ . TYR C 3 30 ? 12.027 44.120 53.751 1.00 130.90 ? 1446 TYR C CZ 1 ATOM 12718 O OH . TYR C 3 30 ? 11.802 42.940 53.081 1.00 126.62 ? 1446 TYR C OH 1 ATOM 12719 N N . TYR C 3 31 ? 14.859 46.974 57.667 1.00 140.67 ? 1447 TYR C N 1 ATOM 12720 C CA . TYR C 3 31 ? 15.683 46.002 58.376 1.00 143.78 ? 1447 TYR C CA 1 ATOM 12721 C C . TYR C 3 31 ? 14.824 44.842 58.881 1.00 142.38 ? 1447 TYR C C 1 ATOM 12722 O O . TYR C 3 31 ? 13.605 44.962 58.975 1.00 137.75 ? 1447 TYR C O 1 ATOM 12723 C CB . TYR C 3 31 ? 16.425 46.664 59.544 1.00 144.99 ? 1447 TYR C CB 1 ATOM 12724 C CG . TYR C 3 31 ? 17.402 47.746 59.136 1.00 146.01 ? 1447 TYR C CG 1 ATOM 12725 C CD1 . TYR C 3 31 ? 18.650 47.424 58.618 1.00 148.55 ? 1447 TYR C CD1 1 ATOM 12726 C CD2 . TYR C 3 31 ? 17.082 49.090 59.284 1.00 148.13 ? 1447 TYR C CD2 1 ATOM 12727 C CE1 . TYR C 3 31 ? 19.548 48.410 58.249 1.00 151.00 ? 1447 TYR C CE1 1 ATOM 12728 C CE2 . TYR C 3 31 ? 17.974 50.083 58.918 1.00 151.22 ? 1447 TYR C CE2 1 ATOM 12729 C CZ . TYR C 3 31 ? 19.205 49.736 58.402 1.00 150.84 ? 1447 TYR C CZ 1 ATOM 12730 O OH . TYR C 3 31 ? 20.095 50.720 58.036 1.00 151.03 ? 1447 TYR C OH 1 ATOM 12731 N N . ARG C 3 32 ? 15.467 43.719 59.189 1.00 144.54 ? 1448 ARG C N 1 ATOM 12732 C CA . ARG C 3 32 ? 14.776 42.552 59.731 1.00 148.29 ? 1448 ARG C CA 1 ATOM 12733 C C . ARG C 3 32 ? 15.495 41.995 60.962 1.00 164.12 ? 1448 ARG C C 1 ATOM 12734 O O . ARG C 3 32 ? 16.604 41.484 60.860 1.00 168.47 ? 1448 ARG C O 1 ATOM 12735 C CB . ARG C 3 32 ? 14.657 41.456 58.668 1.00 143.12 ? 1448 ARG C CB 1 ATOM 12736 C CG . ARG C 3 32 ? 13.664 41.729 57.550 1.00 137.45 ? 1448 ARG C CG 1 ATOM 12737 C CD . ARG C 3 32 ? 13.775 40.674 56.454 1.00 141.61 ? 1448 ARG C CD 1 ATOM 12738 N NE . ARG C 3 32 ? 13.783 39.311 56.987 1.00 151.87 ? 1448 ARG C NE 1 ATOM 12739 C CZ . ARG C 3 32 ? 14.800 38.462 56.862 1.00 155.31 ? 1448 ARG C CZ 1 ATOM 12740 N NH1 . ARG C 3 32 ? 15.898 38.827 56.216 1.00 153.30 ? 1448 ARG C NH1 1 ATOM 12741 N NH2 . ARG C 3 32 ? 14.720 37.242 57.378 1.00 159.03 ? 1448 ARG C NH2 1 ATOM 12742 N N . ILE C 3 33 ? 14.842 42.062 62.116 1.00 165.05 ? 1449 ILE C N 1 ATOM 12743 C CA . ILE C 3 33 ? 15.450 41.622 63.370 1.00 169.34 ? 1449 ILE C CA 1 ATOM 12744 C C . ILE C 3 33 ? 15.152 40.151 63.670 1.00 177.79 ? 1449 ILE C C 1 ATOM 12745 O O . ILE C 3 33 ? 13.994 39.750 63.789 1.00 177.36 ? 1449 ILE C O 1 ATOM 12746 C CB . ILE C 3 33 ? 14.962 42.472 64.563 1.00 170.51 ? 1449 ILE C CB 1 ATOM 12747 C CG1 . ILE C 3 33 ? 14.867 43.954 64.192 1.00 163.14 ? 1449 ILE C CG1 1 ATOM 12748 C CG2 . ILE C 3 33 ? 15.865 42.280 65.746 1.00 183.03 ? 1449 ILE C CG2 1 ATOM 12749 C CD1 . ILE C 3 33 ? 16.173 44.632 63.946 1.00 163.64 ? 1449 ILE C CD1 1 ATOM 12750 N N . THR C 3 34 ? 16.206 39.354 63.808 1.00 183.57 ? 1450 THR C N 1 ATOM 12751 C CA . THR C 3 34 ? 16.055 37.920 64.036 1.00 181.11 ? 1450 THR C CA 1 ATOM 12752 C C . THR C 3 34 ? 16.800 37.447 65.291 1.00 186.75 ? 1450 THR C C 1 ATOM 12753 O O . THR C 3 34 ? 17.976 37.739 65.472 1.00 187.46 ? 1450 THR C O 1 ATOM 12754 C CB . THR C 3 34 ? 16.546 37.123 62.812 1.00 171.71 ? 1450 THR C CB 1 ATOM 12755 O OG1 . THR C 3 34 ? 15.642 37.321 61.718 1.00 165.51 ? 1450 THR C OG1 1 ATOM 12756 C CG2 . THR C 3 34 ? 16.624 35.649 63.131 1.00 173.70 ? 1450 THR C CG2 1 ATOM 12757 N N . TYR C 3 35 ? 16.117 36.708 66.158 1.00 191.52 ? 1451 TYR C N 1 ATOM 12758 C CA . TYR C 3 35 ? 16.731 36.274 67.411 1.00 197.01 ? 1451 TYR C CA 1 ATOM 12759 C C . TYR C 3 35 ? 16.269 34.888 67.852 1.00 206.03 ? 1451 TYR C C 1 ATOM 12760 O O . TYR C 3 35 ? 15.216 34.411 67.432 1.00 208.81 ? 1451 TYR C O 1 ATOM 12761 C CB . TYR C 3 35 ? 16.435 37.290 68.514 1.00 192.50 ? 1451 TYR C CB 1 ATOM 12762 C CG . TYR C 3 35 ? 14.976 37.665 68.604 1.00 188.48 ? 1451 TYR C CG 1 ATOM 12763 C CD1 . TYR C 3 35 ? 14.483 38.781 67.940 1.00 180.30 ? 1451 TYR C CD1 1 ATOM 12764 C CD2 . TYR C 3 35 ? 14.088 36.895 69.342 1.00 191.35 ? 1451 TYR C CD2 1 ATOM 12765 C CE1 . TYR C 3 35 ? 13.148 39.122 68.014 1.00 178.97 ? 1451 TYR C CE1 1 ATOM 12766 C CE2 . TYR C 3 35 ? 12.752 37.228 69.422 1.00 191.21 ? 1451 TYR C CE2 1 ATOM 12767 C CZ . TYR C 3 35 ? 12.287 38.342 68.757 1.00 184.74 ? 1451 TYR C CZ 1 ATOM 12768 O OH . TYR C 3 35 ? 10.956 38.676 68.836 1.00 184.73 ? 1451 TYR C OH 1 ATOM 12769 N N . GLY C 3 36 ? 17.060 34.251 68.711 1.00 209.55 ? 1452 GLY C N 1 ATOM 12770 C CA . GLY C 3 36 ? 16.721 32.937 69.226 1.00 218.49 ? 1452 GLY C CA 1 ATOM 12771 C C . GLY C 3 36 ? 17.666 32.445 70.305 1.00 227.03 ? 1452 GLY C C 1 ATOM 12772 O O . GLY C 3 36 ? 18.660 33.098 70.622 1.00 225.18 ? 1452 GLY C O 1 ATOM 12773 N N . GLU C 3 37 ? 17.347 31.286 70.874 1.00 214.16 ? 1453 GLU C N 1 ATOM 12774 C CA . GLU C 3 37 ? 18.184 30.669 71.898 1.00 211.39 ? 1453 GLU C CA 1 ATOM 12775 C C . GLU C 3 37 ? 19.500 30.170 71.309 1.00 217.27 ? 1453 GLU C C 1 ATOM 12776 O O . GLU C 3 37 ? 19.613 29.974 70.100 1.00 221.97 ? 1453 GLU C O 1 ATOM 12777 C CB . GLU C 3 37 ? 17.443 29.514 72.577 1.00 205.25 ? 1453 GLU C CB 1 ATOM 12778 C CG . GLU C 3 37 ? 16.247 29.942 73.412 1.00 207.64 ? 1453 GLU C CG 1 ATOM 12779 C CD . GLU C 3 37 ? 15.608 28.783 74.153 1.00 201.02 ? 1453 GLU C CD 1 ATOM 12780 O OE1 . GLU C 3 37 ? 15.961 27.621 73.860 1.00 194.26 ? 1453 GLU C OE1 1 ATOM 12781 O OE2 . GLU C 3 37 ? 14.754 29.034 75.030 1.00 201.39 ? 1453 GLU C OE2 1 ATOM 12782 N N . THR C 3 38 ? 20.491 29.966 72.171 1.00 218.23 ? 1454 THR C N 1 ATOM 12783 C CA . THR C 3 38 ? 21.805 29.513 71.729 1.00 219.93 ? 1454 THR C CA 1 ATOM 12784 C C . THR C 3 38 ? 21.781 28.044 71.320 1.00 210.61 ? 1454 THR C C 1 ATOM 12785 O O . THR C 3 38 ? 20.752 27.375 71.423 1.00 199.93 ? 1454 THR C O 1 ATOM 12786 C CB . THR C 3 38 ? 22.865 29.705 72.829 1.00 217.42 ? 1454 THR C CB 1 ATOM 12787 O OG1 . THR C 3 38 ? 24.165 29.406 72.304 1.00 219.02 ? 1454 THR C OG1 1 ATOM 12788 C CG2 . THR C 3 38 ? 22.577 28.789 74.010 1.00 206.25 ? 1454 THR C CG2 1 ATOM 12789 N N . GLY C 3 39 ? 22.925 27.546 70.861 1.00 214.22 ? 1455 GLY C N 1 ATOM 12790 C CA . GLY C 3 39 ? 23.047 26.159 70.453 1.00 204.50 ? 1455 GLY C CA 1 ATOM 12791 C C . GLY C 3 39 ? 22.268 25.825 69.194 1.00 205.73 ? 1455 GLY C C 1 ATOM 12792 O O . GLY C 3 39 ? 22.166 26.638 68.275 1.00 216.40 ? 1455 GLY C O 1 ATOM 12793 N N . GLY C 3 40 ? 21.721 24.614 69.159 1.00 198.47 ? 1456 GLY C N 1 ATOM 12794 C CA . GLY C 3 40 ? 20.968 24.124 68.018 1.00 203.03 ? 1456 GLY C CA 1 ATOM 12795 C C . GLY C 3 40 ? 19.468 24.193 68.232 1.00 202.07 ? 1456 GLY C C 1 ATOM 12796 O O . GLY C 3 40 ? 18.709 23.440 67.622 1.00 197.36 ? 1456 GLY C O 1 ATOM 12797 N N . ASN C 3 41 ? 19.041 25.102 69.102 1.00 203.77 ? 1457 ASN C N 1 ATOM 12798 C CA . ASN C 3 41 ? 17.663 25.135 69.586 1.00 197.66 ? 1457 ASN C CA 1 ATOM 12799 C C . ASN C 3 41 ? 16.636 25.657 68.582 1.00 201.37 ? 1457 ASN C C 1 ATOM 12800 O O . ASN C 3 41 ? 16.932 25.844 67.402 1.00 209.99 ? 1457 ASN C O 1 ATOM 12801 C CB . ASN C 3 41 ? 17.583 25.970 70.864 1.00 195.73 ? 1457 ASN C CB 1 ATOM 12802 C CG . ASN C 3 41 ? 17.437 25.117 72.108 1.00 191.55 ? 1457 ASN C CG 1 ATOM 12803 O OD1 . ASN C 3 41 ? 16.324 24.831 72.551 1.00 188.43 ? 1457 ASN C OD1 1 ATOM 12804 N ND2 . ASN C 3 41 ? 18.562 24.701 72.677 1.00 192.97 ? 1457 ASN C ND2 1 ATOM 12805 N N . SER C 3 42 ? 15.424 25.880 69.086 1.00 197.85 ? 1458 SER C N 1 ATOM 12806 C CA . SER C 3 42 ? 14.234 26.165 68.282 1.00 200.46 ? 1458 SER C CA 1 ATOM 12807 C C . SER C 3 42 ? 14.397 27.314 67.282 1.00 209.66 ? 1458 SER C C 1 ATOM 12808 O O . SER C 3 42 ? 15.186 28.232 67.508 1.00 216.11 ? 1458 SER C O 1 ATOM 12809 C CB . SER C 3 42 ? 13.057 26.468 69.218 1.00 196.40 ? 1458 SER C CB 1 ATOM 12810 O OG . SER C 3 42 ? 12.788 25.368 70.070 1.00 192.24 ? 1458 SER C OG 1 ATOM 12811 N N . PRO C 3 43 ? 13.643 27.254 66.167 1.00 211.80 ? 1459 PRO C N 1 ATOM 12812 C CA . PRO C 3 43 ? 13.661 28.245 65.083 1.00 218.02 ? 1459 PRO C CA 1 ATOM 12813 C C . PRO C 3 43 ? 13.444 29.683 65.550 1.00 220.20 ? 1459 PRO C C 1 ATOM 12814 O O . PRO C 3 43 ? 12.835 29.927 66.592 1.00 214.20 ? 1459 PRO C O 1 ATOM 12815 C CB . PRO C 3 43 ? 12.508 27.792 64.186 1.00 216.29 ? 1459 PRO C CB 1 ATOM 12816 C CG . PRO C 3 43 ? 12.469 26.325 64.369 1.00 206.28 ? 1459 PRO C CG 1 ATOM 12817 C CD . PRO C 3 43 ? 12.807 26.089 65.816 1.00 204.37 ? 1459 PRO C CD 1 ATOM 12818 N N . VAL C 3 44 ? 13.954 30.624 64.761 1.00 227.42 ? 1460 VAL C N 1 ATOM 12819 C CA . VAL C 3 44 ? 14.036 32.026 65.152 1.00 234.91 ? 1460 VAL C CA 1 ATOM 12820 C C . VAL C 3 44 ? 12.892 32.899 64.624 1.00 242.46 ? 1460 VAL C C 1 ATOM 12821 O O . VAL C 3 44 ? 12.457 32.755 63.481 1.00 244.77 ? 1460 VAL C O 1 ATOM 12822 C CB . VAL C 3 44 ? 15.369 32.625 64.676 1.00 239.70 ? 1460 VAL C CB 1 ATOM 12823 C CG1 . VAL C 3 44 ? 16.511 32.137 65.554 1.00 229.56 ? 1460 VAL C CG1 1 ATOM 12824 C CG2 . VAL C 3 44 ? 15.620 32.250 63.222 1.00 243.02 ? 1460 VAL C CG2 1 ATOM 12825 N N . GLN C 3 45 ? 12.411 33.800 65.478 1.00 244.09 ? 1461 GLN C N 1 ATOM 12826 C CA . GLN C 3 45 ? 11.379 34.770 65.113 1.00 250.33 ? 1461 GLN C CA 1 ATOM 12827 C C . GLN C 3 45 ? 11.982 36.009 64.449 1.00 264.40 ? 1461 GLN C C 1 ATOM 12828 O O . GLN C 3 45 ? 13.108 36.397 64.761 1.00 263.54 ? 1461 GLN C O 1 ATOM 12829 C CB . GLN C 3 45 ? 10.575 35.181 66.349 1.00 242.86 ? 1461 GLN C CB 1 ATOM 12830 C CG . GLN C 3 45 ? 10.206 34.026 67.268 1.00 230.13 ? 1461 GLN C CG 1 ATOM 12831 C CD . GLN C 3 45 ? 9.285 33.017 66.608 1.00 223.32 ? 1461 GLN C CD 1 ATOM 12832 O OE1 . GLN C 3 45 ? 8.526 33.352 65.699 1.00 224.97 ? 1461 GLN C OE1 1 ATOM 12833 N NE2 . GLN C 3 45 ? 9.349 31.772 67.066 1.00 213.30 ? 1461 GLN C NE2 1 ATOM 12834 N N . GLU C 3 46 ? 11.237 36.628 63.536 1.00 189.19 ? 1462 GLU C N 1 ATOM 12835 C CA . GLU C 3 46 ? 11.722 37.828 62.857 1.00 185.20 ? 1462 GLU C CA 1 ATOM 12836 C C . GLU C 3 46 ? 10.641 38.891 62.641 1.00 189.11 ? 1462 GLU C C 1 ATOM 12837 O O . GLU C 3 46 ? 9.475 38.572 62.408 1.00 192.71 ? 1462 GLU C O 1 ATOM 12838 C CB . GLU C 3 46 ? 12.349 37.454 61.512 1.00 184.85 ? 1462 GLU C CB 1 ATOM 12839 C CG . GLU C 3 46 ? 11.429 36.680 60.584 1.00 194.11 ? 1462 GLU C CG 1 ATOM 12840 C CD . GLU C 3 46 ? 12.111 36.293 59.288 1.00 187.67 ? 1462 GLU C CD 1 ATOM 12841 O OE1 . GLU C 3 46 ? 13.231 36.786 59.038 1.00 179.02 ? 1462 GLU C OE1 1 ATOM 12842 O OE2 . GLU C 3 46 ? 11.532 35.495 58.521 1.00 186.95 ? 1462 GLU C OE2 1 ATOM 12843 N N . PHE C 3 47 ? 11.047 40.157 62.723 1.00 187.95 ? 1463 PHE C N 1 ATOM 12844 C CA . PHE C 3 47 ? 10.154 41.289 62.478 1.00 183.58 ? 1463 PHE C CA 1 ATOM 12845 C C . PHE C 3 47 ? 10.831 42.337 61.597 1.00 181.76 ? 1463 PHE C C 1 ATOM 12846 O O . PHE C 3 47 ? 11.949 42.128 61.128 1.00 179.81 ? 1463 PHE C O 1 ATOM 12847 C CB . PHE C 3 47 ? 9.702 41.920 63.795 1.00 182.21 ? 1463 PHE C CB 1 ATOM 12848 C CG . PHE C 3 47 ? 8.294 41.571 64.182 1.00 184.44 ? 1463 PHE C CG 1 ATOM 12849 C CD1 . PHE C 3 47 ? 7.407 41.073 63.242 1.00 180.79 ? 1463 PHE C CD1 1 ATOM 12850 C CD2 . PHE C 3 47 ? 7.854 41.744 65.484 1.00 186.09 ? 1463 PHE C CD2 1 ATOM 12851 C CE1 . PHE C 3 47 ? 6.110 40.751 63.592 1.00 185.60 ? 1463 PHE C CE1 1 ATOM 12852 C CE2 . PHE C 3 47 ? 6.558 41.424 65.841 1.00 185.48 ? 1463 PHE C CE2 1 ATOM 12853 C CZ . PHE C 3 47 ? 5.685 40.927 64.894 1.00 187.47 ? 1463 PHE C CZ 1 ATOM 12854 N N . THR C 3 48 ? 10.159 43.464 61.376 1.00 187.07 ? 1464 THR C N 1 ATOM 12855 C CA . THR C 3 48 ? 10.678 44.488 60.472 1.00 182.44 ? 1464 THR C CA 1 ATOM 12856 C C . THR C 3 48 ? 10.626 45.906 61.043 1.00 178.35 ? 1464 THR C C 1 ATOM 12857 O O . THR C 3 48 ? 9.722 46.256 61.802 1.00 180.91 ? 1464 THR C O 1 ATOM 12858 C CB . THR C 3 48 ? 9.917 44.479 59.130 1.00 177.59 ? 1464 THR C CB 1 ATOM 12859 O OG1 . THR C 3 48 ? 10.359 45.576 58.320 1.00 167.36 ? 1464 THR C OG1 1 ATOM 12860 C CG2 . THR C 3 48 ? 8.418 44.600 59.362 1.00 184.08 ? 1464 THR C CG2 1 ATOM 12861 N N . VAL C 3 49 ? 11.615 46.711 60.664 1.00 170.24 ? 1465 VAL C N 1 ATOM 12862 C CA . VAL C 3 49 ? 11.681 48.124 61.026 1.00 163.94 ? 1465 VAL C CA 1 ATOM 12863 C C . VAL C 3 49 ? 12.160 48.917 59.810 1.00 159.50 ? 1465 VAL C C 1 ATOM 12864 O O . VAL C 3 49 ? 12.868 48.372 58.964 1.00 160.70 ? 1465 VAL C O 1 ATOM 12865 C CB . VAL C 3 49 ? 12.627 48.369 62.226 1.00 163.23 ? 1465 VAL C CB 1 ATOM 12866 C CG1 . VAL C 3 49 ? 11.997 47.870 63.519 1.00 167.79 ? 1465 VAL C CG1 1 ATOM 12867 C CG2 . VAL C 3 49 ? 13.976 47.711 61.988 1.00 164.07 ? 1465 VAL C CG2 1 ATOM 12868 N N . PRO C 3 50 ? 11.778 50.204 59.711 1.00 156.63 ? 1466 PRO C N 1 ATOM 12869 C CA . PRO C 3 50 ? 12.138 50.989 58.520 1.00 149.30 ? 1466 PRO C CA 1 ATOM 12870 C C . PRO C 3 50 ? 13.645 51.192 58.348 1.00 155.66 ? 1466 PRO C C 1 ATOM 12871 O O . PRO C 3 50 ? 14.429 50.775 59.200 1.00 169.18 ? 1466 PRO C O 1 ATOM 12872 C CB . PRO C 3 50 ? 11.438 52.333 58.761 1.00 143.07 ? 1466 PRO C CB 1 ATOM 12873 C CG . PRO C 3 50 ? 11.221 52.395 60.235 1.00 152.61 ? 1466 PRO C CG 1 ATOM 12874 C CD . PRO C 3 50 ? 10.955 50.983 60.651 1.00 157.21 ? 1466 PRO C CD 1 ATOM 12875 N N . GLY C 3 51 ? 14.035 51.843 57.256 1.00 154.25 ? 1467 GLY C N 1 ATOM 12876 C CA . GLY C 3 51 ? 15.438 51.980 56.911 1.00 158.43 ? 1467 GLY C CA 1 ATOM 12877 C C . GLY C 3 51 ? 16.050 53.321 57.265 1.00 154.74 ? 1467 GLY C C 1 ATOM 12878 O O . GLY C 3 51 ? 17.269 53.485 57.217 1.00 157.54 ? 1467 GLY C O 1 ATOM 12879 N N . SER C 3 52 ? 15.207 54.285 57.619 1.00 152.96 ? 1468 SER C N 1 ATOM 12880 C CA . SER C 3 52 ? 15.685 55.614 57.978 1.00 147.01 ? 1468 SER C CA 1 ATOM 12881 C C . SER C 3 52 ? 15.963 55.717 59.474 1.00 140.72 ? 1468 SER C C 1 ATOM 12882 O O . SER C 3 52 ? 16.400 56.759 59.963 1.00 141.39 ? 1468 SER C O 1 ATOM 12883 C CB . SER C 3 52 ? 14.674 56.681 57.555 1.00 151.09 ? 1468 SER C CB 1 ATOM 12884 O OG . SER C 3 52 ? 14.521 56.706 56.146 1.00 152.43 ? 1468 SER C OG 1 ATOM 12885 N N . LYS C 3 53 ? 15.705 54.632 60.197 1.00 141.61 ? 1469 LYS C N 1 ATOM 12886 C CA . LYS C 3 53 ? 15.960 54.593 61.633 1.00 144.46 ? 1469 LYS C CA 1 ATOM 12887 C C . LYS C 3 53 ? 17.017 53.548 61.974 1.00 142.84 ? 1469 LYS C C 1 ATOM 12888 O O . LYS C 3 53 ? 16.979 52.423 61.474 1.00 130.10 ? 1469 LYS C O 1 ATOM 12889 C CB . LYS C 3 53 ? 14.668 54.315 62.405 1.00 141.31 ? 1469 LYS C CB 1 ATOM 12890 C CG . LYS C 3 53 ? 14.012 55.563 62.983 1.00 142.56 ? 1469 LYS C CG 1 ATOM 12891 C CD . LYS C 3 53 ? 13.692 56.582 61.900 1.00 136.90 ? 1469 LYS C CD 1 ATOM 12892 C CE . LYS C 3 53 ? 13.244 57.907 62.495 1.00 135.35 ? 1469 LYS C CE 1 ATOM 12893 N NZ . LYS C 3 53 ? 12.007 57.764 63.309 1.00 141.90 ? 1469 LYS C NZ 1 ATOM 12894 N N . SER C 3 54 ? 17.959 53.931 62.829 1.00 148.44 ? 1470 SER C N 1 ATOM 12895 C CA . SER C 3 54 ? 19.087 53.074 63.175 1.00 139.80 ? 1470 SER C CA 1 ATOM 12896 C C . SER C 3 54 ? 18.828 52.246 64.431 1.00 133.53 ? 1470 SER C C 1 ATOM 12897 O O . SER C 3 54 ? 19.706 51.516 64.890 1.00 133.45 ? 1470 SER C O 1 ATOM 12898 C CB . SER C 3 54 ? 20.350 53.918 63.361 1.00 138.62 ? 1470 SER C CB 1 ATOM 12899 O OG . SER C 3 54 ? 21.446 53.115 63.765 1.00 143.00 ? 1470 SER C OG 1 ATOM 12900 N N . THR C 3 55 ? 17.626 52.361 64.985 1.00 128.06 ? 1471 THR C N 1 ATOM 12901 C CA . THR C 3 55 ? 17.289 51.637 66.206 1.00 134.86 ? 1471 THR C CA 1 ATOM 12902 C C . THR C 3 55 ? 16.163 50.630 65.990 1.00 137.89 ? 1471 THR C C 1 ATOM 12903 O O . THR C 3 55 ? 15.597 50.537 64.901 1.00 134.10 ? 1471 THR C O 1 ATOM 12904 C CB . THR C 3 55 ? 16.878 52.605 67.331 1.00 135.16 ? 1471 THR C CB 1 ATOM 12905 O OG1 . THR C 3 55 ? 16.517 51.859 68.500 1.00 138.47 ? 1471 THR C OG1 1 ATOM 12906 C CG2 . THR C 3 55 ? 15.695 53.456 66.894 1.00 129.94 ? 1471 THR C CG2 1 ATOM 12907 N N . ALA C 3 56 ? 15.846 49.880 67.042 1.00 143.20 ? 1472 ALA C N 1 ATOM 12908 C CA . ALA C 3 56 ? 14.761 48.905 67.012 1.00 142.85 ? 1472 ALA C CA 1 ATOM 12909 C C . ALA C 3 56 ? 14.289 48.594 68.429 1.00 152.28 ? 1472 ALA C C 1 ATOM 12910 O O . ALA C 3 56 ? 15.017 48.822 69.393 1.00 156.07 ? 1472 ALA C O 1 ATOM 12911 C CB . ALA C 3 56 ? 15.204 47.633 66.306 1.00 144.55 ? 1472 ALA C CB 1 ATOM 12912 N N . THR C 3 57 ? 13.074 48.068 68.552 1.00 160.30 ? 1473 THR C N 1 ATOM 12913 C CA . THR C 3 57 ? 12.517 47.735 69.860 1.00 169.65 ? 1473 THR C CA 1 ATOM 12914 C C . THR C 3 57 ? 11.693 46.449 69.802 1.00 168.95 ? 1473 THR C C 1 ATOM 12915 O O . THR C 3 57 ? 10.906 46.249 68.876 1.00 164.04 ? 1473 THR C O 1 ATOM 12916 C CB . THR C 3 57 ? 11.638 48.880 70.403 1.00 169.59 ? 1473 THR C CB 1 ATOM 12917 O OG1 . THR C 3 57 ? 12.372 50.110 70.366 1.00 169.86 ? 1473 THR C OG1 1 ATOM 12918 C CG2 . THR C 3 57 ? 11.206 48.597 71.836 1.00 168.56 ? 1473 THR C CG2 1 ATOM 12919 N N . ILE C 3 58 ? 11.877 45.583 70.794 1.00 172.31 ? 1474 ILE C N 1 ATOM 12920 C CA . ILE C 3 58 ? 11.158 44.314 70.851 1.00 176.75 ? 1474 ILE C CA 1 ATOM 12921 C C . ILE C 3 58 ? 10.621 44.056 72.262 1.00 181.92 ? 1474 ILE C C 1 ATOM 12922 O O . ILE C 3 58 ? 11.256 44.416 73.253 1.00 188.64 ? 1474 ILE C O 1 ATOM 12923 C CB . ILE C 3 58 ? 12.062 43.139 70.397 1.00 172.02 ? 1474 ILE C CB 1 ATOM 12924 C CG1 . ILE C 3 58 ? 11.263 41.836 70.305 1.00 173.60 ? 1474 ILE C CG1 1 ATOM 12925 C CG2 . ILE C 3 58 ? 13.267 42.988 71.319 1.00 170.46 ? 1474 ILE C CG2 1 ATOM 12926 C CD1 . ILE C 3 58 ? 10.117 41.891 69.318 1.00 169.52 ? 1474 ILE C CD1 1 ATOM 12927 N N . SER C 3 59 ? 9.441 43.448 72.345 1.00 179.64 ? 1475 SER C N 1 ATOM 12928 C CA . SER C 3 59 ? 8.792 43.186 73.628 1.00 175.12 ? 1475 SER C CA 1 ATOM 12929 C C . SER C 3 59 ? 8.892 41.717 74.040 1.00 177.66 ? 1475 SER C C 1 ATOM 12930 O O . SER C 3 59 ? 9.532 40.914 73.362 1.00 181.22 ? 1475 SER C O 1 ATOM 12931 C CB . SER C 3 59 ? 7.323 43.609 73.572 1.00 164.83 ? 1475 SER C CB 1 ATOM 12932 O OG . SER C 3 59 ? 7.201 44.983 73.247 1.00 157.80 ? 1475 SER C OG 1 ATOM 12933 N N . GLY C 3 60 ? 8.255 41.377 75.157 1.00 174.36 ? 1476 GLY C N 1 ATOM 12934 C CA . GLY C 3 60 ? 8.247 40.013 75.657 1.00 178.46 ? 1476 GLY C CA 1 ATOM 12935 C C . GLY C 3 60 ? 9.090 39.818 76.904 1.00 189.85 ? 1476 GLY C C 1 ATOM 12936 O O . GLY C 3 60 ? 10.009 40.592 77.169 1.00 195.70 ? 1476 GLY C O 1 ATOM 12937 N N . LEU C 3 61 ? 8.773 38.779 77.672 1.00 194.87 ? 1477 LEU C N 1 ATOM 12938 C CA . LEU C 3 61 ? 9.493 38.491 78.910 1.00 195.40 ? 1477 LEU C CA 1 ATOM 12939 C C . LEU C 3 61 ? 9.998 37.050 78.940 1.00 200.49 ? 1477 LEU C C 1 ATOM 12940 O O . LEU C 3 61 ? 9.208 36.109 79.012 1.00 200.30 ? 1477 LEU C O 1 ATOM 12941 C CB . LEU C 3 61 ? 8.600 38.751 80.129 1.00 185.15 ? 1477 LEU C CB 1 ATOM 12942 C CG . LEU C 3 61 ? 8.036 40.157 80.366 1.00 177.45 ? 1477 LEU C CG 1 ATOM 12943 C CD1 . LEU C 3 61 ? 6.768 40.404 79.557 1.00 173.56 ? 1477 LEU C CD1 1 ATOM 12944 C CD2 . LEU C 3 61 ? 7.778 40.382 81.849 1.00 176.61 ? 1477 LEU C CD2 1 ATOM 12945 N N . LYS C 3 62 ? 11.318 36.888 78.898 1.00 203.07 ? 1478 LYS C N 1 ATOM 12946 C CA . LYS C 3 62 ? 11.949 35.570 78.922 1.00 210.47 ? 1478 LYS C CA 1 ATOM 12947 C C . LYS C 3 62 ? 13.273 35.619 79.682 1.00 214.29 ? 1478 LYS C C 1 ATOM 12948 O O . LYS C 3 62 ? 13.891 36.680 79.782 1.00 212.75 ? 1478 LYS C O 1 ATOM 12949 C CB . LYS C 3 62 ? 12.183 35.055 77.496 1.00 215.07 ? 1478 LYS C CB 1 ATOM 12950 C CG . LYS C 3 62 ? 10.922 34.654 76.743 1.00 208.95 ? 1478 LYS C CG 1 ATOM 12951 C CD . LYS C 3 62 ? 10.227 33.474 77.405 1.00 205.22 ? 1478 LYS C CD 1 ATOM 12952 C CE . LYS C 3 62 ? 11.098 32.228 77.371 1.00 212.12 ? 1478 LYS C CE 1 ATOM 12953 N NZ . LYS C 3 62 ? 10.423 31.063 78.006 1.00 212.88 ? 1478 LYS C NZ 1 ATOM 12954 N N . PRO C 3 63 ? 13.716 34.472 80.225 1.00 217.16 ? 1479 PRO C N 1 ATOM 12955 C CA . PRO C 3 63 ? 15.043 34.423 80.849 1.00 221.57 ? 1479 PRO C CA 1 ATOM 12956 C C . PRO C 3 63 ? 16.160 34.547 79.814 1.00 226.88 ? 1479 PRO C C 1 ATOM 12957 O O . PRO C 3 63 ? 15.879 34.617 78.617 1.00 223.64 ? 1479 PRO C O 1 ATOM 12958 C CB . PRO C 3 63 ? 15.066 33.048 81.524 1.00 222.52 ? 1479 PRO C CB 1 ATOM 12959 C CG . PRO C 3 63 ? 14.070 32.238 80.764 1.00 220.89 ? 1479 PRO C CG 1 ATOM 12960 C CD . PRO C 3 63 ? 12.989 33.200 80.375 1.00 214.77 ? 1479 PRO C CD 1 ATOM 12961 N N . GLY C 3 64 ? 17.410 34.568 80.267 1.00 232.73 ? 1480 GLY C N 1 ATOM 12962 C CA . GLY C 3 64 ? 18.532 34.760 79.367 1.00 237.25 ? 1480 GLY C CA 1 ATOM 12963 C C . GLY C 3 64 ? 18.757 33.613 78.399 1.00 242.33 ? 1480 GLY C C 1 ATOM 12964 O O . GLY C 3 64 ? 18.718 33.809 77.184 1.00 236.44 ? 1480 GLY C O 1 ATOM 12965 N N . VAL C 3 65 ? 18.971 32.417 78.946 1.00 251.83 ? 1481 VAL C N 1 ATOM 12966 C CA . VAL C 3 65 ? 19.237 31.205 78.163 1.00 259.02 ? 1481 VAL C CA 1 ATOM 12967 C C . VAL C 3 65 ? 20.307 31.449 77.091 1.00 267.21 ? 1481 VAL C C 1 ATOM 12968 O O . VAL C 3 65 ? 20.235 30.902 75.989 1.00 272.06 ? 1481 VAL C O 1 ATOM 12969 C CB . VAL C 3 65 ? 17.947 30.663 77.499 1.00 250.53 ? 1481 VAL C CB 1 ATOM 12970 C CG1 . VAL C 3 65 ? 18.062 29.164 77.248 1.00 258.69 ? 1481 VAL C CG1 1 ATOM 12971 C CG2 . VAL C 3 65 ? 16.738 30.941 78.379 1.00 240.41 ? 1481 VAL C CG2 1 ATOM 12972 N N . ASP C 3 66 ? 21.297 32.272 77.433 1.00 267.18 ? 1482 ASP C N 1 ATOM 12973 C CA . ASP C 3 66 ? 22.341 32.695 76.499 1.00 265.67 ? 1482 ASP C CA 1 ATOM 12974 C C . ASP C 3 66 ? 21.750 33.192 75.180 1.00 259.95 ? 1482 ASP C C 1 ATOM 12975 O O . ASP C 3 66 ? 21.975 32.596 74.127 1.00 264.17 ? 1482 ASP C O 1 ATOM 12976 C CB . ASP C 3 66 ? 23.325 31.552 76.232 1.00 271.29 ? 1482 ASP C CB 1 ATOM 12977 C CG . ASP C 3 66 ? 23.961 31.020 77.502 1.00 269.89 ? 1482 ASP C CG 1 ATOM 12978 O OD1 . ASP C 3 66 ? 24.003 31.762 78.504 1.00 263.55 ? 1482 ASP C OD1 1 ATOM 12979 O OD2 . ASP C 3 66 ? 24.422 29.859 77.495 1.00 275.10 ? 1482 ASP C OD2 1 ATOM 12980 N N . TYR C 3 67 ? 20.997 34.286 75.243 1.00 251.58 ? 1483 TYR C N 1 ATOM 12981 C CA . TYR C 3 67 ? 20.313 34.812 74.066 1.00 240.12 ? 1483 TYR C CA 1 ATOM 12982 C C . TYR C 3 67 ? 21.273 35.462 73.074 1.00 240.63 ? 1483 TYR C C 1 ATOM 12983 O O . TYR C 3 67 ? 22.251 36.098 73.463 1.00 244.65 ? 1483 TYR C O 1 ATOM 12984 C CB . TYR C 3 67 ? 19.237 35.819 74.482 1.00 227.60 ? 1483 TYR C CB 1 ATOM 12985 C CG . TYR C 3 67 ? 17.854 35.221 74.604 1.00 227.28 ? 1483 TYR C CG 1 ATOM 12986 C CD1 . TYR C 3 67 ? 16.848 35.882 75.298 1.00 221.79 ? 1483 TYR C CD1 1 ATOM 12987 C CD2 . TYR C 3 67 ? 17.552 33.997 74.021 1.00 234.81 ? 1483 TYR C CD2 1 ATOM 12988 C CE1 . TYR C 3 67 ? 15.581 35.339 75.409 1.00 220.67 ? 1483 TYR C CE1 1 ATOM 12989 C CE2 . TYR C 3 67 ? 16.289 33.447 74.127 1.00 233.83 ? 1483 TYR C CE2 1 ATOM 12990 C CZ . TYR C 3 67 ? 15.308 34.121 74.822 1.00 227.01 ? 1483 TYR C CZ 1 ATOM 12991 O OH . TYR C 3 67 ? 14.049 33.576 74.929 1.00 225.70 ? 1483 TYR C OH 1 ATOM 12992 N N . THR C 3 68 ? 20.981 35.290 71.789 1.00 274.26 ? 1484 THR C N 1 ATOM 12993 C CA . THR C 3 68 ? 21.778 35.890 70.726 1.00 266.75 ? 1484 THR C CA 1 ATOM 12994 C C . THR C 3 68 ? 20.878 36.425 69.615 1.00 254.17 ? 1484 THR C C 1 ATOM 12995 O O . THR C 3 68 ? 19.984 35.728 69.139 1.00 251.34 ? 1484 THR C O 1 ATOM 12996 C CB . THR C 3 68 ? 22.782 34.880 70.133 1.00 268.78 ? 1484 THR C CB 1 ATOM 12997 O OG1 . THR C 3 68 ? 23.265 35.366 68.874 1.00 260.30 ? 1484 THR C OG1 1 ATOM 12998 C CG2 . THR C 3 68 ? 22.121 33.523 69.926 1.00 271.18 ? 1484 THR C CG2 1 ATOM 12999 N N . ILE C 3 69 ? 21.110 37.667 69.202 1.00 246.27 ? 1485 ILE C N 1 ATOM 13000 C CA . ILE C 3 69 ? 20.232 38.286 68.220 1.00 233.21 ? 1485 ILE C CA 1 ATOM 13001 C C . ILE C 3 69 ? 20.891 38.309 66.856 1.00 223.90 ? 1485 ILE C C 1 ATOM 13002 O O . ILE C 3 69 ? 22.070 37.998 66.723 1.00 224.23 ? 1485 ILE C O 1 ATOM 13003 C CB . ILE C 3 69 ? 19.864 39.734 68.632 1.00 227.72 ? 1485 ILE C CB 1 ATOM 13004 C CG1 . ILE C 3 69 ? 19.831 39.874 70.152 1.00 235.60 ? 1485 ILE C CG1 1 ATOM 13005 C CG2 . ILE C 3 69 ? 18.525 40.166 68.033 1.00 218.36 ? 1485 ILE C CG2 1 ATOM 13006 C CD1 . ILE C 3 69 ? 18.644 39.193 70.794 1.00 240.35 ? 1485 ILE C CD1 1 ATOM 13007 N N . THR C 3 70 ? 20.117 38.712 65.857 1.00 214.20 ? 1486 THR C N 1 ATOM 13008 C CA . THR C 3 70 ? 20.606 38.963 64.514 1.00 207.60 ? 1486 THR C CA 1 ATOM 13009 C C . THR C 3 70 ? 19.691 40.021 63.907 1.00 197.29 ? 1486 THR C C 1 ATOM 13010 O O . THR C 3 70 ? 18.522 40.144 64.281 1.00 201.54 ? 1486 THR C O 1 ATOM 13011 C CB . THR C 3 70 ? 20.624 37.688 63.629 1.00 212.85 ? 1486 THR C CB 1 ATOM 13012 O OG1 . THR C 3 70 ? 19.475 36.886 63.919 1.00 214.03 ? 1486 THR C OG1 1 ATOM 13013 C CG2 . THR C 3 70 ? 21.873 36.861 63.888 1.00 217.59 ? 1486 THR C CG2 1 ATOM 13014 N N . VAL C 3 71 ? 20.240 40.806 62.989 1.00 189.07 ? 1487 VAL C N 1 ATOM 13015 C CA . VAL C 3 71 ? 19.457 41.803 62.275 1.00 179.28 ? 1487 VAL C CA 1 ATOM 13016 C C . VAL C 3 71 ? 19.839 41.844 60.791 1.00 176.97 ? 1487 VAL C C 1 ATOM 13017 O O . VAL C 3 71 ? 21.006 42.000 60.440 1.00 183.58 ? 1487 VAL C O 1 ATOM 13018 C CB . VAL C 3 71 ? 19.612 43.202 62.921 1.00 177.36 ? 1487 VAL C CB 1 ATOM 13019 C CG1 . VAL C 3 71 ? 20.989 43.363 63.576 1.00 185.60 ? 1487 VAL C CG1 1 ATOM 13020 C CG2 . VAL C 3 71 ? 19.337 44.317 61.910 1.00 168.35 ? 1487 VAL C CG2 1 ATOM 13021 N N . TYR C 3 72 ? 18.816 41.712 59.943 1.00 170.88 ? 1488 TYR C N 1 ATOM 13022 C CA . TYR C 3 72 ? 18.947 41.609 58.491 1.00 155.61 ? 1488 TYR C CA 1 ATOM 13023 C C . TYR C 3 72 ? 18.666 42.898 57.756 1.00 148.60 ? 1488 TYR C C 1 ATOM 13024 O O . TYR C 3 72 ? 17.525 43.345 57.659 1.00 146.04 ? 1488 TYR C O 1 ATOM 13025 C CB . TYR C 3 72 ? 18.016 40.517 57.940 1.00 157.69 ? 1488 TYR C CB 1 ATOM 13026 C CG . TYR C 3 72 ? 18.525 39.114 58.110 1.00 163.14 ? 1488 TYR C CG 1 ATOM 13027 C CD1 . TYR C 3 72 ? 19.481 38.603 57.252 1.00 158.07 ? 1488 TYR C CD1 1 ATOM 13028 C CD2 . TYR C 3 72 ? 18.034 38.298 59.112 1.00 171.64 ? 1488 TYR C CD2 1 ATOM 13029 C CE1 . TYR C 3 72 ? 19.948 37.309 57.385 1.00 172.00 ? 1488 TYR C CE1 1 ATOM 13030 C CE2 . TYR C 3 72 ? 18.489 36.997 59.263 1.00 178.68 ? 1488 TYR C CE2 1 ATOM 13031 C CZ . TYR C 3 72 ? 19.447 36.509 58.396 1.00 178.67 ? 1488 TYR C CZ 1 ATOM 13032 O OH . TYR C 3 72 ? 19.899 35.223 58.543 1.00 184.55 ? 1488 TYR C OH 1 ATOM 13033 N N . ALA C 3 73 ? 19.743 43.447 57.201 1.00 145.84 ? 1489 ALA C N 1 ATOM 13034 C CA . ALA C 3 73 ? 19.690 44.627 56.358 1.00 139.45 ? 1489 ALA C CA 1 ATOM 13035 C C . ALA C 3 73 ? 19.420 44.184 54.942 1.00 133.42 ? 1489 ALA C C 1 ATOM 13036 O O . ALA C 3 73 ? 20.254 43.513 54.333 1.00 153.08 ? 1489 ALA C O 1 ATOM 13037 C CB . ALA C 3 73 ? 21.008 45.410 56.429 1.00 155.98 ? 1489 ALA C CB 1 ATOM 13038 N N . VAL C 3 74 ? 18.254 44.549 54.423 1.00 129.48 ? 1490 VAL C N 1 ATOM 13039 C CA . VAL C 3 74 ? 17.813 44.040 53.136 1.00 124.63 ? 1490 VAL C CA 1 ATOM 13040 C C . VAL C 3 74 ? 17.970 45.114 52.072 1.00 129.46 ? 1490 VAL C C 1 ATOM 13041 O O . VAL C 3 74 ? 17.255 46.116 52.065 1.00 116.60 ? 1490 VAL C O 1 ATOM 13042 C CB . VAL C 3 74 ? 16.351 43.545 53.204 1.00 125.22 ? 1490 VAL C CB 1 ATOM 13043 C CG1 . VAL C 3 74 ? 15.496 44.492 54.024 1.00 126.38 ? 1490 VAL C CG1 1 ATOM 13044 C CG2 . VAL C 3 74 ? 15.765 43.362 51.806 1.00 119.89 ? 1490 VAL C CG2 1 ATOM 13045 N N . THR C 3 75 ? 18.939 44.898 51.188 1.00 95.11 ? 1491 THR C N 1 ATOM 13046 C CA . THR C 3 75 ? 19.192 45.796 50.072 1.00 89.35 ? 1491 THR C CA 1 ATOM 13047 C C . THR C 3 75 ? 19.488 44.989 48.818 1.00 101.37 ? 1491 THR C C 1 ATOM 13048 O O . THR C 3 75 ? 20.409 44.171 48.799 1.00 129.48 ? 1491 THR C O 1 ATOM 13049 C CB . THR C 3 75 ? 20.376 46.747 50.346 1.00 101.38 ? 1491 THR C CB 1 ATOM 13050 O OG1 . THR C 3 75 ? 21.555 45.978 50.614 1.00 104.29 ? 1491 THR C OG1 1 ATOM 13051 C CG2 . THR C 3 75 ? 20.086 47.656 51.529 1.00 121.32 ? 1491 THR C CG2 1 ATOM 13052 N N . GLY C 3 76 ? 18.702 45.217 47.775 1.00 81.76 ? 1492 GLY C N 1 ATOM 13053 C CA . GLY C 3 76 ? 18.967 44.623 46.479 1.00 80.38 ? 1492 GLY C CA 1 ATOM 13054 C C . GLY C 3 76 ? 17.899 45.030 45.489 1.00 78.13 ? 1492 GLY C C 1 ATOM 13055 O O . GLY C 3 76 ? 16.786 45.383 45.879 1.00 89.57 ? 1492 GLY C O 1 ATOM 13056 N N . ARG C 3 77 ? 18.231 44.982 44.205 1.00 69.99 ? 1493 ARG C N 1 ATOM 13057 C CA . ARG C 3 77 ? 17.297 45.415 43.175 1.00 69.85 ? 1493 ARG C CA 1 ATOM 13058 C C . ARG C 3 77 ? 17.190 44.424 42.020 1.00 81.98 ? 1493 ARG C C 1 ATOM 13059 O O . ARG C 3 77 ? 16.133 43.837 41.785 1.00 98.68 ? 1493 ARG C O 1 ATOM 13060 C CB . ARG C 3 77 ? 17.696 46.790 42.651 1.00 70.15 ? 1493 ARG C CB 1 ATOM 13061 C CG . ARG C 3 77 ? 16.534 47.753 42.567 1.00 72.83 ? 1493 ARG C CG 1 ATOM 13062 C CD . ARG C 3 77 ? 16.289 48.473 43.877 1.00 60.07 ? 1493 ARG C CD 1 ATOM 13063 N NE . ARG C 3 77 ? 16.468 49.913 43.722 1.00 82.25 ? 1493 ARG C NE 1 ATOM 13064 C CZ . ARG C 3 77 ? 15.576 50.721 43.155 1.00 87.90 ? 1493 ARG C CZ 1 ATOM 13065 N NH1 . ARG C 3 77 ? 14.437 50.230 42.686 1.00 72.97 ? 1493 ARG C NH1 1 ATOM 13066 N NH2 . ARG C 3 77 ? 15.825 52.019 43.055 1.00 97.68 ? 1493 ARG C NH2 1 ATOM 13067 N N . GLY C 3 78 ? 18.293 44.245 41.301 1.00 76.40 ? 1494 GLY C N 1 ATOM 13068 C CA . GLY C 3 78 ? 18.324 43.375 40.139 1.00 78.57 ? 1494 GLY C CA 1 ATOM 13069 C C . GLY C 3 78 ? 18.508 41.942 40.583 1.00 74.46 ? 1494 GLY C C 1 ATOM 13070 O O . GLY C 3 78 ? 18.073 41.576 41.674 1.00 66.46 ? 1494 GLY C O 1 ATOM 13071 N N . ASP C 3 79 ? 19.140 41.116 39.757 1.00 65.77 ? 1495 ASP C N 1 ATOM 13072 C CA . ASP C 3 79 ? 19.327 39.738 40.171 1.00 78.51 ? 1495 ASP C CA 1 ATOM 13073 C C . ASP C 3 79 ? 20.459 39.701 41.181 1.00 86.74 ? 1495 ASP C C 1 ATOM 13074 O O . ASP C 3 79 ? 21.622 39.949 40.857 1.00 92.39 ? 1495 ASP C O 1 ATOM 13075 C CB . ASP C 3 79 ? 19.629 38.838 38.972 1.00 80.13 ? 1495 ASP C CB 1 ATOM 13076 C CG . ASP C 3 79 ? 20.354 37.564 39.362 1.00 74.60 ? 1495 ASP C CG 1 ATOM 13077 O OD1 . ASP C 3 79 ? 19.912 36.888 40.315 1.00 77.71 ? 1495 ASP C OD1 1 ATOM 13078 O OD2 . ASP C 3 79 ? 21.373 37.241 38.716 1.00 76.04 ? 1495 ASP C OD2 1 ATOM 13079 N N . SER C 3 80 ? 20.075 39.350 42.404 1.00 97.95 ? 1496 SER C N 1 ATOM 13080 C CA . SER C 3 80 ? 20.928 39.356 43.583 1.00 99.19 ? 1496 SER C CA 1 ATOM 13081 C C . SER C 3 80 ? 20.014 39.108 44.772 1.00 99.73 ? 1496 SER C C 1 ATOM 13082 O O . SER C 3 80 ? 18.865 39.551 44.767 1.00 80.42 ? 1496 SER C O 1 ATOM 13083 C CB . SER C 3 80 ? 21.676 40.682 43.747 1.00 97.25 ? 1496 SER C CB 1 ATOM 13084 O OG . SER C 3 80 ? 20.775 41.775 43.797 1.00 94.13 ? 1496 SER C OG 1 ATOM 13085 N N . PRO C 3 81 ? 20.510 38.407 45.798 1.00 108.12 ? 1497 PRO C N 1 ATOM 13086 C CA . PRO C 3 81 ? 19.687 38.264 47.002 1.00 110.81 ? 1497 PRO C CA 1 ATOM 13087 C C . PRO C 3 81 ? 19.502 39.627 47.647 1.00 105.72 ? 1497 PRO C C 1 ATOM 13088 O O . PRO C 3 81 ? 20.389 40.468 47.497 1.00 111.17 ? 1497 PRO C O 1 ATOM 13089 C CB . PRO C 3 81 ? 20.515 37.334 47.898 1.00 122.25 ? 1497 PRO C CB 1 ATOM 13090 C CG . PRO C 3 81 ? 21.557 36.731 46.997 1.00 121.78 ? 1497 PRO C CG 1 ATOM 13091 C CD . PRO C 3 81 ? 21.816 37.745 45.934 1.00 116.29 ? 1497 PRO C CD 1 ATOM 13092 N N . ALA C 3 82 ? 18.398 39.863 48.346 1.00 108.82 ? 1498 ALA C N 1 ATOM 13093 C CA . ALA C 3 82 ? 18.288 41.139 49.029 1.00 122.69 ? 1498 ALA C CA 1 ATOM 13094 C C . ALA C 3 82 ? 18.634 40.930 50.493 1.00 137.71 ? 1498 ALA C C 1 ATOM 13095 O O . ALA C 3 82 ? 17.809 40.494 51.298 1.00 141.08 ? 1498 ALA C O 1 ATOM 13096 C CB . ALA C 3 82 ? 16.893 41.715 48.872 1.00 121.35 ? 1498 ALA C CB 1 ATOM 13097 N N . SER C 3 83 ? 19.875 41.292 50.801 1.00 143.56 ? 1499 SER C N 1 ATOM 13098 C CA . SER C 3 83 ? 20.514 41.133 52.101 1.00 143.98 ? 1499 SER C CA 1 ATOM 13099 C C . SER C 3 83 ? 21.979 41.466 51.870 1.00 148.73 ? 1499 SER C C 1 ATOM 13100 O O . SER C 3 83 ? 22.385 41.703 50.732 1.00 149.75 ? 1499 SER C O 1 ATOM 13101 C CB . SER C 3 83 ? 20.357 39.719 52.666 1.00 143.86 ? 1499 SER C CB 1 ATOM 13102 O OG . SER C 3 83 ? 19.027 39.482 53.095 1.00 138.01 ? 1499 SER C OG 1 ATOM 13103 N N . SER C 3 84 ? 22.780 41.483 52.927 1.00 155.89 ? 1500 SER C N 1 ATOM 13104 C CA . SER C 3 84 ? 24.223 41.456 52.732 1.00 161.56 ? 1500 SER C CA 1 ATOM 13105 C C . SER C 3 84 ? 24.793 40.228 53.425 1.00 163.32 ? 1500 SER C C 1 ATOM 13106 O O . SER C 3 84 ? 25.071 39.216 52.781 1.00 170.35 ? 1500 SER C O 1 ATOM 13107 C CB . SER C 3 84 ? 24.872 42.731 53.270 1.00 169.69 ? 1500 SER C CB 1 ATOM 13108 O OG . SER C 3 84 ? 24.578 42.908 54.644 1.00 175.49 ? 1500 SER C OG 1 ATOM 13109 N N . LYS C 3 85 ? 24.941 40.319 54.742 1.00 162.89 ? 1501 LYS C N 1 ATOM 13110 C CA . LYS C 3 85 ? 25.233 39.163 55.581 1.00 171.53 ? 1501 LYS C CA 1 ATOM 13111 C C . LYS C 3 85 ? 24.617 39.368 56.957 1.00 172.00 ? 1501 LYS C C 1 ATOM 13112 O O . LYS C 3 85 ? 24.553 40.495 57.447 1.00 169.91 ? 1501 LYS C O 1 ATOM 13113 C CB . LYS C 3 85 ? 26.742 38.931 55.701 1.00 185.79 ? 1501 LYS C CB 1 ATOM 13114 C CG . LYS C 3 85 ? 27.344 38.127 54.560 1.00 182.70 ? 1501 LYS C CG 1 ATOM 13115 C CD . LYS C 3 85 ? 28.835 37.910 54.748 1.00 191.45 ? 1501 LYS C CD 1 ATOM 13116 C CE . LYS C 3 85 ? 29.414 37.093 53.605 1.00 191.78 ? 1501 LYS C CE 1 ATOM 13117 N NZ . LYS C 3 85 ? 30.873 36.854 53.775 1.00 201.51 ? 1501 LYS C NZ 1 ATOM 13118 N N . PRO C 3 86 ? 24.155 38.280 57.588 1.00 173.78 ? 1502 PRO C N 1 ATOM 13119 C CA . PRO C 3 86 ? 23.715 38.388 58.982 1.00 178.23 ? 1502 PRO C CA 1 ATOM 13120 C C . PRO C 3 86 ? 24.891 38.579 59.937 1.00 195.72 ? 1502 PRO C C 1 ATOM 13121 O O . PRO C 3 86 ? 25.897 37.879 59.826 1.00 204.81 ? 1502 PRO C O 1 ATOM 13122 C CB . PRO C 3 86 ? 23.011 37.051 59.232 1.00 179.38 ? 1502 PRO C CB 1 ATOM 13123 C CG . PRO C 3 86 ? 23.634 36.111 58.257 1.00 184.34 ? 1502 PRO C CG 1 ATOM 13124 C CD . PRO C 3 86 ? 23.941 36.931 57.038 1.00 176.13 ? 1502 PRO C CD 1 ATOM 13125 N N . ILE C 3 87 ? 24.760 39.523 60.863 1.00 185.08 ? 1503 ILE C N 1 ATOM 13126 C CA . ILE C 3 87 ? 25.739 39.708 61.928 1.00 186.15 ? 1503 ILE C CA 1 ATOM 13127 C C . ILE C 3 87 ? 24.985 39.483 63.233 1.00 187.14 ? 1503 ILE C C 1 ATOM 13128 O O . ILE C 3 87 ? 23.795 39.176 63.192 1.00 179.08 ? 1503 ILE C O 1 ATOM 13129 C CB . ILE C 3 87 ? 26.398 41.101 61.874 1.00 192.77 ? 1503 ILE C CB 1 ATOM 13130 C CG1 . ILE C 3 87 ? 26.462 41.587 60.421 1.00 190.56 ? 1503 ILE C CG1 1 ATOM 13131 C CG2 . ILE C 3 87 ? 27.781 41.070 62.522 1.00 194.62 ? 1503 ILE C CG2 1 ATOM 13132 C CD1 . ILE C 3 87 ? 27.742 42.291 60.039 1.00 189.86 ? 1503 ILE C CD1 1 ATOM 13133 N N . SER C 3 88 ? 25.631 39.664 64.382 1.00 193.38 ? 1504 SER C N 1 ATOM 13134 C CA . SER C 3 88 ? 25.036 39.190 65.630 1.00 193.89 ? 1504 SER C CA 1 ATOM 13135 C C . SER C 3 88 ? 25.773 39.586 66.905 1.00 201.45 ? 1504 SER C C 1 ATOM 13136 O O . SER C 3 88 ? 26.930 40.004 66.878 1.00 204.54 ? 1504 SER C O 1 ATOM 13137 C CB . SER C 3 88 ? 24.934 37.662 65.595 1.00 188.12 ? 1504 SER C CB 1 ATOM 13138 O OG . SER C 3 88 ? 24.328 37.164 66.775 1.00 191.64 ? 1504 SER C OG 1 ATOM 13139 N N . ILE C 3 89 ? 25.063 39.442 68.021 1.00 204.22 ? 1505 ILE C N 1 ATOM 13140 C CA . ILE C 3 89 ? 25.583 39.731 69.353 1.00 217.27 ? 1505 ILE C CA 1 ATOM 13141 C C . ILE C 3 89 ? 25.196 38.613 70.315 1.00 223.50 ? 1505 ILE C C 1 ATOM 13142 O O . ILE C 3 89 ? 24.362 37.769 69.991 1.00 222.32 ? 1505 ILE C O 1 ATOM 13143 C CB . ILE C 3 89 ? 25.046 41.067 69.907 1.00 224.13 ? 1505 ILE C CB 1 ATOM 13144 C CG1 . ILE C 3 89 ? 23.522 41.014 70.035 1.00 218.48 ? 1505 ILE C CG1 1 ATOM 13145 C CG2 . ILE C 3 89 ? 25.470 42.229 69.029 1.00 227.53 ? 1505 ILE C CG2 1 ATOM 13146 C CD1 . ILE C 3 89 ? 22.910 42.282 70.589 1.00 220.89 ? 1505 ILE C CD1 1 ATOM 13147 N N . ASN C 3 90 ? 25.804 38.609 71.496 1.00 227.11 ? 1506 ASN C N 1 ATOM 13148 C CA . ASN C 3 90 ? 25.433 37.665 72.544 1.00 219.62 ? 1506 ASN C CA 1 ATOM 13149 C C . ASN C 3 90 ? 25.218 38.376 73.875 1.00 228.84 ? 1506 ASN C C 1 ATOM 13150 O O . ASN C 3 90 ? 26.143 38.974 74.426 1.00 235.43 ? 1506 ASN C O 1 ATOM 13151 C CB . ASN C 3 90 ? 26.497 36.576 72.690 1.00 214.87 ? 1506 ASN C CB 1 ATOM 13152 C CG . ASN C 3 90 ? 26.539 35.640 71.498 1.00 208.18 ? 1506 ASN C CG 1 ATOM 13153 O OD1 . ASN C 3 90 ? 25.839 34.627 71.464 1.00 198.31 ? 1506 ASN C OD1 1 ATOM 13154 N ND2 . ASN C 3 90 ? 27.361 35.974 70.511 1.00 211.54 ? 1506 ASN C ND2 1 ATOM 13155 N N . TYR C 3 91 ? 23.994 38.308 74.389 1.00 234.34 ? 1507 TYR C N 1 ATOM 13156 C CA . TYR C 3 91 ? 23.637 39.013 75.615 1.00 248.03 ? 1507 TYR C CA 1 ATOM 13157 C C . TYR C 3 91 ? 22.675 38.188 76.467 1.00 245.44 ? 1507 TYR C C 1 ATOM 13158 O O . TYR C 3 91 ? 21.844 37.449 75.941 1.00 241.84 ? 1507 TYR C O 1 ATOM 13159 C CB . TYR C 3 91 ? 23.020 40.373 75.280 1.00 256.96 ? 1507 TYR C CB 1 ATOM 13160 C CG . TYR C 3 91 ? 22.862 41.297 76.467 1.00 265.66 ? 1507 TYR C CG 1 ATOM 13161 C CD1 . TYR C 3 91 ? 23.952 41.987 76.982 1.00 271.02 ? 1507 TYR C CD1 1 ATOM 13162 C CD2 . TYR C 3 91 ? 21.623 41.489 77.063 1.00 265.98 ? 1507 TYR C CD2 1 ATOM 13163 C CE1 . TYR C 3 91 ? 23.813 42.836 78.064 1.00 276.28 ? 1507 TYR C CE1 1 ATOM 13164 C CE2 . TYR C 3 91 ? 21.475 42.337 78.145 1.00 271.73 ? 1507 TYR C CE2 1 ATOM 13165 C CZ . TYR C 3 91 ? 22.573 43.007 78.641 1.00 276.68 ? 1507 TYR C CZ 1 ATOM 13166 O OH . TYR C 3 91 ? 22.431 43.852 79.718 1.00 282.52 ? 1507 TYR C OH 1 ATOM 13167 N N . ARG C 3 92 ? 22.791 38.321 77.785 1.00 244.91 ? 1508 ARG C N 1 ATOM 13168 C CA . ARG C 3 92 ? 21.956 37.558 78.707 1.00 236.39 ? 1508 ARG C CA 1 ATOM 13169 C C . ARG C 3 92 ? 21.060 38.461 79.547 1.00 235.86 ? 1508 ARG C C 1 ATOM 13170 O O . ARG C 3 92 ? 21.366 39.634 79.760 1.00 238.24 ? 1508 ARG C O 1 ATOM 13171 C CB . ARG C 3 92 ? 22.823 36.692 79.624 1.00 233.33 ? 1508 ARG C CB 1 ATOM 13172 C CG . ARG C 3 92 ? 23.532 35.550 78.918 1.00 223.50 ? 1508 ARG C CG 1 ATOM 13173 C CD . ARG C 3 92 ? 24.215 34.628 79.915 1.00 220.10 ? 1508 ARG C CD 1 ATOM 13174 N NE . ARG C 3 92 ? 25.346 35.269 80.579 1.00 227.30 ? 1508 ARG C NE 1 ATOM 13175 C CZ . ARG C 3 92 ? 26.606 35.172 80.165 1.00 229.96 ? 1508 ARG C CZ 1 ATOM 13176 N NH1 . ARG C 3 92 ? 26.898 34.459 79.087 1.00 225.50 ? 1508 ARG C NH1 1 ATOM 13177 N NH2 . ARG C 3 92 ? 27.574 35.788 80.830 1.00 234.62 ? 1508 ARG C NH2 1 ATOM 13178 N N . THR C 3 93 ? 19.952 37.903 80.024 1.00 232.63 ? 1509 THR C N 1 ATOM 13179 C CA . THR C 3 93 ? 19.011 38.648 80.853 1.00 239.04 ? 1509 THR C CA 1 ATOM 13180 C C . THR C 3 93 ? 19.318 38.463 82.335 1.00 243.53 ? 1509 THR C C 1 ATOM 13181 O O . THR C 3 93 ? 19.077 37.396 82.901 1.00 238.32 ? 1509 THR C O 1 ATOM 13182 C CB . THR C 3 93 ? 17.557 38.218 80.581 1.00 235.69 ? 1509 THR C CB 1 ATOM 13183 O OG1 . THR C 3 93 ? 17.254 38.397 79.192 1.00 227.33 ? 1509 THR C OG1 1 ATOM 13184 C CG2 . THR C 3 93 ? 16.592 39.044 81.418 1.00 243.70 ? 1509 THR C CG2 1 HETATM 13185 C C1 . NAG D 4 . ? 21.843 45.127 7.038 1.00 74.37 ? 1001 NAG A C1 1 HETATM 13186 C C2 . NAG D 4 . ? 21.076 43.852 6.725 1.00 80.61 ? 1001 NAG A C2 1 HETATM 13187 C C3 . NAG D 4 . ? 21.617 42.699 7.568 1.00 79.08 ? 1001 NAG A C3 1 HETATM 13188 C C4 . NAG D 4 . ? 23.134 42.594 7.452 1.00 76.85 ? 1001 NAG A C4 1 HETATM 13189 C C5 . NAG D 4 . ? 23.804 43.957 7.640 1.00 67.08 ? 1001 NAG A C5 1 HETATM 13190 C C6 . NAG D 4 . ? 25.282 43.944 7.325 1.00 66.19 ? 1001 NAG A C6 1 HETATM 13191 C C7 . NAG D 4 . ? 18.821 44.548 6.047 1.00 89.00 ? 1001 NAG A C7 1 HETATM 13192 C C8 . NAG D 4 . ? 17.386 44.664 6.459 1.00 87.69 ? 1001 NAG A C8 1 HETATM 13193 N N2 . NAG D 4 . ? 19.653 44.031 6.958 1.00 82.08 ? 1001 NAG A N2 1 HETATM 13194 O O3 . NAG D 4 . ? 21.012 41.482 7.146 1.00 69.00 ? 1001 NAG A O3 1 HETATM 13195 O O4 . NAG D 4 . ? 23.609 41.728 8.476 1.00 92.40 ? 1001 NAG A O4 1 HETATM 13196 O O5 . NAG D 4 . ? 23.210 44.931 6.771 1.00 72.24 ? 1001 NAG A O5 1 HETATM 13197 O O6 . NAG D 4 . ? 25.548 44.543 6.064 1.00 75.09 ? 1001 NAG A O6 1 HETATM 13198 O O7 . NAG D 4 . ? 19.212 44.909 4.941 1.00 96.65 ? 1001 NAG A O7 1 HETATM 13199 C C1 . NAG E 4 . ? 24.314 40.597 7.937 1.00 103.73 ? 1002 NAG A C1 1 HETATM 13200 C C2 . NAG E 4 . ? 25.384 40.204 8.949 1.00 106.05 ? 1002 NAG A C2 1 HETATM 13201 C C3 . NAG E 4 . ? 26.161 38.991 8.449 1.00 112.01 ? 1002 NAG A C3 1 HETATM 13202 C C4 . NAG E 4 . ? 25.207 37.858 8.094 1.00 118.39 ? 1002 NAG A C4 1 HETATM 13203 C C5 . NAG E 4 . ? 24.130 38.353 7.131 1.00 113.39 ? 1002 NAG A C5 1 HETATM 13204 C C6 . NAG E 4 . ? 23.068 37.316 6.848 1.00 113.25 ? 1002 NAG A C6 1 HETATM 13205 C C7 . NAG E 4 . ? 26.297 41.989 10.371 1.00 117.22 ? 1002 NAG A C7 1 HETATM 13206 C C8 . NAG E 4 . ? 25.314 41.536 11.409 1.00 119.79 ? 1002 NAG A C8 1 HETATM 13207 N N2 . NAG E 4 . ? 26.284 41.314 9.215 1.00 107.18 ? 1002 NAG A N2 1 HETATM 13208 O O3 . NAG E 4 . ? 27.068 38.565 9.460 1.00 117.34 ? 1002 NAG A O3 1 HETATM 13209 O O4 . NAG E 4 . ? 25.933 36.799 7.481 1.00 138.69 ? 1002 NAG A O4 1 HETATM 13210 O O5 . NAG E 4 . ? 23.456 39.489 7.693 1.00 115.75 ? 1002 NAG A O5 1 HETATM 13211 O O6 . NAG E 4 . ? 21.832 37.661 7.459 1.00 116.57 ? 1002 NAG A O6 1 HETATM 13212 O O7 . NAG E 4 . ? 27.067 42.922 10.569 1.00 120.19 ? 1002 NAG A O7 1 HETATM 13213 C C1 . BMA F 5 . ? 25.935 35.651 8.347 1.00 156.01 ? 1003 BMA A C1 1 HETATM 13214 C C2 . BMA F 5 . ? 25.447 34.453 7.542 1.00 160.19 ? 1003 BMA A C2 1 HETATM 13215 C C3 . BMA F 5 . ? 25.515 33.190 8.437 1.00 162.42 ? 1003 BMA A C3 1 HETATM 13216 C C4 . BMA F 5 . ? 26.922 33.008 9.025 1.00 159.84 ? 1003 BMA A C4 1 HETATM 13217 C C5 . BMA F 5 . ? 27.271 34.280 9.822 1.00 158.33 ? 1003 BMA A C5 1 HETATM 13218 C C6 . BMA F 5 . ? 28.652 34.239 10.452 1.00 152.16 ? 1003 BMA A C6 1 HETATM 13219 O O2 . BMA F 5 . ? 26.307 34.273 6.427 1.00 157.24 ? 1003 BMA A O2 1 HETATM 13220 O O3 . BMA F 5 . ? 24.971 31.970 7.840 1.00 169.25 ? 1003 BMA A O3 1 HETATM 13221 O O4 . BMA F 5 . ? 26.953 31.886 9.889 1.00 161.25 ? 1003 BMA A O4 1 HETATM 13222 O O5 . BMA F 5 . ? 27.211 35.418 8.928 1.00 160.71 ? 1003 BMA A O5 1 HETATM 13223 O O6 . BMA F 5 . ? 28.757 35.326 11.365 1.00 148.36 ? 1003 BMA A O6 1 HETATM 13224 C C1 . MAN G 6 . ? 25.834 31.335 6.873 1.00 175.55 ? 1004 MAN A C1 1 HETATM 13225 C C2 . MAN G 6 . ? 25.170 31.444 5.489 1.00 174.15 ? 1004 MAN A C2 1 HETATM 13226 C C3 . MAN G 6 . ? 23.980 30.496 5.417 1.00 172.99 ? 1004 MAN A C3 1 HETATM 13227 C C4 . MAN G 6 . ? 24.410 29.070 5.780 1.00 177.53 ? 1004 MAN A C4 1 HETATM 13228 C C5 . MAN G 6 . ? 25.059 29.058 7.175 1.00 174.95 ? 1004 MAN A C5 1 HETATM 13229 C C6 . MAN G 6 . ? 25.619 27.697 7.544 1.00 167.63 ? 1004 MAN A C6 1 HETATM 13230 O O2 . MAN G 6 . ? 26.059 31.030 4.449 1.00 170.78 ? 1004 MAN A O2 1 HETATM 13231 O O3 . MAN G 6 . ? 23.363 30.515 4.134 1.00 166.69 ? 1004 MAN A O3 1 HETATM 13232 O O4 . MAN G 6 . ? 23.281 28.209 5.778 1.00 180.62 ? 1004 MAN A O4 1 HETATM 13233 O O5 . MAN G 6 . ? 26.156 30.008 7.214 1.00 177.70 ? 1004 MAN A O5 1 HETATM 13234 O O6 . MAN G 6 . ? 26.034 27.737 8.904 1.00 164.97 ? 1004 MAN A O6 1 HETATM 13235 C C1 . NAG H 4 . ? -1.041 68.996 40.575 1.00 102.29 ? 1005 NAG A C1 1 HETATM 13236 C C2 . NAG H 4 . ? -0.786 70.121 41.569 1.00 110.12 ? 1005 NAG A C2 1 HETATM 13237 C C3 . NAG H 4 . ? -2.088 70.769 42.073 1.00 114.20 ? 1005 NAG A C3 1 HETATM 13238 C C4 . NAG H 4 . ? -3.360 70.029 41.642 1.00 114.75 ? 1005 NAG A C4 1 HETATM 13239 C C5 . NAG H 4 . ? -3.319 69.382 40.248 1.00 111.16 ? 1005 NAG A C5 1 HETATM 13240 C C6 . NAG H 4 . ? -4.231 70.064 39.254 1.00 102.42 ? 1005 NAG A C6 1 HETATM 13241 C C7 . NAG H 4 . ? 0.037 68.812 43.596 1.00 123.25 ? 1005 NAG A C7 1 HETATM 13242 C C8 . NAG H 4 . ? -1.170 67.917 43.562 1.00 115.40 ? 1005 NAG A C8 1 HETATM 13243 N N2 . NAG H 4 . ? 0.134 69.781 42.664 1.00 119.86 ? 1005 NAG A N2 1 HETATM 13244 O O3 . NAG H 4 . ? -2.142 72.119 41.628 1.00 120.39 ? 1005 NAG A O3 1 HETATM 13245 O O4 . NAG H 4 . ? -3.776 69.089 42.627 1.00 119.88 ? 1005 NAG A O4 1 HETATM 13246 O O5 . NAG H 4 . ? -2.004 69.400 39.682 1.00 110.69 ? 1005 NAG A O5 1 HETATM 13247 O O6 . NAG H 4 . ? -3.495 70.657 38.193 1.00 96.24 ? 1005 NAG A O6 1 HETATM 13248 O O7 . NAG H 4 . ? 0.909 68.666 44.448 1.00 131.37 ? 1005 NAG A O7 1 HETATM 13249 C C1 . NAG I 4 . ? -4.318 69.847 43.726 1.00 131.12 ? 1006 NAG A C1 1 HETATM 13250 C C2 . NAG I 4 . ? -5.813 69.574 43.869 1.00 134.38 ? 1006 NAG A C2 1 HETATM 13251 C C3 . NAG I 4 . ? -6.391 70.408 45.010 1.00 144.06 ? 1006 NAG A C3 1 HETATM 13252 C C4 . NAG I 4 . ? -5.594 70.189 46.289 1.00 142.76 ? 1006 NAG A C4 1 HETATM 13253 C C5 . NAG I 4 . ? -4.108 70.426 46.033 1.00 143.55 ? 1006 NAG A C5 1 HETATM 13254 C C6 . NAG I 4 . ? -3.242 70.109 47.230 1.00 140.59 ? 1006 NAG A C6 1 HETATM 13255 C C7 . NAG I 4 . ? -6.997 68.894 41.824 1.00 126.73 ? 1006 NAG A C7 1 HETATM 13256 C C8 . NAG I 4 . ? -6.777 67.481 42.277 1.00 125.75 ? 1006 NAG A C8 1 HETATM 13257 N N2 . NAG I 4 . ? -6.515 69.850 42.627 1.00 127.00 ? 1006 NAG A N2 1 HETATM 13258 O O3 . NAG I 4 . ? -7.752 70.047 45.216 1.00 148.14 ? 1006 NAG A O3 1 HETATM 13259 O O4 . NAG I 4 . ? -6.042 71.085 47.300 1.00 134.25 ? 1006 NAG A O4 1 HETATM 13260 O O5 . NAG I 4 . ? -3.660 69.580 44.962 1.00 138.48 ? 1006 NAG A O5 1 HETATM 13261 O O6 . NAG I 4 . ? -3.099 71.239 48.081 1.00 137.72 ? 1006 NAG A O6 1 HETATM 13262 O O7 . NAG I 4 . ? -7.585 69.157 40.781 1.00 130.20 ? 1006 NAG A O7 1 HETATM 13263 C C1 . NAG J 4 . ? -2.090 54.309 41.210 1.00 40.15 ? 1007 NAG A C1 1 HETATM 13264 C C2 . NAG J 4 . ? -2.204 55.262 42.392 1.00 43.30 ? 1007 NAG A C2 1 HETATM 13265 C C3 . NAG J 4 . ? -0.830 55.815 42.756 1.00 46.27 ? 1007 NAG A C3 1 HETATM 13266 C C4 . NAG J 4 . ? 0.174 54.684 42.948 1.00 52.57 ? 1007 NAG A C4 1 HETATM 13267 C C5 . NAG J 4 . ? 0.148 53.725 41.759 1.00 53.29 ? 1007 NAG A C5 1 HETATM 13268 C C6 . NAG J 4 . ? 0.997 52.494 41.976 1.00 60.08 ? 1007 NAG A C6 1 HETATM 13269 C C7 . NAG J 4 . ? -4.439 56.280 42.357 1.00 76.12 ? 1007 NAG A C7 1 HETATM 13270 C C8 . NAG J 4 . ? -5.243 57.490 41.989 1.00 83.93 ? 1007 NAG A C8 1 HETATM 13271 N N2 . NAG J 4 . ? -3.129 56.346 42.099 1.00 54.95 ? 1007 NAG A N2 1 HETATM 13272 O O3 . NAG J 4 . ? -0.935 56.577 43.953 1.00 58.02 ? 1007 NAG A O3 1 HETATM 13273 O O4 . NAG J 4 . ? 1.486 55.224 43.056 1.00 59.89 ? 1007 NAG A O4 1 HETATM 13274 O O5 . NAG J 4 . ? -1.191 53.265 41.530 1.00 48.13 ? 1007 NAG A O5 1 HETATM 13275 O O6 . NAG J 4 . ? 0.607 51.794 43.149 1.00 71.74 ? 1007 NAG A O6 1 HETATM 13276 O O7 . NAG J 4 . ? -4.953 55.287 42.863 1.00 85.21 ? 1007 NAG A O7 1 HETATM 13277 C C1 . NAG K 4 . ? 1.976 55.022 44.391 1.00 60.09 ? 1008 NAG A C1 1 HETATM 13278 C C2 . NAG K 4 . ? 3.462 55.362 44.428 1.00 49.68 ? 1008 NAG A C2 1 HETATM 13279 C C3 . NAG K 4 . ? 4.009 55.184 45.841 1.00 56.34 ? 1008 NAG A C3 1 HETATM 13280 C C4 . NAG K 4 . ? 3.167 55.967 46.841 1.00 67.37 ? 1008 NAG A C4 1 HETATM 13281 C C5 . NAG K 4 . ? 1.691 55.609 46.689 1.00 70.25 ? 1008 NAG A C5 1 HETATM 13282 C C6 . NAG K 4 . ? 0.786 56.451 47.558 1.00 84.06 ? 1008 NAG A C6 1 HETATM 13283 C C7 . NAG K 4 . ? 4.382 54.884 42.203 1.00 52.87 ? 1008 NAG A C7 1 HETATM 13284 C C8 . NAG K 4 . ? 5.180 53.925 41.372 1.00 57.58 ? 1008 NAG A C8 1 HETATM 13285 N N2 . NAG K 4 . ? 4.209 54.545 43.485 1.00 44.92 ? 1008 NAG A N2 1 HETATM 13286 O O3 . NAG K 4 . ? 5.357 55.636 45.882 1.00 55.21 ? 1008 NAG A O3 1 HETATM 13287 O O4 . NAG K 4 . ? 3.586 55.667 48.168 1.00 84.75 ? 1008 NAG A O4 1 HETATM 13288 O O5 . NAG K 4 . ? 1.277 55.826 45.333 1.00 67.01 ? 1008 NAG A O5 1 HETATM 13289 O O6 . NAG K 4 . ? 1.048 57.837 47.386 1.00 91.67 ? 1008 NAG A O6 1 HETATM 13290 O O7 . NAG K 4 . ? 3.915 55.917 41.735 1.00 73.43 ? 1008 NAG A O7 1 HETATM 13291 C C1 . BMA L 5 . ? 4.200 56.842 48.726 1.00 100.55 ? 1009 BMA A C1 1 HETATM 13292 C C2 . BMA L 5 . ? 3.910 56.907 50.224 1.00 113.19 ? 1009 BMA A C2 1 HETATM 13293 C C3 . BMA L 5 . ? 4.559 58.158 50.805 1.00 116.36 ? 1009 BMA A C3 1 HETATM 13294 C C4 . BMA L 5 . ? 6.045 58.253 50.411 1.00 100.10 ? 1009 BMA A C4 1 HETATM 13295 C C5 . BMA L 5 . ? 6.219 58.113 48.879 1.00 95.34 ? 1009 BMA A C5 1 HETATM 13296 C C6 . BMA L 5 . ? 7.673 58.025 48.419 1.00 102.52 ? 1009 BMA A C6 1 HETATM 13297 O O2 . BMA L 5 . ? 4.493 55.797 50.895 1.00 107.02 ? 1009 BMA A O2 1 HETATM 13298 O O3 . BMA L 5 . ? 4.429 58.206 52.222 1.00 127.82 ? 1009 BMA A O3 1 HETATM 13299 O O4 . BMA L 5 . ? 6.574 59.497 50.838 1.00 99.42 ? 1009 BMA A O4 1 HETATM 13300 O O5 . BMA L 5 . ? 5.579 56.899 48.456 1.00 93.81 ? 1009 BMA A O5 1 HETATM 13301 O O6 . BMA L 5 . ? 8.452 59.077 49.002 1.00 110.58 ? 1009 BMA A O6 1 HETATM 13302 C C1 . MAN M 6 . ? 3.046 58.408 52.565 1.00 125.53 ? 1010 MAN A C1 1 HETATM 13303 C C2 . MAN M 6 . ? 2.793 59.908 52.819 1.00 136.83 ? 1010 MAN A C2 1 HETATM 13304 C C3 . MAN M 6 . ? 3.345 60.316 54.188 1.00 141.32 ? 1010 MAN A C3 1 HETATM 13305 C C4 . MAN M 6 . ? 2.859 59.355 55.284 1.00 136.35 ? 1010 MAN A C4 1 HETATM 13306 C C5 . MAN M 6 . ? 3.243 57.917 54.910 1.00 126.16 ? 1010 MAN A C5 1 HETATM 13307 C C6 . MAN M 6 . ? 2.762 56.893 55.919 1.00 118.36 ? 1010 MAN A C6 1 HETATM 13308 O O2 . MAN M 6 . ? 1.393 60.198 52.867 1.00 139.07 ? 1010 MAN A O2 1 HETATM 13309 O O3 . MAN M 6 . ? 3.000 61.658 54.520 1.00 140.56 ? 1010 MAN A O3 1 HETATM 13310 O O4 . MAN M 6 . ? 3.452 59.697 56.528 1.00 128.49 ? 1010 MAN A O4 1 HETATM 13311 O O5 . MAN M 6 . ? 2.644 57.593 53.637 1.00 115.71 ? 1010 MAN A O5 1 HETATM 13312 O O6 . MAN M 6 . ? 3.321 55.632 55.569 1.00 114.39 ? 1010 MAN A O6 1 HETATM 13313 C C1 . BMA N 5 . ? 9.498 58.513 49.827 1.00 106.80 ? 1011 BMA A C1 1 HETATM 13314 C C2 . BMA N 5 . ? 10.160 57.293 49.176 1.00 101.81 ? 1011 BMA A C2 1 HETATM 13315 C C3 . BMA N 5 . ? 10.957 56.534 50.243 1.00 94.53 ? 1011 BMA A C3 1 HETATM 13316 C C4 . BMA N 5 . ? 11.339 57.417 51.479 1.00 119.74 ? 1011 BMA A C4 1 HETATM 13317 C C5 . BMA N 5 . ? 11.547 58.931 51.103 1.00 121.40 ? 1011 BMA A C5 1 HETATM 13318 C C6 . BMA N 5 . ? 12.892 59.228 50.439 1.00 129.49 ? 1011 BMA A C6 1 HETATM 13319 O O2 . BMA N 5 . ? 11.078 57.686 48.164 1.00 107.52 ? 1011 BMA A O2 1 HETATM 13320 O O3 . BMA N 5 . ? 12.120 55.922 49.694 1.00 92.33 ? 1011 BMA A O3 1 HETATM 13321 O O4 . BMA N 5 . ? 10.348 57.302 52.517 1.00 115.68 ? 1011 BMA A O4 1 HETATM 13322 O O5 . BMA N 5 . ? 10.465 59.456 50.253 1.00 108.24 ? 1011 BMA A O5 1 HETATM 13323 O O6 . BMA N 5 . ? 13.912 58.550 51.163 1.00 128.76 ? 1011 BMA A O6 1 HETATM 13324 C C1 . MAN O 6 . ? 10.613 56.297 53.531 1.00 113.34 ? 1012 MAN A C1 1 HETATM 13325 C C2 . MAN O 6 . ? 12.126 55.855 53.654 1.00 114.70 ? 1012 MAN A C2 1 HETATM 13326 C C3 . MAN O 6 . ? 12.410 54.449 53.071 1.00 110.32 ? 1012 MAN A C3 1 HETATM 13327 C C4 . MAN O 6 . ? 11.254 53.479 53.319 1.00 110.61 ? 1012 MAN A C4 1 HETATM 13328 C C5 . MAN O 6 . ? 9.989 54.084 52.736 1.00 115.23 ? 1012 MAN A C5 1 HETATM 13329 C C6 . MAN O 6 . ? 8.801 53.142 52.782 1.00 108.23 ? 1012 MAN A C6 1 HETATM 13330 O O2 . MAN O 6 . ? 12.534 55.793 55.023 1.00 120.29 ? 1012 MAN A O2 1 HETATM 13331 O O3 . MAN O 6 . ? 13.625 53.904 53.580 1.00 107.76 ? 1012 MAN A O3 1 HETATM 13332 O O4 . MAN O 6 . ? 11.518 52.237 52.686 1.00 107.79 ? 1012 MAN A O4 1 HETATM 13333 O O5 . MAN O 6 . ? 9.659 55.238 53.520 1.00 119.95 ? 1012 MAN A O5 1 HETATM 13334 O O6 . MAN O 6 . ? 7.769 53.691 51.968 1.00 103.74 ? 1012 MAN A O6 1 HETATM 13335 C C1 . NAG P 4 . ? -61.996 51.005 -10.415 1.00 92.41 ? 1013 NAG A C1 1 HETATM 13336 C C2 . NAG P 4 . ? -62.367 52.088 -9.403 1.00 99.35 ? 1013 NAG A C2 1 HETATM 13337 C C3 . NAG P 4 . ? -61.736 53.419 -9.804 1.00 100.37 ? 1013 NAG A C3 1 HETATM 13338 C C4 . NAG P 4 . ? -60.234 53.254 -10.002 1.00 114.54 ? 1013 NAG A C4 1 HETATM 13339 C C5 . NAG P 4 . ? -59.955 52.119 -10.985 1.00 109.27 ? 1013 NAG A C5 1 HETATM 13340 C C6 . NAG P 4 . ? -58.482 51.818 -11.140 1.00 110.69 ? 1013 NAG A C6 1 HETATM 13341 C C7 . NAG P 4 . ? -64.417 52.655 -8.175 1.00 118.68 ? 1013 NAG A C7 1 HETATM 13342 C C8 . NAG P 4 . ? -65.913 52.729 -8.229 1.00 115.08 ? 1013 NAG A C8 1 HETATM 13343 N N2 . NAG P 4 . ? -63.811 52.220 -9.285 1.00 110.40 ? 1013 NAG A N2 1 HETATM 13344 O O3 . NAG P 4 . ? -61.990 54.393 -8.798 1.00 94.77 ? 1013 NAG A O3 1 HETATM 13345 O O4 . NAG P 4 . ? -59.666 54.461 -10.498 1.00 132.22 ? 1013 NAG A O4 1 HETATM 13346 O O5 . NAG P 4 . ? -60.576 50.912 -10.518 1.00 106.51 ? 1013 NAG A O5 1 HETATM 13347 O O6 . NAG P 4 . ? -58.272 50.558 -11.763 1.00 121.34 ? 1013 NAG A O6 1 HETATM 13348 O O7 . NAG P 4 . ? -63.786 52.977 -7.173 1.00 124.90 ? 1013 NAG A O7 1 HETATM 13349 C C1 . NAG Q 4 . ? -58.809 54.997 -9.474 1.00 139.74 ? 1014 NAG A C1 1 HETATM 13350 C C2 . NAG Q 4 . ? -57.667 55.795 -10.094 1.00 135.69 ? 1014 NAG A C2 1 HETATM 13351 C C3 . NAG Q 4 . ? -56.745 56.330 -9.001 1.00 142.08 ? 1014 NAG A C3 1 HETATM 13352 C C4 . NAG Q 4 . ? -57.542 57.089 -7.947 1.00 153.50 ? 1014 NAG A C4 1 HETATM 13353 C C5 . NAG Q 4 . ? -58.707 56.237 -7.444 1.00 152.40 ? 1014 NAG A C5 1 HETATM 13354 C C6 . NAG Q 4 . ? -59.623 56.979 -6.499 1.00 153.63 ? 1014 NAG A C6 1 HETATM 13355 C C7 . NAG Q 4 . ? -56.979 55.158 -12.364 1.00 124.76 ? 1014 NAG A C7 1 HETATM 13356 C C8 . NAG Q 4 . ? -56.139 54.230 -13.188 1.00 123.46 ? 1014 NAG A C8 1 HETATM 13357 N N2 . NAG Q 4 . ? -56.918 54.983 -11.040 1.00 128.12 ? 1014 NAG A N2 1 HETATM 13358 O O3 . NAG Q 4 . ? -55.769 57.187 -9.584 1.00 137.41 ? 1014 NAG A O3 1 HETATM 13359 O O4 . NAG Q 4 . ? -56.697 57.408 -6.847 1.00 160.34 ? 1014 NAG A O4 1 HETATM 13360 O O5 . NAG Q 4 . ? -59.514 55.814 -8.552 1.00 148.12 ? 1014 NAG A O5 1 HETATM 13361 O O6 . NAG Q 4 . ? -60.988 56.694 -6.769 1.00 152.19 ? 1014 NAG A O6 1 HETATM 13362 O O7 . NAG Q 4 . ? -57.679 56.027 -12.873 1.00 124.59 ? 1014 NAG A O7 1 HETATM 13363 C C1 . BMA R 5 . ? -56.518 58.834 -6.741 1.00 158.46 ? 1015 BMA A C1 1 HETATM 13364 C C2 . BMA R 5 . ? -55.174 59.121 -6.059 1.00 158.09 ? 1015 BMA A C2 1 HETATM 13365 C C3 . BMA R 5 . ? -54.955 60.631 -5.949 1.00 162.30 ? 1015 BMA A C3 1 HETATM 13366 C C4 . BMA R 5 . ? -55.214 61.339 -7.293 1.00 166.55 ? 1015 BMA A C4 1 HETATM 13367 C C5 . BMA R 5 . ? -56.587 60.934 -7.864 1.00 158.94 ? 1015 BMA A C5 1 HETATM 13368 C C6 . BMA R 5 . ? -56.850 61.520 -9.240 1.00 156.22 ? 1015 BMA A C6 1 HETATM 13369 O O2 . BMA R 5 . ? -54.109 58.616 -6.845 1.00 159.85 ? 1015 BMA A O2 1 HETATM 13370 O O3 . BMA R 5 . ? -53.637 60.940 -5.492 1.00 170.27 ? 1015 BMA A O3 1 HETATM 13371 O O4 . BMA R 5 . ? -55.173 62.746 -7.113 1.00 178.23 ? 1015 BMA A O4 1 HETATM 13372 O O5 . BMA R 5 . ? -56.631 59.502 -7.977 1.00 157.95 ? 1015 BMA A O5 1 HETATM 13373 O O6 . BMA R 5 . ? -56.397 62.868 -9.247 1.00 157.51 ? 1015 BMA A O6 1 HETATM 13374 C C1 . MAN S 6 . ? -53.478 60.523 -4.123 1.00 172.94 ? 1016 MAN A C1 1 HETATM 13375 C C2 . MAN S 6 . ? -53.906 61.665 -3.185 1.00 174.29 ? 1016 MAN A C2 1 HETATM 13376 C C3 . MAN S 6 . ? -52.839 62.760 -3.171 1.00 176.50 ? 1016 MAN A C3 1 HETATM 13377 C C4 . MAN S 6 . ? -51.448 62.167 -2.894 1.00 172.36 ? 1016 MAN A C4 1 HETATM 13378 C C5 . MAN S 6 . ? -51.140 61.070 -3.923 1.00 166.53 ? 1016 MAN A C5 1 HETATM 13379 C C6 . MAN S 6 . ? -49.812 60.381 -3.669 1.00 163.17 ? 1016 MAN A C6 1 HETATM 13380 O O2 . MAN S 6 . ? -54.010 61.213 -1.832 1.00 170.51 ? 1016 MAN A O2 1 HETATM 13381 O O3 . MAN S 6 . ? -53.137 63.777 -2.219 1.00 179.72 ? 1016 MAN A O3 1 HETATM 13382 O O4 . MAN S 6 . ? -50.463 63.185 -2.981 1.00 174.02 ? 1016 MAN A O4 1 HETATM 13383 O O5 . MAN S 6 . ? -52.174 60.063 -3.859 1.00 169.88 ? 1016 MAN A O5 1 HETATM 13384 O O6 . MAN S 6 . ? -49.439 59.680 -4.851 1.00 161.85 ? 1016 MAN A O6 1 HETATM 13385 C C1 . NAG T 4 . ? -30.050 49.808 -17.347 1.00 124.07 ? 1017 NAG A C1 1 HETATM 13386 C C2 . NAG T 4 . ? -30.742 49.344 -18.629 1.00 141.29 ? 1017 NAG A C2 1 HETATM 13387 C C3 . NAG T 4 . ? -30.176 47.998 -19.077 1.00 146.12 ? 1017 NAG A C3 1 HETATM 13388 C C4 . NAG T 4 . ? -28.659 48.069 -19.189 1.00 141.50 ? 1017 NAG A C4 1 HETATM 13389 C C5 . NAG T 4 . ? -28.060 48.581 -17.883 1.00 138.50 ? 1017 NAG A C5 1 HETATM 13390 C C6 . NAG T 4 . ? -26.565 48.783 -17.956 1.00 144.09 ? 1017 NAG A C6 1 HETATM 13391 C C7 . NAG T 4 . ? -33.060 49.485 -19.427 1.00 146.12 ? 1017 NAG A C7 1 HETATM 13392 C C8 . NAG T 4 . ? -34.507 49.348 -19.059 1.00 142.81 ? 1017 NAG A C8 1 HETATM 13393 N N2 . NAG T 4 . ? -32.182 49.256 -18.445 1.00 146.89 ? 1017 NAG A N2 1 HETATM 13394 O O3 . NAG T 4 . ? -30.740 47.638 -20.333 1.00 152.68 ? 1017 NAG A O3 1 HETATM 13395 O O4 . NAG T 4 . ? -28.130 46.780 -19.476 1.00 137.83 ? 1017 NAG A O4 1 HETATM 13396 O O5 . NAG T 4 . ? -28.635 49.855 -17.554 1.00 131.89 ? 1017 NAG A O5 1 HETATM 13397 O O6 . NAG T 4 . ? -26.185 50.051 -17.439 1.00 149.44 ? 1017 NAG A O6 1 HETATM 13398 O O7 . NAG T 4 . ? -32.703 49.788 -20.561 1.00 144.49 ? 1017 NAG A O7 1 HETATM 13399 C C1 . NAG U 4 . ? -35.129 42.297 1.715 1.00 101.49 ? 1018 NAG A C1 1 HETATM 13400 C C2 . NAG U 4 . ? -34.051 41.234 1.518 1.00 120.48 ? 1018 NAG A C2 1 HETATM 13401 C C3 . NAG U 4 . ? -33.007 41.330 2.628 1.00 128.83 ? 1018 NAG A C3 1 HETATM 13402 C C4 . NAG U 4 . ? -33.663 41.156 3.992 1.00 126.40 ? 1018 NAG A C4 1 HETATM 13403 C C5 . NAG U 4 . ? -34.908 42.033 4.090 1.00 117.30 ? 1018 NAG A C5 1 HETATM 13404 C C6 . NAG U 4 . ? -34.941 42.878 5.342 1.00 113.08 ? 1018 NAG A C6 1 HETATM 13405 C C7 . NAG U 4 . ? -35.111 39.349 0.356 1.00 115.73 ? 1018 NAG A C7 1 HETATM 13406 C C8 . NAG U 4 . ? -35.677 37.968 0.495 1.00 122.23 ? 1018 NAG A C8 1 HETATM 13407 N N2 . NAG U 4 . ? -34.633 39.902 1.476 1.00 118.41 ? 1018 NAG A N2 1 HETATM 13408 O O3 . NAG U 4 . ? -32.355 42.593 2.559 1.00 126.64 ? 1018 NAG A O3 1 HETATM 13409 O O4 . NAG U 4 . ? -34.029 39.794 4.184 1.00 132.12 ? 1018 NAG A O4 1 HETATM 13410 O O5 . NAG U 4 . ? -34.948 42.941 2.978 1.00 113.56 ? 1018 NAG A O5 1 HETATM 13411 O O6 . NAG U 4 . ? -34.631 44.236 5.060 1.00 103.50 ? 1018 NAG A O6 1 HETATM 13412 O O7 . NAG U 4 . ? -35.087 39.938 -0.721 1.00 105.76 ? 1018 NAG A O7 1 HETATM 13413 C C1 . NAG V 4 . ? -33.439 39.296 5.402 1.00 133.78 ? 1019 NAG A C1 1 HETATM 13414 C C2 . NAG V 4 . ? -31.963 38.971 5.177 1.00 134.63 ? 1019 NAG A C2 1 HETATM 13415 C C3 . NAG V 4 . ? -31.341 38.423 6.459 1.00 135.72 ? 1019 NAG A C3 1 HETATM 13416 C C4 . NAG V 4 . ? -31.599 39.369 7.625 1.00 132.96 ? 1019 NAG A C4 1 HETATM 13417 C C5 . NAG V 4 . ? -33.090 39.676 7.735 1.00 132.72 ? 1019 NAG A C5 1 HETATM 13418 C C6 . NAG V 4 . ? -33.407 40.702 8.798 1.00 129.38 ? 1019 NAG A C6 1 HETATM 13419 C C7 . NAG V 4 . ? -30.972 38.235 3.054 1.00 132.01 ? 1019 NAG A C7 1 HETATM 13420 C C8 . NAG V 4 . ? -30.928 37.154 2.017 1.00 130.15 ? 1019 NAG A C8 1 HETATM 13421 N N2 . NAG V 4 . ? -31.798 38.026 4.084 1.00 133.64 ? 1019 NAG A N2 1 HETATM 13422 O O3 . NAG V 4 . ? -29.941 38.254 6.271 1.00 138.17 ? 1019 NAG A O3 1 HETATM 13423 O O4 . NAG V 4 . ? -31.152 38.777 8.839 1.00 131.46 ? 1019 NAG A O4 1 HETATM 13424 O O5 . NAG V 4 . ? -33.568 40.208 6.491 1.00 132.52 ? 1019 NAG A O5 1 HETATM 13425 O O6 . NAG V 4 . ? -34.790 40.702 9.125 1.00 123.28 ? 1019 NAG A O6 1 HETATM 13426 O O7 . NAG V 4 . ? -30.289 39.251 2.964 1.00 133.41 ? 1019 NAG A O7 1 HETATM 13427 C C1 . NAG W 4 . ? -42.018 58.668 14.135 1.00 136.23 ? 1020 NAG A C1 1 HETATM 13428 C C2 . NAG W 4 . ? -41.960 58.237 12.667 1.00 151.62 ? 1020 NAG A C2 1 HETATM 13429 C C3 . NAG W 4 . ? -42.875 59.118 11.827 1.00 150.91 ? 1020 NAG A C3 1 HETATM 13430 C C4 . NAG W 4 . ? -44.315 58.967 12.294 1.00 151.62 ? 1020 NAG A C4 1 HETATM 13431 C C5 . NAG W 4 . ? -44.416 59.228 13.796 1.00 157.32 ? 1020 NAG A C5 1 HETATM 13432 C C6 . NAG W 4 . ? -44.920 58.040 14.585 1.00 158.58 ? 1020 NAG A C6 1 HETATM 13433 C C7 . NAG W 4 . ? -40.105 57.412 11.284 1.00 153.42 ? 1020 NAG A C7 1 HETATM 13434 C C8 . NAG W 4 . ? -38.678 57.621 10.874 1.00 144.49 ? 1020 NAG A C8 1 HETATM 13435 N N2 . NAG W 4 . ? -40.597 58.291 12.163 1.00 158.33 ? 1020 NAG A N2 1 HETATM 13436 O O3 . NAG W 4 . ? -42.767 58.750 10.456 1.00 148.29 ? 1020 NAG A O3 1 HETATM 13437 O O4 . NAG W 4 . ? -45.148 59.890 11.603 1.00 142.82 ? 1020 NAG A O4 1 HETATM 13438 O O5 . NAG W 4 . ? -43.136 59.605 14.338 1.00 153.14 ? 1020 NAG A O5 1 HETATM 13439 O O6 . NAG W 4 . ? -45.658 58.451 15.728 1.00 158.73 ? 1020 NAG A O6 1 HETATM 13440 O O7 . NAG W 4 . ? -40.781 56.490 10.839 1.00 154.23 ? 1020 NAG A O7 1 HETATM 13441 C C1 . NAG X 4 . ? -24.037 54.080 62.942 1.00 92.73 ? 1021 NAG A C1 1 HETATM 13442 C C2 . NAG X 4 . ? -24.916 54.339 61.720 1.00 99.69 ? 1021 NAG A C2 1 HETATM 13443 C C3 . NAG X 4 . ? -24.194 55.253 60.733 1.00 108.24 ? 1021 NAG A C3 1 HETATM 13444 C C4 . NAG X 4 . ? -23.735 56.527 61.429 1.00 115.93 ? 1021 NAG A C4 1 HETATM 13445 C C5 . NAG X 4 . ? -22.898 56.179 62.657 1.00 117.10 ? 1021 NAG A C5 1 HETATM 13446 C C6 . NAG X 4 . ? -22.500 57.393 63.464 1.00 111.19 ? 1021 NAG A C6 1 HETATM 13447 C C7 . NAG X 4 . ? -26.515 52.553 61.192 1.00 108.54 ? 1021 NAG A C7 1 HETATM 13448 C C8 . NAG X 4 . ? -26.734 51.263 60.461 1.00 109.87 ? 1021 NAG A C8 1 HETATM 13449 N N2 . NAG X 4 . ? -25.297 53.092 61.076 1.00 107.22 ? 1021 NAG A N2 1 HETATM 13450 O O3 . NAG X 4 . ? -25.069 55.574 59.657 1.00 107.44 ? 1021 NAG A O3 1 HETATM 13451 O O4 . NAG X 4 . ? -22.957 57.318 60.538 1.00 120.60 ? 1021 NAG A O4 1 HETATM 13452 O O5 . NAG X 4 . ? -23.653 55.328 63.533 1.00 116.46 ? 1021 NAG A O5 1 HETATM 13453 O O6 . NAG X 4 . ? -22.081 57.034 64.774 1.00 105.66 ? 1021 NAG A O6 1 HETATM 13454 O O7 . NAG X 4 . ? -27.399 53.082 61.858 1.00 105.85 ? 1021 NAG A O7 1 HETATM 13455 C C1 . NAG Y 4 . ? -40.643 32.475 62.177 1.00 97.73 ? 1022 NAG A C1 1 HETATM 13456 C C2 . NAG Y 4 . ? -41.991 32.415 61.457 1.00 115.46 ? 1022 NAG A C2 1 HETATM 13457 C C3 . NAG Y 4 . ? -41.892 31.533 60.214 1.00 119.93 ? 1022 NAG A C3 1 HETATM 13458 C C4 . NAG Y 4 . ? -41.426 30.131 60.589 1.00 121.08 ? 1022 NAG A C4 1 HETATM 13459 C C5 . NAG Y 4 . ? -40.230 30.207 61.534 1.00 118.04 ? 1022 NAG A C5 1 HETATM 13460 C C6 . NAG Y 4 . ? -39.077 29.333 61.101 1.00 130.44 ? 1022 NAG A C6 1 HETATM 13461 C C7 . NAG Y 4 . ? -43.663 32.720 63.229 1.00 116.36 ? 1022 NAG A C7 1 HETATM 13462 C C8 . NAG Y 4 . ? -44.719 32.059 64.063 1.00 117.80 ? 1022 NAG A C8 1 HETATM 13463 N N2 . NAG Y 4 . ? -43.039 31.935 62.344 1.00 122.28 ? 1022 NAG A N2 1 HETATM 13464 O O3 . NAG Y 4 . ? -40.982 32.117 59.288 1.00 122.46 ? 1022 NAG A O3 1 HETATM 13465 O O4 . NAG Y 4 . ? -42.481 29.415 61.221 1.00 133.81 ? 1022 NAG A O4 1 HETATM 13466 O O5 . NAG Y 4 . ? -39.736 31.553 61.576 1.00 108.16 ? 1022 NAG A O5 1 HETATM 13467 O O6 . NAG Y 4 . ? -38.208 29.047 62.188 1.00 136.64 ? 1022 NAG A O6 1 HETATM 13468 O O7 . NAG Y 4 . ? -43.388 33.910 63.351 1.00 103.04 ? 1022 NAG A O7 1 HETATM 13469 C C1 . NAG Z 4 . ? -42.594 28.118 60.598 1.00 147.22 ? 1023 NAG A C1 1 HETATM 13470 C C2 . NAG Z 4 . ? -42.177 27.007 61.568 1.00 149.36 ? 1023 NAG A C2 1 HETATM 13471 C C3 . NAG Z 4 . ? -43.408 26.324 62.159 1.00 154.46 ? 1023 NAG A C3 1 HETATM 13472 C C4 . NAG Z 4 . ? -44.544 27.323 62.326 1.00 159.79 ? 1023 NAG A C4 1 HETATM 13473 C C5 . NAG Z 4 . ? -44.995 27.829 60.959 1.00 157.78 ? 1023 NAG A C5 1 HETATM 13474 C C6 . NAG Z 4 . ? -45.532 29.242 60.986 1.00 148.25 ? 1023 NAG A C6 1 HETATM 13475 C C7 . NAG Z 4 . ? -40.177 25.581 61.431 1.00 143.60 ? 1023 NAG A C7 1 HETATM 13476 C C8 . NAG Z 4 . ? -39.801 26.135 62.774 1.00 141.42 ? 1023 NAG A C8 1 HETATM 13477 N N2 . NAG Z 4 . ? -41.321 26.034 60.907 1.00 141.73 ? 1023 NAG A N2 1 HETATM 13478 O O3 . NAG Z 4 . ? -43.072 25.755 63.420 1.00 145.35 ? 1023 NAG A O3 1 HETATM 13479 O O4 . NAG Z 4 . ? -45.644 26.705 62.984 1.00 155.89 ? 1023 NAG A O4 1 HETATM 13480 O O5 . NAG Z 4 . ? -43.897 27.810 60.031 1.00 154.51 ? 1023 NAG A O5 1 HETATM 13481 O O6 . NAG Z 4 . ? -46.288 29.533 59.819 1.00 145.05 ? 1023 NAG A O6 1 HETATM 13482 O O7 . NAG Z 4 . ? -39.476 24.760 60.848 1.00 150.63 ? 1023 NAG A O7 1 HETATM 13483 C C1 . NAG AA 4 . ? -28.996 21.770 75.896 1.00 64.66 ? 1024 NAG A C1 1 HETATM 13484 C C2 . NAG AA 4 . ? -29.024 21.197 74.476 1.00 79.03 ? 1024 NAG A C2 1 HETATM 13485 C C3 . NAG AA 4 . ? -30.428 21.312 73.882 1.00 80.77 ? 1024 NAG A C3 1 HETATM 13486 C C4 . NAG AA 4 . ? -31.457 20.694 74.819 1.00 91.22 ? 1024 NAG A C4 1 HETATM 13487 C C5 . NAG AA 4 . ? -31.334 21.330 76.198 1.00 87.28 ? 1024 NAG A C5 1 HETATM 13488 C C6 . NAG AA 4 . ? -32.273 20.729 77.218 1.00 97.01 ? 1024 NAG A C6 1 HETATM 13489 C C7 . NAG AA 4 . ? -27.210 21.214 72.823 1.00 91.64 ? 1024 NAG A C7 1 HETATM 13490 C C8 . NAG AA 4 . ? -26.278 22.067 72.016 1.00 92.17 ? 1024 NAG A C8 1 HETATM 13491 N N2 . NAG AA 4 . ? -28.055 21.868 73.627 1.00 88.22 ? 1024 NAG A N2 1 HETATM 13492 O O3 . NAG AA 4 . ? -30.459 20.659 72.617 1.00 79.40 ? 1024 NAG A O3 1 HETATM 13493 O O4 . NAG AA 4 . ? -32.772 20.908 74.320 1.00 108.31 ? 1024 NAG A O4 1 HETATM 13494 O O5 . NAG AA 4 . ? -30.002 21.138 76.693 1.00 76.51 ? 1024 NAG A O5 1 HETATM 13495 O O6 . NAG AA 4 . ? -32.191 19.310 77.231 1.00 106.22 ? 1024 NAG A O6 1 HETATM 13496 O O7 . NAG AA 4 . ? -27.199 19.989 72.749 1.00 89.94 ? 1024 NAG A O7 1 HETATM 13497 C C1 . NAG BA 4 . ? -33.286 19.687 73.756 1.00 129.60 ? 1025 NAG A C1 1 HETATM 13498 C C2 . NAG BA 4 . ? -34.547 19.268 74.521 1.00 148.77 ? 1025 NAG A C2 1 HETATM 13499 C C3 . NAG BA 4 . ? -35.803 19.706 73.766 1.00 155.31 ? 1025 NAG A C3 1 HETATM 13500 C C4 . NAG BA 4 . ? -35.871 19.052 72.390 1.00 164.54 ? 1025 NAG A C4 1 HETATM 13501 C C5 . NAG BA 4 . ? -34.469 18.852 71.824 1.00 152.11 ? 1025 NAG A C5 1 HETATM 13502 C C6 . NAG BA 4 . ? -34.410 18.984 70.320 1.00 149.84 ? 1025 NAG A C6 1 HETATM 13503 C C7 . NAG BA 4 . ? -34.735 17.308 75.991 1.00 145.54 ? 1025 NAG A C7 1 HETATM 13504 C C8 . NAG BA 4 . ? -34.730 15.811 76.065 1.00 143.16 ? 1025 NAG A C8 1 HETATM 13505 N N2 . NAG BA 4 . ? -34.568 17.835 74.773 1.00 151.37 ? 1025 NAG A N2 1 HETATM 13506 O O3 . NAG BA 4 . ? -35.803 21.123 73.631 1.00 142.64 ? 1025 NAG A O3 1 HETATM 13507 O O4 . NAG BA 4 . ? -36.550 17.802 72.459 1.00 177.69 ? 1025 NAG A O4 1 HETATM 13508 O O5 . NAG BA 4 . ? -33.594 19.854 72.362 1.00 137.74 ? 1025 NAG A O5 1 HETATM 13509 O O6 . NAG BA 4 . ? -33.070 18.965 69.848 1.00 142.76 ? 1025 NAG A O6 1 HETATM 13510 O O7 . NAG BA 4 . ? -34.885 18.008 76.988 1.00 142.48 ? 1025 NAG A O7 1 HETATM 13511 C C1 . BMA CA 5 . ? -37.927 18.025 72.828 1.00 186.09 ? 1026 BMA A C1 1 HETATM 13512 C C2 . BMA CA 5 . ? -38.869 17.925 71.572 1.00 180.55 ? 1026 BMA A C2 1 HETATM 13513 C C3 . BMA CA 5 . ? -39.385 16.488 71.315 1.00 181.30 ? 1026 BMA A C3 1 HETATM 13514 C C4 . BMA CA 5 . ? -39.407 15.621 72.583 1.00 187.76 ? 1026 BMA A C4 1 HETATM 13515 C C5 . BMA CA 5 . ? -39.556 16.517 73.804 1.00 188.21 ? 1026 BMA A C5 1 HETATM 13516 C C6 . BMA CA 5 . ? -39.809 15.737 75.080 1.00 181.59 ? 1026 BMA A C6 1 HETATM 13517 O O2 . BMA CA 5 . ? -38.203 18.335 70.384 1.00 176.41 ? 1026 BMA A O2 1 HETATM 13518 O O3 . BMA CA 5 . ? -38.650 15.840 70.280 1.00 175.36 ? 1026 BMA A O3 1 HETATM 13519 O O4 . BMA CA 5 . ? -40.488 14.703 72.528 1.00 190.09 ? 1026 BMA A O4 1 HETATM 13520 O O5 . BMA CA 5 . ? -38.317 17.219 73.948 1.00 190.84 ? 1026 BMA A O5 1 HETATM 13521 O O6 . BMA CA 5 . ? -40.304 16.638 76.062 1.00 175.96 ? 1026 BMA A O6 1 HETATM 13522 MN MN . MN DA 7 . ? -6.073 67.712 31.809 1.00 89.13 ? 1027 MN A MN 1 HETATM 13523 MN MN . MN EA 7 . ? -16.747 59.517 26.120 1.00 90.54 ? 1028 MN A MN 1 HETATM 13524 MN MN . MN FA 7 . ? -18.880 56.334 13.478 1.00 177.82 ? 1029 MN A MN 1 HETATM 13525 MN MN . MN GA 7 . ? -10.438 59.293 3.226 1.00 137.51 ? 1030 MN A MN 1 HETATM 13526 MN MN . MN HA 7 . ? -68.997 46.779 4.952 1.00 84.84 ? 1031 MN A MN 1 HETATM 13527 C C1 . NAG IA 4 . ? -26.733 4.533 29.270 1.00 99.63 ? 701 NAG B C1 1 HETATM 13528 C C2 . NAG IA 4 . ? -26.180 3.108 29.330 1.00 112.61 ? 701 NAG B C2 1 HETATM 13529 C C3 . NAG IA 4 . ? -26.799 2.352 30.495 1.00 122.65 ? 701 NAG B C3 1 HETATM 13530 C C4 . NAG IA 4 . ? -26.427 3.028 31.807 1.00 127.34 ? 701 NAG B C4 1 HETATM 13531 C C5 . NAG IA 4 . ? -26.778 4.514 31.757 1.00 128.48 ? 701 NAG B C5 1 HETATM 13532 C C6 . NAG IA 4 . ? -25.579 5.426 31.898 1.00 129.60 ? 701 NAG B C6 1 HETATM 13533 C C7 . NAG IA 4 . ? -25.443 1.847 27.357 1.00 136.34 ? 701 NAG B C7 1 HETATM 13534 C C8 . NAG IA 4 . ? -25.869 1.162 26.093 1.00 130.92 ? 701 NAG B C8 1 HETATM 13535 N N2 . NAG IA 4 . ? -26.420 2.403 28.079 1.00 124.64 ? 701 NAG B N2 1 HETATM 13536 O O3 . NAG IA 4 . ? -26.332 1.009 30.491 1.00 129.03 ? 701 NAG B O3 1 HETATM 13537 O O4 . NAG IA 4 . ? -27.129 2.417 32.884 1.00 121.08 ? 701 NAG B O4 1 HETATM 13538 O O5 . NAG IA 4 . ? -27.442 4.845 30.524 1.00 118.87 ? 701 NAG B O5 1 HETATM 13539 O O6 . NAG IA 4 . ? -24.950 5.269 33.162 1.00 127.71 ? 701 NAG B O6 1 HETATM 13540 O O7 . NAG IA 4 . ? -24.267 1.893 27.707 1.00 146.56 ? 701 NAG B O7 1 HETATM 13541 C C1 . NAG JA 4 . ? -2.406 35.976 45.133 1.00 80.74 ? 702 NAG B C1 1 HETATM 13542 C C2 . NAG JA 4 . ? -2.002 37.403 45.526 1.00 93.09 ? 702 NAG B C2 1 HETATM 13543 C C3 . NAG JA 4 . ? -2.909 37.926 46.640 1.00 99.23 ? 702 NAG B C3 1 HETATM 13544 C C4 . NAG JA 4 . ? -4.372 37.790 46.245 1.00 102.54 ? 702 NAG B C4 1 HETATM 13545 C C5 . NAG JA 4 . ? -4.668 36.342 45.874 1.00 97.99 ? 702 NAG B C5 1 HETATM 13546 C C6 . NAG JA 4 . ? -6.084 36.131 45.387 1.00 104.52 ? 702 NAG B C6 1 HETATM 13547 C C7 . NAG JA 4 . ? 0.423 37.308 45.092 1.00 94.03 ? 702 NAG B C7 1 HETATM 13548 C C8 . NAG JA 4 . ? 1.789 37.432 45.696 1.00 104.04 ? 702 NAG B C8 1 HETATM 13549 N N2 . NAG JA 4 . ? -0.607 37.476 45.930 1.00 93.65 ? 702 NAG B N2 1 HETATM 13550 O O3 . NAG JA 4 . ? -2.600 39.290 46.903 1.00 95.48 ? 702 NAG B O3 1 HETATM 13551 O O4 . NAG JA 4 . ? -5.212 38.185 47.323 1.00 114.77 ? 702 NAG B O4 1 HETATM 13552 O O5 . NAG JA 4 . ? -3.800 35.938 44.806 1.00 92.86 ? 702 NAG B O5 1 HETATM 13553 O O6 . NAG JA 4 . ? -6.138 35.156 44.355 1.00 106.66 ? 702 NAG B O6 1 HETATM 13554 O O7 . NAG JA 4 . ? 0.260 37.056 43.901 1.00 82.34 ? 702 NAG B O7 1 HETATM 13555 C C1 . NAG KA 4 . ? -26.249 11.041 34.350 1.00 91.87 ? 703 NAG B C1 1 HETATM 13556 C C2 . NAG KA 4 . ? -26.342 10.117 33.130 1.00 110.91 ? 703 NAG B C2 1 HETATM 13557 C C3 . NAG KA 4 . ? -27.742 10.155 32.527 1.00 130.57 ? 703 NAG B C3 1 HETATM 13558 C C4 . NAG KA 4 . ? -28.766 9.800 33.592 1.00 134.37 ? 703 NAG B C4 1 HETATM 13559 C C5 . NAG KA 4 . ? -28.659 10.813 34.725 1.00 117.85 ? 703 NAG B C5 1 HETATM 13560 C C6 . NAG KA 4 . ? -29.610 10.537 35.867 1.00 118.73 ? 703 NAG B C6 1 HETATM 13561 C C7 . NAG KA 4 . ? -24.420 9.605 31.698 1.00 112.92 ? 703 NAG B C7 1 HETATM 13562 C C8 . NAG KA 4 . ? -23.466 10.131 30.669 1.00 117.57 ? 703 NAG B C8 1 HETATM 13563 N N2 . NAG KA 4 . ? -25.346 10.466 32.132 1.00 108.87 ? 703 NAG B N2 1 HETATM 13564 O O3 . NAG KA 4 . ? -27.814 9.226 31.451 1.00 137.84 ? 703 NAG B O3 1 HETATM 13565 O O4 . NAG KA 4 . ? -30.081 9.695 33.051 1.00 142.08 ? 703 NAG B O4 1 HETATM 13566 O O5 . NAG KA 4 . ? -27.333 10.754 35.274 1.00 105.34 ? 703 NAG B O5 1 HETATM 13567 O O6 . NAG KA 4 . ? -30.695 11.455 35.870 1.00 117.82 ? 703 NAG B O6 1 HETATM 13568 O O7 . NAG KA 4 . ? -24.356 8.454 32.117 1.00 107.78 ? 703 NAG B O7 1 HETATM 13569 C C1 . NAG LA 4 . ? -30.667 10.923 32.581 1.00 143.71 ? 704 NAG B C1 1 HETATM 13570 C C2 . NAG LA 4 . ? -31.157 10.710 31.155 1.00 155.22 ? 704 NAG B C2 1 HETATM 13571 C C3 . NAG LA 4 . ? -31.728 12.010 30.587 1.00 159.39 ? 704 NAG B C3 1 HETATM 13572 C C4 . NAG LA 4 . ? -32.160 12.973 31.690 1.00 150.78 ? 704 NAG B C4 1 HETATM 13573 C C5 . NAG LA 4 . ? -32.699 12.249 32.929 1.00 144.53 ? 704 NAG B C5 1 HETATM 13574 C C6 . NAG LA 4 . ? -34.029 11.559 32.708 1.00 141.85 ? 704 NAG B C6 1 HETATM 13575 C C7 . NAG LA 4 . ? -30.200 9.089 29.572 1.00 148.30 ? 704 NAG B C7 1 HETATM 13576 C C8 . NAG LA 4 . ? -31.505 8.358 29.673 1.00 143.79 ? 704 NAG B C8 1 HETATM 13577 N N2 . NAG LA 4 . ? -30.092 10.205 30.304 1.00 156.97 ? 704 NAG B N2 1 HETATM 13578 O O3 . NAG LA 4 . ? -32.831 11.711 29.738 1.00 165.26 ? 704 NAG B O3 1 HETATM 13579 O O4 . NAG LA 4 . ? -31.100 13.855 32.047 1.00 144.43 ? 704 NAG B O4 1 HETATM 13580 O O5 . NAG LA 4 . ? -31.776 11.263 33.427 1.00 140.57 ? 704 NAG B O5 1 HETATM 13581 O O6 . NAG LA 4 . ? -34.605 11.128 33.933 1.00 141.96 ? 704 NAG B O6 1 HETATM 13582 O O7 . NAG LA 4 . ? -29.283 8.688 28.863 1.00 141.23 ? 704 NAG B O7 1 HETATM 13583 C C1 . NAG MA 4 . ? -33.190 30.654 31.644 1.00 61.36 ? 705 NAG B C1 1 HETATM 13584 C C2 . NAG MA 4 . ? -32.861 31.033 33.082 1.00 81.15 ? 705 NAG B C2 1 HETATM 13585 C C3 . NAG MA 4 . ? -33.997 30.613 34.009 1.00 89.41 ? 705 NAG B C3 1 HETATM 13586 C C4 . NAG MA 4 . ? -35.330 31.162 33.513 1.00 84.05 ? 705 NAG B C4 1 HETATM 13587 C C5 . NAG MA 4 . ? -35.538 30.816 32.039 1.00 78.22 ? 705 NAG B C5 1 HETATM 13588 C C6 . NAG MA 4 . ? -36.764 31.469 31.444 1.00 87.80 ? 705 NAG B C6 1 HETATM 13589 C C7 . NAG MA 4 . ? -30.443 31.095 33.501 1.00 87.32 ? 705 NAG B C7 1 HETATM 13590 C C8 . NAG MA 4 . ? -29.247 30.322 33.970 1.00 93.78 ? 705 NAG B C8 1 HETATM 13591 N N2 . NAG MA 4 . ? -31.606 30.434 33.505 1.00 80.32 ? 705 NAG B N2 1 HETATM 13592 O O3 . NAG MA 4 . ? -33.734 31.091 35.323 1.00 93.96 ? 705 NAG B O3 1 HETATM 13593 O O4 . NAG MA 4 . ? -36.386 30.584 34.271 1.00 92.96 ? 705 NAG B O4 1 HETATM 13594 O O5 . NAG MA 4 . ? -34.416 31.261 31.261 1.00 65.23 ? 705 NAG B O5 1 HETATM 13595 O O6 . NAG MA 4 . ? -36.413 32.512 30.545 1.00 92.47 ? 705 NAG B O6 1 HETATM 13596 O O7 . NAG MA 4 . ? -30.360 32.263 33.137 1.00 88.40 ? 705 NAG B O7 1 HETATM 13597 C C1 . NAG NA 4 . ? -37.096 31.581 35.039 1.00 93.39 ? 706 NAG B C1 1 HETATM 13598 C C2 . NAG NA 4 . ? -38.589 31.245 35.050 1.00 99.48 ? 706 NAG B C2 1 HETATM 13599 C C3 . NAG NA 4 . ? -39.154 31.387 36.457 1.00 104.88 ? 706 NAG B C3 1 HETATM 13600 C C4 . NAG NA 4 . ? -38.403 30.463 37.405 1.00 110.73 ? 706 NAG B C4 1 HETATM 13601 C C5 . NAG NA 4 . ? -36.911 30.791 37.389 1.00 112.77 ? 706 NAG B C5 1 HETATM 13602 C C6 . NAG NA 4 . ? -36.039 29.597 37.070 1.00 120.27 ? 706 NAG B C6 1 HETATM 13603 C C7 . NAG NA 4 . ? -39.922 31.591 33.022 1.00 108.39 ? 706 NAG B C7 1 HETATM 13604 C C8 . NAG NA 4 . ? -40.638 32.590 32.163 1.00 120.38 ? 706 NAG B C8 1 HETATM 13605 N N2 . NAG NA 4 . ? -39.324 32.078 34.114 1.00 105.52 ? 706 NAG B N2 1 HETATM 13606 O O3 . NAG NA 4 . ? -40.537 31.052 36.437 1.00 112.88 ? 706 NAG B O3 1 HETATM 13607 O O4 . NAG NA 4 . ? -38.908 30.526 38.737 1.00 109.59 ? 706 NAG B O4 1 HETATM 13608 O O5 . NAG NA 4 . ? -36.624 31.813 36.416 1.00 98.44 ? 706 NAG B O5 1 HETATM 13609 O O6 . NAG NA 4 . ? -34.731 29.745 37.604 1.00 118.99 ? 706 NAG B O6 1 HETATM 13610 O O7 . NAG NA 4 . ? -39.886 30.398 32.739 1.00 99.28 ? 706 NAG B O7 1 HETATM 13611 C C1 . BMA OA 5 . ? -39.270 31.850 39.184 1.00 100.96 ? 707 BMA B C1 1 HETATM 13612 C C2 . BMA OA 5 . ? -40.725 31.803 39.728 1.00 116.29 ? 707 BMA B C2 1 HETATM 13613 C C3 . BMA OA 5 . ? -40.785 31.091 41.096 1.00 117.01 ? 707 BMA B C3 1 HETATM 13614 C C4 . BMA OA 5 . ? -39.444 31.156 41.843 1.00 112.03 ? 707 BMA B C4 1 HETATM 13615 C C5 . BMA OA 5 . ? -38.746 32.474 41.491 1.00 114.35 ? 707 BMA B C5 1 HETATM 13616 C C6 . BMA OA 5 . ? -37.528 32.756 42.353 1.00 115.04 ? 707 BMA B C6 1 HETATM 13617 O O2 . BMA OA 5 . ? -41.565 31.068 38.852 1.00 109.44 ? 707 BMA B O2 1 HETATM 13618 O O3 . BMA OA 5 . ? -41.220 29.740 40.971 1.00 113.33 ? 707 BMA B O3 1 HETATM 13619 O O4 . BMA OA 5 . ? -39.657 31.078 43.245 1.00 103.66 ? 707 BMA B O4 1 HETATM 13620 O O5 . BMA OA 5 . ? -38.323 32.412 40.103 1.00 107.76 ? 707 BMA B O5 1 HETATM 13621 O O6 . BMA OA 5 . ? -37.949 32.841 43.709 1.00 103.97 ? 707 BMA B O6 1 HETATM 13622 MN MN . MN PA 7 . ? 18.076 35.891 39.845 1.00 48.33 ? 708 MN B MN 1 HETATM 13623 MN MN . MN QA 7 . ? 18.321 33.878 46.892 1.00 88.63 ? 709 MN B MN 1 HETATM 13624 MN MN . MN RA 7 . ? 16.896 38.282 34.764 1.00 56.09 ? 710 MN B MN 1 HETATM 13625 O O . HOH SA 8 . ? 16.747 37.311 40.863 1.00 39.37 ? 801 HOH B O 1 HETATM 13626 O O . HOH SA 8 . ? 16.604 34.500 40.676 1.00 60.09 ? 802 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . PHE A 1 ? 0.9361 0.8766 0.8656 -0.3294 -0.3972 0.2209 1 PHE A N 2 C CA . PHE A 1 ? 1.0807 1.0343 0.9879 -0.3609 -0.4255 0.2172 1 PHE A CA 3 C C . PHE A 1 ? 1.1102 1.0574 0.9538 -0.3836 -0.4510 0.2288 1 PHE A C 4 O O . PHE A 1 ? 1.0726 1.0257 0.8761 -0.4136 -0.4725 0.2204 1 PHE A O 5 C CB . PHE A 1 ? 1.0759 1.0647 1.0534 -0.3592 -0.4501 0.2380 1 PHE A CB 6 C CG . PHE A 1 ? 0.9978 1.0039 1.0155 -0.3441 -0.4729 0.2757 1 PHE A CG 7 C CD1 . PHE A 1 ? 1.0215 1.0416 1.0241 -0.3648 -0.5147 0.2992 1 PHE A CD1 8 C CD2 . PHE A 1 ? 1.0340 1.0424 1.1055 -0.3092 -0.4533 0.2871 1 PHE A CD2 9 C CE1 . PHE A 1 ? 1.0283 1.0634 1.0743 -0.3498 -0.5374 0.3360 1 PHE A CE1 10 C CE2 . PHE A 1 ? 1.0920 1.1139 1.2062 -0.2932 -0.4737 0.3198 1 PHE A CE2 11 C CZ . PHE A 1 ? 1.0833 1.1183 1.1877 -0.3129 -0.5163 0.3456 1 PHE A CZ 12 N N . ASN A 2 ? 1.1512 1.0858 0.9847 -0.3701 -0.4488 0.2481 2 ASN A N 13 C CA . ASN A 2 ? 1.2888 1.2197 1.0684 -0.3903 -0.4745 0.2679 2 ASN A CA 14 C C . ASN A 2 ? 1.2458 1.1519 0.9455 -0.4053 -0.4542 0.2472 2 ASN A C 15 O O . ASN A 2 ? 1.2838 1.1863 0.9342 -0.4222 -0.4709 0.2648 2 ASN A O 16 C CB . ASN A 2 ? 1.3220 1.2535 1.1416 -0.3692 -0.4891 0.3063 2 ASN A CB 17 C CG . ASN A 2 ? 1.2413 1.1568 1.1036 -0.3337 -0.4558 0.3004 2 ASN A CG 18 O OD1 . ASN A 2 ? 1.1784 1.0973 1.0730 -0.3191 -0.4304 0.2785 2 ASN A OD1 19 N ND2 . ASN A 2 ? 1.2067 1.1042 1.0686 -0.3207 -0.4570 0.3205 2 ASN A ND2 20 N N . LEU A 3 ? 1.0987 0.9898 0.7880 -0.3991 -0.4182 0.2123 3 LEU A N 21 C CA . LEU A 3 ? 1.0969 0.9691 0.7163 -0.4131 -0.3967 0.1899 3 LEU A CA 22 C C . LEU A 3 ? 1.1519 1.0322 0.7104 -0.4482 -0.4114 0.1718 3 LEU A C 23 O O . LEU A 3 ? 1.2932 1.1843 0.8674 -0.4577 -0.4214 0.1563 3 LEU A O 24 C CB . LEU A 3 ? 1.0500 0.9055 0.6828 -0.3950 -0.3555 0.1590 3 LEU A CB 25 C CG . LEU A 3 ? 1.0042 0.8481 0.6795 -0.3631 -0.3369 0.1715 3 LEU A CG 26 C CD1 . LEU A 3 ? 0.9636 0.7939 0.6472 -0.3489 -0.2993 0.1416 3 LEU A CD1 27 C CD2 . LEU A 3 ? 1.0276 0.8590 0.6718 -0.3648 -0.3422 0.1940 3 LEU A CD2 28 N N . ASP A 4 ? 1.1978 1.0731 0.6875 -0.4675 -0.4111 0.1734 4 ASP A N 29 C CA . ASP A 4 ? 1.2549 1.1382 0.6948 -0.4899 -0.4089 0.1553 4 ASP A CA 30 C C . ASP A 4 ? 1.3159 1.1869 0.7196 -0.4939 -0.3722 0.1092 4 ASP A C 31 O O . ASP A 4 ? 1.2553 1.1159 0.6265 -0.4930 -0.3480 0.1023 4 ASP A O 32 C CB . ASP A 4 ? 1.3578 1.2471 0.7557 -0.5038 -0.4205 0.1837 4 ASP A CB 33 C CG . ASP A 4 ? 1.5338 1.4329 0.8732 -0.5277 -0.4150 0.1630 4 ASP A CG 34 O OD1 . ASP A 4 ? 1.5187 1.4115 0.8120 -0.5341 -0.3854 0.1383 4 ASP A OD1 35 O OD2 . ASP A 4 ? 1.7423 1.6569 1.0833 -0.5397 -0.4405 0.1711 4 ASP A OD2 36 N N . VAL A 5 ? 1.4436 1.3164 0.8583 -0.4974 -0.3682 0.0784 5 VAL A N 37 C CA . VAL A 5 ? 1.4284 1.2883 0.8230 -0.4969 -0.3341 0.0333 5 VAL A CA 38 C C . VAL A 5 ? 1.4286 1.2951 0.7657 -0.5157 -0.3262 0.0084 5 VAL A C 39 O O . VAL A 5 ? 1.4440 1.3016 0.7631 -0.5148 -0.2973 -0.0299 5 VAL A O 40 C CB . VAL A 5 ? 1.3647 1.2182 0.8136 -0.4868 -0.3308 0.0112 5 VAL A CB 41 C CG1 . VAL A 5 ? 1.3748 1.2090 0.8254 -0.4758 -0.2934 -0.0235 5 VAL A CG1 42 C CG2 . VAL A 5 ? 1.2939 1.1531 0.8059 -0.4740 -0.3519 0.0427 5 VAL A CG2 43 N N . ASP A 6 ? 1.5162 1.3991 0.8269 -0.5322 -0.3517 0.0297 6 ASP A N 44 C CA . ASP A 6 ? 1.7336 1.6249 0.9895 -0.5513 -0.3468 0.0053 6 ASP A CA 45 C C . ASP A 6 ? 1.7131 1.6066 0.9143 -0.5583 -0.3218 0.0026 6 ASP A C 46 O O . ASP A 6 ? 1.8514 1.7462 1.0148 -0.5657 -0.2990 -0.0330 6 ASP A O 47 C CB . ASP A 6 ? 1.9509 1.8606 1.1985 -0.5682 -0.3843 0.0283 6 ASP A CB 48 C CG . ASP A 6 ? 2.1499 2.0723 1.3620 -0.5804 -0.3977 0.0667 6 ASP A CG 49 O OD1 . ASP A 6 ? 2.3025 2.2198 1.5314 -0.5701 -0.3969 0.0970 6 ASP A OD1 50 O OD2 . ASP A 6 ? 2.0899 2.0267 1.2580 -0.6009 -0.4098 0.0665 6 ASP A OD2 51 N N . SER A 7 ? 1.5657 1.4600 0.7665 -0.5557 -0.3262 0.0402 7 SER A N 52 C CA . SER A 7 ? 1.6259 1.5246 0.7807 -0.5639 -0.3046 0.0435 7 SER A CA 53 C C . SER A 7 ? 1.7018 1.5886 0.8781 -0.5498 -0.2949 0.0674 7 SER A C 54 O O . SER A 7 ? 1.7681 1.6584 0.9428 -0.5538 -0.3117 0.1076 7 SER A O 55 C CB . SER A 7 ? 1.6653 1.5834 0.7794 -0.5863 -0.3264 0.0704 7 SER A CB 56 O OG . SER A 7 ? 1.8231 1.7488 0.8942 -0.5964 -0.3049 0.0736 7 SER A OG 57 N N . PRO A 8 ? 1.6043 1.4759 0.8031 -0.5330 -0.2685 0.0426 8 PRO A N 58 C CA . PRO A 8 ? 1.4563 1.3155 0.6715 -0.5200 -0.2572 0.0607 8 PRO A CA 59 C C . PRO A 8 ? 1.4853 1.3504 0.6599 -0.5289 -0.2290 0.0556 8 PRO A C 60 O O . PRO A 8 ? 1.4990 1.3803 0.6321 -0.5454 -0.2196 0.0405 8 PRO A O 61 C CB . PRO A 8 ? 1.2803 1.1232 0.5360 -0.5006 -0.2415 0.0331 8 PRO A CB 62 C CG . PRO A 8 ? 1.4860 1.3330 0.7292 -0.5058 -0.2257 -0.0102 8 PRO A CG 63 C CD . PRO A 8 ? 1.5378 1.4013 0.7530 -0.5247 -0.2501 -0.0022 8 PRO A CD 64 N N . ALA A 9 ? 1.4196 1.2733 0.6073 -0.5183 -0.2158 0.0677 9 ALA A N 65 C CA . ALA A 9 ? 1.5076 1.3687 0.6656 -0.5259 -0.1879 0.0640 9 ALA A CA 66 C C . ALA A 9 ? 1.4294 1.2829 0.5987 -0.5131 -0.1520 0.0262 9 ALA A C 67 O O . ALA A 9 ? 1.3814 1.2168 0.5852 -0.4956 -0.1494 0.0266 9 ALA A O 68 C CB . ALA A 9 ? 1.6576 1.5123 0.8236 -0.5254 -0.1994 0.1072 9 ALA A CB 69 N N . GLU A 10 ? 1.4214 1.2897 0.5633 -0.5213 -0.1246 -0.0066 10 GLU A N 70 C CA . GLU A 10 ? 1.4014 1.2649 0.5588 -0.5086 -0.0901 -0.0446 10 GLU A CA 71 C C . GLU A 10 ? 1.4607 1.3360 0.6031 -0.5129 -0.0618 -0.0425 10 GLU A C 72 O O . GLU A 10 ? 1.5251 1.4225 0.6314 -0.5296 -0.0529 -0.0414 10 GLU A O 73 C CB . GLU A 10 ? 1.3650 1.2350 0.5138 -0.5102 -0.0775 -0.0882 10 GLU A CB 74 C CG . GLU A 10 ? 1.4861 1.3437 0.6588 -0.5048 -0.1029 -0.0943 10 GLU A CG 75 C CD . GLU A 10 ? 1.7594 1.6216 0.9223 -0.5080 -0.0936 -0.1362 10 GLU A CD 76 O OE1 . GLU A 10 ? 2.0540 1.9284 1.1921 -0.5125 -0.0657 -0.1629 10 GLU A OE1 77 O OE2 . GLU A 10 ? 1.6693 1.5231 0.8513 -0.5060 -0.1146 -0.1426 10 GLU A OE2 78 N N . TYR A 11 ? 1.2692 1.1309 0.4405 -0.4983 -0.0482 -0.0417 11 TYR A N 79 C CA . TYR A 11 ? 1.2685 1.1414 0.4347 -0.5008 -0.0208 -0.0403 11 TYR A CA 80 C C . TYR A 11 ? 1.2433 1.1159 0.4321 -0.4870 0.0130 -0.0818 11 TYR A C 81 O O . TYR A 11 ? 1.2027 1.0554 0.4246 -0.4705 0.0109 -0.0976 11 TYR A O 82 C CB . TYR A 11 ? 1.3591 1.2172 0.5416 -0.4963 -0.0337 -0.0007 11 TYR A CB 83 C CG . TYR A 11 ? 1.2621 1.1187 0.4323 -0.5073 -0.0673 0.0424 11 TYR A CG 84 C CD1 . TYR A 11 ? 1.2479 1.0875 0.4333 -0.5004 -0.1000 0.0595 11 TYR A CD1 85 C CD2 . TYR A 11 ? 1.3686 1.2422 0.5172 -0.5242 -0.0669 0.0666 11 TYR A CD2 86 C CE1 . TYR A 11 ? 1.2719 1.1106 0.4534 -0.5087 -0.1311 0.0993 11 TYR A CE1 87 C CE2 . TYR A 11 ? 1.4680 1.3391 0.6113 -0.5334 -0.0988 0.1063 11 TYR A CE2 88 C CZ . TYR A 11 ? 1.5769 1.4302 0.7378 -0.5249 -0.1307 0.1223 11 TYR A CZ 89 O OH . TYR A 11 ? 1.6796 1.5313 0.8418 -0.5325 -0.1626 0.1619 11 TYR A OH 90 N N . SER A 12 ? 1.2690 1.1647 0.4445 -0.4935 0.0436 -0.0988 12 SER A N 91 C CA . SER A 12 ? 1.2515 1.1502 0.4527 -0.4801 0.0768 -0.1393 12 SER A CA 92 C C . SER A 12 ? 1.3402 1.2569 0.5478 -0.4814 0.1052 -0.1354 12 SER A C 93 O O . SER A 12 ? 1.5184 1.4601 0.6991 -0.4975 0.1127 -0.1224 12 SER A O 94 C CB . SER A 12 ? 1.3030 1.2151 0.4895 -0.4831 0.0902 -0.1784 12 SER A CB 95 O OG . SER A 12 ? 1.3698 1.3113 0.5148 -0.5020 0.0994 -0.1740 12 SER A OG 96 N N . GLY A 13 ? 1.1979 1.1034 0.4437 -0.4651 0.1204 -0.1461 13 GLY A N 97 C CA . GLY A 13 ? 1.1885 1.1130 0.4494 -0.4647 0.1492 -0.1454 13 GLY A CA 98 C C . GLY A 13 ? 1.3847 1.3269 0.6660 -0.4555 0.1845 -0.1912 13 GLY A C 99 O O . GLY A 13 ? 1.6044 1.5413 0.8858 -0.4501 0.1850 -0.2224 13 GLY A O 100 N N . PRO A 14 ? 1.2729 1.2365 0.5771 -0.4529 0.2135 -0.1946 14 PRO A N 101 C CA . PRO A 14 ? 1.3413 1.3240 0.6745 -0.4414 0.2490 -0.2374 14 PRO A CA 102 C C . PRO A 14 ? 1.3055 1.2616 0.6970 -0.4138 0.2462 -0.2616 14 PRO A C 103 O O . PRO A 14 ? 1.2540 1.1878 0.6877 -0.3981 0.2255 -0.2378 14 PRO A O 104 C CB . PRO A 14 ? 1.1846 1.1953 0.5418 -0.4434 0.2729 -0.2230 14 PRO A CB 105 C CG . PRO A 14 ? 1.1427 1.1337 0.5157 -0.4423 0.2434 -0.1760 14 PRO A CG 106 C CD . PRO A 14 ? 1.1646 1.1352 0.4854 -0.4565 0.2110 -0.1559 14 PRO A CD 107 N N . GLU A 15 ? 1.2935 1.2515 0.6900 -0.4076 0.2656 -0.3072 15 GLU A N 108 C CA . GLU A 15 ? 1.2314 1.1622 0.6864 -0.3823 0.2606 -0.3285 15 GLU A CA 109 C C . GLU A 15 ? 1.1788 1.1134 0.7092 -0.3590 0.2727 -0.3217 15 GLU A C 110 O O . GLU A 15 ? 1.1015 1.0664 0.6450 -0.3601 0.2990 -0.3239 15 GLU A O 111 C CB . GLU A 15 ? 1.2739 1.2054 0.7262 -0.3793 0.2771 -0.3768 15 GLU A CB 112 C CG . GLU A 15 ? 1.4311 1.3991 0.8931 -0.3776 0.3148 -0.4019 15 GLU A CG 113 C CD . GLU A 15 ? 1.6714 1.6370 1.1432 -0.3688 0.3256 -0.4451 15 GLU A CD 114 O OE1 . GLU A 15 ? 1.7947 1.7279 1.2804 -0.3605 0.3058 -0.4567 15 GLU A OE1 115 O OE2 . GLU A 15 ? 1.7275 1.7235 1.1941 -0.3704 0.3532 -0.4667 15 GLU A OE2 116 N N . GLY A 16 ? 1.1427 1.0490 0.7226 -0.3391 0.2525 -0.3117 16 GLY A N 117 C CA . GLY A 16 ? 1.0227 0.9307 0.6732 -0.3174 0.2584 -0.3027 16 GLY A CA 118 C C . GLY A 16 ? 0.9608 0.8716 0.6155 -0.3194 0.2428 -0.2590 16 GLY A C 119 O O . GLY A 16 ? 0.9765 0.8905 0.6843 -0.3043 0.2442 -0.2475 16 GLY A O 120 N N . SER A 17 ? 0.9792 0.8882 0.5791 -0.3387 0.2264 -0.2348 17 SER A N 121 C CA . SER A 17 ? 0.9783 0.8864 0.5785 -0.3427 0.2108 -0.1950 17 SER A CA 122 C C . SER A 17 ? 0.9606 0.8369 0.5710 -0.3323 0.1783 -0.1722 17 SER A C 123 O O . SER A 17 ? 0.9499 0.8195 0.5632 -0.3329 0.1628 -0.1419 17 SER A O 124 C CB . SER A 17 ? 1.0013 0.9256 0.5410 -0.3696 0.2114 -0.1778 17 SER A CB 125 O OG . SER A 17 ? 1.0167 0.9275 0.5049 -0.3821 0.1935 -0.1773 17 SER A OG 126 N N . TYR A 18 ? 0.9551 0.8124 0.5727 -0.3232 0.1689 -0.1880 18 TYR A N 127 C CA . TYR A 18 ? 1.0310 0.8623 0.6551 -0.3151 0.1401 -0.1687 18 TYR A CA 128 C C . TYR A 18 ? 1.0524 0.8790 0.6296 -0.3311 0.1196 -0.1411 18 TYR A C 129 O O . TYR A 18 ? 1.0007 0.8126 0.5883 -0.3242 0.0995 -0.1154 18 TYR A O 130 C CB . TYR A 18 ? 1.0347 0.8579 0.7108 -0.2952 0.1338 -0.1529 18 TYR A CB 131 C CG . TYR A 18 ? 0.9013 0.7238 0.6306 -0.2770 0.1458 -0.1731 18 TYR A CG 132 C CD1 . TYR A 18 ? 0.8644 0.6805 0.6388 -0.2597 0.1383 -0.1587 18 TYR A CD1 133 C CD2 . TYR A 18 ? 0.9973 0.8248 0.7318 -0.2772 0.1639 -0.2065 18 TYR A CD2 134 C CE1 . TYR A 18 ? 0.9108 0.7263 0.7360 -0.2437 0.1467 -0.1725 18 TYR A CE1 135 C CE2 . TYR A 18 ? 1.1821 1.0059 0.9711 -0.2596 0.1734 -0.2233 18 TYR A CE2 136 C CZ . TYR A 18 ? 1.0885 0.9067 0.9238 -0.2431 0.1638 -0.2040 18 TYR A CZ 137 O OH . TYR A 18 ? 1.2163 1.0310 1.1079 -0.2262 0.1708 -0.2162 18 TYR A OH 138 N N . PHE A 19 ? 1.0639 0.9037 0.5901 -0.3524 0.1250 -0.1467 19 PHE A N 139 C CA . PHE A 19 ? 0.9712 0.8075 0.4517 -0.3696 0.1040 -0.1190 19 PHE A CA 140 C C . PHE A 19 ? 0.9504 0.7647 0.4336 -0.3631 0.0758 -0.1096 19 PHE A C 141 O O . PHE A 19 ? 0.9612 0.7708 0.4434 -0.3619 0.0737 -0.1313 19 PHE A O 142 C CB . PHE A 19 ? 1.1212 0.9785 0.5434 -0.3948 0.1153 -0.1295 19 PHE A CB 143 C CG . PHE A 19 ? 1.1826 1.0380 0.5561 -0.4147 0.0918 -0.0984 19 PHE A CG 144 C CD1 . PHE A 19 ? 1.3805 1.2264 0.7259 -0.4221 0.0693 -0.0980 19 PHE A CD1 145 C CD2 . PHE A 19 ? 1.1317 0.9951 0.4905 -0.4271 0.0908 -0.0683 19 PHE A CD2 146 C CE1 . PHE A 19 ? 1.3175 1.1629 0.6219 -0.4400 0.0454 -0.0669 19 PHE A CE1 147 C CE2 . PHE A 19 ? 1.2058 1.0657 0.5235 -0.4454 0.0674 -0.0369 19 PHE A CE2 148 C CZ . PHE A 19 ? 1.1994 1.0509 0.4902 -0.4512 0.0445 -0.0357 19 PHE A CZ 149 N N . GLY A 20 ? 0.9297 0.7307 0.4192 -0.3589 0.0543 -0.0779 20 GLY A N 150 C CA . GLY A 20 ? 0.9801 0.7642 0.4799 -0.3506 0.0289 -0.0666 20 GLY A CA 151 C C . GLY A 20 ? 0.9008 0.6720 0.4537 -0.3260 0.0270 -0.0654 20 GLY A C 152 O O . GLY A 20 ? 1.0601 0.8211 0.6296 -0.3168 0.0110 -0.0605 20 GLY A O 153 N N . PHE A 21 ? 0.8401 0.6147 0.4198 -0.3162 0.0431 -0.0686 21 PHE A N 154 C CA . PHE A 21 ? 0.8508 0.6159 0.4765 -0.2945 0.0413 -0.0657 21 PHE A CA 155 C C . PHE A 21 ? 0.7804 0.5321 0.4099 -0.2877 0.0216 -0.0389 21 PHE A C 156 O O . PHE A 21 ? 0.7516 0.4949 0.4099 -0.2711 0.0144 -0.0343 21 PHE A O 157 C CB . PHE A 21 ? 0.7872 0.5620 0.4397 -0.2878 0.0613 -0.0749 21 PHE A CB 158 C CG . PHE A 21 ? 0.7558 0.5239 0.4529 -0.2672 0.0595 -0.0731 21 PHE A CG 159 C CD1 . PHE A 21 ? 0.7299 0.4968 0.4555 -0.2569 0.0646 -0.0890 21 PHE A CD1 160 C CD2 . PHE A 21 ? 0.7205 0.4829 0.4299 -0.2594 0.0518 -0.0550 21 PHE A CD2 161 C CE1 . PHE A 21 ? 0.6979 0.4608 0.4622 -0.2398 0.0620 -0.0835 21 PHE A CE1 162 C CE2 . PHE A 21 ? 0.8669 0.6258 0.6113 -0.2422 0.0499 -0.0529 21 PHE A CE2 163 C CZ . PHE A 21 ? 0.7360 0.4965 0.5073 -0.2327 0.0550 -0.0653 21 PHE A CZ 164 N N . ALA A 22 ? 0.8518 0.6019 0.4527 -0.3007 0.0137 -0.0212 22 ALA A N 165 C CA . ALA A 22 ? 0.9416 0.6759 0.5457 -0.2949 -0.0058 0.0031 22 ALA A CA 166 C C . ALA A 22 ? 1.0742 0.8066 0.6418 -0.3126 -0.0211 0.0211 22 ALA A C 167 O O . ALA A 22 ? 1.3871 1.1305 0.9236 -0.3319 -0.0135 0.0217 22 ALA A O 168 C CB . ALA A 22 ? 1.1696 0.8982 0.7898 -0.2894 -0.0013 0.0106 22 ALA A CB 169 N N . VAL A 23 ? 0.9914 0.7122 0.5639 -0.3062 -0.0426 0.0372 23 VAL A N 170 C CA . VAL A 23 ? 0.9840 0.7027 0.5267 -0.3218 -0.0617 0.0583 23 VAL A CA 171 C C . VAL A 23 ? 1.0754 0.7746 0.6360 -0.3112 -0.0820 0.0831 23 VAL A C 172 O O . VAL A 23 ? 1.1902 0.8802 0.7850 -0.2898 -0.0838 0.0803 23 VAL A O 173 C CB . VAL A 23 ? 0.8991 0.6276 0.4277 -0.3286 -0.0719 0.0523 23 VAL A CB 174 C CG1 . VAL A 23 ? 1.0014 0.7468 0.5022 -0.3440 -0.0537 0.0276 23 VAL A CG1 175 C CG2 . VAL A 23 ? 0.8530 0.5779 0.4208 -0.3078 -0.0771 0.0457 23 VAL A CG2 176 N N . ASP A 24 ? 1.0426 0.7359 0.5802 -0.3263 -0.0968 0.1073 24 ASP A N 177 C CA . ASP A 24 ? 1.0803 0.7528 0.6364 -0.3171 -0.1189 0.1320 24 ASP A CA 178 C C . ASP A 24 ? 1.0339 0.7052 0.5591 -0.3388 -0.1385 0.1607 24 ASP A C 179 O O . ASP A 24 ? 1.1243 0.8127 0.6094 -0.3619 -0.1328 0.1604 24 ASP A O 180 C CB . ASP A 24 ? 1.2772 0.9304 0.8564 -0.3055 -0.1128 0.1324 24 ASP A CB 181 C CG . ASP A 24 ? 1.5162 1.1465 1.1279 -0.2855 -0.1305 0.1448 24 ASP A CG 182 O OD1 . ASP A 24 ? 1.5948 1.2196 1.2068 -0.2875 -0.1520 0.1659 24 ASP A OD1 183 O OD2 . ASP A 24 ? 1.5718 1.1907 1.2092 -0.2674 -0.1229 0.1328 24 ASP A OD2 184 N N . PHE A 25 ? 1.1416 0.7931 0.6860 -0.3312 -0.1613 0.1856 25 PHE A N 185 C CA . PHE A 25 ? 1.1668 0.8141 0.6876 -0.3508 -0.1838 0.2189 25 PHE A CA 186 C C . PHE A 25 ? 1.2802 0.9063 0.8020 -0.3584 -0.1852 0.2374 25 PHE A C 187 O O . PHE A 25 ? 1.2990 0.9036 0.8542 -0.3405 -0.1813 0.2308 25 PHE A O 188 C CB . PHE A 25 ? 1.0642 0.7036 0.6110 -0.3385 -0.2122 0.2389 25 PHE A CB 189 C CG . PHE A 25 ? 1.1423 0.8051 0.6840 -0.3388 -0.2174 0.2289 25 PHE A CG 190 C CD1 . PHE A 25 ? 1.3829 1.0508 0.9595 -0.3158 -0.2087 0.2063 25 PHE A CD1 191 C CD2 . PHE A 25 ? 1.0805 0.7609 0.5815 -0.3638 -0.2321 0.2429 25 PHE A CD2 192 C CE1 . PHE A 25 ? 1.3868 1.0753 0.9626 -0.3179 -0.2150 0.1983 25 PHE A CE1 193 C CE2 . PHE A 25 ? 1.0821 0.7826 0.5789 -0.3658 -0.2393 0.2325 25 PHE A CE2 194 C CZ . PHE A 25 ? 1.1593 0.8631 0.6959 -0.3430 -0.2310 0.2103 25 PHE A CZ 195 N N . PHE A 26 ? 1.3710 1.0051 0.8563 -0.3857 -0.1909 0.2595 26 PHE A N 196 C CA . PHE A 26 ? 1.3010 0.9258 0.8017 -0.3884 -0.1956 0.2749 26 PHE A CA 197 C C . PHE A 26 ? 1.3364 0.9574 0.8464 -0.3912 -0.2260 0.3067 26 PHE A C 198 O O . PHE A 26 ? 1.4244 1.0691 0.9034 -0.4111 -0.2340 0.3197 26 PHE A O 199 C CB . PHE A 26 ? 1.1400 0.7895 0.6103 -0.4106 -0.1739 0.2684 26 PHE A CB 200 C CG . PHE A 26 ? 1.2480 0.8907 0.7334 -0.4166 -0.1793 0.2868 26 PHE A CG 201 C CD1 . PHE A 26 ? 1.3766 1.0374 0.8407 -0.4378 -0.1887 0.3100 26 PHE A CD1 202 C CD2 . PHE A 26 ? 1.1800 0.7982 0.7008 -0.4021 -0.1758 0.2810 26 PHE A CD2 203 C CE1 . PHE A 26 ? 1.3961 1.0501 0.8756 -0.4446 -0.1942 0.3290 26 PHE A CE1 204 C CE2 . PHE A 26 ? 1.1723 0.7828 0.7079 -0.4088 -0.1820 0.2979 26 PHE A CE2 205 C CZ . PHE A 26 ? 1.3354 0.9634 0.8513 -0.4301 -0.1911 0.3230 26 PHE A CZ 206 N N . VAL A 27 ? 1.2788 0.8702 0.8330 -0.3710 -0.2426 0.3178 27 VAL A N 207 C CA . VAL A 27 ? 1.4021 0.9869 0.9752 -0.3704 -0.2721 0.3484 27 VAL A CA 208 C C . VAL A 27 ? 1.3171 0.8779 0.9195 -0.3663 -0.2779 0.3606 27 VAL A C 209 O O . VAL A 27 ? 1.2466 0.7764 0.8908 -0.3431 -0.2833 0.3561 27 VAL A O 210 C CB . VAL A 27 ? 1.3868 0.9597 0.9928 -0.3478 -0.2907 0.3523 27 VAL A CB 211 C CG1 . VAL A 27 ? 1.2608 0.8083 0.8994 -0.3207 -0.2781 0.3286 27 VAL A CG1 212 C CG2 . VAL A 27 ? 1.5203 1.0833 1.1583 -0.3430 -0.3213 0.3836 27 VAL A CG2 213 N N . PRO A 28 ? 1.2302 0.8057 0.8100 -0.3899 -0.2757 0.3748 28 PRO A N 214 C CA . PRO A 28 ? 1.2526 0.8082 0.8563 -0.3910 -0.2802 0.3875 28 PRO A CA 215 C C . PRO A 28 ? 1.2890 0.8223 0.9292 -0.3821 -0.3106 0.4156 28 PRO A C 216 O O . PRO A 28 ? 1.4485 0.9942 1.0844 -0.3861 -0.3295 0.4343 28 PRO A O 217 C CB . PRO A 28 ? 1.4202 1.0065 0.9846 -0.4216 -0.2687 0.3969 28 PRO A CB 218 C CG . PRO A 28 ? 1.5969 1.2148 1.1226 -0.4364 -0.2720 0.4017 28 PRO A CG 219 C CD . PRO A 28 ? 1.2523 0.8658 0.7817 -0.4178 -0.2679 0.3788 28 PRO A CD 220 N N . SER A 29 ? 1.2978 0.7988 0.9755 -0.3704 -0.3157 0.4176 29 SER A N 221 C CA . SER A 29 ? 1.4410 0.9169 1.1593 -0.3605 -0.3432 0.4423 29 SER A CA 222 C C . SER A 29 ? 1.5265 1.0127 1.2333 -0.3866 -0.3558 0.4752 29 SER A C 223 O O . SER A 29 ? 1.5103 0.9825 1.2450 -0.3844 -0.3811 0.5020 29 SER A O 224 C CB . SER A 29 ? 1.3271 0.7605 1.0915 -0.3356 -0.3428 0.4263 29 SER A CB 225 O OG . SER A 29 ? 1.3201 0.7487 1.0758 -0.3452 -0.3252 0.4129 29 SER A OG 226 N N . ALA A 30 ? 1.5343 1.0464 1.2019 -0.4112 -0.3377 0.4734 30 ALA A N 227 C CA . ALA A 30 ? 1.4463 0.9719 1.0997 -0.4380 -0.3458 0.5039 30 ALA A CA 228 C C . ALA A 30 ? 1.4735 1.0382 1.0843 -0.4605 -0.3516 0.5217 30 ALA A C 229 O O . ALA A 30 ? 1.5226 1.1042 1.1158 -0.4850 -0.3587 0.5487 30 ALA A O 230 C CB . ALA A 30 ? 1.6461 1.1802 1.2850 -0.4527 -0.3223 0.4935 30 ALA A CB 231 N N . SER A 31 ? 1.7446 1.3238 1.3386 -0.4530 -0.3490 0.5063 31 SER A N 232 C CA . SER A 31 ? 1.6508 1.2673 1.2015 -0.4745 -0.3535 0.5175 31 SER A CA 233 C C . SER A 31 ? 1.6050 1.2224 1.1639 -0.4598 -0.3685 0.5139 31 SER A C 234 O O . SER A 31 ? 1.6250 1.2245 1.2076 -0.4348 -0.3629 0.4913 31 SER A O 235 C CB . SER A 31 ? 1.5617 1.2118 1.0610 -0.4930 -0.3221 0.4948 31 SER A CB 236 O OG . SER A 31 ? 1.5158 1.2007 0.9710 -0.5128 -0.3247 0.4998 31 SER A OG 237 N N . SER A 32 ? 1.5238 1.1639 1.0637 -0.4763 -0.3879 0.5369 32 SER A N 238 C CA . SER A 32 ? 1.4862 1.1331 1.0323 -0.4666 -0.4041 0.5363 32 SER A CA 239 C C . SER A 32 ? 1.4672 1.1412 0.9665 -0.4748 -0.3827 0.5066 32 SER A C 240 O O . SER A 32 ? 1.4669 1.1454 0.9711 -0.4646 -0.3903 0.4976 32 SER A O 241 C CB . SER A 32 ? 1.5460 1.2070 1.0923 -0.4824 -0.4354 0.5737 32 SER A CB 242 O OG . SER A 32 ? 1.6135 1.3066 1.1055 -0.5160 -0.4288 0.5839 32 SER A OG 243 N N . ARG A 33 ? 1.4618 1.1545 0.9187 -0.4933 -0.3558 0.4912 33 ARG A N 244 C CA . ARG A 33 ? 1.4408 1.1576 0.8541 -0.5012 -0.3318 0.4595 33 ARG A CA 245 C C . ARG A 33 ? 1.4935 1.1911 0.9265 -0.4766 -0.3133 0.4275 33 ARG A C 246 O O . ARG A 33 ? 1.4722 1.1409 0.9437 -0.4576 -0.3110 0.4259 33 ARG A O 247 C CB . ARG A 33 ? 1.4785 1.2230 0.8453 -0.5273 -0.3069 0.4527 33 ARG A CB 248 C CG . ARG A 33 ? 1.6098 1.3853 0.9374 -0.5560 -0.3184 0.4743 33 ARG A CG 249 C CD . ARG A 33 ? 1.7985 1.5927 1.0989 -0.5610 -0.3253 0.4623 33 ARG A CD 250 N NE . ARG A 33 ? 1.9513 1.7509 1.2335 -0.5537 -0.2974 0.4205 33 ARG A NE 251 C CZ . ARG A 33 ? 2.0100 1.8233 1.2692 -0.5562 -0.2978 0.4015 33 ARG A CZ 252 N NH1 . ARG A 33 ? 1.9677 1.7924 1.2187 -0.5662 -0.3248 0.4206 33 ARG A NH1 253 N NH2 . ARG A 33 ? 2.0263 1.8420 1.2728 -0.5490 -0.2719 0.3637 33 ARG A NH2 254 N N . MET A 34 ? 1.5134 1.2267 0.9194 -0.4779 -0.3005 0.4017 34 MET A N 255 C CA . MET A 34 ? 1.3895 1.0885 0.8081 -0.4579 -0.2813 0.3712 34 MET A CA 256 C C . MET A 34 ? 1.3706 1.0939 0.7440 -0.4724 -0.2500 0.3402 34 MET A C 257 O O . MET A 34 ? 1.5684 1.3207 0.9004 -0.4947 -0.2468 0.3387 34 MET A O 258 C CB . MET A 34 ? 1.3407 1.0302 0.7841 -0.4393 -0.2995 0.3704 34 MET A CB 259 C CG . MET A 34 ? 1.5079 1.1749 1.0034 -0.4214 -0.3290 0.3984 34 MET A CG 260 S SD . MET A 34 ? 1.4715 1.1357 1.0003 -0.4003 -0.3501 0.3995 34 MET A SD 261 C CE . MET A 34 ? 1.5431 1.1830 1.1361 -0.3806 -0.3803 0.4325 34 MET A CE 262 N N . PHE A 35 ? 1.2369 0.9489 0.6200 -0.4591 -0.2262 0.3143 35 PHE A N 263 C CA . PHE A 35 ? 1.2274 0.9611 0.5754 -0.4702 -0.1941 0.2835 35 PHE A CA 264 C C . PHE A 35 ? 1.2430 0.9657 0.5999 -0.4532 -0.1797 0.2551 35 PHE A C 265 O O . PHE A 35 ? 1.3279 1.0241 0.7213 -0.4317 -0.1902 0.2590 35 PHE A O 266 C CB . PHE A 35 ? 1.2858 1.0250 0.6342 -0.4779 -0.1727 0.2820 35 PHE A CB 267 C CG . PHE A 35 ? 1.3446 1.0980 0.6804 -0.4976 -0.1834 0.3097 35 PHE A CG 268 C CD1 . PHE A 35 ? 1.2949 1.0263 0.6639 -0.4917 -0.2053 0.3395 35 PHE A CD1 269 C CD2 . PHE A 35 ? 1.4089 1.1976 0.7007 -0.5217 -0.1707 0.3053 35 PHE A CD2 270 C CE1 . PHE A 35 ? 1.6315 1.3754 0.9899 -0.5109 -0.2157 0.3673 35 PHE A CE1 271 C CE2 . PHE A 35 ? 1.5981 1.4013 0.8771 -0.5409 -0.1801 0.3329 35 PHE A CE2 272 C CZ . PHE A 35 ? 1.7448 1.5255 1.0572 -0.5361 -0.2033 0.3653 35 PHE A CZ 273 N N . LEU A 36 ? 1.2140 0.9576 0.5389 -0.4627 -0.1545 0.2256 36 LEU A N 274 C CA . LEU A 36 ? 1.1876 0.9255 0.5259 -0.4460 -0.1374 0.1943 36 LEU A CA 275 C C . LEU A 36 ? 1.2905 1.0302 0.6442 -0.4404 -0.1065 0.1741 36 LEU A C 276 O O . LEU A 36 ? 1.5103 1.2702 0.8324 -0.4599 -0.0865 0.1688 36 LEU A O 277 C CB . LEU A 36 ? 1.2012 0.9618 0.5094 -0.4539 -0.1315 0.1676 36 LEU A CB 278 C CG . LEU A 36 ? 1.4041 1.1676 0.6996 -0.4594 -0.1621 0.1811 36 LEU A CG 279 C CD1 . LEU A 36 ? 1.8302 1.6131 1.0922 -0.4838 -0.1748 0.2019 36 LEU A CD1 280 C CD2 . LEU A 36 ? 1.2124 0.9879 0.5074 -0.4543 -0.1542 0.1447 36 LEU A CD2 281 N N . LEU A 37 ? 1.0542 0.7757 0.4570 -0.4142 -0.1028 0.1633 37 LEU A N 282 C CA . LEU A 37 ? 1.1309 0.8552 0.5536 -0.4070 -0.0765 0.1436 37 LEU A CA 283 C C . LEU A 37 ? 1.1265 0.8638 0.5624 -0.3932 -0.0566 0.1061 37 LEU A C 284 O O . LEU A 37 ? 1.0260 0.7543 0.4882 -0.3736 -0.0646 0.0968 37 LEU A O 285 C CB . LEU A 37 ? 1.1280 0.8246 0.5929 -0.3891 -0.0848 0.1541 37 LEU A CB 286 C CG . LEU A 37 ? 1.0322 0.7105 0.4925 -0.4022 -0.1030 0.1898 37 LEU A CG 287 C CD1 . LEU A 37 ? 1.0079 0.6579 0.5100 -0.3844 -0.1074 0.1915 37 LEU A CD1 288 C CD2 . LEU A 37 ? 1.0671 0.7684 0.4957 -0.4291 -0.0899 0.1981 37 LEU A CD2 289 N N . VAL A 38 ? 0.9980 0.7575 0.4185 -0.4035 -0.0304 0.0857 38 VAL A N 290 C CA . VAL A 38 ? 0.9726 0.7433 0.4080 -0.3914 -0.0109 0.0502 38 VAL A CA 291 C C . VAL A 38 ? 1.0190 0.7988 0.4802 -0.3851 0.0147 0.0347 38 VAL A C 292 O O . VAL A 38 ? 0.9833 0.7805 0.4273 -0.4016 0.0303 0.0374 38 VAL A O 293 C CB . VAL A 38 ? 1.0715 0.8629 0.4650 -0.4084 -0.0028 0.0321 38 VAL A CB 294 C CG1 . VAL A 38 ? 0.9921 0.7874 0.4083 -0.3937 0.0125 -0.0040 38 VAL A CG1 295 C CG2 . VAL A 38 ? 1.0795 0.8660 0.4427 -0.4197 -0.0310 0.0515 38 VAL A CG2 296 N N . GLY A 39 ? 0.9042 0.6752 0.4080 -0.3619 0.0184 0.0206 39 GLY A N 297 C CA . GLY A 39 ? 0.9080 0.6886 0.4416 -0.3543 0.0395 0.0068 39 GLY A CA 298 C C . GLY A 39 ? 1.0357 0.8378 0.5710 -0.3545 0.0642 -0.0242 39 GLY A C 299 O O . GLY A 39 ? 1.1718 0.9727 0.7023 -0.3502 0.0629 -0.0412 39 GLY A O 300 N N . ALA A 40 ? 0.9188 0.7407 0.4650 -0.3593 0.0864 -0.0321 40 ALA A N 301 C CA . ALA A 40 ? 0.8906 0.7340 0.4468 -0.3570 0.1128 -0.0633 40 ALA A CA 302 C C . ALA A 40 ? 0.9088 0.7646 0.5111 -0.3467 0.1289 -0.0684 40 ALA A C 303 O O . ALA A 40 ? 1.0309 0.9108 0.6314 -0.3589 0.1472 -0.0682 40 ALA A O 304 C CB . ALA A 40 ? 0.9418 0.8085 0.4512 -0.3803 0.1283 -0.0709 40 ALA A CB 305 N N . PRO A 41 ? 0.8624 0.7046 0.5070 -0.3251 0.1217 -0.0714 41 PRO A N 306 C CA . PRO A 41 ? 0.8959 0.7466 0.5860 -0.3147 0.1287 -0.0698 41 PRO A CA 307 C C . PRO A 41 ? 0.8706 0.7503 0.5881 -0.3130 0.1570 -0.0922 41 PRO A C 308 O O . PRO A 41 ? 0.9525 0.8474 0.7031 -0.3110 0.1642 -0.0870 41 PRO A O 309 C CB . PRO A 41 ? 0.9073 0.7372 0.6267 -0.2930 0.1133 -0.0695 41 PRO A CB 310 C CG . PRO A 41 ? 1.0302 0.8500 0.7331 -0.2902 0.1099 -0.0827 41 PRO A CG 311 C CD . PRO A 41 ? 1.0145 0.8352 0.6660 -0.3105 0.1061 -0.0760 41 PRO A CD 312 N N . LYS A 42 ? 0.8379 0.7251 0.5451 -0.3131 0.1722 -0.1178 42 LYS A N 313 C CA . LYS A 42 ? 0.8791 0.7934 0.6161 -0.3090 0.2011 -0.1430 42 LYS A CA 314 C C . LYS A 42 ? 0.9735 0.9172 0.6759 -0.3302 0.2242 -0.1503 42 LYS A C 315 O O . LYS A 42 ? 1.0960 1.0660 0.8190 -0.3278 0.2521 -0.1743 42 LYS A O 316 C CB . LYS A 42 ? 0.9139 0.8178 0.6698 -0.2939 0.2064 -0.1717 42 LYS A CB 317 C CG . LYS A 42 ? 0.9062 0.7866 0.7014 -0.2735 0.1870 -0.1634 42 LYS A CG 318 C CD . LYS A 42 ? 1.0102 0.8895 0.8505 -0.2565 0.1990 -0.1896 42 LYS A CD 319 C CE . LYS A 42 ? 1.2855 1.1916 1.1761 -0.2483 0.2203 -0.1980 42 LYS A CE 320 N NZ . LYS A 42 ? 1.5189 1.4213 1.4605 -0.2300 0.2307 -0.2224 42 LYS A NZ 321 N N . ALA A 43 ? 0.9980 0.9384 0.6490 -0.3506 0.2130 -0.1291 43 ALA A N 322 C CA . ALA A 43 ? 1.0136 0.9830 0.6236 -0.3742 0.2330 -0.1308 43 ALA A CA 323 C C . ALA A 43 ? 1.1358 1.1385 0.7765 -0.3802 0.2535 -0.1233 43 ALA A C 324 O O . ALA A 43 ? 1.2062 1.2030 0.8833 -0.3743 0.2414 -0.1030 43 ALA A O 325 C CB . ALA A 43 ? 0.9693 0.9251 0.5214 -0.3949 0.2113 -0.1030 43 ALA A CB 326 N N . ASN A 44 ? 1.1964 1.2358 0.8221 -0.3928 0.2849 -0.1406 44 ASN A N 327 C CA . ASN A 44 ? 1.1238 1.2022 0.7774 -0.4018 0.3076 -0.1327 44 ASN A CA 328 C C . ASN A 44 ? 1.0969 1.1811 0.7136 -0.4294 0.2975 -0.0948 44 ASN A C 329 O O . ASN A 44 ? 1.2263 1.2983 0.7829 -0.4464 0.2851 -0.0825 44 ASN A O 330 C CB . ASN A 44 ? 1.1745 1.2940 0.8290 -0.4037 0.3487 -0.1676 44 ASN A CB 331 C CG . ASN A 44 ? 1.1923 1.3181 0.9166 -0.3755 0.3642 -0.1977 44 ASN A CG 332 O OD1 . ASN A 44 ? 1.1398 1.2793 0.9246 -0.3656 0.3662 -0.1875 44 ASN A OD1 333 N ND2 . ASN A 44 ? 1.6177 1.7329 1.3362 -0.3629 0.3736 -0.2341 44 ASN A ND2 334 N N . THR A 45 ? 1.0260 1.1287 0.6813 -0.4347 0.3011 -0.0750 45 THR A N 335 C CA . THR A 45 ? 1.0115 1.1163 0.6417 -0.4611 0.2893 -0.0364 45 THR A CA 336 C C . THR A 45 ? 1.1596 1.3156 0.8054 -0.4771 0.3177 -0.0313 45 THR A C 337 O O . THR A 45 ? 1.1356 1.3271 0.8237 -0.4679 0.3481 -0.0554 45 THR A O 338 C CB . THR A 45 ? 1.0194 1.0899 0.6814 -0.4543 0.2560 -0.0098 45 THR A CB 339 O OG1 . THR A 45 ? 0.9414 1.0274 0.6710 -0.4382 0.2638 -0.0191 45 THR A OG1 340 C CG2 . THR A 45 ? 1.0684 1.0900 0.7141 -0.4375 0.2257 -0.0113 45 THR A CG2 341 N N . THR A 46 ? 1.2414 1.3989 0.8613 -0.4945 0.3025 0.0006 46 THR A N 342 C CA . THR A 46 ? 1.0974 1.2991 0.7358 -0.5060 0.3206 0.0122 46 THR A CA 343 C C . THR A 46 ? 1.1534 1.3612 0.8571 -0.5037 0.3155 0.0286 46 THR A C 344 O O . THR A 46 ? 1.1648 1.4111 0.8976 -0.5118 0.3309 0.0387 46 THR A O 345 C CB . THR A 46 ? 1.1473 1.3469 0.7374 -0.5266 0.3045 0.0436 46 THR A CB 346 O OG1 . THR A 46 ? 1.7184 1.9626 1.3289 -0.5385 0.3242 0.0562 46 THR A OG1 347 C CG2 . THR A 46 ? 1.1307 1.2825 0.7174 -0.5303 0.2631 0.0776 46 THR A CG2 348 N N . GLN A 47 ? 1.0595 1.2294 0.7858 -0.4932 0.2924 0.0316 47 GLN A N 349 C CA . GLN A 47 ? 0.9805 1.1509 0.7674 -0.4902 0.2820 0.0445 47 GLN A CA 350 C C . GLN A 47 ? 1.0367 1.2582 0.8834 -0.4826 0.3151 0.0240 47 GLN A C 351 O O . GLN A 47 ? 1.0408 1.2740 0.9001 -0.4679 0.3373 -0.0083 47 GLN A O 352 C CB . GLN A 47 ? 0.9379 1.0599 0.7343 -0.4773 0.2542 0.0436 47 GLN A CB 353 C CG . GLN A 47 ? 0.9491 1.0204 0.6928 -0.4798 0.2226 0.0599 47 GLN A CG 354 C CD . GLN A 47 ? 0.9095 0.9351 0.6667 -0.4590 0.1947 0.0556 47 GLN A CD 355 O OE1 . GLN A 47 ? 1.0763 1.0787 0.8109 -0.4424 0.1882 0.0400 47 GLN A OE1 356 N NE2 . GLN A 47 ? 1.0404 1.0538 0.8353 -0.4578 0.1761 0.0686 47 GLN A NE2 357 N N . PRO A 48 ? 1.0300 1.2822 0.9183 -0.4917 0.3181 0.0428 48 PRO A N 358 C CA . PRO A 48 ? 0.9626 1.2691 0.9156 -0.4850 0.3484 0.0281 48 PRO A CA 359 C C . PRO A 48 ? 1.0042 1.3078 1.0132 -0.4654 0.3484 0.0075 48 PRO A C 360 O O . PRO A 48 ? 0.9534 1.2212 0.9775 -0.4604 0.3155 0.0202 48 PRO A O 361 C CB . PRO A 48 ? 0.9728 1.2968 0.9583 -0.5008 0.3373 0.0613 48 PRO A CB 362 C CG . PRO A 48 ? 1.0080 1.2998 0.9331 -0.5177 0.3152 0.0881 48 PRO A CG 363 C CD . PRO A 48 ? 1.0423 1.2795 0.9205 -0.5092 0.2927 0.0801 48 PRO A CD 364 N N . GLY A 49 ? 1.0070 1.3445 1.0477 -0.4484 0.3810 -0.0247 49 GLY A N 365 C CA . GLY A 49 ? 0.9383 1.2704 1.0399 -0.4170 0.3743 -0.0433 49 GLY A CA 366 C C . GLY A 49 ? 0.9260 1.1977 1.0021 -0.3970 0.3428 -0.0497 49 GLY A C 367 O O . GLY A 49 ? 0.9650 1.2238 1.0872 -0.3761 0.3252 -0.0523 49 GLY A O 368 N N . ILE A 50 ? 0.9192 1.1569 0.9232 -0.4041 0.3352 -0.0506 50 ILE A N 369 C CA . ILE A 50 ? 0.9383 1.1214 0.9165 -0.3870 0.3064 -0.0551 50 ILE A CA 370 C C . ILE A 50 ? 1.0274 1.2015 0.9739 -0.3747 0.3223 -0.0861 50 ILE A C 371 O O . ILE A 50 ? 1.1503 1.3294 1.0412 -0.3907 0.3356 -0.0904 50 ILE A O 372 C CB . ILE A 50 ? 0.9841 1.1263 0.9097 -0.4039 0.2749 -0.0268 50 ILE A CB 373 C CG1 . ILE A 50 ? 1.0794 1.2262 1.0347 -0.4184 0.2578 0.0020 50 ILE A CG1 374 C CG2 . ILE A 50 ? 0.8235 0.9146 0.7294 -0.3847 0.2472 -0.0318 50 ILE A CG2 375 C CD1 . ILE A 50 ? 1.0326 1.1812 1.0513 -0.3997 0.2445 -0.0003 50 ILE A CD1 376 N N . VAL A 51 ? 0.9630 1.1236 0.9450 -0.3475 0.3192 -0.1066 51 VAL A N 377 C CA . VAL A 51 ? 0.9300 1.0777 0.8901 -0.3346 0.3314 -0.1379 51 VAL A CA 378 C C . VAL A 51 ? 0.9819 1.0769 0.9086 -0.3258 0.2995 -0.1330 51 VAL A C 379 O O . VAL A 51 ? 0.8830 0.9557 0.8386 -0.3121 0.2751 -0.1208 51 VAL A O 380 C CB . VAL A 51 ? 0.8701 1.0390 0.8978 -0.3099 0.3526 -0.1664 51 VAL A CB 381 C CG1 . VAL A 51 ? 0.9447 1.1097 1.0381 -0.2935 0.3317 -0.1505 51 VAL A CG1 382 C CG2 . VAL A 51 ? 0.8869 1.0302 0.8971 -0.2946 0.3570 -0.1977 51 VAL A CG2 383 N N . GLU A 52 ? 1.0352 1.1137 0.9006 -0.3349 0.3000 -0.1419 52 GLU A N 384 C CA . GLU A 52 ? 0.9269 0.9602 0.7589 -0.3288 0.2719 -0.1374 52 GLU A CA 385 C C . GLU A 52 ? 0.8835 0.8909 0.7110 -0.3320 0.2396 -0.1041 52 GLU A C 386 O O . GLU A 52 ? 0.8564 0.8350 0.6979 -0.3160 0.2178 -0.1002 52 GLU A O 387 C CB . GLU A 52 ? 0.9783 0.9951 0.8473 -0.3029 0.2704 -0.1604 52 GLU A CB 388 C CG . GLU A 52 ? 1.2116 1.2415 1.0781 -0.2986 0.2980 -0.1979 52 GLU A CG 389 C CD . GLU A 52 ? 1.4001 1.4041 1.2978 -0.2756 0.2908 -0.2174 52 GLU A CD 390 O OE1 . GLU A 52 ? 1.4507 1.4353 1.3810 -0.2617 0.2684 -0.2004 52 GLU A OE1 391 O OE2 . GLU A 52 ? 1.4078 1.4109 1.2965 -0.2725 0.3072 -0.2496 52 GLU A OE2 392 N N . GLY A 53 ? 0.8737 0.8915 0.6816 -0.3533 0.2373 -0.0808 53 GLY A N 393 C CA . GLY A 53 ? 0.8463 0.8384 0.6504 -0.3579 0.2078 -0.0517 53 GLY A CA 394 C C . GLY A 53 ? 0.8626 0.8141 0.6221 -0.3569 0.1828 -0.0430 53 GLY A C 395 O O . GLY A 53 ? 0.8199 0.7435 0.5825 -0.3519 0.1574 -0.0265 53 GLY A O 396 N N . GLY A 54 ? 0.9513 0.9012 0.6702 -0.3617 0.1901 -0.0555 54 GLY A N 397 C CA . GLY A 54 ? 0.8855 0.8020 0.5644 -0.3619 0.1669 -0.0468 54 GLY A CA 398 C C . GLY A 54 ? 0.9694 0.8793 0.6070 -0.3850 0.1546 -0.0188 54 GLY A C 399 O O . GLY A 54 ? 1.3839 1.3102 1.0282 -0.4002 0.1606 -0.0031 54 GLY A O 400 N N . GLN A 55 ? 0.9015 0.7872 0.5009 -0.3879 0.1355 -0.0101 55 GLN A N 401 C CA . GLN A 55 ? 1.0232 0.9005 0.5833 -0.4096 0.1211 0.0188 55 GLN A CA 402 C C . GLN A 55 ? 1.0652 0.9144 0.5948 -0.4067 0.0966 0.0270 55 GLN A C 403 O O . GLN A 55 ? 1.2075 1.0500 0.7386 -0.3922 0.0950 0.0075 55 GLN A O 404 C CB . GLN A 55 ? 1.0119 0.9242 0.5383 -0.4349 0.1439 0.0193 55 GLN A CB 405 C CG . GLN A 55 ? 0.9993 0.9240 0.4873 -0.4382 0.1558 -0.0039 55 GLN A CG 406 C CD . GLN A 55 ? 1.1879 1.1483 0.6335 -0.4655 0.1778 -0.0018 55 GLN A CD 407 O OE1 . GLN A 55 ? 1.2829 1.2667 0.7391 -0.4792 0.1920 0.0116 55 GLN A OE1 408 N NE2 . GLN A 55 ? 1.1167 1.0835 0.5131 -0.4750 0.1805 -0.0147 55 GLN A NE2 409 N N . VAL A 56 ? 1.0682 0.9016 0.5745 -0.4212 0.0766 0.0575 56 VAL A N 410 C CA . VAL A 56 ? 1.0248 0.8338 0.5065 -0.4198 0.0510 0.0708 56 VAL A CA 411 C C . VAL A 56 ? 1.2621 1.0838 0.6920 -0.4475 0.0484 0.0898 56 VAL A C 412 O O . VAL A 56 ? 1.4544 1.2865 0.8736 -0.4679 0.0525 0.1111 56 VAL A O 413 C CB . VAL A 56 ? 0.9520 0.7255 0.4570 -0.4089 0.0245 0.0923 56 VAL A CB 414 C CG1 . VAL A 56 ? 0.9632 0.7146 0.4506 -0.4048 -0.0012 0.1054 56 VAL A CG1 415 C CG2 . VAL A 56 ? 0.9041 0.6685 0.4544 -0.3842 0.0276 0.0745 56 VAL A CG2 416 N N . LEU A 57 ? 1.0429 0.8652 0.4405 -0.4499 0.0405 0.0837 57 LEU A N 417 C CA . LEU A 57 ? 1.1746 1.0128 0.5168 -0.4776 0.0375 0.1003 57 LEU A CA 418 C C . LEU A 57 ? 1.2594 1.0741 0.5928 -0.4779 0.0006 0.1298 57 LEU A C 419 O O . LEU A 57 ? 1.3096 1.0986 0.6600 -0.4610 -0.0172 0.1301 57 LEU A O 420 C CB . LEU A 57 ? 1.1264 0.9898 0.4360 -0.4829 0.0560 0.0680 57 LEU A CB 421 C CG . LEU A 57 ? 1.1199 1.0146 0.4380 -0.4833 0.0944 0.0363 57 LEU A CG 422 C CD1 . LEU A 57 ? 1.0837 0.9689 0.4560 -0.4536 0.1038 0.0063 57 LEU A CD1 423 C CD2 . LEU A 57 ? 1.2765 1.2005 0.5524 -0.4969 0.1089 0.0140 57 LEU A CD2 424 N N . LYS A 58 ? 1.1578 0.9851 0.4749 -0.4935 -0.0110 0.1532 58 LYS A N 425 C CA . LYS A 58 ? 1.1809 0.9918 0.4915 -0.4956 -0.0456 0.1823 58 LYS A CA 426 C C . LYS A 58 ? 1.2226 1.0558 0.4898 -0.5104 -0.0496 0.1769 58 LYS A C 427 O O . LYS A 58 ? 1.3900 1.2535 0.6306 -0.5286 -0.0373 0.1763 58 LYS A O 428 C CB . LYS A 58 ? 1.2043 1.0116 0.5296 -0.5032 -0.0593 0.2150 58 LYS A CB 429 C CG . LYS A 58 ? 1.3764 1.1656 0.7031 -0.5038 -0.0955 0.2468 58 LYS A CG 430 C CD . LYS A 58 ? 1.4725 1.2686 0.8008 -0.5189 -0.1057 0.2780 58 LYS A CD 431 C CE . LYS A 58 ? 1.5362 1.3151 0.9040 -0.5108 -0.1019 0.2849 58 LYS A CE 432 N NZ . LYS A 58 ? 1.5458 1.3535 0.9089 -0.5216 -0.0702 0.2706 58 LYS A NZ 433 N N . CYS A 59 ? 1.2265 1.0463 0.4878 -0.5029 -0.0669 0.1727 59 CYS A N 434 C CA . CYS A 59 ? 1.3776 1.2173 0.6010 -0.5163 -0.0729 0.1645 59 CYS A CA 435 C C . CYS A 59 ? 1.3426 1.1769 0.5614 -0.5240 -0.1088 0.2003 59 CYS A C 436 O O . CYS A 59 ? 1.2989 1.1068 0.5449 -0.5103 -0.1344 0.2191 59 CYS A O 437 C CB . CYS A 59 ? 1.4804 1.3137 0.7005 -0.5050 -0.0691 0.1337 59 CYS A CB 438 S SG . CYS A 59 ? 1.6696 1.5166 0.8899 -0.4989 -0.0255 0.0857 59 CYS A SG 439 N N . ASP A 60 ? 1.4451 1.3059 0.6312 -0.5455 -0.1098 0.2096 60 ASP A N 440 C CA . ASP A 60 ? 1.6018 1.4620 0.7821 -0.5560 -0.1430 0.2454 60 ASP A CA 441 C C . ASP A 60 ? 1.7258 1.5895 0.8886 -0.5583 -0.1615 0.2388 60 ASP A C 442 O O . ASP A 60 ? 2.0141 1.8991 1.1435 -0.5679 -0.1461 0.2106 60 ASP A O 443 C CB . ASP A 60 ? 1.7302 1.6187 0.8814 -0.5799 -0.1366 0.2610 60 ASP A CB 444 C CG . ASP A 60 ? 1.8552 1.7414 1.0057 -0.5908 -0.1716 0.3028 60 ASP A CG 445 O OD1 . ASP A 60 ? 1.9846 1.8982 1.0985 -0.6135 -0.1721 0.3129 60 ASP A OD1 446 O OD2 . ASP A 60 ? 1.8207 1.6782 1.0087 -0.5763 -0.1982 0.3255 60 ASP A OD2 447 N N . TRP A 61 ? 1.5460 1.3891 0.7352 -0.5484 -0.1946 0.2641 61 TRP A N 448 C CA . TRP A 61 ? 1.5384 1.3844 0.7198 -0.5492 -0.2160 0.2616 61 TRP A CA 449 C C . TRP A 61 ? 1.6855 1.5554 0.8335 -0.5730 -0.2333 0.2804 61 TRP A C 450 O O . TRP A 61 ? 1.7593 1.6413 0.8866 -0.5802 -0.2424 0.2690 61 TRP A O 451 C CB . TRP A 61 ? 1.4546 1.2725 0.6830 -0.5278 -0.2444 0.2819 61 TRP A CB 452 C CG . TRP A 61 ? 1.4120 1.2352 0.6400 -0.5278 -0.2682 0.2820 61 TRP A CG 453 C CD1 . TRP A 61 ? 1.3583 1.1833 0.5822 -0.5214 -0.2618 0.2514 61 TRP A CD1 454 C CD2 . TRP A 61 ? 1.4743 1.3029 0.7101 -0.5350 -0.3034 0.3146 61 TRP A CD2 455 N NE1 . TRP A 61 ? 1.3696 1.2017 0.5987 -0.5246 -0.2911 0.2628 61 TRP A NE1 456 C CE2 . TRP A 61 ? 1.4479 1.2829 0.6844 -0.5328 -0.3168 0.3020 61 TRP A CE2 457 C CE3 . TRP A 61 ? 1.7729 1.6022 1.0182 -0.5433 -0.3257 0.3537 61 TRP A CE3 458 C CZ2 . TRP A 61 ? 1.6736 1.5171 0.9203 -0.5386 -0.3512 0.3276 61 TRP A CZ2 459 C CZ3 . TRP A 61 ? 1.9406 1.7772 1.1955 -0.5486 -0.3597 0.3791 61 TRP A CZ3 460 C CH2 . TRP A 61 ? 1.8503 1.6946 1.1060 -0.5463 -0.3720 0.3662 61 TRP A CH2 461 N N . SER A 62 ? 1.7909 1.6676 0.9343 -0.5858 -0.2384 0.3095 62 SER A N 462 C CA . SER A 62 ? 1.9903 1.8877 1.1056 -0.6086 -0.2592 0.3356 62 SER A CA 463 C C . SER A 62 ? 2.2591 2.1868 1.3202 -0.6277 -0.2448 0.3083 62 SER A C 464 O O . SER A 62 ? 2.2719 2.2079 1.3180 -0.6361 -0.2665 0.3131 62 SER A O 465 C CB . SER A 62 ? 1.9698 1.8728 1.0837 -0.6210 -0.2586 0.3653 62 SER A CB 466 O OG . SER A 62 ? 1.9715 1.8945 1.0569 -0.6308 -0.2221 0.3424 62 SER A OG 467 N N . SER A 63 ? 2.4223 2.3667 1.4568 -0.6336 -0.2082 0.2787 63 SER A N 468 C CA . SER A 63 ? 2.4562 2.4281 1.4417 -0.6483 -0.1894 0.2459 63 SER A CA 469 C C . SER A 63 ? 2.4292 2.4121 1.4053 -0.6443 -0.1457 0.2073 63 SER A C 470 O O . SER A 63 ? 2.4008 2.3714 1.4071 -0.6319 -0.1312 0.2087 63 SER A O 471 C CB . SER A 63 ? 2.4457 2.4451 1.3882 -0.6759 -0.2013 0.2697 63 SER A CB 472 O OG . SER A 63 ? 2.3732 2.3666 1.3210 -0.6809 -0.2414 0.2998 63 SER A OG 473 N N . THR A 64 ? 2.3987 2.4044 1.3354 -0.6538 -0.1254 0.1718 64 THR A N 474 C CA . THR A 64 ? 2.3352 2.3573 1.2605 -0.6513 -0.0825 0.1320 64 THR A CA 475 C C . THR A 64 ? 2.1041 2.1041 1.0686 -0.6261 -0.0649 0.1016 64 THR A C 476 O O . THR A 64 ? 2.0895 2.1008 1.0502 -0.6208 -0.0309 0.0625 64 THR A O 477 C CB . THR A 64 ? 1.9091 1.9502 0.8295 -0.6618 -0.0643 0.1504 64 THR A CB 478 O OG1 . THR A 64 ? 1.9985 2.0155 0.9653 -0.6482 -0.0716 0.1755 64 THR A OG1 479 C CG2 . THR A 64 ? 1.8645 1.9280 0.7466 -0.6877 -0.0820 0.1838 64 THR A CG2 480 N N . ARG A 65 ? 1.8784 1.8478 0.8813 -0.6104 -0.0881 0.1195 65 ARG A N 481 C CA . ARG A 65 ? 1.7518 1.6982 0.7927 -0.5869 -0.0758 0.0969 65 ARG A CA 482 C C . ARG A 65 ? 1.7716 1.7255 0.8250 -0.5811 -0.0399 0.0807 65 ARG A C 483 O O . ARG A 65 ? 1.9814 1.9303 1.0512 -0.5668 -0.0166 0.0457 65 ARG A O 484 C CB . ARG A 65 ? 1.8396 1.7830 0.8754 -0.5797 -0.0716 0.0573 65 ARG A CB 485 C CG . ARG A 65 ? 2.0113 1.9494 1.0384 -0.5853 -0.1075 0.0719 65 ARG A CG 486 C CD . ARG A 65 ? 2.0227 1.9367 1.0853 -0.5754 -0.1400 0.1118 65 ARG A CD 487 N NE . ARG A 65 ? 2.1223 2.0434 1.1710 -0.5905 -0.1732 0.1492 65 ARG A NE 488 C CZ . ARG A 65 ? 2.0526 1.9736 1.0989 -0.5937 -0.2007 0.1541 65 ARG A CZ 489 N NH1 . ARG A 65 ? 1.9308 1.8442 0.9878 -0.5830 -0.1992 0.1235 65 ARG A NH1 490 N NH2 . ARG A 65 ? 2.0202 1.9492 1.0566 -0.6078 -0.2306 0.1904 65 ARG A NH2 491 N N . ARG A 66 ? 1.6745 1.6411 0.7236 -0.5925 -0.0365 0.1074 66 ARG A N 492 C CA . ARG A 66 ? 1.6371 1.6172 0.6979 -0.5902 -0.0032 0.0955 66 ARG A CA 493 C C . ARG A 66 ? 1.5533 1.5060 0.6606 -0.5723 -0.0054 0.1078 66 ARG A C 494 O O . ARG A 66 ? 1.5862 1.5156 0.7125 -0.5686 -0.0341 0.1421 66 ARG A O 495 C CB . ARG A 66 ? 1.7905 1.7989 0.8267 -0.6114 0.0016 0.1190 66 ARG A CB 496 C CG . ARG A 66 ? 1.8883 1.9193 0.9338 -0.6116 0.0385 0.1046 66 ARG A CG 497 C CD . ARG A 66 ? 1.9416 2.0036 0.9596 -0.6342 0.0426 0.1287 66 ARG A CD 498 N NE . ARG A 66 ? 1.9912 2.0761 0.9584 -0.6515 0.0400 0.1206 66 ARG A NE 499 C CZ . ARG A 66 ? 2.0277 2.1422 0.9602 -0.6738 0.0419 0.1399 66 ARG A CZ 500 N NH1 . ARG A 66 ? 2.0422 2.1668 0.9879 -0.6814 0.0463 0.1691 66 ARG A NH1 501 N NH2 . ARG A 66 ? 2.0569 2.1911 0.9412 -0.6890 0.0390 0.1303 66 ARG A NH2 502 N N . CYS A 67 ? 1.5012 1.4569 0.6286 -0.5606 0.0252 0.0790 67 CYS A N 503 C CA . CYS A 67 ? 1.4757 1.4075 0.6456 -0.5442 0.0264 0.0872 67 CYS A CA 504 C C . CYS A 67 ? 1.5582 1.5097 0.7432 -0.5486 0.0513 0.0906 67 CYS A C 505 O O . CYS A 67 ? 1.6537 1.6357 0.8282 -0.5536 0.0824 0.0645 67 CYS A O 506 C CB . CYS A 67 ? 1.3775 1.2930 0.5663 -0.5249 0.0378 0.0535 67 CYS A CB 507 S SG . CYS A 67 ? 2.0983 1.9909 1.2777 -0.5179 0.0076 0.0492 67 CYS A SG 508 N N . GLN A 68 ? 1.4728 1.4070 0.6860 -0.5457 0.0373 0.1221 68 GLN A N 509 C CA . GLN A 68 ? 1.5397 1.4903 0.7744 -0.5493 0.0574 0.1282 68 GLN A CA 510 C C . GLN A 68 ? 1.4836 1.4070 0.7653 -0.5313 0.0566 0.1298 68 GLN A C 511 O O . GLN A 68 ? 1.5185 1.4066 0.8163 -0.5202 0.0301 0.1458 68 GLN A O 512 C CB . GLN A 68 ? 1.6532 1.6124 0.8784 -0.5668 0.0414 0.1668 68 GLN A CB 513 C CG . GLN A 68 ? 1.7998 1.7876 0.9769 -0.5869 0.0409 0.1695 68 GLN A CG 514 C CD . GLN A 68 ? 1.9447 1.9750 1.1029 -0.5954 0.0796 0.1404 68 GLN A CD 515 O OE1 . GLN A 68 ? 2.0534 2.0963 1.2387 -0.5894 0.1058 0.1273 68 GLN A OE1 516 N NE2 . GLN A 68 ? 1.9112 1.9647 1.0249 -0.6090 0.0834 0.1297 68 GLN A NE2 517 N N . PRO A 69 ? 1.3973 1.3385 0.7035 -0.5278 0.0857 0.1130 69 PRO A N 518 C CA . PRO A 69 ? 1.1837 1.1032 0.5364 -0.5121 0.0867 0.1126 69 PRO A CA 519 C C . PRO A 69 ? 1.1927 1.0915 0.5706 -0.5133 0.0630 0.1481 69 PRO A C 520 O O . PRO A 69 ? 1.3746 1.2916 0.7465 -0.5285 0.0628 0.1683 69 PRO A O 521 C CB . PRO A 69 ? 1.1537 1.1076 0.5255 -0.5122 0.1246 0.0875 69 PRO A CB 522 C CG . PRO A 69 ? 1.2906 1.2773 0.6240 -0.5217 0.1453 0.0638 69 PRO A CG 523 C CD . PRO A 69 ? 1.4805 1.4651 0.7744 -0.5370 0.1207 0.0895 69 PRO A CD 524 N N . ILE A 70 ? 1.1945 1.0554 0.6011 -0.4969 0.0437 0.1543 70 ILE A N 525 C CA . ILE A 70 ? 1.2311 1.0690 0.6682 -0.4943 0.0228 0.1808 70 ILE A CA 526 C C . ILE A 70 ? 1.2730 1.1233 0.7475 -0.4925 0.0416 0.1728 70 ILE A C 527 O O . ILE A 70 ? 1.4956 1.3459 0.9908 -0.4806 0.0563 0.1494 70 ILE A O 528 C CB . ILE A 70 ? 1.1601 0.9528 0.6152 -0.4754 -0.0050 0.1873 70 ILE A CB 529 C CG1 . ILE A 70 ? 1.1234 0.9070 0.5470 -0.4766 -0.0241 0.1955 70 ILE A CG1 530 C CG2 . ILE A 70 ? 1.0942 0.8621 0.5809 -0.4720 -0.0258 0.2107 70 ILE A CG2 531 C CD1 . ILE A 70 ? 1.0885 0.8319 0.5325 -0.4568 -0.0497 0.2016 70 ILE A CD1 532 N N . GLU A 71 ? 1.2383 1.1002 0.7241 -0.5051 0.0401 0.1937 71 GLU A N 533 C CA . GLU A 71 ? 1.3985 1.2789 0.9207 -0.5067 0.0580 0.1883 71 GLU A CA 534 C C . GLU A 71 ? 1.3778 1.2224 0.9413 -0.4935 0.0377 0.1947 71 GLU A C 535 O O . GLU A 71 ? 1.5162 1.3348 1.0864 -0.4950 0.0130 0.2179 71 GLU A O 536 C CB . GLU A 71 ? 1.6575 1.5713 1.1741 -0.5279 0.0683 0.2072 71 GLU A CB 537 C CG . GLU A 71 ? 1.8843 1.8327 1.4344 -0.5318 0.0954 0.1969 71 GLU A CG 538 C CD . GLU A 71 ? 2.0048 1.9830 1.5525 -0.5252 0.1273 0.1624 71 GLU A CD 539 O OE1 . GLU A 71 ? 2.1655 2.1801 1.6851 -0.5357 0.1501 0.1534 71 GLU A OE1 540 O OE2 . GLU A 71 ? 1.8674 1.8324 1.4420 -0.5093 0.1296 0.1433 71 GLU A OE2 541 N N . PHE A 72 ? 1.1451 0.9887 0.7368 -0.4804 0.0481 0.1727 72 PHE A N 542 C CA . PHE A 72 ? 1.0917 0.9044 0.7208 -0.4672 0.0303 0.1733 72 PHE A CA 543 C C . PHE A 72 ? 1.1468 0.9834 0.8139 -0.4741 0.0424 0.1726 72 PHE A C 544 O O . PHE A 72 ? 1.4752 1.3027 1.1608 -0.4814 0.0288 0.1910 72 PHE A O 545 C CB . PHE A 72 ? 1.1955 0.9867 0.8308 -0.4464 0.0277 0.1508 72 PHE A CB 546 C CG . PHE A 72 ? 1.1954 0.9571 0.8038 -0.4369 0.0101 0.1539 72 PHE A CG 547 C CD1 . PHE A 72 ? 1.2481 1.0237 0.8218 -0.4412 0.0208 0.1468 72 PHE A CD1 548 C CD2 . PHE A 72 ? 1.0883 0.8097 0.7082 -0.4236 -0.0170 0.1626 72 PHE A CD2 549 C CE1 . PHE A 72 ? 1.1828 0.9336 0.7355 -0.4335 0.0029 0.1514 72 PHE A CE1 550 C CE2 . PHE A 72 ? 0.9955 0.6931 0.5970 -0.4141 -0.0327 0.1664 72 PHE A CE2 551 C CZ . PHE A 72 ? 1.0318 0.7448 0.6007 -0.4195 -0.0238 0.1623 72 PHE A CZ 552 N N . ASP A 73 ? 1.0561 0.9236 0.7382 -0.4720 0.0678 0.1516 73 ASP A N 553 C CA . ASP A 73 ? 1.0861 0.9797 0.8116 -0.4766 0.0791 0.1494 73 ASP A CA 554 C C . ASP A 73 ? 1.1890 1.1307 0.9140 -0.4957 0.1039 0.1576 73 ASP A C 555 O O . ASP A 73 ? 1.3071 1.2566 1.0503 -0.5082 0.0984 0.1775 73 ASP A O 556 C CB . ASP A 73 ? 1.1674 1.0708 0.9192 -0.4627 0.0922 0.1233 73 ASP A CB 557 C CG . ASP A 73 ? 1.3879 1.3075 1.1911 -0.4638 0.0923 0.1232 73 ASP A CG 558 O OD1 . ASP A 73 ? 1.7222 1.6216 1.5470 -0.4502 0.0785 0.1132 73 ASP A OD1 559 O OD2 . ASP A 73 ? 1.2980 1.2526 1.1206 -0.4785 0.1055 0.1334 73 ASP A OD2 560 N N . ALA A 74 ? 1.1956 1.1700 0.9017 -0.4972 0.1321 0.1402 74 ALA A N 561 C CA . ALA A 74 ? 1.2335 1.2574 0.9331 -0.5128 0.1601 0.1425 74 ALA A CA 562 C C . ALA A 74 ? 1.0862 1.1490 0.8395 -0.5170 0.1782 0.1414 74 ALA A C 563 O O . ALA A 74 ? 1.0391 1.1481 0.7952 -0.5276 0.2053 0.1406 74 ALA A O 564 C CB . ALA A 74 ? 1.1227 1.1409 0.7892 -0.5294 0.1466 0.1714 74 ALA A CB 565 N N . THR A 75 ? 0.9805 1.0267 0.7771 -0.5086 0.1630 0.1410 75 THR A N 566 C CA . THR A 75 ? 1.1241 1.2063 0.9772 -0.5132 0.1749 0.1426 75 THR A CA 567 C C . THR A 75 ? 1.0766 1.1820 0.9677 -0.4989 0.1934 0.1154 75 THR A C 568 O O . THR A 75 ? 0.9117 1.0043 0.7839 -0.4861 0.1990 0.0943 75 THR A O 569 C CB . THR A 75 ? 1.1701 1.2228 1.0519 -0.5163 0.1432 0.1619 75 THR A CB 570 O OG1 . THR A 75 ? 0.9349 0.9437 0.8173 -0.4995 0.1192 0.1510 75 THR A OG1 571 C CG2 . THR A 75 ? 1.3012 1.3311 1.1544 -0.5302 0.1254 0.1893 75 THR A CG2 572 N N . GLY A 76 ? 1.0873 1.2271 1.0362 -0.5015 0.2016 0.1170 76 GLY A N 573 C CA . GLY A 76 ? 0.9310 1.0957 0.9281 -0.4882 0.2159 0.0948 76 GLY A CA 574 C C . GLY A 76 ? 0.8480 0.9698 0.8575 -0.4775 0.1830 0.0942 76 GLY A C 575 O O . GLY A 76 ? 0.8526 0.9240 0.8214 -0.4747 0.1575 0.1007 76 GLY A O 576 N N . ASN A 77 ? 0.8183 0.9595 0.8840 -0.4672 0.1815 0.0856 77 ASN A N 577 C CA . ASN A 77 ? 1.1400 1.2402 1.2114 -0.4518 0.1476 0.0840 77 ASN A CA 578 C C . ASN A 77 ? 1.1064 1.1934 1.1958 -0.4702 0.1200 0.1052 77 ASN A C 579 O O . ASN A 77 ? 1.3753 1.4198 1.4281 -0.4736 0.0980 0.1167 77 ASN A O 580 C CB . ASN A 77 ? 0.9660 1.0871 1.0852 -0.4255 0.1522 0.0651 77 ASN A CB 581 C CG . ASN A 77 ? 1.0175 1.1574 1.1330 -0.4074 0.1822 0.0420 77 ASN A CG 582 O OD1 . ASN A 77 ? 0.8140 0.9230 0.9015 -0.3882 0.1765 0.0281 77 ASN A OD1 583 N ND2 . ASN A 77 ? 1.2777 1.4693 1.4234 -0.4135 0.2150 0.0365 77 ASN A ND2 584 N N . ARG A 78 ? 0.8180 0.9426 0.9673 -0.4745 0.1205 0.1086 78 ARG A N 585 C CA . ARG A 78 ? 0.9005 1.0173 1.0758 -0.4847 0.0934 0.1247 78 ARG A CA 586 C C . ARG A 78 ? 0.9713 1.1372 1.2182 -0.4852 0.0964 0.1236 78 ARG A C 587 O O . ARG A 78 ? 1.1799 1.3781 1.4544 -0.4696 0.1165 0.1091 78 ARG A O 588 C CB . ARG A 78 ? 0.9149 0.9701 1.0580 -0.4772 0.0559 0.1233 78 ARG A CB 589 C CG . ARG A 78 ? 0.9336 0.9527 1.0487 -0.4878 0.0381 0.1384 78 ARG A CG 590 C CD . ARG A 78 ? 0.8851 0.8418 0.9551 -0.4757 0.0115 0.1319 78 ARG A CD 591 N NE . ARG A 78 ? 0.8814 0.8185 0.9038 -0.4670 0.0229 0.1274 78 ARG A NE 592 C CZ . ARG A 78 ? 1.1244 1.0113 1.1068 -0.4563 0.0047 0.1241 78 ARG A CZ 593 N NH1 . ARG A 78 ? 0.8621 0.7127 0.8443 -0.4523 -0.0234 0.1224 78 ARG A NH1 594 N NH2 . ARG A 78 ? 1.3844 1.2590 1.3280 -0.4496 0.0151 0.1214 78 ARG A NH2 595 N N . ASP A 79 ? 0.8572 1.0260 1.1360 -0.4958 0.0750 0.1366 79 ASP A N 596 C CA . ASP A 79 ? 0.8638 1.0795 1.2136 -0.4965 0.0726 0.1381 79 ASP A CA 597 C C . ASP A 79 ? 0.8618 1.0496 1.2208 -0.4975 0.0313 0.1408 79 ASP A C 598 O O . ASP A 79 ? 1.2051 1.3604 1.5438 -0.5083 0.0111 0.1486 79 ASP A O 599 C CB . ASP A 79 ? 1.2370 1.5072 1.6335 -0.5111 0.0966 0.1506 79 ASP A CB 600 C CG . ASP A 79 ? 1.3204 1.6396 1.7304 -0.5059 0.1414 0.1420 79 ASP A CG 601 O OD1 . ASP A 79 ? 1.4852 1.8650 1.9625 -0.5049 0.1609 0.1417 79 ASP A OD1 602 O OD2 . ASP A 79 ? 1.1965 1.4948 1.5507 -0.5018 0.1574 0.1339 79 ASP A OD2 603 N N . TYR A 80 ? 0.8221 1.0229 1.2106 -0.4858 0.0185 0.1339 80 TYR A N 604 C CA . TYR A 80 ? 0.7601 0.9467 1.1626 -0.4866 -0.0194 0.1356 80 TYR A CA 605 C C . TYR A 80 ? 0.7734 1.0112 1.2443 -0.4986 -0.0209 0.1471 80 TYR A C 606 O O . TYR A 80 ? 0.7908 1.0149 1.2658 -0.5084 -0.0496 0.1516 80 TYR A O 607 C CB . TYR A 80 ? 0.8031 0.9840 1.2066 -0.4681 -0.0340 0.1263 80 TYR A CB 608 C CG . TYR A 80 ? 0.7398 0.9113 1.1541 -0.4691 -0.0734 0.1277 80 TYR A CG 609 C CD1 . TYR A 80 ? 0.8822 0.9964 1.2401 -0.4707 -0.1016 0.1205 80 TYR A CD1 610 C CD2 . TYR A 80 ? 0.7262 0.9470 1.2065 -0.4664 -0.0819 0.1350 80 TYR A CD2 611 C CE1 . TYR A 80 ? 0.9441 1.0508 1.3052 -0.4721 -0.1364 0.1189 80 TYR A CE1 612 C CE2 . TYR A 80 ? 0.9731 1.1866 1.4572 -0.4678 -0.1191 0.1364 80 TYR A CE2 613 C CZ . TYR A 80 ? 1.0205 1.1769 1.4419 -0.4718 -0.1459 0.1275 80 TYR A CZ 614 O OH . TYR A 80 ? 1.1875 1.3379 1.6073 -0.4746 -0.1821 0.1267 80 TYR A OH 615 N N . ALA A 81 ? 0.7703 1.0682 1.2952 -0.4973 0.0110 0.1504 81 ALA A N 616 C CA . ALA A 81 ? 0.8112 1.1660 1.4086 -0.5061 0.0151 0.1606 81 ALA A CA 617 C C . ALA A 81 ? 0.9406 1.3483 1.5715 -0.5089 0.0616 0.1624 81 ALA A C 618 O O . ALA A 81 ? 0.9429 1.3355 1.5295 -0.5086 0.0862 0.1577 81 ALA A O 619 C CB . ALA A 81 ? 0.8462 1.2311 1.4980 -0.4928 -0.0040 0.1606 81 ALA A CB 620 N N . LYS A 82 ? 1.0341 1.5040 1.7399 -0.5117 0.0734 0.1684 82 LYS A N 621 C CA . LYS A 82 ? 1.0691 1.5962 1.8129 -0.5139 0.1202 0.1679 82 LYS A CA 622 C C . LYS A 82 ? 1.1703 1.7047 1.8970 -0.4972 0.1535 0.1532 82 LYS A C 623 O O . LYS A 82 ? 1.4266 1.9447 2.1009 -0.5029 0.1766 0.1506 82 LYS A O 624 C CB . LYS A 82 ? 1.0663 1.6624 1.9008 -0.5113 0.1260 0.1718 82 LYS A CB 625 C CG . LYS A 82 ? 1.1501 1.7495 2.0042 -0.5323 0.1006 0.1868 82 LYS A CG 626 C CD . LYS A 82 ? 1.1123 1.7872 2.0555 -0.5315 0.1134 0.1914 82 LYS A CD 627 C CE . LYS A 82 ? 1.1216 1.8007 2.0831 -0.5554 0.0900 0.2074 82 LYS A CE 628 N NZ . LYS A 82 ? 1.1542 1.9096 2.2032 -0.5560 0.1035 0.2130 82 LYS A NZ 629 N N . ASP A 83 ? 0.9428 1.5001 1.7128 -0.4751 0.1545 0.1447 83 ASP A N 630 C CA . ASP A 83 ? 0.8716 1.3946 1.5913 -0.4479 0.1708 0.1212 83 ASP A CA 631 C C . ASP A 83 ? 0.7948 1.2661 1.4881 -0.4296 0.1318 0.1172 83 ASP A C 632 O O . ASP A 83 ? 0.8827 1.3717 1.6275 -0.4087 0.1213 0.1150 83 ASP A O 633 C CB . ASP A 83 ? 0.9677 1.5416 1.7428 -0.4232 0.2117 0.1030 83 ASP A CB 634 C CG . ASP A 83 ? 1.3218 1.9530 2.1216 -0.4406 0.2549 0.1045 83 ASP A CG 635 O OD1 . ASP A 83 ? 1.5552 2.1708 2.2968 -0.4660 0.2625 0.1125 83 ASP A OD1 636 O OD2 . ASP A 83 ? 1.3373 2.0308 2.2163 -0.4287 0.2815 0.0985 83 ASP A OD2 637 N N . ASP A 84 ? 0.7462 1.1549 1.3600 -0.4375 0.1111 0.1172 84 ASP A N 638 C CA . ASP A 84 ? 0.7024 1.0591 1.2773 -0.4200 0.0797 0.1108 84 ASP A CA 639 C C . ASP A 84 ? 0.6946 0.9916 1.1807 -0.4212 0.0799 0.1024 84 ASP A C 640 O O . ASP A 84 ? 0.8018 1.0599 1.2467 -0.4389 0.0545 0.1111 84 ASP A O 641 C CB . ASP A 84 ? 0.7275 1.0761 1.3186 -0.4333 0.0359 0.1258 84 ASP A CB 642 C CG . ASP A 84 ? 0.9425 1.2664 1.5252 -0.4102 0.0089 0.1203 84 ASP A CG 643 O OD1 . ASP A 84 ? 1.2174 1.5056 1.7531 -0.3899 0.0157 0.1063 84 ASP A OD1 644 O OD2 . ASP A 84 ? 0.9121 1.2546 1.5357 -0.4138 -0.0199 0.1314 84 ASP A OD2 645 N N . PRO A 85 ? 0.6787 0.9682 1.1377 -0.4031 0.1078 0.0854 85 PRO A N 646 C CA . PRO A 85 ? 0.7007 0.9391 1.0793 -0.4055 0.1091 0.0793 85 PRO A CA 647 C C . PRO A 85 ? 0.7053 0.8867 1.0383 -0.4024 0.0714 0.0813 85 PRO A C 648 O O . PRO A 85 ? 0.8008 0.9734 1.1447 -0.3833 0.0545 0.0763 85 PRO A O 649 C CB . PRO A 85 ? 0.7647 1.0062 1.1347 -0.3807 0.1377 0.0579 85 PRO A CB 650 C CG . PRO A 85 ? 0.7816 1.0619 1.2250 -0.3604 0.1423 0.0526 85 PRO A CG 651 C CD . PRO A 85 ? 0.7865 1.1114 1.2897 -0.3787 0.1365 0.0700 85 PRO A CD 652 N N . LEU A 86 ? 0.7568 0.9012 1.0406 -0.4214 0.0590 0.0892 86 LEU A N 653 C CA . LEU A 86 ? 0.7874 0.8786 1.0301 -0.4205 0.0246 0.0895 86 LEU A CA 654 C C . LEU A 86 ? 0.8294 0.8790 1.0159 -0.4006 0.0275 0.0761 86 LEU A C 655 O O . LEU A 86 ? 0.8808 0.8900 1.0348 -0.3927 0.0037 0.0721 86 LEU A O 656 C CB . LEU A 86 ? 0.9834 1.0521 1.2080 -0.4497 0.0081 0.1041 86 LEU A CB 657 C CG . LEU A 86 ? 0.9981 1.0112 1.1848 -0.4522 -0.0276 0.1027 86 LEU A CG 658 C CD1 . LEU A 86 ? 1.0670 1.0833 1.2733 -0.4388 -0.0508 0.0958 86 LEU A CD1 659 C CD2 . LEU A 86 ? 1.3611 1.3610 1.5478 -0.4674 -0.0402 0.1135 86 LEU A CD2 660 N N . GLU A 87 ? 0.7938 0.8554 0.9691 -0.3936 0.0572 0.0684 87 GLU A N 661 C CA . GLU A 87 ? 0.7423 0.7709 0.8712 -0.3751 0.0614 0.0556 87 GLU A CA 662 C C . GLU A 87 ? 0.7883 0.8452 0.9267 -0.3645 0.0952 0.0428 87 GLU A C 663 O O . GLU A 87 ? 0.6984 0.7981 0.8707 -0.3738 0.1180 0.0440 87 GLU A O 664 C CB . GLU A 87 ? 0.7214 0.7057 0.7926 -0.3872 0.0510 0.0617 87 GLU A CB 665 C CG . GLU A 87 ? 0.7487 0.7455 0.8128 -0.4138 0.0636 0.0756 87 GLU A CG 666 C CD . GLU A 87 ? 0.8341 0.7835 0.8457 -0.4243 0.0489 0.0847 87 GLU A CD 667 O OE1 . GLU A 87 ? 0.7977 0.7528 0.7915 -0.4435 0.0609 0.0969 87 GLU A OE1 668 O OE2 . GLU A 87 ? 0.9748 0.8825 0.9640 -0.4132 0.0254 0.0803 87 GLU A OE2 669 N N . PHE A 88 ? 0.8319 0.8664 0.9429 -0.3451 0.0989 0.0293 88 PHE A N 670 C CA . PHE A 88 ? 0.6799 0.7350 0.7964 -0.3345 0.1289 0.0130 88 PHE A CA 671 C C . PHE A 88 ? 0.7788 0.8016 0.8349 -0.3332 0.1330 0.0059 88 PHE A C 672 O O . PHE A 88 ? 1.0254 1.0140 1.0567 -0.3195 0.1172 0.0024 88 PHE A O 673 C CB . PHE A 88 ? 0.6558 0.7237 0.8169 -0.3097 0.1304 0.0019 88 PHE A CB 674 C CG . PHE A 88 ? 0.6443 0.7394 0.8634 -0.3095 0.1177 0.0126 88 PHE A CG 675 C CD1 . PHE A 88 ? 0.6462 0.7906 0.9221 -0.3137 0.1375 0.0125 88 PHE A CD1 676 C CD2 . PHE A 88 ? 0.6347 0.7085 0.8514 -0.3058 0.0859 0.0225 88 PHE A CD2 677 C CE1 . PHE A 88 ? 0.6365 0.8085 0.9697 -0.3143 0.1234 0.0242 88 PHE A CE1 678 C CE2 . PHE A 88 ? 0.6281 0.7281 0.8957 -0.3076 0.0711 0.0333 88 PHE A CE2 679 C CZ . PHE A 88 ? 0.6279 0.7771 0.9557 -0.3120 0.0887 0.0352 88 PHE A CZ 680 N N . LYS A 89 ? 0.7687 0.8054 0.8016 -0.3485 0.1542 0.0049 89 LYS A N 681 C CA . LYS A 89 ? 0.7527 0.7635 0.7276 -0.3509 0.1570 0.0004 89 LYS A CA 682 C C . LYS A 89 ? 0.7538 0.7756 0.7290 -0.3357 0.1797 -0.0240 89 LYS A C 683 O O . LYS A 89 ? 0.9031 0.9046 0.8336 -0.3353 0.1809 -0.0310 89 LYS A O 684 C CB . LYS A 89 ? 1.0248 1.0435 0.9677 -0.3784 0.1649 0.0152 89 LYS A CB 685 C CG . LYS A 89 ? 1.1421 1.1497 1.0895 -0.3967 0.1436 0.0396 89 LYS A CG 686 C CD . LYS A 89 ? 1.3020 1.2570 1.2092 -0.3956 0.1142 0.0495 89 LYS A CD 687 C CE . LYS A 89 ? 1.4190 1.3587 1.3312 -0.4149 0.0931 0.0714 89 LYS A CE 688 N NZ . LYS A 89 ? 1.2197 1.1856 1.1297 -0.4432 0.1075 0.0886 89 LYS A NZ 689 N N . SER A 90 ? 0.8452 0.8987 0.8738 -0.3233 0.1964 -0.0372 90 SER A N 690 C CA . SER A 90 ? 0.8962 0.9600 0.9332 -0.3084 0.2194 -0.0635 90 SER A CA 691 C C . SER A 90 ? 0.8631 0.8902 0.8897 -0.2885 0.2027 -0.0715 90 SER A C 692 O O . SER A 90 ? 0.8201 0.8355 0.8744 -0.2754 0.1832 -0.0635 90 SER A O 693 C CB . SER A 90 ? 0.8961 1.0022 1.0026 -0.2980 0.2402 -0.0746 90 SER A CB 694 O OG . SER A 90 ? 0.9516 1.0977 1.0704 -0.3170 0.2595 -0.0681 90 SER A OG 695 N N . HIS A 91 ? 0.8950 0.9062 0.8807 -0.2880 0.2103 -0.0862 91 HIS A N 696 C CA . HIS A 91 ? 0.8542 0.8321 0.8277 -0.2721 0.1960 -0.0933 91 HIS A CA 697 C C . HIS A 91 ? 0.7830 0.7300 0.7392 -0.2706 0.1647 -0.0717 91 HIS A C 698 O O . HIS A 91 ? 0.7002 0.6300 0.6719 -0.2543 0.1506 -0.0711 91 HIS A O 699 C CB . HIS A 91 ? 0.7447 0.7307 0.7744 -0.2500 0.2036 -0.1092 91 HIS A CB 700 C CG . HIS A 91 ? 0.7664 0.7830 0.8222 -0.2480 0.2359 -0.1341 91 HIS A CG 701 N ND1 . HIS A 91 ? 0.8095 0.8192 0.8436 -0.2457 0.2519 -0.1604 91 HIS A ND1 702 C CD2 . HIS A 91 ? 0.8816 0.9372 0.9850 -0.2477 0.2559 -0.1385 91 HIS A CD2 703 C CE1 . HIS A 91 ? 0.8521 0.8938 0.9169 -0.2432 0.2818 -0.1822 91 HIS A CE1 704 N NE2 . HIS A 91 ? 0.9001 0.9717 1.0095 -0.2438 0.2856 -0.1687 91 HIS A NE2 705 N N . GLN A 92 ? 0.7244 0.6645 0.6490 -0.2880 0.1545 -0.0541 92 GLN A N 706 C CA . GLN A 92 ? 0.7321 0.6431 0.6415 -0.2870 0.1266 -0.0363 92 GLN A CA 707 C C . GLN A 92 ? 0.7505 0.6293 0.6175 -0.2831 0.1144 -0.0365 92 GLN A C 708 O O . GLN A 92 ? 0.7988 0.6523 0.6531 -0.2788 0.0932 -0.0253 92 GLN A O 709 C CB . GLN A 92 ? 0.7506 0.6637 0.6492 -0.3071 0.1192 -0.0179 92 GLN A CB 710 C CG . GLN A 92 ? 0.7335 0.6426 0.5866 -0.3265 0.1249 -0.0116 92 GLN A CG 711 C CD . GLN A 92 ? 0.9417 0.8504 0.7895 -0.3474 0.1160 0.0097 92 GLN A CD 712 O OE1 . GLN A 92 ? 0.8583 0.7595 0.7286 -0.3464 0.0999 0.0187 92 GLN A OE1 713 N NE2 . GLN A 92 ? 1.3016 1.2184 1.1188 -0.3679 0.1255 0.0185 92 GLN A NE2 714 N N . TRP A 93 ? 0.7644 0.6459 0.6109 -0.2847 0.1281 -0.0504 93 TRP A N 715 C CA . TRP A 93 ? 0.8482 0.7040 0.6577 -0.2826 0.1169 -0.0508 93 TRP A CA 716 C C . TRP A 93 ? 0.8900 0.7258 0.6626 -0.2951 0.0993 -0.0307 93 TRP A C 717 O O . TRP A 93 ? 0.9182 0.7288 0.6802 -0.2868 0.0805 -0.0230 93 TRP A O 718 C CB . TRP A 93 ? 0.8015 0.6406 0.6306 -0.2621 0.1046 -0.0537 93 TRP A CB 719 C CG . TRP A 93 ? 0.7157 0.5629 0.5691 -0.2506 0.1181 -0.0737 93 TRP A CG 720 C CD1 . TRP A 93 ? 0.9417 0.8113 0.8357 -0.2449 0.1354 -0.0865 93 TRP A CD1 721 C CD2 . TRP A 93 ? 0.7127 0.5443 0.5565 -0.2432 0.1143 -0.0831 93 TRP A CD2 722 N NE1 . TRP A 93 ? 0.9765 0.8419 0.8864 -0.2338 0.1426 -0.1044 93 TRP A NE1 723 C CE2 . TRP A 93 ? 0.8031 0.6452 0.6818 -0.2338 0.1294 -0.1024 93 TRP A CE2 724 C CE3 . TRP A 93 ? 0.7446 0.5551 0.5579 -0.2438 0.0990 -0.0767 93 TRP A CE3 725 C CZ2 . TRP A 93 ? 0.8341 0.6634 0.7160 -0.2266 0.1288 -0.1157 93 TRP A CZ2 726 C CZ3 . TRP A 93 ? 0.7095 0.5115 0.5265 -0.2372 0.0986 -0.0887 93 TRP A CZ3 727 C CH2 . TRP A 93 ? 0.7237 0.5337 0.5737 -0.2295 0.1130 -0.1082 93 TRP A CH2 728 N N . PHE A 94 ? 0.9626 0.8103 0.7186 -0.3150 0.1057 -0.0211 94 PHE A N 729 C CA . PHE A 94 ? 1.0755 0.9023 0.7996 -0.3282 0.0881 0.0002 94 PHE A CA 730 C C . PHE A 94 ? 1.1200 0.9356 0.8030 -0.3332 0.0835 0.0009 94 PHE A C 731 O O . PHE A 94 ? 1.1970 1.0314 0.8598 -0.3436 0.0996 -0.0089 94 PHE A O 732 C CB . PHE A 94 ? 1.0026 0.8461 0.7246 -0.3502 0.0951 0.0144 94 PHE A CB 733 C CG . PHE A 94 ? 0.9072 0.7289 0.5962 -0.3664 0.0778 0.0383 94 PHE A CG 734 C CD1 . PHE A 94 ? 0.8285 0.6181 0.5231 -0.3612 0.0535 0.0517 94 PHE A CD1 735 C CD2 . PHE A 94 ? 0.9339 0.7669 0.5863 -0.3867 0.0852 0.0472 94 PHE A CD2 736 C CE1 . PHE A 94 ? 0.9605 0.7269 0.6310 -0.3746 0.0365 0.0740 94 PHE A CE1 737 C CE2 . PHE A 94 ? 0.8843 0.6963 0.5096 -0.4019 0.0669 0.0731 94 PHE A CE2 738 C CZ . PHE A 94 ? 0.9380 0.7153 0.5755 -0.3950 0.0422 0.0867 94 PHE A CZ 739 N N . GLY A 95 ? 0.9799 0.7664 0.6511 -0.3261 0.0612 0.0119 95 GLY A N 740 C CA . GLY A 95 ? 1.0179 0.7938 0.6566 -0.3290 0.0523 0.0146 95 GLY A CA 741 C C . GLY A 95 ? 0.9259 0.6933 0.5772 -0.3090 0.0480 0.0007 95 GLY A C 742 O O . GLY A 95 ? 0.9017 0.6623 0.5323 -0.3097 0.0398 0.0007 95 GLY A O 743 N N . ALA A 96 ? 0.8316 0.6010 0.5182 -0.2926 0.0523 -0.0093 96 ALA A N 744 C CA . ALA A 96 ? 0.8251 0.5875 0.5282 -0.2743 0.0483 -0.0191 96 ALA A CA 745 C C . ALA A 96 ? 0.9397 0.6795 0.6342 -0.2664 0.0275 -0.0058 96 ALA A C 746 O O . ALA A 96 ? 1.3594 1.0949 1.0576 -0.2566 0.0224 -0.0098 96 ALA A O 747 C CB . ALA A 96 ? 0.9099 0.6799 0.6518 -0.2602 0.0547 -0.0266 96 ALA A CB 748 N N . SER A 97 ? 0.7306 0.4564 0.4177 -0.2705 0.0157 0.0099 97 SER A N 749 C CA . SER A 97 ? 0.8599 0.5637 0.5409 -0.2628 -0.0032 0.0221 97 SER A CA 750 C C . SER A 97 ? 0.8751 0.5660 0.5342 -0.2782 -0.0145 0.0405 97 SER A C 751 O O . SER A 97 ? 1.0127 0.7006 0.6734 -0.2876 -0.0139 0.0471 97 SER A O 752 C CB . SER A 97 ? 0.9846 0.6777 0.6879 -0.2455 -0.0089 0.0206 97 SER A CB 753 O OG . SER A 97 ? 1.1442 0.8337 0.8529 -0.2517 -0.0091 0.0237 97 SER A OG 754 N N . VAL A 98 ? 0.8480 0.5317 0.4892 -0.2818 -0.0265 0.0508 98 VAL A N 755 C CA . VAL A 98 ? 0.8168 0.4880 0.4377 -0.2973 -0.0399 0.0725 98 VAL A CA 756 C C . VAL A 98 ? 0.8817 0.5311 0.5076 -0.2862 -0.0613 0.0860 98 VAL A C 757 O O . VAL A 98 ? 0.9764 0.6310 0.6027 -0.2786 -0.0662 0.0835 98 VAL A O 758 C CB . VAL A 98 ? 0.8454 0.5351 0.4335 -0.3193 -0.0340 0.0766 98 VAL A CB 759 C CG1 . VAL A 98 ? 0.8849 0.5619 0.4512 -0.3362 -0.0509 0.1045 98 VAL A CG1 760 C CG2 . VAL A 98 ? 1.2678 0.9812 0.8539 -0.3300 -0.0103 0.0629 98 VAL A CG2 761 N N . ARG A 99 ? 0.8502 0.4754 0.4838 -0.2851 -0.0744 0.0998 99 ARG A N 762 C CA . ARG A 99 ? 0.8911 0.4939 0.5352 -0.2732 -0.0946 0.1128 99 ARG A CA 763 C C . ARG A 99 ? 0.9131 0.4949 0.5485 -0.2886 -0.1110 0.1383 99 ARG A C 764 O O . ARG A 99 ? 0.9877 0.5643 0.6190 -0.3025 -0.1072 0.1429 99 ARG A O 765 C CB . ARG A 99 ? 0.9845 0.5729 0.6565 -0.2486 -0.0949 0.0993 99 ARG A CB 766 C CG . ARG A 99 ? 1.1639 0.7386 0.8533 -0.2303 -0.1097 0.1054 99 ARG A CG 767 C CD . ARG A 99 ? 1.3064 0.9019 1.0074 -0.2144 -0.1015 0.0919 99 ARG A CD 768 N NE . ARG A 99 ? 1.5102 1.1298 1.1942 -0.2278 -0.0961 0.0917 99 ARG A NE 769 C CZ . ARG A 99 ? 1.5742 1.2126 1.2670 -0.2195 -0.0896 0.0814 99 ARG A CZ 770 N NH1 . ARG A 99 ? 1.5854 1.2250 1.3032 -0.1984 -0.0865 0.0731 99 ARG A NH1 771 N NH2 . ARG A 99 ? 1.5078 1.1641 1.1839 -0.2333 -0.0860 0.0788 99 ARG A NH2 772 N N . SER A 100 ? 0.9303 0.5007 0.5662 -0.2867 -0.1304 0.1571 100 SER A N 773 C CA . SER A 100 ? 0.9744 0.5235 0.6044 -0.3017 -0.1492 0.1862 100 SER A CA 774 C C . SER A 100 ? 1.1039 0.6251 0.7616 -0.2837 -0.1717 0.1990 100 SER A C 775 O O . SER A 100 ? 1.5308 1.0607 1.1972 -0.2713 -0.1789 0.1998 100 SER A O 776 C CB . SER A 100 ? 1.0376 0.6075 0.6310 -0.3278 -0.1521 0.2051 100 SER A CB 777 O OG . SER A 100 ? 1.4071 0.9642 1.0015 -0.3366 -0.1739 0.2348 100 SER A OG 778 N N . LYS A 101 ? 1.0233 0.5114 0.6984 -0.2822 -0.1829 0.2084 101 LYS A N 779 C CA . LYS A 101 ? 1.1630 0.6236 0.8693 -0.2647 -0.2044 0.2208 101 LYS A CA 780 C C . LYS A 101 ? 1.2406 0.6967 0.9506 -0.2773 -0.2208 0.2471 101 LYS A C 781 O O . LYS A 101 ? 1.2096 0.6588 0.9223 -0.2854 -0.2174 0.2462 101 LYS A O 782 C CB . LYS A 101 ? 1.3056 0.7375 1.0417 -0.2409 -0.2015 0.1982 101 LYS A CB 783 C CG . LYS A 101 ? 1.4472 0.8468 1.2199 -0.2214 -0.2220 0.2080 101 LYS A CG 784 C CD . LYS A 101 ? 1.3778 0.7505 1.1756 -0.1977 -0.2164 0.1800 101 LYS A CD 785 C CE . LYS A 101 ? 1.4089 0.7472 1.2466 -0.1773 -0.2356 0.1875 101 LYS A CE 786 N NZ . LYS A 101 ? 1.5828 0.9376 1.4385 -0.1631 -0.2439 0.2001 101 LYS A NZ 787 N N . GLN A 102 ? 1.3022 0.7636 1.0139 -0.2797 -0.2396 0.2716 102 GLN A N 788 C CA . GLN A 102 ? 1.2747 0.7346 0.9897 -0.2928 -0.2574 0.3002 102 GLN A CA 789 C C . GLN A 102 ? 1.2784 0.7623 0.9587 -0.3213 -0.2455 0.3058 102 GLN A C 790 O O . GLN A 102 ? 1.4555 0.9704 1.0992 -0.3375 -0.2342 0.3037 102 GLN A O 791 C CB . GLN A 102 ? 1.2698 0.6917 1.0274 -0.2761 -0.2697 0.3018 102 GLN A CB 792 C CG . GLN A 102 ? 1.3943 0.7937 1.1911 -0.2469 -0.2822 0.2984 102 GLN A CG 793 C CD . GLN A 102 ? 1.7716 1.1311 1.6087 -0.2273 -0.2871 0.2871 102 GLN A CD 794 O OE1 . GLN A 102 ? 1.9802 1.3271 1.8146 -0.2264 -0.2733 0.2646 102 GLN A OE1 795 N NE2 . GLN A 102 ? 1.8595 1.1998 1.7352 -0.2114 -0.3071 0.3017 102 GLN A NE2 796 N N . ASP A 103 ? 1.2024 0.6723 0.8957 -0.3272 -0.2476 0.3120 103 ASP A N 797 C CA . ASP A 103 ? 1.2186 0.7123 0.8855 -0.3537 -0.2366 0.3199 103 ASP A CA 798 C C . ASP A 103 ? 1.1358 0.6371 0.7966 -0.3550 -0.2115 0.2927 103 ASP A C 799 O O . ASP A 103 ? 1.1407 0.6662 0.7819 -0.3753 -0.1978 0.2947 103 ASP A O 800 C CB . ASP A 103 ? 1.3263 0.8039 1.0123 -0.3625 -0.2532 0.3449 103 ASP A CB 801 C CG . ASP A 103 ? 1.5568 1.0660 1.2116 -0.3926 -0.2512 0.3678 103 ASP A CG 802 O OD1 . ASP A 103 ? 1.5659 1.1051 1.1910 -0.4074 -0.2289 0.3561 103 ASP A OD1 803 O OD2 . ASP A 103 ? 1.6296 1.1344 1.2907 -0.4013 -0.2716 0.3973 103 ASP A OD2 804 N N . LYS A 104 ? 1.1032 0.5857 0.7825 -0.3334 -0.2057 0.2676 104 LYS A N 805 C CA . LYS A 104 ? 1.0705 0.5602 0.7479 -0.3328 -0.1845 0.2416 104 LYS A CA 806 C C . LYS A 104 ? 1.3884 0.9056 1.0399 -0.3348 -0.1656 0.2253 104 LYS A C 807 O O . LYS A 104 ? 1.5458 1.0619 1.1929 -0.3247 -0.1699 0.2234 104 LYS A O 808 C CB . LYS A 104 ? 1.0587 0.5148 0.7672 -0.3097 -0.1880 0.2212 104 LYS A CB 809 C CG . LYS A 104 ? 1.1593 0.5808 0.8979 -0.3027 -0.2081 0.2330 104 LYS A CG 810 C CD . LYS A 104 ? 1.1197 0.5426 0.8624 -0.3213 -0.2080 0.2423 104 LYS A CD 811 C CE . LYS A 104 ? 1.1617 0.5470 0.9363 -0.3147 -0.2285 0.2533 104 LYS A CE 812 N NZ . LYS A 104 ? 1.1895 0.5760 0.9696 -0.3350 -0.2302 0.2659 104 LYS A NZ 813 N N . ILE A 105 ? 1.2186 0.7608 0.8566 -0.3479 -0.1450 0.2138 105 ILE A N 814 C CA . ILE A 105 ? 1.0722 0.6375 0.6919 -0.3483 -0.1250 0.1942 105 ILE A CA 815 C C . ILE A 105 ? 1.0399 0.6099 0.6739 -0.3436 -0.1081 0.1711 105 ILE A C 816 O O . ILE A 105 ? 1.2060 0.7767 0.8527 -0.3509 -0.1067 0.1735 105 ILE A O 817 C CB . ILE A 105 ? 1.0956 0.6958 0.6799 -0.3713 -0.1134 0.2022 105 ILE A CB 818 C CG1 . ILE A 105 ? 1.4385 1.0587 1.0200 -0.3904 -0.1025 0.2088 105 ILE A CG1 819 C CG2 . ILE A 105 ? 1.1224 0.7218 0.6897 -0.3770 -0.1323 0.2249 105 ILE A CG2 820 C CD1 . ILE A 105 ? 1.7006 1.3581 1.2462 -0.4125 -0.0872 0.2125 105 ILE A CD1 821 N N . LEU A 106 ? 0.9753 0.5494 0.6096 -0.3320 -0.0968 0.1501 106 LEU A N 822 C CA . LEU A 106 ? 0.9156 0.4964 0.5656 -0.3258 -0.0829 0.1285 106 LEU A CA 823 C C . LEU A 106 ? 0.9503 0.5674 0.5946 -0.3225 -0.0612 0.1097 106 LEU A C 824 O O . LEU A 106 ? 1.0127 0.6359 0.6555 -0.3079 -0.0597 0.0998 106 LEU A O 825 C CB . LEU A 106 ? 0.8817 0.4373 0.5537 -0.3008 -0.0924 0.1145 106 LEU A CB 826 C CG . LEU A 106 ? 0.8534 0.4190 0.5405 -0.2913 -0.0812 0.0922 106 LEU A CG 827 C CD1 . LEU A 106 ? 1.2250 0.7921 0.9193 -0.3094 -0.0803 0.0970 106 LEU A CD1 828 C CD2 . LEU A 106 ? 0.8461 0.3897 0.5472 -0.2671 -0.0897 0.0781 106 LEU A CD2 829 N N . ALA A 107 ? 0.9240 0.5650 0.5695 -0.3362 -0.0447 0.1050 107 ALA A N 830 C CA . ALA A 107 ? 0.8796 0.5533 0.5262 -0.3325 -0.0232 0.0857 107 ALA A CA 831 C C . ALA A 107 ? 0.8631 0.5469 0.5379 -0.3253 -0.0139 0.0713 107 ALA A C 832 O O . ALA A 107 ? 0.9422 0.6193 0.6286 -0.3347 -0.0187 0.0787 107 ALA A O 833 C CB . ALA A 107 ? 0.8593 0.5597 0.4823 -0.3547 -0.0087 0.0914 107 ALA A CB 834 N N . CYS A 108 ? 0.7810 0.4808 0.4687 -0.3099 -0.0025 0.0524 108 CYS A N 835 C CA . CYS A 108 ? 0.7570 0.4662 0.4732 -0.3008 0.0025 0.0410 108 CYS A CA 836 C C . CYS A 108 ? 0.8306 0.5729 0.5622 -0.2996 0.0238 0.0268 108 CYS A C 837 O O . CYS A 108 ? 0.8520 0.6057 0.5725 -0.2991 0.0345 0.0191 108 CYS A O 838 C CB . CYS A 108 ? 0.7383 0.4295 0.4633 -0.2788 -0.0089 0.0337 108 CYS A CB 839 S SG . CYS A 108 ? 1.0515 0.7024 0.7659 -0.2750 -0.0321 0.0445 108 CYS A SG 840 N N . ALA A 109 ? 0.8848 0.6417 0.6444 -0.2990 0.0286 0.0227 109 ALA A N 841 C CA . ALA A 109 ? 0.8669 0.6547 0.6519 -0.2948 0.0476 0.0096 109 ALA A CA 842 C C . ALA A 109 ? 0.8427 0.6314 0.6563 -0.2770 0.0417 0.0030 109 ALA A C 843 O O . ALA A 109 ? 0.9224 0.7207 0.7595 -0.2795 0.0382 0.0059 109 ALA A O 844 C CB . ALA A 109 ? 0.7408 0.5547 0.5395 -0.3127 0.0607 0.0137 109 ALA A CB 845 N N . PRO A 110 ? 0.6969 0.4774 0.5087 -0.2604 0.0395 -0.0040 110 PRO A N 846 C CA . PRO A 110 ? 0.6732 0.4534 0.5060 -0.2440 0.0322 -0.0065 110 PRO A CA 847 C C . PRO A 110 ? 0.8312 0.6385 0.7033 -0.2410 0.0415 -0.0107 110 PRO A C 848 O O . PRO A 110 ? 1.1036 0.9134 0.9931 -0.2330 0.0317 -0.0076 110 PRO A O 849 C CB . PRO A 110 ? 0.6523 0.4241 0.4767 -0.2310 0.0330 -0.0117 110 PRO A CB 850 C CG . PRO A 110 ? 0.8460 0.6046 0.6387 -0.2400 0.0319 -0.0090 110 PRO A CG 851 C CD . PRO A 110 ? 0.6740 0.4458 0.4624 -0.2581 0.0421 -0.0076 110 PRO A CD 852 N N . LEU A 111 ? 0.7341 0.5627 0.6205 -0.2471 0.0599 -0.0179 111 LEU A N 853 C CA . LEU A 111 ? 0.6303 0.4864 0.5618 -0.2421 0.0701 -0.0226 111 LEU A CA 854 C C . LEU A 111 ? 0.6341 0.5109 0.5846 -0.2561 0.0728 -0.0163 111 LEU A C 855 O O . LEU A 111 ? 0.6271 0.5317 0.6200 -0.2534 0.0826 -0.0194 111 LEU A O 856 C CB . LEU A 111 ? 0.6278 0.4968 0.5724 -0.2372 0.0907 -0.0382 111 LEU A CB 857 C CG . LEU A 111 ? 0.8192 0.6819 0.7844 -0.2188 0.0879 -0.0432 111 LEU A CG 858 C CD1 . LEU A 111 ? 0.6081 0.4436 0.5401 -0.2138 0.0728 -0.0375 111 LEU A CD1 859 C CD2 . LEU A 111 ? 1.0301 0.9029 1.0139 -0.2141 0.1079 -0.0617 111 LEU A CD2 860 N N . TYR A 112 ? 0.6502 0.5140 0.5737 -0.2712 0.0638 -0.0066 112 TYR A N 861 C CA . TYR A 112 ? 0.6600 0.5402 0.6011 -0.2873 0.0625 0.0024 112 TYR A CA 862 C C . TYR A 112 ? 0.6513 0.5422 0.6280 -0.2811 0.0487 0.0066 112 TYR A C 863 O O . TYR A 112 ? 0.6427 0.5138 0.6090 -0.2710 0.0309 0.0080 112 TYR A O 864 C CB . TYR A 112 ? 0.6823 0.5368 0.5875 -0.3032 0.0494 0.0139 112 TYR A CB 865 C CG . TYR A 112 ? 0.6944 0.5551 0.6161 -0.3201 0.0394 0.0255 112 TYR A CG 866 C CD1 . TYR A 112 ? 1.0961 0.9821 1.0300 -0.3397 0.0534 0.0327 112 TYR A CD1 867 C CD2 . TYR A 112 ? 0.6948 0.5361 0.6182 -0.3180 0.0158 0.0290 112 TYR A CD2 868 C CE1 . TYR A 112 ? 0.7223 0.6143 0.6748 -0.3573 0.0430 0.0450 112 TYR A CE1 869 C CE2 . TYR A 112 ? 0.9905 0.8352 0.9296 -0.3352 0.0041 0.0384 112 TYR A CE2 870 C CZ . TYR A 112 ? 0.7221 0.5918 0.6779 -0.3552 0.0171 0.0474 112 TYR A CZ 871 O OH . TYR A 112 ? 0.7381 0.6116 0.7130 -0.3743 0.0043 0.0584 112 TYR A OH 872 N N . HIS A 113 ? 0.6767 0.6013 0.6952 -0.2880 0.0570 0.0091 113 HIS A N 873 C CA . HIS A 113 ? 0.8974 0.8387 0.9558 -0.2829 0.0434 0.0144 113 HIS A CA 874 C C . HIS A 113 ? 0.6470 0.5986 0.7192 -0.3029 0.0318 0.0258 113 HIS A C 875 O O . HIS A 113 ? 0.6633 0.6193 0.7271 -0.3207 0.0410 0.0301 113 HIS A O 876 C CB . HIS A 113 ? 0.9931 0.9689 1.1032 -0.2704 0.0602 0.0083 113 HIS A CB 877 C CG . HIS A 113 ? 0.7774 0.7410 0.8865 -0.2493 0.0616 0.0006 113 HIS A CG 878 N ND1 . HIS A 113 ? 0.7391 0.6878 0.8218 -0.2437 0.0765 -0.0114 113 HIS A ND1 879 C CD2 . HIS A 113 ? 0.7013 0.6658 0.8329 -0.2342 0.0485 0.0052 113 HIS A CD2 880 C CE1 . HIS A 113 ? 0.8088 0.7488 0.9009 -0.2262 0.0729 -0.0145 113 HIS A CE1 881 N NE2 . HIS A 113 ? 0.7973 0.7468 0.9186 -0.2201 0.0565 -0.0034 113 HIS A NE2 882 N N . TRP A 114 ? 0.6436 0.5999 0.7365 -0.3016 0.0105 0.0319 114 TRP A N 883 C CA . TRP A 114 ? 0.7368 0.6915 0.8331 -0.3217 -0.0079 0.0414 114 TRP A CA 884 C C . TRP A 114 ? 0.8228 0.8188 0.9772 -0.3299 -0.0131 0.0501 114 TRP A C 885 O O . TRP A 114 ? 0.9401 0.9569 1.1160 -0.3485 -0.0052 0.0569 114 TRP A O 886 C CB . TRP A 114 ? 0.7400 0.6562 0.7978 -0.3191 -0.0350 0.0398 114 TRP A CB 887 C CG . TRP A 114 ? 0.8765 0.7761 0.9248 -0.3407 -0.0536 0.0452 114 TRP A CG 888 C CD1 . TRP A 114 ? 1.0350 0.9467 1.1002 -0.3628 -0.0480 0.0542 114 TRP A CD1 889 C CD2 . TRP A 114 ? 1.0906 0.9581 1.1114 -0.3433 -0.0808 0.0415 114 TRP A CD2 890 N NE1 . TRP A 114 ? 1.1121 0.9984 1.1649 -0.3795 -0.0719 0.0575 114 TRP A NE1 891 C CE2 . TRP A 114 ? 1.1553 1.0129 1.1800 -0.3674 -0.0922 0.0476 114 TRP A CE2 892 C CE3 . TRP A 114 ? 1.2806 1.1274 1.2733 -0.3283 -0.0957 0.0328 114 TRP A CE3 893 C CZ2 . TRP A 114 ? 1.2594 1.0836 1.2620 -0.3759 -0.1190 0.0425 114 TRP A CZ2 894 C CZ3 . TRP A 114 ? 1.4826 1.2999 1.4500 -0.3363 -0.1200 0.0268 114 TRP A CZ3 895 C CH2 . TRP A 114 ? 1.4195 1.2237 1.3924 -0.3595 -0.1320 0.0302 114 TRP A CH2 896 N N . ARG A 115 ? 0.8020 0.8110 0.9818 -0.3175 -0.0275 0.0521 115 ARG A N 897 C CA . ARG A 115 ? 0.8654 0.9110 1.0992 -0.3248 -0.0418 0.0628 115 ARG A CA 898 C C . ARG A 115 ? 0.7903 0.8161 1.0028 -0.3411 -0.0745 0.0675 115 ARG A C 899 O O . ARG A 115 ? 0.7496 0.7989 0.9959 -0.3476 -0.0947 0.0760 115 ARG A O 900 C CB . ARG A 115 ? 1.0012 1.0899 1.2870 -0.3369 -0.0207 0.0679 115 ARG A CB 901 C CG . ARG A 115 ? 1.0149 1.1475 1.3659 -0.3448 -0.0339 0.0805 115 ARG A CG 902 C CD . ARG A 115 ? 0.7553 0.9031 1.1219 -0.3733 -0.0351 0.0895 115 ARG A CD 903 N NE . ARG A 115 ? 0.7052 0.9000 1.1404 -0.3821 -0.0473 0.1024 115 ARG A NE 904 C CZ . ARG A 115 ? 0.7010 0.8924 1.1409 -0.3948 -0.0827 0.1110 115 ARG A CZ 905 N NH1 . ARG A 115 ? 0.9371 1.0792 1.3155 -0.3991 -0.1073 0.1053 115 ARG A NH1 906 N NH2 . ARG A 115 ? 0.6751 0.9139 1.1824 -0.4031 -0.0938 0.1241 115 ARG A NH2 907 N N . THR A 116 ? 0.9518 0.9331 1.1082 -0.3469 -0.0804 0.0607 116 THR A N 908 C CA . THR A 116 ? 1.1842 1.1370 1.3139 -0.3630 -0.1085 0.0599 116 THR A CA 909 C C . THR A 116 ? 1.1539 1.1299 1.3231 -0.3889 -0.1191 0.0707 116 THR A C 910 O O . THR A 116 ? 1.3318 1.3395 1.5388 -0.3979 -0.0991 0.0789 116 THR A O 911 C CB . THR A 116 ? 1.1226 1.0660 1.2339 -0.3527 -0.1337 0.0557 116 THR A CB 912 O OG1 . THR A 116 ? 0.9169 0.9022 1.0784 -0.3567 -0.1468 0.0666 116 THR A OG1 913 C CG2 . THR A 116 ? 0.9794 0.9123 1.0654 -0.3271 -0.1219 0.0496 116 THR A CG2 914 N N . GLU A 117 ? 0.8942 0.8559 1.0548 -0.4018 -0.1503 0.0698 117 GLU A N 915 C CA . GLU A 117 ? 0.8758 0.8596 1.0769 -0.4281 -0.1658 0.0804 117 GLU A CA 916 C C . GLU A 117 ? 0.9667 0.9888 1.2097 -0.4301 -0.1880 0.0877 117 GLU A C 917 O O . GLU A 117 ? 1.0200 1.0667 1.3035 -0.4512 -0.2015 0.0976 117 GLU A O 918 C CB . GLU A 117 ? 0.9222 0.8591 1.0853 -0.4424 -0.1845 0.0732 117 GLU A CB 919 C CG . GLU A 117 ? 0.9501 0.8811 1.1170 -0.4515 -0.1649 0.0801 117 GLU A CG 920 C CD . GLU A 117 ? 1.2585 1.1316 1.3735 -0.4488 -0.1715 0.0702 117 GLU A CD 921 O OE1 . GLU A 117 ? 1.4312 1.2685 1.5037 -0.4361 -0.1831 0.0554 117 GLU A OE1 922 O OE2 . GLU A 117 ? 1.2806 1.1455 1.4000 -0.4592 -0.1648 0.0782 117 GLU A OE2 923 N N . MET A 118 ? 0.9505 0.9789 1.1852 -0.4085 -0.1927 0.0849 118 MET A N 924 C CA . MET A 118 ? 0.8723 0.9295 1.1345 -0.4115 -0.2211 0.0929 118 MET A CA 925 C C . MET A 118 ? 0.9444 1.0589 1.2780 -0.4008 -0.2090 0.1084 118 MET A C 926 O O . MET A 118 ? 1.0003 1.1552 1.3938 -0.4158 -0.2140 0.1210 118 MET A O 927 C CB . MET A 118 ? 0.7894 0.8187 0.9959 -0.3976 -0.2394 0.0830 118 MET A CB 928 C CG . MET A 118 ? 0.9189 0.9015 1.0677 -0.4120 -0.2633 0.0670 118 MET A CG 929 S SD . MET A 118 ? 1.0460 0.9750 1.1143 -0.3906 -0.2540 0.0466 118 MET A SD 930 C CE . MET A 118 ? 1.2696 1.1815 1.3401 -0.3848 -0.2169 0.0458 118 MET A CE 931 N N . LYS A 119 ? 0.7126 0.8305 1.0437 -0.3747 -0.1930 0.1075 119 LYS A N 932 C CA . LYS A 119 ? 0.7037 0.8704 1.1048 -0.3606 -0.1798 0.1199 119 LYS A CA 933 C C . LYS A 119 ? 0.7276 0.8932 1.1349 -0.3450 -0.1389 0.1119 119 LYS A C 934 O O . LYS A 119 ? 0.9890 1.1143 1.3391 -0.3396 -0.1258 0.0989 119 LYS A O 935 C CB . LYS A 119 ? 0.7146 0.8899 1.1180 -0.3441 -0.1996 0.1286 119 LYS A CB 936 C CG . LYS A 119 ? 0.8790 1.0107 1.2114 -0.3288 -0.1982 0.1178 119 LYS A CG 937 C CD . LYS A 119 ? 1.0653 1.2104 1.4025 -0.3154 -0.2183 0.1311 119 LYS A CD 938 C CE . LYS A 119 ? 1.0492 1.1541 1.3128 -0.3040 -0.2190 0.1215 119 LYS A CE 939 N NZ . LYS A 119 ? 0.8541 0.9366 1.1029 -0.2877 -0.1850 0.1102 119 LYS A NZ 940 N N . GLN A 120 ? 0.6886 0.8996 1.1664 -0.3380 -0.1192 0.1185 120 GLN A N 941 C CA . GLN A 120 ? 0.6832 0.8967 1.1691 -0.3229 -0.0799 0.1079 120 GLN A CA 942 C C . GLN A 120 ? 0.6839 0.8670 1.1333 -0.2990 -0.0760 0.1003 120 GLN A C 943 O O . GLN A 120 ? 0.7855 0.9703 1.2417 -0.2882 -0.0972 0.1093 120 GLN A O 944 C CB . GLN A 120 ? 0.6979 0.9680 1.2717 -0.3164 -0.0605 0.1140 120 GLN A CB 945 C CG . GLN A 120 ? 0.8307 1.1062 1.4125 -0.3035 -0.0176 0.0988 120 GLN A CG 946 C CD . GLN A 120 ? 1.1002 1.4340 1.7656 -0.3028 0.0058 0.1014 120 GLN A CD 947 O OE1 . GLN A 120 ? 1.1083 1.4777 1.8188 -0.3195 -0.0062 0.1152 120 GLN A OE1 948 N NE2 . GLN A 120 ? 1.2109 1.5558 1.8994 -0.2836 0.0399 0.0868 120 GLN A NE2 949 N N . GLU A 121 ? 0.6876 0.8449 1.0990 -0.2924 -0.0498 0.0855 121 GLU A N 950 C CA . GLU A 121 ? 0.7769 0.9004 1.1459 -0.2737 -0.0464 0.0776 121 GLU A CA 951 C C . GLU A 121 ? 0.7927 0.8964 1.1294 -0.2713 -0.0159 0.0617 121 GLU A C 952 O O . GLU A 121 ? 0.8901 1.0045 1.2303 -0.2856 0.0004 0.0583 121 GLU A O 953 C CB . GLU A 121 ? 0.7863 0.8735 1.0941 -0.2783 -0.0750 0.0793 121 GLU A CB 954 C CG . GLU A 121 ? 1.0671 1.1343 1.3492 -0.2587 -0.0799 0.0793 121 GLU A CG 955 C CD . GLU A 121 ? 1.3575 1.4519 1.6831 -0.2497 -0.0993 0.0961 121 GLU A CD 956 O OE1 . GLU A 121 ? 1.4700 1.5577 1.7947 -0.2324 -0.0981 0.0999 121 GLU A OE1 957 O OE2 . GLU A 121 ? 1.4124 1.5355 1.7744 -0.2611 -0.1173 0.1074 121 GLU A OE2 958 N N . ARG A 122 ? 0.6441 0.7222 0.9518 -0.2545 -0.0085 0.0535 122 ARG A N 959 C CA . ARG A 122 ? 0.6217 0.6716 0.8807 -0.2553 0.0110 0.0397 122 ARG A CA 960 C C . ARG A 122 ? 0.8116 0.8218 1.0161 -0.2467 -0.0028 0.0379 122 ARG A C 961 O O . ARG A 122 ? 1.1831 1.1901 1.3960 -0.2297 -0.0042 0.0388 122 ARG A O 962 C CB . ARG A 122 ? 0.6148 0.6804 0.9025 -0.2434 0.0422 0.0272 122 ARG A CB 963 C CG . ARG A 122 ? 0.6290 0.7383 0.9721 -0.2503 0.0615 0.0262 122 ARG A CG 964 C CD . ARG A 122 ? 0.7417 0.8669 1.1186 -0.2342 0.0915 0.0102 122 ARG A CD 965 N NE . ARG A 122 ? 0.7766 0.8794 1.1022 -0.2370 0.1122 -0.0063 122 ARG A NE 966 C CZ . ARG A 122 ? 0.7262 0.8479 1.0492 -0.2475 0.1394 -0.0169 122 ARG A CZ 967 N NH1 . ARG A 122 ? 0.6312 0.7960 1.0035 -0.2555 0.1515 -0.0132 122 ARG A NH1 968 N NH2 . ARG A 122 ? 0.7628 0.8632 1.0342 -0.2508 0.1543 -0.0303 122 ARG A NH2 969 N N . GLU A 123 ? 0.7562 0.7368 0.9082 -0.2583 -0.0126 0.0362 123 GLU A N 970 C CA . GLU A 123 ? 0.7278 0.6735 0.8298 -0.2501 -0.0246 0.0335 123 GLU A CA 971 C C . GLU A 123 ? 0.7184 0.6348 0.7755 -0.2517 -0.0117 0.0240 123 GLU A C 972 O O . GLU A 123 ? 0.7451 0.6498 0.7818 -0.2669 -0.0121 0.0235 123 GLU A O 973 C CB . GLU A 123 ? 0.6525 0.5864 0.7325 -0.2590 -0.0523 0.0387 123 GLU A CB 974 C CG . GLU A 123 ? 0.6709 0.6320 0.7870 -0.2559 -0.0699 0.0500 123 GLU A CG 975 C CD . GLU A 123 ? 0.8749 0.8241 0.9621 -0.2653 -0.0984 0.0522 123 GLU A CD 976 O OE1 . GLU A 123 ? 0.7066 0.6795 0.8195 -0.2665 -0.1166 0.0629 123 GLU A OE1 977 O OE2 . GLU A 123 ? 1.1386 1.0548 1.1784 -0.2714 -0.1034 0.0427 123 GLU A OE2 978 N N . PRO A 124 ? 0.6551 0.5599 0.6991 -0.2369 -0.0020 0.0183 124 PRO A N 979 C CA . PRO A 124 ? 0.6925 0.5721 0.6965 -0.2375 0.0082 0.0105 124 PRO A CA 980 C C . PRO A 124 ? 0.8328 0.6800 0.7910 -0.2405 -0.0083 0.0112 124 PRO A C 981 O O . PRO A 124 ? 0.7880 0.6175 0.7225 -0.2289 -0.0112 0.0087 124 PRO A O 982 C CB . PRO A 124 ? 0.5939 0.4724 0.6043 -0.2205 0.0178 0.0057 124 PRO A CB 983 C CG . PRO A 124 ? 0.5859 0.4756 0.6206 -0.2103 0.0042 0.0145 124 PRO A CG 984 C CD . PRO A 124 ? 0.6003 0.5146 0.6681 -0.2198 -0.0033 0.0214 124 PRO A CD 985 N N . VAL A 125 ? 0.6395 0.4795 0.5892 -0.2559 -0.0186 0.0142 125 VAL A N 986 C CA . VAL A 125 ? 0.6583 0.4642 0.5686 -0.2585 -0.0336 0.0123 125 VAL A CA 987 C C . VAL A 125 ? 0.7008 0.4845 0.5822 -0.2581 -0.0243 0.0098 125 VAL A C 988 O O . VAL A 125 ? 0.7325 0.4892 0.5847 -0.2508 -0.0321 0.0065 125 VAL A O 989 C CB . VAL A 125 ? 0.6809 0.4807 0.5932 -0.2769 -0.0485 0.0158 125 VAL A CB 990 C CG1 . VAL A 125 ? 0.8950 0.7121 0.8279 -0.2776 -0.0645 0.0179 125 VAL A CG1 991 C CG2 . VAL A 125 ? 1.0315 0.8475 0.9633 -0.2943 -0.0360 0.0223 125 VAL A CG2 992 N N . GLY A 126 ? 0.6608 0.4583 0.5510 -0.2659 -0.0074 0.0112 126 GLY A N 993 C CA . GLY A 126 ? 0.6941 0.4744 0.5562 -0.2694 -0.0004 0.0114 126 GLY A CA 994 C C . GLY A 126 ? 0.7489 0.5078 0.5935 -0.2861 -0.0111 0.0194 126 GLY A C 995 O O . GLY A 126 ? 0.8450 0.5935 0.6936 -0.2916 -0.0268 0.0213 126 GLY A O 996 N N . THR A 127 ? 0.7863 0.5376 0.6113 -0.2952 -0.0043 0.0248 127 THR A N 997 C CA . THR A 127 ? 0.7401 0.4689 0.5501 -0.3119 -0.0153 0.0364 127 THR A CA 998 C C . THR A 127 ? 0.8553 0.5686 0.6361 -0.3141 -0.0129 0.0427 127 THR A C 999 O O . THR A 127 ? 0.8118 0.5389 0.5852 -0.3076 0.0004 0.0374 127 THR A O 1000 C CB . THR A 127 ? 0.9998 0.7514 0.8297 -0.3343 -0.0090 0.0461 127 THR A CB 1001 O OG1 . THR A 127 ? 1.0150 0.7403 0.8331 -0.3515 -0.0232 0.0597 127 THR A OG1 1002 C CG2 . THR A 127 ? 0.7494 0.5329 0.5803 -0.3413 0.0155 0.0466 127 THR A CG2 1003 N N . CYS A 128 ? 0.7816 0.4652 0.5476 -0.3236 -0.0278 0.0544 128 CYS A N 1004 C CA . CYS A 128 ? 0.7995 0.4687 0.5399 -0.3277 -0.0294 0.0649 128 CYS A CA 1005 C C . CYS A 128 ? 1.1531 0.8165 0.8883 -0.3506 -0.0348 0.0851 128 CYS A C 1006 O O . CYS A 128 ? 1.4198 1.0913 1.1746 -0.3599 -0.0373 0.0891 128 CYS A O 1007 C CB . CYS A 128 ? 0.8017 0.4375 0.5314 -0.3094 -0.0449 0.0615 128 CYS A CB 1008 S SG . CYS A 128 ? 1.2751 0.9217 1.0103 -0.2819 -0.0383 0.0417 128 CYS A SG 1009 N N . PHE A 129 ? 1.0002 0.6561 0.7128 -0.3553 -0.0375 0.0981 129 PHE A N 1010 C CA . PHE A 129 ? 0.9239 0.5779 0.6327 -0.3705 -0.0451 0.1193 129 PHE A CA 1011 C C . PHE A 129 ? 0.9093 0.5334 0.6019 -0.3644 -0.0630 0.1320 129 PHE A C 1012 O O . PHE A 129 ? 0.9055 0.5298 0.5779 -0.3602 -0.0607 0.1316 129 PHE A O 1013 C CB . PHE A 129 ? 0.9104 0.6026 0.6080 -0.3909 -0.0248 0.1273 129 PHE A CB 1014 C CG . PHE A 129 ? 0.9643 0.6881 0.6874 -0.3998 -0.0087 0.1205 129 PHE A CG 1015 C CD1 . PHE A 129 ? 0.9461 0.6921 0.6787 -0.3948 0.0099 0.1015 129 PHE A CD1 1016 C CD2 . PHE A 129 ? 0.9040 0.6356 0.6459 -0.4133 -0.0127 0.1340 129 PHE A CD2 1017 C CE1 . PHE A 129 ? 0.8750 0.6525 0.6376 -0.4024 0.0240 0.0965 129 PHE A CE1 1018 C CE2 . PHE A 129 ? 0.8925 0.6563 0.6630 -0.4217 0.0013 0.1292 129 PHE A CE2 1019 C CZ . PHE A 129 ? 0.8636 0.6514 0.6454 -0.4159 0.0196 0.1106 129 PHE A CZ 1020 N N . LEU A 130 ? 1.0443 0.6429 0.7493 -0.3642 -0.0814 0.1432 130 LEU A N 1021 C CA . LEU A 130 ? 1.0608 0.6311 0.7586 -0.3588 -0.0998 0.1578 130 LEU A CA 1022 C C . LEU A 130 ? 1.2085 0.7859 0.9021 -0.3789 -0.1051 0.1842 130 LEU A C 1023 O O . LEU A 130 ? 1.4460 1.0269 1.1561 -0.3902 -0.1059 0.1903 130 LEU A O 1024 C CB . LEU A 130 ? 0.9655 0.4965 0.6833 -0.3404 -0.1173 0.1484 130 LEU A CB 1025 C CG . LEU A 130 ? 0.9759 0.4772 0.6918 -0.3236 -0.1320 0.1514 130 LEU A CG 1026 C CD1 . LEU A 130 ? 0.9801 0.4466 0.7161 -0.3045 -0.1433 0.1342 130 LEU A CD1 1027 C CD2 . LEU A 130 ? 1.0424 0.5359 0.7548 -0.3336 -0.1459 0.1796 130 LEU A CD2 1028 N N . GLN A 131 ? 1.0174 0.5982 0.6890 -0.3844 -0.1097 0.2008 131 GLN A N 1029 C CA . GLN A 131 ? 1.2877 0.8791 0.9507 -0.4046 -0.1148 0.2279 131 GLN A CA 1030 C C . GLN A 131 ? 1.1884 0.7567 0.8460 -0.4005 -0.1370 0.2480 131 GLN A C 1031 O O . GLN A 131 ? 1.1512 0.7201 0.7919 -0.3928 -0.1392 0.2459 131 GLN A O 1032 C CB . GLN A 131 ? 1.3186 0.9544 0.9538 -0.4235 -0.0928 0.2299 131 GLN A CB 1033 C CG . GLN A 131 ? 1.3907 1.0407 1.0058 -0.4437 -0.0984 0.2581 131 GLN A CG 1034 C CD . GLN A 131 ? 1.3496 1.0431 0.9306 -0.4599 -0.0758 0.2550 131 GLN A CD 1035 O OE1 . GLN A 131 ? 1.2232 0.9380 0.8017 -0.4579 -0.0534 0.2321 131 GLN A OE1 1036 N NE2 . GLN A 131 ? 1.5301 1.2374 1.0853 -0.4761 -0.0816 0.2771 131 GLN A NE2 1037 N N . ASP A 132 ? 1.2205 0.7684 0.8954 -0.4057 -0.1544 0.2681 132 ASP A N 1038 C CA . ASP A 132 ? 1.3053 0.8381 0.9766 -0.4056 -0.1752 0.2922 132 ASP A CA 1039 C C . ASP A 132 ? 1.3520 0.9061 1.0092 -0.4315 -0.1775 0.3217 132 ASP A C 1040 O O . ASP A 132 ? 1.4105 0.9525 1.0876 -0.4404 -0.1863 0.3366 132 ASP A O 1041 C CB . ASP A 132 ? 1.3566 0.8432 1.0629 -0.3875 -0.1966 0.2925 132 ASP A CB 1042 C CG . ASP A 132 ? 1.7240 1.1940 1.4352 -0.3868 -0.2198 0.3196 132 ASP A CG 1043 O OD1 . ASP A 132 ? 1.8379 1.3029 1.5577 -0.4014 -0.2312 0.3440 132 ASP A OD1 1044 O OD2 . ASP A 132 ? 1.9473 1.4101 1.6566 -0.3718 -0.2275 0.3176 132 ASP A OD2 1045 N N . GLY A 133 ? 1.4184 1.0049 1.0402 -0.4443 -0.1693 0.3289 133 GLY A N 1046 C CA . GLY A 133 ? 1.5403 1.1474 1.1413 -0.4671 -0.1753 0.3585 133 GLY A CA 1047 C C . GLY A 133 ? 1.6081 1.2417 1.2064 -0.4899 -0.1603 0.3678 133 GLY A C 1048 O O . GLY A 133 ? 1.7904 1.4577 1.3593 -0.5109 -0.1522 0.3825 133 GLY A O 1049 N N . THR A 134 ? 1.5520 1.1717 1.1815 -0.4860 -0.1564 0.3587 134 THR A N 1050 C CA . THR A 134 ? 1.6635 1.3089 1.2986 -0.5058 -0.1411 0.3652 134 THR A CA 1051 C C . THR A 134 ? 1.6324 1.2789 1.2909 -0.4969 -0.1255 0.3378 134 THR A C 1052 O O . THR A 134 ? 1.7809 1.4635 1.4296 -0.5033 -0.1003 0.3232 134 THR A O 1053 C CB . THR A 134 ? 1.6745 1.3007 1.3311 -0.5183 -0.1607 0.3957 134 THR A CB 1054 O OG1 . THR A 134 ? 1.6796 1.3133 1.3608 -0.5279 -0.1503 0.3929 134 THR A OG1 1055 C CG2 . THR A 134 ? 1.6087 1.1829 1.2918 -0.4991 -0.1891 0.3990 134 THR A CG2 1056 N N . LYS A 135 ? 1.3680 0.9746 1.0591 -0.4820 -0.1416 0.3304 135 LYS A N 1057 C CA . LYS A 135 ? 1.3657 0.9681 1.0833 -0.4749 -0.1336 0.3076 135 LYS A CA 1058 C C . LYS A 135 ? 1.3421 0.9520 1.0514 -0.4575 -0.1196 0.2769 135 LYS A C 1059 O O . LYS A 135 ? 1.1882 0.7816 0.8852 -0.4413 -0.1263 0.2692 135 LYS A O 1060 C CB . LYS A 135 ? 1.3880 0.9427 1.1383 -0.4643 -0.1569 0.3073 135 LYS A CB 1061 C CG . LYS A 135 ? 1.4670 1.0171 1.2458 -0.4630 -0.1533 0.2889 135 LYS A CG 1062 C CD . LYS A 135 ? 1.5719 1.0739 1.3793 -0.4559 -0.1773 0.2896 135 LYS A CD 1063 C CE . LYS A 135 ? 1.6033 1.1023 1.4377 -0.4596 -0.1765 0.2742 135 LYS A CE 1064 N NZ . LYS A 135 ? 1.1755 0.6776 1.0094 -0.4422 -0.1678 0.2413 135 LYS A NZ 1065 N N . THR A 136 ? 1.3647 1.0007 1.0841 -0.4612 -0.1006 0.2608 136 THR A N 1066 C CA . THR A 136 ? 1.0708 0.7164 0.7861 -0.4464 -0.0867 0.2328 136 THR A CA 1067 C C . THR A 136 ? 1.2310 0.8682 0.9776 -0.4386 -0.0876 0.2142 136 THR A C 1068 O O . THR A 136 ? 1.4059 1.0631 1.1725 -0.4523 -0.0808 0.2179 136 THR A O 1069 C CB . THR A 136 ? 1.0681 0.7615 0.7628 -0.4580 -0.0591 0.2282 136 THR A CB 1070 O OG1 . THR A 136 ? 1.0857 0.7887 0.7466 -0.4673 -0.0592 0.2443 136 THR A OG1 1071 C CG2 . THR A 136 ? 1.0131 0.7130 0.7059 -0.4423 -0.0460 0.2001 136 THR A CG2 1072 N N . VAL A 137 ? 1.0310 0.6405 0.7819 -0.4171 -0.0966 0.1945 137 VAL A N 1073 C CA . VAL A 137 ? 1.0062 0.6076 0.7816 -0.4089 -0.0996 0.1748 137 VAL A CA 1074 C C . VAL A 137 ? 1.0200 0.6393 0.7901 -0.3969 -0.0847 0.1520 137 VAL A C 1075 O O . VAL A 137 ? 1.2251 0.8466 0.9738 -0.3881 -0.0781 0.1474 137 VAL A O 1076 C CB . VAL A 137 ? 1.0227 0.5761 0.8091 -0.3938 -0.1227 0.1679 137 VAL A CB 1077 C CG1 . VAL A 137 ? 1.0693 0.6024 0.8669 -0.4058 -0.1383 0.1902 137 VAL A CG1 1078 C CG2 . VAL A 137 ? 1.0113 0.5430 0.7806 -0.3732 -0.1273 0.1593 137 VAL A CG2 1079 N N . GLU A 138 ? 0.9933 0.6263 0.7850 -0.3975 -0.0806 0.1389 138 GLU A N 1080 C CA . GLU A 138 ? 1.1080 0.7572 0.9000 -0.3863 -0.0687 0.1185 138 GLU A CA 1081 C C . GLU A 138 ? 1.1751 0.7923 0.9686 -0.3667 -0.0840 0.1002 138 GLU A C 1082 O O . GLU A 138 ? 1.2627 0.8584 1.0696 -0.3663 -0.1000 0.0971 138 GLU A O 1083 C CB . GLU A 138 ? 1.0796 0.7679 0.8967 -0.3987 -0.0550 0.1161 138 GLU A CB 1084 C CG . GLU A 138 ? 0.9518 0.6604 0.7736 -0.3887 -0.0417 0.0979 138 GLU A CG 1085 C CD . GLU A 138 ? 1.1518 0.9018 1.0057 -0.4008 -0.0285 0.0971 138 GLU A CD 1086 O OE1 . GLU A 138 ? 1.4265 1.1862 1.3012 -0.4153 -0.0331 0.1086 138 GLU A OE1 1087 O OE2 . GLU A 138 ? 1.0078 0.7814 0.8700 -0.3958 -0.0134 0.0856 138 GLU A OE2 1088 N N . TYR A 139 ? 1.0258 0.6406 0.8047 -0.3510 -0.0782 0.0872 139 TYR A N 1089 C CA . TYR A 139 ? 0.8679 0.4557 0.6438 -0.3319 -0.0897 0.0695 139 TYR A CA 1090 C C . TYR A 139 ? 0.9937 0.6026 0.7723 -0.3248 -0.0792 0.0540 139 TYR A C 1091 O O . TYR A 139 ? 1.1075 0.7314 0.8769 -0.3207 -0.0651 0.0522 139 TYR A O 1092 C CB . TYR A 139 ? 0.8763 0.4362 0.6338 -0.3179 -0.0957 0.0709 139 TYR A CB 1093 C CG . TYR A 139 ? 1.0654 0.5965 0.8190 -0.2977 -0.1058 0.0525 139 TYR A CG 1094 C CD1 . TYR A 139 ? 1.1048 0.6106 0.8675 -0.2944 -0.1210 0.0431 139 TYR A CD1 1095 C CD2 . TYR A 139 ? 1.0936 0.6229 0.8338 -0.2826 -0.0996 0.0436 139 TYR A CD2 1096 C CE1 . TYR A 139 ? 1.0485 0.5290 0.8039 -0.2761 -0.1281 0.0233 139 TYR A CE1 1097 C CE2 . TYR A 139 ? 0.9593 0.4679 0.6958 -0.2627 -0.1061 0.0265 139 TYR A CE2 1098 C CZ . TYR A 139 ? 0.8883 0.3694 0.6293 -0.2612 -0.1203 0.0156 139 TYR A CZ 1099 O OH . TYR A 139 ? 1.0090 0.4721 0.7431 -0.2410 -0.1242 -0.0044 139 TYR A OH 1100 N N . ALA A 140 ? 0.8338 0.4436 0.6259 -0.3245 -0.0874 0.0435 140 ALA A N 1101 C CA . ALA A 140 ? 0.8390 0.4731 0.6386 -0.3174 -0.0802 0.0319 140 ALA A CA 1102 C C . ALA A 140 ? 0.8133 0.4315 0.6101 -0.3071 -0.0960 0.0165 140 ALA A C 1103 O O . ALA A 140 ? 0.8186 0.4475 0.6311 -0.3172 -0.1045 0.0145 140 ALA A O 1104 C CB . ALA A 140 ? 0.7928 0.4668 0.6193 -0.3328 -0.0693 0.0391 140 ALA A CB 1105 N N . PRO A 141 ? 0.8956 0.4910 0.6722 -0.2874 -0.0996 0.0054 141 PRO A N 1106 C CA . PRO A 141 ? 0.9200 0.4999 0.6866 -0.2769 -0.1127 -0.0118 141 PRO A CA 1107 C C . PRO A 141 ? 0.9822 0.5964 0.7569 -0.2721 -0.1100 -0.0169 141 PRO A C 1108 O O . PRO A 141 ? 1.1590 0.7699 0.9317 -0.2758 -0.1241 -0.0262 141 PRO A O 1109 C CB . PRO A 141 ? 0.8682 0.4283 0.6154 -0.2551 -0.1094 -0.0200 141 PRO A CB 1110 C CG . PRO A 141 ? 0.8791 0.4324 0.6269 -0.2587 -0.1027 -0.0053 141 PRO A CG 1111 C CD . PRO A 141 ? 0.9166 0.5024 0.6790 -0.2747 -0.0914 0.0084 141 PRO A CD 1112 N N . CYS A 142 ? 0.9398 0.5856 0.7243 -0.2645 -0.0935 -0.0106 142 CYS A N 1113 C CA . CYS A 142 ? 1.0453 0.7238 0.8429 -0.2588 -0.0914 -0.0116 142 CYS A CA 1114 C C . CYS A 142 ? 1.0006 0.7023 0.8268 -0.2766 -0.0968 -0.0045 142 CYS A C 1115 O O . CYS A 142 ? 1.1464 0.8737 0.9876 -0.2745 -0.1008 -0.0037 142 CYS A O 1116 C CB . CYS A 142 ? 1.2338 0.9355 1.0395 -0.2461 -0.0729 -0.0068 142 CYS A CB 1117 S SG . CYS A 142 ? 0.7398 0.4386 0.5247 -0.2225 -0.0707 -0.0143 142 CYS A SG 1118 N N . ARG A 143 ? 0.8051 0.4996 0.6411 -0.2949 -0.0976 0.0028 143 ARG A N 1119 C CA . ARG A 143 ? 0.8087 0.5270 0.6760 -0.3138 -0.1023 0.0108 143 ARG A CA 1120 C C . ARG A 143 ? 0.9907 0.6849 0.8511 -0.3261 -0.1270 0.0044 143 ARG A C 1121 O O . ARG A 143 ? 1.3119 0.9720 1.1605 -0.3362 -0.1354 0.0039 143 ARG A O 1122 C CB . ARG A 143 ? 0.7799 0.5086 0.6626 -0.3294 -0.0881 0.0237 143 ARG A CB 1123 C CG . ARG A 143 ? 0.7718 0.5299 0.6917 -0.3500 -0.0900 0.0335 143 ARG A CG 1124 C CD . ARG A 143 ? 0.9281 0.7034 0.8604 -0.3644 -0.0707 0.0462 143 ARG A CD 1125 N NE . ARG A 143 ? 0.8005 0.5418 0.7110 -0.3764 -0.0773 0.0534 143 ARG A NE 1126 C CZ . ARG A 143 ? 0.8895 0.6397 0.7975 -0.3848 -0.0620 0.0654 143 ARG A CZ 1127 N NH1 . ARG A 143 ? 0.7886 0.5755 0.7099 -0.3904 -0.0384 0.0690 143 ARG A NH1 1128 N NH2 . ARG A 143 ? 1.1631 0.8862 1.0551 -0.3880 -0.0702 0.0736 143 ARG A NH2 1129 N N . SER A 144 ? 0.9770 0.6885 0.8460 -0.3261 -0.1401 0.0001 144 SER A N 1130 C CA . SER A 144 ? 1.2171 0.9046 1.0721 -0.3357 -0.1654 -0.0112 144 SER A CA 1131 C C . SER A 144 ? 1.1092 0.8287 0.9833 -0.3423 -0.1803 -0.0096 144 SER A C 1132 O O . SER A 144 ? 1.0314 0.7923 0.9365 -0.3394 -0.1710 0.0024 144 SER A O 1133 C CB . SER A 144 ? 1.4020 1.0541 1.2140 -0.3181 -0.1698 -0.0296 144 SER A CB 1134 O OG . SER A 144 ? 1.2850 0.9590 1.0866 -0.2981 -0.1605 -0.0316 144 SER A OG 1135 N N . GLN A 145 ? 0.9962 0.6957 0.8522 -0.3507 -0.2046 -0.0226 145 GLN A N 1136 C CA . GLN A 145 ? 1.0433 0.7720 0.9143 -0.3602 -0.2240 -0.0206 145 GLN A CA 1137 C C . GLN A 145 ? 1.1311 0.8779 0.9807 -0.3407 -0.2236 -0.0242 145 GLN A C 1138 O O . GLN A 145 ? 1.3997 1.1737 1.2580 -0.3459 -0.2402 -0.0199 145 GLN A O 1139 C CB . GLN A 145 ? 1.3931 1.0932 1.2507 -0.3788 -0.2518 -0.0345 145 GLN A CB 1140 C CG . GLN A 145 ? 1.5772 1.2642 1.4596 -0.3883 -0.2473 -0.0282 145 GLN A CG 1141 C CD . GLN A 145 ? 1.5259 1.2557 1.4621 -0.4042 -0.2415 -0.0053 145 GLN A CD 1142 O OE1 . GLN A 145 ? 1.6873 1.4575 1.6492 -0.4094 -0.2462 0.0044 145 GLN A OE1 1143 N NE2 . GLN A 145 ? 1.2885 1.0121 1.2443 -0.4119 -0.2311 0.0045 145 GLN A NE2 1144 N N . ASP A 146 ? 1.0716 0.8046 0.8947 -0.3196 -0.2055 -0.0297 146 ASP A N 1145 C CA . ASP A 146 ? 1.1073 0.8605 0.9147 -0.3011 -0.2003 -0.0281 146 ASP A CA 1146 C C . ASP A 146 ? 1.0193 0.8060 0.8652 -0.2921 -0.1801 -0.0089 146 ASP A C 1147 O O . ASP A 146 ? 1.2233 1.0005 1.0730 -0.2846 -0.1595 -0.0074 146 ASP A O 1148 C CB . ASP A 146 ? 1.2801 1.0024 1.0413 -0.2836 -0.1917 -0.0447 146 ASP A CB 1149 C CG . ASP A 146 ? 1.4152 1.1549 1.1491 -0.2708 -0.1944 -0.0467 146 ASP A CG 1150 O OD1 . ASP A 146 ? 1.5756 1.3513 1.3288 -0.2738 -0.2021 -0.0315 146 ASP A OD1 1151 O OD2 . ASP A 146 ? 1.3317 1.0509 1.0268 -0.2578 -0.1887 -0.0621 146 ASP A OD2 1152 N N . ILE A 147 ? 0.9325 0.7578 0.8077 -0.2929 -0.1869 0.0051 147 ILE A N 1153 C CA . ILE A 147 ? 0.9919 0.8490 0.9153 -0.2872 -0.1696 0.0215 147 ILE A CA 1154 C C . ILE A 147 ? 1.0266 0.9095 0.9608 -0.2708 -0.1661 0.0333 147 ILE A C 1155 O O . ILE A 147 ? 1.0899 0.9677 0.9892 -0.2630 -0.1744 0.0309 147 ILE A O 1156 C CB . ILE A 147 ? 0.8110 0.6969 0.7855 -0.3047 -0.1777 0.0325 147 ILE A CB 1157 C CG1 . ILE A 147 ? 0.8318 0.7405 0.8143 -0.3128 -0.2060 0.0392 147 ILE A CG1 1158 C CG2 . ILE A 147 ? 0.8274 0.6907 0.7992 -0.3231 -0.1788 0.0257 147 ILE A CG2 1159 C CD1 . ILE A 147 ? 0.7651 0.7108 0.8080 -0.3278 -0.2142 0.0534 147 ILE A CD1 1160 N N . ASP A 148 ? 0.8129 0.7236 0.7978 -0.2663 -0.1527 0.0460 148 ASP A N 1161 C CA . ASP A 148 ? 0.8905 0.8242 0.9003 -0.2506 -0.1464 0.0593 148 ASP A CA 1162 C C . ASP A 148 ? 1.0494 0.9628 1.0243 -0.2343 -0.1328 0.0545 148 ASP A C 1163 O O . ASP A 148 ? 1.2175 1.1042 1.1660 -0.2321 -0.1189 0.0418 148 ASP A O 1164 C CB . ASP A 148 ? 0.8700 0.8292 0.8898 -0.2538 -0.1722 0.0735 148 ASP A CB 1165 C CG . ASP A 148 ? 0.8445 0.8265 0.9014 -0.2714 -0.1893 0.0793 148 ASP A CG 1166 O OD1 . ASP A 148 ? 0.8786 0.8698 0.9746 -0.2768 -0.1757 0.0786 148 ASP A OD1 1167 O OD2 . ASP A 148 ? 0.8230 0.8161 0.8696 -0.2808 -0.2165 0.0849 148 ASP A OD2 1168 N N . ALA A 149 ? 0.9054 0.8329 0.8819 -0.2238 -0.1382 0.0671 149 ALA A N 1169 C CA . ALA A 149 ? 0.7846 0.6979 0.7334 -0.2096 -0.1258 0.0657 149 ALA A CA 1170 C C . ALA A 149 ? 0.8611 0.7589 0.7508 -0.2101 -0.1366 0.0577 149 ALA A C 1171 O O . ALA A 149 ? 1.0774 0.9598 0.9373 -0.2001 -0.1250 0.0519 149 ALA A O 1172 C CB . ALA A 149 ? 0.7733 0.7090 0.7584 -0.1984 -0.1238 0.0853 149 ALA A CB 1173 N N . ASP A 150 ? 0.9067 0.8098 0.7805 -0.2222 -0.1585 0.0558 150 ASP A N 1174 C CA . ASP A 150 ? 0.9744 0.8647 0.7903 -0.2236 -0.1694 0.0444 150 ASP A CA 1175 C C . ASP A 150 ? 0.9725 0.8260 0.7574 -0.2252 -0.1615 0.0199 150 ASP A C 1176 O O . ASP A 150 ? 0.9827 0.8181 0.7239 -0.2180 -0.1570 0.0063 150 ASP A O 1177 C CB . ASP A 150 ? 1.1205 1.0284 0.9291 -0.2379 -0.1977 0.0488 150 ASP A CB 1178 C CG . ASP A 150 ? 1.5507 1.4576 1.3003 -0.2372 -0.2082 0.0424 150 ASP A CG 1179 O OD1 . ASP A 150 ? 1.8490 1.7360 1.5611 -0.2268 -0.1928 0.0284 150 ASP A OD1 1180 O OD2 . ASP A 150 ? 1.5655 1.4941 1.3065 -0.2475 -0.2317 0.0514 150 ASP A OD2 1181 N N . GLY A 151 ? 1.1541 0.9982 0.9653 -0.2345 -0.1593 0.0157 151 GLY A N 1182 C CA . GLY A 151 ? 1.1697 0.9783 0.9599 -0.2379 -0.1539 -0.0028 151 GLY A CA 1183 C C . GLY A 151 ? 1.0666 0.8642 0.8699 -0.2289 -0.1306 -0.0018 151 GLY A C 1184 O O . GLY A 151 ? 1.1596 0.9675 0.9690 -0.2156 -0.1169 0.0059 151 GLY A O 1185 N N . GLN A 152 ? 0.9231 0.6994 0.7301 -0.2379 -0.1276 -0.0088 152 GLN A N 1186 C CA . GLN A 152 ? 0.9988 0.7624 0.8112 -0.2326 -0.1084 -0.0086 152 GLN A CA 1187 C C . GLN A 152 ? 0.8653 0.6523 0.7203 -0.2382 -0.0966 0.0032 152 GLN A C 1188 O O . GLN A 152 ? 0.9725 0.7520 0.8313 -0.2377 -0.0814 0.0032 152 GLN A O 1189 C CB . GLN A 152 ? 1.2291 0.9560 1.0202 -0.2395 -0.1121 -0.0201 152 GLN A CB 1190 C CG . GLN A 152 ? 1.2984 0.9990 1.0498 -0.2308 -0.1200 -0.0362 152 GLN A CG 1191 C CD . GLN A 152 ? 1.3928 1.0563 1.1312 -0.2410 -0.1313 -0.0483 152 GLN A CD 1192 O OE1 . GLN A 152 ? 1.4455 1.1069 1.2020 -0.2591 -0.1404 -0.0439 152 GLN A OE1 1193 N NE2 . GLN A 152 ? 1.4960 1.1303 1.2066 -0.2294 -0.1307 -0.0630 152 GLN A NE2 1194 N N . GLY A 153 ? 0.7741 0.5910 0.6613 -0.2437 -0.1038 0.0126 153 GLY A N 1195 C CA . GLY A 153 ? 0.7478 0.5908 0.6810 -0.2480 -0.0916 0.0215 153 GLY A CA 1196 C C . GLY A 153 ? 0.7138 0.5619 0.6588 -0.2353 -0.0692 0.0225 153 GLY A C 1197 O O . GLY A 153 ? 0.7364 0.5907 0.6996 -0.2402 -0.0536 0.0217 153 GLY A O 1198 N N . PHE A 154 ? 0.6816 0.5284 0.6157 -0.2202 -0.0675 0.0241 154 PHE A N 1199 C CA . PHE A 154 ? 0.6635 0.5128 0.6094 -0.2087 -0.0489 0.0242 154 PHE A CA 1200 C C . PHE A 154 ? 0.7998 0.6220 0.7088 -0.2034 -0.0410 0.0160 154 PHE A C 1201 O O . PHE A 154 ? 0.8649 0.6868 0.7790 -0.1946 -0.0283 0.0155 154 PHE A O 1202 C CB . PHE A 154 ? 0.6596 0.5268 0.6265 -0.1966 -0.0519 0.0349 154 PHE A CB 1203 C CG . PHE A 154 ? 0.6634 0.5603 0.6827 -0.1980 -0.0535 0.0442 154 PHE A CG 1204 C CD1 . PHE A 154 ? 0.6914 0.6047 0.7224 -0.2061 -0.0724 0.0523 154 PHE A CD1 1205 C CD2 . PHE A 154 ? 0.6760 0.5847 0.7349 -0.1912 -0.0364 0.0436 154 PHE A CD2 1206 C CE1 . PHE A 154 ? 0.7983 0.7419 0.8840 -0.2067 -0.0747 0.0625 154 PHE A CE1 1207 C CE2 . PHE A 154 ? 0.7089 0.6458 0.8225 -0.1903 -0.0366 0.0510 154 PHE A CE2 1208 C CZ . PHE A 154 ? 0.7755 0.7312 0.9047 -0.1977 -0.0560 0.0619 154 PHE A CZ 1209 N N . CYS A 155 ? 0.9172 0.7162 0.7926 -0.2088 -0.0499 0.0096 155 CYS A N 1210 C CA . CYS A 155 ? 0.9339 0.7074 0.7770 -0.2023 -0.0458 0.0030 155 CYS A CA 1211 C C . CYS A 155 ? 0.9253 0.6955 0.7728 -0.2014 -0.0299 0.0023 155 CYS A C 1212 O O . CYS A 155 ? 0.7003 0.4630 0.5361 -0.1912 -0.0244 0.0011 155 CYS A O 1213 C CB . CYS A 155 ? 0.7299 0.4771 0.5472 -0.2106 -0.0570 -0.0042 155 CYS A CB 1214 S SG . CYS A 155 ? 2.0551 1.7710 1.8419 -0.2020 -0.0532 -0.0108 155 CYS A SG 1215 N N . GLN A 156 ? 0.9355 0.7140 0.7997 -0.2130 -0.0224 0.0029 156 GLN A N 1216 C CA . GLN A 156 ? 0.8802 0.6554 0.7408 -0.2160 -0.0083 0.0007 156 GLN A CA 1217 C C . GLN A 156 ? 1.0017 0.7487 0.8286 -0.2162 -0.0133 -0.0006 156 GLN A C 1218 O O . GLN A 156 ? 1.1410 0.8822 0.9579 -0.2102 -0.0071 -0.0019 156 GLN A O 1219 C CB . GLN A 156 ? 0.6518 0.4397 0.5289 -0.2050 0.0037 -0.0013 156 GLN A CB 1220 C CG . GLN A 156 ? 0.6421 0.4562 0.5596 -0.2022 0.0086 0.0006 156 GLN A CG 1221 C CD . GLN A 156 ? 0.6854 0.5066 0.6224 -0.1923 0.0206 -0.0030 156 GLN A CD 1222 O OE1 . GLN A 156 ? 0.7460 0.5776 0.7082 -0.1826 0.0179 0.0023 156 GLN A OE1 1223 N NE2 . GLN A 156 ? 0.6804 0.4950 0.6056 -0.1958 0.0326 -0.0114 156 GLN A NE2 1224 N N . GLY A 157 ? 0.8494 0.5785 0.6623 -0.2231 -0.0261 -0.0001 157 GLY A N 1225 C CA . GLY A 157 ? 0.7621 0.4619 0.5494 -0.2223 -0.0329 -0.0007 157 GLY A CA 1226 C C . GLY A 157 ? 0.8717 0.5677 0.6519 -0.2314 -0.0254 0.0048 157 GLY A C 1227 O O . GLY A 157 ? 0.8872 0.5972 0.6766 -0.2456 -0.0179 0.0087 157 GLY A O 1228 N N . GLY A 158 ? 0.8664 0.5463 0.6304 -0.2238 -0.0273 0.0056 158 GLY A N 1229 C CA . GLY A 158 ? 0.7936 0.4712 0.5467 -0.2326 -0.0226 0.0121 158 GLY A CA 1230 C C . GLY A 158 ? 0.7773 0.4705 0.5330 -0.2247 -0.0117 0.0082 158 GLY A C 1231 O O . GLY A 158 ? 0.8598 0.5548 0.6043 -0.2321 -0.0075 0.0113 158 GLY A O 1232 N N . PHE A 159 ? 0.6892 0.3937 0.4591 -0.2112 -0.0084 0.0021 159 PHE A N 1233 C CA . PHE A 159 ? 0.7145 0.4311 0.4919 -0.2033 0.0000 -0.0014 159 PHE A CA 1234 C C . PHE A 159 ? 0.6871 0.3907 0.4494 -0.1989 -0.0055 0.0020 159 PHE A C 1235 O O . PHE A 159 ? 0.6463 0.3560 0.4065 -0.2018 -0.0006 0.0007 159 PHE A O 1236 C CB . PHE A 159 ? 0.8677 0.5953 0.6631 -0.1899 0.0010 -0.0036 159 PHE A CB 1237 C CG . PHE A 159 ? 0.7846 0.5260 0.5970 -0.1846 0.0102 -0.0063 159 PHE A CG 1238 C CD1 . PHE A 159 ? 0.6973 0.4532 0.5287 -0.1900 0.0209 -0.0116 159 PHE A CD1 1239 C CD2 . PHE A 159 ? 0.8140 0.5539 0.6272 -0.1740 0.0084 -0.0040 159 PHE A CD2 1240 C CE1 . PHE A 159 ? 0.8067 0.5706 0.6568 -0.1848 0.0283 -0.0161 159 PHE A CE1 1241 C CE2 . PHE A 159 ? 0.8003 0.5501 0.6322 -0.1708 0.0150 -0.0057 159 PHE A CE2 1242 C CZ . PHE A 159 ? 0.8523 0.6116 0.7023 -0.1761 0.0244 -0.0125 159 PHE A CZ 1243 N N . SER A 160 ? 0.7421 0.4283 0.4959 -0.1919 -0.0163 0.0053 160 SER A N 1244 C CA . SER A 160 ? 0.8038 0.4779 0.5490 -0.1868 -0.0234 0.0104 160 SER A CA 1245 C C . SER A 160 ? 0.9565 0.6057 0.6922 -0.1873 -0.0357 0.0148 160 SER A C 1246 O O . SER A 160 ? 1.2945 0.9348 1.0317 -0.1822 -0.0392 0.0094 160 SER A O 1247 C CB . SER A 160 ? 0.8490 0.5312 0.6050 -0.1700 -0.0216 0.0083 160 SER A CB 1248 O OG . SER A 160 ? 0.7056 0.3867 0.4645 -0.1593 -0.0224 0.0037 160 SER A OG 1249 N N . ILE A 161 ? 0.7497 0.3867 0.4763 -0.1939 -0.0436 0.0246 161 ILE A N 1250 C CA . ILE A 161 ? 0.7777 0.3874 0.4998 -0.1955 -0.0570 0.0313 161 ILE A CA 1251 C C . ILE A 161 ? 0.7938 0.3916 0.5176 -0.1882 -0.0678 0.0410 161 ILE A C 1252 O O . ILE A 161 ? 1.0140 0.6260 0.7367 -0.1892 -0.0666 0.0459 161 ILE A O 1253 C CB . ILE A 161 ? 0.8734 0.4771 0.5852 -0.2175 -0.0595 0.0405 161 ILE A CB 1254 C CG1 . ILE A 161 ? 0.8991 0.5203 0.5984 -0.2321 -0.0536 0.0482 161 ILE A CG1 1255 C CG2 . ILE A 161 ? 0.9806 0.5924 0.6979 -0.2235 -0.0527 0.0321 161 ILE A CG2 1256 C CD1 . ILE A 161 ? 1.1363 0.7581 0.8233 -0.2552 -0.0528 0.0587 161 ILE A CD1 1257 N N . ASP A 162 ? 0.8402 0.4112 0.5692 -0.1809 -0.0795 0.0431 162 ASP A N 1258 C CA . ASP A 162 ? 0.9729 0.5308 0.7105 -0.1727 -0.0919 0.0542 162 ASP A CA 1259 C C . ASP A 162 ? 1.0552 0.5770 0.7987 -0.1718 -0.1067 0.0594 162 ASP A C 1260 O O . ASP A 162 ? 1.0391 0.5454 0.7813 -0.1730 -0.1065 0.0491 162 ASP A O 1261 C CB . ASP A 162 ? 0.9629 0.5337 0.7171 -0.1500 -0.0866 0.0454 162 ASP A CB 1262 C CG . ASP A 162 ? 1.1338 0.7135 0.8973 -0.1475 -0.0945 0.0593 162 ASP A CG 1263 O OD1 . ASP A 162 ? 1.3090 0.8745 1.0691 -0.1577 -0.1090 0.0763 162 ASP A OD1 1264 O OD2 . ASP A 162 ? 1.2216 0.8237 0.9968 -0.1368 -0.0873 0.0552 162 ASP A OD2 1265 N N . PHE A 163 ? 1.0106 0.5183 0.7628 -0.1700 -0.1212 0.0759 163 PHE A N 1266 C CA . PHE A 163 ? 0.9620 0.4316 0.7269 -0.1669 -0.1375 0.0828 163 PHE A CA 1267 C C . PHE A 163 ? 1.0445 0.5041 0.8366 -0.1393 -0.1415 0.0755 163 PHE A C 1268 O O . PHE A 163 ? 1.1534 0.6371 0.9553 -0.1280 -0.1372 0.0767 163 PHE A O 1269 C CB . PHE A 163 ? 0.9853 0.4438 0.7433 -0.1872 -0.1537 0.1120 163 PHE A CB 1270 C CG . PHE A 163 ? 0.9189 0.3812 0.6537 -0.2149 -0.1504 0.1202 163 PHE A CG 1271 C CD1 . PHE A 163 ? 0.9059 0.3988 0.6178 -0.2328 -0.1422 0.1286 163 PHE A CD1 1272 C CD2 . PHE A 163 ? 1.1991 0.6353 0.9365 -0.2236 -0.1552 0.1186 163 PHE A CD2 1273 C CE1 . PHE A 163 ? 1.1082 0.6089 0.8012 -0.2574 -0.1361 0.1352 163 PHE A CE1 1274 C CE2 . PHE A 163 ? 1.2173 0.6615 0.9380 -0.2497 -0.1511 0.1279 163 PHE A CE2 1275 C CZ . PHE A 163 ? 1.1826 0.6607 0.8815 -0.2660 -0.1403 0.1362 163 PHE A CZ 1276 N N . THR A 164 ? 0.9237 0.3484 0.7307 -0.1287 -0.1495 0.0670 164 THR A N 1277 C CA . THR A 164 ? 1.0450 0.4572 0.8826 -0.1016 -0.1537 0.0602 164 THR A CA 1278 C C . THR A 164 ? 1.0774 0.4584 0.9362 -0.1038 -0.1769 0.0845 164 THR A C 1279 O O . THR A 164 ? 1.2084 0.5775 1.0538 -0.1278 -0.1891 0.1067 164 THR A O 1280 C CB . THR A 164 ? 1.0376 0.4310 0.8802 -0.0838 -0.1457 0.0292 164 THR A CB 1281 O OG1 . THR A 164 ? 1.0185 0.3709 0.8582 -0.0957 -0.1585 0.0282 164 THR A OG1 1282 C CG2 . THR A 164 ? 0.9273 0.3520 0.7471 -0.0842 -0.1255 0.0095 164 THR A CG2 1283 N N . LYS A 165 ? 0.9977 0.3671 0.8918 -0.0787 -0.1826 0.0817 165 LYS A N 1284 C CA . LYS A 165 ? 1.0473 0.3856 0.9695 -0.0774 -0.2067 0.1062 165 LYS A CA 1285 C C . LYS A 165 ? 1.2713 0.5583 1.1995 -0.0812 -0.2181 0.1007 165 LYS A C 1286 O O . LYS A 165 ? 1.3884 0.6437 1.3340 -0.0888 -0.2405 0.1258 165 LYS A O 1287 C CB . LYS A 165 ? 1.0809 0.4253 1.0470 -0.0468 -0.2088 0.1041 165 LYS A CB 1288 C CG . LYS A 165 ? 1.3123 0.7009 1.2819 -0.0482 -0.2087 0.1225 165 LYS A CG 1289 C CD . LYS A 165 ? 1.5912 0.9781 1.5480 -0.0746 -0.2311 0.1608 165 LYS A CD 1290 C CE . LYS A 165 ? 1.6346 1.0642 1.5924 -0.0780 -0.2336 0.1772 165 LYS A CE 1291 N NZ . LYS A 165 ? 1.5286 0.9957 1.4553 -0.0857 -0.2108 0.1592 165 LYS A NZ 1292 N N . ALA A 166 ? 1.3395 0.6187 1.2532 -0.0777 -0.2042 0.0690 166 ALA A N 1293 C CA . ALA A 166 ? 1.3874 0.6180 1.3058 -0.0819 -0.2143 0.0578 166 ALA A CA 1294 C C . ALA A 166 ? 1.2897 0.5193 1.1786 -0.1165 -0.2186 0.0729 166 ALA A C 1295 O O . ALA A 166 ? 1.2835 0.4963 1.1750 -0.1232 -0.2209 0.0628 166 ALA A O 1296 C CB . ALA A 166 ? 1.4993 0.7240 1.4154 -0.0615 -0.1985 0.0145 166 ALA A CB 1297 N N . ASP A 167 ? 1.2405 0.5058 1.1054 -0.1358 -0.2142 0.0944 167 ASP A N 1298 C CA . ASP A 167 ? 1.3215 0.6062 1.1597 -0.1657 -0.2100 0.1056 167 ASP A CA 1299 C C . ASP A 167 ? 1.1994 0.4856 1.0211 -0.1683 -0.1968 0.0763 167 ASP A C 1300 O O . ASP A 167 ? 1.3774 0.6585 1.1999 -0.1810 -0.1990 0.0740 167 ASP A O 1301 C CB . ASP A 167 ? 1.6680 0.9419 1.5200 -0.1799 -0.2246 0.1291 167 ASP A CB 1302 C CG . ASP A 167 ? 1.9292 1.2145 1.7860 -0.1864 -0.2374 0.1641 167 ASP A CG 1303 O OD1 . ASP A 167 ? 1.9504 1.2661 1.7813 -0.2095 -0.2341 0.1835 167 ASP A OD1 1304 O OD2 . ASP A 167 ? 2.0656 1.3316 1.9526 -0.1683 -0.2506 0.1714 167 ASP A OD2 1305 N N . ARG A 168 ? 1.0542 0.3645 0.8665 -0.1527 -0.1802 0.0538 168 ARG A N 1306 C CA . ARG A 168 ? 1.0421 0.3660 0.8369 -0.1544 -0.1667 0.0284 168 ARG A CA 1307 C C . ARG A 168 ? 1.0308 0.4045 0.8063 -0.1611 -0.1494 0.0315 168 ARG A C 1308 O O . ARG A 168 ? 1.1626 0.5611 0.9412 -0.1486 -0.1417 0.0344 168 ARG A O 1309 C CB . ARG A 168 ? 1.0203 0.3329 0.8230 -0.1272 -0.1608 -0.0043 168 ARG A CB 1310 C CG . ARG A 168 ? 1.0047 0.3350 0.7859 -0.1285 -0.1484 -0.0292 168 ARG A CG 1311 C CD . ARG A 168 ? 1.1091 0.4352 0.8921 -0.1016 -0.1399 -0.0609 168 ARG A CD 1312 N NE . ARG A 168 ? 1.2676 0.5446 1.0605 -0.0960 -0.1528 -0.0796 168 ARG A NE 1313 C CZ . ARG A 168 ? 1.2984 0.5585 1.0762 -0.1052 -0.1574 -0.1004 168 ARG A CZ 1314 N NH1 . ARG A 168 ? 1.2963 0.5871 1.0502 -0.1199 -0.1504 -0.1025 168 ARG A NH1 1315 N NH2 . ARG A 168 ? 1.3364 0.5480 1.1251 -0.1000 -0.1703 -0.1193 168 ARG A NH2 1316 N N . VAL A 169 ? 0.9530 0.3411 0.7128 -0.1810 -0.1440 0.0311 169 VAL A N 1317 C CA . VAL A 169 ? 0.9041 0.3361 0.6500 -0.1879 -0.1280 0.0335 169 VAL A CA 1318 C C . VAL A 169 ? 0.8782 0.3324 0.6201 -0.1713 -0.1140 0.0103 169 VAL A C 1319 O O . VAL A 169 ? 0.8883 0.3335 0.6267 -0.1696 -0.1147 -0.0071 169 VAL A O 1320 C CB . VAL A 169 ? 0.9444 0.3868 0.6806 -0.2152 -0.1263 0.0437 169 VAL A CB 1321 C CG1 . VAL A 169 ? 0.8603 0.3457 0.5878 -0.2180 -0.1083 0.0386 169 VAL A CG1 1322 C CG2 . VAL A 169 ? 0.9231 0.3561 0.6575 -0.2347 -0.1360 0.0715 169 VAL A CG2 1323 N N . LEU A 170 ? 0.8482 0.3317 0.5902 -0.1608 -0.1027 0.0113 170 LEU A N 1324 C CA . LEU A 170 ? 0.9124 0.4225 0.6505 -0.1489 -0.0888 -0.0046 170 LEU A CA 1325 C C . LEU A 170 ? 0.9980 0.5395 0.7295 -0.1630 -0.0785 0.0011 170 LEU A C 1326 O O . LEU A 170 ? 1.1249 0.6826 0.8568 -0.1689 -0.0744 0.0131 170 LEU A O 1327 C CB . LEU A 170 ? 0.8115 0.3343 0.5596 -0.1273 -0.0824 -0.0075 170 LEU A CB 1328 C CG . LEU A 170 ? 0.7853 0.3393 0.5298 -0.1170 -0.0674 -0.0187 170 LEU A CG 1329 C CD1 . LEU A 170 ? 0.9228 0.4689 0.6565 -0.1118 -0.0666 -0.0382 170 LEU A CD1 1330 C CD2 . LEU A 170 ? 0.7876 0.3580 0.5459 -0.0986 -0.0606 -0.0176 170 LEU A CD2 1331 N N . LEU A 171 ? 0.9878 0.5378 0.7148 -0.1684 -0.0752 -0.0083 171 LEU A N 1332 C CA . LEU A 171 ? 0.8601 0.4384 0.5876 -0.1807 -0.0659 -0.0038 171 LEU A CA 1333 C C . LEU A 171 ? 0.8701 0.4701 0.5984 -0.1717 -0.0585 -0.0146 171 LEU A C 1334 O O . LEU A 171 ? 0.9201 0.5129 0.6434 -0.1707 -0.0640 -0.0249 171 LEU A O 1335 C CB . LEU A 171 ? 1.0117 0.5830 0.7394 -0.2022 -0.0714 0.0024 171 LEU A CB 1336 C CG . LEU A 171 ? 1.0978 0.6985 0.8318 -0.2156 -0.0613 0.0059 171 LEU A CG 1337 C CD1 . LEU A 171 ? 1.3877 0.9839 1.1215 -0.2375 -0.0636 0.0188 171 LEU A CD1 1338 C CD2 . LEU A 171 ? 0.8304 0.4421 0.5705 -0.2149 -0.0624 -0.0039 171 LEU A CD2 1339 N N . GLY A 172 ? 0.8170 0.4430 0.5513 -0.1663 -0.0475 -0.0114 172 GLY A N 1340 C CA . GLY A 172 ? 0.8872 0.5358 0.6251 -0.1602 -0.0414 -0.0161 172 GLY A CA 1341 C C . GLY A 172 ? 0.8284 0.4986 0.5789 -0.1716 -0.0355 -0.0109 172 GLY A C 1342 O O . GLY A 172 ? 0.6741 0.3460 0.4291 -0.1831 -0.0321 -0.0054 172 GLY A O 1343 N N . GLY A 173 ? 0.7147 0.4030 0.4714 -0.1682 -0.0340 -0.0125 173 GLY A N 1344 C CA . GLY A 173 ? 0.7952 0.5071 0.5721 -0.1734 -0.0269 -0.0072 173 GLY A CA 1345 C C . GLY A 173 ? 0.9166 0.6475 0.7005 -0.1638 -0.0260 -0.0049 173 GLY A C 1346 O O . GLY A 173 ? 1.1044 0.8329 0.8734 -0.1585 -0.0328 -0.0086 173 GLY A O 1347 N N . PRO A 174 ? 0.7787 0.5282 0.5847 -0.1622 -0.0180 0.0013 174 PRO A N 1348 C CA . PRO A 174 ? 0.6679 0.4359 0.4856 -0.1539 -0.0171 0.0087 174 PRO A CA 1349 C C . PRO A 174 ? 0.7230 0.5057 0.5495 -0.1572 -0.0256 0.0134 174 PRO A C 1350 O O . PRO A 174 ? 0.9425 0.7372 0.7651 -0.1511 -0.0294 0.0204 174 PRO A O 1351 C CB . PRO A 174 ? 0.6802 0.4571 0.5240 -0.1535 -0.0070 0.0125 174 PRO A CB 1352 C CG . PRO A 174 ? 0.7314 0.5027 0.5798 -0.1641 -0.0028 0.0059 174 PRO A CG 1353 C CD . PRO A 174 ? 0.7774 0.5293 0.5980 -0.1688 -0.0088 0.0011 174 PRO A CD 1354 N N . GLY A 175 ? 0.6726 0.4569 0.5108 -0.1677 -0.0290 0.0114 175 GLY A N 1355 C CA . GLY A 175 ? 0.6842 0.4883 0.5433 -0.1713 -0.0369 0.0188 175 GLY A CA 1356 C C . GLY A 175 ? 0.7157 0.5195 0.5551 -0.1760 -0.0529 0.0173 175 GLY A C 1357 O O . GLY A 175 ? 0.7565 0.5795 0.6132 -0.1796 -0.0624 0.0256 175 GLY A O 1358 N N . SER A 176 ? 0.7435 0.5255 0.5487 -0.1762 -0.0571 0.0061 176 SER A N 1359 C CA . SER A 176 ? 0.8373 0.6146 0.6200 -0.1816 -0.0728 -0.0003 176 SER A CA 1360 C C . SER A 176 ? 0.8653 0.6617 0.6360 -0.1755 -0.0793 0.0063 176 SER A C 1361 O O . SER A 176 ? 0.8961 0.6982 0.6588 -0.1644 -0.0705 0.0109 176 SER A O 1362 C CB . SER A 176 ? 1.0038 0.7502 0.7548 -0.1802 -0.0746 -0.0162 176 SER A CB 1363 O OG . SER A 176 ? 1.0454 0.7739 0.8045 -0.1914 -0.0760 -0.0197 176 SER A OG 1364 N N . PHE A 177 ? 0.8463 0.6544 0.6159 -0.1846 -0.0957 0.0086 177 PHE A N 1365 C CA . PHE A 177 ? 0.8612 0.6889 0.6129 -0.1826 -0.1059 0.0160 177 PHE A CA 1366 C C . PHE A 177 ? 0.8846 0.7361 0.6600 -0.1741 -0.0984 0.0371 177 PHE A C 1367 O O . PHE A 177 ? 0.9541 0.8104 0.7090 -0.1652 -0.0917 0.0408 177 PHE A O 1368 C CB . PHE A 177 ? 0.8638 0.6765 0.5659 -0.1767 -0.1053 -0.0006 177 PHE A CB 1369 C CG . PHE A 177 ? 0.8657 0.6450 0.5502 -0.1805 -0.1075 -0.0230 177 PHE A CG 1370 C CD1 . PHE A 177 ? 0.8772 0.6340 0.5523 -0.1702 -0.0938 -0.0338 177 PHE A CD1 1371 C CD2 . PHE A 177 ? 0.8871 0.6574 0.5689 -0.1950 -0.1250 -0.0315 177 PHE A CD2 1372 C CE1 . PHE A 177 ? 0.9967 0.7205 0.6601 -0.1733 -0.0976 -0.0517 177 PHE A CE1 1373 C CE2 . PHE A 177 ? 1.0071 0.7434 0.6763 -0.1995 -0.1286 -0.0503 177 PHE A CE2 1374 C CZ . PHE A 177 ? 1.0899 0.8019 0.7504 -0.1882 -0.1149 -0.0600 177 PHE A CZ 1375 N N . TYR A 178 ? 0.8417 0.7084 0.6631 -0.1770 -0.0992 0.0508 178 TYR A N 1376 C CA . TYR A 178 ? 0.8528 0.7376 0.7067 -0.1692 -0.0930 0.0704 178 TYR A CA 1377 C C . TYR A 178 ? 0.8580 0.7306 0.7062 -0.1588 -0.0746 0.0676 178 TYR A C 1378 O O . TYR A 178 ? 0.7417 0.6246 0.5863 -0.1523 -0.0718 0.0805 178 TYR A O 1379 C CB . TYR A 178 ? 0.8238 0.7324 0.6693 -0.1698 -0.1078 0.0894 178 TYR A CB 1380 C CG . TYR A 178 ? 0.8438 0.7735 0.7219 -0.1781 -0.1261 0.1029 178 TYR A CG 1381 C CD1 . TYR A 178 ? 0.8330 0.7801 0.7667 -0.1739 -0.1262 0.1230 178 TYR A CD1 1382 C CD2 . TYR A 178 ? 0.9244 0.8565 0.7821 -0.1900 -0.1441 0.0951 178 TYR A CD2 1383 C CE1 . TYR A 178 ? 0.8773 0.8465 0.8479 -0.1800 -0.1433 0.1366 178 TYR A CE1 1384 C CE2 . TYR A 178 ? 0.9048 0.8597 0.7966 -0.1984 -0.1626 0.1091 178 TYR A CE2 1385 C CZ . TYR A 178 ? 0.8893 0.8642 0.8390 -0.1927 -0.1619 0.1307 178 TYR A CZ 1386 O OH . TYR A 178 ? 0.9529 0.9532 0.9436 -0.1995 -0.1806 0.1459 178 TYR A OH 1387 N N . TRP A 179 ? 0.9778 0.8300 0.8260 -0.1589 -0.0635 0.0522 179 TRP A N 1388 C CA . TRP A 179 ? 0.8650 0.7056 0.7129 -0.1512 -0.0479 0.0487 179 TRP A CA 1389 C C . TRP A 179 ? 0.8646 0.7021 0.6777 -0.1437 -0.0446 0.0469 179 TRP A C 1390 O O . TRP A 179 ? 0.8629 0.7018 0.6826 -0.1368 -0.0343 0.0524 179 TRP A O 1391 C CB . TRP A 179 ? 0.6590 0.5111 0.5493 -0.1471 -0.0410 0.0619 179 TRP A CB 1392 C CG . TRP A 179 ? 0.6316 0.4859 0.5577 -0.1521 -0.0383 0.0582 179 TRP A CG 1393 C CD1 . TRP A 179 ? 0.6059 0.4483 0.5403 -0.1543 -0.0261 0.0456 179 TRP A CD1 1394 C CD2 . TRP A 179 ? 0.6193 0.4920 0.5777 -0.1560 -0.0476 0.0672 179 TRP A CD2 1395 N NE1 . TRP A 179 ? 0.5955 0.4489 0.5646 -0.1589 -0.0244 0.0446 179 TRP A NE1 1396 C CE2 . TRP A 179 ? 0.6104 0.4826 0.5984 -0.1592 -0.0375 0.0580 179 TRP A CE2 1397 C CE3 . TRP A 179 ? 0.6053 0.4972 0.5711 -0.1573 -0.0638 0.0831 179 TRP A CE3 1398 C CZ2 . TRP A 179 ? 0.6151 0.5065 0.6448 -0.1623 -0.0415 0.0633 179 TRP A CZ2 1399 C CZ3 . TRP A 179 ? 0.6020 0.5117 0.6097 -0.1609 -0.0709 0.0901 179 TRP A CZ3 1400 C CH2 . TRP A 179 ? 0.5932 0.5030 0.6350 -0.1626 -0.0589 0.0799 179 TRP A CH2 1401 N N . GLN A 180 ? 0.8025 0.6365 0.5798 -0.1453 -0.0528 0.0379 180 GLN A N 1402 C CA . GLN A 180 ? 0.7480 0.5764 0.4912 -0.1371 -0.0464 0.0292 180 GLN A CA 1403 C C . GLN A 180 ? 0.7345 0.5388 0.4773 -0.1333 -0.0371 0.0157 180 GLN A C 1404 O O . GLN A 180 ? 0.7366 0.5400 0.4737 -0.1241 -0.0269 0.0146 180 GLN A O 1405 C CB . GLN A 180 ? 0.7457 0.5722 0.4498 -0.1399 -0.0570 0.0169 180 GLN A CB 1406 C CG . GLN A 180 ? 0.7582 0.6121 0.4497 -0.1427 -0.0659 0.0313 180 GLN A CG 1407 C CD . GLN A 180 ? 0.8102 0.6613 0.4559 -0.1461 -0.0759 0.0145 180 GLN A CD 1408 O OE1 . GLN A 180 ? 0.8326 0.6589 0.4573 -0.1437 -0.0739 -0.0093 180 GLN A OE1 1409 N NE2 . GLN A 180 ? 0.8208 0.6962 0.4509 -0.1522 -0.0879 0.0266 180 GLN A NE2 1410 N N . GLY A 181 ? 0.7225 0.5099 0.4733 -0.1413 -0.0415 0.0076 181 GLY A N 1411 C CA . GLY A 181 ? 0.7187 0.4826 0.4670 -0.1404 -0.0362 -0.0026 181 GLY A CA 1412 C C . GLY A 181 ? 0.8690 0.6102 0.5897 -0.1406 -0.0436 -0.0192 181 GLY A C 1413 O O . GLY A 181 ? 1.1297 0.8742 0.8275 -0.1383 -0.0493 -0.0262 181 GLY A O 1414 N N . GLN A 182 ? 0.9407 0.6581 0.6629 -0.1442 -0.0442 -0.0256 182 GLN A N 1415 C CA . GLN A 182 ? 0.9165 0.6064 0.6185 -0.1444 -0.0523 -0.0410 182 GLN A CA 1416 C C . GLN A 182 ? 0.9310 0.5974 0.6375 -0.1420 -0.0497 -0.0424 182 GLN A C 1417 O O . GLN A 182 ? 0.7569 0.4258 0.4794 -0.1481 -0.0456 -0.0321 182 GLN A O 1418 C CB . GLN A 182 ? 0.7938 0.4764 0.4955 -0.1599 -0.0660 -0.0444 182 GLN A CB 1419 C CG . GLN A 182 ? 0.8331 0.4839 0.5156 -0.1621 -0.0772 -0.0617 182 GLN A CG 1420 C CD . GLN A 182 ? 1.0531 0.6977 0.7405 -0.1805 -0.0920 -0.0629 182 GLN A CD 1421 O OE1 . GLN A 182 ? 0.9374 0.6007 0.6471 -0.1916 -0.0919 -0.0495 182 GLN A OE1 1422 N NE2 . GLN A 182 ? 1.3686 0.9875 1.0378 -0.1838 -0.1047 -0.0799 182 GLN A NE2 1423 N N . LEU A 183 ? 0.9828 0.6266 0.6751 -0.1329 -0.0524 -0.0556 183 LEU A N 1424 C CA . LEU A 183 ? 0.7932 0.4107 0.4917 -0.1316 -0.0547 -0.0555 183 LEU A CA 1425 C C . LEU A 183 ? 0.9000 0.4846 0.5910 -0.1399 -0.0686 -0.0662 183 LEU A C 1426 O O . LEU A 183 ? 1.1110 0.6849 0.7862 -0.1350 -0.0736 -0.0834 183 LEU A O 1427 C CB . LEU A 183 ? 0.7729 0.3894 0.4715 -0.1123 -0.0469 -0.0602 183 LEU A CB 1428 C CG . LEU A 183 ? 0.7429 0.3904 0.4519 -0.1042 -0.0340 -0.0492 183 LEU A CG 1429 C CD1 . LEU A 183 ? 0.7560 0.4003 0.4719 -0.0871 -0.0282 -0.0524 183 LEU A CD1 1430 C CD2 . LEU A 183 ? 0.7852 0.4425 0.5097 -0.1163 -0.0327 -0.0331 183 LEU A CD2 1431 N N . ILE A 184 ? 0.8247 0.3936 0.5262 -0.1538 -0.0750 -0.0562 184 ILE A N 1432 C CA . ILE A 184 ? 0.9456 0.4812 0.6449 -0.1646 -0.0895 -0.0625 184 ILE A CA 1433 C C . ILE A 184 ? 1.0104 0.5178 0.7186 -0.1640 -0.0944 -0.0544 184 ILE A C 1434 O O . ILE A 184 ? 1.1375 0.6554 0.8540 -0.1688 -0.0895 -0.0373 184 ILE A O 1435 C CB . ILE A 184 ? 0.8309 0.3755 0.5371 -0.1870 -0.0955 -0.0540 184 ILE A CB 1436 C CG1 . ILE A 184 ? 0.8137 0.3909 0.5171 -0.1871 -0.0919 -0.0569 184 ILE A CG1 1437 C CG2 . ILE A 184 ? 1.1103 0.6205 0.8157 -0.1997 -0.1122 -0.0608 184 ILE A CG2 1438 C CD1 . ILE A 184 ? 1.0801 0.6726 0.7978 -0.2071 -0.0969 -0.0480 184 ILE A CD1 1439 N N . SER A 185 ? 1.0420 0.5130 0.7488 -0.1583 -0.1049 -0.0670 185 SER A N 1440 C CA . SER A 185 ? 1.0627 0.5043 0.7820 -0.1558 -0.1121 -0.0576 185 SER A CA 1441 C C . SER A 185 ? 1.1109 0.5104 0.8351 -0.1686 -0.1299 -0.0601 185 SER A C 1442 O O . SER A 185 ? 1.1641 0.5450 0.8809 -0.1674 -0.1368 -0.0813 185 SER A O 1443 C CB . SER A 185 ? 1.0920 0.5286 0.8158 -0.1296 -0.1063 -0.0684 185 SER A CB 1444 O OG . SER A 185 ? 1.0717 0.4879 0.8129 -0.1266 -0.1134 -0.0537 185 SER A OG 1445 N N . ASP A 186 ? 0.9671 0.3513 0.7029 -0.1823 -0.1380 -0.0379 186 ASP A N 1446 C CA . ASP A 186 ? 1.0377 0.3825 0.7828 -0.1974 -0.1558 -0.0340 186 ASP A CA 1447 C C . ASP A 186 ? 1.0833 0.4083 0.8469 -0.1949 -0.1640 -0.0135 186 ASP A C 1448 O O . ASP A 186 ? 1.0116 0.3480 0.7730 -0.1946 -0.1599 0.0045 186 ASP A O 1449 C CB . ASP A 186 ? 1.0842 0.4566 0.8330 -0.2216 -0.1550 -0.0203 186 ASP A CB 1450 C CG . ASP A 186 ? 1.2998 0.6872 1.0383 -0.2254 -0.1533 -0.0393 186 ASP A CG 1451 O OD1 . ASP A 186 ? 1.4596 0.8299 1.2029 -0.2269 -0.1640 -0.0538 186 ASP A OD1 1452 O OD2 . ASP A 186 ? 1.3958 0.8144 1.1235 -0.2266 -0.1419 -0.0392 186 ASP A OD2 1453 N N . GLN A 187 ? 1.1482 0.4438 0.9306 -0.1938 -0.1768 -0.0159 187 GLN A N 1454 C CA . GLN A 187 ? 1.0928 0.3696 0.8962 -0.1939 -0.1873 0.0069 187 GLN A CA 1455 C C . GLN A 187 ? 1.0751 0.3771 0.8776 -0.2192 -0.1876 0.0387 187 GLN A C 1456 O O . GLN A 187 ? 1.0681 0.3844 0.8692 -0.2367 -0.1864 0.0400 187 GLN A O 1457 C CB . GLN A 187 ? 1.1622 0.3996 0.9879 -0.1867 -0.2002 -0.0055 187 GLN A CB 1458 C CG . GLN A 187 ? 1.2784 0.4926 1.1023 -0.1621 -0.1977 -0.0430 187 GLN A CG 1459 C CD . GLN A 187 ? 1.3827 0.5598 1.2272 -0.1577 -0.2086 -0.0597 187 GLN A CD 1460 O OE1 . GLN A 187 ? 1.4998 0.6676 1.3601 -0.1746 -0.2191 -0.0421 187 GLN A OE1 1461 N NE2 . GLN A 187 ? 1.4162 0.5723 1.2597 -0.1350 -0.2051 -0.0948 187 GLN A NE2 1462 N N . VAL A 188 ? 1.0649 0.3743 0.8679 -0.2212 -0.1891 0.0639 188 VAL A N 1463 C CA . VAL A 188 ? 1.0588 0.3945 0.8553 -0.2449 -0.1878 0.0930 188 VAL A CA 1464 C C . VAL A 188 ? 1.1349 0.4579 0.9474 -0.2603 -0.1986 0.1049 188 VAL A C 1465 O O . VAL A 188 ? 1.0873 0.4342 0.8946 -0.2806 -0.1930 0.1132 188 VAL A O 1466 C CB . VAL A 188 ? 1.0599 0.4010 0.8535 -0.2440 -0.1921 0.1178 188 VAL A CB 1467 C CG1 . VAL A 188 ? 1.0682 0.4326 0.8532 -0.2693 -0.1929 0.1473 188 VAL A CG1 1468 C CG2 . VAL A 188 ? 1.1603 0.5208 0.9365 -0.2347 -0.1801 0.1097 188 VAL A CG2 1469 N N . ALA A 189 ? 1.1521 0.4375 0.9869 -0.2502 -0.2136 0.1054 189 ALA A N 1470 C CA . ALA A 189 ? 1.4289 0.6961 1.2823 -0.2638 -0.2256 0.1162 189 ALA A CA 1471 C C . ALA A 189 ? 1.3580 0.6274 1.2117 -0.2722 -0.2222 0.0951 189 ALA A C 1472 O O . ALA A 189 ? 1.5226 0.7962 1.3846 -0.2922 -0.2266 0.1079 189 ALA A O 1473 C CB . ALA A 189 ? 1.7688 0.9917 1.6489 -0.2475 -0.2414 0.1148 189 ALA A CB 1474 N N . GLU A 190 ? 1.2219 0.4901 1.0667 -0.2574 -0.2151 0.0637 190 GLU A N 1475 C CA . GLU A 190 ? 1.1971 0.4698 1.0400 -0.2644 -0.2137 0.0423 190 GLU A CA 1476 C C . GLU A 190 ? 1.1194 0.4374 0.9500 -0.2838 -0.2021 0.0534 190 GLU A C 1477 O O . GLU A 190 ? 1.1267 0.4541 0.9644 -0.2992 -0.2044 0.0514 190 GLU A O 1478 C CB . GLU A 190 ? 1.2371 0.4975 1.0698 -0.2428 -0.2100 0.0061 190 GLU A CB 1479 C CG . GLU A 190 ? 1.4421 0.6748 1.2837 -0.2409 -0.2195 -0.0205 190 GLU A CG 1480 C CD . GLU A 190 ? 1.6984 0.9562 1.5318 -0.2576 -0.2182 -0.0290 190 GLU A CD 1481 O OE1 . GLU A 190 ? 1.7238 0.9634 1.5675 -0.2648 -0.2287 -0.0422 190 GLU A OE1 1482 O OE2 . GLU A 190 ? 1.9101 1.2055 1.7286 -0.2634 -0.2072 -0.0227 190 GLU A OE2 1483 N N . ILE A 191 ? 1.0819 0.4279 0.8963 -0.2830 -0.1898 0.0644 191 ILE A N 1484 C CA . ILE A 191 ? 1.0475 0.4371 0.8520 -0.2993 -0.1761 0.0734 191 ILE A CA 1485 C C . ILE A 191 ? 1.0650 0.4684 0.8799 -0.3233 -0.1779 0.0996 191 ILE A C 1486 O O . ILE A 191 ? 1.3921 0.8185 1.2137 -0.3386 -0.1733 0.1001 191 ILE A O 1487 C CB . ILE A 191 ? 1.0815 0.4950 0.8667 -0.2937 -0.1623 0.0791 191 ILE A CB 1488 C CG1 . ILE A 191 ? 1.1401 0.5458 0.9149 -0.2720 -0.1582 0.0541 191 ILE A CG1 1489 C CG2 . ILE A 191 ? 0.9828 0.4403 0.7614 -0.3111 -0.1468 0.0882 191 ILE A CG2 1490 C CD1 . ILE A 191 ? 1.0994 0.5253 0.8577 -0.2663 -0.1458 0.0588 191 ILE A CD1 1491 N N . VAL A 192 ? 1.0901 0.4807 0.9076 -0.3270 -0.1851 0.1224 192 VAL A N 1492 C CA . VAL A 192 ? 1.1118 0.5167 0.9354 -0.3504 -0.1865 0.1502 192 VAL A CA 1493 C C . VAL A 192 ? 1.3038 0.6866 1.1516 -0.3604 -0.1999 0.1502 192 VAL A C 1494 O O . VAL A 192 ? 1.2911 0.6957 1.1470 -0.3813 -0.1965 0.1627 192 VAL A O 1495 C CB . VAL A 192 ? 1.1325 0.5311 0.9492 -0.3521 -0.1927 0.1768 192 VAL A CB 1496 C CG1 . VAL A 192 ? 1.2598 0.6141 1.0887 -0.3315 -0.2088 0.1709 192 VAL A CG1 1497 C CG2 . VAL A 192 ? 1.2257 0.6344 1.0488 -0.3767 -0.1968 0.2064 192 VAL A CG2 1498 N N . SER A 193 ? 1.1780 0.5181 1.0385 -0.3455 -0.2142 0.1347 193 SER A N 1499 C CA . SER A 193 ? 1.4057 0.7188 1.2895 -0.3544 -0.2286 0.1326 193 SER A CA 1500 C C . SER A 193 ? 1.3903 0.7179 1.2786 -0.3624 -0.2258 0.1130 193 SER A C 1501 O O . SER A 193 ? 1.4941 0.8176 1.4005 -0.3796 -0.2339 0.1192 193 SER A O 1502 C CB . SER A 193 ? 1.2583 0.5208 1.1545 -0.3345 -0.2430 0.1169 193 SER A CB 1503 O OG . SER A 193 ? 1.2377 0.4929 1.1235 -0.3133 -0.2380 0.0831 193 SER A OG 1504 N N . LYS A 194 ? 1.2796 0.6250 1.1526 -0.3508 -0.2155 0.0908 194 LYS A N 1505 C CA . LYS A 194 ? 1.2199 0.5803 1.0965 -0.3568 -0.2151 0.0717 194 LYS A CA 1506 C C . LYS A 194 ? 1.1972 0.6080 1.0739 -0.3738 -0.2010 0.0854 194 LYS A C 1507 O O . LYS A 194 ? 1.2319 0.6615 1.1147 -0.3799 -0.2006 0.0733 194 LYS A O 1508 C CB . LYS A 194 ? 1.1439 0.4958 1.0042 -0.3352 -0.2134 0.0395 194 LYS A CB 1509 C CG . LYS A 194 ? 1.1964 0.5032 1.0615 -0.3225 -0.2276 0.0141 194 LYS A CG 1510 C CD . LYS A 194 ? 1.3202 0.6228 1.1985 -0.3374 -0.2392 0.0029 194 LYS A CD 1511 C CE . LYS A 194 ? 1.5193 0.7808 1.3956 -0.3236 -0.2506 -0.0302 194 LYS A CE 1512 N NZ . LYS A 194 ? 1.6957 0.9137 1.5843 -0.3130 -0.2573 -0.0274 194 LYS A NZ 1513 N N . TYR A 195 ? 1.1127 0.5465 0.9834 -0.3819 -0.1896 0.1101 195 TYR A N 1514 C CA . TYR A 195 ? 1.1010 0.5841 0.9714 -0.3954 -0.1724 0.1196 195 TYR A CA 1515 C C . TYR A 195 ? 1.1004 0.6018 0.9949 -0.4197 -0.1741 0.1347 195 TYR A C 1516 O O . TYR A 195 ? 1.3596 0.8533 1.2619 -0.4332 -0.1790 0.1570 195 TYR A O 1517 C CB . TYR A 195 ? 1.0630 0.5663 0.9146 -0.3961 -0.1578 0.1374 195 TYR A CB 1518 C CG . TYR A 195 ? 1.0397 0.5933 0.8933 -0.4123 -0.1381 0.1480 195 TYR A CG 1519 C CD1 . TYR A 195 ? 1.0610 0.6344 0.9182 -0.4326 -0.1320 0.1738 195 TYR A CD1 1520 C CD2 . TYR A 195 ? 1.2098 0.7919 1.0634 -0.4072 -0.1251 0.1320 195 TYR A CD2 1521 C CE1 . TYR A 195 ? 1.0435 0.6649 0.9040 -0.4468 -0.1112 0.1811 195 TYR A CE1 1522 C CE2 . TYR A 195 ? 1.2190 0.8474 1.0798 -0.4208 -0.1055 0.1397 195 TYR A CE2 1523 C CZ . TYR A 195 ? 1.2516 0.9000 1.1157 -0.4402 -0.0976 0.1631 195 TYR A CZ 1524 O OH . TYR A 195 ? 1.2758 0.9725 1.1481 -0.4530 -0.0753 0.1685 195 TYR A OH 1525 N N . ASP A 196 ? 1.0822 0.6094 0.9902 -0.4257 -0.1708 0.1238 196 ASP A N 1526 C CA . ASP A 196 ? 1.0958 0.6491 1.0309 -0.4490 -0.1700 0.1376 196 ASP A CA 1527 C C . ASP A 196 ? 1.1806 0.7887 1.1220 -0.4564 -0.1481 0.1425 196 ASP A C 1528 O O . ASP A 196 ? 1.2490 0.8732 1.1905 -0.4471 -0.1438 0.1252 196 ASP A O 1529 C CB . ASP A 196 ? 1.1173 0.6535 1.0709 -0.4523 -0.1886 0.1212 196 ASP A CB 1530 C CG . ASP A 196 ? 1.3941 0.9524 1.3792 -0.4775 -0.1911 0.1374 196 ASP A CG 1531 O OD1 . ASP A 196 ? 1.5790 1.1786 1.5815 -0.4858 -0.1828 0.1365 196 ASP A OD1 1532 O OD2 . ASP A 196 ? 1.5054 1.0405 1.5006 -0.4892 -0.2016 0.1519 196 ASP A OD2 1533 N N . PRO A 197 ? 1.0639 0.7016 1.0114 -0.4732 -0.1336 0.1660 197 PRO A N 1534 C CA . PRO A 197 ? 1.0327 0.7241 0.9878 -0.4803 -0.1089 0.1703 197 PRO A CA 1535 C C . PRO A 197 ? 1.2078 0.9300 1.1980 -0.4881 -0.1085 0.1626 197 PRO A C 1536 O O . PRO A 197 ? 1.2845 1.0486 1.2859 -0.4880 -0.0899 0.1592 197 PRO A O 1537 C CB . PRO A 197 ? 1.0596 0.7701 1.0144 -0.4994 -0.0974 0.1977 197 PRO A CB 1538 C CG . PRO A 197 ? 1.3465 1.0205 1.3106 -0.5084 -0.1196 0.2094 197 PRO A CG 1539 C CD . PRO A 197 ? 1.2332 0.8561 1.1829 -0.4879 -0.1399 0.1902 197 PRO A CD 1540 N N . ASN A 198 ? 1.0455 0.7475 1.0548 -0.4949 -0.1296 0.1598 198 ASN A N 1541 C CA . ASN A 198 ? 1.0379 0.7676 1.0816 -0.5035 -0.1341 0.1534 198 ASN A CA 1542 C C . ASN A 198 ? 1.0198 0.7337 1.0558 -0.4870 -0.1486 0.1278 198 ASN A C 1543 O O . ASN A 198 ? 1.1822 0.9137 1.2432 -0.4930 -0.1584 0.1211 198 ASN A O 1544 C CB . ASN A 198 ? 1.1053 0.8261 1.1750 -0.5234 -0.1496 0.1652 198 ASN A CB 1545 C CG . ASN A 198 ? 1.2628 1.0076 1.3440 -0.5428 -0.1343 0.1931 198 ASN A CG 1546 O OD1 . ASN A 198 ? 1.4095 1.1947 1.4904 -0.5450 -0.1089 0.2020 198 ASN A OD1 1547 N ND2 . ASN A 198 ? 1.2811 1.0014 1.3719 -0.5574 -0.1492 0.2066 198 ASN A ND2 1548 N N . VAL A 199 ? 1.0098 0.6918 1.0110 -0.4670 -0.1509 0.1144 199 VAL A N 1549 C CA . VAL A 199 ? 1.0694 0.7372 1.0576 -0.4509 -0.1627 0.0904 199 VAL A CA 1550 C C . VAL A 199 ? 0.9556 0.6338 0.9217 -0.4337 -0.1466 0.0832 199 VAL A C 1551 O O . VAL A 199 ? 1.0441 0.7007 0.9836 -0.4229 -0.1402 0.0843 199 VAL A O 1552 C CB . VAL A 199 ? 1.2690 0.8820 1.2371 -0.4416 -0.1842 0.0755 199 VAL A CB 1553 C CG1 . VAL A 199 ? 1.4648 1.0657 1.4124 -0.4241 -0.1928 0.0502 199 VAL A CG1 1554 C CG2 . VAL A 199 ? 1.1895 0.7904 1.1811 -0.4591 -0.2021 0.0790 199 VAL A CG2 1555 N N . TYR A 200 ? 1.0844 0.7960 1.0641 -0.4318 -0.1414 0.0768 200 TYR A N 1556 C CA . TYR A 200 ? 1.0451 0.7713 1.0107 -0.4181 -0.1249 0.0713 200 TYR A CA 1557 C C . TYR A 200 ? 1.1144 0.8065 1.0465 -0.3981 -0.1356 0.0522 200 TYR A C 1558 O O . TYR A 200 ? 1.0879 0.7733 0.9973 -0.3849 -0.1237 0.0488 200 TYR A O 1559 C CB . TYR A 200 ? 0.9031 0.6795 0.9030 -0.4241 -0.1155 0.0736 200 TYR A CB 1560 C CG . TYR A 200 ? 0.8782 0.6939 0.9158 -0.4432 -0.1024 0.0910 200 TYR A CG 1561 C CD1 . TYR A 200 ? 0.8615 0.6917 0.8947 -0.4484 -0.0788 0.1031 200 TYR A CD1 1562 C CD2 . TYR A 200 ? 1.0122 0.8525 1.0890 -0.4568 -0.1136 0.0955 200 TYR A CD2 1563 C CE1 . TYR A 200 ? 0.8690 0.7380 0.9349 -0.4661 -0.0644 0.1186 200 TYR A CE1 1564 C CE2 . TYR A 200 ? 0.8777 0.7570 0.9920 -0.4740 -0.0999 0.1117 200 TYR A CE2 1565 C CZ . TYR A 200 ? 0.9006 0.7943 1.0089 -0.4784 -0.0742 0.1230 200 TYR A CZ 1566 O OH . TYR A 200 ? 0.8895 0.8249 1.0334 -0.4957 -0.0581 0.1387 200 TYR A OH 1567 N N . SER A 201 ? 1.0962 0.7686 1.0247 -0.3967 -0.1575 0.0389 201 SER A N 1568 C CA . SER A 201 ? 1.0105 0.6505 0.9052 -0.3785 -0.1671 0.0191 201 SER A CA 1569 C C . SER A 201 ? 1.1161 0.7098 0.9955 -0.3746 -0.1802 0.0114 201 SER A C 1570 O O . SER A 201 ? 1.2774 0.8590 1.1664 -0.3835 -0.1973 0.0056 201 SER A O 1571 C CB . SER A 201 ? 0.9774 0.6308 0.8733 -0.3785 -0.1817 0.0066 201 SER A CB 1572 O OG . SER A 201 ? 1.0097 0.7068 0.9280 -0.3825 -0.1712 0.0157 201 SER A OG 1573 N N . ILE A 202 ? 1.2345 0.8026 1.0929 -0.3612 -0.1729 0.0109 202 ILE A N 1574 C CA . ILE A 202 ? 1.2237 0.7492 1.0757 -0.3573 -0.1835 0.0072 202 ILE A CA 1575 C C . ILE A 202 ? 1.1937 0.6855 1.0189 -0.3367 -0.1907 -0.0173 202 ILE A C 1576 O O . ILE A 202 ? 1.1887 0.6794 0.9945 -0.3211 -0.1805 -0.0218 202 ILE A O 1577 C CB . ILE A 202 ? 1.1381 0.6581 0.9908 -0.3586 -0.1728 0.0276 202 ILE A CB 1578 C CG1 . ILE A 202 ? 1.0648 0.6184 0.9415 -0.3802 -0.1644 0.0509 202 ILE A CG1 1579 C CG2 . ILE A 202 ? 1.1321 0.6065 0.9822 -0.3532 -0.1855 0.0251 202 ILE A CG2 1580 C CD1 . ILE A 202 ? 1.2017 0.7565 1.0738 -0.3843 -0.1532 0.0723 202 ILE A CD1 1581 N N . LYS A 203 ? 1.3158 0.7809 1.1407 -0.3371 -0.2075 -0.0342 203 LYS A N 1582 C CA . LYS A 203 ? 1.3498 0.7824 1.1505 -0.3180 -0.2132 -0.0609 203 LYS A CA 1583 C C . LYS A 203 ? 1.2962 0.6923 1.0975 -0.3064 -0.2116 -0.0586 203 LYS A C 1584 O O . LYS A 203 ? 1.4500 0.8260 1.2706 -0.3156 -0.2196 -0.0494 203 LYS A O 1585 C CB . LYS A 203 ? 1.5360 0.9552 1.3352 -0.3236 -0.2312 -0.0829 203 LYS A CB 1586 C CG . LYS A 203 ? 1.5435 0.9573 1.3722 -0.3444 -0.2429 -0.0716 203 LYS A CG 1587 C CD . LYS A 203 ? 1.5161 0.9220 1.3426 -0.3522 -0.2613 -0.0940 203 LYS A CD 1588 C CE . LYS A 203 ? 1.5081 0.9119 1.3666 -0.3752 -0.2731 -0.0807 203 LYS A CE 1589 N NZ . LYS A 203 ? 1.4021 0.7988 1.2590 -0.3846 -0.2925 -0.1028 203 LYS A NZ 1590 N N . TYR A 204 ? 1.2310 0.6192 1.0135 -0.2868 -0.2020 -0.0655 204 TYR A N 1591 C CA . TYR A 204 ? 1.3488 0.7048 1.1346 -0.2740 -0.2013 -0.0625 204 TYR A CA 1592 C C . TYR A 204 ? 1.4657 0.7868 1.2394 -0.2543 -0.2068 -0.0939 204 TYR A C 1593 O O . TYR A 204 ? 1.6393 0.9676 1.3891 -0.2424 -0.2024 -0.1152 204 TYR A O 1594 C CB . TYR A 204 ? 1.2194 0.5907 0.9969 -0.2659 -0.1866 -0.0464 204 TYR A CB 1595 C CG . TYR A 204 ? 1.0717 0.4755 0.8598 -0.2837 -0.1784 -0.0171 204 TYR A CG 1596 C CD1 . TYR A 204 ? 1.0934 0.5361 0.8759 -0.2900 -0.1672 -0.0133 204 TYR A CD1 1597 C CD2 . TYR A 204 ? 1.0747 0.4709 0.8782 -0.2943 -0.1813 0.0062 204 TYR A CD2 1598 C CE1 . TYR A 204 ? 1.1463 0.6198 0.9391 -0.3052 -0.1570 0.0098 204 TYR A CE1 1599 C CE2 . TYR A 204 ? 1.1633 0.5917 0.9724 -0.3109 -0.1717 0.0308 204 TYR A CE2 1600 C CZ . TYR A 204 ? 1.2102 0.6772 1.0141 -0.3158 -0.1586 0.0308 204 TYR A CZ 1601 O OH . TYR A 204 ? 1.2384 0.7382 1.0484 -0.3315 -0.1466 0.0518 204 TYR A OH 1602 N N . ASN A 205 ? 1.2201 0.5041 1.0106 -0.2511 -0.2158 -0.0970 205 ASN A N 1603 C CA . ASN A 205 ? 1.2683 0.5172 1.0521 -0.2304 -0.2184 -0.1280 205 ASN A CA 1604 C C . ASN A 205 ? 1.2368 0.4794 1.0132 -0.2078 -0.2074 -0.1280 205 ASN A C 1605 O O . ASN A 205 ? 1.3061 0.5594 1.0904 -0.2101 -0.2025 -0.1000 205 ASN A O 1606 C CB . ASN A 205 ? 1.4228 0.6321 1.2318 -0.2345 -0.2314 -0.1310 205 ASN A CB 1607 C CG . ASN A 205 ? 1.5171 0.7280 1.3321 -0.2553 -0.2436 -0.1376 205 ASN A CG 1608 O OD1 . ASN A 205 ? 1.5307 0.7599 1.3266 -0.2585 -0.2447 -0.1569 205 ASN A OD1 1609 N ND2 . ASN A 205 ? 1.6747 0.8673 1.5165 -0.2705 -0.2541 -0.1201 205 ASN A ND2 1610 N N . ASN A 206 ? 1.2626 0.4897 1.0235 -0.1863 -0.2032 -0.1600 206 ASN A N 1611 C CA . ASN A 206 ? 1.3698 0.5919 1.1240 -0.1626 -0.1921 -0.1641 206 ASN A CA 1612 C C . ASN A 206 ? 1.3399 0.5981 1.0764 -0.1654 -0.1808 -0.1457 206 ASN A C 1613 O O . ASN A 206 ? 1.2937 0.5519 1.0363 -0.1567 -0.1750 -0.1293 206 ASN A O 1614 C CB . ASN A 206 ? 1.3480 0.5404 1.1336 -0.1543 -0.1969 -0.1478 206 ASN A CB 1615 C CG . ASN A 206 ? 1.5596 0.7154 1.3686 -0.1570 -0.2093 -0.1580 206 ASN A CG 1616 O OD1 . ASN A 206 ? 1.8514 0.9806 1.6616 -0.1393 -0.2084 -0.1900 206 ASN A OD1 1617 N ND2 . ASN A 206 ? 1.5338 0.6884 1.3613 -0.1794 -0.2198 -0.1314 206 ASN A ND2 1618 N N . GLN A 207 ? 1.2106 0.4995 0.9272 -0.1782 -0.1784 -0.1479 207 GLN A N 1619 C CA . GLN A 207 ? 1.1760 0.4985 0.8767 -0.1811 -0.1668 -0.1333 207 GLN A CA 1620 C C . GLN A 207 ? 1.1919 0.5346 0.8696 -0.1590 -0.1525 -0.1541 207 GLN A C 1621 O O . GLN A 207 ? 1.2777 0.6182 0.9341 -0.1556 -0.1550 -0.1803 207 GLN A O 1622 C CB . GLN A 207 ? 1.2735 0.6292 0.9745 -0.2044 -0.1691 -0.1198 207 GLN A CB 1623 C CG . GLN A 207 ? 1.2889 0.6877 0.9822 -0.2047 -0.1541 -0.1053 207 GLN A CG 1624 C CD . GLN A 207 ? 1.1987 0.6261 0.8998 -0.2279 -0.1567 -0.0904 207 GLN A CD 1625 O OE1 . GLN A 207 ? 1.2056 0.6582 0.8976 -0.2301 -0.1571 -0.0982 207 GLN A OE1 1626 N NE2 . GLN A 207 ? 1.1874 0.6191 0.9093 -0.2430 -0.1566 -0.0669 207 GLN A NE2 1627 N N . LEU A 208 ? 1.0377 0.4064 0.7211 -0.1442 -0.1366 -0.1409 208 LEU A N 1628 C CA . LEU A 208 ? 1.0360 0.4354 0.7041 -0.1237 -0.1197 -0.1536 208 LEU A CA 1629 C C . LEU A 208 ? 1.1477 0.5960 0.8108 -0.1313 -0.1094 -0.1354 208 LEU A C 1630 O O . LEU A 208 ? 1.2911 0.7559 0.9694 -0.1353 -0.1037 -0.1120 208 LEU A O 1631 C CB . LEU A 208 ? 1.0181 0.4129 0.7018 -0.1004 -0.1096 -0.1527 208 LEU A CB 1632 C CG . LEU A 208 ? 1.0688 0.4146 0.7662 -0.0883 -0.1189 -0.1697 208 LEU A CG 1633 C CD1 . LEU A 208 ? 1.0593 0.4074 0.7810 -0.0671 -0.1104 -0.1606 208 LEU A CD1 1634 C CD2 . LEU A 208 ? 1.1158 0.4470 0.7914 -0.0777 -0.1181 -0.2079 208 LEU A CD2 1635 N N . ALA A 209 ? 1.1613 0.6319 0.8033 -0.1336 -0.1080 -0.1465 209 ALA A N 1636 C CA . ALA A 209 ? 1.0756 0.5901 0.7172 -0.1403 -0.1003 -0.1291 209 ALA A CA 1637 C C . ALA A 209 ? 1.0667 0.6100 0.6846 -0.1294 -0.0916 -0.1403 209 ALA A C 1638 O O . ALA A 209 ? 1.1694 0.7010 0.7633 -0.1256 -0.0965 -0.1642 209 ALA A O 1639 C CB . ALA A 209 ? 1.0311 0.5490 0.6796 -0.1644 -0.1131 -0.1190 209 ALA A CB 1640 N N . THR A 210 ? 0.9313 0.5120 0.5551 -0.1252 -0.0790 -0.1230 210 THR A N 1641 C CA . THR A 210 ? 0.9614 0.5744 0.5647 -0.1181 -0.0713 -0.1262 210 THR A CA 1642 C C . THR A 210 ? 0.9771 0.6047 0.5699 -0.1349 -0.0843 -0.1232 210 THR A C 1643 O O . THR A 210 ? 1.1288 0.7562 0.7413 -0.1504 -0.0932 -0.1100 210 THR A O 1644 C CB . THR A 210 ? 0.9412 0.5875 0.5595 -0.1098 -0.0553 -0.1057 210 THR A CB 1645 O OG1 . THR A 210 ? 0.9068 0.5693 0.5454 -0.1234 -0.0585 -0.0843 210 THR A OG1 1646 C CG2 . THR A 210 ? 0.9436 0.5774 0.5797 -0.0968 -0.0459 -0.1039 210 THR A CG2 1647 N N . ARG A 211 ? 1.0158 0.6589 0.5781 -0.1323 -0.0855 -0.1349 211 ARG A N 1648 C CA . ARG A 211 ? 1.1523 0.8119 0.7032 -0.1483 -0.1009 -0.1311 211 ARG A CA 1649 C C . ARG A 211 ? 1.0631 0.7661 0.6219 -0.1486 -0.0950 -0.1057 211 ARG A C 1650 O O . ARG A 211 ? 1.1648 0.8830 0.7365 -0.1371 -0.0787 -0.0928 211 ARG A O 1651 C CB . ARG A 211 ? 1.4388 1.0891 0.9471 -0.1486 -0.1096 -0.1591 211 ARG A CB 1652 C CG . ARG A 211 ? 1.5294 1.1319 1.0322 -0.1487 -0.1179 -0.1869 211 ARG A CG 1653 C CD . ARG A 211 ? 1.5771 1.1702 1.0348 -0.1470 -0.1241 -0.2196 211 ARG A CD 1654 N NE . ARG A 211 ? 1.6742 1.2867 1.1070 -0.1270 -0.1031 -0.2300 211 ARG A NE 1655 C CZ . ARG A 211 ? 1.8698 1.4814 1.2588 -0.1216 -0.1013 -0.2601 211 ARG A CZ 1656 N NH1 . ARG A 211 ? 1.9843 1.5731 1.3481 -0.1354 -0.1217 -0.2842 211 ARG A NH1 1657 N NH2 . ARG A 211 ? 1.8951 1.5300 1.2650 -0.1034 -0.0788 -0.2669 211 ARG A NH2 1658 N N . THR A 212 ? 0.9747 0.6970 0.5290 -0.1622 -0.1101 -0.0975 212 THR A N 1659 C CA . THR A 212 ? 0.9579 0.7198 0.5208 -0.1627 -0.1079 -0.0722 212 THR A CA 1660 C C . THR A 212 ? 1.0165 0.7984 0.5426 -0.1522 -0.0983 -0.0761 212 THR A C 1661 O O . THR A 212 ? 1.1637 0.9320 0.6524 -0.1476 -0.0973 -0.1021 212 THR A O 1662 C CB . THR A 212 ? 1.0218 0.8009 0.5931 -0.1800 -0.1293 -0.0606 212 THR A CB 1663 O OG1 . THR A 212 ? 1.0461 0.8624 0.6297 -0.1789 -0.1281 -0.0337 212 THR A OG1 1664 C CG2 . THR A 212 ? 1.1911 0.9625 0.7199 -0.1890 -0.1467 -0.0824 212 THR A CG2 1665 N N . ALA A 213 ? 0.9889 0.8032 0.5267 -0.1486 -0.0904 -0.0507 213 ALA A N 1666 C CA . ALA A 213 ? 0.9866 0.8261 0.4919 -0.1406 -0.0796 -0.0485 213 ALA A CA 1667 C C . ALA A 213 ? 0.9705 0.8465 0.4740 -0.1501 -0.0907 -0.0208 213 ALA A C 1668 O O . ALA A 213 ? 0.9073 0.7874 0.4351 -0.1617 -0.1079 -0.0069 213 ALA A O 1669 C CB . ALA A 213 ? 0.9735 0.8171 0.4967 -0.1254 -0.0564 -0.0417 213 ALA A CB 1670 N N . GLN A 214 ? 0.9896 0.8938 0.4664 -0.1453 -0.0808 -0.0113 214 GLN A N 1671 C CA . GLN A 214 ? 0.9879 0.9283 0.4639 -0.1541 -0.0912 0.0206 214 GLN A CA 1672 C C . GLN A 214 ? 1.1019 1.0479 0.6385 -0.1541 -0.0914 0.0514 214 GLN A C 1673 O O . GLN A 214 ? 1.0610 0.9919 0.6297 -0.1451 -0.0765 0.0498 214 GLN A O 1674 C CB . GLN A 214 ? 1.0904 1.0612 0.5284 -0.1491 -0.0766 0.0278 214 GLN A CB 1675 C CG . GLN A 214 ? 1.2087 1.1799 0.5814 -0.1493 -0.0752 -0.0039 214 GLN A CG 1676 C CD . GLN A 214 ? 1.1772 1.1215 0.5418 -0.1338 -0.0548 -0.0394 214 GLN A CD 1677 O OE1 . GLN A 214 ? 1.0921 1.0142 0.4989 -0.1249 -0.0457 -0.0404 214 GLN A OE1 1678 N NE2 . GLN A 214 ? 1.2565 1.2030 0.5670 -0.1302 -0.0478 -0.0689 214 GLN A NE2 1679 N N . ALA A 215 ? 1.1476 1.1154 0.7008 -0.1642 -0.1093 0.0785 215 ALA A N 1680 C CA . ALA A 215 ? 0.8970 0.8689 0.5117 -0.1638 -0.1111 0.1053 215 ALA A CA 1681 C C . ALA A 215 ? 0.8592 0.8409 0.4942 -0.1545 -0.0924 0.1244 215 ALA A C 1682 O O . ALA A 215 ? 0.9507 0.9278 0.6372 -0.1516 -0.0891 0.1391 215 ALA A O 1683 C CB . ALA A 215 ? 0.9212 0.9169 0.5512 -0.1750 -0.1353 0.1319 215 ALA A CB 1684 N N . ILE A 216 ? 0.8747 0.8706 0.4701 -0.1505 -0.0797 0.1228 216 ILE A N 1685 C CA . ILE A 216 ? 0.8661 0.8732 0.4793 -0.1430 -0.0611 0.1399 216 ILE A CA 1686 C C . ILE A 216 ? 0.8577 0.8372 0.5037 -0.1334 -0.0463 0.1237 216 ILE A C 1687 O O . ILE A 216 ? 0.9538 0.9357 0.6356 -0.1297 -0.0366 0.1400 216 ILE A O 1688 C CB . ILE A 216 ? 0.9165 0.9461 0.4786 -0.1400 -0.0469 0.1360 216 ILE A CB 1689 C CG1 . ILE A 216 ? 1.2580 1.3117 0.7712 -0.1511 -0.0626 0.1420 216 ILE A CG1 1690 C CG2 . ILE A 216 ? 0.8845 0.9351 0.4696 -0.1366 -0.0314 0.1637 216 ILE A CG2 1691 C CD1 . ILE A 216 ? 1.3804 1.4584 0.9164 -0.1618 -0.0811 0.1845 216 ILE A CD1 1692 N N . PHE A 217 ? 1.0130 0.9656 0.6465 -0.1311 -0.0464 0.0925 217 PHE A N 1693 C CA . PHE A 217 ? 0.9463 0.8727 0.6037 -0.1234 -0.0347 0.0767 217 PHE A CA 1694 C C . PHE A 217 ? 0.8788 0.7884 0.5795 -0.1281 -0.0427 0.0799 217 PHE A C 1695 O O . PHE A 217 ? 0.8811 0.7689 0.5987 -0.1245 -0.0354 0.0671 217 PHE A O 1696 C CB . PHE A 217 ? 0.8552 0.7599 0.4786 -0.1182 -0.0305 0.0434 217 PHE A CB 1697 C CG . PHE A 217 ? 0.9266 0.8466 0.5113 -0.1103 -0.0173 0.0342 217 PHE A CG 1698 C CD1 . PHE A 217 ? 0.8603 0.7843 0.4557 -0.0989 0.0018 0.0334 217 PHE A CD1 1699 C CD2 . PHE A 217 ? 1.1082 1.0412 0.6462 -0.1146 -0.0238 0.0255 217 PHE A CD2 1700 C CE1 . PHE A 217 ? 0.8870 0.8295 0.4509 -0.0905 0.0168 0.0242 217 PHE A CE1 1701 C CE2 . PHE A 217 ? 1.1631 1.1130 0.6635 -0.1068 -0.0087 0.0142 217 PHE A CE2 1702 C CZ . PHE A 217 ? 0.9775 0.9330 0.4927 -0.0940 0.0129 0.0136 217 PHE A CZ 1703 N N . ASP A 218 ? 0.8305 0.7523 0.5495 -0.1361 -0.0574 0.0972 218 ASP A N 1704 C CA . ASP A 218 ? 0.8265 0.7378 0.5902 -0.1396 -0.0629 0.0999 218 ASP A CA 1705 C C . ASP A 218 ? 0.8939 0.7999 0.6979 -0.1341 -0.0502 0.1082 218 ASP A C 1706 O O . ASP A 218 ? 1.1673 1.0845 0.9749 -0.1300 -0.0425 0.1228 218 ASP A O 1707 C CB . ASP A 218 ? 0.8550 0.7855 0.6378 -0.1473 -0.0811 0.1199 218 ASP A CB 1708 C CG . ASP A 218 ? 0.9721 0.9037 0.7240 -0.1560 -0.0976 0.1081 218 ASP A CG 1709 O OD1 . ASP A 218 ? 0.9263 0.8800 0.6740 -0.1627 -0.1142 0.1257 218 ASP A OD1 1710 O OD2 . ASP A 218 ? 1.2114 1.1211 0.9444 -0.1573 -0.0955 0.0824 218 ASP A OD2 1711 N N . ASP A 219 ? 0.7714 0.6611 0.6045 -0.1354 -0.0481 0.0984 219 ASP A N 1712 C CA . ASP A 219 ? 0.7516 0.6336 0.6218 -0.1318 -0.0373 0.1013 219 ASP A CA 1713 C C . ASP A 219 ? 0.8419 0.7161 0.6967 -0.1261 -0.0243 0.0949 219 ASP A C 1714 O O . ASP A 219 ? 1.0176 0.8936 0.8974 -0.1236 -0.0175 0.1047 219 ASP A O 1715 C CB . ASP A 219 ? 0.7773 0.6750 0.6873 -0.1313 -0.0416 0.1266 219 ASP A CB 1716 C CG . ASP A 219 ? 0.8911 0.8022 0.8188 -0.1359 -0.0571 0.1377 219 ASP A CG 1717 O OD1 . ASP A 219 ? 0.9797 0.8854 0.9390 -0.1373 -0.0576 0.1301 219 ASP A OD1 1718 O OD2 . ASP A 219 ? 1.0039 0.9336 0.9141 -0.1385 -0.0687 0.1543 219 ASP A OD2 1719 N N . SER A 220 ? 0.7466 0.6122 0.5640 -0.1239 -0.0218 0.0785 220 SER A N 1720 C CA . SER A 220 ? 0.7378 0.5970 0.5446 -0.1173 -0.0102 0.0714 220 SER A CA 1721 C C . SER A 220 ? 0.8012 0.6391 0.6225 -0.1183 -0.0057 0.0586 220 SER A C 1722 O O . SER A 220 ? 1.0161 0.8517 0.8466 -0.1148 0.0020 0.0593 220 SER A O 1723 C CB . SER A 220 ? 0.7622 0.6203 0.5274 -0.1125 -0.0090 0.0577 220 SER A CB 1724 O OG . SER A 220 ? 0.7746 0.6566 0.5205 -0.1117 -0.0101 0.0694 220 SER A OG 1725 N N . TYR A 221 ? 0.7859 0.6109 0.6094 -0.1245 -0.0112 0.0485 221 TYR A N 1726 C CA . TYR A 221 ? 0.7234 0.5297 0.5530 -0.1280 -0.0076 0.0366 221 TYR A CA 1727 C C . TYR A 221 ? 0.7866 0.5776 0.5920 -0.1238 -0.0054 0.0253 221 TYR A C 1728 O O . TYR A 221 ? 0.9269 0.7106 0.7392 -0.1230 -0.0005 0.0236 221 TYR A O 1729 C CB . TYR A 221 ? 0.6401 0.4481 0.5004 -0.1289 -0.0008 0.0418 221 TYR A CB 1730 C CG . TYR A 221 ? 0.6249 0.4411 0.5176 -0.1326 -0.0019 0.0480 221 TYR A CG 1731 C CD1 . TYR A 221 ? 0.6153 0.4297 0.5377 -0.1333 0.0043 0.0483 221 TYR A CD1 1732 C CD2 . TYR A 221 ? 0.8058 0.6315 0.7024 -0.1350 -0.0098 0.0526 221 TYR A CD2 1733 C CE1 . TYR A 221 ? 0.8605 0.6811 0.8181 -0.1343 0.0045 0.0518 221 TYR A CE1 1734 C CE2 . TYR A 221 ? 0.9151 0.7502 0.8487 -0.1366 -0.0110 0.0592 221 TYR A CE2 1735 C CZ . TYR A 221 ? 0.9122 0.7441 0.8775 -0.1352 -0.0029 0.0582 221 TYR A CZ 1736 O OH . TYR A 221 ? 0.8544 0.6943 0.8617 -0.1344 -0.0030 0.0626 221 TYR A OH 1737 N N . LEU A 222 ? 0.7975 0.5829 0.5761 -0.1212 -0.0101 0.0171 222 LEU A N 1738 C CA . LEU A 222 ? 0.8405 0.6077 0.6013 -0.1160 -0.0094 0.0049 222 LEU A CA 1739 C C . LEU A 222 ? 0.8433 0.5888 0.6069 -0.1245 -0.0135 -0.0013 222 LEU A C 1740 O O . LEU A 222 ? 0.9510 0.6937 0.7181 -0.1346 -0.0186 -0.0022 222 LEU A O 1741 C CB . LEU A 222 ? 0.8232 0.5865 0.5556 -0.1112 -0.0136 -0.0062 222 LEU A CB 1742 C CG . LEU A 222 ? 0.8194 0.5571 0.5369 -0.1059 -0.0156 -0.0219 222 LEU A CG 1743 C CD1 . LEU A 222 ? 0.8323 0.5727 0.5580 -0.0938 -0.0063 -0.0205 222 LEU A CD1 1744 C CD2 . LEU A 222 ? 0.8480 0.5789 0.5376 -0.1030 -0.0209 -0.0372 222 LEU A CD2 1745 N N . GLY A 223 ? 0.7837 0.5166 0.5471 -0.1214 -0.0115 -0.0036 223 GLY A N 1746 C CA . GLY A 223 ? 0.8299 0.5436 0.5925 -0.1308 -0.0160 -0.0060 223 GLY A CA 1747 C C . GLY A 223 ? 0.7930 0.5146 0.5716 -0.1392 -0.0111 0.0001 223 GLY A C 1748 O O . GLY A 223 ? 0.7639 0.4765 0.5410 -0.1503 -0.0127 -0.0008 223 GLY A O 1749 N N . TYR A 224 ? 0.7981 0.5368 0.5920 -0.1346 -0.0048 0.0059 224 TYR A N 1750 C CA . TYR A 224 ? 0.6603 0.4043 0.4700 -0.1412 0.0001 0.0081 224 TYR A CA 1751 C C . TYR A 224 ? 0.6382 0.3705 0.4396 -0.1448 -0.0025 0.0071 224 TYR A C 1752 O O . TYR A 224 ? 0.7437 0.4729 0.5442 -0.1556 -0.0011 0.0047 224 TYR A O 1753 C CB . TYR A 224 ? 0.7275 0.4884 0.5574 -0.1354 0.0051 0.0154 224 TYR A CB 1754 C CG . TYR A 224 ? 0.7575 0.5226 0.6085 -0.1421 0.0098 0.0145 224 TYR A CG 1755 C CD1 . TYR A 224 ? 0.7851 0.5592 0.6564 -0.1431 0.0125 0.0164 224 TYR A CD1 1756 C CD2 . TYR A 224 ? 0.6332 0.3929 0.4850 -0.1473 0.0107 0.0108 224 TYR A CD2 1757 C CE1 . TYR A 224 ? 0.6735 0.4491 0.5678 -0.1474 0.0179 0.0123 224 TYR A CE1 1758 C CE2 . TYR A 224 ? 0.6014 0.3629 0.4703 -0.1535 0.0155 0.0055 224 TYR A CE2 1759 C CZ . TYR A 224 ? 0.6205 0.3889 0.5118 -0.1527 0.0201 0.0050 224 TYR A CZ 1760 O OH . TYR A 224 ? 0.8099 0.5778 0.7218 -0.1570 0.0260 -0.0034 224 TYR A OH 1761 N N . SER A 225 ? 0.6531 0.3808 0.4488 -0.1357 -0.0061 0.0091 225 SER A N 1762 C CA . SER A 225 ? 0.8497 0.5665 0.6399 -0.1376 -0.0120 0.0113 225 SER A CA 1763 C C . SER A 225 ? 0.9009 0.6060 0.6844 -0.1263 -0.0172 0.0101 225 SER A C 1764 O O . SER A 225 ? 0.9139 0.6264 0.6991 -0.1145 -0.0131 0.0072 225 SER A O 1765 C CB . SER A 225 ? 1.0464 0.7758 0.8516 -0.1369 -0.0105 0.0163 225 SER A CB 1766 O OG . SER A 225 ? 1.0524 0.7965 0.8714 -0.1243 -0.0062 0.0204 225 SER A OG 1767 N N . VAL A 226 ? 0.9672 0.6542 0.7432 -0.1299 -0.0262 0.0124 226 VAL A N 1768 C CA . VAL A 226 ? 0.7928 0.4638 0.5674 -0.1182 -0.0321 0.0099 226 VAL A CA 1769 C C . VAL A 226 ? 0.7742 0.4375 0.5567 -0.1163 -0.0415 0.0190 226 VAL A C 1770 O O . VAL A 226 ? 0.7463 0.4120 0.5264 -0.1288 -0.0463 0.0274 226 VAL A O 1771 C CB . VAL A 226 ? 0.7212 0.3691 0.4815 -0.1240 -0.0381 0.0039 226 VAL A CB 1772 C CG1 . VAL A 226 ? 0.8519 0.5083 0.6061 -0.1237 -0.0319 -0.0050 226 VAL A CG1 1773 C CG2 . VAL A 226 ? 0.7579 0.3957 0.5098 -0.1430 -0.0441 0.0116 226 VAL A CG2 1774 N N . ALA A 227 ? 0.7539 0.4091 0.5462 -0.1003 -0.0444 0.0166 227 ALA A N 1775 C CA . ALA A 227 ? 0.7731 0.4197 0.5791 -0.0956 -0.0557 0.0266 227 ALA A CA 1776 C C . ALA A 227 ? 0.8634 0.4898 0.6782 -0.0785 -0.0589 0.0187 227 ALA A C 1777 O O . ALA A 227 ? 1.0552 0.6812 0.8648 -0.0683 -0.0497 0.0035 227 ALA A O 1778 C CB . ALA A 227 ? 0.8177 0.4913 0.6442 -0.0902 -0.0530 0.0343 227 ALA A CB 1779 N N . VAL A 228 ? 0.8854 0.4945 0.7135 -0.0754 -0.0728 0.0287 228 VAL A N 1780 C CA . VAL A 228 ? 0.8509 0.4354 0.6924 -0.0582 -0.0772 0.0201 228 VAL A CA 1781 C C . VAL A 228 ? 0.8833 0.4774 0.7598 -0.0392 -0.0803 0.0265 228 VAL A C 1782 O O . VAL A 228 ? 0.9173 0.5269 0.8064 -0.0450 -0.0883 0.0444 228 VAL A O 1783 C CB . VAL A 228 ? 0.8540 0.4004 0.6867 -0.0703 -0.0936 0.0267 228 VAL A CB 1784 C CG1 . VAL A 228 ? 0.8212 0.3586 0.6259 -0.0860 -0.0895 0.0174 228 VAL A CG1 1785 C CG2 . VAL A 228 ? 1.1152 0.6615 0.9490 -0.0860 -0.1087 0.0518 228 VAL A CG2 1786 N N . GLY A 229 ? 0.9027 0.4890 0.7958 -0.0166 -0.0738 0.0106 229 GLY A N 1787 C CA . GLY A 229 ? 0.9480 0.5445 0.8810 0.0053 -0.0743 0.0136 229 GLY A CA 1788 C C . GLY A 229 ? 1.0236 0.6100 0.9658 0.0295 -0.0618 -0.0124 229 GLY A C 1789 O O . GLY A 229 ? 1.1807 0.7621 1.0942 0.0276 -0.0509 -0.0319 229 GLY A O 1790 N N . ASP A 230 ? 1.0616 0.6462 1.0440 0.0523 -0.0633 -0.0139 230 ASP A N 1791 C CA . ASP A 230 ? 1.1190 0.6910 1.1105 0.0767 -0.0503 -0.0429 230 ASP A CA 1792 C C . ASP A 230 ? 1.1324 0.7478 1.1489 0.0998 -0.0272 -0.0536 230 ASP A C 1793 O O . ASP A 230 ? 1.2432 0.8773 1.3051 0.1140 -0.0291 -0.0414 230 ASP A O 1794 C CB . ASP A 230 ? 1.2997 0.8279 1.3211 0.0889 -0.0679 -0.0433 230 ASP A CB 1795 C CG . ASP A 230 ? 1.3492 0.8647 1.3866 0.1172 -0.0536 -0.0762 230 ASP A CG 1796 O OD1 . ASP A 230 ? 1.3022 0.8362 1.3849 0.1421 -0.0463 -0.0782 230 ASP A OD1 1797 O OD2 . ASP A 230 ? 1.4074 0.8969 1.4126 0.1145 -0.0492 -0.1015 230 ASP A OD2 1798 N N . PHE A 231 ? 1.1079 0.7420 1.0949 0.1019 -0.0058 -0.0743 231 PHE A N 1799 C CA . PHE A 231 ? 1.1343 0.8149 1.1370 0.1202 0.0196 -0.0837 231 PHE A CA 1800 C C . PHE A 231 ? 1.2334 0.9087 1.2416 0.1472 0.0379 -0.1182 231 PHE A C 1801 O O . PHE A 231 ? 1.3592 1.0763 1.3798 0.1631 0.0620 -0.1271 231 PHE A O 1802 C CB . PHE A 231 ? 1.0993 0.8132 1.0665 0.1027 0.0320 -0.0783 231 PHE A CB 1803 C CG . PHE A 231 ? 1.0567 0.7751 1.0191 0.0777 0.0166 -0.0498 231 PHE A CG 1804 C CD1 . PHE A 231 ? 1.0434 0.7980 1.0362 0.0755 0.0172 -0.0278 231 PHE A CD1 1805 C CD2 . PHE A 231 ? 1.0265 0.7135 0.9559 0.0561 0.0015 -0.0464 231 PHE A CD2 1806 C CE1 . PHE A 231 ? 1.0173 0.7738 1.0035 0.0524 0.0030 -0.0058 231 PHE A CE1 1807 C CE2 . PHE A 231 ? 1.0346 0.7265 0.9588 0.0342 -0.0104 -0.0239 231 PHE A CE2 1808 C CZ . PHE A 231 ? 1.0024 0.7276 0.9532 0.0324 -0.0097 -0.0050 231 PHE A CZ 1809 N N . ASN A 232 ? 1.2654 0.8903 1.2634 0.1515 0.0276 -0.1384 232 ASN A N 1810 C CA . ASN A 232 ? 1.2509 0.8643 1.2586 0.1789 0.0431 -0.1747 232 ASN A CA 1811 C C . ASN A 232 ? 1.2638 0.8419 1.3246 0.1986 0.0286 -0.1754 232 ASN A C 1812 O O . ASN A 232 ? 1.2562 0.8217 1.3433 0.1894 0.0057 -0.1446 232 ASN A O 1813 C CB . ASN A 232 ? 1.2412 0.8235 1.1956 0.1707 0.0444 -0.2048 232 ASN A CB 1814 C CG . ASN A 232 ? 1.2155 0.7546 1.1463 0.1441 0.0173 -0.1912 232 ASN A CG 1815 O OD1 . ASN A 232 ? 1.2128 0.7459 1.1625 0.1312 -0.0009 -0.1597 232 ASN A OD1 1816 N ND2 . ASN A 232 ? 1.2036 0.7148 1.0927 0.1344 0.0145 -0.2146 232 ASN A ND2 1817 N N . GLY A 233 ? 1.4359 0.9981 1.5124 0.2256 0.0417 -0.2105 233 GLY A N 1818 C CA . GLY A 233 ? 1.6722 1.2028 1.8082 0.2492 0.0303 -0.2130 233 GLY A CA 1819 C C . GLY A 233 ? 1.6343 1.1055 1.7765 0.2336 -0.0050 -0.1940 233 GLY A C 1820 O O . GLY A 233 ? 1.5112 0.9718 1.7045 0.2405 -0.0235 -0.1690 233 GLY A O 1821 N N . ASP A 234 ? 1.5845 1.0206 1.6752 0.2107 -0.0152 -0.2027 234 ASP A N 1822 C CA . ASP A 234 ? 1.4012 0.7789 1.4938 0.1941 -0.0466 -0.1879 234 ASP A CA 1823 C C . ASP A 234 ? 1.2507 0.6382 1.3551 0.1728 -0.0685 -0.1390 234 ASP A C 1824 O O . ASP A 234 ? 1.2055 0.6415 1.2999 0.1629 -0.0604 -0.1196 234 ASP A O 1825 C CB . ASP A 234 ? 1.4657 0.8145 1.4998 0.1713 -0.0505 -0.2063 234 ASP A CB 1826 C CG . ASP A 234 ? 1.5239 0.9182 1.5071 0.1496 -0.0376 -0.1989 234 ASP A CG 1827 O OD1 . ASP A 234 ? 1.5177 0.9482 1.5050 0.1378 -0.0390 -0.1663 234 ASP A OD1 1828 O OD2 . ASP A 234 ? 1.5445 0.9374 1.4839 0.1438 -0.0275 -0.2261 234 ASP A OD2 1829 N N . GLY A 235 ? 1.2585 0.5998 1.3841 0.1650 -0.0967 -0.1191 235 GLY A N 1830 C CA . GLY A 235 ? 1.2615 0.6107 1.3934 0.1433 -0.1187 -0.0733 235 GLY A CA 1831 C C . GLY A 235 ? 1.2238 0.5792 1.2988 0.1073 -0.1228 -0.0596 235 GLY A C 1832 O O . GLY A 235 ? 1.1949 0.5690 1.2636 0.0872 -0.1343 -0.0261 235 GLY A O 1833 N N . ILE A 236 ? 1.2690 0.6102 1.3033 0.0992 -0.1132 -0.0868 236 ILE A N 1834 C CA . ILE A 236 ? 1.3004 0.6433 1.2864 0.0665 -0.1176 -0.0766 236 ILE A CA 1835 C C . ILE A 236 ? 1.1642 0.5632 1.1242 0.0574 -0.1001 -0.0701 236 ILE A C 1836 O O . ILE A 236 ? 1.1530 0.5846 1.1116 0.0739 -0.0782 -0.0892 236 ILE A O 1837 C CB . ILE A 236 ? 1.4248 0.7344 1.3802 0.0606 -0.1159 -0.1074 236 ILE A CB 1838 C CG1 . ILE A 236 ? 1.4336 0.6831 1.4186 0.0709 -0.1331 -0.1177 236 ILE A CG1 1839 C CG2 . ILE A 236 ? 1.4826 0.7938 1.3971 0.0266 -0.1228 -0.0935 236 ILE A CG2 1840 C CD1 . ILE A 236 ? 1.5094 0.7213 1.4668 0.0629 -0.1354 -0.1486 236 ILE A CD1 1841 N N . ASP A 237 ? 1.1902 0.6002 1.1304 0.0306 -0.1095 -0.0430 237 ASP A N 1842 C CA . ASP A 237 ? 1.1588 0.6156 1.0763 0.0192 -0.0958 -0.0357 237 ASP A CA 1843 C C . ASP A 237 ? 1.1363 0.6055 1.0197 0.0174 -0.0783 -0.0610 237 ASP A C 1844 O O . ASP A 237 ? 1.2448 0.6840 1.1091 0.0115 -0.0824 -0.0776 237 ASP A O 1845 C CB . ASP A 237 ? 1.2363 0.6954 1.1363 -0.0099 -0.1093 -0.0071 237 ASP A CB 1846 C CG . ASP A 237 ? 1.5317 0.9861 1.4592 -0.0114 -0.1277 0.0217 237 ASP A CG 1847 O OD1 . ASP A 237 ? 1.4846 0.9560 1.3985 -0.0318 -0.1342 0.0442 237 ASP A OD1 1848 O OD2 . ASP A 237 ? 1.7880 1.2220 1.7511 0.0079 -0.1363 0.0215 237 ASP A OD2 1849 N N . ASP A 238 ? 1.0731 0.5868 0.9500 0.0211 -0.0606 -0.0622 238 ASP A N 1850 C CA . ASP A 238 ? 1.0646 0.5961 0.9093 0.0181 -0.0451 -0.0806 238 ASP A CA 1851 C C . ASP A 238 ? 1.0224 0.5814 0.8481 -0.0036 -0.0432 -0.0627 238 ASP A C 1852 O O . ASP A 238 ? 1.0410 0.6153 0.8804 -0.0107 -0.0476 -0.0409 238 ASP A O 1853 C CB . ASP A 238 ? 1.1011 0.6621 0.9549 0.0422 -0.0239 -0.0984 238 ASP A CB 1854 C CG . ASP A 238 ? 1.3210 0.8572 1.2006 0.0671 -0.0233 -0.1182 238 ASP A CG 1855 O OD1 . ASP A 238 ? 1.4535 0.9575 1.3167 0.0705 -0.0253 -0.1434 238 ASP A OD1 1856 O OD2 . ASP A 238 ? 1.4301 0.9789 1.3494 0.0836 -0.0216 -0.1092 238 ASP A OD2 1857 N N . PHE A 239 ? 1.1154 0.6800 0.9110 -0.0141 -0.0377 -0.0728 239 PHE A N 1858 C CA . PHE A 239 ? 1.0097 0.5940 0.7908 -0.0346 -0.0375 -0.0578 239 PHE A CA 1859 C C . PHE A 239 ? 0.9334 0.5610 0.7185 -0.0304 -0.0222 -0.0512 239 PHE A C 1860 O O . PHE A 239 ? 0.9568 0.6034 0.7381 -0.0169 -0.0088 -0.0632 239 PHE A O 1861 C CB . PHE A 239 ? 0.9841 0.5563 0.7378 -0.0483 -0.0409 -0.0685 239 PHE A CB 1862 C CG . PHE A 239 ? 0.9740 0.5032 0.7253 -0.0554 -0.0566 -0.0743 239 PHE A CG 1863 C CD1 . PHE A 239 ? 1.1091 0.6199 0.8413 -0.0583 -0.0603 -0.0941 239 PHE A CD1 1864 C CD2 . PHE A 239 ? 0.9618 0.4691 0.7299 -0.0608 -0.0694 -0.0584 239 PHE A CD2 1865 C CE1 . PHE A 239 ? 1.3566 0.8258 1.0900 -0.0665 -0.0761 -0.0987 239 PHE A CE1 1866 C CE2 . PHE A 239 ? 1.1075 0.5744 0.8761 -0.0689 -0.0848 -0.0602 239 PHE A CE2 1867 C CZ . PHE A 239 ? 1.3629 0.8097 1.1159 -0.0717 -0.0880 -0.0808 239 PHE A CZ 1868 N N . VAL A 240 ? 0.8816 0.5246 0.6739 -0.0431 -0.0245 -0.0321 240 VAL A N 1869 C CA . VAL A 240 ? 0.8543 0.5346 0.6544 -0.0426 -0.0128 -0.0232 240 VAL A CA 1870 C C . VAL A 240 ? 0.9045 0.5923 0.6942 -0.0621 -0.0144 -0.0139 240 VAL A C 1871 O O . VAL A 240 ? 1.0303 0.7068 0.8207 -0.0755 -0.0236 -0.0050 240 VAL A O 1872 C CB . VAL A 240 ? 0.8354 0.5305 0.6650 -0.0357 -0.0136 -0.0102 240 VAL A CB 1873 C CG1 . VAL A 240 ? 0.8065 0.5369 0.6459 -0.0399 -0.0042 0.0008 240 VAL A CG1 1874 C CG2 . VAL A 240 ? 0.9218 0.6165 0.7697 -0.0132 -0.0089 -0.0196 240 VAL A CG2 1875 N N . SER A 241 ? 0.8471 0.5549 0.6279 -0.0637 -0.0053 -0.0157 241 SER A N 1876 C CA . SER A 241 ? 0.7773 0.4925 0.5545 -0.0795 -0.0061 -0.0081 241 SER A CA 1877 C C . SER A 241 ? 0.7404 0.4865 0.5279 -0.0783 0.0040 0.0007 241 SER A C 1878 O O . SER A 241 ? 0.7138 0.4766 0.4961 -0.0692 0.0122 -0.0017 241 SER A O 1879 C CB . SER A 241 ? 0.8075 0.5092 0.5649 -0.0874 -0.0106 -0.0167 241 SER A CB 1880 O OG . SER A 241 ? 0.9819 0.6934 0.7420 -0.1007 -0.0104 -0.0096 241 SER A OG 1881 N N . GLY A 242 ? 0.7184 0.4717 0.5198 -0.0884 0.0031 0.0109 242 GLY A N 1882 C CA . GLY A 242 ? 0.8783 0.6557 0.6936 -0.0901 0.0102 0.0208 242 GLY A CA 1883 C C . GLY A 242 ? 0.9864 0.7666 0.7932 -0.0963 0.0105 0.0206 242 GLY A C 1884 O O . GLY A 242 ? 1.1220 0.8870 0.9202 -0.1047 0.0048 0.0150 242 GLY A O 1885 N N . VAL A 243 ? 0.8282 0.6303 0.6391 -0.0929 0.0165 0.0290 243 VAL A N 1886 C CA . VAL A 243 ? 0.7165 0.5249 0.5236 -0.0984 0.0146 0.0331 243 VAL A CA 1887 C C . VAL A 243 ? 0.6551 0.4843 0.4864 -0.1006 0.0188 0.0504 243 VAL A C 1888 O O . VAL A 243 ? 0.6488 0.4991 0.4784 -0.0960 0.0239 0.0608 243 VAL A O 1889 C CB . VAL A 243 ? 1.0897 0.9012 0.8686 -0.0930 0.0139 0.0257 243 VAL A CB 1890 C CG1 . VAL A 243 ? 1.0008 0.8283 0.7716 -0.0808 0.0235 0.0250 243 VAL A CG1 1891 C CG2 . VAL A 243 ? 1.2603 1.0838 1.0365 -0.0992 0.0095 0.0340 243 VAL A CG2 1892 N N . PRO A 244 ? 0.6533 0.4761 0.5076 -0.1084 0.0167 0.0533 244 PRO A N 1893 C CA . PRO A 244 ? 0.6820 0.5159 0.5665 -0.1116 0.0191 0.0671 244 PRO A CA 1894 C C . PRO A 244 ? 0.6197 0.4696 0.5161 -0.1124 0.0187 0.0836 244 PRO A C 1895 O O . PRO A 244 ? 0.5901 0.4537 0.5076 -0.1130 0.0214 0.0996 244 PRO A O 1896 C CB . PRO A 244 ? 0.6603 0.4771 0.5589 -0.1199 0.0164 0.0580 244 PRO A CB 1897 C CG . PRO A 244 ? 0.5752 0.3797 0.4550 -0.1222 0.0133 0.0462 244 PRO A CG 1898 C CD . PRO A 244 ? 0.5938 0.3966 0.4453 -0.1157 0.0122 0.0415 244 PRO A CD 1899 N N . ARG A 245 ? 0.6614 0.5103 0.5471 -0.1136 0.0138 0.0821 245 ARG A N 1900 C CA . ARG A 245 ? 0.6182 0.4828 0.5167 -0.1152 0.0101 0.1006 245 ARG A CA 1901 C C . ARG A 245 ? 0.7655 0.6499 0.6350 -0.1114 0.0108 0.1090 245 ARG A C 1902 O O . ARG A 245 ? 1.1164 1.0168 0.9890 -0.1137 0.0060 0.1267 245 ARG A O 1903 C CB . ARG A 245 ? 0.5949 0.4520 0.5043 -0.1194 0.0028 0.0971 245 ARG A CB 1904 C CG . ARG A 245 ? 0.5866 0.4333 0.5351 -0.1228 0.0037 0.0957 245 ARG A CG 1905 C CD . ARG A 245 ? 0.6812 0.5309 0.6514 -0.1245 -0.0028 0.1001 245 ARG A CD 1906 N NE . ARG A 245 ? 0.6613 0.5301 0.6336 -0.1236 -0.0107 0.1230 245 ARG A NE 1907 C CZ . ARG A 245 ? 0.6845 0.5613 0.6906 -0.1234 -0.0138 0.1447 245 ARG A CZ 1908 N NH1 . ARG A 245 ? 0.7797 0.6445 0.8225 -0.1235 -0.0095 0.1432 245 ARG A NH1 1909 N NH2 . ARG A 245 ? 0.7825 0.6786 0.7853 -0.1241 -0.0225 0.1683 245 ARG A NH2 1910 N N . ALA A 246 ? 0.7245 0.6084 0.5661 -0.1054 0.0167 0.0961 246 ALA A N 1911 C CA . ALA A 246 ? 0.8904 0.7930 0.6999 -0.1009 0.0201 0.0981 246 ALA A CA 1912 C C . ALA A 246 ? 0.9004 0.8311 0.7197 -0.1000 0.0285 0.1203 246 ALA A C 1913 O O . ALA A 246 ? 0.7604 0.6930 0.6143 -0.1029 0.0305 0.1335 246 ALA A O 1914 C CB . ALA A 246 ? 0.9301 0.8216 0.7121 -0.0929 0.0249 0.0750 246 ALA A CB 1915 N N . ALA A 247 ? 1.0176 0.9705 0.8054 -0.0969 0.0338 0.1232 247 ALA A N 1916 C CA . ALA A 247 ? 0.9510 0.9367 0.7417 -0.0971 0.0440 0.1456 247 ALA A CA 1917 C C . ALA A 247 ? 0.9553 0.9484 0.7847 -0.1063 0.0379 0.1759 247 ALA A C 1918 O O . ALA A 247 ? 0.9440 0.9419 0.8056 -0.1076 0.0437 0.1876 247 ALA A O 1919 C CB . ALA A 247 ? 0.8928 0.8859 0.6921 -0.0888 0.0588 0.1382 247 ALA A CB 1920 N N . ARG A 248 ? 0.9759 0.9686 0.8054 -0.1128 0.0248 0.1884 248 ARG A N 1921 C CA . ARG A 248 ? 0.8252 0.8209 0.6955 -0.1206 0.0162 0.2175 248 ARG A CA 1922 C C . ARG A 248 ? 0.7724 0.7468 0.6892 -0.1211 0.0174 0.2142 248 ARG A C 1923 O O . ARG A 248 ? 1.0063 0.9883 0.9566 -0.1259 0.0187 0.2365 248 ARG A O 1924 C CB . ARG A 248 ? 0.8795 0.9100 0.7461 -0.1259 0.0200 0.2511 248 ARG A CB 1925 C CG . ARG A 248 ? 1.2125 1.2634 1.0806 -0.1239 0.0376 0.2562 248 ARG A CG 1926 C CD . ARG A 248 ? 1.4646 1.5525 1.3308 -0.1318 0.0414 0.2932 248 ARG A CD 1927 N NE . ARG A 248 ? 1.5835 1.6913 1.4685 -0.1320 0.0574 0.3032 248 ARG A NE 1928 C CZ . ARG A 248 ? 1.4194 1.5205 1.3563 -0.1382 0.0552 0.3207 248 ARG A CZ 1929 N NH1 . ARG A 248 ? 1.3569 1.4297 1.3311 -0.1431 0.0392 0.3276 248 ARG A NH1 1930 N NH2 . ARG A 248 ? 1.2169 1.3399 1.1709 -0.1395 0.0691 0.3300 248 ARG A NH2 1931 N N . THR A 249 ? 0.7099 0.6579 0.6258 -0.1176 0.0166 0.1861 249 THR A N 1932 C CA . THR A 249 ? 0.6643 0.5893 0.6145 -0.1190 0.0165 0.1758 249 THR A CA 1933 C C . THR A 249 ? 0.6851 0.6138 0.6428 -0.1177 0.0259 0.1730 249 THR A C 1934 O O . THR A 249 ? 0.6929 0.6034 0.6724 -0.1200 0.0249 0.1621 249 THR A O 1935 C CB . THR A 249 ? 0.6810 0.5988 0.6775 -0.1247 0.0084 0.1934 249 THR A CB 1936 O OG1 . THR A 249 ? 0.8804 0.7719 0.8942 -0.1248 0.0056 0.1722 249 THR A OG1 1937 C CG2 . THR A 249 ? 0.6684 0.5933 0.6984 -0.1295 0.0113 0.2134 249 THR A CG2 1938 N N . LEU A 250 ? 0.6541 0.6083 0.5935 -0.1143 0.0351 0.1817 250 LEU A N 1939 C CA . LEU A 250 ? 0.6436 0.6062 0.5916 -0.1115 0.0444 0.1783 250 LEU A CA 1940 C C . LEU A 250 ? 0.7162 0.6558 0.6536 -0.1064 0.0434 0.1500 250 LEU A C 1941 O O . LEU A 250 ? 0.7448 0.6791 0.7026 -0.1077 0.0437 0.1461 250 LEU A O 1942 C CB . LEU A 250 ? 0.6349 0.6314 0.5606 -0.1060 0.0574 0.1869 250 LEU A CB 1943 C CG . LEU A 250 ? 0.7074 0.7364 0.6532 -0.1125 0.0637 0.2194 250 LEU A CG 1944 C CD1 . LEU A 250 ? 1.0070 1.0379 0.9564 -0.1208 0.0540 0.2422 250 LEU A CD1 1945 C CD2 . LEU A 250 ? 0.6501 0.7149 0.5695 -0.1054 0.0807 0.2212 250 LEU A CD2 1946 N N . GLY A 251 ? 0.7713 0.6976 0.6769 -0.1019 0.0406 0.1321 251 GLY A N 1947 C CA . GLY A 251 ? 0.7386 0.6425 0.6315 -0.0979 0.0385 0.1083 251 GLY A CA 1948 C C . GLY A 251 ? 0.6824 0.5957 0.5527 -0.0869 0.0467 0.0979 251 GLY A C 1949 O O . GLY A 251 ? 0.7684 0.7079 0.6446 -0.0823 0.0568 0.1083 251 GLY A O 1950 N N . MET A 252 ? 0.6885 0.5806 0.5362 -0.0825 0.0429 0.0774 252 MET A N 1951 C CA . MET A 252 ? 0.7241 0.6190 0.5527 -0.0703 0.0497 0.0637 252 MET A CA 1952 C C . MET A 252 ? 0.7398 0.6052 0.5646 -0.0678 0.0425 0.0464 252 MET A C 1953 O O . MET A 252 ? 0.7045 0.5486 0.5323 -0.0769 0.0329 0.0436 252 MET A O 1954 C CB . MET A 252 ? 0.7405 0.6426 0.5342 -0.0666 0.0525 0.0569 252 MET A CB 1955 C CG . MET A 252 ? 0.7295 0.6682 0.5179 -0.0643 0.0644 0.0718 252 MET A CG 1956 S SD . MET A 252 ? 0.8544 0.8011 0.5922 -0.0599 0.0675 0.0575 252 MET A SD 1957 C CE . MET A 252 ? 1.2637 1.2598 0.9979 -0.0572 0.0858 0.0772 252 MET A CE 1958 N N . VAL A 253 ? 0.7730 0.6387 0.5932 -0.0553 0.0477 0.0356 253 VAL A N 1959 C CA . VAL A 253 ? 0.8019 0.6386 0.6182 -0.0519 0.0395 0.0212 253 VAL A CA 1960 C C . VAL A 253 ? 0.9393 0.7684 0.7330 -0.0390 0.0438 0.0025 253 VAL A C 1961 O O . VAL A 253 ? 1.1918 1.0405 0.9895 -0.0255 0.0560 -0.0010 253 VAL A O 1962 C CB . VAL A 253 ? 0.7819 0.6209 0.6271 -0.0489 0.0376 0.0273 253 VAL A CB 1963 C CG1 . VAL A 253 ? 0.8020 0.6125 0.6433 -0.0438 0.0284 0.0155 253 VAL A CG1 1964 C CG2 . VAL A 253 ? 0.7199 0.5598 0.5832 -0.0636 0.0310 0.0405 253 VAL A CG2 1965 N N . TYR A 254 ? 0.8943 0.6953 0.6660 -0.0433 0.0342 -0.0105 254 TYR A N 1966 C CA . TYR A 254 ? 0.9175 0.7051 0.6662 -0.0330 0.0358 -0.0316 254 TYR A CA 1967 C C . TYR A 254 ? 0.9864 0.7458 0.7464 -0.0246 0.0295 -0.0421 254 TYR A C 1968 O O . TYR A 254 ? 0.9039 0.6437 0.6754 -0.0333 0.0179 -0.0348 254 TYR A O 1969 C CB . TYR A 254 ? 0.9088 0.6817 0.6292 -0.0438 0.0267 -0.0397 254 TYR A CB 1970 C CG . TYR A 254 ? 0.9309 0.7315 0.6388 -0.0506 0.0307 -0.0291 254 TYR A CG 1971 C CD1 . TYR A 254 ? 0.9195 0.7550 0.6321 -0.0446 0.0445 -0.0181 254 TYR A CD1 1972 C CD2 . TYR A 254 ? 1.0681 0.8619 0.7624 -0.0638 0.0198 -0.0276 254 TYR A CD2 1973 C CE1 . TYR A 254 ? 0.9263 0.7868 0.6282 -0.0520 0.0462 -0.0042 254 TYR A CE1 1974 C CE2 . TYR A 254 ? 0.9925 0.8118 0.6788 -0.0699 0.0207 -0.0147 254 TYR A CE2 1975 C CZ . TYR A 254 ? 0.9335 0.7849 0.6224 -0.0642 0.0334 -0.0023 254 TYR A CZ 1976 O OH . TYR A 254 ? 0.9591 0.8356 0.6406 -0.0714 0.0325 0.0145 254 TYR A OH 1977 N N . ILE A 255 ? 1.0972 0.8552 0.8542 -0.0074 0.0375 -0.0591 255 ILE A N 1978 C CA . ILE A 255 ? 0.9426 0.6703 0.7130 0.0028 0.0303 -0.0703 255 ILE A CA 1979 C C . ILE A 255 ? 0.9598 0.6615 0.7048 0.0093 0.0288 -0.0972 255 ILE A C 1980 O O . ILE A 255 ? 0.9953 0.7133 0.7243 0.0206 0.0425 -0.1134 255 ILE A O 1981 C CB . ILE A 255 ? 0.9348 0.6819 0.7386 0.0211 0.0406 -0.0673 255 ILE A CB 1982 C CG1 . ILE A 255 ? 0.8871 0.6546 0.7180 0.0123 0.0375 -0.0413 255 ILE A CG1 1983 C CG2 . ILE A 255 ? 0.9542 0.6682 0.7745 0.0345 0.0325 -0.0799 255 ILE A CG2 1984 C CD1 . ILE A 255 ? 0.8909 0.6779 0.7610 0.0277 0.0433 -0.0350 255 ILE A CD1 1985 N N . TYR A 256 ? 0.9512 0.6132 0.6914 0.0005 0.0119 -0.1021 256 TYR A N 1986 C CA . TYR A 256 ? 1.0475 0.6788 0.7660 0.0037 0.0066 -0.1281 256 TYR A CA 1987 C C . TYR A 256 ? 1.1325 0.7269 0.8737 0.0163 -0.0012 -0.1383 256 TYR A C 1988 O O . TYR A 256 ? 1.3232 0.9082 1.0915 0.0144 -0.0100 -0.1200 256 TYR A O 1989 C CB . TYR A 256 ? 1.1013 0.7149 0.7977 -0.0186 -0.0082 -0.1260 256 TYR A CB 1990 C CG . TYR A 256 ? 1.1061 0.7528 0.7833 -0.0303 -0.0032 -0.1164 256 TYR A CG 1991 C CD1 . TYR A 256 ? 1.0400 0.6961 0.7257 -0.0471 -0.0090 -0.0940 256 TYR A CD1 1992 C CD2 . TYR A 256 ? 1.1881 0.8570 0.8393 -0.0245 0.0072 -0.1294 256 TYR A CD2 1993 C CE1 . TYR A 256 ? 0.9470 0.6313 0.6218 -0.0563 -0.0059 -0.0841 256 TYR A CE1 1994 C CE2 . TYR A 256 ? 1.1368 0.8356 0.7729 -0.0356 0.0091 -0.1166 256 TYR A CE2 1995 C CZ . TYR A 256 ? 1.0317 0.7369 0.6829 -0.0508 0.0019 -0.0934 256 TYR A CZ 1996 O OH . TYR A 256 ? 1.1181 0.8513 0.7608 -0.0604 0.0026 -0.0796 256 TYR A OH 1997 N N . ASP A 257 ? 1.0997 0.6727 0.8295 0.0289 0.0011 -0.1678 257 ASP A N 1998 C CA . ASP A 257 ? 1.1340 0.6663 0.8880 0.0424 -0.0074 -0.1803 257 ASP A CA 1999 C C . ASP A 257 ? 1.1147 0.6057 0.8725 0.0231 -0.0314 -0.1678 257 ASP A C 2000 O O . ASP A 257 ? 1.1740 0.6620 0.9077 0.0015 -0.0397 -0.1629 257 ASP A O 2001 C CB . ASP A 257 ? 1.2554 0.7713 0.9924 0.0585 0.0007 -0.2195 257 ASP A CB 2002 C CG . ASP A 257 ? 1.4932 0.9730 1.2652 0.0800 -0.0029 -0.2349 257 ASP A CG 2003 O OD1 . ASP A 257 ? 1.6923 1.1832 1.4710 0.1043 0.0152 -0.2598 257 ASP A OD1 2004 O OD2 . ASP A 257 ? 1.5310 0.9723 1.3252 0.0728 -0.0233 -0.2218 257 ASP A OD2 2005 N N . GLY A 258 ? 1.1292 0.5908 0.9199 0.0305 -0.0426 -0.1606 258 GLY A N 2006 C CA . GLY A 258 ? 1.1003 0.5229 0.8964 0.0119 -0.0651 -0.1458 258 GLY A CA 2007 C C . GLY A 258 ? 1.2288 0.6044 1.0147 0.0102 -0.0763 -0.1713 258 GLY A C 2008 O O . GLY A 258 ? 1.2831 0.6304 1.0634 -0.0111 -0.0938 -0.1619 258 GLY A O 2009 N N . LYS A 259 ? 1.3023 0.6704 1.0860 0.0319 -0.0657 -0.2046 259 LYS A N 2010 C CA . LYS A 259 ? 1.3535 0.6750 1.1262 0.0319 -0.0758 -0.2354 259 LYS A CA 2011 C C . LYS A 259 ? 1.3503 0.6808 1.0788 0.0103 -0.0780 -0.2453 259 LYS A C 2012 O O . LYS A 259 ? 1.3898 0.6928 1.1120 -0.0123 -0.0968 -0.2388 259 LYS A O 2013 C CB . LYS A 259 ? 1.4727 0.7874 1.2538 0.0628 -0.0608 -0.2723 259 LYS A CB 2014 C CG . LYS A 259 ? 1.4815 0.7879 1.3143 0.0874 -0.0589 -0.2646 259 LYS A CG 2015 C CD . LYS A 259 ? 1.5586 0.8021 1.4227 0.0859 -0.0834 -0.2620 259 LYS A CD 2016 C CE . LYS A 259 ? 1.6300 0.8627 1.5489 0.1154 -0.0815 -0.2610 259 LYS A CE 2017 N NZ . LYS A 259 ? 1.6864 0.8533 1.6388 0.1160 -0.1064 -0.2600 259 LYS A NZ 2018 N N . ASN A 260 ? 1.3566 0.7281 1.0567 0.0168 -0.0595 -0.2588 260 ASN A N 2019 C CA . ASN A 260 ? 1.4286 0.8191 1.0888 -0.0033 -0.0617 -0.2619 260 ASN A CA 2020 C C . ASN A 260 ? 1.3543 0.8017 1.0064 -0.0071 -0.0473 -0.2376 260 ASN A C 2021 O O . ASN A 260 ? 1.4610 0.9344 1.1330 0.0079 -0.0329 -0.2258 260 ASN A O 2022 C CB . ASN A 260 ? 1.5998 0.9817 1.2257 0.0040 -0.0571 -0.3035 260 ASN A CB 2023 C CG . ASN A 260 ? 1.9344 1.3147 1.5706 0.0352 -0.0387 -0.3311 260 ASN A CG 2024 O OD1 . ASN A 260 ? 1.8697 1.2083 1.5364 0.0488 -0.0448 -0.3431 260 ASN A OD1 2025 N ND2 . ASN A 260 ? 2.3444 1.7712 1.9575 0.0468 -0.0159 -0.3405 260 ASN A ND2 2026 N N . MET A 261 ? 1.2605 0.7266 0.8871 -0.0275 -0.0525 -0.2295 261 MET A N 2027 C CA . MET A 261 ? 1.1808 0.6937 0.8062 -0.0349 -0.0435 -0.2022 261 MET A CA 2028 C C . MET A 261 ? 1.1653 0.7211 0.7763 -0.0196 -0.0219 -0.2077 261 MET A C 2029 O O . MET A 261 ? 1.1797 0.7736 0.7921 -0.0247 -0.0142 -0.1851 261 MET A O 2030 C CB . MET A 261 ? 1.5574 1.0775 1.1657 -0.0597 -0.0562 -0.1922 261 MET A CB 2031 C CG . MET A 261 ? 1.6133 1.1555 1.2413 -0.0723 -0.0563 -0.1587 261 MET A CG 2032 S SD . MET A 261 ? 1.4497 0.9719 1.1145 -0.0669 -0.0575 -0.1414 261 MET A SD 2033 C CE . MET A 261 ? 0.8733 0.4214 0.5496 -0.0864 -0.0584 -0.1095 261 MET A CE 2034 N N . SER A 262 ? 1.3439 0.8934 0.9418 -0.0015 -0.0118 -0.2380 262 SER A N 2035 C CA . SER A 262 ? 1.4598 1.0523 1.0414 0.0128 0.0110 -0.2452 262 SER A CA 2036 C C . SER A 262 ? 1.2920 0.9208 0.9045 0.0205 0.0252 -0.2168 262 SER A C 2037 O O . SER A 262 ? 1.1254 0.7404 0.7755 0.0275 0.0226 -0.2054 262 SER A O 2038 C CB . SER A 262 ? 1.4585 1.0352 1.0320 0.0350 0.0225 -0.2838 262 SER A CB 2039 O OG . SER A 262 ? 1.2581 0.8146 0.8759 0.0532 0.0254 -0.2838 262 SER A OG 2040 N N . SER A 263 ? 1.1860 0.8612 0.7828 0.0177 0.0383 -0.2039 263 SER A N 2041 C CA . SER A 263 ? 1.0756 0.7873 0.7009 0.0218 0.0507 -0.1761 263 SER A CA 2042 C C . SER A 263 ? 1.0731 0.7948 0.7255 0.0461 0.0683 -0.1855 263 SER A C 2043 O O . SER A 263 ? 1.1094 0.8267 0.7486 0.0621 0.0794 -0.2154 263 SER A O 2044 C CB . SER A 263 ? 1.0790 0.8362 0.6814 0.0129 0.0602 -0.1606 263 SER A CB 2045 O OG . SER A 263 ? 1.1434 0.9342 0.7758 0.0156 0.0714 -0.1340 263 SER A OG 2046 N N . LEU A 264 ? 1.0446 0.7809 0.7367 0.0489 0.0705 -0.1609 264 LEU A N 2047 C CA . LEU A 264 ? 1.0494 0.8005 0.7767 0.0713 0.0855 -0.1646 264 LEU A CA 2048 C C . LEU A 264 ? 1.0516 0.8568 0.7947 0.0721 0.1026 -0.1415 264 LEU A C 2049 O O . LEU A 264 ? 1.1587 0.9985 0.8944 0.0844 0.1247 -0.1513 264 LEU A O 2050 C CB . LEU A 264 ? 1.0322 0.7507 0.7998 0.0747 0.0697 -0.1558 264 LEU A CB 2051 C CG . LEU A 264 ? 1.0721 0.7513 0.8524 0.0930 0.0661 -0.1829 264 LEU A CG 2052 C CD1 . LEU A 264 ? 1.2359 0.8839 0.9739 0.0880 0.0605 -0.2121 264 LEU A CD1 2053 C CD2 . LEU A 264 ? 1.0617 0.7066 0.8770 0.0900 0.0448 -0.1664 264 LEU A CD2 2054 N N . TYR A 265 ? 1.0414 0.8541 0.8059 0.0581 0.0928 -0.1113 265 TYR A N 2055 C CA . TYR A 265 ? 1.0592 0.9188 0.8441 0.0562 0.1057 -0.0872 265 TYR A CA 2056 C C . TYR A 265 ? 1.0990 0.9662 0.8738 0.0332 0.0961 -0.0628 265 TYR A C 2057 O O . TYR A 265 ? 1.0172 0.8537 0.7796 0.0194 0.0785 -0.0615 265 TYR A O 2058 C CB . TYR A 265 ? 1.0916 0.9578 0.9280 0.0659 0.1048 -0.0747 265 TYR A CB 2059 C CG . TYR A 265 ? 1.2307 1.0937 1.0887 0.0915 0.1152 -0.0962 265 TYR A CG 2060 C CD1 . TYR A 265 ? 1.3232 1.2283 1.1903 0.1083 0.1412 -0.1043 265 TYR A CD1 2061 C CD2 . TYR A 265 ? 1.2636 1.0825 1.1359 0.0991 0.0995 -0.1076 265 TYR A CD2 2062 C CE1 . TYR A 265 ? 1.3433 1.2467 1.2351 0.1340 0.1526 -0.1264 265 TYR A CE1 2063 C CE2 . TYR A 265 ? 1.2826 1.0960 1.1811 0.1243 0.1081 -0.1275 265 TYR A CE2 2064 C CZ . TYR A 265 ? 1.3993 1.2552 1.3086 0.1428 0.1353 -0.1384 265 TYR A CZ 2065 O OH . TYR A 265 ? 1.6355 1.4871 1.5756 0.1701 0.1458 -0.1606 265 TYR A OH 2066 N N . ASN A 266 ? 1.1480 1.0572 0.9319 0.0293 0.1084 -0.0431 266 ASN A N 2067 C CA . ASN A 266 ? 1.0015 0.9196 0.7824 0.0095 0.1007 -0.0194 266 ASN A CA 2068 C C . ASN A 266 ? 0.9448 0.8893 0.7660 0.0049 0.1038 0.0065 266 ASN A C 2069 O O . ASN A 266 ? 1.0768 1.0512 0.9223 0.0159 0.1182 0.0104 266 ASN A O 2070 C CB . ASN A 266 ? 1.0342 0.9752 0.7790 0.0038 0.1090 -0.0178 266 ASN A CB 2071 C CG . ASN A 266 ? 1.0830 0.9943 0.7888 -0.0031 0.0961 -0.0342 266 ASN A CG 2072 O OD1 . ASN A 266 ? 1.0664 0.9403 0.7750 -0.0075 0.0802 -0.0418 266 ASN A OD1 2073 N ND2 . ASN A 266 ? 1.2449 1.1751 0.9139 -0.0057 0.1022 -0.0382 266 ASN A ND2 2074 N N . PHE A 267 ? 0.8941 0.8281 0.7242 -0.0118 0.0903 0.0231 267 PHE A N 2075 C CA . PHE A 267 ? 0.8627 0.8188 0.7280 -0.0200 0.0908 0.0470 267 PHE A CA 2076 C C . PHE A 267 ? 1.1002 1.0622 0.9580 -0.0360 0.0869 0.0638 267 PHE A C 2077 O O . PHE A 267 ? 0.9978 0.9381 0.8311 -0.0428 0.0777 0.0576 267 PHE A O 2078 C CB . PHE A 267 ? 0.8431 0.7772 0.7348 -0.0240 0.0762 0.0489 267 PHE A CB 2079 C CG . PHE A 267 ? 0.8906 0.8209 0.7986 -0.0083 0.0774 0.0381 267 PHE A CG 2080 C CD1 . PHE A 267 ? 0.9209 0.8175 0.8112 -0.0010 0.0698 0.0188 267 PHE A CD1 2081 C CD2 . PHE A 267 ? 1.0513 1.0124 0.9973 -0.0009 0.0851 0.0487 267 PHE A CD2 2082 C CE1 . PHE A 267 ? 0.9585 0.8493 0.8692 0.0146 0.0693 0.0104 267 PHE A CE1 2083 C CE2 . PHE A 267 ? 0.9977 0.9569 0.9653 0.0152 0.0852 0.0401 267 PHE A CE2 2084 C CZ . PHE A 267 ? 0.9644 0.8871 0.9147 0.0236 0.0770 0.0210 267 PHE A CZ 2085 N N . THR A 268 ? 1.1803 1.1721 1.0633 -0.0422 0.0932 0.0864 268 THR A N 2086 C CA . THR A 268 ? 0.9046 0.9025 0.7874 -0.0563 0.0891 0.1056 268 THR A CA 2087 C C . THR A 268 ? 0.7594 0.7647 0.6846 -0.0672 0.0846 0.1262 268 THR A C 2088 O O . THR A 268 ? 0.7652 0.7938 0.7182 -0.0643 0.0920 0.1347 268 THR A O 2089 C CB . THR A 268 ? 0.7559 0.7875 0.6171 -0.0550 0.1027 0.1160 268 THR A CB 2090 O OG1 . THR A 268 ? 0.7519 0.7763 0.5712 -0.0451 0.1066 0.0929 268 THR A OG1 2091 C CG2 . THR A 268 ? 0.7298 0.7639 0.5914 -0.0695 0.0947 0.1380 268 THR A CG2 2092 N N . GLY A 269 ? 0.7645 0.7500 0.6974 -0.0797 0.0723 0.1328 269 GLY A N 2093 C CA . GLY A 269 ? 0.9981 0.9861 0.9703 -0.0914 0.0668 0.1498 269 GLY A CA 2094 C C . GLY A 269 ? 1.0218 1.0442 1.0115 -0.0964 0.0758 0.1772 269 GLY A C 2095 O O . GLY A 269 ? 1.1602 1.1991 1.1267 -0.0947 0.0826 0.1854 269 GLY A O 2096 N N . GLU A 270 ? 0.8115 0.8461 0.8416 -0.1042 0.0748 0.1926 270 GLU A N 2097 C CA . GLU A 270 ? 0.8511 0.9193 0.9042 -0.1117 0.0827 0.2226 270 GLU A CA 2098 C C . GLU A 270 ? 0.7822 0.8346 0.8582 -0.1263 0.0709 0.2405 270 GLU A C 2099 O O . GLU A 270 ? 0.9511 1.0263 1.0480 -0.1350 0.0743 0.2694 270 GLU A O 2100 C CB . GLU A 270 ? 1.0708 1.1656 1.1611 -0.1128 0.0886 0.2321 270 GLU A CB 2101 C CG . GLU A 270 ? 1.3482 1.4184 1.4692 -0.1208 0.0730 0.2242 270 GLU A CG 2102 C CD . GLU A 270 ? 1.4703 1.5706 1.6336 -0.1247 0.0760 0.2377 270 GLU A CD 2103 O OE1 . GLU A 270 ? 1.5456 1.6865 1.7231 -0.1248 0.0907 0.2593 270 GLU A OE1 2104 O OE2 . GLU A 270 ? 1.3932 1.4789 1.5756 -0.1286 0.0635 0.2277 270 GLU A OE2 2105 N N . GLN A 271 ? 0.7033 0.7171 0.7773 -0.1288 0.0575 0.2238 271 GLN A N 2106 C CA . GLN A 271 ? 0.7981 0.7926 0.8987 -0.1401 0.0464 0.2358 271 GLN A CA 2107 C C . GLN A 271 ? 0.9129 0.8797 0.9915 -0.1368 0.0392 0.2207 271 GLN A C 2108 O O . GLN A 271 ? 1.0558 1.0033 1.1112 -0.1309 0.0373 0.1943 271 GLN A O 2109 C CB . GLN A 271 ? 0.7649 0.7412 0.9039 -0.1499 0.0370 0.2310 271 GLN A CB 2110 C CG . GLN A 271 ? 0.6248 0.5756 0.7951 -0.1602 0.0257 0.2378 271 GLN A CG 2111 C CD . GLN A 271 ? 0.5752 0.5045 0.7776 -0.1704 0.0159 0.2264 271 GLN A CD 2112 O OE1 . GLN A 271 ? 0.5751 0.4720 0.7810 -0.1727 0.0081 0.2065 271 GLN A OE1 2113 N NE2 . GLN A 271 ? 0.5764 0.5258 0.8028 -0.1772 0.0165 0.2383 271 GLN A NE2 2114 N N . MET A 272 ? 0.8811 0.8478 0.9704 -0.1414 0.0345 0.2399 272 MET A N 2115 C CA . MET A 272 ? 0.7175 0.6628 0.7955 -0.1388 0.0268 0.2299 272 MET A CA 2116 C C . MET A 272 ? 0.6617 0.5722 0.7607 -0.1414 0.0192 0.2079 272 MET A C 2117 O O . MET A 272 ? 0.7846 0.6853 0.9156 -0.1485 0.0163 0.2079 272 MET A O 2118 C CB . MET A 272 ? 0.7158 0.6715 0.8095 -0.1435 0.0213 0.2604 272 MET A CB 2119 C CG . MET A 272 ? 0.6212 0.6140 0.6864 -0.1427 0.0290 0.2825 272 MET A CG 2120 S SD . MET A 272 ? 1.6503 1.6573 1.7310 -0.1505 0.0192 0.3236 272 MET A SD 2121 C CE . MET A 272 ? 0.7936 0.7719 0.8714 -0.1453 0.0056 0.3058 272 MET A CE 2122 N N . ALA A 273 ? 0.5765 0.4702 0.6560 -0.1366 0.0166 0.1880 273 ALA A N 2123 C CA . ALA A 273 ? 0.5847 0.4491 0.6809 -0.1388 0.0118 0.1667 273 ALA A CA 2124 C C . ALA A 273 ? 0.5782 0.4297 0.6690 -0.1416 0.0132 0.1443 273 ALA A C 2125 O O . ALA A 273 ? 0.5750 0.4044 0.6714 -0.1444 0.0111 0.1235 273 ALA A O 2126 C CB . ALA A 273 ? 0.5973 0.4508 0.7420 -0.1440 0.0055 0.1807 273 ALA A CB 2127 N N . ALA A 274 ? 0.6461 0.5138 0.7263 -0.1411 0.0169 0.1491 274 ALA A N 2128 C CA . ALA A 274 ? 0.6335 0.4931 0.7101 -0.1443 0.0154 0.1325 274 ALA A CA 2129 C C . ALA A 274 ? 0.6382 0.4844 0.6787 -0.1399 0.0156 0.1088 274 ALA A C 2130 O O . ALA A 274 ? 0.5495 0.3859 0.5834 -0.1437 0.0122 0.0944 274 ALA A O 2131 C CB . ALA A 274 ? 0.6769 0.5619 0.7575 -0.1432 0.0192 0.1465 274 ALA A CB 2132 N N . TYR A 275 ? 0.5992 0.4460 0.6171 -0.1334 0.0182 0.1067 275 TYR A N 2133 C CA . TYR A 275 ? 0.6208 0.4554 0.6062 -0.1304 0.0180 0.0875 275 TYR A CA 2134 C C . TYR A 275 ? 0.6185 0.4576 0.5837 -0.1260 0.0188 0.0826 275 TYR A C 2135 O O . TYR A 275 ? 0.5865 0.4115 0.5381 -0.1286 0.0152 0.0683 275 TYR A O 2136 C CB . TYR A 275 ? 0.7528 0.5657 0.7425 -0.1375 0.0154 0.0694 275 TYR A CB 2137 C CG . TYR A 275 ? 0.7535 0.5590 0.7287 -0.1358 0.0165 0.0599 275 TYR A CG 2138 C CD1 . TYR A 275 ? 0.7332 0.5449 0.7231 -0.1331 0.0163 0.0701 275 TYR A CD1 2139 C CD2 . TYR A 275 ? 0.7013 0.4955 0.6506 -0.1382 0.0164 0.0435 275 TYR A CD2 2140 C CE1 . TYR A 275 ? 0.5869 0.3952 0.5685 -0.1323 0.0161 0.0627 275 TYR A CE1 2141 C CE2 . TYR A 275 ? 0.6982 0.4884 0.6381 -0.1383 0.0175 0.0365 275 TYR A CE2 2142 C CZ . TYR A 275 ? 0.6378 0.4359 0.5952 -0.1352 0.0173 0.0455 275 TYR A CZ 2143 O OH . TYR A 275 ? 0.7255 0.5228 0.6785 -0.1360 0.0171 0.0396 275 TYR A OH 2144 N N . PHE A 276 ? 0.7589 0.6196 0.7242 -0.1193 0.0238 0.0956 276 PHE A N 2145 C CA . PHE A 276 ? 0.7563 0.6244 0.7080 -0.1114 0.0263 0.0914 276 PHE A CA 2146 C C . PHE A 276 ? 0.6975 0.5490 0.6164 -0.1062 0.0246 0.0751 276 PHE A C 2147 O O . PHE A 276 ? 0.8444 0.6957 0.7455 -0.1031 0.0265 0.0734 276 PHE A O 2148 C CB . PHE A 276 ? 0.7929 0.6908 0.7494 -0.1039 0.0358 0.1066 276 PHE A CB 2149 C CG . PHE A 276 ? 0.6898 0.5986 0.6385 -0.0928 0.0410 0.1012 276 PHE A CG 2150 C CD1 . PHE A 276 ? 0.8122 0.7331 0.7870 -0.0930 0.0401 0.1068 276 PHE A CD1 2151 C CD2 . PHE A 276 ? 0.7155 0.6230 0.6344 -0.0818 0.0460 0.0901 276 PHE A CD2 2152 C CE1 . PHE A 276 ? 0.8541 0.7868 0.8289 -0.0808 0.0450 0.1026 276 PHE A CE1 2153 C CE2 . PHE A 276 ? 0.7621 0.6778 0.6789 -0.0694 0.0515 0.0831 276 PHE A CE2 2154 C CZ . PHE A 276 ? 0.7838 0.7131 0.7305 -0.0680 0.0515 0.0900 276 PHE A CZ 2155 N N . GLY A 277 ? 0.8584 0.6961 0.7702 -0.1066 0.0192 0.0648 277 GLY A N 2156 C CA . GLY A 277 ? 0.9235 0.7422 0.8080 -0.1041 0.0158 0.0515 277 GLY A CA 2157 C C . GLY A 277 ? 0.7817 0.5802 0.6582 -0.1154 0.0102 0.0426 277 GLY A C 2158 O O . GLY A 277 ? 0.6402 0.4247 0.4963 -0.1161 0.0080 0.0341 277 GLY A O 2159 N N . PHE A 278 ? 0.9496 0.7473 0.8429 -0.1250 0.0086 0.0436 278 PHE A N 2160 C CA . PHE A 278 ? 0.8115 0.5934 0.6973 -0.1358 0.0062 0.0326 278 PHE A CA 2161 C C . PHE A 278 ? 0.6983 0.4675 0.5633 -0.1398 -0.0005 0.0265 278 PHE A C 2162 O O . PHE A 278 ? 0.8101 0.5671 0.6584 -0.1471 -0.0012 0.0185 278 PHE A O 2163 C CB . PHE A 278 ? 0.7101 0.4928 0.6184 -0.1444 0.0063 0.0313 278 PHE A CB 2164 C CG . PHE A 278 ? 0.6400 0.4091 0.5389 -0.1553 0.0064 0.0165 278 PHE A CG 2165 C CD1 . PHE A 278 ? 0.7886 0.5547 0.6919 -0.1565 0.0125 0.0098 278 PHE A CD1 2166 C CD2 . PHE A 278 ? 0.6170 0.3796 0.5033 -0.1647 0.0006 0.0096 278 PHE A CD2 2167 C CE1 . PHE A 278 ? 0.8248 0.5826 0.7207 -0.1658 0.0160 -0.0053 278 PHE A CE1 2168 C CE2 . PHE A 278 ? 0.6475 0.4010 0.5204 -0.1757 0.0028 -0.0050 278 PHE A CE2 2169 C CZ . PHE A 278 ? 0.5927 0.3445 0.4708 -0.1758 0.0121 -0.0134 278 PHE A CZ 2170 N N . SER A 279 ? 0.6102 0.3842 0.4790 -0.1353 -0.0055 0.0326 279 SER A N 2171 C CA . SER A 279 ? 0.7145 0.4771 0.5679 -0.1381 -0.0147 0.0316 279 SER A CA 2172 C C . SER A 279 ? 0.7274 0.4967 0.5892 -0.1244 -0.0172 0.0387 279 SER A C 2173 O O . SER A 279 ? 0.8406 0.6286 0.7239 -0.1170 -0.0129 0.0456 279 SER A O 2174 C CB . SER A 279 ? 0.9323 0.6938 0.7864 -0.1518 -0.0222 0.0303 279 SER A CB 2175 O OG . SER A 279 ? 0.9883 0.7650 0.8683 -0.1508 -0.0237 0.0369 279 SER A OG 2176 N N . VAL A 280 ? 0.7290 0.4833 0.5765 -0.1209 -0.0235 0.0375 280 VAL A N 2177 C CA . VAL A 280 ? 0.6850 0.4426 0.5435 -0.1055 -0.0253 0.0414 280 VAL A CA 2178 C C . VAL A 280 ? 0.7215 0.4649 0.5772 -0.1080 -0.0400 0.0467 280 VAL A C 2179 O O . VAL A 280 ? 0.9422 0.6692 0.7777 -0.1216 -0.0474 0.0465 280 VAL A O 2180 C CB . VAL A 280 ? 0.6863 0.4373 0.5341 -0.0932 -0.0177 0.0330 280 VAL A CB 2181 C CG1 . VAL A 280 ? 0.6697 0.4413 0.5231 -0.0883 -0.0047 0.0326 280 VAL A CG1 2182 C CG2 . VAL A 280 ? 0.7781 0.5051 0.6010 -0.1025 -0.0219 0.0261 280 VAL A CG2 2183 N N . ALA A 281 ? 0.7453 0.4972 0.6233 -0.0950 -0.0439 0.0532 281 ALA A N 2184 C CA . ALA A 281 ? 0.8618 0.6012 0.7438 -0.0952 -0.0601 0.0619 281 ALA A CA 2185 C C . ALA A 281 ? 0.8864 0.6300 0.7951 -0.0730 -0.0593 0.0633 281 ALA A C 2186 O O . ALA A 281 ? 0.9215 0.6873 0.8492 -0.0597 -0.0460 0.0599 281 ALA A O 2187 C CB . ALA A 281 ? 0.9940 0.7451 0.8827 -0.1094 -0.0726 0.0729 281 ALA A CB 2188 N N . ALA A 282 ? 0.8564 0.5794 0.7681 -0.0691 -0.0731 0.0687 282 ALA A N 2189 C CA . ALA A 282 ? 0.8675 0.5913 0.8098 -0.0462 -0.0732 0.0684 282 ALA A CA 2190 C C . ALA A 282 ? 0.9570 0.6754 0.9207 -0.0467 -0.0950 0.0865 282 ALA A C 2191 O O . ALA A 282 ? 1.2593 0.9527 1.2044 -0.0596 -0.1108 0.0949 282 ALA A O 2192 C CB . ALA A 282 ? 0.8873 0.5841 0.8162 -0.0349 -0.0670 0.0527 282 ALA A CB 2193 N N . THR A 283 ? 0.9039 0.6486 0.9084 -0.0337 -0.0963 0.0947 283 THR A N 2194 C CA . THR A 283 ? 0.9469 0.6916 0.9802 -0.0317 -0.1186 0.1141 283 THR A CA 2195 C C . THR A 283 ? 1.1289 0.9013 1.2159 -0.0066 -0.1118 0.1154 283 THR A C 2196 O O . THR A 283 ? 1.4088 1.2077 1.5062 0.0026 -0.0904 0.1048 283 THR A O 2197 C CB . THR A 283 ? 0.9282 0.6866 0.9518 -0.0563 -0.1359 0.1309 283 THR A CB 2198 O OG1 . THR A 283 ? 1.1063 0.8539 1.0829 -0.0779 -0.1305 0.1225 283 THR A OG1 2199 C CG2 . THR A 283 ? 1.0933 0.8382 1.1249 -0.0621 -0.1644 0.1527 283 THR A CG2 2200 N N . ASP A 284 ? 0.9811 0.7497 1.1044 0.0044 -0.1296 0.1299 284 ASP A N 2201 C CA . ASP A 284 ? 0.9711 0.7736 1.1530 0.0265 -0.1247 0.1343 284 ASP A CA 2202 C C . ASP A 284 ? 0.9252 0.7595 1.1280 0.0110 -0.1425 0.1569 284 ASP A C 2203 O O . ASP A 284 ? 0.9231 0.7486 1.1316 0.0008 -0.1703 0.1773 284 ASP A O 2204 C CB . ASP A 284 ? 1.0920 0.8749 1.3124 0.0508 -0.1338 0.1365 284 ASP A CB 2205 C CG . ASP A 284 ? 1.2157 1.0369 1.5025 0.0769 -0.1254 0.1387 284 ASP A CG 2206 O OD1 . ASP A 284 ? 1.5102 1.3262 1.8428 0.0918 -0.1425 0.1520 284 ASP A OD1 2207 O OD2 . ASP A 284 ? 1.0082 0.8660 1.3040 0.0823 -0.1015 0.1288 284 ASP A OD2 2208 N N . ILE A 285 ? 0.8863 0.7575 1.0999 0.0075 -0.1276 0.1541 285 ILE A N 2209 C CA . ILE A 285 ? 0.8511 0.7513 1.0811 -0.0109 -0.1441 0.1724 285 ILE A CA 2210 C C . ILE A 285 ? 0.8454 0.7838 1.1458 0.0058 -0.1507 0.1880 285 ILE A C 2211 O O . ILE A 285 ? 1.0011 0.9613 1.3230 -0.0086 -0.1725 0.2071 285 ILE A O 2212 C CB . ILE A 285 ? 0.8402 0.7587 1.0494 -0.0268 -0.1277 0.1637 285 ILE A CB 2213 C CG1 . ILE A 285 ? 0.8338 0.7563 1.0268 -0.0566 -0.1497 0.1753 285 ILE A CG1 2214 C CG2 . ILE A 285 ? 0.9868 0.9480 1.2419 -0.0105 -0.1058 0.1625 285 ILE A CG2 2215 C CD1 . ILE A 285 ? 0.8280 0.7123 0.9614 -0.0766 -0.1609 0.1705 285 ILE A CD1 2216 N N . ASN A 286 ? 0.8422 0.7901 1.1797 0.0359 -0.1318 0.1786 286 ASN A N 2217 C CA . ASN A 286 ? 0.8384 0.8270 1.2498 0.0556 -0.1333 0.1913 286 ASN A CA 2218 C C . ASN A 286 ? 0.8845 0.8556 1.3330 0.0738 -0.1539 0.2025 286 ASN A C 2219 O O . ASN A 286 ? 1.0349 1.0386 1.5517 0.0926 -0.1576 0.2142 286 ASN A O 2220 C CB . ASN A 286 ? 0.8487 0.8688 1.2853 0.0784 -0.0961 0.1741 286 ASN A CB 2221 C CG . ASN A 286 ? 0.8849 0.8715 1.2783 0.0910 -0.0729 0.1463 286 ASN A CG 2222 O OD1 . ASN A 286 ? 0.9081 0.8481 1.2529 0.0808 -0.0837 0.1401 286 ASN A OD1 2223 N ND2 . ASN A 286 ? 0.8918 0.9044 1.3016 0.1117 -0.0408 0.1297 286 ASN A ND2 2224 N N . GLY A 287 ? 0.8454 0.7662 1.2530 0.0684 -0.1675 0.2002 287 GLY A N 2225 C CA . GLY A 287 ? 0.8691 0.7660 1.3097 0.0844 -0.1886 0.2123 287 GLY A CA 2226 C C . GLY A 287 ? 0.8846 0.7827 1.3721 0.1228 -0.1659 0.1936 287 GLY A C 2227 O O . GLY A 287 ? 0.8529 0.7466 1.3954 0.1437 -0.1802 0.2046 287 GLY A O 2228 N N . ASP A 288 ? 0.9805 0.8848 1.4462 0.1322 -0.1306 0.1649 288 ASP A N 2229 C CA . ASP A 288 ? 0.9453 0.8549 1.4474 0.1677 -0.1037 0.1411 288 ASP A CA 2230 C C . ASP A 288 ? 0.9357 0.7873 1.4022 0.1768 -0.1001 0.1183 288 ASP A C 2231 O O . ASP A 288 ? 0.9705 0.8181 1.4526 0.2041 -0.0761 0.0913 288 ASP A O 2232 C CB . ASP A 288 ? 0.8704 0.8244 1.3689 0.1726 -0.0669 0.1236 288 ASP A CB 2233 C CG . ASP A 288 ? 0.8789 0.8096 1.3015 0.1573 -0.0493 0.1021 288 ASP A CG 2234 O OD1 . ASP A 288 ? 0.8909 0.8001 1.2639 0.1282 -0.0653 0.1114 288 ASP A OD1 2235 O OD2 . ASP A 288 ? 0.8988 0.8348 1.3119 0.1747 -0.0191 0.0755 288 ASP A OD2 2236 N N . ASP A 289 ? 0.9108 0.7195 1.3280 0.1522 -0.1231 0.1283 289 ASP A N 2237 C CA . ASP A 289 ? 0.9638 0.7144 1.3458 0.1539 -0.1259 0.1122 289 ASP A CA 2238 C C . ASP A 289 ? 0.9692 0.7111 1.2966 0.1510 -0.0968 0.0800 289 ASP A C 2239 O O . ASP A 289 ? 1.0296 0.7257 1.3227 0.1488 -0.0981 0.0648 289 ASP A O 2240 C CB . ASP A 289 ? 1.2413 0.9684 1.6797 0.1865 -0.1302 0.1056 289 ASP A CB 2241 C CG . ASP A 289 ? 1.4429 1.1676 1.9317 0.1869 -0.1657 0.1416 289 ASP A CG 2242 O OD1 . ASP A 289 ? 1.3635 1.1008 1.9239 0.2168 -0.1663 0.1433 289 ASP A OD1 2243 O OD2 . ASP A 289 ? 1.5917 1.3038 2.0488 0.1574 -0.1930 0.1685 289 ASP A OD2 2244 N N . TYR A 290 ? 0.9533 0.7396 1.2741 0.1498 -0.0725 0.0718 290 TYR A N 2245 C CA . TYR A 290 ? 0.9495 0.7329 1.2159 0.1430 -0.0482 0.0472 290 TYR A CA 2246 C C . TYR A 290 ? 0.9315 0.7198 1.1502 0.1093 -0.0552 0.0605 290 TYR A C 2247 O O . TYR A 290 ? 0.9064 0.7302 1.1400 0.0977 -0.0592 0.0791 290 TYR A O 2248 C CB . TYR A 290 ? 0.9487 0.7773 1.2355 0.1634 -0.0147 0.0292 290 TYR A CB 2249 C CG . TYR A 290 ? 0.9787 0.7992 1.2996 0.1980 0.0005 0.0043 290 TYR A CG 2250 C CD1 . TYR A 290 ? 0.9870 0.8561 1.3505 0.2218 0.0270 -0.0053 290 TYR A CD1 2251 C CD2 . TYR A 290 ? 1.0163 0.7808 1.3286 0.2065 -0.0109 -0.0106 290 TYR A CD2 2252 C CE1 . TYR A 290 ? 1.0122 0.8749 1.4076 0.2550 0.0434 -0.0321 290 TYR A CE1 2253 C CE2 . TYR A 290 ? 1.1411 0.8943 1.4862 0.2390 0.0030 -0.0371 290 TYR A CE2 2254 C CZ . TYR A 290 ? 1.1339 0.9365 1.5198 0.2641 0.0310 -0.0493 290 TYR A CZ 2255 O OH . TYR A 290 ? 1.2546 1.0469 1.6738 0.2979 0.0472 -0.0796 290 TYR A OH 2256 N N . ALA A 291 ? 0.9391 0.6917 1.1036 0.0939 -0.0568 0.0500 291 ALA A N 2257 C CA . ALA A 291 ? 0.8646 0.6178 0.9849 0.0637 -0.0623 0.0594 291 ALA A CA 2258 C C . ALA A 291 ? 0.9082 0.7014 1.0194 0.0598 -0.0398 0.0540 291 ALA A C 2259 O O . ALA A 291 ? 0.8711 0.6779 0.9813 0.0754 -0.0166 0.0355 291 ALA A O 2260 C CB . ALA A 291 ? 0.8943 0.6035 0.9660 0.0508 -0.0670 0.0485 291 ALA A CB 2261 N N . ASP A 292 ? 0.8977 0.7088 1.0014 0.0380 -0.0473 0.0703 292 ASP A N 2262 C CA . ASP A 292 ? 0.9056 0.7531 1.0069 0.0319 -0.0296 0.0701 292 ASP A CA 2263 C C . ASP A 292 ? 0.9112 0.7447 0.9654 0.0078 -0.0303 0.0681 292 ASP A C 2264 O O . ASP A 292 ? 0.8731 0.6789 0.9035 -0.0085 -0.0473 0.0726 292 ASP A O 2265 C CB . ASP A 292 ? 0.9075 0.7932 1.0530 0.0289 -0.0365 0.0903 292 ASP A CB 2266 C CG . ASP A 292 ? 1.0653 0.9627 1.2639 0.0510 -0.0424 0.0966 292 ASP A CG 2267 O OD1 . ASP A 292 ? 1.1125 1.0001 1.3278 0.0450 -0.0678 0.1131 292 ASP A OD1 2268 O OD2 . ASP A 292 ? 1.2703 1.1879 1.4946 0.0747 -0.0215 0.0852 292 ASP A OD2 2269 N N . VAL A 293 ? 0.9626 0.8169 1.0054 0.0058 -0.0114 0.0623 293 VAL A N 2270 C CA . VAL A 293 ? 0.8756 0.7165 0.8785 -0.0126 -0.0095 0.0581 293 VAL A CA 2271 C C . VAL A 293 ? 0.8477 0.7065 0.8568 -0.0319 -0.0140 0.0714 293 VAL A C 2272 O O . VAL A 293 ? 0.8955 0.7878 0.9354 -0.0298 -0.0077 0.0812 293 VAL A O 2273 C CB . VAL A 293 ? 0.8968 0.7453 0.8796 -0.0042 0.0115 0.0441 293 VAL A CB 2274 C CG1 . VAL A 293 ? 0.8734 0.7056 0.8192 -0.0216 0.0106 0.0405 293 VAL A CG1 2275 C CG2 . VAL A 293 ? 0.9371 0.7682 0.9144 0.0155 0.0169 0.0265 293 VAL A CG2 2276 N N . PHE A 294 ? 0.8283 0.6649 0.8097 -0.0509 -0.0244 0.0708 294 PHE A N 2277 C CA . PHE A 294 ? 0.9220 0.7687 0.9054 -0.0697 -0.0284 0.0781 294 PHE A CA 2278 C C . PHE A 294 ? 0.9534 0.7887 0.9082 -0.0793 -0.0199 0.0696 294 PHE A C 2279 O O . PHE A 294 ? 1.1784 0.9879 1.1041 -0.0843 -0.0232 0.0610 294 PHE A O 2280 C CB . PHE A 294 ? 0.9157 0.7498 0.8957 -0.0848 -0.0495 0.0847 294 PHE A CB 2281 C CG . PHE A 294 ? 0.8339 0.6820 0.8469 -0.0774 -0.0621 0.0970 294 PHE A CG 2282 C CD1 . PHE A 294 ? 0.8560 0.6900 0.8731 -0.0635 -0.0685 0.0977 294 PHE A CD1 2283 C CD2 . PHE A 294 ? 0.8211 0.6958 0.8650 -0.0846 -0.0691 0.1087 294 PHE A CD2 2284 C CE1 . PHE A 294 ? 0.9782 0.8261 1.0319 -0.0552 -0.0813 0.1108 294 PHE A CE1 2285 C CE2 . PHE A 294 ? 0.8582 0.7491 0.9372 -0.0779 -0.0824 0.1219 294 PHE A CE2 2286 C CZ . PHE A 294 ? 0.9529 0.8311 1.0379 -0.0623 -0.0884 0.1235 294 PHE A CZ 2287 N N . ILE A 295 ? 0.7649 0.6206 0.7320 -0.0824 -0.0097 0.0740 295 ILE A N 2288 C CA . ILE A 295 ? 0.7255 0.5737 0.6731 -0.0892 -0.0020 0.0686 295 ILE A CA 2289 C C . ILE A 295 ? 0.7061 0.5575 0.6652 -0.1054 -0.0054 0.0735 295 ILE A C 2290 O O . ILE A 295 ? 0.8357 0.7090 0.8236 -0.1074 -0.0035 0.0844 295 ILE A O 2291 C CB . ILE A 295 ? 0.7288 0.5955 0.6767 -0.0771 0.0142 0.0698 295 ILE A CB 2292 C CG1 . ILE A 295 ? 0.7505 0.6126 0.6870 -0.0600 0.0188 0.0602 295 ILE A CG1 2293 C CG2 . ILE A 295 ? 0.7081 0.5668 0.6374 -0.0844 0.0185 0.0669 295 ILE A CG2 2294 C CD1 . ILE A 295 ? 0.7593 0.6468 0.6971 -0.0468 0.0361 0.0602 295 ILE A CD1 2295 N N . GLY A 296 ? 0.6877 0.5176 0.6269 -0.1170 -0.0097 0.0645 296 GLY A N 2296 C CA . GLY A 296 ? 0.6896 0.5177 0.6394 -0.1313 -0.0122 0.0640 296 GLY A CA 2297 C C . GLY A 296 ? 0.9890 0.8231 0.9485 -0.1308 -0.0021 0.0675 296 GLY A C 2298 O O . GLY A 296 ? 1.1148 0.9459 1.0590 -0.1241 0.0049 0.0652 296 GLY A O 2299 N N . ALA A 297 ? 1.0888 0.9306 1.0755 -0.1391 -0.0035 0.0744 297 ALA A N 2300 C CA . ALA A 297 ? 0.8070 0.6513 0.8091 -0.1411 0.0028 0.0805 297 ALA A CA 2301 C C . ALA A 297 ? 0.7387 0.5716 0.7617 -0.1551 -0.0039 0.0758 297 ALA A C 2302 O O . ALA A 297 ? 0.7138 0.5578 0.7680 -0.1604 -0.0061 0.0877 297 ALA A O 2303 C CB . ALA A 297 ? 0.6241 0.4957 0.6455 -0.1340 0.0106 0.1000 297 ALA A CB 2304 N N . PRO A 298 ? 0.7161 0.5272 0.7223 -0.1618 -0.0065 0.0574 298 PRO A N 2305 C CA . PRO A 298 ? 0.6582 0.4551 0.6770 -0.1753 -0.0127 0.0453 298 PRO A CA 2306 C C . PRO A 298 ? 0.7550 0.5488 0.8096 -0.1781 -0.0103 0.0510 298 PRO A C 2307 O O . PRO A 298 ? 1.1097 0.8931 1.1839 -0.1891 -0.0166 0.0434 298 PRO A O 2308 C CB . PRO A 298 ? 0.7359 0.5149 0.7240 -0.1785 -0.0105 0.0244 298 PRO A CB 2309 C CG . PRO A 298 ? 0.5728 0.3549 0.5466 -0.1670 -0.0023 0.0290 298 PRO A CG 2310 C CD . PRO A 298 ? 0.5636 0.3633 0.5382 -0.1573 -0.0025 0.0462 298 PRO A CD 2311 N N . LEU A 299 ? 0.5863 0.3875 0.6493 -0.1690 -0.0029 0.0643 299 LEU A N 2312 C CA . LEU A 299 ? 0.5917 0.3892 0.6911 -0.1711 -0.0022 0.0742 299 LEU A CA 2313 C C . LEU A 299 ? 0.7608 0.5793 0.8884 -0.1720 -0.0031 0.1013 299 LEU A C 2314 O O . LEU A 299 ? 0.8572 0.6748 1.0172 -0.1745 -0.0037 0.1161 299 LEU A O 2315 C CB . LEU A 299 ? 0.6014 0.3959 0.6966 -0.1627 0.0041 0.0756 299 LEU A CB 2316 C CG . LEU A 299 ? 0.6226 0.3953 0.7211 -0.1646 0.0059 0.0532 299 LEU A CG 2317 C CD1 . LEU A 299 ? 0.5846 0.3448 0.6596 -0.1725 0.0045 0.0275 299 LEU A CD1 2318 C CD2 . LEU A 299 ? 0.9398 0.7165 1.0234 -0.1557 0.0114 0.0538 299 LEU A CD2 2319 N N . PHE A 300 ? 0.8410 0.6796 0.9592 -0.1699 -0.0030 0.1093 300 PHE A N 2320 C CA . PHE A 300 ? 0.5617 0.4272 0.7058 -0.1705 -0.0008 0.1356 300 PHE A CA 2321 C C . PHE A 300 ? 0.5721 0.4327 0.7592 -0.1848 -0.0094 0.1431 300 PHE A C 2322 O O . PHE A 300 ? 0.6413 0.4844 0.8325 -0.1946 -0.0190 0.1254 300 PHE A O 2323 C CB . PHE A 300 ? 0.6686 0.5573 0.7990 -0.1641 0.0019 0.1388 300 PHE A CB 2324 C CG . PHE A 300 ? 0.6642 0.5867 0.8222 -0.1640 0.0075 0.1648 300 PHE A CG 2325 C CD1 . PHE A 300 ? 0.5902 0.5362 0.7382 -0.1541 0.0203 0.1805 300 PHE A CD1 2326 C CD2 . PHE A 300 ? 0.6992 0.6326 0.8926 -0.1751 0.0001 0.1738 300 PHE A CD2 2327 C CE1 . PHE A 300 ? 0.6763 0.6579 0.8479 -0.1547 0.0282 0.2048 300 PHE A CE1 2328 C CE2 . PHE A 300 ? 0.6269 0.5957 0.8491 -0.1760 0.0068 0.1994 300 PHE A CE2 2329 C CZ . PHE A 300 ? 0.6763 0.6703 0.8871 -0.1655 0.0222 0.2151 300 PHE A CZ 2330 N N . MET A 301 ? 0.5750 0.4515 0.7929 -0.1874 -0.0067 0.1700 301 MET A N 2331 C CA . MET A 301 ? 0.5876 0.4596 0.8519 -0.2023 -0.0156 0.1814 301 MET A CA 2332 C C . MET A 301 ? 0.6287 0.5372 0.9165 -0.2068 -0.0134 0.2072 301 MET A C 2333 O O . MET A 301 ? 0.6501 0.5872 0.9392 -0.2012 -0.0026 0.2321 301 MET A O 2334 C CB . MET A 301 ? 0.5980 0.4553 0.8901 -0.2049 -0.0166 0.1951 301 MET A CB 2335 C CG . MET A 301 ? 0.6009 0.4258 0.8794 -0.1993 -0.0173 0.1709 301 MET A CG 2336 S SD . MET A 301 ? 1.3494 1.1546 1.6743 -0.2020 -0.0217 0.1877 301 MET A SD 2337 C CE . MET A 301 ? 0.6113 0.4548 0.9312 -0.1962 -0.0142 0.2302 301 MET A CE 2338 N N . ASP A 302 ? 0.7443 0.6543 1.0503 -0.2175 -0.0236 0.2012 302 ASP A N 2339 C CA . ASP A 302 ? 0.6780 0.6234 1.0187 -0.2247 -0.0232 0.2266 302 ASP A CA 2340 C C . ASP A 302 ? 0.6423 0.5778 1.0337 -0.2428 -0.0328 0.2433 302 ASP A C 2341 O O . ASP A 302 ? 0.6323 0.5351 1.0269 -0.2440 -0.0373 0.2341 302 ASP A O 2342 C CB . ASP A 302 ? 0.8182 0.7749 1.1568 -0.2271 -0.0315 0.2147 302 ASP A CB 2343 C CG . ASP A 302 ? 0.9607 0.8872 1.3119 -0.2442 -0.0514 0.1946 302 ASP A CG 2344 O OD1 . ASP A 302 ? 1.2571 1.1462 1.5999 -0.2480 -0.0557 0.1764 302 ASP A OD1 2345 O OD2 . ASP A 302 ? 0.8095 0.7510 1.1794 -0.2537 -0.0628 0.1962 302 ASP A OD2 2346 N N . ARG A 303 ? 0.6126 0.5773 1.0406 -0.2525 -0.0356 0.2640 303 ARG A N 2347 C CA . ARG A 303 ? 0.6434 0.6002 1.1051 -0.2609 -0.0450 0.2707 303 ARG A CA 2348 C C . ARG A 303 ? 0.7129 0.6676 1.1980 -0.2748 -0.0616 0.2595 303 ARG A C 2349 O O . ARG A 303 ? 0.7591 0.7457 1.2543 -0.2781 -0.0623 0.2678 303 ARG A O 2350 C CB . ARG A 303 ? 0.7233 0.7182 1.2052 -0.2586 -0.0336 0.3075 303 ARG A CB 2351 C CG . ARG A 303 ? 0.6858 0.6806 1.1442 -0.2472 -0.0211 0.3194 303 ARG A CG 2352 C CD . ARG A 303 ? 0.7094 0.7415 1.1841 -0.2472 -0.0118 0.3555 303 ARG A CD 2353 N NE . ARG A 303 ? 0.7742 0.8074 1.2223 -0.2375 -0.0025 0.3670 303 ARG A NE 2354 C CZ . ARG A 303 ? 0.8888 0.8961 1.3439 -0.2367 -0.0107 0.3704 303 ARG A CZ 2355 N NH1 . ARG A 303 ? 0.9350 0.9118 1.4225 -0.2440 -0.0263 0.3618 303 ARG A NH1 2356 N NH2 . ARG A 303 ? 0.9884 1.0012 1.4192 -0.2285 -0.0039 0.3825 303 ARG A NH2 2357 N N . GLY A 304 ? 0.8084 0.7265 1.3033 -0.2828 -0.0753 0.2402 304 GLY A N 2358 C CA . GLY A 304 ? 0.7855 0.6968 1.2981 -0.2977 -0.0929 0.2262 304 GLY A CA 2359 C C . GLY A 304 ? 0.7090 0.6522 1.2655 -0.3065 -0.0969 0.2544 304 GLY A C 2360 O O . GLY A 304 ? 0.8377 0.8143 1.4087 -0.3008 -0.0839 0.2859 304 GLY A O 2361 N N . SER A 305 ? 0.7495 0.6837 1.3258 -0.3213 -0.1148 0.2428 305 SER A N 2362 C CA . SER A 305 ? 0.7848 0.7486 1.4057 -0.3319 -0.1211 0.2681 305 SER A CA 2363 C C . SER A 305 ? 0.8005 0.7608 1.4476 -0.3316 -0.1163 0.2908 305 SER A C 2364 O O . SER A 305 ? 0.8000 0.7975 1.4781 -0.3346 -0.1117 0.3234 305 SER A O 2365 C CB . SER A 305 ? 0.9388 0.8868 1.5722 -0.3492 -0.1437 0.2474 305 SER A CB 2366 O OG . SER A 305 ? 1.1884 1.0849 1.8103 -0.3540 -0.1522 0.2177 305 SER A OG 2367 N N . ASP A 306 ? 0.9035 0.8207 1.5396 -0.3280 -0.1175 0.2745 306 ASP A N 2368 C CA . ASP A 306 ? 1.0751 0.9850 1.7376 -0.3273 -0.1160 0.2961 306 ASP A CA 2369 C C . ASP A 306 ? 1.0327 0.9652 1.6809 -0.3127 -0.0977 0.3215 306 ASP A C 2370 O O . ASP A 306 ? 1.1386 1.0743 1.8068 -0.3117 -0.0959 0.3464 306 ASP A O 2371 C CB . ASP A 306 ? 1.1968 1.0519 1.8603 -0.3290 -0.1261 0.2681 306 ASP A CB 2372 C CG . ASP A 306 ? 1.2683 1.0946 1.8895 -0.3175 -0.1197 0.2361 306 ASP A CG 2373 O OD1 . ASP A 306 ? 1.2519 1.0942 1.8418 -0.3130 -0.1132 0.2280 306 ASP A OD1 2374 O OD2 . ASP A 306 ? 1.3509 1.1392 1.9729 -0.3130 -0.1212 0.2196 306 ASP A OD2 2375 N N . GLY A 307 ? 0.8226 0.7705 1.4356 -0.3023 -0.0854 0.3157 307 GLY A N 2376 C CA . GLY A 307 ? 0.8108 0.7837 1.4051 -0.2894 -0.0675 0.3380 307 GLY A CA 2377 C C . GLY A 307 ? 0.8068 0.7463 1.3741 -0.2780 -0.0641 0.3237 307 GLY A C 2378 O O . GLY A 307 ? 0.8089 0.7655 1.3557 -0.2677 -0.0510 0.3395 307 GLY A O 2379 N N . LYS A 308 ? 0.9416 0.8349 1.5089 -0.2801 -0.0754 0.2933 308 LYS A N 2380 C CA . LYS A 308 ? 0.9139 0.7753 1.4616 -0.2690 -0.0725 0.2774 308 LYS A CA 2381 C C . LYS A 308 ? 0.8366 0.7009 1.3407 -0.2598 -0.0621 0.2614 308 LYS A C 2382 O O . LYS A 308 ? 0.7873 0.6653 1.2771 -0.2635 -0.0616 0.2521 308 LYS A O 2383 C CB . LYS A 308 ? 1.0134 0.8272 1.5736 -0.2734 -0.0849 0.2457 308 LYS A CB 2384 C CG . LYS A 308 ? 1.3007 1.0979 1.8396 -0.2803 -0.0905 0.2089 308 LYS A CG 2385 C CD . LYS A 308 ? 1.4620 1.2120 2.0044 -0.2830 -0.0988 0.1735 308 LYS A CD 2386 C CE . LYS A 308 ? 1.3110 1.0472 1.8247 -0.2914 -0.1041 0.1367 308 LYS A CE 2387 N NZ . LYS A 308 ? 1.0313 0.7775 1.5034 -0.2833 -0.0944 0.1280 308 LYS A NZ 2388 N N . LEU A 309 ? 0.8384 0.6902 1.3243 -0.2481 -0.0554 0.2595 309 LEU A N 2389 C CA . LEU A 309 ? 0.7445 0.5940 1.1901 -0.2398 -0.0467 0.2432 309 LEU A CA 2390 C C . LEU A 309 ? 0.8123 0.6233 1.2444 -0.2417 -0.0531 0.2019 309 LEU A C 2391 O O . LEU A 309 ? 0.9464 0.7260 1.3944 -0.2421 -0.0593 0.1852 309 LEU A O 2392 C CB . LEU A 309 ? 0.7388 0.5920 1.1704 -0.2277 -0.0382 0.2580 309 LEU A CB 2393 C CG . LEU A 309 ? 0.6560 0.5530 1.0779 -0.2246 -0.0272 0.2934 309 LEU A CG 2394 C CD1 . LEU A 309 ? 0.6555 0.5530 1.0621 -0.2146 -0.0226 0.3064 309 LEU A CD1 2395 C CD2 . LEU A 309 ? 0.6325 0.5541 1.0278 -0.2243 -0.0177 0.2903 309 LEU A CD2 2396 N N . GLN A 310 ? 0.8322 0.6471 1.2351 -0.2432 -0.0513 0.1858 310 GLN A N 2397 C CA . GLN A 310 ? 0.9481 0.7314 1.3297 -0.2461 -0.0563 0.1470 310 GLN A CA 2398 C C . GLN A 310 ? 0.8777 0.6682 1.2206 -0.2415 -0.0500 0.1400 310 GLN A C 2399 O O . GLN A 310 ? 1.0754 0.8991 1.4043 -0.2367 -0.0450 0.1563 310 GLN A O 2400 C CB . GLN A 310 ? 1.0563 0.8330 1.4487 -0.2609 -0.0697 0.1311 310 GLN A CB 2401 C CG . GLN A 310 ? 0.8635 0.6753 1.2594 -0.2680 -0.0737 0.1491 310 GLN A CG 2402 C CD . GLN A 310 ? 0.8919 0.6993 1.3019 -0.2837 -0.0898 0.1356 310 GLN A CD 2403 O OE1 . GLN A 310 ? 0.9921 0.7723 1.4150 -0.2900 -0.0970 0.1181 310 GLN A OE1 2404 N NE2 . GLN A 310 ? 0.8602 0.6949 1.2693 -0.2901 -0.0961 0.1439 310 GLN A NE2 2405 N N . GLU A 311 ? 0.7312 0.4979 1.0441 -0.2350 -0.0469 0.1099 311 GLU A N 2406 C CA . GLU A 311 ? 0.7409 0.5189 1.0025 -0.2233 -0.0389 0.0985 311 GLU A CA 2407 C C . GLU A 311 ? 0.7949 0.5694 1.0307 -0.2316 -0.0473 0.0756 311 GLU A C 2408 O O . GLU A 311 ? 0.9796 0.7286 1.2044 -0.2386 -0.0517 0.0466 311 GLU A O 2409 C CB . GLU A 311 ? 0.8548 0.6146 1.0982 -0.2125 -0.0302 0.0824 311 GLU A CB 2410 C CG . GLU A 311 ? 1.1317 0.8942 1.3236 -0.2047 -0.0242 0.0637 311 GLU A CG 2411 C CD . GLU A 311 ? 1.3141 1.0547 1.4950 -0.2000 -0.0178 0.0399 311 GLU A CD 2412 O OE1 . GLU A 311 ? 1.6312 1.3701 1.7727 -0.1978 -0.0138 0.0214 311 GLU A OE1 2413 O OE2 . GLU A 311 ? 1.0729 0.7991 1.2879 -0.1985 -0.0167 0.0410 311 GLU A OE2 2414 N N . VAL A 312 ? 0.6819 0.4839 0.9092 -0.2309 -0.0496 0.0893 312 VAL A N 2415 C CA . VAL A 312 ? 0.6650 0.4681 0.8650 -0.2369 -0.0591 0.0730 312 VAL A CA 2416 C C . VAL A 312 ? 0.6233 0.4351 0.7787 -0.2233 -0.0516 0.0691 312 VAL A C 2417 O O . VAL A 312 ? 0.6244 0.4352 0.7529 -0.2273 -0.0596 0.0571 312 VAL A O 2418 C CB . VAL A 312 ? 0.7094 0.5368 0.9377 -0.2466 -0.0707 0.0905 312 VAL A CB 2419 C CG1 . VAL A 312 ? 0.8136 0.6304 1.0885 -0.2630 -0.0805 0.0946 312 VAL A CG1 2420 C CG2 . VAL A 312 ? 0.7857 0.6492 1.0240 -0.2334 -0.0601 0.1192 312 VAL A CG2 2421 N N . GLY A 313 ? 0.6064 0.4257 0.7540 -0.2085 -0.0379 0.0798 313 GLY A N 2422 C CA . GLY A 313 ? 0.7553 0.5836 0.8667 -0.1955 -0.0314 0.0789 313 GLY A CA 2423 C C . GLY A 313 ? 0.7248 0.5827 0.8444 -0.1895 -0.0321 0.0970 313 GLY A C 2424 O O . GLY A 313 ? 0.7275 0.5998 0.8776 -0.1979 -0.0400 0.1078 313 GLY A O 2425 N N . GLN A 314 ? 0.7213 0.5887 0.8170 -0.1748 -0.0238 0.0996 314 GLN A N 2426 C CA . GLN A 314 ? 0.7615 0.6571 0.8671 -0.1656 -0.0217 0.1138 314 GLN A CA 2427 C C . GLN A 314 ? 0.7706 0.6623 0.8429 -0.1526 -0.0195 0.1053 314 GLN A C 2428 O O . GLN A 314 ? 0.9208 0.7964 0.9640 -0.1469 -0.0134 0.0954 314 GLN A O 2429 C CB . GLN A 314 ? 0.7697 0.6917 0.8980 -0.1585 -0.0083 0.1345 314 GLN A CB 2430 C CG . GLN A 314 ? 0.8027 0.7601 0.9505 -0.1496 -0.0030 0.1493 314 GLN A CG 2431 C CD . GLN A 314 ? 0.7737 0.7596 0.9337 -0.1424 0.0138 0.1681 314 GLN A CD 2432 O OE1 . GLN A 314 ? 0.6512 0.6638 0.8482 -0.1487 0.0163 0.1877 314 GLN A OE1 2433 N NE2 . GLN A 314 ? 0.8606 0.8424 0.9886 -0.1309 0.0250 0.1631 314 GLN A NE2 2434 N N . VAL A 315 ? 0.6466 0.5532 0.7277 -0.1482 -0.0257 0.1104 315 VAL A N 2435 C CA . VAL A 315 ? 0.6811 0.5829 0.7384 -0.1350 -0.0252 0.1045 315 VAL A CA 2436 C C . VAL A 315 ? 0.7751 0.7065 0.8533 -0.1180 -0.0150 0.1160 315 VAL A C 2437 O O . VAL A 315 ? 0.8406 0.7987 0.9552 -0.1191 -0.0174 0.1290 315 VAL A O 2438 C CB . VAL A 315 ? 0.6904 0.5795 0.7373 -0.1434 -0.0436 0.0990 315 VAL A CB 2439 C CG1 . VAL A 315 ? 0.7077 0.5918 0.7387 -0.1291 -0.0448 0.0974 315 VAL A CG1 2440 C CG2 . VAL A 315 ? 0.7712 0.6325 0.7903 -0.1592 -0.0501 0.0839 315 VAL A CG2 2441 N N . SER A 316 ? 0.7464 0.6740 0.8025 -0.1028 -0.0033 0.1097 316 SER A N 2442 C CA . SER A 316 ? 0.7232 0.6776 0.7942 -0.0846 0.0098 0.1151 316 SER A CA 2443 C C . SER A 316 ? 0.7477 0.6961 0.8196 -0.0724 0.0025 0.1096 316 SER A C 2444 O O . SER A 316 ? 0.8366 0.7548 0.8789 -0.0714 -0.0046 0.0980 316 SER A O 2445 C CB . SER A 316 ? 0.7400 0.6947 0.7858 -0.0752 0.0267 0.1097 316 SER A CB 2446 O OG . SER A 316 ? 0.8940 0.8761 0.9502 -0.0577 0.0419 0.1113 316 SER A OG 2447 N N . VAL A 317 ? 0.7347 0.7127 0.8448 -0.0634 0.0038 0.1197 317 VAL A N 2448 C CA . VAL A 317 ? 0.7590 0.7342 0.8807 -0.0495 -0.0039 0.1174 317 VAL A CA 2449 C C . VAL A 317 ? 0.8176 0.8163 0.9551 -0.0253 0.0162 0.1137 317 VAL A C 2450 O O . VAL A 317 ? 1.0441 1.0829 1.2173 -0.0200 0.0284 0.1243 317 VAL A O 2451 C CB . VAL A 317 ? 0.7273 0.7181 0.8866 -0.0579 -0.0228 0.1317 317 VAL A CB 2452 C CG1 . VAL A 317 ? 0.7588 0.7531 0.9410 -0.0404 -0.0301 0.1335 317 VAL A CG1 2453 C CG2 . VAL A 317 ? 0.6900 0.6542 0.8260 -0.0813 -0.0435 0.1305 317 VAL A CG2 2454 N N . SER A 318 ? 0.8385 0.8128 0.9500 -0.0113 0.0201 0.0976 318 SER A N 2455 C CA . SER A 318 ? 0.8829 0.8745 1.0029 0.0124 0.0404 0.0876 318 SER A CA 2456 C C . SER A 318 ? 0.9012 0.8811 1.0426 0.0308 0.0324 0.0817 318 SER A C 2457 O O . SER A 318 ? 0.9059 0.8456 1.0232 0.0311 0.0195 0.0723 318 SER A O 2458 C CB . SER A 318 ? 0.9073 0.8809 0.9802 0.0150 0.0536 0.0707 318 SER A CB 2459 O OG . SER A 318 ? 0.8738 0.8586 0.9311 -0.0008 0.0596 0.0789 318 SER A OG 2460 N N . LEU A 319 ? 0.8904 0.9067 1.0813 0.0460 0.0399 0.0887 319 LEU A N 2461 C CA . LEU A 319 ? 0.8956 0.9051 1.1188 0.0662 0.0323 0.0853 319 LEU A CA 2462 C C . LEU A 319 ? 0.9332 0.9378 1.1492 0.0920 0.0537 0.0612 319 LEU A C 2463 O O . LEU A 319 ? 0.9387 0.9792 1.1622 0.1032 0.0802 0.0547 319 LEU A O 2464 C CB . LEU A 319 ? 0.8534 0.9071 1.1414 0.0714 0.0289 0.1046 319 LEU A CB 2465 C CG . LEU A 319 ? 0.8148 0.8729 1.1198 0.0481 0.0020 0.1276 319 LEU A CG 2466 C CD1 . LEU A 319 ? 0.7945 0.8039 1.0678 0.0362 -0.0257 0.1275 319 LEU A CD1 2467 C CD2 . LEU A 319 ? 1.0257 1.1018 1.3179 0.0249 0.0071 0.1366 319 LEU A CD2 2468 N N . GLN A 320 ? 0.9655 0.9257 1.1660 0.1005 0.0423 0.0476 320 GLN A N 2469 C CA . GLN A 320 ? 1.0036 0.9523 1.1990 0.1254 0.0597 0.0210 320 GLN A CA 2470 C C . GLN A 320 ? 1.0215 0.9959 1.2802 0.1529 0.0668 0.0202 320 GLN A C 2471 O O . GLN A 320 ? 1.0028 0.9741 1.3027 0.1547 0.0455 0.0374 320 GLN A O 2472 C CB . GLN A 320 ? 1.0233 0.9121 1.1835 0.1231 0.0433 0.0073 320 GLN A CB 2473 C CG . GLN A 320 ? 1.0639 0.9338 1.2179 0.1476 0.0584 -0.0236 320 GLN A CG 2474 C CD . GLN A 320 ? 1.1159 0.9249 1.2443 0.1442 0.0389 -0.0343 320 GLN A CD 2475 O OE1 . GLN A 320 ? 1.2126 0.9963 1.3263 0.1233 0.0153 -0.0172 320 GLN A OE1 2476 N NE2 . GLN A 320 ? 1.1353 0.9212 1.2584 0.1641 0.0490 -0.0634 320 GLN A NE2 2477 N N . ARG A 321 ? 0.9219 1.4438 1.2591 -0.0642 -0.1192 -0.2945 321 ARG A N 2478 C CA . ARG A 321 ? 1.0001 1.5786 1.3781 -0.0461 -0.1385 -0.3316 321 ARG A CA 2479 C C . ARG A 321 ? 1.0613 1.6720 1.4985 -0.0177 -0.1583 -0.3893 321 ARG A C 2480 O O . ARG A 321 ? 0.9625 1.5447 1.4074 -0.0135 -0.1573 -0.3972 321 ARG A O 2481 C CB . ARG A 321 ? 0.9632 1.6524 1.3336 -0.0500 -0.1260 -0.3293 321 ARG A CB 2482 C CG . ARG A 321 ? 0.9662 1.6553 1.3309 -0.0555 -0.1342 -0.3167 321 ARG A CG 2483 C CD . ARG A 321 ? 0.9776 1.5616 1.2966 -0.0796 -0.1278 -0.2642 321 ARG A CD 2484 N NE . ARG A 321 ? 1.0279 1.6075 1.3425 -0.0844 -0.1365 -0.2530 321 ARG A NE 2485 C CZ . ARG A 321 ? 1.1798 1.6813 1.4596 -0.1032 -0.1338 -0.2126 321 ARG A CZ 2486 N NH1 . ARG A 321 ? 1.2843 1.7087 1.5311 -0.1185 -0.1230 -0.1809 321 ARG A NH1 2487 N NH2 . ARG A 321 ? 1.2455 1.7497 1.5243 -0.1061 -0.1423 -0.2057 321 ARG A NH2 2488 N N . ALA A 322 ? 1.1474 1.8175 1.6289 0.0021 -0.1779 -0.4308 322 ALA A N 2489 C CA . ALA A 322 ? 1.1659 1.8764 1.7138 0.0322 -0.2014 -0.4933 322 ALA A CA 2490 C C . ALA A 322 ? 1.0983 1.8891 1.6559 0.0416 -0.1879 -0.5190 322 ALA A C 2491 O O . ALA A 322 ? 1.0192 1.7731 1.5990 0.0505 -0.1950 -0.5359 322 ALA A O 2492 C CB . ALA A 322 ? 1.2557 2.0407 1.8455 0.0513 -0.2208 -0.5347 322 ALA A CB 2493 N N . SER A 323 ? 1.1458 2.0504 1.6884 0.0387 -0.1693 -0.5201 323 SER A N 2494 C CA . SER A 323 ? 1.0885 2.0905 1.6402 0.0468 -0.1553 -0.5438 323 SER A CA 2495 C C . SER A 323 ? 1.1145 2.0508 1.6324 0.0315 -0.1369 -0.5110 323 SER A C 2496 O O . SER A 323 ? 1.0560 2.0383 1.5942 0.0436 -0.1334 -0.5397 323 SER A O 2497 C CB . SER A 323 ? 0.9865 2.1153 1.5177 0.0374 -0.1362 -0.5315 323 SER A CB 2498 O OG . SER A 323 ? 0.9692 2.0507 1.4408 0.0053 -0.1151 -0.4631 323 SER A OG 2499 N N . GLY A 324 ? 1.2660 2.0982 1.7337 0.0059 -0.1258 -0.4531 324 GLY A N 2500 C CA . GLY A 324 ? 1.3198 2.0884 1.7519 -0.0099 -0.1081 -0.4195 324 GLY A CA 2501 C C . GLY A 324 ? 1.2511 2.0489 1.6315 -0.0359 -0.0796 -0.3698 324 GLY A C 2502 O O . GLY A 324 ? 1.0871 1.8299 1.4330 -0.0520 -0.0636 -0.3360 324 GLY A O 2503 N N . ASP A 325 ? 1.2333 2.1194 1.6115 -0.0402 -0.0751 -0.3646 325 ASP A N 2504 C CA . ASP A 325 ? 1.0351 1.9545 1.3729 -0.0661 -0.0526 -0.3145 325 ASP A CA 2505 C C . ASP A 325 ? 0.9572 1.7764 1.2568 -0.0879 -0.0516 -0.2656 325 ASP A C 2506 O O . ASP A 325 ? 1.2040 2.0096 1.5097 -0.0857 -0.0647 -0.2679 325 ASP A O 2507 C CB . ASP A 325 ? 1.0947 2.1598 1.4497 -0.0633 -0.0498 -0.3258 325 ASP A CB 2508 C CG . ASP A 325 ? 1.2302 2.4109 1.6232 -0.0416 -0.0498 -0.3762 325 ASP A CG 2509 O OD1 . ASP A 325 ? 1.3244 2.4855 1.7163 -0.0389 -0.0418 -0.3826 325 ASP A OD1 2510 O OD2 . ASP A 325 ? 1.1740 2.4690 1.5985 -0.0268 -0.0582 -0.4108 325 ASP A OD2 2511 N N . PHE A 326 ? 0.9037 1.6559 1.1655 -0.1082 -0.0365 -0.2236 326 PHE A N 2512 C CA . PHE A 326 ? 0.8898 1.5438 1.1166 -0.1276 -0.0360 -0.1810 326 PHE A CA 2513 C C . PHE A 326 ? 0.8492 1.5484 1.0635 -0.1445 -0.0322 -0.1489 326 PHE A C 2514 O O . PHE A 326 ? 0.8831 1.6752 1.1006 -0.1525 -0.0218 -0.1365 326 PHE A O 2515 C CB . PHE A 326 ? 0.8754 1.4541 1.0691 -0.1429 -0.0219 -0.1498 326 PHE A CB 2516 C CG . PHE A 326 ? 0.8877 1.4011 1.0885 -0.1303 -0.0273 -0.1722 326 PHE A CG 2517 C CD1 . PHE A 326 ? 0.9253 1.3346 1.1152 -0.1318 -0.0383 -0.1644 326 PHE A CD1 2518 C CD2 . PHE A 326 ? 0.9000 1.4601 1.1198 -0.1178 -0.0222 -0.1994 326 PHE A CD2 2519 C CE1 . PHE A 326 ? 0.9432 1.2960 1.1427 -0.1223 -0.0453 -0.1802 326 PHE A CE1 2520 C CE2 . PHE A 326 ? 0.9189 1.4182 1.1485 -0.1070 -0.0290 -0.2181 326 PHE A CE2 2521 C CZ . PHE A 326 ? 0.9309 1.3262 1.1510 -0.1099 -0.0411 -0.2069 326 PHE A CZ 2522 N N . GLN A 327 ? 0.8770 1.5132 1.0796 -0.1505 -0.0419 -0.1339 327 GLN A N 2523 C CA . GLN A 327 ? 0.8986 1.5534 1.0858 -0.1696 -0.0393 -0.0967 327 GLN A CA 2524 C C . GLN A 327 ? 0.8787 1.4339 1.0304 -0.1897 -0.0328 -0.0558 327 GLN A C 2525 O O . GLN A 327 ? 0.8776 1.3411 1.0160 -0.1890 -0.0404 -0.0547 327 GLN A O 2526 C CB . GLN A 327 ? 1.0588 1.7213 1.2595 -0.1618 -0.0552 -0.1104 327 GLN A CB 2527 C CG . GLN A 327 ? 1.2407 1.9886 1.4811 -0.1370 -0.0659 -0.1608 327 GLN A CG 2528 C CD . GLN A 327 ? 1.2690 2.1531 1.5258 -0.1366 -0.0568 -0.1666 327 GLN A CD 2529 O OE1 . GLN A 327 ? 1.2937 2.2225 1.5367 -0.1569 -0.0474 -0.1276 327 GLN A OE1 2530 N NE2 . GLN A 327 ? 1.1848 2.1398 1.4747 -0.1137 -0.0611 -0.2151 327 GLN A NE2 2531 N N . THR A 328 ? 0.9122 1.4904 1.0518 -0.2077 -0.0202 -0.0228 328 THR A N 2532 C CA . THR A 328 ? 0.7895 1.2796 0.9004 -0.2240 -0.0140 0.0091 328 THR A CA 2533 C C . THR A 328 ? 0.7688 1.2458 0.8700 -0.2445 -0.0170 0.0482 328 THR A C 2534 O O . THR A 328 ? 0.7726 1.3280 0.8881 -0.2548 -0.0166 0.0674 328 THR A O 2535 C CB . THR A 328 ? 0.7451 1.2530 0.8517 -0.2296 0.0007 0.0179 328 THR A CB 2536 O OG1 . THR A 328 ? 0.7511 1.2651 0.8678 -0.2103 0.0025 -0.0192 328 THR A OG1 2537 C CG2 . THR A 328 ? 0.7556 1.1730 0.8348 -0.2446 0.0057 0.0465 328 THR A CG2 2538 N N . THR A 329 ? 0.7917 1.1731 0.8716 -0.2504 -0.0215 0.0599 329 THR A N 2539 C CA . THR A 329 ? 0.7946 1.1495 0.8666 -0.2689 -0.0261 0.0940 329 THR A CA 2540 C C . THR A 329 ? 0.9662 1.2447 1.0175 -0.2796 -0.0210 0.1118 329 THR A C 2541 O O . THR A 329 ? 1.1408 1.3658 1.1765 -0.2715 -0.0165 0.0962 329 THR A O 2542 C CB . THR A 329 ? 0.8399 1.1587 0.9082 -0.2656 -0.0390 0.0888 329 THR A CB 2543 O OG1 . THR A 329 ? 1.2279 1.5016 1.2862 -0.2822 -0.0438 0.1183 329 THR A OG1 2544 C CG2 . THR A 329 ? 0.8763 1.1267 0.9326 -0.2510 -0.0426 0.0624 329 THR A CG2 2545 N N . LYS A 330 ? 0.8529 1.1291 0.9074 -0.2977 -0.0234 0.1442 330 LYS A N 2546 C CA . LYS A 330 ? 0.7611 0.9708 0.8013 -0.3073 -0.0209 0.1588 330 LYS A CA 2547 C C . LYS A 330 ? 0.8288 0.9803 0.8626 -0.3159 -0.0328 0.1717 330 LYS A C 2548 O O . LYS A 330 ? 1.0153 1.1931 1.0636 -0.3226 -0.0428 0.1850 330 LYS A O 2549 C CB . LYS A 330 ? 0.6810 0.9350 0.7375 -0.3213 -0.0154 0.1846 330 LYS A CB 2550 C CG . LYS A 330 ? 0.7178 1.0307 0.7795 -0.3139 -0.0024 0.1726 330 LYS A CG 2551 C CD . LYS A 330 ? 0.7800 1.1279 0.8567 -0.3300 0.0023 0.2022 330 LYS A CD 2552 C CE . LYS A 330 ? 0.8186 1.2351 0.9016 -0.3232 0.0157 0.1910 330 LYS A CE 2553 N NZ . LYS A 330 ? 0.9075 1.4251 1.0102 -0.3176 0.0147 0.1827 330 LYS A NZ 2554 N N . LEU A 331 ? 0.7926 0.8695 0.8057 -0.3155 -0.0321 0.1667 331 LEU A N 2555 C CA . LEU A 331 ? 0.8534 0.8790 0.8627 -0.3236 -0.0433 0.1766 331 LEU A CA 2556 C C . LEU A 331 ? 0.9293 0.9166 0.9360 -0.3317 -0.0419 0.1858 331 LEU A C 2557 O O . LEU A 331 ? 0.9647 0.9427 0.9598 -0.3276 -0.0306 0.1781 331 LEU A O 2558 C CB . LEU A 331 ? 0.7448 0.7203 0.7319 -0.3136 -0.0476 0.1571 331 LEU A CB 2559 C CG . LEU A 331 ? 0.8971 0.8279 0.8589 -0.3038 -0.0401 0.1383 331 LEU A CG 2560 C CD1 . LEU A 331 ? 0.7655 0.6397 0.7084 -0.3035 -0.0478 0.1329 331 LEU A CD1 2561 C CD2 . LEU A 331 ? 1.1574 1.1135 1.1207 -0.2904 -0.0360 0.1199 331 LEU A CD2 2562 N N . ASN A 332 ? 0.9224 0.8879 0.9427 -0.3425 -0.0547 0.2005 332 ASN A N 2563 C CA . ASN A 332 ? 0.9129 0.8505 0.9422 -0.3509 -0.0576 0.2098 332 ASN A CA 2564 C C . ASN A 332 ? 1.0494 0.9225 1.0635 -0.3479 -0.0653 0.1949 332 ASN A C 2565 O O . ASN A 332 ? 1.2189 1.0734 1.2223 -0.3435 -0.0718 0.1851 332 ASN A O 2566 C CB . ASN A 332 ? 0.7385 0.7123 0.8093 -0.3673 -0.0704 0.2410 332 ASN A CB 2567 C CG . ASN A 332 ? 0.7181 0.7673 0.8059 -0.3725 -0.0625 0.2589 332 ASN A CG 2568 O OD1 . ASN A 332 ? 0.7147 0.7887 0.7841 -0.3620 -0.0473 0.2437 332 ASN A OD1 2569 N ND2 . ASN A 332 ? 0.7131 0.8033 0.8383 -0.3855 -0.0741 0.2892 332 ASN A ND2 2570 N N . GLY A 333 ? 0.7686 0.6125 0.7825 -0.3500 -0.0647 0.1922 333 GLY A N 2571 C CA . GLY A 333 ? 0.9846 0.7779 0.9879 -0.3470 -0.0728 0.1756 333 GLY A CA 2572 C C . GLY A 333 ? 1.0859 0.8714 1.1207 -0.3550 -0.0940 0.1838 333 GLY A C 2573 O O . GLY A 333 ? 1.1647 0.9822 1.2275 -0.3637 -0.1026 0.2052 333 GLY A O 2574 N N . PHE A 334 ? 1.1072 0.8539 1.1394 -0.3519 -0.1037 0.1661 334 PHE A N 2575 C CA . PHE A 334 ? 0.9739 0.7089 1.0369 -0.3570 -0.1259 0.1673 334 PHE A CA 2576 C C . PHE A 334 ? 0.9761 0.6906 1.0688 -0.3574 -0.1391 0.1601 334 PHE A C 2577 O O . PHE A 334 ? 1.1793 0.9101 1.3156 -0.3580 -0.1515 0.1747 334 PHE A O 2578 C CB . PHE A 334 ? 1.0550 0.7708 1.0916 -0.3484 -0.1284 0.1462 334 PHE A CB 2579 C CG . PHE A 334 ? 1.0128 0.7444 1.0178 -0.3430 -0.1143 0.1472 334 PHE A CG 2580 C CD1 . PHE A 334 ? 0.8345 0.5562 0.8007 -0.3340 -0.0990 0.1324 334 PHE A CD1 2581 C CD2 . PHE A 334 ? 0.9433 0.7017 0.9615 -0.3472 -0.1184 0.1631 334 PHE A CD2 2582 C CE1 . PHE A 334 ? 0.8287 0.5628 0.7741 -0.3287 -0.0899 0.1327 334 PHE A CE1 2583 C CE2 . PHE A 334 ? 0.8634 0.6368 0.8576 -0.3408 -0.1078 0.1606 334 PHE A CE2 2584 C CZ . PHE A 334 ? 0.8225 0.5819 0.7826 -0.3314 -0.0945 0.1449 334 PHE A CZ 2585 N N . GLU A 335 ? 0.8912 0.5775 0.9599 -0.3508 -0.1351 0.1343 335 GLU A N 2586 C CA . GLU A 335 ? 0.9678 0.6360 1.0636 -0.3498 -0.1471 0.1222 335 GLU A CA 2587 C C . GLU A 335 ? 0.8745 0.5588 0.9762 -0.3477 -0.1334 0.1348 335 GLU A C 2588 O O . GLU A 335 ? 0.8296 0.5248 0.8984 -0.3478 -0.1130 0.1409 335 GLU A O 2589 C CB . GLU A 335 ? 0.9937 0.6391 1.0596 -0.3387 -0.1460 0.0861 335 GLU A CB 2590 C CG . GLU A 335 ? 1.1341 0.7740 1.1961 -0.3337 -0.1580 0.0682 335 GLU A CG 2591 C CD . GLU A 335 ? 1.2978 0.9289 1.3352 -0.3224 -0.1583 0.0321 335 GLU A CD 2592 O OE1 . GLU A 335 ? 1.4016 1.0302 1.4514 -0.3182 -0.1747 0.0116 335 GLU A OE1 2593 O OE2 . GLU A 335 ? 1.3055 0.9368 1.3116 -0.3178 -0.1425 0.0240 335 GLU A OE2 2594 N N . VAL A 336 ? 0.8483 0.5352 0.9936 -0.3454 -0.1458 0.1381 336 VAL A N 2595 C CA . VAL A 336 ? 0.8441 0.5464 0.9975 -0.3437 -0.1349 0.1499 336 VAL A CA 2596 C C . VAL A 336 ? 0.9593 0.6364 1.0833 -0.3396 -0.1245 0.1261 336 VAL A C 2597 O O . VAL A 336 ? 1.0820 0.7304 1.1978 -0.3377 -0.1346 0.0986 336 VAL A O 2598 C CB . VAL A 336 ? 0.8390 0.5517 1.0490 -0.3432 -0.1539 0.1627 336 VAL A CB 2599 C CG1 . VAL A 336 ? 1.0394 0.7865 1.2757 -0.3489 -0.1626 0.1934 336 VAL A CG1 2600 C CG2 . VAL A 336 ? 1.1626 0.8434 1.3997 -0.3384 -0.1769 0.1359 336 VAL A CG2 2601 N N . PHE A 337 ? 1.0508 0.7426 1.1577 -0.3383 -0.1048 0.1358 337 PHE A N 2602 C CA . PHE A 337 ? 0.9994 0.6719 1.0767 -0.3346 -0.0928 0.1175 337 PHE A CA 2603 C C . PHE A 337 ? 1.0533 0.7059 1.0757 -0.3355 -0.0833 0.0998 337 PHE A C 2604 O O . PHE A 337 ? 1.3731 1.0131 1.3632 -0.3320 -0.0720 0.0847 337 PHE A O 2605 C CB . PHE A 337 ? 1.0043 0.6553 1.1121 -0.3315 -0.1098 0.0980 337 PHE A CB 2606 C CG . PHE A 337 ? 0.9935 0.6622 1.1479 -0.3303 -0.1160 0.1155 337 PHE A CG 2607 C CD1 . PHE A 337 ? 0.9787 0.6784 1.1306 -0.3314 -0.0996 0.1412 337 PHE A CD1 2608 C CD2 . PHE A 337 ? 0.8469 0.5039 1.0479 -0.3275 -0.1401 0.1053 337 PHE A CD2 2609 C CE1 . PHE A 337 ? 0.8075 0.5263 0.9989 -0.3317 -0.1070 0.1591 337 PHE A CE1 2610 C CE2 . PHE A 337 ? 0.8454 0.5187 1.0880 -0.3272 -0.1483 0.1243 337 PHE A CE2 2611 C CZ . PHE A 337 ? 0.8259 0.5303 1.0622 -0.3303 -0.1318 0.1526 337 PHE A CZ 2612 N N . ALA A 338 ? 0.8329 0.4874 0.8449 -0.3379 -0.0871 0.1018 338 ALA A N 2613 C CA . ALA A 338 ? 0.8382 0.4882 0.8031 -0.3286 -0.0762 0.0847 338 ALA A CA 2614 C C . ALA A 338 ? 1.1087 0.7686 1.0375 -0.3258 -0.0531 0.0920 338 ALA A C 2615 O O . ALA A 338 ? 1.0570 0.7110 0.9486 -0.3188 -0.0441 0.0789 338 ALA A O 2616 C CB . ALA A 338 ? 0.8434 0.4987 0.8114 -0.3292 -0.0852 0.0878 338 ALA A CB 2617 N N . ARG A 339 ? 1.2253 0.9046 1.1690 -0.3318 -0.0454 0.1134 339 ARG A N 2618 C CA . ARG A 339 ? 1.0752 0.7683 0.9927 -0.3285 -0.0254 0.1186 339 ARG A CA 2619 C C . ARG A 339 ? 0.9642 0.6619 0.8574 -0.3226 -0.0210 0.1146 339 ARG A C 2620 O O . ARG A 339 ? 1.0000 0.6848 0.8616 -0.3158 -0.0140 0.1024 339 ARG A O 2621 C CB . ARG A 339 ? 0.8068 0.4839 0.6999 -0.3237 -0.0144 0.1057 339 ARG A CB 2622 C CG . ARG A 339 ? 0.7886 0.4685 0.7100 -0.3238 -0.0169 0.1088 339 ARG A CG 2623 C CD . ARG A 339 ? 0.7911 0.4552 0.6864 -0.3193 -0.0064 0.0948 339 ARG A CD 2624 N NE . ARG A 339 ? 0.7830 0.4535 0.7084 -0.3171 -0.0081 0.0984 339 ARG A NE 2625 C CZ . ARG A 339 ? 0.9578 0.6170 0.8690 -0.3135 -0.0011 0.0872 339 ARG A CZ 2626 N NH1 . ARG A 339 ? 0.8825 0.5257 0.7485 -0.3123 0.0084 0.0727 339 ARG A NH1 2627 N NH2 . ARG A 339 ? 1.1111 0.7768 1.0546 -0.3117 -0.0041 0.0919 339 ARG A NH2 2628 N N . PHE A 340 ? 0.8114 0.5299 0.7230 -0.3260 -0.0270 0.1268 340 PHE A N 2629 C CA . PHE A 340 ? 0.7913 0.5141 0.6887 -0.3210 -0.0275 0.1231 340 PHE A CA 2630 C C . PHE A 340 ? 1.0445 0.7756 0.9202 -0.3136 -0.0138 0.1191 340 PHE A C 2631 O O . PHE A 340 ? 1.2423 0.9614 1.0987 -0.3079 -0.0147 0.1106 340 PHE A O 2632 C CB . PHE A 340 ? 0.8482 0.5979 0.7738 -0.3268 -0.0366 0.1381 340 PHE A CB 2633 C CG . PHE A 340 ? 0.7873 0.5446 0.7027 -0.3215 -0.0381 0.1344 340 PHE A CG 2634 C CD1 . PHE A 340 ? 0.8551 0.5864 0.7516 -0.3173 -0.0443 0.1221 340 PHE A CD1 2635 C CD2 . PHE A 340 ? 0.8035 0.5991 0.7304 -0.3207 -0.0343 0.1428 340 PHE A CD2 2636 C CE1 . PHE A 340 ? 0.9243 0.6618 0.8145 -0.3131 -0.0471 0.1202 340 PHE A CE1 2637 C CE2 . PHE A 340 ? 1.0075 0.8100 0.9287 -0.3150 -0.0374 0.1373 340 PHE A CE2 2638 C CZ . PHE A 340 ? 0.9788 0.7493 0.8822 -0.3116 -0.0441 0.1271 340 PHE A CZ 2639 N N . GLY A 341 ? 0.8580 0.6118 0.7408 -0.3138 -0.0029 0.1255 341 GLY A N 2640 C CA . GLY A 341 ? 0.8184 0.5845 0.6894 -0.3058 0.0076 0.1195 341 GLY A CA 2641 C C . GLY A 341 ? 0.9760 0.7175 0.8221 -0.3013 0.0166 0.1103 341 GLY A C 2642 O O . GLY A 341 ? 1.2579 1.0105 1.1004 -0.2957 0.0256 0.1066 341 GLY A O 2643 N N . SER A 342 ? 0.7761 0.4879 0.6069 -0.3034 0.0131 0.1054 342 SER A N 2644 C CA . SER A 342 ? 1.0054 0.6983 0.8124 -0.3006 0.0210 0.0984 342 SER A CA 2645 C C . SER A 342 ? 1.0500 0.7366 0.8398 -0.2944 0.0228 0.0944 342 SER A C 2646 O O . SER A 342 ? 1.4284 1.1147 1.2105 -0.2911 0.0318 0.0932 342 SER A O 2647 C CB . SER A 342 ? 1.0934 0.7652 0.8894 -0.3031 0.0144 0.0907 342 SER A CB 2648 O OG . SER A 342 ? 1.0978 0.7718 0.9173 -0.3086 0.0091 0.0934 342 SER A OG 2649 N N . ALA A 343 ? 0.8987 0.5801 0.6855 -0.2933 0.0126 0.0937 343 ALA A N 2650 C CA . ALA A 343 ? 0.8019 0.4768 0.5796 -0.2889 0.0098 0.0934 343 ALA A CA 2651 C C . ALA A 343 ? 0.9894 0.6736 0.7833 -0.2859 0.0000 0.0943 343 ALA A C 2652 O O . ALA A 343 ? 1.0079 0.6912 0.8037 -0.2889 -0.0085 0.0955 343 ALA A O 2653 C CB . ALA A 343 ? 0.8190 0.4781 0.5720 -0.2918 0.0056 0.0935 343 ALA A CB 2654 N N . ILE A 344 ? 0.8719 0.5660 0.6798 -0.2793 0.0001 0.0916 344 ILE A N 2655 C CA . ILE A 344 ? 0.7968 0.5013 0.6237 -0.2747 -0.0105 0.0892 344 ILE A CA 2656 C C . ILE A 344 ? 0.8083 0.4975 0.6370 -0.2712 -0.0205 0.0903 344 ILE A C 2657 O O . ILE A 344 ? 1.3743 1.0640 1.2126 -0.2657 -0.0191 0.0860 344 ILE A O 2658 C CB . ILE A 344 ? 0.8048 0.5437 0.6571 -0.2682 -0.0063 0.0816 344 ILE A CB 2659 C CG1 . ILE A 344 ? 0.7673 0.5265 0.6221 -0.2743 0.0022 0.0868 344 ILE A CG1 2660 C CG2 . ILE A 344 ? 0.7807 0.5342 0.6537 -0.2627 -0.0183 0.0763 344 ILE A CG2 2661 C CD1 . ILE A 344 ? 0.7991 0.6054 0.6785 -0.2699 0.0067 0.0825 344 ILE A CD1 2662 N N . ALA A 345 ? 0.8235 0.5007 0.6464 -0.2750 -0.0322 0.0972 345 ALA A N 2663 C CA . ALA A 345 ? 1.2938 0.9580 1.1218 -0.2748 -0.0449 0.1043 345 ALA A CA 2664 C C . ALA A 345 ? 1.0910 0.7589 0.9431 -0.2710 -0.0604 0.1034 345 ALA A C 2665 O O . ALA A 345 ? 0.9982 0.6676 0.8446 -0.2749 -0.0651 0.1068 345 ALA A O 2666 C CB . ALA A 345 ? 1.3155 0.9684 1.1160 -0.2843 -0.0468 0.1169 345 ALA A CB 2667 N N . PRO A 346 ? 0.8404 0.5105 0.7226 -0.2626 -0.0697 0.0969 346 PRO A N 2668 C CA . PRO A 346 ? 0.8487 0.5192 0.7576 -0.2590 -0.0882 0.0964 346 PRO A CA 2669 C C . PRO A 346 ? 1.0707 0.7237 0.9703 -0.2690 -0.1014 0.1174 346 PRO A C 2670 O O . PRO A 346 ? 1.0499 0.6916 0.9451 -0.2740 -0.1051 0.1302 346 PRO A O 2671 C CB . PRO A 346 ? 0.8796 0.5548 0.8265 -0.2473 -0.0972 0.0827 346 PRO A CB 2672 C CG . PRO A 346 ? 0.8912 0.5777 0.8295 -0.2436 -0.0794 0.0725 346 PRO A CG 2673 C CD . PRO A 346 ? 0.9376 0.6107 0.8346 -0.2554 -0.0657 0.0877 346 PRO A CD 2674 N N . LEU A 347 ? 1.0487 0.7037 0.9457 -0.2727 -0.1087 0.1224 347 LEU A N 2675 C CA . LEU A 347 ? 1.0392 0.6865 0.9293 -0.2829 -0.1219 0.1434 347 LEU A CA 2676 C C . LEU A 347 ? 0.9060 0.5483 0.8351 -0.2800 -0.1451 0.1487 347 LEU A C 2677 O O . LEU A 347 ? 0.9202 0.5598 0.8504 -0.2892 -0.1592 0.1691 347 LEU A O 2678 C CB . LEU A 347 ? 0.8979 0.5523 0.7596 -0.2899 -0.1161 0.1462 347 LEU A CB 2679 C CG . LEU A 347 ? 0.9822 0.6453 0.8490 -0.2842 -0.1115 0.1314 347 LEU A CG 2680 C CD1 . LEU A 347 ? 1.3363 1.0005 1.2264 -0.2824 -0.1283 0.1342 347 LEU A CD1 2681 C CD2 . LEU A 347 ? 0.8874 0.5552 0.7250 -0.2902 -0.1008 0.1299 347 LEU A CD2 2682 N N . GLY A 348 ? 0.8955 0.5411 0.8592 -0.2670 -0.1503 0.1296 348 GLY A N 2683 C CA . GLY A 348 ? 0.9044 0.5464 0.9124 -0.2615 -0.1742 0.1284 348 GLY A CA 2684 C C . GLY A 348 ? 1.0144 0.6666 1.0233 -0.2597 -0.1768 0.1223 348 GLY A C 2685 O O . GLY A 348 ? 1.1519 0.8190 1.1410 -0.2570 -0.1605 0.1096 348 GLY A O 2686 N N . ASP A 349 ? 0.9694 0.6147 1.0038 -0.2619 -0.1987 0.1331 349 ASP A N 2687 C CA . ASP A 349 ? 1.1748 0.8284 1.2069 -0.2620 -0.2017 0.1307 349 ASP A CA 2688 C C . ASP A 349 ? 1.1824 0.8318 1.1830 -0.2779 -0.2018 0.1570 349 ASP A C 2689 O O . ASP A 349 ? 1.2379 0.8801 1.2523 -0.2865 -0.2196 0.1798 349 ASP A O 2690 C CB . ASP A 349 ? 1.2559 0.9091 1.3399 -0.2525 -0.2263 0.1216 349 ASP A CB 2691 C CG . ASP A 349 ? 1.2157 0.8807 1.2981 -0.2504 -0.2277 0.1149 349 ASP A CG 2692 O OD1 . ASP A 349 ? 1.2934 0.9692 1.3386 -0.2541 -0.2087 0.1131 349 ASP A OD1 2693 O OD2 . ASP A 349 ? 1.0609 0.7245 1.1826 -0.2449 -0.2493 0.1112 349 ASP A OD2 2694 N N . LEU A 350 ? 1.0832 0.7412 1.0452 -0.2818 -0.1835 0.1538 350 LEU A N 2695 C CA . LEU A 350 ? 1.0117 0.6728 0.9407 -0.2952 -0.1807 0.1724 350 LEU A CA 2696 C C . LEU A 350 ? 1.0940 0.7592 1.0304 -0.2998 -0.1947 0.1825 350 LEU A C 2697 O O . LEU A 350 ? 1.2994 0.9690 1.2314 -0.3110 -0.2053 0.2053 350 LEU A O 2698 C CB . LEU A 350 ? 0.9940 0.6622 0.8866 -0.2963 -0.1593 0.1613 350 LEU A CB 2699 C CG . LEU A 350 ? 0.9359 0.6123 0.7938 -0.3076 -0.1541 0.1726 350 LEU A CG 2700 C CD1 . LEU A 350 ? 0.9471 0.6258 0.8021 -0.3157 -0.1608 0.1926 350 LEU A CD1 2701 C CD2 . LEU A 350 ? 0.9253 0.6045 0.7586 -0.3060 -0.1356 0.1574 350 LEU A CD2 2702 N N . ASP A 351 ? 1.1057 0.7742 1.0536 -0.2918 -0.1947 0.1667 351 ASP A N 2703 C CA . ASP A 351 ? 1.1904 0.8629 1.1431 -0.2953 -0.2060 0.1740 351 ASP A CA 2704 C C . ASP A 351 ? 1.3072 0.9733 1.3055 -0.2903 -0.2290 0.1768 351 ASP A C 2705 O O . ASP A 351 ? 1.5543 1.2230 1.5630 -0.2919 -0.2404 0.1818 351 ASP A O 2706 C CB . ASP A 351 ? 1.1293 0.8110 1.0687 -0.2908 -0.1945 0.1574 351 ASP A CB 2707 C CG . ASP A 351 ? 1.0542 0.7431 1.0137 -0.2777 -0.1893 0.1353 351 ASP A CG 2708 O OD1 . ASP A 351 ? 1.0619 0.7634 1.0240 -0.2737 -0.1870 0.1251 351 ASP A OD1 2709 O OD2 . ASP A 351 ? 0.9894 0.6761 0.9630 -0.2718 -0.1879 0.1284 351 ASP A OD2 2710 N N . GLN A 352 ? 1.1002 0.7581 1.1287 -0.2837 -0.2370 0.1722 352 GLN A N 2711 C CA . GLN A 352 ? 1.0729 0.7236 1.1548 -0.2763 -0.2621 0.1697 352 GLN A CA 2712 C C . GLN A 352 ? 1.1118 0.7735 1.2120 -0.2637 -0.2645 0.1454 352 GLN A C 2713 O O . GLN A 352 ? 1.1203 0.7792 1.2552 -0.2611 -0.2857 0.1471 352 GLN A O 2714 C CB . GLN A 352 ? 1.1002 0.7441 1.1978 -0.2898 -0.2844 0.2023 352 GLN A CB 2715 C CG . GLN A 352 ? 1.3203 0.9603 1.4124 -0.3022 -0.2882 0.2290 352 GLN A CG 2716 C CD . GLN A 352 ? 1.3747 1.0012 1.5072 -0.2938 -0.2996 0.2213 352 GLN A CD 2717 O OE1 . GLN A 352 ? 1.4501 1.0686 1.6335 -0.2819 -0.3188 0.2061 352 GLN A OE1 2718 N NE2 . GLN A 352 ? 1.3082 0.9337 1.4201 -0.2990 -0.2887 0.2295 352 GLN A NE2 2719 N N . ASP A 353 ? 1.1808 0.8584 1.2596 -0.2566 -0.2438 0.1242 353 ASP A N 2720 C CA . ASP A 353 ? 1.1687 0.8665 1.2609 -0.2456 -0.2437 0.1021 353 ASP A CA 2721 C C . ASP A 353 ? 1.2411 0.9511 1.3831 -0.2283 -0.2572 0.0755 353 ASP A C 2722 O O . ASP A 353 ? 1.4649 1.1984 1.6268 -0.2173 -0.2614 0.0544 353 ASP A O 2723 C CB . ASP A 353 ? 1.1008 0.8175 1.1568 -0.2463 -0.2190 0.0934 353 ASP A CB 2724 C CG . ASP A 353 ? 1.1799 0.8987 1.2215 -0.2453 -0.2028 0.0884 353 ASP A CG 2725 O OD1 . ASP A 353 ? 1.4751 1.1873 1.5400 -0.2396 -0.2098 0.0831 353 ASP A OD1 2726 O OD2 . ASP A 353 ? 1.0736 0.8002 1.0836 -0.2505 -0.1843 0.0899 353 ASP A OD2 2727 N N . GLY A 354 ? 1.0940 0.7915 1.2579 -0.2255 -0.2648 0.0749 354 GLY A N 2728 C CA . GLY A 354 ? 1.0893 0.7997 1.3043 -0.2077 -0.2788 0.0457 354 GLY A CA 2729 C C . GLY A 354 ? 1.0926 0.8260 1.2954 -0.1997 -0.2585 0.0252 354 GLY A C 2730 O O . GLY A 354 ? 1.1282 0.8733 1.3693 -0.1857 -0.2673 0.0011 354 GLY A O 2731 N N . PHE A 355 ? 1.0880 0.8295 1.2405 -0.2086 -0.2326 0.0343 355 PHE A N 2732 C CA . PHE A 355 ? 0.9839 0.7482 1.1215 -0.2041 -0.2121 0.0207 355 PHE A CA 2733 C C . PHE A 355 ? 1.0040 0.7431 1.1013 -0.2179 -0.1966 0.0436 355 PHE A C 2734 O O . PHE A 355 ? 1.0349 0.7568 1.0984 -0.2315 -0.1908 0.0660 355 PHE A O 2735 C CB . PHE A 355 ? 0.9452 0.7501 1.0668 -0.2017 -0.1967 0.0095 355 PHE A CB 2736 C CG . PHE A 355 ? 0.9568 0.7939 1.1135 -0.1888 -0.2107 -0.0129 355 PHE A CG 2737 C CD1 . PHE A 355 ? 0.9779 0.8527 1.1755 -0.1707 -0.2182 -0.0460 355 PHE A CD1 2738 C CD2 . PHE A 355 ? 0.9809 0.8148 1.1308 -0.1939 -0.2167 -0.0033 355 PHE A CD2 2739 C CE1 . PHE A 355 ? 0.9990 0.9097 1.2306 -0.1575 -0.2320 -0.0703 355 PHE A CE1 2740 C CE2 . PHE A 355 ? 1.1197 0.9853 1.3017 -0.1817 -0.2297 -0.0248 355 PHE A CE2 2741 C CZ . PHE A 355 ? 1.0898 0.9950 1.3129 -0.1632 -0.2375 -0.0589 355 PHE A CZ 2742 N N . ASN A 356 ? 1.0085 0.7489 1.1110 -0.2134 -0.1904 0.0355 356 ASN A N 2743 C CA . ASN A 356 ? 0.9455 0.6652 1.0125 -0.2248 -0.1760 0.0542 356 ASN A CA 2744 C C . ASN A 356 ? 0.9101 0.6407 0.9341 -0.2330 -0.1531 0.0603 356 ASN A C 2745 O O . ASN A 356 ? 0.9966 0.7580 1.0221 -0.2283 -0.1455 0.0478 356 ASN A O 2746 C CB . ASN A 356 ? 0.9577 0.6799 1.0418 -0.2169 -0.1739 0.0415 356 ASN A CB 2747 C CG . ASN A 356 ? 1.1520 0.8564 1.2826 -0.2107 -0.1999 0.0391 356 ASN A CG 2748 O OD1 . ASN A 356 ? 1.2394 0.9147 1.3670 -0.2207 -0.2082 0.0623 356 ASN A OD1 2749 N ND2 . ASN A 356 ? 1.3630 1.0888 1.5406 -0.1943 -0.2147 0.0109 356 ASN A ND2 2750 N N . ASP A 357 ? 0.8980 0.6069 0.8876 -0.2454 -0.1443 0.0798 357 ASP A N 2751 C CA . ASP A 357 ? 0.8989 0.6133 0.8534 -0.2534 -0.1265 0.0853 357 ASP A CA 2752 C C . ASP A 357 ? 0.8836 0.5889 0.8167 -0.2575 -0.1125 0.0894 357 ASP A C 2753 O O . ASP A 357 ? 0.9164 0.6081 0.8562 -0.2566 -0.1171 0.0927 357 ASP A O 2754 C CB . ASP A 357 ? 0.9235 0.6250 0.8576 -0.2637 -0.1312 0.1007 357 ASP A CB 2755 C CG . ASP A 357 ? 1.0254 0.7268 0.9829 -0.2609 -0.1494 0.1014 357 ASP A CG 2756 O OD1 . ASP A 357 ? 1.2292 0.9502 1.2003 -0.2549 -0.1508 0.0900 357 ASP A OD1 2757 O OD2 . ASP A 357 ? 0.9782 0.6629 0.9421 -0.2654 -0.1633 0.1150 357 ASP A OD2 2758 N N . ILE A 358 ? 0.8723 0.5853 0.7831 -0.2623 -0.0972 0.0901 358 ILE A N 2759 C CA . ILE A 358 ? 0.8448 0.5528 0.7386 -0.2649 -0.0834 0.0912 358 ILE A CA 2760 C C . ILE A 358 ? 0.9309 0.6311 0.7957 -0.2747 -0.0747 0.0991 358 ILE A C 2761 O O . ILE A 358 ? 0.9365 0.6415 0.7986 -0.2782 -0.0771 0.1008 358 ILE A O 2762 C CB . ILE A 358 ? 0.8333 0.5689 0.7432 -0.2569 -0.0735 0.0776 358 ILE A CB 2763 C CG1 . ILE A 358 ? 0.9120 0.6395 0.8124 -0.2569 -0.0630 0.0772 358 ILE A CG1 2764 C CG2 . ILE A 358 ? 0.8279 0.5880 0.7353 -0.2604 -0.0655 0.0780 358 ILE A CG2 2765 C CD1 . ILE A 358 ? 1.0265 0.7854 0.9463 -0.2480 -0.0551 0.0627 358 ILE A CD1 2766 N N . ALA A 359 ? 0.8440 0.5329 0.6900 -0.2784 -0.0661 0.1022 359 ALA A N 2767 C CA . ALA A 359 ? 0.8479 0.5308 0.6710 -0.2858 -0.0598 0.1049 359 ALA A CA 2768 C C . ALA A 359 ? 1.1395 0.8274 0.9596 -0.2858 -0.0461 0.1007 359 ALA A C 2769 O O . ALA A 359 ? 1.1565 0.8441 0.9775 -0.2824 -0.0393 0.0988 359 ALA A O 2770 C CB . ALA A 359 ? 0.8639 0.5342 0.6656 -0.2913 -0.0639 0.1123 359 ALA A CB 2771 N N . ILE A 360 ? 1.0731 0.7656 0.8930 -0.2901 -0.0436 0.1000 360 ILE A N 2772 C CA . ILE A 360 ? 0.9036 0.6010 0.7250 -0.2920 -0.0333 0.0991 360 ILE A CA 2773 C C . ILE A 360 ? 0.9423 0.6263 0.7508 -0.2975 -0.0348 0.0968 360 ILE A C 2774 O O . ILE A 360 ? 0.9219 0.6032 0.7312 -0.3002 -0.0442 0.0954 360 ILE A O 2775 C CB . ILE A 360 ? 0.8065 0.5302 0.6521 -0.2925 -0.0319 0.1021 360 ILE A CB 2776 C CG1 . ILE A 360 ? 0.7974 0.5431 0.6585 -0.2850 -0.0324 0.0986 360 ILE A CG1 2777 C CG2 . ILE A 360 ? 0.8257 0.5581 0.6765 -0.2959 -0.0222 0.1051 360 ILE A CG2 2778 C CD1 . ILE A 360 ? 0.7824 0.5673 0.6670 -0.2854 -0.0312 0.1016 360 ILE A CD1 2779 N N . ALA A 361 ? 0.8292 0.5068 0.6279 -0.2983 -0.0265 0.0940 361 ALA A N 2780 C CA . ALA A 361 ? 0.8404 0.5080 0.6278 -0.3013 -0.0293 0.0865 361 ALA A CA 2781 C C . ALA A 361 ? 1.0182 0.6858 0.8203 -0.3041 -0.0263 0.0847 361 ALA A C 2782 O O . ALA A 361 ? 1.0649 0.7387 0.8741 -0.3041 -0.0169 0.0901 361 ALA A O 2783 C CB . ALA A 361 ? 1.0958 0.7575 0.8568 -0.3002 -0.0254 0.0836 361 ALA A CB 2784 N N . ALA A 362 ? 1.0133 0.6758 0.8233 -0.3064 -0.0362 0.0764 362 ALA A N 2785 C CA . ALA A 362 ? 0.8774 0.5364 0.7070 -0.3092 -0.0381 0.0734 362 ALA A CA 2786 C C . ALA A 362 ? 0.8544 0.5054 0.6707 -0.3065 -0.0417 0.0544 362 ALA A C 2787 O O . ALA A 362 ? 0.8672 0.5172 0.6936 -0.3059 -0.0551 0.0412 362 ALA A O 2788 C CB . ALA A 362 ? 0.8402 0.5035 0.7044 -0.3142 -0.0513 0.0796 362 ALA A CB 2789 N N . PRO A 363 ? 0.8520 0.5012 0.6470 -0.3043 -0.0302 0.0513 363 PRO A N 2790 C CA . PRO A 363 ? 0.8642 0.5149 0.6392 -0.3010 -0.0307 0.0334 363 PRO A CA 2791 C C . PRO A 363 ? 1.0564 0.7043 0.8547 -0.2998 -0.0427 0.0146 363 PRO A C 2792 O O . PRO A 363 ? 1.1076 0.7650 0.8956 -0.2956 -0.0493 -0.0066 363 PRO A O 2793 C CB . PRO A 363 ? 0.9039 0.5524 0.6604 -0.3004 -0.0151 0.0397 363 PRO A CB 2794 C CG . PRO A 363 ? 1.0032 0.6515 0.7631 -0.3017 -0.0073 0.0585 363 PRO A CG 2795 C CD . PRO A 363 ? 0.8361 0.4867 0.6267 -0.3047 -0.0157 0.0648 363 PRO A CD 2796 N N . TYR A 364 ? 1.0019 0.6411 0.8343 -0.3035 -0.0468 0.0221 364 TYR A N 2797 C CA . TYR A 364 ? 0.9166 0.5499 0.7821 -0.3028 -0.0622 0.0059 364 TYR A CA 2798 C C . TYR A 364 ? 0.8828 0.5143 0.7830 -0.3051 -0.0816 0.0051 364 TYR A C 2799 O O . TYR A 364 ? 1.1471 0.7719 1.0858 -0.3051 -0.0992 -0.0067 364 TYR A O 2800 C CB . TYR A 364 ? 0.9327 0.5587 0.8195 -0.3069 -0.0576 0.0172 364 TYR A CB 2801 C CG . TYR A 364 ? 0.9319 0.5597 0.7831 -0.3046 -0.0376 0.0193 364 TYR A CG 2802 C CD1 . TYR A 364 ? 0.9400 0.5716 0.7813 -0.3081 -0.0218 0.0418 364 TYR A CD1 2803 C CD2 . TYR A 364 ? 0.9622 0.5927 0.7902 -0.2984 -0.0353 -0.0027 364 TYR A CD2 2804 C CE1 . TYR A 364 ? 0.9443 0.5765 0.7559 -0.3057 -0.0051 0.0430 364 TYR A CE1 2805 C CE2 . TYR A 364 ? 1.1988 0.8314 0.9949 -0.2971 -0.0180 0.0012 364 TYR A CE2 2806 C CZ . TYR A 364 ? 1.1195 0.7502 0.9083 -0.3008 -0.0033 0.0244 364 TYR A CZ 2807 O OH . TYR A 364 ? 1.2021 0.8337 0.9624 -0.2993 0.0124 0.0276 364 TYR A OH 2808 N N . GLY A 365 ? 0.8973 0.5342 0.7870 -0.3070 -0.0798 0.0176 365 GLY A N 2809 C CA . GLY A 365 ? 0.9499 0.5864 0.8679 -0.3093 -0.0971 0.0180 365 GLY A CA 2810 C C . GLY A 365 ? 1.0284 0.6712 0.9360 -0.3028 -0.1078 -0.0082 365 GLY A C 2811 O O . GLY A 365 ? 1.1516 0.8026 1.0378 -0.2967 -0.1052 -0.0297 365 GLY A O 2812 N N . GLY A 366 ? 1.0733 0.7175 0.9962 -0.3044 -0.1200 -0.0064 366 GLY A N 2813 C CA . GLY A 366 ? 1.2259 0.8813 1.1409 -0.2986 -0.1307 -0.0306 366 GLY A CA 2814 C C . GLY A 366 ? 1.4527 1.1074 1.4048 -0.2934 -0.1519 -0.0606 366 GLY A C 2815 O O . GLY A 366 ? 1.4360 1.0756 1.4314 -0.2966 -0.1637 -0.0569 366 GLY A O 2816 N N . GLU A 367 ? 1.5888 1.2641 1.5278 -0.2855 -0.1587 -0.0907 367 GLU A N 2817 C CA . GLU A 367 ? 1.4514 1.1325 1.4272 -0.2776 -0.1806 -0.1277 367 GLU A CA 2818 C C . GLU A 367 ? 1.4381 1.1233 1.4121 -0.2721 -0.1772 -0.1465 367 GLU A C 2819 O O . GLU A 367 ? 1.4600 1.1683 1.3910 -0.2683 -0.1628 -0.1549 367 GLU A O 2820 C CB . GLU A 367 ? 1.4578 1.1700 1.4203 -0.2702 -0.1891 -0.1561 367 GLU A CB 2821 C CG . GLU A 367 ? 1.6529 1.3857 1.6435 -0.2582 -0.2087 -0.2041 367 GLU A CG 2822 C CD . GLU A 367 ? 1.7757 1.5579 1.7337 -0.2504 -0.2079 -0.2321 367 GLU A CD 2823 O OE1 . GLU A 367 ? 1.7807 1.5761 1.7011 -0.2558 -0.1955 -0.2113 367 GLU A OE1 2824 O OE2 . GLU A 367 ? 1.8292 1.6416 1.8015 -0.2391 -0.2205 -0.2752 367 GLU A OE2 2825 N N . ASP A 368 ? 1.4763 1.1410 1.5001 -0.2723 -0.1924 -0.1518 368 ASP A N 2826 C CA . ASP A 368 ? 1.4412 1.1057 1.4721 -0.2672 -0.1919 -0.1694 368 ASP A CA 2827 C C . ASP A 368 ? 1.2516 0.9215 1.2283 -0.2698 -0.1632 -0.1514 368 ASP A C 2828 O O . ASP A 368 ? 1.2547 0.9496 1.2008 -0.2626 -0.1559 -0.1738 368 ASP A O 2829 C CB . ASP A 368 ? 1.5669 1.2595 1.6096 -0.2531 -0.2087 -0.2216 368 ASP A CB 2830 C CG . ASP A 368 ? 1.8195 1.5033 1.9289 -0.2486 -0.2418 -0.2455 368 ASP A CG 2831 O OD1 . ASP A 368 ? 1.9755 1.6717 2.1190 -0.2369 -0.2616 -0.2887 368 ASP A OD1 2832 O OD2 . ASP A 368 ? 1.8819 1.5480 2.0124 -0.2565 -0.2495 -0.2221 368 ASP A OD2 2833 N N . LYS A 369 ? 1.1979 0.8489 1.1655 -0.2801 -0.1482 -0.1115 369 LYS A N 2834 C CA . LYS A 369 ? 1.2897 0.9410 1.2157 -0.2829 -0.1231 -0.0926 369 LYS A CA 2835 C C . LYS A 369 ? 1.2384 0.9152 1.1091 -0.2793 -0.1085 -0.0984 369 LYS A C 2836 O O . LYS A 369 ? 1.5459 1.2295 1.3857 -0.2785 -0.0931 -0.0960 369 LYS A O 2837 C CB . LYS A 369 ? 1.5582 1.2023 1.5000 -0.2804 -0.1236 -0.1038 369 LYS A CB 2838 C CG . LYS A 369 ? 1.6840 1.3138 1.6167 -0.2882 -0.1053 -0.0718 369 LYS A CG 2839 C CD . LYS A 369 ? 1.6320 1.2538 1.5863 -0.2861 -0.1086 -0.0831 369 LYS A CD 2840 C CE . LYS A 369 ? 1.4771 1.0877 1.4289 -0.2947 -0.0921 -0.0503 369 LYS A CE 2841 N NZ . LYS A 369 ? 1.4070 1.0095 1.3977 -0.3052 -0.0998 -0.0201 369 LYS A NZ 2842 N N . LYS A 370 ? 1.0844 0.7771 0.9448 -0.2781 -0.1142 -0.1035 370 LYS A N 2843 C CA . LYS A 370 ? 1.0906 0.8124 0.9038 -0.2770 -0.1033 -0.1038 370 LYS A CA 2844 C C . LYS A 370 ? 1.0561 0.7673 0.8412 -0.2845 -0.0859 -0.0674 370 LYS A C 2845 O O . LYS A 370 ? 1.0898 0.8188 0.8387 -0.2856 -0.0749 -0.0598 370 LYS A O 2846 C CB . LYS A 370 ? 1.0999 0.8477 0.9146 -0.2734 -0.1170 -0.1223 370 LYS A CB 2847 C CG . LYS A 370 ? 1.1081 0.8915 0.9294 -0.2633 -0.1297 -0.1653 370 LYS A CG 2848 C CD . LYS A 370 ? 1.2368 1.0546 1.0544 -0.2602 -0.1408 -0.1820 370 LYS A CD 2849 C CE . LYS A 370 ? 1.3569 1.2227 1.1802 -0.2488 -0.1533 -0.2289 370 LYS A CE 2850 N NZ . LYS A 370 ? 1.4180 1.3261 1.2368 -0.2456 -0.1636 -0.2462 370 LYS A NZ 2851 N N . GLY A 371 ? 1.0108 0.6970 0.8163 -0.2896 -0.0853 -0.0453 371 GLY A N 2852 C CA . GLY A 371 ? 0.9537 0.6322 0.7406 -0.2947 -0.0715 -0.0158 371 GLY A CA 2853 C C . GLY A 371 ? 1.0210 0.7024 0.8083 -0.2971 -0.0770 -0.0054 371 GLY A C 2854 O O . GLY A 371 ? 1.2924 0.9886 1.0791 -0.2949 -0.0880 -0.0200 371 GLY A O 2855 N N . ILE A 372 ? 0.8985 0.5691 0.6879 -0.3008 -0.0698 0.0181 372 ILE A N 2856 C CA . ILE A 372 ? 0.8990 0.5715 0.6913 -0.3027 -0.0750 0.0288 372 ILE A CA 2857 C C . ILE A 372 ? 0.8869 0.5561 0.6694 -0.3042 -0.0641 0.0501 372 ILE A C 2858 O O . ILE A 372 ? 0.8741 0.5378 0.6602 -0.3044 -0.0541 0.0581 372 ILE A O 2859 C CB . ILE A 372 ? 0.8979 0.5634 0.7266 -0.3049 -0.0875 0.0288 372 ILE A CB 2860 C CG1 . ILE A 372 ? 0.9018 0.5718 0.7319 -0.3062 -0.0946 0.0355 372 ILE A CG1 2861 C CG2 . ILE A 372 ? 1.3876 1.0453 1.2388 -0.3087 -0.0822 0.0450 372 ILE A CG2 2862 C CD1 . ILE A 372 ? 1.1961 0.8616 1.0623 -0.3090 -0.1087 0.0362 372 ILE A CD1 2863 N N . VAL A 373 ? 0.8914 0.5663 0.6643 -0.3047 -0.0672 0.0576 373 VAL A N 2864 C CA . VAL A 373 ? 0.8824 0.5551 0.6524 -0.3044 -0.0609 0.0737 373 VAL A CA 2865 C C . VAL A 373 ? 0.9816 0.6564 0.7663 -0.3049 -0.0684 0.0809 373 VAL A C 2866 O O . VAL A 373 ? 1.0194 0.6991 0.7983 -0.3059 -0.0771 0.0797 373 VAL A O 2867 C CB . VAL A 373 ? 0.8900 0.5681 0.6361 -0.3048 -0.0588 0.0794 373 VAL A CB 2868 C CG1 . VAL A 373 ? 0.9483 0.6222 0.7009 -0.3035 -0.0575 0.0935 373 VAL A CG1 2869 C CG2 . VAL A 373 ? 0.8899 0.5688 0.6204 -0.3045 -0.0503 0.0742 373 VAL A CG2 2870 N N . TYR A 374 ? 0.8672 0.5433 0.6707 -0.3043 -0.0650 0.0882 374 TYR A N 2871 C CA . TYR A 374 ? 0.8644 0.5477 0.6831 -0.3041 -0.0715 0.0944 374 TYR A CA 2872 C C . TYR A 374 ? 0.8633 0.5497 0.6800 -0.3001 -0.0699 0.1003 374 TYR A C 2873 O O . TYR A 374 ? 0.8898 0.5773 0.7067 -0.2970 -0.0618 0.1013 374 TYR A O 2874 C CB . TYR A 374 ? 0.8513 0.5454 0.6956 -0.3063 -0.0710 0.0996 374 TYR A CB 2875 C CG . TYR A 374 ? 0.8543 0.5433 0.7112 -0.3108 -0.0757 0.0961 374 TYR A CG 2876 C CD1 . TYR A 374 ? 0.9410 0.6279 0.8113 -0.3138 -0.0890 0.0932 374 TYR A CD1 2877 C CD2 . TYR A 374 ? 0.8483 0.5343 0.7079 -0.3119 -0.0688 0.0950 374 TYR A CD2 2878 C CE1 . TYR A 374 ? 0.9962 0.6772 0.8865 -0.3172 -0.0973 0.0883 374 TYR A CE1 2879 C CE2 . TYR A 374 ? 0.9523 0.6324 0.8305 -0.3157 -0.0764 0.0911 374 TYR A CE2 2880 C CZ . TYR A 374 ? 0.9431 0.6203 0.8388 -0.3182 -0.0917 0.0872 374 TYR A CZ 2881 O OH . TYR A 374 ? 0.9133 0.5833 0.8356 -0.3213 -0.1031 0.0817 374 TYR A OH 2882 N N . ILE A 375 ? 0.8939 0.5818 0.7122 -0.2997 -0.0791 0.1031 375 ILE A N 2883 C CA . ILE A 375 ? 0.8881 0.5785 0.7137 -0.2953 -0.0819 0.1073 375 ILE A CA 2884 C C . ILE A 375 ? 0.8635 0.5685 0.7108 -0.2923 -0.0864 0.1071 375 ILE A C 2885 O O . ILE A 375 ? 0.9002 0.6098 0.7520 -0.2956 -0.0912 0.1079 375 ILE A O 2886 C CB . ILE A 375 ? 0.9406 0.6242 0.7545 -0.2976 -0.0911 0.1133 375 ILE A CB 2887 C CG1 . ILE A 375 ? 1.2078 0.8949 1.0221 -0.3005 -0.1010 0.1144 375 ILE A CG1 2888 C CG2 . ILE A 375 ? 0.9280 0.6077 0.7191 -0.3016 -0.0871 0.1143 375 ILE A CG2 2889 C CD1 . ILE A 375 ? 1.4841 1.1713 1.2926 -0.3035 -0.1114 0.1240 375 ILE A CD1 2890 N N . PHE A 376 ? 0.8500 0.5658 0.7132 -0.2855 -0.0860 0.1045 376 PHE A N 2891 C CA . PHE A 376 ? 0.8581 0.5981 0.7433 -0.2813 -0.0894 0.1014 376 PHE A CA 2892 C C . PHE A 376 ? 0.9622 0.7051 0.8636 -0.2735 -0.0993 0.0964 376 PHE A C 2893 O O . PHE A 376 ? 1.0611 0.8015 0.9707 -0.2676 -0.0993 0.0913 376 PHE A O 2894 C CB . PHE A 376 ? 0.8995 0.6665 0.7972 -0.2792 -0.0792 0.0983 376 PHE A CB 2895 C CG . PHE A 376 ? 0.9670 0.7321 0.8574 -0.2874 -0.0723 0.1051 376 PHE A CG 2896 C CD1 . PHE A 376 ? 0.8880 0.6362 0.7641 -0.2894 -0.0641 0.1047 376 PHE A CD1 2897 C CD2 . PHE A 376 ? 1.0650 0.8456 0.9668 -0.2934 -0.0761 0.1122 376 PHE A CD2 2898 C CE1 . PHE A 376 ? 0.8246 0.5701 0.6995 -0.2962 -0.0604 0.1092 376 PHE A CE1 2899 C CE2 . PHE A 376 ? 0.9637 0.7408 0.8673 -0.3013 -0.0739 0.1190 376 PHE A CE2 2900 C CZ . PHE A 376 ? 0.8377 0.5967 0.7288 -0.3022 -0.0663 0.1164 376 PHE A CZ 2901 N N . ASN A 377 ? 0.9072 0.6548 0.8166 -0.2732 -0.1094 0.0974 377 ASN A N 2902 C CA . ASN A 377 ? 0.9543 0.7056 0.8851 -0.2654 -0.1217 0.0914 377 ASN A CA 2903 C C . ASN A 377 ? 0.9672 0.7547 0.9248 -0.2548 -0.1207 0.0764 377 ASN A C 2904 O O . ASN A 377 ? 1.0919 0.9092 1.0524 -0.2560 -0.1145 0.0754 377 ASN A O 2905 C CB . ASN A 377 ? 1.1618 0.9071 1.0920 -0.2688 -0.1331 0.0974 377 ASN A CB 2906 C CG . ASN A 377 ? 1.3570 1.0759 1.2655 -0.2776 -0.1371 0.1102 377 ASN A CG 2907 O OD1 . ASN A 377 ? 1.4362 1.1447 1.3243 -0.2830 -0.1289 0.1144 377 ASN A OD1 2908 N ND2 . ASN A 377 ? 1.4124 1.1254 1.3262 -0.2791 -0.1501 0.1163 377 ASN A ND2 2909 N N . GLY A 378 ? 0.9310 0.7204 0.9115 -0.2447 -0.1286 0.0646 378 GLY A N 2910 C CA . GLY A 378 ? 0.9606 0.7914 0.9709 -0.2321 -0.1302 0.0443 378 GLY A CA 2911 C C . GLY A 378 ? 1.0017 0.8461 1.0360 -0.2251 -0.1459 0.0351 378 GLY A C 2912 O O . GLY A 378 ? 1.1104 0.9249 1.1428 -0.2290 -0.1576 0.0447 378 GLY A O 2913 N N . ARG A 379 ? 1.0148 0.9094 1.0726 -0.2148 -0.1464 0.0163 379 ARG A N 2914 C CA . ARG A 379 ? 1.0444 0.9592 1.1280 -0.2062 -0.1615 0.0033 379 ARG A CA 2915 C C . ARG A 379 ? 1.0516 1.0233 1.1716 -0.1891 -0.1655 -0.0277 379 ARG A C 2916 O O . ARG A 379 ? 1.0347 1.0274 1.1600 -0.1842 -0.1569 -0.0382 379 ARG A O 2917 C CB . ARG A 379 ? 1.0674 0.9952 1.1339 -0.2155 -0.1581 0.0171 379 ARG A CB 2918 C CG . ARG A 379 ? 1.1692 1.1435 1.2268 -0.2205 -0.1430 0.0217 379 ARG A CG 2919 C CD . ARG A 379 ? 1.3773 1.3531 1.4187 -0.2326 -0.1418 0.0410 379 ARG A CD 2920 N NE . ARG A 379 ? 1.3754 1.3964 1.4144 -0.2397 -0.1307 0.0507 379 ARG A NE 2921 C CZ . ARG A 379 ? 1.3204 1.3466 1.3500 -0.2520 -0.1298 0.0705 379 ARG A CZ 2922 N NH1 . ARG A 379 ? 1.2510 1.2401 1.2696 -0.2573 -0.1377 0.0792 379 ARG A NH1 2923 N NH2 . ARG A 379 ? 1.3146 1.3850 1.3488 -0.2597 -0.1224 0.0827 379 ARG A NH2 2924 N N . SER A 380 ? 1.0780 1.0784 1.2241 -0.1794 -0.1790 -0.0441 380 SER A N 2925 C CA . SER A 380 ? 1.1206 1.1831 1.3062 -0.1607 -0.1859 -0.0794 380 SER A CA 2926 C C . SER A 380 ? 1.0990 1.2312 1.2767 -0.1615 -0.1682 -0.0830 380 SER A C 2927 O O . SER A 380 ? 1.1086 1.2917 1.3112 -0.1482 -0.1675 -0.1098 380 SER A O 2928 C CB . SER A 380 ? 1.2200 1.3026 1.4326 -0.1513 -0.2038 -0.0952 380 SER A CB 2929 O OG . SER A 380 ? 1.3022 1.3995 1.4896 -0.1628 -0.1964 -0.0757 380 SER A OG 2930 N N . THR A 381 ? 1.0957 1.2327 1.2421 -0.1777 -0.1555 -0.0552 381 THR A N 2931 C CA . THR A 381 ? 1.0866 1.2904 1.2271 -0.1829 -0.1406 -0.0494 381 THR A CA 2932 C C . THR A 381 ? 1.0578 1.2535 1.1855 -0.1875 -0.1260 -0.0425 381 THR A C 2933 O O . THR A 381 ? 1.0258 1.2768 1.1512 -0.1927 -0.1138 -0.0356 381 THR A O 2934 C CB . THR A 381 ? 1.1865 1.3919 1.3037 -0.2005 -0.1353 -0.0181 381 THR A CB 2935 O OG1 . THR A 381 ? 1.2893 1.4279 1.3755 -0.2157 -0.1277 0.0090 381 THR A OG1 2936 C CG2 . THR A 381 ? 1.1839 1.3820 1.3080 -0.1978 -0.1493 -0.0211 381 THR A CG2 2937 N N . GLY A 382 ? 1.1031 1.2327 1.2236 -0.1867 -0.1280 -0.0421 382 GLY A N 2938 C CA . GLY A 382 ? 1.0920 1.2009 1.1947 -0.1931 -0.1142 -0.0317 382 GLY A CA 2939 C C . GLY A 382 ? 1.1209 1.1642 1.1882 -0.2103 -0.1091 -0.0007 382 GLY A C 2940 O O . GLY A 382 ? 1.2952 1.3066 1.3546 -0.2151 -0.1177 0.0091 382 GLY A O 2941 N N . LEU A 383 ? 1.0384 1.0641 1.0858 -0.2188 -0.0958 0.0127 383 LEU A N 2942 C CA . LEU A 383 ? 0.9874 0.9564 1.0040 -0.2333 -0.0919 0.0370 383 LEU A CA 2943 C C . LEU A 383 ? 0.9565 0.9399 0.9650 -0.2452 -0.0908 0.0556 383 LEU A C 2944 O O . LEU A 383 ? 0.9501 0.9809 0.9653 -0.2501 -0.0839 0.0630 383 LEU A O 2945 C CB . LEU A 383 ? 0.9531 0.9038 0.9534 -0.2386 -0.0789 0.0443 383 LEU A CB 2946 C CG . LEU A 383 ? 0.9239 0.8280 0.8955 -0.2528 -0.0747 0.0657 383 LEU A CG 2947 C CD1 . LEU A 383 ? 0.9402 0.7930 0.8994 -0.2535 -0.0848 0.0681 383 LEU A CD1 2948 C CD2 . LEU A 383 ? 0.8971 0.7911 0.8557 -0.2572 -0.0618 0.0711 383 LEU A CD2 2949 N N . ASN A 384 ? 1.0543 0.9992 1.0510 -0.2506 -0.0991 0.0647 384 ASN A N 2950 C CA . ASN A 384 ? 1.0831 1.0310 1.0728 -0.2624 -0.1002 0.0826 384 ASN A CA 2951 C C . ASN A 384 ? 0.9275 0.8461 0.8990 -0.2741 -0.0925 0.0982 384 ASN A C 2952 O O . ASN A 384 ? 0.8586 0.7315 0.8122 -0.2750 -0.0913 0.0978 384 ASN A O 2953 C CB . ASN A 384 ? 1.0864 1.0053 1.0712 -0.2629 -0.1123 0.0840 384 ASN A CB 2954 C CG . ASN A 384 ? 0.9603 0.8577 0.9312 -0.2759 -0.1138 0.1019 384 ASN A CG 2955 O OD1 . ASN A 384 ? 0.9600 0.8139 0.9120 -0.2810 -0.1135 0.1067 384 ASN A OD1 2956 N ND2 . ASN A 384 ? 0.9721 0.9041 0.9550 -0.2812 -0.1169 0.1109 384 ASN A ND2 2957 N N . ALA A 385 ? 0.8569 0.8048 0.8362 -0.2834 -0.0891 0.1127 385 ALA A N 2958 C CA . ALA A 385 ? 0.8323 0.7548 0.8018 -0.2932 -0.0838 0.1249 385 ALA A CA 2959 C C . ALA A 385 ? 0.8345 0.7290 0.8004 -0.3032 -0.0928 0.1369 385 ALA A C 2960 O O . ALA A 385 ? 1.2948 1.2155 1.2778 -0.3111 -0.0989 0.1509 385 ALA A O 2961 C CB . ALA A 385 ? 0.7626 0.7324 0.7483 -0.2984 -0.0764 0.1353 385 ALA A CB 2962 N N . VAL A 386 ? 0.8460 0.6914 0.7916 -0.3027 -0.0943 0.1310 386 VAL A N 2963 C CA . VAL A 386 ? 0.8658 0.6808 0.8061 -0.3099 -0.1025 0.1356 386 VAL A CA 2964 C C . VAL A 386 ? 0.9104 0.6871 0.8254 -0.3056 -0.1015 0.1244 386 VAL A C 2965 O O . VAL A 386 ? 0.9758 0.7494 0.8834 -0.2987 -0.1015 0.1180 386 VAL A O 2966 C CB . VAL A 386 ? 0.9692 0.7945 0.9207 -0.3132 -0.1143 0.1416 386 VAL A CB 2967 C CG1 . VAL A 386 ? 1.1576 0.9870 1.1031 -0.3048 -0.1167 0.1328 386 VAL A CG1 2968 C CG2 . VAL A 386 ? 0.9504 0.7444 0.8984 -0.3192 -0.1238 0.1419 386 VAL A CG2 2969 N N . PRO A 387 ? 0.9008 0.6525 0.8058 -0.3097 -0.1022 0.1222 387 PRO A N 2970 C CA . PRO A 387 ? 1.0186 0.7454 0.8992 -0.3066 -0.1015 0.1134 387 PRO A CA 2971 C C . PRO A 387 ? 1.0060 0.7272 0.8805 -0.3060 -0.1113 0.1122 387 PRO A C 2972 O O . PRO A 387 ? 1.2759 0.9984 1.1589 -0.3098 -0.1199 0.1135 387 PRO A O 2973 C CB . PRO A 387 ? 1.2659 0.9773 1.1415 -0.3106 -0.1019 0.1083 387 PRO A CB 2974 C CG . PRO A 387 ? 1.1571 0.8809 1.0544 -0.3146 -0.0992 0.1158 387 PRO A CG 2975 C CD . PRO A 387 ? 0.9989 0.7484 0.9166 -0.3165 -0.1034 0.1267 387 PRO A CD 2976 N N . SER A 388 ? 0.9153 0.6310 0.7784 -0.3020 -0.1114 0.1112 388 SER A N 2977 C CA . SER A 388 ? 0.9507 0.6623 0.8083 -0.3025 -0.1212 0.1125 388 SER A CA 2978 C C . SER A 388 ? 1.0909 0.7924 0.9281 -0.3062 -0.1233 0.1093 388 SER A C 2979 O O . SER A 388 ? 1.4005 1.1030 1.2305 -0.3081 -0.1312 0.1108 388 SER A O 2980 C CB . SER A 388 ? 0.9481 0.6616 0.8111 -0.2972 -0.1242 0.1152 388 SER A CB 2981 O OG . SER A 388 ? 1.0170 0.7208 0.8699 -0.2963 -0.1206 0.1164 388 SER A OG 2982 N N . GLN A 389 ? 1.0482 0.7453 0.8772 -0.3071 -0.1163 0.1041 389 GLN A N 2983 C CA . GLN A 389 ? 1.1338 0.8302 0.9441 -0.3094 -0.1175 0.0971 389 GLN A CA 2984 C C . GLN A 389 ? 1.1147 0.8068 0.9225 -0.3090 -0.1094 0.0897 389 GLN A C 2985 O O . GLN A 389 ? 0.9629 0.6516 0.7787 -0.3074 -0.1014 0.0937 389 GLN A O 2986 C CB . GLN A 389 ? 0.9639 0.6644 0.7579 -0.3105 -0.1190 0.1051 389 GLN A CB 2987 C CG . GLN A 389 ? 1.0115 0.7257 0.7855 -0.3140 -0.1219 0.0996 389 GLN A CG 2988 C CD . GLN A 389 ? 0.9670 0.6917 0.7284 -0.3177 -0.1246 0.1143 389 GLN A CD 2989 O OE1 . GLN A 389 ? 0.9531 0.6687 0.7244 -0.3171 -0.1261 0.1275 389 GLN A OE1 2990 N NE2 . GLN A 389 ? 0.9900 0.7382 0.7334 -0.3217 -0.1272 0.1120 389 GLN A NE2 2991 N N . ILE A 390 ? 1.0749 0.7709 0.8729 -0.3099 -0.1121 0.0773 390 ILE A N 2992 C CA . ILE A 390 ? 0.9723 0.6646 0.7705 -0.3089 -0.1068 0.0672 390 ILE A CA 2993 C C . ILE A 390 ? 1.1535 0.8585 0.9277 -0.3086 -0.1053 0.0582 390 ILE A C 2994 O O . ILE A 390 ? 1.4822 1.2041 1.2485 -0.3091 -0.1132 0.0492 390 ILE A O 2995 C CB . ILE A 390 ? 0.9553 0.6437 0.7777 -0.3093 -0.1155 0.0557 390 ILE A CB 2996 C CG1 . ILE A 390 ? 1.0808 0.7632 0.9289 -0.3116 -0.1148 0.0690 390 ILE A CG1 2997 C CG2 . ILE A 390 ? 0.9442 0.6321 0.7669 -0.3075 -0.1149 0.0393 390 ILE A CG2 2998 C CD1 . ILE A 390 ? 1.3164 1.0034 1.1762 -0.3133 -0.1225 0.0776 390 ILE A CD1 2999 N N . LEU A 391 ? 1.0252 0.7276 0.7881 -0.3080 -0.0954 0.0609 391 LEU A N 3000 C CA . LEU A 391 ? 1.0349 0.7550 0.7752 -0.3084 -0.0936 0.0537 391 LEU A CA 3001 C C . LEU A 391 ? 1.0337 0.7535 0.7791 -0.3052 -0.0922 0.0335 391 LEU A C 3002 O O . LEU A 391 ? 1.0182 0.7229 0.7693 -0.3043 -0.0840 0.0358 391 LEU A O 3003 C CB . LEU A 391 ? 1.0269 0.7463 0.7522 -0.3104 -0.0856 0.0709 391 LEU A CB 3004 C CG . LEU A 391 ? 1.1254 0.8434 0.8531 -0.3130 -0.0901 0.0907 391 LEU A CG 3005 C CD1 . LEU A 391 ? 1.3615 1.0787 1.0809 -0.3151 -0.0861 0.1066 391 LEU A CD1 3006 C CD2 . LEU A 391 ? 1.1091 0.8489 0.8303 -0.3166 -0.1010 0.0915 391 LEU A CD2 3007 N N . GLU A 392 ? 1.0729 0.8119 0.8189 -0.3030 -0.1015 0.0122 392 GLU A N 3008 C CA . GLU A 392 ? 1.1316 0.8724 0.8885 -0.2985 -0.1043 -0.0119 392 GLU A CA 3009 C C . GLU A 392 ? 1.1662 0.9399 0.8974 -0.2967 -0.1015 -0.0248 392 GLU A C 3010 O O . GLU A 392 ? 1.2429 1.0516 0.9635 -0.2960 -0.1087 -0.0365 392 GLU A O 3011 C CB . GLU A 392 ? 1.4656 1.2070 1.2511 -0.2953 -0.1202 -0.0325 392 GLU A CB 3012 C CG . GLU A 392 ? 1.7459 1.4854 1.5548 -0.2898 -0.1281 -0.0593 392 GLU A CG 3013 C CD . GLU A 392 ? 1.8334 1.5722 1.6779 -0.2865 -0.1478 -0.0801 392 GLU A CD 3014 O OE1 . GLU A 392 ? 1.8314 1.5636 1.7072 -0.2821 -0.1590 -0.1016 392 GLU A OE1 3015 O OE2 . GLU A 392 ? 1.7825 1.5270 1.6272 -0.2882 -0.1536 -0.0752 392 GLU A OE2 3016 N N . GLY A 393 ? 1.1876 0.9554 0.9090 -0.2963 -0.0911 -0.0222 393 GLY A N 3017 C CA . GLY A 393 ? 1.3150 1.1173 1.0121 -0.2951 -0.0879 -0.0330 393 GLY A CA 3018 C C . GLY A 393 ? 1.2949 1.1195 1.0052 -0.2874 -0.0984 -0.0707 393 GLY A C 3019 O O . GLY A 393 ? 1.3913 1.1910 1.1303 -0.2830 -0.1034 -0.0855 393 GLY A O 3020 N N . GLN A 394 ? 1.3378 1.2135 1.0311 -0.2857 -0.1037 -0.0868 394 GLN A N 3021 C CA . GLN A 394 ? 1.5563 1.4627 1.2638 -0.2761 -0.1150 -0.1290 394 GLN A CA 3022 C C . GLN A 394 ? 1.4013 1.3478 1.0847 -0.2739 -0.1086 -0.1407 394 GLN A C 3023 O O . GLN A 394 ? 1.3591 1.3578 1.0138 -0.2778 -0.1063 -0.1346 394 GLN A O 3024 C CB . GLN A 394 ? 1.8103 1.7566 1.5222 -0.2734 -0.1285 -0.1477 394 GLN A CB 3025 C CG . GLN A 394 ? 1.8899 1.8020 1.6230 -0.2761 -0.1354 -0.1354 394 GLN A CG 3026 C CD . GLN A 394 ? 1.8017 1.7198 1.5106 -0.2858 -0.1290 -0.1000 394 GLN A CD 3027 O OE1 . GLN A 394 ? 1.5954 1.5328 1.2755 -0.2920 -0.1193 -0.0781 394 GLN A OE1 3028 N NE2 . GLN A 394 ? 1.8177 1.7196 1.5415 -0.2874 -0.1364 -0.0935 394 GLN A NE2 3029 N N . TRP A 395 ? 1.2952 1.2207 0.9924 -0.2684 -0.1068 -0.1563 395 TRP A N 3030 C CA . TRP A 395 ? 1.2584 1.2209 0.9372 -0.2646 -0.1019 -0.1730 395 TRP A CA 3031 C C . TRP A 395 ? 1.2642 1.2066 0.9767 -0.2544 -0.1100 -0.2068 395 TRP A C 3032 O O . TRP A 395 ? 1.2398 1.1278 0.9832 -0.2549 -0.1129 -0.1997 395 TRP A O 3033 C CB . TRP A 395 ? 1.2382 1.1892 0.8855 -0.2736 -0.0839 -0.1359 395 TRP A CB 3034 C CG . TRP A 395 ? 1.2414 1.2214 0.8596 -0.2838 -0.0798 -0.1042 395 TRP A CG 3035 C CD1 . TRP A 395 ? 1.2467 1.1927 0.8621 -0.2925 -0.0749 -0.0668 395 TRP A CD1 3036 C CD2 . TRP A 395 ? 1.3113 1.3649 0.9038 -0.2868 -0.0825 -0.1066 395 TRP A CD2 3037 N NE1 . TRP A 395 ? 1.2468 1.2347 0.8393 -0.3010 -0.0758 -0.0444 395 TRP A NE1 3038 C CE2 . TRP A 395 ? 1.2506 1.3070 0.8278 -0.2988 -0.0800 -0.0657 395 TRP A CE2 3039 C CE3 . TRP A 395 ? 1.5785 1.7016 1.1619 -0.2805 -0.0879 -0.1396 395 TRP A CE3 3040 C CZ2 . TRP A 395 ? 1.5068 1.6323 1.0609 -0.3068 -0.0832 -0.0517 395 TRP A CZ2 3041 C CZ3 . TRP A 395 ? 1.6627 1.8606 1.2197 -0.2878 -0.0894 -0.1277 395 TRP A CZ3 3042 C CH2 . TRP A 395 ? 1.6522 1.8504 1.1951 -0.3018 -0.0873 -0.0816 395 TRP A CH2 3043 N N . ALA A 396 ? 1.3824 1.3728 1.0919 -0.2455 -0.1152 -0.2427 396 ALA A N 3044 C CA . ALA A 396 ? 1.4293 1.4046 1.1764 -0.2346 -0.1265 -0.2791 396 ALA A CA 3045 C C . ALA A 396 ? 1.1845 1.1157 0.9281 -0.2386 -0.1128 -0.2582 396 ALA A C 3046 O O . ALA A 396 ? 1.1746 1.0900 0.8863 -0.2487 -0.0947 -0.2188 396 ALA A O 3047 C CB . ALA A 396 ? 1.6597 1.7066 1.4058 -0.2223 -0.1370 -0.3282 396 ALA A CB 3048 N N . ALA A 397 ? 1.1872 1.0999 0.9675 -0.2304 -0.1232 -0.2857 397 ALA A N 3049 C CA . ALA A 397 ? 1.2378 1.1127 1.0186 -0.2336 -0.1116 -0.2692 397 ALA A CA 3050 C C . ALA A 397 ? 1.5575 1.4674 1.3375 -0.2233 -0.1147 -0.3062 397 ALA A C 3051 O O . ALA A 397 ? 1.8259 1.7499 1.6457 -0.2112 -0.1354 -0.3505 397 ALA A O 3052 C CB . ALA A 397 ? 1.1848 1.0000 1.0153 -0.2360 -0.1211 -0.2591 397 ALA A CB 3053 N N . ARG A 398 ? 1.4637 1.3888 1.2012 -0.2275 -0.0956 -0.2891 398 ARG A N 3054 C CA . ARG A 398 ? 1.3591 1.3238 1.0890 -0.2185 -0.0962 -0.3215 398 ARG A CA 3055 C C . ARG A 398 ? 1.2692 1.1865 1.0202 -0.2180 -0.0924 -0.3182 398 ARG A C 3056 O O . ARG A 398 ? 1.4477 1.3604 1.2416 -0.2075 -0.1096 -0.3548 398 ARG A O 3057 C CB . ARG A 398 ? 1.3802 1.3982 1.0523 -0.2242 -0.0794 -0.3046 398 ARG A CB 3058 C CG . ARG A 398 ? 1.5116 1.5931 1.1648 -0.2245 -0.0854 -0.3117 398 ARG A CG 3059 C CD . ARG A 398 ? 1.6329 1.7611 1.2330 -0.2351 -0.0698 -0.2801 398 ARG A CD 3060 N NE . ARG A 398 ? 1.8041 2.0044 1.3888 -0.2361 -0.0772 -0.2873 398 ARG A NE 3061 C CZ . ARG A 398 ? 1.6574 1.8488 1.2396 -0.2442 -0.0788 -0.2618 398 ARG A CZ 3062 N NH1 . ARG A 398 ? 1.5246 1.6394 1.1186 -0.2510 -0.0736 -0.2296 398 ARG A NH1 3063 N NH2 . ARG A 398 ? 1.4860 1.7500 1.0547 -0.2453 -0.0859 -0.2690 398 ARG A NH2 3064 N N . SER A 399 ? 1.1989 1.0825 0.9231 -0.2291 -0.0715 -0.2749 399 SER A N 3065 C CA . SER A 399 ? 1.3642 1.2065 1.1035 -0.2303 -0.0651 -0.2663 399 SER A CA 3066 C C . SER A 399 ? 1.3867 1.1690 1.1528 -0.2394 -0.0632 -0.2321 399 SER A C 3067 O O . SER A 399 ? 1.2637 1.0157 1.0791 -0.2376 -0.0772 -0.2407 399 SER A O 3068 C CB . SER A 399 ? 1.4757 1.3313 1.1665 -0.2352 -0.0428 -0.2461 399 SER A CB 3069 O OG . SER A 399 ? 1.5793 1.3949 1.2834 -0.2370 -0.0352 -0.2355 399 SER A OG 3070 N N . MET A 400 ? 1.4031 1.1732 1.1398 -0.2495 -0.0476 -0.1930 400 MET A N 3071 C CA . MET A 400 ? 1.2142 0.9386 0.9701 -0.2582 -0.0430 -0.1593 400 MET A CA 3072 C C . MET A 400 ? 1.1087 0.8332 0.8674 -0.2617 -0.0492 -0.1477 400 MET A C 3073 O O . MET A 400 ? 1.1517 0.9104 0.8955 -0.2579 -0.0558 -0.1646 400 MET A O 3074 C CB . MET A 400 ? 1.0945 0.8047 0.8182 -0.2655 -0.0197 -0.1260 400 MET A CB 3075 C CG . MET A 400 ? 1.0135 0.7448 0.6913 -0.2696 -0.0075 -0.1074 400 MET A CG 3076 S SD . MET A 400 ? 1.9108 1.6285 1.5571 -0.2756 0.0158 -0.0770 400 MET A SD 3077 C CE . MET A 400 ? 1.6519 1.3838 1.2948 -0.2690 0.0171 -0.1042 400 MET A CE 3078 N N . PRO A 401 ? 1.0049 0.6969 0.7831 -0.2691 -0.0476 -0.1195 401 PRO A N 3079 C CA . PRO A 401 ? 1.0019 0.6954 0.7820 -0.2720 -0.0536 -0.1097 401 PRO A CA 3080 C C . PRO A 401 ? 1.1145 0.8316 0.8487 -0.2742 -0.0426 -0.0976 401 PRO A C 3081 O O . PRO A 401 ? 1.2906 1.0042 0.9968 -0.2784 -0.0262 -0.0756 401 PRO A O 3082 C CB . PRO A 401 ? 0.9712 0.6331 0.7735 -0.2802 -0.0494 -0.0781 401 PRO A CB 3083 C CG . PRO A 401 ? 1.0710 0.7162 0.9047 -0.2805 -0.0527 -0.0812 401 PRO A CG 3084 C CD . PRO A 401 ? 1.1052 0.7648 0.9131 -0.2746 -0.0448 -0.1002 401 PRO A CD 3085 N N . PRO A 402 ? 1.1354 0.8781 0.8655 -0.2717 -0.0534 -0.1113 402 PRO A N 3086 C CA . PRO A 402 ? 1.1929 0.9590 0.8866 -0.2759 -0.0464 -0.0945 402 PRO A CA 3087 C C . PRO A 402 ? 1.2535 0.9908 0.9506 -0.2829 -0.0409 -0.0619 402 PRO A C 3088 O O . PRO A 402 ? 1.5695 1.3073 1.2772 -0.2840 -0.0499 -0.0600 402 PRO A O 3089 C CB . PRO A 402 ? 1.1624 0.9653 0.8601 -0.2709 -0.0620 -0.1211 402 PRO A CB 3090 C CG . PRO A 402 ? 1.1657 0.9468 0.9103 -0.2659 -0.0782 -0.1421 402 PRO A CG 3091 C CD . PRO A 402 ? 1.1414 0.8940 0.9052 -0.2650 -0.0745 -0.1429 402 PRO A CD 3092 N N . SER A 403 ? 1.0358 0.7513 0.7253 -0.2869 -0.0268 -0.0389 403 SER A N 3093 C CA . SER A 403 ? 1.0060 0.6973 0.7069 -0.2914 -0.0228 -0.0139 403 SER A CA 3094 C C . SER A 403 ? 1.0029 0.7061 0.6862 -0.2945 -0.0240 0.0008 403 SER A C 3095 O O . SER A 403 ? 1.1688 0.8853 0.8262 -0.2968 -0.0180 0.0118 403 SER A O 3096 C CB . SER A 403 ? 1.2051 0.8787 0.9026 -0.2935 -0.0078 0.0034 403 SER A CB 3097 O OG . SER A 403 ? 0.8736 0.5392 0.5852 -0.2915 -0.0064 -0.0085 403 SER A OG 3098 N N . PHE A 404 ? 0.9992 0.6973 0.6997 -0.2954 -0.0331 0.0032 404 PHE A N 3099 C CA . PHE A 404 ? 0.9565 0.6645 0.6452 -0.2984 -0.0364 0.0170 404 PHE A CA 3100 C C . PHE A 404 ? 0.9832 0.6695 0.6841 -0.3005 -0.0315 0.0381 404 PHE A C 3101 O O . PHE A 404 ? 1.3569 1.0307 1.0824 -0.3004 -0.0348 0.0387 404 PHE A O 3102 C CB . PHE A 404 ? 0.9625 0.6853 0.6604 -0.2971 -0.0506 0.0025 404 PHE A CB 3103 C CG . PHE A 404 ? 0.9650 0.7018 0.6504 -0.3009 -0.0547 0.0169 404 PHE A CG 3104 C CD1 . PHE A 404 ? 0.9888 0.7582 0.6486 -0.3037 -0.0554 0.0207 404 PHE A CD1 3105 C CD2 . PHE A 404 ? 0.9460 0.6674 0.6473 -0.3024 -0.0591 0.0286 404 PHE A CD2 3106 C CE1 . PHE A 404 ? 1.0049 0.7887 0.6575 -0.3087 -0.0611 0.0376 404 PHE A CE1 3107 C CE2 . PHE A 404 ? 0.9622 0.6954 0.6549 -0.3059 -0.0642 0.0421 404 PHE A CE2 3108 C CZ . PHE A 404 ? 0.9947 0.7578 0.6643 -0.3094 -0.0657 0.0475 404 PHE A CZ 3109 N N . GLY A 405 ? 0.9368 0.6231 0.6236 -0.3025 -0.0255 0.0552 405 GLY A N 3110 C CA . GLY A 405 ? 1.0358 0.7057 0.7354 -0.3020 -0.0189 0.0692 405 GLY A CA 3111 C C . GLY A 405 ? 1.1635 0.8276 0.8559 -0.3009 -0.0069 0.0691 405 GLY A C 3112 O O . GLY A 405 ? 1.5343 1.2076 1.2078 -0.3014 -0.0046 0.0628 405 GLY A O 3113 N N . TYR A 406 ? 0.8957 0.5500 0.6031 -0.2994 0.0007 0.0755 406 TYR A N 3114 C CA . TYR A 406 ? 0.8392 0.4887 0.5420 -0.2981 0.0131 0.0773 406 TYR A CA 3115 C C . TYR A 406 ? 0.9492 0.5990 0.6376 -0.2981 0.0148 0.0876 406 TYR A C 3116 O O . TYR A 406 ? 1.1553 0.8005 0.8440 -0.2963 0.0236 0.0913 406 TYR A O 3117 C CB . TYR A 406 ? 0.8422 0.4918 0.5365 -0.2984 0.0166 0.0649 406 TYR A CB 3118 C CG . TYR A 406 ? 0.8292 0.4730 0.5246 -0.2976 0.0293 0.0662 406 TYR A CG 3119 C CD1 . TYR A 406 ? 0.8170 0.4586 0.5360 -0.2984 0.0322 0.0665 406 TYR A CD1 3120 C CD2 . TYR A 406 ? 0.8294 0.4732 0.5039 -0.2971 0.0374 0.0694 406 TYR A CD2 3121 C CE1 . TYR A 406 ? 1.0055 0.6456 0.7263 -0.2983 0.0438 0.0691 406 TYR A CE1 3122 C CE2 . TYR A 406 ? 0.9152 0.5541 0.5902 -0.2962 0.0494 0.0701 406 TYR A CE2 3123 C CZ . TYR A 406 ? 1.0422 0.6797 0.7398 -0.2966 0.0530 0.0694 406 TYR A CZ 3124 O OH . TYR A 406 ? 1.1424 0.7871 0.8468 -0.2896 0.0633 0.0692 406 TYR A OH 3125 N N . SER A 407 ? 0.8564 0.5134 0.5353 -0.3008 0.0048 0.0934 407 SER A N 3126 C CA . SER A 407 ? 0.8617 0.5194 0.5374 -0.3026 0.0003 0.1085 407 SER A CA 3127 C C . SER A 407 ? 1.0830 0.7462 0.7666 -0.3050 -0.0137 0.1168 407 SER A C 3128 O O . SER A 407 ? 0.8833 0.5602 0.5561 -0.3083 -0.0200 0.1140 407 SER A O 3129 C CB . SER A 407 ? 1.2566 0.9259 0.9078 -0.3070 0.0023 0.1133 407 SER A CB 3130 O OG . SER A 407 ? 1.2721 0.9610 0.9068 -0.3094 -0.0012 0.1039 407 SER A OG 3131 N N . MET A 408 ? 1.1304 0.7854 0.8349 -0.3026 -0.0197 0.1252 408 MET A N 3132 C CA . MET A 408 ? 0.8784 0.5367 0.5945 -0.3047 -0.0343 0.1343 408 MET A CA 3133 C C . MET A 408 ? 0.9303 0.5806 0.6691 -0.3033 -0.0442 0.1467 408 MET A C 3134 O O . MET A 408 ? 1.0554 0.6970 0.8097 -0.2969 -0.0391 0.1408 408 MET A O 3135 C CB . MET A 408 ? 0.8721 0.5288 0.6025 -0.3008 -0.0355 0.1239 408 MET A CB 3136 C CG . MET A 408 ? 1.0132 0.6770 0.7308 -0.3029 -0.0333 0.1132 408 MET A CG 3137 S SD . MET A 408 ? 0.9914 0.6541 0.7306 -0.3000 -0.0375 0.1062 408 MET A SD 3138 C CE . MET A 408 ? 0.9214 0.5815 0.6817 -0.2938 -0.0277 0.1034 408 MET A CE 3139 N N . LYS A 409 ? 0.9724 0.6283 0.7170 -0.3093 -0.0599 0.1634 409 LYS A N 3140 C CA . LYS A 409 ? 0.9883 0.6347 0.7653 -0.3077 -0.0751 0.1746 409 LYS A CA 3141 C C . LYS A 409 ? 0.9093 0.5601 0.7012 -0.3111 -0.0921 0.1846 409 LYS A C 3142 O O . LYS A 409 ? 0.9224 0.5894 0.6983 -0.3207 -0.0983 0.1992 409 LYS A O 3143 C CB . LYS A 409 ? 0.9368 0.5839 0.7145 -0.3141 -0.0815 0.1939 409 LYS A CB 3144 C CG . LYS A 409 ? 1.0555 0.6889 0.8759 -0.3111 -0.0998 0.2031 409 LYS A CG 3145 C CD . LYS A 409 ? 1.4012 1.0223 1.2455 -0.2966 -0.0933 0.1780 409 LYS A CD 3146 C CE . LYS A 409 ? 1.6470 1.2570 1.5411 -0.2908 -0.1147 0.1800 409 LYS A CE 3147 N NZ . LYS A 409 ? 1.6342 1.2370 1.5403 -0.2962 -0.1247 0.1983 409 LYS A NZ 3148 N N . GLY A 410 ? 0.9362 0.5775 0.7594 -0.3028 -0.0996 0.1757 410 GLY A N 3149 C CA . GLY A 410 ? 1.1121 0.7552 0.9541 -0.3049 -0.1168 0.1842 410 GLY A CA 3150 C C . GLY A 410 ? 1.1463 0.7795 1.0310 -0.3036 -0.1388 0.1959 410 GLY A C 3151 O O . GLY A 410 ? 1.2555 0.8826 1.1517 -0.3055 -0.1442 0.2060 410 GLY A O 3152 N N . ALA A 411 ? 1.0236 0.6550 0.9347 -0.3005 -0.1533 0.1945 411 ALA A N 3153 C CA . ALA A 411 ? 1.0012 0.6217 0.9638 -0.2954 -0.1769 0.1976 411 ALA A CA 3154 C C . ALA A 411 ? 1.0905 0.7078 1.0721 -0.3077 -0.1985 0.2304 411 ALA A C 3155 O O . ALA A 411 ? 1.2987 0.9031 1.3240 -0.3034 -0.2163 0.2325 411 ALA A O 3156 C CB . ALA A 411 ? 1.0920 0.7065 1.0792 -0.2803 -0.1722 0.1714 411 ALA A CB 3157 N N . THR A 412 ? 0.9631 0.5966 0.9157 -0.3230 -0.1987 0.2561 412 THR A N 3158 C CA . THR A 412 ? 1.0241 0.6650 0.9960 -0.3379 -0.2214 0.2939 412 THR A CA 3159 C C . THR A 412 ? 1.1136 0.7804 1.0663 -0.3518 -0.2271 0.3167 412 THR A C 3160 O O . THR A 412 ? 1.3266 1.0110 1.2348 -0.3533 -0.2079 0.3066 412 THR A O 3161 C CB . THR A 412 ? 0.9829 0.6309 0.9358 -0.3453 -0.2142 0.3078 412 THR A CB 3162 O OG1 . THR A 412 ? 1.3225 0.9487 1.2897 -0.3317 -0.2063 0.2839 412 THR A OG1 3163 C CG2 . THR A 412 ? 0.9998 0.6668 0.9815 -0.3549 -0.2385 0.3443 412 THR A CG2 3164 N N . ASP A 413 ? 1.0747 0.7459 1.0646 -0.3621 -0.2550 0.3473 413 ASP A N 3165 C CA . ASP A 413 ? 1.0231 0.7252 0.9979 -0.3764 -0.2621 0.3718 413 ASP A CA 3166 C C . ASP A 413 ? 1.0347 0.7780 0.9997 -0.3910 -0.2687 0.4063 413 ASP A C 3167 O O . ASP A 413 ? 1.6425 1.3960 1.6502 -0.3919 -0.2914 0.4287 413 ASP A O 3168 C CB . ASP A 413 ? 1.1758 0.8662 1.1990 -0.3764 -0.2882 0.3818 413 ASP A CB 3169 C CG . ASP A 413 ? 1.3185 1.0424 1.3270 -0.3907 -0.2950 0.4060 413 ASP A CG 3170 O OD1 . ASP A 413 ? 1.6314 1.3865 1.5889 -0.3960 -0.2756 0.4030 413 ASP A OD1 3171 O OD2 . ASP A 413 ? 1.0641 0.7895 1.1147 -0.3922 -0.3193 0.4222 413 ASP A OD2 3172 N N . ILE A 414 ? 1.0335 0.8064 0.9447 -0.4007 -0.2497 0.4078 414 ILE A N 3173 C CA . ILE A 414 ? 1.0416 0.8649 0.9377 -0.4122 -0.2518 0.4336 414 ILE A CA 3174 C C . ILE A 414 ? 1.0570 0.9320 0.9593 -0.4277 -0.2692 0.4667 414 ILE A C 3175 O O . ILE A 414 ? 1.0667 0.9839 0.9865 -0.4365 -0.2839 0.4956 414 ILE A O 3176 C CB . ILE A 414 ? 1.1876 1.0267 1.0245 -0.4148 -0.2244 0.4171 414 ILE A CB 3177 C CG1 . ILE A 414 ? 1.0402 0.9312 0.8669 -0.4232 -0.2265 0.4387 414 ILE A CG1 3178 C CG2 . ILE A 414 ? 1.1812 1.0432 0.9822 -0.4115 -0.2100 0.3942 414 ILE A CG2 3179 C CD1 . ILE A 414 ? 1.0319 0.9329 0.8092 -0.4218 -0.2014 0.4185 414 ILE A CD1 3180 N N . ASP A 415 ? 1.2454 1.1204 1.1353 -0.4317 -0.2682 0.4629 415 ASP A N 3181 C CA . ASP A 415 ? 1.0729 1.0012 0.9652 -0.4466 -0.2827 0.4925 415 ASP A CA 3182 C C . ASP A 415 ? 1.0815 0.9946 1.0334 -0.4454 -0.3108 0.5105 415 ASP A C 3183 O O . ASP A 415 ? 1.4521 1.4059 1.4151 -0.4574 -0.3259 0.5364 415 ASP A O 3184 C CB . ASP A 415 ? 1.0697 1.0182 0.9174 -0.4464 -0.2655 0.4711 415 ASP A CB 3185 C CG . ASP A 415 ? 1.1207 1.0142 0.9692 -0.4258 -0.2527 0.4278 415 ASP A CG 3186 O OD1 . ASP A 415 ? 1.0501 0.9561 0.8671 -0.4195 -0.2372 0.4008 415 ASP A OD1 3187 O OD2 . ASP A 415 ? 1.3212 1.1635 1.2038 -0.4160 -0.2590 0.4201 415 ASP A OD2 3188 N N . LYS A 416 ? 1.0762 0.9346 1.0679 -0.4304 -0.3184 0.4952 416 LYS A N 3189 C CA . LYS A 416 ? 1.1027 0.9411 1.1562 -0.4259 -0.3466 0.5057 416 LYS A CA 3190 C C . LYS A 416 ? 1.0983 0.9361 1.1487 -0.4295 -0.3501 0.5053 416 LYS A C 3191 O O . LYS A 416 ? 1.1213 0.9723 1.2129 -0.4345 -0.3752 0.5282 416 LYS A O 3192 C CB . LYS A 416 ? 1.1220 1.0006 1.2184 -0.4363 -0.3744 0.5450 416 LYS A CB 3193 C CG . LYS A 416 ? 1.1316 1.0085 1.2391 -0.4324 -0.3749 0.5467 416 LYS A CG 3194 C CD . LYS A 416 ? 1.3115 1.2294 1.4686 -0.4443 -0.4060 0.5872 416 LYS A CD 3195 C CE . LYS A 416 ? 1.3871 1.3016 1.5565 -0.4404 -0.4072 0.5883 416 LYS A CE 3196 N NZ . LYS A 416 ? 1.3295 1.2856 1.5524 -0.4536 -0.4400 0.6293 416 LYS A NZ 3197 N N . ASN A 417 ? 1.2280 1.0509 1.2316 -0.4276 -0.3258 0.4794 417 ASN A N 3198 C CA . ASN A 417 ? 1.2340 1.0566 1.2307 -0.4283 -0.3259 0.4728 417 ASN A CA 3199 C C . ASN A 417 ? 1.1789 0.9497 1.2126 -0.4107 -0.3325 0.4457 417 ASN A C 3200 O O . ASN A 417 ? 1.2905 1.0579 1.3229 -0.4058 -0.3319 0.4331 417 ASN A O 3201 C CB . ASN A 417 ? 1.1470 0.9931 1.0825 -0.4230 -0.2961 0.4431 417 ASN A CB 3202 C CG . ASN A 417 ? 1.2237 1.0375 1.1355 -0.4053 -0.2710 0.4009 417 ASN A CG 3203 O OD1 . ASN A 417 ? 1.4829 1.2598 1.4199 -0.3961 -0.2733 0.3919 417 ASN A OD1 3204 N ND2 . ASN A 417 ? 1.1421 0.9723 1.0085 -0.4004 -0.2484 0.3747 417 ASN A ND2 3205 N N . GLY A 418 ? 1.0677 0.8027 1.1349 -0.4007 -0.3390 0.4353 418 GLY A N 3206 C CA . GLY A 418 ? 1.1328 0.8273 1.2386 -0.3824 -0.3462 0.4058 418 GLY A CA 3207 C C . GLY A 418 ? 1.1503 0.8302 1.2204 -0.3640 -0.3159 0.3587 418 GLY A C 3208 O O . GLY A 418 ? 1.0922 0.7488 1.1866 -0.3476 -0.3171 0.3295 418 GLY A O 3209 N N . TYR A 419 ? 1.0323 0.7309 1.0476 -0.3669 -0.2901 0.3519 419 TYR A N 3210 C CA . TYR A 419 ? 1.0135 0.7009 0.9968 -0.3522 -0.2628 0.3125 419 TYR A CA 3211 C C . TYR A 419 ? 1.0058 0.6945 0.9630 -0.3516 -0.2454 0.3066 419 TYR A C 3212 O O . TYR A 419 ? 1.0139 0.7266 0.9503 -0.3648 -0.2447 0.3294 419 TYR A O 3213 C CB . TYR A 419 ? 1.2047 0.9108 1.1489 -0.3538 -0.2482 0.3025 419 TYR A CB 3214 C CG . TYR A 419 ? 1.3091 1.0099 1.2751 -0.3507 -0.2604 0.2999 419 TYR A CG 3215 C CD1 . TYR A 419 ? 1.3189 1.0335 1.3064 -0.3631 -0.2828 0.3308 419 TYR A CD1 3216 C CD2 . TYR A 419 ? 1.2793 0.9653 1.2453 -0.3364 -0.2502 0.2685 419 TYR A CD2 3217 C CE1 . TYR A 419 ? 1.1707 0.8800 1.1786 -0.3601 -0.2941 0.3281 419 TYR A CE1 3218 C CE2 . TYR A 419 ? 1.0973 0.7807 1.0823 -0.3334 -0.2612 0.2657 419 TYR A CE2 3219 C CZ . TYR A 419 ? 1.0859 0.7786 1.0914 -0.3447 -0.2829 0.2943 419 TYR A CZ 3220 O OH . TYR A 419 ? 1.1405 0.8300 1.1654 -0.3415 -0.2940 0.2912 419 TYR A OH 3221 N N . PRO A 420 ? 1.0688 0.7368 1.0268 -0.3366 -0.2313 0.2759 420 PRO A N 3222 C CA . PRO A 420 ? 0.9806 0.6468 0.9152 -0.3343 -0.2135 0.2668 420 PRO A CA 3223 C C . PRO A 420 ? 0.9774 0.6647 0.8597 -0.3396 -0.1925 0.2618 420 PRO A C 3224 O O . PRO A 420 ? 0.9740 0.6674 0.8393 -0.3372 -0.1848 0.2485 420 PRO A O 3225 C CB . PRO A 420 ? 0.9635 0.6102 0.9136 -0.3167 -0.2040 0.2336 420 PRO A CB 3226 C CG . PRO A 420 ? 1.0777 0.7152 1.0723 -0.3099 -0.2241 0.2294 420 PRO A CG 3227 C CD . PRO A 420 ? 1.1092 0.7594 1.0949 -0.3210 -0.2333 0.2490 420 PRO A CD 3228 N N . ASP A 421 ? 0.9790 0.6783 0.8391 -0.3460 -0.1848 0.2708 421 ASP A N 3229 C CA . ASP A 421 ? 0.9773 0.7001 0.7924 -0.3497 -0.1673 0.2626 421 ASP A CA 3230 C C . ASP A 421 ? 0.9669 0.6760 0.7653 -0.3409 -0.1471 0.2397 421 ASP A C 3231 O O . ASP A 421 ? 1.0465 0.7321 0.8663 -0.3328 -0.1463 0.2323 421 ASP A O 3232 C CB . ASP A 421 ? 1.0773 0.8382 0.8778 -0.3656 -0.1755 0.2919 421 ASP A CB 3233 C CG . ASP A 421 ? 1.2815 1.0566 1.1079 -0.3765 -0.1992 0.3222 421 ASP A CG 3234 O OD1 . ASP A 421 ? 1.2198 1.0104 1.0381 -0.3784 -0.2010 0.3196 421 ASP A OD1 3235 O OD2 . ASP A 421 ? 1.4649 1.2354 1.3232 -0.3835 -0.2177 0.3494 421 ASP A OD2 3236 N N . LEU A 422 ? 0.9602 0.6863 0.7235 -0.3419 -0.1321 0.2272 422 LEU A N 3237 C CA . LEU A 422 ? 0.9459 0.6582 0.6961 -0.3335 -0.1136 0.2045 422 LEU A CA 3238 C C . LEU A 422 ? 0.9488 0.6835 0.6673 -0.3382 -0.1035 0.2026 422 LEU A C 3239 O O . LEU A 422 ? 0.9601 0.7257 0.6584 -0.3438 -0.1047 0.2024 422 LEU A O 3240 C CB . LEU A 422 ? 0.9356 0.6375 0.6850 -0.3251 -0.1050 0.1803 422 LEU A CB 3241 C CG . LEU A 422 ? 0.9208 0.6108 0.6621 -0.3178 -0.0879 0.1597 422 LEU A CG 3242 C CD1 . LEU A 422 ? 0.9102 0.5824 0.6701 -0.3120 -0.0847 0.1601 422 LEU A CD1 3243 C CD2 . LEU A 422 ? 0.9131 0.5984 0.6587 -0.3126 -0.0836 0.1424 422 LEU A CD2 3244 N N . ILE A 423 ? 0.9631 0.6855 0.6785 -0.3349 -0.0938 0.1987 423 ILE A N 3245 C CA . ILE A 423 ? 1.0439 0.7854 0.7307 -0.3375 -0.0832 0.1934 423 ILE A CA 3246 C C . ILE A 423 ? 1.1970 0.9221 0.8758 -0.3282 -0.0666 0.1657 423 ILE A C 3247 O O . ILE A 423 ? 1.3858 1.0847 1.0796 -0.3213 -0.0602 0.1592 423 ILE A O 3248 C CB . ILE A 423 ? 0.9759 0.7194 0.6640 -0.3429 -0.0853 0.2132 423 ILE A CB 3249 C CG1 . ILE A 423 ? 0.9871 0.7465 0.6920 -0.3541 -0.1057 0.2463 423 ILE A CG1 3250 C CG2 . ILE A 423 ? 0.9460 0.7152 0.6027 -0.3457 -0.0746 0.2071 423 ILE A CG2 3251 C CD1 . ILE A 423 ? 1.1803 0.9422 0.8930 -0.3610 -0.1119 0.2702 423 ILE A CD1 3252 N N . VAL A 424 ? 1.1079 0.8524 0.7667 -0.3279 -0.0614 0.1491 424 VAL A N 3253 C CA . VAL A 424 ? 0.9290 0.6601 0.5847 -0.3206 -0.0490 0.1252 424 VAL A CA 3254 C C . VAL A 424 ? 1.0374 0.7898 0.6700 -0.3218 -0.0423 0.1166 424 VAL A C 3255 O O . VAL A 424 ? 1.4417 1.2284 1.0592 -0.3245 -0.0469 0.1096 424 VAL A O 3256 C CB . VAL A 424 ? 0.9298 0.6601 0.5927 -0.3170 -0.0519 0.1072 424 VAL A CB 3257 C CG1 . VAL A 424 ? 0.9103 0.6269 0.5774 -0.3112 -0.0427 0.0866 424 VAL A CG1 3258 C CG2 . VAL A 424 ? 0.9163 0.6297 0.6008 -0.3158 -0.0584 0.1152 424 VAL A CG2 3259 N N . GLY A 425 ? 0.9142 0.6508 0.5446 -0.3193 -0.0318 0.1157 425 GLY A N 3260 C CA . GLY A 425 ? 0.9583 0.7141 0.5676 -0.3198 -0.0250 0.1069 425 GLY A CA 3261 C C . GLY A 425 ? 0.9589 0.7104 0.5692 -0.3130 -0.0192 0.0784 425 GLY A C 3262 O O . GLY A 425 ? 0.9017 0.6256 0.5311 -0.3085 -0.0159 0.0709 425 GLY A O 3263 N N . ALA A 426 ? 1.0411 0.8244 0.6345 -0.3126 -0.0198 0.0628 426 ALA A N 3264 C CA . ALA A 426 ? 0.9658 0.7459 0.5651 -0.3055 -0.0171 0.0338 426 ALA A CA 3265 C C . ALA A 426 ? 1.0041 0.8032 0.5842 -0.3047 -0.0099 0.0258 426 ALA A C 3266 O O . ALA A 426 ? 1.3211 1.1650 0.8817 -0.3068 -0.0138 0.0215 426 ALA A O 3267 C CB . ALA A 426 ? 0.9549 0.7585 0.5609 -0.3024 -0.0288 0.0114 426 ALA A CB 3268 N N . PHE A 427 ? 0.9531 0.7234 0.5392 -0.3018 0.0003 0.0235 427 PHE A N 3269 C CA . PHE A 427 ? 0.9627 0.7470 0.5304 -0.3010 0.0082 0.0180 427 PHE A CA 3270 C C . PHE A 427 ? 1.0290 0.8253 0.6035 -0.2936 0.0052 -0.0163 427 PHE A C 3271 O O . PHE A 427 ? 1.0339 0.8496 0.5935 -0.2916 0.0098 -0.0272 427 PHE A O 3272 C CB . PHE A 427 ? 0.9295 0.6796 0.4997 -0.3019 0.0209 0.0342 427 PHE A CB 3273 C CG . PHE A 427 ? 0.9619 0.6770 0.5582 -0.2977 0.0249 0.0266 427 PHE A CG 3274 C CD1 . PHE A 427 ? 0.9208 0.6278 0.5225 -0.2940 0.0306 0.0113 427 PHE A CD1 3275 C CD2 . PHE A 427 ? 1.1390 0.8336 0.7562 -0.2984 0.0220 0.0366 427 PHE A CD2 3276 C CE1 . PHE A 427 ? 0.8998 0.5803 0.5290 -0.2925 0.0326 0.0095 427 PHE A CE1 3277 C CE2 . PHE A 427 ? 1.1698 0.8420 0.8122 -0.2964 0.0249 0.0336 427 PHE A CE2 3278 C CZ . PHE A 427 ? 1.0574 0.7232 0.7066 -0.2942 0.0299 0.0219 427 PHE A CZ 3279 N N . GLY A 428 ? 1.1795 0.9649 0.7797 -0.2892 -0.0043 -0.0337 428 GLY A N 3280 C CA . GLY A 428 ? 1.2168 1.0136 0.8331 -0.2813 -0.0127 -0.0690 428 GLY A CA 3281 C C . GLY A 428 ? 1.2903 1.1451 0.8879 -0.2783 -0.0203 -0.0903 428 GLY A C 3282 O O . GLY A 428 ? 1.4142 1.2949 1.0071 -0.2725 -0.0212 -0.1153 428 GLY A O 3283 N N . VAL A 429 ? 1.2116 1.0921 0.7996 -0.2824 -0.0264 -0.0808 429 VAL A N 3284 C CA . VAL A 429 ? 1.3219 1.2695 0.8907 -0.2815 -0.0336 -0.0963 429 VAL A CA 3285 C C . VAL A 429 ? 1.4829 1.4626 1.0175 -0.2914 -0.0256 -0.0653 429 VAL A C 3286 O O . VAL A 429 ? 1.4428 1.4875 0.9586 -0.2939 -0.0308 -0.0687 429 VAL A O 3287 C CB . VAL A 429 ? 1.2524 1.2190 0.8320 -0.2811 -0.0465 -0.1034 429 VAL A CB 3288 C CG1 . VAL A 429 ? 1.3353 1.2864 0.9510 -0.2704 -0.0589 -0.1409 429 VAL A CG1 3289 C CG2 . VAL A 429 ? 1.2074 1.1379 0.7885 -0.2899 -0.0437 -0.0659 429 VAL A CG2 3290 N N . ASP A 430 ? 1.4876 1.4256 1.0176 -0.2973 -0.0146 -0.0347 430 ASP A N 3291 C CA . ASP A 430 ? 1.2252 1.1829 0.7311 -0.3077 -0.0096 -0.0004 430 ASP A CA 3292 C C . ASP A 430 ? 1.0977 1.0880 0.5983 -0.3166 -0.0193 0.0224 430 ASP A C 3293 O O . ASP A 430 ? 1.1296 1.1799 0.6103 -0.3238 -0.0233 0.0340 430 ASP A O 3294 C CB . ASP A 430 ? 1.0953 1.1021 0.5778 -0.3072 -0.0057 -0.0111 430 ASP A CB 3295 C CG . ASP A 430 ? 1.4074 1.3805 0.8953 -0.2994 0.0040 -0.0301 430 ASP A CG 3296 O OD1 . ASP A 430 ? 1.5609 1.5456 1.0299 -0.3023 0.0122 -0.0203 430 ASP A OD1 3297 O OD2 . ASP A 430 ? 1.5608 1.4968 1.0738 -0.2911 0.0023 -0.0528 430 ASP A OD2 3298 N N . ARG A 431 ? 1.0042 0.9588 0.5240 -0.3168 -0.0238 0.0302 431 ARG A N 3299 C CA . ARG A 431 ? 1.0087 0.9882 0.5282 -0.3248 -0.0341 0.0513 431 ARG A CA 3300 C C . ARG A 431 ? 0.9812 0.9079 0.5186 -0.3286 -0.0348 0.0785 431 ARG A C 3301 O O . ARG A 431 ? 0.9449 0.8189 0.4972 -0.3233 -0.0277 0.0747 431 ARG A O 3302 C CB . ARG A 431 ? 1.0677 1.0770 0.5940 -0.3191 -0.0436 0.0221 431 ARG A CB 3303 C CG . ARG A 431 ? 1.1931 1.2770 0.7024 -0.3164 -0.0476 -0.0033 431 ARG A CG 3304 C CD . ARG A 431 ? 1.1910 1.2986 0.7140 -0.3075 -0.0579 -0.0400 431 ARG A CD 3305 N NE . ARG A 431 ? 1.2200 1.4162 0.7269 -0.3062 -0.0643 -0.0612 431 ARG A NE 3306 C CZ . ARG A 431 ? 1.3559 1.5866 0.8587 -0.2969 -0.0635 -0.0967 431 ARG A CZ 3307 N NH1 . ARG A 431 ? 1.4060 1.5846 0.9200 -0.2891 -0.0569 -0.1122 431 ARG A NH1 3308 N NH2 . ARG A 431 ? 1.4409 1.7629 0.9298 -0.2954 -0.0701 -0.1171 431 ARG A NH2 3309 N N . ALA A 432 ? 1.0069 0.9533 0.5449 -0.3380 -0.0445 0.1058 432 ALA A N 3310 C CA . ALA A 432 ? 1.0398 0.9429 0.5986 -0.3407 -0.0486 0.1286 432 ALA A CA 3311 C C . ALA A 432 ? 1.0378 0.9654 0.6024 -0.3458 -0.0615 0.1379 432 ALA A C 3312 O O . ALA A 432 ? 1.0156 0.9994 0.5674 -0.3545 -0.0694 0.1509 432 ALA A O 3313 C CB . ALA A 432 ? 1.1834 1.0742 0.7451 -0.3483 -0.0491 0.1615 432 ALA A CB 3314 N N . ILE A 433 ? 0.9759 0.8662 0.5600 -0.3411 -0.0638 0.1324 433 ILE A N 3315 C CA . ILE A 433 ? 0.9739 0.8834 0.5644 -0.3449 -0.0755 0.1387 433 ILE A CA 3316 C C . ILE A 433 ? 0.9722 0.8506 0.5842 -0.3495 -0.0833 0.1670 433 ILE A C 3317 O O . ILE A 433 ? 0.9607 0.7915 0.5893 -0.3439 -0.0786 0.1663 433 ILE A O 3318 C CB . ILE A 433 ? 1.1179 1.0174 0.7157 -0.3356 -0.0751 0.1062 433 ILE A CB 3319 C CG1 . ILE A 433 ? 1.1343 1.0566 0.7204 -0.3285 -0.0698 0.0730 433 ILE A CG1 3320 C CG2 . ILE A 433 ? 1.0655 0.9942 0.6659 -0.3397 -0.0869 0.1102 433 ILE A CG2 3321 C CD1 . ILE A 433 ? 1.4415 1.3565 1.0416 -0.3196 -0.0736 0.0405 433 ILE A CD1 3322 N N . LEU A 434 ? 0.9841 0.8945 0.5982 -0.3596 -0.0965 0.1912 434 LEU A N 3323 C CA . LEU A 434 ? 0.9854 0.8706 0.6249 -0.3642 -0.1080 0.2179 434 LEU A CA 3324 C C . LEU A 434 ? 1.1787 1.0688 0.8264 -0.3638 -0.1160 0.2134 434 LEU A C 3325 O O . LEU A 434 ? 1.3745 1.3133 1.0113 -0.3710 -0.1232 0.2193 434 LEU A O 3326 C CB . LEU A 434 ? 1.0060 0.9210 0.6497 -0.3786 -0.1206 0.2573 434 LEU A CB 3327 C CG . LEU A 434 ? 1.2134 1.1080 0.8910 -0.3854 -0.1382 0.2898 434 LEU A CG 3328 C CD1 . LEU A 434 ? 1.3295 1.2592 1.0123 -0.3948 -0.1529 0.3072 434 LEU A CD1 3329 C CD2 . LEU A 434 ? 1.2292 1.0617 0.9322 -0.3731 -0.1354 0.2750 434 LEU A CD2 3330 N N . TYR A 435 ? 1.0507 0.8952 0.7176 -0.3555 -0.1146 0.2028 435 TYR A N 3331 C CA . TYR A 435 ? 1.0391 0.8828 0.7160 -0.3547 -0.1222 0.1995 435 TYR A CA 3332 C C . TYR A 435 ? 1.0402 0.8720 0.7429 -0.3606 -0.1373 0.2285 435 TYR A C 3333 O O . TYR A 435 ? 1.2112 1.0119 0.9341 -0.3583 -0.1394 0.2378 435 TYR A O 3334 C CB . TYR A 435 ? 1.0417 0.8495 0.7261 -0.3429 -0.1135 0.1716 435 TYR A CB 3335 C CG . TYR A 435 ? 1.1629 0.9791 0.8311 -0.3370 -0.1029 0.1427 435 TYR A CG 3336 C CD1 . TYR A 435 ? 1.1423 0.9399 0.8070 -0.3321 -0.0913 0.1327 435 TYR A CD1 3337 C CD2 . TYR A 435 ? 1.1640 1.0073 0.8241 -0.3359 -0.1062 0.1242 435 TYR A CD2 3338 C CE1 . TYR A 435 ? 1.0182 0.8220 0.6737 -0.3267 -0.0843 0.1064 435 TYR A CE1 3339 C CE2 . TYR A 435 ? 1.0900 0.9401 0.7431 -0.3294 -0.1002 0.0950 435 TYR A CE2 3340 C CZ . TYR A 435 ? 1.0450 0.8742 0.6968 -0.3251 -0.0898 0.0869 435 TYR A CZ 3341 O OH . TYR A 435 ? 1.0389 0.8736 0.6892 -0.3186 -0.0865 0.0580 435 TYR A OH 3342 N N . ARG A 436 ? 1.0447 0.9030 0.7499 -0.3677 -0.1491 0.2411 436 ARG A N 3343 C CA . ARG A 436 ? 1.0503 0.8999 0.7843 -0.3742 -0.1666 0.2697 436 ARG A CA 3344 C C . ARG A 436 ? 1.0841 0.9092 0.8338 -0.3673 -0.1700 0.2578 436 ARG A C 3345 O O . ARG A 436 ? 1.3181 1.1561 1.0529 -0.3645 -0.1651 0.2396 436 ARG A O 3346 C CB . ARG A 436 ? 1.0740 0.9775 0.8039 -0.3904 -0.1805 0.3017 436 ARG A CB 3347 C CG . ARG A 436 ? 1.0835 1.0216 0.7984 -0.3994 -0.1792 0.3182 436 ARG A CG 3348 C CD . ARG A 436 ? 1.0836 1.0819 0.8006 -0.4178 -0.1959 0.3567 436 ARG A CD 3349 N NE . ARG A 436 ? 1.1068 1.1494 0.8068 -0.4199 -0.1958 0.3468 436 ARG A NE 3350 C CZ . ARG A 436 ? 1.2339 1.3314 0.9382 -0.4351 -0.2109 0.3778 436 ARG A CZ 3351 N NH1 . ARG A 436 ? 1.2983 1.4113 1.0263 -0.4508 -0.2288 0.4240 436 ARG A NH1 3352 N NH2 . ARG A 436 ? 1.3332 1.4720 1.0215 -0.4351 -0.2094 0.3636 436 ARG A NH2 3353 N N . ALA A 437 ? 1.0112 0.8030 0.7935 -0.3640 -0.1797 0.2666 437 ALA A N 3354 C CA . ALA A 437 ? 1.0193 0.7905 0.8192 -0.3573 -0.1842 0.2564 437 ALA A CA 3355 C C . ALA A 437 ? 1.2447 1.0417 1.0498 -0.3672 -0.1993 0.2764 437 ALA A C 3356 O O . ALA A 437 ? 1.4446 1.2732 1.2499 -0.3803 -0.2105 0.3048 437 ALA A O 3357 C CB . ALA A 437 ? 0.9895 0.7246 0.8252 -0.3490 -0.1910 0.2553 437 ALA A CB 3358 N N . ARG A 438 ? 1.1547 0.9416 0.9652 -0.3617 -0.2002 0.2634 438 ARG A N 3359 C CA . ARG A 438 ? 1.0670 0.8772 0.8817 -0.3700 -0.2132 0.2793 438 ARG A CA 3360 C C . ARG A 438 ? 1.0510 0.8338 0.9042 -0.3667 -0.2287 0.2876 438 ARG A C 3361 O O . ARG A 438 ? 1.1440 0.8939 1.0140 -0.3546 -0.2252 0.2697 438 ARG A O 3362 C CB . ARG A 438 ? 1.0728 0.8990 0.8617 -0.3668 -0.2029 0.2562 438 ARG A CB 3363 C CG . ARG A 438 ? 1.1024 0.9620 0.8589 -0.3691 -0.1914 0.2446 438 ARG A CG 3364 C CD . ARG A 438 ? 1.3050 1.1614 1.0461 -0.3600 -0.1799 0.2107 438 ARG A CD 3365 N NE . ARG A 438 ? 1.3114 1.1881 1.0510 -0.3623 -0.1867 0.2081 438 ARG A NE 3366 C CZ . ARG A 438 ? 1.2013 1.0800 0.9328 -0.3560 -0.1817 0.1810 438 ARG A CZ 3367 N NH1 . ARG A 438 ? 1.1888 1.0500 0.9155 -0.3476 -0.1709 0.1561 438 ARG A NH1 3368 N NH2 . ARG A 438 ? 1.1790 1.0771 0.9106 -0.3583 -0.1889 0.1798 438 ARG A NH2 3369 N N . PRO A 439 ? 1.0587 0.8601 0.9281 -0.3774 -0.2471 0.3146 439 PRO A N 3370 C CA . PRO A 439 ? 1.0851 0.8643 0.9980 -0.3760 -0.2671 0.3269 439 PRO A CA 3371 C C . PRO A 439 ? 1.0760 0.8273 1.0004 -0.3618 -0.2639 0.3000 439 PRO A C 3372 O O . PRO A 439 ? 1.3192 1.0498 1.2836 -0.3569 -0.2798 0.3030 439 PRO A O 3373 C CB . PRO A 439 ? 1.4042 1.2197 1.3211 -0.3922 -0.2835 0.3597 439 PRO A CB 3374 C CG . PRO A 439 ? 1.3894 1.2471 1.2778 -0.4043 -0.2776 0.3752 439 PRO A CG 3375 C CD . PRO A 439 ? 1.2086 1.0607 1.0597 -0.3932 -0.2522 0.3391 439 PRO A CD 3376 N N . VAL A 440 ? 1.0748 0.8285 0.9696 -0.3557 -0.2464 0.2751 440 VAL A N 3377 C CA . VAL A 440 ? 1.0901 0.8236 0.9949 -0.3435 -0.2429 0.2518 440 VAL A CA 3378 C C . VAL A 440 ? 1.2381 0.9705 1.1699 -0.3451 -0.2612 0.2632 440 VAL A C 3379 O O . VAL A 440 ? 1.2780 0.9919 1.2471 -0.3383 -0.2742 0.2620 440 VAL A O 3380 C CB . VAL A 440 ? 1.4524 1.1608 1.3766 -0.3303 -0.2380 0.2330 440 VAL A CB 3381 C CG1 . VAL A 440 ? 1.2565 0.9576 1.1841 -0.3191 -0.2310 0.2088 440 VAL A CG1 3382 C CG2 . VAL A 440 ? 1.6780 1.3863 1.5799 -0.3296 -0.2218 0.2255 440 VAL A CG2 3383 N N . ILE A 441 ? 1.3184 1.0730 1.2337 -0.3538 -0.2636 0.2730 441 ILE A N 3384 C CA . ILE A 441 ? 1.2675 1.0225 1.2054 -0.3559 -0.2797 0.2836 441 ILE A CA 3385 C C . ILE A 441 ? 1.2231 0.9627 1.1627 -0.3436 -0.2733 0.2575 441 ILE A C 3386 O O . ILE A 441 ? 1.2142 0.9585 1.1259 -0.3407 -0.2575 0.2395 441 ILE A O 3387 C CB . ILE A 441 ? 1.2184 1.0092 1.1378 -0.3702 -0.2844 0.3042 441 ILE A CB 3388 C CG1 . ILE A 441 ? 1.3946 1.2130 1.3107 -0.3842 -0.2907 0.3329 441 ILE A CG1 3389 C CG2 . ILE A 441 ? 1.1796 0.9702 1.1247 -0.3732 -0.3022 0.3178 441 ILE A CG2 3390 C CD1 . ILE A 441 ? 1.4844 1.3519 1.3815 -0.3989 -0.2948 0.3532 441 ILE A CD1 3391 N N . THR A 442 ? 1.1827 0.9068 1.1586 -0.3367 -0.2873 0.2556 442 THR A N 3392 C CA . THR A 442 ? 1.1597 0.8773 1.1397 -0.3260 -0.2834 0.2336 442 THR A CA 3393 C C . THR A 442 ? 1.1858 0.9111 1.1739 -0.3313 -0.2964 0.2455 442 THR A C 3394 O O . THR A 442 ? 1.1902 0.9107 1.2134 -0.3329 -0.3169 0.2600 442 THR A O 3395 C CB . THR A 442 ? 1.2173 0.9201 1.2326 -0.3115 -0.2888 0.2154 442 THR A CB 3396 O OG1 . THR A 442 ? 1.4548 1.1498 1.5136 -0.3119 -0.3133 0.2291 442 THR A OG1 3397 C CG2 . THR A 442 ? 1.1974 0.8949 1.2059 -0.3064 -0.2760 0.2042 442 THR A CG2 3398 N N . VAL A 443 ? 1.2379 0.9749 1.1970 -0.3339 -0.2861 0.2392 443 VAL A N 3399 C CA . VAL A 443 ? 1.2092 0.9567 1.1708 -0.3398 -0.2964 0.2504 443 VAL A CA 3400 C C . VAL A 443 ? 1.1984 0.9375 1.1714 -0.3294 -0.2969 0.2322 443 VAL A C 3401 O O . VAL A 443 ? 1.3099 1.0482 1.2670 -0.3229 -0.2828 0.2124 443 VAL A O 3402 C CB . VAL A 443 ? 1.3232 1.0953 1.2479 -0.3498 -0.2875 0.2550 443 VAL A CB 3403 C CG1 . VAL A 443 ? 1.5161 1.2865 1.4137 -0.3442 -0.2681 0.2310 443 VAL A CG1 3404 C CG2 . VAL A 443 ? 1.3127 1.0961 1.2377 -0.3538 -0.2952 0.2608 443 VAL A CG2 3405 N N . ASN A 444 ? 1.2179 0.9534 1.2217 -0.3284 -0.3150 0.2406 444 ASN A N 3406 C CA . ASN A 444 ? 1.3000 1.0331 1.3162 -0.3190 -0.3176 0.2247 444 ASN A CA 3407 C C . ASN A 444 ? 1.2933 1.0373 1.2979 -0.3272 -0.3221 0.2362 444 ASN A C 3408 O O . ASN A 444 ? 1.2366 0.9849 1.2567 -0.3356 -0.3380 0.2583 444 ASN A O 3409 C CB . ASN A 444 ? 1.5186 1.2414 1.5828 -0.3088 -0.3358 0.2189 444 ASN A CB 3410 C CG . ASN A 444 ? 1.6325 1.3605 1.7086 -0.2952 -0.3345 0.1939 444 ASN A CG 3411 O OD1 . ASN A 444 ? 1.6327 1.3701 1.6855 -0.2964 -0.3250 0.1890 444 ASN A OD1 3412 N ND2 . ASN A 444 ? 1.6551 1.3813 1.7701 -0.2820 -0.3454 0.1772 444 ASN A ND2 3413 N N . ALA A 445 ? 1.4507 1.2011 1.4308 -0.3253 -0.3095 0.2226 445 ALA A N 3414 C CA . ALA A 445 ? 1.4348 1.1966 1.4017 -0.3324 -0.3124 0.2305 445 ALA A CA 3415 C C . ALA A 445 ? 1.2065 0.9664 1.1848 -0.3242 -0.3151 0.2175 445 ALA A C 3416 O O . ALA A 445 ? 1.1763 0.9332 1.1629 -0.3137 -0.3097 0.1995 445 ALA A O 3417 C CB . ALA A 445 ? 1.4892 1.2637 1.4196 -0.3387 -0.2982 0.2264 445 ALA A CB 3418 N N . GLY A 446 ? 1.2083 0.9752 1.1869 -0.3294 -0.3236 0.2274 446 GLY A N 3419 C CA . GLY A 446 ? 1.4193 1.1873 1.4065 -0.3227 -0.3266 0.2166 446 GLY A CA 3420 C C . GLY A 446 ? 1.4538 1.2324 1.4241 -0.3311 -0.3281 0.2254 446 GLY A C 3421 O O . GLY A 446 ? 1.2342 1.0225 1.1963 -0.3418 -0.3326 0.2431 446 GLY A O 3422 N N . LEU A 447 ? 1.5019 1.2835 1.4682 -0.3265 -0.3249 0.2137 447 LEU A N 3423 C CA . LEU A 447 ? 1.3281 1.1194 1.2786 -0.3332 -0.3257 0.2186 447 LEU A CA 3424 C C . LEU A 447 ? 1.3336 1.1259 1.2996 -0.3274 -0.3333 0.2141 447 LEU A C 3425 O O . LEU A 447 ? 1.2785 1.0724 1.2507 -0.3189 -0.3292 0.1997 447 LEU A O 3426 C CB . LEU A 447 ? 1.1797 0.9760 1.1040 -0.3356 -0.3126 0.2078 447 LEU A CB 3427 C CG . LEU A 447 ? 1.1959 1.0028 1.1064 -0.3408 -0.3136 0.2075 447 LEU A CG 3428 C CD1 . LEU A 447 ? 1.1096 0.9322 1.0121 -0.3505 -0.3197 0.2227 447 LEU A CD1 3429 C CD2 . LEU A 447 ? 1.2166 1.0247 1.1124 -0.3410 -0.3042 0.1932 447 LEU A CD2 3430 N N . GLU A 448 ? 1.3648 1.1610 1.3378 -0.3325 -0.3449 0.2274 448 GLU A N 3431 C CA . GLU A 448 ? 1.3512 1.1496 1.3382 -0.3272 -0.3527 0.2231 448 GLU A CA 3432 C C . GLU A 448 ? 1.3899 1.1978 1.3583 -0.3355 -0.3527 0.2305 448 GLU A C 3433 O O . GLU A 448 ? 1.3767 1.1915 1.3427 -0.3449 -0.3593 0.2476 448 GLU A O 3434 C CB . GLU A 448 ? 1.4667 1.2593 1.4904 -0.3232 -0.3709 0.2298 448 GLU A CB 3435 C CG . GLU A 448 ? 1.5982 1.3954 1.6387 -0.3170 -0.3806 0.2237 448 GLU A CG 3436 C CD . GLU A 448 ? 1.7233 1.5138 1.8061 -0.3133 -0.4024 0.2300 448 GLU A CD 3437 O OE1 . GLU A 448 ? 1.8577 1.6391 1.9586 -0.3164 -0.4108 0.2415 448 GLU A OE1 3438 O OE2 . GLU A 448 ? 1.6172 1.4120 1.7182 -0.3073 -0.4127 0.2239 448 GLU A OE2 3439 N N . VAL A 449 ? 1.5517 1.3639 1.5089 -0.3328 -0.3462 0.2190 449 VAL A N 3440 C CA . VAL A 449 ? 1.6097 1.4306 1.5532 -0.3394 -0.3479 0.2242 449 VAL A CA 3441 C C . VAL A 449 ? 1.7151 1.5373 1.6775 -0.3352 -0.3593 0.2268 449 VAL A C 3442 O O . VAL A 449 ? 1.6668 1.4892 1.6455 -0.3254 -0.3612 0.2157 449 VAL A O 3443 C CB . VAL A 449 ? 1.6390 1.4634 1.5638 -0.3403 -0.3380 0.2123 449 VAL A CB 3444 C CG1 . VAL A 449 ? 1.6205 1.4457 1.5554 -0.3329 -0.3363 0.2026 449 VAL A CG1 3445 C CG2 . VAL A 449 ? 1.6360 1.4710 1.5461 -0.3479 -0.3401 0.2157 449 VAL A CG2 3446 N N . TYR A 450 ? 1.9108 1.7386 1.8724 -0.3429 -0.3676 0.2414 450 TYR A N 3447 C CA . TYR A 450 ? 1.9532 1.7835 1.9294 -0.3418 -0.3792 0.2468 450 TYR A CA 3448 C C . TYR A 450 ? 2.0208 1.8575 1.9816 -0.3401 -0.3729 0.2362 450 TYR A C 3449 O O . TYR A 450 ? 2.1155 1.9524 2.0627 -0.3388 -0.3623 0.2253 450 TYR A O 3450 C CB . TYR A 450 ? 1.8862 1.7247 1.8651 -0.3533 -0.3891 0.2700 450 TYR A CB 3451 C CG . TYR A 450 ? 1.8727 1.7032 1.8840 -0.3532 -0.4033 0.2832 450 TYR A CG 3452 C CD1 . TYR A 450 ? 1.8778 1.6945 1.9174 -0.3404 -0.4096 0.2695 450 TYR A CD1 3453 C CD2 . TYR A 450 ? 1.9475 1.7885 1.9647 -0.3657 -0.4120 0.3090 450 TYR A CD2 3454 C CE1 . TYR A 450 ? 1.9504 1.7577 2.0267 -0.3386 -0.4256 0.2781 450 TYR A CE1 3455 C CE2 . TYR A 450 ? 2.0797 1.9115 2.1344 -0.3663 -0.4288 0.3237 450 TYR A CE2 3456 C CZ . TYR A 450 ? 2.1222 1.9338 2.2077 -0.3521 -0.4361 0.3067 450 TYR A CZ 3457 O OH . TYR A 450 ? 2.2255 2.0264 2.3541 -0.3516 -0.4555 0.3184 450 TYR A OH 3458 N N . PRO A 451 ? 1.8013 1.6437 1.7650 -0.3414 -0.3802 0.2408 451 PRO A N 3459 C CA . PRO A 451 ? 1.6970 1.5450 1.6601 -0.3354 -0.3782 0.2292 451 PRO A CA 3460 C C . PRO A 451 ? 1.6196 1.4703 1.5658 -0.3362 -0.3665 0.2196 451 PRO A C 3461 O O . PRO A 451 ? 1.9006 1.7535 1.8304 -0.3427 -0.3630 0.2200 451 PRO A O 3462 C CB . PRO A 451 ? 1.7534 1.6074 1.7112 -0.3410 -0.3845 0.2382 451 PRO A CB 3463 C CG . PRO A 451 ? 1.7736 1.6282 1.7330 -0.3495 -0.3909 0.2551 451 PRO A CG 3464 C CD . PRO A 451 ? 1.7850 1.6317 1.7568 -0.3481 -0.3920 0.2579 451 PRO A CD 3465 N N . SER A 452 ? 1.4132 1.2645 1.3681 -0.3294 -0.3620 0.2107 452 SER A N 3466 C CA . SER A 452 ? 1.3067 1.1634 1.2555 -0.3293 -0.3537 0.2039 452 SER A CA 3467 C C . SER A 452 ? 1.4844 1.3509 1.4285 -0.3329 -0.3554 0.2055 452 SER A C 3468 O O . SER A 452 ? 1.6243 1.4858 1.5576 -0.3396 -0.3532 0.2060 452 SER A O 3469 C CB . SER A 452 ? 1.2905 1.1590 1.2560 -0.3199 -0.3522 0.1955 452 SER A CB 3470 O OG . SER A 452 ? 1.4710 1.3456 1.4327 -0.3217 -0.3443 0.1929 452 SER A OG 3471 N N . ILE A 453 ? 1.4117 1.2938 1.3663 -0.3284 -0.3609 0.2051 453 ILE A N 3472 C CA . ILE A 453 ? 1.1580 1.0508 1.1091 -0.3329 -0.3636 0.2092 453 ILE A CA 3473 C C . ILE A 453 ? 1.1367 1.0177 1.0756 -0.3392 -0.3673 0.2144 453 ILE A C 3474 O O . ILE A 453 ? 1.1103 0.9895 1.0515 -0.3376 -0.3726 0.2176 453 ILE A O 3475 C CB . ILE A 453 ? 1.1688 1.0884 1.1332 -0.3266 -0.3686 0.2076 453 ILE A CB 3476 C CG1 . ILE A 453 ? 1.1367 1.0789 1.1147 -0.3194 -0.3652 0.2004 453 ILE A CG1 3477 C CG2 . ILE A 453 ? 1.3966 1.3292 1.3580 -0.3331 -0.3718 0.2152 453 ILE A CG2 3478 C CD1 . ILE A 453 ? 1.1493 1.1299 1.1424 -0.3114 -0.3704 0.1946 453 ILE A CD1 3479 N N . LEU A 454 ? 1.1277 1.0038 1.0575 -0.3462 -0.3663 0.2146 454 LEU A N 3480 C CA . LEU A 454 ? 1.1493 1.0204 1.0671 -0.3519 -0.3689 0.2159 454 LEU A CA 3481 C C . LEU A 454 ? 1.2592 1.1380 1.1778 -0.3547 -0.3751 0.2192 454 LEU A C 3482 O O . LEU A 454 ? 1.4529 1.3357 1.3784 -0.3568 -0.3774 0.2192 454 LEU A O 3483 C CB . LEU A 454 ? 1.1177 0.9825 1.0280 -0.3562 -0.3655 0.2082 454 LEU A CB 3484 C CG . LEU A 454 ? 1.1326 0.9918 1.0382 -0.3550 -0.3592 0.2052 454 LEU A CG 3485 C CD1 . LEU A 454 ? 1.1594 1.0185 1.0590 -0.3583 -0.3574 0.1938 454 LEU A CD1 3486 C CD2 . LEU A 454 ? 1.1497 1.0121 1.0506 -0.3559 -0.3606 0.2138 454 LEU A CD2 3487 N N . ASN A 455 ? 1.1835 1.0652 1.0974 -0.3555 -0.3793 0.2243 455 ASN A N 3488 C CA . ASN A 455 ? 1.1993 1.0880 1.1123 -0.3584 -0.3850 0.2275 455 ASN A CA 3489 C C . ASN A 455 ? 1.2338 1.1218 1.1367 -0.3647 -0.3864 0.2231 455 ASN A C 3490 O O . ASN A 455 ? 1.2716 1.1632 1.1648 -0.3673 -0.3855 0.2239 455 ASN A O 3491 C CB . ASN A 455 ? 1.2011 1.0954 1.1168 -0.3555 -0.3899 0.2343 455 ASN A CB 3492 C CG . ASN A 455 ? 1.2028 1.1054 1.1167 -0.3582 -0.3954 0.2379 455 ASN A CG 3493 O OD1 . ASN A 455 ? 1.3533 1.2559 1.2579 -0.3633 -0.3977 0.2402 455 ASN A OD1 3494 N ND2 . ASN A 455 ? 1.2221 1.1366 1.1450 -0.3553 -0.3978 0.2390 455 ASN A ND2 3495 N N . GLN A 456 ? 1.2578 1.1456 1.1666 -0.3674 -0.3902 0.2186 456 GLN A N 3496 C CA . GLN A 456 ? 1.3073 1.1971 1.2131 -0.3714 -0.3940 0.2086 456 GLN A CA 3497 C C . GLN A 456 ? 1.3442 1.2449 1.2386 -0.3740 -0.3964 0.2116 456 GLN A C 3498 O O . GLN A 456 ? 1.3453 1.2571 1.2316 -0.3763 -0.3964 0.2030 456 GLN A O 3499 C CB . GLN A 456 ? 1.3099 1.1963 1.2329 -0.3739 -0.4025 0.2059 456 GLN A CB 3500 C CG . GLN A 456 ? 1.2944 1.1722 1.2325 -0.3737 -0.4031 0.2006 456 GLN A CG 3501 C CD . GLN A 456 ? 1.3874 1.2626 1.3282 -0.3735 -0.4053 0.1809 456 GLN A CD 3502 O OE1 . GLN A 456 ? 1.6289 1.5132 1.5533 -0.3722 -0.4003 0.1722 456 GLN A OE1 3503 N NE2 . GLN A 456 ? 1.2760 1.1434 1.2408 -0.3749 -0.4146 0.1740 456 GLN A NE2 3504 N N . ASP A 457 ? 1.4310 1.3336 1.3259 -0.3733 -0.3988 0.2232 457 ASP A N 3505 C CA . ASP A 457 ? 1.5006 1.4132 1.3872 -0.3763 -0.4023 0.2280 457 ASP A CA 3506 C C . ASP A 457 ? 1.6540 1.5718 1.5344 -0.3766 -0.4003 0.2384 457 ASP A C 3507 O O . ASP A 457 ? 1.7756 1.7032 1.6514 -0.3798 -0.4039 0.2461 457 ASP A O 3508 C CB . ASP A 457 ? 1.4669 1.3804 1.3594 -0.3760 -0.4079 0.2351 457 ASP A CB 3509 C CG . ASP A 457 ? 1.6866 1.6089 1.5730 -0.3803 -0.4129 0.2347 457 ASP A CG 3510 O OD1 . ASP A 457 ? 1.8053 1.7349 1.6840 -0.3814 -0.4132 0.2428 457 ASP A OD1 3511 O OD2 . ASP A 457 ? 1.7356 1.6578 1.6279 -0.3826 -0.4180 0.2262 457 ASP A OD2 3512 N N . ASN A 458 ? 1.6396 1.5514 1.5231 -0.3740 -0.3963 0.2401 458 ASN A N 3513 C CA . ASN A 458 ? 1.6527 1.5689 1.5372 -0.3756 -0.3979 0.2524 458 ASN A CA 3514 C C . ASN A 458 ? 1.6696 1.6007 1.5440 -0.3815 -0.3945 0.2518 458 ASN A C 3515 O O . ASN A 458 ? 1.8169 1.7442 1.6907 -0.3801 -0.3895 0.2460 458 ASN A O 3516 C CB . ASN A 458 ? 1.7182 1.6216 1.6173 -0.3688 -0.3983 0.2551 458 ASN A CB 3517 C CG . ASN A 458 ? 1.8054 1.7103 1.7133 -0.3710 -0.4029 0.2684 458 ASN A CG 3518 O OD1 . ASN A 458 ? 1.7532 1.6702 1.6598 -0.3779 -0.4082 0.2814 458 ASN A OD1 3519 N ND2 . ASN A 458 ? 2.0382 1.9326 1.9580 -0.3659 -0.4022 0.2669 458 ASN A ND2 3520 N N . LYS A 459 ? 1.6038 1.5571 1.4706 -0.3883 -0.3975 0.2583 459 LYS A N 3521 C CA . LYS A 459 ? 1.5973 1.5805 1.4526 -0.3945 -0.3950 0.2549 459 LYS A CA 3522 C C . LYS A 459 ? 1.7385 1.7414 1.5960 -0.4019 -0.3975 0.2765 459 LYS A C 3523 O O . LYS A 459 ? 1.7283 1.7691 1.5766 -0.4092 -0.3969 0.2792 459 LYS A O 3524 C CB . LYS A 459 ? 1.5629 1.5685 1.4099 -0.3977 -0.3972 0.2465 459 LYS A CB 3525 C CG . LYS A 459 ? 1.5161 1.5056 1.3660 -0.3919 -0.3974 0.2248 459 LYS A CG 3526 C CD . LYS A 459 ? 1.5936 1.5985 1.4405 -0.3939 -0.4021 0.2176 459 LYS A CD 3527 C CE . LYS A 459 ? 1.4961 1.4795 1.3538 -0.3891 -0.4060 0.2020 459 LYS A CE 3528 N NZ . LYS A 459 ? 1.4445 1.4399 1.3027 -0.3907 -0.4123 0.1952 459 LYS A NZ 3529 N N . THR A 460 ? 1.8175 1.7992 1.6908 -0.4000 -0.4022 0.2917 460 THR A N 3530 C CA . THR A 460 ? 1.7772 1.7718 1.6635 -0.4080 -0.4110 0.3186 460 THR A CA 3531 C C . THR A 460 ? 1.7151 1.7493 1.5942 -0.4187 -0.4102 0.3308 460 THR A C 3532 O O . THR A 460 ? 1.8369 1.9074 1.7135 -0.4290 -0.4149 0.3471 460 THR A O 3533 C CB . THR A 460 ? 1.7539 1.7181 1.6639 -0.4018 -0.4167 0.3253 460 THR A CB 3534 O OG1 . THR A 460 ? 1.7979 1.7365 1.7170 -0.3917 -0.4188 0.3145 460 THR A OG1 3535 C CG2 . THR A 460 ? 1.7196 1.6944 1.6521 -0.4106 -0.4305 0.3549 460 THR A CG2 3536 N N . CYS A 461 ? 1.6648 1.6969 1.5409 -0.4169 -0.4044 0.3240 461 CYS A N 3537 C CA . CYS A 461 ? 1.7314 1.8055 1.6018 -0.4271 -0.4040 0.3367 461 CYS A CA 3538 C C . CYS A 461 ? 1.7809 1.8871 1.6286 -0.4261 -0.3942 0.3114 461 CYS A C 3539 O O . CYS A 461 ? 1.9291 2.0151 1.7711 -0.4172 -0.3867 0.2869 461 CYS A O 3540 C CB . CYS A 461 ? 1.8212 1.8771 1.7051 -0.4264 -0.4055 0.3467 461 CYS A CB 3541 S SG . CYS A 461 ? 3.1363 3.1294 3.0362 -0.4111 -0.4050 0.3318 461 CYS A SG 3542 N N . SER A 462 ? 1.7471 1.9071 1.5854 -0.4349 -0.3959 0.3166 462 SER A N 3543 C CA . SER A 462 ? 1.7909 1.9957 1.6123 -0.4341 -0.3894 0.2914 462 SER A CA 3544 C C . SER A 462 ? 1.8110 2.0895 1.6276 -0.4480 -0.3924 0.3124 462 SER A C 3545 O O . SER A 462 ? 1.8423 2.1503 1.6626 -0.4580 -0.3992 0.3362 462 SER A O 3546 C CB . SER A 462 ? 1.8969 2.1020 1.7117 -0.4276 -0.3884 0.2645 462 SER A CB 3547 O OG . SER A 462 ? 2.0554 2.2901 1.8696 -0.4358 -0.3940 0.2816 462 SER A OG 3548 N N . LEU A 463 ? 1.9379 2.2501 1.7474 -0.4493 -0.3880 0.3052 463 LEU A N 3549 C CA . LEU A 463 ? 2.0239 2.4239 1.8249 -0.4610 -0.3892 0.3151 463 LEU A CA 3550 C C . LEU A 463 ? 2.0050 2.4419 1.7924 -0.4528 -0.3815 0.2752 463 LEU A C 3551 O O . LEU A 463 ? 1.9892 2.4704 1.7725 -0.4585 -0.3800 0.2826 463 LEU A O 3552 C CB . LEU A 463 ? 1.9708 2.3917 1.7833 -0.4760 -0.3961 0.3608 463 LEU A CB 3553 C CG . LEU A 463 ? 1.8910 2.3846 1.7091 -0.4950 -0.4057 0.4005 463 LEU A CG 3554 C CD1 . LEU A 463 ? 1.9307 2.4430 1.7653 -0.5097 -0.4143 0.4445 463 LEU A CD1 3555 C CD2 . LEU A 463 ? 1.7806 2.3669 1.5800 -0.4979 -0.4012 0.3804 463 LEU A CD2 3556 N N . PRO A 464 ? 1.8995 2.3209 1.6835 -0.4395 -0.3786 0.2328 464 PRO A N 3557 C CA . PRO A 464 ? 1.8395 2.2979 1.6175 -0.4306 -0.3747 0.1915 464 PRO A CA 3558 C C . PRO A 464 ? 1.8545 2.4068 1.6255 -0.4326 -0.3768 0.1709 464 PRO A C 3559 O O . PRO A 464 ? 1.9740 2.5254 1.7491 -0.4222 -0.3792 0.1342 464 PRO A O 3560 C CB . PRO A 464 ? 1.8624 2.2492 1.6493 -0.4153 -0.3741 0.1579 464 PRO A CB 3561 C CG . PRO A 464 ? 1.8602 2.2130 1.6517 -0.4168 -0.3782 0.1714 464 PRO A CG 3562 C CD . PRO A 464 ? 1.8577 2.2240 1.6475 -0.4313 -0.3804 0.2194 464 PRO A CD 3563 N N . GLY A 465 ? 1.7998 2.4359 1.5631 -0.4456 -0.3773 0.1934 465 GLY A N 3564 C CA . GLY A 465 ? 1.8442 2.5819 1.6010 -0.4455 -0.3787 0.1669 465 GLY A CA 3565 C C . GLY A 465 ? 1.8283 2.5911 1.5857 -0.4476 -0.3830 0.1649 465 GLY A C 3566 O O . GLY A 465 ? 1.7405 2.5040 1.5025 -0.4342 -0.3849 0.1193 465 GLY A O 3567 N N . THR A 466 ? 1.8580 2.6368 1.6148 -0.4642 -0.3863 0.2142 466 THR A N 3568 C CA . THR A 466 ? 1.8742 2.6541 1.6328 -0.4673 -0.3903 0.2214 466 THR A CA 3569 C C . THR A 466 ? 1.8933 2.5617 1.6598 -0.4555 -0.3904 0.2100 466 THR A C 3570 O O . THR A 466 ? 1.8591 2.5071 1.6287 -0.4420 -0.3910 0.1687 466 THR A O 3571 C CB . THR A 466 ? 1.7705 2.6419 1.5242 -0.4626 -0.3914 0.1824 466 THR A CB 3572 O OG1 . THR A 466 ? 1.6605 2.6442 1.4067 -0.4712 -0.3906 0.1855 466 THR A OG1 3573 C CG2 . THR A 466 ? 1.7304 2.6170 1.4845 -0.4705 -0.3955 0.2016 466 THR A CG2 3574 N N . ALA A 467 ? 1.8986 2.5001 1.6714 -0.4614 -0.3915 0.2484 467 ALA A N 3575 C CA . ALA A 467 ? 1.8410 2.3389 1.6220 -0.4516 -0.3908 0.2450 467 ALA A CA 3576 C C . ALA A 467 ? 1.7737 2.2325 1.5577 -0.4435 -0.3929 0.2262 467 ALA A C 3577 O O . ALA A 467 ? 1.6792 2.1702 1.4613 -0.4497 -0.3964 0.2363 467 ALA A O 3578 C CB . ALA A 467 ? 1.8437 2.3023 1.6345 -0.4617 -0.3947 0.2929 467 ALA A CB 3579 N N . LEU A 468 ? 1.7838 2.1757 1.5738 -0.4303 -0.3912 0.2006 468 LEU A N 3580 C CA . LEU A 468 ? 1.6756 2.0120 1.4722 -0.4235 -0.3941 0.1921 468 LEU A CA 3581 C C . LEU A 468 ? 1.6112 1.8691 1.4158 -0.4191 -0.3926 0.2043 468 LEU A C 3582 O O . LEU A 468 ? 1.6792 1.9180 1.4858 -0.4144 -0.3889 0.1953 468 LEU A O 3583 C CB . LEU A 468 ? 1.6793 2.0220 1.4815 -0.4121 -0.3968 0.1460 468 LEU A CB 3584 C CG . LEU A 468 ? 1.7647 2.1912 1.5627 -0.4129 -0.3994 0.1227 468 LEU A CG 3585 C CD1 . LEU A 468 ? 1.8621 2.2828 1.6749 -0.3991 -0.4057 0.0733 468 LEU A CD1 3586 C CD2 . LEU A 468 ? 1.6586 2.1164 1.4499 -0.4229 -0.4014 0.1473 468 LEU A CD2 3587 N N . LYS A 469 ? 1.6526 1.8696 1.4621 -0.4199 -0.3955 0.2224 469 LYS A N 3588 C CA . LYS A 469 ? 1.7163 1.8711 1.5346 -0.4161 -0.3950 0.2364 469 LYS A CA 3589 C C . LYS A 469 ? 1.6311 1.7475 1.4547 -0.4058 -0.3916 0.2121 469 LYS A C 3590 O O . LYS A 469 ? 1.6868 1.7961 1.5145 -0.3997 -0.3936 0.1866 469 LYS A O 3591 C CB . LYS A 469 ? 1.8287 1.9538 1.6523 -0.4159 -0.3996 0.2490 469 LYS A CB 3592 C CG . LYS A 469 ? 1.7830 1.9283 1.6089 -0.4261 -0.4048 0.2818 469 LYS A CG 3593 C CD . LYS A 469 ? 1.6566 1.7868 1.4938 -0.4296 -0.4071 0.3070 469 LYS A CD 3594 C CE . LYS A 469 ? 1.5803 1.7264 1.4289 -0.4402 -0.4167 0.3418 469 LYS A CE 3595 N NZ . LYS A 469 ? 1.5250 1.6532 1.3930 -0.4431 -0.4230 0.3657 469 LYS A NZ 3596 N N . VAL A 470 ? 1.5309 1.6238 1.3579 -0.4046 -0.3881 0.2216 470 VAL A N 3597 C CA . VAL A 470 ? 1.5164 1.5762 1.3494 -0.3963 -0.3847 0.2029 470 VAL A CA 3598 C C . VAL A 470 ? 1.4906 1.5117 1.3308 -0.3942 -0.3825 0.2200 470 VAL A C 3599 O O . VAL A 470 ? 1.5069 1.5332 1.3487 -0.3992 -0.3837 0.2430 470 VAL A O 3600 C CB . VAL A 470 ? 1.2867 1.3774 1.1148 -0.3950 -0.3814 0.1822 470 VAL A CB 3601 C CG1 . VAL A 470 ? 1.2128 1.3233 1.0350 -0.4011 -0.3776 0.2021 470 VAL A CG1 3602 C CG2 . VAL A 470 ? 1.2081 1.2665 1.0467 -0.3862 -0.3807 0.1584 470 VAL A CG2 3603 N N . SER A 471 ? 1.4872 1.4731 1.3357 -0.3870 -0.3811 0.2090 471 SER A N 3604 C CA . SER A 471 ? 1.4857 1.4407 1.3426 -0.3833 -0.3789 0.2198 471 SER A CA 3605 C C . SER A 471 ? 1.5369 1.4947 1.3919 -0.3835 -0.3738 0.2205 471 SER A C 3606 O O . SER A 471 ? 1.5512 1.5158 1.4026 -0.3817 -0.3702 0.2031 471 SER A O 3607 C CB . SER A 471 ? 1.4368 1.3645 1.3036 -0.3771 -0.3792 0.2095 471 SER A CB 3608 O OG . SER A 471 ? 1.3797 1.2869 1.2549 -0.3728 -0.3768 0.2175 471 SER A OG 3609 N N . CYS A 472 ? 1.5512 1.5032 1.4120 -0.3852 -0.3750 0.2398 472 CYS A N 3610 C CA . CYS A 472 ? 1.4824 1.4385 1.3427 -0.3866 -0.3714 0.2443 472 CYS A CA 3611 C C . CYS A 472 ? 1.5195 1.4453 1.3946 -0.3810 -0.3718 0.2514 472 CYS A C 3612 O O . CYS A 472 ? 1.5071 1.4155 1.3942 -0.3766 -0.3762 0.2551 472 CYS A O 3613 C CB . CYS A 472 ? 1.3846 1.3768 1.2413 -0.3970 -0.3756 0.2641 472 CYS A CB 3614 S SG . CYS A 472 ? 3.0076 2.9950 2.8823 -0.4022 -0.3877 0.2945 472 CYS A SG 3615 N N . PHE A 473 ? 1.5308 1.4547 1.4057 -0.3807 -0.3675 0.2511 473 PHE A N 3616 C CA . PHE A 473 ? 1.4461 1.3467 1.3369 -0.3755 -0.3686 0.2567 473 PHE A CA 3617 C C . PHE A 473 ? 1.5003 1.4110 1.3897 -0.3801 -0.3669 0.2652 473 PHE A C 3618 O O . PHE A 473 ? 1.5253 1.4611 1.3988 -0.3854 -0.3623 0.2613 473 PHE A O 3619 C CB . PHE A 473 ? 1.3904 1.2687 1.2843 -0.3660 -0.3625 0.2392 473 PHE A CB 3620 C CG . PHE A 473 ? 1.3670 1.2471 1.2489 -0.3655 -0.3540 0.2230 473 PHE A CG 3621 C CD1 . PHE A 473 ? 1.3695 1.2434 1.2512 -0.3637 -0.3483 0.2197 473 PHE A CD1 3622 C CD2 . PHE A 473 ? 1.3432 1.2304 1.2177 -0.3665 -0.3536 0.2101 473 PHE A CD2 3623 C CE1 . PHE A 473 ? 1.3609 1.2360 1.2348 -0.3628 -0.3420 0.2039 473 PHE A CE1 3624 C CE2 . PHE A 473 ? 1.2998 1.1875 1.1706 -0.3652 -0.3493 0.1932 473 PHE A CE2 3625 C CZ . PHE A 473 ? 1.2761 1.1579 1.1464 -0.3633 -0.3433 0.1901 473 PHE A CZ 3626 N N . ASN A 474 ? 1.5603 1.4549 1.4683 -0.3776 -0.3716 0.2753 474 ASN A N 3627 C CA . ASN A 474 ? 1.6342 1.5381 1.5446 -0.3830 -0.3722 0.2875 474 ASN A CA 3628 C C . ASN A 474 ? 1.6009 1.4849 1.5112 -0.3752 -0.3636 0.2731 474 ASN A C 3629 O O . ASN A 474 ? 1.6901 1.5510 1.6109 -0.3654 -0.3620 0.2611 474 ASN A O 3630 C CB . ASN A 474 ? 1.7120 1.6146 1.6501 -0.3879 -0.3878 0.3135 474 ASN A CB 3631 C CG . ASN A 474 ? 2.0017 1.9029 1.9527 -0.3883 -0.3984 0.3213 474 ASN A CG 3632 O OD1 . ASN A 474 ? 2.2049 2.0951 2.1500 -0.3808 -0.3942 0.3044 474 ASN A OD1 3633 N ND2 . ASN A 474 ? 1.9869 1.9011 1.9582 -0.3980 -0.4134 0.3489 474 ASN A ND2 3634 N N . VAL A 475 ? 1.5713 1.4699 1.4699 -0.3799 -0.3581 0.2745 475 VAL A N 3635 C CA . VAL A 475 ? 1.5425 1.4242 1.4407 -0.3738 -0.3500 0.2630 475 VAL A CA 3636 C C . VAL A 475 ? 1.6678 1.5513 1.5798 -0.3784 -0.3561 0.2822 475 VAL A C 3637 O O . VAL A 475 ? 1.8092 1.7216 1.7130 -0.3886 -0.3577 0.2968 475 VAL A O 3638 C CB . VAL A 475 ? 1.5150 1.4095 1.3902 -0.3737 -0.3385 0.2442 475 VAL A CB 3639 C CG1 . VAL A 475 ? 1.4943 1.3718 1.3701 -0.3682 -0.3306 0.2348 475 VAL A CG1 3640 C CG2 . VAL A 475 ? 1.5127 1.4023 1.3817 -0.3693 -0.3358 0.2260 475 VAL A CG2 3641 N N . ARG A 476 ? 1.6945 1.5515 1.6298 -0.3708 -0.3608 0.2818 476 ARG A N 3642 C CA . ARG A 476 ? 1.6967 1.5502 1.6533 -0.3741 -0.3700 0.2995 476 ARG A CA 3643 C C . ARG A 476 ? 1.6331 1.4705 1.5877 -0.3666 -0.3603 0.2850 476 ARG A C 3644 O O . ARG A 476 ? 1.7309 1.5508 1.6863 -0.3555 -0.3531 0.2640 476 ARG A O 3645 C CB . ARG A 476 ? 1.6297 1.4677 1.6245 -0.3707 -0.3881 0.3098 476 ARG A CB 3646 C CG . ARG A 476 ? 1.4430 1.2745 1.4704 -0.3741 -0.4030 0.3292 476 ARG A CG 3647 C CD . ARG A 476 ? 1.4202 1.2345 1.4927 -0.3680 -0.4238 0.3330 476 ARG A CD 3648 N NE . ARG A 476 ? 1.5198 1.3234 1.6325 -0.3694 -0.4413 0.3481 476 ARG A NE 3649 C CZ . ARG A 476 ? 1.6510 1.4661 1.7890 -0.3836 -0.4605 0.3831 476 ARG A CZ 3650 N NH1 . ARG A 476 ? 1.7476 1.5897 1.8718 -0.3977 -0.4628 0.4059 476 ARG A NH1 3651 N NH2 . ARG A 476 ? 1.5954 1.3982 1.7754 -0.3845 -0.4786 0.3964 476 ARG A NH2 3652 N N . PHE A 477 ? 1.4809 1.3285 1.4332 -0.3736 -0.3603 0.2979 477 PHE A N 3653 C CA . PHE A 477 ? 1.4684 1.3028 1.4166 -0.3676 -0.3504 0.2854 477 PHE A CA 3654 C C . PHE A 477 ? 1.4450 1.2790 1.4142 -0.3730 -0.3608 0.3063 477 PHE A C 3655 O O . PHE A 477 ? 1.4793 1.3389 1.4483 -0.3863 -0.3685 0.3316 477 PHE A O 3656 C CB . PHE A 477 ? 1.4368 1.2868 1.3504 -0.3695 -0.3343 0.2712 477 PHE A CB 3657 C CG . PHE A 477 ? 1.3312 1.2203 1.2282 -0.3823 -0.3357 0.2862 477 PHE A CG 3658 C CD1 . PHE A 477 ? 1.3169 1.2243 1.2073 -0.3887 -0.3338 0.2963 477 PHE A CD1 3659 C CD2 . PHE A 477 ? 1.3164 1.2296 1.2042 -0.3880 -0.3390 0.2897 477 PHE A CD2 3660 C CE1 . PHE A 477 ? 1.3066 1.2618 1.1818 -0.4007 -0.3352 0.3096 477 PHE A CE1 3661 C CE2 . PHE A 477 ? 1.3143 1.2742 1.1874 -0.3995 -0.3402 0.3019 477 PHE A CE2 3662 C CZ . PHE A 477 ? 1.3077 1.2916 1.1745 -0.4059 -0.3384 0.3119 477 PHE A CZ 3663 N N . CYS A 478 ? 1.4486 1.2579 1.4378 -0.3632 -0.3617 0.2963 478 CYS A N 3664 C CA . CYS A 478 ? 1.6170 1.4207 1.6338 -0.3667 -0.3744 0.3143 478 CYS A CA 3665 C C . CYS A 478 ? 1.6189 1.4200 1.6193 -0.3649 -0.3609 0.3058 478 CYS A C 3666 O O . CYS A 478 ? 1.5466 1.3397 1.5262 -0.3562 -0.3441 0.2809 478 CYS A O 3667 C CB . CYS A 478 ? 1.7251 1.5045 1.7874 -0.3558 -0.3908 0.3083 478 CYS A CB 3668 S SG . CYS A 478 ? 2.4555 2.2360 2.5440 -0.3566 -0.4095 0.3173 478 CYS A SG 3669 N N . LEU A 479 ? 1.5957 1.4052 1.6075 -0.3743 -0.3695 0.3290 479 LEU A N 3670 C CA . LEU A 479 ? 1.4991 1.3091 1.4946 -0.3740 -0.3575 0.3239 479 LEU A CA 3671 C C . LEU A 479 ? 1.4540 1.2501 1.4861 -0.3749 -0.3725 0.3394 479 LEU A C 3672 O O . LEU A 479 ? 1.4423 1.2515 1.4981 -0.3874 -0.3912 0.3717 479 LEU A O 3673 C CB . LEU A 479 ? 1.5023 1.3503 1.4628 -0.3869 -0.3487 0.3353 479 LEU A CB 3674 C CG . LEU A 479 ? 1.5177 1.3707 1.4494 -0.3845 -0.3307 0.3196 479 LEU A CG 3675 C CD1 . LEU A 479 ? 1.2311 1.0613 1.1476 -0.3706 -0.3146 0.2849 479 LEU A CD1 3676 C CD2 . LEU A 479 ? 1.3574 1.2578 1.2597 -0.3965 -0.3257 0.3287 479 LEU A CD2 3677 N N . LYS A 480 ? 1.5202 1.2926 1.5596 -0.3622 -0.3656 0.3175 480 LYS A N 3678 C CA . LYS A 480 ? 1.5648 1.3222 1.6402 -0.3607 -0.3792 0.3268 480 LYS A CA 3679 C C . LYS A 480 ? 1.5891 1.3502 1.6397 -0.3624 -0.3639 0.3239 480 LYS A C 3680 O O . LYS A 480 ? 1.6538 1.4125 1.6727 -0.3550 -0.3425 0.2992 480 LYS A O 3681 C CB . LYS A 480 ? 1.6709 1.4025 1.7829 -0.3429 -0.3868 0.3013 480 LYS A CB 3682 C CG . LYS A 480 ? 1.7930 1.5081 1.9475 -0.3385 -0.4023 0.3041 480 LYS A CG 3683 C CD . LYS A 480 ? 1.7924 1.4921 1.9754 -0.3178 -0.4042 0.2686 480 LYS A CD 3684 C CE . LYS A 480 ? 1.6916 1.3906 1.9019 -0.3105 -0.4186 0.2592 480 LYS A CE 3685 N NZ . LYS A 480 ? 1.5599 1.2558 1.7973 -0.2895 -0.4202 0.2212 480 LYS A NZ 3686 N N . ALA A 481 ? 1.5343 1.3021 1.6023 -0.3729 -0.3764 0.3510 481 ALA A N 3687 C CA . ALA A 481 ? 1.4860 1.2587 1.5325 -0.3752 -0.3634 0.3505 481 ALA A CA 3688 C C . ALA A 481 ? 1.5314 1.2876 1.6205 -0.3753 -0.3810 0.3643 481 ALA A C 3689 O O . ALA A 481 ? 1.6679 1.4308 1.7926 -0.3870 -0.4053 0.3974 481 ALA A O 3690 C CB . ALA A 481 ? 1.5210 1.3349 1.5321 -0.3915 -0.3567 0.3716 481 ALA A CB 3691 N N . ASP A 482 ? 1.4949 1.2308 1.5833 -0.3629 -0.3701 0.3401 482 ASP A N 3692 C CA . ASP A 482 ? 1.6577 1.3773 1.7859 -0.3613 -0.3854 0.3485 482 ASP A CA 3693 C C . ASP A 482 ? 1.5624 1.2751 1.6653 -0.3538 -0.3643 0.3280 482 ASP A C 3694 O O . ASP A 482 ? 1.5048 1.2175 1.5719 -0.3452 -0.3409 0.3007 482 ASP A O 3695 C CB . ASP A 482 ? 1.8174 1.5119 2.0027 -0.3477 -0.4069 0.3341 482 ASP A CB 3696 C CG . ASP A 482 ? 1.8233 1.5025 2.0632 -0.3483 -0.4318 0.3483 482 ASP A CG 3697 O OD1 . ASP A 482 ? 1.8930 1.5579 2.1412 -0.3360 -0.4256 0.3251 482 ASP A OD1 3698 O OD2 . ASP A 482 ? 1.6500 1.3332 1.9275 -0.3618 -0.4588 0.3840 482 ASP A OD2 3699 N N . GLY A 483 ? 1.5512 1.2584 1.6758 -0.3578 -0.3742 0.3431 483 GLY A N 3700 C CA . GLY A 483 ? 1.5194 1.2205 1.6224 -0.3518 -0.3558 0.3268 483 GLY A CA 3701 C C . GLY A 483 ? 1.5643 1.2499 1.7109 -0.3512 -0.3737 0.3373 483 GLY A C 3702 O O . GLY A 483 ? 1.6573 1.3333 1.8578 -0.3534 -0.4028 0.3540 483 GLY A O 3703 N N . LYS A 484 ? 1.4425 1.1249 1.5688 -0.3480 -0.3578 0.3273 484 LYS A N 3704 C CA . LYS A 484 ? 1.2554 0.9231 1.4201 -0.3469 -0.3727 0.3351 484 LYS A CA 3705 C C . LYS A 484 ? 1.2005 0.8866 1.3371 -0.3624 -0.3658 0.3624 484 LYS A C 3706 O O . LYS A 484 ? 1.1855 0.8952 1.2693 -0.3696 -0.3450 0.3643 484 LYS A O 3707 C CB . LYS A 484 ? 1.2424 0.8908 1.4165 -0.3262 -0.3617 0.2943 484 LYS A CB 3708 C CG . LYS A 484 ? 1.3188 0.9578 1.5263 -0.3093 -0.3705 0.2649 484 LYS A CG 3709 C CD . LYS A 484 ? 1.4012 1.0340 1.6180 -0.2898 -0.3595 0.2255 484 LYS A CD 3710 C CE . LYS A 484 ? 1.5332 1.1525 1.7904 -0.2871 -0.3751 0.2286 484 LYS A CE 3711 N NZ . LYS A 484 ? 1.5706 1.1908 1.8342 -0.2681 -0.3628 0.1893 484 LYS A NZ 3712 N N . GLY A 485 ? 1.1800 0.8576 1.3550 -0.3673 -0.3851 0.3824 485 GLY A N 3713 C CA . GLY A 485 ? 1.1820 0.8815 1.3358 -0.3833 -0.3820 0.4123 485 GLY A CA 3714 C C . GLY A 485 ? 1.1744 0.9117 1.3227 -0.4055 -0.3948 0.4561 485 GLY A C 3715 O O . GLY A 485 ? 1.1938 0.9336 1.3634 -0.4085 -0.4099 0.4657 485 GLY A O 3716 N N . VAL A 486 ? 1.1906 0.9628 1.3107 -0.4213 -0.3892 0.4829 486 VAL A N 3717 C CA . VAL A 486 ? 1.3008 1.1265 1.4142 -0.4404 -0.3997 0.5221 486 VAL A CA 3718 C C . VAL A 486 ? 1.3319 1.1832 1.3904 -0.4426 -0.3776 0.5076 486 VAL A C 3719 O O . VAL A 486 ? 1.3463 1.1932 1.3595 -0.4308 -0.3494 0.4712 486 VAL A O 3720 C CB . VAL A 486 ? 1.3098 1.1820 1.4152 -0.4516 -0.4013 0.5495 486 VAL A CB 3721 C CG1 . VAL A 486 ? 1.3419 1.1935 1.5024 -0.4422 -0.4211 0.5535 486 VAL A CG1 3722 C CG2 . VAL A 486 ? 1.2548 1.1384 1.2957 -0.4544 -0.3704 0.5337 486 VAL A CG2 3723 N N . LEU A 487 ? 1.4209 1.3022 1.4884 -0.4553 -0.3919 0.5337 487 LEU A N 3724 C CA . LEU A 487 ? 1.5159 1.4269 1.5400 -0.4551 -0.3750 0.5184 487 LEU A CA 3725 C C . LEU A 487 ? 1.6564 1.6033 1.7049 -0.4728 -0.3985 0.5590 487 LEU A C 3726 O O . LEU A 487 ? 1.7718 1.6953 1.8763 -0.4766 -0.4261 0.5822 487 LEU A O 3727 C CB . LEU A 487 ? 1.3366 1.2033 1.3494 -0.4330 -0.3584 0.4697 487 LEU A CB 3728 C CG . LEU A 487 ? 1.3125 1.1434 1.3666 -0.4246 -0.3747 0.4631 487 LEU A CG 3729 C CD1 . LEU A 487 ? 1.2628 1.0640 1.2941 -0.4042 -0.3530 0.4149 487 LEU A CD1 3730 C CD2 . LEU A 487 ? 1.3456 1.1422 1.4625 -0.4223 -0.4009 0.4767 487 LEU A CD2 3731 N N . PRO A 488 ? 1.5861 1.5929 1.5959 -0.4836 -0.3890 0.5670 488 PRO A N 3732 C CA . PRO A 488 ? 1.5657 1.6232 1.5931 -0.5038 -0.4097 0.6104 488 PRO A CA 3733 C C . PRO A 488 ? 1.4440 1.4646 1.5143 -0.5004 -0.4290 0.6149 488 PRO A C 3734 O O . PRO A 488 ? 1.3808 1.3511 1.4484 -0.4806 -0.4184 0.5742 488 PRO A O 3735 C CB . PRO A 488 ? 1.5439 1.6604 1.5144 -0.5056 -0.3878 0.5931 488 PRO A CB 3736 C CG . PRO A 488 ? 1.5255 1.6438 1.4568 -0.4964 -0.3641 0.5634 488 PRO A CG 3737 C CD . PRO A 488 ? 1.5104 1.5472 1.4600 -0.4776 -0.3594 0.5351 488 PRO A CD 3738 N N . ARG A 489 ? 1.3777 1.4322 1.4916 -0.5154 -0.4567 0.6577 489 ARG A N 3739 C CA . ARG A 489 ? 1.4639 1.4912 1.6277 -0.5112 -0.4793 0.6632 489 ARG A CA 3740 C C . ARG A 489 ? 1.4514 1.4667 1.5811 -0.5085 -0.4654 0.6434 489 ARG A C 3741 O O . ARG A 489 ? 1.3713 1.3356 1.5252 -0.4938 -0.4705 0.6202 489 ARG A O 3742 C CB . ARG A 489 ? 1.6312 1.7177 1.8434 -0.5275 -0.5084 0.7084 489 ARG A CB 3743 C CG . ARG A 489 ? 1.7412 1.8598 1.9839 -0.5348 -0.5218 0.7323 489 ARG A CG 3744 C CD . ARG A 489 ? 1.8471 2.0512 2.0480 -0.5540 -0.5075 0.7522 489 ARG A CD 3745 N NE . ARG A 489 ? 1.9173 2.1926 2.1238 -0.5729 -0.5162 0.7815 489 ARG A NE 3746 C CZ . ARG A 489 ? 1.8348 2.1993 2.0113 -0.5905 -0.5051 0.7981 489 ARG A CZ 3747 N NH1 . ARG A 489 ? 1.8109 2.2026 1.9485 -0.5909 -0.4857 0.7881 489 ARG A NH1 3748 N NH2 . ARG A 489 ? 1.7232 2.1535 1.9103 -0.6073 -0.5127 0.8228 489 ARG A NH2 3749 N N . LYS A 490 ? 1.4575 1.5308 1.5346 -0.5149 -0.4461 0.6392 490 LYS A N 3750 C CA . LYS A 490 ? 1.4085 1.4849 1.4557 -0.5060 -0.4314 0.6099 490 LYS A CA 3751 C C . LYS A 490 ? 1.4254 1.5177 1.4106 -0.4943 -0.3983 0.5658 490 LYS A C 3752 O O . LYS A 490 ? 1.5022 1.6384 1.4599 -0.5008 -0.3885 0.5698 490 LYS A O 3753 C CB . LYS A 490 ? 1.4887 1.6268 1.5444 -0.5265 -0.4473 0.6503 490 LYS A CB 3754 C CG . LYS A 490 ? 1.5812 1.6987 1.7041 -0.5372 -0.4825 0.6918 490 LYS A CG 3755 C CD . LYS A 490 ? 1.7303 1.9186 1.8641 -0.5558 -0.4964 0.7278 490 LYS A CD 3756 C CE . LYS A 490 ? 1.7742 1.9486 1.9857 -0.5573 -0.5300 0.7513 490 LYS A CE 3757 N NZ . LYS A 490 ? 1.6716 1.8403 1.9352 -0.5566 -0.5497 0.7662 490 LYS A NZ 3758 N N . LEU A 491 ? 1.4651 1.5233 1.4321 -0.4770 -0.3833 0.5242 491 LEU A N 3759 C CA . LEU A 491 ? 1.4679 1.5317 1.3856 -0.4644 -0.3556 0.4801 491 LEU A CA 3760 C C . LEU A 491 ? 1.5436 1.6439 1.4372 -0.4654 -0.3495 0.4680 491 LEU A C 3761 O O . LEU A 491 ? 1.5415 1.6396 1.4555 -0.4699 -0.3627 0.4835 491 LEU A O 3762 C CB . LEU A 491 ? 1.3685 1.3620 1.2874 -0.4430 -0.3429 0.4401 491 LEU A CB 3763 C CG . LEU A 491 ? 1.4160 1.3659 1.3679 -0.4389 -0.3518 0.4478 491 LEU A CG 3764 C CD1 . LEU A 491 ? 1.3884 1.2792 1.3449 -0.4180 -0.3410 0.4086 491 LEU A CD1 3765 C CD2 . LEU A 491 ? 1.4976 1.4720 1.4333 -0.4453 -0.3452 0.4568 491 LEU A CD2 3766 N N . ASN A 492 ? 1.5382 1.6718 1.3911 -0.4606 -0.3307 0.4387 492 ASN A N 3767 C CA . ASN A 492 ? 1.5334 1.7055 1.3645 -0.4603 -0.3254 0.4224 492 ASN A CA 3768 C C . ASN A 492 ? 1.6808 1.8135 1.4921 -0.4409 -0.3079 0.3718 492 ASN A C 3769 O O . ASN A 492 ? 1.6943 1.8252 1.4850 -0.4321 -0.2936 0.3431 492 ASN A O 3770 C CB . ASN A 492 ? 1.4396 1.7028 1.2460 -0.4726 -0.3233 0.4315 492 ASN A CB 3771 C CG . ASN A 492 ? 1.4901 1.8080 1.3179 -0.4956 -0.3433 0.4881 492 ASN A CG 3772 O OD1 . ASN A 492 ? 1.4274 1.7885 1.2613 -0.5067 -0.3536 0.5089 492 ASN A OD1 3773 N ND2 . ASN A 492 ? 1.6103 1.9281 1.4523 -0.5039 -0.3502 0.5154 492 ASN A ND2 3774 N N . PHE A 493 ? 1.7173 1.8204 1.5379 -0.4351 -0.3107 0.3629 493 PHE A N 3775 C CA . PHE A 493 ? 1.5545 1.6213 1.3627 -0.4188 -0.2976 0.3209 493 PHE A CA 3776 C C . PHE A 493 ? 1.5635 1.6728 1.3537 -0.4191 -0.2952 0.3037 493 PHE A C 3777 O O . PHE A 493 ? 1.5506 1.7024 1.3441 -0.4305 -0.3053 0.3263 493 PHE A O 3778 C CB . PHE A 493 ? 1.4563 1.4596 1.2889 -0.4103 -0.3021 0.3192 493 PHE A CB 3779 C CG . PHE A 493 ? 1.4153 1.3726 1.2656 -0.4042 -0.3017 0.3212 493 PHE A CG 3780 C CD1 . PHE A 493 ? 1.5556 1.5112 1.4324 -0.4129 -0.3164 0.3544 493 PHE A CD1 3781 C CD2 . PHE A 493 ? 1.3910 1.3092 1.2355 -0.3901 -0.2885 0.2907 493 PHE A CD2 3782 C CE1 . PHE A 493 ? 1.6342 1.5492 1.5304 -0.4060 -0.3173 0.3527 493 PHE A CE1 3783 C CE2 . PHE A 493 ? 1.3646 1.2467 1.2256 -0.3841 -0.2878 0.2908 493 PHE A CE2 3784 C CZ . PHE A 493 ? 1.5152 1.3952 1.4017 -0.3911 -0.3019 0.3197 493 PHE A CZ 3785 N N . GLN A 494 ? 1.5725 1.6715 1.3473 -0.4069 -0.2835 0.2638 494 GLN A N 3786 C CA . GLN A 494 ? 1.6228 1.7516 1.3868 -0.4039 -0.2828 0.2408 494 GLN A CA 3787 C C . GLN A 494 ? 1.5766 1.6481 1.3504 -0.3928 -0.2809 0.2213 494 GLN A C 3788 O O . GLN A 494 ? 1.5283 1.5610 1.3030 -0.3821 -0.2731 0.1974 494 GLN A O 3789 C CB . GLN A 494 ? 1.7010 1.8730 1.4459 -0.3989 -0.2752 0.2083 494 GLN A CB 3790 C CG . GLN A 494 ? 1.8067 2.0495 1.5395 -0.4100 -0.2767 0.2254 494 GLN A CG 3791 C CD . GLN A 494 ? 1.8540 2.1671 1.5847 -0.4236 -0.2864 0.2491 494 GLN A CD 3792 O OE1 . GLN A 494 ? 1.8458 2.2101 1.5756 -0.4380 -0.2923 0.2830 494 GLN A OE1 3793 N NE2 . GLN A 494 ? 1.8323 2.1517 1.5636 -0.4199 -0.2889 0.2333 494 GLN A NE2 3794 N N . VAL A 495 ? 1.5805 1.6507 1.3630 -0.3962 -0.2887 0.2337 495 VAL A N 3795 C CA . VAL A 495 ? 1.5116 1.5327 1.3048 -0.3873 -0.2884 0.2205 495 VAL A CA 3796 C C . VAL A 495 ? 1.4665 1.5057 1.2518 -0.3825 -0.2875 0.1923 495 VAL A C 3797 O O . VAL A 495 ? 1.5152 1.6076 1.2913 -0.3884 -0.2915 0.1924 495 VAL A O 3798 C CB . VAL A 495 ? 1.4223 1.4252 1.2339 -0.3924 -0.2989 0.2490 495 VAL A CB 3799 C CG1 . VAL A 495 ? 1.3888 1.3430 1.2118 -0.3824 -0.2978 0.2352 495 VAL A CG1 3800 C CG2 . VAL A 495 ? 1.4043 1.3954 1.2311 -0.3979 -0.3045 0.2773 495 VAL A CG2 3801 N N . GLU A 496 ? 1.4022 1.4008 1.1939 -0.3722 -0.2837 0.1689 496 GLU A N 3802 C CA . GLU A 496 ? 1.4085 1.4160 1.2003 -0.3671 -0.2859 0.1420 496 GLU A CA 3803 C C . GLU A 496 ? 1.4408 1.4067 1.2464 -0.3634 -0.2890 0.1440 496 GLU A C 3804 O O . GLU A 496 ? 1.5621 1.4859 1.3780 -0.3587 -0.2857 0.1458 496 GLU A O 3805 C CB . GLU A 496 ? 1.4345 1.4405 1.2265 -0.3588 -0.2817 0.1095 496 GLU A CB 3806 C CG . GLU A 496 ? 1.5965 1.6170 1.3955 -0.3531 -0.2878 0.0785 496 GLU A CG 3807 C CD . GLU A 496 ? 1.7681 1.8552 1.5558 -0.3569 -0.2923 0.0707 496 GLU A CD 3808 O OE1 . GLU A 496 ? 1.8640 1.9642 1.6579 -0.3548 -0.2992 0.0560 496 GLU A OE1 3809 O OE2 . GLU A 496 ? 1.7631 1.8939 1.5365 -0.3625 -0.2895 0.0799 496 GLU A OE2 3810 N N . LEU A 497 ? 1.3594 1.3429 1.1652 -0.3657 -0.2953 0.1436 497 LEU A N 3811 C CA . LEU A 497 ? 1.3123 1.2631 1.1301 -0.3630 -0.2990 0.1464 497 LEU A CA 3812 C C . LEU A 497 ? 1.3415 1.2923 1.1659 -0.3577 -0.3028 0.1191 497 LEU A C 3813 O O . LEU A 497 ? 1.3635 1.3525 1.1826 -0.3580 -0.3065 0.1026 497 LEU A O 3814 C CB . LEU A 497 ? 1.2990 1.2632 1.1166 -0.3702 -0.3053 0.1709 497 LEU A CB 3815 C CG . LEU A 497 ? 1.2813 1.2346 1.1048 -0.3750 -0.3070 0.2004 497 LEU A CG 3816 C CD1 . LEU A 497 ? 1.2883 1.2584 1.1168 -0.3829 -0.3164 0.2241 497 LEU A CD1 3817 C CD2 . LEU A 497 ? 1.2665 1.1721 1.1041 -0.3676 -0.3042 0.2001 497 LEU A CD2 3818 N N . LEU A 498 ? 1.3203 1.2324 1.1594 -0.3529 -0.3034 0.1147 498 LEU A N 3819 C CA . LEU A 498 ? 1.3859 1.2924 1.2391 -0.3489 -0.3103 0.0933 498 LEU A CA 3820 C C . LEU A 498 ? 1.3766 1.2607 1.2403 -0.3496 -0.3148 0.1054 498 LEU A C 3821 O O . LEU A 498 ? 1.4358 1.2954 1.3045 -0.3492 -0.3113 0.1213 498 LEU A O 3822 C CB . LEU A 498 ? 1.5300 1.4170 1.3974 -0.3438 -0.3098 0.0762 498 LEU A CB 3823 C CG . LEU A 498 ? 1.5386 1.4488 1.4010 -0.3410 -0.3079 0.0551 498 LEU A CG 3824 C CD1 . LEU A 498 ? 1.4248 1.3821 1.2804 -0.3406 -0.3139 0.0357 498 LEU A CD1 3825 C CD2 . LEU A 498 ? 1.5457 1.4579 1.3914 -0.3433 -0.2972 0.0708 498 LEU A CD2 3826 N N . LEU A 499 ? 1.3521 1.2492 1.2200 -0.3501 -0.3228 0.0963 499 LEU A N 3827 C CA . LEU A 499 ? 1.4126 1.2930 1.2896 -0.3512 -0.3278 0.1073 499 LEU A CA 3828 C C . LEU A 499 ? 1.4781 1.3392 1.3794 -0.3487 -0.3358 0.0955 499 LEU A C 3829 O O . LEU A 499 ? 1.3760 1.2457 1.2895 -0.3462 -0.3436 0.0723 499 LEU A O 3830 C CB . LEU A 499 ? 1.3778 1.2841 1.2459 -0.3545 -0.3326 0.1088 499 LEU A CB 3831 C CG . LEU A 499 ? 1.3813 1.3079 1.2319 -0.3598 -0.3285 0.1291 499 LEU A CG 3832 C CD1 . LEU A 499 ? 1.4145 1.3714 1.2587 -0.3639 -0.3341 0.1304 499 LEU A CD1 3833 C CD2 . LEU A 499 ? 1.3863 1.2856 1.2404 -0.3602 -0.3256 0.1526 499 LEU A CD2 3834 N N . ASP A 500 ? 1.5492 1.3886 1.4611 -0.3496 -0.3358 0.1116 500 ASP A N 3835 C CA . ASP A 500 ? 1.4678 1.2927 1.4065 -0.3501 -0.3452 0.1093 500 ASP A CA 3836 C C . ASP A 500 ? 1.4204 1.2376 1.3766 -0.3481 -0.3485 0.0941 500 ASP A C 3837 O O . ASP A 500 ? 1.3708 1.1873 1.3500 -0.3473 -0.3614 0.0771 500 ASP A O 3838 C CB . ASP A 500 ? 1.3786 1.2107 1.3273 -0.3514 -0.3573 0.1014 500 ASP A CB 3839 C CG . ASP A 500 ? 1.4491 1.2681 1.4234 -0.3546 -0.3673 0.1129 500 ASP A CG 3840 O OD1 . ASP A 500 ? 1.3914 1.2127 1.3811 -0.3559 -0.3799 0.1054 500 ASP A OD1 3841 O OD2 . ASP A 500 ? 1.5301 1.3410 1.5107 -0.3564 -0.3633 0.1299 500 ASP A OD2 3842 N N . LYS A 501 ? 1.3894 1.2006 1.3376 -0.3469 -0.3381 0.0992 501 LYS A N 3843 C CA . LYS A 501 ? 1.4021 1.2061 1.3645 -0.3449 -0.3396 0.0858 501 LYS A CA 3844 C C . LYS A 501 ? 1.4015 1.1915 1.4014 -0.3475 -0.3533 0.0872 501 LYS A C 3845 O O . LYS A 501 ? 1.5708 1.3560 1.5930 -0.3456 -0.3625 0.0696 501 LYS A O 3846 C CB . LYS A 501 ? 1.4445 1.2431 1.3924 -0.3439 -0.3255 0.0964 501 LYS A CB 3847 C CG . LYS A 501 ? 1.5249 1.3166 1.4847 -0.3419 -0.3255 0.0834 501 LYS A CG 3848 C CD . LYS A 501 ? 1.5615 1.3477 1.5071 -0.3411 -0.3114 0.0950 501 LYS A CD 3849 C CE . LYS A 501 ? 1.5893 1.3675 1.5489 -0.3396 -0.3118 0.0840 501 LYS A CE 3850 N NZ . LYS A 501 ? 1.6448 1.4344 1.6019 -0.3357 -0.3161 0.0570 501 LYS A NZ 3851 N N . LEU A 502 ? 1.3144 1.1009 1.3244 -0.3522 -0.3563 0.1088 502 LEU A N 3852 C CA . LEU A 502 ? 1.3215 1.1007 1.3705 -0.3575 -0.3716 0.1176 502 LEU A CA 3853 C C . LEU A 502 ? 1.4613 1.2370 1.5376 -0.3566 -0.3908 0.0965 502 LEU A C 3854 O O . LEU A 502 ? 1.5984 1.3643 1.7130 -0.3584 -0.4062 0.0911 502 LEU A O 3855 C CB . LEU A 502 ? 1.2690 1.0562 1.3211 -0.3630 -0.3721 0.1442 502 LEU A CB 3856 C CG . LEU A 502 ? 1.2321 1.0287 1.2704 -0.3633 -0.3577 0.1633 502 LEU A CG 3857 C CD1 . LEU A 502 ? 1.2188 1.0328 1.2634 -0.3679 -0.3607 0.1851 502 LEU A CD1 3858 C CD2 . LEU A 502 ? 1.2084 1.0020 1.2651 -0.3655 -0.3572 0.1679 502 LEU A CD2 3859 N N . LYS A 503 ? 1.5205 1.3062 1.5802 -0.3536 -0.3913 0.0840 503 LYS A N 3860 C CA . LYS A 503 ? 1.5977 1.3868 1.6804 -0.3506 -0.4088 0.0578 503 LYS A CA 3861 C C . LYS A 503 ? 1.7929 1.5933 1.8695 -0.3425 -0.4072 0.0248 503 LYS A C 3862 O O . LYS A 503 ? 1.6742 1.4732 1.7368 -0.3408 -0.3955 0.0249 503 LYS A O 3863 C CB . LYS A 503 ? 1.5192 1.3208 1.5863 -0.3509 -0.4096 0.0583 503 LYS A CB 3864 C CG . LYS A 503 ? 1.4719 1.2670 1.5477 -0.3583 -0.4136 0.0875 503 LYS A CG 3865 C CD . LYS A 503 ? 1.5751 1.3579 1.7018 -0.3635 -0.4362 0.0924 503 LYS A CD 3866 C CE . LYS A 503 ? 1.5690 1.3541 1.7035 -0.3718 -0.4407 0.1231 503 LYS A CE 3867 N NZ . LYS A 503 ? 1.6112 1.3879 1.7997 -0.3794 -0.4652 0.1341 503 LYS A NZ 3868 N N . GLN A 504 ? 2.0004 1.8156 2.0903 -0.3374 -0.4203 -0.0048 504 GLN A N 3869 C CA . GLN A 504 ? 2.0218 1.8615 2.1072 -0.3285 -0.4210 -0.0418 504 GLN A CA 3870 C C . GLN A 504 ? 1.9415 1.7684 2.0657 -0.3243 -0.4342 -0.0618 504 GLN A C 3871 O O . GLN A 504 ? 1.8907 1.7395 2.0201 -0.3155 -0.4387 -0.0977 504 GLN A O 3872 C CB . GLN A 504 ? 1.9619 1.8228 1.9978 -0.3280 -0.3979 -0.0355 504 GLN A CB 3873 C CG . GLN A 504 ? 1.8849 1.7592 1.8867 -0.3325 -0.3868 -0.0149 504 GLN A CG 3874 C CD . GLN A 504 ? 1.9700 1.8725 1.9323 -0.3325 -0.3701 -0.0118 504 GLN A CD 3875 O OE1 . GLN A 504 ? 2.0472 1.9682 2.0053 -0.3282 -0.3674 -0.0308 504 GLN A OE1 3876 N NE2 . GLN A 504 ? 1.9967 1.9046 1.9327 -0.3378 -0.3605 0.0133 504 GLN A NE2 3877 N N . LYS A 505 ? 1.8405 1.6365 1.9936 -0.3308 -0.4414 -0.0382 505 LYS A N 3878 C CA . LYS A 505 ? 1.6967 1.4770 1.8971 -0.3286 -0.4591 -0.0530 505 LYS A CA 3879 C C . LYS A 505 ? 1.7158 1.4851 1.9735 -0.3296 -0.4894 -0.0621 505 LYS A C 3880 O O . LYS A 505 ? 1.7693 1.5215 2.0477 -0.3396 -0.4975 -0.0297 505 LYS A O 3881 C CB . LYS A 505 ? 1.5622 1.3209 1.7646 -0.3366 -0.4507 -0.0189 505 LYS A CB 3882 C CG . LYS A 505 ? 1.5019 1.2680 1.6571 -0.3346 -0.4243 -0.0133 505 LYS A CG 3883 C CD . LYS A 505 ? 1.5688 1.3400 1.7344 -0.3264 -0.4274 -0.0453 505 LYS A CD 3884 C CE . LYS A 505 ? 1.4235 1.1972 1.5492 -0.3264 -0.4033 -0.0342 505 LYS A CE 3885 N NZ . LYS A 505 ? 1.3805 1.1619 1.5141 -0.3184 -0.4055 -0.0652 505 LYS A NZ 3886 N N . GLY A 506 ? 1.6926 1.4757 1.9789 -0.3189 -0.5073 -0.1071 506 GLY A N 3887 C CA . GLY A 506 ? 1.6686 1.4452 2.0115 -0.3175 -0.5384 -0.1237 506 GLY A CA 3888 C C . GLY A 506 ? 1.6894 1.4651 2.0193 -0.3250 -0.5370 -0.0982 506 GLY A C 3889 O O . GLY A 506 ? 1.7206 1.4781 2.0985 -0.3311 -0.5606 -0.0860 506 GLY A O 3890 N N . ALA A 507 ? 1.7341 1.5305 2.0027 -0.3253 -0.5112 -0.0890 507 ALA A N 3891 C CA . ALA A 507 ? 1.7820 1.5759 2.0317 -0.3335 -0.5057 -0.0585 507 ALA A CA 3892 C C . ALA A 507 ? 1.7738 1.5990 1.9726 -0.3294 -0.4882 -0.0686 507 ALA A C 3893 O O . ALA A 507 ? 1.8797 1.7315 2.0494 -0.3224 -0.4756 -0.0907 507 ALA A O 3894 C CB . ALA A 507 ? 1.6967 1.4728 1.9281 -0.3446 -0.4908 -0.0107 507 ALA A CB 3895 N N . ILE A 508 ? 1.5945 1.4193 1.7848 -0.3347 -0.4886 -0.0501 508 ILE A N 3896 C CA . ILE A 508 ? 1.6396 1.4933 1.7871 -0.3329 -0.4748 -0.0544 508 ILE A CA 3897 C C . ILE A 508 ? 1.7671 1.6284 1.8601 -0.3360 -0.4468 -0.0305 508 ILE A C 3898 O O . ILE A 508 ? 1.7809 1.6205 1.8664 -0.3419 -0.4374 -0.0001 508 ILE A O 3899 C CB . ILE A 508 ? 1.8245 1.6718 1.9800 -0.3385 -0.4834 -0.0374 508 ILE A CB 3900 C CG1 . ILE A 508 ? 1.7295 1.6076 1.8429 -0.3372 -0.4702 -0.0408 508 ILE A CG1 3901 C CG2 . ILE A 508 ? 1.8095 1.6302 1.9649 -0.3492 -0.4790 0.0073 508 ILE A CG2 3902 C CD1 . ILE A 508 ? 1.6976 1.6157 1.8120 -0.3274 -0.4755 -0.0848 508 ILE A CD1 3903 N N . ARG A 509 ? 1.8493 1.7459 1.9083 -0.3323 -0.4353 -0.0444 509 ARG A N 3904 C CA . ARG A 509 ? 1.7806 1.6872 1.7935 -0.3360 -0.4127 -0.0213 509 ARG A CA 3905 C C . ARG A 509 ? 1.6265 1.5336 1.6187 -0.3419 -0.4070 0.0044 509 ARG A C 3906 O O . ARG A 509 ? 1.6873 1.6192 1.6751 -0.3411 -0.4116 -0.0069 509 ARG A O 3907 C CB . ARG A 509 ? 1.8842 1.8349 1.8744 -0.3312 -0.4051 -0.0443 509 ARG A CB 3908 C CG . ARG A 509 ? 1.9782 1.9325 1.9835 -0.3247 -0.4082 -0.0699 509 ARG A CG 3909 C CD . ARG A 509 ? 2.0673 2.0309 2.1160 -0.3160 -0.4306 -0.1117 509 ARG A CD 3910 N NE . ARG A 509 ? 2.0727 2.0294 2.1446 -0.3099 -0.4365 -0.1337 509 ARG A NE 3911 C CZ . ARG A 509 ? 1.9976 1.9545 2.1169 -0.3014 -0.4589 -0.1708 509 ARG A CZ 3912 N NH1 . ARG A 509 ? 1.9384 1.9021 2.0874 -0.2980 -0.4778 -0.1905 509 ARG A NH1 3913 N NH2 . ARG A 509 ? 1.9469 1.8968 2.0872 -0.2960 -0.4641 -0.1891 509 ARG A NH2 3914 N N . ARG A 510 ? 1.5257 1.4087 1.5069 -0.3473 -0.3977 0.0372 510 ARG A N 3915 C CA . ARG A 510 ? 1.4612 1.3398 1.4319 -0.3521 -0.3958 0.0606 510 ARG A CA 3916 C C . ARG A 510 ? 1.4269 1.3219 1.3622 -0.3545 -0.3817 0.0771 510 ARG A C 3917 O O . ARG A 510 ? 1.4212 1.3146 1.3485 -0.3577 -0.3809 0.0945 510 ARG A O 3918 C CB . ARG A 510 ? 1.4311 1.2813 1.4172 -0.3561 -0.3973 0.0849 510 ARG A CB 3919 C CG . ARG A 510 ? 1.4552 1.2905 1.4831 -0.3571 -0.4156 0.0779 510 ARG A CG 3920 C CD . ARG A 510 ? 1.5438 1.3616 1.5868 -0.3621 -0.4153 0.1033 510 ARG A CD 3921 N NE . ARG A 510 ? 1.6110 1.4322 1.6325 -0.3651 -0.4045 0.1293 510 ARG A NE 3922 C CZ . ARG A 510 ? 1.6834 1.5019 1.7055 -0.3675 -0.3979 0.1499 510 ARG A CZ 3923 N NH1 . ARG A 510 ? 1.6800 1.4910 1.7211 -0.3687 -0.4000 0.1511 510 ARG A NH1 3924 N NH2 . ARG A 510 ? 1.7352 1.5622 1.7408 -0.3683 -0.3900 0.1677 510 ARG A NH2 3925 N N . ALA A 511 ? 1.3873 1.2991 1.3046 -0.3534 -0.3723 0.0732 511 ALA A N 3926 C CA . ALA A 511 ? 1.3443 1.2726 1.2349 -0.3572 -0.3625 0.0923 511 ALA A CA 3927 C C . ALA A 511 ? 1.3117 1.2784 1.1867 -0.3573 -0.3580 0.0809 511 ALA A C 3928 O O . ALA A 511 ? 1.3181 1.2890 1.1975 -0.3536 -0.3569 0.0637 511 ALA A O 3929 C CB . ALA A 511 ? 1.1992 1.1014 1.0856 -0.3584 -0.3543 0.1166 511 ALA A CB 3930 N N . LEU A 512 ? 1.2969 1.2957 1.1550 -0.3624 -0.3561 0.0923 512 LEU A N 3931 C CA . LEU A 512 ? 1.4462 1.4947 1.2894 -0.3648 -0.3529 0.0866 512 LEU A CA 3932 C C . LEU A 512 ? 1.3643 1.4265 1.1920 -0.3736 -0.3479 0.1205 512 LEU A C 3933 O O . LEU A 512 ? 1.3108 1.3525 1.1399 -0.3769 -0.3494 0.1425 512 LEU A O 3934 C CB . LEU A 512 ? 1.5268 1.6224 1.3715 -0.3632 -0.3602 0.0612 512 LEU A CB 3935 C CG . LEU A 512 ? 1.4466 1.5322 1.3153 -0.3543 -0.3706 0.0250 512 LEU A CG 3936 C CD1 . LEU A 512 ? 1.3615 1.4994 1.2325 -0.3522 -0.3786 -0.0002 512 LEU A CD1 3937 C CD2 . LEU A 512 ? 1.5087 1.5884 1.3881 -0.3478 -0.3706 0.0028 512 LEU A CD2 3938 N N . PHE A 513 ? 1.3404 1.4392 1.1568 -0.3776 -0.3439 0.1251 513 PHE A N 3939 C CA . PHE A 513 ? 1.3746 1.4944 1.1823 -0.3879 -0.3432 0.1596 513 PHE A CA 3940 C C . PHE A 513 ? 1.5097 1.6810 1.3112 -0.3949 -0.3484 0.1653 513 PHE A C 3941 O O . PHE A 513 ? 1.5321 1.7416 1.3313 -0.3914 -0.3505 0.1377 513 PHE A O 3942 C CB . PHE A 513 ? 1.3651 1.5115 1.1650 -0.3916 -0.3386 0.1662 513 PHE A CB 3943 C CG . PHE A 513 ? 1.4733 1.5694 1.2790 -0.3866 -0.3333 0.1682 513 PHE A CG 3944 C CD1 . PHE A 513 ? 1.5186 1.6076 1.3249 -0.3788 -0.3290 0.1408 513 PHE A CD1 3945 C CD2 . PHE A 513 ? 1.4368 1.4951 1.2504 -0.3891 -0.3338 0.1959 513 PHE A CD2 3946 C CE1 . PHE A 513 ? 1.3464 1.3925 1.1579 -0.3748 -0.3238 0.1436 513 PHE A CE1 3947 C CE2 . PHE A 513 ? 1.3447 1.3625 1.1644 -0.3839 -0.3289 0.1956 513 PHE A CE2 3948 C CZ . PHE A 513 ? 1.3353 1.3476 1.1523 -0.3773 -0.3231 0.1708 513 PHE A CZ 3949 N N . LEU A 514 ? 1.6413 1.8154 1.4436 -0.4043 -0.3518 0.2001 514 LEU A N 3950 C CA . LEU A 514 ? 1.6227 1.8412 1.4213 -0.4120 -0.3573 0.2106 514 LEU A CA 3951 C C . LEU A 514 ? 1.4912 1.7937 1.2782 -0.4187 -0.3573 0.2061 514 LEU A C 3952 O O . LEU A 514 ? 1.4632 1.8091 1.2457 -0.4164 -0.3590 0.1827 514 LEU A O 3953 C CB . LEU A 514 ? 1.6022 1.8043 1.4098 -0.4212 -0.3633 0.2516 514 LEU A CB 3954 C CG . LEU A 514 ? 1.5947 1.8307 1.4021 -0.4294 -0.3700 0.2669 514 LEU A CG 3955 C CD1 . LEU A 514 ? 1.5040 1.6861 1.3252 -0.4281 -0.3753 0.2838 514 LEU A CD1 3956 C CD2 . LEU A 514 ? 1.7150 2.0175 1.5212 -0.4451 -0.3750 0.2990 514 LEU A CD2 3957 N N . TYR A 515 ? 1.5039 1.8341 1.2879 -0.4269 -0.3563 0.2280 515 TYR A N 3958 C CA . TYR A 515 ? 1.5404 1.9617 1.3137 -0.4353 -0.3568 0.2293 515 TYR A CA 3959 C C . TYR A 515 ? 1.5371 1.9863 1.3029 -0.4241 -0.3515 0.1839 515 TYR A C 3960 O O . TYR A 515 ? 1.5292 2.0545 1.2881 -0.4238 -0.3527 0.1619 515 TYR A O 3961 C CB . TYR A 515 ? 1.6309 2.0748 1.4072 -0.4499 -0.3599 0.2738 515 TYR A CB 3962 C CG . TYR A 515 ? 1.7347 2.1552 1.5264 -0.4613 -0.3693 0.3189 515 TYR A CG 3963 C CD1 . TYR A 515 ? 1.8059 2.1464 1.6137 -0.4576 -0.3717 0.3336 515 TYR A CD1 3964 C CD2 . TYR A 515 ? 1.7536 2.2357 1.5469 -0.4751 -0.3771 0.3452 515 TYR A CD2 3965 C CE1 . TYR A 515 ? 1.8989 2.2186 1.7266 -0.4663 -0.3830 0.3706 515 TYR A CE1 3966 C CE2 . TYR A 515 ? 1.8300 2.2894 1.6425 -0.4855 -0.3881 0.3864 515 TYR A CE2 3967 C CZ . TYR A 515 ? 1.9473 2.3239 1.7783 -0.4804 -0.3917 0.3975 515 TYR A CZ 3968 O OH . TYR A 515 ? 2.0313 2.3859 1.8870 -0.4890 -0.4053 0.4344 515 TYR A OH 3969 N N . SER A 516 ? 1.6878 2.0785 1.4575 -0.4143 -0.3466 0.1683 516 SER A N 3970 C CA . SER A 516 ? 1.6770 2.0878 1.4443 -0.4037 -0.3432 0.1271 516 SER A CA 3971 C C . SER A 516 ? 1.5330 1.9343 1.3099 -0.3902 -0.3470 0.0811 516 SER A C 3972 O O . SER A 516 ? 1.4993 1.9438 1.2783 -0.3818 -0.3486 0.0417 516 SER A O 3973 C CB . SER A 516 ? 1.6613 2.0122 1.4319 -0.3990 -0.3376 0.1294 516 SER A CB 3974 O OG . SER A 516 ? 1.6081 1.9710 1.3737 -0.4108 -0.3360 0.1687 516 SER A OG 3975 N N . ARG A 517 ? 1.5171 1.8638 1.3031 -0.3879 -0.3501 0.0856 517 ARG A N 3976 C CA . ARG A 517 ? 1.5608 1.8857 1.3620 -0.3762 -0.3562 0.0475 517 ARG A CA 3977 C C . ARG A 517 ? 1.5927 1.8827 1.4076 -0.3646 -0.3566 0.0163 517 ARG A C 3978 O O . ARG A 517 ? 1.6219 1.9202 1.4539 -0.3543 -0.3646 -0.0242 517 ARG A O 3979 C CB . ARG A 517 ? 1.5177 1.9199 1.3184 -0.3743 -0.3623 0.0196 517 ARG A CB 3980 C CG . ARG A 517 ? 1.5489 1.9841 1.3401 -0.3852 -0.3637 0.0474 517 ARG A CG 3981 C CD . ARG A 517 ? 1.6671 2.1887 1.4581 -0.3825 -0.3692 0.0160 517 ARG A CD 3982 N NE . ARG A 517 ? 1.6472 2.2010 1.4305 -0.3929 -0.3710 0.0416 517 ARG A NE 3983 C CZ . ARG A 517 ? 1.4142 1.9432 1.2061 -0.3894 -0.3764 0.0328 517 ARG A CZ 3984 N NH1 . ARG A 517 ? 1.3771 1.8497 1.1876 -0.3766 -0.3818 0.0010 517 ARG A NH1 3985 N NH2 . ARG A 517 ? 1.3682 1.9300 1.1523 -0.3997 -0.3775 0.0579 517 ARG A NH2 3986 N N . SER A 518 ? 1.5570 1.8083 1.3681 -0.3664 -0.3496 0.0353 518 SER A N 3987 C CA . SER A 518 ? 1.4780 1.7001 1.3010 -0.3572 -0.3491 0.0108 518 SER A CA 3988 C C . SER A 518 ? 1.3868 1.5313 1.2167 -0.3572 -0.3450 0.0325 518 SER A C 3989 O O . SER A 518 ? 1.3667 1.4898 1.1876 -0.3646 -0.3403 0.0678 518 SER A O 3990 C CB . SER A 518 ? 1.4400 1.7120 1.2499 -0.3585 -0.3435 0.0058 518 SER A CB 3991 O OG . SER A 518 ? 1.4011 1.6452 1.2228 -0.3495 -0.3432 -0.0179 518 SER A OG 3992 N N . PRO A 519 ? 1.3883 1.4941 1.2378 -0.3489 -0.3485 0.0108 519 PRO A N 3993 C CA . PRO A 519 ? 1.4233 1.4664 1.2800 -0.3491 -0.3444 0.0301 519 PRO A CA 3994 C C . PRO A 519 ? 1.5539 1.5932 1.3960 -0.3521 -0.3336 0.0484 519 PRO A C 3995 O O . PRO A 519 ? 1.6026 1.6000 1.4461 -0.3537 -0.3286 0.0703 519 PRO A O 3996 C CB . PRO A 519 ? 1.4392 1.4569 1.3241 -0.3408 -0.3534 0.0008 519 PRO A CB 3997 C CG . PRO A 519 ? 1.4638 1.5191 1.3611 -0.3359 -0.3653 -0.0319 519 PRO A CG 3998 C CD . PRO A 519 ? 1.4430 1.5627 1.3149 -0.3391 -0.3596 -0.0327 519 PRO A CD 3999 N N . SER A 520 ? 1.6037 1.6910 1.4334 -0.3528 -0.3308 0.0383 520 SER A N 4000 C CA . SER A 520 ? 1.5207 1.6079 1.3384 -0.3558 -0.3219 0.0539 520 SER A CA 4001 C C . SER A 520 ? 1.4510 1.5914 1.2492 -0.3657 -0.3192 0.0766 520 SER A C 4002 O O . SER A 520 ? 1.5129 1.7105 1.3049 -0.3682 -0.3233 0.0680 520 SER A O 4003 C CB . SER A 520 ? 1.5802 1.6747 1.4045 -0.3480 -0.3216 0.0228 520 SER A CB 4004 O OG . SER A 520 ? 1.6991 1.8557 1.5224 -0.3445 -0.3271 -0.0079 520 SER A OG 4005 N N . HIS A 521 ? 1.4613 1.5858 1.2531 -0.3716 -0.3136 0.1065 521 HIS A N 4006 C CA . HIS A 521 ? 1.5828 1.7557 1.3622 -0.3830 -0.3135 0.1345 521 HIS A CA 4007 C C . HIS A 521 ? 1.5298 1.6889 1.3062 -0.3856 -0.3079 0.1510 521 HIS A C 4008 O O . HIS A 521 ? 1.4962 1.5970 1.2810 -0.3806 -0.3043 0.1539 521 HIS A O 4009 C CB . HIS A 521 ? 1.6612 1.8274 1.4442 -0.3916 -0.3189 0.1674 521 HIS A CB 4010 C CG . HIS A 521 ? 1.6148 1.8367 1.3914 -0.4056 -0.3228 0.1998 521 HIS A CG 4011 N ND1 . HIS A 521 ? 1.5470 1.7603 1.3277 -0.4133 -0.3235 0.2319 521 HIS A ND1 4012 C CD2 . HIS A 521 ? 1.6243 1.9151 1.3939 -0.4143 -0.3277 0.2073 521 HIS A CD2 4013 C CE1 . HIS A 521 ? 1.6086 1.8819 1.3869 -0.4273 -0.3299 0.2608 521 HIS A CE1 4014 N NE2 . HIS A 521 ? 1.6929 2.0168 1.4632 -0.4285 -0.3318 0.2470 521 HIS A NE2 4015 N N . SER A 522 ? 1.5137 1.7314 1.2790 -0.3937 -0.3077 0.1624 522 SER A N 4016 C CA . SER A 522 ? 1.5299 1.7408 1.2926 -0.3972 -0.3035 0.1795 522 SER A CA 4017 C C . SER A 522 ? 1.6981 1.9551 1.4592 -0.4133 -0.3094 0.2217 522 SER A C 4018 O O . SER A 522 ? 1.9410 2.2615 1.6966 -0.4218 -0.3147 0.2303 522 SER A O 4019 C CB . SER A 522 ? 1.5036 1.7416 1.2572 -0.3902 -0.2977 0.1471 522 SER A CB 4020 O OG . SER A 522 ? 1.5484 1.8692 1.2916 -0.3928 -0.3005 0.1319 522 SER A OG 4021 N N . LYS A 523 ? 1.6136 1.8409 1.3827 -0.4179 -0.3100 0.2491 523 LYS A N 4022 C CA . LYS A 523 ? 1.6552 1.9201 1.4310 -0.4345 -0.3192 0.2940 523 LYS A CA 4023 C C . LYS A 523 ? 1.6780 1.9289 1.4577 -0.4373 -0.3177 0.3099 523 LYS A C 4024 O O . LYS A 523 ? 1.6156 1.8043 1.4004 -0.4267 -0.3116 0.2961 523 LYS A O 4025 C CB . LYS A 523 ? 1.7065 1.9386 1.5035 -0.4400 -0.3303 0.3235 523 LYS A CB 4026 C CG . LYS A 523 ? 1.7283 2.0029 1.5402 -0.4590 -0.3446 0.3734 523 LYS A CG 4027 C CD . LYS A 523 ? 1.6874 2.0582 1.4835 -0.4708 -0.3465 0.3805 523 LYS A CD 4028 C CE . LYS A 523 ? 1.6684 2.0870 1.4834 -0.4926 -0.3629 0.4367 523 LYS A CE 4029 N NZ . LYS A 523 ? 1.6167 1.9941 1.4593 -0.4967 -0.3765 0.4625 523 LYS A NZ 4030 N N . ASN A 524 ? 1.8492 2.1627 1.6275 -0.4523 -0.3239 0.3404 524 ASN A N 4031 C CA . ASN A 524 ? 1.8991 2.2055 1.6835 -0.4574 -0.3249 0.3614 524 ASN A CA 4032 C C . ASN A 524 ? 1.7729 2.0371 1.5899 -0.4657 -0.3395 0.4030 524 ASN A C 4033 O O . ASN A 524 ? 1.8080 2.0967 1.6415 -0.4783 -0.3536 0.4358 524 ASN A O 4034 C CB . ASN A 524 ? 2.0185 2.4188 1.7886 -0.4706 -0.3262 0.3763 524 ASN A CB 4035 C CG . ASN A 524 ? 2.1983 2.6452 1.9410 -0.4603 -0.3139 0.3293 524 ASN A CG 4036 O OD1 . ASN A 524 ? 2.0564 2.4680 1.7939 -0.4451 -0.3068 0.2889 524 ASN A OD1 4037 N ND2 . ASN A 524 ? 2.5644 3.0943 2.2931 -0.4684 -0.3131 0.3340 524 ASN A ND2 4038 N N . MET A 525 ? 1.6248 1.8273 1.4544 -0.4581 -0.3376 0.4004 525 MET A N 4039 C CA . MET A 525 ? 1.6099 1.7662 1.4767 -0.4618 -0.3530 0.4309 525 MET A CA 4040 C C . MET A 525 ? 1.7174 1.8708 1.5995 -0.4686 -0.3593 0.4553 525 MET A C 4041 O O . MET A 525 ? 1.8077 1.9776 1.6680 -0.4663 -0.3474 0.4415 525 MET A O 4042 C CB . MET A 525 ? 1.5831 1.6628 1.4600 -0.4441 -0.3482 0.4028 525 MET A CB 4043 C CG . MET A 525 ? 1.5885 1.6551 1.4795 -0.4435 -0.3570 0.4064 525 MET A CG 4044 S SD . MET A 525 ? 1.4812 1.4681 1.3883 -0.4239 -0.3535 0.3776 525 MET A SD 4045 C CE . MET A 525 ? 2.3028 2.2885 2.2327 -0.4283 -0.3697 0.3949 525 MET A CE 4046 N N . THR A 526 ? 1.6994 1.8314 1.6223 -0.4767 -0.3798 0.4912 526 THR A N 4047 C CA . THR A 526 ? 1.5914 1.7128 1.5382 -0.4828 -0.3899 0.5161 526 THR A CA 4048 C C . THR A 526 ? 1.5258 1.5800 1.5204 -0.4760 -0.4066 0.5229 526 THR A C 4049 O O . THR A 526 ? 1.5590 1.6057 1.5854 -0.4809 -0.4249 0.5428 526 THR A O 4050 C CB . THR A 526 ? 1.5111 1.7057 1.4684 -0.5074 -0.4060 0.5673 526 THR A CB 4051 O OG1 . THR A 526 ? 1.4426 1.7092 1.3560 -0.5121 -0.3904 0.5560 526 THR A OG1 4052 C CG2 . THR A 526 ? 1.5313 1.7129 1.5174 -0.5145 -0.4187 0.5953 526 THR A CG2 4053 N N . ILE A 527 ? 1.4240 1.4327 1.4255 -0.4641 -0.4010 0.5046 527 ILE A N 4054 C CA . ILE A 527 ? 1.4999 1.4512 1.5499 -0.4556 -0.4176 0.5057 527 ILE A CA 4055 C C . ILE A 527 ? 1.5423 1.4933 1.6210 -0.4642 -0.4317 0.5336 527 ILE A C 4056 O O . ILE A 527 ? 1.6618 1.6571 1.7179 -0.4764 -0.4261 0.5511 527 ILE A O 4057 C CB . ILE A 527 ? 1.5019 1.4004 1.5412 -0.4320 -0.4003 0.4565 527 ILE A CB 4058 C CG1 . ILE A 527 ? 1.4312 1.3416 1.4249 -0.4252 -0.3783 0.4261 527 ILE A CG1 4059 C CG2 . ILE A 527 ? 1.6059 1.4596 1.6939 -0.4216 -0.4184 0.4511 527 ILE A CG2 4060 C CD1 . ILE A 527 ? 1.5229 1.4403 1.5244 -0.4277 -0.3870 0.4316 527 ILE A CD1 4061 N N . SER A 528 ? 1.4593 1.3643 1.5899 -0.4575 -0.4512 0.5365 528 SER A N 4062 C CA . SER A 528 ? 1.5957 1.4944 1.7588 -0.4640 -0.4663 0.5601 528 SER A CA 4063 C C . SER A 528 ? 1.5453 1.3864 1.7307 -0.4432 -0.4644 0.5256 528 SER A C 4064 O O . SER A 528 ? 1.3876 1.2224 1.5482 -0.4370 -0.4469 0.5082 528 SER A O 4065 C CB . SER A 528 ? 1.7783 1.6913 2.0015 -0.4829 -0.5036 0.6129 528 SER A CB 4066 O OG . SER A 528 ? 1.8907 1.7551 2.1705 -0.4714 -0.5258 0.6033 528 SER A OG 4067 N N . ARG A 529 ? 1.5877 1.3912 1.8213 -0.4320 -0.4830 0.5146 529 ARG A N 4068 C CA . ARG A 529 ? 1.5812 1.3391 1.8464 -0.4120 -0.4864 0.4821 529 ARG A CA 4069 C C . ARG A 529 ? 1.8073 1.5412 2.0660 -0.3911 -0.4751 0.4373 529 ARG A C 4070 O O . ARG A 529 ? 1.9340 1.6825 2.1610 -0.3925 -0.4634 0.4320 529 ARG A O 4071 C CB . ARG A 529 ? 1.5490 1.2883 1.8934 -0.4166 -0.5259 0.5087 529 ARG A CB 4072 C CG . ARG A 529 ? 1.6871 1.3952 2.0615 -0.4032 -0.5305 0.4882 529 ARG A CG 4073 C CD . ARG A 529 ? 1.7273 1.4308 2.1816 -0.3964 -0.5685 0.5036 529 ARG A CD 4074 N NE . ARG A 529 ? 1.6675 1.4143 2.1329 -0.4140 -0.5835 0.5527 529 ARG A NE 4075 C CZ . ARG A 529 ? 1.6380 1.3924 2.1716 -0.4124 -0.6179 0.5747 529 ARG A CZ 4076 N NH1 . ARG A 529 ? 1.6913 1.4102 2.2883 -0.3918 -0.6408 0.5498 529 ARG A NH1 4077 N NH2 . ARG A 529 ? 1.5889 1.3912 2.1309 -0.4316 -0.6310 0.6206 529 ARG A NH2 4078 N N . GLY A 530 ? 1.8625 1.5646 2.1517 -0.3717 -0.4788 0.4047 530 GLY A N 4079 C CA . GLY A 530 ? 1.8393 1.5272 2.1264 -0.3517 -0.4695 0.3624 530 GLY A CA 4080 C C . GLY A 530 ? 1.7522 1.4318 2.0900 -0.3485 -0.4968 0.3653 530 GLY A C 4081 O O . GLY A 530 ? 1.6458 1.3175 2.0423 -0.3554 -0.5294 0.3909 530 GLY A O 4082 N N . GLY A 531 ? 1.7701 1.4522 2.0883 -0.3384 -0.4852 0.3401 531 GLY A N 4083 C CA . GLY A 531 ? 1.8928 1.5695 2.2536 -0.3344 -0.5085 0.3395 531 GLY A CA 4084 C C . GLY A 531 ? 2.0108 1.7040 2.3704 -0.3561 -0.5210 0.3839 531 GLY A C 4085 O O . GLY A 531 ? 2.0274 1.7168 2.4274 -0.3570 -0.5446 0.3932 531 GLY A O 4086 N N . LEU A 532 ? 2.0608 1.7772 2.3746 -0.3734 -0.5054 0.4103 532 LEU A N 4087 C CA . LEU A 532 ? 2.0409 1.7864 2.3498 -0.3963 -0.5155 0.4554 532 LEU A CA 4088 C C . LEU A 532 ? 1.9838 1.7512 2.2393 -0.3988 -0.4940 0.4478 532 LEU A C 4089 O O . LEU A 532 ? 1.9146 1.7159 2.1533 -0.4172 -0.4958 0.4804 532 LEU A O 4090 C CB . LEU A 532 ? 1.9936 1.7637 2.2863 -0.4142 -0.5130 0.4889 532 LEU A CB 4091 C CG . LEU A 532 ? 1.9966 1.8007 2.3135 -0.4399 -0.5371 0.5458 532 LEU A CG 4092 C CD1 . LEU A 532 ? 2.0057 1.7983 2.3878 -0.4473 -0.5692 0.5761 532 LEU A CD1 4093 C CD2 . LEU A 532 ? 1.9925 1.8487 2.2485 -0.4565 -0.5154 0.5647 532 LEU A CD2 4094 N N . MET A 533 ? 1.8812 1.6338 2.1123 -0.3808 -0.4747 0.4058 533 MET A N 4095 C CA . MET A 533 ? 1.6802 1.4512 1.8533 -0.3815 -0.4489 0.3924 533 MET A CA 4096 C C . MET A 533 ? 1.6194 1.4186 1.7858 -0.3973 -0.4569 0.4213 533 MET A C 4097 O O . MET A 533 ? 1.7801 1.5734 1.9854 -0.3990 -0.4789 0.4342 533 MET A O 4098 C CB . MET A 533 ? 1.6807 1.4327 1.8473 -0.3618 -0.4374 0.3511 533 MET A CB 4099 C CG . MET A 533 ? 1.7361 1.4671 1.9151 -0.3446 -0.4314 0.3202 533 MET A CG 4100 S SD . MET A 533 ? 2.1915 1.9215 2.3381 -0.3275 -0.4068 0.2774 533 MET A SD 4101 C CE . MET A 533 ? 1.2398 0.9704 1.4129 -0.3232 -0.4237 0.2748 533 MET A CE 4102 N N . GLN A 534 ? 1.5555 1.3885 1.6738 -0.4084 -0.4393 0.4295 534 GLN A N 4103 C CA . GLN A 534 ? 1.6033 1.4753 1.7099 -0.4247 -0.4443 0.4569 534 GLN A CA 4104 C C . GLN A 534 ? 1.6868 1.5675 1.7494 -0.4183 -0.4234 0.4298 534 GLN A C 4105 O O . GLN A 534 ? 1.7709 1.6558 1.7937 -0.4125 -0.4008 0.4051 534 GLN A O 4106 C CB . GLN A 534 ? 1.5306 1.4484 1.6217 -0.4435 -0.4442 0.4890 534 GLN A CB 4107 C CG . GLN A 534 ? 1.5744 1.5477 1.6401 -0.4590 -0.4422 0.5092 534 GLN A CG 4108 C CD . GLN A 534 ? 1.6391 1.6695 1.6911 -0.4775 -0.4428 0.5403 534 GLN A CD 4109 O OE1 . GLN A 534 ? 1.6336 1.6608 1.7101 -0.4837 -0.4541 0.5621 534 GLN A OE1 4110 N NE2 . GLN A 534 ? 1.6410 1.7282 1.6552 -0.4860 -0.4313 0.5414 534 GLN A NE2 4111 N N . CYS A 535 ? 1.6103 1.4928 1.6838 -0.4196 -0.4326 0.4347 535 CYS A N 4112 C CA . CYS A 535 ? 1.5648 1.4529 1.6026 -0.4134 -0.4158 0.4100 535 CYS A CA 4113 C C . CYS A 535 ? 1.5353 1.4734 1.5496 -0.4289 -0.4146 0.4297 535 CYS A C 4114 O O . CYS A 535 ? 1.5867 1.5603 1.6125 -0.4456 -0.4271 0.4656 535 CYS A O 4115 C CB . CYS A 535 ? 1.6245 1.4817 1.6868 -0.4015 -0.4241 0.3950 535 CYS A CB 4116 S SG . CYS A 535 ? 2.2446 2.0561 2.3386 -0.3814 -0.4271 0.3670 535 CYS A SG 4117 N N . GLU A 536 ? 1.5422 1.4868 1.5258 -0.4236 -0.4005 0.4064 536 GLU A N 4118 C CA . GLU A 536 ? 1.6642 1.6569 1.6271 -0.4353 -0.3995 0.4180 536 GLU A CA 4119 C C . GLU A 536 ? 1.6406 1.6183 1.5946 -0.4266 -0.3947 0.3965 536 GLU A C 4120 O O . GLU A 536 ? 1.4968 1.4397 1.4428 -0.4120 -0.3839 0.3656 536 GLU A O 4121 C CB . GLU A 536 ? 1.7029 1.7381 1.6281 -0.4393 -0.3836 0.4075 536 GLU A CB 4122 C CG . GLU A 536 ? 1.7053 1.7852 1.6357 -0.4553 -0.3914 0.4407 536 GLU A CG 4123 C CD . GLU A 536 ? 1.8185 1.9588 1.7121 -0.4604 -0.3782 0.4302 536 GLU A CD 4124 O OE1 . GLU A 536 ? 2.0249 2.1702 1.8927 -0.4515 -0.3652 0.3969 536 GLU A OE1 4125 O OE2 . GLU A 536 ? 1.7315 1.9173 1.6246 -0.4731 -0.3824 0.4547 536 GLU A OE2 4126 N N . GLU A 537 ? 1.7038 1.7112 1.6602 -0.4366 -0.4035 0.4151 537 GLU A N 4127 C CA . GLU A 537 ? 1.6465 1.6406 1.5974 -0.4297 -0.4013 0.3987 537 GLU A CA 4128 C C . GLU A 537 ? 1.5987 1.6338 1.5141 -0.4329 -0.3892 0.3847 537 GLU A C 4129 O O . GLU A 537 ? 1.7896 1.8768 1.6996 -0.4466 -0.3944 0.4060 537 GLU A O 4130 C CB . GLU A 537 ? 1.7136 1.7045 1.6988 -0.4365 -0.4221 0.4266 537 GLU A CB 4131 C CG . GLU A 537 ? 1.7794 1.7399 1.7693 -0.4252 -0.4223 0.4075 537 GLU A CG 4132 C CD . GLU A 537 ? 1.7416 1.6532 1.7454 -0.4078 -0.4196 0.3818 537 GLU A CD 4133 O OE1 . GLU A 537 ? 1.5870 1.4830 1.6084 -0.4052 -0.4233 0.3845 537 GLU A OE1 4134 O OE2 . GLU A 537 ? 1.7853 1.6788 1.7829 -0.3971 -0.4140 0.3593 537 GLU A OE2 4135 N N . LEU A 538 ? 1.4839 1.4992 1.3787 -0.4204 -0.3748 0.3490 538 LEU A N 4136 C CA . LEU A 538 ? 1.5163 1.5640 1.3843 -0.4204 -0.3659 0.3293 538 LEU A CA 4137 C C . LEU A 538 ? 1.6310 1.6544 1.4998 -0.4131 -0.3659 0.3146 538 LEU A C 4138 O O . LEU A 538 ? 1.6828 1.6612 1.5649 -0.4038 -0.3666 0.3074 538 LEU A O 4139 C CB . LEU A 538 ? 1.4285 1.4782 1.2764 -0.4132 -0.3521 0.2998 538 LEU A CB 4140 C CG . LEU A 538 ? 1.4426 1.5436 1.2774 -0.4214 -0.3494 0.3055 538 LEU A CG 4141 C CD1 . LEU A 538 ? 1.5558 1.6507 1.4066 -0.4282 -0.3557 0.3347 538 LEU A CD1 4142 C CD2 . LEU A 538 ? 1.4139 1.5167 1.2308 -0.4119 -0.3371 0.2689 538 LEU A CD2 4143 N N . ILE A 539 ? 1.5180 1.5765 1.3732 -0.4173 -0.3656 0.3097 539 ILE A N 4144 C CA . ILE A 539 ? 1.3838 1.4235 1.2388 -0.4114 -0.3660 0.2965 539 ILE A CA 4145 C C . ILE A 539 ? 1.3356 1.3838 1.1727 -0.4046 -0.3570 0.2625 539 ILE A C 4146 O O . ILE A 539 ? 1.4138 1.5098 1.2377 -0.4088 -0.3553 0.2541 539 ILE A O 4147 C CB . ILE A 539 ? 1.5024 1.5714 1.3625 -0.4215 -0.3761 0.3194 539 ILE A CB 4148 C CG1 . ILE A 539 ? 1.5787 1.6351 1.4660 -0.4282 -0.3896 0.3538 539 ILE A CG1 4149 C CG2 . ILE A 539 ? 1.5023 1.5532 1.3600 -0.4151 -0.3757 0.3039 539 ILE A CG2 4150 C CD1 . ILE A 539 ? 1.6121 1.7125 1.5048 -0.4428 -0.3965 0.3842 539 ILE A CD1 4151 N N . ALA A 540 ? 1.3146 1.3206 1.1554 -0.3940 -0.3529 0.2429 540 ALA A N 4152 C CA . ALA A 540 ? 1.3165 1.3235 1.1499 -0.3877 -0.3486 0.2126 540 ALA A CA 4153 C C . ALA A 540 ? 1.3119 1.3012 1.1508 -0.3846 -0.3527 0.2080 540 ALA A C 4154 O O . ALA A 540 ? 1.4020 1.3580 1.2514 -0.3812 -0.3543 0.2166 540 ALA A O 4155 C CB . ALA A 540 ? 1.3458 1.3237 1.1822 -0.3799 -0.3422 0.1961 540 ALA A CB 4156 N N . TYR A 541 ? 1.3061 1.3217 1.1391 -0.3854 -0.3550 0.1931 541 TYR A N 4157 C CA . TYR A 541 ? 1.2917 1.2934 1.1299 -0.3835 -0.3597 0.1898 541 TYR A CA 4158 C C . TYR A 541 ? 1.2600 1.2352 1.1077 -0.3759 -0.3601 0.1669 541 TYR A C 4159 O O . TYR A 541 ? 1.2526 1.2198 1.1037 -0.3720 -0.3570 0.1527 541 TYR A O 4160 C CB . TYR A 541 ? 1.3913 1.4367 1.2217 -0.3889 -0.3640 0.1877 541 TYR A CB 4161 C CG . TYR A 541 ? 1.4741 1.5562 1.3000 -0.3863 -0.3640 0.1581 541 TYR A CG 4162 C CD1 . TYR A 541 ? 1.5284 1.6557 1.3448 -0.3899 -0.3610 0.1559 541 TYR A CD1 4163 C CD2 . TYR A 541 ? 1.4494 1.5250 1.2844 -0.3801 -0.3689 0.1314 541 TYR A CD2 4164 C CE1 . TYR A 541 ? 1.4707 1.6388 1.2855 -0.3858 -0.3621 0.1240 541 TYR A CE1 4165 C CE2 . TYR A 541 ? 1.4125 1.5233 1.2500 -0.3759 -0.3718 0.0993 541 TYR A CE2 4166 C CZ . TYR A 541 ? 1.4047 1.5634 1.2315 -0.3779 -0.3680 0.0937 541 TYR A CZ 4167 O OH . TYR A 541 ? 1.3792 1.5800 1.2108 -0.3720 -0.3720 0.0571 541 TYR A OH 4168 N N . LEU A 542 ? 1.2594 1.2223 1.1139 -0.3748 -0.3653 0.1656 542 LEU A N 4169 C CA . LEU A 542 ? 1.2283 1.1693 1.0973 -0.3701 -0.3694 0.1493 542 LEU A CA 4170 C C . LEU A 542 ? 1.2383 1.1996 1.1113 -0.3701 -0.3774 0.1312 542 LEU A C 4171 O O . LEU A 542 ? 1.1831 1.1582 1.0498 -0.3734 -0.3799 0.1393 542 LEU A O 4172 C CB . LEU A 542 ? 1.1994 1.1108 1.0776 -0.3689 -0.3704 0.1647 542 LEU A CB 4173 C CG . LEU A 542 ? 1.1876 1.0779 1.0845 -0.3662 -0.3748 0.1571 542 LEU A CG 4174 C CD1 . LEU A 542 ? 1.1846 1.0657 1.0871 -0.3636 -0.3706 0.1489 542 LEU A CD1 4175 C CD2 . LEU A 542 ? 1.1745 1.0510 1.0782 -0.3661 -0.3758 0.1744 542 LEU A CD2 4176 N N . ARG A 543 ? 1.2519 1.2154 1.1387 -0.3659 -0.3827 0.1053 543 ARG A N 4177 C CA . ARG A 543 ? 1.3082 1.2945 1.2042 -0.3640 -0.3925 0.0816 543 ARG A CA 4178 C C . ARG A 543 ? 1.4743 1.4416 1.3819 -0.3655 -0.4006 0.0893 543 ARG A C 4179 O O . ARG A 543 ? 1.4874 1.4234 1.4013 -0.3668 -0.4002 0.1080 543 ARG A O 4180 C CB . ARG A 543 ? 1.3116 1.3000 1.2290 -0.3576 -0.4002 0.0496 543 ARG A CB 4181 C CG . ARG A 543 ? 1.5122 1.4578 1.4559 -0.3561 -0.4069 0.0517 543 ARG A CG 4182 C CD . ARG A 543 ? 1.5924 1.5404 1.5654 -0.3497 -0.4193 0.0183 543 ARG A CD 4183 N NE . ARG A 543 ? 1.5302 1.4986 1.4926 -0.3461 -0.4119 0.0031 543 ARG A NE 4184 C CZ . ARG A 543 ? 1.4136 1.4283 1.3689 -0.3419 -0.4126 -0.0236 543 ARG A CZ 4185 N NH1 . ARG A 543 ? 1.3656 1.4110 1.3238 -0.3406 -0.4202 -0.0396 543 ARG A NH1 4186 N NH2 . ARG A 543 ? 1.3825 1.4180 1.3280 -0.3392 -0.4057 -0.0349 543 ARG A NH2 4187 N N . ASP A 544 ? 1.5737 1.5656 1.4843 -0.3651 -0.4082 0.0743 544 ASP A N 4188 C CA . ASP A 544 ? 1.4336 1.4132 1.3526 -0.3672 -0.4159 0.0822 544 ASP A CA 4189 C C . ASP A 544 ? 1.3987 1.3417 1.3464 -0.3663 -0.4262 0.0834 544 ASP A C 4190 O O . ASP A 544 ? 1.3813 1.3147 1.3511 -0.3629 -0.4329 0.0668 544 ASP A O 4191 C CB . ASP A 544 ? 1.4475 1.4628 1.3694 -0.3657 -0.4238 0.0591 544 ASP A CB 4192 C CG . ASP A 544 ? 1.6653 1.6715 1.5911 -0.3687 -0.4303 0.0700 544 ASP A CG 4193 O OD1 . ASP A 544 ? 1.8023 1.8216 1.7063 -0.3734 -0.4233 0.0894 544 ASP A OD1 4194 O OD2 . ASP A 544 ? 1.7189 1.7054 1.6721 -0.3669 -0.4437 0.0603 544 ASP A OD2 4195 N N . GLU A 545 ? 1.4196 1.3461 1.3689 -0.3702 -0.4283 0.1049 545 GLU A N 4196 C CA . GLU A 545 ? 1.4628 1.3627 1.4387 -0.3722 -0.4382 0.1150 545 GLU A CA 4197 C C . GLU A 545 ? 1.4358 1.3313 1.4488 -0.3703 -0.4570 0.0920 545 GLU A C 4198 O O . GLU A 545 ? 1.4126 1.2884 1.4548 -0.3720 -0.4668 0.0967 545 GLU A O 4199 C CB . GLU A 545 ? 1.6754 1.5711 1.6457 -0.3766 -0.4389 0.1383 545 GLU A CB 4200 C CG . GLU A 545 ? 1.7896 1.6935 1.7287 -0.3771 -0.4248 0.1554 545 GLU A CG 4201 C CD . GLU A 545 ? 1.7181 1.6241 1.6522 -0.3801 -0.4274 0.1710 545 GLU A CD 4202 O OE1 . GLU A 545 ? 1.5266 1.4411 1.4402 -0.3805 -0.4196 0.1820 545 GLU A OE1 4203 O OE2 . GLU A 545 ? 1.7431 1.6428 1.6967 -0.3826 -0.4388 0.1732 545 GLU A OE2 4204 N N . SER A 546 ? 1.5095 1.4267 1.5251 -0.3669 -0.4637 0.0669 546 SER A N 4205 C CA . SER A 546 ? 1.6181 1.5334 1.6750 -0.3635 -0.4852 0.0403 546 SER A CA 4206 C C . SER A 546 ? 1.4973 1.4221 1.5707 -0.3561 -0.4899 0.0075 546 SER A C 4207 O O . SER A 546 ? 1.4409 1.3614 1.5568 -0.3518 -0.5105 -0.0180 546 SER A O 4208 C CB . SER A 546 ? 1.7508 1.6893 1.8067 -0.3620 -0.4921 0.0248 546 SER A CB 4209 O OG . SER A 546 ? 1.8048 1.7352 1.8453 -0.3686 -0.4881 0.0541 546 SER A OG 4210 N N . GLU A 547 ? 1.4625 1.4010 1.5059 -0.3544 -0.4725 0.0077 547 GLU A N 4211 C CA . GLU A 547 ? 1.4770 1.4305 1.5314 -0.3471 -0.4750 -0.0236 547 GLU A CA 4212 C C . GLU A 547 ? 1.4246 1.3437 1.5113 -0.3471 -0.4838 -0.0206 547 GLU A C 4213 O O . GLU A 547 ? 1.3988 1.3243 1.5061 -0.3404 -0.4912 -0.0492 547 GLU A O 4214 C CB . GLU A 547 ? 1.5168 1.4989 1.5291 -0.3468 -0.4542 -0.0200 547 GLU A CB 4215 C CG . GLU A 547 ? 1.5874 1.6150 1.5726 -0.3475 -0.4477 -0.0250 547 GLU A CG 4216 C CD . GLU A 547 ? 1.6276 1.6904 1.5795 -0.3487 -0.4314 -0.0209 547 GLU A CD 4217 O OE1 . GLU A 547 ? 1.5837 1.6433 1.5379 -0.3457 -0.4279 -0.0290 547 GLU A OE1 4218 O OE2 . GLU A 547 ? 1.6935 1.7882 1.6189 -0.3536 -0.4231 -0.0074 547 GLU A OE2 4219 N N . PHE A 548 ? 1.4499 1.3376 1.5421 -0.3547 -0.4836 0.0140 548 PHE A N 4220 C CA . PHE A 548 ? 1.4820 1.3421 1.6047 -0.3571 -0.4915 0.0238 548 PHE A CA 4221 C C . PHE A 548 ? 1.6072 1.4456 1.7468 -0.3667 -0.4985 0.0599 548 PHE A C 4222 O O . PHE A 548 ? 1.6282 1.4708 1.7558 -0.3706 -0.4974 0.0753 548 PHE A O 4223 C CB . PHE A 548 ? 1.3862 1.2458 1.4818 -0.3559 -0.4724 0.0305 548 PHE A CB 4224 C CG . PHE A 548 ? 1.4599 1.3188 1.5146 -0.3607 -0.4515 0.0630 548 PHE A CG 4225 C CD1 . PHE A 548 ? 1.4495 1.2962 1.4953 -0.3624 -0.4401 0.0807 548 PHE A CD1 4226 C CD2 . PHE A 548 ? 1.5166 1.3886 1.5450 -0.3626 -0.4444 0.0734 548 PHE A CD2 4227 C CE1 . PHE A 548 ? 1.3011 1.1488 1.3159 -0.3648 -0.4237 0.1055 548 PHE A CE1 4228 C CE2 . PHE A 548 ? 1.4145 1.2853 1.4127 -0.3656 -0.4286 0.0998 548 PHE A CE2 4229 C CZ . PHE A 548 ? 1.2993 1.1583 1.2922 -0.3661 -0.4189 0.1144 548 PHE A CZ 4230 N N . ARG A 549 ? 1.6452 1.4653 1.8133 -0.3709 -0.5060 0.0739 549 ARG A N 4231 C CA . ARG A 549 ? 1.6594 1.4683 1.8525 -0.3814 -0.5164 0.1089 549 ARG A CA 4232 C C . ARG A 549 ? 1.7216 1.5366 1.8775 -0.3855 -0.4946 0.1405 549 ARG A C 4233 O O . ARG A 549 ? 1.6641 1.4806 1.8343 -0.3941 -0.4991 0.1713 549 ARG A O 4234 C CB . ARG A 549 ? 1.6533 1.4461 1.9014 -0.3851 -0.5378 0.1104 549 ARG A CB 4235 C CG . ARG A 549 ? 1.6610 1.4485 1.9518 -0.3977 -0.5586 0.1438 549 ARG A CG 4236 C CD . ARG A 549 ? 1.7610 1.5336 2.1115 -0.4023 -0.5822 0.1464 549 ARG A CD 4237 N NE . ARG A 549 ? 1.9318 1.7029 2.2668 -0.4006 -0.5667 0.1492 549 ARG A NE 4238 C CZ . ARG A 549 ? 1.9412 1.7003 2.3205 -0.4034 -0.5823 0.1498 549 ARG A CZ 4239 N NH1 . ARG A 549 ? 2.0328 1.7810 2.4712 -0.4003 -0.6077 0.1480 549 ARG A NH1 4240 N NH2 . ARG A 549 ? 1.7134 1.4727 2.0733 -0.4016 -0.5657 0.1523 549 ARG A NH2 4241 N N . ASP A 550 ? 1.9108 1.7342 2.0222 -0.3794 -0.4728 0.1320 550 ASP A N 4242 C CA . ASP A 550 ? 1.8973 1.7257 1.9770 -0.3802 -0.4530 0.1534 550 ASP A CA 4243 C C . ASP A 550 ? 1.5800 1.4018 1.6790 -0.3835 -0.4537 0.1663 550 ASP A C 4244 O O . ASP A 550 ? 1.4628 1.2742 1.5871 -0.3822 -0.4631 0.1514 550 ASP A O 4245 C CB . ASP A 550 ? 1.9942 1.8326 2.0621 -0.3847 -0.4504 0.1777 550 ASP A CB 4246 C CG . ASP A 550 ? 2.0215 1.8656 2.0771 -0.3831 -0.4532 0.1676 550 ASP A CG 4247 O OD1 . ASP A 550 ? 2.0799 1.9283 2.1183 -0.3776 -0.4479 0.1452 550 ASP A OD1 4248 O OD2 . ASP A 550 ? 1.9696 1.8184 2.0331 -0.3880 -0.4609 0.1831 550 ASP A OD2 4249 N N . LYS A 551 ? 1.4176 1.2496 1.5080 -0.3874 -0.4453 0.1928 551 LYS A N 4250 C CA . LYS A 551 ? 1.4141 1.2493 1.5207 -0.3915 -0.4445 0.2093 551 LYS A CA 4251 C C . LYS A 551 ? 1.3661 1.2242 1.4554 -0.3931 -0.4326 0.2325 551 LYS A C 4252 O O . LYS A 551 ? 1.2739 1.1398 1.3354 -0.3889 -0.4230 0.2317 551 LYS A O 4253 C CB . LYS A 551 ? 1.4853 1.3093 1.5822 -0.3854 -0.4343 0.1918 551 LYS A CB 4254 C CG . LYS A 551 ? 1.4777 1.2871 1.6131 -0.3872 -0.4503 0.1807 551 LYS A CG 4255 C CD . LYS A 551 ? 1.5845 1.3968 1.7665 -0.3982 -0.4716 0.2045 551 LYS A CD 4256 C CE . LYS A 551 ? 1.6600 1.4550 1.8860 -0.3985 -0.4965 0.1857 551 LYS A CE 4257 N NZ . LYS A 551 ? 1.6314 1.4244 1.8442 -0.3921 -0.4990 0.1611 551 LYS A NZ 4258 N N . LEU A 552 ? 1.3530 1.2259 1.4618 -0.3989 -0.4348 0.2523 552 LEU A N 4259 C CA . LEU A 552 ? 1.1550 1.0548 1.2466 -0.3971 -0.4206 0.2655 552 LEU A CA 4260 C C . LEU A 552 ? 1.1136 1.0033 1.1918 -0.3907 -0.4069 0.2532 552 LEU A C 4261 O O . LEU A 552 ? 1.0953 1.0038 1.1598 -0.3867 -0.3945 0.2575 552 LEU A O 4262 C CB . LEU A 552 ? 1.1276 1.0627 1.2474 -0.4078 -0.4304 0.2959 552 LEU A CB 4263 C CG . LEU A 552 ? 1.3241 1.2859 1.4461 -0.4125 -0.4374 0.3123 552 LEU A CG 4264 C CD1 . LEU A 552 ? 1.4077 1.4161 1.5576 -0.4241 -0.4463 0.3450 552 LEU A CD1 4265 C CD2 . LEU A 552 ? 1.3657 1.3366 1.4508 -0.4018 -0.4218 0.3003 552 LEU A CD2 4266 N N . THR A 553 ? 1.0930 0.9552 1.1773 -0.3890 -0.4104 0.2357 553 THR A N 4267 C CA . THR A 553 ? 1.0779 0.9289 1.1513 -0.3837 -0.3990 0.2233 553 THR A CA 4268 C C . THR A 553 ? 1.0623 0.9086 1.0973 -0.3744 -0.3825 0.2089 553 THR A C 4269 O O . THR A 553 ? 1.0821 0.9190 1.1026 -0.3714 -0.3830 0.1956 553 THR A O 4270 C CB . THR A 553 ? 1.1496 0.9770 1.2433 -0.3839 -0.4095 0.2059 553 THR A CB 4271 O OG1 . THR A 553 ? 1.2367 1.0651 1.3744 -0.3933 -0.4303 0.2201 553 THR A OG1 4272 C CG2 . THR A 553 ? 1.1323 0.9520 1.2188 -0.3799 -0.3988 0.1972 553 THR A CG2 4273 N N . PRO A 554 ? 1.0539 0.9097 1.0757 -0.3702 -0.3694 0.2126 554 PRO A N 4274 C CA . PRO A 554 ? 1.0393 0.8906 1.0323 -0.3623 -0.3568 0.2026 554 PRO A CA 4275 C C . PRO A 554 ? 1.1015 0.9332 1.0814 -0.3596 -0.3536 0.1847 554 PRO A C 4276 O O . PRO A 554 ? 1.0471 0.8691 1.0395 -0.3614 -0.3577 0.1767 554 PRO A O 4277 C CB . PRO A 554 ? 1.0291 0.8944 1.0219 -0.3588 -0.3472 0.2084 554 PRO A CB 4278 C CG . PRO A 554 ? 1.0479 0.9377 1.0649 -0.3653 -0.3541 0.2255 554 PRO A CG 4279 C CD . PRO A 554 ? 1.0520 0.9278 1.0897 -0.3733 -0.3677 0.2278 554 PRO A CD 4280 N N . ILE A 555 ? 1.1206 0.9509 1.0783 -0.3559 -0.3479 0.1793 555 ILE A N 4281 C CA . ILE A 555 ? 1.1437 0.9670 1.0869 -0.3542 -0.3442 0.1652 555 ILE A CA 4282 C C . ILE A 555 ? 1.1423 0.9628 1.0754 -0.3505 -0.3332 0.1661 555 ILE A C 4283 O O . ILE A 555 ? 1.1731 0.9968 1.0981 -0.3477 -0.3288 0.1736 555 ILE A O 4284 C CB . ILE A 555 ? 1.1553 0.9855 1.0826 -0.3545 -0.3457 0.1628 555 ILE A CB 4285 C CG1 . ILE A 555 ? 1.0924 0.9256 1.0303 -0.3576 -0.3568 0.1605 555 ILE A CG1 4286 C CG2 . ILE A 555 ? 1.1705 1.0060 1.0833 -0.3539 -0.3421 0.1503 555 ILE A CG2 4287 C CD1 . ILE A 555 ? 1.1072 0.9509 1.0302 -0.3585 -0.3585 0.1589 555 ILE A CD1 4288 N N . THR A 556 ? 1.1488 0.9627 1.0857 -0.3502 -0.3306 0.1575 556 THR A N 4289 C CA . THR A 556 ? 1.1711 0.9815 1.1000 -0.3470 -0.3205 0.1584 556 THR A CA 4290 C C . THR A 556 ? 1.2658 1.0786 1.1759 -0.3464 -0.3164 0.1510 556 THR A C 4291 O O . THR A 556 ? 1.3018 1.1182 1.2098 -0.3472 -0.3184 0.1370 556 THR A O 4292 C CB . THR A 556 ? 1.2359 1.0402 1.1796 -0.3475 -0.3193 0.1553 556 THR A CB 4293 O OG1 . THR A 556 ? 1.5289 1.3284 1.4786 -0.3488 -0.3254 0.1399 556 THR A OG1 4294 C CG2 . THR A 556 ? 1.1464 0.9576 1.1114 -0.3504 -0.3245 0.1679 556 THR A CG2 4295 N N . ILE A 557 ? 1.2579 1.0732 1.1579 -0.3452 -0.3123 0.1605 557 ILE A N 4296 C CA . ILE A 557 ? 1.2790 1.1024 1.1639 -0.3468 -0.3096 0.1603 557 ILE A CA 4297 C C . ILE A 557 ? 1.0856 0.9025 0.9686 -0.3447 -0.3019 0.1578 557 ILE A C 4298 O O . ILE A 557 ? 1.0747 0.8824 0.9646 -0.3414 -0.2983 0.1642 557 ILE A O 4299 C CB . ILE A 557 ? 1.3129 1.1415 1.1946 -0.3481 -0.3125 0.1755 557 ILE A CB 4300 C CG1 . ILE A 557 ? 1.1084 0.9453 0.9898 -0.3507 -0.3197 0.1780 557 ILE A CG1 4301 C CG2 . ILE A 557 ? 1.3395 1.1811 1.2099 -0.3521 -0.3112 0.1814 557 ILE A CG2 4302 C CD1 . ILE A 557 ? 1.0989 0.9278 0.9933 -0.3475 -0.3230 0.1820 557 ILE A CD1 4303 N N . PHE A 558 ? 1.2103 1.0356 1.0847 -0.3460 -0.3000 0.1462 558 PHE A N 4304 C CA . PHE A 558 ? 1.2009 1.0203 1.0735 -0.3441 -0.2928 0.1413 558 PHE A CA 4305 C C . PHE A 558 ? 1.4059 1.2410 1.2633 -0.3468 -0.2896 0.1463 558 PHE A C 4306 O O . PHE A 558 ? 1.6429 1.5024 1.4898 -0.3497 -0.2916 0.1386 558 PHE A O 4307 C CB . PHE A 558 ? 1.2101 1.0278 1.0907 -0.3428 -0.2948 0.1222 558 PHE A CB 4308 C CG . PHE A 558 ? 1.1780 0.9882 1.0591 -0.3406 -0.2880 0.1164 558 PHE A CG 4309 C CD1 . PHE A 558 ? 1.1666 0.9600 1.0603 -0.3389 -0.2842 0.1226 558 PHE A CD1 4310 C CD2 . PHE A 558 ? 1.1986 1.0241 1.0678 -0.3404 -0.2854 0.1044 558 PHE A CD2 4311 C CE1 . PHE A 558 ? 1.2160 1.0029 1.1103 -0.3372 -0.2778 0.1177 558 PHE A CE1 4312 C CE2 . PHE A 558 ? 1.2752 1.0936 1.1446 -0.3383 -0.2792 0.0986 558 PHE A CE2 4313 C CZ . PHE A 558 ? 1.3294 1.1259 1.2114 -0.3367 -0.2753 0.1056 558 PHE A CZ 4314 N N . MET A 559 ? 1.3684 1.1943 1.2270 -0.3461 -0.2858 0.1592 559 MET A N 4315 C CA . MET A 559 ? 1.3180 1.1586 1.1664 -0.3501 -0.2844 0.1687 559 MET A CA 4316 C C . MET A 559 ? 1.3378 1.1729 1.1822 -0.3478 -0.2763 0.1607 559 MET A C 4317 O O . MET A 559 ? 1.3133 1.1268 1.1671 -0.3429 -0.2718 0.1587 559 MET A O 4318 C CB . MET A 559 ? 1.3094 1.1437 1.1676 -0.3516 -0.2895 0.1899 559 MET A CB 4319 C CG . MET A 559 ? 1.3137 1.1605 1.1682 -0.3569 -0.2902 0.2045 559 MET A CG 4320 S SD . MET A 559 ? 1.3454 1.1854 1.2221 -0.3600 -0.3026 0.2311 559 MET A SD 4321 C CE . MET A 559 ? 1.2656 1.0719 1.1630 -0.3476 -0.3003 0.2200 559 MET A CE 4322 N N . GLU A 560 ? 1.4492 1.3092 1.2799 -0.3513 -0.2747 0.1561 560 GLU A N 4323 C CA . GLU A 560 ? 1.4466 1.3051 1.2718 -0.3495 -0.2673 0.1486 560 GLU A CA 4324 C C . GLU A 560 ? 1.4598 1.3471 1.2730 -0.3562 -0.2676 0.1628 560 GLU A C 4325 O O . GLU A 560 ? 1.5429 1.4664 1.3475 -0.3623 -0.2725 0.1674 560 GLU A O 4326 C CB . GLU A 560 ? 1.5059 1.3704 1.3302 -0.3456 -0.2661 0.1218 560 GLU A CB 4327 C CG . GLU A 560 ? 1.7304 1.5875 1.5530 -0.3424 -0.2588 0.1116 560 GLU A CG 4328 C CD . GLU A 560 ? 1.8639 1.7233 1.6945 -0.3378 -0.2614 0.0839 560 GLU A CD 4329 O OE1 . GLU A 560 ? 1.8110 1.6886 1.6447 -0.3374 -0.2692 0.0699 560 GLU A OE1 4330 O OE2 . GLU A 560 ? 1.9482 1.7914 1.7853 -0.3344 -0.2572 0.0754 560 GLU A OE2 4331 N N . TYR A 561 ? 1.4429 1.3185 1.2571 -0.3559 -0.2629 0.1713 561 TYR A N 4332 C CA . TYR A 561 ? 1.4787 1.3817 1.2851 -0.3637 -0.2647 0.1894 561 TYR A CA 4333 C C . TYR A 561 ? 1.5438 1.4573 1.3381 -0.3622 -0.2564 0.1770 561 TYR A C 4334 O O . TYR A 561 ? 1.5718 1.4601 1.3684 -0.3547 -0.2493 0.1587 561 TYR A O 4335 C CB . TYR A 561 ? 1.4612 1.3441 1.2848 -0.3662 -0.2707 0.2153 561 TYR A CB 4336 C CG . TYR A 561 ? 1.4976 1.3378 1.3367 -0.3567 -0.2670 0.2080 561 TYR A CG 4337 C CD1 . TYR A 561 ? 1.5583 1.3836 1.3986 -0.3530 -0.2599 0.2045 561 TYR A CD1 4338 C CD2 . TYR A 561 ? 1.5192 1.3405 1.3721 -0.3516 -0.2706 0.2044 561 TYR A CD2 4339 C CE1 . TYR A 561 ? 1.6319 1.4277 1.4872 -0.3444 -0.2564 0.1970 561 TYR A CE1 4340 C CE2 . TYR A 561 ? 1.5614 1.3561 1.4289 -0.3431 -0.2673 0.1970 561 TYR A CE2 4341 C CZ . TYR A 561 ? 1.6656 1.4493 1.5346 -0.3394 -0.2602 0.1931 561 TYR A CZ 4342 O OH . TYR A 561 ? 1.7588 1.5250 1.6431 -0.3309 -0.2570 0.1849 561 TYR A OH 4343 N N . ARG A 562 ? 1.5874 1.5422 1.3703 -0.3702 -0.2581 0.1890 562 ARG A N 4344 C CA . ARG A 562 ? 1.6438 1.6221 1.4123 -0.3692 -0.2512 0.1745 562 ARG A CA 4345 C C . ARG A 562 ? 1.7171 1.6983 1.4848 -0.3750 -0.2501 0.1975 562 ARG A C 4346 O O . ARG A 562 ? 1.8200 1.7771 1.5870 -0.3696 -0.2422 0.1885 562 ARG A O 4347 C CB . ARG A 562 ? 1.6940 1.7344 1.4480 -0.3728 -0.2540 0.1621 562 ARG A CB 4348 C CG . ARG A 562 ? 1.6872 1.7533 1.4295 -0.3676 -0.2477 0.1343 562 ARG A CG 4349 C CD . ARG A 562 ? 1.7613 1.7829 1.5136 -0.3554 -0.2435 0.1034 562 ARG A CD 4350 N NE . ARG A 562 ? 1.8661 1.8782 1.6291 -0.3513 -0.2495 0.0882 562 ARG A NE 4351 C CZ . ARG A 562 ? 1.8644 1.8411 1.6425 -0.3429 -0.2500 0.0659 562 ARG A CZ 4352 N NH1 . ARG A 562 ? 1.8782 1.8266 1.6622 -0.3378 -0.2444 0.0563 562 ARG A NH1 4353 N NH2 . ARG A 562 ? 1.8048 1.7760 1.5942 -0.3406 -0.2572 0.0555 562 ARG A NH2 4354 N N . LEU A 563 ? 1.6974 1.7100 1.4677 -0.3868 -0.2593 0.2287 563 LEU A N 4355 C CA . LEU A 563 ? 1.7448 1.7689 1.5181 -0.3952 -0.2622 0.2557 563 LEU A CA 4356 C C . LEU A 563 ? 1.7633 1.8272 1.5155 -0.3960 -0.2542 0.2431 563 LEU A C 4357 O O . LEU A 563 ? 1.6573 1.6950 1.4071 -0.3900 -0.2458 0.2327 563 LEU A O 4358 C CB . LEU A 563 ? 1.7785 1.7429 1.5718 -0.3894 -0.2618 0.2622 563 LEU A CB 4359 C CG . LEU A 563 ? 1.7907 1.7556 1.5962 -0.3969 -0.2680 0.2909 563 LEU A CG 4360 C CD1 . LEU A 563 ? 1.8554 1.8493 1.6785 -0.4117 -0.2860 0.3303 563 LEU A CD1 4361 C CD2 . LEU A 563 ? 1.7421 1.6492 1.5678 -0.3871 -0.2662 0.2857 563 LEU A CD2 4362 N N . ASP A 564 ? 1.8390 1.9706 1.5763 -0.4027 -0.2567 0.2417 564 ASP A N 4363 C CA . ASP A 564 ? 1.7353 1.9213 1.4537 -0.4049 -0.2516 0.2323 564 ASP A CA 4364 C C . ASP A 564 ? 1.7063 1.8959 1.4292 -0.4150 -0.2545 0.2670 564 ASP A C 4365 O O . ASP A 564 ? 1.6490 1.8311 1.3903 -0.4257 -0.2660 0.3053 564 ASP A O 4366 C CB . ASP A 564 ? 1.6588 1.9304 1.3641 -0.4119 -0.2565 0.2293 564 ASP A CB 4367 C CG . ASP A 564 ? 1.7868 2.0563 1.4913 -0.4018 -0.2559 0.1942 564 ASP A CG 4368 O OD1 . ASP A 564 ? 1.8897 2.1054 1.5990 -0.3882 -0.2497 0.1631 564 ASP A OD1 4369 O OD2 . ASP A 564 ? 1.7994 2.1235 1.5010 -0.4082 -0.2627 0.1995 564 ASP A OD2 4370 N N . TYR A 565 ? 1.7137 1.9146 1.4233 -0.4118 -0.2459 0.2539 565 TYR A N 4371 C CA . TYR A 565 ? 1.5810 1.7729 1.2970 -0.4194 -0.2478 0.2835 565 TYR A CA 4372 C C . TYR A 565 ? 1.5068 1.7824 1.2115 -0.4347 -0.2533 0.3092 565 TYR A C 4373 O O . TYR A 565 ? 1.4876 1.8120 1.1708 -0.4318 -0.2456 0.2867 565 TYR A O 4374 C CB . TYR A 565 ? 1.6031 1.7459 1.3142 -0.4066 -0.2347 0.2571 565 TYR A CB 4375 C CG . TYR A 565 ? 1.6247 1.6979 1.3457 -0.3923 -0.2286 0.2307 565 TYR A CG 4376 C CD1 . TYR A 565 ? 1.6848 1.7030 1.4287 -0.3910 -0.2335 0.2468 565 TYR A CD1 4377 C CD2 . TYR A 565 ? 1.5725 1.6398 1.2840 -0.3803 -0.2200 0.1898 565 TYR A CD2 4378 C CE1 . TYR A 565 ? 1.6927 1.6583 1.4454 -0.3789 -0.2281 0.2245 565 TYR A CE1 4379 C CE2 . TYR A 565 ? 1.5817 1.5916 1.3052 -0.3696 -0.2161 0.1710 565 TYR A CE2 4380 C CZ . TYR A 565 ? 1.6025 1.5649 1.3444 -0.3694 -0.2193 0.1893 565 TYR A CZ 4381 O OH . TYR A 565 ? 1.5314 1.4473 1.2850 -0.3597 -0.2156 0.1724 565 TYR A OH 4382 N N . ARG A 566 ? 1.4970 1.7919 1.2198 -0.4512 -0.2684 0.3573 566 ARG A N 4383 C CA . ARG A 566 ? 1.5532 1.9214 1.2734 -0.4691 -0.2767 0.3946 566 ARG A CA 4384 C C . ARG A 566 ? 1.6103 1.9372 1.3637 -0.4797 -0.2914 0.4406 566 ARG A C 4385 O O . ARG A 566 ? 1.5381 1.8431 1.3192 -0.4859 -0.3060 0.4664 566 ARG A O 4386 C CB . ARG A 566 ? 1.6926 2.1533 1.4062 -0.4827 -0.2856 0.4116 566 ARG A CB 4387 C CG . ARG A 566 ? 1.7803 2.2990 1.4641 -0.4725 -0.2738 0.3643 566 ARG A CG 4388 C CD . ARG A 566 ? 1.8295 2.3902 1.4916 -0.4690 -0.2638 0.3446 566 ARG A CD 4389 N NE . ARG A 566 ? 1.8691 2.4910 1.5090 -0.4579 -0.2558 0.2954 566 ARG A NE 4390 C CZ . ARG A 566 ? 1.7928 2.3693 1.4266 -0.4373 -0.2449 0.2413 566 ARG A CZ 4391 N NH1 . ARG A 566 ? 1.7224 2.1965 1.3668 -0.4268 -0.2389 0.2321 566 ARG A NH1 4392 N NH2 . ARG A 566 ? 1.7323 2.3699 1.3530 -0.4274 -0.2418 0.1964 566 ARG A NH2 4393 N N . THR A 567 ? 1.6942 2.0145 1.4480 -0.4820 -0.2894 0.4509 567 THR A N 4394 C CA . THR A 567 ? 1.5883 1.8437 1.3760 -0.4836 -0.3000 0.4764 567 THR A CA 4395 C C . THR A 567 ? 1.5967 1.8634 1.3801 -0.4883 -0.2977 0.4889 567 THR A C 4396 O O . THR A 567 ? 1.6563 1.9753 1.4074 -0.4880 -0.2853 0.4726 567 THR A O 4397 C CB . THR A 567 ? 1.5212 1.6835 1.3176 -0.4629 -0.2905 0.4400 567 THR A CB 4398 O OG1 . THR A 567 ? 1.6679 1.8278 1.4311 -0.4476 -0.2697 0.3907 567 THR A OG1 4399 C CG2 . THR A 567 ? 1.4216 1.5503 1.2458 -0.4621 -0.3032 0.4487 567 THR A CG2 4400 N N . ALA A 568 ? 1.6468 1.8656 1.4655 -0.4921 -0.3109 0.5161 568 ALA A N 4401 C CA . ALA A 568 ? 1.6730 1.8848 1.4921 -0.4939 -0.3086 0.5250 568 ALA A CA 4402 C C . ALA A 568 ? 1.6052 1.9097 1.4073 -0.5127 -0.3125 0.5557 568 ALA A C 4403 O O . ALA A 568 ? 1.5384 1.8785 1.3031 -0.5072 -0.2948 0.5290 568 ALA A O 4404 C CB . ALA A 568 ? 1.7367 1.9015 1.5291 -0.4726 -0.2840 0.4731 568 ALA A CB 4405 N N . ALA A 569 ? 1.7453 2.0924 1.5780 -0.5350 -0.3372 0.6123 569 ALA A N 4406 C CA . ALA A 569 ? 1.8144 2.2642 1.6496 -0.5496 -0.3403 0.6345 569 ALA A CA 4407 C C . ALA A 569 ? 1.8124 2.2784 1.6298 -0.5464 -0.3277 0.6235 569 ALA A C 4408 O O . ALA A 569 ? 1.6742 2.0778 1.5105 -0.5401 -0.3298 0.6240 569 ALA A O 4409 C CB . ALA A 569 ? 1.7931 2.2686 1.6956 -0.5647 -0.3672 0.6798 569 ALA A CB 4410 N N . ASP A 570 ? 1.8940 2.4482 1.6776 -0.5495 -0.3144 0.6103 570 ASP A N 4411 C CA . ASP A 570 ? 1.9000 2.4812 1.6585 -0.5448 -0.2992 0.5922 570 ASP A CA 4412 C C . ASP A 570 ? 1.9276 2.4208 1.6515 -0.5281 -0.2846 0.5579 570 ASP A C 4413 O O . ASP A 570 ? 1.8231 2.2609 1.5353 -0.5130 -0.2756 0.5227 570 ASP A O 4414 C CB . ASP A 570 ? 1.8627 2.4702 1.6688 -0.5568 -0.3123 0.6289 570 ASP A CB 4415 C CG . ASP A 570 ? 1.8860 2.5939 1.7274 -0.5768 -0.3255 0.6645 570 ASP A CG 4416 O OD1 . ASP A 570 ? 1.8998 2.6826 1.7170 -0.5791 -0.3157 0.6516 570 ASP A OD1 4417 O OD2 . ASP A 570 ? 1.8738 2.5884 1.7701 -0.5902 -0.3465 0.7043 570 ASP A OD2 4418 N N . THR A 571 ? 2.0702 2.5481 1.7975 -0.5252 -0.2791 0.5570 571 THR A N 4419 C CA . THR A 571 ? 2.1359 2.5402 1.8361 -0.5092 -0.2621 0.5222 571 THR A CA 4420 C C . THR A 571 ? 2.0935 2.4959 1.7608 -0.4894 -0.2413 0.4612 571 THR A C 4421 O O . THR A 571 ? 2.0649 2.3904 1.7385 -0.4729 -0.2333 0.4295 571 THR A O 4422 C CB . THR A 571 ? 2.1170 2.4153 1.8543 -0.5006 -0.2683 0.5242 571 THR A CB 4423 O OG1 . THR A 571 ? 1.9353 2.2028 1.6854 -0.4942 -0.2719 0.5123 571 THR A OG1 4424 C CG2 . THR A 571 ? 2.2104 2.5054 2.0004 -0.5118 -0.2908 0.5690 571 THR A CG2 4425 N N . THR A 572 ? 2.0940 2.5844 1.7299 -0.4911 -0.2342 0.4446 572 THR A N 4426 C CA . THR A 572 ? 2.1243 2.6272 1.7373 -0.4745 -0.2209 0.3897 572 THR A CA 4427 C C . THR A 572 ? 1.9908 2.4669 1.6218 -0.4742 -0.2292 0.3932 572 THR A C 4428 O O . THR A 572 ? 1.9692 2.5035 1.6093 -0.4903 -0.2436 0.4283 572 THR A O 4429 C CB . THR A 572 ? 2.1632 2.5953 1.7649 -0.4522 -0.2023 0.3380 572 THR A CB 4430 O OG1 . THR A 572 ? 2.2481 2.6786 1.8423 -0.4542 -0.1969 0.3462 572 THR A OG1 4431 C CG2 . THR A 572 ? 2.0173 2.4886 1.5968 -0.4378 -0.1922 0.2833 572 THR A CG2 4432 N N . GLY A 573 ? 1.8195 2.2115 1.4563 -0.4565 -0.2204 0.3585 573 GLY A N 4433 C CA . GLY A 573 ? 1.6822 2.0310 1.3406 -0.4557 -0.2285 0.3656 573 GLY A CA 4434 C C . GLY A 573 ? 1.6971 1.9428 1.3689 -0.4395 -0.2204 0.3426 573 GLY A C 4435 O O . GLY A 573 ? 1.9137 2.1293 1.5726 -0.4264 -0.2059 0.3093 573 GLY A O 4436 N N . LEU A 574 ? 1.5228 1.7190 1.2224 -0.4407 -0.2306 0.3604 574 LEU A N 4437 C CA . LEU A 574 ? 1.4919 1.6009 1.2066 -0.4258 -0.2242 0.3396 574 LEU A CA 4438 C C . LEU A 574 ? 1.4652 1.5490 1.1931 -0.4212 -0.2291 0.3318 574 LEU A C 4439 O O . LEU A 574 ? 1.4739 1.5633 1.2239 -0.4313 -0.2452 0.3632 574 LEU A O 4440 C CB . LEU A 574 ? 1.4395 1.5058 1.1822 -0.4297 -0.2329 0.3682 574 LEU A CB 4441 C CG . LEU A 574 ? 1.4108 1.3988 1.1677 -0.4138 -0.2247 0.3447 574 LEU A CG 4442 C CD1 . LEU A 574 ? 1.2436 1.2216 0.9740 -0.4023 -0.2043 0.3094 574 LEU A CD1 4443 C CD2 . LEU A 574 ? 1.3817 1.3368 1.1739 -0.4181 -0.2386 0.3736 574 LEU A CD2 4444 N N . GLN A 575 ? 1.4836 1.5398 1.2005 -0.4064 -0.2166 0.2913 575 GLN A N 4445 C CA . GLN A 575 ? 1.5765 1.6135 1.3024 -0.4016 -0.2200 0.2806 575 GLN A CA 4446 C C . GLN A 575 ? 1.6325 1.5985 1.3836 -0.3929 -0.2209 0.2787 575 GLN A C 4447 O O . GLN A 575 ? 1.8409 1.7678 1.5902 -0.3813 -0.2091 0.2547 575 GLN A O 4448 C CB . GLN A 575 ? 1.6143 1.6642 1.3204 -0.3912 -0.2093 0.2390 575 GLN A CB 4449 C CG . GLN A 575 ? 1.5647 1.6860 1.2464 -0.3947 -0.2062 0.2274 575 GLN A CG 4450 C CD . GLN A 575 ? 1.5758 1.7671 1.2527 -0.4062 -0.2169 0.2439 575 GLN A CD 4451 O OE1 . GLN A 575 ? 1.7109 1.9187 1.4001 -0.4201 -0.2288 0.2850 575 GLN A OE1 4452 N NE2 . GLN A 575 ? 1.4932 1.7283 1.1562 -0.4006 -0.2142 0.2116 575 GLN A NE2 4453 N N . PRO A 576 ? 1.3945 1.3484 1.1713 -0.3984 -0.2358 0.3038 576 PRO A N 4454 C CA . PRO A 576 ? 1.3235 1.2190 1.1259 -0.3882 -0.2377 0.2964 576 PRO A CA 4455 C C . PRO A 576 ? 1.4210 1.2976 1.2136 -0.3766 -0.2273 0.2632 576 PRO A C 4456 O O . PRO A 576 ? 1.6374 1.5422 1.4169 -0.3791 -0.2278 0.2566 576 PRO A O 4457 C CB . PRO A 576 ? 1.2757 1.1744 1.1080 -0.3975 -0.2586 0.3286 576 PRO A CB 4458 C CG . PRO A 576 ? 1.3237 1.2778 1.1506 -0.4148 -0.2683 0.3617 576 PRO A CG 4459 C CD . PRO A 576 ? 1.4551 1.4524 1.2421 -0.4143 -0.2529 0.3404 576 PRO A CD 4460 N N . ILE A 577 ? 1.2391 1.0731 1.0401 -0.3647 -0.2189 0.2437 577 ILE A N 4461 C CA . ILE A 577 ? 1.2197 1.0374 1.0159 -0.3553 -0.2107 0.2166 577 ILE A CA 4462 C C . ILE A 577 ? 1.2051 0.9939 1.0273 -0.3497 -0.2178 0.2182 577 ILE A C 4463 O O . ILE A 577 ? 1.1314 0.9036 0.9771 -0.3486 -0.2257 0.2308 577 ILE A O 4464 C CB . ILE A 577 ? 1.1860 0.9873 0.9718 -0.3470 -0.1955 0.1928 577 ILE A CB 4465 C CG1 . ILE A 577 ? 1.3030 1.0974 1.0853 -0.3406 -0.1902 0.1686 577 ILE A CG1 4466 C CG2 . ILE A 577 ? 1.0040 0.7735 0.8077 -0.3408 -0.1927 0.1946 577 ILE A CG2 4467 C CD1 . ILE A 577 ? 1.1975 1.0243 0.9662 -0.3447 -0.1943 0.1617 577 ILE A CD1 4468 N N . LEU A 578 ? 1.2150 1.0004 1.0360 -0.3457 -0.2165 0.2043 578 LEU A N 4469 C CA . LEU A 578 ? 1.2069 0.9722 1.0510 -0.3402 -0.2233 0.2042 578 LEU A CA 4470 C C . LEU A 578 ? 1.3258 1.0667 1.1835 -0.3299 -0.2160 0.1907 578 LEU A C 4471 O O . LEU A 578 ? 1.5854 1.3223 1.4338 -0.3278 -0.2055 0.1832 578 LEU A O 4472 C CB . LEU A 578 ? 1.1896 0.9610 1.0276 -0.3394 -0.2236 0.1937 578 LEU A CB 4473 C CG . LEU A 578 ? 1.1623 0.9598 0.9936 -0.3482 -0.2333 0.2063 578 LEU A CG 4474 C CD1 . LEU A 578 ? 1.1744 1.0061 0.9814 -0.3551 -0.2296 0.2055 578 LEU A CD1 4475 C CD2 . LEU A 578 ? 1.2273 1.0219 1.0606 -0.3450 -0.2349 0.1953 578 LEU A CD2 4476 N N . ASN A 579 ? 1.2101 0.9399 1.0901 -0.3233 -0.2216 0.1869 579 ASN A N 4477 C CA . ASN A 579 ? 1.2244 0.9426 1.1204 -0.3131 -0.2161 0.1736 579 ASN A CA 4478 C C . ASN A 579 ? 1.2358 0.9553 1.1170 -0.3105 -0.2014 0.1581 579 ASN A C 4479 O O . ASN A 579 ? 1.2274 0.9529 1.0937 -0.3145 -0.1991 0.1547 579 ASN A O 4480 C CB . ASN A 579 ? 1.4063 1.1227 1.3303 -0.3060 -0.2264 0.1698 579 ASN A CB 4481 C CG . ASN A 579 ? 1.5288 1.2423 1.4771 -0.2950 -0.2257 0.1575 579 ASN A CG 4482 O OD1 . ASN A 579 ? 1.5971 1.3103 1.5378 -0.2924 -0.2137 0.1496 579 ASN A OD1 4483 N ND2 . ASN A 579 ? 1.5313 1.2456 1.5112 -0.2879 -0.2394 0.1538 579 ASN A ND2 4484 N N . GLN A 580 ? 1.4329 1.1488 1.3219 -0.3042 -0.1934 0.1493 580 GLN A N 4485 C CA . GLN A 580 ? 1.4767 1.1956 1.3578 -0.3030 -0.1813 0.1386 580 GLN A CA 4486 C C . GLN A 580 ? 1.4905 1.2176 1.3767 -0.3030 -0.1835 0.1348 580 GLN A C 4487 O O . GLN A 580 ? 1.3503 1.0778 1.2251 -0.3079 -0.1825 0.1329 580 GLN A O 4488 C CB . GLN A 580 ? 1.4035 1.1244 1.2974 -0.2959 -0.1739 0.1316 580 GLN A CB 4489 C CG . GLN A 580 ? 1.4026 1.1281 1.2901 -0.2968 -0.1621 0.1254 580 GLN A CG 4490 C CD . GLN A 580 ? 1.5711 1.3031 1.4693 -0.2908 -0.1541 0.1199 580 GLN A CD 4491 O OE1 . GLN A 580 ? 1.5050 1.2374 1.4168 -0.2846 -0.1580 0.1176 580 GLN A OE1 4492 N NE2 . GLN A 580 ? 1.7185 1.4570 1.6142 -0.2926 -0.1445 0.1174 580 GLN A NE2 4493 N N . PHE A 581 ? 1.6272 1.3636 1.5333 -0.2971 -0.1881 0.1323 581 PHE A N 4494 C CA . PHE A 581 ? 1.7254 1.4729 1.6376 -0.2978 -0.1922 0.1316 581 PHE A CA 4495 C C . PHE A 581 ? 1.6779 1.4230 1.5949 -0.2979 -0.2043 0.1366 581 PHE A C 4496 O O . PHE A 581 ? 1.4870 1.2356 1.4230 -0.2915 -0.2116 0.1349 581 PHE A O 4497 C CB . PHE A 581 ? 1.7413 1.5114 1.6724 -0.2917 -0.1890 0.1254 581 PHE A CB 4498 C CG . PHE A 581 ? 1.6702 1.4476 1.5997 -0.2933 -0.1780 0.1240 581 PHE A CG 4499 C CD1 . PHE A 581 ? 1.6076 1.3867 1.5404 -0.2884 -0.1710 0.1190 581 PHE A CD1 4500 C CD2 . PHE A 581 ? 1.5945 1.3768 1.5228 -0.3001 -0.1764 0.1284 581 PHE A CD2 4501 C CE1 . PHE A 581 ? 1.5199 1.3072 1.4519 -0.2905 -0.1610 0.1192 581 PHE A CE1 4502 C CE2 . PHE A 581 ? 1.6462 1.4354 1.5777 -0.3027 -0.1686 0.1298 581 PHE A CE2 4503 C CZ . PHE A 581 ? 1.6033 1.3957 1.5351 -0.2980 -0.1601 0.1255 581 PHE A CZ 4504 N N . THR A 582 ? 1.7481 1.4891 1.6507 -0.3048 -0.2078 0.1416 582 THR A N 4505 C CA . THR A 582 ? 1.6943 1.4357 1.6001 -0.3066 -0.2192 0.1485 582 THR A CA 4506 C C . THR A 582 ? 1.6098 1.3554 1.5053 -0.3118 -0.2209 0.1480 582 THR A C 4507 O O . THR A 582 ? 1.5725 1.3171 1.4557 -0.3156 -0.2157 0.1433 582 THR A O 4508 C CB . THR A 582 ? 1.6456 1.3809 1.5453 -0.3113 -0.2250 0.1599 582 THR A CB 4509 O OG1 . THR A 582 ? 1.6693 1.4080 1.5743 -0.3146 -0.2371 0.1695 582 THR A OG1 4510 C CG2 . THR A 582 ? 1.5591 1.2966 1.4343 -0.3181 -0.2182 0.1604 582 THR A CG2 4511 N N . PRO A 583 ? 1.4952 1.2456 1.3988 -0.3114 -0.2295 0.1511 583 PRO A N 4512 C CA . PRO A 583 ? 1.4928 1.2470 1.3878 -0.3165 -0.2328 0.1508 583 PRO A CA 4513 C C . PRO A 583 ? 1.5253 1.2810 1.4020 -0.3231 -0.2346 0.1538 583 PRO A C 4514 O O . PRO A 583 ? 1.5166 1.2743 1.3913 -0.3255 -0.2393 0.1640 583 PRO A O 4515 C CB . PRO A 583 ? 1.5235 1.2832 1.4318 -0.3140 -0.2419 0.1546 583 PRO A CB 4516 C CG . PRO A 583 ? 1.5208 1.2845 1.4486 -0.3057 -0.2419 0.1511 583 PRO A CG 4517 C CD . PRO A 583 ? 1.5066 1.2611 1.4315 -0.3049 -0.2373 0.1517 583 PRO A CD 4518 N N . ALA A 584 ? 1.7130 1.4721 1.5800 -0.3260 -0.2327 0.1449 584 ALA A N 4519 C CA . ALA A 584 ? 1.7446 1.5165 1.5953 -0.3310 -0.2351 0.1428 584 ALA A CA 4520 C C . ALA A 584 ? 1.6385 1.4205 1.4891 -0.3339 -0.2438 0.1453 584 ALA A C 4521 O O . ALA A 584 ? 1.5309 1.3317 1.3695 -0.3380 -0.2471 0.1427 584 ALA A O 4522 C CB . ALA A 584 ? 1.8124 1.5865 1.6578 -0.3308 -0.2310 0.1265 584 ALA A CB 4523 N N . ASN A 585 ? 1.6418 1.4160 1.5059 -0.3315 -0.2475 0.1497 585 ASN A N 4524 C CA . ASN A 585 ? 1.5103 1.2914 1.3763 -0.3336 -0.2554 0.1517 585 ASN A CA 4525 C C . ASN A 585 ? 1.4123 1.1870 1.2946 -0.3297 -0.2585 0.1567 585 ASN A C 4526 O O . ASN A 585 ? 1.4206 1.1903 1.3137 -0.3250 -0.2541 0.1554 585 ASN A O 4527 C CB . ASN A 585 ? 1.5680 1.3540 1.4321 -0.3349 -0.2573 0.1374 585 ASN A CB 4528 C CG . ASN A 585 ? 1.6105 1.3848 1.4898 -0.3324 -0.2554 0.1311 585 ASN A CG 4529 O OD1 . ASN A 585 ? 1.5848 1.3571 1.4772 -0.3318 -0.2588 0.1361 585 ASN A OD1 4530 N ND2 . ASN A 585 ? 1.9409 1.7113 1.8202 -0.3316 -0.2509 0.1217 585 ASN A ND2 4531 N N . ILE A 586 ? 1.3318 1.1119 1.2162 -0.3313 -0.2661 0.1615 586 ILE A N 4532 C CA . ILE A 586 ? 1.2513 1.0313 1.1511 -0.3273 -0.2699 0.1639 586 ILE A CA 4533 C C . ILE A 586 ? 1.2106 0.9965 1.1091 -0.3306 -0.2763 0.1637 586 ILE A C 4534 O O . ILE A 586 ? 1.2105 1.0020 1.0975 -0.3353 -0.2795 0.1635 586 ILE A O 4535 C CB . ILE A 586 ? 1.3287 1.1076 1.2403 -0.3236 -0.2754 0.1718 586 ILE A CB 4536 C CG1 . ILE A 586 ? 1.4776 1.2627 1.4082 -0.3161 -0.2773 0.1675 586 ILE A CG1 4537 C CG2 . ILE A 586 ? 1.2310 1.0139 1.1395 -0.3286 -0.2847 0.1823 586 ILE A CG2 4538 C CD1 . ILE A 586 ? 1.4366 1.2271 1.3726 -0.3122 -0.2686 0.1600 586 ILE A CD1 4539 N N . SER A 587 ? 1.2692 1.0591 1.1802 -0.3283 -0.2785 0.1636 587 SER A N 4540 C CA . SER A 587 ? 1.2932 1.0882 1.2054 -0.3314 -0.2851 0.1643 587 SER A CA 4541 C C . SER A 587 ? 1.3859 1.1891 1.3087 -0.3280 -0.2905 0.1700 587 SER A C 4542 O O . SER A 587 ? 1.4976 1.3071 1.4321 -0.3220 -0.2890 0.1696 587 SER A O 4543 C CB . SER A 587 ? 1.2705 1.0663 1.1912 -0.3340 -0.2855 0.1601 587 SER A CB 4544 O OG . SER A 587 ? 1.3295 1.1179 1.2447 -0.3359 -0.2827 0.1513 587 SER A OG 4545 N N . ARG A 588 ? 1.3298 1.1361 1.2498 -0.3310 -0.2972 0.1729 588 ARG A N 4546 C CA . ARG A 588 ? 1.1790 0.9949 1.1094 -0.3279 -0.3032 0.1769 588 ARG A CA 4547 C C . ARG A 588 ? 1.1421 0.9621 1.0701 -0.3328 -0.3088 0.1786 588 ARG A C 4548 O O . ARG A 588 ? 1.1454 0.9604 1.0625 -0.3377 -0.3104 0.1765 588 ARG A O 4549 C CB . ARG A 588 ? 1.1907 1.0039 1.1243 -0.3251 -0.3085 0.1815 588 ARG A CB 4550 C CG . ARG A 588 ? 1.3079 1.1326 1.2591 -0.3182 -0.3150 0.1804 588 ARG A CG 4551 C CD . ARG A 588 ? 1.4751 1.2944 1.4410 -0.3129 -0.3219 0.1816 588 ARG A CD 4552 N NE . ARG A 588 ? 1.5439 1.3539 1.5100 -0.3119 -0.3169 0.1802 588 ARG A NE 4553 C CZ . ARG A 588 ? 1.4551 1.2714 1.4311 -0.3048 -0.3116 0.1706 588 ARG A CZ 4554 N NH1 . ARG A 588 ? 1.2925 1.1303 1.2795 -0.2986 -0.3109 0.1619 588 ARG A NH1 4555 N NH2 . ARG A 588 ? 1.4799 1.2861 1.4551 -0.3044 -0.3073 0.1702 588 ARG A NH2 4556 N N . GLN A 589 ? 1.1242 0.9578 1.0636 -0.3313 -0.3124 0.1815 589 GLN A N 4557 C CA . GLN A 589 ? 1.1218 0.9595 1.0625 -0.3366 -0.3185 0.1845 589 GLN A CA 4558 C C . GLN A 589 ? 1.1236 0.9677 1.0635 -0.3356 -0.3250 0.1885 589 GLN A C 4559 O O . GLN A 589 ? 1.0620 0.9160 1.0095 -0.3296 -0.3265 0.1891 589 GLN A O 4560 C CB . GLN A 589 ? 1.1121 0.9655 1.0685 -0.3386 -0.3195 0.1892 589 GLN A CB 4561 C CG . GLN A 589 ? 1.2465 1.0950 1.2078 -0.3403 -0.3144 0.1874 589 GLN A CG 4562 C CD . GLN A 589 ? 1.3103 1.1774 1.2916 -0.3455 -0.3186 0.1975 589 GLN A CD 4563 O OE1 . GLN A 589 ? 1.2106 1.0970 1.2012 -0.3482 -0.3251 0.2066 589 GLN A OE1 4564 N NE2 . GLN A 589 ? 1.4025 1.2665 1.3922 -0.3481 -0.3159 0.1982 589 GLN A NE2 4565 N N . ALA A 590 ? 1.1261 0.9658 1.0592 -0.3409 -0.3299 0.1891 590 ALA A N 4566 C CA . ALA A 590 ? 1.1205 0.9669 1.0532 -0.3413 -0.3365 0.1938 590 ALA A CA 4567 C C . ALA A 590 ? 1.0965 0.9507 1.0373 -0.3458 -0.3421 0.1968 590 ALA A C 4568 O O . ALA A 590 ? 1.0942 0.9428 1.0399 -0.3501 -0.3436 0.1941 590 ALA A O 4569 C CB . ALA A 590 ? 1.1378 0.9779 1.0570 -0.3444 -0.3386 0.1939 590 ALA A CB 4570 N N . HIS A 591 ? 1.3764 0.8355 0.8550 -0.1642 -0.4027 0.1056 591 HIS A N 4571 C CA . HIS A 591 ? 1.3825 0.8097 0.8640 -0.1695 -0.4234 0.0894 591 HIS A CA 4572 C C . HIS A 591 ? 1.4496 0.8520 0.9084 -0.1838 -0.4613 0.0907 591 HIS A C 4573 O O . HIS A 591 ? 1.5254 0.9436 0.9957 -0.1894 -0.4742 0.1071 591 HIS A O 4574 C CB . HIS A 591 ? 1.2872 0.7384 0.8469 -0.1779 -0.4207 0.0911 591 HIS A CB 4575 C CG . HIS A 591 ? 1.2750 0.7513 0.8580 -0.1651 -0.3875 0.0895 591 HIS A CG 4576 N ND1 . HIS A 591 ? 1.4154 0.9278 1.0173 -0.1627 -0.3677 0.1027 591 HIS A ND1 4577 C CD2 . HIS A 591 ? 1.2848 0.7541 0.8723 -0.1557 -0.3730 0.0773 591 HIS A CD2 4578 C CE1 . HIS A 591 ? 1.4232 0.9576 1.0442 -0.1527 -0.3433 0.0978 591 HIS A CE1 4579 N NE2 . HIS A 591 ? 1.3824 0.8912 0.9947 -0.1453 -0.3453 0.0826 591 HIS A NE2 4580 N N . ILE A 592 ? 1.4388 0.7982 0.8604 -0.1903 -0.4815 0.0738 592 ILE A N 4581 C CA . ILE A 592 ? 1.4870 0.8268 0.8900 -0.2094 -0.5225 0.0737 592 ILE A CA 4582 C C . ILE A 592 ? 1.4390 0.8135 0.9241 -0.2315 -0.5424 0.0817 592 ILE A C 4583 O O . ILE A 592 ? 1.4050 0.7851 0.9288 -0.2373 -0.5315 0.0766 592 ILE A O 4584 C CB . ILE A 592 ? 1.5798 0.8500 0.8961 -0.2115 -0.5398 0.0513 592 ILE A CB 4585 C CG1 . ILE A 592 ? 1.6295 0.8728 0.8632 -0.1800 -0.5136 0.0423 592 ILE A CG1 4586 C CG2 . ILE A 592 ? 1.6536 0.9070 0.9460 -0.2348 -0.5861 0.0519 592 ILE A CG2 4587 C CD1 . ILE A 592 ? 1.8311 0.9933 0.9633 -0.1727 -0.5288 0.0173 592 ILE A CD1 4588 N N . LEU A 593 ? 1.4398 0.8423 0.9504 -0.2412 -0.5706 0.0957 593 LEU A N 4589 C CA . LEU A 593 ? 1.3931 0.8471 0.9872 -0.2554 -0.5870 0.1066 593 LEU A CA 4590 C C . LEU A 593 ? 1.4255 0.8671 1.0211 -0.2859 -0.6125 0.0962 593 LEU A C 4591 O O . LEU A 593 ? 1.4972 0.9059 1.0398 -0.3033 -0.6448 0.0889 593 LEU A O 4592 C CB . LEU A 593 ? 1.3972 0.8861 1.0115 -0.2510 -0.6122 0.1251 593 LEU A CB 4593 C CG . LEU A 593 ? 1.4216 0.9785 1.1247 -0.2516 -0.6250 0.1405 593 LEU A CG 4594 C CD1 . LEU A 593 ? 1.4791 1.0534 1.1912 -0.2269 -0.6289 0.1592 593 LEU A CD1 4595 C CD2 . LEU A 593 ? 1.3777 0.9637 1.1006 -0.2799 -0.6652 0.1408 593 LEU A CD2 4596 N N . LEU A 594 ? 1.4335 0.8984 1.0853 -0.2953 -0.5990 0.0965 594 LEU A N 4597 C CA . LEU A 594 ? 1.4114 0.8677 1.0708 -0.3313 -0.6217 0.0915 594 LEU A CA 4598 C C . LEU A 594 ? 1.4603 0.9900 1.2165 -0.3414 -0.6140 0.1061 594 LEU A C 4599 O O . LEU A 594 ? 1.4403 0.9870 1.2309 -0.3205 -0.5793 0.1082 594 LEU A O 4600 C CB . LEU A 594 ? 1.4654 0.8365 1.0509 -0.3339 -0.6094 0.0708 594 LEU A CB 4601 C CG . LEU A 594 ? 1.5245 0.8561 1.0927 -0.3755 -0.6341 0.0640 594 LEU A CG 4602 C CD1 . LEU A 594 ? 1.6333 0.8576 1.0854 -0.3752 -0.6454 0.0414 594 LEU A CD1 4603 C CD2 . LEU A 594 ? 1.8171 1.1598 1.4308 -0.3789 -0.6071 0.0677 594 LEU A CD2 4604 N N . ASP A 595 ? 1.5603 1.1378 1.3580 -0.3739 -0.6468 0.1165 595 ASP A N 4605 C CA . ASP A 595 ? 1.4498 1.1094 1.3393 -0.3862 -0.6412 0.1326 595 ASP A CA 4606 C C . ASP A 595 ? 1.3552 1.0749 1.3073 -0.3446 -0.6116 0.1439 595 ASP A C 4607 O O . ASP A 595 ? 1.1747 0.9182 1.1686 -0.3375 -0.5832 0.1468 595 ASP A O 4608 C CB . ASP A 595 ? 1.3779 0.9998 1.2586 -0.4109 -0.6260 0.1261 595 ASP A CB 4609 C CG . ASP A 595 ? 1.4789 1.0514 1.3084 -0.4502 -0.6476 0.1205 595 ASP A CG 4610 O OD1 . ASP A 595 ? 1.4467 0.9393 1.2191 -0.4574 -0.6346 0.1081 595 ASP A OD1 4611 O OD2 . ASP A 595 ? 1.5317 1.1444 1.3749 -0.4687 -0.6739 0.1292 595 ASP A OD2 4612 N N . CYS A 596 ? 1.3415 1.0771 1.2916 -0.3171 -0.6195 0.1501 596 CYS A N 4613 C CA . CYS A 596 ? 1.3788 1.1559 1.3753 -0.2774 -0.5972 0.1604 596 CYS A CA 4614 C C . CYS A 596 ? 1.2574 1.1310 1.3291 -0.2702 -0.6161 0.1795 596 CYS A C 4615 O O . CYS A 596 ? 1.1538 1.0609 1.2606 -0.2325 -0.6025 0.1883 596 CYS A O 4616 C CB . CYS A 596 ? 1.5484 1.2764 1.4915 -0.2495 -0.5921 0.1584 596 CYS A CB 4617 S SG . CYS A 596 ? 2.6807 2.3257 2.5545 -0.2446 -0.5577 0.1406 596 CYS A SG 4618 N N . GLY A 597 ? 1.2833 1.2015 1.3765 -0.3056 -0.6487 0.1860 597 GLY A N 4619 C CA . GLY A 597 ? 1.3216 1.3502 1.4917 -0.3004 -0.6687 0.2062 597 GLY A CA 4620 C C . GLY A 597 ? 1.3505 1.3958 1.5062 -0.2820 -0.7025 0.2149 597 GLY A C 4621 O O . GLY A 597 ? 1.4223 1.3892 1.5045 -0.2771 -0.7102 0.2055 597 GLY A O 4622 N N . GLU A 598 ? 1.2660 1.4187 1.4909 -0.2691 -0.7221 0.2343 598 GLU A N 4623 C CA . GLU A 598 ? 1.3653 1.5450 1.5817 -0.2471 -0.7574 0.2457 598 GLU A CA 4624 C C . GLU A 598 ? 1.3934 1.5163 1.5722 -0.1898 -0.7405 0.2460 598 GLU A C 4625 O O . GLU A 598 ? 1.4569 1.5597 1.5973 -0.1717 -0.7659 0.2524 598 GLU A O 4626 C CB . GLU A 598 ? 1.4208 1.7389 1.7232 -0.2385 -0.7700 0.2650 598 GLU A CB 4627 C CG . GLU A 598 ? 1.5337 1.9051 1.8634 -0.2976 -0.7779 0.2643 598 GLU A CG 4628 C CD . GLU A 598 ? 1.5374 2.0556 1.9492 -0.2886 -0.7908 0.2839 598 GLU A CD 4629 O OE1 . GLU A 598 ? 1.6453 2.2273 2.0968 -0.2295 -0.7898 0.2974 598 GLU A OE1 4630 O OE2 . GLU A 598 ? 1.3755 1.9424 1.8078 -0.3384 -0.8019 0.2858 598 GLU A OE2 4631 N N . ASP A 599 ? 1.2863 1.3792 1.4716 -0.1643 -0.6993 0.2401 599 ASP A N 4632 C CA . ASP A 599 ? 1.3081 1.3360 1.4528 -0.1179 -0.6826 0.2403 599 ASP A CA 4633 C C . ASP A 599 ? 1.4897 1.4076 1.5465 -0.1346 -0.6764 0.2277 599 ASP A C 4634 O O . ASP A 599 ? 1.6126 1.4696 1.6240 -0.1074 -0.6679 0.2305 599 ASP A O 4635 C CB . ASP A 599 ? 1.2763 1.3089 1.4540 -0.0893 -0.6435 0.2371 599 ASP A CB 4636 C CG . ASP A 599 ? 1.3878 1.3974 1.5679 -0.1242 -0.6147 0.2219 599 ASP A CG 4637 O OD1 . ASP A 599 ? 1.5867 1.6017 1.7633 -0.1698 -0.6268 0.2168 599 ASP A OD1 4638 O OD2 . ASP A 599 ? 1.3080 1.2894 1.4884 -0.1055 -0.5817 0.2150 599 ASP A OD2 4639 N N . ASN A 600 ? 1.5481 1.4406 1.5778 -0.1791 -0.6805 0.2148 600 ASN A N 4640 C CA . ASN A 600 ? 1.4873 1.2871 1.4335 -0.1934 -0.6726 0.2017 600 ASN A CA 4641 C C . ASN A 600 ? 1.3566 1.1022 1.2819 -0.1769 -0.6311 0.1947 600 ASN A C 4642 O O . ASN A 600 ? 1.3383 1.0197 1.1992 -0.1761 -0.6217 0.1909 600 ASN A O 4643 C CB . ASN A 600 ? 1.4667 1.2378 1.3567 -0.1835 -0.7014 0.2103 600 ASN A CB 4644 C CG . ASN A 600 ? 1.6426 1.4506 1.5314 -0.2100 -0.7454 0.2122 600 ASN A CG 4645 O OD1 . ASN A 600 ? 1.7645 1.5785 1.6575 -0.2482 -0.7529 0.2007 600 ASN A OD1 4646 N ND2 . ASN A 600 ? 1.7836 1.6117 1.6616 -0.1913 -0.7773 0.2273 600 ASN A ND2 4647 N N . VAL A 601 ? 1.2598 1.0375 1.2397 -0.1652 -0.6069 0.1940 601 VAL A N 4648 C CA . VAL A 601 ? 1.2329 0.9671 1.1986 -0.1540 -0.5700 0.1865 601 VAL A CA 4649 C C . VAL A 601 ? 1.1883 0.9567 1.2039 -0.1627 -0.5474 0.1787 601 VAL A C 4650 O O . VAL A 601 ? 1.0787 0.9155 1.1553 -0.1582 -0.5535 0.1860 601 VAL A O 4651 C CB . VAL A 601 ? 1.2495 0.9668 1.2125 -0.1166 -0.5645 0.1974 601 VAL A CB 4652 C CG1 . VAL A 601 ? 1.3257 1.1103 1.3472 -0.0875 -0.5795 0.2093 601 VAL A CG1 4653 C CG2 . VAL A 601 ? 1.2375 0.9182 1.1932 -0.1107 -0.5296 0.1892 601 VAL A CG2 4654 N N . CYS A 602 ? 1.1586 0.8852 1.1479 -0.1740 -0.5212 0.1656 602 CYS A N 4655 C CA . CYS A 602 ? 1.1115 0.8608 1.1373 -0.1828 -0.4998 0.1588 602 CYS A CA 4656 C C . CYS A 602 ? 1.1115 0.8716 1.1662 -0.1549 -0.4743 0.1600 602 CYS A C 4657 O O . CYS A 602 ? 1.2297 0.9454 1.2518 -0.1438 -0.4585 0.1559 602 CYS A O 4658 C CB . CYS A 602 ? 1.1930 0.8918 1.1725 -0.2034 -0.4859 0.1441 602 CYS A CB 4659 S SG . CYS A 602 ? 1.1455 0.8175 1.0799 -0.2364 -0.5165 0.1379 602 CYS A SG 4660 N N . LYS A 603 ? 1.0756 0.8974 1.1896 -0.1453 -0.4712 0.1661 603 LYS A N 4661 C CA . LYS A 603 ? 1.0881 0.9212 1.2261 -0.1149 -0.4485 0.1658 603 LYS A CA 4662 C C . LYS A 603 ? 1.1235 0.9904 1.2965 -0.1256 -0.4267 0.1619 603 LYS A C 4663 O O . LYS A 603 ? 1.2101 1.1476 1.4359 -0.1237 -0.4283 0.1713 603 LYS A O 4664 C CB . LYS A 603 ? 1.1733 1.0517 1.3441 -0.0793 -0.4618 0.1782 603 LYS A CB 4665 C CG . LYS A 603 ? 1.2746 1.1185 1.4081 -0.0672 -0.4869 0.1853 603 LYS A CG 4666 C CD . LYS A 603 ? 1.3412 1.2291 1.5040 -0.0240 -0.5008 0.1981 603 LYS A CD 4667 C CE . LYS A 603 ? 1.3798 1.2400 1.5361 0.0164 -0.4799 0.1936 603 LYS A CE 4668 N NZ . LYS A 603 ? 1.4047 1.2953 1.5764 0.0685 -0.4937 0.2050 603 LYS A NZ 4669 N N . PRO A 604 ? 1.0995 0.9210 1.2424 -0.1366 -0.4060 0.1501 604 PRO A N 4670 C CA . PRO A 604 ? 1.1057 0.9440 1.2677 -0.1487 -0.3857 0.1466 604 PRO A CA 4671 C C . PRO A 604 ? 1.2185 1.0946 1.4166 -0.1214 -0.3650 0.1486 604 PRO A C 4672 O O . PRO A 604 ? 1.3330 1.1898 1.5196 -0.0920 -0.3593 0.1451 604 PRO A O 4673 C CB . PRO A 604 ? 1.0913 0.8668 1.2021 -0.1572 -0.3718 0.1336 604 PRO A CB 4674 C CG . PRO A 604 ? 1.1042 0.8446 1.1836 -0.1415 -0.3746 0.1314 604 PRO A CG 4675 C CD . PRO A 604 ? 1.1230 0.8785 1.2099 -0.1372 -0.4009 0.1416 604 PRO A CD 4676 N N . LYS A 605 ? 1.2628 1.1871 1.4976 -0.1323 -0.3544 0.1547 605 LYS A N 4677 C CA . LYS A 605 ? 1.2968 1.2529 1.5564 -0.1074 -0.3298 0.1550 605 LYS A CA 4678 C C . LYS A 605 ? 1.2550 1.1726 1.4882 -0.1195 -0.3086 0.1458 605 LYS A C 4679 O O . LYS A 605 ? 1.2971 1.2196 1.5333 -0.1481 -0.3061 0.1504 605 LYS A O 4680 C CB . LYS A 605 ? 1.3459 1.3949 1.6664 -0.1082 -0.3287 0.1718 605 LYS A CB 4681 C CG . LYS A 605 ? 1.4636 1.5683 1.8170 -0.0783 -0.3439 0.1814 605 LYS A CG 4682 C CD . LYS A 605 ? 1.5203 1.7365 1.9402 -0.0733 -0.3369 0.1996 605 LYS A CD 4683 C CE . LYS A 605 ? 1.4727 1.7117 1.9016 -0.0379 -0.3043 0.1969 605 LYS A CE 4684 N NZ . LYS A 605 ? 1.3686 1.5890 1.7869 -0.0673 -0.2829 0.1950 605 LYS A NZ 4685 N N . LEU A 606 ? 1.1212 0.9979 1.3249 -0.0984 -0.2955 0.1338 606 LEU A N 4686 C CA . LEU A 606 ? 1.0973 0.9402 1.2732 -0.1057 -0.2780 0.1248 606 LEU A CA 4687 C C . LEU A 606 ? 1.1177 0.9834 1.3063 -0.0832 -0.2557 0.1230 606 LEU A C 4688 O O . LEU A 606 ? 1.1621 1.0332 1.3539 -0.0541 -0.2531 0.1195 606 LEU A O 4689 C CB . LEU A 606 ? 1.1467 0.9334 1.2775 -0.1052 -0.2812 0.1134 606 LEU A CB 4690 C CG . LEU A 606 ? 1.1156 0.8768 1.2242 -0.1226 -0.3009 0.1144 606 LEU A CG 4691 C CD1 . LEU A 606 ? 1.0750 0.7954 1.1436 -0.1204 -0.3004 0.1070 606 LEU A CD1 4692 C CD2 . LEU A 606 ? 1.1420 0.8940 1.2395 -0.1473 -0.3041 0.1154 606 LEU A CD2 4693 N N . GLU A 607 ? 1.1372 1.0095 1.3258 -0.0949 -0.2406 0.1255 607 GLU A N 4694 C CA . GLU A 607 ? 1.1173 1.0081 1.3099 -0.0745 -0.2184 0.1238 607 GLU A CA 4695 C C . GLU A 607 ? 1.0142 0.8739 1.1767 -0.0851 -0.2059 0.1198 607 GLU A C 4696 O O . GLU A 607 ? 0.9705 0.8149 1.1239 -0.1100 -0.2094 0.1258 607 GLU A O 4697 C CB . GLU A 607 ? 1.1821 1.1446 1.4208 -0.0707 -0.2094 0.1397 607 GLU A CB 4698 C CG . GLU A 607 ? 1.3617 1.3499 1.6225 -0.1096 -0.2167 0.1562 607 GLU A CG 4699 C CD . GLU A 607 ? 1.3921 1.4702 1.7080 -0.1095 -0.2107 0.1757 607 GLU A CD 4700 O OE1 . GLU A 607 ? 1.3651 1.4725 1.7031 -0.1478 -0.2187 0.1923 607 GLU A OE1 4701 O OE2 . GLU A 607 ? 1.3921 1.5124 1.7267 -0.0710 -0.1986 0.1747 607 GLU A OE2 4702 N N . VAL A 608 ? 1.0598 0.9053 1.2012 -0.0647 -0.1936 0.1092 608 VAL A N 4703 C CA . VAL A 608 ? 1.0420 0.8631 1.1535 -0.0680 -0.1830 0.1052 608 VAL A CA 4704 C C . VAL A 608 ? 1.0706 0.9160 1.1842 -0.0515 -0.1627 0.1080 608 VAL A C 4705 O O . VAL A 608 ? 1.0813 0.9384 1.1957 -0.0275 -0.1572 0.1007 608 VAL A O 4706 C CB . VAL A 608 ? 1.0282 0.8146 1.1073 -0.0630 -0.1891 0.0908 608 VAL A CB 4707 C CG1 . VAL A 608 ? 1.0334 0.8158 1.1114 -0.0473 -0.1947 0.0818 608 VAL A CG1 4708 C CG2 . VAL A 608 ? 1.1198 0.8970 1.1724 -0.0568 -0.1772 0.0867 608 VAL A CG2 4709 N N . SER A 609 ? 1.1039 0.9497 1.2109 -0.0634 -0.1523 0.1187 609 SER A N 4710 C CA . SER A 609 ? 1.1791 1.0475 1.2828 -0.0500 -0.1317 0.1245 609 SER A CA 4711 C C . SER A 609 ? 1.2371 1.0699 1.2987 -0.0449 -0.1261 0.1191 609 SER A C 4712 O O . SER A 609 ? 1.2182 1.0147 1.2577 -0.0554 -0.1355 0.1168 609 SER A O 4713 C CB . SER A 609 ? 1.2009 1.1071 1.3321 -0.0698 -0.1225 0.1472 609 SER A CB 4714 O OG . SER A 609 ? 1.2683 1.1987 1.3928 -0.0574 -0.1002 0.1556 609 SER A OG 4715 N N . VAL A 610 ? 1.3266 1.1719 1.3740 -0.0246 -0.1111 0.1170 610 VAL A N 4716 C CA . VAL A 610 ? 1.3342 1.1539 1.3419 -0.0152 -0.1073 0.1124 610 VAL A CA 4717 C C . VAL A 610 ? 1.4360 1.2735 1.4303 -0.0027 -0.0871 0.1223 610 VAL A C 4718 O O . VAL A 610 ? 1.4991 1.3709 1.5077 0.0112 -0.0759 0.1225 610 VAL A O 4719 C CB . VAL A 610 ? 1.3106 1.1197 1.3014 -0.0013 -0.1184 0.0916 610 VAL A CB 4720 C CG1 . VAL A 610 ? 1.3773 1.2017 1.3752 0.0151 -0.1170 0.0810 610 VAL A CG1 4721 C CG2 . VAL A 610 ? 1.3166 1.1152 1.2711 0.0104 -0.1159 0.0879 610 VAL A CG2 4722 N N . ASP A 611 ? 1.5257 1.3383 1.4878 -0.0042 -0.0821 0.1312 611 ASP A N 4723 C CA . ASP A 611 ? 1.7138 1.5377 1.6551 0.0065 -0.0630 0.1434 611 ASP A CA 4724 C C . ASP A 611 ? 1.8398 1.6504 1.7406 0.0315 -0.0647 0.1306 611 ASP A C 4725 O O . ASP A 611 ? 1.8358 1.6252 1.7218 0.0350 -0.0793 0.1197 611 ASP A O 4726 C CB . ASP A 611 ? 1.8594 1.6599 1.7879 -0.0167 -0.0564 0.1685 611 ASP A CB 4727 C CG . ASP A 611 ? 1.8841 1.7127 1.8063 -0.0158 -0.0332 0.1888 611 ASP A CG 4728 O OD1 . ASP A 611 ? 1.7976 1.6483 1.7049 0.0119 -0.0223 0.1809 611 ASP A OD1 4729 O OD2 . ASP A 611 ? 1.9274 1.7558 1.8567 -0.0453 -0.0265 0.2136 611 ASP A OD2 4730 N N . SER A 612 ? 1.9709 1.8007 1.8536 0.0495 -0.0497 0.1329 612 SER A N 4731 C CA . SER A 612 ? 2.0506 1.8756 1.8952 0.0733 -0.0537 0.1189 612 SER A CA 4732 C C . SER A 612 ? 2.0867 1.8838 1.8943 0.0787 -0.0580 0.1267 612 SER A C 4733 O O . SER A 612 ? 2.0619 1.8594 1.8502 0.0926 -0.0714 0.1127 612 SER A O 4734 C CB . SER A 612 ? 2.0099 1.8591 1.8366 0.0931 -0.0356 0.1203 612 SER A CB 4735 O OG . SER A 612 ? 1.9834 1.8381 1.8009 0.0873 -0.0150 0.1471 612 SER A OG 4736 N N . ASP A 613 ? 2.0536 1.8265 1.8492 0.0676 -0.0482 0.1499 613 ASP A N 4737 C CA . ASP A 613 ? 2.0463 1.7815 1.7946 0.0795 -0.0502 0.1606 613 ASP A CA 4738 C C . ASP A 613 ? 2.0211 1.7724 1.7330 0.1072 -0.0453 0.1573 613 ASP A C 4739 O O . ASP A 613 ? 1.9994 1.7669 1.7022 0.1099 -0.0279 0.1670 613 ASP A O 4740 C CB . ASP A 613 ? 2.0657 1.7799 1.8096 0.0850 -0.0693 0.1491 613 ASP A CB 4741 C CG . ASP A 613 ? 2.1742 1.8360 1.8680 0.0981 -0.0708 0.1636 613 ASP A CG 4742 O OD1 . ASP A 613 ? 2.1930 1.8368 1.8482 0.1083 -0.0602 0.1799 613 ASP A OD1 4743 O OD2 . ASP A 613 ? 2.2017 1.8361 1.8886 0.1010 -0.0824 0.1591 613 ASP A OD2 4744 N N . GLN A 614 ? 2.0079 1.7610 1.6985 0.1280 -0.0608 0.1446 614 GLN A N 4745 C CA . GLN A 614 ? 1.9508 1.7243 1.6075 0.1526 -0.0619 0.1386 614 GLN A CA 4746 C C . GLN A 614 ? 1.8431 1.6495 1.5171 0.1509 -0.0620 0.1190 614 GLN A C 4747 O O . GLN A 614 ? 1.7879 1.6073 1.4926 0.1401 -0.0756 0.1004 614 GLN A O 4748 C CB . GLN A 614 ? 1.9651 1.7487 1.6038 0.1729 -0.0819 0.1292 614 GLN A CB 4749 C CG . GLN A 614 ? 2.0256 1.7704 1.6284 0.1900 -0.0819 0.1475 614 GLN A CG 4750 C CD . GLN A 614 ? 1.9314 1.6601 1.5539 0.1841 -0.0912 0.1442 614 GLN A CD 4751 O OE1 . GLN A 614 ? 1.8394 1.5839 1.5059 0.1614 -0.0952 0.1321 614 GLN A OE1 4752 N NE2 . GLN A 614 ? 1.9026 1.5958 1.4861 0.2084 -0.0948 0.1549 614 GLN A NE2 4753 N N . LYS A 615 ? 1.8534 1.6676 1.5004 0.1632 -0.0467 0.1238 615 LYS A N 4754 C CA . LYS A 615 ? 1.8106 1.6449 1.4596 0.1693 -0.0450 0.1046 615 LYS A CA 4755 C C . LYS A 615 ? 1.8103 1.6515 1.4303 0.1817 -0.0679 0.0807 615 LYS A C 4756 O O . LYS A 615 ? 1.8299 1.6725 1.4516 0.1799 -0.0783 0.0580 615 LYS A O 4757 C CB . LYS A 615 ? 1.7851 1.6294 1.4114 0.1815 -0.0175 0.1191 615 LYS A CB 4758 C CG . LYS A 615 ? 1.7887 1.6394 1.4485 0.1621 0.0047 0.1452 615 LYS A CG 4759 C CD . LYS A 615 ? 1.7085 1.5777 1.4220 0.1493 0.0036 0.1346 615 LYS A CD 4760 C CE . LYS A 615 ? 1.7051 1.6099 1.4201 0.1671 0.0246 0.1324 615 LYS A CE 4761 N NZ . LYS A 615 ? 1.7364 1.6345 1.4027 0.1979 0.0192 0.1076 615 LYS A NZ 4762 N N . LYS A 616 ? 1.6884 1.5318 1.2783 0.1938 -0.0779 0.0865 616 LYS A N 4763 C CA . LYS A 616 ? 1.5851 1.4455 1.1447 0.2037 -0.1011 0.0676 616 LYS A CA 4764 C C . LYS A 616 ? 1.4804 1.3630 1.0548 0.2000 -0.1242 0.0661 616 LYS A C 4765 O O . LYS A 616 ? 1.4596 1.3362 1.0408 0.2064 -0.1190 0.0840 616 LYS A O 4766 C CB . LYS A 616 ? 1.6985 1.5580 1.1998 0.2296 -0.0928 0.0757 616 LYS A CB 4767 C CG . LYS A 616 ? 1.7461 1.5938 1.2304 0.2378 -0.0632 0.0846 616 LYS A CG 4768 C CD . LYS A 616 ? 1.7899 1.6352 1.2145 0.2623 -0.0514 0.1004 616 LYS A CD 4769 C CE . LYS A 616 ? 1.7777 1.6229 1.1894 0.2690 -0.0172 0.1148 616 LYS A CE 4770 N NZ . LYS A 616 ? 1.8250 1.6666 1.1740 0.2911 -0.0036 0.1338 616 LYS A NZ 4771 N N . ILE A 617 ? 1.4306 1.3385 1.0066 0.1896 -0.1501 0.0452 617 ILE A N 4772 C CA . ILE A 617 ? 1.3751 1.3258 0.9636 0.1882 -0.1727 0.0449 617 ILE A CA 4773 C C . ILE A 617 ? 1.4182 1.4008 0.9746 0.1888 -0.1985 0.0297 617 ILE A C 4774 O O . ILE A 617 ? 1.4216 1.3922 0.9675 0.1693 -0.2116 0.0091 617 ILE A O 4775 C CB . ILE A 617 ? 1.3094 1.2740 0.9491 0.1603 -0.1822 0.0384 617 ILE A CB 4776 C CG1 . ILE A 617 ? 1.4015 1.3413 1.0496 0.1337 -0.1881 0.0190 617 ILE A CG1 4777 C CG2 . ILE A 617 ? 1.2767 1.2185 0.9421 0.1638 -0.1630 0.0552 617 ILE A CG2 4778 C CD1 . ILE A 617 ? 1.5648 1.5158 1.2558 0.1039 -0.1998 0.0139 617 ILE A CD1 4779 N N . TYR A 618 ? 1.4215 1.4403 0.9569 0.2122 -0.2076 0.0401 618 TYR A N 4780 C CA . TYR A 618 ? 1.3867 1.4395 0.8863 0.2150 -0.2334 0.0284 618 TYR A CA 4781 C C . TYR A 618 ? 1.3413 1.4541 0.8719 0.1842 -0.2662 0.0156 618 TYR A C 4782 O O . TYR A 618 ? 1.3887 1.5360 0.9670 0.1741 -0.2674 0.0227 618 TYR A O 4783 C CB . TYR A 618 ? 1.4919 1.5628 0.9543 0.2553 -0.2313 0.0470 618 TYR A CB 4784 C CG . TYR A 618 ? 1.6116 1.6219 1.0400 0.2785 -0.1989 0.0638 618 TYR A CG 4785 C CD1 . TYR A 618 ? 1.6874 1.6731 1.1222 0.2966 -0.1788 0.0879 618 TYR A CD1 4786 C CD2 . TYR A 618 ? 1.6694 1.6453 1.0562 0.2805 -0.1883 0.0561 618 TYR A CD2 4787 C CE1 . TYR A 618 ? 1.7379 1.6688 1.1413 0.3086 -0.1506 0.1066 618 TYR A CE1 4788 C CE2 . TYR A 618 ? 1.6889 1.6217 1.0483 0.2974 -0.1567 0.0752 618 TYR A CE2 4789 C CZ . TYR A 618 ? 1.6973 1.6090 1.0672 0.3075 -0.1386 0.1017 618 TYR A CZ 4790 O OH . TYR A 618 ? 1.6902 1.5597 1.0323 0.3159 -0.1087 0.1240 618 TYR A OH 4791 N N . ILE A 619 ? 1.3678 1.4920 0.8667 0.1675 -0.2931 -0.0025 619 ILE A N 4792 C CA . ILE A 619 ? 1.3711 1.5384 0.8925 0.1237 -0.3267 -0.0165 619 ILE A CA 4793 C C . ILE A 619 ? 1.4573 1.7272 1.0204 0.1219 -0.3444 -0.0027 619 ILE A C 4794 O O . ILE A 619 ? 1.6695 1.9745 1.2828 0.0952 -0.3479 0.0005 619 ILE A O 4795 C CB . ILE A 619 ? 1.4471 1.5970 0.9116 0.1061 -0.3559 -0.0389 619 ILE A CB 4796 C CG1 . ILE A 619 ? 1.4897 1.5413 0.9085 0.1125 -0.3386 -0.0553 619 ILE A CG1 4797 C CG2 . ILE A 619 ? 1.5473 1.7362 1.0309 0.0514 -0.3941 -0.0512 619 ILE A CG2 4798 C CD1 . ILE A 619 ? 1.4450 1.4465 0.8923 0.0849 -0.3306 -0.0640 619 ILE A CD1 4799 N N . GLY A 620 ? 1.4139 1.7362 0.9546 0.1532 -0.3548 0.0067 620 GLY A N 4800 C CA . GLY A 620 ? 1.4420 1.8779 1.0183 0.1542 -0.3767 0.0181 620 GLY A CA 4801 C C . GLY A 620 ? 1.4615 1.9350 1.0769 0.1905 -0.3549 0.0401 620 GLY A C 4802 O O . GLY A 620 ? 1.4068 1.9808 1.0634 0.1895 -0.3684 0.0494 620 GLY A O 4803 N N . ASP A 621 ? 1.5735 1.9676 1.1732 0.2223 -0.3216 0.0488 621 ASP A N 4804 C CA . ASP A 621 ? 1.5519 1.9585 1.1696 0.2625 -0.3020 0.0682 621 ASP A CA 4805 C C . ASP A 621 ? 1.3595 1.7539 1.0251 0.2379 -0.2881 0.0670 621 ASP A C 4806 O O . ASP A 621 ? 1.3183 1.6913 1.0038 0.1903 -0.2927 0.0530 621 ASP A O 4807 C CB . ASP A 621 ? 1.7029 2.0230 1.2707 0.3051 -0.2763 0.0808 621 ASP A CB 4808 C CG . ASP A 621 ? 1.9204 2.2551 1.4783 0.3596 -0.2672 0.1015 621 ASP A CG 4809 O OD1 . ASP A 621 ? 2.0064 2.4361 1.5782 0.3818 -0.2859 0.1070 621 ASP A OD1 4810 O OD2 . ASP A 621 ? 2.0098 2.2603 1.5431 0.3806 -0.2424 0.1129 621 ASP A OD2 4811 N N . ASP A 622 ? 1.3778 1.7797 1.0542 0.2735 -0.2724 0.0817 622 ASP A N 4812 C CA . ASP A 622 ? 1.5142 1.8848 1.2221 0.2595 -0.2550 0.0820 622 ASP A CA 4813 C C . ASP A 622 ? 1.5477 1.8085 1.2213 0.2820 -0.2287 0.0891 622 ASP A C 4814 O O . ASP A 622 ? 1.5380 1.7732 1.1714 0.3274 -0.2213 0.1024 622 ASP A O 4815 C CB . ASP A 622 ? 1.6278 2.0830 1.3666 0.2826 -0.2565 0.0919 622 ASP A CB 4816 C CG . ASP A 622 ? 1.5743 2.1548 1.3536 0.2541 -0.2826 0.0893 622 ASP A CG 4817 O OD1 . ASP A 622 ? 1.5733 2.1538 1.3640 0.1996 -0.2987 0.0766 622 ASP A OD1 4818 O OD2 . ASP A 622 ? 1.4521 2.1314 1.2491 0.2864 -0.2877 0.1008 622 ASP A OD2 4819 N N . ASN A 623 ? 1.5226 1.7189 1.2100 0.2490 -0.2160 0.0820 623 ASN A N 4820 C CA . ASN A 623 ? 1.5671 1.6676 1.2253 0.2586 -0.1937 0.0895 623 ASN A CA 4821 C C . ASN A 623 ? 1.5218 1.5773 1.1962 0.2545 -0.1788 0.0940 623 ASN A C 4822 O O . ASN A 623 ? 1.4893 1.5705 1.2033 0.2286 -0.1829 0.0859 623 ASN A O 4823 C CB . ASN A 623 ? 1.6871 1.7482 1.3399 0.2286 -0.1902 0.0790 623 ASN A CB 4824 C CG . ASN A 623 ? 1.7108 1.8066 1.3383 0.2306 -0.2071 0.0710 623 ASN A CG 4825 O OD1 . ASN A 623 ? 1.6039 1.7130 1.2412 0.1992 -0.2210 0.0540 623 ASN A OD1 4826 N ND2 . ASN A 623 ? 1.7800 1.8833 1.3676 0.2681 -0.2080 0.0830 623 ASN A ND2 4827 N N . PRO A 624 ? 1.5883 1.5716 1.2265 0.2778 -0.1631 0.1078 624 PRO A N 4828 C CA . PRO A 624 ? 1.7553 1.6808 1.3967 0.2728 -0.1514 0.1122 624 PRO A CA 4829 C C . PRO A 624 ? 1.8212 1.7021 1.4853 0.2309 -0.1416 0.1082 624 PRO A C 4830 O O . PRO A 624 ? 2.0211 1.8355 1.6622 0.2275 -0.1284 0.1196 624 PRO A O 4831 C CB . PRO A 624 ? 1.9021 1.7607 1.4837 0.3113 -0.1429 0.1297 624 PRO A CB 4832 C CG . PRO A 624 ? 1.8702 1.7280 1.4230 0.3190 -0.1422 0.1363 624 PRO A CG 4833 C CD . PRO A 624 ? 1.6841 1.6337 1.2680 0.3105 -0.1584 0.1217 624 PRO A CD 4834 N N . LEU A 625 ? 1.6536 1.5727 1.3609 0.1990 -0.1490 0.0938 625 LEU A N 4835 C CA . LEU A 625 ? 1.5403 1.4259 1.2705 0.1655 -0.1415 0.0892 625 LEU A CA 4836 C C . LEU A 625 ? 1.4445 1.2932 1.1898 0.1533 -0.1360 0.0927 625 LEU A C 4837 O O . LEU A 625 ? 1.4203 1.2940 1.1838 0.1507 -0.1434 0.0873 625 LEU A O 4838 C CB . LEU A 625 ? 1.4898 1.4153 1.2491 0.1392 -0.1540 0.0724 625 LEU A CB 4839 C CG . LEU A 625 ? 1.4653 1.3595 1.2452 0.1125 -0.1478 0.0662 625 LEU A CG 4840 C CD1 . LEU A 625 ? 1.4996 1.3622 1.2577 0.1211 -0.1318 0.0735 625 LEU A CD1 4841 C CD2 . LEU A 625 ? 1.5016 1.4201 1.2968 0.0899 -0.1639 0.0491 625 LEU A CD2 4842 N N . THR A 626 ? 1.4134 1.2066 1.1499 0.1438 -0.1234 0.1029 626 THR A N 4843 C CA . THR A 626 ? 1.3739 1.1264 1.1196 0.1280 -0.1211 0.1067 626 THR A CA 4844 C C . THR A 626 ? 1.4356 1.1820 1.2158 0.0956 -0.1161 0.1056 626 THR A C 4845 O O . THR A 626 ? 1.5794 1.3224 1.3577 0.0910 -0.1057 0.1123 626 THR A O 4846 C CB . THR A 626 ? 1.4017 1.0870 1.1003 0.1424 -0.1147 0.1228 626 THR A CB 4847 O OG1 . THR A 626 ? 1.5581 1.2482 1.2184 0.1824 -0.1188 0.1248 626 THR A OG1 4848 C CG2 . THR A 626 ? 1.3897 1.0293 1.0895 0.1261 -0.1177 0.1234 626 THR A CG2 4849 N N . LEU A 627 ? 1.3091 1.0588 1.1191 0.0765 -0.1229 0.0983 627 LEU A N 4850 C CA . LEU A 627 ? 1.2727 1.0219 1.1168 0.0507 -0.1205 0.0977 627 LEU A CA 4851 C C . LEU A 627 ? 1.2604 0.9710 1.1084 0.0326 -0.1211 0.1064 627 LEU A C 4852 O O . LEU A 627 ? 1.3258 1.0236 1.1700 0.0314 -0.1302 0.1015 627 LEU A O 4853 C CB . LEU A 627 ? 1.2337 1.0162 1.1071 0.0405 -0.1312 0.0822 627 LEU A CB 4854 C CG . LEU A 627 ? 1.3148 1.1291 1.1813 0.0497 -0.1356 0.0715 627 LEU A CG 4855 C CD1 . LEU A 627 ? 1.1996 1.0278 1.0874 0.0322 -0.1482 0.0582 627 LEU A CD1 4856 C CD2 . LEU A 627 ? 1.6212 1.4315 1.4736 0.0598 -0.1234 0.0755 627 LEU A CD2 4857 N N . ILE A 628 ? 1.2649 0.9605 1.1186 0.0172 -0.1121 0.1199 628 ILE A N 4858 C CA . ILE A 628 ? 1.2827 0.9448 1.1414 -0.0080 -0.1160 0.1296 628 ILE A CA 4859 C C . ILE A 628 ? 1.3995 1.0933 1.3068 -0.0275 -0.1217 0.1243 628 ILE A C 4860 O O . ILE A 628 ? 1.5271 1.2589 1.4634 -0.0287 -0.1140 0.1257 628 ILE A O 4861 C CB . ILE A 628 ? 1.3321 0.9690 1.1748 -0.0228 -0.1050 0.1514 628 ILE A CB 4862 C CG1 . ILE A 628 ? 1.3619 0.9587 1.1481 0.0002 -0.0999 0.1586 628 ILE A CG1 4863 C CG2 . ILE A 628 ? 1.4369 1.0369 1.2815 -0.0564 -0.1140 0.1616 628 ILE A CG2 4864 C CD1 . ILE A 628 ? 1.3816 0.9253 1.1245 0.0168 -0.1117 0.1521 628 ILE A CD1 4865 N N . VAL A 629 ? 1.3753 1.0524 1.2866 -0.0383 -0.1353 0.1182 629 VAL A N 4866 C CA . VAL A 629 ? 1.2980 1.0015 1.2502 -0.0533 -0.1436 0.1136 629 VAL A CA 4867 C C . VAL A 629 ? 1.2851 0.9717 1.2488 -0.0822 -0.1515 0.1248 629 VAL A C 4868 O O . VAL A 629 ? 1.2929 0.9296 1.2228 -0.0923 -0.1579 0.1291 629 VAL A O 4869 C CB . VAL A 629 ? 1.2585 0.9658 1.2095 -0.0464 -0.1550 0.0985 629 VAL A CB 4870 C CG1 . VAL A 629 ? 1.3101 1.0444 1.2573 -0.0274 -0.1512 0.0885 629 VAL A CG1 4871 C CG2 . VAL A 629 ? 1.2444 0.9123 1.1595 -0.0439 -0.1620 0.0967 629 VAL A CG2 4872 N N . LYS A 630 ? 1.3207 1.0480 1.3286 -0.0941 -0.1526 0.1293 630 LYS A N 4873 C CA . LYS A 630 ? 1.3431 1.0718 1.3715 -0.1244 -0.1636 0.1406 630 LYS A CA 4874 C C . LYS A 630 ? 1.4490 1.1927 1.5010 -0.1259 -0.1794 0.1312 630 LYS A C 4875 O O . LYS A 630 ? 1.5128 1.2985 1.5973 -0.1134 -0.1772 0.1282 630 LYS A O 4876 C CB . LYS A 630 ? 1.2741 1.0531 1.3388 -0.1369 -0.1516 0.1590 630 LYS A CB 4877 C CG . LYS A 630 ? 1.2679 1.0612 1.3581 -0.1752 -0.1641 0.1751 630 LYS A CG 4878 C CD . LYS A 630 ? 1.4013 1.1335 1.4492 -0.2056 -0.1689 0.1875 630 LYS A CD 4879 C CE . LYS A 630 ? 1.4722 1.2264 1.5474 -0.2528 -0.1820 0.2072 630 LYS A CE 4880 N NZ . LYS A 630 ? 1.4340 1.1148 1.4584 -0.2879 -0.1886 0.2207 630 LYS A NZ 4881 N N . ALA A 631 ? 1.4658 1.1689 1.4939 -0.1384 -0.1956 0.1264 631 ALA A N 4882 C CA . ALA A 631 ? 1.4215 1.1329 1.4637 -0.1407 -0.2115 0.1191 631 ALA A CA 4883 C C . ALA A 631 ? 1.5561 1.2749 1.6179 -0.1708 -0.2284 0.1297 631 ALA A C 4884 O O . ALA A 631 ? 1.7776 1.4521 1.8089 -0.1930 -0.2388 0.1329 631 ALA A O 4885 C CB . ALA A 631 ? 1.3405 1.0112 1.3407 -0.1306 -0.2174 0.1060 631 ALA A CB 4886 N N . GLN A 632 ? 1.3871 1.1596 1.4958 -0.1705 -0.2332 0.1350 632 GLN A N 4887 C CA . GLN A 632 ? 1.2533 1.0524 1.3903 -0.1988 -0.2509 0.1473 632 GLN A CA 4888 C C . GLN A 632 ? 1.2709 1.0836 1.4217 -0.1926 -0.2696 0.1423 632 GLN A C 4889 O O . GLN A 632 ? 1.4728 1.3056 1.6377 -0.1649 -0.2645 0.1367 632 GLN A O 4890 C CB . GLN A 632 ? 1.2211 1.0924 1.4094 -0.2044 -0.2395 0.1651 632 GLN A CB 4891 C CG . GLN A 632 ? 1.2530 1.1153 1.4277 -0.2135 -0.2203 0.1748 632 GLN A CG 4892 C CD . GLN A 632 ? 1.4132 1.3590 1.6402 -0.2197 -0.2066 0.1953 632 GLN A CD 4893 O OE1 . GLN A 632 ? 1.3068 1.3215 1.5831 -0.2204 -0.2142 0.2037 632 GLN A OE1 4894 N NE2 . GLN A 632 ? 1.6362 1.5818 1.8519 -0.2216 -0.1856 0.2051 632 GLN A NE2 4895 N N . ASN A 633 ? 1.1805 0.9740 1.3197 -0.2190 -0.2929 0.1443 633 ASN A N 4896 C CA . ASN A 633 ? 1.1533 0.9692 1.3099 -0.2169 -0.3135 0.1446 633 ASN A CA 4897 C C . ASN A 633 ? 1.1444 1.0186 1.3457 -0.2447 -0.3306 0.1618 633 ASN A C 4898 O O . ASN A 633 ? 1.1790 1.0295 1.3628 -0.2822 -0.3478 0.1662 633 ASN A O 4899 C CB . ASN A 633 ? 1.1951 0.9474 1.2982 -0.2219 -0.3294 0.1324 633 ASN A CB 4900 C CG . ASN A 633 ? 1.2246 0.9945 1.3381 -0.2173 -0.3504 0.1336 633 ASN A CG 4901 O OD1 . ASN A 633 ? 1.1948 1.0150 1.3496 -0.1994 -0.3500 0.1404 633 ASN A OD1 4902 N ND2 . ASN A 633 ? 1.2727 0.9974 1.3424 -0.2298 -0.3689 0.1271 633 ASN A ND2 4903 N N . GLN A 634 ? 1.1329 1.0840 1.3891 -0.2256 -0.3268 0.1716 634 GLN A N 4904 C CA . GLN A 634 ? 1.2130 1.2446 1.5231 -0.2482 -0.3411 0.1911 634 GLN A CA 4905 C C . GLN A 634 ? 1.2204 1.2726 1.5417 -0.2448 -0.3702 0.1923 634 GLN A C 4906 O O . GLN A 634 ? 1.3447 1.4709 1.7119 -0.2630 -0.3879 0.2086 634 GLN A O 4907 C CB . GLN A 634 ? 1.2623 1.3810 1.6279 -0.2239 -0.3179 0.2038 634 GLN A CB 4908 C CG . GLN A 634 ? 1.2473 1.3479 1.5989 -0.2226 -0.2880 0.2034 634 GLN A CG 4909 C CD . GLN A 634 ? 1.2747 1.3456 1.6072 -0.2740 -0.2923 0.2131 634 GLN A CD 4910 O OE1 . GLN A 634 ? 1.2384 1.2437 1.5263 -0.2760 -0.2781 0.2059 634 GLN A OE1 4911 N NE2 . GLN A 634 ? 1.3011 1.4177 1.6636 -0.3165 -0.3137 0.2304 634 GLN A NE2 4912 N N . GLY A 635 ? 1.1440 1.1353 1.4230 -0.2226 -0.3754 0.1771 635 GLY A N 4913 C CA . GLY A 635 ? 1.2634 1.2612 1.5410 -0.2168 -0.4026 0.1784 635 GLY A CA 4914 C C . GLY A 635 ? 1.3687 1.2964 1.5901 -0.2456 -0.4244 0.1692 635 GLY A C 4915 O O . GLY A 635 ? 1.3171 1.1975 1.5052 -0.2735 -0.4220 0.1636 635 GLY A O 4916 N N . GLU A 636 ? 1.4049 1.3204 1.6085 -0.2354 -0.4456 0.1677 636 GLU A N 4917 C CA . GLU A 636 ? 1.3135 1.1643 1.4574 -0.2568 -0.4665 0.1585 636 GLU A CA 4918 C C . GLU A 636 ? 1.1917 0.9638 1.2759 -0.2463 -0.4451 0.1421 636 GLU A C 4919 O O . GLU A 636 ? 1.1450 0.9156 1.2363 -0.2214 -0.4192 0.1388 636 GLU A O 4920 C CB . GLU A 636 ? 1.2923 1.1548 1.4313 -0.2439 -0.4924 0.1634 636 GLU A CB 4921 C CG . GLU A 636 ? 1.4367 1.3914 1.6394 -0.2479 -0.5148 0.1812 636 GLU A CG 4922 C CD . GLU A 636 ? 1.6370 1.6037 1.8332 -0.2277 -0.5410 0.1876 636 GLU A CD 4923 O OE1 . GLU A 636 ? 1.5679 1.6184 1.8185 -0.2185 -0.5578 0.2031 636 GLU A OE1 4924 O OE2 . GLU A 636 ? 1.8158 1.7129 1.9520 -0.2195 -0.5444 0.1789 636 GLU A OE2 4925 N N . GLY A 637 ? 1.1601 0.8703 1.1839 -0.2643 -0.4569 0.1318 637 GLY A N 4926 C CA . GLY A 637 ? 1.1957 0.8421 1.1628 -0.2527 -0.4366 0.1173 637 GLY A CA 4927 C C . GLY A 637 ? 1.1736 0.8176 1.1338 -0.2218 -0.4175 0.1150 637 GLY A C 4928 O O . GLY A 637 ? 1.1632 0.8143 1.1208 -0.2125 -0.4289 0.1201 637 GLY A O 4929 N N . ALA A 638 ? 1.0837 0.7159 1.0378 -0.2085 -0.3902 0.1087 638 ALA A N 4930 C CA . ALA A 638 ? 1.0702 0.7024 1.0183 -0.1870 -0.3728 0.1074 638 ALA A CA 4931 C C . ALA A 638 ? 1.1111 0.7059 1.0017 -0.1818 -0.3625 0.0981 638 ALA A C 4932 O O . ALA A 638 ? 1.1293 0.7048 0.9978 -0.1790 -0.3497 0.0898 638 ALA A O 4933 C CB . ALA A 638 ? 1.0343 0.6919 1.0192 -0.1746 -0.3509 0.1079 638 ALA A CB 4934 N N . TYR A 639 ? 1.2282 0.8154 1.0926 -0.1782 -0.3673 0.1013 639 TYR A N 4935 C CA . TYR A 639 ? 1.2352 0.8019 1.0467 -0.1715 -0.3559 0.0955 639 TYR A CA 4936 C C . TYR A 639 ? 1.1419 0.7283 0.9610 -0.1600 -0.3293 0.0941 639 TYR A C 4937 O O . TYR A 639 ? 1.0974 0.7042 0.9495 -0.1599 -0.3239 0.1003 639 TYR A O 4938 C CB . TYR A 639 ? 1.2652 0.8249 1.0472 -0.1741 -0.3675 0.1034 639 TYR A CB 4939 C CG . TYR A 639 ? 1.3228 0.8705 1.0998 -0.1846 -0.3975 0.1068 639 TYR A CG 4940 C CD1 . TYR A 639 ? 1.3982 0.9145 1.1306 -0.1913 -0.4119 0.0975 639 TYR A CD1 4941 C CD2 . TYR A 639 ? 1.3266 0.8925 1.1385 -0.1858 -0.4136 0.1190 639 TYR A CD2 4942 C CE1 . TYR A 639 ? 1.5060 1.0157 1.2333 -0.2048 -0.4431 0.1008 639 TYR A CE1 4943 C CE2 . TYR A 639 ? 1.3276 0.8938 1.1384 -0.1937 -0.4430 0.1237 639 TYR A CE2 4944 C CZ . TYR A 639 ? 1.4028 0.9441 1.1734 -0.2061 -0.4586 0.1148 639 TYR A CZ 4945 O OH . TYR A 639 ? 1.4636 1.0093 1.2328 -0.2178 -0.4916 0.1196 639 TYR A OH 4946 N N . GLU A 640 ? 1.2006 0.7790 0.9843 -0.1484 -0.3145 0.0855 640 GLU A N 4947 C CA . GLU A 640 ? 1.2583 0.8663 1.0458 -0.1364 -0.2908 0.0850 640 GLU A CA 4948 C C . GLU A 640 ? 1.2792 0.9072 1.1147 -0.1368 -0.2832 0.0858 640 GLU A C 4949 O O . GLU A 640 ? 1.2621 0.9172 1.1155 -0.1388 -0.2743 0.0906 640 GLU A O 4950 C CB . GLU A 640 ? 1.2580 0.8910 1.0351 -0.1420 -0.2856 0.0953 640 GLU A CB 4951 C CG . GLU A 640 ? 1.4215 1.0411 1.1465 -0.1394 -0.2898 0.0963 640 GLU A CG 4952 C CD . GLU A 640 ? 1.5571 1.2074 1.2713 -0.1491 -0.2817 0.1107 640 GLU A CD 4953 O OE1 . GLU A 640 ? 1.6804 1.3222 1.3529 -0.1496 -0.2857 0.1153 640 GLU A OE1 4954 O OE2 . GLU A 640 ? 1.5215 1.2029 1.2652 -0.1589 -0.2723 0.1183 640 GLU A OE2 4955 N N . ALA A 641 ? 1.3210 0.9343 1.1731 -0.1374 -0.2876 0.0819 641 ALA A N 4956 C CA . ALA A 641 ? 1.2858 0.9183 1.1788 -0.1354 -0.2791 0.0829 641 ALA A CA 4957 C C . ALA A 641 ? 1.1067 0.7560 0.9920 -0.1203 -0.2590 0.0784 641 ALA A C 4958 O O . ALA A 641 ? 1.1237 0.7598 0.9747 -0.1070 -0.2519 0.0727 641 ALA A O 4959 C CB . ALA A 641 ? 1.4773 1.0967 1.3867 -0.1427 -0.2866 0.0833 641 ALA A CB 4960 N N . GLU A 642 ? 1.0969 0.7729 1.0095 -0.1200 -0.2518 0.0804 642 GLU A N 4961 C CA . GLU A 642 ? 1.1218 0.8228 1.0319 -0.1077 -0.2360 0.0772 642 GLU A CA 4962 C C . GLU A 642 ? 1.1214 0.8329 1.0614 -0.1058 -0.2314 0.0763 642 GLU A C 4963 O O . GLU A 642 ? 1.0713 0.7806 1.0323 -0.1136 -0.2385 0.0785 642 GLU A O 4964 C CB . GLU A 642 ? 1.1766 0.9093 1.0773 -0.1127 -0.2320 0.0809 642 GLU A CB 4965 C CG . GLU A 642 ? 1.4311 1.1681 1.2961 -0.1052 -0.2285 0.0814 642 GLU A CG 4966 C CD . GLU A 642 ? 1.6362 1.4202 1.4972 -0.1142 -0.2221 0.0894 642 GLU A CD 4967 O OE1 . GLU A 642 ? 1.6377 1.4344 1.5195 -0.1350 -0.2267 0.0954 642 GLU A OE1 4968 O OE2 . GLU A 642 ? 1.7269 1.5347 1.5607 -0.1007 -0.2127 0.0904 642 GLU A OE2 4969 N N . LEU A 643 ? 1.2020 0.9215 1.1374 -0.0914 -0.2197 0.0730 643 LEU A N 4970 C CA . LEU A 643 ? 1.1301 0.8614 1.0858 -0.0868 -0.2135 0.0717 643 LEU A CA 4971 C C . LEU A 643 ? 0.9996 0.7628 0.9549 -0.0869 -0.2102 0.0694 643 LEU A C 4972 O O . LEU A 643 ? 0.9984 0.7870 0.9394 -0.0771 -0.2033 0.0687 643 LEU A O 4973 C CB . LEU A 643 ? 1.0990 0.8187 1.0458 -0.0733 -0.2041 0.0718 643 LEU A CB 4974 C CG . LEU A 643 ? 1.1331 0.8685 1.0925 -0.0646 -0.1950 0.0710 643 LEU A CG 4975 C CD1 . LEU A 643 ? 1.1770 0.9142 1.1648 -0.0719 -0.1981 0.0726 643 LEU A CD1 4976 C CD2 . LEU A 643 ? 1.1486 0.8676 1.0898 -0.0516 -0.1855 0.0742 643 LEU A CD2 4977 N N . ILE A 644 ? 0.9821 0.7436 0.9501 -0.0973 -0.2166 0.0683 644 ILE A N 4978 C CA . ILE A 644 ? 1.0148 0.7987 0.9782 -0.1065 -0.2187 0.0662 644 ILE A CA 4979 C C . ILE A 644 ? 1.1484 0.9396 1.1140 -0.0949 -0.2134 0.0598 644 ILE A C 4980 O O . ILE A 644 ? 1.2817 1.0499 1.2528 -0.0895 -0.2144 0.0561 644 ILE A O 4981 C CB . ILE A 644 ? 1.0715 0.8324 1.0317 -0.1275 -0.2326 0.0682 644 ILE A CB 4982 C CG1 . ILE A 644 ? 1.0908 0.8425 1.0449 -0.1382 -0.2382 0.0762 644 ILE A CG1 4983 C CG2 . ILE A 644 ? 1.1235 0.9030 1.0735 -0.1466 -0.2382 0.0675 644 ILE A CG2 4984 C CD1 . ILE A 644 ? 1.0041 0.7949 0.9477 -0.1412 -0.2311 0.0811 644 ILE A CD1 4985 N N . VAL A 645 ? 1.1383 0.9657 1.0974 -0.0876 -0.2075 0.0591 645 VAL A N 4986 C CA . VAL A 645 ? 1.0920 0.9300 1.0476 -0.0761 -0.2039 0.0536 645 VAL A CA 4987 C C . VAL A 645 ? 1.2078 1.0736 1.1575 -0.0945 -0.2144 0.0506 645 VAL A C 4988 O O . VAL A 645 ? 1.3028 1.2174 1.2537 -0.1003 -0.2150 0.0554 645 VAL A O 4989 C CB . VAL A 645 ? 1.0770 0.9330 1.0246 -0.0507 -0.1917 0.0561 645 VAL A CB 4990 C CG1 . VAL A 645 ? 1.1391 1.0074 1.0791 -0.0385 -0.1890 0.0518 645 VAL A CG1 4991 C CG2 . VAL A 645 ? 1.0956 0.9147 1.0422 -0.0407 -0.1845 0.0602 645 VAL A CG2 4992 N N . SER A 646 ? 1.2663 1.1027 1.2071 -0.1034 -0.2235 0.0428 646 SER A N 4993 C CA . SER A 646 ? 1.3377 1.1865 1.2651 -0.1285 -0.2387 0.0391 646 SER A CA 4994 C C . SER A 646 ? 1.5656 1.4427 1.4839 -0.1159 -0.2380 0.0326 646 SER A C 4995 O O . SER A 646 ? 1.7857 1.6318 1.6908 -0.0981 -0.2347 0.0239 646 SER A O 4996 C CB . SER A 646 ? 1.2336 1.0184 1.1412 -0.1446 -0.2530 0.0323 646 SER A CB 4997 O OG . SER A 646 ? 1.2080 0.9660 1.1212 -0.1540 -0.2554 0.0398 646 SER A OG 4998 N N . ILE A 647 ? 1.5244 1.4665 1.4491 -0.1231 -0.2408 0.0380 647 ILE A N 4999 C CA . ILE A 647 ? 1.5323 1.5103 1.4479 -0.1110 -0.2433 0.0335 647 ILE A CA 5000 C C . ILE A 647 ? 1.7220 1.7214 1.6262 -0.1487 -0.2664 0.0297 647 ILE A C 5001 O O . ILE A 647 ? 1.8708 1.9309 1.7903 -0.1746 -0.2740 0.0396 647 ILE A O 5002 C CB . ILE A 647 ? 1.4381 1.4807 1.3665 -0.0833 -0.2309 0.0428 647 ILE A CB 5003 C CG1 . ILE A 647 ? 1.4413 1.5334 1.3885 -0.0960 -0.2293 0.0541 647 ILE A CG1 5004 C CG2 . ILE A 647 ? 1.4234 1.4278 1.3469 -0.0468 -0.2122 0.0441 647 ILE A CG2 5005 C CD1 . ILE A 647 ? 1.4162 1.5711 1.3686 -0.0611 -0.2173 0.0620 647 ILE A CD1 5006 N N . PRO A 648 ? 1.7704 1.7199 1.6444 -0.1534 -0.2782 0.0158 648 PRO A N 5007 C CA . PRO A 648 ? 1.8569 1.8073 1.7084 -0.1945 -0.3050 0.0099 648 PRO A CA 5008 C C . PRO A 648 ? 1.7065 1.7412 1.5637 -0.1978 -0.3144 0.0124 648 PRO A C 5009 O O . PRO A 648 ? 1.5709 1.6280 1.4272 -0.1591 -0.3029 0.0103 648 PRO A O 5010 C CB . PRO A 648 ? 2.0213 1.8797 1.8288 -0.1853 -0.3119 -0.0086 648 PRO A CB 5011 C CG . PRO A 648 ? 1.9333 1.7882 1.7473 -0.1346 -0.2871 -0.0104 648 PRO A CG 5012 C CD . PRO A 648 ? 1.7894 1.6792 1.6444 -0.1208 -0.2672 0.0052 648 PRO A CD 5013 N N . LEU A 649 ? 1.7176 1.8007 1.5799 -0.2453 -0.3359 0.0188 649 LEU A N 5014 C CA . LEU A 649 ? 1.6677 1.8269 1.5295 -0.2601 -0.3544 0.0191 649 LEU A CA 5015 C C . LEU A 649 ? 1.5472 1.7973 1.4363 -0.2138 -0.3381 0.0277 649 LEU A C 5016 O O . LEU A 649 ? 1.4625 1.7796 1.3870 -0.1989 -0.3223 0.0429 649 LEU A O 5017 C CB . LEU A 649 ? 1.7495 1.8357 1.5582 -0.2660 -0.3744 -0.0019 649 LEU A CB 5018 C CG . LEU A 649 ? 1.7671 1.7383 1.5327 -0.2983 -0.3900 -0.0139 649 LEU A CG 5019 C CD1 . LEU A 649 ? 1.8922 1.7715 1.6021 -0.2705 -0.3933 -0.0373 649 LEU A CD1 5020 C CD2 . LEU A 649 ? 1.7123 1.6972 1.4657 -0.3698 -0.4236 -0.0088 649 LEU A CD2 5021 N N . GLN A 650 ? 1.5903 1.8355 1.4548 -0.1882 -0.3426 0.0174 650 GLN A N 5022 C CA . GLN A 650 ? 1.4899 1.8131 1.3676 -0.1443 -0.3332 0.0251 650 GLN A CA 5023 C C . GLN A 650 ? 1.4505 1.7694 1.3449 -0.0933 -0.3013 0.0346 650 GLN A C 5024 O O . GLN A 650 ? 1.3836 1.7746 1.2926 -0.0588 -0.2930 0.0456 650 GLN A O 5025 C CB . GLN A 650 ? 1.4635 1.7542 1.2996 -0.1242 -0.3420 0.0114 650 GLN A CB 5026 C CG . GLN A 650 ? 1.5619 1.7501 1.3523 -0.1501 -0.3563 -0.0086 650 GLN A CG 5027 C CD . GLN A 650 ? 1.3973 1.4890 1.1763 -0.1246 -0.3317 -0.0145 650 GLN A CD 5028 O OE1 . GLN A 650 ? 1.3081 1.4031 1.1065 -0.0864 -0.3049 -0.0050 650 GLN A OE1 5029 N NE2 . GLN A 650 ? 1.3662 1.3709 1.1108 -0.1458 -0.3424 -0.0298 650 GLN A NE2 5030 N N . ALA A 651 ? 1.4885 1.7208 1.3768 -0.0876 -0.2853 0.0303 651 ALA A N 5031 C CA . ALA A 651 ? 1.3708 1.5840 1.2677 -0.0467 -0.2589 0.0380 651 ALA A CA 5032 C C . ALA A 651 ? 1.2593 1.5349 1.1864 -0.0463 -0.2517 0.0514 651 ALA A C 5033 O O . ALA A 651 ? 1.2427 1.5316 1.1866 -0.0846 -0.2590 0.0545 651 ALA A O 5034 C CB . ALA A 651 ? 1.4104 1.5270 1.2972 -0.0471 -0.2474 0.0312 651 ALA A CB 5035 N N . ASP A 652 ? 1.2629 1.5721 1.1903 -0.0007 -0.2373 0.0598 652 ASP A N 5036 C CA . ASP A 652 ? 1.3389 1.6996 1.2851 0.0125 -0.2266 0.0708 652 ASP A CA 5037 C C . ASP A 652 ? 1.3722 1.6744 1.2976 0.0590 -0.2058 0.0726 652 ASP A C 5038 O O . ASP A 652 ? 1.2980 1.5621 1.1975 0.0917 -0.2003 0.0716 652 ASP A O 5039 C CB . ASP A 652 ? 1.4435 1.9283 1.4078 0.0238 -0.2340 0.0809 652 ASP A CB 5040 C CG . ASP A 652 ? 1.5423 2.0455 1.4856 0.0733 -0.2331 0.0819 652 ASP A CG 5041 O OD1 . ASP A 652 ? 1.6200 2.0506 1.5361 0.0798 -0.2342 0.0738 652 ASP A OD1 5042 O OD2 . ASP A 652 ? 1.5085 2.1015 1.4601 0.1083 -0.2308 0.0921 652 ASP A OD2 5043 N N . PHE A 653 ? 1.4458 1.7361 1.3770 0.0589 -0.1957 0.0761 653 PHE A N 5044 C CA . PHE A 653 ? 1.3837 1.6035 1.2889 0.0933 -0.1801 0.0762 653 PHE A CA 5045 C C . PHE A 653 ? 1.3683 1.6182 1.2489 0.1504 -0.1716 0.0821 653 PHE A C 5046 O O . PHE A 653 ? 1.4399 1.7857 1.3340 0.1661 -0.1727 0.0884 653 PHE A O 5047 C CB . PHE A 653 ? 1.3085 1.5067 1.2214 0.0749 -0.1752 0.0768 653 PHE A CB 5048 C CG . PHE A 653 ? 1.3016 1.4187 1.1839 0.1009 -0.1640 0.0752 653 PHE A CG 5049 C CD1 . PHE A 653 ? 1.3014 1.3319 1.1738 0.0900 -0.1635 0.0713 653 PHE A CD1 5050 C CD2 . PHE A 653 ? 1.3993 1.5280 1.2598 0.1353 -0.1548 0.0780 653 PHE A CD2 5051 C CE1 . PHE A 653 ? 1.3636 1.3204 1.2073 0.1052 -0.1568 0.0713 653 PHE A CE1 5052 C CE2 . PHE A 653 ? 1.4657 1.5072 1.2884 0.1551 -0.1486 0.0750 653 PHE A CE2 5053 C CZ . PHE A 653 ? 1.4140 1.3692 1.2294 0.1359 -0.1510 0.0723 653 PHE A CZ 5054 N N . ILE A 654 ? 1.3370 1.5053 1.1794 0.1818 -0.1635 0.0816 654 ILE A N 5055 C CA . ILE A 654 ? 1.4183 1.5870 1.2221 0.2413 -0.1562 0.0869 654 ILE A CA 5056 C C . ILE A 654 ? 1.5103 1.6110 1.2803 0.2624 -0.1461 0.0855 654 ILE A C 5057 O O . ILE A 654 ? 1.5900 1.7360 1.3510 0.2941 -0.1406 0.0870 654 ILE A O 5058 C CB . ILE A 654 ? 1.4995 1.6140 1.2685 0.2646 -0.1563 0.0899 654 ILE A CB 5059 C CG1 . ILE A 654 ? 1.5559 1.7393 1.3484 0.2503 -0.1680 0.0899 654 ILE A CG1 5060 C CG2 . ILE A 654 ? 1.4949 1.5874 1.2117 0.3293 -0.1499 0.0961 654 ILE A CG2 5061 C CD1 . ILE A 654 ? 1.6003 1.7432 1.3546 0.2781 -0.1678 0.0947 654 ILE A CD1 5062 N N . GLY A 655 ? 1.5558 1.5514 1.3055 0.2448 -0.1443 0.0827 655 GLY A N 5063 C CA . GLY A 655 ? 1.6585 1.5761 1.3694 0.2577 -0.1393 0.0801 655 GLY A CA 5064 C C . GLY A 655 ? 1.5524 1.3683 1.2519 0.2254 -0.1410 0.0794 655 GLY A C 5065 O O . GLY A 655 ? 1.4198 1.2369 1.1521 0.1891 -0.1437 0.0803 655 GLY A O 5066 N N . VAL A 656 ? 1.5614 1.2908 1.2112 0.2393 -0.1400 0.0780 656 VAL A N 5067 C CA . VAL A 656 ? 1.5976 1.2338 1.2336 0.2065 -0.1436 0.0800 656 VAL A CA 5068 C C . VAL A 656 ? 1.7541 1.2980 1.3205 0.2358 -0.1428 0.0866 656 VAL A C 5069 O O . VAL A 656 ? 1.9284 1.4666 1.4484 0.2878 -0.1402 0.0862 656 VAL A O 5070 C CB . VAL A 656 ? 1.5927 1.1951 1.2264 0.1840 -0.1489 0.0731 656 VAL A CB 5071 C CG1 . VAL A 656 ? 1.6134 1.1603 1.2625 0.1362 -0.1551 0.0769 656 VAL A CG1 5072 C CG2 . VAL A 656 ? 1.6135 1.3060 1.2960 0.1715 -0.1486 0.0682 656 VAL A CG2 5073 N N . VAL A 657 ? 1.7921 1.2647 1.3485 0.2034 -0.1450 0.0944 657 VAL A N 5074 C CA . VAL A 657 ? 2.0132 1.3920 1.5006 0.2226 -0.1451 0.1047 657 VAL A CA 5075 C C . VAL A 657 ? 2.0818 1.3482 1.5004 0.2246 -0.1539 0.1013 657 VAL A C 5076 O O . VAL A 657 ? 2.0722 1.2936 1.4980 0.1780 -0.1615 0.1024 657 VAL A O 5077 C CB . VAL A 657 ? 1.9406 1.3028 1.4473 0.1840 -0.1418 0.1190 657 VAL A CB 5078 C CG1 . VAL A 657 ? 1.8207 1.2549 1.3518 0.2024 -0.1341 0.1235 657 VAL A CG1 5079 C CG2 . VAL A 657 ? 1.8523 1.2418 1.4206 0.1290 -0.1441 0.1174 657 VAL A CG2 5080 N N . ARG A 658 ? 2.0372 1.2593 1.3855 0.2815 -0.1542 0.0969 658 ARG A N 5081 C CA . ARG A 658 ? 2.1817 1.2798 1.4439 0.2940 -0.1641 0.0911 658 ARG A CA 5082 C C . ARG A 658 ? 2.3434 1.3116 1.5326 0.2838 -0.1708 0.1055 658 ARG A C 5083 O O . ARG A 658 ? 2.4459 1.3014 1.5798 0.2566 -0.1839 0.1049 658 ARG A O 5084 C CB . ARG A 658 ? 2.3028 1.4091 1.5141 0.3677 -0.1603 0.0791 658 ARG A CB 5085 C CG . ARG A 658 ? 2.2359 1.4818 1.5193 0.3758 -0.1520 0.0696 658 ARG A CG 5086 C CD . ARG A 658 ? 2.3786 1.6489 1.6146 0.4511 -0.1453 0.0606 658 ARG A CD 5087 N NE . ARG A 658 ? 2.2192 1.6345 1.5280 0.4522 -0.1362 0.0563 658 ARG A NE 5088 C CZ . ARG A 658 ? 2.0746 1.5090 1.3966 0.4344 -0.1362 0.0469 658 ARG A CZ 5089 N NH1 . ARG A 658 ? 2.1180 1.4375 1.3861 0.4160 -0.1464 0.0385 658 ARG A NH1 5090 N NH2 . ARG A 658 ? 1.9011 1.4684 1.2872 0.4320 -0.1275 0.0472 658 ARG A NH2 5091 N N . ASN A 659 ? 2.3464 1.3295 1.5322 0.3025 -0.1632 0.1195 659 ASN A N 5092 C CA . ASN A 659 ? 2.3787 1.2378 1.4841 0.3019 -0.1679 0.1366 659 ASN A CA 5093 C C . ASN A 659 ? 2.3370 1.1408 1.4546 0.2235 -0.1739 0.1514 659 ASN A C 5094 O O . ASN A 659 ? 2.4199 1.0900 1.4559 0.2077 -0.1844 0.1626 659 ASN A O 5095 C CB . ASN A 659 ? 2.2632 1.1683 1.3701 0.3383 -0.1577 0.1497 659 ASN A CB 5096 C CG . ASN A 659 ? 2.0295 1.0573 1.2368 0.2994 -0.1475 0.1558 659 ASN A CG 5097 O OD1 . ASN A 659 ? 1.9363 1.0538 1.2227 0.2708 -0.1456 0.1444 659 ASN A OD1 5098 N ND2 . ASN A 659 ? 2.0270 1.0522 1.2239 0.3004 -0.1413 0.1737 659 ASN A ND2 5099 N N . ASN A 660 ? 2.1881 1.0944 1.4046 0.1746 -0.1681 0.1526 660 ASN A N 5100 C CA . ASN A 660 ? 2.1822 1.0657 1.4242 0.1031 -0.1711 0.1692 660 ASN A CA 5101 C C . ASN A 660 ? 2.1433 0.9654 1.3709 0.0613 -0.1888 0.1617 660 ASN A C 5102 O O . ASN A 660 ? 2.0370 0.9025 1.2943 0.0685 -0.1932 0.1424 660 ASN A O 5103 C CB . ASN A 660 ? 2.1256 1.1424 1.4735 0.0754 -0.1578 0.1729 660 ASN A CB 5104 C CG . ASN A 660 ? 2.0702 1.0806 1.4418 0.0151 -0.1544 0.1961 660 ASN A CG 5105 O OD1 . ASN A 660 ? 1.9683 0.9029 1.3106 -0.0290 -0.1667 0.2057 660 ASN A OD1 5106 N ND2 . ASN A 660 ? 2.0633 1.1568 1.4861 0.0124 -0.1381 0.2059 660 ASN A ND2 5107 N N . GLU A 661 ? 2.2610 0.9817 1.4399 0.0144 -0.2002 0.1788 661 GLU A N 5108 C CA . GLU A 661 ? 2.3710 1.0282 1.5320 -0.0352 -0.2214 0.1745 661 GLU A CA 5109 C C . GLU A 661 ? 2.1758 0.9448 1.4452 -0.0930 -0.2199 0.1795 661 GLU A C 5110 O O . GLU A 661 ? 2.0939 0.8706 1.3831 -0.1173 -0.2346 0.1673 661 GLU A O 5111 C CB . GLU A 661 ? 2.5318 1.0911 1.6255 -0.0693 -0.2303 0.1844 661 GLU A CB 5112 C CG . GLU A 661 ? 2.6357 1.1585 1.7207 -0.1247 -0.2522 0.1763 661 GLU A CG 5113 C CD . GLU A 661 ? 2.8056 1.2708 1.8282 -0.0853 -0.2659 0.1458 661 GLU A CD 5114 O OE1 . GLU A 661 ? 2.9038 1.3374 1.8717 -0.0143 -0.2580 0.1325 661 GLU A OE1 5115 O OE2 . GLU A 661 ? 2.8307 1.2871 1.8574 -0.1231 -0.2844 0.1359 661 GLU A OE2 5116 N N . ALA A 662 ? 2.0236 0.8792 1.3587 -0.1099 -0.2022 0.1973 662 ALA A N 5117 C CA . ALA A 662 ? 1.9239 0.8898 1.3594 -0.1558 -0.1980 0.2041 662 ALA A CA 5118 C C . ALA A 662 ? 1.9357 1.0084 1.4423 -0.1263 -0.1917 0.1820 662 ALA A C 5119 O O . ALA A 662 ? 1.8714 1.0312 1.4563 -0.1541 -0.1902 0.1834 662 ALA A O 5120 C CB . ALA A 662 ? 1.9009 0.9207 1.3729 -0.1759 -0.1789 0.2299 662 ALA A CB 5121 N N . LEU A 663 ? 1.9542 1.0207 1.4311 -0.0698 -0.1885 0.1634 663 LEU A N 5122 C CA . LEU A 663 ? 1.7703 0.9348 1.3076 -0.0442 -0.1823 0.1454 663 LEU A CA 5123 C C . LEU A 663 ? 1.8071 0.9399 1.3108 -0.0220 -0.1944 0.1250 663 LEU A C 5124 O O . LEU A 663 ? 1.8617 0.8924 1.2838 -0.0092 -0.2051 0.1212 663 LEU A O 5125 C CB . LEU A 663 ? 1.6394 0.8608 1.1885 0.0000 -0.1650 0.1441 663 LEU A CB 5126 C CG . LEU A 663 ? 1.5400 0.8127 1.1307 -0.0183 -0.1509 0.1609 663 LEU A CG 5127 C CD1 . LEU A 663 ? 1.5088 0.8296 1.1008 0.0252 -0.1379 0.1579 663 LEU A CD1 5128 C CD2 . LEU A 663 ? 1.4616 0.8141 1.1335 -0.0538 -0.1497 0.1608 663 LEU A CD2 5129 N N . ALA A 664 ? 1.7973 1.0132 1.3577 -0.0164 -0.1925 0.1125 664 ALA A N 5130 C CA . ALA A 664 ? 1.7378 0.9382 1.2765 -0.0044 -0.2030 0.0958 664 ALA A CA 5131 C C . ALA A 664 ? 1.7241 0.9555 1.2424 0.0526 -0.1929 0.0835 664 ALA A C 5132 O O . ALA A 664 ? 1.6812 0.9851 1.2351 0.0732 -0.1797 0.0855 664 ALA A O 5133 C CB . ALA A 664 ? 1.6266 0.8940 1.2344 -0.0378 -0.2093 0.0928 664 ALA A CB 5134 N N . ARG A 665 ? 1.8789 1.0579 1.3375 0.0773 -0.2000 0.0710 665 ARG A N 5135 C CA . ARG A 665 ? 2.0311 1.2392 1.4613 0.1360 -0.1899 0.0607 665 ARG A CA 5136 C C . ARG A 665 ? 1.8208 1.1295 1.3085 0.1341 -0.1853 0.0536 665 ARG A C 5137 O O . ARG A 665 ? 1.8305 1.1789 1.3014 0.1760 -0.1770 0.0464 665 ARG A O 5138 C CB . ARG A 665 ? 2.3238 1.4216 1.6507 0.1709 -0.1980 0.0505 665 ARG A CB 5139 C CG . ARG A 665 ? 2.3972 1.5098 1.6780 0.2446 -0.1853 0.0446 665 ARG A CG 5140 C CD . ARG A 665 ? 2.5900 1.6021 1.7683 0.2847 -0.1926 0.0299 665 ARG A CD 5141 N NE . ARG A 665 ? 2.6742 1.7070 1.8626 0.2676 -0.1980 0.0183 665 ARG A NE 5142 C CZ . ARG A 665 ? 2.5383 1.6639 1.7484 0.2996 -0.1852 0.0116 665 ARG A CZ 5143 N NH1 . ARG A 665 ? 2.4934 1.7075 1.7226 0.3486 -0.1673 0.0153 665 ARG A NH1 5144 N NH2 . ARG A 665 ? 2.3822 1.5170 1.5947 0.2806 -0.1909 0.0032 665 ARG A NH2 5145 N N . LEU A 666 ? 1.7116 1.0623 1.2646 0.0863 -0.1905 0.0574 666 LEU A N 5146 C CA . LEU A 666 ? 1.6998 1.1197 1.2962 0.0744 -0.1911 0.0526 666 LEU A CA 5147 C C . LEU A 666 ? 1.6564 1.1658 1.2737 0.1065 -0.1771 0.0509 666 LEU A C 5148 O O . LEU A 666 ? 1.5917 1.1512 1.2377 0.1158 -0.1686 0.0562 666 LEU A O 5149 C CB . LEU A 666 ? 1.6504 1.1097 1.3176 0.0273 -0.1964 0.0597 666 LEU A CB 5150 C CG . LEU A 666 ? 1.7679 1.1701 1.4347 -0.0122 -0.2108 0.0650 666 LEU A CG 5151 C CD1 . LEU A 666 ? 1.5149 0.9752 1.2557 -0.0445 -0.2109 0.0735 666 LEU A CD1 5152 C CD2 . LEU A 666 ? 1.9528 1.3070 1.5827 -0.0229 -0.2269 0.0571 666 LEU A CD2 5153 N N . SER A 667 ? 1.7538 1.2863 1.3546 0.1213 -0.1755 0.0446 667 SER A N 5154 C CA . SER A 667 ? 1.7016 1.3275 1.3193 0.1495 -0.1621 0.0457 667 SER A CA 5155 C C . SER A 667 ? 1.4958 1.2077 1.1885 0.1139 -0.1614 0.0530 667 SER A C 5156 O O . SER A 667 ? 1.3573 1.0698 1.0773 0.0770 -0.1696 0.0542 667 SER A O 5157 C CB . SER A 667 ? 1.6983 1.3276 1.2748 0.1730 -0.1587 0.0391 667 SER A CB 5158 O OG . SER A 667 ? 1.6407 1.2594 1.2329 0.1336 -0.1689 0.0385 667 SER A OG 5159 N N . CYS A 668 ? 1.3905 1.1697 1.1102 0.1263 -0.1539 0.0577 668 CYS A N 5160 C CA . CYS A 668 ? 1.3048 1.1559 1.0840 0.0930 -0.1558 0.0633 668 CYS A CA 5161 C C . CYS A 668 ? 1.3166 1.2690 1.1107 0.1083 -0.1477 0.0682 668 CYS A C 5162 O O . CYS A 668 ? 1.4687 1.4477 1.2354 0.1533 -0.1386 0.0681 668 CYS A O 5163 C CB . CYS A 668 ? 1.2491 1.0900 1.0512 0.0819 -0.1584 0.0649 668 CYS A CB 5164 S SG . CYS A 668 ? 2.0041 1.7517 1.8018 0.0577 -0.1659 0.0642 668 CYS A SG 5165 N N . ALA A 669 ? 1.3002 1.3095 1.1354 0.0706 -0.1518 0.0740 669 ALA A N 5166 C CA . ALA A 669 ? 1.3139 1.4300 1.1701 0.0718 -0.1462 0.0825 669 ALA A CA 5167 C C . ALA A 669 ? 1.3299 1.4897 1.2295 0.0305 -0.1563 0.0872 669 ALA A C 5168 O O . ALA A 669 ? 1.2709 1.3797 1.1834 -0.0045 -0.1668 0.0845 669 ALA A O 5169 C CB . ALA A 669 ? 1.3381 1.4825 1.1868 0.0634 -0.1411 0.0879 669 ALA A CB 5170 N N . PHE A 670 ? 1.4212 1.6755 1.3397 0.0365 -0.1545 0.0939 670 PHE A N 5171 C CA . PHE A 670 ? 1.3553 1.6512 1.3069 -0.0053 -0.1675 0.0977 670 PHE A CA 5172 C C . PHE A 670 ? 1.3423 1.6991 1.3145 -0.0494 -0.1713 0.1101 670 PHE A C 5173 O O . PHE A 670 ? 1.4013 1.8550 1.3829 -0.0404 -0.1624 0.1215 670 PHE A O 5174 C CB . PHE A 670 ? 1.3175 1.6844 1.2779 0.0192 -0.1682 0.0992 670 PHE A CB 5175 C CG . PHE A 670 ? 1.3671 1.7764 1.3545 -0.0251 -0.1851 0.1016 670 PHE A CG 5176 C CD1 . PHE A 670 ? 1.3455 1.6773 1.3290 -0.0509 -0.1974 0.0918 670 PHE A CD1 5177 C CD2 . PHE A 670 ? 1.5342 2.0628 1.5477 -0.0405 -0.1896 0.1137 670 PHE A CD2 5178 C CE1 . PHE A 670 ? 1.5050 1.8616 1.5007 -0.0900 -0.2152 0.0913 670 PHE A CE1 5179 C CE2 . PHE A 670 ? 1.6048 2.1645 1.6362 -0.0871 -0.2094 0.1151 670 PHE A CE2 5180 C CZ . PHE A 670 ? 1.6124 2.0781 1.6302 -0.1111 -0.2230 0.1024 670 PHE A CZ 5181 N N . LYS A 671 ? 1.3389 1.6395 1.3156 -0.0957 -0.1839 0.1095 671 LYS A N 5182 C CA . LYS A 671 ? 1.4112 1.7448 1.3971 -0.1420 -0.1889 0.1232 671 LYS A CA 5183 C C . LYS A 671 ? 1.4943 1.8319 1.4937 -0.1955 -0.2090 0.1264 671 LYS A C 5184 O O . LYS A 671 ? 1.4375 1.6956 1.4282 -0.2050 -0.2212 0.1146 671 LYS A O 5185 C CB . LYS A 671 ? 1.4818 1.7333 1.4481 -0.1497 -0.1885 0.1221 671 LYS A CB 5186 C CG . LYS A 671 ? 1.5791 1.8566 1.5458 -0.1937 -0.1918 0.1389 671 LYS A CG 5187 C CD . LYS A 671 ? 1.5413 1.7339 1.4849 -0.1963 -0.1937 0.1374 671 LYS A CD 5188 C CE . LYS A 671 ? 1.5174 1.7337 1.4542 -0.2375 -0.1956 0.1568 671 LYS A CE 5189 N NZ . LYS A 671 ? 1.5460 1.7663 1.4922 -0.2932 -0.2128 0.1668 671 LYS A NZ 5190 N N . THR A 672 ? 1.6077 2.0387 1.6247 -0.2307 -0.2126 0.1429 672 THR A N 5191 C CA . THR A 672 ? 1.6711 2.1026 1.6928 -0.2905 -0.2355 0.1477 672 THR A CA 5192 C C . THR A 672 ? 1.7478 2.1956 1.7672 -0.3458 -0.2404 0.1680 672 THR A C 5193 O O . THR A 672 ? 1.7836 2.3326 1.8193 -0.3487 -0.2268 0.1863 672 THR A O 5194 C CB . THR A 672 ? 1.6498 2.1864 1.6954 -0.2955 -0.2425 0.1514 672 THR A CB 5195 O OG1 . THR A 672 ? 1.7060 2.3765 1.7772 -0.2877 -0.2277 0.1704 672 THR A OG1 5196 C CG2 . THR A 672 ? 1.5378 2.0538 1.5793 -0.2413 -0.2386 0.1335 672 THR A CG2 5197 N N . GLU A 673 ? 1.7583 2.1067 1.7533 -0.3876 -0.2594 0.1660 673 GLU A N 5198 C CA . GLU A 673 ? 1.7424 2.0803 1.7238 -0.4440 -0.2673 0.1864 673 GLU A CA 5199 C C . GLU A 673 ? 1.8002 2.0053 1.7441 -0.4790 -0.2922 0.1789 673 GLU A C 5200 O O . GLU A 673 ? 1.7047 1.8238 1.6346 -0.4480 -0.2973 0.1570 673 GLU A O 5201 C CB . GLU A 673 ? 1.6599 2.0005 1.6354 -0.4204 -0.2468 0.1958 673 GLU A CB 5202 C CG . GLU A 673 ? 1.6981 2.1660 1.6917 -0.4400 -0.2320 0.2221 673 GLU A CG 5203 C CD . GLU A 673 ? 1.6793 2.1580 1.6627 -0.3974 -0.2079 0.2253 673 GLU A CD 5204 O OE1 . GLU A 673 ? 1.6051 1.9991 1.5714 -0.3524 -0.2041 0.2059 673 GLU A OE1 5205 O OE2 . GLU A 673 ? 1.7150 2.2891 1.7052 -0.4102 -0.1930 0.2476 673 GLU A OE2 5206 N N . ASN A 674 ? 1.9633 2.1520 1.8872 -0.5419 -0.3069 0.1986 674 ASN A N 5207 C CA . ASN A 674 ? 2.0234 2.0813 1.9002 -0.5798 -0.3342 0.1939 674 ASN A CA 5208 C C . ASN A 674 ? 1.9601 1.9708 1.8243 -0.5758 -0.3528 0.1706 674 ASN A C 5209 O O . ASN A 674 ? 1.9758 1.8659 1.8041 -0.5585 -0.3642 0.1525 674 ASN A O 5210 C CB . ASN A 674 ? 1.9996 1.9465 1.8485 -0.5485 -0.3309 0.1875 674 ASN A CB 5211 C CG . ASN A 674 ? 2.3002 2.1887 2.1108 -0.5986 -0.3432 0.2103 674 ASN A CG 5212 O OD1 . ASN A 674 ? 2.1761 2.1355 1.9917 -0.6503 -0.3432 0.2360 674 ASN A OD1 5213 N ND2 . ASN A 674 ? 2.7843 2.5473 2.5557 -0.5831 -0.3536 0.2030 674 ASN A ND2 5214 N N . GLN A 675 ? 1.8062 1.9188 1.6991 -0.5881 -0.3551 0.1716 675 GLN A N 5215 C CA . GLN A 675 ? 1.7784 1.8641 1.6585 -0.5868 -0.3734 0.1508 675 GLN A CA 5216 C C . GLN A 675 ? 1.8422 1.8666 1.7189 -0.5150 -0.3610 0.1241 675 GLN A C 5217 O O . GLN A 675 ? 1.9617 1.9103 1.8074 -0.5084 -0.3762 0.1041 675 GLN A O 5218 C CB . GLN A 675 ? 1.8274 1.8051 1.6503 -0.6487 -0.4084 0.1492 675 GLN A CB 5219 C CG . GLN A 675 ? 1.9157 1.9053 1.7255 -0.6654 -0.4266 0.1370 675 GLN A CG 5220 C CD . GLN A 675 ? 2.0770 1.9450 1.8186 -0.6998 -0.4463 0.1344 675 GLN A CD 5221 O OE1 . GLN A 675 ? 2.2562 2.0293 1.9583 -0.7093 -0.4479 0.1423 675 GLN A OE1 5222 N NE2 . GLN A 675 ? 1.9635 1.8321 1.6863 -0.7167 -0.4634 0.1237 675 GLN A NE2 5223 N N . THR A 676 ? 1.7594 1.8161 1.6642 -0.4629 -0.3336 0.1247 676 THR A N 5224 C CA . THR A 676 ? 1.6551 1.6646 1.5606 -0.4006 -0.3204 0.1041 676 THR A CA 5225 C C . THR A 676 ? 1.5539 1.6535 1.4966 -0.3525 -0.2954 0.1054 676 THR A C 5226 O O . THR A 676 ? 1.5597 1.7020 1.5179 -0.3416 -0.2792 0.1176 676 THR A O 5227 C CB . THR A 676 ? 1.6309 1.5391 1.5160 -0.3824 -0.3171 0.1002 676 THR A CB 5228 O OG1 . THR A 676 ? 1.7768 1.5847 1.6171 -0.4152 -0.3411 0.0961 676 THR A OG1 5229 C CG2 . THR A 676 ? 1.4922 1.3708 1.3856 -0.3233 -0.3022 0.0832 676 THR A CG2 5230 N N . ARG A 677 ? 1.5271 1.6476 1.4759 -0.3218 -0.2930 0.0925 677 ARG A N 5231 C CA . ARG A 677 ? 1.5343 1.7171 1.5059 -0.2703 -0.2712 0.0921 677 ARG A CA 5232 C C . ARG A 677 ? 1.4222 1.5260 1.3834 -0.2256 -0.2593 0.0785 677 ARG A C 5233 O O . ARG A 677 ? 1.3824 1.4134 1.3249 -0.2251 -0.2677 0.0659 677 ARG A O 5234 C CB . ARG A 677 ? 1.6000 1.8634 1.5831 -0.2636 -0.2764 0.0907 677 ARG A CB 5235 C CG . ARG A 677 ? 1.5463 1.7544 1.5058 -0.2680 -0.2930 0.0741 677 ARG A CG 5236 C CD . ARG A 677 ? 1.3660 1.6633 1.3349 -0.2801 -0.3066 0.0762 677 ARG A CD 5237 N NE . ARG A 677 ? 1.2978 1.6885 1.2922 -0.2342 -0.2890 0.0835 677 ARG A NE 5238 C CZ . ARG A 677 ? 1.3411 1.7232 1.3271 -0.1845 -0.2800 0.0747 677 ARG A CZ 5239 N NH1 . ARG A 677 ? 1.3561 1.6515 1.3139 -0.1759 -0.2847 0.0589 677 ARG A NH1 5240 N NH2 . ARG A 677 ? 1.2979 1.7567 1.2991 -0.1408 -0.2657 0.0826 677 ARG A NH2 5241 N N . GLN A 678 ? 1.3242 1.4440 1.2945 -0.1883 -0.2400 0.0815 678 GLN A N 5242 C CA . GLN A 678 ? 1.2330 1.2816 1.1954 -0.1560 -0.2300 0.0730 678 GLN A CA 5243 C C . GLN A 678 ? 1.1432 1.2119 1.1070 -0.1194 -0.2124 0.0768 678 GLN A C 5244 O O . GLN A 678 ? 1.1796 1.3151 1.1485 -0.1142 -0.2059 0.0855 678 GLN A O 5245 C CB . GLN A 678 ? 1.3460 1.3207 1.2996 -0.1766 -0.2377 0.0723 678 GLN A CB 5246 C CG . GLN A 678 ? 1.4118 1.4028 1.3659 -0.2009 -0.2388 0.0854 678 GLN A CG 5247 C CD . GLN A 678 ? 1.4400 1.3547 1.3800 -0.2205 -0.2499 0.0861 678 GLN A CD 5248 O OE1 . GLN A 678 ? 1.4688 1.3224 1.3991 -0.2162 -0.2578 0.0761 678 GLN A OE1 5249 N NE2 . GLN A 678 ? 1.4220 1.3411 1.3574 -0.2381 -0.2501 0.0986 678 GLN A NE2 5250 N N . VAL A 679 ? 1.1157 1.1256 1.0714 -0.0943 -0.2051 0.0705 679 VAL A N 5251 C CA . VAL A 679 ? 1.1131 1.1174 1.0576 -0.0613 -0.1921 0.0719 679 VAL A CA 5252 C C . VAL A 679 ? 1.1330 1.0789 1.0716 -0.0674 -0.1928 0.0719 679 VAL A C 5253 O O . VAL A 679 ? 1.2364 1.1328 1.1808 -0.0775 -0.1984 0.0684 679 VAL A O 5254 C CB . VAL A 679 ? 1.1154 1.0995 1.0484 -0.0287 -0.1847 0.0673 679 VAL A CB 5255 C CG1 . VAL A 679 ? 1.1400 1.0997 1.0489 0.0031 -0.1744 0.0685 679 VAL A CG1 5256 C CG2 . VAL A 679 ? 1.2014 1.2451 1.1375 -0.0194 -0.1862 0.0676 679 VAL A CG2 5257 N N . VAL A 680 ? 1.1149 1.0714 1.0405 -0.0585 -0.1874 0.0758 680 VAL A N 5258 C CA . VAL A 680 ? 1.1243 1.0277 1.0390 -0.0635 -0.1905 0.0755 680 VAL A CA 5259 C C . VAL A 680 ? 1.2065 1.0737 1.0930 -0.0326 -0.1837 0.0712 680 VAL A C 5260 O O . VAL A 680 ? 1.3669 1.2590 1.2335 -0.0030 -0.1743 0.0705 680 VAL A O 5261 C CB . VAL A 680 ? 1.1627 1.0908 1.0728 -0.0819 -0.1926 0.0833 680 VAL A CB 5262 C CG1 . VAL A 680 ? 1.2115 1.1470 1.1395 -0.1197 -0.2039 0.0889 680 VAL A CG1 5263 C CG2 . VAL A 680 ? 1.2922 1.2888 1.1912 -0.0621 -0.1803 0.0879 680 VAL A CG2 5264 N N . CYS A 681 ? 1.2115 1.0183 1.0932 -0.0395 -0.1901 0.0689 681 CYS A N 5265 C CA . CYS A 681 ? 1.2169 0.9730 1.0655 -0.0198 -0.1884 0.0652 681 CYS A CA 5266 C C . CYS A 681 ? 1.2863 0.9963 1.1236 -0.0359 -0.1997 0.0645 681 CYS A C 5267 O O . CYS A 681 ? 1.4659 1.1701 1.3312 -0.0603 -0.2093 0.0675 681 CYS A O 5268 C CB . CYS A 681 ? 1.1979 0.9271 1.0514 -0.0148 -0.1860 0.0652 681 CYS A CB 5269 S SG . CYS A 681 ? 1.7959 1.5731 1.6549 0.0074 -0.1754 0.0657 681 CYS A SG 5270 N N . ASP A 682 ? 1.2459 0.9211 1.0376 -0.0193 -0.2001 0.0601 682 ASP A N 5271 C CA . ASP A 682 ? 1.2720 0.9021 1.0451 -0.0350 -0.2140 0.0583 682 ASP A CA 5272 C C . ASP A 682 ? 1.2433 0.8190 1.0177 -0.0512 -0.2252 0.0586 682 ASP A C 5273 O O . ASP A 682 ? 1.2718 0.8045 1.0149 -0.0388 -0.2229 0.0562 682 ASP A O 5274 C CB . ASP A 682 ? 1.3656 0.9727 1.0790 -0.0099 -0.2114 0.0514 682 ASP A CB 5275 C CG . ASP A 682 ? 1.5555 1.2270 1.2717 -0.0027 -0.2016 0.0552 682 ASP A CG 5276 O OD1 . ASP A 682 ? 1.6172 1.3516 1.3749 -0.0113 -0.1944 0.0624 682 ASP A OD1 5277 O OD2 . ASP A 682 ? 1.6322 1.2909 1.3055 0.0094 -0.2017 0.0516 682 ASP A OD2 5278 N N . LEU A 683 ? 1.2391 0.8189 1.0485 -0.0793 -0.2377 0.0636 683 LEU A N 5279 C CA . LEU A 683 ? 1.2638 0.8118 1.0843 -0.1004 -0.2495 0.0675 683 LEU A CA 5280 C C . LEU A 683 ? 1.2853 0.7860 1.0699 -0.1145 -0.2688 0.0642 683 LEU A C 5281 O O . LEU A 683 ? 1.2802 0.7598 1.0741 -0.1396 -0.2837 0.0688 683 LEU A O 5282 C CB . LEU A 683 ? 1.2919 0.8819 1.1731 -0.1172 -0.2520 0.0755 683 LEU A CB 5283 C CG . LEU A 683 ? 1.1806 0.8086 1.0903 -0.1049 -0.2358 0.0768 683 LEU A CG 5284 C CD1 . LEU A 683 ? 1.1469 0.8033 1.1050 -0.1155 -0.2383 0.0832 683 LEU A CD1 5285 C CD2 . LEU A 683 ? 1.0963 0.7064 0.9841 -0.0906 -0.2235 0.0761 683 LEU A CD2 5286 N N . GLY A 684 ? 1.3075 0.7970 1.0502 -0.0993 -0.2689 0.0569 684 GLY A N 5287 C CA . GLY A 684 ? 1.3957 0.8357 1.0915 -0.1080 -0.2875 0.0510 684 GLY A CA 5288 C C . GLY A 684 ? 1.3649 0.8342 1.0763 -0.1198 -0.2979 0.0548 684 GLY A C 5289 O O . GLY A 684 ? 1.4218 0.9377 1.1879 -0.1313 -0.2980 0.0639 684 GLY A O 5290 N N . ASN A 685 ? 1.3686 0.8034 1.0237 -0.1142 -0.3071 0.0474 685 ASN A N 5291 C CA . ASN A 685 ? 1.2898 0.7462 0.9453 -0.1218 -0.3160 0.0519 685 ASN A CA 5292 C C . ASN A 685 ? 1.4940 0.8977 1.1019 -0.1356 -0.3425 0.0458 685 ASN A C 5293 O O . ASN A 685 ? 1.6962 1.0589 1.2336 -0.1177 -0.3423 0.0348 685 ASN A O 5294 C CB . ASN A 685 ? 1.2935 0.7826 0.9253 -0.0967 -0.2950 0.0518 685 ASN A CB 5295 C CG . ASN A 685 ? 1.3017 0.8166 0.9362 -0.1081 -0.3013 0.0612 685 ASN A CG 5296 O OD1 . ASN A 685 ? 1.3322 0.8474 0.9962 -0.1307 -0.3200 0.0687 685 ASN A OD1 5297 N ND2 . ASN A 685 ? 1.3842 0.9250 0.9868 -0.0911 -0.2852 0.0630 685 ASN A ND2 5298 N N . PRO A 686 ? 1.4401 0.8475 1.0837 -0.1656 -0.3661 0.0528 686 PRO A N 5299 C CA . PRO A 686 ? 1.2568 0.7143 0.9793 -0.1813 -0.3670 0.0656 686 PRO A CA 5300 C C . PRO A 686 ? 1.2072 0.6593 0.9546 -0.1891 -0.3611 0.0664 686 PRO A C 5301 O O . PRO A 686 ? 1.2422 0.6389 0.9427 -0.1906 -0.3640 0.0581 686 PRO A O 5302 C CB . PRO A 686 ? 1.2926 0.7552 1.0281 -0.2050 -0.3975 0.0721 686 PRO A CB 5303 C CG . PRO A 686 ? 1.4913 0.8893 1.1578 -0.2148 -0.4169 0.0604 686 PRO A CG 5304 C CD . PRO A 686 ? 1.5715 0.9344 1.1723 -0.1840 -0.3964 0.0479 686 PRO A CD 5305 N N . MET A 687 ? 1.1815 0.6853 0.9954 -0.1926 -0.3530 0.0767 687 MET A N 5306 C CA . MET A 687 ? 1.1234 0.6328 0.9672 -0.2048 -0.3488 0.0817 687 MET A CA 5307 C C . MET A 687 ? 1.2202 0.7498 1.0980 -0.2361 -0.3736 0.0918 687 MET A C 5308 O O . MET A 687 ? 1.3613 0.9452 1.2897 -0.2363 -0.3792 0.1011 687 MET A O 5309 C CB . MET A 687 ? 1.0908 0.6485 0.9832 -0.1886 -0.3256 0.0868 687 MET A CB 5310 C CG . MET A 687 ? 1.2870 0.8594 1.2116 -0.1989 -0.3181 0.0945 687 MET A CG 5311 S SD . MET A 687 ? 1.1378 0.7616 1.1079 -0.1757 -0.2922 0.0974 687 MET A SD 5312 C CE . MET A 687 ? 1.0460 0.6841 1.0430 -0.1908 -0.2846 0.1087 687 MET A CE 5313 N N . LYS A 688 ? 1.2464 0.7315 1.0933 -0.2624 -0.3898 0.0907 688 LYS A N 5314 C CA . LYS A 688 ? 1.2129 0.7182 1.0848 -0.2995 -0.4189 0.1006 688 LYS A CA 5315 C C . LYS A 688 ? 1.3217 0.9024 1.2720 -0.3136 -0.4128 0.1185 688 LYS A C 5316 O O . LYS A 688 ? 1.6044 1.2008 1.5754 -0.2996 -0.3870 0.1216 688 LYS A O 5317 C CB . LYS A 688 ? 1.2582 0.6824 1.0634 -0.3295 -0.4408 0.0938 688 LYS A CB 5318 C CG . LYS A 688 ? 1.3088 0.6579 1.0283 -0.3119 -0.4488 0.0750 688 LYS A CG 5319 C CD . LYS A 688 ? 1.4669 0.7213 1.1091 -0.3406 -0.4743 0.0660 688 LYS A CD 5320 C CE . LYS A 688 ? 1.5543 0.8314 1.2225 -0.3922 -0.5118 0.0767 688 LYS A CE 5321 N NZ . LYS A 688 ? 1.6832 0.8730 1.2727 -0.4174 -0.5316 0.0696 688 LYS A NZ 5322 N N . ALA A 689 ? 1.2975 0.9310 1.2904 -0.3388 -0.4367 0.1308 689 ALA A N 5323 C CA . ALA A 689 ? 1.3392 1.0620 1.4108 -0.3493 -0.4316 0.1500 689 ALA A CA 5324 C C . ALA A 689 ? 1.4198 1.1316 1.4925 -0.3775 -0.4214 0.1591 689 ALA A C 5325 O O . ALA A 689 ? 1.5284 1.1639 1.5436 -0.4070 -0.4346 0.1545 689 ALA A O 5326 C CB . ALA A 689 ? 1.3748 1.1598 1.4866 -0.3733 -0.4634 0.1624 689 ALA A CB 5327 N N . GLY A 690 ? 1.3711 1.1531 1.5022 -0.3669 -0.3980 0.1722 690 GLY A N 5328 C CA . GLY A 690 ? 1.4171 1.2012 1.5549 -0.3944 -0.3860 0.1859 690 GLY A CA 5329 C C . GLY A 690 ? 1.4763 1.1719 1.5511 -0.3798 -0.3658 0.1742 690 GLY A C 5330 O O . GLY A 690 ? 1.6245 1.2987 1.6869 -0.4032 -0.3578 0.1852 690 GLY A O 5331 N N . THR A 691 ? 1.3425 0.9908 1.3771 -0.3411 -0.3579 0.1542 691 THR A N 5332 C CA . THR A 691 ? 1.3388 0.9136 1.3149 -0.3197 -0.3397 0.1427 691 THR A CA 5333 C C . THR A 691 ? 1.3553 0.9717 1.3636 -0.2961 -0.3087 0.1491 691 THR A C 5334 O O . THR A 691 ? 1.4930 1.1706 1.5457 -0.2692 -0.2959 0.1480 691 THR A O 5335 C CB . THR A 691 ? 1.3263 0.8589 1.2572 -0.2851 -0.3389 0.1221 691 THR A CB 5336 O OG1 . THR A 691 ? 1.4089 0.8987 1.3009 -0.3038 -0.3671 0.1151 691 THR A OG1 5337 C CG2 . THR A 691 ? 1.4349 0.9044 1.3081 -0.2592 -0.3207 0.1118 691 THR A CG2 5338 N N . GLN A 692 ? 1.3455 0.9203 1.3234 -0.3059 -0.2982 0.1555 692 GLN A N 5339 C CA . GLN A 692 ? 1.2944 0.8979 1.2894 -0.2826 -0.2694 0.1610 692 GLN A CA 5340 C C . GLN A 692 ? 1.3588 0.8814 1.2844 -0.2607 -0.2594 0.1511 692 GLN A C 5341 O O . GLN A 692 ? 1.5741 1.0172 1.4421 -0.2802 -0.2704 0.1530 692 GLN A O 5342 C CB . GLN A 692 ? 1.4956 1.1483 1.5306 -0.3148 -0.2629 0.1856 692 GLN A CB 5343 C CG . GLN A 692 ? 1.5627 1.3137 1.6725 -0.3304 -0.2707 0.1980 692 GLN A CG 5344 C CD . GLN A 692 ? 1.4940 1.3109 1.6473 -0.3604 -0.2601 0.2252 692 GLN A CD 5345 O OE1 . GLN A 692 ? 1.3935 1.1855 1.5233 -0.3648 -0.2424 0.2348 692 GLN A OE1 5346 N NE2 . GLN A 692 ? 1.4708 1.3782 1.6878 -0.3803 -0.2705 0.2399 692 GLN A NE2 5347 N N . LEU A 693 ? 1.3702 0.9107 1.2973 -0.2196 -0.2403 0.1409 693 LEU A N 5348 C CA . LEU A 693 ? 1.4597 0.9400 1.3265 -0.1912 -0.2311 0.1316 693 LEU A CA 5349 C C . LEU A 693 ? 1.4369 0.9458 1.3142 -0.1683 -0.2076 0.1368 693 LEU A C 5350 O O . LEU A 693 ? 1.3351 0.9133 1.2639 -0.1609 -0.1965 0.1391 693 LEU A O 5351 C CB . LEU A 693 ? 1.3175 0.7899 1.1632 -0.1617 -0.2344 0.1125 693 LEU A CB 5352 C CG . LEU A 693 ? 1.3304 0.7587 1.1439 -0.1759 -0.2566 0.1044 693 LEU A CG 5353 C CD1 . LEU A 693 ? 1.3285 0.7591 1.1200 -0.1436 -0.2540 0.0885 693 LEU A CD1 5354 C CD2 . LEU A 693 ? 1.4532 0.7882 1.1990 -0.1926 -0.2688 0.1064 693 LEU A CD2 5355 N N . LEU A 694 ? 1.4741 0.9234 1.2951 -0.1540 -0.2015 0.1380 694 LEU A N 5356 C CA . LEU A 694 ? 1.5920 1.0598 1.4106 -0.1289 -0.1815 0.1424 694 LEU A CA 5357 C C . LEU A 694 ? 1.6785 1.1052 1.4416 -0.0881 -0.1784 0.1304 694 LEU A C 5358 O O . LEU A 694 ? 1.9478 1.2951 1.6480 -0.0833 -0.1866 0.1291 694 LEU A O 5359 C CB . LEU A 694 ? 1.7353 1.1806 1.5425 -0.1543 -0.1751 0.1646 694 LEU A CB 5360 C CG . LEU A 694 ? 1.6401 1.1616 1.5125 -0.1814 -0.1667 0.1808 694 LEU A CG 5361 C CD1 . LEU A 694 ? 1.6791 1.1722 1.5327 -0.2164 -0.1629 0.2066 694 LEU A CD1 5362 C CD2 . LEU A 694 ? 1.4461 1.0378 1.3542 -0.1492 -0.1477 0.1752 694 LEU A CD2 5363 N N . ALA A 695 ? 1.4569 0.9383 1.2409 -0.0579 -0.1678 0.1215 695 ALA A N 5364 C CA . ALA A 695 ? 1.4675 0.9351 1.2098 -0.0171 -0.1639 0.1124 695 ALA A CA 5365 C C . ALA A 695 ? 1.4081 0.9363 1.1737 0.0046 -0.1512 0.1115 695 ALA A C 5366 O O . ALA A 695 ? 1.3754 0.9607 1.1906 -0.0064 -0.1484 0.1092 695 ALA A O 5367 C CB . ALA A 695 ? 1.4614 0.9368 1.1984 -0.0050 -0.1722 0.0976 695 ALA A CB 5368 N N . GLY A 696 ? 1.4582 0.9693 1.1822 0.0374 -0.1456 0.1130 696 GLY A N 5369 C CA . GLY A 696 ? 1.4827 1.0502 1.2218 0.0584 -0.1372 0.1116 696 GLY A CA 5370 C C . GLY A 696 ? 1.3775 0.9992 1.1264 0.0818 -0.1406 0.0985 696 GLY A C 5371 O O . GLY A 696 ? 1.3016 0.9097 1.0282 0.0968 -0.1452 0.0929 696 GLY A O 5372 N N . LEU A 697 ? 1.3820 1.0666 1.1612 0.0837 -0.1387 0.0943 697 LEU A N 5373 C CA . LEU A 697 ? 1.3686 1.1158 1.1612 0.0974 -0.1435 0.0852 697 LEU A CA 5374 C C . LEU A 697 ? 1.3923 1.1813 1.1786 0.1184 -0.1420 0.0860 697 LEU A C 5375 O O . LEU A 697 ? 1.3429 1.1457 1.1444 0.1059 -0.1408 0.0853 697 LEU A O 5376 C CB . LEU A 697 ? 1.2055 0.9885 1.0429 0.0667 -0.1499 0.0774 697 LEU A CB 5377 C CG . LEU A 697 ? 1.1863 0.9405 1.0307 0.0480 -0.1544 0.0761 697 LEU A CG 5378 C CD1 . LEU A 697 ? 1.1392 0.9243 1.0220 0.0209 -0.1616 0.0706 697 LEU A CD1 5379 C CD2 . LEU A 697 ? 1.2131 0.9616 1.0271 0.0706 -0.1549 0.0745 697 LEU A CD2 5380 N N . ARG A 698 ? 1.3810 1.1921 1.1418 0.1536 -0.1427 0.0873 698 ARG A N 5381 C CA . ARG A 698 ? 1.3907 1.2469 1.1428 0.1769 -0.1442 0.0893 698 ARG A CA 5382 C C . ARG A 698 ? 1.4020 1.3491 1.1906 0.1664 -0.1540 0.0817 698 ARG A C 5383 O O . ARG A 698 ? 1.4364 1.4228 1.2424 0.1628 -0.1569 0.0790 698 ARG A O 5384 C CB . ARG A 698 ? 1.4300 1.2658 1.1320 0.2260 -0.1413 0.0969 698 ARG A CB 5385 C CG . ARG A 698 ? 1.5581 1.3072 1.2128 0.2359 -0.1345 0.1083 698 ARG A CG 5386 C CD . ARG A 698 ? 1.6339 1.3630 1.2316 0.2901 -0.1343 0.1163 698 ARG A CD 5387 N NE . ARG A 698 ? 1.6198 1.2904 1.1763 0.3148 -0.1337 0.1157 698 ARG A NE 5388 C CZ . ARG A 698 ? 1.5986 1.1578 1.0971 0.3190 -0.1317 0.1237 698 ARG A CZ 5389 N NH1 . ARG A 698 ? 1.5870 1.0924 1.0690 0.2974 -0.1280 0.1363 698 ARG A NH1 5390 N NH2 . ARG A 698 ? 1.6400 1.1395 1.0925 0.3432 -0.1338 0.1199 698 ARG A NH2 5391 N N . PHE A 699 ? 1.4627 1.4412 1.2588 0.1587 -0.1597 0.0791 699 PHE A N 5392 C CA . PHE A 699 ? 1.4819 1.5413 1.3057 0.1423 -0.1734 0.0728 699 PHE A CA 5393 C C . PHE A 699 ? 1.4341 1.5376 1.2409 0.1650 -0.1807 0.0749 699 PHE A C 5394 O O . PHE A 699 ? 1.4751 1.5419 1.2468 0.1954 -0.1736 0.0817 699 PHE A O 5395 C CB . PHE A 699 ? 1.5227 1.5687 1.3706 0.0980 -0.1801 0.0631 699 PHE A CB 5396 C CG . PHE A 699 ? 1.4335 1.4387 1.2982 0.0762 -0.1753 0.0619 699 PHE A CG 5397 C CD1 . PHE A 699 ? 1.3874 1.4279 1.2745 0.0570 -0.1814 0.0611 699 PHE A CD1 5398 C CD2 . PHE A 699 ? 1.4824 1.4204 1.3408 0.0734 -0.1653 0.0636 699 PHE A CD2 5399 C CE1 . PHE A 699 ? 1.5665 1.5682 1.4646 0.0385 -0.1786 0.0606 699 PHE A CE1 5400 C CE2 . PHE A 699 ? 1.5783 1.4852 1.4529 0.0537 -0.1639 0.0630 699 PHE A CE2 5401 C CZ . PHE A 699 ? 1.6540 1.5891 1.5462 0.0378 -0.1711 0.0608 699 PHE A CZ 5402 N N . SER A 700 ? 1.3585 1.5398 1.1876 0.1470 -0.1966 0.0703 700 SER A N 5403 C CA . SER A 700 ? 1.4501 1.6801 1.2656 0.1606 -0.2090 0.0705 700 SER A CA 5404 C C . SER A 700 ? 1.4477 1.7006 1.2775 0.1148 -0.2279 0.0587 700 SER A C 5405 O O . SER A 700 ? 1.4671 1.7669 1.3268 0.0804 -0.2394 0.0564 700 SER A O 5406 C CB . SER A 700 ? 1.5256 1.8466 1.3467 0.1942 -0.2141 0.0799 700 SER A CB 5407 O OG . SER A 700 ? 1.5827 1.9497 1.3870 0.2130 -0.2271 0.0819 700 SER A OG 5408 N N . VAL A 701 ? 1.4319 1.6457 1.2339 0.1138 -0.2313 0.0516 701 VAL A N 5409 C CA . VAL A 701 ? 1.4618 1.6765 1.2612 0.0746 -0.2509 0.0373 701 VAL A CA 5410 C C . VAL A 701 ? 1.5892 1.8644 1.3705 0.0809 -0.2716 0.0356 701 VAL A C 5411 O O . VAL A 701 ? 1.5981 1.8693 1.3500 0.1191 -0.2659 0.0411 701 VAL A O 5412 C CB . VAL A 701 ? 1.4813 1.6061 1.2566 0.0692 -0.2408 0.0273 701 VAL A CB 5413 C CG1 . VAL A 701 ? 1.6117 1.7212 1.3741 0.0319 -0.2624 0.0098 701 VAL A CG1 5414 C CG2 . VAL A 701 ? 1.4629 1.5359 1.2578 0.0665 -0.2212 0.0315 701 VAL A CG2 5415 N N . HIS A 702 ? 1.6648 1.9953 1.4608 0.0407 -0.2976 0.0293 702 HIS A N 5416 C CA . HIS A 702 ? 1.7836 2.1774 1.5634 0.0388 -0.3228 0.0269 702 HIS A CA 5417 C C . HIS A 702 ? 1.7331 2.0690 1.4747 0.0051 -0.3424 0.0069 702 HIS A C 5418 O O . HIS A 702 ? 1.6905 1.9761 1.3878 0.0296 -0.3380 -0.0005 702 HIS A O 5419 C CB . HIS A 702 ? 1.8698 2.3835 1.6919 0.0154 -0.3421 0.0367 702 HIS A CB 5420 C CG . HIS A 702 ? 1.8262 2.3884 1.6856 0.0422 -0.3215 0.0531 702 HIS A CG 5421 N ND1 . HIS A 702 ? 1.7947 2.3212 1.6402 0.0995 -0.2956 0.0613 702 HIS A ND1 5422 C CD2 . HIS A 702 ? 1.7568 2.3958 1.6603 0.0196 -0.3232 0.0629 702 HIS A CD2 5423 C CE1 . HIS A 702 ? 1.7357 2.3090 1.6108 0.1147 -0.2832 0.0726 702 HIS A CE1 5424 N NE2 . HIS A 702 ? 1.6897 2.3373 1.6024 0.0686 -0.2979 0.0743 702 HIS A NE2 5425 N N . GLN A 703 ? 1.7459 2.0816 1.4985 -0.0501 -0.3631 -0.0013 703 GLN A N 5426 C CA . GLN A 703 ? 1.8404 2.1052 1.5477 -0.0856 -0.3853 -0.0226 703 GLN A CA 5427 C C . GLN A 703 ? 1.9008 2.1746 1.6237 -0.1509 -0.4102 -0.0252 703 GLN A C 5428 O O . GLN A 703 ? 1.9559 2.3185 1.7275 -0.1716 -0.4140 -0.0089 703 GLN A O 5429 C CB . GLN A 703 ? 1.9042 2.1916 1.5682 -0.0787 -0.4088 -0.0316 703 GLN A CB 5430 C CG . GLN A 703 ? 1.8860 2.3011 1.5789 -0.0965 -0.4356 -0.0200 703 GLN A CG 5431 C CD . GLN A 703 ? 1.9426 2.3792 1.5894 -0.0881 -0.4612 -0.0289 703 GLN A CD 5432 O OE1 . GLN A 703 ? 1.9816 2.3306 1.5687 -0.0721 -0.4595 -0.0457 703 GLN A OE1 5433 N NE2 . GLN A 703 ? 1.9598 2.5197 1.6333 -0.0969 -0.4851 -0.0170 703 GLN A NE2 5434 N N . GLN A 704 ? 1.9089 2.0875 1.5850 -0.1816 -0.4266 -0.0448 704 GLN A N 5435 C CA . GLN A 704 ? 1.9245 2.0937 1.5952 -0.2504 -0.4583 -0.0486 704 GLN A CA 5436 C C . GLN A 704 ? 1.9284 2.0346 1.5268 -0.2753 -0.4928 -0.0721 704 GLN A C 5437 O O . GLN A 704 ? 1.9346 1.9295 1.4765 -0.2528 -0.4867 -0.0921 704 GLN A O 5438 C CB . GLN A 704 ? 1.9545 2.0418 1.6298 -0.2662 -0.4455 -0.0490 704 GLN A CB 5439 C CG . GLN A 704 ? 2.0995 2.1704 1.7658 -0.3402 -0.4774 -0.0484 704 GLN A CG 5440 C CD . GLN A 704 ? 2.1309 2.0736 1.7641 -0.3506 -0.4739 -0.0582 704 GLN A CD 5441 O OE1 . GLN A 704 ? 2.1316 1.9914 1.7368 -0.3044 -0.4542 -0.0715 704 GLN A OE1 5442 N NE2 . GLN A 704 ? 2.1117 2.0415 1.7472 -0.4110 -0.4932 -0.0496 704 GLN A NE2 5443 N N . SER A 705 ? 1.9377 2.1178 1.5362 -0.3213 -0.5295 -0.0696 705 SER A N 5444 C CA . SER A 705 ? 2.0733 2.2072 1.5995 -0.3428 -0.5664 -0.0919 705 SER A CA 5445 C C . SER A 705 ? 2.1611 2.2626 1.6482 -0.2734 -0.5469 -0.1038 705 SER A C 5446 O O . SER A 705 ? 2.1440 2.3284 1.6694 -0.2269 -0.5249 -0.0882 705 SER A O 5447 C CB . SER A 705 ? 2.1003 2.0947 1.5593 -0.3889 -0.5902 -0.1131 705 SER A CB 5448 O OG . SER A 705 ? 2.1732 2.1119 1.5512 -0.4091 -0.6282 -0.1373 705 SER A OG 5449 N N . GLU A 706 ? 2.1691 2.1469 1.5752 -0.2642 -0.5539 -0.1306 706 GLU A N 5450 C CA . GLU A 706 ? 2.0267 1.9662 1.3919 -0.1977 -0.5297 -0.1405 706 GLU A CA 5451 C C . GLU A 706 ? 2.0925 1.8935 1.4002 -0.1739 -0.5128 -0.1614 706 GLU A C 5452 O O . GLU A 706 ? 2.0997 1.8260 1.3917 -0.2083 -0.5246 -0.1702 706 GLU A O 5453 C CB . GLU A 706 ? 2.0166 1.9810 1.3269 -0.1995 -0.5618 -0.1529 706 GLU A CB 5454 C CG . GLU A 706 ? 1.9267 2.0403 1.2929 -0.1983 -0.5709 -0.1301 706 GLU A CG 5455 C CD . GLU A 706 ? 2.1448 2.2844 1.4542 -0.2013 -0.6067 -0.1422 706 GLU A CD 5456 O OE1 . GLU A 706 ? 2.4038 2.4383 1.6248 -0.2013 -0.6218 -0.1698 706 GLU A OE1 5457 O OE2 . GLU A 706 ? 2.0927 2.3584 1.4423 -0.2004 -0.6202 -0.1245 706 GLU A OE2 5458 N N . MET A 707 ? 2.1800 1.9514 1.4546 -0.1136 -0.4853 -0.1675 707 MET A N 5459 C CA . MET A 707 ? 2.1999 1.8616 1.4233 -0.0759 -0.4622 -0.1847 707 MET A CA 5460 C C . MET A 707 ? 2.1477 1.7628 1.4071 -0.0844 -0.4456 -0.1799 707 MET A C 5461 O O . MET A 707 ? 2.3281 1.8432 1.5358 -0.0996 -0.4611 -0.1993 707 MET A O 5462 C CB . MET A 707 ? 2.2332 1.7962 1.3483 -0.0837 -0.4944 -0.2185 707 MET A CB 5463 C CG . MET A 707 ? 2.2164 1.7299 1.2962 -0.1543 -0.5449 -0.2332 707 MET A CG 5464 S SD . MET A 707 ? 2.8368 2.2340 1.7763 -0.1619 -0.5877 -0.2740 707 MET A SD 5465 C CE . MET A 707 ? 2.1116 1.6292 1.0588 -0.1590 -0.6034 -0.2655 707 MET A CE 5466 N N . ASP A 708 ? 1.9468 1.6286 1.2883 -0.0718 -0.4153 -0.1541 708 ASP A N 5467 C CA . ASP A 708 ? 1.9339 1.5819 1.3137 -0.0756 -0.3978 -0.1468 708 ASP A CA 5468 C C . ASP A 708 ? 1.9221 1.5374 1.3029 -0.0191 -0.3569 -0.1452 708 ASP A C 5469 O O . ASP A 708 ? 1.9685 1.5636 1.3841 -0.0147 -0.3395 -0.1377 708 ASP A O 5470 C CB . ASP A 708 ? 1.8917 1.6290 1.3567 -0.0994 -0.3918 -0.1205 708 ASP A CB 5471 C CG . ASP A 708 ? 1.8709 1.6422 1.3436 -0.1627 -0.4301 -0.1188 708 ASP A CG 5472 O OD1 . ASP A 708 ? 1.8166 1.5808 1.2402 -0.1867 -0.4627 -0.1330 708 ASP A OD1 5473 O OD2 . ASP A 708 ? 1.8757 1.6837 1.4022 -0.1906 -0.4281 -0.1024 708 ASP A OD2 5474 N N . THR A 709 ? 1.8935 1.5102 1.2366 0.0220 -0.3422 -0.1504 709 THR A N 5475 C CA . THR A 709 ? 1.9342 1.5442 1.2843 0.0734 -0.3006 -0.1431 709 THR A CA 5476 C C . THR A 709 ? 1.9393 1.6149 1.3741 0.0756 -0.2740 -0.1137 709 THR A C 5477 O O . THR A 709 ? 2.0796 1.8211 1.5441 0.0729 -0.2725 -0.0972 709 THR A O 5478 C CB . THR A 709 ? 2.0799 1.6037 1.3930 0.0933 -0.2935 -0.1604 709 THR A CB 5479 O OG1 . THR A 709 ? 2.3448 1.7886 1.5770 0.0761 -0.3293 -0.1894 709 THR A OG1 5480 C CG2 . THR A 709 ? 2.0460 1.5709 1.3425 0.1503 -0.2551 -0.1578 709 THR A CG2 5481 N N . SER A 710 ? 1.7806 1.4350 1.2489 0.0827 -0.2549 -0.1077 710 SER A N 5482 C CA . SER A 710 ? 1.7072 1.4118 1.2478 0.0824 -0.2325 -0.0821 710 SER A CA 5483 C C . SER A 710 ? 1.6318 1.3532 1.2155 0.0413 -0.2511 -0.0762 710 SER A C 5484 O O . SER A 710 ? 1.6500 1.3481 1.2114 0.0088 -0.2810 -0.0892 710 SER A O 5485 C CB . SER A 710 ? 1.7288 1.4142 1.2869 0.1101 -0.2026 -0.0760 710 SER A CB 5486 O OG . SER A 710 ? 1.7778 1.4019 1.3138 0.1081 -0.2137 -0.0931 710 SER A OG 5487 N N . VAL A 711 ? 1.5693 1.3294 1.2104 0.0411 -0.2338 -0.0556 711 VAL A N 5488 C CA . VAL A 711 ? 1.5589 1.3391 1.2411 0.0079 -0.2457 -0.0479 711 VAL A CA 5489 C C . VAL A 711 ? 1.7059 1.4688 1.4253 0.0135 -0.2272 -0.0382 711 VAL A C 5490 O O . VAL A 711 ? 1.7409 1.5122 1.4763 0.0390 -0.2023 -0.0273 711 VAL A O 5491 C CB . VAL A 711 ? 1.4293 1.2825 1.1405 0.0028 -0.2474 -0.0327 711 VAL A CB 5492 C CG1 . VAL A 711 ? 1.3877 1.2603 1.1126 0.0369 -0.2198 -0.0166 711 VAL A CG1 5493 C CG2 . VAL A 711 ? 1.4777 1.3587 1.2290 -0.0280 -0.2566 -0.0241 711 VAL A CG2 5494 N N . LYS A 712 ? 1.6937 1.4328 1.4245 -0.0132 -0.2411 -0.0406 712 LYS A N 5495 C CA . LYS A 712 ? 1.6712 1.3864 1.4287 -0.0074 -0.2288 -0.0342 712 LYS A CA 5496 C C . LYS A 712 ? 1.6147 1.3626 1.4178 -0.0278 -0.2279 -0.0186 712 LYS A C 5497 O O . LYS A 712 ? 1.5596 1.3221 1.3662 -0.0585 -0.2453 -0.0175 712 LYS A O 5498 C CB . LYS A 712 ? 1.7262 1.3712 1.4492 -0.0132 -0.2444 -0.0495 712 LYS A CB 5499 C CG . LYS A 712 ? 1.7185 1.3402 1.4664 -0.0058 -0.2363 -0.0429 712 LYS A CG 5500 C CD . LYS A 712 ? 1.8053 1.3475 1.5078 -0.0064 -0.2542 -0.0581 712 LYS A CD 5501 C CE . LYS A 712 ? 1.8147 1.3379 1.5417 0.0035 -0.2489 -0.0499 712 LYS A CE 5502 N NZ . LYS A 712 ? 1.8736 1.3087 1.5476 0.0093 -0.2673 -0.0640 712 LYS A NZ 5503 N N . PHE A 713 ? 1.5402 1.3005 1.3750 -0.0120 -0.2078 -0.0059 713 PHE A N 5504 C CA . PHE A 713 ? 1.3797 1.1588 1.2492 -0.0265 -0.2064 0.0068 713 PHE A CA 5505 C C . PHE A 713 ? 1.4170 1.1621 1.3002 -0.0283 -0.2060 0.0082 713 PHE A C 5506 O O . PHE A 713 ? 1.5827 1.3074 1.4622 -0.0076 -0.1972 0.0052 713 PHE A O 5507 C CB . PHE A 713 ? 1.3442 1.1545 1.2315 -0.0106 -0.1887 0.0202 713 PHE A CB 5508 C CG . PHE A 713 ? 1.4044 1.2531 1.2805 -0.0057 -0.1910 0.0222 713 PHE A CG 5509 C CD1 . PHE A 713 ? 1.6703 1.5244 1.5198 0.0096 -0.1900 0.0168 713 PHE A CD1 5510 C CD2 . PHE A 713 ? 1.3192 1.2021 1.2089 -0.0118 -0.1937 0.0300 713 PHE A CD2 5511 C CE1 . PHE A 713 ? 1.7296 1.6239 1.5688 0.0174 -0.1940 0.0200 713 PHE A CE1 5512 C CE2 . PHE A 713 ? 1.4013 1.3280 1.2819 -0.0003 -0.1958 0.0330 713 PHE A CE2 5513 C CZ . PHE A 713 ? 1.5602 1.4933 1.4169 0.0138 -0.1970 0.0284 713 PHE A CZ 5514 N N . ASP A 714 ? 1.3217 1.0666 1.2201 -0.0503 -0.2152 0.0140 714 ASP A N 5515 C CA . ASP A 714 ? 1.2957 1.0100 1.2054 -0.0517 -0.2177 0.0169 714 ASP A CA 5516 C C . ASP A 714 ? 1.2095 0.9457 1.1497 -0.0564 -0.2110 0.0302 714 ASP A C 5517 O O . ASP A 714 ? 1.1686 0.9264 1.1126 -0.0724 -0.2147 0.0353 714 ASP A O 5518 C CB . ASP A 714 ? 1.3927 1.0672 1.2789 -0.0755 -0.2389 0.0114 714 ASP A CB 5519 C CG . ASP A 714 ? 1.6418 1.2718 1.4853 -0.0699 -0.2494 -0.0045 714 ASP A CG 5520 O OD1 . ASP A 714 ? 1.8528 1.4883 1.6743 -0.0898 -0.2614 -0.0105 714 ASP A OD1 5521 O OD2 . ASP A 714 ? 1.5984 1.1895 1.4280 -0.0442 -0.2466 -0.0111 714 ASP A OD2 5522 N N . LEU A 715 ? 1.2791 1.0124 1.2388 -0.0424 -0.2018 0.0360 715 LEU A N 5523 C CA . LEU A 715 ? 1.1921 0.9377 1.1743 -0.0486 -0.1983 0.0472 715 LEU A CA 5524 C C . LEU A 715 ? 1.1609 0.8894 1.1570 -0.0523 -0.2070 0.0511 715 LEU A C 5525 O O . LEU A 715 ? 1.1484 0.8707 1.1518 -0.0367 -0.2056 0.0501 715 LEU A O 5526 C CB . LEU A 715 ? 1.1222 0.8851 1.1157 -0.0363 -0.1823 0.0547 715 LEU A CB 5527 C CG . LEU A 715 ? 1.1112 0.8875 1.0868 -0.0272 -0.1731 0.0534 715 LEU A CG 5528 C CD1 . LEU A 715 ? 1.1152 0.8959 1.0957 -0.0200 -0.1588 0.0648 715 LEU A CD1 5529 C CD2 . LEU A 715 ? 1.0865 0.8737 1.0501 -0.0353 -0.1797 0.0522 715 LEU A CD2 5530 N N . GLN A 716 ? 1.1642 0.8889 1.1618 -0.0692 -0.2158 0.0562 716 GLN A N 5531 C CA . GLN A 716 ? 1.1887 0.8986 1.1968 -0.0728 -0.2263 0.0616 716 GLN A CA 5532 C C . GLN A 716 ? 1.2301 0.9456 1.2417 -0.0867 -0.2298 0.0690 716 GLN A C 5533 O O . GLN A 716 ? 1.3556 1.0782 1.3524 -0.0955 -0.2280 0.0685 716 GLN A O 5534 C CB . GLN A 716 ? 1.2064 0.8815 1.1929 -0.0792 -0.2409 0.0579 716 GLN A CB 5535 C CG . GLN A 716 ? 1.2307 0.8854 1.2230 -0.0748 -0.2528 0.0640 716 GLN A CG 5536 C CD . GLN A 716 ? 1.2973 0.9083 1.2586 -0.0901 -0.2693 0.0651 716 GLN A CD 5537 O OE1 . GLN A 716 ? 1.3134 0.9208 1.2554 -0.1131 -0.2718 0.0646 716 GLN A OE1 5538 N NE2 . GLN A 716 ? 1.3204 0.9008 1.2760 -0.0779 -0.2813 0.0687 716 GLN A NE2 5539 N N . ILE A 717 ? 1.0955 0.8110 1.1244 -0.0867 -0.2356 0.0755 717 ILE A N 5540 C CA . ILE A 717 ? 0.9969 0.7077 1.0210 -0.1000 -0.2433 0.0807 717 ILE A CA 5541 C C . ILE A 717 ? 1.0231 0.7156 1.0389 -0.1071 -0.2591 0.0842 717 ILE A C 5542 O O . ILE A 717 ? 1.2530 0.9385 1.2791 -0.0978 -0.2667 0.0861 717 ILE A O 5543 C CB . ILE A 717 ? 0.9673 0.6889 1.0117 -0.1024 -0.2439 0.0871 717 ILE A CB 5544 C CG1 . ILE A 717 ? 0.9780 0.7106 1.0260 -0.0973 -0.2281 0.0872 717 ILE A CG1 5545 C CG2 . ILE A 717 ? 0.9618 0.6672 0.9893 -0.1169 -0.2548 0.0895 717 ILE A CG2 5546 C CD1 . ILE A 717 ? 1.1000 0.8441 1.1680 -0.1073 -0.2290 0.0969 717 ILE A CD1 5547 N N . GLN A 718 ? 0.9784 0.6629 0.9715 -0.1202 -0.2634 0.0860 718 GLN A N 5548 C CA . GLN A 718 ? 1.0022 0.6665 0.9811 -0.1293 -0.2782 0.0922 718 GLN A CA 5549 C C . GLN A 718 ? 1.1527 0.8148 1.1136 -0.1388 -0.2836 0.0960 718 GLN A C 5550 O O . GLN A 718 ? 1.1931 0.8649 1.1415 -0.1384 -0.2741 0.0922 718 GLN A O 5551 C CB . GLN A 718 ? 1.0204 0.6718 0.9780 -0.1399 -0.2788 0.0926 718 GLN A CB 5552 C CG . GLN A 718 ? 1.1071 0.7848 1.0517 -0.1507 -0.2676 0.0916 718 GLN A CG 5553 C CD . GLN A 718 ? 1.2073 0.8811 1.1369 -0.1686 -0.2703 0.0937 718 GLN A CD 5554 O OE1 . GLN A 718 ? 1.2201 0.8652 1.1469 -0.1675 -0.2771 0.0900 718 GLN A OE1 5555 N NE2 . GLN A 718 ? 1.2435 0.9467 1.1602 -0.1856 -0.2657 0.1000 718 GLN A NE2 5556 N N . SER A 719 ? 1.2502 0.8957 1.2040 -0.1433 -0.2996 0.1032 719 SER A N 5557 C CA . SER A 719 ? 1.2115 0.8502 1.1422 -0.1511 -0.3078 0.1061 719 SER A CA 5558 C C . SER A 719 ? 1.2009 0.8198 1.1059 -0.1601 -0.3200 0.1162 719 SER A C 5559 O O . SER A 719 ? 1.2196 0.8219 1.1252 -0.1603 -0.3254 0.1216 719 SER A O 5560 C CB . SER A 719 ? 1.2247 0.8659 1.1730 -0.1497 -0.3198 0.1060 719 SER A CB 5561 O OG . SER A 719 ? 1.2556 0.9029 1.2313 -0.1427 -0.3325 0.1123 719 SER A OG 5562 N N . SER A 720 ? 1.2126 0.8259 1.0873 -0.1665 -0.3249 0.1190 720 SER A N 5563 C CA . SER A 720 ? 1.2038 0.7993 1.0463 -0.1768 -0.3343 0.1310 720 SER A CA 5564 C C . SER A 720 ? 1.2101 0.7853 1.0531 -0.1730 -0.3584 0.1381 720 SER A C 5565 O O . SER A 720 ? 1.2601 0.8148 1.0710 -0.1796 -0.3694 0.1495 720 SER A O 5566 C CB . SER A 720 ? 1.2406 0.8456 1.0441 -0.1816 -0.3255 0.1313 720 SER A CB 5567 O OG . SER A 720 ? 1.2933 0.8882 1.0823 -0.1749 -0.3348 0.1239 720 SER A OG 5568 N N . ASN A 721 ? 1.1867 0.7732 1.0659 -0.1624 -0.3667 0.1334 721 ASN A N 5569 C CA . ASN A 721 ? 1.3437 0.9273 1.2322 -0.1556 -0.3907 0.1412 721 ASN A CA 5570 C C . ASN A 721 ? 1.5384 1.0956 1.4191 -0.1454 -0.3993 0.1521 721 ASN A C 5571 O O . ASN A 721 ? 1.6815 1.2233 1.5601 -0.1442 -0.3875 0.1508 721 ASN A O 5572 C CB . ASN A 721 ? 1.2462 0.8641 1.1832 -0.1482 -0.3950 0.1368 721 ASN A CB 5573 C CG . ASN A 721 ? 1.3012 0.9282 1.2357 -0.1621 -0.3919 0.1278 721 ASN A CG 5574 O OD1 . ASN A 721 ? 1.5336 1.1453 1.4385 -0.1675 -0.3770 0.1202 721 ASN A OD1 5575 N ND2 . ASN A 721 ? 1.1766 0.8282 1.1392 -0.1678 -0.4071 0.1294 721 ASN A ND2 5576 N N . LEU A 722 ? 1.4780 1.0243 1.3482 -0.1380 -0.4224 0.1627 722 LEU A N 5577 C CA . LEU A 722 ? 1.3801 0.8864 1.2294 -0.1247 -0.4339 0.1746 722 LEU A CA 5578 C C . LEU A 722 ? 1.3892 0.9049 1.2749 -0.0953 -0.4348 0.1715 722 LEU A C 5579 O O . LEU A 722 ? 1.6129 1.0831 1.4765 -0.0819 -0.4364 0.1750 722 LEU A O 5580 C CB . LEU A 722 ? 1.4656 0.9560 1.2860 -0.1214 -0.4594 0.1884 722 LEU A CB 5581 C CG . LEU A 722 ? 1.6332 1.1053 1.4028 -0.1454 -0.4596 0.1945 722 LEU A CG 5582 C CD1 . LEU A 722 ? 1.8559 1.3632 1.6326 -0.1557 -0.4603 0.1837 722 LEU A CD1 5583 C CD2 . LEU A 722 ? 1.5262 0.9582 1.2515 -0.1398 -0.4826 0.2132 722 LEU A CD2 5584 N N . PHE A 723 ? 1.3353 0.9078 1.2719 -0.0857 -0.4339 0.1655 723 PHE A N 5585 C CA . PHE A 723 ? 1.3328 0.9309 1.3077 -0.0540 -0.4319 0.1639 723 PHE A CA 5586 C C . PHE A 723 ? 1.2805 0.9302 1.3012 -0.0590 -0.4120 0.1534 723 PHE A C 5587 O O . PHE A 723 ? 1.2472 0.9240 1.2805 -0.0833 -0.4096 0.1504 723 PHE A O 5588 C CB . PHE A 723 ? 1.3504 0.9821 1.3469 -0.0296 -0.4561 0.1755 723 PHE A CB 5589 C CG . PHE A 723 ? 1.4450 1.0209 1.3923 -0.0175 -0.4772 0.1879 723 PHE A CG 5590 C CD1 . PHE A 723 ? 1.6238 1.1467 1.5429 0.0150 -0.4803 0.1914 723 PHE A CD1 5591 C CD2 . PHE A 723 ? 1.4081 0.9758 1.3286 -0.0377 -0.4949 0.1963 723 PHE A CD2 5592 C CE1 . PHE A 723 ? 1.7689 1.2290 1.6345 0.0255 -0.5010 0.2051 723 PHE A CE1 5593 C CE2 . PHE A 723 ? 1.4952 1.0091 1.3656 -0.0271 -0.5143 0.2103 723 PHE A CE2 5594 C CZ . PHE A 723 ? 1.7462 1.2047 1.5893 0.0037 -0.5175 0.2158 723 PHE A CZ 5595 N N . ASP A 724 ? 1.2901 0.9452 1.3275 -0.0347 -0.3986 0.1481 724 ASP A N 5596 C CA . ASP A 724 ? 1.2712 0.9719 1.3469 -0.0363 -0.3778 0.1402 724 ASP A CA 5597 C C . ASP A 724 ? 1.2359 0.9217 1.2952 -0.0686 -0.3631 0.1317 724 ASP A C 5598 O O . ASP A 724 ? 1.1691 0.8899 1.2531 -0.0822 -0.3536 0.1290 724 ASP A O 5599 C CB . ASP A 724 ? 1.3625 1.1404 1.4925 -0.0350 -0.3841 0.1481 724 ASP A CB 5600 C CG . ASP A 724 ? 1.5117 1.3211 1.6625 0.0014 -0.4001 0.1588 724 ASP A CG 5601 O OD1 . ASP A 724 ? 1.6674 1.5560 1.8716 0.0120 -0.3991 0.1660 724 ASP A OD1 5602 O OD2 . ASP A 724 ? 1.3778 1.1351 1.4903 0.0199 -0.4139 0.1617 724 ASP A OD2 5603 N N . LYS A 725 ? 1.3628 0.9970 1.3780 -0.0801 -0.3618 0.1292 725 LYS A N 5604 C CA . LYS A 725 ? 1.3102 0.9369 1.3057 -0.1060 -0.3498 0.1236 725 LYS A CA 5605 C C . LYS A 725 ? 1.0922 0.7296 1.0974 -0.1052 -0.3283 0.1134 725 LYS A C 5606 O O . LYS A 725 ? 1.0459 0.6868 1.0394 -0.1201 -0.3170 0.1087 725 LYS A O 5607 C CB . LYS A 725 ? 1.3647 0.9479 1.3137 -0.1204 -0.3554 0.1286 725 LYS A CB 5608 C CG . LYS A 725 ? 1.4021 0.9415 1.3285 -0.1124 -0.3580 0.1300 725 LYS A CG 5609 C CD . LYS A 725 ? 1.4591 0.9550 1.3379 -0.1336 -0.3668 0.1406 725 LYS A CD 5610 C CE . LYS A 725 ? 1.6964 1.1315 1.5425 -0.1298 -0.3745 0.1432 725 LYS A CE 5611 N NZ . LYS A 725 ? 1.8631 1.2520 1.6594 -0.1566 -0.3844 0.1581 725 LYS A NZ 5612 N N . VAL A 726 ? 1.0971 0.7404 1.1197 -0.0836 -0.3225 0.1099 726 VAL A N 5613 C CA . VAL A 726 ? 1.0826 0.7333 1.1089 -0.0807 -0.3037 0.1002 726 VAL A CA 5614 C C . VAL A 726 ? 1.0775 0.7698 1.1417 -0.0612 -0.2932 0.0994 726 VAL A C 5615 O O . VAL A 726 ? 1.1026 0.8199 1.1918 -0.0446 -0.3006 0.1062 726 VAL A O 5616 C CB . VAL A 726 ? 1.1735 0.7791 1.1667 -0.0762 -0.3045 0.0946 726 VAL A CB 5617 C CG1 . VAL A 726 ? 1.3375 0.9134 1.2955 -0.1040 -0.3111 0.0985 726 VAL A CG1 5618 C CG2 . VAL A 726 ? 1.2817 0.8604 1.2683 -0.0476 -0.3160 0.0963 726 VAL A CG2 5619 N N . SER A 727 ? 1.0662 0.7723 1.1345 -0.0627 -0.2756 0.0929 727 SER A N 5620 C CA . SER A 727 ? 1.0940 0.8382 1.1912 -0.0448 -0.2617 0.0932 727 SER A CA 5621 C C . SER A 727 ? 1.1779 0.8995 1.2565 -0.0182 -0.2567 0.0841 727 SER A C 5622 O O . SER A 727 ? 1.1874 0.8588 1.2298 -0.0207 -0.2663 0.0780 727 SER A O 5623 C CB . SER A 727 ? 1.1026 0.8644 1.2045 -0.0589 -0.2461 0.0923 727 SER A CB 5624 O OG . SER A 727 ? 1.3157 1.0531 1.3884 -0.0602 -0.2383 0.0824 727 SER A OG 5625 N N . PRO A 728 ? 1.2549 1.0100 1.3524 0.0060 -0.2422 0.0834 728 PRO A N 5626 C CA . PRO A 728 ? 1.2222 0.9429 1.2872 0.0312 -0.2375 0.0705 728 PRO A CA 5627 C C . PRO A 728 ? 1.2462 0.9445 1.2838 0.0134 -0.2304 0.0605 728 PRO A C 5628 O O . PRO A 728 ? 1.2827 0.9965 1.3288 -0.0122 -0.2270 0.0645 728 PRO A O 5629 C CB . PRO A 728 ? 1.2521 1.0255 1.3446 0.0642 -0.2209 0.0738 728 PRO A CB 5630 C CG . PRO A 728 ? 1.2447 1.0812 1.3834 0.0418 -0.2126 0.0887 728 PRO A CG 5631 C CD . PRO A 728 ? 1.3200 1.1425 1.4636 0.0133 -0.2319 0.0950 728 PRO A CD 5632 N N . VAL A 729 ? 1.3270 0.9884 1.3282 0.0291 -0.2297 0.0473 729 VAL A N 5633 C CA . VAL A 729 ? 1.2481 0.8972 1.2248 0.0132 -0.2254 0.0382 729 VAL A CA 5634 C C . VAL A 729 ? 1.2618 0.9434 1.2439 0.0345 -0.2053 0.0347 729 VAL A C 5635 O O . VAL A 729 ? 1.4937 1.1629 1.4574 0.0660 -0.2005 0.0263 729 VAL A O 5636 C CB . VAL A 729 ? 1.2661 0.8482 1.1909 0.0064 -0.2421 0.0258 729 VAL A CB 5637 C CG1 . VAL A 729 ? 1.2361 0.8014 1.1539 -0.0315 -0.2570 0.0322 729 VAL A CG1 5638 C CG2 . VAL A 729 ? 1.3449 0.8797 1.2432 0.0394 -0.2504 0.0198 729 VAL A CG2 5639 N N . VAL A 730 ? 1.8994 2.2675 1.3558 0.6599 -0.6583 0.0211 730 VAL A N 5640 C CA . VAL A 730 ? 1.8416 2.2199 1.3695 0.6334 -0.6651 0.0052 730 VAL A CA 5641 C C . VAL A 730 ? 1.7832 2.1082 1.2982 0.6205 -0.6162 0.0014 730 VAL A C 5642 O O . VAL A 730 ? 1.7743 2.0607 1.2266 0.6193 -0.6160 -0.0226 730 VAL A O 5643 C CB . VAL A 730 ? 1.8186 2.2085 1.3620 0.6034 -0.7194 -0.0331 730 VAL A CB 5644 C CG1 . VAL A 730 ? 1.7531 2.1482 1.3818 0.5598 -0.7113 -0.0427 730 VAL A CG1 5645 C CG2 . VAL A 730 ? 1.8926 2.3360 1.4651 0.6019 -0.7595 -0.0265 730 VAL A CG2 5646 N N . SER A 731 ? 1.6785 2.0019 1.2506 0.6141 -0.5760 0.0240 731 SER A N 5647 C CA . SER A 731 ? 1.6198 1.8955 1.1869 0.6005 -0.5295 0.0239 731 SER A CA 5648 C C . SER A 731 ? 1.5548 1.8320 1.1900 0.5619 -0.5261 0.0021 731 SER A C 5649 O O . SER A 731 ? 1.5448 1.8677 1.2548 0.5495 -0.5389 0.0059 731 SER A O 5650 C CB . SER A 731 ? 1.6794 1.9392 1.2555 0.6182 -0.4897 0.0625 731 SER A CB 5651 O OG . SER A 731 ? 1.8297 2.1218 1.4801 0.6203 -0.4912 0.0746 731 SER A OG 5652 N N . HIS A 732 ? 1.5472 1.7800 1.1563 0.5448 -0.5083 -0.0178 732 HIS A N 5653 C CA . HIS A 732 ? 1.5327 1.7591 1.1983 0.5074 -0.5041 -0.0363 732 HIS A CA 5654 C C . HIS A 732 ? 1.5518 1.7356 1.2135 0.5012 -0.4537 -0.0308 732 HIS A C 5655 O O . HIS A 732 ? 1.5779 1.7257 1.1752 0.5152 -0.4350 -0.0314 732 HIS A O 5656 C CB . HIS A 732 ? 1.5780 1.7863 1.2179 0.4874 -0.5471 -0.0735 732 HIS A CB 5657 C CG . HIS A 732 ? 1.5113 1.6945 1.1902 0.4496 -0.5402 -0.0909 732 HIS A CG 5658 N ND1 . HIS A 732 ? 1.5957 1.8148 1.3646 0.4212 -0.5305 -0.0778 732 HIS A ND1 5659 C CD2 . HIS A 732 ? 1.5344 1.6619 1.1720 0.4387 -0.5417 -0.1187 732 HIS A CD2 5660 C CE1 . HIS A 732 ? 1.5901 1.7755 1.3726 0.3906 -0.5265 -0.0943 732 HIS A CE1 5661 N NE2 . HIS A 732 ? 1.6297 1.7555 1.3336 0.4007 -0.5344 -0.1204 732 HIS A NE2 5662 N N . LYS A 733 ? 1.5075 1.7021 1.2386 0.4817 -0.4322 -0.0239 733 LYS A N 5663 C CA . LYS A 733 ? 1.4433 1.5987 1.1753 0.4744 -0.3878 -0.0193 733 LYS A CA 5664 C C . LYS A 733 ? 1.4301 1.5781 1.2034 0.4389 -0.3857 -0.0392 733 LYS A C 5665 O O . LYS A 733 ? 1.4636 1.6482 1.2879 0.4173 -0.4127 -0.0461 733 LYS A O 5666 C CB . LYS A 733 ? 1.4066 1.5686 1.1713 0.4906 -0.3592 0.0094 733 LYS A CB 5667 C CG . LYS A 733 ? 1.3832 1.5874 1.2272 0.4798 -0.3571 0.0114 733 LYS A CG 5668 C CD . LYS A 733 ? 1.4342 1.6262 1.2954 0.5015 -0.3269 0.0323 733 LYS A CD 5669 C CE . LYS A 733 ? 1.4899 1.7279 1.4229 0.4965 -0.3188 0.0322 733 LYS A CE 5670 N NZ . LYS A 733 ? 1.5865 1.9030 1.5659 0.5023 -0.3490 0.0367 733 LYS A NZ 5671 N N . VAL A 734 ? 1.4379 1.5417 1.1907 0.4315 -0.3549 -0.0446 734 VAL A N 5672 C CA . VAL A 734 ? 1.4544 1.5454 1.2437 0.3999 -0.3477 -0.0589 734 VAL A CA 5673 C C . VAL A 734 ? 1.4173 1.4874 1.2212 0.4002 -0.3020 -0.0455 734 VAL A C 5674 O O . VAL A 734 ? 1.4140 1.4539 1.1757 0.4167 -0.2785 -0.0358 734 VAL A O 5675 C CB . VAL A 734 ? 1.5531 1.6014 1.2942 0.3889 -0.3669 -0.0887 734 VAL A CB 5676 C CG1 . VAL A 734 ? 1.6036 1.6663 1.3457 0.3775 -0.4216 -0.1069 734 VAL A CG1 5677 C CG2 . VAL A 734 ? 1.5768 1.5934 1.2391 0.4182 -0.3503 -0.0900 734 VAL A CG2 5678 N N . ASP A 735 ? 1.4015 1.4916 1.2658 0.3815 -0.2912 -0.0426 735 ASP A N 5679 C CA . ASP A 735 ? 1.4041 1.4766 1.2838 0.3842 -0.2525 -0.0318 735 ASP A CA 5680 C C . ASP A 735 ? 1.4662 1.4887 1.3158 0.3707 -0.2331 -0.0438 735 ASP A C 5681 O O . ASP A 735 ? 1.5453 1.5555 1.3913 0.3498 -0.2471 -0.0623 735 ASP A O 5682 C CB . ASP A 735 ? 1.4570 1.5756 1.4059 0.3737 -0.2466 -0.0252 735 ASP A CB 5683 C CG . ASP A 735 ? 1.6103 1.7894 1.5941 0.3926 -0.2628 -0.0112 735 ASP A CG 5684 O OD1 . ASP A 735 ? 1.7458 1.9163 1.7001 0.4215 -0.2660 -0.0017 735 ASP A OD1 5685 O OD2 . ASP A 735 ? 1.6226 1.8625 1.6651 0.3788 -0.2727 -0.0064 735 ASP A OD2 5686 N N . LEU A 736 ? 1.3978 1.3897 1.2262 0.3826 -0.2042 -0.0319 736 LEU A N 5687 C CA . LEU A 736 ? 1.2873 1.2406 1.0942 0.3714 -0.1830 -0.0391 736 LEU A CA 5688 C C . LEU A 736 ? 1.2589 1.2115 1.1099 0.3544 -0.1654 -0.0415 736 LEU A C 5689 O O . LEU A 736 ? 1.3174 1.2812 1.1967 0.3634 -0.1534 -0.0295 736 LEU A O 5690 C CB . LEU A 736 ? 1.2635 1.1911 1.0330 0.3867 -0.1628 -0.0203 736 LEU A CB 5691 C CG . LEU A 736 ? 1.3150 1.2418 1.0277 0.4020 -0.1698 -0.0161 736 LEU A CG 5692 C CD1 . LEU A 736 ? 1.5552 1.5086 1.2570 0.4189 -0.1960 -0.0114 736 LEU A CD1 5693 C CD2 . LEU A 736 ? 1.2932 1.2028 0.9826 0.4081 -0.1458 0.0109 736 LEU A CD2 5694 N N . ALA A 737 ? 1.2739 1.2114 1.1261 0.3335 -0.1655 -0.0573 737 ALA A N 5695 C CA . ALA A 737 ? 1.1910 1.1311 1.0822 0.3160 -0.1501 -0.0579 737 ALA A CA 5696 C C . ALA A 737 ? 1.1157 1.0148 0.9843 0.3131 -0.1252 -0.0602 737 ALA A C 5697 O O . ALA A 737 ? 1.1189 0.9923 0.9457 0.3176 -0.1246 -0.0663 737 ALA A O 5698 C CB . ALA A 737 ? 1.1898 1.1458 1.1088 0.2894 -0.1727 -0.0685 737 ALA A CB 5699 N N . VAL A 738 ? 1.0748 0.9736 0.9700 0.3088 -0.1051 -0.0547 738 VAL A N 5700 C CA . VAL A 738 ? 1.0362 0.8999 0.9158 0.3038 -0.0839 -0.0564 738 VAL A CA 5701 C C . VAL A 738 ? 1.0173 0.8773 0.9136 0.2816 -0.0832 -0.0670 738 VAL A C 5702 O O . VAL A 738 ? 1.0174 0.9023 0.9509 0.2728 -0.0790 -0.0627 738 VAL A O 5703 C CB . VAL A 738 ? 0.9016 0.7555 0.7901 0.3154 -0.0657 -0.0451 738 VAL A CB 5704 C CG1 . VAL A 738 ? 0.8794 0.7006 0.7568 0.3063 -0.0480 -0.0470 738 VAL A CG1 5705 C CG2 . VAL A 738 ? 0.9187 0.7627 0.7875 0.3349 -0.0701 -0.0311 738 VAL A CG2 5706 N N . LEU A 739 ? 1.0228 0.8542 0.8898 0.2754 -0.0877 -0.0790 739 LEU A N 5707 C CA . LEU A 739 ? 1.0805 0.8959 0.9569 0.2557 -0.0893 -0.0881 739 LEU A CA 5708 C C . LEU A 739 ? 1.0531 0.8342 0.8974 0.2609 -0.0741 -0.0938 739 LEU A C 5709 O O . LEU A 739 ? 1.0052 0.7716 0.8105 0.2743 -0.0795 -0.1021 739 LEU A O 5710 C CB . LEU A 739 ? 1.2626 1.0734 1.1380 0.2418 -0.1224 -0.1006 739 LEU A CB 5711 C CG . LEU A 739 ? 1.1993 0.9872 1.0874 0.2167 -0.1337 -0.1066 739 LEU A CG 5712 C CD1 . LEU A 739 ? 1.1777 0.9839 1.0979 0.1923 -0.1678 -0.1042 739 LEU A CD1 5713 C CD2 . LEU A 739 ? 1.2149 0.9499 1.0528 0.2260 -0.1407 -0.1266 739 LEU A CD2 5714 N N . ALA A 740 ? 1.1073 0.8819 0.9674 0.2532 -0.0552 -0.0887 740 ALA A N 5715 C CA . ALA A 740 ? 1.1457 0.8940 0.9828 0.2560 -0.0420 -0.0925 740 ALA A CA 5716 C C . ALA A 740 ? 1.0355 0.7700 0.8884 0.2388 -0.0408 -0.0966 740 ALA A C 5717 O O . ALA A 740 ? 0.8682 0.6166 0.7491 0.2303 -0.0295 -0.0874 740 ALA A O 5718 C CB . ALA A 740 ? 1.1590 0.9089 0.9946 0.2645 -0.0216 -0.0787 740 ALA A CB 5719 N N . ALA A 741 ? 1.0305 0.7362 0.8611 0.2371 -0.0536 -0.1101 741 ALA A N 5720 C CA . ALA A 741 ? 0.9938 0.6793 0.8365 0.2198 -0.0567 -0.1114 741 ALA A CA 5721 C C . ALA A 741 ? 0.9658 0.6415 0.7997 0.2265 -0.0338 -0.1083 741 ALA A C 5722 O O . ALA A 741 ? 1.0230 0.6862 0.8266 0.2435 -0.0296 -0.1152 741 ALA A O 5723 C CB . ALA A 741 ? 1.0241 0.6704 0.8431 0.2166 -0.0867 -0.1284 741 ALA A CB 5724 N N . VAL A 742 ? 0.9169 0.6043 0.7769 0.2151 -0.0197 -0.0968 742 VAL A N 5725 C CA . VAL A 742 ? 0.9226 0.6024 0.7760 0.2200 -0.0010 -0.0934 742 VAL A CA 5726 C C . VAL A 742 ? 0.9867 0.6510 0.8477 0.2062 -0.0017 -0.0911 742 VAL A C 5727 O O . VAL A 742 ? 1.0463 0.7285 0.9333 0.1918 -0.0004 -0.0803 742 VAL A O 5728 C CB . VAL A 742 ? 0.8631 0.5632 0.7298 0.2249 0.0151 -0.0835 742 VAL A CB 5729 C CG1 . VAL A 742 ? 0.7967 0.4845 0.6515 0.2300 0.0273 -0.0814 742 VAL A CG1 5730 C CG2 . VAL A 742 ? 0.8076 0.5216 0.6724 0.2351 0.0113 -0.0812 742 VAL A CG2 5731 N N . GLU A 743 ? 1.0169 0.6532 0.8553 0.2127 -0.0033 -0.0985 743 GLU A N 5732 C CA . GLU A 743 ? 1.0709 0.6859 0.9116 0.2017 -0.0056 -0.0949 743 GLU A CA 5733 C C . GLU A 743 ? 1.0634 0.6818 0.8987 0.2099 0.0132 -0.0909 743 GLU A C 5734 O O . GLU A 743 ? 0.9439 0.5712 0.7681 0.2243 0.0220 -0.0934 743 GLU A O 5735 C CB . GLU A 743 ? 1.0916 0.6622 0.9072 0.2053 -0.0288 -0.1082 743 GLU A CB 5736 C CG . GLU A 743 ? 1.1806 0.7408 0.9610 0.2346 -0.0260 -0.1227 743 GLU A CG 5737 C CD . GLU A 743 ? 1.5010 1.0103 1.2486 0.2469 -0.0500 -0.1394 743 GLU A CD 5738 O OE1 . GLU A 743 ? 1.5825 1.0556 1.3360 0.2269 -0.0732 -0.1387 743 GLU A OE1 5739 O OE2 . GLU A 743 ? 1.7573 1.2637 1.4728 0.2777 -0.0474 -0.1517 743 GLU A OE2 5740 N N . ILE A 744 ? 1.0466 0.6618 0.8912 0.1990 0.0177 -0.0815 744 ILE A N 5741 C CA . ILE A 744 ? 0.9650 0.5803 0.8022 0.2061 0.0309 -0.0787 744 ILE A CA 5742 C C . ILE A 744 ? 1.0396 0.6243 0.8646 0.2043 0.0229 -0.0779 744 ILE A C 5743 O O . ILE A 744 ? 1.2176 0.7915 1.0515 0.1881 0.0152 -0.0678 744 ILE A O 5744 C CB . ILE A 744 ? 0.9055 0.5462 0.7566 0.2023 0.0447 -0.0691 744 ILE A CB 5745 C CG1 . ILE A 744 ? 0.8392 0.4738 0.6786 0.2083 0.0524 -0.0677 744 ILE A CG1 5746 C CG2 . ILE A 744 ? 1.0180 0.6755 0.8885 0.1872 0.0437 -0.0558 744 ILE A CG2 5747 C CD1 . ILE A 744 ? 0.8347 0.4878 0.6763 0.2116 0.0626 -0.0633 744 ILE A CD1 5748 N N . ARG A 745 ? 1.0447 0.6184 0.8508 0.2212 0.0236 -0.0855 745 ARG A N 5749 C CA . ARG A 745 ? 1.0568 0.5972 0.8463 0.2270 0.0136 -0.0872 745 ARG A CA 5750 C C . ARG A 745 ? 1.1025 0.6541 0.8897 0.2339 0.0252 -0.0811 745 ARG A C 5751 O O . ARG A 745 ? 1.1147 0.6963 0.9090 0.2375 0.0372 -0.0793 745 ARG A O 5752 C CB . ARG A 745 ? 0.9386 0.4563 0.7018 0.2497 0.0002 -0.1041 745 ARG A CB 5753 C CG . ARG A 745 ? 0.9943 0.4928 0.7523 0.2452 -0.0179 -0.1139 745 ARG A CG 5754 C CD . ARG A 745 ? 1.1189 0.5895 0.8392 0.2759 -0.0335 -0.1347 745 ARG A CD 5755 N NE . ARG A 745 ? 1.4357 0.8712 1.1344 0.2924 -0.0418 -0.1390 745 ARG A NE 5756 C CZ . ARG A 745 ? 1.6221 0.9968 1.3092 0.2837 -0.0675 -0.1411 745 ARG A CZ 5757 N NH1 . ARG A 745 ? 1.6834 1.0315 1.3831 0.2544 -0.0878 -0.1369 745 ARG A NH1 5758 N NH2 . ARG A 745 ? 1.6100 0.9532 1.2759 0.3022 -0.0751 -0.1442 745 ARG A NH2 5759 N N . GLY A 746 ? 1.0364 0.5606 0.8135 0.2342 0.0178 -0.0765 746 GLY A N 5760 C CA . GLY A 746 ? 0.8952 0.4291 0.6680 0.2423 0.0254 -0.0709 746 GLY A CA 5761 C C . GLY A 746 ? 1.0852 0.5824 0.8385 0.2544 0.0126 -0.0709 746 GLY A C 5762 O O . GLY A 746 ? 1.3362 0.7905 1.0807 0.2481 -0.0042 -0.0702 746 GLY A O 5763 N N . VAL A 747 ? 0.9313 0.4438 0.6789 0.2710 0.0173 -0.0703 747 VAL A N 5764 C CA . VAL A 747 ? 0.9716 0.4527 0.6992 0.2887 0.0054 -0.0700 747 VAL A CA 5765 C C . VAL A 747 ? 1.0445 0.5502 0.7756 0.2915 0.0127 -0.0594 747 VAL A C 5766 O O . VAL A 747 ? 1.0476 0.5944 0.7941 0.2843 0.0242 -0.0566 747 VAL A O 5767 C CB . VAL A 747 ? 0.9975 0.4739 0.7063 0.3233 -0.0020 -0.0864 747 VAL A CB 5768 C CG1 . VAL A 747 ? 1.4969 0.9297 1.1890 0.3257 -0.0185 -0.1006 747 VAL A CG1 5769 C CG2 . VAL A 747 ? 0.9876 0.5289 0.7115 0.3341 0.0145 -0.0869 747 VAL A CG2 5770 N N . SER A 748 ? 1.1516 0.6266 0.8660 0.3021 0.0019 -0.0538 748 SER A N 5771 C CA . SER A 748 ? 1.0696 0.5661 0.7835 0.3081 0.0052 -0.0441 748 SER A CA 5772 C C . SER A 748 ? 1.1706 0.6582 0.8688 0.3419 -0.0053 -0.0486 748 SER A C 5773 O O . SER A 748 ? 1.2673 0.7010 0.9432 0.3553 -0.0212 -0.0518 748 SER A O 5774 C CB . SER A 748 ? 1.0590 0.5357 0.7669 0.2885 0.0041 -0.0264 748 SER A CB 5775 O OG . SER A 748 ? 1.2922 0.7891 0.9947 0.2963 0.0052 -0.0186 748 SER A OG 5776 N N . SER A 749 ? 1.0000 0.5405 0.7104 0.3563 0.0010 -0.0480 749 SER A N 5777 C CA . SER A 749 ? 1.0330 0.5826 0.7329 0.3929 -0.0065 -0.0497 749 SER A CA 5778 C C . SER A 749 ? 1.1431 0.7149 0.8476 0.3922 -0.0092 -0.0360 749 SER A C 5779 O O . SER A 749 ? 1.2921 0.9166 1.0199 0.3792 -0.0031 -0.0300 749 SER A O 5780 C CB . SER A 749 ? 1.0816 0.6908 0.7958 0.4154 0.0021 -0.0560 749 SER A CB 5781 O OG . SER A 749 ? 1.5134 1.1852 1.2608 0.3933 0.0126 -0.0452 749 SER A OG 5782 N N . PRO A 750 ? 1.1598 0.6868 0.8402 0.4057 -0.0222 -0.0303 750 PRO A N 5783 C CA . PRO A 750 ? 1.2325 0.6838 0.8839 0.4176 -0.0372 -0.0354 750 PRO A CA 5784 C C . PRO A 750 ? 1.2833 0.6878 0.9313 0.3797 -0.0390 -0.0256 750 PRO A C 5785 O O . PRO A 750 ? 1.1916 0.6267 0.8561 0.3507 -0.0255 -0.0169 750 PRO A O 5786 C CB . PRO A 750 ? 1.3240 0.7526 0.9547 0.4454 -0.0523 -0.0272 750 PRO A CB 5787 C CG . PRO A 750 ? 1.1938 0.6994 0.8468 0.4511 -0.0433 -0.0198 750 PRO A CG 5788 C CD . PRO A 750 ? 1.0816 0.6283 0.7607 0.4135 -0.0279 -0.0178 750 PRO A CD 5789 N N . ASP A 751 ? 1.4967 0.8288 1.1231 0.3813 -0.0581 -0.0262 751 ASP A N 5790 C CA . ASP A 751 ? 1.4325 0.7256 1.0612 0.3428 -0.0631 -0.0095 751 ASP A CA 5791 C C . ASP A 751 ? 1.4287 0.7167 1.0519 0.3287 -0.0638 0.0188 751 ASP A C 5792 O O . ASP A 751 ? 1.5565 0.8560 1.1906 0.2958 -0.0550 0.0393 751 ASP A O 5793 C CB . ASP A 751 ? 1.5482 0.7596 1.1568 0.3450 -0.0910 -0.0161 751 ASP A CB 5794 C CG . ASP A 751 ? 1.8520 1.0829 1.4658 0.3549 -0.0902 -0.0445 751 ASP A CG 5795 O OD1 . ASP A 751 ? 1.9743 1.2488 1.6057 0.3481 -0.0700 -0.0505 751 ASP A OD1 5796 O OD2 . ASP A 751 ? 1.9799 1.1848 1.5776 0.3700 -0.1102 -0.0600 751 ASP A OD2 5797 N N . HIS A 752 ? 1.3668 0.6440 0.9718 0.3574 -0.0736 0.0212 752 HIS A N 5798 C CA . HIS A 752 ? 1.4047 0.6711 0.9976 0.3495 -0.0779 0.0491 752 HIS A CA 5799 C C . HIS A 752 ? 1.3855 0.6912 0.9725 0.3795 -0.0755 0.0465 752 HIS A C 5800 O O . HIS A 752 ? 1.5751 0.9029 1.1650 0.4117 -0.0768 0.0262 752 HIS A O 5801 C CB . HIS A 752 ? 1.6680 0.8446 1.2373 0.3473 -0.1071 0.0658 752 HIS A CB 5802 C CG . HIS A 752 ? 1.9852 1.1136 1.5380 0.3798 -0.1295 0.0398 752 HIS A CG 5803 N ND1 . HIS A 752 ? 1.9996 1.1708 1.5510 0.4178 -0.1266 0.0187 752 HIS A ND1 5804 C CD2 . HIS A 752 ? 2.2090 1.2857 1.7589 0.3682 -0.1517 0.0300 752 HIS A CD2 5805 C CE1 . HIS A 752 ? 2.0939 1.2407 1.6360 0.4325 -0.1434 -0.0028 752 HIS A CE1 5806 N NE2 . HIS A 752 ? 2.2460 1.3326 1.7855 0.4033 -0.1602 0.0014 752 HIS A NE2 5807 N N . VAL A 753 ? 1.3413 0.6627 0.9206 0.3694 -0.0722 0.0691 753 VAL A N 5808 C CA . VAL A 753 ? 1.3401 0.6945 0.9118 0.3950 -0.0753 0.0705 753 VAL A CA 5809 C C . VAL A 753 ? 1.5062 0.8163 1.0496 0.3982 -0.0908 0.0993 753 VAL A C 5810 O O . VAL A 753 ? 1.4636 0.7676 0.9995 0.3705 -0.0854 0.1250 753 VAL A O 5811 C CB . VAL A 753 ? 1.2945 0.7217 0.8810 0.3826 -0.0585 0.0663 753 VAL A CB 5812 C CG1 . VAL A 753 ? 1.3090 0.7663 0.8863 0.4044 -0.0677 0.0715 753 VAL A CG1 5813 C CG2 . VAL A 753 ? 1.1708 0.6397 0.7862 0.3798 -0.0471 0.0418 753 VAL A CG2 5814 N N . PHE A 754 ? 1.6487 0.9322 1.1757 0.4344 -0.1096 0.0976 754 PHE A N 5815 C CA . PHE A 754 ? 1.6123 0.8424 1.1095 0.4409 -0.1289 0.1262 754 PHE A CA 5816 C C . PHE A 754 ? 1.5735 0.8537 1.0621 0.4521 -0.1265 0.1389 754 PHE A C 5817 O O . PHE A 754 ? 1.6037 0.9233 1.0982 0.4841 -0.1306 0.1240 754 PHE A O 5818 C CB . PHE A 754 ? 1.5374 0.7057 1.0192 0.4739 -0.1547 0.1156 754 PHE A CB 5819 C CG . PHE A 754 ? 1.5606 0.6767 1.0487 0.4545 -0.1638 0.1031 754 PHE A CG 5820 C CD1 . PHE A 754 ? 1.7640 0.9083 1.2694 0.4646 -0.1556 0.0684 754 PHE A CD1 5821 C CD2 . PHE A 754 ? 1.6765 0.7188 1.1538 0.4246 -0.1828 0.1291 754 PHE A CD2 5822 C CE1 . PHE A 754 ? 1.7289 0.8264 1.2357 0.4483 -0.1671 0.0556 754 PHE A CE1 5823 C CE2 . PHE A 754 ? 1.7732 0.7672 1.2576 0.4050 -0.1966 0.1176 754 PHE A CE2 5824 C CZ . PHE A 754 ? 1.7370 0.7574 1.2335 0.4185 -0.1892 0.0786 754 PHE A CZ 5825 N N . LEU A 755 ? 1.5382 0.8228 1.0130 0.4264 -0.1203 0.1680 755 LEU A N 5826 C CA . LEU A 755 ? 1.5522 0.8729 1.0081 0.4381 -0.1225 0.1829 755 LEU A CA 5827 C C . LEU A 755 ? 1.6641 0.9228 1.0890 0.4560 -0.1465 0.2119 755 LEU A C 5828 O O . LEU A 755 ? 1.8240 1.0114 1.2391 0.4417 -0.1580 0.2329 755 LEU A O 5829 C CB . LEU A 755 ? 1.6187 0.9817 1.0670 0.4091 -0.1029 0.1984 755 LEU A CB 5830 C CG . LEU A 755 ? 1.6373 1.0566 1.1096 0.3950 -0.0829 0.1696 755 LEU A CG 5831 C CD1 . LEU A 755 ? 1.6845 1.1428 1.1378 0.3786 -0.0668 0.1830 755 LEU A CD1 5832 C CD2 . LEU A 755 ? 1.5983 1.0611 1.0881 0.4167 -0.0893 0.1395 755 LEU A CD2 5833 N N . PRO A 756 ? 1.6581 0.9407 1.0683 0.4863 -0.1579 0.2149 756 PRO A N 5834 C CA . PRO A 756 ? 1.6391 1.0026 1.0619 0.5017 -0.1532 0.1944 756 PRO A CA 5835 C C . PRO A 756 ? 1.7309 1.1275 1.1886 0.5221 -0.1525 0.1597 756 PRO A C 5836 O O . PRO A 756 ? 1.8230 1.1755 1.2853 0.5368 -0.1581 0.1498 756 PRO A O 5837 C CB . PRO A 756 ? 1.7361 1.0944 1.1302 0.5303 -0.1736 0.2155 756 PRO A CB 5838 C CG . PRO A 756 ? 1.9385 1.2084 1.3139 0.5460 -0.1928 0.2327 756 PRO A CG 5839 C CD . PRO A 756 ? 1.8741 1.0943 1.2522 0.5073 -0.1831 0.2435 756 PRO A CD 5840 N N . ILE A 757 ? 1.7413 1.2151 1.2215 0.5233 -0.1481 0.1434 757 ILE A N 5841 C CA . ILE A 757 ? 1.6400 1.1620 1.1599 0.5348 -0.1439 0.1176 757 ILE A CA 5842 C C . ILE A 757 ? 1.5597 1.1375 1.0929 0.5698 -0.1601 0.1175 757 ILE A C 5843 O O . ILE A 757 ? 1.6037 1.2091 1.1257 0.5698 -0.1714 0.1286 757 ILE A O 5844 C CB . ILE A 757 ? 1.6607 1.2300 1.2060 0.4996 -0.1275 0.1019 757 ILE A CB 5845 C CG1 . ILE A 757 ? 1.6806 1.3187 1.2707 0.5073 -0.1267 0.0841 757 ILE A CG1 5846 C CG2 . ILE A 757 ? 1.6816 1.2730 1.2070 0.4818 -0.1306 0.1095 757 ILE A CG2 5847 C CD1 . ILE A 757 ? 1.7315 1.3611 1.3427 0.5036 -0.1115 0.0689 757 ILE A CD1 5848 N N . PRO A 758 ? 1.5816 1.1819 1.1379 0.6023 -0.1616 0.1055 758 PRO A N 5849 C CA . PRO A 758 ? 1.7735 1.4364 1.3473 0.6421 -0.1759 0.1086 758 PRO A CA 5850 C C . PRO A 758 ? 1.8024 1.5615 1.4146 0.6224 -0.1792 0.1088 758 PRO A C 5851 O O . PRO A 758 ? 1.6583 1.4520 1.2998 0.5897 -0.1674 0.0983 758 PRO A O 5852 C CB . PRO A 758 ? 1.8590 1.5334 1.4501 0.6780 -0.1696 0.0933 758 PRO A CB 5853 C CG . PRO A 758 ? 1.7452 1.3826 1.3383 0.6466 -0.1513 0.0792 758 PRO A CG 5854 C CD . PRO A 758 ? 1.5949 1.1570 1.1545 0.6104 -0.1519 0.0904 758 PRO A CD 5855 N N . ASN A 759 ? 1.9489 1.7459 1.5599 0.6422 -0.1991 0.1217 759 ASN A N 5856 C CA . ASN A 759 ? 1.8467 1.7298 1.4919 0.6234 -0.2121 0.1242 759 ASN A CA 5857 C C . ASN A 759 ? 1.7599 1.6302 1.3980 0.5723 -0.2087 0.1159 759 ASN A C 5858 O O . ASN A 759 ? 1.7079 1.6241 1.3847 0.5446 -0.2056 0.1066 759 ASN A O 5859 C CB . ASN A 759 ? 1.7515 1.7309 1.4588 0.6345 -0.2092 0.1222 759 ASN A CB 5860 C CG . ASN A 759 ? 1.8391 1.8500 1.5532 0.6946 -0.2143 0.1299 759 ASN A CG 5861 O OD1 . ASN A 759 ? 1.8611 1.8437 1.5435 0.7250 -0.2305 0.1399 759 ASN A OD1 5862 N ND2 . ASN A 759 ? 1.8667 1.9383 1.6192 0.7160 -0.2006 0.1262 759 ASN A ND2 5863 N N . TRP A 760 ? 1.8041 1.6128 1.3908 0.5626 -0.2100 0.1210 760 TRP A N 5864 C CA . TRP A 760 ? 1.8939 1.6887 1.4630 0.5245 -0.2066 0.1115 760 TRP A CA 5865 C C . TRP A 760 ? 1.8955 1.7067 1.4353 0.5233 -0.2311 0.1164 760 TRP A C 5866 O O . TRP A 760 ? 1.8334 1.6137 1.3294 0.5417 -0.2367 0.1324 760 TRP A O 5867 C CB . TRP A 760 ? 1.9585 1.6791 1.4906 0.5126 -0.1840 0.1138 760 TRP A CB 5868 C CG . TRP A 760 ? 1.9467 1.6547 1.4450 0.4876 -0.1814 0.1093 760 TRP A CG 5869 C CD1 . TRP A 760 ? 1.9770 1.6498 1.4231 0.4897 -0.1782 0.1253 760 TRP A CD1 5870 C CD2 . TRP A 760 ? 1.7922 1.5242 1.3027 0.4613 -0.1830 0.0883 760 TRP A CD2 5871 N NE1 . TRP A 760 ? 1.8806 1.5600 1.3031 0.4715 -0.1751 0.1130 760 TRP A NE1 5872 C CE2 . TRP A 760 ? 1.8169 1.5255 1.2764 0.4546 -0.1803 0.0881 760 TRP A CE2 5873 C CE3 . TRP A 760 ? 1.6796 1.4500 1.2377 0.4438 -0.1879 0.0718 760 TRP A CE3 5874 C CZ2 . TRP A 760 ? 1.8479 1.5625 1.2976 0.4363 -0.1843 0.0664 760 TRP A CZ2 5875 C CZ3 . TRP A 760 ? 1.7479 1.5187 1.2998 0.4193 -0.1942 0.0537 760 TRP A CZ3 5876 C CH2 . TRP A 760 ? 1.8656 1.6048 1.3613 0.4182 -0.1934 0.0484 760 TRP A CH2 5877 N N . GLU A 761 ? 1.8897 1.7466 1.4518 0.5010 -0.2488 0.1035 761 GLU A N 5878 C CA . GLU A 761 ? 1.9387 1.8068 1.4686 0.4980 -0.2775 0.1017 761 GLU A CA 5879 C C . GLU A 761 ? 1.9085 1.7590 1.4204 0.4672 -0.2812 0.0795 761 GLU A C 5880 O O . GLU A 761 ? 1.7401 1.6153 1.2943 0.4422 -0.2886 0.0664 761 GLU A O 5881 C CB . GLU A 761 ? 1.9490 1.8902 1.5212 0.5050 -0.3102 0.1079 761 GLU A CB 5882 C CG . GLU A 761 ? 1.9804 1.9425 1.5628 0.5451 -0.3106 0.1289 761 GLU A CG 5883 C CD . GLU A 761 ? 1.9991 2.0488 1.6298 0.5532 -0.3423 0.1380 761 GLU A CD 5884 O OE1 . GLU A 761 ? 2.0532 2.1256 1.6865 0.5913 -0.3486 0.1547 761 GLU A OE1 5885 O OE2 . GLU A 761 ? 1.9462 2.0418 1.6134 0.5210 -0.3634 0.1301 761 GLU A OE2 5886 N N . HIS A 762 ? 1.9875 1.7959 1.4344 0.4716 -0.2764 0.0770 762 HIS A N 5887 C CA . HIS A 762 ? 1.8432 1.6299 1.2599 0.4533 -0.2796 0.0534 762 HIS A CA 5888 C C . HIS A 762 ? 1.8628 1.6736 1.2791 0.4431 -0.3252 0.0357 762 HIS A C 5889 O O . HIS A 762 ? 2.0029 1.8299 1.3940 0.4586 -0.3526 0.0415 762 HIS A O 5890 C CB . HIS A 762 ? 1.8357 1.5851 1.1800 0.4682 -0.2613 0.0593 762 HIS A CB 5891 C CG . HIS A 762 ? 1.9509 1.6888 1.2420 0.4679 -0.2787 0.0346 762 HIS A CG 5892 N ND1 . HIS A 762 ? 1.9665 1.6900 1.2652 0.4494 -0.2806 0.0070 762 HIS A ND1 5893 C CD2 . HIS A 762 ? 2.0996 1.8350 1.3232 0.4886 -0.2975 0.0316 762 HIS A CD2 5894 C CE1 . HIS A 762 ? 2.0528 1.7607 1.2891 0.4610 -0.3012 -0.0145 762 HIS A CE1 5895 N NE2 . HIS A 762 ? 2.1315 1.8488 1.3201 0.4854 -0.3110 -0.0007 762 HIS A NE2 5896 N N . LYS A 763 ? 1.7967 1.6059 1.2406 0.4155 -0.3368 0.0151 763 LYS A N 5897 C CA . LYS A 763 ? 1.8737 1.6929 1.3184 0.3988 -0.3869 -0.0027 763 LYS A CA 5898 C C . LYS A 763 ? 1.9989 1.7631 1.3784 0.3983 -0.3966 -0.0335 763 LYS A C 5899 O O . LYS A 763 ? 2.0064 1.7402 1.3772 0.3950 -0.3659 -0.0425 763 LYS A O 5900 C CB . LYS A 763 ? 1.8312 1.6913 1.3602 0.3657 -0.4023 0.0016 763 LYS A CB 5901 C CG . LYS A 763 ? 1.9525 1.8379 1.5011 0.3435 -0.4618 -0.0043 763 LYS A CG 5902 C CD . LYS A 763 ? 1.8683 1.8098 1.5100 0.3081 -0.4730 0.0119 763 LYS A CD 5903 C CE . LYS A 763 ? 1.8141 1.7924 1.4870 0.2814 -0.5360 0.0154 763 LYS A CE 5904 N NZ . LYS A 763 ? 1.8341 1.8623 1.5053 0.3061 -0.5522 0.0317 763 LYS A NZ 5905 N N . GLU A 764 ? 2.0430 1.7954 1.3737 0.4056 -0.4410 -0.0508 764 GLU A N 5906 C CA . GLU A 764 ? 2.0283 1.7264 1.2842 0.4156 -0.4562 -0.0847 764 GLU A CA 5907 C C . GLU A 764 ? 2.0063 1.6732 1.2916 0.3862 -0.4663 -0.1062 764 GLU A C 5908 O O . GLU A 764 ? 2.0340 1.6582 1.2746 0.3978 -0.4492 -0.1271 764 GLU A O 5909 C CB . GLU A 764 ? 2.0717 1.7608 1.2730 0.4276 -0.5130 -0.1027 764 GLU A CB 5910 C CG . GLU A 764 ? 2.1769 1.8947 1.3406 0.4591 -0.5076 -0.0815 764 GLU A CG 5911 C CD . GLU A 764 ? 2.4010 2.1066 1.5007 0.4742 -0.5654 -0.1030 764 GLU A CD 5912 O OE1 . GLU A 764 ? 2.4401 2.1039 1.5132 0.4638 -0.6092 -0.1386 764 GLU A OE1 5913 O OE2 . GLU A 764 ? 2.4863 2.2194 1.5593 0.4975 -0.5705 -0.0849 764 GLU A OE2 5914 N N . ASN A 765 ? 1.9686 1.6620 1.3305 0.3492 -0.4942 -0.0976 765 ASN A N 5915 C CA . ASN A 765 ? 2.0148 1.6819 1.4135 0.3159 -0.5073 -0.1102 765 ASN A CA 5916 C C . ASN A 765 ? 1.9993 1.7197 1.4932 0.2895 -0.4784 -0.0794 765 ASN A C 5917 O O . ASN A 765 ? 2.0384 1.8102 1.5991 0.2628 -0.5053 -0.0595 765 ASN A O 5918 C CB . ASN A 765 ? 2.1177 1.7593 1.5136 0.2904 -0.5812 -0.1292 765 ASN A CB 5919 C CG . ASN A 765 ? 2.1177 1.7088 1.5301 0.2601 -0.6016 -0.1464 765 ASN A CG 5920 O OD1 . ASN A 765 ? 2.0998 1.6655 1.5041 0.2678 -0.5608 -0.1529 765 ASN A OD1 5921 N ND2 . ASN A 765 ? 2.1219 1.6967 1.5586 0.2238 -0.6684 -0.1518 765 ASN A ND2 5922 N N . PRO A 766 ? 1.9509 1.6647 1.4504 0.2985 -0.4239 -0.0741 766 PRO A N 5923 C CA . PRO A 766 ? 1.7569 1.5165 1.3325 0.2833 -0.3903 -0.0484 766 PRO A CA 5924 C C . PRO A 766 ? 1.7016 1.4848 1.3465 0.2411 -0.4191 -0.0403 766 PRO A C 5925 O O . PRO A 766 ? 1.7429 1.4798 1.3723 0.2202 -0.4551 -0.0599 766 PRO A O 5926 C CB . PRO A 766 ? 1.7203 1.4427 1.2697 0.2965 -0.3421 -0.0567 766 PRO A CB 5927 C CG . PRO A 766 ? 1.8563 1.5423 1.3229 0.3287 -0.3361 -0.0716 766 PRO A CG 5928 C CD . PRO A 766 ? 2.0047 1.6705 1.4335 0.3273 -0.3916 -0.0922 766 PRO A CD 5929 N N . GLU A 767 ? 1.6396 1.4945 1.3582 0.2308 -0.4043 -0.0099 767 GLU A N 5930 C CA . GLU A 767 ? 1.6292 1.5284 1.4230 0.1896 -0.4289 0.0092 767 GLU A CA 5931 C C . GLU A 767 ? 1.5647 1.5009 1.4093 0.1862 -0.3839 0.0281 767 GLU A C 5932 O O . GLU A 767 ? 1.6059 1.5185 1.4665 0.1614 -0.3832 0.0255 767 GLU A O 5933 C CB . GLU A 767 ? 1.7247 1.7017 1.5682 0.1790 -0.4638 0.0344 767 GLU A CB 5934 C CG . GLU A 767 ? 1.7696 1.7133 1.5660 0.1788 -0.5169 0.0162 767 GLU A CG 5935 C CD . GLU A 767 ? 1.7994 1.8282 1.6505 0.1678 -0.5524 0.0438 767 GLU A CD 5936 O OE1 . GLU A 767 ? 1.8169 1.8269 1.6306 0.1710 -0.5967 0.0309 767 GLU A OE1 5937 O OE2 . GLU A 767 ? 1.8096 1.9292 1.7402 0.1587 -0.5363 0.0787 767 GLU A OE2 5938 N N . THR A 768 ? 1.5277 1.5185 1.3933 0.2141 -0.3492 0.0461 768 THR A N 5939 C CA . THR A 768 ? 1.5050 1.5349 1.4129 0.2186 -0.3087 0.0622 768 THR A CA 5940 C C . THR A 768 ? 1.4747 1.4575 1.3352 0.2539 -0.2633 0.0478 768 THR A C 5941 O O . THR A 768 ? 1.4906 1.4174 1.2905 0.2717 -0.2616 0.0303 768 THR A O 5942 C CB . THR A 768 ? 1.6172 1.7543 1.5914 0.2265 -0.3067 0.0957 768 THR A CB 5943 O OG1 . THR A 768 ? 1.7048 1.8830 1.7026 0.2090 -0.3533 0.1077 768 THR A OG1 5944 C CG2 . THR A 768 ? 1.5866 1.7829 1.6242 0.2057 -0.2918 0.1189 768 THR A CG2 5945 N N . GLU A 769 ? 1.4348 1.4426 1.3226 0.2633 -0.2288 0.0573 769 GLU A N 5946 C CA . GLU A 769 ? 1.4193 1.3832 1.2694 0.2928 -0.1911 0.0466 769 GLU A CA 5947 C C . GLU A 769 ? 1.4336 1.3971 1.2564 0.3286 -0.1879 0.0506 769 GLU A C 5948 O O . GLU A 769 ? 1.4474 1.3540 1.2229 0.3466 -0.1707 0.0413 769 GLU A O 5949 C CB . GLU A 769 ? 1.3692 1.3652 1.2539 0.2990 -0.1618 0.0557 769 GLU A CB 5950 C CG . GLU A 769 ? 1.3667 1.3637 1.2783 0.2650 -0.1624 0.0561 769 GLU A CG 5951 C CD . GLU A 769 ? 1.4713 1.4960 1.4059 0.2764 -0.1312 0.0633 769 GLU A CD 5952 O OE1 . GLU A 769 ? 1.5930 1.6385 1.5238 0.3125 -0.1124 0.0665 769 GLU A OE1 5953 O OE2 . GLU A 769 ? 1.4540 1.4758 1.4062 0.2519 -0.1277 0.0649 769 GLU A OE2 5954 N N . GLU A 770 ? 1.4723 1.5028 1.3282 0.3377 -0.2062 0.0680 770 GLU A N 5955 C CA . GLU A 770 ? 1.5511 1.5860 1.3843 0.3736 -0.2086 0.0742 770 GLU A CA 5956 C C . GLU A 770 ? 1.6186 1.5953 1.3931 0.3727 -0.2253 0.0624 770 GLU A C 5957 O O . GLU A 770 ? 1.8109 1.7561 1.5452 0.4008 -0.2178 0.0646 770 GLU A O 5958 C CB . GLU A 770 ? 1.6246 1.7554 1.5110 0.3819 -0.2285 0.0967 770 GLU A CB 5959 C CG . GLU A 770 ? 1.6728 1.8161 1.5413 0.4270 -0.2292 0.1052 770 GLU A CG 5960 C CD . GLU A 770 ? 1.6421 1.7743 1.5028 0.4677 -0.1976 0.1052 770 GLU A CD 5961 O OE1 . GLU A 770 ? 1.4472 1.5891 1.3292 0.4622 -0.1761 0.1024 770 GLU A OE1 5962 O OE2 . GLU A 770 ? 1.7889 1.8979 1.6186 0.5065 -0.1974 0.1076 770 GLU A OE2 5963 N N . ASP A 771 ? 1.5231 1.4837 1.2895 0.3420 -0.2497 0.0507 771 ASP A N 5964 C CA . ASP A 771 ? 1.5938 1.5063 1.2994 0.3449 -0.2684 0.0370 771 ASP A CA 5965 C C . ASP A 771 ? 1.6493 1.4912 1.3012 0.3479 -0.2426 0.0207 771 ASP A C 5966 O O . ASP A 771 ? 1.6905 1.4961 1.2845 0.3583 -0.2487 0.0120 771 ASP A O 5967 C CB . ASP A 771 ? 1.7801 1.7023 1.4943 0.3156 -0.3136 0.0283 771 ASP A CB 5968 C CG . ASP A 771 ? 1.9186 1.9228 1.6964 0.3054 -0.3423 0.0501 771 ASP A CG 5969 O OD1 . ASP A 771 ? 2.0375 2.0628 1.8027 0.3183 -0.3682 0.0555 771 ASP A OD1 5970 O OD2 . ASP A 771 ? 1.8287 1.8830 1.6703 0.2848 -0.3387 0.0647 771 ASP A OD2 5971 N N . VAL A 772 ? 1.6467 1.4765 1.3182 0.3404 -0.2138 0.0187 772 VAL A N 5972 C CA . VAL A 772 ? 1.4754 1.2498 1.1067 0.3404 -0.1893 0.0063 772 VAL A CA 5973 C C . VAL A 772 ? 1.3817 1.1377 1.0048 0.3593 -0.1566 0.0182 772 VAL A C 5974 O O . VAL A 772 ? 1.4257 1.1505 1.0043 0.3727 -0.1472 0.0234 772 VAL A O 5975 C CB . VAL A 772 ? 1.3828 1.1474 1.0372 0.3151 -0.1852 -0.0066 772 VAL A CB 5976 C CG1 . VAL A 772 ? 1.4217 1.1389 1.0383 0.3186 -0.1590 -0.0176 772 VAL A CG1 5977 C CG2 . VAL A 772 ? 1.4125 1.1793 1.0712 0.2933 -0.2246 -0.0183 772 VAL A CG2 5978 N N . GLY A 773 ? 1.3031 1.0778 0.9674 0.3603 -0.1419 0.0239 773 GLY A N 5979 C CA . GLY A 773 ? 1.2665 1.0141 0.9226 0.3779 -0.1184 0.0318 773 GLY A CA 5980 C C . GLY A 773 ? 1.2213 0.9890 0.9181 0.3787 -0.1047 0.0305 773 GLY A C 5981 O O . GLY A 773 ? 1.2001 1.0124 0.9355 0.3648 -0.1111 0.0287 773 GLY A O 5982 N N . PRO A 774 ? 1.2090 0.9428 0.8954 0.3947 -0.0884 0.0329 774 PRO A N 5983 C CA . PRO A 774 ? 1.1924 0.9398 0.9063 0.4027 -0.0758 0.0286 774 PRO A CA 5984 C C . PRO A 774 ? 1.1653 0.9127 0.8955 0.3750 -0.0640 0.0180 774 PRO A C 5985 O O . PRO A 774 ? 1.1710 0.9025 0.8892 0.3521 -0.0659 0.0124 774 PRO A O 5986 C CB . PRO A 774 ? 1.2098 0.8976 0.8943 0.4234 -0.0690 0.0304 774 PRO A CB 5987 C CG . PRO A 774 ? 1.2438 0.8859 0.8923 0.4100 -0.0703 0.0380 774 PRO A CG 5988 C CD . PRO A 774 ? 1.1621 0.8400 0.8077 0.4058 -0.0846 0.0416 774 PRO A CD 5989 N N . VAL A 775 ? 1.1527 0.9173 0.9054 0.3817 -0.0527 0.0146 775 VAL A N 5990 C CA . VAL A 775 ? 1.1168 0.8871 0.8875 0.3574 -0.0429 0.0074 775 VAL A CA 5991 C C . VAL A 775 ? 1.1228 0.8411 0.8745 0.3573 -0.0276 -0.0018 775 VAL A C 5992 O O . VAL A 775 ? 1.3085 1.0185 1.0575 0.3794 -0.0220 -0.0048 775 VAL A O 5993 C CB . VAL A 775 ? 1.1655 1.0052 0.9790 0.3605 -0.0412 0.0145 775 VAL A CB 5994 C CG1 . VAL A 775 ? 1.0741 0.9172 0.9052 0.3321 -0.0345 0.0109 775 VAL A CG1 5995 C CG2 . VAL A 775 ? 1.3247 1.2258 1.1656 0.3584 -0.0596 0.0290 775 VAL A CG2 5996 N N . VAL A 776 ? 1.0817 0.7668 0.8190 0.3347 -0.0230 -0.0068 776 VAL A N 5997 C CA . VAL A 776 ? 1.0953 0.7410 0.8226 0.3283 -0.0105 -0.0127 776 VAL A CA 5998 C C . VAL A 776 ? 1.1548 0.8193 0.9040 0.3113 -0.0030 -0.0205 776 VAL A C 5999 O O . VAL A 776 ? 1.0761 0.7532 0.8316 0.2941 -0.0072 -0.0227 776 VAL A O 6000 C CB . VAL A 776 ? 1.1073 0.7151 0.8075 0.3168 -0.0075 -0.0079 776 VAL A CB 6001 C CG1 . VAL A 776 ? 1.0633 0.6406 0.7622 0.3060 0.0030 -0.0098 776 VAL A CG1 6002 C CG2 . VAL A 776 ? 1.1451 0.7323 0.8222 0.3317 -0.0161 0.0050 776 VAL A CG2 6003 N N . GLN A 777 ? 1.1507 0.8120 0.9071 0.3184 0.0049 -0.0255 777 GLN A N 6004 C CA . GLN A 777 ? 1.0950 0.7778 0.8720 0.3052 0.0116 -0.0297 777 GLN A CA 6005 C C . GLN A 777 ? 1.1098 0.7570 0.8773 0.2987 0.0202 -0.0379 777 GLN A C 6006 O O . GLN A 777 ? 1.2010 0.8250 0.9573 0.3135 0.0204 -0.0424 777 GLN A O 6007 C CB . GLN A 777 ? 1.0321 0.7659 0.8312 0.3213 0.0131 -0.0248 777 GLN A CB 6008 C CG . GLN A 777 ? 1.2153 0.9836 1.0405 0.3040 0.0175 -0.0206 777 GLN A CG 6009 C CD . GLN A 777 ? 1.4283 1.2645 1.2788 0.3194 0.0208 -0.0075 777 GLN A CD 6010 O OE1 . GLN A 777 ? 1.3701 1.2260 1.2146 0.3506 0.0222 -0.0065 777 GLN A OE1 6011 N NE2 . GLN A 777 ? 1.5645 1.4398 1.4432 0.2996 0.0217 0.0051 777 GLN A NE2 6012 N N . HIS A 778 ? 0.9674 0.6086 0.7379 0.2783 0.0241 -0.0406 778 HIS A N 6013 C CA . HIS A 778 ? 0.9094 0.5286 0.6776 0.2701 0.0315 -0.0462 778 HIS A CA 6014 C C . HIS A 778 ? 1.0247 0.6666 0.8107 0.2666 0.0354 -0.0501 778 HIS A C 6015 O O . HIS A 778 ? 1.1570 0.8215 0.9569 0.2567 0.0328 -0.0472 778 HIS A O 6016 C CB . HIS A 778 ? 0.9092 0.5154 0.6686 0.2561 0.0352 -0.0451 778 HIS A CB 6017 C CG . HIS A 778 ? 1.0010 0.5874 0.7420 0.2576 0.0346 -0.0355 778 HIS A CG 6018 N ND1 . HIS A 778 ? 1.0081 0.5911 0.7408 0.2485 0.0417 -0.0286 778 HIS A ND1 6019 C CD2 . HIS A 778 ? 1.1566 0.7293 0.8860 0.2682 0.0277 -0.0281 778 HIS A CD2 6020 C CE1 . HIS A 778 ? 1.1053 0.6751 0.8233 0.2499 0.0397 -0.0143 778 HIS A CE1 6021 N NE2 . HIS A 778 ? 1.2039 0.7616 0.9184 0.2616 0.0298 -0.0147 778 HIS A NE2 6022 N N . ILE A 779 ? 1.0991 0.7311 0.8823 0.2743 0.0382 -0.0556 779 ILE A N 6023 C CA . ILE A 779 ? 0.8363 0.4910 0.6318 0.2735 0.0427 -0.0575 779 ILE A CA 6024 C C . ILE A 779 ? 0.8334 0.4649 0.6262 0.2625 0.0450 -0.0640 779 ILE A C 6025 O O . ILE A 779 ? 0.8757 0.4772 0.6565 0.2652 0.0410 -0.0693 779 ILE A O 6026 C CB . ILE A 779 ? 1.0137 0.6880 0.8043 0.2990 0.0434 -0.0597 779 ILE A CB 6027 C CG1 . ILE A 779 ? 1.2668 0.9657 1.0588 0.3162 0.0407 -0.0528 779 ILE A CG1 6028 C CG2 . ILE A 779 ? 0.8315 0.5454 0.6365 0.2981 0.0499 -0.0544 779 ILE A CG2 6029 C CD1 . ILE A 779 ? 1.4403 1.1833 1.2587 0.3009 0.0397 -0.0376 779 ILE A CD1 6030 N N . TYR A 780 ? 1.0023 0.6460 0.8072 0.2495 0.0481 -0.0625 780 TYR A N 6031 C CA . TYR A 780 ? 0.8150 0.4462 0.6210 0.2415 0.0502 -0.0673 780 TYR A CA 6032 C C . TYR A 780 ? 0.8150 0.4642 0.6278 0.2443 0.0516 -0.0676 780 TYR A C 6033 O O . TYR A 780 ? 0.7974 0.4697 0.6211 0.2410 0.0520 -0.0594 780 TYR A O 6034 C CB . TYR A 780 ? 0.8103 0.4380 0.6187 0.2306 0.0522 -0.0664 780 TYR A CB 6035 C CG . TYR A 780 ? 0.9047 0.5206 0.7030 0.2292 0.0537 -0.0634 780 TYR A CG 6036 C CD1 . TYR A 780 ? 1.0287 0.6454 0.8178 0.2317 0.0513 -0.0614 780 TYR A CD1 6037 C CD2 . TYR A 780 ? 0.9459 0.5525 0.7444 0.2235 0.0555 -0.0595 780 TYR A CD2 6038 C CE1 . TYR A 780 ? 1.2340 0.8445 1.0103 0.2323 0.0538 -0.0557 780 TYR A CE1 6039 C CE2 . TYR A 780 ? 0.9983 0.6011 0.7897 0.2199 0.0578 -0.0495 780 TYR A CE2 6040 C CZ . TYR A 780 ? 1.2529 0.8587 1.0310 0.2262 0.0586 -0.0477 780 TYR A CZ 6041 O OH . TYR A 780 ? 1.4306 1.0371 1.1982 0.2245 0.0619 -0.0349 780 TYR A OH 6042 N N . GLU A 781 ? 0.8108 0.4485 0.6167 0.2486 0.0496 -0.0750 781 GLU A N 6043 C CA . GLU A 781 ? 0.8495 0.5044 0.6559 0.2543 0.0505 -0.0756 781 GLU A CA 6044 C C . GLU A 781 ? 1.0050 0.6510 0.8169 0.2440 0.0484 -0.0790 781 GLU A C 6045 O O . GLU A 781 ? 1.0988 0.7245 0.9080 0.2392 0.0423 -0.0850 781 GLU A O 6046 C CB . GLU A 781 ? 0.8502 0.5040 0.6366 0.2767 0.0465 -0.0842 781 GLU A CB 6047 C CG . GLU A 781 ? 1.0227 0.6911 0.8015 0.2857 0.0459 -0.0873 781 GLU A CG 6048 C CD . GLU A 781 ? 1.3897 1.0584 1.1390 0.3166 0.0410 -0.0992 781 GLU A CD 6049 O OE1 . GLU A 781 ? 1.6208 1.2553 1.3523 0.3282 0.0310 -0.1114 781 GLU A OE1 6050 O OE2 . GLU A 781 ? 1.4338 1.1358 1.1743 0.3320 0.0459 -0.0960 781 GLU A OE2 6051 N N . LEU A 782 ? 0.7910 0.4532 0.6126 0.2395 0.0511 -0.0724 782 LEU A N 6052 C CA . LEU A 782 ? 0.7889 0.4494 0.6156 0.2352 0.0487 -0.0748 782 LEU A CA 6053 C C . LEU A 782 ? 0.9343 0.6096 0.7530 0.2449 0.0466 -0.0741 782 LEU A C 6054 O O . LEU A 782 ? 1.2270 0.9227 1.0485 0.2467 0.0499 -0.0618 782 LEU A O 6055 C CB . LEU A 782 ? 0.9782 0.6385 0.8151 0.2285 0.0498 -0.0694 782 LEU A CB 6056 C CG . LEU A 782 ? 0.8395 0.5023 0.6826 0.2290 0.0476 -0.0712 782 LEU A CG 6057 C CD1 . LEU A 782 ? 0.8402 0.5047 0.6893 0.2254 0.0477 -0.0763 782 LEU A CD1 6058 C CD2 . LEU A 782 ? 0.7860 0.4401 0.6311 0.2305 0.0455 -0.0688 782 LEU A CD2 6059 N N . ARG A 783 ? 0.8374 0.5027 0.6451 0.2504 0.0386 -0.0853 783 ARG A N 6060 C CA . ARG A 783 ? 0.8901 0.5685 0.6805 0.2657 0.0350 -0.0882 783 ARG A CA 6061 C C . ARG A 783 ? 0.9559 0.6332 0.7488 0.2618 0.0260 -0.0919 783 ARG A C 6062 O O . ARG A 783 ? 0.9187 0.5796 0.7201 0.2510 0.0162 -0.0990 783 ARG A O 6063 C CB . ARG A 783 ? 0.9375 0.6007 0.7005 0.2847 0.0272 -0.1029 783 ARG A CB 6064 C CG . ARG A 783 ? 1.0170 0.6979 0.7518 0.3099 0.0242 -0.1084 783 ARG A CG 6065 C CD . ARG A 783 ? 1.2279 0.8986 0.9294 0.3395 0.0191 -0.1232 783 ARG A CD 6066 N NE . ARG A 783 ? 1.3042 1.0012 0.9723 0.3715 0.0190 -0.1283 783 ARG A NE 6067 C CZ . ARG A 783 ? 1.2866 1.0428 0.9543 0.3877 0.0378 -0.1092 783 ARG A CZ 6068 N NH1 . ARG A 783 ? 0.9125 0.7010 0.6142 0.3707 0.0537 -0.0847 783 ARG A NH1 6069 N NH2 . ARG A 783 ? 1.3471 1.1333 0.9802 0.4204 0.0388 -0.1125 783 ARG A NH2 6070 N N . ASN A 784 ? 0.9652 0.6651 0.7533 0.2693 0.0285 -0.0831 784 ASN A N 6071 C CA . ASN A 784 ? 0.9397 0.6428 0.7258 0.2704 0.0184 -0.0863 784 ASN A CA 6072 C C . ASN A 784 ? 1.0286 0.7290 0.7817 0.2897 0.0066 -0.1008 784 ASN A C 6073 O O . ASN A 784 ? 1.1071 0.8274 0.8373 0.3097 0.0135 -0.0973 784 ASN A O 6074 C CB . ASN A 784 ? 0.9900 0.7132 0.7845 0.2697 0.0243 -0.0675 784 ASN A CB 6075 C CG . ASN A 784 ? 1.1223 0.8506 0.9160 0.2726 0.0134 -0.0693 784 ASN A CG 6076 O OD1 . ASN A 784 ? 1.1920 0.9116 0.9876 0.2697 0.0010 -0.0836 784 ASN A OD1 6077 N ND2 . ASN A 784 ? 1.1989 0.9417 0.9916 0.2762 0.0154 -0.0520 784 ASN A ND2 6078 N N . ASN A 785 ? 1.0562 0.7345 0.8061 0.2848 -0.0130 -0.1163 785 ASN A N 6079 C CA . ASN A 785 ? 1.2142 0.8757 0.9262 0.3041 -0.0328 -0.1361 785 ASN A CA 6080 C C . ASN A 785 ? 1.4296 1.1044 1.1337 0.3083 -0.0459 -0.1377 785 ASN A C 6081 O O . ASN A 785 ? 1.5432 1.2352 1.2136 0.3334 -0.0457 -0.1397 785 ASN A O 6082 C CB . ASN A 785 ? 1.2654 0.8802 0.9743 0.2937 -0.0554 -0.1534 785 ASN A CB 6083 C CG . ASN A 785 ? 1.3852 0.9804 1.0834 0.3018 -0.0478 -0.1569 785 ASN A CG 6084 O OD1 . ASN A 785 ? 1.4609 1.0398 1.1832 0.2810 -0.0464 -0.1509 785 ASN A OD1 6085 N ND2 . ASN A 785 ? 1.4323 1.0353 1.0935 0.3352 -0.0422 -0.1648 785 ASN A ND2 6086 N N . GLY A 786 ? 1.4769 1.1507 1.2124 0.2858 -0.0570 -0.1349 786 GLY A N 6087 C CA . GLY A 786 ? 1.3297 1.0155 1.0620 0.2878 -0.0746 -0.1374 786 GLY A CA 6088 C C . GLY A 786 ? 1.2652 0.9844 0.9857 0.3049 -0.0606 -0.1227 786 GLY A C 6089 O O . GLY A 786 ? 1.3764 1.1115 1.1055 0.3061 -0.0371 -0.1047 786 GLY A O 6090 N N . PRO A 787 ? 1.2063 0.9344 0.9068 0.3162 -0.0785 -0.1282 787 PRO A N 6091 C CA . PRO A 787 ? 1.2332 0.9912 0.9101 0.3368 -0.0705 -0.1143 787 PRO A CA 6092 C C . PRO A 787 ? 1.1459 0.9254 0.8523 0.3282 -0.0486 -0.0848 787 PRO A C 6093 O O . PRO A 787 ? 1.2277 1.0271 0.9196 0.3390 -0.0327 -0.0654 787 PRO A O 6094 C CB . PRO A 787 ? 1.3463 1.1064 1.0145 0.3397 -0.0989 -0.1249 787 PRO A CB 6095 C CG . PRO A 787 ? 1.3336 1.0576 0.9989 0.3291 -0.1265 -0.1512 787 PRO A CG 6096 C CD . PRO A 787 ? 1.2109 0.9208 0.9131 0.3063 -0.1120 -0.1461 787 PRO A CD 6097 N N . SER A 788 ? 1.0642 0.8402 0.8109 0.3100 -0.0495 -0.0801 788 SER A N 6098 C CA . SER A 788 ? 1.0420 0.8254 0.8099 0.3065 -0.0363 -0.0572 788 SER A CA 6099 C C . SER A 788 ? 0.9994 0.7721 0.7755 0.2986 -0.0172 -0.0471 788 SER A C 6100 O O . SER A 788 ? 1.1244 0.8902 0.8926 0.2968 -0.0115 -0.0570 788 SER A O 6101 C CB . SER A 788 ? 1.1414 0.9282 0.9445 0.2984 -0.0435 -0.0585 788 SER A CB 6102 O OG . SER A 788 ? 1.2605 1.0635 1.0623 0.3028 -0.0641 -0.0660 788 SER A OG 6103 N N . SER A 789 ? 0.9985 0.7658 0.7889 0.2946 -0.0113 -0.0279 789 SER A N 6104 C CA . SER A 789 ? 1.0148 0.7684 0.8143 0.2843 0.0006 -0.0170 789 SER A CA 6105 C C . SER A 789 ? 1.0211 0.7511 0.8418 0.2798 -0.0021 -0.0162 789 SER A C 6106 O O . SER A 789 ? 1.1571 0.8858 0.9824 0.2884 -0.0111 -0.0140 789 SER A O 6107 C CB . SER A 789 ? 1.0885 0.8561 0.8755 0.2847 0.0057 0.0113 789 SER A CB 6108 O OG . SER A 789 ? 1.3159 1.1145 1.0762 0.2988 0.0088 0.0106 789 SER A OG 6109 N N . PHE A 790 ? 0.9232 0.6354 0.7531 0.2707 0.0044 -0.0194 790 PHE A N 6110 C CA . PHE A 790 ? 0.9711 0.6576 0.8115 0.2732 0.0003 -0.0221 790 PHE A CA 6111 C C . PHE A 790 ? 0.9419 0.5971 0.7787 0.2647 -0.0050 -0.0055 790 PHE A C 6112 O O . PHE A 790 ? 0.9174 0.5773 0.7540 0.2513 0.0001 0.0042 790 PHE A O 6113 C CB . PHE A 790 ? 0.9608 0.6501 0.8122 0.2721 0.0077 -0.0408 790 PHE A CB 6114 C CG . PHE A 790 ? 1.0085 0.6936 0.8577 0.2598 0.0163 -0.0438 790 PHE A CG 6115 C CD1 . PHE A 790 ? 1.1239 0.7846 0.9718 0.2551 0.0166 -0.0417 790 PHE A CD1 6116 C CD2 . PHE A 790 ? 1.0376 0.7391 0.8832 0.2555 0.0206 -0.0504 790 PHE A CD2 6117 C CE1 . PHE A 790 ? 0.9687 0.6298 0.8159 0.2452 0.0234 -0.0435 790 PHE A CE1 6118 C CE2 . PHE A 790 ? 1.0174 0.7143 0.8596 0.2487 0.0274 -0.0533 790 PHE A CE2 6119 C CZ . PHE A 790 ? 0.8893 0.5703 0.7345 0.2432 0.0302 -0.0486 790 PHE A CZ 6120 N N . SER A 791 ? 0.9513 0.5738 0.7856 0.2733 -0.0185 -0.0017 791 SER A N 6121 C CA . SER A 791 ? 0.9805 0.5604 0.8102 0.2628 -0.0335 0.0160 791 SER A CA 6122 C C . SER A 791 ? 0.9680 0.5170 0.7966 0.2579 -0.0367 0.0028 791 SER A C 6123 O O . SER A 791 ? 1.0004 0.5293 0.8311 0.2383 -0.0461 0.0182 791 SER A O 6124 C CB . SER A 791 ? 1.1229 0.6659 0.9434 0.2774 -0.0532 0.0233 791 SER A CB 6125 O OG . SER A 791 ? 1.3945 0.9298 1.2116 0.3041 -0.0540 -0.0021 791 SER A OG 6126 N N . LYS A 792 ? 0.9940 0.5446 0.8203 0.2753 -0.0300 -0.0229 792 LYS A N 6127 C CA . LYS A 792 ? 1.0183 0.5428 0.8370 0.2764 -0.0326 -0.0378 792 LYS A CA 6128 C C . LYS A 792 ? 0.9563 0.5171 0.7801 0.2863 -0.0129 -0.0570 792 LYS A C 6129 O O . LYS A 792 ? 0.9713 0.5653 0.8034 0.2995 -0.0040 -0.0626 792 LYS A O 6130 C CB . LYS A 792 ? 1.0089 0.4741 0.8068 0.2959 -0.0560 -0.0464 792 LYS A CB 6131 C CG . LYS A 792 ? 1.1592 0.5688 0.9510 0.2767 -0.0839 -0.0261 792 LYS A CG 6132 C CD . LYS A 792 ? 1.3388 0.6732 1.1018 0.2992 -0.1139 -0.0411 792 LYS A CD 6133 C CE . LYS A 792 ? 1.4025 0.6725 1.1621 0.2727 -0.1493 -0.0172 792 LYS A CE 6134 N NZ . LYS A 792 ? 1.3542 0.5388 1.0800 0.2946 -0.1855 -0.0354 792 LYS A NZ 6135 N N . ALA A 793 ? 0.9068 0.4635 0.7277 0.2777 -0.0081 -0.0635 793 ALA A N 6136 C CA . ALA A 793 ? 0.8944 0.4826 0.7192 0.2839 0.0091 -0.0762 793 ALA A CA 6137 C C . ALA A 793 ? 0.9784 0.5447 0.7886 0.2844 0.0068 -0.0855 793 ALA A C 6138 O O . ALA A 793 ? 1.0390 0.5711 0.8418 0.2723 -0.0078 -0.0810 793 ALA A O 6139 C CB . ALA A 793 ? 0.8608 0.4863 0.7020 0.2673 0.0225 -0.0701 793 ALA A CB 6140 N N . MET A 794 ? 0.9453 0.5359 0.7527 0.2972 0.0201 -0.0954 794 MET A N 6141 C CA . MET A 794 ? 0.9534 0.5280 0.7415 0.3024 0.0189 -0.1050 794 MET A CA 6142 C C . MET A 794 ? 1.0830 0.6874 0.8826 0.2859 0.0345 -0.0993 794 MET A C 6143 O O . MET A 794 ? 1.0896 0.7293 0.9089 0.2778 0.0472 -0.0919 794 MET A O 6144 C CB . MET A 794 ? 0.9381 0.5167 0.7047 0.3377 0.0208 -0.1195 794 MET A CB 6145 C CG . MET A 794 ? 1.0850 0.6212 0.8316 0.3598 -0.0002 -0.1291 794 MET A CG 6146 S SD . MET A 794 ? 1.1801 0.6401 0.9069 0.3414 -0.0344 -0.1314 794 MET A SD 6147 C CE . MET A 794 ? 1.1039 0.5642 0.8028 0.3510 -0.0353 -0.1474 794 MET A CE 6148 N N . LEU A 795 ? 1.1431 0.7282 0.9290 0.2808 0.0294 -0.1027 795 LEU A N 6149 C CA . LEU A 795 ? 0.9045 0.5101 0.6967 0.2682 0.0410 -0.0971 795 LEU A CA 6150 C C . LEU A 795 ? 1.0656 0.6644 0.8330 0.2813 0.0408 -0.1056 795 LEU A C 6151 O O . LEU A 795 ? 1.3831 0.9461 1.1297 0.2861 0.0231 -0.1149 795 LEU A O 6152 C CB . LEU A 795 ? 0.8399 0.4381 0.6436 0.2470 0.0353 -0.0881 795 LEU A CB 6153 C CG . LEU A 795 ? 0.8187 0.4347 0.6291 0.2375 0.0453 -0.0825 795 LEU A CG 6154 C CD1 . LEU A 795 ? 0.9946 0.6325 0.8182 0.2349 0.0559 -0.0789 795 LEU A CD1 6155 C CD2 . LEU A 795 ? 0.8193 0.4345 0.6375 0.2256 0.0391 -0.0746 795 LEU A CD2 6156 N N . HIS A 796 ? 0.9667 0.5994 0.7353 0.2860 0.0576 -0.1004 796 HIS A N 6157 C CA . HIS A 796 ? 1.0215 0.6571 0.7630 0.3018 0.0605 -0.1055 796 HIS A CA 6158 C C . HIS A 796 ? 1.0873 0.7335 0.8339 0.2854 0.0674 -0.0935 796 HIS A C 6159 O O . HIS A 796 ? 1.1260 0.7971 0.8944 0.2715 0.0789 -0.0786 796 HIS A O 6160 C CB . HIS A 796 ? 0.9380 0.6141 0.6720 0.3278 0.0757 -0.1046 796 HIS A CB 6161 C CG . HIS A 796 ? 1.0626 0.7246 0.7818 0.3549 0.0669 -0.1201 796 HIS A CG 6162 N ND1 . HIS A 796 ? 1.1414 0.7744 0.8170 0.3880 0.0545 -0.1407 796 HIS A ND1 6163 C CD2 . HIS A 796 ? 1.0852 0.7527 0.8233 0.3569 0.0655 -0.1192 796 HIS A CD2 6164 C CE1 . HIS A 796 ? 1.0214 0.6422 0.6919 0.4069 0.0448 -0.1507 796 HIS A CE1 6165 N NE2 . HIS A 796 ? 1.1139 0.7548 0.8212 0.3914 0.0530 -0.1378 796 HIS A NE2 6166 N N . LEU A 797 ? 0.9392 0.5616 0.6644 0.2869 0.0563 -0.1000 797 LEU A N 6167 C CA . LEU A 797 ? 0.9016 0.5311 0.6267 0.2763 0.0606 -0.0893 797 LEU A CA 6168 C C . LEU A 797 ? 0.9987 0.6396 0.6911 0.2960 0.0653 -0.0906 797 LEU A C 6169 O O . LEU A 797 ? 1.1481 0.7697 0.8086 0.3162 0.0531 -0.1079 797 LEU A O 6170 C CB . LEU A 797 ? 0.8885 0.4933 0.6188 0.2623 0.0443 -0.0912 797 LEU A CB 6171 C CG . LEU A 797 ? 0.9205 0.5288 0.6460 0.2575 0.0444 -0.0828 797 LEU A CG 6172 C CD1 . LEU A 797 ? 1.0286 0.6527 0.7702 0.2489 0.0587 -0.0675 797 LEU A CD1 6173 C CD2 . LEU A 797 ? 0.8842 0.4813 0.6201 0.2466 0.0281 -0.0830 797 LEU A CD2 6174 N N . GLN A 798 ? 0.9220 0.5916 0.6191 0.2910 0.0804 -0.0715 798 GLN A N 6175 C CA . GLN A 798 ? 1.0269 0.7155 0.6920 0.3090 0.0872 -0.0667 798 GLN A CA 6176 C C . GLN A 798 ? 1.1643 0.8399 0.8246 0.2969 0.0815 -0.0566 798 GLN A C 6177 O O . GLN A 798 ? 1.4499 1.1324 1.1318 0.2783 0.0880 -0.0362 798 GLN A O 6178 C CB . GLN A 798 ? 1.0270 0.7706 0.7011 0.3145 0.1101 -0.0446 798 GLN A CB 6179 C CG . GLN A 798 ? 0.9988 0.7660 0.6808 0.3305 0.1170 -0.0524 798 GLN A CG 6180 C CD . GLN A 798 ? 1.0237 0.8623 0.7105 0.3436 0.1404 -0.0286 798 GLN A CD 6181 O OE1 . GLN A 798 ? 1.0184 0.8881 0.6965 0.3425 0.1516 -0.0060 798 GLN A OE1 6182 N NE2 . GLN A 798 ? 1.1988 1.0700 0.9014 0.3564 0.1480 -0.0301 798 GLN A NE2 6183 N N . TRP A 799 ? 1.0798 0.7325 0.7103 0.3083 0.0655 -0.0715 799 TRP A N 6184 C CA . TRP A 799 ? 1.1103 0.7525 0.7352 0.3004 0.0572 -0.0636 799 TRP A CA 6185 C C . TRP A 799 ? 1.2936 0.9549 0.8801 0.3192 0.0632 -0.0552 799 TRP A C 6186 O O . TRP A 799 ? 1.4275 1.0911 0.9757 0.3450 0.0594 -0.0710 799 TRP A O 6187 C CB . TRP A 799 ? 1.0938 0.7047 0.7185 0.2955 0.0317 -0.0809 799 TRP A CB 6188 C CG . TRP A 799 ? 1.1412 0.7495 0.7765 0.2845 0.0240 -0.0703 799 TRP A CG 6189 C CD1 . TRP A 799 ? 1.1932 0.8000 0.8035 0.2928 0.0131 -0.0691 799 TRP A CD1 6190 C CD2 . TRP A 799 ? 1.1617 0.7708 0.8320 0.2687 0.0258 -0.0604 799 TRP A CD2 6191 N NE1 . TRP A 799 ? 1.1483 0.7568 0.7797 0.2827 0.0083 -0.0577 799 TRP A NE1 6192 C CE2 . TRP A 799 ? 1.1313 0.7410 0.7976 0.2701 0.0163 -0.0532 799 TRP A CE2 6193 C CE3 . TRP A 799 ? 1.1950 0.8053 0.8955 0.2577 0.0333 -0.0583 799 TRP A CE3 6194 C CZ2 . TRP A 799 ? 1.1847 0.7974 0.8755 0.2648 0.0153 -0.0448 799 TRP A CZ2 6195 C CZ3 . TRP A 799 ? 1.2404 0.8514 0.9610 0.2523 0.0317 -0.0512 799 TRP A CZ3 6196 C CH2 . TRP A 799 ? 1.2432 0.8559 0.9586 0.2577 0.0232 -0.0450 799 TRP A CH2 6197 N N . PRO A 800 ? 1.3076 0.9796 0.8996 0.3090 0.0708 -0.0301 800 PRO A N 6198 C CA . PRO A 800 ? 1.3047 0.9976 0.8606 0.3245 0.0766 -0.0154 800 PRO A CA 6199 C C . PRO A 800 ? 1.3747 1.0444 0.8962 0.3385 0.0541 -0.0342 800 PRO A C 6200 O O . PRO A 800 ? 1.4432 1.1022 0.9667 0.3306 0.0450 -0.0238 800 PRO A O 6201 C CB . PRO A 800 ? 1.2597 0.9550 0.8384 0.3031 0.0836 0.0178 800 PRO A CB 6202 C CG . PRO A 800 ? 1.2059 0.8874 0.8289 0.2805 0.0845 0.0183 800 PRO A CG 6203 C CD . PRO A 800 ? 1.2545 0.9162 0.8839 0.2843 0.0726 -0.0134 800 PRO A CD 6204 N N . TYR A 801 ? 1.3900 1.0490 0.8792 0.3599 0.0416 -0.0622 801 TYR A N 6205 C CA . TYR A 801 ? 1.3996 1.0292 0.8582 0.3692 0.0117 -0.0836 801 TYR A CA 6206 C C . TYR A 801 ? 1.4467 1.0910 0.8662 0.3844 0.0106 -0.0714 801 TYR A C 6207 O O . TYR A 801 ? 1.5084 1.1408 0.9345 0.3737 -0.0057 -0.0666 801 TYR A O 6208 C CB . TYR A 801 ? 1.4426 1.0477 0.8655 0.3923 -0.0060 -0.1170 801 TYR A CB 6209 C CG . TYR A 801 ? 1.5378 1.1051 0.9260 0.3998 -0.0449 -0.1407 801 TYR A CG 6210 C CD1 . TYR A 801 ? 1.5534 1.0986 0.9765 0.3706 -0.0703 -0.1409 801 TYR A CD1 6211 C CD2 . TYR A 801 ? 1.7021 1.2597 1.0221 0.4374 -0.0581 -0.1623 801 TYR A CD2 6212 C CE1 . TYR A 801 ? 1.7891 1.3036 1.1869 0.3721 -0.1104 -0.1591 801 TYR A CE1 6213 C CE2 . TYR A 801 ? 1.9776 1.4941 1.2635 0.4425 -0.1004 -0.1858 801 TYR A CE2 6214 C CZ . TYR A 801 ? 2.0791 1.5741 1.4076 0.4065 -0.1277 -0.1828 801 TYR A CZ 6215 O OH . TYR A 801 ? 2.2494 1.7073 1.5503 0.4064 -0.1740 -0.2027 801 TYR A OH 6216 N N . LYS A 802 ? 1.4428 1.1194 0.8215 0.4116 0.0286 -0.0641 802 LYS A N 6217 C CA . LYS A 802 ? 1.4633 1.1590 0.7976 0.4300 0.0289 -0.0502 802 LYS A CA 6218 C C . LYS A 802 ? 1.4575 1.2104 0.7845 0.4387 0.0641 -0.0130 802 LYS A C 6219 O O . LYS A 802 ? 1.5628 1.3472 0.9040 0.4424 0.0863 -0.0061 802 LYS A O 6220 C CB . LYS A 802 ? 1.5225 1.1988 0.7903 0.4657 0.0034 -0.0852 802 LYS A CB 6221 C CG . LYS A 802 ? 1.6742 1.3005 0.9439 0.4529 -0.0389 -0.1101 802 LYS A CG 6222 C CD . LYS A 802 ? 1.7928 1.3957 0.9887 0.4882 -0.0698 -0.1422 802 LYS A CD 6223 C CE . LYS A 802 ? 1.7471 1.3068 0.9510 0.4690 -0.1162 -0.1599 802 LYS A CE 6224 N NZ . LYS A 802 ? 1.8337 1.3632 0.9619 0.5018 -0.1537 -0.1926 802 LYS A NZ 6225 N N . TYR A 803 ? 1.4713 1.2412 0.7784 0.4405 0.0676 0.0148 803 TYR A N 6226 C CA . TYR A 803 ? 1.4535 1.2833 0.7488 0.4479 0.0979 0.0577 803 TYR A CA 6227 C C . TYR A 803 ? 1.4850 1.3347 0.7119 0.4815 0.0935 0.0617 803 TYR A C 6228 O O . TYR A 803 ? 1.5064 1.3297 0.7236 0.4748 0.0747 0.0665 803 TYR A O 6229 C CB . TYR A 803 ? 1.4322 1.2609 0.7809 0.4073 0.1075 0.1015 803 TYR A CB 6230 C CG . TYR A 803 ? 1.4872 1.3759 0.8317 0.4050 0.1341 0.1557 803 TYR A CG 6231 C CD1 . TYR A 803 ? 1.4978 1.3838 0.8310 0.3958 0.1307 0.1928 803 TYR A CD1 6232 C CD2 . TYR A 803 ? 1.6282 1.5807 0.9823 0.4114 0.1618 0.1739 803 TYR A CD2 6233 C CE1 . TYR A 803 ? 1.5200 1.4626 0.8524 0.3889 0.1533 0.2497 803 TYR A CE1 6234 C CE2 . TYR A 803 ? 1.6030 1.6225 0.9601 0.4052 0.1863 0.2313 803 TYR A CE2 6235 C CZ . TYR A 803 ? 1.5383 1.5512 0.8849 0.3917 0.1815 0.2706 803 TYR A CZ 6236 O OH . TYR A 803 ? 1.5769 1.6579 0.9292 0.3810 0.2041 0.3346 803 TYR A OH 6237 N N . ASN A 804 ? 1.5011 1.4011 0.6783 0.5216 0.1106 0.0595 804 ASN A N 6238 C CA . ASN A 804 ? 1.5739 1.4975 0.6737 0.5633 0.1066 0.0581 804 ASN A CA 6239 C C . ASN A 804 ? 1.5990 1.4567 0.6594 0.5761 0.0628 0.0110 804 ASN A C 6240 O O . ASN A 804 ? 1.7326 1.5815 0.7694 0.5763 0.0480 0.0220 804 ASN A O 6241 C CB . ASN A 804 ? 1.7126 1.6775 0.8145 0.5494 0.1245 0.1176 804 ASN A CB 6242 C CG . ASN A 804 ? 1.8061 1.8477 0.9405 0.5379 0.1648 0.1710 804 ASN A CG 6243 O OD1 . ASN A 804 ? 1.8493 1.9303 0.9902 0.5537 0.1835 0.1621 804 ASN A OD1 6244 N ND2 . ASN A 804 ? 1.8433 1.9070 0.9996 0.5097 0.1759 0.2293 804 ASN A ND2 6245 N N . ASN A 805 ? 1.5912 1.4025 0.6492 0.5834 0.0396 -0.0381 805 ASN A N 6246 C CA . ASN A 805 ? 1.7027 1.4517 0.7216 0.5958 -0.0076 -0.0851 805 ASN A CA 6247 C C . ASN A 805 ? 1.8135 1.5194 0.8800 0.5538 -0.0358 -0.0831 805 ASN A C 6248 O O . ASN A 805 ? 1.9575 1.6168 1.0054 0.5551 -0.0780 -0.1167 805 ASN A O 6249 C CB . ASN A 805 ? 1.8638 1.6298 0.7894 0.6464 -0.0178 -0.0961 805 ASN A CB 6250 C CG . ASN A 805 ? 1.8929 1.7043 0.7601 0.7002 0.0062 -0.1056 805 ASN A CG 6251 O OD1 . ASN A 805 ? 1.7453 1.5534 0.6375 0.7032 0.0143 -0.1216 805 ASN A OD1 6252 N ND2 . ASN A 805 ? 1.9319 1.7943 0.7608 0.7321 0.0155 -0.0892 805 ASN A ND2 6253 N N . ASN A 806 ? 1.7596 1.4817 0.8866 0.5182 -0.0155 -0.0437 806 ASN A N 6254 C CA . ASN A 806 ? 1.5660 1.2556 0.7400 0.4849 -0.0386 -0.0414 806 ASN A CA 6255 C C . ASN A 806 ? 1.4798 1.1559 0.7298 0.4483 -0.0287 -0.0364 806 ASN A C 6256 O O . ASN A 806 ? 1.4223 1.1205 0.6986 0.4392 0.0021 -0.0154 806 ASN A O 6257 C CB . ASN A 806 ? 1.5628 1.2712 0.7316 0.4819 -0.0332 -0.0035 806 ASN A CB 6258 C CG . ASN A 806 ? 1.5838 1.3412 0.7275 0.4957 0.0030 0.0360 806 ASN A CG 6259 O OD1 . ASN A 806 ? 1.5513 1.3233 0.7393 0.4715 0.0281 0.0714 806 ASN A OD1 6260 N ND2 . ASN A 806 ? 1.6604 1.4450 0.7316 0.5347 0.0038 0.0321 806 ASN A ND2 6261 N N . THR A 807 ? 1.4713 1.1161 0.7561 0.4278 -0.0564 -0.0538 807 THR A N 6262 C CA . THR A 807 ? 1.4298 1.0625 0.7792 0.3984 -0.0512 -0.0548 807 THR A CA 6263 C C . THR A 807 ? 1.4114 1.0557 0.8044 0.3791 -0.0287 -0.0211 807 THR A C 6264 O O . THR A 807 ? 1.5174 1.1658 0.9058 0.3804 -0.0317 -0.0003 807 THR A O 6265 C CB . THR A 807 ? 1.4295 1.0381 0.8055 0.3819 -0.0871 -0.0753 807 THR A CB 6266 O OG1 . THR A 807 ? 1.4720 1.0584 0.8006 0.3984 -0.1194 -0.1052 807 THR A OG1 6267 C CG2 . THR A 807 ? 1.4101 1.0095 0.8404 0.3580 -0.0821 -0.0806 807 THR A CG2 6268 N N . LEU A 808 ? 1.3829 1.0269 0.8150 0.3628 -0.0101 -0.0171 808 LEU A N 6269 C CA . LEU A 808 ? 1.3432 0.9855 0.8147 0.3444 0.0043 0.0090 808 LEU A CA 6270 C C . LEU A 808 ? 1.3973 1.0236 0.9139 0.3289 -0.0084 -0.0023 808 LEU A C 6271 O O . LEU A 808 ? 1.6635 1.2858 1.1913 0.3289 -0.0206 0.0048 808 LEU A O 6272 C CB . LEU A 808 ? 1.3095 0.9658 0.7944 0.3363 0.0310 0.0239 808 LEU A CB 6273 C CG . LEU A 808 ? 1.3452 1.0351 0.7958 0.3492 0.0503 0.0484 808 LEU A CG 6274 C CD1 . LEU A 808 ? 1.3143 1.0278 0.7912 0.3368 0.0742 0.0648 808 LEU A CD1 6275 C CD2 . LEU A 808 ? 1.4022 1.0908 0.8402 0.3476 0.0487 0.0815 808 LEU A CD2 6276 N N . LEU A 809 ? 1.2709 0.8936 0.8122 0.3187 -0.0048 -0.0182 809 LEU A N 6277 C CA . LEU A 809 ? 1.2375 0.8554 0.8195 0.3057 -0.0152 -0.0272 809 LEU A CA 6278 C C . LEU A 809 ? 1.3503 0.9647 0.9313 0.3028 -0.0363 -0.0499 809 LEU A C 6279 O O . LEU A 809 ? 1.5256 1.1308 1.0979 0.3033 -0.0339 -0.0641 809 LEU A O 6280 C CB . LEU A 809 ? 1.1943 0.8081 0.8078 0.2934 0.0024 -0.0233 809 LEU A CB 6281 C CG . LEU A 809 ? 1.2613 0.8653 0.8843 0.2909 0.0124 -0.0026 809 LEU A CG 6282 C CD1 . LEU A 809 ? 1.3721 0.9688 1.0204 0.2786 0.0248 -0.0027 809 LEU A CD1 6283 C CD2 . LEU A 809 ? 1.2273 0.8282 0.8614 0.2979 -0.0010 0.0008 809 LEU A CD2 6284 N N . TYR A 810 ? 1.2677 0.8887 0.8588 0.2996 -0.0600 -0.0517 810 TYR A N 6285 C CA . TYR A 810 ? 1.2898 0.9029 0.8821 0.2911 -0.0888 -0.0689 810 TYR A CA 6286 C C . TYR A 810 ? 1.2432 0.8663 0.8863 0.2699 -0.0914 -0.0664 810 TYR A C 6287 O O . TYR A 810 ? 1.2131 0.8653 0.8926 0.2638 -0.0911 -0.0519 810 TYR A O 6288 C CB . TYR A 810 ? 1.2434 0.8652 0.8241 0.2944 -0.1177 -0.0681 810 TYR A CB 6289 C CG . TYR A 810 ? 1.2911 0.8982 0.8715 0.2814 -0.1567 -0.0842 810 TYR A CG 6290 C CD1 . TYR A 810 ? 1.3551 0.9256 0.8821 0.2942 -0.1761 -0.1079 810 TYR A CD1 6291 C CD2 . TYR A 810 ? 1.2797 0.9103 0.9117 0.2573 -0.1769 -0.0741 810 TYR A CD2 6292 C CE1 . TYR A 810 ? 1.4635 1.0064 0.9862 0.2810 -0.2201 -0.1243 810 TYR A CE1 6293 C CE2 . TYR A 810 ? 1.3271 0.9410 0.9635 0.2384 -0.2184 -0.0837 810 TYR A CE2 6294 C CZ . TYR A 810 ? 1.4509 1.0136 1.0313 0.2491 -0.2427 -0.1103 810 TYR A CZ 6295 O OH . TYR A 810 ? 1.5035 1.0361 1.0849 0.2289 -0.2919 -0.1214 810 TYR A OH 6296 N N . ILE A 811 ? 1.2985 0.9007 0.9413 0.2624 -0.0938 -0.0792 811 ILE A N 6297 C CA . ILE A 811 ? 1.2310 0.8426 0.9184 0.2422 -0.0947 -0.0736 811 ILE A CA 6298 C C . ILE A 811 ? 1.2840 0.9025 0.9952 0.2214 -0.1307 -0.0701 811 ILE A C 6299 O O . ILE A 811 ? 1.3422 0.9288 1.0266 0.2192 -0.1616 -0.0848 811 ILE A O 6300 C CB . ILE A 811 ? 1.1092 0.6940 0.7877 0.2423 -0.0852 -0.0858 811 ILE A CB 6301 C CG1 . ILE A 811 ? 1.0672 0.6558 0.7320 0.2576 -0.0513 -0.0837 811 ILE A CG1 6302 C CG2 . ILE A 811 ? 1.0648 0.6597 0.7867 0.2211 -0.0877 -0.0768 811 ILE A CG2 6303 C CD1 . ILE A 811 ? 1.0215 0.5953 0.6832 0.2597 -0.0399 -0.0930 811 ILE A CD1 6304 N N . LEU A 812 ? 1.2102 0.8725 0.9712 0.2069 -0.1285 -0.0494 812 LEU A N 6305 C CA . LEU A 812 ? 1.1709 0.8570 0.9681 0.1815 -0.1614 -0.0359 812 LEU A CA 6306 C C . LEU A 812 ? 1.3676 1.0472 1.1934 0.1570 -0.1688 -0.0286 812 LEU A C 6307 O O . LEU A 812 ? 1.4419 1.0788 1.2574 0.1401 -0.2016 -0.0373 812 LEU A O 6308 C CB . LEU A 812 ? 1.2280 0.9831 1.0661 0.1833 -0.1547 -0.0115 812 LEU A CB 6309 C CG . LEU A 812 ? 1.2746 1.0456 1.0993 0.1967 -0.1677 -0.0104 812 LEU A CG 6310 C CD1 . LEU A 812 ? 1.2836 1.0141 1.0530 0.2243 -0.1499 -0.0279 812 LEU A CD1 6311 C CD2 . LEU A 812 ? 1.2926 1.1367 1.1604 0.2050 -0.1571 0.0141 812 LEU A CD2 6312 N N . HIS A 813 ? 1.2978 1.0158 1.1555 0.1573 -0.1405 -0.0128 813 HIS A N 6313 C CA . HIS A 813 ? 1.2989 1.0217 1.1864 0.1352 -0.1435 0.0006 813 HIS A CA 6314 C C . HIS A 813 ? 1.2293 0.9585 1.1149 0.1514 -0.1055 -0.0014 813 HIS A C 6315 O O . HIS A 813 ? 1.2613 1.0186 1.1459 0.1729 -0.0796 -0.0002 813 HIS A O 6316 C CB . HIS A 813 ? 1.4036 1.1947 1.3489 0.1100 -0.1586 0.0356 813 HIS A CB 6317 C CG . HIS A 813 ? 1.4633 1.2704 1.4429 0.0857 -0.1599 0.0580 813 HIS A CG 6318 N ND1 . HIS A 813 ? 1.6507 1.3958 1.6197 0.0640 -0.1858 0.0520 813 HIS A ND1 6319 C CD2 . HIS A 813 ? 1.3821 1.2605 1.4029 0.0825 -0.1391 0.0877 813 HIS A CD2 6320 C CE1 . HIS A 813 ? 1.7087 1.4848 1.7138 0.0444 -0.1814 0.0800 813 HIS A CE1 6321 N NE2 . HIS A 813 ? 1.5615 1.4228 1.5982 0.0555 -0.1517 0.1026 813 HIS A NE2 6322 N N . TYR A 814 ? 1.2046 0.9021 1.0869 0.1422 -0.1061 -0.0055 814 TYR A N 6323 C CA . TYR A 814 ? 1.1360 0.8405 1.0184 0.1545 -0.0752 -0.0065 814 TYR A CA 6324 C C . TYR A 814 ? 1.1304 0.8591 1.0471 0.1336 -0.0791 0.0167 814 TYR A C 6325 O O . TYR A 814 ? 1.1728 0.8759 1.0980 0.1092 -0.1078 0.0241 814 TYR A O 6326 C CB . TYR A 814 ? 1.0972 0.7465 0.9393 0.1698 -0.0662 -0.0328 814 TYR A CB 6327 C CG . TYR A 814 ? 1.1856 0.7839 1.0131 0.1594 -0.0905 -0.0427 814 TYR A CG 6328 C CD1 . TYR A 814 ? 1.2538 0.8106 1.0538 0.1592 -0.1199 -0.0580 814 TYR A CD1 6329 C CD2 . TYR A 814 ? 1.2411 0.8277 1.0770 0.1536 -0.0868 -0.0388 814 TYR A CD2 6330 C CE1 . TYR A 814 ? 1.3008 0.7999 1.0796 0.1557 -0.1469 -0.0712 814 TYR A CE1 6331 C CE2 . TYR A 814 ? 1.2130 0.7450 1.0319 0.1483 -0.1121 -0.0487 814 TYR A CE2 6332 C CZ . TYR A 814 ? 1.2164 0.7018 1.0055 0.1505 -0.1430 -0.0661 814 TYR A CZ 6333 O OH . TYR A 814 ? 1.2188 0.6393 0.9834 0.1509 -0.1730 -0.0800 814 TYR A OH 6334 N N . ASP A 815 ? 1.0979 0.8729 1.0309 0.1441 -0.0530 0.0290 815 ASP A N 6335 C CA . ASP A 815 ? 1.1830 0.9907 1.1457 0.1278 -0.0523 0.0549 815 ASP A CA 6336 C C . ASP A 815 ? 1.0915 0.8766 1.0353 0.1413 -0.0322 0.0428 815 ASP A C 6337 O O . ASP A 815 ? 1.0393 0.7904 0.9528 0.1614 -0.0188 0.0167 815 ASP A O 6338 C CB . ASP A 815 ? 1.3070 1.2039 1.3054 0.1316 -0.0403 0.0846 815 ASP A CB 6339 C CG . ASP A 815 ? 1.4063 1.3387 1.4334 0.1143 -0.0630 0.1030 815 ASP A CG 6340 O OD1 . ASP A 815 ? 1.4868 1.4386 1.5489 0.0795 -0.0876 0.1321 815 ASP A OD1 6341 O OD2 . ASP A 815 ? 1.3487 1.2887 1.3645 0.1337 -0.0591 0.0905 815 ASP A OD2 6342 N N . ILE A 816 ? 1.0628 0.8716 1.0269 0.1284 -0.0316 0.0657 816 ILE A N 6343 C CA . ILE A 816 ? 1.0269 0.8141 0.9745 0.1385 -0.0178 0.0566 816 ILE A CA 6344 C C . ILE A 816 ? 1.0362 0.8876 1.0029 0.1424 -0.0012 0.0830 816 ILE A C 6345 O O . ILE A 816 ? 1.1317 1.0283 1.1310 0.1209 -0.0103 0.1188 816 ILE A O 6346 C CB . ILE A 816 ? 0.9671 0.6925 0.9065 0.1209 -0.0406 0.0528 816 ILE A CB 6347 C CG1 . ILE A 816 ? 1.0505 0.7141 0.9611 0.1264 -0.0555 0.0228 816 ILE A CG1 6348 C CG2 . ILE A 816 ? 0.9532 0.6652 0.8794 0.1324 -0.0268 0.0467 816 ILE A CG2 6349 C CD1 . ILE A 816 ? 1.2480 0.8468 1.1454 0.1146 -0.0849 0.0170 816 ILE A CD1 6350 N N . ASP A 817 ? 0.9870 0.8442 0.9323 0.1696 0.0211 0.0672 817 ASP A N 6351 C CA . ASP A 817 ? 0.9908 0.9024 0.9416 0.1807 0.0368 0.0865 817 ASP A CA 6352 C C . ASP A 817 ? 0.9789 0.8540 0.9126 0.1813 0.0379 0.0779 817 ASP A C 6353 O O . ASP A 817 ? 0.9490 0.7788 0.8573 0.1949 0.0417 0.0474 817 ASP A O 6354 C CB . ASP A 817 ? 1.0990 1.0471 1.0330 0.2173 0.0567 0.0739 817 ASP A CB 6355 C CG . ASP A 817 ? 1.2817 1.3203 1.2404 0.2257 0.0654 0.1056 817 ASP A CG 6356 O OD1 . ASP A 817 ? 1.1476 1.2116 1.0985 0.2528 0.0735 0.0962 817 ASP A OD1 6357 O OD2 . ASP A 817 ? 1.5299 1.6175 1.5166 0.2062 0.0636 0.1428 817 ASP A OD2 6358 N N . GLY A 818 ? 1.0039 0.9027 0.9543 0.1650 0.0332 0.1086 818 GLY A N 6359 C CA . GLY A 818 ? 0.9952 0.8631 0.9308 0.1661 0.0322 0.1047 818 GLY A CA 6360 C C . GLY A 818 ? 1.0158 0.8227 0.9570 0.1403 0.0071 0.1083 818 GLY A C 6361 O O . GLY A 818 ? 1.0249 0.8132 0.9813 0.1186 -0.0126 0.1160 818 GLY A O 6362 N N . PRO A 819 ? 1.0891 0.8616 1.0148 0.1453 0.0045 0.1010 819 PRO A N 6363 C CA . PRO A 819 ? 1.0696 0.7783 0.9933 0.1295 -0.0210 0.1022 819 PRO A CA 6364 C C . PRO A 819 ? 1.0206 0.6684 0.9236 0.1402 -0.0291 0.0638 819 PRO A C 6365 O O . PRO A 819 ? 0.9997 0.6202 0.8836 0.1584 -0.0248 0.0415 819 PRO A O 6366 C CB . PRO A 819 ? 1.0686 0.7774 0.9811 0.1400 -0.0156 0.1078 819 PRO A CB 6367 C CG . PRO A 819 ? 0.9749 0.7187 0.8719 0.1673 0.0103 0.0861 819 PRO A CG 6368 C CD . PRO A 819 ? 1.0900 0.8820 0.9964 0.1699 0.0230 0.0901 819 PRO A CD 6369 N N . MET A 820 ? 1.0377 0.6719 0.9447 0.1306 -0.0407 0.0582 820 MET A N 6370 C CA . MET A 820 ? 1.0301 0.6138 0.9131 0.1439 -0.0475 0.0243 820 MET A CA 6371 C C . MET A 820 ? 1.0872 0.6329 0.9706 0.1264 -0.0779 0.0256 820 MET A C 6372 O O . MET A 820 ? 1.1194 0.6964 1.0267 0.1055 -0.0850 0.0473 820 MET A O 6373 C CB . MET A 820 ? 0.8937 0.5052 0.7682 0.1629 -0.0221 0.0034 820 MET A CB 6374 C CG . MET A 820 ? 0.8738 0.4487 0.7235 0.1799 -0.0223 -0.0267 820 MET A CG 6375 S SD . MET A 820 ? 1.4010 1.0046 1.2456 0.1921 0.0000 -0.0403 820 MET A SD 6376 C CE . MET A 820 ? 0.8108 0.4481 0.6612 0.2013 0.0214 -0.0382 820 MET A CE 6377 N N . ASN A 821 ? 1.1097 0.5900 0.9648 0.1377 -0.0975 0.0017 821 ASN A N 6378 C CA . ASN A 821 ? 1.1695 0.6021 1.0115 0.1293 -0.1296 -0.0080 821 ASN A CA 6379 C C . ASN A 821 ? 1.1305 0.5528 0.9404 0.1585 -0.1174 -0.0432 821 ASN A C 6380 O O . ASN A 821 ? 1.0995 0.5226 0.8912 0.1855 -0.0974 -0.0618 821 ASN A O 6381 C CB . ASN A 821 ? 1.3661 0.7210 1.1919 0.1231 -0.1699 -0.0083 821 ASN A CB 6382 C CG . ASN A 821 ? 1.6006 0.9624 1.4614 0.0855 -0.1894 0.0352 821 ASN A CG 6383 O OD1 . ASN A 821 ? 1.5561 0.9854 1.4547 0.0618 -0.1771 0.0667 821 ASN A OD1 6384 N ND2 . ASN A 821 ? 2.0151 1.3095 1.8626 0.0818 -0.2207 0.0395 821 ASN A ND2 6385 N N . CYS A 822 ? 1.1488 0.5678 0.9536 0.1526 -0.1297 -0.0489 822 CYS A N 6386 C CA . CYS A 822 ? 1.0888 0.5059 0.8624 0.1796 -0.1167 -0.0768 822 CYS A CA 6387 C C . CYS A 822 ? 1.1412 0.5004 0.8801 0.1854 -0.1526 -0.0969 822 CYS A C 6388 O O . CYS A 822 ? 1.2161 0.5467 0.9651 0.1592 -0.1889 -0.0855 822 CYS A O 6389 C CB . CYS A 822 ? 1.0509 0.5285 0.8439 0.1760 -0.0902 -0.0677 822 CYS A CB 6390 S SG . CYS A 822 ? 1.5702 1.1039 1.3866 0.1810 -0.0505 -0.0560 822 CYS A SG 6391 N N . THR A 823 ? 1.2203 0.5655 0.9178 0.2200 -0.1437 -0.1252 823 THR A N 6392 C CA . THR A 823 ? 1.3005 0.5899 0.9516 0.2367 -0.1764 -0.1507 823 THR A CA 6393 C C . THR A 823 ? 1.3163 0.6364 0.9394 0.2637 -0.1530 -0.1661 823 THR A C 6394 O O . THR A 823 ? 1.2963 0.6578 0.9187 0.2837 -0.1158 -0.1669 823 THR A O 6395 C CB . THR A 823 ? 1.2604 0.4826 0.8707 0.2648 -0.1994 -0.1742 823 THR A CB 6396 O OG1 . THR A 823 ? 1.6056 0.8007 1.2434 0.2393 -0.2182 -0.1548 823 THR A OG1 6397 C CG2 . THR A 823 ? 1.3486 0.5096 0.9085 0.2795 -0.2413 -0.2007 823 THR A CG2 6398 N N . SER A 824 ? 1.2153 0.5169 0.8168 0.2620 -0.1770 -0.1751 824 SER A N 6399 C CA . SER A 824 ? 1.2141 0.5427 0.7844 0.2876 -0.1583 -0.1868 824 SER A CA 6400 C C . SER A 824 ? 1.3581 0.6347 0.8594 0.3277 -0.1823 -0.2212 824 SER A C 6401 O O . SER A 824 ? 1.5635 0.7736 1.0401 0.3239 -0.2301 -0.2367 824 SER A O 6402 C CB . SER A 824 ? 1.2912 0.6465 0.8828 0.2630 -0.1646 -0.1717 824 SER A CB 6403 O OG . SER A 824 ? 1.4843 0.8621 1.0428 0.2876 -0.1490 -0.1804 824 SER A OG 6404 N N . ASP A 825 ? 1.3418 0.6513 0.8116 0.3665 -0.1511 -0.2313 825 ASP A N 6405 C CA . ASP A 825 ? 1.4673 0.7691 0.8828 0.4015 -0.1645 -0.2524 825 ASP A CA 6406 C C . ASP A 825 ? 1.5289 0.8047 0.9031 0.4088 -0.1918 -0.2670 825 ASP A C 6407 O O . ASP A 825 ? 1.6431 0.8882 0.9689 0.4320 -0.2217 -0.2876 825 ASP A O 6408 C CB . ASP A 825 ? 1.5199 0.8898 0.9258 0.4344 -0.1200 -0.2473 825 ASP A CB 6409 C CG . ASP A 825 ? 1.6336 1.0540 1.0424 0.4381 -0.0853 -0.2332 825 ASP A CG 6410 O OD1 . ASP A 825 ? 1.7886 1.2041 1.2252 0.4083 -0.0868 -0.2210 825 ASP A OD1 6411 O OD2 . ASP A 825 ? 1.6165 1.0890 1.0041 0.4684 -0.0568 -0.2290 825 ASP A OD2 6412 N N . MET A 826 ? 1.3972 0.6913 0.7929 0.3886 -0.1824 -0.2536 826 MET A N 6413 C CA . MET A 826 ? 1.4572 0.7369 0.8264 0.3859 -0.2103 -0.2608 826 MET A CA 6414 C C . MET A 826 ? 1.4758 0.7451 0.8990 0.3336 -0.2390 -0.2417 826 MET A C 6415 O O . MET A 826 ? 1.4663 0.7717 0.9517 0.3019 -0.2178 -0.2141 826 MET A O 6416 C CB . MET A 826 ? 1.4392 0.7844 0.8004 0.3998 -0.1726 -0.2467 826 MET A CB 6417 C CG . MET A 826 ? 1.6399 1.0196 0.9606 0.4464 -0.1370 -0.2532 826 MET A CG 6418 S SD . MET A 826 ? 1.6281 1.0767 0.9323 0.4598 -0.1026 -0.2317 826 MET A SD 6419 C CE . MET A 826 ? 1.7465 1.1468 0.9844 0.4779 -0.1514 -0.2597 826 MET A CE 6420 N N . GLU A 827 ? 1.6417 0.8662 1.0404 0.3259 -0.2883 -0.2552 827 GLU A N 6421 C CA . GLU A 827 ? 1.6704 0.8951 1.1241 0.2750 -0.3193 -0.2328 827 GLU A CA 6422 C C . GLU A 827 ? 1.5603 0.8656 1.0641 0.2558 -0.2853 -0.2013 827 GLU A C 6423 O O . GLU A 827 ? 1.6238 0.9562 1.1010 0.2761 -0.2714 -0.2043 827 GLU A O 6424 C CB . GLU A 827 ? 1.8537 1.0154 1.2690 0.2706 -0.3839 -0.2539 827 GLU A CB 6425 C CG . GLU A 827 ? 1.9084 1.0859 1.3865 0.2155 -0.4176 -0.2249 827 GLU A CG 6426 C CD . GLU A 827 ? 2.1162 1.2406 1.5578 0.2097 -0.4825 -0.2441 827 GLU A CD 6427 O OE1 . GLU A 827 ? 2.1916 1.3278 1.6858 0.1620 -0.5185 -0.2193 827 GLU A OE1 6428 O OE2 . GLU A 827 ? 2.2401 1.3157 1.6003 0.2538 -0.4985 -0.2829 827 GLU A OE2 6429 N N . ILE A 828 ? 1.4639 0.8067 1.0362 0.2202 -0.2729 -0.1706 828 ILE A N 6430 C CA . ILE A 828 ? 1.3930 0.8073 1.0113 0.2058 -0.2466 -0.1425 828 ILE A CA 6431 C C . ILE A 828 ? 1.4617 0.8835 1.0949 0.1834 -0.2869 -0.1340 828 ILE A C 6432 O O . ILE A 828 ? 1.6125 0.9976 1.2553 0.1574 -0.3342 -0.1341 828 ILE A O 6433 C CB . ILE A 828 ? 1.3138 0.7712 0.9941 0.1828 -0.2196 -0.1143 828 ILE A CB 6434 C CG1 . ILE A 828 ? 1.5833 1.0173 1.2967 0.1480 -0.2553 -0.1018 828 ILE A CG1 6435 C CG2 . ILE A 828 ? 1.2127 0.6728 0.8812 0.2050 -0.1781 -0.1208 828 ILE A CG2 6436 C CD1 . ILE A 828 ? 1.5333 1.0194 1.3060 0.1265 -0.2304 -0.0703 828 ILE A CD1 6437 N N . ASN A 829 ? 1.4623 0.9303 1.0981 0.1927 -0.2712 -0.1248 829 ASN A N 6438 C CA . ASN A 829 ? 1.5456 1.0302 1.1936 0.1768 -0.3074 -0.1167 829 ASN A CA 6439 C C . ASN A 829 ? 1.6603 1.0771 1.2563 0.1796 -0.3629 -0.1450 829 ASN A C 6440 O O . ASN A 829 ? 1.9163 1.3112 1.5374 0.1457 -0.4115 -0.1388 829 ASN A O 6441 C CB . ASN A 829 ? 1.5324 1.0666 1.2583 0.1356 -0.3191 -0.0819 829 ASN A CB 6442 C CG . ASN A 829 ? 1.5298 1.1455 1.2971 0.1401 -0.2851 -0.0554 829 ASN A CG 6443 O OD1 . ASN A 829 ? 1.4727 1.1012 1.2126 0.1659 -0.2705 -0.0614 829 ASN A OD1 6444 N ND2 . ASN A 829 ? 1.6263 1.2975 1.4567 0.1181 -0.2736 -0.0252 829 ASN A ND2 6445 N N . PRO A 830 ? 1.6757 1.0594 1.1975 0.2204 -0.3584 -0.1748 830 PRO A N 6446 C CA . PRO A 830 ? 1.9010 1.2190 1.3617 0.2314 -0.4139 -0.2063 830 PRO A CA 6447 C C . PRO A 830 ? 1.9449 1.2854 1.4208 0.2120 -0.4524 -0.1961 830 PRO A C 6448 O O . PRO A 830 ? 2.0335 1.3233 1.4938 0.1953 -0.5146 -0.2103 830 PRO A O 6449 C CB . PRO A 830 ? 1.9492 1.2533 1.3301 0.2864 -0.3863 -0.2333 830 PRO A CB 6450 C CG . PRO A 830 ? 1.7625 1.1384 1.1732 0.2939 -0.3237 -0.2065 830 PRO A CG 6451 C CD . PRO A 830 ? 1.6309 1.0361 1.1197 0.2583 -0.3051 -0.1794 830 PRO A CD 6452 N N . LEU A 831 ? 1.8148 1.2280 1.3202 0.2147 -0.4190 -0.1716 831 LEU A N 6453 C CA . LEU A 831 ? 1.8294 1.2792 1.3566 0.1994 -0.4496 -0.1572 831 LEU A CA 6454 C C . LEU A 831 ? 1.8166 1.3264 1.4388 0.1540 -0.4541 -0.1183 831 LEU A C 6455 O O . LEU A 831 ? 1.8322 1.3929 1.4922 0.1373 -0.4750 -0.0976 831 LEU A O 6456 C CB . LEU A 831 ? 1.7786 1.2729 1.2813 0.2326 -0.4129 -0.1508 831 LEU A CB 6457 C CG . LEU A 831 ? 1.7761 1.2399 1.1996 0.2790 -0.3828 -0.1747 831 LEU A CG 6458 C CD1 . LEU A 831 ? 1.7364 1.2489 1.1490 0.3030 -0.3449 -0.1568 831 LEU A CD1 6459 C CD2 . LEU A 831 ? 2.1264 1.5235 1.4699 0.3006 -0.4297 -0.2134 831 LEU A CD2 6460 N N . ARG A 832 ? 1.9086 1.4176 1.5676 0.1372 -0.4335 -0.1072 832 ARG A N 6461 C CA . ARG A 832 ? 1.9031 1.4808 1.6487 0.1028 -0.4214 -0.0671 832 ARG A CA 6462 C C . ARG A 832 ? 1.8398 1.5029 1.6186 0.1184 -0.3802 -0.0431 832 ARG A C 6463 O O . ARG A 832 ? 1.9511 1.6111 1.6893 0.1549 -0.3446 -0.0554 832 ARG A O 6464 C CB . ARG A 832 ? 1.8719 1.4551 1.6645 0.0545 -0.4828 -0.0479 832 ARG A CB 6465 C CG . ARG A 832 ? 1.9135 1.4021 1.6788 0.0338 -0.5322 -0.0679 832 ARG A CG 6466 C CD . ARG A 832 ? 2.0180 1.4288 1.7095 0.0489 -0.5859 -0.1069 832 ARG A CD 6467 N NE . ARG A 832 ? 2.2639 1.5721 1.9223 0.0338 -0.6394 -0.1298 832 ARG A NE 6468 C CZ . ARG A 832 ? 2.3502 1.5732 1.9422 0.0431 -0.7003 -0.1663 832 ARG A CZ 6469 N NH1 . ARG A 832 ? 2.3105 1.5460 1.8635 0.0658 -0.7133 -0.1822 832 ARG A NH1 6470 N NH2 . ARG A 832 ? 2.3862 1.5072 1.9463 0.0321 -0.7510 -0.1879 832 ARG A NH2 6471 N N . ILE A 833 ? 1.6638 1.4028 1.5148 0.0915 -0.3891 -0.0074 833 ILE A N 6472 C CA . ILE A 833 ? 1.6045 1.4285 1.4930 0.1093 -0.3509 0.0172 833 ILE A CA 6473 C C . ILE A 833 ? 1.5922 1.5039 1.5658 0.0749 -0.3669 0.0591 833 ILE A C 6474 O O . ILE A 833 ? 1.6075 1.5083 1.6114 0.0337 -0.4023 0.0713 833 ILE A O 6475 C CB . ILE A 833 ? 1.8820 1.7032 1.7582 0.1368 -0.2921 0.0127 833 ILE A CB 6476 C CG1 . ILE A 833 ? 1.8979 1.7316 1.7438 0.1771 -0.2613 0.0076 833 ILE A CG1 6477 C CG2 . ILE A 833 ? 1.8696 1.7487 1.8082 0.1200 -0.2712 0.0414 833 ILE A CG2 6478 C CD1 . ILE A 833 ? 1.9991 1.9140 1.8879 0.1854 -0.2604 0.0337 833 ILE A CD1 6479 N N . LYS A 834 ? 1.5721 1.5721 1.5841 0.0922 -0.3430 0.0834 834 LYS A N 6480 C CA . LYS A 834 ? 1.6066 1.7091 1.7017 0.0679 -0.3447 0.1276 834 LYS A CA 6481 C C . LYS A 834 ? 1.6616 1.8023 1.7744 0.0877 -0.2917 0.1391 834 LYS A C 6482 O O . LYS A 834 ? 1.5659 1.7001 1.6990 0.0635 -0.2876 0.1496 834 LYS A O 6483 C CB . LYS A 834 ? 1.6126 1.8036 1.7438 0.0779 -0.3571 0.1501 834 LYS A CB 6484 C CG . LYS A 834 ? 1.6662 1.8530 1.8113 0.0416 -0.4207 0.1553 834 LYS A CG 6485 C CD . LYS A 834 ? 1.5585 1.7659 1.7644 -0.0181 -0.4576 0.1858 834 LYS A CD 6486 C CE . LYS A 834 ? 1.5506 1.7509 1.7737 -0.0585 -0.5290 0.1925 834 LYS A CE 6487 N NZ . LYS A 834 ? 1.5963 1.6694 1.7301 -0.0474 -0.5603 0.1408 834 LYS A NZ 6488 N N . ILE A 835 ? 1.7499 1.9223 1.8492 0.1335 -0.2545 0.1353 835 ILE A N 6489 C CA . ILE A 835 ? 1.6732 1.8717 1.7765 0.1609 -0.2072 0.1393 835 ILE A CA 6490 C C . ILE A 835 ? 1.5928 1.7989 1.6664 0.2137 -0.1796 0.1278 835 ILE A C 6491 O O . ILE A 835 ? 1.5373 1.7653 1.6088 0.2280 -0.1949 0.1303 835 ILE A O 6492 C CB . ILE A 835 ? 1.6152 1.9227 1.7912 0.1453 -0.2005 0.1820 835 ILE A CB 6493 C CG1 . ILE A 835 ? 1.4327 1.7552 1.5997 0.1775 -0.1538 0.1798 835 ILE A CG1 6494 C CG2 . ILE A 835 ? 1.6817 2.0979 1.9075 0.1541 -0.2121 0.2126 835 ILE A CG2 6495 C CD1 . ILE A 835 ? 1.3902 1.8267 1.6211 0.1694 -0.1415 0.2228 835 ILE A CD1 6496 N N . ASP A 868 ? 2.2261 1.5148 1.9113 -0.0887 -0.1241 0.7178 868 ASP A N 6497 C CA . ASP A 868 ? 2.2061 1.5995 1.9217 -0.0856 -0.0855 0.6936 868 ASP A CA 6498 C C . ASP A 868 ? 2.0986 1.5131 1.7812 -0.0258 -0.0590 0.6153 868 ASP A C 6499 O O . ASP A 868 ? 2.0994 1.5003 1.7379 0.0126 -0.0544 0.5976 868 ASP A O 6500 C CB . ASP A 868 ? 2.3287 1.8583 2.0657 -0.1053 -0.0468 0.7599 868 ASP A CB 6501 C CG . ASP A 868 ? 2.4799 2.0621 2.1673 -0.0672 -0.0189 0.7740 868 ASP A CG 6502 O OD1 . ASP A 868 ? 2.5594 2.0587 2.2065 -0.0482 -0.0419 0.7658 868 ASP A OD1 6503 O OD2 . ASP A 868 ? 2.4991 2.2061 2.1849 -0.0526 0.0247 0.7921 868 ASP A OD2 6504 N N . ILE A 869 ? 2.0261 1.4745 1.7326 -0.0204 -0.0444 0.5716 869 ILE A N 6505 C CA . ILE A 869 ? 1.9283 1.3941 1.6105 0.0290 -0.0235 0.5010 869 ILE A CA 6506 C C . ILE A 869 ? 1.9269 1.5103 1.6210 0.0406 0.0197 0.4945 869 ILE A C 6507 O O . ILE A 869 ? 2.0071 1.6419 1.7424 0.0120 0.0285 0.5171 869 ILE A O 6508 C CB . ILE A 869 ? 1.8372 1.2225 1.5269 0.0359 -0.0488 0.4440 869 ILE A CB 6509 C CG1 . ILE A 869 ? 1.6503 1.0672 1.3240 0.0797 -0.0257 0.3798 869 ILE A CG1 6510 C CG2 . ILE A 869 ? 1.9703 1.3534 1.7068 -0.0064 -0.0619 0.4579 869 ILE A CG2 6511 C CD1 . ILE A 869 ? 1.5947 0.9397 1.2674 0.0948 -0.0478 0.3268 869 ILE A CD1 6512 N N . HIS A 870 ? 1.8051 1.4290 1.4616 0.0842 0.0434 0.4636 870 HIS A N 6513 C CA . HIS A 870 ? 1.7317 1.4552 1.3865 0.1051 0.0803 0.4513 870 HIS A CA 6514 C C . HIS A 870 ? 1.5722 1.2825 1.2308 0.1275 0.0829 0.3837 870 HIS A C 6515 O O . HIS A 870 ? 1.5171 1.1797 1.1508 0.1534 0.0723 0.3393 870 HIS A O 6516 C CB . HIS A 870 ? 1.8485 1.6226 1.4535 0.1402 0.1004 0.4590 870 HIS A CB 6517 C CG . HIS A 870 ? 1.9757 1.8555 1.5717 0.1633 0.1364 0.4592 870 HIS A CG 6518 N ND1 . HIS A 870 ? 2.0142 1.9429 1.5572 0.2040 0.1543 0.4536 870 HIS A ND1 6519 C CD2 . HIS A 870 ? 1.9031 1.8484 1.5323 0.1562 0.1557 0.4627 870 HIS A CD2 6520 C CE1 . HIS A 870 ? 1.8708 1.8870 1.4107 0.2244 0.1832 0.4515 870 HIS A CE1 6521 N NE2 . HIS A 870 ? 1.7903 1.8213 1.3843 0.1962 0.1858 0.4581 870 HIS A NE2 6522 N N . THR A 871 ? 1.5396 1.2975 1.2319 0.1165 0.0965 0.3804 871 THR A N 6523 C CA . THR A 871 ? 1.4241 1.1715 1.1231 0.1338 0.0985 0.3231 871 THR A CA 6524 C C . THR A 871 ? 1.3783 1.1842 1.0463 0.1746 0.1237 0.2935 871 THR A C 6525 O O . THR A 871 ? 1.4007 1.2862 1.0623 0.1845 0.1479 0.3187 871 THR A O 6526 C CB . THR A 871 ? 1.4107 1.1761 1.1595 0.1043 0.0970 0.3311 871 THR A CB 6527 O OG1 . THR A 871 ? 1.6155 1.3192 1.3896 0.0645 0.0670 0.3591 871 THR A OG1 6528 C CG2 . THR A 871 ? 1.3265 1.0715 1.0798 0.1216 0.0958 0.2738 871 THR A CG2 6529 N N . LEU A 872 ? 1.3301 1.0969 0.9776 0.1995 0.1157 0.2413 872 LEU A N 6530 C CA . LEU A 872 ? 1.3236 1.1270 0.9408 0.2358 0.1301 0.2077 872 LEU A CA 6531 C C . LEU A 872 ? 1.4241 1.2187 1.0626 0.2389 0.1291 0.1682 872 LEU A C 6532 O O . LEU A 872 ? 1.3998 1.1410 1.0449 0.2370 0.1122 0.1372 872 LEU A O 6533 C CB . LEU A 872 ? 1.3027 1.0736 0.8771 0.2606 0.1179 0.1837 872 LEU A CB 6534 C CG . LEU A 872 ? 1.3436 1.1278 0.8861 0.2663 0.1193 0.2192 872 LEU A CG 6535 C CD1 . LEU A 872 ? 1.3177 1.0710 0.8207 0.2917 0.1034 0.1904 872 LEU A CD1 6536 C CD2 . LEU A 872 ? 1.3924 1.2586 0.9157 0.2805 0.1459 0.2485 872 LEU A CD2 6537 N N . GLY A 873 ? 1.4803 1.3333 1.1289 0.2461 0.1479 0.1721 873 GLY A N 6538 C CA . GLY A 873 ? 1.3850 1.2339 1.0510 0.2518 0.1476 0.1382 873 GLY A CA 6539 C C . GLY A 873 ? 1.4492 1.3158 1.0755 0.2926 0.1541 0.1045 873 GLY A C 6540 O O . GLY A 873 ? 1.4146 1.2966 0.9974 0.3176 0.1579 0.1050 873 GLY A O 6541 N N . CYS A 874 ? 1.5335 1.3929 1.1707 0.3008 0.1520 0.0749 874 CYS A N 6542 C CA . CYS A 874 ? 1.5244 1.3872 1.1223 0.3399 0.1517 0.0406 874 CYS A CA 6543 C C . CYS A 874 ? 1.5180 1.4581 1.0971 0.3700 0.1760 0.0571 874 CYS A C 6544 O O . CYS A 874 ? 1.6055 1.5527 1.1362 0.4123 0.1762 0.0318 874 CYS A O 6545 C CB . CYS A 874 ? 1.4521 1.2802 1.0682 0.3382 0.1400 0.0086 874 CYS A CB 6546 S SG . CYS A 874 ? 2.4925 2.2912 2.0576 0.3806 0.1252 -0.0377 874 CYS A SG 6547 N N . GLY A 875 ? 1.4607 1.4603 1.0778 0.3491 0.1944 0.1007 875 GLY A N 6548 C CA . GLY A 875 ? 1.4917 1.5854 1.1005 0.3754 0.2215 0.1268 875 GLY A CA 6549 C C . GLY A 875 ? 1.5073 1.6382 1.0726 0.3951 0.2332 0.1504 875 GLY A C 6550 O O . GLY A 875 ? 1.5968 1.7834 1.1182 0.4428 0.2495 0.1455 875 GLY A O 6551 N N . VAL A 876 ? 1.5128 1.6122 1.0857 0.3625 0.2239 0.1754 876 VAL A N 6552 C CA . VAL A 876 ? 1.5936 1.7269 1.1271 0.3765 0.2336 0.2044 876 VAL A CA 6553 C C . VAL A 876 ? 1.5487 1.6181 1.0229 0.4026 0.2136 0.1640 876 VAL A C 6554 O O . VAL A 876 ? 1.3970 1.4831 0.8314 0.4167 0.2167 0.1819 876 VAL A O 6555 C CB . VAL A 876 ? 1.6378 1.7731 1.2103 0.3271 0.2321 0.2611 876 VAL A CB 6556 C CG1 . VAL A 876 ? 1.6999 1.9044 1.3335 0.2964 0.2475 0.3077 876 VAL A CG1 6557 C CG2 . VAL A 876 ? 1.6187 1.6516 1.2088 0.2948 0.2018 0.2413 876 VAL A CG2 6558 N N . ALA A 877 ? 1.5277 1.5273 0.9981 0.4069 0.1912 0.1131 877 ALA A N 6559 C CA . ALA A 877 ? 1.4239 1.3641 0.8459 0.4267 0.1667 0.0749 877 ALA A CA 6560 C C . ALA A 877 ? 1.4099 1.3179 0.8053 0.4572 0.1520 0.0222 877 ALA A C 6561 O O . ALA A 877 ? 1.4655 1.3970 0.8777 0.4666 0.1628 0.0149 877 ALA A O 6562 C CB . ALA A 877 ? 1.4099 1.2842 0.8610 0.3893 0.1446 0.0742 877 ALA A CB 6563 N N . GLN A 878 ? 1.4324 1.2846 0.7873 0.4716 0.1239 -0.0128 878 GLN A N 6564 C CA . GLN A 878 ? 1.5151 1.3205 0.8435 0.4951 0.1005 -0.0616 878 GLN A CA 6565 C C . GLN A 878 ? 1.3950 1.1531 0.7796 0.4581 0.0865 -0.0731 878 GLN A C 6566 O O . GLN A 878 ? 1.3327 1.0616 0.7496 0.4241 0.0750 -0.0651 878 GLN A O 6567 C CB . GLN A 878 ? 1.7359 1.4962 1.0045 0.5175 0.0689 -0.0918 878 GLN A CB 6568 C CG . GLN A 878 ? 1.9523 1.6568 1.1841 0.5440 0.0378 -0.1414 878 GLN A CG 6569 C CD . GLN A 878 ? 2.1184 1.7766 1.2883 0.5649 0.0006 -0.1708 878 GLN A CD 6570 O OE1 . GLN A 878 ? 2.0098 1.6704 1.1779 0.5501 -0.0058 -0.1555 878 GLN A OE1 6571 N NE2 . GLN A 878 ? 2.3136 1.9254 1.4301 0.6007 -0.0281 -0.2138 878 GLN A NE2 6572 N N . CYS A 879 ? 1.4181 1.1722 0.8114 0.4690 0.0877 -0.0912 879 CYS A N 6573 C CA . CYS A 879 ? 1.3868 1.1091 0.8339 0.4358 0.0799 -0.0957 879 CYS A CA 6574 C C . CYS A 879 ? 1.3542 1.0075 0.7883 0.4367 0.0443 -0.1323 879 CYS A C 6575 O O . CYS A 879 ? 1.2673 0.8977 0.6588 0.4705 0.0298 -0.1610 879 CYS A O 6576 C CB . CYS A 879 ? 1.3869 1.1524 0.8626 0.4402 0.1033 -0.0849 879 CYS A CB 6577 S SG . CYS A 879 ? 2.5720 2.3027 2.1062 0.4052 0.0942 -0.0909 879 CYS A SG 6578 N N . LEU A 880 ? 1.4193 1.0405 0.8900 0.4003 0.0285 -0.1292 880 LEU A N 6579 C CA . LEU A 880 ? 1.3184 0.8848 0.7958 0.3889 -0.0034 -0.1520 880 LEU A CA 6580 C C . LEU A 880 ? 1.2694 0.8385 0.7949 0.3690 0.0068 -0.1450 880 LEU A C 6581 O O . LEU A 880 ? 1.2452 0.8324 0.8147 0.3413 0.0199 -0.1243 880 LEU A O 6582 C CB . LEU A 880 ? 1.2861 0.8306 0.7771 0.3634 -0.0263 -0.1486 880 LEU A CB 6583 C CG . LEU A 880 ? 1.3385 0.8353 0.8419 0.3447 -0.0633 -0.1634 880 LEU A CG 6584 C CD1 . LEU A 880 ? 1.6124 1.0949 1.1027 0.3371 -0.0918 -0.1661 880 LEU A CD1 6585 C CD2 . LEU A 880 ? 1.1973 0.7032 0.7609 0.3121 -0.0556 -0.1466 880 LEU A CD2 6586 N N . LYS A 881 ? 1.2668 0.8144 0.7791 0.3866 -0.0018 -0.1637 881 LYS A N 6587 C CA . LYS A 881 ? 1.1153 0.6702 0.6671 0.3738 0.0090 -0.1569 881 LYS A CA 6588 C C . LYS A 881 ? 1.0881 0.5963 0.6624 0.3488 -0.0181 -0.1628 881 LYS A C 6589 O O . LYS A 881 ? 1.3778 0.8360 0.9260 0.3535 -0.0511 -0.1811 881 LYS A O 6590 C CB . LYS A 881 ? 1.2908 0.8597 0.8182 0.4111 0.0189 -0.1689 881 LYS A CB 6591 C CG . LYS A 881 ? 1.4411 1.0340 1.0099 0.4013 0.0351 -0.1576 881 LYS A CG 6592 C CD . LYS A 881 ? 1.4803 1.0905 1.0244 0.4430 0.0415 -0.1704 881 LYS A CD 6593 C CE . LYS A 881 ? 1.3004 0.9669 0.8121 0.4785 0.0644 -0.1656 881 LYS A CE 6594 N NZ . LYS A 881 ? 1.3814 1.0230 0.8383 0.5027 0.0404 -0.1860 881 LYS A NZ 6595 N N . ILE A 882 ? 1.0333 0.5583 0.6549 0.3219 -0.0064 -0.1455 882 ILE A N 6596 C CA . ILE A 882 ? 1.0252 0.5206 0.6718 0.2988 -0.0267 -0.1438 882 ILE A CA 6597 C C . ILE A 882 ? 1.0376 0.5394 0.7035 0.3003 -0.0161 -0.1410 882 ILE A C 6598 O O . ILE A 882 ? 0.9614 0.5011 0.6544 0.2925 0.0078 -0.1272 882 ILE A O 6599 C CB . ILE A 882 ? 0.9833 0.4971 0.6661 0.2684 -0.0252 -0.1247 882 ILE A CB 6600 C CG1 . ILE A 882 ? 1.0045 0.5135 0.6705 0.2672 -0.0391 -0.1265 882 ILE A CG1 6601 C CG2 . ILE A 882 ? 1.0969 0.5961 0.8085 0.2454 -0.0418 -0.1161 882 ILE A CG2 6602 C CD1 . ILE A 882 ? 0.9718 0.5024 0.6724 0.2429 -0.0413 -0.1084 882 ILE A CD1 6603 N N . VAL A 883 ? 1.0479 0.5074 0.6974 0.3110 -0.0381 -0.1545 883 VAL A N 6604 C CA . VAL A 883 ? 1.1401 0.6011 0.8038 0.3159 -0.0323 -0.1525 883 VAL A CA 6605 C C . VAL A 883 ? 1.2502 0.6880 0.9423 0.2860 -0.0501 -0.1390 883 VAL A C 6606 O O . VAL A 883 ? 1.4487 0.8408 1.1323 0.2743 -0.0819 -0.1411 883 VAL A O 6607 C CB . VAL A 883 ? 1.2313 0.6733 0.8610 0.3482 -0.0436 -0.1716 883 VAL A CB 6608 C CG1 . VAL A 883 ? 1.1917 0.6326 0.8400 0.3481 -0.0445 -0.1668 883 VAL A CG1 6609 C CG2 . VAL A 883 ? 1.4060 0.8976 1.0159 0.3776 -0.0188 -0.1761 883 VAL A CG2 6610 N N . CYS A 884 ? 0.9821 0.4534 0.7073 0.2729 -0.0317 -0.1230 884 CYS A N 6611 C CA . CYS A 884 ? 0.9997 0.4645 0.7519 0.2464 -0.0430 -0.1048 884 CYS A CA 6612 C C . CYS A 884 ? 1.0990 0.5575 0.8576 0.2526 -0.0430 -0.1013 884 CYS A C 6613 O O . CYS A 884 ? 1.0791 0.5650 0.8393 0.2692 -0.0231 -0.1060 884 CYS A O 6614 C CB . CYS A 884 ? 0.9184 0.4303 0.7002 0.2267 -0.0242 -0.0873 884 CYS A CB 6615 S SG . CYS A 884 ? 0.9747 0.4941 0.7555 0.2160 -0.0300 -0.0851 884 CYS A SG 6616 N N . GLN A 885 ? 1.2200 0.6442 0.9844 0.2371 -0.0675 -0.0896 885 GLN A N 6617 C CA . GLN A 885 ? 1.0105 0.4265 0.7815 0.2402 -0.0704 -0.0811 885 GLN A CA 6618 C C . GLN A 885 ? 0.9805 0.4420 0.7844 0.2168 -0.0561 -0.0546 885 GLN A C 6619 O O . GLN A 885 ? 1.1332 0.6027 0.9548 0.1912 -0.0651 -0.0337 885 GLN A O 6620 C CB . GLN A 885 ? 1.0825 0.4272 0.8364 0.2382 -0.1094 -0.0808 885 GLN A CB 6621 C CG . GLN A 885 ? 1.2284 0.5183 0.9381 0.2711 -0.1287 -0.1124 885 GLN A CG 6622 C CD . GLN A 885 ? 1.4969 0.7607 1.1907 0.2623 -0.1481 -0.1220 885 GLN A CD 6623 O OE1 . GLN A 885 ? 1.5285 0.8181 1.2495 0.2296 -0.1473 -0.1029 885 GLN A OE1 6624 N NE2 . GLN A 885 ? 1.6419 0.8800 1.2979 0.2870 -0.1624 -0.1479 885 GLN A NE2 6625 N N . VAL A 886 ? 0.9363 0.4324 0.7476 0.2276 -0.0349 -0.0550 886 VAL A N 6626 C CA . VAL A 886 ? 0.9411 0.4792 0.7734 0.2140 -0.0219 -0.0350 886 VAL A CA 6627 C C . VAL A 886 ? 1.1148 0.6449 0.9481 0.2176 -0.0289 -0.0238 886 VAL A C 6628 O O . VAL A 886 ? 1.3284 0.8360 1.1491 0.2373 -0.0341 -0.0370 886 VAL A O 6629 C CB . VAL A 886 ? 0.8753 0.4560 0.7122 0.2217 0.0031 -0.0446 886 VAL A CB 6630 C CG1 . VAL A 886 ? 0.8549 0.4735 0.7038 0.2128 0.0128 -0.0285 886 VAL A CG1 6631 C CG2 . VAL A 886 ? 1.2419 0.8230 1.0729 0.2232 0.0088 -0.0569 886 VAL A CG2 6632 N N . GLY A 887 ? 1.0385 0.5924 0.8856 0.2016 -0.0284 0.0024 887 GLY A N 6633 C CA . GLY A 887 ? 1.1120 0.6633 0.9585 0.2048 -0.0341 0.0170 887 GLY A CA 6634 C C . GLY A 887 ? 1.3239 0.9271 1.1806 0.1970 -0.0213 0.0411 887 GLY A C 6635 O O . GLY A 887 ? 1.5915 1.2295 1.4593 0.1846 -0.0133 0.0554 887 GLY A O 6636 N N . ARG A 888 ? 1.2876 0.8994 1.1383 0.2082 -0.0198 0.0455 888 ARG A N 6637 C CA . ARG A 888 ? 1.1714 0.8314 1.0225 0.2078 -0.0094 0.0672 888 ARG A CA 6638 C C . ARG A 888 ? 1.0830 0.7920 0.9334 0.2126 0.0107 0.0603 888 ARG A C 6639 O O . ARG A 888 ? 1.1996 0.9444 1.0582 0.2032 0.0165 0.0835 888 ARG A O 6640 C CB . ARG A 888 ? 1.2796 0.9412 1.1411 0.1866 -0.0222 0.1096 888 ARG A CB 6641 C CG . ARG A 888 ? 1.3737 1.0835 1.2296 0.1914 -0.0133 0.1366 888 ARG A CG 6642 C CD . ARG A 888 ? 1.3829 1.0770 1.2217 0.2120 -0.0171 0.1226 888 ARG A CD 6643 N NE . ARG A 888 ? 1.3968 1.1402 1.2233 0.2215 -0.0081 0.1432 888 ARG A NE 6644 C CZ . ARG A 888 ? 1.3017 1.0430 1.1127 0.2385 -0.0127 0.1383 888 ARG A CZ 6645 N NH1 . ARG A 888 ? 1.2385 0.9362 1.0491 0.2481 -0.0248 0.1152 888 ARG A NH1 6646 N NH2 . ARG A 888 ? 1.2894 1.0777 1.0838 0.2490 -0.0052 0.1570 888 ARG A NH2 6647 N N . LEU A 889 ? 0.9836 0.6946 0.8248 0.2278 0.0192 0.0302 889 LEU A N 6648 C CA . LEU A 889 ? 0.9357 0.6809 0.7677 0.2381 0.0324 0.0203 889 LEU A CA 6649 C C . LEU A 889 ? 0.9688 0.7327 0.7824 0.2550 0.0331 0.0144 889 LEU A C 6650 O O . LEU A 889 ? 1.0718 0.8195 0.8827 0.2607 0.0271 -0.0048 889 LEU A O 6651 C CB . LEU A 889 ? 0.8916 0.6191 0.7245 0.2397 0.0358 -0.0066 889 LEU A CB 6652 C CG . LEU A 889 ? 0.9225 0.6437 0.7660 0.2286 0.0376 -0.0036 889 LEU A CG 6653 C CD1 . LEU A 889 ? 0.8799 0.5883 0.7196 0.2331 0.0419 -0.0274 889 LEU A CD1 6654 C CD2 . LEU A 889 ? 1.0382 0.8002 0.8854 0.2271 0.0440 0.0188 889 LEU A CD2 6655 N N . ASP A 890 ? 0.9739 0.7779 0.7747 0.2639 0.0396 0.0325 890 ASP A N 6656 C CA . ASP A 890 ? 1.0080 0.8308 0.7837 0.2834 0.0378 0.0275 890 ASP A CA 6657 C C . ASP A 890 ? 1.0456 0.8670 0.7984 0.3021 0.0374 -0.0046 890 ASP A C 6658 O O . ASP A 890 ? 1.0245 0.8257 0.7843 0.2976 0.0383 -0.0220 890 ASP A O 6659 C CB . ASP A 890 ? 1.0356 0.9075 0.8014 0.2898 0.0453 0.0623 890 ASP A CB 6660 C CG . ASP A 890 ? 1.0534 0.9162 0.8372 0.2703 0.0375 0.0963 890 ASP A CG 6661 O OD1 . ASP A 890 ? 1.0154 0.8347 0.8060 0.2646 0.0246 0.0857 890 ASP A OD1 6662 O OD2 . ASP A 890 ? 1.1922 1.0924 0.9839 0.2613 0.0429 0.1357 890 ASP A OD2 6663 N N . ARG A 891 ? 1.1316 0.9693 0.8538 0.3234 0.0325 -0.0119 891 ARG A N 6664 C CA . ARG A 891 ? 1.1653 0.9895 0.8575 0.3433 0.0232 -0.0448 891 ARG A CA 6665 C C . ARG A 891 ? 1.1880 1.0151 0.8712 0.3543 0.0316 -0.0540 891 ARG A C 6666 O O . ARG A 891 ? 1.3374 1.1272 1.0250 0.3482 0.0238 -0.0762 891 ARG A O 6667 C CB . ARG A 891 ? 1.3194 1.1674 0.9704 0.3710 0.0165 -0.0478 891 ARG A CB 6668 C CG . ARG A 891 ? 1.5189 1.3421 1.1295 0.3951 -0.0010 -0.0852 891 ARG A CG 6669 C CD . ARG A 891 ? 1.7611 1.6020 1.3259 0.4238 -0.0128 -0.0920 891 ARG A CD 6670 N NE . ARG A 891 ? 1.8432 1.7459 1.3855 0.4482 0.0082 -0.0644 891 ARG A NE 6671 C CZ . ARG A 891 ? 1.7807 1.7209 1.3322 0.4419 0.0173 -0.0297 891 ARG A CZ 6672 N NH1 . ARG A 891 ? 1.8341 1.7510 1.4133 0.4167 0.0063 -0.0231 891 ARG A NH1 6673 N NH2 . ARG A 891 ? 1.6286 1.6330 1.1620 0.4620 0.0369 0.0012 891 ARG A NH2 6674 N N . GLY A 892 ? 1.1212 0.9975 0.7929 0.3715 0.0474 -0.0338 892 GLY A N 6675 C CA . GLY A 892 ? 1.2660 1.1556 0.9271 0.3896 0.0561 -0.0412 892 GLY A CA 6676 C C . GLY A 892 ? 1.2504 1.1319 0.9503 0.3645 0.0636 -0.0310 892 GLY A C 6677 O O . GLY A 892 ? 1.3040 1.1590 0.9992 0.3703 0.0602 -0.0515 892 GLY A O 6678 N N . LYS A 893 ? 1.1247 1.0235 0.8600 0.3370 0.0701 0.0005 893 LYS A N 6679 C CA . LYS A 893 ? 1.1172 1.0158 0.8856 0.3153 0.0749 0.0136 893 LYS A CA 6680 C C . LYS A 893 ? 1.0332 0.8719 0.8135 0.2982 0.0653 -0.0106 893 LYS A C 6681 O O . LYS A 893 ? 1.0062 0.8082 0.7828 0.2930 0.0555 -0.0277 893 LYS A O 6682 C CB . LYS A 893 ? 1.3627 1.2842 1.1618 0.2885 0.0761 0.0533 893 LYS A CB 6683 C CG . LYS A 893 ? 1.6365 1.5752 1.4674 0.2686 0.0784 0.0740 893 LYS A CG 6684 C CD . LYS A 893 ? 1.7756 1.7320 1.6358 0.2391 0.0724 0.1166 893 LYS A CD 6685 C CE . LYS A 893 ? 1.7766 1.7430 1.6701 0.2146 0.0672 0.1355 893 LYS A CE 6686 N NZ . LYS A 893 ? 1.7187 1.7533 1.6157 0.2332 0.0828 0.1441 893 LYS A NZ 6687 N N . SER A 894 ? 1.0677 0.9051 0.8633 0.2905 0.0686 -0.0089 894 SER A N 6688 C CA . SER A 894 ? 1.0360 0.8265 0.8421 0.2754 0.0622 -0.0258 894 SER A CA 6689 C C . SER A 894 ? 1.0402 0.8362 0.8717 0.2559 0.0627 -0.0087 894 SER A C 6690 O O . SER A 894 ? 1.1937 1.0322 1.0386 0.2526 0.0669 0.0167 894 SER A O 6691 C CB . SER A 894 ? 1.1305 0.8992 0.9163 0.2922 0.0596 -0.0510 894 SER A CB 6692 O OG . SER A 894 ? 1.2994 1.0998 1.0776 0.3115 0.0668 -0.0461 894 SER A OG 6693 N N . ALA A 895 ? 0.8936 0.6508 0.7320 0.2430 0.0570 -0.0208 895 ALA A N 6694 C CA . ALA A 895 ? 0.8967 0.6493 0.7525 0.2263 0.0521 -0.0100 895 ALA A CA 6695 C C . ALA A 895 ? 0.9930 0.7322 0.8441 0.2305 0.0533 -0.0241 895 ALA A C 6696 O O . ALA A 895 ? 1.1620 0.8744 1.0009 0.2363 0.0541 -0.0427 895 ALA A O 6697 C CB . ALA A 895 ? 0.9034 0.6202 0.7644 0.2117 0.0411 -0.0105 895 ALA A CB 6698 N N . ILE A 896 ? 0.9790 0.7399 0.8424 0.2256 0.0518 -0.0114 896 ILE A N 6699 C CA . ILE A 896 ? 0.9168 0.6706 0.7748 0.2325 0.0525 -0.0214 896 ILE A CA 6700 C C . ILE A 896 ? 0.9920 0.7301 0.8597 0.2154 0.0413 -0.0178 896 ILE A C 6701 O O . ILE A 896 ? 1.1003 0.8449 0.9842 0.1980 0.0304 -0.0019 896 ILE A O 6702 C CB . ILE A 896 ? 0.8358 0.6360 0.6948 0.2514 0.0597 -0.0127 896 ILE A CB 6703 C CG1 . ILE A 896 ? 0.8400 0.6653 0.6859 0.2716 0.0682 -0.0126 896 ILE A CG1 6704 C CG2 . ILE A 896 ? 0.8887 0.6693 0.7326 0.2666 0.0596 -0.0282 896 ILE A CG2 6705 C CD1 . ILE A 896 ? 0.9672 0.7497 0.7847 0.2865 0.0665 -0.0391 896 ILE A CD1 6706 N N . LEU A 897 ? 0.9447 0.6591 0.8000 0.2202 0.0408 -0.0316 897 LEU A N 6707 C CA . LEU A 897 ? 0.8937 0.5952 0.7504 0.2101 0.0291 -0.0310 897 LEU A CA 6708 C C . LEU A 897 ? 1.0824 0.7948 0.9344 0.2210 0.0312 -0.0322 897 LEU A C 6709 O O . LEU A 897 ? 1.2488 0.9420 1.0838 0.2327 0.0379 -0.0434 897 LEU A O 6710 C CB . LEU A 897 ? 0.8840 0.5439 0.7235 0.2083 0.0254 -0.0462 897 LEU A CB 6711 C CG . LEU A 897 ? 0.8227 0.4639 0.6503 0.2060 0.0132 -0.0517 897 LEU A CG 6712 C CD1 . LEU A 897 ? 0.8637 0.5074 0.7054 0.1896 -0.0083 -0.0405 897 LEU A CD1 6713 C CD2 . LEU A 897 ? 0.8379 0.4486 0.6427 0.2137 0.0139 -0.0670 897 LEU A CD2 6714 N N . TYR A 898 ? 1.0111 0.7553 0.8805 0.2157 0.0229 -0.0177 898 TYR A N 6715 C CA . TYR A 898 ? 0.8864 0.6456 0.7530 0.2283 0.0226 -0.0170 898 TYR A CA 6716 C C . TYR A 898 ? 0.9017 0.6374 0.7604 0.2183 0.0074 -0.0214 898 TYR A C 6717 O O . TYR A 898 ? 0.9418 0.6805 0.8137 0.1997 -0.0101 -0.0136 898 TYR A O 6718 C CB . TYR A 898 ? 0.9038 0.7274 0.7967 0.2337 0.0237 0.0039 898 TYR A CB 6719 C CG . TYR A 898 ? 0.8930 0.7493 0.7894 0.2479 0.0383 0.0100 898 TYR A CG 6720 C CD1 . TYR A 898 ? 0.9975 0.8846 0.9160 0.2313 0.0377 0.0296 898 TYR A CD1 6721 C CD2 . TYR A 898 ? 0.8724 0.7246 0.7458 0.2792 0.0496 -0.0036 898 TYR A CD2 6722 C CE1 . TYR A 898 ? 1.0561 0.9782 0.9729 0.2475 0.0518 0.0363 898 TYR A CE1 6723 C CE2 . TYR A 898 ? 0.8683 0.7483 0.7364 0.2975 0.0604 -0.0018 898 TYR A CE2 6724 C CZ . TYR A 898 ? 0.9677 0.8872 0.8571 0.2827 0.0635 0.0186 898 TYR A CZ 6725 O OH . TYR A 898 ? 1.1197 1.0718 0.9991 0.3040 0.0752 0.0217 898 TYR A OH 6726 N N . VAL A 899 ? 0.8846 0.5946 0.7194 0.2304 0.0113 -0.0326 899 VAL A N 6727 C CA . VAL A 899 ? 0.8806 0.5713 0.6998 0.2268 -0.0018 -0.0374 899 VAL A CA 6728 C C . VAL A 899 ? 0.9662 0.6757 0.7842 0.2390 -0.0051 -0.0312 899 VAL A C 6729 O O . VAL A 899 ? 1.0340 0.7319 0.8369 0.2550 0.0049 -0.0335 899 VAL A O 6730 C CB . VAL A 899 ? 0.8706 0.5230 0.6603 0.2315 0.0054 -0.0507 899 VAL A CB 6731 C CG1 . VAL A 899 ? 0.9425 0.5804 0.7083 0.2342 -0.0070 -0.0559 899 VAL A CG1 6732 C CG2 . VAL A 899 ? 0.8567 0.4939 0.6471 0.2243 0.0077 -0.0576 899 VAL A CG2 6733 N N . LYS A 900 ? 0.9898 0.7262 0.8247 0.2303 -0.0226 -0.0216 900 LYS A N 6734 C CA . LYS A 900 ? 0.9943 0.7548 0.8306 0.2430 -0.0286 -0.0143 900 LYS A CA 6735 C C . LYS A 900 ? 1.0273 0.7586 0.8357 0.2416 -0.0437 -0.0226 900 LYS A C 6736 O O . LYS A 900 ? 1.0580 0.7783 0.8647 0.2254 -0.0644 -0.0266 900 LYS A O 6737 C CB . LYS A 900 ? 1.0115 0.8349 0.8890 0.2353 -0.0394 0.0059 900 LYS A CB 6738 C CG . LYS A 900 ? 1.0460 0.9037 0.9294 0.2501 -0.0479 0.0149 900 LYS A CG 6739 C CD . LYS A 900 ? 1.0611 0.9975 0.9934 0.2415 -0.0574 0.0405 900 LYS A CD 6740 C CE . LYS A 900 ? 1.0762 1.0543 1.0170 0.2595 -0.0665 0.0502 900 LYS A CE 6741 N NZ . LYS A 900 ? 1.1529 1.2248 1.1487 0.2516 -0.0743 0.0804 900 LYS A NZ 6742 N N . SER A 901 ? 1.0205 0.7358 0.8034 0.2598 -0.0361 -0.0248 901 SER A N 6743 C CA . SER A 901 ? 1.0661 0.7581 0.8161 0.2631 -0.0470 -0.0305 901 SER A CA 6744 C C . SER A 901 ? 1.0966 0.8022 0.8394 0.2800 -0.0517 -0.0209 901 SER A C 6745 O O . SER A 901 ? 1.1095 0.8290 0.8644 0.2946 -0.0426 -0.0130 901 SER A O 6746 C CB . SER A 901 ? 1.0479 0.7029 0.7657 0.2671 -0.0315 -0.0388 901 SER A CB 6747 O OG . SER A 901 ? 1.0086 0.6542 0.7215 0.2777 -0.0149 -0.0308 901 SER A OG 6748 N N . LEU A 902 ? 1.1395 0.8380 0.8579 0.2819 -0.0682 -0.0232 902 LEU A N 6749 C CA . LEU A 902 ? 1.1654 0.8717 0.8701 0.2995 -0.0741 -0.0135 902 LEU A CA 6750 C C . LEU A 902 ? 1.3107 0.9816 0.9701 0.3097 -0.0642 -0.0129 902 LEU A C 6751 O O . LEU A 902 ? 1.4699 1.1240 1.1015 0.3057 -0.0654 -0.0227 902 LEU A O 6752 C CB . LEU A 902 ? 1.2018 0.9354 0.9136 0.2947 -0.1037 -0.0119 902 LEU A CB 6753 C CG . LEU A 902 ? 1.2637 1.0503 1.0284 0.2825 -0.1167 -0.0017 902 LEU A CG 6754 C CD1 . LEU A 902 ? 1.3533 1.1610 1.1236 0.2713 -0.1523 0.0006 902 LEU A CD1 6755 C CD2 . LEU A 902 ? 1.3941 1.2175 1.1827 0.3042 -0.1020 0.0124 902 LEU A CD2 6756 N N . LEU A 903 ? 1.2842 0.9445 0.9349 0.3245 -0.0555 0.0002 903 LEU A N 6757 C CA . LEU A 903 ? 1.2547 0.8893 0.8661 0.3314 -0.0487 0.0104 903 LEU A CA 6758 C C . LEU A 903 ? 1.3244 0.9705 0.9077 0.3397 -0.0673 0.0105 903 LEU A C 6759 O O . LEU A 903 ? 1.5367 1.2052 1.1331 0.3464 -0.0858 0.0121 903 LEU A O 6760 C CB . LEU A 903 ? 1.2490 0.8604 0.8581 0.3429 -0.0428 0.0273 903 LEU A CB 6761 C CG . LEU A 903 ? 1.2853 0.8707 0.8589 0.3454 -0.0375 0.0479 903 LEU A CG 6762 C CD1 . LEU A 903 ? 1.3137 0.8611 0.8933 0.3407 -0.0292 0.0610 903 LEU A CD1 6763 C CD2 . LEU A 903 ? 1.3664 0.9556 0.9176 0.3634 -0.0534 0.0604 903 LEU A CD2 6764 N N . TRP A 904 ? 1.3372 0.9735 0.8809 0.3419 -0.0632 0.0093 904 TRP A N 6765 C CA . TRP A 904 ? 1.3829 1.0270 0.8901 0.3537 -0.0827 0.0064 904 TRP A CA 6766 C C . TRP A 904 ? 1.4650 1.1040 0.9454 0.3687 -0.0787 0.0316 904 TRP A C 6767 O O . TRP A 904 ? 1.6279 1.2573 1.0837 0.3706 -0.0600 0.0480 904 TRP A O 6768 C CB . TRP A 904 ? 1.3926 1.0307 0.8612 0.3570 -0.0821 -0.0105 904 TRP A CB 6769 C CG . TRP A 904 ? 1.4369 1.0770 0.8697 0.3679 -0.1124 -0.0259 904 TRP A CG 6770 C CD1 . TRP A 904 ? 1.5739 1.2186 0.9575 0.3880 -0.1198 -0.0182 904 TRP A CD1 6771 C CD2 . TRP A 904 ? 1.4486 1.0828 0.8898 0.3582 -0.1438 -0.0506 904 TRP A CD2 6772 N NE1 . TRP A 904 ? 1.6625 1.3030 1.0203 0.3938 -0.1550 -0.0408 904 TRP A NE1 6773 C CE2 . TRP A 904 ? 1.5571 1.1882 0.9512 0.3735 -0.1723 -0.0605 904 TRP A CE2 6774 C CE3 . TRP A 904 ? 1.4185 1.0479 0.9019 0.3364 -0.1532 -0.0630 904 TRP A CE3 6775 C CZ2 . TRP A 904 ? 1.5409 1.1582 0.9296 0.3656 -0.2139 -0.0842 904 TRP A CZ2 6776 C CZ3 . TRP A 904 ? 1.4502 1.0683 0.9315 0.3264 -0.1926 -0.0819 904 TRP A CZ3 6777 C CH2 . TRP A 904 ? 1.5050 1.1142 0.9397 0.3399 -0.2246 -0.0933 904 TRP A CH2 6778 N N . THR A 905 ? 1.4607 1.1103 0.9481 0.3788 -0.0976 0.0382 905 THR A N 6779 C CA . THR A 905 ? 1.4968 1.1357 0.9625 0.3944 -0.0975 0.0640 905 THR A CA 6780 C C . THR A 905 ? 1.5500 1.1943 0.9604 0.4069 -0.1042 0.0710 905 THR A C 6781 O O . THR A 905 ? 1.5729 1.2056 0.9541 0.4147 -0.0945 0.0981 905 THR A O 6782 C CB . THR A 905 ? 1.4939 1.1467 0.9862 0.4073 -0.1159 0.0683 905 THR A CB 6783 O OG1 . THR A 905 ? 1.4331 1.0960 0.9741 0.4000 -0.1111 0.0575 905 THR A OG1 6784 C CG2 . THR A 905 ? 1.6049 1.2307 1.0786 0.4244 -0.1146 0.0953 905 THR A CG2 6785 N N . GLU A 906 ? 1.5948 1.2548 0.9888 0.4087 -0.1232 0.0476 906 GLU A N 6786 C CA . GLU A 906 ? 1.7458 1.4119 1.0794 0.4263 -0.1345 0.0469 906 GLU A CA 6787 C C . GLU A 906 ? 1.8072 1.4711 1.1001 0.4325 -0.1061 0.0595 906 GLU A C 6788 O O . GLU A 906 ? 2.0219 1.6960 1.2624 0.4513 -0.1050 0.0746 906 GLU A O 6789 C CB . GLU A 906 ? 1.8671 1.5383 1.1905 0.4251 -0.1655 0.0131 906 GLU A CB 6790 C CG . GLU A 906 ? 2.0558 1.7296 1.3104 0.4481 -0.1860 0.0054 906 GLU A CG 6791 C CD . GLU A 906 ? 2.2085 1.8740 1.4530 0.4444 -0.2262 -0.0306 906 GLU A CD 6792 O OE1 . GLU A 906 ? 2.2995 1.9586 1.4792 0.4659 -0.2469 -0.0458 906 GLU A OE1 6793 O OE2 . GLU A 906 ? 2.2400 1.9042 1.5393 0.4199 -0.2394 -0.0424 906 GLU A OE2 6794 N N . THR A 907 ? 1.6826 1.3406 1.0010 0.4177 -0.0826 0.0562 907 THR A N 6795 C CA . THR A 907 ? 1.6879 1.3572 0.9793 0.4216 -0.0537 0.0716 907 THR A CA 6796 C C . THR A 907 ? 1.6993 1.3679 0.9909 0.4168 -0.0360 0.1176 907 THR A C 6797 O O . THR A 907 ? 1.9386 1.6300 1.1905 0.4276 -0.0211 0.1433 907 THR A O 6798 C CB . THR A 907 ? 1.7279 1.3941 1.0525 0.4058 -0.0364 0.0562 907 THR A CB 6799 O OG1 . THR A 907 ? 1.8099 1.4705 1.1266 0.4109 -0.0552 0.0165 907 THR A OG1 6800 C CG2 . THR A 907 ? 1.7477 1.4384 1.0533 0.4094 -0.0053 0.0781 907 THR A CG2 6801 N N . PHE A 908 ? 1.6482 1.2903 0.9824 0.4022 -0.0397 0.1296 908 PHE A N 6802 C CA . PHE A 908 ? 1.7048 1.3291 1.0414 0.3943 -0.0308 0.1725 908 PHE A CA 6803 C C . PHE A 908 ? 2.0047 1.6292 1.3022 0.4129 -0.0453 0.1961 908 PHE A C 6804 O O . PHE A 908 ? 2.2478 1.8910 1.5153 0.4323 -0.0614 0.1773 908 PHE A O 6805 C CB . PHE A 908 ? 1.6233 1.2085 1.0086 0.3796 -0.0357 0.1714 908 PHE A CB 6806 C CG . PHE A 908 ? 1.7943 1.3792 1.2158 0.3614 -0.0217 0.1519 908 PHE A CG 6807 C CD1 . PHE A 908 ? 1.8239 1.4077 1.2555 0.3420 -0.0025 0.1743 908 PHE A CD1 6808 C CD2 . PHE A 908 ? 1.7307 1.3212 1.1782 0.3619 -0.0292 0.1149 908 PHE A CD2 6809 C CE1 . PHE A 908 ? 1.5415 1.1272 1.0057 0.3267 0.0087 0.1564 908 PHE A CE1 6810 C CE2 . PHE A 908 ? 1.4900 1.0800 0.9679 0.3465 -0.0170 0.0989 908 PHE A CE2 6811 C CZ . PHE A 908 ? 1.4790 1.0655 0.9638 0.3305 0.0018 0.1178 908 PHE A CZ 6812 N N . MET A 909 ? 1.9684 1.5677 1.2654 0.4059 -0.0435 0.2379 909 MET A N 6813 C CA . MET A 909 ? 2.0028 1.6031 1.2576 0.4215 -0.0529 0.2718 909 MET A CA 6814 C C . MET A 909 ? 2.0728 1.7247 1.2767 0.4335 -0.0370 0.2832 909 MET A C 6815 O O . MET A 909 ? 1.9802 1.6589 1.1860 0.4217 -0.0117 0.2967 909 MET A O 6816 C CB . MET A 909 ? 2.0211 1.6130 1.2697 0.4443 -0.0821 0.2525 909 MET A CB 6817 C CG . MET A 909 ? 2.1198 1.6703 1.4115 0.4435 -0.0973 0.2445 909 MET A CG 6818 S SD . MET A 909 ? 1.7531 1.3139 1.0978 0.4339 -0.0955 0.1949 909 MET A SD 6819 C CE . MET A 909 ? 1.4768 1.0008 0.8541 0.4485 -0.1142 0.1938 909 MET A CE 6820 N N . ASN A 910 ? 2.2899 1.9598 1.4470 0.4602 -0.0527 0.2783 910 ASN A N 6821 C CA . ASN A 910 ? 2.3211 2.0401 1.4180 0.4825 -0.0426 0.2781 910 ASN A CA 6822 C C . ASN A 910 ? 2.2218 1.9774 1.2990 0.4765 -0.0106 0.3285 910 ASN A C 6823 O O . ASN A 910 ? 2.1646 1.9062 1.2512 0.4602 -0.0063 0.3808 910 ASN A O 6824 C CB . ASN A 910 ? 2.1770 1.9111 1.2721 0.4903 -0.0437 0.2235 910 ASN A CB 6825 C CG . ASN A 910 ? 2.0672 1.7720 1.1987 0.4853 -0.0728 0.1804 910 ASN A CG 6826 O OD1 . ASN A 910 ? 2.1475 1.8342 1.2921 0.4872 -0.0946 0.1862 910 ASN A OD1 6827 N ND2 . ASN A 910 ? 1.9324 1.6369 1.0820 0.4796 -0.0737 0.1400 910 ASN A ND2 6828 N N . LYS A 911 ? 2.1567 1.9606 1.2068 0.4906 0.0099 0.3138 911 LYS A N 6829 C CA . LYS A 911 ? 2.2585 2.1180 1.2966 0.4871 0.0448 0.3601 911 LYS A CA 6830 C C . LYS A 911 ? 2.2231 2.0805 1.3242 0.4550 0.0639 0.3606 911 LYS A C 6831 O O . LYS A 911 ? 2.2064 2.1176 1.3126 0.4478 0.0934 0.3950 911 LYS A O 6832 C CB . LYS A 911 ? 2.3603 2.2822 1.3269 0.5302 0.0573 0.3439 911 LYS A CB 6833 C CG . LYS A 911 ? 2.4036 2.3357 1.2990 0.5639 0.0397 0.3499 911 LYS A CG 6834 C CD . LYS A 911 ? 2.4098 2.4055 1.2364 0.6079 0.0533 0.3324 911 LYS A CD 6835 C CE . LYS A 911 ? 2.4214 2.4301 1.2024 0.6306 0.0356 0.3332 911 LYS A CE 6836 N NZ . LYS A 911 ? 2.3933 2.4621 1.1272 0.6697 0.0479 0.3093 911 LYS A NZ 6837 N N . GLU A 912 ? 2.2551 2.0565 1.4045 0.4372 0.0461 0.3238 912 GLU A N 6838 C CA . GLU A 912 ? 2.3282 2.1168 1.5374 0.4077 0.0577 0.3167 912 GLU A CA 6839 C C . GLU A 912 ? 2.3783 2.1491 1.6268 0.3709 0.0637 0.3733 912 GLU A C 6840 O O . GLU A 912 ? 2.2729 2.0262 1.5719 0.3431 0.0683 0.3722 912 GLU A O 6841 C CB . GLU A 912 ? 2.2215 1.9586 1.4652 0.4028 0.0353 0.2637 912 GLU A CB 6842 C CG . GLU A 912 ? 2.0593 1.7930 1.3504 0.3835 0.0470 0.2415 912 GLU A CG 6843 C CD . GLU A 912 ? 2.1031 1.8899 1.3717 0.4004 0.0683 0.2266 912 GLU A CD 6844 O OE1 . GLU A 912 ? 2.0542 1.8629 1.3551 0.3835 0.0888 0.2390 912 GLU A OE1 6845 O OE2 . GLU A 912 ? 2.2295 2.0348 1.4463 0.4331 0.0620 0.2012 912 GLU A OE2 6846 N N . ASN A 913 ? 2.5186 2.2887 1.7422 0.3703 0.0592 0.4229 913 ASN A N 6847 C CA . ASN A 913 ? 2.5972 2.3276 1.8533 0.3344 0.0520 0.4772 913 ASN A CA 6848 C C . ASN A 913 ? 2.4867 2.1290 1.7759 0.3245 0.0223 0.4491 913 ASN A C 6849 O O . ASN A 913 ? 2.4036 2.0150 1.7387 0.3009 0.0203 0.4359 913 ASN A O 6850 C CB . ASN A 913 ? 2.6139 2.3826 1.9099 0.3004 0.0751 0.5145 913 ASN A CB 6851 C CG . ASN A 913 ? 2.5754 2.4416 1.8405 0.3104 0.1062 0.5604 913 ASN A CG 6852 O OD1 . ASN A 913 ? 2.5422 2.4765 1.8080 0.3220 0.1322 0.5462 913 ASN A OD1 6853 N ND2 . ASN A 913 ? 2.5458 2.4224 1.7816 0.3092 0.1037 0.6174 913 ASN A ND2 6854 N N . GLN A 914 ? 2.3890 1.9977 1.6510 0.3475 -0.0007 0.4393 914 GLN A N 6855 C CA . GLN A 914 ? 2.2550 1.7960 1.5380 0.3538 -0.0285 0.4068 914 GLN A CA 6856 C C . GLN A 914 ? 2.2563 1.7335 1.5825 0.3242 -0.0386 0.4194 914 GLN A C 6857 O O . GLN A 914 ? 2.2303 1.6878 1.5894 0.3208 -0.0411 0.3792 914 GLN A O 6858 C CB . GLN A 914 ? 2.2659 1.7819 1.5137 0.3779 -0.0517 0.4218 914 GLN A CB 6859 C CG . GLN A 914 ? 2.2688 1.8437 1.4655 0.4069 -0.0469 0.4161 914 GLN A CG 6860 C CD . GLN A 914 ? 2.3740 1.9256 1.5382 0.4314 -0.0726 0.4299 914 GLN A CD 6861 O OE1 . GLN A 914 ? 2.4581 1.9495 1.6335 0.4268 -0.0916 0.4540 914 GLN A OE1 6862 N NE2 . GLN A 914 ? 2.3819 1.9772 1.5028 0.4598 -0.0768 0.4131 914 GLN A NE2 6863 N N . ASN A 915 ? 2.3824 1.8250 1.7071 0.3020 -0.0473 0.4759 915 ASN A N 6864 C CA . ASN A 915 ? 2.4503 1.8257 1.8128 0.2714 -0.0626 0.4864 915 ASN A CA 6865 C C . ASN A 915 ? 2.3898 1.8114 1.7828 0.2345 -0.0392 0.5104 915 ASN A C 6866 O O . ASN A 915 ? 2.4925 1.9470 1.8829 0.2108 -0.0292 0.5701 915 ASN A O 6867 C CB . ASN A 915 ? 2.6024 1.8999 1.9515 0.2619 -0.0932 0.5349 915 ASN A CB 6868 C CG . ASN A 915 ? 2.6490 1.8726 2.0319 0.2236 -0.1140 0.5551 915 ASN A CG 6869 O OD1 . ASN A 915 ? 2.6605 1.8594 2.0714 0.2201 -0.1178 0.5134 915 ASN A OD1 6870 N ND2 . ASN A 915 ? 2.6495 1.8362 2.0287 0.1932 -0.1305 0.6214 915 ASN A ND2 6871 N N . HIS A 916 ? 2.2176 1.6477 1.6416 0.2309 -0.0305 0.4656 916 HIS A N 6872 C CA . HIS A 916 ? 2.0783 1.5419 1.5400 0.1970 -0.0140 0.4798 916 HIS A CA 6873 C C . HIS A 916 ? 1.9772 1.4049 1.4692 0.1974 -0.0217 0.4254 916 HIS A C 6874 O O . HIS A 916 ? 1.8893 1.3093 1.3716 0.2281 -0.0245 0.3746 916 HIS A O 6875 C CB . HIS A 916 ? 1.9771 1.5476 1.4281 0.2052 0.0235 0.4870 916 HIS A CB 6876 C CG . HIS A 916 ? 2.0702 1.6936 1.5200 0.1811 0.0377 0.5601 916 HIS A CG 6877 N ND1 . HIS A 916 ? 2.0706 1.7970 1.4998 0.1964 0.0719 0.5766 916 HIS A ND1 6878 C CD2 . HIS A 916 ? 2.1960 1.7860 1.6625 0.1431 0.0211 0.6239 916 HIS A CD2 6879 C CE1 . HIS A 916 ? 2.1479 1.9142 1.5840 0.1693 0.0800 0.6508 916 HIS A CE1 6880 N NE2 . HIS A 916 ? 2.2037 1.8866 1.6650 0.1328 0.0482 0.6828 916 HIS A NE2 6881 N N . SER A 917 ? 2.0199 1.4309 1.5497 0.1625 -0.0261 0.4383 917 SER A N 6882 C CA . SER A 917 ? 1.9132 1.2917 1.4681 0.1638 -0.0338 0.3888 917 SER A CA 6883 C C . SER A 917 ? 1.7179 1.1756 1.2895 0.1674 -0.0024 0.3616 917 SER A C 6884 O O . SER A 917 ? 1.6719 1.1858 1.2643 0.1440 0.0157 0.3912 917 SER A O 6885 C CB . SER A 917 ? 2.0310 1.3399 1.6136 0.1269 -0.0618 0.4102 917 SER A CB 6886 O OG . SER A 917 ? 2.0445 1.2637 1.6062 0.1283 -0.0970 0.4296 917 SER A OG 6887 N N . TYR A 918 ? 1.7000 1.1638 1.2635 0.1975 0.0024 0.3077 918 TYR A N 6888 C CA . TYR A 918 ? 1.5130 1.0369 1.0879 0.2047 0.0263 0.2770 918 TYR A CA 6889 C C . TYR A 918 ? 1.4367 0.9292 1.0393 0.2014 0.0180 0.2379 918 TYR A C 6890 O O . TYR A 918 ? 1.4517 0.8954 1.0501 0.2167 0.0001 0.2113 918 TYR A O 6891 C CB . TYR A 918 ? 1.4455 1.0060 0.9879 0.2389 0.0360 0.2491 918 TYR A CB 6892 C CG . TYR A 918 ? 1.4939 1.1039 1.0020 0.2488 0.0499 0.2808 918 TYR A CG 6893 C CD1 . TYR A 918 ? 1.6289 1.2805 1.1437 0.2283 0.0656 0.3299 918 TYR A CD1 6894 C CD2 . TYR A 918 ? 1.5164 1.1380 0.9853 0.2792 0.0464 0.2635 918 TYR A CD2 6895 C CE1 . TYR A 918 ? 1.7570 1.4636 1.2363 0.2419 0.0810 0.3614 918 TYR A CE1 6896 C CE2 . TYR A 918 ? 1.6552 1.3225 1.0850 0.2931 0.0581 0.2902 918 TYR A CE2 6897 C CZ . TYR A 918 ? 1.7203 1.4318 1.1533 0.2765 0.0772 0.3392 918 TYR A CZ 6898 O OH . TYR A 918 ? 1.6717 1.4379 1.0619 0.2947 0.0913 0.3683 918 TYR A OH 6899 N N . SER A 919 ? 1.3871 0.9139 1.0167 0.1848 0.0319 0.2359 919 SER A N 6900 C CA . SER A 919 ? 1.3274 0.8349 0.9800 0.1840 0.0271 0.1987 919 SER A CA 6901 C C . SER A 919 ? 1.2667 0.8313 0.9209 0.1988 0.0490 0.1703 919 SER A C 6902 O O . SER A 919 ? 1.3242 0.9447 0.9824 0.1942 0.0685 0.1863 919 SER A O 6903 C CB . SER A 919 ? 1.4353 0.9209 1.1199 0.1502 0.0162 0.2185 919 SER A CB 6904 O OG . SER A 919 ? 1.5545 1.1086 1.2603 0.1328 0.0375 0.2423 919 SER A OG 6905 N N . LEU A 920 ? 1.2119 0.7636 0.8627 0.2179 0.0445 0.1303 920 LEU A N 6906 C CA . LEU A 920 ? 1.1890 0.7802 0.8378 0.2316 0.0581 0.1027 920 LEU A CA 6907 C C . LEU A 920 ? 1.3190 0.9129 0.9974 0.2204 0.0616 0.0870 920 LEU A C 6908 O O . LEU A 920 ? 1.4113 0.9734 1.1026 0.2198 0.0501 0.0683 920 LEU A O 6909 C CB . LEU A 920 ? 1.1499 0.7313 0.7832 0.2530 0.0482 0.0749 920 LEU A CB 6910 C CG . LEU A 920 ? 1.1661 0.7428 0.7701 0.2655 0.0407 0.0896 920 LEU A CG 6911 C CD1 . LEU A 920 ? 1.1491 0.7221 0.7459 0.2833 0.0272 0.0647 920 LEU A CD1 6912 C CD2 . LEU A 920 ? 1.2066 0.8233 0.7837 0.2712 0.0549 0.1076 920 LEU A CD2 6913 N N . LYS A 921 ? 1.2471 0.8848 0.9340 0.2156 0.0780 0.0952 921 LYS A N 6914 C CA . LYS A 921 ? 1.1504 0.7965 0.8671 0.2033 0.0812 0.0872 921 LYS A CA 6915 C C . LYS A 921 ? 1.1528 0.8208 0.8657 0.2211 0.0894 0.0565 921 LYS A C 6916 O O . LYS A 921 ? 1.3796 1.0862 1.0765 0.2365 0.1026 0.0565 921 LYS A O 6917 C CB . LYS A 921 ? 1.2001 0.8849 0.9375 0.1828 0.0912 0.1237 921 LYS A CB 6918 C CG . LYS A 921 ? 1.2772 0.9910 1.0445 0.1747 0.0979 0.1174 921 LYS A CG 6919 C CD . LYS A 921 ? 1.3591 1.1302 1.1511 0.1554 0.1094 0.1595 921 LYS A CD 6920 C CE . LYS A 921 ? 1.4026 1.2228 1.2195 0.1585 0.1211 0.1520 921 LYS A CE 6921 N NZ . LYS A 921 ? 1.3803 1.2308 1.1690 0.1970 0.1378 0.1245 921 LYS A NZ 6922 N N . SER A 922 ? 1.0667 0.7084 0.7914 0.2213 0.0799 0.0314 922 SER A N 6923 C CA . SER A 922 ? 1.1014 0.7548 0.8265 0.2329 0.0831 0.0064 922 SER A CA 6924 C C . SER A 922 ? 1.0150 0.6782 0.7680 0.2215 0.0865 0.0055 922 SER A C 6925 O O . SER A 922 ? 0.9892 0.6306 0.7599 0.2067 0.0780 0.0089 922 SER A O 6926 C CB . SER A 922 ? 1.2031 0.8309 0.9239 0.2398 0.0700 -0.0154 922 SER A CB 6927 O OG . SER A 922 ? 1.2695 0.8738 1.0066 0.2316 0.0618 -0.0162 922 SER A OG 6928 N N . SER A 923 ? 0.9888 0.6827 0.7417 0.2320 0.0967 -0.0006 923 SER A N 6929 C CA . SER A 923 ? 0.9799 0.6913 0.7595 0.2240 0.1001 0.0001 923 SER A CA 6930 C C . SER A 923 ? 0.9328 0.6279 0.7128 0.2333 0.0940 -0.0259 923 SER A C 6931 O O . SER A 923 ? 0.9407 0.6247 0.6993 0.2493 0.0902 -0.0423 923 SER A O 6932 C CB . SER A 923 ? 1.1428 0.9107 0.9265 0.2317 0.1168 0.0172 923 SER A CB 6933 O OG . SER A 923 ? 1.2882 1.0792 1.0997 0.2265 0.1190 0.0175 923 SER A OG 6934 N N . ALA A 924 ? 0.9166 0.6077 0.7199 0.2219 0.0897 -0.0280 924 ALA A N 6935 C CA . ALA A 924 ? 0.9397 0.6199 0.7452 0.2290 0.0845 -0.0464 924 ALA A CA 6936 C C . ALA A 924 ? 0.8782 0.5824 0.7054 0.2261 0.0876 -0.0434 924 ALA A C 6937 O O . ALA A 924 ? 0.8192 0.5260 0.6662 0.2093 0.0834 -0.0341 924 ALA A O 6938 C CB . ALA A 924 ? 1.0841 0.7344 0.8911 0.2224 0.0736 -0.0541 924 ALA A CB 6939 N N . SER A 925 ? 0.9377 0.6557 0.7590 0.2441 0.0913 -0.0525 925 SER A N 6940 C CA . SER A 925 ? 0.9704 0.7165 0.8119 0.2467 0.0940 -0.0499 925 SER A CA 6941 C C . SER A 925 ? 0.9395 0.6594 0.7783 0.2526 0.0838 -0.0654 925 SER A C 6942 O O . SER A 925 ? 1.1170 0.8054 0.9363 0.2603 0.0763 -0.0771 925 SER A O 6943 C CB . SER A 925 ? 1.0789 0.8699 0.9153 0.2695 0.1072 -0.0451 925 SER A CB 6944 O OG . SER A 925 ? 1.1946 1.0155 1.0300 0.2652 0.1183 -0.0261 925 SER A OG 6945 N N . PHE A 926 ? 0.8426 0.5764 0.7020 0.2468 0.0810 -0.0626 926 PHE A N 6946 C CA . PHE A 926 ? 0.9800 0.6946 0.8368 0.2534 0.0720 -0.0724 926 PHE A CA 6947 C C . PHE A 926 ? 0.9993 0.7463 0.8722 0.2637 0.0734 -0.0697 926 PHE A C 6948 O O . PHE A 926 ? 1.1021 0.8876 0.9985 0.2545 0.0775 -0.0578 926 PHE A O 6949 C CB . PHE A 926 ? 0.9742 0.6677 0.8344 0.2374 0.0637 -0.0728 926 PHE A CB 6950 C CG . PHE A 926 ? 0.9142 0.6236 0.7920 0.2282 0.0588 -0.0690 926 PHE A CG 6951 C CD1 . PHE A 926 ? 0.8238 0.5354 0.7044 0.2341 0.0527 -0.0716 926 PHE A CD1 6952 C CD2 . PHE A 926 ? 0.9880 0.7059 0.8780 0.2126 0.0563 -0.0617 926 PHE A CD2 6953 C CE1 . PHE A 926 ? 0.8628 0.5883 0.7564 0.2266 0.0447 -0.0698 926 PHE A CE1 6954 C CE2 . PHE A 926 ? 0.8939 0.6197 0.7983 0.2022 0.0449 -0.0599 926 PHE A CE2 6955 C CZ . PHE A 926 ? 0.8552 0.5867 0.7606 0.2103 0.0393 -0.0653 926 PHE A CZ 6956 N N . ASN A 927 ? 0.8905 0.6211 0.7521 0.2817 0.0670 -0.0786 927 ASN A N 6957 C CA . ASN A 927 ? 0.8474 0.6062 0.7218 0.2967 0.0663 -0.0771 927 ASN A CA 6958 C C . ASN A 927 ? 0.8540 0.5785 0.7203 0.3006 0.0525 -0.0820 927 ASN A C 6959 O O . ASN A 927 ? 0.8751 0.5554 0.7198 0.3058 0.0432 -0.0884 927 ASN A O 6960 C CB . ASN A 927 ? 0.8992 0.6829 0.7626 0.3290 0.0746 -0.0813 927 ASN A CB 6961 C CG . ASN A 927 ? 1.2230 1.0527 1.1051 0.3483 0.0765 -0.0767 927 ASN A CG 6962 O OD1 . ASN A 927 ? 1.5034 1.3536 1.4122 0.3316 0.0721 -0.0677 927 ASN A OD1 6963 N ND2 . ASN A 927 ? 1.3317 1.1790 1.1970 0.3873 0.0816 -0.0841 927 ASN A ND2 6964 N N . VAL A 928 ? 0.8601 0.6054 0.7444 0.2962 0.0484 -0.0763 928 VAL A N 6965 C CA . VAL A 928 ? 0.9006 0.6196 0.7770 0.2996 0.0359 -0.0760 928 VAL A CA 6966 C C . VAL A 928 ? 1.0117 0.7333 0.8836 0.3294 0.0306 -0.0793 928 VAL A C 6967 O O . VAL A 928 ? 1.1133 0.8811 1.0044 0.3403 0.0341 -0.0760 928 VAL A O 6968 C CB . VAL A 928 ? 0.8126 0.5489 0.7026 0.2835 0.0313 -0.0698 928 VAL A CB 6969 C CG1 . VAL A 928 ? 0.9909 0.7108 0.8721 0.2914 0.0200 -0.0654 928 VAL A CG1 6970 C CG2 . VAL A 928 ? 0.7989 0.5222 0.6837 0.2628 0.0331 -0.0699 928 VAL A CG2 6971 N N . ILE A 929 ? 0.8902 0.5613 0.7370 0.3428 0.0191 -0.0851 929 ILE A N 6972 C CA . ILE A 929 ? 1.0964 0.7550 0.9286 0.3787 0.0103 -0.0929 929 ILE A CA 6973 C C . ILE A 929 ? 1.1976 0.8323 1.0269 0.3855 -0.0063 -0.0858 929 ILE A C 6974 O O . ILE A 929 ? 1.4012 1.0253 1.2185 0.4192 -0.0156 -0.0922 929 ILE A O 6975 C CB . ILE A 929 ? 1.0811 0.6840 0.8792 0.3950 -0.0004 -0.1070 929 ILE A CB 6976 C CG1 . ILE A 929 ? 1.2081 0.7454 0.9938 0.3723 -0.0213 -0.1003 929 ILE A CG1 6977 C CG2 . ILE A 929 ? 0.9587 0.5842 0.7547 0.3903 0.0153 -0.1128 929 ILE A CG2 6978 C CD1 . ILE A 929 ? 1.5421 1.0225 1.2984 0.3770 -0.0407 -0.1120 929 ILE A CD1 6979 N N . GLU A 930 ? 1.0096 0.6381 0.8468 0.3581 -0.0102 -0.0721 930 GLU A N 6980 C CA . GLU A 930 ? 1.0467 0.6520 0.8780 0.3630 -0.0263 -0.0605 930 GLU A CA 6981 C C . GLU A 930 ? 1.0803 0.7093 0.9228 0.3384 -0.0236 -0.0450 930 GLU A C 6982 O O . GLU A 930 ? 0.9741 0.6199 0.8227 0.3164 -0.0130 -0.0440 930 GLU A O 6983 C CB . GLU A 930 ? 1.2123 0.7434 1.0187 0.3638 -0.0477 -0.0570 930 GLU A CB 6984 C CG . GLU A 930 ? 1.4824 0.9767 1.2765 0.3810 -0.0695 -0.0473 930 GLU A CG 6985 C CD . GLU A 930 ? 1.8184 1.2273 1.5855 0.3844 -0.0979 -0.0468 930 GLU A CD 6986 O OE1 . GLU A 930 ? 1.9398 1.3078 1.7010 0.3739 -0.1189 -0.0251 930 GLU A OE1 6987 O OE2 . GLU A 930 ? 1.9537 1.3391 1.7059 0.3940 -0.1013 -0.0664 930 GLU A OE2 6988 N N . PHE A 931 ? 1.2190 0.8480 1.0593 0.3469 -0.0345 -0.0337 931 PHE A N 6989 C CA . PHE A 931 ? 1.1833 0.8340 1.0249 0.3310 -0.0342 -0.0191 931 PHE A CA 6990 C C . PHE A 931 ? 1.2989 0.9164 1.1257 0.3335 -0.0506 0.0030 931 PHE A C 6991 O O . PHE A 931 ? 1.5267 1.1113 1.3458 0.3539 -0.0653 0.0035 931 PHE A O 6992 C CB . PHE A 931 ? 1.0878 0.7913 0.9449 0.3375 -0.0311 -0.0260 931 PHE A CB 6993 C CG . PHE A 931 ? 0.9367 0.6729 0.8116 0.3273 -0.0188 -0.0401 931 PHE A CG 6994 C CD1 . PHE A 931 ? 0.8639 0.6103 0.7371 0.3070 -0.0140 -0.0424 931 PHE A CD1 6995 C CD2 . PHE A 931 ? 0.9952 0.7528 0.8863 0.3404 -0.0131 -0.0492 931 PHE A CD2 6996 C CE1 . PHE A 931 ? 0.9392 0.7061 0.8277 0.2955 -0.0073 -0.0525 931 PHE A CE1 6997 C CE2 . PHE A 931 ? 1.0041 0.7943 0.9141 0.3270 -0.0028 -0.0550 931 PHE A CE2 6998 C CZ . PHE A 931 ? 1.0013 0.7908 0.9104 0.3023 -0.0017 -0.0562 931 PHE A CZ 6999 N N . PRO A 932 ? 1.1315 0.7584 0.9524 0.3150 -0.0488 0.0232 932 PRO A N 7000 C CA . PRO A 932 ? 1.2130 0.8165 1.0219 0.3120 -0.0632 0.0532 932 PRO A CA 7001 C C . PRO A 932 ? 1.3476 0.9638 1.1509 0.3329 -0.0732 0.0582 932 PRO A C 7002 O O . PRO A 932 ? 1.4946 1.0758 1.2874 0.3381 -0.0906 0.0797 932 PRO A O 7003 C CB . PRO A 932 ? 1.1564 0.7925 0.9624 0.2911 -0.0516 0.0728 932 PRO A CB 7004 C CG . PRO A 932 ? 1.1133 0.7911 0.9230 0.2936 -0.0353 0.0474 932 PRO A CG 7005 C CD . PRO A 932 ? 1.0614 0.7232 0.8842 0.2986 -0.0332 0.0209 932 PRO A CD 7006 N N . TYR A 933 ? 1.2854 0.9486 1.0962 0.3430 -0.0659 0.0404 933 TYR A N 7007 C CA . TYR A 933 ? 1.3234 1.0073 1.1313 0.3623 -0.0770 0.0445 933 TYR A CA 7008 C C . TYR A 933 ? 1.4432 1.1206 1.2633 0.3886 -0.0851 0.0299 933 TYR A C 7009 O O . TYR A 933 ? 1.5783 1.2833 1.4175 0.3928 -0.0757 0.0088 933 TYR A O 7010 C CB . TYR A 933 ? 1.2620 0.9998 1.0717 0.3592 -0.0718 0.0334 933 TYR A CB 7011 C CG . TYR A 933 ? 1.2630 1.0128 1.0654 0.3399 -0.0580 0.0288 933 TYR A CG 7012 C CD1 . TYR A 933 ? 1.3801 1.1378 1.1595 0.3343 -0.0545 0.0491 933 TYR A CD1 7013 C CD2 . TYR A 933 ? 1.1731 0.9307 0.9906 0.3303 -0.0483 0.0062 933 TYR A CD2 7014 C CE1 . TYR A 933 ? 1.1757 0.9494 0.9459 0.3245 -0.0416 0.0436 933 TYR A CE1 7015 C CE2 . TYR A 933 ? 1.2027 0.9666 1.0106 0.3175 -0.0381 0.0008 933 TYR A CE2 7016 C CZ . TYR A 933 ? 1.1307 0.9030 0.9142 0.3171 -0.0347 0.0177 933 TYR A CZ 7017 O OH . TYR A 933 ? 1.0984 0.8818 0.8700 0.3119 -0.0241 0.0111 933 TYR A OH 7018 N N . LYS A 934 ? 1.5165 1.1605 1.3249 0.4085 -0.1027 0.0435 934 LYS A N 7019 C CA . LYS A 934 ? 1.5899 1.2313 1.4053 0.4432 -0.1111 0.0294 934 LYS A CA 7020 C C . LYS A 934 ? 1.5460 1.2404 1.3723 0.4623 -0.1178 0.0311 934 LYS A C 7021 O O . LYS A 934 ? 1.4749 1.1966 1.2968 0.4488 -0.1195 0.0426 934 LYS A O 7022 C CB . LYS A 934 ? 1.7057 1.2675 1.4978 0.4605 -0.1320 0.0386 934 LYS A CB 7023 C CG . LYS A 934 ? 1.7397 1.2430 1.5206 0.4378 -0.1334 0.0403 934 LYS A CG 7024 C CD . LYS A 934 ? 1.6892 1.2150 1.4826 0.4359 -0.1143 0.0126 934 LYS A CD 7025 C CE . LYS A 934 ? 1.6254 1.0966 1.4079 0.4117 -0.1180 0.0148 934 LYS A CE 7026 N NZ . LYS A 934 ? 1.5733 1.0675 1.3648 0.4100 -0.0994 -0.0101 934 LYS A NZ 7027 N N . ASN A 935 ? 1.6285 1.3410 1.4672 0.4969 -0.1226 0.0195 935 ASN A N 7028 C CA . ASN A 935 ? 1.7406 1.5147 1.5980 0.5176 -0.1301 0.0206 935 ASN A CA 7029 C C . ASN A 935 ? 1.6589 1.5041 1.5430 0.4910 -0.1213 0.0146 935 ASN A C 7030 O O . ASN A 935 ? 1.5985 1.4912 1.4947 0.4960 -0.1327 0.0190 935 ASN A O 7031 C CB . ASN A 935 ? 1.7819 1.5280 1.6158 0.5295 -0.1511 0.0428 935 ASN A CB 7032 C CG . ASN A 935 ? 1.8108 1.4804 1.6192 0.5594 -0.1683 0.0497 935 ASN A CG 7033 O OD1 . ASN A 935 ? 1.9148 1.5124 1.6990 0.5426 -0.1745 0.0620 935 ASN A OD1 7034 N ND2 . ASN A 935 ? 1.6651 1.3495 1.4791 0.6045 -0.1790 0.0426 935 ASN A ND2 7035 N N . LEU A 936 ? 1.5217 1.3681 1.4126 0.4630 -0.1050 0.0042 936 LEU A N 7036 C CA . LEU A 936 ? 1.4492 1.3484 1.3635 0.4368 -0.1005 -0.0039 936 LEU A CA 7037 C C . LEU A 936 ? 1.4459 1.3790 1.3917 0.4333 -0.0855 -0.0152 936 LEU A C 7038 O O . LEU A 936 ? 1.4514 1.3495 1.3870 0.4291 -0.0717 -0.0212 936 LEU A O 7039 C CB . LEU A 936 ? 1.4358 1.3070 1.3256 0.4070 -0.0967 -0.0035 936 LEU A CB 7040 C CG . LEU A 936 ? 1.5370 1.4158 1.4043 0.4049 -0.1114 0.0051 936 LEU A CG 7041 C CD1 . LEU A 936 ? 1.6133 1.4608 1.4557 0.4250 -0.1203 0.0260 936 LEU A CD1 7042 C CD2 . LEU A 936 ? 1.7429 1.6089 1.5867 0.3822 -0.1051 0.0006 936 LEU A CD2 7043 N N . PRO A 937 ? 1.6002 1.6060 1.5855 0.4346 -0.0893 -0.0147 937 PRO A N 7044 C CA . PRO A 937 ? 1.6378 1.6906 1.6577 0.4287 -0.0741 -0.0177 937 PRO A CA 7045 C C . PRO A 937 ? 1.6747 1.6988 1.6877 0.3933 -0.0631 -0.0246 937 PRO A C 7046 O O . PRO A 937 ? 1.6052 1.6155 1.6103 0.3655 -0.0729 -0.0272 937 PRO A O 7047 C CB . PRO A 937 ? 1.6486 1.7863 1.7152 0.4207 -0.0872 -0.0087 937 PRO A CB 7048 C CG . PRO A 937 ? 1.7329 1.8711 1.7879 0.4440 -0.1063 -0.0037 937 PRO A CG 7049 C CD . PRO A 937 ? 1.7348 1.7886 1.7369 0.4400 -0.1095 -0.0075 937 PRO A CD 7050 N N . ILE A 938 ? 1.7296 1.7436 1.7413 0.3988 -0.0445 -0.0290 938 ILE A N 7051 C CA . ILE A 938 ? 1.5685 1.5488 1.5692 0.3704 -0.0337 -0.0351 938 ILE A CA 7052 C C . ILE A 938 ? 1.4133 1.4428 1.4455 0.3608 -0.0195 -0.0315 938 ILE A C 7053 O O . ILE A 938 ? 1.4393 1.5268 1.4962 0.3838 -0.0121 -0.0247 938 ILE A O 7054 C CB . ILE A 938 ? 1.5170 1.4249 1.4779 0.3807 -0.0267 -0.0419 938 ILE A CB 7055 C CG1 . ILE A 938 ? 1.3774 1.2807 1.3307 0.4207 -0.0228 -0.0453 938 ILE A CG1 7056 C CG2 . ILE A 938 ? 1.5571 1.4181 1.4889 0.3762 -0.0391 -0.0379 938 ILE A CG2 7057 C CD1 . ILE A 938 ? 1.3413 1.1652 1.2556 0.4290 -0.0246 -0.0519 938 ILE A CD1 7058 N N . GLU A 939 ? 1.3303 1.3401 1.3607 0.3291 -0.0155 -0.0338 939 GLU A N 7059 C CA . GLU A 939 ? 1.4730 1.5225 1.5300 0.3153 -0.0025 -0.0260 939 GLU A CA 7060 C C . GLU A 939 ? 1.4794 1.4752 1.5071 0.3090 0.0111 -0.0350 939 GLU A C 7061 O O . GLU A 939 ? 1.4182 1.3572 1.4191 0.2950 0.0055 -0.0439 939 GLU A O 7062 C CB . GLU A 939 ? 1.5924 1.6762 1.6840 0.2771 -0.0180 -0.0152 939 GLU A CB 7063 C CG . GLU A 939 ? 1.6996 1.8422 1.8252 0.2784 -0.0362 -0.0047 939 GLU A CG 7064 C CD . GLU A 939 ? 1.7225 1.8860 1.8797 0.2357 -0.0604 0.0050 939 GLU A CD 7065 O OE1 . GLU A 939 ? 1.7212 1.8519 1.8735 0.2073 -0.0621 0.0041 939 GLU A OE1 7066 O OE2 . GLU A 939 ? 1.7002 1.9091 1.8863 0.2306 -0.0815 0.0134 939 GLU A OE2 7067 N N . ASP A 940 ? 1.4744 1.4946 1.5064 0.3224 0.0289 -0.0317 940 ASP A N 7068 C CA . ASP A 940 ? 1.3309 1.3046 1.3348 0.3194 0.0403 -0.0401 940 ASP A CA 7069 C C . ASP A 940 ? 1.1069 1.0663 1.1178 0.2805 0.0375 -0.0358 940 ASP A C 7070 O O . ASP A 940 ? 1.1111 1.1127 1.1555 0.2571 0.0321 -0.0214 940 ASP A O 7071 C CB . ASP A 940 ? 1.3943 1.4042 1.3972 0.3470 0.0586 -0.0378 940 ASP A CB 7072 C CG . ASP A 940 ? 1.6278 1.6181 1.6029 0.3932 0.0577 -0.0513 940 ASP A CG 7073 O OD1 . ASP A 940 ? 1.5930 1.5141 1.5391 0.3965 0.0448 -0.0632 940 ASP A OD1 7074 O OD2 . ASP A 940 ? 1.8598 1.9046 1.8412 0.4276 0.0686 -0.0483 940 ASP A OD2 7075 N N . ILE A 941 ? 1.0653 0.9640 1.0450 0.2740 0.0384 -0.0470 941 ILE A N 7076 C CA . ILE A 941 ? 1.0464 0.9220 1.0246 0.2449 0.0348 -0.0462 941 ILE A CA 7077 C C . ILE A 941 ? 1.0551 0.9174 1.0201 0.2460 0.0494 -0.0462 941 ILE A C 7078 O O . ILE A 941 ? 1.1740 1.0014 1.1118 0.2613 0.0545 -0.0566 941 ILE A O 7079 C CB . ILE A 941 ? 1.0093 0.8347 0.9620 0.2388 0.0231 -0.0576 941 ILE A CB 7080 C CG1 . ILE A 941 ? 1.0211 0.8592 0.9794 0.2421 0.0081 -0.0581 941 ILE A CG1 7081 C CG2 . ILE A 941 ? 1.0040 0.8044 0.9510 0.2165 0.0168 -0.0597 941 ILE A CG2 7082 C CD1 . ILE A 941 ? 1.0080 0.8081 0.9363 0.2445 0.0001 -0.0664 941 ILE A CD1 7083 N N . THR A 942 ? 1.0709 0.9607 1.0559 0.2277 0.0531 -0.0322 942 THR A N 7084 C CA . THR A 942 ? 1.0985 0.9840 1.0713 0.2294 0.0671 -0.0287 942 THR A CA 7085 C C . THR A 942 ? 1.2747 1.1535 1.2598 0.1976 0.0606 -0.0155 942 THR A C 7086 O O . THR A 942 ? 1.5964 1.4968 1.6105 0.1746 0.0473 -0.0020 942 THR A O 7087 C CB . THR A 942 ? 1.2658 1.2106 1.2476 0.2531 0.0846 -0.0184 942 THR A CB 7088 O OG1 . THR A 942 ? 1.4455 1.3937 1.4172 0.2851 0.0846 -0.0308 942 THR A OG1 7089 C CG2 . THR A 942 ? 1.3041 1.2364 1.2594 0.2641 0.0981 -0.0206 942 THR A CG2 7090 N N . ASN A 943 ? 1.2162 1.0620 1.1789 0.1961 0.0663 -0.0187 943 ASN A N 7091 C CA . ASN A 943 ? 1.2761 1.1048 1.2440 0.1699 0.0586 -0.0062 943 ASN A CA 7092 C C . ASN A 943 ? 1.1881 0.9868 1.1274 0.1779 0.0682 -0.0111 943 ASN A C 7093 O O . ASN A 943 ? 1.1759 0.9562 1.0909 0.1990 0.0750 -0.0276 943 ASN A O 7094 C CB . ASN A 943 ? 1.3826 1.1661 1.3471 0.1532 0.0346 -0.0161 943 ASN A CB 7095 C CG . ASN A 943 ? 1.5275 1.3061 1.5130 0.1211 0.0160 0.0027 943 ASN A CG 7096 O OD1 . ASN A 943 ? 1.5622 1.3428 1.5512 0.1093 0.0207 0.0206 943 ASN A OD1 7097 N ND2 . ASN A 943 ? 1.8079 1.5767 1.8059 0.1058 -0.0086 0.0003 943 ASN A ND2 7098 N N . SER A 944 ? 1.1279 0.9195 1.0712 0.1589 0.0650 0.0054 944 SER A N 7099 C CA . SER A 944 ? 1.1080 0.8789 1.0261 0.1666 0.0736 0.0047 944 SER A CA 7100 C C . SER A 944 ? 1.1944 0.9154 1.1041 0.1489 0.0574 0.0074 944 SER A C 7101 O O . SER A 944 ? 1.4838 1.1880 1.4084 0.1274 0.0383 0.0147 944 SER A O 7102 C CB . SER A 944 ? 1.1371 0.9620 1.0614 0.1715 0.0918 0.0273 944 SER A CB 7103 O OG . SER A 944 ? 1.4423 1.3126 1.3689 0.1961 0.1054 0.0221 944 SER A OG 7104 N N . THR A 945 ? 1.0065 0.7004 0.8901 0.1599 0.0616 0.0004 945 THR A N 7105 C CA . THR A 945 ? 1.0060 0.6530 0.8770 0.1505 0.0472 0.0032 945 THR A CA 7106 C C . THR A 945 ? 0.9907 0.6365 0.8414 0.1611 0.0580 0.0085 945 THR A C 7107 O O . THR A 945 ? 0.9776 0.6443 0.8166 0.1791 0.0720 -0.0004 945 THR A O 7108 C CB . THR A 945 ? 0.9688 0.5715 0.8232 0.1607 0.0332 -0.0214 945 THR A CB 7109 O OG1 . THR A 945 ? 1.3332 0.8875 1.1734 0.1561 0.0155 -0.0197 945 THR A OG1 7110 C CG2 . THR A 945 ? 0.9139 0.5207 0.7515 0.1832 0.0449 -0.0383 945 THR A CG2 7111 N N . LEU A 946 ? 1.1099 0.7262 0.9539 0.1504 0.0476 0.0226 946 LEU A N 7112 C CA . LEU A 946 ? 1.0473 0.6626 0.8707 0.1602 0.0554 0.0301 946 LEU A CA 7113 C C . LEU A 946 ? 0.9581 0.5199 0.7608 0.1682 0.0402 0.0194 946 LEU A C 7114 O O . LEU A 946 ? 0.9730 0.4929 0.7755 0.1618 0.0207 0.0153 946 LEU A O 7115 C CB . LEU A 946 ? 1.1096 0.7531 0.9429 0.1430 0.0610 0.0664 946 LEU A CB 7116 C CG . LEU A 946 ? 1.2177 0.8249 1.0613 0.1152 0.0397 0.0924 946 LEU A CG 7117 C CD1 . LEU A 946 ? 1.2588 0.9024 1.1073 0.1019 0.0496 0.1335 946 LEU A CD1 7118 C CD2 . LEU A 946 ? 1.3374 0.9380 1.2100 0.0915 0.0225 0.0958 946 LEU A CD2 7119 N N . VAL A 947 ? 0.9467 0.5106 0.7297 0.1854 0.0468 0.0137 947 VAL A N 7120 C CA . VAL A 947 ? 0.9864 0.5122 0.7512 0.1983 0.0346 0.0057 947 VAL A CA 7121 C C . VAL A 947 ? 1.0849 0.6086 0.8338 0.2002 0.0357 0.0244 947 VAL A C 7122 O O . VAL A 947 ? 1.2897 0.8463 1.0305 0.2069 0.0488 0.0272 947 VAL A O 7123 C CB . VAL A 947 ? 0.9261 0.4625 0.6863 0.2181 0.0379 -0.0180 947 VAL A CB 7124 C CG1 . VAL A 947 ? 0.9442 0.4617 0.6882 0.2354 0.0293 -0.0211 947 VAL A CG1 7125 C CG2 . VAL A 947 ? 0.9125 0.4453 0.6828 0.2192 0.0342 -0.0334 947 VAL A CG2 7126 N N . THR A 948 ? 1.0712 0.5510 0.8111 0.1964 0.0190 0.0365 948 THR A N 7127 C CA . THR A 948 ? 1.0670 0.5409 0.7913 0.1959 0.0178 0.0600 948 THR A CA 7128 C C . THR A 948 ? 1.1060 0.5490 0.8086 0.2198 0.0060 0.0495 948 THR A C 7129 O O . THR A 948 ? 1.1143 0.5186 0.8118 0.2321 -0.0095 0.0340 948 THR A O 7130 C CB . THR A 948 ? 1.1834 0.6312 0.9160 0.1684 0.0050 0.0934 948 THR A CB 7131 O OG1 . THR A 948 ? 1.4747 0.9086 1.1886 0.1697 0.0006 0.1185 948 THR A OG1 7132 C CG2 . THR A 948 ? 1.1916 0.5755 0.9259 0.1629 -0.0224 0.0828 948 THR A CG2 7133 N N . THR A 949 ? 1.1832 0.6475 0.8706 0.2301 0.0128 0.0572 949 THR A N 7134 C CA . THR A 949 ? 1.2002 0.6428 0.8689 0.2523 0.0008 0.0538 949 THR A CA 7135 C C . THR A 949 ? 1.3632 0.7902 1.0138 0.2468 -0.0044 0.0853 949 THR A C 7136 O O . THR A 949 ? 1.5442 1.0089 1.1860 0.2442 0.0087 0.0988 949 THR A O 7137 C CB . THR A 949 ? 1.0825 0.5658 0.7498 0.2703 0.0080 0.0350 949 THR A CB 7138 O OG1 . THR A 949 ? 1.1376 0.6386 0.8238 0.2716 0.0129 0.0124 949 THR A OG1 7139 C CG2 . THR A 949 ? 1.0858 0.5567 0.7397 0.2941 -0.0053 0.0335 949 THR A CG2 7140 N N . ASN A 950 ? 1.3337 0.7020 0.9745 0.2475 -0.0255 0.0972 950 ASN A N 7141 C CA . ASN A 950 ? 1.4390 0.7847 1.0643 0.2372 -0.0338 0.1341 950 ASN A CA 7142 C C . ASN A 950 ? 1.4378 0.7714 1.0373 0.2653 -0.0432 0.1346 950 ASN A C 7143 O O . ASN A 950 ? 1.6745 0.9634 1.2639 0.2880 -0.0623 0.1207 950 ASN A O 7144 C CB . ASN A 950 ? 1.5566 0.8338 1.1855 0.2161 -0.0585 0.1530 950 ASN A CB 7145 C CG . ASN A 950 ? 1.6110 0.9033 1.2691 0.1850 -0.0532 0.1567 950 ASN A CG 7146 O OD1 . ASN A 950 ? 1.5497 0.8853 1.2229 0.1890 -0.0358 0.1315 950 ASN A OD1 7147 N ND2 . ASN A 950 ? 1.8916 1.1485 1.5599 0.1521 -0.0709 0.1911 950 ASN A ND2 7148 N N . VAL A 951 ? 1.3900 0.7656 0.9762 0.2676 -0.0309 0.1502 951 VAL A N 7149 C CA . VAL A 951 ? 1.3711 0.7399 0.9324 0.2923 -0.0413 0.1550 951 VAL A CA 7150 C C . VAL A 951 ? 1.4142 0.7457 0.9562 0.2810 -0.0532 0.1986 951 VAL A C 7151 O O . VAL A 951 ? 1.4252 0.7848 0.9658 0.2586 -0.0401 0.2302 951 VAL A O 7152 C CB . VAL A 951 ? 1.2825 0.7147 0.8345 0.3046 -0.0272 0.1435 951 VAL A CB 7153 C CG1 . VAL A 951 ? 1.3917 0.8685 0.9428 0.2862 -0.0056 0.1551 951 VAL A CG1 7154 C CG2 . VAL A 951 ? 1.3526 0.7816 0.8764 0.3250 -0.0392 0.1577 951 VAL A CG2 7155 N N . THR A 952 ? 1.4562 0.7265 0.9827 0.2984 -0.0784 0.2027 952 THR A N 7156 C CA . THR A 952 ? 1.5448 0.7625 1.0532 0.2857 -0.0966 0.2464 952 THR A CA 7157 C C . THR A 952 ? 1.6904 0.8800 1.1690 0.3191 -0.1151 0.2511 952 THR A C 7158 O O . THR A 952 ? 1.7371 0.9564 1.2127 0.3519 -0.1130 0.2208 952 THR A O 7159 C CB . THR A 952 ? 1.6365 0.7738 1.1545 0.2654 -0.1215 0.2539 952 THR A CB 7160 O OG1 . THR A 952 ? 2.0081 1.0821 1.5074 0.2528 -0.1466 0.2984 952 THR A OG1 7161 C CG2 . THR A 952 ? 1.5719 0.6638 1.0860 0.2988 -0.1391 0.2091 952 THR A CG2 7162 N N . TRP A 953 ? 1.8331 0.9679 1.2923 0.3093 -0.1349 0.2928 953 TRP A N 7163 C CA . TRP A 953 ? 1.9253 1.0265 1.3533 0.3413 -0.1555 0.3030 953 TRP A CA 7164 C C . TRP A 953 ? 1.9748 0.9651 1.3883 0.3515 -0.1946 0.3078 953 TRP A C 7165 O O . TRP A 953 ? 1.9618 0.8963 1.3807 0.3158 -0.2111 0.3392 953 TRP A O 7166 C CB . TRP A 953 ? 2.0178 1.1489 1.4249 0.3279 -0.1478 0.3517 953 TRP A CB 7167 C CG . TRP A 953 ? 1.9691 1.1988 1.3738 0.3339 -0.1172 0.3404 953 TRP A CG 7168 C CD1 . TRP A 953 ? 1.8186 1.1127 1.2390 0.3112 -0.0884 0.3386 953 TRP A CD1 7169 C CD2 . TRP A 953 ? 1.9883 1.2583 1.3703 0.3671 -0.1170 0.3278 953 TRP A CD2 7170 N NE1 . TRP A 953 ? 1.7545 1.1178 1.1581 0.3302 -0.0724 0.3228 953 TRP A NE1 7171 C CE2 . TRP A 953 ? 1.7688 1.1190 1.1502 0.3617 -0.0907 0.3164 953 TRP A CE2 7172 C CE3 . TRP A 953 ? 2.1106 1.3565 1.4721 0.4025 -0.1393 0.3245 953 TRP A CE3 7173 C CZ2 . TRP A 953 ? 1.7582 1.1580 1.1178 0.3869 -0.0897 0.3010 953 TRP A CZ2 7174 C CZ3 . TRP A 953 ? 2.0593 1.3653 1.4053 0.4259 -0.1355 0.3122 953 TRP A CZ3 7175 C CH2 . TRP A 953 ? 1.8942 1.2731 1.2386 0.4162 -0.1126 0.3001 953 TRP A CH2 7176 N N . GLY A 954 ? 2.0081 0.9938 1.4204 0.3921 -0.2067 0.2717 954 GLY A N 7177 C CA . GLY A 954 ? 2.1353 1.0570 1.5511 0.3992 -0.2363 0.2603 954 GLY A CA 7178 C C . GLY A 954 ? 2.2768 1.1596 1.6749 0.3955 -0.2566 0.3008 954 GLY A C 7179 O O . GLY A 954 ? 2.2423 1.0553 1.6403 0.3870 -0.2841 0.3073 954 GLY A O 7180 N N . ILE A 955 ? 2.3890 1.3168 1.7692 0.4028 -0.2441 0.3277 955 ILE A N 7181 C CA . ILE A 955 ? 2.5000 1.4017 1.8620 0.3997 -0.2605 0.3708 955 ILE A CA 7182 C C . ILE A 955 ? 2.5472 1.4882 1.8923 0.3724 -0.2422 0.4237 955 ILE A C 7183 O O . ILE A 955 ? 2.3865 1.3948 1.7182 0.3839 -0.2164 0.4158 955 ILE A O 7184 C CB . ILE A 955 ? 2.4058 1.3293 1.7541 0.4490 -0.2684 0.3497 955 ILE A CB 7185 C CG1 . ILE A 955 ? 2.3085 1.3179 1.6569 0.4766 -0.2442 0.3192 955 ILE A CG1 7186 C CG2 . ILE A 955 ? 2.2928 1.1657 1.6474 0.4757 -0.2914 0.3130 955 ILE A CG2 7187 C CD1 . ILE A 955 ? 2.2713 1.3157 1.6136 0.5222 -0.2523 0.3007 955 ILE A CD1 7188 N N . GLN A 956 ? 2.6545 1.5580 1.9992 0.3372 -0.2549 0.4787 956 GLN A N 7189 C CA . GLN A 956 ? 2.4923 1.4420 1.8193 0.3102 -0.2359 0.5368 956 GLN A CA 7190 C C . GLN A 956 ? 2.4079 1.3598 1.7119 0.3208 -0.2471 0.5766 956 GLN A C 7191 O O . GLN A 956 ? 2.4082 1.3498 1.7135 0.2870 -0.2515 0.6384 956 GLN A O 7192 C CB . GLN A 956 ? 2.4843 1.4130 1.8357 0.2533 -0.2359 0.5815 956 GLN A CB 7193 C CG . GLN A 956 ? 2.3768 1.3181 1.7474 0.2377 -0.2207 0.5521 956 GLN A CG 7194 C CD . GLN A 956 ? 2.3331 1.2123 1.7307 0.2462 -0.2432 0.4983 956 GLN A CD 7195 O OE1 . GLN A 956 ? 2.4610 1.2825 1.8605 0.2615 -0.2708 0.4849 956 GLN A OE1 7196 N NE2 . GLN A 956 ? 2.1706 1.0634 1.5838 0.2395 -0.2306 0.4663 956 GLN A NE2 7224 N N . CYS B 5 ? 2.4762 2.2514 2.3026 -0.1084 -0.1636 0.1289 5 CYS B N 7225 C CA . CYS B 5 ? 2.3149 2.0311 2.1410 -0.1561 -0.1672 0.1162 5 CYS B CA 7226 C C . CYS B 5 ? 2.2627 1.9892 2.0830 -0.1681 -0.1828 0.1172 5 CYS B C 7227 O O . CYS B 5 ? 2.2471 1.9194 2.0351 -0.1821 -0.1905 0.0998 5 CYS B O 7228 C CB . CYS B 5 ? 2.1795 1.9072 2.0537 -0.1941 -0.1599 0.1272 5 CYS B CB 7229 S SG . CYS B 5 ? 1.9740 1.6708 1.8527 -0.1907 -0.1428 0.1223 5 CYS B SG 7230 N N . THR B 6 ? 2.1779 1.9831 2.0312 -0.1629 -0.1876 0.1418 6 THR B N 7231 C CA . THR B 6 ? 2.1115 1.9347 1.9665 -0.1766 -0.2044 0.1458 6 THR B CA 7232 C C . THR B 6 ? 2.1375 1.9522 1.9491 -0.1387 -0.2157 0.1375 6 THR B C 7233 O O . THR B 6 ? 2.2430 2.0634 2.0472 -0.1473 -0.2307 0.1387 6 THR B O 7234 C CB . THR B 6 ? 2.0693 1.9874 1.9844 -0.1886 -0.2097 0.1821 6 THR B CB 7235 O OG1 . THR B 6 ? 2.0620 2.0634 1.9879 -0.1432 -0.1997 0.2050 6 THR B OG1 7236 C CG2 . THR B 6 ? 2.0985 2.0145 2.0639 -0.2321 -0.2105 0.1944 6 THR B CG2 7237 N N . THR B 7 ? 2.0581 1.8563 1.8417 -0.0950 -0.2137 0.1283 7 THR B N 7238 C CA . THR B 7 ? 2.0671 1.8433 1.8107 -0.0543 -0.2342 0.1179 7 THR B CA 7239 C C . THR B 7 ? 2.0771 1.7513 1.7777 -0.0645 -0.2480 0.0993 7 THR B C 7240 O O . THR B 7 ? 2.2143 1.8540 1.8844 -0.0381 -0.2735 0.0938 7 THR B O 7241 C CB . THR B 7 ? 2.0768 1.8971 1.8125 0.0108 -0.2360 0.1158 7 THR B CB 7242 O OG1 . THR B 7 ? 2.0640 1.8598 1.7968 0.0166 -0.2224 0.1071 7 THR B OG1 7243 C CG2 . THR B 7 ? 2.0853 2.0317 1.8627 0.0281 -0.2258 0.1438 7 THR B CG2 7244 N N . ARG B 8 ? 2.0429 1.6730 1.7446 -0.1024 -0.2344 0.0932 8 ARG B N 7245 C CA . ARG B 8 ? 2.0589 1.6095 1.7274 -0.1143 -0.2455 0.0848 8 ARG B CA 7246 C C . ARG B 8 ? 2.0624 1.5956 1.7284 -0.1633 -0.2359 0.0842 8 ARG B C 7247 O O . ARG B 8 ? 2.0791 1.5981 1.7234 -0.1771 -0.2498 0.0899 8 ARG B O 7248 C CB . ARG B 8 ? 1.9845 1.4973 1.6476 -0.0969 -0.2418 0.0757 8 ARG B CB 7249 C CG . ARG B 8 ? 2.0452 1.5475 1.6893 -0.0393 -0.2654 0.0675 8 ARG B CG 7250 C CD . ARG B 8 ? 2.0967 1.5670 1.7359 -0.0212 -0.2630 0.0556 8 ARG B CD 7251 N NE . ARG B 8 ? 2.1384 1.5832 1.7501 0.0392 -0.2959 0.0394 8 ARG B NE 7252 C CZ . ARG B 8 ? 2.1188 1.6287 1.7293 0.0948 -0.2947 0.0313 8 ARG B CZ 7253 N NH1 . ARG B 8 ? 2.0946 1.7037 1.7374 0.0894 -0.2616 0.0476 8 ARG B NH1 7254 N NH2 . ARG B 8 ? 2.1532 1.6332 1.7315 0.1575 -0.3306 0.0083 8 ARG B NH2 7255 N N . GLY B 9 ? 1.9890 1.5281 1.6760 -0.1855 -0.2140 0.0770 9 GLY B N 7256 C CA . GLY B 9 ? 1.9704 1.4917 1.6493 -0.2200 -0.2053 0.0686 9 GLY B CA 7257 C C . GLY B 9 ? 1.9798 1.5321 1.6642 -0.2427 -0.2076 0.0622 9 GLY B C 7258 O O . GLY B 9 ? 2.0640 1.6109 1.7450 -0.2633 -0.2002 0.0470 9 GLY B O 7259 N N . VAL B 10 ? 1.9633 1.5496 1.6554 -0.2352 -0.2211 0.0713 10 VAL B N 7260 C CA . VAL B 10 ? 2.0001 1.6134 1.6978 -0.2562 -0.2308 0.0651 10 VAL B CA 7261 C C . VAL B 10 ? 2.0355 1.6356 1.6901 -0.2683 -0.2369 0.0584 10 VAL B C 7262 O O . VAL B 10 ? 2.0610 1.6770 1.7089 -0.2841 -0.2445 0.0440 10 VAL B O 7263 C CB . VAL B 10 ? 2.0723 1.7324 1.7905 -0.2450 -0.2455 0.0819 10 VAL B CB 7264 C CG1 . VAL B 10 ? 2.0802 1.7683 1.8209 -0.2709 -0.2596 0.0765 10 VAL B CG1 7265 C CG2 . VAL B 10 ? 2.0857 1.7770 1.8380 -0.2217 -0.2372 0.0972 10 VAL B CG2 7266 N N . SER B 11 ? 2.0761 1.6503 1.7026 -0.2604 -0.2374 0.0711 11 SER B N 7267 C CA . SER B 11 ? 2.1069 1.6826 1.6961 -0.2732 -0.2431 0.0782 11 SER B CA 7268 C C . SER B 11 ? 2.1311 1.7189 1.7079 -0.2892 -0.2274 0.0581 11 SER B C 7269 O O . SER B 11 ? 2.1723 1.7901 1.7223 -0.2972 -0.2320 0.0518 11 SER B O 7270 C CB . SER B 11 ? 2.0888 1.6304 1.6626 -0.2666 -0.2529 0.1041 11 SER B CB 7271 O OG . SER B 11 ? 2.0438 1.5547 1.6304 -0.2630 -0.2403 0.1007 11 SER B OG 7272 N N . SER B 12 ? 2.1747 1.7436 1.7686 -0.2890 -0.2102 0.0461 12 SER B N 7273 C CA . SER B 12 ? 2.1937 1.7754 1.7759 -0.2962 -0.1961 0.0242 12 SER B CA 7274 C C . SER B 12 ? 2.2100 1.7703 1.8249 -0.2943 -0.1845 0.0018 12 SER B C 7275 O O . SER B 12 ? 2.1981 1.7424 1.8465 -0.2907 -0.1867 0.0064 12 SER B O 7276 C CB . SER B 12 ? 2.1283 1.7188 1.6863 -0.3012 -0.1871 0.0474 12 SER B CB 7277 O OG . SER B 12 ? 2.1240 1.7404 1.6717 -0.3012 -0.1701 0.0267 12 SER B OG 7278 N N . CYS B 13 ? 2.2190 1.7870 1.8240 -0.2943 -0.1730 -0.0203 13 CYS B N 7279 C CA . CYS B 13 ? 2.1409 1.6854 1.7759 -0.2920 -0.1647 -0.0414 13 CYS B CA 7280 C C . CYS B 13 ? 2.0190 1.5448 1.6634 -0.2904 -0.1468 -0.0220 13 CYS B C 7281 O O . CYS B 13 ? 1.9203 1.4200 1.5952 -0.2883 -0.1447 -0.0144 13 CYS B O 7282 C CB . CYS B 13 ? 2.1887 1.7485 1.8076 -0.2849 -0.1659 -0.0812 13 CYS B CB 7283 S SG . CYS B 13 ? 2.3618 1.8902 2.0135 -0.2787 -0.1572 -0.1060 13 CYS B SG 7284 N N . GLN B 14 ? 1.9753 1.5222 1.5947 -0.2914 -0.1356 -0.0114 14 GLN B N 7285 C CA . GLN B 14 ? 1.9720 1.5029 1.6011 -0.2937 -0.1243 0.0106 14 GLN B CA 7286 C C . GLN B 14 ? 1.9546 1.4480 1.5939 -0.2926 -0.1370 0.0377 14 GLN B C 7287 O O . GLN B 14 ? 1.9819 1.4445 1.6399 -0.2880 -0.1339 0.0430 14 GLN B O 7288 C CB . GLN B 14 ? 2.0172 1.5928 1.6215 -0.3003 -0.1163 0.0314 14 GLN B CB 7289 C CG . GLN B 14 ? 1.9877 1.5500 1.6074 -0.3079 -0.1104 0.0599 14 GLN B CG 7290 C CD . GLN B 14 ? 2.0090 1.6320 1.6127 -0.3198 -0.1049 0.0932 14 GLN B CD 7291 O OE1 . GLN B 14 ? 2.0103 1.6909 1.5865 -0.3195 -0.1036 0.0959 14 GLN B OE1 7292 N NE2 . GLN B 14 ? 2.0834 1.7019 1.7062 -0.3308 -0.1033 0.1227 14 GLN B NE2 7293 N N . GLN B 15 ? 1.9302 1.4275 1.5548 -0.2924 -0.1539 0.0515 15 GLN B N 7294 C CA . GLN B 15 ? 1.9458 1.4092 1.5750 -0.2816 -0.1718 0.0703 15 GLN B CA 7295 C C . GLN B 15 ? 1.8781 1.3330 1.5333 -0.2654 -0.1694 0.0554 15 GLN B C 7296 O O . GLN B 15 ? 1.8484 1.2800 1.5096 -0.2468 -0.1782 0.0630 15 GLN B O 7297 C CB . GLN B 15 ? 2.0956 1.5690 1.7031 -0.2828 -0.1929 0.0884 15 GLN B CB 7298 C CG . GLN B 15 ? 2.2241 1.7124 1.8102 -0.3008 -0.2005 0.1182 15 GLN B CG 7299 C CD . GLN B 15 ? 2.3217 1.8148 1.8895 -0.3025 -0.2260 0.1413 15 GLN B CD 7300 O OE1 . GLN B 15 ? 2.4277 1.9170 1.9965 -0.2881 -0.2358 0.1299 15 GLN B OE1 7301 N NE2 . GLN B 15 ? 2.2648 1.7728 1.8194 -0.3212 -0.2385 0.1790 15 GLN B NE2 7302 N N . CYS B 16 ? 1.8609 1.3389 1.5323 -0.2710 -0.1614 0.0358 16 CYS B N 7303 C CA . CYS B 16 ? 1.7935 1.2779 1.4992 -0.2627 -0.1599 0.0324 16 CYS B CA 7304 C C . CYS B 16 ? 1.7131 1.1793 1.4400 -0.2607 -0.1454 0.0277 16 CYS B C 7305 O O . CYS B 16 ? 1.6474 1.1189 1.3969 -0.2477 -0.1433 0.0359 16 CYS B O 7306 C CB . CYS B 16 ? 1.7794 1.2889 1.5035 -0.2757 -0.1667 0.0196 16 CYS B CB 7307 S SG . CYS B 16 ? 1.5106 1.0422 1.2908 -0.2758 -0.1691 0.0302 16 CYS B SG 7308 N N . LEU B 17 ? 1.7592 1.2135 1.4781 -0.2710 -0.1350 0.0161 17 LEU B N 7309 C CA . LEU B 17 ? 1.7218 1.1585 1.4606 -0.2697 -0.1220 0.0113 17 LEU B CA 7310 C C . LEU B 17 ? 1.6213 1.0354 1.3556 -0.2552 -0.1236 0.0282 17 LEU B C 7311 O O . LEU B 17 ? 1.5589 0.9646 1.3135 -0.2469 -0.1170 0.0286 17 LEU B O 7312 C CB . LEU B 17 ? 1.6537 1.0923 1.3823 -0.2784 -0.1113 -0.0041 17 LEU B CB 7313 C CG . LEU B 17 ? 1.5218 0.9603 1.2744 -0.2812 -0.1098 -0.0312 17 LEU B CG 7314 C CD1 . LEU B 17 ? 1.6095 1.0590 1.3678 -0.2865 -0.1277 -0.0431 17 LEU B CD1 7315 C CD2 . LEU B 17 ? 1.5347 0.9841 1.2725 -0.2787 -0.0993 -0.0513 17 LEU B CD2 7316 N N . ALA B 18 ? 1.6317 1.0332 1.3396 -0.2511 -0.1376 0.0422 18 ALA B N 7317 C CA . ALA B 18 ? 1.6761 1.0473 1.3781 -0.2304 -0.1519 0.0524 18 ALA B CA 7318 C C . ALA B 18 ? 1.7057 1.0862 1.3988 -0.2067 -0.1688 0.0559 18 ALA B C 7319 O O . ALA B 18 ? 1.7605 1.1323 1.4331 -0.2062 -0.1879 0.0648 18 ALA B O 7320 C CB . ALA B 18 ? 1.7483 1.0874 1.4337 -0.2406 -0.1669 0.0684 18 ALA B CB 7321 N N . VAL B 19 ? 1.6897 1.0957 1.4005 -0.1857 -0.1623 0.0522 19 VAL B N 7322 C CA . VAL B 19 ? 1.8623 1.2873 1.5652 -0.1491 -0.1769 0.0550 19 VAL B CA 7323 C C . VAL B 19 ? 1.8907 1.3256 1.6025 -0.1210 -0.1708 0.0519 19 VAL B C 7324 O O . VAL B 19 ? 2.0338 1.4380 1.7231 -0.0882 -0.1899 0.0446 19 VAL B O 7325 C CB . VAL B 19 ? 2.0574 1.5414 1.7779 -0.1517 -0.1721 0.0617 19 VAL B CB 7326 C CG1 . VAL B 19 ? 2.0824 1.6043 1.7975 -0.1067 -0.1837 0.0661 19 VAL B CG1 7327 C CG2 . VAL B 19 ? 2.2050 1.6812 1.9119 -0.1771 -0.1801 0.0623 19 VAL B CG2 7328 N N . SER B 20 ? 1.7752 1.2527 1.5211 -0.1344 -0.1484 0.0581 20 SER B N 7329 C CA . SER B 20 ? 1.7516 1.2490 1.5133 -0.1180 -0.1371 0.0615 20 SER B CA 7330 C C . SER B 20 ? 1.6379 1.1308 1.4332 -0.1568 -0.1191 0.0641 20 SER B C 7331 O O . SER B 20 ? 1.6078 1.1067 1.4201 -0.1865 -0.1167 0.0644 20 SER B O 7332 C CB . SER B 20 ? 1.8018 1.3811 1.5784 -0.0862 -0.1334 0.0773 20 SER B CB 7333 O OG . SER B 20 ? 1.7843 1.3971 1.5764 -0.0704 -0.1213 0.0862 20 SER B OG 7334 N N . PRO B 21 ? 1.6037 1.0825 1.4071 -0.1536 -0.1108 0.0631 21 PRO B N 7335 C CA . PRO B 21 ? 1.5618 1.0318 1.3983 -0.1852 -0.0977 0.0635 21 PRO B CA 7336 C C . PRO B 21 ? 1.5821 1.1014 1.4644 -0.2032 -0.0948 0.0820 21 PRO B C 7337 O O . PRO B 21 ? 1.6253 1.1274 1.5359 -0.2310 -0.0941 0.0780 21 PRO B O 7338 C CB . PRO B 21 ? 1.5456 1.0035 1.3821 -0.1694 -0.0924 0.0641 21 PRO B CB 7339 C CG . PRO B 21 ? 1.6650 1.1444 1.4738 -0.1253 -0.1024 0.0659 21 PRO B CG 7340 C CD . PRO B 21 ? 1.6730 1.1359 1.4526 -0.1179 -0.1184 0.0574 21 PRO B CD 7341 N N . MET B 22 ? 1.6429 1.2247 1.5351 -0.1863 -0.0976 0.1032 22 MET B N 7342 C CA . MET B 22 ? 1.7931 1.4320 1.7375 -0.2077 -0.1006 0.1323 22 MET B CA 7343 C C . MET B 22 ? 1.8193 1.4458 1.7717 -0.2353 -0.1145 0.1247 22 MET B C 7344 O O . MET B 22 ? 1.8922 1.5393 1.8921 -0.2639 -0.1266 0.1424 22 MET B O 7345 C CB . MET B 22 ? 1.8622 1.5939 1.8171 -0.1769 -0.0970 0.1645 22 MET B CB 7346 C CG . MET B 22 ? 1.8687 1.6176 1.7828 -0.1427 -0.1026 0.1536 22 MET B CG 7347 S SD . MET B 22 ? 2.0946 1.9683 2.0144 -0.0911 -0.0968 0.1856 22 MET B SD 7348 C CE . MET B 22 ? 2.2724 2.1383 2.1683 -0.0556 -0.0868 0.1764 22 MET B CE 7349 N N . CYS B 23 ? 1.7568 1.3485 1.6641 -0.2274 -0.1176 0.1003 23 CYS B N 7350 C CA . CYS B 23 ? 1.7892 1.3759 1.6944 -0.2473 -0.1312 0.0917 23 CYS B CA 7351 C C . CYS B 23 ? 1.7512 1.2952 1.6709 -0.2781 -0.1392 0.0708 23 CYS B C 7352 O O . CYS B 23 ? 1.7435 1.2503 1.6610 -0.2808 -0.1311 0.0559 23 CYS B O 7353 C CB . CYS B 23 ? 1.8198 1.3816 1.6721 -0.2310 -0.1336 0.0752 23 CYS B CB 7354 S SG . CYS B 23 ? 2.7536 2.3504 2.5816 -0.1844 -0.1359 0.0880 23 CYS B SG 7355 N N . ALA B 24 ? 1.7802 1.3311 1.7135 -0.2974 -0.1584 0.0673 24 ALA B N 7356 C CA . ALA B 24 ? 1.8179 1.3271 1.7573 -0.3177 -0.1743 0.0382 24 ALA B CA 7357 C C . ALA B 24 ? 1.9326 1.4388 1.8403 -0.3212 -0.1882 0.0176 24 ALA B C 7358 O O . ALA B 24 ? 1.9748 1.5087 1.8609 -0.3117 -0.1851 0.0300 24 ALA B O 7359 C CB . ALA B 24 ? 1.7232 1.2368 1.7271 -0.3418 -0.1982 0.0553 24 ALA B CB 7360 N N . TRP B 25 ? 1.9599 1.4339 1.8628 -0.3308 -0.2061 -0.0160 25 TRP B N 7361 C CA . TRP B 25 ? 2.0052 1.4804 1.8709 -0.3301 -0.2196 -0.0402 25 TRP B CA 7362 C C . TRP B 25 ? 2.0922 1.5453 1.9821 -0.3448 -0.2600 -0.0651 25 TRP B C 7363 O O . TRP B 25 ? 2.1425 1.5632 2.0684 -0.3523 -0.2772 -0.0750 25 TRP B O 7364 C CB . TRP B 25 ? 1.9824 1.4480 1.7911 -0.3135 -0.1988 -0.0658 25 TRP B CB 7365 C CG . TRP B 25 ? 2.0334 1.5123 1.8004 -0.3102 -0.2109 -0.0880 25 TRP B CG 7366 C CD1 . TRP B 25 ? 2.1160 1.5876 1.8567 -0.3014 -0.2232 -0.1300 25 TRP B CD1 7367 C CD2 . TRP B 25 ? 2.1077 1.6147 1.8524 -0.3113 -0.2145 -0.0708 25 TRP B CD2 7368 N NE1 . TRP B 25 ? 2.2115 1.7099 1.9124 -0.2978 -0.2323 -0.1384 25 TRP B NE1 7369 C CE2 . TRP B 25 ? 2.1922 1.7097 1.8973 -0.3066 -0.2275 -0.1005 25 TRP B CE2 7370 C CE3 . TRP B 25 ? 2.1274 1.6550 1.8799 -0.3110 -0.2097 -0.0352 25 TRP B CE3 7371 C CZ2 . TRP B 25 ? 2.2173 1.7631 1.8932 -0.3072 -0.2350 -0.0910 25 TRP B CZ2 7372 C CZ3 . TRP B 25 ? 2.1135 1.6643 1.8387 -0.3097 -0.2188 -0.0281 25 TRP B CZ3 7373 C CH2 . TRP B 25 ? 2.1462 1.7049 1.8347 -0.3106 -0.2310 -0.0536 25 TRP B CH2 7374 N N . CYS B 26 ? 2.0982 1.5636 1.9685 -0.3480 -0.2807 -0.0763 26 CYS B N 7375 C CA . CYS B 26 ? 2.1270 1.5660 2.0188 -0.3607 -0.3289 -0.1025 26 CYS B CA 7376 C C . CYS B 26 ? 2.1774 1.6078 2.0082 -0.3423 -0.3417 -0.1539 26 CYS B C 7377 O O . CYS B 26 ? 2.2291 1.6920 2.0218 -0.3378 -0.3359 -0.1509 26 CYS B O 7378 C CB . CYS B 26 ? 2.1373 1.6061 2.0779 -0.3859 -0.3560 -0.0639 26 CYS B CB 7379 S SG . CYS B 26 ? 2.6228 2.0660 2.6569 -0.4205 -0.4069 -0.0412 26 CYS B SG 7380 N N . SER B 27 ? 2.1877 1.5783 2.0092 -0.3281 -0.3607 -0.2013 27 SER B N 7381 C CA . SER B 27 ? 2.3029 1.6869 2.0715 -0.3038 -0.3847 -0.2592 27 SER B CA 7382 C C . SER B 27 ? 2.4189 1.7629 2.2229 -0.3193 -0.4516 -0.2787 27 SER B C 7383 O O . SER B 27 ? 2.4610 1.8054 2.3248 -0.3533 -0.4703 -0.2342 27 SER B O 7384 C CB . SER B 27 ? 2.4145 1.7829 2.1535 -0.2714 -0.3741 -0.3045 27 SER B CB 7385 O OG . SER B 27 ? 2.4805 1.8888 2.1927 -0.2621 -0.3171 -0.2807 27 SER B OG 7386 N N . ASP B 28 ? 2.4797 1.7959 2.2468 -0.2926 -0.4902 -0.3435 28 ASP B N 7387 C CA . ASP B 28 ? 2.4711 1.7341 2.2708 -0.3048 -0.5669 -0.3704 28 ASP B CA 7388 C C . ASP B 28 ? 2.4638 1.7587 2.2684 -0.3291 -0.5841 -0.3425 28 ASP B C 7389 O O . ASP B 28 ? 2.4281 1.7265 2.3012 -0.3697 -0.5989 -0.2879 28 ASP B O 7390 C CB . ASP B 28 ? 2.4645 1.6682 2.3538 -0.3363 -0.6042 -0.3449 28 ASP B CB 7391 C CG . ASP B 28 ? 2.6101 1.7492 2.5438 -0.3546 -0.6949 -0.3673 28 ASP B CG 7392 O OD1 . ASP B 28 ? 2.7429 1.8574 2.6248 -0.3237 -0.7358 -0.4340 28 ASP B OD1 7393 O OD2 . ASP B 28 ? 2.6053 1.7220 2.6270 -0.3995 -0.7287 -0.3159 28 ASP B OD2 7394 N N . GLU B 29 ? 2.5349 1.8637 2.2654 -0.3018 -0.5802 -0.3776 29 GLU B N 7395 C CA . GLU B 29 ? 2.4922 1.8635 2.2103 -0.3172 -0.5856 -0.3533 29 GLU B CA 7396 C C . GLU B 29 ? 2.3971 1.7333 2.1792 -0.3526 -0.6556 -0.3416 29 GLU B C 7397 O O . GLU B 29 ? 2.3326 1.7071 2.1184 -0.3704 -0.6613 -0.3127 29 GLU B O 7398 C CB . GLU B 29 ? 2.5303 1.9387 2.1556 -0.2773 -0.5821 -0.4032 29 GLU B CB 7399 C CG . GLU B 29 ? 2.4742 1.9183 2.0366 -0.2371 -0.5307 -0.4272 29 GLU B CG 7400 C CD . GLU B 29 ? 2.4715 1.8729 2.0131 -0.1977 -0.5642 -0.5006 29 GLU B CD 7401 O OE1 . GLU B 29 ? 2.4789 1.8073 2.0807 -0.2112 -0.6014 -0.5093 29 GLU B OE1 7402 O OE2 . GLU B 29 ? 2.4966 1.9427 1.9619 -0.1507 -0.5553 -0.5481 29 GLU B OE2 7403 N N . ALA B 30 ? 2.3776 1.6415 2.2127 -0.3636 -0.7134 -0.3621 30 ALA B N 7404 C CA . ALA B 30 ? 2.4012 1.6289 2.3127 -0.4055 -0.7882 -0.3404 30 ALA B CA 7405 C C . ALA B 30 ? 2.4289 1.7205 2.4059 -0.4503 -0.7611 -0.2500 30 ALA B C 7406 O O . ALA B 30 ? 2.2624 1.5860 2.2691 -0.4596 -0.7088 -0.2008 30 ALA B O 7407 C CB . ALA B 30 ? 2.3997 1.5402 2.3733 -0.4172 -0.8485 -0.3572 30 ALA B CB 7408 N N . LEU B 31 ? 2.6220 1.9368 2.6190 -0.4733 -0.7988 -0.2311 31 LEU B N 7409 C CA . LEU B 31 ? 2.4929 1.8843 2.5465 -0.5081 -0.7765 -0.1493 31 LEU B CA 7410 C C . LEU B 31 ? 2.2946 1.7571 2.3025 -0.4856 -0.6870 -0.1208 31 LEU B C 7411 O O . LEU B 31 ? 2.1588 1.6514 2.2044 -0.4933 -0.6460 -0.0733 31 LEU B O 7412 C CB . LEU B 31 ? 2.3733 1.7624 2.5384 -0.5538 -0.8048 -0.0856 31 LEU B CB 7413 C CG . LEU B 31 ? 2.2402 1.5593 2.4732 -0.5889 -0.9069 -0.0945 31 LEU B CG 7414 C CD1 . LEU B 31 ? 2.1716 1.5079 2.5157 -0.6301 -0.9205 -0.0160 31 LEU B CD1 7415 C CD2 . LEU B 31 ? 2.2496 1.5902 2.4878 -0.6060 -0.9553 -0.0917 31 LEU B CD2 7416 N N . PRO B 32 ? 2.3611 1.8496 2.2877 -0.4569 -0.6616 -0.1492 32 PRO B N 7417 C CA . PRO B 32 ? 2.3897 1.9328 2.2712 -0.4356 -0.5883 -0.1248 32 PRO B CA 7418 C C . PRO B 32 ? 2.4615 2.0743 2.3871 -0.4528 -0.5706 -0.0573 32 PRO B C 7419 O O . PRO B 32 ? 2.4556 2.0884 2.4484 -0.4835 -0.6115 -0.0244 32 PRO B O 7420 C CB . PRO B 32 ? 2.4220 1.9719 2.2117 -0.4054 -0.5832 -0.1718 32 PRO B CB 7421 C CG . PRO B 32 ? 2.5179 2.0144 2.2948 -0.4008 -0.6481 -0.2329 32 PRO B CG 7422 C CD . PRO B 32 ? 2.4915 1.9582 2.3626 -0.4413 -0.7054 -0.2063 32 PRO B CD 7423 N N . LEU B 33 ? 2.5030 2.1540 2.3916 -0.4309 -0.5140 -0.0372 33 LEU B N 7424 C CA . LEU B 33 ? 2.4547 2.1737 2.3722 -0.4321 -0.4924 0.0188 33 LEU B CA 7425 C C . LEU B 33 ? 2.5024 2.2568 2.5107 -0.4564 -0.5013 0.0705 33 LEU B C 7426 O O . LEU B 33 ? 2.5550 2.2807 2.5942 -0.4649 -0.4990 0.0717 33 LEU B O 7427 C CB . LEU B 33 ? 2.3985 2.1522 2.3025 -0.4356 -0.5182 0.0233 33 LEU B CB 7428 C CG . LEU B 33 ? 2.3500 2.1029 2.1683 -0.4101 -0.5013 -0.0035 33 LEU B CG 7429 C CD1 . LEU B 33 ? 2.3758 2.0809 2.1392 -0.4035 -0.5233 -0.0639 33 LEU B CD1 7430 C CD2 . LEU B 33 ? 2.3417 2.1471 2.1638 -0.4124 -0.5171 0.0228 33 LEU B CD2 7431 N N . GLY B 34 ? 2.5199 2.3458 2.5721 -0.4667 -0.5118 0.1172 34 GLY B N 7432 C CA . GLY B 34 ? 2.5350 2.4216 2.6801 -0.4925 -0.5250 0.1774 34 GLY B CA 7433 C C . GLY B 34 ? 2.5330 2.4536 2.6972 -0.4762 -0.4795 0.2086 34 GLY B C 7434 O O . GLY B 34 ? 2.4653 2.4539 2.7059 -0.4944 -0.4852 0.2652 34 GLY B O 7435 N N . SER B 35 ? 2.5836 2.4655 2.6796 -0.4419 -0.4365 0.1758 35 SER B N 7436 C CA . SER B 35 ? 2.5194 2.4132 2.6212 -0.4235 -0.3970 0.1918 35 SER B CA 7437 C C . SER B 35 ? 2.4837 2.3165 2.5043 -0.3917 -0.3622 0.1472 35 SER B C 7438 O O . SER B 35 ? 2.5310 2.3070 2.5010 -0.3920 -0.3712 0.1037 35 SER B O 7439 C CB . SER B 35 ? 2.4600 2.3311 2.6226 -0.4548 -0.4163 0.2052 35 SER B CB 7440 O OG . SER B 35 ? 2.4216 2.1963 2.5559 -0.4658 -0.4395 0.1509 35 SER B OG 7441 N N . PRO B 36 ? 2.3911 2.2421 2.4000 -0.3633 -0.3249 0.1602 36 PRO B N 7442 C CA . PRO B 36 ? 2.3655 2.1566 2.3095 -0.3396 -0.2974 0.1254 36 PRO B CA 7443 C C . PRO B 36 ? 2.2895 2.0164 2.2332 -0.3559 -0.2985 0.0966 36 PRO B C 7444 O O . PRO B 36 ? 2.2966 2.0289 2.2952 -0.3754 -0.3091 0.1133 36 PRO B O 7445 C CB . PRO B 36 ? 2.3759 2.2064 2.3199 -0.3056 -0.2683 0.1496 36 PRO B CB 7446 C CG . PRO B 36 ? 2.3833 2.3079 2.3748 -0.3008 -0.2768 0.1927 36 PRO B CG 7447 C CD . PRO B 36 ? 2.3785 2.3164 2.4292 -0.3464 -0.3090 0.2085 36 PRO B CD 7448 N N . ARG B 37 ? 2.2220 1.8958 2.1073 -0.3472 -0.2895 0.0577 37 ARG B N 7449 C CA . ARG B 37 ? 2.2023 1.8224 2.0811 -0.3539 -0.2885 0.0260 37 ARG B CA 7450 C C . ARG B 37 ? 2.2116 1.8186 2.0852 -0.3382 -0.2555 0.0324 37 ARG B C 7451 O O . ARG B 37 ? 2.2502 1.8208 2.1299 -0.3425 -0.2521 0.0139 37 ARG B O 7452 C CB . ARG B 37 ? 2.1707 1.7603 1.9897 -0.3481 -0.2932 -0.0163 37 ARG B CB 7453 C CG . ARG B 37 ? 2.2190 1.8140 2.0354 -0.3606 -0.3307 -0.0327 37 ARG B CG 7454 C CD . ARG B 37 ? 2.3279 1.9102 2.0764 -0.3469 -0.3304 -0.0729 37 ARG B CD 7455 N NE . ARG B 37 ? 2.4559 2.0418 2.1953 -0.3542 -0.3699 -0.0953 37 ARG B NE 7456 C CZ . ARG B 37 ? 2.4627 2.0148 2.2043 -0.3564 -0.4055 -0.1377 37 ARG B CZ 7457 N NH1 . ARG B 37 ? 2.4365 1.9498 2.1910 -0.3516 -0.4046 -0.1608 37 ARG B NH1 7458 N NH2 . ARG B 37 ? 2.4635 2.0174 2.1936 -0.3605 -0.4465 -0.1596 37 ARG B NH2 7459 N N . CYS B 38 ? 2.1105 1.7454 1.9721 -0.3169 -0.2355 0.0560 38 CYS B N 7460 C CA . CYS B 38 ? 1.9905 1.6082 1.8377 -0.2977 -0.2094 0.0583 38 CYS B CA 7461 C C . CYS B 38 ? 1.9455 1.5973 1.8408 -0.2936 -0.2017 0.0870 38 CYS B C 7462 O O . CYS B 38 ? 1.9419 1.5857 1.8266 -0.2740 -0.1827 0.0899 38 CYS B O 7463 C CB . CYS B 38 ? 2.0270 1.6439 1.8291 -0.2717 -0.2009 0.0627 38 CYS B CB 7464 S SG . CYS B 38 ? 2.7091 2.2826 2.4826 -0.2525 -0.1808 0.0569 38 CYS B SG 7465 N N . ASP B 39 ? 1.9943 1.6887 1.9446 -0.3133 -0.2191 0.1116 39 ASP B N 7466 C CA . ASP B 39 ? 1.9550 1.7071 1.9548 -0.3095 -0.2116 0.1512 39 ASP B CA 7467 C C . ASP B 39 ? 1.9322 1.6462 1.9491 -0.3191 -0.2037 0.1456 39 ASP B C 7468 O O . ASP B 39 ? 1.9531 1.5985 1.9457 -0.3272 -0.2051 0.1092 39 ASP B O 7469 C CB . ASP B 39 ? 1.8786 1.6950 1.9428 -0.3357 -0.2369 0.1900 39 ASP B CB 7470 C CG . ASP B 39 ? 1.8780 1.7972 1.9814 -0.3184 -0.2242 0.2419 39 ASP B CG 7471 O OD1 . ASP B 39 ? 2.0017 1.9364 2.0739 -0.2796 -0.1974 0.2396 39 ASP B OD1 7472 O OD2 . ASP B 39 ? 1.8745 1.8651 2.0401 -0.3417 -0.2435 0.2862 39 ASP B OD2 7473 N N . LEU B 40 ? 1.8474 1.6146 1.9061 -0.3156 -0.1953 0.1832 40 LEU B N 7474 C CA . LEU B 40 ? 1.8666 1.6010 1.9340 -0.3171 -0.1837 0.1794 40 LEU B CA 7475 C C . LEU B 40 ? 1.8705 1.6221 2.0121 -0.3521 -0.2043 0.2136 40 LEU B C 7476 O O . LEU B 40 ? 1.9316 1.7295 2.1257 -0.3779 -0.2295 0.2482 40 LEU B O 7477 C CB . LEU B 40 ? 1.9263 1.6984 1.9684 -0.2763 -0.1557 0.1903 40 LEU B CB 7478 C CG . LEU B 40 ? 1.8936 1.7734 1.9526 -0.2499 -0.1495 0.2311 40 LEU B CG 7479 C CD1 . LEU B 40 ? 1.8090 1.7723 1.9423 -0.2714 -0.1547 0.2882 40 LEU B CD1 7480 C CD2 . LEU B 40 ? 2.0004 1.8900 2.0071 -0.1960 -0.1294 0.2169 40 LEU B CD2 7481 N N . LYS B 41 ? 1.8006 1.5142 1.9492 -0.3542 -0.1968 0.2071 41 LYS B N 7482 C CA . LYS B 41 ? 1.7650 1.4957 1.9847 -0.3831 -0.2148 0.2467 41 LYS B CA 7483 C C . LYS B 41 ? 1.7643 1.4832 2.0456 -0.4273 -0.2627 0.2636 41 LYS B C 7484 O O . LYS B 41 ? 1.7798 1.4207 2.0445 -0.4382 -0.2874 0.2176 41 LYS B O 7485 C CB . LYS B 41 ? 1.8441 1.6835 2.0919 -0.3678 -0.1952 0.3053 41 LYS B CB 7486 C CG . LYS B 41 ? 1.8909 1.7324 2.0832 -0.3230 -0.1580 0.2869 41 LYS B CG 7487 C CD . LYS B 41 ? 1.9105 1.8683 2.1266 -0.3006 -0.1412 0.3411 41 LYS B CD 7488 C CE . LYS B 41 ? 1.9088 1.8576 2.0659 -0.2526 -0.1126 0.3153 41 LYS B CE 7489 N NZ . LYS B 41 ? 1.9231 1.9931 2.0957 -0.2219 -0.0968 0.3628 41 LYS B NZ 7490 N N . GLU B 42 ? 1.8118 1.6146 2.1654 -0.4512 -0.2788 0.3318 42 GLU B N 7491 C CA . GLU B 42 ? 1.8843 1.6793 2.3121 -0.5001 -0.3341 0.3611 42 GLU B CA 7492 C C . GLU B 42 ? 1.8384 1.6794 2.2696 -0.5071 -0.3489 0.3711 42 GLU B C 7493 O O . GLU B 42 ? 1.8119 1.6553 2.3074 -0.5489 -0.3991 0.4000 42 GLU B O 7494 C CB . GLU B 42 ? 1.9730 1.8418 2.4914 -0.5317 -0.3510 0.4435 42 GLU B CB 7495 C CG . GLU B 42 ? 2.0361 2.0609 2.5826 -0.5219 -0.3264 0.5156 42 GLU B CG 7496 C CD . GLU B 42 ? 2.0438 2.1207 2.5217 -0.4631 -0.2661 0.5009 42 GLU B CD 7497 O OE1 . GLU B 42 ? 1.9881 2.0063 2.4322 -0.4457 -0.2470 0.4699 42 GLU B OE1 7498 O OE2 . GLU B 42 ? 2.0677 2.2417 2.5254 -0.4318 -0.2420 0.5184 42 GLU B OE2 7499 N N . ASN B 43 ? 1.8697 1.7444 2.2351 -0.4672 -0.3105 0.3489 43 ASN B N 7500 C CA . ASN B 43 ? 1.8981 1.8172 2.2612 -0.4688 -0.3220 0.3558 43 ASN B CA 7501 C C . ASN B 43 ? 1.8874 1.7097 2.2280 -0.4868 -0.3588 0.3014 43 ASN B C 7502 O O . ASN B 43 ? 1.9106 1.7554 2.2799 -0.5091 -0.3921 0.3160 43 ASN B O 7503 C CB . ASN B 43 ? 1.9633 1.9313 2.2591 -0.4170 -0.2770 0.3418 43 ASN B CB 7504 C CG . ASN B 43 ? 1.9987 2.0811 2.3137 -0.3896 -0.2463 0.3936 43 ASN B CG 7505 O OD1 . ASN B 43 ? 2.0188 2.1784 2.4083 -0.4150 -0.2583 0.4571 43 ASN B OD1 7506 N ND2 . ASN B 43 ? 1.9801 2.0773 2.2284 -0.3360 -0.2108 0.3682 43 ASN B ND2 7507 N N . LEU B 44 ? 1.8917 1.6149 2.1802 -0.4742 -0.3535 0.2391 44 LEU B N 7508 C CA . LEU B 44 ? 1.9926 1.6298 2.2565 -0.4843 -0.3899 0.1831 44 LEU B CA 7509 C C . LEU B 44 ? 2.1171 1.7011 2.4495 -0.5221 -0.4473 0.1900 44 LEU B C 7510 O O . LEU B 44 ? 2.1852 1.7036 2.5151 -0.5340 -0.4951 0.1503 44 LEU B O 7511 C CB . LEU B 44 ? 1.9960 1.5676 2.1753 -0.4502 -0.3598 0.1167 44 LEU B CB 7512 C CG . LEU B 44 ? 1.9820 1.5881 2.1006 -0.4138 -0.3054 0.1144 44 LEU B CG 7513 C CD1 . LEU B 44 ? 2.0616 1.6680 2.1830 -0.3999 -0.2742 0.1261 44 LEU B CD1 7514 C CD2 . LEU B 44 ? 1.9296 1.4921 1.9710 -0.3929 -0.2946 0.0600 44 LEU B CD2 7515 N N . LEU B 45 ? 2.0469 1.6575 2.4388 -0.5383 -0.4465 0.2395 45 LEU B N 7516 C CA . LEU B 45 ? 1.9935 1.5592 2.4655 -0.5796 -0.5079 0.2622 45 LEU B CA 7517 C C . LEU B 45 ? 2.0753 1.7068 2.6323 -0.6246 -0.5541 0.3315 45 LEU B C 7518 O O . LEU B 45 ? 2.2156 1.7982 2.8367 -0.6618 -0.6226 0.3437 45 LEU B O 7519 C CB . LEU B 45 ? 1.9303 1.5042 2.4356 -0.5817 -0.4901 0.2953 45 LEU B CB 7520 C CG . LEU B 45 ? 2.0709 1.5832 2.6484 -0.6136 -0.5507 0.3103 45 LEU B CG 7521 C CD1 . LEU B 45 ? 2.1858 1.5798 2.7119 -0.5866 -0.5786 0.2186 45 LEU B CD1 7522 C CD2 . LEU B 45 ? 2.0507 1.5954 2.6543 -0.6091 -0.5223 0.3508 45 LEU B CD2 7523 N N . LYS B 46 ? 2.0736 1.8195 2.6297 -0.6158 -0.5177 0.3765 46 LYS B N 7524 C CA . LYS B 46 ? 2.2056 2.0338 2.8362 -0.6535 -0.5548 0.4429 46 LYS B CA 7525 C C . LYS B 46 ? 2.3032 2.0499 2.9279 -0.6724 -0.6148 0.3966 46 LYS B C 7526 O O . LYS B 46 ? 2.4198 2.1331 3.1191 -0.7171 -0.6863 0.4219 46 LYS B O 7527 C CB . LYS B 46 ? 2.2205 2.1813 2.8294 -0.6240 -0.5000 0.4794 46 LYS B CB 7528 C CG . LYS B 46 ? 2.1940 2.2561 2.8179 -0.6036 -0.4504 0.5332 46 LYS B CG 7529 C CD . LYS B 46 ? 2.1520 2.3460 2.7516 -0.5648 -0.4040 0.5619 46 LYS B CD 7530 C CE . LYS B 46 ? 2.0827 2.3846 2.6928 -0.5370 -0.3592 0.6112 46 LYS B CE 7531 N NZ . LYS B 46 ? 2.0420 2.4741 2.6233 -0.4876 -0.3180 0.6316 46 LYS B NZ 7532 N N . ASP B 47 ? 2.2256 1.9418 2.7590 -0.6349 -0.5879 0.3295 47 ASP B N 7533 C CA . ASP B 47 ? 2.2563 1.8811 2.7594 -0.6392 -0.6386 0.2653 47 ASP B CA 7534 C C . ASP B 47 ? 2.3200 1.8242 2.8142 -0.6372 -0.6720 0.2099 47 ASP B C 7535 O O . ASP B 47 ? 2.2819 1.7743 2.7620 -0.6196 -0.6345 0.2060 47 ASP B O 7536 C CB . ASP B 47 ? 2.1760 1.8021 2.5775 -0.5955 -0.5952 0.2090 47 ASP B CB 7537 C CG . ASP B 47 ? 2.1250 1.8647 2.5141 -0.5754 -0.5375 0.2544 47 ASP B CG 7538 O OD1 . ASP B 47 ? 2.0829 1.9174 2.5463 -0.5979 -0.5407 0.3307 47 ASP B OD1 7539 O OD2 . ASP B 47 ? 2.1592 1.8972 2.4657 -0.5353 -0.4921 0.2156 47 ASP B OD2 7540 N N . ASN B 48 ? 2.3756 1.7952 2.8740 -0.6463 -0.7407 0.1650 48 ASN B N 7541 C CA . ASN B 48 ? 2.3829 1.7091 2.8646 -0.6188 -0.7624 0.1116 48 ASN B CA 7542 C C . ASN B 48 ? 2.4189 1.7007 2.8194 -0.5813 -0.7148 0.0467 48 ASN B C 7543 O O . ASN B 48 ? 2.4180 1.7023 2.8300 -0.5749 -0.6823 0.0638 48 ASN B O 7544 C CB . ASN B 48 ? 2.3344 1.5900 2.8031 -0.6074 -0.8286 0.0585 48 ASN B CB 7545 C CG . ASN B 48 ? 2.2717 1.5590 2.8244 -0.6450 -0.8840 0.1248 48 ASN B CG 7546 O OD1 . ASN B 48 ? 2.1779 1.5588 2.7916 -0.6799 -0.8683 0.2099 48 ASN B OD1 7547 N ND2 . ASN B 48 ? 2.3775 1.5915 2.9339 -0.6359 -0.9511 0.0879 48 ASN B ND2 7548 N N . CYS B 49 ? 2.4079 1.6589 2.7246 -0.5530 -0.7090 -0.0237 49 CYS B N 7549 C CA . CYS B 49 ? 2.3329 1.5977 2.5580 -0.5051 -0.6351 -0.0655 49 CYS B CA 7550 C C . CYS B 49 ? 2.4066 1.6379 2.6296 -0.4881 -0.6090 -0.0776 49 CYS B C 7551 O O . CYS B 49 ? 2.3951 1.6683 2.5814 -0.4676 -0.5410 -0.0667 49 CYS B O 7552 C CB . CYS B 49 ? 2.1945 1.5558 2.3982 -0.5009 -0.5692 -0.0185 49 CYS B CB 7553 S SG . CYS B 49 ? 2.4940 1.8717 2.5826 -0.4502 -0.5006 -0.0683 49 CYS B SG 7554 N N . ALA B 50 ? 2.4976 1.6542 2.7601 -0.4934 -0.6639 -0.0993 50 ALA B N 7555 C CA . ALA B 50 ? 2.4926 1.6262 2.7565 -0.4737 -0.6369 -0.1067 50 ALA B CA 7556 C C . ALA B 50 ? 2.6660 1.7292 2.8949 -0.4302 -0.6640 -0.1838 50 ALA B C 7557 O O . ALA B 50 ? 2.7010 1.7349 2.9757 -0.4263 -0.6898 -0.1750 50 ALA B O 7558 C CB . ALA B 50 ? 2.4894 1.6573 2.8423 -0.5040 -0.6414 -0.0271 50 ALA B CB 7559 N N . PRO B 51 ? 2.7700 1.8119 2.9160 -0.3946 -0.6606 -0.2583 51 PRO B N 7560 C CA . PRO B 51 ? 2.8217 1.8170 2.9242 -0.3438 -0.6701 -0.3322 51 PRO B CA 7561 C C . PRO B 51 ? 2.7117 1.7183 2.7838 -0.3283 -0.6120 -0.3366 51 PRO B C 7562 O O . PRO B 51 ? 2.5579 1.6172 2.6516 -0.3524 -0.5602 -0.2725 51 PRO B O 7563 C CB . PRO B 51 ? 2.8667 1.8568 2.8898 -0.3111 -0.6899 -0.4038 51 PRO B CB 7564 C CG . PRO B 51 ? 2.8318 1.8598 2.8644 -0.3502 -0.6939 -0.3621 51 PRO B CG 7565 C CD . PRO B 51 ? 2.7487 1.8298 2.8343 -0.3891 -0.6446 -0.2750 51 PRO B CD 7566 N N . GLU B 52 ? 2.7734 1.7579 2.7943 -0.2781 -0.6084 -0.4039 52 GLU B N 7567 C CA . GLU B 52 ? 2.6993 1.7360 2.6769 -0.2512 -0.5334 -0.4030 52 GLU B CA 7568 C C . GLU B 52 ? 2.6417 1.7635 2.5657 -0.2527 -0.4707 -0.3768 52 GLU B C 7569 O O . GLU B 52 ? 2.5855 1.7558 2.4901 -0.2491 -0.4087 -0.3489 52 GLU B O 7570 C CB . GLU B 52 ? 2.7404 1.7576 2.6679 -0.1914 -0.5436 -0.4826 52 GLU B CB 7571 C CG . GLU B 52 ? 2.6875 1.7700 2.5709 -0.1628 -0.4696 -0.4812 52 GLU B CG 7572 C CD . GLU B 52 ? 2.6793 1.7547 2.6160 -0.1890 -0.4397 -0.4274 52 GLU B CD 7573 O OE1 . GLU B 52 ? 2.7259 1.7354 2.7288 -0.2103 -0.4845 -0.4141 52 GLU B OE1 7574 O OE2 . GLU B 52 ? 2.6306 1.7663 2.5444 -0.1890 -0.3754 -0.3961 52 GLU B OE2 7575 N N . SER B 53 ? 2.6663 1.8001 2.5702 -0.2595 -0.4940 -0.3846 53 SER B N 7576 C CA . SER B 53 ? 2.6348 1.8406 2.4914 -0.2623 -0.4481 -0.3604 53 SER B CA 7577 C C . SER B 53 ? 2.6754 1.9222 2.5604 -0.2936 -0.3988 -0.2865 53 SER B C 7578 O O . SER B 53 ? 2.6912 1.9922 2.5332 -0.2871 -0.3517 -0.2684 53 SER B O 7579 C CB . SER B 53 ? 2.5943 1.7950 2.4449 -0.2733 -0.4939 -0.3725 53 SER B CB 7580 O OG . SER B 53 ? 2.6870 1.8499 2.5023 -0.2372 -0.5444 -0.4481 53 SER B OG 7581 N N . ILE B 54 ? 2.6410 1.8647 2.5982 -0.3251 -0.4138 -0.2433 54 ILE B N 7582 C CA . ILE B 54 ? 2.4184 1.6873 2.4006 -0.3465 -0.3717 -0.1775 54 ILE B CA 7583 C C . ILE B 54 ? 2.1542 1.4450 2.1005 -0.3250 -0.3150 -0.1756 54 ILE B C 7584 O O . ILE B 54 ? 2.1197 1.3828 2.0655 -0.3086 -0.3124 -0.2013 54 ILE B O 7585 C CB . ILE B 54 ? 1.8958 1.1504 1.9638 -0.3809 -0.3989 -0.1284 54 ILE B CB 7586 C CG1 . ILE B 54 ? 1.7224 1.0403 1.8083 -0.3932 -0.3554 -0.0642 54 ILE B CG1 7587 C CG2 . ILE B 54 ? 1.9195 1.1187 2.0173 -0.3753 -0.4172 -0.1470 54 ILE B CG2 7588 C CD1 . ILE B 54 ? 1.6768 1.0479 1.7581 -0.4037 -0.3529 -0.0355 54 ILE B CD1 7589 N N . GLU B 55 ? 2.0669 1.4054 1.9842 -0.3242 -0.2747 -0.1458 55 GLU B N 7590 C CA . GLU B 55 ? 2.0823 1.4384 1.9683 -0.3080 -0.2289 -0.1394 55 GLU B CA 7591 C C . GLU B 55 ? 1.9676 1.3395 1.8847 -0.3186 -0.2066 -0.0900 55 GLU B C 7592 O O . GLU B 55 ? 1.8150 1.2193 1.7296 -0.3234 -0.1978 -0.0589 55 GLU B O 7593 C CB . GLU B 55 ? 2.1085 1.5009 1.9329 -0.2949 -0.2066 -0.1456 55 GLU B CB 7594 C CG . GLU B 55 ? 2.1648 1.5627 1.9445 -0.2734 -0.2157 -0.1949 55 GLU B CG 7595 C CD . GLU B 55 ? 2.1359 1.5407 1.8975 -0.2517 -0.1920 -0.2138 55 GLU B CD 7596 O OE1 . GLU B 55 ? 2.0022 1.4015 1.7848 -0.2574 -0.1689 -0.1869 55 GLU B OE1 7597 O OE2 . GLU B 55 ? 2.2019 1.6246 1.9272 -0.2261 -0.1974 -0.2557 55 GLU B OE2 7598 N N . PHE B 56 ? 1.9508 1.3031 1.8948 -0.3173 -0.1993 -0.0853 56 PHE B N 7599 C CA . PHE B 56 ? 1.7898 1.1615 1.7546 -0.3198 -0.1770 -0.0439 56 PHE B CA 7600 C C . PHE B 56 ? 1.7002 1.0540 1.6590 -0.3073 -0.1556 -0.0526 56 PHE B C 7601 O O . PHE B 56 ? 1.6568 0.9912 1.6560 -0.3129 -0.1646 -0.0465 56 PHE B O 7602 C CB . PHE B 56 ? 1.7530 1.1360 1.7820 -0.3411 -0.1994 -0.0071 56 PHE B CB 7603 C CG . PHE B 56 ? 1.6188 1.0411 1.6642 -0.3371 -0.1763 0.0364 56 PHE B CG 7604 C CD1 . PHE B 56 ? 1.6012 1.0651 1.6168 -0.3224 -0.1563 0.0541 56 PHE B CD1 7605 C CD2 . PHE B 56 ? 1.6596 1.0782 1.7477 -0.3437 -0.1780 0.0578 56 PHE B CD2 7606 C CE1 . PHE B 56 ? 1.6771 1.1805 1.7006 -0.3087 -0.1388 0.0865 56 PHE B CE1 7607 C CE2 . PHE B 56 ? 1.7958 1.2602 1.8929 -0.3344 -0.1571 0.0958 56 PHE B CE2 7608 C CZ . PHE B 56 ? 1.8139 1.3219 1.8762 -0.3141 -0.1377 0.1073 56 PHE B CZ 7609 N N . PRO B 57 ? 1.6523 1.0142 1.5646 -0.2927 -0.1307 -0.0625 57 PRO B N 7610 C CA . PRO B 57 ? 1.5725 0.9245 1.4811 -0.2827 -0.1110 -0.0655 57 PRO B CA 7611 C C . PRO B 57 ? 1.5248 0.8787 1.4597 -0.2843 -0.1021 -0.0323 57 PRO B C 7612 O O . PRO B 57 ? 1.4745 0.8495 1.4011 -0.2817 -0.0971 -0.0075 57 PRO B O 7613 C CB . PRO B 57 ? 1.5587 0.9301 1.4189 -0.2745 -0.0927 -0.0669 57 PRO B CB 7614 C CG . PRO B 57 ? 1.6203 1.0075 1.4555 -0.2765 -0.1044 -0.0796 57 PRO B CG 7615 C CD . PRO B 57 ? 1.6466 1.0298 1.5124 -0.2879 -0.1240 -0.0669 57 PRO B CD 7616 N N . VAL B 58 ? 1.4593 0.7950 1.4234 -0.2839 -0.1018 -0.0337 58 VAL B N 7617 C CA . VAL B 58 ? 1.3915 0.7352 1.3793 -0.2831 -0.0941 -0.0026 58 VAL B CA 7618 C C . VAL B 58 ? 1.4078 0.7399 1.3802 -0.2715 -0.0760 -0.0075 58 VAL B C 7619 O O . VAL B 58 ? 1.5271 0.8417 1.5036 -0.2687 -0.0746 -0.0300 58 VAL B O 7620 C CB . VAL B 58 ? 1.4150 0.7521 1.4605 -0.2975 -0.1143 0.0128 58 VAL B CB 7621 C CG1 . VAL B 58 ? 1.3612 0.6561 1.4221 -0.2992 -0.1333 -0.0226 58 VAL B CG1 7622 C CG2 . VAL B 58 ? 1.5595 0.9118 1.6265 -0.2936 -0.1034 0.0438 58 VAL B CG2 7623 N N . SER B 59 ? 1.3219 0.6653 1.2764 -0.2617 -0.0658 0.0120 59 SER B N 7624 C CA . SER B 59 ? 1.4258 0.7557 1.3678 -0.2532 -0.0552 0.0113 59 SER B CA 7625 C C . SER B 59 ? 1.3564 0.6771 1.3347 -0.2540 -0.0540 0.0151 59 SER B C 7626 O O . SER B 59 ? 1.2764 0.6105 1.2828 -0.2554 -0.0591 0.0361 59 SER B O 7627 C CB . SER B 59 ? 1.6367 0.9711 1.5519 -0.2385 -0.0560 0.0272 59 SER B CB 7628 O OG . SER B 59 ? 1.7447 1.0792 1.6271 -0.2376 -0.0614 0.0241 59 SER B OG 7629 N N . GLU B 60 ? 1.4461 0.7523 1.4258 -0.2528 -0.0478 -0.0008 60 GLU B N 7630 C CA . GLU B 60 ? 1.3859 0.6799 1.4006 -0.2520 -0.0487 -0.0002 60 GLU B CA 7631 C C . GLU B 60 ? 1.4152 0.7058 1.4221 -0.2448 -0.0386 0.0051 60 GLU B C 7632 O O . GLU B 60 ? 1.2215 0.5168 1.2024 -0.2441 -0.0327 0.0014 60 GLU B O 7633 C CB . GLU B 60 ? 1.3698 0.6497 1.4028 -0.2520 -0.0569 -0.0296 60 GLU B CB 7634 C CG . GLU B 60 ? 1.6300 0.9016 1.6781 -0.2608 -0.0776 -0.0375 60 GLU B CG 7635 C CD . GLU B 60 ? 1.8690 1.1176 1.9286 -0.2522 -0.0944 -0.0765 60 GLU B CD 7636 O OE1 . GLU B 60 ? 1.7454 0.9979 1.7955 -0.2357 -0.0836 -0.0980 60 GLU B OE1 7637 O OE2 . GLU B 60 ? 2.0841 1.3131 2.1629 -0.2595 -0.1220 -0.0864 60 GLU B OE2 7638 N N . ALA B 61 ? 1.4403 0.7258 1.4735 -0.2421 -0.0401 0.0187 61 ALA B N 7639 C CA . ALA B 61 ? 1.2040 0.4835 1.2396 -0.2366 -0.0344 0.0209 61 ALA B CA 7640 C C . ALA B 61 ? 1.2408 0.5100 1.3181 -0.2364 -0.0378 0.0166 61 ALA B C 7641 O O . ALA B 61 ? 1.3545 0.6228 1.4590 -0.2392 -0.0459 0.0352 61 ALA B O 7642 C CB . ALA B 61 ? 1.1951 0.4767 1.2142 -0.2277 -0.0374 0.0412 61 ALA B CB 7643 N N . ARG B 62 ? 1.2192 0.4870 1.3032 -0.2314 -0.0333 -0.0051 62 ARG B N 7644 C CA . ARG B 62 ? 1.2340 0.4862 1.3567 -0.2254 -0.0419 -0.0168 62 ARG B CA 7645 C C . ARG B 62 ? 1.3089 0.5696 1.4410 -0.2165 -0.0328 -0.0165 62 ARG B C 7646 O O . ARG B 62 ? 1.3268 0.6132 1.4395 -0.2133 -0.0203 -0.0215 62 ARG B O 7647 C CB . ARG B 62 ? 1.2670 0.5121 1.3927 -0.2170 -0.0516 -0.0526 62 ARG B CB 7648 C CG . ARG B 62 ? 1.5329 0.7687 1.6522 -0.2278 -0.0650 -0.0539 62 ARG B CG 7649 C CD . ARG B 62 ? 1.6881 0.8977 1.8246 -0.2182 -0.0901 -0.0899 62 ARG B CD 7650 N NE . ARG B 62 ? 1.7050 0.9342 1.8196 -0.1921 -0.0812 -0.1294 62 ARG B NE 7651 C CZ . ARG B 62 ? 1.8177 1.0289 1.9376 -0.1695 -0.1038 -0.1731 62 ARG B CZ 7652 N NH1 . ARG B 62 ? 1.8166 0.9755 1.9682 -0.1761 -0.1427 -0.1813 62 ARG B NH1 7653 N NH2 . ARG B 62 ? 1.8972 1.1468 1.9922 -0.1386 -0.0914 -0.2075 62 ARG B NH2 7654 N N . VAL B 63 ? 1.2270 0.4720 1.3933 -0.2148 -0.0412 -0.0052 63 VAL B N 7655 C CA . VAL B 63 ? 1.2221 0.4753 1.4027 -0.2061 -0.0351 -0.0038 63 VAL B CA 7656 C C . VAL B 63 ? 1.2477 0.5091 1.4432 -0.1873 -0.0353 -0.0373 63 VAL B C 7657 O O . VAL B 63 ? 1.3913 0.6254 1.6111 -0.1780 -0.0536 -0.0573 63 VAL B O 7658 C CB . VAL B 63 ? 1.2165 0.4537 1.4283 -0.2086 -0.0454 0.0208 63 VAL B CB 7659 C CG1 . VAL B 63 ? 1.2156 0.4600 1.4470 -0.1982 -0.0418 0.0188 63 VAL B CG1 7660 C CG2 . VAL B 63 ? 1.2089 0.4549 1.3984 -0.2163 -0.0436 0.0508 63 VAL B CG2 7661 N N . LEU B 64 ? 1.2429 0.5455 1.4252 -0.1798 -0.0189 -0.0420 64 LEU B N 7662 C CA . LEU B 64 ? 1.2690 0.6028 1.4609 -0.1533 -0.0147 -0.0731 64 LEU B CA 7663 C C . LEU B 64 ? 1.2710 0.6039 1.4999 -0.1404 -0.0183 -0.0705 64 LEU B C 7664 O O . LEU B 64 ? 1.6000 0.9082 1.8548 -0.1189 -0.0348 -0.0963 64 LEU B O 7665 C CB . LEU B 64 ? 1.3044 0.7054 1.4693 -0.1519 0.0060 -0.0699 64 LEU B CB 7666 C CG . LEU B 64 ? 1.2841 0.6942 1.4122 -0.1583 0.0087 -0.0784 64 LEU B CG 7667 C CD1 . LEU B 64 ? 1.4458 0.9300 1.5533 -0.1626 0.0271 -0.0613 64 LEU B CD1 7668 C CD2 . LEU B 64 ? 1.3125 0.7066 1.4379 -0.1329 -0.0044 -0.1241 64 LEU B CD2 7669 N N . GLU B 65 ? 1.2438 0.5994 1.4765 -0.1529 -0.0082 -0.0399 65 GLU B N 7670 C CA . GLU B 65 ? 1.2428 0.6020 1.5107 -0.1429 -0.0114 -0.0329 65 GLU B CA 7671 C C . GLU B 65 ? 1.2197 0.5449 1.4944 -0.1636 -0.0199 0.0009 65 GLU B C 7672 O O . GLU B 65 ? 1.2788 0.6136 1.5339 -0.1811 -0.0165 0.0251 65 GLU B O 7673 C CB . GLU B 65 ? 1.3571 0.7898 1.6301 -0.1344 0.0055 -0.0266 65 GLU B CB 7674 C CG . GLU B 65 ? 1.4475 0.8908 1.7566 -0.1295 0.0027 -0.0111 65 GLU B CG 7675 C CD . GLU B 65 ? 1.4945 1.0245 1.8154 -0.1246 0.0184 0.0036 65 GLU B CD 7676 O OE1 . GLU B 65 ? 1.3516 0.9027 1.7056 -0.1178 0.0167 0.0153 65 GLU B OE1 7677 O OE2 . GLU B 65 ? 1.6149 1.1991 1.9149 -0.1291 0.0315 0.0083 65 GLU B OE2 7678 N N . ASP B 66 ? 1.3488 0.6353 1.6511 -0.1597 -0.0355 0.0032 66 ASP B N 7679 C CA . ASP B 66 ? 1.3412 0.6118 1.6509 -0.1721 -0.0427 0.0356 66 ASP B CA 7680 C C . ASP B 66 ? 1.2249 0.4885 1.5776 -0.1596 -0.0530 0.0387 66 ASP B C 7681 O O . ASP B 66 ? 1.2467 0.4799 1.6292 -0.1518 -0.0698 0.0311 66 ASP B O 7682 C CB . ASP B 66 ? 1.3357 0.5792 1.6353 -0.1852 -0.0522 0.0526 66 ASP B CB 7683 C CG . ASP B 66 ? 1.3502 0.5643 1.6790 -0.1828 -0.0690 0.0419 66 ASP B CG 7684 O OD1 . ASP B 66 ? 1.6509 0.8591 1.9896 -0.1672 -0.0728 0.0079 66 ASP B OD1 7685 O OD2 . ASP B 66 ? 1.2670 0.4766 1.6012 -0.1929 -0.0798 0.0676 66 ASP B OD2 7686 N N . ARG B 67 ? 1.2288 0.5178 1.5877 -0.1591 -0.0479 0.0522 67 ARG B N 7687 C CA . ARG B 67 ? 1.2358 0.5209 1.6337 -0.1488 -0.0581 0.0607 67 ARG B CA 7688 C C . ARG B 67 ? 1.2127 0.4791 1.6067 -0.1622 -0.0690 0.0941 67 ARG B C 7689 O O . ARG B 67 ? 1.2971 0.5675 1.6546 -0.1740 -0.0664 0.1077 67 ARG B O 7690 C CB . ARG B 67 ? 1.3413 0.6742 1.7526 -0.1403 -0.0483 0.0601 67 ARG B CB 7691 C CG . ARG B 67 ? 1.2799 0.6551 1.6969 -0.1183 -0.0354 0.0293 67 ARG B CG 7692 C CD . ARG B 67 ? 1.2172 0.6627 1.6467 -0.1167 -0.0228 0.0427 67 ARG B CD 7693 N NE . ARG B 67 ? 1.1964 0.6566 1.5992 -0.1475 -0.0196 0.0707 67 ARG B NE 7694 C CZ . ARG B 67 ? 1.4286 0.9420 1.8449 -0.1601 -0.0177 0.0970 67 ARG B CZ 7695 N NH1 . ARG B 67 ? 1.5868 1.1564 2.0425 -0.1429 -0.0125 0.1001 67 ARG B NH1 7696 N NH2 . ARG B 67 ? 1.3409 0.8517 1.7350 -0.1898 -0.0256 0.1224 67 ARG B NH2 7697 N N . PRO B 68 ? 1.2614 0.5103 1.6918 -0.1569 -0.0841 0.1073 68 PRO B N 7698 C CA . PRO B 68 ? 1.2552 0.5077 1.6767 -0.1647 -0.0923 0.1418 68 PRO B CA 7699 C C . PRO B 68 ? 1.2017 0.4712 1.6108 -0.1654 -0.0913 0.1520 68 PRO B C 7700 O O . PRO B 68 ? 1.2001 0.4860 1.6258 -0.1600 -0.0870 0.1403 68 PRO B O 7701 C CB . PRO B 68 ? 1.2879 0.5335 1.7495 -0.1568 -0.1086 0.1523 68 PRO B CB 7702 C CG . PRO B 68 ? 1.3042 0.5316 1.8055 -0.1404 -0.1124 0.1208 68 PRO B CG 7703 C CD . PRO B 68 ? 1.2891 0.5195 1.7655 -0.1394 -0.0976 0.0903 68 PRO B CD 7704 N N . LEU B 69 ? 1.1984 0.4726 1.5753 -0.1690 -0.0974 0.1725 69 LEU B N 7705 C CA . LEU B 69 ? 1.1984 0.4821 1.5569 -0.1674 -0.1062 0.1788 69 LEU B CA 7706 C C . LEU B 69 ? 1.2035 0.4944 1.6038 -0.1619 -0.1149 0.1905 69 LEU B C 7707 O O . LEU B 69 ? 1.5466 0.8339 1.9769 -0.1576 -0.1200 0.2057 69 LEU B O 7708 C CB . LEU B 69 ? 1.2067 0.4942 1.5180 -0.1614 -0.1166 0.1921 69 LEU B CB 7709 C CG . LEU B 69 ? 1.2215 0.5056 1.4888 -0.1616 -0.1108 0.1814 69 LEU B CG 7710 C CD1 . LEU B 69 ? 1.3359 0.6390 1.5604 -0.1445 -0.1206 0.1948 69 LEU B CD1 7711 C CD2 . LEU B 69 ? 1.2442 0.5135 1.4901 -0.1693 -0.1142 0.1615 69 LEU B CD2 7712 N N . SER B 70 ? 1.2022 0.5050 1.6093 -0.1641 -0.1199 0.1878 70 SER B N 7713 C CA . SER B 70 ? 1.2068 0.5221 1.6549 -0.1581 -0.1285 0.1991 70 SER B CA 7714 C C . SER B 70 ? 1.2188 0.5312 1.6512 -0.1535 -0.1473 0.2216 70 SER B C 7715 O O . SER B 70 ? 1.3141 0.6217 1.7012 -0.1507 -0.1526 0.2264 70 SER B O 7716 C CB . SER B 70 ? 1.2709 0.6126 1.7363 -0.1647 -0.1296 0.1962 70 SER B CB 7717 O OG . SER B 70 ? 1.3726 0.7364 1.8541 -0.1632 -0.1099 0.1785 70 SER B OG 7718 N N . ASP B 71 ? 1.2245 0.5476 1.6930 -0.1484 -0.1574 0.2347 71 ASP B N 7719 C CA . ASP B 71 ? 1.2544 0.5825 1.7098 -0.1416 -0.1765 0.2570 71 ASP B CA 7720 C C . ASP B 71 ? 1.2824 0.6190 1.7445 -0.1441 -0.1952 0.2588 71 ASP B C 7721 O O . ASP B 71 ? 1.4865 0.8161 1.9065 -0.1428 -0.2164 0.2581 71 ASP B O 7722 C CB . ASP B 71 ? 1.3977 0.7292 1.8940 -0.1353 -0.1783 0.2798 71 ASP B CB 7723 C CG . ASP B 71 ? 1.7142 1.0379 2.2691 -0.1325 -0.1711 0.2679 71 ASP B CG 7724 O OD1 . ASP B 71 ? 1.7975 1.1183 2.3532 -0.1338 -0.1563 0.2414 71 ASP B OD1 7725 O OD2 . ASP B 71 ? 1.8759 1.1987 2.4742 -0.1251 -0.1826 0.2838 71 ASP B OD2 7726 N N . LYS B 72 ? 1.2997 0.6528 1.8163 -0.1452 -0.1915 0.2602 72 LYS B N 7727 C CA . LYS B 72 ? 1.5922 0.9636 2.1286 -0.1514 -0.2096 0.2682 72 LYS B CA 7728 C C . LYS B 72 ? 1.6734 1.0719 2.2355 -0.1637 -0.1983 0.2601 72 LYS B C 7729 O O . LYS B 72 ? 1.7037 1.1127 2.2781 -0.1591 -0.1732 0.2452 72 LYS B O 7730 C CB . LYS B 72 ? 1.5937 0.9813 2.1772 -0.1403 -0.2170 0.2850 72 LYS B CB 7731 C CG . LYS B 72 ? 1.5821 0.9619 2.1399 -0.1337 -0.2413 0.3037 72 LYS B CG 7732 C CD . LYS B 72 ? 1.5616 0.9288 2.0790 -0.1255 -0.2355 0.3093 72 LYS B CD 7733 C CE . LYS B 72 ? 1.4997 0.8780 1.9833 -0.1134 -0.2584 0.3286 72 LYS B CE 7734 N NZ . LYS B 72 ? 1.3468 0.7362 1.7926 -0.1038 -0.2505 0.3418 72 LYS B NZ 7735 N N . GLY B 73 ? 1.5861 1.0006 2.1571 -0.1794 -0.2201 0.2728 73 GLY B N 7736 C CA . GLY B 73 ? 1.6867 1.1398 2.2819 -0.1973 -0.2139 0.2779 73 GLY B CA 7737 C C . GLY B 73 ? 1.7504 1.2723 2.4116 -0.1904 -0.1983 0.2883 73 GLY B C 7738 O O . GLY B 73 ? 1.8033 1.3793 2.4949 -0.2078 -0.2005 0.3071 73 GLY B O 7739 N N . SER B 74 ? 1.9022 1.4276 2.5886 -0.1640 -0.1855 0.2793 74 SER B N 7740 C CA . SER B 74 ? 1.8351 1.4267 2.5822 -0.1459 -0.1720 0.2821 74 SER B CA 7741 C C . SER B 74 ? 1.8372 1.4756 2.5928 -0.1320 -0.1408 0.2625 74 SER B C 7742 O O . SER B 74 ? 1.8192 1.4354 2.5357 -0.1419 -0.1305 0.2500 74 SER B O 7743 C CB . SER B 74 ? 1.7288 1.2983 2.4993 -0.1184 -0.1754 0.2756 74 SER B CB 7744 O OG . SER B 74 ? 1.7376 1.2572 2.4857 -0.1037 -0.1648 0.2524 74 SER B OG 7745 N N . GLY B 75 ? 1.8175 1.5257 2.6222 -0.1045 -0.1269 0.2581 75 GLY B N 7746 C CA . GLY B 75 ? 1.7706 1.5439 2.5826 -0.0828 -0.0985 0.2383 75 GLY B CA 7747 C C . GLY B 75 ? 1.7422 1.4836 2.5497 -0.0394 -0.0876 0.1928 75 GLY B C 7748 O O . GLY B 75 ? 1.7710 1.5609 2.5764 -0.0131 -0.0671 0.1672 75 GLY B O 7749 N N . ASP B 76 ? 1.6630 0.9637 2.4694 0.0538 -0.1232 0.0250 76 ASP B N 7750 C CA . ASP B 76 ? 1.7301 1.0128 2.5636 0.0527 -0.1236 0.0144 76 ASP B CA 7751 C C . ASP B 76 ? 1.8260 1.0910 2.5899 0.0390 -0.1192 0.0087 76 ASP B C 7752 O O . ASP B 76 ? 1.7159 0.9642 2.4929 0.0350 -0.1220 0.0029 76 ASP B O 7753 C CB . ASP B 76 ? 1.8056 1.0887 2.7027 0.0483 -0.1561 0.0527 76 ASP B CB 7754 C CG . ASP B 76 ? 1.7820 1.0792 2.7689 0.0632 -0.1571 0.0496 76 ASP B CG 7755 O OD1 . ASP B 76 ? 1.7062 0.9993 2.7602 0.0639 -0.1731 0.0622 76 ASP B OD1 7756 O OD2 . ASP B 76 ? 1.7412 1.0546 2.7350 0.0739 -0.1416 0.0351 76 ASP B OD2 7757 N N . SER B 77 ? 2.0218 1.2909 2.7152 0.0314 -0.1127 0.0108 77 SER B N 7758 C CA . SER B 77 ? 2.0177 1.2736 2.6465 0.0178 -0.1071 0.0060 77 SER B CA 7759 C C . SER B 77 ? 2.0562 1.3036 2.6682 0.0235 -0.0790 -0.0425 77 SER B C 7760 O O . SER B 77 ? 2.0092 1.2590 2.6603 0.0375 -0.0640 -0.0712 77 SER B O 7761 C CB . SER B 77 ? 1.8463 1.1104 2.4096 0.0079 -0.1079 0.0234 77 SER B CB 7762 O OG . SER B 77 ? 1.7952 1.0731 2.3456 0.0187 -0.0885 0.0000 77 SER B OG 7763 N N . SER B 78 ? 2.1120 1.3500 2.6659 0.0111 -0.0724 -0.0506 78 SER B N 7764 C CA . SER B 78 ? 2.1251 1.3550 2.6522 0.0124 -0.0488 -0.0944 78 SER B CA 7765 C C . SER B 78 ? 2.0487 1.2954 2.5670 0.0253 -0.0249 -0.1246 78 SER B C 7766 O O . SER B 78 ? 2.1434 1.3912 2.6978 0.0380 -0.0111 -0.1511 78 SER B O 7767 C CB . SER B 78 ? 2.1345 1.3576 2.5987 -0.0047 -0.0480 -0.0922 78 SER B CB 7768 O OG . SER B 78 ? 2.1723 1.3847 2.6436 -0.0176 -0.0700 -0.0587 78 SER B OG 7769 N N . GLN B 79 ? 1.8217 1.0822 2.2924 0.0216 -0.0191 -0.1201 79 GLN B N 7770 C CA . GLN B 79 ? 1.7943 1.0760 2.2687 0.0337 -0.0057 -0.1300 79 GLN B CA 7771 C C . GLN B 79 ? 1.7891 1.0789 2.2509 0.0282 -0.0237 -0.0907 79 GLN B C 7772 O O . GLN B 79 ? 1.9759 1.2705 2.4802 0.0329 -0.0408 -0.0641 79 GLN B O 7773 C CB . GLN B 79 ? 1.8187 1.1103 2.2412 0.0336 0.0210 -0.1669 79 GLN B CB 7774 C CG . GLN B 79 ? 1.8972 1.1744 2.3010 0.0287 0.0332 -0.1997 79 GLN B CG 7775 C CD . GLN B 79 ? 2.0989 1.3710 2.5522 0.0412 0.0435 -0.2235 79 GLN B CD 7776 O OE1 . GLN B 79 ? 2.2246 1.5100 2.7254 0.0551 0.0474 -0.2212 79 GLN B OE1 7777 N NE2 . GLN B 79 ? 2.1099 1.3621 2.5543 0.0356 0.0481 -0.2462 79 GLN B NE2 7778 N N . VAL B 80 ? 1.5403 0.8311 1.9419 0.0166 -0.0199 -0.0872 80 VAL B N 7779 C CA . VAL B 80 ? 1.3794 0.6682 1.7539 0.0039 -0.0384 -0.0476 80 VAL B CA 7780 C C . VAL B 80 ? 1.2961 0.5800 1.6140 -0.0099 -0.0289 -0.0558 80 VAL B C 7781 O O . VAL B 80 ? 1.4203 0.7119 1.7119 -0.0076 -0.0072 -0.0891 80 VAL B O 7782 C CB . VAL B 80 ? 1.4258 0.7297 1.7943 0.0085 -0.0411 -0.0327 80 VAL B CB 7783 C CG1 . VAL B 80 ? 1.6081 0.9255 1.9038 -0.0053 -0.0405 -0.0150 80 VAL B CG1 7784 C CG2 . VAL B 80 ? 1.3625 0.6672 1.7783 0.0113 -0.0664 0.0012 80 VAL B CG2 7785 N N . THR B 81 ? 1.1605 0.4346 1.4598 -0.0253 -0.0443 -0.0248 81 THR B N 7786 C CA . THR B 81 ? 1.0726 0.3562 1.3140 -0.0384 -0.0339 -0.0285 81 THR B CA 7787 C C . THR B 81 ? 1.0484 0.3476 1.2426 -0.0512 -0.0414 0.0094 81 THR B C 7788 O O . THR B 81 ? 1.2696 0.5561 1.4747 -0.0609 -0.0598 0.0425 81 THR B O 7789 C CB . THR B 81 ? 1.1210 0.3793 1.3808 -0.0469 -0.0385 -0.0369 81 THR B CB 7790 O OG1 . THR B 81 ? 1.2698 0.5240 1.5551 -0.0356 -0.0279 -0.0742 81 THR B OG1 7791 C CG2 . THR B 81 ? 1.1359 0.4078 1.3402 -0.0606 -0.0283 -0.0399 81 THR B CG2 7792 N N . GLN B 82 ? 1.0212 0.3472 1.1628 -0.0517 -0.0260 0.0042 82 GLN B N 7793 C CA . GLN B 82 ? 1.0125 0.3532 1.1039 -0.0639 -0.0269 0.0338 82 GLN B CA 7794 C C . GLN B 82 ? 1.0025 0.3529 1.0561 -0.0748 -0.0136 0.0295 82 GLN B C 7795 O O . GLN B 82 ? 0.9979 0.3597 1.0131 -0.0852 -0.0105 0.0523 82 GLN B O 7796 C CB . GLN B 82 ? 1.1804 0.5429 1.2413 -0.0580 -0.0204 0.0351 82 GLN B CB 7797 C CG . GLN B 82 ? 1.1808 0.5357 1.2761 -0.0512 -0.0383 0.0506 82 GLN B CG 7798 C CD . GLN B 82 ? 1.2734 0.6492 1.3418 -0.0457 -0.0329 0.0493 82 GLN B CD 7799 O OE1 . GLN B 82 ? 1.4224 0.7987 1.4742 -0.0521 -0.0469 0.0772 82 GLN B OE1 7800 N NE2 . GLN B 82 ? 1.2739 0.6659 1.3363 -0.0354 -0.0136 0.0174 82 GLN B NE2 7801 N N . VAL B 83 ? 1.0023 0.3478 1.0672 -0.0734 -0.0055 0.0004 83 VAL B N 7802 C CA . VAL B 83 ? 1.0597 0.4156 1.0940 -0.0845 0.0047 -0.0036 83 VAL B CA 7803 C C . VAL B 83 ? 1.0168 0.3510 1.0783 -0.0914 -0.0018 -0.0155 83 VAL B C 7804 O O . VAL B 83 ? 1.0979 0.4194 1.1804 -0.0851 0.0006 -0.0469 83 VAL B O 7805 C CB . VAL B 83 ? 0.9665 0.3467 0.9673 -0.0798 0.0237 -0.0292 83 VAL B CB 7806 C CG1 . VAL B 83 ? 0.9607 0.3497 0.9397 -0.0919 0.0307 -0.0333 83 VAL B CG1 7807 C CG2 . VAL B 83 ? 0.9451 0.3472 0.9139 -0.0757 0.0306 -0.0160 83 VAL B CG2 7808 N N . SER B 84 ? 1.0269 0.3563 1.0873 -0.1053 -0.0092 0.0094 84 SER B N 7809 C CA . SER B 84 ? 1.0819 0.3924 1.1642 -0.1152 -0.0168 0.0020 84 SER B CA 7810 C C . SER B 84 ? 1.1456 0.4745 1.1981 -0.1281 -0.0084 0.0058 84 SER B C 7811 O O . SER B 84 ? 1.2440 0.5898 1.2766 -0.1351 -0.0040 0.0342 84 SER B O 7812 C CB . SER B 84 ? 1.0722 0.3593 1.1909 -0.1219 -0.0361 0.0305 84 SER B CB 7813 O OG . SER B 84 ? 1.1830 0.4480 1.3432 -0.1106 -0.0468 0.0230 84 SER B OG 7814 N N . PRO B 85 ? 1.0367 0.3620 1.0865 -0.1323 -0.0059 -0.0222 85 PRO B N 7815 C CA . PRO B 85 ? 1.0871 0.3917 1.1528 -0.1265 -0.0068 -0.0605 85 PRO B CA 7816 C C . PRO B 85 ? 1.2267 0.5476 1.2689 -0.1141 0.0093 -0.0880 85 PRO B C 7817 O O . PRO B 85 ? 1.3401 0.6864 1.3585 -0.1084 0.0186 -0.0759 85 PRO B O 7818 C CB . PRO B 85 ? 1.0719 0.3692 1.1323 -0.1427 -0.0118 -0.0714 85 PRO B CB 7819 C CG . PRO B 85 ? 1.0446 0.3730 1.0757 -0.1517 -0.0053 -0.0490 85 PRO B CG 7820 C CD . PRO B 85 ? 1.0289 0.3692 1.0609 -0.1471 -0.0032 -0.0139 85 PRO B CD 7821 N N . GLN B 86 ? 1.0588 0.3640 1.1076 -0.1109 0.0133 -0.1251 86 GLN B N 7822 C CA . GLN B 86 ? 1.0472 0.3671 1.0756 -0.1005 0.0301 -0.1533 86 GLN B CA 7823 C C . GLN B 86 ? 1.1271 0.4570 1.1174 -0.1124 0.0376 -0.1760 86 GLN B C 7824 O O . GLN B 86 ? 1.3604 0.7196 1.3171 -0.1129 0.0474 -0.1732 86 GLN B O 7825 C CB . GLN B 86 ? 1.0712 0.3676 1.1358 -0.0866 0.0333 -0.1798 86 GLN B CB 7826 C CG . GLN B 86 ? 1.0660 0.3573 1.1694 -0.0736 0.0253 -0.1568 86 GLN B CG 7827 C CD . GLN B 86 ? 1.1313 0.3979 1.2701 -0.0803 0.0052 -0.1316 86 GLN B CD 7828 O OE1 . GLN B 86 ? 1.2705 0.5095 1.4388 -0.0818 -0.0014 -0.1471 86 GLN B OE1 7829 N NE2 . GLN B 86 ? 1.0702 0.3491 1.2017 -0.0850 -0.0041 -0.0918 86 GLN B NE2 7830 N N . ARG B 87 ? 1.0863 0.3905 1.0817 -0.1229 0.0318 -0.1984 87 ARG B N 7831 C CA . ARG B 87 ? 1.0974 0.4078 1.0542 -0.1380 0.0352 -0.2191 87 ARG B CA 7832 C C . ARG B 87 ? 1.1056 0.4125 1.0590 -0.1584 0.0186 -0.1998 87 ARG B C 7833 O O . ARG B 87 ? 1.2505 0.5316 1.2344 -0.1637 0.0045 -0.1917 87 ARG B O 7834 C CB . ARG B 87 ? 1.2864 0.5702 1.2412 -0.1380 0.0429 -0.2644 87 ARG B CB 7835 C CG . ARG B 87 ? 1.4395 0.7354 1.4048 -0.1152 0.0580 -0.2806 87 ARG B CG 7836 C CD . ARG B 87 ? 1.5437 0.8413 1.4903 -0.1129 0.0654 -0.3166 87 ARG B CD 7837 N NE . ARG B 87 ? 1.6523 0.9692 1.5477 -0.1288 0.0701 -0.3269 87 ARG B NE 7838 C CZ . ARG B 87 ? 1.5677 0.9153 1.4357 -0.1251 0.0847 -0.3282 87 ARG B CZ 7839 N NH1 . ARG B 87 ? 1.2819 0.6441 1.1692 -0.1060 0.0962 -0.3214 87 ARG B NH1 7840 N NH2 . ARG B 87 ? 1.6765 1.0403 1.4992 -0.1416 0.0859 -0.3344 87 ARG B NH2 7841 N N . ILE B 88 ? 1.0875 0.4209 1.0082 -0.1701 0.0195 -0.1909 88 ILE B N 7842 C CA . ILE B 88 ? 1.1897 0.5240 1.1100 -0.1905 0.0039 -0.1718 88 ILE B CA 7843 C C . ILE B 88 ? 1.1339 0.4756 1.0167 -0.2082 0.0016 -0.1902 88 ILE B C 7844 O O . ILE B 88 ? 1.0888 0.4568 0.9425 -0.2057 0.0129 -0.1947 88 ILE B O 7845 C CB . ILE B 88 ? 1.1816 0.5453 1.1097 -0.1898 0.0042 -0.1293 88 ILE B CB 7846 C CG1 . ILE B 88 ? 1.2080 0.5626 1.1681 -0.1775 0.0033 -0.1071 88 ILE B CG1 7847 C CG2 . ILE B 88 ? 1.0605 0.4292 0.9930 -0.2110 -0.0101 -0.1094 88 ILE B CG2 7848 C CD1 . ILE B 88 ? 1.1772 0.5572 1.1405 -0.1782 0.0067 -0.0674 88 ILE B CD1 7849 N N . ALA B 89 ? 1.1495 0.4668 1.0326 -0.2275 -0.0148 -0.1997 89 ALA B N 7850 C CA . ALA B 89 ? 1.1711 0.4935 1.0174 -0.2494 -0.0225 -0.2122 89 ALA B CA 7851 C C . ALA B 89 ? 1.1613 0.5100 1.0154 -0.2638 -0.0355 -0.1737 89 ALA B C 7852 O O . ALA B 89 ? 1.1456 0.4877 1.0337 -0.2688 -0.0478 -0.1484 89 ALA B O 7853 C CB . ALA B 89 ? 1.3729 0.6536 1.2116 -0.2655 -0.0346 -0.2437 89 ALA B CB 7854 N N . LEU B 90 ? 1.1563 0.5355 0.9829 -0.2704 -0.0324 -0.1682 90 LEU B N 7855 C CA . LEU B 90 ? 1.1429 0.5503 0.9831 -0.2826 -0.0426 -0.1313 90 LEU B CA 7856 C C . LEU B 90 ? 1.1665 0.5769 0.9792 -0.3096 -0.0602 -0.1370 90 LEU B C 7857 O O . LEU B 90 ? 1.2711 0.6921 1.0452 -0.3131 -0.0545 -0.1550 90 LEU B O 7858 C CB . LEU B 90 ? 1.1134 0.5587 0.9560 -0.2657 -0.0244 -0.1103 90 LEU B CB 7859 C CG . LEU B 90 ? 1.1027 0.5683 0.9832 -0.2615 -0.0226 -0.0692 90 LEU B CG 7860 C CD1 . LEU B 90 ? 1.0421 0.5427 0.9169 -0.2477 -0.0040 -0.0548 90 LEU B CD1 7861 C CD2 . LEU B 90 ? 1.1641 0.6337 1.0662 -0.2847 -0.0429 -0.0461 90 LEU B CD2 7862 N N . ARG B 91 ? 1.2019 0.6031 1.0350 -0.3302 -0.0829 -0.1198 91 ARG B N 7863 C CA . ARG B 91 ? 1.2843 0.6898 1.0963 -0.3591 -0.1047 -0.1177 91 ARG B CA 7864 C C . ARG B 91 ? 1.2558 0.6972 1.1035 -0.3660 -0.1130 -0.0723 91 ARG B C 7865 O O . ARG B 91 ? 1.2203 0.6655 1.1139 -0.3613 -0.1139 -0.0445 91 ARG B O 7866 C CB . ARG B 91 ? 1.5539 0.9183 1.3606 -0.3814 -0.1278 -0.1354 91 ARG B CB 7867 C CG . ARG B 91 ? 1.6312 0.9569 1.4056 -0.3756 -0.1180 -0.1835 91 ARG B CG 7868 C CD . ARG B 91 ? 1.6177 0.9107 1.3909 -0.3943 -0.1394 -0.2009 91 ARG B CD 7869 N NE . ARG B 91 ? 1.7236 1.0289 1.4671 -0.4209 -0.1602 -0.1989 91 ARG B NE 7870 C CZ . ARG B 91 ? 1.9354 1.2239 1.6734 -0.4375 -0.1796 -0.2113 91 ARG B CZ 7871 N NH1 . ARG B 91 ? 1.9324 1.1912 1.6959 -0.4299 -0.1799 -0.2279 91 ARG B NH1 7872 N NH2 . ARG B 91 ? 2.0859 1.3868 1.7939 -0.4623 -0.1994 -0.2061 91 ARG B NH2 7873 N N . LEU B 92 ? 1.2699 0.7382 1.0992 -0.3775 -0.1180 -0.0639 92 LEU B N 7874 C CA . LEU B 92 ? 1.2272 0.7325 1.0960 -0.3816 -0.1227 -0.0213 92 LEU B CA 7875 C C . LEU B 92 ? 1.2796 0.7954 1.1387 -0.4126 -0.1506 -0.0094 92 LEU B C 7876 O O . LEU B 92 ? 1.3010 0.8165 1.1120 -0.4236 -0.1553 -0.0296 92 LEU B O 7877 C CB . LEU B 92 ? 1.1709 0.7086 1.0426 -0.3572 -0.0956 -0.0124 92 LEU B CB 7878 C CG . LEU B 92 ? 1.1547 0.6909 1.0479 -0.3287 -0.0705 -0.0091 92 LEU B CG 7879 C CD1 . LEU B 92 ? 1.0982 0.6611 0.9818 -0.3075 -0.0458 -0.0078 92 LEU B CD1 7880 C CD2 . LEU B 92 ? 1.3370 0.8799 1.2843 -0.3302 -0.0735 0.0262 92 LEU B CD2 7881 N N . ARG B 93 ? 1.3254 0.8511 1.2319 -0.4277 -0.1697 0.0250 93 ARG B N 7882 C CA . ARG B 93 ? 1.3941 0.9373 1.3063 -0.4563 -0.1977 0.0472 93 ARG B CA 7883 C C . ARG B 93 ? 1.6206 1.2096 1.5668 -0.4441 -0.1838 0.0786 93 ARG B C 7884 O O . ARG B 93 ? 1.7434 1.3472 1.7208 -0.4176 -0.1564 0.0898 93 ARG B O 7885 C CB . ARG B 93 ? 1.3533 0.8871 1.3070 -0.4778 -0.2258 0.0704 93 ARG B CB 7886 C CG . ARG B 93 ? 1.4070 0.9649 1.4340 -0.4614 -0.2130 0.1080 93 ARG B CG 7887 C CD . ARG B 93 ? 1.4471 1.0092 1.5146 -0.4723 -0.2359 0.1283 93 ARG B CD 7888 N NE . ARG B 93 ? 1.3856 0.9682 1.4530 -0.4931 -0.2639 0.1435 93 ARG B NE 7889 C CZ . ARG B 93 ? 1.4599 1.0463 1.5540 -0.5072 -0.2898 0.1610 93 ARG B CZ 7890 N NH1 . ARG B 93 ? 1.4279 1.0001 1.5518 -0.5028 -0.2900 0.1646 93 ARG B NH1 7891 N NH2 . ARG B 93 ? 1.5692 1.1735 1.6601 -0.5262 -0.3166 0.1763 93 ARG B NH2 7892 N N . PRO B 94 ? 1.6760 1.2859 1.6150 -0.4641 -0.2027 0.0926 94 PRO B N 7893 C CA . PRO B 94 ? 1.6127 1.2643 1.5831 -0.4532 -0.1904 0.1198 94 PRO B CA 7894 C C . PRO B 94 ? 1.4697 1.1459 1.5181 -0.4390 -0.1768 0.1574 94 PRO B C 7895 O O . PRO B 94 ? 1.5158 1.1925 1.6067 -0.4485 -0.1920 0.1782 94 PRO B O 7896 C CB . PRO B 94 ? 1.6554 1.3194 1.6161 -0.4863 -0.2250 0.1353 94 PRO B CB 7897 C CG . PRO B 94 ? 1.6820 1.3178 1.6218 -0.5089 -0.2540 0.1241 94 PRO B CG 7898 C CD . PRO B 94 ? 1.6971 1.2909 1.5975 -0.5002 -0.2386 0.0844 94 PRO B CD 7899 N N . ASP B 95 ? 1.2856 0.9846 1.3497 -0.4120 -0.1452 0.1629 95 ASP B N 7900 C CA . ASP B 95 ? 1.3491 1.0718 1.4810 -0.3961 -0.1247 0.1946 95 ASP B CA 7901 C C . ASP B 95 ? 1.4052 1.1084 1.5582 -0.3898 -0.1170 0.1965 95 ASP B C 7902 O O . ASP B 95 ? 1.5401 1.2620 1.7501 -0.3867 -0.1151 0.2236 95 ASP B O 7903 C CB . ASP B 95 ? 1.4946 1.2532 1.6839 -0.4049 -0.1405 0.2300 95 ASP B CB 7904 C CG . ASP B 95 ? 1.5683 1.3508 1.7497 -0.4080 -0.1447 0.2356 95 ASP B CG 7905 O OD1 . ASP B 95 ? 1.6259 1.4258 1.8201 -0.4235 -0.1726 0.2510 95 ASP B OD1 7906 O OD2 . ASP B 95 ? 1.4644 1.2486 1.6264 -0.3943 -0.1209 0.2252 95 ASP B OD2 7907 N N . ASP B 96 ? 1.2996 0.9717 1.4057 -0.3798 -0.1089 0.1636 96 ASP B N 7908 C CA . ASP B 96 ? 1.2994 0.9509 1.4223 -0.3731 -0.1019 0.1645 96 ASP B CA 7909 C C . ASP B 96 ? 1.2813 0.9198 1.3720 -0.3458 -0.0726 0.1407 96 ASP B C 7910 O O . ASP B 96 ? 1.3584 0.9960 1.4056 -0.3353 -0.0632 0.1162 96 ASP B O 7911 C CB . ASP B 96 ? 1.3418 0.9600 1.4487 -0.3961 -0.1329 0.1513 96 ASP B CB 7912 C CG . ASP B 96 ? 1.4090 1.0093 1.5478 -0.3938 -0.1311 0.1614 96 ASP B CG 7913 O OD1 . ASP B 96 ? 1.3458 0.9655 1.5260 -0.3791 -0.1088 0.1862 96 ASP B OD1 7914 O OD2 . ASP B 96 ? 1.5763 1.1430 1.6982 -0.4071 -0.1513 0.1443 96 ASP B OD2 7915 N N . SER B 97 ? 1.1258 0.7547 1.2393 -0.3356 -0.0596 0.1501 97 SER B N 7916 C CA . SER B 97 ? 1.0612 0.6786 1.1495 -0.3116 -0.0344 0.1334 97 SER B CA 7917 C C . SER B 97 ? 1.0492 0.6369 1.1433 -0.3112 -0.0383 0.1306 97 SER B C 7918 O O . SER B 97 ? 1.3085 0.8963 1.4438 -0.3221 -0.0463 0.1555 97 SER B O 7919 C CB . SER B 97 ? 1.2663 0.9115 1.3767 -0.2939 -0.0039 0.1540 97 SER B CB 7920 O OG . SER B 97 ? 1.5312 1.1647 1.6127 -0.2731 0.0176 0.1389 97 SER B OG 7921 N N . LYS B 98 ? 1.0622 0.6250 1.1191 -0.2988 -0.0331 0.1017 98 LYS B N 7922 C CA . LYS B 98 ? 1.2408 0.7760 1.3055 -0.2948 -0.0342 0.1002 98 LYS B CA 7923 C C . LYS B 98 ? 1.3037 0.8371 1.3484 -0.2710 -0.0100 0.0924 98 LYS B C 7924 O O . LYS B 98 ? 1.1278 0.6695 1.1413 -0.2590 0.0015 0.0742 98 LYS B O 7925 C CB . LYS B 98 ? 1.1615 0.6605 1.2081 -0.3065 -0.0578 0.0720 98 LYS B CB 7926 C CG . LYS B 98 ? 1.1571 0.6271 1.2259 -0.3077 -0.0654 0.0767 98 LYS B CG 7927 C CD . LYS B 98 ? 1.4414 0.8763 1.5023 -0.3248 -0.0917 0.0531 98 LYS B CD 7928 C CE . LYS B 98 ? 1.7558 1.1607 1.8445 -0.3260 -0.1005 0.0592 98 LYS B CE 7929 N NZ . LYS B 98 ? 1.8509 1.2178 1.9335 -0.3430 -0.1257 0.0341 98 LYS B NZ 7930 N N . ASN B 99 ? 1.4029 0.9256 1.4656 -0.2660 -0.0039 0.1080 99 ASN B N 7931 C CA . ASN B 99 ? 1.3170 0.8390 1.3623 -0.2466 0.0169 0.1070 99 ASN B CA 7932 C C . ASN B 99 ? 1.1133 0.6014 1.1515 -0.2409 0.0083 0.0922 99 ASN B C 7933 O O . ASN B 99 ? 1.1166 0.5816 1.1743 -0.2523 -0.0105 0.0919 99 ASN B O 7934 C CB . ASN B 99 ? 1.4494 0.9910 1.5176 -0.2447 0.0359 0.1415 99 ASN B CB 7935 C CG . ASN B 99 ? 1.6094 1.1426 1.7168 -0.2593 0.0248 0.1666 99 ASN B CG 7936 O OD1 . ASN B 99 ? 1.3901 0.9133 1.5162 -0.2746 0.0019 0.1644 99 ASN B OD1 7937 N ND2 . ASN B 99 ? 2.0324 1.5691 2.1508 -0.2561 0.0405 0.1912 99 ASN B ND2 7938 N N . PHE B 100 ? 1.0335 0.5182 1.0472 -0.2238 0.0212 0.0806 100 PHE B N 7939 C CA . PHE B 100 ? 1.0182 0.4732 1.0310 -0.2164 0.0140 0.0693 100 PHE B CA 7940 C C . PHE B 100 ? 1.0286 0.4882 1.0297 -0.2027 0.0298 0.0827 100 PHE B C 7941 O O . PHE B 100 ? 0.9407 0.4247 0.9306 -0.1991 0.0479 0.0977 100 PHE B O 7942 C CB . PHE B 100 ? 1.0415 0.4798 1.0347 -0.2110 0.0069 0.0305 100 PHE B CB 7943 C CG . PHE B 100 ? 1.0447 0.5046 1.0064 -0.2010 0.0211 0.0143 100 PHE B CG 7944 C CD1 . PHE B 100 ? 1.2519 0.7150 1.1968 -0.1838 0.0342 0.0089 100 PHE B CD1 7945 C CD2 . PHE B 100 ? 1.0739 0.5507 1.0241 -0.2102 0.0193 0.0062 100 PHE B CD2 7946 C CE1 . PHE B 100 ? 1.2473 0.7302 1.1657 -0.1752 0.0464 -0.0051 100 PHE B CE1 7947 C CE2 . PHE B 100 ? 1.1057 0.6026 1.0289 -0.2019 0.0314 -0.0068 100 PHE B CE2 7948 C CZ . PHE B 100 ? 1.1299 0.6298 1.0377 -0.1840 0.0456 -0.0129 100 PHE B CZ 7949 N N . SER B 101 ? 1.2329 0.6677 1.2374 -0.1960 0.0222 0.0773 101 SER B N 7950 C CA . SER B 101 ? 1.2072 0.6425 1.2001 -0.1862 0.0318 0.0923 101 SER B CA 7951 C C . SER B 101 ? 1.1292 0.5484 1.1124 -0.1720 0.0275 0.0690 101 SER B C 7952 O O . SER B 101 ? 1.3968 0.7972 1.3915 -0.1705 0.0161 0.0439 101 SER B O 7953 C CB . SER B 101 ? 1.3892 0.8117 1.4053 -0.1954 0.0247 0.1233 101 SER B CB 7954 O OG . SER B 101 ? 1.4808 0.9004 1.4816 -0.1888 0.0306 0.1384 101 SER B OG 7955 N N . ILE B 102 ? 0.9746 0.4009 0.9376 -0.1623 0.0373 0.0772 102 ILE B N 7956 C CA . ILE B 102 ? 0.9940 0.4080 0.9530 -0.1488 0.0330 0.0599 102 ILE B CA 7957 C C . ILE B 102 ? 1.0012 0.4102 0.9531 -0.1460 0.0321 0.0842 102 ILE B C 7958 O O . ILE B 102 ? 0.9813 0.4061 0.9084 -0.1493 0.0449 0.1041 102 ILE B O 7959 C CB . ILE B 102 ? 0.9538 0.3862 0.8871 -0.1385 0.0454 0.0345 102 ILE B CB 7960 C CG1 . ILE B 102 ? 1.0983 0.5223 1.0296 -0.1243 0.0432 0.0217 102 ILE B CG1 7961 C CG2 . ILE B 102 ? 0.9183 0.3786 0.8245 -0.1401 0.0630 0.0481 102 ILE B CG2 7962 C CD1 . ILE B 102 ? 1.2858 0.7295 1.1923 -0.1146 0.0559 0.0006 102 ILE B CD1 7963 N N . GLN B 103 ? 0.9943 0.3802 0.9685 -0.1410 0.0167 0.0828 103 GLN B N 7964 C CA . GLN B 103 ? 1.0726 0.4518 1.0410 -0.1398 0.0108 0.1064 103 GLN B CA 7965 C C . GLN B 103 ? 1.1132 0.4945 1.0730 -0.1253 0.0111 0.0899 103 GLN B C 7966 O O . GLN B 103 ? 1.2522 0.6269 1.2319 -0.1152 0.0083 0.0618 103 GLN B O 7967 C CB . GLN B 103 ? 1.1144 0.4666 1.1211 -0.1459 -0.0101 0.1243 103 GLN B CB 7968 C CG . GLN B 103 ? 1.2393 0.5914 1.2462 -0.1626 -0.0111 0.1579 103 GLN B CG 7969 C CD . GLN B 103 ? 1.4632 0.8203 1.4833 -0.1710 -0.0069 0.1513 103 GLN B CD 7970 O OE1 . GLN B 103 ? 1.6423 0.9981 1.6715 -0.1660 -0.0070 0.1212 103 GLN B OE1 7971 N NE2 . GLN B 103 ? 1.4463 0.8090 1.4672 -0.1852 -0.0035 0.1805 103 GLN B NE2 7972 N N . VAL B 104 ? 1.0987 0.4888 1.0280 -0.1252 0.0153 0.1071 104 VAL B N 7973 C CA . VAL B 104 ? 1.1458 0.5384 1.0679 -0.1133 0.0132 0.0967 104 VAL B CA 7974 C C . VAL B 104 ? 1.0141 0.3941 0.9339 -0.1181 -0.0024 0.1264 104 VAL B C 7975 O O . VAL B 104 ? 1.0301 0.4111 0.9222 -0.1310 -0.0001 0.1536 104 VAL B O 7976 C CB . VAL B 104 ? 1.2144 0.6320 1.0949 -0.1090 0.0328 0.0851 104 VAL B CB 7977 C CG1 . VAL B 104 ? 1.2099 0.6302 1.0882 -0.0969 0.0291 0.0736 104 VAL B CG1 7978 C CG2 . VAL B 104 ? 1.3351 0.7666 1.2161 -0.1075 0.0462 0.0612 104 VAL B CG2 7979 N N . ARG B 105 ? 1.0212 0.3892 0.9707 -0.1089 -0.0182 0.1222 105 ARG B N 7980 C CA . ARG B 105 ? 1.0987 0.4533 1.0523 -0.1149 -0.0383 0.1528 105 ARG B CA 7981 C C . ARG B 105 ? 1.2559 0.6141 1.2109 -0.1048 -0.0457 0.1478 105 ARG B C 7982 O O . ARG B 105 ? 1.3143 0.6730 1.3043 -0.0900 -0.0456 0.1224 105 ARG B O 7983 C CB . ARG B 105 ? 1.1046 0.4344 1.1129 -0.1176 -0.0595 0.1650 105 ARG B CB 7984 C CG . ARG B 105 ? 1.1046 0.4194 1.1280 -0.1232 -0.0852 0.1974 105 ARG B CG 7985 C CD . ARG B 105 ? 1.1301 0.4199 1.2128 -0.1261 -0.1064 0.2107 105 ARG B CD 7986 N NE . ARG B 105 ? 1.2453 0.5307 1.3179 -0.1411 -0.1035 0.2274 105 ARG B NE 7987 C CZ . ARG B 105 ? 1.1655 0.4368 1.2816 -0.1453 -0.1180 0.2389 105 ARG B CZ 7988 N NH1 . ARG B 105 ? 1.1769 0.4413 1.3475 -0.1340 -0.1342 0.2328 105 ARG B NH1 7989 N NH2 . ARG B 105 ? 1.1752 0.4501 1.2793 -0.1583 -0.1124 0.2529 105 ARG B NH2 7990 N N . GLN B 106 ? 1.2678 0.6280 1.1838 -0.1141 -0.0517 0.1723 106 GLN B N 7991 C CA . GLN B 106 ? 1.0781 0.4383 0.9992 -0.1084 -0.0659 0.1762 106 GLN B CA 7992 C C . GLN B 106 ? 1.0907 0.4294 1.0661 -0.1098 -0.0953 0.1980 106 GLN B C 7993 O O . GLN B 106 ? 1.4286 0.7540 1.3970 -0.1255 -0.1098 0.2300 106 GLN B O 7994 C CB . GLN B 106 ? 1.1392 0.5058 0.9951 -0.1209 -0.0639 0.1950 106 GLN B CB 7995 C CG . GLN B 106 ? 1.1172 0.5024 0.9204 -0.1219 -0.0342 0.1786 106 GLN B CG 7996 C CD . GLN B 106 ? 1.3299 0.7320 1.1264 -0.1081 -0.0234 0.1516 106 GLN B CD 7997 O OE1 . GLN B 106 ? 1.6881 1.0907 1.5267 -0.0952 -0.0331 0.1386 106 GLN B OE1 7998 N NE2 . GLN B 106 ? 1.2303 0.6464 0.9769 -0.1110 -0.0024 0.1437 106 GLN B NE2 7999 N N . VAL B 107 ? 1.0811 0.4167 1.1133 -0.0940 -0.1036 0.1818 107 VAL B N 8000 C CA . VAL B 107 ? 1.1092 0.4237 1.2066 -0.0929 -0.1304 0.1999 107 VAL B CA 8001 C C . VAL B 107 ? 1.2263 0.5388 1.3368 -0.0944 -0.1551 0.2238 107 VAL B C 8002 O O . VAL B 107 ? 1.3848 0.7126 1.4789 -0.0874 -0.1495 0.2123 107 VAL B O 8003 C CB . VAL B 107 ? 1.0930 0.4006 1.2580 -0.0745 -0.1238 0.1670 107 VAL B CB 8004 C CG1 . VAL B 107 ? 1.1728 0.4734 1.3357 -0.0783 -0.1107 0.1533 107 VAL B CG1 8005 C CG2 . VAL B 107 ? 1.1366 0.4632 1.3009 -0.0579 -0.1045 0.1320 107 VAL B CG2 8006 N N . GLU B 108 ? 1.2087 0.5023 1.3503 -0.1049 -0.1845 0.2593 108 GLU B N 8007 C CA . GLU B 108 ? 1.3660 0.6666 1.5191 -0.1085 -0.2102 0.2846 108 GLU B CA 8008 C C . GLU B 108 ? 1.4745 0.7814 1.7062 -0.0871 -0.2158 0.2667 108 GLU B C 8009 O O . GLU B 108 ? 1.4501 0.7547 1.7359 -0.0710 -0.2033 0.2391 108 GLU B O 8010 C CB . GLU B 108 ? 1.3881 0.6898 1.5450 -0.1243 -0.2331 0.3202 108 GLU B CB 8011 C CG . GLU B 108 ? 1.4251 0.7243 1.5080 -0.1455 -0.2246 0.3383 108 GLU B CG 8012 C CD . GLU B 108 ? 1.6920 0.9939 1.7768 -0.1621 -0.2477 0.3739 108 GLU B CD 8013 O OE1 . GLU B 108 ? 1.8253 1.1320 1.9532 -0.1613 -0.2749 0.3903 108 GLU B OE1 8014 O OE2 . GLU B 108 ? 1.8100 1.1108 1.8557 -0.1762 -0.2387 0.3858 108 GLU B OE2 8015 N N . ASP B 109 ? 1.5005 0.8164 1.7363 -0.0881 -0.2335 0.2819 109 ASP B N 8016 C CA . ASP B 109 ? 1.3127 0.6390 1.6236 -0.0691 -0.2389 0.2690 109 ASP B CA 8017 C C . ASP B 109 ? 1.2509 0.5779 1.5805 -0.0485 -0.2083 0.2246 109 ASP B C 8018 O O . ASP B 109 ? 1.2793 0.6132 1.6796 -0.0297 -0.2011 0.2025 109 ASP B O 8019 C CB . ASP B 109 ? 1.2935 0.6227 1.6834 -0.0634 -0.2556 0.2782 109 ASP B CB 8020 C CG . ASP B 109 ? 1.6129 0.9570 2.0782 -0.0497 -0.2687 0.2782 109 ASP B CG 8021 O OD1 . ASP B 109 ? 1.7425 1.0958 2.2017 -0.0606 -0.2948 0.3079 109 ASP B OD1 8022 O OD2 . ASP B 109 ? 1.8037 1.1515 2.3337 -0.0291 -0.2524 0.2482 109 ASP B OD2 8023 N N . TYR B 110 ? 1.1435 0.4751 1.4028 -0.0523 -0.1857 0.2076 110 TYR B N 8024 C CA . TYR B 110 ? 1.0886 0.4373 1.3475 -0.0350 -0.1527 0.1625 110 TYR B CA 8025 C C . TYR B 110 ? 1.1781 0.5445 1.4547 -0.0248 -0.1538 0.1567 110 TYR B C 8026 O O . TYR B 110 ? 1.2339 0.6089 1.4629 -0.0357 -0.1643 0.1753 110 TYR B O 8027 C CB . TYR B 110 ? 1.1224 0.4820 1.2988 -0.0429 -0.1277 0.1475 110 TYR B CB 8028 C CG . TYR B 110 ? 1.1537 0.5259 1.3303 -0.0288 -0.0955 0.1032 110 TYR B CG 8029 C CD1 . TYR B 110 ? 1.0717 0.4316 1.2937 -0.0203 -0.0865 0.0812 110 TYR B CD1 8030 C CD2 . TYR B 110 ? 1.2288 0.6238 1.3577 -0.0260 -0.0750 0.0839 110 TYR B CD2 8031 C CE1 . TYR B 110 ? 1.0660 0.4358 1.2812 -0.0107 -0.0585 0.0414 110 TYR B CE1 8032 C CE2 . TYR B 110 ? 1.2505 0.6572 1.3766 -0.0158 -0.0477 0.0464 110 TYR B CE2 8033 C CZ . TYR B 110 ? 1.1983 0.5924 1.3650 -0.0090 -0.0398 0.0254 110 TYR B CZ 8034 O OH . TYR B 110 ? 1.2823 0.6865 1.4397 -0.0019 -0.0140 -0.0115 110 TYR B OH 8035 N N . PRO B 111 ? 1.1391 0.5103 1.4847 -0.0048 -0.1424 0.1305 111 PRO B N 8036 C CA . PRO B 111 ? 1.1339 0.5229 1.5129 0.0067 -0.1427 0.1253 111 PRO B CA 8037 C C . PRO B 111 ? 1.1818 0.5936 1.4877 0.0026 -0.1281 0.1154 111 PRO B C 8038 O O . PRO B 111 ? 1.1496 0.5685 1.3993 0.0008 -0.1034 0.0929 111 PRO B O 8039 C CB . PRO B 111 ? 1.0098 0.4003 1.4573 0.0284 -0.1185 0.0872 111 PRO B CB 8040 C CG . PRO B 111 ? 1.0097 0.3871 1.4328 0.0264 -0.1003 0.0653 111 PRO B CG 8041 C CD . PRO B 111 ? 1.0541 0.4138 1.4467 0.0076 -0.1248 0.1011 111 PRO B CD 8042 N N . VAL B 112 ? 1.1613 0.5837 1.4713 0.0003 -0.1451 0.1337 112 VAL B N 8043 C CA . VAL B 112 ? 1.0249 0.4657 1.2668 -0.0055 -0.1358 0.1284 112 VAL B CA 8044 C C . VAL B 112 ? 1.0482 0.5107 1.3313 0.0083 -0.1297 0.1153 112 VAL B C 8045 O O . VAL B 112 ? 1.0421 0.5043 1.3881 0.0120 -0.1521 0.1346 112 VAL B O 8046 C CB . VAL B 112 ? 1.0066 0.4381 1.1899 -0.0280 -0.1637 0.1658 112 VAL B CB 8047 C CG1 . VAL B 112 ? 1.1913 0.6394 1.3103 -0.0332 -0.1544 0.1584 112 VAL B CG1 8048 C CG2 . VAL B 112 ? 1.0273 0.4405 1.1625 -0.0431 -0.1652 0.1784 112 VAL B CG2 8049 N N . ASP B 113 ? 1.1117 0.5938 1.3620 0.0153 -0.1000 0.0844 113 ASP B N 8050 C CA . ASP B 113 ? 1.0901 0.5953 1.3691 0.0263 -0.0918 0.0725 113 ASP B CA 8051 C C . ASP B 113 ? 1.1127 0.6286 1.3248 0.0139 -0.0986 0.0835 113 ASP B C 8052 O O . ASP B 113 ? 1.1806 0.6978 1.3198 0.0057 -0.0844 0.0742 113 ASP B O 8053 C CB . ASP B 113 ? 1.0416 0.5621 1.3344 0.0419 -0.0539 0.0306 113 ASP B CB 8054 C CG . ASP B 113 ? 1.2978 0.8063 1.6609 0.0549 -0.0449 0.0150 113 ASP B CG 8055 O OD1 . ASP B 113 ? 1.5041 1.0112 1.8522 0.0595 -0.0184 -0.0156 113 ASP B OD1 8056 O OD2 . ASP B 113 ? 1.2996 0.7988 1.7340 0.0599 -0.0652 0.0337 113 ASP B OD2 8057 N N . ILE B 114 ? 1.0827 0.6055 1.3231 0.0123 -0.1209 0.1036 114 ILE B N 8058 C CA . ILE B 114 ? 1.0791 0.6092 1.2600 -0.0002 -0.1301 0.1140 114 ILE B CA 8059 C C . ILE B 114 ? 0.9361 0.4918 1.1548 0.0107 -0.1230 0.1034 114 ILE B C 8060 O O . ILE B 114 ? 0.9331 0.4941 1.2248 0.0172 -0.1399 0.1173 114 ILE B O 8061 C CB . ILE B 114 ? 0.9485 0.4596 1.1099 -0.0200 -0.1708 0.1547 114 ILE B CB 8062 C CG1 . ILE B 114 ? 1.1269 0.6137 1.2452 -0.0332 -0.1771 0.1677 114 ILE B CG1 8063 C CG2 . ILE B 114 ? 0.9534 0.4693 1.0519 -0.0336 -0.1797 0.1621 114 ILE B CG2 8064 C CD1 . ILE B 114 ? 1.0193 0.4859 1.1090 -0.0559 -0.2162 0.2083 114 ILE B CD1 8065 N N . TYR B 115 ? 0.8799 0.4521 1.0527 0.0125 -0.0983 0.0804 115 TYR B N 8066 C CA . TYR B 115 ? 0.8855 0.4829 1.0859 0.0205 -0.0913 0.0720 115 TYR B CA 8067 C C . TYR B 115 ? 0.8858 0.4840 1.0227 0.0052 -0.1051 0.0845 115 TYR B C 8068 O O . TYR B 115 ? 0.8852 0.4771 0.9473 -0.0039 -0.0944 0.0767 115 TYR B O 8069 C CB . TYR B 115 ? 0.9511 0.5691 1.1582 0.0349 -0.0515 0.0352 115 TYR B CB 8070 C CG . TYR B 115 ? 1.0550 0.7006 1.3083 0.0452 -0.0419 0.0269 115 TYR B CG 8071 C CD1 . TYR B 115 ? 1.2119 0.8668 1.5551 0.0596 -0.0396 0.0254 115 TYR B CD1 8072 C CD2 . TYR B 115 ? 0.8991 0.5616 1.1101 0.0404 -0.0344 0.0211 115 TYR B CD2 8073 C CE1 . TYR B 115 ? 1.1429 0.8249 1.5316 0.0688 -0.0286 0.0187 115 TYR B CE1 8074 C CE2 . TYR B 115 ? 0.9319 0.6208 1.1866 0.0488 -0.0258 0.0155 115 TYR B CE2 8075 C CZ . TYR B 115 ? 0.9986 0.6980 1.3416 0.0628 -0.0223 0.0145 115 TYR B CZ 8076 O OH . TYR B 115 ? 0.9016 0.6290 1.2911 0.0710 -0.0114 0.0097 115 TYR B OH 8077 N N . TYR B 116 ? 0.9038 0.5091 1.0741 0.0023 -0.1289 0.1038 116 TYR B N 8078 C CA . TYR B 116 ? 0.9420 0.5441 1.0552 -0.0140 -0.1466 0.1171 116 TYR B CA 8079 C C . TYR B 116 ? 1.1506 0.7786 1.2619 -0.0072 -0.1266 0.0980 116 TYR B C 8080 O O . TYR B 116 ? 1.2621 0.9131 1.4420 0.0066 -0.1184 0.0917 116 TYR B O 8081 C CB . TYR B 116 ? 0.9591 0.5512 1.1034 -0.0256 -0.1900 0.1531 116 TYR B CB 8082 C CG . TYR B 116 ? 1.0058 0.5691 1.0725 -0.0505 -0.2175 0.1762 116 TYR B CG 8083 C CD1 . TYR B 116 ? 1.0676 0.6079 1.1350 -0.0603 -0.2400 0.1995 116 TYR B CD1 8084 C CD2 . TYR B 116 ? 1.1220 0.6799 1.1136 -0.0651 -0.2201 0.1743 116 TYR B CD2 8085 C CE1 . TYR B 116 ? 1.2972 0.8109 1.2882 -0.0851 -0.2633 0.2206 116 TYR B CE1 8086 C CE2 . TYR B 116 ? 1.2735 0.8030 1.1891 -0.0890 -0.2420 0.1926 116 TYR B CE2 8087 C CZ . TYR B 116 ? 1.3626 0.8706 1.2759 -0.0995 -0.2630 0.2158 116 TYR B CZ 8088 O OH . TYR B 116 ? 1.4455 0.9252 1.2781 -0.1254 -0.2832 0.2342 116 TYR B OH 8089 N N . LEU B 117 ? 1.1732 0.7975 1.2080 -0.0170 -0.1177 0.0892 117 LEU B N 8090 C CA . LEU B 117 ? 0.9254 0.5709 0.9524 -0.0146 -0.1054 0.0767 117 LEU B CA 8091 C C . LEU B 117 ? 0.9820 0.6149 0.9699 -0.0327 -0.1350 0.0968 117 LEU B C 8092 O O . LEU B 117 ? 0.9524 0.5628 0.8658 -0.0477 -0.1403 0.0998 117 LEU B O 8093 C CB . LEU B 117 ? 0.8826 0.5349 0.8599 -0.0112 -0.0714 0.0498 117 LEU B CB 8094 C CG . LEU B 117 ? 0.8734 0.5419 0.8866 0.0053 -0.0406 0.0263 117 LEU B CG 8095 C CD1 . LEU B 117 ? 0.9209 0.5965 0.8829 0.0052 -0.0125 0.0043 117 LEU B CD1 8096 C CD2 . LEU B 117 ? 0.8601 0.5552 0.9488 0.0189 -0.0336 0.0211 117 LEU B CD2 8097 N N . MET B 118 ? 1.0810 0.7280 1.1204 -0.0318 -0.1534 0.1100 118 MET B N 8098 C CA . MET B 118 ? 1.1448 0.7782 1.1552 -0.0506 -0.1874 0.1319 118 MET B CA 8099 C C . MET B 118 ? 1.1747 0.8264 1.1793 -0.0506 -0.1800 0.1222 118 MET B C 8100 O O . MET B 118 ? 1.1653 0.8474 1.2272 -0.0352 -0.1615 0.1112 118 MET B O 8101 C CB . MET B 118 ? 1.1045 0.7360 1.1809 -0.0541 -0.2242 0.1626 118 MET B CB 8102 C CG . MET B 118 ? 1.1584 0.8206 1.3391 -0.0327 -0.2121 0.1589 118 MET B CG 8103 S SD . MET B 118 ? 1.9801 1.6382 2.2503 -0.0342 -0.2526 0.1957 118 MET B SD 8104 C CE . MET B 118 ? 0.9869 0.6123 1.2172 -0.0410 -0.2589 0.2023 118 MET B CE 8105 N N . ASP B 119 ? 1.1277 0.7598 1.0619 -0.0686 -0.1936 0.1260 119 ASP B N 8106 C CA . ASP B 119 ? 1.0024 0.6469 0.9271 -0.0713 -0.1909 0.1189 119 ASP B CA 8107 C C . ASP B 119 ? 1.1360 0.7854 1.1079 -0.0795 -0.2276 0.1443 119 ASP B C 8108 O O . ASP B 119 ? 1.2234 0.8472 1.1691 -0.0984 -0.2635 0.1667 119 ASP B O 8109 C CB . ASP B 119 ? 1.0200 0.6385 0.8502 -0.0867 -0.1872 0.1091 119 ASP B CB 8110 C CG . ASP B 119 ? 1.2291 0.8576 1.0494 -0.0898 -0.1843 0.1010 119 ASP B CG 8111 O OD1 . ASP B 119 ? 1.2013 0.8043 0.9525 -0.1057 -0.1912 0.0980 119 ASP B OD1 8112 O OD2 . ASP B 119 ? 1.5107 1.1716 1.3921 -0.0768 -0.1742 0.0972 119 ASP B OD2 8113 N N . LEU B 120 ? 1.1402 0.8232 1.1828 -0.0664 -0.2188 0.1420 120 LEU B N 8114 C CA . LEU B 120 ? 1.1730 0.8664 1.2756 -0.0720 -0.2516 0.1672 120 LEU B CA 8115 C C . LEU B 120 ? 1.0549 0.7493 1.1309 -0.0842 -0.2629 0.1680 120 LEU B C 8116 O O . LEU B 120 ? 1.0277 0.7342 1.1554 -0.0891 -0.2885 0.1879 120 LEU B O 8117 C CB . LEU B 120 ? 1.1650 0.8951 1.3728 -0.0505 -0.2361 0.1673 120 LEU B CB 8118 C CG . LEU B 120 ? 0.8858 0.6114 1.1565 -0.0472 -0.2574 0.1892 120 LEU B CG 8119 C CD1 . LEU B 120 ? 0.8547 0.5531 1.0764 -0.0490 -0.2526 0.1839 120 LEU B CD1 8120 C CD2 . LEU B 120 ? 0.8603 0.6218 1.2374 -0.0244 -0.2358 0.1848 120 LEU B CD2 8121 N N . SER B 121 ? 0.9293 0.6115 0.9300 -0.0889 -0.2437 0.1471 121 SER B N 8122 C CA . SER B 121 ? 0.9451 0.6243 0.9165 -0.1006 -0.2526 0.1454 121 SER B CA 8123 C C . SER B 121 ? 0.9832 0.6306 0.9202 -0.1261 -0.2994 0.1686 121 SER B C 8124 O O . SER B 121 ? 1.1179 0.7393 1.0268 -0.1374 -0.3205 0.1822 121 SER B O 8125 C CB . SER B 121 ? 0.9419 0.6104 0.8409 -0.1004 -0.2224 0.1185 121 SER B CB 8126 O OG . SER B 121 ? 1.0151 0.6457 0.8356 -0.1131 -0.2268 0.1154 121 SER B OG 8127 N N . TYR B 122 ? 0.9846 0.6339 0.9229 -0.1366 -0.3163 0.1739 122 TYR B N 8128 C CA . TYR B 122 ? 1.0524 0.6746 0.9673 -0.1624 -0.3645 0.1975 122 TYR B CA 8129 C C . TYR B 122 ? 1.2413 0.8145 1.0516 -0.1846 -0.3780 0.1948 122 TYR B C 8130 O O . TYR B 122 ? 1.3152 0.8624 1.1027 -0.2073 -0.4199 0.2179 122 TYR B O 8131 C CB . TYR B 122 ? 1.0409 0.6711 0.9649 -0.1697 -0.3743 0.1974 122 TYR B CB 8132 C CG . TYR B 122 ? 1.2213 0.8320 1.1454 -0.1950 -0.4275 0.2255 122 TYR B CG 8133 C CD1 . TYR B 122 ? 1.3658 1.0007 1.3817 -0.1934 -0.4556 0.2552 122 TYR B CD1 8134 C CD2 . TYR B 122 ? 1.2884 0.8557 1.1220 -0.2214 -0.4497 0.2223 122 TYR B CD2 8135 C CE1 . TYR B 122 ? 1.3517 0.9693 1.3707 -0.2182 -0.5077 0.2838 122 TYR B CE1 8136 C CE2 . TYR B 122 ? 1.4212 0.9684 1.2501 -0.2473 -0.5010 0.2483 122 TYR B CE2 8137 C CZ . TYR B 122 ? 1.3099 0.8830 1.2324 -0.2461 -0.5316 0.2804 122 TYR B CZ 8138 O OH . TYR B 122 ? 1.2067 0.7604 1.1275 -0.2736 -0.5860 0.3089 122 TYR B OH 8139 N N . SER B 123 ? 1.2485 0.8093 0.9958 -0.1792 -0.3426 0.1678 123 SER B N 8140 C CA . SER B 123 ? 1.1856 0.7013 0.8326 -0.1988 -0.3474 0.1619 123 SER B CA 8141 C C . SER B 123 ? 1.1662 0.6690 0.8076 -0.2036 -0.3614 0.1793 123 SER B C 8142 O O . SER B 123 ? 1.1883 0.6530 0.7509 -0.2247 -0.3749 0.1831 123 SER B O 8143 C CB . SER B 123 ? 1.1010 0.6116 0.6957 -0.1892 -0.3025 0.1293 123 SER B CB 8144 O OG . SER B 123 ? 1.0262 0.5649 0.6625 -0.1650 -0.2688 0.1192 123 SER B OG 8145 N N . MET B 124 ? 1.1016 0.6355 0.8272 -0.1845 -0.3573 0.1897 124 MET B N 8146 C CA . MET B 124 ? 1.2013 0.7264 0.9352 -0.1853 -0.3677 0.2059 124 MET B CA 8147 C C . MET B 124 ? 1.4124 0.9341 1.1927 -0.1994 -0.4179 0.2435 124 MET B C 8148 O O . MET B 124 ? 1.7738 1.2890 1.5714 -0.2010 -0.4318 0.2616 124 MET B O 8149 C CB . MET B 124 ? 1.1399 0.6968 0.9372 -0.1561 -0.3314 0.1928 124 MET B CB 8150 C CG . MET B 124 ? 1.0731 0.6265 0.8170 -0.1461 -0.2872 0.1620 124 MET B CG 8151 S SD . MET B 124 ? 1.1617 0.6792 0.8322 -0.1587 -0.2870 0.1655 124 MET B SD 8152 C CE . MET B 124 ? 1.9399 1.4745 1.6995 -0.1455 -0.2994 0.1868 124 MET B CE 8153 N N . LYS B 125 ? 1.1953 0.7216 0.9997 -0.2100 -0.4466 0.2570 125 LYS B N 8154 C CA . LYS B 125 ? 1.2740 0.7984 1.1282 -0.2249 -0.4979 0.2956 125 LYS B CA 8155 C C . LYS B 125 ? 1.3863 0.8655 1.1559 -0.2567 -0.5337 0.3147 125 LYS B C 8156 O O . LYS B 125 ? 1.3615 0.8359 1.1662 -0.2674 -0.5714 0.3482 125 LYS B O 8157 C CB . LYS B 125 ? 1.3205 0.8581 1.2132 -0.2320 -0.5217 0.3059 125 LYS B CB 8158 C CG . LYS B 125 ? 1.5049 1.0496 1.4733 -0.2434 -0.5731 0.3479 125 LYS B CG 8159 C CD . LYS B 125 ? 1.5998 1.1677 1.6286 -0.2443 -0.5897 0.3571 125 LYS B CD 8160 C CE . LYS B 125 ? 1.6539 1.1890 1.5915 -0.2717 -0.6094 0.3506 125 LYS B CE 8161 N NZ . LYS B 125 ? 1.6174 1.1747 1.6176 -0.2740 -0.6287 0.3623 125 LYS B NZ 8162 N N . ASP B 126 ? 1.5288 0.9749 1.1878 -0.2722 -0.5208 0.2936 126 ASP B N 8163 C CA . ASP B 126 ? 1.5540 0.9547 1.1169 -0.3039 -0.5472 0.3066 126 ASP B CA 8164 C C . ASP B 126 ? 1.4270 0.8226 0.9774 -0.2972 -0.5302 0.3081 126 ASP B C 8165 O O . ASP B 126 ? 1.4675 0.8353 0.9734 -0.3210 -0.5602 0.3318 126 ASP B O 8166 C CB . ASP B 126 ? 1.6978 1.0646 1.1487 -0.3214 -0.5330 0.2795 126 ASP B CB 8167 C CG . ASP B 126 ? 1.7562 1.1346 1.1888 -0.2969 -0.4733 0.2398 126 ASP B CG 8168 O OD1 . ASP B 126 ? 1.6566 1.0713 1.1593 -0.2712 -0.4496 0.2263 126 ASP B OD1 8169 O OD2 . ASP B 126 ? 1.8774 1.2293 1.2267 -0.3043 -0.4505 0.2233 126 ASP B OD2 8170 N N . ASP B 127 ? 1.3740 0.7960 0.9621 -0.2663 -0.4830 0.2838 127 ASP B N 8171 C CA . ASP B 127 ? 1.3872 0.8060 0.9667 -0.2576 -0.4624 0.2816 127 ASP B CA 8172 C C . ASP B 127 ? 1.4582 0.9047 1.1470 -0.2391 -0.4720 0.3023 127 ASP B C 8173 O O . ASP B 127 ? 1.5035 0.9503 1.2014 -0.2296 -0.4565 0.3019 127 ASP B O 8174 C CB . ASP B 127 ? 1.4109 0.8386 0.9620 -0.2370 -0.4058 0.2425 127 ASP B CB 8175 C CG . ASP B 127 ? 1.6934 1.1009 1.1604 -0.2489 -0.3909 0.2184 127 ASP B CG 8176 O OD1 . ASP B 127 ? 1.5337 0.9600 1.0305 -0.2383 -0.3810 0.2043 127 ASP B OD1 8177 O OD2 . ASP B 127 ? 2.0691 1.4414 1.4416 -0.2690 -0.3881 0.2135 127 ASP B OD2 8178 N N . LEU B 128 ? 1.4647 0.9342 1.2394 -0.2340 -0.4968 0.3202 128 LEU B N 8179 C CA . LEU B 128 ? 1.4456 0.9453 1.3375 -0.2121 -0.4992 0.3350 128 LEU B CA 8180 C C . LEU B 128 ? 1.4081 0.8908 1.3183 -0.2266 -0.5380 0.3720 128 LEU B C 8181 O O . LEU B 128 ? 1.2316 0.7345 1.2382 -0.2092 -0.5402 0.3851 128 LEU B O 8182 C CB . LEU B 128 ? 1.5074 1.0376 1.4889 -0.2033 -0.5130 0.3444 128 LEU B CB 8183 C CG . LEU B 128 ? 1.4082 0.9799 1.5072 -0.1696 -0.4856 0.3366 128 LEU B CG 8184 C CD1 . LEU B 128 ? 1.1488 0.7342 1.2249 -0.1465 -0.4275 0.2947 128 LEU B CD1 8185 C CD2 . LEU B 128 ? 1.5129 1.1140 1.6967 -0.1643 -0.5003 0.3486 128 LEU B CD2 8186 N N . TRP B 129 ? 1.4839 0.9286 1.3016 -0.2594 -0.5683 0.3889 129 TRP B N 8187 C CA . TRP B 129 ? 1.4299 0.8726 1.2601 -0.2761 -0.5953 0.4117 129 TRP B CA 8188 C C . TRP B 129 ? 1.4233 0.8636 1.2638 -0.2596 -0.5701 0.4077 129 TRP B C 8189 O O . TRP B 129 ? 1.4233 0.8734 1.3181 -0.2614 -0.5875 0.4272 129 TRP B O 8190 C CB . TRP B 129 ? 1.6056 1.0182 1.3279 -0.3150 -0.6164 0.4137 129 TRP B CB 8191 C CG . TRP B 129 ? 1.7571 1.1407 1.3628 -0.3196 -0.5823 0.3851 129 TRP B CG 8192 C CD1 . TRP B 129 ? 2.0816 1.4518 1.6242 -0.3235 -0.5684 0.3630 129 TRP B CD1 8193 C CD2 . TRP B 129 ? 1.7028 1.0696 1.2469 -0.3200 -0.5557 0.3745 129 TRP B CD2 8194 N NE1 . TRP B 129 ? 2.1742 1.5212 1.6218 -0.3259 -0.5331 0.3380 129 TRP B NE1 8195 C CE2 . TRP B 129 ? 1.9226 1.2677 1.3696 -0.3240 -0.5243 0.3449 129 TRP B CE2 8196 C CE3 . TRP B 129 ? 1.7170 1.0861 1.2824 -0.3177 -0.5548 0.3870 129 TRP B CE3 8197 C CZ2 . TRP B 129 ? 1.8932 1.2213 1.2676 -0.3252 -0.4906 0.3275 129 TRP B CZ2 8198 C CZ3 . TRP B 129 ? 1.8093 1.1600 1.2992 -0.3197 -0.5236 0.3712 129 TRP B CZ3 8199 C CH2 . TRP B 129 ? 1.8957 1.2272 1.2926 -0.3234 -0.4911 0.3417 129 TRP B CH2 8200 N N . SER B 130 ? 1.4341 0.8655 1.2263 -0.2442 -0.5266 0.3789 130 SER B N 8201 C CA . SER B 130 ? 1.6058 1.0362 1.3975 -0.2307 -0.4973 0.3682 130 SER B CA 8202 C C . SER B 130 ? 1.6175 1.0796 1.5304 -0.1988 -0.4819 0.3651 130 SER B C 8203 O O . SER B 130 ? 1.4381 0.8969 1.3743 -0.1910 -0.4741 0.3690 130 SER B O 8204 C CB . SER B 130 ? 1.5693 0.9948 1.2800 -0.2241 -0.4482 0.3281 130 SER B CB 8205 O OG . SER B 130 ? 1.3910 0.8436 1.1333 -0.2025 -0.4181 0.2987 130 SER B OG 8206 N N . ILE B 131 ? 1.7350 1.2267 1.7243 -0.1809 -0.4763 0.3574 131 ILE B N 8207 C CA . ILE B 131 ? 1.6179 1.1399 1.7209 -0.1503 -0.4566 0.3502 131 ILE B CA 8208 C C . ILE B 131 ? 1.5763 1.0969 1.7657 -0.1543 -0.4983 0.3906 131 ILE B C 8209 O O . ILE B 131 ? 1.5175 1.0506 1.7890 -0.1334 -0.4854 0.3891 131 ILE B O 8210 C CB . ILE B 131 ? 1.6617 1.2176 1.8202 -0.1307 -0.4346 0.3296 131 ILE B CB 8211 C CG1 . ILE B 131 ? 1.4910 1.0745 1.7307 -0.0978 -0.3936 0.3052 131 ILE B CG1 8212 C CG2 . ILE B 131 ? 1.8673 1.4329 2.0888 -0.1401 -0.4769 0.3610 131 ILE B CG2 8213 C CD1 . ILE B 131 ? 1.4505 1.0697 1.7626 -0.0794 -0.3759 0.2920 131 ILE B CD1 8214 N N . GLN B 132 ? 1.5435 1.0562 1.7136 -0.1819 -0.5441 0.4202 132 GLN B N 8215 C CA . GLN B 132 ? 1.4264 0.9568 1.6733 -0.1900 -0.5773 0.4475 132 GLN B CA 8216 C C . GLN B 132 ? 1.4127 0.9277 1.6350 -0.1945 -0.5749 0.4521 132 GLN B C 8217 O O . GLN B 132 ? 1.4241 0.9128 1.5512 -0.2000 -0.5551 0.4380 132 GLN B O 8218 C CB . GLN B 132 ? 1.4836 1.0126 1.7014 -0.2236 -0.6225 0.4703 132 GLN B CB 8219 C CG . GLN B 132 ? 1.6270 1.1659 1.8490 -0.2239 -0.6262 0.4649 132 GLN B CG 8220 C CD . GLN B 132 ? 1.6380 1.2142 1.9898 -0.1943 -0.6134 0.4635 132 GLN B CD 8221 O OE1 . GLN B 132 ? 1.7839 1.3824 2.2362 -0.1838 -0.6196 0.4765 132 GLN B OE1 8222 N NE2 . GLN B 132 ? 1.4743 1.0576 1.8257 -0.1811 -0.5936 0.4470 132 GLN B NE2 8223 N N . ASN B 133 ? 1.5267 1.0586 1.8352 -0.1931 -0.5943 0.4721 133 ASN B N 8224 C CA . ASN B 133 ? 1.6147 1.1356 1.9179 -0.1926 -0.5890 0.4757 133 ASN B CA 8225 C C . ASN B 133 ? 1.4934 1.0086 1.8028 -0.1621 -0.5407 0.4454 133 ASN B C 8226 O O . ASN B 133 ? 1.4061 0.9420 1.8135 -0.1341 -0.5210 0.4340 133 ASN B O 8227 C CB . ASN B 133 ? 1.7825 1.2754 1.9686 -0.2266 -0.6076 0.4866 133 ASN B CB 8228 C CG . ASN B 133 ? 1.7878 1.2852 1.9815 -0.2587 -0.6576 0.5183 133 ASN B CG 8229 O OD1 . ASN B 133 ? 1.6393 1.1288 1.8182 -0.2777 -0.6779 0.5370 133 ASN B OD1 8230 N ND2 . ASN B 133 ? 1.8413 1.3511 2.0600 -0.2664 -0.6783 0.5251 133 ASN B ND2 8231 N N . LEU B 134 ? 1.5680 1.0557 1.7765 -0.1685 -0.5203 0.4315 134 LEU B N 8232 C CA . LEU B 134 ? 1.5623 1.0417 1.7705 -0.1435 -0.4758 0.4025 134 LEU B CA 8233 C C . LEU B 134 ? 1.5111 1.0011 1.8106 -0.1246 -0.4675 0.4024 134 LEU B C 8234 O O . LEU B 134 ? 1.4226 0.9039 1.7067 -0.1373 -0.4814 0.4176 134 LEU B O 8235 C CB . LEU B 134 ? 1.4195 0.9186 1.6515 -0.1224 -0.4458 0.3732 134 LEU B CB 8236 C CG . LEU B 134 ? 1.2628 0.7704 1.4515 -0.1049 -0.3909 0.3271 134 LEU B CG 8237 C CD1 . LEU B 134 ? 1.2825 0.7654 1.3483 -0.1254 -0.3843 0.3219 134 LEU B CD1 8238 C CD2 . LEU B 134 ? 1.1359 0.6714 1.3419 -0.0892 -0.3643 0.2992 134 LEU B CD2 8239 N N . GLY B 135 ? 1.5005 1.0094 1.8944 -0.0953 -0.4440 0.3843 135 GLY B N 8240 C CA . GLY B 135 ? 1.5005 1.0163 1.9744 -0.0753 -0.4277 0.3755 135 GLY B CA 8241 C C . GLY B 135 ? 1.4564 0.9767 1.9686 -0.0885 -0.4602 0.4046 135 GLY B C 8242 O O . GLY B 135 ? 1.4061 0.9201 1.9417 -0.0809 -0.4494 0.3997 135 GLY B O 8243 N N . THR B 136 ? 1.5701 1.1008 2.0891 -0.1098 -0.5010 0.4346 136 THR B N 8244 C CA . THR B 136 ? 1.6276 1.1584 2.1610 -0.1299 -0.5365 0.4652 136 THR B CA 8245 C C . THR B 136 ? 1.7856 1.2874 2.2027 -0.1529 -0.5405 0.4712 136 THR B C 8246 O O . THR B 136 ? 1.8692 1.3640 2.2934 -0.1556 -0.5427 0.4787 136 THR B O 8247 C CB . THR B 136 ? 1.6064 1.1543 2.1702 -0.1513 -0.5811 0.4956 136 THR B CB 8248 O OG1 . THR B 136 ? 1.6757 1.2536 2.3595 -0.1306 -0.5770 0.4927 136 THR B OG1 8249 C CG2 . THR B 136 ? 1.5627 1.1079 2.1305 -0.1766 -0.6198 0.5281 136 THR B CG2 8250 N N . LYS B 137 ? 1.8692 1.3556 2.1819 -0.1695 -0.5401 0.4670 137 LYS B N 8251 C CA . LYS B 137 ? 1.8983 1.3580 2.0909 -0.1928 -0.5385 0.4691 137 LYS B CA 8252 C C . LYS B 137 ? 1.8108 1.2534 1.9596 -0.1769 -0.4948 0.4413 137 LYS B C 8253 O O . LYS B 137 ? 2.0128 1.4384 2.0972 -0.1898 -0.4891 0.4441 137 LYS B O 8254 C CB . LYS B 137 ? 1.9368 1.3869 2.0373 -0.2174 -0.5531 0.4722 137 LYS B CB 8255 C CG . LYS B 137 ? 1.9563 1.4176 2.0797 -0.2419 -0.6005 0.5014 137 LYS B CG 8256 C CD . LYS B 137 ? 1.8697 1.3197 1.9509 -0.2715 -0.6274 0.5257 137 LYS B CD 8257 C CE . LYS B 137 ? 1.8861 1.3487 2.0118 -0.2949 -0.6764 0.5568 137 LYS B CE 8258 N NZ . LYS B 137 ? 1.8615 1.3502 2.1234 -0.2764 -0.6881 0.5704 137 LYS B NZ 8259 N N . LEU B 138 ? 1.5801 1.0282 1.7663 -0.1502 -0.4642 0.4147 138 LEU B N 8260 C CA . LEU B 138 ? 1.5377 0.9711 1.6940 -0.1344 -0.4229 0.3858 138 LEU B CA 8261 C C . LEU B 138 ? 1.6226 1.0523 1.8162 -0.1269 -0.4150 0.3862 138 LEU B C 8262 O O . LEU B 138 ? 1.5700 0.9813 1.6986 -0.1349 -0.4004 0.3816 138 LEU B O 8263 C CB . LEU B 138 ? 1.4056 0.8600 1.6195 -0.1057 -0.3918 0.3533 138 LEU B CB 8264 C CG . LEU B 138 ? 1.3442 0.8107 1.4906 -0.0972 -0.3472 0.3109 138 LEU B CG 8265 C CD1 . LEU B 138 ? 1.2674 0.7590 1.4800 -0.0661 -0.3072 0.2733 138 LEU B CD1 8266 C CD2 . LEU B 138 ? 1.4925 0.9404 1.5390 -0.1109 -0.3306 0.3030 138 LEU B CD2 8267 N N . ALA B 139 ? 1.7183 1.1668 2.0202 -0.1121 -0.4246 0.3919 139 ALA B N 8268 C CA . ALA B 139 ? 1.6835 1.1312 2.0348 -0.1066 -0.4246 0.3965 139 ALA B CA 8269 C C . ALA B 139 ? 1.7123 1.1467 1.9992 -0.1344 -0.4478 0.4233 139 ALA B C 8270 O O . ALA B 139 ? 1.8542 1.2736 2.1053 -0.1353 -0.4305 0.4163 139 ALA B O 8271 C CB . ALA B 139 ? 1.7026 1.1743 2.1732 -0.0932 -0.4395 0.4048 139 ALA B CB 8272 N N . THR B 140 ? 1.6919 1.1328 1.9651 -0.1581 -0.4866 0.4534 140 THR B N 8273 C CA . THR B 140 ? 1.8454 1.2790 2.0821 -0.1848 -0.5138 0.4821 140 THR B CA 8274 C C . THR B 140 ? 1.8870 1.2986 2.0255 -0.1957 -0.4921 0.4746 140 THR B C 8275 O O . THR B 140 ? 1.9419 1.3483 2.0869 -0.1995 -0.4928 0.4835 140 THR B O 8276 C CB . THR B 140 ? 2.0934 1.5300 2.2876 -0.2172 -0.5557 0.5112 140 THR B CB 8277 O OG1 . THR B 140 ? 2.0711 1.4905 2.1449 -0.2355 -0.5462 0.5032 140 THR B OG1 8278 C CG2 . THR B 140 ? 2.1058 1.5649 2.3830 -0.2125 -0.5805 0.5213 140 THR B CG2 8279 N N . GLN B 141 ? 1.8639 1.2637 1.9136 -0.2011 -0.4724 0.4583 141 GLN B N 8280 C CA . GLN B 141 ? 1.8909 1.2721 1.8435 -0.2133 -0.4496 0.4505 141 GLN B CA 8281 C C . GLN B 141 ? 1.8349 1.2096 1.8079 -0.1894 -0.4109 0.4240 141 GLN B C 8282 O O . GLN B 141 ? 1.8862 1.2481 1.7990 -0.1963 -0.3901 0.4182 141 GLN B O 8283 C CB . GLN B 141 ? 1.9108 1.2826 1.7608 -0.2303 -0.4436 0.4427 141 GLN B CB 8284 C CG . GLN B 141 ? 2.0515 1.4195 1.8408 -0.2641 -0.4739 0.4674 141 GLN B CG 8285 C CD . GLN B 141 ? 2.1810 1.5474 1.9805 -0.2754 -0.4851 0.4881 141 GLN B CD 8286 O OE1 . GLN B 141 ? 2.3310 1.6882 2.0946 -0.2738 -0.4585 0.4795 141 GLN B OE1 8287 N NE2 . GLN B 141 ? 2.0753 1.4519 1.9311 -0.2863 -0.5249 0.5162 141 GLN B NE2 8288 N N . MET B 142 ? 1.6928 1.0772 1.7536 -0.1621 -0.4006 0.4072 142 MET B N 8289 C CA . MET B 142 ? 1.5503 0.9283 1.6394 -0.1409 -0.3671 0.3812 142 MET B CA 8290 C C . MET B 142 ? 1.4812 0.8630 1.6457 -0.1331 -0.3740 0.3890 142 MET B C 8291 O O . MET B 142 ? 1.4428 0.8170 1.6229 -0.1203 -0.3490 0.3696 142 MET B O 8292 C CB . MET B 142 ? 1.4976 0.8827 1.6366 -0.1154 -0.3459 0.3521 142 MET B CB 8293 C CG . MET B 142 ? 1.4938 0.8894 1.5566 -0.1173 -0.3233 0.3282 142 MET B CG 8294 S SD . MET B 142 ? 1.4272 0.8238 1.4152 -0.1138 -0.2760 0.2931 142 MET B SD 8295 C CE . MET B 142 ? 1.4542 0.8605 1.5375 -0.0844 -0.2522 0.2651 142 MET B CE 8296 N N . ARG B 143 ? 1.5468 0.9399 1.7580 -0.1422 -0.4086 0.4169 143 ARG B N 8297 C CA . ARG B 143 ? 1.5555 0.9534 1.8468 -0.1345 -0.4173 0.4249 143 ARG B CA 8298 C C . ARG B 143 ? 1.6105 0.9938 1.8502 -0.1486 -0.4125 0.4336 143 ARG B C 8299 O O . ARG B 143 ? 1.7522 1.1333 2.0434 -0.1382 -0.4055 0.4286 143 ARG B O 8300 C CB . ARG B 143 ? 1.6333 1.0480 1.9877 -0.1436 -0.4583 0.4554 143 ARG B CB 8301 C CG . ARG B 143 ? 1.7018 1.1231 2.1489 -0.1353 -0.4690 0.4641 143 ARG B CG 8302 C CD . ARG B 143 ? 1.6844 1.1238 2.1963 -0.1466 -0.5115 0.4963 143 ARG B CD 8303 N NE . ARG B 143 ? 1.6295 1.0868 2.1979 -0.1340 -0.5147 0.4895 143 ARG B NE 8304 C CZ . ARG B 143 ? 1.5787 1.0423 2.1106 -0.1500 -0.5360 0.5042 143 ARG B CZ 8305 N NH1 . ARG B 143 ? 1.6573 1.1094 2.0922 -0.1798 -0.5550 0.5245 143 ARG B NH1 8306 N NH2 . ARG B 143 ? 1.4678 0.9495 2.0600 -0.1370 -0.5373 0.4976 143 ARG B NH2 8307 N N . LYS B 144 ? 1.6242 0.9981 1.7620 -0.1726 -0.4147 0.4455 144 LYS B N 8308 C CA . LYS B 144 ? 1.7680 1.1302 1.8475 -0.1882 -0.4070 0.4543 144 LYS B CA 8309 C C . LYS B 144 ? 1.7097 1.0621 1.7925 -0.1711 -0.3699 0.4263 144 LYS B C 8310 O O . LYS B 144 ? 1.8692 1.2184 1.9848 -0.1685 -0.3677 0.4294 144 LYS B O 8311 C CB . LYS B 144 ? 1.9207 1.2759 1.8858 -0.2144 -0.4066 0.4632 144 LYS B CB 8312 C CG . LYS B 144 ? 2.0883 1.4507 2.0367 -0.2345 -0.4423 0.4868 144 LYS B CG 8313 C CD . LYS B 144 ? 2.1561 1.5091 1.9865 -0.2611 -0.4371 0.4903 144 LYS B CD 8314 C CE . LYS B 144 ? 2.0265 1.3711 1.7963 -0.2515 -0.3964 0.4594 144 LYS B CE 8315 N NZ . LYS B 144 ? 1.9697 1.3074 1.6315 -0.2751 -0.3905 0.4578 144 LYS B NZ 8316 N N . LEU B 145 ? 1.4231 0.7707 1.4719 -0.1610 -0.3423 0.3993 145 LEU B N 8317 C CA . LEU B 145 ? 1.3618 0.6996 1.4047 -0.1481 -0.3078 0.3719 145 LEU B CA 8318 C C . LEU B 145 ? 1.3288 0.6702 1.4687 -0.1207 -0.2977 0.3478 145 LEU B C 8319 O O . LEU B 145 ? 1.4897 0.8249 1.6535 -0.1135 -0.2831 0.3357 145 LEU B O 8320 C CB . LEU B 145 ? 1.3273 0.6586 1.2950 -0.1497 -0.2826 0.3520 145 LEU B CB 8321 C CG . LEU B 145 ? 1.3586 0.6861 1.2216 -0.1757 -0.2830 0.3673 145 LEU B CG 8322 C CD1 . LEU B 145 ? 1.2580 0.5938 1.0577 -0.1708 -0.2478 0.3352 145 LEU B CD1 8323 C CD2 . LEU B 145 ? 1.4991 0.8232 1.3321 -0.1914 -0.2813 0.3841 145 LEU B CD2 8324 N N . THR B 146 ? 1.2707 0.6232 1.4662 -0.1059 -0.3039 0.3392 146 THR B N 8325 C CA . THR B 146 ? 1.2363 0.5941 1.5166 -0.0789 -0.2865 0.3091 146 THR B CA 8326 C C . THR B 146 ? 1.4015 0.7768 1.7748 -0.0672 -0.3062 0.3166 146 THR B C 8327 O O . THR B 146 ? 1.5843 0.9711 1.9639 -0.0682 -0.3198 0.3254 146 THR B O 8328 C CB . THR B 146 ? 1.3838 0.7449 1.6406 -0.0652 -0.2547 0.2726 146 THR B CB 8329 O OG1 . THR B 146 ? 1.7610 1.1219 1.9485 -0.0701 -0.2269 0.2538 146 THR B OG1 8330 C CG2 . THR B 146 ? 1.1328 0.5030 1.4764 -0.0382 -0.2365 0.2405 146 THR B CG2 8331 N N . SER B 147 ? 1.3945 0.7721 1.8411 -0.0571 -0.3080 0.3136 147 SER B N 8332 C CA . SER B 147 ? 1.4007 0.7955 1.9485 -0.0403 -0.3155 0.3096 147 SER B CA 8333 C C . SER B 147 ? 1.5214 0.9205 2.1051 -0.0148 -0.2787 0.2648 147 SER B C 8334 O O . SER B 147 ? 1.5050 0.8915 2.0491 -0.0102 -0.2506 0.2374 147 SER B O 8335 C CB . SER B 147 ? 1.4190 0.8141 2.0305 -0.0408 -0.3314 0.3236 147 SER B CB 8336 O OG . SER B 147 ? 1.3985 0.7802 2.0130 -0.0316 -0.3060 0.2973 147 SER B OG 8337 N N . ASN B 148 ? 1.7245 1.1428 2.3830 0.0004 -0.2785 0.2574 148 ASN B N 8338 C CA . ASN B 148 ? 1.7186 1.1453 2.4112 0.0237 -0.2421 0.2147 148 ASN B CA 8339 C C . ASN B 148 ? 1.4759 0.8981 2.0943 0.0230 -0.2221 0.1969 148 ASN B C 8340 O O . ASN B 148 ? 1.2933 0.7040 1.8725 0.0272 -0.1940 0.1676 148 ASN B O 8341 C CB . ASN B 148 ? 1.7478 1.1660 2.4709 0.0366 -0.2160 0.1827 148 ASN B CB 8342 C CG . ASN B 148 ? 1.6120 1.0404 2.3643 0.0583 -0.1765 0.1362 148 ASN B CG 8343 O OD1 . ASN B 148 ? 1.6159 1.0635 2.4013 0.0679 -0.1708 0.1307 148 ASN B OD1 8344 N ND2 . ASN B 148 ? 1.4837 0.9003 2.2209 0.0646 -0.1490 0.1027 148 ASN B ND2 8345 N N . LEU B 149 ? 1.4049 0.8362 2.0044 0.0158 -0.2387 0.2158 149 LEU B N 8346 C CA . LEU B 149 ? 1.3758 0.8064 1.9162 0.0162 -0.2212 0.1994 149 LEU B CA 8347 C C . LEU B 149 ? 1.2842 0.7385 1.8830 0.0316 -0.2143 0.1888 149 LEU B C 8348 O O . LEU B 149 ? 1.3273 0.7980 1.9970 0.0347 -0.2336 0.2068 149 LEU B O 8349 C CB . LEU B 149 ? 1.3702 0.7969 1.8143 -0.0091 -0.2423 0.2271 149 LEU B CB 8350 C CG . LEU B 149 ? 1.1835 0.6178 1.6302 -0.0199 -0.2743 0.2580 149 LEU B CG 8351 C CD1 . LEU B 149 ? 1.1424 0.5975 1.5279 -0.0197 -0.2545 0.2369 149 LEU B CD1 8352 C CD2 . LEU B 149 ? 1.2196 0.6392 1.6166 -0.0471 -0.3114 0.3001 149 LEU B CD2 8353 N N . ARG B 150 ? 1.1113 0.5866 1.6701 0.0391 -0.1818 0.1556 150 ARG B N 8354 C CA . ARG B 150 ? 1.1381 0.6384 1.7495 0.0535 -0.1709 0.1436 150 ARG B CA 8355 C C . ARG B 150 ? 1.2058 0.7249 1.7434 0.0443 -0.1675 0.1418 150 ARG B C 8356 O O . ARG B 150 ? 1.3352 0.8573 1.7917 0.0394 -0.1455 0.1210 150 ARG B O 8357 C CB . ARG B 150 ? 1.1803 0.6898 1.8385 0.0759 -0.1288 0.0990 150 ARG B CB 8358 C CG . ARG B 150 ? 1.3327 0.8243 2.0555 0.0850 -0.1261 0.0928 150 ARG B CG 8359 C CD . ARG B 150 ? 1.4379 0.9495 2.2225 0.1060 -0.0887 0.0535 150 ARG B CD 8360 N NE . ARG B 150 ? 1.5921 1.1071 2.3290 0.1126 -0.0504 0.0138 150 ARG B NE 8361 C CZ . ARG B 150 ? 1.5496 1.0822 2.3156 0.1272 -0.0128 -0.0248 150 ARG B CZ 8362 N NH1 . ARG B 150 ? 1.5975 1.1430 2.4431 0.1376 -0.0071 -0.0296 150 ARG B NH1 8363 N NH2 . ARG B 150 ? 1.3524 0.8903 2.0656 0.1294 0.0194 -0.0582 150 ARG B NH2 8364 N N . ILE B 151 ? 1.1716 0.7027 1.7414 0.0415 -0.1910 0.1651 151 ILE B N 8365 C CA . ILE B 151 ? 1.2421 0.7886 1.7479 0.0316 -0.1924 0.1663 151 ILE B CA 8366 C C . ILE B 151 ? 1.2441 0.8207 1.7974 0.0482 -0.1690 0.1445 151 ILE B C 8367 O O . ILE B 151 ? 1.1139 0.6996 1.7524 0.0673 -0.1518 0.1295 151 ILE B O 8368 C CB . ILE B 151 ? 1.0969 0.6330 1.5861 0.0104 -0.2398 0.2111 151 ILE B CB 8369 C CG1 . ILE B 151 ? 0.9771 0.5173 1.5776 0.0172 -0.2675 0.2378 151 ILE B CG1 8370 C CG2 . ILE B 151 ? 1.1180 0.6256 1.5441 -0.0093 -0.2596 0.2322 151 ILE B CG2 8371 C CD1 . ILE B 151 ? 1.0141 0.5417 1.6029 -0.0062 -0.3192 0.2855 151 ILE B CD1 8372 N N . GLY B 152 ? 1.3613 0.9524 1.8603 0.0402 -0.1685 0.1435 152 GLY B N 8373 C CA . GLY B 152 ? 1.3015 0.9226 1.8328 0.0529 -0.1459 0.1242 152 GLY B CA 8374 C C . GLY B 152 ? 1.0471 0.6768 1.4924 0.0403 -0.1441 0.1209 152 GLY B C 8375 O O . GLY B 152 ? 0.9694 0.5816 1.3296 0.0247 -0.1514 0.1256 152 GLY B O 8376 N N . PHE B 153 ? 0.9635 0.6196 1.4326 0.0467 -0.1332 0.1128 153 PHE B N 8377 C CA . PHE B 153 ? 0.9815 0.6447 1.3769 0.0344 -0.1350 0.1121 153 PHE B CA 8378 C C . PHE B 153 ? 0.9514 0.6468 1.3682 0.0455 -0.1072 0.0906 153 PHE B C 8379 O O . PHE B 153 ? 0.9571 0.6718 1.4542 0.0619 -0.0906 0.0810 153 PHE B O 8380 C CB . PHE B 153 ? 1.0571 0.7088 1.4414 0.0156 -0.1809 0.1499 153 PHE B CB 8381 C CG . PHE B 153 ? 1.0779 0.7480 1.5529 0.0211 -0.1998 0.1693 153 PHE B CG 8382 C CD1 . PHE B 153 ? 1.0299 0.7199 1.5031 0.0179 -0.2024 0.1710 153 PHE B CD1 8383 C CD2 . PHE B 153 ? 1.2388 0.9065 1.8060 0.0292 -0.2158 0.1874 153 PHE B CD2 8384 C CE1 . PHE B 153 ? 1.2585 0.9672 1.8197 0.0223 -0.2203 0.1908 153 PHE B CE1 8385 C CE2 . PHE B 153 ? 1.3384 1.0247 1.9971 0.0345 -0.2331 0.2071 153 PHE B CE2 8386 C CZ . PHE B 153 ? 1.3870 1.0945 2.0425 0.0308 -0.2354 0.2092 153 PHE B CZ 8387 N N . GLY B 154 ? 0.9265 0.6267 1.2708 0.0360 -0.1013 0.0832 154 GLY B N 8388 C CA . GLY B 154 ? 0.8900 0.6197 1.2437 0.0422 -0.0799 0.0678 154 GLY B CA 8389 C C . GLY B 154 ? 0.9135 0.6397 1.2030 0.0254 -0.0984 0.0795 154 GLY B C 8390 O O . GLY B 154 ? 0.9630 0.6632 1.1881 0.0100 -0.1184 0.0916 154 GLY B O 8391 N N . ALA B 155 ? 0.8536 0.6049 1.1597 0.0277 -0.0907 0.0756 155 ALA B N 8392 C CA . ALA B 155 ? 0.8545 0.6016 1.1084 0.0118 -0.1101 0.0871 155 ALA B CA 8393 C C . ALA B 155 ? 0.8703 0.6373 1.0901 0.0141 -0.0814 0.0647 155 ALA B C 8394 O O . ALA B 155 ? 0.8379 0.6290 1.0894 0.0278 -0.0493 0.0446 155 ALA B O 8395 C CB . ALA B 155 ? 0.7994 0.5543 1.1109 0.0068 -0.1429 0.1150 155 ALA B CB 8396 N N . PHE B 156 ? 0.8514 0.6064 1.0053 -0.0005 -0.0933 0.0687 156 PHE B N 8397 C CA . PHE B 156 ? 0.8294 0.6007 0.9512 -0.0007 -0.0716 0.0521 156 PHE B CA 8398 C C . PHE B 156 ? 0.9796 0.7442 1.0753 -0.0157 -0.0975 0.0671 156 PHE B C 8399 O O . PHE B 156 ? 1.0907 0.8283 1.1578 -0.0298 -0.1288 0.0849 156 PHE B O 8400 C CB . PHE B 156 ? 0.8207 0.5795 0.8741 -0.0018 -0.0489 0.0322 156 PHE B CB 8401 C CG . PHE B 156 ? 0.8927 0.6162 0.8775 -0.0167 -0.0677 0.0409 156 PHE B CG 8402 C CD1 . PHE B 156 ? 0.8471 0.5585 0.7765 -0.0298 -0.0763 0.0427 156 PHE B CD1 8403 C CD2 . PHE B 156 ? 1.0799 0.7815 1.0557 -0.0180 -0.0754 0.0468 156 PHE B CD2 8404 C CE1 . PHE B 156 ? 0.8417 0.5196 0.7054 -0.0441 -0.0898 0.0485 156 PHE B CE1 8405 C CE2 . PHE B 156 ? 1.0674 0.7375 0.9776 -0.0330 -0.0902 0.0552 156 PHE B CE2 8406 C CZ . PHE B 156 ? 0.8497 0.5077 0.7023 -0.0461 -0.0961 0.0551 156 PHE B CZ 8407 N N . VAL B 157 ? 0.8733 0.6611 0.9770 -0.0142 -0.0852 0.0601 157 VAL B N 8408 C CA . VAL B 157 ? 0.8129 0.5924 0.8866 -0.0288 -0.1069 0.0706 157 VAL B CA 8409 C C . VAL B 157 ? 0.7584 0.5401 0.7787 -0.0308 -0.0842 0.0519 157 VAL B C 8410 O O . VAL B 157 ? 0.7623 0.5163 0.7150 -0.0410 -0.0882 0.0477 157 VAL B O 8411 C CB . VAL B 157 ? 0.8075 0.6127 0.9509 -0.0278 -0.1211 0.0863 157 VAL B CB 8412 C CG1 . VAL B 157 ? 0.8584 0.6524 0.9677 -0.0444 -0.1446 0.0959 157 VAL B CG1 8413 C CG2 . VAL B 157 ? 0.7775 0.5811 0.9826 -0.0260 -0.1457 0.1077 157 VAL B CG2 8414 N N . ASP B 158 ? 0.7710 0.5858 0.8238 -0.0214 -0.0598 0.0415 158 ASP B N 8415 C CA . ASP B 158 ? 0.7560 0.5777 0.7692 -0.0224 -0.0375 0.0258 158 ASP B CA 8416 C C . ASP B 158 ? 0.7146 0.5763 0.7744 -0.0115 -0.0102 0.0167 158 ASP B C 8417 O O . ASP B 158 ? 0.7230 0.6045 0.8427 -0.0024 -0.0056 0.0201 158 ASP B O 8418 C CB . ASP B 158 ? 0.8601 0.6683 0.8398 -0.0363 -0.0563 0.0329 158 ASP B CB 8419 C CG . ASP B 158 ? 0.8282 0.6239 0.7477 -0.0403 -0.0400 0.0180 158 ASP B CG 8420 O OD1 . ASP B 158 ? 0.7053 0.5154 0.6214 -0.0319 -0.0124 0.0039 158 ASP B OD1 8421 O OD2 . ASP B 158 ? 0.8538 0.6243 0.7308 -0.0525 -0.0551 0.0204 158 ASP B OD2 8422 N N . LYS B 159 ? 0.6940 0.5672 0.7273 -0.0131 0.0087 0.0058 159 LYS B N 8423 C CA . LYS B 159 ? 0.6797 0.5904 0.7484 -0.0063 0.0343 -0.0017 159 LYS B CA 8424 C C . LYS B 159 ? 0.7164 0.6503 0.8338 -0.0088 0.0235 0.0131 159 LYS B C 8425 O O . LYS B 159 ? 0.8230 0.7497 0.9237 -0.0188 0.0062 0.0223 159 LYS B O 8426 C CB . LYS B 159 ? 0.6500 0.5655 0.6752 -0.0095 0.0541 -0.0142 159 LYS B CB 8427 C CG . LYS B 159 ? 0.6435 0.5451 0.6327 -0.0060 0.0701 -0.0293 159 LYS B CG 8428 C CD . LYS B 159 ? 0.6957 0.6058 0.6510 -0.0103 0.0874 -0.0381 159 LYS B CD 8429 C CE . LYS B 159 ? 0.6986 0.5975 0.6235 -0.0077 0.1023 -0.0517 159 LYS B CE 8430 N NZ . LYS B 159 ? 0.8955 0.8077 0.8487 0.0008 0.1185 -0.0620 159 LYS B NZ 8431 N N . PRO B 160 ? 0.7082 0.6694 0.8890 0.0004 0.0345 0.0151 160 PRO B N 8432 C CA . PRO B 160 ? 0.7358 0.7243 0.9758 -0.0004 0.0277 0.0301 160 PRO B CA 8433 C C . PRO B 160 ? 0.8704 0.8895 1.1104 -0.0036 0.0483 0.0264 160 PRO B C 8434 O O . PRO B 160 ? 1.1197 1.1714 1.3989 0.0030 0.0745 0.0209 160 PRO B O 8435 C CB . PRO B 160 ? 0.6827 0.6884 0.9892 0.0126 0.0402 0.0291 160 PRO B CB 8436 C CG . PRO B 160 ? 0.7383 0.7394 1.0162 0.0202 0.0686 0.0060 160 PRO B CG 8437 C CD . PRO B 160 ? 0.7077 0.6744 0.9099 0.0124 0.0564 0.0015 160 PRO B CD 8438 N N . VAL B 161 ? 0.7889 0.7963 0.9870 -0.0147 0.0357 0.0306 161 VAL B N 8439 C CA . VAL B 161 ? 0.7962 0.8246 0.9789 -0.0200 0.0523 0.0273 161 VAL B CA 8440 C C . VAL B 161 ? 1.0634 1.0799 1.2323 -0.0321 0.0269 0.0407 161 VAL B C 8441 O O . VAL B 161 ? 1.2070 1.2120 1.3961 -0.0366 -0.0006 0.0549 161 VAL B O 8442 C CB . VAL B 161 ? 0.7575 0.7775 0.8854 -0.0197 0.0727 0.0096 161 VAL B CB 8443 C CG1 . VAL B 161 ? 0.8277 0.8705 0.9699 -0.0113 0.1048 -0.0051 161 VAL B CG1 8444 C CG2 . VAL B 161 ? 0.9114 0.8903 0.9923 -0.0206 0.0579 0.0045 161 VAL B CG2 8445 N N . SER B 162 ? 1.1689 1.1894 1.3068 -0.0381 0.0363 0.0368 162 SER B N 8446 C CA . SER B 162 ? 1.0135 1.0166 1.1277 -0.0493 0.0167 0.0443 162 SER B CA 8447 C C . SER B 162 ? 0.7842 0.7403 0.8565 -0.0535 -0.0078 0.0421 162 SER B C 8448 O O . SER B 162 ? 0.8365 0.7796 0.9099 -0.0486 -0.0137 0.0405 162 SER B O 8449 C CB . SER B 162 ? 1.0686 1.0804 1.1538 -0.0525 0.0353 0.0371 162 SER B CB 8450 O OG . SER B 162 ? 1.1609 1.1921 1.2425 -0.0454 0.0636 0.0252 162 SER B OG 8451 N N . PRO B 163 ? 0.7616 0.6910 0.7979 -0.0632 -0.0221 0.0421 163 PRO B N 8452 C CA . PRO B 163 ? 0.7604 0.6549 0.7811 -0.0723 -0.0541 0.0489 163 PRO B CA 8453 C C . PRO B 163 ? 0.7404 0.6128 0.7512 -0.0704 -0.0677 0.0496 163 PRO B C 8454 O O . PRO B 163 ? 0.8632 0.7186 0.8797 -0.0790 -0.0969 0.0614 163 PRO B O 8455 C CB . PRO B 163 ? 0.7416 0.6027 0.7067 -0.0793 -0.0549 0.0383 163 PRO B CB 8456 C CG . PRO B 163 ? 0.7083 0.5777 0.6538 -0.0712 -0.0262 0.0251 163 PRO B CG 8457 C CD . PRO B 163 ? 0.6988 0.6144 0.6897 -0.0641 -0.0073 0.0295 163 PRO B CD 8458 N N . TYR B 164 ? 0.7154 0.5872 0.7120 -0.0609 -0.0492 0.0386 164 TYR B N 8459 C CA . TYR B 164 ? 0.7210 0.5719 0.7088 -0.0592 -0.0611 0.0402 164 TYR B CA 8460 C C . TYR B 164 ? 0.7500 0.6112 0.7921 -0.0604 -0.0847 0.0588 164 TYR B C 8461 O O . TYR B 164 ? 0.9615 0.7954 0.9897 -0.0685 -0.1121 0.0682 164 TYR B O 8462 C CB . TYR B 164 ? 0.7329 0.5945 0.7192 -0.0466 -0.0337 0.0273 164 TYR B CB 8463 C CG . TYR B 164 ? 0.6787 0.5343 0.6199 -0.0459 -0.0114 0.0117 164 TYR B CG 8464 C CD1 . TYR B 164 ? 0.6435 0.5266 0.5966 -0.0375 0.0171 0.0021 164 TYR B CD1 8465 C CD2 . TYR B 164 ? 0.6938 0.5153 0.5810 -0.0544 -0.0187 0.0068 164 TYR B CD2 8466 C CE1 . TYR B 164 ? 0.6232 0.5015 0.5397 -0.0382 0.0341 -0.0089 164 TYR B CE1 8467 C CE2 . TYR B 164 ? 0.7618 0.5789 0.6167 -0.0531 0.0015 -0.0055 164 TYR B CE2 8468 C CZ . TYR B 164 ? 0.6855 0.5316 0.5568 -0.0452 0.0261 -0.0118 164 TYR B CZ 8469 O OH . TYR B 164 ? 0.7637 0.6056 0.6066 -0.0454 0.0428 -0.0211 164 TYR B OH 8470 N N . MET B 165 ? 0.7422 0.6432 0.8470 -0.0539 -0.0747 0.0657 165 MET B N 8471 C CA . MET B 165 ? 0.8298 0.7449 0.9976 -0.0539 -0.0949 0.0848 165 MET B CA 8472 C C . MET B 165 ? 0.8184 0.7431 1.0125 -0.0647 -0.1154 0.1006 165 MET B C 8473 O O . MET B 165 ? 0.8787 0.8015 1.0451 -0.0710 -0.1109 0.0955 165 MET B O 8474 C CB . MET B 165 ? 0.8990 0.8524 1.1283 -0.0382 -0.0677 0.0820 165 MET B CB 8475 C CG . MET B 165 ? 1.0220 1.0183 1.3069 -0.0356 -0.0527 0.0881 165 MET B CG 8476 S SD . MET B 165 ? 1.2660 1.2965 1.6461 -0.0223 -0.0432 0.0975 165 MET B SD 8477 C CE . MET B 165 ? 0.7980 0.8626 1.1820 -0.0099 0.0095 0.0746 165 MET B CE 8478 N N . TYR B 166 ? 0.8239 0.7595 1.0765 -0.0670 -0.1384 0.1210 166 TYR B N 8479 C CA . TYR B 166 ? 0.8302 0.7773 1.1180 -0.0777 -0.1605 0.1390 166 TYR B CA 8480 C C . TYR B 166 ? 0.9003 0.8993 1.2601 -0.0683 -0.1357 0.1443 166 TYR B C 8481 O O . TYR B 166 ? 0.8525 0.8781 1.2777 -0.0581 -0.1274 0.1518 166 TYR B O 8482 C CB . TYR B 166 ? 0.8097 0.7396 1.1231 -0.0883 -0.2034 0.1616 166 TYR B CB 8483 C CG . TYR B 166 ? 0.8333 0.7100 1.0693 -0.1048 -0.2339 0.1599 166 TYR B CG 8484 C CD1 . TYR B 166 ? 0.7917 0.6456 1.0016 -0.1235 -0.2638 0.1675 166 TYR B CD1 8485 C CD2 . TYR B 166 ? 0.9079 0.7562 1.0954 -0.1027 -0.2320 0.1500 166 TYR B CD2 8486 C CE1 . TYR B 166 ? 0.7983 0.6014 0.9320 -0.1401 -0.2890 0.1634 166 TYR B CE1 8487 C CE2 . TYR B 166 ? 0.9074 0.7073 1.0203 -0.1191 -0.2570 0.1480 166 TYR B CE2 8488 C CZ . TYR B 166 ? 0.8120 0.5890 0.8965 -0.1380 -0.2845 0.1537 166 TYR B CZ 8489 O OH . TYR B 166 ? 0.8596 0.5863 0.8647 -0.1558 -0.3068 0.1492 166 TYR B OH 8490 N N . ILE B 167 ? 1.0225 1.0353 1.3707 -0.0723 -0.1229 0.1404 167 ILE B N 8491 C CA . ILE B 167 ? 0.9525 1.0137 1.3619 -0.0677 -0.1013 0.1477 167 ILE B CA 8492 C C . ILE B 167 ? 1.1633 1.2325 1.6175 -0.0802 -0.1319 0.1720 167 ILE B C 8493 O O . ILE B 167 ? 1.2712 1.3785 1.7753 -0.0802 -0.1196 0.1821 167 ILE B O 8494 C CB . ILE B 167 ? 0.9356 1.0105 1.3100 -0.0665 -0.0703 0.1329 167 ILE B CB 8495 C CG1 . ILE B 167 ? 1.1170 1.1526 1.4205 -0.0775 -0.0859 0.1253 167 ILE B CG1 8496 C CG2 . ILE B 167 ? 0.9478 1.0333 1.3072 -0.0528 -0.0338 0.1130 167 ILE B CG2 8497 C CD1 . ILE B 167 ? 1.2365 1.2818 1.5057 -0.0763 -0.0582 0.1121 167 ILE B CD1 8498 N N . SER B 168 ? 1.2890 1.3208 1.7219 -0.0923 -0.1725 0.1815 168 SER B N 8499 C CA . SER B 168 ? 1.1644 1.1933 1.6293 -0.1077 -0.2097 0.2045 168 SER B CA 8500 C C . SER B 168 ? 0.9881 1.0599 1.5543 -0.1023 -0.2117 0.2274 168 SER B C 8501 O O . SER B 168 ? 1.1344 1.2361 1.7400 -0.0859 -0.1801 0.2219 168 SER B O 8502 C CB . SER B 168 ? 1.2704 1.2459 1.6816 -0.1225 -0.2512 0.2070 168 SER B CB 8503 O OG . SER B 168 ? 1.3499 1.3205 1.7861 -0.1185 -0.2652 0.2162 168 SER B OG 8504 N N . PRO B 169 ? 0.9205 0.9953 1.5315 -0.1160 -0.2474 0.2527 169 PRO B N 8505 C CA . PRO B 169 ? 0.8976 1.0185 1.6138 -0.1103 -0.2454 0.2759 169 PRO B CA 8506 C C . PRO B 169 ? 0.8530 0.9892 1.6181 -0.0938 -0.2307 0.2761 169 PRO B C 8507 O O . PRO B 169 ? 0.8644 0.9667 1.5937 -0.0938 -0.2473 0.2715 169 PRO B O 8508 C CB . PRO B 169 ? 1.0068 1.1101 1.7469 -0.1305 -0.2995 0.3031 169 PRO B CB 8509 C CG . PRO B 169 ? 1.1384 1.1860 1.7783 -0.1471 -0.3252 0.2903 169 PRO B CG 8510 C CD . PRO B 169 ? 1.1491 1.1929 1.7248 -0.1369 -0.2845 0.2606 169 PRO B CD 8511 N N . PRO B 170 ? 0.9445 1.0801 1.6207 -0.3384 0.1759 -0.0619 170 PRO B N 8512 C CA . PRO B 170 ? 1.0643 1.2282 1.8023 -0.3065 0.1885 -0.0664 170 PRO B CA 8513 C C . PRO B 170 ? 1.0979 1.2885 1.8946 -0.2950 0.1468 -0.0534 170 PRO B C 8514 O O . PRO B 170 ? 1.0284 1.2155 1.8359 -0.2665 0.1502 -0.0575 170 PRO B O 8515 C CB . PRO B 170 ? 1.1145 1.3260 1.9324 -0.3090 0.2252 -0.0700 170 PRO B CB 8516 C CG . PRO B 170 ? 1.0478 1.2333 1.8065 -0.3334 0.2491 -0.0755 170 PRO B CG 8517 C CD . PRO B 170 ? 0.9460 1.0974 1.6399 -0.3578 0.2093 -0.0664 170 PRO B CD 8518 N N . GLU B 171 ? 1.1608 1.3746 1.9918 -0.3174 0.1071 -0.0376 171 GLU B N 8519 C CA . GLU B 171 ? 1.1253 1.3634 2.0099 -0.3075 0.0644 -0.0229 171 GLU B CA 8520 C C . GLU B 171 ? 1.0371 1.2215 1.8390 -0.2958 0.0407 -0.0219 171 GLU B C 8521 O O . GLU B 171 ? 1.1439 1.3376 1.9768 -0.2800 0.0122 -0.0122 171 GLU B O 8522 C CB . GLU B 171 ? 1.2132 1.4853 2.1469 -0.3380 0.0235 -0.0051 171 GLU B CB 8523 C CG . GLU B 171 ? 1.4239 1.6448 2.2655 -0.3636 -0.0144 0.0013 171 GLU B CG 8524 C CD . GLU B 171 ? 1.7061 1.8802 2.4579 -0.3841 0.0118 -0.0102 171 GLU B CD 8525 O OE1 . GLU B 171 ? 1.6925 1.8873 2.4718 -0.3903 0.0495 -0.0185 171 GLU B OE1 8526 O OE2 . GLU B 171 ? 1.9184 2.0328 2.5714 -0.3929 -0.0035 -0.0099 171 GLU B OE2 8527 N N . ALA B 172 ? 0.9932 1.1219 1.6925 -0.3029 0.0538 -0.0303 172 ALA B N 8528 C CA . ALA B 172 ? 1.0156 1.0931 1.6361 -0.2914 0.0379 -0.0285 172 ALA B CA 8529 C C . ALA B 172 ? 0.9509 1.0153 1.5603 -0.2609 0.0659 -0.0404 172 ALA B C 8530 O O . ALA B 172 ? 0.9374 0.9692 1.5020 -0.2472 0.0533 -0.0377 172 ALA B O 8531 C CB . ALA B 172 ? 1.0303 1.0541 1.5493 -0.3120 0.0383 -0.0290 172 ALA B CB 8532 N N . LEU B 173 ? 0.9118 0.9991 1.5594 -0.2515 0.1042 -0.0534 173 LEU B N 8533 C CA . LEU B 173 ? 0.8988 0.9726 1.5388 -0.2242 0.1297 -0.0658 173 LEU B CA 8534 C C . LEU B 173 ? 0.9757 1.0730 1.6827 -0.2019 0.1108 -0.0598 173 LEU B C 8535 O O . LEU B 173 ? 1.0009 1.0705 1.6782 -0.1849 0.1020 -0.0603 173 LEU B O 8536 C CB . LEU B 173 ? 0.9329 1.0191 1.5898 -0.2208 0.1771 -0.0814 173 LEU B CB 8537 C CG . LEU B 173 ? 1.0815 1.1354 1.6614 -0.2373 0.2022 -0.0893 173 LEU B CG 8538 C CD1 . LEU B 173 ? 1.1802 1.2494 1.7845 -0.2345 0.2487 -0.1029 173 LEU B CD1 8539 C CD2 . LEU B 173 ? 1.0820 1.0835 1.5719 -0.2287 0.2011 -0.0928 173 LEU B CD2 8540 N N . GLU B 174 ? 1.0193 1.1685 1.8198 -0.2022 0.1046 -0.0524 174 GLU B N 8541 C CA . GLU B 174 ? 0.9683 1.1440 1.8416 -0.1807 0.0856 -0.0436 174 GLU B CA 8542 C C . GLU B 174 ? 0.8234 0.9876 1.6790 -0.1873 0.0341 -0.0255 174 GLU B C 8543 O O . GLU B 174 ? 0.8072 0.9634 1.6748 -0.1675 0.0166 -0.0197 174 GLU B O 8544 C CB . GLU B 174 ? 1.0181 1.2571 2.0032 -0.1786 0.0953 -0.0380 174 GLU B CB 8545 C CG . GLU B 174 ? 1.1204 1.3902 2.1898 -0.1536 0.0781 -0.0268 174 GLU B CG 8546 C CD . GLU B 174 ? 1.1986 1.4389 2.2538 -0.1219 0.1042 -0.0408 174 GLU B CD 8547 O OE1 . GLU B 174 ? 1.1809 1.3970 2.1959 -0.1171 0.1464 -0.0603 174 GLU B OE1 8548 O OE2 . GLU B 174 ? 1.2291 1.4669 2.3096 -0.1029 0.0815 -0.0321 174 GLU B OE2 8549 N N . ASN B 175 ? 0.7972 0.9555 1.6190 -0.2158 0.0111 -0.0167 175 ASN B N 8550 C CA . ASN B 175 ? 0.7937 0.9340 1.5865 -0.2256 -0.0369 0.0003 175 ASN B CA 8551 C C . ASN B 175 ? 0.7959 0.8828 1.4812 -0.2468 -0.0419 -0.0006 175 ASN B C 8552 O O . ASN B 175 ? 0.7739 0.8616 1.4439 -0.2745 -0.0525 0.0034 175 ASN B O 8553 C CB . ASN B 175 ? 0.8523 1.0420 1.7246 -0.2405 -0.0714 0.0175 175 ASN B CB 8554 C CG . ASN B 175 ? 1.0138 1.1809 1.8511 -0.2517 -0.1237 0.0356 175 ASN B CG 8555 O OD1 . ASN B 175 ? 0.9116 1.0357 1.6901 -0.2390 -0.1337 0.0377 175 ASN B OD1 8556 N ND2 . ASN B 175 ? 1.2531 1.4473 2.1247 -0.2770 -0.1577 0.0496 175 ASN B ND2 8557 N N . PRO B 176 ? 0.7907 0.8297 1.4026 -0.2339 -0.0343 -0.0047 176 PRO B N 8558 C CA . PRO B 176 ? 0.7917 0.7764 1.3008 -0.2474 -0.0330 -0.0044 176 PRO B CA 8559 C C . PRO B 176 ? 0.8061 0.7722 1.2806 -0.2711 -0.0704 0.0103 176 PRO B C 8560 O O . PRO B 176 ? 0.8453 0.7697 1.2409 -0.2878 -0.0658 0.0099 176 PRO B O 8561 C CB . PRO B 176 ? 0.7682 0.7196 1.2377 -0.2246 -0.0304 -0.0038 176 PRO B CB 8562 C CG . PRO B 176 ? 0.7613 0.7428 1.2958 -0.2019 -0.0108 -0.0141 176 PRO B CG 8563 C CD . PRO B 176 ? 0.8654 0.9001 1.4935 -0.2042 -0.0238 -0.0094 176 PRO B CD 8564 N N . CYS B 177 ? 0.7648 0.7580 1.2946 -0.2722 -0.1073 0.0236 177 CYS B N 8565 C CA . CYS B 177 ? 0.8035 0.7808 1.3040 -0.2981 -0.1466 0.0373 177 CYS B CA 8566 C C . CYS B 177 ? 1.1334 1.1602 1.7039 -0.3212 -0.1561 0.0389 177 CYS B C 8567 O O . CYS B 177 ? 1.1800 1.2630 1.8485 -0.3141 -0.1696 0.0456 177 CYS B O 8568 C CB . CYS B 177 ? 0.8170 0.7869 1.3242 -0.2879 -0.1875 0.0544 177 CYS B CB 8569 S SG . CYS B 177 ? 1.1608 1.0802 1.6033 -0.2597 -0.1765 0.0555 177 CYS B SG 8570 N N . TYR B 178 ? 1.1115 1.1168 1.6327 -0.3486 -0.1474 0.0336 178 TYR B N 8571 C CA . TYR B 178 ? 1.0822 1.1236 1.6531 -0.3787 -0.1623 0.0376 178 TYR B CA 8572 C C . TYR B 178 ? 1.2950 1.2812 1.7771 -0.4090 -0.1952 0.0454 178 TYR B C 8573 O O . TYR B 178 ? 1.5998 1.5975 2.1041 -0.4285 -0.2412 0.0596 178 TYR B O 8574 C CB . TYR B 178 ? 1.0663 1.1283 1.6581 -0.3857 -0.1173 0.0228 178 TYR B CB 8575 C CG . TYR B 178 ? 1.2807 1.3918 1.9454 -0.4151 -0.1302 0.0286 178 TYR B CG 8576 C CD1 . TYR B 178 ? 1.3760 1.5582 2.1603 -0.4093 -0.1487 0.0398 178 TYR B CD1 8577 C CD2 . TYR B 178 ? 1.3022 1.3890 1.9197 -0.4486 -0.1238 0.0244 178 TYR B CD2 8578 C CE1 . TYR B 178 ? 1.4033 1.6361 2.2635 -0.4369 -0.1612 0.0479 178 TYR B CE1 8579 C CE2 . TYR B 178 ? 1.3121 1.4452 2.0002 -0.4782 -0.1368 0.0310 178 TYR B CE2 8580 C CZ . TYR B 178 ? 1.3748 1.5834 2.1869 -0.4726 -0.1559 0.0433 178 TYR B CZ 8581 O OH . TYR B 178 ? 1.3644 1.6248 2.2557 -0.5027 -0.1694 0.0525 178 TYR B OH 8582 N N . ASP B 179 ? 1.1444 1.0678 1.5232 -0.4127 -0.1703 0.0364 179 ASP B N 8583 C CA . ASP B 179 ? 1.2414 1.0930 1.5126 -0.4310 -0.1931 0.0427 179 ASP B CA 8584 C C . ASP B 179 ? 1.4086 1.2441 1.6669 -0.4152 -0.2275 0.0566 179 ASP B C 8585 O O . ASP B 179 ? 1.4191 1.2807 1.7231 -0.3843 -0.2189 0.0573 179 ASP B O 8586 C CB . ASP B 179 ? 1.2408 1.0311 1.4127 -0.4253 -0.1524 0.0322 179 ASP B CB 8587 C CG . ASP B 179 ? 1.5537 1.2630 1.6098 -0.4343 -0.1683 0.0396 179 ASP B CG 8588 O OD1 . ASP B 179 ? 1.4871 1.1528 1.4773 -0.4139 -0.1421 0.0382 179 ASP B OD1 8589 O OD2 . ASP B 179 ? 1.8376 1.5256 1.8678 -0.4620 -0.2064 0.0476 179 ASP B OD2 8590 N N . MET B 180 ? 1.5334 1.3232 1.7276 -0.4379 -0.2665 0.0674 180 MET B N 8591 C CA . MET B 180 ? 1.5687 1.3356 1.7398 -0.4297 -0.3057 0.0832 180 MET B CA 8592 C C . MET B 180 ? 1.5834 1.4160 1.8593 -0.4348 -0.3500 0.0964 180 MET B C 8593 O O . MET B 180 ? 1.7181 1.5391 1.9867 -0.4298 -0.3882 0.1116 180 MET B O 8594 C CB . MET B 180 ? 1.4345 1.1846 1.5867 -0.3917 -0.2824 0.0834 180 MET B CB 8595 C CG . MET B 180 ? 1.3803 1.0700 1.4365 -0.3835 -0.2405 0.0745 180 MET B CG 8596 S SD . MET B 180 ? 1.6153 1.2962 1.6664 -0.3416 -0.2154 0.0768 180 MET B SD 8597 C CE . MET B 180 ? 1.1175 0.7587 1.1260 -0.3402 -0.2611 0.0975 180 MET B CE 8598 N N . LYS B 181 ? 1.4364 1.3378 1.8109 -0.4436 -0.3431 0.0921 181 LYS B N 8599 C CA . LYS B 181 ? 1.5166 1.4880 2.0025 -0.4508 -0.3829 0.1066 181 LYS B CA 8600 C C . LYS B 181 ? 1.4757 1.4797 2.0256 -0.4151 -0.3938 0.1170 181 LYS B C 8601 O O . LYS B 181 ? 1.5268 1.5579 2.1262 -0.4189 -0.4410 0.1356 181 LYS B O 8602 C CB . LYS B 181 ? 1.6119 1.5567 2.0572 -0.4895 -0.4404 0.1209 181 LYS B CB 8603 C CG . LYS B 181 ? 1.5939 1.5079 1.9839 -0.5295 -0.4355 0.1119 181 LYS B CG 8604 C CD . LYS B 181 ? 1.5441 1.5361 2.0461 -0.5420 -0.4195 0.1079 181 LYS B CD 8605 C CE . LYS B 181 ? 1.6078 1.5676 2.0528 -0.5813 -0.4155 0.0998 181 LYS B CE 8606 N NZ . LYS B 181 ? 1.7056 1.6291 2.0892 -0.6062 -0.4661 0.1108 181 LYS B NZ 8607 N N . THR B 182 ? 1.2771 1.2763 1.8244 -0.3813 -0.3511 0.1057 182 THR B N 8608 C CA . THR B 182 ? 1.1978 1.2205 1.7997 -0.3463 -0.3550 0.1132 182 THR B CA 8609 C C . THR B 182 ? 1.0936 1.1605 1.7680 -0.3192 -0.3063 0.0984 182 THR B C 8610 O O . THR B 182 ? 1.0969 1.1672 1.7629 -0.3264 -0.2684 0.0823 182 THR B O 8611 C CB . THR B 182 ? 1.3728 1.3266 1.8779 -0.3308 -0.3576 0.1168 182 THR B CB 8612 O OG1 . THR B 182 ? 1.5420 1.4477 1.9626 -0.3296 -0.3150 0.1008 182 THR B OG1 8613 C CG2 . THR B 182 ? 1.4341 1.3430 1.8717 -0.3533 -0.4086 0.1339 182 THR B CG2 8614 N N . THR B 183 ? 1.0158 1.1124 1.7576 -0.2885 -0.3073 0.1039 183 THR B N 8615 C CA . THR B 183 ? 0.9521 1.0815 1.7548 -0.2613 -0.2615 0.0893 183 THR B CA 8616 C C . THR B 183 ? 0.9222 1.0166 1.6905 -0.2305 -0.2468 0.0856 183 THR B C 8617 O O . THR B 183 ? 0.9663 1.0520 1.7409 -0.2177 -0.2768 0.1006 183 THR B O 8618 C CB . THR B 183 ? 0.9300 1.1360 1.8666 -0.2507 -0.2676 0.0978 183 THR B CB 8619 O OG1 . THR B 183 ? 1.1050 1.3206 2.0786 -0.2370 -0.3090 0.1183 183 THR B OG1 8620 C CG2 . THR B 183 ? 0.9329 1.1807 1.9155 -0.2828 -0.2809 0.1029 183 THR B CG2 8621 N N . CYS B 184 ? 0.9311 1.0047 1.6626 -0.2198 -0.2020 0.0667 184 CYS B N 8622 C CA . CYS B 184 ? 0.8721 0.9155 1.5763 -0.1930 -0.1857 0.0620 184 CYS B CA 8623 C C . CYS B 184 ? 0.7809 0.8459 1.5284 -0.1734 -0.1409 0.0432 184 CYS B C 8624 O O . CYS B 184 ? 0.8534 0.9581 1.6552 -0.1785 -0.1211 0.0351 184 CYS B O 8625 C CB . CYS B 184 ? 0.8918 0.8710 1.4827 -0.2005 -0.1805 0.0604 184 CYS B CB 8626 S SG . CYS B 184 ? 1.1343 1.0937 1.6609 -0.2210 -0.1442 0.0435 184 CYS B SG 8627 N N . LEU B 185 ? 0.7473 0.7831 1.4679 -0.1523 -0.1248 0.0368 185 LEU B N 8628 C CA . LEU B 185 ? 0.7437 0.7903 1.4968 -0.1328 -0.0856 0.0189 185 LEU B CA 8629 C C . LEU B 185 ? 0.7333 0.7562 1.4233 -0.1420 -0.0498 0.0011 185 LEU B C 8630 O O . LEU B 185 ? 0.9730 0.9604 1.5853 -0.1563 -0.0543 0.0039 185 LEU B O 8631 C CB . LEU B 185 ? 0.7690 0.7929 1.5242 -0.1075 -0.0882 0.0205 185 LEU B CB 8632 C CG . LEU B 185 ? 0.8067 0.8600 1.6469 -0.0873 -0.1065 0.0318 185 LEU B CG 8633 C CD1 . LEU B 185 ? 0.9135 1.0136 1.8389 -0.0767 -0.0796 0.0219 185 LEU B CD1 8634 C CD2 . LEU B 185 ? 0.8390 0.9042 1.6935 -0.0979 -0.1538 0.0558 185 LEU B CD2 8635 N N . PRO B 186 ? 0.7275 0.7678 1.4492 -0.1330 -0.0129 -0.0161 186 PRO B N 8636 C CA . PRO B 186 ? 0.7215 0.7374 1.3832 -0.1391 0.0215 -0.0329 186 PRO B CA 8637 C C . PRO B 186 ? 0.7262 0.6963 1.3244 -0.1288 0.0254 -0.0364 186 PRO B C 8638 O O . PRO B 186 ? 0.8082 0.7715 1.4290 -0.1098 0.0212 -0.0365 186 PRO B O 8639 C CB . PRO B 186 ? 0.7392 0.7839 1.4582 -0.1283 0.0572 -0.0484 186 PRO B CB 8640 C CG . PRO B 186 ? 0.8038 0.8739 1.6022 -0.1071 0.0455 -0.0418 186 PRO B CG 8641 C CD . PRO B 186 ? 0.7835 0.8663 1.5989 -0.1162 -0.0002 -0.0196 186 PRO B CD 8642 N N . MET B 187 ? 0.7232 0.6627 1.2455 -0.1415 0.0333 -0.0380 187 MET B N 8643 C CA . MET B 187 ? 0.7377 0.6377 1.2025 -0.1346 0.0335 -0.0367 187 MET B CA 8644 C C . MET B 187 ? 0.7511 0.6406 1.2115 -0.1224 0.0610 -0.0541 187 MET B C 8645 O O . MET B 187 ? 0.6948 0.6000 1.1776 -0.1212 0.0870 -0.0692 187 MET B O 8646 C CB . MET B 187 ? 0.8669 0.7388 1.2558 -0.1504 0.0337 -0.0297 187 MET B CB 8647 C CG . MET B 187 ? 0.8864 0.7574 1.2453 -0.1615 0.0631 -0.0420 187 MET B CG 8648 S SD . MET B 187 ? 0.8383 0.6667 1.1049 -0.1707 0.0667 -0.0323 187 MET B SD 8649 C CE . MET B 187 ? 0.6704 0.4795 0.9201 -0.1543 0.0745 -0.0357 187 MET B CE 8650 N N . PHE B 188 ? 0.7574 0.6176 1.1866 -0.1143 0.0546 -0.0511 188 PHE B N 8651 C CA . PHE B 188 ? 0.7598 0.6027 1.1794 -0.1044 0.0734 -0.0662 188 PHE B CA 8652 C C . PHE B 188 ? 0.7586 0.5683 1.1210 -0.1067 0.0664 -0.0589 188 PHE B C 8653 O O . PHE B 188 ? 0.7519 0.5528 1.0863 -0.1132 0.0502 -0.0415 188 PHE B O 8654 C CB . PHE B 188 ? 0.7712 0.6208 1.2487 -0.0862 0.0698 -0.0710 188 PHE B CB 8655 C CG . PHE B 188 ? 0.7549 0.6094 1.2619 -0.0803 0.0379 -0.0521 188 PHE B CG 8656 C CD1 . PHE B 188 ? 0.7172 0.5432 1.1966 -0.0770 0.0202 -0.0410 188 PHE B CD1 8657 C CD2 . PHE B 188 ? 0.9545 0.8421 1.5171 -0.0791 0.0247 -0.0439 188 PHE B CD2 8658 C CE1 . PHE B 188 ? 0.7067 0.5331 1.2077 -0.0715 -0.0079 -0.0228 188 PHE B CE1 8659 C CE2 . PHE B 188 ? 0.9801 0.8693 1.5646 -0.0740 -0.0069 -0.0253 188 PHE B CE2 8660 C CZ . PHE B 188 ? 0.7682 0.6246 1.3189 -0.0697 -0.0222 -0.0152 188 PHE B CZ 8661 N N . GLY B 189 ? 0.7817 0.5718 1.1275 -0.1016 0.0786 -0.0713 189 GLY B N 8662 C CA . GLY B 189 ? 0.7678 0.5306 1.0711 -0.1040 0.0697 -0.0631 189 GLY B CA 8663 C C . GLY B 189 ? 0.7864 0.5392 1.1172 -0.0937 0.0488 -0.0545 189 GLY B C 8664 O O . GLY B 189 ? 0.8868 0.6535 1.2556 -0.0876 0.0347 -0.0458 189 GLY B O 8665 N N . TYR B 190 ? 0.8742 0.6020 1.1854 -0.0929 0.0447 -0.0551 190 TYR B N 8666 C CA . TYR B 190 ? 0.7675 0.4818 1.1066 -0.0831 0.0280 -0.0498 190 TYR B CA 8667 C C . TYR B 190 ? 0.7649 0.4832 1.1491 -0.0696 0.0375 -0.0673 190 TYR B C 8668 O O . TYR B 190 ? 0.7792 0.4930 1.1574 -0.0686 0.0596 -0.0880 190 TYR B O 8669 C CB . TYR B 190 ? 0.7509 0.4365 1.0612 -0.0879 0.0217 -0.0479 190 TYR B CB 8670 C CG . TYR B 190 ? 0.7505 0.4158 1.0886 -0.0784 0.0100 -0.0491 190 TYR B CG 8671 C CD1 . TYR B 190 ? 0.8071 0.4746 1.1729 -0.0713 -0.0087 -0.0307 190 TYR B CD1 8672 C CD2 . TYR B 190 ? 0.7865 0.4253 1.1182 -0.0769 0.0179 -0.0688 190 TYR B CD2 8673 C CE1 . TYR B 190 ? 0.9118 0.5580 1.3023 -0.0621 -0.0187 -0.0309 190 TYR B CE1 8674 C CE2 . TYR B 190 ? 0.7985 0.4131 1.1525 -0.0684 0.0083 -0.0704 190 TYR B CE2 8675 C CZ . TYR B 190 ? 0.9035 0.5232 1.2890 -0.0607 -0.0098 -0.0509 190 TYR B CZ 8676 O OH . TYR B 190 ? 1.0812 0.6741 1.4882 -0.0518 -0.0187 -0.0514 190 TYR B OH 8677 N N . LYS B 191 ? 0.8202 0.5450 1.2483 -0.0582 0.0223 -0.0577 191 LYS B N 8678 C CA . LYS B 191 ? 0.9732 0.7027 1.4518 -0.0420 0.0312 -0.0704 191 LYS B CA 8679 C C . LYS B 191 ? 1.0336 0.7395 1.5337 -0.0301 0.0148 -0.0633 191 LYS B C 8680 O O . LYS B 191 ? 1.0558 0.7663 1.5700 -0.0279 -0.0083 -0.0426 191 LYS B O 8681 C CB . LYS B 191 ? 0.8884 0.6584 1.4147 -0.0376 0.0301 -0.0648 191 LYS B CB 8682 C CG . LYS B 191 ? 0.8465 0.6282 1.4367 -0.0181 0.0396 -0.0732 191 LYS B CG 8683 C CD . LYS B 191 ? 0.8560 0.6834 1.5013 -0.0158 0.0318 -0.0623 191 LYS B CD 8684 C CE . LYS B 191 ? 0.9106 0.7631 1.5431 -0.0305 0.0491 -0.0695 191 LYS B CE 8685 N NZ . LYS B 191 ? 0.9738 0.8722 1.6653 -0.0308 0.0405 -0.0591 191 LYS B NZ 8686 N N . HIS B 192 ? 0.9155 0.5912 1.4130 -0.0229 0.0275 -0.0807 192 HIS B N 8687 C CA . HIS B 192 ? 0.8633 0.5112 1.3814 -0.0109 0.0151 -0.0764 192 HIS B CA 8688 C C . HIS B 192 ? 0.9201 0.5887 1.5044 0.0099 0.0153 -0.0729 192 HIS B C 8689 O O . HIS B 192 ? 0.9113 0.5984 1.5250 0.0193 0.0375 -0.0867 192 HIS B O 8690 C CB . HIS B 192 ? 0.9003 0.5024 1.3888 -0.0113 0.0288 -0.0975 192 HIS B CB 8691 C CG . HIS B 192 ? 1.0287 0.5962 1.5366 0.0007 0.0189 -0.0953 192 HIS B CG 8692 N ND1 . HIS B 192 ? 1.0389 0.6003 1.5538 -0.0011 -0.0077 -0.0722 192 HIS B ND1 8693 C CD2 . HIS B 192 ? 1.1834 0.7161 1.7024 0.0150 0.0340 -0.1129 192 HIS B CD2 8694 C CE1 . HIS B 192 ? 1.1604 0.6863 1.6916 0.0109 -0.0101 -0.0754 192 HIS B CE1 8695 N NE2 . HIS B 192 ? 1.2511 0.7578 1.7844 0.0211 0.0150 -0.1003 192 HIS B NE2 8696 N N . VAL B 193 ? 1.0176 0.6840 1.6271 0.0176 -0.0090 -0.0528 193 VAL B N 8697 C CA . VAL B 193 ? 1.0434 0.7320 1.7188 0.0377 -0.0144 -0.0445 193 VAL B CA 8698 C C . VAL B 193 ? 1.0693 0.7212 1.7667 0.0559 -0.0159 -0.0456 193 VAL B C 8699 O O . VAL B 193 ? 1.2706 0.9171 2.0027 0.0742 0.0051 -0.0599 193 VAL B O 8700 C CB . VAL B 193 ? 0.7946 0.5118 1.4844 0.0336 -0.0442 -0.0173 193 VAL B CB 8701 C CG1 . VAL B 193 ? 0.8246 0.5730 1.5871 0.0526 -0.0515 -0.0081 193 VAL B CG1 8702 C CG2 . VAL B 193 ? 0.7647 0.5071 1.4208 0.0134 -0.0435 -0.0156 193 VAL B CG2 8703 N N . LEU B 194 ? 0.9391 0.5634 1.6158 0.0515 -0.0384 -0.0299 194 LEU B N 8704 C CA . LEU B 194 ? 0.9357 0.5215 1.6311 0.0674 -0.0426 -0.0280 194 LEU B CA 8705 C C . LEU B 194 ? 0.9248 0.4593 1.5681 0.0537 -0.0433 -0.0350 194 LEU B C 8706 O O . LEU B 194 ? 0.9083 0.4380 1.5185 0.0367 -0.0607 -0.0198 194 LEU B O 8707 C CB . LEU B 194 ? 0.9472 0.5437 1.6752 0.0769 -0.0715 0.0010 194 LEU B CB 8708 C CG . LEU B 194 ? 1.0730 0.6312 1.8262 0.0960 -0.0772 0.0069 194 LEU B CG 8709 C CD1 . LEU B 194 ? 1.1273 0.6859 1.9304 0.1210 -0.0536 -0.0091 194 LEU B CD1 8710 C CD2 . LEU B 194 ? 1.0644 0.6315 1.8381 0.1020 -0.1085 0.0383 194 LEU B CD2 8711 N N . THR B 195 ? 0.9682 0.4632 1.6045 0.0608 -0.0237 -0.0575 195 THR B N 8712 C CA . THR B 195 ? 1.0369 0.4779 1.6270 0.0470 -0.0268 -0.0652 195 THR B CA 8713 C C . THR B 195 ? 1.1420 0.5588 1.7456 0.0511 -0.0502 -0.0428 195 THR B C 8714 O O . THR B 195 ? 1.1493 0.5783 1.7994 0.0714 -0.0574 -0.0286 195 THR B O 8715 C CB . THR B 195 ? 1.0586 0.4541 1.6341 0.0549 -0.0002 -0.0955 195 THR B CB 8716 O OG1 . THR B 195 ? 1.0500 0.4715 1.6243 0.0576 0.0256 -0.1140 195 THR B OG1 8717 C CG2 . THR B 195 ? 1.0940 0.4367 1.6099 0.0325 -0.0055 -0.1063 195 THR B CG2 8718 N N . LEU B 196 ? 1.1397 0.5239 1.7048 0.0315 -0.0629 -0.0377 196 LEU B N 8719 C CA . LEU B 196 ? 1.0601 0.4256 1.6275 0.0321 -0.0826 -0.0150 196 LEU B CA 8720 C C . LEU B 196 ? 1.1104 0.4458 1.6987 0.0545 -0.0755 -0.0206 196 LEU B C 8721 O O . LEU B 196 ? 1.1685 0.4645 1.7376 0.0564 -0.0587 -0.0443 196 LEU B O 8722 C CB . LEU B 196 ? 1.0530 0.3966 1.5700 0.0056 -0.0916 -0.0113 196 LEU B CB 8723 C CG . LEU B 196 ? 1.0081 0.3808 1.5024 -0.0163 -0.0988 -0.0007 196 LEU B CG 8724 C CD1 . LEU B 196 ? 1.0266 0.3787 1.4807 -0.0404 -0.1068 0.0034 196 LEU B CD1 8725 C CD2 . LEU B 196 ? 0.9670 0.3765 1.4785 -0.0117 -0.1115 0.0280 196 LEU B CD2 8726 N N . THR B 197 ? 1.1049 0.4560 1.7276 0.0712 -0.0884 0.0017 197 THR B N 8727 C CA . THR B 197 ? 1.2804 0.6070 1.9272 0.0949 -0.0826 0.0008 197 THR B CA 8728 C C . THR B 197 ? 1.2957 0.6191 1.9441 0.0980 -0.1038 0.0292 197 THR B C 8729 O O . THR B 197 ? 1.1313 0.4723 1.7617 0.0826 -0.1212 0.0495 197 THR B O 8730 C CB . THR B 197 ? 1.4625 0.8183 2.1701 0.1228 -0.0702 -0.0038 197 THR B CB 8731 O OG1 . THR B 197 ? 1.4999 0.9063 2.2408 0.1244 -0.0889 0.0183 197 THR B OG1 8732 C CG2 . THR B 197 ? 1.5876 0.9396 2.2934 0.1237 -0.0416 -0.0346 197 THR B CG2 8733 N N . ASP B 198 ? 1.4621 0.7607 2.1290 0.1190 -0.0996 0.0306 198 ASP B N 8734 C CA . ASP B 198 ? 1.3578 0.6480 2.0255 0.1244 -0.1171 0.0562 198 ASP B CA 8735 C C . ASP B 198 ? 1.3714 0.7066 2.0828 0.1404 -0.1341 0.0804 198 ASP B C 8736 O O . ASP B 198 ? 1.2619 0.6060 1.9597 0.1335 -0.1539 0.1049 198 ASP B O 8737 C CB . ASP B 198 ? 1.3448 0.5847 2.0103 0.1404 -0.1053 0.0482 198 ASP B CB 8738 C CG . ASP B 198 ? 1.4696 0.6598 2.0928 0.1275 -0.0867 0.0196 198 ASP B CG 8739 O OD1 . ASP B 198 ? 1.4702 0.6627 2.0595 0.1013 -0.0888 0.0115 198 ASP B OD1 8740 O OD2 . ASP B 198 ? 1.5974 0.7442 2.2185 0.1435 -0.0703 0.0057 198 ASP B OD2 8741 N N . GLN B 199 ? 1.4873 0.8501 2.2500 0.1611 -0.1260 0.0738 199 GLN B N 8742 C CA . GLN B 199 ? 1.4768 0.8806 2.2883 0.1782 -0.1441 0.0969 199 GLN B CA 8743 C C . GLN B 199 ? 1.2868 0.7292 2.0913 0.1619 -0.1653 0.1128 199 GLN B C 8744 O O . GLN B 199 ? 1.1221 0.5836 1.9246 0.1504 -0.1581 0.1003 199 GLN B O 8745 C CB . GLN B 199 ? 1.5019 0.9303 2.3773 0.2041 -0.1278 0.0862 199 GLN B CB 8746 C CG . GLN B 199 ? 1.4999 0.8862 2.3755 0.2204 -0.0985 0.0645 199 GLN B CG 8747 C CD . GLN B 199 ? 1.5081 0.8747 2.3553 0.2088 -0.0712 0.0320 199 GLN B CD 8748 O OE1 . GLN B 199 ? 1.4125 0.7982 2.2415 0.1881 -0.0745 0.0262 199 GLN B OE1 8749 N NE2 . GLN B 199 ? 1.5911 0.9155 2.4292 0.2220 -0.0436 0.0108 199 GLN B NE2 8750 N N . VAL B 200 ? 1.3152 0.7642 2.1106 0.1610 -0.1902 0.1404 200 VAL B N 8751 C CA . VAL B 200 ? 1.2961 0.7756 2.0797 0.1479 -0.2115 0.1579 200 VAL B CA 8752 C C . VAL B 200 ? 1.2545 0.7787 2.0988 0.1631 -0.2243 0.1656 200 VAL B C 8753 O O . VAL B 200 ? 1.2670 0.8184 2.1103 0.1522 -0.2370 0.1718 200 VAL B O 8754 C CB . VAL B 200 ? 1.2839 0.7478 2.0249 0.1402 -0.2314 0.1840 200 VAL B CB 8755 C CG1 . VAL B 200 ? 1.1379 0.5661 1.8236 0.1223 -0.2187 0.1789 200 VAL B CG1 8756 C CG2 . VAL B 200 ? 1.4412 0.8989 2.2106 0.1621 -0.2434 0.2000 200 VAL B CG2 8757 N N . THR B 201 ? 1.1585 0.6900 2.0563 0.1880 -0.2209 0.1662 201 THR B N 8758 C CA . THR B 201 ? 1.1982 0.7787 2.1649 0.2038 -0.2325 0.1752 201 THR B CA 8759 C C . THR B 201 ? 1.2859 0.8933 2.2862 0.2032 -0.2111 0.1527 201 THR B C 8760 O O . THR B 201 ? 1.2732 0.9240 2.3081 0.2008 -0.2249 0.1602 201 THR B O 8761 C CB . THR B 201 ? 1.2254 0.8085 2.2435 0.2322 -0.2296 0.1823 201 THR B CB 8762 O OG1 . THR B 201 ? 1.2070 0.7597 2.2281 0.2437 -0.1938 0.1570 201 THR B OG1 8763 C CG2 . THR B 201 ? 1.3436 0.9008 2.3300 0.2338 -0.2519 0.2063 201 THR B CG2 8764 N N . ARG B 202 ? 1.3200 0.8989 2.3066 0.2043 -0.1777 0.1251 202 ARG B N 8765 C CA . ARG B 202 ? 1.1915 0.7856 2.1952 0.2016 -0.1519 0.1000 202 ARG B CA 8766 C C . ARG B 202 ? 1.0765 0.6899 2.0259 0.1703 -0.1602 0.0984 202 ARG B C 8767 O O . ARG B 202 ? 1.1086 0.7622 2.0651 0.1615 -0.1484 0.0861 202 ARG B O 8768 C CB . ARG B 202 ? 1.2211 0.7697 2.1956 0.2036 -0.1166 0.0705 202 ARG B CB 8769 C CG . ARG B 202 ? 1.2983 0.8546 2.2572 0.1923 -0.0875 0.0413 202 ARG B CG 8770 C CD . ARG B 202 ? 1.4136 1.0244 2.4365 0.2077 -0.0712 0.0362 202 ARG B CD 8771 N NE . ARG B 202 ? 1.5096 1.1326 2.5042 0.1927 -0.0429 0.0097 202 ARG B NE 8772 C CZ . ARG B 202 ? 1.5440 1.2150 2.5831 0.1992 -0.0242 0.0024 202 ARG B CZ 8773 N NH1 . ARG B 202 ? 1.5369 1.2525 2.6566 0.2200 -0.0322 0.0205 202 ARG B NH1 8774 N NH2 . ARG B 202 ? 1.5219 1.1971 2.5267 0.1844 0.0020 -0.0213 202 ARG B NH2 8775 N N . PHE B 203 ? 1.0329 0.6169 1.9278 0.1541 -0.1790 0.1125 203 PHE B N 8776 C CA . PHE B 203 ? 1.0715 0.6668 1.9096 0.1261 -0.1849 0.1137 203 PHE B CA 8777 C C . PHE B 203 ? 1.1333 0.7722 1.9824 0.1208 -0.2102 0.1331 203 PHE B C 8778 O O . PHE B 203 ? 1.0206 0.6961 1.8674 0.1088 -0.2033 0.1231 203 PHE B O 8779 C CB . PHE B 203 ? 1.0512 0.6001 1.8328 0.1127 -0.1937 0.1251 203 PHE B CB 8780 C CG . PHE B 203 ? 0.9775 0.5331 1.7008 0.0864 -0.1938 0.1263 203 PHE B CG 8781 C CD1 . PHE B 203 ? 0.9787 0.5267 1.6698 0.0713 -0.1714 0.1047 203 PHE B CD1 8782 C CD2 . PHE B 203 ? 0.9245 0.4904 1.6223 0.0775 -0.2160 0.1497 203 PHE B CD2 8783 C CE1 . PHE B 203 ? 1.0385 0.5936 1.6803 0.0496 -0.1703 0.1080 203 PHE B CE1 8784 C CE2 . PHE B 203 ? 0.9500 0.5178 1.5934 0.0559 -0.2124 0.1514 203 PHE B CE2 8785 C CZ . PHE B 203 ? 1.0379 0.6025 1.6567 0.0428 -0.1890 0.1313 203 PHE B CZ 8786 N N . ASN B 204 ? 1.2272 0.8577 2.0834 0.1285 -0.2402 0.1610 204 ASN B N 8787 C CA . ASN B 204 ? 1.1916 0.8543 2.0502 0.1218 -0.2702 0.1818 204 ASN B CA 8788 C C . ASN B 204 ? 1.1804 0.9008 2.1021 0.1277 -0.2692 0.1751 204 ASN B C 8789 O O . ASN B 204 ? 1.1221 0.8738 2.0315 0.1108 -0.2812 0.1785 204 ASN B O 8790 C CB . ASN B 204 ? 1.1619 0.8034 2.0275 0.1344 -0.3026 0.2126 204 ASN B CB 8791 C CG . ASN B 204 ? 1.3627 0.9534 2.1607 0.1254 -0.3012 0.2205 204 ASN B CG 8792 O OD1 . ASN B 204 ? 1.5685 1.1389 2.3649 0.1362 -0.2984 0.2246 204 ASN B OD1 8793 N ND2 . ASN B 204 ? 1.3878 0.9640 2.1240 0.1035 -0.2985 0.2212 204 ASN B ND2 8794 N N . GLU B 205 ? 1.2579 0.9902 2.2474 0.1516 -0.2533 0.1664 205 GLU B N 8795 C CA . GLU B 205 ? 1.3100 1.0994 2.3713 0.1603 -0.2472 0.1614 205 GLU B CA 8796 C C . GLU B 205 ? 1.2750 1.0873 2.3142 0.1409 -0.2205 0.1362 205 GLU B C 8797 O O . GLU B 205 ? 1.3165 1.1750 2.3765 0.1295 -0.2294 0.1393 205 GLU B O 8798 C CB . GLU B 205 ? 1.3727 1.1615 2.5063 0.1927 -0.2268 0.1558 205 GLU B CB 8799 C CG . GLU B 205 ? 1.4837 1.3314 2.6985 0.2046 -0.2109 0.1493 205 GLU B CG 8800 C CD . GLU B 205 ? 1.5083 1.3539 2.7111 0.2009 -0.1642 0.1153 205 GLU B CD 8801 O OE1 . GLU B 205 ? 1.4454 1.2409 2.5825 0.1924 -0.1456 0.0966 205 GLU B OE1 8802 O OE2 . GLU B 205 ? 1.5516 1.4454 2.8105 0.2055 -0.1468 0.1084 205 GLU B OE2 8803 N N . GLU B 206 ? 1.1829 0.9610 2.1786 0.1359 -0.1894 0.1123 206 GLU B N 8804 C CA . GLU B 206 ? 1.1198 0.9131 2.0894 0.1190 -0.1622 0.0881 206 GLU B CA 8805 C C . GLU B 206 ? 0.9964 0.7918 1.9006 0.0903 -0.1775 0.0943 206 GLU B C 8806 O O . GLU B 206 ? 1.0178 0.8378 1.9083 0.0748 -0.1643 0.0818 206 GLU B O 8807 C CB . GLU B 206 ? 1.2244 0.9753 2.1618 0.1215 -0.1285 0.0624 206 GLU B CB 8808 C CG . GLU B 206 ? 1.3793 1.1438 2.2956 0.1086 -0.0972 0.0362 206 GLU B CG 8809 C CD . GLU B 206 ? 1.4734 1.2824 2.4589 0.1223 -0.0773 0.0278 206 GLU B CD 8810 O OE1 . GLU B 206 ? 1.4682 1.2825 2.5174 0.1482 -0.0741 0.0333 206 GLU B OE1 8811 O OE2 . GLU B 206 ? 1.4724 1.3109 2.4504 0.1079 -0.0633 0.0170 206 GLU B OE2 8812 N N . VAL B 207 ? 0.9541 0.7204 1.8164 0.0842 -0.2035 0.1145 207 VAL B N 8813 C CA . VAL B 207 ? 0.9353 0.6934 1.7289 0.0597 -0.2149 0.1221 207 VAL B CA 8814 C C . VAL B 207 ? 0.9723 0.7664 1.7768 0.0493 -0.2406 0.1364 207 VAL B C 8815 O O . VAL B 207 ? 0.9227 0.7257 1.6865 0.0287 -0.2374 0.1316 207 VAL B O 8816 C CB . VAL B 207 ? 0.9367 0.6467 1.6795 0.0577 -0.2297 0.1399 207 VAL B CB 8817 C CG1 . VAL B 207 ? 0.9625 0.6690 1.6628 0.0440 -0.2584 0.1631 207 VAL B CG1 8818 C CG2 . VAL B 207 ? 0.8388 0.5175 1.5313 0.0473 -0.2052 0.1256 207 VAL B CG2 8819 N N . LYS B 208 ? 1.0772 0.8908 1.9367 0.0630 -0.2669 0.1546 208 LYS B N 8820 C CA . LYS B 208 ? 0.9967 0.8428 1.8683 0.0513 -0.2982 0.1709 208 LYS B CA 8821 C C . LYS B 208 ? 0.9270 0.8232 1.8382 0.0425 -0.2824 0.1549 208 LYS B C 8822 O O . LYS B 208 ? 0.9948 0.9121 1.8930 0.0226 -0.3006 0.1613 208 LYS B O 8823 C CB . LYS B 208 ? 1.0629 0.9213 1.9923 0.0695 -0.3319 0.1958 208 LYS B CB 8824 C CG . LYS B 208 ? 1.1508 1.0311 2.0776 0.0541 -0.3743 0.2177 208 LYS B CG 8825 C CD . LYS B 208 ? 1.1062 1.0053 2.1008 0.0736 -0.4087 0.2433 208 LYS B CD 8826 C CE . LYS B 208 ? 0.9808 0.9330 2.0843 0.0951 -0.3918 0.2362 208 LYS B CE 8827 N NZ . LYS B 208 ? 0.9524 0.9286 2.1300 0.1155 -0.4264 0.2643 208 LYS B NZ 8828 N N . LYS B 209 ? 0.8809 0.7915 1.8363 0.0564 -0.2473 0.1340 209 LYS B N 8829 C CA . LYS B 209 ? 0.8770 0.8331 1.8735 0.0506 -0.2254 0.1181 209 LYS B CA 8830 C C . LYS B 209 ? 0.9645 0.9130 1.8910 0.0235 -0.2116 0.1042 209 LYS B C 8831 O O . LYS B 209 ? 1.1849 1.1701 2.1318 0.0105 -0.2048 0.0978 209 LYS B O 8832 C CB . LYS B 209 ? 0.9164 0.8765 1.9615 0.0731 -0.1860 0.0979 209 LYS B CB 8833 C CG . LYS B 209 ? 0.9662 0.9325 2.0853 0.1034 -0.1934 0.1105 209 LYS B CG 8834 C CD . LYS B 209 ? 0.9182 0.8693 2.0635 0.1255 -0.1502 0.0880 209 LYS B CD 8835 C CE . LYS B 209 ? 0.8841 0.8735 2.0642 0.1230 -0.1155 0.0688 209 LYS B CE 8836 N NZ . LYS B 209 ? 0.8511 0.8182 2.0487 0.1452 -0.0714 0.0464 209 LYS B NZ 8837 N N . GLN B 210 ? 0.8774 0.7786 1.7245 0.0153 -0.2067 0.1011 210 GLN B N 8838 C CA . GLN B 210 ? 0.8633 0.7524 1.6427 -0.0068 -0.1898 0.0887 210 GLN B CA 8839 C C . GLN B 210 ? 0.8685 0.7682 1.6174 -0.0295 -0.2141 0.1011 210 GLN B C 8840 O O . GLN B 210 ? 0.8734 0.7592 1.6037 -0.0329 -0.2476 0.1224 210 GLN B O 8841 C CB . GLN B 210 ? 0.8458 0.6844 1.5558 -0.0084 -0.1813 0.0874 210 GLN B CB 8842 C CG . GLN B 210 ? 0.9085 0.7281 1.6379 0.0096 -0.1600 0.0745 210 GLN B CG 8843 C CD . GLN B 210 ? 0.9204 0.7578 1.6729 0.0123 -0.1251 0.0483 210 GLN B CD 8844 O OE1 . GLN B 210 ? 1.0190 0.8693 1.7456 -0.0033 -0.1103 0.0375 210 GLN B OE1 8845 N NE2 . GLN B 210 ? 0.8385 0.6720 1.6359 0.0327 -0.1102 0.0382 210 GLN B NE2 8846 N N . SER B 211 ? 0.9259 0.8452 1.6647 -0.0457 -0.1966 0.0876 211 SER B N 8847 C CA . SER B 211 ? 0.9210 0.8448 1.6242 -0.0700 -0.2157 0.0960 211 SER B CA 8848 C C . SER B 211 ? 0.8707 0.7688 1.4976 -0.0866 -0.1908 0.0832 211 SER B C 8849 O O . SER B 211 ? 0.9732 0.8542 1.5793 -0.0793 -0.1623 0.0696 211 SER B O 8850 C CB . SER B 211 ? 1.0533 1.0319 1.8292 -0.0762 -0.2233 0.0960 211 SER B CB 8851 O OG . SER B 211 ? 1.1996 1.2062 2.0545 -0.0582 -0.2451 0.1099 211 SER B OG 8852 N N . VAL B 212 ? 0.8484 0.7421 1.4331 -0.1092 -0.2025 0.0881 212 VAL B N 8853 C CA . VAL B 212 ? 0.8289 0.6926 1.3358 -0.1238 -0.1807 0.0798 212 VAL B CA 8854 C C . VAL B 212 ? 0.8086 0.6993 1.3286 -0.1362 -0.1558 0.0623 212 VAL B C 8855 O O . VAL B 212 ? 0.9583 0.8883 1.5331 -0.1436 -0.1644 0.0616 212 VAL B O 8856 C CB . VAL B 212 ? 0.8723 0.6976 1.3037 -0.1408 -0.2039 0.0960 212 VAL B CB 8857 C CG1 . VAL B 212 ? 1.0435 0.8306 1.4418 -0.1287 -0.2185 0.1126 212 VAL B CG1 8858 C CG2 . VAL B 212 ? 1.1113 0.9592 1.5675 -0.1571 -0.2365 0.1050 212 VAL B CG2 8859 N N . SER B 213 ? 0.7708 0.6410 1.2423 -0.1385 -0.1249 0.0498 213 SER B N 8860 C CA . SER B 213 ? 0.7513 0.6379 1.2202 -0.1508 -0.0985 0.0340 213 SER B CA 8861 C C . SER B 213 ? 0.8755 0.7265 1.2602 -0.1696 -0.0945 0.0375 213 SER B C 8862 O O . SER B 213 ? 1.1847 1.0005 1.5176 -0.1726 -0.1123 0.0523 213 SER B O 8863 C CB . SER B 213 ? 0.7163 0.6076 1.1986 -0.1374 -0.0638 0.0158 213 SER B CB 8864 O OG . SER B 213 ? 0.7087 0.6217 1.2025 -0.1473 -0.0391 0.0012 213 SER B OG 8865 N N . ARG B 214 ? 0.7664 0.6227 1.1346 -0.1812 -0.0693 0.0248 214 ARG B N 8866 C CA . ARG B 214 ? 0.8110 0.6317 1.1006 -0.1985 -0.0636 0.0282 214 ARG B CA 8867 C C . ARG B 214 ? 0.7844 0.5957 1.0394 -0.1998 -0.0269 0.0151 214 ARG B C 8868 O O . ARG B 214 ? 0.7675 0.6074 1.0614 -0.1981 -0.0061 0.0003 214 ARG B O 8869 C CB . ARG B 214 ? 1.0942 0.9247 1.3880 -0.2217 -0.0828 0.0319 214 ARG B CB 8870 C CG . ARG B 214 ? 1.1032 0.8896 1.3108 -0.2409 -0.0772 0.0348 214 ARG B CG 8871 C CD . ARG B 214 ? 1.0152 0.8112 1.2300 -0.2673 -0.0968 0.0364 214 ARG B CD 8872 N NE . ARG B 214 ? 0.9024 0.6478 1.0282 -0.2862 -0.0911 0.0384 214 ARG B NE 8873 C CZ . ARG B 214 ? 0.9370 0.6732 1.0449 -0.3133 -0.1096 0.0407 214 ARG B CZ 8874 N NH1 . ARG B 214 ? 1.1842 0.9651 1.3637 -0.3251 -0.1372 0.0429 214 ARG B NH1 8875 N NH2 . ARG B 214 ? 1.0375 0.7190 1.0569 -0.3289 -0.1010 0.0416 214 ARG B NH2 8876 N N . ASN B 215 ? 0.8006 0.5699 0.9811 -0.2018 -0.0182 0.0222 215 ASN B N 8877 C CA . ASN B 215 ? 0.8087 0.5634 0.9459 -0.2052 0.0131 0.0143 215 ASN B CA 8878 C C . ASN B 215 ? 0.8465 0.5552 0.9038 -0.2159 0.0143 0.0262 215 ASN B C 8879 O O . ASN B 215 ? 1.0729 0.7564 1.1036 -0.2162 -0.0061 0.0403 215 ASN B O 8880 C CB . ASN B 215 ? 0.7729 0.5268 0.9123 -0.1874 0.0300 0.0105 215 ASN B CB 8881 C CG . ASN B 215 ? 0.8412 0.5623 0.9388 -0.1780 0.0240 0.0272 215 ASN B CG 8882 O OD1 . ASN B 215 ? 0.7491 0.4517 0.8074 -0.1741 0.0421 0.0308 215 ASN B OD1 8883 N ND2 . ASN B 215 ? 1.0458 0.7611 1.1551 -0.1737 -0.0012 0.0392 215 ASN B ND2 8884 N N . ARG B 216 ? 0.8506 0.5438 0.8659 -0.2243 0.0389 0.0210 216 ARG B N 8885 C CA . ARG B 216 ? 0.9081 0.5525 0.8452 -0.2341 0.0430 0.0317 216 ARG B CA 8886 C C . ARG B 216 ? 0.9620 0.5714 0.8468 -0.2192 0.0584 0.0450 216 ARG B C 8887 O O . ARG B 216 ? 1.1243 0.6887 0.9456 -0.2227 0.0605 0.0572 216 ARG B O 8888 C CB . ARG B 216 ? 1.0335 0.6716 0.9457 -0.2512 0.0624 0.0222 216 ARG B CB 8889 C CG . ARG B 216 ? 1.1329 0.7845 1.0501 -0.2434 0.0927 0.0126 216 ARG B CG 8890 C CD . ARG B 216 ? 1.3187 1.0047 1.2801 -0.2567 0.0997 -0.0034 216 ARG B CD 8891 N NE . ARG B 216 ? 1.2263 0.8998 1.1706 -0.2805 0.0897 -0.0028 216 ARG B NE 8892 C CZ . ARG B 216 ? 0.9821 0.6781 0.9541 -0.2972 0.0983 -0.0135 216 ARG B CZ 8893 N NH1 . ARG B 216 ? 0.8902 0.6193 0.9035 -0.2905 0.1202 -0.0258 216 ARG B NH1 8894 N NH2 . ARG B 216 ? 0.9860 0.6682 0.9411 -0.3218 0.0857 -0.0117 216 ARG B NH2 8895 N N . ASP B 217 ? 0.9246 0.5529 0.8353 -0.2033 0.0696 0.0433 217 ASP B N 8896 C CA . ASP B 217 ? 0.8767 0.4802 0.7485 -0.1902 0.0854 0.0574 217 ASP B CA 8897 C C . ASP B 217 ? 0.8526 0.4463 0.7299 -0.1784 0.0687 0.0731 217 ASP B C 8898 O O . ASP B 217 ? 0.8406 0.4609 0.7704 -0.1723 0.0524 0.0690 217 ASP B O 8899 C CB . ASP B 217 ? 0.9369 0.5637 0.8303 -0.1821 0.1029 0.0492 217 ASP B CB 8900 C CG . ASP B 217 ? 1.1992 0.8275 1.1031 -0.1664 0.1010 0.0613 217 ASP B CG 8901 O OD1 . ASP B 217 ? 1.1539 0.8024 1.1040 -0.1606 0.0844 0.0577 217 ASP B OD1 8902 O OD2 . ASP B 217 ? 1.4114 1.0208 1.2799 -0.1599 0.1163 0.0755 217 ASP B OD2 8903 N N . ALA B 218 ? 1.0268 0.5795 0.8488 -0.1745 0.0749 0.0915 218 ALA B N 8904 C CA . ALA B 218 ? 1.0036 0.5402 0.8231 -0.1658 0.0594 0.1078 218 ALA B CA 8905 C C . ALA B 218 ? 0.8173 0.3777 0.6820 -0.1508 0.0574 0.1135 218 ALA B C 8906 O O . ALA B 218 ? 0.9584 0.5297 0.8583 -0.1469 0.0363 0.1150 218 ALA B O 8907 C CB . ALA B 218 ? 1.0351 0.5175 0.7801 -0.1634 0.0732 0.1270 218 ALA B CB 8908 N N . PRO B 219 ? 0.7791 0.3458 0.6426 -0.1431 0.0775 0.1181 219 PRO B N 8909 C CA . PRO B 219 ? 0.8257 0.4160 0.7359 -0.1332 0.0703 0.1213 219 PRO B CA 8910 C C . PRO B 219 ? 0.7380 0.3634 0.7030 -0.1367 0.0571 0.0984 219 PRO B C 8911 O O . PRO B 219 ? 0.7186 0.3583 0.6871 -0.1438 0.0657 0.0812 219 PRO B O 8912 C CB . PRO B 219 ? 1.0720 0.6633 0.9687 -0.1273 0.0918 0.1312 219 PRO B CB 8913 C CG . PRO B 219 ? 1.1309 0.7108 0.9884 -0.1342 0.1099 0.1242 219 PRO B CG 8914 C CD . PRO B 219 ? 1.0629 0.6168 0.8876 -0.1429 0.1040 0.1218 219 PRO B CD 8915 N N . GLU B 220 ? 0.7833 0.4193 0.7887 -0.1309 0.0388 0.0991 220 GLU B N 8916 C CA . GLU B 220 ? 0.7234 0.3871 0.7806 -0.1316 0.0271 0.0789 220 GLU B CA 8917 C C . GLU B 220 ? 0.7582 0.4381 0.8426 -0.1275 0.0330 0.0685 220 GLU B C 8918 O O . GLU B 220 ? 0.8234 0.5222 0.9429 -0.1275 0.0312 0.0491 220 GLU B O 8919 C CB . GLU B 220 ? 0.7265 0.3889 0.8117 -0.1269 0.0032 0.0848 220 GLU B CB 8920 C CG . GLU B 220 ? 0.8284 0.5004 0.9275 -0.1339 -0.0107 0.0765 220 GLU B CG 8921 C CD . GLU B 220 ? 0.7458 0.4017 0.7957 -0.1464 -0.0027 0.0783 220 GLU B CD 8922 O OE1 . GLU B 220 ? 0.7635 0.3876 0.7689 -0.1485 -0.0085 0.0945 220 GLU B OE1 8923 O OE2 . GLU B 220 ? 0.7566 0.4273 0.8086 -0.1545 0.0104 0.0633 220 GLU B OE2 8924 N N . GLY B 221 ? 0.7954 0.4665 0.8621 -0.1244 0.0407 0.0822 221 GLY B N 8925 C CA . GLY B 221 ? 1.1193 0.8011 1.2039 -0.1236 0.0427 0.0743 221 GLY B CA 8926 C C . GLY B 221 ? 1.1387 0.8262 1.2668 -0.1195 0.0266 0.0653 221 GLY B C 8927 O O . GLY B 221 ? 0.7768 0.4738 0.9245 -0.1203 0.0283 0.0440 221 GLY B O 8928 N N . GLY B 222 ? 1.1694 0.8470 1.3095 -0.1143 0.0130 0.0818 222 GLY B N 8929 C CA . GLY B 222 ? 0.9504 0.6279 1.1297 -0.1095 -0.0023 0.0761 222 GLY B CA 8930 C C . GLY B 222 ? 0.8439 0.5185 1.0310 -0.1119 -0.0038 0.0759 222 GLY B C 8931 O O . GLY B 222 ? 0.8816 0.5518 1.0966 -0.1097 -0.0140 0.0664 222 GLY B O 8932 N N . PHE B 223 ? 0.8286 0.5040 0.9905 -0.1168 0.0054 0.0873 223 PHE B N 8933 C CA . PHE B 223 ? 0.6719 0.3465 0.8396 -0.1224 0.0006 0.0900 223 PHE B CA 8934 C C . PHE B 223 ? 0.6820 0.3560 0.8560 -0.1264 -0.0004 0.0611 223 PHE B C 8935 O O . PHE B 223 ? 0.8047 0.4696 0.9895 -0.1312 -0.0111 0.0572 223 PHE B O 8936 C CB . PHE B 223 ? 0.7999 0.4804 0.9415 -0.1261 0.0112 0.1077 223 PHE B CB 8937 C CG . PHE B 223 ? 0.8616 0.5382 0.9999 -0.1213 0.0142 0.1397 223 PHE B CG 8938 C CD1 . PHE B 223 ? 0.8688 0.5344 1.0216 -0.1157 0.0063 0.1505 223 PHE B CD1 8939 C CD2 . PHE B 223 ? 0.8485 0.5304 0.9685 -0.1211 0.0266 0.1605 223 PHE B CD2 8940 C CE1 . PHE B 223 ? 0.6742 0.3316 0.8189 -0.1106 0.0126 0.1803 223 PHE B CE1 8941 C CE2 . PHE B 223 ? 0.7747 0.4509 0.8918 -0.1145 0.0342 0.1909 223 PHE B CE2 8942 C CZ . PHE B 223 ? 0.6733 0.3358 0.8008 -0.1096 0.0282 0.2003 223 PHE B CZ 8943 N N . ASP B 224 ? 0.6808 0.3615 0.8457 -0.1253 0.0120 0.0413 224 ASP B N 8944 C CA . ASP B 224 ? 0.7653 0.4423 0.9343 -0.1266 0.0168 0.0130 224 ASP B CA 8945 C C . ASP B 224 ? 0.8723 0.5382 1.0755 -0.1206 0.0053 0.0035 224 ASP B C 8946 O O . ASP B 224 ? 1.0669 0.7168 1.2698 -0.1233 0.0030 -0.0120 224 ASP B O 8947 C CB . ASP B 224 ? 0.9638 0.6528 1.1264 -0.1251 0.0341 -0.0030 224 ASP B CB 8948 C CG . ASP B 224 ? 0.8921 0.5803 1.0197 -0.1324 0.0495 -0.0141 224 ASP B CG 8949 O OD1 . ASP B 224 ? 0.8311 0.5123 0.9362 -0.1386 0.0449 -0.0048 224 ASP B OD1 8950 O OD2 . ASP B 224 ? 0.7285 0.4237 0.8525 -0.1323 0.0657 -0.0307 224 ASP B OD2 8951 N N . ALA B 225 ? 0.8282 0.4984 1.0567 -0.1124 -0.0023 0.0134 225 ALA B N 8952 C CA . ALA B 225 ? 0.7096 0.3691 0.9731 -0.1042 -0.0135 0.0080 225 ALA B CA 8953 C C . ALA B 225 ? 0.7221 0.3619 0.9885 -0.1084 -0.0280 0.0198 225 ALA B C 8954 O O . ALA B 225 ? 0.7450 0.3659 1.0250 -0.1070 -0.0331 0.0066 225 ALA B O 8955 C CB . ALA B 225 ? 0.6989 0.3681 0.9851 -0.0954 -0.0210 0.0194 225 ALA B CB 8956 N N . ILE B 226 ? 0.7108 0.3534 0.9647 -0.1136 -0.0332 0.0453 226 ILE B N 8957 C CA . ILE B 226 ? 0.7751 0.4038 1.0363 -0.1198 -0.0466 0.0611 226 ILE B CA 8958 C C . ILE B 226 ? 0.7424 0.3593 0.9923 -0.1314 -0.0498 0.0462 226 ILE B C 8959 O O . ILE B 226 ? 0.7655 0.3612 1.0278 -0.1357 -0.0622 0.0427 226 ILE B O 8960 C CB . ILE B 226 ? 0.7061 0.3441 0.9563 -0.1230 -0.0458 0.0926 226 ILE B CB 8961 C CG1 . ILE B 226 ? 0.7281 0.3679 0.9786 -0.1128 -0.0434 0.1076 226 ILE B CG1 8962 C CG2 . ILE B 226 ? 0.7170 0.3453 0.9822 -0.1310 -0.0589 0.1108 226 ILE B CG2 8963 C CD1 . ILE B 226 ? 0.8053 0.4465 1.0412 -0.1133 -0.0381 0.1391 226 ILE B CD1 8964 N N . MET B 227 ? 0.7401 0.3667 0.9621 -0.1372 -0.0393 0.0373 227 MET B N 8965 C CA . MET B 227 ? 0.8278 0.4407 1.0289 -0.1497 -0.0435 0.0235 227 MET B CA 8966 C C . MET B 227 ? 0.8326 0.4186 1.0349 -0.1473 -0.0423 -0.0067 227 MET B C 8967 O O . MET B 227 ? 0.8337 0.3935 1.0284 -0.1574 -0.0546 -0.0141 227 MET B O 8968 C CB . MET B 227 ? 0.8500 0.4769 1.0175 -0.1541 -0.0304 0.0197 227 MET B CB 8969 C CG . MET B 227 ? 0.9171 0.5264 1.0542 -0.1674 -0.0354 0.0041 227 MET B CG 8970 S SD . MET B 227 ? 0.9112 0.5079 1.0567 -0.1845 -0.0641 0.0220 227 MET B SD 8971 C CE . MET B 227 ? 1.3395 0.9723 1.4981 -0.1846 -0.0649 0.0632 227 MET B CE 8972 N N . GLN B 228 ? 0.9278 0.5188 1.1403 -0.1341 -0.0273 -0.0233 228 GLN B N 8973 C CA . GLN B 228 ? 0.8284 0.3950 1.0441 -0.1279 -0.0195 -0.0516 228 GLN B CA 8974 C C . GLN B 228 ? 1.2033 0.7474 1.4492 -0.1216 -0.0322 -0.0499 228 GLN B C 8975 O O . GLN B 228 ? 1.1532 0.6620 1.3900 -0.1240 -0.0337 -0.0677 228 GLN B O 8976 C CB . GLN B 228 ? 0.8160 0.4011 1.0430 -0.1151 0.0018 -0.0661 228 GLN B CB 8977 C CG . GLN B 228 ? 0.8972 0.4929 1.0887 -0.1216 0.0188 -0.0760 228 GLN B CG 8978 C CD . GLN B 228 ? 0.9167 0.4806 1.0665 -0.1322 0.0215 -0.0946 228 GLN B CD 8979 O OE1 . GLN B 228 ? 0.8993 0.4315 1.0477 -0.1289 0.0243 -0.1140 228 GLN B OE1 8980 N NE2 . GLN B 228 ? 1.0904 0.6588 1.2026 -0.1448 0.0201 -0.0881 228 GLN B NE2 8981 N N . ALA B 229 ? 1.1779 0.7375 1.4548 -0.1138 -0.0408 -0.0284 229 ALA B N 8982 C CA . ALA B 229 ? 0.8350 0.3733 1.1408 -0.1068 -0.0531 -0.0231 229 ALA B CA 8983 C C . ALA B 229 ? 0.8606 0.3717 1.1554 -0.1225 -0.0699 -0.0155 229 ALA B C 8984 O O . ALA B 229 ? 0.8922 0.3716 1.1993 -0.1208 -0.0779 -0.0206 229 ALA B O 8985 C CB . ALA B 229 ? 0.9430 0.5018 1.2758 -0.0970 -0.0600 0.0011 229 ALA B CB 8986 N N . THR B 230 ? 0.8581 0.3820 1.1318 -0.1381 -0.0756 -0.0019 230 THR B N 8987 C CA . THR B 230 ? 0.8721 0.3772 1.1393 -0.1564 -0.0940 0.0084 230 THR B CA 8988 C C . THR B 230 ? 0.9215 0.3921 1.1562 -0.1688 -0.0965 -0.0185 230 THR B C 8989 O O . THR B 230 ? 1.2408 0.6754 1.4746 -0.1786 -0.1105 -0.0231 230 THR B O 8990 C CB . THR B 230 ? 0.8432 0.3785 1.1058 -0.1676 -0.0992 0.0363 230 THR B CB 8991 O OG1 . THR B 230 ? 0.8071 0.3658 1.0913 -0.1561 -0.0946 0.0610 230 THR B OG1 8992 C CG2 . THR B 230 ? 0.9052 0.4270 1.1713 -0.1879 -0.1204 0.0505 230 THR B CG2 8993 N N . VAL B 231 ? 0.9245 0.4013 1.1278 -0.1692 -0.0826 -0.0364 231 VAL B N 8994 C CA . VAL B 231 ? 0.9775 0.4187 1.1376 -0.1828 -0.0846 -0.0605 231 VAL B CA 8995 C C . VAL B 231 ? 1.0216 0.4233 1.1716 -0.1710 -0.0688 -0.0930 231 VAL B C 8996 O O . VAL B 231 ? 1.2620 0.6196 1.3717 -0.1818 -0.0706 -0.1146 231 VAL B O 8997 C CB . VAL B 231 ? 1.2873 0.7477 1.4112 -0.1893 -0.0758 -0.0641 231 VAL B CB 8998 C CG1 . VAL B 231 ? 1.1916 0.6896 1.3261 -0.1988 -0.0887 -0.0309 231 VAL B CG1 8999 C CG2 . VAL B 231 ? 1.3493 0.8288 1.4750 -0.1707 -0.0476 -0.0782 231 VAL B CG2 9000 N N . CYS B 232 ? 0.9989 0.4140 1.1841 -0.1486 -0.0532 -0.0957 232 CYS B N 9001 C CA . CYS B 232 ? 1.1927 0.5733 1.3785 -0.1338 -0.0358 -0.1230 232 CYS B CA 9002 C C . CYS B 232 ? 1.2813 0.6362 1.4988 -0.1273 -0.0479 -0.1164 232 CYS B C 9003 O O . CYS B 232 ? 1.5547 0.9355 1.8168 -0.1134 -0.0503 -0.0988 232 CYS B O 9004 C CB . CYS B 232 ? 1.1636 0.5767 1.3731 -0.1128 -0.0101 -0.1306 232 CYS B CB 9005 S SG . CYS B 232 ? 1.0345 0.4770 1.2083 -0.1196 0.0072 -0.1372 232 CYS B SG 9006 N N . ASP B 233 ? 1.1962 0.4959 1.3860 -0.1384 -0.0561 -0.1307 233 ASP B N 9007 C CA . ASP B 233 ? 1.3256 0.5925 1.5391 -0.1355 -0.0686 -0.1245 233 ASP B CA 9008 C C . ASP B 233 ? 1.3628 0.6059 1.5983 -0.1086 -0.0472 -0.1422 233 ASP B C 9009 O O . ASP B 233 ? 1.4006 0.6482 1.6797 -0.0939 -0.0517 -0.1281 233 ASP B O 9010 C CB . ASP B 233 ? 1.5872 0.8010 1.7603 -0.1617 -0.0886 -0.1314 233 ASP B CB 9011 C CG . ASP B 233 ? 1.6452 0.8859 1.8025 -0.1883 -0.1110 -0.1118 233 ASP B CG 9012 O OD1 . ASP B 233 ? 1.2607 0.5577 1.4471 -0.1849 -0.1129 -0.0867 233 ASP B OD1 9013 O OD2 . ASP B 233 ? 1.9230 1.1269 2.0382 -0.2126 -0.1268 -0.1209 233 ASP B OD2 9014 N N . GLU B 234 ? 1.4410 0.6582 1.6462 -0.1013 -0.0228 -0.1717 234 GLU B N 9015 C CA . GLU B 234 ? 1.5791 0.7679 1.8035 -0.0749 0.0017 -0.1899 234 GLU B CA 9016 C C . GLU B 234 ? 1.5790 0.8252 1.8655 -0.0489 0.0151 -0.1779 234 GLU B C 9017 O O . GLU B 234 ? 1.6896 0.9315 2.0207 -0.0279 0.0178 -0.1722 234 GLU B O 9018 C CB . GLU B 234 ? 1.7670 0.9101 1.9376 -0.0742 0.0285 -0.2242 234 GLU B CB 9019 C CG . GLU B 234 ? 1.9524 1.0199 2.0570 -0.0971 0.0163 -0.2413 234 GLU B CG 9020 C CD . GLU B 234 ? 2.1036 1.1827 2.1686 -0.1307 -0.0119 -0.2309 234 GLU B CD 9021 O OE1 . GLU B 234 ? 2.1179 1.2593 2.1989 -0.1336 -0.0150 -0.2146 234 GLU B OE1 9022 O OE2 . GLU B 234 ? 2.1864 1.2113 2.2050 -0.1544 -0.0315 -0.2383 234 GLU B OE2 9023 N N . LYS B 235 ? 1.5142 0.8126 1.8028 -0.0513 0.0218 -0.1731 235 LYS B N 9024 C CA . LYS B 235 ? 1.4495 0.8029 1.7928 -0.0310 0.0325 -0.1625 235 LYS B CA 9025 C C . LYS B 235 ? 1.4493 0.8311 1.8369 -0.0270 0.0077 -0.1320 235 LYS B C 9026 O O . LYS B 235 ? 1.6338 1.0364 2.0723 -0.0060 0.0107 -0.1239 235 LYS B O 9027 C CB . LYS B 235 ? 1.2490 0.6463 1.5772 -0.0390 0.0429 -0.1635 235 LYS B CB 9028 C CG . LYS B 235 ? 1.2322 0.6528 1.5883 -0.0196 0.0739 -0.1772 235 LYS B CG 9029 C CD . LYS B 235 ? 1.4279 0.7954 1.7624 -0.0087 0.1016 -0.2063 235 LYS B CD 9030 C CE . LYS B 235 ? 1.3985 0.7921 1.7715 0.0133 0.1359 -0.2170 235 LYS B CE 9031 N NZ . LYS B 235 ? 1.4265 0.7637 1.7764 0.0267 0.1684 -0.2450 235 LYS B NZ 9032 N N . ILE B 236 ? 1.1969 0.5790 1.5650 -0.0471 -0.0165 -0.1138 236 ILE B N 9033 C CA . ILE B 236 ? 1.1395 0.5411 1.5399 -0.0450 -0.0382 -0.0840 236 ILE B CA 9034 C C . ILE B 236 ? 1.1587 0.5162 1.5758 -0.0372 -0.0476 -0.0813 236 ILE B C 9035 O O . ILE B 236 ? 1.1673 0.5352 1.6246 -0.0214 -0.0550 -0.0646 236 ILE B O 9036 C CB . ILE B 236 ? 1.1006 0.5186 1.4773 -0.0677 -0.0564 -0.0631 236 ILE B CB 9037 C CG1 . ILE B 236 ? 1.2651 0.7238 1.6239 -0.0740 -0.0464 -0.0641 236 ILE B CG1 9038 C CG2 . ILE B 236 ? 1.0590 0.4908 1.4640 -0.0643 -0.0747 -0.0321 236 ILE B CG2 9039 C CD1 . ILE B 236 ? 1.2842 0.7842 1.6752 -0.0578 -0.0379 -0.0585 236 ILE B CD1 9040 N N . GLY B 237 ? 1.3406 0.6454 1.7235 -0.0493 -0.0482 -0.0974 237 GLY B N 9041 C CA . GLY B 237 ? 1.5176 0.7747 1.9066 -0.0440 -0.0553 -0.0966 237 GLY B CA 9042 C C . GLY B 237 ? 1.4492 0.7065 1.8255 -0.0623 -0.0798 -0.0710 237 GLY B C 9043 O O . GLY B 237 ? 1.4037 0.6442 1.7912 -0.0545 -0.0863 -0.0597 237 GLY B O 9044 N N . TRP B 238 ? 1.3509 0.6291 1.7066 -0.0857 -0.0915 -0.0606 238 TRP B N 9045 C CA . TRP B 238 ? 1.1698 0.4524 1.5164 -0.1041 -0.1109 -0.0361 238 TRP B CA 9046 C C . TRP B 238 ? 1.2315 0.4607 1.5523 -0.1141 -0.1158 -0.0465 238 TRP B C 9047 O O . TRP B 238 ? 1.2219 0.4120 1.5061 -0.1247 -0.1110 -0.0719 238 TRP B O 9048 C CB . TRP B 238 ? 1.2157 0.5257 1.5436 -0.1274 -0.1196 -0.0265 238 TRP B CB 9049 C CG . TRP B 238 ? 1.1090 0.4694 1.4568 -0.1211 -0.1163 -0.0099 238 TRP B CG 9050 C CD1 . TRP B 238 ? 1.0428 0.4238 1.3804 -0.1234 -0.1069 -0.0202 238 TRP B CD1 9051 C CD2 . TRP B 238 ? 1.0781 0.4720 1.4506 -0.1120 -0.1207 0.0196 238 TRP B CD2 9052 N NE1 . TRP B 238 ? 0.9534 0.3797 1.3064 -0.1163 -0.1047 0.0010 238 TRP B NE1 9053 C CE2 . TRP B 238 ? 0.9259 0.3548 1.3019 -0.1101 -0.1143 0.0254 238 TRP B CE2 9054 C CE3 . TRP B 238 ? 1.2021 0.5960 1.5892 -0.1057 -0.1283 0.0410 238 TRP B CE3 9055 C CZ2 . TRP B 238 ? 0.8886 0.3486 1.2775 -0.1024 -0.1156 0.0513 238 TRP B CZ2 9056 C CZ3 . TRP B 238 ? 1.2469 0.6734 1.6471 -0.0975 -0.1294 0.0665 238 TRP B CZ3 9057 C CH2 . TRP B 238 ? 0.8965 0.3540 1.2954 -0.0961 -0.1232 0.0712 238 TRP B CH2 9058 N N . ARG B 239 ? 1.2970 0.5206 1.6323 -0.1116 -0.1245 -0.0273 239 ARG B N 9059 C CA . ARG B 239 ? 1.3659 0.5374 1.6778 -0.1225 -0.1291 -0.0349 239 ARG B CA 9060 C C . ARG B 239 ? 1.2566 0.4330 1.5497 -0.1543 -0.1463 -0.0230 239 ARG B C 9061 O O . ARG B 239 ? 1.4942 0.7157 1.7948 -0.1651 -0.1535 -0.0071 239 ARG B O 9062 C CB . ARG B 239 ? 1.3184 0.4787 1.6549 -0.1050 -0.1296 -0.0200 239 ARG B CB 9063 C CG . ARG B 239 ? 1.3893 0.5428 1.7497 -0.0725 -0.1144 -0.0304 239 ARG B CG 9064 C CD . ARG B 239 ? 1.2873 0.4299 1.6704 -0.0562 -0.1177 -0.0129 239 ARG B CD 9065 N NE . ARG B 239 ? 1.2344 0.4240 1.6413 -0.0561 -0.1297 0.0191 239 ARG B NE 9066 C CZ . ARG B 239 ? 1.2952 0.4835 1.7198 -0.0436 -0.1347 0.0391 239 ARG B CZ 9067 N NH1 . ARG B 239 ? 1.3301 0.4746 1.7557 -0.0297 -0.1295 0.0316 239 ARG B NH1 9068 N NH2 . ARG B 239 ? 1.1993 0.4264 1.6364 -0.0446 -0.1435 0.0666 239 ARG B NH2 9069 N N . ASN B 240 ? 1.3196 0.4497 1.5907 -0.1690 -0.1524 -0.0297 240 ASN B N 9070 C CA . ASN B 240 ? 1.4937 0.6304 1.7562 -0.1995 -0.1709 -0.0161 240 ASN B CA 9071 C C . ASN B 240 ? 1.6390 0.7705 1.9223 -0.2005 -0.1778 0.0063 240 ASN B C 9072 O O . ASN B 240 ? 1.6469 0.7472 1.9351 -0.1822 -0.1688 0.0024 240 ASN B O 9073 C CB . ASN B 240 ? 1.5851 0.6726 1.8007 -0.2224 -0.1753 -0.0432 240 ASN B CB 9074 C CG . ASN B 240 ? 1.7572 0.7746 1.9455 -0.2109 -0.1601 -0.0708 240 ASN B CG 9075 O OD1 . ASN B 240 ? 1.8172 0.8264 2.0180 -0.1816 -0.1425 -0.0777 240 ASN B OD1 9076 N ND2 . ASN B 240 ? 1.8058 0.7723 1.9579 -0.2334 -0.1665 -0.0861 240 ASN B ND2 9077 N N . ASP B 241 ? 1.7304 0.8931 2.0277 -0.2209 -0.1928 0.0307 241 ASP B N 9078 C CA . ASP B 241 ? 1.6347 0.8015 1.9556 -0.2225 -0.1981 0.0561 241 ASP B CA 9079 C C . ASP B 241 ? 1.4980 0.6872 1.8449 -0.1932 -0.1869 0.0720 241 ASP B C 9080 O O . ASP B 241 ? 1.3149 0.4808 1.6694 -0.1828 -0.1841 0.0792 241 ASP B O 9081 C CB . ASP B 241 ? 1.5921 0.6956 1.8928 -0.2327 -0.2007 0.0425 241 ASP B CB 9082 C CG . ASP B 241 ? 1.6087 0.6918 1.8841 -0.2660 -0.2161 0.0312 241 ASP B CG 9083 O OD1 . ASP B 241 ? 1.5623 0.6101 1.8009 -0.2708 -0.2129 0.0013 241 ASP B OD1 9084 O OD2 . ASP B 241 ? 1.6781 0.7809 1.9704 -0.2874 -0.2316 0.0526 241 ASP B OD2 9085 N N . ALA B 242 ? 1.3942 0.6272 1.7521 -0.1808 -0.1812 0.0776 242 ALA B N 9086 C CA . ALA B 242 ? 1.3262 0.5853 1.7056 -0.1555 -0.1730 0.0934 242 ALA B CA 9087 C C . ALA B 242 ? 1.1241 0.4387 1.5135 -0.1557 -0.1714 0.1109 242 ALA B C 9088 O O . ALA B 242 ? 1.1065 0.4361 1.4862 -0.1666 -0.1726 0.1017 242 ALA B O 9089 C CB . ALA B 242 ? 1.1981 0.4356 1.5767 -0.1312 -0.1627 0.0721 242 ALA B CB 9090 N N . SER B 243 ? 1.0950 0.4361 1.4992 -0.1438 -0.1678 0.1358 243 SER B N 9091 C CA . SER B 243 ? 1.1388 0.5266 1.5469 -0.1423 -0.1629 0.1532 243 SER B CA 9092 C C . SER B 243 ? 1.1775 0.5775 1.5811 -0.1292 -0.1563 0.1376 243 SER B C 9093 O O . SER B 243 ? 1.1904 0.5790 1.5990 -0.1104 -0.1530 0.1286 243 SER B O 9094 C CB . SER B 243 ? 1.0298 0.4334 1.4450 -0.1315 -0.1580 0.1809 243 SER B CB 9095 O OG . SER B 243 ? 1.0498 0.4523 1.4721 -0.1461 -0.1615 0.1991 243 SER B OG 9096 N N . HIS B 244 ? 1.0981 0.5226 1.4949 -0.1394 -0.1547 0.1359 244 HIS B N 9097 C CA . HIS B 244 ? 0.9794 0.4157 1.3711 -0.1302 -0.1475 0.1210 244 HIS B CA 9098 C C . HIS B 244 ? 0.9304 0.4031 1.3222 -0.1218 -0.1397 0.1418 244 HIS B C 9099 O O . HIS B 244 ? 0.9191 0.4166 1.3066 -0.1318 -0.1373 0.1585 244 HIS B O 9100 C CB . HIS B 244 ? 1.0520 0.4849 1.4290 -0.1469 -0.1496 0.1025 244 HIS B CB 9101 C CG . HIS B 244 ? 1.1669 0.5573 1.5321 -0.1576 -0.1565 0.0802 244 HIS B CG 9102 N ND1 . HIS B 244 ? 1.2353 0.6169 1.5829 -0.1809 -0.1656 0.0724 244 HIS B ND1 9103 C CD2 . HIS B 244 ? 1.2000 0.5508 1.5647 -0.1483 -0.1553 0.0642 244 HIS B CD2 9104 C CE1 . HIS B 244 ? 1.2618 0.5970 1.5935 -0.1867 -0.1695 0.0511 244 HIS B CE1 9105 N NE2 . HIS B 244 ? 1.2983 0.6133 1.6403 -0.1662 -0.1617 0.0457 244 HIS B NE2 9106 N N . LEU B 245 ? 0.9373 0.4116 1.3333 -0.1033 -0.1359 0.1414 245 LEU B N 9107 C CA . LEU B 245 ? 0.8697 0.3703 1.2573 -0.0957 -0.1290 0.1589 245 LEU B CA 9108 C C . LEU B 245 ? 1.0386 0.5482 1.4254 -0.0890 -0.1243 0.1436 245 LEU B C 9109 O O . LEU B 245 ? 1.1951 0.6936 1.5969 -0.0771 -0.1269 0.1290 245 LEU B O 9110 C CB . LEU B 245 ? 0.8818 0.3765 1.2696 -0.0822 -0.1310 0.1760 245 LEU B CB 9111 C CG . LEU B 245 ? 0.9033 0.3912 1.2898 -0.0880 -0.1320 0.1951 245 LEU B CG 9112 C CD1 . LEU B 245 ? 1.0420 0.5221 1.4206 -0.0742 -0.1322 0.2114 245 LEU B CD1 9113 C CD2 . LEU B 245 ? 0.8863 0.3974 1.2646 -0.1009 -0.1241 0.2111 245 LEU B CD2 9114 N N . LEU B 246 ? 1.0005 0.5311 1.3729 -0.0965 -0.1166 0.1479 246 LEU B N 9115 C CA . LEU B 246 ? 0.7997 0.3399 1.1690 -0.0919 -0.1105 0.1364 246 LEU B CA 9116 C C . LEU B 246 ? 0.7830 0.3385 1.1335 -0.0858 -0.1047 0.1573 246 LEU B C 9117 O O . LEU B 246 ? 0.8248 0.3940 1.1553 -0.0917 -0.0958 0.1731 246 LEU B O 9118 C CB . LEU B 246 ? 0.7892 0.3357 1.1501 -0.1054 -0.1049 0.1227 246 LEU B CB 9119 C CG . LEU B 246 ? 0.7700 0.3323 1.1216 -0.1012 -0.0945 0.1058 246 LEU B CG 9120 C CD1 . LEU B 246 ? 0.7812 0.3374 1.1512 -0.0882 -0.0947 0.0827 246 LEU B CD1 9121 C CD2 . LEU B 246 ? 0.8652 0.4380 1.1966 -0.1138 -0.0872 0.0930 246 LEU B CD2 9122 N N . VAL B 247 ? 0.7864 0.3374 1.1421 -0.0737 -0.1098 0.1576 247 VAL B N 9123 C CA . VAL B 247 ? 0.8327 0.3890 1.1621 -0.0689 -0.1068 0.1762 247 VAL B CA 9124 C C . VAL B 247 ? 1.0321 0.5972 1.3544 -0.0706 -0.1023 0.1677 247 VAL B C 9125 O O . VAL B 247 ? 1.0998 0.6745 1.4411 -0.0664 -0.1052 0.1460 247 VAL B O 9126 C CB . VAL B 247 ? 0.8907 0.4340 1.2242 -0.0569 -0.1192 0.1861 247 VAL B CB 9127 C CG1 . VAL B 247 ? 0.8125 0.3491 1.1862 -0.0484 -0.1315 0.1685 247 VAL B CG1 9128 C CG2 . VAL B 247 ? 1.1649 0.7071 1.4661 -0.0533 -0.1193 0.2005 247 VAL B CG2 9129 N N . PHE B 248 ? 1.0431 0.6148 1.3297 -0.0748 -0.0901 0.1808 248 PHE B N 9130 C CA . PHE B 248 ? 0.7610 0.3464 1.0281 -0.0780 -0.0811 0.1708 248 PHE B CA 9131 C C . PHE B 248 ? 0.8367 0.4116 1.0706 -0.0745 -0.0828 0.1851 248 PHE B C 9132 O O . PHE B 248 ? 1.1817 0.7423 1.3845 -0.0726 -0.0767 0.2066 248 PHE B O 9133 C CB . PHE B 248 ? 0.7618 0.3577 1.0116 -0.0868 -0.0645 0.1734 248 PHE B CB 9134 C CG . PHE B 248 ? 0.7975 0.4093 1.0232 -0.0899 -0.0522 0.1600 248 PHE B CG 9135 C CD1 . PHE B 248 ? 0.9389 0.5674 1.1781 -0.0926 -0.0501 0.1326 248 PHE B CD1 9136 C CD2 . PHE B 248 ? 0.9021 0.5076 1.0878 -0.0901 -0.0405 0.1750 248 PHE B CD2 9137 C CE1 . PHE B 248 ? 1.0988 0.7406 1.3158 -0.0963 -0.0375 0.1213 248 PHE B CE1 9138 C CE2 . PHE B 248 ? 0.9937 0.6099 1.1554 -0.0939 -0.0288 0.1629 248 PHE B CE2 9139 C CZ . PHE B 248 ? 1.1562 0.7922 1.3353 -0.0975 -0.0278 0.1365 248 PHE B CZ 9140 N N . THR B 249 ? 0.7637 0.3500 0.9981 -0.0734 -0.0890 0.1702 249 THR B N 9141 C CA . THR B 249 ? 0.8637 0.4373 1.0622 -0.0735 -0.0948 0.1816 249 THR B CA 9142 C C . THR B 249 ? 0.9328 0.5210 1.1085 -0.0810 -0.0853 0.1678 249 THR B C 9143 O O . THR B 249 ? 1.2040 0.8181 1.4081 -0.0829 -0.0839 0.1454 249 THR B O 9144 C CB . THR B 249 ? 1.0101 0.5799 1.2317 -0.0665 -0.1196 0.1829 249 THR B CB 9145 O OG1 . THR B 249 ? 1.1576 0.7564 1.4255 -0.0642 -0.1251 0.1592 249 THR B OG1 9146 C CG2 . THR B 249 ? 1.1186 0.6674 1.3567 -0.0588 -0.1287 0.1990 249 THR B CG2 9147 N N . THR B 250 ? 0.8004 0.3680 0.9222 -0.0852 -0.0768 0.1816 250 THR B N 9148 C CA . THR B 250 ? 0.7972 0.3708 0.8899 -0.0937 -0.0680 0.1706 250 THR B CA 9149 C C . THR B 250 ? 0.8557 0.3939 0.8859 -0.0975 -0.0691 0.1868 250 THR B C 9150 O O . THR B 250 ? 0.8471 0.3541 0.8466 -0.0926 -0.0660 0.2087 250 THR B O 9151 C CB . THR B 250 ? 0.8834 0.4684 0.9668 -0.0971 -0.0430 0.1642 250 THR B CB 9152 O OG1 . THR B 250 ? 0.9722 0.5562 1.0206 -0.1053 -0.0331 0.1561 250 THR B OG1 9153 C CG2 . THR B 250 ? 0.9948 0.5599 1.0539 -0.0929 -0.0277 0.1878 250 THR B CG2 9154 N N . ASP B 251 ? 1.1662 0.7064 1.1754 -0.1072 -0.0728 0.1759 251 ASP B N 9155 C CA . ASP B 251 ? 1.0627 0.5634 1.0042 -0.1140 -0.0753 0.1876 251 ASP B CA 9156 C C . ASP B 251 ? 0.9696 0.4443 0.8546 -0.1146 -0.0439 0.1961 251 ASP B C 9157 O O . ASP B 251 ? 0.9339 0.3633 0.7564 -0.1138 -0.0366 0.2135 251 ASP B O 9158 C CB . ASP B 251 ? 0.9812 0.4940 0.9247 -0.1272 -0.0934 0.1728 251 ASP B CB 9159 C CG . ASP B 251 ? 1.4303 0.9020 1.3171 -0.1351 -0.1135 0.1856 251 ASP B CG 9160 O OD1 . ASP B 251 ? 1.5924 1.0502 1.4392 -0.1497 -0.1152 0.1794 251 ASP B OD1 9161 O OD2 . ASP B 251 ? 1.6169 1.0671 1.4960 -0.1279 -0.1286 0.2019 251 ASP B OD2 9162 N N . ALA B 252 ? 0.8932 0.3943 0.7987 -0.1148 -0.0245 0.1846 252 ALA B N 9163 C CA . ALA B 252 ? 1.0141 0.4962 0.8716 -0.1154 0.0048 0.1905 252 ALA B CA 9164 C C . ALA B 252 ? 0.9500 0.4571 0.8390 -0.1081 0.0240 0.1925 252 ALA B C 9165 O O . ALA B 252 ? 0.9388 0.4701 0.8792 -0.1033 0.0147 0.1914 252 ALA B O 9166 C CB . ALA B 252 ? 1.1674 0.6502 1.0011 -0.1284 0.0074 0.1733 252 ALA B CB 9167 N N . LYS B 253 ? 0.9043 0.4029 0.7605 -0.1079 0.0495 0.1962 253 LYS B N 9168 C CA . LYS B 253 ? 0.8753 0.3971 0.7566 -0.1017 0.0661 0.2016 253 LYS B CA 9169 C C . LYS B 253 ? 0.8056 0.3673 0.7344 -0.1074 0.0579 0.1779 253 LYS B C 9170 O O . LYS B 253 ? 0.8019 0.3766 0.7491 -0.1142 0.0424 0.1577 253 LYS B O 9171 C CB . LYS B 253 ? 0.9310 0.4653 0.7810 -0.0946 0.0855 0.2048 253 LYS B CB 9172 C CG . LYS B 253 ? 1.0170 0.5334 0.8256 -0.1035 0.0924 0.1899 253 LYS B CG 9173 C CD . LYS B 253 ? 1.1583 0.6803 0.9333 -0.0932 0.1109 0.1934 253 LYS B CD 9174 C CE . LYS B 253 ? 1.2295 0.7277 0.9590 -0.1030 0.1164 0.1785 253 LYS B CE 9175 N NZ . LYS B 253 ? 1.2024 0.7003 0.8987 -0.0919 0.1349 0.1794 253 LYS B NZ 9176 N N . THR B 254 ? 0.7850 0.3661 0.7338 -0.1045 0.0682 0.1813 254 THR B N 9177 C CA . THR B 254 ? 0.8257 0.4387 0.8141 -0.1094 0.0604 0.1596 254 THR B CA 9178 C C . THR B 254 ? 0.8130 0.4367 0.7891 -0.1112 0.0776 0.1572 254 THR B C 9179 O O . THR B 254 ? 0.9299 0.5433 0.8817 -0.1060 0.0946 0.1777 254 THR B O 9180 C CB . THR B 254 ? 0.9145 0.5414 0.9494 -0.1066 0.0452 0.1627 254 THR B CB 9181 O OG1 . THR B 254 ? 0.9261 0.5757 0.9870 -0.1115 0.0416 0.1428 254 THR B OG1 9182 C CG2 . THR B 254 ? 0.7022 0.3227 0.7358 -0.1007 0.0538 0.1920 254 THR B CG2 9183 N N . HIS B 255 ? 0.7308 0.3740 0.7236 -0.1176 0.0744 0.1331 255 HIS B N 9184 C CA . HIS B 255 ? 0.7447 0.3984 0.7279 -0.1200 0.0869 0.1292 255 HIS B CA 9185 C C . HIS B 255 ? 0.7639 0.4293 0.7707 -0.1177 0.0807 0.1426 255 HIS B C 9186 O O . HIS B 255 ? 0.7793 0.4514 0.8202 -0.1183 0.0638 0.1397 255 HIS B O 9187 C CB . HIS B 255 ? 0.7655 0.4331 0.7582 -0.1275 0.0860 0.0995 255 HIS B CB 9188 C CG . HIS B 255 ? 0.7812 0.4414 0.7468 -0.1330 0.0975 0.0888 255 HIS B CG 9189 N ND1 . HIS B 255 ? 1.0692 0.7162 0.9925 -0.1343 0.1170 0.0963 255 HIS B ND1 9190 C CD2 . HIS B 255 ? 0.7064 0.3709 0.6836 -0.1385 0.0917 0.0723 255 HIS B CD2 9191 C CE1 . HIS B 255 ? 1.1018 0.7422 1.0085 -0.1420 0.1225 0.0837 255 HIS B CE1 9192 N NE2 . HIS B 255 ? 0.8531 0.5065 0.7944 -0.1453 0.1065 0.0695 255 HIS B NE2 9193 N N . ILE B 256 ? 0.7707 0.4381 0.7604 -0.1156 0.0937 0.1585 256 ILE B N 9194 C CA . ILE B 256 ? 0.7720 0.4553 0.7855 -0.1167 0.0854 0.1710 256 ILE B CA 9195 C C . ILE B 256 ? 0.7380 0.4310 0.7412 -0.1239 0.0856 0.1534 256 ILE B C 9196 O O . ILE B 256 ? 0.6785 0.3665 0.6601 -0.1271 0.0944 0.1319 256 ILE B O 9197 C CB . ILE B 256 ? 0.8548 0.5372 0.8641 -0.1079 0.0980 0.2066 256 ILE B CB 9198 C CG1 . ILE B 256 ? 0.6905 0.3604 0.6564 -0.1025 0.1227 0.2124 256 ILE B CG1 9199 C CG2 . ILE B 256 ? 0.6821 0.3533 0.6995 -0.1007 0.0973 0.2232 256 ILE B CG2 9200 C CD1 . ILE B 256 ? 0.6955 0.3800 0.6508 -0.0883 0.1265 0.2314 256 ILE B CD1 9201 N N . ALA B 257 ? 0.7613 0.4671 0.7790 -0.1278 0.0752 0.1632 257 ALA B N 9202 C CA . ALA B 257 ? 0.6856 0.3959 0.6860 -0.1353 0.0738 0.1488 257 ALA B CA 9203 C C . ALA B 257 ? 0.7251 0.4316 0.6889 -0.1304 0.0955 0.1583 257 ALA B C 9204 O O . ALA B 257 ? 0.7158 0.4176 0.6721 -0.1207 0.1101 0.1817 257 ALA B O 9205 C CB . ALA B 257 ? 0.7233 0.4456 0.7450 -0.1428 0.0531 0.1597 257 ALA B CB 9206 N N . LEU B 258 ? 0.7053 0.4091 0.6432 -0.1366 0.0995 0.1396 258 LEU B N 9207 C CA . LEU B 258 ? 0.8516 0.5483 0.7509 -0.1334 0.1201 0.1447 258 LEU B CA 9208 C C . LEU B 258 ? 0.8836 0.5642 0.7595 -0.1303 0.1410 0.1349 258 LEU B C 9209 O O . LEU B 258 ? 0.8677 0.5372 0.7085 -0.1291 0.1597 0.1357 258 LEU B O 9210 C CB . LEU B 258 ? 0.7202 0.4247 0.6212 -0.1246 0.1243 0.1815 258 LEU B CB 9211 C CG . LEU B 258 ? 0.8084 0.5318 0.7307 -0.1300 0.1022 0.1958 258 LEU B CG 9212 C CD1 . LEU B 258 ? 0.8883 0.6239 0.8202 -0.1189 0.1094 0.2359 258 LEU B CD1 9213 C CD2 . LEU B 258 ? 0.8295 0.5480 0.7231 -0.1408 0.0951 0.1742 258 LEU B CD2 9214 N N . ASP B 259 ? 0.8009 0.4786 0.6951 -0.1302 0.1361 0.1264 259 ASP B N 9215 C CA . ASP B 259 ? 0.7155 0.3783 0.5898 -0.1311 0.1496 0.1157 259 ASP B CA 9216 C C . ASP B 259 ? 0.7159 0.3803 0.5814 -0.1405 0.1550 0.0859 259 ASP B C 9217 O O . ASP B 259 ? 0.8254 0.4783 0.6659 -0.1442 0.1704 0.0787 259 ASP B O 9218 C CB . ASP B 259 ? 0.8430 0.5032 0.7404 -0.1293 0.1385 0.1161 259 ASP B CB 9219 C CG . ASP B 259 ? 0.9954 0.6426 0.8845 -0.1195 0.1439 0.1456 259 ASP B CG 9220 O OD1 . ASP B 259 ? 1.0712 0.7075 0.9317 -0.1134 0.1618 0.1638 259 ASP B OD1 9221 O OD2 . ASP B 259 ? 1.0941 0.7396 1.0040 -0.1168 0.1322 0.1516 259 ASP B OD2 9222 N N . GLY B 260 ? 0.7145 0.3906 0.5995 -0.1450 0.1436 0.0690 260 GLY B N 9223 C CA . GLY B 260 ? 0.7360 0.4136 0.6180 -0.1523 0.1511 0.0406 260 GLY B CA 9224 C C . GLY B 260 ? 0.7530 0.4218 0.5943 -0.1563 0.1704 0.0366 260 GLY B C 9225 O O . GLY B 260 ? 0.8815 0.5496 0.7169 -0.1624 0.1821 0.0148 260 GLY B O 9226 N N . ARG B 261 ? 0.7765 0.4386 0.5916 -0.1520 0.1751 0.0592 261 ARG B N 9227 C CA . ARG B 261 ? 0.7866 0.4377 0.5602 -0.1545 0.1929 0.0590 261 ARG B CA 9228 C C . ARG B 261 ? 0.8196 0.4583 0.5728 -0.1590 0.2141 0.0496 261 ARG B C 9229 O O . ARG B 261 ? 0.9131 0.5442 0.6406 -0.1652 0.2300 0.0369 261 ARG B O 9230 C CB . ARG B 261 ? 0.8429 0.4907 0.5986 -0.1463 0.1936 0.0896 261 ARG B CB 9231 C CG . ARG B 261 ? 0.8051 0.4404 0.5172 -0.1474 0.2095 0.0923 261 ARG B CG 9232 C CD . ARG B 261 ? 0.8126 0.4484 0.5149 -0.1371 0.2088 0.1259 261 ARG B CD 9233 N NE . ARG B 261 ? 0.9149 0.5368 0.5740 -0.1370 0.2237 0.1300 261 ARG B NE 9234 C CZ . ARG B 261 ? 1.0026 0.6352 0.6594 -0.1236 0.2195 0.1552 261 ARG B CZ 9235 N NH1 . ARG B 261 ? 1.1933 0.8447 0.8836 -0.1128 0.2076 0.1818 261 ARG B NH1 9236 N NH2 . ARG B 261 ? 0.9970 0.6253 0.6238 -0.1203 0.2261 0.1539 261 ARG B NH2 9237 N N . LEU B 262 ? 0.8644 0.4987 0.6268 -0.1573 0.2136 0.0564 262 LEU B N 9238 C CA . LEU B 262 ? 0.9439 0.5654 0.6898 -0.1650 0.2283 0.0472 262 LEU B CA 9239 C C . LEU B 262 ? 1.0020 0.6381 0.7718 -0.1753 0.2293 0.0193 262 LEU B C 9240 O O . LEU B 262 ? 1.2619 0.8912 1.0142 -0.1845 0.2465 0.0084 262 LEU B O 9241 C CB . LEU B 262 ? 0.7744 0.3860 0.5249 -0.1629 0.2217 0.0584 262 LEU B CB 9242 C CG . LEU B 262 ? 0.7904 0.3872 0.5100 -0.1493 0.2266 0.0797 262 LEU B CG 9243 C CD1 . LEU B 262 ? 0.7768 0.3865 0.5035 -0.1337 0.2211 0.1001 262 LEU B CD1 9244 C CD2 . LEU B 262 ? 0.9455 0.5326 0.6673 -0.1472 0.2171 0.0850 262 LEU B CD2 9245 N N . ALA B 263 ? 0.8028 0.4580 0.6140 -0.1732 0.2127 0.0088 263 ALA B N 9246 C CA . ALA B 263 ? 0.7747 0.4450 0.6155 -0.1791 0.2155 -0.0161 263 ALA B CA 9247 C C . ALA B 263 ? 0.7886 0.4551 0.6078 -0.1816 0.2304 -0.0295 263 ALA B C 9248 O O . ALA B 263 ? 0.8238 0.4987 0.6604 -0.1857 0.2404 -0.0501 263 ALA B O 9249 C CB . ALA B 263 ? 0.8281 0.5144 0.7166 -0.1736 0.1948 -0.0217 263 ALA B CB 9250 N N . GLY B 264 ? 0.7909 0.4439 0.5718 -0.1785 0.2325 -0.0162 264 GLY B N 9251 C CA . GLY B 264 ? 1.1375 0.7816 0.8891 -0.1810 0.2429 -0.0264 264 GLY B CA 9252 C C . GLY B 264 ? 0.9080 0.5552 0.6734 -0.1780 0.2252 -0.0337 264 GLY B C 9253 O O . GLY B 264 ? 0.8896 0.5283 0.6397 -0.1813 0.2328 -0.0515 264 GLY B O 9254 N N . ILE B 265 ? 0.8861 0.5416 0.6773 -0.1725 0.2025 -0.0199 265 ILE B N 9255 C CA . ILE B 265 ? 0.8761 0.5317 0.6813 -0.1716 0.1828 -0.0253 265 ILE B CA 9256 C C . ILE B 265 ? 0.8717 0.5243 0.6592 -0.1706 0.1661 -0.0021 265 ILE B C 9257 O O . ILE B 265 ? 0.8450 0.5067 0.6504 -0.1654 0.1551 0.0211 265 ILE B O 9258 C CB . ILE B 265 ? 0.8112 0.4795 0.6669 -0.1674 0.1676 -0.0277 265 ILE B CB 9259 C CG1 . ILE B 265 ? 0.7700 0.4475 0.6519 -0.1678 0.1813 -0.0449 265 ILE B CG1 9260 C CG2 . ILE B 265 ? 0.7919 0.4541 0.6588 -0.1679 0.1504 -0.0374 265 ILE B CG2 9261 C CD1 . ILE B 265 ? 0.7466 0.4367 0.6776 -0.1626 0.1652 -0.0443 265 ILE B CD1 9262 N N . VAL B 266 ? 0.9141 0.5533 0.6662 -0.1758 0.1643 -0.0073 266 VAL B N 9263 C CA . VAL B 266 ? 0.9354 0.5744 0.6721 -0.1768 0.1456 0.0158 266 VAL B CA 9264 C C . VAL B 266 ? 0.9620 0.5983 0.7118 -0.1827 0.1177 0.0123 266 VAL B C 9265 O O . VAL B 266 ? 0.9799 0.6200 0.7255 -0.1858 0.0971 0.0331 266 VAL B O 9266 C CB . VAL B 266 ? 1.0662 0.6895 0.7488 -0.1805 0.1567 0.0173 266 VAL B CB 9267 C CG1 . VAL B 266 ? 0.9424 0.5650 0.6095 -0.1754 0.1829 0.0256 266 VAL B CG1 9268 C CG2 . VAL B 266 ? 1.2825 0.8839 0.9346 -0.1883 0.1647 -0.0136 266 VAL B CG2 9269 N N . GLN B 267 ? 1.0344 0.6635 0.8015 -0.1845 0.1167 -0.0127 267 GLN B N 9270 C CA . GLN B 267 ? 1.1485 0.7653 0.9189 -0.1917 0.0923 -0.0203 267 GLN B CA 9271 C C . GLN B 267 ? 1.0171 0.6504 0.8386 -0.1890 0.0714 -0.0044 267 GLN B C 9272 O O . GLN B 267 ? 1.0869 0.7297 0.9441 -0.1816 0.0783 -0.0091 267 GLN B O 9273 C CB . GLN B 267 ? 1.2228 0.8161 0.9813 -0.1936 0.1044 -0.0555 267 GLN B CB 9274 C CG . GLN B 267 ? 1.1471 0.7155 0.8942 -0.2026 0.0815 -0.0666 267 GLN B CG 9275 C CD . GLN B 267 ? 1.4229 0.9635 1.1585 -0.2012 0.0982 -0.1011 267 GLN B CD 9276 O OE1 . GLN B 267 ? 1.6439 1.1941 1.4213 -0.1917 0.1096 -0.1115 267 GLN B OE1 9277 N NE2 . GLN B 267 ? 1.5373 1.0412 1.2146 -0.2098 0.1003 -0.1180 267 GLN B NE2 9278 N N . PRO B 268 ? 0.9627 0.5997 0.7887 -0.1958 0.0449 0.0159 268 PRO B N 9279 C CA . PRO B 268 ? 0.9415 0.5938 0.8160 -0.1946 0.0255 0.0345 268 PRO B CA 9280 C C . PRO B 268 ? 0.9525 0.5890 0.8467 -0.1969 0.0177 0.0114 268 PRO B C 9281 O O . PRO B 268 ? 1.0881 0.6979 0.9532 -0.2030 0.0189 -0.0154 268 PRO B O 9282 C CB . PRO B 268 ? 0.8626 0.5206 0.7332 -0.2052 -0.0014 0.0585 268 PRO B CB 9283 C CG . PRO B 268 ? 0.8966 0.5471 0.7174 -0.2081 0.0061 0.0586 268 PRO B CG 9284 C CD . PRO B 268 ? 1.0121 0.6388 0.7982 -0.2065 0.0302 0.0235 268 PRO B CD 9285 N N . ASN B 269 ? 0.9020 0.5510 0.8419 -0.1909 0.0116 0.0222 269 ASN B N 9286 C CA . ASN B 269 ? 0.8809 0.5143 0.8432 -0.1915 0.0031 0.0042 269 ASN B CA 9287 C C . ASN B 269 ? 0.9234 0.5352 0.8729 -0.2070 -0.0229 0.0004 269 ASN B C 9288 O O . ASN B 269 ? 0.9334 0.5567 0.8932 -0.2157 -0.0441 0.0257 269 ASN B O 9289 C CB . ASN B 269 ? 0.8882 0.5381 0.8985 -0.1827 -0.0007 0.0217 269 ASN B CB 9290 C CG . ASN B 269 ? 0.9307 0.5659 0.9649 -0.1780 -0.0018 0.0013 269 ASN B CG 9291 O OD1 . ASN B 269 ? 1.1325 0.7429 1.1594 -0.1851 -0.0123 -0.0161 269 ASN B OD1 9292 N ND2 . ASN B 269 ? 0.8056 0.4532 0.8663 -0.1660 0.0086 0.0037 269 ASN B ND2 9293 N N . ASP B 270 ? 0.9710 0.5498 0.8976 -0.2107 -0.0206 -0.0306 270 ASP B N 9294 C CA . ASP B 270 ? 1.1544 0.7017 1.0563 -0.2277 -0.0450 -0.0388 270 ASP B CA 9295 C C . ASP B 270 ? 1.1638 0.7018 1.1043 -0.2305 -0.0635 -0.0360 270 ASP B C 9296 O O . ASP B 270 ? 1.2924 0.8057 1.2202 -0.2471 -0.0886 -0.0375 270 ASP B O 9297 C CB . ASP B 270 ? 1.2828 0.7889 1.1306 -0.2304 -0.0306 -0.0743 270 ASP B CB 9298 C CG . ASP B 270 ? 1.2409 0.7362 1.1065 -0.2148 -0.0051 -0.0996 270 ASP B CG 9299 O OD1 . ASP B 270 ? 1.2335 0.7578 1.1490 -0.2017 0.0025 -0.0892 270 ASP B OD1 9300 O OD2 . ASP B 270 ? 1.2208 0.6773 1.0495 -0.2154 0.0078 -0.1288 270 ASP B OD2 9301 N N . GLY B 271 ? 1.0569 0.6124 1.0421 -0.2154 -0.0523 -0.0313 271 GLY B N 9302 C CA . GLY B 271 ? 1.0119 0.5597 1.0357 -0.2158 -0.0676 -0.0255 271 GLY B CA 9303 C C . GLY B 271 ? 1.0589 0.5613 1.0676 -0.2182 -0.0688 -0.0562 271 GLY B C 9304 O O . GLY B 271 ? 1.1681 0.6515 1.1945 -0.2253 -0.0875 -0.0532 271 GLY B O 9305 N N . GLN B 272 ? 1.0905 0.5726 1.0656 -0.2118 -0.0465 -0.0851 272 GLN B N 9306 C CA . GLN B 272 ? 1.1789 0.6138 1.1369 -0.2099 -0.0401 -0.1157 272 GLN B CA 9307 C C . GLN B 272 ? 1.3170 0.7622 1.3170 -0.1873 -0.0176 -0.1250 272 GLN B C 9308 O O . GLN B 272 ? 1.4605 0.9472 1.4967 -0.1762 -0.0103 -0.1086 272 GLN B O 9309 C CB . GLN B 272 ? 1.2223 0.6225 1.1145 -0.2164 -0.0269 -0.1418 272 GLN B CB 9310 C CG . GLN B 272 ? 1.2959 0.6888 1.1431 -0.2388 -0.0508 -0.1309 272 GLN B CG 9311 C CD . GLN B 272 ? 1.6535 1.0255 1.5041 -0.2585 -0.0875 -0.1203 272 GLN B CD 9312 O OE1 . GLN B 272 ? 1.8554 1.2531 1.7172 -0.2724 -0.1131 -0.0925 272 GLN B OE1 9313 N NE2 . GLN B 272 ? 1.7298 1.0545 1.5728 -0.2598 -0.0895 -0.1415 272 GLN B NE2 9314 N N . CYS B 273 ? 1.2121 0.6175 1.2058 -0.1804 -0.0071 -0.1505 273 CYS B N 9315 C CA . CYS B 273 ? 1.1559 0.5721 1.1947 -0.1578 0.0131 -0.1581 273 CYS B CA 9316 C C . CYS B 273 ? 1.2555 0.6691 1.2773 -0.1461 0.0475 -0.1818 273 CYS B C 9317 O O . CYS B 273 ? 1.4789 0.8471 1.4618 -0.1462 0.0619 -0.2076 273 CYS B O 9318 C CB . CYS B 273 ? 1.1844 0.5610 1.2391 -0.1532 0.0056 -0.1674 273 CYS B CB 9319 S SG . CYS B 273 ? 1.4080 0.7919 1.5169 -0.1233 0.0315 -0.1787 273 CYS B SG 9320 N N . HIS B 274 ? 1.1959 0.6558 1.2452 -0.1369 0.0616 -0.1723 274 HIS B N 9321 C CA . HIS B 274 ? 1.2021 0.6682 1.2446 -0.1270 0.0950 -0.1906 274 HIS B CA 9322 C C . HIS B 274 ? 1.3012 0.7839 1.4029 -0.1055 0.1124 -0.1962 274 HIS B C 9323 O O . HIS B 274 ? 1.4667 0.9612 1.5774 -0.0958 0.1414 -0.2088 274 HIS B O 9324 C CB . HIS B 274 ? 1.2283 0.7320 1.2594 -0.1332 0.1002 -0.1773 274 HIS B CB 9325 C CG . HIS B 274 ? 1.2645 0.7568 1.2432 -0.1519 0.0834 -0.1685 274 HIS B CG 9326 N ND1 . HIS B 274 ? 1.3046 0.7589 1.2208 -0.1618 0.0905 -0.1864 274 HIS B ND1 9327 C CD2 . HIS B 274 ? 1.3088 0.8222 1.2891 -0.1620 0.0596 -0.1419 274 HIS B CD2 9328 C CE1 . HIS B 274 ? 1.4186 0.8743 1.3029 -0.1779 0.0686 -0.1704 274 HIS B CE1 9329 N NE2 . HIS B 274 ? 1.3915 0.8844 1.3171 -0.1775 0.0509 -0.1429 274 HIS B NE2 9330 N N . VAL B 275 ? 1.2455 0.7304 1.3900 -0.0983 0.0945 -0.1850 275 VAL B N 9331 C CA . VAL B 275 ? 1.1390 0.6406 1.3440 -0.0774 0.1061 -0.1866 275 VAL B CA 9332 C C . VAL B 275 ? 1.1901 0.6511 1.3885 -0.0644 0.1322 -0.2138 275 VAL B C 9333 O O . VAL B 275 ? 1.2548 0.6644 1.4208 -0.0683 0.1263 -0.2254 275 VAL B O 9334 C CB . VAL B 275 ? 1.1121 0.6206 1.3591 -0.0727 0.0791 -0.1662 275 VAL B CB 9335 C CG1 . VAL B 275 ? 0.9452 0.4725 1.2558 -0.0503 0.0886 -0.1659 275 VAL B CG1 9336 C CG2 . VAL B 275 ? 0.9024 0.4453 1.1515 -0.0840 0.0573 -0.1389 275 VAL B CG2 9337 N N . GLY B 276 ? 1.2051 0.6876 1.4343 -0.0493 0.1621 -0.2233 276 GLY B N 9338 C CA . GLY B 276 ? 1.3585 0.8044 1.5836 -0.0339 0.1945 -0.2482 276 GLY B CA 9339 C C . GLY B 276 ? 1.4489 0.8980 1.7408 -0.0104 0.1976 -0.2454 276 GLY B C 9340 O O . GLY B 276 ? 1.6093 1.0767 1.9391 -0.0087 0.1691 -0.2254 276 GLY B O 9341 N N . SER B 277 ? 1.3406 0.7704 1.6464 0.0090 0.2338 -0.2642 277 SER B N 9342 C CA . SER B 277 ? 1.3466 0.7791 1.7200 0.0351 0.2414 -0.2613 277 SER B CA 9343 C C . SER B 277 ? 1.2451 0.7525 1.7031 0.0456 0.2367 -0.2396 277 SER B C 9344 O O . SER B 277 ? 1.3363 0.8598 1.8593 0.0643 0.2294 -0.2278 277 SER B O 9345 C CB . SER B 277 ? 1.4840 0.8713 1.8460 0.0545 0.2865 -0.2872 277 SER B CB 9346 O OG . SER B 277 ? 1.4446 0.8575 1.8072 0.0563 0.3211 -0.2958 277 SER B OG 9347 N N . ASP B 278 ? 1.1463 0.6970 1.6010 0.0324 0.2392 -0.2339 278 ASP B N 9348 C CA . ASP B 278 ? 1.1094 0.7289 1.6356 0.0367 0.2325 -0.2142 278 ASP B CA 9349 C C . ASP B 278 ? 1.1008 0.7451 1.6331 0.0236 0.1883 -0.1891 278 ASP B C 9350 O O . ASP B 278 ? 1.0226 0.7179 1.6020 0.0228 0.1754 -0.1712 278 ASP B O 9351 C CB . ASP B 278 ? 1.2144 0.8640 1.7318 0.0275 0.2577 -0.2202 278 ASP B CB 9352 C CG . ASP B 278 ? 1.2762 0.9039 1.7093 0.0028 0.2516 -0.2256 278 ASP B CG 9353 O OD1 . ASP B 278 ? 1.0821 0.7418 1.5102 -0.0130 0.2294 -0.2091 278 ASP B OD1 9354 O OD2 . ASP B 278 ? 1.5065 1.0825 1.8765 -0.0004 0.2686 -0.2458 278 ASP B OD2 9355 N N . ASN B 279 ? 1.2950 0.8037 1.9652 -0.0650 0.3437 -0.2703 279 ASN B N 9356 C CA . ASN B 279 ? 1.2130 0.7094 1.8502 -0.0406 0.2943 -0.2317 279 ASN B CA 9357 C C . ASN B 279 ? 1.1989 0.6841 1.7647 -0.0306 0.2721 -0.2140 279 ASN B C 9358 O O . ASN B 279 ? 1.1903 0.6802 1.7684 -0.0068 0.2324 -0.1854 279 ASN B O 9359 C CB . ASN B 279 ? 1.0733 0.5897 1.8084 -0.0177 0.2614 -0.2108 279 ASN B CB 9360 C CG . ASN B 279 ? 1.0940 0.6221 1.9067 -0.0251 0.2783 -0.2242 279 ASN B CG 9361 O OD1 . ASN B 279 ? 1.0704 0.5857 1.8461 -0.0409 0.3009 -0.2374 279 ASN B OD1 9362 N ND2 . ASN B 279 ? 1.1484 0.7018 2.0730 -0.0148 0.2669 -0.2210 279 ASN B ND2 9363 N N . HIS B 280 ? 1.2099 0.6804 1.7008 -0.0511 0.2980 -0.2309 280 HIS B N 9364 C CA . HIS B 280 ? 1.1614 0.6201 1.5830 -0.0444 0.2801 -0.2159 280 HIS B CA 9365 C C . HIS B 280 ? 1.1010 0.5306 1.4185 -0.0648 0.2893 -0.2170 280 HIS B C 9366 O O . HIS B 280 ? 1.2218 0.6415 1.5122 -0.0922 0.3205 -0.2383 280 HIS B O 9367 C CB . HIS B 280 ? 1.2924 0.7637 1.7315 -0.0499 0.2987 -0.2326 280 HIS B CB 9368 C CG . HIS B 280 ? 1.4847 0.9833 2.0155 -0.0276 0.2802 -0.2250 280 HIS B CG 9369 N ND1 . HIS B 280 ? 1.6215 1.1394 2.2080 -0.0349 0.3045 -0.2467 280 HIS B ND1 9370 C CD2 . HIS B 280 ? 1.5414 1.0508 2.1162 -0.0013 0.2390 -0.1973 280 HIS B CD2 9371 C CE1 . HIS B 280 ? 1.6524 1.1921 2.3162 -0.0133 0.2777 -0.2328 280 HIS B CE1 9372 N NE2 . HIS B 280 ? 1.6106 1.1449 2.2661 0.0064 0.2371 -0.2023 280 HIS B NE2 9373 N N . TYR B 281 ? 1.0360 0.4528 1.2963 -0.0533 0.2620 -0.1939 281 TYR B N 9374 C CA . TYR B 281 ? 1.0820 0.4703 1.2443 -0.0738 0.2669 -0.1919 281 TYR B CA 9375 C C . TYR B 281 ? 1.1628 0.5433 1.2815 -0.0991 0.2940 -0.2115 281 TYR B C 9376 O O . TYR B 281 ? 1.3786 0.7671 1.5057 -0.0876 0.2862 -0.2069 281 TYR B O 9377 C CB . TYR B 281 ? 1.1090 0.4884 1.2352 -0.0527 0.2294 -0.1596 281 TYR B CB 9378 C CG . TYR B 281 ? 1.1170 0.4784 1.1465 -0.0707 0.2231 -0.1486 281 TYR B CG 9379 C CD1 . TYR B 281 ? 1.2491 0.5887 1.2263 -0.1059 0.2493 -0.1672 281 TYR B CD1 9380 C CD2 . TYR B 281 ? 1.0054 0.3865 0.9974 -0.0533 0.1849 -0.1166 281 TYR B CD2 9381 C CE1 . TYR B 281 ? 1.1072 0.4439 0.9982 -0.1219 0.2327 -0.1505 281 TYR B CE1 9382 C CE2 . TYR B 281 ? 1.0189 0.3980 0.9338 -0.0677 0.1713 -0.1027 281 TYR B CE2 9383 C CZ . TYR B 281 ? 1.0677 0.4243 0.9329 -0.1013 0.1927 -0.1177 281 TYR B CZ 9384 O OH . TYR B 281 ? 1.1388 0.4925 0.9318 -0.1165 0.1739 -0.1010 281 TYR B OH 9385 N N . SER B 282 ? 1.1196 0.4847 1.1887 -0.1357 0.3255 -0.2327 282 SER B N 9386 C CA . SER B 282 ? 1.1738 0.5306 1.1983 -0.1668 0.3550 -0.2524 282 SER B CA 9387 C C . SER B 282 ? 1.3384 0.6669 1.2671 -0.1794 0.3373 -0.2348 282 SER B C 9388 O O . SER B 282 ? 1.5282 0.8526 1.4336 -0.1891 0.3443 -0.2383 282 SER B O 9389 C CB . SER B 282 ? 1.2270 0.5789 1.2298 -0.2063 0.3964 -0.2812 282 SER B CB 9390 O OG . SER B 282 ? 1.2090 0.5342 1.1251 -0.2301 0.3900 -0.2737 282 SER B OG 9391 N N . ALA B 283 ? 1.2688 0.5773 1.1448 -0.1801 0.3130 -0.2145 283 ALA B N 9392 C CA . ALA B 283 ? 1.2946 0.5907 1.0829 -0.1923 0.2871 -0.1899 283 ALA B CA 9393 C C . ALA B 283 ? 1.1567 0.4812 0.9693 -0.1512 0.2455 -0.1575 283 ALA B C 9394 O O . ALA B 283 ? 1.2523 0.5824 1.0126 -0.1523 0.2161 -0.1318 283 ALA B O 9395 C CB . ALA B 283 ? 1.3637 0.6523 1.0896 -0.2110 0.2731 -0.1769 283 ALA B CB 9396 N N . SER B 284 ? 1.0949 0.4370 0.9902 -0.1174 0.2425 -0.1594 284 SER B N 9397 C CA . SER B 284 ? 1.0625 0.4322 0.9841 -0.0812 0.2066 -0.1329 284 SER B CA 9398 C C . SER B 284 ? 1.0646 0.4366 0.9505 -0.0859 0.1989 -0.1252 284 SER B C 9399 O O . SER B 284 ? 1.0150 0.4056 0.8843 -0.0698 0.1661 -0.0994 284 SER B O 9400 C CB . SER B 284 ? 1.1614 0.5435 1.1758 -0.0532 0.2090 -0.1404 284 SER B CB 9401 O OG . SER B 284 ? 1.1978 0.6061 1.2311 -0.0233 0.1755 -0.1164 284 SER B OG 9402 N N . THR B 285 ? 1.1362 0.4889 1.0145 -0.1095 0.2312 -0.1494 285 THR B N 9403 C CA . THR B 285 ? 1.0838 0.4334 0.9241 -0.1198 0.2272 -0.1433 285 THR B CA 9404 C C . THR B 285 ? 1.1320 0.4634 0.8806 -0.1546 0.2178 -0.1296 285 THR B C 9405 O O . THR B 285 ? 1.1449 0.4814 0.8621 -0.1546 0.1929 -0.1076 285 THR B O 9406 C CB . THR B 285 ? 1.1006 0.4349 0.9679 -0.1346 0.2671 -0.1755 285 THR B CB 9407 O OG1 . THR B 285 ? 1.3640 0.6675 1.1927 -0.1778 0.3055 -0.2029 285 THR B OG1 9408 C CG2 . THR B 285 ? 1.0586 0.4143 1.0265 -0.1018 0.2727 -0.1879 285 THR B CG2 9409 N N . THR B 286 ? 1.1710 0.4806 0.8805 -0.1857 0.2363 -0.1424 286 THR B N 9410 C CA . THR B 286 ? 1.2275 0.5132 0.8451 -0.2286 0.2314 -0.1332 286 THR B CA 9411 C C . THR B 286 ? 1.2212 0.5150 0.8024 -0.2243 0.1893 -0.1002 286 THR B C 9412 O O . THR B 286 ? 1.3392 0.6165 0.8508 -0.2554 0.1725 -0.0837 286 THR B O 9413 C CB . THR B 286 ? 1.3298 0.5851 0.9133 -0.2734 0.2751 -0.1664 286 THR B CB 9414 O OG1 . THR B 286 ? 1.2715 0.5305 0.8669 -0.2678 0.2734 -0.1683 286 THR B OG1 9415 C CG2 . THR B 286 ? 1.3618 0.6106 1.0021 -0.2755 0.3220 -0.2058 286 THR B CG2 9416 N N . MET B 287 ? 1.1732 0.4911 0.8018 -0.1884 0.1709 -0.0899 287 MET B N 9417 C CA . MET B 287 ? 1.1889 0.5150 0.7903 -0.1845 0.1343 -0.0625 287 MET B CA 9418 C C . MET B 287 ? 1.1187 0.4788 0.7755 -0.1396 0.1057 -0.0441 287 MET B C 9419 O O . MET B 287 ? 1.0658 0.4423 0.7815 -0.1116 0.1145 -0.0531 287 MET B O 9420 C CB . MET B 287 ? 1.2707 0.5824 0.8472 -0.2045 0.1466 -0.0727 287 MET B CB 9421 C CG . MET B 287 ? 1.3648 0.6905 1.0047 -0.1768 0.1589 -0.0849 287 MET B CG 9422 S SD . MET B 287 ? 1.3815 0.6922 0.9898 -0.1999 0.1671 -0.0922 287 MET B SD 9423 C CE . MET B 287 ? 1.2583 0.5315 0.7927 -0.2597 0.2013 -0.1167 287 MET B CE 9424 N N . ASP B 288 ? 1.0958 0.4654 0.7340 -0.1362 0.0709 -0.0190 288 ASP B N 9425 C CA . ASP B 288 ? 1.0684 0.4694 0.7511 -0.1011 0.0444 -0.0027 288 ASP B CA 9426 C C . ASP B 288 ? 1.0479 0.4645 0.7667 -0.0782 0.0453 -0.0055 288 ASP B C 9427 O O . ASP B 288 ? 1.0744 0.4778 0.7897 -0.0870 0.0647 -0.0187 288 ASP B O 9428 C CB . ASP B 288 ? 1.0811 0.4856 0.7411 -0.1085 0.0094 0.0217 288 ASP B CB 9429 C CG . ASP B 288 ? 1.0848 0.5194 0.7916 -0.0801 -0.0124 0.0335 288 ASP B CG 9430 O OD1 . ASP B 288 ? 1.1841 0.6406 0.9341 -0.0530 -0.0061 0.0263 288 ASP B OD1 9431 O OD2 . ASP B 288 ? 1.0293 0.4651 0.7313 -0.0872 -0.0367 0.0499 288 ASP B OD2 9432 N N . TYR B 289 ? 0.9762 0.4204 0.7302 -0.0513 0.0250 0.0062 289 TYR B N 9433 C CA . TYR B 289 ? 0.9387 0.3978 0.7204 -0.0327 0.0210 0.0080 289 TYR B CA 9434 C C . TYR B 289 ? 1.0850 0.5378 0.8386 -0.0443 0.0098 0.0162 289 TYR B C 9435 O O . TYR B 289 ? 1.2717 0.7207 0.9992 -0.0575 -0.0074 0.0271 289 TYR B O 9436 C CB . TYR B 289 ? 0.8844 0.3738 0.7029 -0.0076 0.0043 0.0164 289 TYR B CB 9437 C CG . TYR B 289 ? 0.8846 0.3825 0.7340 0.0051 0.0127 0.0090 289 TYR B CG 9438 C CD1 . TYR B 289 ? 0.8833 0.3863 0.7327 0.0044 0.0078 0.0106 289 TYR B CD1 9439 C CD2 . TYR B 289 ? 0.8732 0.3736 0.7570 0.0176 0.0233 0.0014 289 TYR B CD2 9440 C CE1 . TYR B 289 ? 0.8758 0.3870 0.7549 0.0161 0.0159 0.0028 289 TYR B CE1 9441 C CE2 . TYR B 289 ? 0.8548 0.3630 0.7714 0.0291 0.0287 -0.0052 289 TYR B CE2 9442 C CZ . TYR B 289 ? 0.8871 0.4012 0.7995 0.0285 0.0263 -0.0055 289 TYR B CZ 9443 O OH . TYR B 289 ? 0.8368 0.3590 0.7830 0.0400 0.0323 -0.0131 289 TYR B OH 9444 N N . PRO B 290 ? 1.0759 0.5269 0.8391 -0.0400 0.0176 0.0121 290 PRO B N 9445 C CA . PRO B 290 ? 1.0369 0.4823 0.7766 -0.0502 0.0087 0.0183 290 PRO B CA 9446 C C . PRO B 290 ? 1.0251 0.4926 0.7763 -0.0381 -0.0168 0.0328 290 PRO B C 9447 O O . PRO B 290 ? 1.0194 0.5083 0.8021 -0.0185 -0.0216 0.0353 290 PRO B O 9448 C CB . PRO B 290 ? 0.9684 0.4090 0.7284 -0.0447 0.0250 0.0095 290 PRO B CB 9449 C CG . PRO B 290 ? 0.9200 0.3746 0.7248 -0.0232 0.0284 0.0078 290 PRO B CG 9450 C CD . PRO B 290 ? 0.9578 0.4118 0.7605 -0.0254 0.0325 0.0031 290 PRO B CD 9451 N N . SER B 291 ? 0.9672 0.4289 0.6948 -0.0524 -0.0325 0.0410 291 SER B N 9452 C CA . SER B 291 ? 1.0108 0.4922 0.7584 -0.0434 -0.0538 0.0508 291 SER B CA 9453 C C . SER B 291 ? 1.2494 0.7383 1.0081 -0.0345 -0.0494 0.0489 291 SER B C 9454 O O . SER B 291 ? 1.2493 0.7239 0.9956 -0.0392 -0.0346 0.0432 291 SER B O 9455 C CB . SER B 291 ? 0.9490 0.4201 0.6774 -0.0622 -0.0752 0.0612 291 SER B CB 9456 O OG . SER B 291 ? 0.9497 0.3993 0.6423 -0.0812 -0.0710 0.0599 291 SER B OG 9457 N N . LEU B 292 ? 1.2955 0.8064 1.0797 -0.0237 -0.0604 0.0522 292 LEU B N 9458 C CA . LEU B 292 ? 1.0820 0.6001 0.8734 -0.0183 -0.0570 0.0515 292 LEU B CA 9459 C C . LEU B 292 ? 1.0419 0.5426 0.8115 -0.0315 -0.0573 0.0522 292 LEU B C 9460 O O . LEU B 292 ? 0.9686 0.4630 0.7342 -0.0305 -0.0468 0.0502 292 LEU B O 9461 C CB . LEU B 292 ? 0.9238 0.4671 0.7427 -0.0117 -0.0665 0.0512 292 LEU B CB 9462 C CG . LEU B 292 ? 0.8774 0.4403 0.7132 -0.0001 -0.0607 0.0485 292 LEU B CG 9463 C CD1 . LEU B 292 ? 1.1518 0.7159 0.9930 0.0067 -0.0582 0.0476 292 LEU B CD1 9464 C CD2 . LEU B 292 ? 0.8781 0.4649 0.7384 -0.0004 -0.0657 0.0430 292 LEU B CD2 9465 N N . GLY B 293 ? 1.1147 0.6071 0.8726 -0.0450 -0.0715 0.0564 293 GLY B N 9466 C CA . GLY B 293 ? 1.1060 0.5813 0.8402 -0.0608 -0.0749 0.0576 293 GLY B CA 9467 C C . GLY B 293 ? 1.0165 0.4698 0.7208 -0.0711 -0.0547 0.0502 293 GLY B C 9468 O O . GLY B 293 ? 1.0090 0.4561 0.7095 -0.0728 -0.0452 0.0460 293 GLY B O 9469 N N . LEU B 294 ? 1.0359 0.4773 0.7229 -0.0791 -0.0460 0.0465 294 LEU B N 9470 C CA . LEU B 294 ? 1.0689 0.4892 0.7343 -0.0921 -0.0217 0.0338 294 LEU B CA 9471 C C . LEU B 294 ? 1.0578 0.4844 0.7559 -0.0740 -0.0033 0.0266 294 LEU B C 9472 O O . LEU B 294 ? 1.0713 0.4843 0.7679 -0.0815 0.0147 0.0164 294 LEU B O 9473 C CB . LEU B 294 ? 1.0110 0.4184 0.6554 -0.1057 -0.0132 0.0287 294 LEU B CB 9474 C CG . LEU B 294 ? 1.0498 0.4339 0.6728 -0.1256 0.0169 0.0099 294 LEU B CG 9475 C CD1 . LEU B 294 ? 1.0890 0.4537 0.6678 -0.1550 0.0159 0.0075 294 LEU B CD1 9476 C CD2 . LEU B 294 ? 1.3484 0.7220 0.9578 -0.1371 0.0301 0.0017 294 LEU B CD2 9477 N N . MET B 295 ? 1.0362 0.4830 0.7660 -0.0523 -0.0092 0.0323 295 MET B N 9478 C CA . MET B 295 ? 1.0505 0.5032 0.8119 -0.0369 -0.0001 0.0315 295 MET B CA 9479 C C . MET B 295 ? 1.0329 0.4870 0.7957 -0.0364 -0.0038 0.0362 295 MET B C 9480 O O . MET B 295 ? 1.0090 0.4539 0.7862 -0.0356 0.0080 0.0330 295 MET B O 9481 C CB . MET B 295 ? 1.0450 0.5187 0.8316 -0.0188 -0.0093 0.0384 295 MET B CB 9482 C CG . MET B 295 ? 1.0525 0.5246 0.8493 -0.0155 -0.0016 0.0324 295 MET B CG 9483 S SD . MET B 295 ? 1.1548 0.6498 0.9864 0.0051 -0.0106 0.0396 295 MET B SD 9484 C CE . MET B 295 ? 1.1049 0.6232 0.9273 0.0070 -0.0294 0.0478 295 MET B CE 9485 N N . THR B 296 ? 1.1858 0.6510 0.9398 -0.0374 -0.0198 0.0429 296 THR B N 9486 C CA . THR B 296 ? 1.1701 0.6369 0.9246 -0.0385 -0.0229 0.0460 296 THR B CA 9487 C C . THR B 296 ? 1.0849 0.5308 0.8218 -0.0533 -0.0123 0.0390 296 THR B C 9488 O O . THR B 296 ? 1.0767 0.5173 0.8236 -0.0518 -0.0037 0.0381 296 THR B O 9489 C CB . THR B 296 ? 1.0592 0.5407 0.8147 -0.0398 -0.0400 0.0500 296 THR B CB 9490 O OG1 . THR B 296 ? 0.9572 0.4602 0.7327 -0.0281 -0.0450 0.0528 296 THR B OG1 9491 C CG2 . THR B 296 ? 1.1400 0.6197 0.8945 -0.0446 -0.0408 0.0501 296 THR B CG2 9492 N N . GLU B 297 ? 1.0401 0.4733 0.7495 -0.0700 -0.0136 0.0344 297 GLU B N 9493 C CA . GLU B 297 ? 1.1030 0.5158 0.7878 -0.0900 -0.0034 0.0256 297 GLU B CA 9494 C C . GLU B 297 ? 1.2338 0.6341 0.9329 -0.0911 0.0234 0.0126 297 GLU B C 9495 O O . GLU B 297 ? 1.5720 0.9662 1.2807 -0.0930 0.0330 0.0081 297 GLU B O 9496 C CB . GLU B 297 ? 1.1578 0.5571 0.8032 -0.1133 -0.0108 0.0244 297 GLU B CB 9497 C CG . GLU B 297 ? 1.2325 0.6096 0.8430 -0.1407 0.0001 0.0138 297 GLU B CG 9498 C CD . GLU B 297 ? 1.4814 0.8412 1.0438 -0.1702 -0.0060 0.0134 297 GLU B CD 9499 O OE1 . GLU B 297 ? 1.4565 0.8144 1.0144 -0.1711 -0.0006 0.0119 297 GLU B OE1 9500 O OE2 . GLU B 297 ? 1.7364 1.0834 1.2636 -0.1946 -0.0175 0.0157 297 GLU B OE2 9501 N N . LYS B 298 ? 1.1498 0.5465 0.8577 -0.0897 0.0357 0.0055 298 LYS B N 9502 C CA . LYS B 298 ? 1.1226 0.5067 0.8565 -0.0925 0.0628 -0.0105 298 LYS B CA 9503 C C . LYS B 298 ? 1.0877 0.4800 0.8716 -0.0714 0.0628 -0.0034 298 LYS B C 9504 O O . LYS B 298 ? 0.9976 0.3788 0.8124 -0.0741 0.0815 -0.0144 298 LYS B O 9505 C CB . LYS B 298 ? 1.1158 0.4954 0.8543 -0.0953 0.0753 -0.0204 298 LYS B CB 9506 C CG . LYS B 298 ? 1.0656 0.4223 0.7769 -0.1257 0.1017 -0.0435 298 LYS B CG 9507 C CD . LYS B 298 ? 1.2325 0.5800 0.8784 -0.1517 0.0890 -0.0394 298 LYS B CD 9508 C CE . LYS B 298 ? 1.4089 0.7319 1.0167 -0.1891 0.1163 -0.0629 298 LYS B CE 9509 N NZ . LYS B 298 ? 1.5316 0.8431 1.0699 -0.2191 0.0980 -0.0543 298 LYS B NZ 9510 N N . LEU B 299 ? 1.0573 0.4682 0.8504 -0.0533 0.0416 0.0148 299 LEU B N 9511 C CA . LEU B 299 ? 1.0404 0.4579 0.8716 -0.0377 0.0362 0.0264 299 LEU B CA 9512 C C . LEU B 299 ? 1.0615 0.4721 0.8953 -0.0426 0.0391 0.0278 299 LEU B C 9513 O O . LEU B 299 ? 1.0511 0.4549 0.9231 -0.0382 0.0453 0.0298 299 LEU B O 9514 C CB . LEU B 299 ? 1.0168 0.4553 0.8446 -0.0247 0.0145 0.0433 299 LEU B CB 9515 C CG . LEU B 299 ? 0.9093 0.3552 0.7719 -0.0110 0.0073 0.0539 299 LEU B CG 9516 C CD1 . LEU B 299 ? 0.9148 0.3525 0.8034 -0.0091 0.0202 0.0423 299 LEU B CD1 9517 C CD2 . LEU B 299 ? 0.8924 0.3595 0.7404 -0.0046 -0.0105 0.0651 299 LEU B CD2 9518 N N . SER B 300 ? 1.0464 0.4582 0.8445 -0.0520 0.0331 0.0274 300 SER B N 9519 C CA . SER B 300 ? 1.1413 0.5476 0.9393 -0.0570 0.0353 0.0281 300 SER B CA 9520 C C . SER B 300 ? 1.1650 0.5520 0.9653 -0.0726 0.0578 0.0096 300 SER B C 9521 O O . SER B 300 ? 1.3759 0.7559 1.1968 -0.0738 0.0659 0.0079 300 SER B O 9522 C CB . SER B 300 ? 1.2492 0.6645 1.0161 -0.0618 0.0202 0.0328 300 SER B CB 9523 O OG . SER B 300 ? 1.4399 0.8478 1.1753 -0.0774 0.0197 0.0236 300 SER B OG 9524 N N . GLN B 301 ? 1.1256 0.5035 0.9039 -0.0873 0.0689 -0.0053 301 GLN B N 9525 C CA . GLN B 301 ? 1.2011 0.5602 0.9750 -0.1087 0.0945 -0.0279 301 GLN B CA 9526 C C . GLN B 301 ? 1.2354 0.5872 1.0702 -0.1025 0.1162 -0.0383 301 GLN B C 9527 O O . GLN B 301 ? 1.3057 0.6457 1.1578 -0.1142 0.1361 -0.0538 301 GLN B O 9528 C CB . GLN B 301 ? 1.2917 0.6412 1.0248 -0.1302 0.1028 -0.0413 301 GLN B CB 9529 C CG . GLN B 301 ? 1.6226 0.9747 1.3004 -0.1418 0.0791 -0.0306 301 GLN B CG 9530 C CD . GLN B 301 ? 1.9646 1.3100 1.6175 -0.1576 0.0751 -0.0326 301 GLN B CD 9531 O OE1 . GLN B 301 ? 2.1113 1.4450 1.7723 -0.1698 0.0973 -0.0491 301 GLN B OE1 9532 N NE2 . GLN B 301 ? 1.9839 1.3370 1.6129 -0.1578 0.0468 -0.0171 301 GLN B NE2 9533 N N . LYS B 302 ? 1.1927 0.5515 1.0657 -0.0847 0.1112 -0.0300 302 LYS B N 9534 C CA . LYS B 302 ? 1.1029 0.4552 1.0474 -0.0771 0.1259 -0.0365 302 LYS B CA 9535 C C . LYS B 302 ? 1.0971 0.4561 1.0788 -0.0587 0.1059 -0.0118 302 LYS B C 9536 O O . LYS B 302 ? 1.1893 0.5431 1.2377 -0.0505 0.1092 -0.0096 302 LYS B O 9537 C CB . LYS B 302 ? 1.0271 0.3812 0.9986 -0.0703 0.1302 -0.0414 302 LYS B CB 9538 C CG . LYS B 302 ? 1.0311 0.3753 0.9682 -0.0922 0.1535 -0.0671 302 LYS B CG 9539 C CD . LYS B 302 ? 1.0696 0.3954 1.0277 -0.1156 0.1905 -0.0994 302 LYS B CD 9540 C CE . LYS B 302 ? 1.2910 0.6047 1.2116 -0.1431 0.2165 -0.1265 302 LYS B CE 9541 N NZ . LYS B 302 ? 1.4494 0.7452 1.3937 -0.1705 0.2586 -0.1639 302 LYS B NZ 9542 N N . ASN B 303 ? 1.0494 0.4187 0.9902 -0.0548 0.0848 0.0066 303 ASN B N 9543 C CA . ASN B 303 ? 1.0493 0.4244 1.0095 -0.0428 0.0653 0.0311 303 ASN B CA 9544 C C . ASN B 303 ? 1.0572 0.4380 1.0557 -0.0284 0.0491 0.0491 303 ASN B C 9545 O O . ASN B 303 ? 1.0522 0.4275 1.0981 -0.0228 0.0406 0.0639 303 ASN B O 9546 C CB . ASN B 303 ? 1.0801 0.4422 1.0766 -0.0477 0.0770 0.0272 303 ASN B CB 9547 C CG . ASN B 303 ? 1.1074 0.4659 1.0622 -0.0619 0.0872 0.0142 303 ASN B CG 9548 O OD1 . ASN B 303 ? 1.1654 0.5117 1.1303 -0.0756 0.1111 -0.0088 303 ASN B OD1 9549 N ND2 . ASN B 303 ? 1.1641 0.5331 1.0744 -0.0608 0.0700 0.0271 303 ASN B ND2 9550 N N . ILE B 304 ? 1.1023 0.4935 1.0814 -0.0237 0.0425 0.0493 304 ILE B N 9551 C CA . ILE B 304 ? 1.0812 0.4789 1.0919 -0.0116 0.0260 0.0651 304 ILE B CA 9552 C C . ILE B 304 ? 1.0092 0.4245 0.9784 -0.0076 0.0020 0.0853 304 ILE B C 9553 O O . ILE B 304 ? 0.9682 0.3942 0.8913 -0.0105 0.0020 0.0790 304 ILE B O 9554 C CB . ILE B 304 ? 1.0508 0.4475 1.0788 -0.0096 0.0388 0.0480 304 ILE B CB 9555 C CG1 . ILE B 304 ? 1.1736 0.5526 1.2506 -0.0173 0.0674 0.0235 304 ILE B CG1 9556 C CG2 . ILE B 304 ? 0.9932 0.3986 1.0518 0.0031 0.0187 0.0651 304 ILE B CG2 9557 C CD1 . ILE B 304 ? 1.2391 0.6147 1.3365 -0.0191 0.0850 0.0028 304 ILE B CD1 9558 N N . ASN B 305 ? 1.0001 0.4175 0.9884 -0.0038 -0.0188 0.1092 305 ASN B N 9559 C CA . ASN B 305 ? 1.0869 0.5204 1.0361 -0.0052 -0.0388 0.1260 305 ASN B CA 9560 C C . ASN B 305 ? 1.1617 0.6057 1.1199 0.0019 -0.0501 0.1305 305 ASN B C 9561 O O . ASN B 305 ? 1.2328 0.6697 1.2398 0.0077 -0.0579 0.1384 305 ASN B O 9562 C CB . ASN B 305 ? 1.0425 0.4712 0.9932 -0.0119 -0.0563 0.1508 305 ASN B CB 9563 C CG . ASN B 305 ? 1.1474 0.5710 1.0747 -0.0201 -0.0463 0.1465 305 ASN B CG 9564 O OD1 . ASN B 305 ? 1.3228 0.7313 1.2805 -0.0219 -0.0435 0.1514 305 ASN B OD1 9565 N ND2 . ASN B 305 ? 1.2345 0.6707 1.1144 -0.0252 -0.0412 0.1366 305 ASN B ND2 9566 N N . LEU B 306 ? 1.0195 0.4806 0.9373 0.0012 -0.0514 0.1248 306 LEU B N 9567 C CA . LEU B 306 ? 0.9923 0.4655 0.9151 0.0073 -0.0605 0.1267 306 LEU B CA 9568 C C . LEU B 306 ? 1.0507 0.5359 0.9528 0.0001 -0.0823 0.1469 306 LEU B C 9569 O O . LEU B 306 ? 1.0659 0.5595 0.9289 -0.0105 -0.0831 0.1484 306 LEU B O 9570 C CB . LEU B 306 ? 0.9652 0.4496 0.8624 0.0094 -0.0485 0.1074 306 LEU B CB 9571 C CG . LEU B 306 ? 0.9395 0.4364 0.8446 0.0166 -0.0539 0.1054 306 LEU B CG 9572 C CD1 . LEU B 306 ? 0.9312 0.4159 0.8859 0.0247 -0.0510 0.1039 306 LEU B CD1 9573 C CD2 . LEU B 306 ? 0.9679 0.4742 0.8488 0.0168 -0.0440 0.0890 306 LEU B CD2 9574 N N . ILE B 307 ? 1.0560 0.5412 0.9851 0.0033 -0.0996 0.1611 307 ILE B N 9575 C CA . ILE B 307 ? 1.0306 0.5255 0.9355 -0.0085 -0.1226 0.1816 307 ILE B CA 9576 C C . ILE B 307 ? 1.0987 0.6095 1.0042 -0.0038 -0.1290 0.1775 307 ILE B C 9577 O O . ILE B 307 ? 1.1851 0.6915 1.1343 0.0090 -0.1299 0.1745 307 ILE B O 9578 C CB . ILE B 307 ? 1.0282 0.5066 0.9627 -0.0147 -0.1475 0.2111 307 ILE B CB 9579 C CG1 . ILE B 307 ? 1.2923 0.7540 1.2342 -0.0183 -0.1405 0.2151 307 ILE B CG1 9580 C CG2 . ILE B 307 ? 1.0402 0.5265 0.9354 -0.0342 -0.1731 0.2340 307 ILE B CG2 9581 C CD1 . ILE B 307 ? 1.5102 0.9552 1.5178 -0.0044 -0.1287 0.2061 307 ILE B CD1 9582 N N . PHE B 308 ? 1.0889 0.6184 0.9497 -0.0155 -0.1311 0.1749 308 PHE B N 9583 C CA . PHE B 308 ? 1.0499 0.5965 0.9090 -0.0134 -0.1367 0.1702 308 PHE B CA 9584 C C . PHE B 308 ? 1.1064 0.6552 0.9532 -0.0296 -0.1648 0.1946 308 PHE B C 9585 O O . PHE B 308 ? 1.3328 0.8868 1.1337 -0.0521 -0.1705 0.2023 308 PHE B O 9586 C CB . PHE B 308 ? 1.1224 0.6901 0.9485 -0.0174 -0.1196 0.1480 308 PHE B CB 9587 C CG . PHE B 308 ? 1.1976 0.7642 1.0371 -0.0028 -0.0988 0.1269 308 PHE B CG 9588 C CD1 . PHE B 308 ? 1.1281 0.7003 0.9888 0.0105 -0.0931 0.1151 308 PHE B CD1 9589 C CD2 . PHE B 308 ? 1.2917 0.8507 1.1203 -0.0051 -0.0865 0.1199 308 PHE B CD2 9590 C CE1 . PHE B 308 ? 1.0211 0.5895 0.8869 0.0187 -0.0769 0.0989 308 PHE B CE1 9591 C CE2 . PHE B 308 ? 1.2263 0.7823 1.0618 0.0037 -0.0719 0.1036 308 PHE B CE2 9592 C CZ . PHE B 308 ? 1.0632 0.6231 0.9148 0.0143 -0.0678 0.0941 308 PHE B CZ 9593 N N . ALA B 309 ? 1.0786 0.6223 0.9664 -0.0209 -0.1826 0.2065 309 ALA B N 9594 C CA . ALA B 309 ? 1.1704 0.7169 1.0470 -0.0374 -0.2139 0.2306 309 ALA B CA 9595 C C . ALA B 309 ? 1.1907 0.7561 1.0732 -0.0309 -0.2137 0.2180 309 ALA B C 9596 O O . ALA B 309 ? 1.1820 0.7437 1.1172 -0.0111 -0.2137 0.2131 309 ALA B O 9597 C CB . ALA B 309 ? 1.0527 0.5768 0.9809 -0.0351 -0.2425 0.2598 309 ALA B CB 9598 N N . VAL B 310 ? 1.1453 0.7307 0.9766 -0.0492 -0.2113 0.2105 310 VAL B N 9599 C CA . VAL B 310 ? 1.0756 0.6816 0.9118 -0.0430 -0.2057 0.1935 310 VAL B CA 9600 C C . VAL B 310 ? 1.1466 0.7664 0.9418 -0.0706 -0.2254 0.2038 310 VAL B C 9601 O O . VAL B 310 ? 1.3122 0.9247 1.0673 -0.0981 -0.2433 0.2246 310 VAL B O 9602 C CB . VAL B 310 ? 1.0444 0.6668 0.8694 -0.0343 -0.1719 0.1608 310 VAL B CB 9603 C CG1 . VAL B 310 ? 0.9943 0.6034 0.8565 -0.0095 -0.1543 0.1499 310 VAL B CG1 9604 C CG2 . VAL B 310 ? 1.0765 0.7068 0.8514 -0.0572 -0.1602 0.1536 310 VAL B CG2 9605 N N . THR B 311 ? 1.1605 0.7995 0.9627 -0.0659 -0.2213 0.1885 311 THR B N 9606 C CA . THR B 311 ? 1.2302 0.8843 0.9946 -0.0934 -0.2379 0.1941 311 THR B CA 9607 C C . THR B 311 ? 1.2915 0.9633 0.9971 -0.1208 -0.2153 0.1736 311 THR B C 9608 O O . THR B 311 ? 1.2812 0.9613 0.9925 -0.1098 -0.1845 0.1479 311 THR B O 9609 C CB . THR B 311 ? 1.3263 0.9961 1.1234 -0.0785 -0.2388 0.1817 311 THR B CB 9610 O OG1 . THR B 311 ? 1.1525 0.8091 1.0156 -0.0447 -0.2382 0.1824 311 THR B OG1 9611 C CG2 . THR B 311 ? 1.6574 1.3305 1.4346 -0.1032 -0.2734 0.2031 311 THR B CG2 9612 N N . GLU B 312 ? 1.3720 1.0489 1.0237 -0.1591 -0.2311 0.1844 312 GLU B N 9613 C CA . GLU B 312 ? 1.4703 1.1618 1.0638 -0.1935 -0.2083 0.1640 312 GLU B CA 9614 C C . GLU B 312 ? 1.5048 1.2236 1.1160 -0.1835 -0.1705 0.1212 312 GLU B C 9615 O O . GLU B 312 ? 1.6833 1.4103 1.2806 -0.1941 -0.1422 0.0979 312 GLU B O 9616 C CB . GLU B 312 ? 1.6139 1.3085 1.1457 -0.2400 -0.2311 0.1792 312 GLU B CB 9617 C CG . GLU B 312 ? 1.8676 1.5756 1.3347 -0.2836 -0.2046 0.1557 312 GLU B CG 9618 C CD . GLU B 312 ? 2.2274 1.9375 1.6243 -0.3360 -0.2261 0.1694 312 GLU B CD 9619 O OE1 . GLU B 312 ? 2.2829 1.9845 1.6845 -0.3362 -0.2657 0.1996 312 GLU B OE1 9620 O OE2 . GLU B 312 ? 2.4114 2.1308 1.7489 -0.3794 -0.2032 0.1490 312 GLU B OE2 9621 N N . ASN B 313 ? 1.3749 1.1071 1.0234 -0.1632 -0.1710 0.1112 313 ASN B N 9622 C CA . ASN B 313 ? 1.3215 1.0789 0.9960 -0.1526 -0.1394 0.0736 313 ASN B CA 9623 C C . ASN B 313 ? 1.2622 1.0150 0.9752 -0.1236 -0.1174 0.0598 313 ASN B C 9624 O O . ASN B 313 ? 1.2677 1.0363 0.9881 -0.1284 -0.0905 0.0316 313 ASN B O 9625 C CB . ASN B 313 ? 1.2774 1.0466 0.9866 -0.1349 -0.1478 0.0702 313 ASN B CB 9626 C CG . ASN B 313 ? 1.1996 0.9481 0.9538 -0.1000 -0.1672 0.0923 313 ASN B CG 9627 O OD1 . ASN B 313 ? 1.1261 0.8693 0.9201 -0.0701 -0.1524 0.0831 313 ASN B OD1 9628 N ND2 . ASN B 313 ? 1.2106 0.9466 0.9610 -0.1064 -0.2007 0.1210 313 ASN B ND2 9629 N N . VAL B 314 ? 1.2003 0.9309 0.9409 -0.0959 -0.1296 0.0792 314 VAL B N 9630 C CA . VAL B 314 ? 1.1389 0.8623 0.9129 -0.0696 -0.1126 0.0688 314 VAL B CA 9631 C C . VAL B 314 ? 1.1482 0.8548 0.9023 -0.0766 -0.1093 0.0771 314 VAL B C 9632 O O . VAL B 314 ? 1.1182 0.8159 0.8937 -0.0587 -0.0982 0.0714 314 VAL B O 9633 C CB . VAL B 314 ? 1.0684 0.7779 0.8850 -0.0380 -0.1215 0.0787 314 VAL B CB 9634 C CG1 . VAL B 314 ? 1.1547 0.8373 0.9735 -0.0337 -0.1407 0.1062 314 VAL B CG1 9635 C CG2 . VAL B 314 ? 1.2016 0.9110 1.0486 -0.0163 -0.1017 0.0613 314 VAL B CG2 9636 N N . VAL B 315 ? 1.1888 0.8903 0.8991 -0.1052 -0.1199 0.0910 315 VAL B N 9637 C CA . VAL B 315 ? 1.1862 0.8712 0.8750 -0.1147 -0.1176 0.1002 315 VAL B CA 9638 C C . VAL B 315 ? 1.2529 0.9479 0.9486 -0.1151 -0.0889 0.0727 315 VAL B C 9639 O O . VAL B 315 ? 1.3921 1.0735 1.1046 -0.0991 -0.0838 0.0744 315 VAL B O 9640 C CB . VAL B 315 ? 1.2279 0.9074 0.8606 -0.1530 -0.1322 0.1181 315 VAL B CB 9641 C CG1 . VAL B 315 ? 1.2312 0.9017 0.8372 -0.1694 -0.1188 0.1155 315 VAL B CG1 9642 C CG2 . VAL B 315 ? 1.4915 1.1504 1.1268 -0.1502 -0.1682 0.1554 315 VAL B CG2 9643 N N . ASN B 316 ? 1.2077 0.9265 0.8957 -0.1344 -0.0705 0.0463 316 ASN B N 9644 C CA . ASN B 316 ? 1.1821 0.9121 0.8879 -0.1379 -0.0442 0.0182 316 ASN B CA 9645 C C . ASN B 316 ? 1.1519 0.8795 0.9096 -0.1040 -0.0399 0.0115 316 ASN B C 9646 O O . ASN B 316 ? 1.1682 0.8923 0.9425 -0.1004 -0.0290 0.0018 316 ASN B O 9647 C CB . ASN B 316 ? 1.2069 0.9651 0.9114 -0.1635 -0.0234 -0.0132 316 ASN B CB 9648 C CG . ASN B 316 ? 1.3813 1.1409 1.0238 -0.2070 -0.0226 -0.0111 316 ASN B CG 9649 O OD1 . ASN B 316 ? 1.5424 1.3050 1.1547 -0.2215 -0.0377 0.0005 316 ASN B OD1 9650 N ND2 . ASN B 316 ? 1.4921 1.2485 1.1135 -0.2307 -0.0057 -0.0219 316 ASN B ND2 9651 N N . LEU B 317 ? 1.0692 0.7975 0.8509 -0.0818 -0.0496 0.0171 317 LEU B N 9652 C CA . LEU B 317 ? 1.0057 0.7273 0.8268 -0.0537 -0.0485 0.0151 317 LEU B CA 9653 C C . LEU B 317 ? 0.9780 0.6734 0.7929 -0.0430 -0.0546 0.0318 317 LEU B C 9654 O O . LEU B 317 ? 1.0921 0.7837 0.9193 -0.0403 -0.0468 0.0241 317 LEU B O 9655 C CB . LEU B 317 ? 0.9878 0.7110 0.8281 -0.0356 -0.0575 0.0202 317 LEU B CB 9656 C CG . LEU B 317 ? 0.8699 0.5834 0.7425 -0.0116 -0.0562 0.0192 317 LEU B CG 9657 C CD1 . LEU B 317 ? 0.8521 0.5808 0.7550 -0.0126 -0.0443 -0.0014 317 LEU B CD1 9658 C CD2 . LEU B 317 ? 0.8518 0.5641 0.7400 0.0038 -0.0631 0.0243 317 LEU B CD2 9659 N N . TYR B 318 ? 0.9602 0.6380 0.7616 -0.0378 -0.0693 0.0541 318 TYR B N 9660 C CA . TYR B 318 ? 0.9480 0.6010 0.7491 -0.0284 -0.0734 0.0684 318 TYR B CA 9661 C C . TYR B 318 ? 0.9825 0.6301 0.7599 -0.0449 -0.0685 0.0694 318 TYR B C 9662 O O . TYR B 318 ? 0.9449 0.5767 0.7262 -0.0383 -0.0658 0.0729 318 TYR B O 9663 C CB . TYR B 318 ? 0.9597 0.5967 0.7642 -0.0216 -0.0899 0.0901 318 TYR B CB 9664 C CG . TYR B 318 ? 0.9483 0.5852 0.7834 -0.0025 -0.0914 0.0872 318 TYR B CG 9665 C CD1 . TYR B 318 ? 0.9667 0.6177 0.8072 -0.0035 -0.0993 0.0871 318 TYR B CD1 9666 C CD2 . TYR B 318 ? 0.9500 0.5722 0.8059 0.0135 -0.0834 0.0830 318 TYR B CD2 9667 C CE1 . TYR B 318 ? 0.9886 0.6393 0.8593 0.0136 -0.0990 0.0831 318 TYR B CE1 9668 C CE2 . TYR B 318 ? 0.9074 0.5281 0.7885 0.0274 -0.0816 0.0783 318 TYR B CE2 9669 C CZ . TYR B 318 ? 0.9112 0.5463 0.8020 0.0288 -0.0891 0.0783 318 TYR B CZ 9670 O OH . TYR B 318 ? 0.8876 0.5209 0.8057 0.0424 -0.0858 0.0724 318 TYR B OH 9671 N N . GLN B 319 ? 1.1334 0.7941 0.8847 -0.0690 -0.0656 0.0649 319 GLN B N 9672 C CA . GLN B 319 ? 1.2797 0.9377 1.0085 -0.0885 -0.0564 0.0608 319 GLN B CA 9673 C C . GLN B 319 ? 1.1941 0.8600 0.9511 -0.0823 -0.0396 0.0380 319 GLN B C 9674 O O . GLN B 319 ? 1.1305 0.7855 0.8862 -0.0839 -0.0348 0.0379 319 GLN B O 9675 C CB . GLN B 319 ? 1.3734 1.0447 1.0654 -0.1212 -0.0527 0.0558 319 GLN B CB 9676 C CG . GLN B 319 ? 1.4841 1.1484 1.1444 -0.1465 -0.0437 0.0550 319 GLN B CG 9677 C CD . GLN B 319 ? 1.6385 1.3138 1.2530 -0.1856 -0.0388 0.0496 319 GLN B CD 9678 O OE1 . GLN B 319 ? 1.6732 1.3679 1.2875 -0.1947 -0.0341 0.0353 319 GLN B OE1 9679 N NE2 . GLN B 319 ? 1.6960 1.3579 1.2685 -0.2117 -0.0391 0.0605 319 GLN B NE2 9680 N N . ASN B 320 ? 1.1727 0.8570 0.9598 -0.0755 -0.0330 0.0198 320 ASN B N 9681 C CA . ASN B 320 ? 1.1953 0.8867 1.0207 -0.0689 -0.0231 0.0012 320 ASN B CA 9682 C C . ASN B 320 ? 1.1360 0.8089 0.9769 -0.0462 -0.0330 0.0127 320 ASN B C 9683 O O . ASN B 320 ? 1.1732 0.8410 1.0318 -0.0441 -0.0311 0.0072 320 ASN B O 9684 C CB . ASN B 320 ? 1.2333 0.9500 1.0927 -0.0706 -0.0147 -0.0207 320 ASN B CB 9685 C CG . ASN B 320 ? 1.3229 1.0599 1.1830 -0.0982 0.0047 -0.0453 320 ASN B CG 9686 O OD1 . ASN B 320 ? 1.3724 1.1042 1.2143 -0.1150 0.0134 -0.0490 320 ASN B OD1 9687 N ND2 . ASN B 320 ? 1.4648 1.2250 1.3472 -0.1049 0.0140 -0.0648 320 ASN B ND2 9688 N N . TYR B 321 ? 1.0880 0.7504 0.9229 -0.0321 -0.0430 0.0275 321 TYR B N 9689 C CA . TYR B 321 ? 1.0192 0.6614 0.8602 -0.0164 -0.0487 0.0368 321 TYR B CA 9690 C C . TYR B 321 ? 1.0539 0.6764 0.8773 -0.0198 -0.0487 0.0461 321 TYR B C 9691 O O . TYR B 321 ? 1.1506 0.7614 0.9798 -0.0160 -0.0486 0.0450 321 TYR B O 9692 C CB . TYR B 321 ? 1.0818 0.7162 0.9227 -0.0041 -0.0550 0.0472 321 TYR B CB 9693 C CG . TYR B 321 ? 0.9684 0.6123 0.8319 0.0055 -0.0550 0.0392 321 TYR B CG 9694 C CD1 . TYR B 321 ? 0.8793 0.5165 0.7562 0.0104 -0.0553 0.0352 321 TYR B CD1 9695 C CD2 . TYR B 321 ? 1.0073 0.6655 0.8773 0.0078 -0.0568 0.0374 321 TYR B CD2 9696 C CE1 . TYR B 321 ? 0.9127 0.5565 0.8094 0.0173 -0.0569 0.0305 321 TYR B CE1 9697 C CE2 . TYR B 321 ? 0.9700 0.6365 0.8625 0.0167 -0.0562 0.0300 321 TYR B CE2 9698 C CZ . TYR B 321 ? 0.9769 0.6358 0.8829 0.0215 -0.0560 0.0271 321 TYR B CZ 9699 O OH . TYR B 321 ? 0.9878 0.6530 0.9154 0.0284 -0.0569 0.0222 321 TYR B OH 9700 N N . SER B 322 ? 1.0647 0.6832 0.8659 -0.0291 -0.0504 0.0563 322 SER B N 9701 C CA . SER B 322 ? 1.0908 0.6902 0.8779 -0.0326 -0.0509 0.0671 322 SER B CA 9702 C C . SER B 322 ? 1.1001 0.7006 0.8890 -0.0405 -0.0427 0.0557 322 SER B C 9703 O O . SER B 322 ? 1.1450 0.7290 0.9309 -0.0385 -0.0421 0.0604 322 SER B O 9704 C CB . SER B 322 ? 1.2296 0.8257 0.9936 -0.0452 -0.0577 0.0824 322 SER B CB 9705 O OG . SER B 322 ? 1.4510 1.0653 1.1980 -0.0648 -0.0524 0.0730 322 SER B OG 9706 N N . GLU B 323 ? 1.0778 0.6983 0.8771 -0.0502 -0.0354 0.0388 323 GLU B N 9707 C CA . GLU B 323 ? 1.0775 0.7011 0.8907 -0.0582 -0.0275 0.0251 323 GLU B CA 9708 C C . GLU B 323 ? 1.1244 0.7384 0.9600 -0.0459 -0.0340 0.0243 323 GLU B C 9709 O O . GLU B 323 ? 1.1775 0.7844 1.0199 -0.0498 -0.0330 0.0208 323 GLU B O 9710 C CB . GLU B 323 ? 1.1136 0.7621 0.9476 -0.0718 -0.0160 0.0028 323 GLU B CB 9711 C CG . GLU B 323 ? 1.2028 0.8604 1.0053 -0.0923 -0.0078 0.0011 323 GLU B CG 9712 C CD . GLU B 323 ? 1.5121 1.1946 1.3367 -0.1105 0.0098 -0.0274 323 GLU B CD 9713 O OE1 . GLU B 323 ? 1.6383 1.3310 1.5131 -0.1048 0.0143 -0.0453 323 GLU B OE1 9714 O OE2 . GLU B 323 ? 1.5774 1.2687 1.3718 -0.1331 0.0187 -0.0324 323 GLU B OE2 9715 N N . LEU B 324 ? 1.0963 0.7090 0.9408 -0.0337 -0.0417 0.0282 324 LEU B N 9716 C CA . LEU B 324 ? 0.9793 0.5802 0.8356 -0.0273 -0.0503 0.0301 324 LEU B CA 9717 C C . LEU B 324 ? 1.0431 0.6192 0.8733 -0.0241 -0.0514 0.0420 324 LEU B C 9718 O O . LEU B 324 ? 1.2043 0.7670 1.0330 -0.0255 -0.0569 0.0434 324 LEU B O 9719 C CB . LEU B 324 ? 0.8739 0.4824 0.7478 -0.0196 -0.0568 0.0288 324 LEU B CB 9720 C CG . LEU B 324 ? 0.8622 0.4951 0.7755 -0.0230 -0.0558 0.0140 324 LEU B CG 9721 C CD1 . LEU B 324 ? 1.2142 0.8531 1.1463 -0.0149 -0.0629 0.0146 324 LEU B CD1 9722 C CD2 . LEU B 324 ? 0.8517 0.4865 0.7971 -0.0302 -0.0600 0.0058 324 LEU B CD2 9723 N N . ILE B 325 ? 0.9446 0.5141 0.7571 -0.0222 -0.0468 0.0504 325 ILE B N 9724 C CA . ILE B 325 ? 0.9738 0.5209 0.7728 -0.0203 -0.0443 0.0586 325 ILE B CA 9725 C C . ILE B 325 ? 1.3058 0.8482 1.0951 -0.0267 -0.0407 0.0645 325 ILE B C 9726 O O . ILE B 325 ? 1.6231 1.1639 1.4081 -0.0263 -0.0420 0.0748 325 ILE B O 9727 C CB . ILE B 325 ? 0.9413 0.4807 0.7421 -0.0116 -0.0435 0.0644 325 ILE B CB 9728 C CG1 . ILE B 325 ? 0.9249 0.4713 0.7336 -0.0066 -0.0464 0.0588 325 ILE B CG1 9729 C CG2 . ILE B 325 ? 0.9858 0.5020 0.7834 -0.0117 -0.0368 0.0665 325 ILE B CG2 9730 C CD1 . ILE B 325 ? 0.8439 0.3830 0.6585 0.0012 -0.0431 0.0613 325 ILE B CD1 9731 N N . PRO B 326 ? 1.1848 0.7241 0.9724 -0.0340 -0.0382 0.0595 326 PRO B N 9732 C CA . PRO B 326 ? 1.1696 0.7045 0.9474 -0.0424 -0.0336 0.0639 326 PRO B CA 9733 C C . PRO B 326 ? 1.2752 0.7913 1.0481 -0.0394 -0.0330 0.0773 326 PRO B C 9734 O O . PRO B 326 ? 1.3232 0.8253 1.1019 -0.0336 -0.0307 0.0765 326 PRO B O 9735 C CB . PRO B 326 ? 1.1877 0.7197 0.9716 -0.0479 -0.0316 0.0541 326 PRO B CB 9736 C CG . PRO B 326 ? 1.1511 0.6772 0.9410 -0.0428 -0.0380 0.0507 326 PRO B CG 9737 C CD . PRO B 326 ? 1.1295 0.6669 0.9255 -0.0360 -0.0419 0.0510 326 PRO B CD 9738 N N . GLY B 327 ? 1.3695 0.8846 1.1340 -0.0459 -0.0350 0.0892 327 GLY B N 9739 C CA . GLY B 327 ? 1.5317 1.0291 1.3031 -0.0436 -0.0381 0.1047 327 GLY B CA 9740 C C . GLY B 327 ? 1.4850 0.9831 1.2668 -0.0377 -0.0483 0.1170 327 GLY B C 9741 O O . GLY B 327 ? 1.4387 0.9222 1.2404 -0.0340 -0.0535 0.1301 327 GLY B O 9742 N N . THR B 328 ? 1.3549 0.8703 1.1302 -0.0371 -0.0518 0.1123 328 THR B N 9743 C CA . THR B 328 ? 1.2046 0.7228 0.9901 -0.0320 -0.0629 0.1229 328 THR B CA 9744 C C . THR B 328 ? 1.1944 0.7262 0.9555 -0.0470 -0.0721 0.1311 328 THR B C 9745 O O . THR B 328 ? 1.3023 0.8498 1.0447 -0.0572 -0.0643 0.1177 328 THR B O 9746 C CB . THR B 328 ? 1.1134 0.6393 0.9126 -0.0195 -0.0589 0.1098 328 THR B CB 9747 O OG1 . THR B 328 ? 1.1106 0.6558 0.8968 -0.0237 -0.0550 0.0962 328 THR B OG1 9748 C CG2 . THR B 328 ? 1.0839 0.5948 0.8969 -0.0118 -0.0482 0.1001 328 THR B CG2 9749 N N . THR B 329 ? 1.1146 0.6397 0.8787 -0.0509 -0.0889 0.1522 329 THR B N 9750 C CA . THR B 329 ? 1.2161 0.7509 0.9484 -0.0713 -0.1003 0.1630 329 THR B CA 9751 C C . THR B 329 ? 1.2369 0.7807 0.9788 -0.0669 -0.1138 0.1687 329 THR B C 9752 O O . THR B 329 ? 1.2195 0.7566 0.9987 -0.0481 -0.1185 0.1713 329 THR B O 9753 C CB . THR B 329 ? 1.2577 0.7752 0.9755 -0.0882 -0.1155 0.1895 329 THR B CB 9754 O OG1 . THR B 329 ? 1.3171 0.8165 1.0768 -0.0748 -0.1314 0.2088 329 THR B OG1 9755 C CG2 . THR B 329 ? 1.3301 0.8405 1.0344 -0.0956 -0.1007 0.1825 329 THR B CG2 9756 N N . VAL B 330 ? 1.2111 0.7704 0.9197 -0.0865 -0.1179 0.1681 330 VAL B N 9757 C CA . VAL B 330 ? 1.0838 0.6537 0.7963 -0.0861 -0.1313 0.1726 330 VAL B CA 9758 C C . VAL B 330 ? 1.1047 0.6694 0.7837 -0.1134 -0.1556 0.1990 330 VAL B C 9759 O O . VAL B 330 ? 1.1007 0.6614 0.7394 -0.1389 -0.1542 0.2046 330 VAL B O 9760 C CB . VAL B 330 ? 1.0788 0.6747 0.7835 -0.0870 -0.1139 0.1446 330 VAL B CB 9761 C CG1 . VAL B 330 ? 1.0766 0.6837 0.7915 -0.0829 -0.1260 0.1471 330 VAL B CG1 9762 C CG2 . VAL B 330 ? 1.1224 0.7207 0.8550 -0.0657 -0.0945 0.1230 330 VAL B CG2 9763 N N . GLY B 331 ? 1.0697 0.6332 0.7648 -0.1106 -0.1790 0.2158 331 GLY B N 9764 C CA . GLY B 331 ? 1.2527 0.8098 0.9153 -0.1393 -0.2086 0.2448 331 GLY B CA 9765 C C . GLY B 331 ? 1.2528 0.8220 0.9212 -0.1403 -0.2257 0.2485 331 GLY B C 9766 O O . GLY B 331 ? 1.3039 0.8804 1.0171 -0.1128 -0.2195 0.2352 331 GLY B O 9767 N N . VAL B 332 ? 1.2372 0.8075 0.8572 -0.1750 -0.2477 0.2670 332 VAL B N 9768 C CA . VAL B 332 ? 1.2425 0.8270 0.8570 -0.1828 -0.2634 0.2685 332 VAL B CA 9769 C C . VAL B 332 ? 1.3064 0.8739 0.9656 -0.1739 -0.3052 0.3037 332 VAL B C 9770 O O . VAL B 332 ? 1.4898 1.0343 1.1497 -0.1871 -0.3348 0.3384 332 VAL B O 9771 C CB . VAL B 332 ? 1.3471 0.9423 0.8817 -0.2311 -0.2657 0.2682 332 VAL B CB 9772 C CG1 . VAL B 332 ? 1.3027 0.9150 0.8306 -0.2400 -0.2789 0.2654 332 VAL B CG1 9773 C CG2 . VAL B 332 ? 1.4112 1.0228 0.9136 -0.2418 -0.2224 0.2306 332 VAL B CG2 9774 N N . LEU B 333 ? 1.2406 0.8188 0.9433 -0.1516 -0.3079 0.2943 333 LEU B N 9775 C CA . LEU B 333 ? 1.2351 0.8002 0.9913 -0.1426 -0.3466 0.3231 333 LEU B CA 9776 C C . LEU B 333 ? 1.4740 1.0505 1.1925 -0.1709 -0.3738 0.3354 333 LEU B C 9777 O O . LEU B 333 ? 1.8533 1.4528 1.5669 -0.1655 -0.3570 0.3095 333 LEU B O 9778 C CB . LEU B 333 ? 1.1400 0.7071 0.9759 -0.0997 -0.3303 0.3032 333 LEU B CB 9779 C CG . LEU B 333 ? 1.1076 0.6537 1.0286 -0.0804 -0.3577 0.3260 333 LEU B CG 9780 C CD1 . LEU B 333 ? 1.1140 0.6367 1.0608 -0.0757 -0.3573 0.3391 333 LEU B CD1 9781 C CD2 . LEU B 333 ? 1.0598 0.6134 1.0456 -0.0464 -0.3369 0.2993 333 LEU B CD2 9782 N N . SER B 334 ? 1.4149 0.9747 1.1063 -0.2031 -0.4170 0.3758 334 SER B N 9783 C CA . SER B 334 ? 1.5959 1.1644 1.2392 -0.2383 -0.4465 0.3905 334 SER B CA 9784 C C . SER B 334 ? 1.7681 1.3111 1.4301 -0.2571 -0.5086 0.4441 334 SER B C 9785 O O . SER B 334 ? 1.8534 1.3788 1.5463 -0.2547 -0.5211 0.4642 334 SER B O 9786 C CB . SER B 334 ? 1.7465 1.3276 1.2861 -0.2835 -0.4263 0.3760 334 SER B CB 9787 O OG . SER B 334 ? 1.9733 1.5627 1.4594 -0.3229 -0.4524 0.3876 334 SER B OG 9788 N N . MET B 335 ? 1.8310 1.3798 1.4842 -0.2755 -0.5429 0.4597 335 MET B N 9789 C CA . MET B 335 ? 1.7820 1.3257 1.4816 -0.2897 -0.5876 0.4894 335 MET B CA 9790 C C . MET B 335 ? 1.8906 1.4282 1.5142 -0.3433 -0.6055 0.5104 335 MET B C 9791 O O . MET B 335 ? 2.0787 1.6076 1.7357 -0.3601 -0.6444 0.5387 335 MET B O 9792 C CB . MET B 335 ? 1.8035 1.3589 1.5279 -0.2913 -0.6139 0.4928 335 MET B CB 9793 C CG . MET B 335 ? 1.7377 1.2991 1.5412 -0.2402 -0.5970 0.4711 335 MET B CG 9794 S SD . MET B 335 ? 1.9304 1.5018 1.7983 -0.2368 -0.6348 0.4799 335 MET B SD 9795 C CE . MET B 335 ? 1.4470 1.0037 1.3979 -0.2447 -0.6762 0.5123 335 MET B CE 9796 N N . ASP B 336 ? 1.9747 1.5163 1.4990 -0.3721 -0.5760 0.4949 336 ASP B N 9797 C CA . ASP B 336 ? 2.3101 1.8460 1.7549 -0.4268 -0.5849 0.5082 336 ASP B CA 9798 C C . ASP B 336 ? 2.3971 1.9247 1.8105 -0.4257 -0.5508 0.4970 336 ASP B C 9799 O O . ASP B 336 ? 2.3452 1.8729 1.7838 -0.3875 -0.5181 0.4765 336 ASP B O 9800 C CB . ASP B 336 ? 2.4726 2.0240 1.8204 -0.4763 -0.5785 0.4949 336 ASP B CB 9801 C CG . ASP B 336 ? 2.6094 2.1518 1.9025 -0.5359 -0.6084 0.5193 336 ASP B CG 9802 O OD1 . ASP B 336 ? 2.6333 2.1683 1.9685 -0.5433 -0.6548 0.5488 336 ASP B OD1 9803 O OD2 . ASP B 336 ? 2.6386 2.1801 1.8485 -0.5774 -0.5853 0.5082 336 ASP B OD2 9804 N N . SER B 337 ? 2.4499 1.9685 1.8095 -0.4690 -0.5597 0.5111 337 SER B N 9805 C CA . SER B 337 ? 2.4039 1.9120 1.7403 -0.4720 -0.5349 0.5063 337 SER B CA 9806 C C . SER B 337 ? 2.3990 1.8940 1.8336 -0.4247 -0.5432 0.5200 337 SER B C 9807 O O . SER B 337 ? 2.3718 1.8610 1.8786 -0.4146 -0.5823 0.5458 337 SER B O 9808 C CB . SER B 337 ? 2.3331 1.8514 1.6102 -0.4714 -0.4805 0.4675 337 SER B CB 9809 O OG . SER B 337 ? 2.2214 1.7431 1.5558 -0.4188 -0.4616 0.4514 337 SER B OG 9810 N N . SER B 338 ? 2.4523 1.9432 1.8929 -0.3982 -0.5053 0.5005 338 SER B N 9811 C CA . SER B 338 ? 2.3790 1.8574 1.9014 -0.3609 -0.5057 0.5089 338 SER B CA 9812 C C . SER B 338 ? 2.3331 1.8135 1.9626 -0.3093 -0.5108 0.5053 338 SER B C 9813 O O . SER B 338 ? 2.3474 1.8239 2.0572 -0.2959 -0.5394 0.5242 338 SER B O 9814 C CB . SER B 338 ? 2.1876 1.6598 1.6773 -0.3534 -0.4619 0.4874 338 SER B CB 9815 O OG . SER B 338 ? 2.0794 1.5586 1.5522 -0.3346 -0.4273 0.4580 338 SER B OG 9816 N N . ASN B 339 ? 2.1554 1.6418 1.7865 -0.2827 -0.4808 0.4788 339 ASN B N 9817 C CA . ASN B 339 ? 2.0380 1.5265 1.7614 -0.2350 -0.4756 0.4668 339 ASN B CA 9818 C C . ASN B 339 ? 2.0710 1.5497 1.8843 -0.2011 -0.4673 0.4653 339 ASN B C 9819 O O . ASN B 339 ? 2.1169 1.5864 1.9066 -0.2095 -0.4555 0.4678 339 ASN B O 9820 C CB . ASN B 339 ? 2.1138 1.6121 1.8686 -0.2410 -0.5125 0.4812 339 ASN B CB 9821 C CG . ASN B 339 ? 2.1789 1.6808 2.0377 -0.1970 -0.5111 0.4697 339 ASN B CG 9822 O OD1 . ASN B 339 ? 2.1649 1.6660 2.0463 -0.1648 -0.4775 0.4438 339 ASN B OD1 9823 N ND2 . ASN B 339 ? 2.1959 1.7009 2.1215 -0.1979 -0.5476 0.4881 339 ASN B ND2 9824 N N . VAL B 340 ? 2.1132 1.5947 2.0280 -0.1693 -0.4749 0.4621 340 VAL B N 9825 C CA . VAL B 340 ? 2.1036 1.5788 2.0964 -0.1328 -0.4475 0.4435 340 VAL B CA 9826 C C . VAL B 340 ? 2.1263 1.5923 2.1389 -0.1398 -0.4529 0.4577 340 VAL B C 9827 O O . VAL B 340 ? 2.2224 1.6805 2.2548 -0.1217 -0.4230 0.4417 340 VAL B O 9828 C CB . VAL B 340 ? 1.6785 1.1610 1.7824 -0.1025 -0.4514 0.4332 340 VAL B CB 9829 C CG1 . VAL B 340 ? 1.6208 1.0980 1.7874 -0.0699 -0.4127 0.4051 340 VAL B CG1 9830 C CG2 . VAL B 340 ? 1.6457 1.1385 1.7446 -0.0955 -0.4535 0.4226 340 VAL B CG2 9831 N N . LEU B 341 ? 1.9438 1.4103 1.9523 -0.1678 -0.4929 0.4884 341 LEU B N 9832 C CA . LEU B 341 ? 1.8780 1.3364 1.9134 -0.1780 -0.5081 0.5079 341 LEU B CA 9833 C C . LEU B 341 ? 1.8850 1.3327 1.8531 -0.1895 -0.4839 0.5047 341 LEU B C 9834 O O . LEU B 341 ? 1.8428 1.2839 1.8497 -0.1671 -0.4572 0.4903 341 LEU B O 9835 C CB . LEU B 341 ? 1.9720 1.4316 1.9946 -0.2144 -0.5593 0.5433 341 LEU B CB 9836 C CG . LEU B 341 ? 1.9236 1.3913 2.0175 -0.2149 -0.5988 0.5581 341 LEU B CG 9837 C CD1 . LEU B 341 ? 1.8034 1.2818 1.9014 -0.1981 -0.5884 0.5385 341 LEU B CD1 9838 C CD2 . LEU B 341 ? 2.0104 1.4741 2.0503 -0.2630 -0.6453 0.5937 341 LEU B CD2 9839 N N . GLN B 342 ? 2.0332 1.4797 1.8997 -0.2272 -0.4913 0.5158 342 GLN B N 9840 C CA . GLN B 342 ? 2.0281 1.4654 1.8264 -0.2440 -0.4689 0.5123 342 GLN B CA 9841 C C . GLN B 342 ? 1.7470 1.1850 1.5033 -0.2292 -0.4251 0.4803 342 GLN B C 9842 O O . GLN B 342 ? 1.7045 1.1349 1.4138 -0.2367 -0.3988 0.4700 342 GLN B O 9843 C CB . GLN B 342 ? 2.1861 1.6218 1.8938 -0.2962 -0.4916 0.5339 342 GLN B CB 9844 C CG . GLN B 342 ? 1.8648 1.2886 1.5732 -0.3139 -0.5043 0.5547 342 GLN B CG 9845 C CD . GLN B 342 ? 2.0350 1.4520 1.6485 -0.3420 -0.4765 0.5453 342 GLN B CD 9846 O OE1 . GLN B 342 ? 2.1276 1.5503 1.6578 -0.3654 -0.4577 0.5294 342 GLN B OE1 9847 N NE2 . GLN B 342 ? 2.0614 1.4672 1.6918 -0.3410 -0.4724 0.5531 342 GLN B NE2 9848 N N . LEU B 343 ? 1.5533 0.9996 1.3314 -0.2082 -0.4182 0.4646 343 LEU B N 9849 C CA . LEU B 343 ? 1.7621 1.2065 1.5246 -0.1868 -0.3788 0.4339 343 LEU B CA 9850 C C . LEU B 343 ? 1.8908 1.3244 1.7076 -0.1575 -0.3522 0.4185 343 LEU B C 9851 O O . LEU B 343 ? 2.0246 1.4494 1.7952 -0.1675 -0.3314 0.4117 343 LEU B O 9852 C CB . LEU B 343 ? 1.6390 1.0926 1.4290 -0.1660 -0.3776 0.4201 343 LEU B CB 9853 C CG . LEU B 343 ? 1.3648 0.8325 1.1959 -0.1277 -0.3359 0.3772 343 LEU B CG 9854 C CD1 . LEU B 343 ? 1.2918 0.7756 1.0705 -0.1278 -0.2922 0.3411 343 LEU B CD1 9855 C CD2 . LEU B 343 ? 1.2891 0.7723 1.1475 -0.1138 -0.3413 0.3668 343 LEU B CD2 9856 N N . ILE B 344 ? 1.8035 1.2379 1.7152 -0.1260 -0.3514 0.4115 344 ILE B N 9857 C CA . ILE B 344 ? 1.6573 1.0828 1.6122 -0.0997 -0.3186 0.3880 344 ILE B CA 9858 C C . ILE B 344 ? 1.5919 1.0060 1.5241 -0.1118 -0.3106 0.3948 344 ILE B C 9859 O O . ILE B 344 ? 1.5610 0.9670 1.4645 -0.1076 -0.2815 0.3759 344 ILE B O 9860 C CB . ILE B 344 ? 1.5360 0.9645 1.5968 -0.0727 -0.3174 0.3793 344 ILE B CB 9861 C CG1 . ILE B 344 ? 1.1222 0.5581 1.2152 -0.0508 -0.3045 0.3562 344 ILE B CG1 9862 C CG2 . ILE B 344 ? 1.1424 0.5601 1.2393 -0.0592 -0.2897 0.3633 344 ILE B CG2 9863 C CD1 . ILE B 344 ? 1.1424 0.5746 1.3097 -0.0236 -0.2714 0.3253 344 ILE B CD1 9864 N N . VAL B 345 ? 1.2959 0.7099 1.2395 -0.1287 -0.3376 0.4214 345 VAL B N 9865 C CA . VAL B 345 ? 1.3108 0.7140 1.2420 -0.1394 -0.3319 0.4293 345 VAL B CA 9866 C C . VAL B 345 ? 1.4439 0.8411 1.2770 -0.1615 -0.3122 0.4223 345 VAL B C 9867 O O . VAL B 345 ? 1.6832 1.0699 1.5082 -0.1583 -0.2884 0.4111 345 VAL B O 9868 C CB . VAL B 345 ? 1.5157 0.9200 1.4649 -0.1598 -0.3707 0.4627 345 VAL B CB 9869 C CG1 . VAL B 345 ? 1.7907 1.1835 1.7194 -0.1743 -0.3666 0.4730 345 VAL B CG1 9870 C CG2 . VAL B 345 ? 1.4770 0.8870 1.5353 -0.1376 -0.3870 0.4658 345 VAL B CG2 9871 N N . ASP B 346 ? 1.3582 0.7625 1.1195 -0.1852 -0.3201 0.4260 346 ASP B N 9872 C CA . ASP B 346 ? 1.4249 0.8307 1.1001 -0.2059 -0.2938 0.4085 346 ASP B CA 9873 C C . ASP B 346 ? 1.3648 0.7890 1.0611 -0.1745 -0.2501 0.3619 346 ASP B C 9874 O O . ASP B 346 ? 1.5823 1.0116 1.2478 -0.1788 -0.2213 0.3398 346 ASP B O 9875 C CB . ASP B 346 ? 1.6242 1.0447 1.2305 -0.2357 -0.3038 0.4105 346 ASP B CB 9876 C CG . ASP B 346 ? 1.8492 1.2655 1.4254 -0.2717 -0.3411 0.4454 346 ASP B CG 9877 O OD1 . ASP B 346 ? 1.9714 1.3978 1.4977 -0.2981 -0.3550 0.4502 346 ASP B OD1 9878 O OD2 . ASP B 346 ? 1.8934 1.3021 1.5012 -0.2729 -0.3551 0.4632 346 ASP B OD2 9879 N N . ALA B 347 ? 1.2622 0.6948 1.0115 -0.1449 -0.2463 0.3476 347 ALA B N 9880 C CA . ALA B 347 ? 1.3249 0.7716 1.0904 -0.1192 -0.2092 0.3076 347 ALA B CA 9881 C C . ALA B 347 ? 1.3952 0.8269 1.1985 -0.1051 -0.1940 0.3018 347 ALA B C 9882 O O . ALA B 347 ? 1.3778 0.8161 1.1621 -0.1014 -0.1659 0.2764 347 ALA B O 9883 C CB . ALA B 347 ? 1.3449 0.8017 1.1533 -0.0953 -0.2085 0.2948 347 ALA B CB 9884 N N . TYR B 348 ? 1.3353 0.7467 1.1967 -0.0987 -0.2136 0.3250 348 TYR B N 9885 C CA . TYR B 348 ? 1.1620 0.5580 1.0646 -0.0884 -0.2001 0.3206 348 TYR B CA 9886 C C . TYR B 348 ? 1.2647 0.6547 1.1163 -0.1097 -0.1950 0.3274 348 TYR B C 9887 O O . TYR B 348 ? 1.4288 0.8148 1.2886 -0.1028 -0.1719 0.3104 348 TYR B O 9888 C CB . TYR B 348 ? 1.1484 0.5238 1.1328 -0.0809 -0.2248 0.3459 348 TYR B CB 9889 C CG . TYR B 348 ? 1.1686 0.5342 1.2045 -0.0708 -0.2071 0.3363 348 TYR B CG 9890 C CD1 . TYR B 348 ? 1.1499 0.5135 1.2156 -0.0524 -0.1745 0.3029 348 TYR B CD1 9891 C CD2 . TYR B 348 ? 1.2343 0.5965 1.2872 -0.0815 -0.2216 0.3577 348 TYR B CD2 9892 C CE1 . TYR B 348 ? 1.1291 0.4800 1.2408 -0.0469 -0.1580 0.2937 348 TYR B CE1 9893 C CE2 . TYR B 348 ? 1.2643 0.6179 1.3663 -0.0728 -0.2044 0.3475 348 TYR B CE2 9894 C CZ . TYR B 348 ? 1.2135 0.5619 1.3444 -0.0558 -0.1717 0.3146 348 TYR B CZ 9895 O OH . TYR B 348 ? 1.2858 0.6262 1.4632 -0.0502 -0.1529 0.3018 348 TYR B OH 9896 N N . GLY B 349 ? 1.3361 0.7251 1.1328 -0.1383 -0.2161 0.3514 349 GLY B N 9897 C CA . GLY B 349 ? 1.4357 0.8195 1.1757 -0.1639 -0.2090 0.3560 349 GLY B CA 9898 C C . GLY B 349 ? 1.5029 0.9066 1.2031 -0.1621 -0.1717 0.3163 349 GLY B C 9899 O O . GLY B 349 ? 1.7041 1.1034 1.3971 -0.1639 -0.1524 0.3046 349 GLY B O 9900 N N . LYS B 350 ? 1.3510 0.7762 1.0316 -0.1585 -0.1630 0.2960 350 LYS B N 9901 C CA . LYS B 350 ? 1.2959 0.7410 0.9516 -0.1559 -0.1312 0.2588 350 LYS B CA 9902 C C . LYS B 350 ? 1.2504 0.6942 0.9471 -0.1292 -0.1102 0.2363 350 LYS B C 9903 O O . LYS B 350 ? 1.2554 0.7033 0.9381 -0.1323 -0.0893 0.2166 350 LYS B O 9904 C CB . LYS B 350 ? 1.2949 0.7623 0.9380 -0.1533 -0.1287 0.2430 350 LYS B CB 9905 C CG . LYS B 350 ? 1.4781 0.9510 1.0688 -0.1857 -0.1432 0.2570 350 LYS B CG 9906 C CD . LYS B 350 ? 1.4160 0.9127 1.0012 -0.1815 -0.1375 0.2374 350 LYS B CD 9907 C CE . LYS B 350 ? 1.3210 0.8232 0.8511 -0.2176 -0.1512 0.2496 350 LYS B CE 9908 N NZ . LYS B 350 ? 1.3026 0.8287 0.8316 -0.2136 -0.1449 0.2292 350 LYS B NZ 9909 N N . ILE B 351 ? 1.2232 0.6610 0.9712 -0.1057 -0.1155 0.2381 351 ILE B N 9910 C CA . ILE B 351 ? 1.3141 0.7487 1.0968 -0.0851 -0.0958 0.2165 351 ILE B CA 9911 C C . ILE B 351 ? 1.4303 0.8496 1.2192 -0.0903 -0.0883 0.2199 351 ILE B C 9912 O O . ILE B 351 ? 1.6909 1.1130 1.4762 -0.0859 -0.0681 0.1977 351 ILE B O 9913 C CB . ILE B 351 ? 1.3146 0.7418 1.1534 -0.0651 -0.1008 0.2180 351 ILE B CB 9914 C CG1 . ILE B 351 ? 1.2352 0.6775 1.0707 -0.0589 -0.1074 0.2138 351 ILE B CG1 9915 C CG2 . ILE B 351 ? 1.3914 0.8139 1.2570 -0.0510 -0.0776 0.1936 351 ILE B CG2 9916 C CD1 . ILE B 351 ? 1.4619 0.9239 1.2664 -0.0562 -0.0896 0.1868 351 ILE B CD1 9917 N N . ARG B 352 ? 1.2340 0.6363 1.0335 -0.1010 -0.1071 0.2492 352 ARG B N 9918 C CA . ARG B 352 ? 1.2333 0.6194 1.0433 -0.1067 -0.1021 0.2558 352 ARG B CA 9919 C C . ARG B 352 ? 1.3976 0.7863 1.1495 -0.1311 -0.0966 0.2569 352 ARG B C 9920 O O . ARG B 352 ? 1.6089 0.9848 1.3616 -0.1391 -0.0917 0.2624 352 ARG B O 9921 C CB . ARG B 352 ? 1.2873 0.6520 1.1450 -0.1078 -0.1267 0.2886 352 ARG B CB 9922 C CG . ARG B 352 ? 1.2012 0.5611 1.1320 -0.0852 -0.1277 0.2835 352 ARG B CG 9923 C CD . ARG B 352 ? 1.1976 0.5531 1.1644 -0.0714 -0.0994 0.2560 352 ARG B CD 9924 N NE . ARG B 352 ? 1.2266 0.5977 1.1747 -0.0604 -0.0760 0.2220 352 ARG B NE 9925 C CZ . ARG B 352 ? 1.4068 0.7789 1.3941 -0.0461 -0.0660 0.2048 352 ARG B CZ 9926 N NH1 . ARG B 352 ? 1.4254 0.8097 1.3872 -0.0406 -0.0477 0.1775 352 ARG B NH1 9927 N NH2 . ARG B 352 ? 1.4421 0.8017 1.4973 -0.0393 -0.0747 0.2150 352 ARG B NH2 9928 N N . SER B 353 ? 1.3149 0.7204 1.0197 -0.1443 -0.0949 0.2492 353 SER B N 9929 C CA . SER B 353 ? 1.3812 0.7907 1.0322 -0.1716 -0.0848 0.2446 353 SER B CA 9930 C C . SER B 353 ? 1.4239 0.8464 1.0733 -0.1651 -0.0557 0.2086 353 SER B C 9931 O O . SER B 353 ? 1.5081 0.9350 1.1244 -0.1859 -0.0416 0.1975 353 SER B O 9932 C CB . SER B 353 ? 1.4813 0.9030 1.0855 -0.1939 -0.0934 0.2492 353 SER B CB 9933 O OG . SER B 353 ? 1.7886 1.1967 1.3905 -0.2044 -0.1254 0.2861 353 SER B OG 9934 N N . LYS B 354 ? 1.3494 0.7770 1.0358 -0.1388 -0.0473 0.1905 354 LYS B N 9935 C CA . LYS B 354 ? 1.2278 0.6668 0.9177 -0.1324 -0.0263 0.1596 354 LYS B CA 9936 C C . LYS B 354 ? 1.3186 0.7473 1.0449 -0.1136 -0.0202 0.1521 354 LYS B C 9937 O O . LYS B 354 ? 1.4890 0.9101 1.2437 -0.0990 -0.0271 0.1592 354 LYS B O 9938 C CB . LYS B 354 ? 1.2106 0.6713 0.8975 -0.1261 -0.0226 0.1403 354 LYS B CB 9939 C CG . LYS B 354 ? 1.3576 0.8309 1.0526 -0.1234 -0.0063 0.1112 354 LYS B CG 9940 C CD . LYS B 354 ? 1.3669 0.8607 1.0668 -0.1177 -0.0058 0.0955 354 LYS B CD 9941 C CE . LYS B 354 ? 1.2849 0.7905 1.0030 -0.1166 0.0056 0.0692 354 LYS B CE 9942 N NZ . LYS B 354 ? 1.2418 0.7365 0.9804 -0.1028 0.0046 0.0657 354 LYS B NZ 9943 N N . VAL B 355 ? 1.2234 0.6516 0.9502 -0.1163 -0.0059 0.1358 355 VAL B N 9944 C CA . VAL B 355 ? 1.2084 0.6279 0.9629 -0.1032 0.0015 0.1252 355 VAL B CA 9945 C C . VAL B 355 ? 1.3109 0.7423 1.0645 -0.1007 0.0111 0.0992 355 VAL B C 9946 O O . VAL B 355 ? 1.4318 0.8688 1.1768 -0.1115 0.0188 0.0888 355 VAL B O 9947 C CB . VAL B 355 ? 1.1825 0.5842 0.9471 -0.1095 0.0055 0.1349 355 VAL B CB 9948 C CG1 . VAL B 355 ? 1.1611 0.5566 0.9493 -0.1002 0.0169 0.1176 355 VAL B CG1 9949 C CG2 . VAL B 355 ? 1.1876 0.5744 0.9683 -0.1099 -0.0087 0.1632 355 VAL B CG2 9950 N N . GLU B 356 ? 1.2523 0.6867 1.0175 -0.0886 0.0096 0.0891 356 GLU B N 9951 C CA . GLU B 356 ? 1.2475 0.6905 1.0148 -0.0876 0.0119 0.0693 356 GLU B CA 9952 C C . GLU B 356 ? 1.3009 0.7322 1.0775 -0.0822 0.0142 0.0621 356 GLU B C 9953 O O . GLU B 356 ? 1.4670 0.8905 1.2503 -0.0760 0.0145 0.0668 356 GLU B O 9954 C CB . GLU B 356 ? 1.4470 0.9074 1.2110 -0.0847 0.0052 0.0635 356 GLU B CB 9955 C CG . GLU B 356 ? 1.6940 1.1633 1.4687 -0.0853 0.0023 0.0465 356 GLU B CG 9956 C CD . GLU B 356 ? 1.7397 1.2273 1.5205 -0.0835 -0.0039 0.0409 356 GLU B CD 9957 O OE1 . GLU B 356 ? 1.5694 1.0620 1.3413 -0.0801 -0.0055 0.0492 356 GLU B OE1 9958 O OE2 . GLU B 356 ? 1.8192 1.3161 1.6189 -0.0859 -0.0082 0.0282 356 GLU B OE2 9959 N N . LEU B 357 ? 1.1768 0.6067 0.9551 -0.0873 0.0163 0.0492 357 LEU B N 9960 C CA . LEU B 357 ? 1.1448 0.5627 0.9238 -0.0889 0.0191 0.0406 357 LEU B CA 9961 C C . LEU B 357 ? 1.1160 0.5388 0.8855 -0.0896 0.0088 0.0336 357 LEU B C 9962 O O . LEU B 357 ? 1.1950 0.6297 0.9672 -0.0913 -0.0020 0.0298 357 LEU B O 9963 C CB . LEU B 357 ? 1.1503 0.5620 0.9335 -0.0970 0.0242 0.0320 357 LEU B CB 9964 C CG . LEU B 357 ? 1.1927 0.5982 0.9847 -0.0988 0.0341 0.0391 357 LEU B CG 9965 C CD1 . LEU B 357 ? 1.1521 0.5530 0.9500 -0.1066 0.0393 0.0279 357 LEU B CD1 9966 C CD2 . LEU B 357 ? 1.2836 0.6759 1.0875 -0.0945 0.0412 0.0493 357 LEU B CD2 9967 N N . GLU B 358 ? 1.1100 0.5230 0.8724 -0.0902 0.0125 0.0314 358 GLU B N 9968 C CA . GLU B 358 ? 1.1325 0.5457 0.8790 -0.0958 0.0027 0.0262 358 GLU B CA 9969 C C . GLU B 358 ? 1.1142 0.5122 0.8445 -0.1117 0.0062 0.0155 358 GLU B C 9970 O O . GLU B 358 ? 1.2774 0.6635 1.0118 -0.1158 0.0229 0.0093 358 GLU B O 9971 C CB . GLU B 358 ? 1.4122 0.8254 1.1564 -0.0892 0.0055 0.0297 358 GLU B CB 9972 C CG . GLU B 358 ? 1.6290 1.0296 1.3859 -0.0872 0.0233 0.0279 358 GLU B CG 9973 C CD . GLU B 358 ? 1.6713 1.0718 1.4321 -0.0817 0.0262 0.0287 358 GLU B CD 9974 O OE1 . GLU B 358 ? 1.6725 1.0665 1.4588 -0.0758 0.0373 0.0302 358 GLU B OE1 9975 O OE2 . GLU B 358 ? 1.6381 1.0444 1.3816 -0.0834 0.0165 0.0281 358 GLU B OE2 9976 N N . VAL B 359 ? 1.0816 0.4795 0.7954 -0.1229 -0.0107 0.0136 359 VAL B N 9977 C CA . VAL B 359 ? 1.1062 0.4894 0.7969 -0.1436 -0.0123 0.0050 359 VAL B CA 9978 C C . VAL B 359 ? 1.1447 0.5171 0.8016 -0.1600 -0.0163 0.0027 359 VAL B C 9979 O O . VAL B 359 ? 1.5389 0.9164 1.1884 -0.1616 -0.0371 0.0112 359 VAL B O 9980 C CB . VAL B 359 ? 1.0921 0.4800 0.7901 -0.1501 -0.0338 0.0066 359 VAL B CB 9981 C CG1 . VAL B 359 ? 1.2676 0.6392 0.9383 -0.1744 -0.0375 -0.0010 359 VAL B CG1 9982 C CG2 . VAL B 359 ? 1.0199 0.4180 0.7499 -0.1370 -0.0268 0.0063 359 VAL B CG2 9983 N N . ARG B 360 ? 1.1753 0.5322 0.8137 -0.1745 0.0051 -0.0102 360 ARG B N 9984 C CA . ARG B 360 ? 1.2475 0.5912 0.8472 -0.1965 0.0074 -0.0163 360 ARG B CA 9985 C C . ARG B 360 ? 1.3069 0.6346 0.8657 -0.2296 0.0016 -0.0244 360 ARG B C 9986 O O . ARG B 360 ? 1.4923 0.8154 1.0563 -0.2359 0.0124 -0.0343 360 ARG B O 9987 C CB . ARG B 360 ? 1.3165 0.6532 0.9261 -0.1946 0.0395 -0.0298 360 ARG B CB 9988 C CG . ARG B 360 ? 1.4715 0.8218 1.1180 -0.1657 0.0418 -0.0201 360 ARG B CG 9989 C CD . ARG B 360 ? 1.5674 0.9093 1.2347 -0.1650 0.0713 -0.0339 360 ARG B CD 9990 N NE . ARG B 360 ? 1.5430 0.8969 1.2490 -0.1383 0.0699 -0.0224 360 ARG B NE 9991 C CZ . ARG B 360 ? 1.5712 0.9206 1.3131 -0.1315 0.0898 -0.0297 360 ARG B CZ 9992 N NH1 . ARG B 360 ? 1.5441 0.8783 1.2934 -0.1492 0.1171 -0.0522 360 ARG B NH1 9993 N NH2 . ARG B 360 ? 1.5910 0.9512 1.3652 -0.1091 0.0823 -0.0157 360 ARG B NH2 9994 N N . ASP B 361 ? 1.3870 0.7056 0.9038 -0.2526 -0.0169 -0.0189 361 ASP B N 9995 C CA . ASP B 361 ? 1.4602 0.7601 0.9250 -0.2920 -0.0254 -0.0244 361 ASP B CA 9996 C C . ASP B 361 ? 1.3434 0.6455 0.8164 -0.2960 -0.0483 -0.0186 361 ASP B C 9997 O O . ASP B 361 ? 1.3613 0.6500 0.8045 -0.3234 -0.0426 -0.0302 361 ASP B O 9998 C CB . ASP B 361 ? 1.6254 0.9097 1.0672 -0.3148 0.0150 -0.0513 361 ASP B CB 9999 C CG . ASP B 361 ? 1.7731 1.0530 1.2093 -0.3159 0.0391 -0.0607 361 ASP B CG 10000 O OD1 . ASP B 361 ? 1.7944 1.0721 1.2574 -0.3109 0.0767 -0.0814 361 ASP B OD1 10001 O OD2 . ASP B 361 ? 1.8499 1.1280 1.2609 -0.3218 0.0200 -0.0476 361 ASP B OD2 10002 N N . LEU B 362 ? 1.2893 0.6084 0.8052 -0.2706 -0.0724 -0.0030 362 LEU B N 10003 C CA . LEU B 362 ? 1.2936 0.6159 0.8277 -0.2731 -0.0955 0.0019 362 LEU B CA 10004 C C . LEU B 362 ? 1.3600 0.6700 0.8608 -0.3041 -0.1362 0.0159 362 LEU B C 10005 O O . LEU B 362 ? 1.5964 0.9090 1.1007 -0.3032 -0.1634 0.0329 362 LEU B O 10006 C CB . LEU B 362 ? 1.2495 0.5937 0.8452 -0.2393 -0.1042 0.0100 362 LEU B CB 10007 C CG . LEU B 362 ? 1.2555 0.6048 0.8833 -0.2394 -0.1254 0.0122 362 LEU B CG 10008 C CD1 . LEU B 362 ? 1.3375 0.6806 0.9614 -0.2444 -0.1020 -0.0031 362 LEU B CD1 10009 C CD2 . LEU B 362 ? 1.3874 0.7582 1.0753 -0.2112 -0.1314 0.0169 362 LEU B CD2 10010 N N . PRO B 363 ? 1.4151 0.7109 0.8845 -0.3334 -0.1425 0.0100 363 PRO B N 10011 C CA . PRO B 363 ? 1.6107 0.8917 1.0443 -0.3685 -0.1864 0.0261 363 PRO B CA 10012 C C . PRO B 363 ? 1.6923 0.9858 1.1831 -0.3527 -0.2313 0.0476 363 PRO B C 10013 O O . PRO B 363 ? 1.6510 0.9630 1.2053 -0.3214 -0.2252 0.0433 363 PRO B O 10014 C CB . PRO B 363 ? 1.5950 0.8636 0.9992 -0.3955 -0.1786 0.0116 363 PRO B CB 10015 C CG . PRO B 363 ? 1.4965 0.7671 0.9012 -0.3842 -0.1234 -0.0150 363 PRO B CG 10016 C CD . PRO B 363 ? 1.4260 0.7174 0.8907 -0.3379 -0.1085 -0.0122 363 PRO B CD 10017 N N . GLU B 364 ? 1.7463 1.0286 1.2170 -0.3769 -0.2756 0.0700 364 GLU B N 10018 C CA . GLU B 364 ? 1.7222 1.0154 1.2578 -0.3639 -0.3209 0.0911 364 GLU B CA 10019 C C . GLU B 364 ? 1.6410 0.9397 1.2277 -0.3609 -0.3417 0.0902 364 GLU B C 10020 O O . GLU B 364 ? 1.6407 0.9571 1.3082 -0.3360 -0.3576 0.0943 364 GLU B O 10021 C CB . GLU B 364 ? 1.8089 1.0840 1.3088 -0.3969 -0.3684 0.1185 364 GLU B CB 10022 C CG . GLU B 364 ? 1.9451 1.2124 1.3927 -0.4043 -0.3509 0.1204 364 GLU B CG 10023 C CD . GLU B 364 ? 1.9745 1.2624 1.4832 -0.3674 -0.3496 0.1262 364 GLU B CD 10024 O OE1 . GLU B 364 ? 1.9059 1.1879 1.4159 -0.3780 -0.3844 0.1489 364 GLU B OE1 10025 O OE2 . GLU B 364 ? 2.0151 1.3243 1.5693 -0.3301 -0.3146 0.1086 364 GLU B OE2 10026 N N . GLU B 365 ? 1.5931 0.8772 1.1355 -0.3879 -0.3391 0.0822 365 GLU B N 10027 C CA . GLU B 365 ? 1.7125 0.9970 1.2941 -0.3941 -0.3675 0.0846 365 GLU B CA 10028 C C . GLU B 365 ? 1.5723 0.8778 1.2223 -0.3578 -0.3371 0.0644 365 GLU B C 10029 O O . GLU B 365 ? 1.5323 0.8430 1.2378 -0.3549 -0.3603 0.0655 365 GLU B O 10030 C CB . GLU B 365 ? 2.0329 1.2942 1.5384 -0.4387 -0.3737 0.0813 365 GLU B CB 10031 C CG . GLU B 365 ? 2.3333 1.5701 1.7685 -0.4855 -0.4156 0.1054 365 GLU B CG 10032 C CD . GLU B 365 ? 2.4069 1.6341 1.7718 -0.4972 -0.3845 0.1002 365 GLU B CD 10033 O OE1 . GLU B 365 ? 2.4383 1.6783 1.8132 -0.4680 -0.3318 0.0779 365 GLU B OE1 10034 O OE2 . GLU B 365 ? 2.3559 1.5617 1.6566 -0.5374 -0.4142 0.1191 365 GLU B OE2 10035 N N . LEU B 366 ? 1.4943 0.8105 1.1419 -0.3323 -0.2867 0.0467 366 LEU B N 10036 C CA . LEU B 366 ? 1.4789 0.8121 1.1815 -0.3022 -0.2570 0.0294 366 LEU B CA 10037 C C . LEU B 366 ? 1.3732 0.7257 1.1150 -0.2679 -0.2333 0.0263 366 LEU B C 10038 O O . LEU B 366 ? 1.3324 0.6846 1.0485 -0.2646 -0.2270 0.0324 366 LEU B O 10039 C CB . LEU B 366 ? 1.4669 0.7925 1.1310 -0.3084 -0.2175 0.0097 366 LEU B CB 10040 C CG . LEU B 366 ? 1.4607 0.7855 1.0911 -0.2985 -0.1714 -0.0022 366 LEU B CG 10041 C CD1 . LEU B 366 ? 1.5327 0.8529 1.1539 -0.3008 -0.1360 -0.0222 366 LEU B CD1 10042 C CD2 . LEU B 366 ? 1.4434 0.7533 1.0099 -0.3230 -0.1752 0.0036 366 LEU B CD2 10043 N N . SER B 367 ? 1.2873 0.6560 1.0894 -0.2451 -0.2196 0.0159 367 SER B N 10044 C CA . SER B 367 ? 1.4000 0.7872 1.2391 -0.2172 -0.1980 0.0116 367 SER B CA 10045 C C . SER B 367 ? 1.3702 0.7639 1.2161 -0.2013 -0.1566 -0.0043 367 SER B C 10046 O O . SER B 367 ? 1.4475 0.8341 1.2878 -0.2085 -0.1476 -0.0130 367 SER B O 10047 C CB . SER B 367 ? 1.6798 1.0819 1.5952 -0.2090 -0.2246 0.0146 367 SER B CB 10048 O OG . SER B 367 ? 1.8338 1.2373 1.7959 -0.2132 -0.2353 0.0065 367 SER B OG 10049 N N . LEU B 368 ? 1.3417 0.7480 1.1990 -0.1816 -0.1334 -0.0067 368 LEU B N 10050 C CA . LEU B 368 ? 1.2793 0.6891 1.1369 -0.1694 -0.0973 -0.0167 368 LEU B CA 10051 C C . LEU B 368 ? 1.2671 0.6948 1.1738 -0.1559 -0.0869 -0.0238 368 LEU B C 10052 O O . LEU B 368 ? 1.3048 0.7449 1.2340 -0.1495 -0.0951 -0.0213 368 LEU B O 10053 C CB . LEU B 368 ? 1.1349 0.5391 0.9493 -0.1637 -0.0746 -0.0127 368 LEU B CB 10054 C CG . LEU B 368 ? 1.1385 0.5247 0.9042 -0.1802 -0.0746 -0.0119 368 LEU B CG 10055 C CD1 . LEU B 368 ? 1.1262 0.5087 0.8669 -0.1726 -0.0496 -0.0112 368 LEU B CD1 10056 C CD2 . LEU B 368 ? 1.1601 0.5357 0.9202 -0.1931 -0.0684 -0.0218 368 LEU B CD2 10057 N N . SER B 369 ? 1.2218 0.6504 1.1442 -0.1543 -0.0670 -0.0343 369 SER B N 10058 C CA . SER B 369 ? 1.2718 0.7149 1.2315 -0.1474 -0.0500 -0.0444 369 SER B CA 10059 C C . SER B 369 ? 1.3081 0.7481 1.2364 -0.1420 -0.0191 -0.0421 369 SER B C 10060 O O . SER B 369 ? 1.4846 0.9112 1.3836 -0.1433 -0.0094 -0.0380 369 SER B O 10061 C CB . SER B 369 ? 1.2888 0.7349 1.2983 -0.1538 -0.0529 -0.0591 369 SER B CB 10062 O OG . SER B 369 ? 1.2277 0.6740 1.2706 -0.1604 -0.0876 -0.0574 369 SER B OG 10063 N N . PHE B 370 ? 1.1486 0.6004 1.0851 -0.1382 -0.0047 -0.0446 370 PHE B N 10064 C CA . PHE B 370 ? 1.1289 0.5762 1.0336 -0.1361 0.0182 -0.0372 370 PHE B CA 10065 C C . PHE B 370 ? 1.2526 0.7080 1.1717 -0.1433 0.0386 -0.0473 370 PHE B C 10066 O O . PHE B 370 ? 1.3909 0.8611 1.3304 -0.1461 0.0405 -0.0565 370 PHE B O 10067 C CB . PHE B 370 ? 1.0933 0.5426 0.9702 -0.1283 0.0149 -0.0235 370 PHE B CB 10068 C CG . PHE B 370 ? 1.0900 0.5302 0.9477 -0.1248 -0.0002 -0.0155 370 PHE B CG 10069 C CD1 . PHE B 370 ? 1.2575 0.7034 1.1256 -0.1251 -0.0218 -0.0158 370 PHE B CD1 10070 C CD2 . PHE B 370 ? 1.1661 0.5913 0.9978 -0.1241 0.0083 -0.0087 370 PHE B CD2 10071 C CE1 . PHE B 370 ? 1.3084 0.7438 1.1508 -0.1274 -0.0343 -0.0088 370 PHE B CE1 10072 C CE2 . PHE B 370 ? 1.2544 0.6705 1.0664 -0.1259 -0.0005 -0.0060 370 PHE B CE2 10073 C CZ . PHE B 370 ? 1.2893 0.7099 1.1013 -0.1289 -0.0215 -0.0057 370 PHE B CZ 10074 N N . ASN B 371 ? 1.2525 0.6975 1.1605 -0.1490 0.0553 -0.0469 371 ASN B N 10075 C CA . ASN B 371 ? 1.3350 0.7827 1.2370 -0.1605 0.0771 -0.0512 371 ASN B CA 10076 C C . ASN B 371 ? 1.4643 0.9010 1.3222 -0.1600 0.0829 -0.0285 371 ASN B C 10077 O O . ASN B 371 ? 1.5978 1.0200 1.4440 -0.1541 0.0807 -0.0162 371 ASN B O 10078 C CB . ASN B 371 ? 1.4136 0.8564 1.3370 -0.1709 0.0916 -0.0657 371 ASN B CB 10079 C CG . ASN B 371 ? 1.5291 0.9795 1.5046 -0.1701 0.0805 -0.0855 371 ASN B CG 10080 O OD1 . ASN B 371 ? 1.5256 0.9818 1.5177 -0.1621 0.0579 -0.0843 371 ASN B OD1 10081 N ND2 . ASN B 371 ? 1.8556 1.3047 1.8591 -0.1801 0.0948 -0.1025 371 ASN B ND2 10082 N N . ALA B 372 ? 1.4124 0.8554 1.2501 -0.1677 0.0894 -0.0235 372 ALA B N 10083 C CA . ALA B 372 ? 1.3740 0.8064 1.1743 -0.1682 0.0882 0.0016 372 ALA B CA 10084 C C . ALA B 372 ? 1.5566 0.9786 1.3341 -0.1879 0.1035 0.0087 372 ALA B C 10085 O O . ALA B 372 ? 1.7558 1.1855 1.5260 -0.2070 0.1177 -0.0040 372 ALA B O 10086 C CB . ALA B 372 ? 1.2833 0.7271 1.0691 -0.1657 0.0802 0.0079 372 ALA B CB 10087 N N . THR B 373 ? 1.4850 0.8888 1.2530 -0.1857 0.1013 0.0284 373 THR B N 10088 C CA . THR B 373 ? 1.2839 0.6737 1.0256 -0.2054 0.1099 0.0438 373 THR B CA 10089 C C . THR B 373 ? 1.2424 0.6241 0.9572 -0.2067 0.0949 0.0747 373 THR B C 10090 O O . THR B 373 ? 1.2654 0.6372 0.9939 -0.1910 0.0822 0.0920 373 THR B O 10091 C CB . THR B 373 ? 1.3454 0.7187 1.1025 -0.2043 0.1159 0.0471 373 THR B CB 10092 O OG1 . THR B 373 ? 1.4218 0.8024 1.2044 -0.2060 0.1289 0.0185 373 THR B OG1 10093 C CG2 . THR B 373 ? 1.4140 0.7701 1.1426 -0.2260 0.1207 0.0689 373 THR B CG2 10094 N N . CYS B 374 ? 1.2362 0.6221 0.9158 -0.2276 0.0968 0.0800 374 CYS B N 10095 C CA . CYS B 374 ? 1.2398 0.6194 0.8930 -0.2316 0.0787 0.1099 374 CYS B CA 10096 C C . CYS B 374 ? 1.5451 0.9060 1.1597 -0.2611 0.0773 0.1350 374 CYS B C 10097 O O . CYS B 374 ? 1.8920 1.2343 1.5106 -0.2586 0.0602 0.1662 374 CYS B O 10098 C CB . CYS B 374 ? 1.2300 0.6291 0.8681 -0.2344 0.0769 0.0996 374 CYS B CB 10099 S SG . CYS B 374 ? 1.6405 1.0601 1.3212 -0.2040 0.0752 0.0735 374 CYS B SG 10100 N N . LEU B 375 ? 1.4431 0.8082 1.0231 -0.2916 0.0953 0.1208 375 LEU B N 10101 C CA . LEU B 375 ? 1.4471 0.7932 0.9783 -0.3277 0.0949 0.1440 375 LEU B CA 10102 C C . LEU B 375 ? 1.4433 0.7778 0.9783 -0.3413 0.1156 0.1332 375 LEU B C 10103 O O . LEU B 375 ? 1.4505 0.7965 0.9877 -0.3536 0.1428 0.0983 375 LEU B O 10104 C CB . LEU B 375 ? 1.4084 0.7642 0.8873 -0.3617 0.1038 0.1356 375 LEU B CB 10105 C CG . LEU B 375 ? 1.5975 0.9334 1.0109 -0.4094 0.1056 0.1567 375 LEU B CG 10106 C CD1 . LEU B 375 ? 1.8358 1.1480 1.2336 -0.4107 0.0684 0.2097 375 LEU B CD1 10107 C CD2 . LEU B 375 ? 1.5946 0.9439 0.9582 -0.4453 0.1216 0.1375 375 LEU B CD2 10108 N N . ASN B 376 ? 1.4506 0.7626 0.9943 -0.3380 0.1027 0.1622 376 ASN B N 10109 C CA . ASN B 376 ? 1.4747 0.7710 1.0198 -0.3524 0.1183 0.1604 376 ASN B CA 10110 C C . ASN B 376 ? 1.4778 0.7886 1.0519 -0.3468 0.1487 0.1153 376 ASN B C 10111 O O . ASN B 376 ? 1.5098 0.8203 1.0595 -0.3767 0.1731 0.0962 376 ASN B O 10112 C CB . ASN B 376 ? 1.6135 0.8904 1.0930 -0.3998 0.1193 0.1831 376 ASN B CB 10113 C CG . ASN B 376 ? 1.7195 1.0096 1.1463 -0.4322 0.1338 0.1648 376 ASN B CG 10114 O OD1 . ASN B 376 ? 1.9359 1.2466 1.3766 -0.4324 0.1615 0.1216 376 ASN B OD1 10115 N ND2 . ASN B 376 ? 1.6236 0.9013 0.9925 -0.4624 0.1143 0.1976 376 ASN B ND2 10116 N N . ASN B 377 ? 1.5093 0.8316 1.1366 -0.3111 0.1462 0.0987 377 ASN B N 10117 C CA . ASN B 377 ? 1.5800 0.9145 1.2449 -0.3024 0.1670 0.0605 377 ASN B CA 10118 C C . ASN B 377 ? 1.6406 0.9947 1.3011 -0.3187 0.1872 0.0261 377 ASN B C 10119 O O . ASN B 377 ? 1.6643 1.0197 1.3345 -0.3357 0.2117 0.0002 377 ASN B O 10120 C CB . ASN B 377 ? 1.5916 0.9090 1.2628 -0.3139 0.1811 0.0607 377 ASN B CB 10121 C CG . ASN B 377 ? 1.6818 0.9770 1.3563 -0.3064 0.1632 0.0977 377 ASN B CG 10122 O OD1 . ASN B 377 ? 1.6986 0.9739 1.3418 -0.3310 0.1617 0.1229 377 ASN B OD1 10123 N ND2 . ASN B 377 ? 1.7399 1.0376 1.4549 -0.2748 0.1496 0.1006 377 ASN B ND2 10124 N N . GLU B 378 ? 1.6063 0.9758 1.2588 -0.3141 0.1784 0.0239 378 GLU B N 10125 C CA . GLU B 378 ? 1.6742 1.0640 1.3328 -0.3288 0.1976 -0.0104 378 GLU B CA 10126 C C . GLU B 378 ? 1.7803 1.1887 1.5036 -0.3027 0.1979 -0.0406 378 GLU B C 10127 O O . GLU B 378 ? 2.0107 1.4357 1.7614 -0.3129 0.2154 -0.0739 378 GLU B O 10128 C CB . GLU B 378 ? 1.7458 1.1442 1.3682 -0.3379 0.1883 0.0003 378 GLU B CB 10129 C CG . GLU B 378 ? 1.7370 1.1418 1.3764 -0.3036 0.1601 0.0174 378 GLU B CG 10130 C CD . GLU B 378 ? 2.0139 1.4283 1.6210 -0.3129 0.1519 0.0256 378 GLU B CD 10131 O OE1 . GLU B 378 ? 2.1647 1.5790 1.7294 -0.3486 0.1666 0.0210 378 GLU B OE1 10132 O OE2 . GLU B 378 ? 2.1571 1.5788 1.7792 -0.2870 0.1319 0.0353 378 GLU B OE2 10133 N N . VAL B 379 ? 1.6722 1.0769 1.4215 -0.2720 0.1778 -0.0286 379 VAL B N 10134 C CA . VAL B 379 ? 1.4720 0.8887 1.2762 -0.2490 0.1709 -0.0495 379 VAL B CA 10135 C C . VAL B 379 ? 1.3334 0.7729 1.1677 -0.2470 0.1709 -0.0735 379 VAL B C 10136 O O . VAL B 379 ? 1.2858 0.7359 1.1706 -0.2467 0.1776 -0.1014 379 VAL B O 10137 C CB . VAL B 379 ? 1.6154 1.0269 1.4537 -0.2528 0.1848 -0.0689 379 VAL B CB 10138 C CG1 . VAL B 379 ? 1.5894 0.9797 1.4117 -0.2475 0.1806 -0.0458 379 VAL B CG1 10139 C CG2 . VAL B 379 ? 1.5467 0.9616 1.3885 -0.2825 0.2148 -0.0948 379 VAL B CG2 10140 N N . ILE B 380 ? 1.3265 0.7733 1.1362 -0.2453 0.1617 -0.0620 380 ILE B N 10141 C CA . ILE B 380 ? 1.3052 0.7735 1.1462 -0.2419 0.1601 -0.0823 380 ILE B CA 10142 C C . ILE B 380 ? 1.3863 0.8607 1.2717 -0.2147 0.1370 -0.0845 380 ILE B C 10143 O O . ILE B 380 ? 1.4500 0.9173 1.3177 -0.1965 0.1169 -0.0622 380 ILE B O 10144 C CB . ILE B 380 ? 1.3266 0.8006 1.1276 -0.2467 0.1549 -0.0679 380 ILE B CB 10145 C CG1 . ILE B 380 ? 1.6022 1.0722 1.3573 -0.2819 0.1775 -0.0699 380 ILE B CG1 10146 C CG2 . ILE B 380 ? 1.2532 0.7491 1.0932 -0.2376 0.1494 -0.0863 380 ILE B CG2 10147 C CD1 . ILE B 380 ? 1.7489 1.2254 1.4632 -0.2919 0.1726 -0.0582 380 ILE B CD1 10148 N N . PRO B 381 ? 1.3721 0.8583 1.3172 -0.2147 0.1395 -0.1118 381 PRO B N 10149 C CA . PRO B 381 ? 1.3180 0.8078 1.3071 -0.1951 0.1143 -0.1133 381 PRO B CA 10150 C C . PRO B 381 ? 1.2773 0.7799 1.2786 -0.1834 0.0953 -0.1094 381 PRO B C 10151 O O . PRO B 381 ? 1.3222 0.8367 1.3177 -0.1913 0.1058 -0.1156 381 PRO B O 10152 C CB . PRO B 381 ? 1.3496 0.8471 1.4049 -0.2044 0.1244 -0.1439 381 PRO B CB 10153 C CG . PRO B 381 ? 1.3980 0.9063 1.4568 -0.2270 0.1550 -0.1658 381 PRO B CG 10154 C CD . PRO B 381 ? 1.4287 0.9252 1.4069 -0.2375 0.1670 -0.1440 381 PRO B CD 10155 N N . GLY B 382 ? 1.2446 0.7439 1.2596 -0.1675 0.0679 -0.0992 382 GLY B N 10156 C CA . GLY B 382 ? 1.2559 0.7659 1.2903 -0.1577 0.0471 -0.0959 382 GLY B CA 10157 C C . GLY B 382 ? 1.1913 0.6998 1.1747 -0.1498 0.0428 -0.0755 382 GLY B C 10158 O O . GLY B 382 ? 1.3374 0.8529 1.3310 -0.1412 0.0253 -0.0705 382 GLY B O 10159 N N . LEU B 383 ? 1.0996 0.5982 1.0319 -0.1532 0.0568 -0.0624 383 LEU B N 10160 C CA . LEU B 383 ? 1.1256 0.6231 1.0167 -0.1471 0.0529 -0.0436 383 LEU B CA 10161 C C . LEU B 383 ? 1.1781 0.6572 1.0358 -0.1367 0.0442 -0.0219 383 LEU B C 10162 O O . LEU B 383 ? 1.2295 0.6953 1.0756 -0.1403 0.0522 -0.0172 383 LEU B O 10163 C CB . LEU B 383 ? 1.1583 0.6598 1.0216 -0.1629 0.0727 -0.0442 383 LEU B CB 10164 C CG . LEU B 383 ? 1.3571 0.8618 1.1869 -0.1594 0.0670 -0.0280 383 LEU B CG 10165 C CD1 . LEU B 383 ? 1.4805 1.0001 1.3382 -0.1478 0.0537 -0.0346 383 LEU B CD1 10166 C CD2 . LEU B 383 ? 1.4880 0.9973 1.2892 -0.1821 0.0850 -0.0310 383 LEU B CD2 10167 N N . LYS B 384 ? 1.1437 0.6223 0.9909 -0.1249 0.0296 -0.0108 384 LYS B N 10168 C CA . LYS B 384 ? 1.1064 0.5687 0.9293 -0.1168 0.0250 0.0051 384 LYS B CA 10169 C C . LYS B 384 ? 1.1802 0.6389 0.9768 -0.1146 0.0290 0.0221 384 LYS B C 10170 O O . LYS B 384 ? 1.2882 0.7345 1.0746 -0.1076 0.0265 0.0342 384 LYS B O 10171 C CB . LYS B 384 ? 1.1059 0.5667 0.9322 -0.1093 0.0082 0.0055 384 LYS B CB 10172 C CG . LYS B 384 ? 1.3733 0.8449 1.1969 -0.1030 -0.0003 0.0096 384 LYS B CG 10173 C CD . LYS B 384 ? 1.4283 0.8966 1.2534 -0.1002 -0.0179 0.0101 384 LYS B CD 10174 C CE . LYS B 384 ? 1.5453 1.0183 1.4019 -0.1066 -0.0317 -0.0003 384 LYS B CE 10175 N NZ . LYS B 384 ? 1.6490 1.1172 1.5031 -0.1085 -0.0541 0.0046 384 LYS B NZ 10176 N N . SER B 385 ? 1.1878 0.6570 0.9765 -0.1228 0.0351 0.0220 385 SER B N 10177 C CA . SER B 385 ? 1.2685 0.7346 1.0317 -0.1236 0.0337 0.0405 385 SER B CA 10178 C C . SER B 385 ? 1.2488 0.7115 0.9904 -0.1425 0.0442 0.0467 385 SER B C 10179 O O . SER B 385 ? 1.1810 0.6494 0.9273 -0.1566 0.0572 0.0306 385 SER B O 10180 C CB . SER B 385 ? 1.4257 0.9072 1.1886 -0.1189 0.0266 0.0386 385 SER B CB 10181 O OG . SER B 385 ? 1.5948 1.0939 1.3741 -0.1278 0.0333 0.0184 385 SER B OG 10182 N N . CYS B 386 ? 1.3224 0.7746 1.0421 -0.1450 0.0377 0.0703 386 CYS B N 10183 C CA . CYS B 386 ? 1.2366 0.6819 0.9266 -0.1674 0.0424 0.0828 386 CYS B CA 10184 C C . CYS B 386 ? 1.2009 0.6473 0.8656 -0.1735 0.0295 0.1030 386 CYS B C 10185 O O . CYS B 386 ? 1.1771 0.6157 0.8511 -0.1590 0.0142 0.1215 386 CYS B O 10186 C CB . CYS B 386 ? 1.1493 0.5733 0.8413 -0.1693 0.0424 0.0984 386 CYS B CB 10187 S SG . CYS B 386 ? 2.0243 1.4458 1.7422 -0.1664 0.0577 0.0754 386 CYS B SG 10188 N N . MET B 387 ? 1.2217 0.6777 0.8565 -0.1972 0.0367 0.0975 387 MET B N 10189 C CA . MET B 387 ? 1.2534 0.7118 0.8589 -0.2078 0.0237 0.1153 387 MET B CA 10190 C C . MET B 387 ? 1.2876 0.7289 0.8503 -0.2369 0.0170 0.1414 387 MET B C 10191 O O . MET B 387 ? 1.3213 0.7489 0.8773 -0.2487 0.0248 0.1447 387 MET B O 10192 C CB . MET B 387 ? 1.2613 0.7433 0.8599 -0.2182 0.0353 0.0904 387 MET B CB 10193 C CG . MET B 387 ? 1.2902 0.7790 0.8721 -0.2485 0.0604 0.0665 387 MET B CG 10194 S SD . MET B 387 ? 2.1323 1.6458 1.6977 -0.2721 0.0748 0.0418 387 MET B SD 10195 C CE . MET B 387 ? 1.2508 0.7533 0.7588 -0.2888 0.0505 0.0800 387 MET B CE 10196 N N . GLY B 388 ? 1.3079 0.7491 0.8404 -0.2505 0.0009 0.1610 388 GLY B N 10197 C CA . GLY B 388 ? 1.4091 0.8333 0.8930 -0.2842 -0.0113 0.1899 388 GLY B CA 10198 C C . GLY B 388 ? 1.5757 0.9735 1.0750 -0.2781 -0.0302 0.2233 388 GLY B C 10199 O O . GLY B 388 ? 1.6967 1.0785 1.1688 -0.3033 -0.0277 0.2356 388 GLY B O 10200 N N . LEU B 389 ? 1.5818 0.9747 1.1281 -0.2467 -0.0479 0.2371 389 LEU B N 10201 C CA . LEU B 389 ? 1.5532 0.9229 1.1327 -0.2372 -0.0625 0.2632 389 LEU B CA 10202 C C . LEU B 389 ? 1.5065 0.8622 1.1000 -0.2372 -0.0979 0.3025 389 LEU B C 10203 O O . LEU B 389 ? 1.3589 0.7251 0.9493 -0.2331 -0.1105 0.3055 389 LEU B O 10204 C CB . LEU B 389 ? 1.4205 0.7933 1.0568 -0.2025 -0.0491 0.2420 389 LEU B CB 10205 C CG . LEU B 389 ? 1.3327 0.7161 0.9666 -0.2007 -0.0200 0.2070 389 LEU B CG 10206 C CD1 . LEU B 389 ? 1.2316 0.6153 0.9150 -0.1711 -0.0118 0.1905 389 LEU B CD1 10207 C CD2 . LEU B 389 ? 1.4714 0.8419 1.0788 -0.2265 -0.0110 0.2127 389 LEU B CD2 10208 N N . LYS B 390 ? 1.5625 0.8943 1.1773 -0.2422 -0.1149 0.3328 390 LYS B N 10209 C CA . LYS B 390 ? 1.5538 0.8692 1.2020 -0.2401 -0.1519 0.3723 390 LYS B CA 10210 C C . LYS B 390 ? 1.5927 0.8969 1.3245 -0.2100 -0.1519 0.3733 390 LYS B C 10211 O O . LYS B 390 ? 1.7206 1.0242 1.4687 -0.2002 -0.1272 0.3519 390 LYS B O 10212 C CB . LYS B 390 ? 1.5404 0.8412 1.1481 -0.2768 -0.1771 0.4099 390 LYS B CB 10213 C CG . LYS B 390 ? 1.6273 0.9346 1.1437 -0.3162 -0.1733 0.4075 390 LYS B CG 10214 C CD . LYS B 390 ? 1.8348 1.1404 1.3156 -0.3503 -0.1928 0.4337 390 LYS B CD 10215 C CE . LYS B 390 ? 1.9144 1.2272 1.3016 -0.3948 -0.1836 0.4250 390 LYS B CE 10216 N NZ . LYS B 390 ? 1.8549 1.1634 1.2002 -0.4325 -0.2019 0.4481 390 LYS B NZ 10217 N N . ILE B 391 ? 1.4752 0.7765 1.2653 -0.1950 -0.1764 0.3924 391 ILE B N 10218 C CA . ILE B 391 ? 1.3825 0.6801 1.2616 -0.1679 -0.1719 0.3868 391 ILE B CA 10219 C C . ILE B 391 ? 1.3912 0.6791 1.2881 -0.1772 -0.1739 0.4016 391 ILE B C 10220 O O . ILE B 391 ? 1.5042 0.7928 1.3811 -0.1976 -0.1977 0.4297 391 ILE B O 10221 C CB . ILE B 391 ? 1.3738 0.6823 1.3196 -0.1504 -0.1936 0.3964 391 ILE B CB 10222 C CG1 . ILE B 391 ? 1.3772 0.6936 1.3217 -0.1349 -0.1851 0.3759 391 ILE B CG1 10223 C CG2 . ILE B 391 ? 1.3400 0.6449 1.3786 -0.1305 -0.1886 0.3915 391 ILE B CG2 10224 C CD1 . ILE B 391 ? 1.4811 0.8064 1.3581 -0.1524 -0.2010 0.3863 391 ILE B CD1 10225 N N . GLY B 392 ? 1.3347 0.6132 1.2681 -0.1640 -0.1497 0.3822 392 GLY B N 10226 C CA . GLY B 392 ? 1.5970 0.8652 1.5485 -0.1715 -0.1474 0.3925 392 GLY B CA 10227 C C . GLY B 392 ? 1.6753 0.9327 1.5687 -0.1874 -0.1238 0.3790 392 GLY B C 10228 O O . GLY B 392 ? 1.7694 1.0169 1.6801 -0.1909 -0.1144 0.3800 392 GLY B O 10229 N N . ASP B 393 ? 1.5231 0.7907 1.3516 -0.1949 -0.1109 0.3598 393 ASP B N 10230 C CA . ASP B 393 ? 1.5628 0.8396 1.3451 -0.2035 -0.0811 0.3315 393 ASP B CA 10231 C C . ASP B 393 ? 1.4758 0.7629 1.2971 -0.1773 -0.0527 0.2929 393 ASP B C 10232 O O . ASP B 393 ? 1.2766 0.5704 1.1391 -0.1549 -0.0509 0.2801 393 ASP B O 10233 C CB . ASP B 393 ? 1.6612 0.9564 1.3723 -0.2196 -0.0743 0.3177 393 ASP B CB 10234 C CG . ASP B 393 ? 1.7111 0.9950 1.3655 -0.2559 -0.0966 0.3515 393 ASP B CG 10235 O OD1 . ASP B 393 ? 1.7079 0.9692 1.3598 -0.2750 -0.1099 0.3808 393 ASP B OD1 10236 O OD2 . ASP B 393 ? 1.6809 0.9778 1.2915 -0.2679 -0.1012 0.3489 393 ASP B OD2 10237 N N . THR B 394 ? 1.4963 0.7836 1.3025 -0.1832 -0.0306 0.2744 394 THR B N 10238 C CA . THR B 394 ? 1.2479 0.5434 1.0835 -0.1640 -0.0061 0.2394 394 THR B CA 10239 C C . THR B 394 ? 1.2354 0.5466 1.0276 -0.1710 0.0147 0.2100 394 THR B C 10240 O O . THR B 394 ? 1.4771 0.7846 1.2341 -0.1923 0.0200 0.2139 394 THR B O 10241 C CB . THR B 394 ? 1.2747 0.5527 1.1591 -0.1608 0.0000 0.2439 394 THR B CB 10242 O OG1 . THR B 394 ? 1.5591 0.8212 1.4957 -0.1565 -0.0213 0.2731 394 THR B OG1 10243 C CG2 . THR B 394 ? 1.2069 0.4928 1.1207 -0.1434 0.0237 0.2075 394 THR B CG2 10244 N N . VAL B 395 ? 1.1905 0.5182 0.9884 -0.1553 0.0260 0.1806 395 VAL B N 10245 C CA . VAL B 395 ? 1.2926 0.6357 1.0646 -0.1600 0.0420 0.1525 395 VAL B CA 10246 C C . VAL B 395 ? 1.2224 0.5670 1.0217 -0.1478 0.0564 0.1268 395 VAL B C 10247 O O . VAL B 395 ? 1.1283 0.4666 0.9603 -0.1347 0.0564 0.1249 395 VAL B O 10248 C CB . VAL B 395 ? 1.2552 0.6179 1.0057 -0.1569 0.0384 0.1415 395 VAL B CB 10249 C CG1 . VAL B 395 ? 1.2429 0.6060 0.9566 -0.1755 0.0275 0.1620 395 VAL B CG1 10250 C CG2 . VAL B 395 ? 1.1705 0.5369 0.9468 -0.1358 0.0315 0.1379 395 VAL B CG2 10251 N N . SER B 396 ? 1.1434 0.4963 0.9311 -0.1549 0.0690 0.1057 396 SER B N 10252 C CA . SER B 396 ? 1.1415 0.4956 0.9510 -0.1474 0.0793 0.0824 396 SER B CA 10253 C C . SER B 396 ? 1.2166 0.5888 1.0206 -0.1446 0.0797 0.0585 396 SER B C 10254 O O . SER B 396 ? 1.2532 0.6373 1.0411 -0.1526 0.0800 0.0541 396 SER B O 10255 C CB . SER B 396 ? 1.1557 0.4996 0.9711 -0.1585 0.0916 0.0799 396 SER B CB 10256 O OG . SER B 396 ? 1.2805 0.6269 1.1151 -0.1533 0.1000 0.0563 396 SER B OG 10257 N N . PHE B 397 ? 1.2270 0.6005 1.0468 -0.1358 0.0792 0.0431 397 PHE B N 10258 C CA . PHE B 397 ? 1.1714 0.5591 0.9926 -0.1344 0.0741 0.0238 397 PHE B CA 10259 C C . PHE B 397 ? 1.2484 0.6322 1.0856 -0.1366 0.0774 0.0069 397 PHE B C 10260 O O . PHE B 397 ? 1.3025 0.6759 1.1449 -0.1341 0.0797 0.0056 397 PHE B O 10261 C CB . PHE B 397 ? 1.1740 0.5675 0.9893 -0.1248 0.0623 0.0253 397 PHE B CB 10262 C CG . PHE B 397 ? 1.1225 0.5223 0.9240 -0.1224 0.0569 0.0396 397 PHE B CG 10263 C CD1 . PHE B 397 ? 1.1882 0.5786 0.9888 -0.1172 0.0547 0.0575 397 PHE B CD1 10264 C CD2 . PHE B 397 ? 1.1225 0.5382 0.9177 -0.1263 0.0539 0.0336 397 PHE B CD2 10265 C CE1 . PHE B 397 ? 1.3126 0.7086 1.1005 -0.1162 0.0468 0.0716 397 PHE B CE1 10266 C CE2 . PHE B 397 ? 1.2753 0.6975 1.0553 -0.1263 0.0495 0.0452 397 PHE B CE2 10267 C CZ . PHE B 397 ? 1.3808 0.7928 1.1541 -0.1214 0.0445 0.0654 397 PHE B CZ 10268 N N . SER B 398 ? 1.3687 0.7609 1.2171 -0.1430 0.0783 -0.0077 398 SER B N 10269 C CA . SER B 398 ? 1.3143 0.7046 1.1803 -0.1459 0.0758 -0.0236 398 SER B CA 10270 C C . SER B 398 ? 1.2907 0.6900 1.1603 -0.1438 0.0562 -0.0309 398 SER B C 10271 O O . SER B 398 ? 1.1354 0.5476 1.0119 -0.1425 0.0483 -0.0325 398 SER B O 10272 C CB . SER B 398 ? 1.2745 0.6675 1.1604 -0.1549 0.0861 -0.0361 398 SER B CB 10273 O OG . SER B 398 ? 1.3999 0.8075 1.2957 -0.1588 0.0856 -0.0438 398 SER B OG 10274 N N . ILE B 399 ? 1.2601 0.6516 1.1247 -0.1462 0.0483 -0.0349 399 ILE B N 10275 C CA . ILE B 399 ? 1.0780 0.4735 0.9376 -0.1484 0.0263 -0.0370 399 ILE B CA 10276 C C . ILE B 399 ? 1.0768 0.4689 0.9487 -0.1593 0.0125 -0.0481 399 ILE B C 10277 O O . ILE B 399 ? 1.1786 0.5599 1.0453 -0.1659 0.0214 -0.0539 399 ILE B O 10278 C CB . ILE B 399 ? 1.0839 0.4713 0.9139 -0.1474 0.0261 -0.0298 399 ILE B CB 10279 C CG1 . ILE B 399 ? 1.0959 0.4862 0.9193 -0.1364 0.0363 -0.0174 399 ILE B CG1 10280 C CG2 . ILE B 399 ? 1.1068 0.4962 0.9246 -0.1536 0.0025 -0.0297 399 ILE B CG2 10281 C CD1 . ILE B 399 ? 1.2948 0.6771 1.0996 -0.1346 0.0392 -0.0127 399 ILE B CD1 10282 N N . GLU B 400 ? 1.1213 0.5223 1.0138 -0.1622 -0.0107 -0.0505 400 GLU B N 10283 C CA . GLU B 400 ? 1.1920 0.5891 1.0992 -0.1744 -0.0324 -0.0571 400 GLU B CA 10284 C C . GLU B 400 ? 1.1291 0.5208 1.0100 -0.1843 -0.0596 -0.0483 400 GLU B C 10285 O O . GLU B 400 ? 1.0974 0.4960 0.9778 -0.1792 -0.0713 -0.0399 400 GLU B O 10286 C CB . GLU B 400 ? 1.3294 0.7388 1.2931 -0.1735 -0.0425 -0.0662 400 GLU B CB 10287 C CG . GLU B 400 ? 1.3160 0.7210 1.3058 -0.1859 -0.0663 -0.0725 400 GLU B CG 10288 C CD . GLU B 400 ? 1.4415 0.8595 1.5011 -0.1849 -0.0818 -0.0814 400 GLU B CD 10289 O OE1 . GLU B 400 ? 1.4266 0.8429 1.5235 -0.1923 -0.0919 -0.0911 400 GLU B OE1 10290 O OE2 . GLU B 400 ? 1.5788 1.0091 1.6614 -0.1776 -0.0831 -0.0806 400 GLU B OE2 10291 N N . ALA B 401 ? 1.2032 0.5818 1.0593 -0.2012 -0.0690 -0.0506 401 ALA B N 10292 C CA . ALA B 401 ? 1.2824 0.6520 1.1027 -0.2181 -0.0949 -0.0420 401 ALA B CA 10293 C C . ALA B 401 ? 1.3847 0.7498 1.2198 -0.2367 -0.1310 -0.0407 401 ALA B C 10294 O O . ALA B 401 ? 1.4483 0.8054 1.2782 -0.2492 -0.1286 -0.0496 401 ALA B O 10295 C CB . ALA B 401 ? 1.2606 0.6159 1.0274 -0.2297 -0.0741 -0.0461 401 ALA B CB 10296 N N . LYS B 402 ? 1.3300 0.6998 1.1879 -0.2392 -0.1663 -0.0288 402 LYS B N 10297 C CA . LYS B 402 ? 1.3359 0.7007 1.2171 -0.2576 -0.2087 -0.0228 402 LYS B CA 10298 C C . LYS B 402 ? 1.3597 0.7123 1.1999 -0.2799 -0.2458 -0.0038 402 LYS B C 10299 O O . LYS B 402 ? 1.3924 0.7502 1.2357 -0.2722 -0.2543 0.0072 402 LYS B O 10300 C CB . LYS B 402 ? 1.4686 0.8495 1.4369 -0.2430 -0.2236 -0.0257 402 LYS B CB 10301 C CG . LYS B 402 ? 1.6997 1.0758 1.7104 -0.2599 -0.2678 -0.0209 402 LYS B CG 10302 C CD . LYS B 402 ? 1.8391 1.2320 1.9502 -0.2450 -0.2753 -0.0301 402 LYS B CD 10303 C CE . LYS B 402 ? 1.9639 1.3516 2.1286 -0.2610 -0.3191 -0.0267 402 LYS B CE 10304 N NZ . LYS B 402 ? 2.0429 1.4167 2.1844 -0.2843 -0.3738 0.0000 402 LYS B NZ 10305 N N . VAL B 403 ? 1.3644 0.7001 1.1638 -0.3103 -0.2679 0.0001 403 VAL B N 10306 C CA . VAL B 403 ? 1.4022 0.7223 1.1523 -0.3398 -0.3058 0.0198 403 VAL B CA 10307 C C . VAL B 403 ? 1.4736 0.7906 1.2705 -0.3547 -0.3648 0.0372 403 VAL B C 10308 O O . VAL B 403 ? 1.5566 0.8755 1.3948 -0.3565 -0.3753 0.0302 403 VAL B O 10309 C CB . VAL B 403 ? 1.5642 0.8642 1.2245 -0.3729 -0.2914 0.0130 403 VAL B CB 10310 C CG1 . VAL B 403 ? 1.5365 0.8313 1.2001 -0.3871 -0.2911 0.0002 403 VAL B CG1 10311 C CG2 . VAL B 403 ? 1.7230 1.0045 1.3217 -0.4095 -0.3292 0.0335 403 VAL B CG2 10312 N N . ARG B 404 ? 1.4330 0.7452 1.2301 -0.3651 -0.4047 0.0607 404 ARG B N 10313 C CA . ARG B 404 ? 1.4727 0.7787 1.3162 -0.3832 -0.4683 0.0824 404 ARG B CA 10314 C C . ARG B 404 ? 1.5452 0.8253 1.3021 -0.4309 -0.5020 0.0994 404 ARG B C 10315 O O . ARG B 404 ? 1.5733 0.8401 1.2588 -0.4519 -0.5084 0.1133 404 ARG B O 10316 C CB . ARG B 404 ? 1.4711 0.7861 1.3733 -0.3695 -0.4971 0.1007 404 ARG B CB 10317 C CG . ARG B 404 ? 1.6271 0.9540 1.5997 -0.3731 -0.5550 0.1240 404 ARG B CG 10318 C CD . ARG B 404 ? 1.5935 0.9387 1.6407 -0.3513 -0.5734 0.1371 404 ARG B CD 10319 N NE . ARG B 404 ? 1.6859 1.0160 1.6639 -0.3671 -0.5849 0.1575 404 ARG B NE 10320 C CZ . ARG B 404 ? 1.7055 1.0335 1.6600 -0.3547 -0.5502 0.1474 404 ARG B CZ 10321 N NH1 . ARG B 404 ? 1.7347 1.0775 1.7251 -0.3245 -0.5014 0.1192 404 ARG B NH1 10322 N NH2 . ARG B 404 ? 1.6594 0.9736 1.5522 -0.3710 -0.5622 0.1662 404 ARG B NH2 10323 N N . GLY B 405 ? 1.6035 0.8842 1.3660 -0.4446 -0.5179 0.0978 405 GLY B N 10324 C CA . GLY B 405 ? 1.8105 1.0745 1.4836 -0.4873 -0.5376 0.1094 405 GLY B CA 10325 C C . GLY B 405 ? 2.0441 1.2911 1.6170 -0.5070 -0.4876 0.0879 405 GLY B C 10326 O O . GLY B 405 ? 2.3030 1.5536 1.8856 -0.4869 -0.4369 0.0593 405 GLY B O 10327 N N . CYS B 406 ? 1.9744 1.2064 1.4557 -0.5434 -0.4983 0.1022 406 CYS B N 10328 C CA . CYS B 406 ? 2.0499 1.2681 1.4391 -0.5643 -0.4489 0.0810 406 CYS B CA 10329 C C . CYS B 406 ? 2.1247 1.3283 1.4237 -0.6068 -0.4723 0.1040 406 CYS B C 10330 O O . CYS B 406 ? 2.2332 1.4315 1.5100 -0.6339 -0.5149 0.1275 406 CYS B O 10331 C CB . CYS B 406 ? 2.2458 1.4621 1.6104 -0.5745 -0.4089 0.0496 406 CYS B CB 10332 S SG . CYS B 406 ? 2.3516 1.5684 1.7067 -0.6042 -0.4495 0.0610 406 CYS B SG 10333 N N . PRO B 407 ? 2.1125 1.3076 1.3583 -0.6138 -0.4435 0.0983 407 PRO B N 10334 C CA . PRO B 407 ? 2.4804 1.6600 1.6417 -0.6545 -0.4648 0.1224 407 PRO B CA 10335 C C . PRO B 407 ? 2.5382 1.7052 1.5997 -0.6994 -0.4294 0.1040 407 PRO B C 10336 O O . PRO B 407 ? 2.4792 1.6348 1.4698 -0.7242 -0.4064 0.1017 407 PRO B O 10337 C CB . PRO B 407 ? 2.4898 1.6681 1.6513 -0.6380 -0.4462 0.1214 407 PRO B CB 10338 C CG . PRO B 407 ? 2.2733 1.4590 1.4681 -0.6069 -0.3870 0.0822 407 PRO B CG 10339 C CD . PRO B 407 ? 2.0027 1.2001 1.2671 -0.5848 -0.3932 0.0734 407 PRO B CD 10340 N N . GLN B 408 ? 2.4812 1.6512 1.5412 -0.7106 -0.4246 0.0909 408 GLN B N 10341 C CA . GLN B 408 ? 2.5202 1.6814 1.4947 -0.7538 -0.3892 0.0707 408 GLN B CA 10342 C C . GLN B 408 ? 2.6713 1.8292 1.5982 -0.7615 -0.3241 0.0395 408 GLN B C 10343 O O . GLN B 408 ? 2.8093 1.9539 1.6559 -0.8008 -0.3148 0.0458 408 GLN B O 10344 C CB . GLN B 408 ? 2.5273 1.6710 1.4301 -0.8032 -0.4345 0.1071 408 GLN B CB 10345 C CG . GLN B 408 ? 2.6467 1.7824 1.4691 -0.8506 -0.4033 0.0882 408 GLN B CG 10346 C CD . GLN B 408 ? 2.5807 1.7318 1.4473 -0.8334 -0.3757 0.0537 408 GLN B CD 10347 O OE1 . GLN B 408 ? 2.5809 1.7416 1.5206 -0.8058 -0.4104 0.0628 408 GLN B OE1 10348 N NE2 . GLN B 408 ? 2.4899 1.6438 1.3188 -0.8494 -0.3110 0.0129 408 GLN B NE2 10349 N N . GLU B 409 ? 2.6320 1.8007 1.6129 -0.7243 -0.2786 0.0071 409 GLU B N 10350 C CA . GLU B 409 ? 2.5976 1.7647 1.5537 -0.7243 -0.2186 -0.0218 409 GLU B CA 10351 C C . GLU B 409 ? 2.6612 1.8335 1.6053 -0.7365 -0.1588 -0.0634 409 GLU B C 10352 O O . GLU B 409 ? 2.6226 1.7994 1.5764 -0.7430 -0.1644 -0.0697 409 GLU B O 10353 C CB . GLU B 409 ? 2.4493 1.6223 1.4771 -0.6744 -0.2078 -0.0259 409 GLU B CB 10354 C CG . GLU B 409 ? 2.4275 1.5959 1.4310 -0.6740 -0.1690 -0.0387 409 GLU B CG 10355 C CD . GLU B 409 ? 2.5956 1.7530 1.5406 -0.7016 -0.2027 -0.0088 409 GLU B CD 10356 O OE1 . GLU B 409 ? 2.6319 1.7866 1.5800 -0.7066 -0.2638 0.0281 409 GLU B OE1 10357 O OE2 . GLU B 409 ? 2.7376 1.8891 1.6393 -0.7180 -0.1676 -0.0216 409 GLU B OE2 10358 N N . LYS B 410 ? 2.7130 1.8859 1.6436 -0.7385 -0.1012 -0.0923 410 LYS B N 10359 C CA . LYS B 410 ? 2.7639 1.9453 1.7060 -0.7423 -0.0393 -0.1344 410 LYS B CA 10360 C C . LYS B 410 ? 2.5993 1.7893 1.6297 -0.6901 -0.0095 -0.1529 410 LYS B C 10361 O O . LYS B 410 ? 2.6120 1.8086 1.6941 -0.6686 -0.0064 -0.1618 410 LYS B O 10362 C CB . LYS B 410 ? 2.8143 1.9929 1.6969 -0.7796 0.0090 -0.1561 410 LYS B CB 10363 C CG . LYS B 410 ? 2.8246 1.9908 1.6111 -0.8378 -0.0147 -0.1364 410 LYS B CG 10364 C CD . LYS B 410 ? 2.7303 1.8985 1.4993 -0.8615 -0.0273 -0.1380 410 LYS B CD 10365 C CE . LYS B 410 ? 2.8375 1.9901 1.5080 -0.9231 -0.0507 -0.1151 410 LYS B CE 10366 N NZ . LYS B 410 ? 2.8522 1.9900 1.4981 -0.9267 -0.1198 -0.0641 410 LYS B NZ 10367 N N . GLU B 411 ? 2.3231 1.5117 1.3702 -0.6710 0.0118 -0.1569 411 GLU B N 10368 C CA . GLU B 411 ? 2.1299 1.3233 1.2579 -0.6217 0.0343 -0.1666 411 GLU B CA 10369 C C . GLU B 411 ? 1.9929 1.1806 1.1298 -0.6010 0.0238 -0.1502 411 GLU B C 10370 O O . GLU B 411 ? 2.0270 1.2101 1.1151 -0.6242 0.0295 -0.1491 411 GLU B O 10371 C CB . GLU B 411 ? 2.2955 1.4986 1.4589 -0.6167 0.1000 -0.2059 411 GLU B CB 10372 C CG . GLU B 411 ? 2.2591 1.4663 1.5085 -0.5669 0.1231 -0.2124 411 GLU B CG 10373 C CD . GLU B 411 ? 2.2727 1.4918 1.5692 -0.5614 0.1833 -0.2477 411 GLU B CD 10374 O OE1 . GLU B 411 ? 2.2551 1.4780 1.6242 -0.5227 0.2029 -0.2511 411 GLU B OE1 10375 O OE2 . GLU B 411 ? 2.2882 1.5134 1.5523 -0.5964 0.2102 -0.2706 411 GLU B OE2 10376 N N . LYS B 412 ? 1.8602 1.0619 1.0677 -0.5490 0.0109 -0.1336 412 LYS B N 10377 C CA . LYS B 412 ? 1.8250 1.0365 1.0621 -0.5149 0.0107 -0.1193 412 LYS B CA 10378 C C . LYS B 412 ? 1.7152 0.9445 1.0334 -0.4655 0.0437 -0.1288 412 LYS B C 10379 O O . LYS B 412 ? 1.7435 0.9769 1.0950 -0.4577 0.0630 -0.1435 412 LYS B O 10380 C CB . LYS B 412 ? 1.8843 1.1028 1.1285 -0.4988 -0.0461 -0.0812 412 LYS B CB 10381 C CG . LYS B 412 ? 2.0091 1.2085 1.1776 -0.5442 -0.0828 -0.0641 412 LYS B CG 10382 C CD . LYS B 412 ? 2.0316 1.2201 1.1580 -0.5625 -0.0557 -0.0746 412 LYS B CD 10383 C CE . LYS B 412 ? 2.0218 1.1930 1.0809 -0.6003 -0.0989 -0.0490 412 LYS B CE 10384 N NZ . LYS B 412 ? 1.9199 1.1048 1.0261 -0.5651 -0.1474 -0.0126 412 LYS B NZ 10385 N N . SER B 413 ? 1.5951 0.8342 0.9444 -0.4340 0.0483 -0.1189 413 SER B N 10386 C CA . SER B 413 ? 1.4781 0.7325 0.9007 -0.3895 0.0726 -0.1221 413 SER B CA 10387 C C . SER B 413 ? 1.4891 0.7580 0.9412 -0.3531 0.0529 -0.0977 413 SER B C 10388 O O . SER B 413 ? 1.6517 0.9167 1.0727 -0.3622 0.0402 -0.0886 413 SER B O 10389 C CB . SER B 413 ? 1.4730 0.7202 0.9115 -0.3978 0.1240 -0.1530 413 SER B CB 10390 O OG . SER B 413 ? 1.6352 0.8710 1.0553 -0.4310 0.1475 -0.1799 413 SER B OG 10391 N N . PHE B 414 ? 1.3580 0.6430 0.8679 -0.3146 0.0514 -0.0877 414 PHE B N 10392 C CA . PHE B 414 ? 1.2741 0.5738 0.8152 -0.2810 0.0399 -0.0690 414 PHE B CA 10393 C C . PHE B 414 ? 1.2837 0.5922 0.8811 -0.2507 0.0648 -0.0720 414 PHE B C 10394 O O . PHE B 414 ? 1.3409 0.6471 0.9610 -0.2501 0.0816 -0.0825 414 PHE B O 10395 C CB . PHE B 414 ? 1.2384 0.5496 0.7876 -0.2693 -0.0004 -0.0468 414 PHE B CB 10396 C CG . PHE B 414 ? 1.2015 0.5201 0.7835 -0.2579 -0.0050 -0.0463 414 PHE B CG 10397 C CD1 . PHE B 414 ? 1.1585 0.4917 0.7882 -0.2262 0.0016 -0.0400 414 PHE B CD1 10398 C CD2 . PHE B 414 ? 1.2332 0.5432 0.7957 -0.2816 -0.0165 -0.0520 414 PHE B CD2 10399 C CE1 . PHE B 414 ? 1.2198 0.5585 0.8776 -0.2183 -0.0002 -0.0408 414 PHE B CE1 10400 C CE2 . PHE B 414 ? 1.2166 0.5333 0.8125 -0.2710 -0.0196 -0.0529 414 PHE B CE2 10401 C CZ . PHE B 414 ? 1.1732 0.5040 0.8170 -0.2393 -0.0101 -0.0479 414 PHE B CZ 10402 N N . THR B 415 ? 1.1858 0.5035 0.8059 -0.2272 0.0651 -0.0614 415 THR B N 10403 C CA . THR B 415 ? 1.1419 0.4653 0.8126 -0.2022 0.0841 -0.0602 415 THR B CA 10404 C C . THR B 415 ? 1.1017 0.4417 0.7969 -0.1744 0.0647 -0.0386 415 THR B C 10405 O O . THR B 415 ? 1.1139 0.4629 0.7990 -0.1671 0.0461 -0.0267 415 THR B O 10406 C CB . THR B 415 ? 1.1439 0.4621 0.8273 -0.2011 0.1058 -0.0690 415 THR B CB 10407 O OG1 . THR B 415 ? 1.1852 0.4874 0.8479 -0.2313 0.1306 -0.0948 415 THR B OG1 10408 C CG2 . THR B 415 ? 1.3211 0.6435 1.0634 -0.1768 0.1193 -0.0640 415 THR B CG2 10409 N N . ILE B 416 ? 1.1510 0.4943 0.8779 -0.1619 0.0706 -0.0349 416 ILE B N 10410 C CA . ILE B 416 ? 1.1361 0.4932 0.8839 -0.1407 0.0585 -0.0172 416 ILE B CA 10411 C C . ILE B 416 ? 1.1295 0.4855 0.9110 -0.1260 0.0718 -0.0099 416 ILE B C 10412 O O . ILE B 416 ? 1.2145 0.5611 1.0222 -0.1274 0.0887 -0.0153 416 ILE B O 10413 C CB . ILE B 416 ? 1.1959 0.5567 0.9519 -0.1406 0.0527 -0.0159 416 ILE B CB 10414 C CG1 . ILE B 416 ? 1.2335 0.5942 0.9653 -0.1561 0.0353 -0.0220 416 ILE B CG1 10415 C CG2 . ILE B 416 ? 1.2156 0.5898 0.9878 -0.1246 0.0443 -0.0010 416 ILE B CG2 10416 C CD1 . ILE B 416 ? 1.0651 0.4287 0.8110 -0.1575 0.0305 -0.0242 416 ILE B CD1 10417 N N . LYS B 417 ? 1.0348 0.3999 0.8197 -0.1130 0.0625 0.0032 417 LYS B N 10418 C CA . LYS B 417 ? 1.0484 0.4117 0.8660 -0.1007 0.0688 0.0138 417 LYS B CA 10419 C C . LYS B 417 ? 1.0379 0.4147 0.8536 -0.0883 0.0524 0.0330 417 LYS B C 10420 O O . LYS B 417 ? 1.0761 0.4647 0.8691 -0.0878 0.0399 0.0338 417 LYS B O 10421 C CB . LYS B 417 ? 1.0775 0.4332 0.9066 -0.1030 0.0814 0.0035 417 LYS B CB 10422 C CG . LYS B 417 ? 1.0821 0.4446 0.8815 -0.1040 0.0718 0.0024 417 LYS B CG 10423 C CD . LYS B 417 ? 1.0960 0.4556 0.9196 -0.0977 0.0802 0.0013 417 LYS B CD 10424 C CE . LYS B 417 ? 1.4193 0.7632 1.2716 -0.1085 0.1069 -0.0190 417 LYS B CE 10425 N NZ . LYS B 417 ? 1.7035 1.0446 1.5918 -0.1021 0.1163 -0.0223 417 LYS B NZ 10426 N N . PRO B 418 ? 1.0351 0.4097 0.8765 -0.0807 0.0516 0.0487 418 PRO B N 10427 C CA . PRO B 418 ? 1.0759 0.4616 0.9111 -0.0736 0.0369 0.0666 418 PRO B CA 10428 C C . PRO B 418 ? 1.1735 0.5636 1.0109 -0.0667 0.0330 0.0667 418 PRO B C 10429 O O . PRO B 418 ? 1.1832 0.5635 1.0435 -0.0657 0.0432 0.0590 418 PRO B O 10430 C CB . PRO B 418 ? 1.0306 0.4072 0.8921 -0.0723 0.0348 0.0853 418 PRO B CB 10431 C CG . PRO B 418 ? 1.0250 0.3862 0.9237 -0.0731 0.0497 0.0759 418 PRO B CG 10432 C CD . PRO B 418 ? 1.0225 0.3833 0.9006 -0.0813 0.0622 0.0518 418 PRO B CD 10433 N N . VAL B 419 ? 1.1478 0.5526 0.9653 -0.0634 0.0208 0.0726 419 VAL B N 10434 C CA . VAL B 419 ? 1.1537 0.5642 0.9715 -0.0570 0.0168 0.0718 419 VAL B CA 10435 C C . VAL B 419 ? 1.1919 0.5969 1.0407 -0.0497 0.0135 0.0858 419 VAL B C 10436 O O . VAL B 419 ? 1.1900 0.5968 1.0427 -0.0495 0.0024 0.1045 419 VAL B O 10437 C CB . VAL B 419 ? 1.1937 0.6226 0.9885 -0.0557 0.0050 0.0738 419 VAL B CB 10438 C CG1 . VAL B 419 ? 1.3420 0.7766 1.1388 -0.0487 0.0012 0.0730 419 VAL B CG1 10439 C CG2 . VAL B 419 ? 1.1525 0.5866 0.9303 -0.0626 0.0042 0.0612 419 VAL B CG2 10440 N N . GLY B 420 ? 1.3505 0.7479 1.2226 -0.0464 0.0225 0.0766 420 GLY B N 10441 C CA . GLY B 420 ? 1.4614 0.8535 1.3756 -0.0387 0.0182 0.0878 420 GLY B CA 10442 C C . GLY B 420 ? 1.4458 0.8212 1.4097 -0.0398 0.0270 0.0889 420 GLY B C 10443 O O . GLY B 420 ? 1.4527 0.8223 1.4620 -0.0342 0.0174 0.1042 420 GLY B O 10444 N N . PHE B 421 ? 1.4252 0.7926 1.3854 -0.0480 0.0437 0.0729 421 PHE B N 10445 C CA . PHE B 421 ? 1.3495 0.7017 1.3619 -0.0503 0.0556 0.0697 421 PHE B CA 10446 C C . PHE B 421 ? 1.2575 0.6009 1.2748 -0.0611 0.0839 0.0378 421 PHE B C 10447 O O . PHE B 421 ? 1.3941 0.7415 1.3605 -0.0701 0.0898 0.0232 421 PHE B O 10448 C CB . PHE B 421 ? 1.3466 0.6962 1.3525 -0.0534 0.0470 0.0861 421 PHE B CB 10449 C CG . PHE B 421 ? 1.3196 0.6690 1.3399 -0.0492 0.0224 0.1187 421 PHE B CG 10450 C CD1 . PHE B 421 ? 1.2693 0.6129 1.3429 -0.0423 0.0118 0.1320 421 PHE B CD1 10451 C CD2 . PHE B 421 ? 1.2488 0.6028 1.2296 -0.0552 0.0094 0.1359 421 PHE B CD2 10452 C CE1 . PHE B 421 ? 1.2185 0.5600 1.3009 -0.0425 -0.0159 0.1656 421 PHE B CE1 10453 C CE2 . PHE B 421 ? 1.3260 0.6777 1.3098 -0.0578 -0.0138 0.1667 421 PHE B CE2 10454 C CZ . PHE B 421 ? 1.3248 0.6698 1.3570 -0.0520 -0.0287 0.1836 421 PHE B CZ 10455 N N . LYS B 422 ? 1.1667 0.4974 1.2481 -0.0627 0.1008 0.0268 422 LYS B N 10456 C CA . LYS B 422 ? 1.1911 0.5122 1.2808 -0.0780 0.1326 -0.0076 422 LYS B CA 10457 C C . LYS B 422 ? 1.3404 0.6571 1.4122 -0.0885 0.1411 -0.0149 422 LYS B C 10458 O O . LYS B 422 ? 1.4256 0.7396 1.4588 -0.1053 0.1579 -0.0387 422 LYS B O 10459 C CB . LYS B 422 ? 1.2824 0.5924 1.4595 -0.0775 0.1518 -0.0217 422 LYS B CB 10460 C CG . LYS B 422 ? 1.4070 0.7072 1.5929 -0.0985 0.1909 -0.0636 422 LYS B CG 10461 C CD . LYS B 422 ? 1.4611 0.7684 1.7402 -0.0959 0.2068 -0.0791 422 LYS B CD 10462 C CE . LYS B 422 ? 1.4781 0.7910 1.7571 -0.1192 0.2462 -0.1229 422 LYS B CE 10463 N NZ . LYS B 422 ? 1.3788 0.6841 1.5893 -0.1348 0.2577 -0.1397 422 LYS B NZ 10464 N N . ASP B 423 ? 1.4317 0.7467 1.5296 -0.0806 0.1281 0.0068 423 ASP B N 10465 C CA . ASP B 423 ? 1.3819 0.6927 1.4701 -0.0888 0.1354 0.0019 423 ASP B CA 10466 C C . ASP B 423 ? 1.3042 0.6240 1.3141 -0.0962 0.1288 -0.0021 423 ASP B C 10467 O O . ASP B 423 ? 1.1741 0.5053 1.1454 -0.0890 0.1076 0.0153 423 ASP B O 10468 C CB . ASP B 423 ? 1.3639 0.6712 1.4858 -0.0797 0.1178 0.0315 423 ASP B CB 10469 C CG . ASP B 423 ? 1.4110 0.7071 1.6233 -0.0737 0.1199 0.0382 423 ASP B CG 10470 O OD1 . ASP B 423 ? 1.3750 0.6607 1.6408 -0.0799 0.1411 0.0211 423 ASP B OD1 10471 O OD2 . ASP B 423 ? 1.4408 0.7384 1.6754 -0.0636 0.0996 0.0603 423 ASP B OD2 10472 N N . SER B 424 ? 1.3935 0.6542 1.4385 -0.1320 0.0389 0.0348 424 SER B N 10473 C CA . SER B 424 ? 1.4302 0.6821 1.4624 -0.1441 0.0192 0.0472 424 SER B CA 10474 C C . SER B 424 ? 1.2469 0.5292 1.2823 -0.1424 0.0477 0.0229 424 SER B C 10475 O O . SER B 424 ? 1.0612 0.3615 1.0863 -0.1387 0.0889 -0.0004 424 SER B O 10476 C CB . SER B 424 ? 1.4971 0.7385 1.5169 -0.1716 0.0145 0.0891 424 SER B CB 10477 O OG . SER B 424 ? 1.3908 0.6602 1.4362 -0.1840 0.0396 0.1042 424 SER B OG 10478 N N . LEU B 425 ? 1.1776 0.4556 1.2089 -0.1467 0.0280 0.0273 425 LEU B N 10479 C CA . LEU B 425 ? 1.0728 0.3701 1.0942 -0.1495 0.0531 0.0071 425 LEU B CA 10480 C C . LEU B 425 ? 1.2500 0.5544 1.2814 -0.1755 0.0453 0.0380 425 LEU B C 10481 O O . LEU B 425 ? 1.5062 0.8048 1.5466 -0.1851 0.0109 0.0663 425 LEU B O 10482 C CB . LEU B 425 ? 1.0524 0.3469 1.0667 -0.1344 0.0417 -0.0100 425 LEU B CB 10483 C CG . LEU B 425 ? 1.0207 0.3275 1.0182 -0.1403 0.0599 -0.0263 425 LEU B CG 10484 C CD1 . LEU B 425 ? 0.9846 0.3031 0.9499 -0.1365 0.1026 -0.0602 425 LEU B CD1 10485 C CD2 . LEU B 425 ? 1.1112 0.4127 1.1127 -0.1287 0.0385 -0.0269 425 LEU B CD2 10486 N N . ILE B 426 ? 1.2460 0.5621 1.2643 -0.1879 0.0820 0.0331 426 ILE B N 10487 C CA . ILE B 426 ? 1.2981 0.6064 1.3106 -0.2184 0.1133 0.0597 426 ILE B CA 10488 C C . ILE B 426 ? 1.2868 0.5878 1.2622 -0.2266 0.1337 0.0308 426 ILE B C 10489 O O . ILE B 426 ? 1.3954 0.6874 1.3282 -0.2197 0.1606 -0.0140 426 ILE B O 10490 C CB . ILE B 426 ? 1.1169 0.4161 1.1095 -0.2346 0.1734 0.0716 426 ILE B CB 10491 C CG1 . ILE B 426 ? 1.1069 0.4184 1.1423 -0.2297 0.1526 0.1088 426 ILE B CG1 10492 C CG2 . ILE B 426 ? 1.1705 0.4729 1.1444 -0.2662 0.2089 0.1058 426 ILE B CG2 10493 C CD1 . ILE B 426 ? 1.0998 0.4061 1.1281 -0.2053 0.1550 0.0741 426 ILE B CD1 10494 N N . VAL B 427 ? 1.1569 0.4636 1.1469 -0.2429 0.1169 0.0586 427 VAL B N 10495 C CA . VAL B 427 ? 1.1095 0.4085 1.0629 -0.2546 0.1304 0.0350 427 VAL B CA 10496 C C . VAL B 427 ? 1.2741 0.5654 1.1890 -0.2945 0.1668 0.0586 427 VAL B C 10497 O O . VAL B 427 ? 1.4816 0.7956 1.4310 -0.3075 0.1517 0.1109 427 VAL B O 10498 C CB . VAL B 427 ? 1.0595 0.3759 1.0552 -0.2384 0.0802 0.0442 427 VAL B CB 10499 C CG1 . VAL B 427 ? 1.0776 0.3874 1.0378 -0.2533 0.0948 0.0246 427 VAL B CG1 10500 C CG2 . VAL B 427 ? 1.0619 0.3908 1.0813 -0.2017 0.0444 0.0249 427 VAL B CG2 10501 N N . GLN B 428 ? 1.3037 0.5676 1.1431 -0.3148 0.2116 0.0224 428 GLN B N 10502 C CA . GLN B 428 ? 1.2843 0.5858 1.0780 -0.3379 0.2321 0.0412 428 GLN B CA 10503 C C . GLN B 428 ? 1.3019 0.6102 1.0840 -0.3522 0.2087 0.0346 428 GLN B C 10504 O O . GLN B 428 ? 1.5275 0.7911 1.2859 -0.3567 0.2058 -0.0124 428 GLN B O 10505 C CB . GLN B 428 ? 1.3765 0.7007 1.1025 -0.3252 0.2640 0.0008 428 GLN B CB 10506 C CG . GLN B 428 ? 1.5051 0.8198 1.2364 -0.3088 0.2911 0.0026 428 GLN B CG 10507 C CD . GLN B 428 ? 1.6398 0.9586 1.2953 -0.2933 0.3207 -0.0472 428 GLN B CD 10508 O OE1 . GLN B 428 ? 1.5091 0.8130 1.1577 -0.2785 0.3456 -0.0565 428 GLN B OE1 10509 N NE2 . GLN B 428 ? 1.7966 1.1327 1.3935 -0.2956 0.3158 -0.0799 428 GLN B NE2 10510 N N . VAL B 429 ? 1.3089 0.6756 1.1117 -0.3593 0.1923 0.0847 429 VAL B N 10511 C CA . VAL B 429 ? 1.3383 0.7141 1.1361 -0.3730 0.1685 0.0858 429 VAL B CA 10512 C C . VAL B 429 ? 1.4115 0.8627 1.1593 -0.3745 0.1740 0.0840 429 VAL B C 10513 O O . VAL B 429 ? 1.4746 0.9953 1.2224 -0.3675 0.1821 0.1249 429 VAL B O 10514 C CB . VAL B 429 ? 1.4482 0.8245 1.3054 -0.3799 0.1393 0.1423 429 VAL B CB 10515 C CG1 . VAL B 429 ? 1.4673 0.8352 1.3193 -0.3914 0.1158 0.1372 429 VAL B CG1 10516 C CG2 . VAL B 429 ? 1.5920 0.9338 1.5151 -0.3536 0.1212 0.1463 429 VAL B CG2 10517 N N . THR B 430 ? 1.4298 0.8664 1.1366 -0.3818 0.1683 0.0385 430 THR B N 10518 C CA . THR B 430 ? 1.5238 1.0209 1.1786 -0.3828 0.1662 0.0305 430 THR B CA 10519 C C . THR B 430 ? 1.5288 1.0197 1.1898 -0.4011 0.1388 0.0251 430 THR B C 10520 O O . THR B 430 ? 1.4889 0.9192 1.1676 -0.4093 0.1296 -0.0007 430 THR B O 10521 C CB . THR B 430 ? 1.6285 1.1164 1.2144 -0.3712 0.1841 -0.0261 430 THR B CB 10522 O OG1 . THR B 430 ? 1.6632 1.1481 1.2453 -0.3526 0.2119 -0.0227 430 THR B OG1 10523 C CG2 . THR B 430 ? 1.7471 1.2987 1.2722 -0.3648 0.1799 -0.0301 430 THR B CG2 10524 N N . PHE B 431 ? 1.5828 1.1391 1.2309 -0.4052 0.1272 0.0527 431 PHE B N 10525 C CA . PHE B 431 ? 1.5780 1.1366 1.2338 -0.4224 0.1011 0.0539 431 PHE B CA 10526 C C . PHE B 431 ? 1.6921 1.2807 1.2883 -0.4256 0.0933 0.0184 431 PHE B C 10527 O O . PHE B 431 ? 1.8746 1.5188 1.4254 -0.4126 0.1012 0.0228 431 PHE B O 10528 C CB . PHE B 431 ? 1.5369 1.1410 1.2321 -0.4273 0.0871 0.1165 431 PHE B CB 10529 C CG . PHE B 431 ? 1.4499 1.0187 1.2049 -0.4246 0.0849 0.1534 431 PHE B CG 10530 C CD1 . PHE B 431 ? 1.4819 1.0879 1.2617 -0.4155 0.0944 0.1983 431 PHE B CD1 10531 C CD2 . PHE B 431 ? 1.3909 0.8882 1.1783 -0.4285 0.0714 0.1453 431 PHE B CD2 10532 C CE1 . PHE B 431 ? 1.4769 1.0450 1.3148 -0.4141 0.0853 0.2322 431 PHE B CE1 10533 C CE2 . PHE B 431 ? 1.3444 0.8010 1.1802 -0.4223 0.0638 0.1763 431 PHE B CE2 10534 C CZ . PHE B 431 ? 1.3843 0.8741 1.2465 -0.4169 0.0682 0.2187 431 PHE B CZ 10535 N N . ASP B 432 ? 1.6483 1.1987 1.2455 -0.4405 0.0760 -0.0148 432 ASP B N 10536 C CA . ASP B 432 ? 1.7385 1.3119 1.2895 -0.4479 0.0582 -0.0450 432 ASP B CA 10537 C C . ASP B 432 ? 1.7472 1.3626 1.3190 -0.4621 0.0351 -0.0093 432 ASP B C 10538 O O . ASP B 432 ? 1.6748 1.2630 1.2926 -0.4755 0.0224 0.0034 432 ASP B O 10539 C CB . ASP B 432 ? 1.7703 1.2816 1.3173 -0.4579 0.0497 -0.0986 432 ASP B CB 10540 C CG . ASP B 432 ? 1.8607 1.3376 1.3681 -0.4431 0.0693 -0.1426 432 ASP B CG 10541 O OD1 . ASP B 432 ? 1.8682 1.3026 1.4038 -0.4365 0.0895 -0.1435 432 ASP B OD1 10542 O OD2 . ASP B 432 ? 1.8865 1.3760 1.3309 -0.4359 0.0630 -0.1770 432 ASP B OD2 10543 N N . CYS B 433 ? 1.8592 1.5420 1.3946 -0.4556 0.0311 0.0084 433 CYS B N 10544 C CA . CYS B 433 ? 1.9107 1.6405 1.4623 -0.4673 0.0111 0.0449 433 CYS B CA 10545 C C . CYS B 433 ? 2.0018 1.7682 1.4971 -0.4690 -0.0086 0.0196 433 CYS B C 10546 O O . CYS B 433 ? 2.0608 1.8189 1.5665 -0.4879 -0.0339 0.0084 433 CYS B O 10547 C CB . CYS B 433 ? 1.9424 1.7255 1.5159 -0.4572 0.0228 0.1048 433 CYS B CB 10548 S SG . CYS B 433 ? 2.5508 2.2874 2.1959 -0.4566 0.0340 0.1408 433 CYS B SG 10549 N N . ASP B 434 ? 2.1204 1.9274 1.5558 -0.4466 0.0021 0.0129 434 ASP B N 10550 C CA . ASP B 434 ? 2.2572 2.0955 1.6272 -0.4407 -0.0186 -0.0133 434 ASP B CA 10551 C C . ASP B 434 ? 2.2517 2.0310 1.5863 -0.4465 -0.0371 -0.0794 434 ASP B C 10552 O O . ASP B 434 ? 2.1832 1.9105 1.5180 -0.4420 -0.0223 -0.1083 434 ASP B O 10553 C CB . ASP B 434 ? 2.3614 2.2589 1.6718 -0.4063 0.0006 0.0020 434 ASP B CB 10554 C CG . ASP B 434 ? 2.3247 2.2881 1.6743 -0.4015 0.0153 0.0719 434 ASP B CG 10555 O OD1 . ASP B 434 ? 2.2084 2.1573 1.6313 -0.4211 0.0162 0.1057 434 ASP B OD1 10556 O OD2 . ASP B 434 ? 2.3854 2.4134 1.6918 -0.3757 0.0248 0.0940 434 ASP B OD2 10557 N N . CYS B 435 ? 2.3333 2.1199 1.6403 -0.4570 -0.0717 -0.1022 435 CYS B N 10558 C CA . CYS B 435 ? 2.4225 2.1544 1.6972 -0.4638 -0.0979 -0.1633 435 CYS B CA 10559 C C . CYS B 435 ? 2.5293 2.2556 1.7116 -0.4296 -0.0917 -0.2022 435 CYS B C 10560 O O . CYS B 435 ? 2.5368 2.3162 1.6722 -0.3996 -0.0736 -0.1796 435 CYS B O 10561 C CB . CYS B 435 ? 2.4827 2.2252 1.7598 -0.4857 -0.1422 -0.1720 435 CYS B CB 10562 S SG . CYS B 435 ? 2.1140 1.8541 1.4959 -0.5236 -0.1523 -0.1315 435 CYS B SG 10563 N N . ALA B 436 ? 2.5751 2.2373 1.7312 -0.4315 -0.1067 -0.2583 436 ALA B N 10564 C CA . ALA B 436 ? 2.5976 2.2424 1.6589 -0.3961 -0.1035 -0.3005 436 ALA B CA 10565 C C . ALA B 436 ? 2.6711 2.3424 1.6493 -0.3773 -0.1386 -0.3203 436 ALA B C 10566 O O . ALA B 436 ? 2.7589 2.4475 1.6484 -0.3347 -0.1284 -0.3322 436 ALA B O 10567 C CB . ALA B 436 ? 2.5640 2.1269 1.6238 -0.4049 -0.1130 -0.3553 436 ALA B CB 10568 N N . CYS B 437 ? 2.6355 2.3102 1.6413 -0.4061 -0.1800 -0.3219 437 CYS B N 10569 C CA . CYS B 437 ? 2.7137 2.4067 1.6444 -0.3912 -0.2210 -0.3437 437 CYS B CA 10570 C C . CYS B 437 ? 2.6530 2.4321 1.5684 -0.3727 -0.2058 -0.2923 437 CYS B C 10571 O O . CYS B 437 ? 2.8198 2.6240 1.6676 -0.3535 -0.2343 -0.3038 437 CYS B O 10572 C CB . CYS B 437 ? 2.7751 2.4344 1.7470 -0.4314 -0.2758 -0.3664 437 CYS B CB 10573 S SG . CYS B 437 ? 2.3635 2.0580 1.4625 -0.4788 -0.2720 -0.3070 437 CYS B SG 10574 N N . GLN B 438 ? 2.4699 2.2916 1.4480 -0.3775 -0.1631 -0.2357 438 GLN B N 10575 C CA . GLN B 438 ? 2.4626 2.3674 1.4403 -0.3628 -0.1462 -0.1800 438 GLN B CA 10576 C C . GLN B 438 ? 2.5726 2.5164 1.4553 -0.3073 -0.1245 -0.1785 438 GLN B C 10577 O O . GLN B 438 ? 2.6592 2.6660 1.5045 -0.2851 -0.1265 -0.1523 438 GLN B O 10578 C CB . GLN B 438 ? 2.4146 2.3447 1.4870 -0.3821 -0.1106 -0.1206 438 GLN B CB 10579 C CG . GLN B 438 ? 2.4658 2.4796 1.5531 -0.3729 -0.0960 -0.0581 438 GLN B CG 10580 C CD . GLN B 438 ? 2.3716 2.3977 1.5547 -0.3950 -0.0714 -0.0028 438 GLN B CD 10581 O OE1 . GLN B 438 ? 2.2279 2.1989 1.4674 -0.4190 -0.0692 -0.0120 438 GLN B OE1 10582 N NE2 . GLN B 438 ? 2.4096 2.5057 1.6101 -0.3845 -0.0545 0.0556 438 GLN B NE2 10583 N N . ALA B 439 ? 2.6479 2.5553 1.4907 -0.2820 -0.1023 -0.2049 439 ALA B N 10584 C CA . ALA B 439 ? 2.7658 2.7076 1.5163 -0.2233 -0.0772 -0.2015 439 ALA B CA 10585 C C . ALA B 439 ? 2.8638 2.7851 1.4989 -0.1909 -0.1177 -0.2548 439 ALA B C 10586 O O . ALA B 439 ? 2.9789 2.9415 1.5265 -0.1364 -0.1046 -0.2465 439 ALA B O 10587 C CB . ALA B 439 ? 2.8073 2.7153 1.5533 -0.2062 -0.0402 -0.2110 439 ALA B CB 10588 N N . GLN B 440 ? 2.9138 2.7703 1.5501 -0.2224 -0.1687 -0.3073 440 GLN B N 10589 C CA . GLN B 440 ? 2.9734 2.7952 1.5046 -0.1964 -0.2187 -0.3640 440 GLN B CA 10590 C C . GLN B 440 ? 3.0041 2.8861 1.5049 -0.1850 -0.2423 -0.3422 440 GLN B C 10591 O O . GLN B 440 ? 3.1506 3.0174 1.5491 -0.1499 -0.2797 -0.3808 440 GLN B O 10592 C CB . GLN B 440 ? 2.9097 2.6442 1.4677 -0.2389 -0.2704 -0.4211 440 GLN B CB 10593 C CG . GLN B 440 ? 2.8716 2.5378 1.4441 -0.2452 -0.2534 -0.4529 440 GLN B CG 10594 C CD . GLN B 440 ? 2.8895 2.4735 1.4938 -0.2863 -0.3061 -0.5050 440 GLN B CD 10595 O OE1 . GLN B 440 ? 2.8690 2.4513 1.5060 -0.3179 -0.3529 -0.5089 440 GLN B OE1 10596 N NE2 . GLN B 440 ? 2.9367 2.4539 1.5356 -0.2860 -0.2989 -0.5423 440 GLN B NE2 10597 N N . ALA B 441 ? 2.8855 2.8324 1.4724 -0.2127 -0.2222 -0.2814 441 ALA B N 10598 C CA . ALA B 441 ? 2.9381 2.9466 1.5091 -0.2070 -0.2414 -0.2554 441 ALA B CA 10599 C C . ALA B 441 ? 3.1318 3.1996 1.6024 -0.1379 -0.2172 -0.2366 441 ALA B C 10600 O O . ALA B 441 ? 3.1086 3.2180 1.5830 -0.1092 -0.1633 -0.1960 441 ALA B O 10601 C CB . ALA B 441 ? 2.7591 2.8205 1.4463 -0.2506 -0.2215 -0.1920 441 ALA B CB 10602 N N . GLU B 442 ? 3.3166 3.3887 1.6990 -0.1095 -0.2580 -0.2639 442 GLU B N 10603 C CA . GLU B 442 ? 3.4347 3.5655 1.7147 -0.0377 -0.2380 -0.2452 442 GLU B CA 10604 C C . GLU B 442 ? 3.4616 3.6864 1.7869 -0.0432 -0.2227 -0.1802 442 GLU B C 10605 O O . GLU B 442 ? 3.4510 3.6813 1.7724 -0.0610 -0.2660 -0.1911 442 GLU B O 10606 C CB . GLU B 442 ? 3.4665 3.5435 1.6117 0.0056 -0.2928 -0.3138 442 GLU B CB 10607 C CG . GLU B 442 ? 3.4599 3.4374 1.5555 0.0115 -0.3143 -0.3815 442 GLU B CG 10608 C CD . GLU B 442 ? 3.6032 3.5146 1.5722 0.0473 -0.3817 -0.4532 442 GLU B CD 10609 O OE1 . GLU B 442 ? 3.6605 3.6033 1.5810 0.0669 -0.4126 -0.4512 442 GLU B OE1 10610 O OE2 . GLU B 442 ? 3.6949 3.5197 1.6117 0.0566 -0.4062 -0.5122 442 GLU B OE2 10611 N N . PRO B 443 ? 3.4632 3.7629 1.8296 -0.0253 -0.1623 -0.1111 443 PRO B N 10612 C CA . PRO B 443 ? 3.3601 3.7457 1.8112 -0.0457 -0.1365 -0.0363 443 PRO B CA 10613 C C . PRO B 443 ? 3.4037 3.8426 1.8160 -0.0313 -0.1622 -0.0240 443 PRO B C 10614 O O . PRO B 443 ? 3.3701 3.8559 1.8661 -0.0690 -0.1588 0.0220 443 PRO B O 10615 C CB . PRO B 443 ? 3.3054 3.7552 1.7601 -0.0015 -0.0723 0.0238 443 PRO B CB 10616 C CG . PRO B 443 ? 3.4336 3.8465 1.7711 0.0596 -0.0675 -0.0203 443 PRO B CG 10617 C CD . PRO B 443 ? 3.4976 3.8035 1.8187 0.0254 -0.1153 -0.1006 443 PRO B CD 10618 N N . ASN B 444 ? 3.4584 3.8881 1.7452 0.0236 -0.1886 -0.0641 444 ASN B N 10619 C CA . ASN B 444 ? 3.3991 3.8912 1.6407 0.0503 -0.2034 -0.0441 444 ASN B CA 10620 C C . ASN B 444 ? 3.2788 3.7488 1.5583 -0.0044 -0.2606 -0.0679 444 ASN B C 10621 O O . ASN B 444 ? 3.1688 3.5717 1.5069 -0.0620 -0.2924 -0.1025 444 ASN B O 10622 C CB . ASN B 444 ? 3.5505 4.0359 1.6356 0.1346 -0.2151 -0.0803 444 ASN B CB 10623 C CG . ASN B 444 ? 3.6068 4.1879 1.6453 0.1877 -0.1951 -0.0303 444 ASN B CG 10624 O OD1 . ASN B 444 ? 3.6789 4.2673 1.6804 0.1887 -0.2371 -0.0476 444 ASN B OD1 10625 N ND2 . ASN B 444 ? 3.5876 4.2450 1.6321 0.2325 -0.1308 0.0350 444 ASN B ND2 10626 N N . SER B 445 ? 3.3418 3.8729 1.5884 0.0171 -0.2714 -0.0454 445 SER B N 10627 C CA . SER B 445 ? 3.3391 3.8658 1.6157 -0.0268 -0.3226 -0.0585 445 SER B CA 10628 C C . SER B 445 ? 3.4483 3.8926 1.6394 -0.0211 -0.3953 -0.1406 445 SER B C 10629 O O . SER B 445 ? 3.6202 4.0154 1.7077 0.0287 -0.4064 -0.1879 445 SER B O 10630 C CB . SER B 445 ? 3.3475 3.9711 1.6133 -0.0006 -0.3065 -0.0044 445 SER B CB 10631 O OG . SER B 445 ? 3.2266 3.9223 1.5886 -0.0167 -0.2485 0.0740 445 SER B OG 10632 N N . HIS B 446 ? 3.3263 3.7527 1.5675 -0.0744 -0.4456 -0.1549 446 HIS B N 10633 C CA . HIS B 446 ? 3.3264 3.6846 1.5029 -0.0766 -0.5245 -0.2236 446 HIS B CA 10634 C C . HIS B 446 ? 3.2988 3.5548 1.5005 -0.1145 -0.5605 -0.2800 446 HIS B C 10635 O O . HIS B 446 ? 3.3530 3.5422 1.5164 -0.1240 -0.6309 -0.3374 446 HIS B O 10636 C CB . HIS B 446 ? 3.4228 3.7797 1.4414 0.0078 -0.5434 -0.2569 446 HIS B CB 10637 C CG . HIS B 446 ? 3.4300 3.8809 1.4157 0.0455 -0.5240 -0.2100 446 HIS B CG 10638 N ND1 . HIS B 446 ? 3.5073 3.9580 1.4267 0.0626 -0.5803 -0.2363 446 HIS B ND1 10639 C CD2 . HIS B 446 ? 3.3664 3.9146 1.3797 0.0694 -0.4558 -0.1371 446 HIS B CD2 10640 C CE1 . HIS B 446 ? 3.4713 4.0166 1.3755 0.0970 -0.5446 -0.1824 446 HIS B CE1 10641 N NE2 . HIS B 446 ? 3.4002 4.0067 1.3628 0.1012 -0.4691 -0.1204 446 HIS B NE2 10642 N N . ARG B 447 ? 3.2094 3.4529 1.4777 -0.1355 -0.5142 -0.2626 447 ARG B N 10643 C CA . ARG B 447 ? 3.1455 3.2965 1.4428 -0.1692 -0.5396 -0.3111 447 ARG B CA 10644 C C . ARG B 447 ? 3.0993 3.2150 1.4920 -0.2415 -0.5915 -0.3224 447 ARG B C 10645 O O . ARG B 447 ? 3.1268 3.1598 1.5224 -0.2641 -0.6382 -0.3743 447 ARG B O 10646 C CB . ARG B 447 ? 2.9784 3.1329 1.3382 -0.1786 -0.4745 -0.2814 447 ARG B CB 10647 C CG . ARG B 447 ? 2.9768 3.0372 1.3508 -0.2010 -0.4925 -0.3326 447 ARG B CG 10648 C CD . ARG B 447 ? 3.1129 3.1087 1.3509 -0.1470 -0.5295 -0.4003 447 ARG B CD 10649 N NE . ARG B 447 ? 3.1263 3.0267 1.3794 -0.1726 -0.5570 -0.4532 447 ARG B NE 10650 C CZ . ARG B 447 ? 3.1458 2.9766 1.4119 -0.2077 -0.6284 -0.5010 447 ARG B CZ 10651 N NH1 . ARG B 447 ? 3.1531 2.9985 1.4178 -0.2218 -0.6809 -0.5035 447 ARG B NH1 10652 N NH2 . ARG B 447 ? 3.1695 2.9172 1.4540 -0.2292 -0.6485 -0.5441 447 ARG B NH2 10653 N N . CYS B 448 ? 3.0311 3.2100 1.5029 -0.2763 -0.5840 -0.2714 448 CYS B N 10654 C CA . CYS B 448 ? 3.0185 3.1733 1.5907 -0.3435 -0.6253 -0.2708 448 CYS B CA 10655 C C . CYS B 448 ? 3.1069 3.2700 1.6514 -0.3494 -0.6901 -0.2863 448 CYS B C 10656 O O . CYS B 448 ? 3.1560 3.2509 1.6670 -0.3557 -0.7571 -0.3417 448 CYS B O 10657 C CB . CYS B 448 ? 2.8918 3.1010 1.5847 -0.3846 -0.5751 -0.2022 448 CYS B CB 10658 S SG . CYS B 448 ? 3.0612 3.2606 1.8777 -0.4587 -0.6165 -0.1851 448 CYS B SG 10659 N N . ASN B 449 ? 3.1381 3.3826 1.6966 -0.3471 -0.6731 -0.2376 449 ASN B N 10660 C CA . ASN B 449 ? 3.2206 3.4802 1.7581 -0.3537 -0.7318 -0.2470 449 ASN B CA 10661 C C . ASN B 449 ? 3.2178 3.5677 1.7091 -0.3164 -0.7048 -0.2059 449 ASN B C 10662 O O . ASN B 449 ? 3.1035 3.5205 1.6429 -0.3174 -0.6421 -0.1463 449 ASN B O 10663 C CB . ASN B 449 ? 3.1734 3.4284 1.8364 -0.4257 -0.7601 -0.2253 449 ASN B CB 10664 C CG . ASN B 449 ? 3.2051 3.3686 1.9037 -0.4607 -0.8123 -0.2734 449 ASN B CG 10665 O OD1 . ASN B 449 ? 3.2940 3.4127 1.9584 -0.4647 -0.8857 -0.3172 449 ASN B OD1 10666 N ND2 . ASN B 449 ? 3.1080 3.2422 1.8778 -0.4858 -0.7767 -0.2643 449 ASN B ND2 10667 N N . ASN B 450 ? 3.4347 3.7829 1.8330 -0.2827 -0.7553 -0.2381 450 ASN B N 10668 C CA . ASN B 450 ? 3.5220 3.9534 1.8744 -0.2482 -0.7411 -0.2035 450 ASN B CA 10669 C C . ASN B 450 ? 3.4870 3.9825 1.7964 -0.1936 -0.6642 -0.1630 450 ASN B C 10670 O O . ASN B 450 ? 3.4905 4.0705 1.8016 -0.1764 -0.6316 -0.1124 450 ASN B O 10671 C CB . ASN B 450 ? 3.4391 3.9259 1.9014 -0.3050 -0.7407 -0.1513 450 ASN B CB 10672 C CG . ASN B 450 ? 3.3875 3.9416 1.7983 -0.2774 -0.7541 -0.1325 450 ASN B CG 10673 O OD1 . ASN B 450 ? 3.3045 3.9409 1.7243 -0.2592 -0.6995 -0.0767 450 ASN B OD1 10674 N ND2 . ASN B 450 ? 3.4323 3.9498 1.7904 -0.2741 -0.8293 -0.1786 450 ASN B ND2 10675 N N . GLY B 451 ? 3.4445 3.9012 1.7189 -0.1664 -0.6358 -0.1827 451 GLY B N 10676 C CA . GLY B 451 ? 3.3711 3.8866 1.6206 -0.1189 -0.5616 -0.1394 451 GLY B CA 10677 C C . GLY B 451 ? 3.1369 3.7144 1.5112 -0.1616 -0.5038 -0.0659 451 GLY B C 10678 O O . GLY B 451 ? 2.9790 3.5527 1.4517 -0.2244 -0.5200 -0.0501 451 GLY B O 10679 N N . ASN B 452 ? 3.0888 3.7225 1.4582 -0.1248 -0.4385 -0.0191 452 ASN B N 10680 C CA . ASN B 452 ? 2.8939 3.5915 1.3708 -0.1549 -0.3848 0.0556 452 ASN B CA 10681 C C . ASN B 452 ? 2.7637 3.4184 1.3602 -0.2284 -0.3893 0.0615 452 ASN B C 10682 O O . ASN B 452 ? 2.6872 3.3681 1.3582 -0.2717 -0.3981 0.0929 452 ASN B O 10683 C CB . ASN B 452 ? 2.8456 3.6274 1.3298 -0.1498 -0.3819 0.1024 452 ASN B CB 10684 C CG . ASN B 452 ? 2.9296 3.7430 1.2873 -0.0794 -0.3951 0.0846 452 ASN B CG 10685 O OD1 . ASN B 452 ? 2.9265 3.7410 1.2458 -0.0800 -0.4424 0.0613 452 ASN B OD1 10686 N ND2 . ASN B 452 ? 2.9991 3.8383 1.2903 -0.0153 -0.3536 0.0970 452 ASN B ND2 10687 N N . GLY B 453 ? 2.7616 3.3506 1.3731 -0.2389 -0.3825 0.0324 453 GLY B N 10688 C CA . GLY B 453 ? 2.6858 3.2284 1.4028 -0.3015 -0.3868 0.0345 453 GLY B CA 10689 C C . GLY B 453 ? 2.6773 3.1768 1.4204 -0.3019 -0.3519 0.0291 453 GLY B C 10690 O O . GLY B 453 ? 2.6819 3.1883 1.3625 -0.2542 -0.3229 0.0247 453 GLY B O 10691 N N . THR B 454 ? 2.6788 3.1346 1.5137 -0.3533 -0.3537 0.0313 454 THR B N 10692 C CA . THR B 454 ? 2.6861 3.0966 1.5543 -0.3582 -0.3225 0.0259 454 THR B CA 10693 C C . THR B 454 ? 2.7501 3.0708 1.6162 -0.3811 -0.3612 -0.0375 454 THR B C 10694 O O . THR B 454 ? 2.7686 3.0635 1.6103 -0.3933 -0.4141 -0.0746 454 THR B O 10695 C CB . THR B 454 ? 2.4965 2.9249 1.4737 -0.3927 -0.2877 0.0835 454 THR B CB 10696 O OG1 . THR B 454 ? 2.4700 2.9717 1.4726 -0.3963 -0.2811 0.1373 454 THR B OG1 10697 C CG2 . THR B 454 ? 2.4236 2.8532 1.4113 -0.3711 -0.2375 0.1053 454 THR B CG2 10698 N N . PHE B 455 ? 2.7313 3.0049 1.6282 -0.3879 -0.3363 -0.0474 455 PHE B N 10699 C CA . PHE B 455 ? 2.7724 2.9606 1.6566 -0.4000 -0.3657 -0.1085 455 PHE B CA 10700 C C . PHE B 455 ? 2.8163 2.9671 1.7452 -0.4060 -0.3256 -0.1048 455 PHE B C 10701 O O . PHE B 455 ? 2.9015 3.0914 1.8501 -0.3907 -0.2771 -0.0611 455 PHE B O 10702 C CB . PHE B 455 ? 2.8789 3.0429 1.6414 -0.3541 -0.3931 -0.1635 455 PHE B CB 10703 C CG . PHE B 455 ? 2.9227 3.1244 1.6139 -0.2966 -0.3470 -0.1483 455 PHE B CG 10704 C CD1 . PHE B 455 ? 2.8926 3.0546 1.5641 -0.2773 -0.3180 -0.1671 455 PHE B CD1 10705 C CD2 . PHE B 455 ? 3.0070 3.2881 1.6560 -0.2609 -0.3301 -0.1100 455 PHE B CD2 10706 C CE1 . PHE B 455 ? 2.9381 3.1403 1.5503 -0.2232 -0.2737 -0.1462 455 PHE B CE1 10707 C CE2 . PHE B 455 ? 3.0120 3.3344 1.6037 -0.2060 -0.2851 -0.0877 455 PHE B CE2 10708 C CZ . PHE B 455 ? 2.9615 3.2455 1.5362 -0.1872 -0.2568 -0.1044 455 PHE B CZ 10709 N N . GLU B 456 ? 2.8356 2.9104 1.7825 -0.4280 -0.3480 -0.1497 456 GLU B N 10710 C CA . GLU B 456 ? 2.8274 2.8569 1.8036 -0.4297 -0.3146 -0.1575 456 GLU B CA 10711 C C . GLU B 456 ? 2.8355 2.7810 1.8045 -0.4460 -0.3524 -0.2192 456 GLU B C 10712 O O . GLU B 456 ? 2.9132 2.8373 1.8492 -0.4524 -0.4053 -0.2548 456 GLU B O 10713 C CB . GLU B 456 ? 2.6879 2.7306 1.7709 -0.4611 -0.2822 -0.1051 456 GLU B CB 10714 C CG . GLU B 456 ? 2.6020 2.6348 1.7011 -0.4456 -0.2320 -0.0891 456 GLU B CG 10715 C CD . GLU B 456 ? 2.5600 2.5996 1.7574 -0.4725 -0.2067 -0.0387 456 GLU B CD 10716 O OE1 . GLU B 456 ? 2.5105 2.5474 1.7655 -0.5048 -0.2280 -0.0243 456 GLU B OE1 10717 O OE2 . GLU B 456 ? 2.6362 2.6823 1.8521 -0.4591 -0.1672 -0.0122 456 GLU B OE2 10718 N N . CYS B 457 ? 2.7401 2.6367 1.7411 -0.4524 -0.3277 -0.2316 457 CYS B N 10719 C CA . CYS B 457 ? 2.7865 2.6033 1.7947 -0.4712 -0.3607 -0.2849 457 CYS B CA 10720 C C . CYS B 457 ? 2.7024 2.5086 1.7975 -0.5197 -0.3972 -0.2744 457 CYS B C 10721 O O . CYS B 457 ? 2.5682 2.3943 1.7505 -0.5445 -0.3737 -0.2288 457 CYS B O 10722 C CB . CYS B 457 ? 2.8211 2.5942 1.8565 -0.4693 -0.3209 -0.2923 457 CYS B CB 10723 S SG . CYS B 457 ? 3.7269 3.4016 2.7778 -0.4914 -0.3553 -0.3544 457 CYS B SG 10724 N N . GLY B 458 ? 2.7960 2.5686 1.8666 -0.5307 -0.4565 -0.3154 458 GLY B N 10725 C CA . GLY B 458 ? 2.7786 2.5474 1.9298 -0.5749 -0.4972 -0.3030 458 GLY B CA 10726 C C . GLY B 458 ? 2.7326 2.5743 1.9347 -0.5893 -0.4849 -0.2421 458 GLY B C 10727 O O . GLY B 458 ? 2.6882 2.5337 1.9840 -0.6242 -0.4883 -0.2101 458 GLY B O 10728 N N . VAL B 459 ? 2.7598 2.6602 1.8996 -0.5599 -0.4697 -0.2238 459 VAL B N 10729 C CA . VAL B 459 ? 2.7138 2.6854 1.8961 -0.5696 -0.4531 -0.1641 459 VAL B CA 10730 C C . VAL B 459 ? 2.7828 2.8084 1.8916 -0.5465 -0.4741 -0.1623 459 VAL B C 10731 O O . VAL B 459 ? 2.8243 2.8568 1.8394 -0.5048 -0.4676 -0.1857 459 VAL B O 10732 C CB . VAL B 459 ? 3.0016 3.0026 2.2136 -0.5577 -0.3891 -0.1181 459 VAL B CB 10733 C CG1 . VAL B 459 ? 2.9529 3.0337 2.1628 -0.5481 -0.3712 -0.0651 459 VAL B CG1 10734 C CG2 . VAL B 459 ? 2.9147 2.8820 2.2243 -0.5878 -0.3720 -0.0970 459 VAL B CG2 10735 N N . CYS B 460 ? 2.8065 2.8711 1.9570 -0.5708 -0.4984 -0.1326 460 CYS B N 10736 C CA . CYS B 460 ? 2.9466 3.0729 2.0399 -0.5504 -0.5109 -0.1191 460 CYS B CA 10737 C C . CYS B 460 ? 2.9836 3.1754 2.1441 -0.5692 -0.4882 -0.0528 460 CYS B C 10738 O O . CYS B 460 ? 3.0142 3.2047 2.2501 -0.6065 -0.5087 -0.0328 460 CYS B O 10739 C CB . CYS B 460 ? 3.0238 3.1268 2.0780 -0.5570 -0.5809 -0.1620 460 CYS B CB 10740 S SG . CYS B 460 ? 2.9723 3.1492 1.9583 -0.5324 -0.6017 -0.1463 460 CYS B SG 10741 N N . ARG B 461 ? 2.9594 3.2086 2.0935 -0.5416 -0.4460 -0.0161 461 ARG B N 10742 C CA . ARG B 461 ? 2.8384 3.1506 2.0248 -0.5541 -0.4256 0.0466 461 ARG B CA 10743 C C . ARG B 461 ? 2.8735 3.2560 1.9929 -0.5175 -0.4112 0.0672 461 ARG B C 10744 O O . ARG B 461 ? 2.9475 3.3404 2.0130 -0.4803 -0.3814 0.0632 461 ARG B O 10745 C CB . ARG B 461 ? 2.6800 2.9841 1.9387 -0.5650 -0.3795 0.0869 461 ARG B CB 10746 C CG . ARG B 461 ? 2.6351 2.9945 1.9471 -0.5767 -0.3613 0.1515 461 ARG B CG 10747 C CD . ARG B 461 ? 2.6065 2.9448 1.9838 -0.5841 -0.3230 0.1864 461 ARG B CD 10748 N NE . ARG B 461 ? 2.5921 2.9751 2.0153 -0.5929 -0.3101 0.2468 461 ARG B NE 10749 C CZ . ARG B 461 ? 2.5369 2.9049 2.0148 -0.5972 -0.2830 0.2845 461 ARG B CZ 10750 N NH1 . ARG B 461 ? 2.4880 2.8004 1.9841 -0.5942 -0.2643 0.2686 461 ARG B NH1 10751 N NH2 . ARG B 461 ? 2.5098 2.9154 2.0213 -0.6027 -0.2766 0.3373 461 ARG B NH2 10752 N N . CYS B 462 ? 2.7967 3.2300 1.9211 -0.5262 -0.4309 0.0923 462 CYS B N 10753 C CA . CYS B 462 ? 2.8086 3.3117 1.8694 -0.4902 -0.4195 0.1126 462 CYS B CA 10754 C C . CYS B 462 ? 2.7579 3.3135 1.8537 -0.4794 -0.3647 0.1749 462 CYS B C 10755 O O . CYS B 462 ? 2.6561 3.1887 1.8215 -0.4998 -0.3395 0.1994 462 CYS B O 10756 C CB . CYS B 462 ? 2.7503 3.2903 1.8066 -0.5037 -0.4596 0.1191 462 CYS B CB 10757 S SG . CYS B 462 ? 3.4592 4.0233 2.3891 -0.4554 -0.4924 0.0790 462 CYS B SG 10758 N N . GLY B 463 ? 3.0447 3.3153 1.9184 -0.3230 -0.6413 0.0037 463 GLY B N 10759 C CA . GLY B 463 ? 3.0332 3.3047 1.8630 -0.3553 -0.6289 0.0798 463 GLY B CA 10760 C C . GLY B 463 ? 3.0304 3.2256 1.8901 -0.3695 -0.6722 0.1443 463 GLY B C 10761 O O . GLY B 463 ? 3.0357 3.1733 1.9655 -0.3512 -0.7057 0.1249 463 GLY B O 10762 N N . PRO B 464 ? 3.0020 3.1978 1.8125 -0.4027 -0.6735 0.2197 464 PRO B N 10763 C CA . PRO B 464 ? 2.9931 3.1138 1.8309 -0.4176 -0.7187 0.2853 464 PRO B CA 10764 C C . PRO B 464 ? 3.0377 3.1497 1.8427 -0.4165 -0.7873 0.3018 464 PRO B C 10765 O O . PRO B 464 ? 3.1239 3.3034 1.8327 -0.4284 -0.8008 0.3105 464 PRO B O 10766 C CB . PRO B 464 ? 3.0626 3.2051 1.8371 -0.4573 -0.7008 0.3580 464 PRO B CB 10767 C CG . PRO B 464 ? 3.0969 3.3466 1.7777 -0.4678 -0.6658 0.3386 464 PRO B CG 10768 C CD . PRO B 464 ? 3.0165 3.2893 1.7432 -0.4293 -0.6341 0.2454 464 PRO B CD 10769 N N . GLY B 465 ? 3.0322 3.0662 1.9172 -0.4013 -0.8309 0.3033 465 GLY B N 10770 C CA . GLY B 465 ? 3.1301 3.1483 1.9982 -0.3950 -0.9008 0.3131 465 GLY B CA 10771 C C . GLY B 465 ? 3.0898 3.1385 1.9803 -0.3632 -0.9065 0.2324 465 GLY B C 10772 O O . GLY B 465 ? 3.0732 3.1010 1.9803 -0.3491 -0.9632 0.2220 465 GLY B O 10773 N N . TRP B 466 ? 3.0928 3.1895 1.9875 -0.3514 -0.8506 0.1735 466 TRP B N 10774 C CA . TRP B 466 ? 3.0889 3.2130 2.0120 -0.3220 -0.8525 0.0924 466 TRP B CA 10775 C C . TRP B 466 ? 3.0480 3.1199 2.0935 -0.2997 -0.8257 0.0398 466 TRP B C 10776 O O . TRP B 466 ? 3.0805 3.1173 2.1975 -0.2814 -0.8584 0.0070 466 TRP B O 10777 C CB . TRP B 466 ? 3.0335 3.2500 1.8764 -0.3221 -0.8167 0.0567 466 TRP B CB 10778 C CG . TRP B 466 ? 3.0432 3.3122 1.8373 -0.3086 -0.8564 0.0193 466 TRP B CG 10779 C CD1 . TRP B 466 ? 2.9930 3.2322 1.8417 -0.2859 -0.9028 -0.0188 466 TRP B CD1 10780 C CD2 . TRP B 466 ? 3.1013 3.4681 1.7823 -0.3169 -0.8544 0.0143 466 TRP B CD2 10781 N NE1 . TRP B 466 ? 3.0387 3.3470 1.8155 -0.2780 -0.9313 -0.0478 466 TRP B NE1 10782 C CE2 . TRP B 466 ? 3.1100 3.4992 1.7814 -0.2966 -0.9021 -0.0285 466 TRP B CE2 10783 C CE3 . TRP B 466 ? 3.1143 3.5588 1.7029 -0.3399 -0.8162 0.0386 466 TRP B CE3 10784 C CZ2 . TRP B 466 ? 3.1766 3.6628 1.7465 -0.2970 -0.9133 -0.0477 466 TRP B CZ2 10785 C CZ3 . TRP B 466 ? 3.1900 3.7354 1.6788 -0.3419 -0.8253 0.0193 466 TRP B CZ3 10786 C CH2 . TRP B 466 ? 3.2193 3.7846 1.6978 -0.3200 -0.8738 -0.0236 466 TRP B CH2 10787 N N . LEU B 467 ? 2.9709 3.0435 2.0373 -0.3021 -0.7662 0.0303 467 LEU B N 10788 C CA . LEU B 467 ? 2.8746 2.8890 2.0493 -0.2902 -0.7381 0.0057 467 LEU B CA 10789 C C . LEU B 467 ? 2.8453 2.8339 2.1079 -0.2665 -0.7560 -0.0569 467 LEU B C 10790 O O . LEU B 467 ? 2.8461 2.7865 2.1788 -0.2620 -0.7875 -0.0504 467 LEU B O 10791 C CB . LEU B 467 ? 2.9152 2.8714 2.1254 -0.3040 -0.7516 0.0663 467 LEU B CB 10792 C CG . LEU B 467 ? 2.8704 2.7781 2.1749 -0.2973 -0.7142 0.0534 467 LEU B CG 10793 C CD1 . LEU B 467 ? 2.7875 2.7202 2.0667 -0.3028 -0.6513 0.0491 467 LEU B CD1 10794 C CD2 . LEU B 467 ? 2.9369 2.7945 2.2724 -0.3078 -0.7431 0.1082 467 LEU B CD2 10795 N N . GLY B 468 ? 2.8237 2.8468 2.0860 -0.2518 -0.7382 -0.1195 468 GLY B N 10796 C CA . GLY B 468 ? 2.8210 2.8242 2.1644 -0.2331 -0.7557 -0.1794 468 GLY B CA 10797 C C . GLY B 468 ? 2.7782 2.7914 2.1534 -0.2207 -0.7150 -0.2416 468 GLY B C 10798 O O . GLY B 468 ? 2.7541 2.7943 2.0844 -0.2229 -0.6750 -0.2428 468 GLY B O 10799 N N . SER B 469 ? 2.7524 2.7422 2.2100 -0.2086 -0.7272 -0.2932 469 SER B N 10800 C CA . SER B 469 ? 2.6706 2.6609 2.1665 -0.1975 -0.6987 -0.3544 469 SER B CA 10801 C C . SER B 469 ? 2.6665 2.7204 2.0803 -0.1878 -0.6974 -0.3851 469 SER B C 10802 O O . SER B 469 ? 2.6007 2.6645 2.0068 -0.1821 -0.6606 -0.4110 469 SER B O 10803 C CB . SER B 469 ? 2.6736 2.6386 2.2623 -0.1897 -0.7240 -0.4034 469 SER B CB 10804 O OG . SER B 469 ? 2.6473 2.5643 2.3169 -0.1985 -0.7212 -0.3815 469 SER B OG 10805 N N . GLN B 470 ? 2.7749 2.8746 2.1274 -0.1848 -0.7397 -0.3840 470 GLN B N 10806 C CA . GLN B 470 ? 2.8766 3.0520 2.1330 -0.1793 -0.7379 -0.4010 470 GLN B CA 10807 C C . GLN B 470 ? 2.9626 3.1726 2.1236 -0.1971 -0.7543 -0.3324 470 GLN B C 10808 O O . GLN B 470 ? 2.9558 3.1809 2.0677 -0.2118 -0.7207 -0.2903 470 GLN B O 10809 C CB . GLN B 470 ? 2.9521 3.1643 2.2124 -0.1594 -0.7738 -0.4703 470 GLN B CB 10810 C CG . GLN B 470 ? 2.9061 3.0826 2.2620 -0.1446 -0.7626 -0.5389 470 GLN B CG 10811 C CD . GLN B 470 ? 2.8334 2.9415 2.2945 -0.1494 -0.7780 -0.5383 470 GLN B CD 10812 O OE1 . GLN B 470 ? 2.8116 2.9027 2.2778 -0.1584 -0.8039 -0.4955 470 GLN B OE1 10813 N NE2 . GLN B 470 ? 2.8027 2.8729 2.3502 -0.1442 -0.7636 -0.5865 470 GLN B NE2 10814 N N . CYS B 471 ? 3.0554 3.2763 2.1913 -0.1972 -0.8077 -0.3197 471 CYS B N 10815 C CA . CYS B 471 ? 3.1465 3.3716 2.2126 -0.2177 -0.8330 -0.2421 471 CYS B CA 10816 C C . CYS B 471 ? 3.1609 3.3424 2.2675 -0.2148 -0.8926 -0.2252 471 CYS B C 10817 O O . CYS B 471 ? 3.2212 3.4291 2.3199 -0.2005 -0.9346 -0.2629 471 CYS B O 10818 C CB . CYS B 471 ? 3.2633 3.5784 2.2034 -0.2249 -0.8403 -0.2318 471 CYS B CB 10819 S SG . CYS B 471 ? 3.5426 3.9189 2.4160 -0.2375 -0.7738 -0.2241 471 CYS B SG 10820 N N . GLU B 472 ? 3.1629 3.2816 2.3140 -0.2265 -0.8980 -0.1727 472 GLU B N 10821 C CA . GLU B 472 ? 3.1632 3.2445 2.3314 -0.2277 -0.9593 -0.1368 472 GLU B CA 10822 C C . GLU B 472 ? 3.1466 3.1584 2.3831 -0.2373 -0.9518 -0.0920 472 GLU B C 10823 O O . GLU B 472 ? 3.1014 3.0893 2.3977 -0.2377 -0.9019 -0.1060 472 GLU B O 10824 C CB . GLU B 472 ? 3.1262 3.2014 2.3634 -0.2048 -1.0011 -0.1984 472 GLU B CB 10825 C CG . GLU B 472 ? 3.2812 3.3954 2.4433 -0.1995 -1.0635 -0.1934 472 GLU B CG 10826 C CD . GLU B 472 ? 3.3338 3.4553 2.5603 -0.1752 -1.0997 -0.2661 472 GLU B CD 10827 O OE1 . GLU B 472 ? 3.2819 3.3756 2.6151 -0.1658 -1.0763 -0.3171 472 GLU B OE1 10828 O OE2 . GLU B 472 ? 3.4024 3.5589 2.5720 -0.1672 -1.1522 -0.2714 472 GLU B OE2 10829 N N . CYS B 473 ? 3.1849 3.1643 2.4141 -0.2434 -1.0052 -0.0407 473 CYS B N 10830 C CA . CYS B 473 ? 3.1092 3.0243 2.4048 -0.2499 -1.0084 -0.0002 473 CYS B CA 10831 C C . CYS B 473 ? 3.0531 2.9315 2.3503 -0.2493 -1.0838 0.0422 473 CYS B C 10832 O O . CYS B 473 ? 3.0628 2.9601 2.3237 -0.2408 -1.1367 0.0337 473 CYS B O 10833 C CB . CYS B 473 ? 3.1593 3.0714 2.4099 -0.2727 -0.9618 0.0533 473 CYS B CB 10834 S SG . CYS B 473 ? 3.6398 3.4812 2.9986 -0.2739 -0.9431 0.0732 473 CYS B SG 10835 N N . SER B 474 ? 3.0427 2.8669 2.3845 -0.2570 -1.0903 0.0860 474 SER B N 10836 C CA . SER B 474 ? 3.0552 2.8332 2.4018 -0.2580 -1.1628 0.1350 474 SER B CA 10837 C C . SER B 474 ? 3.0848 2.8818 2.2977 -0.2805 -1.1962 0.2032 474 SER B C 10838 O O . SER B 474 ? 3.0749 2.9225 2.1979 -0.2988 -1.1527 0.2176 474 SER B O 10839 C CB . SER B 474 ? 2.9912 2.7115 2.4107 -0.2626 -1.1556 0.1661 474 SER B CB 10840 O OG . SER B 474 ? 2.8730 2.5989 2.2329 -0.2881 -1.1074 0.2141 474 SER B OG 10841 N N . GLU B 475 ? 3.0979 2.8552 2.3026 -0.2792 -1.2744 0.2438 475 GLU B N 10842 C CA . GLU B 475 ? 3.1742 2.9487 2.2631 -0.2924 -1.3316 0.2943 475 GLU B CA 10843 C C . GLU B 475 ? 3.2157 3.0223 2.3166 -0.2646 -1.3680 0.2305 475 GLU B C 10844 O O . GLU B 475 ? 3.3377 3.1627 2.3764 -0.2611 -1.4054 0.2511 475 GLU B O 10845 C CB . GLU B 475 ? 3.1881 3.0215 2.1439 -0.3251 -1.2894 0.3384 475 GLU B CB 10846 C CG . GLU B 475 ? 3.1673 2.9725 2.1018 -0.3571 -1.2596 0.4086 475 GLU B CG 10847 C CD . GLU B 475 ? 3.1901 3.0695 2.0127 -0.3869 -1.2013 0.4329 475 GLU B CD 10848 O OE1 . GLU B 475 ? 3.2207 3.1737 1.9732 -0.3822 -1.1903 0.4031 475 GLU B OE1 10849 O OE2 . GLU B 475 ? 3.1744 3.0439 1.9871 -0.4123 -1.1627 0.4760 475 GLU B OE2 10850 N N . GLU B 476 ? 3.1251 2.9440 2.3242 -0.2411 -1.3321 0.1488 476 GLU B N 10851 C CA . GLU B 476 ? 3.1819 3.0108 2.4440 -0.2113 -1.3718 0.0808 476 GLU B CA 10852 C C . GLU B 476 ? 3.1344 2.9228 2.5477 -0.1934 -1.3606 0.0349 476 GLU B C 10853 O O . GLU B 476 ? 3.1849 2.9322 2.6687 -0.1779 -1.4200 0.0337 476 GLU B O 10854 C CB . GLU B 476 ? 3.1621 3.0625 2.3889 -0.2037 -1.3361 0.0178 476 GLU B CB 10855 C CG . GLU B 476 ? 3.2291 3.1829 2.3206 -0.2112 -1.3680 0.0414 476 GLU B CG 10856 C CD . GLU B 476 ? 3.1588 3.1806 2.2400 -0.1946 -1.3482 -0.0372 476 GLU B CD 10857 O OE1 . GLU B 476 ? 3.0432 3.0657 2.2179 -0.1817 -1.3046 -0.1034 476 GLU B OE1 10858 O OE2 . GLU B 476 ? 3.2291 3.3038 2.2091 -0.1950 -1.3780 -0.0330 476 GLU B OE2 10859 N N . ASP B 477 ? 3.0352 2.8397 2.4965 -0.1956 -1.2847 -0.0047 477 ASP B N 10860 C CA . ASP B 477 ? 2.9616 2.7370 2.5554 -0.1857 -1.2565 -0.0426 477 ASP B CA 10861 C C . ASP B 477 ? 2.9990 2.7795 2.6979 -0.1608 -1.2909 -0.1131 477 ASP B C 10862 O O . ASP B 477 ? 2.8811 2.6550 2.6899 -0.1544 -1.2602 -0.1571 477 ASP B O 10863 C CB . ASP B 477 ? 2.9441 2.6631 2.5694 -0.1925 -1.2746 0.0131 477 ASP B CB 10864 C CG . ASP B 477 ? 2.8889 2.5905 2.6298 -0.1879 -1.2267 -0.0192 477 ASP B CG 10865 O OD1 . ASP B 477 ? 2.8703 2.6000 2.6338 -0.1901 -1.1617 -0.0617 477 ASP B OD1 10866 O OD2 . ASP B 477 ? 2.9131 2.5732 2.7216 -0.1818 -1.2562 -0.0026 477 ASP B OD2 10867 N N . TYR B 478 ? 3.1896 2.9868 2.8526 -0.1485 -1.3534 -0.1239 478 TYR B N 10868 C CA . TYR B 478 ? 3.2450 3.0546 2.9997 -0.1247 -1.3929 -0.1925 478 TYR B CA 10869 C C . TYR B 478 ? 3.1348 2.9108 3.0250 -0.1130 -1.4074 -0.2133 478 TYR B C 10870 O O . TYR B 478 ? 3.1219 2.8546 3.0207 -0.1138 -1.4366 -0.1652 478 TYR B O 10871 C CB . TYR B 478 ? 3.2999 3.1556 3.0817 -0.1225 -1.3432 -0.2639 478 TYR B CB 10872 C CG . TYR B 478 ? 3.3719 3.2567 3.0554 -0.1391 -1.2834 -0.2495 478 TYR B CG 10873 C CD1 . TYR B 478 ? 3.4751 3.3976 3.0388 -0.1408 -1.3043 -0.2342 478 TYR B CD1 10874 C CD2 . TYR B 478 ? 3.3003 3.1799 3.0120 -0.1519 -1.2073 -0.2545 478 TYR B CD2 10875 C CE1 . TYR B 478 ? 3.4915 3.4498 2.9710 -0.1539 -1.2503 -0.2281 478 TYR B CE1 10876 C CE2 . TYR B 478 ? 3.2979 3.2057 2.9260 -0.1639 -1.1561 -0.2463 478 TYR B CE2 10877 C CZ . TYR B 478 ? 3.4124 3.3617 2.9273 -0.1644 -1.1774 -0.2354 478 TYR B CZ 10878 O OH . TYR B 478 ? 3.4362 3.4225 2.8731 -0.1744 -1.1269 -0.2340 478 TYR B OH 10879 N N . ARG B 479 ? 3.0545 2.8543 3.0527 -0.1030 -1.3872 -0.2876 479 ARG B N 10880 C CA . ARG B 479 ? 2.9191 2.7061 3.0477 -0.0990 -1.3677 -0.3165 479 ARG B CA 10881 C C . ARG B 479 ? 2.8908 2.6774 3.0115 -0.1198 -1.2791 -0.3051 479 ARG B C 10882 O O . ARG B 479 ? 2.9204 2.7223 2.9535 -0.1325 -1.2396 -0.2925 479 ARG B O 10883 C CB . ARG B 479 ? 2.7582 2.5788 3.0009 -0.0838 -1.3699 -0.3958 479 ARG B CB 10884 C CG . ARG B 479 ? 2.6831 2.5097 2.9289 -0.0584 -1.4268 -0.4065 479 ARG B CG 10885 C CD . ARG B 479 ? 2.5406 2.4006 2.9118 -0.0439 -1.4139 -0.4805 479 ARG B CD 10886 N NE . ARG B 479 ? 2.5647 2.4331 2.9384 -0.0190 -1.4681 -0.4962 479 ARG B NE 10887 C CZ . ARG B 479 ? 2.5937 2.4887 3.0717 -0.0021 -1.4705 -0.5545 479 ARG B CZ 10888 N NH1 . ARG B 479 ? 2.5130 2.4323 3.0990 -0.0098 -1.4188 -0.5994 479 ARG B NH1 10889 N NH2 . ARG B 479 ? 2.6961 2.5957 3.1686 0.0213 -1.5233 -0.5662 479 ARG B NH2 10890 N N . PRO B 480 ? 2.8693 2.6424 3.0808 -0.1218 -1.2490 -0.3122 480 PRO B N 10891 C CA . PRO B 480 ? 2.8521 2.6253 3.0607 -0.1402 -1.1658 -0.3047 480 PRO B CA 10892 C C . PRO B 480 ? 2.9480 2.7523 3.1404 -0.1497 -1.1145 -0.3448 480 PRO B C 10893 O O . PRO B 480 ? 2.8913 2.6931 3.0339 -0.1642 -1.0554 -0.3259 480 PRO B O 10894 C CB . PRO B 480 ? 2.7572 2.5298 3.0944 -0.1360 -1.1509 -0.3343 480 PRO B CB 10895 C CG . PRO B 480 ? 2.7738 2.5465 3.1821 -0.1136 -1.2297 -0.3579 480 PRO B CG 10896 C CD . PRO B 480 ? 2.8665 2.6219 3.1758 -0.1062 -1.2939 -0.3201 480 PRO B CD 10897 N N . SER B 481 ? 3.1037 2.9354 3.3453 -0.1406 -1.1400 -0.4019 481 SER B N 10898 C CA . SER B 481 ? 3.0907 2.9494 3.3232 -0.1469 -1.1076 -0.4462 481 SER B CA 10899 C C . SER B 481 ? 2.9531 2.8148 3.2649 -0.1622 -1.0396 -0.4763 481 SER B C 10900 O O . SER B 481 ? 2.9019 2.7813 3.2450 -0.1684 -1.0174 -0.5228 481 SER B O 10901 C CB . SER B 481 ? 3.1306 2.9932 3.2303 -0.1521 -1.0925 -0.4136 481 SER B CB 10902 O OG . SER B 481 ? 3.1101 2.9962 3.2081 -0.1557 -1.0615 -0.4604 481 SER B OG 10903 N N . GLN B 482 ? 2.8724 2.7154 3.2164 -0.1686 -1.0107 -0.4482 482 GLN B N 10904 C CA . GLN B 482 ? 2.6967 2.5424 3.1171 -0.1836 -0.9496 -0.4675 482 GLN B CA 10905 C C . GLN B 482 ? 2.5301 2.3541 2.9529 -0.1840 -0.9358 -0.4230 482 GLN B C 10906 O O . GLN B 482 ? 2.4742 2.2759 2.8236 -0.1776 -0.9622 -0.3734 482 GLN B O 10907 C CB . GLN B 482 ? 2.6219 2.4648 2.9989 -0.1990 -0.8906 -0.4729 482 GLN B CB 10908 C CG . GLN B 482 ? 2.5259 2.3884 2.9780 -0.2090 -0.8743 -0.5327 482 GLN B CG 10909 C CD . GLN B 482 ? 2.4088 2.2836 2.9765 -0.2225 -0.8454 -0.5565 482 GLN B CD 10910 O OE1 . GLN B 482 ? 2.4072 2.2739 2.9899 -0.2256 -0.8208 -0.5286 482 GLN B OE1 10911 N NE2 . GLN B 482 ? 2.3048 2.2041 2.9558 -0.2317 -0.8480 -0.6099 482 GLN B NE2 10912 N N . GLN B 483 ? 2.4076 2.2401 2.9140 -0.1931 -0.8951 -0.4401 483 GLN B N 10913 C CA . GLN B 483 ? 2.2485 2.0630 2.7547 -0.1943 -0.8721 -0.4020 483 GLN B CA 10914 C C . GLN B 483 ? 2.2256 2.0210 2.6489 -0.2082 -0.8137 -0.3680 483 GLN B C 10915 O O . GLN B 483 ? 2.2319 2.0068 2.6186 -0.2092 -0.7965 -0.3253 483 GLN B O 10916 C CB . GLN B 483 ? 2.1519 1.9927 2.7768 -0.1978 -0.8502 -0.4370 483 GLN B CB 10917 C CG . GLN B 483 ? 2.1415 2.0079 2.8172 -0.2180 -0.7987 -0.4779 483 GLN B CG 10918 C CD . GLN B 483 ? 2.0405 1.9512 2.8436 -0.2217 -0.7955 -0.5254 483 GLN B CD 10919 O OE1 . GLN B 483 ? 2.0297 1.9528 2.8859 -0.2069 -0.8236 -0.5288 483 GLN B OE1 10920 N NE2 . GLN B 483 ? 1.9118 1.8491 2.7678 -0.2422 -0.7628 -0.5641 483 GLN B NE2 10921 N N . ASP B 484 ? 2.3160 2.1185 2.7159 -0.2178 -0.7865 -0.3912 484 ASP B N 10922 C CA . ASP B 484 ? 2.3700 2.1577 2.7010 -0.2289 -0.7328 -0.3715 484 ASP B CA 10923 C C . ASP B 484 ? 2.2572 2.0381 2.6295 -0.2401 -0.6783 -0.3618 484 ASP B C 10924 O O . ASP B 484 ? 2.2476 2.0117 2.5641 -0.2462 -0.6362 -0.3355 484 ASP B O 10925 C CB . ASP B 484 ? 2.4896 2.2630 2.7064 -0.2231 -0.7461 -0.3229 484 ASP B CB 10926 C CG . ASP B 484 ? 2.5391 2.3079 2.6828 -0.2304 -0.7001 -0.3153 484 ASP B CG 10927 O OD1 . ASP B 484 ? 2.5990 2.3735 2.7633 -0.2351 -0.6804 -0.3542 484 ASP B OD1 10928 O OD2 . ASP B 484 ? 2.4949 2.2544 2.5645 -0.2316 -0.6855 -0.2720 484 ASP B OD2 10929 N N . GLU B 485 ? 2.1582 1.9582 2.6305 -0.2421 -0.6801 -0.3876 485 GLU B N 10930 C CA . GLU B 485 ? 2.1182 1.9221 2.6374 -0.2504 -0.6362 -0.3809 485 GLU B CA 10931 C C . GLU B 485 ? 2.1594 1.9373 2.6102 -0.2449 -0.6229 -0.3291 485 GLU B C 10932 O O . GLU B 485 ? 2.1345 1.8995 2.5505 -0.2543 -0.5729 -0.3114 485 GLU B O 10933 C CB . GLU B 485 ? 2.1225 1.9306 2.6656 -0.2717 -0.5800 -0.4012 485 GLU B CB 10934 C CG . GLU B 485 ? 2.1914 2.0281 2.8163 -0.2828 -0.5897 -0.4525 485 GLU B CG 10935 C CD . GLU B 485 ? 2.1838 2.0248 2.8475 -0.3092 -0.5344 -0.4672 485 GLU B CD 10936 O OE1 . GLU B 485 ? 2.1997 2.0239 2.8324 -0.3164 -0.4898 -0.4387 485 GLU B OE1 10937 O OE2 . GLU B 485 ? 2.1169 1.9777 2.8425 -0.3241 -0.5372 -0.5060 485 GLU B OE2 10938 N N . CYS B 486 ? 2.1641 1.9324 2.5978 -0.2304 -0.6706 -0.3045 486 CYS B N 10939 C CA . CYS B 486 ? 2.0316 1.7751 2.4072 -0.2273 -0.6649 -0.2540 486 CYS B CA 10940 C C . CYS B 486 ? 1.9376 1.6881 2.3739 -0.2289 -0.6298 -0.2558 486 CYS B C 10941 O O . CYS B 486 ? 1.9386 1.6716 2.3366 -0.2295 -0.6084 -0.2204 486 CYS B O 10942 C CB . CYS B 486 ? 2.0859 1.8135 2.4367 -0.2144 -0.7308 -0.2259 486 CYS B CB 10943 S SG . CYS B 486 ? 1.7082 1.4260 1.9424 -0.2156 -0.7631 -0.1991 486 CYS B SG 10944 N N . SER B 487 ? 1.8995 1.6818 2.4324 -0.2303 -0.6242 -0.2997 487 SER B N 10945 C CA . SER B 487 ? 1.9702 1.7733 2.5641 -0.2344 -0.5841 -0.3109 487 SER B CA 10946 C C . SER B 487 ? 2.0582 1.8822 2.6774 -0.2548 -0.5317 -0.3389 487 SER B C 10947 O O . SER B 487 ? 2.0778 1.9076 2.7031 -0.2623 -0.5405 -0.3630 487 SER B O 10948 C CB . SER B 487 ? 1.9421 1.7747 2.6342 -0.2197 -0.6226 -0.3399 487 SER B CB 10949 O OG . SER B 487 ? 1.9190 1.7225 2.5889 -0.2018 -0.6756 -0.3101 487 SER B OG 10950 N N . PRO B 488 ? 2.0142 1.8478 2.6467 -0.2648 -0.4792 -0.3346 488 PRO B N 10951 C CA . PRO B 488 ? 1.9655 1.8145 2.6197 -0.2881 -0.4294 -0.3540 488 PRO B CA 10952 C C . PRO B 488 ? 1.9557 1.8485 2.7009 -0.2987 -0.4416 -0.4026 488 PRO B C 10953 O O . PRO B 488 ? 2.0167 1.9117 2.7704 -0.3199 -0.4179 -0.4182 488 PRO B O 10954 C CB . PRO B 488 ? 1.8705 1.7335 2.5389 -0.2923 -0.3841 -0.3428 488 PRO B CB 10955 C CG . PRO B 488 ? 1.8397 1.7075 2.5256 -0.2694 -0.4169 -0.3334 488 PRO B CG 10956 C CD . PRO B 488 ? 1.9033 1.7328 2.5304 -0.2555 -0.4659 -0.3100 488 PRO B CD 10957 N N . ARG B 489 ? 1.8740 1.8010 2.6902 -0.2840 -0.4806 -0.4276 489 ARG B N 10958 C CA . ARG B 489 ? 1.8355 1.8099 2.7427 -0.2902 -0.5008 -0.4779 489 ARG B CA 10959 C C . ARG B 489 ? 1.7872 1.7574 2.7093 -0.2647 -0.5732 -0.4894 489 ARG B C 10960 O O . ARG B 489 ? 1.7716 1.7150 2.6604 -0.2430 -0.6057 -0.4619 489 ARG B O 10961 C CB . ARG B 489 ? 1.7391 1.7787 2.7410 -0.2992 -0.4727 -0.5101 489 ARG B CB 10962 C CG . ARG B 489 ? 1.5711 1.6195 2.5857 -0.2773 -0.4801 -0.4996 489 ARG B CG 10963 C CD . ARG B 489 ? 1.5530 1.6756 2.6558 -0.2874 -0.4451 -0.5351 489 ARG B CD 10964 N NE . ARG B 489 ? 1.6099 1.7421 2.7268 -0.2645 -0.4521 -0.5294 489 ARG B NE 10965 C CZ . ARG B 489 ? 1.5756 1.7753 2.7626 -0.2664 -0.4252 -0.5597 489 ARG B CZ 10966 N NH1 . ARG B 489 ? 1.5644 1.8308 2.8106 -0.2937 -0.3867 -0.5942 489 ARG B NH1 10967 N NH2 . ARG B 489 ? 1.5380 1.7418 2.7368 -0.2424 -0.4372 -0.5565 489 ARG B NH2 10968 N N . GLU B 490 ? 1.7179 1.7128 2.6905 -0.2683 -0.6006 -0.5286 490 GLU B N 10969 C CA . GLU B 490 ? 1.7736 1.7622 2.7553 -0.2440 -0.6731 -0.5400 490 GLU B CA 10970 C C . GLU B 490 ? 1.8253 1.8507 2.8960 -0.2225 -0.7115 -0.5672 490 GLU B C 10971 O O . GLU B 490 ? 1.8441 1.8587 2.9201 -0.1970 -0.7740 -0.5699 490 GLU B O 10972 C CB . GLU B 490 ? 1.7992 1.8049 2.8101 -0.2531 -0.6919 -0.5780 490 GLU B CB 10973 C CG . GLU B 490 ? 1.8009 1.8751 2.9199 -0.2608 -0.6737 -0.6276 490 GLU B CG 10974 C CD . GLU B 490 ? 1.8407 1.9302 2.9800 -0.2559 -0.7007 -0.6571 490 GLU B CD 10975 O OE1 . GLU B 490 ? 1.9156 1.9647 2.9921 -0.2463 -0.7417 -0.6450 490 GLU B OE1 10976 O OE2 . GLU B 490 ? 1.7806 1.9260 2.9981 -0.2621 -0.6815 -0.6933 490 GLU B OE2 10977 N N . GLY B 491 ? 1.8096 1.8793 2.9434 -0.2297 -0.6715 -0.5850 491 GLY B N 10978 C CA . GLY B 491 ? 1.7256 1.8355 2.9305 -0.2012 -0.6909 -0.6068 491 GLY B CA 10979 C C . GLY B 491 ? 1.7406 1.8118 2.9171 -0.1825 -0.7160 -0.5739 491 GLY B C 10980 O O . GLY B 491 ? 1.7877 1.8897 3.0220 -0.1608 -0.7211 -0.5906 491 GLY B O 10981 N N . GLN B 492 ? 1.7758 1.7793 2.8505 -0.1867 -0.7229 -0.5211 492 GLN B N 10982 C CA . GLN B 492 ? 1.8447 1.8039 2.8729 -0.1708 -0.7394 -0.4770 492 GLN B CA 10983 C C . GLN B 492 ? 1.9260 1.8246 2.8812 -0.1575 -0.8017 -0.4370 492 GLN B C 10984 O O . GLN B 492 ? 1.8188 1.7039 2.7268 -0.1649 -0.8128 -0.4326 492 GLN B O 10985 C CB . GLN B 492 ? 1.7723 1.7125 2.7300 -0.1888 -0.6709 -0.4388 492 GLN B CB 10986 C CG . GLN B 492 ? 1.6886 1.6859 2.7090 -0.2016 -0.6115 -0.4695 492 GLN B CG 10987 C CD . GLN B 492 ? 1.6877 1.7220 2.7926 -0.1803 -0.6316 -0.4968 492 GLN B CD 10988 O OE1 . GLN B 492 ? 1.6813 1.6799 2.7786 -0.1573 -0.6803 -0.4769 492 GLN B OE1 10989 N NE2 . GLN B 492 ? 1.6758 1.7842 2.8633 -0.1887 -0.5955 -0.5433 492 GLN B NE2 10990 N N . PRO B 493 ? 1.9585 1.8216 2.9041 -0.1390 -0.8442 -0.4073 493 PRO B N 10991 C CA . PRO B 493 ? 1.9892 1.7949 2.8653 -0.1293 -0.9077 -0.3632 493 PRO B CA 10992 C C . PRO B 493 ? 1.9854 1.7504 2.7312 -0.1482 -0.8786 -0.3066 493 PRO B C 10993 O O . PRO B 493 ? 1.9601 1.7381 2.6720 -0.1667 -0.8123 -0.3063 493 PRO B O 10994 C CB . PRO B 493 ? 1.8839 1.6629 2.7913 -0.1102 -0.9486 -0.3449 493 PRO B CB 10995 C CG . PRO B 493 ? 1.7447 1.5561 2.6919 -0.1152 -0.8866 -0.3606 493 PRO B CG 10996 C CD . PRO B 493 ? 1.7861 1.6638 2.7927 -0.1264 -0.8395 -0.4165 493 PRO B CD 10997 N N . VAL B 494 ? 1.9791 1.6974 2.6537 -0.1438 -0.9305 -0.2601 494 VAL B N 10998 C CA . VAL B 494 ? 1.9614 1.6498 2.5112 -0.1607 -0.9102 -0.2076 494 VAL B CA 10999 C C . VAL B 494 ? 1.8901 1.5705 2.4002 -0.1739 -0.8466 -0.1784 494 VAL B C 11000 O O . VAL B 494 ? 1.9836 1.6633 2.5463 -0.1671 -0.8401 -0.1798 494 VAL B O 11001 C CB . VAL B 494 ? 2.0999 1.7434 2.5845 -0.1562 -0.9794 -0.1566 494 VAL B CB 11002 C CG1 . VAL B 494 ? 2.1296 1.7765 2.5380 -0.1625 -0.9957 -0.1509 494 VAL B CG1 11003 C CG2 . VAL B 494 ? 2.1498 1.7813 2.7207 -0.1329 -1.0540 -0.1731 494 VAL B CG2 11004 N N . CYS B 495 ? 1.8348 1.5121 2.2557 -0.1906 -0.8022 -0.1565 495 CYS B N 11005 C CA . CYS B 495 ? 1.9188 1.5963 2.3090 -0.2023 -0.7353 -0.1406 495 CYS B CA 11006 C C . CYS B 495 ? 1.8139 1.4638 2.1915 -0.2006 -0.7421 -0.0983 495 CYS B C 11007 O O . CYS B 495 ? 1.8396 1.4591 2.1519 -0.2049 -0.7753 -0.0503 495 CYS B O 11008 C CB . CYS B 495 ? 2.1205 1.7960 2.4113 -0.2168 -0.7001 -0.1224 495 CYS B CB 11009 S SG . CYS B 495 ? 2.7789 2.4318 2.9588 -0.2216 -0.7472 -0.0708 495 CYS B SG 11010 N N . SER B 496 ? 1.7025 1.3663 2.1425 -0.1963 -0.7091 -0.1167 496 SER B N 11011 C CA . SER B 496 ? 1.7042 1.3470 2.1439 -0.1940 -0.7069 -0.0854 496 SER B CA 11012 C C . SER B 496 ? 1.7473 1.3514 2.1870 -0.1866 -0.7795 -0.0507 496 SER B C 11013 O O . SER B 496 ? 1.8855 1.4601 2.2843 -0.1935 -0.7825 -0.0051 496 SER B O 11014 C CB . SER B 496 ? 1.7663 1.3992 2.1156 -0.2102 -0.6540 -0.0485 496 SER B CB 11015 O OG . SER B 496 ? 1.6754 1.3353 2.0230 -0.2164 -0.5922 -0.0774 496 SER B OG 11016 N N . GLN B 497 ? 1.7659 1.3690 2.2554 -0.1732 -0.8395 -0.0726 497 GLN B N 11017 C CA . GLN B 497 ? 1.9477 1.5068 2.4290 -0.1669 -0.9180 -0.0365 497 GLN B CA 11018 C C . GLN B 497 ? 2.1289 1.6571 2.4884 -0.1888 -0.9189 0.0299 497 GLN B C 11019 O O . GLN B 497 ? 2.1787 1.7239 2.4688 -0.2003 -0.8948 0.0321 497 GLN B O 11020 C CB . GLN B 497 ? 1.9014 1.4401 2.4562 -0.1527 -0.9476 -0.0352 497 GLN B CB 11021 C CG . GLN B 497 ? 1.7744 1.3585 2.4463 -0.1329 -0.9310 -0.1034 497 GLN B CG 11022 C CD . GLN B 497 ? 1.7789 1.3893 2.5233 -0.1158 -0.9733 -0.1551 497 GLN B CD 11023 O OE1 . GLN B 497 ? 1.8312 1.4126 2.5547 -0.1115 -1.0361 -0.1381 497 GLN B OE1 11024 N NE2 . GLN B 497 ? 1.7709 1.4404 2.6010 -0.1071 -0.9393 -0.2186 497 GLN B NE2 11025 N N . ARG B 498 ? 2.2218 1.7087 2.5594 -0.1952 -0.9476 0.0812 498 ARG B N 11026 C CA . ARG B 498 ? 2.3085 1.7789 2.5354 -0.2215 -0.9272 0.1439 498 ARG B CA 11027 C C . ARG B 498 ? 2.5400 2.0184 2.6758 -0.2339 -0.9405 0.1632 498 ARG B C 11028 O O . ARG B 498 ? 2.4635 1.9777 2.5594 -0.2392 -0.8896 0.1416 498 ARG B O 11029 C CB . ARG B 498 ? 2.1650 1.6630 2.3708 -0.2305 -0.8431 0.1361 498 ARG B CB 11030 C CG . ARG B 498 ? 2.1891 1.6639 2.3534 -0.2473 -0.8299 0.1886 498 ARG B CG 11031 C CD . ARG B 498 ? 2.0971 1.6009 2.2575 -0.2497 -0.7509 0.1705 498 ARG B CD 11032 N NE . ARG B 498 ? 1.9512 1.4727 2.2113 -0.2283 -0.7321 0.1162 498 ARG B NE 11033 C CZ . ARG B 498 ? 1.7598 1.3033 2.0341 -0.2264 -0.6720 0.0972 498 ARG B CZ 11034 N NH1 . ARG B 498 ? 1.7152 1.2626 1.9155 -0.2420 -0.6264 0.1255 498 ARG B NH1 11035 N NH2 . ARG B 498 ? 1.6858 1.2517 2.0483 -0.2086 -0.6582 0.0487 498 ARG B NH2 11036 N N . GLY B 499 ? 2.7950 2.2428 2.9095 -0.2344 -1.0134 0.1940 499 GLY B N 11037 C CA . GLY B 499 ? 2.9308 2.3904 2.9478 -0.2478 -1.0269 0.2171 499 GLY B CA 11038 C C . GLY B 499 ? 2.8221 2.3202 2.8601 -0.2329 -1.0178 0.1570 499 GLY B C 11039 O O . GLY B 499 ? 2.8003 2.3214 2.7588 -0.2421 -1.0118 0.1623 499 GLY B O 11040 N N . GLU B 500 ? 2.7338 2.2430 2.8822 -0.2106 -1.0172 0.0978 500 GLU B N 11041 C CA . GLU B 500 ? 2.7520 2.2963 2.9445 -0.1967 -1.0157 0.0362 500 GLU B CA 11042 C C . GLU B 500 ? 2.7555 2.3377 2.8880 -0.2085 -0.9525 0.0175 500 GLU B C 11043 O O . GLU B 500 ? 2.6740 2.2656 2.7764 -0.2202 -0.8900 0.0262 500 GLU B O 11044 C CB . GLU B 500 ? 2.8673 2.3961 3.0531 -0.1864 -1.0973 0.0410 500 GLU B CB 11045 C CG . GLU B 500 ? 2.8925 2.3686 3.0984 -0.1800 -1.1727 0.0825 500 GLU B CG 11046 C CD . GLU B 500 ? 2.7669 2.2345 3.0948 -0.1608 -1.1798 0.0495 500 GLU B CD 11047 O OE1 . GLU B 500 ? 2.7503 2.2574 3.1679 -0.1448 -1.1576 -0.0180 500 GLU B OE1 11048 O OE2 . GLU B 500 ? 2.6879 2.1127 3.0234 -0.1629 -1.2080 0.0899 500 GLU B OE2 11049 N N . CYS B 501 ? 2.8741 2.4768 2.9924 -0.2036 -0.9732 -0.0102 501 CYS B N 11050 C CA . CYS B 501 ? 2.8052 2.4419 2.8730 -0.2118 -0.9245 -0.0341 501 CYS B CA 11051 C C . CYS B 501 ? 2.7618 2.4079 2.7587 -0.2116 -0.9697 -0.0269 501 CYS B C 11052 O O . CYS B 501 ? 2.7566 2.3971 2.7913 -0.1979 -1.0306 -0.0422 501 CYS B O 11053 C CB . CYS B 501 ? 2.7486 2.4126 2.9080 -0.2040 -0.8882 -0.1009 501 CYS B CB 11054 S SG . CYS B 501 ? 2.8058 2.5003 2.9199 -0.2148 -0.8222 -0.1317 501 CYS B SG 11055 N N . LEU B 502 ? 2.6824 2.3473 2.5777 -0.2253 -0.9416 -0.0067 502 LEU B N 11056 C CA . LEU B 502 ? 2.6378 2.3188 2.4515 -0.2267 -0.9829 0.0048 502 LEU B CA 11057 C C . LEU B 502 ? 2.6201 2.3439 2.3916 -0.2276 -0.9446 -0.0353 502 LEU B C 11058 O O . LEU B 502 ? 2.6425 2.3823 2.3657 -0.2384 -0.8892 -0.0286 502 LEU B O 11059 C CB . LEU B 502 ? 2.7237 2.3915 2.4349 -0.2451 -1.0034 0.0800 502 LEU B CB 11060 C CG . LEU B 502 ? 2.8711 2.4928 2.5923 -0.2452 -1.0737 0.1295 502 LEU B CG 11061 C CD1 . LEU B 502 ? 2.8861 2.4707 2.6953 -0.2412 -1.0649 0.1355 502 LEU B CD1 11062 C CD2 . LEU B 502 ? 2.9620 2.5819 2.5610 -0.2694 -1.0940 0.2029 502 LEU B CD2 11063 N N . CYS B 503 ? 2.6277 2.3695 2.4224 -0.2146 -0.9779 -0.0796 503 CYS B N 11064 C CA . CYS B 503 ? 2.5401 2.3220 2.2922 -0.2127 -0.9594 -0.1197 503 CYS B CA 11065 C C . CYS B 503 ? 2.4188 2.2132 2.1769 -0.2188 -0.8851 -0.1454 503 CYS B C 11066 O O . CYS B 503 ? 2.4381 2.2535 2.1122 -0.2274 -0.8544 -0.1282 503 CYS B O 11067 C CB . CYS B 503 ? 2.6027 2.4099 2.2300 -0.2196 -0.9874 -0.0833 503 CYS B CB 11068 S SG . CYS B 503 ? 3.5528 3.3614 3.0715 -0.2442 -0.9578 -0.0058 503 CYS B SG 11069 N N . GLY B 504 ? 2.4028 2.1871 2.2600 -0.2147 -0.8575 -0.1872 504 GLY B N 11070 C CA . GLY B 504 ? 2.3827 2.1685 2.2485 -0.2214 -0.7906 -0.2040 504 GLY B CA 11071 C C . GLY B 504 ? 2.3214 2.0881 2.1636 -0.2312 -0.7564 -0.1552 504 GLY B C 11072 O O . GLY B 504 ? 2.1610 1.9040 2.0606 -0.2310 -0.7636 -0.1381 504 GLY B O 11073 N N . GLN B 505 ? 2.2826 2.0637 2.0453 -0.2384 -0.7203 -0.1379 505 GLN B N 11074 C CA . GLN B 505 ? 2.2915 2.0594 2.0330 -0.2479 -0.6799 -0.0990 505 GLN B CA 11075 C C . GLN B 505 ? 2.2686 2.0120 2.0145 -0.2532 -0.7107 -0.0467 505 GLN B C 11076 O O . GLN B 505 ? 2.3270 2.0721 2.0249 -0.2564 -0.7585 -0.0148 505 GLN B O 11077 C CB . GLN B 505 ? 2.3896 2.1882 2.0320 -0.2543 -0.6523 -0.0853 505 GLN B CB 11078 C CG . GLN B 505 ? 2.4316 2.2527 2.0685 -0.2463 -0.6267 -0.1396 505 GLN B CG 11079 C CD . GLN B 505 ? 2.5252 2.3880 2.0648 -0.2491 -0.6073 -0.1337 505 GLN B CD 11080 O OE1 . GLN B 505 ? 2.5955 2.4762 2.0660 -0.2605 -0.6135 -0.0863 505 GLN B OE1 11081 N NE2 . GLN B 505 ? 2.5304 2.4113 2.0672 -0.2395 -0.5850 -0.1832 505 GLN B NE2 11082 N N . CYS B 506 ? 2.1964 1.9158 2.0012 -0.2540 -0.6849 -0.0386 506 CYS B N 11083 C CA . CYS B 506 ? 2.2229 1.9139 2.0598 -0.2549 -0.7175 -0.0015 506 CYS B CA 11084 C C . CYS B 506 ? 2.3434 2.0287 2.1027 -0.2700 -0.7160 0.0595 506 CYS B C 11085 O O . CYS B 506 ? 2.3690 2.0612 2.1014 -0.2775 -0.6665 0.0701 506 CYS B O 11086 C CB . CYS B 506 ? 2.1195 1.7951 2.0531 -0.2488 -0.6904 -0.0223 506 CYS B CB 11087 S SG . CYS B 506 ? 1.8384 1.4890 1.8629 -0.2374 -0.7496 -0.0191 506 CYS B SG 11088 N N . VAL B 507 ? 2.4682 2.1404 2.1923 -0.2760 -0.7718 0.1013 507 VAL B N 11089 C CA . VAL B 507 ? 2.5236 2.1885 2.1787 -0.2958 -0.7723 0.1648 507 VAL B CA 11090 C C . VAL B 507 ? 2.5391 2.1569 2.2578 -0.2947 -0.8072 0.1949 507 VAL B C 11091 O O . VAL B 507 ? 2.4873 2.0788 2.2349 -0.2879 -0.8704 0.2045 507 VAL B O 11092 C CB . VAL B 507 ? 2.5487 2.2377 2.0979 -0.3101 -0.8054 0.1991 507 VAL B CB 11093 C CG1 . VAL B 507 ? 2.6098 2.3418 2.1318 -0.3002 -0.7898 0.1481 507 VAL B CG1 11094 C CG2 . VAL B 507 ? 2.6040 2.2617 2.1561 -0.3098 -0.8833 0.2306 507 VAL B CG2 11095 N N . CYS B 508 ? 2.5780 2.1847 2.3295 -0.2973 -0.7680 0.2018 508 CYS B N 11096 C CA . CYS B 508 ? 2.6133 2.1780 2.4126 -0.2986 -0.8012 0.2353 508 CYS B CA 11097 C C . CYS B 508 ? 2.6389 2.1991 2.4009 -0.3178 -0.7691 0.2793 508 CYS B C 11098 O O . CYS B 508 ? 2.6921 2.2483 2.5077 -0.3108 -0.7318 0.2622 508 CYS B O 11099 C CB . CYS B 508 ? 2.5299 2.0854 2.4445 -0.2759 -0.7928 0.1852 508 CYS B CB 11100 S SG . CYS B 508 ? 2.0613 1.6533 1.9958 -0.2698 -0.7062 0.1319 508 CYS B SG 11101 N N . HIS B 509 ? 2.6693 2.2267 2.3494 -0.3426 -0.7903 0.3390 509 HIS B N 11102 C CA . HIS B 509 ? 2.6932 2.2559 2.3385 -0.3633 -0.7527 0.3760 509 HIS B CA 11103 C C . HIS B 509 ? 2.7044 2.2143 2.4056 -0.3675 -0.7926 0.4127 509 HIS B C 11104 O O . HIS B 509 ? 2.6195 2.1221 2.3647 -0.3651 -0.7615 0.4080 509 HIS B O 11105 C CB . HIS B 509 ? 2.8308 2.4310 2.3583 -0.3929 -0.7420 0.4197 509 HIS B CB 11106 C CG . HIS B 509 ? 2.9500 2.5828 2.4174 -0.3907 -0.7589 0.4044 509 HIS B CG 11107 N ND1 . HIS B 509 ? 2.9552 2.5964 2.4642 -0.3639 -0.7595 0.3434 509 HIS B ND1 11108 C CD2 . HIS B 509 ? 3.0724 2.7371 2.4385 -0.4138 -0.7750 0.4423 509 HIS B CD2 11109 C CE1 . HIS B 509 ? 3.0609 2.7337 2.5002 -0.3680 -0.7786 0.3425 509 HIS B CE1 11110 N NE2 . HIS B 509 ? 3.1368 2.8268 2.4861 -0.3975 -0.7875 0.4015 509 HIS B NE2 11111 N N . SER B 510 ? 2.7981 2.2703 2.4966 -0.3727 -0.8653 0.4483 510 SER B N 11112 C CA . SER B 510 ? 2.7857 2.1978 2.5410 -0.3749 -0.9215 0.4838 510 SER B CA 11113 C C . SER B 510 ? 2.7387 2.1389 2.4532 -0.4077 -0.9100 0.5460 510 SER B C 11114 O O . SER B 510 ? 2.8167 2.1628 2.5583 -0.4182 -0.9649 0.5904 510 SER B O 11115 C CB . SER B 510 ? 2.6959 2.0911 2.5756 -0.3413 -0.9202 0.4268 510 SER B CB 11116 O OG . SER B 510 ? 2.7037 2.0414 2.6467 -0.3383 -0.9824 0.4525 510 SER B OG 11117 N N . SER B 511 ? 2.6371 2.0872 2.2913 -0.4237 -0.8411 0.5471 511 SER B N 11118 C CA . SER B 511 ? 2.7140 2.1696 2.3130 -0.4606 -0.8244 0.6066 511 SER B CA 11119 C C . SER B 511 ? 2.6955 2.1086 2.3716 -0.4608 -0.8311 0.6194 511 SER B C 11120 O O . SER B 511 ? 2.6653 2.0822 2.3071 -0.4919 -0.8160 0.6658 511 SER B O 11121 C CB . SER B 511 ? 2.8049 2.2484 2.3187 -0.4962 -0.8766 0.6795 511 SER B CB 11122 O OG . SER B 511 ? 2.7937 2.1630 2.3595 -0.4945 -0.9568 0.7118 511 SER B OG 11123 N N . ASP B 512 ? 2.6412 2.0190 2.4230 -0.4271 -0.8541 0.5766 512 ASP B N 11124 C CA . ASP B 512 ? 2.5387 1.8722 2.3990 -0.4249 -0.8755 0.5880 512 ASP B CA 11125 C C . ASP B 512 ? 2.3783 1.7439 2.2630 -0.4197 -0.8053 0.5595 512 ASP B C 11126 O O . ASP B 512 ? 2.2291 1.6235 2.1547 -0.3904 -0.7621 0.4970 512 ASP B O 11127 C CB . ASP B 512 ? 2.4672 1.7587 2.4358 -0.3887 -0.9306 0.5477 512 ASP B CB 11128 C CG . ASP B 512 ? 2.1941 1.5256 2.2109 -0.3524 -0.8904 0.4677 512 ASP B CG 11129 O OD1 . ASP B 512 ? 2.0668 1.3909 2.1829 -0.3239 -0.8937 0.4210 512 ASP B OD1 11130 O OD2 . ASP B 512 ? 2.1704 1.5432 2.1269 -0.3537 -0.8561 0.4510 512 ASP B OD2 11131 N N . PHE B 513 ? 2.3655 1.7254 2.2237 -0.4504 -0.7969 0.6085 513 PHE B N 11132 C CA . PHE B 513 ? 2.1320 1.5143 2.0164 -0.4490 -0.7420 0.5917 513 PHE B CA 11133 C C . PHE B 513 ? 2.0366 1.4754 1.9133 -0.4249 -0.6678 0.5298 513 PHE B C 11134 O O . PHE B 513 ? 1.9311 1.3718 1.8797 -0.3960 -0.6453 0.4810 513 PHE B O 11135 C CB . PHE B 513 ? 2.0124 1.3467 2.0067 -0.4302 -0.7772 0.5778 513 PHE B CB 11136 C CG . PHE B 513 ? 2.0164 1.3247 2.0958 -0.3914 -0.8188 0.5291 513 PHE B CG 11137 C CD1 . PHE B 513 ? 1.8695 1.2107 2.0040 -0.3553 -0.7777 0.4573 513 PHE B CD1 11138 C CD2 . PHE B 513 ? 2.1846 1.4375 2.2915 -0.3920 -0.9008 0.5555 513 PHE B CD2 11139 C CE1 . PHE B 513 ? 1.8365 1.1650 2.0525 -0.3223 -0.8132 0.4100 513 PHE B CE1 11140 C CE2 . PHE B 513 ? 2.1664 1.4026 2.3580 -0.3548 -0.9400 0.5051 513 PHE B CE2 11141 C CZ . PHE B 513 ? 1.9949 1.2733 2.2421 -0.3206 -0.8942 0.4310 513 PHE B CZ 11142 N N . GLY B 514 ? 2.1850 1.6707 1.9741 -0.4373 -0.6315 0.5320 514 GLY B N 11143 C CA . GLY B 514 ? 2.1599 1.6929 1.9378 -0.4162 -0.5665 0.4769 514 GLY B CA 11144 C C . GLY B 514 ? 2.1812 1.7461 1.8934 -0.4155 -0.5586 0.4628 514 GLY B C 11145 O O . GLY B 514 ? 2.1923 1.7537 1.8507 -0.4357 -0.5961 0.5009 514 GLY B O 11146 N N . LYS B 515 ? 2.1691 1.7639 1.8861 -0.3923 -0.5119 0.4080 515 LYS B N 11147 C CA . LYS B 515 ? 2.1876 1.8085 1.8599 -0.3857 -0.5067 0.3827 515 LYS B CA 11148 C C . LYS B 515 ? 2.2138 1.8228 1.9562 -0.3537 -0.5029 0.3249 515 LYS B C 11149 O O . LYS B 515 ? 2.1806 1.7906 1.9723 -0.3368 -0.4675 0.2920 515 LYS B O 11150 C CB . LYS B 515 ? 2.1633 1.8399 1.7602 -0.3938 -0.4526 0.3729 515 LYS B CB 11151 C CG . LYS B 515 ? 2.1422 1.8333 1.7658 -0.3787 -0.3963 0.3394 515 LYS B CG 11152 C CD . LYS B 515 ? 2.1884 1.9344 1.7411 -0.3826 -0.3502 0.3234 515 LYS B CD 11153 C CE . LYS B 515 ? 2.1485 1.9038 1.7277 -0.3648 -0.2993 0.2894 515 LYS B CE 11154 N NZ . LYS B 515 ? 2.1154 1.9233 1.6322 -0.3644 -0.2591 0.2680 515 LYS B NZ 11155 N N . ILE B 516 ? 2.2450 1.8458 1.9913 -0.3472 -0.5402 0.3136 516 ILE B N 11156 C CA . ILE B 516 ? 2.0429 1.6374 1.8586 -0.3213 -0.5404 0.2601 516 ILE B CA 11157 C C . ILE B 516 ? 2.0122 1.6377 1.7872 -0.3161 -0.5175 0.2257 516 ILE B C 11158 O O . ILE B 516 ? 2.1135 1.7532 1.8250 -0.3269 -0.5388 0.2416 516 ILE B O 11159 C CB . ILE B 516 ? 1.9842 1.5444 1.8586 -0.3133 -0.6063 0.2634 516 ILE B CB 11160 C CG1 . ILE B 516 ? 2.1243 1.6483 2.0348 -0.3199 -0.6397 0.3017 516 ILE B CG1 11161 C CG2 . ILE B 516 ? 1.8908 1.4539 1.8488 -0.2882 -0.6014 0.2046 516 ILE B CG2 11162 C CD1 . ILE B 516 ? 2.2281 1.7135 2.1970 -0.3107 -0.7125 0.3069 516 ILE B CD1 11163 N N . THR B 517 ? 1.8929 1.5287 1.7037 -0.3003 -0.4759 0.1790 517 THR B N 11164 C CA . THR B 517 ? 1.9310 1.5903 1.7125 -0.2949 -0.4556 0.1433 517 THR B CA 11165 C C . THR B 517 ? 1.8723 1.5264 1.7270 -0.2784 -0.4414 0.0933 517 THR B C 11166 O O . THR B 517 ? 1.7777 1.4179 1.7043 -0.2704 -0.4413 0.0834 517 THR B O 11167 C CB . THR B 517 ? 2.0133 1.7008 1.7296 -0.2998 -0.4062 0.1418 517 THR B CB 11168 O OG1 . THR B 517 ? 2.0621 1.7668 1.7624 -0.2912 -0.3895 0.1006 517 THR B OG1 11169 C CG2 . THR B 517 ? 1.9815 1.6619 1.7311 -0.2937 -0.3648 0.1370 517 THR B CG2 11170 N N . GLY B 518 ? 1.8849 1.5539 1.7213 -0.2749 -0.4300 0.0608 518 GLY B N 11171 C CA . GLY B 518 ? 1.7677 1.4347 1.6653 -0.2652 -0.4127 0.0152 518 GLY B CA 11172 C C . GLY B 518 ? 1.7341 1.4117 1.6193 -0.2641 -0.4357 -0.0108 518 GLY B C 11173 O O . GLY B 518 ? 1.7956 1.4842 1.6212 -0.2688 -0.4630 0.0064 518 GLY B O 11174 N N . LYS B 519 ? 1.6773 1.3545 1.6176 -0.2594 -0.4254 -0.0520 519 LYS B N 11175 C CA . LYS B 519 ? 1.7055 1.3915 1.6537 -0.2577 -0.4554 -0.0802 519 LYS B CA 11176 C C . LYS B 519 ? 1.7043 1.3865 1.7077 -0.2539 -0.5050 -0.0785 519 LYS B C 11177 O O . LYS B 519 ? 1.7473 1.4344 1.7282 -0.2525 -0.5494 -0.0753 519 LYS B O 11178 C CB . LYS B 519 ? 1.6896 1.3759 1.6796 -0.2577 -0.4272 -0.1242 519 LYS B CB 11179 C CG . LYS B 519 ? 1.6630 1.3594 1.6680 -0.2564 -0.4583 -0.1580 519 LYS B CG 11180 C CD . LYS B 519 ? 1.6078 1.3001 1.6535 -0.2607 -0.4300 -0.1979 519 LYS B CD 11181 C CE . LYS B 519 ? 1.6508 1.3539 1.7117 -0.2596 -0.4623 -0.2339 519 LYS B CE 11182 N NZ . LYS B 519 ? 1.7474 1.4417 1.8480 -0.2671 -0.4374 -0.2707 519 LYS B NZ 11183 N N . TYR B 520 ? 1.6678 1.3440 1.7445 -0.2508 -0.4986 -0.0833 520 TYR B N 11184 C CA . TYR B 520 ? 1.6832 1.3568 1.8237 -0.2436 -0.5461 -0.0856 520 TYR B CA 11185 C C . TYR B 520 ? 1.7280 1.3828 1.8517 -0.2428 -0.5663 -0.0408 520 TYR B C 11186 O O . TYR B 520 ? 1.7341 1.3798 1.9111 -0.2349 -0.6095 -0.0383 520 TYR B O 11187 C CB . TYR B 520 ? 1.4972 1.1856 1.7373 -0.2399 -0.5297 -0.1259 520 TYR B CB 11188 C CG . TYR B 520 ? 1.6299 1.3341 1.8915 -0.2465 -0.5034 -0.1664 520 TYR B CG 11189 C CD1 . TYR B 520 ? 1.6381 1.3569 1.9600 -0.2523 -0.4626 -0.1924 520 TYR B CD1 11190 C CD2 . TYR B 520 ? 1.7610 1.4667 1.9830 -0.2484 -0.5209 -0.1781 520 TYR B CD2 11191 C CE1 . TYR B 520 ? 1.5826 1.3111 1.9258 -0.2629 -0.4406 -0.2248 520 TYR B CE1 11192 C CE2 . TYR B 520 ? 1.6796 1.3952 1.9269 -0.2555 -0.5005 -0.2157 520 TYR B CE2 11193 C CZ . TYR B 520 ? 1.5253 1.2494 1.8340 -0.2642 -0.4607 -0.2369 520 TYR B CZ 11194 O OH . TYR B 520 ? 1.4524 1.1820 1.7879 -0.2757 -0.4423 -0.2699 520 TYR B OH 11195 N N . CYS B 521 ? 1.8165 1.4660 1.8704 -0.2510 -0.5364 -0.0081 521 CYS B N 11196 C CA . CYS B 521 ? 1.8632 1.4951 1.8982 -0.2548 -0.5479 0.0368 521 CYS B CA 11197 C C . CYS B 521 ? 1.8497 1.4762 1.9673 -0.2457 -0.5384 0.0249 521 CYS B C 11198 O O . CYS B 521 ? 1.7977 1.4062 1.9475 -0.2417 -0.5764 0.0446 521 CYS B O 11199 C CB . CYS B 521 ? 1.8469 1.4622 1.8576 -0.2581 -0.6127 0.0705 521 CYS B CB 11200 S SG . CYS B 521 ? 2.2678 1.8787 2.1667 -0.2790 -0.6165 0.1351 521 CYS B SG 11201 N N . GLU B 522 ? 1.8245 1.4671 1.9755 -0.2425 -0.4894 -0.0076 522 GLU B N 11202 C CA . GLU B 522 ? 1.7363 1.3855 1.9627 -0.2339 -0.4742 -0.0247 522 GLU B CA 11203 C C . GLU B 522 ? 1.6897 1.3308 1.8861 -0.2361 -0.4428 0.0029 522 GLU B C 11204 O O . GLU B 522 ? 1.6211 1.2671 1.8726 -0.2278 -0.4350 -0.0059 522 GLU B O 11205 C CB . GLU B 522 ? 1.7833 1.4580 2.0590 -0.2330 -0.4369 -0.0701 522 GLU B CB 11206 C CG . GLU B 522 ? 1.8727 1.5484 2.0943 -0.2417 -0.3815 -0.0709 522 GLU B CG 11207 C CD . GLU B 522 ? 1.8960 1.5674 2.0606 -0.2483 -0.3868 -0.0733 522 GLU B CD 11208 O OE1 . GLU B 522 ? 2.0157 1.6859 2.1782 -0.2472 -0.4318 -0.0729 522 GLU B OE1 11209 O OE2 . GLU B 522 ? 1.7555 1.4246 1.8782 -0.2531 -0.3486 -0.0777 522 GLU B OE2 11210 N N . CYS B 523 ? 1.7758 1.4103 1.8875 -0.2464 -0.4251 0.0324 523 CYS B N 11211 C CA . CYS B 523 ? 1.8149 1.4456 1.8952 -0.2494 -0.3953 0.0576 523 CYS B CA 11212 C C . CYS B 523 ? 1.9601 1.5719 2.0207 -0.2569 -0.4341 0.1023 523 CYS B C 11213 O O . CYS B 523 ? 2.0426 1.6504 2.0406 -0.2694 -0.4558 0.1317 523 CYS B O 11214 C CB . CYS B 523 ? 1.8694 1.5099 1.8746 -0.2560 -0.3519 0.0600 523 CYS B CB 11215 S SG . CYS B 523 ? 1.9390 1.5900 1.9650 -0.2501 -0.3051 0.0149 523 CYS B SG 11216 N N . ASP B 524 ? 2.0187 1.6205 2.1333 -0.2502 -0.4438 0.1072 524 ASP B N 11217 C CA . ASP B 524 ? 1.9926 1.5692 2.1023 -0.2584 -0.4855 0.1500 524 ASP B CA 11218 C C . ASP B 524 ? 1.9761 1.5550 2.0165 -0.2748 -0.4576 0.1878 524 ASP B C 11219 O O . ASP B 524 ? 2.1023 1.6695 2.0928 -0.2934 -0.4846 0.2320 524 ASP B O 11220 C CB . ASP B 524 ? 1.8596 1.4253 2.0622 -0.2430 -0.5100 0.1347 524 ASP B CB 11221 C CG . ASP B 524 ? 1.7624 1.3534 2.0055 -0.2295 -0.4593 0.0980 524 ASP B CG 11222 O OD1 . ASP B 524 ? 1.7090 1.3124 1.9010 -0.2352 -0.4092 0.1030 524 ASP B OD1 11223 O OD2 . ASP B 524 ? 1.7514 1.3533 2.0775 -0.2126 -0.4707 0.0625 524 ASP B OD2 11224 N N . ASP B 525 ? 1.8239 1.4205 1.8622 -0.2688 -0.4044 0.1701 525 ASP B N 11225 C CA . ASP B 525 ? 1.8341 1.4406 1.8167 -0.2805 -0.3716 0.1957 525 ASP B CA 11226 C C . ASP B 525 ? 1.7735 1.3617 1.7820 -0.2877 -0.3945 0.2281 525 ASP B C 11227 O O . ASP B 525 ? 1.7530 1.3521 1.7363 -0.2947 -0.3655 0.2424 525 ASP B O 11228 C CB . ASP B 525 ? 1.9926 1.6145 1.8851 -0.2988 -0.3674 0.2193 525 ASP B CB 11229 C CG . ASP B 525 ? 1.9785 1.6220 1.8158 -0.3110 -0.3316 0.2399 525 ASP B CG 11230 O OD1 . ASP B 525 ? 1.9544 1.6185 1.7718 -0.3013 -0.2855 0.2132 525 ASP B OD1 11231 O OD2 . ASP B 525 ? 1.9362 1.5758 1.7517 -0.3311 -0.3513 0.2828 525 ASP B OD2 11232 N N . PHE B 526 ? 1.7720 1.3321 1.8365 -0.2850 -0.4484 0.2367 526 PHE B N 11233 C CA . PHE B 526 ? 1.6999 1.2370 1.8066 -0.2884 -0.4744 0.2599 526 PHE B CA 11234 C C . PHE B 526 ? 1.6393 1.1756 1.8436 -0.2610 -0.4801 0.2159 526 PHE B C 11235 O O . PHE B 526 ? 1.6042 1.1506 1.8348 -0.2528 -0.4537 0.2040 526 PHE B O 11236 C CB . PHE B 526 ? 1.7438 1.2443 1.8401 -0.3082 -0.5385 0.3096 526 PHE B CB 11237 C CG . PHE B 526 ? 1.8729 1.3561 1.9912 -0.3001 -0.5871 0.3000 526 PHE B CG 11238 C CD1 . PHE B 526 ? 1.8942 1.3512 2.1034 -0.2809 -0.6371 0.2802 526 PHE B CD1 11239 C CD2 . PHE B 526 ? 1.9140 1.4097 1.9642 -0.3106 -0.5868 0.3088 526 PHE B CD2 11240 C CE1 . PHE B 526 ? 1.8710 1.3147 2.1041 -0.2717 -0.6844 0.2684 526 PHE B CE1 11241 C CE2 . PHE B 526 ? 1.8935 1.3746 1.9647 -0.3022 -0.6336 0.2986 526 PHE B CE2 11242 C CZ . PHE B 526 ? 1.8790 1.3336 2.0421 -0.2829 -0.6826 0.2789 526 PHE B CZ 11243 N N . SER B 527 ? 1.7014 1.2313 1.9601 -0.2464 -0.5150 0.1893 527 SER B N 11244 C CA . SER B 527 ? 1.7090 1.2514 2.0627 -0.2201 -0.5197 0.1406 527 SER B CA 11245 C C . SER B 527 ? 1.5679 1.1506 1.9185 -0.2095 -0.4527 0.1037 527 SER B C 11246 O O . SER B 527 ? 1.5469 1.1476 1.8548 -0.2132 -0.4179 0.0920 527 SER B O 11247 C CB . SER B 527 ? 1.8303 1.3711 2.2371 -0.2074 -0.5624 0.1129 527 SER B CB 11248 O OG . SER B 527 ? 1.8615 1.4274 2.3622 -0.1823 -0.5638 0.0603 527 SER B OG 11249 N N . CYS B 528 ? 1.5967 1.1916 1.9932 -0.1963 -0.4379 0.0857 528 CYS B N 11250 C CA . CYS B 528 ? 1.6136 1.2435 2.0008 -0.1874 -0.3766 0.0574 528 CYS B CA 11251 C C . CYS B 528 ? 1.7430 1.3939 2.2097 -0.1659 -0.3777 0.0227 528 CYS B C 11252 O O . CYS B 528 ? 1.9334 1.5736 2.4704 -0.1553 -0.4273 0.0129 528 CYS B O 11253 C CB . CYS B 528 ? 1.5317 1.1584 1.8375 -0.2018 -0.3375 0.0889 528 CYS B CB 11254 S SG . CYS B 528 ? 1.8404 1.4930 2.0861 -0.2014 -0.2709 0.0699 528 CYS B SG 11255 N N . VAL B 529 ? 1.6236 1.3049 2.0792 -0.1582 -0.3257 0.0025 529 VAL B N 11256 C CA . VAL B 529 ? 1.4809 1.1912 2.0038 -0.1372 -0.3212 -0.0329 529 VAL B CA 11257 C C . VAL B 529 ? 1.4548 1.1486 1.9708 -0.1374 -0.3249 -0.0104 529 VAL B C 11258 O O . VAL B 529 ? 1.4795 1.1597 1.9251 -0.1520 -0.2997 0.0225 529 VAL B O 11259 C CB . VAL B 529 ? 1.3098 1.0652 1.8247 -0.1293 -0.2648 -0.0664 529 VAL B CB 11260 C CG1 . VAL B 529 ? 1.3867 1.1328 1.8124 -0.1411 -0.2168 -0.0408 529 VAL B CG1 11261 C CG2 . VAL B 529 ? 1.0848 0.8798 1.6658 -0.1072 -0.2600 -0.1052 529 VAL B CG2 11262 N N . ARG B 530 ? 1.4795 1.1773 2.0738 -0.1208 -0.3586 -0.0314 530 ARG B N 11263 C CA . ARG B 530 ? 1.4084 1.0907 2.0105 -0.1206 -0.3677 -0.0144 530 ARG B CA 11264 C C . ARG B 530 ? 1.3421 1.0676 1.9978 -0.0947 -0.3484 -0.0610 530 ARG B C 11265 O O . ARG B 530 ? 1.3726 1.1367 2.0856 -0.0754 -0.3499 -0.1078 530 ARG B O 11266 C CB . ARG B 530 ? 1.4282 1.0645 2.0757 -0.1271 -0.4368 0.0100 530 ARG B CB 11267 C CG . ARG B 530 ? 1.4469 1.0433 2.0419 -0.1527 -0.4621 0.0568 530 ARG B CG 11268 C CD . ARG B 530 ? 1.4593 1.0033 2.0878 -0.1641 -0.5306 0.0922 530 ARG B CD 11269 N NE . ARG B 530 ? 1.6164 1.1549 2.3489 -0.1391 -0.5857 0.0540 530 ARG B NE 11270 C CZ . ARG B 530 ? 1.8083 1.3462 2.6176 -0.1215 -0.6107 0.0300 530 ARG B CZ 11271 N NH1 . ARG B 530 ? 1.7694 1.3108 2.5619 -0.1276 -0.5847 0.0427 530 ARG B NH1 11272 N NH2 . ARG B 530 ? 1.9528 1.4894 2.8596 -0.0961 -0.6639 -0.0107 530 ARG B NH2 11273 N N . TYR B 531 ? 1.3391 1.0645 1.9768 -0.0945 -0.3301 -0.0501 531 TYR B N 11274 C CA . TYR B 531 ? 1.4454 1.2133 2.1278 -0.0692 -0.3126 -0.0935 531 TYR B CA 11275 C C . TYR B 531 ? 1.6074 1.3605 2.3714 -0.0575 -0.3646 -0.1040 531 TYR B C 11276 O O . TYR B 531 ? 1.6999 1.4713 2.5480 -0.0362 -0.3991 -0.1458 531 TYR B O 11277 C CB . TYR B 531 ? 1.3144 1.0969 1.9264 -0.0720 -0.2571 -0.0824 531 TYR B CB 11278 C CG . TYR B 531 ? 1.2096 1.0298 1.8590 -0.0478 -0.2436 -0.1185 531 TYR B CG 11279 C CD1 . TYR B 531 ? 1.2529 1.1259 1.9503 -0.0239 -0.2339 -0.1706 531 TYR B CD1 11280 C CD2 . TYR B 531 ? 1.2104 1.0198 1.8463 -0.0497 -0.2395 -0.1023 531 TYR B CD2 11281 C CE1 . TYR B 531 ? 1.3361 1.2493 2.0639 -0.0007 -0.2221 -0.2055 531 TYR B CE1 11282 C CE2 . TYR B 531 ? 1.2958 1.1412 1.9656 -0.0260 -0.2291 -0.1376 531 TYR B CE2 11283 C CZ . TYR B 531 ? 1.3374 1.2343 2.0511 -0.0007 -0.2209 -0.1891 531 TYR B CZ 11284 O OH . TYR B 531 ? 1.2399 1.1782 1.9842 0.0239 -0.2112 -0.2262 531 TYR B OH 11285 N N . LYS B 532 ? 1.5035 1.2256 2.2472 -0.0716 -0.3718 -0.0686 532 LYS B N 11286 C CA . LYS B 532 ? 1.3362 1.0299 2.1555 -0.0678 -0.4285 -0.0681 532 LYS B CA 11287 C C . LYS B 532 ? 1.3470 0.9793 2.1345 -0.1027 -0.4618 -0.0032 532 LYS B C 11288 O O . LYS B 532 ? 1.3370 0.9614 2.0621 -0.1250 -0.4346 0.0347 532 LYS B O 11289 C CB . LYS B 532 ? 1.2141 0.9350 2.0577 -0.0516 -0.4111 -0.0924 532 LYS B CB 11290 C CG . LYS B 532 ? 1.1481 0.9348 2.0269 -0.0168 -0.3835 -0.1573 532 LYS B CG 11291 C CD . LYS B 532 ? 1.1832 0.9843 2.1739 0.0103 -0.4365 -0.2083 532 LYS B CD 11292 C CE . LYS B 532 ? 1.3294 1.1062 2.3876 0.0170 -0.4812 -0.2124 532 LYS B CE 11293 N NZ . LYS B 532 ? 1.3776 1.1729 2.5518 0.0491 -0.5350 -0.2716 532 LYS B NZ 11294 N N . GLY B 533 ? 1.4433 1.0357 2.2731 -0.1079 -0.5214 0.0092 533 GLY B N 11295 C CA . GLY B 533 ? 1.6066 1.1384 2.4173 -0.1416 -0.5640 0.0721 533 GLY B CA 11296 C C . GLY B 533 ? 1.6389 1.1604 2.3419 -0.1756 -0.5333 0.1263 533 GLY B C 11297 O O . GLY B 533 ? 1.8751 1.3523 2.5524 -0.2068 -0.5677 0.1813 533 GLY B O 11298 N N . GLU B 534 ? 1.4015 0.9646 2.0414 -0.1703 -0.4708 0.1106 534 GLU B N 11299 C CA . GLU B 534 ? 1.4038 0.9663 1.9424 -0.1984 -0.4365 0.1529 534 GLU B CA 11300 C C . GLU B 534 ? 1.5269 1.1174 2.0235 -0.1877 -0.3981 0.1287 534 GLU B C 11301 O O . GLU B 534 ? 1.5689 1.1927 2.0967 -0.1610 -0.3746 0.0804 534 GLU B O 11302 C CB . GLU B 534 ? 1.4070 0.9892 1.8982 -0.2106 -0.3928 0.1688 534 GLU B CB 11303 C CG . GLU B 534 ? 1.5094 1.0629 2.0195 -0.2359 -0.4257 0.2092 534 GLU B CG 11304 C CD . GLU B 534 ? 1.4418 1.0248 1.9126 -0.2456 -0.3802 0.2168 534 GLU B CD 11305 O OE1 . GLU B 534 ? 1.4060 1.0235 1.8894 -0.2181 -0.3440 0.1738 534 GLU B OE1 11306 O OE2 . GLU B 534 ? 1.4128 0.9882 1.8395 -0.2814 -0.3808 0.2653 534 GLU B OE2 11307 N N . MET B 535 ? 1.6106 1.1900 2.0357 -0.2104 -0.3922 0.1628 535 MET B N 11308 C CA . MET B 535 ? 1.5517 1.1525 1.9336 -0.2043 -0.3584 0.1440 535 MET B CA 11309 C C . MET B 535 ? 1.3912 1.0249 1.7173 -0.1999 -0.2941 0.1318 535 MET B C 11310 O O . MET B 535 ? 1.3898 1.0259 1.6621 -0.2166 -0.2742 0.1597 535 MET B O 11311 C CB . MET B 535 ? 1.6313 1.2104 1.9574 -0.2284 -0.3782 0.1817 535 MET B CB 11312 C CG . MET B 535 ? 1.5432 1.1414 1.8264 -0.2240 -0.3472 0.1624 535 MET B CG 11313 S SD . MET B 535 ? 1.4203 1.0005 1.6292 -0.2518 -0.3682 0.2052 535 MET B SD 11314 C CE . MET B 535 ? 1.7273 1.3160 1.8623 -0.2788 -0.3433 0.2495 535 MET B CE 11315 N N . CYS B 536 ? 1.3273 0.9878 1.6681 -0.1781 -0.2636 0.0899 536 CYS B N 11316 C CA . CYS B 536 ? 1.3271 1.0134 1.6210 -0.1703 -0.2075 0.0755 536 CYS B CA 11317 C C . CYS B 536 ? 1.2978 0.9936 1.5970 -0.1653 -0.1945 0.0776 536 CYS B C 11318 O O . CYS B 536 ? 1.3318 1.0409 1.5780 -0.1657 -0.1560 0.0808 536 CYS B O 11319 C CB . CYS B 536 ? 1.3712 1.0536 1.5808 -0.1869 -0.1829 0.0972 536 CYS B CB 11320 S SG . CYS B 536 ? 1.2280 0.9050 1.4269 -0.1899 -0.1890 0.0864 536 CYS B SG 11321 N N . SER B 537 ? 1.3547 1.0432 1.7226 -0.1595 -0.2302 0.0733 537 SER B N 11322 C CA . SER B 537 ? 1.2831 0.9794 1.6712 -0.1550 -0.2265 0.0727 537 SER B CA 11323 C C . SER B 537 ? 1.2354 0.9234 1.5656 -0.1814 -0.2170 0.1149 537 SER B C 11324 O O . SER B 537 ? 1.2091 0.9129 1.5348 -0.1789 -0.1977 0.1128 537 SER B O 11325 C CB . SER B 537 ? 1.1819 0.9146 1.5691 -0.1290 -0.1839 0.0338 537 SER B CB 11326 O OG . SER B 537 ? 1.1139 0.8658 1.5440 -0.1089 -0.1848 -0.0045 537 SER B OG 11327 N N . GLY B 538 ? 1.3522 1.0213 1.6384 -0.2069 -0.2306 0.1509 538 GLY B N 11328 C CA . GLY B 538 ? 1.4479 1.1197 1.6755 -0.2357 -0.2209 0.1907 538 GLY B CA 11329 C C . GLY B 538 ? 1.3574 1.0610 1.5171 -0.2308 -0.1669 0.1796 538 GLY B C 11330 O O . GLY B 538 ? 1.3985 1.1164 1.5046 -0.2525 -0.1529 0.2049 538 GLY B O 11331 N N . HIS B 539 ? 1.3348 1.0514 1.4979 -0.2027 -0.1382 0.1408 539 HIS B N 11332 C CA . HIS B 539 ? 1.3673 1.1072 1.4746 -0.1925 -0.0919 0.1258 539 HIS B CA 11333 C C . HIS B 539 ? 1.4386 1.1751 1.4931 -0.1933 -0.0757 0.1219 539 HIS B C 11334 O O . HIS B 539 ? 1.4548 1.2034 1.4667 -0.1822 -0.0420 0.1063 539 HIS B O 11335 C CB . HIS B 539 ? 1.3189 1.0729 1.4562 -0.1626 -0.0711 0.0895 539 HIS B CB 11336 C CG . HIS B 539 ? 1.2830 1.0464 1.4665 -0.1585 -0.0817 0.0870 539 HIS B CG 11337 N ND1 . HIS B 539 ? 1.2842 1.0476 1.4676 -0.1824 -0.0963 0.1169 539 HIS B ND1 11338 C CD2 . HIS B 539 ? 1.2854 1.0615 1.5182 -0.1345 -0.0807 0.0574 539 HIS B CD2 11339 C CE1 . HIS B 539 ? 1.3014 1.0727 1.5360 -0.1733 -0.1050 0.1054 539 HIS B CE1 11340 N NE2 . HIS B 539 ? 1.3193 1.0991 1.5843 -0.1424 -0.0964 0.0675 539 HIS B NE2 11341 N N . GLY B 540 ? 1.4979 1.2159 1.5588 -0.2050 -0.1029 0.1340 540 GLY B N 11342 C CA . GLY B 540 ? 1.5826 1.2971 1.6002 -0.2064 -0.0916 0.1280 540 GLY B CA 11343 C C . GLY B 540 ? 1.6928 1.3931 1.6976 -0.2275 -0.1243 0.1533 540 GLY B C 11344 O O . GLY B 540 ? 1.7098 1.3945 1.7515 -0.2385 -0.1624 0.1736 540 GLY B O 11345 N N . GLN B 541 ? 1.7645 1.4684 1.7172 -0.2322 -0.1125 0.1510 541 GLN B N 11346 C CA . GLN B 541 ? 1.8402 1.5340 1.7740 -0.2499 -0.1425 0.1709 541 GLN B CA 11347 C C . GLN B 541 ? 1.8610 1.5366 1.8407 -0.2396 -0.1621 0.1512 541 GLN B C 11348 O O . GLN B 541 ? 1.9437 1.6197 1.9669 -0.2214 -0.1493 0.1233 541 GLN B O 11349 C CB . GLN B 541 ? 1.8420 1.5544 1.7024 -0.2577 -0.1228 0.1713 541 GLN B CB 11350 C CG . GLN B 541 ? 1.8674 1.6103 1.6823 -0.2682 -0.1016 0.1851 541 GLN B CG 11351 C CD . GLN B 541 ? 1.9105 1.6797 1.6586 -0.2709 -0.0823 0.1750 541 GLN B CD 11352 O OE1 . GLN B 541 ? 1.8949 1.6542 1.6314 -0.2631 -0.0835 0.1560 541 GLN B OE1 11353 N NE2 . GLN B 541 ? 1.9882 1.7951 1.6958 -0.2820 -0.0653 0.1844 541 GLN B NE2 11354 N N . CYS B 542 ? 1.7488 1.4136 1.7184 -0.2518 -0.1931 0.1647 542 CYS B N 11355 C CA . CYS B 542 ? 1.6658 1.3184 1.6813 -0.2429 -0.2141 0.1435 542 CYS B CA 11356 C C . CYS B 542 ? 1.6999 1.3535 1.6730 -0.2497 -0.2173 0.1396 542 CYS B C 11357 O O . CYS B 542 ? 1.7562 1.4079 1.6898 -0.2660 -0.2413 0.1663 542 CYS B O 11358 C CB . CYS B 542 ? 1.6871 1.3200 1.7599 -0.2460 -0.2650 0.1584 542 CYS B CB 11359 S SG . CYS B 542 ? 1.7235 1.3527 1.8761 -0.2289 -0.2901 0.1208 542 CYS B SG 11360 N N . SER B 543 ? 1.6707 1.3284 1.6516 -0.2386 -0.1938 0.1068 543 SER B N 11361 C CA . SER B 543 ? 1.5926 1.2502 1.5439 -0.2431 -0.1980 0.0963 543 SER B CA 11362 C C . SER B 543 ? 1.5109 1.1639 1.5222 -0.2367 -0.2126 0.0694 543 SER B C 11363 O O . SER B 543 ? 1.4646 1.1232 1.5083 -0.2276 -0.1867 0.0435 543 SER B O 11364 C CB . SER B 543 ? 1.6005 1.2665 1.5010 -0.2392 -0.1578 0.0808 543 SER B CB 11365 O OG . SER B 543 ? 1.6558 1.3357 1.5018 -0.2448 -0.1452 0.1003 543 SER B OG 11366 N N . CYS B 544 ? 1.6039 1.2501 1.6285 -0.2426 -0.2547 0.0760 544 CYS B N 11367 C CA . CYS B 544 ? 1.6455 1.2931 1.7293 -0.2373 -0.2737 0.0481 544 CYS B CA 11368 C C . CYS B 544 ? 1.5015 1.1593 1.6626 -0.2252 -0.2679 0.0256 544 CYS B C 11369 O O . CYS B 544 ? 1.4451 1.1183 1.6456 -0.2212 -0.2514 -0.0063 544 CYS B O 11370 C CB . CYS B 544 ? 1.6348 1.2882 1.6981 -0.2391 -0.2501 0.0228 544 CYS B CB 11371 S SG . CYS B 544 ? 2.1613 1.8198 2.2801 -0.2395 -0.2825 -0.0063 544 CYS B SG 11372 N N . GLY B 545 ? 1.4153 1.0682 1.5989 -0.2207 -0.2814 0.0413 545 GLY B N 11373 C CA . GLY B 545 ? 1.4513 1.1197 1.7098 -0.2066 -0.2800 0.0167 545 GLY B CA 11374 C C . GLY B 545 ? 1.4157 1.1009 1.6647 -0.2004 -0.2287 0.0046 545 GLY B C 11375 O O . GLY B 545 ? 1.4169 1.1236 1.7219 -0.1884 -0.2209 -0.0190 545 GLY B O 11376 N N . ASP B 546 ? 1.3633 1.0413 1.5415 -0.2070 -0.1957 0.0186 546 ASP B N 11377 C CA . ASP B 546 ? 1.3561 1.0442 1.5170 -0.2003 -0.1502 0.0102 546 ASP B CA 11378 C C . ASP B 546 ? 1.3533 1.0336 1.4690 -0.2004 -0.1414 0.0362 546 ASP B C 11379 O O . ASP B 546 ? 1.4127 1.0819 1.4885 -0.2112 -0.1588 0.0621 546 ASP B O 11380 C CB . ASP B 546 ? 1.4308 1.1167 1.5549 -0.2052 -0.1186 -0.0020 546 ASP B CB 11381 C CG . ASP B 546 ? 1.5470 1.2455 1.7195 -0.2089 -0.1228 -0.0285 546 ASP B CG 11382 O OD1 . ASP B 546 ? 1.7122 1.4011 1.8615 -0.2181 -0.1202 -0.0336 546 ASP B OD1 11383 O OD2 . ASP B 546 ? 1.5009 1.2231 1.7381 -0.2026 -0.1294 -0.0473 546 ASP B OD2 11384 N N . CYS B 547 ? 1.2987 0.9899 1.4208 -0.1895 -0.1140 0.0287 547 CYS B N 11385 C CA . CYS B 547 ? 1.2857 0.9751 1.3764 -0.1885 -0.1057 0.0485 547 CYS B CA 11386 C C . CYS B 547 ? 1.3209 1.0109 1.3509 -0.1854 -0.0664 0.0470 547 CYS B C 11387 O O . CYS B 547 ? 1.3146 1.0084 1.3454 -0.1761 -0.0390 0.0282 547 CYS B O 11388 C CB . CYS B 547 ? 1.2308 0.9328 1.3760 -0.1756 -0.1096 0.0394 547 CYS B CB 11389 S SG . CYS B 547 ? 1.7602 1.4562 1.9816 -0.1759 -0.1651 0.0416 547 CYS B SG 11390 N N . LEU B 548 ? 1.3679 1.0560 1.3455 -0.1937 -0.0657 0.0668 548 LEU B N 11391 C CA . LEU B 548 ? 1.4277 1.1198 1.3524 -0.1874 -0.0335 0.0621 548 LEU B CA 11392 C C . LEU B 548 ? 1.4205 1.1265 1.3433 -0.1829 -0.0252 0.0717 548 LEU B C 11393 O O . LEU B 548 ? 1.4164 1.1309 1.3270 -0.1961 -0.0398 0.0941 548 LEU B O 11394 C CB . LEU B 548 ? 1.5033 1.1956 1.3723 -0.1978 -0.0358 0.0681 548 LEU B CB 11395 C CG . LEU B 548 ? 1.4939 1.1730 1.3656 -0.2031 -0.0477 0.0571 548 LEU B CG 11396 C CD1 . LEU B 548 ? 1.5761 1.2612 1.3911 -0.2104 -0.0504 0.0583 548 LEU B CD1 11397 C CD2 . LEU B 548 ? 1.3992 1.0657 1.2894 -0.1930 -0.0266 0.0335 548 LEU B CD2 11398 N N . CYS B 549 ? 1.3958 1.1056 1.3297 -0.1658 -0.0022 0.0557 549 CYS B N 11399 C CA . CYS B 549 ? 1.3845 1.1090 1.3313 -0.1586 0.0030 0.0593 549 CYS B CA 11400 C C . CYS B 549 ? 1.4459 1.1841 1.3421 -0.1594 0.0194 0.0650 549 CYS B C 11401 O O . CYS B 549 ? 1.4483 1.1840 1.3005 -0.1535 0.0371 0.0541 549 CYS B O 11402 C CB . CYS B 549 ? 1.3357 1.0646 1.3097 -0.1384 0.0208 0.0377 549 CYS B CB 11403 S SG . CYS B 549 ? 1.4099 1.1418 1.4533 -0.1356 0.0043 0.0230 549 CYS B SG 11404 N N . ASP B 550 ? 1.4464 1.2011 1.3540 -0.1671 0.0115 0.0800 550 ASP B N 11405 C CA . ASP B 550 ? 1.4540 1.2335 1.3238 -0.1683 0.0285 0.0819 550 ASP B CA 11406 C C . ASP B 550 ? 1.3667 1.1504 1.2315 -0.1419 0.0544 0.0566 550 ASP B C 11407 O O . ASP B 550 ? 1.3700 1.1412 1.2643 -0.1262 0.0574 0.0436 550 ASP B O 11408 C CB . ASP B 550 ? 1.4514 1.2483 1.3420 -0.1875 0.0127 0.1065 550 ASP B CB 11409 C CG . ASP B 550 ? 1.4739 1.2635 1.3623 -0.2158 -0.0166 0.1376 550 ASP B CG 11410 O OD1 . ASP B 550 ? 1.5576 1.3437 1.4086 -0.2221 -0.0179 0.1389 550 ASP B OD1 11411 O OD2 . ASP B 550 ? 1.4431 1.2282 1.3675 -0.2315 -0.0413 0.1609 550 ASP B OD2 11412 N N . SER B 551 ? 1.3362 1.1415 1.1627 -0.1366 0.0718 0.0484 551 SER B N 11413 C CA . SER B 551 ? 1.3022 1.1093 1.1171 -0.1097 0.0928 0.0241 551 SER B CA 11414 C C . SER B 551 ? 1.2858 1.0967 1.1447 -0.0968 0.0926 0.0191 551 SER B C 11415 O O . SER B 551 ? 1.3558 1.1803 1.2515 -0.1095 0.0788 0.0324 551 SER B O 11416 C CB . SER B 551 ? 1.3009 1.1412 1.0796 -0.1072 0.1059 0.0143 551 SER B CB 11417 O OG . SER B 551 ? 1.4308 1.2744 1.1692 -0.1159 0.1057 0.0125 551 SER B OG 11418 N N . ASP B 552 ? 1.2879 1.0855 1.1422 -0.0723 0.1057 0.0003 552 ASP B N 11419 C CA . ASP B 552 ? 1.2647 1.0696 1.1549 -0.0556 0.1071 -0.0103 552 ASP B CA 11420 C C . ASP B 552 ? 1.2775 1.0780 1.2202 -0.0638 0.0901 -0.0045 552 ASP B C 11421 O O . ASP B 552 ? 1.2634 1.0791 1.2494 -0.0557 0.0830 -0.0121 552 ASP B O 11422 C CB . ASP B 552 ? 1.3180 1.1543 1.2221 -0.0519 0.1081 -0.0143 552 ASP B CB 11423 C CG . ASP B 552 ? 1.4796 1.3293 1.3393 -0.0402 0.1239 -0.0273 552 ASP B CG 11424 O OD1 . ASP B 552 ? 1.3830 1.2510 1.2229 -0.0571 0.1240 -0.0197 552 ASP B OD1 11425 O OD2 . ASP B 552 ? 1.7177 1.5623 1.5620 -0.0135 0.1346 -0.0465 552 ASP B OD2 11426 N N . TRP B 553 ? 1.3188 1.1009 1.2613 -0.0779 0.0816 0.0046 553 TRP B N 11427 C CA . TRP B 553 ? 1.3486 1.1289 1.3431 -0.0826 0.0643 0.0038 553 TRP B CA 11428 C C . TRP B 553 ? 1.3897 1.1529 1.3731 -0.0856 0.0699 -0.0003 553 TRP B C 11429 O O . TRP B 553 ? 1.4877 1.2338 1.4325 -0.0955 0.0733 0.0076 553 TRP B O 11430 C CB . TRP B 553 ? 1.3079 1.0876 1.3339 -0.1039 0.0351 0.0238 553 TRP B CB 11431 C CG . TRP B 553 ? 1.2712 1.0671 1.3215 -0.1059 0.0259 0.0298 553 TRP B CG 11432 C CD1 . TRP B 553 ? 1.4496 1.2564 1.4730 -0.1201 0.0283 0.0464 553 TRP B CD1 11433 C CD2 . TRP B 553 ? 1.2255 1.0332 1.3358 -0.0945 0.0125 0.0170 553 TRP B CD2 11434 N NE1 . TRP B 553 ? 1.4068 1.2283 1.4704 -0.1211 0.0176 0.0480 553 TRP B NE1 11435 C CE2 . TRP B 553 ? 1.2129 1.0324 1.3312 -0.1041 0.0062 0.0292 553 TRP B CE2 11436 C CE3 . TRP B 553 ? 1.2542 1.0690 1.4145 -0.0773 0.0051 -0.0065 553 TRP B CE3 11437 C CZ2 . TRP B 553 ? 1.1671 0.9980 1.3440 -0.0967 -0.0099 0.0192 553 TRP B CZ2 11438 C CZ3 . TRP B 553 ? 1.1602 0.9903 1.3771 -0.0671 -0.0109 -0.0197 553 TRP B CZ3 11439 C CH2 . TRP B 553 ? 1.1429 0.9772 1.3689 -0.0765 -0.0196 -0.0065 553 TRP B CH2 11440 N N . THR B 554 ? 1.2791 1.0521 1.2988 -0.0775 0.0710 -0.0151 554 THR B N 11441 C CA . THR B 554 ? 1.2529 1.0174 1.2704 -0.0838 0.0775 -0.0200 554 THR B CA 11442 C C . THR B 554 ? 1.1930 0.9785 1.2762 -0.0856 0.0608 -0.0332 554 THR B C 11443 O O . THR B 554 ? 1.3441 1.1458 1.4746 -0.0796 0.0417 -0.0393 554 THR B O 11444 C CB . THR B 554 ? 1.2543 1.0156 1.2357 -0.0723 0.1055 -0.0283 554 THR B CB 11445 O OG1 . THR B 554 ? 1.2336 1.0218 1.2337 -0.0537 0.1125 -0.0424 554 THR B OG1 11446 C CG2 . THR B 554 ? 1.2876 1.0218 1.2067 -0.0693 0.1170 -0.0194 554 THR B CG2 11447 N N . GLY B 555 ? 1.1754 0.9623 1.2659 -0.0938 0.0664 -0.0401 555 GLY B N 11448 C CA . GLY B 555 ? 1.1833 0.9986 1.3392 -0.0942 0.0521 -0.0594 555 GLY B CA 11449 C C . GLY B 555 ? 1.1658 0.9685 1.3492 -0.1093 0.0235 -0.0535 555 GLY B C 11450 O O . GLY B 555 ? 1.1388 0.9129 1.2934 -0.1195 0.0102 -0.0318 555 GLY B O 11451 N N . TYR B 556 ? 1.1382 0.9673 1.3773 -0.1103 0.0134 -0.0751 556 TYR B N 11452 C CA . TYR B 556 ? 1.1343 0.9548 1.4079 -0.1214 -0.0181 -0.0746 556 TYR B CA 11453 C C . TYR B 556 ? 1.1184 0.9247 1.4240 -0.1182 -0.0583 -0.0640 556 TYR B C 11454 O O . TYR B 556 ? 1.1242 0.9028 1.4197 -0.1308 -0.0840 -0.0437 556 TYR B O 11455 C CB . TYR B 556 ? 1.1370 0.9988 1.4712 -0.1205 -0.0192 -0.1069 556 TYR B CB 11456 C CG . TYR B 556 ? 1.1978 1.0543 1.5734 -0.1294 -0.0536 -0.1119 556 TYR B CG 11457 C CD1 . TYR B 556 ? 1.2298 1.1005 1.6783 -0.1185 -0.0941 -0.1296 556 TYR B CD1 11458 C CD2 . TYR B 556 ? 1.2591 1.0952 1.6039 -0.1469 -0.0492 -0.1012 556 TYR B CD2 11459 C CE1 . TYR B 556 ? 1.2796 1.1434 1.7664 -0.1243 -0.1299 -0.1350 556 TYR B CE1 11460 C CE2 . TYR B 556 ? 1.2391 1.0721 1.6216 -0.1534 -0.0827 -0.1076 556 TYR B CE2 11461 C CZ . TYR B 556 ? 1.2663 1.1130 1.7185 -0.1418 -0.1232 -0.1237 556 TYR B CZ 11462 O OH . TYR B 556 ? 1.3152 1.1566 1.8053 -0.1460 -0.1608 -0.1306 556 TYR B OH 11463 N N . TYR B 557 ? 1.1134 0.9385 1.4569 -0.1024 -0.0654 -0.0771 557 TYR B N 11464 C CA . TYR B 557 ? 1.1304 0.9384 1.5089 -0.1008 -0.1051 -0.0656 557 TYR B CA 11465 C C . TYR B 557 ? 1.2175 1.0029 1.5419 -0.1066 -0.0948 -0.0355 557 TYR B C 11466 O O . TYR B 557 ? 1.3255 1.0939 1.6680 -0.1118 -0.1240 -0.0176 557 TYR B O 11467 C CB . TYR B 557 ? 1.1949 1.0358 1.6526 -0.0799 -0.1233 -0.1001 557 TYR B CB 11468 C CG . TYR B 557 ? 1.2459 1.1164 1.7720 -0.0730 -0.1428 -0.1347 557 TYR B CG 11469 C CD1 . TYR B 557 ? 1.2165 1.0742 1.8095 -0.0698 -0.1960 -0.1408 557 TYR B CD1 11470 C CD2 . TYR B 557 ? 1.2883 1.2011 1.8141 -0.0708 -0.1095 -0.1615 557 TYR B CD2 11471 C CE1 . TYR B 557 ? 1.2931 1.1829 1.9545 -0.0606 -0.2162 -0.1784 557 TYR B CE1 11472 C CE2 . TYR B 557 ? 1.2214 1.1719 1.8139 -0.0657 -0.1253 -0.1972 557 TYR B CE2 11473 C CZ . TYR B 557 ? 1.3032 1.2439 1.9654 -0.0587 -0.1789 -0.2084 557 TYR B CZ 11474 O OH . TYR B 557 ? 1.3812 1.3642 2.1155 -0.0507 -0.1969 -0.2496 557 TYR B OH 11475 N N . CYS B 558 ? 1.1941 0.9808 1.4552 -0.1064 -0.0547 -0.0309 558 CYS B N 11476 C CA . CYS B 558 ? 1.2062 0.9810 1.4151 -0.1091 -0.0398 -0.0099 558 CYS B CA 11477 C C . CYS B 558 ? 1.2132 1.0023 1.4562 -0.0962 -0.0465 -0.0175 558 CYS B C 11478 O O . CYS B 558 ? 1.2421 1.0229 1.4639 -0.1032 -0.0485 0.0022 558 CYS B O 11479 C CB . CYS B 558 ? 1.2209 0.9697 1.3964 -0.1310 -0.0578 0.0232 558 CYS B CB 11480 S SG . CYS B 558 ? 1.9863 1.7191 2.1074 -0.1445 -0.0464 0.0306 558 CYS B SG 11481 N N . ASN B 559 ? 1.2127 1.0288 1.5108 -0.0779 -0.0500 -0.0485 559 ASN B N 11482 C CA . ASN B 559 ? 1.2375 1.0708 1.5736 -0.0622 -0.0576 -0.0627 559 ASN B CA 11483 C C . ASN B 559 ? 1.2226 1.0805 1.5250 -0.0439 -0.0200 -0.0795 559 ASN B C 11484 O O . ASN B 559 ? 1.2378 1.1155 1.5684 -0.0277 -0.0228 -0.0963 559 ASN B O 11485 C CB . ASN B 559 ? 1.2668 1.1193 1.6913 -0.0496 -0.0912 -0.0921 559 ASN B CB 11486 C CG . ASN B 559 ? 1.3262 1.2169 1.7703 -0.0365 -0.0744 -0.1271 559 ASN B CG 11487 O OD1 . ASN B 559 ? 1.3431 1.2397 1.7336 -0.0406 -0.0389 -0.1241 559 ASN B OD1 11488 N ND2 . ASN B 559 ? 1.3751 1.2943 1.8994 -0.0217 -0.1016 -0.1617 559 ASN B ND2 11489 N N . CYS B 560 ? 1.2098 1.0638 1.4527 -0.0464 0.0120 -0.0749 560 CYS B N 11490 C CA . CYS B 560 ? 1.2081 1.0783 1.4116 -0.0301 0.0447 -0.0863 560 CYS B CA 11491 C C . CYS B 560 ? 1.2566 1.1065 1.4029 -0.0310 0.0581 -0.0673 560 CYS B C 11492 O O . CYS B 560 ? 1.4327 1.2570 1.5459 -0.0478 0.0558 -0.0445 560 CYS B O 11493 C CB . CYS B 560 ? 1.1363 1.0107 1.3093 -0.0333 0.0693 -0.0909 560 CYS B CB 11494 S SG . CYS B 560 ? 1.4119 1.3036 1.5356 -0.0150 0.1047 -0.1009 560 CYS B SG 11495 N N . THR B 561 ? 1.2391 1.1062 1.3750 -0.0114 0.0713 -0.0802 561 THR B N 11496 C CA . THR B 561 ? 1.2503 1.1077 1.3448 -0.0086 0.0807 -0.0696 561 THR B CA 11497 C C . THR B 561 ? 1.2533 1.1039 1.2854 0.0056 0.1083 -0.0729 561 THR B C 11498 O O . THR B 561 ? 1.2436 1.1072 1.2709 0.0189 0.1205 -0.0865 561 THR B O 11499 C CB . THR B 561 ? 1.2253 1.1053 1.3619 0.0030 0.0680 -0.0818 561 THR B CB 11500 O OG1 . THR B 561 ? 1.3991 1.2841 1.6051 -0.0052 0.0377 -0.0844 561 THR B OG1 11501 C CG2 . THR B 561 ? 1.2248 1.0992 1.3341 -0.0046 0.0707 -0.0668 561 THR B CG2 11502 N N . THR B 562 ? 1.3065 1.1384 1.2912 0.0025 0.1161 -0.0609 562 THR B N 11503 C CA . THR B 562 ? 1.2823 1.1000 1.2093 0.0179 0.1353 -0.0641 562 THR B CA 11504 C C . THR B 562 ? 1.2181 1.0575 1.1451 0.0431 0.1395 -0.0811 562 THR B C 11505 O O . THR B 562 ? 1.1874 1.0188 1.0753 0.0615 0.1515 -0.0872 562 THR B O 11506 C CB . THR B 562 ? 1.4016 1.1956 1.2837 0.0087 0.1382 -0.0525 562 THR B CB 11507 O OG1 . THR B 562 ? 1.4130 1.1933 1.3024 -0.0156 0.1294 -0.0379 562 THR B OG1 11508 C CG2 . THR B 562 ? 1.5810 1.3478 1.4079 0.0231 0.1517 -0.0554 562 THR B CG2 11509 N N . ARG B 563 ? 1.1748 1.0395 1.1467 0.0431 0.1270 -0.0875 563 ARG B N 11510 C CA . ARG B 563 ? 1.1304 1.0192 1.1096 0.0655 0.1282 -0.1057 563 ARG B CA 11511 C C . ARG B 563 ? 1.1742 1.0781 1.1517 0.0907 0.1348 -0.1249 563 ARG B C 11512 O O . ARG B 563 ? 1.1677 1.0888 1.1826 0.0905 0.1294 -0.1336 563 ARG B O 11513 C CB . ARG B 563 ? 1.1167 1.0291 1.1568 0.0559 0.1101 -0.1081 563 ARG B CB 11514 C CG . ARG B 563 ? 1.1908 1.0978 1.2274 0.0294 0.1047 -0.0871 563 ARG B CG 11515 C CD . ARG B 563 ? 1.1322 1.0540 1.2333 0.0125 0.0822 -0.0813 563 ARG B CD 11516 N NE . ARG B 563 ? 1.0810 1.0306 1.2193 0.0314 0.0777 -0.1044 563 ARG B NE 11517 C CZ . ARG B 563 ? 1.0684 1.0304 1.2713 0.0217 0.0555 -0.1054 563 ARG B CZ 11518 N NH1 . ARG B 563 ? 1.0789 1.0243 1.3134 -0.0069 0.0341 -0.0815 563 ARG B NH1 11519 N NH2 . ARG B 563 ? 1.0391 1.0275 1.2762 0.0409 0.0514 -0.1304 563 ARG B NH2 11520 N N . THR B 564 ? 1.2460 1.1465 1.1792 0.1130 0.1449 -0.1329 564 THR B N 11521 C CA . THR B 564 ? 1.1815 1.1003 1.1052 0.1383 0.1499 -0.1499 564 THR B CA 11522 C C . THR B 564 ? 1.1457 1.0995 1.1020 0.1602 0.1411 -0.1747 564 THR B C 11523 O O . THR B 564 ? 1.2364 1.2132 1.1891 0.1839 0.1424 -0.1930 564 THR B O 11524 C CB . THR B 564 ? 1.2024 1.0900 1.0530 0.1508 0.1620 -0.1410 564 THR B CB 11525 O OG1 . THR B 564 ? 1.3026 1.1737 1.1264 0.1601 0.1599 -0.1424 564 THR B OG1 11526 C CG2 . THR B 564 ? 1.1444 0.9987 0.9679 0.1283 0.1701 -0.1181 564 THR B CG2 11527 N N . ASP B 565 ? 1.1623 1.1235 1.1501 0.1505 0.1322 -0.1750 565 ASP B N 11528 C CA . ASP B 565 ? 1.2656 1.2586 1.2840 0.1682 0.1243 -0.1979 565 ASP B CA 11529 C C . ASP B 565 ? 1.2165 1.2435 1.2979 0.1779 0.1106 -0.2204 565 ASP B C 11530 O O . ASP B 565 ? 1.3222 1.3772 1.4151 0.2041 0.1067 -0.2465 565 ASP B O 11531 C CB . ASP B 565 ? 1.3756 1.3735 1.4152 0.1477 0.1196 -0.1894 565 ASP B CB 11532 C CG . ASP B 565 ? 1.3568 1.3524 1.4472 0.1155 0.1063 -0.1720 565 ASP B CG 11533 O OD1 . ASP B 565 ? 1.3960 1.3742 1.4893 0.1057 0.1039 -0.1613 565 ASP B OD1 11534 O OD2 . ASP B 565 ? 1.3143 1.3259 1.4427 0.0989 0.0967 -0.1684 565 ASP B OD2 11535 N N . THR B 566 ? 1.1416 1.1676 1.2665 0.1590 0.1004 -0.2139 566 THR B N 11536 C CA . THR B 566 ? 1.1725 1.2311 1.3657 0.1692 0.0828 -0.2401 566 THR B CA 11537 C C . THR B 566 ? 1.1532 1.2344 1.3256 0.1918 0.0927 -0.2593 566 THR B C 11538 O O . THR B 566 ? 1.1659 1.2851 1.3881 0.2078 0.0805 -0.2898 566 THR B O 11539 C CB . THR B 566 ? 0.9888 1.0372 1.2415 0.1430 0.0627 -0.2291 566 THR B CB 11540 O OG1 . THR B 566 ? 1.0042 1.0329 1.2279 0.1297 0.0724 -0.2121 566 THR B OG1 11541 C CG2 . THR B 566 ? 1.0056 1.0344 1.2730 0.1158 0.0530 -0.2046 566 THR B CG2 11542 N N . CYS B 567 ? 1.2125 1.2724 1.3119 0.1917 0.1138 -0.2415 567 CYS B N 11543 C CA . CYS B 567 ? 1.2794 1.3609 1.3456 0.2076 0.1268 -0.2520 567 CYS B CA 11544 C C . CYS B 567 ? 1.3472 1.4412 1.3698 0.2381 0.1320 -0.2653 567 CYS B C 11545 O O . CYS B 567 ? 1.4081 1.5272 1.4005 0.2541 0.1406 -0.2755 567 CYS B O 11546 C CB . CYS B 567 ? 1.2680 1.3165 1.2797 0.1875 0.1444 -0.2222 567 CYS B CB 11547 S SG . CYS B 567 ? 1.5780 1.6160 1.6381 0.1545 0.1372 -0.2097 567 CYS B SG 11548 N N . MET B 568 ? 1.2726 1.3530 1.2916 0.2454 0.1261 -0.2659 568 MET B N 11549 C CA . MET B 568 ? 1.2235 1.3116 1.2022 0.2760 0.1272 -0.2794 568 MET B CA 11550 C C . MET B 568 ? 1.2874 1.4293 1.3142 0.3023 0.1141 -0.3188 568 MET B C 11551 O O . MET B 568 ? 1.2779 1.4421 1.3806 0.2969 0.0986 -0.3366 568 MET B O 11552 C CB . MET B 568 ? 1.2876 1.3509 1.2528 0.2755 0.1250 -0.2724 568 MET B CB 11553 C CG . MET B 568 ? 1.4236 1.4607 1.3129 0.2969 0.1307 -0.2664 568 MET B CG 11554 S SD . MET B 568 ? 2.0914 2.0729 1.9071 0.2787 0.1452 -0.2279 568 MET B SD 11555 C CE . MET B 568 ? 1.2154 1.1704 1.0553 0.2441 0.1469 -0.2090 568 MET B CE 11556 N N . SER B 569 ? 1.3868 1.5479 1.3687 0.3306 0.1178 -0.3318 569 SER B N 11557 C CA . SER B 569 ? 1.2914 1.5088 1.3118 0.3595 0.1052 -0.3731 569 SER B CA 11558 C C . SER B 569 ? 1.2259 1.4502 1.2556 0.3834 0.0926 -0.3936 569 SER B C 11559 O O . SER B 569 ? 1.2272 1.4181 1.2422 0.3756 0.0939 -0.3778 569 SER B O 11560 C CB . SER B 569 ? 1.3328 1.5780 1.2980 0.3769 0.1154 -0.3780 569 SER B CB 11561 O OG . SER B 569 ? 1.3238 1.6294 1.3228 0.4077 0.1025 -0.4219 569 SER B OG 11562 N N . SER B 570 ? 1.2567 1.5278 1.3130 0.4086 0.0791 -0.4276 570 SER B N 11563 C CA . SER B 570 ? 1.2326 1.5088 1.3011 0.4178 0.0624 -0.4364 570 SER B CA 11564 C C . SER B 570 ? 1.2666 1.5163 1.2504 0.4361 0.0676 -0.4216 570 SER B C 11565 O O . SER B 570 ? 1.3051 1.5411 1.2881 0.4395 0.0602 -0.4212 570 SER B O 11566 C CB . SER B 570 ? 1.3392 1.6635 1.4538 0.4260 0.0413 -0.4631 570 SER B CB 11567 O OG . SER B 570 ? 1.3436 1.6882 1.5391 0.4113 0.0306 -0.4789 570 SER B OG 11568 N N . ASN B 571 ? 1.3769 1.6218 1.2902 0.4485 0.0791 -0.4110 571 ASN B N 11569 C CA . ASN B 571 ? 1.4645 1.6777 1.2905 0.4700 0.0802 -0.3961 571 ASN B CA 11570 C C . ASN B 571 ? 1.5148 1.6676 1.2981 0.4636 0.0913 -0.3719 571 ASN B C 11571 O O . ASN B 571 ? 1.6487 1.7663 1.3756 0.4812 0.0847 -0.3629 571 ASN B O 11572 C CB . ASN B 571 ? 1.5237 1.7518 1.2803 0.4845 0.0903 -0.3901 571 ASN B CB 11573 C CG . ASN B 571 ? 1.5679 1.8028 1.3303 0.4572 0.1105 -0.3757 571 ASN B CG 11574 O OD1 . ASN B 571 ? 1.7049 1.8887 1.4309 0.4301 0.1231 -0.3367 571 ASN B OD1 11575 N ND2 . ASN B 571 ? 1.3930 1.6904 1.2091 0.4586 0.1098 -0.4053 571 ASN B ND2 11576 N N . GLY B 572 ? 1.4421 1.5785 1.2588 0.4277 0.1021 -0.3533 572 GLY B N 11577 C CA . GLY B 572 ? 1.4243 1.5047 1.2130 0.4063 0.1089 -0.3227 572 GLY B CA 11578 C C . GLY B 572 ? 1.4148 1.4565 1.1526 0.3821 0.1235 -0.2848 572 GLY B C 11579 O O . GLY B 572 ? 1.5062 1.5055 1.2328 0.3588 0.1296 -0.2607 572 GLY B O 11580 N N . LEU B 573 ? 1.2332 1.2945 0.9411 0.3865 0.1295 -0.2810 573 LEU B N 11581 C CA . LEU B 573 ? 1.2659 1.3006 0.9310 0.3598 0.1452 -0.2461 573 LEU B CA 11582 C C . LEU B 573 ? 1.1502 1.2159 0.8790 0.3322 0.1545 -0.2507 573 LEU B C 11583 O O . LEU B 573 ? 1.1189 1.2415 0.9040 0.3414 0.1497 -0.2822 573 LEU B O 11584 C CB . LEU B 573 ? 1.3502 1.3977 0.9489 0.3730 0.1489 -0.2370 573 LEU B CB 11585 C CG . LEU B 573 ? 1.4085 1.4280 0.9531 0.3432 0.1657 -0.1967 573 LEU B CG 11586 C CD1 . LEU B 573 ? 1.4835 1.4204 0.9864 0.3293 0.1627 -0.1623 573 LEU B CD1 11587 C CD2 . LEU B 573 ? 1.3574 1.4012 0.8362 0.3549 0.1693 -0.1878 573 LEU B CD2 11588 N N . LEU B 574 ? 1.1675 1.1949 0.8905 0.3004 0.1643 -0.2222 574 LEU B N 11589 C CA . LEU B 574 ? 1.2681 1.3177 1.0528 0.2744 0.1689 -0.2257 574 LEU B CA 11590 C C . LEU B 574 ? 1.3479 1.4531 1.1433 0.2737 0.1777 -0.2389 574 LEU B C 11591 O O . LEU B 574 ? 1.5154 1.6212 1.2504 0.2711 0.1906 -0.2220 574 LEU B O 11592 C CB . LEU B 574 ? 1.3322 1.3293 1.1007 0.2422 0.1767 -0.1926 574 LEU B CB 11593 C CG . LEU B 574 ? 1.4768 1.4473 1.1888 0.2221 0.1921 -0.1616 574 LEU B CG 11594 C CD1 . LEU B 574 ? 1.3669 1.2975 1.0896 0.1903 0.1956 -0.1396 574 LEU B CD1 11595 C CD2 . LEU B 574 ? 1.7013 1.6310 1.3320 0.2369 0.1913 -0.1422 574 LEU B CD2 11596 N N . CYS B 575 ? 1.1827 1.3370 1.0569 0.2759 0.1689 -0.2707 575 CYS B N 11597 C CA . CYS B 575 ? 1.1526 1.3733 1.0548 0.2786 0.1740 -0.2955 575 CYS B CA 11598 C C . CYS B 575 ? 1.1629 1.4267 1.0183 0.3063 0.1784 -0.3111 575 CYS B C 11599 O O . CYS B 575 ? 1.4001 1.7182 1.2462 0.3047 0.1905 -0.3216 575 CYS B O 11600 C CB . CYS B 575 ? 1.2677 1.4832 1.1552 0.2466 0.1918 -0.2721 575 CYS B CB 11601 S SG . CYS B 575 ? 1.6247 1.7981 1.5686 0.2152 0.1840 -0.2572 575 CYS B SG 11602 N N . SER B 576 ? 1.0909 1.3350 0.9169 0.3313 0.1680 -0.3136 576 SER B N 11603 C CA . SER B 576 ? 1.1661 1.4465 0.9455 0.3617 0.1666 -0.3288 576 SER B CA 11604 C C . SER B 576 ? 1.2637 1.5396 0.9537 0.3498 0.1860 -0.2955 576 SER B C 11605 O O . SER B 576 ? 1.2483 1.5746 0.9019 0.3673 0.1892 -0.3079 576 SER B O 11606 C CB . SER B 576 ? 1.1536 1.5183 0.9997 0.3838 0.1567 -0.3822 576 SER B CB 11607 O OG . SER B 576 ? 1.1609 1.5254 1.0907 0.3931 0.1354 -0.4103 576 SER B OG 11608 N N . GLY B 577 ? 1.3598 1.5770 1.0145 0.3183 0.1981 -0.2525 577 GLY B N 11609 C CA . GLY B 577 ? 1.3955 1.6005 0.9697 0.2989 0.2158 -0.2145 577 GLY B CA 11610 C C . GLY B 577 ? 1.3400 1.6204 0.9323 0.2802 0.2355 -0.2260 577 GLY B C 11611 O O . GLY B 577 ? 1.4464 1.7273 0.9790 0.2561 0.2540 -0.1937 577 GLY B O 11612 N N . ARG B 578 ? 1.2751 1.6213 0.9533 0.2904 0.2300 -0.2733 578 ARG B N 11613 C CA . ARG B 578 ? 1.3111 1.7444 1.0197 0.2799 0.2452 -0.2982 578 ARG B CA 11614 C C . ARG B 578 ? 1.2935 1.7187 1.0545 0.2461 0.2533 -0.2916 578 ARG B C 11615 O O . ARG B 578 ? 1.3090 1.8078 1.1092 0.2364 0.2641 -0.3171 578 ARG B O 11616 C CB . ARG B 578 ? 1.2361 1.7508 1.0155 0.3141 0.2296 -0.3611 578 ARG B CB 11617 C CG . ARG B 578 ? 1.1494 1.6782 0.8908 0.3519 0.2170 -0.3767 578 ARG B CG 11618 C CD . ARG B 578 ? 1.1132 1.7306 0.9312 0.3840 0.2014 -0.4438 578 ARG B CD 11619 N NE . ARG B 578 ? 1.1325 1.7561 0.9285 0.4178 0.1828 -0.4590 578 ARG B NE 11620 C CZ . ARG B 578 ? 1.1899 1.8548 0.9198 0.4288 0.1872 -0.4563 578 ARG B CZ 11621 N NH1 . ARG B 578 ? 1.2349 1.9479 0.9076 0.4108 0.2150 -0.4418 578 ARG B NH1 11622 N NH2 . ARG B 578 ? 1.2057 1.8666 0.9266 0.4555 0.1636 -0.4664 578 ARG B NH2 11623 N N . GLY B 579 ? 1.2863 1.6275 1.0500 0.2298 0.2469 -0.2614 579 GLY B N 11624 C CA . GLY B 579 ? 1.3119 1.6400 1.1240 0.1997 0.2508 -0.2548 579 GLY B CA 11625 C C . GLY B 579 ? 1.4124 1.6453 1.2030 0.1806 0.2465 -0.2146 579 GLY B C 11626 O O . GLY B 579 ? 1.5631 1.7381 1.2970 0.1895 0.2421 -0.1902 579 GLY B O 11627 N N . LYS B 580 ? 1.3125 1.5328 1.1507 0.1563 0.2457 -0.2113 580 LYS B N 11628 C CA . LYS B 580 ? 1.3092 1.4482 1.1313 0.1367 0.2417 -0.1773 580 LYS B CA 11629 C C . LYS B 580 ? 1.1923 1.3206 1.0902 0.1362 0.2213 -0.1934 580 LYS B C 11630 O O . LYS B 580 ? 1.1287 1.3061 1.0970 0.1368 0.2132 -0.2232 580 LYS B O 11631 C CB . LYS B 580 ? 1.4575 1.5804 1.2499 0.1008 0.2605 -0.1475 580 LYS B CB 11632 C CG . LYS B 580 ? 1.6270 1.6686 1.4019 0.0810 0.2554 -0.1155 580 LYS B CG 11633 C CD . LYS B 580 ? 1.6644 1.6415 1.3789 0.0969 0.2476 -0.0948 580 LYS B CD 11634 C CE . LYS B 580 ? 1.6221 1.5272 1.3258 0.0806 0.2405 -0.0714 580 LYS B CE 11635 N NZ . LYS B 580 ? 1.5894 1.4382 1.2423 0.0996 0.2301 -0.0593 580 LYS B NZ 11636 N N . CYS B 581 ? 1.1610 1.2264 1.0439 0.1350 0.2112 -0.1741 581 CYS B N 11637 C CA . CYS B 581 ? 1.1012 1.1525 1.0445 0.1312 0.1917 -0.1817 581 CYS B CA 11638 C C . CYS B 581 ? 1.1136 1.1409 1.0757 0.1008 0.1915 -0.1650 581 CYS B C 11639 O O . CYS B 581 ? 1.1439 1.1255 1.0574 0.0835 0.2014 -0.1363 581 CYS B O 11640 C CB . CYS B 581 ? 1.1546 1.1620 1.0731 0.1420 0.1829 -0.1711 581 CYS B CB 11641 S SG . CYS B 581 ? 1.4648 1.4546 1.4444 0.1302 0.1613 -0.1713 581 CYS B SG 11642 N N . GLU B 582 ? 1.1082 1.1650 1.1439 0.0959 0.1765 -0.1850 582 GLU B N 11643 C CA . GLU B 582 ? 1.1480 1.1844 1.2093 0.0699 0.1706 -0.1727 582 GLU B CA 11644 C C . GLU B 582 ? 1.0564 1.0857 1.1830 0.0689 0.1414 -0.1807 582 GLU B C 11645 O O . GLU B 582 ? 1.0253 1.0937 1.2155 0.0827 0.1241 -0.2102 582 GLU B O 11646 C CB . GLU B 582 ? 1.1933 1.2768 1.2789 0.0591 0.1813 -0.1875 582 GLU B CB 11647 C CG . GLU B 582 ? 1.4176 1.4996 1.4355 0.0469 0.2104 -0.1681 582 GLU B CG 11648 C CD . GLU B 582 ? 1.5319 1.6648 1.5775 0.0286 0.2231 -0.1805 582 GLU B CD 11649 O OE1 . GLU B 582 ? 1.4489 1.6246 1.5696 0.0319 0.2078 -0.2115 582 GLU B OE1 11650 O OE2 . GLU B 582 ? 1.6594 1.7899 1.6540 0.0102 0.2467 -0.1599 582 GLU B OE2 11651 N N . CYS B 583 ? 1.0802 1.0598 1.1900 0.0520 0.1344 -0.1540 583 CYS B N 11652 C CA . CYS B 583 ? 1.0827 1.0482 1.2424 0.0440 0.1066 -0.1508 583 CYS B CA 11653 C C . CYS B 583 ? 1.0642 1.0440 1.2573 0.0613 0.0909 -0.1652 583 CYS B C 11654 O O . CYS B 583 ? 1.0578 1.0488 1.3186 0.0613 0.0637 -0.1776 583 CYS B O 11655 C CB . CYS B 583 ? 1.0771 1.0621 1.3018 0.0347 0.0880 -0.1647 583 CYS B CB 11656 S SG . CYS B 583 ? 1.3057 1.2669 1.5058 0.0077 0.0974 -0.1449 583 CYS B SG 11657 N N . GLY B 584 ? 1.0572 1.0348 1.2061 0.0760 0.1051 -0.1642 584 GLY B N 11658 C CA . GLY B 584 ? 1.0433 1.0336 1.2207 0.0905 0.0920 -0.1769 584 GLY B CA 11659 C C . GLY B 584 ? 1.0256 1.0646 1.2499 0.1156 0.0845 -0.2145 584 GLY B C 11660 O O . GLY B 584 ? 1.0718 1.1252 1.3205 0.1308 0.0741 -0.2298 584 GLY B O 11661 N N . SER B 585 ? 0.9982 1.0683 1.2375 0.1199 0.0896 -0.2325 585 SER B N 11662 C CA . SER B 585 ? 0.9740 1.1014 1.2568 0.1452 0.0836 -0.2741 585 SER B CA 11663 C C . SER B 585 ? 0.9685 1.1285 1.1972 0.1546 0.1128 -0.2811 585 SER B C 11664 O O . SER B 585 ? 0.9847 1.1406 1.1863 0.1371 0.1289 -0.2666 585 SER B O 11665 C CB . SER B 585 ? 1.1411 1.2926 1.5122 0.1432 0.0557 -0.2993 585 SER B CB 11666 O OG . SER B 585 ? 1.2096 1.3291 1.6321 0.1340 0.0240 -0.2904 585 SER B OG 11667 N N . CYS B 586 ? 0.9367 1.1298 1.1490 0.1806 0.1186 -0.3022 586 CYS B N 11668 C CA . CYS B 586 ? 0.9452 1.1710 1.0989 0.1890 0.1448 -0.3052 586 CYS B CA 11669 C C . CYS B 586 ? 0.9356 1.2256 1.1277 0.1875 0.1493 -0.3339 586 CYS B C 11670 O O . CYS B 586 ? 0.9757 1.3111 1.2465 0.2019 0.1280 -0.3745 586 CYS B O 11671 C CB . CYS B 586 ? 0.9303 1.1810 1.0608 0.2199 0.1452 -0.3241 586 CYS B CB 11672 S SG . CYS B 586 ? 1.2585 1.4454 1.3152 0.2243 0.1508 -0.2909 586 CYS B SG 11673 N N . VAL B 587 ? 0.9711 1.2667 1.1108 0.1694 0.1757 -0.3142 587 VAL B N 11674 C CA . VAL B 587 ? 0.9688 1.3390 1.1339 0.1665 0.1872 -0.3421 587 VAL B CA 11675 C C . VAL B 587 ? 1.1721 1.5887 1.2725 0.1784 0.2111 -0.3456 587 VAL B C 11676 O O . VAL B 587 ? 1.3006 1.6836 1.3179 0.1630 0.2333 -0.3057 587 VAL B O 11677 C CB . VAL B 587 ? 1.0018 1.3563 1.1608 0.1323 0.2005 -0.3187 587 VAL B CB 11678 C CG1 . VAL B 587 ? 1.0068 1.4513 1.1961 0.1283 0.2146 -0.3519 587 VAL B CG1 11679 C CG2 . VAL B 587 ? 1.1021 1.4088 1.3180 0.1210 0.1743 -0.3126 587 VAL B CG2 11680 N N . CYS B 588 ? 1.1595 1.6522 1.2980 0.2060 0.2039 -0.3934 588 CYS B N 11681 C CA . CYS B 588 ? 1.2126 1.7531 1.2884 0.2218 0.2222 -0.3993 588 CYS B CA 11682 C C . CYS B 588 ? 1.2990 1.8968 1.3340 0.1992 0.2540 -0.3919 588 CYS B C 11683 O O . CYS B 588 ? 1.2896 1.9587 1.3838 0.1937 0.2565 -0.4271 588 CYS B O 11684 C CB . CYS B 588 ? 1.1667 1.7772 1.3001 0.2601 0.2023 -0.4582 588 CYS B CB 11685 S SG . CYS B 588 ? 1.2146 1.7673 1.3918 0.2854 0.1667 -0.4668 588 CYS B SG 11686 N N . ILE B 589 ? 1.4334 1.0960 0.9938 -0.0665 0.3272 -0.0349 589 ILE B N 11687 C CA . ILE B 589 ? 1.4435 1.1174 0.9459 -0.0830 0.2868 -0.0041 589 ILE B CA 11688 C C . ILE B 589 ? 1.3540 1.0314 0.9021 -0.0754 0.2415 0.0005 589 ILE B C 11689 O O . ILE B 589 ? 1.4326 1.0786 1.0299 -0.0764 0.2257 -0.0059 589 ILE B O 11690 C CB . ILE B 589 ? 1.4635 1.1025 0.9322 -0.1011 0.2771 0.0107 589 ILE B CB 11691 C CG1 . ILE B 589 ? 1.4241 1.0061 0.9394 -0.0854 0.2884 -0.0190 589 ILE B CG1 11692 C CG2 . ILE B 589 ? 1.4991 1.1836 0.9607 -0.1022 0.2710 0.0200 589 ILE B CG2 11693 C CD1 . ILE B 589 ? 1.4758 1.0172 1.0120 -0.0906 0.2410 -0.0116 589 ILE B CD1 11694 N N . GLN B 590 ? 1.2062 0.9215 0.7271 -0.0619 0.2196 0.0121 590 GLN B N 11695 C CA . GLN B 590 ? 1.2945 1.0197 0.8480 -0.0440 0.1750 0.0149 590 GLN B CA 11696 C C . GLN B 590 ? 1.3966 1.1552 0.8913 -0.0143 0.1575 0.0210 590 GLN B C 11697 O O . GLN B 590 ? 1.5808 1.3381 1.0454 -0.0100 0.1816 0.0069 590 GLN B O 11698 C CB . GLN B 590 ? 1.3112 1.0009 0.9625 -0.0391 0.1723 -0.0170 590 GLN B CB 11699 C CG . GLN B 590 ? 1.3611 1.0472 1.0574 -0.0354 0.1350 -0.0114 590 GLN B CG 11700 C CD . GLN B 590 ? 1.5193 1.1834 1.3029 -0.0243 0.1232 -0.0353 590 GLN B CD 11701 O OE1 . GLN B 590 ? 1.7492 1.4029 1.5675 -0.0193 0.1352 -0.0503 590 GLN B OE1 11702 N NE2 . GLN B 590 ? 1.4506 1.1109 1.2774 -0.0219 0.0973 -0.0334 590 GLN B NE2 11703 N N . PRO B 591 ? 1.4481 1.2374 0.9213 0.0136 0.1143 0.0427 591 PRO B N 11704 C CA . PRO B 591 ? 1.6169 1.4278 1.0194 0.0594 0.0899 0.0445 591 PRO B CA 11705 C C . PRO B 591 ? 1.5618 1.3228 1.0095 0.0730 0.0747 -0.0042 591 PRO B C 11706 O O . PRO B 591 ? 1.4752 1.2047 1.0136 0.0680 0.0549 -0.0264 591 PRO B O 11707 C CB . PRO B 591 ? 1.8338 1.6874 1.2228 0.0967 0.0448 0.0765 591 PRO B CB 11708 C CG . PRO B 591 ? 1.7900 1.6272 1.2752 0.0646 0.0421 0.0726 591 PRO B CG 11709 C CD . PRO B 591 ? 1.6143 1.4238 1.1185 0.0129 0.0850 0.0696 591 PRO B CD 11710 N N . GLY B 592 ? 1.5514 1.3062 0.9394 0.0885 0.0807 -0.0151 592 GLY B N 11711 C CA . GLY B 592 ? 1.5775 1.2836 1.0078 0.1016 0.0533 -0.0531 592 GLY B CA 11712 C C . GLY B 592 ? 1.4123 1.0857 0.9785 0.0636 0.0727 -0.0738 592 GLY B C 11713 O O . GLY B 592 ? 1.5169 1.1554 1.1634 0.0706 0.0305 -0.0903 592 GLY B O 11714 N N . SER B 593 ? 1.1645 0.8519 0.7559 0.0292 0.1345 -0.0680 593 SER B N 11715 C CA . SER B 593 ? 1.1077 0.7791 0.8210 0.0070 0.1607 -0.0768 593 SER B CA 11716 C C . SER B 593 ? 1.0300 0.7167 0.7479 -0.0040 0.2135 -0.0787 593 SER B C 11717 O O . SER B 593 ? 1.2145 0.9242 0.8475 -0.0103 0.2525 -0.0723 593 SER B O 11718 C CB . SER B 593 ? 1.1346 0.8070 0.8877 -0.0101 0.1835 -0.0672 593 SER B CB 11719 O OG . SER B 593 ? 1.2343 0.9237 0.9147 -0.0235 0.2225 -0.0554 593 SER B OG 11720 N N . TYR B 594 ? 0.9770 0.6569 0.8020 -0.0057 0.2137 -0.0816 594 TYR B N 11721 C CA . TYR B 594 ? 0.9061 0.6113 0.7561 -0.0109 0.2634 -0.0793 594 TYR B CA 11722 C C . TYR B 594 ? 0.8892 0.6045 0.8977 -0.0121 0.2691 -0.0629 594 TYR B C 11723 O O . TYR B 594 ? 0.9065 0.6055 1.0002 -0.0116 0.2343 -0.0523 594 TYR B O 11724 C CB . TYR B 594 ? 0.9200 0.6206 0.6892 -0.0010 0.2429 -0.0907 594 TYR B CB 11725 C CG . TYR B 594 ? 0.9270 0.5826 0.7157 0.0165 0.1581 -0.1010 594 TYR B CG 11726 C CD1 . TYR B 594 ? 0.9354 0.5751 0.8335 0.0136 0.1283 -0.0982 594 TYR B CD1 11727 C CD2 . TYR B 594 ? 0.9846 0.6138 0.6856 0.0406 0.1020 -0.1096 594 TYR B CD2 11728 C CE1 . TYR B 594 ? 1.0038 0.5863 0.9174 0.0305 0.0365 -0.1094 594 TYR B CE1 11729 C CE2 . TYR B 594 ? 1.0526 0.6304 0.7602 0.0668 0.0173 -0.1241 594 TYR B CE2 11730 C CZ . TYR B 594 ? 1.0619 0.6084 0.8726 0.0599 -0.0194 -0.1268 594 TYR B CZ 11731 O OH . TYR B 594 ? 1.1171 0.5967 0.9321 0.0868 -0.1177 -0.1429 594 TYR B OH 11732 N N . GLY B 595 ? 0.8617 0.6127 0.9142 -0.0115 0.3144 -0.0537 595 GLY B N 11733 C CA . GLY B 595 ? 0.9203 0.7043 1.1334 -0.0062 0.3296 -0.0214 595 GLY B CA 11734 C C . GLY B 595 ? 0.8270 0.6563 1.0599 0.0101 0.4093 -0.0067 595 GLY B C 11735 O O . GLY B 595 ? 0.8512 0.6678 0.9783 0.0117 0.4384 -0.0259 595 GLY B O 11736 N N . ASP B 596 ? 0.7391 0.6218 1.1091 0.0279 0.4391 0.0322 596 ASP B N 11737 C CA . ASP B 596 ? 0.7597 0.6806 1.1291 0.0590 0.4880 0.0489 596 ASP B CA 11738 C C . ASP B 596 ? 0.9224 0.8183 1.2686 0.0763 0.5018 0.0480 596 ASP B C 11739 O O . ASP B 596 ? 1.0937 0.9675 1.3253 0.0834 0.4940 0.0289 596 ASP B O 11740 C CB . ASP B 596 ? 0.7982 0.7777 1.3030 0.0808 0.4862 0.1018 596 ASP B CB 11741 C CG . ASP B 596 ? 0.9430 0.9441 1.4737 0.0659 0.4710 0.1032 596 ASP B CG 11742 O OD1 . ASP B 596 ? 1.1775 1.1537 1.5834 0.0473 0.4610 0.0604 596 ASP B OD1 11743 O OD2 . ASP B 596 ? 0.8951 0.9391 1.5707 0.0736 0.4616 0.1528 596 ASP B OD2 11744 N N . THR B 597 ? 0.9941 0.8795 1.4277 0.0738 0.4687 0.0708 597 THR B N 11745 C CA . THR B 597 ? 1.1017 0.9567 1.5084 0.0884 0.4644 0.0713 597 THR B CA 11746 C C . THR B 597 ? 1.1800 0.9684 1.4849 0.0540 0.4121 0.0311 597 THR B C 11747 O O . THR B 597 ? 1.4273 1.1859 1.7145 0.0580 0.3970 0.0294 597 THR B O 11748 C CB . THR B 597 ? 1.2448 1.1315 1.7967 0.1068 0.4508 0.1274 597 THR B CB 11749 O OG1 . THR B 597 ? 1.4533 1.3218 2.0762 0.0700 0.3826 0.1347 597 THR B OG1 11750 C CG2 . THR B 597 ? 1.1708 1.1433 1.8371 0.1511 0.5042 0.1844 597 THR B CG2 11751 N N . CYS B 598 ? 0.9674 0.7389 1.2075 0.0266 0.3851 0.0040 598 CYS B N 11752 C CA . CYS B 598 ? 1.0103 0.7363 1.1585 0.0047 0.3345 -0.0238 598 CYS B CA 11753 C C . CYS B 598 ? 0.9943 0.6989 1.2174 -0.0002 0.2765 -0.0141 598 CYS B C 11754 O O . CYS B 598 ? 1.0359 0.7120 1.2105 -0.0061 0.2464 -0.0275 598 CYS B O 11755 C CB . CYS B 598 ? 1.0011 0.7045 1.0443 0.0041 0.3520 -0.0391 598 CYS B CB 11756 S SG . CYS B 598 ? 1.5747 1.2913 1.5192 0.0072 0.4097 -0.0511 598 CYS B SG 11757 N N . GLU B 599 ? 0.9792 0.7013 1.3284 0.0018 0.2587 0.0141 599 GLU B N 11758 C CA . GLU B 599 ? 0.9921 0.6940 1.4296 -0.0040 0.2007 0.0301 599 GLU B CA 11759 C C . GLU B 599 ? 1.1585 0.8144 1.5496 -0.0139 0.1251 0.0006 599 GLU B C 11760 O O . GLU B 599 ? 1.2965 0.9223 1.7199 -0.0158 0.0702 -0.0008 599 GLU B O 11761 C CB . GLU B 599 ? 0.8838 0.6260 1.4876 0.0016 0.2027 0.0854 599 GLU B CB 11762 C CG . GLU B 599 ? 0.8892 0.6408 1.5506 -0.0075 0.1755 0.0950 599 GLU B CG 11763 C CD . GLU B 599 ? 1.0834 0.8716 1.6873 0.0012 0.2394 0.0839 599 GLU B CD 11764 O OE1 . GLU B 599 ? 1.2975 1.0888 1.9216 -0.0069 0.2198 0.0827 599 GLU B OE1 11765 O OE2 . GLU B 599 ? 1.0553 0.8642 1.5916 0.0176 0.3051 0.0755 599 GLU B OE2 11766 N N . LYS B 600 ? 1.1242 0.7743 1.4317 -0.0132 0.1224 -0.0226 600 LYS B N 11767 C CA . LYS B 600 ? 1.0353 0.6395 1.2792 -0.0061 0.0486 -0.0496 600 LYS B CA 11768 C C . LYS B 600 ? 1.0931 0.6866 1.1894 0.0067 0.0431 -0.0767 600 LYS B C 11769 O O . LYS B 600 ? 1.1009 0.7182 1.0980 0.0065 0.0894 -0.0823 600 LYS B O 11770 C CB . LYS B 600 ? 1.0131 0.6160 1.2407 -0.0042 0.0415 -0.0548 600 LYS B CB 11771 C CG . LYS B 600 ? 0.9821 0.5961 1.3728 -0.0154 0.0240 -0.0195 600 LYS B CG 11772 C CD . LYS B 600 ? 1.0507 0.6566 1.4185 -0.0135 0.0076 -0.0283 600 LYS B CD 11773 C CE . LYS B 600 ? 1.0573 0.6757 1.6063 -0.0268 -0.0248 0.0161 600 LYS B CE 11774 N NZ . LYS B 600 ? 1.0789 0.6807 1.6067 -0.0257 -0.0519 0.0055 600 LYS B NZ 11775 N N . CYS B 601 ? 1.1535 0.7173 1.2436 0.0195 -0.0149 -0.0867 601 CYS B N 11776 C CA . CYS B 601 ? 1.1787 0.7437 1.1438 0.0419 -0.0312 -0.1019 601 CYS B CA 11777 C C . CYS B 601 ? 1.2355 0.7565 1.1824 0.0765 -0.1192 -0.1201 601 CYS B C 11778 O O . CYS B 601 ? 1.4710 0.9833 1.4541 0.0835 -0.1481 -0.1218 601 CYS B O 11779 C CB . CYS B 601 ? 1.1550 0.7451 1.1256 0.0290 0.0050 -0.0911 601 CYS B CB 11780 S SG . CYS B 601 ? 1.4199 1.0333 1.2658 0.0551 -0.0138 -0.0906 601 CYS B SG 11781 N N . PRO B 602 ? 1.2679 0.7562 1.1544 0.1032 -0.1653 -0.1358 602 PRO B N 11782 C CA . PRO B 602 ? 1.2004 0.6317 1.0510 0.1499 -0.2610 -0.1584 602 PRO B CA 11783 C C . PRO B 602 ? 1.2666 0.7216 1.0063 0.1967 -0.2741 -0.1626 602 PRO B C 11784 O O . PRO B 602 ? 1.2575 0.6859 1.0167 0.2256 -0.3317 -0.1744 602 PRO B O 11785 C CB . PRO B 602 ? 1.3923 0.7861 1.1706 0.1733 -0.2961 -0.1731 602 PRO B CB 11786 C CG . PRO B 602 ? 1.4137 0.8663 1.1376 0.1498 -0.2067 -0.1583 602 PRO B CG 11787 C CD . PRO B 602 ? 1.3787 0.8773 1.2154 0.0975 -0.1330 -0.1356 602 PRO B CD 11788 N N . THR B 603 ? 1.2696 0.7806 0.9019 0.2055 -0.2217 -0.1464 603 THR B N 11789 C CA . THR B 603 ? 1.3215 0.8775 0.8631 0.2502 -0.2282 -0.1320 603 THR B CA 11790 C C . THR B 603 ? 1.5000 1.1175 1.0803 0.2063 -0.1602 -0.1027 603 THR B C 11791 O O . THR B 603 ? 1.9169 1.5710 1.4606 0.1783 -0.1027 -0.0817 603 THR B O 11792 C CB . THR B 603 ? 1.3443 0.9246 0.7230 0.3067 -0.2352 -0.1202 603 THR B CB 11793 O OG1 . THR B 603 ? 1.2520 0.8665 0.6033 0.2645 -0.1643 -0.1015 603 THR B OG1 11794 C CG2 . THR B 603 ? 1.6141 1.1190 0.9332 0.3623 -0.3151 -0.1536 603 THR B CG2 11795 N N . CYS B 604 ? 1.3671 0.9901 1.0171 0.2033 -0.1736 -0.1022 604 CYS B N 11796 C CA . CYS B 604 ? 1.3526 1.0186 1.0476 0.1644 -0.1245 -0.0784 604 CYS B CA 11797 C C . CYS B 604 ? 1.3532 1.0134 1.1209 0.1748 -0.1565 -0.0867 604 CYS B C 11798 O O . CYS B 604 ? 1.3733 0.9873 1.1781 0.1965 -0.2080 -0.1124 604 CYS B O 11799 C CB . CYS B 604 ? 1.3134 0.9653 1.0766 0.1036 -0.0664 -0.0783 604 CYS B CB 11800 S SG . CYS B 604 ? 2.4250 2.0230 2.3277 0.0781 -0.0776 -0.0982 604 CYS B SG 11801 N N . PRO B 605 ? 1.3777 1.0815 1.1672 0.1592 -0.1314 -0.0639 605 PRO B N 11802 C CA . PRO B 605 ? 1.3115 1.0155 1.1729 0.1662 -0.1538 -0.0713 605 PRO B CA 11803 C C . PRO B 605 ? 1.2907 0.9359 1.2553 0.1369 -0.1600 -0.0962 605 PRO B C 11804 O O . PRO B 605 ? 1.2631 0.8890 1.2723 0.0938 -0.1200 -0.0931 605 PRO B O 11805 C CB . PRO B 605 ? 1.4816 1.2299 1.3608 0.1342 -0.1143 -0.0414 605 PRO B CB 11806 C CG . PRO B 605 ? 1.5477 1.2999 1.3799 0.1016 -0.0726 -0.0240 605 PRO B CG 11807 C CD . PRO B 605 ? 1.5646 1.3167 1.3156 0.1346 -0.0884 -0.0278 605 PRO B CD 11808 N N . ASP B 606 ? 1.3115 0.9330 1.3146 0.1657 -0.2119 -0.1147 606 ASP B N 11809 C CA . ASP B 606 ? 1.4922 1.0598 1.5980 0.1415 -0.2313 -0.1274 606 ASP B CA 11810 C C . ASP B 606 ? 1.4199 0.9946 1.6090 0.1284 -0.2275 -0.1245 606 ASP B C 11811 O O . ASP B 606 ? 1.4060 1.0147 1.5714 0.1577 -0.2392 -0.1266 606 ASP B O 11812 C CB . ASP B 606 ? 1.7400 1.2525 1.8296 0.1820 -0.3103 -0.1517 606 ASP B CB 11813 C CG . ASP B 606 ? 1.8346 1.3431 1.9034 0.2391 -0.3705 -0.1700 606 ASP B CG 11814 O OD1 . ASP B 606 ? 2.0455 1.4954 2.1724 0.2492 -0.4334 -0.1879 606 ASP B OD1 11815 O OD2 . ASP B 606 ? 1.6373 1.2044 1.6376 0.2762 -0.3578 -0.1617 606 ASP B OD2 11816 N N . ALA B 607 ? 1.3505 0.9017 1.6387 0.0882 -0.2083 -0.1134 607 ALA B N 11817 C CA . ALA B 607 ? 1.3335 0.8839 1.7074 0.0764 -0.2096 -0.1075 607 ALA B CA 11818 C C . ALA B 607 ? 1.3036 0.9000 1.6527 0.0769 -0.1735 -0.1037 607 ALA B C 11819 O O . ALA B 607 ? 1.3029 0.9190 1.6308 0.0528 -0.1205 -0.0889 607 ALA B O 11820 C CB . ALA B 607 ? 1.3960 0.9086 1.8011 0.1073 -0.2882 -0.1270 607 ALA B CB 11821 N N . CYS B 608 ? 1.3981 1.0083 1.7521 0.1078 -0.2088 -0.1170 608 CYS B N 11822 C CA . CYS B 608 ? 1.4636 1.1223 1.8171 0.1102 -0.1829 -0.1106 608 CYS B CA 11823 C C . CYS B 608 ? 1.2392 0.9426 1.5240 0.1055 -0.1481 -0.0933 608 CYS B C 11824 O O . CYS B 608 ? 1.2811 1.0040 1.5815 0.0810 -0.1129 -0.0792 608 CYS B O 11825 C CB . CYS B 608 ? 1.6439 1.3220 1.9954 0.1622 -0.2327 -0.1283 608 CYS B CB 11826 S SG . CYS B 608 ? 2.0619 1.7113 2.3391 0.2285 -0.3087 -0.1523 608 CYS B SG 11827 N N . THR B 609 ? 1.2795 0.9953 1.4876 0.1293 -0.1628 -0.0908 609 THR B N 11828 C CA . THR B 609 ? 1.3337 1.0952 1.4801 0.1241 -0.1376 -0.0639 609 THR B CA 11829 C C . THR B 609 ? 1.3217 1.0601 1.4829 0.0701 -0.0891 -0.0528 609 THR B C 11830 O O . THR B 609 ? 1.3504 1.1165 1.4946 0.0556 -0.0739 -0.0301 609 THR B O 11831 C CB . THR B 609 ? 1.4371 1.2067 1.4969 0.1523 -0.1537 -0.0589 609 THR B CB 11832 O OG1 . THR B 609 ? 1.7336 1.4439 1.7992 0.1292 -0.1471 -0.0772 609 THR B OG1 11833 C CG2 . THR B 609 ? 1.5004 1.2944 1.5192 0.2246 -0.2070 -0.0666 609 THR B CG2 11834 N N . PHE B 610 ? 1.2971 0.9845 1.4915 0.0464 -0.0706 -0.0647 610 PHE B N 11835 C CA . PHE B 610 ? 1.3969 1.0581 1.6034 0.0122 -0.0263 -0.0561 610 PHE B CA 11836 C C . PHE B 610 ? 1.2764 0.9317 1.5387 0.0026 -0.0142 -0.0541 610 PHE B C 11837 O O . PHE B 610 ? 1.2360 0.8841 1.4808 -0.0119 0.0068 -0.0450 610 PHE B O 11838 C CB . PHE B 610 ? 1.5891 1.2155 1.8175 0.0024 -0.0076 -0.0587 610 PHE B CB 11839 C CG . PHE B 610 ? 1.5954 1.2240 1.7610 0.0052 -0.0054 -0.0600 610 PHE B CG 11840 C CD1 . PHE B 610 ? 1.5528 1.2060 1.6411 0.0050 -0.0021 -0.0503 610 PHE B CD1 11841 C CD2 . PHE B 610 ? 1.6545 1.2644 1.8442 0.0066 -0.0083 -0.0646 610 PHE B CD2 11842 C CE1 . PHE B 610 ? 1.6505 1.3094 1.6766 0.0075 0.0039 -0.0478 610 PHE B CE1 11843 C CE2 . PHE B 610 ? 1.7338 1.3472 1.8621 0.0095 -0.0027 -0.0669 610 PHE B CE2 11844 C CZ . PHE B 610 ? 1.7437 1.3815 1.7849 0.0106 0.0062 -0.0599 610 PHE B CZ 11845 N N . LYS B 611 ? 1.1831 0.8357 1.5090 0.0122 -0.0324 -0.0620 611 LYS B N 11846 C CA . LYS B 611 ? 1.1056 0.7528 1.4885 0.0031 -0.0161 -0.0567 611 LYS B CA 11847 C C . LYS B 611 ? 1.1015 0.7856 1.4858 0.0115 -0.0266 -0.0594 611 LYS B C 11848 O O . LYS B 611 ? 1.0796 0.7602 1.4909 0.0010 -0.0055 -0.0540 611 LYS B O 11849 C CB . LYS B 611 ? 1.0449 0.6752 1.5068 0.0054 -0.0331 -0.0552 611 LYS B CB 11850 C CG . LYS B 611 ? 1.0422 0.6472 1.5289 -0.0040 -0.0218 -0.0396 611 LYS B CG 11851 C CD . LYS B 611 ? 1.0226 0.6150 1.6090 -0.0080 -0.0433 -0.0211 611 LYS B CD 11852 C CE . LYS B 611 ? 1.0929 0.6762 1.7222 -0.0163 -0.0285 0.0090 611 LYS B CE 11853 N NZ . LYS B 611 ? 1.2796 0.8580 2.0254 -0.0242 -0.0545 0.0445 611 LYS B NZ 11854 N N . LYS B 612 ? 1.2721 0.9980 1.6273 0.0363 -0.0578 -0.0629 612 LYS B N 11855 C CA . LYS B 612 ? 1.1784 0.9576 1.5461 0.0509 -0.0668 -0.0561 612 LYS B CA 11856 C C . LYS B 612 ? 1.1933 0.9788 1.5360 0.0252 -0.0465 -0.0347 612 LYS B C 11857 O O . LYS B 612 ? 1.3503 1.1676 1.7197 0.0236 -0.0462 -0.0245 612 LYS B O 11858 C CB . LYS B 612 ? 1.1577 0.9932 1.4978 0.0987 -0.1052 -0.0536 612 LYS B CB 11859 C CG . LYS B 612 ? 1.2554 1.1236 1.5287 0.1041 -0.1084 -0.0266 612 LYS B CG 11860 C CD . LYS B 612 ? 1.3130 1.2525 1.5555 0.1665 -0.1436 -0.0121 612 LYS B CD 11861 C CE . LYS B 612 ? 1.2506 1.2348 1.4297 0.1723 -0.1444 0.0295 612 LYS B CE 11862 N NZ . LYS B 612 ? 1.1890 1.2532 1.3279 0.2476 -0.1765 0.0546 612 LYS B NZ 11863 N N . GLU B 613 ? 1.1652 0.9167 1.4580 0.0061 -0.0345 -0.0278 613 GLU B N 11864 C CA . GLU B 613 ? 1.1958 0.9289 1.4589 -0.0187 -0.0264 -0.0107 613 GLU B CA 11865 C C . GLU B 613 ? 1.1774 0.8549 1.4555 -0.0327 -0.0004 -0.0216 613 GLU B C 11866 O O . GLU B 613 ? 1.2598 0.9177 1.5244 -0.0452 -0.0034 -0.0130 613 GLU B O 11867 C CB . GLU B 613 ? 1.2486 0.9567 1.4490 -0.0296 -0.0237 -0.0029 613 GLU B CB 11868 C CG . GLU B 613 ? 1.3877 1.0673 1.5521 -0.0532 -0.0310 0.0161 613 GLU B CG 11869 C CD . GLU B 613 ? 1.5007 1.1548 1.6032 -0.0630 -0.0283 0.0227 613 GLU B CD 11870 O OE1 . GLU B 613 ? 1.5225 1.1941 1.6095 -0.0512 -0.0188 0.0158 613 GLU B OE1 11871 O OE2 . GLU B 613 ? 1.5762 1.1877 1.6432 -0.0813 -0.0396 0.0338 613 GLU B OE2 11872 N N . CYS B 614 ? 1.1655 0.8184 1.4719 -0.0267 0.0206 -0.0347 614 CYS B N 11873 C CA . CYS B 614 ? 1.1149 0.7247 1.4306 -0.0288 0.0505 -0.0341 614 CYS B CA 11874 C C . CYS B 614 ? 1.0818 0.7133 1.4435 -0.0274 0.0521 -0.0346 614 CYS B C 11875 O O . CYS B 614 ? 1.1467 0.7480 1.4905 -0.0290 0.0679 -0.0308 614 CYS B O 11876 C CB . CYS B 614 ? 0.9794 0.5715 1.3239 -0.0212 0.0718 -0.0302 614 CYS B CB 11877 S SG . CYS B 614 ? 1.4721 1.0150 1.7938 -0.0068 0.1154 -0.0124 614 CYS B SG 11878 N N . VAL B 615 ? 0.8975 0.5783 1.3114 -0.0189 0.0339 -0.0409 615 VAL B N 11879 C CA . VAL B 615 ? 0.8554 0.5647 1.3184 -0.0154 0.0377 -0.0430 615 VAL B CA 11880 C C . VAL B 615 ? 0.9674 0.7065 1.4186 -0.0200 0.0272 -0.0362 615 VAL B C 11881 O O . VAL B 615 ? 1.1401 0.8807 1.6105 -0.0244 0.0409 -0.0351 615 VAL B O 11882 C CB . VAL B 615 ? 0.8085 0.5584 1.3273 0.0039 0.0140 -0.0546 615 VAL B CB 11883 C CG1 . VAL B 615 ? 0.8131 0.5279 1.3669 0.0018 0.0159 -0.0534 615 VAL B CG1 11884 C CG2 . VAL B 615 ? 0.8444 0.6356 1.3386 0.0260 -0.0216 -0.0582 615 VAL B CG2 11885 N N . GLU B 616 ? 0.9501 0.7169 1.3746 -0.0191 0.0012 -0.0249 616 GLU B N 11886 C CA . GLU B 616 ? 0.9683 0.7661 1.3936 -0.0278 -0.0175 -0.0032 616 GLU B CA 11887 C C . GLU B 616 ? 1.1227 0.8415 1.5019 -0.0502 -0.0107 -0.0027 616 GLU B C 11888 O O . GLU B 616 ? 1.1610 0.8770 1.5523 -0.0589 -0.0180 0.0047 616 GLU B O 11889 C CB . GLU B 616 ? 0.9375 0.7849 1.3451 -0.0213 -0.0481 0.0237 616 GLU B CB 11890 C CG . GLU B 616 ? 0.8950 0.8231 1.3302 0.0184 -0.0619 0.0267 616 GLU B CG 11891 C CD . GLU B 616 ? 0.8414 0.8508 1.3417 0.0417 -0.0684 0.0389 616 GLU B CD 11892 O OE1 . GLU B 616 ? 0.8365 0.8987 1.3613 0.0358 -0.0842 0.0782 616 GLU B OE1 11893 O OE2 . GLU B 616 ? 0.7889 0.8112 1.3224 0.0660 -0.0608 0.0127 616 GLU B OE2 11894 N N . CYS B 617 ? 1.2475 0.9005 1.5701 -0.0533 0.0001 -0.0110 617 CYS B N 11895 C CA . CYS B 617 ? 1.2175 0.7835 1.4782 -0.0571 0.0055 -0.0154 617 CYS B CA 11896 C C . CYS B 617 ? 1.1577 0.6976 1.4255 -0.0455 0.0343 -0.0241 617 CYS B C 11897 O O . CYS B 617 ? 1.0473 0.5631 1.3013 -0.0492 0.0216 -0.0222 617 CYS B O 11898 C CB . CYS B 617 ? 1.1444 0.6609 1.3516 -0.0490 0.0208 -0.0224 617 CYS B CB 11899 S SG . CYS B 617 ? 1.4845 0.8930 1.6026 -0.0280 0.0324 -0.0302 617 CYS B SG 11900 N N . LYS B 618 ? 1.2242 0.7703 1.5160 -0.0316 0.0698 -0.0278 618 LYS B N 11901 C CA . LYS B 618 ? 1.2045 0.7305 1.4993 -0.0166 0.1030 -0.0241 618 LYS B CA 11902 C C . LYS B 618 ? 1.1283 0.7019 1.4786 -0.0241 0.1049 -0.0258 618 LYS B C 11903 O O . LYS B 618 ? 1.3193 0.8641 1.6404 -0.0201 0.1102 -0.0253 618 LYS B O 11904 C CB . LYS B 618 ? 1.0986 0.6340 1.4270 -0.0033 0.1346 -0.0118 618 LYS B CB 11905 C CG . LYS B 618 ? 1.1676 0.6509 1.4357 0.0212 0.1542 0.0002 618 LYS B CG 11906 C CD . LYS B 618 ? 1.3701 0.7993 1.5678 0.0528 0.1741 0.0094 618 LYS B CD 11907 C CE . LYS B 618 ? 1.4389 0.8261 1.5751 0.0954 0.1968 0.0265 618 LYS B CE 11908 N NZ . LYS B 618 ? 1.4748 0.8063 1.5244 0.1440 0.2135 0.0376 618 LYS B NZ 11909 N N . LYS B 619 ? 0.9443 0.5874 1.3689 -0.0293 0.0984 -0.0294 619 LYS B N 11910 C CA . LYS B 619 ? 0.8698 0.5644 1.3542 -0.0291 0.1067 -0.0321 619 LYS B CA 11911 C C . LYS B 619 ? 1.1069 0.8458 1.6085 -0.0361 0.0817 -0.0312 619 LYS B C 11912 O O . LYS B 619 ? 1.4738 1.2246 1.9923 -0.0380 0.0938 -0.0307 619 LYS B O 11913 C CB . LYS B 619 ? 0.7713 0.5151 1.3255 -0.0214 0.1030 -0.0379 619 LYS B CB 11914 C CG . LYS B 619 ? 0.7899 0.5065 1.3659 -0.0190 0.1290 -0.0254 619 LYS B CG 11915 C CD . LYS B 619 ? 1.0662 0.7589 1.6214 -0.0170 0.1680 -0.0097 619 LYS B CD 11916 C CE . LYS B 619 ? 1.0937 0.7764 1.6804 -0.0106 0.1957 0.0215 619 LYS B CE 11917 N NZ . LYS B 619 ? 1.2378 0.9628 1.9166 -0.0173 0.1829 0.0221 619 LYS B NZ 11918 N N . PHE B 620 ? 0.9090 0.6798 1.4116 -0.0382 0.0473 -0.0236 620 PHE B N 11919 C CA . PHE B 620 ? 0.8280 0.6618 1.3675 -0.0414 0.0201 -0.0055 620 PHE B CA 11920 C C . PHE B 620 ? 0.9030 0.6826 1.3959 -0.0628 -0.0088 0.0110 620 PHE B C 11921 O O . PHE B 620 ? 0.9087 0.7357 1.4412 -0.0713 -0.0390 0.0370 620 PHE B O 11922 C CB . PHE B 620 ? 0.8134 0.7319 1.3882 -0.0219 -0.0047 0.0085 620 PHE B CB 11923 C CG . PHE B 620 ? 0.8019 0.7824 1.4304 0.0093 0.0058 -0.0071 620 PHE B CG 11924 C CD1 . PHE B 620 ? 0.9252 0.8915 1.5410 0.0270 0.0019 -0.0246 620 PHE B CD1 11925 C CD2 . PHE B 620 ? 0.8097 0.8575 1.5013 0.0230 0.0146 -0.0054 620 PHE B CD2 11926 C CE1 . PHE B 620 ? 1.0802 1.0870 1.7398 0.0596 -0.0024 -0.0418 620 PHE B CE1 11927 C CE2 . PHE B 620 ? 0.9276 1.0250 1.6638 0.0576 0.0188 -0.0232 620 PHE B CE2 11928 C CZ . PHE B 620 ? 1.0888 1.1598 1.8062 0.0767 0.0059 -0.0424 620 PHE B CZ 11929 N N . ASP B 621 ? 1.0584 0.7396 1.4716 -0.0673 -0.0046 -0.0004 621 ASP B N 11930 C CA . ASP B 621 ? 1.1493 0.7532 1.5012 -0.0812 -0.0420 0.0085 621 ASP B CA 11931 C C . ASP B 621 ? 1.1417 0.7917 1.5203 -0.0984 -0.0909 0.0419 621 ASP B C 11932 O O . ASP B 621 ? 1.1798 0.7977 1.5503 -0.1171 -0.1387 0.0639 621 ASP B O 11933 C CB . ASP B 621 ? 1.2324 0.8009 1.5777 -0.0845 -0.0503 0.0070 621 ASP B CB 11934 C CG . ASP B 621 ? 1.3276 0.7748 1.5802 -0.0862 -0.0910 0.0036 621 ASP B CG 11935 O OD1 . ASP B 621 ? 1.1859 0.6119 1.4474 -0.1010 -0.1368 0.0171 621 ASP B OD1 11936 O OD2 . ASP B 621 ? 1.5291 0.9007 1.7010 -0.0688 -0.0816 -0.0116 621 ASP B OD2 11937 N N . ARG B 622 ? 1.1848 0.9086 1.5939 -0.0895 -0.0838 0.0510 622 ARG B N 11938 C CA . ARG B 622 ? 1.2500 1.0377 1.6846 -0.0969 -0.1237 0.0944 622 ARG B CA 11939 C C . ARG B 622 ? 1.4116 1.1423 1.7756 -0.1046 -0.1324 0.0930 622 ARG B C 11940 O O . ARG B 622 ? 1.4050 1.0906 1.7242 -0.0937 -0.0988 0.0594 622 ARG B O 11941 C CB . ARG B 622 ? 1.1858 1.1003 1.6884 -0.0680 -0.1146 0.1115 622 ARG B CB 11942 C CG . ARG B 622 ? 1.0940 1.0931 1.6815 -0.0601 -0.1212 0.1347 622 ARG B CG 11943 C CD . ARG B 622 ? 1.0023 1.1319 1.6489 -0.0155 -0.1170 0.1554 622 ARG B CD 11944 N NE . ARG B 622 ? 1.0809 1.2014 1.7177 0.0125 -0.0822 0.1055 622 ARG B NE 11945 C CZ . ARG B 622 ? 1.0569 1.2675 1.7375 0.0606 -0.0783 0.1052 622 ARG B CZ 11946 N NH1 . ARG B 622 ? 0.9464 1.2771 1.6832 0.0933 -0.0985 0.1558 622 ARG B NH1 11947 N NH2 . ARG B 622 ? 1.0337 1.2157 1.7047 0.0807 -0.0589 0.0593 622 ARG B NH2 11948 N N . GLY B 623 ? 1.5540 1.2930 1.9169 -0.1242 -0.1794 0.1362 623 GLY B N 11949 C CA . GLY B 623 ? 1.7155 1.3747 2.0038 -0.1387 -0.1965 0.1347 623 GLY B CA 11950 C C . GLY B 623 ? 1.6833 1.3675 1.9377 -0.1280 -0.1741 0.1321 623 GLY B C 11951 O O . GLY B 623 ? 1.7275 1.4651 1.9981 -0.1037 -0.1391 0.1150 623 GLY B O 11952 N N . ALA B 624 ? 1.6160 1.2493 1.8186 -0.1462 -0.2005 0.1473 624 ALA B N 11953 C CA . ALA B 624 ? 1.5700 1.2086 1.7249 -0.1428 -0.1850 0.1481 624 ALA B CA 11954 C C . ALA B 624 ? 1.5125 1.0787 1.6111 -0.1265 -0.1371 0.0909 624 ALA B C 11955 O O . ALA B 624 ? 1.5462 1.0842 1.5928 -0.1277 -0.1273 0.0852 624 ALA B O 11956 C CB . ALA B 624 ? 1.5433 1.3050 1.7359 -0.1224 -0.1756 0.1798 624 ALA B CB 11957 N N . LEU B 625 ? 1.4106 0.9546 1.5248 -0.1101 -0.1062 0.0560 625 LEU B N 11958 C CA . LEU B 625 ? 1.4412 0.9026 1.5046 -0.0934 -0.0723 0.0184 625 LEU B CA 11959 C C . LEU B 625 ? 1.4474 0.8255 1.4790 -0.0881 -0.0887 0.0071 625 LEU B C 11960 O O . LEU B 625 ? 1.4509 0.7521 1.4228 -0.0631 -0.0698 -0.0158 625 LEU B O 11961 C CB . LEU B 625 ? 1.4308 0.9275 1.5323 -0.0734 -0.0259 -0.0020 625 LEU B CB 11962 C CG . LEU B 625 ? 1.2908 0.7385 1.3584 -0.0528 0.0134 -0.0218 625 LEU B CG 11963 C CD1 . LEU B 625 ? 1.2358 0.6718 1.2560 -0.0571 0.0124 -0.0199 625 LEU B CD1 11964 C CD2 . LEU B 625 ? 1.1785 0.6680 1.3067 -0.0404 0.0452 -0.0281 625 LEU B CD2 11965 N N . HIS B 626 ? 1.4623 0.8600 1.5325 -0.1050 -0.1258 0.0270 626 HIS B N 11966 C CA . HIS B 626 ? 1.4786 0.7994 1.5209 -0.0991 -0.1477 0.0163 626 HIS B CA 11967 C C . HIS B 626 ? 1.6221 0.8647 1.6196 -0.1173 -0.2185 0.0327 626 HIS B C 11968 O O . HIS B 626 ? 1.9545 1.1033 1.9035 -0.1071 -0.2519 0.0197 626 HIS B O 11969 C CB . HIS B 626 ? 1.4242 0.8152 1.5458 -0.1057 -0.1438 0.0265 626 HIS B CB 11970 C CG . HIS B 626 ? 1.5105 0.8409 1.6193 -0.1112 -0.1845 0.0289 626 HIS B CG 11971 N ND1 . HIS B 626 ? 1.7663 0.9873 1.7912 -0.0834 -0.1807 -0.0006 626 HIS B ND1 11972 C CD2 . HIS B 626 ? 1.4198 0.7858 1.5889 -0.1362 -0.2327 0.0613 626 HIS B CD2 11973 C CE1 . HIS B 626 ? 1.7309 0.9103 1.7555 -0.0930 -0.2285 0.0067 626 HIS B CE1 11974 N NE2 . HIS B 626 ? 1.5324 0.8005 1.6525 -0.1291 -0.2611 0.0454 626 HIS B NE2 11975 N N . ASP B 627 ? 1.5635 0.8380 1.5706 -0.1412 -0.2457 0.0629 627 ASP B N 11976 C CA . ASP B 627 ? 1.7306 0.9396 1.7124 -0.1663 -0.3232 0.0906 627 ASP B CA 11977 C C . ASP B 627 ? 1.8690 0.9470 1.7387 -0.1431 -0.3344 0.0551 627 ASP B C 11978 O O . ASP B 627 ? 2.0529 1.0208 1.8714 -0.1445 -0.4032 0.0536 627 ASP B O 11979 C CB . ASP B 627 ? 1.6402 0.9473 1.6804 -0.1987 -0.3474 0.1503 627 ASP B CB 11980 C CG . ASP B 627 ? 1.5456 0.9910 1.6924 -0.2059 -0.3399 0.1921 627 ASP B CG 11981 O OD1 . ASP B 627 ? 1.6428 1.0937 1.8280 -0.2002 -0.3381 0.1814 627 ASP B OD1 11982 O OD2 . ASP B 627 ? 1.4177 0.9687 1.6044 -0.2104 -0.3349 0.2370 627 ASP B OD2 11983 N N . GLU B 628 ? 1.6910 0.7799 1.5240 -0.1171 -0.2711 0.0276 628 GLU B N 11984 C CA . GLU B 628 ? 1.7837 0.7692 1.5156 -0.0845 -0.2704 -0.0035 628 GLU B CA 11985 C C . GLU B 628 ? 1.8949 0.8128 1.5652 -0.0257 -0.2342 -0.0438 628 GLU B C 11986 O O . GLU B 628 ? 2.1467 0.9909 1.7314 0.0208 -0.2214 -0.0691 628 GLU B O 11987 C CB . GLU B 628 ? 1.8243 0.8671 1.5547 -0.0855 -0.2219 -0.0030 628 GLU B CB 11988 C CG . GLU B 628 ? 1.9531 1.0664 1.7266 -0.1334 -0.2517 0.0433 628 GLU B CG 11989 C CD . GLU B 628 ? 1.9097 1.1559 1.7767 -0.1526 -0.2291 0.0738 628 GLU B CD 11990 O OE1 . GLU B 628 ? 1.8991 1.1749 1.8031 -0.1360 -0.1961 0.0553 628 GLU B OE1 11991 O OE2 . GLU B 628 ? 1.8297 1.1518 1.7287 -0.1784 -0.2454 0.1193 628 GLU B OE2 11992 N N . ASN B 629 ? 1.7588 0.7114 1.4735 -0.0224 -0.2149 -0.0441 629 ASN B N 11993 C CA . ASN B 629 ? 1.7761 0.6803 1.4387 0.0339 -0.1786 -0.0689 629 ASN B CA 11994 C C . ASN B 629 ? 1.7233 0.6657 1.3786 0.0736 -0.1018 -0.0772 629 ASN B C 11995 O O . ASN B 629 ? 1.7666 0.6583 1.3547 0.1364 -0.0744 -0.0887 629 ASN B O 11996 C CB . ASN B 629 ? 1.9205 0.6761 1.4652 0.0752 -0.2391 -0.0892 629 ASN B CB 11997 C CG . ASN B 629 ? 1.9994 0.7110 1.4962 0.1261 -0.2215 -0.1026 629 ASN B CG 11998 O OD1 . ASN B 629 ? 2.1501 0.8319 1.5761 0.1956 -0.1768 -0.1143 629 ASN B OD1 11999 N ND2 . ASN B 629 ? 1.9210 0.6366 1.4579 0.0958 -0.2549 -0.0945 629 ASN B ND2 12000 N N . THR B 630 ? 1.6386 0.6744 1.3647 0.0415 -0.0703 -0.0653 630 THR B N 12001 C CA . THR B 630 ? 1.6683 0.7484 1.4079 0.0693 -0.0061 -0.0665 630 THR B CA 12002 C C . THR B 630 ? 1.7332 0.8944 1.5577 0.0683 0.0414 -0.0552 630 THR B C 12003 O O . THR B 630 ? 1.7033 0.9127 1.5657 0.0828 0.0875 -0.0470 630 THR B O 12004 C CB . THR B 630 ? 1.5799 0.7066 1.3407 0.0384 -0.0026 -0.0614 630 THR B CB 12005 O OG1 . THR B 630 ? 1.4634 0.6770 1.3058 -0.0090 -0.0101 -0.0454 630 THR B OG1 12006 C CG2 . THR B 630 ? 1.6868 0.7384 1.3734 0.0309 -0.0547 -0.0661 630 THR B CG2 12007 N N . CYS B 631 ? 1.7426 1.1093 1.4820 0.1758 0.1760 0.0166 631 CYS B N 12008 C CA . CYS B 631 ? 1.7331 1.0848 1.5029 0.1965 0.1581 0.0187 631 CYS B CA 12009 C C . CYS B 631 ? 1.6674 1.0597 1.4773 0.1906 0.1642 0.0099 631 CYS B C 12010 O O . CYS B 631 ? 1.6675 1.0742 1.4884 0.1848 0.1542 0.0238 631 CYS B O 12011 C CB . CYS B 631 ? 1.8933 1.2001 1.6627 0.2189 0.1507 0.0065 631 CYS B CB 12012 S SG . CYS B 631 ? 2.6223 1.9139 2.4277 0.2453 0.1262 0.0091 631 CYS B SG 12013 N N . ASN B 632 ? 1.6874 1.0984 1.5175 0.1904 0.1811 -0.0156 632 ASN B N 12014 C CA . ASN B 632 ? 1.7227 1.1830 1.5945 0.1836 0.1894 -0.0315 632 ASN B CA 12015 C C . ASN B 632 ? 1.7928 1.2984 1.6563 0.1479 0.1996 -0.0201 632 ASN B C 12016 O O . ASN B 632 ? 1.8564 1.3964 1.7437 0.1361 0.1985 -0.0215 632 ASN B O 12017 C CB . ASN B 632 ? 1.7972 1.2714 1.6922 0.1916 0.2072 -0.0665 632 ASN B CB 12018 C CG . ASN B 632 ? 1.9190 1.3472 1.8285 0.2296 0.1920 -0.0784 632 ASN B CG 12019 O OD1 . ASN B 632 ? 1.9793 1.3593 1.8688 0.2449 0.1712 -0.0590 632 ASN B OD1 12020 N ND2 . ASN B 632 ? 1.9480 1.3914 1.8919 0.2451 0.2011 -0.1113 632 ASN B ND2 12021 N N . ARG B 633 ? 1.7916 1.2972 1.6180 0.1286 0.2083 -0.0086 633 ARG B N 12022 C CA . ARG B 633 ? 1.7602 1.3039 1.5714 0.0934 0.2156 0.0050 633 ARG B CA 12023 C C . ARG B 633 ? 1.7332 1.2586 1.5289 0.0902 0.1928 0.0372 633 ARG B C 12024 O O . ARG B 633 ? 1.7679 1.3169 1.5671 0.0671 0.1913 0.0455 633 ARG B O 12025 C CB . ARG B 633 ? 1.7789 1.3319 1.5554 0.0749 0.2304 0.0066 633 ARG B CB 12026 C CG . ARG B 633 ? 1.7760 1.3610 1.5277 0.0396 0.2321 0.0272 633 ARG B CG 12027 C CD . ARG B 633 ? 1.8095 1.4462 1.5813 0.0092 0.2478 0.0128 633 ARG B CD 12028 N NE . ARG B 633 ? 1.6426 1.3128 1.4324 0.0023 0.2756 -0.0237 633 ARG B NE 12029 C CZ . ARG B 633 ? 1.6605 1.3625 1.4287 -0.0264 0.2959 -0.0310 633 ARG B CZ 12030 N NH1 . ARG B 633 ? 1.6637 1.3709 1.3915 -0.0500 0.2895 -0.0018 633 ARG B NH1 12031 N NH2 . ARG B 633 ? 1.6883 1.4170 1.4754 -0.0308 0.3217 -0.0683 633 ARG B NH2 12032 N N . TYR B 634 ? 1.6973 1.1798 1.4740 0.1116 0.1752 0.0535 634 TYR B N 12033 C CA . TYR B 634 ? 1.7162 1.1769 1.4765 0.1119 0.1532 0.0815 634 TYR B CA 12034 C C . TYR B 634 ? 1.8575 1.3057 1.6424 0.1204 0.1393 0.0836 634 TYR B C 12035 O O . TYR B 634 ? 2.1517 1.6120 1.9362 0.0988 0.1358 0.0938 634 TYR B O 12036 C CB . TYR B 634 ? 1.6277 1.0559 1.3642 0.1323 0.1403 0.0919 634 TYR B CB 12037 C CG . TYR B 634 ? 1.6303 1.0752 1.3350 0.1183 0.1451 0.1016 634 TYR B CG 12038 C CD1 . TYR B 634 ? 1.6624 1.1416 1.3569 0.0882 0.1557 0.1073 634 TYR B CD1 12039 C CD2 . TYR B 634 ? 1.6893 1.1216 1.3732 0.1326 0.1385 0.1041 634 TYR B CD2 12040 C CE1 . TYR B 634 ? 1.6777 1.1761 1.3426 0.0752 0.1579 0.1174 634 TYR B CE1 12041 C CE2 . TYR B 634 ? 1.7471 1.2035 1.4043 0.1206 0.1417 0.1114 634 TYR B CE2 12042 C CZ . TYR B 634 ? 1.6999 1.1882 1.3480 0.0931 0.1506 0.1191 634 TYR B CZ 12043 O OH . TYR B 634 ? 1.6748 1.1905 1.2959 0.0810 0.1518 0.1275 634 TYR B OH 12044 N N . CYS B 635 ? 1.7289 1.1526 1.5312 0.1481 0.1309 0.0744 635 CYS B N 12045 C CA . CYS B 635 ? 1.8054 1.2219 1.6316 0.1557 0.1176 0.0750 635 CYS B CA 12046 C C . CYS B 635 ? 1.8778 1.3303 1.7435 0.1565 0.1293 0.0493 635 CYS B C 12047 O O . CYS B 635 ? 1.8721 1.3188 1.7539 0.1786 0.1324 0.0314 635 CYS B O 12048 C CB . CYS B 635 ? 1.8955 1.2694 1.7183 0.1835 0.0988 0.0804 635 CYS B CB 12049 S SG . CYS B 635 ? 1.3313 0.6840 1.1495 0.2070 0.1028 0.0649 635 CYS B SG 12050 N N . ARG B 636 ? 1.9777 1.4670 1.8571 0.1316 0.1347 0.0467 636 ARG B N 12051 C CA . ARG B 636 ? 2.0030 1.5402 1.9254 0.1309 0.1454 0.0185 636 ARG B CA 12052 C C . ARG B 636 ? 2.0090 1.5429 1.9550 0.1427 0.1283 0.0187 636 ARG B C 12053 O O . ARG B 636 ? 2.0189 1.5983 2.0041 0.1432 0.1328 -0.0042 636 ARG B O 12054 C CB . ARG B 636 ? 2.0341 1.6268 1.9575 0.0902 0.1644 0.0101 636 ARG B CB 12055 C CG . ARG B 636 ? 2.0628 1.7176 2.0324 0.0910 0.1828 -0.0291 636 ARG B CG 12056 C CD . ARG B 636 ? 2.1969 1.9138 2.1650 0.0436 0.2024 -0.0391 636 ARG B CD 12057 N NE . ARG B 636 ? 2.3314 2.1175 2.3500 0.0455 0.2206 -0.0828 636 ARG B NE 12058 C CZ . ARG B 636 ? 2.3463 2.2034 2.3747 0.0046 0.2408 -0.1030 636 ARG B CZ 12059 N NH1 . ARG B 636 ? 2.3854 2.2461 2.3703 -0.0443 0.2437 -0.0788 636 ARG B NH1 12060 N NH2 . ARG B 636 ? 2.2668 2.1913 2.3473 0.0121 0.2569 -0.1484 636 ARG B NH2 12061 N N . ASP B 637 ? 2.0015 1.4863 1.9245 0.1514 0.1089 0.0425 637 ASP B N 12062 C CA . ASP B 637 ? 2.0289 1.5058 1.9678 0.1595 0.0920 0.0452 637 ASP B CA 12063 C C . ASP B 637 ? 2.0426 1.5342 2.0209 0.1902 0.0874 0.0232 637 ASP B C 12064 O O . ASP B 637 ? 2.2343 1.6967 2.2085 0.2168 0.0838 0.0202 637 ASP B O 12065 C CB . ASP B 637 ? 2.1123 1.5305 2.0199 0.1691 0.0732 0.0696 637 ASP B CB 12066 C CG . ASP B 637 ? 2.2790 1.6737 2.1465 0.1515 0.0741 0.0907 637 ASP B CG 12067 O OD1 . ASP B 637 ? 2.3856 1.8068 2.2448 0.1227 0.0860 0.0926 637 ASP B OD1 12068 O OD2 . ASP B 637 ? 2.2939 1.6468 2.1381 0.1661 0.0620 0.1045 637 ASP B OD2 12069 N N . GLU B 638 ? 1.9377 1.4743 1.9516 0.1856 0.0861 0.0077 638 GLU B N 12070 C CA . GLU B 638 ? 1.9108 1.4663 1.9659 0.2178 0.0779 -0.0136 638 GLU B CA 12071 C C . GLU B 638 ? 1.7706 1.2804 1.8171 0.2396 0.0535 0.0016 638 GLU B C 12072 O O . GLU B 638 ? 1.7330 1.2305 1.7658 0.2243 0.0441 0.0170 638 GLU B O 12073 C CB . GLU B 638 ? 1.9914 1.6239 2.0921 0.2059 0.0846 -0.0395 638 GLU B CB 12074 C CG . GLU B 638 ? 2.0237 1.6729 2.1187 0.1750 0.0791 -0.0291 638 GLU B CG 12075 C CD . GLU B 638 ? 2.0245 1.7581 2.1678 0.1651 0.0846 -0.0589 638 GLU B CD 12076 O OE1 . GLU B 638 ? 2.0433 1.8263 2.2276 0.1836 0.0937 -0.0895 638 GLU B OE1 12077 O OE2 . GLU B 638 ? 2.0210 1.7734 2.1617 0.1387 0.0799 -0.0543 638 GLU B OE2 12078 N N . ILE B 639 ? 1.7014 1.1824 1.7518 0.2728 0.0432 -0.0029 639 ILE B N 12079 C CA . ILE B 639 ? 1.5701 1.0078 1.6076 0.2907 0.0200 0.0112 639 ILE B CA 12080 C C . ILE B 639 ? 1.5957 1.0554 1.6725 0.3185 0.0035 -0.0043 639 ILE B C 12081 O O . ILE B 639 ? 1.6972 1.1512 1.7881 0.3446 0.0012 -0.0183 639 ILE B O 12082 C CB . ILE B 639 ? 1.4978 0.8737 1.4941 0.3018 0.0167 0.0241 639 ILE B CB 12083 C CG1 . ILE B 639 ? 1.4771 0.8408 1.4393 0.2785 0.0325 0.0362 639 ILE B CG1 12084 C CG2 . ILE B 639 ? 1.5198 0.8556 1.4973 0.3117 -0.0058 0.0385 639 ILE B CG2 12085 C CD1 . ILE B 639 ? 1.4485 0.7641 1.3709 0.2852 0.0319 0.0452 639 ILE B CD1 12086 N N . GLU B 640 ? 1.5738 1.0573 1.6673 0.3131 -0.0093 -0.0022 640 GLU B N 12087 C CA . GLU B 640 ? 1.5791 1.0883 1.7099 0.3395 -0.0291 -0.0147 640 GLU B CA 12088 C C . GLU B 640 ? 1.4965 0.9562 1.6014 0.3494 -0.0536 0.0052 640 GLU B C 12089 O O . GLU B 640 ? 1.5956 1.0496 1.6844 0.3283 -0.0574 0.0183 640 GLU B O 12090 C CB . GLU B 640 ? 1.7279 1.3150 1.9002 0.3235 -0.0253 -0.0315 640 GLU B CB 12091 C CG . GLU B 640 ? 1.8387 1.4650 2.0545 0.3515 -0.0475 -0.0461 640 GLU B CG 12092 C CD . GLU B 640 ? 1.8625 1.5724 2.1157 0.3294 -0.0429 -0.0633 640 GLU B CD 12093 O OE1 . GLU B 640 ? 1.8490 1.5773 2.0880 0.2891 -0.0227 -0.0615 640 GLU B OE1 12094 O OE2 . GLU B 640 ? 1.8548 1.6119 2.1490 0.3508 -0.0606 -0.0783 640 GLU B OE2 12095 N N . SER B 641 ? 1.4769 0.8981 1.5746 0.3791 -0.0705 0.0068 641 SER B N 12096 C CA . SER B 641 ? 1.5078 0.8826 1.5762 0.3849 -0.0945 0.0254 641 SER B CA 12097 C C . SER B 641 ? 1.5939 1.0117 1.6943 0.3890 -0.1139 0.0220 641 SER B C 12098 O O . SER B 641 ? 1.7123 1.1734 1.8568 0.4123 -0.1242 0.0050 641 SER B O 12099 C CB . SER B 641 ? 1.5764 0.8946 1.6223 0.4115 -0.1095 0.0292 641 SER B CB 12100 O OG . SER B 641 ? 1.5884 0.8634 1.6005 0.4114 -0.1332 0.0476 641 SER B OG 12101 N N . VAL B 642 ? 1.6418 1.0504 1.7209 0.3667 -0.1191 0.0360 642 VAL B N 12102 C CA . VAL B 642 ? 1.6718 1.1220 1.7756 0.3636 -0.1356 0.0335 642 VAL B CA 12103 C C . VAL B 642 ? 1.6412 1.0514 1.7208 0.3766 -0.1645 0.0482 642 VAL B C 12104 O O . VAL B 642 ? 1.7184 1.0680 1.7513 0.3713 -0.1663 0.0631 642 VAL B O 12105 C CB . VAL B 642 ? 1.6446 1.1120 1.7400 0.3261 -0.1222 0.0369 642 VAL B CB 12106 C CG1 . VAL B 642 ? 1.5844 0.9885 1.6283 0.3101 -0.1195 0.0549 642 VAL B CG1 12107 C CG2 . VAL B 642 ? 1.6355 1.1533 1.7575 0.3187 -0.1367 0.0310 642 VAL B CG2 12108 N N . LYS B 643 ? 1.8308 1.2791 1.9410 0.3917 -0.1877 0.0433 643 LYS B N 12109 C CA . LYS B 643 ? 2.0071 1.4191 2.0931 0.4039 -0.2187 0.0586 643 LYS B CA 12110 C C . LYS B 643 ? 1.9319 1.3477 1.9973 0.3737 -0.2240 0.0687 643 LYS B C 12111 O O . LYS B 643 ? 1.9505 1.4244 2.0466 0.3638 -0.2274 0.0604 643 LYS B O 12112 C CB . LYS B 643 ? 2.1239 1.5724 2.2525 0.4405 -0.2462 0.0491 643 LYS B CB 12113 C CG . LYS B 643 ? 2.0689 1.4923 2.1760 0.4498 -0.2835 0.0664 643 LYS B CG 12114 C CD . LYS B 643 ? 1.9500 1.4145 2.1048 0.4911 -0.3133 0.0558 643 LYS B CD 12115 C CE . LYS B 643 ? 1.8851 1.3241 2.0149 0.4990 -0.3542 0.0763 643 LYS B CE 12116 N NZ . LYS B 643 ? 1.8552 1.3372 2.0347 0.5438 -0.3876 0.0660 643 LYS B NZ 12117 N N . GLU B 644 ? 1.9910 1.3480 2.0039 0.3569 -0.2228 0.0836 644 GLU B N 12118 C CA . GLU B 644 ? 2.1375 1.4887 2.1247 0.3301 -0.2302 0.0917 644 GLU B CA 12119 C C . GLU B 644 ? 2.1187 1.5052 2.1204 0.3019 -0.2105 0.0825 644 GLU B C 12120 O O . GLU B 644 ? 2.2053 1.5835 2.1852 0.2778 -0.2120 0.0856 644 GLU B O 12121 C CB . GLU B 644 ? 2.3640 1.7331 2.3580 0.3404 -0.2640 0.0980 644 GLU B CB 12122 C CG . GLU B 644 ? 2.4993 1.8238 2.4734 0.3685 -0.2897 0.1099 644 GLU B CG 12123 C CD . GLU B 644 ? 2.5142 1.7663 2.4243 0.3531 -0.2880 0.1239 644 GLU B CD 12124 O OE1 . GLU B 644 ? 2.5244 1.7692 2.4063 0.3217 -0.2777 0.1256 644 GLU B OE1 12125 O OE2 . GLU B 644 ? 2.4511 1.6548 2.3387 0.3713 -0.2966 0.1309 644 GLU B OE2 12126 N N . LEU B 645 ? 2.0022 1.4252 2.0372 0.3025 -0.1920 0.0704 645 LEU B N 12127 C CA . LEU B 645 ? 1.9922 1.4515 2.0412 0.2741 -0.1778 0.0619 645 LEU B CA 12128 C C . LEU B 645 ? 1.9629 1.3943 1.9927 0.2549 -0.1515 0.0622 645 LEU B C 12129 O O . LEU B 645 ? 1.9632 1.4015 2.0047 0.2613 -0.1363 0.0578 645 LEU B O 12130 C CB . LEU B 645 ? 2.0674 1.6025 2.1683 0.2805 -0.1788 0.0459 645 LEU B CB 12131 C CG . LEU B 645 ? 2.0664 1.6487 2.1934 0.2923 -0.2059 0.0425 645 LEU B CG 12132 C CD1 . LEU B 645 ? 2.0036 1.6714 2.1871 0.3003 -0.2040 0.0211 645 LEU B CD1 12133 C CD2 . LEU B 645 ? 2.0094 1.5903 2.1146 0.2615 -0.2120 0.0478 645 LEU B CD2 12134 N N . LYS B 646 ? 1.9550 1.3549 1.9550 0.2318 -0.1476 0.0667 646 LYS B N 12135 C CA . LYS B 646 ? 1.9178 1.2976 1.9036 0.2103 -0.1278 0.0662 646 LYS B CA 12136 C C . LYS B 646 ? 1.9921 1.4047 1.9892 0.1818 -0.1267 0.0588 646 LYS B C 12137 O O . LYS B 646 ? 2.0096 1.4226 1.9989 0.1701 -0.1375 0.0575 646 LYS B O 12138 C CB . LYS B 646 ? 1.8745 1.1948 1.8208 0.2069 -0.1249 0.0726 646 LYS B CB 12139 C CG . LYS B 646 ? 1.8278 1.1199 1.7587 0.2291 -0.1241 0.0783 646 LYS B CG 12140 C CD . LYS B 646 ? 2.0112 1.2576 1.9075 0.2246 -0.1193 0.0799 646 LYS B CD 12141 C CE . LYS B 646 ? 2.2554 1.4840 2.1454 0.2141 -0.1045 0.0801 646 LYS B CE 12142 N NZ . LYS B 646 ? 2.3457 1.5350 2.2075 0.2160 -0.1022 0.0786 646 LYS B NZ 12143 N N . ASP B 647 ? 2.1216 1.5634 2.1339 0.1667 -0.1127 0.0529 647 ASP B N 12144 C CA . ASP B 647 ? 2.2183 1.7091 2.2471 0.1384 -0.1116 0.0426 647 ASP B CA 12145 C C . ASP B 647 ? 2.2869 1.7385 2.2828 0.1057 -0.1091 0.0447 647 ASP B C 12146 O O . ASP B 647 ? 2.2536 1.6424 2.2181 0.1091 -0.1097 0.0524 647 ASP B O 12147 C CB . ASP B 647 ? 2.1983 1.7315 2.2463 0.1252 -0.0953 0.0340 647 ASP B CB 12148 C CG . ASP B 647 ? 2.1237 1.6725 2.1940 0.1570 -0.0918 0.0317 647 ASP B CG 12149 O OD1 . ASP B 647 ? 2.0909 1.6914 2.1992 0.1812 -0.1022 0.0210 647 ASP B OD1 12150 O OD2 . ASP B 647 ? 2.0805 1.5890 2.1299 0.1586 -0.0796 0.0398 647 ASP B OD2 12151 N N . THR B 648 ? 2.3678 1.8593 2.3716 0.0738 -0.1063 0.0352 648 THR B N 12152 C CA . THR B 648 ? 2.4438 1.8974 2.4152 0.0382 -0.1033 0.0347 648 THR B CA 12153 C C . THR B 648 ? 2.4269 1.8033 2.3594 0.0286 -0.0925 0.0449 648 THR B C 12154 O O . THR B 648 ? 2.4603 1.7786 2.3605 0.0136 -0.0936 0.0464 648 THR B O 12155 C CB . THR B 648 ? 2.5023 2.0147 2.4850 -0.0009 -0.0984 0.0220 648 THR B CB 12156 O OG1 . THR B 648 ? 2.6099 2.0696 2.5523 -0.0389 -0.0934 0.0225 648 THR B OG1 12157 C CG2 . THR B 648 ? 2.4874 2.0429 2.4866 -0.0113 -0.0845 0.0171 648 THR B CG2 12158 N N . GLY B 649 ? 2.3690 1.7454 2.3052 0.0386 -0.0833 0.0508 649 GLY B N 12159 C CA . GLY B 649 ? 2.4413 1.7483 2.3426 0.0357 -0.0764 0.0630 649 GLY B CA 12160 C C . GLY B 649 ? 2.5380 1.8385 2.4185 -0.0037 -0.0653 0.0661 649 GLY B C 12161 O O . GLY B 649 ? 2.5957 1.9242 2.4743 -0.0398 -0.0626 0.0578 649 GLY B O 12162 N N . LYS B 650 ? 2.4842 1.7471 2.3450 0.0006 -0.0595 0.0784 650 LYS B N 12163 C CA . LYS B 650 ? 2.3866 1.6294 2.2168 -0.0373 -0.0509 0.0865 650 LYS B CA 12164 C C . LYS B 650 ? 2.3064 1.4651 2.1007 -0.0215 -0.0559 0.1041 650 LYS B C 12165 O O . LYS B 650 ? 2.2829 1.4075 2.0782 0.0116 -0.0648 0.1045 650 LYS B O 12166 C CB . LYS B 650 ? 2.3673 1.6838 2.2230 -0.0468 -0.0375 0.0803 650 LYS B CB 12167 C CG . LYS B 650 ? 2.3840 1.7979 2.2904 -0.0446 -0.0351 0.0587 650 LYS B CG 12168 C CD . LYS B 650 ? 2.4340 1.8758 2.3332 -0.0897 -0.0337 0.0481 650 LYS B CD 12169 C CE . LYS B 650 ? 2.3798 1.9217 2.3338 -0.0796 -0.0359 0.0258 650 LYS B CE 12170 N NZ . LYS B 650 ? 2.4325 2.0090 2.3803 -0.1245 -0.0348 0.0136 650 LYS B NZ 12171 N N . ASP B 651 ? 2.3271 1.4541 2.0885 -0.0457 -0.0517 0.1177 651 ASP B N 12172 C CA . ASP B 651 ? 2.3556 1.4170 2.0909 -0.0229 -0.0584 0.1343 651 ASP B CA 12173 C C . ASP B 651 ? 2.3636 1.4687 2.1346 0.0185 -0.0539 0.1302 651 ASP B C 12174 O O . ASP B 651 ? 2.3353 1.5029 2.1308 0.0155 -0.0422 0.1251 651 ASP B O 12175 C CB . ASP B 651 ? 2.3717 1.3988 2.0649 -0.0571 -0.0562 0.1521 651 ASP B CB 12176 C CG . ASP B 651 ? 2.3912 1.4977 2.1027 -0.0831 -0.0393 0.1466 651 ASP B CG 12177 O OD1 . ASP B 651 ? 2.3938 1.4936 2.0858 -0.0928 -0.0351 0.1596 651 ASP B OD1 12178 O OD2 . ASP B 651 ? 2.3879 1.5677 2.1346 -0.0934 -0.0308 0.1274 651 ASP B OD2 12179 N N . ALA B 652 ? 2.3592 1.4322 2.1320 0.0553 -0.0628 0.1300 652 ALA B N 12180 C CA . ALA B 652 ? 2.2146 1.3249 2.0164 0.0910 -0.0595 0.1244 652 ALA B CA 12181 C C . ALA B 652 ? 2.2396 1.3048 2.0289 0.1229 -0.0684 0.1268 652 ALA B C 12182 O O . ALA B 652 ? 2.4487 1.4600 2.2164 0.1235 -0.0787 0.1274 652 ALA B O 12183 C CB . ALA B 652 ? 2.0244 1.1900 1.8622 0.0984 -0.0593 0.1089 652 ALA B CB 12184 N N . VAL B 653 ? 1.9987 1.0880 1.8016 0.1487 -0.0640 0.1253 653 VAL B N 12185 C CA . VAL B 653 ? 1.9537 1.0176 1.7490 0.1775 -0.0706 0.1226 653 VAL B CA 12186 C C . VAL B 653 ? 1.9945 1.0945 1.8112 0.1958 -0.0692 0.1110 653 VAL B C 12187 O O . VAL B 653 ? 1.9889 1.1239 1.8197 0.2021 -0.0612 0.1110 653 VAL B O 12188 C CB . VAL B 653 ? 1.9539 1.0050 1.7339 0.1883 -0.0680 0.1334 653 VAL B CB 12189 C CG1 . VAL B 653 ? 1.9818 1.0186 1.7569 0.2172 -0.0742 0.1261 653 VAL B CG1 12190 C CG2 . VAL B 653 ? 2.1234 1.1311 1.8753 0.1689 -0.0734 0.1487 653 VAL B CG2 12191 N N . ASN B 654 ? 2.0834 1.1716 1.8992 0.2025 -0.0777 0.1008 654 ASN B N 12192 C CA . ASN B 654 ? 1.9045 1.0196 1.7318 0.2148 -0.0796 0.0921 654 ASN B CA 12193 C C . ASN B 654 ? 1.7437 0.8501 1.5579 0.2342 -0.0793 0.0878 654 ASN B C 12194 O O . ASN B 654 ? 2.0223 1.1052 1.8243 0.2403 -0.0845 0.0797 654 ASN B O 12195 C CB . ASN B 654 ? 2.0556 1.1704 1.8860 0.2056 -0.0887 0.0824 654 ASN B CB 12196 C CG . ASN B 654 ? 2.1380 1.2626 1.9780 0.1822 -0.0888 0.0843 654 ASN B CG 12197 O OD1 . ASN B 654 ? 2.0407 1.2065 1.9018 0.1771 -0.0884 0.0838 654 ASN B OD1 12198 N ND2 . ASN B 654 ? 2.1688 1.2552 1.9923 0.1677 -0.0903 0.0850 654 ASN B ND2 12199 N N . CYS B 655 ? 1.5951 0.7228 1.4120 0.2432 -0.0727 0.0906 655 CYS B N 12200 C CA . CYS B 655 ? 1.6147 0.7400 1.4161 0.2566 -0.0701 0.0861 655 CYS B CA 12201 C C . CYS B 655 ? 1.5320 0.6713 1.3286 0.2598 -0.0719 0.0804 655 CYS B C 12202 O O . CYS B 655 ? 1.6549 0.8077 1.4623 0.2591 -0.0720 0.0848 655 CYS B O 12203 C CB . CYS B 655 ? 1.5919 0.7225 1.3898 0.2605 -0.0598 0.0949 655 CYS B CB 12204 S SG . CYS B 655 ? 2.2628 1.3657 2.0502 0.2601 -0.0625 0.1032 655 CYS B SG 12205 N N . THR B 656 ? 1.4513 0.5871 1.2302 0.2626 -0.0745 0.0695 656 THR B N 12206 C CA . THR B 656 ? 1.4282 0.5708 1.1908 0.2598 -0.0770 0.0651 656 THR B CA 12207 C C . THR B 656 ? 1.3574 0.5056 1.0982 0.2631 -0.0694 0.0571 656 THR B C 12208 O O . THR B 656 ? 1.3570 0.5075 1.0991 0.2705 -0.0656 0.0519 656 THR B O 12209 C CB . THR B 656 ? 1.3728 0.5146 1.1294 0.2497 -0.0882 0.0559 656 THR B CB 12210 O OG1 . THR B 656 ? 1.3802 0.5207 1.1308 0.2500 -0.0879 0.0398 656 THR B OG1 12211 C CG2 . THR B 656 ? 1.3771 0.5196 1.1554 0.2443 -0.0957 0.0621 656 THR B CG2 12212 N N . TYR B 657 ? 1.3607 0.5104 1.0791 0.2566 -0.0689 0.0560 657 TYR B N 12213 C CA . TYR B 657 ? 1.3605 0.5203 1.0535 0.2536 -0.0603 0.0471 657 TYR B CA 12214 C C . TYR B 657 ? 1.3771 0.5271 1.0378 0.2395 -0.0629 0.0480 657 TYR B C 12215 O O . TYR B 657 ? 1.3882 0.5204 1.0500 0.2385 -0.0721 0.0590 657 TYR B O 12216 C CB . TYR B 657 ? 1.4434 0.6094 1.1428 0.2627 -0.0481 0.0537 657 TYR B CB 12217 C CG . TYR B 657 ? 1.3479 0.5042 1.0477 0.2626 -0.0431 0.0658 657 TYR B CG 12218 C CD1 . TYR B 657 ? 1.5209 0.6739 1.1929 0.2556 -0.0355 0.0639 657 TYR B CD1 12219 C CD2 . TYR B 657 ? 1.3436 0.4956 1.0713 0.2685 -0.0457 0.0760 657 TYR B CD2 12220 C CE1 . TYR B 657 ? 1.6663 0.8057 1.3395 0.2580 -0.0313 0.0716 657 TYR B CE1 12221 C CE2 . TYR B 657 ? 1.5419 0.6903 1.2752 0.2716 -0.0411 0.0816 657 TYR B CE2 12222 C CZ . TYR B 657 ? 1.6184 0.7574 1.3250 0.2682 -0.0344 0.0792 657 TYR B CZ 12223 O OH . TYR B 657 ? 1.3637 0.4944 1.0766 0.2738 -0.0303 0.0818 657 TYR B OH 12224 N N . LYS B 658 ? 1.3842 0.5456 1.0140 0.2281 -0.0562 0.0361 658 LYS B N 12225 C CA . LYS B 658 ? 1.4211 0.5665 1.0087 0.2084 -0.0589 0.0372 658 LYS B CA 12226 C C . LYS B 658 ? 1.4250 0.5625 0.9944 0.2073 -0.0466 0.0417 658 LYS B C 12227 O O . LYS B 658 ? 1.3983 0.5612 0.9719 0.2111 -0.0335 0.0339 658 LYS B O 12228 C CB . LYS B 658 ? 1.4835 0.6501 1.0411 0.1867 -0.0593 0.0173 658 LYS B CB 12229 C CG . LYS B 658 ? 1.6020 0.7442 1.1125 0.1597 -0.0693 0.0215 658 LYS B CG 12230 C CD . LYS B 658 ? 1.6900 0.8625 1.1688 0.1319 -0.0670 -0.0019 658 LYS B CD 12231 C CE . LYS B 658 ? 1.7927 0.9984 1.2546 0.1240 -0.0497 -0.0196 658 LYS B CE 12232 N NZ . LYS B 658 ? 1.9072 1.1513 1.3366 0.0929 -0.0462 -0.0467 658 LYS B NZ 12233 N N . ASN B 659 ? 1.4419 0.5432 0.9907 0.2027 -0.0521 0.0539 659 ASN B N 12234 C CA . ASN B 659 ? 1.4743 0.5604 1.0043 0.2010 -0.0404 0.0569 659 ASN B CA 12235 C C . ASN B 659 ? 1.5543 0.6306 1.0250 0.1718 -0.0357 0.0487 659 ASN B C 12236 O O . ASN B 659 ? 1.5910 0.6815 1.0370 0.1518 -0.0399 0.0383 659 ASN B O 12237 C CB . ASN B 659 ? 1.6302 0.6787 1.1718 0.2154 -0.0490 0.0713 659 ASN B CB 12238 C CG . ASN B 659 ? 1.8617 0.8734 1.3803 0.2091 -0.0714 0.0802 659 ASN B CG 12239 O OD1 . ASN B 659 ? 2.0202 1.0281 1.5015 0.1862 -0.0783 0.0765 659 ASN B OD1 12240 N ND2 . ASN B 659 ? 1.8186 0.8068 1.3596 0.2288 -0.0837 0.0908 659 ASN B ND2 12241 N N . GLU B 660 ? 1.5884 0.6418 1.0345 0.1662 -0.0260 0.0513 660 GLU B N 12242 C CA . GLU B 660 ? 1.6673 0.7041 1.0496 0.1335 -0.0205 0.0445 660 GLU B CA 12243 C C . GLU B 660 ? 1.7230 0.7124 1.0599 0.1135 -0.0405 0.0529 660 GLU B C 12244 O O . GLU B 660 ? 1.9746 0.9586 1.2542 0.0780 -0.0393 0.0453 660 GLU B O 12245 C CB . GLU B 660 ? 1.7289 0.7396 1.0937 0.1322 -0.0072 0.0468 660 GLU B CB 12246 C CG . GLU B 660 ? 1.8669 0.9229 1.2712 0.1481 0.0120 0.0408 660 GLU B CG 12247 C CD . GLU B 660 ? 2.0489 1.0781 1.4388 0.1465 0.0253 0.0420 660 GLU B CD 12248 O OE1 . GLU B 660 ? 2.1890 1.1578 1.5408 0.1374 0.0182 0.0473 660 GLU B OE1 12249 O OE2 . GLU B 660 ? 2.0117 1.0776 1.4265 0.1538 0.0417 0.0374 660 GLU B OE2 12250 N N . ASP B 661 ? 1.7167 0.6750 1.0779 0.1344 -0.0596 0.0683 661 ASP B N 12251 C CA . ASP B 661 ? 1.8847 0.7933 1.2051 0.1197 -0.0836 0.0809 661 ASP B CA 12252 C C . ASP B 661 ? 1.9158 0.8565 1.2413 0.1079 -0.0938 0.0760 661 ASP B C 12253 O O . ASP B 661 ? 2.1177 1.0262 1.4148 0.0953 -0.1157 0.0873 661 ASP B O 12254 C CB . ASP B 661 ? 1.9778 0.8415 1.3235 0.1506 -0.1017 0.0983 661 ASP B CB 12255 C CG . ASP B 661 ? 2.0561 0.8877 1.3997 0.1638 -0.0912 0.0988 661 ASP B CG 12256 O OD1 . ASP B 661 ? 2.0586 0.8768 1.3551 0.1390 -0.0765 0.0918 661 ASP B OD1 12257 O OD2 . ASP B 661 ? 2.1068 0.9307 1.4960 0.1972 -0.0967 0.1037 661 ASP B OD2 12258 N N . ASP B 662 ? 1.7149 0.7173 1.0767 0.1129 -0.0791 0.0590 662 ASP B N 12259 C CA . ASP B 662 ? 1.6758 0.7146 1.0489 0.1038 -0.0850 0.0480 662 ASP B CA 12260 C C . ASP B 662 ? 1.6020 0.6272 1.0098 0.1231 -0.1044 0.0623 662 ASP B C 12261 O O . ASP B 662 ? 1.6106 0.6429 1.0080 0.1075 -0.1169 0.0601 662 ASP B O 12262 C CB . ASP B 662 ? 1.7791 0.8159 1.0866 0.0591 -0.0889 0.0388 662 ASP B CB 12263 C CG . ASP B 662 ? 1.9879 1.0520 1.2615 0.0354 -0.0681 0.0197 662 ASP B CG 12264 O OD1 . ASP B 662 ? 2.0746 1.1857 1.3871 0.0539 -0.0511 0.0050 662 ASP B OD1 12265 O OD2 . ASP B 662 ? 2.1089 1.1473 1.3143 -0.0034 -0.0701 0.0199 662 ASP B OD2 12266 N N . CYS B 663 ? 1.5624 0.5742 1.0115 0.1548 -0.1060 0.0748 663 CYS B N 12267 C CA . CYS B 663 ? 1.5535 0.5634 1.0424 0.1745 -0.1223 0.0858 663 CYS B CA 12268 C C . CYS B 663 ? 1.4990 0.5495 1.0470 0.1958 -0.1103 0.0782 663 CYS B C 12269 O O . CYS B 663 ? 1.4731 0.5378 1.0377 0.2064 -0.0929 0.0731 663 CYS B O 12270 C CB . CYS B 663 ? 1.6599 0.6275 1.1519 0.1936 -0.1360 0.1031 663 CYS B CB 12271 S SG . CYS B 663 ? 1.8062 0.7058 1.2209 0.1707 -0.1554 0.1166 663 CYS B SG 12272 N N . VAL B 664 ? 1.4875 0.5538 1.0629 0.1993 -0.1204 0.0782 664 VAL B N 12273 C CA . VAL B 664 ? 1.6162 0.7122 1.2385 0.2139 -0.1108 0.0714 664 VAL B CA 12274 C C . VAL B 664 ? 1.4343 0.5301 1.0980 0.2357 -0.1132 0.0826 664 VAL B C 12275 O O . VAL B 664 ? 1.4450 0.5387 1.1224 0.2396 -0.1290 0.0903 664 VAL B O 12276 C CB . VAL B 664 ? 1.4456 0.5596 1.0747 0.2028 -0.1176 0.0614 664 VAL B CB 12277 C CG1 . VAL B 664 ? 1.4166 0.5481 1.0885 0.2170 -0.1099 0.0562 664 VAL B CG1 12278 C CG2 . VAL B 664 ? 1.4572 0.5832 1.0507 0.1805 -0.1129 0.0437 664 VAL B CG2 12279 N N . VAL B 665 ? 1.4120 0.5163 1.0956 0.2480 -0.0976 0.0819 665 VAL B N 12280 C CA . VAL B 665 ? 1.4244 0.5371 1.1467 0.2645 -0.0959 0.0883 665 VAL B CA 12281 C C . VAL B 665 ? 1.3959 0.5310 1.1509 0.2653 -0.0924 0.0858 665 VAL B C 12282 O O . VAL B 665 ? 1.3802 0.5209 1.1348 0.2632 -0.0816 0.0808 665 VAL B O 12283 C CB . VAL B 665 ? 1.3919 0.5030 1.1151 0.2725 -0.0800 0.0885 665 VAL B CB 12284 C CG1 . VAL B 665 ? 1.3786 0.5081 1.1438 0.2858 -0.0761 0.0906 665 VAL B CG1 12285 C CG2 . VAL B 665 ? 1.7638 0.8440 1.4505 0.2700 -0.0834 0.0907 665 VAL B CG2 12286 N N . ARG B 666 ? 1.4818 0.6283 1.2628 0.2679 -0.1029 0.0890 666 ARG B N 12287 C CA . ARG B 666 ? 1.4798 0.6431 1.2866 0.2634 -0.0999 0.0869 666 ARG B CA 12288 C C . ARG B 666 ? 1.4067 0.5909 1.2458 0.2701 -0.0927 0.0895 666 ARG B C 12289 O O . ARG B 666 ? 1.4736 0.6697 1.3292 0.2803 -0.0987 0.0904 666 ARG B O 12290 C CB . ARG B 666 ? 1.6344 0.8039 1.4453 0.2541 -0.1150 0.0853 666 ARG B CB 12291 C CG . ARG B 666 ? 1.7314 0.8863 1.5092 0.2451 -0.1255 0.0827 666 ARG B CG 12292 C CD . ARG B 666 ? 1.7453 0.9101 1.5263 0.2314 -0.1376 0.0788 666 ARG B CD 12293 N NE . ARG B 666 ? 1.8205 0.9847 1.6049 0.2228 -0.1288 0.0676 666 ARG B NE 12294 C CZ . ARG B 666 ? 1.8223 0.9792 1.5851 0.2138 -0.1268 0.0548 666 ARG B CZ 12295 N NH1 . ARG B 666 ? 1.7579 0.9119 1.4909 0.2066 -0.1314 0.0522 666 ARG B NH1 12296 N NH2 . ARG B 666 ? 1.7673 0.9192 1.5367 0.2111 -0.1207 0.0430 666 ARG B NH2 12297 N N . PHE B 667 ? 1.3520 0.5411 1.1989 0.2640 -0.0807 0.0895 667 PHE B N 12298 C CA . PHE B 667 ? 1.3506 0.5648 1.2243 0.2626 -0.0720 0.0902 667 PHE B CA 12299 C C . PHE B 667 ? 1.3475 0.5606 1.2232 0.2463 -0.0668 0.0923 667 PHE B C 12300 O O . PHE B 667 ? 1.7361 0.9263 1.5965 0.2401 -0.0720 0.0922 667 PHE B O 12301 C CB . PHE B 667 ? 1.3735 0.5900 1.2446 0.2707 -0.0587 0.0904 667 PHE B CB 12302 C CG . PHE B 667 ? 1.3315 0.5305 1.1786 0.2668 -0.0485 0.0939 667 PHE B CG 12303 C CD1 . PHE B 667 ? 1.3317 0.5376 1.1823 0.2568 -0.0385 0.0983 667 PHE B CD1 12304 C CD2 . PHE B 667 ? 1.4482 0.6272 1.2677 0.2715 -0.0501 0.0926 667 PHE B CD2 12305 C CE1 . PHE B 667 ? 1.3338 0.5250 1.1629 0.2561 -0.0329 0.1029 667 PHE B CE1 12306 C CE2 . PHE B 667 ? 1.4357 0.6079 1.2373 0.2704 -0.0422 0.0935 667 PHE B CE2 12307 C CZ . PHE B 667 ? 1.3314 0.5088 1.1389 0.2650 -0.0348 0.0995 667 PHE B CZ 12308 N N . GLN B 668 ? 1.3459 0.5817 1.2380 0.2379 -0.0567 0.0930 668 GLN B N 12309 C CA . GLN B 668 ? 1.5378 0.7686 1.4257 0.2166 -0.0527 0.0973 668 GLN B CA 12310 C C . GLN B 668 ? 1.5068 0.7705 1.4095 0.2045 -0.0395 0.0965 668 GLN B C 12311 O O . GLN B 668 ? 1.5897 0.8885 1.5161 0.2144 -0.0347 0.0880 668 GLN B O 12312 C CB . GLN B 668 ? 1.6861 0.9210 1.5813 0.2030 -0.0625 0.0936 668 GLN B CB 12313 C CG . GLN B 668 ? 1.6359 0.9204 1.5642 0.2038 -0.0659 0.0848 668 GLN B CG 12314 C CD . GLN B 668 ? 1.6419 0.9385 1.5767 0.1847 -0.0737 0.0807 668 GLN B CD 12315 O OE1 . GLN B 668 ? 1.7100 0.9755 1.6236 0.1657 -0.0734 0.0842 668 GLN B OE1 12316 N NE2 . GLN B 668 ? 1.5512 0.8917 1.5143 0.1903 -0.0821 0.0725 668 GLN B NE2 12317 N N . TYR B 669 ? 1.5567 0.8076 1.4438 0.1821 -0.0346 0.1042 669 TYR B N 12318 C CA . TYR B 669 ? 1.6674 0.9513 1.5622 0.1626 -0.0210 0.1033 669 TYR B CA 12319 C C . TYR B 669 ? 1.8937 1.1723 1.7754 0.1276 -0.0211 0.1082 669 TYR B C 12320 O O . TYR B 669 ? 1.9136 1.1408 1.7664 0.1197 -0.0301 0.1190 669 TYR B O 12321 C CB . TYR B 669 ? 1.6032 0.8737 1.4790 0.1662 -0.0119 0.1116 669 TYR B CB 12322 C CG . TYR B 669 ? 1.5970 0.8126 1.4367 0.1656 -0.0198 0.1271 669 TYR B CG 12323 C CD1 . TYR B 669 ? 1.8967 1.0891 1.7113 0.1396 -0.0209 0.1402 669 TYR B CD1 12324 C CD2 . TYR B 669 ? 1.5441 0.7316 1.3734 0.1908 -0.0276 0.1276 669 TYR B CD2 12325 C CE1 . TYR B 669 ? 2.0227 1.1610 1.8057 0.1446 -0.0321 0.1541 669 TYR B CE1 12326 C CE2 . TYR B 669 ? 1.5863 0.7309 1.3887 0.1951 -0.0362 0.1374 669 TYR B CE2 12327 C CZ . TYR B 669 ? 1.8574 0.9753 1.6381 0.1750 -0.0397 0.1510 669 TYR B CZ 12328 O OH . TYR B 669 ? 1.8861 0.9570 1.6412 0.1846 -0.0522 0.1605 669 TYR B OH 12329 N N . TYR B 670 ? 1.9984 1.3303 1.9005 0.1057 -0.0112 0.0980 670 TYR B N 12330 C CA . TYR B 670 ? 2.0585 1.3904 1.9424 0.0637 -0.0086 0.1018 670 TYR B CA 12331 C C . TYR B 670 ? 2.1169 1.4219 1.9651 0.0414 -0.0019 0.1175 670 TYR B C 12332 O O . TYR B 670 ? 2.0645 1.3873 1.9176 0.0515 0.0075 0.1173 670 TYR B O 12333 C CB . TYR B 670 ? 2.0581 1.4692 1.9780 0.0450 0.0005 0.0812 670 TYR B CB 12334 C CG . TYR B 670 ? 2.0959 1.5286 2.0391 0.0504 -0.0099 0.0700 670 TYR B CG 12335 C CD1 . TYR B 670 ? 2.1936 1.5702 2.1141 0.0533 -0.0238 0.0800 670 TYR B CD1 12336 C CD2 . TYR B 670 ? 2.1069 1.6203 2.0965 0.0531 -0.0066 0.0474 670 TYR B CD2 12337 C CE1 . TYR B 670 ? 2.2469 1.6463 2.1864 0.0547 -0.0331 0.0698 670 TYR B CE1 12338 C CE2 . TYR B 670 ? 2.1681 1.7059 2.1786 0.0578 -0.0183 0.0382 670 TYR B CE2 12339 C CZ . TYR B 670 ? 2.1959 1.6761 2.1794 0.0565 -0.0310 0.0505 670 TYR B CZ 12340 O OH . TYR B 670 ? 2.1128 1.6202 2.1150 0.0579 -0.0424 0.0414 670 TYR B OH 12341 N N . GLU B 671 ? 2.2901 1.5492 2.0990 0.0094 -0.0080 0.1317 671 GLU B N 12342 C CA . GLU B 671 ? 2.3846 1.6167 2.1536 -0.0186 -0.0050 0.1494 671 GLU B CA 12343 C C . GLU B 671 ? 2.3720 1.6728 2.1504 -0.0606 0.0122 0.1374 671 GLU B C 12344 O O . GLU B 671 ? 2.3220 1.6939 2.1448 -0.0577 0.0212 0.1135 671 GLU B O 12345 C CB . GLU B 671 ? 2.4805 1.6261 2.1983 -0.0358 -0.0216 0.1702 671 GLU B CB 12346 C CG . GLU B 671 ? 2.5160 1.6100 2.1882 -0.0454 -0.0279 0.1949 671 GLU B CG 12347 C CD . GLU B 671 ? 2.4576 1.5656 2.1448 -0.0077 -0.0250 0.1963 671 GLU B CD 12348 O OE1 . GLU B 671 ? 2.4100 1.5039 2.1150 0.0343 -0.0321 0.1908 671 GLU B OE1 12349 O OE2 . GLU B 671 ? 2.4383 1.5744 2.1173 -0.0238 -0.0147 0.2016 671 GLU B OE2 12350 N N . ASP B 672 ? 2.4631 1.7463 2.2001 -0.0998 0.0156 0.1527 672 ASP B N 12351 C CA . ASP B 672 ? 2.5403 1.8965 2.2842 -0.1433 0.0345 0.1389 672 ASP B CA 12352 C C . ASP B 672 ? 2.7099 2.1106 2.4653 -0.1789 0.0394 0.1210 672 ASP B C 12353 O O . ASP B 672 ? 2.7944 2.1422 2.5098 -0.2088 0.0290 0.1339 672 ASP B O 12354 C CB . ASP B 672 ? 2.5552 1.8740 2.2407 -0.1849 0.0342 0.1631 672 ASP B CB 12355 C CG . ASP B 672 ? 2.6383 1.8589 2.2619 -0.2079 0.0136 0.1911 672 ASP B CG 12356 O OD1 . ASP B 672 ? 2.6848 1.8512 2.3107 -0.1758 -0.0020 0.1952 672 ASP B OD1 12357 O OD2 . ASP B 672 ? 2.6466 1.8418 2.2170 -0.2595 0.0124 0.2083 672 ASP B OD2 12358 N N . SER B 673 ? 2.8202 2.3193 2.6313 -0.1745 0.0546 0.0894 673 SER B N 12359 C CA . SER B 673 ? 3.0399 2.6106 2.8640 -0.2190 0.0650 0.0670 673 SER B CA 12360 C C . SER B 673 ? 3.2101 2.8637 3.0491 -0.2473 0.0871 0.0477 673 SER B C 12361 O O . SER B 673 ? 3.2224 2.9425 3.1171 -0.2127 0.0972 0.0230 673 SER B O 12362 C CB . SER B 673 ? 3.0832 2.7093 2.9663 -0.1865 0.0614 0.0416 673 SER B CB 12363 O OG . SER B 673 ? 3.1290 2.8485 3.0365 -0.2253 0.0738 0.0132 673 SER B OG 12364 N N . SER B 674 ? 3.3660 3.0113 3.1520 -0.3113 0.0940 0.0587 674 SER B N 12365 C CA . SER B 674 ? 3.3685 3.0740 3.1507 -0.3455 0.1141 0.0478 674 SER B CA 12366 C C . SER B 674 ? 3.2655 2.9285 3.0408 -0.3085 0.1121 0.0657 674 SER B C 12367 O O . SER B 674 ? 3.2810 2.9783 3.0457 -0.3336 0.1268 0.0623 674 SER B O 12368 C CB . SER B 674 ? 3.3567 3.1972 3.2097 -0.3462 0.1354 -0.0011 674 SER B CB 12369 O OG . SER B 674 ? 3.3223 3.1885 3.2403 -0.2750 0.1339 -0.0189 674 SER B OG 12370 N N . GLY B 675 ? 3.1561 2.7489 2.9365 -0.2521 0.0944 0.0829 675 GLY B N 12371 C CA . GLY B 675 ? 3.0649 2.6177 2.8434 -0.2098 0.0903 0.0976 675 GLY B CA 12372 C C . GLY B 675 ? 2.9609 2.5707 2.8062 -0.1572 0.0994 0.0691 675 GLY B C 12373 O O . GLY B 675 ? 3.0491 2.7487 2.9395 -0.1639 0.1164 0.0354 675 GLY B O 12374 N N . LYS B 676 ? 2.7957 2.3514 2.6443 -0.1062 0.0874 0.0819 676 LYS B N 12375 C CA . LYS B 676 ? 2.6152 2.1999 2.5119 -0.0556 0.0924 0.0623 676 LYS B CA 12376 C C . LYS B 676 ? 2.5347 2.0442 2.4175 -0.0114 0.0751 0.0825 676 LYS B C 12377 O O . LYS B 676 ? 2.5799 2.0253 2.4296 -0.0136 0.0585 0.1051 676 LYS B O 12378 C CB . LYS B 676 ? 2.5187 2.1703 2.4741 -0.0382 0.0953 0.0298 676 LYS B CB 12379 C CG . LYS B 676 ? 2.5232 2.1578 2.4795 -0.0403 0.0797 0.0338 676 LYS B CG 12380 C CD . LYS B 676 ? 2.4560 2.1722 2.4729 -0.0257 0.0827 -0.0003 676 LYS B CD 12381 C CE . LYS B 676 ? 2.3805 2.1910 2.4229 -0.0588 0.1046 -0.0302 676 LYS B CE 12382 N NZ . LYS B 676 ? 2.3327 2.2309 2.4424 -0.0361 0.1061 -0.0681 676 LYS B NZ 12383 N N . SER B 677 ? 2.4382 1.9570 2.3457 0.0268 0.0795 0.0718 677 SER B N 12384 C CA . SER B 677 ? 2.3922 1.8525 2.2881 0.0658 0.0662 0.0858 677 SER B CA 12385 C C . SER B 677 ? 2.3335 1.7908 2.2603 0.1011 0.0545 0.0748 677 SER B C 12386 O O . SER B 677 ? 2.4929 1.9110 2.4127 0.1318 0.0453 0.0814 677 SER B O 12387 C CB . SER B 677 ? 2.4072 1.8718 2.2999 0.0804 0.0776 0.0832 677 SER B CB 12388 O OG . SER B 677 ? 2.3948 1.8500 2.2502 0.0505 0.0832 0.1000 677 SER B OG 12389 N N . ILE B 678 ? 2.1701 1.6725 2.1290 0.0941 0.0544 0.0576 678 ILE B N 12390 C CA . ILE B 678 ? 2.0148 1.5323 2.0107 0.1276 0.0441 0.0429 678 ILE B CA 12391 C C . ILE B 678 ? 1.8558 1.3110 1.8330 0.1530 0.0254 0.0589 678 ILE B C 12392 O O . ILE B 678 ? 1.8658 1.2781 1.8132 0.1399 0.0164 0.0759 678 ILE B O 12393 C CB . ILE B 678 ? 2.1001 1.6730 2.1257 0.1097 0.0426 0.0267 678 ILE B CB 12394 C CG1 . ILE B 678 ? 2.0556 1.6429 2.1174 0.1455 0.0274 0.0145 678 ILE B CG1 12395 C CG2 . ILE B 678 ? 2.1877 1.7299 2.1780 0.0732 0.0369 0.0441 678 ILE B CG2 12396 C CD1 . ILE B 678 ? 2.0291 1.6441 2.1266 0.1817 0.0301 -0.0050 678 ILE B CD1 12397 N N . LEU B 679 ? 1.7073 1.1567 1.7004 0.1880 0.0195 0.0518 679 LEU B N 12398 C CA . LEU B 679 ? 1.5675 0.9632 1.5398 0.2098 0.0043 0.0642 679 LEU B CA 12399 C C . LEU B 679 ? 1.4877 0.8929 1.4857 0.2364 -0.0100 0.0543 679 LEU B C 12400 O O . LEU B 679 ? 1.5032 0.9358 1.5281 0.2548 -0.0076 0.0393 679 LEU B O 12401 C CB . LEU B 679 ? 1.4982 0.8615 1.4444 0.2204 0.0110 0.0715 679 LEU B CB 12402 C CG . LEU B 679 ? 1.4386 0.7552 1.3613 0.2405 -0.0009 0.0797 679 LEU B CG 12403 C CD1 . LEU B 679 ? 1.6328 0.9151 1.5305 0.2311 -0.0105 0.0931 679 LEU B CD1 12404 C CD2 . LEU B 679 ? 1.4090 0.7122 1.3128 0.2483 0.0095 0.0800 679 LEU B CD2 12405 N N . TYR B 680 ? 1.4325 0.8131 1.4207 0.2388 -0.0262 0.0622 680 TYR B N 12406 C CA . TYR B 680 ? 1.4013 0.7878 1.4076 0.2608 -0.0436 0.0566 680 TYR B CA 12407 C C . TYR B 680 ? 1.3629 0.6963 1.3375 0.2754 -0.0552 0.0675 680 TYR B C 12408 O O . TYR B 680 ? 1.5212 0.8237 1.4694 0.2647 -0.0588 0.0770 680 TYR B O 12409 C CB . TYR B 680 ? 1.4745 0.8878 1.4968 0.2469 -0.0536 0.0538 680 TYR B CB 12410 C CG . TYR B 680 ? 1.5645 1.0407 1.6188 0.2286 -0.0431 0.0394 680 TYR B CG 12411 C CD1 . TYR B 680 ? 1.6254 1.1594 1.7244 0.2460 -0.0457 0.0198 680 TYR B CD1 12412 C CD2 . TYR B 680 ? 1.6007 1.0786 1.6388 0.1931 -0.0317 0.0439 680 TYR B CD2 12413 C CE1 . TYR B 680 ? 1.7391 1.3422 1.8695 0.2267 -0.0346 0.0017 680 TYR B CE1 12414 C CE2 . TYR B 680 ? 1.6727 1.2115 1.7345 0.1690 -0.0210 0.0294 680 TYR B CE2 12415 C CZ . TYR B 680 ? 1.8047 1.4117 1.9145 0.1851 -0.0212 0.0066 680 TYR B CZ 12416 O OH . TYR B 680 ? 1.9785 1.6576 2.1144 0.1588 -0.0089 -0.0126 680 TYR B OH 12417 N N . VAL B 681 ? 1.4601 0.7827 1.4361 0.2985 -0.0613 0.0641 681 VAL B N 12418 C CA . VAL B 681 ? 1.3434 0.6180 1.2845 0.3072 -0.0726 0.0732 681 VAL B CA 12419 C C . VAL B 681 ? 1.4105 0.6828 1.3591 0.3213 -0.0964 0.0739 681 VAL B C 12420 O O . VAL B 681 ? 1.6911 0.9817 1.6666 0.3411 -0.1046 0.0660 681 VAL B O 12421 C CB . VAL B 681 ? 1.3486 0.5979 1.2699 0.3170 -0.0629 0.0723 681 VAL B CB 12422 C CG1 . VAL B 681 ? 1.3681 0.5709 1.2506 0.3218 -0.0761 0.0799 681 VAL B CG1 12423 C CG2 . VAL B 681 ? 1.5167 0.7667 1.4238 0.3016 -0.0422 0.0744 681 VAL B CG2 12424 N N . VAL B 682 ? 1.3670 0.6181 1.2919 0.3118 -0.1087 0.0821 682 VAL B N 12425 C CA . VAL B 682 ? 1.3877 0.6349 1.3123 0.3204 -0.1334 0.0857 682 VAL B CA 12426 C C . VAL B 682 ? 1.5024 0.7101 1.4029 0.3376 -0.1452 0.0905 682 VAL B C 12427 O O . VAL B 682 ? 1.5195 0.6889 1.3803 0.3304 -0.1385 0.0952 682 VAL B O 12428 C CB . VAL B 682 ? 1.4457 0.6793 1.3452 0.3009 -0.1415 0.0915 682 VAL B CB 12429 C CG1 . VAL B 682 ? 1.4156 0.6485 1.3119 0.3060 -0.1682 0.0967 682 VAL B CG1 12430 C CG2 . VAL B 682 ? 1.5185 0.7787 1.4355 0.2827 -0.1309 0.0868 682 VAL B CG2 12431 N N . GLU B 683 ? 1.5793 0.7961 1.5024 0.3601 -0.1639 0.0885 683 GLU B N 12432 C CA . GLU B 683 ? 1.5089 0.6767 1.4042 0.3772 -0.1808 0.0951 683 GLU B CA 12433 C C . GLU B 683 ? 1.6395 0.7696 1.4877 0.3621 -0.2007 0.1102 683 GLU B C 12434 O O . GLU B 683 ? 1.8876 1.0403 1.7384 0.3457 -0.2057 0.1125 683 GLU B O 12435 C CB . GLU B 683 ? 1.5399 0.7262 1.4751 0.4103 -0.1998 0.0878 683 GLU B CB 12436 C CG . GLU B 683 ? 1.6639 0.8831 1.6221 0.4156 -0.2259 0.0911 683 GLU B CG 12437 C CD . GLU B 683 ? 1.9147 1.1197 1.8853 0.4511 -0.2581 0.0924 683 GLU B CD 12438 O OE1 . GLU B 683 ? 1.7411 1.0020 1.7611 0.4692 -0.2726 0.0829 683 GLU B OE1 12439 O OE2 . GLU B 683 ? 2.2736 1.4106 2.2030 0.4609 -0.2701 0.1023 683 GLU B OE2 12440 N N . GLU B 684 ? 1.6552 0.7274 1.4572 0.3639 -0.2112 0.1191 684 GLU B N 12441 C CA . GLU B 684 ? 1.7890 0.8230 1.5380 0.3447 -0.2309 0.1334 684 GLU B CA 12442 C C . GLU B 684 ? 1.7763 0.8248 1.5047 0.3121 -0.2150 0.1309 684 GLU B C 12443 O O . GLU B 684 ? 1.5477 0.6211 1.2833 0.2999 -0.2239 0.1319 684 GLU B O 12444 C CB . GLU B 684 ? 1.7589 0.8026 1.5218 0.3567 -0.2646 0.1421 684 GLU B CB 12445 C CG . GLU B 684 ? 1.8527 0.8489 1.5546 0.3378 -0.2906 0.1596 684 GLU B CG 12446 C CD . GLU B 684 ? 2.0433 0.9715 1.6968 0.3418 -0.3007 0.1692 684 GLU B CD 12447 O OE1 . GLU B 684 ? 2.0689 0.9897 1.7342 0.3629 -0.3227 0.1752 684 GLU B OE1 12448 O OE2 . GLU B 684 ? 2.1283 1.0299 1.7390 0.3177 -0.2811 0.1674 684 GLU B OE2 12449 N N . PRO B 685 ? 1.5399 0.5760 1.2446 0.2991 -0.1914 0.1252 685 PRO B N 12450 C CA . PRO B 685 ? 1.5171 0.5664 1.2029 0.2728 -0.1779 0.1193 685 PRO B CA 12451 C C . PRO B 685 ? 1.5649 0.5918 1.2007 0.2482 -0.1947 0.1251 685 PRO B C 12452 O O . PRO B 685 ? 1.6156 0.6094 1.2251 0.2498 -0.2184 0.1379 685 PRO B O 12453 C CB . PRO B 685 ? 1.5026 0.5431 1.1727 0.2693 -0.1535 0.1123 685 PRO B CB 12454 C CG . PRO B 685 ? 1.5353 0.5399 1.1919 0.2836 -0.1583 0.1177 685 PRO B CG 12455 C CD . PRO B 685 ? 1.5429 0.5580 1.2413 0.3093 -0.1757 0.1214 685 PRO B CD 12456 N N . GLU B 686 ? 1.5660 0.6102 1.1875 0.2253 -0.1836 0.1149 686 GLU B N 12457 C CA . GLU B 686 ? 1.6496 0.6834 1.2246 0.1962 -0.1962 0.1156 686 GLU B CA 12458 C C . GLU B 686 ? 1.6359 0.6404 1.1534 0.1757 -0.1896 0.1137 686 GLU B C 12459 O O . GLU B 686 ? 1.6171 0.6341 1.1344 0.1737 -0.1670 0.1009 686 GLU B O 12460 C CB . GLU B 686 ? 1.8279 0.8993 1.4173 0.1807 -0.1873 0.0999 686 GLU B CB 12461 C CG . GLU B 686 ? 2.0017 1.0999 1.6359 0.1903 -0.1954 0.1011 686 GLU B CG 12462 C CD . GLU B 686 ? 2.1472 1.2668 1.8301 0.2095 -0.1772 0.0942 686 GLU B CD 12463 O OE1 . GLU B 686 ? 2.0429 1.1864 1.7546 0.2073 -0.1768 0.0887 686 GLU B OE1 12464 O OE2 . GLU B 686 ? 2.3329 1.4442 2.0214 0.2232 -0.1634 0.0945 686 GLU B OE2 12465 N N . CYS B 687 ? 1.6698 0.6356 1.1357 0.1583 -0.2109 0.1269 687 CYS B N 12466 C CA . CYS B 687 ? 1.7024 0.6357 1.1031 0.1309 -0.2068 0.1262 687 CYS B CA 12467 C C . CYS B 687 ? 1.7652 0.6885 1.1090 0.0911 -0.2242 0.1297 687 CYS B C 12468 O O . CYS B 687 ? 1.7944 0.7233 1.1470 0.0903 -0.2450 0.1388 687 CYS B O 12469 C CB . CYS B 687 ? 1.7370 0.6132 1.1172 0.1469 -0.2156 0.1417 687 CYS B CB 12470 S SG . CYS B 687 ? 2.2828 1.1736 1.7224 0.1865 -0.1924 0.1343 687 CYS B SG 12471 N N . PRO B 688 ? 1.8040 0.7175 1.0873 0.0541 -0.2153 0.1214 688 PRO B N 12472 C CA . PRO B 688 ? 2.0002 0.9051 1.2212 0.0086 -0.2312 0.1239 688 PRO B CA 12473 C C . PRO B 688 ? 2.0368 0.8751 1.2139 0.0052 -0.2677 0.1556 688 PRO B C 12474 O O . PRO B 688 ? 2.0652 0.8643 1.2633 0.0419 -0.2805 0.1728 688 PRO B O 12475 C CB . PRO B 688 ? 2.0891 0.9972 1.2547 -0.0289 -0.2115 0.1072 688 PRO B CB 12476 C CG . PRO B 688 ? 1.9564 0.8497 1.1422 -0.0009 -0.1940 0.1065 688 PRO B CG 12477 C CD . PRO B 688 ? 1.7760 0.6981 1.0469 0.0479 -0.1885 0.1056 688 PRO B CD 12478 N N . LYS B 689 ? 2.0633 0.8898 1.1788 -0.0389 -0.2856 0.1619 689 LYS B N 12479 C CA . LYS B 689 ? 2.2753 1.0389 1.3463 -0.0435 -0.3258 0.1944 689 LYS B CA 12480 C C . LYS B 689 ? 2.4020 1.0982 1.3705 -0.0896 -0.3381 0.2079 689 LYS B C 12481 O O . LYS B 689 ? 2.4689 1.1729 1.4032 -0.1188 -0.3127 0.1900 689 LYS B O 12482 C CB . LYS B 689 ? 2.2663 1.0662 1.3464 -0.0584 -0.3441 0.1973 689 LYS B CB 12483 C CG . LYS B 689 ? 2.1131 0.9805 1.2856 -0.0231 -0.3301 0.1812 689 LYS B CG 12484 C CD . LYS B 689 ? 2.1408 0.9930 1.3746 0.0351 -0.3361 0.1930 689 LYS B CD 12485 C CE . LYS B 689 ? 2.1507 1.0684 1.4683 0.0625 -0.3214 0.1772 689 LYS B CE 12486 N NZ . LYS B 689 ? 2.2089 1.1582 1.5313 0.0459 -0.3397 0.1801 689 LYS B NZ 12487 N N . GLY B 690 ? 2.3509 0.9804 1.2682 -0.0972 -0.3785 0.2397 690 GLY B N 12488 C CA . GLY B 690 ? 2.4747 1.0255 1.2843 -0.1443 -0.3962 0.2579 690 GLY B CA 12489 C C . GLY B 690 ? 2.5634 1.0391 1.3259 -0.1433 -0.4479 0.2969 690 GLY B C 12490 O O . GLY B 690 ? 2.5972 1.0302 1.2667 -0.1986 -0.4693 0.3130 690 GLY B O 12491 N N . SER C 1 ? 3.0895 2.3853 2.4588 0.7283 -0.8750 -0.4267 1417 SER C N 12492 C CA . SER C 1 ? 3.0562 2.3429 2.4181 0.7452 -0.8438 -0.4118 1417 SER C CA 12493 C C . SER C 1 ? 3.1043 2.3263 2.4284 0.7525 -0.8260 -0.4031 1417 SER C C 12494 O O . SER C 1 ? 3.1294 2.2966 2.4161 0.7337 -0.8029 -0.3954 1417 SER C O 12495 C CB . SER C 1 ? 2.9145 2.2670 2.3197 0.7782 -0.8523 -0.4119 1417 SER C CB 12496 O OG . SER C 1 ? 2.8489 2.2629 2.2915 0.7696 -0.8690 -0.4216 1417 SER C OG 12497 N N . ASP C 2 ? 3.0978 2.3280 2.4335 0.7787 -0.8357 -0.4072 1418 ASP C N 12498 C CA . ASP C 2 ? 3.0911 2.2664 2.3965 0.7870 -0.8205 -0.4063 1418 ASP C CA 12499 C C . ASP C 2 ? 3.0362 2.1942 2.3389 0.7858 -0.8402 -0.4194 1418 ASP C C 12500 O O . ASP C 2 ? 3.0130 2.2157 2.3471 0.8048 -0.8581 -0.4286 1418 ASP C O 12501 C CB . ASP C 2 ? 3.0491 2.2457 2.3659 0.8245 -0.8035 -0.4040 1418 ASP C CB 12502 C CG . ASP C 2 ? 2.9553 2.2292 2.3232 0.8525 -0.8201 -0.4109 1418 ASP C CG 12503 O OD1 . ASP C 2 ? 2.9796 2.3008 2.3718 0.8562 -0.8217 -0.4049 1418 ASP C OD1 12504 O OD2 . ASP C 2 ? 2.8319 2.1187 2.2159 0.8692 -0.8296 -0.4239 1418 ASP C OD2 12505 N N . VAL C 3 ? 3.0162 2.1062 2.2792 0.7630 -0.8349 -0.4205 1419 VAL C N 12506 C CA . VAL C 3 ? 3.0356 2.0928 2.2831 0.7555 -0.8516 -0.4327 1419 VAL C CA 12507 C C . VAL C 3 ? 3.1081 2.0860 2.3089 0.7262 -0.8405 -0.4311 1419 VAL C C 12508 O O . VAL C 3 ? 3.1411 2.0992 2.3267 0.7051 -0.8280 -0.4203 1419 VAL C O 12509 C CB . VAL C 3 ? 2.9216 2.0138 2.1857 0.7495 -0.8844 -0.4387 1419 VAL C CB 12510 C CG1 . VAL C 3 ? 3.0002 2.0415 2.2282 0.7186 -0.8962 -0.4409 1419 VAL C CG1 12511 C CG2 . VAL C 3 ? 2.8191 1.9400 2.1040 0.7744 -0.9007 -0.4509 1419 VAL C CG2 12512 N N . PRO C 4 ? 3.1022 2.0335 2.2798 0.7235 -0.8433 -0.4431 1420 PRO C N 12513 C CA . PRO C 4 ? 3.1200 1.9738 2.2534 0.6953 -0.8390 -0.4462 1420 PRO C CA 12514 C C . PRO C 4 ? 3.1801 2.0192 2.2968 0.6706 -0.8609 -0.4440 1420 PRO C C 12515 O O . PRO C 4 ? 3.1805 2.0581 2.3146 0.6641 -0.8667 -0.4363 1420 PRO C O 12516 C CB . PRO C 4 ? 3.1152 1.9404 2.2373 0.7072 -0.8379 -0.4651 1420 PRO C CB 12517 C CG . PRO C 4 ? 3.0998 1.9899 2.2588 0.7362 -0.8522 -0.4709 1420 PRO C CG 12518 C CD . PRO C 4 ? 3.0318 1.9856 2.2278 0.7518 -0.8457 -0.4580 1420 PRO C CD 12519 N N . ARG C 5 ? 3.2248 2.0038 2.3046 0.6561 -0.8692 -0.4527 1421 ARG C N 12520 C CA . ARG C 5 ? 3.2533 2.0028 2.3058 0.6342 -0.8897 -0.4539 1421 ARG C CA 12521 C C . ARG C 5 ? 3.2701 1.9832 2.3037 0.6017 -0.8748 -0.4447 1421 ARG C C 12522 O O . ARG C 5 ? 3.2475 1.9274 2.2716 0.5932 -0.8496 -0.4404 1421 ARG C O 12523 C CB . ARG C 5 ? 3.4519 2.2696 2.5338 0.6481 -0.9183 -0.4563 1421 ARG C CB 12524 C CG . ARG C 5 ? 3.4429 2.2735 2.5208 0.6308 -0.9385 -0.4588 1421 ARG C CG 12525 C CD . ARG C 5 ? 3.4389 2.3545 2.5621 0.6426 -0.9546 -0.4626 1421 ARG C CD 12526 N NE . ARG C 5 ? 3.4315 2.3655 2.5605 0.6196 -0.9549 -0.4660 1421 ARG C NE 12527 C CZ . ARG C 5 ? 3.3647 2.3657 2.5318 0.6197 -0.9575 -0.4713 1421 ARG C CZ 12528 N NH1 . ARG C 5 ? 3.2990 2.3574 2.5032 0.6420 -0.9630 -0.4711 1421 ARG C NH1 12529 N NH2 . ARG C 5 ? 3.3540 2.3652 2.5230 0.5957 -0.9526 -0.4792 1421 ARG C NH2 12530 N N . ASP C 6 ? 3.4078 2.1294 2.4376 0.5849 -0.8892 -0.4443 1422 ASP C N 12531 C CA . ASP C 6 ? 3.5649 2.2405 2.5683 0.5519 -0.8808 -0.4411 1422 ASP C CA 12532 C C . ASP C 6 ? 3.5992 2.1944 2.5622 0.5388 -0.8712 -0.4433 1422 ASP C C 12533 O O . ASP C 6 ? 3.6860 2.2469 2.6403 0.5195 -0.8463 -0.4365 1422 ASP C O 12534 C CB . ASP C 6 ? 3.6112 2.3083 2.6337 0.5361 -0.8540 -0.4294 1422 ASP C CB 12535 C CG . ASP C 6 ? 3.6133 2.3724 2.6635 0.5339 -0.8638 -0.4338 1422 ASP C CG 12536 O OD1 . ASP C 6 ? 3.6409 2.4566 2.7221 0.5552 -0.8684 -0.4346 1422 ASP C OD1 12537 O OD2 . ASP C 6 ? 3.6007 2.3545 2.6433 0.5107 -0.8668 -0.4395 1422 ASP C OD2 12538 N N . LEU C 7 ? 3.5047 2.0677 2.4404 0.5482 -0.8912 -0.4547 1423 LEU C N 12539 C CA . LEU C 7 ? 3.4337 1.9221 2.3312 0.5408 -0.8813 -0.4624 1423 LEU C CA 12540 C C . LEU C 7 ? 3.5034 1.9234 2.3556 0.5123 -0.8872 -0.4644 1423 LEU C C 12541 O O . LEU C 7 ? 3.5195 1.9276 2.3471 0.5156 -0.9131 -0.4701 1423 LEU C O 12542 C CB . LEU C 7 ? 3.3322 1.8184 2.2213 0.5679 -0.8936 -0.4754 1423 LEU C CB 12543 C CG . LEU C 7 ? 3.3379 1.8883 2.2509 0.5951 -0.9211 -0.4770 1423 LEU C CG 12544 C CD1 . LEU C 7 ? 3.3685 1.9007 2.2505 0.5902 -0.9515 -0.4810 1423 LEU C CD1 12545 C CD2 . LEU C 7 ? 3.3842 1.9404 2.3005 0.6220 -0.9214 -0.4882 1423 LEU C CD2 12546 N N . GLU C 8 ? 3.5151 1.8909 2.3559 0.4857 -0.8636 -0.4607 1424 GLU C N 12547 C CA . GLU C 8 ? 3.5692 1.8814 2.3715 0.4551 -0.8654 -0.4614 1424 GLU C CA 12548 C C . GLU C 8 ? 3.6039 1.8323 2.3622 0.4442 -0.8560 -0.4741 1424 GLU C C 12549 O O . GLU C 8 ? 3.5388 1.7615 2.2990 0.4602 -0.8462 -0.4850 1424 GLU C O 12550 C CB . GLU C 8 ? 3.5468 1.8682 2.3683 0.4274 -0.8447 -0.4487 1424 GLU C CB 12551 C CG . GLU C 8 ? 3.4934 1.8941 2.3587 0.4355 -0.8434 -0.4387 1424 GLU C CG 12552 C CD . GLU C 8 ? 3.4404 1.8436 2.3212 0.4100 -0.8149 -0.4264 1424 GLU C CD 12553 O OE1 . GLU C 8 ? 3.3992 1.7460 2.2593 0.3853 -0.7999 -0.4252 1424 GLU C OE1 12554 O OE2 . GLU C 8 ? 3.4209 1.8801 2.3329 0.4137 -0.8060 -0.4190 1424 GLU C OE2 12555 N N . VAL C 9 ? 3.6735 1.8380 2.3931 0.4160 -0.8576 -0.4754 1425 VAL C N 12556 C CA . VAL C 9 ? 3.6314 1.7088 2.3080 0.3954 -0.8436 -0.4883 1425 VAL C CA 12557 C C . VAL C 9 ? 3.5382 1.5843 2.2114 0.3564 -0.8299 -0.4807 1425 VAL C C 12558 O O . VAL C 9 ? 3.5129 1.5550 2.1750 0.3428 -0.8431 -0.4733 1425 VAL C O 12559 C CB . VAL C 9 ? 3.6311 1.6428 2.2473 0.4016 -0.8624 -0.5006 1425 VAL C CB 12560 C CG1 . VAL C 9 ? 3.6687 1.5813 2.2352 0.3714 -0.8454 -0.5142 1425 VAL C CG1 12561 C CG2 . VAL C 9 ? 3.5169 1.5521 2.1349 0.4382 -0.8708 -0.5102 1425 VAL C CG2 12562 N N . VAL C 10 ? 5.3498 4.2355 2.5825 1.1852 -1.1775 -1.3108 1426 VAL C N 12563 C CA . VAL C 10 ? 5.4716 4.3004 2.6952 1.1359 -1.1848 -1.3753 1426 VAL C CA 12564 C C . VAL C 10 ? 5.5439 4.3590 2.7726 1.1283 -1.1222 -1.4526 1426 VAL C C 12565 O O . VAL C 10 ? 5.6284 4.4949 2.7758 1.0807 -1.0944 -1.4535 1426 VAL C O 12566 C CB . VAL C 10 ? 5.4776 4.1979 2.7883 1.1486 -1.2333 -1.4147 1426 VAL C CB 12567 C CG1 . VAL C 10 ? 5.5740 4.2431 2.8745 1.0929 -1.2418 -1.4719 1426 VAL C CG1 12568 C CG2 . VAL C 10 ? 5.4025 4.1314 2.7138 1.1569 -1.2929 -1.3386 1426 VAL C CG2 12569 N N . ALA C 11 ? 5.5010 4.2486 2.8322 1.1720 -1.0970 -1.5133 1427 ALA C N 12570 C CA . ALA C 11 ? 5.5631 4.2916 2.9219 1.1627 -1.0332 -1.5862 1427 ALA C CA 12571 C C . ALA C 11 ? 5.5438 4.3448 2.8835 1.1919 -0.9728 -1.5689 1427 ALA C C 12572 O O . ALA C 11 ? 5.4623 4.2829 2.8419 1.2460 -0.9714 -1.5327 1427 ALA C O 12573 C CB . ALA C 11 ? 5.5844 4.2124 3.0827 1.1866 -1.0281 -1.6524 1427 ALA C CB 12574 N N . ALA C 12 ? 5.6628 4.5031 2.9412 1.1544 -0.9223 -1.5940 1428 ALA C N 12575 C CA . ALA C 12 ? 5.6017 4.5152 2.8562 1.1743 -0.8615 -1.5773 1428 ALA C CA 12576 C C . ALA C 12 ? 5.6342 4.5203 2.9245 1.1593 -0.7933 -1.6532 1428 ALA C C 12577 O O . ALA C 12 ? 5.6852 4.5549 2.9278 1.1041 -0.7828 -1.6933 1428 ALA C O 12578 C CB . ALA C 12 ? 5.5571 4.5768 2.6830 1.1383 -0.8649 -1.5041 1428 ALA C CB 12579 N N . THR C 13 ? 5.6024 4.4847 2.9809 1.2067 -0.7456 -1.6695 1429 THR C N 12580 C CA . THR C 13 ? 5.6419 4.5069 3.0669 1.1952 -0.6738 -1.7317 1429 THR C CA 12581 C C . THR C 13 ? 5.6031 4.5552 2.9922 1.2156 -0.6193 -1.6971 1429 THR C C 12582 O O . THR C 13 ? 5.5545 4.5752 2.8895 1.2383 -0.6402 -1.6264 1429 THR C O 12583 C CB . THR C 13 ? 5.5907 4.3700 3.1801 1.2260 -0.6605 -1.7810 1429 THR C CB 12584 O OG1 . THR C 13 ? 5.4712 4.2618 3.1374 1.2888 -0.6690 -1.7391 1429 THR C OG1 12585 C CG2 . THR C 13 ? 5.6244 4.3215 3.2531 1.2020 -0.7130 -1.8109 1429 THR C CG2 12586 N N . PRO C 14 ? 5.6004 4.5529 3.0198 1.2046 -0.5483 -1.7426 1430 PRO C N 12587 C CA . PRO C 14 ? 5.5375 4.5672 2.9454 1.2305 -0.4957 -1.7086 1430 PRO C CA 12588 C C . PRO C 14 ? 5.4209 4.4621 2.9161 1.2999 -0.5051 -1.6651 1430 PRO C C 12589 O O . PRO C 14 ? 5.3996 4.5185 2.8637 1.3241 -0.4810 -1.6143 1430 PRO C O 12590 C CB . PRO C 14 ? 5.5561 4.5560 3.0210 1.2108 -0.4226 -1.7748 1430 PRO C CB 12591 C CG . PRO C 14 ? 5.6324 4.5804 3.0512 1.1509 -0.4339 -1.8281 1430 PRO C CG 12592 C CD . PRO C 14 ? 5.6388 4.5379 3.0701 1.1558 -0.5121 -1.8175 1430 PRO C CD 12593 N N . THR C 15 ? 5.3510 4.3170 2.9557 1.3286 -0.5394 -1.6819 1431 THR C N 12594 C CA . THR C 15 ? 5.3181 4.2872 3.0081 1.3909 -0.5545 -1.6397 1431 THR C CA 12595 C C . THR C 15 ? 5.2463 4.1568 2.9684 1.4068 -0.6303 -1.6262 1431 THR C C 12596 O O . THR C 15 ? 5.3134 4.1895 2.9819 1.3694 -0.6735 -1.6431 1431 THR C O 12597 C CB . THR C 15 ? 5.0860 4.0255 2.9251 1.4155 -0.4999 -1.6691 1431 THR C CB 12598 O OG1 . THR C 15 ? 5.1439 4.0046 3.0583 1.3823 -0.4897 -1.7356 1431 THR C OG1 12599 C CG2 . THR C 15 ? 5.0792 4.0886 2.8918 1.4136 -0.4278 -1.6630 1431 THR C CG2 12600 N N . SER C 16 ? 5.1607 4.0612 2.9708 1.4599 -0.6454 -1.5930 1432 SER C N 12601 C CA . SER C 16 ? 5.1347 3.9821 2.9827 1.4812 -0.7156 -1.5720 1432 SER C CA 12602 C C . SER C 16 ? 5.1867 4.0627 2.8988 1.4645 -0.7757 -1.5295 1432 SER C C 12603 O O . SER C 16 ? 5.1888 4.1497 2.7923 1.4580 -0.7641 -1.4846 1432 SER C O 12604 C CB . SER C 16 ? 5.1314 3.8854 3.0827 1.4582 -0.7311 -1.6283 1432 SER C CB 12605 O OG . SER C 16 ? 5.0689 3.7717 3.0520 1.4733 -0.8010 -1.6070 1432 SER C OG 12606 N N . LEU C 17 ? 5.2261 4.0364 2.9507 1.4508 -0.8379 -1.5386 1433 LEU C N 12607 C CA . LEU C 17 ? 5.2420 4.0724 2.8571 1.4300 -0.9019 -1.4922 1433 LEU C CA 12608 C C . LEU C 17 ? 5.2969 4.0383 2.9631 1.4200 -0.9659 -1.5106 1433 LEU C C 12609 O O . LEU C 17 ? 5.2332 3.9021 3.0262 1.4363 -0.9631 -1.5496 1433 LEU C O 12610 C CB . LEU C 17 ? 5.0977 4.0051 2.6935 1.4605 -0.9121 -1.3974 1433 LEU C CB 12611 C CG . LEU C 17 ? 5.0623 4.0847 2.5426 1.4253 -0.8997 -1.3260 1433 LEU C CG 12612 C CD1 . LEU C 17 ? 4.9536 4.0402 2.4301 1.4583 -0.9149 -1.2336 1433 LEU C CD1 12613 C CD2 . LEU C 17 ? 5.1384 4.1626 2.5307 1.3616 -0.9403 -1.3215 1433 LEU C CD2 12614 N N . LEU C 18 ? 3.6351 3.3772 1.3397 0.0158 -0.2465 -0.3567 1434 LEU C N 12615 C CA . LEU C 18 ? 3.5161 3.2389 1.3888 0.0134 -0.2775 -0.4142 1434 LEU C CA 12616 C C . LEU C 18 ? 3.4630 3.0907 1.4430 0.0229 -0.3090 -0.3535 1434 LEU C C 12617 O O . LEU C 18 ? 3.5629 3.1724 1.5289 0.0585 -0.3642 -0.3230 1434 LEU C O 12618 C CB . LEU C 18 ? 3.4852 3.3017 1.4102 0.0578 -0.3627 -0.5270 1434 LEU C CB 12619 C CG . LEU C 18 ? 3.2529 3.0824 1.3567 0.0435 -0.3928 -0.5952 1434 LEU C CG 12620 C CD1 . LEU C 18 ? 3.1421 3.0168 1.2163 0.0009 -0.3157 -0.6346 1434 LEU C CD1 12621 C CD2 . LEU C 18 ? 3.2714 3.1577 1.4693 0.0974 -0.5199 -0.6856 1434 LEU C CD2 12622 N N . ILE C 19 ? 3.3031 2.8774 1.3887 -0.0048 -0.2737 -0.3320 1435 ILE C N 12623 C CA . ILE C 19 ? 3.2695 2.7740 1.4541 0.0137 -0.2946 -0.2653 1435 ILE C CA 12624 C C . ILE C 19 ? 3.1346 2.6795 1.5233 0.0202 -0.3406 -0.3009 1435 ILE C C 12625 O O . ILE C 19 ? 3.0552 2.6330 1.5078 -0.0125 -0.3119 -0.3532 1435 ILE C O 12626 C CB . ILE C 19 ? 3.3623 2.7651 1.4852 -0.0097 -0.2161 -0.1845 1435 ILE C CB 12627 C CG1 . ILE C 19 ? 3.3906 2.7377 1.6101 0.0251 -0.2362 -0.1181 1435 ILE C CG1 12628 C CG2 . ILE C 19 ? 3.3418 2.7357 1.4734 -0.0569 -0.1491 -0.2127 1435 ILE C CG2 12629 C CD1 . ILE C 19 ? 3.4175 2.6574 1.5714 0.0195 -0.1747 -0.0488 1435 ILE C CD1 12630 N N . SER C 20 ? 3.0871 2.6373 1.5877 0.0601 -0.4163 -0.2638 1436 SER C N 12631 C CA . SER C 20 ? 2.9882 2.5954 1.7082 0.0685 -0.4734 -0.2719 1436 SER C CA 12632 C C . SER C 20 ? 2.9979 2.5758 1.8055 0.1010 -0.4799 -0.1651 1436 SER C C 12633 O O . SER C 20 ? 3.1385 2.6636 1.8668 0.1309 -0.4895 -0.0985 1436 SER C O 12634 C CB . SER C 20 ? 2.9740 2.6549 1.7905 0.0931 -0.5949 -0.3358 1436 SER C CB 12635 O OG . SER C 20 ? 3.0168 2.7389 1.7522 0.0764 -0.5909 -0.4419 1436 SER C OG 12636 N N . TRP C 21 ? 2.8227 2.4458 1.7951 0.0980 -0.4736 -0.1458 1437 TRP C N 12637 C CA . TRP C 21 ? 2.7459 2.3704 1.8092 0.1404 -0.4756 -0.0402 1437 TRP C CA 12638 C C . TRP C 21 ? 2.6051 2.3506 1.9264 0.1490 -0.5380 -0.0220 1437 TRP C C 12639 O O . TRP C 21 ? 2.5752 2.3906 2.0074 0.1163 -0.5839 -0.0974 1437 TRP C O 12640 C CB . TRP C 21 ? 2.7502 2.2908 1.6988 0.1397 -0.3681 -0.0045 1437 TRP C CB 12641 C CG . TRP C 21 ? 2.6645 2.2125 1.6362 0.0943 -0.3049 -0.0639 1437 TRP C CG 12642 C CD1 . TRP C 21 ? 2.5408 2.1486 1.6631 0.0986 -0.2884 -0.0490 1437 TRP C CD1 12643 C CD2 . TRP C 21 ? 2.6918 2.1929 1.5358 0.0380 -0.2498 -0.1390 1437 TRP C CD2 12644 N NE1 . TRP C 21 ? 2.5041 2.0895 1.5974 0.0440 -0.2267 -0.1160 1437 TRP C NE1 12645 C CE2 . TRP C 21 ? 2.5163 2.0353 1.4408 0.0060 -0.2025 -0.1683 1437 TRP C CE2 12646 C CE3 . TRP C 21 ? 2.7278 2.1866 1.4020 0.0134 -0.2360 -0.1755 1437 TRP C CE3 12647 C CZ2 . TRP C 21 ? 2.4618 1.9443 1.3023 -0.0526 -0.1434 -0.2301 1437 TRP C CZ2 12648 C CZ3 . TRP C 21 ? 2.6799 2.1212 1.2742 -0.0396 -0.1770 -0.2309 1437 TRP C CZ3 12649 C CH2 . TRP C 21 ? 2.5324 1.9788 1.2096 -0.0735 -0.1320 -0.2566 1437 TRP C CH2 12650 N N . ASP C 22 ? 2.5405 2.3221 1.9630 0.1960 -0.5431 0.0834 1438 ASP C N 12651 C CA . ASP C 22 ? 2.3555 2.2784 2.0398 0.2082 -0.6012 0.1273 1438 ASP C CA 12652 C C . ASP C 22 ? 2.2322 2.1834 1.9525 0.2057 -0.5115 0.1384 1438 ASP C C 12653 O O . ASP C 22 ? 2.3028 2.1623 1.8649 0.2276 -0.4224 0.1600 1438 ASP C O 12654 C CB . ASP C 22 ? 2.3638 2.3475 2.1701 0.2703 -0.6803 0.2546 1438 ASP C CB 12655 C CG . ASP C 22 ? 2.4093 2.3877 2.2490 0.2708 -0.8009 0.2452 1438 ASP C CG 12656 O OD1 . ASP C 22 ? 2.4403 2.3305 2.1152 0.2428 -0.7962 0.1516 1438 ASP C OD1 12657 O OD2 . ASP C 22 ? 2.4216 2.4883 2.4532 0.3036 -0.9050 0.3375 1438 ASP C OD2 12658 N N . ALA C 23 ? 2.0917 2.1687 2.0253 0.1801 -0.5439 0.1220 1439 ALA C N 12659 C CA . ALA C 23 ? 2.0586 2.1775 2.0465 0.1736 -0.4656 0.1253 1439 ALA C CA 12660 C C . ALA C 23 ? 2.0224 2.1846 2.0350 0.2551 -0.4341 0.2455 1439 ALA C C 12661 O O . ALA C 23 ? 2.0327 2.2733 2.1468 0.3094 -0.5016 0.3465 1439 ALA C O 12662 C CB . ALA C 23 ? 1.9310 2.1980 2.1729 0.1278 -0.5222 0.0939 1439 ALA C CB 12663 N N . PRO C 24 ? 2.0683 2.1786 1.9846 0.2693 -0.3353 0.2363 1440 PRO C N 12664 C CA . PRO C 24 ? 2.0830 2.2364 2.0040 0.3585 -0.2953 0.3316 1440 PRO C CA 12665 C C . PRO C 24 ? 1.8599 2.2446 2.0631 0.3979 -0.3482 0.4269 1440 PRO C C 12666 O O . PRO C 24 ? 1.8847 2.3415 2.1070 0.4885 -0.3260 0.5231 1440 PRO C O 12667 C CB . PRO C 24 ? 2.2234 2.2690 2.0055 0.3431 -0.1960 0.2646 1440 PRO C CB 12668 C CG . PRO C 24 ? 2.3316 2.2214 1.9468 0.2613 -0.1754 0.1623 1440 PRO C CG 12669 C CD . PRO C 24 ? 2.2180 2.1983 1.9765 0.2053 -0.2571 0.1292 1440 PRO C CD 12670 N N . ALA C 25 ? 1.6559 2.1597 2.0731 0.3335 -0.4179 0.3999 1441 ALA C N 12671 C CA . ALA C 25 ? 1.4611 2.2056 2.1902 0.3521 -0.4918 0.4949 1441 ALA C CA 12672 C C . ALA C 25 ? 1.4219 2.2713 2.2459 0.3547 -0.4247 0.4942 1441 ALA C C 12673 O O . ALA C 25 ? 1.3697 2.2792 2.2957 0.3211 -0.4145 0.4694 1441 ALA C O 12674 C CB . ALA C 25 ? 1.4094 2.1583 2.1183 0.4122 -0.4978 0.5674 1441 ALA C CB 12675 N N . VAL C 26 ? 1.5256 2.2204 2.1340 0.3474 -0.3171 0.4130 1442 VAL C N 12676 C CA . VAL C 26 ? 1.4418 2.1989 2.1097 0.3407 -0.2500 0.3908 1442 VAL C CA 12677 C C . VAL C 26 ? 1.4081 2.0191 1.9780 0.2329 -0.2051 0.2489 1442 VAL C C 12678 O O . VAL C 26 ? 1.6082 2.0564 2.0092 0.1890 -0.2057 0.1775 1442 VAL C O 12679 C CB . VAL C 26 ? 1.6170 2.3217 2.1204 0.4460 -0.1673 0.4330 1442 VAL C CB 12680 C CG1 . VAL C 26 ? 1.4170 2.2689 2.0570 0.4683 -0.1247 0.4518 1442 VAL C CG1 12681 C CG2 . VAL C 26 ? 1.6858 2.4626 2.1888 0.5559 -0.2041 0.5588 1442 VAL C CG2 12682 N N . THR C 27 ? 1.3197 2.0017 2.0019 0.1913 -0.1672 0.2154 1443 THR C N 12683 C CA . THR C 27 ? 1.4456 2.0044 2.0547 0.0875 -0.1219 0.0919 1443 THR C CA 12684 C C . THR C 27 ? 1.6765 1.9792 1.9661 0.0891 -0.0447 0.0317 1443 THR C C 12685 O O . THR C 27 ? 1.8179 2.0427 1.9691 0.1623 0.0093 0.0636 1443 THR C O 12686 C CB . THR C 27 ? 1.3631 2.0271 2.1255 0.0540 -0.0799 0.0794 1443 THR C CB 12687 O OG1 . THR C 27 ? 1.4689 2.1133 2.1340 0.1438 -0.0111 0.1267 1443 THR C OG1 12688 C CG2 . THR C 27 ? 1.1547 2.0882 2.2620 0.0376 -0.1662 0.1427 1443 THR C CG2 12689 N N . VAL C 28 ? 1.7072 1.8887 1.8867 0.0132 -0.0483 -0.0516 1444 VAL C N 12690 C CA . VAL C 28 ? 1.8855 1.8433 1.7830 0.0049 0.0108 -0.0952 1444 VAL C CA 12691 C C . VAL C 28 ? 1.7783 1.6443 1.6206 -0.0928 0.0625 -0.1864 1444 VAL C C 12692 O O . VAL C 28 ? 1.6522 1.5856 1.6031 -0.1660 0.0324 -0.2437 1444 VAL C O 12693 C CB . VAL C 28 ? 2.0053 1.8990 1.7825 0.0137 -0.0347 -0.0945 1444 VAL C CB 12694 C CG1 . VAL C 28 ? 2.1473 1.8325 1.6540 -0.0002 0.0213 -0.1266 1444 VAL C CG1 12695 C CG2 . VAL C 28 ? 1.9944 1.9656 1.8199 0.1069 -0.0850 0.0034 1444 VAL C CG2 12696 N N . ARG C 29 ? 1.8096 1.5192 1.4852 -0.0905 0.1333 -0.1970 1445 ARG C N 12697 C CA . ARG C 29 ? 1.7785 1.3841 1.3857 -0.1817 0.1847 -0.2666 1445 ARG C CA 12698 C C . ARG C 29 ? 2.0338 1.5540 1.4968 -0.2305 0.1768 -0.3071 1445 ARG C C 12699 O O . ARG C 29 ? 2.1454 1.7051 1.6607 -0.3066 0.1742 -0.3685 1445 ARG C O 12700 C CB . ARG C 29 ? 1.7893 1.2358 1.2556 -0.1598 0.2464 -0.2553 1445 ARG C CB 12701 C CG . ARG C 29 ? 1.6585 1.1923 1.2505 -0.1045 0.2611 -0.2235 1445 ARG C CG 12702 C CD . ARG C 29 ? 1.6557 1.0282 1.1352 -0.1136 0.3180 -0.2422 1445 ARG C CD 12703 N NE . ARG C 29 ? 1.7087 0.8826 0.9559 -0.0523 0.3208 -0.2185 1445 ARG C NE 12704 C CZ . ARG C 29 ? 1.7842 0.9330 0.9714 0.0640 0.3111 -0.1750 1445 ARG C CZ 12705 N NH1 . ARG C 29 ? 1.6516 0.9775 0.9910 0.1356 0.3058 -0.1421 1445 ARG C NH1 12706 N NH2 . ARG C 29 ? 2.0893 1.0465 1.0703 0.1127 0.3016 -0.1601 1445 ARG C NH2 12707 N N . TYR C 30 ? 2.1865 1.6010 1.4706 -0.1817 0.1712 -0.2707 1446 TYR C N 12708 C CA . TYR C 30 ? 2.2619 1.6105 1.3995 -0.2161 0.1640 -0.2942 1446 TYR C CA 12709 C C . TYR C 30 ? 2.3692 1.6489 1.3670 -0.1471 0.1402 -0.2369 1446 TYR C C 12710 O O . TYR C 30 ? 2.4211 1.7097 1.4428 -0.0710 0.1265 -0.1828 1446 TYR C O 12711 C CB . TYR C 30 ? 2.3184 1.5391 1.3283 -0.2859 0.2227 -0.3221 1446 TYR C CB 12712 C CG . TYR C 30 ? 2.3780 1.4334 1.2615 -0.2594 0.2595 -0.2787 1446 TYR C CG 12713 C CD1 . TYR C 30 ? 2.1841 1.2229 1.1435 -0.2465 0.2862 -0.2769 1446 TYR C CD1 12714 C CD2 . TYR C 30 ? 2.6716 1.5888 1.3646 -0.2458 0.2589 -0.2398 1446 TYR C CD2 12715 C CE1 . TYR C 30 ? 2.2902 1.1652 1.1280 -0.2120 0.3057 -0.2455 1446 TYR C CE1 12716 C CE2 . TYR C 30 ? 2.7797 1.5339 1.3647 -0.2186 0.2729 -0.2026 1446 TYR C CE2 12717 C CZ . TYR C 30 ? 2.5317 1.2581 1.1839 -0.1979 0.2937 -0.2098 1446 TYR C CZ 12718 O OH . TYR C 30 ? 2.5732 1.1255 1.1122 -0.1605 0.2941 -0.1805 1446 TYR C OH 12719 N N . TYR C 31 ? 2.4214 1.6457 1.2778 -0.1712 0.1350 -0.2454 1447 TYR C N 12720 C CA . TYR C 31 ? 2.5295 1.6839 1.2495 -0.1186 0.1135 -0.1914 1447 TYR C CA 12721 C C . TYR C 31 ? 2.6242 1.6328 1.1529 -0.1516 0.1470 -0.1752 1447 TYR C C 12722 O O . TYR C 31 ? 2.5826 1.5679 1.0834 -0.2186 0.1812 -0.2066 1447 TYR C O 12723 C CB . TYR C 31 ? 2.5027 1.7553 1.2511 -0.1065 0.0556 -0.1999 1447 TYR C CB 12724 C CG . TYR C 31 ? 2.4021 1.7954 1.3503 -0.0703 0.0002 -0.1945 1447 TYR C CG 12725 C CD1 . TYR C 31 ? 2.4130 1.8247 1.4065 0.0060 -0.0234 -0.1224 1447 TYR C CD1 12726 C CD2 . TYR C 31 ? 2.3380 1.8528 1.4374 -0.1099 -0.0366 -0.2543 1447 TYR C CD2 12727 C CE1 . TYR C 31 ? 2.3294 1.8859 1.5219 0.0385 -0.0809 -0.0964 1447 TYR C CE1 12728 C CE2 . TYR C 31 ? 2.2642 1.9129 1.5686 -0.0807 -0.1039 -0.2363 1447 TYR C CE2 12729 C CZ . TYR C 31 ? 2.2345 1.9082 1.5887 -0.0082 -0.1253 -0.1504 1447 TYR C CZ 12730 O OH . TYR C 31 ? 2.1141 1.9365 1.6877 0.0203 -0.1985 -0.1124 1447 TYR C OH 12731 N N . ARG C 32 ? 2.7224 1.6387 1.1306 -0.1051 0.1321 -0.1181 1448 ARG C N 12732 C CA . ARG C 32 ? 2.8679 1.6548 1.1115 -0.1342 0.1453 -0.0851 1448 ARG C CA 12733 C C . ARG C 32 ? 3.1014 1.8879 1.2465 -0.1133 0.1113 -0.0448 1448 ARG C C 12734 O O . ARG C 32 ? 3.1717 1.9285 1.3008 -0.0495 0.0836 -0.0047 1448 ARG C O 12735 C CB . ARG C 32 ? 2.8724 1.5058 1.0598 -0.1014 0.1535 -0.0498 1448 ARG C CB 12736 C CG . ARG C 32 ? 2.7941 1.3895 1.0388 -0.1350 0.1905 -0.0819 1448 ARG C CG 12737 C CD . ARG C 32 ? 2.9156 1.3599 1.1050 -0.0772 0.1826 -0.0528 1448 ARG C CD 12738 N NE . ARG C 32 ? 3.1438 1.4423 1.1842 -0.0644 0.1484 0.0016 1448 ARG C NE 12739 C CZ . ARG C 32 ? 3.2284 1.4628 1.2100 0.0190 0.1097 0.0371 1448 ARG C CZ 12740 N NH1 . ARG C 32 ? 3.1540 1.4646 1.2062 0.1028 0.1064 0.0302 1448 ARG C NH1 12741 N NH2 . ARG C 32 ? 3.3598 1.4625 1.2200 0.0199 0.0701 0.0862 1448 ARG C NH2 12742 N N . ILE C 33 ? 3.1232 1.9483 1.1996 -0.1647 0.1151 -0.0513 1449 ILE C N 12743 C CA . ILE C 33 ? 3.2000 2.0462 1.1879 -0.1508 0.0846 -0.0157 1449 ILE C CA 12744 C C . ILE C 33 ? 3.3917 2.1158 1.2477 -0.1632 0.0812 0.0577 1449 ILE C C 12745 O O . ILE C 33 ? 3.4158 2.1038 1.2194 -0.2172 0.1024 0.0761 1449 ILE C O 12746 C CB . ILE C 33 ? 3.1747 2.1512 1.1527 -0.1864 0.0831 -0.0591 1449 ILE C CB 12747 C CG1 . ILE C 33 ? 2.9983 2.0835 1.1166 -0.1902 0.0793 -0.1404 1449 ILE C CG1 12748 C CG2 . ILE C 33 ? 3.3392 2.3589 1.2561 -0.1566 0.0439 -0.0338 1449 ILE C CG2 12749 C CD1 . ILE C 33 ? 2.9485 2.0883 1.1807 -0.1351 0.0314 -0.1503 1449 ILE C CD1 12750 N N . THR C 34 ? 3.4992 2.1644 1.3112 -0.1144 0.0478 0.1065 1450 THR C N 12751 C CA . THR C 34 ? 3.5440 2.0879 1.2494 -0.1217 0.0272 0.1788 1450 THR C CA 12752 C C . THR C 34 ? 3.6253 2.2060 1.2642 -0.1153 -0.0044 0.2250 1450 THR C C 12753 O O . THR C 34 ? 3.6131 2.2307 1.2789 -0.0674 -0.0237 0.2204 1450 THR C O 12754 C CB . THR C 34 ? 3.4727 1.8734 1.1779 -0.0627 0.0088 0.1984 1450 THR C CB 12755 O OG1 . THR C 34 ? 3.3993 1.7457 1.1436 -0.0780 0.0353 0.1669 1450 THR C OG1 12756 C CG2 . THR C 34 ? 3.5735 1.8472 1.1793 -0.0597 -0.0350 0.2711 1450 THR C CG2 12757 N N . TYR C 35 ? 3.7133 2.2910 1.2726 -0.1650 -0.0121 0.2789 1451 TYR C N 12758 C CA . TYR C 35 ? 3.7847 2.4159 1.2849 -0.1665 -0.0395 0.3257 1451 TYR C CA 12759 C C . TYR C 35 ? 3.9467 2.5071 1.3744 -0.2038 -0.0701 0.4188 1451 TYR C C 12760 O O . TYR C 35 ? 4.0055 2.5031 1.4252 -0.2419 -0.0690 0.4489 1451 TYR C O 12761 C CB . TYR C 35 ? 3.6709 2.4746 1.1687 -0.1891 -0.0203 0.2862 1451 TYR C CB 12762 C CG . TYR C 35 ? 3.6004 2.4683 1.0926 -0.2420 0.0163 0.2712 1451 TYR C CG 12763 C CD1 . TYR C 35 ? 3.4602 2.3660 1.0246 -0.2446 0.0481 0.1909 1451 TYR C CD1 12764 C CD2 . TYR C 35 ? 3.6487 2.5484 1.0734 -0.2905 0.0165 0.3468 1451 TYR C CD2 12765 C CE1 . TYR C 35 ? 3.4261 2.3891 0.9848 -0.2928 0.0838 0.1795 1451 TYR C CE1 12766 C CE2 . TYR C 35 ? 3.6255 2.5933 1.0464 -0.3354 0.0515 0.3463 1451 TYR C CE2 12767 C CZ . TYR C 35 ? 3.5142 2.5080 0.9969 -0.3358 0.0876 0.2591 1451 TYR C CZ 12768 O OH . TYR C 35 ? 3.4933 2.5541 0.9714 -0.3805 0.1246 0.2604 1451 TYR C OH 12769 N N . GLY C 36 ? 4.0015 2.5738 1.3868 -0.1962 -0.1041 0.4709 1452 GLY C N 12770 C CA . GLY C 36 ? 4.1473 2.6711 1.4833 -0.2350 -0.1460 0.5687 1452 GLY C CA 12771 C C . GLY C 36 ? 4.2514 2.8227 1.5522 -0.2308 -0.1772 0.6180 1452 GLY C C 12772 O O . GLY C 36 ? 4.2077 2.8322 1.5160 -0.1930 -0.1680 0.5760 1452 GLY C O 12773 N N . GLU C 37 ? 3.2202 1.9126 3.0045 0.2116 -0.3370 0.2812 1453 GLU C N 12774 C CA . GLU C 37 ? 3.1538 1.8957 2.9822 0.1680 -0.2854 0.2522 1453 GLU C CA 12775 C C . GLU C 37 ? 3.2008 2.0420 3.0124 0.1194 -0.2146 0.3686 1453 GLU C C 12776 O O . GLU C 37 ? 3.2628 2.1638 3.0073 0.1284 -0.1824 0.4512 1453 GLU C O 12777 C CB . GLU C 37 ? 3.0671 1.8753 2.8563 0.2049 -0.2335 0.1070 1453 GLU C CB 12778 C CG . GLU C 37 ? 3.1113 1.8421 2.9360 0.2434 -0.2917 -0.0253 1453 GLU C CG 12779 C CD . GLU C 37 ? 3.0198 1.8155 2.8027 0.2624 -0.2299 -0.1644 1453 GLU C CD 12780 O OE1 . GLU C 37 ? 2.9263 1.8186 2.6361 0.2552 -0.1493 -0.1577 1453 GLU C OE1 12781 O OE2 . GLU C 37 ? 3.0293 1.7763 2.8462 0.2833 -0.2624 -0.2815 1453 GLU C OE2 12782 N N . THR C 38 ? 3.1864 2.0472 3.0581 0.0717 -0.1922 0.3699 1454 THR C N 12783 C CA . THR C 38 ? 3.1705 2.1396 3.0463 0.0260 -0.1284 0.4674 1454 THR C CA 12784 C C . THR C 38 ? 3.0392 2.1468 2.8164 0.0618 -0.0393 0.4299 1454 THR C C 12785 O O . THR C 38 ? 2.9254 2.0379 2.6330 0.1142 -0.0266 0.3294 1454 THR C O 12786 C CB . THR C 38 ? 3.1117 2.0618 3.0874 -0.0286 -0.1394 0.4654 1454 THR C CB 12787 O OG1 . THR C 38 ? 3.0857 2.1527 3.0834 -0.0744 -0.0840 0.5648 1454 THR C OG1 12788 C CG2 . THR C 38 ? 2.9777 1.9283 2.9306 -0.0010 -0.1177 0.3263 1454 THR C CG2 12789 N N . GLY C 39 ? 3.0478 2.2704 2.8212 0.0326 0.0201 0.5079 1455 GLY C N 12790 C CA . GLY C 39 ? 2.9141 2.2661 2.5897 0.0681 0.0986 0.4793 1455 GLY C CA 12791 C C . GLY C 39 ? 2.9509 2.3457 2.5201 0.1189 0.1215 0.5038 1455 GLY C C 12792 O O . GLY C 39 ? 3.0962 2.4625 2.6636 0.1126 0.0976 0.5967 1455 GLY C O 12793 N N . GLY C 40 ? 2.8727 2.3248 2.3436 0.1691 0.1643 0.4192 1456 GLY C N 12794 C CA . GLY C 40 ? 2.9507 2.4491 2.3145 0.2244 0.1863 0.4273 1456 GLY C CA 12795 C C . GLY C 40 ? 2.9728 2.3926 2.3122 0.2682 0.1455 0.3224 1456 GLY C C 12796 O O . GLY C 40 ? 2.9296 2.3924 2.1769 0.3195 0.1676 0.2802 1456 GLY C O 12797 N N . ASN C 41 ? 3.0020 2.3117 2.4286 0.2497 0.0836 0.2761 1457 ASN C N 12798 C CA . ASN C 41 ? 2.9456 2.1943 2.3703 0.2870 0.0475 0.1519 1457 ASN C CA 12799 C C . ASN C 41 ? 3.0115 2.2317 2.4078 0.3372 0.0033 0.1627 1457 ASN C C 12800 O O . ASN C 41 ? 3.1284 2.3731 2.4771 0.3488 0.0079 0.2679 1457 ASN C O 12801 C CB . ASN C 41 ? 2.9224 2.0651 2.4492 0.2567 -0.0075 0.0961 1457 ASN C CB 12802 C CG . ASN C 41 ? 2.8737 2.0178 2.3867 0.2482 0.0261 -0.0269 1457 ASN C CG 12803 O OD1 . ASN C 41 ? 2.8463 1.9730 2.3403 0.2749 0.0222 -0.1444 1457 ASN C OD1 12804 N ND2 . ASN C 41 ? 2.8833 2.0470 2.4019 0.2099 0.0590 -0.0032 1457 ASN C ND2 12805 N N . SER C 42 ? 2.9753 2.1438 2.3982 0.3686 -0.0398 0.0469 1458 SER C N 12806 C CA . SER C 42 ? 3.0232 2.1752 2.4183 0.4299 -0.0841 0.0137 1458 SER C CA 12807 C C . SER C 42 ? 3.1655 2.2424 2.5584 0.4406 -0.1467 0.1322 1458 SER C C 12808 O O . SER C 42 ? 3.2532 2.2575 2.7005 0.3941 -0.1792 0.2166 1458 SER C O 12809 C CB . SER C 42 ? 2.9656 2.0712 2.4253 0.4517 -0.1301 -0.1328 1458 SER C CB 12810 O OG . SER C 42 ? 2.8990 2.0657 2.3394 0.4392 -0.0681 -0.2451 1458 SER C OG 12811 N N . PRO C 43 ? 3.2135 2.2987 2.5351 0.5008 -0.1662 0.1378 1459 PRO C N 12812 C CA . PRO C 43 ? 3.3343 2.3326 2.6169 0.5209 -0.2270 0.2450 1459 PRO C CA 12813 C C . PRO C 43 ? 3.3861 2.2365 2.7442 0.5112 -0.3277 0.2481 1459 PRO C C 12814 O O . PRO C 43 ? 3.2926 2.1132 2.7327 0.5181 -0.3651 0.1338 1459 PRO C O 12815 C CB . PRO C 43 ? 3.3278 2.3555 2.5348 0.6034 -0.2426 0.1836 1459 PRO C CB 12816 C CG . PRO C 43 ? 3.1675 2.3312 2.3389 0.6071 -0.1547 0.1162 1459 PRO C CG 12817 C CD . PRO C 43 ? 3.1098 2.2899 2.3653 0.5516 -0.1244 0.0467 1459 PRO C CD 12818 N N . VAL C 44 ? 3.5224 2.2761 2.8425 0.4946 -0.3710 0.3801 1460 VAL C N 12819 C CA . VAL C 44 ? 3.6510 2.2468 3.0277 0.4702 -0.4666 0.4139 1460 VAL C CA 12820 C C . VAL C 44 ? 3.8016 2.2695 3.1413 0.5444 -0.5785 0.3742 1460 VAL C C 12821 O O . VAL C 44 ? 3.8670 2.3288 3.1042 0.5970 -0.5876 0.4032 1460 VAL C O 12822 C CB . VAL C 44 ? 3.7347 2.2822 3.0906 0.3921 -0.4517 0.5888 1460 VAL C CB 12823 C CG1 . VAL C 44 ? 3.5483 2.1888 2.9853 0.3154 -0.3761 0.6085 1460 VAL C CG1 12824 C CG2 . VAL C 44 ? 3.8066 2.3948 3.0324 0.4078 -0.4056 0.6946 1460 VAL C CG2 12825 N N . GLN C 45 ? 3.8304 2.1932 3.2507 0.5543 -0.6686 0.3023 1461 GLN C N 12826 C CA . GLN C 45 ? 3.9638 2.1887 3.3587 0.6271 -0.7927 0.2568 1461 GLN C CA 12827 C C . GLN C 45 ? 4.2264 2.2656 3.5539 0.5952 -0.8696 0.4061 1461 GLN C C 12828 O O . GLN C 45 ? 4.2183 2.2197 3.5752 0.5072 -0.8488 0.5124 1461 GLN C O 12829 C CB . GLN C 45 ? 3.8401 2.0389 3.3484 0.6579 -0.8583 0.1042 1461 GLN C CB 12830 C CG . GLN C 45 ? 3.5982 1.9661 3.1794 0.6588 -0.7712 -0.0317 1461 GLN C CG 12831 C CD . GLN C 45 ? 3.4867 1.9787 3.0199 0.7228 -0.7282 -0.1149 1461 GLN C CD 12832 O OE1 . GLN C 45 ? 3.5426 1.9865 3.0189 0.7936 -0.7945 -0.1264 1461 GLN C OE1 12833 N NE2 . GLN C 45 ? 3.3040 1.9466 2.8536 0.6989 -0.6223 -0.1753 1461 GLN C NE2 12834 N N . GLU C 46 ? 3.2980 1.6008 2.2896 0.0252 0.8357 0.1773 1462 GLU C N 12835 C CA . GLU C 46 ? 3.1664 1.6688 2.2016 0.0445 0.7304 0.1503 1462 GLU C CA 12836 C C . GLU C 46 ? 3.1213 1.6942 2.3699 -0.0305 0.7469 0.0543 1462 GLU C C 12837 O O . GLU C 46 ? 3.1270 1.6301 2.5649 -0.0741 0.7957 -0.0196 1462 GLU C O 12838 C CB . GLU C 46 ? 3.1271 1.7000 2.1962 0.1387 0.6088 0.1464 1462 GLU C CB 12839 C CG . GLU C 46 ? 3.2025 1.6991 2.4738 0.1483 0.6002 0.0706 1462 GLU C CG 12840 C CD . GLU C 46 ? 3.0951 1.6607 2.3750 0.2552 0.4770 0.0704 1462 GLU C CD 12841 O OE1 . GLU C 46 ? 2.9853 1.6772 2.1395 0.3133 0.4006 0.1240 1462 GLU C OE1 12842 O OE2 . GLU C 46 ? 3.0634 1.5603 2.4796 0.2821 0.4575 0.0136 1462 GLU C OE2 12843 N N . PHE C 47 ? 3.0698 1.7824 2.2890 -0.0436 0.7057 0.0523 1463 PHE C N 12844 C CA . PHE C 47 ? 2.9301 1.7186 2.3265 -0.1013 0.7090 -0.0343 1463 PHE C CA 12845 C C . PHE C 47 ? 2.8484 1.7995 2.2583 -0.0588 0.5999 -0.0431 1463 PHE C C 12846 O O . PHE C 47 ? 2.8399 1.8504 2.1418 0.0124 0.5242 0.0141 1463 PHE C O 12847 C CB . PHE C 47 ? 2.9395 1.6983 2.2855 -0.1854 0.8084 -0.0329 1463 PHE C CB 12848 C CG . PHE C 47 ? 2.9522 1.6043 2.4512 -0.2560 0.9150 -0.0954 1463 PHE C CG 12849 C CD1 . PHE C 47 ? 2.8416 1.4691 2.5585 -0.2525 0.9021 -0.1753 1463 PHE C CD1 12850 C CD2 . PHE C 47 ? 3.0188 1.6024 2.4494 -0.3230 1.0287 -0.0792 1463 PHE C CD2 12851 C CE1 . PHE C 47 ? 2.8763 1.4194 2.7561 -0.3229 1.0026 -0.2408 1463 PHE C CE1 12852 C CE2 . PHE C 47 ? 2.9911 1.4839 2.5723 -0.3908 1.1356 -0.1358 1463 PHE C CE2 12853 C CZ . PHE C 47 ? 2.9442 1.4202 2.7586 -0.3950 1.1236 -0.2183 1463 PHE C CZ 12854 N N . THR C 48 ? 2.8496 1.8689 2.3892 -0.1002 0.5967 -0.1132 1464 THR C N 12855 C CA . THR C 48 ? 2.7377 1.8912 2.3031 -0.0606 0.5047 -0.1248 1464 THR C CA 12856 C C . THR C 48 ? 2.6684 1.8883 2.2198 -0.1219 0.5242 -0.1411 1464 THR C C 12857 O O . THR C 48 ? 2.6985 1.8723 2.3030 -0.1930 0.5999 -0.1850 1464 THR C O 12858 C CB . THR C 48 ? 2.6038 1.7801 2.3637 -0.0143 0.4497 -0.2083 1464 THR C CB 12859 O OG1 . THR C 48 ? 2.4318 1.7236 2.2034 0.0241 0.3757 -0.2152 1464 THR C OG1 12860 C CG2 . THR C 48 ? 2.6449 1.7662 2.5829 -0.0776 0.5171 -0.3053 1464 THR C CG2 12861 N N . VAL C 49 ? 2.5528 1.8805 2.0350 -0.0933 0.4574 -0.1061 1465 VAL C N 12862 C CA . VAL C 49 ? 2.4533 1.8472 1.9286 -0.1444 0.4621 -0.1236 1465 VAL C CA 12863 C C . VAL C 49 ? 2.3485 1.8398 1.8717 -0.0920 0.3801 -0.1289 1465 VAL C C 12864 O O . VAL C 49 ? 2.3595 1.8889 1.8575 -0.0166 0.3189 -0.0899 1465 VAL C O 12865 C CB . VAL C 49 ? 2.4951 1.9144 1.7925 -0.1810 0.4853 -0.0605 1465 VAL C CB 12866 C CG1 . VAL C 49 ? 2.6049 1.9210 1.8495 -0.2356 0.5807 -0.0620 1465 VAL C CG1 12867 C CG2 . VAL C 49 ? 2.5310 2.0034 1.6993 -0.1158 0.4280 0.0191 1465 VAL C CG2 12868 N N . PRO C 50 ? 2.2804 1.8056 1.8653 -0.1266 0.3823 -0.1745 1466 PRO C N 12869 C CA . PRO C 50 ? 2.1491 1.7461 1.7775 -0.0726 0.3166 -0.1782 1466 PRO C CA 12870 C C . PRO C 50 ? 2.2382 1.9258 1.7502 -0.0469 0.2705 -0.0963 1466 PRO C C 12871 O O . PRO C 50 ? 2.4426 2.1475 1.8379 -0.0705 0.2826 -0.0430 1466 PRO C O 12872 C CB . PRO C 50 ? 2.0515 1.6438 1.7408 -0.1284 0.3457 -0.2379 1466 PRO C CB 12873 C CG . PRO C 50 ? 2.2052 1.7586 1.8347 -0.2164 0.4156 -0.2400 1466 PRO C CG 12874 C CD . PRO C 50 ? 2.2899 1.7792 1.9041 -0.2096 0.4483 -0.2252 1466 PRO C CD 12875 N N . GLY C 51 ? 2.1900 1.9371 1.7337 0.0049 0.2210 -0.0886 1467 GLY C N 12876 C CA . GLY C 51 ? 2.2393 2.0823 1.6979 0.0366 0.1788 -0.0137 1467 GLY C CA 12877 C C . GLY C 51 ? 2.1822 2.0838 1.6134 -0.0254 0.1902 -0.0011 1467 GLY C C 12878 O O . GLY C 51 ? 2.2091 2.2015 1.5754 -0.0205 0.1657 0.0569 1467 GLY C O 12879 N N . SER C 52 ? 2.1578 2.0095 1.6446 -0.0842 0.2275 -0.0597 1468 SER C N 12880 C CA . SER C 52 ? 2.0759 1.9647 1.5453 -0.1485 0.2414 -0.0579 1468 SER C CA 12881 C C . SER C 52 ? 2.0184 1.9156 1.4125 -0.2356 0.2757 -0.0588 1468 SER C C 12882 O O . SER C 52 ? 2.0219 1.9521 1.3981 -0.2978 0.2860 -0.0647 1468 SER C O 12883 C CB . SER C 52 ? 2.1199 1.9455 1.6755 -0.1574 0.2600 -0.1216 1468 SER C CB 12884 O OG . SER C 52 ? 2.1202 1.9437 1.7278 -0.0647 0.2247 -0.1193 1468 SER C OG 12885 N N . LYS C 53 ? 2.0576 1.9188 1.4042 -0.2358 0.2948 -0.0544 1469 LYS C N 12886 C CA . LYS C 53 ? 2.1247 1.9871 1.3770 -0.2994 0.3284 -0.0512 1469 LYS C CA 12887 C C . LYS C 53 ? 2.1243 2.0411 1.2620 -0.2630 0.3040 0.0138 1469 LYS C C 12888 O O . LYS C 53 ? 1.9737 1.8655 1.1039 -0.1988 0.2888 0.0418 1469 LYS C O 12889 C CB . LYS C 53 ? 2.1125 1.8690 1.3876 -0.3351 0.3903 -0.1027 1469 LYS C CB 12890 C CG . LYS C 53 ? 2.1253 1.8541 1.4372 -0.4059 0.4267 -0.1636 1469 LYS C CG 12891 C CD . LYS C 53 ? 2.0176 1.7499 1.4339 -0.3928 0.4030 -0.1967 1469 LYS C CD 12892 C CE . LYS C 53 ? 2.0007 1.7079 1.4341 -0.4612 0.4328 -0.2514 1469 LYS C CE 12893 N NZ . LYS C 53 ? 2.1014 1.7311 1.5589 -0.4953 0.4915 -0.3087 1469 LYS C NZ 12894 N N . SER C 54 ? 2.1998 2.1920 1.2484 -0.3000 0.2971 0.0317 1470 SER C N 12895 C CA . SER C 54 ? 2.1054 2.1694 1.0368 -0.2592 0.2664 0.0889 1470 SER C CA 12896 C C . SER C 54 ? 2.0891 2.0838 0.9004 -0.2635 0.3080 0.0944 1470 SER C C 12897 O O . SER C 54 ? 2.1135 2.1538 0.8030 -0.2240 0.2873 0.1384 1470 SER C O 12898 C CB . SER C 54 ? 2.0521 2.2560 0.9588 -0.2876 0.2292 0.0997 1470 SER C CB 12899 O OG . SER C 54 ? 2.1179 2.4055 0.9097 -0.2436 0.1961 0.1460 1470 SER C OG 12900 N N . THR C 55 ? 2.0473 1.9311 0.8874 -0.3057 0.3698 0.0506 1471 THR C N 12901 C CA . THR C 55 ? 2.1992 2.0018 0.9229 -0.3112 0.4253 0.0584 1471 THR C CA 12902 C C . THR C 55 ? 2.2670 1.9357 1.0365 -0.2915 0.4769 0.0555 1471 THR C C 12903 O O . THR C 55 ? 2.1827 1.8297 1.0829 -0.2733 0.4621 0.0360 1471 THR C O 12904 C CB . THR C 55 ? 2.2166 2.0042 0.9149 -0.3828 0.4687 0.0093 1471 THR C CB 12905 O OG1 . THR C 55 ? 2.3291 2.0290 0.9030 -0.3780 0.5312 0.0229 1471 THR C OG1 12906 C CG2 . THR C 55 ? 2.1182 1.8522 0.9668 -0.4315 0.4982 -0.0539 1471 THR C CG2 12907 N N . ALA C 56 ? 2.4004 1.9789 1.0617 -0.2926 0.5394 0.0724 1472 ALA C N 12908 C CA . ALA C 56 ? 2.4266 1.8680 1.1331 -0.2869 0.6048 0.0679 1472 ALA C CA 12909 C C . ALA C 56 ? 2.6171 1.9612 1.2078 -0.3149 0.6959 0.0743 1472 ALA C C 12910 O O . ALA C 56 ? 2.6903 2.0851 1.1543 -0.3050 0.6822 0.0962 1472 ALA C O 12911 C CB . ALA C 56 ? 2.4660 1.8819 1.1444 -0.2118 0.5726 0.1199 1472 ALA C CB 12912 N N . THR C 57 ? 2.7338 1.9559 1.4008 -0.3395 0.7766 0.0511 1473 THR C N 12913 C CA . THR C 57 ? 2.9196 2.0380 1.4882 -0.3641 0.8769 0.0607 1473 THR C CA 12914 C C . THR C 57 ? 2.9491 1.9185 1.5516 -0.3569 0.9585 0.0779 1473 THR C C 12915 O O . THR C 57 ? 2.8326 1.7796 1.6208 -0.3703 0.9571 0.0345 1473 THR C O 12916 C CB . THR C 57 ? 2.8882 2.0173 1.5380 -0.4338 0.9188 -0.0078 1473 THR C CB 12917 O OG1 . THR C 57 ? 2.8553 2.1103 1.4885 -0.4473 0.8457 -0.0297 1473 THR C OG1 12918 C CG2 . THR C 57 ? 2.9219 1.9834 1.4990 -0.4333 0.9808 0.0056 1473 THR C CG2 12919 N N . ILE C 58 ? 1.3923 2.9310 2.2235 0.0088 0.2879 0.8558 1474 ILE C N 12920 C CA . ILE C 58 ? 1.5808 2.9265 2.2086 0.0235 0.2885 0.8294 1474 ILE C CA 12921 C C . ILE C 58 ? 1.6542 2.9741 2.2839 -0.0196 0.2647 0.7842 1474 ILE C C 12922 O O . ILE C 58 ? 1.6638 3.1080 2.3957 -0.0213 0.2611 0.7820 1474 ILE C O 12923 C CB . ILE C 58 ? 1.6016 2.8771 2.0573 0.1314 0.3276 0.8583 1474 ILE C CB 12924 C CG1 . ILE C 58 ? 1.7732 2.8210 2.0018 0.1402 0.3290 0.8309 1474 ILE C CG1 12925 C CG2 . ILE C 58 ? 1.5231 2.9222 2.0314 0.1923 0.3408 0.8798 1474 ILE C CG2 12926 C CD1 . ILE C 58 ? 1.7843 2.7143 1.9424 0.0784 0.3159 0.8183 1474 ILE C CD1 12927 N N . SER C 59 ? 1.7153 2.8808 2.2294 -0.0621 0.2474 0.7497 1475 SER C N 12928 C CA . SER C 59 ? 1.6704 2.8066 2.1768 -0.1129 0.2237 0.7051 1475 SER C CA 12929 C C . SER C 59 ? 1.8193 2.8130 2.1178 -0.0638 0.2294 0.7021 1475 SER C C 12930 O O . SER C 59 ? 1.9346 2.8507 2.1004 0.0179 0.2565 0.7327 1475 SER C O 12931 C CB . SER C 59 ? 1.5460 2.6283 2.0886 -0.2055 0.1968 0.6697 1475 SER C CB 12932 O OG . SER C 59 ? 1.3484 2.5544 2.0927 -0.2485 0.1916 0.6747 1475 SER C OG 12933 N N . GLY C 60 ? 1.7991 2.7563 2.0697 -0.1142 0.2057 0.6649 1476 GLY C N 12934 C CA . GLY C 60 ? 1.9620 2.7786 2.0403 -0.0800 0.2043 0.6628 1476 GLY C CA 12935 C C . GLY C 60 ? 2.0604 2.9746 2.1783 -0.0553 0.2015 0.6708 1476 GLY C C 12936 O O . GLY C 60 ? 2.0257 3.1151 2.2949 -0.0382 0.2102 0.6908 1476 GLY C O 12937 N N . LEU C 61 ? 2.2074 3.0108 2.1858 -0.0597 0.1866 0.6597 1477 LEU C N 12938 C CA . LEU C 61 ? 2.1775 3.0677 2.1793 -0.0443 0.1782 0.6730 1477 LEU C CA 12939 C C . LEU C 61 ? 2.3533 3.1002 2.1643 0.0433 0.1889 0.7093 1477 LEU C C 12940 O O . LEU C 61 ? 2.4683 3.0320 2.1104 0.0241 0.1752 0.6919 1477 LEU C O 12941 C CB . LEU C 61 ? 2.0206 2.9468 2.0674 -0.1520 0.1438 0.6231 1477 LEU C CB 12942 C CG . LEU C 61 ? 1.8130 2.8759 2.0534 -0.2432 0.1355 0.5787 1477 LEU C CG 12943 C CD1 . LEU C 61 ? 1.8027 2.7659 2.0259 -0.2937 0.1300 0.5481 1477 LEU C CD1 12944 C CD2 . LEU C 61 ? 1.7517 2.9062 2.0523 -0.3231 0.1136 0.5409 1477 LEU C CD2 12945 N N . LYS C 62 ? 2.3472 3.1798 2.1888 0.1389 0.2137 0.7626 1478 LYS C N 12946 C CA . LYS C 62 ? 2.5347 3.2446 2.2176 0.2394 0.2309 0.8054 1478 LYS C CA 12947 C C . LYS C 62 ? 2.4886 3.3797 2.2736 0.3002 0.2363 0.8618 1478 LYS C C 12948 O O . LYS C 62 ? 2.3387 3.4412 2.3034 0.2852 0.2388 0.8742 1478 LYS C O 12949 C CB . LYS C 62 ? 2.6810 3.2475 2.2430 0.3289 0.2744 0.8222 1478 LYS C CB 12950 C CG . LYS C 62 ? 2.7277 3.0776 2.1338 0.2765 0.2683 0.7777 1478 LYS C CG 12951 C CD . LYS C 62 ? 2.8067 2.9622 2.0284 0.2522 0.2439 0.7626 1478 LYS C CD 12952 C CE . LYS C 62 ? 2.9856 3.0133 2.0607 0.3735 0.2743 0.8070 1478 LYS C CE 12953 N NZ . LYS C 62 ? 3.1252 2.9497 2.0138 0.3468 0.2479 0.7963 1478 LYS C NZ 12954 N N . PRO C 63 ? 2.5898 3.4001 2.2609 0.3661 0.2363 0.9010 1479 PRO C N 12955 C CA . PRO C 63 ? 2.5563 3.5422 2.3203 0.4366 0.2432 0.9697 1479 PRO C CA 12956 C C . PRO C 63 ? 2.5858 3.6399 2.3948 0.5552 0.2945 1.0192 1479 PRO C C 12957 O O . PRO C 63 ? 2.5979 3.5481 2.3514 0.5803 0.3247 0.9968 1479 PRO C O 12958 C CB . PRO C 63 ? 2.6696 3.5077 2.2776 0.4820 0.2315 1.0005 1479 PRO C CB 12959 C CG . PRO C 63 ? 2.8114 3.3640 2.2172 0.4832 0.2407 0.9587 1479 PRO C CG 12960 C CD . PRO C 63 ? 2.7130 3.2755 2.1718 0.3692 0.2249 0.8882 1479 PRO C CD 12961 N N . GLY C 64 ? 2.5665 3.8022 2.4740 0.6234 0.3037 1.0890 1480 GLY C N 12962 C CA . GLY C 64 ? 2.5684 3.9069 2.5391 0.7325 0.3526 1.1408 1480 GLY C CA 12963 C C . GLY C 64 ? 2.7592 3.8889 2.5594 0.8637 0.4050 1.1598 1480 GLY C C 12964 O O . GLY C 64 ? 2.7151 3.7855 2.4832 0.8971 0.4436 1.1414 1480 GLY C O 12965 N N . VAL C 65 ? 2.9570 3.9685 2.6430 0.9337 0.4066 1.1958 1481 VAL C N 12966 C CA . VAL C 65 ? 3.1794 3.9709 2.6913 1.0666 0.4603 1.2151 1481 VAL C CA 12967 C C . VAL C 65 ? 3.2281 4.1226 2.8020 1.1827 0.5253 1.2543 1481 VAL C C 12968 O O . VAL C 65 ? 3.3960 4.1078 2.8333 1.2553 0.5779 1.2348 1481 VAL C O 12969 C CB . VAL C 65 ? 3.2416 3.7293 2.5481 1.0188 0.4615 1.1392 1481 VAL C CB 12970 C CG1 . VAL C 65 ? 3.5042 3.7252 2.5996 1.1304 0.4983 1.1573 1481 VAL C CG1 12971 C CG2 . VAL C 65 ? 3.1264 3.5824 2.4258 0.8665 0.3942 1.0860 1481 VAL C CG2 12972 N N . ASP C 66 ? 3.0617 4.2530 2.8367 1.1931 0.5216 1.3093 1482 ASP C N 12973 C CA . ASP C 66 ? 2.9620 4.3049 2.8275 1.2852 0.5767 1.3508 1482 ASP C CA 12974 C C . ASP C 66 ? 2.9389 4.1858 2.7523 1.2522 0.6036 1.2884 1482 ASP C C 12975 O O . ASP C 66 ? 3.0762 4.1877 2.7734 1.3500 0.6648 1.2866 1482 ASP C O 12976 C CB . ASP C 66 ? 3.0778 4.3600 2.8700 1.4621 0.6378 1.4176 1482 ASP C CB 12977 C CG . ASP C 66 ? 3.0066 4.3919 2.8562 1.5026 0.6104 1.4938 1482 ASP C CG 12978 O OD1 . ASP C 66 ? 2.8106 4.4017 2.8013 1.4023 0.5518 1.5100 1482 ASP C OD1 12979 O OD2 . ASP C 66 ? 3.1474 4.4056 2.8994 1.6335 0.6484 1.5389 1482 ASP C OD2 12980 N N . TYR C 67 ? 2.7803 4.0985 2.6800 1.1136 0.5593 1.2386 1483 TYR C N 12981 C CA . TYR C 67 ? 2.6771 3.9100 2.5365 1.0647 0.5735 1.1838 1483 TYR C CA 12982 C C . TYR C 67 ? 2.5922 3.9974 2.5533 1.1253 0.6194 1.2213 1483 TYR C C 12983 O O . TYR C 67 ? 2.5001 4.1626 2.6328 1.1417 0.6160 1.2771 1483 TYR C O 12984 C CB . TYR C 67 ? 2.4795 3.7484 2.4200 0.9038 0.5127 1.1269 1483 TYR C CB 12985 C CG . TYR C 67 ? 2.6150 3.6291 2.3916 0.8337 0.4858 1.0622 1483 TYR C CG 12986 C CD1 . TYR C 67 ? 2.5180 3.5526 2.3565 0.6980 0.4297 1.0144 1483 TYR C CD1 12987 C CD2 . TYR C 67 ? 2.8705 3.6233 2.4278 0.9012 0.5187 1.0487 1483 TYR C CD2 12988 C CE1 . TYR C 67 ? 2.6240 3.4429 2.3176 0.6316 0.4046 0.9603 1483 TYR C CE1 12989 C CE2 . TYR C 67 ? 2.9860 3.5109 2.3878 0.8286 0.4911 0.9937 1483 TYR C CE2 12990 C CZ . TYR C 67 ? 2.8611 3.4288 2.3355 0.6939 0.4327 0.9525 1483 TYR C CZ 12991 O OH . TYR C 67 ? 2.9644 3.3221 2.2889 0.6196 0.4048 0.9026 1483 TYR C OH 12992 N N . THR C 68 ? 4.8445 4.1635 1.4127 -0.4703 -0.2580 0.0214 1484 THR C N 12993 C CA . THR C 68 ? 4.6817 4.0547 1.3991 -0.4909 -0.3022 -0.0545 1484 THR C CA 12994 C C . THR C 68 ? 4.4748 3.8268 1.3558 -0.6039 -0.2428 -0.0845 1484 THR C C 12995 O O . THR C 68 ? 4.4985 3.7075 1.3438 -0.6613 -0.1753 -0.0198 1484 THR C O 12996 C CB . THR C 68 ? 4.7691 4.0187 1.4245 -0.4309 -0.3358 -0.0046 1484 THR C CB 12997 O OG1 . THR C 68 ? 4.5797 3.8629 1.4476 -0.4629 -0.3515 -0.0670 1484 THR C OG1 12998 C CG2 . THR C 68 ? 4.9272 3.9448 1.4317 -0.4497 -0.2663 0.1145 1484 THR C CG2 12999 N N . ILE C 69 ? 4.2619 3.7630 1.3324 -0.6309 -0.2630 -0.1852 1485 ILE C N 13000 C CA . ILE C 69 ? 4.0415 3.5451 1.2743 -0.7230 -0.2037 -0.2138 1485 ILE C CA 13001 C C . ILE C 69 ? 3.8996 3.3673 1.2404 -0.7418 -0.2184 -0.2433 1485 ILE C C 13002 O O . ILE C 69 ? 3.8996 3.3678 1.2521 -0.6727 -0.2767 -0.2512 1485 ILE C O 13003 C CB . ILE C 69 ? 3.8608 3.5419 1.2495 -0.7408 -0.1952 -0.2980 1485 ILE C CB 13004 C CG1 . ILE C 69 ? 3.9677 3.7300 1.2539 -0.6867 -0.2191 -0.2981 1485 ILE C CG1 13005 C CG2 . ILE C 69 ? 3.7121 3.3780 1.2064 -0.8263 -0.1169 -0.2914 1485 ILE C CG2 13006 C CD1 . ILE C 69 ? 4.1030 3.7719 1.2572 -0.7102 -0.1646 -0.2149 1485 ILE C CD1 13007 N N . THR C 70 ? 3.7356 3.1933 1.2098 -0.8154 -0.1617 -0.2579 1486 THR C N 13008 C CA . THR C 70 ? 3.6028 3.0552 1.2298 -0.8309 -0.1646 -0.2953 1486 THR C CA 13009 C C . THR C 70 ? 3.3876 2.9227 1.1859 -0.8932 -0.1045 -0.3398 1486 THR C C 13010 O O . THR C 70 ? 3.4438 2.9866 1.2273 -0.9331 -0.0524 -0.3137 1486 THR C O 13011 C CB . THR C 70 ? 3.7385 3.0216 1.3271 -0.8336 -0.1469 -0.2186 1486 THR C CB 13012 O OG1 . THR C 70 ? 3.8398 3.0105 1.2817 -0.8846 -0.0874 -0.1459 1486 THR C OG1 13013 C CG2 . THR C 70 ? 3.8399 3.0672 1.3601 -0.7436 -0.2109 -0.1864 1486 THR C CG2 13014 N N . VAL C 71 ? 3.2015 2.8029 1.1793 -0.8901 -0.1096 -0.4036 1487 VAL C N 13015 C CA . VAL C 71 ? 2.9945 2.6687 1.1487 -0.9301 -0.0472 -0.4344 1487 VAL C CA 13016 C C . VAL C 71 ? 2.9317 2.5754 1.2170 -0.9361 -0.0351 -0.4510 1487 VAL C C 13017 O O . VAL C 71 ? 2.9859 2.6461 1.3431 -0.8945 -0.0801 -0.4932 1487 VAL C O 13018 C CB . VAL C 71 ? 2.8767 2.7068 1.1555 -0.9062 -0.0473 -0.5057 1487 VAL C CB 13019 C CG1 . VAL C 71 ? 2.9616 2.8537 1.2367 -0.8420 -0.1217 -0.5606 1487 VAL C CG1 13020 C CG2 . VAL C 71 ? 2.6710 2.5692 1.1563 -0.9218 0.0074 -0.5458 1487 VAL C CG2 13021 N N . TYR C 72 ? 2.8533 2.4626 1.1767 -0.9850 0.0272 -0.4189 1488 TYR C N 13022 C CA . TYR C 72 ? 2.6341 2.2101 1.0683 -0.9920 0.0484 -0.4213 1488 TYR C CA 13023 C C . TYR C 72 ? 2.4404 2.1299 1.0757 -0.9834 0.0982 -0.4622 1488 TYR C C 13024 O O . TYR C 72 ? 2.3814 2.1197 1.0478 -1.0155 0.1574 -0.4489 1488 TYR C O 13025 C CB . TYR C 72 ? 2.7276 2.1957 1.0683 -1.0465 0.0875 -0.3600 1488 TYR C CB 13026 C CG . TYR C 72 ? 2.8961 2.2182 1.0843 -1.0382 0.0499 -0.3072 1488 TYR C CG 13027 C CD1 . TYR C 72 ? 2.8286 2.0912 1.0860 -0.9979 0.0179 -0.2987 1488 TYR C CD1 13028 C CD2 . TYR C 72 ? 3.0896 2.3360 1.0960 -1.0547 0.0548 -0.2526 1488 TYR C CD2 13029 C CE1 . TYR C 72 ? 3.0854 2.2162 1.2338 -0.9737 -0.0090 -0.2372 1488 TYR C CE1 13030 C CE2 . TYR C 72 ? 3.2625 2.3712 1.1551 -1.0284 0.0333 -0.1883 1488 TYR C CE2 13031 C CZ . TYR C 72 ? 3.2575 2.3091 1.2220 -0.9878 0.0015 -0.1809 1488 TYR C CZ 13032 O OH . TYR C 72 ? 3.4174 2.3277 1.2671 -0.9588 -0.0147 -0.1150 1488 TYR C OH 13033 N N . ALA C 73 ? 2.3496 2.0738 1.1180 -0.9356 0.0754 -0.5084 1489 ALA C N 13034 C CA . ALA C 73 ? 2.1769 1.9879 1.1337 -0.9133 0.1255 -0.5425 1489 ALA C CA 13035 C C . ALA C 73 ? 2.0970 1.8615 1.1107 -0.9169 0.1570 -0.5112 1489 ALA C C 13036 O O . ALA C 73 ? 2.3642 2.0599 1.3923 -0.8943 0.1194 -0.5053 1489 ALA C O 13037 C CB . ALA C 73 ? 2.3271 2.1928 1.4064 -0.8569 0.0923 -0.6066 1489 ALA C CB 13038 N N . VAL C 74 ? 2.0216 1.8306 1.0675 -0.9422 0.2251 -0.4920 1490 VAL C N 13039 C CA . VAL C 74 ? 1.9580 1.7391 1.0385 -0.9466 0.2577 -0.4612 1490 VAL C CA 13040 C C . VAL C 74 ? 1.9380 1.7960 1.1849 -0.8982 0.3029 -0.4883 1490 VAL C C 13041 O O . VAL C 74 ? 1.7303 1.6737 1.0262 -0.9024 0.3605 -0.5035 1490 VAL C O 13042 C CB . VAL C 74 ? 1.9957 1.7775 0.9847 -1.0082 0.3033 -0.4222 1490 VAL C CB 13043 C CG1 . VAL C 74 ? 1.9796 1.8499 0.9722 -1.0309 0.3395 -0.4338 1490 VAL C CG1 13044 C CG2 . VAL C 74 ? 1.8995 1.7037 0.9522 -1.0029 0.3511 -0.4071 1490 VAL C CG2 13045 N N . THR C 75 ? 1.4331 0.9274 1.2535 -0.3453 -0.4893 -0.0705 1491 THR C N 13046 C CA . THR C 75 ? 1.2405 0.8450 1.3093 -0.3383 -0.4445 -0.0682 1491 THR C CA 13047 C C . THR C 75 ? 1.4287 0.9509 1.4719 -0.2936 -0.3870 -0.0052 1491 THR C C 13048 O O . THR C 75 ? 1.8175 1.2798 1.8222 -0.2273 -0.4118 0.0341 1491 THR C O 13049 C CB . THR C 75 ? 1.2519 1.0096 1.5903 -0.2958 -0.4931 -0.0982 1491 THR C CB 13050 O OG1 . THR C 75 ? 1.3025 1.0365 1.6237 -0.2149 -0.5462 -0.0736 1491 THR C OG1 13051 C CG2 . THR C 75 ? 1.4565 1.3258 1.8274 -0.3255 -0.5154 -0.1624 1491 THR C CG2 13052 N N . GLY C 76 ? 1.1732 0.6994 1.2338 -0.3234 -0.3114 0.0016 1492 GLY C N 13053 C CA . GLY C 76 ? 1.1697 0.6461 1.2381 -0.2792 -0.2528 0.0544 1492 GLY C CA 13054 C C . GLY C 76 ? 1.1276 0.6380 1.2030 -0.3128 -0.1759 0.0436 1492 GLY C C 13055 O O . GLY C 76 ? 1.2876 0.8280 1.2875 -0.3718 -0.1635 -0.0039 1492 GLY C O 13056 N N . ARG C 77 ? 0.9909 0.5132 1.1550 -0.2619 -0.1209 0.0840 1493 ARG C N 13057 C CA . ARG C 77 ? 0.9675 0.5413 1.1451 -0.2705 -0.0483 0.0744 1493 ARG C CA 13058 C C . ARG C 77 ? 1.1725 0.6828 1.2597 -0.2375 0.0074 0.1089 1493 ARG C C 13059 O O . ARG C 77 ? 1.4481 0.9272 1.3742 -0.2788 0.0422 0.0783 1493 ARG C O 13060 C CB . ARG C 77 ? 0.8528 0.5416 1.2711 -0.2321 -0.0199 0.0807 1493 ARG C CB 13061 C CG . ARG C 77 ? 0.8615 0.6349 1.2707 -0.2618 0.0151 0.0365 1493 ARG C CG 13062 C CD . ARG C 77 ? 0.6899 0.5142 1.0784 -0.3062 -0.0326 -0.0148 1493 ARG C CD 13063 N NE . ARG C 77 ? 0.8906 0.8102 1.4243 -0.2681 -0.0073 -0.0198 1493 ARG C NE 13064 C CZ . ARG C 77 ? 0.9461 0.9163 1.4774 -0.2557 0.0386 -0.0285 1493 ARG C CZ 13065 N NH1 . ARG C 77 ? 0.7980 0.7633 1.2111 -0.2783 0.0584 -0.0389 1493 ARG C NH1 13066 N NH2 . ARG C 77 ? 1.0121 1.0333 1.6660 -0.2157 0.0674 -0.0320 1493 ARG C NH2 13067 N N . GLY C 78 ? 1.0677 0.5674 1.2677 -0.1651 0.0180 0.1646 1494 GLY C N 13068 C CA . GLY C 78 ? 1.1317 0.5814 1.2721 -0.1251 0.0708 0.2002 1494 GLY C CA 13069 C C . GLY C 78 ? 1.1891 0.4976 1.1426 -0.1400 0.0491 0.2130 1494 GLY C C 13070 O O . GLY C 78 ? 1.1564 0.4019 0.9669 -0.1967 0.0142 0.1816 1494 GLY C O 13071 N N . ASP C 79 ? 1.0897 0.3789 1.0305 -0.0866 0.0581 0.2460 1495 ASP C N 13072 C CA . ASP C 79 ? 1.3205 0.5244 1.1380 -0.0867 0.0514 0.2579 1495 ASP C CA 13073 C C . ASP C 79 ? 1.4361 0.5836 1.2760 -0.0511 -0.0008 0.2867 1495 ASP C C 13074 O O . ASP C 79 ? 1.4786 0.6383 1.3937 0.0143 -0.0142 0.3047 1495 ASP C O 13075 C CB . ASP C 79 ? 1.3373 0.5568 1.1503 -0.0494 0.0754 0.2744 1495 ASP C CB 13076 C CG . ASP C 79 ? 1.3161 0.4593 1.0591 -0.0270 0.0598 0.2996 1495 ASP C CG 13077 O OD1 . ASP C 79 ? 1.4427 0.4890 1.0208 -0.0582 0.0673 0.2793 1495 ASP C OD1 13078 O OD2 . ASP C 79 ? 1.3035 0.4671 1.1185 0.0172 0.0326 0.3277 1495 ASP C OD2 13079 N N . SER C 80 ? 1.6642 0.7211 1.3362 -0.0962 -0.0403 0.2632 1496 SER C N 13080 C CA . SER C 80 ? 1.7115 0.7034 1.3540 -0.0709 -0.1234 0.2808 1496 SER C CA 13081 C C . SER C 80 ? 1.8206 0.7167 1.2521 -0.1412 -0.1432 0.2450 1496 SER C C 13082 O O . SER C 80 ? 1.5724 0.5083 0.9747 -0.2160 -0.1115 0.1967 1496 SER C O 13083 C CB . SER C 80 ? 1.5564 0.6898 1.4487 -0.0450 -0.1775 0.2723 1496 SER C CB 13084 O OG . SER C 80 ? 1.4573 0.6931 1.4260 -0.1068 -0.1611 0.2240 1496 SER C OG 13085 N N . PRO C 81 ? 2.0144 0.7967 1.2968 -0.1104 -0.1907 0.2647 1497 PRO C N 13086 C CA . PRO C 81 ? 2.1356 0.8454 1.2292 -0.1700 -0.2044 0.2280 1497 PRO C CA 13087 C C . PRO C 81 ? 1.9633 0.8400 1.2134 -0.2030 -0.2603 0.1763 1497 PRO C C 13088 O O . PRO C 81 ? 1.9091 0.9265 1.3882 -0.1559 -0.3056 0.1773 1497 PRO C O 13089 C CB . PRO C 81 ? 2.3800 0.9555 1.3093 -0.0959 -0.2482 0.2697 1497 PRO C CB 13090 C CG . PRO C 81 ? 2.3292 0.9365 1.3612 -0.0112 -0.2283 0.3123 1497 PRO C CG 13091 C CD . PRO C 81 ? 2.1269 0.8760 1.4157 -0.0116 -0.2278 0.3122 1497 PRO C CD 13092 N N . ALA C 82 ? 2.0438 0.9076 1.1835 -0.2844 -0.2523 0.1271 1498 ALA C N 13093 C CA . ALA C 82 ? 2.1194 1.1369 1.4055 -0.3116 -0.3082 0.0783 1498 ALA C CA 13094 C C . ALA C 82 ? 2.3647 1.3376 1.5302 -0.2891 -0.3810 0.0704 1498 ALA C C 13095 O O . ALA C 82 ? 2.5137 1.3808 1.4660 -0.3397 -0.3693 0.0509 1498 ALA C O 13096 C CB . ALA C 82 ? 2.0917 1.1566 1.3625 -0.4079 -0.2617 0.0233 1498 ALA C CB 13097 N N . SER C 83 ? 2.3574 1.4249 1.6725 -0.2094 -0.4536 0.0795 1499 SER C N 13098 C CA . SER C 83 ? 2.3890 1.4546 1.6268 -0.1534 -0.5373 0.0713 1499 SER C CA 13099 C C . SER C 83 ? 2.3317 1.5274 1.7918 -0.0597 -0.5947 0.0787 1499 SER C C 13100 O O . SER C 83 ? 2.2677 1.5173 1.9046 -0.0475 -0.5581 0.0980 1499 SER C O 13101 C CB . SER C 83 ? 2.5716 1.4119 1.4826 -0.1217 -0.5192 0.1159 1499 SER C CB 13102 O OG . SER C 83 ? 2.6011 1.3301 1.3124 -0.2145 -0.4678 0.0927 1499 SER C OG 13103 N N . SER C 84 ? 2.4052 1.6589 1.8589 0.0102 -0.6820 0.0583 1500 SER C N 13104 C CA . SER C 84 ? 2.3907 1.7426 2.0052 0.1134 -0.7337 0.0650 1500 SER C CA 13105 C C . SER C 84 ? 2.5395 1.7599 1.9060 0.2183 -0.7743 0.1086 1500 SER C C 13106 O O . SER C 84 ? 2.7146 1.7931 1.9649 0.2663 -0.7330 0.1751 1500 SER C O 13107 C CB . SER C 84 ? 2.3203 1.9148 2.2124 0.1187 -0.8049 -0.0177 1500 SER C CB 13108 O OG . SER C 84 ? 2.4211 2.0463 2.2006 0.1158 -0.8705 -0.0647 1500 SER C OG 13109 N N . LYS C 85 ? 2.5498 1.8135 1.8256 0.2587 -0.8515 0.0714 1501 LYS C N 13110 C CA . LYS C 85 ? 2.8097 1.9203 1.7874 0.3603 -0.8814 0.1153 1501 LYS C CA 13111 C C . LYS C 85 ? 2.8723 1.9757 1.6873 0.3441 -0.9242 0.0765 1501 LYS C C 13112 O O . LYS C 85 ? 2.7184 2.0163 1.7210 0.3007 -0.9766 -0.0015 1501 LYS C O 13113 C CB . LYS C 85 ? 2.9225 2.1435 1.9932 0.5045 -0.9602 0.1135 1501 LYS C CB 13114 C CG . LYS C 85 ? 2.9130 2.0386 1.9902 0.5558 -0.9116 0.1827 1501 LYS C CG 13115 C CD . LYS C 85 ? 2.9524 2.2014 2.1202 0.7028 -0.9948 0.1719 1501 LYS C CD 13116 C CE . LYS C 85 ? 2.9845 2.1404 2.1620 0.7448 -0.9348 0.2399 1501 LYS C CE 13117 N NZ . LYS C 85 ? 3.0197 2.3266 2.3101 0.8586 -0.9785 0.2170 1501 LYS C NZ 13118 N N . PRO C 86 ? 3.0899 1.9606 1.5525 0.3785 -0.8943 0.1302 1502 PRO C N 13119 C CA . PRO C 86 ? 3.2102 2.0666 1.4950 0.3881 -0.9393 0.0991 1502 PRO C CA 13120 C C . PRO C 86 ? 3.3408 2.3858 1.7100 0.5192 -1.0362 0.0577 1502 PRO C C 13121 O O . PRO C 86 ? 3.4656 2.5025 1.8137 0.6366 -1.0456 0.0917 1502 PRO C O 13122 C CB . PRO C 86 ? 3.4283 1.9983 1.3888 0.3846 -0.8231 0.1672 1502 PRO C CB 13123 C CG . PRO C 86 ? 3.5338 1.9958 1.4744 0.4427 -0.7699 0.2323 1502 PRO C CG 13124 C CD . PRO C 86 ? 3.2945 1.8935 1.5041 0.4011 -0.8042 0.2189 1502 PRO C CD 13125 N N . ILE C 87 ? 2.2909 2.8797 1.8617 0.3781 0.8041 0.5561 1503 ILE C N 13126 C CA . ILE C 87 ? 2.3226 2.9392 1.8111 0.2560 0.7985 0.5099 1503 ILE C CA 13127 C C . ILE C 87 ? 2.3146 3.0007 1.7953 0.2952 0.8008 0.5530 1503 ILE C C 13128 O O . ILE C 87 ? 2.1823 2.8946 1.7275 0.4116 0.8041 0.6149 1503 ILE C O 13129 C CB . ILE C 87 ? 2.5774 2.9477 1.7992 0.1783 0.8803 0.4287 1503 ILE C CB 13130 C CG1 . ILE C 87 ? 2.6076 2.8370 1.7957 0.2044 0.9098 0.4045 1503 ILE C CG1 13131 C CG2 . ILE C 87 ? 2.5882 3.0219 1.7845 0.0320 0.8510 0.3728 1503 ILE C CG2 13132 C CD1 . ILE C 87 ? 2.6777 2.7937 1.7423 0.0857 0.9311 0.3227 1503 ILE C CD1 13133 N N . SER C 88 ? 2.4140 3.1229 1.8105 0.2023 0.8020 0.5211 1504 SER C N 13134 C CA . SER C 88 ? 2.3672 3.1942 1.8055 0.2312 0.7839 0.5669 1504 SER C CA 13135 C C . SER C 88 ? 2.5100 3.3265 1.8177 0.1238 0.7981 0.5233 1504 SER C C 13136 O O . SER C 88 ? 2.5935 3.3599 1.8183 0.0107 0.8030 0.4584 1504 SER C O 13137 C CB . SER C 88 ? 2.1018 3.2114 1.8345 0.2609 0.6813 0.6295 1504 SER C CB 13138 O OG . SER C 88 ? 2.0901 3.3195 1.8718 0.2930 0.6617 0.6765 1504 SER C OG 13139 N N . ILE C 89 ? 2.5341 3.3993 1.8261 0.1628 0.8047 0.5610 1505 ILE C N 13140 C CA . ILE C 89 ? 2.7344 3.6058 1.9149 0.0755 0.8161 0.5307 1505 ILE C CA 13141 C C . ILE C 89 ? 2.6767 3.7819 2.0332 0.1006 0.7492 0.5917 1505 ILE C C 13142 O O . ILE C 89 ? 2.5607 3.7916 2.0949 0.1979 0.7079 0.6585 1505 ILE C O 13143 C CB . ILE C 89 ? 2.9949 3.6221 1.8988 0.0945 0.9195 0.5036 1505 ILE C CB 13144 C CG1 . ILE C 89 ? 2.9281 3.5313 1.8420 0.2346 0.9473 0.5703 1505 ILE C CG1 13145 C CG2 . ILE C 89 ? 3.1802 3.5691 1.8959 0.0632 0.9890 0.4395 1505 ILE C CG2 13146 C CD1 . ILE C 89 ? 3.1242 3.4941 1.7747 0.2615 1.0476 0.5489 1505 ILE C CD1 13147 N N . ASN C 90 ? 2.7197 3.8828 2.0265 0.0128 0.7386 0.5686 1506 ASN C N 13148 C CA . ASN C 90 ? 2.5103 3.8780 1.9563 0.0320 0.6834 0.6224 1506 ASN C CA 13149 C C . ASN C 90 ? 2.7208 3.9971 1.9770 0.0083 0.7387 0.6071 1506 ASN C C 13150 O O . ASN C 90 ? 2.8740 4.0812 1.9901 -0.1002 0.7617 0.5463 1506 ASN C O 13151 C CB . ASN C 90 ? 2.3052 3.9090 1.9500 -0.0578 0.5874 0.6193 1506 ASN C CB 13152 C CG . ASN C 90 ? 2.0996 3.8378 1.9723 -0.0187 0.5204 0.6509 1506 ASN C CG 13153 O OD1 . ASN C 90 ? 1.8519 3.7609 1.9222 0.0605 0.4653 0.7190 1506 ASN C OD1 13154 N ND2 . ASN C 90 ? 2.1768 3.8380 2.0230 -0.0742 0.5247 0.6014 1506 ASN C ND2 13155 N N . TYR C 91 ? 2.7917 4.0681 2.0442 0.1105 0.7599 0.6625 1507 TYR C N 13156 C CA . TYR C 91 ? 3.0589 4.2377 2.1275 0.1030 0.8176 0.6532 1507 TYR C CA 13157 C C . TYR C 91 ? 2.9304 4.2697 2.1255 0.1812 0.7822 0.7271 1507 TYR C C 13158 O O . TYR C 91 ? 2.7965 4.2348 2.1576 0.2822 0.7477 0.7893 1507 TYR C O 13159 C CB . TYR C 91 ? 3.3477 4.2441 2.1716 0.1524 0.9227 0.6267 1507 TYR C CB 13160 C CG . TYR C 91 ? 3.5777 4.3392 2.1768 0.1245 0.9912 0.6006 1507 TYR C CG 13161 C CD1 . TYR C 91 ? 3.7259 4.4036 2.1680 0.0003 1.0170 0.5293 1507 TYR C CD1 13162 C CD2 . TYR C 91 ? 3.6156 4.3247 2.1659 0.2190 1.0241 0.6416 1507 TYR C CD2 13163 C CE1 . TYR C 91 ? 3.9027 4.4562 2.1385 -0.0257 1.0798 0.5050 1507 TYR C CE1 13164 C CE2 . TYR C 91 ? 3.7948 4.3710 2.1587 0.1855 1.0726 0.6073 1507 TYR C CE2 13165 C CZ . TYR C 91 ? 3.9364 4.4400 2.1360 0.0664 1.1063 0.5438 1507 TYR C CZ 13166 O OH . TYR C 91 ? 4.1100 4.4910 2.1335 0.0303 1.1499 0.5090 1507 TYR C OH 13167 N N . ARG C 92 ? 2.9420 4.3059 2.0574 0.1343 0.7913 0.7198 1508 ARG C N 13168 C CA . ARG C 92 ? 2.7454 4.2640 1.9723 0.1982 0.7577 0.7861 1508 ARG C CA 13169 C C . ARG C 92 ? 2.8616 4.2117 1.8883 0.2475 0.8356 0.7877 1508 ARG C C 13170 O O . ARG C 92 ? 3.0381 4.1810 1.8330 0.1974 0.9080 0.7288 1508 ARG C O 13171 C CB . ARG C 92 ? 2.5926 4.3280 1.9450 0.1039 0.6823 0.7843 1508 ARG C CB 13172 C CG . ARG C 92 ? 2.3173 4.2597 1.9148 0.0703 0.5885 0.7964 1508 ARG C CG 13173 C CD . ARG C 92 ? 2.1546 4.3225 1.8857 -0.0082 0.5133 0.8047 1508 ARG C CD 13174 N NE . ARG C 92 ? 2.3199 4.4196 1.8971 -0.1396 0.5352 0.7338 1508 ARG C NE 13175 C CZ . ARG C 92 ? 2.3315 4.4664 1.9397 -0.2457 0.5022 0.6834 1508 ARG C CZ 13176 N NH1 . ARG C 92 ? 2.1807 4.4186 1.9685 -0.2359 0.4456 0.6961 1508 ARG C NH1 13177 N NH2 . ARG C 92 ? 2.4624 4.5300 1.9222 -0.3615 0.5258 0.6203 1508 ARG C NH2 13178 N N . THR C 93 ? 2.7612 4.1853 1.8923 0.3414 0.8088 0.8448 1509 THR C N 13179 C CA . THR C 93 ? 2.9449 4.2125 1.9249 0.3896 0.8627 0.8414 1509 THR C CA 13180 C C . THR C 93 ? 2.9805 4.3385 1.9342 0.3262 0.8474 0.8384 1509 THR C C 13181 O O . THR C 93 ? 2.7842 4.3521 1.9187 0.3493 0.7804 0.8890 1509 THR C O 13182 C CB . THR C 93 ? 2.8574 4.1423 1.9553 0.5298 0.8455 0.9028 1509 THR C CB 13183 O OG1 . THR C 93 ? 2.7719 3.9698 1.8955 0.5900 0.8585 0.9049 1509 THR C OG1 13184 C CG2 . THR C 93 ? 3.0663 4.1860 2.0072 0.5741 0.9006 0.8952 1509 THR C CG2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 PHE 1 1 1 PHE PHE A . n A 1 2 ASN 2 2 2 ASN ASN A . n A 1 3 LEU 3 3 3 LEU LEU A . n A 1 4 ASP 4 4 4 ASP ASP A . n A 1 5 VAL 5 5 5 VAL VAL A . n A 1 6 ASP 6 6 6 ASP ASP A . n A 1 7 SER 7 7 7 SER SER A . n A 1 8 PRO 8 8 8 PRO PRO A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 GLU 10 10 10 GLU GLU A . n A 1 11 TYR 11 11 11 TYR TYR A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 GLY 13 13 13 GLY GLY A . n A 1 14 PRO 14 14 14 PRO PRO A . n A 1 15 GLU 15 15 15 GLU GLU A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 SER 17 17 17 SER SER A . n A 1 18 TYR 18 18 18 TYR TYR A . n A 1 19 PHE 19 19 19 PHE PHE A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 PHE 21 21 21 PHE PHE A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 VAL 23 23 23 VAL VAL A . n A 1 24 ASP 24 24 24 ASP ASP A . n A 1 25 PHE 25 25 25 PHE PHE A . n A 1 26 PHE 26 26 26 PHE PHE A . n A 1 27 VAL 27 27 27 VAL VAL A . n A 1 28 PRO 28 28 28 PRO PRO A . n A 1 29 SER 29 29 29 SER SER A . n A 1 30 ALA 30 30 30 ALA ALA A . n A 1 31 SER 31 31 31 SER SER A . n A 1 32 SER 32 32 32 SER SER A . n A 1 33 ARG 33 33 33 ARG ARG A . n A 1 34 MET 34 34 34 MET MET A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 LEU 37 37 37 LEU LEU A . n A 1 38 VAL 38 38 38 VAL VAL A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 ALA 40 40 40 ALA ALA A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 LYS 42 42 42 LYS LYS A . n A 1 43 ALA 43 43 43 ALA ALA A . n A 1 44 ASN 44 44 44 ASN ASN A . n A 1 45 THR 45 45 45 THR THR A . n A 1 46 THR 46 46 46 THR THR A . n A 1 47 GLN 47 47 47 GLN GLN A . n A 1 48 PRO 48 48 48 PRO PRO A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 VAL 51 51 51 VAL VAL A . n A 1 52 GLU 52 52 52 GLU GLU A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 GLY 54 54 54 GLY GLY A . n A 1 55 GLN 55 55 55 GLN GLN A . n A 1 56 VAL 56 56 56 VAL VAL A . n A 1 57 LEU 57 57 57 LEU LEU A . n A 1 58 LYS 58 58 58 LYS LYS A . n A 1 59 CYS 59 59 59 CYS CYS A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 TRP 61 61 61 TRP TRP A . n A 1 62 SER 62 62 62 SER SER A . n A 1 63 SER 63 63 63 SER SER A . n A 1 64 THR 64 64 64 THR THR A . n A 1 65 ARG 65 65 65 ARG ARG A . n A 1 66 ARG 66 66 66 ARG ARG A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 GLN 68 68 68 GLN GLN A . n A 1 69 PRO 69 69 69 PRO PRO A . n A 1 70 ILE 70 70 70 ILE ILE A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 PHE 72 72 72 PHE PHE A . n A 1 73 ASP 73 73 73 ASP ASP A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 THR 75 75 75 THR THR A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 ASN 77 77 77 ASN ASN A . n A 1 78 ARG 78 78 78 ARG ARG A . n A 1 79 ASP 79 79 79 ASP ASP A . n A 1 80 TYR 80 80 80 TYR TYR A . n A 1 81 ALA 81 81 81 ALA ALA A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ASP 83 83 83 ASP ASP A . n A 1 84 ASP 84 84 84 ASP ASP A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 GLU 87 87 87 GLU GLU A . n A 1 88 PHE 88 88 88 PHE PHE A . n A 1 89 LYS 89 89 89 LYS LYS A . n A 1 90 SER 90 90 90 SER SER A . n A 1 91 HIS 91 91 91 HIS HIS A . n A 1 92 GLN 92 92 92 GLN GLN A . n A 1 93 TRP 93 93 93 TRP TRP A . n A 1 94 PHE 94 94 94 PHE PHE A . n A 1 95 GLY 95 95 95 GLY GLY A . n A 1 96 ALA 96 96 96 ALA ALA A . n A 1 97 SER 97 97 97 SER SER A . n A 1 98 VAL 98 98 98 VAL VAL A . n A 1 99 ARG 99 99 99 ARG ARG A . n A 1 100 SER 100 100 100 SER SER A . n A 1 101 LYS 101 101 101 LYS LYS A . n A 1 102 GLN 102 102 102 GLN GLN A . n A 1 103 ASP 103 103 103 ASP ASP A . n A 1 104 LYS 104 104 104 LYS LYS A . n A 1 105 ILE 105 105 105 ILE ILE A . n A 1 106 LEU 106 106 106 LEU LEU A . n A 1 107 ALA 107 107 107 ALA ALA A . n A 1 108 CYS 108 108 108 CYS CYS A . n A 1 109 ALA 109 109 109 ALA ALA A . n A 1 110 PRO 110 110 110 PRO PRO A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 TYR 112 112 112 TYR TYR A . n A 1 113 HIS 113 113 113 HIS HIS A . n A 1 114 TRP 114 114 114 TRP TRP A . n A 1 115 ARG 115 115 115 ARG ARG A . n A 1 116 THR 116 116 116 THR THR A . n A 1 117 GLU 117 117 117 GLU GLU A . n A 1 118 MET 118 118 118 MET MET A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 GLN 120 120 120 GLN GLN A . n A 1 121 GLU 121 121 121 GLU GLU A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 PRO 124 124 124 PRO PRO A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 GLY 126 126 126 GLY GLY A . n A 1 127 THR 127 127 127 THR THR A . n A 1 128 CYS 128 128 128 CYS CYS A . n A 1 129 PHE 129 129 129 PHE PHE A . n A 1 130 LEU 130 130 130 LEU LEU A . n A 1 131 GLN 131 131 131 GLN GLN A . n A 1 132 ASP 132 132 132 ASP ASP A . n A 1 133 GLY 133 133 133 GLY GLY A . n A 1 134 THR 134 134 134 THR THR A . n A 1 135 LYS 135 135 135 LYS LYS A . n A 1 136 THR 136 136 136 THR THR A . n A 1 137 VAL 137 137 137 VAL VAL A . n A 1 138 GLU 138 138 138 GLU GLU A . n A 1 139 TYR 139 139 139 TYR TYR A . n A 1 140 ALA 140 140 140 ALA ALA A . n A 1 141 PRO 141 141 141 PRO PRO A . n A 1 142 CYS 142 142 142 CYS CYS A . n A 1 143 ARG 143 143 143 ARG ARG A . n A 1 144 SER 144 144 144 SER SER A . n A 1 145 GLN 145 145 145 GLN GLN A . n A 1 146 ASP 146 146 146 ASP ASP A . n A 1 147 ILE 147 147 147 ILE ILE A . n A 1 148 ASP 148 148 148 ASP ASP A . n A 1 149 ALA 149 149 149 ALA ALA A . n A 1 150 ASP 150 150 150 ASP ASP A . n A 1 151 GLY 151 151 151 GLY GLY A . n A 1 152 GLN 152 152 152 GLN GLN A . n A 1 153 GLY 153 153 153 GLY GLY A . n A 1 154 PHE 154 154 154 PHE PHE A . n A 1 155 CYS 155 155 155 CYS CYS A . n A 1 156 GLN 156 156 156 GLN GLN A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 GLY 158 158 158 GLY GLY A . n A 1 159 PHE 159 159 159 PHE PHE A . n A 1 160 SER 160 160 160 SER SER A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 ASP 162 162 162 ASP ASP A . n A 1 163 PHE 163 163 163 PHE PHE A . n A 1 164 THR 164 164 164 THR THR A . n A 1 165 LYS 165 165 165 LYS LYS A . n A 1 166 ALA 166 166 166 ALA ALA A . n A 1 167 ASP 167 167 167 ASP ASP A . n A 1 168 ARG 168 168 168 ARG ARG A . n A 1 169 VAL 169 169 169 VAL VAL A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 LEU 171 171 171 LEU LEU A . n A 1 172 GLY 172 172 172 GLY GLY A . n A 1 173 GLY 173 173 173 GLY GLY A . n A 1 174 PRO 174 174 174 PRO PRO A . n A 1 175 GLY 175 175 175 GLY GLY A . n A 1 176 SER 176 176 176 SER SER A . n A 1 177 PHE 177 177 177 PHE PHE A . n A 1 178 TYR 178 178 178 TYR TYR A . n A 1 179 TRP 179 179 179 TRP TRP A . n A 1 180 GLN 180 180 180 GLN GLN A . n A 1 181 GLY 181 181 181 GLY GLY A . n A 1 182 GLN 182 182 182 GLN GLN A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 ILE 184 184 184 ILE ILE A . n A 1 185 SER 185 185 185 SER SER A . n A 1 186 ASP 186 186 186 ASP ASP A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 VAL 188 188 188 VAL VAL A . n A 1 189 ALA 189 189 189 ALA ALA A . n A 1 190 GLU 190 190 190 GLU GLU A . n A 1 191 ILE 191 191 191 ILE ILE A . n A 1 192 VAL 192 192 192 VAL VAL A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LYS 194 194 194 LYS LYS A . n A 1 195 TYR 195 195 195 TYR TYR A . n A 1 196 ASP 196 196 196 ASP ASP A . n A 1 197 PRO 197 197 197 PRO PRO A . n A 1 198 ASN 198 198 198 ASN ASN A . n A 1 199 VAL 199 199 199 VAL VAL A . n A 1 200 TYR 200 200 200 TYR TYR A . n A 1 201 SER 201 201 201 SER SER A . n A 1 202 ILE 202 202 202 ILE ILE A . n A 1 203 LYS 203 203 203 LYS LYS A . n A 1 204 TYR 204 204 204 TYR TYR A . n A 1 205 ASN 205 205 205 ASN ASN A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 LEU 208 208 208 LEU LEU A . n A 1 209 ALA 209 209 209 ALA ALA A . n A 1 210 THR 210 210 210 THR THR A . n A 1 211 ARG 211 211 211 ARG ARG A . n A 1 212 THR 212 212 212 THR THR A . n A 1 213 ALA 213 213 213 ALA ALA A . n A 1 214 GLN 214 214 214 GLN GLN A . n A 1 215 ALA 215 215 215 ALA ALA A . n A 1 216 ILE 216 216 216 ILE ILE A . n A 1 217 PHE 217 217 217 PHE PHE A . n A 1 218 ASP 218 218 218 ASP ASP A . n A 1 219 ASP 219 219 219 ASP ASP A . n A 1 220 SER 220 220 220 SER SER A . n A 1 221 TYR 221 221 221 TYR TYR A . n A 1 222 LEU 222 222 222 LEU LEU A . n A 1 223 GLY 223 223 223 GLY GLY A . n A 1 224 TYR 224 224 224 TYR TYR A . n A 1 225 SER 225 225 225 SER SER A . n A 1 226 VAL 226 226 226 VAL VAL A . n A 1 227 ALA 227 227 227 ALA ALA A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 GLY 229 229 229 GLY GLY A . n A 1 230 ASP 230 230 230 ASP ASP A . n A 1 231 PHE 231 231 231 PHE PHE A . n A 1 232 ASN 232 232 232 ASN ASN A . n A 1 233 GLY 233 233 233 GLY GLY A . n A 1 234 ASP 234 234 234 ASP ASP A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 ILE 236 236 236 ILE ILE A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ASP 238 238 238 ASP ASP A . n A 1 239 PHE 239 239 239 PHE PHE A . n A 1 240 VAL 240 240 240 VAL VAL A . n A 1 241 SER 241 241 241 SER SER A . n A 1 242 GLY 242 242 242 GLY GLY A . n A 1 243 VAL 243 243 243 VAL VAL A . n A 1 244 PRO 244 244 244 PRO PRO A . n A 1 245 ARG 245 245 245 ARG ARG A . n A 1 246 ALA 246 246 246 ALA ALA A . n A 1 247 ALA 247 247 247 ALA ALA A . n A 1 248 ARG 248 248 248 ARG ARG A . n A 1 249 THR 249 249 249 THR THR A . n A 1 250 LEU 250 250 250 LEU LEU A . n A 1 251 GLY 251 251 251 GLY GLY A . n A 1 252 MET 252 252 252 MET MET A . n A 1 253 VAL 253 253 253 VAL VAL A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 ILE 255 255 255 ILE ILE A . n A 1 256 TYR 256 256 256 TYR TYR A . n A 1 257 ASP 257 257 257 ASP ASP A . n A 1 258 GLY 258 258 258 GLY GLY A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 ASN 260 260 260 ASN ASN A . n A 1 261 MET 261 261 261 MET MET A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 SER 263 263 263 SER SER A . n A 1 264 LEU 264 264 264 LEU LEU A . n A 1 265 TYR 265 265 265 TYR TYR A . n A 1 266 ASN 266 266 266 ASN ASN A . n A 1 267 PHE 267 267 267 PHE PHE A . n A 1 268 THR 268 268 268 THR THR A . n A 1 269 GLY 269 269 269 GLY GLY A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 GLN 271 271 271 GLN GLN A . n A 1 272 MET 272 272 272 MET MET A . n A 1 273 ALA 273 273 273 ALA ALA A . n A 1 274 ALA 274 274 274 ALA ALA A . n A 1 275 TYR 275 275 275 TYR TYR A . n A 1 276 PHE 276 276 276 PHE PHE A . n A 1 277 GLY 277 277 277 GLY GLY A . n A 1 278 PHE 278 278 278 PHE PHE A . n A 1 279 SER 279 279 279 SER SER A . n A 1 280 VAL 280 280 280 VAL VAL A . n A 1 281 ALA 281 281 281 ALA ALA A . n A 1 282 ALA 282 282 282 ALA ALA A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 ASP 284 284 284 ASP ASP A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 GLY 287 287 287 GLY GLY A . n A 1 288 ASP 288 288 288 ASP ASP A . n A 1 289 ASP 289 289 289 ASP ASP A . n A 1 290 TYR 290 290 290 TYR TYR A . n A 1 291 ALA 291 291 291 ALA ALA A . n A 1 292 ASP 292 292 292 ASP ASP A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 PHE 294 294 294 PHE PHE A . n A 1 295 ILE 295 295 295 ILE ILE A . n A 1 296 GLY 296 296 296 GLY GLY A . n A 1 297 ALA 297 297 297 ALA ALA A . n A 1 298 PRO 298 298 298 PRO PRO A . n A 1 299 LEU 299 299 299 LEU LEU A . n A 1 300 PHE 300 300 300 PHE PHE A . n A 1 301 MET 301 301 301 MET MET A . n A 1 302 ASP 302 302 302 ASP ASP A . n A 1 303 ARG 303 303 303 ARG ARG A . n A 1 304 GLY 304 304 304 GLY GLY A . n A 1 305 SER 305 305 305 SER SER A . n A 1 306 ASP 306 306 306 ASP ASP A . n A 1 307 GLY 307 307 307 GLY GLY A . n A 1 308 LYS 308 308 308 LYS LYS A . n A 1 309 LEU 309 309 309 LEU LEU A . n A 1 310 GLN 310 310 310 GLN GLN A . n A 1 311 GLU 311 311 311 GLU GLU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 GLY 313 313 313 GLY GLY A . n A 1 314 GLN 314 314 314 GLN GLN A . n A 1 315 VAL 315 315 315 VAL VAL A . n A 1 316 SER 316 316 316 SER SER A . n A 1 317 VAL 317 317 317 VAL VAL A . n A 1 318 SER 318 318 318 SER SER A . n A 1 319 LEU 319 319 319 LEU LEU A . n A 1 320 GLN 320 320 320 GLN GLN A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 ALA 322 322 322 ALA ALA A . n A 1 323 SER 323 323 323 SER SER A . n A 1 324 GLY 324 324 324 GLY GLY A . n A 1 325 ASP 325 325 325 ASP ASP A . n A 1 326 PHE 326 326 326 PHE PHE A . n A 1 327 GLN 327 327 327 GLN GLN A . n A 1 328 THR 328 328 328 THR THR A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 LYS 330 330 330 LYS LYS A . n A 1 331 LEU 331 331 331 LEU LEU A . n A 1 332 ASN 332 332 332 ASN ASN A . n A 1 333 GLY 333 333 333 GLY GLY A . n A 1 334 PHE 334 334 334 PHE PHE A . n A 1 335 GLU 335 335 335 GLU GLU A . n A 1 336 VAL 336 336 336 VAL VAL A . n A 1 337 PHE 337 337 337 PHE PHE A . n A 1 338 ALA 338 338 338 ALA ALA A . n A 1 339 ARG 339 339 339 ARG ARG A . n A 1 340 PHE 340 340 340 PHE PHE A . n A 1 341 GLY 341 341 341 GLY GLY A . n A 1 342 SER 342 342 342 SER SER A . n A 1 343 ALA 343 343 343 ALA ALA A . n A 1 344 ILE 344 344 344 ILE ILE A . n A 1 345 ALA 345 345 345 ALA ALA A . n A 1 346 PRO 346 346 346 PRO PRO A . n A 1 347 LEU 347 347 347 LEU LEU A . n A 1 348 GLY 348 348 348 GLY GLY A . n A 1 349 ASP 349 349 349 ASP ASP A . n A 1 350 LEU 350 350 350 LEU LEU A . n A 1 351 ASP 351 351 351 ASP ASP A . n A 1 352 GLN 352 352 352 GLN GLN A . n A 1 353 ASP 353 353 353 ASP ASP A . n A 1 354 GLY 354 354 354 GLY GLY A . n A 1 355 PHE 355 355 355 PHE PHE A . n A 1 356 ASN 356 356 356 ASN ASN A . n A 1 357 ASP 357 357 357 ASP ASP A . n A 1 358 ILE 358 358 358 ILE ILE A . n A 1 359 ALA 359 359 359 ALA ALA A . n A 1 360 ILE 360 360 360 ILE ILE A . n A 1 361 ALA 361 361 361 ALA ALA A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 PRO 363 363 363 PRO PRO A . n A 1 364 TYR 364 364 364 TYR TYR A . n A 1 365 GLY 365 365 365 GLY GLY A . n A 1 366 GLY 366 366 366 GLY GLY A . n A 1 367 GLU 367 367 367 GLU GLU A . n A 1 368 ASP 368 368 368 ASP ASP A . n A 1 369 LYS 369 369 369 LYS LYS A . n A 1 370 LYS 370 370 370 LYS LYS A . n A 1 371 GLY 371 371 371 GLY GLY A . n A 1 372 ILE 372 372 372 ILE ILE A . n A 1 373 VAL 373 373 373 VAL VAL A . n A 1 374 TYR 374 374 374 TYR TYR A . n A 1 375 ILE 375 375 375 ILE ILE A . n A 1 376 PHE 376 376 376 PHE PHE A . n A 1 377 ASN 377 377 377 ASN ASN A . n A 1 378 GLY 378 378 378 GLY GLY A . n A 1 379 ARG 379 379 379 ARG ARG A . n A 1 380 SER 380 380 380 SER SER A . n A 1 381 THR 381 381 381 THR THR A . n A 1 382 GLY 382 382 382 GLY GLY A . n A 1 383 LEU 383 383 383 LEU LEU A . n A 1 384 ASN 384 384 384 ASN ASN A . n A 1 385 ALA 385 385 385 ALA ALA A . n A 1 386 VAL 386 386 386 VAL VAL A . n A 1 387 PRO 387 387 387 PRO PRO A . n A 1 388 SER 388 388 388 SER SER A . n A 1 389 GLN 389 389 389 GLN GLN A . n A 1 390 ILE 390 390 390 ILE ILE A . n A 1 391 LEU 391 391 391 LEU LEU A . n A 1 392 GLU 392 392 392 GLU GLU A . n A 1 393 GLY 393 393 393 GLY GLY A . n A 1 394 GLN 394 394 394 GLN GLN A . n A 1 395 TRP 395 395 395 TRP TRP A . n A 1 396 ALA 396 396 396 ALA ALA A . n A 1 397 ALA 397 397 397 ALA ALA A . n A 1 398 ARG 398 398 398 ARG ARG A . n A 1 399 SER 399 399 399 SER SER A . n A 1 400 MET 400 400 400 MET MET A . n A 1 401 PRO 401 401 401 PRO PRO A . n A 1 402 PRO 402 402 402 PRO PRO A . n A 1 403 SER 403 403 403 SER SER A . n A 1 404 PHE 404 404 404 PHE PHE A . n A 1 405 GLY 405 405 405 GLY GLY A . n A 1 406 TYR 406 406 406 TYR TYR A . n A 1 407 SER 407 407 407 SER SER A . n A 1 408 MET 408 408 408 MET MET A . n A 1 409 LYS 409 409 409 LYS LYS A . n A 1 410 GLY 410 410 410 GLY GLY A . n A 1 411 ALA 411 411 411 ALA ALA A . n A 1 412 THR 412 412 412 THR THR A . n A 1 413 ASP 413 413 413 ASP ASP A . n A 1 414 ILE 414 414 414 ILE ILE A . n A 1 415 ASP 415 415 415 ASP ASP A . n A 1 416 LYS 416 416 416 LYS LYS A . n A 1 417 ASN 417 417 417 ASN ASN A . n A 1 418 GLY 418 418 418 GLY GLY A . n A 1 419 TYR 419 419 419 TYR TYR A . n A 1 420 PRO 420 420 420 PRO PRO A . n A 1 421 ASP 421 421 421 ASP ASP A . n A 1 422 LEU 422 422 422 LEU LEU A . n A 1 423 ILE 423 423 423 ILE ILE A . n A 1 424 VAL 424 424 424 VAL VAL A . n A 1 425 GLY 425 425 425 GLY GLY A . n A 1 426 ALA 426 426 426 ALA ALA A . n A 1 427 PHE 427 427 427 PHE PHE A . n A 1 428 GLY 428 428 428 GLY GLY A . n A 1 429 VAL 429 429 429 VAL VAL A . n A 1 430 ASP 430 430 430 ASP ASP A . n A 1 431 ARG 431 431 431 ARG ARG A . n A 1 432 ALA 432 432 432 ALA ALA A . n A 1 433 ILE 433 433 433 ILE ILE A . n A 1 434 LEU 434 434 434 LEU LEU A . n A 1 435 TYR 435 435 435 TYR TYR A . n A 1 436 ARG 436 436 436 ARG ARG A . n A 1 437 ALA 437 437 437 ALA ALA A . n A 1 438 ARG 438 438 438 ARG ARG A . n A 1 439 PRO 439 439 439 PRO PRO A . n A 1 440 VAL 440 440 440 VAL VAL A . n A 1 441 ILE 441 441 441 ILE ILE A . n A 1 442 THR 442 442 442 THR THR A . n A 1 443 VAL 443 443 443 VAL VAL A . n A 1 444 ASN 444 444 444 ASN ASN A . n A 1 445 ALA 445 445 445 ALA ALA A . n A 1 446 GLY 446 446 446 GLY GLY A . n A 1 447 LEU 447 447 447 LEU LEU A . n A 1 448 GLU 448 448 448 GLU GLU A . n A 1 449 VAL 449 449 449 VAL VAL A . n A 1 450 TYR 450 450 450 TYR TYR A . n A 1 451 PRO 451 451 451 PRO PRO A . n A 1 452 SER 452 452 452 SER SER A . n A 1 453 ILE 453 453 453 ILE ILE A . n A 1 454 LEU 454 454 454 LEU LEU A . n A 1 455 ASN 455 455 455 ASN ASN A . n A 1 456 GLN 456 456 456 GLN GLN A . n A 1 457 ASP 457 457 457 ASP ASP A . n A 1 458 ASN 458 458 458 ASN ASN A . n A 1 459 LYS 459 459 459 LYS LYS A . n A 1 460 THR 460 460 460 THR THR A . n A 1 461 CYS 461 461 461 CYS CYS A . n A 1 462 SER 462 462 462 SER SER A . n A 1 463 LEU 463 463 463 LEU LEU A . n A 1 464 PRO 464 464 464 PRO PRO A . n A 1 465 GLY 465 465 465 GLY GLY A . n A 1 466 THR 466 466 466 THR THR A . n A 1 467 ALA 467 467 467 ALA ALA A . n A 1 468 LEU 468 468 468 LEU LEU A . n A 1 469 LYS 469 469 469 LYS LYS A . n A 1 470 VAL 470 470 470 VAL VAL A . n A 1 471 SER 471 471 471 SER SER A . n A 1 472 CYS 472 472 472 CYS CYS A . n A 1 473 PHE 473 473 473 PHE PHE A . n A 1 474 ASN 474 474 474 ASN ASN A . n A 1 475 VAL 475 475 475 VAL VAL A . n A 1 476 ARG 476 476 476 ARG ARG A . n A 1 477 PHE 477 477 477 PHE PHE A . n A 1 478 CYS 478 478 478 CYS CYS A . n A 1 479 LEU 479 479 479 LEU LEU A . n A 1 480 LYS 480 480 480 LYS LYS A . n A 1 481 ALA 481 481 481 ALA ALA A . n A 1 482 ASP 482 482 482 ASP ASP A . n A 1 483 GLY 483 483 483 GLY GLY A . n A 1 484 LYS 484 484 484 LYS LYS A . n A 1 485 GLY 485 485 485 GLY GLY A . n A 1 486 VAL 486 486 486 VAL VAL A . n A 1 487 LEU 487 487 487 LEU LEU A . n A 1 488 PRO 488 488 488 PRO PRO A . n A 1 489 ARG 489 489 489 ARG ARG A . n A 1 490 LYS 490 490 490 LYS LYS A . n A 1 491 LEU 491 491 491 LEU LEU A . n A 1 492 ASN 492 492 492 ASN ASN A . n A 1 493 PHE 493 493 493 PHE PHE A . n A 1 494 GLN 494 494 494 GLN GLN A . n A 1 495 VAL 495 495 495 VAL VAL A . n A 1 496 GLU 496 496 496 GLU GLU A . n A 1 497 LEU 497 497 497 LEU LEU A . n A 1 498 LEU 498 498 498 LEU LEU A . n A 1 499 LEU 499 499 499 LEU LEU A . n A 1 500 ASP 500 500 500 ASP ASP A . n A 1 501 LYS 501 501 501 LYS LYS A . n A 1 502 LEU 502 502 502 LEU LEU A . n A 1 503 LYS 503 503 503 LYS LYS A . n A 1 504 GLN 504 504 504 GLN GLN A . n A 1 505 LYS 505 505 505 LYS LYS A . n A 1 506 GLY 506 506 506 GLY GLY A . n A 1 507 ALA 507 507 507 ALA ALA A . n A 1 508 ILE 508 508 508 ILE ILE A . n A 1 509 ARG 509 509 509 ARG ARG A . n A 1 510 ARG 510 510 510 ARG ARG A . n A 1 511 ALA 511 511 511 ALA ALA A . n A 1 512 LEU 512 512 512 LEU LEU A . n A 1 513 PHE 513 513 513 PHE PHE A . n A 1 514 LEU 514 514 514 LEU LEU A . n A 1 515 TYR 515 515 515 TYR TYR A . n A 1 516 SER 516 516 516 SER SER A . n A 1 517 ARG 517 517 517 ARG ARG A . n A 1 518 SER 518 518 518 SER SER A . n A 1 519 PRO 519 519 519 PRO PRO A . n A 1 520 SER 520 520 520 SER SER A . n A 1 521 HIS 521 521 521 HIS HIS A . n A 1 522 SER 522 522 522 SER SER A . n A 1 523 LYS 523 523 523 LYS LYS A . n A 1 524 ASN 524 524 524 ASN ASN A . n A 1 525 MET 525 525 525 MET MET A . n A 1 526 THR 526 526 526 THR THR A . n A 1 527 ILE 527 527 527 ILE ILE A . n A 1 528 SER 528 528 528 SER SER A . n A 1 529 ARG 529 529 529 ARG ARG A . n A 1 530 GLY 530 530 530 GLY GLY A . n A 1 531 GLY 531 531 531 GLY GLY A . n A 1 532 LEU 532 532 532 LEU LEU A . n A 1 533 MET 533 533 533 MET MET A . n A 1 534 GLN 534 534 534 GLN GLN A . n A 1 535 CYS 535 535 535 CYS CYS A . n A 1 536 GLU 536 536 536 GLU GLU A . n A 1 537 GLU 537 537 537 GLU GLU A . n A 1 538 LEU 538 538 538 LEU LEU A . n A 1 539 ILE 539 539 539 ILE ILE A . n A 1 540 ALA 540 540 540 ALA ALA A . n A 1 541 TYR 541 541 541 TYR TYR A . n A 1 542 LEU 542 542 542 LEU LEU A . n A 1 543 ARG 543 543 543 ARG ARG A . n A 1 544 ASP 544 544 544 ASP ASP A . n A 1 545 GLU 545 545 545 GLU GLU A . n A 1 546 SER 546 546 546 SER SER A . n A 1 547 GLU 547 547 547 GLU GLU A . n A 1 548 PHE 548 548 548 PHE PHE A . n A 1 549 ARG 549 549 549 ARG ARG A . n A 1 550 ASP 550 550 550 ASP ASP A . n A 1 551 LYS 551 551 551 LYS LYS A . n A 1 552 LEU 552 552 552 LEU LEU A . n A 1 553 THR 553 553 553 THR THR A . n A 1 554 PRO 554 554 554 PRO PRO A . n A 1 555 ILE 555 555 555 ILE ILE A . n A 1 556 THR 556 556 556 THR THR A . n A 1 557 ILE 557 557 557 ILE ILE A . n A 1 558 PHE 558 558 558 PHE PHE A . n A 1 559 MET 559 559 559 MET MET A . n A 1 560 GLU 560 560 560 GLU GLU A . n A 1 561 TYR 561 561 561 TYR TYR A . n A 1 562 ARG 562 562 562 ARG ARG A . n A 1 563 LEU 563 563 563 LEU LEU A . n A 1 564 ASP 564 564 564 ASP ASP A . n A 1 565 TYR 565 565 565 TYR TYR A . n A 1 566 ARG 566 566 566 ARG ARG A . n A 1 567 THR 567 567 567 THR THR A . n A 1 568 ALA 568 568 568 ALA ALA A . n A 1 569 ALA 569 569 569 ALA ALA A . n A 1 570 ASP 570 570 570 ASP ASP A . n A 1 571 THR 571 571 571 THR THR A . n A 1 572 THR 572 572 572 THR THR A . n A 1 573 GLY 573 573 573 GLY GLY A . n A 1 574 LEU 574 574 574 LEU LEU A . n A 1 575 GLN 575 575 575 GLN GLN A . n A 1 576 PRO 576 576 576 PRO PRO A . n A 1 577 ILE 577 577 577 ILE ILE A . n A 1 578 LEU 578 578 578 LEU LEU A . n A 1 579 ASN 579 579 579 ASN ASN A . n A 1 580 GLN 580 580 580 GLN GLN A . n A 1 581 PHE 581 581 581 PHE PHE A . n A 1 582 THR 582 582 582 THR THR A . n A 1 583 PRO 583 583 583 PRO PRO A . n A 1 584 ALA 584 584 584 ALA ALA A . n A 1 585 ASN 585 585 585 ASN ASN A . n A 1 586 ILE 586 586 586 ILE ILE A . n A 1 587 SER 587 587 587 SER SER A . n A 1 588 ARG 588 588 588 ARG ARG A . n A 1 589 GLN 589 589 589 GLN GLN A . n A 1 590 ALA 590 590 590 ALA ALA A . n A 1 591 HIS 591 591 591 HIS HIS A . n A 1 592 ILE 592 592 592 ILE ILE A . n A 1 593 LEU 593 593 593 LEU LEU A . n A 1 594 LEU 594 594 594 LEU LEU A . n A 1 595 ASP 595 595 595 ASP ASP A . n A 1 596 CYS 596 596 596 CYS CYS A . n A 1 597 GLY 597 597 597 GLY GLY A . n A 1 598 GLU 598 598 598 GLU GLU A . n A 1 599 ASP 599 599 599 ASP ASP A . n A 1 600 ASN 600 600 600 ASN ASN A . n A 1 601 VAL 601 601 601 VAL VAL A . n A 1 602 CYS 602 602 602 CYS CYS A . n A 1 603 LYS 603 603 603 LYS LYS A . n A 1 604 PRO 604 604 604 PRO PRO A . n A 1 605 LYS 605 605 605 LYS LYS A . n A 1 606 LEU 606 606 606 LEU LEU A . n A 1 607 GLU 607 607 607 GLU GLU A . n A 1 608 VAL 608 608 608 VAL VAL A . n A 1 609 SER 609 609 609 SER SER A . n A 1 610 VAL 610 610 610 VAL VAL A . n A 1 611 ASP 611 611 611 ASP ASP A . n A 1 612 SER 612 612 612 SER SER A . n A 1 613 ASP 613 613 613 ASP ASP A . n A 1 614 GLN 614 614 614 GLN GLN A . n A 1 615 LYS 615 615 615 LYS LYS A . n A 1 616 LYS 616 616 616 LYS LYS A . n A 1 617 ILE 617 617 617 ILE ILE A . n A 1 618 TYR 618 618 618 TYR TYR A . n A 1 619 ILE 619 619 619 ILE ILE A . n A 1 620 GLY 620 620 620 GLY GLY A . n A 1 621 ASP 621 621 621 ASP ASP A . n A 1 622 ASP 622 622 622 ASP ASP A . n A 1 623 ASN 623 623 623 ASN ASN A . n A 1 624 PRO 624 624 624 PRO PRO A . n A 1 625 LEU 625 625 625 LEU LEU A . n A 1 626 THR 626 626 626 THR THR A . n A 1 627 LEU 627 627 627 LEU LEU A . n A 1 628 ILE 628 628 628 ILE ILE A . n A 1 629 VAL 629 629 629 VAL VAL A . n A 1 630 LYS 630 630 630 LYS LYS A . n A 1 631 ALA 631 631 631 ALA ALA A . n A 1 632 GLN 632 632 632 GLN GLN A . n A 1 633 ASN 633 633 633 ASN ASN A . n A 1 634 GLN 634 634 634 GLN GLN A . n A 1 635 GLY 635 635 635 GLY GLY A . n A 1 636 GLU 636 636 636 GLU GLU A . n A 1 637 GLY 637 637 637 GLY GLY A . n A 1 638 ALA 638 638 638 ALA ALA A . n A 1 639 TYR 639 639 639 TYR TYR A . n A 1 640 GLU 640 640 640 GLU GLU A . n A 1 641 ALA 641 641 641 ALA ALA A . n A 1 642 GLU 642 642 642 GLU GLU A . n A 1 643 LEU 643 643 643 LEU LEU A . n A 1 644 ILE 644 644 644 ILE ILE A . n A 1 645 VAL 645 645 645 VAL VAL A . n A 1 646 SER 646 646 646 SER SER A . n A 1 647 ILE 647 647 647 ILE ILE A . n A 1 648 PRO 648 648 648 PRO PRO A . n A 1 649 LEU 649 649 649 LEU LEU A . n A 1 650 GLN 650 650 650 GLN GLN A . n A 1 651 ALA 651 651 651 ALA ALA A . n A 1 652 ASP 652 652 652 ASP ASP A . n A 1 653 PHE 653 653 653 PHE PHE A . n A 1 654 ILE 654 654 654 ILE ILE A . n A 1 655 GLY 655 655 655 GLY GLY A . n A 1 656 VAL 656 656 656 VAL VAL A . n A 1 657 VAL 657 657 657 VAL VAL A . n A 1 658 ARG 658 658 658 ARG ARG A . n A 1 659 ASN 659 659 659 ASN ASN A . n A 1 660 ASN 660 660 660 ASN ASN A . n A 1 661 GLU 661 661 661 GLU GLU A . n A 1 662 ALA 662 662 662 ALA ALA A . n A 1 663 LEU 663 663 663 LEU LEU A . n A 1 664 ALA 664 664 664 ALA ALA A . n A 1 665 ARG 665 665 665 ARG ARG A . n A 1 666 LEU 666 666 666 LEU LEU A . n A 1 667 SER 667 667 667 SER SER A . n A 1 668 CYS 668 668 668 CYS CYS A . n A 1 669 ALA 669 669 669 ALA ALA A . n A 1 670 PHE 670 670 670 PHE PHE A . n A 1 671 LYS 671 671 671 LYS LYS A . n A 1 672 THR 672 672 672 THR THR A . n A 1 673 GLU 673 673 673 GLU GLU A . n A 1 674 ASN 674 674 674 ASN ASN A . n A 1 675 GLN 675 675 675 GLN GLN A . n A 1 676 THR 676 676 676 THR THR A . n A 1 677 ARG 677 677 677 ARG ARG A . n A 1 678 GLN 678 678 678 GLN GLN A . n A 1 679 VAL 679 679 679 VAL VAL A . n A 1 680 VAL 680 680 680 VAL VAL A . n A 1 681 CYS 681 681 681 CYS CYS A . n A 1 682 ASP 682 682 682 ASP ASP A . n A 1 683 LEU 683 683 683 LEU LEU A . n A 1 684 GLY 684 684 684 GLY GLY A . n A 1 685 ASN 685 685 685 ASN ASN A . n A 1 686 PRO 686 686 686 PRO PRO A . n A 1 687 MET 687 687 687 MET MET A . n A 1 688 LYS 688 688 688 LYS LYS A . n A 1 689 ALA 689 689 689 ALA ALA A . n A 1 690 GLY 690 690 690 GLY GLY A . n A 1 691 THR 691 691 691 THR THR A . n A 1 692 GLN 692 692 692 GLN GLN A . n A 1 693 LEU 693 693 693 LEU LEU A . n A 1 694 LEU 694 694 694 LEU LEU A . n A 1 695 ALA 695 695 695 ALA ALA A . n A 1 696 GLY 696 696 696 GLY GLY A . n A 1 697 LEU 697 697 697 LEU LEU A . n A 1 698 ARG 698 698 698 ARG ARG A . n A 1 699 PHE 699 699 699 PHE PHE A . n A 1 700 SER 700 700 700 SER SER A . n A 1 701 VAL 701 701 701 VAL VAL A . n A 1 702 HIS 702 702 702 HIS HIS A . n A 1 703 GLN 703 703 703 GLN GLN A . n A 1 704 GLN 704 704 704 GLN GLN A . n A 1 705 SER 705 705 705 SER SER A . n A 1 706 GLU 706 706 706 GLU GLU A . n A 1 707 MET 707 707 707 MET MET A . n A 1 708 ASP 708 708 708 ASP ASP A . n A 1 709 THR 709 709 709 THR THR A . n A 1 710 SER 710 710 710 SER SER A . n A 1 711 VAL 711 711 711 VAL VAL A . n A 1 712 LYS 712 712 712 LYS LYS A . n A 1 713 PHE 713 713 713 PHE PHE A . n A 1 714 ASP 714 714 714 ASP ASP A . n A 1 715 LEU 715 715 715 LEU LEU A . n A 1 716 GLN 716 716 716 GLN GLN A . n A 1 717 ILE 717 717 717 ILE ILE A . n A 1 718 GLN 718 718 718 GLN GLN A . n A 1 719 SER 719 719 719 SER SER A . n A 1 720 SER 720 720 720 SER SER A . n A 1 721 ASN 721 721 721 ASN ASN A . n A 1 722 LEU 722 722 722 LEU LEU A . n A 1 723 PHE 723 723 723 PHE PHE A . n A 1 724 ASP 724 724 724 ASP ASP A . n A 1 725 LYS 725 725 725 LYS LYS A . n A 1 726 VAL 726 726 726 VAL VAL A . n A 1 727 SER 727 727 727 SER SER A . n A 1 728 PRO 728 728 728 PRO PRO A . n A 1 729 VAL 729 729 729 VAL VAL A . n A 1 730 VAL 730 730 730 VAL VAL A . n A 1 731 SER 731 731 731 SER SER A . n A 1 732 HIS 732 732 732 HIS HIS A . n A 1 733 LYS 733 733 733 LYS LYS A . n A 1 734 VAL 734 734 734 VAL VAL A . n A 1 735 ASP 735 735 735 ASP ASP A . n A 1 736 LEU 736 736 736 LEU LEU A . n A 1 737 ALA 737 737 737 ALA ALA A . n A 1 738 VAL 738 738 738 VAL VAL A . n A 1 739 LEU 739 739 739 LEU LEU A . n A 1 740 ALA 740 740 740 ALA ALA A . n A 1 741 ALA 741 741 741 ALA ALA A . n A 1 742 VAL 742 742 742 VAL VAL A . n A 1 743 GLU 743 743 743 GLU GLU A . n A 1 744 ILE 744 744 744 ILE ILE A . n A 1 745 ARG 745 745 745 ARG ARG A . n A 1 746 GLY 746 746 746 GLY GLY A . n A 1 747 VAL 747 747 747 VAL VAL A . n A 1 748 SER 748 748 748 SER SER A . n A 1 749 SER 749 749 749 SER SER A . n A 1 750 PRO 750 750 750 PRO PRO A . n A 1 751 ASP 751 751 751 ASP ASP A . n A 1 752 HIS 752 752 752 HIS HIS A . n A 1 753 VAL 753 753 753 VAL VAL A . n A 1 754 PHE 754 754 754 PHE PHE A . n A 1 755 LEU 755 755 755 LEU LEU A . n A 1 756 PRO 756 756 756 PRO PRO A . n A 1 757 ILE 757 757 757 ILE ILE A . n A 1 758 PRO 758 758 758 PRO PRO A . n A 1 759 ASN 759 759 759 ASN ASN A . n A 1 760 TRP 760 760 760 TRP TRP A . n A 1 761 GLU 761 761 761 GLU GLU A . n A 1 762 HIS 762 762 762 HIS HIS A . n A 1 763 LYS 763 763 763 LYS LYS A . n A 1 764 GLU 764 764 764 GLU GLU A . n A 1 765 ASN 765 765 765 ASN ASN A . n A 1 766 PRO 766 766 766 PRO PRO A . n A 1 767 GLU 767 767 767 GLU GLU A . n A 1 768 THR 768 768 768 THR THR A . n A 1 769 GLU 769 769 769 GLU GLU A . n A 1 770 GLU 770 770 770 GLU GLU A . n A 1 771 ASP 771 771 771 ASP ASP A . n A 1 772 VAL 772 772 772 VAL VAL A . n A 1 773 GLY 773 773 773 GLY GLY A . n A 1 774 PRO 774 774 774 PRO PRO A . n A 1 775 VAL 775 775 775 VAL VAL A . n A 1 776 VAL 776 776 776 VAL VAL A . n A 1 777 GLN 777 777 777 GLN GLN A . n A 1 778 HIS 778 778 778 HIS HIS A . n A 1 779 ILE 779 779 779 ILE ILE A . n A 1 780 TYR 780 780 780 TYR TYR A . n A 1 781 GLU 781 781 781 GLU GLU A . n A 1 782 LEU 782 782 782 LEU LEU A . n A 1 783 ARG 783 783 783 ARG ARG A . n A 1 784 ASN 784 784 784 ASN ASN A . n A 1 785 ASN 785 785 785 ASN ASN A . n A 1 786 GLY 786 786 786 GLY GLY A . n A 1 787 PRO 787 787 787 PRO PRO A . n A 1 788 SER 788 788 788 SER SER A . n A 1 789 SER 789 789 789 SER SER A . n A 1 790 PHE 790 790 790 PHE PHE A . n A 1 791 SER 791 791 791 SER SER A . n A 1 792 LYS 792 792 792 LYS LYS A . n A 1 793 ALA 793 793 793 ALA ALA A . n A 1 794 MET 794 794 794 MET MET A . n A 1 795 LEU 795 795 795 LEU LEU A . n A 1 796 HIS 796 796 796 HIS HIS A . n A 1 797 LEU 797 797 797 LEU LEU A . n A 1 798 GLN 798 798 798 GLN GLN A . n A 1 799 TRP 799 799 799 TRP TRP A . n A 1 800 PRO 800 800 800 PRO PRO A . n A 1 801 TYR 801 801 801 TYR TYR A . n A 1 802 LYS 802 802 802 LYS LYS A . n A 1 803 TYR 803 803 803 TYR TYR A . n A 1 804 ASN 804 804 804 ASN ASN A . n A 1 805 ASN 805 805 805 ASN ASN A . n A 1 806 ASN 806 806 806 ASN ASN A . n A 1 807 THR 807 807 807 THR THR A . n A 1 808 LEU 808 808 808 LEU LEU A . n A 1 809 LEU 809 809 809 LEU LEU A . n A 1 810 TYR 810 810 810 TYR TYR A . n A 1 811 ILE 811 811 811 ILE ILE A . n A 1 812 LEU 812 812 812 LEU LEU A . n A 1 813 HIS 813 813 813 HIS HIS A . n A 1 814 TYR 814 814 814 TYR TYR A . n A 1 815 ASP 815 815 815 ASP ASP A . n A 1 816 ILE 816 816 816 ILE ILE A . n A 1 817 ASP 817 817 817 ASP ASP A . n A 1 818 GLY 818 818 818 GLY GLY A . n A 1 819 PRO 819 819 819 PRO PRO A . n A 1 820 MET 820 820 820 MET MET A . n A 1 821 ASN 821 821 821 ASN ASN A . n A 1 822 CYS 822 822 822 CYS CYS A . n A 1 823 THR 823 823 823 THR THR A . n A 1 824 SER 824 824 824 SER SER A . n A 1 825 ASP 825 825 825 ASP ASP A . n A 1 826 MET 826 826 826 MET MET A . n A 1 827 GLU 827 827 827 GLU GLU A . n A 1 828 ILE 828 828 828 ILE ILE A . n A 1 829 ASN 829 829 829 ASN ASN A . n A 1 830 PRO 830 830 830 PRO PRO A . n A 1 831 LEU 831 831 831 LEU LEU A . n A 1 832 ARG 832 832 832 ARG ARG A . n A 1 833 ILE 833 833 833 ILE ILE A . n A 1 834 LYS 834 834 834 LYS LYS A . n A 1 835 ILE 835 835 835 ILE ILE A . n A 1 836 SER 836 836 ? ? ? A . n A 1 837 SER 837 837 ? ? ? A . n A 1 838 LEU 838 838 ? ? ? A . n A 1 839 GLN 839 839 ? ? ? A . n A 1 840 THR 840 840 ? ? ? A . n A 1 841 THR 841 841 ? ? ? A . n A 1 842 GLU 842 842 ? ? ? A . n A 1 843 LYS 843 843 ? ? ? A . n A 1 844 ASN 844 844 ? ? ? A . n A 1 845 ASP 845 845 ? ? ? A . n A 1 846 THR 846 846 ? ? ? A . n A 1 847 VAL 847 847 ? ? ? A . n A 1 848 ALA 848 848 ? ? ? A . n A 1 849 GLY 849 849 ? ? ? A . n A 1 850 GLN 850 850 ? ? ? A . n A 1 851 GLY 851 851 ? ? ? A . n A 1 852 GLU 852 852 ? ? ? A . n A 1 853 ARG 853 853 ? ? ? A . n A 1 854 ASP 854 854 ? ? ? A . n A 1 855 HIS 855 855 ? ? ? A . n A 1 856 LEU 856 856 ? ? ? A . n A 1 857 ILE 857 857 ? ? ? A . n A 1 858 THR 858 858 ? ? ? A . n A 1 859 LYS 859 859 ? ? ? A . n A 1 860 ARG 860 860 ? ? ? A . n A 1 861 ASP 861 861 ? ? ? A . n A 1 862 LEU 862 862 ? ? ? A . n A 1 863 ALA 863 863 ? ? ? A . n A 1 864 LEU 864 864 ? ? ? A . n A 1 865 SER 865 865 ? ? ? A . n A 1 866 GLU 866 866 ? ? ? A . n A 1 867 GLY 867 867 ? ? ? A . n A 1 868 ASP 868 868 868 ASP ASP A . n A 1 869 ILE 869 869 869 ILE ILE A . n A 1 870 HIS 870 870 870 HIS HIS A . n A 1 871 THR 871 871 871 THR THR A . n A 1 872 LEU 872 872 872 LEU LEU A . n A 1 873 GLY 873 873 873 GLY GLY A . n A 1 874 CYS 874 874 874 CYS CYS A . n A 1 875 GLY 875 875 875 GLY GLY A . n A 1 876 VAL 876 876 876 VAL VAL A . n A 1 877 ALA 877 877 877 ALA ALA A . n A 1 878 GLN 878 878 878 GLN GLN A . n A 1 879 CYS 879 879 879 CYS CYS A . n A 1 880 LEU 880 880 880 LEU LEU A . n A 1 881 LYS 881 881 881 LYS LYS A . n A 1 882 ILE 882 882 882 ILE ILE A . n A 1 883 VAL 883 883 883 VAL VAL A . n A 1 884 CYS 884 884 884 CYS CYS A . n A 1 885 GLN 885 885 885 GLN GLN A . n A 1 886 VAL 886 886 886 VAL VAL A . n A 1 887 GLY 887 887 887 GLY GLY A . n A 1 888 ARG 888 888 888 ARG ARG A . n A 1 889 LEU 889 889 889 LEU LEU A . n A 1 890 ASP 890 890 890 ASP ASP A . n A 1 891 ARG 891 891 891 ARG ARG A . n A 1 892 GLY 892 892 892 GLY GLY A . n A 1 893 LYS 893 893 893 LYS LYS A . n A 1 894 SER 894 894 894 SER SER A . n A 1 895 ALA 895 895 895 ALA ALA A . n A 1 896 ILE 896 896 896 ILE ILE A . n A 1 897 LEU 897 897 897 LEU LEU A . n A 1 898 TYR 898 898 898 TYR TYR A . n A 1 899 VAL 899 899 899 VAL VAL A . n A 1 900 LYS 900 900 900 LYS LYS A . n A 1 901 SER 901 901 901 SER SER A . n A 1 902 LEU 902 902 902 LEU LEU A . n A 1 903 LEU 903 903 903 LEU LEU A . n A 1 904 TRP 904 904 904 TRP TRP A . n A 1 905 THR 905 905 905 THR THR A . n A 1 906 GLU 906 906 906 GLU GLU A . n A 1 907 THR 907 907 907 THR THR A . n A 1 908 PHE 908 908 908 PHE PHE A . n A 1 909 MET 909 909 909 MET MET A . n A 1 910 ASN 910 910 910 ASN ASN A . n A 1 911 LYS 911 911 911 LYS LYS A . n A 1 912 GLU 912 912 912 GLU GLU A . n A 1 913 ASN 913 913 913 ASN ASN A . n A 1 914 GLN 914 914 914 GLN GLN A . n A 1 915 ASN 915 915 915 ASN ASN A . n A 1 916 HIS 916 916 916 HIS HIS A . n A 1 917 SER 917 917 917 SER SER A . n A 1 918 TYR 918 918 918 TYR TYR A . n A 1 919 SER 919 919 919 SER SER A . n A 1 920 LEU 920 920 920 LEU LEU A . n A 1 921 LYS 921 921 921 LYS LYS A . n A 1 922 SER 922 922 922 SER SER A . n A 1 923 SER 923 923 923 SER SER A . n A 1 924 ALA 924 924 924 ALA ALA A . n A 1 925 SER 925 925 925 SER SER A . n A 1 926 PHE 926 926 926 PHE PHE A . n A 1 927 ASN 927 927 927 ASN ASN A . n A 1 928 VAL 928 928 928 VAL VAL A . n A 1 929 ILE 929 929 929 ILE ILE A . n A 1 930 GLU 930 930 930 GLU GLU A . n A 1 931 PHE 931 931 931 PHE PHE A . n A 1 932 PRO 932 932 932 PRO PRO A . n A 1 933 TYR 933 933 933 TYR TYR A . n A 1 934 LYS 934 934 934 LYS LYS A . n A 1 935 ASN 935 935 935 ASN ASN A . n A 1 936 LEU 936 936 936 LEU LEU A . n A 1 937 PRO 937 937 937 PRO PRO A . n A 1 938 ILE 938 938 938 ILE ILE A . n A 1 939 GLU 939 939 939 GLU GLU A . n A 1 940 ASP 940 940 940 ASP ASP A . n A 1 941 ILE 941 941 941 ILE ILE A . n A 1 942 THR 942 942 942 THR THR A . n A 1 943 ASN 943 943 943 ASN ASN A . n A 1 944 SER 944 944 944 SER SER A . n A 1 945 THR 945 945 945 THR THR A . n A 1 946 LEU 946 946 946 LEU LEU A . n A 1 947 VAL 947 947 947 VAL VAL A . n A 1 948 THR 948 948 948 THR THR A . n A 1 949 THR 949 949 949 THR THR A . n A 1 950 ASN 950 950 950 ASN ASN A . n A 1 951 VAL 951 951 951 VAL VAL A . n A 1 952 THR 952 952 952 THR THR A . n A 1 953 TRP 953 953 953 TRP TRP A . n A 1 954 GLY 954 954 954 GLY GLY A . n A 1 955 ILE 955 955 955 ILE ILE A . n A 1 956 GLN 956 956 956 GLN GLN A . n A 1 957 PRO 957 957 ? ? ? A . n A 1 958 ALA 958 958 ? ? ? A . n A 1 959 PRO 959 959 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 PRO 2 2 2 PRO PRO B . n B 2 3 ASN 3 3 3 ASN ASN B . n B 2 4 ILE 4 4 4 ILE ILE B . n B 2 5 CYS 5 5 5 CYS CYS B . n B 2 6 THR 6 6 6 THR THR B . n B 2 7 THR 7 7 7 THR THR B . n B 2 8 ARG 8 8 8 ARG ARG B . n B 2 9 GLY 9 9 9 GLY GLY B . n B 2 10 VAL 10 10 10 VAL VAL B . n B 2 11 SER 11 11 11 SER SER B . n B 2 12 SER 12 12 12 SER SER B . n B 2 13 CYS 13 13 13 CYS CYS B . n B 2 14 GLN 14 14 14 GLN GLN B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 CYS 16 16 16 CYS CYS B . n B 2 17 LEU 17 17 17 LEU LEU B . n B 2 18 ALA 18 18 18 ALA ALA B . n B 2 19 VAL 19 19 19 VAL VAL B . n B 2 20 SER 20 20 20 SER SER B . n B 2 21 PRO 21 21 21 PRO PRO B . n B 2 22 MET 22 22 22 MET MET B . n B 2 23 CYS 23 23 23 CYS CYS B . n B 2 24 ALA 24 24 24 ALA ALA B . n B 2 25 TRP 25 25 25 TRP TRP B . n B 2 26 CYS 26 26 26 CYS CYS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASP 28 28 28 ASP ASP B . n B 2 29 GLU 29 29 29 GLU GLU B . n B 2 30 ALA 30 30 30 ALA ALA B . n B 2 31 LEU 31 31 31 LEU LEU B . n B 2 32 PRO 32 32 32 PRO PRO B . n B 2 33 LEU 33 33 33 LEU LEU B . n B 2 34 GLY 34 34 34 GLY GLY B . n B 2 35 SER 35 35 35 SER SER B . n B 2 36 PRO 36 36 36 PRO PRO B . n B 2 37 ARG 37 37 37 ARG ARG B . n B 2 38 CYS 38 38 38 CYS CYS B . n B 2 39 ASP 39 39 39 ASP ASP B . n B 2 40 LEU 40 40 40 LEU LEU B . n B 2 41 LYS 41 41 41 LYS LYS B . n B 2 42 GLU 42 42 42 GLU GLU B . n B 2 43 ASN 43 43 43 ASN ASN B . n B 2 44 LEU 44 44 44 LEU LEU B . n B 2 45 LEU 45 45 45 LEU LEU B . n B 2 46 LYS 46 46 46 LYS LYS B . n B 2 47 ASP 47 47 47 ASP ASP B . n B 2 48 ASN 48 48 48 ASN ASN B . n B 2 49 CYS 49 49 49 CYS CYS B . n B 2 50 ALA 50 50 50 ALA ALA B . n B 2 51 PRO 51 51 51 PRO PRO B . n B 2 52 GLU 52 52 52 GLU GLU B . n B 2 53 SER 53 53 53 SER SER B . n B 2 54 ILE 54 54 54 ILE ILE B . n B 2 55 GLU 55 55 55 GLU GLU B . n B 2 56 PHE 56 56 56 PHE PHE B . n B 2 57 PRO 57 57 57 PRO PRO B . n B 2 58 VAL 58 58 58 VAL VAL B . n B 2 59 SER 59 59 59 SER SER B . n B 2 60 GLU 60 60 60 GLU GLU B . n B 2 61 ALA 61 61 61 ALA ALA B . n B 2 62 ARG 62 62 62 ARG ARG B . n B 2 63 VAL 63 63 63 VAL VAL B . n B 2 64 LEU 64 64 64 LEU LEU B . n B 2 65 GLU 65 65 65 GLU GLU B . n B 2 66 ASP 66 66 66 ASP ASP B . n B 2 67 ARG 67 67 67 ARG ARG B . n B 2 68 PRO 68 68 68 PRO PRO B . n B 2 69 LEU 69 69 69 LEU LEU B . n B 2 70 SER 70 70 70 SER SER B . n B 2 71 ASP 71 71 71 ASP ASP B . n B 2 72 LYS 72 72 72 LYS LYS B . n B 2 73 GLY 73 73 73 GLY GLY B . n B 2 74 SER 74 74 74 SER SER B . n B 2 75 GLY 75 75 75 GLY GLY B . n B 2 76 ASP 76 76 76 ASP ASP B . n B 2 77 SER 77 77 77 SER SER B . n B 2 78 SER 78 78 78 SER SER B . n B 2 79 GLN 79 79 79 GLN GLN B . n B 2 80 VAL 80 80 80 VAL VAL B . n B 2 81 THR 81 81 81 THR THR B . n B 2 82 GLN 82 82 82 GLN GLN B . n B 2 83 VAL 83 83 83 VAL VAL B . n B 2 84 SER 84 84 84 SER SER B . n B 2 85 PRO 85 85 85 PRO PRO B . n B 2 86 GLN 86 86 86 GLN GLN B . n B 2 87 ARG 87 87 87 ARG ARG B . n B 2 88 ILE 88 88 88 ILE ILE B . n B 2 89 ALA 89 89 89 ALA ALA B . n B 2 90 LEU 90 90 90 LEU LEU B . n B 2 91 ARG 91 91 91 ARG ARG B . n B 2 92 LEU 92 92 92 LEU LEU B . n B 2 93 ARG 93 93 93 ARG ARG B . n B 2 94 PRO 94 94 94 PRO PRO B . n B 2 95 ASP 95 95 95 ASP ASP B . n B 2 96 ASP 96 96 96 ASP ASP B . n B 2 97 SER 97 97 97 SER SER B . n B 2 98 LYS 98 98 98 LYS LYS B . n B 2 99 ASN 99 99 99 ASN ASN B . n B 2 100 PHE 100 100 100 PHE PHE B . n B 2 101 SER 101 101 101 SER SER B . n B 2 102 ILE 102 102 102 ILE ILE B . n B 2 103 GLN 103 103 103 GLN GLN B . n B 2 104 VAL 104 104 104 VAL VAL B . n B 2 105 ARG 105 105 105 ARG ARG B . n B 2 106 GLN 106 106 106 GLN GLN B . n B 2 107 VAL 107 107 107 VAL VAL B . n B 2 108 GLU 108 108 108 GLU GLU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 TYR 110 110 110 TYR TYR B . n B 2 111 PRO 111 111 111 PRO PRO B . n B 2 112 VAL 112 112 112 VAL VAL B . n B 2 113 ASP 113 113 113 ASP ASP B . n B 2 114 ILE 114 114 114 ILE ILE B . n B 2 115 TYR 115 115 115 TYR TYR B . n B 2 116 TYR 116 116 116 TYR TYR B . n B 2 117 LEU 117 117 117 LEU LEU B . n B 2 118 MET 118 118 118 MET MET B . n B 2 119 ASP 119 119 119 ASP ASP B . n B 2 120 LEU 120 120 120 LEU LEU B . n B 2 121 SER 121 121 121 SER SER B . n B 2 122 TYR 122 122 122 TYR TYR B . n B 2 123 SER 123 123 123 SER SER B . n B 2 124 MET 124 124 124 MET MET B . n B 2 125 LYS 125 125 125 LYS LYS B . n B 2 126 ASP 126 126 126 ASP ASP B . n B 2 127 ASP 127 127 127 ASP ASP B . n B 2 128 LEU 128 128 128 LEU LEU B . n B 2 129 TRP 129 129 129 TRP TRP B . n B 2 130 SER 130 130 130 SER SER B . n B 2 131 ILE 131 131 131 ILE ILE B . n B 2 132 GLN 132 132 132 GLN GLN B . n B 2 133 ASN 133 133 133 ASN ASN B . n B 2 134 LEU 134 134 134 LEU LEU B . n B 2 135 GLY 135 135 135 GLY GLY B . n B 2 136 THR 136 136 136 THR THR B . n B 2 137 LYS 137 137 137 LYS LYS B . n B 2 138 LEU 138 138 138 LEU LEU B . n B 2 139 ALA 139 139 139 ALA ALA B . n B 2 140 THR 140 140 140 THR THR B . n B 2 141 GLN 141 141 141 GLN GLN B . n B 2 142 MET 142 142 142 MET MET B . n B 2 143 ARG 143 143 143 ARG ARG B . n B 2 144 LYS 144 144 144 LYS LYS B . n B 2 145 LEU 145 145 145 LEU LEU B . n B 2 146 THR 146 146 146 THR THR B . n B 2 147 SER 147 147 147 SER SER B . n B 2 148 ASN 148 148 148 ASN ASN B . n B 2 149 LEU 149 149 149 LEU LEU B . n B 2 150 ARG 150 150 150 ARG ARG B . n B 2 151 ILE 151 151 151 ILE ILE B . n B 2 152 GLY 152 152 152 GLY GLY B . n B 2 153 PHE 153 153 153 PHE PHE B . n B 2 154 GLY 154 154 154 GLY GLY B . n B 2 155 ALA 155 155 155 ALA ALA B . n B 2 156 PHE 156 156 156 PHE PHE B . n B 2 157 VAL 157 157 157 VAL VAL B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 LYS 159 159 159 LYS LYS B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 VAL 161 161 161 VAL VAL B . n B 2 162 SER 162 162 162 SER SER B . n B 2 163 PRO 163 163 163 PRO PRO B . n B 2 164 TYR 164 164 164 TYR TYR B . n B 2 165 MET 165 165 165 MET MET B . n B 2 166 TYR 166 166 166 TYR TYR B . n B 2 167 ILE 167 167 167 ILE ILE B . n B 2 168 SER 168 168 168 SER SER B . n B 2 169 PRO 169 169 169 PRO PRO B . n B 2 170 PRO 170 170 170 PRO PRO B . n B 2 171 GLU 171 171 171 GLU GLU B . n B 2 172 ALA 172 172 172 ALA ALA B . n B 2 173 LEU 173 173 173 LEU LEU B . n B 2 174 GLU 174 174 174 GLU GLU B . n B 2 175 ASN 175 175 175 ASN ASN B . n B 2 176 PRO 176 176 176 PRO PRO B . n B 2 177 CYS 177 177 177 CYS CYS B . n B 2 178 TYR 178 178 178 TYR TYR B . n B 2 179 ASP 179 179 179 ASP ASP B . n B 2 180 MET 180 180 180 MET MET B . n B 2 181 LYS 181 181 181 LYS LYS B . n B 2 182 THR 182 182 182 THR THR B . n B 2 183 THR 183 183 183 THR THR B . n B 2 184 CYS 184 184 184 CYS CYS B . n B 2 185 LEU 185 185 185 LEU LEU B . n B 2 186 PRO 186 186 186 PRO PRO B . n B 2 187 MET 187 187 187 MET MET B . n B 2 188 PHE 188 188 188 PHE PHE B . n B 2 189 GLY 189 189 189 GLY GLY B . n B 2 190 TYR 190 190 190 TYR TYR B . n B 2 191 LYS 191 191 191 LYS LYS B . n B 2 192 HIS 192 192 192 HIS HIS B . n B 2 193 VAL 193 193 193 VAL VAL B . n B 2 194 LEU 194 194 194 LEU LEU B . n B 2 195 THR 195 195 195 THR THR B . n B 2 196 LEU 196 196 196 LEU LEU B . n B 2 197 THR 197 197 197 THR THR B . n B 2 198 ASP 198 198 198 ASP ASP B . n B 2 199 GLN 199 199 199 GLN GLN B . n B 2 200 VAL 200 200 200 VAL VAL B . n B 2 201 THR 201 201 201 THR THR B . n B 2 202 ARG 202 202 202 ARG ARG B . n B 2 203 PHE 203 203 203 PHE PHE B . n B 2 204 ASN 204 204 204 ASN ASN B . n B 2 205 GLU 205 205 205 GLU GLU B . n B 2 206 GLU 206 206 206 GLU GLU B . n B 2 207 VAL 207 207 207 VAL VAL B . n B 2 208 LYS 208 208 208 LYS LYS B . n B 2 209 LYS 209 209 209 LYS LYS B . n B 2 210 GLN 210 210 210 GLN GLN B . n B 2 211 SER 211 211 211 SER SER B . n B 2 212 VAL 212 212 212 VAL VAL B . n B 2 213 SER 213 213 213 SER SER B . n B 2 214 ARG 214 214 214 ARG ARG B . n B 2 215 ASN 215 215 215 ASN ASN B . n B 2 216 ARG 216 216 216 ARG ARG B . n B 2 217 ASP 217 217 217 ASP ASP B . n B 2 218 ALA 218 218 218 ALA ALA B . n B 2 219 PRO 219 219 219 PRO PRO B . n B 2 220 GLU 220 220 220 GLU GLU B . n B 2 221 GLY 221 221 221 GLY GLY B . n B 2 222 GLY 222 222 222 GLY GLY B . n B 2 223 PHE 223 223 223 PHE PHE B . n B 2 224 ASP 224 224 224 ASP ASP B . n B 2 225 ALA 225 225 225 ALA ALA B . n B 2 226 ILE 226 226 226 ILE ILE B . n B 2 227 MET 227 227 227 MET MET B . n B 2 228 GLN 228 228 228 GLN GLN B . n B 2 229 ALA 229 229 229 ALA ALA B . n B 2 230 THR 230 230 230 THR THR B . n B 2 231 VAL 231 231 231 VAL VAL B . n B 2 232 CYS 232 232 232 CYS CYS B . n B 2 233 ASP 233 233 233 ASP ASP B . n B 2 234 GLU 234 234 234 GLU GLU B . n B 2 235 LYS 235 235 235 LYS LYS B . n B 2 236 ILE 236 236 236 ILE ILE B . n B 2 237 GLY 237 237 237 GLY GLY B . n B 2 238 TRP 238 238 238 TRP TRP B . n B 2 239 ARG 239 239 239 ARG ARG B . n B 2 240 ASN 240 240 240 ASN ASN B . n B 2 241 ASP 241 241 241 ASP ASP B . n B 2 242 ALA 242 242 242 ALA ALA B . n B 2 243 SER 243 243 243 SER SER B . n B 2 244 HIS 244 244 244 HIS HIS B . n B 2 245 LEU 245 245 245 LEU LEU B . n B 2 246 LEU 246 246 246 LEU LEU B . n B 2 247 VAL 247 247 247 VAL VAL B . n B 2 248 PHE 248 248 248 PHE PHE B . n B 2 249 THR 249 249 249 THR THR B . n B 2 250 THR 250 250 250 THR THR B . n B 2 251 ASP 251 251 251 ASP ASP B . n B 2 252 ALA 252 252 252 ALA ALA B . n B 2 253 LYS 253 253 253 LYS LYS B . n B 2 254 THR 254 254 254 THR THR B . n B 2 255 HIS 255 255 255 HIS HIS B . n B 2 256 ILE 256 256 256 ILE ILE B . n B 2 257 ALA 257 257 257 ALA ALA B . n B 2 258 LEU 258 258 258 LEU LEU B . n B 2 259 ASP 259 259 259 ASP ASP B . n B 2 260 GLY 260 260 260 GLY GLY B . n B 2 261 ARG 261 261 261 ARG ARG B . n B 2 262 LEU 262 262 262 LEU LEU B . n B 2 263 ALA 263 263 263 ALA ALA B . n B 2 264 GLY 264 264 264 GLY GLY B . n B 2 265 ILE 265 265 265 ILE ILE B . n B 2 266 VAL 266 266 266 VAL VAL B . n B 2 267 GLN 267 267 267 GLN GLN B . n B 2 268 PRO 268 268 268 PRO PRO B . n B 2 269 ASN 269 269 269 ASN ASN B . n B 2 270 ASP 270 270 270 ASP ASP B . n B 2 271 GLY 271 271 271 GLY GLY B . n B 2 272 GLN 272 272 272 GLN GLN B . n B 2 273 CYS 273 273 273 CYS CYS B . n B 2 274 HIS 274 274 274 HIS HIS B . n B 2 275 VAL 275 275 275 VAL VAL B . n B 2 276 GLY 276 276 276 GLY GLY B . n B 2 277 SER 277 277 277 SER SER B . n B 2 278 ASP 278 278 278 ASP ASP B . n B 2 279 ASN 279 279 279 ASN ASN B . n B 2 280 HIS 280 280 280 HIS HIS B . n B 2 281 TYR 281 281 281 TYR TYR B . n B 2 282 SER 282 282 282 SER SER B . n B 2 283 ALA 283 283 283 ALA ALA B . n B 2 284 SER 284 284 284 SER SER B . n B 2 285 THR 285 285 285 THR THR B . n B 2 286 THR 286 286 286 THR THR B . n B 2 287 MET 287 287 287 MET MET B . n B 2 288 ASP 288 288 288 ASP ASP B . n B 2 289 TYR 289 289 289 TYR TYR B . n B 2 290 PRO 290 290 290 PRO PRO B . n B 2 291 SER 291 291 291 SER SER B . n B 2 292 LEU 292 292 292 LEU LEU B . n B 2 293 GLY 293 293 293 GLY GLY B . n B 2 294 LEU 294 294 294 LEU LEU B . n B 2 295 MET 295 295 295 MET MET B . n B 2 296 THR 296 296 296 THR THR B . n B 2 297 GLU 297 297 297 GLU GLU B . n B 2 298 LYS 298 298 298 LYS LYS B . n B 2 299 LEU 299 299 299 LEU LEU B . n B 2 300 SER 300 300 300 SER SER B . n B 2 301 GLN 301 301 301 GLN GLN B . n B 2 302 LYS 302 302 302 LYS LYS B . n B 2 303 ASN 303 303 303 ASN ASN B . n B 2 304 ILE 304 304 304 ILE ILE B . n B 2 305 ASN 305 305 305 ASN ASN B . n B 2 306 LEU 306 306 306 LEU LEU B . n B 2 307 ILE 307 307 307 ILE ILE B . n B 2 308 PHE 308 308 308 PHE PHE B . n B 2 309 ALA 309 309 309 ALA ALA B . n B 2 310 VAL 310 310 310 VAL VAL B . n B 2 311 THR 311 311 311 THR THR B . n B 2 312 GLU 312 312 312 GLU GLU B . n B 2 313 ASN 313 313 313 ASN ASN B . n B 2 314 VAL 314 314 314 VAL VAL B . n B 2 315 VAL 315 315 315 VAL VAL B . n B 2 316 ASN 316 316 316 ASN ASN B . n B 2 317 LEU 317 317 317 LEU LEU B . n B 2 318 TYR 318 318 318 TYR TYR B . n B 2 319 GLN 319 319 319 GLN GLN B . n B 2 320 ASN 320 320 320 ASN ASN B . n B 2 321 TYR 321 321 321 TYR TYR B . n B 2 322 SER 322 322 322 SER SER B . n B 2 323 GLU 323 323 323 GLU GLU B . n B 2 324 LEU 324 324 324 LEU LEU B . n B 2 325 ILE 325 325 325 ILE ILE B . n B 2 326 PRO 326 326 326 PRO PRO B . n B 2 327 GLY 327 327 327 GLY GLY B . n B 2 328 THR 328 328 328 THR THR B . n B 2 329 THR 329 329 329 THR THR B . n B 2 330 VAL 330 330 330 VAL VAL B . n B 2 331 GLY 331 331 331 GLY GLY B . n B 2 332 VAL 332 332 332 VAL VAL B . n B 2 333 LEU 333 333 333 LEU LEU B . n B 2 334 SER 334 334 334 SER SER B . n B 2 335 MET 335 335 335 MET MET B . n B 2 336 ASP 336 336 336 ASP ASP B . n B 2 337 SER 337 337 337 SER SER B . n B 2 338 SER 338 338 338 SER SER B . n B 2 339 ASN 339 339 339 ASN ASN B . n B 2 340 VAL 340 340 340 VAL VAL B . n B 2 341 LEU 341 341 341 LEU LEU B . n B 2 342 GLN 342 342 342 GLN GLN B . n B 2 343 LEU 343 343 343 LEU LEU B . n B 2 344 ILE 344 344 344 ILE ILE B . n B 2 345 VAL 345 345 345 VAL VAL B . n B 2 346 ASP 346 346 346 ASP ASP B . n B 2 347 ALA 347 347 347 ALA ALA B . n B 2 348 TYR 348 348 348 TYR TYR B . n B 2 349 GLY 349 349 349 GLY GLY B . n B 2 350 LYS 350 350 350 LYS LYS B . n B 2 351 ILE 351 351 351 ILE ILE B . n B 2 352 ARG 352 352 352 ARG ARG B . n B 2 353 SER 353 353 353 SER SER B . n B 2 354 LYS 354 354 354 LYS LYS B . n B 2 355 VAL 355 355 355 VAL VAL B . n B 2 356 GLU 356 356 356 GLU GLU B . n B 2 357 LEU 357 357 357 LEU LEU B . n B 2 358 GLU 358 358 358 GLU GLU B . n B 2 359 VAL 359 359 359 VAL VAL B . n B 2 360 ARG 360 360 360 ARG ARG B . n B 2 361 ASP 361 361 361 ASP ASP B . n B 2 362 LEU 362 362 362 LEU LEU B . n B 2 363 PRO 363 363 363 PRO PRO B . n B 2 364 GLU 364 364 364 GLU GLU B . n B 2 365 GLU 365 365 365 GLU GLU B . n B 2 366 LEU 366 366 366 LEU LEU B . n B 2 367 SER 367 367 367 SER SER B . n B 2 368 LEU 368 368 368 LEU LEU B . n B 2 369 SER 369 369 369 SER SER B . n B 2 370 PHE 370 370 370 PHE PHE B . n B 2 371 ASN 371 371 371 ASN ASN B . n B 2 372 ALA 372 372 372 ALA ALA B . n B 2 373 THR 373 373 373 THR THR B . n B 2 374 CYS 374 374 374 CYS CYS B . n B 2 375 LEU 375 375 375 LEU LEU B . n B 2 376 ASN 376 376 376 ASN ASN B . n B 2 377 ASN 377 377 377 ASN ASN B . n B 2 378 GLU 378 378 378 GLU GLU B . n B 2 379 VAL 379 379 379 VAL VAL B . n B 2 380 ILE 380 380 380 ILE ILE B . n B 2 381 PRO 381 381 381 PRO PRO B . n B 2 382 GLY 382 382 382 GLY GLY B . n B 2 383 LEU 383 383 383 LEU LEU B . n B 2 384 LYS 384 384 384 LYS LYS B . n B 2 385 SER 385 385 385 SER SER B . n B 2 386 CYS 386 386 386 CYS CYS B . n B 2 387 MET 387 387 387 MET MET B . n B 2 388 GLY 388 388 388 GLY GLY B . n B 2 389 LEU 389 389 389 LEU LEU B . n B 2 390 LYS 390 390 390 LYS LYS B . n B 2 391 ILE 391 391 391 ILE ILE B . n B 2 392 GLY 392 392 392 GLY GLY B . n B 2 393 ASP 393 393 393 ASP ASP B . n B 2 394 THR 394 394 394 THR THR B . n B 2 395 VAL 395 395 395 VAL VAL B . n B 2 396 SER 396 396 396 SER SER B . n B 2 397 PHE 397 397 397 PHE PHE B . n B 2 398 SER 398 398 398 SER SER B . n B 2 399 ILE 399 399 399 ILE ILE B . n B 2 400 GLU 400 400 400 GLU GLU B . n B 2 401 ALA 401 401 401 ALA ALA B . n B 2 402 LYS 402 402 402 LYS LYS B . n B 2 403 VAL 403 403 403 VAL VAL B . n B 2 404 ARG 404 404 404 ARG ARG B . n B 2 405 GLY 405 405 405 GLY GLY B . n B 2 406 CYS 406 406 406 CYS CYS B . n B 2 407 PRO 407 407 407 PRO PRO B . n B 2 408 GLN 408 408 408 GLN GLN B . n B 2 409 GLU 409 409 409 GLU GLU B . n B 2 410 LYS 410 410 410 LYS LYS B . n B 2 411 GLU 411 411 411 GLU GLU B . n B 2 412 LYS 412 412 412 LYS LYS B . n B 2 413 SER 413 413 413 SER SER B . n B 2 414 PHE 414 414 414 PHE PHE B . n B 2 415 THR 415 415 415 THR THR B . n B 2 416 ILE 416 416 416 ILE ILE B . n B 2 417 LYS 417 417 417 LYS LYS B . n B 2 418 PRO 418 418 418 PRO PRO B . n B 2 419 VAL 419 419 419 VAL VAL B . n B 2 420 GLY 420 420 420 GLY GLY B . n B 2 421 PHE 421 421 421 PHE PHE B . n B 2 422 LYS 422 422 422 LYS LYS B . n B 2 423 ASP 423 423 423 ASP ASP B . n B 2 424 SER 424 424 424 SER SER B . n B 2 425 LEU 425 425 425 LEU LEU B . n B 2 426 ILE 426 426 426 ILE ILE B . n B 2 427 VAL 427 427 427 VAL VAL B . n B 2 428 GLN 428 428 428 GLN GLN B . n B 2 429 VAL 429 429 429 VAL VAL B . n B 2 430 THR 430 430 430 THR THR B . n B 2 431 PHE 431 431 431 PHE PHE B . n B 2 432 ASP 432 432 432 ASP ASP B . n B 2 433 CYS 433 433 433 CYS CYS B . n B 2 434 ASP 434 434 434 ASP ASP B . n B 2 435 CYS 435 435 435 CYS CYS B . n B 2 436 ALA 436 436 436 ALA ALA B . n B 2 437 CYS 437 437 437 CYS CYS B . n B 2 438 GLN 438 438 438 GLN GLN B . n B 2 439 ALA 439 439 439 ALA ALA B . n B 2 440 GLN 440 440 440 GLN GLN B . n B 2 441 ALA 441 441 441 ALA ALA B . n B 2 442 GLU 442 442 442 GLU GLU B . n B 2 443 PRO 443 443 443 PRO PRO B . n B 2 444 ASN 444 444 444 ASN ASN B . n B 2 445 SER 445 445 445 SER SER B . n B 2 446 HIS 446 446 446 HIS HIS B . n B 2 447 ARG 447 447 447 ARG ARG B . n B 2 448 CYS 448 448 448 CYS CYS B . n B 2 449 ASN 449 449 449 ASN ASN B . n B 2 450 ASN 450 450 450 ASN ASN B . n B 2 451 GLY 451 451 451 GLY GLY B . n B 2 452 ASN 452 452 452 ASN ASN B . n B 2 453 GLY 453 453 453 GLY GLY B . n B 2 454 THR 454 454 454 THR THR B . n B 2 455 PHE 455 455 455 PHE PHE B . n B 2 456 GLU 456 456 456 GLU GLU B . n B 2 457 CYS 457 457 457 CYS CYS B . n B 2 458 GLY 458 458 458 GLY GLY B . n B 2 459 VAL 459 459 459 VAL VAL B . n B 2 460 CYS 460 460 460 CYS CYS B . n B 2 461 ARG 461 461 461 ARG ARG B . n B 2 462 CYS 462 462 462 CYS CYS B . n B 2 463 GLY 463 463 463 GLY GLY B . n B 2 464 PRO 464 464 464 PRO PRO B . n B 2 465 GLY 465 465 465 GLY GLY B . n B 2 466 TRP 466 466 466 TRP TRP B . n B 2 467 LEU 467 467 467 LEU LEU B . n B 2 468 GLY 468 468 468 GLY GLY B . n B 2 469 SER 469 469 469 SER SER B . n B 2 470 GLN 470 470 470 GLN GLN B . n B 2 471 CYS 471 471 471 CYS CYS B . n B 2 472 GLU 472 472 472 GLU GLU B . n B 2 473 CYS 473 473 473 CYS CYS B . n B 2 474 SER 474 474 474 SER SER B . n B 2 475 GLU 475 475 475 GLU GLU B . n B 2 476 GLU 476 476 476 GLU GLU B . n B 2 477 ASP 477 477 477 ASP ASP B . n B 2 478 TYR 478 478 478 TYR TYR B . n B 2 479 ARG 479 479 479 ARG ARG B . n B 2 480 PRO 480 480 480 PRO PRO B . n B 2 481 SER 481 481 481 SER SER B . n B 2 482 GLN 482 482 482 GLN GLN B . n B 2 483 GLN 483 483 483 GLN GLN B . n B 2 484 ASP 484 484 484 ASP ASP B . n B 2 485 GLU 485 485 485 GLU GLU B . n B 2 486 CYS 486 486 486 CYS CYS B . n B 2 487 SER 487 487 487 SER SER B . n B 2 488 PRO 488 488 488 PRO PRO B . n B 2 489 ARG 489 489 489 ARG ARG B . n B 2 490 GLU 490 490 490 GLU GLU B . n B 2 491 GLY 491 491 491 GLY GLY B . n B 2 492 GLN 492 492 492 GLN GLN B . n B 2 493 PRO 493 493 493 PRO PRO B . n B 2 494 VAL 494 494 494 VAL VAL B . n B 2 495 CYS 495 495 495 CYS CYS B . n B 2 496 SER 496 496 496 SER SER B . n B 2 497 GLN 497 497 497 GLN GLN B . n B 2 498 ARG 498 498 498 ARG ARG B . n B 2 499 GLY 499 499 499 GLY GLY B . n B 2 500 GLU 500 500 500 GLU GLU B . n B 2 501 CYS 501 501 501 CYS CYS B . n B 2 502 LEU 502 502 502 LEU LEU B . n B 2 503 CYS 503 503 503 CYS CYS B . n B 2 504 GLY 504 504 504 GLY GLY B . n B 2 505 GLN 505 505 505 GLN GLN B . n B 2 506 CYS 506 506 506 CYS CYS B . n B 2 507 VAL 507 507 507 VAL VAL B . n B 2 508 CYS 508 508 508 CYS CYS B . n B 2 509 HIS 509 509 509 HIS HIS B . n B 2 510 SER 510 510 510 SER SER B . n B 2 511 SER 511 511 511 SER SER B . n B 2 512 ASP 512 512 512 ASP ASP B . n B 2 513 PHE 513 513 513 PHE PHE B . n B 2 514 GLY 514 514 514 GLY GLY B . n B 2 515 LYS 515 515 515 LYS LYS B . n B 2 516 ILE 516 516 516 ILE ILE B . n B 2 517 THR 517 517 517 THR THR B . n B 2 518 GLY 518 518 518 GLY GLY B . n B 2 519 LYS 519 519 519 LYS LYS B . n B 2 520 TYR 520 520 520 TYR TYR B . n B 2 521 CYS 521 521 521 CYS CYS B . n B 2 522 GLU 522 522 522 GLU GLU B . n B 2 523 CYS 523 523 523 CYS CYS B . n B 2 524 ASP 524 524 524 ASP ASP B . n B 2 525 ASP 525 525 525 ASP ASP B . n B 2 526 PHE 526 526 526 PHE PHE B . n B 2 527 SER 527 527 527 SER SER B . n B 2 528 CYS 528 528 528 CYS CYS B . n B 2 529 VAL 529 529 529 VAL VAL B . n B 2 530 ARG 530 530 530 ARG ARG B . n B 2 531 TYR 531 531 531 TYR TYR B . n B 2 532 LYS 532 532 532 LYS LYS B . n B 2 533 GLY 533 533 533 GLY GLY B . n B 2 534 GLU 534 534 534 GLU GLU B . n B 2 535 MET 535 535 535 MET MET B . n B 2 536 CYS 536 536 536 CYS CYS B . n B 2 537 SER 537 537 537 SER SER B . n B 2 538 GLY 538 538 538 GLY GLY B . n B 2 539 HIS 539 539 539 HIS HIS B . n B 2 540 GLY 540 540 540 GLY GLY B . n B 2 541 GLN 541 541 541 GLN GLN B . n B 2 542 CYS 542 542 542 CYS CYS B . n B 2 543 SER 543 543 543 SER SER B . n B 2 544 CYS 544 544 544 CYS CYS B . n B 2 545 GLY 545 545 545 GLY GLY B . n B 2 546 ASP 546 546 546 ASP ASP B . n B 2 547 CYS 547 547 547 CYS CYS B . n B 2 548 LEU 548 548 548 LEU LEU B . n B 2 549 CYS 549 549 549 CYS CYS B . n B 2 550 ASP 550 550 550 ASP ASP B . n B 2 551 SER 551 551 551 SER SER B . n B 2 552 ASP 552 552 552 ASP ASP B . n B 2 553 TRP 553 553 553 TRP TRP B . n B 2 554 THR 554 554 554 THR THR B . n B 2 555 GLY 555 555 555 GLY GLY B . n B 2 556 TYR 556 556 556 TYR TYR B . n B 2 557 TYR 557 557 557 TYR TYR B . n B 2 558 CYS 558 558 558 CYS CYS B . n B 2 559 ASN 559 559 559 ASN ASN B . n B 2 560 CYS 560 560 560 CYS CYS B . n B 2 561 THR 561 561 561 THR THR B . n B 2 562 THR 562 562 562 THR THR B . n B 2 563 ARG 563 563 563 ARG ARG B . n B 2 564 THR 564 564 564 THR THR B . n B 2 565 ASP 565 565 565 ASP ASP B . n B 2 566 THR 566 566 566 THR THR B . n B 2 567 CYS 567 567 567 CYS CYS B . n B 2 568 MET 568 568 568 MET MET B . n B 2 569 SER 569 569 569 SER SER B . n B 2 570 SER 570 570 570 SER SER B . n B 2 571 ASN 571 571 571 ASN ASN B . n B 2 572 GLY 572 572 572 GLY GLY B . n B 2 573 LEU 573 573 573 LEU LEU B . n B 2 574 LEU 574 574 574 LEU LEU B . n B 2 575 CYS 575 575 575 CYS CYS B . n B 2 576 SER 576 576 576 SER SER B . n B 2 577 GLY 577 577 577 GLY GLY B . n B 2 578 ARG 578 578 578 ARG ARG B . n B 2 579 GLY 579 579 579 GLY GLY B . n B 2 580 LYS 580 580 580 LYS LYS B . n B 2 581 CYS 581 581 581 CYS CYS B . n B 2 582 GLU 582 582 582 GLU GLU B . n B 2 583 CYS 583 583 583 CYS CYS B . n B 2 584 GLY 584 584 584 GLY GLY B . n B 2 585 SER 585 585 585 SER SER B . n B 2 586 CYS 586 586 586 CYS CYS B . n B 2 587 VAL 587 587 587 VAL VAL B . n B 2 588 CYS 588 588 588 CYS CYS B . n B 2 589 ILE 589 589 589 ILE ILE B . n B 2 590 GLN 590 590 590 GLN GLN B . n B 2 591 PRO 591 591 591 PRO PRO B . n B 2 592 GLY 592 592 592 GLY GLY B . n B 2 593 SER 593 593 593 SER SER B . n B 2 594 TYR 594 594 594 TYR TYR B . n B 2 595 GLY 595 595 595 GLY GLY B . n B 2 596 ASP 596 596 596 ASP ASP B . n B 2 597 THR 597 597 597 THR THR B . n B 2 598 CYS 598 598 598 CYS CYS B . n B 2 599 GLU 599 599 599 GLU GLU B . n B 2 600 LYS 600 600 600 LYS LYS B . n B 2 601 CYS 601 601 601 CYS CYS B . n B 2 602 PRO 602 602 602 PRO PRO B . n B 2 603 THR 603 603 603 THR THR B . n B 2 604 CYS 604 604 604 CYS CYS B . n B 2 605 PRO 605 605 605 PRO PRO B . n B 2 606 ASP 606 606 606 ASP ASP B . n B 2 607 ALA 607 607 607 ALA ALA B . n B 2 608 CYS 608 608 608 CYS CYS B . n B 2 609 THR 609 609 609 THR THR B . n B 2 610 PHE 610 610 610 PHE PHE B . n B 2 611 LYS 611 611 611 LYS LYS B . n B 2 612 LYS 612 612 612 LYS LYS B . n B 2 613 GLU 613 613 613 GLU GLU B . n B 2 614 CYS 614 614 614 CYS CYS B . n B 2 615 VAL 615 615 615 VAL VAL B . n B 2 616 GLU 616 616 616 GLU GLU B . n B 2 617 CYS 617 617 617 CYS CYS B . n B 2 618 LYS 618 618 618 LYS LYS B . n B 2 619 LYS 619 619 619 LYS LYS B . n B 2 620 PHE 620 620 620 PHE PHE B . n B 2 621 ASP 621 621 621 ASP ASP B . n B 2 622 ARG 622 622 622 ARG ARG B . n B 2 623 GLY 623 623 623 GLY GLY B . n B 2 624 ALA 624 624 624 ALA ALA B . n B 2 625 LEU 625 625 625 LEU LEU B . n B 2 626 HIS 626 626 626 HIS HIS B . n B 2 627 ASP 627 627 627 ASP ASP B . n B 2 628 GLU 628 628 628 GLU GLU B . n B 2 629 ASN 629 629 629 ASN ASN B . n B 2 630 THR 630 630 630 THR THR B . n B 2 631 CYS 631 631 631 CYS CYS B . n B 2 632 ASN 632 632 632 ASN ASN B . n B 2 633 ARG 633 633 633 ARG ARG B . n B 2 634 TYR 634 634 634 TYR TYR B . n B 2 635 CYS 635 635 635 CYS CYS B . n B 2 636 ARG 636 636 636 ARG ARG B . n B 2 637 ASP 637 637 637 ASP ASP B . n B 2 638 GLU 638 638 638 GLU GLU B . n B 2 639 ILE 639 639 639 ILE ILE B . n B 2 640 GLU 640 640 640 GLU GLU B . n B 2 641 SER 641 641 641 SER SER B . n B 2 642 VAL 642 642 642 VAL VAL B . n B 2 643 LYS 643 643 643 LYS LYS B . n B 2 644 GLU 644 644 644 GLU GLU B . n B 2 645 LEU 645 645 645 LEU LEU B . n B 2 646 LYS 646 646 646 LYS LYS B . n B 2 647 ASP 647 647 647 ASP ASP B . n B 2 648 THR 648 648 648 THR THR B . n B 2 649 GLY 649 649 649 GLY GLY B . n B 2 650 LYS 650 650 650 LYS LYS B . n B 2 651 ASP 651 651 651 ASP ASP B . n B 2 652 ALA 652 652 652 ALA ALA B . n B 2 653 VAL 653 653 653 VAL VAL B . n B 2 654 ASN 654 654 654 ASN ASN B . n B 2 655 CYS 655 655 655 CYS CYS B . n B 2 656 THR 656 656 656 THR THR B . n B 2 657 TYR 657 657 657 TYR TYR B . n B 2 658 LYS 658 658 658 LYS LYS B . n B 2 659 ASN 659 659 659 ASN ASN B . n B 2 660 GLU 660 660 660 GLU GLU B . n B 2 661 ASP 661 661 661 ASP ASP B . n B 2 662 ASP 662 662 662 ASP ASP B . n B 2 663 CYS 663 663 663 CYS CYS B . n B 2 664 VAL 664 664 664 VAL VAL B . n B 2 665 VAL 665 665 665 VAL VAL B . n B 2 666 ARG 666 666 666 ARG ARG B . n B 2 667 PHE 667 667 667 PHE PHE B . n B 2 668 GLN 668 668 668 GLN GLN B . n B 2 669 TYR 669 669 669 TYR TYR B . n B 2 670 TYR 670 670 670 TYR TYR B . n B 2 671 GLU 671 671 671 GLU GLU B . n B 2 672 ASP 672 672 672 ASP ASP B . n B 2 673 SER 673 673 673 SER SER B . n B 2 674 SER 674 674 674 SER SER B . n B 2 675 GLY 675 675 675 GLY GLY B . n B 2 676 LYS 676 676 676 LYS LYS B . n B 2 677 SER 677 677 677 SER SER B . n B 2 678 ILE 678 678 678 ILE ILE B . n B 2 679 LEU 679 679 679 LEU LEU B . n B 2 680 TYR 680 680 680 TYR TYR B . n B 2 681 VAL 681 681 681 VAL VAL B . n B 2 682 VAL 682 682 682 VAL VAL B . n B 2 683 GLU 683 683 683 GLU GLU B . n B 2 684 GLU 684 684 684 GLU GLU B . n B 2 685 PRO 685 685 685 PRO PRO B . n B 2 686 GLU 686 686 686 GLU GLU B . n B 2 687 CYS 687 687 687 CYS CYS B . n B 2 688 PRO 688 688 688 PRO PRO B . n B 2 689 LYS 689 689 689 LYS LYS B . n B 2 690 GLY 690 690 690 GLY GLY B . n B 2 691 PRO 691 691 ? ? ? B . n B 2 692 ASP 692 692 ? ? ? B . n C 3 1 SER 1 1417 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 GLY 76 1492 1492 GLY GLY 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 SER 80 1496 1496 SER SER C . n C 3 81 PRO 81 1497 1497 PRO PRO C . n C 3 82 ALA 82 1498 1498 ALA ALA C . n C 3 83 SER 83 1499 1499 SER SER 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 1508 ARG ARG C . n C 3 93 THR 93 1509 1509 THR THR C . n C 3 94 GLY 94 1510 ? ? ? C . n C 3 95 LYS 95 1511 ? ? ? C . n C 3 96 LYS 96 1512 ? ? ? C . n C 3 97 GLY 97 1513 ? ? ? C . n C 3 98 LYS 98 1514 ? ? ? C . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code D 4 NAG 1 1001 1001 NAG NAG A . E 4 NAG 2 1002 1002 NAG NAG A . F 5 BMA 3 1003 1003 BMA BMA A . G 6 MAN 4 1004 1004 MAN MAN A . H 4 NAG 1 1005 1005 NAG NAG A . I 4 NAG 2 1006 1006 NAG NAG A . J 4 NAG 1 1007 1007 NAG NAG A . K 4 NAG 2 1008 1008 NAG NAG A . L 5 BMA 3 1009 1009 BMA BMA A . M 6 MAN 4 1010 1010 MAN MAN A . N 5 BMA 5 1011 1011 BMA BMA A . O 6 MAN 6 1012 1012 MAN MAN A . P 4 NAG 1 1013 1013 NAG NAG A . Q 4 NAG 2 1014 1014 NAG NAG A . R 5 BMA 3 1015 1015 BMA BMA A . S 6 MAN 4 1016 1016 MAN MAN A . T 4 NAG 1 1017 1017 NAG NAG A . U 4 NAG 1 1018 1018 NAG NAG A . V 4 NAG 2 1019 1019 NAG NAG A . W 4 NAG 1 1020 1020 NAG NAG A . X 4 NAG 1 1021 1021 NAG NAG A . Y 4 NAG 1 1022 1022 NAG NAG A . Z 4 NAG 2 1023 1023 NAG NAG A . AA 4 NAG 1 1024 1024 NAG NAG A . BA 4 NAG 2 1025 1025 NAG NAG A . CA 5 BMA 3 1026 1026 BMA BMA A . DA 7 MN 1 1027 1027 MN MN A . EA 7 MN 1 1028 1028 MN MN A . FA 7 MN 1 1029 1029 MN MN A . GA 7 MN 1 1030 1030 MN MN A . HA 7 MN 1 1031 1031 MN MN A . IA 4 NAG 1 701 701 NAG NAG B . JA 4 NAG 1 702 702 NAG NAG B . KA 4 NAG 1 703 703 NAG NAG B . LA 4 NAG 2 704 704 NAG NAG B . MA 4 NAG 1 705 705 NAG NAG B . NA 4 NAG 2 706 706 NAG NAG B . OA 5 BMA 3 707 707 BMA BMA B . PA 7 MN 1 708 708 MN MN B . QA 7 MN 1 709 709 MN MN B . RA 7 MN 1 710 710 MN MN B . SA 8 HOH 1 801 801 HOH HOH B . SA 8 HOH 2 802 802 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 266 A ASN 266 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 371 B ASN 371 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 943 A ASN 943 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 260 A ASN 260 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 585 A ASN 585 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 458 A ASN 458 ? ASN 'GLYCOSYLATION SITE' 7 B ASN 320 B ASN 320 ? ASN 'GLYCOSYLATION SITE' 8 A ASN 950 A ASN 950 ? ASN 'GLYCOSYLATION SITE' 9 B ASN 559 B ASN 559 ? ASN 'GLYCOSYLATION SITE' 10 A ASN 821 A ASN 821 ? ASN 'GLYCOSYLATION SITE' 11 A ASN 44 A ASN 44 ? ASN 'GLYCOSYLATION SITE' 12 A ASN 524 A ASN 524 ? ASN 'GLYCOSYLATION SITE' 13 B ASN 99 B ASN 99 ? ASN 'GLYCOSYLATION SITE' 14 A ASN 674 A ASN 674 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 16100 ? 1 MORE 49 ? 1 'SSA (A^2)' 79550 ? # _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 ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 74.3 ? 2 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 101.7 ? 3 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 89.9 ? 4 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 136.4 ? 5 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 62.4 ? 6 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 83.5 ? 7 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 102.7 ? 8 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 149.4 ? 9 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 60.5 ? 10 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 116.7 ? 11 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 92.1 ? 12 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 62.3 ? 13 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 144.3 ? 14 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 64.4 ? 15 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 147.7 ? 16 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 77.1 ? 17 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 103.8 ? 18 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 86.8 ? 19 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 113.6 ? 20 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 147.1 ? 21 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 60.7 ? 22 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 143.7 ? 23 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 70.2 ? 24 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 89.7 ? 25 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 102.4 ? 26 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 78.7 ? 27 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 71.7 ? 28 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 157.4 ? 29 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 139.4 ? 30 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 76.7 ? 31 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 76.6 ? 32 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 92.7 ? 33 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 163.6 ? 34 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 141.8 ? 35 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 69.1 ? 36 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 124.2 ? 37 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 88.8 ? 38 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 110.0 ? 39 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 81.8 ? 40 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 87.5 ? 41 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 93.0 ? 42 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 58.5 ? 43 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 110.6 ? 44 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 83.3 ? 45 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 167.3 ? 46 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 75.2 ? 47 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 69.4 ? 48 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 138.6 ? 49 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 90.5 ? 50 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 141.4 ? 51 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 60.7 ? 52 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 81.5 ? 53 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 71.1 ? 54 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 82.8 ? 55 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 143.0 ? 56 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 142.2 ? 57 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 92.2 ? 58 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 102.5 ? 59 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 118.6 ? 60 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 60.7 ? 61 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 121.9 ? 62 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 123 ? B SER 123 ? 1_555 149.1 ? 63 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 123 ? B SER 123 ? 1_555 79.2 ? 64 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 121 ? B SER 121 ? 1_555 106.5 ? 65 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 121 ? B SER 121 ? 1_555 92.9 ? 66 OG ? B SER 123 ? B SER 123 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 121 ? B SER 121 ? 1_555 93.3 ? 67 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 802 ? 1_555 94.7 ? 68 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 802 ? 1_555 142.1 ? 69 OG ? B SER 123 ? B SER 123 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 802 ? 1_555 63.2 ? 70 OG ? B SER 121 ? B SER 121 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 802 ? 1_555 84.9 ? 71 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 801 ? 1_555 78.5 ? 72 OD1 ? C ASP 79 ? C ASP 1495 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 801 ? 1_555 96.7 ? 73 OG ? B SER 123 ? B SER 123 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 801 ? 1_555 76.7 ? 74 OG ? B SER 121 ? B SER 121 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 801 ? 1_555 164.6 ? 75 O ? SA HOH . ? B HOH 802 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? SA HOH . ? B HOH 801 ? 1_555 80.1 ? 76 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 89.0 ? 77 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 128.2 ? 78 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 110.7 ? 79 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 148.5 ? 80 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 61.4 ? 81 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 61.3 ? 82 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 61.3 ? 83 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 87.1 ? 84 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 158.6 ? 85 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 122.5 ? 86 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 63.2 ? 87 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 88.7 ? 88 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 69.6 ? 89 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 103.0 ? 90 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 124.4 ? 91 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 61.2 ? 92 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 118.6 ? 93 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 139.7 ? 94 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 132.5 ? 95 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 152.8 ? 96 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 61.0 ? 97 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 70.7 ? 98 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 122.5 ? 99 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 89.9 ? 100 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 61.9 ? 101 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 95.8 ? 102 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 76.2 ? 103 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 138.3 ? 104 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 78.7 ? 105 O ? A CYS 596 ? A CYS 596 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 79.4 ? 106 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 127.5 ? 107 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 95.6 ? 108 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 134.2 ? 109 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 73.9 ? 110 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 94.0 ? 111 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 114.6 ? 112 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 60.9 ? 113 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 70.7 ? 114 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 134.1 ? 115 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 97.0 ? 116 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 145.7 ? 117 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 84.0 ? 118 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 60.8 ? 119 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 92.8 ? 120 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 153.4 ? 121 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 104.1 ? 122 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 67.9 ? 123 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 89.4 ? 124 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 156.0 ? 125 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 63.0 ? 126 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 100.4 ? # 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 7.6704 56.0227 22.3377 0.6904 0.3533 0.4231 -0.2076 -0.0271 0.0160 4.3906 3.0593 2.1627 0.8884 0.6957 -0.5939 -0.3552 0.2645 0.2765 -0.2235 0.2243 -0.0609 -0.4653 0.1520 0.1425 'X-RAY DIFFRACTION' 2 ? refined -27.3462 48.1263 1.3003 0.9959 0.7645 0.8212 -0.3319 -0.2124 0.1530 5.2981 -0.2665 0.8940 0.1933 2.1397 0.0027 -0.1531 0.7351 0.1780 -0.2755 0.1111 0.2250 -0.0398 0.0724 0.0594 'X-RAY DIFFRACTION' 3 ? refined -51.8249 42.5084 21.8435 0.7898 0.5470 0.7545 -0.0566 -0.1890 0.0677 2.7018 3.2187 9.0208 -0.7638 1.2682 -1.3198 -0.2405 -0.1566 0.0558 -0.0511 0.1971 0.3381 0.2684 0.4128 -0.0759 'X-RAY DIFFRACTION' 4 ? refined -26.1579 36.5412 71.6901 0.8593 0.4727 0.6140 0.2395 0.0473 -0.0590 4.9222 3.2128 6.7644 -2.0789 3.2605 -2.1224 -0.1550 -0.4131 -0.0615 0.4357 0.0949 -0.0331 0.0388 -0.0316 0.0321 'X-RAY DIFFRACTION' 5 ? refined -33.1360 2.3980 11.7970 1.3274 0.7164 1.2830 -0.3053 -0.1377 -0.0130 8.1396 2.4857 6.1747 -2.3066 5.5588 -2.3752 0.2957 0.3559 -1.2890 -0.5987 0.3098 0.3827 0.4292 -0.5509 -0.5062 'X-RAY DIFFRACTION' 6 ? refined 6.7715 15.5187 34.8628 0.8462 0.3871 0.8027 -0.0059 -0.0195 0.0251 2.9381 3.6621 0.9410 1.4970 0.2989 -0.9872 0.2982 -0.2075 -1.2058 0.5488 -0.2607 -1.0019 0.3011 0.1458 -0.1428 'X-RAY DIFFRACTION' 7 ? refined 18.3917 27.1448 31.7473 0.6910 0.4161 1.0625 -0.0766 -0.0120 -0.0094 1.2874 4.6073 2.7900 0.2862 -0.5693 -1.5402 0.0984 0.0834 -0.8833 -0.1256 0.1570 -0.8196 0.2755 0.4518 -0.2355 'X-RAY DIFFRACTION' 8 ? refined -3.8331 18.6510 33.7582 0.9226 0.3813 0.7074 -0.0438 -0.0131 0.0795 3.8418 4.7899 0.0008 3.3952 0.0765 0.8594 -0.0753 -0.2195 -0.5022 0.0282 -0.0898 -0.2800 0.3084 -0.0967 0.1667 'X-RAY DIFFRACTION' 9 ? refined -30.5690 7.8594 -2.3379 2.0135 2.0320 1.0894 -0.3861 -0.1296 -0.0713 2.1800 3.2293 2.1099 -3.2691 1.6845 -2.7061 0.6809 2.6311 -0.2506 -1.6997 -0.6401 0.4364 1.3027 0.2625 -0.0145 'X-RAY DIFFRACTION' 10 ? refined -38.5301 24.4071 15.2156 1.2157 0.8646 1.3107 -0.2304 -0.2502 0.0657 6.0040 2.6980 3.5831 0.2562 2.8339 2.0840 -0.6597 0.7280 0.9211 -0.9438 -0.1495 1.0887 -0.1710 -0.0259 0.8049 'X-RAY DIFFRACTION' 11 ? refined -18.5482 17.3280 58.9574 0.9494 0.5691 1.0607 -0.0260 0.0384 -0.0382 4.3504 2.2259 4.3707 -6.7994 4.5894 -6.5626 -0.1708 -0.3350 -0.0070 -0.4141 0.2678 -1.3793 0.1384 -0.4051 -0.1612 'X-RAY DIFFRACTION' 12 ? refined -7.5494 15.2362 68.4775 1.3279 0.5809 1.2316 0.2755 -0.0487 0.0842 3.2280 1.6969 5.7685 2.3051 0.8759 1.9466 -0.0670 0.1901 -0.0700 0.1472 0.1623 -0.7019 0.0135 0.6996 -0.1742 'X-RAY DIFFRACTION' 13 ? refined 27.4369 47.1899 61.8913 3.0541 1.8254 2.1234 0.6199 -0.8702 -0.4401 0.1995 1.1815 1.9972 -0.4275 -1.3764 3.5686 0.6349 0.4684 0.1802 0.8019 -0.3390 -0.2921 -0.2192 0.8305 -0.1297 'X-RAY DIFFRACTION' 14 ? refined 15.9331 46.4354 78.4304 5.2685 4.1225 2.7309 1.3106 -0.8064 -1.6195 0.5514 2.0306 0.0502 1.0101 -0.1249 -0.3060 0.0147 -2.0355 1.3881 1.3349 -1.5611 2.1458 -1.5102 1.5451 1.2885 'X-RAY DIFFRACTION' 15 ? refined 18.6445 46.6688 60.1587 2.3062 1.6258 1.0968 -0.0045 -0.0317 -0.1215 9.2787 2.0660 2.0855 -4.1987 8.9062 -6.5389 -0.2749 -1.8038 0.7175 1.9619 -1.0808 -1.1184 2.7997 0.8585 1.3704 'X-RAY DIFFRACTION' 16 ? refined 16.3178 28.8732 68.6822 2.8450 1.7921 2.3978 0.3147 -0.1910 0.2550 2.0047 7.5850 9.3371 -1.5476 4.3422 4.4741 -0.8602 2.1821 3.7840 -1.6325 -1.8395 -0.3513 -2.6104 0.5692 2.5497 'X-RAY DIFFRACTION' 17 ? refined 13.2785 48.2996 62.6235 1.9604 1.4019 1.1627 -0.1782 0.4799 -0.0212 6.6580 7.6071 8.5513 -6.7997 -1.6307 4.0153 0.5768 -1.3693 -0.6912 2.2399 -1.6917 2.7145 1.5124 1.7217 1.1122 'X-RAY DIFFRACTION' 18 ? refined 14.5963 36.3368 76.4496 2.1361 3.0573 1.9623 0.4741 0.3413 0.9116 6.8784 3.8529 9.0328 4.4080 -0.6743 -3.4556 0.4175 -0.4821 -0.0227 -1.2215 -1.4617 -1.5183 4.0437 2.9725 1.1077 'X-RAY DIFFRACTION' 19 ? refined 19.6309 40.1499 61.7817 3.0997 2.5867 1.0750 -0.9451 -0.0637 -0.3614 6.0018 1.6628 5.6361 -3.1645 -5.8047 3.0484 -0.1676 -3.3730 -0.2199 2.7305 0.6362 -1.0777 2.9459 0.4031 -0.5229 'X-RAY DIFFRACTION' 20 ? refined 20.8235 41.5616 48.3461 1.5795 0.7429 1.2194 -0.1504 -0.3793 0.1359 7.0362 4.7647 9.1199 -5.0136 -7.1467 6.5656 -0.2013 -1.8619 1.1858 2.0880 -0.4101 -2.7486 3.6507 1.0801 0.4315 'X-RAY DIFFRACTION' 21 ? refined 23.8692 38.8688 73.2168 2.4879 3.6146 1.6814 0.1458 0.7988 0.6440 -0.0149 -0.0195 -0.0054 -0.0151 -0.0129 -0.0095 1.8068 -2.1859 -0.1172 1.1708 0.3077 0.0987 -5.3689 0.7216 -1.8447 # 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 320 ) ; 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 321 through 590 ) ; 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 591 through 729 ) ; 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 730 through 956 ) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 5 through 75 ) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 76 through 169 ) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 170 through 278 ) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 279 through 423 ) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 424 through 462 ) ; 'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 463 through 588 ) ; 'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 589 through 630 ) ; 'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 631 through 690 ) ; 'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1417 through 1425 ) ; 'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1426 through 1433 ) ; 'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1434 through 1452 ) ; 'X-RAY DIFFRACTION' 16 16 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1453 through 1461 ) ; 'X-RAY DIFFRACTION' 17 17 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1462 through 1473 ) ; 'X-RAY DIFFRACTION' 18 18 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1474 through 1483 ) ; 'X-RAY DIFFRACTION' 19 19 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1484 through 1490 ) ; 'X-RAY DIFFRACTION' 20 20 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1491 through 1502 ) ; 'X-RAY DIFFRACTION' 21 21 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1503 through 1509 ) ; # 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_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 C A TYR 450 ? ? N A PRO 451 ? ? CD A PRO 451 ? ? 102.97 128.40 -25.43 2.10 Y 2 1 C B SER 162 ? ? N B PRO 163 ? ? CD B PRO 163 ? ? 110.24 128.40 -18.16 2.10 Y # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 THR A 64 ? ? 66.28 -13.46 2 1 PHE A 72 ? ? -107.54 -67.37 3 1 ASP A 73 ? ? -92.21 -65.35 4 1 ALA A 74 ? ? 66.97 -4.63 5 1 ASN A 77 ? ? -90.67 -83.56 6 1 ARG A 78 ? ? 170.90 173.97 7 1 LYS A 82 ? ? -47.68 -71.31 8 1 ASP A 84 ? ? -151.67 80.60 9 1 GLN A 102 ? ? 55.70 -119.36 10 1 ARG A 115 ? ? 85.53 -10.56 11 1 THR A 116 ? ? 51.30 -152.39 12 1 MET A 118 ? ? -100.55 -74.54 13 1 PRO A 124 ? ? -68.59 68.85 14 1 THR A 134 ? ? -140.02 -66.80 15 1 ASP A 148 ? ? 55.81 -145.44 16 1 THR A 249 ? ? 74.57 -3.83 17 1 ALA A 273 ? ? 66.47 -3.65 18 1 ASP A 289 ? ? 72.74 -3.82 19 1 PHE A 334 ? ? -124.39 -62.99 20 1 PHE A 337 ? ? 66.85 -2.05 21 1 ARG A 339 ? ? 57.08 71.07 22 1 VAL A 386 ? ? 174.49 136.65 23 1 ARG A 398 ? ? -95.85 -66.45 24 1 SER A 399 ? ? -108.34 -62.79 25 1 TYR A 406 ? ? 74.39 -18.27 26 1 VAL A 440 ? ? 56.44 73.46 27 1 PRO A 451 ? ? 9.37 62.35 28 1 THR A 466 ? ? 65.30 75.81 29 1 LEU A 487 ? ? -177.23 143.07 30 1 GLN A 504 ? ? 74.19 -5.52 31 1 SER A 528 ? ? -131.84 -68.71 32 1 ASP A 550 ? ? 55.66 -143.60 33 1 LYS A 551 ? ? 174.30 163.91 34 1 LEU A 563 ? ? 62.13 71.92 35 1 ALA A 568 ? ? 57.48 73.93 36 1 ASP A 570 ? ? 52.52 -142.94 37 1 THR A 572 ? ? 52.00 -113.39 38 1 ASP A 613 ? ? 55.75 -117.69 39 1 LEU A 649 ? ? 53.19 -118.33 40 1 ILE A 654 ? ? -105.34 -64.82 41 1 HIS A 702 ? ? -106.61 -78.22 42 1 GLN A 703 ? ? 175.77 162.93 43 1 SER A 705 ? ? 50.50 -127.78 44 1 THR A 709 ? ? 56.14 -116.31 45 1 GLU A 767 ? ? -126.42 -63.18 46 1 VAL A 772 ? ? -108.18 -64.85 47 1 ASN A 785 ? ? -107.07 -60.48 48 1 PRO A 800 ? ? -69.88 77.75 49 1 ASN A 805 ? ? 71.06 -3.78 50 1 LEU A 808 ? ? -100.96 -73.68 51 1 LEU A 812 ? ? -97.54 -69.87 52 1 ARG A 832 ? ? 52.76 -145.00 53 1 ILE A 833 ? ? 172.44 169.61 54 1 LYS A 834 ? ? -101.48 -76.47 55 1 MET A 909 ? ? 59.08 -131.98 56 1 ASN A 910 ? ? 49.20 -136.01 57 1 ASN A 913 ? ? 64.82 77.49 58 1 ASN A 935 ? ? 56.33 19.98 59 1 ARG B 8 ? ? -131.27 -67.84 60 1 VAL B 19 ? ? -136.69 -66.80 61 1 ASP B 28 ? ? 65.14 79.15 62 1 GLU B 29 ? ? -55.66 -9.84 63 1 LEU B 31 ? ? 53.22 72.45 64 1 LEU B 33 ? ? 50.75 -142.74 65 1 SER B 35 ? ? 175.15 155.34 66 1 LYS B 41 ? ? 44.39 -123.93 67 1 ASN B 48 ? ? -55.08 -75.12 68 1 ASP B 71 ? ? -121.33 -61.64 69 1 SER B 78 ? ? -54.97 -74.81 70 1 GLN B 79 ? ? -126.04 -78.95 71 1 GLN B 86 ? ? -108.88 -62.17 72 1 ASN B 133 ? ? 59.02 -108.67 73 1 LEU B 134 ? ? 61.39 -112.09 74 1 ASN B 148 ? ? 59.79 70.88 75 1 VAL B 157 ? ? -122.42 -73.74 76 1 VAL B 161 ? ? -158.95 -152.08 77 1 SER B 162 ? ? -25.62 -172.57 78 1 PRO B 163 ? ? -5.46 -72.09 79 1 TYR B 164 ? ? -15.75 -55.72 80 1 SER B 168 ? ? -61.65 -177.16 81 1 TYR B 178 ? ? -121.49 -59.32 82 1 MET B 180 ? ? 82.94 -2.53 83 1 LEU B 258 ? ? 72.13 -4.80 84 1 SER B 337 ? ? 64.27 -134.20 85 1 ASN B 339 ? ? 57.11 -148.03 86 1 LEU B 341 ? ? -59.33 -73.33 87 1 LEU B 343 ? ? -57.50 -73.68 88 1 ASN B 376 ? ? 37.42 65.59 89 1 CYS B 406 ? ? -177.79 134.43 90 1 PRO B 407 ? ? -89.45 46.59 91 1 GLN B 408 ? ? 38.38 64.80 92 1 LYS B 410 ? ? -100.08 -70.37 93 1 CYS B 433 ? ? -125.39 -63.78 94 1 HIS B 446 ? ? 83.04 -1.77 95 1 CYS B 448 ? ? -104.73 -78.86 96 1 TRP B 466 ? ? -103.69 -64.04 97 1 LEU B 467 ? ? 43.68 72.90 98 1 GLN B 470 ? ? -120.62 -80.07 99 1 GLU B 472 ? ? 175.44 157.98 100 1 CYS B 473 ? ? -170.26 -167.50 101 1 GLU B 475 ? ? 89.21 -9.12 102 1 GLU B 476 ? ? -129.60 -69.77 103 1 ASP B 477 ? ? 65.47 -11.87 104 1 TYR B 478 ? ? 46.15 -136.73 105 1 SER B 481 ? ? 73.73 -16.47 106 1 GLN B 482 ? ? 175.91 161.79 107 1 PRO B 493 ? ? -67.48 -172.62 108 1 GLN B 497 ? ? 47.77 -127.06 109 1 ARG B 498 ? ? 50.73 78.62 110 1 GLU B 500 ? ? 53.40 -141.09 111 1 CYS B 503 ? ? 43.03 72.78 112 1 SER B 510 ? ? 64.77 -15.54 113 1 SER B 511 ? ? 64.31 -3.09 114 1 PHE B 513 ? ? 36.52 60.99 115 1 ASP B 525 ? ? 70.91 -13.32 116 1 PHE B 526 ? ? -108.59 -60.79 117 1 TYR B 531 ? ? -102.54 -77.46 118 1 GLN B 590 ? ? 172.59 148.12 119 1 CYS B 604 ? ? 179.93 160.77 120 1 ALA B 607 ? ? 52.78 -116.34 121 1 ALA B 624 ? ? 75.66 -23.41 122 1 GLU B 644 ? ? 62.92 -6.68 123 1 SER B 674 ? ? 63.32 -5.21 124 1 LYS B 676 ? ? 172.54 163.97 125 1 GLU B 684 ? ? 55.64 71.02 126 1 VAL C 1419 ? ? 174.40 164.22 127 1 PRO C 1420 ? ? -69.41 -138.30 128 1 ARG C 1421 ? ? 79.80 -147.11 129 1 ASP C 1422 ? ? 36.16 62.15 130 1 VAL C 1426 ? ? -104.09 -74.64 131 1 SER C 1432 ? ? 54.86 -142.65 132 1 LEU C 1433 ? ? 175.64 169.41 133 1 ALA C 1441 ? ? 80.24 -3.55 134 1 ARG C 1493 ? ? -133.00 -64.26 135 1 SER C 1496 ? ? 170.85 146.14 136 1 SER C 1499 ? ? 170.28 175.69 137 1 SER C 1500 ? ? -120.60 -78.73 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A SER 836 ? A SER 836 2 1 Y 1 A SER 837 ? A SER 837 3 1 Y 1 A LEU 838 ? A LEU 838 4 1 Y 1 A GLN 839 ? A GLN 839 5 1 Y 1 A THR 840 ? A THR 840 6 1 Y 1 A THR 841 ? A THR 841 7 1 Y 1 A GLU 842 ? A GLU 842 8 1 Y 1 A LYS 843 ? A LYS 843 9 1 Y 1 A ASN 844 ? A ASN 844 10 1 Y 1 A ASP 845 ? A ASP 845 11 1 Y 1 A THR 846 ? A THR 846 12 1 Y 1 A VAL 847 ? A VAL 847 13 1 Y 1 A ALA 848 ? A ALA 848 14 1 Y 1 A GLY 849 ? A GLY 849 15 1 Y 1 A GLN 850 ? A GLN 850 16 1 Y 1 A GLY 851 ? A GLY 851 17 1 Y 1 A GLU 852 ? A GLU 852 18 1 Y 1 A ARG 853 ? A ARG 853 19 1 Y 1 A ASP 854 ? A ASP 854 20 1 Y 1 A HIS 855 ? A HIS 855 21 1 Y 1 A LEU 856 ? A LEU 856 22 1 Y 1 A ILE 857 ? A ILE 857 23 1 Y 1 A THR 858 ? A THR 858 24 1 Y 1 A LYS 859 ? A LYS 859 25 1 Y 1 A ARG 860 ? A ARG 860 26 1 Y 1 A ASP 861 ? A ASP 861 27 1 Y 1 A LEU 862 ? A LEU 862 28 1 Y 1 A ALA 863 ? A ALA 863 29 1 Y 1 A LEU 864 ? A LEU 864 30 1 Y 1 A SER 865 ? A SER 865 31 1 Y 1 A GLU 866 ? A GLU 866 32 1 Y 1 A GLY 867 ? A GLY 867 33 1 Y 1 A PRO 957 ? A PRO 957 34 1 Y 1 A ALA 958 ? A ALA 958 35 1 Y 1 A PRO 959 ? A PRO 959 36 1 Y 1 B PRO 691 ? B PRO 691 37 1 Y 1 B ASP 692 ? B ASP 692 38 1 Y 1 C GLY 1510 ? C GLY 94 39 1 Y 1 C LYS 1511 ? C LYS 95 40 1 Y 1 C LYS 1512 ? C LYS 96 41 1 Y 1 C GLY 1513 ? C GLY 97 42 1 Y 1 C LYS 1514 ? C LYS 98 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 N-ACETYL-D-GLUCOSAMINE NAG 5 BETA-D-MANNOSE BMA 6 ALPHA-D-MANNOSE MAN 7 'MANGANESE (II) ION' MN 8 water HOH #