data_5GQR # _entry.id 5GQR # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.284 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5GQR WWPDB D_1300001301 # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5GQR _pdbx_database_status.recvd_initial_deposition_date 2016-08-08 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _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 'Chai, J.J.' 1 'Zhang, H.Q.' 2 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country UK _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Mol Plant' _citation.journal_id_ASTM ? _citation.journal_id_CSD ? _citation.journal_id_ISSN 1752-9867 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 9 _citation.language ? _citation.page_first 1406 _citation.page_last 1414 _citation.title 'SERK Family Receptor-like Kinases Function as Co-receptors with PXY for Plant Vascular Development' _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1016/j.molp.2016.07.004 _citation.pdbx_database_id_PubMed 27449136 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zhang, H.Q.' 1 primary 'Lin, X.Y.' 2 primary 'Han, Z.F.' 3 primary 'Wang, J.' 4 primary 'Qu, L.J.' 5 primary 'Chai, J.J.' 6 # _cell.entry_id 5GQR _cell.length_a 162.422 _cell.length_b 162.422 _cell.length_c 187.234 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5GQR _symmetry.space_group_name_H-M 'P 62 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 180 # 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 'Leucine-rich repeat receptor-like protein kinase TDR' 65853.289 1 2.7.11.1 ? 'UNP residues 32-629' ? 2 polymer syn TDIF 1264.322 1 ? ? ? ? 3 polymer man 'Somatic embryogenesis receptor kinase 2' 20191.816 1 2.7.11.1 ? 'UNP residues 30-214' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Protein PHLOEM INTERCALATED WITH XYLEM' 3 SERK2 # 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 ;FSPQLLSLLSLKTSLSGPPSAFQDWKVPVNGQNDAVWCSWSGVVCDNVTAQVISLDLSHRNLSGRIPIQIRYLSSLLYLN LSGNSLEGSFPTSIFDLTKLTTLDISRNSFDSSFPPGISKLKFLKVFNAFSNNFEGLLPSDVSRLRFLEELNFGGSYFEG EIPAAYGGLQRLKFIHLAGNVLGGKLPPRLGLLTELQHMEIGYNHFNGNIPSEFALLSNLKYFDVSNCSLSGSLPQELGN LSNLETLFLFQNGFTGEIPESYSNLKSLKLLDFSSNQLSGSIPSGFSTLKNLTWLSLISNNLSGEVPEGIGELPELTTLF LWNNNFTGVLPHKLGSNGKLETMDVSNNSFTGTIPSSLCHGNKLYKLILFSNMFEGELPKSLTRCESLWRFRSQNNRLNG TIPIGFGSLRNLTFVDLSNNRFTDQIPADFATAPVLQYLNLSTNFFHRKLPENIWKAPNLQIFSASFSNLIGEIPNYVGC KSFYRIELQGNSLNGTIPWDIGHCEKLLCLNLSQNHLNGIIPWEISTLPSIADVDLSHNLLTGTIPSDFGSSKTITTFNV SYNQLIGPIPSGSFAHLNPSFFSSNEGLCGDLVGKPCN ; ;FSPQLLSLLSLKTSLSGPPSAFQDWKVPVNGQNDAVWCSWSGVVCDNVTAQVISLDLSHRNLSGRIPIQIRYLSSLLYLN LSGNSLEGSFPTSIFDLTKLTTLDISRNSFDSSFPPGISKLKFLKVFNAFSNNFEGLLPSDVSRLRFLEELNFGGSYFEG EIPAAYGGLQRLKFIHLAGNVLGGKLPPRLGLLTELQHMEIGYNHFNGNIPSEFALLSNLKYFDVSNCSLSGSLPQELGN LSNLETLFLFQNGFTGEIPESYSNLKSLKLLDFSSNQLSGSIPSGFSTLKNLTWLSLISNNLSGEVPEGIGELPELTTLF LWNNNFTGVLPHKLGSNGKLETMDVSNNSFTGTIPSSLCHGNKLYKLILFSNMFEGELPKSLTRCESLWRFRSQNNRLNG TIPIGFGSLRNLTFVDLSNNRFTDQIPADFATAPVLQYLNLSTNFFHRKLPENIWKAPNLQIFSASFSNLIGEIPNYVGC KSFYRIELQGNSLNGTIPWDIGHCEKLLCLNLSQNHLNGIIPWEISTLPSIADVDLSHNLLTGTIPSDFGSSKTITTFNV SYNQLIGPIPSGSFAHLNPSFFSSNEGLCGDLVGKPCN ; B ? 2 'polypeptide(L)' no yes 'HEVPSG(HYP)NPISN' HEVPSGPNPISN C ? 3 'polypeptide(L)' no no ;NMEGDALHSLRANLVDPNNVLQSWDPTLVNPCTWFHVTCNNENSVIRVDLGNADLSGQLVPQLGQLKNLQYLELYSNNIT GPVPSDLGNLTNLVSLDLYLNSFTGPIPDSLGKLFKLRFLRLNNNSLTGPIPMSLTNIMTLQVLDLSNNRLSGSVPDNGS FSLFTPISFANNLDLCGPVTSRPCP ; ;NMEGDALHSLRANLVDPNNVLQSWDPTLVNPCTWFHVTCNNENSVIRVDLGNADLSGQLVPQLGQLKNLQYLELYSNNIT GPVPSDLGNLTNLVSLDLYLNSFTGPIPDSLGKLFKLRFLRLNNNSLTGPIPMSLTNIMTLQVLDLSNNRLSGSVPDNGS FSLFTPISFANNLDLCGPVTSRPCP ; K ? # 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 SER n 1 3 PRO n 1 4 GLN n 1 5 LEU n 1 6 LEU n 1 7 SER n 1 8 LEU n 1 9 LEU n 1 10 SER n 1 11 LEU n 1 12 LYS n 1 13 THR n 1 14 SER n 1 15 LEU n 1 16 SER n 1 17 GLY n 1 18 PRO n 1 19 PRO n 1 20 SER n 1 21 ALA n 1 22 PHE n 1 23 GLN n 1 24 ASP n 1 25 TRP n 1 26 LYS n 1 27 VAL n 1 28 PRO n 1 29 VAL n 1 30 ASN n 1 31 GLY n 1 32 GLN n 1 33 ASN n 1 34 ASP n 1 35 ALA n 1 36 VAL n 1 37 TRP n 1 38 CYS n 1 39 SER n 1 40 TRP n 1 41 SER n 1 42 GLY n 1 43 VAL n 1 44 VAL n 1 45 CYS n 1 46 ASP n 1 47 ASN n 1 48 VAL n 1 49 THR n 1 50 ALA n 1 51 GLN n 1 52 VAL n 1 53 ILE n 1 54 SER n 1 55 LEU n 1 56 ASP n 1 57 LEU n 1 58 SER n 1 59 HIS n 1 60 ARG n 1 61 ASN n 1 62 LEU n 1 63 SER n 1 64 GLY n 1 65 ARG n 1 66 ILE n 1 67 PRO n 1 68 ILE n 1 69 GLN n 1 70 ILE n 1 71 ARG n 1 72 TYR n 1 73 LEU n 1 74 SER n 1 75 SER n 1 76 LEU n 1 77 LEU n 1 78 TYR n 1 79 LEU n 1 80 ASN n 1 81 LEU n 1 82 SER n 1 83 GLY n 1 84 ASN n 1 85 SER n 1 86 LEU n 1 87 GLU n 1 88 GLY n 1 89 SER n 1 90 PHE n 1 91 PRO n 1 92 THR n 1 93 SER n 1 94 ILE n 1 95 PHE n 1 96 ASP n 1 97 LEU n 1 98 THR n 1 99 LYS n 1 100 LEU n 1 101 THR n 1 102 THR n 1 103 LEU n 1 104 ASP n 1 105 ILE n 1 106 SER n 1 107 ARG n 1 108 ASN n 1 109 SER n 1 110 PHE n 1 111 ASP n 1 112 SER n 1 113 SER n 1 114 PHE n 1 115 PRO n 1 116 PRO n 1 117 GLY n 1 118 ILE n 1 119 SER n 1 120 LYS n 1 121 LEU n 1 122 LYS n 1 123 PHE n 1 124 LEU n 1 125 LYS n 1 126 VAL n 1 127 PHE n 1 128 ASN n 1 129 ALA n 1 130 PHE n 1 131 SER n 1 132 ASN n 1 133 ASN n 1 134 PHE n 1 135 GLU n 1 136 GLY n 1 137 LEU n 1 138 LEU n 1 139 PRO n 1 140 SER n 1 141 ASP n 1 142 VAL n 1 143 SER n 1 144 ARG n 1 145 LEU n 1 146 ARG n 1 147 PHE n 1 148 LEU n 1 149 GLU n 1 150 GLU n 1 151 LEU n 1 152 ASN n 1 153 PHE n 1 154 GLY n 1 155 GLY n 1 156 SER n 1 157 TYR n 1 158 PHE n 1 159 GLU n 1 160 GLY n 1 161 GLU n 1 162 ILE n 1 163 PRO n 1 164 ALA n 1 165 ALA n 1 166 TYR n 1 167 GLY n 1 168 GLY n 1 169 LEU n 1 170 GLN n 1 171 ARG n 1 172 LEU n 1 173 LYS n 1 174 PHE n 1 175 ILE n 1 176 HIS n 1 177 LEU n 1 178 ALA n 1 179 GLY n 1 180 ASN n 1 181 VAL n 1 182 LEU n 1 183 GLY n 1 184 GLY n 1 185 LYS n 1 186 LEU n 1 187 PRO n 1 188 PRO n 1 189 ARG n 1 190 LEU n 1 191 GLY n 1 192 LEU n 1 193 LEU n 1 194 THR n 1 195 GLU n 1 196 LEU n 1 197 GLN n 1 198 HIS n 1 199 MET n 1 200 GLU n 1 201 ILE n 1 202 GLY n 1 203 TYR n 1 204 ASN n 1 205 HIS n 1 206 PHE n 1 207 ASN n 1 208 GLY n 1 209 ASN n 1 210 ILE n 1 211 PRO n 1 212 SER n 1 213 GLU n 1 214 PHE n 1 215 ALA n 1 216 LEU n 1 217 LEU n 1 218 SER n 1 219 ASN n 1 220 LEU n 1 221 LYS n 1 222 TYR n 1 223 PHE n 1 224 ASP n 1 225 VAL n 1 226 SER n 1 227 ASN n 1 228 CYS n 1 229 SER n 1 230 LEU n 1 231 SER n 1 232 GLY n 1 233 SER n 1 234 LEU n 1 235 PRO n 1 236 GLN n 1 237 GLU n 1 238 LEU n 1 239 GLY n 1 240 ASN n 1 241 LEU n 1 242 SER n 1 243 ASN n 1 244 LEU n 1 245 GLU n 1 246 THR n 1 247 LEU n 1 248 PHE n 1 249 LEU n 1 250 PHE n 1 251 GLN n 1 252 ASN n 1 253 GLY n 1 254 PHE n 1 255 THR n 1 256 GLY n 1 257 GLU n 1 258 ILE n 1 259 PRO n 1 260 GLU n 1 261 SER n 1 262 TYR n 1 263 SER n 1 264 ASN n 1 265 LEU n 1 266 LYS n 1 267 SER n 1 268 LEU n 1 269 LYS n 1 270 LEU n 1 271 LEU n 1 272 ASP n 1 273 PHE n 1 274 SER n 1 275 SER n 1 276 ASN n 1 277 GLN n 1 278 LEU n 1 279 SER n 1 280 GLY n 1 281 SER n 1 282 ILE n 1 283 PRO n 1 284 SER n 1 285 GLY n 1 286 PHE n 1 287 SER n 1 288 THR n 1 289 LEU n 1 290 LYS n 1 291 ASN n 1 292 LEU n 1 293 THR n 1 294 TRP n 1 295 LEU n 1 296 SER n 1 297 LEU n 1 298 ILE n 1 299 SER n 1 300 ASN n 1 301 ASN n 1 302 LEU n 1 303 SER n 1 304 GLY n 1 305 GLU n 1 306 VAL n 1 307 PRO n 1 308 GLU n 1 309 GLY n 1 310 ILE n 1 311 GLY n 1 312 GLU n 1 313 LEU n 1 314 PRO n 1 315 GLU n 1 316 LEU n 1 317 THR n 1 318 THR n 1 319 LEU n 1 320 PHE n 1 321 LEU n 1 322 TRP n 1 323 ASN n 1 324 ASN n 1 325 ASN n 1 326 PHE n 1 327 THR n 1 328 GLY n 1 329 VAL n 1 330 LEU n 1 331 PRO n 1 332 HIS n 1 333 LYS n 1 334 LEU n 1 335 GLY n 1 336 SER n 1 337 ASN n 1 338 GLY n 1 339 LYS n 1 340 LEU n 1 341 GLU n 1 342 THR n 1 343 MET n 1 344 ASP n 1 345 VAL n 1 346 SER n 1 347 ASN n 1 348 ASN n 1 349 SER n 1 350 PHE n 1 351 THR n 1 352 GLY n 1 353 THR n 1 354 ILE n 1 355 PRO n 1 356 SER n 1 357 SER n 1 358 LEU n 1 359 CYS n 1 360 HIS n 1 361 GLY n 1 362 ASN n 1 363 LYS n 1 364 LEU n 1 365 TYR n 1 366 LYS n 1 367 LEU n 1 368 ILE n 1 369 LEU n 1 370 PHE n 1 371 SER n 1 372 ASN n 1 373 MET n 1 374 PHE n 1 375 GLU n 1 376 GLY n 1 377 GLU n 1 378 LEU n 1 379 PRO n 1 380 LYS n 1 381 SER n 1 382 LEU n 1 383 THR n 1 384 ARG n 1 385 CYS n 1 386 GLU n 1 387 SER n 1 388 LEU n 1 389 TRP n 1 390 ARG n 1 391 PHE n 1 392 ARG n 1 393 SER n 1 394 GLN n 1 395 ASN n 1 396 ASN n 1 397 ARG n 1 398 LEU n 1 399 ASN n 1 400 GLY n 1 401 THR n 1 402 ILE n 1 403 PRO n 1 404 ILE n 1 405 GLY n 1 406 PHE n 1 407 GLY n 1 408 SER n 1 409 LEU n 1 410 ARG n 1 411 ASN n 1 412 LEU n 1 413 THR n 1 414 PHE n 1 415 VAL n 1 416 ASP n 1 417 LEU n 1 418 SER n 1 419 ASN n 1 420 ASN n 1 421 ARG n 1 422 PHE n 1 423 THR n 1 424 ASP n 1 425 GLN n 1 426 ILE n 1 427 PRO n 1 428 ALA n 1 429 ASP n 1 430 PHE n 1 431 ALA n 1 432 THR n 1 433 ALA n 1 434 PRO n 1 435 VAL n 1 436 LEU n 1 437 GLN n 1 438 TYR n 1 439 LEU n 1 440 ASN n 1 441 LEU n 1 442 SER n 1 443 THR n 1 444 ASN n 1 445 PHE n 1 446 PHE n 1 447 HIS n 1 448 ARG n 1 449 LYS n 1 450 LEU n 1 451 PRO n 1 452 GLU n 1 453 ASN n 1 454 ILE n 1 455 TRP n 1 456 LYS n 1 457 ALA n 1 458 PRO n 1 459 ASN n 1 460 LEU n 1 461 GLN n 1 462 ILE n 1 463 PHE n 1 464 SER n 1 465 ALA n 1 466 SER n 1 467 PHE n 1 468 SER n 1 469 ASN n 1 470 LEU n 1 471 ILE n 1 472 GLY n 1 473 GLU n 1 474 ILE n 1 475 PRO n 1 476 ASN n 1 477 TYR n 1 478 VAL n 1 479 GLY n 1 480 CYS n 1 481 LYS n 1 482 SER n 1 483 PHE n 1 484 TYR n 1 485 ARG n 1 486 ILE n 1 487 GLU n 1 488 LEU n 1 489 GLN n 1 490 GLY n 1 491 ASN n 1 492 SER n 1 493 LEU n 1 494 ASN n 1 495 GLY n 1 496 THR n 1 497 ILE n 1 498 PRO n 1 499 TRP n 1 500 ASP n 1 501 ILE n 1 502 GLY n 1 503 HIS n 1 504 CYS n 1 505 GLU n 1 506 LYS n 1 507 LEU n 1 508 LEU n 1 509 CYS n 1 510 LEU n 1 511 ASN n 1 512 LEU n 1 513 SER n 1 514 GLN n 1 515 ASN n 1 516 HIS n 1 517 LEU n 1 518 ASN n 1 519 GLY n 1 520 ILE n 1 521 ILE n 1 522 PRO n 1 523 TRP n 1 524 GLU n 1 525 ILE n 1 526 SER n 1 527 THR n 1 528 LEU n 1 529 PRO n 1 530 SER n 1 531 ILE n 1 532 ALA n 1 533 ASP n 1 534 VAL n 1 535 ASP n 1 536 LEU n 1 537 SER n 1 538 HIS n 1 539 ASN n 1 540 LEU n 1 541 LEU n 1 542 THR n 1 543 GLY n 1 544 THR n 1 545 ILE n 1 546 PRO n 1 547 SER n 1 548 ASP n 1 549 PHE n 1 550 GLY n 1 551 SER n 1 552 SER n 1 553 LYS n 1 554 THR n 1 555 ILE n 1 556 THR n 1 557 THR n 1 558 PHE n 1 559 ASN n 1 560 VAL n 1 561 SER n 1 562 TYR n 1 563 ASN n 1 564 GLN n 1 565 LEU n 1 566 ILE n 1 567 GLY n 1 568 PRO n 1 569 ILE n 1 570 PRO n 1 571 SER n 1 572 GLY n 1 573 SER n 1 574 PHE n 1 575 ALA n 1 576 HIS n 1 577 LEU n 1 578 ASN n 1 579 PRO n 1 580 SER n 1 581 PHE n 1 582 PHE n 1 583 SER n 1 584 SER n 1 585 ASN n 1 586 GLU n 1 587 GLY n 1 588 LEU n 1 589 CYS n 1 590 GLY n 1 591 ASP n 1 592 LEU n 1 593 VAL n 1 594 GLY n 1 595 LYS n 1 596 PRO n 1 597 CYS n 1 598 ASN n 2 1 HIS n 2 2 GLU n 2 3 VAL n 2 4 PRO n 2 5 SER n 2 6 GLY n 2 7 HYP n 2 8 ASN n 2 9 PRO n 2 10 ILE n 2 11 SER n 2 12 ASN n 3 1 ASN n 3 2 MET n 3 3 GLU n 3 4 GLY n 3 5 ASP n 3 6 ALA n 3 7 LEU n 3 8 HIS n 3 9 SER n 3 10 LEU n 3 11 ARG n 3 12 ALA n 3 13 ASN n 3 14 LEU n 3 15 VAL n 3 16 ASP n 3 17 PRO n 3 18 ASN n 3 19 ASN n 3 20 VAL n 3 21 LEU n 3 22 GLN n 3 23 SER n 3 24 TRP n 3 25 ASP n 3 26 PRO n 3 27 THR n 3 28 LEU n 3 29 VAL n 3 30 ASN n 3 31 PRO n 3 32 CYS n 3 33 THR n 3 34 TRP n 3 35 PHE n 3 36 HIS n 3 37 VAL n 3 38 THR n 3 39 CYS n 3 40 ASN n 3 41 ASN n 3 42 GLU n 3 43 ASN n 3 44 SER n 3 45 VAL n 3 46 ILE n 3 47 ARG n 3 48 VAL n 3 49 ASP n 3 50 LEU n 3 51 GLY n 3 52 ASN n 3 53 ALA n 3 54 ASP n 3 55 LEU n 3 56 SER n 3 57 GLY n 3 58 GLN n 3 59 LEU n 3 60 VAL n 3 61 PRO n 3 62 GLN n 3 63 LEU n 3 64 GLY n 3 65 GLN n 3 66 LEU n 3 67 LYS n 3 68 ASN n 3 69 LEU n 3 70 GLN n 3 71 TYR n 3 72 LEU n 3 73 GLU n 3 74 LEU n 3 75 TYR n 3 76 SER n 3 77 ASN n 3 78 ASN n 3 79 ILE n 3 80 THR n 3 81 GLY n 3 82 PRO n 3 83 VAL n 3 84 PRO n 3 85 SER n 3 86 ASP n 3 87 LEU n 3 88 GLY n 3 89 ASN n 3 90 LEU n 3 91 THR n 3 92 ASN n 3 93 LEU n 3 94 VAL n 3 95 SER n 3 96 LEU n 3 97 ASP n 3 98 LEU n 3 99 TYR n 3 100 LEU n 3 101 ASN n 3 102 SER n 3 103 PHE n 3 104 THR n 3 105 GLY n 3 106 PRO n 3 107 ILE n 3 108 PRO n 3 109 ASP n 3 110 SER n 3 111 LEU n 3 112 GLY n 3 113 LYS n 3 114 LEU n 3 115 PHE n 3 116 LYS n 3 117 LEU n 3 118 ARG n 3 119 PHE n 3 120 LEU n 3 121 ARG n 3 122 LEU n 3 123 ASN n 3 124 ASN n 3 125 ASN n 3 126 SER n 3 127 LEU n 3 128 THR n 3 129 GLY n 3 130 PRO n 3 131 ILE n 3 132 PRO n 3 133 MET n 3 134 SER n 3 135 LEU n 3 136 THR n 3 137 ASN n 3 138 ILE n 3 139 MET n 3 140 THR n 3 141 LEU n 3 142 GLN n 3 143 VAL n 3 144 LEU n 3 145 ASP n 3 146 LEU n 3 147 SER n 3 148 ASN n 3 149 ASN n 3 150 ARG n 3 151 LEU n 3 152 SER n 3 153 GLY n 3 154 SER n 3 155 VAL n 3 156 PRO n 3 157 ASP n 3 158 ASN n 3 159 GLY n 3 160 SER n 3 161 PHE n 3 162 SER n 3 163 LEU n 3 164 PHE n 3 165 THR n 3 166 PRO n 3 167 ILE n 3 168 SER n 3 169 PHE n 3 170 ALA n 3 171 ASN n 3 172 ASN n 3 173 LEU n 3 174 ASP n 3 175 LEU n 3 176 CYS n 3 177 GLY n 3 178 PRO n 3 179 VAL n 3 180 THR n 3 181 SER n 3 182 ARG n 3 183 PRO n 3 184 CYS n 3 185 PRO n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample 'Biological sequence' 1 598 'Mouse-ear cress' ? TDR ? ? ? ? ? ? 'Arabidopsis thaliana' 3702 ? ? ? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 3 1 sample 'Biological sequence' 1 185 'Mouse-ear cress' ? SERK2 ? ? ? ? ? ? 'Arabidopsis thaliana' 3702 ? ? ? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # _pdbx_entity_src_syn.entity_id 2 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num 1 _pdbx_entity_src_syn.pdbx_end_seq_num 12 _pdbx_entity_src_syn.organism_scientific Arabideae _pdbx_entity_src_syn.organism_common_name ? _pdbx_entity_src_syn.ncbi_taxonomy_id 981070 _pdbx_entity_src_syn.details ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin 1 UNP TDR_ARATH Q9FII5 ? 1 ;FSPQLLSLLSLKTSLSGPPSAFQDWKVPVNGQNDAVWCSWSGVVCDNVTAQVISLDLSHRNLSGRIPIQIRYLSSLLYLN LSGNSLEGSFPTSIFDLTKLTTLDISRNSFDSSFPPGISKLKFLKVFNAFSNNFEGLLPSDVSRLRFLEELNFGGSYFEG EIPAAYGGLQRLKFIHLAGNVLGGKLPPRLGLLTELQHMEIGYNHFNGNIPSEFALLSNLKYFDVSNCSLSGSLPQELGN LSNLETLFLFQNGFTGEIPESYSNLKSLKLLDFSSNQLSGSIPSGFSTLKNLTWLSLISNNLSGEVPEGIGELPELTTLF LWNNNFTGVLPHKLGSNGKLETMDVSNNSFTGTIPSSLCHGNKLYKLILFSNMFEGELPKSLTRCESLWRFRSQNNRLNG TIPIGFGSLRNLTFVDLSNNRFTDQIPADFATAPVLQYLNLSTNFFHRKLPENIWKAPNLQIFSASFSNLIGEIPNYVGC KSFYRIELQGNSLNGTIPWDIGHCEKLLCLNLSQNHLNGIIPWEISTLPSIADVDLSHNLLTGTIPSDFGSSKTITTFNV SYNQLIGPIPSGSFAHLNPSFFSSNEGLCGDLVGKPCN ; 32 2 PDB 5GQR 5GQR ? 2 ? 1 3 UNP SERK2_ARATH Q9XIC7 ? 3 ;NMEGDALHSLRANLVDPNNVLQSWDPTLVNPCTWFHVTCNNENSVIRVDLGNADLSGQLVPQLGQLKNLQYLELYSNNIT GPVPSDLGNLTNLVSLDLYLNSFTGPIPDSLGKLFKLRFLRLNNNSLTGPIPMSLTNIMTLQVLDLSNNRLSGSVPDNGS FSLFTPISFANNLDLCGPVTSRPCP ; 30 # 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 5GQR B 1 ? 598 ? Q9FII5 32 ? 629 ? 32 629 2 2 5GQR C 1 ? 12 ? 5GQR 93 ? 104 ? 93 104 3 3 5GQR K 1 ? 185 ? Q9XIC7 30 ? 214 ? 27 211 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HYP 'L-peptide linking' n 4-HYDROXYPROLINE HYDROXYPROLINE 'C5 H9 N O3' 131.130 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5GQR _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 4.11 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 70.06 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 291 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '0.1 M Potassium chloride, 20% w/v Polyethylene glycol 3350' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'DECTRIS PILATUS3 6M' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2015-05-15 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.979 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'SSRF BEAMLINE BL19U1' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.979 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BL19U1 _diffrn_source.pdbx_synchrotron_site SSRF # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5GQR _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 3.5 _reflns.d_resolution_low 50 _reflns.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.number_all ? _reflns.number_obs 18060 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 95.13 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 4.3 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value 0.144 _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 6.5 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high . _reflns_shell.d_res_low ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all ? _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5GQR _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 18033 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.00 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 40.472 _refine.ls_d_res_high 3.500 _refine.ls_percent_reflns_obs 95.05 _refine.ls_R_factor_obs 0.2219 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2190 _refine.ls_R_factor_R_free 0.2759 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.14 _refine.ls_number_reflns_R_free 926 _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 'FREE R-VALUE' _refine.details ? _refine.pdbx_starting_model 4MN8 _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 0.52 _refine.pdbx_overall_phase_error 27.31 _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_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 6104 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 56 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 6160 _refine_hist.d_res_high 3.500 _refine_hist.d_res_low 40.472 # 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 ? ? 6364 'X-RAY DIFFRACTION' ? f_angle_d 1.629 ? ? 8663 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 18.305 ? ? 2311 'X-RAY DIFFRACTION' ? f_chiral_restr 0.124 ? ? 996 'X-RAY DIFFRACTION' ? f_plane_restr 0.008 ? ? 1118 '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 'X-RAY DIFFRACTION' . 3.5002 3.6846 2400 0.3146 96.00 0.3886 . . 148 . . 'X-RAY DIFFRACTION' . 3.6846 3.9153 2440 0.2561 97.00 0.2933 . . 123 . . 'X-RAY DIFFRACTION' . 3.9153 4.2173 2430 0.2072 97.00 0.2425 . . 141 . . 'X-RAY DIFFRACTION' . 4.2173 4.6411 2430 0.1857 96.00 0.2628 . . 148 . . 'X-RAY DIFFRACTION' . 4.6411 5.3114 2428 0.1818 95.00 0.2222 . . 129 . . 'X-RAY DIFFRACTION' . 5.3114 6.6870 2467 0.2356 94.00 0.3390 . . 125 . . 'X-RAY DIFFRACTION' . 6.6870 40.4743 2512 0.2132 90.00 0.2520 . . 112 . . # _struct.entry_id 5GQR _struct.title 'Crystal structure of PXY-CLE41-SERK2' _struct.pdbx_descriptor 'Leucine-rich repeat receptor-like protein kinase TDR (E.C.2.7.11.1), TDIF, Somatic embryogenesis receptor kinase 2 (E.C.2.7.11.1)' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag N # _struct_keywords.entry_id 5GQR _struct_keywords.text 'Meristem cell proliferation, SERK, CLE peptides, leucine rich repeat, TRANSFERASE' _struct_keywords.pdbx_keywords TRANSFERASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 4 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 SER A 2 ? SER A 14 ? SER B 33 SER B 45 1 ? 13 HELX_P HELX_P2 AA2 ALA A 35 ? TRP A 40 ? ALA B 66 TRP B 71 5 ? 6 HELX_P HELX_P3 AA3 THR A 92 ? LEU A 97 ? THR B 123 LEU B 128 5 ? 6 HELX_P HELX_P4 AA4 PRO A 115 ? LEU A 121 ? PRO B 146 LEU B 152 5 ? 7 HELX_P HELX_P5 AA5 SER A 140 ? LEU A 145 ? SER B 171 LEU B 176 5 ? 6 HELX_P HELX_P6 AA6 PRO A 163 ? LEU A 169 ? PRO B 194 LEU B 200 5 ? 7 HELX_P HELX_P7 AA7 PRO A 187 ? LEU A 193 ? PRO B 218 LEU B 224 5 ? 7 HELX_P HELX_P8 AA8 PRO A 211 ? LEU A 217 ? PRO B 242 LEU B 248 5 ? 7 HELX_P HELX_P9 AA9 PRO A 235 ? LEU A 241 ? PRO B 266 LEU B 272 5 ? 7 HELX_P HELX_P10 AB1 PRO A 259 ? LEU A 265 ? PRO B 290 LEU B 296 5 ? 7 HELX_P HELX_P11 AB2 PRO A 283 ? LEU A 289 ? PRO B 314 LEU B 320 5 ? 7 HELX_P HELX_P12 AB3 PRO A 307 ? GLU A 312 ? PRO B 338 GLU B 343 5 ? 6 HELX_P HELX_P13 AB4 PRO A 379 ? CYS A 385 ? PRO B 410 CYS B 416 5 ? 7 HELX_P HELX_P14 AB5 GLY A 405 ? LEU A 409 ? GLY B 436 LEU B 440 5 ? 5 HELX_P HELX_P15 AB6 PRO A 427 ? THR A 432 ? PRO B 458 THR B 463 5 ? 6 HELX_P HELX_P16 AB7 PRO A 451 ? ALA A 457 ? PRO B 482 ALA B 488 5 ? 7 HELX_P HELX_P17 AB8 ASP A 500 ? CYS A 504 ? ASP B 531 CYS B 535 5 ? 5 HELX_P HELX_P18 AB9 PRO A 522 ? LEU A 528 ? PRO B 553 LEU B 559 5 ? 7 HELX_P HELX_P19 AC1 PRO A 546 ? SER A 552 ? PRO B 577 SER B 583 5 ? 7 HELX_P HELX_P20 AC2 GLY A 572 ? LEU A 577 ? GLY B 603 LEU B 608 5 ? 6 HELX_P HELX_P21 AC3 ASN A 578 ? PHE A 582 ? ASN B 609 PHE B 613 5 ? 5 HELX_P HELX_P22 AC4 MET C 2 ? ASN C 13 ? MET K 28 ASN K 39 1 ? 12 HELX_P HELX_P23 AC5 VAL C 20 ? TRP C 24 ? VAL K 46 TRP K 50 5 ? 5 HELX_P HELX_P24 AC6 ASN C 30 ? TRP C 34 ? ASN K 56 TRP K 60 5 ? 5 HELX_P HELX_P25 AC7 VAL C 60 ? LEU C 66 ? VAL K 86 LEU K 92 5 ? 7 HELX_P HELX_P26 AC8 PRO C 84 ? LEU C 90 ? PRO K 110 LEU K 116 5 ? 7 HELX_P HELX_P27 AC9 PRO C 108 ? LEU C 114 ? PRO K 134 LEU K 140 5 ? 7 HELX_P HELX_P28 AD1 PRO C 132 ? ILE C 138 ? PRO K 158 ILE K 164 5 ? 7 HELX_P HELX_P29 AD2 ASN C 158 ? PHE C 164 ? ASN K 184 PHE K 190 5 ? 7 HELX_P HELX_P30 AD3 THR C 165 ? PHE C 169 ? THR K 191 PHE K 195 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 38 SG ? ? ? 1_555 A CYS 45 SG ? ? B CYS 69 B CYS 76 1_555 ? ? ? ? ? ? ? 2.038 ? disulf2 disulf ? ? A CYS 359 SG ? ? ? 1_555 A CYS 385 SG ? ? B CYS 390 B CYS 416 1_555 ? ? ? ? ? ? ? 2.034 ? disulf3 disulf ? ? A CYS 480 SG ? ? ? 1_555 A CYS 504 SG ? ? B CYS 511 B CYS 535 1_555 ? ? ? ? ? ? ? 2.039 ? disulf4 disulf ? ? A CYS 589 SG ? ? ? 1_555 A CYS 597 SG ? ? B CYS 620 B CYS 628 1_555 ? ? ? ? ? ? ? 2.043 ? disulf5 disulf ? ? C CYS 32 SG ? ? ? 1_555 C CYS 39 SG ? ? K CYS 58 K CYS 65 1_555 ? ? ? ? ? ? ? 2.046 ? disulf6 disulf ? ? C CYS 176 SG ? ? ? 1_555 C CYS 184 SG ? ? K CYS 202 K CYS 210 1_555 ? ? ? ? ? ? ? 2.040 ? covale1 covale one ? A ASN 80 ND2 ? ? ? 1_555 E NAG . C1 ? ? B ASN 111 B NAG 702 1_555 ? ? ? ? ? ? ? 1.458 ? covale2 covale one ? A ASN 291 ND2 ? ? ? 1_555 D NAG . C1 ? ? B ASN 322 B NAG 701 1_555 ? ? ? ? ? ? ? 1.454 ? covale3 covale both ? B GLY 6 C ? ? ? 1_555 B HYP 7 N ? ? C GLY 98 C HYP 99 1_555 ? ? ? ? ? ? ? 1.321 ? covale4 covale both ? B HYP 7 C ? ? ? 1_555 B ASN 8 N ? ? C HYP 99 C ASN 100 1_555 ? ? ? ? ? ? ? 1.344 ? covale5 covale one ? C ASN 124 ND2 ? ? ? 1_555 G NAG . C1 ? ? K ASN 150 K NAG 302 1_555 ? ? ? ? ? ? ? 1.468 ? covale6 covale one ? C ASN 158 ND2 ? ? ? 1_555 F NAG . C1 ? ? K ASN 184 K NAG 301 1_555 ? ? ? ? ? ? ? 1.477 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 2 ? AA2 ? 23 ? AA3 ? 2 ? AA4 ? 2 ? AA5 ? 2 ? AA6 ? 2 ? AA7 ? 2 ? AA8 ? 2 ? AA9 ? 2 ? AB1 ? 2 ? AB2 ? 6 ? AB3 ? 2 ? AB4 ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA2 1 2 ? anti-parallel AA2 2 3 ? parallel AA2 3 4 ? parallel AA2 4 5 ? parallel AA2 5 6 ? parallel AA2 6 7 ? parallel AA2 7 8 ? parallel AA2 8 9 ? parallel AA2 9 10 ? parallel AA2 10 11 ? parallel AA2 11 12 ? parallel AA2 12 13 ? parallel AA2 13 14 ? parallel AA2 14 15 ? parallel AA2 15 16 ? parallel AA2 16 17 ? parallel AA2 17 18 ? parallel AA2 18 19 ? parallel AA2 19 20 ? parallel AA2 20 21 ? parallel AA2 21 22 ? parallel AA2 22 23 ? parallel AA3 1 2 ? parallel AA4 1 2 ? parallel AA5 1 2 ? parallel AA6 1 2 ? parallel AA7 1 2 ? parallel AA8 1 2 ? parallel AA9 1 2 ? parallel AB1 1 2 ? anti-parallel AB2 1 2 ? anti-parallel AB2 2 3 ? parallel AB2 3 4 ? parallel AB2 4 5 ? parallel AB2 5 6 ? parallel AB3 1 2 ? parallel AB4 1 2 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 LEU A 15 ? SER A 16 ? LEU B 46 SER B 47 AA1 2 SER A 63 ? GLY A 64 ? SER B 94 GLY B 95 AA2 1 VAL A 43 ? CYS A 45 ? VAL B 74 CYS B 76 AA2 2 VAL A 52 ? ASP A 56 ? VAL B 83 ASP B 87 AA2 3 TYR A 78 ? ASN A 80 ? TYR B 109 ASN B 111 AA2 4 THR A 102 ? ASP A 104 ? THR B 133 ASP B 135 AA2 5 VAL A 126 ? ASN A 128 ? VAL B 157 ASN B 159 AA2 6 GLU A 150 ? ASN A 152 ? GLU B 181 ASN B 183 AA2 7 PHE A 174 ? HIS A 176 ? PHE B 205 HIS B 207 AA2 8 HIS A 198 ? GLU A 200 ? HIS B 229 GLU B 231 AA2 9 TYR A 222 ? ASP A 224 ? TYR B 253 ASP B 255 AA2 10 THR A 246 ? PHE A 248 ? THR B 277 PHE B 279 AA2 11 LEU A 270 ? ASP A 272 ? LEU B 301 ASP B 303 AA2 12 TRP A 294 ? SER A 296 ? TRP B 325 SER B 327 AA2 13 THR A 318 ? PHE A 320 ? THR B 349 PHE B 351 AA2 14 THR A 342 ? ASP A 344 ? THR B 373 ASP B 375 AA2 15 LYS A 366 ? ILE A 368 ? LYS B 397 ILE B 399 AA2 16 ARG A 390 ? ARG A 392 ? ARG B 421 ARG B 423 AA2 17 PHE A 414 ? ASP A 416 ? PHE B 445 ASP B 447 AA2 18 TYR A 438 ? ASN A 440 ? TYR B 469 ASN B 471 AA2 19 ILE A 462 ? SER A 464 ? ILE B 493 SER B 495 AA2 20 ARG A 485 ? GLU A 487 ? ARG B 516 GLU B 518 AA2 21 CYS A 509 ? ASN A 511 ? CYS B 540 ASN B 542 AA2 22 ASP A 533 ? ASP A 535 ? ASP B 564 ASP B 566 AA2 23 THR A 557 ? ASN A 559 ? THR B 588 ASN B 590 AA3 1 ASP A 111 ? SER A 112 ? ASP B 142 SER B 143 AA3 2 ASN A 133 ? PHE A 134 ? ASN B 164 PHE B 165 AA4 1 GLY A 183 ? GLY A 184 ? GLY B 214 GLY B 215 AA4 2 HIS A 205 ? PHE A 206 ? HIS B 236 PHE B 237 AA5 1 SER A 231 ? SER A 233 ? SER B 262 SER B 264 AA5 2 GLY A 253 ? THR A 255 ? GLY B 284 THR B 286 AA6 1 THR A 351 ? GLY A 352 ? THR B 382 GLY B 383 AA6 2 MET A 373 ? PHE A 374 ? MET B 404 PHE B 405 AA7 1 ASN A 399 ? GLY A 400 ? ASN B 430 GLY B 431 AA7 2 ARG A 421 ? PHE A 422 ? ARG B 452 PHE B 453 AA8 1 ASN A 494 ? GLY A 495 ? ASN B 525 GLY B 526 AA8 2 HIS A 516 ? LEU A 517 ? HIS B 547 LEU B 548 AA9 1 ILE A 566 ? PRO A 568 ? ILE B 597 PRO B 599 AA9 2 GLY A 587 ? CYS A 589 ? GLY B 618 CYS B 620 AB1 1 LEU C 14 ? VAL C 15 ? LEU K 40 VAL K 41 AB1 2 SER C 56 ? GLY C 57 ? SER K 82 GLY K 83 AB2 1 VAL C 37 ? CYS C 39 ? VAL K 63 CYS K 65 AB2 2 VAL C 45 ? ASP C 49 ? VAL K 71 ASP K 75 AB2 3 TYR C 71 ? GLU C 73 ? TYR K 97 GLU K 99 AB2 4 SER C 95 ? ASP C 97 ? SER K 121 ASP K 123 AB2 5 PHE C 119 ? ARG C 121 ? PHE K 145 ARG K 147 AB2 6 VAL C 143 ? ASP C 145 ? VAL K 169 ASP K 171 AB3 1 THR C 80 ? GLY C 81 ? THR K 106 GLY K 107 AB3 2 SER C 102 ? PHE C 103 ? SER K 128 PHE K 129 AB4 1 GLY C 153 ? SER C 154 ? GLY K 179 SER K 180 AB4 2 LEU C 175 ? CYS C 176 ? LEU K 201 CYS K 202 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 N SER A 16 ? N SER B 47 O SER A 63 ? O SER B 94 AA2 1 2 N VAL A 44 ? N VAL B 75 O SER A 54 ? O SER B 85 AA2 2 3 N LEU A 55 ? N LEU B 86 O ASN A 80 ? O ASN B 111 AA2 3 4 N LEU A 79 ? N LEU B 110 O ASP A 104 ? O ASP B 135 AA2 4 5 N LEU A 103 ? N LEU B 134 O ASN A 128 ? O ASN B 159 AA2 5 6 N PHE A 127 ? N PHE B 158 O GLU A 150 ? O GLU B 181 AA2 6 7 N LEU A 151 ? N LEU B 182 O HIS A 176 ? O HIS B 207 AA2 7 8 N ILE A 175 ? N ILE B 206 O HIS A 198 ? O HIS B 229 AA2 8 9 N MET A 199 ? N MET B 230 O TYR A 222 ? O TYR B 253 AA2 9 10 N PHE A 223 ? N PHE B 254 O PHE A 248 ? O PHE B 279 AA2 10 11 N LEU A 247 ? N LEU B 278 O ASP A 272 ? O ASP B 303 AA2 11 12 N LEU A 271 ? N LEU B 302 O SER A 296 ? O SER B 327 AA2 12 13 N LEU A 295 ? N LEU B 326 O THR A 318 ? O THR B 349 AA2 13 14 N LEU A 319 ? N LEU B 350 O THR A 342 ? O THR B 373 AA2 14 15 N MET A 343 ? N MET B 374 O ILE A 368 ? O ILE B 399 AA2 15 16 N LEU A 367 ? N LEU B 398 O ARG A 390 ? O ARG B 421 AA2 16 17 N PHE A 391 ? N PHE B 422 O PHE A 414 ? O PHE B 445 AA2 17 18 N VAL A 415 ? N VAL B 446 O TYR A 438 ? O TYR B 469 AA2 18 19 N LEU A 439 ? N LEU B 470 O SER A 464 ? O SER B 495 AA2 19 20 N PHE A 463 ? N PHE B 494 O ARG A 485 ? O ARG B 516 AA2 20 21 N ILE A 486 ? N ILE B 517 O CYS A 509 ? O CYS B 540 AA2 21 22 N LEU A 510 ? N LEU B 541 O ASP A 533 ? O ASP B 564 AA2 22 23 N VAL A 534 ? N VAL B 565 O ASN A 559 ? O ASN B 590 AA3 1 2 N SER A 112 ? N SER B 143 O ASN A 133 ? O ASN B 164 AA4 1 2 N GLY A 184 ? N GLY B 215 O HIS A 205 ? O HIS B 236 AA5 1 2 N GLY A 232 ? N GLY B 263 O THR A 255 ? O THR B 286 AA6 1 2 N GLY A 352 ? N GLY B 383 O MET A 373 ? O MET B 404 AA7 1 2 N GLY A 400 ? N GLY B 431 O ARG A 421 ? O ARG B 452 AA8 1 2 N GLY A 495 ? N GLY B 526 O HIS A 516 ? O HIS B 547 AA9 1 2 N GLY A 567 ? N GLY B 598 O GLY A 587 ? O GLY B 618 AB1 1 2 N VAL C 15 ? N VAL K 41 O SER C 56 ? O SER K 82 AB2 1 2 N THR C 38 ? N THR K 64 O ILE C 46 ? O ILE K 72 AB2 2 3 O ILE C 46 ? O ILE K 72 N TYR C 71 ? N TYR K 97 AB2 3 4 N LEU C 72 ? N LEU K 98 O SER C 95 ? O SER K 121 AB2 4 5 N LEU C 96 ? N LEU K 122 O PHE C 119 ? O PHE K 145 AB2 5 6 N LEU C 120 ? N LEU K 146 O ASP C 145 ? O ASP K 171 AB3 1 2 N GLY C 81 ? N GLY K 107 O SER C 102 ? O SER K 128 AB4 1 2 N GLY C 153 ? N GLY K 179 O CYS C 176 ? O CYS K 202 # 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 B NAG 702 ? 6 'binding site for Mono-Saccharide NAG B 702 bound to ASN B 111' AC2 Software B NAG 701 ? 3 'binding site for Mono-Saccharide NAG B 701 bound to ASN B 322' AC3 Software K NAG 302 ? 2 'binding site for Mono-Saccharide NAG K 302 bound to ASN K 150' AC4 Software K NAG 301 ? 3 'binding site for Mono-Saccharide NAG K 301 bound to ASN K 184' # 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 6 ASP A 56 ? ASP B 87 . ? 1_555 ? 2 AC1 6 SER A 58 ? SER B 89 . ? 1_555 ? 3 AC1 6 HIS A 59 ? HIS B 90 . ? 1_555 ? 4 AC1 6 TYR A 78 ? TYR B 109 . ? 1_555 ? 5 AC1 6 ASN A 80 ? ASN B 111 . ? 1_555 ? 6 AC1 6 ASP A 104 ? ASP B 135 . ? 1_555 ? 7 AC2 3 LYS A 266 ? LYS B 297 . ? 1_555 ? 8 AC2 3 LYS A 269 ? LYS B 300 . ? 1_555 ? 9 AC2 3 ASN A 291 ? ASN B 322 . ? 1_555 ? 10 AC3 2 ASN C 124 ? ASN K 150 . ? 1_555 ? 11 AC3 2 ASN C 148 ? ASN K 174 . ? 1_555 ? 12 AC4 3 THR C 136 ? THR K 162 . ? 1_555 ? 13 AC4 3 ASN C 137 ? ASN K 163 . ? 1_555 ? 14 AC4 3 ASN C 158 ? ASN K 184 . ? 1_555 ? # _atom_sites.entry_id 5GQR _atom_sites.fract_transf_matrix[1][1] 0.006157 _atom_sites.fract_transf_matrix[1][2] 0.003555 _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] 0.007109 _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] 0.005341 _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 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 ? 113.689 -26.397 32.738 1.00 124.95 ? 32 PHE B N 1 ATOM 2 C CA . PHE A 1 1 ? 113.150 -25.238 32.043 1.00 119.54 ? 32 PHE B CA 1 ATOM 3 C C . PHE A 1 1 ? 112.038 -24.601 32.871 1.00 118.33 ? 32 PHE B C 1 ATOM 4 O O . PHE A 1 1 ? 111.721 -25.070 33.960 1.00 121.11 ? 32 PHE B O 1 ATOM 5 C CB . PHE A 1 1 ? 112.635 -25.625 30.650 1.00 119.72 ? 32 PHE B CB 1 ATOM 6 C CG . PHE A 1 1 ? 113.727 -25.811 29.608 1.00 125.25 ? 32 PHE B CG 1 ATOM 7 C CD1 . PHE A 1 1 ? 114.951 -25.163 29.725 1.00 129.32 ? 32 PHE B CD1 1 ATOM 8 C CD2 . PHE A 1 1 ? 113.516 -26.630 28.502 1.00 125.48 ? 32 PHE B CD2 1 ATOM 9 C CE1 . PHE A 1 1 ? 115.942 -25.336 28.762 1.00 130.06 ? 32 PHE B CE1 1 ATOM 10 C CE2 . PHE A 1 1 ? 114.503 -26.802 27.540 1.00 126.68 ? 32 PHE B CE2 1 ATOM 11 C CZ . PHE A 1 1 ? 115.715 -26.155 27.672 1.00 129.41 ? 32 PHE B CZ 1 ATOM 12 N N . SER A 1 2 ? 111.446 -23.541 32.329 1.00 81.41 ? 33 SER B N 1 ATOM 13 C CA . SER A 1 2 ? 110.505 -22.683 33.047 1.00 80.05 ? 33 SER B CA 1 ATOM 14 C C . SER A 1 2 ? 109.254 -23.431 33.472 1.00 79.56 ? 33 SER B C 1 ATOM 15 O O . SER A 1 2 ? 108.806 -24.310 32.742 1.00 80.02 ? 33 SER B O 1 ATOM 16 C CB . SER A 1 2 ? 110.101 -21.510 32.143 1.00 82.13 ? 33 SER B CB 1 ATOM 17 O OG . SER A 1 2 ? 109.644 -20.376 32.874 1.00 79.88 ? 33 SER B OG 1 ATOM 18 N N . PRO A 1 3 ? 108.665 -23.055 34.637 1.00 73.10 ? 34 PRO B N 1 ATOM 19 C CA . PRO A 1 3 ? 107.428 -23.665 35.164 1.00 70.48 ? 34 PRO B CA 1 ATOM 20 C C . PRO A 1 3 ? 106.277 -23.481 34.192 1.00 73.56 ? 34 PRO B C 1 ATOM 21 O O . PRO A 1 3 ? 105.362 -24.280 34.167 1.00 75.40 ? 34 PRO B O 1 ATOM 22 C CB . PRO A 1 3 ? 107.121 -22.843 36.420 1.00 71.11 ? 34 PRO B CB 1 ATOM 23 C CG . PRO A 1 3 ? 108.322 -22.014 36.694 1.00 71.55 ? 34 PRO B CG 1 ATOM 24 C CD . PRO A 1 3 ? 109.072 -21.871 35.422 1.00 72.21 ? 34 PRO B CD 1 ATOM 25 N N . GLN A 1 4 ? 106.324 -22.399 33.426 1.00 73.64 ? 35 GLN B N 1 ATOM 26 C CA . GLN A 1 4 ? 105.403 -22.187 32.331 1.00 74.74 ? 35 GLN B CA 1 ATOM 27 C C . GLN A 1 4 ? 105.483 -23.381 31.416 1.00 72.62 ? 35 GLN B C 1 ATOM 28 O O . GLN A 1 4 ? 104.458 -23.902 31.000 1.00 73.03 ? 35 GLN B O 1 ATOM 29 C CB . GLN A 1 4 ? 105.794 -20.940 31.535 1.00 77.74 ? 35 GLN B CB 1 ATOM 30 C CG . GLN A 1 4 ? 105.839 -19.652 32.335 1.00 74.50 ? 35 GLN B CG 1 ATOM 31 C CD . GLN A 1 4 ? 104.542 -19.386 33.081 1.00 73.53 ? 35 GLN B CD 1 ATOM 32 O OE1 . GLN A 1 4 ? 103.495 -19.111 32.479 1.00 79.24 ? 35 GLN B OE1 1 ATOM 33 N NE2 . GLN A 1 4 ? 104.605 -19.470 34.405 1.00 70.18 ? 35 GLN B NE2 1 ATOM 34 N N . LEU A 1 5 ? 106.710 -23.810 31.113 1.00 80.09 ? 36 LEU B N 1 ATOM 35 C CA . LEU A 1 5 ? 106.949 -24.906 30.170 1.00 82.75 ? 36 LEU B CA 1 ATOM 36 C C . LEU A 1 5 ? 106.563 -26.274 30.740 1.00 82.06 ? 36 LEU B C 1 ATOM 37 O O . LEU A 1 5 ? 105.991 -27.106 30.031 1.00 84.78 ? 36 LEU B O 1 ATOM 38 C CB . LEU A 1 5 ? 108.416 -24.916 29.712 1.00 82.98 ? 36 LEU B CB 1 ATOM 39 C CG . LEU A 1 5 ? 108.724 -25.126 28.216 1.00 84.69 ? 36 LEU B CG 1 ATOM 40 C CD1 . LEU A 1 5 ? 110.230 -25.169 27.948 1.00 89.03 ? 36 LEU B CD1 1 ATOM 41 C CD2 . LEU A 1 5 ? 108.052 -26.357 27.649 1.00 86.68 ? 36 LEU B CD2 1 ATOM 42 N N . LEU A 1 6 ? 106.889 -26.501 32.014 1.00 95.94 ? 37 LEU B N 1 ATOM 43 C CA . LEU A 1 6 ? 106.513 -27.731 32.703 1.00 97.28 ? 37 LEU B CA 1 ATOM 44 C C . LEU A 1 6 ? 105.006 -27.803 32.708 1.00 96.96 ? 37 LEU B C 1 ATOM 45 O O . LEU A 1 6 ? 104.422 -28.862 32.546 1.00 97.84 ? 37 LEU B O 1 ATOM 46 C CB . LEU A 1 6 ? 107.007 -27.730 34.150 1.00 97.62 ? 37 LEU B CB 1 ATOM 47 C CG . LEU A 1 6 ? 108.456 -27.329 34.438 1.00 97.71 ? 37 LEU B CG 1 ATOM 48 C CD1 . LEU A 1 6 ? 108.716 -27.375 35.944 1.00 97.13 ? 37 LEU B CD1 1 ATOM 49 C CD2 . LEU A 1 6 ? 109.476 -28.183 33.660 1.00 96.62 ? 37 LEU B CD2 1 ATOM 50 N N . SER A 1 7 ? 104.392 -26.641 32.883 1.00 67.51 ? 38 SER B N 1 ATOM 51 C CA . SER A 1 7 ? 102.945 -26.494 32.952 1.00 67.22 ? 38 SER B CA 1 ATOM 52 C C . SER A 1 7 ? 102.247 -26.812 31.634 1.00 67.28 ? 38 SER B C 1 ATOM 53 O O . SER A 1 7 ? 101.341 -27.636 31.585 1.00 67.90 ? 38 SER B O 1 ATOM 54 C CB . SER A 1 7 ? 102.592 -25.069 33.372 1.00 68.36 ? 38 SER B CB 1 ATOM 55 O OG . SER A 1 7 ? 101.344 -25.034 34.040 1.00 72.76 ? 38 SER B OG 1 ATOM 56 N N . LEU A 1 8 ? 102.668 -26.135 30.573 1.00 72.77 ? 39 LEU B N 1 ATOM 57 C CA . LEU A 1 8 ? 102.093 -26.334 29.248 1.00 74.94 ? 39 LEU B CA 1 ATOM 58 C C . LEU A 1 8 ? 102.324 -27.747 28.759 1.00 74.38 ? 39 LEU B C 1 ATOM 59 O O . LEU A 1 8 ? 101.446 -28.342 28.140 1.00 70.22 ? 39 LEU B O 1 ATOM 60 C CB . LEU A 1 8 ? 102.704 -25.357 28.254 1.00 75.38 ? 39 LEU B CB 1 ATOM 61 C CG . LEU A 1 8 ? 102.230 -23.929 28.434 1.00 75.01 ? 39 LEU B CG 1 ATOM 62 C CD1 . LEU A 1 8 ? 103.200 -23.022 27.762 1.00 78.05 ? 39 LEU B CD1 1 ATOM 63 C CD2 . LEU A 1 8 ? 100.854 -23.783 27.831 1.00 72.37 ? 39 LEU B CD2 1 ATOM 64 N N . LEU A 1 9 ? 103.518 -28.271 29.031 1.00 80.85 ? 40 LEU B N 1 ATOM 65 C CA . LEU A 1 9 ? 103.861 -29.623 28.620 1.00 81.88 ? 40 LEU B CA 1 ATOM 66 C C . LEU A 1 9 ? 102.994 -30.634 29.348 1.00 81.07 ? 40 LEU B C 1 ATOM 67 O O . LEU A 1 9 ? 102.433 -31.539 28.729 1.00 82.45 ? 40 LEU B O 1 ATOM 68 C CB . LEU A 1 9 ? 105.339 -29.905 28.866 1.00 80.35 ? 40 LEU B CB 1 ATOM 69 C CG . LEU A 1 9 ? 106.251 -29.419 27.742 1.00 84.08 ? 40 LEU B CG 1 ATOM 70 C CD1 . LEU A 1 9 ? 107.705 -29.763 28.029 1.00 81.54 ? 40 LEU B CD1 1 ATOM 71 C CD2 . LEU A 1 9 ? 105.800 -30.024 26.421 1.00 85.33 ? 40 LEU B CD2 1 ATOM 72 N N . SER A 1 10 ? 102.871 -30.458 30.662 1.00 67.55 ? 41 SER B N 1 ATOM 73 C CA . SER A 1 10 ? 102.053 -31.333 31.507 1.00 67.62 ? 41 SER B CA 1 ATOM 74 C C . SER A 1 10 ? 100.582 -31.267 31.126 1.00 69.86 ? 41 SER B C 1 ATOM 75 O O . SER A 1 10 ? 99.832 -32.244 31.249 1.00 72.15 ? 41 SER B O 1 ATOM 76 C CB . SER A 1 10 ? 102.206 -30.916 32.955 1.00 67.38 ? 41 SER B CB 1 ATOM 77 O OG . SER A 1 10 ? 102.296 -29.508 33.020 1.00 68.23 ? 41 SER B OG 1 ATOM 78 N N . LEU A 1 11 ? 100.178 -30.099 30.658 1.00 59.73 ? 42 LEU B N 1 ATOM 79 C CA . LEU A 1 11 ? 98.827 -29.894 30.179 1.00 58.81 ? 42 LEU B CA 1 ATOM 80 C C . LEU A 1 11 ? 98.602 -30.610 28.856 1.00 59.43 ? 42 LEU B C 1 ATOM 81 O O . LEU A 1 11 ? 97.527 -31.182 28.625 1.00 58.79 ? 42 LEU B O 1 ATOM 82 C CB . LEU A 1 11 ? 98.581 -28.402 30.016 1.00 58.47 ? 42 LEU B CB 1 ATOM 83 C CG . LEU A 1 11 ? 97.497 -27.818 30.912 1.00 57.16 ? 42 LEU B CG 1 ATOM 84 C CD1 . LEU A 1 11 ? 97.592 -26.309 30.898 1.00 57.11 ? 42 LEU B CD1 1 ATOM 85 C CD2 . LEU A 1 11 ? 96.134 -28.297 30.434 1.00 56.47 ? 42 LEU B CD2 1 ATOM 86 N N . LYS A 1 12 ? 99.631 -30.558 28.002 1.00 63.72 ? 43 LYS B N 1 ATOM 87 C CA . LYS A 1 12 ? 99.662 -31.236 26.701 1.00 65.37 ? 43 LYS B CA 1 ATOM 88 C C . LYS A 1 12 ? 99.434 -32.709 26.875 1.00 64.78 ? 43 LYS B C 1 ATOM 89 O O . LYS A 1 12 ? 98.544 -33.284 26.249 1.00 65.63 ? 43 LYS B O 1 ATOM 90 C CB . LYS A 1 12 ? 101.026 -31.045 26.021 1.00 65.82 ? 43 LYS B CB 1 ATOM 91 C CG . LYS A 1 12 ? 101.278 -31.902 24.769 1.00 66.73 ? 43 LYS B CG 1 ATOM 92 C CD . LYS A 1 12 ? 102.769 -31.914 24.389 1.00 70.16 ? 43 LYS B CD 1 ATOM 93 C CE . LYS A 1 12 ? 103.006 -32.418 22.964 1.00 73.07 ? 43 LYS B CE 1 ATOM 94 N NZ . LYS A 1 12 ? 102.337 -33.732 22.708 1.00 72.87 ? 43 LYS B NZ 1 ATOM 95 N N . THR A 1 13 ? 100.254 -33.308 27.735 1.00 66.54 ? 44 THR B N 1 ATOM 96 C CA . THR A 1 13 ? 100.265 -34.757 27.903 1.00 69.08 ? 44 THR B CA 1 ATOM 97 C C . THR A 1 13 ? 99.129 -35.305 28.767 1.00 69.76 ? 44 THR B C 1 ATOM 98 O O . THR A 1 13 ? 98.711 -36.448 28.586 1.00 71.00 ? 44 THR B O 1 ATOM 99 C CB . THR A 1 13 ? 101.601 -35.243 28.489 1.00 71.47 ? 44 THR B CB 1 ATOM 100 O OG1 . THR A 1 13 ? 101.527 -35.225 29.914 1.00 69.00 ? 44 THR B OG1 1 ATOM 101 C CG2 . THR A 1 13 ? 102.767 -34.361 28.027 1.00 72.62 ? 44 THR B CG2 1 ATOM 102 N N . SER A 1 14 ? 98.642 -34.503 29.713 1.00 75.60 ? 45 SER B N 1 ATOM 103 C CA . SER A 1 14 ? 97.565 -34.959 30.590 1.00 73.72 ? 45 SER B CA 1 ATOM 104 C C . SER A 1 14 ? 96.201 -34.979 29.903 1.00 72.95 ? 45 SER B C 1 ATOM 105 O O . SER A 1 14 ? 95.265 -35.645 30.354 1.00 71.89 ? 45 SER B O 1 ATOM 106 C CB . SER A 1 14 ? 97.477 -34.088 31.827 1.00 74.24 ? 45 SER B CB 1 ATOM 107 O OG . SER A 1 14 ? 96.135 -33.691 32.033 1.00 74.47 ? 45 SER B OG 1 ATOM 108 N N . LEU A 1 15 ? 96.083 -34.230 28.818 1.00 80.63 ? 46 LEU B N 1 ATOM 109 C CA . LEU A 1 15 ? 94.847 -34.198 28.061 1.00 82.31 ? 46 LEU B CA 1 ATOM 110 C C . LEU A 1 15 ? 94.913 -35.136 26.874 1.00 82.64 ? 46 LEU B C 1 ATOM 111 O O . LEU A 1 15 ? 95.673 -34.932 25.917 1.00 82.79 ? 46 LEU B O 1 ATOM 112 C CB . LEU A 1 15 ? 94.577 -32.783 27.604 1.00 82.75 ? 46 LEU B CB 1 ATOM 113 C CG . LEU A 1 15 ? 93.807 -32.075 28.693 1.00 80.81 ? 46 LEU B CG 1 ATOM 114 C CD1 . LEU A 1 15 ? 93.948 -30.572 28.569 1.00 79.15 ? 46 LEU B CD1 1 ATOM 115 C CD2 . LEU A 1 15 ? 92.375 -32.532 28.541 1.00 82.44 ? 46 LEU B CD2 1 ATOM 116 N N . SER A 1 16 ? 94.113 -36.183 26.932 1.00 92.84 ? 47 SER B N 1 ATOM 117 C CA . SER A 1 16 ? 94.127 -37.121 25.838 1.00 91.78 ? 47 SER B CA 1 ATOM 118 C C . SER A 1 16 ? 93.310 -36.516 24.711 1.00 92.56 ? 47 SER B C 1 ATOM 119 O O . SER A 1 16 ? 92.118 -36.251 24.866 1.00 94.17 ? 47 SER B O 1 ATOM 120 C CB . SER A 1 16 ? 93.555 -38.471 26.278 1.00 90.76 ? 47 SER B CB 1 ATOM 121 O OG . SER A 1 16 ? 94.334 -39.037 27.320 1.00 94.61 ? 47 SER B OG 1 ATOM 122 N N . GLY A 1 17 ? 93.961 -36.284 23.578 1.00 88.05 ? 48 GLY B N 1 ATOM 123 C CA . GLY A 1 17 ? 93.263 -35.822 22.394 1.00 88.36 ? 48 GLY B CA 1 ATOM 124 C C . GLY A 1 17 ? 93.980 -36.258 21.134 1.00 91.10 ? 48 GLY B C 1 ATOM 125 O O . GLY A 1 17 ? 95.146 -36.638 21.197 1.00 93.58 ? 48 GLY B O 1 ATOM 126 N N . PRO A 1 18 ? 93.283 -36.219 19.987 1.00 89.49 ? 49 PRO B N 1 ATOM 127 C CA . PRO A 1 18 ? 93.913 -36.430 18.684 1.00 90.50 ? 49 PRO B CA 1 ATOM 128 C C . PRO A 1 18 ? 95.159 -35.552 18.521 1.00 92.86 ? 49 PRO B C 1 ATOM 129 O O . PRO A 1 18 ? 95.083 -34.348 18.772 1.00 93.89 ? 49 PRO B O 1 ATOM 130 C CB . PRO A 1 18 ? 92.826 -35.969 17.716 1.00 90.52 ? 49 PRO B CB 1 ATOM 131 C CG . PRO A 1 18 ? 91.555 -36.306 18.416 1.00 88.68 ? 49 PRO B CG 1 ATOM 132 C CD . PRO A 1 18 ? 91.817 -36.127 19.882 1.00 87.74 ? 49 PRO B CD 1 ATOM 133 N N . PRO A 1 19 ? 96.289 -36.143 18.089 1.00 129.98 ? 50 PRO B N 1 ATOM 134 C CA . PRO A 1 19 ? 97.604 -35.483 18.012 1.00 131.08 ? 50 PRO B CA 1 ATOM 135 C C . PRO A 1 19 ? 97.595 -34.215 17.165 1.00 130.82 ? 50 PRO B C 1 ATOM 136 O O . PRO A 1 19 ? 98.494 -33.375 17.283 1.00 132.94 ? 50 PRO B O 1 ATOM 137 C CB . PRO A 1 19 ? 98.483 -36.546 17.355 1.00 130.53 ? 50 PRO B CB 1 ATOM 138 C CG . PRO A 1 19 ? 97.849 -37.831 17.750 1.00 130.75 ? 50 PRO B CG 1 ATOM 139 C CD . PRO A 1 19 ? 96.375 -37.568 17.730 1.00 129.76 ? 50 PRO B CD 1 ATOM 140 N N . SER A 1 20 ? 96.584 -34.097 16.314 1.00 98.23 ? 51 SER B N 1 ATOM 141 C CA . SER A 1 20 ? 96.339 -32.880 15.563 1.00 101.21 ? 51 SER B CA 1 ATOM 142 C C . SER A 1 20 ? 96.232 -31.686 16.507 1.00 100.85 ? 51 SER B C 1 ATOM 143 O O . SER A 1 20 ? 96.671 -30.585 16.167 1.00 98.81 ? 51 SER B O 1 ATOM 144 C CB . SER A 1 20 ? 95.060 -33.030 14.732 1.00 100.05 ? 51 SER B CB 1 ATOM 145 O OG . SER A 1 20 ? 94.092 -33.812 15.415 1.00 96.26 ? 51 SER B OG 1 ATOM 146 N N . ALA A 1 21 ? 95.671 -31.925 17.696 1.00 95.11 ? 52 ALA B N 1 ATOM 147 C CA . ALA A 1 21 ? 95.424 -30.885 18.698 1.00 92.22 ? 52 ALA B CA 1 ATOM 148 C C . ALA A 1 21 ? 96.685 -30.206 19.240 1.00 94.12 ? 52 ALA B C 1 ATOM 149 O O . ALA A 1 21 ? 96.760 -28.981 19.283 1.00 94.26 ? 52 ALA B O 1 ATOM 150 C CB . ALA A 1 21 ? 94.599 -31.438 19.841 1.00 88.98 ? 52 ALA B CB 1 ATOM 151 N N . PHE A 1 22 ? 97.658 -30.993 19.681 1.00 87.15 ? 53 PHE B N 1 ATOM 152 C CA . PHE A 1 22 ? 98.895 -30.449 20.254 1.00 85.74 ? 53 PHE B CA 1 ATOM 153 C C . PHE A 1 22 ? 100.109 -30.324 19.317 1.00 89.85 ? 53 PHE B C 1 ATOM 154 O O . PHE A 1 22 ? 101.234 -30.086 19.758 1.00 91.09 ? 53 PHE B O 1 ATOM 155 C CB . PHE A 1 22 ? 99.228 -31.129 21.573 1.00 82.41 ? 53 PHE B CB 1 ATOM 156 C CG . PHE A 1 22 ? 98.285 -30.753 22.699 1.00 76.20 ? 53 PHE B CG 1 ATOM 157 C CD1 . PHE A 1 22 ? 97.075 -31.422 22.870 1.00 71.44 ? 53 PHE B CD1 1 ATOM 158 C CD2 . PHE A 1 22 ? 98.604 -29.730 23.581 1.00 73.48 ? 53 PHE B CD2 1 ATOM 159 C CE1 . PHE A 1 22 ? 96.211 -31.087 23.900 1.00 69.35 ? 53 PHE B CE1 1 ATOM 160 C CE2 . PHE A 1 22 ? 97.739 -29.389 24.607 1.00 72.10 ? 53 PHE B CE2 1 ATOM 161 C CZ . PHE A 1 22 ? 96.545 -30.074 24.767 1.00 71.35 ? 53 PHE B CZ 1 ATOM 162 N N . GLN A 1 23 ? 99.852 -30.490 18.028 1.00 94.85 ? 54 GLN B N 1 ATOM 163 C CA . GLN A 1 23 ? 100.866 -30.709 17.013 1.00 97.76 ? 54 GLN B CA 1 ATOM 164 C C . GLN A 1 23 ? 102.097 -29.807 17.093 1.00 98.92 ? 54 GLN B C 1 ATOM 165 O O . GLN A 1 23 ? 103.196 -30.239 16.766 1.00 103.94 ? 54 GLN B O 1 ATOM 166 C CB . GLN A 1 23 ? 100.214 -30.531 15.641 1.00 101.93 ? 54 GLN B CB 1 ATOM 167 C CG . GLN A 1 23 ? 100.951 -31.192 14.494 1.00 107.25 ? 54 GLN B CG 1 ATOM 168 C CD . GLN A 1 23 ? 100.635 -32.673 14.373 1.00 109.62 ? 54 GLN B CD 1 ATOM 169 O OE1 . GLN A 1 23 ? 101.426 -33.526 14.781 1.00 112.16 ? 54 GLN B OE1 1 ATOM 170 N NE2 . GLN A 1 23 ? 99.477 -32.984 13.800 1.00 107.98 ? 54 GLN B NE2 1 ATOM 171 N N . ASP A 1 24 ? 101.935 -28.561 17.510 1.00 95.76 ? 55 ASP B N 1 ATOM 172 C CA . ASP A 1 24 ? 103.081 -27.649 17.486 1.00 97.80 ? 55 ASP B CA 1 ATOM 173 C C . ASP A 1 24 ? 103.871 -27.449 18.780 1.00 90.88 ? 55 ASP B C 1 ATOM 174 O O . ASP A 1 24 ? 104.745 -26.581 18.847 1.00 92.75 ? 55 ASP B O 1 ATOM 175 C CB . ASP A 1 24 ? 102.719 -26.303 16.865 1.00 98.04 ? 55 ASP B CB 1 ATOM 176 C CG . ASP A 1 24 ? 101.510 -25.687 17.489 1.00 96.79 ? 55 ASP B CG 1 ATOM 177 O OD1 . ASP A 1 24 ? 100.522 -26.424 17.708 1.00 95.43 ? 55 ASP B OD1 1 ATOM 178 O OD2 . ASP A 1 24 ? 101.561 -24.465 17.752 1.00 96.50 ? 55 ASP B OD2 1 ATOM 179 N N . TRP A 1 25 ? 103.563 -28.225 19.807 1.00 112.49 ? 56 TRP B N 1 ATOM 180 C CA . TRP A 1 25 ? 104.057 -27.898 21.138 1.00 110.89 ? 56 TRP B CA 1 ATOM 181 C C . TRP A 1 25 ? 105.415 -28.456 21.539 1.00 111.88 ? 56 TRP B C 1 ATOM 182 O O . TRP A 1 25 ? 105.785 -28.347 22.696 1.00 112.81 ? 56 TRP B O 1 ATOM 183 C CB . TRP A 1 25 ? 103.043 -28.288 22.207 1.00 107.79 ? 56 TRP B CB 1 ATOM 184 C CG . TRP A 1 25 ? 101.799 -27.492 22.176 1.00 107.15 ? 56 TRP B CG 1 ATOM 185 C CD1 . TRP A 1 25 ? 101.173 -26.999 21.079 1.00 106.57 ? 56 TRP B CD1 1 ATOM 186 C CD2 . TRP A 1 25 ? 101.017 -27.089 23.301 1.00 104.79 ? 56 TRP B CD2 1 ATOM 187 N NE1 . TRP A 1 25 ? 100.042 -26.317 21.447 1.00 103.63 ? 56 TRP B NE1 1 ATOM 188 C CE2 . TRP A 1 25 ? 99.925 -26.359 22.809 1.00 102.86 ? 56 TRP B CE2 1 ATOM 189 C CE3 . TRP A 1 25 ? 101.129 -27.283 24.679 1.00 101.56 ? 56 TRP B CE3 1 ATOM 190 C CZ2 . TRP A 1 25 ? 98.958 -25.818 23.640 1.00 99.98 ? 56 TRP B CZ2 1 ATOM 191 C CZ3 . TRP A 1 25 ? 100.171 -26.739 25.505 1.00 100.59 ? 56 TRP B CZ3 1 ATOM 192 C CH2 . TRP A 1 25 ? 99.098 -26.017 24.984 1.00 99.35 ? 56 TRP B CH2 1 ATOM 193 N N . LYS A 1 26 ? 106.151 -29.093 20.640 1.00 90.47 ? 57 LYS B N 1 ATOM 194 C CA . LYS A 1 26 ? 107.422 -29.660 21.089 1.00 92.64 ? 57 LYS B CA 1 ATOM 195 C C . LYS A 1 26 ? 108.482 -28.598 21.424 1.00 92.30 ? 57 LYS B C 1 ATOM 196 O O . LYS A 1 26 ? 108.474 -27.502 20.868 1.00 93.92 ? 57 LYS B O 1 ATOM 197 C CB . LYS A 1 26 ? 107.946 -30.730 20.121 1.00 95.39 ? 57 LYS B CB 1 ATOM 198 C CG . LYS A 1 26 ? 107.472 -32.152 20.448 1.00 95.11 ? 57 LYS B CG 1 ATOM 199 C CD . LYS A 1 26 ? 108.123 -33.158 19.518 1.00 96.73 ? 57 LYS B CD 1 ATOM 200 C CE . LYS A 1 26 ? 107.853 -32.829 18.046 1.00 98.31 ? 57 LYS B CE 1 ATOM 201 N NZ . LYS A 1 26 ? 106.434 -33.068 17.635 1.00 96.68 ? 57 LYS B NZ 1 ATOM 202 N N . VAL A 1 27 ? 109.352 -28.931 22.376 1.00 76.42 ? 58 VAL B N 1 ATOM 203 C CA . VAL A 1 27 ? 110.455 -28.068 22.815 1.00 79.38 ? 58 VAL B CA 1 ATOM 204 C C . VAL A 1 27 ? 111.845 -28.474 22.292 1.00 84.00 ? 58 VAL B C 1 ATOM 205 O O . VAL A 1 27 ? 112.227 -29.643 22.375 1.00 83.65 ? 58 VAL B O 1 ATOM 206 C CB . VAL A 1 27 ? 110.518 -28.043 24.334 1.00 76.70 ? 58 VAL B CB 1 ATOM 207 C CG1 . VAL A 1 27 ? 110.358 -29.464 24.867 1.00 79.70 ? 58 VAL B CG1 1 ATOM 208 C CG2 . VAL A 1 27 ? 111.816 -27.372 24.823 1.00 76.67 ? 58 VAL B CG2 1 ATOM 209 N N . PRO A 1 28 ? 112.610 -27.507 21.753 1.00 124.36 ? 59 PRO B N 1 ATOM 210 C CA . PRO A 1 28 ? 113.989 -27.742 21.295 1.00 127.58 ? 59 PRO B CA 1 ATOM 211 C C . PRO A 1 28 ? 114.875 -28.395 22.356 1.00 129.13 ? 59 PRO B C 1 ATOM 212 O O . PRO A 1 28 ? 116.050 -28.032 22.451 1.00 130.16 ? 59 PRO B O 1 ATOM 213 C CB . PRO A 1 28 ? 114.506 -26.331 21.009 1.00 128.31 ? 59 PRO B CB 1 ATOM 214 C CG . PRO A 1 28 ? 113.295 -25.554 20.690 1.00 128.20 ? 59 PRO B CG 1 ATOM 215 C CD . PRO A 1 28 ? 112.199 -26.109 21.551 1.00 126.56 ? 59 PRO B CD 1 ATOM 216 N N . ASP A 1 34 ? 114.285 -21.351 24.878 1.00 124.66 ? 65 ASP B N 1 ATOM 217 C CA . ASP A 1 34 ? 114.236 -20.058 25.551 1.00 127.59 ? 65 ASP B CA 1 ATOM 218 C C . ASP A 1 34 ? 112.991 -19.279 25.137 1.00 128.43 ? 65 ASP B C 1 ATOM 219 O O . ASP A 1 34 ? 112.882 -18.826 23.997 1.00 131.65 ? 65 ASP B O 1 ATOM 220 C CB . ASP A 1 34 ? 115.498 -19.246 25.250 1.00 130.96 ? 65 ASP B CB 1 ATOM 221 C CG . ASP A 1 34 ? 116.759 -19.906 25.779 1.00 133.99 ? 65 ASP B CG 1 ATOM 222 O OD1 . ASP A 1 34 ? 117.116 -19.649 26.946 1.00 134.18 ? 65 ASP B OD1 1 ATOM 223 O OD2 . ASP A 1 34 ? 117.395 -20.676 25.028 1.00 133.51 ? 65 ASP B OD2 1 ATOM 224 N N . ALA A 1 35 ? 112.054 -19.143 26.074 1.00 111.05 ? 66 ALA B N 1 ATOM 225 C CA . ALA A 1 35 ? 110.760 -18.505 25.829 1.00 106.22 ? 66 ALA B CA 1 ATOM 226 C C . ALA A 1 35 ? 110.042 -19.160 24.658 1.00 106.37 ? 66 ALA B C 1 ATOM 227 O O . ALA A 1 35 ? 109.239 -18.533 23.977 1.00 105.58 ? 66 ALA B O 1 ATOM 228 C CB . ALA A 1 35 ? 110.926 -17.013 25.598 1.00 105.86 ? 66 ALA B CB 1 ATOM 229 N N . VAL A 1 36 ? 110.331 -20.438 24.452 1.00 115.75 ? 67 VAL B N 1 ATOM 230 C CA . VAL A 1 36 ? 109.848 -21.178 23.298 1.00 117.00 ? 67 VAL B CA 1 ATOM 231 C C . VAL A 1 36 ? 108.335 -21.341 23.300 1.00 117.47 ? 67 VAL B C 1 ATOM 232 O O . VAL A 1 36 ? 107.659 -21.068 22.305 1.00 117.92 ? 67 VAL B O 1 ATOM 233 C CB . VAL A 1 36 ? 110.510 -22.570 23.245 1.00 116.52 ? 67 VAL B CB 1 ATOM 234 C CG1 . VAL A 1 36 ? 110.822 -23.066 24.654 1.00 114.93 ? 67 VAL B CG1 1 ATOM 235 C CG2 . VAL A 1 36 ? 109.635 -23.563 22.491 1.00 117.40 ? 67 VAL B CG2 1 ATOM 236 N N . TRP A 1 37 ? 107.813 -21.764 24.442 1.00 103.91 ? 68 TRP B N 1 ATOM 237 C CA . TRP A 1 37 ? 106.422 -22.156 24.575 1.00 98.70 ? 68 TRP B CA 1 ATOM 238 C C . TRP A 1 37 ? 105.448 -21.059 24.179 1.00 95.46 ? 68 TRP B C 1 ATOM 239 O O . TRP A 1 37 ? 104.292 -21.332 23.875 1.00 95.90 ? 68 TRP B O 1 ATOM 240 C CB . TRP A 1 37 ? 106.165 -22.564 26.012 1.00 93.07 ? 68 TRP B CB 1 ATOM 241 C CG . TRP A 1 37 ? 106.467 -21.472 26.987 1.00 91.57 ? 68 TRP B CG 1 ATOM 242 C CD1 . TRP A 1 37 ? 105.588 -20.559 27.489 1.00 91.74 ? 68 TRP B CD1 1 ATOM 243 C CD2 . TRP A 1 37 ? 107.739 -21.171 27.582 1.00 88.69 ? 68 TRP B CD2 1 ATOM 244 N NE1 . TRP A 1 37 ? 106.228 -19.712 28.367 1.00 90.01 ? 68 TRP B NE1 1 ATOM 245 C CE2 . TRP A 1 37 ? 107.549 -20.067 28.442 1.00 88.40 ? 68 TRP B CE2 1 ATOM 246 C CE3 . TRP A 1 37 ? 109.017 -21.730 27.476 1.00 89.49 ? 68 TRP B CE3 1 ATOM 247 C CZ2 . TRP A 1 37 ? 108.586 -19.511 29.189 1.00 91.40 ? 68 TRP B CZ2 1 ATOM 248 C CZ3 . TRP A 1 37 ? 110.046 -21.179 28.220 1.00 90.75 ? 68 TRP B CZ3 1 ATOM 249 C CH2 . TRP A 1 37 ? 109.824 -20.076 29.063 1.00 91.75 ? 68 TRP B CH2 1 ATOM 250 N N . CYS A 1 38 ? 105.927 -19.819 24.181 1.00 87.23 ? 69 CYS B N 1 ATOM 251 C CA . CYS A 1 38 ? 105.103 -18.665 23.834 1.00 85.51 ? 69 CYS B CA 1 ATOM 252 C C . CYS A 1 38 ? 104.692 -18.633 22.366 1.00 85.82 ? 69 CYS B C 1 ATOM 253 O O . CYS A 1 38 ? 103.853 -17.826 21.965 1.00 87.97 ? 69 CYS B O 1 ATOM 254 C CB . CYS A 1 38 ? 105.825 -17.367 24.188 1.00 83.98 ? 69 CYS B CB 1 ATOM 255 S SG . CYS A 1 38 ? 105.783 -16.975 25.941 1.00 120.36 ? 69 CYS B SG 1 ATOM 256 N N . SER A 1 39 ? 105.301 -19.490 21.560 1.00 99.46 ? 70 SER B N 1 ATOM 257 C CA . SER A 1 39 ? 104.955 -19.546 20.156 1.00 101.45 ? 70 SER B CA 1 ATOM 258 C C . SER A 1 39 ? 103.706 -20.371 19.973 1.00 99.77 ? 70 SER B C 1 ATOM 259 O O . SER A 1 39 ? 102.939 -20.155 19.046 1.00 98.22 ? 70 SER B O 1 ATOM 260 C CB . SER A 1 39 ? 106.102 -20.160 19.363 1.00 104.00 ? 70 SER B CB 1 ATOM 261 O OG . SER A 1 39 ? 107.317 -19.505 19.679 1.00 107.79 ? 70 SER B OG 1 ATOM 262 N N . TRP A 1 40 ? 103.479 -21.277 20.912 1.00 105.79 ? 71 TRP B N 1 ATOM 263 C CA . TRP A 1 40 ? 102.604 -22.414 20.681 1.00 104.38 ? 71 TRP B CA 1 ATOM 264 C C . TRP A 1 40 ? 101.185 -22.008 20.368 1.00 101.75 ? 71 TRP B C 1 ATOM 265 O O . TRP A 1 40 ? 100.768 -20.883 20.632 1.00 102.73 ? 71 TRP B O 1 ATOM 266 C CB . TRP A 1 40 ? 102.621 -23.377 21.870 1.00 102.86 ? 71 TRP B CB 1 ATOM 267 C CG . TRP A 1 40 ? 103.963 -23.971 22.134 1.00 101.42 ? 71 TRP B CG 1 ATOM 268 C CD1 . TRP A 1 40 ? 105.086 -23.822 21.379 1.00 100.35 ? 71 TRP B CD1 1 ATOM 269 C CD2 . TRP A 1 40 ? 104.329 -24.805 23.233 1.00 99.29 ? 71 TRP B CD2 1 ATOM 270 N NE1 . TRP A 1 40 ? 106.131 -24.512 21.939 1.00 101.02 ? 71 TRP B NE1 1 ATOM 271 C CE2 . TRP A 1 40 ? 105.691 -25.125 23.079 1.00 100.05 ? 71 TRP B CE2 1 ATOM 272 C CE3 . TRP A 1 40 ? 103.641 -25.308 24.333 1.00 97.28 ? 71 TRP B CE3 1 ATOM 273 C CZ2 . TRP A 1 40 ? 106.378 -25.916 23.991 1.00 100.36 ? 71 TRP B CZ2 1 ATOM 274 C CZ3 . TRP A 1 40 ? 104.319 -26.109 25.229 1.00 99.11 ? 71 TRP B CZ3 1 ATOM 275 C CH2 . TRP A 1 40 ? 105.674 -26.408 25.052 1.00 100.45 ? 71 TRP B CH2 1 ATOM 276 N N . SER A 1 41 ? 100.465 -22.939 19.760 1.00 75.26 ? 72 SER B N 1 ATOM 277 C CA . SER A 1 41 ? 99.104 -22.694 19.315 1.00 75.96 ? 72 SER B CA 1 ATOM 278 C C . SER A 1 41 ? 98.119 -22.774 20.460 1.00 75.19 ? 72 SER B C 1 ATOM 279 O O . SER A 1 41 ? 97.902 -23.848 21.020 1.00 73.26 ? 72 SER B O 1 ATOM 280 C CB . SER A 1 41 ? 98.692 -23.745 18.282 1.00 75.78 ? 72 SER B CB 1 ATOM 281 O OG . SER A 1 41 ? 98.487 -25.010 18.894 1.00 76.31 ? 72 SER B OG 1 ATOM 282 N N . GLY A 1 42 ? 97.457 -21.655 20.739 1.00 70.12 ? 73 GLY B N 1 ATOM 283 C CA . GLY A 1 42 ? 96.497 -21.563 21.821 1.00 66.56 ? 73 GLY B CA 1 ATOM 284 C C . GLY A 1 42 ? 97.088 -20.751 22.941 1.00 68.08 ? 73 GLY B C 1 ATOM 285 O O . GLY A 1 42 ? 96.374 -20.221 23.788 1.00 69.26 ? 73 GLY B O 1 ATOM 286 N N . VAL A 1 43 ? 98.406 -20.632 22.914 1.00 68.69 ? 74 VAL B N 1 ATOM 287 C CA . VAL A 1 43 ? 99.127 -19.910 23.940 1.00 70.05 ? 74 VAL B CA 1 ATOM 288 C C . VAL A 1 43 ? 99.394 -18.474 23.497 1.00 72.20 ? 74 VAL B C 1 ATOM 289 O O . VAL A 1 43 ? 99.729 -18.222 22.339 1.00 73.87 ? 74 VAL B O 1 ATOM 290 C CB . VAL A 1 43 ? 100.452 -20.617 24.258 1.00 70.61 ? 74 VAL B CB 1 ATOM 291 C CG1 . VAL A 1 43 ? 101.255 -19.836 25.298 1.00 67.34 ? 74 VAL B CG1 1 ATOM 292 C CG2 . VAL A 1 43 ? 100.185 -22.039 24.722 1.00 66.51 ? 74 VAL B CG2 1 ATOM 293 N N . VAL A 1 44 ? 99.216 -17.532 24.419 1.00 71.46 ? 75 VAL B N 1 ATOM 294 C CA . VAL A 1 44 ? 99.581 -16.135 24.201 1.00 70.02 ? 75 VAL B CA 1 ATOM 295 C C . VAL A 1 44 ? 100.346 -15.672 25.423 1.00 70.19 ? 75 VAL B C 1 ATOM 296 O O . VAL A 1 44 ? 99.896 -15.880 26.542 1.00 70.66 ? 75 VAL B O 1 ATOM 297 C CB . VAL A 1 44 ? 98.341 -15.253 24.050 1.00 72.86 ? 75 VAL B CB 1 ATOM 298 C CG1 . VAL A 1 44 ? 98.720 -13.786 24.142 1.00 71.14 ? 75 VAL B CG1 1 ATOM 299 C CG2 . VAL A 1 44 ? 97.629 -15.569 22.745 1.00 67.42 ? 75 VAL B CG2 1 ATOM 300 N N . CYS A 1 45 ? 101.501 -15.053 25.232 1.00 81.45 ? 76 CYS B N 1 ATOM 301 C CA . CYS A 1 45 ? 102.302 -14.665 26.384 1.00 80.84 ? 76 CYS B CA 1 ATOM 302 C C . CYS A 1 45 ? 102.382 -13.162 26.487 1.00 85.11 ? 76 CYS B C 1 ATOM 303 O O . CYS A 1 45 ? 102.173 -12.448 25.512 1.00 90.97 ? 76 CYS B O 1 ATOM 304 C CB . CYS A 1 45 ? 103.712 -15.262 26.327 1.00 83.72 ? 76 CYS B CB 1 ATOM 305 S SG . CYS A 1 45 ? 103.809 -17.076 26.439 1.00 91.53 ? 76 CYS B SG 1 ATOM 306 N N . ASP A 1 46 ? 102.658 -12.687 27.690 1.00 84.81 ? 77 ASP B N 1 ATOM 307 C CA . ASP A 1 46 ? 102.785 -11.266 27.929 1.00 86.73 ? 77 ASP B CA 1 ATOM 308 C C . ASP A 1 46 ? 104.177 -10.862 27.480 1.00 87.90 ? 77 ASP B C 1 ATOM 309 O O . ASP A 1 46 ? 105.158 -11.295 28.069 1.00 91.63 ? 77 ASP B O 1 ATOM 310 C CB . ASP A 1 46 ? 102.609 -11.016 29.420 1.00 89.42 ? 77 ASP B CB 1 ATOM 311 C CG . ASP A 1 46 ? 102.736 -9.570 29.784 1.00 92.55 ? 77 ASP B CG 1 ATOM 312 O OD1 . ASP A 1 46 ? 103.884 -9.107 29.945 1.00 91.49 ? 77 ASP B OD1 1 ATOM 313 O OD2 . ASP A 1 46 ? 101.689 -8.900 29.921 1.00 95.51 ? 77 ASP B OD2 1 ATOM 314 N N . ASN A 1 47 ? 104.262 -10.001 26.470 1.00 91.05 ? 78 ASN B N 1 ATOM 315 C CA . ASN A 1 47 ? 105.512 -9.823 25.723 1.00 90.40 ? 78 ASN B CA 1 ATOM 316 C C . ASN A 1 47 ? 106.745 -9.403 26.538 1.00 88.51 ? 78 ASN B C 1 ATOM 317 O O . ASN A 1 47 ? 107.878 -9.605 26.106 1.00 92.20 ? 78 ASN B O 1 ATOM 318 C CB . ASN A 1 47 ? 105.307 -8.919 24.492 1.00 94.03 ? 78 ASN B CB 1 ATOM 319 C CG . ASN A 1 47 ? 105.119 -9.714 23.192 1.00 98.17 ? 78 ASN B CG 1 ATOM 320 O OD1 . ASN A 1 47 ? 105.732 -10.769 22.997 1.00 100.39 ? 78 ASN B OD1 1 ATOM 321 N ND2 . ASN A 1 47 ? 104.274 -9.201 22.297 1.00 101.39 ? 78 ASN B ND2 1 ATOM 322 N N . VAL A 1 48 ? 106.538 -8.824 27.711 1.00 93.69 ? 79 VAL B N 1 ATOM 323 C CA . VAL A 1 48 ? 107.666 -8.533 28.594 1.00 94.37 ? 79 VAL B CA 1 ATOM 324 C C . VAL A 1 48 ? 108.113 -9.764 29.375 1.00 96.46 ? 79 VAL B C 1 ATOM 325 O O . VAL A 1 48 ? 109.306 -10.066 29.470 1.00 96.69 ? 79 VAL B O 1 ATOM 326 C CB . VAL A 1 48 ? 107.316 -7.450 29.634 1.00 92.05 ? 79 VAL B CB 1 ATOM 327 C CG1 . VAL A 1 48 ? 108.561 -7.042 30.418 1.00 92.56 ? 79 VAL B CG1 1 ATOM 328 C CG2 . VAL A 1 48 ? 106.669 -6.247 28.964 1.00 92.91 ? 79 VAL B CG2 1 ATOM 329 N N . THR A 1 49 ? 107.132 -10.453 29.949 1.00 98.48 ? 80 THR B N 1 ATOM 330 C CA . THR A 1 49 ? 107.380 -11.454 30.979 1.00 95.25 ? 80 THR B CA 1 ATOM 331 C C . THR A 1 49 ? 107.406 -12.919 30.538 1.00 95.53 ? 80 THR B C 1 ATOM 332 O O . THR A 1 49 ? 107.688 -13.796 31.350 1.00 96.54 ? 80 THR B O 1 ATOM 333 C CB . THR A 1 49 ? 106.319 -11.321 32.082 1.00 92.21 ? 80 THR B CB 1 ATOM 334 O OG1 . THR A 1 49 ? 105.148 -12.063 31.713 1.00 90.46 ? 80 THR B OG1 1 ATOM 335 C CG2 . THR A 1 49 ? 105.952 -9.852 32.279 1.00 91.86 ? 80 THR B CG2 1 ATOM 336 N N . ALA A 1 50 ? 107.081 -13.189 29.280 1.00 83.96 ? 81 ALA B N 1 ATOM 337 C CA . ALA A 1 50 ? 107.048 -14.560 28.766 1.00 83.56 ? 81 ALA B CA 1 ATOM 338 C C . ALA A 1 50 ? 105.982 -15.455 29.414 1.00 81.52 ? 81 ALA B C 1 ATOM 339 O O . ALA A 1 50 ? 105.858 -16.627 29.059 1.00 81.76 ? 81 ALA B O 1 ATOM 340 C CB . ALA A 1 50 ? 108.429 -15.218 28.834 1.00 82.95 ? 81 ALA B CB 1 ATOM 341 N N . GLN A 1 51 ? 105.244 -14.916 30.383 1.00 80.91 ? 82 GLN B N 1 ATOM 342 C CA . GLN A 1 51 ? 104.254 -15.695 31.127 1.00 77.39 ? 82 GLN B CA 1 ATOM 343 C C . GLN A 1 51 ? 102.974 -15.870 30.323 1.00 76.36 ? 82 GLN B C 1 ATOM 344 O O . GLN A 1 51 ? 102.598 -14.990 29.557 1.00 77.05 ? 82 GLN B O 1 ATOM 345 C CB . GLN A 1 51 ? 103.978 -15.035 32.473 1.00 75.11 ? 82 GLN B CB 1 ATOM 346 C CG . GLN A 1 51 ? 105.248 -14.784 33.289 1.00 75.44 ? 82 GLN B CG 1 ATOM 347 C CD . GLN A 1 51 ? 105.997 -16.063 33.644 1.00 80.39 ? 82 GLN B CD 1 ATOM 348 O OE1 . GLN A 1 51 ? 106.912 -16.488 32.932 1.00 81.89 ? 82 GLN B OE1 1 ATOM 349 N NE2 . GLN A 1 51 ? 105.615 -16.679 34.757 1.00 81.56 ? 82 GLN B NE2 1 ATOM 350 N N . VAL A 1 52 ? 102.294 -16.997 30.499 1.00 73.94 ? 83 VAL B N 1 ATOM 351 C CA . VAL A 1 52 ? 101.246 -17.346 29.553 1.00 73.01 ? 83 VAL B CA 1 ATOM 352 C C . VAL A 1 52 ? 99.973 -16.741 30.061 1.00 74.93 ? 83 VAL B C 1 ATOM 353 O O . VAL A 1 52 ? 99.406 -17.219 31.037 1.00 76.11 ? 83 VAL B O 1 ATOM 354 C CB . VAL A 1 52 ? 101.024 -18.874 29.480 1.00 70.83 ? 83 VAL B CB 1 ATOM 355 C CG1 . VAL A 1 52 ? 99.807 -19.199 28.623 1.00 70.49 ? 83 VAL B CG1 1 ATOM 356 C CG2 . VAL A 1 52 ? 102.257 -19.578 28.946 1.00 71.75 ? 83 VAL B CG2 1 ATOM 357 N N . ILE A 1 53 ? 99.519 -15.690 29.383 1.00 62.86 ? 84 ILE B N 1 ATOM 358 C CA . ILE A 1 53 ? 98.348 -14.951 29.825 1.00 64.59 ? 84 ILE B CA 1 ATOM 359 C C . ILE A 1 53 ? 97.055 -15.382 29.163 1.00 63.79 ? 84 ILE B C 1 ATOM 360 O O . ILE A 1 53 ? 95.988 -14.981 29.598 1.00 62.86 ? 84 ILE B O 1 ATOM 361 C CB . ILE A 1 53 ? 98.522 -13.430 29.661 1.00 67.00 ? 84 ILE B CB 1 ATOM 362 C CG1 . ILE A 1 53 ? 98.689 -13.067 28.200 1.00 69.01 ? 84 ILE B CG1 1 ATOM 363 C CG2 . ILE A 1 53 ? 99.724 -12.953 30.415 1.00 63.22 ? 84 ILE B CG2 1 ATOM 364 C CD1 . ILE A 1 53 ? 99.206 -11.673 28.003 1.00 68.32 ? 84 ILE B CD1 1 ATOM 365 N N . SER A 1 54 ? 97.126 -16.187 28.114 1.00 68.39 ? 85 SER B N 1 ATOM 366 C CA . SER A 1 54 ? 95.895 -16.630 27.474 1.00 67.93 ? 85 SER B CA 1 ATOM 367 C C . SER A 1 54 ? 96.023 -18.041 26.964 1.00 67.81 ? 85 SER B C 1 ATOM 368 O O . SER A 1 54 ? 96.962 -18.366 26.242 1.00 68.47 ? 85 SER B O 1 ATOM 369 C CB . SER A 1 54 ? 95.511 -15.691 26.328 1.00 68.50 ? 85 SER B CB 1 ATOM 370 O OG . SER A 1 54 ? 94.231 -15.999 25.797 1.00 68.09 ? 85 SER B OG 1 ATOM 371 N N . LEU A 1 55 ? 95.063 -18.877 27.326 1.00 68.07 ? 86 LEU B N 1 ATOM 372 C CA . LEU A 1 55 ? 95.063 -20.242 26.851 1.00 67.92 ? 86 LEU B CA 1 ATOM 373 C C . LEU A 1 55 ? 93.700 -20.585 26.298 1.00 67.42 ? 86 LEU B C 1 ATOM 374 O O . LEU A 1 55 ? 92.744 -20.737 27.043 1.00 66.71 ? 86 LEU B O 1 ATOM 375 C CB . LEU A 1 55 ? 95.409 -21.168 28.011 1.00 67.48 ? 86 LEU B CB 1 ATOM 376 C CG . LEU A 1 55 ? 96.053 -22.519 27.713 1.00 67.65 ? 86 LEU B CG 1 ATOM 377 C CD1 . LEU A 1 55 ? 97.114 -22.417 26.638 1.00 68.49 ? 86 LEU B CD1 1 ATOM 378 C CD2 . LEU A 1 55 ? 96.665 -23.061 28.983 1.00 67.46 ? 86 LEU B CD2 1 ATOM 379 N N . ASP A 1 56 ? 93.608 -20.742 24.989 1.00 81.08 ? 87 ASP B N 1 ATOM 380 C CA . ASP A 1 56 ? 92.344 -21.145 24.413 1.00 80.67 ? 87 ASP B CA 1 ATOM 381 C C . ASP A 1 56 ? 92.515 -22.481 23.746 1.00 80.63 ? 87 ASP B C 1 ATOM 382 O O . ASP A 1 56 ? 93.275 -22.611 22.793 1.00 81.20 ? 87 ASP B O 1 ATOM 383 C CB . ASP A 1 56 ? 91.834 -20.126 23.394 1.00 81.12 ? 87 ASP B CB 1 ATOM 384 C CG . ASP A 1 56 ? 90.544 -20.587 22.692 1.00 80.81 ? 87 ASP B CG 1 ATOM 385 O OD1 . ASP A 1 56 ? 89.772 -21.360 23.299 1.00 80.14 ? 87 ASP B OD1 1 ATOM 386 O OD2 . ASP A 1 56 ? 90.296 -20.178 21.532 1.00 81.27 ? 87 ASP B OD2 1 ATOM 387 N N . LEU A 1 57 ? 91.848 -23.492 24.279 1.00 57.72 ? 88 LEU B N 1 ATOM 388 C CA . LEU A 1 57 ? 91.747 -24.745 23.561 1.00 57.79 ? 88 LEU B CA 1 ATOM 389 C C . LEU A 1 57 ? 90.342 -25.333 23.618 1.00 57.01 ? 88 LEU B C 1 ATOM 390 O O . LEU A 1 57 ? 89.934 -25.856 24.641 1.00 56.25 ? 88 LEU B O 1 ATOM 391 C CB . LEU A 1 57 ? 92.745 -25.722 24.157 1.00 57.81 ? 88 LEU B CB 1 ATOM 392 C CG . LEU A 1 57 ? 93.014 -25.578 25.648 1.00 57.24 ? 88 LEU B CG 1 ATOM 393 C CD1 . LEU A 1 57 ? 93.061 -26.966 26.239 1.00 56.81 ? 88 LEU B CD1 1 ATOM 394 C CD2 . LEU A 1 57 ? 94.323 -24.858 25.875 1.00 57.95 ? 88 LEU B CD2 1 ATOM 395 N N . SER A 1 58 ? 89.637 -25.356 22.500 1.00 60.17 ? 89 SER B N 1 ATOM 396 C CA . SER A 1 58 ? 88.239 -25.738 22.539 1.00 59.66 ? 89 SER B CA 1 ATOM 397 C C . SER A 1 58 ? 87.838 -26.388 21.231 1.00 59.81 ? 89 SER B C 1 ATOM 398 O O . SER A 1 58 ? 88.461 -26.142 20.196 1.00 60.33 ? 89 SER B O 1 ATOM 399 C CB . SER A 1 58 ? 87.405 -24.496 22.788 1.00 59.64 ? 89 SER B CB 1 ATOM 400 O OG . SER A 1 58 ? 88.141 -23.346 22.407 1.00 60.38 ? 89 SER B OG 1 ATOM 401 N N . HIS A 1 59 ? 86.805 -27.223 21.272 1.00 101.92 ? 90 HIS B N 1 ATOM 402 C CA . HIS A 1 59 ? 86.399 -27.988 20.098 1.00 102.03 ? 90 HIS B CA 1 ATOM 403 C C . HIS A 1 59 ? 87.590 -28.776 19.577 1.00 102.30 ? 90 HIS B C 1 ATOM 404 O O . HIS A 1 59 ? 87.727 -29.005 18.373 1.00 102.64 ? 90 HIS B O 1 ATOM 405 C CB . HIS A 1 59 ? 85.852 -27.070 19.004 1.00 102.47 ? 90 HIS B CB 1 ATOM 406 C CG . HIS A 1 59 ? 84.794 -26.132 19.485 1.00 102.37 ? 90 HIS B CG 1 ATOM 407 N ND1 . HIS A 1 59 ? 85.071 -25.051 20.293 1.00 102.40 ? 90 HIS B ND1 1 ATOM 408 C CD2 . HIS A 1 59 ? 83.456 -26.118 19.282 1.00 102.25 ? 90 HIS B CD2 1 ATOM 409 C CE1 . HIS A 1 59 ? 83.950 -24.409 20.564 1.00 102.30 ? 90 HIS B CE1 1 ATOM 410 N NE2 . HIS A 1 59 ? 82.955 -25.036 19.962 1.00 102.23 ? 90 HIS B NE2 1 ATOM 411 N N . ARG A 1 60 ? 88.457 -29.167 20.504 1.00 89.51 ? 91 ARG B N 1 ATOM 412 C CA . ARG A 1 60 ? 89.646 -29.938 20.189 1.00 89.77 ? 91 ARG B CA 1 ATOM 413 C C . ARG A 1 60 ? 89.381 -31.441 20.271 1.00 89.48 ? 91 ARG B C 1 ATOM 414 O O . ARG A 1 60 ? 90.312 -32.239 20.172 1.00 89.64 ? 91 ARG B O 1 ATOM 415 C CB . ARG A 1 60 ? 90.800 -29.548 21.111 1.00 89.82 ? 91 ARG B CB 1 ATOM 416 C CG . ARG A 1 60 ? 91.376 -28.179 20.828 1.00 90.49 ? 91 ARG B CG 1 ATOM 417 C CD . ARG A 1 60 ? 92.729 -28.007 21.494 1.00 90.59 ? 91 ARG B CD 1 ATOM 418 N NE . ARG A 1 60 ? 93.456 -26.845 20.982 1.00 91.57 ? 91 ARG B NE 1 ATOM 419 C CZ . ARG A 1 60 ? 94.669 -26.475 21.389 1.00 91.87 ? 91 ARG B CZ 1 ATOM 420 N NH1 . ARG A 1 60 ? 95.301 -27.166 22.324 1.00 91.24 ? 91 ARG B NH1 1 ATOM 421 N NH2 . ARG A 1 60 ? 95.256 -25.410 20.863 1.00 92.86 ? 91 ARG B NH2 1 ATOM 422 N N . ASN A 1 61 ? 88.116 -31.818 20.475 1.00 87.20 ? 92 ASN B N 1 ATOM 423 C CA . ASN A 1 61 ? 87.734 -33.218 20.674 1.00 86.98 ? 92 ASN B CA 1 ATOM 424 C C . ASN A 1 61 ? 88.566 -33.831 21.802 1.00 86.97 ? 92 ASN B C 1 ATOM 425 O O . ASN A 1 61 ? 88.833 -35.033 21.803 1.00 87.11 ? 92 ASN B O 1 ATOM 426 C CB . ASN A 1 61 ? 87.879 -34.042 19.378 1.00 87.63 ? 92 ASN B CB 1 ATOM 427 C CG . ASN A 1 61 ? 86.746 -33.798 18.382 1.00 87.49 ? 92 ASN B CG 1 ATOM 428 O OD1 . ASN A 1 61 ? 86.047 -32.786 18.449 1.00 87.29 ? 92 ASN B OD1 1 ATOM 429 N ND2 . ASN A 1 61 ? 86.566 -34.732 17.449 1.00 87.66 ? 92 ASN B ND2 1 ATOM 430 N N . LEU A 1 62 ? 88.958 -32.988 22.762 1.00 70.68 ? 93 LEU B N 1 ATOM 431 C CA . LEU A 1 62 ? 89.900 -33.375 23.818 1.00 70.70 ? 93 LEU B CA 1 ATOM 432 C C . LEU A 1 62 ? 89.264 -33.674 25.200 1.00 70.33 ? 93 LEU B C 1 ATOM 433 O O . LEU A 1 62 ? 88.589 -32.834 25.802 1.00 69.93 ? 93 LEU B O 1 ATOM 434 C CB . LEU A 1 62 ? 91.064 -32.367 23.909 1.00 70.48 ? 93 LEU B CB 1 ATOM 435 C CG . LEU A 1 62 ? 91.272 -31.465 25.131 1.00 69.95 ? 93 LEU B CG 1 ATOM 436 C CD1 . LEU A 1 62 ? 92.681 -30.914 25.162 1.00 70.10 ? 93 LEU B CD1 1 ATOM 437 C CD2 . LEU A 1 62 ? 90.312 -30.331 25.082 1.00 69.94 ? 93 LEU B CD2 1 ATOM 438 N N . SER A 1 63 ? 89.496 -34.897 25.678 1.00 88.76 ? 94 SER B N 1 ATOM 439 C CA . SER A 1 63 ? 88.893 -35.412 26.900 1.00 88.51 ? 94 SER B CA 1 ATOM 440 C C . SER A 1 63 ? 89.984 -35.807 27.864 1.00 89.04 ? 94 SER B C 1 ATOM 441 O O . SER A 1 63 ? 91.134 -35.980 27.470 1.00 89.84 ? 94 SER B O 1 ATOM 442 C CB . SER A 1 63 ? 88.093 -36.657 26.589 1.00 87.93 ? 94 SER B CB 1 ATOM 443 O OG . SER A 1 63 ? 88.965 -37.674 26.154 1.00 88.82 ? 94 SER B OG 1 ATOM 444 N N . GLY A 1 64 ? 89.643 -35.927 29.139 1.00 72.35 ? 95 GLY B N 1 ATOM 445 C CA . GLY A 1 64 ? 90.652 -36.286 30.104 1.00 72.84 ? 95 GLY B CA 1 ATOM 446 C C . GLY A 1 64 ? 90.501 -35.599 31.442 1.00 72.88 ? 95 GLY B C 1 ATOM 447 O O . GLY A 1 64 ? 89.440 -35.081 31.797 1.00 72.46 ? 95 GLY B O 1 ATOM 448 N N . ARG A 1 65 ? 91.598 -35.613 32.188 1.00 83.11 ? 96 ARG B N 1 ATOM 449 C CA . ARG A 1 65 ? 91.695 -34.936 33.466 1.00 83.20 ? 96 ARG B CA 1 ATOM 450 C C . ARG A 1 65 ? 92.458 -33.660 33.237 1.00 83.10 ? 96 ARG B C 1 ATOM 451 O O . ARG A 1 65 ? 93.376 -33.604 32.425 1.00 83.39 ? 96 ARG B O 1 ATOM 452 C CB . ARG A 1 65 ? 92.433 -35.814 34.495 1.00 84.17 ? 96 ARG B CB 1 ATOM 453 C CG . ARG A 1 65 ? 92.980 -35.074 35.745 1.00 84.31 ? 96 ARG B CG 1 ATOM 454 C CD . ARG A 1 65 ? 93.902 -35.961 36.619 1.00 85.41 ? 96 ARG B CD 1 ATOM 455 N NE . ARG A 1 65 ? 95.028 -36.536 35.874 1.00 85.84 ? 96 ARG B NE 1 ATOM 456 C CZ . ARG A 1 65 ? 96.242 -35.993 35.785 1.00 86.15 ? 96 ARG B CZ 1 ATOM 457 N NH1 . ARG A 1 65 ? 96.513 -34.846 36.398 1.00 86.11 ? 96 ARG B NH1 1 ATOM 458 N NH2 . ARG A 1 65 ? 97.189 -36.602 35.080 1.00 86.42 ? 96 ARG B NH2 1 ATOM 459 N N . ILE A 1 66 ? 92.065 -32.629 33.960 1.00 59.86 ? 97 ILE B N 1 ATOM 460 C CA . ILE A 1 66 ? 92.731 -31.343 33.861 1.00 59.79 ? 97 ILE B CA 1 ATOM 461 C C . ILE A 1 66 ? 93.844 -31.212 34.939 1.00 60.34 ? 97 ILE B C 1 ATOM 462 O O . ILE A 1 66 ? 93.564 -31.201 36.141 1.00 60.35 ? 97 ILE B O 1 ATOM 463 C CB . ILE A 1 66 ? 91.672 -30.161 33.776 1.00 59.06 ? 97 ILE B CB 1 ATOM 464 C CG1 . ILE A 1 66 ? 92.295 -28.805 34.101 1.00 59.06 ? 97 ILE B CG1 1 ATOM 465 C CG2 . ILE A 1 66 ? 90.391 -30.475 34.596 1.00 58.61 ? 97 ILE B CG2 1 ATOM 466 C CD1 . ILE A 1 66 ? 92.126 -28.389 35.536 1.00 58.87 ? 97 ILE B CD1 1 ATOM 467 N N . PRO A 1 67 ? 95.111 -31.098 34.488 1.00 71.95 ? 98 PRO B N 1 ATOM 468 C CA . PRO A 1 67 ? 96.364 -31.253 35.237 1.00 72.66 ? 98 PRO B CA 1 ATOM 469 C C . PRO A 1 67 ? 96.389 -30.434 36.486 1.00 72.63 ? 98 PRO B C 1 ATOM 470 O O . PRO A 1 67 ? 95.666 -29.452 36.603 1.00 71.96 ? 98 PRO B O 1 ATOM 471 C CB . PRO A 1 67 ? 97.413 -30.662 34.304 1.00 72.91 ? 98 PRO B CB 1 ATOM 472 C CG . PRO A 1 67 ? 96.863 -30.833 32.976 1.00 72.62 ? 98 PRO B CG 1 ATOM 473 C CD . PRO A 1 67 ? 95.368 -30.750 33.082 1.00 71.92 ? 98 PRO B CD 1 ATOM 474 N N . ILE A 1 68 ? 97.198 -30.865 37.436 1.00 90.70 ? 99 ILE B N 1 ATOM 475 C CA . ILE A 1 68 ? 97.360 -30.124 38.664 1.00 90.66 ? 99 ILE B CA 1 ATOM 476 C C . ILE A 1 68 ? 98.587 -29.256 38.551 1.00 91.00 ? 99 ILE B C 1 ATOM 477 O O . ILE A 1 68 ? 98.904 -28.507 39.465 1.00 90.99 ? 99 ILE B O 1 ATOM 478 C CB . ILE A 1 68 ? 97.504 -31.048 39.872 1.00 91.12 ? 99 ILE B CB 1 ATOM 479 C CG1 . ILE A 1 68 ? 96.940 -32.442 39.555 1.00 91.47 ? 99 ILE B CG1 1 ATOM 480 C CG2 . ILE A 1 68 ? 96.820 -30.424 41.083 1.00 90.64 ? 99 ILE B CG2 1 ATOM 481 C CD1 . ILE A 1 68 ? 97.954 -33.442 38.968 1.00 92.31 ? 99 ILE B CD1 1 ATOM 482 N N . GLN A 1 69 ? 99.275 -29.350 37.422 1.00 68.56 ? 100 GLN B N 1 ATOM 483 C CA . GLN A 1 69 ? 100.453 -28.524 37.210 1.00 68.95 ? 100 GLN B CA 1 ATOM 484 C C . GLN A 1 69 ? 100.121 -27.186 36.559 1.00 68.51 ? 100 GLN B C 1 ATOM 485 O O . GLN A 1 69 ? 101.027 -26.456 36.150 1.00 68.93 ? 100 GLN B O 1 ATOM 486 C CB . GLN A 1 69 ? 101.555 -29.264 36.464 1.00 69.54 ? 100 GLN B CB 1 ATOM 487 C CG . GLN A 1 69 ? 102.311 -30.251 37.335 1.00 70.13 ? 100 GLN B CG 1 ATOM 488 C CD . GLN A 1 69 ? 101.775 -31.663 37.217 1.00 70.21 ? 100 GLN B CD 1 ATOM 489 O OE1 . GLN A 1 69 ? 100.753 -31.906 36.572 1.00 69.81 ? 100 GLN B OE1 1 ATOM 490 N NE2 . GLN A 1 69 ? 102.468 -32.605 37.836 1.00 70.76 ? 100 GLN B NE2 1 ATOM 491 N N . ILE A 1 70 ? 98.820 -26.894 36.434 1.00 65.48 ? 101 ILE B N 1 ATOM 492 C CA . ILE A 1 70 ? 98.346 -25.525 36.184 1.00 65.03 ? 101 ILE B CA 1 ATOM 493 C C . ILE A 1 70 ? 98.544 -24.729 37.488 1.00 64.92 ? 101 ILE B C 1 ATOM 494 O O . ILE A 1 70 ? 98.979 -25.279 38.504 1.00 65.27 ? 101 ILE B O 1 ATOM 495 C CB . ILE A 1 70 ? 96.830 -25.446 35.813 1.00 64.19 ? 101 ILE B CB 1 ATOM 496 C CG1 . ILE A 1 70 ? 96.350 -26.646 35.025 1.00 64.08 ? 101 ILE B CG1 1 ATOM 497 C CG2 . ILE A 1 70 ? 96.529 -24.241 34.975 1.00 64.06 ? 101 ILE B CG2 1 ATOM 498 C CD1 . ILE A 1 70 ? 94.995 -26.404 34.396 1.00 63.38 ? 101 ILE B CD1 1 ATOM 499 N N . ARG A 1 71 ? 98.214 -23.440 37.457 1.00 108.64 ? 102 ARG B N 1 ATOM 500 C CA . ARG A 1 71 ? 98.517 -22.500 38.544 1.00 108.55 ? 102 ARG B CA 1 ATOM 501 C C . ARG A 1 71 ? 100.026 -22.305 38.637 1.00 109.53 ? 102 ARG B C 1 ATOM 502 O O . ARG A 1 71 ? 100.522 -21.464 39.386 1.00 109.66 ? 102 ARG B O 1 ATOM 503 C CB . ARG A 1 71 ? 97.854 -22.887 39.886 1.00 107.98 ? 102 ARG B CB 1 ATOM 504 C CG . ARG A 1 71 ? 98.725 -23.630 40.894 1.00 108.60 ? 102 ARG B CG 1 ATOM 505 C CD . ARG A 1 71 ? 97.921 -24.714 41.613 1.00 108.35 ? 102 ARG B CD 1 ATOM 506 N NE . ARG A 1 71 ? 97.279 -24.237 42.839 1.00 107.92 ? 102 ARG B NE 1 ATOM 507 C CZ . ARG A 1 71 ? 96.325 -24.900 43.489 1.00 107.80 ? 102 ARG B CZ 1 ATOM 508 N NH1 . ARG A 1 71 ? 95.803 -24.401 44.601 1.00 107.65 ? 102 ARG B NH1 1 ATOM 509 N NH2 . ARG A 1 71 ? 95.889 -26.064 43.025 1.00 107.99 ? 102 ARG B NH2 1 ATOM 510 N N . TYR A 1 72 ? 100.741 -23.088 37.838 1.00 79.32 ? 103 TYR B N 1 ATOM 511 C CA . TYR A 1 72 ? 102.135 -22.851 37.565 1.00 80.23 ? 103 TYR B CA 1 ATOM 512 C C . TYR A 1 72 ? 102.249 -21.702 36.557 1.00 80.41 ? 103 TYR B C 1 ATOM 513 O O . TYR A 1 72 ? 103.263 -20.995 36.535 1.00 81.10 ? 103 TYR B O 1 ATOM 514 C CB . TYR A 1 72 ? 102.784 -24.113 37.018 1.00 80.75 ? 103 TYR B CB 1 ATOM 515 C CG . TYR A 1 72 ? 103.707 -24.810 37.981 1.00 81.29 ? 103 TYR B CG 1 ATOM 516 C CD1 . TYR A 1 72 ? 104.273 -24.131 39.044 1.00 81.50 ? 103 TYR B CD1 1 ATOM 517 C CD2 . TYR A 1 72 ? 104.026 -26.151 37.811 1.00 81.60 ? 103 TYR B CD2 1 ATOM 518 C CE1 . TYR A 1 72 ? 105.127 -24.769 39.922 1.00 82.03 ? 103 TYR B CE1 1 ATOM 519 C CE2 . TYR A 1 72 ? 104.882 -26.805 38.680 1.00 82.10 ? 103 TYR B CE2 1 ATOM 520 C CZ . TYR A 1 72 ? 105.433 -26.112 39.741 1.00 82.32 ? 103 TYR B CZ 1 ATOM 521 O OH . TYR A 1 72 ? 106.288 -26.771 40.614 1.00 82.85 ? 103 TYR B OH 1 ATOM 522 N N . LEU A 1 73 ? 101.221 -21.490 35.729 1.00 64.49 ? 104 LEU B N 1 ATOM 523 C CA . LEU A 1 73 ? 101.208 -20.257 34.942 1.00 64.70 ? 104 LEU B CA 1 ATOM 524 C C . LEU A 1 73 ? 100.273 -19.309 35.677 1.00 63.96 ? 104 LEU B C 1 ATOM 525 O O . LEU A 1 73 ? 99.043 -19.321 35.507 1.00 63.23 ? 104 LEU B O 1 ATOM 526 C CB . LEU A 1 73 ? 100.749 -20.496 33.494 1.00 64.75 ? 104 LEU B CB 1 ATOM 527 C CG . LEU A 1 73 ? 100.158 -21.866 33.135 1.00 64.38 ? 104 LEU B CG 1 ATOM 528 C CD1 . LEU A 1 73 ? 98.819 -22.055 33.779 1.00 63.47 ? 104 LEU B CD1 1 ATOM 529 C CD2 . LEU A 1 73 ? 100.048 -22.050 31.630 1.00 64.74 ? 104 LEU B CD2 1 ATOM 530 N N . SER A 1 74 ? 100.903 -18.434 36.450 1.00 81.69 ? 105 SER B N 1 ATOM 531 C CA . SER A 1 74 ? 100.192 -17.657 37.434 1.00 80.94 ? 105 SER B CA 1 ATOM 532 C C . SER A 1 74 ? 99.522 -16.472 36.782 1.00 80.81 ? 105 SER B C 1 ATOM 533 O O . SER A 1 74 ? 98.325 -16.268 36.964 1.00 80.00 ? 105 SER B O 1 ATOM 534 C CB . SER A 1 74 ? 101.123 -17.222 38.559 1.00 81.25 ? 105 SER B CB 1 ATOM 535 O OG . SER A 1 74 ? 100.375 -16.744 39.662 1.00 80.46 ? 105 SER B OG 1 ATOM 536 N N . SER A 1 75 ? 100.257 -15.727 35.959 1.00 71.57 ? 106 SER B N 1 ATOM 537 C CA . SER A 1 75 ? 99.611 -14.599 35.325 1.00 71.59 ? 106 SER B CA 1 ATOM 538 C C . SER A 1 75 ? 99.040 -15.225 34.096 1.00 71.63 ? 106 SER B C 1 ATOM 539 O O . SER A 1 75 ? 99.737 -15.466 33.118 1.00 72.43 ? 106 SER B O 1 ATOM 540 C CB . SER A 1 75 ? 100.632 -13.527 34.942 1.00 72.61 ? 106 SER B CB 1 ATOM 541 O OG . SER A 1 75 ? 101.961 -14.016 35.042 1.00 73.33 ? 106 SER B OG 1 ATOM 542 N N . LEU A 1 76 ? 97.750 -15.508 34.191 1.00 56.59 ? 107 LEU B N 1 ATOM 543 C CA . LEU A 1 76 ? 96.965 -16.075 33.116 1.00 56.59 ? 107 LEU B CA 1 ATOM 544 C C . LEU A 1 76 ? 95.622 -15.385 33.227 1.00 56.08 ? 107 LEU B C 1 ATOM 545 O O . LEU A 1 76 ? 94.965 -15.485 34.266 1.00 55.29 ? 107 LEU B O 1 ATOM 546 C CB . LEU A 1 76 ? 96.815 -17.590 33.289 1.00 56.09 ? 107 LEU B CB 1 ATOM 547 C CG . LEU A 1 76 ? 95.844 -18.245 32.306 1.00 55.94 ? 107 LEU B CG 1 ATOM 548 C CD1 . LEU A 1 76 ? 96.578 -18.720 31.069 1.00 56.88 ? 107 LEU B CD1 1 ATOM 549 C CD2 . LEU A 1 76 ? 95.078 -19.379 32.952 1.00 55.05 ? 107 LEU B CD2 1 ATOM 550 N N . LEU A 1 77 ? 95.223 -14.642 32.204 1.00 56.65 ? 108 LEU B N 1 ATOM 551 C CA . LEU A 1 77 ? 93.968 -13.928 32.299 1.00 56.34 ? 108 LEU B CA 1 ATOM 552 C C . LEU A 1 77 ? 92.810 -14.579 31.553 1.00 56.05 ? 108 LEU B C 1 ATOM 553 O O . LEU A 1 77 ? 91.669 -14.137 31.672 1.00 55.76 ? 108 LEU B O 1 ATOM 554 C CB . LEU A 1 77 ? 94.163 -12.493 31.859 1.00 57.20 ? 108 LEU B CB 1 ATOM 555 C CG . LEU A 1 77 ? 95.646 -12.175 31.856 1.00 57.92 ? 108 LEU B CG 1 ATOM 556 C CD1 . LEU A 1 77 ? 95.884 -10.980 30.981 1.00 59.04 ? 108 LEU B CD1 1 ATOM 557 C CD2 . LEU A 1 77 ? 96.189 -11.926 33.249 1.00 57.47 ? 108 LEU B CD2 1 ATOM 558 N N . TYR A 1 78 ? 93.075 -15.631 30.798 1.00 63.56 ? 109 TYR B N 1 ATOM 559 C CA . TYR A 1 78 ? 92.019 -16.175 29.962 1.00 63.36 ? 109 TYR B CA 1 ATOM 560 C C . TYR A 1 78 ? 92.117 -17.677 29.871 1.00 63.08 ? 109 TYR B C 1 ATOM 561 O O . TYR A 1 78 ? 93.180 -18.208 29.560 1.00 63.52 ? 109 TYR B O 1 ATOM 562 C CB . TYR A 1 78 ? 92.090 -15.549 28.570 1.00 64.16 ? 109 TYR B CB 1 ATOM 563 C CG . TYR A 1 78 ? 91.079 -16.077 27.575 1.00 64.08 ? 109 TYR B CG 1 ATOM 564 C CD1 . TYR A 1 78 ? 91.327 -17.231 26.843 1.00 64.18 ? 109 TYR B CD1 1 ATOM 565 C CD2 . TYR A 1 78 ? 89.886 -15.411 27.343 1.00 63.94 ? 109 TYR B CD2 1 ATOM 566 C CE1 . TYR A 1 78 ? 90.408 -17.718 25.918 1.00 64.11 ? 109 TYR B CE1 1 ATOM 567 C CE2 . TYR A 1 78 ? 88.957 -15.894 26.410 1.00 63.93 ? 109 TYR B CE2 1 ATOM 568 C CZ . TYR A 1 78 ? 89.229 -17.047 25.705 1.00 63.99 ? 109 TYR B CZ 1 ATOM 569 O OH . TYR A 1 78 ? 88.325 -17.529 24.789 1.00 63.96 ? 109 TYR B OH 1 ATOM 570 N N . LEU A 1 79 ? 91.008 -18.365 30.117 1.00 57.77 ? 110 LEU B N 1 ATOM 571 C CA . LEU A 1 79 ? 90.979 -19.808 29.946 1.00 57.48 ? 110 LEU B CA 1 ATOM 572 C C . LEU A 1 79 ? 89.711 -20.254 29.258 1.00 57.18 ? 110 LEU B C 1 ATOM 573 O O . LEU A 1 79 ? 88.625 -20.105 29.796 1.00 56.61 ? 110 LEU B O 1 ATOM 574 C CB . LEU A 1 79 ? 91.081 -20.507 31.293 1.00 56.83 ? 110 LEU B CB 1 ATOM 575 C CG . LEU A 1 79 ? 91.690 -21.898 31.175 1.00 56.88 ? 110 LEU B CG 1 ATOM 576 C CD1 . LEU A 1 79 ? 93.184 -21.733 31.108 1.00 57.66 ? 110 LEU B CD1 1 ATOM 577 C CD2 . LEU A 1 79 ? 91.286 -22.816 32.313 1.00 56.20 ? 110 LEU B CD2 1 ATOM 578 N N . ASN A 1 80 ? 89.844 -20.842 28.085 1.00 61.14 ? 111 ASN B N 1 ATOM 579 C CA . ASN A 1 80 ? 88.674 -21.285 27.366 1.00 60.95 ? 111 ASN B CA 1 ATOM 580 C C . ASN A 1 80 ? 88.838 -22.755 27.040 1.00 60.81 ? 111 ASN B C 1 ATOM 581 O O . ASN A 1 80 ? 89.789 -23.125 26.366 1.00 61.28 ? 111 ASN B O 1 ATOM 582 C CB . ASN A 1 80 ? 88.520 -20.452 26.086 1.00 61.61 ? 111 ASN B CB 1 ATOM 583 C CG . ASN A 1 80 ? 87.113 -20.529 25.477 1.00 61.44 ? 111 ASN B CG 1 ATOM 584 O OD1 . ASN A 1 80 ? 86.478 -21.594 25.495 1.00 61.00 ? 111 ASN B OD1 1 ATOM 585 N ND2 . ASN A 1 80 ? 86.623 -19.386 24.928 1.00 61.88 ? 111 ASN B ND2 1 ATOM 586 N N . LEU A 1 81 ? 87.954 -23.598 27.573 1.00 55.22 ? 112 LEU B N 1 ATOM 587 C CA . LEU A 1 81 ? 87.836 -24.992 27.128 1.00 55.10 ? 112 LEU B CA 1 ATOM 588 C C . LEU A 1 81 ? 86.379 -25.338 26.800 1.00 54.71 ? 112 LEU B C 1 ATOM 589 O O . LEU A 1 81 ? 85.607 -25.613 27.715 1.00 54.08 ? 112 LEU B O 1 ATOM 590 C CB . LEU A 1 81 ? 88.305 -25.934 28.246 1.00 54.67 ? 112 LEU B CB 1 ATOM 591 C CG . LEU A 1 81 ? 89.316 -25.345 29.231 1.00 54.72 ? 112 LEU B CG 1 ATOM 592 C CD1 . LEU A 1 81 ? 89.254 -26.040 30.563 1.00 54.17 ? 112 LEU B CD1 1 ATOM 593 C CD2 . LEU A 1 81 ? 90.718 -25.417 28.690 1.00 55.47 ? 112 LEU B CD2 1 ATOM 594 N N . SER A 1 82 ? 86.031 -25.457 25.516 1.00 57.88 ? 113 SER B N 1 ATOM 595 C CA . SER A 1 82 ? 84.630 -25.663 25.124 1.00 57.67 ? 113 SER B CA 1 ATOM 596 C C . SER A 1 82 ? 84.334 -26.888 24.235 1.00 57.68 ? 113 SER B C 1 ATOM 597 O O . SER A 1 82 ? 85.103 -27.241 23.336 1.00 58.04 ? 113 SER B O 1 ATOM 598 C CB . SER A 1 82 ? 84.068 -24.398 24.476 1.00 58.03 ? 113 SER B CB 1 ATOM 599 O OG . SER A 1 82 ? 84.172 -23.317 25.364 1.00 57.93 ? 113 SER B OG 1 ATOM 600 N N . GLY A 1 83 ? 83.225 -27.556 24.531 1.00 87.68 ? 114 GLY B N 1 ATOM 601 C CA . GLY A 1 83 ? 82.663 -28.568 23.652 1.00 87.69 ? 114 GLY B CA 1 ATOM 602 C C . GLY A 1 83 ? 83.386 -29.886 23.773 1.00 87.58 ? 114 GLY B C 1 ATOM 603 O O . GLY A 1 83 ? 82.853 -30.954 23.457 1.00 87.46 ? 114 GLY B O 1 ATOM 604 N N . ASN A 1 84 ? 84.611 -29.789 24.270 1.00 72.80 ? 115 ASN B N 1 ATOM 605 C CA . ASN A 1 84 ? 85.444 -30.936 24.538 1.00 72.87 ? 115 ASN B CA 1 ATOM 606 C C . ASN A 1 84 ? 84.738 -31.757 25.595 1.00 72.55 ? 115 ASN B C 1 ATOM 607 O O . ASN A 1 84 ? 84.382 -31.235 26.638 1.00 72.32 ? 115 ASN B O 1 ATOM 608 C CB . ASN A 1 84 ? 86.795 -30.450 25.057 1.00 73.14 ? 115 ASN B CB 1 ATOM 609 C CG . ASN A 1 84 ? 87.312 -29.242 24.291 1.00 73.53 ? 115 ASN B CG 1 ATOM 610 O OD1 . ASN A 1 84 ? 87.144 -29.143 23.079 1.00 73.91 ? 115 ASN B OD1 1 ATOM 611 N ND2 . ASN A 1 84 ? 87.937 -28.316 24.998 1.00 73.52 ? 115 ASN B ND2 1 ATOM 612 N N . SER A 1 85 ? 84.530 -33.039 25.351 1.00 93.70 ? 116 SER B N 1 ATOM 613 C CA . SER A 1 85 ? 83.744 -33.780 26.308 1.00 93.51 ? 116 SER B CA 1 ATOM 614 C C . SER A 1 85 ? 84.719 -34.320 27.335 1.00 93.78 ? 116 SER B C 1 ATOM 615 O O . SER A 1 85 ? 85.510 -35.202 27.043 1.00 94.23 ? 116 SER B O 1 ATOM 616 C CB . SER A 1 85 ? 82.989 -34.918 25.615 1.00 93.61 ? 116 SER B CB 1 ATOM 617 O OG . SER A 1 85 ? 82.062 -35.538 26.494 1.00 93.53 ? 116 SER B OG 1 ATOM 618 N N . LEU A 1 86 ? 84.669 -33.752 28.537 1.00 61.03 ? 117 LEU B N 1 ATOM 619 C CA . LEU A 1 86 ? 85.483 -34.198 29.662 1.00 61.33 ? 117 LEU B CA 1 ATOM 620 C C . LEU A 1 86 ? 84.691 -34.015 30.945 1.00 61.19 ? 117 LEU B C 1 ATOM 621 O O . LEU A 1 86 ? 84.071 -32.976 31.166 1.00 60.83 ? 117 LEU B O 1 ATOM 622 C CB . LEU A 1 86 ? 86.852 -33.485 29.702 1.00 61.55 ? 117 LEU B CB 1 ATOM 623 C CG . LEU A 1 86 ? 87.162 -32.043 30.120 1.00 61.14 ? 117 LEU B CG 1 ATOM 624 C CD1 . LEU A 1 86 ? 88.476 -31.564 29.515 1.00 61.63 ? 117 LEU B CD1 1 ATOM 625 C CD2 . LEU A 1 86 ? 86.074 -31.149 29.712 1.00 60.46 ? 117 LEU B CD2 1 ATOM 626 N N . GLU A 1 87 ? 84.699 -35.035 31.784 1.00 73.04 ? 118 GLU B N 1 ATOM 627 C CA . GLU A 1 87 ? 83.811 -35.043 32.928 1.00 73.13 ? 118 GLU B CA 1 ATOM 628 C C . GLU A 1 87 ? 84.688 -35.128 34.154 1.00 73.35 ? 118 GLU B C 1 ATOM 629 O O . GLU A 1 87 ? 85.876 -35.423 34.044 1.00 73.63 ? 118 GLU B O 1 ATOM 630 C CB . GLU A 1 87 ? 82.768 -36.181 32.802 1.00 73.65 ? 118 GLU B CB 1 ATOM 631 C CG . GLU A 1 87 ? 82.527 -37.102 34.010 1.00 74.51 ? 118 GLU B CG 1 ATOM 632 C CD . GLU A 1 87 ? 81.410 -36.630 34.942 1.00 74.54 ? 118 GLU B CD 1 ATOM 633 O OE1 . GLU A 1 87 ? 80.248 -37.071 34.770 1.00 74.76 ? 118 GLU B OE1 1 ATOM 634 O OE2 . GLU A 1 87 ? 81.711 -35.834 35.857 1.00 74.47 ? 118 GLU B OE2 1 ATOM 635 N N . GLY A 1 88 ? 84.118 -34.778 35.301 1.00 72.11 ? 119 GLY B N 1 ATOM 636 C CA . GLY A 1 88 ? 84.788 -34.888 36.575 1.00 72.48 ? 119 GLY B CA 1 ATOM 637 C C . GLY A 1 88 ? 83.946 -34.158 37.585 1.00 72.67 ? 119 GLY B C 1 ATOM 638 O O . GLY A 1 88 ? 82.815 -33.756 37.297 1.00 72.39 ? 119 GLY B O 1 ATOM 639 N N . SER A 1 89 ? 84.473 -34.033 38.791 1.00 87.15 ? 120 SER B N 1 ATOM 640 C CA . SER A 1 89 ? 84.042 -32.970 39.655 1.00 87.42 ? 120 SER B CA 1 ATOM 641 C C . SER A 1 89 ? 84.902 -31.878 39.090 1.00 86.64 ? 120 SER B C 1 ATOM 642 O O . SER A 1 89 ? 86.017 -32.140 38.631 1.00 86.98 ? 120 SER B O 1 ATOM 643 C CB . SER A 1 89 ? 84.444 -33.246 41.091 1.00 88.47 ? 120 SER B CB 1 ATOM 644 O OG . SER A 1 89 ? 85.852 -33.215 41.205 1.00 88.41 ? 120 SER B OG 1 ATOM 645 N N . PHE A 1 90 ? 84.384 -30.665 39.075 1.00 69.37 ? 121 PHE B N 1 ATOM 646 C CA . PHE A 1 90 ? 85.176 -29.555 38.585 1.00 68.68 ? 121 PHE B CA 1 ATOM 647 C C . PHE A 1 90 ? 86.431 -29.421 39.454 1.00 68.90 ? 121 PHE B C 1 ATOM 648 O O . PHE A 1 90 ? 86.364 -29.605 40.665 1.00 69.50 ? 121 PHE B O 1 ATOM 649 C CB . PHE A 1 90 ? 84.328 -28.289 38.615 1.00 68.29 ? 121 PHE B CB 1 ATOM 650 C CG . PHE A 1 90 ? 85.063 -27.055 38.210 1.00 67.77 ? 121 PHE B CG 1 ATOM 651 C CD1 . PHE A 1 90 ? 85.672 -26.971 36.979 1.00 67.83 ? 121 PHE B CD1 1 ATOM 652 C CD2 . PHE A 1 90 ? 85.104 -25.957 39.045 1.00 67.38 ? 121 PHE B CD2 1 ATOM 653 C CE1 . PHE A 1 90 ? 86.351 -25.831 36.604 1.00 67.56 ? 121 PHE B CE1 1 ATOM 654 C CE2 . PHE A 1 90 ? 85.767 -24.810 38.673 1.00 67.16 ? 121 PHE B CE2 1 ATOM 655 C CZ . PHE A 1 90 ? 86.393 -24.743 37.454 1.00 67.27 ? 121 PHE B CZ 1 ATOM 656 N N . PRO A 1 91 ? 87.591 -29.165 38.838 1.00 69.80 ? 122 PRO B N 1 ATOM 657 C CA . PRO A 1 91 ? 88.857 -28.918 39.542 1.00 70.16 ? 122 PRO B CA 1 ATOM 658 C C . PRO A 1 91 ? 88.812 -27.680 40.404 1.00 69.95 ? 122 PRO B C 1 ATOM 659 O O . PRO A 1 91 ? 88.392 -26.635 39.925 1.00 69.49 ? 122 PRO B O 1 ATOM 660 C CB . PRO A 1 91 ? 89.835 -28.646 38.399 1.00 70.06 ? 122 PRO B CB 1 ATOM 661 C CG . PRO A 1 91 ? 88.968 -28.325 37.222 1.00 69.54 ? 122 PRO B CG 1 ATOM 662 C CD . PRO A 1 91 ? 87.810 -29.242 37.393 1.00 69.51 ? 122 PRO B CD 1 ATOM 663 N N . THR A 1 92 ? 89.265 -27.781 41.646 1.00 64.84 ? 123 THR B N 1 ATOM 664 C CA . THR A 1 92 ? 89.283 -26.625 42.526 1.00 64.64 ? 123 THR B CA 1 ATOM 665 C C . THR A 1 92 ? 90.583 -25.912 42.291 1.00 64.48 ? 123 THR B C 1 ATOM 666 O O . THR A 1 92 ? 90.814 -24.817 42.786 1.00 64.20 ? 123 THR B O 1 ATOM 667 C CB . THR A 1 92 ? 89.216 -27.038 43.987 1.00 65.47 ? 123 THR B CB 1 ATOM 668 O OG1 . THR A 1 92 ? 88.912 -28.439 44.073 1.00 66.30 ? 123 THR B OG1 1 ATOM 669 C CG2 . THR A 1 92 ? 88.145 -26.224 44.713 1.00 65.31 ? 123 THR B CG2 1 ATOM 670 N N . SER A 1 93 ? 91.430 -26.565 41.513 1.00 64.78 ? 124 SER B N 1 ATOM 671 C CA . SER A 1 93 ? 92.757 -26.073 41.187 1.00 64.96 ? 124 SER B CA 1 ATOM 672 C C . SER A 1 93 ? 92.690 -24.764 40.422 1.00 64.48 ? 124 SER B C 1 ATOM 673 O O . SER A 1 93 ? 93.471 -23.847 40.647 1.00 64.54 ? 124 SER B O 1 ATOM 674 C CB . SER A 1 93 ? 93.457 -27.126 40.339 1.00 65.49 ? 124 SER B CB 1 ATOM 675 O OG . SER A 1 93 ? 92.491 -28.019 39.792 1.00 65.45 ? 124 SER B OG 1 ATOM 676 N N . ILE A 1 94 ? 91.731 -24.694 39.516 1.00 55.66 ? 125 ILE B N 1 ATOM 677 C CA . ILE A 1 94 ? 91.558 -23.544 38.641 1.00 55.41 ? 125 ILE B CA 1 ATOM 678 C C . ILE A 1 94 ? 91.247 -22.269 39.425 1.00 55.06 ? 125 ILE B C 1 ATOM 679 O O . ILE A 1 94 ? 91.603 -21.167 38.994 1.00 55.11 ? 125 ILE B O 1 ATOM 680 C CB . ILE A 1 94 ? 90.467 -23.841 37.586 1.00 55.21 ? 125 ILE B CB 1 ATOM 681 C CG1 . ILE A 1 94 ? 91.107 -24.089 36.230 1.00 55.61 ? 125 ILE B CG1 1 ATOM 682 C CG2 . ILE A 1 94 ? 89.413 -22.741 37.521 1.00 54.77 ? 125 ILE B CG2 1 ATOM 683 C CD1 . ILE A 1 94 ? 90.422 -25.165 35.477 1.00 55.59 ? 125 ILE B CD1 1 ATOM 684 N N . PHE A 1 95 ? 90.608 -22.422 40.586 1.00 56.00 ? 126 PHE B N 1 ATOM 685 C CA . PHE A 1 95 ? 90.264 -21.276 41.419 1.00 55.73 ? 126 PHE B CA 1 ATOM 686 C C . PHE A 1 95 ? 91.523 -20.619 41.934 1.00 55.99 ? 126 PHE B C 1 ATOM 687 O O . PHE A 1 95 ? 91.493 -19.492 42.398 1.00 55.83 ? 126 PHE B O 1 ATOM 688 C CB . PHE A 1 95 ? 89.412 -21.682 42.623 1.00 55.73 ? 126 PHE B CB 1 ATOM 689 C CG . PHE A 1 95 ? 88.075 -22.255 42.268 1.00 55.60 ? 126 PHE B CG 1 ATOM 690 C CD1 . PHE A 1 95 ? 87.374 -21.796 41.181 1.00 55.26 ? 126 PHE B CD1 1 ATOM 691 C CD2 . PHE A 1 95 ? 87.523 -23.267 43.038 1.00 56.00 ? 126 PHE B CD2 1 ATOM 692 C CE1 . PHE A 1 95 ? 86.147 -22.332 40.866 1.00 55.20 ? 126 PHE B CE1 1 ATOM 693 C CE2 . PHE A 1 95 ? 86.292 -23.810 42.731 1.00 56.00 ? 126 PHE B CE2 1 ATOM 694 C CZ . PHE A 1 95 ? 85.601 -23.335 41.644 1.00 55.52 ? 126 PHE B CZ 1 ATOM 695 N N . ASP A 1 96 ? 92.635 -21.328 41.887 1.00 78.61 ? 127 ASP B N 1 ATOM 696 C CA . ASP A 1 96 ? 93.853 -20.754 42.415 1.00 78.98 ? 127 ASP B CA 1 ATOM 697 C C . ASP A 1 96 ? 94.677 -20.068 41.346 1.00 79.27 ? 127 ASP B C 1 ATOM 698 O O . ASP A 1 96 ? 95.824 -19.719 41.580 1.00 79.75 ? 127 ASP B O 1 ATOM 699 C CB . ASP A 1 96 ? 94.630 -21.750 43.270 1.00 79.57 ? 127 ASP B CB 1 ATOM 700 C CG . ASP A 1 96 ? 93.955 -21.994 44.632 1.00 79.66 ? 127 ASP B CG 1 ATOM 701 O OD1 . ASP A 1 96 ? 94.165 -21.173 45.562 1.00 79.86 ? 127 ASP B OD1 1 ATOM 702 O OD2 . ASP A 1 96 ? 93.207 -22.995 44.773 1.00 79.67 ? 127 ASP B OD2 1 ATOM 703 N N . LEU A 1 97 ? 94.090 -19.924 40.160 1.00 67.96 ? 128 LEU B N 1 ATOM 704 C CA . LEU A 1 97 ? 94.660 -19.098 39.089 1.00 68.39 ? 128 LEU B CA 1 ATOM 705 C C . LEU A 1 97 ? 94.601 -17.593 39.380 1.00 68.28 ? 128 LEU B C 1 ATOM 706 O O . LEU A 1 97 ? 95.612 -16.911 39.300 1.00 68.81 ? 128 LEU B O 1 ATOM 707 C CB . LEU A 1 97 ? 93.976 -19.378 37.758 1.00 68.40 ? 128 LEU B CB 1 ATOM 708 C CG . LEU A 1 97 ? 94.664 -20.286 36.718 1.00 69.05 ? 128 LEU B CG 1 ATOM 709 C CD1 . LEU A 1 97 ? 96.184 -20.322 36.878 1.00 69.81 ? 128 LEU B CD1 1 ATOM 710 C CD2 . LEU A 1 97 ? 94.070 -21.689 36.695 1.00 68.80 ? 128 LEU B CD2 1 ATOM 711 N N . THR A 1 98 ? 93.414 -17.074 39.679 1.00 76.63 ? 129 THR B N 1 ATOM 712 C CA . THR A 1 98 ? 93.235 -15.759 40.337 1.00 76.41 ? 129 THR B CA 1 ATOM 713 C C . THR A 1 98 ? 93.608 -14.469 39.605 1.00 76.88 ? 129 THR B C 1 ATOM 714 O O . THR A 1 98 ? 93.206 -13.402 40.046 1.00 76.68 ? 129 THR B O 1 ATOM 715 C CB . THR A 1 98 ? 93.959 -15.644 41.709 1.00 76.30 ? 129 THR B CB 1 ATOM 716 O OG1 . THR A 1 98 ? 95.326 -15.274 41.502 1.00 76.94 ? 129 THR B OG1 1 ATOM 717 C CG2 . THR A 1 98 ? 93.876 -16.931 42.504 1.00 76.14 ? 129 THR B CG2 1 ATOM 718 N N . LYS A 1 99 ? 94.376 -14.510 38.526 1.00 84.45 ? 130 LYS B N 1 ATOM 719 C CA . LYS A 1 99 ? 94.498 -13.283 37.754 1.00 85.00 ? 130 LYS B CA 1 ATOM 720 C C . LYS A 1 99 ? 93.540 -13.385 36.587 1.00 85.06 ? 130 LYS B C 1 ATOM 721 O O . LYS A 1 99 ? 93.341 -12.431 35.842 1.00 85.51 ? 130 LYS B O 1 ATOM 722 C CB . LYS A 1 99 ? 95.930 -13.003 37.312 1.00 85.97 ? 130 LYS B CB 1 ATOM 723 C CG . LYS A 1 99 ? 96.129 -11.585 36.769 1.00 86.62 ? 130 LYS B CG 1 ATOM 724 C CD . LYS A 1 99 ? 95.336 -10.535 37.557 1.00 86.07 ? 130 LYS B CD 1 ATOM 725 C CE . LYS A 1 99 ? 94.353 -9.746 36.682 1.00 86.20 ? 130 LYS B CE 1 ATOM 726 N NZ . LYS A 1 99 ? 94.952 -9.248 35.411 1.00 87.21 ? 130 LYS B NZ 1 ATOM 727 N N . LEU A 1 100 ? 92.913 -14.551 36.472 1.00 69.81 ? 131 LEU B N 1 ATOM 728 C CA . LEU A 1 100 ? 91.905 -14.780 35.454 1.00 69.78 ? 131 LEU B CA 1 ATOM 729 C C . LEU A 1 100 ? 90.868 -13.680 35.504 1.00 69.60 ? 131 LEU B C 1 ATOM 730 O O . LEU A 1 100 ? 90.332 -13.371 36.576 1.00 69.02 ? 131 LEU B O 1 ATOM 731 C CB . LEU A 1 100 ? 91.166 -16.080 35.730 1.00 69.17 ? 131 LEU B CB 1 ATOM 732 C CG . LEU A 1 100 ? 91.838 -17.427 35.586 1.00 69.28 ? 131 LEU B CG 1 ATOM 733 C CD1 . LEU A 1 100 ? 90.976 -18.446 36.321 1.00 68.60 ? 131 LEU B CD1 1 ATOM 734 C CD2 . LEU A 1 100 ? 91.972 -17.771 34.105 1.00 69.85 ? 131 LEU B CD2 1 ATOM 735 N N . THR A 1 101 ? 90.625 -13.047 34.362 1.00 56.30 ? 132 THR B N 1 ATOM 736 C CA . THR A 1 101 ? 89.395 -12.300 34.208 1.00 56.36 ? 132 THR B CA 1 ATOM 737 C C . THR A 1 101 ? 88.313 -13.076 33.455 1.00 56.16 ? 132 THR B C 1 ATOM 738 O O . THR A 1 101 ? 87.140 -12.730 33.559 1.00 56.06 ? 132 THR B O 1 ATOM 739 C CB . THR A 1 101 ? 89.629 -10.886 33.613 1.00 57.27 ? 132 THR B CB 1 ATOM 740 O OG1 . THR A 1 101 ? 90.471 -10.965 32.453 1.00 58.02 ? 132 THR B OG1 1 ATOM 741 C CG2 . THR A 1 101 ? 90.275 -9.974 34.655 1.00 57.33 ? 132 THR B CG2 1 ATOM 742 N N . THR A 1 102 ? 88.681 -14.160 32.774 1.00 54.42 ? 133 THR B N 1 ATOM 743 C CA . THR A 1 102 ? 87.722 -14.871 31.897 1.00 54.29 ? 133 THR B CA 1 ATOM 744 C C . THR A 1 102 ? 87.819 -16.410 31.901 1.00 53.68 ? 133 THR B C 1 ATOM 745 O O . THR A 1 102 ? 88.886 -16.978 31.673 1.00 53.85 ? 133 THR B O 1 ATOM 746 C CB . THR A 1 102 ? 87.844 -14.405 30.424 1.00 55.21 ? 133 THR B CB 1 ATOM 747 O OG1 . THR A 1 102 ? 87.827 -12.976 30.357 1.00 55.94 ? 133 THR B OG1 1 ATOM 748 C CG2 . THR A 1 102 ? 86.712 -14.959 29.592 1.00 55.13 ? 133 THR B CG2 1 ATOM 749 N N . LEU A 1 103 ? 86.715 -17.100 32.138 1.00 53.28 ? 134 LEU B N 1 ATOM 750 C CA . LEU A 1 103 ? 86.792 -18.552 32.173 1.00 52.83 ? 134 LEU B CA 1 ATOM 751 C C . LEU A 1 103 ? 85.630 -19.261 31.484 1.00 52.67 ? 134 LEU B C 1 ATOM 752 O O . LEU A 1 103 ? 84.498 -19.216 31.959 1.00 52.34 ? 134 LEU B O 1 ATOM 753 C CB . LEU A 1 103 ? 86.825 -18.976 33.623 1.00 52.20 ? 134 LEU B CB 1 ATOM 754 C CG . LEU A 1 103 ? 87.142 -20.424 33.892 1.00 51.85 ? 134 LEU B CG 1 ATOM 755 C CD1 . LEU A 1 103 ? 88.636 -20.582 33.918 1.00 52.18 ? 134 LEU B CD1 1 ATOM 756 C CD2 . LEU A 1 103 ? 86.527 -20.778 35.218 1.00 51.29 ? 134 LEU B CD2 1 ATOM 757 N N . ASP A 1 104 ? 85.891 -19.974 30.404 1.00 62.55 ? 135 ASP B N 1 ATOM 758 C CA . ASP A 1 104 ? 84.794 -20.671 29.776 1.00 62.45 ? 135 ASP B CA 1 ATOM 759 C C . ASP A 1 104 ? 85.040 -22.169 29.891 1.00 62.17 ? 135 ASP B C 1 ATOM 760 O O . ASP A 1 104 ? 85.960 -22.694 29.289 1.00 62.46 ? 135 ASP B O 1 ATOM 761 C CB . ASP A 1 104 ? 84.621 -20.214 28.323 1.00 63.07 ? 135 ASP B CB 1 ATOM 762 C CG . ASP A 1 104 ? 83.342 -20.750 27.691 1.00 63.00 ? 135 ASP B CG 1 ATOM 763 O OD1 . ASP A 1 104 ? 82.836 -21.771 28.200 1.00 62.50 ? 135 ASP B OD1 1 ATOM 764 O OD2 . ASP A 1 104 ? 82.841 -20.176 26.690 1.00 63.50 ? 135 ASP B OD2 1 ATOM 765 N N . ILE A 1 105 ? 84.259 -22.838 30.725 1.00 61.21 ? 136 ILE B N 1 ATOM 766 C CA . ILE A 1 105 ? 84.262 -24.296 30.810 1.00 61.03 ? 136 ILE B CA 1 ATOM 767 C C . ILE A 1 105 ? 83.103 -24.975 30.063 1.00 61.01 ? 136 ILE B C 1 ATOM 768 O O . ILE A 1 105 ? 82.771 -26.131 30.353 1.00 60.81 ? 136 ILE B O 1 ATOM 769 C CB . ILE A 1 105 ? 84.446 -24.829 32.246 1.00 60.70 ? 136 ILE B CB 1 ATOM 770 C CG1 . ILE A 1 105 ? 83.307 -24.381 33.149 1.00 60.42 ? 136 ILE B CG1 1 ATOM 771 C CG2 . ILE A 1 105 ? 85.759 -24.358 32.808 1.00 60.82 ? 136 ILE B CG2 1 ATOM 772 C CD1 . ILE A 1 105 ? 83.257 -25.125 34.462 1.00 60.17 ? 136 ILE B CD1 1 ATOM 773 N N . SER A 1 106 ? 82.419 -24.220 29.203 1.00 55.03 ? 137 SER B N 1 ATOM 774 C CA . SER A 1 106 ? 81.139 -24.649 28.613 1.00 55.03 ? 137 SER B CA 1 ATOM 775 C C . SER A 1 106 ? 81.087 -25.811 27.605 1.00 55.13 ? 137 SER B C 1 ATOM 776 O O . SER A 1 106 ? 82.039 -26.081 26.873 1.00 55.38 ? 137 SER B O 1 ATOM 777 C CB . SER A 1 106 ? 80.448 -23.458 27.969 1.00 55.41 ? 137 SER B CB 1 ATOM 778 O OG . SER A 1 106 ? 81.294 -22.899 26.981 1.00 55.93 ? 137 SER B OG 1 ATOM 779 N N . ARG A 1 107 ? 79.917 -26.447 27.555 1.00 69.82 ? 138 ARG B N 1 ATOM 780 C CA . ARG A 1 107 ? 79.607 -27.549 26.636 1.00 69.91 ? 138 ARG B CA 1 ATOM 781 C C . ARG A 1 107 ? 80.349 -28.872 26.898 1.00 69.76 ? 138 ARG B C 1 ATOM 782 O O . ARG A 1 107 ? 80.516 -29.704 26.012 1.00 69.95 ? 138 ARG B O 1 ATOM 783 C CB . ARG A 1 107 ? 79.767 -27.088 25.176 1.00 70.35 ? 138 ARG B CB 1 ATOM 784 C CG . ARG A 1 107 ? 78.928 -25.847 24.816 1.00 70.68 ? 138 ARG B CG 1 ATOM 785 C CD . ARG A 1 107 ? 78.913 -25.534 23.320 1.00 71.23 ? 138 ARG B CD 1 ATOM 786 N NE . ARG A 1 107 ? 77.949 -24.484 23.005 1.00 71.63 ? 138 ARG B NE 1 ATOM 787 C CZ . ARG A 1 107 ? 76.662 -24.712 22.768 1.00 71.73 ? 138 ARG B CZ 1 ATOM 788 N NH1 . ARG A 1 107 ? 76.202 -25.954 22.811 1.00 71.44 ? 138 ARG B NH1 1 ATOM 789 N NH2 . ARG A 1 107 ? 75.838 -23.705 22.487 1.00 72.16 ? 138 ARG B NH2 1 ATOM 790 N N . ASN A 1 108 ? 80.752 -29.084 28.137 1.00 66.34 ? 139 ASN B N 1 ATOM 791 C CA . ASN A 1 108 ? 81.587 -30.220 28.469 1.00 66.35 ? 139 ASN B CA 1 ATOM 792 C C . ASN A 1 108 ? 80.808 -31.158 29.385 1.00 66.32 ? 139 ASN B C 1 ATOM 793 O O . ASN A 1 108 ? 79.600 -31.008 29.540 1.00 66.27 ? 139 ASN B O 1 ATOM 794 C CB . ASN A 1 108 ? 82.895 -29.743 29.092 1.00 66.34 ? 139 ASN B CB 1 ATOM 795 C CG . ASN A 1 108 ? 83.732 -28.910 28.127 1.00 66.60 ? 139 ASN B CG 1 ATOM 796 O OD1 . ASN A 1 108 ? 84.951 -28.998 28.107 1.00 66.82 ? 139 ASN B OD1 1 ATOM 797 N ND2 . ASN A 1 108 ? 83.078 -28.115 27.308 1.00 66.75 ? 139 ASN B ND2 1 ATOM 798 N N . SER A 1 109 ? 81.459 -32.171 29.931 1.00 58.52 ? 140 SER B N 1 ATOM 799 C CA . SER A 1 109 ? 80.746 -33.127 30.775 1.00 58.72 ? 140 SER B CA 1 ATOM 800 C C . SER A 1 109 ? 80.836 -33.033 32.318 1.00 58.94 ? 140 SER B C 1 ATOM 801 O O . SER A 1 109 ? 80.332 -33.929 32.994 1.00 59.40 ? 140 SER B O 1 ATOM 802 C CB . SER A 1 109 ? 80.922 -34.566 30.256 1.00 59.06 ? 140 SER B CB 1 ATOM 803 O OG . SER A 1 109 ? 79.939 -34.875 29.275 1.00 58.89 ? 140 SER B OG 1 ATOM 804 N N . PHE A 1 110 ? 81.468 -31.990 32.864 1.00 62.33 ? 141 PHE B N 1 ATOM 805 C CA . PHE A 1 110 ? 81.757 -31.904 34.308 1.00 62.58 ? 141 PHE B CA 1 ATOM 806 C C . PHE A 1 110 ? 80.542 -32.217 35.163 1.00 62.99 ? 141 PHE B C 1 ATOM 807 O O . PHE A 1 110 ? 79.450 -31.813 34.822 1.00 62.83 ? 141 PHE B O 1 ATOM 808 C CB . PHE A 1 110 ? 82.169 -30.490 34.682 1.00 62.20 ? 141 PHE B CB 1 ATOM 809 C CG . PHE A 1 110 ? 83.493 -30.077 34.155 1.00 62.04 ? 141 PHE B CG 1 ATOM 810 C CD1 . PHE A 1 110 ? 83.635 -29.662 32.847 1.00 61.93 ? 141 PHE B CD1 1 ATOM 811 C CD2 . PHE A 1 110 ? 84.600 -30.060 34.976 1.00 62.19 ? 141 PHE B CD2 1 ATOM 812 C CE1 . PHE A 1 110 ? 84.868 -29.261 32.362 1.00 62.01 ? 141 PHE B CE1 1 ATOM 813 C CE2 . PHE A 1 110 ? 85.838 -29.659 34.493 1.00 62.19 ? 141 PHE B CE2 1 ATOM 814 C CZ . PHE A 1 110 ? 85.969 -29.264 33.187 1.00 62.14 ? 141 PHE B CZ 1 ATOM 815 N N . ASP A 1 111 ? 80.711 -32.922 36.276 1.00 70.45 ? 142 ASP B N 1 ATOM 816 C CA . ASP A 1 111 ? 79.540 -33.280 37.075 1.00 71.16 ? 142 ASP B CA 1 ATOM 817 C C . ASP A 1 111 ? 79.695 -33.167 38.592 1.00 72.02 ? 142 ASP B C 1 ATOM 818 O O . ASP A 1 111 ? 80.632 -32.537 39.096 1.00 71.86 ? 142 ASP B O 1 ATOM 819 C CB . ASP A 1 111 ? 78.966 -34.639 36.653 1.00 71.78 ? 142 ASP B CB 1 ATOM 820 C CG . ASP A 1 111 ? 79.294 -35.748 37.622 1.00 73.21 ? 142 ASP B CG 1 ATOM 821 O OD1 . ASP A 1 111 ? 80.473 -35.861 38.019 1.00 73.54 ? 142 ASP B OD1 1 ATOM 822 O OD2 . ASP A 1 111 ? 78.346 -36.460 38.031 1.00 74.23 ? 142 ASP B OD2 1 ATOM 823 N N . SER A 1 112 ? 78.727 -33.754 39.292 1.00 85.28 ? 143 SER B N 1 ATOM 824 C CA . SER A 1 112 ? 78.630 -33.747 40.734 1.00 86.53 ? 143 SER B CA 1 ATOM 825 C C . SER A 1 112 ? 78.454 -32.321 41.160 1.00 85.76 ? 143 SER B C 1 ATOM 826 O O . SER A 1 112 ? 77.732 -31.569 40.519 1.00 84.81 ? 143 SER B O 1 ATOM 827 C CB . SER A 1 112 ? 79.886 -34.343 41.372 1.00 87.46 ? 143 SER B CB 1 ATOM 828 O OG . SER A 1 112 ? 81.015 -33.518 41.131 1.00 86.35 ? 143 SER B OG 1 ATOM 829 N N . SER A 1 113 ? 79.128 -31.913 42.217 1.00 66.79 ? 144 SER B N 1 ATOM 830 C CA . SER A 1 113 ? 78.837 -30.596 42.695 1.00 66.26 ? 144 SER B CA 1 ATOM 831 C C . SER A 1 113 ? 79.784 -29.594 42.138 1.00 64.87 ? 144 SER B C 1 ATOM 832 O O . SER A 1 113 ? 80.767 -29.931 41.469 1.00 64.38 ? 144 SER B O 1 ATOM 833 C CB . SER A 1 113 ? 78.888 -30.545 44.204 1.00 67.67 ? 144 SER B CB 1 ATOM 834 O OG . SER A 1 113 ? 77.571 -30.580 44.709 1.00 68.70 ? 144 SER B OG 1 ATOM 835 N N . PHE A 1 114 ? 79.484 -28.345 42.446 1.00 51.65 ? 145 PHE B N 1 ATOM 836 C CA . PHE A 1 114 ? 80.383 -27.289 42.106 1.00 51.16 ? 145 PHE B CA 1 ATOM 837 C C . PHE A 1 114 ? 81.190 -26.852 43.322 1.00 51.44 ? 145 PHE B C 1 ATOM 838 O O . PHE A 1 114 ? 80.653 -26.307 44.289 1.00 51.77 ? 145 PHE B O 1 ATOM 839 C CB . PHE A 1 114 ? 79.650 -26.131 41.471 1.00 50.82 ? 145 PHE B CB 1 ATOM 840 C CG . PHE A 1 114 ? 80.548 -25.276 40.681 1.00 50.43 ? 145 PHE B CG 1 ATOM 841 C CD1 . PHE A 1 114 ? 81.319 -24.320 41.300 1.00 50.42 ? 145 PHE B CD1 1 ATOM 842 C CD2 . PHE A 1 114 ? 80.694 -25.479 39.335 1.00 50.20 ? 145 PHE B CD2 1 ATOM 843 C CE1 . PHE A 1 114 ? 82.185 -23.550 40.587 1.00 50.21 ? 145 PHE B CE1 1 ATOM 844 C CE2 . PHE A 1 114 ? 81.565 -24.720 38.611 1.00 50.05 ? 145 PHE B CE2 1 ATOM 845 C CZ . PHE A 1 114 ? 82.316 -23.753 39.238 1.00 50.07 ? 145 PHE B CZ 1 ATOM 846 N N . PRO A 1 115 ? 82.494 -27.110 43.270 1.00 68.96 ? 146 PRO B N 1 ATOM 847 C CA . PRO A 1 115 ? 83.478 -26.854 44.319 1.00 69.34 ? 146 PRO B CA 1 ATOM 848 C C . PRO A 1 115 ? 83.390 -25.432 44.807 1.00 68.85 ? 146 PRO B C 1 ATOM 849 O O . PRO A 1 115 ? 83.155 -24.536 44.005 1.00 67.93 ? 146 PRO B O 1 ATOM 850 C CB . PRO A 1 115 ? 84.811 -27.079 43.608 1.00 68.86 ? 146 PRO B CB 1 ATOM 851 C CG . PRO A 1 115 ? 84.494 -27.026 42.184 1.00 68.20 ? 146 PRO B CG 1 ATOM 852 C CD . PRO A 1 115 ? 83.137 -27.593 42.049 1.00 68.54 ? 146 PRO B CD 1 ATOM 853 N N . PRO A 1 116 ? 83.585 -25.229 46.114 1.00 69.85 ? 147 PRO B N 1 ATOM 854 C CA . PRO A 1 116 ? 83.251 -23.972 46.772 1.00 69.54 ? 147 PRO B CA 1 ATOM 855 C C . PRO A 1 116 ? 84.183 -22.815 46.432 1.00 68.49 ? 147 PRO B C 1 ATOM 856 O O . PRO A 1 116 ? 83.680 -21.704 46.400 1.00 67.96 ? 147 PRO B O 1 ATOM 857 C CB . PRO A 1 116 ? 83.383 -24.323 48.243 1.00 70.85 ? 147 PRO B CB 1 ATOM 858 C CG . PRO A 1 116 ? 84.512 -25.280 48.253 1.00 72.09 ? 147 PRO B CG 1 ATOM 859 C CD . PRO A 1 116 ? 84.348 -26.114 47.009 1.00 71.21 ? 147 PRO B CD 1 ATOM 860 N N . GLY A 1 117 ? 85.458 -23.053 46.118 1.00 81.33 ? 148 GLY B N 1 ATOM 861 C CA . GLY A 1 117 ? 86.480 -22.000 46.163 1.00 80.77 ? 148 GLY B CA 1 ATOM 862 C C . GLY A 1 117 ? 86.439 -20.852 45.148 1.00 79.90 ? 148 GLY B C 1 ATOM 863 O O . GLY A 1 117 ? 87.359 -20.018 45.085 1.00 79.62 ? 148 GLY B O 1 ATOM 864 N N . ILE A 1 118 ? 85.352 -20.788 44.383 1.00 50.65 ? 149 ILE B N 1 ATOM 865 C CA . ILE A 1 118 ? 85.229 -19.913 43.213 1.00 50.44 ? 149 ILE B CA 1 ATOM 866 C C . ILE A 1 118 ? 85.386 -18.407 43.470 1.00 50.52 ? 149 ILE B C 1 ATOM 867 O O . ILE A 1 118 ? 85.819 -17.658 42.593 1.00 50.63 ? 149 ILE B O 1 ATOM 868 C CB . ILE A 1 118 ? 83.919 -20.250 42.413 1.00 50.34 ? 149 ILE B CB 1 ATOM 869 C CG1 . ILE A 1 118 ? 83.413 -19.047 41.587 1.00 50.38 ? 149 ILE B CG1 1 ATOM 870 C CG2 . ILE A 1 118 ? 82.852 -20.912 43.344 1.00 50.51 ? 149 ILE B CG2 1 ATOM 871 C CD1 . ILE A 1 118 ? 84.024 -18.925 40.191 1.00 50.36 ? 149 ILE B CD1 1 ATOM 872 N N . SER A 1 119 ? 85.076 -17.956 44.675 1.00 66.89 ? 150 SER B N 1 ATOM 873 C CA . SER A 1 119 ? 85.163 -16.528 44.945 1.00 66.69 ? 150 SER B CA 1 ATOM 874 C C . SER A 1 119 ? 86.607 -16.069 44.966 1.00 66.59 ? 150 SER B C 1 ATOM 875 O O . SER A 1 119 ? 86.873 -14.873 44.971 1.00 66.46 ? 150 SER B O 1 ATOM 876 C CB . SER A 1 119 ? 84.443 -16.141 46.246 1.00 66.97 ? 150 SER B CB 1 ATOM 877 O OG . SER A 1 119 ? 85.089 -16.663 47.393 1.00 67.39 ? 150 SER B OG 1 ATOM 878 N N . LYS A 1 120 ? 87.537 -17.022 44.963 1.00 70.80 ? 151 LYS B N 1 ATOM 879 C CA . LYS A 1 120 ? 88.959 -16.688 45.045 1.00 70.88 ? 151 LYS B CA 1 ATOM 880 C C . LYS A 1 120 ? 89.460 -15.930 43.795 1.00 70.83 ? 151 LYS B C 1 ATOM 881 O O . LYS A 1 120 ? 90.452 -15.198 43.870 1.00 70.97 ? 151 LYS B O 1 ATOM 882 C CB . LYS A 1 120 ? 89.778 -17.962 45.315 1.00 71.27 ? 151 LYS B CB 1 ATOM 883 C CG . LYS A 1 120 ? 91.188 -17.757 45.866 1.00 71.53 ? 151 LYS B CG 1 ATOM 884 C CD . LYS A 1 120 ? 91.637 -18.953 46.725 1.00 72.11 ? 151 LYS B CD 1 ATOM 885 C CE . LYS A 1 120 ? 90.963 -20.268 46.289 1.00 72.26 ? 151 LYS B CE 1 ATOM 886 N NZ . LYS A 1 120 ? 91.174 -21.407 47.248 1.00 72.86 ? 151 LYS B NZ 1 ATOM 887 N N . LEU A 1 121 ? 88.775 -16.115 42.660 1.00 54.75 ? 152 LEU B N 1 ATOM 888 C CA . LEU A 1 121 ? 89.086 -15.415 41.406 1.00 54.97 ? 152 LEU B CA 1 ATOM 889 C C . LEU A 1 121 ? 88.981 -13.880 41.518 1.00 55.14 ? 152 LEU B C 1 ATOM 890 O O . LEU A 1 121 ? 89.957 -13.159 41.314 1.00 55.51 ? 152 LEU B O 1 ATOM 891 C CB . LEU A 1 121 ? 88.206 -15.931 40.271 1.00 54.96 ? 152 LEU B CB 1 ATOM 892 C CG . LEU A 1 121 ? 88.570 -17.228 39.522 1.00 55.07 ? 152 LEU B CG 1 ATOM 893 C CD1 . LEU A 1 121 ? 90.029 -17.626 39.688 1.00 55.36 ? 152 LEU B CD1 1 ATOM 894 C CD2 . LEU A 1 121 ? 87.644 -18.376 39.879 1.00 54.80 ? 152 LEU B CD2 1 ATOM 895 N N . LYS A 1 122 ? 87.767 -13.395 41.759 1.00 66.87 ? 153 LYS B N 1 ATOM 896 C CA . LYS A 1 122 ? 87.492 -12.048 42.282 1.00 66.84 ? 153 LYS B CA 1 ATOM 897 C C . LYS A 1 122 ? 87.676 -10.905 41.318 1.00 67.19 ? 153 LYS B C 1 ATOM 898 O O . LYS A 1 122 ? 86.886 -9.972 41.317 1.00 67.19 ? 153 LYS B O 1 ATOM 899 C CB . LYS A 1 122 ? 88.413 -11.781 43.484 1.00 66.81 ? 153 LYS B CB 1 ATOM 900 C CG . LYS A 1 122 ? 88.445 -10.355 44.010 1.00 66.88 ? 153 LYS B CG 1 ATOM 901 C CD . LYS A 1 122 ? 87.095 -9.922 44.618 1.00 66.70 ? 153 LYS B CD 1 ATOM 902 C CE . LYS A 1 122 ? 86.433 -11.003 45.502 1.00 66.26 ? 153 LYS B CE 1 ATOM 903 N NZ . LYS A 1 122 ? 87.253 -11.498 46.655 1.00 66.53 ? 153 LYS B NZ 1 ATOM 904 N N . PHE A 1 123 ? 88.609 -11.035 40.395 1.00 75.13 ? 154 PHE B N 1 ATOM 905 C CA . PHE A 1 123 ? 88.778 -10.004 39.397 1.00 75.68 ? 154 PHE B CA 1 ATOM 906 C C . PHE A 1 123 ? 88.058 -10.514 38.184 1.00 75.90 ? 154 PHE B C 1 ATOM 907 O O . PHE A 1 123 ? 88.022 -9.867 37.130 1.00 76.45 ? 154 PHE B O 1 ATOM 908 C CB . PHE A 1 123 ? 90.250 -9.746 39.115 1.00 76.19 ? 154 PHE B CB 1 ATOM 909 C CG . PHE A 1 123 ? 90.833 -8.660 39.959 1.00 76.20 ? 154 PHE B CG 1 ATOM 910 C CD1 . PHE A 1 123 ? 90.221 -8.287 41.141 1.00 75.68 ? 154 PHE B CD1 1 ATOM 911 C CD2 . PHE A 1 123 ? 91.976 -7.993 39.563 1.00 76.79 ? 154 PHE B CD2 1 ATOM 912 C CE1 . PHE A 1 123 ? 90.745 -7.278 41.926 1.00 75.67 ? 154 PHE B CE1 1 ATOM 913 C CE2 . PHE A 1 123 ? 92.498 -6.977 40.340 1.00 76.78 ? 154 PHE B CE2 1 ATOM 914 C CZ . PHE A 1 123 ? 91.882 -6.624 41.528 1.00 76.18 ? 154 PHE B CZ 1 ATOM 915 N N . LEU A 1 124 ? 87.484 -11.700 38.369 1.00 53.46 ? 155 LEU B N 1 ATOM 916 C CA . LEU A 1 124 ? 86.778 -12.424 37.329 1.00 53.34 ? 155 LEU B CA 1 ATOM 917 C C . LEU A 1 124 ? 85.627 -11.602 36.721 1.00 53.84 ? 155 LEU B C 1 ATOM 918 O O . LEU A 1 124 ? 84.803 -11.016 37.447 1.00 53.94 ? 155 LEU B O 1 ATOM 919 C CB . LEU A 1 124 ? 86.264 -13.738 37.899 1.00 52.57 ? 155 LEU B CB 1 ATOM 920 C CG . LEU A 1 124 ? 85.689 -14.714 36.894 1.00 52.35 ? 155 LEU B CG 1 ATOM 921 C CD1 . LEU A 1 124 ? 86.798 -15.490 36.228 1.00 52.34 ? 155 LEU B CD1 1 ATOM 922 C CD2 . LEU A 1 124 ? 84.741 -15.628 37.602 1.00 51.76 ? 155 LEU B CD2 1 ATOM 923 N N . LYS A 1 125 ? 85.597 -11.548 35.388 1.00 60.37 ? 156 LYS B N 1 ATOM 924 C CA . LYS A 1 125 ? 84.527 -10.874 34.656 1.00 60.69 ? 156 LYS B CA 1 ATOM 925 C C . LYS A 1 125 ? 83.543 -11.883 34.095 1.00 60.59 ? 156 LYS B C 1 ATOM 926 O O . LYS A 1 125 ? 82.369 -11.848 34.438 1.00 60.38 ? 156 LYS B O 1 ATOM 927 C CB . LYS A 1 125 ? 85.068 -9.977 33.539 1.00 61.48 ? 156 LYS B CB 1 ATOM 928 C CG . LYS A 1 125 ? 85.941 -8.825 34.038 1.00 61.82 ? 156 LYS B CG 1 ATOM 929 C CD . LYS A 1 125 ? 85.777 -7.559 33.193 1.00 62.65 ? 156 LYS B CD 1 ATOM 930 C CE . LYS A 1 125 ? 86.338 -6.312 33.920 1.00 62.54 ? 156 LYS B CE 1 ATOM 931 N NZ . LYS A 1 125 ? 85.620 -5.924 35.200 1.00 61.88 ? 156 LYS B NZ 1 ATOM 932 N N . VAL A 1 126 ? 84.029 -12.770 33.230 1.00 56.10 ? 157 VAL B N 1 ATOM 933 C CA . VAL A 1 126 ? 83.192 -13.744 32.517 1.00 55.93 ? 157 VAL B CA 1 ATOM 934 C C . VAL A 1 126 ? 83.307 -15.178 33.024 1.00 55.14 ? 157 VAL B C 1 ATOM 935 O O . VAL A 1 126 ? 84.395 -15.738 32.979 1.00 55.04 ? 157 VAL B O 1 ATOM 936 C CB . VAL A 1 126 ? 83.644 -13.853 31.063 1.00 56.53 ? 157 VAL B CB 1 ATOM 937 C CG1 . VAL A 1 126 ? 82.470 -14.177 30.188 1.00 56.72 ? 157 VAL B CG1 1 ATOM 938 C CG2 . VAL A 1 126 ? 84.338 -12.581 30.622 1.00 57.36 ? 157 VAL B CG2 1 ATOM 939 N N . PHE A 1 127 ? 82.210 -15.803 33.452 1.00 60.15 ? 158 PHE B N 1 ATOM 940 C CA . PHE A 1 127 ? 82.257 -17.236 33.768 1.00 59.75 ? 158 PHE B CA 1 ATOM 941 C C . PHE A 1 127 ? 81.243 -18.023 32.956 1.00 59.85 ? 158 PHE B C 1 ATOM 942 O O . PHE A 1 127 ? 80.043 -17.834 33.118 1.00 59.87 ? 158 PHE B O 1 ATOM 943 C CB . PHE A 1 127 ? 82.037 -17.480 35.264 1.00 59.27 ? 158 PHE B CB 1 ATOM 944 C CG . PHE A 1 127 ? 81.910 -18.946 35.644 1.00 59.00 ? 158 PHE B CG 1 ATOM 945 C CD1 . PHE A 1 127 ? 82.997 -19.802 35.567 1.00 58.95 ? 158 PHE B CD1 1 ATOM 946 C CD2 . PHE A 1 127 ? 80.700 -19.457 36.104 1.00 58.92 ? 158 PHE B CD2 1 ATOM 947 C CE1 . PHE A 1 127 ? 82.865 -21.136 35.920 1.00 58.80 ? 158 PHE B CE1 1 ATOM 948 C CE2 . PHE A 1 127 ? 80.566 -20.787 36.456 1.00 58.82 ? 158 PHE B CE2 1 ATOM 949 C CZ . PHE A 1 127 ? 81.647 -21.624 36.363 1.00 58.75 ? 158 PHE B CZ 1 ATOM 950 N N . ASN A 1 128 ? 81.709 -18.900 32.072 1.00 62.76 ? 159 ASN B N 1 ATOM 951 C CA . ASN A 1 128 ? 80.765 -19.742 31.348 1.00 62.81 ? 159 ASN B CA 1 ATOM 952 C C . ASN A 1 128 ? 80.875 -21.241 31.609 1.00 62.49 ? 159 ASN B C 1 ATOM 953 O O . ASN A 1 128 ? 81.760 -21.914 31.087 1.00 62.56 ? 159 ASN B O 1 ATOM 954 C CB . ASN A 1 128 ? 80.868 -19.485 29.858 1.00 63.35 ? 159 ASN B CB 1 ATOM 955 C CG . ASN A 1 128 ? 79.607 -19.841 29.140 1.00 63.58 ? 159 ASN B CG 1 ATOM 956 O OD1 . ASN A 1 128 ? 78.941 -20.817 29.485 1.00 63.25 ? 159 ASN B OD1 1 ATOM 957 N ND2 . ASN A 1 128 ? 79.246 -19.034 28.149 1.00 64.22 ? 159 ASN B ND2 1 ATOM 958 N N . ALA A 1 129 ? 79.930 -21.747 32.394 1.00 57.61 ? 160 ALA B N 1 ATOM 959 C CA . ALA A 1 129 ? 79.800 -23.163 32.733 1.00 57.42 ? 160 ALA B CA 1 ATOM 960 C C . ALA A 1 129 ? 78.724 -23.868 31.920 1.00 57.59 ? 160 ALA B C 1 ATOM 961 O O . ALA A 1 129 ? 78.318 -24.975 32.268 1.00 57.54 ? 160 ALA B O 1 ATOM 962 C CB . ALA A 1 129 ? 79.544 -23.336 34.222 1.00 57.22 ? 160 ALA B CB 1 ATOM 963 N N . PHE A 1 130 ? 78.184 -23.175 30.919 1.00 58.35 ? 161 PHE B N 1 ATOM 964 C CA . PHE A 1 130 ? 77.001 -23.642 30.201 1.00 58.60 ? 161 PHE B CA 1 ATOM 965 C C . PHE A 1 130 ? 77.162 -25.005 29.503 1.00 58.56 ? 161 PHE B C 1 ATOM 966 O O . PHE A 1 130 ? 78.175 -25.276 28.865 1.00 58.55 ? 161 PHE B O 1 ATOM 967 C CB . PHE A 1 130 ? 76.515 -22.576 29.223 1.00 59.06 ? 161 PHE B CB 1 ATOM 968 C CG . PHE A 1 130 ? 75.507 -23.075 28.257 1.00 59.40 ? 161 PHE B CG 1 ATOM 969 C CD1 . PHE A 1 130 ? 74.201 -23.267 28.645 1.00 59.52 ? 161 PHE B CD1 1 ATOM 970 C CD2 . PHE A 1 130 ? 75.862 -23.377 26.963 1.00 59.67 ? 161 PHE B CD2 1 ATOM 971 C CE1 . PHE A 1 130 ? 73.258 -23.749 27.753 1.00 59.90 ? 161 PHE B CE1 1 ATOM 972 C CE2 . PHE A 1 130 ? 74.930 -23.855 26.067 1.00 60.01 ? 161 PHE B CE2 1 ATOM 973 C CZ . PHE A 1 130 ? 73.627 -24.042 26.462 1.00 60.11 ? 161 PHE B CZ 1 ATOM 974 N N . SER A 1 131 ? 76.131 -25.842 29.610 1.00 71.34 ? 162 SER B N 1 ATOM 975 C CA . SER A 1 131 ? 76.137 -27.217 29.088 1.00 71.31 ? 162 SER B CA 1 ATOM 976 C C . SER A 1 131 ? 77.150 -28.190 29.697 1.00 71.07 ? 162 SER B C 1 ATOM 977 O O . SER A 1 131 ? 78.105 -28.585 29.047 1.00 71.14 ? 162 SER B O 1 ATOM 978 C CB . SER A 1 131 ? 76.251 -27.237 27.567 1.00 71.52 ? 162 SER B CB 1 ATOM 979 O OG . SER A 1 131 ? 76.273 -28.572 27.094 1.00 71.43 ? 162 SER B OG 1 ATOM 980 N N . ASN A 1 132 ? 76.918 -28.579 30.945 1.00 50.11 ? 163 ASN B N 1 ATOM 981 C CA . ASN A 1 132 ? 77.752 -29.549 31.646 1.00 50.01 ? 163 ASN B CA 1 ATOM 982 C C . ASN A 1 132 ? 76.842 -30.489 32.429 1.00 50.02 ? 163 ASN B C 1 ATOM 983 O O . ASN A 1 132 ? 75.626 -30.384 32.337 1.00 50.10 ? 163 ASN B O 1 ATOM 984 C CB . ASN A 1 132 ? 78.733 -28.837 32.581 1.00 49.98 ? 163 ASN B CB 1 ATOM 985 C CG . ASN A 1 132 ? 79.980 -28.310 31.854 1.00 50.08 ? 163 ASN B CG 1 ATOM 986 O OD1 . ASN A 1 132 ? 80.613 -29.031 31.117 1.00 50.17 ? 163 ASN B OD1 1 ATOM 987 N ND2 . ASN A 1 132 ? 80.336 -27.055 32.089 1.00 50.16 ? 163 ASN B ND2 1 ATOM 988 N N . ASN A 1 133 ? 77.422 -31.430 33.168 1.00 64.16 ? 164 ASN B N 1 ATOM 989 C CA . ASN A 1 133 ? 76.659 -32.397 33.986 1.00 64.82 ? 164 ASN B CA 1 ATOM 990 C C . ASN A 1 133 ? 76.491 -32.050 35.471 1.00 65.30 ? 164 ASN B C 1 ATOM 991 O O . ASN A 1 133 ? 76.192 -32.933 36.275 1.00 66.18 ? 164 ASN B O 1 ATOM 992 C CB . ASN A 1 133 ? 77.153 -33.827 33.779 1.00 65.15 ? 164 ASN B CB 1 ATOM 993 C CG . ASN A 1 133 ? 77.181 -34.214 32.314 1.00 64.90 ? 164 ASN B CG 1 ATOM 994 O OD1 . ASN A 1 133 ? 76.362 -33.737 31.514 1.00 64.86 ? 164 ASN B OD1 1 ATOM 995 N ND2 . ASN A 1 133 ? 78.133 -35.071 31.946 1.00 64.84 ? 164 ASN B ND2 1 ATOM 996 N N . PHE A 1 134 ? 76.792 -30.802 35.837 1.00 54.73 ? 165 PHE B N 1 ATOM 997 C CA . PHE A 1 134 ? 76.664 -30.352 37.221 1.00 55.15 ? 165 PHE B CA 1 ATOM 998 C C . PHE A 1 134 ? 75.321 -30.704 37.809 1.00 55.93 ? 165 PHE B C 1 ATOM 999 O O . PHE A 1 134 ? 74.289 -30.570 37.155 1.00 55.84 ? 165 PHE B O 1 ATOM 1000 C CB . PHE A 1 134 ? 76.848 -28.839 37.350 1.00 54.61 ? 165 PHE B CB 1 ATOM 1001 C CG . PHE A 1 134 ? 78.232 -28.392 37.102 1.00 54.09 ? 165 PHE B CG 1 ATOM 1002 C CD1 . PHE A 1 134 ? 79.298 -29.124 37.587 1.00 54.31 ? 165 PHE B CD1 1 ATOM 1003 C CD2 . PHE A 1 134 ? 78.484 -27.266 36.351 1.00 53.58 ? 165 PHE B CD2 1 ATOM 1004 C CE1 . PHE A 1 134 ? 80.608 -28.728 37.337 1.00 53.94 ? 165 PHE B CE1 1 ATOM 1005 C CE2 . PHE A 1 134 ? 79.784 -26.862 36.088 1.00 53.29 ? 165 PHE B CE2 1 ATOM 1006 C CZ . PHE A 1 134 ? 80.850 -27.591 36.577 1.00 53.42 ? 165 PHE B CZ 1 ATOM 1007 N N . GLU A 1 135 ? 75.374 -31.187 39.046 1.00 71.41 ? 166 GLU B N 1 ATOM 1008 C CA . GLU A 1 135 ? 74.222 -31.305 39.919 1.00 72.47 ? 166 GLU B CA 1 ATOM 1009 C C . GLU A 1 135 ? 74.557 -30.519 41.179 1.00 72.81 ? 166 GLU B C 1 ATOM 1010 O O . GLU A 1 135 ? 75.653 -29.964 41.309 1.00 72.10 ? 166 GLU B O 1 ATOM 1011 C CB . GLU A 1 135 ? 73.925 -32.772 40.233 1.00 73.84 ? 166 GLU B CB 1 ATOM 1012 C CG . GLU A 1 135 ? 75.171 -33.572 40.600 1.00 74.89 ? 166 GLU B CG 1 ATOM 1013 C CD . GLU A 1 135 ? 75.015 -35.083 40.446 1.00 75.51 ? 166 GLU B CD 1 ATOM 1014 O OE1 . GLU A 1 135 ? 74.761 -35.561 39.310 1.00 75.04 ? 166 GLU B OE1 1 ATOM 1015 O OE2 . GLU A 1 135 ? 75.168 -35.787 41.473 1.00 76.54 ? 166 GLU B OE2 1 ATOM 1016 N N . GLY A 1 136 ? 73.615 -30.454 42.105 1.00 69.25 ? 167 GLY B N 1 ATOM 1017 C CA . GLY A 1 136 ? 73.846 -29.737 43.347 1.00 69.72 ? 167 GLY B CA 1 ATOM 1018 C C . GLY A 1 136 ? 73.345 -28.309 43.296 1.00 68.87 ? 167 GLY B C 1 ATOM 1019 O O . GLY A 1 136 ? 72.937 -27.836 42.237 1.00 68.06 ? 167 GLY B O 1 ATOM 1020 N N . LEU A 1 137 ? 73.367 -27.633 44.444 1.00 57.86 ? 168 LEU B N 1 ATOM 1021 C CA . LEU A 1 137 ? 72.921 -26.249 44.546 1.00 57.29 ? 168 LEU B CA 1 ATOM 1022 C C . LEU A 1 137 ? 73.874 -25.345 43.808 1.00 55.84 ? 168 LEU B C 1 ATOM 1023 O O . LEU A 1 137 ? 75.069 -25.641 43.716 1.00 55.42 ? 168 LEU B O 1 ATOM 1024 C CB . LEU A 1 137 ? 72.909 -25.781 45.995 1.00 58.21 ? 168 LEU B CB 1 ATOM 1025 C CG . LEU A 1 137 ? 72.009 -26.349 47.099 1.00 59.35 ? 168 LEU B CG 1 ATOM 1026 C CD1 . LEU A 1 137 ? 70.564 -26.486 46.638 1.00 60.03 ? 168 LEU B CD1 1 ATOM 1027 C CD2 . LEU A 1 137 ? 72.571 -27.666 47.664 1.00 60.30 ? 168 LEU B CD2 1 ATOM 1028 N N . LEU A 1 138 ? 73.348 -24.233 43.298 1.00 52.62 ? 169 LEU B N 1 ATOM 1029 C CA . LEU A 1 138 ? 74.181 -23.225 42.647 1.00 52.10 ? 169 LEU B CA 1 ATOM 1030 C C . LEU A 1 138 ? 75.178 -22.820 43.689 1.00 52.10 ? 169 LEU B C 1 ATOM 1031 O O . LEU A 1 138 ? 74.793 -22.654 44.832 1.00 52.60 ? 169 LEU B O 1 ATOM 1032 C CB . LEU A 1 138 ? 73.339 -22.015 42.271 1.00 52.35 ? 169 LEU B CB 1 ATOM 1033 C CG . LEU A 1 138 ? 72.923 -21.765 40.827 1.00 52.12 ? 169 LEU B CG 1 ATOM 1034 C CD1 . LEU A 1 138 ? 73.165 -22.968 39.987 1.00 51.72 ? 169 LEU B CD1 1 ATOM 1035 C CD2 . LEU A 1 138 ? 71.474 -21.375 40.784 1.00 52.66 ? 169 LEU B CD2 1 ATOM 1036 N N . PRO A 1 139 ? 76.462 -22.711 43.325 1.00 54.71 ? 170 PRO B N 1 ATOM 1037 C CA . PRO A 1 139 ? 77.425 -22.289 44.345 1.00 54.80 ? 170 PRO B CA 1 ATOM 1038 C C . PRO A 1 139 ? 77.017 -20.931 44.853 1.00 54.70 ? 170 PRO B C 1 ATOM 1039 O O . PRO A 1 139 ? 76.763 -20.059 44.042 1.00 54.20 ? 170 PRO B O 1 ATOM 1040 C CB . PRO A 1 139 ? 78.752 -22.183 43.581 1.00 54.19 ? 170 PRO B CB 1 ATOM 1041 C CG . PRO A 1 139 ? 78.385 -22.201 42.144 1.00 53.67 ? 170 PRO B CG 1 ATOM 1042 C CD . PRO A 1 139 ? 77.106 -22.977 42.035 1.00 54.00 ? 170 PRO B CD 1 ATOM 1043 N N . SER A 1 140 ? 76.910 -20.759 46.164 1.00 73.13 ? 171 SER B N 1 ATOM 1044 C CA . SER A 1 140 ? 76.527 -19.467 46.687 1.00 72.99 ? 171 SER B CA 1 ATOM 1045 C C . SER A 1 140 ? 77.740 -18.596 46.513 1.00 72.22 ? 171 SER B C 1 ATOM 1046 O O . SER A 1 140 ? 77.640 -17.414 46.213 1.00 71.76 ? 171 SER B O 1 ATOM 1047 C CB . SER A 1 140 ? 76.151 -19.563 48.156 1.00 73.95 ? 171 SER B CB 1 ATOM 1048 O OG . SER A 1 140 ? 75.625 -18.329 48.617 1.00 73.89 ? 171 SER B OG 1 ATOM 1049 N N . ASP A 1 141 ? 78.894 -19.231 46.645 1.00 77.69 ? 172 ASP B N 1 ATOM 1050 C CA . ASP A 1 141 ? 80.179 -18.562 46.669 1.00 77.17 ? 172 ASP B CA 1 ATOM 1051 C C . ASP A 1 141 ? 80.415 -17.515 45.564 1.00 76.38 ? 172 ASP B C 1 ATOM 1052 O O . ASP A 1 141 ? 80.962 -16.439 45.833 1.00 76.11 ? 172 ASP B O 1 ATOM 1053 C CB . ASP A 1 141 ? 81.261 -19.629 46.636 1.00 77.35 ? 172 ASP B CB 1 ATOM 1054 C CG . ASP A 1 141 ? 82.635 -19.051 46.744 1.00 76.93 ? 172 ASP B CG 1 ATOM 1055 O OD1 . ASP A 1 141 ? 83.006 -18.585 47.839 1.00 77.42 ? 172 ASP B OD1 1 ATOM 1056 O OD2 . ASP A 1 141 ? 83.358 -19.074 45.733 1.00 76.26 ? 172 ASP B OD2 1 ATOM 1057 N N . VAL A 1 142 ? 79.984 -17.819 44.338 1.00 70.04 ? 173 VAL B N 1 ATOM 1058 C CA . VAL A 1 142 ? 80.170 -16.925 43.184 1.00 69.62 ? 173 VAL B CA 1 ATOM 1059 C C . VAL A 1 142 ? 79.565 -15.543 43.425 1.00 69.64 ? 173 VAL B C 1 ATOM 1060 O O . VAL A 1 142 ? 80.013 -14.527 42.860 1.00 69.46 ? 173 VAL B O 1 ATOM 1061 C CB . VAL A 1 142 ? 79.615 -17.558 41.871 1.00 69.62 ? 173 VAL B CB 1 ATOM 1062 C CG1 . VAL A 1 142 ? 78.664 -18.655 42.187 1.00 70.07 ? 173 VAL B CG1 1 ATOM 1063 C CG2 . VAL A 1 142 ? 78.938 -16.536 40.973 1.00 69.85 ? 173 VAL B CG2 1 ATOM 1064 N N . SER A 1 143 ? 78.583 -15.505 44.317 1.00 69.60 ? 174 SER B N 1 ATOM 1065 C CA . SER A 1 143 ? 77.929 -14.260 44.677 1.00 69.68 ? 174 SER B CA 1 ATOM 1066 C C . SER A 1 143 ? 78.894 -13.227 45.239 1.00 69.43 ? 174 SER B C 1 ATOM 1067 O O . SER A 1 143 ? 78.527 -12.071 45.412 1.00 69.44 ? 174 SER B O 1 ATOM 1068 C CB . SER A 1 143 ? 76.835 -14.516 45.704 1.00 70.22 ? 174 SER B CB 1 ATOM 1069 O OG . SER A 1 143 ? 76.571 -13.338 46.436 1.00 70.35 ? 174 SER B OG 1 ATOM 1070 N N . ARG A 1 144 ? 80.109 -13.639 45.569 1.00 71.99 ? 175 ARG B N 1 ATOM 1071 C CA . ARG A 1 144 ? 81.054 -12.686 46.121 1.00 71.82 ? 175 ARG B CA 1 ATOM 1072 C C . ARG A 1 144 ? 82.105 -12.053 45.197 1.00 71.54 ? 175 ARG B C 1 ATOM 1073 O O . ARG A 1 144 ? 82.976 -11.323 45.666 1.00 71.46 ? 175 ARG B O 1 ATOM 1074 C CB . ARG A 1 144 ? 81.631 -13.183 47.436 1.00 72.07 ? 175 ARG B CB 1 ATOM 1075 C CG . ARG A 1 144 ? 80.635 -13.018 48.575 1.00 72.56 ? 175 ARG B CG 1 ATOM 1076 C CD . ARG A 1 144 ? 81.331 -12.936 49.914 1.00 73.01 ? 175 ARG B CD 1 ATOM 1077 N NE . ARG A 1 144 ? 82.259 -14.043 50.058 1.00 73.43 ? 175 ARG B NE 1 ATOM 1078 C CZ . ARG A 1 144 ? 81.889 -15.292 50.318 1.00 73.93 ? 175 ARG B CZ 1 ATOM 1079 N NH1 . ARG A 1 144 ? 80.603 -15.592 50.471 1.00 74.02 ? 175 ARG B NH1 1 ATOM 1080 N NH2 . ARG A 1 144 ? 82.812 -16.240 50.427 1.00 74.47 ? 175 ARG B NH2 1 ATOM 1081 N N . LEU A 1 145 ? 82.034 -12.309 43.895 1.00 68.68 ? 176 LEU B N 1 ATOM 1082 C CA . LEU A 1 145 ? 82.942 -11.617 42.987 1.00 68.71 ? 176 LEU B CA 1 ATOM 1083 C C . LEU A 1 145 ? 82.225 -10.357 42.583 1.00 68.88 ? 176 LEU B C 1 ATOM 1084 O O . LEU A 1 145 ? 81.276 -10.414 41.807 1.00 69.04 ? 176 LEU B O 1 ATOM 1085 C CB . LEU A 1 145 ? 83.162 -12.444 41.732 1.00 68.79 ? 176 LEU B CB 1 ATOM 1086 C CG . LEU A 1 145 ? 83.211 -13.943 41.944 1.00 68.68 ? 176 LEU B CG 1 ATOM 1087 C CD1 . LEU A 1 145 ? 82.476 -14.626 40.820 1.00 68.83 ? 176 LEU B CD1 1 ATOM 1088 C CD2 . LEU A 1 145 ? 84.656 -14.387 42.002 1.00 68.53 ? 176 LEU B CD2 1 ATOM 1089 N N . ARG A 1 146 ? 82.681 -9.213 43.068 1.00 83.45 ? 177 ARG B N 1 ATOM 1090 C CA . ARG A 1 146 ? 81.913 -8.005 42.837 1.00 83.65 ? 177 ARG B CA 1 ATOM 1091 C C . ARG A 1 146 ? 81.950 -7.620 41.361 1.00 83.99 ? 177 ARG B C 1 ATOM 1092 O O . ARG A 1 146 ? 80.990 -7.068 40.833 1.00 84.22 ? 177 ARG B O 1 ATOM 1093 C CB . ARG A 1 146 ? 82.387 -6.861 43.737 1.00 83.64 ? 177 ARG B CB 1 ATOM 1094 C CG . ARG A 1 146 ? 83.748 -7.093 44.398 1.00 83.45 ? 177 ARG B CG 1 ATOM 1095 C CD . ARG A 1 146 ? 83.672 -7.025 45.939 1.00 83.22 ? 177 ARG B CD 1 ATOM 1096 N NE . ARG A 1 146 ? 83.970 -5.708 46.512 1.00 83.16 ? 177 ARG B NE 1 ATOM 1097 C CZ . ARG A 1 146 ? 83.071 -4.925 47.111 1.00 83.68 ? 177 ARG B CZ 1 ATOM 1098 N NH1 . ARG A 1 146 ? 81.809 -5.321 47.208 1.00 84.10 ? 177 ARG B NH1 1 ATOM 1099 N NH2 . ARG A 1 146 ? 83.429 -3.744 47.619 1.00 83.90 ? 177 ARG B NH2 1 ATOM 1100 N N . PHE A 1 147 ? 83.041 -7.965 40.686 1.00 63.41 ? 178 PHE B N 1 ATOM 1101 C CA . PHE A 1 147 ? 83.276 -7.492 39.324 1.00 63.90 ? 178 PHE B CA 1 ATOM 1102 C C . PHE A 1 147 ? 82.743 -8.408 38.250 1.00 64.05 ? 178 PHE B C 1 ATOM 1103 O O . PHE A 1 147 ? 82.863 -8.100 37.067 1.00 64.53 ? 178 PHE B O 1 ATOM 1104 C CB . PHE A 1 147 ? 84.763 -7.328 39.076 1.00 64.09 ? 178 PHE B CB 1 ATOM 1105 C CG . PHE A 1 147 ? 85.405 -6.312 39.940 1.00 64.03 ? 178 PHE B CG 1 ATOM 1106 C CD1 . PHE A 1 147 ? 84.837 -5.076 40.098 1.00 64.15 ? 178 PHE B CD1 1 ATOM 1107 C CD2 . PHE A 1 147 ? 86.579 -6.597 40.601 1.00 63.88 ? 178 PHE B CD2 1 ATOM 1108 C CE1 . PHE A 1 147 ? 85.430 -4.138 40.895 1.00 64.09 ? 178 PHE B CE1 1 ATOM 1109 C CE2 . PHE A 1 147 ? 87.180 -5.665 41.392 1.00 63.86 ? 178 PHE B CE2 1 ATOM 1110 C CZ . PHE A 1 147 ? 86.606 -4.433 41.543 1.00 63.95 ? 178 PHE B CZ 1 ATOM 1111 N N . LEU A 1 148 ? 82.189 -9.540 38.657 1.00 59.33 ? 179 LEU B N 1 ATOM 1112 C CA . LEU A 1 148 ? 81.630 -10.490 37.713 1.00 59.39 ? 179 LEU B CA 1 ATOM 1113 C C . LEU A 1 148 ? 80.593 -9.828 36.825 1.00 59.86 ? 179 LEU B C 1 ATOM 1114 O O . LEU A 1 148 ? 79.647 -9.217 37.325 1.00 59.95 ? 179 LEU B O 1 ATOM 1115 C CB . LEU A 1 148 ? 80.950 -11.608 38.473 1.00 58.99 ? 179 LEU B CB 1 ATOM 1116 C CG . LEU A 1 148 ? 80.444 -12.735 37.589 1.00 59.08 ? 179 LEU B CG 1 ATOM 1117 C CD1 . LEU A 1 148 ? 81.609 -13.622 37.181 1.00 58.94 ? 179 LEU B CD1 1 ATOM 1118 C CD2 . LEU A 1 148 ? 79.380 -13.532 38.311 1.00 58.92 ? 179 LEU B CD2 1 ATOM 1119 N N . GLU A 1 149 ? 80.767 -9.960 35.513 1.00 64.14 ? 180 GLU B N 1 ATOM 1120 C CA . GLU A 1 149 ? 79.883 -9.334 34.523 1.00 64.65 ? 180 GLU B CA 1 ATOM 1121 C C . GLU A 1 149 ? 78.902 -10.325 33.902 1.00 64.73 ? 180 GLU B C 1 ATOM 1122 O O . GLU A 1 149 ? 77.697 -10.094 33.894 1.00 64.88 ? 180 GLU B O 1 ATOM 1123 C CB . GLU A 1 149 ? 80.670 -8.574 33.444 1.00 65.27 ? 180 GLU B CB 1 ATOM 1124 C CG . GLU A 1 149 ? 81.301 -7.258 33.934 1.00 65.45 ? 180 GLU B CG 1 ATOM 1125 C CD . GLU A 1 149 ? 81.750 -6.344 32.800 1.00 66.04 ? 180 GLU B CD 1 ATOM 1126 O OE1 . GLU A 1 149 ? 82.718 -5.586 33.002 1.00 65.89 ? 180 GLU B OE1 1 ATOM 1127 O OE2 . GLU A 1 149 ? 81.131 -6.375 31.713 1.00 66.66 ? 180 GLU B OE2 1 ATOM 1128 N N . GLU A 1 150 ? 79.447 -11.380 33.304 1.00 81.14 ? 181 GLU B N 1 ATOM 1129 C CA . GLU A 1 150 ? 78.663 -12.436 32.673 1.00 81.19 ? 181 GLU B CA 1 ATOM 1130 C C . GLU A 1 150 ? 78.782 -13.777 33.410 1.00 80.63 ? 181 GLU B C 1 ATOM 1131 O O . GLU A 1 150 ? 79.882 -14.288 33.598 1.00 80.40 ? 181 GLU B O 1 ATOM 1132 C CB . GLU A 1 150 ? 79.117 -12.601 31.218 1.00 81.69 ? 181 GLU B CB 1 ATOM 1133 C CG . GLU A 1 150 ? 78.742 -13.934 30.587 1.00 81.72 ? 181 GLU B CG 1 ATOM 1134 C CD . GLU A 1 150 ? 79.265 -14.078 29.171 1.00 82.22 ? 181 GLU B CD 1 ATOM 1135 O OE1 . GLU A 1 150 ? 79.889 -13.093 28.709 1.00 82.64 ? 181 GLU B OE1 1 ATOM 1136 O OE2 . GLU A 1 150 ? 79.056 -15.157 28.537 1.00 82.20 ? 181 GLU B OE2 1 ATOM 1137 N N . LEU A 1 151 ? 77.645 -14.345 33.811 1.00 53.47 ? 182 LEU B N 1 ATOM 1138 C CA . LEU A 1 151 ? 77.601 -15.682 34.418 1.00 52.65 ? 182 LEU B CA 1 ATOM 1139 C C . LEU A 1 151 ? 76.606 -16.655 33.759 1.00 52.61 ? 182 LEU B C 1 ATOM 1140 O O . LEU A 1 151 ? 75.390 -16.470 33.843 1.00 52.91 ? 182 LEU B O 1 ATOM 1141 C CB . LEU A 1 151 ? 77.279 -15.560 35.900 1.00 52.44 ? 182 LEU B CB 1 ATOM 1142 C CG . LEU A 1 151 ? 76.730 -16.770 36.651 1.00 52.01 ? 182 LEU B CG 1 ATOM 1143 C CD1 . LEU A 1 151 ? 77.637 -17.970 36.548 1.00 51.45 ? 182 LEU B CD1 1 ATOM 1144 C CD2 . LEU A 1 151 ? 76.551 -16.386 38.095 1.00 52.02 ? 182 LEU B CD2 1 ATOM 1145 N N . ASN A 1 152 ? 77.128 -17.712 33.139 1.00 60.48 ? 183 ASN B N 1 ATOM 1146 C CA . ASN A 1 152 ? 76.296 -18.701 32.472 1.00 60.61 ? 183 ASN B CA 1 ATOM 1147 C C . ASN A 1 152 ? 76.415 -19.990 33.232 1.00 60.25 ? 183 ASN B C 1 ATOM 1148 O O . ASN A 1 152 ? 77.433 -20.645 33.133 1.00 60.01 ? 183 ASN B O 1 ATOM 1149 C CB . ASN A 1 152 ? 76.874 -18.956 31.084 1.00 60.81 ? 183 ASN B CB 1 ATOM 1150 C CG . ASN A 1 152 ? 75.836 -18.876 29.976 1.00 61.50 ? 183 ASN B CG 1 ATOM 1151 O OD1 . ASN A 1 152 ? 74.979 -19.759 29.841 1.00 61.55 ? 183 ASN B OD1 1 ATOM 1152 N ND2 . ASN A 1 152 ? 75.938 -17.833 29.143 1.00 62.09 ? 183 ASN B ND2 1 ATOM 1153 N N . PHE A 1 153 ? 75.404 -20.346 34.015 1.00 59.48 ? 184 PHE B N 1 ATOM 1154 C CA . PHE A 1 153 ? 75.384 -21.646 34.687 1.00 59.34 ? 184 PHE B CA 1 ATOM 1155 C C . PHE A 1 153 ? 74.443 -22.662 34.085 1.00 59.61 ? 184 PHE B C 1 ATOM 1156 O O . PHE A 1 153 ? 74.315 -23.769 34.601 1.00 59.64 ? 184 PHE B O 1 ATOM 1157 C CB . PHE A 1 153 ? 75.145 -21.511 36.180 1.00 59.36 ? 184 PHE B CB 1 ATOM 1158 C CG . PHE A 1 153 ? 76.322 -21.904 36.999 1.00 59.04 ? 184 PHE B CG 1 ATOM 1159 C CD1 . PHE A 1 153 ? 77.013 -23.065 36.710 1.00 58.96 ? 184 PHE B CD1 1 ATOM 1160 C CD2 . PHE A 1 153 ? 76.760 -21.098 38.040 1.00 58.89 ? 184 PHE B CD2 1 ATOM 1161 C CE1 . PHE A 1 153 ? 78.108 -23.440 37.456 1.00 58.80 ? 184 PHE B CE1 1 ATOM 1162 C CE2 . PHE A 1 153 ? 77.859 -21.457 38.788 1.00 58.69 ? 184 PHE B CE2 1 ATOM 1163 C CZ . PHE A 1 153 ? 78.535 -22.637 38.498 1.00 58.67 ? 184 PHE B CZ 1 ATOM 1164 N N . GLY A 1 154 ? 73.777 -22.267 33.006 1.00 56.41 ? 185 GLY B N 1 ATOM 1165 C CA . GLY A 1 154 ? 72.764 -23.091 32.382 1.00 56.74 ? 185 GLY B CA 1 ATOM 1166 C C . GLY A 1 154 ? 73.314 -24.362 31.758 1.00 56.54 ? 185 GLY B C 1 ATOM 1167 O O . GLY A 1 154 ? 74.506 -24.679 31.881 1.00 56.14 ? 185 GLY B O 1 ATOM 1168 N N . GLY A 1 155 ? 72.428 -25.112 31.108 1.00 66.71 ? 186 GLY B N 1 ATOM 1169 C CA . GLY A 1 155 ? 72.814 -26.345 30.451 1.00 66.60 ? 186 GLY B CA 1 ATOM 1170 C C . GLY A 1 155 ? 73.393 -27.418 31.360 1.00 66.33 ? 186 GLY B C 1 ATOM 1171 O O . GLY A 1 155 ? 74.118 -28.295 30.905 1.00 65.98 ? 186 GLY B O 1 ATOM 1172 N N . SER A 1 156 ? 73.075 -27.359 32.646 1.00 53.09 ? 187 SER B N 1 ATOM 1173 C CA . SER A 1 156 ? 73.484 -28.390 33.601 1.00 53.14 ? 187 SER B CA 1 ATOM 1174 C C . SER A 1 156 ? 72.218 -28.867 34.274 1.00 53.90 ? 187 SER B C 1 ATOM 1175 O O . SER A 1 156 ? 71.123 -28.560 33.795 1.00 54.24 ? 187 SER B O 1 ATOM 1176 C CB . SER A 1 156 ? 74.490 -27.857 34.629 1.00 52.88 ? 187 SER B CB 1 ATOM 1177 O OG . SER A 1 156 ? 75.737 -27.541 34.017 1.00 52.48 ? 187 SER B OG 1 ATOM 1178 N N . TYR A 1 157 ? 72.348 -29.678 35.317 1.00 66.53 ? 188 TYR B N 1 ATOM 1179 C CA . TYR A 1 157 ? 71.190 -29.946 36.148 1.00 67.49 ? 188 TYR B CA 1 ATOM 1180 C C . TYR A 1 157 ? 71.475 -29.433 37.533 1.00 67.75 ? 188 TYR B C 1 ATOM 1181 O O . TYR A 1 157 ? 71.987 -30.181 38.347 1.00 68.29 ? 188 TYR B O 1 ATOM 1182 C CB . TYR A 1 157 ? 70.971 -31.456 36.236 1.00 68.23 ? 188 TYR B CB 1 ATOM 1183 C CG . TYR A 1 157 ? 71.383 -32.193 34.988 1.00 67.72 ? 188 TYR B CG 1 ATOM 1184 C CD1 . TYR A 1 157 ? 72.710 -32.533 34.773 1.00 67.16 ? 188 TYR B CD1 1 ATOM 1185 C CD2 . TYR A 1 157 ? 70.450 -32.544 34.025 1.00 67.82 ? 188 TYR B CD2 1 ATOM 1186 C CE1 . TYR A 1 157 ? 73.103 -33.196 33.632 1.00 66.74 ? 188 TYR B CE1 1 ATOM 1187 C CE2 . TYR A 1 157 ? 70.830 -33.215 32.876 1.00 67.38 ? 188 TYR B CE2 1 ATOM 1188 C CZ . TYR A 1 157 ? 72.162 -33.539 32.685 1.00 66.85 ? 188 TYR B CZ 1 ATOM 1189 O OH . TYR A 1 157 ? 72.570 -34.202 31.548 1.00 66.48 ? 188 TYR B OH 1 ATOM 1190 N N . PHE A 1 158 ? 71.008 -28.234 37.864 1.00 52.27 ? 189 PHE B N 1 ATOM 1191 C CA . PHE A 1 158 ? 71.393 -27.629 39.139 1.00 52.47 ? 189 PHE B CA 1 ATOM 1192 C C . PHE A 1 158 ? 70.219 -27.691 40.072 1.00 53.26 ? 189 PHE B C 1 ATOM 1193 O O . PHE A 1 158 ? 69.168 -27.155 39.777 1.00 53.52 ? 189 PHE B O 1 ATOM 1194 C CB . PHE A 1 158 ? 71.879 -26.184 38.976 1.00 52.24 ? 189 PHE B CB 1 ATOM 1195 C CG . PHE A 1 158 ? 73.374 -26.050 38.902 1.00 51.76 ? 189 PHE B CG 1 ATOM 1196 C CD1 . PHE A 1 158 ? 74.151 -26.164 40.035 1.00 51.81 ? 189 PHE B CD1 1 ATOM 1197 C CD2 . PHE A 1 158 ? 74.004 -25.803 37.699 1.00 51.38 ? 189 PHE B CD2 1 ATOM 1198 C CE1 . PHE A 1 158 ? 75.532 -26.040 39.969 1.00 51.43 ? 189 PHE B CE1 1 ATOM 1199 C CE2 . PHE A 1 158 ? 75.380 -25.680 37.626 1.00 51.05 ? 189 PHE B CE2 1 ATOM 1200 C CZ . PHE A 1 158 ? 76.146 -25.799 38.755 1.00 51.05 ? 189 PHE B CZ 1 ATOM 1201 N N . GLU A 1 159 ? 70.382 -28.378 41.187 1.00 70.07 ? 190 GLU B N 1 ATOM 1202 C CA . GLU A 1 159 ? 69.294 -28.505 42.129 1.00 71.26 ? 190 GLU B CA 1 ATOM 1203 C C . GLU A 1 159 ? 69.175 -27.272 43.013 1.00 71.21 ? 190 GLU B C 1 ATOM 1204 O O . GLU A 1 159 ? 70.141 -26.527 43.210 1.00 70.33 ? 190 GLU B O 1 ATOM 1205 C CB . GLU A 1 159 ? 69.499 -29.746 42.982 1.00 72.52 ? 190 GLU B CB 1 ATOM 1206 C CG . GLU A 1 159 ? 69.921 -30.951 42.180 1.00 72.52 ? 190 GLU B CG 1 ATOM 1207 C CD . GLU A 1 159 ? 70.382 -32.095 43.052 1.00 73.88 ? 190 GLU B CD 1 ATOM 1208 O OE1 . GLU A 1 159 ? 69.940 -32.165 44.224 1.00 75.01 ? 190 GLU B OE1 1 ATOM 1209 O OE2 . GLU A 1 159 ? 71.194 -32.913 42.561 1.00 73.94 ? 190 GLU B OE2 1 ATOM 1210 N N . GLY A 1 160 ? 67.978 -27.052 43.542 1.00 77.35 ? 191 GLY B N 1 ATOM 1211 C CA . GLY A 1 160 ? 67.793 -26.079 44.602 1.00 77.49 ? 191 GLY B CA 1 ATOM 1212 C C . GLY A 1 160 ? 67.412 -24.721 44.085 1.00 76.77 ? 191 GLY B C 1 ATOM 1213 O O . GLY A 1 160 ? 67.230 -24.551 42.892 1.00 76.29 ? 191 GLY B O 1 ATOM 1214 N N . GLU A 1 161 ? 67.292 -23.751 44.980 1.00 64.27 ? 192 GLU B N 1 ATOM 1215 C CA . GLU A 1 161 ? 66.840 -22.425 44.580 1.00 63.80 ? 192 GLU B CA 1 ATOM 1216 C C . GLU A 1 161 ? 67.968 -21.556 44.067 1.00 62.58 ? 192 GLU B C 1 ATOM 1217 O O . GLU A 1 161 ? 69.139 -21.942 44.080 1.00 62.06 ? 192 GLU B O 1 ATOM 1218 C CB . GLU A 1 161 ? 66.159 -21.708 45.741 1.00 64.43 ? 192 GLU B CB 1 ATOM 1219 C CG . GLU A 1 161 ? 64.866 -22.341 46.186 1.00 65.81 ? 192 GLU B CG 1 ATOM 1220 C CD . GLU A 1 161 ? 64.331 -21.724 47.454 1.00 66.59 ? 192 GLU B CD 1 ATOM 1221 O OE1 . GLU A 1 161 ? 64.967 -21.904 48.517 1.00 66.66 ? 192 GLU B OE1 1 ATOM 1222 O OE2 . GLU A 1 161 ? 63.278 -21.055 47.384 1.00 67.15 ? 192 GLU B OE2 1 ATOM 1223 N N . ILE A 1 162 ? 67.587 -20.365 43.624 1.00 63.25 ? 193 ILE B N 1 ATOM 1224 C CA . ILE A 1 162 ? 68.529 -19.386 43.113 1.00 62.28 ? 193 ILE B CA 1 ATOM 1225 C C . ILE A 1 162 ? 68.961 -18.535 44.282 1.00 62.22 ? 193 ILE B C 1 ATOM 1226 O O . ILE A 1 162 ? 68.144 -17.789 44.825 1.00 62.69 ? 193 ILE B O 1 ATOM 1227 C CB . ILE A 1 162 ? 67.861 -18.460 42.078 1.00 62.22 ? 193 ILE B CB 1 ATOM 1228 C CG1 . ILE A 1 162 ? 67.321 -19.271 40.898 1.00 62.41 ? 193 ILE B CG1 1 ATOM 1229 C CG2 . ILE A 1 162 ? 68.831 -17.399 41.622 1.00 61.42 ? 193 ILE B CG2 1 ATOM 1230 C CD1 . ILE A 1 162 ? 66.982 -18.455 39.680 1.00 62.34 ? 193 ILE B CD1 1 ATOM 1231 N N . PRO A 1 163 ? 70.237 -18.632 44.683 1.00 57.29 ? 194 PRO B N 1 ATOM 1232 C CA . PRO A 1 163 ? 70.656 -17.906 45.879 1.00 57.36 ? 194 PRO B CA 1 ATOM 1233 C C . PRO A 1 163 ? 70.311 -16.437 45.747 1.00 57.28 ? 194 PRO B C 1 ATOM 1234 O O . PRO A 1 163 ? 70.699 -15.814 44.766 1.00 56.75 ? 194 PRO B O 1 ATOM 1235 C CB . PRO A 1 163 ? 72.178 -18.076 45.873 1.00 56.61 ? 194 PRO B CB 1 ATOM 1236 C CG . PRO A 1 163 ? 72.520 -18.383 44.497 1.00 56.61 ? 194 PRO B CG 1 ATOM 1237 C CD . PRO A 1 163 ? 71.383 -19.194 43.966 1.00 56.72 ? 194 PRO B CD 1 ATOM 1238 N N . ALA A 1 164 ? 69.597 -15.887 46.723 1.00 55.94 ? 195 ALA B N 1 ATOM 1239 C CA . ALA A 1 164 ? 69.236 -14.488 46.653 1.00 56.55 ? 195 ALA B CA 1 ATOM 1240 C C . ALA A 1 164 ? 70.490 -13.645 46.700 1.00 56.37 ? 195 ALA B C 1 ATOM 1241 O O . ALA A 1 164 ? 70.526 -12.541 46.178 1.00 56.87 ? 195 ALA B O 1 ATOM 1242 C CB . ALA A 1 164 ? 68.332 -14.133 47.771 1.00 57.63 ? 195 ALA B CB 1 ATOM 1243 N N . ALA A 1 165 ? 71.535 -14.199 47.294 1.00 60.85 ? 196 ALA B N 1 ATOM 1244 C CA . ALA A 1 165 ? 72.821 -13.525 47.391 1.00 60.19 ? 196 ALA B CA 1 ATOM 1245 C C . ALA A 1 165 ? 73.265 -12.956 46.045 1.00 59.61 ? 196 ALA B C 1 ATOM 1246 O O . ALA A 1 165 ? 73.879 -11.875 45.986 1.00 59.34 ? 196 ALA B O 1 ATOM 1247 C CB . ALA A 1 165 ? 73.872 -14.486 47.925 1.00 60.15 ? 196 ALA B CB 1 ATOM 1248 N N . TYR A 1 166 ? 72.923 -13.661 44.968 1.00 67.99 ? 197 TYR B N 1 ATOM 1249 C CA . TYR A 1 166 ? 73.334 -13.251 43.629 1.00 67.59 ? 197 TYR B CA 1 ATOM 1250 C C . TYR A 1 166 ? 72.962 -11.793 43.284 1.00 67.66 ? 197 TYR B C 1 ATOM 1251 O O . TYR A 1 166 ? 73.674 -11.131 42.523 1.00 67.32 ? 197 TYR B O 1 ATOM 1252 C CB . TYR A 1 166 ? 72.805 -14.220 42.560 1.00 67.77 ? 197 TYR B CB 1 ATOM 1253 C CG . TYR A 1 166 ? 73.580 -15.533 42.392 1.00 67.53 ? 197 TYR B CG 1 ATOM 1254 C CD1 . TYR A 1 166 ? 74.702 -15.821 43.168 1.00 67.33 ? 197 TYR B CD1 1 ATOM 1255 C CD2 . TYR A 1 166 ? 73.185 -16.478 41.444 1.00 67.58 ? 197 TYR B CD2 1 ATOM 1256 C CE1 . TYR A 1 166 ? 75.396 -17.012 43.006 1.00 67.21 ? 197 TYR B CE1 1 ATOM 1257 C CE2 . TYR A 1 166 ? 73.867 -17.657 41.283 1.00 67.39 ? 197 TYR B CE2 1 ATOM 1258 C CZ . TYR A 1 166 ? 74.967 -17.917 42.063 1.00 67.22 ? 197 TYR B CZ 1 ATOM 1259 O OH . TYR A 1 166 ? 75.643 -19.096 41.900 1.00 67.15 ? 197 TYR B OH 1 ATOM 1260 N N . GLY A 1 167 ? 71.902 -11.262 43.887 1.00 56.69 ? 198 GLY B N 1 ATOM 1261 C CA . GLY A 1 167 ? 71.479 -9.910 43.567 1.00 57.62 ? 198 GLY B CA 1 ATOM 1262 C C . GLY A 1 167 ? 72.528 -8.867 43.903 1.00 57.88 ? 198 GLY B C 1 ATOM 1263 O O . GLY A 1 167 ? 72.340 -7.677 43.656 1.00 58.83 ? 198 GLY B O 1 ATOM 1264 N N . GLY A 1 168 ? 73.636 -9.313 44.481 1.00 60.12 ? 199 GLY B N 1 ATOM 1265 C CA . GLY A 1 168 ? 74.678 -8.402 44.891 1.00 59.75 ? 199 GLY B CA 1 ATOM 1266 C C . GLY A 1 168 ? 75.878 -8.297 43.979 1.00 59.44 ? 199 GLY B C 1 ATOM 1267 O O . GLY A 1 168 ? 76.933 -7.842 44.407 1.00 59.11 ? 199 GLY B O 1 ATOM 1268 N N . LEU A 1 169 ? 75.745 -8.687 42.720 1.00 65.92 ? 200 LEU B N 1 ATOM 1269 C CA . LEU A 1 169 ? 76.866 -8.459 41.821 1.00 65.81 ? 200 LEU B CA 1 ATOM 1270 C C . LEU A 1 169 ? 76.558 -7.214 41.010 1.00 66.11 ? 200 LEU B C 1 ATOM 1271 O O . LEU A 1 169 ? 75.899 -7.276 39.967 1.00 66.38 ? 200 LEU B O 1 ATOM 1272 C CB . LEU A 1 169 ? 77.024 -9.650 40.887 1.00 65.79 ? 200 LEU B CB 1 ATOM 1273 C CG . LEU A 1 169 ? 76.898 -10.998 41.593 1.00 65.63 ? 200 LEU B CG 1 ATOM 1274 C CD1 . LEU A 1 169 ? 76.367 -12.015 40.625 1.00 65.89 ? 200 LEU B CD1 1 ATOM 1275 C CD2 . LEU A 1 169 ? 78.230 -11.464 42.160 1.00 64.95 ? 200 LEU B CD2 1 ATOM 1276 N N . GLN A 1 170 ? 77.148 -6.104 41.439 1.00 93.34 ? 201 GLN B N 1 ATOM 1277 C CA . GLN A 1 170 ? 76.672 -4.816 41.002 1.00 93.86 ? 201 GLN B CA 1 ATOM 1278 C C . GLN A 1 170 ? 76.932 -4.718 39.539 1.00 94.04 ? 201 GLN B C 1 ATOM 1279 O O . GLN A 1 170 ? 76.168 -4.125 38.793 1.00 94.60 ? 201 GLN B O 1 ATOM 1280 C CB . GLN A 1 170 ? 77.398 -3.684 41.708 1.00 94.18 ? 201 GLN B CB 1 ATOM 1281 C CG . GLN A 1 170 ? 76.755 -2.333 41.410 1.00 95.08 ? 201 GLN B CG 1 ATOM 1282 C CD . GLN A 1 170 ? 77.674 -1.147 41.652 1.00 95.48 ? 201 GLN B CD 1 ATOM 1283 O OE1 . GLN A 1 170 ? 78.888 -1.302 41.806 1.00 95.08 ? 201 GLN B OE1 1 ATOM 1284 N NE2 . GLN A 1 170 ? 77.093 0.051 41.681 1.00 96.35 ? 201 GLN B NE2 1 ATOM 1285 N N . ARG A 1 171 ? 78.015 -5.345 39.125 1.00 82.58 ? 202 ARG B N 1 ATOM 1286 C CA . ARG A 1 171 ? 78.499 -5.152 37.781 1.00 82.90 ? 202 ARG B CA 1 ATOM 1287 C C . ARG A 1 171 ? 78.005 -6.192 36.802 1.00 83.06 ? 202 ARG B C 1 ATOM 1288 O O . ARG A 1 171 ? 78.401 -6.176 35.646 1.00 83.38 ? 202 ARG B O 1 ATOM 1289 C CB . ARG A 1 171 ? 80.019 -5.036 37.788 1.00 82.85 ? 202 ARG B CB 1 ATOM 1290 C CG . ARG A 1 171 ? 80.461 -3.742 38.457 1.00 83.03 ? 202 ARG B CG 1 ATOM 1291 C CD . ARG A 1 171 ? 81.876 -3.792 38.975 1.00 82.75 ? 202 ARG B CD 1 ATOM 1292 N NE . ARG A 1 171 ? 82.234 -2.564 39.686 1.00 83.28 ? 202 ARG B NE 1 ATOM 1293 C CZ . ARG A 1 171 ? 82.065 -2.373 40.992 1.00 83.07 ? 202 ARG B CZ 1 ATOM 1294 N NH1 . ARG A 1 171 ? 81.538 -3.328 41.748 1.00 82.39 ? 202 ARG B NH1 1 ATOM 1295 N NH2 . ARG A 1 171 ? 82.424 -1.224 41.547 1.00 83.58 ? 202 ARG B NH2 1 ATOM 1296 N N . LEU A 1 172 ? 77.112 -7.068 37.251 1.00 57.73 ? 203 LEU B N 1 ATOM 1297 C CA . LEU A 1 172 ? 76.662 -8.171 36.406 1.00 57.19 ? 203 LEU B CA 1 ATOM 1298 C C . LEU A 1 172 ? 75.722 -7.734 35.276 1.00 58.06 ? 203 LEU B C 1 ATOM 1299 O O . LEU A 1 172 ? 74.642 -7.195 35.520 1.00 58.79 ? 203 LEU B O 1 ATOM 1300 C CB . LEU A 1 172 ? 75.940 -9.214 37.250 1.00 56.47 ? 203 LEU B CB 1 ATOM 1301 C CG . LEU A 1 172 ? 75.325 -10.327 36.413 1.00 55.99 ? 203 LEU B CG 1 ATOM 1302 C CD1 . LEU A 1 172 ? 76.316 -11.429 36.275 1.00 54.99 ? 203 LEU B CD1 1 ATOM 1303 C CD2 . LEU A 1 172 ? 74.082 -10.850 37.051 1.00 55.91 ? 203 LEU B CD2 1 ATOM 1304 N N . LYS A 1 173 ? 76.164 -7.959 34.039 1.00 61.04 ? 204 LYS B N 1 ATOM 1305 C CA . LYS A 1 173 ? 75.394 -7.662 32.829 1.00 61.63 ? 204 LYS B CA 1 ATOM 1306 C C . LYS A 1 173 ? 74.441 -8.763 32.354 1.00 61.76 ? 204 LYS B C 1 ATOM 1307 O O . LYS A 1 173 ? 73.354 -8.490 31.851 1.00 62.17 ? 204 LYS B O 1 ATOM 1308 C CB . LYS A 1 173 ? 76.339 -7.269 31.693 1.00 62.03 ? 204 LYS B CB 1 ATOM 1309 C CG . LYS A 1 173 ? 76.795 -5.817 31.710 1.00 62.42 ? 204 LYS B CG 1 ATOM 1310 C CD . LYS A 1 173 ? 77.969 -5.603 30.750 1.00 62.78 ? 204 LYS B CD 1 ATOM 1311 C CE . LYS A 1 173 ? 78.244 -4.122 30.498 1.00 63.20 ? 204 LYS B CE 1 ATOM 1312 N NZ . LYS A 1 173 ? 79.502 -3.915 29.720 1.00 63.52 ? 204 LYS B NZ 1 ATOM 1313 N N . PHE A 1 174 ? 74.886 -10.008 32.478 1.00 57.29 ? 205 PHE B N 1 ATOM 1314 C CA . PHE A 1 174 ? 74.291 -11.126 31.754 1.00 56.99 ? 205 PHE B CA 1 ATOM 1315 C C . PHE A 1 174 ? 74.190 -12.337 32.647 1.00 56.14 ? 205 PHE B C 1 ATOM 1316 O O . PHE A 1 174 ? 75.191 -12.762 33.212 1.00 55.56 ? 205 PHE B O 1 ATOM 1317 C CB . PHE A 1 174 ? 75.193 -11.495 30.582 1.00 56.99 ? 205 PHE B CB 1 ATOM 1318 C CG . PHE A 1 174 ? 74.751 -12.712 29.824 1.00 56.75 ? 205 PHE B CG 1 ATOM 1319 C CD1 . PHE A 1 174 ? 74.999 -13.985 30.305 1.00 55.87 ? 205 PHE B CD1 1 ATOM 1320 C CD2 . PHE A 1 174 ? 74.121 -12.580 28.601 1.00 57.44 ? 205 PHE B CD2 1 ATOM 1321 C CE1 . PHE A 1 174 ? 74.602 -15.088 29.611 1.00 55.67 ? 205 PHE B CE1 1 ATOM 1322 C CE2 . PHE A 1 174 ? 73.732 -13.684 27.889 1.00 57.24 ? 205 PHE B CE2 1 ATOM 1323 C CZ . PHE A 1 174 ? 73.968 -14.942 28.398 1.00 56.33 ? 205 PHE B CZ 1 ATOM 1324 N N . ILE A 1 175 ? 73.009 -12.936 32.736 1.00 55.57 ? 206 ILE B N 1 ATOM 1325 C CA . ILE A 1 175 ? 72.844 -14.065 33.630 1.00 54.65 ? 206 ILE B CA 1 ATOM 1326 C C . ILE A 1 175 ? 72.077 -15.218 33.002 1.00 54.52 ? 206 ILE B C 1 ATOM 1327 O O . ILE A 1 175 ? 70.896 -15.100 32.687 1.00 55.04 ? 206 ILE B O 1 ATOM 1328 C CB . ILE A 1 175 ? 72.163 -13.609 34.913 1.00 54.93 ? 206 ILE B CB 1 ATOM 1329 C CG1 . ILE A 1 175 ? 71.861 -14.789 35.813 1.00 54.28 ? 206 ILE B CG1 1 ATOM 1330 C CG2 . ILE A 1 175 ? 70.916 -12.840 34.596 1.00 55.94 ? 206 ILE B CG2 1 ATOM 1331 C CD1 . ILE A 1 175 ? 73.066 -15.286 36.506 1.00 53.60 ? 206 ILE B CD1 1 ATOM 1332 N N . HIS A 1 176 ? 72.744 -16.352 32.825 1.00 56.20 ? 207 HIS B N 1 ATOM 1333 C CA . HIS A 1 176 ? 72.059 -17.510 32.268 1.00 56.29 ? 207 HIS B CA 1 ATOM 1334 C C . HIS A 1 176 ? 72.107 -18.686 33.245 1.00 55.86 ? 207 HIS B C 1 ATOM 1335 O O . HIS A 1 176 ? 73.153 -19.313 33.449 1.00 55.39 ? 207 HIS B O 1 ATOM 1336 C CB . HIS A 1 176 ? 72.704 -17.871 30.926 1.00 56.33 ? 207 HIS B CB 1 ATOM 1337 C CG . HIS A 1 176 ? 72.007 -18.961 30.180 1.00 56.44 ? 207 HIS B CG 1 ATOM 1338 N ND1 . HIS A 1 176 ? 72.040 -20.278 30.583 1.00 56.07 ? 207 HIS B ND1 1 ATOM 1339 C CD2 . HIS A 1 176 ? 71.285 -18.936 29.039 1.00 56.92 ? 207 HIS B CD2 1 ATOM 1340 C CE1 . HIS A 1 176 ? 71.351 -21.013 29.734 1.00 56.29 ? 207 HIS B CE1 1 ATOM 1341 N NE2 . HIS A 1 176 ? 70.884 -20.224 28.785 1.00 56.79 ? 207 HIS B NE2 1 ATOM 1342 N N . LEU A 1 177 ? 70.962 -18.939 33.875 1.00 57.50 ? 208 LEU B N 1 ATOM 1343 C CA . LEU A 1 177 ? 70.697 -20.143 34.666 1.00 57.48 ? 208 LEU B CA 1 ATOM 1344 C C . LEU A 1 177 ? 69.792 -21.144 33.964 1.00 57.88 ? 208 LEU B C 1 ATOM 1345 O O . LEU A 1 177 ? 69.353 -22.099 34.601 1.00 58.08 ? 208 LEU B O 1 ATOM 1346 C CB . LEU A 1 177 ? 70.105 -19.783 36.023 1.00 57.74 ? 208 LEU B CB 1 ATOM 1347 C CG . LEU A 1 177 ? 70.890 -18.700 36.761 1.00 57.42 ? 208 LEU B CG 1 ATOM 1348 C CD1 . LEU A 1 177 ? 70.238 -18.389 38.092 1.00 57.79 ? 208 LEU B CD1 1 ATOM 1349 C CD2 . LEU A 1 177 ? 72.338 -19.134 36.940 1.00 56.81 ? 208 LEU B CD2 1 ATOM 1350 N N . ALA A 1 178 ? 69.453 -20.864 32.698 1.00 53.30 ? 209 ALA B N 1 ATOM 1351 C CA . ALA A 1 178 ? 68.383 -21.552 31.955 1.00 53.57 ? 209 ALA B CA 1 ATOM 1352 C C . ALA A 1 178 ? 68.678 -22.994 31.654 1.00 53.02 ? 209 ALA B C 1 ATOM 1353 O O . ALA A 1 178 ? 69.823 -23.351 31.377 1.00 52.52 ? 209 ALA B O 1 ATOM 1354 C CB . ALA A 1 178 ? 68.055 -20.825 30.657 1.00 54.11 ? 209 ALA B CB 1 ATOM 1355 N N . GLY A 1 179 ? 67.631 -23.815 31.690 1.00 53.19 ? 210 GLY B N 1 ATOM 1356 C CA . GLY A 1 179 ? 67.773 -25.242 31.456 1.00 52.76 ? 210 GLY B CA 1 ATOM 1357 C C . GLY A 1 179 ? 68.545 -26.005 32.523 1.00 52.27 ? 210 GLY B C 1 ATOM 1358 O O . GLY A 1 179 ? 69.574 -26.644 32.278 1.00 51.77 ? 210 GLY B O 1 ATOM 1359 N N . ASN A 1 180 ? 68.050 -25.901 33.738 1.00 53.61 ? 211 ASN B N 1 ATOM 1360 C CA . ASN A 1 180 ? 68.574 -26.657 34.850 1.00 53.52 ? 211 ASN B CA 1 ATOM 1361 C C . ASN A 1 180 ? 67.371 -27.278 35.544 1.00 54.35 ? 211 ASN B C 1 ATOM 1362 O O . ASN A 1 180 ? 66.287 -27.370 34.956 1.00 54.82 ? 211 ASN B O 1 ATOM 1363 C CB . ASN A 1 180 ? 69.412 -25.785 35.795 1.00 53.21 ? 211 ASN B CB 1 ATOM 1364 C CG . ASN A 1 180 ? 70.851 -25.606 35.315 1.00 52.53 ? 211 ASN B CG 1 ATOM 1365 O OD1 . ASN A 1 180 ? 71.776 -26.257 35.805 1.00 52.34 ? 211 ASN B OD1 1 ATOM 1366 N ND2 . ASN A 1 180 ? 71.040 -24.716 34.357 1.00 52.54 ? 211 ASN B ND2 1 ATOM 1367 N N . VAL A 1 181 ? 67.576 -27.815 36.735 1.00 59.10 ? 212 VAL B N 1 ATOM 1368 C CA . VAL A 1 181 ? 66.444 -28.239 37.529 1.00 60.25 ? 212 VAL B CA 1 ATOM 1369 C C . VAL A 1 181 ? 65.982 -27.220 38.574 1.00 60.63 ? 212 VAL B C 1 ATOM 1370 O O . VAL A 1 181 ? 65.113 -27.546 39.385 1.00 61.65 ? 212 VAL B O 1 ATOM 1371 C CB . VAL A 1 181 ? 66.665 -29.598 38.174 1.00 60.89 ? 212 VAL B CB 1 ATOM 1372 C CG1 . VAL A 1 181 ? 65.842 -30.624 37.433 1.00 61.49 ? 212 VAL B CG1 1 ATOM 1373 C CG2 . VAL A 1 181 ? 68.161 -29.948 38.202 1.00 60.18 ? 212 VAL B CG2 1 ATOM 1374 N N . LEU A 1 182 ? 66.543 -26.005 38.565 1.00 59.40 ? 213 LEU B N 1 ATOM 1375 C CA . LEU A 1 182 ? 66.360 -25.049 39.682 1.00 59.64 ? 213 LEU B CA 1 ATOM 1376 C C . LEU A 1 182 ? 64.878 -24.733 39.978 1.00 60.69 ? 213 LEU B C 1 ATOM 1377 O O . LEU A 1 182 ? 64.019 -24.903 39.111 1.00 61.06 ? 213 LEU B O 1 ATOM 1378 C CB . LEU A 1 182 ? 67.164 -23.765 39.449 1.00 58.75 ? 213 LEU B CB 1 ATOM 1379 C CG . LEU A 1 182 ? 68.673 -23.957 39.313 1.00 57.90 ? 213 LEU B CG 1 ATOM 1380 C CD1 . LEU A 1 182 ? 69.306 -22.871 38.452 1.00 57.26 ? 213 LEU B CD1 1 ATOM 1381 C CD2 . LEU A 1 182 ? 69.319 -23.994 40.683 1.00 58.00 ? 213 LEU B CD2 1 ATOM 1382 N N . GLY A 1 183 ? 64.574 -24.328 41.213 1.00 55.89 ? 214 GLY B N 1 ATOM 1383 C CA . GLY A 1 183 ? 63.188 -24.237 41.660 1.00 56.90 ? 214 GLY B CA 1 ATOM 1384 C C . GLY A 1 183 ? 62.701 -23.183 42.662 1.00 57.67 ? 214 GLY B C 1 ATOM 1385 O O . GLY A 1 183 ? 63.470 -22.388 43.219 1.00 57.48 ? 214 GLY B O 1 ATOM 1386 N N . GLY A 1 184 ? 61.386 -23.164 42.864 1.00 90.50 ? 215 GLY B N 1 ATOM 1387 C CA . GLY A 1 184 ? 60.779 -22.327 43.881 1.00 91.04 ? 215 GLY B CA 1 ATOM 1388 C C . GLY A 1 184 ? 60.427 -20.904 43.483 1.00 90.65 ? 215 GLY B C 1 ATOM 1389 O O . GLY A 1 184 ? 60.081 -20.625 42.336 1.00 90.41 ? 215 GLY B O 1 ATOM 1390 N N . LYS A 1 185 ? 60.490 -20.004 44.459 1.00 80.64 ? 216 LYS B N 1 ATOM 1391 C CA . LYS A 1 185 ? 60.138 -18.610 44.252 1.00 80.41 ? 216 LYS B CA 1 ATOM 1392 C C . LYS A 1 185 ? 61.371 -17.939 43.695 1.00 79.15 ? 216 LYS B C 1 ATOM 1393 O O . LYS A 1 185 ? 62.478 -18.282 44.100 1.00 78.50 ? 216 LYS B O 1 ATOM 1394 C CB . LYS A 1 185 ? 59.750 -17.971 45.584 1.00 80.84 ? 216 LYS B CB 1 ATOM 1395 C CG . LYS A 1 185 ? 58.697 -18.739 46.374 1.00 82.21 ? 216 LYS B CG 1 ATOM 1396 C CD . LYS A 1 185 ? 57.346 -18.691 45.679 1.00 83.30 ? 216 LYS B CD 1 ATOM 1397 C CE . LYS A 1 185 ? 56.739 -17.298 45.711 1.00 83.49 ? 216 LYS B CE 1 ATOM 1398 N NZ . LYS A 1 185 ? 55.845 -17.097 46.886 1.00 84.24 ? 216 LYS B NZ 1 ATOM 1399 N N . LEU A 1 186 ? 61.193 -17.012 42.753 1.00 59.95 ? 217 LEU B N 1 ATOM 1400 C CA . LEU A 1 186 ? 62.319 -16.245 42.211 1.00 59.26 ? 217 LEU B CA 1 ATOM 1401 C C . LEU A 1 186 ? 62.633 -15.118 43.186 1.00 59.58 ? 217 LEU B C 1 ATOM 1402 O O . LEU A 1 186 ? 61.769 -14.289 43.469 1.00 60.53 ? 217 LEU B O 1 ATOM 1403 C CB . LEU A 1 186 ? 61.981 -15.635 40.853 1.00 59.46 ? 217 LEU B CB 1 ATOM 1404 C CG . LEU A 1 186 ? 61.255 -16.378 39.733 1.00 59.59 ? 217 LEU B CG 1 ATOM 1405 C CD1 . LEU A 1 186 ? 60.586 -15.365 38.825 1.00 60.37 ? 217 LEU B CD1 1 ATOM 1406 C CD2 . LEU A 1 186 ? 62.202 -17.239 38.926 1.00 58.54 ? 217 LEU B CD2 1 ATOM 1407 N N . PRO A 1 187 ? 63.867 -15.073 43.701 1.00 60.20 ? 218 PRO B N 1 ATOM 1408 C CA . PRO A 1 187 ? 64.124 -14.160 44.807 1.00 60.53 ? 218 PRO B CA 1 ATOM 1409 C C . PRO A 1 187 ? 64.058 -12.703 44.350 1.00 60.94 ? 218 PRO B C 1 ATOM 1410 O O . PRO A 1 187 ? 64.738 -12.342 43.389 1.00 60.42 ? 218 PRO B O 1 ATOM 1411 C CB . PRO A 1 187 ? 65.539 -14.548 45.231 1.00 59.58 ? 218 PRO B CB 1 ATOM 1412 C CG . PRO A 1 187 ? 66.184 -14.978 43.989 1.00 58.83 ? 218 PRO B CG 1 ATOM 1413 C CD . PRO A 1 187 ? 65.114 -15.593 43.126 1.00 59.29 ? 218 PRO B CD 1 ATOM 1414 N N . PRO A 1 188 ? 63.258 -11.871 45.049 1.00 61.86 ? 219 PRO B N 1 ATOM 1415 C CA . PRO A 1 188 ? 63.049 -10.459 44.718 1.00 62.81 ? 219 PRO B CA 1 ATOM 1416 C C . PRO A 1 188 ? 64.346 -9.671 44.619 1.00 62.44 ? 219 PRO B C 1 ATOM 1417 O O . PRO A 1 188 ? 64.435 -8.748 43.798 1.00 62.95 ? 219 PRO B O 1 ATOM 1418 C CB . PRO A 1 188 ? 62.204 -9.967 45.888 1.00 64.22 ? 219 PRO B CB 1 ATOM 1419 C CG . PRO A 1 188 ? 61.374 -11.124 46.219 1.00 64.09 ? 219 PRO B CG 1 ATOM 1420 C CD . PRO A 1 188 ? 62.292 -12.318 46.068 1.00 62.66 ? 219 PRO B CD 1 ATOM 1421 N N . ARG A 1 189 ? 65.350 -10.071 45.400 1.00 75.24 ? 220 ARG B N 1 ATOM 1422 C CA . ARG A 1 189 ? 66.614 -9.346 45.493 1.00 74.46 ? 220 ARG B CA 1 ATOM 1423 C C . ARG A 1 189 ? 67.241 -9.158 44.109 1.00 74.08 ? 220 ARG B C 1 ATOM 1424 O O . ARG A 1 189 ? 68.078 -8.273 43.889 1.00 73.61 ? 220 ARG B O 1 ATOM 1425 C CB . ARG A 1 189 ? 67.569 -10.065 46.440 1.00 74.13 ? 220 ARG B CB 1 ATOM 1426 C CG . ARG A 1 189 ? 68.940 -9.445 46.499 1.00 73.34 ? 220 ARG B CG 1 ATOM 1427 C CD . ARG A 1 189 ? 69.219 -8.808 47.833 1.00 73.38 ? 220 ARG B CD 1 ATOM 1428 N NE . ARG A 1 189 ? 70.134 -9.615 48.635 1.00 73.24 ? 220 ARG B NE 1 ATOM 1429 C CZ . ARG A 1 189 ? 69.746 -10.575 49.467 1.00 73.83 ? 220 ARG B CZ 1 ATOM 1430 N NH1 . ARG A 1 189 ? 68.457 -10.851 49.607 1.00 74.55 ? 220 ARG B NH1 1 ATOM 1431 N NH2 . ARG A 1 189 ? 70.644 -11.255 50.158 1.00 73.77 ? 220 ARG B NH2 1 ATOM 1432 N N . LEU A 1 190 ? 66.786 -9.961 43.160 1.00 60.22 ? 221 LEU B N 1 ATOM 1433 C CA . LEU A 1 190 ? 67.278 -9.882 41.796 1.00 59.79 ? 221 LEU B CA 1 ATOM 1434 C C . LEU A 1 190 ? 67.106 -8.521 41.123 1.00 60.94 ? 221 LEU B C 1 ATOM 1435 O O . LEU A 1 190 ? 67.933 -8.118 40.309 1.00 60.72 ? 221 LEU B O 1 ATOM 1436 C CB . LEU A 1 190 ? 66.656 -10.988 40.952 1.00 59.21 ? 221 LEU B CB 1 ATOM 1437 C CG . LEU A 1 190 ? 67.287 -12.351 41.233 1.00 57.86 ? 221 LEU B CG 1 ATOM 1438 C CD1 . LEU A 1 190 ? 66.580 -13.479 40.498 1.00 57.38 ? 221 LEU B CD1 1 ATOM 1439 C CD2 . LEU A 1 190 ? 68.751 -12.279 40.859 1.00 57.08 ? 221 LEU B CD2 1 ATOM 1440 N N . GLY A 1 191 ? 66.074 -7.780 41.487 1.00 62.27 ? 222 GLY B N 1 ATOM 1441 C CA . GLY A 1 191 ? 65.895 -6.470 40.876 1.00 63.53 ? 222 GLY B CA 1 ATOM 1442 C C . GLY A 1 191 ? 66.999 -5.472 41.236 1.00 63.72 ? 222 GLY B C 1 ATOM 1443 O O . GLY A 1 191 ? 66.977 -4.292 40.830 1.00 64.84 ? 222 GLY B O 1 ATOM 1444 N N . LEU A 1 192 ? 67.973 -5.941 42.010 1.00 67.84 ? 223 LEU B N 1 ATOM 1445 C CA . LEU A 1 192 ? 69.045 -5.070 42.444 1.00 67.58 ? 223 LEU B CA 1 ATOM 1446 C C . LEU A 1 192 ? 70.317 -5.138 41.586 1.00 66.92 ? 223 LEU B C 1 ATOM 1447 O O . LEU A 1 192 ? 71.298 -4.465 41.900 1.00 66.66 ? 223 LEU B O 1 ATOM 1448 C CB . LEU A 1 192 ? 69.331 -5.285 43.930 1.00 67.34 ? 223 LEU B CB 1 ATOM 1449 C CG . LEU A 1 192 ? 68.074 -5.212 44.809 1.00 68.06 ? 223 LEU B CG 1 ATOM 1450 C CD1 . LEU A 1 192 ? 68.443 -5.212 46.266 1.00 67.96 ? 223 LEU B CD1 1 ATOM 1451 C CD2 . LEU A 1 192 ? 67.245 -4.010 44.503 1.00 69.33 ? 223 LEU B CD2 1 ATOM 1452 N N . LEU A 1 193 ? 70.308 -5.908 40.494 1.00 61.26 ? 224 LEU B N 1 ATOM 1453 C CA . LEU A 1 193 ? 71.456 -5.856 39.590 1.00 60.72 ? 224 LEU B CA 1 ATOM 1454 C C . LEU A 1 193 ? 71.094 -4.776 38.639 1.00 61.95 ? 224 LEU B C 1 ATOM 1455 O O . LEU A 1 193 ? 70.313 -4.978 37.721 1.00 62.28 ? 224 LEU B O 1 ATOM 1456 C CB . LEU A 1 193 ? 71.581 -7.127 38.793 1.00 59.62 ? 224 LEU B CB 1 ATOM 1457 C CG . LEU A 1 193 ? 71.654 -8.335 39.697 1.00 58.55 ? 224 LEU B CG 1 ATOM 1458 C CD1 . LEU A 1 193 ? 70.755 -9.412 39.165 1.00 58.15 ? 224 LEU B CD1 1 ATOM 1459 C CD2 . LEU A 1 193 ? 73.091 -8.805 39.797 1.00 57.54 ? 224 LEU B CD2 1 ATOM 1460 N N . THR A 1 194 ? 71.721 -3.632 38.830 1.00 80.98 ? 225 THR B N 1 ATOM 1461 C CA . THR A 1 194 ? 71.284 -2.437 38.162 1.00 82.07 ? 225 THR B CA 1 ATOM 1462 C C . THR A 1 194 ? 71.823 -2.470 36.754 1.00 82.08 ? 225 THR B C 1 ATOM 1463 O O . THR A 1 194 ? 71.116 -2.157 35.798 1.00 82.92 ? 225 THR B O 1 ATOM 1464 C CB . THR A 1 194 ? 71.763 -1.221 38.929 1.00 82.68 ? 225 THR B CB 1 ATOM 1465 O OG1 . THR A 1 194 ? 73.060 -1.496 39.472 1.00 81.63 ? 225 THR B OG1 1 ATOM 1466 C CG2 . THR A 1 194 ? 70.819 -0.961 40.075 1.00 83.20 ? 225 THR B CG2 1 ATOM 1467 N N . GLU A 1 195 ? 73.070 -2.914 36.642 1.00 77.21 ? 226 GLU B N 1 ATOM 1468 C CA . GLU A 1 195 ? 73.781 -2.973 35.372 1.00 77.35 ? 226 GLU B CA 1 ATOM 1469 C C . GLU A 1 195 ? 73.277 -4.072 34.453 1.00 77.20 ? 226 GLU B C 1 ATOM 1470 O O . GLU A 1 195 ? 73.702 -4.162 33.299 1.00 77.44 ? 226 GLU B O 1 ATOM 1471 C CB . GLU A 1 195 ? 75.271 -3.173 35.637 1.00 76.80 ? 226 GLU B CB 1 ATOM 1472 C CG . GLU A 1 195 ? 75.946 -1.933 36.161 1.00 77.18 ? 226 GLU B CG 1 ATOM 1473 C CD . GLU A 1 195 ? 75.995 -0.860 35.108 1.00 78.06 ? 226 GLU B CD 1 ATOM 1474 O OE1 . GLU A 1 195 ? 76.203 -1.214 33.922 1.00 78.08 ? 226 GLU B OE1 1 ATOM 1475 O OE2 . GLU A 1 195 ? 75.804 0.325 35.456 1.00 78.98 ? 226 GLU B OE2 1 ATOM 1476 N N . LEU A 1 196 ? 72.372 -4.896 34.979 1.00 61.85 ? 227 LEU B N 1 ATOM 1477 C CA . LEU A 1 196 ? 71.904 -6.098 34.293 1.00 61.10 ? 227 LEU B CA 1 ATOM 1478 C C . LEU A 1 196 ? 71.135 -5.819 33.013 1.00 62.04 ? 227 LEU B C 1 ATOM 1479 O O . LEU A 1 196 ? 70.152 -5.074 33.019 1.00 63.21 ? 227 LEU B O 1 ATOM 1480 C CB . LEU A 1 196 ? 71.031 -6.952 35.203 1.00 60.52 ? 227 LEU B CB 1 ATOM 1481 C CG . LEU A 1 196 ? 70.713 -8.296 34.557 1.00 59.61 ? 227 LEU B CG 1 ATOM 1482 C CD1 . LEU A 1 196 ? 71.940 -9.168 34.626 1.00 58.36 ? 227 LEU B CD1 1 ATOM 1483 C CD2 . LEU A 1 196 ? 69.525 -8.981 35.188 1.00 59.45 ? 227 LEU B CD2 1 ATOM 1484 N N . GLN A 1 197 ? 71.588 -6.464 31.936 1.00 61.57 ? 228 GLN B N 1 ATOM 1485 C CA . GLN A 1 197 ? 71.069 -6.302 30.584 1.00 62.39 ? 228 GLN B CA 1 ATOM 1486 C C . GLN A 1 197 ? 70.303 -7.549 30.184 1.00 61.66 ? 228 GLN B C 1 ATOM 1487 O O . GLN A 1 197 ? 69.143 -7.477 29.803 1.00 62.35 ? 228 GLN B O 1 ATOM 1488 C CB . GLN A 1 197 ? 72.204 -6.017 29.595 1.00 62.61 ? 228 GLN B CB 1 ATOM 1489 C CG . GLN A 1 197 ? 73.141 -4.882 30.036 1.00 63.20 ? 228 GLN B CG 1 ATOM 1490 C CD . GLN A 1 197 ? 73.775 -4.101 28.875 1.00 64.28 ? 228 GLN B CD 1 ATOM 1491 O OE1 . GLN A 1 197 ? 73.558 -4.412 27.703 1.00 64.61 ? 228 GLN B OE1 1 ATOM 1492 N NE2 . GLN A 1 197 ? 74.563 -3.080 29.208 1.00 64.89 ? 228 GLN B NE2 1 ATOM 1493 N N . HIS A 1 198 ? 70.990 -8.688 30.222 1.00 65.35 ? 229 HIS B N 1 ATOM 1494 C CA . HIS A 1 198 ? 70.448 -9.963 29.744 1.00 65.45 ? 229 HIS B CA 1 ATOM 1495 C C . HIS A 1 198 ? 70.152 -10.952 30.858 1.00 65.07 ? 229 HIS B C 1 ATOM 1496 O O . HIS A 1 198 ? 71.039 -11.320 31.624 1.00 64.50 ? 229 HIS B O 1 ATOM 1497 C CB . HIS A 1 198 ? 71.444 -10.606 28.772 1.00 65.38 ? 229 HIS B CB 1 ATOM 1498 C CG . HIS A 1 198 ? 70.973 -11.892 28.166 1.00 65.48 ? 229 HIS B CG 1 ATOM 1499 N ND1 . HIS A 1 198 ? 70.615 -11.997 26.842 1.00 65.96 ? 229 HIS B ND1 1 ATOM 1500 C CD2 . HIS A 1 198 ? 70.817 -13.127 28.699 1.00 65.16 ? 229 HIS B CD2 1 ATOM 1501 C CE1 . HIS A 1 198 ? 70.256 -13.243 26.586 1.00 65.94 ? 229 HIS B CE1 1 ATOM 1502 N NE2 . HIS A 1 198 ? 70.368 -13.949 27.696 1.00 65.46 ? 229 HIS B NE2 1 ATOM 1503 N N . MET A 1 199 ? 68.906 -11.402 30.924 1.00 65.62 ? 230 MET B N 1 ATOM 1504 C CA . MET A 1 199 ? 68.531 -12.420 31.885 1.00 65.39 ? 230 MET B CA 1 ATOM 1505 C C . MET A 1 199 ? 67.780 -13.584 31.245 1.00 65.70 ? 230 MET B C 1 ATOM 1506 O O . MET A 1 199 ? 66.623 -13.439 30.862 1.00 66.32 ? 230 MET B O 1 ATOM 1507 C CB . MET A 1 199 ? 67.664 -11.765 32.952 1.00 65.58 ? 230 MET B CB 1 ATOM 1508 C CG . MET A 1 199 ? 66.927 -12.706 33.894 1.00 65.65 ? 230 MET B CG 1 ATOM 1509 S SD . MET A 1 199 ? 66.127 -11.799 35.255 1.00 65.84 ? 230 MET B SD 1 ATOM 1510 C CE . MET A 1 199 ? 65.098 -13.091 35.913 1.00 66.20 ? 230 MET B CE 1 ATOM 1511 N N . GLU A 1 200 ? 68.429 -14.745 31.158 1.00 70.03 ? 231 GLU B N 1 ATOM 1512 C CA . GLU A 1 200 ? 67.762 -15.954 30.701 1.00 70.25 ? 231 GLU B CA 1 ATOM 1513 C C . GLU A 1 200 ? 67.875 -17.014 31.800 1.00 69.88 ? 231 GLU B C 1 ATOM 1514 O O . GLU A 1 200 ? 68.945 -17.576 32.028 1.00 69.29 ? 231 GLU B O 1 ATOM 1515 C CB . GLU A 1 200 ? 68.410 -16.428 29.397 1.00 70.16 ? 231 GLU B CB 1 ATOM 1516 C CG . GLU A 1 200 ? 67.664 -17.549 28.688 1.00 70.36 ? 231 GLU B CG 1 ATOM 1517 C CD . GLU A 1 200 ? 68.290 -17.921 27.350 1.00 70.27 ? 231 GLU B CD 1 ATOM 1518 O OE1 . GLU A 1 200 ? 67.778 -18.866 26.699 1.00 70.44 ? 231 GLU B OE1 1 ATOM 1519 O OE2 . GLU A 1 200 ? 69.287 -17.262 26.963 1.00 70.06 ? 231 GLU B OE2 1 ATOM 1520 N N . ILE A 1 201 ? 66.767 -17.200 32.521 1.00 55.91 ? 232 ILE B N 1 ATOM 1521 C CA . ILE A 1 201 ? 66.540 -18.243 33.544 1.00 55.50 ? 232 ILE B CA 1 ATOM 1522 C C . ILE A 1 201 ? 65.544 -19.387 33.266 1.00 55.59 ? 232 ILE B C 1 ATOM 1523 O O . ILE A 1 201 ? 65.109 -20.050 34.199 1.00 55.57 ? 232 ILE B O 1 ATOM 1524 C CB . ILE A 1 201 ? 66.343 -17.665 34.972 1.00 55.75 ? 232 ILE B CB 1 ATOM 1525 C CG1 . ILE A 1 201 ? 65.042 -16.885 35.090 1.00 56.68 ? 232 ILE B CG1 1 ATOM 1526 C CG2 . ILE A 1 201 ? 67.511 -16.772 35.355 1.00 55.52 ? 232 ILE B CG2 1 ATOM 1527 C CD1 . ILE A 1 201 ? 64.706 -16.537 36.517 1.00 56.95 ? 232 ILE B CD1 1 ATOM 1528 N N . GLY A 1 202 ? 65.071 -19.530 32.035 1.00 66.70 ? 233 GLY B N 1 ATOM 1529 C CA . GLY A 1 202 ? 64.020 -20.503 31.747 1.00 67.33 ? 233 GLY B CA 1 ATOM 1530 C C . GLY A 1 202 ? 64.309 -22.012 31.783 1.00 67.08 ? 233 GLY B C 1 ATOM 1531 O O . GLY A 1 202 ? 65.451 -22.455 31.954 1.00 66.30 ? 233 GLY B O 1 ATOM 1532 N N . TYR A 1 203 ? 63.252 -22.806 31.621 1.00 64.27 ? 234 TYR B N 1 ATOM 1533 C CA . TYR A 1 203 ? 63.379 -24.254 31.445 1.00 64.14 ? 234 TYR B CA 1 ATOM 1534 C C . TYR A 1 203 ? 63.666 -25.014 32.750 1.00 64.07 ? 234 TYR B C 1 ATOM 1535 O O . TYR A 1 203 ? 63.783 -26.252 32.743 1.00 64.01 ? 234 TYR B O 1 ATOM 1536 C CB . TYR A 1 203 ? 64.296 -24.623 30.244 1.00 63.38 ? 234 TYR B CB 1 ATOM 1537 C CG . TYR A 1 203 ? 63.849 -23.904 28.962 1.00 63.75 ? 234 TYR B CG 1 ATOM 1538 C CD1 . TYR A 1 203 ? 62.727 -24.329 28.251 1.00 64.53 ? 234 TYR B CD1 1 ATOM 1539 C CD2 . TYR A 1 203 ? 64.512 -22.770 28.495 1.00 63.43 ? 234 TYR B CD2 1 ATOM 1540 C CE1 . TYR A 1 203 ? 62.281 -23.652 27.110 1.00 64.96 ? 234 TYR B CE1 1 ATOM 1541 C CE2 . TYR A 1 203 ? 64.067 -22.088 27.351 1.00 63.90 ? 234 TYR B CE2 1 ATOM 1542 C CZ . TYR A 1 203 ? 62.953 -22.539 26.669 1.00 64.65 ? 234 TYR B CZ 1 ATOM 1543 O OH . TYR A 1 203 ? 62.516 -21.871 25.549 1.00 65.14 ? 234 TYR B OH 1 ATOM 1544 N N . ASN A 1 204 ? 63.772 -24.256 33.854 1.00 59.44 ? 235 ASN B N 1 ATOM 1545 C CA . ASN A 1 204 ? 63.754 -24.798 35.232 1.00 59.64 ? 235 ASN B CA 1 ATOM 1546 C C . ASN A 1 204 ? 62.325 -24.812 35.790 1.00 60.77 ? 235 ASN B C 1 ATOM 1547 O O . ASN A 1 204 ? 61.397 -24.488 35.057 1.00 61.37 ? 235 ASN B O 1 ATOM 1548 C CB . ASN A 1 204 ? 64.678 -23.997 36.144 1.00 59.18 ? 235 ASN B CB 1 ATOM 1549 C CG . ASN A 1 204 ? 66.030 -23.762 35.521 1.00 58.23 ? 235 ASN B CG 1 ATOM 1550 O OD1 . ASN A 1 204 ? 66.166 -23.833 34.302 1.00 58.00 ? 235 ASN B OD1 1 ATOM 1551 N ND2 . ASN A 1 204 ? 67.038 -23.485 36.339 1.00 57.77 ? 235 ASN B ND2 1 ATOM 1552 N N . HIS A 1 205 ? 62.120 -25.203 37.052 1.00 86.14 ? 236 HIS B N 1 ATOM 1553 C CA . HIS A 1 205 ? 60.758 -25.189 37.614 1.00 87.38 ? 236 HIS B CA 1 ATOM 1554 C C . HIS A 1 205 ? 60.580 -24.171 38.735 1.00 87.59 ? 236 HIS B C 1 ATOM 1555 O O . HIS A 1 205 ? 60.944 -24.438 39.863 1.00 87.65 ? 236 HIS B O 1 ATOM 1556 C CB . HIS A 1 205 ? 60.379 -26.566 38.173 1.00 88.17 ? 236 HIS B CB 1 ATOM 1557 C CG . HIS A 1 205 ? 61.064 -27.707 37.494 1.00 87.72 ? 236 HIS B CG 1 ATOM 1558 N ND1 . HIS A 1 205 ? 60.870 -28.006 36.162 1.00 87.44 ? 236 HIS B ND1 1 ATOM 1559 C CD2 . HIS A 1 205 ? 61.939 -28.630 37.962 1.00 87.54 ? 236 HIS B CD2 1 ATOM 1560 C CE1 . HIS A 1 205 ? 61.599 -29.059 35.836 1.00 87.01 ? 236 HIS B CE1 1 ATOM 1561 N NE2 . HIS A 1 205 ? 62.257 -29.457 36.911 1.00 87.10 ? 236 HIS B NE2 1 ATOM 1562 N N . PHE A 1 206 ? 59.923 -23.054 38.451 1.00 62.88 ? 237 PHE B N 1 ATOM 1563 C CA . PHE A 1 206 ? 59.697 -22.021 39.459 1.00 62.99 ? 237 PHE B CA 1 ATOM 1564 C C . PHE A 1 206 ? 58.189 -21.869 39.651 1.00 64.17 ? 237 PHE B C 1 ATOM 1565 O O . PHE A 1 206 ? 57.408 -22.272 38.775 1.00 64.78 ? 237 PHE B O 1 ATOM 1566 C CB . PHE A 1 206 ? 60.289 -20.666 39.041 1.00 62.29 ? 237 PHE B CB 1 ATOM 1567 C CG . PHE A 1 206 ? 61.779 -20.675 38.794 1.00 61.16 ? 237 PHE B CG 1 ATOM 1568 C CD1 . PHE A 1 206 ? 62.675 -20.736 39.836 1.00 60.66 ? 237 PHE B CD1 1 ATOM 1569 C CD2 . PHE A 1 206 ? 62.280 -20.572 37.518 1.00 60.68 ? 237 PHE B CD2 1 ATOM 1570 C CE1 . PHE A 1 206 ? 64.044 -20.722 39.607 1.00 59.71 ? 237 PHE B CE1 1 ATOM 1571 C CE2 . PHE A 1 206 ? 63.638 -20.562 37.287 1.00 59.72 ? 237 PHE B CE2 1 ATOM 1572 C CZ . PHE A 1 206 ? 64.518 -20.632 38.339 1.00 59.23 ? 237 PHE B CZ 1 ATOM 1573 N N . ASN A 1 207 ? 57.779 -21.313 40.793 1.00 77.34 ? 238 ASN B N 1 ATOM 1574 C CA . ASN A 1 207 ? 56.372 -20.973 41.011 1.00 78.66 ? 238 ASN B CA 1 ATOM 1575 C C . ASN A 1 207 ? 56.196 -19.593 41.623 1.00 78.64 ? 238 ASN B C 1 ATOM 1576 O O . ASN A 1 207 ? 57.169 -18.914 41.946 1.00 77.50 ? 238 ASN B O 1 ATOM 1577 C CB . ASN A 1 207 ? 55.651 -22.033 41.856 1.00 79.22 ? 238 ASN B CB 1 ATOM 1578 C CG . ASN A 1 207 ? 56.605 -22.864 42.722 1.00 79.65 ? 238 ASN B CG 1 ATOM 1579 O OD1 . ASN A 1 207 ? 57.068 -22.417 43.774 1.00 80.39 ? 238 ASN B OD1 1 ATOM 1580 N ND2 . ASN A 1 207 ? 56.878 -24.092 42.288 1.00 79.30 ? 238 ASN B ND2 1 ATOM 1581 N N . GLY A 1 208 ? 54.947 -19.183 41.789 1.00 89.37 ? 239 GLY B N 1 ATOM 1582 C CA . GLY A 1 208 ? 54.668 -17.862 42.313 1.00 89.46 ? 239 GLY B CA 1 ATOM 1583 C C . GLY A 1 208 ? 54.526 -16.860 41.192 1.00 89.15 ? 239 GLY B C 1 ATOM 1584 O O . GLY A 1 208 ? 54.192 -17.225 40.074 1.00 89.30 ? 239 GLY B O 1 ATOM 1585 N N . ASN A 1 209 ? 54.776 -15.594 41.488 1.00 85.95 ? 240 ASN B N 1 ATOM 1586 C CA . ASN A 1 209 ? 54.645 -14.550 40.488 1.00 85.62 ? 240 ASN B CA 1 ATOM 1587 C C . ASN A 1 209 ? 56.006 -14.173 39.948 1.00 84.13 ? 240 ASN B C 1 ATOM 1588 O O . ASN A 1 209 ? 57.021 -14.736 40.358 1.00 83.31 ? 240 ASN B O 1 ATOM 1589 C CB . ASN A 1 209 ? 54.008 -13.301 41.104 1.00 86.13 ? 240 ASN B CB 1 ATOM 1590 C CG . ASN A 1 209 ? 52.591 -13.539 41.602 1.00 86.88 ? 240 ASN B CG 1 ATOM 1591 O OD1 . ASN A 1 209 ? 51.720 -13.986 40.852 1.00 87.73 ? 240 ASN B OD1 1 ATOM 1592 N ND2 . ASN A 1 209 ? 52.354 -13.230 42.876 1.00 86.58 ? 240 ASN B ND2 1 ATOM 1593 N N . ILE A 1 210 ? 56.021 -13.222 39.020 1.00 64.93 ? 241 ILE B N 1 ATOM 1594 C CA . ILE A 1 210 ? 57.240 -12.498 38.696 1.00 64.46 ? 241 ILE B CA 1 ATOM 1595 C C . ILE A 1 210 ? 57.341 -11.352 39.682 1.00 65.57 ? 241 ILE B C 1 ATOM 1596 O O . ILE A 1 210 ? 56.450 -10.507 39.732 1.00 67.16 ? 241 ILE B O 1 ATOM 1597 C CB . ILE A 1 210 ? 57.203 -11.891 37.299 1.00 64.86 ? 241 ILE B CB 1 ATOM 1598 C CG1 . ILE A 1 210 ? 57.163 -12.987 36.238 1.00 63.80 ? 241 ILE B CG1 1 ATOM 1599 C CG2 . ILE A 1 210 ? 58.412 -11.008 37.097 1.00 64.67 ? 241 ILE B CG2 1 ATOM 1600 C CD1 . ILE A 1 210 ? 57.732 -12.575 34.902 1.00 63.65 ? 241 ILE B CD1 1 ATOM 1601 N N . PRO A 1 211 ? 58.421 -11.324 40.479 1.00 64.83 ? 242 PRO B N 1 ATOM 1602 C CA . PRO A 1 211 ? 58.580 -10.331 41.543 1.00 65.80 ? 242 PRO B CA 1 ATOM 1603 C C . PRO A 1 211 ? 58.425 -8.917 41.023 1.00 67.14 ? 242 PRO B C 1 ATOM 1604 O O . PRO A 1 211 ? 59.142 -8.567 40.099 1.00 66.70 ? 242 PRO B O 1 ATOM 1605 C CB . PRO A 1 211 ? 60.030 -10.548 41.976 1.00 64.47 ? 242 PRO B CB 1 ATOM 1606 C CG . PRO A 1 211 ? 60.265 -11.987 41.753 1.00 63.01 ? 242 PRO B CG 1 ATOM 1607 C CD . PRO A 1 211 ? 59.492 -12.336 40.511 1.00 63.08 ? 242 PRO B CD 1 ATOM 1608 N N . SER A 1 212 ? 57.544 -8.118 41.625 1.00 76.25 ? 243 SER B N 1 ATOM 1609 C CA . SER A 1 212 ? 57.319 -6.743 41.171 1.00 77.34 ? 243 SER B CA 1 ATOM 1610 C C . SER A 1 212 ? 58.639 -5.977 41.131 1.00 76.72 ? 243 SER B C 1 ATOM 1611 O O . SER A 1 212 ? 58.893 -5.166 40.239 1.00 77.04 ? 243 SER B O 1 ATOM 1612 C CB . SER A 1 212 ? 56.306 -6.037 42.079 1.00 78.92 ? 243 SER B CB 1 ATOM 1613 O OG . SER A 1 212 ? 56.531 -6.326 43.449 1.00 78.68 ? 243 SER B OG 1 ATOM 1614 N N . GLU A 1 213 ? 59.497 -6.303 42.090 1.00 70.93 ? 244 GLU B N 1 ATOM 1615 C CA . GLU A 1 213 ? 60.807 -5.684 42.256 1.00 70.27 ? 244 GLU B CA 1 ATOM 1616 C C . GLU A 1 213 ? 61.679 -5.790 40.988 1.00 69.38 ? 244 GLU B C 1 ATOM 1617 O O . GLU A 1 213 ? 62.621 -5.012 40.798 1.00 69.22 ? 244 GLU B O 1 ATOM 1618 C CB . GLU A 1 213 ? 61.503 -6.279 43.499 1.00 69.39 ? 244 GLU B CB 1 ATOM 1619 C CG . GLU A 1 213 ? 60.755 -7.478 44.143 1.00 69.37 ? 244 GLU B CG 1 ATOM 1620 C CD . GLU A 1 213 ? 59.789 -7.127 45.309 1.00 70.73 ? 244 GLU B CD 1 ATOM 1621 O OE1 . GLU A 1 213 ? 58.637 -7.626 45.308 1.00 71.48 ? 244 GLU B OE1 1 ATOM 1622 O OE2 . GLU A 1 213 ? 60.180 -6.395 46.250 1.00 71.08 ? 244 GLU B OE2 1 ATOM 1623 N N . PHE A 1 214 ? 61.336 -6.724 40.104 1.00 67.95 ? 245 PHE B N 1 ATOM 1624 C CA . PHE A 1 214 ? 62.067 -6.906 38.852 1.00 67.34 ? 245 PHE B CA 1 ATOM 1625 C C . PHE A 1 214 ? 61.953 -5.693 37.937 1.00 68.24 ? 245 PHE B C 1 ATOM 1626 O O . PHE A 1 214 ? 62.688 -5.583 36.953 1.00 67.81 ? 245 PHE B O 1 ATOM 1627 C CB . PHE A 1 214 ? 61.576 -8.139 38.090 1.00 67.42 ? 245 PHE B CB 1 ATOM 1628 C CG . PHE A 1 214 ? 62.226 -9.417 38.515 1.00 67.03 ? 245 PHE B CG 1 ATOM 1629 C CD1 . PHE A 1 214 ? 62.717 -9.575 39.795 1.00 66.61 ? 245 PHE B CD1 1 ATOM 1630 C CD2 . PHE A 1 214 ? 62.359 -10.466 37.628 1.00 67.11 ? 245 PHE B CD2 1 ATOM 1631 C CE1 . PHE A 1 214 ? 63.317 -10.764 40.183 1.00 66.29 ? 245 PHE B CE1 1 ATOM 1632 C CE2 . PHE A 1 214 ? 62.965 -11.652 38.015 1.00 66.75 ? 245 PHE B CE2 1 ATOM 1633 C CZ . PHE A 1 214 ? 63.445 -11.796 39.286 1.00 66.34 ? 245 PHE B CZ 1 ATOM 1634 N N . ALA A 1 215 ? 61.035 -4.784 38.241 1.00 68.82 ? 246 ALA B N 1 ATOM 1635 C CA . ALA A 1 215 ? 60.914 -3.601 37.410 1.00 70.22 ? 246 ALA B CA 1 ATOM 1636 C C . ALA A 1 215 ? 62.085 -2.665 37.649 1.00 70.29 ? 246 ALA B C 1 ATOM 1637 O O . ALA A 1 215 ? 62.229 -1.669 36.951 1.00 71.36 ? 246 ALA B O 1 ATOM 1638 C CB . ALA A 1 215 ? 59.611 -2.893 37.665 1.00 72.16 ? 246 ALA B CB 1 ATOM 1639 N N . LEU A 1 216 ? 62.921 -2.985 38.637 1.00 69.23 ? 247 LEU B N 1 ATOM 1640 C CA . LEU A 1 216 ? 64.055 -2.123 38.984 1.00 69.27 ? 247 LEU B CA 1 ATOM 1641 C C . LEU A 1 216 ? 65.286 -2.237 38.083 1.00 68.25 ? 247 LEU B C 1 ATOM 1642 O O . LEU A 1 216 ? 66.207 -1.429 38.219 1.00 68.45 ? 247 LEU B O 1 ATOM 1643 C CB . LEU A 1 216 ? 64.464 -2.299 40.448 1.00 68.75 ? 247 LEU B CB 1 ATOM 1644 C CG . LEU A 1 216 ? 63.765 -1.307 41.383 1.00 70.44 ? 247 LEU B CG 1 ATOM 1645 C CD1 . LEU A 1 216 ? 62.566 -1.948 42.058 1.00 70.81 ? 247 LEU B CD1 1 ATOM 1646 C CD2 . LEU A 1 216 ? 64.724 -0.668 42.417 1.00 70.40 ? 247 LEU B CD2 1 ATOM 1647 N N . LEU A 1 217 ? 65.295 -3.199 37.153 1.00 67.27 ? 248 LEU B N 1 ATOM 1648 C CA . LEU A 1 217 ? 66.444 -3.384 36.266 1.00 66.39 ? 248 LEU B CA 1 ATOM 1649 C C . LEU A 1 217 ? 66.189 -2.545 35.036 1.00 67.67 ? 248 LEU B C 1 ATOM 1650 O O . LEU A 1 217 ? 65.415 -2.925 34.166 1.00 67.93 ? 248 LEU B O 1 ATOM 1651 C CB . LEU A 1 217 ? 66.537 -4.840 35.832 1.00 64.88 ? 248 LEU B CB 1 ATOM 1652 C CG . LEU A 1 217 ? 66.194 -5.866 36.901 1.00 63.95 ? 248 LEU B CG 1 ATOM 1653 C CD1 . LEU A 1 217 ? 65.476 -7.040 36.308 1.00 63.32 ? 248 LEU B CD1 1 ATOM 1654 C CD2 . LEU A 1 217 ? 67.454 -6.316 37.572 1.00 62.68 ? 248 LEU B CD2 1 ATOM 1655 N N . SER A 1 218 ? 66.897 -1.428 34.944 1.00 88.77 ? 249 SER B N 1 ATOM 1656 C CA . SER A 1 218 ? 66.611 -0.421 33.941 1.00 90.23 ? 249 SER B CA 1 ATOM 1657 C C . SER A 1 218 ? 67.236 -0.809 32.624 1.00 89.73 ? 249 SER B C 1 ATOM 1658 O O . SER A 1 218 ? 66.626 -0.699 31.561 1.00 90.58 ? 249 SER B O 1 ATOM 1659 C CB . SER A 1 218 ? 67.215 0.892 34.385 1.00 91.28 ? 249 SER B CB 1 ATOM 1660 O OG . SER A 1 218 ? 68.600 0.708 34.612 1.00 90.10 ? 249 SER B OG 1 ATOM 1661 N N . ASN A 1 219 ? 68.466 -1.291 32.706 1.00 73.07 ? 250 ASN B N 1 ATOM 1662 C CA . ASN A 1 219 ? 69.243 -1.529 31.516 1.00 72.79 ? 250 ASN B CA 1 ATOM 1663 C C . ASN A 1 219 ? 68.827 -2.837 30.885 1.00 72.03 ? 250 ASN B C 1 ATOM 1664 O O . ASN A 1 219 ? 69.364 -3.210 29.852 1.00 71.80 ? 250 ASN B O 1 ATOM 1665 C CB . ASN A 1 219 ? 70.738 -1.542 31.847 1.00 71.91 ? 250 ASN B CB 1 ATOM 1666 C CG . ASN A 1 219 ? 71.204 -0.255 32.526 1.00 72.70 ? 250 ASN B CG 1 ATOM 1667 O OD1 . ASN A 1 219 ? 70.391 0.548 32.980 1.00 73.88 ? 250 ASN B OD1 1 ATOM 1668 N ND2 . ASN A 1 219 ? 72.521 -0.062 32.599 1.00 72.20 ? 250 ASN B ND2 1 ATOM 1669 N N . LEU A 1 220 ? 67.870 -3.526 31.510 1.00 66.45 ? 251 LEU B N 1 ATOM 1670 C CA . LEU A 1 220 ? 67.446 -4.852 31.052 1.00 65.41 ? 251 LEU B CA 1 ATOM 1671 C C . LEU A 1 220 ? 66.944 -4.828 29.623 1.00 66.19 ? 251 LEU B C 1 ATOM 1672 O O . LEU A 1 220 ? 66.163 -3.945 29.258 1.00 67.73 ? 251 LEU B O 1 ATOM 1673 C CB . LEU A 1 220 ? 66.352 -5.457 31.944 1.00 65.14 ? 251 LEU B CB 1 ATOM 1674 C CG . LEU A 1 220 ? 65.911 -6.897 31.584 1.00 64.01 ? 251 LEU B CG 1 ATOM 1675 C CD1 . LEU A 1 220 ? 66.945 -7.910 32.008 1.00 62.34 ? 251 LEU B CD1 1 ATOM 1676 C CD2 . LEU A 1 220 ? 64.552 -7.304 32.143 1.00 64.26 ? 251 LEU B CD2 1 ATOM 1677 N N . LYS A 1 221 ? 67.393 -5.816 28.842 1.00 73.82 ? 252 LYS B N 1 ATOM 1678 C CA . LYS A 1 221 ? 66.992 -6.004 27.454 1.00 74.33 ? 252 LYS B CA 1 ATOM 1679 C C . LYS A 1 221 ? 66.283 -7.342 27.239 1.00 73.99 ? 252 LYS B C 1 ATOM 1680 O O . LYS A 1 221 ? 65.117 -7.370 26.862 1.00 74.40 ? 252 LYS B O 1 ATOM 1681 C CB . LYS A 1 221 ? 68.210 -5.925 26.538 1.00 74.27 ? 252 LYS B CB 1 ATOM 1682 C CG . LYS A 1 221 ? 68.895 -4.572 26.502 1.00 74.99 ? 252 LYS B CG 1 ATOM 1683 C CD . LYS A 1 221 ? 69.105 -4.065 25.069 1.00 75.96 ? 252 LYS B CD 1 ATOM 1684 C CE . LYS A 1 221 ? 70.161 -4.876 24.321 1.00 75.20 ? 252 LYS B CE 1 ATOM 1685 N NZ . LYS A 1 221 ? 69.923 -4.951 22.832 1.00 75.84 ? 252 LYS B NZ 1 ATOM 1686 N N . TYR A 1 222 ? 67.003 -8.444 27.467 1.00 63.24 ? 253 TYR B N 1 ATOM 1687 C CA . TYR A 1 222 ? 66.510 -9.805 27.189 1.00 62.26 ? 253 TYR B CA 1 ATOM 1688 C C . TYR A 1 222 ? 66.000 -10.431 28.468 1.00 61.45 ? 253 TYR B C 1 ATOM 1689 O O . TYR A 1 222 ? 66.739 -10.566 29.432 1.00 60.68 ? 253 TYR B O 1 ATOM 1690 C CB . TYR A 1 222 ? 67.621 -10.683 26.567 1.00 61.21 ? 253 TYR B CB 1 ATOM 1691 C CG . TYR A 1 222 ? 67.189 -12.029 25.968 1.00 60.41 ? 253 TYR B CG 1 ATOM 1692 C CD1 . TYR A 1 222 ? 67.081 -13.171 26.764 1.00 59.50 ? 253 TYR B CD1 1 ATOM 1693 C CD2 . TYR A 1 222 ? 66.941 -12.178 24.602 1.00 60.96 ? 253 TYR B CD2 1 ATOM 1694 C CE1 . TYR A 1 222 ? 66.705 -14.434 26.220 1.00 59.15 ? 253 TYR B CE1 1 ATOM 1695 C CE2 . TYR A 1 222 ? 66.558 -13.446 24.046 1.00 60.51 ? 253 TYR B CE2 1 ATOM 1696 C CZ . TYR A 1 222 ? 66.443 -14.566 24.867 1.00 59.63 ? 253 TYR B CZ 1 ATOM 1697 O OH . TYR A 1 222 ? 66.074 -15.805 24.370 1.00 59.27 ? 253 TYR B OH 1 ATOM 1698 N N . PHE A 1 223 ? 64.724 -10.784 28.476 1.00 61.74 ? 254 PHE B N 1 ATOM 1699 C CA . PHE A 1 223 ? 64.118 -11.442 29.614 1.00 61.13 ? 254 PHE B CA 1 ATOM 1700 C C . PHE A 1 223 ? 63.358 -12.687 29.140 1.00 60.58 ? 254 PHE B C 1 ATOM 1701 O O . PHE A 1 223 ? 62.325 -12.570 28.480 1.00 61.37 ? 254 PHE B O 1 ATOM 1702 C CB . PHE A 1 223 ? 63.177 -10.439 30.280 1.00 62.42 ? 254 PHE B CB 1 ATOM 1703 C CG . PHE A 1 223 ? 62.551 -10.922 31.562 1.00 62.09 ? 254 PHE B CG 1 ATOM 1704 C CD1 . PHE A 1 223 ? 63.331 -11.347 32.625 1.00 61.06 ? 254 PHE B CD1 1 ATOM 1705 C CD2 . PHE A 1 223 ? 61.174 -10.908 31.724 1.00 62.94 ? 254 PHE B CD2 1 ATOM 1706 C CE1 . PHE A 1 223 ? 62.743 -11.783 33.811 1.00 60.90 ? 254 PHE B CE1 1 ATOM 1707 C CE2 . PHE A 1 223 ? 60.583 -11.345 32.913 1.00 62.78 ? 254 PHE B CE2 1 ATOM 1708 C CZ . PHE A 1 223 ? 61.370 -11.778 33.952 1.00 61.77 ? 254 PHE B CZ 1 ATOM 1709 N N . ASP A 1 224 ? 63.861 -13.876 29.473 1.00 61.95 ? 255 ASP B N 1 ATOM 1710 C CA . ASP A 1 224 ? 63.196 -15.129 29.110 1.00 62.27 ? 255 ASP B CA 1 ATOM 1711 C C . ASP A 1 224 ? 63.068 -16.013 30.349 1.00 62.14 ? 255 ASP B C 1 ATOM 1712 O O . ASP A 1 224 ? 64.052 -16.554 30.837 1.00 61.45 ? 255 ASP B O 1 ATOM 1713 C CB . ASP A 1 224 ? 64.015 -15.830 28.010 1.00 61.90 ? 255 ASP B CB 1 ATOM 1714 C CG . ASP A 1 224 ? 63.459 -17.202 27.602 1.00 62.00 ? 255 ASP B CG 1 ATOM 1715 O OD1 . ASP A 1 224 ? 62.382 -17.594 28.096 1.00 62.63 ? 255 ASP B OD1 1 ATOM 1716 O OD2 . ASP A 1 224 ? 64.107 -17.885 26.755 1.00 61.51 ? 255 ASP B OD2 1 ATOM 1717 N N . VAL A 1 225 ? 61.840 -16.141 30.849 1.00 75.78 ? 256 VAL B N 1 ATOM 1718 C CA . VAL A 1 225 ? 61.462 -17.068 31.928 1.00 75.97 ? 256 VAL B CA 1 ATOM 1719 C C . VAL A 1 225 ? 60.741 -18.357 31.499 1.00 76.46 ? 256 VAL B C 1 ATOM 1720 O O . VAL A 1 225 ? 60.167 -19.044 32.337 1.00 76.95 ? 256 VAL B O 1 ATOM 1721 C CB . VAL A 1 225 ? 60.636 -16.395 33.012 1.00 76.56 ? 256 VAL B CB 1 ATOM 1722 C CG1 . VAL A 1 225 ? 61.179 -16.779 34.361 1.00 76.25 ? 256 VAL B CG1 1 ATOM 1723 C CG2 . VAL A 1 225 ? 60.667 -14.903 32.838 1.00 76.56 ? 256 VAL B CG2 1 ATOM 1724 N N . SER A 1 226 ? 60.697 -18.629 30.198 1.00 78.55 ? 257 SER B N 1 ATOM 1725 C CA . SER A 1 226 ? 59.802 -19.630 29.619 1.00 79.19 ? 257 SER B CA 1 ATOM 1726 C C . SER A 1 226 ? 60.004 -21.088 30.069 1.00 79.02 ? 257 SER B C 1 ATOM 1727 O O . SER A 1 226 ? 61.069 -21.461 30.563 1.00 78.22 ? 257 SER B O 1 ATOM 1728 C CB . SER A 1 226 ? 59.886 -19.537 28.101 1.00 79.13 ? 257 SER B CB 1 ATOM 1729 O OG . SER A 1 226 ? 59.869 -18.181 27.693 1.00 79.29 ? 257 SER B OG 1 ATOM 1730 N N . ASN A 1 227 ? 58.951 -21.891 29.886 1.00 81.59 ? 258 ASN B N 1 ATOM 1731 C CA . ASN A 1 227 ? 58.863 -23.288 30.349 1.00 81.71 ? 258 ASN B CA 1 ATOM 1732 C C . ASN A 1 227 ? 59.234 -23.423 31.824 1.00 81.57 ? 258 ASN B C 1 ATOM 1733 O O . ASN A 1 227 ? 60.280 -23.952 32.183 1.00 80.98 ? 258 ASN B O 1 ATOM 1734 C CB . ASN A 1 227 ? 59.646 -24.263 29.449 1.00 80.95 ? 258 ASN B CB 1 ATOM 1735 C CG . ASN A 1 227 ? 59.058 -25.678 29.449 1.00 81.46 ? 258 ASN B CG 1 ATOM 1736 O OD1 . ASN A 1 227 ? 57.956 -25.891 29.941 1.00 82.46 ? 258 ASN B OD1 1 ATOM 1737 N ND2 . ASN A 1 227 ? 59.795 -26.645 28.892 1.00 80.81 ? 258 ASN B ND2 1 ATOM 1738 N N . CYS A 1 228 ? 58.360 -22.882 32.662 1.00 74.34 ? 259 CYS B N 1 ATOM 1739 C CA . CYS A 1 228 ? 58.452 -22.970 34.112 1.00 74.48 ? 259 CYS B CA 1 ATOM 1740 C C . CYS A 1 228 ? 57.032 -23.165 34.605 1.00 75.83 ? 259 CYS B C 1 ATOM 1741 O O . CYS A 1 228 ? 56.123 -23.409 33.807 1.00 76.60 ? 259 CYS B O 1 ATOM 1742 C CB . CYS A 1 228 ? 59.020 -21.688 34.724 1.00 73.99 ? 259 CYS B CB 1 ATOM 1743 S SG . CYS A 1 228 ? 60.814 -21.544 34.690 1.00 72.57 ? 259 CYS B SG 1 ATOM 1744 N N . SER A 1 229 ? 56.849 -23.139 35.919 1.00 78.67 ? 260 SER B N 1 ATOM 1745 C CA . SER A 1 229 ? 55.510 -23.140 36.486 1.00 80.05 ? 260 SER B CA 1 ATOM 1746 C C . SER A 1 229 ? 54.978 -21.816 37.035 1.00 80.43 ? 260 SER B C 1 ATOM 1747 O O . SER A 1 229 ? 53.920 -21.797 37.656 1.00 81.57 ? 260 SER B O 1 ATOM 1748 C CB . SER A 1 229 ? 55.295 -24.321 37.419 1.00 80.60 ? 260 SER B CB 1 ATOM 1749 O OG . SER A 1 229 ? 55.084 -25.488 36.630 1.00 80.91 ? 260 SER B OG 1 ATOM 1750 N N . LEU A 1 230 ? 55.715 -20.726 36.825 1.00 81.86 ? 261 LEU B N 1 ATOM 1751 C CA . LEU A 1 230 ? 55.353 -19.411 37.375 1.00 82.05 ? 261 LEU B CA 1 ATOM 1752 C C . LEU A 1 230 ? 53.912 -19.021 37.103 1.00 83.32 ? 261 LEU B C 1 ATOM 1753 O O . LEU A 1 230 ? 53.358 -19.332 36.058 1.00 83.77 ? 261 LEU B O 1 ATOM 1754 C CB . LEU A 1 230 ? 56.240 -18.324 36.785 1.00 81.02 ? 261 LEU B CB 1 ATOM 1755 C CG . LEU A 1 230 ? 57.686 -18.298 37.246 1.00 79.89 ? 261 LEU B CG 1 ATOM 1756 C CD1 . LEU A 1 230 ? 58.394 -17.193 36.520 1.00 78.96 ? 261 LEU B CD1 1 ATOM 1757 C CD2 . LEU A 1 230 ? 57.746 -18.073 38.739 1.00 80.28 ? 261 LEU B CD2 1 ATOM 1758 N N . SER A 1 231 ? 53.296 -18.345 38.058 1.00 70.13 ? 262 SER B N 1 ATOM 1759 C CA . SER A 1 231 ? 51.875 -18.075 37.950 1.00 71.43 ? 262 SER B CA 1 ATOM 1760 C C . SER A 1 231 ? 51.429 -16.701 38.434 1.00 71.79 ? 262 SER B C 1 ATOM 1761 O O . SER A 1 231 ? 52.228 -15.793 38.694 1.00 71.08 ? 262 SER B O 1 ATOM 1762 C CB . SER A 1 231 ? 51.087 -19.147 38.698 1.00 72.22 ? 262 SER B CB 1 ATOM 1763 O OG . SER A 1 231 ? 51.156 -18.931 40.093 1.00 72.29 ? 262 SER B OG 1 ATOM 1764 N N . GLY A 1 232 ? 50.117 -16.566 38.522 1.00 85.93 ? 263 GLY B N 1 ATOM 1765 C CA . GLY A 1 232 ? 49.517 -15.359 39.028 1.00 86.20 ? 263 GLY B CA 1 ATOM 1766 C C . GLY A 1 232 ? 49.458 -14.301 37.958 1.00 85.86 ? 263 GLY B C 1 ATOM 1767 O O . GLY A 1 232 ? 49.522 -14.599 36.770 1.00 85.75 ? 263 GLY B O 1 ATOM 1768 N N . SER A 1 233 ? 49.330 -13.055 38.392 1.00 79.94 ? 264 SER B N 1 ATOM 1769 C CA . SER A 1 233 ? 49.165 -11.952 37.472 1.00 79.74 ? 264 SER B CA 1 ATOM 1770 C C . SER A 1 233 ? 50.496 -11.501 36.863 1.00 78.36 ? 264 SER B C 1 ATOM 1771 O O . SER A 1 233 ? 51.577 -11.729 37.431 1.00 77.32 ? 264 SER B O 1 ATOM 1772 C CB . SER A 1 233 ? 48.450 -10.793 38.173 1.00 80.18 ? 264 SER B CB 1 ATOM 1773 O OG . SER A 1 233 ? 47.161 -11.187 38.621 1.00 81.50 ? 264 SER B OG 1 ATOM 1774 N N . LEU A 1 234 ? 50.393 -10.894 35.682 1.00 74.18 ? 265 LEU B N 1 ATOM 1775 C CA . LEU A 1 234 ? 51.492 -10.177 35.049 1.00 73.12 ? 265 LEU B CA 1 ATOM 1776 C C . LEU A 1 234 ? 51.589 -8.802 35.701 1.00 73.32 ? 265 LEU B C 1 ATOM 1777 O O . LEU A 1 234 ? 50.609 -8.044 35.673 1.00 75.04 ? 265 LEU B O 1 ATOM 1778 C CB . LEU A 1 234 ? 51.180 -10.004 33.567 1.00 73.52 ? 265 LEU B CB 1 ATOM 1779 C CG . LEU A 1 234 ? 52.025 -10.731 32.536 1.00 72.98 ? 265 LEU B CG 1 ATOM 1780 C CD1 . LEU A 1 234 ? 52.299 -12.116 33.017 1.00 72.71 ? 265 LEU B CD1 1 ATOM 1781 C CD2 . LEU A 1 234 ? 51.259 -10.768 31.248 1.00 74.00 ? 265 LEU B CD2 1 ATOM 1782 N N . PRO A 1 235 ? 52.752 -8.480 36.311 1.00 72.30 ? 266 PRO B N 1 ATOM 1783 C CA . PRO A 1 235 ? 52.917 -7.244 37.108 1.00 73.59 ? 266 PRO B CA 1 ATOM 1784 C C . PRO A 1 235 ? 52.897 -5.955 36.275 1.00 75.03 ? 266 PRO B C 1 ATOM 1785 O O . PRO A 1 235 ? 53.667 -5.859 35.324 1.00 74.32 ? 266 PRO B O 1 ATOM 1786 C CB . PRO A 1 235 ? 54.290 -7.428 37.775 1.00 72.07 ? 266 PRO B CB 1 ATOM 1787 C CG . PRO A 1 235 ? 54.633 -8.890 37.593 1.00 70.15 ? 266 PRO B CG 1 ATOM 1788 C CD . PRO A 1 235 ? 53.963 -9.316 36.329 1.00 70.21 ? 266 PRO B CD 1 ATOM 1789 N N . GLN A 1 236 ? 52.075 -4.978 36.656 1.00 88.38 ? 267 GLN B N 1 ATOM 1790 C CA . GLN A 1 236 ? 51.917 -3.760 35.867 1.00 89.88 ? 267 GLN B CA 1 ATOM 1791 C C . GLN A 1 236 ? 53.261 -3.103 35.692 1.00 89.27 ? 267 GLN B C 1 ATOM 1792 O O . GLN A 1 236 ? 53.626 -2.655 34.607 1.00 89.49 ? 267 GLN B O 1 ATOM 1793 C CB . GLN A 1 236 ? 50.990 -2.773 36.575 1.00 92.24 ? 267 GLN B CB 1 ATOM 1794 C CG . GLN A 1 236 ? 50.927 -1.391 35.898 1.00 94.12 ? 267 GLN B CG 1 ATOM 1795 C CD . GLN A 1 236 ? 51.165 -0.200 36.856 1.00 95.53 ? 267 GLN B CD 1 ATOM 1796 O OE1 . GLN A 1 236 ? 51.711 -0.356 37.958 1.00 94.74 ? 267 GLN B OE1 1 ATOM 1797 N NE2 . GLN A 1 236 ? 50.760 1.000 36.418 1.00 97.70 ? 267 GLN B NE2 1 ATOM 1798 N N . GLU A 1 237 ? 54.001 -3.095 36.791 1.00 88.95 ? 268 GLU B N 1 ATOM 1799 C CA . GLU A 1 237 ? 55.247 -2.357 36.946 1.00 88.59 ? 268 GLU B CA 1 ATOM 1800 C C . GLU A 1 237 ? 56.270 -2.632 35.838 1.00 87.22 ? 268 GLU B C 1 ATOM 1801 O O . GLU A 1 237 ? 57.091 -1.773 35.496 1.00 87.50 ? 268 GLU B O 1 ATOM 1802 C CB . GLU A 1 237 ? 55.824 -2.654 38.335 1.00 87.70 ? 268 GLU B CB 1 ATOM 1803 C CG . GLU A 1 237 ? 55.388 -4.021 38.930 1.00 86.69 ? 268 GLU B CG 1 ATOM 1804 C CD . GLU A 1 237 ? 54.061 -3.982 39.710 1.00 88.12 ? 268 GLU B CD 1 ATOM 1805 O OE1 . GLU A 1 237 ? 53.676 -2.886 40.182 1.00 89.93 ? 268 GLU B OE1 1 ATOM 1806 O OE2 . GLU A 1 237 ? 53.411 -5.052 39.854 1.00 87.77 ? 268 GLU B OE2 1 ATOM 1807 N N . LEU A 1 238 ? 56.185 -3.820 35.251 1.00 74.29 ? 269 LEU B N 1 ATOM 1808 C CA . LEU A 1 238 ? 57.106 -4.243 34.190 1.00 72.98 ? 269 LEU B CA 1 ATOM 1809 C C . LEU A 1 238 ? 57.098 -3.311 32.992 1.00 74.25 ? 269 LEU B C 1 ATOM 1810 O O . LEU A 1 238 ? 58.081 -3.222 32.248 1.00 73.60 ? 269 LEU B O 1 ATOM 1811 C CB . LEU A 1 238 ? 56.780 -5.663 33.744 1.00 71.64 ? 269 LEU B CB 1 ATOM 1812 C CG . LEU A 1 238 ? 57.324 -6.643 34.762 1.00 69.99 ? 269 LEU B CG 1 ATOM 1813 C CD1 . LEU A 1 238 ? 56.715 -7.991 34.540 1.00 69.06 ? 269 LEU B CD1 1 ATOM 1814 C CD2 . LEU A 1 238 ? 58.829 -6.672 34.624 1.00 68.69 ? 269 LEU B CD2 1 ATOM 1815 N N . GLY A 1 239 ? 56.000 -2.581 32.841 1.00 89.94 ? 270 GLY B N 1 ATOM 1816 C CA . GLY A 1 239 ? 55.856 -1.665 31.732 1.00 91.44 ? 270 GLY B CA 1 ATOM 1817 C C . GLY A 1 239 ? 56.902 -0.572 31.785 1.00 91.89 ? 270 GLY B C 1 ATOM 1818 O O . GLY A 1 239 ? 56.969 0.274 30.896 1.00 93.16 ? 270 GLY B O 1 ATOM 1819 N N . ASN A 1 240 ? 57.716 -0.571 32.833 1.00 91.14 ? 271 ASN B N 1 ATOM 1820 C CA . ASN A 1 240 ? 58.725 0.469 32.960 1.00 91.56 ? 271 ASN B CA 1 ATOM 1821 C C . ASN A 1 240 ? 60.147 0.148 32.469 1.00 89.98 ? 271 ASN B C 1 ATOM 1822 O O . ASN A 1 240 ? 61.034 0.999 32.580 1.00 90.32 ? 271 ASN B O 1 ATOM 1823 C CB . ASN A 1 240 ? 58.738 1.034 34.387 1.00 92.05 ? 271 ASN B CB 1 ATOM 1824 C CG . ASN A 1 240 ? 57.665 2.099 34.613 1.00 94.50 ? 271 ASN B CG 1 ATOM 1825 O OD1 . ASN A 1 240 ? 57.977 3.276 34.774 1.00 95.81 ? 271 ASN B OD1 1 ATOM 1826 N ND2 . ASN A 1 240 ? 56.400 1.685 34.624 1.00 95.23 ? 271 ASN B ND2 1 ATOM 1827 N N . LEU A 1 241 ? 60.384 -1.034 31.902 1.00 74.45 ? 272 LEU B N 1 ATOM 1828 C CA . LEU A 1 241 ? 61.747 -1.293 31.439 1.00 73.15 ? 272 LEU B CA 1 ATOM 1829 C C . LEU A 1 241 ? 61.801 -0.804 30.005 1.00 74.15 ? 272 LEU B C 1 ATOM 1830 O O . LEU A 1 241 ? 61.395 -1.491 29.080 1.00 73.89 ? 272 LEU B O 1 ATOM 1831 C CB . LEU A 1 241 ? 62.087 -2.789 31.483 1.00 71.06 ? 272 LEU B CB 1 ATOM 1832 C CG . LEU A 1 241 ? 61.579 -3.615 32.666 1.00 70.20 ? 272 LEU B CG 1 ATOM 1833 C CD1 . LEU A 1 241 ? 60.893 -4.872 32.202 1.00 69.37 ? 272 LEU B CD1 1 ATOM 1834 C CD2 . LEU A 1 241 ? 62.704 -3.972 33.592 1.00 68.78 ? 272 LEU B CD2 1 ATOM 1835 N N . SER A 1 242 ? 62.398 0.361 29.817 1.00 82.98 ? 273 SER B N 1 ATOM 1836 C CA . SER A 1 242 ? 62.275 1.039 28.551 1.00 84.44 ? 273 SER B CA 1 ATOM 1837 C C . SER A 1 242 ? 63.321 0.536 27.599 1.00 83.41 ? 273 SER B C 1 ATOM 1838 O O . SER A 1 242 ? 63.323 0.889 26.431 1.00 84.41 ? 273 SER B O 1 ATOM 1839 C CB . SER A 1 242 ? 62.433 2.536 28.729 1.00 86.29 ? 273 SER B CB 1 ATOM 1840 O OG . SER A 1 242 ? 62.708 3.139 27.481 1.00 87.47 ? 273 SER B OG 1 ATOM 1841 N N . ASN A 1 243 ? 64.236 -0.271 28.098 1.00 86.09 ? 274 ASN B N 1 ATOM 1842 C CA . ASN A 1 243 ? 65.301 -0.732 27.241 1.00 85.20 ? 274 ASN B CA 1 ATOM 1843 C C . ASN A 1 243 ? 65.054 -2.113 26.670 1.00 83.92 ? 274 ASN B C 1 ATOM 1844 O O . ASN A 1 243 ? 65.877 -2.642 25.931 1.00 83.24 ? 274 ASN B O 1 ATOM 1845 C CB . ASN A 1 243 ? 66.641 -0.628 27.956 1.00 84.19 ? 274 ASN B CB 1 ATOM 1846 C CG . ASN A 1 243 ? 67.075 0.815 28.153 1.00 85.66 ? 274 ASN B CG 1 ATOM 1847 O OD1 . ASN A 1 243 ? 66.861 1.672 27.285 1.00 87.32 ? 274 ASN B OD1 1 ATOM 1848 N ND2 . ASN A 1 243 ? 67.676 1.096 29.303 1.00 85.13 ? 274 ASN B ND2 1 ATOM 1849 N N . LEU A 1 244 ? 63.888 -2.670 26.966 1.00 71.52 ? 275 LEU B N 1 ATOM 1850 C CA . LEU A 1 244 ? 63.679 -4.103 26.791 1.00 70.00 ? 275 LEU B CA 1 ATOM 1851 C C . LEU A 1 244 ? 63.307 -4.500 25.371 1.00 70.39 ? 275 LEU B C 1 ATOM 1852 O O . LEU A 1 244 ? 62.224 -4.194 24.892 1.00 71.65 ? 275 LEU B O 1 ATOM 1853 C CB . LEU A 1 244 ? 62.562 -4.542 27.733 1.00 69.82 ? 275 LEU B CB 1 ATOM 1854 C CG . LEU A 1 244 ? 62.221 -6.014 27.884 1.00 68.30 ? 275 LEU B CG 1 ATOM 1855 C CD1 . LEU A 1 244 ? 62.679 -6.480 29.230 1.00 67.05 ? 275 LEU B CD1 1 ATOM 1856 C CD2 . LEU A 1 244 ? 60.737 -6.190 27.744 1.00 69.13 ? 275 LEU B CD2 1 ATOM 1857 N N . GLU A 1 245 ? 64.211 -5.223 24.722 1.00 71.66 ? 276 GLU B N 1 ATOM 1858 C CA . GLU A 1 245 ? 63.997 -5.670 23.358 1.00 71.93 ? 276 GLU B CA 1 ATOM 1859 C C . GLU A 1 245 ? 63.457 -7.092 23.238 1.00 70.97 ? 276 GLU B C 1 ATOM 1860 O O . GLU A 1 245 ? 63.013 -7.502 22.172 1.00 71.28 ? 276 GLU B O 1 ATOM 1861 C CB . GLU A 1 245 ? 65.293 -5.516 22.560 1.00 71.82 ? 276 GLU B CB 1 ATOM 1862 C CG . GLU A 1 245 ? 65.785 -4.069 22.475 1.00 73.03 ? 276 GLU B CG 1 ATOM 1863 C CD . GLU A 1 245 ? 67.091 -3.912 21.704 1.00 73.06 ? 276 GLU B CD 1 ATOM 1864 O OE1 . GLU A 1 245 ? 67.640 -4.929 21.217 1.00 72.16 ? 276 GLU B OE1 1 ATOM 1865 O OE2 . GLU A 1 245 ? 67.571 -2.762 21.590 1.00 74.19 ? 276 GLU B OE2 1 ATOM 1866 N N . THR A 1 246 ? 63.482 -7.847 24.324 1.00 66.96 ? 277 THR B N 1 ATOM 1867 C CA . THR A 1 246 ? 63.005 -9.221 24.266 1.00 65.77 ? 277 THR B CA 1 ATOM 1868 C C . THR A 1 246 ? 62.264 -9.654 25.506 1.00 65.20 ? 277 THR B C 1 ATOM 1869 O O . THR A 1 246 ? 62.793 -9.580 26.604 1.00 64.57 ? 277 THR B O 1 ATOM 1870 C CB . THR A 1 246 ? 64.165 -10.193 24.108 1.00 64.26 ? 277 THR B CB 1 ATOM 1871 O OG1 . THR A 1 246 ? 64.759 -10.015 22.820 1.00 64.78 ? 277 THR B OG1 1 ATOM 1872 C CG2 . THR A 1 246 ? 63.673 -11.621 24.254 1.00 63.01 ? 277 THR B CG2 1 ATOM 1873 N N . LEU A 1 247 ? 61.054 -10.152 25.332 1.00 65.44 ? 278 LEU B N 1 ATOM 1874 C CA . LEU A 1 247 ? 60.329 -10.694 26.456 1.00 64.93 ? 278 LEU B CA 1 ATOM 1875 C C . LEU A 1 247 ? 59.705 -12.040 26.108 1.00 64.06 ? 278 LEU B C 1 ATOM 1876 O O . LEU A 1 247 ? 58.733 -12.096 25.349 1.00 64.85 ? 278 LEU B O 1 ATOM 1877 C CB . LEU A 1 247 ? 59.229 -9.706 26.789 1.00 66.56 ? 278 LEU B CB 1 ATOM 1878 C CG . LEU A 1 247 ? 58.285 -10.058 27.918 1.00 66.52 ? 278 LEU B CG 1 ATOM 1879 C CD1 . LEU A 1 247 ? 59.055 -10.162 29.209 1.00 65.57 ? 278 LEU B CD1 1 ATOM 1880 C CD2 . LEU A 1 247 ? 57.221 -8.986 27.994 1.00 68.44 ? 278 LEU B CD2 1 ATOM 1881 N N . PHE A 1 248 ? 60.215 -13.126 26.682 1.00 63.18 ? 279 PHE B N 1 ATOM 1882 C CA . PHE A 1 248 ? 59.587 -14.424 26.444 1.00 62.90 ? 279 PHE B CA 1 ATOM 1883 C C . PHE A 1 248 ? 59.044 -14.987 27.743 1.00 62.70 ? 279 PHE B C 1 ATOM 1884 O O . PHE A 1 248 ? 59.810 -15.495 28.551 1.00 61.81 ? 279 PHE B O 1 ATOM 1885 C CB . PHE A 1 248 ? 60.604 -15.418 25.880 1.00 61.88 ? 279 PHE B CB 1 ATOM 1886 C CG . PHE A 1 248 ? 61.270 -14.968 24.607 1.00 62.07 ? 279 PHE B CG 1 ATOM 1887 C CD1 . PHE A 1 248 ? 60.584 -14.225 23.669 1.00 63.16 ? 279 PHE B CD1 1 ATOM 1888 C CD2 . PHE A 1 248 ? 62.586 -15.298 24.352 1.00 61.25 ? 279 PHE B CD2 1 ATOM 1889 C CE1 . PHE A 1 248 ? 61.196 -13.816 22.510 1.00 63.42 ? 279 PHE B CE1 1 ATOM 1890 C CE2 . PHE A 1 248 ? 63.196 -14.892 23.197 1.00 61.54 ? 279 PHE B CE2 1 ATOM 1891 C CZ . PHE A 1 248 ? 62.498 -14.150 22.273 1.00 62.62 ? 279 PHE B CZ 1 ATOM 1892 N N . LEU A 1 249 ? 57.729 -14.912 27.934 1.00 62.89 ? 280 LEU B N 1 ATOM 1893 C CA . LEU A 1 249 ? 57.056 -15.468 29.116 1.00 62.93 ? 280 LEU B CA 1 ATOM 1894 C C . LEU A 1 249 ? 56.344 -16.778 28.855 1.00 62.83 ? 280 LEU B C 1 ATOM 1895 O O . LEU A 1 249 ? 55.570 -17.230 29.696 1.00 63.13 ? 280 LEU B O 1 ATOM 1896 C CB . LEU A 1 249 ? 56.062 -14.485 29.718 1.00 64.08 ? 280 LEU B CB 1 ATOM 1897 C CG . LEU A 1 249 ? 56.584 -13.130 30.140 1.00 64.35 ? 280 LEU B CG 1 ATOM 1898 C CD1 . LEU A 1 249 ? 55.643 -12.584 31.166 1.00 65.38 ? 280 LEU B CD1 1 ATOM 1899 C CD2 . LEU A 1 249 ? 57.966 -13.289 30.696 1.00 63.20 ? 280 LEU B CD2 1 ATOM 1900 N N . PHE A 1 250 ? 56.520 -17.323 27.656 1.00 64.96 ? 281 PHE B N 1 ATOM 1901 C CA . PHE A 1 250 ? 55.691 -18.439 27.181 1.00 65.47 ? 281 PHE B CA 1 ATOM 1902 C C . PHE A 1 250 ? 55.750 -19.777 27.939 1.00 65.24 ? 281 PHE B C 1 ATOM 1903 O O . PHE A 1 250 ? 56.797 -20.182 28.446 1.00 64.33 ? 281 PHE B O 1 ATOM 1904 C CB . PHE A 1 250 ? 55.891 -18.671 25.677 1.00 65.33 ? 281 PHE B CB 1 ATOM 1905 C CG . PHE A 1 250 ? 57.293 -19.072 25.281 1.00 64.30 ? 281 PHE B CG 1 ATOM 1906 C CD1 . PHE A 1 250 ? 57.666 -20.406 25.245 1.00 63.84 ? 281 PHE B CD1 1 ATOM 1907 C CD2 . PHE A 1 250 ? 58.222 -18.113 24.899 1.00 63.88 ? 281 PHE B CD2 1 ATOM 1908 C CE1 . PHE A 1 250 ? 58.945 -20.772 24.862 1.00 62.96 ? 281 PHE B CE1 1 ATOM 1909 C CE2 . PHE A 1 250 ? 59.502 -18.479 24.514 1.00 63.05 ? 281 PHE B CE2 1 ATOM 1910 C CZ . PHE A 1 250 ? 59.863 -19.811 24.497 1.00 62.58 ? 281 PHE B CZ 1 ATOM 1911 N N . GLN A 1 251 ? 54.609 -20.462 27.955 1.00 68.75 ? 282 GLN B N 1 ATOM 1912 C CA . GLN A 1 251 ? 54.428 -21.709 28.690 1.00 68.99 ? 282 GLN B CA 1 ATOM 1913 C C . GLN A 1 251 ? 54.567 -21.585 30.198 1.00 68.99 ? 282 GLN B C 1 ATOM 1914 O O . GLN A 1 251 ? 55.491 -22.136 30.796 1.00 68.23 ? 282 GLN B O 1 ATOM 1915 C CB . GLN A 1 251 ? 55.420 -22.762 28.214 1.00 68.05 ? 282 GLN B CB 1 ATOM 1916 C CG . GLN A 1 251 ? 55.159 -23.324 26.847 1.00 67.84 ? 282 GLN B CG 1 ATOM 1917 C CD . GLN A 1 251 ? 56.044 -24.504 26.583 1.00 67.32 ? 282 GLN B CD 1 ATOM 1918 O OE1 . GLN A 1 251 ? 57.119 -24.370 25.993 1.00 66.71 ? 282 GLN B OE1 1 ATOM 1919 N NE2 . GLN A 1 251 ? 55.616 -25.674 27.051 1.00 67.58 ? 282 GLN B NE2 1 ATOM 1920 N N . ASN A 1 252 ? 53.624 -20.881 30.807 1.00 77.52 ? 283 ASN B N 1 ATOM 1921 C CA . ASN A 1 252 ? 53.560 -20.739 32.250 1.00 77.67 ? 283 ASN B CA 1 ATOM 1922 C C . ASN A 1 252 ? 52.106 -20.635 32.694 1.00 79.15 ? 283 ASN B C 1 ATOM 1923 O O . ASN A 1 252 ? 51.200 -20.938 31.926 1.00 80.13 ? 283 ASN B O 1 ATOM 1924 C CB . ASN A 1 252 ? 54.376 -19.536 32.713 1.00 76.77 ? 283 ASN B CB 1 ATOM 1925 C CG . ASN A 1 252 ? 55.859 -19.853 32.852 1.00 75.42 ? 283 ASN B CG 1 ATOM 1926 O OD1 . ASN A 1 252 ? 56.344 -20.137 33.943 1.00 75.31 ? 283 ASN B OD1 1 ATOM 1927 N ND2 . ASN A 1 252 ? 56.585 -19.799 31.746 1.00 74.42 ? 283 ASN B ND2 1 ATOM 1928 N N . GLY A 1 253 ? 51.880 -20.240 33.942 1.00 70.41 ? 284 GLY B N 1 ATOM 1929 C CA . GLY A 1 253 ? 50.533 -20.191 34.496 1.00 71.80 ? 284 GLY B CA 1 ATOM 1930 C C . GLY A 1 253 ? 49.897 -18.828 34.674 1.00 72.22 ? 284 GLY B C 1 ATOM 1931 O O . GLY A 1 253 ? 48.943 -18.698 35.427 1.00 73.17 ? 284 GLY B O 1 ATOM 1932 N N . PHE A 1 254 ? 50.415 -17.824 33.976 1.00 68.97 ? 285 PHE B N 1 ATOM 1933 C CA . PHE A 1 254 ? 49.968 -16.447 34.142 1.00 69.28 ? 285 PHE B CA 1 ATOM 1934 C C . PHE A 1 254 ? 48.490 -16.251 33.844 1.00 70.78 ? 285 PHE B C 1 ATOM 1935 O O . PHE A 1 254 ? 47.936 -16.925 32.995 1.00 71.14 ? 285 PHE B O 1 ATOM 1936 C CB . PHE A 1 254 ? 50.810 -15.524 33.280 1.00 68.86 ? 285 PHE B CB 1 ATOM 1937 C CG . PHE A 1 254 ? 52.243 -15.488 33.684 1.00 67.57 ? 285 PHE B CG 1 ATOM 1938 C CD1 . PHE A 1 254 ? 52.611 -14.975 34.912 1.00 67.52 ? 285 PHE B CD1 1 ATOM 1939 C CD2 . PHE A 1 254 ? 53.225 -15.973 32.849 1.00 66.46 ? 285 PHE B CD2 1 ATOM 1940 C CE1 . PHE A 1 254 ? 53.936 -14.940 35.300 1.00 66.38 ? 285 PHE B CE1 1 ATOM 1941 C CE2 . PHE A 1 254 ? 54.550 -15.940 33.233 1.00 65.34 ? 285 PHE B CE2 1 ATOM 1942 C CZ . PHE A 1 254 ? 54.906 -15.427 34.464 1.00 65.30 ? 285 PHE B CZ 1 ATOM 1943 N N . THR A 1 255 ? 47.864 -15.309 34.544 1.00 75.08 ? 286 THR B N 1 ATOM 1944 C CA . THR A 1 255 ? 46.417 -15.150 34.524 1.00 76.42 ? 286 THR B CA 1 ATOM 1945 C C . THR A 1 255 ? 45.994 -13.691 34.441 1.00 76.45 ? 286 THR B C 1 ATOM 1946 O O . THR A 1 255 ? 46.833 -12.790 34.405 1.00 75.44 ? 286 THR B O 1 ATOM 1947 C CB . THR A 1 255 ? 45.822 -15.749 35.789 1.00 77.27 ? 286 THR B CB 1 ATOM 1948 O OG1 . THR A 1 255 ? 46.865 -15.931 36.758 1.00 76.16 ? 286 THR B OG1 1 ATOM 1949 C CG2 . THR A 1 255 ? 45.224 -17.083 35.481 1.00 78.30 ? 286 THR B CG2 1 ATOM 1950 N N . GLY A 1 256 ? 44.687 -13.459 34.405 1.00 97.34 ? 287 GLY B N 1 ATOM 1951 C CA . GLY A 1 256 ? 44.165 -12.105 34.396 1.00 97.48 ? 287 GLY B CA 1 ATOM 1952 C C . GLY A 1 256 ? 44.510 -11.401 33.100 1.00 97.00 ? 287 GLY B C 1 ATOM 1953 O O . GLY A 1 256 ? 45.200 -11.966 32.256 1.00 96.43 ? 287 GLY B O 1 ATOM 1954 N N . GLU A 1 257 ? 44.042 -10.167 32.940 1.00 99.55 ? 288 GLU B N 1 ATOM 1955 C CA . GLU A 1 257 ? 44.310 -9.414 31.714 1.00 99.39 ? 288 GLU B CA 1 ATOM 1956 C C . GLU A 1 257 ? 45.805 -9.074 31.575 1.00 97.91 ? 288 GLU B C 1 ATOM 1957 O O . GLU A 1 257 ? 46.556 -9.111 32.555 1.00 97.02 ? 288 GLU B O 1 ATOM 1958 C CB . GLU A 1 257 ? 43.446 -8.137 31.635 1.00 101.52 ? 288 GLU B CB 1 ATOM 1959 C CG . GLU A 1 257 ? 42.047 -8.298 31.003 1.00 103.07 ? 288 GLU B CG 1 ATOM 1960 C CD . GLU A 1 257 ? 41.635 -7.079 30.164 1.00 104.63 ? 288 GLU B CD 1 ATOM 1961 O OE1 . GLU A 1 257 ? 40.470 -7.003 29.707 1.00 106.17 ? 288 GLU B OE1 1 ATOM 1962 O OE2 . GLU A 1 257 ? 42.487 -6.192 29.952 1.00 104.37 ? 288 GLU B OE2 1 ATOM 1963 N N . ILE A 1 258 ? 46.229 -8.787 30.344 1.00 78.69 ? 289 ILE B N 1 ATOM 1964 C CA . ILE A 1 258 ? 47.560 -8.256 30.056 1.00 77.89 ? 289 ILE B CA 1 ATOM 1965 C C . ILE A 1 258 ? 47.512 -6.778 30.361 1.00 79.81 ? 289 ILE B C 1 ATOM 1966 O O . ILE A 1 258 ? 46.696 -6.062 29.775 1.00 81.72 ? 289 ILE B O 1 ATOM 1967 C CB . ILE A 1 258 ? 47.898 -8.355 28.555 1.00 77.54 ? 289 ILE B CB 1 ATOM 1968 C CG1 . ILE A 1 258 ? 47.320 -9.625 27.945 1.00 76.63 ? 289 ILE B CG1 1 ATOM 1969 C CG2 . ILE A 1 258 ? 49.385 -8.234 28.309 1.00 76.18 ? 289 ILE B CG2 1 ATOM 1970 C CD1 . ILE A 1 258 ? 45.989 -9.399 27.246 1.00 78.42 ? 289 ILE B CD1 1 ATOM 1971 N N . PRO A 1 259 ? 48.376 -6.308 31.271 1.00 100.22 ? 290 PRO B N 1 ATOM 1972 C CA . PRO A 1 259 ? 48.377 -4.906 31.712 1.00 101.56 ? 290 PRO B CA 1 ATOM 1973 C C . PRO A 1 259 ? 48.601 -3.913 30.572 1.00 102.61 ? 290 PRO B C 1 ATOM 1974 O O . PRO A 1 259 ? 49.475 -4.125 29.737 1.00 101.46 ? 290 PRO B O 1 ATOM 1975 C CB . PRO A 1 259 ? 49.540 -4.859 32.702 1.00 100.31 ? 290 PRO B CB 1 ATOM 1976 C CG . PRO A 1 259 ? 49.635 -6.252 33.216 1.00 98.91 ? 290 PRO B CG 1 ATOM 1977 C CD . PRO A 1 259 ? 49.324 -7.127 32.042 1.00 98.48 ? 290 PRO B CD 1 ATOM 1978 N N . GLU A 1 260 ? 47.815 -2.841 30.546 1.00 97.23 ? 291 GLU B N 1 ATOM 1979 C CA . GLU A 1 260 ? 47.907 -1.867 29.473 1.00 98.66 ? 291 GLU B CA 1 ATOM 1980 C C . GLU A 1 260 ? 49.272 -1.205 29.453 1.00 98.05 ? 291 GLU B C 1 ATOM 1981 O O . GLU A 1 260 ? 49.719 -0.686 28.429 1.00 98.52 ? 291 GLU B O 1 ATOM 1982 C CB . GLU A 1 260 ? 46.818 -0.816 29.621 1.00 101.49 ? 291 GLU B CB 1 ATOM 1983 C CG . GLU A 1 260 ? 45.442 -1.306 29.240 1.00 102.51 ? 291 GLU B CG 1 ATOM 1984 C CD . GLU A 1 260 ? 44.751 -0.360 28.275 1.00 105.00 ? 291 GLU B CD 1 ATOM 1985 O OE1 . GLU A 1 260 ? 44.154 0.639 28.740 1.00 107.28 ? 291 GLU B OE1 1 ATOM 1986 O OE2 . GLU A 1 260 ? 44.812 -0.609 27.050 1.00 104.77 ? 291 GLU B OE2 1 ATOM 1987 N N . SER A 1 261 ? 49.947 -1.255 30.590 1.00 89.57 ? 292 SER B N 1 ATOM 1988 C CA . SER A 1 261 ? 51.202 -0.538 30.760 1.00 89.18 ? 292 SER B CA 1 ATOM 1989 C C . SER A 1 261 ? 52.251 -1.004 29.775 1.00 87.57 ? 292 SER B C 1 ATOM 1990 O O . SER A 1 261 ? 53.177 -0.272 29.450 1.00 87.72 ? 292 SER B O 1 ATOM 1991 C CB . SER A 1 261 ? 51.727 -0.652 32.205 1.00 88.24 ? 292 SER B CB 1 ATOM 1992 O OG . SER A 1 261 ? 52.177 -1.958 32.522 1.00 85.93 ? 292 SER B OG 1 ATOM 1993 N N . TYR A 1 262 ? 52.093 -2.218 29.278 1.00 85.00 ? 293 TYR B N 1 ATOM 1994 C CA . TYR A 1 262 ? 53.101 -2.777 28.399 1.00 83.42 ? 293 TYR B CA 1 ATOM 1995 C C . TYR A 1 262 ? 53.190 -1.975 27.119 1.00 84.78 ? 293 TYR B C 1 ATOM 1996 O O . TYR A 1 262 ? 54.209 -1.997 26.440 1.00 83.99 ? 293 TYR B O 1 ATOM 1997 C CB . TYR A 1 262 ? 52.858 -4.267 28.159 1.00 81.82 ? 293 TYR B CB 1 ATOM 1998 C CG . TYR A 1 262 ? 53.162 -5.068 29.391 1.00 80.48 ? 293 TYR B CG 1 ATOM 1999 C CD1 . TYR A 1 262 ? 52.230 -5.195 30.409 1.00 81.01 ? 293 TYR B CD1 1 ATOM 2000 C CD2 . TYR A 1 262 ? 54.392 -5.657 29.561 1.00 78.87 ? 293 TYR B CD2 1 ATOM 2001 C CE1 . TYR A 1 262 ? 52.512 -5.901 31.544 1.00 80.02 ? 293 TYR B CE1 1 ATOM 2002 C CE2 . TYR A 1 262 ? 54.679 -6.372 30.699 1.00 77.85 ? 293 TYR B CE2 1 ATOM 2003 C CZ . TYR A 1 262 ? 53.735 -6.490 31.689 1.00 78.44 ? 293 TYR B CZ 1 ATOM 2004 O OH . TYR A 1 262 ? 54.022 -7.202 32.830 1.00 77.51 ? 293 TYR B OH 1 ATOM 2005 N N . SER A 1 263 ? 52.181 -1.155 26.864 1.00 95.50 ? 294 SER B N 1 ATOM 2006 C CA . SER A 1 263 ? 52.192 -0.309 25.681 1.00 97.12 ? 294 SER B CA 1 ATOM 2007 C C . SER A 1 263 ? 53.407 0.629 25.736 1.00 97.27 ? 294 SER B C 1 ATOM 2008 O O . SER A 1 263 ? 53.664 1.412 24.814 1.00 98.58 ? 294 SER B O 1 ATOM 2009 C CB . SER A 1 263 ? 50.890 0.493 25.577 1.00 99.70 ? 294 SER B CB 1 ATOM 2010 O OG . SER A 1 263 ? 49.766 -0.364 25.468 1.00 99.64 ? 294 SER B OG 1 ATOM 2011 N N . ASN A 1 264 ? 54.139 0.560 26.843 1.00 87.35 ? 295 ASN B N 1 ATOM 2012 C CA . ASN A 1 264 ? 55.260 1.450 27.067 1.00 87.49 ? 295 ASN B CA 1 ATOM 2013 C C . ASN A 1 264 ? 56.648 0.940 26.687 1.00 85.60 ? 295 ASN B C 1 ATOM 2014 O O . ASN A 1 264 ? 57.606 1.697 26.775 1.00 85.80 ? 295 ASN B O 1 ATOM 2015 C CB . ASN A 1 264 ? 55.257 1.945 28.516 1.00 87.73 ? 295 ASN B CB 1 ATOM 2016 C CG . ASN A 1 264 ? 53.951 2.622 28.895 1.00 89.95 ? 295 ASN B CG 1 ATOM 2017 O OD1 . ASN A 1 264 ? 53.644 3.727 28.436 1.00 92.10 ? 295 ASN B OD1 1 ATOM 2018 N ND2 . ASN A 1 264 ? 53.172 1.958 29.737 1.00 89.54 ? 295 ASN B ND2 1 ATOM 2019 N N . LEU A 1 265 ? 56.798 -0.301 26.243 1.00 80.56 ? 296 LEU B N 1 ATOM 2020 C CA . LEU A 1 265 ? 58.147 -0.681 25.854 1.00 79.04 ? 296 LEU B CA 1 ATOM 2021 C C . LEU A 1 265 ? 58.251 -0.368 24.386 1.00 80.05 ? 296 LEU B C 1 ATOM 2022 O O . LEU A 1 265 ? 57.777 -1.125 23.549 1.00 79.77 ? 296 LEU B O 1 ATOM 2023 C CB . LEU A 1 265 ? 58.377 -2.166 26.078 1.00 76.76 ? 296 LEU B CB 1 ATOM 2024 C CG . LEU A 1 265 ? 57.745 -2.684 27.362 1.00 76.12 ? 296 LEU B CG 1 ATOM 2025 C CD1 . LEU A 1 265 ? 56.716 -3.761 27.086 1.00 75.67 ? 296 LEU B CD1 1 ATOM 2026 C CD2 . LEU A 1 265 ? 58.818 -3.209 28.273 1.00 74.27 ? 296 LEU B CD2 1 ATOM 2027 N N . LYS A 1 266 ? 58.930 0.719 24.061 1.00 100.12 ? 297 LYS B N 1 ATOM 2028 C CA . LYS A 1 266 ? 58.948 1.167 22.683 1.00 101.47 ? 297 LYS B CA 1 ATOM 2029 C C . LYS A 1 266 ? 60.110 0.513 21.970 1.00 100.07 ? 297 LYS B C 1 ATOM 2030 O O . LYS A 1 266 ? 60.212 0.543 20.743 1.00 100.80 ? 297 LYS B O 1 ATOM 2031 C CB . LYS A 1 266 ? 59.035 2.686 22.615 1.00 103.69 ? 297 LYS B CB 1 ATOM 2032 C CG . LYS A 1 266 ? 57.689 3.383 22.761 1.00 105.81 ? 297 LYS B CG 1 ATOM 2033 C CD . LYS A 1 266 ? 56.896 3.345 21.454 1.00 107.21 ? 297 LYS B CD 1 ATOM 2034 C CE . LYS A 1 266 ? 55.666 4.241 21.523 1.00 109.70 ? 297 LYS B CE 1 ATOM 2035 N NZ . LYS A 1 266 ? 54.778 3.849 22.652 1.00 109.26 ? 297 LYS B NZ 1 ATOM 2036 N N . SER A 1 267 ? 60.974 -0.106 22.760 1.00 87.37 ? 298 SER B N 1 ATOM 2037 C CA . SER A 1 267 ? 62.144 -0.762 22.228 1.00 86.00 ? 298 SER B CA 1 ATOM 2038 C C . SER A 1 267 ? 61.848 -2.235 22.036 1.00 84.32 ? 298 SER B C 1 ATOM 2039 O O . SER A 1 267 ? 62.687 -2.980 21.534 1.00 83.14 ? 298 SER B O 1 ATOM 2040 C CB . SER A 1 267 ? 63.290 -0.576 23.203 1.00 84.93 ? 298 SER B CB 1 ATOM 2041 O OG . SER A 1 267 ? 62.800 -0.723 24.524 1.00 84.32 ? 298 SER B OG 1 ATOM 2042 N N . LEU A 1 268 ? 60.646 -2.650 22.426 1.00 86.82 ? 299 LEU B N 1 ATOM 2043 C CA . LEU A 1 268 ? 60.277 -4.061 22.375 1.00 85.27 ? 299 LEU B CA 1 ATOM 2044 C C . LEU A 1 268 ? 60.235 -4.579 20.960 1.00 85.42 ? 299 LEU B C 1 ATOM 2045 O O . LEU A 1 268 ? 59.624 -3.965 20.093 1.00 87.12 ? 299 LEU B O 1 ATOM 2046 C CB . LEU A 1 268 ? 58.924 -4.299 23.032 1.00 85.60 ? 299 LEU B CB 1 ATOM 2047 C CG . LEU A 1 268 ? 58.631 -5.769 23.315 1.00 84.13 ? 299 LEU B CG 1 ATOM 2048 C CD1 . LEU A 1 268 ? 59.844 -6.446 23.926 1.00 82.49 ? 299 LEU B CD1 1 ATOM 2049 C CD2 . LEU A 1 268 ? 57.467 -5.870 24.256 1.00 84.48 ? 299 LEU B CD2 1 ATOM 2050 N N . LYS A 1 269 ? 60.885 -5.714 20.739 1.00 74.46 ? 300 LYS B N 1 ATOM 2051 C CA . LYS A 1 269 ? 60.943 -6.325 19.424 1.00 74.47 ? 300 LYS B CA 1 ATOM 2052 C C . LYS A 1 269 ? 60.174 -7.642 19.389 1.00 73.39 ? 300 LYS B C 1 ATOM 2053 O O . LYS A 1 269 ? 59.209 -7.793 18.645 1.00 74.16 ? 300 LYS B O 1 ATOM 2054 C CB . LYS A 1 269 ? 62.389 -6.564 19.007 1.00 73.65 ? 300 LYS B CB 1 ATOM 2055 C CG . LYS A 1 269 ? 63.233 -5.318 18.897 1.00 74.80 ? 300 LYS B CG 1 ATOM 2056 C CD . LYS A 1 269 ? 64.526 -5.625 18.154 1.00 74.32 ? 300 LYS B CD 1 ATOM 2057 C CE . LYS A 1 269 ? 65.628 -4.599 18.434 1.00 74.87 ? 300 LYS B CE 1 ATOM 2058 N NZ . LYS A 1 269 ? 65.379 -3.239 17.868 1.00 77.10 ? 300 LYS B NZ 1 ATOM 2059 N N . LEU A 1 270 ? 60.630 -8.604 20.182 1.00 69.80 ? 301 LEU B N 1 ATOM 2060 C CA . LEU A 1 270 ? 60.008 -9.918 20.240 1.00 68.66 ? 301 LEU B CA 1 ATOM 2061 C C . LEU A 1 270 ? 59.212 -10.057 21.513 1.00 68.97 ? 301 LEU B C 1 ATOM 2062 O O . LEU A 1 270 ? 59.720 -9.823 22.597 1.00 68.78 ? 301 LEU B O 1 ATOM 2063 C CB . LEU A 1 270 ? 61.070 -11.008 20.233 1.00 67.95 ? 301 LEU B CB 1 ATOM 2064 C CG . LEU A 1 270 ? 62.400 -10.591 19.624 1.00 67.71 ? 301 LEU B CG 1 ATOM 2065 C CD1 . LEU A 1 270 ? 63.521 -11.548 20.039 1.00 67.07 ? 301 LEU B CD1 1 ATOM 2066 C CD2 . LEU A 1 270 ? 62.259 -10.516 18.115 1.00 68.20 ? 301 LEU B CD2 1 ATOM 2067 N N . LEU A 1 271 ? 57.964 -10.462 21.376 1.00 73.58 ? 302 LEU B N 1 ATOM 2068 C CA . LEU A 1 271 ? 57.126 -10.696 22.525 1.00 74.11 ? 302 LEU B CA 1 ATOM 2069 C C . LEU A 1 271 ? 56.455 -12.057 22.364 1.00 74.54 ? 302 LEU B C 1 ATOM 2070 O O . LEU A 1 271 ? 55.714 -12.275 21.399 1.00 75.03 ? 302 LEU B O 1 ATOM 2071 C CB . LEU A 1 271 ? 56.088 -9.585 22.611 1.00 74.82 ? 302 LEU B CB 1 ATOM 2072 C CG . LEU A 1 271 ? 55.393 -9.356 23.947 1.00 75.40 ? 302 LEU B CG 1 ATOM 2073 C CD1 . LEU A 1 271 ? 54.674 -8.057 23.889 1.00 76.49 ? 302 LEU B CD1 1 ATOM 2074 C CD2 . LEU A 1 271 ? 54.400 -10.430 24.222 1.00 75.65 ? 302 LEU B CD2 1 ATOM 2075 N N . ASP A 1 272 ? 56.714 -12.981 23.287 1.00 65.94 ? 303 ASP B N 1 ATOM 2076 C CA . ASP A 1 272 ? 56.030 -14.276 23.234 1.00 65.28 ? 303 ASP B CA 1 ATOM 2077 C C . ASP A 1 272 ? 55.388 -14.660 24.576 1.00 65.23 ? 303 ASP B C 1 ATOM 2078 O O . ASP A 1 272 ? 56.071 -14.984 25.548 1.00 64.39 ? 303 ASP B O 1 ATOM 2079 C CB . ASP A 1 272 ? 56.989 -15.376 22.732 1.00 64.15 ? 303 ASP B CB 1 ATOM 2080 C CG . ASP A 1 272 ? 56.264 -16.643 22.290 1.00 64.00 ? 303 ASP B CG 1 ATOM 2081 O OD1 . ASP A 1 272 ? 55.355 -17.082 23.020 1.00 64.20 ? 303 ASP B OD1 1 ATOM 2082 O OD2 . ASP A 1 272 ? 56.598 -17.200 21.212 1.00 63.74 ? 303 ASP B OD2 1 ATOM 2083 N N . PHE A 1 273 ? 54.060 -14.621 24.599 1.00 73.63 ? 304 PHE B N 1 ATOM 2084 C CA . PHE A 1 273 ? 53.261 -14.950 25.777 1.00 74.21 ? 304 PHE B CA 1 ATOM 2085 C C . PHE A 1 273 ? 52.614 -16.329 25.798 1.00 74.80 ? 304 PHE B C 1 ATOM 2086 O O . PHE A 1 273 ? 51.795 -16.616 26.669 1.00 75.54 ? 304 PHE B O 1 ATOM 2087 C CB . PHE A 1 273 ? 52.216 -13.874 26.017 1.00 74.98 ? 304 PHE B CB 1 ATOM 2088 C CG . PHE A 1 273 ? 52.780 -12.611 26.594 1.00 74.48 ? 304 PHE B CG 1 ATOM 2089 C CD1 . PHE A 1 273 ? 54.121 -12.525 26.917 1.00 73.45 ? 304 PHE B CD1 1 ATOM 2090 C CD2 . PHE A 1 273 ? 51.969 -11.519 26.828 1.00 75.04 ? 304 PHE B CD2 1 ATOM 2091 C CE1 . PHE A 1 273 ? 54.640 -11.370 27.450 1.00 73.01 ? 304 PHE B CE1 1 ATOM 2092 C CE2 . PHE A 1 273 ? 52.485 -10.367 27.357 1.00 74.54 ? 304 PHE B CE2 1 ATOM 2093 C CZ . PHE A 1 273 ? 53.822 -10.288 27.667 1.00 73.54 ? 304 PHE B CZ 1 ATOM 2094 N N . SER A 1 274 ? 52.946 -17.149 24.808 1.00 71.72 ? 305 SER B N 1 ATOM 2095 C CA . SER A 1 274 ? 52.189 -18.361 24.462 1.00 72.37 ? 305 SER B CA 1 ATOM 2096 C C . SER A 1 274 ? 52.043 -19.482 25.489 1.00 72.60 ? 305 SER B C 1 ATOM 2097 O O . SER A 1 274 ? 52.930 -19.731 26.299 1.00 71.86 ? 305 SER B O 1 ATOM 2098 C CB . SER A 1 274 ? 52.759 -18.952 23.186 1.00 71.89 ? 305 SER B CB 1 ATOM 2099 O OG . SER A 1 274 ? 54.165 -19.006 23.267 1.00 70.92 ? 305 SER B OG 1 ATOM 2100 N N . SER A 1 275 ? 50.919 -20.186 25.393 1.00 73.91 ? 306 SER B N 1 ATOM 2101 C CA . SER A 1 275 ? 50.555 -21.244 26.339 1.00 74.44 ? 306 SER B CA 1 ATOM 2102 C C . SER A 1 275 ? 50.427 -20.752 27.787 1.00 74.74 ? 306 SER B C 1 ATOM 2103 O O . SER A 1 275 ? 51.035 -21.317 28.691 1.00 74.32 ? 306 SER B O 1 ATOM 2104 C CB . SER A 1 275 ? 51.522 -22.444 26.257 1.00 73.54 ? 306 SER B CB 1 ATOM 2105 O OG . SER A 1 275 ? 51.000 -23.518 25.475 1.00 73.82 ? 306 SER B OG 1 ATOM 2106 N N . ASN A 1 276 ? 49.640 -19.692 27.981 1.00 76.56 ? 307 ASN B N 1 ATOM 2107 C CA . ASN A 1 276 ? 49.287 -19.172 29.300 1.00 77.03 ? 307 ASN B CA 1 ATOM 2108 C C . ASN A 1 276 ? 47.773 -19.045 29.456 1.00 78.51 ? 307 ASN B C 1 ATOM 2109 O O . ASN A 1 276 ? 47.013 -19.399 28.564 1.00 79.23 ? 307 ASN B O 1 ATOM 2110 C CB . ASN A 1 276 ? 49.918 -17.798 29.530 1.00 76.29 ? 307 ASN B CB 1 ATOM 2111 C CG . ASN A 1 276 ? 51.412 -17.867 29.793 1.00 74.94 ? 307 ASN B CG 1 ATOM 2112 O OD1 . ASN A 1 276 ? 51.851 -18.061 30.930 1.00 74.89 ? 307 ASN B OD1 1 ATOM 2113 N ND2 . ASN A 1 276 ? 52.204 -17.683 28.744 1.00 73.86 ? 307 ASN B ND2 1 ATOM 2114 N N . GLN A 1 277 ? 47.342 -18.542 30.604 1.00 83.60 ? 308 GLN B N 1 ATOM 2115 C CA . GLN A 1 277 ? 45.925 -18.315 30.881 1.00 85.07 ? 308 GLN B CA 1 ATOM 2116 C C . GLN A 1 277 ? 45.442 -16.883 30.642 1.00 85.26 ? 308 GLN B C 1 ATOM 2117 O O . GLN A 1 277 ? 44.339 -16.543 31.056 1.00 86.36 ? 308 GLN B O 1 ATOM 2118 C CB . GLN A 1 277 ? 45.582 -18.713 32.316 1.00 85.64 ? 308 GLN B CB 1 ATOM 2119 C CG . GLN A 1 277 ? 46.200 -20.008 32.774 1.00 85.10 ? 308 GLN B CG 1 ATOM 2120 C CD . GLN A 1 277 ? 45.327 -21.198 32.481 1.00 86.33 ? 308 GLN B CD 1 ATOM 2121 O OE1 . GLN A 1 277 ? 44.870 -21.386 31.353 1.00 87.04 ? 308 GLN B OE1 1 ATOM 2122 N NE2 . GLN A 1 277 ? 45.078 -22.011 33.502 1.00 86.61 ? 308 GLN B NE2 1 ATOM 2123 N N . LEU A 1 278 ? 46.276 -16.026 30.060 1.00 80.68 ? 309 LEU B N 1 ATOM 2124 C CA . LEU A 1 278 ? 45.936 -14.607 29.951 1.00 80.72 ? 309 LEU B CA 1 ATOM 2125 C C . LEU A 1 278 ? 44.554 -14.357 29.329 1.00 82.05 ? 309 LEU B C 1 ATOM 2126 O O . LEU A 1 278 ? 44.178 -15.012 28.354 1.00 82.63 ? 309 LEU B O 1 ATOM 2127 C CB . LEU A 1 278 ? 47.014 -13.858 29.172 1.00 79.49 ? 309 LEU B CB 1 ATOM 2128 C CG . LEU A 1 278 ? 48.430 -13.973 29.725 1.00 78.15 ? 309 LEU B CG 1 ATOM 2129 C CD1 . LEU A 1 278 ? 49.318 -12.963 29.036 1.00 77.17 ? 309 LEU B CD1 1 ATOM 2130 C CD2 . LEU A 1 278 ? 48.449 -13.769 31.227 1.00 78.15 ? 309 LEU B CD2 1 ATOM 2131 N N . SER A 1 279 ? 43.800 -13.419 29.906 1.00 86.59 ? 310 SER B N 1 ATOM 2132 C CA . SER A 1 279 ? 42.408 -13.195 29.516 1.00 87.98 ? 310 SER B CA 1 ATOM 2133 C C . SER A 1 279 ? 42.145 -11.753 29.123 1.00 87.87 ? 310 SER B C 1 ATOM 2134 O O . SER A 1 279 ? 43.025 -10.906 29.226 1.00 86.77 ? 310 SER B O 1 ATOM 2135 C CB . SER A 1 279 ? 41.481 -13.567 30.671 1.00 89.38 ? 310 SER B CB 1 ATOM 2136 O OG . SER A 1 279 ? 42.151 -14.389 31.615 1.00 87.30 ? 310 SER B OG 1 ATOM 2137 N N . GLY A 1 280 ? 40.921 -11.476 28.688 1.00 87.37 ? 311 GLY B N 1 ATOM 2138 C CA . GLY A 1 280 ? 40.540 -10.133 28.281 1.00 87.97 ? 311 GLY B CA 1 ATOM 2139 C C . GLY A 1 280 ? 41.217 -9.664 27.005 1.00 87.47 ? 311 GLY B C 1 ATOM 2140 O O . GLY A 1 280 ? 42.074 -10.355 26.466 1.00 86.30 ? 311 GLY B O 1 ATOM 2141 N N . SER A 1 281 ? 40.868 -8.469 26.538 1.00 89.43 ? 312 SER B N 1 ATOM 2142 C CA . SER A 1 281 ? 41.325 -8.015 25.228 1.00 89.45 ? 312 SER B CA 1 ATOM 2143 C C . SER A 1 281 ? 42.812 -7.689 25.198 1.00 88.06 ? 312 SER B C 1 ATOM 2144 O O . SER A 1 281 ? 43.508 -7.805 26.205 1.00 87.02 ? 312 SER B O 1 ATOM 2145 C CB . SER A 1 281 ? 40.520 -6.799 24.766 1.00 91.74 ? 312 SER B CB 1 ATOM 2146 O OG . SER A 1 281 ? 39.153 -7.123 24.610 1.00 93.06 ? 312 SER B OG 1 ATOM 2147 N N . ILE A 1 282 ? 43.285 -7.290 24.021 1.00 87.88 ? 313 ILE B N 1 ATOM 2148 C CA . ILE A 1 282 ? 44.649 -6.802 23.836 1.00 86.94 ? 313 ILE B CA 1 ATOM 2149 C C . ILE A 1 282 ? 44.663 -5.293 24.064 1.00 88.71 ? 313 ILE B C 1 ATOM 2150 O O . ILE A 1 282 ? 43.720 -4.595 23.665 1.00 90.94 ? 313 ILE B O 1 ATOM 2151 C CB . ILE A 1 282 ? 45.149 -7.094 22.403 1.00 86.36 ? 313 ILE B CB 1 ATOM 2152 C CG1 . ILE A 1 282 ? 45.192 -8.599 22.135 1.00 84.78 ? 313 ILE B CG1 1 ATOM 2153 C CG2 . ILE A 1 282 ? 46.512 -6.475 22.154 1.00 85.74 ? 313 ILE B CG2 1 ATOM 2154 C CD1 . ILE A 1 282 ? 45.743 -8.949 20.775 1.00 84.15 ? 313 ILE B CD1 1 ATOM 2155 N N . PRO A 1 283 ? 45.720 -4.783 24.723 1.00 90.91 ? 314 PRO B N 1 ATOM 2156 C CA . PRO A 1 283 ? 45.865 -3.345 24.971 1.00 92.78 ? 314 PRO B CA 1 ATOM 2157 C C . PRO A 1 283 ? 45.717 -2.517 23.701 1.00 94.56 ? 314 PRO B C 1 ATOM 2158 O O . PRO A 1 283 ? 46.379 -2.800 22.706 1.00 93.72 ? 314 PRO B O 1 ATOM 2159 C CB . PRO A 1 283 ? 47.302 -3.241 25.477 1.00 91.18 ? 314 PRO B CB 1 ATOM 2160 C CG . PRO A 1 283 ? 47.517 -4.513 26.192 1.00 88.94 ? 314 PRO B CG 1 ATOM 2161 C CD . PRO A 1 283 ? 46.732 -5.563 25.456 1.00 88.58 ? 314 PRO B CD 1 ATOM 2162 N N . SER A 1 284 ? 44.870 -1.496 23.738 1.00 91.68 ? 315 SER B N 1 ATOM 2163 C CA . SER A 1 284 ? 44.712 -0.649 22.572 1.00 93.61 ? 315 SER B CA 1 ATOM 2164 C C . SER A 1 284 ? 46.061 -0.023 22.251 1.00 93.16 ? 315 SER B C 1 ATOM 2165 O O . SER A 1 284 ? 46.357 0.300 21.106 1.00 93.82 ? 315 SER B O 1 ATOM 2166 C CB . SER A 1 284 ? 43.655 0.429 22.824 1.00 96.57 ? 315 SER B CB 1 ATOM 2167 O OG . SER A 1 284 ? 43.000 0.805 21.619 1.00 98.46 ? 315 SER B OG 1 ATOM 2168 N N . GLY A 1 285 ? 46.889 0.113 23.280 1.00 106.76 ? 316 GLY B N 1 ATOM 2169 C CA . GLY A 1 285 ? 48.156 0.811 23.165 1.00 106.49 ? 316 GLY B CA 1 ATOM 2170 C C . GLY A 1 285 ? 49.260 0.003 22.518 1.00 104.27 ? 316 GLY B C 1 ATOM 2171 O O . GLY A 1 285 ? 50.323 0.523 22.168 1.00 104.15 ? 316 GLY B O 1 ATOM 2172 N N . PHE A 1 286 ? 49.007 -1.281 22.341 1.00 88.59 ? 317 PHE B N 1 ATOM 2173 C CA . PHE A 1 286 ? 49.969 -2.132 21.658 1.00 86.62 ? 317 PHE B CA 1 ATOM 2174 C C . PHE A 1 286 ? 50.273 -1.691 20.227 1.00 87.66 ? 317 PHE B C 1 ATOM 2175 O O . PHE A 1 286 ? 51.302 -2.084 19.664 1.00 86.38 ? 317 PHE B O 1 ATOM 2176 C CB . PHE A 1 286 ? 49.494 -3.576 21.664 1.00 84.95 ? 317 PHE B CB 1 ATOM 2177 C CG . PHE A 1 286 ? 50.202 -4.417 22.657 1.00 82.65 ? 317 PHE B CG 1 ATOM 2178 C CD1 . PHE A 1 286 ? 51.555 -4.239 22.873 1.00 81.53 ? 317 PHE B CD1 1 ATOM 2179 C CD2 . PHE A 1 286 ? 49.525 -5.360 23.395 1.00 81.72 ? 317 PHE B CD2 1 ATOM 2180 C CE1 . PHE A 1 286 ? 52.227 -5.007 23.795 1.00 79.50 ? 317 PHE B CE1 1 ATOM 2181 C CE2 . PHE A 1 286 ? 50.192 -6.131 24.324 1.00 79.72 ? 317 PHE B CE2 1 ATOM 2182 C CZ . PHE A 1 286 ? 51.547 -5.955 24.522 1.00 78.60 ? 317 PHE B CZ 1 ATOM 2183 N N . SER A 1 287 ? 49.387 -0.866 19.657 1.00 89.41 ? 318 SER B N 1 ATOM 2184 C CA . SER A 1 287 ? 49.565 -0.297 18.319 1.00 90.86 ? 318 SER B CA 1 ATOM 2185 C C . SER A 1 287 ? 50.825 0.552 18.243 1.00 91.03 ? 318 SER B C 1 ATOM 2186 O O . SER A 1 287 ? 51.267 0.912 17.152 1.00 91.87 ? 318 SER B O 1 ATOM 2187 C CB . SER A 1 287 ? 48.372 0.580 17.948 1.00 93.71 ? 318 SER B CB 1 ATOM 2188 O OG . SER A 1 287 ? 47.148 -0.013 18.328 1.00 93.81 ? 318 SER B OG 1 ATOM 2189 N N . THR A 1 288 ? 51.398 0.874 19.405 1.00 93.53 ? 319 THR B N 1 ATOM 2190 C CA . THR A 1 288 ? 52.485 1.848 19.474 1.00 94.00 ? 319 THR B CA 1 ATOM 2191 C C . THR A 1 288 ? 53.914 1.308 19.429 1.00 91.85 ? 319 THR B C 1 ATOM 2192 O O . THR A 1 288 ? 54.855 2.093 19.387 1.00 92.27 ? 319 THR B O 1 ATOM 2193 C CB . THR A 1 288 ? 52.356 2.755 20.724 1.00 94.87 ? 319 THR B CB 1 ATOM 2194 O OG1 . THR A 1 288 ? 52.569 1.980 21.907 1.00 92.79 ? 319 THR B OG1 1 ATOM 2195 C CG2 . THR A 1 288 ? 50.978 3.416 20.786 1.00 97.32 ? 319 THR B CG2 1 ATOM 2196 N N . LEU A 1 289 ? 54.111 -0.006 19.419 1.00 86.66 ? 320 LEU B N 1 ATOM 2197 C CA . LEU A 1 289 ? 55.492 -0.469 19.479 1.00 84.74 ? 320 LEU B CA 1 ATOM 2198 C C . LEU A 1 289 ? 55.984 -0.621 18.059 1.00 85.02 ? 320 LEU B C 1 ATOM 2199 O O . LEU A 1 289 ? 55.685 -1.605 17.384 1.00 84.25 ? 320 LEU B O 1 ATOM 2200 C CB . LEU A 1 289 ? 55.597 -1.811 20.202 1.00 82.27 ? 320 LEU B CB 1 ATOM 2201 C CG . LEU A 1 289 ? 54.633 -2.094 21.353 1.00 82.04 ? 320 LEU B CG 1 ATOM 2202 C CD1 . LEU A 1 289 ? 54.952 -3.435 21.951 1.00 79.59 ? 320 LEU B CD1 1 ATOM 2203 C CD2 . LEU A 1 289 ? 54.730 -1.040 22.409 1.00 82.95 ? 320 LEU B CD2 1 ATOM 2204 N N . LYS A 1 290 ? 56.805 0.332 17.641 1.00 112.25 ? 321 LYS B N 1 ATOM 2205 C CA . LYS A 1 290 ? 57.194 0.420 16.252 1.00 113.09 ? 321 LYS B CA 1 ATOM 2206 C C . LYS A 1 290 ? 58.509 -0.286 16.079 1.00 111.21 ? 321 LYS B C 1 ATOM 2207 O O . LYS A 1 290 ? 59.056 -0.322 14.983 1.00 111.66 ? 321 LYS B O 1 ATOM 2208 C CB . LYS A 1 290 ? 57.297 1.870 15.801 1.00 115.61 ? 321 LYS B CB 1 ATOM 2209 C CG . LYS A 1 290 ? 55.991 2.638 15.902 1.00 117.79 ? 321 LYS B CG 1 ATOM 2210 C CD . LYS A 1 290 ? 55.027 2.300 14.772 1.00 118.91 ? 321 LYS B CD 1 ATOM 2211 C CE . LYS A 1 290 ? 53.996 3.417 14.566 1.00 121.80 ? 321 LYS B CE 1 ATOM 2212 N NZ . LYS A 1 290 ? 53.145 3.263 13.341 1.00 123.28 ? 321 LYS B NZ 1 ATOM 2213 N N . ASN A 1 291 ? 59.044 -0.820 17.168 1.00 85.78 ? 322 ASN B N 1 ATOM 2214 C CA . ASN A 1 291 ? 60.186 -1.695 17.023 1.00 83.89 ? 322 ASN B CA 1 ATOM 2215 C C . ASN A 1 291 ? 59.829 -3.171 17.074 1.00 82.03 ? 322 ASN B C 1 ATOM 2216 O O . ASN A 1 291 ? 60.707 -4.026 16.964 1.00 80.43 ? 322 ASN B O 1 ATOM 2217 C CB . ASN A 1 291 ? 61.333 -1.308 17.953 1.00 83.04 ? 322 ASN B CB 1 ATOM 2218 C CG . ASN A 1 291 ? 62.390 -0.469 17.236 1.00 84.13 ? 322 ASN B CG 1 ATOM 2219 O OD1 . ASN A 1 291 ? 62.209 -0.104 16.072 1.00 85.68 ? 322 ASN B OD1 1 ATOM 2220 N ND2 . ASN A 1 291 ? 63.493 -0.159 17.926 1.00 83.42 ? 322 ASN B ND2 1 ATOM 2221 N N . LEU A 1 292 ? 58.532 -3.454 17.200 1.00 79.46 ? 323 LEU B N 1 ATOM 2222 C CA . LEU A 1 292 ? 58.015 -4.828 17.353 1.00 77.84 ? 323 LEU B CA 1 ATOM 2223 C C . LEU A 1 292 ? 58.100 -5.720 16.106 1.00 77.45 ? 323 LEU B C 1 ATOM 2224 O O . LEU A 1 292 ? 57.535 -5.398 15.070 1.00 78.98 ? 323 LEU B O 1 ATOM 2225 C CB . LEU A 1 292 ? 56.557 -4.765 17.797 1.00 78.63 ? 323 LEU B CB 1 ATOM 2226 C CG . LEU A 1 292 ? 55.895 -6.071 18.215 1.00 77.09 ? 323 LEU B CG 1 ATOM 2227 C CD1 . LEU A 1 292 ? 56.516 -6.582 19.490 1.00 75.25 ? 323 LEU B CD1 1 ATOM 2228 C CD2 . LEU A 1 292 ? 54.425 -5.842 18.420 1.00 78.36 ? 323 LEU B CD2 1 ATOM 2229 N N . THR A 1 293 ? 58.762 -6.866 16.220 1.00 76.52 ? 324 THR B N 1 ATOM 2230 C CA . THR A 1 293 ? 58.971 -7.749 15.066 1.00 76.10 ? 324 THR B CA 1 ATOM 2231 C C . THR A 1 293 ? 58.120 -9.011 15.177 1.00 75.15 ? 324 THR B C 1 ATOM 2232 O O . THR A 1 293 ? 57.353 -9.335 14.282 1.00 75.78 ? 324 THR B O 1 ATOM 2233 C CB . THR A 1 293 ? 60.457 -8.136 14.854 1.00 75.02 ? 324 THR B CB 1 ATOM 2234 O OG1 . THR A 1 293 ? 60.771 -9.304 15.618 1.00 73.21 ? 324 THR B OG1 1 ATOM 2235 C CG2 . THR A 1 293 ? 61.397 -6.993 15.243 1.00 75.64 ? 324 THR B CG2 1 ATOM 2236 N N . TRP A 1 294 ? 58.321 -9.753 16.259 1.00 77.11 ? 325 TRP B N 1 ATOM 2237 C CA . TRP A 1 294 ? 57.563 -10.966 16.555 1.00 76.30 ? 325 TRP B CA 1 ATOM 2238 C C . TRP A 1 294 ? 56.474 -10.706 17.592 1.00 76.70 ? 325 TRP B C 1 ATOM 2239 O O . TRP A 1 294 ? 56.765 -10.269 18.705 1.00 76.49 ? 325 TRP B O 1 ATOM 2240 C CB . TRP A 1 294 ? 58.528 -11.996 17.139 1.00 75.52 ? 325 TRP B CB 1 ATOM 2241 C CG . TRP A 1 294 ? 57.975 -13.369 17.367 1.00 75.67 ? 325 TRP B CG 1 ATOM 2242 C CD1 . TRP A 1 294 ? 56.952 -13.728 18.197 1.00 76.26 ? 325 TRP B CD1 1 ATOM 2243 C CD2 . TRP A 1 294 ? 58.460 -14.574 16.785 1.00 75.27 ? 325 TRP B CD2 1 ATOM 2244 N NE1 . TRP A 1 294 ? 56.756 -15.086 18.144 1.00 76.25 ? 325 TRP B NE1 1 ATOM 2245 C CE2 . TRP A 1 294 ? 57.674 -15.626 17.286 1.00 75.61 ? 325 TRP B CE2 1 ATOM 2246 C CE3 . TRP A 1 294 ? 59.478 -14.863 15.878 1.00 74.69 ? 325 TRP B CE3 1 ATOM 2247 C CZ2 . TRP A 1 294 ? 57.873 -16.934 16.914 1.00 75.34 ? 325 TRP B CZ2 1 ATOM 2248 C CZ3 . TRP A 1 294 ? 59.675 -16.149 15.514 1.00 74.45 ? 325 TRP B CZ3 1 ATOM 2249 C CH2 . TRP A 1 294 ? 58.878 -17.177 16.026 1.00 74.73 ? 325 TRP B CH2 1 ATOM 2250 N N . LEU A 1 295 ? 55.224 -10.990 17.255 1.00 71.93 ? 326 LEU B N 1 ATOM 2251 C CA . LEU A 1 295 ? 54.175 -10.943 18.266 1.00 72.14 ? 326 LEU B CA 1 ATOM 2252 C C . LEU A 1 295 ? 53.439 -12.281 18.402 1.00 71.01 ? 326 LEU B C 1 ATOM 2253 O O . LEU A 1 295 ? 52.666 -12.640 17.512 1.00 71.58 ? 326 LEU B O 1 ATOM 2254 C CB . LEU A 1 295 ? 53.182 -9.844 17.906 1.00 74.38 ? 326 LEU B CB 1 ATOM 2255 C CG . LEU A 1 295 ? 51.912 -9.782 18.745 1.00 75.00 ? 326 LEU B CG 1 ATOM 2256 C CD1 . LEU A 1 295 ? 52.254 -9.695 20.216 1.00 74.15 ? 326 LEU B CD1 1 ATOM 2257 C CD2 . LEU A 1 295 ? 51.064 -8.609 18.319 1.00 77.41 ? 326 LEU B CD2 1 ATOM 2258 N N . SER A 1 296 ? 53.626 -13.003 19.510 1.00 69.53 ? 327 SER B N 1 ATOM 2259 C CA . SER A 1 296 ? 52.956 -14.300 19.646 1.00 68.50 ? 327 SER B CA 1 ATOM 2260 C C . SER A 1 296 ? 52.143 -14.465 20.922 1.00 68.41 ? 327 SER B C 1 ATOM 2261 O O . SER A 1 296 ? 52.676 -14.578 22.014 1.00 67.72 ? 327 SER B O 1 ATOM 2262 C CB . SER A 1 296 ? 53.963 -15.441 19.515 1.00 66.86 ? 327 SER B CB 1 ATOM 2263 O OG . SER A 1 296 ? 53.439 -16.665 19.999 1.00 66.39 ? 327 SER B OG 1 ATOM 2264 N N . LEU A 1 297 ? 50.832 -14.483 20.751 1.00 71.80 ? 328 LEU B N 1 ATOM 2265 C CA . LEU A 1 297 ? 49.873 -14.679 21.835 1.00 72.65 ? 328 LEU B CA 1 ATOM 2266 C C . LEU A 1 297 ? 49.311 -16.097 21.963 1.00 73.22 ? 328 LEU B C 1 ATOM 2267 O O . LEU A 1 297 ? 48.306 -16.314 22.648 1.00 74.21 ? 328 LEU B O 1 ATOM 2268 C CB . LEU A 1 297 ? 48.761 -13.631 21.795 1.00 73.51 ? 328 LEU B CB 1 ATOM 2269 C CG . LEU A 1 297 ? 49.258 -12.254 22.234 1.00 72.85 ? 328 LEU B CG 1 ATOM 2270 C CD1 . LEU A 1 297 ? 48.117 -11.439 22.805 1.00 74.64 ? 328 LEU B CD1 1 ATOM 2271 C CD2 . LEU A 1 297 ? 50.390 -12.374 23.238 1.00 71.69 ? 328 LEU B CD2 1 ATOM 2272 N N . ILE A 1 298 ? 49.923 -17.034 21.248 1.00 74.90 ? 329 ILE B N 1 ATOM 2273 C CA . ILE A 1 298 ? 49.349 -18.349 20.999 1.00 75.43 ? 329 ILE B CA 1 ATOM 2274 C C . ILE A 1 298 ? 48.790 -19.025 22.237 1.00 76.14 ? 329 ILE B C 1 ATOM 2275 O O . ILE A 1 298 ? 49.407 -19.005 23.299 1.00 75.75 ? 329 ILE B O 1 ATOM 2276 C CB . ILE A 1 298 ? 50.453 -19.286 20.507 1.00 74.41 ? 329 ILE B CB 1 ATOM 2277 C CG1 . ILE A 1 298 ? 51.106 -18.749 19.246 1.00 73.75 ? 329 ILE B CG1 1 ATOM 2278 C CG2 . ILE A 1 298 ? 49.932 -20.681 20.276 1.00 74.90 ? 329 ILE B CG2 1 ATOM 2279 C CD1 . ILE A 1 298 ? 52.325 -19.533 18.872 1.00 72.75 ? 329 ILE B CD1 1 ATOM 2280 N N . SER A 1 299 ? 47.613 -19.623 22.090 1.00 70.51 ? 330 SER B N 1 ATOM 2281 C CA . SER A 1 299 ? 47.110 -20.584 23.078 1.00 71.15 ? 330 SER B CA 1 ATOM 2282 C C . SER A 1 299 ? 46.926 -19.987 24.474 1.00 71.50 ? 330 SER B C 1 ATOM 2283 O O . SER A 1 299 ? 47.641 -20.323 25.413 1.00 70.94 ? 330 SER B O 1 ATOM 2284 C CB . SER A 1 299 ? 48.035 -21.814 23.141 1.00 70.35 ? 330 SER B CB 1 ATOM 2285 O OG . SER A 1 299 ? 47.469 -22.859 23.913 1.00 71.08 ? 330 SER B OG 1 ATOM 2286 N N . ASN A 1 300 ? 45.948 -19.101 24.586 1.00 74.83 ? 331 ASN B N 1 ATOM 2287 C CA . ASN A 1 300 ? 45.628 -18.429 25.830 1.00 75.22 ? 331 ASN B CA 1 ATOM 2288 C C . ASN A 1 300 ? 44.122 -18.366 25.952 1.00 76.81 ? 331 ASN B C 1 ATOM 2289 O O . ASN A 1 300 ? 43.412 -19.036 25.204 1.00 77.63 ? 331 ASN B O 1 ATOM 2290 C CB . ASN A 1 300 ? 46.196 -17.016 25.834 1.00 74.41 ? 331 ASN B CB 1 ATOM 2291 C CG . ASN A 1 300 ? 47.537 -16.932 26.525 1.00 73.15 ? 331 ASN B CG 1 ATOM 2292 O OD1 . ASN A 1 300 ? 47.648 -16.405 27.633 1.00 73.02 ? 331 ASN B OD1 1 ATOM 2293 N ND2 . ASN A 1 300 ? 48.566 -17.463 25.879 1.00 72.20 ? 331 ASN B ND2 1 ATOM 2294 N N . ASN A 1 301 ? 43.633 -17.601 26.918 1.00 97.69 ? 332 ASN B N 1 ATOM 2295 C CA . ASN A 1 301 ? 42.208 -17.350 27.023 1.00 99.06 ? 332 ASN B CA 1 ATOM 2296 C C . ASN A 1 301 ? 41.798 -16.051 26.350 1.00 99.08 ? 332 ASN B C 1 ATOM 2297 O O . ASN A 1 301 ? 40.662 -15.608 26.498 1.00 100.21 ? 332 ASN B O 1 ATOM 2298 C CB . ASN A 1 301 ? 41.738 -17.368 28.467 1.00 99.94 ? 332 ASN B CB 1 ATOM 2299 C CG . ASN A 1 301 ? 40.300 -17.806 28.588 1.00 102.26 ? 332 ASN B CG 1 ATOM 2300 O OD1 . ASN A 1 301 ? 39.867 -18.716 27.882 1.00 102.09 ? 332 ASN B OD1 1 ATOM 2301 N ND2 . ASN A 1 301 ? 39.542 -17.152 29.466 1.00 104.51 ? 332 ASN B ND2 1 ATOM 2302 N N . LEU A 1 302 ? 42.733 -15.442 25.626 1.00 83.71 ? 333 LEU B N 1 ATOM 2303 C CA . LEU A 1 302 ? 42.590 -14.066 25.129 1.00 83.57 ? 333 LEU B CA 1 ATOM 2304 C C . LEU A 1 302 ? 41.291 -13.742 24.370 1.00 84.90 ? 333 LEU B C 1 ATOM 2305 O O . LEU A 1 302 ? 40.754 -14.585 23.665 1.00 85.60 ? 333 LEU B O 1 ATOM 2306 C CB . LEU A 1 302 ? 43.801 -13.696 24.269 1.00 82.14 ? 333 LEU B CB 1 ATOM 2307 C CG . LEU A 1 302 ? 44.917 -12.880 24.932 1.00 81.02 ? 333 LEU B CG 1 ATOM 2308 C CD1 . LEU A 1 302 ? 44.548 -12.503 26.359 1.00 81.30 ? 333 LEU B CD1 1 ATOM 2309 C CD2 . LEU A 1 302 ? 46.247 -13.622 24.886 1.00 79.93 ? 333 LEU B CD2 1 ATOM 2310 N N . SER A 1 303 ? 40.789 -12.518 24.541 1.00 84.36 ? 334 SER B N 1 ATOM 2311 C CA . SER A 1 303 ? 39.505 -12.104 23.965 1.00 85.66 ? 334 SER B CA 1 ATOM 2312 C C . SER A 1 303 ? 39.462 -10.719 23.284 1.00 85.93 ? 334 SER B C 1 ATOM 2313 O O . SER A 1 303 ? 40.478 -10.042 23.115 1.00 85.37 ? 334 SER B O 1 ATOM 2314 C CB . SER A 1 303 ? 38.418 -12.160 25.033 1.00 86.77 ? 334 SER B CB 1 ATOM 2315 O OG . SER A 1 303 ? 37.258 -11.493 24.578 1.00 87.75 ? 334 SER B OG 1 ATOM 2316 N N . GLY A 1 304 ? 38.265 -10.316 22.874 1.00 94.86 ? 335 GLY B N 1 ATOM 2317 C CA . GLY A 1 304 ? 38.063 -8.999 22.302 1.00 96.43 ? 335 GLY B CA 1 ATOM 2318 C C . GLY A 1 304 ? 38.686 -8.845 20.929 1.00 95.98 ? 335 GLY B C 1 ATOM 2319 O O . GLY A 1 304 ? 39.399 -9.732 20.466 1.00 94.26 ? 335 GLY B O 1 ATOM 2320 N N . GLU A 1 305 ? 38.423 -7.711 20.282 1.00 103.74 ? 336 GLU B N 1 ATOM 2321 C CA . GLU A 1 305 ? 38.961 -7.433 18.952 1.00 103.86 ? 336 GLU B CA 1 ATOM 2322 C C . GLU A 1 305 ? 40.474 -7.253 18.971 1.00 102.31 ? 336 GLU B C 1 ATOM 2323 O O . GLU A 1 305 ? 41.077 -7.062 20.028 1.00 101.52 ? 336 GLU B O 1 ATOM 2324 C CB . GLU A 1 305 ? 38.302 -6.195 18.336 1.00 106.80 ? 336 GLU B CB 1 ATOM 2325 C CG . GLU A 1 305 ? 36.841 -6.388 17.933 1.00 108.52 ? 336 GLU B CG 1 ATOM 2326 C CD . GLU A 1 305 ? 36.253 -5.209 17.136 1.00 111.52 ? 336 GLU B CD 1 ATOM 2327 O OE1 . GLU A 1 305 ? 35.305 -5.448 16.359 1.00 112.70 ? 336 GLU B OE1 1 ATOM 2328 O OE2 . GLU A 1 305 ? 36.719 -4.052 17.286 1.00 112.79 ? 336 GLU B OE2 1 ATOM 2329 N N . VAL A 1 306 ? 41.087 -7.356 17.799 1.00 90.35 ? 337 VAL B N 1 ATOM 2330 C CA . VAL A 1 306 ? 42.512 -7.087 17.654 1.00 89.21 ? 337 VAL B CA 1 ATOM 2331 C C . VAL A 1 306 ? 42.670 -5.650 17.225 1.00 91.42 ? 337 VAL B C 1 ATOM 2332 O O . VAL A 1 306 ? 42.022 -5.226 16.273 1.00 93.27 ? 337 VAL B O 1 ATOM 2333 C CB . VAL A 1 306 ? 43.138 -7.971 16.574 1.00 87.72 ? 337 VAL B CB 1 ATOM 2334 C CG1 . VAL A 1 306 ? 44.489 -7.423 16.155 1.00 87.33 ? 337 VAL B CG1 1 ATOM 2335 C CG2 . VAL A 1 306 ? 43.260 -9.394 17.071 1.00 85.69 ? 337 VAL B CG2 1 ATOM 2336 N N . PRO A 1 307 ? 43.527 -4.893 17.922 1.00 90.19 ? 338 PRO B N 1 ATOM 2337 C CA . PRO A 1 307 ? 43.636 -3.448 17.685 1.00 92.44 ? 338 PRO B CA 1 ATOM 2338 C C . PRO A 1 307 ? 43.936 -3.103 16.224 1.00 93.42 ? 338 PRO B C 1 ATOM 2339 O O . PRO A 1 307 ? 44.911 -3.609 15.671 1.00 91.87 ? 338 PRO B O 1 ATOM 2340 C CB . PRO A 1 307 ? 44.805 -3.048 18.584 1.00 91.34 ? 338 PRO B CB 1 ATOM 2341 C CG . PRO A 1 307 ? 44.779 -4.055 19.686 1.00 89.31 ? 338 PRO B CG 1 ATOM 2342 C CD . PRO A 1 307 ? 44.381 -5.341 19.033 1.00 88.07 ? 338 PRO B CD 1 ATOM 2343 N N . GLU A 1 308 ? 43.120 -2.228 15.631 1.00 115.64 ? 339 GLU B N 1 ATOM 2344 C CA . GLU A 1 308 ? 43.230 -1.866 14.215 1.00 116.96 ? 339 GLU B CA 1 ATOM 2345 C C . GLU A 1 308 ? 44.631 -1.343 13.954 1.00 116.47 ? 339 GLU B C 1 ATOM 2346 O O . GLU A 1 308 ? 45.176 -1.466 12.855 1.00 116.44 ? 339 GLU B O 1 ATOM 2347 C CB . GLU A 1 308 ? 42.190 -0.796 13.863 1.00 120.20 ? 339 GLU B CB 1 ATOM 2348 C CG . GLU A 1 308 ? 42.107 -0.402 12.389 1.00 121.97 ? 339 GLU B CG 1 ATOM 2349 C CD . GLU A 1 308 ? 41.385 0.932 12.188 1.00 125.36 ? 339 GLU B CD 1 ATOM 2350 O OE1 . GLU A 1 308 ? 40.878 1.194 11.072 1.00 127.24 ? 339 GLU B OE1 1 ATOM 2351 O OE2 . GLU A 1 308 ? 41.331 1.725 13.156 1.00 126.21 ? 339 GLU B OE2 1 ATOM 2352 N N . GLY A 1 309 ? 45.223 -0.795 15.006 1.00 102.51 ? 340 GLY B N 1 ATOM 2353 C CA . GLY A 1 309 ? 46.515 -0.152 14.924 1.00 102.28 ? 340 GLY B CA 1 ATOM 2354 C C . GLY A 1 309 ? 47.663 -1.065 14.571 1.00 99.82 ? 340 GLY B C 1 ATOM 2355 O O . GLY A 1 309 ? 48.754 -0.603 14.248 1.00 99.73 ? 340 GLY B O 1 ATOM 2356 N N . ILE A 1 310 ? 47.439 -2.368 14.624 1.00 91.92 ? 341 ILE B N 1 ATOM 2357 C CA . ILE A 1 310 ? 48.528 -3.280 14.299 1.00 89.65 ? 341 ILE B CA 1 ATOM 2358 C C . ILE A 1 310 ? 48.696 -3.327 12.783 1.00 90.48 ? 341 ILE B C 1 ATOM 2359 O O . ILE A 1 310 ? 49.656 -3.920 12.269 1.00 89.08 ? 341 ILE B O 1 ATOM 2360 C CB . ILE A 1 310 ? 48.323 -4.687 14.903 1.00 87.29 ? 341 ILE B CB 1 ATOM 2361 C CG1 . ILE A 1 310 ? 47.860 -4.572 16.356 1.00 87.02 ? 341 ILE B CG1 1 ATOM 2362 C CG2 . ILE A 1 310 ? 49.609 -5.487 14.844 1.00 84.98 ? 341 ILE B CG2 1 ATOM 2363 C CD1 . ILE A 1 310 ? 47.541 -5.886 17.003 1.00 85.01 ? 341 ILE B CD1 1 ATOM 2364 N N . GLY A 1 311 ? 47.765 -2.670 12.081 1.00 110.47 ? 342 GLY B N 1 ATOM 2365 C CA . GLY A 1 311 ? 47.779 -2.604 10.628 1.00 111.68 ? 342 GLY B CA 1 ATOM 2366 C C . GLY A 1 311 ? 49.128 -2.182 10.082 1.00 111.60 ? 342 GLY B C 1 ATOM 2367 O O . GLY A 1 311 ? 49.686 -2.860 9.213 1.00 110.76 ? 342 GLY B O 1 ATOM 2368 N N . GLU A 1 312 ? 49.657 -1.067 10.586 1.00 114.99 ? 343 GLU B N 1 ATOM 2369 C CA . GLU A 1 312 ? 51.031 -0.702 10.272 1.00 114.69 ? 343 GLU B CA 1 ATOM 2370 C C . GLU A 1 312 ? 51.920 -0.575 11.500 1.00 113.11 ? 343 GLU B C 1 ATOM 2371 O O . GLU A 1 312 ? 51.858 0.393 12.245 1.00 114.15 ? 343 GLU B O 1 ATOM 2372 C CB . GLU A 1 312 ? 51.086 0.594 9.454 1.00 117.54 ? 343 GLU B CB 1 ATOM 2373 C CG . GLU A 1 312 ? 50.224 1.726 9.992 1.00 119.77 ? 343 GLU B CG 1 ATOM 2374 C CD . GLU A 1 312 ? 48.772 1.627 9.550 1.00 121.34 ? 343 GLU B CD 1 ATOM 2375 O OE1 . GLU A 1 312 ? 47.878 1.663 10.426 1.00 121.50 ? 343 GLU B OE1 1 ATOM 2376 O OE2 . GLU A 1 312 ? 48.526 1.520 8.328 1.00 122.49 ? 343 GLU B OE2 1 ATOM 2377 N N . LEU A 1 313 ? 52.767 -1.575 11.674 1.00 97.59 ? 344 LEU B N 1 ATOM 2378 C CA . LEU A 1 313 ? 53.954 -1.465 12.486 1.00 96.15 ? 344 LEU B CA 1 ATOM 2379 C C . LEU A 1 313 ? 54.990 -1.727 11.441 1.00 95.86 ? 344 LEU B C 1 ATOM 2380 O O . LEU A 1 313 ? 55.035 -2.826 10.891 1.00 94.64 ? 344 LEU B O 1 ATOM 2381 C CB . LEU A 1 313 ? 54.040 -2.573 13.529 1.00 93.55 ? 344 LEU B CB 1 ATOM 2382 C CG . LEU A 1 313 ? 52.823 -2.953 14.365 1.00 93.31 ? 344 LEU B CG 1 ATOM 2383 C CD1 . LEU A 1 313 ? 53.285 -3.735 15.575 1.00 90.93 ? 344 LEU B CD1 1 ATOM 2384 C CD2 . LEU A 1 313 ? 52.044 -1.727 14.784 1.00 95.53 ? 344 LEU B CD2 1 ATOM 2385 N N . PRO A 1 314 ? 55.821 -0.730 11.149 1.00 119.03 ? 345 PRO B N 1 ATOM 2386 C CA . PRO A 1 314 ? 56.787 -0.801 10.051 1.00 119.27 ? 345 PRO B CA 1 ATOM 2387 C C . PRO A 1 314 ? 57.602 -2.094 10.081 1.00 116.73 ? 345 PRO B C 1 ATOM 2388 O O . PRO A 1 314 ? 58.006 -2.597 9.031 1.00 116.76 ? 345 PRO B O 1 ATOM 2389 C CB . PRO A 1 314 ? 57.699 0.393 10.325 1.00 120.28 ? 345 PRO B CB 1 ATOM 2390 C CG . PRO A 1 314 ? 56.858 1.337 11.113 1.00 121.63 ? 345 PRO B CG 1 ATOM 2391 C CD . PRO A 1 314 ? 55.979 0.486 11.958 1.00 120.12 ? 345 PRO B CD 1 ATOM 2392 N N . GLU A 1 315 ? 57.843 -2.608 11.283 1.00 111.72 ? 346 GLU B N 1 ATOM 2393 C CA . GLU A 1 315 ? 58.705 -3.768 11.469 1.00 109.35 ? 346 GLU B CA 1 ATOM 2394 C C . GLU A 1 315 ? 58.053 -5.145 11.672 1.00 107.61 ? 346 GLU B C 1 ATOM 2395 O O . GLU A 1 315 ? 58.772 -6.140 11.787 1.00 105.75 ? 346 GLU B O 1 ATOM 2396 C CB . GLU A 1 315 ? 59.687 -3.488 12.604 1.00 108.20 ? 346 GLU B CB 1 ATOM 2397 C CG . GLU A 1 315 ? 61.021 -2.942 12.129 1.00 108.67 ? 346 GLU B CG 1 ATOM 2398 C CD . GLU A 1 315 ? 60.878 -1.932 11.000 1.00 111.25 ? 346 GLU B CD 1 ATOM 2399 O OE1 . GLU A 1 315 ? 60.527 -0.765 11.285 1.00 112.90 ? 346 GLU B OE1 1 ATOM 2400 O OE2 . GLU A 1 315 ? 61.121 -2.303 9.829 1.00 111.73 ? 346 GLU B OE2 1 ATOM 2401 N N . LEU A 1 316 ? 56.721 -5.215 11.720 1.00 86.58 ? 347 LEU B N 1 ATOM 2402 C CA . LEU A 1 316 ? 56.041 -6.478 12.074 1.00 84.95 ? 347 LEU B CA 1 ATOM 2403 C C . LEU A 1 316 ? 56.304 -7.605 11.080 1.00 84.08 ? 347 LEU B C 1 ATOM 2404 O O . LEU A 1 316 ? 56.164 -7.426 9.872 1.00 85.44 ? 347 LEU B O 1 ATOM 2405 C CB . LEU A 1 316 ? 54.529 -6.297 12.262 1.00 86.04 ? 347 LEU B CB 1 ATOM 2406 C CG . LEU A 1 316 ? 53.762 -7.572 12.637 1.00 84.51 ? 347 LEU B CG 1 ATOM 2407 C CD1 . LEU A 1 316 ? 54.404 -8.242 13.807 1.00 82.33 ? 347 LEU B CD1 1 ATOM 2408 C CD2 . LEU A 1 316 ? 52.326 -7.272 12.980 1.00 85.69 ? 347 LEU B CD2 1 ATOM 2409 N N . THR A 1 317 ? 56.678 -8.766 11.606 1.00 92.77 ? 348 THR B N 1 ATOM 2410 C CA . THR A 1 317 ? 57.108 -9.886 10.785 1.00 91.77 ? 348 THR B CA 1 ATOM 2411 C C . THR A 1 317 ? 56.337 -11.146 11.125 1.00 90.38 ? 348 THR B C 1 ATOM 2412 O O . THR A 1 317 ? 55.649 -11.693 10.285 1.00 90.71 ? 348 THR B O 1 ATOM 2413 C CB . THR A 1 317 ? 58.624 -10.115 10.903 1.00 90.63 ? 348 THR B CB 1 ATOM 2414 O OG1 . THR A 1 317 ? 59.300 -9.246 9.984 1.00 92.20 ? 348 THR B OG1 1 ATOM 2415 C CG2 . THR A 1 317 ? 58.990 -11.550 10.587 1.00 89.04 ? 348 THR B CG2 1 ATOM 2416 N N . THR A 1 318 ? 56.457 -11.614 12.356 1.00 73.68 ? 349 THR B N 1 ATOM 2417 C CA . THR A 1 318 ? 55.784 -12.836 12.764 1.00 72.30 ? 349 THR B CA 1 ATOM 2418 C C . THR A 1 318 ? 54.601 -12.522 13.666 1.00 72.73 ? 349 THR B C 1 ATOM 2419 O O . THR A 1 318 ? 54.782 -11.994 14.768 1.00 72.52 ? 349 THR B O 1 ATOM 2420 C CB . THR A 1 318 ? 56.756 -13.759 13.522 1.00 70.20 ? 349 THR B CB 1 ATOM 2421 O OG1 . THR A 1 318 ? 57.739 -14.266 12.615 1.00 69.80 ? 349 THR B OG1 1 ATOM 2422 C CG2 . THR A 1 318 ? 56.025 -14.926 14.152 1.00 68.87 ? 349 THR B CG2 1 ATOM 2423 N N . LEU A 1 319 ? 53.392 -12.824 13.198 1.00 73.42 ? 350 LEU B N 1 ATOM 2424 C CA . LEU A 1 319 ? 52.191 -12.634 14.012 1.00 73.91 ? 350 LEU B CA 1 ATOM 2425 C C . LEU A 1 319 ? 51.414 -13.923 14.335 1.00 72.69 ? 350 LEU B C 1 ATOM 2426 O O . LEU A 1 319 ? 50.741 -14.472 13.469 1.00 73.02 ? 350 LEU B O 1 ATOM 2427 C CB . LEU A 1 319 ? 51.261 -11.663 13.308 1.00 76.21 ? 350 LEU B CB 1 ATOM 2428 C CG . LEU A 1 319 ? 49.954 -11.494 14.057 1.00 76.91 ? 350 LEU B CG 1 ATOM 2429 C CD1 . LEU A 1 319 ? 50.179 -10.633 15.275 1.00 77.13 ? 350 LEU B CD1 1 ATOM 2430 C CD2 . LEU A 1 319 ? 48.917 -10.902 13.142 1.00 79.06 ? 350 LEU B CD2 1 ATOM 2431 N N . PHE A 1 320 ? 51.473 -14.392 15.580 1.00 71.91 ? 351 PHE B N 1 ATOM 2432 C CA . PHE A 1 320 ? 50.736 -15.595 15.958 1.00 72.30 ? 351 PHE B CA 1 ATOM 2433 C C . PHE A 1 320 ? 49.670 -15.259 16.979 1.00 73.19 ? 351 PHE B C 1 ATOM 2434 O O . PHE A 1 320 ? 49.975 -15.001 18.134 1.00 73.06 ? 351 PHE B O 1 ATOM 2435 C CB . PHE A 1 320 ? 51.665 -16.619 16.597 1.00 71.48 ? 351 PHE B CB 1 ATOM 2436 C CG . PHE A 1 320 ? 52.733 -17.153 15.685 1.00 70.73 ? 351 PHE B CG 1 ATOM 2437 C CD1 . PHE A 1 320 ? 52.718 -16.897 14.337 1.00 70.78 ? 351 PHE B CD1 1 ATOM 2438 C CD2 . PHE A 1 320 ? 53.755 -17.943 16.197 1.00 70.07 ? 351 PHE B CD2 1 ATOM 2439 C CE1 . PHE A 1 320 ? 53.706 -17.406 13.523 1.00 70.17 ? 351 PHE B CE1 1 ATOM 2440 C CE2 . PHE A 1 320 ? 54.747 -18.460 15.389 1.00 69.43 ? 351 PHE B CE2 1 ATOM 2441 C CZ . PHE A 1 320 ? 54.727 -18.188 14.056 1.00 69.47 ? 351 PHE B CZ 1 ATOM 2442 N N . LEU A 1 321 ? 48.420 -15.234 16.550 1.00 72.19 ? 352 LEU B N 1 ATOM 2443 C CA . LEU A 1 321 ? 47.289 -15.077 17.459 1.00 72.88 ? 352 LEU B CA 1 ATOM 2444 C C . LEU A 1 321 ? 46.489 -16.346 17.726 1.00 72.50 ? 352 LEU B C 1 ATOM 2445 O O . LEU A 1 321 ? 45.443 -16.281 18.372 1.00 73.38 ? 352 LEU B O 1 ATOM 2446 C CB . LEU A 1 321 ? 46.371 -13.966 16.975 1.00 75.21 ? 352 LEU B CB 1 ATOM 2447 C CG . LEU A 1 321 ? 47.109 -12.647 16.801 1.00 76.29 ? 352 LEU B CG 1 ATOM 2448 C CD1 . LEU A 1 321 ? 46.132 -11.565 16.396 1.00 78.74 ? 352 LEU B CD1 1 ATOM 2449 C CD2 . LEU A 1 321 ? 47.844 -12.313 18.096 1.00 75.49 ? 352 LEU B CD2 1 ATOM 2450 N N . TRP A 1 322 ? 46.933 -17.478 17.180 1.00 72.05 ? 353 TRP B N 1 ATOM 2451 C CA . TRP A 1 322 ? 46.088 -18.678 17.133 1.00 72.08 ? 353 TRP B CA 1 ATOM 2452 C C . TRP A 1 322 ? 45.729 -19.295 18.487 1.00 71.87 ? 353 TRP B C 1 ATOM 2453 O O . TRP A 1 322 ? 46.449 -19.119 19.478 1.00 71.21 ? 353 TRP B O 1 ATOM 2454 C CB . TRP A 1 322 ? 46.612 -19.736 16.137 1.00 71.17 ? 353 TRP B CB 1 ATOM 2455 C CG . TRP A 1 322 ? 48.059 -20.193 16.276 1.00 69.64 ? 353 TRP B CG 1 ATOM 2456 C CD1 . TRP A 1 322 ? 49.177 -19.511 15.889 1.00 69.21 ? 353 TRP B CD1 1 ATOM 2457 C CD2 . TRP A 1 322 ? 48.526 -21.456 16.775 1.00 68.78 ? 353 TRP B CD2 1 ATOM 2458 N NE1 . TRP A 1 322 ? 50.310 -20.258 16.137 1.00 67.86 ? 353 TRP B NE1 1 ATOM 2459 C CE2 . TRP A 1 322 ? 49.934 -21.453 16.682 1.00 67.53 ? 353 TRP B CE2 1 ATOM 2460 C CE3 . TRP A 1 322 ? 47.894 -22.575 17.312 1.00 69.23 ? 353 TRP B CE3 1 ATOM 2461 C CZ2 . TRP A 1 322 ? 50.706 -22.516 17.105 1.00 66.71 ? 353 TRP B CZ2 1 ATOM 2462 C CZ3 . TRP A 1 322 ? 48.667 -23.627 17.730 1.00 68.38 ? 353 TRP B CZ3 1 ATOM 2463 C CH2 . TRP A 1 322 ? 50.054 -23.593 17.625 1.00 67.11 ? 353 TRP B CH2 1 ATOM 2464 N N . ASN A 1 323 ? 44.600 -20.007 18.506 1.00 81.31 ? 354 ASN B N 1 ATOM 2465 C CA . ASN A 1 323 ? 44.040 -20.646 19.711 1.00 82.24 ? 354 ASN B CA 1 ATOM 2466 C C . ASN A 1 323 ? 43.581 -19.752 20.888 1.00 82.93 ? 354 ASN B C 1 ATOM 2467 O O . ASN A 1 323 ? 43.933 -19.992 22.055 1.00 82.96 ? 354 ASN B O 1 ATOM 2468 C CB . ASN A 1 323 ? 44.941 -21.786 20.204 1.00 81.41 ? 354 ASN B CB 1 ATOM 2469 C CG . ASN A 1 323 ? 44.867 -22.998 19.310 1.00 81.58 ? 354 ASN B CG 1 ATOM 2470 O OD1 . ASN A 1 323 ? 44.677 -22.866 18.101 1.00 81.86 ? 354 ASN B OD1 1 ATOM 2471 N ND2 . ASN A 1 323 ? 44.992 -24.187 19.895 1.00 81.40 ? 354 ASN B ND2 1 ATOM 2472 N N . ASN A 1 324 ? 42.781 -18.742 20.560 1.00 79.38 ? 355 ASN B N 1 ATOM 2473 C CA . ASN A 1 324 ? 42.072 -17.949 21.545 1.00 80.27 ? 355 ASN B CA 1 ATOM 2474 C C . ASN A 1 324 ? 40.626 -17.838 21.070 1.00 81.72 ? 355 ASN B C 1 ATOM 2475 O O . ASN A 1 324 ? 40.232 -18.543 20.140 1.00 82.01 ? 355 ASN B O 1 ATOM 2476 C CB . ASN A 1 324 ? 42.714 -16.571 21.687 1.00 79.44 ? 355 ASN B CB 1 ATOM 2477 C CG . ASN A 1 324 ? 44.137 -16.639 22.227 1.00 77.94 ? 355 ASN B CG 1 ATOM 2478 O OD1 . ASN A 1 324 ? 44.491 -17.552 22.960 1.00 77.80 ? 355 ASN B OD1 1 ATOM 2479 N ND2 . ASN A 1 324 ? 44.956 -15.662 21.863 1.00 76.86 ? 355 ASN B ND2 1 ATOM 2480 N N . ASN A 1 325 ? 39.818 -17.016 21.736 1.00 78.43 ? 356 ASN B N 1 ATOM 2481 C CA . ASN A 1 325 ? 38.536 -16.609 21.177 1.00 80.14 ? 356 ASN B CA 1 ATOM 2482 C C . ASN A 1 325 ? 38.640 -15.116 20.925 1.00 80.94 ? 356 ASN B C 1 ATOM 2483 O O . ASN A 1 325 ? 38.527 -14.327 21.850 1.00 81.51 ? 356 ASN B O 1 ATOM 2484 C CB . ASN A 1 325 ? 37.406 -16.895 22.176 1.00 81.33 ? 356 ASN B CB 1 ATOM 2485 C CG . ASN A 1 325 ? 36.195 -17.560 21.529 1.00 82.19 ? 356 ASN B CG 1 ATOM 2486 O OD1 . ASN A 1 325 ? 35.813 -17.213 20.417 1.00 82.67 ? 356 ASN B OD1 1 ATOM 2487 N ND2 . ASN A 1 325 ? 35.591 -18.528 22.224 1.00 82.42 ? 356 ASN B ND2 1 ATOM 2488 N N . PHE A 1 326 ? 38.805 -14.720 19.669 1.00 95.73 ? 357 PHE B N 1 ATOM 2489 C CA . PHE A 1 326 ? 39.005 -13.311 19.318 1.00 95.22 ? 357 PHE B CA 1 ATOM 2490 C C . PHE A 1 326 ? 37.846 -12.902 18.424 1.00 96.14 ? 357 PHE B C 1 ATOM 2491 O O . PHE A 1 326 ? 37.197 -13.758 17.845 1.00 96.53 ? 357 PHE B O 1 ATOM 2492 C CB . PHE A 1 326 ? 40.312 -13.132 18.542 1.00 93.89 ? 357 PHE B CB 1 ATOM 2493 C CG . PHE A 1 326 ? 41.525 -12.888 19.403 1.00 92.47 ? 357 PHE B CG 1 ATOM 2494 C CD1 . PHE A 1 326 ? 41.440 -12.149 20.564 1.00 91.92 ? 357 PHE B CD1 1 ATOM 2495 C CD2 . PHE A 1 326 ? 42.765 -13.381 19.023 1.00 91.67 ? 357 PHE B CD2 1 ATOM 2496 C CE1 . PHE A 1 326 ? 42.568 -11.920 21.336 1.00 90.67 ? 357 PHE B CE1 1 ATOM 2497 C CE2 . PHE A 1 326 ? 43.888 -13.157 19.789 1.00 90.41 ? 357 PHE B CE2 1 ATOM 2498 C CZ . PHE A 1 326 ? 43.790 -12.426 20.943 1.00 89.88 ? 357 PHE B CZ 1 ATOM 2499 N N . THR A 1 327 ? 37.569 -11.614 18.291 1.00 95.30 ? 358 THR B N 1 ATOM 2500 C CA . THR A 1 327 ? 36.464 -11.234 17.423 1.00 96.93 ? 358 THR B CA 1 ATOM 2501 C C . THR A 1 327 ? 36.777 -10.047 16.517 1.00 98.01 ? 358 THR B C 1 ATOM 2502 O O . THR A 1 327 ? 37.743 -9.321 16.740 1.00 97.59 ? 358 THR B O 1 ATOM 2503 C CB . THR A 1 327 ? 35.195 -10.974 18.236 1.00 98.76 ? 358 THR B CB 1 ATOM 2504 O OG1 . THR A 1 327 ? 35.377 -11.483 19.563 1.00 98.47 ? 358 THR B OG1 1 ATOM 2505 C CG2 . THR A 1 327 ? 34.004 -11.667 17.585 1.00 99.60 ? 358 THR B CG2 1 ATOM 2506 N N . GLY A 1 328 ? 35.966 -9.869 15.478 1.00 111.53 ? 359 GLY B N 1 ATOM 2507 C CA . GLY A 1 328 ? 36.092 -8.716 14.603 1.00 113.24 ? 359 GLY B CA 1 ATOM 2508 C C . GLY A 1 328 ? 36.995 -8.930 13.406 1.00 112.37 ? 359 GLY B C 1 ATOM 2509 O O . GLY A 1 328 ? 37.548 -10.013 13.215 1.00 110.23 ? 359 GLY B O 1 ATOM 2510 N N . VAL A 1 329 ? 37.138 -7.887 12.593 1.00 99.83 ? 360 VAL B N 1 ATOM 2511 C CA . VAL A 1 329 ? 37.984 -7.948 11.411 1.00 99.40 ? 360 VAL B CA 1 ATOM 2512 C C . VAL A 1 329 ? 39.434 -8.071 11.828 1.00 97.34 ? 360 VAL B C 1 ATOM 2513 O O . VAL A 1 329 ? 39.814 -7.673 12.933 1.00 96.91 ? 360 VAL B O 1 ATOM 2514 C CB . VAL A 1 329 ? 37.874 -6.667 10.555 1.00 102.13 ? 360 VAL B CB 1 ATOM 2515 C CG1 . VAL A 1 329 ? 37.792 -7.015 9.068 1.00 102.62 ? 360 VAL B CG1 1 ATOM 2516 C CG2 . VAL A 1 329 ? 36.685 -5.823 10.991 1.00 104.68 ? 360 VAL B CG2 1 ATOM 2517 N N . LEU A 1 330 ? 40.251 -8.628 10.945 1.00 103.29 ? 361 LEU B N 1 ATOM 2518 C CA . LEU A 1 330 ? 41.682 -8.469 11.092 1.00 101.96 ? 361 LEU B CA 1 ATOM 2519 C C . LEU A 1 330 ? 41.931 -7.012 10.767 1.00 104.20 ? 361 LEU B C 1 ATOM 2520 O O . LEU A 1 330 ? 41.158 -6.411 10.017 1.00 106.48 ? 361 LEU B O 1 ATOM 2521 C CB . LEU A 1 330 ? 42.445 -9.370 10.122 1.00 100.45 ? 361 LEU B CB 1 ATOM 2522 C CG . LEU A 1 330 ? 42.494 -10.863 10.455 1.00 97.98 ? 361 LEU B CG 1 ATOM 2523 C CD1 . LEU A 1 330 ? 43.567 -11.566 9.645 1.00 96.51 ? 361 LEU B CD1 1 ATOM 2524 C CD2 . LEU A 1 330 ? 42.724 -11.082 11.933 1.00 96.62 ? 361 LEU B CD2 1 ATOM 2525 N N . PRO A 1 331 ? 42.988 -6.431 11.345 1.00 97.70 ? 362 PRO B N 1 ATOM 2526 C CA . PRO A 1 331 ? 43.372 -5.061 11.006 1.00 99.72 ? 362 PRO B CA 1 ATOM 2527 C C . PRO A 1 331 ? 43.505 -4.989 9.501 1.00 100.80 ? 362 PRO B C 1 ATOM 2528 O O . PRO A 1 331 ? 44.200 -5.807 8.913 1.00 99.25 ? 362 PRO B O 1 ATOM 2529 C CB . PRO A 1 331 ? 44.745 -4.931 11.644 1.00 98.10 ? 362 PRO B CB 1 ATOM 2530 C CG . PRO A 1 331 ? 44.697 -5.861 12.790 1.00 95.93 ? 362 PRO B CG 1 ATOM 2531 C CD . PRO A 1 331 ? 43.865 -7.017 12.366 1.00 95.24 ? 362 PRO B CD 1 ATOM 2532 N N . HIS A 1 332 ? 42.839 -4.037 8.872 1.00 97.95 ? 363 HIS B N 1 ATOM 2533 C CA . HIS A 1 332 ? 42.638 -4.178 7.449 1.00 99.05 ? 363 HIS B CA 1 ATOM 2534 C C . HIS A 1 332 ? 43.845 -3.789 6.602 1.00 99.23 ? 363 HIS B C 1 ATOM 2535 O O . HIS A 1 332 ? 44.016 -4.314 5.508 1.00 99.15 ? 363 HIS B O 1 ATOM 2536 C CB . HIS A 1 332 ? 41.359 -3.487 7.000 1.00 101.92 ? 363 HIS B CB 1 ATOM 2537 C CG . HIS A 1 332 ? 41.376 -2.008 7.184 1.00 104.35 ? 363 HIS B CG 1 ATOM 2538 N ND1 . HIS A 1 332 ? 41.973 -1.156 6.280 1.00 106.02 ? 363 HIS B ND1 1 ATOM 2539 C CD2 . HIS A 1 332 ? 40.860 -1.225 8.161 1.00 105.52 ? 363 HIS B CD2 1 ATOM 2540 C CE1 . HIS A 1 332 ? 41.820 0.090 6.690 1.00 108.10 ? 363 HIS B CE1 1 ATOM 2541 N NE2 . HIS A 1 332 ? 41.148 0.076 7.830 1.00 107.85 ? 363 HIS B NE2 1 ATOM 2542 N N . LYS A 1 333 ? 44.705 -2.913 7.102 1.00 111.63 ? 364 LYS B N 1 ATOM 2543 C CA . LYS A 1 333 ? 45.888 -2.555 6.321 1.00 111.82 ? 364 LYS B CA 1 ATOM 2544 C C . LYS A 1 333 ? 47.050 -3.509 6.606 1.00 108.92 ? 364 LYS B C 1 ATOM 2545 O O . LYS A 1 333 ? 48.185 -3.253 6.216 1.00 108.73 ? 364 LYS B O 1 ATOM 2546 C CB . LYS A 1 333 ? 46.290 -1.080 6.463 1.00 113.87 ? 364 LYS B CB 1 ATOM 2547 C CG . LYS A 1 333 ? 46.881 -0.488 5.168 1.00 115.62 ? 364 LYS B CG 1 ATOM 2548 C CD . LYS A 1 333 ? 47.385 0.943 5.353 1.00 117.55 ? 364 LYS B CD 1 ATOM 2549 C CE . LYS A 1 333 ? 48.096 1.473 4.105 1.00 119.17 ? 364 LYS B CE 1 ATOM 2550 N NZ . LYS A 1 333 ? 48.624 2.864 4.309 1.00 121.04 ? 364 LYS B NZ 1 ATOM 2551 N N . LEU A 1 334 ? 46.754 -4.591 7.322 1.00 104.54 ? 365 LEU B N 1 ATOM 2552 C CA . LEU A 1 334 ? 47.742 -5.613 7.683 1.00 101.76 ? 365 LEU B CA 1 ATOM 2553 C C . LEU A 1 334 ? 48.564 -6.100 6.486 1.00 101.39 ? 365 LEU B C 1 ATOM 2554 O O . LEU A 1 334 ? 48.022 -6.353 5.412 1.00 102.41 ? 365 LEU B O 1 ATOM 2555 C CB . LEU A 1 334 ? 47.022 -6.811 8.315 1.00 99.97 ? 365 LEU B CB 1 ATOM 2556 C CG . LEU A 1 334 ? 47.671 -7.681 9.398 1.00 97.24 ? 365 LEU B CG 1 ATOM 2557 C CD1 . LEU A 1 334 ? 46.623 -8.553 10.074 1.00 96.33 ? 365 LEU B CD1 1 ATOM 2558 C CD2 . LEU A 1 334 ? 48.782 -8.550 8.844 1.00 95.52 ? 365 LEU B CD2 1 ATOM 2559 N N . GLY A 1 335 ? 49.874 -6.221 6.682 1.00 90.02 ? 366 GLY B N 1 ATOM 2560 C CA . GLY A 1 335 ? 50.758 -6.767 5.669 1.00 89.50 ? 366 GLY B CA 1 ATOM 2561 C C . GLY A 1 335 ? 51.358 -5.693 4.791 1.00 91.58 ? 366 GLY B C 1 ATOM 2562 O O . GLY A 1 335 ? 52.337 -5.928 4.081 1.00 91.30 ? 366 GLY B O 1 ATOM 2563 N N . SER A 1 336 ? 50.766 -4.505 4.853 1.00 98.44 ? 367 SER B N 1 ATOM 2564 C CA . SER A 1 336 ? 51.174 -3.380 4.020 1.00 100.82 ? 367 SER B CA 1 ATOM 2565 C C . SER A 1 336 ? 52.557 -2.879 4.382 1.00 100.28 ? 367 SER B C 1 ATOM 2566 O O . SER A 1 336 ? 53.205 -2.209 3.587 1.00 101.80 ? 367 SER B O 1 ATOM 2567 C CB . SER A 1 336 ? 50.183 -2.236 4.170 1.00 103.29 ? 367 SER B CB 1 ATOM 2568 O OG . SER A 1 336 ? 50.069 -1.887 5.540 1.00 102.55 ? 367 SER B OG 1 ATOM 2569 N N . ASN A 1 337 ? 53.015 -3.202 5.584 1.00 94.34 ? 368 ASN B N 1 ATOM 2570 C CA . ASN A 1 337 ? 54.372 -2.854 5.971 1.00 93.58 ? 368 ASN B CA 1 ATOM 2571 C C . ASN A 1 337 ? 55.391 -3.595 5.118 1.00 92.69 ? 368 ASN B C 1 ATOM 2572 O O . ASN A 1 337 ? 56.582 -3.299 5.156 1.00 92.41 ? 368 ASN B O 1 ATOM 2573 C CB . ASN A 1 337 ? 54.615 -3.092 7.468 1.00 91.54 ? 368 ASN B CB 1 ATOM 2574 C CG . ASN A 1 337 ? 54.373 -4.530 7.891 1.00 89.09 ? 368 ASN B CG 1 ATOM 2575 O OD1 . ASN A 1 337 ? 55.288 -5.352 7.883 1.00 87.31 ? 368 ASN B OD1 1 ATOM 2576 N ND2 . ASN A 1 337 ? 53.141 -4.832 8.288 1.00 89.09 ? 368 ASN B ND2 1 ATOM 2577 N N . GLY A 1 338 ? 54.910 -4.570 4.356 1.00 91.50 ? 369 GLY B N 1 ATOM 2578 C CA . GLY A 1 338 ? 55.709 -5.210 3.335 1.00 91.19 ? 369 GLY B CA 1 ATOM 2579 C C . GLY A 1 338 ? 56.788 -6.140 3.841 1.00 88.69 ? 369 GLY B C 1 ATOM 2580 O O . GLY A 1 338 ? 57.480 -6.782 3.054 1.00 88.31 ? 369 GLY B O 1 ATOM 2581 N N . LYS A 1 339 ? 56.970 -6.177 5.153 1.00 99.96 ? 370 LYS B N 1 ATOM 2582 C CA . LYS A 1 339 ? 57.922 -7.096 5.761 1.00 97.54 ? 370 LYS B CA 1 ATOM 2583 C C . LYS A 1 339 ? 57.280 -8.362 6.361 1.00 95.50 ? 370 LYS B C 1 ATOM 2584 O O . LYS A 1 339 ? 57.971 -9.203 6.952 1.00 93.46 ? 370 LYS B O 1 ATOM 2585 C CB . LYS A 1 339 ? 58.795 -6.351 6.765 1.00 97.12 ? 370 LYS B CB 1 ATOM 2586 C CG . LYS A 1 339 ? 59.563 -5.203 6.132 1.00 99.04 ? 370 LYS B CG 1 ATOM 2587 C CD . LYS A 1 339 ? 60.216 -4.342 7.187 1.00 98.87 ? 370 LYS B CD 1 ATOM 2588 C CE . LYS A 1 339 ? 61.053 -5.202 8.128 1.00 96.32 ? 370 LYS B CE 1 ATOM 2589 N NZ . LYS A 1 339 ? 61.546 -4.462 9.325 1.00 95.93 ? 370 LYS B NZ 1 ATOM 2590 N N . LEU A 1 340 ? 55.960 -8.486 6.205 1.00 93.54 ? 371 LEU B N 1 ATOM 2591 C CA . LEU A 1 340 ? 55.213 -9.583 6.821 1.00 91.85 ? 371 LEU B CA 1 ATOM 2592 C C . LEU A 1 340 ? 55.608 -10.921 6.242 1.00 90.43 ? 371 LEU B C 1 ATOM 2593 O O . LEU A 1 340 ? 55.541 -11.129 5.032 1.00 91.37 ? 371 LEU B O 1 ATOM 2594 C CB . LEU A 1 340 ? 53.708 -9.395 6.655 1.00 93.11 ? 371 LEU B CB 1 ATOM 2595 C CG . LEU A 1 340 ? 52.881 -10.466 7.362 1.00 91.50 ? 371 LEU B CG 1 ATOM 2596 C CD1 . LEU A 1 340 ? 53.117 -10.402 8.831 1.00 90.17 ? 371 LEU B CD1 1 ATOM 2597 C CD2 . LEU A 1 340 ? 51.429 -10.259 7.092 1.00 92.93 ? 371 LEU B CD2 1 ATOM 2598 N N . GLU A 1 341 ? 55.996 -11.832 7.124 1.00 95.02 ? 372 GLU B N 1 ATOM 2599 C CA . GLU A 1 341 ? 56.472 -13.149 6.723 1.00 93.54 ? 372 GLU B CA 1 ATOM 2600 C C . GLU A 1 341 ? 55.455 -14.246 7.018 1.00 92.43 ? 372 GLU B C 1 ATOM 2601 O O . GLU A 1 341 ? 54.987 -14.936 6.118 1.00 92.63 ? 372 GLU B O 1 ATOM 2602 C CB . GLU A 1 341 ? 57.789 -13.479 7.425 1.00 91.93 ? 372 GLU B CB 1 ATOM 2603 C CG . GLU A 1 341 ? 58.927 -12.544 7.092 1.00 92.91 ? 372 GLU B CG 1 ATOM 2604 C CD . GLU A 1 341 ? 60.250 -13.049 7.620 1.00 91.34 ? 372 GLU B CD 1 ATOM 2605 O OE1 . GLU A 1 341 ? 60.264 -14.117 8.270 1.00 89.66 ? 372 GLU B OE1 1 ATOM 2606 O OE2 . GLU A 1 341 ? 61.274 -12.377 7.385 1.00 92.02 ? 372 GLU B OE2 1 ATOM 2607 N N . THR A 1 342 ? 55.137 -14.425 8.293 1.00 84.32 ? 373 THR B N 1 ATOM 2608 C CA . THR A 1 342 ? 54.279 -15.522 8.709 1.00 83.47 ? 373 THR B CA 1 ATOM 2609 C C . THR A 1 342 ? 53.160 -15.076 9.649 1.00 83.94 ? 373 THR B C 1 ATOM 2610 O O . THR A 1 342 ? 53.406 -14.366 10.620 1.00 83.93 ? 373 THR B O 1 ATOM 2611 C CB . THR A 1 342 ? 55.113 -16.595 9.406 1.00 82.41 ? 373 THR B CB 1 ATOM 2612 O OG1 . THR A 1 342 ? 54.313 -17.259 10.391 1.00 82.76 ? 373 THR B OG1 1 ATOM 2613 C CG2 . THR A 1 342 ? 56.320 -15.956 10.087 1.00 82.06 ? 373 THR B CG2 1 ATOM 2614 N N . MET A 1 343 ? 51.932 -15.498 9.355 1.00 77.22 ? 374 MET B N 1 ATOM 2615 C CA . MET A 1 343 ? 50.793 -15.251 10.237 1.00 77.75 ? 374 MET B CA 1 ATOM 2616 C C . MET A 1 343 ? 49.932 -16.503 10.475 1.00 78.17 ? 374 MET B C 1 ATOM 2617 O O . MET A 1 343 ? 49.540 -17.190 9.527 1.00 78.26 ? 374 MET B O 1 ATOM 2618 C CB . MET A 1 343 ? 49.907 -14.135 9.691 1.00 79.62 ? 374 MET B CB 1 ATOM 2619 C CG . MET A 1 343 ? 48.523 -14.188 10.289 1.00 80.25 ? 374 MET B CG 1 ATOM 2620 S SD . MET A 1 343 ? 47.451 -12.847 9.803 1.00 82.71 ? 374 MET B SD 1 ATOM 2621 C CE . MET A 1 343 ? 47.299 -13.133 8.045 1.00 83.57 ? 374 MET B CE 1 ATOM 2622 N N . ASP A 1 344 ? 49.650 -16.807 11.741 1.00 72.10 ? 375 ASP B N 1 ATOM 2623 C CA . ASP A 1 344 ? 48.674 -17.837 12.060 1.00 71.53 ? 375 ASP B CA 1 ATOM 2624 C C . ASP A 1 344 ? 47.647 -17.318 13.075 1.00 72.35 ? 375 ASP B C 1 ATOM 2625 O O . ASP A 1 344 ? 47.954 -17.130 14.239 1.00 71.96 ? 375 ASP B O 1 ATOM 2626 C CB . ASP A 1 344 ? 49.409 -19.051 12.604 1.00 70.49 ? 375 ASP B CB 1 ATOM 2627 C CG . ASP A 1 344 ? 48.500 -20.223 12.851 1.00 71.05 ? 375 ASP B CG 1 ATOM 2628 O OD1 . ASP A 1 344 ? 47.260 -20.059 12.787 1.00 72.10 ? 375 ASP B OD1 1 ATOM 2629 O OD2 . ASP A 1 344 ? 49.041 -21.323 13.119 1.00 70.48 ? 375 ASP B OD2 1 ATOM 2630 N N . VAL A 1 345 ? 46.425 -17.091 12.607 1.00 73.57 ? 376 VAL B N 1 ATOM 2631 C CA . VAL A 1 345 ? 45.281 -16.678 13.430 1.00 74.53 ? 376 VAL B CA 1 ATOM 2632 C C . VAL A 1 345 ? 44.218 -17.756 13.769 1.00 74.20 ? 376 VAL B C 1 ATOM 2633 O O . VAL A 1 345 ? 43.139 -17.424 14.255 1.00 75.31 ? 376 VAL B O 1 ATOM 2634 C CB . VAL A 1 345 ? 44.641 -15.425 12.865 1.00 76.90 ? 376 VAL B CB 1 ATOM 2635 C CG1 . VAL A 1 345 ? 45.691 -14.346 12.754 1.00 77.43 ? 376 VAL B CG1 1 ATOM 2636 C CG2 . VAL A 1 345 ? 44.047 -15.725 11.506 1.00 77.78 ? 376 VAL B CG2 1 ATOM 2637 N N . SER A 1 346 ? 44.505 -19.020 13.458 1.00 81.21 ? 377 SER B N 1 ATOM 2638 C CA . SER A 1 346 ? 43.513 -20.108 13.464 1.00 82.17 ? 377 SER B CA 1 ATOM 2639 C C . SER A 1 346 ? 42.845 -20.411 14.818 1.00 83.19 ? 377 SER B C 1 ATOM 2640 O O . SER A 1 346 ? 43.360 -20.015 15.858 1.00 82.98 ? 377 SER B O 1 ATOM 2641 C CB . SER A 1 346 ? 44.162 -21.385 12.939 1.00 81.47 ? 377 SER B CB 1 ATOM 2642 O OG . SER A 1 346 ? 44.998 -21.963 13.926 1.00 81.01 ? 377 SER B OG 1 ATOM 2643 N N . ASN A 1 347 ? 41.694 -21.093 14.790 1.00 76.15 ? 378 ASN B N 1 ATOM 2644 C CA . ASN A 1 347 ? 40.961 -21.523 16.001 1.00 77.02 ? 378 ASN B CA 1 ATOM 2645 C C . ASN A 1 347 ? 40.336 -20.381 16.802 1.00 77.84 ? 378 ASN B C 1 ATOM 2646 O O . ASN A 1 347 ? 40.186 -20.466 18.022 1.00 77.89 ? 378 ASN B O 1 ATOM 2647 C CB . ASN A 1 347 ? 41.867 -22.377 16.919 1.00 76.29 ? 378 ASN B CB 1 ATOM 2648 C CG . ASN A 1 347 ? 41.087 -23.161 17.989 1.00 77.07 ? 378 ASN B CG 1 ATOM 2649 O OD1 . ASN A 1 347 ? 39.960 -23.591 17.751 1.00 78.07 ? 378 ASN B OD1 1 ATOM 2650 N ND2 . ASN A 1 347 ? 41.704 -23.353 19.170 1.00 76.59 ? 378 ASN B ND2 1 ATOM 2651 N N . ASN A 1 348 ? 39.955 -19.315 16.111 1.00 85.13 ? 379 ASN B N 1 ATOM 2652 C CA . ASN A 1 348 ? 39.364 -18.157 16.776 1.00 85.80 ? 379 ASN B CA 1 ATOM 2653 C C . ASN A 1 348 ? 37.927 -17.897 16.344 1.00 87.18 ? 379 ASN B C 1 ATOM 2654 O O . ASN A 1 348 ? 37.323 -18.700 15.640 1.00 87.78 ? 379 ASN B O 1 ATOM 2655 C CB . ASN A 1 348 ? 40.210 -16.897 16.553 1.00 84.66 ? 379 ASN B CB 1 ATOM 2656 C CG . ASN A 1 348 ? 41.407 -16.814 17.492 1.00 83.63 ? 379 ASN B CG 1 ATOM 2657 O OD1 . ASN A 1 348 ? 41.371 -16.108 18.501 1.00 84.38 ? 379 ASN B OD1 1 ATOM 2658 N ND2 . ASN A 1 348 ? 42.473 -17.533 17.162 1.00 81.90 ? 379 ASN B ND2 1 ATOM 2659 N N . SER A 1 349 ? 37.364 -16.805 16.842 1.00 83.37 ? 380 SER B N 1 ATOM 2660 C CA . SER A 1 349 ? 36.077 -16.294 16.378 1.00 84.56 ? 380 SER B CA 1 ATOM 2661 C C . SER A 1 349 ? 36.192 -15.142 15.371 1.00 84.67 ? 380 SER B C 1 ATOM 2662 O O . SER A 1 349 ? 35.203 -14.441 15.131 1.00 86.78 ? 380 SER B O 1 ATOM 2663 C CB . SER A 1 349 ? 35.135 -15.952 17.539 1.00 85.73 ? 380 SER B CB 1 ATOM 2664 O OG . SER A 1 349 ? 34.556 -17.128 18.080 1.00 86.77 ? 380 SER B OG 1 ATOM 2665 N N . PHE A 1 350 ? 37.402 -14.897 14.859 1.00 88.30 ? 381 PHE B N 1 ATOM 2666 C CA . PHE A 1 350 ? 37.663 -13.795 13.917 1.00 87.79 ? 381 PHE B CA 1 ATOM 2667 C C . PHE A 1 350 ? 36.644 -13.754 12.787 1.00 88.88 ? 381 PHE B C 1 ATOM 2668 O O . PHE A 1 350 ? 36.282 -14.793 12.255 1.00 88.87 ? 381 PHE B O 1 ATOM 2669 C CB . PHE A 1 350 ? 39.029 -13.983 13.268 1.00 86.30 ? 381 PHE B CB 1 ATOM 2670 C CG . PHE A 1 350 ? 40.149 -13.311 13.993 1.00 85.36 ? 381 PHE B CG 1 ATOM 2671 C CD1 . PHE A 1 350 ? 40.032 -12.005 14.417 1.00 86.62 ? 381 PHE B CD1 1 ATOM 2672 C CD2 . PHE A 1 350 ? 41.329 -13.991 14.239 1.00 83.95 ? 381 PHE B CD2 1 ATOM 2673 C CE1 . PHE A 1 350 ? 41.068 -11.397 15.074 1.00 85.96 ? 381 PHE B CE1 1 ATOM 2674 C CE2 . PHE A 1 350 ? 42.364 -13.391 14.893 1.00 83.01 ? 381 PHE B CE2 1 ATOM 2675 C CZ . PHE A 1 350 ? 42.237 -12.099 15.314 1.00 83.93 ? 381 PHE B CZ 1 ATOM 2676 N N . THR A 1 351 ? 36.172 -12.565 12.417 1.00 102.70 ? 382 THR B N 1 ATOM 2677 C CA . THR A 1 351 ? 35.178 -12.461 11.348 1.00 104.30 ? 382 THR B CA 1 ATOM 2678 C C . THR A 1 351 ? 35.622 -11.495 10.251 1.00 105.46 ? 382 THR B C 1 ATOM 2679 O O . THR A 1 351 ? 36.709 -10.916 10.327 1.00 105.06 ? 382 THR B O 1 ATOM 2680 C CB . THR A 1 351 ? 33.804 -12.016 11.891 1.00 106.33 ? 382 THR B CB 1 ATOM 2681 O OG1 . THR A 1 351 ? 33.882 -10.660 12.342 1.00 107.93 ? 382 THR B OG1 1 ATOM 2682 C CG2 . THR A 1 351 ? 33.367 -12.897 13.051 1.00 105.57 ? 382 THR B CG2 1 ATOM 2683 N N . GLY A 1 352 ? 34.772 -11.316 9.241 1.00 104.33 ? 383 GLY B N 1 ATOM 2684 C CA . GLY A 1 352 ? 35.020 -10.337 8.193 1.00 106.23 ? 383 GLY B CA 1 ATOM 2685 C C . GLY A 1 352 ? 35.798 -10.789 6.971 1.00 105.42 ? 383 GLY B C 1 ATOM 2686 O O . GLY A 1 352 ? 35.658 -11.919 6.512 1.00 104.11 ? 383 GLY B O 1 ATOM 2687 N N . THR A 1 353 ? 36.586 -9.872 6.418 1.00 101.83 ? 384 THR B N 1 ATOM 2688 C CA . THR A 1 353 ? 37.343 -10.116 5.194 1.00 101.52 ? 384 THR B CA 1 ATOM 2689 C C . THR A 1 353 ? 38.834 -10.228 5.457 1.00 99.60 ? 384 THR B C 1 ATOM 2690 O O . THR A 1 353 ? 39.383 -9.526 6.312 1.00 99.51 ? 384 THR B O 1 ATOM 2691 C CB . THR A 1 353 ? 37.163 -8.961 4.199 1.00 104.39 ? 384 THR B CB 1 ATOM 2692 O OG1 . THR A 1 353 ? 35.771 -8.675 4.046 1.00 106.50 ? 384 THR B OG1 1 ATOM 2693 C CG2 . THR A 1 353 ? 37.771 -9.299 2.843 1.00 104.33 ? 384 THR B CG2 1 ATOM 2694 N N . ILE A 1 354 ? 39.486 -11.110 4.708 1.00 95.77 ? 385 ILE B N 1 ATOM 2695 C CA . ILE A 1 354 ? 40.935 -11.190 4.713 1.00 94.28 ? 385 ILE B CA 1 ATOM 2696 C C . ILE A 1 354 ? 41.490 -9.927 4.087 1.00 96.25 ? 385 ILE B C 1 ATOM 2697 O O . ILE A 1 354 ? 40.989 -9.456 3.063 1.00 98.35 ? 385 ILE B O 1 ATOM 2698 C CB . ILE A 1 354 ? 41.451 -12.407 3.919 1.00 92.64 ? 385 ILE B CB 1 ATOM 2699 C CG1 . ILE A 1 354 ? 40.960 -13.706 4.542 1.00 90.65 ? 385 ILE B CG1 1 ATOM 2700 C CG2 . ILE A 1 354 ? 42.973 -12.428 3.868 1.00 91.34 ? 385 ILE B CG2 1 ATOM 2701 C CD1 . ILE A 1 354 ? 41.259 -14.903 3.686 1.00 89.36 ? 385 ILE B CD1 1 ATOM 2702 N N . PRO A 1 355 ? 42.515 -9.362 4.721 1.00 99.92 ? 386 PRO B N 1 ATOM 2703 C CA . PRO A 1 355 ? 43.240 -8.201 4.211 1.00 101.54 ? 386 PRO B CA 1 ATOM 2704 C C . PRO A 1 355 ? 43.862 -8.455 2.840 1.00 101.87 ? 386 PRO B C 1 ATOM 2705 O O . PRO A 1 355 ? 44.562 -9.453 2.642 1.00 99.90 ? 386 PRO B O 1 ATOM 2706 C CB . PRO A 1 355 ? 44.336 -8.003 5.256 1.00 99.95 ? 386 PRO B CB 1 ATOM 2707 C CG . PRO A 1 355 ? 43.748 -8.558 6.520 1.00 98.54 ? 386 PRO B CG 1 ATOM 2708 C CD . PRO A 1 355 ? 42.922 -9.721 6.090 1.00 97.85 ? 386 PRO B CD 1 ATOM 2709 N N . SER A 1 356 ? 43.613 -7.526 1.920 1.00 120.54 ? 387 SER B N 1 ATOM 2710 C CA . SER A 1 356 ? 44.090 -7.605 0.546 1.00 121.41 ? 387 SER B CA 1 ATOM 2711 C C . SER A 1 356 ? 45.604 -7.444 0.459 1.00 120.54 ? 387 SER B C 1 ATOM 2712 O O . SER A 1 356 ? 46.245 -7.940 -0.463 1.00 120.25 ? 387 SER B O 1 ATOM 2713 C CB . SER A 1 356 ? 43.424 -6.507 -0.287 1.00 124.68 ? 387 SER B CB 1 ATOM 2714 O OG . SER A 1 356 ? 42.095 -6.266 0.146 1.00 125.81 ? 387 SER B OG 1 ATOM 2715 N N . SER A 1 357 ? 46.168 -6.736 1.427 1.00 128.24 ? 388 SER B N 1 ATOM 2716 C CA . SER A 1 357 ? 47.563 -6.320 1.368 1.00 127.90 ? 388 SER B CA 1 ATOM 2717 C C . SER A 1 357 ? 48.564 -7.232 2.089 1.00 124.96 ? 388 SER B C 1 ATOM 2718 O O . SER A 1 357 ? 49.726 -6.871 2.221 1.00 124.57 ? 388 SER B O 1 ATOM 2719 C CB . SER A 1 357 ? 47.707 -4.867 1.842 1.00 129.67 ? 388 SER B CB 1 ATOM 2720 O OG . SER A 1 357 ? 47.043 -4.660 3.078 1.00 129.25 ? 388 SER B OG 1 ATOM 2721 N N . LEU A 1 358 ? 48.119 -8.389 2.573 1.00 99.88 ? 389 LEU B N 1 ATOM 2722 C CA . LEU A 1 358 ? 48.978 -9.263 3.386 1.00 97.14 ? 389 LEU B CA 1 ATOM 2723 C C . LEU A 1 358 ? 50.356 -9.465 2.775 1.00 96.55 ? 389 LEU B C 1 ATOM 2724 O O . LEU A 1 358 ? 51.380 -9.408 3.451 1.00 95.30 ? 389 LEU B O 1 ATOM 2725 C CB . LEU A 1 358 ? 48.325 -10.635 3.572 1.00 95.40 ? 389 LEU B CB 1 ATOM 2726 C CG . LEU A 1 358 ? 47.097 -10.744 4.475 1.00 95.27 ? 389 LEU B CG 1 ATOM 2727 C CD1 . LEU A 1 358 ? 46.629 -12.181 4.581 1.00 93.47 ? 389 LEU B CD1 1 ATOM 2728 C CD2 . LEU A 1 358 ? 47.423 -10.189 5.847 1.00 94.61 ? 389 LEU B CD2 1 ATOM 2729 N N . CYS A 1 359 ? 50.361 -9.690 1.476 1.00 99.59 ? 390 CYS B N 1 ATOM 2730 C CA . CYS A 1 359 ? 51.590 -9.936 0.762 1.00 99.28 ? 390 CYS B CA 1 ATOM 2731 C C . CYS A 1 359 ? 52.200 -8.705 0.118 1.00 101.47 ? 390 CYS B C 1 ATOM 2732 O O . CYS A 1 359 ? 53.156 -8.840 -0.632 1.00 101.64 ? 390 CYS B O 1 ATOM 2733 C CB . CYS A 1 359 ? 51.418 -11.039 -0.264 1.00 98.93 ? 390 CYS B CB 1 ATOM 2734 S SG . CYS A 1 359 ? 52.792 -12.180 -0.195 1.00 96.57 ? 390 CYS B SG 1 ATOM 2735 N N . HIS A 1 360 ? 51.678 -7.515 0.429 1.00 122.11 ? 391 HIS B N 1 ATOM 2736 C CA . HIS A 1 360 ? 51.980 -6.260 -0.291 1.00 124.72 ? 391 HIS B CA 1 ATOM 2737 C C . HIS A 1 360 ? 53.478 -6.160 -0.536 1.00 124.33 ? 391 HIS B C 1 ATOM 2738 O O . HIS A 1 360 ? 53.927 -5.503 -1.477 1.00 126.29 ? 391 HIS B O 1 ATOM 2739 C CB . HIS A 1 360 ? 51.514 -5.061 0.563 1.00 125.91 ? 391 HIS B CB 1 ATOM 2740 C CG . HIS A 1 360 ? 51.466 -3.737 -0.149 1.00 128.94 ? 391 HIS B CG 1 ATOM 2741 N ND1 . HIS A 1 360 ? 52.565 -2.912 -0.274 1.00 129.76 ? 391 HIS B ND1 1 ATOM 2742 C CD2 . HIS A 1 360 ? 50.427 -3.055 -0.695 1.00 131.44 ? 391 HIS B CD2 1 ATOM 2743 C CE1 . HIS A 1 360 ? 52.216 -1.801 -0.900 1.00 132.63 ? 391 HIS B CE1 1 ATOM 2744 N NE2 . HIS A 1 360 ? 50.923 -1.864 -1.165 1.00 133.72 ? 391 HIS B NE2 1 ATOM 2745 N N . GLY A 1 361 ? 54.243 -6.838 0.314 1.00 93.00 ? 392 GLY B N 1 ATOM 2746 C CA . GLY A 1 361 ? 55.678 -6.925 0.157 1.00 92.34 ? 392 GLY B CA 1 ATOM 2747 C C . GLY A 1 361 ? 56.243 -8.246 -0.325 1.00 90.73 ? 392 GLY B C 1 ATOM 2748 O O . GLY A 1 361 ? 57.455 -8.365 -0.488 1.00 90.25 ? 392 GLY B O 1 ATOM 2749 N N . ASN A 1 362 ? 55.385 -9.239 -0.532 1.00 89.93 ? 393 ASN B N 1 ATOM 2750 C CA . ASN A 1 362 ? 55.815 -10.530 -1.093 1.00 88.61 ? 393 ASN B CA 1 ATOM 2751 C C . ASN A 1 362 ? 56.856 -11.269 -0.271 1.00 86.20 ? 393 ASN B C 1 ATOM 2752 O O . ASN A 1 362 ? 57.631 -12.051 -0.822 1.00 85.56 ? 393 ASN B O 1 ATOM 2753 C CB . ASN A 1 362 ? 56.337 -10.358 -2.524 1.00 90.43 ? 393 ASN B CB 1 ATOM 2754 C CG . ASN A 1 362 ? 55.297 -10.711 -3.577 1.00 91.67 ? 393 ASN B CG 1 ATOM 2755 O OD1 . ASN A 1 362 ? 55.496 -11.629 -4.368 1.00 91.34 ? 393 ASN B OD1 1 ATOM 2756 N ND2 . ASN A 1 362 ? 54.179 -9.987 -3.588 1.00 93.18 ? 393 ASN B ND2 1 ATOM 2757 N N . LYS A 1 363 ? 56.898 -10.988 1.031 1.00 87.81 ? 394 LYS B N 1 ATOM 2758 C CA . LYS A 1 363 ? 57.785 -11.698 1.952 1.00 85.50 ? 394 LYS B CA 1 ATOM 2759 C C . LYS A 1 363 ? 57.072 -12.802 2.736 1.00 83.50 ? 394 LYS B C 1 ATOM 2760 O O . LYS A 1 363 ? 57.697 -13.547 3.475 1.00 81.55 ? 394 LYS B O 1 ATOM 2761 C CB . LYS A 1 363 ? 58.470 -10.715 2.904 1.00 85.45 ? 394 LYS B CB 1 ATOM 2762 C CG . LYS A 1 363 ? 59.498 -9.819 2.222 1.00 87.03 ? 394 LYS B CG 1 ATOM 2763 C CD . LYS A 1 363 ? 60.767 -9.648 3.068 1.00 85.86 ? 394 LYS B CD 1 ATOM 2764 C CE . LYS A 1 363 ? 60.709 -8.419 3.976 1.00 86.46 ? 394 LYS B CE 1 ATOM 2765 N NZ . LYS A 1 363 ? 60.505 -7.150 3.195 1.00 89.15 ? 394 LYS B NZ 1 ATOM 2766 N N . LEU A 1 364 ? 55.765 -12.917 2.539 1.00 82.78 ? 395 LEU B N 1 ATOM 2767 C CA . LEU A 1 364 ? 54.927 -13.830 3.313 1.00 81.18 ? 395 LEU B CA 1 ATOM 2768 C C . LEU A 1 364 ? 54.925 -15.273 2.774 1.00 79.95 ? 395 LEU B C 1 ATOM 2769 O O . LEU A 1 364 ? 54.653 -15.488 1.597 1.00 81.02 ? 395 LEU B O 1 ATOM 2770 C CB . LEU A 1 364 ? 53.501 -13.266 3.356 1.00 82.52 ? 395 LEU B CB 1 ATOM 2771 C CG . LEU A 1 364 ? 52.370 -13.856 4.202 1.00 81.50 ? 395 LEU B CG 1 ATOM 2772 C CD1 . LEU A 1 364 ? 51.299 -12.805 4.418 1.00 83.26 ? 395 LEU B CD1 1 ATOM 2773 C CD2 . LEU A 1 364 ? 51.740 -15.050 3.539 1.00 80.95 ? 395 LEU B CD2 1 ATOM 2774 N N . TYR A 1 365 ? 55.207 -16.254 3.638 1.00 90.91 ? 396 TYR B N 1 ATOM 2775 C CA . TYR A 1 365 ? 55.202 -17.685 3.254 1.00 89.65 ? 396 TYR B CA 1 ATOM 2776 C C . TYR A 1 365 ? 54.110 -18.559 3.905 1.00 88.67 ? 396 TYR B C 1 ATOM 2777 O O . TYR A 1 365 ? 53.340 -19.212 3.205 1.00 88.91 ? 396 TYR B O 1 ATOM 2778 C CB . TYR A 1 365 ? 56.585 -18.346 3.388 1.00 88.32 ? 396 TYR B CB 1 ATOM 2779 C CG . TYR A 1 365 ? 57.104 -18.491 4.805 1.00 86.87 ? 396 TYR B CG 1 ATOM 2780 C CD1 . TYR A 1 365 ? 57.704 -17.420 5.458 1.00 87.13 ? 396 TYR B CD1 1 ATOM 2781 C CD2 . TYR A 1 365 ? 57.017 -19.698 5.480 1.00 85.93 ? 396 TYR B CD2 1 ATOM 2782 C CE1 . TYR A 1 365 ? 58.191 -17.544 6.737 1.00 86.12 ? 396 TYR B CE1 1 ATOM 2783 C CE2 . TYR A 1 365 ? 57.499 -19.825 6.770 1.00 85.66 ? 396 TYR B CE2 1 ATOM 2784 C CZ . TYR A 1 365 ? 58.084 -18.744 7.384 1.00 85.54 ? 396 TYR B CZ 1 ATOM 2785 O OH . TYR A 1 365 ? 58.570 -18.859 8.657 1.00 85.28 ? 396 TYR B OH 1 ATOM 2786 N N . LYS A 1 366 ? 54.088 -18.630 5.234 1.00 90.53 ? 397 LYS B N 1 ATOM 2787 C CA . LYS A 1 366 ? 53.096 -19.445 5.941 1.00 90.51 ? 397 LYS B CA 1 ATOM 2788 C C . LYS A 1 366 ? 51.859 -18.632 6.359 1.00 91.18 ? 397 LYS B C 1 ATOM 2789 O O . LYS A 1 366 ? 51.950 -17.740 7.196 1.00 91.23 ? 397 LYS B O 1 ATOM 2790 C CB . LYS A 1 366 ? 53.748 -20.125 7.154 1.00 90.12 ? 397 LYS B CB 1 ATOM 2791 C CG . LYS A 1 366 ? 52.830 -21.026 7.965 1.00 90.59 ? 397 LYS B CG 1 ATOM 2792 C CD . LYS A 1 366 ? 53.615 -21.994 8.864 1.00 90.06 ? 397 LYS B CD 1 ATOM 2793 C CE . LYS A 1 366 ? 54.466 -21.278 9.913 1.00 89.94 ? 397 LYS B CE 1 ATOM 2794 N NZ . LYS A 1 366 ? 55.182 -22.247 10.787 1.00 89.07 ? 397 LYS B NZ 1 ATOM 2795 N N . LEU A 1 367 ? 50.709 -18.934 5.754 1.00 73.41 ? 398 LEU B N 1 ATOM 2796 C CA . LEU A 1 367 ? 49.432 -18.318 6.144 1.00 74.50 ? 398 LEU B CA 1 ATOM 2797 C C . LEU A 1 367 ? 48.365 -19.333 6.598 1.00 73.60 ? 398 LEU B C 1 ATOM 2798 O O . LEU A 1 367 ? 47.842 -20.138 5.802 1.00 73.61 ? 398 LEU B O 1 ATOM 2799 C CB . LEU A 1 367 ? 48.876 -17.448 5.021 1.00 76.78 ? 398 LEU B CB 1 ATOM 2800 C CG . LEU A 1 367 ? 47.484 -16.867 5.268 1.00 78.14 ? 398 LEU B CG 1 ATOM 2801 C CD1 . LEU A 1 367 ? 47.367 -16.305 6.653 1.00 77.81 ? 398 LEU B CD1 1 ATOM 2802 C CD2 . LEU A 1 367 ? 47.212 -15.773 4.270 1.00 80.55 ? 398 LEU B CD2 1 ATOM 2803 N N . ILE A 1 368 ? 48.042 -19.277 7.890 1.00 75.50 ? 399 ILE B N 1 ATOM 2804 C CA . ILE A 1 368 ? 47.030 -20.156 8.459 1.00 76.24 ? 399 ILE B CA 1 ATOM 2805 C C . ILE A 1 368 ? 45.833 -19.326 8.950 1.00 77.54 ? 399 ILE B C 1 ATOM 2806 O O . ILE A 1 368 ? 45.881 -18.693 10.001 1.00 77.97 ? 399 ILE B O 1 ATOM 2807 C CB . ILE A 1 368 ? 47.632 -20.962 9.636 1.00 76.09 ? 399 ILE B CB 1 ATOM 2808 C CG1 . ILE A 1 368 ? 49.146 -21.148 9.467 1.00 74.76 ? 399 ILE B CG1 1 ATOM 2809 C CG2 . ILE A 1 368 ? 46.994 -22.296 9.737 1.00 75.86 ? 399 ILE B CG2 1 ATOM 2810 C CD1 . ILE A 1 368 ? 49.531 -22.139 8.407 1.00 75.53 ? 399 ILE B CD1 1 ATOM 2811 N N . LEU A 1 369 ? 44.754 -19.348 8.180 1.00 80.74 ? 400 LEU B N 1 ATOM 2812 C CA . LEU A 1 369 ? 43.535 -18.631 8.530 1.00 82.03 ? 400 LEU B CA 1 ATOM 2813 C C . LEU A 1 369 ? 42.447 -19.538 9.121 1.00 83.19 ? 400 LEU B C 1 ATOM 2814 O O . LEU A 1 369 ? 41.326 -19.089 9.368 1.00 84.44 ? 400 LEU B O 1 ATOM 2815 C CB . LEU A 1 369 ? 43.024 -17.837 7.323 1.00 82.39 ? 400 LEU B CB 1 ATOM 2816 C CG . LEU A 1 369 ? 43.937 -16.672 6.916 1.00 82.38 ? 400 LEU B CG 1 ATOM 2817 C CD1 . LEU A 1 369 ? 43.857 -16.398 5.449 1.00 83.67 ? 400 LEU B CD1 1 ATOM 2818 C CD2 . LEU A 1 369 ? 43.627 -15.395 7.683 1.00 83.54 ? 400 LEU B CD2 1 ATOM 2819 N N . PHE A 1 370 ? 42.774 -20.814 9.329 1.00 74.66 ? 401 PHE B N 1 ATOM 2820 C CA . PHE A 1 370 ? 41.741 -21.851 9.484 1.00 74.88 ? 401 PHE B CA 1 ATOM 2821 C C . PHE A 1 370 ? 40.863 -21.839 10.732 1.00 75.50 ? 401 PHE B C 1 ATOM 2822 O O . PHE A 1 370 ? 41.228 -21.282 11.761 1.00 75.36 ? 401 PHE B O 1 ATOM 2823 C CB . PHE A 1 370 ? 42.276 -23.270 9.174 1.00 73.57 ? 401 PHE B CB 1 ATOM 2824 C CG . PHE A 1 370 ? 43.129 -23.900 10.257 1.00 72.64 ? 401 PHE B CG 1 ATOM 2825 C CD1 . PHE A 1 370 ? 42.605 -24.234 11.495 1.00 73.43 ? 401 PHE B CD1 1 ATOM 2826 C CD2 . PHE A 1 370 ? 44.433 -24.263 9.986 1.00 71.11 ? 401 PHE B CD2 1 ATOM 2827 C CE1 . PHE A 1 370 ? 43.392 -24.853 12.457 1.00 72.64 ? 401 PHE B CE1 1 ATOM 2828 C CE2 . PHE A 1 370 ? 45.222 -24.883 10.944 1.00 70.35 ? 401 PHE B CE2 1 ATOM 2829 C CZ . PHE A 1 370 ? 44.701 -25.177 12.177 1.00 71.09 ? 401 PHE B CZ 1 ATOM 2830 N N . SER A 1 371 ? 39.707 -22.485 10.616 1.00 84.01 ? 402 SER B N 1 ATOM 2831 C CA . SER A 1 371 ? 38.771 -22.620 11.727 1.00 85.33 ? 402 SER B CA 1 ATOM 2832 C C . SER A 1 371 ? 38.366 -21.257 12.296 1.00 85.82 ? 402 SER B C 1 ATOM 2833 O O . SER A 1 371 ? 38.546 -20.977 13.484 1.00 85.93 ? 402 SER B O 1 ATOM 2834 C CB . SER A 1 371 ? 39.341 -23.544 12.820 1.00 85.15 ? 402 SER B CB 1 ATOM 2835 O OG . SER A 1 371 ? 39.332 -24.908 12.423 1.00 85.07 ? 402 SER B OG 1 ATOM 2836 N N . ASN A 1 372 ? 37.849 -20.403 11.421 1.00 91.32 ? 403 ASN B N 1 ATOM 2837 C CA . ASN A 1 372 ? 37.399 -19.079 11.816 1.00 91.84 ? 403 ASN B CA 1 ATOM 2838 C C . ASN A 1 372 ? 36.013 -18.750 11.269 1.00 93.34 ? 403 ASN B C 1 ATOM 2839 O O . ASN A 1 372 ? 35.362 -19.586 10.666 1.00 94.21 ? 403 ASN B O 1 ATOM 2840 C CB . ASN A 1 372 ? 38.410 -18.019 11.374 1.00 90.41 ? 403 ASN B CB 1 ATOM 2841 C CG . ASN A 1 372 ? 39.504 -17.781 12.403 1.00 89.50 ? 403 ASN B CG 1 ATOM 2842 O OD1 . ASN A 1 372 ? 39.283 -17.114 13.412 1.00 90.26 ? 403 ASN B OD1 1 ATOM 2843 N ND2 . ASN A 1 372 ? 40.693 -18.309 12.141 1.00 87.88 ? 403 ASN B ND2 1 ATOM 2844 N N . MET A 1 373 ? 35.549 -17.540 11.535 1.00 105.55 ? 404 MET B N 1 ATOM 2845 C CA . MET A 1 373 ? 34.278 -17.046 11.015 1.00 106.83 ? 404 MET B CA 1 ATOM 2846 C C . MET A 1 373 ? 34.391 -16.169 9.762 1.00 106.22 ? 404 MET B C 1 ATOM 2847 O O . MET A 1 373 ? 33.424 -15.507 9.378 1.00 107.46 ? 404 MET B O 1 ATOM 2848 C CB . MET A 1 373 ? 33.448 -16.387 12.117 1.00 108.06 ? 404 MET B CB 1 ATOM 2849 C CG . MET A 1 373 ? 32.680 -17.385 12.971 1.00 109.51 ? 404 MET B CG 1 ATOM 2850 S SD . MET A 1 373 ? 31.277 -18.097 12.082 1.00 111.16 ? 404 MET B SD 1 ATOM 2851 C CE . MET A 1 373 ? 31.939 -19.613 11.376 1.00 109.64 ? 404 MET B CE 1 ATOM 2852 N N . PHE A 1 374 ? 35.589 -16.122 9.176 1.00 92.02 ? 405 PHE B N 1 ATOM 2853 C CA . PHE A 1 374 ? 35.880 -15.277 8.012 1.00 92.82 ? 405 PHE B CA 1 ATOM 2854 C C . PHE A 1 374 ? 34.827 -15.443 6.901 1.00 94.24 ? 405 PHE B C 1 ATOM 2855 O O . PHE A 1 374 ? 34.508 -16.569 6.517 1.00 93.36 ? 405 PHE B O 1 ATOM 2856 C CB . PHE A 1 374 ? 37.255 -15.654 7.426 1.00 91.17 ? 405 PHE B CB 1 ATOM 2857 C CG . PHE A 1 374 ? 38.438 -15.346 8.327 1.00 89.93 ? 405 PHE B CG 1 ATOM 2858 C CD1 . PHE A 1 374 ? 38.532 -14.138 9.013 1.00 90.96 ? 405 PHE B CD1 1 ATOM 2859 C CD2 . PHE A 1 374 ? 39.473 -16.262 8.473 1.00 87.78 ? 405 PHE B CD2 1 ATOM 2860 C CE1 . PHE A 1 374 ? 39.634 -13.855 9.842 1.00 89.81 ? 405 PHE B CE1 1 ATOM 2861 C CE2 . PHE A 1 374 ? 40.574 -15.985 9.300 1.00 86.67 ? 405 PHE B CE2 1 ATOM 2862 C CZ . PHE A 1 374 ? 40.651 -14.779 9.981 1.00 87.67 ? 405 PHE B CZ 1 ATOM 2863 N N . GLU A 1 375 ? 34.286 -14.338 6.386 1.00 102.88 ? 406 GLU B N 1 ATOM 2864 C CA . GLU A 1 375 ? 33.355 -14.409 5.252 1.00 104.48 ? 406 GLU B CA 1 ATOM 2865 C C . GLU A 1 375 ? 33.924 -13.699 4.025 1.00 105.81 ? 406 GLU B C 1 ATOM 2866 O O . GLU A 1 375 ? 35.069 -13.255 4.034 1.00 105.26 ? 406 GLU B O 1 ATOM 2867 C CB . GLU A 1 375 ? 31.964 -13.863 5.618 1.00 106.67 ? 406 GLU B CB 1 ATOM 2868 C CG . GLU A 1 375 ? 31.962 -12.548 6.406 1.00 108.26 ? 406 GLU B CG 1 ATOM 2869 C CD . GLU A 1 375 ? 30.585 -11.878 6.458 1.00 111.03 ? 406 GLU B CD 1 ATOM 2870 O OE1 . GLU A 1 375 ? 29.753 -12.119 5.549 1.00 112.26 ? 406 GLU B OE1 1 ATOM 2871 O OE2 . GLU A 1 375 ? 30.338 -11.103 7.411 1.00 112.04 ? 406 GLU B OE2 1 ATOM 2872 N N . GLY A 1 376 ? 33.133 -13.619 2.961 1.00 121.76 ? 407 GLY B N 1 ATOM 2873 C CA . GLY A 1 376 ? 33.534 -12.878 1.777 1.00 123.42 ? 407 GLY B CA 1 ATOM 2874 C C . GLY A 1 376 ? 34.485 -13.631 0.864 1.00 121.97 ? 407 GLY B C 1 ATOM 2875 O O . GLY A 1 376 ? 34.903 -14.742 1.176 1.00 119.54 ? 407 GLY B O 1 ATOM 2876 N N . GLU A 1 377 ? 34.819 -13.020 -0.273 1.00 107.84 ? 408 GLU B N 1 ATOM 2877 C CA . GLU A 1 377 ? 35.623 -13.671 -1.309 1.00 106.95 ? 408 GLU B CA 1 ATOM 2878 C C . GLU A 1 377 ? 37.068 -13.799 -0.845 1.00 104.94 ? 408 GLU B C 1 ATOM 2879 O O . GLU A 1 377 ? 37.426 -13.339 0.233 1.00 104.33 ? 408 GLU B O 1 ATOM 2880 C CB . GLU A 1 377 ? 35.550 -12.871 -2.623 1.00 109.59 ? 408 GLU B CB 1 ATOM 2881 C CG . GLU A 1 377 ? 35.694 -13.686 -3.924 1.00 109.46 ? 408 GLU B CG 1 ATOM 2882 C CD . GLU A 1 377 ? 35.232 -12.912 -5.172 1.00 112.47 ? 408 GLU B CD 1 ATOM 2883 O OE1 . GLU A 1 377 ? 35.388 -11.670 -5.203 1.00 114.44 ? 408 GLU B OE1 1 ATOM 2884 O OE2 . GLU A 1 377 ? 34.702 -13.547 -6.119 1.00 112.95 ? 408 GLU B OE2 1 ATOM 2885 N N . LEU A 1 378 ? 37.892 -14.427 -1.670 1.00 95.09 ? 409 LEU B N 1 ATOM 2886 C CA . LEU A 1 378 ? 39.276 -14.718 -1.328 1.00 93.13 ? 409 LEU B CA 1 ATOM 2887 C C . LEU A 1 378 ? 40.156 -13.731 -2.064 1.00 94.62 ? 409 LEU B C 1 ATOM 2888 O O . LEU A 1 378 ? 40.025 -13.611 -3.280 1.00 96.17 ? 409 LEU B O 1 ATOM 2889 C CB . LEU A 1 378 ? 39.606 -16.149 -1.758 1.00 91.15 ? 409 LEU B CB 1 ATOM 2890 C CG . LEU A 1 378 ? 41.034 -16.689 -1.662 1.00 89.16 ? 409 LEU B CG 1 ATOM 2891 C CD1 . LEU A 1 378 ? 41.474 -16.920 -0.212 1.00 87.11 ? 409 LEU B CD1 1 ATOM 2892 C CD2 . LEU A 1 378 ? 41.150 -17.971 -2.469 1.00 88.08 ? 409 LEU B CD2 1 ATOM 2893 N N . PRO A 1 379 ? 41.050 -13.018 -1.338 1.00 99.30 ? 410 PRO B N 1 ATOM 2894 C CA . PRO A 1 379 ? 41.787 -11.895 -1.933 1.00 101.06 ? 410 PRO B CA 1 ATOM 2895 C C . PRO A 1 379 ? 42.501 -12.290 -3.213 1.00 101.26 ? 410 PRO B C 1 ATOM 2896 O O . PRO A 1 379 ? 43.280 -13.243 -3.209 1.00 99.23 ? 410 PRO B O 1 ATOM 2897 C CB . PRO A 1 379 ? 42.816 -11.546 -0.855 1.00 99.66 ? 410 PRO B CB 1 ATOM 2898 C CG . PRO A 1 379 ? 42.156 -11.909 0.394 1.00 98.37 ? 410 PRO B CG 1 ATOM 2899 C CD . PRO A 1 379 ? 41.360 -13.155 0.096 1.00 97.42 ? 410 PRO B CD 1 ATOM 2900 N N . LYS A 1 380 ? 42.242 -11.545 -4.288 1.00 98.86 ? 411 LYS B N 1 ATOM 2901 C CA . LYS A 1 380 ? 42.818 -11.861 -5.582 1.00 99.45 ? 411 LYS B CA 1 ATOM 2902 C C . LYS A 1 380 ? 44.315 -11.633 -5.447 1.00 98.59 ? 411 LYS B C 1 ATOM 2903 O O . LYS A 1 380 ? 45.132 -12.388 -5.975 1.00 97.53 ? 411 LYS B O 1 ATOM 2904 C CB . LYS A 1 380 ? 42.170 -11.016 -6.695 1.00 102.64 ? 411 LYS B CB 1 ATOM 2905 C CG . LYS A 1 380 ? 40.700 -11.384 -6.976 1.00 103.51 ? 411 LYS B CG 1 ATOM 2906 C CD . LYS A 1 380 ? 40.081 -10.616 -8.157 1.00 106.75 ? 411 LYS B CD 1 ATOM 2907 C CE . LYS A 1 380 ? 38.681 -11.168 -8.505 1.00 107.39 ? 411 LYS B CE 1 ATOM 2908 N NZ . LYS A 1 380 ? 37.914 -10.428 -9.565 1.00 110.65 ? 411 LYS B NZ 1 ATOM 2909 N N . SER A 1 381 ? 44.666 -10.633 -4.649 1.00 98.88 ? 412 SER B N 1 ATOM 2910 C CA . SER A 1 381 ? 46.063 -10.289 -4.435 1.00 98.22 ? 412 SER B CA 1 ATOM 2911 C C . SER A 1 381 ? 46.860 -11.486 -3.949 1.00 95.27 ? 412 SER B C 1 ATOM 2912 O O . SER A 1 381 ? 48.065 -11.554 -4.153 1.00 94.68 ? 412 SER B O 1 ATOM 2913 C CB . SER A 1 381 ? 46.204 -9.128 -3.442 1.00 98.77 ? 412 SER B CB 1 ATOM 2914 O OG . SER A 1 381 ? 46.102 -9.564 -2.099 1.00 96.59 ? 412 SER B OG 1 ATOM 2915 N N . LEU A 1 382 ? 46.184 -12.437 -3.317 1.00 102.25 ? 413 LEU B N 1 ATOM 2916 C CA . LEU A 1 382 ? 46.887 -13.563 -2.715 1.00 99.48 ? 413 LEU B CA 1 ATOM 2917 C C . LEU A 1 382 ? 47.504 -14.496 -3.752 1.00 98.96 ? 413 LEU B C 1 ATOM 2918 O O . LEU A 1 382 ? 48.377 -15.296 -3.412 1.00 96.98 ? 413 LEU B O 1 ATOM 2919 C CB . LEU A 1 382 ? 45.990 -14.330 -1.733 1.00 97.86 ? 413 LEU B CB 1 ATOM 2920 C CG . LEU A 1 382 ? 46.392 -14.182 -0.264 1.00 96.26 ? 413 LEU B CG 1 ATOM 2921 C CD1 . LEU A 1 382 ? 45.425 -14.899 0.660 1.00 94.98 ? 413 LEU B CD1 1 ATOM 2922 C CD2 . LEU A 1 382 ? 47.801 -14.698 -0.067 1.00 94.47 ? 413 LEU B CD2 1 ATOM 2923 N N . THR A 1 383 ? 47.065 -14.391 -5.009 1.00 100.08 ? 414 THR B N 1 ATOM 2924 C CA . THR A 1 383 ? 47.635 -15.225 -6.068 1.00 99.88 ? 414 THR B CA 1 ATOM 2925 C C . THR A 1 383 ? 48.887 -14.566 -6.599 1.00 100.85 ? 414 THR B C 1 ATOM 2926 O O . THR A 1 383 ? 49.597 -15.133 -7.435 1.00 100.80 ? 414 THR B O 1 ATOM 2927 C CB . THR A 1 383 ? 46.677 -15.420 -7.243 1.00 101.58 ? 414 THR B CB 1 ATOM 2928 O OG1 . THR A 1 383 ? 46.098 -14.161 -7.581 1.00 104.16 ? 414 THR B OG1 1 ATOM 2929 C CG2 . THR A 1 383 ? 45.568 -16.393 -6.892 1.00 100.35 ? 414 THR B CG2 1 ATOM 2930 N N . ARG A 1 384 ? 49.131 -13.352 -6.112 1.00 106.54 ? 415 ARG B N 1 ATOM 2931 C CA . ARG A 1 384 ? 50.292 -12.560 -6.489 1.00 107.62 ? 415 ARG B CA 1 ATOM 2932 C C . ARG A 1 384 ? 51.439 -12.729 -5.495 1.00 105.55 ? 415 ARG B C 1 ATOM 2933 O O . ARG A 1 384 ? 52.463 -12.058 -5.606 1.00 106.22 ? 415 ARG B O 1 ATOM 2934 C CB . ARG A 1 384 ? 49.930 -11.070 -6.607 1.00 110.17 ? 415 ARG B CB 1 ATOM 2935 C CG . ARG A 1 384 ? 48.578 -10.784 -7.238 1.00 112.17 ? 415 ARG B CG 1 ATOM 2936 C CD . ARG A 1 384 ? 48.454 -9.335 -7.688 1.00 115.13 ? 415 ARG B CD 1 ATOM 2937 N NE . ARG A 1 384 ? 48.484 -8.378 -6.582 1.00 115.17 ? 415 ARG B NE 1 ATOM 2938 C CZ . ARG A 1 384 ? 47.491 -7.541 -6.288 1.00 116.77 ? 415 ARG B CZ 1 ATOM 2939 N NH1 . ARG A 1 384 ? 46.378 -7.542 -7.021 1.00 118.46 ? 415 ARG B NH1 1 ATOM 2940 N NH2 . ARG A 1 384 ? 47.611 -6.698 -5.263 1.00 116.77 ? 415 ARG B NH2 1 ATOM 2941 N N . CYS A 1 385 ? 51.277 -13.612 -4.519 1.00 92.46 ? 416 CYS B N 1 ATOM 2942 C CA . CYS A 1 385 ? 52.297 -13.758 -3.492 1.00 90.54 ? 416 CYS B CA 1 ATOM 2943 C C . CYS A 1 385 ? 53.294 -14.822 -3.913 1.00 89.22 ? 416 CYS B C 1 ATOM 2944 O O . CYS A 1 385 ? 52.977 -16.001 -3.918 1.00 87.81 ? 416 CYS B O 1 ATOM 2945 C CB . CYS A 1 385 ? 51.637 -14.156 -2.173 1.00 88.72 ? 416 CYS B CB 1 ATOM 2946 S SG . CYS A 1 385 ? 52.721 -14.140 -0.734 1.00 86.61 ? 416 CYS B SG 1 ATOM 2947 N N . GLU A 1 386 ? 54.510 -14.411 -4.242 1.00 98.72 ? 417 GLU B N 1 ATOM 2948 C CA . GLU A 1 386 ? 55.516 -15.341 -4.739 1.00 97.82 ? 417 GLU B CA 1 ATOM 2949 C C . GLU A 1 386 ? 55.918 -16.333 -3.681 1.00 95.11 ? 417 GLU B C 1 ATOM 2950 O O . GLU A 1 386 ? 56.025 -17.536 -3.917 1.00 93.92 ? 417 GLU B O 1 ATOM 2951 C CB . GLU A 1 386 ? 56.764 -14.583 -5.162 1.00 98.99 ? 417 GLU B CB 1 ATOM 2952 C CG . GLU A 1 386 ? 56.891 -14.442 -6.647 1.00 101.17 ? 417 GLU B CG 1 ATOM 2953 C CD . GLU A 1 386 ? 55.596 -13.977 -7.266 1.00 103.00 ? 417 GLU B CD 1 ATOM 2954 O OE1 . GLU A 1 386 ? 55.175 -12.841 -6.943 1.00 104.24 ? 417 GLU B OE1 1 ATOM 2955 O OE2 . GLU A 1 386 ? 54.997 -14.750 -8.058 1.00 103.24 ? 417 GLU B OE2 1 ATOM 2956 N N . SER A 1 387 ? 56.144 -15.797 -2.501 1.00 85.11 ? 418 SER B N 1 ATOM 2957 C CA . SER A 1 387 ? 56.706 -16.554 -1.414 1.00 82.72 ? 418 SER B CA 1 ATOM 2958 C C . SER A 1 387 ? 55.772 -17.640 -0.864 1.00 81.08 ? 418 SER B C 1 ATOM 2959 O O . SER A 1 387 ? 56.229 -18.519 -0.122 1.00 79.12 ? 418 SER B O 1 ATOM 2960 C CB . SER A 1 387 ? 57.100 -15.575 -0.310 1.00 82.49 ? 418 SER B CB 1 ATOM 2961 O OG . SER A 1 387 ? 56.734 -14.249 -0.672 1.00 84.67 ? 418 SER B OG 1 ATOM 2962 N N . LEU A 1 388 ? 54.484 -17.591 -1.228 1.00 81.36 ? 419 LEU B N 1 ATOM 2963 C CA . LEU A 1 388 ? 53.486 -18.497 -0.638 1.00 79.98 ? 419 LEU B CA 1 ATOM 2964 C C . LEU A 1 388 ? 53.859 -19.959 -0.823 1.00 78.38 ? 419 LEU B C 1 ATOM 2965 O O . LEU A 1 388 ? 54.152 -20.411 -1.924 1.00 79.00 ? 419 LEU B O 1 ATOM 2966 C CB . LEU A 1 388 ? 52.061 -18.230 -1.142 1.00 81.39 ? 419 LEU B CB 1 ATOM 2967 C CG . LEU A 1 388 ? 50.925 -18.900 -0.348 1.00 80.22 ? 419 LEU B CG 1 ATOM 2968 C CD1 . LEU A 1 388 ? 50.648 -18.211 0.970 1.00 79.83 ? 419 LEU B CD1 1 ATOM 2969 C CD2 . LEU A 1 388 ? 49.653 -18.948 -1.150 1.00 81.58 ? 419 LEU B CD2 1 ATOM 2970 N N . TRP A 1 389 ? 53.876 -20.660 0.301 1.00 75.93 ? 420 TRP B N 1 ATOM 2971 C CA . TRP A 1 389 ? 54.375 -22.017 0.415 1.00 74.26 ? 420 TRP B CA 1 ATOM 2972 C C . TRP A 1 389 ? 53.367 -22.891 1.154 1.00 73.42 ? 420 TRP B C 1 ATOM 2973 O O . TRP A 1 389 ? 52.969 -23.940 0.667 1.00 73.21 ? 420 TRP B O 1 ATOM 2974 C CB . TRP A 1 389 ? 55.748 -22.037 1.079 1.00 73.25 ? 420 TRP B CB 1 ATOM 2975 C CG . TRP A 1 389 ? 56.125 -23.364 1.560 1.00 72.18 ? 420 TRP B CG 1 ATOM 2976 C CD1 . TRP A 1 389 ? 56.486 -24.432 0.804 1.00 71.99 ? 420 TRP B CD1 1 ATOM 2977 C CD2 . TRP A 1 389 ? 56.172 -23.792 2.922 1.00 71.76 ? 420 TRP B CD2 1 ATOM 2978 N NE1 . TRP A 1 389 ? 56.754 -25.511 1.614 1.00 71.58 ? 420 TRP B NE1 1 ATOM 2979 C CE2 . TRP A 1 389 ? 56.566 -25.141 2.921 1.00 71.55 ? 420 TRP B CE2 1 ATOM 2980 C CE3 . TRP A 1 389 ? 55.919 -23.166 4.141 1.00 71.81 ? 420 TRP B CE3 1 ATOM 2981 C CZ2 . TRP A 1 389 ? 56.712 -25.877 4.099 1.00 71.34 ? 420 TRP B CZ2 1 ATOM 2982 C CZ3 . TRP A 1 389 ? 56.060 -23.901 5.302 1.00 71.62 ? 420 TRP B CZ3 1 ATOM 2983 C CH2 . TRP A 1 389 ? 56.456 -25.237 5.274 1.00 71.39 ? 420 TRP B CH2 1 ATOM 2984 N N . ARG A 1 390 ? 53.025 -22.500 2.372 1.00 71.54 ? 421 ARG B N 1 ATOM 2985 C CA . ARG A 1 390 ? 52.008 -23.201 3.141 1.00 70.51 ? 421 ARG B CA 1 ATOM 2986 C C . ARG A 1 390 ? 50.802 -22.303 3.344 1.00 71.75 ? 421 ARG B C 1 ATOM 2987 O O . ARG A 1 390 ? 50.937 -21.211 3.886 1.00 72.37 ? 421 ARG B O 1 ATOM 2988 C CB . ARG A 1 390 ? 52.569 -23.559 4.515 1.00 68.75 ? 421 ARG B CB 1 ATOM 2989 C CG . ARG A 1 390 ? 52.514 -25.030 4.880 1.00 67.33 ? 421 ARG B CG 1 ATOM 2990 C CD . ARG A 1 390 ? 52.317 -25.205 6.369 1.00 67.00 ? 421 ARG B CD 1 ATOM 2991 N NE . ARG A 1 390 ? 51.455 -26.343 6.650 1.00 67.30 ? 421 ARG B NE 1 ATOM 2992 C CZ . ARG A 1 390 ? 51.557 -27.080 7.741 1.00 67.01 ? 421 ARG B CZ 1 ATOM 2993 N NH1 . ARG A 1 390 ? 52.482 -26.774 8.636 1.00 66.41 ? 421 ARG B NH1 1 ATOM 2994 N NH2 . ARG A 1 390 ? 50.743 -28.107 7.940 1.00 67.36 ? 421 ARG B NH2 1 ATOM 2995 N N . PHE A 1 391 ? 49.626 -22.747 2.916 1.00 75.17 ? 422 PHE B N 1 ATOM 2996 C CA . PHE A 1 391 ? 48.394 -21.987 3.143 1.00 76.05 ? 422 PHE B CA 1 ATOM 2997 C C . PHE A 1 391 ? 47.241 -22.911 3.566 1.00 76.74 ? 422 PHE B C 1 ATOM 2998 O O . PHE A 1 391 ? 46.812 -23.798 2.812 1.00 76.82 ? 422 PHE B O 1 ATOM 2999 C CB . PHE A 1 391 ? 48.056 -21.150 1.891 1.00 76.84 ? 422 PHE B CB 1 ATOM 3000 C CG . PHE A 1 391 ? 46.799 -20.300 2.002 1.00 78.34 ? 422 PHE B CG 1 ATOM 3001 C CD1 . PHE A 1 391 ? 46.191 -20.044 3.211 1.00 78.09 ? 422 PHE B CD1 1 ATOM 3002 C CD2 . PHE A 1 391 ? 46.227 -19.759 0.866 1.00 80.23 ? 422 PHE B CD2 1 ATOM 3003 C CE1 . PHE A 1 391 ? 45.035 -19.282 3.277 1.00 79.61 ? 422 PHE B CE1 1 ATOM 3004 C CE2 . PHE A 1 391 ? 45.073 -18.992 0.933 1.00 81.82 ? 422 PHE B CE2 1 ATOM 3005 C CZ . PHE A 1 391 ? 44.480 -18.757 2.135 1.00 81.42 ? 422 PHE B CZ 1 ATOM 3006 N N . ARG A 1 392 ? 46.721 -22.698 4.772 1.00 76.24 ? 423 ARG B N 1 ATOM 3007 C CA . ARG A 1 392 ? 45.589 -23.509 5.218 1.00 77.04 ? 423 ARG B CA 1 ATOM 3008 C C . ARG A 1 392 ? 44.427 -22.630 5.694 1.00 78.11 ? 423 ARG B C 1 ATOM 3009 O O . ARG A 1 392 ? 44.510 -21.990 6.746 1.00 78.34 ? 423 ARG B O 1 ATOM 3010 C CB . ARG A 1 392 ? 46.046 -24.453 6.337 1.00 76.98 ? 423 ARG B CB 1 ATOM 3011 C CG . ARG A 1 392 ? 47.383 -25.158 6.066 1.00 75.87 ? 423 ARG B CG 1 ATOM 3012 C CD . ARG A 1 392 ? 47.903 -25.866 7.301 1.00 75.72 ? 423 ARG B CD 1 ATOM 3013 N NE . ARG A 1 392 ? 47.010 -26.946 7.687 1.00 76.46 ? 423 ARG B NE 1 ATOM 3014 C CZ . ARG A 1 392 ? 46.913 -27.431 8.917 1.00 76.78 ? 423 ARG B CZ 1 ATOM 3015 N NH1 . ARG A 1 392 ? 47.655 -26.928 9.896 1.00 76.37 ? 423 ARG B NH1 1 ATOM 3016 N NH2 . ARG A 1 392 ? 46.065 -28.418 9.161 1.00 77.52 ? 423 ARG B NH2 1 ATOM 3017 N N . SER A 1 393 ? 43.363 -22.591 4.889 1.00 75.89 ? 424 SER B N 1 ATOM 3018 C CA . SER A 1 393 ? 42.142 -21.817 5.170 1.00 77.15 ? 424 SER B CA 1 ATOM 3019 C C . SER A 1 393 ? 40.870 -22.556 5.631 1.00 78.43 ? 424 SER B C 1 ATOM 3020 O O . SER A 1 393 ? 39.794 -21.963 5.663 1.00 79.50 ? 424 SER B O 1 ATOM 3021 C CB . SER A 1 393 ? 41.822 -20.847 4.046 1.00 78.14 ? 424 SER B CB 1 ATOM 3022 O OG . SER A 1 393 ? 40.999 -19.820 4.549 1.00 79.67 ? 424 SER B OG 1 ATOM 3023 N N . GLN A 1 394 ? 40.985 -23.849 5.919 1.00 74.55 ? 425 GLN B N 1 ATOM 3024 C CA . GLN A 1 394 ? 39.827 -24.702 6.204 1.00 74.92 ? 425 GLN B CA 1 ATOM 3025 C C . GLN A 1 394 ? 38.865 -24.229 7.302 1.00 75.96 ? 425 GLN B C 1 ATOM 3026 O O . GLN A 1 394 ? 39.252 -23.544 8.248 1.00 75.97 ? 425 GLN B O 1 ATOM 3027 C CB . GLN A 1 394 ? 40.276 -26.121 6.535 1.00 73.57 ? 425 GLN B CB 1 ATOM 3028 C CG . GLN A 1 394 ? 41.045 -26.252 7.840 1.00 72.69 ? 425 GLN B CG 1 ATOM 3029 C CD . GLN A 1 394 ? 42.528 -26.292 7.610 1.00 71.42 ? 425 GLN B CD 1 ATOM 3030 O OE1 . GLN A 1 394 ? 43.070 -25.425 6.943 1.00 71.60 ? 425 GLN B OE1 1 ATOM 3031 N NE2 . GLN A 1 394 ? 43.193 -27.316 8.135 1.00 70.19 ? 425 GLN B NE2 1 ATOM 3032 N N . ASN A 1 395 ? 37.601 -24.620 7.143 1.00 79.33 ? 426 ASN B N 1 ATOM 3033 C CA . ASN A 1 395 ? 36.494 -24.273 8.047 1.00 80.90 ? 426 ASN B CA 1 ATOM 3034 C C . ASN A 1 395 ? 36.079 -22.804 8.150 1.00 81.31 ? 426 ASN B C 1 ATOM 3035 O O . ASN A 1 395 ? 35.925 -22.284 9.240 1.00 81.92 ? 426 ASN B O 1 ATOM 3036 C CB . ASN A 1 395 ? 36.748 -24.830 9.449 1.00 81.24 ? 426 ASN B CB 1 ATOM 3037 C CG . ASN A 1 395 ? 37.167 -26.275 9.428 1.00 80.73 ? 426 ASN B CG 1 ATOM 3038 O OD1 . ASN A 1 395 ? 36.348 -27.172 9.223 1.00 81.56 ? 426 ASN B OD1 1 ATOM 3039 N ND2 . ASN A 1 395 ? 38.453 -26.513 9.645 1.00 79.35 ? 426 ASN B ND2 1 ATOM 3040 N N . ASN A 1 396 ? 35.872 -22.148 7.019 1.00 84.43 ? 427 ASN B N 1 ATOM 3041 C CA . ASN A 1 396 ? 35.440 -20.764 7.037 1.00 85.01 ? 427 ASN B CA 1 ATOM 3042 C C . ASN A 1 396 ? 34.251 -20.511 6.135 1.00 86.06 ? 427 ASN B C 1 ATOM 3043 O O . ASN A 1 396 ? 33.715 -21.433 5.540 1.00 86.33 ? 427 ASN B O 1 ATOM 3044 C CB . ASN A 1 396 ? 36.593 -19.852 6.640 1.00 83.76 ? 427 ASN B CB 1 ATOM 3045 C CG . ASN A 1 396 ? 37.694 -19.811 7.691 1.00 82.78 ? 427 ASN B CG 1 ATOM 3046 O OD1 . ASN A 1 396 ? 37.870 -18.801 8.386 1.00 82.72 ? 427 ASN B OD1 1 ATOM 3047 N ND2 . ASN A 1 396 ? 38.439 -20.911 7.814 1.00 82.00 ? 427 ASN B ND2 1 ATOM 3048 N N . ARG A 1 397 ? 33.822 -19.258 6.073 1.00 103.03 ? 428 ARG B N 1 ATOM 3049 C CA . ARG A 1 397 ? 32.716 -18.843 5.213 1.00 104.03 ? 428 ARG B CA 1 ATOM 3050 C C . ARG A 1 397 ? 33.097 -18.216 3.871 1.00 104.19 ? 428 ARG B C 1 ATOM 3051 O O . ARG A 1 397 ? 32.243 -17.625 3.215 1.00 106.18 ? 428 ARG B O 1 ATOM 3052 C CB . ARG A 1 397 ? 31.724 -17.972 5.973 1.00 105.41 ? 428 ARG B CB 1 ATOM 3053 C CG . ARG A 1 397 ? 31.139 -18.698 7.149 1.00 106.55 ? 428 ARG B CG 1 ATOM 3054 C CD . ARG A 1 397 ? 30.074 -17.890 7.825 1.00 107.98 ? 428 ARG B CD 1 ATOM 3055 N NE . ARG A 1 397 ? 29.629 -18.562 9.037 1.00 109.04 ? 428 ARG B NE 1 ATOM 3056 C CZ . ARG A 1 397 ? 28.589 -18.178 9.764 1.00 110.57 ? 428 ARG B CZ 1 ATOM 3057 N NH1 . ARG A 1 397 ? 27.873 -17.120 9.399 1.00 111.17 ? 428 ARG B NH1 1 ATOM 3058 N NH2 . ARG A 1 397 ? 28.265 -18.857 10.855 1.00 111.56 ? 428 ARG B NH2 1 ATOM 3059 N N . LEU A 1 398 ? 34.378 -18.274 3.506 1.00 97.37 ? 429 LEU B N 1 ATOM 3060 C CA . LEU A 1 398 ? 34.869 -17.674 2.255 1.00 98.31 ? 429 LEU B CA 1 ATOM 3061 C C . LEU A 1 398 ? 34.040 -18.099 1.038 1.00 99.39 ? 429 LEU B C 1 ATOM 3062 O O . LEU A 1 398 ? 33.753 -19.282 0.873 1.00 98.25 ? 429 LEU B O 1 ATOM 3063 C CB . LEU A 1 398 ? 36.334 -18.052 2.031 1.00 96.57 ? 429 LEU B CB 1 ATOM 3064 C CG . LEU A 1 398 ? 37.257 -18.032 3.255 1.00 94.99 ? 429 LEU B CG 1 ATOM 3065 C CD1 . LEU A 1 398 ? 38.687 -18.364 2.879 1.00 93.64 ? 429 LEU B CD1 1 ATOM 3066 C CD2 . LEU A 1 398 ? 37.214 -16.687 3.932 1.00 96.17 ? 429 LEU B CD2 1 ATOM 3067 N N . ASN A 1 399 ? 33.659 -17.145 0.188 1.00 100.43 ? 430 ASN B N 1 ATOM 3068 C CA . ASN A 1 399 ? 32.669 -17.421 -0.866 1.00 101.88 ? 430 ASN B CA 1 ATOM 3069 C C . ASN A 1 399 ? 33.110 -17.200 -2.316 1.00 103.04 ? 430 ASN B C 1 ATOM 3070 O O . ASN A 1 399 ? 34.282 -16.956 -2.605 1.00 102.54 ? 430 ASN B O 1 ATOM 3071 C CB . ASN A 1 399 ? 31.341 -16.684 -0.590 1.00 104.16 ? 430 ASN B CB 1 ATOM 3072 C CG . ASN A 1 399 ? 31.439 -15.172 -0.794 1.00 106.61 ? 430 ASN B CG 1 ATOM 3073 O OD1 . ASN A 1 399 ? 32.526 -14.615 -0.808 1.00 106.34 ? 430 ASN B OD1 1 ATOM 3074 N ND2 . ASN A 1 399 ? 30.290 -14.507 -0.951 1.00 109.09 ? 430 ASN B ND2 1 ATOM 3075 N N . GLY A 1 400 ? 32.152 -17.333 -3.226 1.00 129.09 ? 431 GLY B N 1 ATOM 3076 C CA . GLY A 1 400 ? 32.354 -16.960 -4.610 1.00 130.77 ? 431 GLY B CA 1 ATOM 3077 C C . GLY A 1 400 ? 33.350 -17.842 -5.320 1.00 129.15 ? 431 GLY B C 1 ATOM 3078 O O . GLY A 1 400 ? 33.772 -18.866 -4.793 1.00 126.69 ? 431 GLY B O 1 ATOM 3079 N N . THR A 1 401 ? 33.721 -17.438 -6.527 1.00 106.73 ? 432 THR B N 1 ATOM 3080 C CA . THR A 1 401 ? 34.694 -18.173 -7.313 1.00 105.58 ? 432 THR B CA 1 ATOM 3081 C C . THR A 1 401 ? 36.042 -18.098 -6.634 1.00 103.83 ? 432 THR B C 1 ATOM 3082 O O . THR A 1 401 ? 36.317 -17.173 -5.868 1.00 104.18 ? 432 THR B O 1 ATOM 3083 C CB . THR A 1 401 ? 34.848 -17.579 -8.719 1.00 107.92 ? 432 THR B CB 1 ATOM 3084 O OG1 . THR A 1 401 ? 33.558 -17.252 -9.255 1.00 110.15 ? 432 THR B OG1 1 ATOM 3085 C CG2 . THR A 1 401 ? 35.545 -18.566 -9.646 1.00 106.90 ? 432 THR B CG2 1 ATOM 3086 N N . ILE A 1 402 ? 36.882 -19.083 -6.914 1.00 103.51 ? 433 ILE B N 1 ATOM 3087 C CA . ILE A 1 402 ? 38.236 -19.092 -6.393 1.00 101.89 ? 433 ILE B CA 1 ATOM 3088 C C . ILE A 1 402 ? 39.163 -18.369 -7.356 1.00 103.34 ? 433 ILE B C 1 ATOM 3089 O O . ILE A 1 402 ? 39.068 -18.564 -8.565 1.00 104.52 ? 433 ILE B O 1 ATOM 3090 C CB . ILE A 1 402 ? 38.735 -20.532 -6.165 1.00 99.26 ? 433 ILE B CB 1 ATOM 3091 C CG1 . ILE A 1 402 ? 37.938 -21.185 -5.039 1.00 97.78 ? 433 ILE B CG1 1 ATOM 3092 C CG2 . ILE A 1 402 ? 40.211 -20.543 -5.837 1.00 97.87 ? 433 ILE B CG2 1 ATOM 3093 C CD1 . ILE A 1 402 ? 38.595 -22.388 -4.464 1.00 95.11 ? 433 ILE B CD1 1 ATOM 3094 N N . PRO A 1 403 ? 40.030 -17.496 -6.823 1.00 102.53 ? 434 PRO B N 1 ATOM 3095 C CA . PRO A 1 403 ? 41.089 -16.805 -7.570 1.00 103.68 ? 434 PRO B CA 1 ATOM 3096 C C . PRO A 1 403 ? 42.007 -17.714 -8.403 1.00 102.75 ? 434 PRO B C 1 ATOM 3097 O O . PRO A 1 403 ? 42.344 -18.845 -8.031 1.00 100.49 ? 434 PRO B O 1 ATOM 3098 C CB . PRO A 1 403 ? 41.848 -16.069 -6.475 1.00 102.97 ? 434 PRO B CB 1 ATOM 3099 C CG . PRO A 1 403 ? 40.756 -15.690 -5.523 1.00 103.21 ? 434 PRO B CG 1 ATOM 3100 C CD . PRO A 1 403 ? 39.794 -16.859 -5.516 1.00 102.17 ? 434 PRO B CD 1 ATOM 3101 N N . ILE A 1 404 ? 42.379 -17.175 -9.559 1.00 107.82 ? 435 ILE B N 1 ATOM 3102 C CA . ILE A 1 404 ? 42.872 -17.954 -10.693 1.00 107.86 ? 435 ILE B CA 1 ATOM 3103 C C . ILE A 1 404 ? 44.394 -18.017 -10.913 1.00 107.24 ? 435 ILE B C 1 ATOM 3104 O O . ILE A 1 404 ? 44.849 -18.567 -11.914 1.00 107.59 ? 435 ILE B O 1 ATOM 3105 C CB . ILE A 1 404 ? 42.159 -17.511 -12.008 1.00 110.65 ? 435 ILE B CB 1 ATOM 3106 C CG1 . ILE A 1 404 ? 40.860 -16.747 -11.696 1.00 112.19 ? 435 ILE B CG1 1 ATOM 3107 C CG2 . ILE A 1 404 ? 41.872 -18.721 -12.896 1.00 110.22 ? 435 ILE B CG2 1 ATOM 3108 C CD1 . ILE A 1 404 ? 40.946 -15.232 -11.851 1.00 114.69 ? 435 ILE B CD1 1 ATOM 3109 N N . GLY A 1 405 ? 45.184 -17.437 -10.020 1.00 110.87 ? 436 GLY B N 1 ATOM 3110 C CA . GLY A 1 405 ? 46.592 -17.249 -10.329 1.00 110.85 ? 436 GLY B CA 1 ATOM 3111 C C . GLY A 1 405 ? 47.588 -18.126 -9.607 1.00 108.23 ? 436 GLY B C 1 ATOM 3112 O O . GLY A 1 405 ? 48.790 -17.866 -9.622 1.00 108.11 ? 436 GLY B O 1 ATOM 3113 N N . PHE A 1 406 ? 47.092 -19.178 -8.983 1.00 94.29 ? 437 PHE B N 1 ATOM 3114 C CA . PHE A 1 406 ? 47.900 -19.943 -8.041 1.00 91.75 ? 437 PHE B CA 1 ATOM 3115 C C . PHE A 1 406 ? 49.058 -20.744 -8.644 1.00 91.06 ? 437 PHE B C 1 ATOM 3116 O O . PHE A 1 406 ? 50.014 -21.087 -7.940 1.00 89.40 ? 437 PHE B O 1 ATOM 3117 C CB . PHE A 1 406 ? 46.995 -20.865 -7.226 1.00 89.97 ? 437 PHE B CB 1 ATOM 3118 C CG . PHE A 1 406 ? 46.221 -20.156 -6.149 1.00 89.95 ? 437 PHE B CG 1 ATOM 3119 C CD1 . PHE A 1 406 ? 46.867 -19.306 -5.258 1.00 89.69 ? 437 PHE B CD1 1 ATOM 3120 C CD2 . PHE A 1 406 ? 44.849 -20.334 -6.030 1.00 90.28 ? 437 PHE B CD2 1 ATOM 3121 C CE1 . PHE A 1 406 ? 46.160 -18.649 -4.261 1.00 89.78 ? 437 PHE B CE1 1 ATOM 3122 C CE2 . PHE A 1 406 ? 44.133 -19.682 -5.035 1.00 90.41 ? 437 PHE B CE2 1 ATOM 3123 C CZ . PHE A 1 406 ? 44.790 -18.837 -4.151 1.00 90.17 ? 437 PHE B CZ 1 ATOM 3124 N N . GLY A 1 407 ? 48.968 -21.035 -9.940 1.00 103.71 ? 438 GLY B N 1 ATOM 3125 C CA . GLY A 1 407 ? 49.899 -21.937 -10.601 1.00 103.17 ? 438 GLY B CA 1 ATOM 3126 C C . GLY A 1 407 ? 51.227 -21.308 -10.963 1.00 104.08 ? 438 GLY B C 1 ATOM 3127 O O . GLY A 1 407 ? 52.147 -21.988 -11.422 1.00 103.69 ? 438 GLY B O 1 ATOM 3128 N N . SER A 1 408 ? 51.309 -19.998 -10.750 1.00 90.20 ? 439 SER B N 1 ATOM 3129 C CA . SER A 1 408 ? 52.526 -19.222 -10.973 1.00 91.18 ? 439 SER B CA 1 ATOM 3130 C C . SER A 1 408 ? 53.690 -19.558 -10.022 1.00 89.14 ? 439 SER B C 1 ATOM 3131 O O . SER A 1 408 ? 54.856 -19.523 -10.430 1.00 89.53 ? 439 SER B O 1 ATOM 3132 C CB . SER A 1 408 ? 52.210 -17.725 -10.857 1.00 93.03 ? 439 SER B CB 1 ATOM 3133 O OG . SER A 1 408 ? 53.381 -16.926 -10.976 1.00 93.95 ? 439 SER B OG 1 ATOM 3134 N N . LEU A 1 409 ? 53.366 -19.901 -8.772 1.00 88.57 ? 440 LEU B N 1 ATOM 3135 C CA . LEU A 1 409 ? 54.311 -19.854 -7.648 1.00 86.89 ? 440 LEU B CA 1 ATOM 3136 C C . LEU A 1 409 ? 55.253 -21.056 -7.548 1.00 85.17 ? 440 LEU B C 1 ATOM 3137 O O . LEU A 1 409 ? 54.803 -22.190 -7.389 1.00 83.78 ? 440 LEU B O 1 ATOM 3138 C CB . LEU A 1 409 ? 53.511 -19.692 -6.354 1.00 85.61 ? 440 LEU B CB 1 ATOM 3139 C CG . LEU A 1 409 ? 52.192 -18.937 -6.595 1.00 87.22 ? 440 LEU B CG 1 ATOM 3140 C CD1 . LEU A 1 409 ? 51.215 -19.077 -5.454 1.00 85.96 ? 440 LEU B CD1 1 ATOM 3141 C CD2 . LEU A 1 409 ? 52.447 -17.473 -6.854 1.00 89.31 ? 440 LEU B CD2 1 ATOM 3142 N N . ARG A 1 410 ? 56.559 -20.800 -7.619 1.00 93.40 ? 441 ARG B N 1 ATOM 3143 C CA . ARG A 1 410 ? 57.553 -21.873 -7.617 1.00 92.09 ? 441 ARG B CA 1 ATOM 3144 C C . ARG A 1 410 ? 57.749 -22.492 -6.236 1.00 89.59 ? 441 ARG B C 1 ATOM 3145 O O . ARG A 1 410 ? 58.345 -23.563 -6.109 1.00 88.30 ? 441 ARG B O 1 ATOM 3146 C CB . ARG A 1 410 ? 58.915 -21.387 -8.128 1.00 93.21 ? 441 ARG B CB 1 ATOM 3147 C CG . ARG A 1 410 ? 58.987 -20.978 -9.593 1.00 95.74 ? 441 ARG B CG 1 ATOM 3148 C CD . ARG A 1 410 ? 58.653 -19.495 -9.763 1.00 97.70 ? 441 ARG B CD 1 ATOM 3149 N NE . ARG A 1 410 ? 59.241 -18.857 -10.953 1.00 100.20 ? 441 ARG B NE 1 ATOM 3150 C CZ . ARG A 1 410 ? 58.657 -18.792 -12.154 1.00 102.15 ? 441 ARG B CZ 1 ATOM 3151 N NH1 . ARG A 1 410 ? 57.466 -19.349 -12.347 1.00 101.85 ? 441 ARG B NH1 1 ATOM 3152 N NH2 . ARG A 1 410 ? 59.267 -18.177 -13.168 1.00 104.46 ? 441 ARG B NH2 1 ATOM 3153 N N . ASN A 1 411 ? 57.327 -21.785 -5.196 1.00 85.20 ? 442 ASN B N 1 ATOM 3154 C CA . ASN A 1 411 ? 57.531 -22.279 -3.844 1.00 82.98 ? 442 ASN B CA 1 ATOM 3155 C C . ASN A 1 411 ? 56.355 -22.926 -3.090 1.00 81.62 ? 442 ASN B C 1 ATOM 3156 O O . ASN A 1 411 ? 56.535 -23.370 -1.954 1.00 79.85 ? 442 ASN B O 1 ATOM 3157 C CB . ASN A 1 411 ? 58.238 -21.223 -2.990 1.00 82.94 ? 442 ASN B CB 1 ATOM 3158 C CG . ASN A 1 411 ? 59.751 -21.237 -3.179 1.00 82.97 ? 442 ASN B CG 1 ATOM 3159 O OD1 . ASN A 1 411 ? 60.302 -22.200 -3.709 1.00 82.62 ? 442 ASN B OD1 1 ATOM 3160 N ND2 . ASN A 1 411 ? 60.428 -20.172 -2.731 1.00 83.47 ? 442 ASN B ND2 1 ATOM 3161 N N . LEU A 1 412 ? 55.178 -23.034 -3.709 1.00 76.78 ? 443 LEU B N 1 ATOM 3162 C CA . LEU A 1 412 ? 53.960 -23.347 -2.937 1.00 75.85 ? 443 LEU B CA 1 ATOM 3163 C C . LEU A 1 412 ? 53.674 -24.836 -2.795 1.00 74.25 ? 443 LEU B C 1 ATOM 3164 O O . LEU A 1 412 ? 53.232 -25.466 -3.744 1.00 74.78 ? 443 LEU B O 1 ATOM 3165 C CB . LEU A 1 412 ? 52.756 -22.696 -3.635 1.00 77.64 ? 443 LEU B CB 1 ATOM 3166 C CG . LEU A 1 412 ? 51.310 -23.127 -3.359 1.00 77.31 ? 443 LEU B CG 1 ATOM 3167 C CD1 . LEU A 1 412 ? 50.792 -22.577 -2.064 1.00 76.69 ? 443 LEU B CD1 1 ATOM 3168 C CD2 . LEU A 1 412 ? 50.435 -22.660 -4.485 1.00 79.38 ? 443 LEU B CD2 1 ATOM 3169 N N . THR A 1 413 ? 53.908 -25.397 -1.609 1.00 72.37 ? 444 THR B N 1 ATOM 3170 C CA . THR A 1 413 ? 53.680 -26.828 -1.431 1.00 70.90 ? 444 THR B CA 1 ATOM 3171 C C . THR A 1 413 ? 52.461 -27.378 -0.648 1.00 69.91 ? 444 THR B C 1 ATOM 3172 O O . THR A 1 413 ? 52.242 -28.579 -0.654 1.00 68.91 ? 444 THR B O 1 ATOM 3173 C CB . THR A 1 413 ? 54.973 -27.542 -0.969 1.00 69.53 ? 444 THR B CB 1 ATOM 3174 O OG1 . THR A 1 413 ? 55.171 -27.348 0.434 1.00 68.26 ? 444 THR B OG1 1 ATOM 3175 C CG2 . THR A 1 413 ? 56.171 -27.009 -1.730 1.00 70.60 ? 444 THR B CG2 1 ATOM 3176 N N . PHE A 1 414 ? 51.677 -26.552 0.029 1.00 72.66 ? 445 PHE B N 1 ATOM 3177 C CA . PHE A 1 414 ? 50.579 -27.101 0.836 1.00 73.19 ? 445 PHE B CA 1 ATOM 3178 C C . PHE A 1 414 ? 49.342 -26.209 0.816 1.00 73.95 ? 445 PHE B C 1 ATOM 3179 O O . PHE A 1 414 ? 49.433 -25.081 1.278 1.00 73.99 ? 445 PHE B O 1 ATOM 3180 C CB . PHE A 1 414 ? 51.070 -27.238 2.275 1.00 73.09 ? 445 PHE B CB 1 ATOM 3181 C CG . PHE A 1 414 ? 50.279 -28.206 3.122 1.00 73.48 ? 445 PHE B CG 1 ATOM 3182 C CD1 . PHE A 1 414 ? 48.979 -27.918 3.514 1.00 74.33 ? 445 PHE B CD1 1 ATOM 3183 C CD2 . PHE A 1 414 ? 50.865 -29.380 3.575 1.00 73.11 ? 445 PHE B CD2 1 ATOM 3184 C CE1 . PHE A 1 414 ? 48.269 -28.794 4.307 1.00 74.89 ? 445 PHE B CE1 1 ATOM 3185 C CE2 . PHE A 1 414 ? 50.161 -30.256 4.361 1.00 73.58 ? 445 PHE B CE2 1 ATOM 3186 C CZ . PHE A 1 414 ? 48.860 -29.964 4.729 1.00 74.50 ? 445 PHE B CZ 1 ATOM 3187 N N . VAL A 1 415 ? 48.184 -26.708 0.363 1.00 71.05 ? 446 VAL B N 1 ATOM 3188 C CA . VAL A 1 415 ? 46.941 -25.894 0.303 1.00 72.46 ? 446 VAL B CA 1 ATOM 3189 C C . VAL A 1 415 ? 45.659 -26.574 0.799 1.00 71.96 ? 446 VAL B C 1 ATOM 3190 O O . VAL A 1 415 ? 45.232 -27.585 0.241 1.00 71.63 ? 446 VAL B O 1 ATOM 3191 C CB . VAL A 1 415 ? 46.623 -25.381 -1.116 1.00 74.45 ? 446 VAL B CB 1 ATOM 3192 C CG1 . VAL A 1 415 ? 45.338 -24.569 -1.088 1.00 75.93 ? 446 VAL B CG1 1 ATOM 3193 C CG2 . VAL A 1 415 ? 47.763 -24.559 -1.661 1.00 75.34 ? 446 VAL B CG2 1 ATOM 3194 N N . ASP A 1 416 ? 45.032 -26.010 1.830 1.00 74.27 ? 447 ASP B N 1 ATOM 3195 C CA . ASP A 1 416 ? 43.745 -26.540 2.285 1.00 75.30 ? 447 ASP B CA 1 ATOM 3196 C C . ASP A 1 416 ? 42.641 -25.482 2.253 1.00 76.24 ? 447 ASP B C 1 ATOM 3197 O O . ASP A 1 416 ? 42.599 -24.596 3.099 1.00 76.54 ? 447 ASP B O 1 ATOM 3198 C CB . ASP A 1 416 ? 43.894 -27.095 3.706 1.00 75.57 ? 447 ASP B CB 1 ATOM 3199 C CG . ASP A 1 416 ? 42.665 -27.851 4.185 1.00 76.76 ? 447 ASP B CG 1 ATOM 3200 O OD1 . ASP A 1 416 ? 41.524 -27.434 3.894 1.00 77.66 ? 447 ASP B OD1 1 ATOM 3201 O OD2 . ASP A 1 416 ? 42.848 -28.874 4.880 1.00 76.83 ? 447 ASP B OD2 1 ATOM 3202 N N . LEU A 1 417 ? 41.736 -25.604 1.291 1.00 75.80 ? 448 LEU B N 1 ATOM 3203 C CA . LEU A 1 417 ? 40.530 -24.781 1.209 1.00 76.89 ? 448 LEU B CA 1 ATOM 3204 C C . LEU A 1 417 ? 39.237 -25.444 1.687 1.00 78.03 ? 448 LEU B C 1 ATOM 3205 O O . LEU A 1 417 ? 38.150 -24.903 1.497 1.00 79.04 ? 448 LEU B O 1 ATOM 3206 C CB . LEU A 1 417 ? 40.378 -24.205 -0.184 1.00 78.52 ? 448 LEU B CB 1 ATOM 3207 C CG . LEU A 1 417 ? 41.448 -23.137 -0.373 1.00 79.23 ? 448 LEU B CG 1 ATOM 3208 C CD1 . LEU A 1 417 ? 41.522 -22.686 -1.807 1.00 81.02 ? 448 LEU B CD1 1 ATOM 3209 C CD2 . LEU A 1 417 ? 41.140 -21.962 0.525 1.00 80.09 ? 448 LEU B CD2 1 ATOM 3210 N N . SER A 1 418 ? 39.362 -26.638 2.252 1.00 79.04 ? 449 SER B N 1 ATOM 3211 C CA . SER A 1 418 ? 38.215 -27.462 2.629 1.00 80.35 ? 449 SER B CA 1 ATOM 3212 C C . SER A 1 418 ? 37.221 -26.796 3.570 1.00 81.87 ? 449 SER B C 1 ATOM 3213 O O . SER A 1 418 ? 37.602 -26.049 4.461 1.00 81.86 ? 449 SER B O 1 ATOM 3214 C CB . SER A 1 418 ? 38.696 -28.760 3.269 1.00 80.11 ? 449 SER B CB 1 ATOM 3215 O OG . SER A 1 418 ? 39.418 -28.518 4.464 1.00 79.99 ? 449 SER B OG 1 ATOM 3216 N N . ASN A 1 419 ? 35.946 -27.116 3.379 1.00 91.38 ? 450 ASN B N 1 ATOM 3217 C CA . ASN A 1 419 ? 34.853 -26.560 4.171 1.00 93.14 ? 450 ASN B CA 1 ATOM 3218 C C . ASN A 1 419 ? 34.744 -25.051 4.078 1.00 93.24 ? 450 ASN B C 1 ATOM 3219 O O . ASN A 1 419 ? 34.961 -24.335 5.044 1.00 93.58 ? 450 ASN B O 1 ATOM 3220 C CB . ASN A 1 419 ? 34.945 -26.986 5.637 1.00 93.69 ? 450 ASN B CB 1 ATOM 3221 C CG . ASN A 1 419 ? 33.739 -26.548 6.444 1.00 95.76 ? 450 ASN B CG 1 ATOM 3222 O OD1 . ASN A 1 419 ? 32.706 -26.175 5.889 1.00 96.71 ? 450 ASN B OD1 1 ATOM 3223 N ND2 . ASN A 1 419 ? 33.865 -26.590 7.760 1.00 96.45 ? 450 ASN B ND2 1 ATOM 3224 N N . ASN A 1 420 ? 34.397 -24.567 2.902 1.00 96.57 ? 451 ASN B N 1 ATOM 3225 C CA . ASN A 1 420 ? 34.109 -23.164 2.751 1.00 96.80 ? 451 ASN B CA 1 ATOM 3226 C C . ASN A 1 420 ? 32.881 -23.017 1.881 1.00 97.70 ? 451 ASN B C 1 ATOM 3227 O O . ASN A 1 420 ? 32.255 -24.000 1.519 1.00 98.08 ? 451 ASN B O 1 ATOM 3228 C CB . ASN A 1 420 ? 35.311 -22.430 2.157 1.00 95.31 ? 451 ASN B CB 1 ATOM 3229 C CG . ASN A 1 420 ? 36.513 -22.414 3.095 1.00 94.55 ? 451 ASN B CG 1 ATOM 3230 O OD1 . ASN A 1 420 ? 36.605 -21.581 3.994 1.00 94.59 ? 451 ASN B OD1 1 ATOM 3231 N ND2 . ASN A 1 420 ? 37.441 -23.329 2.879 1.00 93.85 ? 451 ASN B ND2 1 ATOM 3232 N N . ARG A 1 421 ? 32.508 -21.787 1.584 1.00 95.15 ? 452 ARG B N 1 ATOM 3233 C CA . ARG A 1 421 ? 31.402 -21.526 0.674 1.00 96.01 ? 452 ARG B CA 1 ATOM 3234 C C . ARG A 1 421 ? 31.820 -21.243 -0.783 1.00 96.61 ? 452 ARG B C 1 ATOM 3235 O O . ARG A 1 421 ? 31.032 -20.703 -1.557 1.00 98.52 ? 452 ARG B O 1 ATOM 3236 C CB . ARG A 1 421 ? 30.405 -20.524 1.265 1.00 97.81 ? 452 ARG B CB 1 ATOM 3237 C CG . ARG A 1 421 ? 29.639 -21.111 2.466 1.00 98.76 ? 452 ARG B CG 1 ATOM 3238 C CD . ARG A 1 421 ? 28.826 -20.056 3.224 1.00 99.97 ? 452 ARG B CD 1 ATOM 3239 N NE . ARG A 1 421 ? 28.499 -20.477 4.592 1.00 101.00 ? 452 ARG B NE 1 ATOM 3240 C CZ . ARG A 1 421 ? 28.099 -19.654 5.565 1.00 101.95 ? 452 ARG B CZ 1 ATOM 3241 N NH1 . ARG A 1 421 ? 27.972 -18.351 5.339 1.00 101.99 ? 452 ARG B NH1 1 ATOM 3242 N NH2 . ARG A 1 421 ? 27.830 -20.133 6.773 1.00 102.88 ? 452 ARG B NH2 1 ATOM 3243 N N . PHE A 1 422 ? 33.082 -21.530 -1.116 1.00 96.41 ? 453 PHE B N 1 ATOM 3244 C CA . PHE A 1 422 ? 33.598 -21.353 -2.481 1.00 97.07 ? 453 PHE B CA 1 ATOM 3245 C C . PHE A 1 422 ? 32.687 -21.985 -3.513 1.00 97.93 ? 453 PHE B C 1 ATOM 3246 O O . PHE A 1 422 ? 32.289 -23.141 -3.385 1.00 96.68 ? 453 PHE B O 1 ATOM 3247 C CB . PHE A 1 422 ? 34.982 -21.986 -2.656 1.00 95.14 ? 453 PHE B CB 1 ATOM 3248 C CG . PHE A 1 422 ? 36.084 -21.283 -1.918 1.00 94.51 ? 453 PHE B CG 1 ATOM 3249 C CD1 . PHE A 1 422 ? 36.406 -19.970 -2.205 1.00 96.31 ? 453 PHE B CD1 1 ATOM 3250 C CD2 . PHE A 1 422 ? 36.817 -21.948 -0.950 1.00 92.47 ? 453 PHE B CD2 1 ATOM 3251 C CE1 . PHE A 1 422 ? 37.429 -19.331 -1.524 1.00 95.73 ? 453 PHE B CE1 1 ATOM 3252 C CE2 . PHE A 1 422 ? 37.837 -21.314 -0.268 1.00 91.89 ? 453 PHE B CE2 1 ATOM 3253 C CZ . PHE A 1 422 ? 38.145 -20.009 -0.556 1.00 93.35 ? 453 PHE B CZ 1 ATOM 3254 N N . THR A 1 423 ? 32.376 -21.211 -4.545 1.00 95.24 ? 454 THR B N 1 ATOM 3255 C CA . THR A 1 423 ? 31.472 -21.643 -5.600 1.00 96.43 ? 454 THR B CA 1 ATOM 3256 C C . THR A 1 423 ? 32.196 -21.710 -6.933 1.00 96.97 ? 454 THR B C 1 ATOM 3257 O O . THR A 1 423 ? 33.415 -21.517 -7.004 1.00 96.27 ? 454 THR B O 1 ATOM 3258 C CB . THR A 1 423 ? 30.278 -20.675 -5.764 1.00 99.15 ? 454 THR B CB 1 ATOM 3259 O OG1 . THR A 1 423 ? 30.761 -19.327 -5.880 1.00 100.83 ? 454 THR B OG1 1 ATOM 3260 C CG2 . THR A 1 423 ? 29.317 -20.783 -4.581 1.00 98.86 ? 454 THR B CG2 1 ATOM 3261 N N . ASP A 1 424 ? 31.415 -21.987 -7.977 1.00 107.54 ? 455 ASP B N 1 ATOM 3262 C CA . ASP A 1 424 ? 31.856 -21.965 -9.375 1.00 108.65 ? 455 ASP B CA 1 ATOM 3263 C C . ASP A 1 424 ? 33.018 -22.902 -9.711 1.00 106.68 ? 455 ASP B C 1 ATOM 3264 O O . ASP A 1 424 ? 33.095 -24.037 -9.241 1.00 104.52 ? 455 ASP B O 1 ATOM 3265 C CB . ASP A 1 424 ? 32.216 -20.527 -9.785 1.00 110.93 ? 455 ASP B CB 1 ATOM 3266 C CG . ASP A 1 424 ? 31.391 -20.021 -10.953 1.00 113.69 ? 455 ASP B CG 1 ATOM 3267 O OD1 . ASP A 1 424 ? 30.463 -20.741 -11.376 1.00 113.89 ? 455 ASP B OD1 1 ATOM 3268 O OD2 . ASP A 1 424 ? 31.665 -18.897 -11.436 1.00 115.80 ? 455 ASP B OD2 1 ATOM 3269 N N . GLN A 1 425 ? 33.923 -22.404 -10.536 1.00 123.75 ? 456 GLN B N 1 ATOM 3270 C CA . GLN A 1 425 ? 34.983 -23.227 -11.075 1.00 122.40 ? 456 GLN B CA 1 ATOM 3271 C C . GLN A 1 425 ? 36.116 -23.411 -10.099 1.00 120.22 ? 456 GLN B C 1 ATOM 3272 O O . GLN A 1 425 ? 36.339 -22.594 -9.212 1.00 120.19 ? 456 GLN B O 1 ATOM 3273 C CB . GLN A 1 425 ? 35.526 -22.628 -12.373 1.00 124.42 ? 456 GLN B CB 1 ATOM 3274 C CG . GLN A 1 425 ? 34.506 -22.533 -13.498 1.00 126.68 ? 456 GLN B CG 1 ATOM 3275 C CD . GLN A 1 425 ? 33.595 -21.326 -13.365 1.00 129.00 ? 456 GLN B CD 1 ATOM 3276 O OE1 . GLN A 1 425 ? 33.920 -20.359 -12.673 1.00 129.36 ? 456 GLN B OE1 1 ATOM 3277 N NE2 . GLN A 1 425 ? 32.446 -21.377 -14.029 1.00 130.64 ? 456 GLN B NE2 1 ATOM 3278 N N . ILE A 1 426 ? 36.820 -24.515 -10.285 1.00 100.68 ? 457 ILE B N 1 ATOM 3279 C CA . ILE A 1 426 ? 38.093 -24.766 -9.637 1.00 98.79 ? 457 ILE B CA 1 ATOM 3280 C C . ILE A 1 426 ? 39.149 -24.233 -10.600 1.00 99.97 ? 457 ILE B C 1 ATOM 3281 O O . ILE A 1 426 ? 39.053 -24.479 -11.800 1.00 101.15 ? 457 ILE B O 1 ATOM 3282 C CB . ILE A 1 426 ? 38.296 -26.289 -9.435 1.00 96.52 ? 457 ILE B CB 1 ATOM 3283 C CG1 . ILE A 1 426 ? 37.127 -26.891 -8.649 1.00 95.63 ? 457 ILE B CG1 1 ATOM 3284 C CG2 . ILE A 1 426 ? 39.616 -26.580 -8.755 1.00 94.64 ? 457 ILE B CG2 1 ATOM 3285 C CD1 . ILE A 1 426 ? 36.979 -28.386 -8.821 1.00 94.10 ? 457 ILE B CD1 1 ATOM 3286 N N . PRO A 1 427 ? 40.140 -23.477 -10.093 1.00 100.18 ? 458 PRO B N 1 ATOM 3287 C CA . PRO A 1 427 ? 41.184 -22.899 -10.956 1.00 101.41 ? 458 PRO B CA 1 ATOM 3288 C C . PRO A 1 427 ? 41.965 -23.939 -11.759 1.00 100.66 ? 458 PRO B C 1 ATOM 3289 O O . PRO A 1 427 ? 42.340 -24.980 -11.219 1.00 98.50 ? 458 PRO B O 1 ATOM 3290 C CB . PRO A 1 427 ? 42.110 -22.196 -9.962 1.00 100.61 ? 458 PRO B CB 1 ATOM 3291 C CG . PRO A 1 427 ? 41.235 -21.846 -8.830 1.00 100.21 ? 458 PRO B CG 1 ATOM 3292 C CD . PRO A 1 427 ? 40.236 -22.973 -8.713 1.00 99.17 ? 458 PRO B CD 1 ATOM 3293 N N . ALA A 1 428 ? 42.213 -23.639 -13.032 1.00 93.54 ? 459 ALA B N 1 ATOM 3294 C CA . ALA A 1 428 ? 42.804 -24.592 -13.963 1.00 93.29 ? 459 ALA B CA 1 ATOM 3295 C C . ALA A 1 428 ? 44.301 -24.787 -13.754 1.00 92.15 ? 459 ALA B C 1 ATOM 3296 O O . ALA A 1 428 ? 44.808 -25.909 -13.821 1.00 90.68 ? 459 ALA B O 1 ATOM 3297 C CB . ALA A 1 428 ? 42.532 -24.152 -15.380 1.00 95.92 ? 459 ALA B CB 1 ATOM 3298 N N . ASP A 1 429 ? 44.999 -23.688 -13.492 1.00 113.68 ? 460 ASP B N 1 ATOM 3299 C CA . ASP A 1 429 ? 46.454 -23.683 -13.349 1.00 112.97 ? 460 ASP B CA 1 ATOM 3300 C C . ASP A 1 429 ? 46.947 -24.453 -12.126 1.00 110.20 ? 460 ASP B C 1 ATOM 3301 O O . ASP A 1 429 ? 48.146 -24.653 -11.946 1.00 109.35 ? 460 ASP B O 1 ATOM 3302 C CB . ASP A 1 429 ? 46.941 -22.243 -13.259 1.00 114.51 ? 460 ASP B CB 1 ATOM 3303 C CG . ASP A 1 429 ? 46.335 -21.504 -12.081 1.00 114.07 ? 460 ASP B CG 1 ATOM 3304 O OD1 . ASP A 1 429 ? 45.313 -21.991 -11.547 1.00 113.14 ? 460 ASP B OD1 1 ATOM 3305 O OD2 . ASP A 1 429 ? 46.876 -20.442 -11.691 1.00 114.71 ? 460 ASP B OD2 1 ATOM 3306 N N . PHE A 1 430 ? 46.009 -24.860 -11.284 1.00 88.11 ? 461 PHE B N 1 ATOM 3307 C CA . PHE A 1 430 ? 46.296 -25.559 -10.041 1.00 85.62 ? 461 PHE B CA 1 ATOM 3308 C C . PHE A 1 430 ? 47.241 -26.746 -10.187 1.00 84.14 ? 461 PHE B C 1 ATOM 3309 O O . PHE A 1 430 ? 48.116 -26.942 -9.353 1.00 82.63 ? 461 PHE B O 1 ATOM 3310 C CB . PHE A 1 430 ? 44.989 -26.028 -9.409 1.00 84.80 ? 461 PHE B CB 1 ATOM 3311 C CG . PHE A 1 430 ? 44.601 -25.269 -8.172 1.00 84.37 ? 461 PHE B CG 1 ATOM 3312 C CD1 . PHE A 1 430 ? 45.544 -24.939 -7.221 1.00 83.25 ? 461 PHE B CD1 1 ATOM 3313 C CD2 . PHE A 1 430 ? 43.288 -24.893 -7.957 1.00 85.18 ? 461 PHE B CD2 1 ATOM 3314 C CE1 . PHE A 1 430 ? 45.186 -24.248 -6.082 1.00 82.93 ? 461 PHE B CE1 1 ATOM 3315 C CE2 . PHE A 1 430 ? 42.929 -24.200 -6.819 1.00 84.91 ? 461 PHE B CE2 1 ATOM 3316 C CZ . PHE A 1 430 ? 43.880 -23.878 -5.883 1.00 83.79 ? 461 PHE B CZ 1 ATOM 3317 N N . ALA A 1 431 ? 47.072 -27.540 -11.238 1.00 100.12 ? 462 ALA B N 1 ATOM 3318 C CA . ALA A 1 431 ? 47.931 -28.705 -11.426 1.00 98.89 ? 462 ALA B CA 1 ATOM 3319 C C . ALA A 1 431 ? 49.180 -28.382 -12.250 1.00 100.04 ? 462 ALA B C 1 ATOM 3320 O O . ALA A 1 431 ? 50.038 -29.238 -12.457 1.00 99.28 ? 462 ALA B O 1 ATOM 3321 C CB . ALA A 1 431 ? 47.157 -29.842 -12.047 1.00 98.70 ? 462 ALA B CB 1 ATOM 3322 N N . THR A 1 432 ? 49.267 -27.146 -12.728 1.00 93.40 ? 463 THR B N 1 ATOM 3323 C CA . THR A 1 432 ? 50.466 -26.668 -13.400 1.00 94.61 ? 463 THR B CA 1 ATOM 3324 C C . THR A 1 432 ? 51.555 -26.214 -12.422 1.00 93.58 ? 463 THR B C 1 ATOM 3325 O O . THR A 1 432 ? 52.739 -26.310 -12.739 1.00 93.77 ? 463 THR B O 1 ATOM 3326 C CB . THR A 1 432 ? 50.130 -25.524 -14.332 1.00 97.28 ? 463 THR B CB 1 ATOM 3327 O OG1 . THR A 1 432 ? 49.570 -24.455 -13.567 1.00 97.56 ? 463 THR B OG1 1 ATOM 3328 C CG2 . THR A 1 432 ? 49.111 -25.979 -15.354 1.00 98.43 ? 463 THR B CG2 1 ATOM 3329 N N . ALA A 1 433 ? 51.142 -25.707 -11.253 1.00 91.14 ? 464 ALA B N 1 ATOM 3330 C CA . ALA A 1 433 ? 52.046 -25.271 -10.172 1.00 89.99 ? 464 ALA B CA 1 ATOM 3331 C C . ALA A 1 433 ? 52.988 -26.383 -9.709 1.00 88.05 ? 464 ALA B C 1 ATOM 3332 O O . ALA A 1 433 ? 52.539 -27.441 -9.283 1.00 86.50 ? 464 ALA B O 1 ATOM 3333 C CB . ALA A 1 433 ? 51.247 -24.752 -9.004 1.00 89.20 ? 464 ALA B CB 1 ATOM 3334 N N . PRO A 1 434 ? 54.300 -26.119 -9.768 1.00 81.33 ? 465 PRO B N 1 ATOM 3335 C CA . PRO A 1 434 ? 55.393 -27.097 -9.798 1.00 80.31 ? 465 PRO B CA 1 ATOM 3336 C C . PRO A 1 434 ? 55.649 -27.869 -8.522 1.00 77.88 ? 465 PRO B C 1 ATOM 3337 O O . PRO A 1 434 ? 56.064 -29.024 -8.583 1.00 76.90 ? 465 PRO B O 1 ATOM 3338 C CB . PRO A 1 434 ? 56.613 -26.233 -10.109 1.00 81.51 ? 465 PRO B CB 1 ATOM 3339 C CG . PRO A 1 434 ? 56.286 -24.921 -9.539 1.00 82.06 ? 465 PRO B CG 1 ATOM 3340 C CD . PRO A 1 434 ? 54.804 -24.742 -9.652 1.00 82.53 ? 465 PRO B CD 1 ATOM 3341 N N . VAL A 1 435 ? 55.501 -27.220 -7.382 1.00 77.05 ? 466 VAL B N 1 ATOM 3342 C CA . VAL A 1 435 ? 55.832 -27.871 -6.128 1.00 74.88 ? 466 VAL B CA 1 ATOM 3343 C C . VAL A 1 435 ? 54.672 -28.373 -5.281 1.00 73.55 ? 466 VAL B C 1 ATOM 3344 O O . VAL A 1 435 ? 54.906 -28.965 -4.222 1.00 71.80 ? 466 VAL B O 1 ATOM 3345 C CB . VAL A 1 435 ? 56.683 -26.962 -5.286 1.00 74.62 ? 466 VAL B CB 1 ATOM 3346 C CG1 . VAL A 1 435 ? 58.147 -27.111 -5.667 1.00 74.87 ? 466 VAL B CG1 1 ATOM 3347 C CG2 . VAL A 1 435 ? 56.198 -25.545 -5.485 1.00 76.23 ? 466 VAL B CG2 1 ATOM 3348 N N . LEU A 1 436 ? 53.438 -28.167 -5.731 1.00 79.48 ? 467 LEU B N 1 ATOM 3349 C CA . LEU A 1 436 ? 52.311 -28.229 -4.808 1.00 78.57 ? 467 LEU B CA 1 ATOM 3350 C C . LEU A 1 436 ? 51.983 -29.649 -4.432 1.00 77.51 ? 467 LEU B C 1 ATOM 3351 O O . LEU A 1 436 ? 51.501 -30.412 -5.253 1.00 77.66 ? 467 LEU B O 1 ATOM 3352 C CB . LEU A 1 436 ? 51.079 -27.640 -5.475 1.00 80.15 ? 467 LEU B CB 1 ATOM 3353 C CG . LEU A 1 436 ? 49.791 -27.910 -4.704 1.00 79.43 ? 467 LEU B CG 1 ATOM 3354 C CD1 . LEU A 1 436 ? 49.801 -27.077 -3.449 1.00 79.13 ? 467 LEU B CD1 1 ATOM 3355 C CD2 . LEU A 1 436 ? 48.556 -27.622 -5.531 1.00 80.93 ? 467 LEU B CD2 1 ATOM 3356 N N . GLN A 1 437 ? 52.198 -29.965 -3.159 1.00 70.23 ? 468 GLN B N 1 ATOM 3357 C CA . GLN A 1 437 ? 52.129 -31.333 -2.647 1.00 68.58 ? 468 GLN B CA 1 ATOM 3358 C C . GLN A 1 437 ? 50.818 -31.751 -1.964 1.00 67.85 ? 468 GLN B C 1 ATOM 3359 O O . GLN A 1 437 ? 50.593 -32.929 -1.745 1.00 66.76 ? 468 GLN B O 1 ATOM 3360 C CB . GLN A 1 437 ? 53.272 -31.507 -1.642 1.00 67.24 ? 468 GLN B CB 1 ATOM 3361 C CG . GLN A 1 437 ? 54.212 -32.681 -1.856 1.00 66.44 ? 468 GLN B CG 1 ATOM 3362 C CD . GLN A 1 437 ? 55.564 -32.435 -1.199 1.00 65.83 ? 468 GLN B CD 1 ATOM 3363 O OE1 . GLN A 1 437 ? 55.998 -33.176 -0.301 1.00 64.42 ? 468 GLN B OE1 1 ATOM 3364 N NE2 . GLN A 1 437 ? 56.241 -31.378 -1.655 1.00 67.00 ? 468 GLN B NE2 1 ATOM 3365 N N . TYR A 1 438 ? 49.966 -30.798 -1.610 1.00 68.52 ? 469 TYR B N 1 ATOM 3366 C CA . TYR A 1 438 ? 48.721 -31.120 -0.917 1.00 67.97 ? 469 TYR B CA 1 ATOM 3367 C C . TYR A 1 438 ? 47.604 -30.209 -1.369 1.00 69.56 ? 469 TYR B C 1 ATOM 3368 O O . TYR A 1 438 ? 47.731 -29.008 -1.259 1.00 70.51 ? 469 TYR B O 1 ATOM 3369 C CB . TYR A 1 438 ? 48.894 -30.959 0.597 1.00 66.85 ? 469 TYR B CB 1 ATOM 3370 C CG . TYR A 1 438 ? 47.617 -31.161 1.403 1.00 67.07 ? 469 TYR B CG 1 ATOM 3371 C CD1 . TYR A 1 438 ? 46.689 -30.143 1.551 1.00 68.08 ? 469 TYR B CD1 1 ATOM 3372 C CD2 . TYR A 1 438 ? 47.349 -32.368 2.025 1.00 66.36 ? 469 TYR B CD2 1 ATOM 3373 C CE1 . TYR A 1 438 ? 45.531 -30.327 2.277 1.00 68.42 ? 469 TYR B CE1 1 ATOM 3374 C CE2 . TYR A 1 438 ? 46.191 -32.557 2.757 1.00 66.69 ? 469 TYR B CE2 1 ATOM 3375 C CZ . TYR A 1 438 ? 45.288 -31.530 2.880 1.00 67.74 ? 469 TYR B CZ 1 ATOM 3376 O OH . TYR A 1 438 ? 44.132 -31.703 3.606 1.00 68.21 ? 469 TYR B OH 1 ATOM 3377 N N . LEU A 1 439 ? 46.481 -30.750 -1.813 1.00 70.47 ? 470 LEU B N 1 ATOM 3378 C CA . LEU A 1 439 ? 45.373 -29.872 -2.171 1.00 71.47 ? 470 LEU B CA 1 ATOM 3379 C C . LEU A 1 439 ? 44.030 -30.358 -1.628 1.00 72.23 ? 470 LEU B C 1 ATOM 3380 O O . LEU A 1 439 ? 43.557 -31.424 -2.029 1.00 72.25 ? 470 LEU B O 1 ATOM 3381 C CB . LEU A 1 439 ? 45.312 -29.735 -3.689 1.00 73.06 ? 470 LEU B CB 1 ATOM 3382 C CG . LEU A 1 439 ? 44.298 -28.732 -4.213 1.00 75.00 ? 470 LEU B CG 1 ATOM 3383 C CD1 . LEU A 1 439 ? 44.401 -27.469 -3.403 1.00 75.47 ? 470 LEU B CD1 1 ATOM 3384 C CD2 . LEU A 1 439 ? 44.578 -28.447 -5.664 1.00 76.65 ? 470 LEU B CD2 1 ATOM 3385 N N . ASN A 1 440 ? 43.406 -29.599 -0.728 1.00 73.06 ? 471 ASN B N 1 ATOM 3386 C CA . ASN A 1 440 ? 42.083 -30.001 -0.250 1.00 74.12 ? 471 ASN B CA 1 ATOM 3387 C C . ASN A 1 440 ? 41.043 -28.930 -0.554 1.00 75.07 ? 471 ASN B C 1 ATOM 3388 O O . ASN A 1 440 ? 41.006 -27.895 0.092 1.00 75.34 ? 471 ASN B O 1 ATOM 3389 C CB . ASN A 1 440 ? 42.121 -30.308 1.262 1.00 74.40 ? 471 ASN B CB 1 ATOM 3390 C CG . ASN A 1 440 ? 40.951 -31.185 1.724 1.00 75.67 ? 471 ASN B CG 1 ATOM 3391 O OD1 . ASN A 1 440 ? 39.996 -31.385 0.976 1.00 76.32 ? 471 ASN B OD1 1 ATOM 3392 N ND2 . ASN A 1 440 ? 41.024 -31.701 2.966 1.00 76.01 ? 471 ASN B ND2 1 ATOM 3393 N N . LEU A 1 441 ? 40.204 -29.190 -1.549 1.00 74.25 ? 472 LEU B N 1 ATOM 3394 C CA . LEU A 1 441 ? 39.089 -28.315 -1.920 1.00 76.18 ? 472 LEU B CA 1 ATOM 3395 C C . LEU A 1 441 ? 37.734 -28.820 -1.438 1.00 76.13 ? 472 LEU B C 1 ATOM 3396 O O . LEU A 1 441 ? 36.682 -28.325 -1.864 1.00 77.75 ? 472 LEU B O 1 ATOM 3397 C CB . LEU A 1 441 ? 39.073 -28.038 -3.414 1.00 77.79 ? 472 LEU B CB 1 ATOM 3398 C CG . LEU A 1 441 ? 40.470 -27.673 -3.883 1.00 77.78 ? 472 LEU B CG 1 ATOM 3399 C CD1 . LEU A 1 441 ? 40.418 -27.275 -5.328 1.00 79.65 ? 472 LEU B CD1 1 ATOM 3400 C CD2 . LEU A 1 441 ? 41.022 -26.555 -3.044 1.00 77.93 ? 472 LEU B CD2 1 ATOM 3401 N N . SER A 1 442 ? 37.768 -29.857 -0.614 1.00 77.37 ? 473 SER B N 1 ATOM 3402 C CA . SER A 1 442 ? 36.572 -30.593 -0.249 1.00 78.12 ? 473 SER B CA 1 ATOM 3403 C C . SER A 1 442 ? 35.496 -29.783 0.490 1.00 79.54 ? 473 SER B C 1 ATOM 3404 O O . SER A 1 442 ? 35.782 -28.745 1.083 1.00 79.69 ? 473 SER B O 1 ATOM 3405 C CB . SER A 1 442 ? 36.966 -31.779 0.611 1.00 77.91 ? 473 SER B CB 1 ATOM 3406 O OG . SER A 1 442 ? 36.073 -31.886 1.696 1.00 79.32 ? 473 SER B OG 1 ATOM 3407 N N . THR A 1 443 ? 34.258 -30.279 0.429 1.00 84.44 ? 474 THR B N 1 ATOM 3408 C CA . THR A 1 443 ? 33.096 -29.736 1.154 1.00 85.99 ? 474 THR B CA 1 ATOM 3409 C C . THR A 1 443 ? 32.695 -28.323 0.762 1.00 86.26 ? 474 THR B C 1 ATOM 3410 O O . THR A 1 443 ? 32.344 -27.510 1.614 1.00 87.10 ? 474 THR B O 1 ATOM 3411 C CB . THR A 1 443 ? 33.283 -29.782 2.679 1.00 86.77 ? 474 THR B CB 1 ATOM 3412 O OG1 . THR A 1 443 ? 34.299 -30.729 3.008 1.00 85.69 ? 474 THR B OG1 1 ATOM 3413 C CG2 . THR A 1 443 ? 31.985 -30.179 3.356 1.00 88.51 ? 474 THR B CG2 1 ATOM 3414 N N . ASN A 1 444 ? 32.726 -28.045 -0.531 1.00 101.20 ? 475 ASN B N 1 ATOM 3415 C CA . ASN A 1 444 ? 32.401 -26.721 -1.019 1.00 101.37 ? 475 ASN B CA 1 ATOM 3416 C C . ASN A 1 444 ? 31.143 -26.656 -1.847 1.00 102.20 ? 475 ASN B C 1 ATOM 3417 O O . ASN A 1 444 ? 30.387 -27.613 -1.952 1.00 102.81 ? 475 ASN B O 1 ATOM 3418 C CB . ASN A 1 444 ? 33.558 -26.148 -1.819 1.00 99.91 ? 475 ASN B CB 1 ATOM 3419 C CG . ASN A 1 444 ? 34.648 -25.623 -0.938 1.00 99.27 ? 475 ASN B CG 1 ATOM 3420 O OD1 . ASN A 1 444 ? 34.785 -24.414 -0.752 1.00 99.08 ? 475 ASN B OD1 1 ATOM 3421 N ND2 . ASN A 1 444 ? 35.419 -26.529 -0.358 1.00 98.96 ? 475 ASN B ND2 1 ATOM 3422 N N . PHE A 1 445 ? 30.898 -25.477 -2.379 1.00 106.68 ? 476 PHE B N 1 ATOM 3423 C CA . PHE A 1 445 ? 29.756 -25.254 -3.239 1.00 107.50 ? 476 PHE B CA 1 ATOM 3424 C C . PHE A 1 445 ? 29.930 -25.222 -4.758 1.00 108.23 ? 476 PHE B C 1 ATOM 3425 O O . PHE A 1 445 ? 29.054 -24.739 -5.458 1.00 110.09 ? 476 PHE B O 1 ATOM 3426 C CB . PHE A 1 445 ? 28.791 -24.246 -2.639 1.00 109.15 ? 476 PHE B CB 1 ATOM 3427 C CG . PHE A 1 445 ? 28.026 -24.825 -1.495 1.00 110.06 ? 476 PHE B CG 1 ATOM 3428 C CD1 . PHE A 1 445 ? 28.624 -24.967 -0.258 1.00 110.43 ? 476 PHE B CD1 1 ATOM 3429 C CD2 . PHE A 1 445 ? 26.745 -25.317 -1.680 1.00 110.84 ? 476 PHE B CD2 1 ATOM 3430 C CE1 . PHE A 1 445 ? 27.940 -25.538 0.790 1.00 111.62 ? 476 PHE B CE1 1 ATOM 3431 C CE2 . PHE A 1 445 ? 26.052 -25.890 -0.634 1.00 112.03 ? 476 PHE B CE2 1 ATOM 3432 C CZ . PHE A 1 445 ? 26.652 -26.001 0.604 1.00 112.44 ? 476 PHE B CZ 1 ATOM 3433 N N . PHE A 1 446 ? 31.063 -25.723 -5.245 1.00 108.97 ? 477 PHE B N 1 ATOM 3434 C CA . PHE A 1 446 ? 31.535 -25.505 -6.617 1.00 109.82 ? 477 PHE B CA 1 ATOM 3435 C C . PHE A 1 446 ? 30.475 -25.524 -7.710 1.00 111.75 ? 477 PHE B C 1 ATOM 3436 O O . PHE A 1 446 ? 30.282 -24.518 -8.383 1.00 113.97 ? 477 PHE B O 1 ATOM 3437 C CB . PHE A 1 446 ? 32.575 -26.560 -6.981 1.00 107.96 ? 477 PHE B CB 1 ATOM 3438 C CG . PHE A 1 446 ? 33.821 -26.473 -6.179 1.00 106.41 ? 477 PHE B CG 1 ATOM 3439 C CD1 . PHE A 1 446 ? 34.246 -25.264 -5.667 1.00 107.01 ? 477 PHE B CD1 1 ATOM 3440 C CD2 . PHE A 1 446 ? 34.572 -27.600 -5.930 1.00 104.45 ? 477 PHE B CD2 1 ATOM 3441 C CE1 . PHE A 1 446 ? 35.405 -25.181 -4.915 1.00 105.59 ? 477 PHE B CE1 1 ATOM 3442 C CE2 . PHE A 1 446 ? 35.733 -27.525 -5.176 1.00 103.08 ? 477 PHE B CE2 1 ATOM 3443 C CZ . PHE A 1 446 ? 36.150 -26.314 -4.669 1.00 103.63 ? 477 PHE B CZ 1 ATOM 3444 N N . HIS A 1 447 ? 29.819 -26.665 -7.908 1.00 97.78 ? 478 HIS B N 1 ATOM 3445 C CA . HIS A 1 447 ? 28.846 -26.838 -8.996 1.00 99.44 ? 478 HIS B CA 1 ATOM 3446 C C . HIS A 1 447 ? 29.504 -26.688 -10.364 1.00 100.45 ? 478 HIS B C 1 ATOM 3447 O O . HIS A 1 447 ? 28.986 -26.019 -11.253 1.00 102.75 ? 478 HIS B O 1 ATOM 3448 C CB . HIS A 1 447 ? 27.640 -25.897 -8.852 1.00 101.70 ? 478 HIS B CB 1 ATOM 3449 C CG . HIS A 1 447 ? 26.682 -26.293 -7.767 1.00 101.05 ? 478 HIS B CG 1 ATOM 3450 N ND1 . HIS A 1 447 ? 26.139 -25.383 -6.882 1.00 102.08 ? 478 HIS B ND1 1 ATOM 3451 C CD2 . HIS A 1 447 ? 26.158 -27.496 -7.433 1.00 99.81 ? 478 HIS B CD2 1 ATOM 3452 C CE1 . HIS A 1 447 ? 25.334 -26.010 -6.044 1.00 101.44 ? 478 HIS B CE1 1 ATOM 3453 N NE2 . HIS A 1 447 ? 25.326 -27.294 -6.358 1.00 100.15 ? 478 HIS B NE2 1 ATOM 3454 N N . ARG A 1 448 ? 30.662 -27.318 -10.506 1.00 100.48 ? 479 ARG B N 1 ATOM 3455 C CA . ARG A 1 448 ? 31.403 -27.351 -11.755 1.00 101.19 ? 479 ARG B CA 1 ATOM 3456 C C . ARG A 1 448 ? 32.284 -28.603 -11.734 1.00 98.87 ? 479 ARG B C 1 ATOM 3457 O O . ARG A 1 448 ? 32.057 -29.503 -10.922 1.00 97.03 ? 479 ARG B O 1 ATOM 3458 C CB . ARG A 1 448 ? 32.216 -26.074 -11.951 1.00 102.51 ? 479 ARG B CB 1 ATOM 3459 C CG . ARG A 1 448 ? 32.132 -25.491 -13.360 1.00 105.01 ? 479 ARG B CG 1 ATOM 3460 C CD . ARG A 1 448 ? 30.701 -25.183 -13.762 1.00 107.03 ? 479 ARG B CD 1 ATOM 3461 N NE . ARG A 1 448 ? 30.089 -24.119 -12.964 1.00 108.15 ? 479 ARG B NE 1 ATOM 3462 C CZ . ARG A 1 448 ? 29.700 -22.935 -13.446 1.00 110.82 ? 479 ARG B CZ 1 ATOM 3463 N NH1 . ARG A 1 448 ? 29.850 -22.645 -14.735 1.00 112.68 ? 479 ARG B NH1 1 ATOM 3464 N NH2 . ARG A 1 448 ? 29.149 -22.034 -12.641 1.00 111.74 ? 479 ARG B NH2 1 ATOM 3465 N N . LYS A 1 449 ? 33.254 -28.689 -12.641 1.00 109.44 ? 480 LYS B N 1 ATOM 3466 C CA . LYS A 1 449 ? 34.029 -29.924 -12.810 1.00 107.58 ? 480 LYS B CA 1 ATOM 3467 C C . LYS A 1 449 ? 35.556 -29.755 -12.728 1.00 106.76 ? 480 LYS B C 1 ATOM 3468 O O . LYS A 1 449 ? 36.071 -28.650 -12.882 1.00 108.00 ? 480 LYS B O 1 ATOM 3469 C CB . LYS A 1 449 ? 33.644 -30.583 -14.134 1.00 108.56 ? 480 LYS B CB 1 ATOM 3470 C CG . LYS A 1 449 ? 32.487 -29.882 -14.845 1.00 111.01 ? 480 LYS B CG 1 ATOM 3471 C CD . LYS A 1 449 ? 31.584 -30.880 -15.561 1.00 111.18 ? 480 LYS B CD 1 ATOM 3472 C CE . LYS A 1 449 ? 30.288 -30.236 -16.061 1.00 113.50 ? 480 LYS B CE 1 ATOM 3473 N NZ . LYS A 1 449 ? 29.399 -31.225 -16.762 1.00 113.68 ? 480 LYS B NZ 1 ATOM 3474 N N . LEU A 1 450 ? 36.262 -30.864 -12.500 1.00 86.78 ? 481 LEU B N 1 ATOM 3475 C CA . LEU A 1 450 ? 37.726 -30.882 -12.370 1.00 85.82 ? 481 LEU B CA 1 ATOM 3476 C C . LEU A 1 450 ? 38.450 -30.496 -13.668 1.00 87.46 ? 481 LEU B C 1 ATOM 3477 O O . LEU A 1 450 ? 37.886 -30.630 -14.746 1.00 88.90 ? 481 LEU B O 1 ATOM 3478 C CB . LEU A 1 450 ? 38.177 -32.270 -11.921 1.00 83.54 ? 481 LEU B CB 1 ATOM 3479 C CG . LEU A 1 450 ? 37.633 -32.716 -10.560 1.00 81.83 ? 481 LEU B CG 1 ATOM 3480 C CD1 . LEU A 1 450 ? 36.316 -33.469 -10.674 1.00 81.98 ? 481 LEU B CD1 1 ATOM 3481 C CD2 . LEU A 1 450 ? 38.663 -33.544 -9.826 1.00 79.82 ? 481 LEU B CD2 1 ATOM 3482 N N . PRO A 1 451 ? 39.694 -29.990 -13.578 1.00 90.86 ? 482 PRO B N 1 ATOM 3483 C CA . PRO A 1 451 ? 40.432 -29.688 -14.820 1.00 92.45 ? 482 PRO B CA 1 ATOM 3484 C C . PRO A 1 451 ? 41.030 -30.922 -15.502 1.00 91.70 ? 482 PRO B C 1 ATOM 3485 O O . PRO A 1 451 ? 41.202 -31.949 -14.860 1.00 89.67 ? 482 PRO B O 1 ATOM 3486 C CB . PRO A 1 451 ? 41.550 -28.746 -14.352 1.00 92.49 ? 482 PRO B CB 1 ATOM 3487 C CG . PRO A 1 451 ? 41.737 -29.067 -12.916 1.00 90.21 ? 482 PRO B CG 1 ATOM 3488 C CD . PRO A 1 451 ? 40.378 -29.458 -12.387 1.00 89.70 ? 482 PRO B CD 1 ATOM 3489 N N . GLU A 1 452 ? 41.335 -30.815 -16.791 1.00 104.60 ? 483 GLU B N 1 ATOM 3490 C CA . GLU A 1 452 ? 42.050 -31.871 -17.498 1.00 104.16 ? 483 GLU B CA 1 ATOM 3491 C C . GLU A 1 452 ? 43.449 -31.960 -16.913 1.00 102.87 ? 483 GLU B C 1 ATOM 3492 O O . GLU A 1 452 ? 44.077 -33.028 -16.907 1.00 101.59 ? 483 GLU B O 1 ATOM 3493 C CB . GLU A 1 452 ? 42.129 -31.543 -18.991 1.00 106.61 ? 483 GLU B CB 1 ATOM 3494 C CG . GLU A 1 452 ? 42.342 -32.747 -19.913 1.00 106.59 ? 483 GLU B CG 1 ATOM 3495 C CD . GLU A 1 452 ? 41.927 -32.466 -21.365 1.00 109.17 ? 483 GLU B CD 1 ATOM 3496 O OE1 . GLU A 1 452 ? 41.493 -33.413 -22.069 1.00 109.29 ? 483 GLU B OE1 1 ATOM 3497 O OE2 . GLU A 1 452 ? 42.035 -31.297 -21.804 1.00 111.14 ? 483 GLU B OE2 1 ATOM 3498 N N . ASN A 1 453 ? 43.915 -30.815 -16.411 1.00 99.46 ? 484 ASN B N 1 ATOM 3499 C CA . ASN A 1 453 ? 45.245 -30.662 -15.837 1.00 98.50 ? 484 ASN B CA 1 ATOM 3500 C C . ASN A 1 453 ? 45.461 -31.531 -14.619 1.00 95.89 ? 484 ASN B C 1 ATOM 3501 O O . ASN A 1 453 ? 46.585 -31.914 -14.312 1.00 94.85 ? 484 ASN B O 1 ATOM 3502 C CB . ASN A 1 453 ? 45.475 -29.199 -15.458 1.00 99.53 ? 484 ASN B CB 1 ATOM 3503 C CG . ASN A 1 453 ? 45.787 -28.327 -16.664 1.00 102.14 ? 484 ASN B CG 1 ATOM 3504 O OD1 . ASN A 1 453 ? 45.527 -28.710 -17.809 1.00 103.44 ? 484 ASN B OD1 1 ATOM 3505 N ND2 . ASN A 1 453 ? 46.354 -27.150 -16.413 1.00 103.02 ? 484 ASN B ND2 1 ATOM 3506 N N . ILE A 1 454 ? 44.357 -31.874 -13.968 1.00 82.86 ? 485 ILE B N 1 ATOM 3507 C CA . ILE A 1 454 ? 44.354 -32.331 -12.578 1.00 80.64 ? 485 ILE B CA 1 ATOM 3508 C C . ILE A 1 454 ? 45.355 -33.420 -12.189 1.00 78.84 ? 485 ILE B C 1 ATOM 3509 O O . ILE A 1 454 ? 46.051 -33.278 -11.177 1.00 77.58 ? 485 ILE B O 1 ATOM 3510 C CB . ILE A 1 454 ? 42.929 -32.691 -12.083 1.00 80.12 ? 485 ILE B CB 1 ATOM 3511 C CG1 . ILE A 1 454 ? 42.926 -32.888 -10.569 1.00 78.15 ? 485 ILE B CG1 1 ATOM 3512 C CG2 . ILE A 1 454 ? 42.408 -33.909 -12.775 1.00 79.91 ? 485 ILE B CG2 1 ATOM 3513 C CD1 . ILE A 1 454 ? 43.405 -31.683 -9.788 1.00 78.29 ? 485 ILE B CD1 1 ATOM 3514 N N . TRP A 1 455 ? 45.462 -34.477 -12.986 1.00 81.34 ? 486 TRP B N 1 ATOM 3515 C CA . TRP A 1 455 ? 46.305 -35.608 -12.598 1.00 79.69 ? 486 TRP B CA 1 ATOM 3516 C C . TRP A 1 455 ? 47.751 -35.472 -13.078 1.00 80.18 ? 486 TRP B C 1 ATOM 3517 O O . TRP A 1 455 ? 48.557 -36.402 -12.940 1.00 79.14 ? 486 TRP B O 1 ATOM 3518 C CB . TRP A 1 455 ? 45.689 -36.930 -13.044 1.00 79.21 ? 486 TRP B CB 1 ATOM 3519 C CG . TRP A 1 455 ? 44.209 -37.013 -12.774 1.00 79.11 ? 486 TRP B CG 1 ATOM 3520 C CD1 . TRP A 1 455 ? 43.228 -37.173 -13.698 1.00 80.30 ? 486 TRP B CD1 1 ATOM 3521 C CD2 . TRP A 1 455 ? 43.543 -36.938 -11.496 1.00 77.83 ? 486 TRP B CD2 1 ATOM 3522 N NE1 . TRP A 1 455 ? 41.997 -37.208 -13.088 1.00 79.85 ? 486 TRP B NE1 1 ATOM 3523 C CE2 . TRP A 1 455 ? 42.163 -37.067 -11.737 1.00 78.39 ? 486 TRP B CE2 1 ATOM 3524 C CE3 . TRP A 1 455 ? 43.981 -36.780 -10.178 1.00 76.61 ? 486 TRP B CE3 1 ATOM 3525 C CZ2 . TRP A 1 455 ? 41.216 -37.037 -10.710 1.00 77.85 ? 486 TRP B CZ2 1 ATOM 3526 C CZ3 . TRP A 1 455 ? 43.037 -36.752 -9.158 1.00 76.28 ? 486 TRP B CZ3 1 ATOM 3527 C CH2 . TRP A 1 455 ? 41.674 -36.880 -9.431 1.00 76.95 ? 486 TRP B CH2 1 ATOM 3528 N N . LYS A 1 456 ? 48.059 -34.305 -13.641 1.00 89.81 ? 487 LYS B N 1 ATOM 3529 C CA . LYS A 1 456 ? 49.357 -34.041 -14.237 1.00 90.70 ? 487 LYS B CA 1 ATOM 3530 C C . LYS A 1 456 ? 50.300 -33.373 -13.274 1.00 89.93 ? 487 LYS B C 1 ATOM 3531 O O . LYS A 1 456 ? 51.428 -33.070 -13.619 1.00 90.59 ? 487 LYS B O 1 ATOM 3532 C CB . LYS A 1 456 ? 49.199 -33.157 -15.468 1.00 93.19 ? 487 LYS B CB 1 ATOM 3533 C CG . LYS A 1 456 ? 48.439 -33.813 -16.599 1.00 94.24 ? 487 LYS B CG 1 ATOM 3534 C CD . LYS A 1 456 ? 49.302 -33.948 -17.857 1.00 95.89 ? 487 LYS B CD 1 ATOM 3535 C CE . LYS A 1 456 ? 50.618 -34.691 -17.598 1.00 94.82 ? 487 LYS B CE 1 ATOM 3536 N NZ . LYS A 1 456 ? 51.324 -35.041 -18.870 1.00 96.43 ? 487 LYS B NZ 1 ATOM 3537 N N . ALA A 1 457 ? 49.832 -33.152 -12.061 1.00 82.67 ? 488 ALA B N 1 ATOM 3538 C CA . ALA A 1 457 ? 50.579 -32.392 -11.068 1.00 82.00 ? 488 ALA B CA 1 ATOM 3539 C C . ALA A 1 457 ? 51.973 -32.938 -10.704 1.00 80.94 ? 488 ALA B C 1 ATOM 3540 O O . ALA A 1 457 ? 52.101 -34.041 -10.169 1.00 79.36 ? 488 ALA B O 1 ATOM 3541 C CB . ALA A 1 457 ? 49.734 -32.243 -9.843 1.00 93.83 ? 488 ALA B CB 1 ATOM 3542 N N . PRO A 1 458 ? 53.010 -32.119 -10.935 1.00 83.15 ? 489 PRO B N 1 ATOM 3543 C CA . PRO A 1 458 ? 54.401 -32.577 -11.015 1.00 82.84 ? 489 PRO B CA 1 ATOM 3544 C C . PRO A 1 458 ? 54.864 -33.275 -9.755 1.00 80.66 ? 489 PRO B C 1 ATOM 3545 O O . PRO A 1 458 ? 55.324 -34.409 -9.838 1.00 79.92 ? 489 PRO B O 1 ATOM 3546 C CB . PRO A 1 458 ? 55.193 -31.270 -11.161 1.00 84.14 ? 489 PRO B CB 1 ATOM 3547 C CG . PRO A 1 458 ? 54.198 -30.245 -11.611 1.00 85.65 ? 489 PRO B CG 1 ATOM 3548 C CD . PRO A 1 458 ? 52.894 -30.655 -11.017 1.00 84.56 ? 489 PRO B CD 1 ATOM 3549 N N . ASN A 1 459 ? 54.711 -32.642 -8.600 1.00 95.60 ? 490 ASN B N 1 ATOM 3550 C CA . ASN A 1 459 ? 54.783 -33.388 -7.366 1.00 93.57 ? 490 ASN B CA 1 ATOM 3551 C C . ASN A 1 459 ? 53.552 -32.997 -6.601 1.00 93.37 ? 490 ASN B C 1 ATOM 3552 O O . ASN A 1 459 ? 53.497 -31.909 -6.055 1.00 93.65 ? 490 ASN B O 1 ATOM 3553 C CB . ASN A 1 459 ? 56.031 -33.002 -6.577 1.00 93.14 ? 490 ASN B CB 1 ATOM 3554 C CG . ASN A 1 459 ? 57.312 -33.253 -7.347 1.00 93.70 ? 490 ASN B CG 1 ATOM 3555 O OD1 . ASN A 1 459 ? 57.841 -34.366 -7.349 1.00 93.12 ? 490 ASN B OD1 1 ATOM 3556 N ND2 . ASN A 1 459 ? 57.826 -32.215 -7.997 1.00 95.24 ? 490 ASN B ND2 1 ATOM 3557 N N . LEU A 1 460 ? 52.572 -33.892 -6.556 1.00 70.65 ? 491 LEU B N 1 ATOM 3558 C CA . LEU A 1 460 ? 51.362 -33.692 -5.775 1.00 70.09 ? 491 LEU B CA 1 ATOM 3559 C C . LEU A 1 460 ? 51.015 -35.017 -5.202 1.00 68.53 ? 491 LEU B C 1 ATOM 3560 O O . LEU A 1 460 ? 50.751 -35.952 -5.944 1.00 68.65 ? 491 LEU B O 1 ATOM 3561 C CB . LEU A 1 460 ? 50.198 -33.227 -6.648 1.00 71.59 ? 491 LEU B CB 1 ATOM 3562 C CG . LEU A 1 460 ? 48.786 -33.234 -6.048 1.00 71.21 ? 491 LEU B CG 1 ATOM 3563 C CD1 . LEU A 1 460 ? 48.788 -32.632 -4.679 1.00 70.29 ? 491 LEU B CD1 1 ATOM 3564 C CD2 . LEU A 1 460 ? 47.805 -32.460 -6.894 1.00 73.01 ? 491 LEU B CD2 1 ATOM 3565 N N . GLN A 1 461 ? 50.956 -35.086 -3.883 1.00 68.18 ? 492 GLN B N 1 ATOM 3566 C CA . GLN A 1 461 ? 50.685 -36.346 -3.205 1.00 67.99 ? 492 GLN B CA 1 ATOM 3567 C C . GLN A 1 461 ? 49.209 -36.522 -2.828 1.00 68.61 ? 492 GLN B C 1 ATOM 3568 O O . GLN A 1 461 ? 48.586 -37.478 -3.268 1.00 68.65 ? 492 GLN B O 1 ATOM 3569 C CB . GLN A 1 461 ? 51.654 -36.572 -2.039 1.00 67.62 ? 492 GLN B CB 1 ATOM 3570 C CG . GLN A 1 461 ? 53.109 -36.525 -2.482 1.00 67.20 ? 492 GLN B CG 1 ATOM 3571 C CD . GLN A 1 461 ? 54.069 -36.882 -1.383 1.00 66.55 ? 492 GLN B CD 1 ATOM 3572 O OE1 . GLN A 1 461 ? 54.406 -38.045 -1.204 1.00 66.12 ? 492 GLN B OE1 1 ATOM 3573 N NE2 . GLN A 1 461 ? 54.526 -35.882 -0.642 1.00 66.48 ? 492 GLN B NE2 1 ATOM 3574 N N . ILE A 1 462 ? 48.649 -35.630 -2.017 1.00 67.80 ? 493 ILE B N 1 ATOM 3575 C CA . ILE A 1 462 ? 47.250 -35.779 -1.597 1.00 68.36 ? 493 ILE B CA 1 ATOM 3576 C C . ILE A 1 462 ? 46.269 -34.816 -2.297 1.00 69.23 ? 493 ILE B C 1 ATOM 3577 O O . ILE A 1 462 ? 46.554 -33.626 -2.429 1.00 69.73 ? 493 ILE B O 1 ATOM 3578 C CB . ILE A 1 462 ? 47.107 -35.653 -0.057 1.00 68.38 ? 493 ILE B CB 1 ATOM 3579 C CG1 . ILE A 1 462 ? 48.305 -36.277 0.649 1.00 67.49 ? 493 ILE B CG1 1 ATOM 3580 C CG2 . ILE A 1 462 ? 45.831 -36.315 0.428 1.00 68.90 ? 493 ILE B CG2 1 ATOM 3581 C CD1 . ILE A 1 462 ? 48.264 -36.102 2.129 1.00 67.46 ? 493 ILE B CD1 1 ATOM 3582 N N . PHE A 1 463 ? 45.120 -35.333 -2.745 1.00 72.04 ? 494 PHE B N 1 ATOM 3583 C CA . PHE A 1 463 ? 44.089 -34.488 -3.365 1.00 72.67 ? 494 PHE B CA 1 ATOM 3584 C C . PHE A 1 463 ? 42.664 -34.811 -2.931 1.00 73.73 ? 494 PHE B C 1 ATOM 3585 O O . PHE A 1 463 ? 42.173 -35.927 -3.166 1.00 73.86 ? 494 PHE B O 1 ATOM 3586 C CB . PHE A 1 463 ? 44.173 -34.590 -4.884 1.00 72.17 ? 494 PHE B CB 1 ATOM 3587 C CG . PHE A 1 463 ? 43.073 -33.861 -5.607 1.00 72.74 ? 494 PHE B CG 1 ATOM 3588 C CD1 . PHE A 1 463 ? 43.152 -32.501 -5.825 1.00 73.39 ? 494 PHE B CD1 1 ATOM 3589 C CD2 . PHE A 1 463 ? 41.970 -34.541 -6.097 1.00 73.21 ? 494 PHE B CD2 1 ATOM 3590 C CE1 . PHE A 1 463 ? 42.140 -31.830 -6.504 1.00 75.13 ? 494 PHE B CE1 1 ATOM 3591 C CE2 . PHE A 1 463 ? 40.957 -33.874 -6.780 1.00 73.96 ? 494 PHE B CE2 1 ATOM 3592 C CZ . PHE A 1 463 ? 41.043 -32.517 -6.981 1.00 75.43 ? 494 PHE B CZ 1 ATOM 3593 N N . SER A 1 464 ? 41.978 -33.848 -2.320 1.00 71.86 ? 495 SER B N 1 ATOM 3594 C CA . SER A 1 464 ? 40.595 -34.111 -1.917 1.00 72.46 ? 495 SER B CA 1 ATOM 3595 C C . SER A 1 464 ? 39.582 -33.049 -2.336 1.00 73.89 ? 495 SER B C 1 ATOM 3596 O O . SER A 1 464 ? 39.538 -31.966 -1.764 1.00 74.44 ? 495 SER B O 1 ATOM 3597 C CB . SER A 1 464 ? 40.525 -34.333 -0.394 1.00 72.01 ? 495 SER B CB 1 ATOM 3598 O OG . SER A 1 464 ? 39.306 -34.944 0.021 1.00 72.42 ? 495 SER B OG 1 ATOM 3599 N N . ALA A 1 465 ? 38.740 -33.396 -3.302 1.00 82.89 ? 496 ALA B N 1 ATOM 3600 C CA . ALA A 1 465 ? 37.601 -32.573 -3.706 1.00 83.85 ? 496 ALA B CA 1 ATOM 3601 C C . ALA A 1 465 ? 36.276 -33.056 -3.117 1.00 85.26 ? 496 ALA B C 1 ATOM 3602 O O . ALA A 1 465 ? 35.208 -32.566 -3.489 1.00 86.18 ? 496 ALA B O 1 ATOM 3603 C CB . ALA A 1 465 ? 37.517 -32.470 -5.215 1.00 83.26 ? 496 ALA B CB 1 ATOM 3604 N N . SER A 1 466 ? 36.357 -34.051 -2.237 1.00 73.85 ? 497 SER B N 1 ATOM 3605 C CA . SER A 1 466 ? 35.190 -34.758 -1.692 1.00 74.28 ? 497 SER B CA 1 ATOM 3606 C C . SER A 1 466 ? 34.089 -33.867 -1.120 1.00 75.64 ? 497 SER B C 1 ATOM 3607 O O . SER A 1 466 ? 34.353 -32.974 -0.332 1.00 75.83 ? 497 SER B O 1 ATOM 3608 C CB . SER A 1 466 ? 35.638 -35.735 -0.602 1.00 73.17 ? 497 SER B CB 1 ATOM 3609 O OG . SER A 1 466 ? 36.121 -35.049 0.547 1.00 72.98 ? 497 SER B OG 1 ATOM 3610 N N . PHE A 1 467 ? 32.852 -34.139 -1.517 1.00 76.60 ? 498 PHE B N 1 ATOM 3611 C CA . PHE A 1 467 ? 31.670 -33.424 -1.026 1.00 78.02 ? 498 PHE B CA 1 ATOM 3612 C C . PHE A 1 467 ? 31.564 -31.961 -1.387 1.00 79.06 ? 498 PHE B C 1 ATOM 3613 O O . PHE A 1 467 ? 30.900 -31.200 -0.688 1.00 80.07 ? 498 PHE B O 1 ATOM 3614 C CB . PHE A 1 467 ? 31.500 -33.584 0.480 1.00 77.92 ? 498 PHE B CB 1 ATOM 3615 C CG . PHE A 1 467 ? 31.160 -34.957 0.878 1.00 77.41 ? 498 PHE B CG 1 ATOM 3616 C CD1 . PHE A 1 467 ? 29.904 -35.460 0.622 1.00 78.37 ? 498 PHE B CD1 1 ATOM 3617 C CD2 . PHE A 1 467 ? 32.101 -35.767 1.468 1.00 76.04 ? 498 PHE B CD2 1 ATOM 3618 C CE1 . PHE A 1 467 ? 29.580 -36.755 0.964 1.00 77.95 ? 498 PHE B CE1 1 ATOM 3619 C CE2 . PHE A 1 467 ? 31.787 -37.065 1.814 1.00 75.62 ? 498 PHE B CE2 1 ATOM 3620 C CZ . PHE A 1 467 ? 30.521 -37.562 1.560 1.00 76.58 ? 498 PHE B CZ 1 ATOM 3621 N N . SER A 1 468 ? 32.195 -31.552 -2.474 1.00 105.06 ? 499 SER B N 1 ATOM 3622 C CA . SER A 1 468 ? 31.811 -30.271 -2.991 1.00 105.39 ? 499 SER B CA 1 ATOM 3623 C C . SER A 1 468 ? 31.124 -30.524 -4.295 1.00 105.25 ? 499 SER B C 1 ATOM 3624 O O . SER A 1 468 ? 31.790 -30.581 -5.327 1.00 103.93 ? 499 SER B O 1 ATOM 3625 C CB . SER A 1 468 ? 33.071 -29.487 -3.316 1.00 104.21 ? 499 SER B CB 1 ATOM 3626 O OG . SER A 1 468 ? 33.771 -30.129 -4.371 1.00 103.16 ? 499 SER B OG 1 ATOM 3627 N N . ASN A 1 469 ? 29.804 -30.686 -4.254 1.00 95.43 ? 500 ASN B N 1 ATOM 3628 C CA . ASN A 1 469 ? 28.912 -30.333 -5.349 1.00 95.83 ? 500 ASN B CA 1 ATOM 3629 C C . ASN A 1 469 ? 29.517 -30.459 -6.745 1.00 94.59 ? 500 ASN B C 1 ATOM 3630 O O . ASN A 1 469 ? 29.299 -29.616 -7.596 1.00 95.32 ? 500 ASN B O 1 ATOM 3631 C CB . ASN A 1 469 ? 28.228 -28.995 -5.084 1.00 96.65 ? 500 ASN B CB 1 ATOM 3632 C CG . ASN A 1 469 ? 27.323 -29.054 -3.860 1.00 97.91 ? 500 ASN B CG 1 ATOM 3633 O OD1 . ASN A 1 469 ? 27.613 -29.772 -2.899 1.00 95.56 ? 500 ASN B OD1 1 ATOM 3634 N ND2 . ASN A 1 469 ? 26.212 -28.323 -3.897 1.00 101.66 ? 500 ASN B ND2 1 ATOM 3635 N N . LEU A 1 470 ? 30.330 -31.489 -6.942 1.00 83.82 ? 501 LEU B N 1 ATOM 3636 C CA . LEU A 1 470 ? 30.999 -31.725 -8.213 1.00 83.54 ? 501 LEU B CA 1 ATOM 3637 C C . LEU A 1 470 ? 30.056 -32.403 -9.195 1.00 84.38 ? 501 LEU B C 1 ATOM 3638 O O . LEU A 1 470 ? 29.063 -33.023 -8.803 1.00 84.06 ? 501 LEU B O 1 ATOM 3639 C CB . LEU A 1 470 ? 32.256 -32.574 -8.016 1.00 81.47 ? 501 LEU B CB 1 ATOM 3640 C CG . LEU A 1 470 ? 33.577 -31.883 -7.690 1.00 81.02 ? 501 LEU B CG 1 ATOM 3641 C CD1 . LEU A 1 470 ? 34.651 -32.915 -7.436 1.00 79.31 ? 501 LEU B CD1 1 ATOM 3642 C CD2 . LEU A 1 470 ? 33.978 -30.987 -8.830 1.00 82.86 ? 501 LEU B CD2 1 ATOM 3643 N N . ILE A 1 471 ? 30.357 -32.270 -10.478 1.00 95.03 ? 502 ILE B N 1 ATOM 3644 C CA . ILE A 1 471 ? 29.556 -32.909 -11.505 1.00 95.79 ? 502 ILE B CA 1 ATOM 3645 C C . ILE A 1 471 ? 30.475 -33.205 -12.689 1.00 95.85 ? 502 ILE B C 1 ATOM 3646 O O . ILE A 1 471 ? 31.569 -32.651 -12.777 1.00 95.85 ? 502 ILE B O 1 ATOM 3647 C CB . ILE A 1 471 ? 28.338 -32.012 -11.877 1.00 98.03 ? 502 ILE B CB 1 ATOM 3648 C CG1 . ILE A 1 471 ? 27.556 -32.556 -13.085 1.00 99.20 ? 502 ILE B CG1 1 ATOM 3649 C CG2 . ILE A 1 471 ? 28.782 -30.570 -12.108 1.00 99.73 ? 502 ILE B CG2 1 ATOM 3650 C CD1 . ILE A 1 471 ? 26.870 -33.907 -12.876 1.00 98.03 ? 502 ILE B CD1 1 ATOM 3651 N N . GLY A 1 472 ? 30.068 -34.127 -13.553 1.00 96.06 ? 503 GLY B N 1 ATOM 3652 C CA . GLY A 1 472 ? 30.758 -34.349 -14.805 1.00 96.72 ? 503 GLY B CA 1 ATOM 3653 C C . GLY A 1 472 ? 31.688 -35.543 -14.831 1.00 94.82 ? 503 GLY B C 1 ATOM 3654 O O . GLY A 1 472 ? 31.913 -36.197 -13.819 1.00 92.87 ? 503 GLY B O 1 ATOM 3655 N N . GLU A 1 473 ? 32.234 -35.817 -16.012 1.00 100.06 ? 504 GLU B N 1 ATOM 3656 C CA . GLU A 1 473 ? 33.185 -36.905 -16.212 1.00 98.61 ? 504 GLU B CA 1 ATOM 3657 C C . GLU A 1 473 ? 34.466 -36.681 -15.380 1.00 97.23 ? 504 GLU B C 1 ATOM 3658 O O . GLU A 1 473 ? 34.815 -35.545 -15.040 1.00 97.87 ? 504 GLU B O 1 ATOM 3659 C CB . GLU A 1 473 ? 33.523 -37.043 -17.712 1.00 100.10 ? 504 GLU B CB 1 ATOM 3660 C CG . GLU A 1 473 ? 32.464 -36.478 -18.689 1.00 102.48 ? 504 GLU B CG 1 ATOM 3661 C CD . GLU A 1 473 ? 31.442 -37.517 -19.172 1.00 102.48 ? 504 GLU B CD 1 ATOM 3662 O OE1 . GLU A 1 473 ? 30.555 -37.162 -19.988 1.00 104.37 ? 504 GLU B OE1 1 ATOM 3663 O OE2 . GLU A 1 473 ? 31.524 -38.689 -18.741 1.00 100.66 ? 504 GLU B OE2 1 ATOM 3664 N N . ILE A 1 474 ? 35.147 -37.768 -15.033 1.00 81.63 ? 505 ILE B N 1 ATOM 3665 C CA . ILE A 1 474 ? 36.417 -37.686 -14.315 1.00 80.32 ? 505 ILE B CA 1 ATOM 3666 C C . ILE A 1 474 ? 37.582 -37.759 -15.288 1.00 80.93 ? 505 ILE B C 1 ATOM 3667 O O . ILE A 1 474 ? 37.854 -38.821 -15.838 1.00 80.48 ? 505 ILE B O 1 ATOM 3668 C CB . ILE A 1 474 ? 36.570 -38.840 -13.298 1.00 78.17 ? 505 ILE B CB 1 ATOM 3669 C CG1 . ILE A 1 474 ? 35.607 -38.670 -12.125 1.00 77.81 ? 505 ILE B CG1 1 ATOM 3670 C CG2 . ILE A 1 474 ? 37.993 -38.918 -12.774 1.00 77.01 ? 505 ILE B CG2 1 ATOM 3671 C CD1 . ILE A 1 474 ? 35.744 -39.748 -11.077 1.00 77.35 ? 505 ILE B CD1 1 ATOM 3672 N N . PRO A 1 475 ? 38.291 -36.638 -15.483 1.00 81.92 ? 506 PRO B N 1 ATOM 3673 C CA . PRO A 1 475 ? 39.363 -36.471 -16.474 1.00 82.94 ? 506 PRO B CA 1 ATOM 3674 C C . PRO A 1 475 ? 40.399 -37.590 -16.471 1.00 81.55 ? 506 PRO B C 1 ATOM 3675 O O . PRO A 1 475 ? 40.873 -37.958 -15.409 1.00 79.76 ? 506 PRO B O 1 ATOM 3676 C CB . PRO A 1 475 ? 40.032 -35.167 -16.039 1.00 83.47 ? 506 PRO B CB 1 ATOM 3677 C CG . PRO A 1 475 ? 39.475 -34.875 -14.679 1.00 82.26 ? 506 PRO B CG 1 ATOM 3678 C CD . PRO A 1 475 ? 38.101 -35.415 -14.706 1.00 82.28 ? 506 PRO B CD 1 ATOM 3679 N N . ASN A 1 476 ? 40.737 -38.105 -17.654 1.00 104.32 ? 507 ASN B N 1 ATOM 3680 C CA . ASN A 1 476 ? 41.669 -39.219 -17.786 1.00 103.29 ? 507 ASN B CA 1 ATOM 3681 C C . ASN A 1 476 ? 43.016 -38.877 -17.177 1.00 102.54 ? 507 ASN B C 1 ATOM 3682 O O . ASN A 1 476 ? 43.564 -37.801 -17.423 1.00 103.71 ? 507 ASN B O 1 ATOM 3683 C CB . ASN A 1 476 ? 41.841 -39.626 -19.253 1.00 104.86 ? 507 ASN B CB 1 ATOM 3684 C CG . ASN A 1 476 ? 40.560 -40.183 -19.868 1.00 105.45 ? 507 ASN B CG 1 ATOM 3685 O OD1 . ASN A 1 476 ? 39.466 -39.665 -19.630 1.00 105.83 ? 507 ASN B OD1 1 ATOM 3686 N ND2 . ASN A 1 476 ? 40.694 -41.248 -20.663 1.00 105.58 ? 507 ASN B ND2 1 ATOM 3687 N N . TYR A 1 477 ? 43.554 -39.809 -16.394 1.00 92.11 ? 508 TYR B N 1 ATOM 3688 C CA . TYR A 1 477 ? 44.759 -39.549 -15.623 1.00 91.17 ? 508 TYR B CA 1 ATOM 3689 C C . TYR A 1 477 ? 45.909 -39.633 -16.588 1.00 92.25 ? 508 TYR B C 1 ATOM 3690 O O . TYR A 1 477 ? 46.242 -40.693 -17.107 1.00 92.11 ? 508 TYR B O 1 ATOM 3691 C CB . TYR A 1 477 ? 44.931 -40.617 -14.541 1.00 88.96 ? 508 TYR B CB 1 ATOM 3692 C CG . TYR A 1 477 ? 43.741 -40.761 -13.604 1.00 87.89 ? 508 TYR B CG 1 ATOM 3693 C CD1 . TYR A 1 477 ? 42.647 -41.545 -13.946 1.00 87.92 ? 508 TYR B CD1 1 ATOM 3694 C CD2 . TYR A 1 477 ? 43.721 -40.125 -12.366 1.00 87.10 ? 508 TYR B CD2 1 ATOM 3695 C CE1 . TYR A 1 477 ? 41.564 -41.667 -13.094 1.00 87.32 ? 508 TYR B CE1 1 ATOM 3696 C CE2 . TYR A 1 477 ? 42.645 -40.248 -11.511 1.00 86.54 ? 508 TYR B CE2 1 ATOM 3697 C CZ . TYR A 1 477 ? 41.574 -41.019 -11.881 1.00 86.71 ? 508 TYR B CZ 1 ATOM 3698 O OH . TYR A 1 477 ? 40.506 -41.138 -11.033 1.00 87.34 ? 508 TYR B OH 1 ATOM 3699 N N . VAL A 1 478 ? 46.555 -38.509 -16.802 1.00 132.62 ? 509 VAL B N 1 ATOM 3700 C CA . VAL A 1 478 ? 47.567 -38.475 -17.819 1.00 134.00 ? 509 VAL B CA 1 ATOM 3701 C C . VAL A 1 478 ? 48.885 -38.341 -17.091 1.00 133.09 ? 509 VAL B C 1 ATOM 3702 O O . VAL A 1 478 ? 49.199 -37.293 -16.532 1.00 133.14 ? 509 VAL B O 1 ATOM 3703 C CB . VAL A 1 478 ? 47.284 -37.343 -18.832 1.00 136.39 ? 509 VAL B CB 1 ATOM 3704 C CG1 . VAL A 1 478 ? 46.523 -36.197 -18.169 1.00 136.51 ? 509 VAL B CG1 1 ATOM 3705 C CG2 . VAL A 1 478 ? 48.553 -36.878 -19.509 1.00 137.74 ? 509 VAL B CG2 1 ATOM 3706 N N . GLY A 1 479 ? 49.635 -39.437 -17.080 1.00 101.77 ? 510 GLY B N 1 ATOM 3707 C CA . GLY A 1 479 ? 50.894 -39.505 -16.364 1.00 100.80 ? 510 GLY B CA 1 ATOM 3708 C C . GLY A 1 479 ? 50.739 -39.205 -14.891 1.00 99.01 ? 510 GLY B C 1 ATOM 3709 O O . GLY A 1 479 ? 51.420 -38.334 -14.352 1.00 98.96 ? 510 GLY B O 1 ATOM 3710 N N . CYS A 1 480 ? 49.827 -39.913 -14.242 1.00 90.56 ? 511 CYS B N 1 ATOM 3711 C CA . CYS A 1 480 ? 49.636 -39.737 -12.817 1.00 88.88 ? 511 CYS B CA 1 ATOM 3712 C C . CYS A 1 480 ? 50.990 -39.984 -12.191 1.00 87.95 ? 511 CYS B C 1 ATOM 3713 O O . CYS A 1 480 ? 51.586 -41.040 -12.405 1.00 87.59 ? 511 CYS B O 1 ATOM 3714 C CB . CYS A 1 480 ? 48.632 -40.767 -12.307 1.00 87.58 ? 511 CYS B CB 1 ATOM 3715 S SG . CYS A 1 480 ? 47.905 -40.430 -10.699 1.00 86.29 ? 511 CYS B SG 1 ATOM 3716 N N . LYS A 1 481 ? 51.493 -39.013 -11.437 1.00 81.80 ? 512 LYS B N 1 ATOM 3717 C CA . LYS A 1 481 ? 52.865 -39.121 -10.968 1.00 81.20 ? 512 LYS B CA 1 ATOM 3718 C C . LYS A 1 481 ? 52.993 -39.427 -9.502 1.00 79.57 ? 512 LYS B C 1 ATOM 3719 O O . LYS A 1 481 ? 53.332 -40.542 -9.123 1.00 78.87 ? 512 LYS B O 1 ATOM 3720 C CB . LYS A 1 481 ? 53.669 -37.861 -11.281 1.00 82.46 ? 512 LYS B CB 1 ATOM 3721 C CG . LYS A 1 481 ? 55.092 -37.952 -10.763 1.00 81.88 ? 512 LYS B CG 1 ATOM 3722 C CD . LYS A 1 481 ? 56.016 -36.993 -11.467 1.00 83.51 ? 512 LYS B CD 1 ATOM 3723 C CE . LYS A 1 481 ? 57.330 -36.860 -10.712 1.00 82.81 ? 512 LYS B CE 1 ATOM 3724 N NZ . LYS A 1 481 ? 58.064 -35.601 -11.070 1.00 84.23 ? 512 LYS B NZ 1 ATOM 3725 N N . SER A 1 482 ? 52.739 -38.416 -8.686 1.00 72.34 ? 513 SER B N 1 ATOM 3726 C CA . SER A 1 482 ? 53.090 -38.477 -7.279 1.00 71.54 ? 513 SER B CA 1 ATOM 3727 C C . SER A 1 482 ? 51.946 -38.832 -6.311 1.00 71.71 ? 513 SER B C 1 ATOM 3728 O O . SER A 1 482 ? 52.171 -38.969 -5.112 1.00 71.67 ? 513 SER B O 1 ATOM 3729 C CB . SER A 1 482 ? 53.767 -37.167 -6.891 1.00 71.73 ? 513 SER B CB 1 ATOM 3730 O OG . SER A 1 482 ? 54.632 -36.753 -7.937 1.00 72.31 ? 513 SER B OG 1 ATOM 3731 N N . PHE A 1 483 ? 50.742 -39.021 -6.843 1.00 67.74 ? 514 PHE B N 1 ATOM 3732 C CA . PHE A 1 483 ? 49.531 -39.120 -6.031 1.00 68.18 ? 514 PHE B CA 1 ATOM 3733 C C . PHE A 1 483 ? 49.501 -40.377 -5.196 1.00 67.84 ? 514 PHE B C 1 ATOM 3734 O O . PHE A 1 483 ? 49.569 -41.466 -5.752 1.00 67.51 ? 514 PHE B O 1 ATOM 3735 C CB . PHE A 1 483 ? 48.317 -39.202 -6.960 1.00 68.64 ? 514 PHE B CB 1 ATOM 3736 C CG . PHE A 1 483 ? 47.883 -37.885 -7.520 1.00 69.32 ? 514 PHE B CG 1 ATOM 3737 C CD1 . PHE A 1 483 ? 48.776 -37.070 -8.190 1.00 70.50 ? 514 PHE B CD1 1 ATOM 3738 C CD2 . PHE A 1 483 ? 46.576 -37.465 -7.386 1.00 69.73 ? 514 PHE B CD2 1 ATOM 3739 C CE1 . PHE A 1 483 ? 48.374 -35.856 -8.696 1.00 72.04 ? 514 PHE B CE1 1 ATOM 3740 C CE2 . PHE A 1 483 ? 46.174 -36.259 -7.890 1.00 71.28 ? 514 PHE B CE2 1 ATOM 3741 C CZ . PHE A 1 483 ? 47.069 -35.455 -8.550 1.00 72.44 ? 514 PHE B CZ 1 ATOM 3742 N N . TYR A 1 484 ? 49.432 -40.260 -3.869 1.00 73.73 ? 515 TYR B N 1 ATOM 3743 C CA . TYR A 1 484 ? 49.028 -41.418 -3.064 1.00 73.77 ? 515 TYR B CA 1 ATOM 3744 C C . TYR A 1 484 ? 47.605 -41.479 -2.465 1.00 74.59 ? 515 TYR B C 1 ATOM 3745 O O . TYR A 1 484 ? 47.155 -42.560 -2.105 1.00 74.75 ? 515 TYR B O 1 ATOM 3746 C CB . TYR A 1 484 ? 50.095 -41.779 -2.017 1.00 73.39 ? 515 TYR B CB 1 ATOM 3747 C CG . TYR A 1 484 ? 50.134 -40.927 -0.774 1.00 73.60 ? 515 TYR B CG 1 ATOM 3748 C CD1 . TYR A 1 484 ? 49.158 -41.038 0.196 1.00 74.05 ? 515 TYR B CD1 1 ATOM 3749 C CD2 . TYR A 1 484 ? 51.177 -40.054 -0.549 1.00 73.40 ? 515 TYR B CD2 1 ATOM 3750 C CE1 . TYR A 1 484 ? 49.194 -40.279 1.328 1.00 74.28 ? 515 TYR B CE1 1 ATOM 3751 C CE2 . TYR A 1 484 ? 51.224 -39.295 0.586 1.00 73.57 ? 515 TYR B CE2 1 ATOM 3752 C CZ . TYR A 1 484 ? 50.228 -39.411 1.521 1.00 74.00 ? 515 TYR B CZ 1 ATOM 3753 O OH . TYR A 1 484 ? 50.263 -38.652 2.663 1.00 74.20 ? 515 TYR B OH 1 ATOM 3754 N N . ARG A 1 485 ? 46.888 -40.361 -2.372 1.00 73.77 ? 516 ARG B N 1 ATOM 3755 C CA . ARG A 1 485 ? 45.565 -40.378 -1.726 1.00 74.74 ? 516 ARG B CA 1 ATOM 3756 C C . ARG A 1 485 ? 44.593 -39.496 -2.485 1.00 75.36 ? 516 ARG B C 1 ATOM 3757 O O . ARG A 1 485 ? 44.857 -38.307 -2.680 1.00 75.35 ? 516 ARG B O 1 ATOM 3758 C CB . ARG A 1 485 ? 45.639 -39.967 -0.236 1.00 75.16 ? 516 ARG B CB 1 ATOM 3759 C CG . ARG A 1 485 ? 44.510 -40.545 0.670 1.00 75.98 ? 516 ARG B CG 1 ATOM 3760 C CD . ARG A 1 485 ? 44.922 -40.648 2.162 1.00 75.93 ? 516 ARG B CD 1 ATOM 3761 N NE . ARG A 1 485 ? 44.399 -41.847 2.846 1.00 76.57 ? 516 ARG B NE 1 ATOM 3762 C CZ . ARG A 1 485 ? 44.995 -43.057 2.867 1.00 76.76 ? 516 ARG B CZ 1 ATOM 3763 N NH1 . ARG A 1 485 ? 46.136 -43.265 2.216 1.00 76.29 ? 516 ARG B NH1 1 ATOM 3764 N NH2 . ARG A 1 485 ? 44.444 -44.092 3.514 1.00 77.52 ? 516 ARG B NH2 1 ATOM 3765 N N . ILE A 1 486 ? 43.472 -40.075 -2.916 1.00 66.25 ? 517 ILE B N 1 ATOM 3766 C CA . ILE A 1 486 ? 42.475 -39.336 -3.713 1.00 67.36 ? 517 ILE B CA 1 ATOM 3767 C C . ILE A 1 486 ? 41.037 -39.458 -3.190 1.00 67.95 ? 517 ILE B C 1 ATOM 3768 O O . ILE A 1 486 ? 40.445 -40.550 -3.208 1.00 67.78 ? 517 ILE B O 1 ATOM 3769 C CB . ILE A 1 486 ? 42.488 -39.789 -5.186 1.00 67.66 ? 517 ILE B CB 1 ATOM 3770 C CG1 . ILE A 1 486 ? 43.901 -39.701 -5.753 1.00 67.28 ? 517 ILE B CG1 1 ATOM 3771 C CG2 . ILE A 1 486 ? 41.535 -38.957 -5.994 1.00 68.82 ? 517 ILE B CG2 1 ATOM 3772 C CD1 . ILE A 1 486 ? 44.031 -40.223 -7.129 1.00 68.06 ? 517 ILE B CD1 1 ATOM 3773 N N . GLU A 1 487 ? 40.456 -38.358 -2.725 1.00 77.09 ? 518 GLU B N 1 ATOM 3774 C CA . GLU A 1 487 ? 39.063 -38.465 -2.309 1.00 78.49 ? 518 GLU B CA 1 ATOM 3775 C C . GLU A 1 487 ? 38.166 -37.619 -3.195 1.00 79.11 ? 518 GLU B C 1 ATOM 3776 O O . GLU A 1 487 ? 38.134 -36.398 -3.066 1.00 79.47 ? 518 GLU B O 1 ATOM 3777 C CB . GLU A 1 487 ? 38.909 -38.054 -0.847 1.00 79.41 ? 518 GLU B CB 1 ATOM 3778 C CG . GLU A 1 487 ? 39.619 -38.965 0.134 1.00 79.05 ? 518 GLU B CG 1 ATOM 3779 C CD . GLU A 1 487 ? 40.161 -38.206 1.332 1.00 79.25 ? 518 GLU B CD 1 ATOM 3780 O OE1 . GLU A 1 487 ? 39.694 -37.070 1.584 1.00 79.97 ? 518 GLU B OE1 1 ATOM 3781 O OE2 . GLU A 1 487 ? 41.064 -38.747 2.011 1.00 78.67 ? 518 GLU B OE2 1 ATOM 3782 N N . LEU A 1 488 ? 37.453 -38.281 -4.104 1.00 76.73 ? 519 LEU B N 1 ATOM 3783 C CA . LEU A 1 488 ? 36.478 -37.635 -4.996 1.00 77.36 ? 519 LEU B CA 1 ATOM 3784 C C . LEU A 1 488 ? 35.002 -37.850 -4.627 1.00 78.90 ? 519 LEU B C 1 ATOM 3785 O O . LEU A 1 488 ? 34.103 -37.442 -5.361 1.00 79.48 ? 519 LEU B O 1 ATOM 3786 C CB . LEU A 1 488 ? 36.776 -37.942 -6.464 1.00 76.37 ? 519 LEU B CB 1 ATOM 3787 C CG . LEU A 1 488 ? 38.027 -37.198 -6.918 1.00 75.42 ? 519 LEU B CG 1 ATOM 3788 C CD1 . LEU A 1 488 ? 38.544 -37.738 -8.210 1.00 74.41 ? 519 LEU B CD1 1 ATOM 3789 C CD2 . LEU A 1 488 ? 37.684 -35.756 -7.067 1.00 76.22 ? 519 LEU B CD2 1 ATOM 3790 N N . GLN A 1 489 ? 34.774 -38.503 -3.495 1.00 85.25 ? 520 GLN B N 1 ATOM 3791 C CA . GLN A 1 489 ? 33.458 -38.995 -3.097 1.00 86.64 ? 520 GLN B CA 1 ATOM 3792 C C . GLN A 1 489 ? 32.381 -37.949 -2.793 1.00 88.25 ? 520 GLN B C 1 ATOM 3793 O O . GLN A 1 489 ? 32.682 -36.776 -2.583 1.00 88.55 ? 520 GLN B O 1 ATOM 3794 C CB . GLN A 1 489 ? 33.652 -39.852 -1.869 1.00 86.96 ? 520 GLN B CB 1 ATOM 3795 C CG . GLN A 1 489 ? 35.084 -39.856 -1.448 1.00 85.94 ? 520 GLN B CG 1 ATOM 3796 C CD . GLN A 1 489 ? 35.290 -39.243 -0.115 1.00 86.06 ? 520 GLN B CD 1 ATOM 3797 O OE1 . GLN A 1 489 ? 34.414 -38.556 0.392 1.00 87.05 ? 520 GLN B OE1 1 ATOM 3798 N NE2 . GLN A 1 489 ? 36.446 -39.494 0.483 1.00 85.12 ? 520 GLN B NE2 1 ATOM 3799 N N . GLY A 1 490 ? 31.122 -38.396 -2.811 1.00 92.99 ? 521 GLY B N 1 ATOM 3800 C CA . GLY A 1 490 ? 29.991 -37.641 -2.284 1.00 94.43 ? 521 GLY B CA 1 ATOM 3801 C C . GLY A 1 490 ? 29.355 -36.613 -3.198 1.00 94.51 ? 521 GLY B C 1 ATOM 3802 O O . GLY A 1 490 ? 28.741 -35.644 -2.738 1.00 95.32 ? 521 GLY B O 1 ATOM 3803 N N . ASN A 1 491 ? 29.462 -36.850 -4.499 1.00 78.77 ? 522 ASN B N 1 ATOM 3804 C CA . ASN A 1 491 ? 29.159 -35.828 -5.490 1.00 79.46 ? 522 ASN B CA 1 ATOM 3805 C C . ASN A 1 491 ? 28.124 -36.246 -6.520 1.00 80.30 ? 522 ASN B C 1 ATOM 3806 O O . ASN A 1 491 ? 27.427 -37.241 -6.359 1.00 80.31 ? 522 ASN B O 1 ATOM 3807 C CB . ASN A 1 491 ? 30.448 -35.386 -6.178 1.00 78.71 ? 522 ASN B CB 1 ATOM 3808 C CG . ASN A 1 491 ? 31.400 -34.697 -5.223 1.00 78.14 ? 522 ASN B CG 1 ATOM 3809 O OD1 . ASN A 1 491 ? 30.989 -33.843 -4.441 1.00 78.62 ? 522 ASN B OD1 1 ATOM 3810 N ND2 . ASN A 1 491 ? 32.673 -35.070 -5.270 1.00 77.13 ? 522 ASN B ND2 1 ATOM 3811 N N . SER A 1 492 ? 27.959 -35.413 -7.531 1.00 85.80 ? 523 SER B N 1 ATOM 3812 C CA . SER A 1 492 ? 27.163 -35.779 -8.689 1.00 85.87 ? 523 SER B CA 1 ATOM 3813 C C . SER A 1 492 ? 27.915 -36.271 -9.945 1.00 84.42 ? 523 SER B C 1 ATOM 3814 O O . SER A 1 492 ? 27.322 -36.336 -11.019 1.00 84.52 ? 523 SER B O 1 ATOM 3815 C CB . SER A 1 492 ? 26.078 -34.749 -8.975 1.00 86.91 ? 523 SER B CB 1 ATOM 3816 O OG . SER A 1 492 ? 25.035 -34.911 -8.023 1.00 88.44 ? 523 SER B OG 1 ATOM 3817 N N . LEU A 1 493 ? 29.217 -36.546 -9.819 1.00 80.95 ? 524 LEU B N 1 ATOM 3818 C CA . LEU A 1 493 ? 30.042 -37.021 -10.947 1.00 80.92 ? 524 LEU B CA 1 ATOM 3819 C C . LEU A 1 493 ? 29.438 -38.214 -11.677 1.00 80.79 ? 524 LEU B C 1 ATOM 3820 O O . LEU A 1 493 ? 29.128 -39.233 -11.057 1.00 79.39 ? 524 LEU B O 1 ATOM 3821 C CB . LEU A 1 493 ? 31.440 -37.457 -10.484 1.00 79.13 ? 524 LEU B CB 1 ATOM 3822 C CG . LEU A 1 493 ? 32.402 -36.580 -9.673 1.00 78.65 ? 524 LEU B CG 1 ATOM 3823 C CD1 . LEU A 1 493 ? 33.700 -37.308 -9.438 1.00 76.93 ? 524 LEU B CD1 1 ATOM 3824 C CD2 . LEU A 1 493 ? 32.702 -35.271 -10.352 1.00 80.46 ? 524 LEU B CD2 1 ATOM 3825 N N . ASN A 1 494 ? 29.315 -38.090 -13.000 1.00 100.58 ? 525 ASN B N 1 ATOM 3826 C CA . ASN A 1 494 ? 28.802 -39.156 -13.866 1.00 100.65 ? 525 ASN B CA 1 ATOM 3827 C C . ASN A 1 494 ? 29.902 -39.668 -14.787 1.00 100.17 ? 525 ASN B C 1 ATOM 3828 O O . ASN A 1 494 ? 31.056 -39.279 -14.660 1.00 99.69 ? 525 ASN B O 1 ATOM 3829 C CB . ASN A 1 494 ? 27.561 -38.697 -14.665 1.00 102.55 ? 525 ASN B CB 1 ATOM 3830 C CG . ASN A 1 494 ? 27.853 -37.540 -15.635 1.00 104.33 ? 525 ASN B CG 1 ATOM 3831 O OD1 . ASN A 1 494 ? 28.895 -36.896 -15.548 1.00 104.24 ? 525 ASN B OD1 1 ATOM 3832 N ND2 . ASN A 1 494 ? 26.917 -37.273 -16.557 1.00 106.28 ? 525 ASN B ND2 1 ATOM 3833 N N . GLY A 1 495 ? 29.559 -40.558 -15.703 1.00 119.55 ? 526 GLY B N 1 ATOM 3834 C CA . GLY A 1 495 ? 30.550 -41.048 -16.636 1.00 119.35 ? 526 GLY B CA 1 ATOM 3835 C C . GLY A 1 495 ? 31.256 -42.253 -16.064 1.00 117.43 ? 526 GLY B C 1 ATOM 3836 O O . GLY A 1 495 ? 30.730 -42.906 -15.160 1.00 116.49 ? 526 GLY B O 1 ATOM 3837 N N . THR A 1 496 ? 32.448 -42.548 -16.580 1.00 88.09 ? 527 THR B N 1 ATOM 3838 C CA . THR A 1 496 ? 33.149 -43.782 -16.210 1.00 86.49 ? 527 THR B CA 1 ATOM 3839 C C . THR A 1 496 ? 34.553 -43.569 -15.633 1.00 85.51 ? 527 THR B C 1 ATOM 3840 O O . THR A 1 496 ? 35.196 -42.547 -15.896 1.00 86.22 ? 527 THR B O 1 ATOM 3841 C CB . THR A 1 496 ? 33.262 -44.732 -17.406 1.00 86.79 ? 527 THR B CB 1 ATOM 3842 O OG1 . THR A 1 496 ? 34.097 -44.140 -18.409 1.00 88.15 ? 527 THR B OG1 1 ATOM 3843 C CG2 . THR A 1 496 ? 31.894 -44.991 -17.978 1.00 87.77 ? 527 THR B CG2 1 ATOM 3844 N N . ILE A 1 497 ? 35.016 -44.553 -14.857 1.00 75.44 ? 528 ILE B N 1 ATOM 3845 C CA . ILE A 1 497 ? 36.359 -44.541 -14.272 1.00 74.36 ? 528 ILE B CA 1 ATOM 3846 C C . ILE A 1 497 ? 37.404 -44.817 -15.339 1.00 75.00 ? 528 ILE B C 1 ATOM 3847 O O . ILE A 1 497 ? 37.450 -45.906 -15.895 1.00 74.82 ? 528 ILE B O 1 ATOM 3848 C CB . ILE A 1 497 ? 36.537 -45.625 -13.179 1.00 73.96 ? 528 ILE B CB 1 ATOM 3849 C CG1 . ILE A 1 497 ? 35.577 -45.417 -12.006 1.00 74.90 ? 528 ILE B CG1 1 ATOM 3850 C CG2 . ILE A 1 497 ? 37.959 -45.625 -12.675 1.00 73.44 ? 528 ILE B CG2 1 ATOM 3851 C CD1 . ILE A 1 497 ? 34.243 -46.105 -12.176 1.00 76.88 ? 528 ILE B CD1 1 ATOM 3852 N N . PRO A 1 498 ? 38.270 -43.845 -15.604 1.00 75.80 ? 529 PRO B N 1 ATOM 3853 C CA . PRO A 1 498 ? 39.187 -43.883 -16.737 1.00 76.87 ? 529 PRO B CA 1 ATOM 3854 C C . PRO A 1 498 ? 40.009 -45.142 -16.962 1.00 76.06 ? 529 PRO B C 1 ATOM 3855 O O . PRO A 1 498 ? 40.545 -45.788 -16.073 1.00 74.47 ? 529 PRO B O 1 ATOM 3856 C CB . PRO A 1 498 ? 40.109 -42.698 -16.467 1.00 77.25 ? 529 PRO B CB 1 ATOM 3857 C CG . PRO A 1 498 ? 39.210 -41.712 -15.851 1.00 77.51 ? 529 PRO B CG 1 ATOM 3858 C CD . PRO A 1 498 ? 38.270 -42.523 -14.968 1.00 76.10 ? 529 PRO B CD 1 ATOM 3859 N N . TRP A 1 499 ? 40.098 -45.428 -18.250 1.00 104.97 ? 530 TRP B N 1 ATOM 3860 C CA . TRP A 1 499 ? 40.893 -46.475 -18.844 1.00 104.89 ? 530 TRP B CA 1 ATOM 3861 C C . TRP A 1 499 ? 42.313 -46.522 -18.274 1.00 104.03 ? 530 TRP B C 1 ATOM 3862 O O . TRP A 1 499 ? 42.834 -47.589 -17.968 1.00 102.96 ? 530 TRP B O 1 ATOM 3863 C CB . TRP A 1 499 ? 40.930 -46.156 -20.344 1.00 107.03 ? 530 TRP B CB 1 ATOM 3864 C CG . TRP A 1 499 ? 41.629 -47.110 -21.189 1.00 107.46 ? 530 TRP B CG 1 ATOM 3865 C CD1 . TRP A 1 499 ? 42.619 -46.836 -22.073 1.00 108.84 ? 530 TRP B CD1 1 ATOM 3866 C CD2 . TRP A 1 499 ? 41.393 -48.513 -21.260 1.00 106.66 ? 530 TRP B CD2 1 ATOM 3867 N NE1 . TRP A 1 499 ? 43.025 -47.985 -22.696 1.00 108.96 ? 530 TRP B NE1 1 ATOM 3868 C CE2 . TRP A 1 499 ? 42.287 -49.034 -22.212 1.00 107.61 ? 530 TRP B CE2 1 ATOM 3869 C CE3 . TRP A 1 499 ? 40.513 -49.388 -20.605 1.00 105.30 ? 530 TRP B CE3 1 ATOM 3870 C CZ2 . TRP A 1 499 ? 42.332 -50.390 -22.529 1.00 107.26 ? 530 TRP B CZ2 1 ATOM 3871 C CZ3 . TRP A 1 499 ? 40.556 -50.736 -20.920 1.00 104.91 ? 530 TRP B CZ3 1 ATOM 3872 C CH2 . TRP A 1 499 ? 41.458 -51.223 -21.877 1.00 105.89 ? 530 TRP B CH2 1 ATOM 3873 N N . ASP A 1 500 ? 42.916 -45.353 -18.088 1.00 97.09 ? 531 ASP B N 1 ATOM 3874 C CA . ASP A 1 500 ? 44.349 -45.250 -17.822 1.00 96.75 ? 531 ASP B CA 1 ATOM 3875 C C . ASP A 1 500 ? 44.739 -45.206 -16.354 1.00 94.92 ? 531 ASP B C 1 ATOM 3876 O O . ASP A 1 500 ? 45.906 -44.998 -16.044 1.00 94.64 ? 531 ASP B O 1 ATOM 3877 C CB . ASP A 1 500 ? 44.959 -44.051 -18.562 1.00 98.50 ? 531 ASP B CB 1 ATOM 3878 C CG . ASP A 1 500 ? 44.185 -42.771 -18.339 1.00 99.16 ? 531 ASP B CG 1 ATOM 3879 O OD1 . ASP A 1 500 ? 43.407 -42.711 -17.368 1.00 98.01 ? 531 ASP B OD1 1 ATOM 3880 O OD2 . ASP A 1 500 ? 44.356 -41.824 -19.135 1.00 100.94 ? 531 ASP B OD2 1 ATOM 3881 N N . ILE A 1 501 ? 43.780 -45.412 -15.456 1.00 73.62 ? 532 ILE B N 1 ATOM 3882 C CA . ILE A 1 501 ? 44.004 -45.208 -14.014 1.00 72.05 ? 532 ILE B CA 1 ATOM 3883 C C . ILE A 1 501 ? 45.214 -45.980 -13.475 1.00 70.90 ? 532 ILE B C 1 ATOM 3884 O O . ILE A 1 501 ? 45.730 -45.674 -12.416 1.00 69.86 ? 532 ILE B O 1 ATOM 3885 C CB . ILE A 1 501 ? 42.756 -45.584 -13.186 1.00 71.02 ? 532 ILE B CB 1 ATOM 3886 C CG1 . ILE A 1 501 ? 42.571 -44.638 -12.007 1.00 71.28 ? 532 ILE B CG1 1 ATOM 3887 C CG2 . ILE A 1 501 ? 42.866 -47.000 -12.690 1.00 70.55 ? 532 ILE B CG2 1 ATOM 3888 C CD1 . ILE A 1 501 ? 42.949 -45.237 -10.660 1.00 70.85 ? 532 ILE B CD1 1 ATOM 3889 N N . GLY A 1 502 ? 45.693 -46.958 -14.227 1.00 85.37 ? 533 GLY B N 1 ATOM 3890 C CA . GLY A 1 502 ? 46.853 -47.721 -13.817 1.00 84.59 ? 533 GLY B CA 1 ATOM 3891 C C . GLY A 1 502 ? 48.117 -46.905 -13.943 1.00 85.04 ? 533 GLY B C 1 ATOM 3892 O O . GLY A 1 502 ? 49.226 -47.427 -13.892 1.00 84.79 ? 533 GLY B O 1 ATOM 3893 N N . HIS A 1 503 ? 47.935 -45.611 -14.155 1.00 72.89 ? 534 HIS B N 1 ATOM 3894 C CA . HIS A 1 503 ? 49.044 -44.686 -14.286 1.00 73.62 ? 534 HIS B CA 1 ATOM 3895 C C . HIS A 1 503 ? 49.520 -44.160 -12.950 1.00 72.32 ? 534 HIS B C 1 ATOM 3896 O O . HIS A 1 503 ? 50.618 -43.611 -12.855 1.00 72.58 ? 534 HIS B O 1 ATOM 3897 C CB . HIS A 1 503 ? 48.658 -43.513 -15.189 1.00 75.41 ? 534 HIS B CB 1 ATOM 3898 C CG . HIS A 1 503 ? 49.033 -43.713 -16.622 1.00 77.15 ? 534 HIS B CG 1 ATOM 3899 N ND1 . HIS A 1 503 ? 49.692 -42.751 -17.359 1.00 78.80 ? 534 HIS B ND1 1 ATOM 3900 C CD2 . HIS A 1 503 ? 48.864 -44.773 -17.448 1.00 77.59 ? 534 HIS B CD2 1 ATOM 3901 C CE1 . HIS A 1 503 ? 49.905 -43.208 -18.580 1.00 80.21 ? 534 HIS B CE1 1 ATOM 3902 N NE2 . HIS A 1 503 ? 49.413 -44.433 -18.660 1.00 79.50 ? 534 HIS B NE2 1 ATOM 3903 N N . CYS A 1 504 ? 48.708 -44.331 -11.916 1.00 71.73 ? 535 CYS B N 1 ATOM 3904 C CA . CYS A 1 504 ? 49.112 -43.843 -10.622 1.00 71.19 ? 535 CYS B CA 1 ATOM 3905 C C . CYS A 1 504 ? 49.636 -45.043 -9.891 1.00 70.58 ? 535 CYS B C 1 ATOM 3906 O O . CYS A 1 504 ? 48.863 -45.799 -9.323 1.00 70.65 ? 535 CYS B O 1 ATOM 3907 C CB . CYS A 1 504 ? 47.891 -43.310 -9.892 1.00 71.60 ? 535 CYS B CB 1 ATOM 3908 S SG . CYS A 1 504 ? 46.901 -42.194 -10.891 1.00 72.32 ? 535 CYS B SG 1 ATOM 3909 N N . GLU A 1 505 ? 50.959 -45.169 -9.837 1.00 71.93 ? 536 GLU B N 1 ATOM 3910 C CA . GLU A 1 505 ? 51.584 -46.357 -9.286 1.00 71.57 ? 536 GLU B CA 1 ATOM 3911 C C . GLU A 1 505 ? 51.561 -46.245 -7.767 1.00 71.67 ? 536 GLU B C 1 ATOM 3912 O O . GLU A 1 505 ? 51.430 -47.244 -7.048 1.00 71.65 ? 536 GLU B O 1 ATOM 3913 C CB . GLU A 1 505 ? 53.013 -46.517 -9.823 1.00 71.54 ? 536 GLU B CB 1 ATOM 3914 C CG . GLU A 1 505 ? 53.128 -46.448 -11.346 1.00 72.33 ? 536 GLU B CG 1 ATOM 3915 C CD . GLU A 1 505 ? 53.155 -47.817 -12.066 1.00 72.41 ? 536 GLU B CD 1 ATOM 3916 O OE1 . GLU A 1 505 ? 53.279 -48.874 -11.410 1.00 71.75 ? 536 GLU B OE1 1 ATOM 3917 O OE2 . GLU A 1 505 ? 53.060 -47.841 -13.319 1.00 73.64 ? 536 GLU B OE2 1 ATOM 3918 N N . LYS A 1 506 ? 51.637 -45.004 -7.298 1.00 76.42 ? 537 LYS B N 1 ATOM 3919 C CA . LYS A 1 506 ? 51.793 -44.707 -5.882 1.00 76.48 ? 537 LYS B CA 1 ATOM 3920 C C . LYS A 1 506 ? 50.463 -44.543 -5.159 1.00 77.07 ? 537 LYS B C 1 ATOM 3921 O O . LYS A 1 506 ? 50.421 -44.191 -3.982 1.00 77.36 ? 537 LYS B O 1 ATOM 3922 C CB . LYS A 1 506 ? 52.660 -43.467 -5.703 1.00 76.41 ? 537 LYS B CB 1 ATOM 3923 C CG . LYS A 1 506 ? 53.935 -43.544 -6.500 1.00 76.06 ? 537 LYS B CG 1 ATOM 3924 C CD . LYS A 1 506 ? 55.075 -42.850 -5.790 1.00 75.55 ? 537 LYS B CD 1 ATOM 3925 C CE . LYS A 1 506 ? 56.389 -43.014 -6.554 1.00 75.11 ? 537 LYS B CE 1 ATOM 3926 N NZ . LYS A 1 506 ? 57.530 -42.333 -5.864 1.00 74.63 ? 537 LYS B NZ 1 ATOM 3927 N N . LEU A 1 507 ? 49.377 -44.799 -5.874 1.00 63.47 ? 538 LEU B N 1 ATOM 3928 C CA . LEU A 1 507 ? 48.039 -44.657 -5.316 1.00 63.52 ? 538 LEU B CA 1 ATOM 3929 C C . LEU A 1 507 ? 47.746 -45.694 -4.227 1.00 62.80 ? 538 LEU B C 1 ATOM 3930 O O . LEU A 1 507 ? 47.980 -46.896 -4.433 1.00 62.43 ? 538 LEU B O 1 ATOM 3931 C CB . LEU A 1 507 ? 47.014 -44.751 -6.447 1.00 64.29 ? 538 LEU B CB 1 ATOM 3932 C CG . LEU A 1 507 ? 45.529 -44.564 -6.165 1.00 64.73 ? 538 LEU B CG 1 ATOM 3933 C CD1 . LEU A 1 507 ? 45.315 -43.385 -5.257 1.00 64.90 ? 538 LEU B CD1 1 ATOM 3934 C CD2 . LEU A 1 507 ? 44.821 -44.349 -7.488 1.00 65.64 ? 538 LEU B CD2 1 ATOM 3935 N N . LEU A 1 508 ? 47.222 -45.210 -3.088 1.00 65.60 ? 539 LEU B N 1 ATOM 3936 C CA . LEU A 1 508 ? 46.964 -46.002 -1.867 1.00 65.76 ? 539 LEU B CA 1 ATOM 3937 C C . LEU A 1 508 ? 45.508 -46.097 -1.455 1.00 66.72 ? 539 LEU B C 1 ATOM 3938 O O . LEU A 1 508 ? 44.953 -47.187 -1.365 1.00 66.99 ? 539 LEU B O 1 ATOM 3939 C CB . LEU A 1 508 ? 47.692 -45.395 -0.687 1.00 65.60 ? 539 LEU B CB 1 ATOM 3940 C CG . LEU A 1 508 ? 49.199 -45.477 -0.754 1.00 64.71 ? 539 LEU B CG 1 ATOM 3941 C CD1 . LEU A 1 508 ? 49.757 -45.123 0.618 1.00 64.33 ? 539 LEU B CD1 1 ATOM 3942 C CD2 . LEU A 1 508 ? 49.590 -46.868 -1.186 1.00 64.69 ? 539 LEU B CD2 1 ATOM 3943 N N . CYS A 1 509 ? 44.919 -44.955 -1.119 1.00 72.39 ? 540 CYS B N 1 ATOM 3944 C CA . CYS A 1 509 ? 43.496 -44.910 -0.839 1.00 73.53 ? 540 CYS B CA 1 ATOM 3945 C C . CYS A 1 509 ? 42.766 -44.048 -1.851 1.00 73.83 ? 540 CYS B C 1 ATOM 3946 O O . CYS A 1 509 ? 43.078 -42.862 -2.027 1.00 73.74 ? 540 CYS B O 1 ATOM 3947 C CB . CYS A 1 509 ? 43.218 -44.420 0.573 1.00 74.15 ? 540 CYS B CB 1 ATOM 3948 S SG . CYS A 1 509 ? 41.935 -43.142 0.693 1.00 75.86 ? 540 CYS B SG 1 ATOM 3949 N N . LEU A 1 510 ? 41.807 -44.680 -2.528 1.00 66.28 ? 541 LEU B N 1 ATOM 3950 C CA . LEU A 1 510 ? 40.929 -44.033 -3.495 1.00 67.00 ? 541 LEU B CA 1 ATOM 3951 C C . LEU A 1 510 ? 39.458 -44.152 -3.080 1.00 68.05 ? 541 LEU B C 1 ATOM 3952 O O . LEU A 1 510 ? 38.854 -45.225 -3.220 1.00 68.29 ? 541 LEU B O 1 ATOM 3953 C CB . LEU A 1 510 ? 41.125 -44.686 -4.869 1.00 66.69 ? 541 LEU B CB 1 ATOM 3954 C CG . LEU A 1 510 ? 40.251 -44.207 -6.031 1.00 67.71 ? 541 LEU B CG 1 ATOM 3955 C CD1 . LEU A 1 510 ? 40.192 -42.705 -6.018 1.00 68.30 ? 541 LEU B CD1 1 ATOM 3956 C CD2 . LEU A 1 510 ? 40.777 -44.679 -7.377 1.00 67.78 ? 541 LEU B CD2 1 ATOM 3957 N N . ASN A 1 511 ? 38.861 -43.047 -2.628 1.00 72.14 ? 542 ASN B N 1 ATOM 3958 C CA . ASN A 1 511 ? 37.438 -43.079 -2.293 1.00 73.61 ? 542 ASN B CA 1 ATOM 3959 C C . ASN A 1 511 ? 36.652 -42.357 -3.397 1.00 73.91 ? 542 ASN B C 1 ATOM 3960 O O . ASN A 1 511 ? 36.729 -41.133 -3.543 1.00 74.07 ? 542 ASN B O 1 ATOM 3961 C CB . ASN A 1 511 ? 37.184 -42.480 -0.897 1.00 74.61 ? 542 ASN B CB 1 ATOM 3962 C CG . ASN A 1 511 ? 35.814 -42.861 -0.320 1.00 76.33 ? 542 ASN B CG 1 ATOM 3963 O OD1 . ASN A 1 511 ? 34.853 -43.038 -1.061 1.00 77.05 ? 542 ASN B OD1 1 ATOM 3964 N ND2 . ASN A 1 511 ? 35.726 -42.976 1.012 1.00 77.03 ? 542 ASN B ND2 1 ATOM 3965 N N . LEU A 1 512 ? 35.970 -43.151 -4.225 1.00 72.28 ? 543 LEU B N 1 ATOM 3966 C CA . LEU A 1 512 ? 35.115 -42.677 -5.325 1.00 72.82 ? 543 LEU B CA 1 ATOM 3967 C C . LEU A 1 512 ? 33.599 -42.700 -5.083 1.00 74.27 ? 543 LEU B C 1 ATOM 3968 O O . LEU A 1 512 ? 32.841 -42.476 -6.020 1.00 74.73 ? 543 LEU B O 1 ATOM 3969 C CB . LEU A 1 512 ? 35.454 -43.393 -6.631 1.00 72.12 ? 543 LEU B CB 1 ATOM 3970 C CG . LEU A 1 512 ? 36.812 -43.008 -7.202 1.00 71.16 ? 543 LEU B CG 1 ATOM 3971 C CD1 . LEU A 1 512 ? 36.973 -43.503 -8.596 1.00 70.86 ? 543 LEU B CD1 1 ATOM 3972 C CD2 . LEU A 1 512 ? 36.964 -41.522 -7.193 1.00 71.53 ? 543 LEU B CD2 1 ATOM 3973 N N . SER A 1 513 ? 33.161 -43.022 -3.863 1.00 89.33 ? 544 SER B N 1 ATOM 3974 C CA . SER A 1 513 ? 31.759 -43.396 -3.599 1.00 90.89 ? 544 SER B CA 1 ATOM 3975 C C . SER A 1 513 ? 30.690 -42.285 -3.624 1.00 92.16 ? 544 SER B C 1 ATOM 3976 O O . SER A 1 513 ? 30.992 -41.102 -3.793 1.00 91.90 ? 544 SER B O 1 ATOM 3977 C CB . SER A 1 513 ? 31.665 -44.162 -2.276 1.00 91.70 ? 544 SER B CB 1 ATOM 3978 O OG . SER A 1 513 ? 32.094 -43.368 -1.183 1.00 91.98 ? 544 SER B OG 1 ATOM 3979 N N . GLN A 1 514 ? 29.436 -42.701 -3.442 1.00 86.98 ? 545 GLN B N 1 ATOM 3980 C CA . GLN A 1 514 ? 28.261 -41.816 -3.468 1.00 88.46 ? 545 GLN B CA 1 ATOM 3981 C C . GLN A 1 514 ? 28.148 -40.933 -4.707 1.00 87.95 ? 545 GLN B C 1 ATOM 3982 O O . GLN A 1 514 ? 27.985 -39.716 -4.599 1.00 88.39 ? 545 GLN B O 1 ATOM 3983 C CB . GLN A 1 514 ? 28.176 -40.959 -2.202 1.00 89.45 ? 545 GLN B CB 1 ATOM 3984 C CG . GLN A 1 514 ? 27.657 -41.700 -0.977 1.00 90.67 ? 545 GLN B CG 1 ATOM 3985 C CD . GLN A 1 514 ? 27.194 -40.752 0.112 1.00 92.63 ? 545 GLN B CD 1 ATOM 3986 O OE1 . GLN A 1 514 ? 26.614 -39.697 -0.168 1.00 93.50 ? 545 GLN B OE1 1 ATOM 3987 N NE2 . GLN A 1 514 ? 27.454 -41.118 1.363 1.00 93.34 ? 545 GLN B NE2 1 ATOM 3988 N N . ASN A 1 515 ? 28.214 -41.562 -5.878 1.00 97.75 ? 546 ASN B N 1 ATOM 3989 C CA . ASN A 1 515 ? 28.220 -40.835 -7.141 1.00 97.09 ? 546 ASN B CA 1 ATOM 3990 C C . ASN A 1 515 ? 27.311 -41.397 -8.216 1.00 97.31 ? 546 ASN B C 1 ATOM 3991 O O . ASN A 1 515 ? 26.592 -42.378 -8.022 1.00 98.03 ? 546 ASN B O 1 ATOM 3992 C CB . ASN A 1 515 ? 29.640 -40.721 -7.698 1.00 95.26 ? 546 ASN B CB 1 ATOM 3993 C CG . ASN A 1 515 ? 30.431 -39.610 -7.044 1.00 94.68 ? 546 ASN B CG 1 ATOM 3994 O OD1 . ASN A 1 515 ? 30.593 -38.532 -7.612 1.00 94.68 ? 546 ASN B OD1 1 ATOM 3995 N ND2 . ASN A 1 515 ? 30.917 -39.860 -5.834 1.00 94.20 ? 546 ASN B ND2 1 ATOM 3996 N N . HIS A 1 516 ? 27.344 -40.721 -9.350 1.00 88.80 ? 547 HIS B N 1 ATOM 3997 C CA . HIS A 1 516 ? 26.546 -41.067 -10.506 1.00 88.89 ? 547 HIS B CA 1 ATOM 3998 C C . HIS A 1 516 ? 27.291 -41.885 -11.572 1.00 87.44 ? 547 HIS B C 1 ATOM 3999 O O . HIS A 1 516 ? 26.853 -41.967 -12.719 1.00 87.21 ? 547 HIS B O 1 ATOM 4000 C CB . HIS A 1 516 ? 25.844 -39.828 -11.042 1.00 89.56 ? 547 HIS B CB 1 ATOM 4001 C CG . HIS A 1 516 ? 24.973 -39.165 -10.021 1.00 91.10 ? 547 HIS B CG 1 ATOM 4002 N ND1 . HIS A 1 516 ? 24.678 -39.753 -8.811 1.00 91.93 ? 547 HIS B ND1 1 ATOM 4003 C CD2 . HIS A 1 516 ? 24.336 -37.969 -10.023 1.00 91.99 ? 547 HIS B CD2 1 ATOM 4004 C CE1 . HIS A 1 516 ? 23.897 -38.949 -8.111 1.00 93.26 ? 547 HIS B CE1 1 ATOM 4005 N NE2 . HIS A 1 516 ? 23.675 -37.860 -8.824 1.00 93.31 ? 547 HIS B NE2 1 ATOM 4006 N N . LEU A 1 517 ? 28.465 -42.395 -11.205 1.00 77.83 ? 548 LEU B N 1 ATOM 4007 C CA . LEU A 1 517 ? 29.278 -43.257 -12.073 1.00 76.74 ? 548 LEU B CA 1 ATOM 4008 C C . LEU A 1 517 ? 28.603 -44.517 -12.624 1.00 76.68 ? 548 LEU B C 1 ATOM 4009 O O . LEU A 1 517 ? 27.747 -45.140 -11.989 1.00 77.34 ? 548 LEU B O 1 ATOM 4010 C CB . LEU A 1 517 ? 30.525 -43.725 -11.338 1.00 75.46 ? 548 LEU B CB 1 ATOM 4011 C CG . LEU A 1 517 ? 31.360 -42.693 -10.604 1.00 75.24 ? 548 LEU B CG 1 ATOM 4012 C CD1 . LEU A 1 517 ? 32.415 -43.394 -9.768 1.00 74.46 ? 548 LEU B CD1 1 ATOM 4013 C CD2 . LEU A 1 517 ? 31.985 -41.773 -11.626 1.00 75.83 ? 548 LEU B CD2 1 ATOM 4014 N N . ASN A 1 518 ? 29.050 -44.901 -13.810 1.00 91.41 ? 549 ASN B N 1 ATOM 4015 C CA . ASN A 1 518 ? 28.483 -46.018 -14.547 1.00 91.29 ? 549 ASN B CA 1 ATOM 4016 C C . ASN A 1 518 ? 29.579 -46.721 -15.333 1.00 89.77 ? 549 ASN B C 1 ATOM 4017 O O . ASN A 1 518 ? 30.768 -46.531 -15.059 1.00 88.87 ? 549 ASN B O 1 ATOM 4018 C CB . ASN A 1 518 ? 27.363 -45.543 -15.478 1.00 92.03 ? 549 ASN B CB 1 ATOM 4019 C CG . ASN A 1 518 ? 27.762 -44.328 -16.306 1.00 91.98 ? 549 ASN B CG 1 ATOM 4020 O OD1 . ASN A 1 518 ? 27.519 -43.182 -15.915 1.00 92.77 ? 549 ASN B OD1 1 ATOM 4021 N ND2 . ASN A 1 518 ? 28.377 -44.575 -17.457 1.00 92.17 ? 549 ASN B ND2 1 ATOM 4022 N N . GLY A 1 519 ? 29.181 -47.566 -16.277 1.00 90.73 ? 550 GLY B N 1 ATOM 4023 C CA . GLY A 1 519 ? 30.142 -48.284 -17.087 1.00 89.63 ? 550 GLY B CA 1 ATOM 4024 C C . GLY A 1 519 ? 30.766 -49.362 -16.242 1.00 89.02 ? 550 GLY B C 1 ATOM 4025 O O . GLY A 1 519 ? 30.154 -49.814 -15.286 1.00 89.77 ? 550 GLY B O 1 ATOM 4026 N N . ILE A 1 520 ? 31.978 -49.780 -16.583 1.00 74.53 ? 551 ILE B N 1 ATOM 4027 C CA . ILE A 1 520 ? 32.650 -50.807 -15.800 1.00 72.84 ? 551 ILE B CA 1 ATOM 4028 C C . ILE A 1 520 ? 33.778 -50.262 -14.933 1.00 71.95 ? 551 ILE B C 1 ATOM 4029 O O . ILE A 1 520 ? 34.094 -49.066 -14.974 1.00 72.65 ? 551 ILE B O 1 ATOM 4030 C CB . ILE A 1 520 ? 33.200 -51.939 -16.675 1.00 72.87 ? 551 ILE B CB 1 ATOM 4031 C CG1 . ILE A 1 520 ? 34.004 -51.382 -17.848 1.00 74.23 ? 551 ILE B CG1 1 ATOM 4032 C CG2 . ILE A 1 520 ? 32.084 -52.772 -17.196 1.00 73.24 ? 551 ILE B CG2 1 ATOM 4033 C CD1 . ILE A 1 520 ? 35.489 -51.190 -17.564 1.00 73.69 ? 551 ILE B CD1 1 ATOM 4034 N N . ILE A 1 521 ? 34.383 -51.182 -14.174 1.00 71.31 ? 552 ILE B N 1 ATOM 4035 C CA . ILE A 1 521 ? 35.470 -50.932 -13.227 1.00 70.80 ? 552 ILE B CA 1 ATOM 4036 C C . ILE A 1 521 ? 36.749 -51.456 -13.855 1.00 69.81 ? 552 ILE B C 1 ATOM 4037 O O . ILE A 1 521 ? 36.973 -52.662 -13.869 1.00 69.43 ? 552 ILE B O 1 ATOM 4038 C CB . ILE A 1 521 ? 35.224 -51.769 -11.956 1.00 71.08 ? 552 ILE B CB 1 ATOM 4039 C CG1 . ILE A 1 521 ? 33.921 -51.365 -11.277 1.00 72.35 ? 552 ILE B CG1 1 ATOM 4040 C CG2 . ILE A 1 521 ? 36.377 -51.679 -10.989 1.00 70.63 ? 552 ILE B CG2 1 ATOM 4041 C CD1 . ILE A 1 521 ? 33.484 -52.349 -10.249 1.00 72.84 ? 552 ILE B CD1 1 ATOM 4042 N N . PRO A 1 522 ? 37.611 -50.558 -14.346 1.00 70.21 ? 553 PRO B N 1 ATOM 4043 C CA . PRO A 1 522 ? 38.724 -50.904 -15.243 1.00 70.77 ? 553 PRO B CA 1 ATOM 4044 C C . PRO A 1 522 ? 39.717 -51.904 -14.657 1.00 69.52 ? 553 PRO B C 1 ATOM 4045 O O . PRO A 1 522 ? 40.108 -51.715 -13.520 1.00 68.40 ? 553 PRO B O 1 ATOM 4046 C CB . PRO A 1 522 ? 39.410 -49.559 -15.476 1.00 71.65 ? 553 PRO B CB 1 ATOM 4047 C CG . PRO A 1 522 ? 38.989 -48.720 -14.344 1.00 70.98 ? 553 PRO B CG 1 ATOM 4048 C CD . PRO A 1 522 ? 37.591 -49.124 -14.043 1.00 70.72 ? 553 PRO B CD 1 ATOM 4049 N N . TRP A 1 523 ? 40.124 -52.920 -15.427 1.00 92.40 ? 554 TRP B N 1 ATOM 4050 C CA . TRP A 1 523 ? 41.014 -53.983 -14.939 1.00 92.08 ? 554 TRP B CA 1 ATOM 4051 C C . TRP A 1 523 ? 42.361 -53.441 -14.538 1.00 91.77 ? 554 TRP B C 1 ATOM 4052 O O . TRP A 1 523 ? 43.112 -54.094 -13.815 1.00 91.63 ? 554 TRP B O 1 ATOM 4053 C CB . TRP A 1 523 ? 41.209 -55.085 -15.990 1.00 91.78 ? 554 TRP B CB 1 ATOM 4054 C CG . TRP A 1 523 ? 42.424 -54.948 -16.932 1.00 92.13 ? 554 TRP B CG 1 ATOM 4055 C CD1 . TRP A 1 523 ? 43.750 -55.093 -16.610 1.00 91.83 ? 554 TRP B CD1 1 ATOM 4056 C CD2 . TRP A 1 523 ? 42.391 -54.723 -18.348 1.00 93.55 ? 554 TRP B CD2 1 ATOM 4057 N NE1 . TRP A 1 523 ? 44.535 -54.933 -17.726 1.00 92.97 ? 554 TRP B NE1 1 ATOM 4058 C CE2 . TRP A 1 523 ? 43.724 -54.709 -18.805 1.00 94.15 ? 554 TRP B CE2 1 ATOM 4059 C CE3 . TRP A 1 523 ? 41.363 -54.519 -19.271 1.00 94.61 ? 554 TRP B CE3 1 ATOM 4060 C CZ2 . TRP A 1 523 ? 44.053 -54.497 -20.136 1.00 95.90 ? 554 TRP B CZ2 1 ATOM 4061 C CZ3 . TRP A 1 523 ? 41.693 -54.303 -20.596 1.00 96.34 ? 554 TRP B CZ3 1 ATOM 4062 C CH2 . TRP A 1 523 ? 43.025 -54.298 -21.018 1.00 96.98 ? 554 TRP B CH2 1 ATOM 4063 N N . GLU A 1 524 ? 42.658 -52.249 -15.042 1.00 92.95 ? 555 GLU B N 1 ATOM 4064 C CA . GLU A 1 524 ? 43.929 -51.562 -14.826 1.00 92.80 ? 555 GLU B CA 1 ATOM 4065 C C . GLU A 1 524 ? 44.287 -51.393 -13.328 1.00 92.76 ? 555 GLU B C 1 ATOM 4066 O O . GLU A 1 524 ? 45.458 -51.496 -12.944 1.00 92.41 ? 555 GLU B O 1 ATOM 4067 C CB . GLU A 1 524 ? 43.923 -50.217 -15.589 1.00 93.83 ? 555 GLU B CB 1 ATOM 4068 C CG . GLU A 1 524 ? 44.249 -50.288 -17.118 1.00 95.29 ? 555 GLU B CG 1 ATOM 4069 C CD . GLU A 1 524 ? 43.098 -50.765 -18.042 1.00 96.15 ? 555 GLU B CD 1 ATOM 4070 O OE1 . GLU A 1 524 ? 41.919 -50.815 -17.623 1.00 95.63 ? 555 GLU B OE1 1 ATOM 4071 O OE2 . GLU A 1 524 ? 43.390 -51.085 -19.216 1.00 97.45 ? 555 GLU B OE2 1 ATOM 4072 N N . ILE A 1 525 ? 43.274 -51.166 -12.490 1.00 67.35 ? 556 ILE B N 1 ATOM 4073 C CA . ILE A 1 525 ? 43.459 -51.102 -11.039 1.00 66.50 ? 556 ILE B CA 1 ATOM 4074 C C . ILE A 1 525 ? 44.011 -52.384 -10.409 1.00 65.74 ? 556 ILE B C 1 ATOM 4075 O O . ILE A 1 525 ? 44.667 -52.326 -9.373 1.00 65.14 ? 556 ILE B O 1 ATOM 4076 C CB . ILE A 1 525 ? 42.162 -50.796 -10.300 1.00 66.62 ? 556 ILE B CB 1 ATOM 4077 C CG1 . ILE A 1 525 ? 41.365 -49.723 -11.007 1.00 67.48 ? 556 ILE B CG1 1 ATOM 4078 C CG2 . ILE A 1 525 ? 42.457 -50.306 -8.907 1.00 66.19 ? 556 ILE B CG2 1 ATOM 4079 C CD1 . ILE A 1 525 ? 40.307 -49.122 -10.104 1.00 67.63 ? 556 ILE B CD1 1 ATOM 4080 N N . SER A 1 526 ? 43.752 -53.543 -11.007 1.00 69.99 ? 557 SER B N 1 ATOM 4081 C CA . SER A 1 526 ? 44.352 -54.768 -10.501 1.00 69.80 ? 557 SER B CA 1 ATOM 4082 C C . SER A 1 526 ? 45.871 -54.630 -10.458 1.00 69.07 ? 557 SER B C 1 ATOM 4083 O O . SER A 1 526 ? 46.549 -55.321 -9.698 1.00 68.77 ? 557 SER B O 1 ATOM 4084 C CB . SER A 1 526 ? 43.983 -55.948 -11.382 1.00 70.12 ? 557 SER B CB 1 ATOM 4085 O OG . SER A 1 526 ? 45.146 -56.666 -11.746 1.00 68.78 ? 557 SER B OG 1 ATOM 4086 N N . THR A 1 527 ? 46.392 -53.733 -11.291 1.00 65.29 ? 558 THR B N 1 ATOM 4087 C CA . THR A 1 527 ? 47.824 -53.518 -11.427 1.00 65.63 ? 558 THR B CA 1 ATOM 4088 C C . THR A 1 527 ? 48.438 -52.335 -10.680 1.00 65.28 ? 558 THR B C 1 ATOM 4089 O O . THR A 1 527 ? 49.622 -52.055 -10.866 1.00 65.70 ? 558 THR B O 1 ATOM 4090 C CB . THR A 1 527 ? 48.188 -53.387 -12.878 1.00 67.24 ? 558 THR B CB 1 ATOM 4091 O OG1 . THR A 1 527 ? 47.281 -52.465 -13.499 1.00 68.07 ? 558 THR B OG1 1 ATOM 4092 C CG2 . THR A 1 527 ? 48.091 -54.752 -13.545 1.00 67.57 ? 558 THR B CG2 1 ATOM 4093 N N . LEU A 1 528 ? 47.657 -51.609 -9.881 1.00 81.80 ? 559 LEU B N 1 ATOM 4094 C CA . LEU A 1 528 ? 48.247 -50.602 -8.991 1.00 81.72 ? 559 LEU B CA 1 ATOM 4095 C C . LEU A 1 528 ? 49.002 -51.336 -7.898 1.00 81.45 ? 559 LEU B C 1 ATOM 4096 O O . LEU A 1 528 ? 48.405 -52.061 -7.113 1.00 81.71 ? 559 LEU B O 1 ATOM 4097 C CB . LEU A 1 528 ? 47.189 -49.685 -8.381 1.00 82.22 ? 559 LEU B CB 1 ATOM 4098 C CG . LEU A 1 528 ? 46.443 -48.784 -9.358 1.00 82.43 ? 559 LEU B CG 1 ATOM 4099 C CD1 . LEU A 1 528 ? 45.827 -47.622 -8.620 1.00 82.89 ? 559 LEU B CD1 1 ATOM 4100 C CD2 . LEU A 1 528 ? 47.372 -48.305 -10.448 1.00 82.12 ? 559 LEU B CD2 1 ATOM 4101 N N . PRO A 1 529 ? 50.324 -51.160 -7.859 1.00 64.34 ? 560 PRO B N 1 ATOM 4102 C CA . PRO A 1 529 ? 51.294 -51.936 -7.078 1.00 63.87 ? 560 PRO B CA 1 ATOM 4103 C C . PRO A 1 529 ? 51.247 -51.784 -5.547 1.00 63.82 ? 560 PRO B C 1 ATOM 4104 O O . PRO A 1 529 ? 51.567 -52.740 -4.832 1.00 63.71 ? 560 PRO B O 1 ATOM 4105 C CB . PRO A 1 529 ? 52.640 -51.437 -7.615 1.00 63.51 ? 560 PRO B CB 1 ATOM 4106 C CG . PRO A 1 529 ? 52.324 -50.882 -8.955 1.00 64.51 ? 560 PRO B CG 1 ATOM 4107 C CD . PRO A 1 529 ? 51.003 -50.223 -8.759 1.00 64.34 ? 560 PRO B CD 1 ATOM 4108 N N . SER A 1 530 ? 50.952 -50.596 -5.042 1.00 68.52 ? 561 SER B N 1 ATOM 4109 C CA . SER A 1 530 ? 50.797 -50.450 -3.603 1.00 68.73 ? 561 SER B CA 1 ATOM 4110 C C . SER A 1 530 ? 49.362 -50.351 -3.047 1.00 69.44 ? 561 SER B C 1 ATOM 4111 O O . SER A 1 530 ? 49.189 -50.238 -1.844 1.00 69.77 ? 561 SER B O 1 ATOM 4112 C CB . SER A 1 530 ? 51.708 -49.335 -3.082 1.00 68.41 ? 561 SER B CB 1 ATOM 4113 O OG . SER A 1 530 ? 53.082 -49.683 -3.225 1.00 67.90 ? 561 SER B OG 1 ATOM 4114 N N . ILE A 1 531 ? 48.351 -50.427 -3.909 1.00 66.33 ? 562 ILE B N 1 ATOM 4115 C CA . ILE A 1 531 ? 46.958 -50.058 -3.577 1.00 67.01 ? 562 ILE B CA 1 ATOM 4116 C C . ILE A 1 531 ? 46.328 -50.658 -2.312 1.00 67.49 ? 562 ILE B C 1 ATOM 4117 O O . ILE A 1 531 ? 46.333 -51.871 -2.125 1.00 67.42 ? 562 ILE B O 1 ATOM 4118 C CB . ILE A 1 531 ? 46.014 -50.413 -4.734 1.00 67.25 ? 562 ILE B CB 1 ATOM 4119 C CG1 . ILE A 1 531 ? 44.624 -49.850 -4.477 1.00 67.92 ? 562 ILE B CG1 1 ATOM 4120 C CG2 . ILE A 1 531 ? 45.971 -51.922 -4.963 1.00 67.15 ? 562 ILE B CG2 1 ATOM 4121 C CD1 . ILE A 1 531 ? 44.556 -48.383 -4.725 1.00 68.15 ? 562 ILE B CD1 1 ATOM 4122 N N . ALA A 1 532 ? 45.746 -49.806 -1.464 1.00 63.40 ? 563 ALA B N 1 ATOM 4123 C CA . ALA A 1 532 ? 45.238 -50.260 -0.165 1.00 63.80 ? 563 ALA B CA 1 ATOM 4124 C C . ALA A 1 532 ? 43.729 -50.184 -0.006 1.00 64.81 ? 563 ALA B C 1 ATOM 4125 O O . ALA A 1 532 ? 43.075 -51.203 0.181 1.00 65.07 ? 563 ALA B O 1 ATOM 4126 C CB . ALA A 1 532 ? 45.914 -49.513 0.963 1.00 63.61 ? 563 ALA B CB 1 ATOM 4127 N N . ASP A 1 533 ? 43.191 -48.973 -0.043 1.00 73.11 ? 564 ASP B N 1 ATOM 4128 C CA . ASP A 1 533 ? 41.773 -48.751 0.188 1.00 74.55 ? 564 ASP B CA 1 ATOM 4129 C C . ASP A 1 533 ? 41.093 -48.350 -1.087 1.00 74.81 ? 564 ASP B C 1 ATOM 4130 O O . ASP A 1 533 ? 41.578 -47.461 -1.771 1.00 74.79 ? 564 ASP B O 1 ATOM 4131 C CB . ASP A 1 533 ? 41.582 -47.609 1.170 1.00 75.77 ? 564 ASP B CB 1 ATOM 4132 C CG . ASP A 1 533 ? 41.796 -48.032 2.595 1.00 75.86 ? 564 ASP B CG 1 ATOM 4133 O OD1 . ASP A 1 533 ? 42.289 -49.173 2.819 1.00 74.64 ? 564 ASP B OD1 1 ATOM 4134 O OD2 . ASP A 1 533 ? 41.470 -47.207 3.483 1.00 77.23 ? 564 ASP B OD2 1 ATOM 4135 N N . VAL A 1 534 ? 39.971 -48.988 -1.409 1.00 66.97 ? 565 VAL B N 1 ATOM 4136 C CA . VAL A 1 534 ? 39.155 -48.577 -2.555 1.00 67.39 ? 565 VAL B CA 1 ATOM 4137 C C . VAL A 1 534 ? 37.673 -48.525 -2.186 1.00 68.65 ? 565 VAL B C 1 ATOM 4138 O O . VAL A 1 534 ? 37.077 -49.552 -1.888 1.00 68.95 ? 565 VAL B O 1 ATOM 4139 C CB . VAL A 1 534 ? 39.339 -49.551 -3.727 1.00 66.60 ? 565 VAL B CB 1 ATOM 4140 C CG1 . VAL A 1 534 ? 38.265 -49.359 -4.739 1.00 67.12 ? 565 VAL B CG1 1 ATOM 4141 C CG2 . VAL A 1 534 ? 40.698 -49.372 -4.362 1.00 65.79 ? 565 VAL B CG2 1 ATOM 4142 N N . ASP A 1 535 ? 37.062 -47.348 -2.193 1.00 69.58 ? 566 ASP B N 1 ATOM 4143 C CA . ASP A 1 535 ? 35.640 -47.311 -1.874 1.00 71.08 ? 566 ASP B CA 1 ATOM 4144 C C . ASP A 1 535 ? 34.851 -46.825 -3.075 1.00 71.22 ? 566 ASP B C 1 ATOM 4145 O O . ASP A 1 535 ? 34.860 -45.644 -3.393 1.00 71.19 ? 566 ASP B O 1 ATOM 4146 C CB . ASP A 1 535 ? 35.380 -46.433 -0.645 1.00 72.28 ? 566 ASP B CB 1 ATOM 4147 C CG . ASP A 1 535 ? 33.937 -46.511 -0.152 1.00 74.09 ? 566 ASP B CG 1 ATOM 4148 O OD1 . ASP A 1 535 ? 33.390 -47.624 -0.051 1.00 74.53 ? 566 ASP B OD1 1 ATOM 4149 O OD2 . ASP A 1 535 ? 33.343 -45.452 0.146 1.00 75.11 ? 566 ASP B OD2 1 ATOM 4150 N N . LEU A 1 536 ? 34.180 -47.764 -3.737 1.00 75.03 ? 567 LEU B N 1 ATOM 4151 C CA . LEU A 1 536 ? 33.345 -47.519 -4.924 1.00 75.27 ? 567 LEU B CA 1 ATOM 4152 C C . LEU A 1 536 ? 31.814 -47.483 -4.756 1.00 77.02 ? 567 LEU B C 1 ATOM 4153 O O . LEU A 1 536 ? 31.106 -47.530 -5.757 1.00 77.15 ? 567 LEU B O 1 ATOM 4154 C CB . LEU A 1 536 ? 33.729 -48.459 -6.066 1.00 74.08 ? 567 LEU B CB 1 ATOM 4155 C CG . LEU A 1 536 ? 35.224 -48.442 -6.357 1.00 72.51 ? 567 LEU B CG 1 ATOM 4156 C CD1 . LEU A 1 536 ? 35.562 -49.291 -7.545 1.00 71.55 ? 567 LEU B CD1 1 ATOM 4157 C CD2 . LEU A 1 536 ? 35.718 -47.033 -6.563 1.00 72.31 ? 567 LEU B CD2 1 ATOM 4158 N N . SER A 1 537 ? 31.300 -47.497 -3.526 1.00 71.35 ? 568 SER B N 1 ATOM 4159 C CA . SER A 1 537 ? 29.860 -47.722 -3.287 1.00 72.45 ? 568 SER B CA 1 ATOM 4160 C C . SER A 1 537 ? 28.813 -46.653 -3.749 1.00 73.83 ? 568 SER B C 1 ATOM 4161 O O . SER A 1 537 ? 29.131 -45.483 -4.001 1.00 74.14 ? 568 SER B O 1 ATOM 4162 C CB . SER A 1 537 ? 29.620 -48.161 -1.825 1.00 72.53 ? 568 SER B CB 1 ATOM 4163 O OG . SER A 1 537 ? 30.586 -47.633 -0.925 1.00 71.99 ? 568 SER B OG 1 ATOM 4164 N N . HIS A 1 538 ? 27.563 -47.105 -3.865 1.00 84.14 ? 569 HIS B N 1 ATOM 4165 C CA . HIS A 1 538 ? 26.403 -46.268 -4.212 1.00 85.25 ? 569 HIS B CA 1 ATOM 4166 C C . HIS A 1 538 ? 26.386 -45.613 -5.594 1.00 84.34 ? 569 HIS B C 1 ATOM 4167 O O . HIS A 1 538 ? 26.155 -44.404 -5.733 1.00 84.61 ? 569 HIS B O 1 ATOM 4168 C CB . HIS A 1 538 ? 26.115 -45.260 -3.106 1.00 86.51 ? 569 HIS B CB 1 ATOM 4169 C CG . HIS A 1 538 ? 25.653 -45.904 -1.846 1.00 87.88 ? 569 HIS B CG 1 ATOM 4170 N ND1 . HIS A 1 538 ? 26.524 -46.323 -0.865 1.00 87.55 ? 569 HIS B ND1 1 ATOM 4171 C CD2 . HIS A 1 538 ? 24.416 -46.260 -1.431 1.00 89.59 ? 569 HIS B CD2 1 ATOM 4172 C CE1 . HIS A 1 538 ? 25.842 -46.884 0.115 1.00 89.01 ? 569 HIS B CE1 1 ATOM 4173 N NE2 . HIS A 1 538 ? 24.559 -46.859 -0.205 1.00 90.28 ? 569 HIS B NE2 1 ATOM 4174 N N . ASN A 1 539 ? 26.610 -46.436 -6.615 1.00 89.05 ? 570 ASN B N 1 ATOM 4175 C CA . ASN A 1 539 ? 26.640 -45.958 -7.987 1.00 88.18 ? 570 ASN B CA 1 ATOM 4176 C C . ASN A 1 539 ? 25.821 -46.804 -8.944 1.00 88.33 ? 570 ASN B C 1 ATOM 4177 O O . ASN A 1 539 ? 25.087 -47.715 -8.548 1.00 89.27 ? 570 ASN B O 1 ATOM 4178 C CB . ASN A 1 539 ? 28.084 -45.854 -8.490 1.00 86.39 ? 570 ASN B CB 1 ATOM 4179 C CG . ASN A 1 539 ? 28.822 -44.668 -7.901 1.00 86.11 ? 570 ASN B CG 1 ATOM 4180 O OD1 . ASN A 1 539 ? 29.144 -43.714 -8.603 1.00 85.71 ? 570 ASN B OD1 1 ATOM 4181 N ND2 . ASN A 1 539 ? 29.078 -44.714 -6.601 1.00 86.30 ? 570 ASN B ND2 1 ATOM 4182 N N . LEU A 1 540 ? 25.932 -46.443 -10.214 1.00 92.33 ? 571 LEU B N 1 ATOM 4183 C CA . LEU A 1 540 ? 25.287 -47.149 -11.300 1.00 92.31 ? 571 LEU B CA 1 ATOM 4184 C C . LEU A 1 540 ? 26.241 -48.112 -11.978 1.00 90.83 ? 571 LEU B C 1 ATOM 4185 O O . LEU A 1 540 ? 25.910 -48.685 -13.010 1.00 90.55 ? 571 LEU B O 1 ATOM 4186 C CB . LEU A 1 540 ? 24.684 -46.169 -12.300 1.00 92.55 ? 571 LEU B CB 1 ATOM 4187 C CG . LEU A 1 540 ? 23.449 -45.443 -11.761 1.00 94.19 ? 571 LEU B CG 1 ATOM 4188 C CD1 . LEU A 1 540 ? 22.543 -46.420 -10.987 1.00 95.35 ? 571 LEU B CD1 1 ATOM 4189 C CD2 . LEU A 1 540 ? 23.828 -44.213 -10.917 1.00 94.52 ? 571 LEU B CD2 1 ATOM 4190 N N . LEU A 1 541 ? 27.431 -48.266 -11.404 1.00 81.42 ? 572 LEU B N 1 ATOM 4191 C CA . LEU A 1 541 ? 28.446 -49.173 -11.935 1.00 79.84 ? 572 LEU B CA 1 ATOM 4192 C C . LEU A 1 541 ? 27.889 -50.547 -12.232 1.00 79.86 ? 572 LEU B C 1 ATOM 4193 O O . LEU A 1 541 ? 27.254 -51.170 -11.393 1.00 80.79 ? 572 LEU B O 1 ATOM 4194 C CB . LEU A 1 541 ? 29.558 -49.373 -10.910 1.00 79.12 ? 572 LEU B CB 1 ATOM 4195 C CG . LEU A 1 541 ? 30.745 -48.421 -10.885 1.00 78.50 ? 572 LEU B CG 1 ATOM 4196 C CD1 . LEU A 1 541 ? 31.518 -48.538 -9.575 1.00 78.09 ? 572 LEU B CD1 1 ATOM 4197 C CD2 . LEU A 1 541 ? 31.629 -48.734 -12.067 1.00 76.73 ? 572 LEU B CD2 1 ATOM 4198 N N . THR A 1 542 ? 28.143 -51.031 -13.431 1.00 90.01 ? 573 THR B N 1 ATOM 4199 C CA . THR A 1 542 ? 27.712 -52.365 -13.777 1.00 89.88 ? 573 THR B CA 1 ATOM 4200 C C . THR A 1 542 ? 28.779 -53.003 -14.638 1.00 88.30 ? 573 THR B C 1 ATOM 4201 O O . THR A 1 542 ? 29.454 -52.319 -15.402 1.00 87.56 ? 573 THR B O 1 ATOM 4202 C CB . THR A 1 542 ? 26.373 -52.349 -14.511 1.00 90.92 ? 573 THR B CB 1 ATOM 4203 O OG1 . THR A 1 542 ? 25.946 -53.703 -14.751 1.00 90.72 ? 573 THR B OG1 1 ATOM 4204 C CG2 . THR A 1 542 ? 26.467 -51.536 -15.826 1.00 90.47 ? 573 THR B CG2 1 ATOM 4205 N N . GLY A 1 543 ? 28.953 -54.309 -14.496 1.00 71.97 ? 574 GLY B N 1 ATOM 4206 C CA . GLY A 1 543 ? 30.053 -54.973 -15.154 1.00 71.24 ? 574 GLY B CA 1 ATOM 4207 C C . GLY A 1 543 ? 30.482 -56.122 -14.293 1.00 70.40 ? 574 GLY B C 1 ATOM 4208 O O . GLY A 1 543 ? 29.706 -56.628 -13.491 1.00 70.52 ? 574 GLY B O 1 ATOM 4209 N N . THR A 1 544 ? 31.728 -56.532 -14.450 1.00 79.51 ? 575 THR B N 1 ATOM 4210 C CA . THR A 1 544 ? 32.271 -57.622 -13.660 1.00 79.45 ? 575 THR B CA 1 ATOM 4211 C C . THR A 1 544 ? 33.356 -57.099 -12.742 1.00 79.03 ? 575 THR B C 1 ATOM 4212 O O . THR A 1 544 ? 33.950 -56.045 -13.007 1.00 78.75 ? 575 THR B O 1 ATOM 4213 C CB . THR A 1 544 ? 32.909 -58.670 -14.557 1.00 79.00 ? 575 THR B CB 1 ATOM 4214 O OG1 . THR A 1 544 ? 33.928 -59.360 -13.825 1.00 78.92 ? 575 THR B OG1 1 ATOM 4215 C CG2 . THR A 1 544 ? 33.540 -57.993 -15.780 1.00 78.61 ? 575 THR B CG2 1 ATOM 4216 N N . ILE A 1 545 ? 33.596 -57.825 -11.652 1.00 74.91 ? 576 ILE B N 1 ATOM 4217 C CA . ILE A 1 545 ? 34.741 -57.556 -10.785 1.00 74.48 ? 576 ILE B CA 1 ATOM 4218 C C . ILE A 1 545 ? 35.952 -58.318 -11.320 1.00 73.56 ? 576 ILE B C 1 ATOM 4219 O O . ILE A 1 545 ? 35.933 -59.548 -11.357 1.00 73.49 ? 576 ILE B O 1 ATOM 4220 C CB . ILE A 1 545 ? 34.466 -57.958 -9.334 1.00 75.13 ? 576 ILE B CB 1 ATOM 4221 C CG1 . ILE A 1 545 ? 33.350 -57.089 -8.763 1.00 76.37 ? 576 ILE B CG1 1 ATOM 4222 C CG2 . ILE A 1 545 ? 35.714 -57.804 -8.514 1.00 74.65 ? 576 ILE B CG2 1 ATOM 4223 C CD1 . ILE A 1 545 ? 33.054 -57.340 -7.322 1.00 77.30 ? 576 ILE B CD1 1 ATOM 4224 N N . PRO A 1 546 ? 37.012 -57.584 -11.716 1.00 72.53 ? 577 PRO B N 1 ATOM 4225 C CA . PRO A 1 546 ? 38.170 -58.032 -12.505 1.00 71.80 ? 577 PRO B CA 1 ATOM 4226 C C . PRO A 1 546 ? 38.827 -59.319 -12.031 1.00 71.65 ? 577 PRO B C 1 ATOM 4227 O O . PRO A 1 546 ? 39.078 -59.492 -10.850 1.00 71.77 ? 577 PRO B O 1 ATOM 4228 C CB . PRO A 1 546 ? 39.158 -56.885 -12.338 1.00 71.46 ? 577 PRO B CB 1 ATOM 4229 C CG . PRO A 1 546 ? 38.305 -55.699 -12.141 1.00 72.04 ? 577 PRO B CG 1 ATOM 4230 C CD . PRO A 1 546 ? 37.114 -56.156 -11.369 1.00 72.74 ? 577 PRO B CD 1 ATOM 4231 N N . SER A 1 547 ? 39.124 -60.197 -12.978 1.00 72.57 ? 578 SER B N 1 ATOM 4232 C CA . SER A 1 547 ? 39.680 -61.517 -12.712 1.00 72.67 ? 578 SER B CA 1 ATOM 4233 C C . SER A 1 547 ? 40.817 -61.479 -11.704 1.00 72.42 ? 578 SER B C 1 ATOM 4234 O O . SER A 1 547 ? 40.694 -62.006 -10.598 1.00 72.69 ? 578 SER B O 1 ATOM 4235 C CB . SER A 1 547 ? 40.174 -62.142 -14.036 1.00 72.49 ? 578 SER B CB 1 ATOM 4236 O OG . SER A 1 547 ? 40.648 -63.479 -13.885 1.00 72.67 ? 578 SER B OG 1 ATOM 4237 N N . ASP A 1 548 ? 41.896 -60.804 -12.089 1.00 83.20 ? 579 ASP B N 1 ATOM 4238 C CA . ASP A 1 548 ? 43.216 -60.959 -11.477 1.00 82.86 ? 579 ASP B CA 1 ATOM 4239 C C . ASP A 1 548 ? 43.430 -60.179 -10.166 1.00 82.83 ? 579 ASP B C 1 ATOM 4240 O O . ASP A 1 548 ? 44.490 -60.264 -9.538 1.00 82.56 ? 579 ASP B O 1 ATOM 4241 C CB . ASP A 1 548 ? 44.299 -60.621 -12.518 1.00 82.36 ? 579 ASP B CB 1 ATOM 4242 C CG . ASP A 1 548 ? 43.829 -59.584 -13.557 1.00 82.41 ? 579 ASP B CG 1 ATOM 4243 O OD1 . ASP A 1 548 ? 42.924 -58.780 -13.237 1.00 82.79 ? 579 ASP B OD1 1 ATOM 4244 O OD2 . ASP A 1 548 ? 44.366 -59.566 -14.692 1.00 82.14 ? 579 ASP B OD2 1 ATOM 4245 N N . PHE A 1 549 ? 42.404 -59.449 -9.747 1.00 63.80 ? 580 PHE B N 1 ATOM 4246 C CA . PHE A 1 549 ? 42.436 -58.662 -8.514 1.00 63.63 ? 580 PHE B CA 1 ATOM 4247 C C . PHE A 1 549 ? 42.777 -59.429 -7.239 1.00 63.63 ? 580 PHE B C 1 ATOM 4248 O O . PHE A 1 549 ? 43.415 -58.905 -6.340 1.00 63.36 ? 580 PHE B O 1 ATOM 4249 C CB . PHE A 1 549 ? 41.099 -57.961 -8.311 1.00 64.21 ? 580 PHE B CB 1 ATOM 4250 C CG . PHE A 1 549 ? 41.229 -56.491 -8.138 1.00 64.16 ? 580 PHE B CG 1 ATOM 4251 C CD1 . PHE A 1 549 ? 41.696 -55.961 -6.945 1.00 64.15 ? 580 PHE B CD1 1 ATOM 4252 C CD2 . PHE A 1 549 ? 40.918 -55.626 -9.176 1.00 64.46 ? 580 PHE B CD2 1 ATOM 4253 C CE1 . PHE A 1 549 ? 41.838 -54.582 -6.775 1.00 64.15 ? 580 PHE B CE1 1 ATOM 4254 C CE2 . PHE A 1 549 ? 41.059 -54.245 -9.018 1.00 64.61 ? 580 PHE B CE2 1 ATOM 4255 C CZ . PHE A 1 549 ? 41.519 -53.725 -7.805 1.00 64.18 ? 580 PHE B CZ 1 ATOM 4256 N N . GLY A 1 550 ? 42.335 -60.671 -7.150 1.00 73.44 ? 581 GLY B N 1 ATOM 4257 C CA . GLY A 1 550 ? 42.616 -61.464 -5.975 1.00 73.79 ? 581 GLY B CA 1 ATOM 4258 C C . GLY A 1 550 ? 44.090 -61.778 -5.816 1.00 73.34 ? 581 GLY B C 1 ATOM 4259 O O . GLY A 1 550 ? 44.495 -62.321 -4.788 1.00 73.59 ? 581 GLY B O 1 ATOM 4260 N N . SER A 1 551 ? 44.898 -61.441 -6.820 1.00 91.43 ? 582 SER B N 1 ATOM 4261 C CA . SER A 1 551 ? 46.313 -61.804 -6.783 1.00 91.04 ? 582 SER B CA 1 ATOM 4262 C C . SER A 1 551 ? 47.167 -60.722 -6.120 1.00 90.67 ? 582 SER B C 1 ATOM 4263 O O . SER A 1 551 ? 48.391 -60.823 -6.086 1.00 90.41 ? 582 SER B O 1 ATOM 4264 C CB . SER A 1 551 ? 46.834 -62.131 -8.188 1.00 90.66 ? 582 SER B CB 1 ATOM 4265 O OG . SER A 1 551 ? 47.723 -63.240 -8.164 1.00 89.79 ? 582 SER B OG 1 ATOM 4266 N N . SER A 1 552 ? 46.517 -59.692 -5.589 1.00 61.86 ? 583 SER B N 1 ATOM 4267 C CA . SER A 1 552 ? 47.235 -58.543 -5.025 1.00 61.54 ? 583 SER B CA 1 ATOM 4268 C C . SER A 1 552 ? 47.427 -58.618 -3.532 1.00 61.71 ? 583 SER B C 1 ATOM 4269 O O . SER A 1 552 ? 46.464 -58.677 -2.781 1.00 62.11 ? 583 SER B O 1 ATOM 4270 C CB . SER A 1 552 ? 46.513 -57.229 -5.344 1.00 61.63 ? 583 SER B CB 1 ATOM 4271 O OG . SER A 1 552 ? 47.171 -56.111 -4.754 1.00 61.33 ? 583 SER B OG 1 ATOM 4272 N N . LYS A 1 553 ? 48.672 -58.567 -3.096 1.00 83.16 ? 584 LYS B N 1 ATOM 4273 C CA . LYS A 1 553 ? 48.956 -58.672 -1.681 1.00 83.49 ? 584 LYS B CA 1 ATOM 4274 C C . LYS A 1 553 ? 48.653 -57.383 -0.902 1.00 83.56 ? 584 LYS B C 1 ATOM 4275 O O . LYS A 1 553 ? 48.681 -57.384 0.318 1.00 83.99 ? 584 LYS B O 1 ATOM 4276 C CB . LYS A 1 553 ? 50.394 -59.170 -1.464 1.00 83.17 ? 584 LYS B CB 1 ATOM 4277 C CG . LYS A 1 553 ? 51.501 -58.119 -1.460 1.00 82.62 ? 584 LYS B CG 1 ATOM 4278 C CD . LYS A 1 553 ? 51.494 -57.216 -2.690 1.00 82.16 ? 584 LYS B CD 1 ATOM 4279 C CE . LYS A 1 553 ? 51.579 -57.966 -4.015 1.00 82.04 ? 584 LYS B CE 1 ATOM 4280 N NZ . LYS A 1 553 ? 51.251 -57.054 -5.158 1.00 81.82 ? 584 LYS B NZ 1 ATOM 4281 N N . THR A 1 554 ? 48.382 -56.283 -1.598 1.00 63.47 ? 585 THR B N 1 ATOM 4282 C CA . THR A 1 554 ? 48.131 -55.007 -0.923 1.00 63.44 ? 585 THR B CA 1 ATOM 4283 C C . THR A 1 554 ? 46.695 -54.480 -0.723 1.00 64.09 ? 585 THR B C 1 ATOM 4284 O O . THR A 1 554 ? 46.514 -53.473 -0.044 1.00 64.30 ? 585 THR B O 1 ATOM 4285 C CB . THR A 1 554 ? 48.913 -53.848 -1.594 1.00 62.91 ? 585 THR B CB 1 ATOM 4286 O OG1 . THR A 1 554 ? 48.378 -53.587 -2.904 1.00 63.00 ? 585 THR B OG1 1 ATOM 4287 C CG2 . THR A 1 554 ? 50.414 -54.150 -1.666 1.00 62.38 ? 585 THR B CG2 1 ATOM 4288 N N . ILE A 1 555 ? 45.665 -55.101 -1.275 1.00 68.63 ? 586 ILE B N 1 ATOM 4289 C CA . ILE A 1 555 ? 44.356 -54.480 -1.078 1.00 69.44 ? 586 ILE B CA 1 ATOM 4290 C C . ILE A 1 555 ? 43.769 -55.003 0.195 1.00 70.24 ? 586 ILE B C 1 ATOM 4291 O O . ILE A 1 555 ? 43.573 -56.210 0.348 1.00 70.46 ? 586 ILE B O 1 ATOM 4292 C CB . ILE A 1 555 ? 43.330 -54.756 -2.187 1.00 69.83 ? 586 ILE B CB 1 ATOM 4293 C CG1 . ILE A 1 555 ? 43.958 -55.516 -3.335 1.00 68.94 ? 586 ILE B CG1 1 ATOM 4294 C CG2 . ILE A 1 555 ? 42.679 -53.478 -2.623 1.00 70.55 ? 586 ILE B CG2 1 ATOM 4295 C CD1 . ILE A 1 555 ? 43.862 -56.988 -3.136 1.00 68.65 ? 586 ILE B CD1 1 ATOM 4296 N N . THR A 1 556 ? 43.544 -54.116 1.147 1.00 64.15 ? 587 THR B N 1 ATOM 4297 C CA . THR A 1 556 ? 42.722 -54.506 2.265 1.00 65.26 ? 587 THR B CA 1 ATOM 4298 C C . THR A 1 556 ? 41.265 -54.048 2.168 1.00 66.36 ? 587 THR B C 1 ATOM 4299 O O . THR A 1 556 ? 40.424 -54.538 2.903 1.00 67.26 ? 587 THR B O 1 ATOM 4300 C CB . THR A 1 556 ? 43.371 -54.092 3.575 1.00 65.43 ? 587 THR B CB 1 ATOM 4301 O OG1 . THR A 1 556 ? 43.529 -52.667 3.599 1.00 65.33 ? 587 THR B OG1 1 ATOM 4302 C CG2 . THR A 1 556 ? 44.745 -54.759 3.688 1.00 64.56 ? 587 THR B CG2 1 ATOM 4303 N N . THR A 1 557 ? 40.956 -53.149 1.238 1.00 69.68 ? 588 THR B N 1 ATOM 4304 C CA . THR A 1 557 ? 39.591 -52.623 1.124 1.00 70.85 ? 588 THR B CA 1 ATOM 4305 C C . THR A 1 557 ? 39.073 -52.507 -0.308 1.00 70.51 ? 588 THR B C 1 ATOM 4306 O O . THR A 1 557 ? 39.701 -51.896 -1.174 1.00 69.66 ? 588 THR B O 1 ATOM 4307 C CB . THR A 1 557 ? 39.421 -51.269 1.871 1.00 71.90 ? 588 THR B CB 1 ATOM 4308 O OG1 . THR A 1 557 ? 38.802 -51.510 3.137 1.00 73.07 ? 588 THR B OG1 1 ATOM 4309 C CG2 . THR A 1 557 ? 38.538 -50.287 1.098 1.00 72.14 ? 588 THR B CG2 1 ATOM 4310 N N . PHE A 1 558 ? 37.936 -53.145 -0.552 1.00 73.23 ? 589 PHE B N 1 ATOM 4311 C CA . PHE A 1 558 ? 37.186 -52.976 -1.780 1.00 73.21 ? 589 PHE B CA 1 ATOM 4312 C C . PHE A 1 558 ? 35.719 -52.841 -1.373 1.00 74.85 ? 589 PHE B C 1 ATOM 4313 O O . PHE A 1 558 ? 35.124 -53.817 -0.928 1.00 75.53 ? 589 PHE B O 1 ATOM 4314 C CB . PHE A 1 558 ? 37.374 -54.257 -2.589 1.00 72.30 ? 589 PHE B CB 1 ATOM 4315 C CG . PHE A 1 558 ? 37.249 -54.087 -4.076 1.00 71.80 ? 589 PHE B CG 1 ATOM 4316 C CD1 . PHE A 1 558 ? 38.271 -53.512 -4.808 1.00 70.69 ? 589 PHE B CD1 1 ATOM 4317 C CD2 . PHE A 1 558 ? 36.135 -54.550 -4.743 1.00 72.47 ? 589 PHE B CD2 1 ATOM 4318 C CE1 . PHE A 1 558 ? 38.170 -53.372 -6.158 1.00 70.28 ? 589 PHE B CE1 1 ATOM 4319 C CE2 . PHE A 1 558 ? 36.030 -54.410 -6.091 1.00 71.99 ? 589 PHE B CE2 1 ATOM 4320 C CZ . PHE A 1 558 ? 37.048 -53.821 -6.800 1.00 70.91 ? 589 PHE B CZ 1 ATOM 4321 N N . ASN A 1 559 ? 35.103 -51.673 -1.522 1.00 72.71 ? 590 ASN B N 1 ATOM 4322 C CA . ASN A 1 559 ? 33.685 -51.615 -1.200 1.00 74.43 ? 590 ASN B CA 1 ATOM 4323 C C . ASN A 1 559 ? 32.889 -51.255 -2.432 1.00 74.62 ? 590 ASN B C 1 ATOM 4324 O O . ASN A 1 559 ? 32.817 -50.093 -2.796 1.00 74.80 ? 590 ASN B O 1 ATOM 4325 C CB . ASN A 1 559 ? 33.445 -50.597 -0.083 1.00 75.82 ? 590 ASN B CB 1 ATOM 4326 C CG . ASN A 1 559 ? 32.058 -50.712 0.539 1.00 77.60 ? 590 ASN B CG 1 ATOM 4327 O OD1 . ASN A 1 559 ? 31.297 -51.631 0.219 1.00 77.89 ? 590 ASN B OD1 1 ATOM 4328 N ND2 . ASN A 1 559 ? 31.728 -49.782 1.446 1.00 78.82 ? 590 ASN B ND2 1 ATOM 4329 N N . VAL A 1 560 ? 32.262 -52.254 -3.045 1.00 68.90 ? 591 VAL B N 1 ATOM 4330 C CA . VAL A 1 560 ? 31.477 -52.077 -4.273 1.00 69.62 ? 591 VAL B CA 1 ATOM 4331 C C . VAL A 1 560 ? 29.954 -52.022 -4.090 1.00 70.81 ? 591 VAL B C 1 ATOM 4332 O O . VAL A 1 560 ? 29.204 -52.116 -5.064 1.00 71.42 ? 591 VAL B O 1 ATOM 4333 C CB . VAL A 1 560 ? 31.902 -53.047 -5.385 1.00 69.09 ? 591 VAL B CB 1 ATOM 4334 C CG1 . VAL A 1 560 ? 33.160 -52.544 -6.049 1.00 68.38 ? 591 VAL B CG1 1 ATOM 4335 C CG2 . VAL A 1 560 ? 32.134 -54.423 -4.821 1.00 68.49 ? 591 VAL B CG2 1 ATOM 4336 N N . SER A 1 561 ? 29.521 -51.946 -2.831 1.00 71.19 ? 592 SER B N 1 ATOM 4337 C CA . SER A 1 561 ? 28.106 -52.036 -2.445 1.00 72.35 ? 592 SER B CA 1 ATOM 4338 C C . SER A 1 561 ? 27.159 -51.008 -3.063 1.00 73.56 ? 592 SER B C 1 ATOM 4339 O O . SER A 1 561 ? 27.545 -49.887 -3.364 1.00 73.68 ? 592 SER B O 1 ATOM 4340 C CB . SER A 1 561 ? 27.957 -52.036 -0.913 1.00 72.52 ? 592 SER B CB 1 ATOM 4341 O OG . SER A 1 561 ? 29.011 -51.342 -0.280 1.00 71.85 ? 592 SER B OG 1 ATOM 4342 N N . TYR A 1 562 ? 25.912 -51.425 -3.243 1.00 87.99 ? 593 TYR B N 1 ATOM 4343 C CA . TYR A 1 562 ? 24.899 -50.595 -3.862 1.00 88.89 ? 593 TYR B CA 1 ATOM 4344 C C . TYR A 1 562 ? 25.334 -50.196 -5.254 1.00 87.43 ? 593 TYR B C 1 ATOM 4345 O O . TYR A 1 562 ? 25.545 -49.016 -5.540 1.00 87.18 ? 593 TYR B O 1 ATOM 4346 C CB . TYR A 1 562 ? 24.621 -49.361 -3.013 1.00 90.08 ? 593 TYR B CB 1 ATOM 4347 C CG . TYR A 1 562 ? 24.124 -49.706 -1.639 1.00 91.68 ? 593 TYR B CG 1 ATOM 4348 C CD1 . TYR A 1 562 ? 25.008 -50.033 -0.626 1.00 91.29 ? 593 TYR B CD1 1 ATOM 4349 C CD2 . TYR A 1 562 ? 22.766 -49.715 -1.356 1.00 93.62 ? 593 TYR B CD2 1 ATOM 4350 C CE1 . TYR A 1 562 ? 24.559 -50.355 0.634 1.00 92.78 ? 593 TYR B CE1 1 ATOM 4351 C CE2 . TYR A 1 562 ? 22.304 -50.036 -0.100 1.00 95.17 ? 593 TYR B CE2 1 ATOM 4352 C CZ . TYR A 1 562 ? 23.206 -50.356 0.892 1.00 94.75 ? 593 TYR B CZ 1 ATOM 4353 O OH . TYR A 1 562 ? 22.754 -50.673 2.149 1.00 96.31 ? 593 TYR B OH 1 ATOM 4354 N N . ASN A 1 563 ? 25.472 -51.202 -6.112 1.00 91.29 ? 594 ASN B N 1 ATOM 4355 C CA . ASN A 1 563 ? 25.776 -50.986 -7.517 1.00 89.92 ? 594 ASN B CA 1 ATOM 4356 C C . ASN A 1 563 ? 25.051 -52.005 -8.354 1.00 89.90 ? 594 ASN B C 1 ATOM 4357 O O . ASN A 1 563 ? 24.308 -52.825 -7.832 1.00 90.98 ? 594 ASN B O 1 ATOM 4358 C CB . ASN A 1 563 ? 27.278 -51.062 -7.770 1.00 88.14 ? 594 ASN B CB 1 ATOM 4359 C CG . ASN A 1 563 ? 27.988 -49.801 -7.348 1.00 87.60 ? 594 ASN B CG 1 ATOM 4360 O OD1 . ASN A 1 563 ? 28.218 -48.904 -8.153 1.00 86.90 ? 594 ASN B OD1 1 ATOM 4361 N ND2 . ASN A 1 563 ? 28.315 -49.712 -6.070 1.00 87.94 ? 594 ASN B ND2 1 ATOM 4362 N N . GLN A 1 564 ? 25.262 -51.931 -9.658 1.00 81.72 ? 595 GLN B N 1 ATOM 4363 C CA . GLN A 1 564 ? 24.597 -52.810 -10.602 1.00 81.58 ? 595 GLN B CA 1 ATOM 4364 C C . GLN A 1 564 ? 25.449 -54.032 -10.967 1.00 80.03 ? 595 GLN B C 1 ATOM 4365 O O . GLN A 1 564 ? 25.074 -54.803 -11.844 1.00 79.81 ? 595 GLN B O 1 ATOM 4366 C CB . GLN A 1 564 ? 24.209 -52.031 -11.855 1.00 81.32 ? 595 GLN B CB 1 ATOM 4367 C CG . GLN A 1 564 ? 23.511 -50.709 -11.594 1.00 82.70 ? 595 GLN B CG 1 ATOM 4368 C CD . GLN A 1 564 ? 22.005 -50.840 -11.569 1.00 84.73 ? 595 GLN B CD 1 ATOM 4369 O OE1 . GLN A 1 564 ? 21.469 -51.810 -11.041 1.00 85.89 ? 595 GLN B OE1 1 ATOM 4370 N NE2 . GLN A 1 564 ? 21.312 -49.864 -12.150 1.00 85.19 ? 595 GLN B NE2 1 ATOM 4371 N N . LEU A 1 565 ? 26.583 -54.207 -10.290 1.00 78.32 ? 596 LEU B N 1 ATOM 4372 C CA . LEU A 1 565 ? 27.562 -55.243 -10.643 1.00 76.72 ? 596 LEU B CA 1 ATOM 4373 C C . LEU A 1 565 ? 26.975 -56.628 -10.742 1.00 77.06 ? 596 LEU B C 1 ATOM 4374 O O . LEU A 1 565 ? 25.997 -56.954 -10.082 1.00 78.59 ? 596 LEU B O 1 ATOM 4375 C CB . LEU A 1 565 ? 28.704 -55.299 -9.633 1.00 76.03 ? 596 LEU B CB 1 ATOM 4376 C CG . LEU A 1 565 ? 29.876 -54.336 -9.789 1.00 75.20 ? 596 LEU B CG 1 ATOM 4377 C CD1 . LEU A 1 565 ? 30.755 -54.425 -8.568 1.00 74.97 ? 596 LEU B CD1 1 ATOM 4378 C CD2 . LEU A 1 565 ? 30.674 -54.661 -11.033 1.00 73.54 ? 596 LEU B CD2 1 ATOM 4379 N N . ILE A 1 566 ? 27.569 -57.424 -11.618 1.00 78.27 ? 597 ILE B N 1 ATOM 4380 C CA . ILE A 1 566 ? 27.125 -58.781 -11.862 1.00 78.34 ? 597 ILE B CA 1 ATOM 4381 C C . ILE A 1 566 ? 28.329 -59.672 -12.139 1.00 76.92 ? 597 ILE B C 1 ATOM 4382 O O . ILE A 1 566 ? 29.397 -59.187 -12.505 1.00 76.10 ? 597 ILE B O 1 ATOM 4383 C CB . ILE A 1 566 ? 26.177 -58.864 -13.077 1.00 78.63 ? 597 ILE B CB 1 ATOM 4384 C CG1 . ILE A 1 566 ? 26.913 -58.452 -14.358 1.00 77.41 ? 597 ILE B CG1 1 ATOM 4385 C CG2 . ILE A 1 566 ? 24.919 -58.018 -12.857 1.00 80.24 ? 597 ILE B CG2 1 ATOM 4386 C CD1 . ILE A 1 566 ? 26.373 -59.088 -15.642 1.00 77.16 ? 597 ILE B CD1 1 ATOM 4387 N N . GLY A 1 567 ? 28.154 -60.979 -11.971 1.00 77.87 ? 598 GLY B N 1 ATOM 4388 C CA . GLY A 1 567 ? 29.242 -61.911 -12.192 1.00 76.77 ? 598 GLY B CA 1 ATOM 4389 C C . GLY A 1 567 ? 29.863 -62.363 -10.887 1.00 76.76 ? 598 GLY B C 1 ATOM 4390 O O . GLY A 1 567 ? 29.426 -61.965 -9.814 1.00 77.71 ? 598 GLY B O 1 ATOM 4391 N N . PRO A 1 568 ? 30.886 -63.214 -10.972 1.00 67.61 ? 599 PRO B N 1 ATOM 4392 C CA . PRO A 1 568 ? 31.550 -63.790 -9.799 1.00 66.99 ? 599 PRO B CA 1 ATOM 4393 C C . PRO A 1 568 ? 32.543 -62.870 -9.105 1.00 66.58 ? 599 PRO B C 1 ATOM 4394 O O . PRO A 1 568 ? 33.144 -62.000 -9.727 1.00 66.57 ? 599 PRO B O 1 ATOM 4395 C CB . PRO A 1 568 ? 32.286 -65.000 -10.377 1.00 66.57 ? 599 PRO B CB 1 ATOM 4396 C CG . PRO A 1 568 ? 31.672 -65.229 -11.726 1.00 66.96 ? 599 PRO B CG 1 ATOM 4397 C CD . PRO A 1 568 ? 31.314 -63.870 -12.210 1.00 67.48 ? 599 PRO B CD 1 ATOM 4398 N N . ILE A 1 569 ? 32.707 -63.095 -7.807 1.00 66.30 ? 600 ILE B N 1 ATOM 4399 C CA . ILE A 1 569 ? 33.682 -62.390 -6.977 1.00 65.83 ? 600 ILE B CA 1 ATOM 4400 C C . ILE A 1 569 ? 34.990 -63.197 -6.953 1.00 65.13 ? 600 ILE B C 1 ATOM 4401 O O . ILE A 1 569 ? 34.939 -64.428 -6.954 1.00 65.08 ? 600 ILE B O 1 ATOM 4402 C CB . ILE A 1 569 ? 33.105 -62.175 -5.558 1.00 66.04 ? 600 ILE B CB 1 ATOM 4403 C CG1 . ILE A 1 569 ? 32.132 -60.995 -5.570 1.00 66.92 ? 600 ILE B CG1 1 ATOM 4404 C CG2 . ILE A 1 569 ? 34.203 -61.940 -4.549 1.00 65.40 ? 600 ILE B CG2 1 ATOM 4405 C CD1 . ILE A 1 569 ? 31.054 -61.047 -4.524 1.00 67.68 ? 600 ILE B CD1 1 ATOM 4406 N N . PRO A 1 570 ? 36.161 -62.521 -6.988 1.00 64.68 ? 601 PRO B N 1 ATOM 4407 C CA . PRO A 1 570 ? 37.447 -63.232 -7.081 1.00 64.22 ? 601 PRO B CA 1 ATOM 4408 C C . PRO A 1 570 ? 37.876 -64.061 -5.859 1.00 63.89 ? 601 PRO B C 1 ATOM 4409 O O . PRO A 1 570 ? 37.839 -63.575 -4.732 1.00 63.74 ? 601 PRO B O 1 ATOM 4410 C CB . PRO A 1 570 ? 38.454 -62.099 -7.331 1.00 63.89 ? 601 PRO B CB 1 ATOM 4411 C CG . PRO A 1 570 ? 37.657 -60.998 -7.901 1.00 64.67 ? 601 PRO B CG 1 ATOM 4412 C CD . PRO A 1 570 ? 36.333 -61.077 -7.204 1.00 64.69 ? 601 PRO B CD 1 ATOM 4413 N N . SER A 1 571 ? 38.288 -65.306 -6.093 1.00 110.23 ? 602 SER B N 1 ATOM 4414 C CA . SER A 1 571 ? 38.972 -66.080 -5.060 1.00 110.53 ? 602 SER B CA 1 ATOM 4415 C C . SER A 1 571 ? 40.429 -65.637 -5.069 1.00 109.83 ? 602 SER B C 1 ATOM 4416 O O . SER A 1 571 ? 41.090 -65.673 -6.107 1.00 109.21 ? 602 SER B O 1 ATOM 4417 C CB . SER A 1 571 ? 38.829 -67.598 -5.272 1.00 110.98 ? 602 SER B CB 1 ATOM 4418 O OG . SER A 1 571 ? 39.312 -68.028 -6.534 1.00 110.52 ? 602 SER B OG 1 ATOM 4419 N N . GLY A 1 572 ? 40.922 -65.204 -3.914 1.00 62.76 ? 603 GLY B N 1 ATOM 4420 C CA . GLY A 1 572 ? 42.153 -64.437 -3.851 1.00 62.35 ? 603 GLY B CA 1 ATOM 4421 C C . GLY A 1 572 ? 42.345 -63.807 -2.492 1.00 62.07 ? 603 GLY B C 1 ATOM 4422 O O . GLY A 1 572 ? 41.952 -64.367 -1.476 1.00 62.14 ? 603 GLY B O 1 ATOM 4423 N N . SER A 1 573 ? 43.020 -62.666 -2.464 1.00 79.72 ? 604 SER B N 1 ATOM 4424 C CA . SER A 1 573 ? 43.014 -61.816 -1.279 1.00 79.99 ? 604 SER B CA 1 ATOM 4425 C C . SER A 1 573 ? 41.581 -61.526 -0.881 1.00 80.77 ? 604 SER B C 1 ATOM 4426 O O . SER A 1 573 ? 41.265 -61.331 0.296 1.00 81.47 ? 604 SER B O 1 ATOM 4427 C CB . SER A 1 573 ? 43.712 -60.497 -1.567 1.00 79.31 ? 604 SER B CB 1 ATOM 4428 O OG . SER A 1 573 ? 44.993 -60.742 -2.095 1.00 78.76 ? 604 SER B OG 1 ATOM 4429 N N . PHE A 1 574 ? 40.707 -61.527 -1.874 1.00 72.55 ? 605 PHE B N 1 ATOM 4430 C CA . PHE A 1 574 ? 39.306 -61.292 -1.630 1.00 73.33 ? 605 PHE B CA 1 ATOM 4431 C C . PHE A 1 574 ? 38.666 -62.304 -0.683 1.00 74.08 ? 605 PHE B C 1 ATOM 4432 O O . PHE A 1 574 ? 37.559 -62.073 -0.202 1.00 74.86 ? 605 PHE B O 1 ATOM 4433 C CB . PHE A 1 574 ? 38.551 -61.261 -2.947 1.00 73.13 ? 605 PHE B CB 1 ATOM 4434 C CG . PHE A 1 574 ? 38.436 -59.890 -3.537 1.00 72.93 ? 605 PHE B CG 1 ATOM 4435 C CD1 . PHE A 1 574 ? 39.568 -59.181 -3.896 1.00 72.09 ? 605 PHE B CD1 1 ATOM 4436 C CD2 . PHE A 1 574 ? 37.193 -59.307 -3.734 1.00 73.68 ? 605 PHE B CD2 1 ATOM 4437 C CE1 . PHE A 1 574 ? 39.465 -57.921 -4.442 1.00 71.92 ? 605 PHE B CE1 1 ATOM 4438 C CE2 . PHE A 1 574 ? 37.086 -58.043 -4.275 1.00 73.59 ? 605 PHE B CE2 1 ATOM 4439 C CZ . PHE A 1 574 ? 38.225 -57.351 -4.632 1.00 72.66 ? 605 PHE B CZ 1 ATOM 4440 N N . ALA A 1 575 ? 39.347 -63.414 -0.405 1.00 62.86 ? 606 ALA B N 1 ATOM 4441 C CA . ALA A 1 575 ? 38.806 -64.412 0.514 1.00 63.06 ? 606 ALA B CA 1 ATOM 4442 C C . ALA A 1 575 ? 38.742 -63.842 1.916 1.00 63.17 ? 606 ALA B C 1 ATOM 4443 O O . ALA A 1 575 ? 37.847 -64.165 2.685 1.00 63.56 ? 606 ALA B O 1 ATOM 4444 C CB . ALA A 1 575 ? 39.643 -65.673 0.494 1.00 62.83 ? 606 ALA B CB 1 ATOM 4445 N N . HIS A 1 576 ? 39.676 -62.950 2.223 1.00 90.77 ? 607 HIS B N 1 ATOM 4446 C CA . HIS A 1 576 ? 39.802 -62.421 3.571 1.00 91.41 ? 607 HIS B CA 1 ATOM 4447 C C . HIS A 1 576 ? 38.897 -61.214 3.769 1.00 92.11 ? 607 HIS B C 1 ATOM 4448 O O . HIS A 1 576 ? 38.980 -60.534 4.790 1.00 92.65 ? 607 HIS B O 1 ATOM 4449 C CB . HIS A 1 576 ? 41.255 -62.052 3.868 1.00 90.85 ? 607 HIS B CB 1 ATOM 4450 C CG . HIS A 1 576 ? 42.189 -63.220 3.824 1.00 90.44 ? 607 HIS B CG 1 ATOM 4451 N ND1 . HIS A 1 576 ? 42.046 -64.319 4.644 1.00 90.93 ? 607 HIS B ND1 1 ATOM 4452 C CD2 . HIS A 1 576 ? 43.277 -63.466 3.054 1.00 89.70 ? 607 HIS B CD2 1 ATOM 4453 C CE1 . HIS A 1 576 ? 43.008 -65.187 4.388 1.00 90.62 ? 607 HIS B CE1 1 ATOM 4454 N NE2 . HIS A 1 576 ? 43.769 -64.694 3.425 1.00 89.90 ? 607 HIS B NE2 1 ATOM 4455 N N . LEU A 1 577 ? 38.048 -60.940 2.778 1.00 66.06 ? 608 LEU B N 1 ATOM 4456 C CA . LEU A 1 577 ? 37.237 -59.719 2.772 1.00 66.79 ? 608 LEU B CA 1 ATOM 4457 C C . LEU A 1 577 ? 35.922 -59.816 3.543 1.00 67.91 ? 608 LEU B C 1 ATOM 4458 O O . LEU A 1 577 ? 35.484 -60.900 3.946 1.00 68.12 ? 608 LEU B O 1 ATOM 4459 C CB . LEU A 1 577 ? 36.914 -59.305 1.329 1.00 66.57 ? 608 LEU B CB 1 ATOM 4460 C CG . LEU A 1 577 ? 37.905 -58.500 0.494 1.00 65.41 ? 608 LEU B CG 1 ATOM 4461 C CD1 . LEU A 1 577 ? 37.163 -57.356 -0.116 1.00 65.53 ? 608 LEU B CD1 1 ATOM 4462 C CD2 . LEU A 1 577 ? 39.062 -57.988 1.318 1.00 64.99 ? 608 LEU B CD2 1 ATOM 4463 N N . ASN A 1 578 ? 35.260 -58.671 3.665 1.00 68.39 ? 609 ASN B N 1 ATOM 4464 C CA . ASN A 1 578 ? 34.022 -58.584 4.413 1.00 69.90 ? 609 ASN B CA 1 ATOM 4465 C C . ASN A 1 578 ? 32.847 -58.636 3.485 1.00 70.67 ? 609 ASN B C 1 ATOM 4466 O O . ASN A 1 578 ? 32.737 -57.802 2.605 1.00 70.49 ? 609 ASN B O 1 ATOM 4467 C CB . ASN A 1 578 ? 33.946 -57.281 5.197 1.00 70.80 ? 609 ASN B CB 1 ATOM 4468 C CG . ASN A 1 578 ? 32.515 -56.897 5.528 1.00 72.71 ? 609 ASN B CG 1 ATOM 4469 O OD1 . ASN A 1 578 ? 31.863 -56.179 4.767 1.00 73.19 ? 609 ASN B OD1 1 ATOM 4470 N ND2 . ASN A 1 578 ? 32.012 -57.391 6.657 1.00 73.92 ? 609 ASN B ND2 1 ATOM 4471 N N . PRO A 1 579 ? 31.945 -59.593 3.703 1.00 67.56 ? 610 PRO B N 1 ATOM 4472 C CA . PRO A 1 579 ? 30.817 -59.802 2.795 1.00 68.30 ? 610 PRO B CA 1 ATOM 4473 C C . PRO A 1 579 ? 30.065 -58.510 2.531 1.00 69.14 ? 610 PRO B C 1 ATOM 4474 O O . PRO A 1 579 ? 29.730 -58.208 1.392 1.00 69.46 ? 610 PRO B O 1 ATOM 4475 C CB . PRO A 1 579 ? 29.930 -60.783 3.555 1.00 68.82 ? 610 PRO B CB 1 ATOM 4476 C CG . PRO A 1 579 ? 30.849 -61.473 4.496 1.00 68.06 ? 610 PRO B CG 1 ATOM 4477 C CD . PRO A 1 579 ? 31.894 -60.482 4.874 1.00 67.54 ? 610 PRO B CD 1 ATOM 4478 N N . SER A 1 580 ? 29.853 -57.713 3.562 1.00 89.40 ? 611 SER B N 1 ATOM 4479 C CA . SER A 1 580 ? 28.987 -56.556 3.411 1.00 90.69 ? 611 SER B CA 1 ATOM 4480 C C . SER A 1 580 ? 29.536 -55.500 2.439 1.00 89.47 ? 611 SER B C 1 ATOM 4481 O O . SER A 1 580 ? 28.859 -54.519 2.131 1.00 90.21 ? 611 SER B O 1 ATOM 4482 C CB . SER A 1 580 ? 28.600 -55.989 4.780 1.00 91.93 ? 611 SER B CB 1 ATOM 4483 O OG . SER A 1 580 ? 27.867 -56.960 5.533 1.00 93.26 ? 611 SER B OG 1 ATOM 4484 N N . PHE A 1 581 ? 30.761 -55.720 1.959 1.00 71.35 ? 612 PHE B N 1 ATOM 4485 C CA . PHE A 1 581 ? 31.352 -54.914 0.874 1.00 70.33 ? 612 PHE B CA 1 ATOM 4486 C C . PHE A 1 581 ? 30.571 -55.038 -0.407 1.00 70.53 ? 612 PHE B C 1 ATOM 4487 O O . PHE A 1 581 ? 30.393 -54.054 -1.121 1.00 70.53 ? 612 PHE B O 1 ATOM 4488 C CB . PHE A 1 581 ? 32.780 -55.360 0.547 1.00 68.62 ? 612 PHE B CB 1 ATOM 4489 C CG . PHE A 1 581 ? 33.814 -54.765 1.433 1.00 68.24 ? 612 PHE B CG 1 ATOM 4490 C CD1 . PHE A 1 581 ? 33.641 -53.501 1.968 1.00 69.06 ? 612 PHE B CD1 1 ATOM 4491 C CD2 . PHE A 1 581 ? 34.961 -55.469 1.743 1.00 67.10 ? 612 PHE B CD2 1 ATOM 4492 C CE1 . PHE A 1 581 ? 34.595 -52.947 2.799 1.00 68.67 ? 612 PHE B CE1 1 ATOM 4493 C CE2 . PHE A 1 581 ? 35.919 -54.920 2.569 1.00 66.74 ? 612 PHE B CE2 1 ATOM 4494 C CZ . PHE A 1 581 ? 35.737 -53.655 3.095 1.00 67.49 ? 612 PHE B CZ 1 ATOM 4495 N N . PHE A 1 582 ? 30.149 -56.262 -0.713 1.00 74.98 ? 613 PHE B N 1 ATOM 4496 C CA . PHE A 1 582 ? 29.506 -56.555 -1.979 1.00 74.87 ? 613 PHE B CA 1 ATOM 4497 C C . PHE A 1 582 ? 27.978 -56.559 -1.926 1.00 76.72 ? 613 PHE B C 1 ATOM 4498 O O . PHE A 1 582 ? 27.321 -56.875 -2.918 1.00 76.77 ? 613 PHE B O 1 ATOM 4499 C CB . PHE A 1 582 ? 29.993 -57.894 -2.496 1.00 73.67 ? 613 PHE B CB 1 ATOM 4500 C CG . PHE A 1 582 ? 31.474 -58.084 -2.392 1.00 72.15 ? 613 PHE B CG 1 ATOM 4501 C CD1 . PHE A 1 582 ? 32.319 -57.609 -3.378 1.00 70.71 ? 613 PHE B CD1 1 ATOM 4502 C CD2 . PHE A 1 582 ? 32.019 -58.771 -1.328 1.00 72.07 ? 613 PHE B CD2 1 ATOM 4503 C CE1 . PHE A 1 582 ? 33.683 -57.805 -3.296 1.00 69.36 ? 613 PHE B CE1 1 ATOM 4504 C CE2 . PHE A 1 582 ? 33.377 -58.975 -1.243 1.00 70.79 ? 613 PHE B CE2 1 ATOM 4505 C CZ . PHE A 1 582 ? 34.211 -58.489 -2.226 1.00 69.44 ? 613 PHE B CZ 1 ATOM 4506 N N . SER A 1 583 ? 27.409 -56.228 -0.773 1.00 80.57 ? 614 SER B N 1 ATOM 4507 C CA . SER A 1 583 ? 25.956 -56.278 -0.613 1.00 82.52 ? 614 SER B CA 1 ATOM 4508 C C . SER A 1 583 ? 25.243 -55.238 -1.477 1.00 83.05 ? 614 SER B C 1 ATOM 4509 O O . SER A 1 583 ? 25.869 -54.319 -1.995 1.00 82.16 ? 614 SER B O 1 ATOM 4510 C CB . SER A 1 583 ? 25.554 -56.156 0.860 1.00 84.11 ? 614 SER B CB 1 ATOM 4511 O OG . SER A 1 583 ? 26.413 -55.266 1.543 1.00 83.59 ? 614 SER B OG 1 ATOM 4512 N N . SER A 1 584 ? 23.945 -55.438 -1.684 1.00 90.74 ? 615 SER B N 1 ATOM 4513 C CA . SER A 1 584 ? 23.138 -54.545 -2.510 1.00 91.27 ? 615 SER B CA 1 ATOM 4514 C C . SER A 1 584 ? 23.688 -54.483 -3.926 1.00 89.51 ? 615 SER B C 1 ATOM 4515 O O . SER A 1 584 ? 23.431 -53.529 -4.673 1.00 89.40 ? 615 SER B O 1 ATOM 4516 C CB . SER A 1 584 ? 23.070 -53.137 -1.910 1.00 92.13 ? 615 SER B CB 1 ATOM 4517 O OG . SER A 1 584 ? 22.473 -53.141 -0.625 1.00 93.42 ? 615 SER B OG 1 ATOM 4518 N N . ASN A 1 585 ? 24.458 -55.507 -4.276 1.00 94.67 ? 616 ASN B N 1 ATOM 4519 C CA . ASN A 1 585 ? 24.738 -55.819 -5.663 1.00 93.30 ? 616 ASN B CA 1 ATOM 4520 C C . ASN A 1 585 ? 24.083 -57.145 -5.916 1.00 93.78 ? 616 ASN B C 1 ATOM 4521 O O . ASN A 1 585 ? 24.500 -58.186 -5.408 1.00 93.57 ? 616 ASN B O 1 ATOM 4522 C CB . ASN A 1 585 ? 26.224 -55.842 -5.967 1.00 91.27 ? 616 ASN B CB 1 ATOM 4523 C CG . ASN A 1 585 ? 26.779 -54.457 -6.175 1.00 90.80 ? 616 ASN B CG 1 ATOM 4524 O OD1 . ASN A 1 585 ? 26.135 -53.468 -5.831 1.00 92.28 ? 616 ASN B OD1 1 ATOM 4525 N ND2 . ASN A 1 585 ? 27.973 -54.371 -6.733 1.00 88.79 ? 616 ASN B ND2 1 ATOM 4526 N N . GLU A 1 586 ? 23.023 -57.070 -6.699 1.00 99.12 ? 617 GLU B N 1 ATOM 4527 C CA . GLU A 1 586 ? 22.037 -58.112 -6.777 1.00 99.96 ? 617 GLU B CA 1 ATOM 4528 C C . GLU A 1 586 ? 22.495 -59.132 -7.776 1.00 98.12 ? 617 GLU B C 1 ATOM 4529 O O . GLU A 1 586 ? 21.947 -60.214 -7.845 1.00 98.29 ? 617 GLU B O 1 ATOM 4530 C CB . GLU A 1 586 ? 20.704 -57.499 -7.205 1.00 101.83 ? 617 GLU B CB 1 ATOM 4531 C CG . GLU A 1 586 ? 20.820 -56.056 -7.773 1.00 102.28 ? 617 GLU B CG 1 ATOM 4532 C CD . GLU A 1 586 ? 20.830 -54.942 -6.696 1.00 103.69 ? 617 GLU B CD 1 ATOM 4533 O OE1 . GLU A 1 586 ? 20.623 -55.242 -5.493 1.00 104.59 ? 617 GLU B OE1 1 ATOM 4534 O OE2 . GLU A 1 586 ? 21.047 -53.758 -7.059 1.00 103.91 ? 617 GLU B OE2 1 ATOM 4535 N N . GLY A 1 587 ? 23.520 -58.787 -8.543 1.00 87.20 ? 618 GLY B N 1 ATOM 4536 C CA . GLY A 1 587 ? 23.967 -59.634 -9.634 1.00 85.47 ? 618 GLY B CA 1 ATOM 4537 C C . GLY A 1 587 ? 25.252 -60.400 -9.396 1.00 83.91 ? 618 GLY B C 1 ATOM 4538 O O . GLY A 1 587 ? 25.735 -61.113 -10.277 1.00 82.60 ? 618 GLY B O 1 ATOM 4539 N N . LEU A 1 588 ? 25.826 -60.247 -8.213 1.00 71.67 ? 619 LEU B N 1 ATOM 4540 C CA . LEU A 1 588 ? 27.087 -60.901 -7.930 1.00 70.46 ? 619 LEU B CA 1 ATOM 4541 C C . LEU A 1 588 ? 26.807 -62.324 -7.511 1.00 70.27 ? 619 LEU B C 1 ATOM 4542 O O . LEU A 1 588 ? 25.772 -62.594 -6.908 1.00 71.10 ? 619 LEU B O 1 ATOM 4543 C CB . LEU A 1 588 ? 27.848 -60.160 -6.833 1.00 70.21 ? 619 LEU B CB 1 ATOM 4544 C CG . LEU A 1 588 ? 29.031 -59.262 -7.213 1.00 69.52 ? 619 LEU B CG 1 ATOM 4545 C CD1 . LEU A 1 588 ? 29.211 -59.115 -8.711 1.00 69.47 ? 619 LEU B CD1 1 ATOM 4546 C CD2 . LEU A 1 588 ? 28.869 -57.904 -6.572 1.00 70.18 ? 619 LEU B CD2 1 ATOM 4547 N N . CYS A 1 589 ? 27.723 -63.226 -7.856 1.00 70.28 ? 620 CYS B N 1 ATOM 4548 C CA . CYS A 1 589 ? 27.693 -64.601 -7.374 1.00 70.12 ? 620 CYS B CA 1 ATOM 4549 C C . CYS A 1 589 ? 29.042 -64.963 -6.746 1.00 69.10 ? 620 CYS B C 1 ATOM 4550 O O . CYS A 1 589 ? 30.036 -64.292 -6.988 1.00 68.22 ? 620 CYS B O 1 ATOM 4551 C CB . CYS A 1 589 ? 27.349 -65.554 -8.517 1.00 69.80 ? 620 CYS B CB 1 ATOM 4552 S SG . CYS A 1 589 ? 28.744 -66.195 -9.463 1.00 68.21 ? 620 CYS B SG 1 ATOM 4553 N N . GLY A 1 590 ? 29.077 -65.985 -5.902 1.00 92.90 ? 621 GLY B N 1 ATOM 4554 C CA . GLY A 1 590 ? 30.333 -66.423 -5.323 1.00 92.15 ? 621 GLY B CA 1 ATOM 4555 C C . GLY A 1 590 ? 30.099 -66.877 -3.901 1.00 93.08 ? 621 GLY B C 1 ATOM 4556 O O . GLY A 1 590 ? 28.960 -67.040 -3.487 1.00 94.43 ? 621 GLY B O 1 ATOM 4557 N N . ASP A 1 591 ? 31.163 -67.072 -3.133 1.00 71.68 ? 622 ASP B N 1 ATOM 4558 C CA . ASP A 1 591 ? 30.979 -67.386 -1.727 1.00 72.46 ? 622 ASP B CA 1 ATOM 4559 C C . ASP A 1 591 ? 30.500 -66.181 -0.939 1.00 73.55 ? 622 ASP B C 1 ATOM 4560 O O . ASP A 1 591 ? 29.468 -66.237 -0.301 1.00 74.95 ? 622 ASP B O 1 ATOM 4561 C CB . ASP A 1 591 ? 32.263 -67.923 -1.111 1.00 71.66 ? 622 ASP B CB 1 ATOM 4562 C CG . ASP A 1 591 ? 32.582 -69.316 -1.575 1.00 71.05 ? 622 ASP B CG 1 ATOM 4563 O OD1 . ASP A 1 591 ? 32.030 -69.723 -2.625 1.00 70.79 ? 622 ASP B OD1 1 ATOM 4564 O OD2 . ASP A 1 591 ? 33.382 -69.994 -0.888 1.00 70.92 ? 622 ASP B OD2 1 ATOM 4565 N N . LEU A 1 592 ? 31.234 -65.078 -1.008 1.00 72.99 ? 623 LEU B N 1 ATOM 4566 C CA . LEU A 1 592 ? 30.982 -63.943 -0.116 1.00 74.02 ? 623 LEU B CA 1 ATOM 4567 C C . LEU A 1 592 ? 29.630 -63.250 -0.302 1.00 75.56 ? 623 LEU B C 1 ATOM 4568 O O . LEU A 1 592 ? 29.224 -62.449 0.547 1.00 76.89 ? 623 LEU B O 1 ATOM 4569 C CB . LEU A 1 592 ? 32.108 -62.907 -0.195 1.00 73.12 ? 623 LEU B CB 1 ATOM 4570 C CG . LEU A 1 592 ? 33.496 -63.381 0.221 1.00 72.03 ? 623 LEU B CG 1 ATOM 4571 C CD1 . LEU A 1 592 ? 34.339 -63.765 -1.008 1.00 70.68 ? 623 LEU B CD1 1 ATOM 4572 C CD2 . LEU A 1 592 ? 34.166 -62.309 1.051 1.00 72.08 ? 623 LEU B CD2 1 ATOM 4573 N N . VAL A 1 593 ? 28.959 -63.508 -1.422 1.00 74.79 ? 624 VAL B N 1 ATOM 4574 C CA . VAL A 1 593 ? 27.589 -63.026 -1.602 1.00 76.34 ? 624 VAL B CA 1 ATOM 4575 C C . VAL A 1 593 ? 26.523 -64.076 -1.255 1.00 77.31 ? 624 VAL B C 1 ATOM 4576 O O . VAL A 1 593 ? 25.332 -63.771 -1.144 1.00 78.96 ? 624 VAL B O 1 ATOM 4577 C CB . VAL A 1 593 ? 27.367 -62.497 -3.010 1.00 76.02 ? 624 VAL B CB 1 ATOM 4578 C CG1 . VAL A 1 593 ? 26.780 -63.593 -3.895 1.00 75.70 ? 624 VAL B CG1 1 ATOM 4579 C CG2 . VAL A 1 593 ? 26.475 -61.250 -2.974 1.00 77.46 ? 624 VAL B CG2 1 ATOM 4580 N N . GLY A 1 594 ? 26.971 -65.312 -1.071 1.00 69.71 ? 625 GLY B N 1 ATOM 4581 C CA . GLY A 1 594 ? 26.133 -66.367 -0.537 1.00 70.19 ? 625 GLY B CA 1 ATOM 4582 C C . GLY A 1 594 ? 25.516 -67.231 -1.603 1.00 70.35 ? 625 GLY B C 1 ATOM 4583 O O . GLY A 1 594 ? 25.175 -68.376 -1.359 1.00 70.40 ? 625 GLY B O 1 ATOM 4584 N N . LYS A 1 595 ? 25.399 -66.676 -2.799 1.00 89.33 ? 626 LYS B N 1 ATOM 4585 C CA . LYS A 1 595 ? 24.765 -67.353 -3.918 1.00 89.04 ? 626 LYS B CA 1 ATOM 4586 C C . LYS A 1 595 ? 25.869 -67.926 -4.807 1.00 86.91 ? 626 LYS B C 1 ATOM 4587 O O . LYS A 1 595 ? 26.790 -67.211 -5.189 1.00 85.81 ? 626 LYS B O 1 ATOM 4588 C CB . LYS A 1 595 ? 23.908 -66.341 -4.698 1.00 90.04 ? 626 LYS B CB 1 ATOM 4589 C CG . LYS A 1 595 ? 23.350 -65.163 -3.846 1.00 91.87 ? 626 LYS B CG 1 ATOM 4590 C CD . LYS A 1 595 ? 23.102 -63.871 -4.669 1.00 92.22 ? 626 LYS B CD 1 ATOM 4591 C CE . LYS A 1 595 ? 22.626 -62.687 -3.797 1.00 93.90 ? 626 LYS B CE 1 ATOM 4592 N NZ . LYS A 1 595 ? 22.645 -61.352 -4.489 1.00 93.85 ? 626 LYS B NZ 1 ATOM 4593 N N . PRO A 1 596 ? 25.808 -69.225 -5.116 1.00 77.05 ? 627 PRO B N 1 ATOM 4594 C CA . PRO A 1 596 ? 26.852 -69.856 -5.929 1.00 75.43 ? 627 PRO B CA 1 ATOM 4595 C C . PRO A 1 596 ? 26.721 -69.590 -7.423 1.00 74.88 ? 627 PRO B C 1 ATOM 4596 O O . PRO A 1 596 ? 25.635 -69.272 -7.918 1.00 75.71 ? 627 PRO B O 1 ATOM 4597 C CB . PRO A 1 596 ? 26.653 -71.349 -5.668 1.00 75.54 ? 627 PRO B CB 1 ATOM 4598 C CG . PRO A 1 596 ? 25.794 -71.419 -4.467 1.00 76.35 ? 627 PRO B CG 1 ATOM 4599 C CD . PRO A 1 596 ? 24.905 -70.222 -4.548 1.00 77.96 ? 627 PRO B CD 1 ATOM 4600 N N . CYS A 1 597 ? 27.842 -69.718 -8.128 1.00 90.57 ? 628 CYS B N 1 ATOM 4601 C CA . CYS A 1 597 ? 27.873 -69.679 -9.579 1.00 90.02 ? 628 CYS B CA 1 ATOM 4602 C C . CYS A 1 597 ? 27.759 -71.135 -9.996 1.00 89.80 ? 628 CYS B C 1 ATOM 4603 O O . CYS A 1 597 ? 27.623 -71.999 -9.128 1.00 90.12 ? 628 CYS B O 1 ATOM 4604 C CB . CYS A 1 597 ? 29.203 -69.087 -10.026 1.00 89.01 ? 628 CYS B CB 1 ATOM 4605 S SG . CYS A 1 597 ? 29.821 -67.827 -8.871 1.00 89.27 ? 628 CYS B SG 1 ATOM 4606 N N . ASN A 1 598 ? 27.808 -71.421 -11.295 1.00 68.00 ? 629 ASN B N 1 ATOM 4607 C CA . ASN A 1 598 ? 27.760 -72.814 -11.773 1.00 67.99 ? 629 ASN B CA 1 ATOM 4608 C C . ASN A 1 598 ? 26.497 -73.574 -11.343 1.00 68.36 ? 629 ASN B C 1 ATOM 4609 O O . ASN A 1 598 ? 26.456 -74.201 -10.280 1.00 68.38 ? 629 ASN B O 1 ATOM 4610 C CB . ASN A 1 598 ? 29.004 -73.609 -11.345 1.00 67.48 ? 629 ASN B CB 1 ATOM 4611 C CG . ASN A 1 598 ? 30.293 -73.049 -11.920 1.00 67.24 ? 629 ASN B CG 1 ATOM 4612 O OD1 . ASN A 1 598 ? 30.284 -72.378 -12.959 1.00 67.49 ? 629 ASN B OD1 1 ATOM 4613 N ND2 . ASN A 1 598 ? 31.417 -73.324 -11.248 1.00 66.82 ? 629 ASN B ND2 1 ATOM 4614 N N . HIS B 2 1 ? 74.148 -31.442 28.284 1.00 72.79 ? 93 HIS C N 1 ATOM 4615 C CA . HIS B 2 1 ? 72.835 -30.807 28.323 1.00 73.15 ? 93 HIS C CA 1 ATOM 4616 C C . HIS B 2 1 ? 72.801 -29.494 27.529 1.00 73.25 ? 93 HIS C C 1 ATOM 4617 O O . HIS B 2 1 ? 73.519 -28.555 27.845 1.00 73.08 ? 93 HIS C O 1 ATOM 4618 C CB . HIS B 2 1 ? 72.432 -30.577 29.774 1.00 73.25 ? 93 HIS C CB 1 ATOM 4619 C CG . HIS B 2 1 ? 71.023 -30.105 29.946 1.00 73.87 ? 93 HIS C CG 1 ATOM 4620 N ND1 . HIS B 2 1 ? 70.577 -29.517 31.111 1.00 74.14 ? 93 HIS C ND1 1 ATOM 4621 C CD2 . HIS B 2 1 ? 69.961 -30.138 29.106 1.00 74.38 ? 93 HIS C CD2 1 ATOM 4622 C CE1 . HIS B 2 1 ? 69.299 -29.209 30.981 1.00 74.84 ? 93 HIS C CE1 1 ATOM 4623 N NE2 . HIS B 2 1 ? 68.900 -29.571 29.773 1.00 74.99 ? 93 HIS C NE2 1 ATOM 4624 N N . GLU B 2 2 ? 71.981 -29.447 26.485 1.00 74.10 ? 94 GLU C N 1 ATOM 4625 C CA . GLU B 2 2 ? 71.737 -28.203 25.776 1.00 74.39 ? 94 GLU C CA 1 ATOM 4626 C C . GLU B 2 2 ? 70.295 -27.787 25.974 1.00 74.90 ? 94 GLU C C 1 ATOM 4627 O O . GLU B 2 2 ? 69.404 -28.628 26.089 1.00 75.15 ? 94 GLU C O 1 ATOM 4628 C CB . GLU B 2 2 ? 72.038 -28.312 24.278 1.00 74.57 ? 94 GLU C CB 1 ATOM 4629 C CG . GLU B 2 2 ? 73.439 -27.823 23.839 1.00 74.47 ? 94 GLU C CG 1 ATOM 4630 C CD . GLU B 2 2 ? 73.457 -27.188 22.427 1.00 74.92 ? 94 GLU C CD 1 ATOM 4631 O OE1 . GLU B 2 2 ? 73.709 -25.963 22.333 1.00 75.27 ? 94 GLU C OE1 1 ATOM 4632 O OE2 . GLU B 2 2 ? 73.234 -27.902 21.417 1.00 74.96 ? 94 GLU C OE2 1 ATOM 4633 N N . VAL B 2 3 ? 70.083 -26.474 25.978 1.00 61.53 ? 95 VAL C N 1 ATOM 4634 C CA . VAL B 2 3 ? 68.816 -25.868 26.373 1.00 62.06 ? 95 VAL C CA 1 ATOM 4635 C C . VAL B 2 3 ? 68.242 -25.057 25.220 1.00 62.61 ? 95 VAL C C 1 ATOM 4636 O O . VAL B 2 3 ? 69.002 -24.340 24.546 1.00 62.57 ? 95 VAL C O 1 ATOM 4637 C CB . VAL B 2 3 ? 69.077 -24.851 27.499 1.00 61.99 ? 95 VAL C CB 1 ATOM 4638 C CG1 . VAL B 2 3 ? 67.774 -24.192 27.983 1.00 62.60 ? 95 VAL C CG1 1 ATOM 4639 C CG2 . VAL B 2 3 ? 69.847 -25.485 28.644 1.00 61.54 ? 95 VAL C CG2 1 ATOM 4640 N N . PRO B 2 4 ? 66.899 -25.139 25.009 1.00 54.02 ? 96 PRO C N 1 ATOM 4641 C CA . PRO B 2 4 ? 66.195 -24.353 23.985 1.00 54.85 ? 96 PRO C CA 1 ATOM 4642 C C . PRO B 2 4 ? 66.397 -22.887 24.199 1.00 55.31 ? 96 PRO C C 1 ATOM 4643 O O . PRO B 2 4 ? 66.485 -22.508 25.375 1.00 55.07 ? 96 PRO C O 1 ATOM 4644 C CB . PRO B 2 4 ? 64.722 -24.602 24.310 1.00 55.23 ? 96 PRO C CB 1 ATOM 4645 C CG . PRO B 2 4 ? 64.659 -25.854 24.975 1.00 54.62 ? 96 PRO C CG 1 ATOM 4646 C CD . PRO B 2 4 ? 65.968 -26.040 25.720 1.00 53.88 ? 96 PRO C CD 1 ATOM 4647 N N . SER B 2 5 ? 66.454 -22.081 23.140 1.00 66.15 ? 97 SER C N 1 ATOM 4648 C CA . SER B 2 5 ? 66.364 -20.631 23.359 1.00 66.36 ? 97 SER C CA 1 ATOM 4649 C C . SER B 2 5 ? 65.614 -19.858 22.296 1.00 67.20 ? 97 SER C C 1 ATOM 4650 O O . SER B 2 5 ? 65.840 -20.027 21.103 1.00 67.96 ? 97 SER C O 1 ATOM 4651 C CB . SER B 2 5 ? 67.743 -19.977 23.559 1.00 65.84 ? 97 SER C CB 1 ATOM 4652 O OG . SER B 2 5 ? 68.396 -19.733 22.314 1.00 66.70 ? 97 SER C OG 1 ATOM 4653 N N . GLY B 2 6 ? 64.698 -19.006 22.708 1.00 66.06 ? 98 GLY C N 1 ATOM 4654 C CA . GLY B 2 6 ? 64.177 -18.064 21.753 1.00 66.72 ? 98 GLY C CA 1 ATOM 4655 C C . GLY B 2 6 ? 62.710 -17.961 21.989 1.00 67.50 ? 98 GLY C C 1 ATOM 4656 O O . GLY B 2 6 ? 62.204 -18.258 23.073 1.00 67.58 ? 98 GLY C O 1 HETATM 4657 N N . HYP B 2 7 ? 62.031 -17.459 20.973 1.00 77.52 ? 99 HYP C N 1 HETATM 4658 C CA . HYP B 2 7 ? 60.563 -17.484 20.945 1.00 78.12 ? 99 HYP C CA 1 HETATM 4659 C C . HYP B 2 7 ? 60.013 -18.903 20.857 1.00 77.19 ? 99 HYP C C 1 HETATM 4660 O O . HYP B 2 7 ? 60.811 -19.833 20.482 1.00 76.27 ? 99 HYP C O 1 HETATM 4661 C CB . HYP B 2 7 ? 60.034 -16.657 19.832 1.00 79.61 ? 99 HYP C CB 1 HETATM 4662 C CG . HYP B 2 7 ? 61.158 -16.688 18.878 1.00 79.58 ? 99 HYP C CG 1 HETATM 4663 C CD . HYP B 2 7 ? 62.332 -17.339 19.576 1.00 78.19 ? 99 HYP C CD 1 HETATM 4664 O OD1 . HYP B 2 7 ? 61.441 -15.378 18.481 1.00 80.90 ? 99 HYP C OD1 1 ATOM 4665 N N . ASN B 2 8 ? 58.744 -19.118 21.244 1.00 65.46 ? 100 ASN C N 1 ATOM 4666 C CA . ASN B 2 8 ? 58.097 -20.423 21.101 1.00 65.74 ? 100 ASN C CA 1 ATOM 4667 C C . ASN B 2 8 ? 57.818 -20.716 19.650 1.00 65.88 ? 100 ASN C C 1 ATOM 4668 O O . ASN B 2 8 ? 57.121 -19.945 18.989 1.00 66.37 ? 100 ASN C O 1 ATOM 4669 C CB . ASN B 2 8 ? 56.757 -20.490 21.837 1.00 66.60 ? 100 ASN C CB 1 ATOM 4670 C CG . ASN B 2 8 ? 56.133 -21.908 21.819 1.00 66.96 ? 100 ASN C CG 1 ATOM 4671 O OD1 . ASN B 2 8 ? 56.544 -22.775 21.061 1.00 66.56 ? 100 ASN C OD1 1 ATOM 4672 N ND2 . ASN B 2 8 ? 55.139 -22.128 22.664 1.00 67.77 ? 100 ASN C ND2 1 ATOM 4673 N N . PRO B 2 9 ? 58.390 -21.819 19.140 1.00 68.80 ? 101 PRO C N 1 ATOM 4674 C CA . PRO B 2 9 ? 58.285 -22.281 17.746 1.00 68.87 ? 101 PRO C CA 1 ATOM 4675 C C . PRO B 2 9 ? 56.977 -22.898 17.271 1.00 69.46 ? 101 PRO C C 1 ATOM 4676 O O . PRO B 2 9 ? 56.655 -22.698 16.099 1.00 69.60 ? 101 PRO C O 1 ATOM 4677 C CB . PRO B 2 9 ? 59.391 -23.330 17.653 1.00 68.30 ? 101 PRO C CB 1 ATOM 4678 C CG . PRO B 2 9 ? 59.608 -23.771 19.043 1.00 68.02 ? 101 PRO C CG 1 ATOM 4679 C CD . PRO B 2 9 ? 59.438 -22.552 19.867 1.00 68.19 ? 101 PRO C CD 1 ATOM 4680 N N . ILE B 2 10 ? 56.233 -23.569 18.147 1.00 66.41 ? 102 ILE C N 1 ATOM 4681 C CA . ILE B 2 10 ? 55.204 -24.487 17.677 1.00 66.96 ? 102 ILE C CA 1 ATOM 4682 C C . ILE B 2 10 ? 54.299 -23.818 16.681 1.00 67.62 ? 102 ILE C C 1 ATOM 4683 O O . ILE B 2 10 ? 54.026 -22.586 16.749 1.00 67.93 ? 102 ILE C O 1 ATOM 4684 C CB . ILE B 2 10 ? 54.366 -25.163 18.798 1.00 67.61 ? 102 ILE C CB 1 ATOM 4685 C CG1 . ILE B 2 10 ? 53.043 -24.448 19.087 1.00 68.64 ? 102 ILE C CG1 1 ATOM 4686 C CG2 . ILE B 2 10 ? 55.197 -25.365 20.063 1.00 67.21 ? 102 ILE C CG2 1 ATOM 4687 C CD1 . ILE B 2 10 ? 52.137 -25.247 20.009 1.00 69.44 ? 102 ILE C CD1 1 ATOM 4688 N N . SER B 2 11 ? 53.912 -24.631 15.703 1.00 67.80 ? 103 SER C N 1 ATOM 4689 C CA . SER B 2 11 ? 53.254 -24.109 14.537 1.00 68.23 ? 103 SER C CA 1 ATOM 4690 C C . SER B 2 11 ? 52.174 -25.007 13.972 1.00 68.94 ? 103 SER C C 1 ATOM 4691 O O . SER B 2 11 ? 51.928 -26.120 14.438 1.00 69.05 ? 103 SER C O 1 ATOM 4692 C CB . SER B 2 11 ? 54.314 -23.861 13.477 1.00 67.40 ? 103 SER C CB 1 ATOM 4693 O OG . SER B 2 11 ? 55.448 -24.680 13.735 1.00 66.46 ? 103 SER C OG 1 ATOM 4694 N N . ASN B 2 12 ? 51.528 -24.480 12.945 1.00 76.68 ? 104 ASN C N 1 ATOM 4695 C CA . ASN B 2 12 ? 50.525 -25.210 12.205 1.00 77.32 ? 104 ASN C CA 1 ATOM 4696 C C . ASN B 2 12 ? 50.974 -25.384 10.758 1.00 76.68 ? 104 ASN C C 1 ATOM 4697 O O . ASN B 2 12 ? 52.136 -25.126 10.412 1.00 75.85 ? 104 ASN C O 1 ATOM 4698 C CB . ASN B 2 12 ? 49.167 -24.501 12.288 1.00 78.56 ? 104 ASN C CB 1 ATOM 4699 C CG . ASN B 2 12 ? 48.467 -24.741 13.610 1.00 79.13 ? 104 ASN C CG 1 ATOM 4700 O OD1 . ASN B 2 12 ? 48.694 -25.760 14.259 1.00 78.85 ? 104 ASN C OD1 1 ATOM 4701 N ND2 . ASN B 2 12 ? 47.610 -23.811 14.012 1.00 79.96 ? 104 ASN C ND2 1 ATOM 4702 O OXT . ASN B 2 12 ? 50.187 -25.805 9.907 1.00 77.01 ? 104 ASN C OXT 1 ATOM 4703 N N . ASN C 3 1 ? 51.305 -34.900 19.208 1.00 63.24 ? 27 ASN K N 1 ATOM 4704 C CA . ASN C 3 1 ? 52.648 -34.365 19.035 1.00 62.18 ? 27 ASN K CA 1 ATOM 4705 C C . ASN C 3 1 ? 53.650 -34.961 20.009 1.00 61.35 ? 27 ASN K C 1 ATOM 4706 O O . ASN C 3 1 ? 54.767 -34.479 20.125 1.00 60.48 ? 27 ASN K O 1 ATOM 4707 C CB . ASN C 3 1 ? 52.660 -32.842 19.144 1.00 62.61 ? 27 ASN K CB 1 ATOM 4708 N N . MET C 3 2 ? 53.228 -35.967 20.759 1.00 99.18 ? 28 MET K N 1 ATOM 4709 C CA . MET C 3 2 ? 54.176 -36.818 21.453 1.00 98.48 ? 28 MET K CA 1 ATOM 4710 C C . MET C 3 2 ? 54.633 -37.801 20.403 1.00 97.81 ? 28 MET K C 1 ATOM 4711 O O . MET C 3 2 ? 55.825 -38.033 20.178 1.00 96.77 ? 28 MET K O 1 ATOM 4712 C CB . MET C 3 2 ? 53.475 -37.544 22.602 1.00 99.46 ? 28 MET K CB 1 ATOM 4713 C CG . MET C 3 2 ? 54.401 -38.213 23.611 1.00 99.01 ? 28 MET K CG 1 ATOM 4714 S SD . MET C 3 2 ? 54.689 -39.956 23.249 1.00 98.83 ? 28 MET K SD 1 ATOM 4715 C CE . MET C 3 2 ? 53.070 -40.646 23.588 1.00 100.36 ? 28 MET K CE 1 ATOM 4716 N N . GLU C 3 3 ? 53.637 -38.342 19.722 1.00 85.01 ? 29 GLU K N 1 ATOM 4717 C CA . GLU C 3 3 ? 53.844 -39.304 18.665 1.00 84.48 ? 29 GLU K CA 1 ATOM 4718 C C . GLU C 3 3 ? 54.528 -38.611 17.517 1.00 83.55 ? 29 GLU K C 1 ATOM 4719 O O . GLU C 3 3 ? 55.113 -39.243 16.649 1.00 82.80 ? 29 GLU K O 1 ATOM 4720 C CB . GLU C 3 3 ? 52.500 -39.845 18.203 1.00 85.35 ? 29 GLU K CB 1 ATOM 4721 C CG . GLU C 3 3 ? 51.452 -38.766 18.038 1.00 87.37 ? 29 GLU K CG 1 ATOM 4722 C CD . GLU C 3 3 ? 50.114 -39.320 17.597 1.00 88.21 ? 29 GLU K CD 1 ATOM 4723 O OE1 . GLU C 3 3 ? 49.315 -38.537 17.041 1.00 88.70 ? 29 GLU K OE1 1 ATOM 4724 O OE2 . GLU C 3 3 ? 49.862 -40.530 17.802 1.00 88.36 ? 29 GLU K OE2 1 ATOM 4725 N N . GLY C 3 4 ? 54.434 -37.295 17.507 1.00 59.10 ? 30 GLY K N 1 ATOM 4726 C CA . GLY C 3 4 ? 55.151 -36.523 16.521 1.00 58.59 ? 30 GLY K CA 1 ATOM 4727 C C . GLY C 3 4 ? 56.620 -36.672 16.808 1.00 57.60 ? 30 GLY K C 1 ATOM 4728 O O . GLY C 3 4 ? 57.420 -36.957 15.924 1.00 57.07 ? 30 GLY K O 1 ATOM 4729 N N . ASP C 3 5 ? 56.971 -36.501 18.071 1.00 69.26 ? 31 ASP K N 1 ATOM 4730 C CA . ASP C 3 5 ? 58.363 -36.581 18.469 1.00 68.34 ? 31 ASP K CA 1 ATOM 4731 C C . ASP C 3 5 ? 58.878 -37.974 18.181 1.00 67.84 ? 31 ASP K C 1 ATOM 4732 O O . ASP C 3 5 ? 60.006 -38.135 17.729 1.00 66.98 ? 31 ASP K O 1 ATOM 4733 C CB . ASP C 3 5 ? 58.514 -36.218 19.942 1.00 68.58 ? 31 ASP K CB 1 ATOM 4734 C CG . ASP C 3 5 ? 57.852 -34.891 20.278 1.00 69.03 ? 31 ASP K CG 1 ATOM 4735 O OD1 . ASP C 3 5 ? 57.922 -33.962 19.436 1.00 68.77 ? 31 ASP K OD1 1 ATOM 4736 O OD2 . ASP C 3 5 ? 57.246 -34.778 21.370 1.00 69.74 ? 31 ASP K OD2 1 ATOM 4737 N N . ALA C 3 6 ? 58.027 -38.972 18.408 1.00 59.24 ? 32 ALA K N 1 ATOM 4738 C CA . ALA C 3 6 ? 58.386 -40.370 18.152 1.00 58.91 ? 32 ALA K CA 1 ATOM 4739 C C . ALA C 3 6 ? 58.643 -40.628 16.664 1.00 58.53 ? 32 ALA K C 1 ATOM 4740 O O . ALA C 3 6 ? 59.675 -41.203 16.269 1.00 57.83 ? 32 ALA K O 1 ATOM 4741 C CB . ALA C 3 6 ? 57.300 -41.300 18.681 1.00 59.77 ? 32 ALA K CB 1 ATOM 4742 N N . LEU C 3 7 ? 57.698 -40.197 15.838 1.00 66.66 ? 33 LEU K N 1 ATOM 4743 C CA . LEU C 3 7 ? 57.823 -40.371 14.406 1.00 66.35 ? 33 LEU K CA 1 ATOM 4744 C C . LEU C 3 7 ? 59.082 -39.669 13.942 1.00 65.53 ? 33 LEU K C 1 ATOM 4745 O O . LEU C 3 7 ? 59.777 -40.136 13.034 1.00 65.02 ? 33 LEU K O 1 ATOM 4746 C CB . LEU C 3 7 ? 56.594 -39.831 13.685 1.00 67.10 ? 33 LEU K CB 1 ATOM 4747 C CG . LEU C 3 7 ? 55.440 -40.824 13.630 1.00 67.82 ? 33 LEU K CG 1 ATOM 4748 C CD1 . LEU C 3 7 ? 54.218 -40.186 13.004 1.00 68.69 ? 33 LEU K CD1 1 ATOM 4749 C CD2 . LEU C 3 7 ? 55.859 -42.073 12.864 1.00 67.25 ? 33 LEU K CD2 1 ATOM 4750 N N . HIS C 3 8 ? 59.398 -38.559 14.594 1.00 64.76 ? 34 HIS K N 1 ATOM 4751 C CA . HIS C 3 8 ? 60.595 -37.846 14.237 1.00 64.12 ? 34 HIS K CA 1 ATOM 4752 C C . HIS C 3 8 ? 61.844 -38.571 14.697 1.00 63.40 ? 34 HIS K C 1 ATOM 4753 O O . HIS C 3 8 ? 62.896 -38.423 14.097 1.00 62.89 ? 34 HIS K O 1 ATOM 4754 C CB . HIS C 3 8 ? 60.602 -36.446 14.796 1.00 64.33 ? 34 HIS K CB 1 ATOM 4755 C CG . HIS C 3 8 ? 61.909 -35.757 14.596 1.00 63.74 ? 34 HIS K CG 1 ATOM 4756 N ND1 . HIS C 3 8 ? 62.277 -35.202 13.389 1.00 63.70 ? 34 HIS K ND1 1 ATOM 4757 C CD2 . HIS C 3 8 ? 62.966 -35.590 15.425 1.00 63.25 ? 34 HIS K CD2 1 ATOM 4758 C CE1 . HIS C 3 8 ? 63.489 -34.688 13.494 1.00 63.28 ? 34 HIS K CE1 1 ATOM 4759 N NE2 . HIS C 3 8 ? 63.930 -34.912 14.718 1.00 62.97 ? 34 HIS K NE2 1 ATOM 4760 N N . SER C 3 9 ? 61.739 -39.348 15.765 1.00 64.99 ? 35 SER K N 1 ATOM 4761 C CA . SER C 3 9 ? 62.884 -40.121 16.229 1.00 64.44 ? 35 SER K CA 1 ATOM 4762 C C . SER C 3 9 ? 63.199 -41.133 15.165 1.00 64.20 ? 35 SER K C 1 ATOM 4763 O O . SER C 3 9 ? 64.365 -41.304 14.770 1.00 63.68 ? 35 SER K O 1 ATOM 4764 C CB . SER C 3 9 ? 62.561 -40.860 17.520 1.00 64.80 ? 35 SER K CB 1 ATOM 4765 O OG . SER C 3 9 ? 61.607 -40.149 18.287 1.00 65.30 ? 35 SER K OG 1 ATOM 4766 N N . LEU C 3 10 ? 62.137 -41.801 14.710 1.00 53.68 ? 36 LEU K N 1 ATOM 4767 C CA . LEU C 3 10 ? 62.253 -42.777 13.636 1.00 53.79 ? 36 LEU K CA 1 ATOM 4768 C C . LEU C 3 10 ? 62.917 -42.128 12.442 1.00 54.02 ? 36 LEU K C 1 ATOM 4769 O O . LEU C 3 10 ? 63.884 -42.653 11.899 1.00 54.00 ? 36 LEU K O 1 ATOM 4770 C CB . LEU C 3 10 ? 60.884 -43.319 13.239 1.00 54.12 ? 36 LEU K CB 1 ATOM 4771 C CG . LEU C 3 10 ? 60.829 -44.034 11.880 1.00 54.34 ? 36 LEU K CG 1 ATOM 4772 C CD1 . LEU C 3 10 ? 61.608 -45.330 11.897 1.00 54.15 ? 36 LEU K CD1 1 ATOM 4773 C CD2 . LEU C 3 10 ? 59.391 -44.267 11.465 1.00 54.68 ? 36 LEU K CD2 1 ATOM 4774 N N . ARG C 3 11 ? 62.390 -40.970 12.059 1.00 58.09 ? 37 ARG K N 1 ATOM 4775 C CA . ARG C 3 11 ? 62.912 -40.175 10.955 1.00 57.98 ? 37 ARG K CA 1 ATOM 4776 C C . ARG C 3 11 ? 64.422 -39.948 11.078 1.00 57.41 ? 37 ARG K C 1 ATOM 4777 O O . ARG C 3 11 ? 65.182 -40.173 10.131 1.00 57.18 ? 37 ARG K O 1 ATOM 4778 C CB . ARG C 3 11 ? 62.178 -38.832 10.950 1.00 58.42 ? 37 ARG K CB 1 ATOM 4779 C CG . ARG C 3 11 ? 62.241 -38.055 9.670 1.00 58.51 ? 37 ARG K CG 1 ATOM 4780 C CD . ARG C 3 11 ? 63.604 -37.471 9.441 1.00 58.35 ? 37 ARG K CD 1 ATOM 4781 N NE . ARG C 3 11 ? 63.614 -36.681 8.233 1.00 58.58 ? 37 ARG K NE 1 ATOM 4782 C CZ . ARG C 3 11 ? 63.166 -35.436 8.188 1.00 59.00 ? 37 ARG K CZ 1 ATOM 4783 N NH1 . ARG C 3 11 ? 62.683 -34.874 9.291 1.00 59.24 ? 37 ARG K NH1 1 ATOM 4784 N NH2 . ARG C 3 11 ? 63.198 -34.759 7.049 1.00 59.19 ? 37 ARG K NH2 1 ATOM 4785 N N . ALA C 3 12 ? 64.835 -39.480 12.252 1.00 62.88 ? 38 ALA K N 1 ATOM 4786 C CA . ALA C 3 12 ? 66.217 -39.096 12.499 1.00 62.44 ? 38 ALA K CA 1 ATOM 4787 C C . ALA C 3 12 ? 67.154 -40.280 12.415 1.00 62.09 ? 38 ALA K C 1 ATOM 4788 O O . ALA C 3 12 ? 68.211 -40.188 11.795 1.00 61.91 ? 38 ALA K O 1 ATOM 4789 C CB . ALA C 3 12 ? 66.344 -38.438 13.832 1.00 62.32 ? 38 ALA K CB 1 ATOM 4790 N N . ASN C 3 13 ? 66.768 -41.393 13.031 1.00 63.98 ? 39 ASN K N 1 ATOM 4791 C CA . ASN C 3 13 ? 67.542 -42.628 12.893 1.00 63.79 ? 39 ASN K CA 1 ATOM 4792 C C . ASN C 3 13 ? 67.556 -43.151 11.453 1.00 63.95 ? 39 ASN K C 1 ATOM 4793 O O . ASN C 3 13 ? 68.343 -44.040 11.116 1.00 63.87 ? 39 ASN K O 1 ATOM 4794 C CB . ASN C 3 13 ? 66.974 -43.703 13.819 1.00 64.00 ? 39 ASN K CB 1 ATOM 4795 C CG . ASN C 3 13 ? 67.908 -44.886 14.001 1.00 63.92 ? 39 ASN K CG 1 ATOM 4796 O OD1 . ASN C 3 13 ? 68.216 -45.280 15.128 1.00 63.88 ? 39 ASN K OD1 1 ATOM 4797 N ND2 . ASN C 3 13 ? 68.357 -45.463 12.898 1.00 63.99 ? 39 ASN K ND2 1 ATOM 4798 N N . LEU C 3 14 ? 66.683 -42.600 10.614 1.00 75.03 ? 40 LEU K N 1 ATOM 4799 C CA . LEU C 3 14 ? 66.480 -43.111 9.261 1.00 75.14 ? 40 LEU K CA 1 ATOM 4800 C C . LEU C 3 14 ? 67.306 -42.413 8.199 1.00 75.07 ? 40 LEU K C 1 ATOM 4801 O O . LEU C 3 14 ? 67.571 -41.205 8.256 1.00 75.11 ? 40 LEU K O 1 ATOM 4802 C CB . LEU C 3 14 ? 65.005 -43.039 8.864 1.00 75.55 ? 40 LEU K CB 1 ATOM 4803 C CG . LEU C 3 14 ? 64.180 -44.300 9.051 1.00 75.77 ? 40 LEU K CG 1 ATOM 4804 C CD1 . LEU C 3 14 ? 62.745 -44.026 8.672 1.00 76.21 ? 40 LEU K CD1 1 ATOM 4805 C CD2 . LEU C 3 14 ? 64.774 -45.380 8.202 1.00 75.63 ? 40 LEU K CD2 1 ATOM 4806 N N . VAL C 3 15 ? 67.711 -43.210 7.225 1.00 55.73 ? 41 VAL K N 1 ATOM 4807 C CA . VAL C 3 15 ? 68.343 -42.705 6.034 1.00 56.92 ? 41 VAL K CA 1 ATOM 4808 C C . VAL C 3 15 ? 67.271 -42.487 4.966 1.00 57.43 ? 41 VAL K C 1 ATOM 4809 O O . VAL C 3 15 ? 66.620 -43.428 4.546 1.00 57.41 ? 41 VAL K O 1 ATOM 4810 C CB . VAL C 3 15 ? 69.347 -43.723 5.537 1.00 57.61 ? 41 VAL K CB 1 ATOM 4811 C CG1 . VAL C 3 15 ? 69.824 -43.347 4.151 1.00 59.01 ? 41 VAL K CG1 1 ATOM 4812 C CG2 . VAL C 3 15 ? 70.490 -43.843 6.525 1.00 57.30 ? 41 VAL K CG2 1 ATOM 4813 N N . ASP C 3 16 ? 67.074 -41.252 4.529 1.00 68.09 ? 42 ASP K N 1 ATOM 4814 C CA . ASP C 3 16 ? 66.012 -40.975 3.569 1.00 68.41 ? 42 ASP K CA 1 ATOM 4815 C C . ASP C 3 16 ? 66.552 -40.300 2.317 1.00 68.52 ? 42 ASP K C 1 ATOM 4816 O O . ASP C 3 16 ? 66.334 -39.109 2.113 1.00 68.81 ? 42 ASP K O 1 ATOM 4817 C CB . ASP C 3 16 ? 64.931 -40.111 4.217 1.00 68.75 ? 42 ASP K CB 1 ATOM 4818 C CG . ASP C 3 16 ? 63.800 -39.774 3.267 1.00 69.23 ? 42 ASP K CG 1 ATOM 4819 O OD1 . ASP C 3 16 ? 63.725 -40.368 2.167 1.00 69.28 ? 42 ASP K OD1 1 ATOM 4820 O OD2 . ASP C 3 16 ? 62.977 -38.911 3.632 1.00 69.56 ? 42 ASP K OD2 1 ATOM 4821 N N . PRO C 3 17 ? 67.218 -41.076 1.449 1.00 64.05 ? 43 PRO K N 1 ATOM 4822 C CA . PRO C 3 17 ? 67.961 -40.551 0.297 1.00 64.38 ? 43 PRO K CA 1 ATOM 4823 C C . PRO C 3 17 ? 67.093 -39.745 -0.653 1.00 65.01 ? 43 PRO K C 1 ATOM 4824 O O . PRO C 3 17 ? 67.619 -38.920 -1.390 1.00 65.75 ? 43 PRO K O 1 ATOM 4825 C CB . PRO C 3 17 ? 68.454 -41.816 -0.402 1.00 64.59 ? 43 PRO K CB 1 ATOM 4826 C CG . PRO C 3 17 ? 67.480 -42.850 -0.019 1.00 64.08 ? 43 PRO K CG 1 ATOM 4827 C CD . PRO C 3 17 ? 67.103 -42.542 1.398 1.00 63.84 ? 43 PRO K CD 1 ATOM 4828 N N . ASN C 3 18 ? 65.794 -40.014 -0.669 1.00 72.11 ? 44 ASN K N 1 ATOM 4829 C CA . ASN C 3 18 ? 64.866 -39.225 -1.470 1.00 72.69 ? 44 ASN K CA 1 ATOM 4830 C C . ASN C 3 18 ? 64.023 -38.156 -0.767 1.00 72.85 ? 44 ASN K C 1 ATOM 4831 O O . ASN C 3 18 ? 63.195 -37.507 -1.411 1.00 73.28 ? 44 ASN K O 1 ATOM 4832 C CB . ASN C 3 18 ? 63.993 -40.141 -2.297 1.00 72.86 ? 44 ASN K CB 1 ATOM 4833 C CG . ASN C 3 18 ? 64.775 -40.845 -3.355 1.00 73.34 ? 44 ASN K CG 1 ATOM 4834 O OD1 . ASN C 3 18 ? 65.775 -40.318 -3.844 1.00 73.87 ? 44 ASN K OD1 1 ATOM 4835 N ND2 . ASN C 3 18 ? 64.341 -42.046 -3.718 1.00 73.25 ? 44 ASN K ND2 1 ATOM 4836 N N . ASN C 3 19 ? 64.219 -37.995 0.541 1.00 75.55 ? 45 ASN K N 1 ATOM 4837 C CA . ASN C 3 19 ? 63.528 -36.963 1.327 1.00 75.88 ? 45 ASN K CA 1 ATOM 4838 C C . ASN C 3 19 ? 61.993 -37.019 1.278 1.00 76.30 ? 45 ASN K C 1 ATOM 4839 O O . ASN C 3 19 ? 61.341 -36.034 0.932 1.00 76.76 ? 45 ASN K O 1 ATOM 4840 C CB . ASN C 3 19 ? 64.026 -35.558 0.956 1.00 76.18 ? 45 ASN K CB 1 ATOM 4841 C CG . ASN C 3 19 ? 65.541 -35.497 0.763 1.00 76.00 ? 45 ASN K CG 1 ATOM 4842 O OD1 . ASN C 3 19 ? 66.303 -35.443 1.730 1.00 75.78 ? 45 ASN K OD1 1 ATOM 4843 N ND2 . ASN C 3 19 ? 65.978 -35.487 -0.498 1.00 76.33 ? 45 ASN K ND2 1 ATOM 4844 N N . VAL C 3 20 ? 61.424 -38.180 1.595 1.00 60.14 ? 46 VAL K N 1 ATOM 4845 C CA . VAL C 3 20 ? 59.973 -38.298 1.759 1.00 59.77 ? 46 VAL K CA 1 ATOM 4846 C C . VAL C 3 20 ? 59.581 -37.801 3.136 1.00 59.20 ? 46 VAL K C 1 ATOM 4847 O O . VAL C 3 20 ? 58.579 -37.093 3.316 1.00 59.55 ? 46 VAL K O 1 ATOM 4848 C CB . VAL C 3 20 ? 59.476 -39.746 1.603 1.00 59.31 ? 46 VAL K CB 1 ATOM 4849 C CG1 . VAL C 3 20 ? 59.171 -40.041 0.147 1.00 60.40 ? 46 VAL K CG1 1 ATOM 4850 C CG2 . VAL C 3 20 ? 60.471 -40.738 2.187 1.00 58.69 ? 46 VAL K CG2 1 ATOM 4851 N N . LEU C 3 21 ? 60.414 -38.175 4.100 1.00 64.29 ? 47 LEU K N 1 ATOM 4852 C CA . LEU C 3 21 ? 60.296 -37.759 5.486 1.00 64.38 ? 47 LEU K CA 1 ATOM 4853 C C . LEU C 3 21 ? 60.500 -36.250 5.612 1.00 64.69 ? 47 LEU K C 1 ATOM 4854 O O . LEU C 3 21 ? 60.255 -35.648 6.647 1.00 64.88 ? 47 LEU K O 1 ATOM 4855 C CB . LEU C 3 21 ? 61.334 -38.521 6.300 1.00 63.75 ? 47 LEU K CB 1 ATOM 4856 C CG . LEU C 3 21 ? 61.133 -40.026 6.127 1.00 63.58 ? 47 LEU K CG 1 ATOM 4857 C CD1 . LEU C 3 21 ? 62.324 -40.825 6.600 1.00 63.19 ? 47 LEU K CD1 1 ATOM 4858 C CD2 . LEU C 3 21 ? 59.889 -40.456 6.870 1.00 63.90 ? 47 LEU K CD2 1 ATOM 4859 N N . GLN C 3 22 ? 60.919 -35.645 4.516 1.00 68.43 ? 48 GLN K N 1 ATOM 4860 C CA . GLN C 3 22 ? 61.251 -34.236 4.449 1.00 68.67 ? 48 GLN K CA 1 ATOM 4861 C C . GLN C 3 22 ? 60.096 -33.337 4.893 1.00 69.39 ? 48 GLN K C 1 ATOM 4862 O O . GLN C 3 22 ? 60.296 -32.176 5.228 1.00 69.79 ? 48 GLN K O 1 ATOM 4863 C CB . GLN C 3 22 ? 61.685 -33.918 3.020 1.00 68.79 ? 48 GLN K CB 1 ATOM 4864 C CG . GLN C 3 22 ? 62.649 -32.796 2.887 1.00 68.66 ? 48 GLN K CG 1 ATOM 4865 C CD . GLN C 3 22 ? 61.955 -31.542 2.445 1.00 69.38 ? 48 GLN K CD 1 ATOM 4866 O OE1 . GLN C 3 22 ? 60.931 -31.590 1.748 1.00 69.63 ? 48 GLN K OE1 1 ATOM 4867 N NE2 . GLN C 3 22 ? 62.495 -30.400 2.854 1.00 69.76 ? 48 GLN K NE2 1 ATOM 4868 N N . SER C 3 23 ? 58.887 -33.876 4.903 1.00 70.93 ? 49 SER K N 1 ATOM 4869 C CA . SER C 3 23 ? 57.743 -33.103 5.360 1.00 71.61 ? 49 SER K CA 1 ATOM 4870 C C . SER C 3 23 ? 57.532 -33.234 6.868 1.00 71.61 ? 49 SER K C 1 ATOM 4871 O O . SER C 3 23 ? 56.663 -32.567 7.431 1.00 72.12 ? 49 SER K O 1 ATOM 4872 C CB . SER C 3 23 ? 56.476 -33.502 4.590 1.00 72.24 ? 49 SER K CB 1 ATOM 4873 O OG . SER C 3 23 ? 56.447 -34.892 4.288 1.00 72.05 ? 49 SER K OG 1 ATOM 4874 N N . TRP C 3 24 ? 58.364 -34.046 7.524 1.00 61.57 ? 50 TRP K N 1 ATOM 4875 C CA . TRP C 3 24 ? 58.126 -34.411 8.921 1.00 61.57 ? 50 TRP K CA 1 ATOM 4876 C C . TRP C 3 24 ? 58.802 -33.416 9.826 1.00 61.37 ? 50 TRP K C 1 ATOM 4877 O O . TRP C 3 24 ? 59.999 -33.521 10.086 1.00 60.77 ? 50 TRP K O 1 ATOM 4878 C CB . TRP C 3 24 ? 58.749 -35.772 9.220 1.00 60.99 ? 50 TRP K CB 1 ATOM 4879 C CG . TRP C 3 24 ? 57.992 -36.893 8.645 1.00 61.13 ? 50 TRP K CG 1 ATOM 4880 C CD1 . TRP C 3 24 ? 57.142 -36.841 7.595 1.00 61.53 ? 50 TRP K CD1 1 ATOM 4881 C CD2 . TRP C 3 24 ? 57.970 -38.244 9.115 1.00 60.90 ? 50 TRP K CD2 1 ATOM 4882 N NE1 . TRP C 3 24 ? 56.601 -38.078 7.362 1.00 61.55 ? 50 TRP K NE1 1 ATOM 4883 C CE2 . TRP C 3 24 ? 57.092 -38.957 8.286 1.00 61.19 ? 50 TRP K CE2 1 ATOM 4884 C CE3 . TRP C 3 24 ? 58.606 -38.920 10.160 1.00 60.51 ? 50 TRP K CE3 1 ATOM 4885 C CZ2 . TRP C 3 24 ? 56.835 -40.301 8.461 1.00 61.10 ? 50 TRP K CZ2 1 ATOM 4886 C CZ3 . TRP C 3 24 ? 58.345 -40.262 10.336 1.00 60.45 ? 50 TRP K CZ3 1 ATOM 4887 C CH2 . TRP C 3 24 ? 57.471 -40.937 9.491 1.00 60.76 ? 50 TRP K CH2 1 ATOM 4888 N N . ASP C 3 25 ? 57.994 -32.543 10.418 1.00 79.96 ? 51 ASP K N 1 ATOM 4889 C CA . ASP C 3 25 ? 58.464 -31.281 10.980 1.00 79.98 ? 51 ASP K CA 1 ATOM 4890 C C . ASP C 3 25 ? 58.165 -31.182 12.459 1.00 80.16 ? 51 ASP K C 1 ATOM 4891 O O . ASP C 3 25 ? 57.105 -30.674 12.833 1.00 80.99 ? 51 ASP K O 1 ATOM 4892 C CB . ASP C 3 25 ? 57.772 -30.119 10.271 1.00 80.60 ? 51 ASP K CB 1 ATOM 4893 C CG . ASP C 3 25 ? 58.113 -28.780 10.881 1.00 80.83 ? 51 ASP K CG 1 ATOM 4894 O OD1 . ASP C 3 25 ? 59.297 -28.576 11.216 1.00 80.38 ? 51 ASP K OD1 1 ATOM 4895 O OD2 . ASP C 3 25 ? 57.197 -27.943 11.031 1.00 81.46 ? 51 ASP K OD2 1 ATOM 4896 N N . PRO C 3 26 ? 59.115 -31.634 13.305 1.00 58.59 ? 52 PRO K N 1 ATOM 4897 C CA . PRO C 3 26 ? 58.918 -31.889 14.741 1.00 58.45 ? 52 PRO K CA 1 ATOM 4898 C C . PRO C 3 26 ? 58.236 -30.752 15.467 1.00 59.06 ? 52 PRO K C 1 ATOM 4899 O O . PRO C 3 26 ? 57.559 -31.030 16.454 1.00 59.34 ? 52 PRO K O 1 ATOM 4900 C CB . PRO C 3 26 ? 60.339 -32.057 15.262 1.00 57.57 ? 52 PRO K CB 1 ATOM 4901 C CG . PRO C 3 26 ? 61.079 -32.574 14.118 1.00 57.27 ? 52 PRO K CG 1 ATOM 4902 C CD . PRO C 3 26 ? 60.482 -31.984 12.880 1.00 57.90 ? 52 PRO K CD 1 ATOM 4903 N N . THR C 3 27 ? 58.381 -29.528 14.966 1.00 67.48 ? 53 THR K N 1 ATOM 4904 C CA . THR C 3 27 ? 57.801 -28.350 15.597 1.00 68.07 ? 53 THR K CA 1 ATOM 4905 C C . THR C 3 27 ? 56.341 -28.111 15.214 1.00 69.08 ? 53 THR K C 1 ATOM 4906 O O . THR C 3 27 ? 55.734 -27.102 15.598 1.00 69.66 ? 53 THR K O 1 ATOM 4907 C CB . THR C 3 27 ? 58.607 -27.099 15.253 1.00 67.81 ? 53 THR K CB 1 ATOM 4908 O OG1 . THR C 3 27 ? 57.715 -25.985 15.051 1.00 68.44 ? 53 THR K OG1 1 ATOM 4909 C CG2 . THR C 3 27 ? 59.437 -27.350 13.993 1.00 67.40 ? 53 THR K CG2 1 ATOM 4910 N N . LEU C 3 28 ? 55.784 -29.023 14.435 1.00 62.60 ? 54 LEU K N 1 ATOM 4911 C CA . LEU C 3 28 ? 54.379 -28.949 14.102 1.00 63.59 ? 54 LEU K CA 1 ATOM 4912 C C . LEU C 3 28 ? 53.501 -29.422 15.279 1.00 64.10 ? 54 LEU K C 1 ATOM 4913 O O . LEU C 3 28 ? 53.888 -30.318 16.037 1.00 63.61 ? 54 LEU K O 1 ATOM 4914 C CB . LEU C 3 28 ? 54.109 -29.792 12.869 1.00 63.63 ? 54 LEU K CB 1 ATOM 4915 C CG . LEU C 3 28 ? 53.047 -29.205 11.967 1.00 64.43 ? 54 LEU K CG 1 ATOM 4916 C CD1 . LEU C 3 28 ? 53.626 -27.981 11.305 1.00 64.34 ? 54 LEU K CD1 1 ATOM 4917 C CD2 . LEU C 3 28 ? 52.621 -30.252 10.973 1.00 64.49 ? 54 LEU K CD2 1 ATOM 4918 N N . VAL C 3 29 ? 52.302 -28.848 15.396 1.00 68.44 ? 55 VAL K N 1 ATOM 4919 C CA . VAL C 3 29 ? 51.397 -29.118 16.513 1.00 69.38 ? 55 VAL K CA 1 ATOM 4920 C C . VAL C 3 29 ? 51.025 -30.605 16.664 1.00 69.63 ? 55 VAL K C 1 ATOM 4921 O O . VAL C 3 29 ? 50.497 -31.008 17.699 1.00 70.32 ? 55 VAL K O 1 ATOM 4922 C CB . VAL C 3 29 ? 50.114 -28.265 16.403 1.00 70.64 ? 55 VAL K CB 1 ATOM 4923 N N . ASN C 3 30 ? 51.318 -31.403 15.638 1.00 71.88 ? 56 ASN K N 1 ATOM 4924 C CA . ASN C 3 30 ? 51.098 -32.846 15.633 1.00 71.90 ? 56 ASN K CA 1 ATOM 4925 C C . ASN C 3 30 ? 51.505 -33.350 14.277 1.00 71.19 ? 56 ASN K C 1 ATOM 4926 O O . ASN C 3 30 ? 51.567 -32.578 13.334 1.00 71.04 ? 56 ASN K O 1 ATOM 4927 C CB . ASN C 3 30 ? 49.628 -33.185 15.846 1.00 73.30 ? 56 ASN K CB 1 ATOM 4928 C CG . ASN C 3 30 ? 48.731 -32.570 14.790 1.00 73.91 ? 56 ASN K CG 1 ATOM 4929 O OD1 . ASN C 3 30 ? 48.757 -32.960 13.622 1.00 72.93 ? 56 ASN K OD1 1 ATOM 4930 N ND2 . ASN C 3 30 ? 47.921 -31.607 15.200 1.00 75.57 ? 56 ASN K ND2 1 ATOM 4931 N N . PRO C 3 31 ? 51.775 -34.646 14.149 1.00 70.22 ? 57 PRO K N 1 ATOM 4932 C CA . PRO C 3 31 ? 52.175 -34.997 12.793 1.00 69.56 ? 57 PRO K CA 1 ATOM 4933 C C . PRO C 3 31 ? 51.010 -35.403 11.862 1.00 70.29 ? 57 PRO K C 1 ATOM 4934 O O . PRO C 3 31 ? 51.191 -36.312 11.051 1.00 69.83 ? 57 PRO K O 1 ATOM 4935 C CB . PRO C 3 31 ? 53.072 -36.208 13.042 1.00 68.69 ? 57 PRO K CB 1 ATOM 4936 C CG . PRO C 3 31 ? 52.426 -36.890 14.200 1.00 69.38 ? 57 PRO K CG 1 ATOM 4937 C CD . PRO C 3 31 ? 51.814 -35.803 15.056 1.00 70.26 ? 57 PRO K CD 1 ATOM 4938 N N . CYS C 3 32 ? 49.882 -34.701 11.880 1.00 75.19 ? 58 CYS K N 1 ATOM 4939 C CA . CYS C 3 32 ? 48.759 -35.160 11.066 1.00 75.99 ? 58 CYS K CA 1 ATOM 4940 C C . CYS C 3 32 ? 48.758 -34.489 9.721 1.00 75.76 ? 58 CYS K C 1 ATOM 4941 O O . CYS C 3 32 ? 48.004 -34.860 8.825 1.00 76.15 ? 58 CYS K O 1 ATOM 4942 C CB . CYS C 3 32 ? 47.421 -34.940 11.772 1.00 77.35 ? 58 CYS K CB 1 ATOM 4943 S SG . CYS C 3 32 ? 47.167 -36.038 13.183 1.00 78.03 ? 58 CYS K SG 1 ATOM 4944 N N . THR C 3 33 ? 49.592 -33.470 9.600 1.00 64.74 ? 59 THR K N 1 ATOM 4945 C CA . THR C 3 33 ? 49.769 -32.790 8.334 1.00 64.57 ? 59 THR K CA 1 ATOM 4946 C C . THR C 3 33 ? 51.028 -33.315 7.668 1.00 63.50 ? 59 THR K C 1 ATOM 4947 O O . THR C 3 33 ? 51.474 -32.804 6.652 1.00 63.32 ? 59 THR K O 1 ATOM 4948 C CB . THR C 3 33 ? 49.757 -31.248 8.474 1.00 64.93 ? 59 THR K CB 1 ATOM 4949 O OG1 . THR C 3 33 ? 51.057 -30.721 8.196 1.00 64.14 ? 59 THR K OG1 1 ATOM 4950 C CG2 . THR C 3 33 ? 49.315 -30.826 9.869 1.00 65.48 ? 59 THR K CG2 1 ATOM 4951 N N . TRP C 3 34 ? 51.628 -34.324 8.274 1.00 75.64 ? 60 TRP K N 1 ATOM 4952 C CA . TRP C 3 34 ? 52.781 -34.943 7.656 1.00 74.67 ? 60 TRP K CA 1 ATOM 4953 C C . TRP C 3 34 ? 52.381 -35.815 6.470 1.00 74.70 ? 60 TRP K C 1 ATOM 4954 O O . TRP C 3 34 ? 51.244 -36.309 6.384 1.00 75.44 ? 60 TRP K O 1 ATOM 4955 C CB . TRP C 3 34 ? 53.551 -35.758 8.676 1.00 74.07 ? 60 TRP K CB 1 ATOM 4956 C CG . TRP C 3 34 ? 54.211 -34.905 9.663 1.00 73.87 ? 60 TRP K CG 1 ATOM 4957 C CD1 . TRP C 3 34 ? 54.020 -33.571 9.849 1.00 74.23 ? 60 TRP K CD1 1 ATOM 4958 C CD2 . TRP C 3 34 ? 55.195 -35.302 10.607 1.00 73.24 ? 60 TRP K CD2 1 ATOM 4959 N NE1 . TRP C 3 34 ? 54.823 -33.112 10.861 1.00 73.86 ? 60 TRP K NE1 1 ATOM 4960 C CE2 . TRP C 3 34 ? 55.554 -34.163 11.344 1.00 73.24 ? 60 TRP K CE2 1 ATOM 4961 C CE3 . TRP C 3 34 ? 55.800 -36.515 10.913 1.00 72.66 ? 60 TRP K CE3 1 ATOM 4962 C CZ2 . TRP C 3 34 ? 56.491 -34.204 12.359 1.00 72.66 ? 60 TRP K CZ2 1 ATOM 4963 C CZ3 . TRP C 3 34 ? 56.734 -36.550 11.916 1.00 72.14 ? 60 TRP K CZ3 1 ATOM 4964 C CH2 . TRP C 3 34 ? 57.075 -35.403 12.626 1.00 72.13 ? 60 TRP K CH2 1 ATOM 4965 N N . PHE C 3 35 ? 53.310 -35.979 5.534 1.00 60.66 ? 61 PHE K N 1 ATOM 4966 C CA . PHE C 3 35 ? 53.094 -36.916 4.445 1.00 60.76 ? 61 PHE K CA 1 ATOM 4967 C C . PHE C 3 35 ? 53.384 -38.298 4.952 1.00 59.93 ? 61 PHE K C 1 ATOM 4968 O O . PHE C 3 35 ? 54.100 -38.464 5.931 1.00 59.28 ? 61 PHE K O 1 ATOM 4969 C CB . PHE C 3 35 ? 53.949 -36.559 3.245 1.00 61.07 ? 61 PHE K CB 1 ATOM 4970 C CG . PHE C 3 35 ? 53.448 -35.366 2.532 1.00 62.04 ? 61 PHE K CG 1 ATOM 4971 C CD1 . PHE C 3 35 ? 52.101 -35.240 2.281 1.00 62.68 ? 61 PHE K CD1 1 ATOM 4972 C CD2 . PHE C 3 35 ? 54.291 -34.345 2.161 1.00 62.40 ? 61 PHE K CD2 1 ATOM 4973 C CE1 . PHE C 3 35 ? 51.607 -34.129 1.645 1.00 63.64 ? 61 PHE K CE1 1 ATOM 4974 C CE2 . PHE C 3 35 ? 53.795 -33.232 1.529 1.00 63.36 ? 61 PHE K CE2 1 ATOM 4975 C CZ . PHE C 3 35 ? 52.454 -33.125 1.269 1.00 63.99 ? 61 PHE K CZ 1 ATOM 4976 N N . HIS C 3 36 ? 52.764 -39.290 4.336 1.00 65.24 ? 62 HIS K N 1 ATOM 4977 C CA . HIS C 3 36 ? 52.984 -40.674 4.719 1.00 64.82 ? 62 HIS K CA 1 ATOM 4978 C C . HIS C 3 36 ? 52.485 -40.994 6.132 1.00 65.20 ? 62 HIS K C 1 ATOM 4979 O O . HIS C 3 36 ? 52.485 -42.149 6.563 1.00 65.07 ? 62 HIS K O 1 ATOM 4980 C CB . HIS C 3 36 ? 54.452 -41.024 4.540 1.00 63.89 ? 62 HIS K CB 1 ATOM 4981 C CG . HIS C 3 36 ? 55.032 -40.465 3.289 1.00 63.71 ? 62 HIS K CG 1 ATOM 4982 N ND1 . HIS C 3 36 ? 54.405 -40.591 2.071 1.00 63.89 ? 62 HIS K ND1 1 ATOM 4983 C CD2 . HIS C 3 36 ? 56.160 -39.756 3.066 1.00 63.43 ? 62 HIS K CD2 1 ATOM 4984 C CE1 . HIS C 3 36 ? 55.135 -40.000 1.142 1.00 63.72 ? 62 HIS K CE1 1 ATOM 4985 N NE2 . HIS C 3 36 ? 56.204 -39.484 1.719 1.00 63.47 ? 62 HIS K NE2 1 ATOM 4986 N N . VAL C 3 37 ? 52.054 -39.969 6.850 1.00 62.31 ? 63 VAL K N 1 ATOM 4987 C CA . VAL C 3 37 ? 51.389 -40.189 8.113 1.00 62.90 ? 63 VAL K CA 1 ATOM 4988 C C . VAL C 3 37 ? 49.926 -39.893 7.873 1.00 64.10 ? 63 VAL K C 1 ATOM 4989 O O . VAL C 3 37 ? 49.594 -39.012 7.071 1.00 64.42 ? 63 VAL K O 1 ATOM 4990 C CB . VAL C 3 37 ? 51.957 -39.283 9.206 1.00 62.70 ? 63 VAL K CB 1 ATOM 4991 C CG1 . VAL C 3 37 ? 51.160 -39.426 10.480 1.00 63.48 ? 63 VAL K CG1 1 ATOM 4992 C CG2 . VAL C 3 37 ? 53.421 -39.617 9.449 1.00 61.45 ? 63 VAL K CG2 1 ATOM 4993 N N . THR C 3 38 ? 49.056 -40.653 8.525 1.00 63.21 ? 64 THR K N 1 ATOM 4994 C CA . THR C 3 38 ? 47.631 -40.446 8.390 1.00 64.48 ? 64 THR K CA 1 ATOM 4995 C C . THR C 3 38 ? 47.060 -40.520 9.773 1.00 65.41 ? 64 THR K C 1 ATOM 4996 O O . THR C 3 38 ? 47.327 -41.475 10.491 1.00 65.34 ? 64 THR K O 1 ATOM 4997 C CB . THR C 3 38 ? 46.979 -41.545 7.526 1.00 64.69 ? 64 THR K CB 1 ATOM 4998 O OG1 . THR C 3 38 ? 47.484 -41.490 6.179 1.00 63.89 ? 64 THR K OG1 1 ATOM 4999 C CG2 . THR C 3 38 ? 45.467 -41.384 7.509 1.00 66.20 ? 64 THR K CG2 1 ATOM 5000 N N . CYS C 3 39 ? 46.282 -39.516 10.157 1.00 71.26 ? 65 CYS K N 1 ATOM 5001 C CA . CYS C 3 39 ? 45.691 -39.512 11.483 1.00 72.25 ? 65 CYS K CA 1 ATOM 5002 C C . CYS C 3 39 ? 44.201 -39.674 11.377 1.00 73.73 ? 65 CYS K C 1 ATOM 5003 O O . CYS C 3 39 ? 43.652 -39.651 10.288 1.00 73.86 ? 65 CYS K O 1 ATOM 5004 C CB . CYS C 3 39 ? 45.968 -38.194 12.186 1.00 72.29 ? 65 CYS K CB 1 ATOM 5005 S SG . CYS C 3 39 ? 47.660 -37.974 12.742 1.00 70.87 ? 65 CYS K SG 1 ATOM 5006 N N . ASN C 3 40 ? 43.545 -39.806 12.521 1.00 77.11 ? 66 ASN K N 1 ATOM 5007 C CA . ASN C 3 40 ? 42.090 -39.926 12.583 1.00 78.75 ? 66 ASN K CA 1 ATOM 5008 C C . ASN C 3 40 ? 41.431 -38.570 12.766 1.00 79.83 ? 66 ASN K C 1 ATOM 5009 O O . ASN C 3 40 ? 42.040 -37.536 12.476 1.00 79.23 ? 66 ASN K O 1 ATOM 5010 C CB . ASN C 3 40 ? 41.627 -40.928 13.649 1.00 79.61 ? 66 ASN K CB 1 ATOM 5011 C CG . ASN C 3 40 ? 42.354 -40.766 14.966 1.00 79.38 ? 66 ASN K CG 1 ATOM 5012 O OD1 . ASN C 3 40 ? 42.731 -39.665 15.355 1.00 79.40 ? 66 ASN K OD1 1 ATOM 5013 N ND2 . ASN C 3 40 ? 42.563 -41.875 15.660 1.00 79.20 ? 66 ASN K ND2 1 ATOM 5014 N N . ASN C 3 41 ? 40.162 -38.576 13.161 1.00 83.78 ? 67 ASN K N 1 ATOM 5015 C CA . ASN C 3 41 ? 39.487 -37.330 13.488 1.00 84.95 ? 67 ASN K CA 1 ATOM 5016 C C . ASN C 3 41 ? 39.777 -36.883 14.904 1.00 85.19 ? 67 ASN K C 1 ATOM 5017 O O . ASN C 3 41 ? 39.386 -35.791 15.312 1.00 85.89 ? 67 ASN K O 1 ATOM 5018 C CB . ASN C 3 41 ? 37.989 -37.430 13.243 1.00 86.85 ? 67 ASN K CB 1 ATOM 5019 C CG . ASN C 3 41 ? 37.596 -36.912 11.866 1.00 86.89 ? 67 ASN K CG 1 ATOM 5020 O OD1 . ASN C 3 41 ? 38.439 -36.806 10.957 1.00 85.42 ? 67 ASN K OD1 1 ATOM 5021 N ND2 . ASN C 3 41 ? 36.315 -36.583 11.701 1.00 88.61 ? 67 ASN K ND2 1 ATOM 5022 N N . GLU C 3 42 ? 40.469 -37.739 15.648 1.00 76.12 ? 68 GLU K N 1 ATOM 5023 C CA . GLU C 3 42 ? 40.960 -37.389 16.982 1.00 76.02 ? 68 GLU K CA 1 ATOM 5024 C C . GLU C 3 42 ? 42.401 -36.864 16.883 1.00 74.20 ? 68 GLU K C 1 ATOM 5025 O O . GLU C 3 42 ? 42.999 -36.471 17.874 1.00 73.79 ? 68 GLU K O 1 ATOM 5026 C CB . GLU C 3 42 ? 40.863 -38.592 17.941 1.00 76.39 ? 68 GLU K CB 1 ATOM 5027 N N . ASN C 3 43 ? 42.937 -36.856 15.671 1.00 73.33 ? 69 ASN K N 1 ATOM 5028 C CA . ASN C 3 43 ? 44.301 -36.413 15.398 1.00 71.64 ? 69 ASN K CA 1 ATOM 5029 C C . ASN C 3 43 ? 45.408 -37.249 16.025 1.00 70.53 ? 69 ASN K C 1 ATOM 5030 O O . ASN C 3 43 ? 46.478 -36.728 16.329 1.00 69.54 ? 69 ASN K O 1 ATOM 5031 C CB . ASN C 3 43 ? 44.493 -34.933 15.726 1.00 71.62 ? 69 ASN K CB 1 ATOM 5032 C CG . ASN C 3 43 ? 43.505 -34.043 14.995 1.00 72.58 ? 69 ASN K CG 1 ATOM 5033 O OD1 . ASN C 3 43 ? 43.630 -33.802 13.787 1.00 72.10 ? 69 ASN K OD1 1 ATOM 5034 N ND2 . ASN C 3 43 ? 42.515 -33.544 15.724 1.00 73.99 ? 69 ASN K ND2 1 ATOM 5035 N N . SER C 3 44 ? 45.159 -38.543 16.194 1.00 79.82 ? 70 SER K N 1 ATOM 5036 C CA . SER C 3 44 ? 46.224 -39.483 16.515 1.00 78.74 ? 70 SER K CA 1 ATOM 5037 C C . SER C 3 44 ? 46.570 -40.278 15.279 1.00 77.89 ? 70 SER K C 1 ATOM 5038 O O . SER C 3 44 ? 45.698 -40.553 14.467 1.00 78.46 ? 70 SER K O 1 ATOM 5039 C CB . SER C 3 44 ? 45.793 -40.474 17.570 1.00 79.58 ? 70 SER K CB 1 ATOM 5040 O OG . SER C 3 44 ? 46.553 -41.660 17.401 1.00 78.75 ? 70 SER K OG 1 ATOM 5041 N N . VAL C 3 45 ? 47.829 -40.673 15.141 1.00 66.57 ? 71 VAL K N 1 ATOM 5042 C CA . VAL C 3 45 ? 48.252 -41.403 13.952 1.00 65.69 ? 71 VAL K CA 1 ATOM 5043 C C . VAL C 3 45 ? 47.656 -42.817 13.903 1.00 66.16 ? 71 VAL K C 1 ATOM 5044 O O . VAL C 3 45 ? 47.811 -43.591 14.844 1.00 66.30 ? 71 VAL K O 1 ATOM 5045 C CB . VAL C 3 45 ? 49.776 -41.518 13.926 1.00 64.18 ? 71 VAL K CB 1 ATOM 5046 C CG1 . VAL C 3 45 ? 50.236 -42.476 12.817 1.00 63.37 ? 71 VAL K CG1 1 ATOM 5047 C CG2 . VAL C 3 45 ? 50.403 -40.135 13.810 1.00 63.65 ? 71 VAL K CG2 1 ATOM 5048 N N . ILE C 3 46 ? 46.909 -43.138 12.851 1.00 60.51 ? 72 ILE K N 1 ATOM 5049 C CA . ILE C 3 46 ? 46.520 -44.528 12.640 1.00 60.46 ? 72 ILE K CA 1 ATOM 5050 C C . ILE C 3 46 ? 47.284 -45.237 11.516 1.00 59.86 ? 72 ILE K C 1 ATOM 5051 O O . ILE C 3 46 ? 47.211 -46.456 11.385 1.00 59.71 ? 72 ILE K O 1 ATOM 5052 C CB . ILE C 3 46 ? 44.996 -44.670 12.445 1.00 61.40 ? 72 ILE K CB 1 ATOM 5053 C CG1 . ILE C 3 46 ? 44.600 -44.466 10.989 1.00 61.66 ? 72 ILE K CG1 1 ATOM 5054 C CG2 . ILE C 3 46 ? 44.260 -43.693 13.346 1.00 62.25 ? 72 ILE K CG2 1 ATOM 5055 C CD1 . ILE C 3 46 ? 44.524 -43.047 10.603 1.00 62.36 ? 72 ILE K CD1 1 ATOM 5056 N N . ARG C 3 47 ? 48.060 -44.483 10.745 1.00 75.84 ? 73 ARG K N 1 ATOM 5057 C CA . ARG C 3 47 ? 48.746 -45.044 9.584 1.00 74.84 ? 73 ARG K CA 1 ATOM 5058 C C . ARG C 3 47 ? 50.102 -44.412 9.394 1.00 73.67 ? 73 ARG K C 1 ATOM 5059 O O . ARG C 3 47 ? 50.255 -43.204 9.572 1.00 73.75 ? 73 ARG K O 1 ATOM 5060 C CB . ARG C 3 47 ? 47.981 -44.769 8.295 1.00 75.19 ? 73 ARG K CB 1 ATOM 5061 C CG . ARG C 3 47 ? 46.599 -45.315 8.205 1.00 76.27 ? 73 ARG K CG 1 ATOM 5062 C CD . ARG C 3 47 ? 46.114 -45.215 6.771 1.00 76.26 ? 73 ARG K CD 1 ATOM 5063 N NE . ARG C 3 47 ? 46.932 -46.032 5.885 1.00 74.94 ? 73 ARG K NE 1 ATOM 5064 C CZ . ARG C 3 47 ? 46.768 -47.340 5.731 1.00 74.57 ? 73 ARG K CZ 1 ATOM 5065 N NH1 . ARG C 3 47 ? 45.808 -47.963 6.398 1.00 75.38 ? 73 ARG K NH1 1 ATOM 5066 N NH2 . ARG C 3 47 ? 47.558 -48.025 4.914 1.00 73.44 ? 73 ARG K NH2 1 ATOM 5067 N N . VAL C 3 48 ? 51.085 -45.227 9.025 1.00 59.13 ? 74 VAL K N 1 ATOM 5068 C CA . VAL C 3 48 ? 52.334 -44.715 8.486 1.00 58.33 ? 74 VAL K CA 1 ATOM 5069 C C . VAL C 3 48 ? 52.686 -45.467 7.207 1.00 57.92 ? 74 VAL K C 1 ATOM 5070 O O . VAL C 3 48 ? 53.060 -46.636 7.277 1.00 57.59 ? 74 VAL K O 1 ATOM 5071 C CB . VAL C 3 48 ? 53.438 -44.961 9.480 1.00 57.68 ? 74 VAL K CB 1 ATOM 5072 C CG1 . VAL C 3 48 ? 54.757 -44.550 8.903 1.00 56.91 ? 74 VAL K CG1 1 ATOM 5073 C CG2 . VAL C 3 48 ? 53.145 -44.213 10.742 1.00 58.08 ? 74 VAL K CG2 1 ATOM 5074 N N . ASP C 3 49 ? 52.619 -44.831 6.038 1.00 88.46 ? 75 ASP K N 1 ATOM 5075 C CA . ASP C 3 49 ? 52.937 -45.596 4.830 1.00 87.99 ? 75 ASP K CA 1 ATOM 5076 C C . ASP C 3 49 ? 54.220 -45.111 4.159 1.00 87.22 ? 75 ASP K C 1 ATOM 5077 O O . ASP C 3 49 ? 54.219 -44.161 3.385 1.00 87.26 ? 75 ASP K O 1 ATOM 5078 C CB . ASP C 3 49 ? 51.783 -45.514 3.817 1.00 88.56 ? 75 ASP K CB 1 ATOM 5079 C CG . ASP C 3 49 ? 50.428 -45.879 4.420 1.00 89.52 ? 75 ASP K CG 1 ATOM 5080 O OD1 . ASP C 3 49 ? 49.795 -45.004 5.059 1.00 90.16 ? 75 ASP K OD1 1 ATOM 5081 O OD2 . ASP C 3 49 ? 49.985 -47.034 4.230 1.00 89.74 ? 75 ASP K OD2 1 ATOM 5082 N N . LEU C 3 50 ? 55.305 -45.814 4.444 1.00 57.45 ? 76 LEU K N 1 ATOM 5083 C CA . LEU C 3 50 ? 56.607 -45.604 3.823 1.00 57.41 ? 76 LEU K CA 1 ATOM 5084 C C . LEU C 3 50 ? 57.044 -46.658 2.807 1.00 57.56 ? 76 LEU K C 1 ATOM 5085 O O . LEU C 3 50 ? 58.215 -46.716 2.458 1.00 57.51 ? 76 LEU K O 1 ATOM 5086 C CB . LEU C 3 50 ? 57.680 -45.332 4.871 1.00 56.86 ? 76 LEU K CB 1 ATOM 5087 C CG . LEU C 3 50 ? 57.443 -44.024 5.627 1.00 56.87 ? 76 LEU K CG 1 ATOM 5088 C CD1 . LEU C 3 50 ? 58.129 -44.043 6.964 1.00 56.26 ? 76 LEU K CD1 1 ATOM 5089 C CD2 . LEU C 3 50 ? 57.922 -42.841 4.806 1.00 57.34 ? 76 LEU K CD2 1 ATOM 5090 N N . GLY C 3 51 ? 56.149 -47.562 2.430 1.00 68.60 ? 77 GLY K N 1 ATOM 5091 C CA . GLY C 3 51 ? 56.497 -48.624 1.501 1.00 68.41 ? 77 GLY K CA 1 ATOM 5092 C C . GLY C 3 51 ? 57.154 -48.097 0.243 1.00 68.12 ? 77 GLY K C 1 ATOM 5093 O O . GLY C 3 51 ? 56.645 -47.158 -0.358 1.00 68.39 ? 77 GLY K O 1 ATOM 5094 N N . ASN C 3 52 ? 58.290 -48.684 -0.138 1.00 61.32 ? 78 ASN K N 1 ATOM 5095 C CA . ASN C 3 52 ? 59.076 -48.255 -1.316 1.00 61.15 ? 78 ASN K CA 1 ATOM 5096 C C . ASN C 3 52 ? 59.658 -46.850 -1.300 1.00 61.05 ? 78 ASN K C 1 ATOM 5097 O O . ASN C 3 52 ? 59.628 -46.186 -2.324 1.00 61.26 ? 78 ASN K O 1 ATOM 5098 C CB . ASN C 3 52 ? 58.274 -48.397 -2.608 1.00 61.54 ? 78 ASN K CB 1 ATOM 5099 C CG . ASN C 3 52 ? 58.019 -49.816 -2.960 1.00 61.08 ? 78 ASN K CG 1 ATOM 5100 O OD1 . ASN C 3 52 ? 56.938 -50.342 -2.701 1.00 61.03 ? 78 ASN K OD1 1 ATOM 5101 N ND2 . ASN C 3 52 ? 59.020 -50.468 -3.541 1.00 61.02 ? 78 ASN K ND2 1 ATOM 5102 N N . ALA C 3 53 ? 60.177 -46.394 -0.166 1.00 72.91 ? 79 ALA K N 1 ATOM 5103 C CA . ALA C 3 53 ? 60.732 -45.049 -0.096 1.00 72.83 ? 79 ALA K CA 1 ATOM 5104 C C . ALA C 3 53 ? 62.244 -45.009 -0.255 1.00 72.39 ? 79 ALA K C 1 ATOM 5105 O O . ALA C 3 53 ? 62.857 -43.944 -0.107 1.00 72.34 ? 79 ALA K O 1 ATOM 5106 C CB . ALA C 3 53 ? 60.320 -44.371 1.174 1.00 72.97 ? 79 ALA K CB 1 ATOM 5107 N N . ASP C 3 54 ? 62.837 -46.170 -0.524 1.00 69.39 ? 80 ASP K N 1 ATOM 5108 C CA . ASP C 3 54 ? 64.287 -46.293 -0.648 1.00 69.00 ? 80 ASP K CA 1 ATOM 5109 C C . ASP C 3 54 ? 64.976 -45.960 0.674 1.00 68.71 ? 80 ASP K C 1 ATOM 5110 O O . ASP C 3 54 ? 66.139 -45.568 0.685 1.00 68.44 ? 80 ASP K O 1 ATOM 5111 C CB . ASP C 3 54 ? 64.834 -45.382 -1.761 1.00 69.10 ? 80 ASP K CB 1 ATOM 5112 C CG . ASP C 3 54 ? 65.174 -46.138 -3.047 1.00 69.69 ? 80 ASP K CG 1 ATOM 5113 O OD1 . ASP C 3 54 ? 66.188 -46.866 -3.062 1.00 69.49 ? 80 ASP K OD1 1 ATOM 5114 O OD2 . ASP C 3 54 ? 64.452 -45.981 -4.060 1.00 70.43 ? 80 ASP K OD2 1 ATOM 5115 N N . LEU C 3 55 ? 64.257 -46.121 1.785 1.00 60.36 ? 81 LEU K N 1 ATOM 5116 C CA . LEU C 3 55 ? 64.794 -45.797 3.112 1.00 59.95 ? 81 LEU K CA 1 ATOM 5117 C C . LEU C 3 55 ? 65.868 -46.799 3.505 1.00 59.75 ? 81 LEU K C 1 ATOM 5118 O O . LEU C 3 55 ? 65.738 -47.987 3.233 1.00 59.82 ? 81 LEU K O 1 ATOM 5119 C CB . LEU C 3 55 ? 63.687 -45.797 4.167 1.00 60.01 ? 81 LEU K CB 1 ATOM 5120 C CG . LEU C 3 55 ? 62.454 -44.934 3.908 1.00 60.34 ? 81 LEU K CG 1 ATOM 5121 C CD1 . LEU C 3 55 ? 61.345 -45.340 4.832 1.00 60.41 ? 81 LEU K CD1 1 ATOM 5122 C CD2 . LEU C 3 55 ? 62.747 -43.458 4.069 1.00 60.59 ? 81 LEU K CD2 1 ATOM 5123 N N . SER C 3 56 ? 66.942 -46.328 4.124 1.00 75.97 ? 82 SER K N 1 ATOM 5124 C CA . SER C 3 56 ? 67.963 -47.239 4.613 1.00 75.89 ? 82 SER K CA 1 ATOM 5125 C C . SER C 3 56 ? 68.088 -47.059 6.107 1.00 75.87 ? 82 SER K C 1 ATOM 5126 O O . SER C 3 56 ? 67.388 -46.242 6.704 1.00 75.94 ? 82 SER K O 1 ATOM 5127 C CB . SER C 3 56 ? 69.306 -46.971 3.934 1.00 75.80 ? 82 SER K CB 1 ATOM 5128 O OG . SER C 3 56 ? 70.270 -47.939 4.315 1.00 75.58 ? 82 SER K OG 1 ATOM 5129 N N . GLY C 3 57 ? 68.995 -47.799 6.722 1.00 86.15 ? 83 GLY K N 1 ATOM 5130 C CA . GLY C 3 57 ? 69.205 -47.623 8.142 1.00 86.08 ? 83 GLY K CA 1 ATOM 5131 C C . GLY C 3 57 ? 68.214 -48.419 8.953 1.00 86.37 ? 83 GLY K C 1 ATOM 5132 O O . GLY C 3 57 ? 67.868 -49.537 8.582 1.00 86.63 ? 83 GLY K O 1 ATOM 5133 N N . GLN C 3 58 ? 67.752 -47.851 10.060 1.00 77.67 ? 84 GLN K N 1 ATOM 5134 C CA . GLN C 3 58 ? 66.993 -48.626 11.027 1.00 78.01 ? 84 GLN K CA 1 ATOM 5135 C C . GLN C 3 58 ? 65.792 -47.926 11.606 1.00 78.18 ? 84 GLN K C 1 ATOM 5136 O O . GLN C 3 58 ? 65.341 -46.893 11.122 1.00 78.09 ? 84 GLN K O 1 ATOM 5137 C CB . GLN C 3 58 ? 67.875 -49.060 12.182 1.00 78.06 ? 84 GLN K CB 1 ATOM 5138 C CG . GLN C 3 58 ? 68.753 -50.209 11.859 1.00 78.58 ? 84 GLN K CG 1 ATOM 5139 C CD . GLN C 3 58 ? 70.146 -49.990 12.369 1.00 77.99 ? 84 GLN K CD 1 ATOM 5140 O OE1 . GLN C 3 58 ? 70.686 -48.882 12.276 1.00 77.43 ? 84 GLN K OE1 1 ATOM 5141 N NE2 . GLN C 3 58 ? 70.742 -51.037 12.927 1.00 78.14 ? 84 GLN K NE2 1 ATOM 5142 N N . LEU C 3 59 ? 65.273 -48.551 12.651 1.00 54.06 ? 85 LEU K N 1 ATOM 5143 C CA . LEU C 3 59 ? 64.071 -48.125 13.340 1.00 53.90 ? 85 LEU K CA 1 ATOM 5144 C C . LEU C 3 59 ? 64.418 -47.800 14.787 1.00 53.66 ? 85 LEU K C 1 ATOM 5145 O O . LEU C 3 59 ? 65.429 -48.264 15.307 1.00 53.64 ? 85 LEU K O 1 ATOM 5146 C CB . LEU C 3 59 ? 63.054 -49.270 13.326 1.00 54.16 ? 85 LEU K CB 1 ATOM 5147 C CG . LEU C 3 59 ? 62.364 -49.631 12.015 1.00 54.47 ? 85 LEU K CG 1 ATOM 5148 C CD1 . LEU C 3 59 ? 61.965 -51.069 12.033 1.00 54.89 ? 85 LEU K CD1 1 ATOM 5149 C CD2 . LEU C 3 59 ? 61.148 -48.786 11.883 1.00 54.40 ? 85 LEU K CD2 1 ATOM 5150 N N . VAL C 3 60 ? 63.574 -47.016 15.439 1.00 81.13 ? 86 VAL K N 1 ATOM 5151 C CA . VAL C 3 60 ? 63.722 -46.790 16.861 1.00 81.39 ? 86 VAL K CA 1 ATOM 5152 C C . VAL C 3 60 ? 62.507 -47.388 17.573 1.00 82.42 ? 86 VAL K C 1 ATOM 5153 O O . VAL C 3 60 ? 61.435 -47.473 16.978 1.00 82.84 ? 86 VAL K O 1 ATOM 5154 C CB . VAL C 3 60 ? 63.840 -45.296 17.152 1.00 81.05 ? 86 VAL K CB 1 ATOM 5155 C CG1 . VAL C 3 60 ? 65.102 -44.757 16.539 1.00 80.23 ? 86 VAL K CG1 1 ATOM 5156 C CG2 . VAL C 3 60 ? 62.645 -44.562 16.602 1.00 81.44 ? 86 VAL K CG2 1 ATOM 5157 N N . PRO C 3 61 ? 62.670 -47.821 18.841 1.00 70.08 ? 87 PRO K N 1 ATOM 5158 C CA . PRO C 3 61 ? 61.578 -48.411 19.624 1.00 71.36 ? 87 PRO K CA 1 ATOM 5159 C C . PRO C 3 61 ? 60.509 -47.390 19.959 1.00 71.74 ? 87 PRO K C 1 ATOM 5160 O O . PRO C 3 61 ? 59.436 -47.770 20.424 1.00 72.90 ? 87 PRO K O 1 ATOM 5161 C CB . PRO C 3 61 ? 62.268 -48.898 20.895 1.00 71.84 ? 87 PRO K CB 1 ATOM 5162 C CG . PRO C 3 61 ? 63.439 -48.024 21.033 1.00 70.69 ? 87 PRO K CG 1 ATOM 5163 C CD . PRO C 3 61 ? 63.903 -47.715 19.637 1.00 69.65 ? 87 PRO K CD 1 ATOM 5164 N N . GLN C 3 62 ? 60.803 -46.112 19.742 1.00 74.97 ? 88 GLN K N 1 ATOM 5165 C CA . GLN C 3 62 ? 59.833 -45.048 19.971 1.00 75.28 ? 88 GLN K CA 1 ATOM 5166 C C . GLN C 3 62 ? 58.510 -45.272 19.250 1.00 75.97 ? 88 GLN K C 1 ATOM 5167 O O . GLN C 3 62 ? 57.487 -44.717 19.654 1.00 76.70 ? 88 GLN K O 1 ATOM 5168 C CB . GLN C 3 62 ? 60.407 -43.709 19.541 1.00 74.29 ? 88 GLN K CB 1 ATOM 5169 C CG . GLN C 3 62 ? 60.644 -42.751 20.689 1.00 74.20 ? 88 GLN K CG 1 ATOM 5170 C CD . GLN C 3 62 ? 62.109 -42.380 20.846 1.00 73.61 ? 88 GLN K CD 1 ATOM 5171 O OE1 . GLN C 3 62 ? 63.007 -43.190 20.556 1.00 73.48 ? 88 GLN K OE1 1 ATOM 5172 N NE2 . GLN C 3 62 ? 62.362 -41.144 21.302 1.00 73.32 ? 88 GLN K NE2 1 ATOM 5173 N N . LEU C 3 63 ? 58.541 -46.086 18.189 1.00 66.13 ? 89 LEU K N 1 ATOM 5174 C CA . LEU C 3 63 ? 57.343 -46.454 17.416 1.00 66.76 ? 89 LEU K CA 1 ATOM 5175 C C . LEU C 3 63 ? 56.253 -47.081 18.276 1.00 68.13 ? 89 LEU K C 1 ATOM 5176 O O . LEU C 3 63 ? 55.086 -47.090 17.889 1.00 68.85 ? 89 LEU K O 1 ATOM 5177 C CB . LEU C 3 63 ? 57.685 -47.384 16.243 1.00 66.31 ? 89 LEU K CB 1 ATOM 5178 C CG . LEU C 3 63 ? 58.097 -46.692 14.941 1.00 65.39 ? 89 LEU K CG 1 ATOM 5179 C CD1 . LEU C 3 63 ? 58.380 -47.701 13.850 1.00 65.07 ? 89 LEU K CD1 1 ATOM 5180 C CD2 . LEU C 3 63 ? 57.033 -45.702 14.475 1.00 65.75 ? 89 LEU K CD2 1 ATOM 5181 N N . GLY C 3 64 ? 56.636 -47.601 19.439 1.00 55.57 ? 90 GLY K N 1 ATOM 5182 C CA . GLY C 3 64 ? 55.661 -48.068 20.400 1.00 56.63 ? 90 GLY K CA 1 ATOM 5183 C C . GLY C 3 64 ? 54.668 -46.986 20.803 1.00 56.97 ? 90 GLY K C 1 ATOM 5184 O O . GLY C 3 64 ? 53.472 -47.256 20.915 1.00 57.79 ? 90 GLY K O 1 ATOM 5185 N N . GLN C 3 65 ? 55.139 -45.759 20.999 1.00 75.84 ? 91 GLN K N 1 ATOM 5186 C CA . GLN C 3 65 ? 54.288 -44.730 21.591 1.00 76.41 ? 91 GLN K CA 1 ATOM 5187 C C . GLN C 3 65 ? 53.091 -44.313 20.774 1.00 76.87 ? 91 GLN K C 1 ATOM 5188 O O . GLN C 3 65 ? 52.268 -43.542 21.261 1.00 77.59 ? 91 GLN K O 1 ATOM 5189 C CB . GLN C 3 65 ? 55.069 -43.488 21.951 1.00 75.62 ? 91 GLN K CB 1 ATOM 5190 C CG . GLN C 3 65 ? 55.939 -43.662 23.125 1.00 75.32 ? 91 GLN K CG 1 ATOM 5191 C CD . GLN C 3 65 ? 57.240 -42.996 22.888 1.00 74.24 ? 91 GLN K CD 1 ATOM 5192 O OE1 . GLN C 3 65 ? 58.237 -43.655 22.612 1.00 73.37 ? 91 GLN K OE1 1 ATOM 5193 N NE2 . GLN C 3 65 ? 57.244 -41.668 22.945 1.00 74.36 ? 91 GLN K NE2 1 ATOM 5194 N N . LEU C 3 66 ? 52.964 -44.818 19.553 1.00 61.36 ? 92 LEU K N 1 ATOM 5195 C CA . LEU C 3 66 ? 51.784 -44.464 18.791 1.00 61.96 ? 92 LEU K CA 1 ATOM 5196 C C . LEU C 3 66 ? 50.752 -45.468 19.258 1.00 63.19 ? 92 LEU K C 1 ATOM 5197 O O . LEU C 3 66 ? 50.782 -46.632 18.861 1.00 63.15 ? 92 LEU K O 1 ATOM 5198 C CB . LEU C 3 66 ? 52.041 -44.654 17.300 1.00 61.15 ? 92 LEU K CB 1 ATOM 5199 C CG . LEU C 3 66 ? 53.094 -43.741 16.692 1.00 59.92 ? 92 LEU K CG 1 ATOM 5200 C CD1 . LEU C 3 66 ? 54.057 -44.533 15.875 1.00 59.17 ? 92 LEU K CD1 1 ATOM 5201 C CD2 . LEU C 3 66 ? 52.425 -42.724 15.828 1.00 60.08 ? 92 LEU K CD2 1 ATOM 5202 N N . LYS C 3 67 ? 49.817 -45.005 20.084 1.00 58.69 ? 93 LYS K N 1 ATOM 5203 C CA . LYS C 3 67 ? 48.935 -45.919 20.780 1.00 59.31 ? 93 LYS K CA 1 ATOM 5204 C C . LYS C 3 67 ? 47.811 -46.368 19.842 1.00 59.84 ? 93 LYS K C 1 ATOM 5205 O O . LYS C 3 67 ? 47.328 -47.507 19.929 1.00 60.12 ? 93 LYS K O 1 ATOM 5206 C CB . LYS C 3 67 ? 48.408 -45.290 22.073 1.00 59.94 ? 93 LYS K CB 1 ATOM 5207 N N . ASN C 3 68 ? 47.415 -45.486 18.926 1.00 65.09 ? 94 ASN K N 1 ATOM 5208 C CA . ASN C 3 68 ? 46.327 -45.803 18.001 1.00 65.81 ? 94 ASN K CA 1 ATOM 5209 C C . ASN C 3 68 ? 46.718 -46.291 16.596 1.00 65.01 ? 94 ASN K C 1 ATOM 5210 O O . ASN C 3 68 ? 45.851 -46.510 15.736 1.00 65.59 ? 94 ASN K O 1 ATOM 5211 C CB . ASN C 3 68 ? 45.355 -44.643 17.942 1.00 66.78 ? 94 ASN K CB 1 ATOM 5212 C CG . ASN C 3 68 ? 44.743 -44.355 19.284 1.00 68.02 ? 94 ASN K CG 1 ATOM 5213 O OD1 . ASN C 3 68 ? 43.843 -45.060 19.730 1.00 69.02 ? 94 ASN K OD1 1 ATOM 5214 N ND2 . ASN C 3 68 ? 45.240 -43.329 19.951 1.00 68.09 ? 94 ASN K ND2 1 ATOM 5215 N N . LEU C 3 69 ? 48.024 -46.455 16.384 1.00 63.03 ? 95 LEU K N 1 ATOM 5216 C CA . LEU C 3 69 ? 48.565 -46.914 15.114 1.00 62.32 ? 95 LEU K CA 1 ATOM 5217 C C . LEU C 3 69 ? 47.943 -48.222 14.695 1.00 62.73 ? 95 LEU K C 1 ATOM 5218 O O . LEU C 3 69 ? 47.983 -49.204 15.427 1.00 62.95 ? 95 LEU K O 1 ATOM 5219 C CB . LEU C 3 69 ? 50.061 -47.124 15.231 1.00 61.22 ? 95 LEU K CB 1 ATOM 5220 C CG . LEU C 3 69 ? 50.663 -47.455 13.880 1.00 60.48 ? 95 LEU K CG 1 ATOM 5221 C CD1 . LEU C 3 69 ? 50.433 -46.288 12.942 1.00 60.40 ? 95 LEU K CD1 1 ATOM 5222 C CD2 . LEU C 3 69 ? 52.124 -47.735 14.025 1.00 59.55 ? 95 LEU K CD2 1 ATOM 5223 N N . GLN C 3 70 ? 47.390 -48.239 13.493 1.00 63.42 ? 96 GLN K N 1 ATOM 5224 C CA . GLN C 3 70 ? 46.688 -49.404 12.994 1.00 63.82 ? 96 GLN K CA 1 ATOM 5225 C C . GLN C 3 70 ? 47.502 -50.070 11.910 1.00 62.85 ? 96 GLN K C 1 ATOM 5226 O O . GLN C 3 70 ? 47.863 -51.228 12.027 1.00 62.76 ? 96 GLN K O 1 ATOM 5227 C CB . GLN C 3 70 ? 45.342 -48.991 12.435 1.00 64.72 ? 96 GLN K CB 1 ATOM 5228 C CG . GLN C 3 70 ? 44.308 -48.652 13.478 1.00 66.11 ? 96 GLN K CG 1 ATOM 5229 C CD . GLN C 3 70 ? 43.017 -48.178 12.836 1.00 67.06 ? 96 GLN K CD 1 ATOM 5230 O OE1 . GLN C 3 70 ? 42.966 -47.954 11.626 1.00 66.54 ? 96 GLN K OE1 1 ATOM 5231 N NE2 . GLN C 3 70 ? 41.969 -48.025 13.638 1.00 68.52 ? 96 GLN K NE2 1 ATOM 5232 N N . TYR C 3 71 ? 47.755 -49.338 10.833 1.00 69.64 ? 97 TYR K N 1 ATOM 5233 C CA . TYR C 3 71 ? 48.525 -49.871 9.721 1.00 68.56 ? 97 TYR K CA 1 ATOM 5234 C C . TYR C 3 71 ? 49.907 -49.260 9.695 1.00 67.41 ? 97 TYR K C 1 ATOM 5235 O O . TYR C 3 71 ? 50.064 -48.048 9.576 1.00 67.04 ? 97 TYR K O 1 ATOM 5236 C CB . TYR C 3 71 ? 47.814 -49.631 8.383 1.00 68.52 ? 97 TYR K CB 1 ATOM 5237 C CG . TYR C 3 71 ? 46.438 -50.244 8.322 1.00 69.55 ? 97 TYR K CG 1 ATOM 5238 C CD1 . TYR C 3 71 ? 45.366 -49.632 8.957 1.00 70.74 ? 97 TYR K CD1 1 ATOM 5239 C CD2 . TYR C 3 71 ? 46.208 -51.436 7.646 1.00 69.43 ? 97 TYR K CD2 1 ATOM 5240 C CE1 . TYR C 3 71 ? 44.108 -50.180 8.930 1.00 71.79 ? 97 TYR K CE1 1 ATOM 5241 C CE2 . TYR C 3 71 ? 44.942 -52.001 7.609 1.00 70.39 ? 97 TYR K CE2 1 ATOM 5242 C CZ . TYR C 3 71 ? 43.895 -51.363 8.259 1.00 71.59 ? 97 TYR K CZ 1 ATOM 5243 O OH . TYR C 3 71 ? 42.624 -51.884 8.257 1.00 72.64 ? 97 TYR K OH 1 ATOM 5244 N N . LEU C 3 72 ? 50.906 -50.119 9.832 1.00 57.59 ? 98 LEU K N 1 ATOM 5245 C CA . LEU C 3 72 ? 52.297 -49.726 9.717 1.00 57.02 ? 98 LEU K CA 1 ATOM 5246 C C . LEU C 3 72 ? 52.900 -50.411 8.500 1.00 56.92 ? 98 LEU K C 1 ATOM 5247 O O . LEU C 3 72 ? 53.188 -51.610 8.525 1.00 56.87 ? 98 LEU K O 1 ATOM 5248 C CB . LEU C 3 72 ? 53.054 -50.173 10.963 1.00 56.69 ? 98 LEU K CB 1 ATOM 5249 C CG . LEU C 3 72 ? 54.535 -49.848 11.017 1.00 56.13 ? 98 LEU K CG 1 ATOM 5250 C CD1 . LEU C 3 72 ? 54.746 -48.488 11.631 1.00 55.90 ? 98 LEU K CD1 1 ATOM 5251 C CD2 . LEU C 3 72 ? 55.241 -50.887 11.803 1.00 55.97 ? 98 LEU K CD2 1 ATOM 5252 N N . GLU C 3 73 ? 53.132 -49.652 7.436 1.00 65.47 ? 99 GLU K N 1 ATOM 5253 C CA . GLU C 3 73 ? 53.654 -50.256 6.227 1.00 64.84 ? 99 GLU K CA 1 ATOM 5254 C C . GLU C 3 73 ? 55.047 -49.751 5.969 1.00 63.99 ? 99 GLU K C 1 ATOM 5255 O O . GLU C 3 73 ? 55.227 -48.625 5.538 1.00 63.81 ? 99 GLU K O 1 ATOM 5256 C CB . GLU C 3 73 ? 52.768 -49.865 5.060 1.00 65.08 ? 99 GLU K CB 1 ATOM 5257 C CG . GLU C 3 73 ? 51.313 -50.102 5.328 1.00 66.10 ? 99 GLU K CG 1 ATOM 5258 C CD . GLU C 3 73 ? 51.045 -51.548 5.650 1.00 66.42 ? 99 GLU K CD 1 ATOM 5259 O OE1 . GLU C 3 73 ? 51.534 -52.413 4.902 1.00 65.97 ? 99 GLU K OE1 1 ATOM 5260 O OE2 . GLU C 3 73 ? 50.356 -51.830 6.651 1.00 67.20 ? 99 GLU K OE2 1 ATOM 5261 N N . LEU C 3 74 ? 56.031 -50.584 6.268 1.00 61.47 ? 100 LEU K N 1 ATOM 5262 C CA . LEU C 3 74 ? 57.417 -50.319 5.916 1.00 60.78 ? 100 LEU K CA 1 ATOM 5263 C C . LEU C 3 74 ? 58.023 -51.134 4.761 1.00 60.51 ? 100 LEU K C 1 ATOM 5264 O O . LEU C 3 74 ? 59.235 -51.081 4.540 1.00 60.02 ? 100 LEU K O 1 ATOM 5265 C CB . LEU C 3 74 ? 58.308 -50.328 7.146 1.00 60.54 ? 100 LEU K CB 1 ATOM 5266 C CG . LEU C 3 74 ? 58.018 -49.253 8.190 1.00 60.74 ? 100 LEU K CG 1 ATOM 5267 C CD1 . LEU C 3 74 ? 59.247 -49.090 8.998 1.00 60.72 ? 100 LEU K CD1 1 ATOM 5268 C CD2 . LEU C 3 74 ? 57.638 -47.930 7.607 1.00 60.59 ? 100 LEU K CD2 1 ATOM 5269 N N . TYR C 3 75 ? 57.206 -51.923 4.067 1.00 59.30 ? 101 TYR K N 1 ATOM 5270 C CA . TYR C 3 75 ? 57.712 -52.917 3.111 1.00 59.23 ? 101 TYR K CA 1 ATOM 5271 C C . TYR C 3 75 ? 58.496 -52.384 1.913 1.00 59.16 ? 101 TYR K C 1 ATOM 5272 O O . TYR C 3 75 ? 58.359 -51.220 1.510 1.00 59.21 ? 101 TYR K O 1 ATOM 5273 C CB . TYR C 3 75 ? 56.579 -53.797 2.593 1.00 59.69 ? 101 TYR K CB 1 ATOM 5274 C CG . TYR C 3 75 ? 55.520 -53.040 1.835 1.00 59.96 ? 101 TYR K CG 1 ATOM 5275 C CD1 . TYR C 3 75 ? 54.585 -52.290 2.505 1.00 60.30 ? 101 TYR K CD1 1 ATOM 5276 C CD2 . TYR C 3 75 ? 55.447 -53.086 0.448 1.00 60.05 ? 101 TYR K CD2 1 ATOM 5277 C CE1 . TYR C 3 75 ? 53.611 -51.599 1.836 1.00 60.64 ? 101 TYR K CE1 1 ATOM 5278 C CE2 . TYR C 3 75 ? 54.463 -52.391 -0.244 1.00 60.38 ? 101 TYR K CE2 1 ATOM 5279 C CZ . TYR C 3 75 ? 53.544 -51.647 0.468 1.00 60.62 ? 101 TYR K CZ 1 ATOM 5280 O OH . TYR C 3 75 ? 52.540 -50.936 -0.154 1.00 61.03 ? 101 TYR K OH 1 ATOM 5281 N N . SER C 3 76 ? 59.322 -53.267 1.351 1.00 59.33 ? 102 SER K N 1 ATOM 5282 C CA . SER C 3 76 ? 60.125 -52.961 0.169 1.00 59.07 ? 102 SER K CA 1 ATOM 5283 C C . SER C 3 76 ? 61.006 -51.753 0.420 1.00 58.82 ? 102 SER K C 1 ATOM 5284 O O . SER C 3 76 ? 60.760 -50.678 -0.111 1.00 58.88 ? 102 SER K O 1 ATOM 5285 C CB . SER C 3 76 ? 59.250 -52.741 -1.069 1.00 59.21 ? 102 SER K CB 1 ATOM 5286 O OG . SER C 3 76 ? 59.618 -53.621 -2.120 1.00 59.79 ? 102 SER K OG 1 ATOM 5287 N N . ASN C 3 77 ? 62.010 -51.948 1.268 1.00 61.37 ? 103 ASN K N 1 ATOM 5288 C CA . ASN C 3 77 ? 62.985 -50.920 1.599 1.00 61.03 ? 103 ASN K CA 1 ATOM 5289 C C . ASN C 3 77 ? 64.319 -51.570 1.978 1.00 60.89 ? 103 ASN K C 1 ATOM 5290 O O . ASN C 3 77 ? 64.427 -52.792 2.010 1.00 61.12 ? 103 ASN K O 1 ATOM 5291 C CB . ASN C 3 77 ? 62.466 -50.031 2.736 1.00 61.01 ? 103 ASN K CB 1 ATOM 5292 C CG . ASN C 3 77 ? 61.458 -48.994 2.258 1.00 61.26 ? 103 ASN K CG 1 ATOM 5293 O OD1 . ASN C 3 77 ? 61.825 -47.875 1.875 1.00 61.07 ? 103 ASN K OD1 1 ATOM 5294 N ND2 . ASN C 3 77 ? 60.181 -49.363 2.274 1.00 61.75 ? 103 ASN K ND2 1 ATOM 5295 N N . ASN C 3 78 ? 65.338 -50.761 2.242 1.00 88.66 ? 104 ASN K N 1 ATOM 5296 C CA . ASN C 3 78 ? 66.642 -51.291 2.623 1.00 88.57 ? 104 ASN K CA 1 ATOM 5297 C C . ASN C 3 78 ? 66.831 -51.319 4.123 1.00 88.57 ? 104 ASN K C 1 ATOM 5298 O O . ASN C 3 78 ? 67.943 -51.539 4.610 1.00 88.52 ? 104 ASN K O 1 ATOM 5299 C CB . ASN C 3 78 ? 67.793 -50.555 1.942 1.00 88.35 ? 104 ASN K CB 1 ATOM 5300 C CG . ASN C 3 78 ? 69.008 -51.453 1.733 1.00 88.49 ? 104 ASN K CG 1 ATOM 5301 O OD1 . ASN C 3 78 ? 68.958 -52.661 2.005 1.00 88.55 ? 104 ASN K OD1 1 ATOM 5302 N ND2 . ASN C 3 78 ? 70.104 -50.869 1.236 1.00 88.71 ? 104 ASN K ND2 1 ATOM 5303 N N . ILE C 3 79 ? 65.747 -51.033 4.844 1.00 62.66 ? 105 ILE K N 1 ATOM 5304 C CA . ILE C 3 79 ? 65.764 -51.030 6.308 1.00 62.71 ? 105 ILE K CA 1 ATOM 5305 C C . ILE C 3 79 ? 66.365 -52.329 6.846 1.00 62.95 ? 105 ILE K C 1 ATOM 5306 O O . ILE C 3 79 ? 66.003 -53.441 6.452 1.00 63.32 ? 105 ILE K O 1 ATOM 5307 C CB . ILE C 3 79 ? 64.355 -50.807 6.919 1.00 62.99 ? 105 ILE K CB 1 ATOM 5308 C CG1 . ILE C 3 79 ? 63.800 -49.455 6.496 1.00 62.82 ? 105 ILE K CG1 1 ATOM 5309 C CG2 . ILE C 3 79 ? 64.396 -50.913 8.435 1.00 63.11 ? 105 ILE K CG2 1 ATOM 5310 C CD1 . ILE C 3 79 ? 62.521 -49.090 7.172 1.00 63.16 ? 105 ILE K CD1 1 ATOM 5311 N N . THR C 3 80 ? 67.318 -52.173 7.738 1.00 66.42 ? 106 THR K N 1 ATOM 5312 C CA . THR C 3 80 ? 67.957 -53.314 8.326 1.00 66.76 ? 106 THR K CA 1 ATOM 5313 C C . THR C 3 80 ? 67.846 -53.149 9.823 1.00 66.87 ? 106 THR K C 1 ATOM 5314 O O . THR C 3 80 ? 67.077 -52.316 10.321 1.00 66.69 ? 106 THR K O 1 ATOM 5315 C CB . THR C 3 80 ? 69.419 -53.430 7.906 1.00 66.61 ? 106 THR K CB 1 ATOM 5316 O OG1 . THR C 3 80 ? 70.035 -54.493 8.646 1.00 67.00 ? 106 THR K OG1 1 ATOM 5317 C CG2 . THR C 3 80 ? 70.158 -52.120 8.168 1.00 66.18 ? 106 THR K CG2 1 ATOM 5318 N N . GLY C 3 81 ? 68.573 -53.982 10.545 1.00 56.18 ? 107 GLY K N 1 ATOM 5319 C CA . GLY C 3 81 ? 68.568 -53.873 11.979 1.00 55.88 ? 107 GLY K CA 1 ATOM 5320 C C . GLY C 3 81 ? 67.658 -54.909 12.565 1.00 56.05 ? 107 GLY K C 1 ATOM 5321 O O . GLY C 3 81 ? 67.360 -55.917 11.935 1.00 56.48 ? 107 GLY K O 1 ATOM 5322 N N . PRO C 3 82 ? 67.304 -54.719 13.823 1.00 61.89 ? 108 PRO K N 1 ATOM 5323 C CA . PRO C 3 82 ? 66.343 -55.612 14.455 1.00 62.71 ? 108 PRO K CA 1 ATOM 5324 C C . PRO C 3 82 ? 64.908 -55.099 14.432 1.00 62.86 ? 108 PRO K C 1 ATOM 5325 O O . PRO C 3 82 ? 64.643 -53.972 13.998 1.00 62.26 ? 108 PRO K O 1 ATOM 5326 C CB . PRO C 3 82 ? 66.861 -55.698 15.888 1.00 63.17 ? 108 PRO K CB 1 ATOM 5327 C CG . PRO C 3 82 ? 67.552 -54.407 16.109 1.00 62.37 ? 108 PRO K CG 1 ATOM 5328 C CD . PRO C 3 82 ? 68.092 -53.950 14.795 1.00 61.62 ? 108 PRO K CD 1 ATOM 5329 N N . VAL C 3 83 ? 64.012 -55.939 14.950 1.00 61.22 ? 109 VAL K N 1 ATOM 5330 C CA . VAL C 3 83 ? 62.597 -55.641 15.105 1.00 61.69 ? 109 VAL K CA 1 ATOM 5331 C C . VAL C 3 83 ? 62.284 -55.393 16.582 1.00 62.51 ? 109 VAL K C 1 ATOM 5332 O O . VAL C 3 83 ? 62.377 -56.311 17.411 1.00 63.41 ? 109 VAL K O 1 ATOM 5333 C CB . VAL C 3 83 ? 61.737 -56.828 14.650 1.00 62.29 ? 109 VAL K CB 1 ATOM 5334 C CG1 . VAL C 3 83 ? 60.575 -56.336 13.822 1.00 61.52 ? 109 VAL K CG1 1 ATOM 5335 C CG2 . VAL C 3 83 ? 62.587 -57.852 13.893 1.00 62.50 ? 109 VAL K CG2 1 ATOM 5336 N N . PRO C 3 84 ? 61.919 -54.147 16.922 1.00 55.78 ? 110 PRO K N 1 ATOM 5337 C CA . PRO C 3 84 ? 61.691 -53.719 18.314 1.00 55.93 ? 110 PRO K CA 1 ATOM 5338 C C . PRO C 3 84 ? 60.557 -54.410 19.080 1.00 56.60 ? 110 PRO K C 1 ATOM 5339 O O . PRO C 3 84 ? 59.412 -54.279 18.690 1.00 56.72 ? 110 PRO K O 1 ATOM 5340 C CB . PRO C 3 84 ? 61.340 -52.237 18.147 1.00 55.46 ? 110 PRO K CB 1 ATOM 5341 C CG . PRO C 3 84 ? 62.098 -51.829 16.948 1.00 55.03 ? 110 PRO K CG 1 ATOM 5342 C CD . PRO C 3 84 ? 62.005 -52.999 16.006 1.00 55.29 ? 110 PRO K CD 1 ATOM 5343 N N . SER C 3 85 ? 60.859 -55.005 20.229 1.00 72.86 ? 111 SER K N 1 ATOM 5344 C CA . SER C 3 85 ? 59.832 -55.660 21.027 1.00 74.66 ? 111 SER K CA 1 ATOM 5345 C C . SER C 3 85 ? 58.751 -54.675 21.452 1.00 75.24 ? 111 SER K C 1 ATOM 5346 O O . SER C 3 85 ? 57.626 -55.064 21.743 1.00 76.70 ? 111 SER K O 1 ATOM 5347 C CB . SER C 3 85 ? 60.437 -56.304 22.270 1.00 75.75 ? 111 SER K CB 1 ATOM 5348 O OG . SER C 3 85 ? 59.856 -55.745 23.440 1.00 75.94 ? 111 SER K OG 1 ATOM 5349 N N . ASP C 3 86 ? 59.089 -53.395 21.474 1.00 80.97 ? 112 ASP K N 1 ATOM 5350 C CA . ASP C 3 86 ? 58.115 -52.373 21.814 1.00 81.23 ? 112 ASP K CA 1 ATOM 5351 C C . ASP C 3 86 ? 56.984 -52.256 20.792 1.00 81.12 ? 112 ASP K C 1 ATOM 5352 O O . ASP C 3 86 ? 56.059 -51.471 20.990 1.00 81.46 ? 112 ASP K O 1 ATOM 5353 C CB . ASP C 3 86 ? 58.793 -51.022 21.992 1.00 79.82 ? 112 ASP K CB 1 ATOM 5354 C CG . ASP C 3 86 ? 59.493 -50.900 23.316 1.00 80.32 ? 112 ASP K CG 1 ATOM 5355 O OD1 . ASP C 3 86 ? 59.244 -51.758 24.196 1.00 81.58 ? 112 ASP K OD1 1 ATOM 5356 O OD2 . ASP C 3 86 ? 60.280 -49.938 23.475 1.00 79.42 ? 112 ASP K OD2 1 ATOM 5357 N N . LEU C 3 87 ? 57.078 -52.991 19.681 1.00 57.07 ? 113 LEU K N 1 ATOM 5358 C CA . LEU C 3 87 ? 55.966 -53.062 18.728 1.00 57.14 ? 113 LEU K CA 1 ATOM 5359 C C . LEU C 3 87 ? 54.814 -53.826 19.350 1.00 58.12 ? 113 LEU K C 1 ATOM 5360 O O . LEU C 3 87 ? 53.663 -53.635 18.969 1.00 58.39 ? 113 LEU K O 1 ATOM 5361 C CB . LEU C 3 87 ? 56.378 -53.698 17.403 1.00 56.83 ? 113 LEU K CB 1 ATOM 5362 C CG . LEU C 3 87 ? 56.768 -52.767 16.253 1.00 56.18 ? 113 LEU K CG 1 ATOM 5363 C CD1 . LEU C 3 87 ? 57.119 -51.394 16.758 1.00 55.75 ? 113 LEU K CD1 1 ATOM 5364 C CD2 . LEU C 3 87 ? 57.934 -53.335 15.472 1.00 55.89 ? 113 LEU K CD2 1 ATOM 5365 N N . GLY C 3 88 ? 55.129 -54.684 20.318 1.00 67.62 ? 114 GLY K N 1 ATOM 5366 C CA . GLY C 3 88 ? 54.112 -55.269 21.170 1.00 69.45 ? 114 GLY K CA 1 ATOM 5367 C C . GLY C 3 88 ? 53.338 -54.189 21.912 1.00 69.61 ? 114 GLY K C 1 ATOM 5368 O O . GLY C 3 88 ? 52.185 -54.372 22.271 1.00 70.23 ? 114 GLY K O 1 ATOM 5369 N N . ASN C 3 89 ? 53.966 -53.045 22.138 1.00 88.79 ? 115 ASN K N 1 ATOM 5370 C CA . ASN C 3 89 ? 53.282 -51.949 22.804 1.00 88.82 ? 115 ASN K CA 1 ATOM 5371 C C . ASN C 3 89 ? 52.192 -51.294 21.930 1.00 88.39 ? 115 ASN K C 1 ATOM 5372 O O . ASN C 3 89 ? 51.510 -50.376 22.381 1.00 88.53 ? 115 ASN K O 1 ATOM 5373 C CB . ASN C 3 89 ? 54.271 -50.920 23.388 1.00 88.11 ? 115 ASN K CB 1 ATOM 5374 C CG . ASN C 3 89 ? 54.864 -51.354 24.737 1.00 89.05 ? 115 ASN K CG 1 ATOM 5375 O OD1 . ASN C 3 89 ? 54.608 -52.456 25.219 1.00 90.12 ? 115 ASN K OD1 1 ATOM 5376 N ND2 . ASN C 3 89 ? 55.663 -50.477 25.344 1.00 88.71 ? 115 ASN K ND2 1 ATOM 5377 N N . LEU C 3 90 ? 52.025 -51.752 20.688 1.00 69.91 ? 116 LEU K N 1 ATOM 5378 C CA . LEU C 3 90 ? 50.977 -51.193 19.823 1.00 69.65 ? 116 LEU K CA 1 ATOM 5379 C C . LEU C 3 90 ? 49.767 -52.106 19.773 1.00 70.66 ? 116 LEU K C 1 ATOM 5380 O O . LEU C 3 90 ? 49.763 -53.094 19.039 1.00 70.71 ? 116 LEU K O 1 ATOM 5381 C CB . LEU C 3 90 ? 51.486 -51.083 18.390 1.00 68.53 ? 116 LEU K CB 1 ATOM 5382 C CG . LEU C 3 90 ? 52.803 -50.381 18.075 1.00 67.09 ? 116 LEU K CG 1 ATOM 5383 C CD1 . LEU C 3 90 ? 53.481 -51.060 16.902 1.00 66.18 ? 116 LEU K CD1 1 ATOM 5384 C CD2 . LEU C 3 90 ? 52.546 -48.926 17.759 1.00 66.64 ? 116 LEU K CD2 1 ATOM 5385 N N . THR C 3 91 ? 48.706 -51.729 20.478 1.00 85.88 ? 117 THR K N 1 ATOM 5386 C CA . THR C 3 91 ? 47.565 -52.625 20.659 1.00 86.91 ? 117 THR K CA 1 ATOM 5387 C C . THR C 3 91 ? 46.584 -52.621 19.491 1.00 86.99 ? 117 THR K C 1 ATOM 5388 O O . THR C 3 91 ? 46.145 -53.672 19.026 1.00 87.29 ? 117 THR K O 1 ATOM 5389 C CB . THR C 3 91 ? 46.816 -52.304 21.958 1.00 88.01 ? 117 THR K CB 1 ATOM 5390 O OG1 . THR C 3 91 ? 46.166 -51.035 21.833 1.00 88.40 ? 117 THR K OG1 1 ATOM 5391 C CG2 . THR C 3 91 ? 47.786 -52.253 23.120 1.00 87.80 ? 117 THR K CG2 1 ATOM 5392 N N . ASN C 3 92 ? 46.282 -51.430 18.995 1.00 67.09 ? 118 ASN K N 1 ATOM 5393 C CA . ASN C 3 92 ? 45.253 -51.256 17.991 1.00 67.47 ? 118 ASN K CA 1 ATOM 5394 C C . ASN C 3 92 ? 45.787 -51.543 16.595 1.00 66.41 ? 118 ASN K C 1 ATOM 5395 O O . ASN C 3 92 ? 45.111 -51.297 15.592 1.00 66.60 ? 118 ASN K O 1 ATOM 5396 C CB . ASN C 3 92 ? 44.682 -49.841 18.049 1.00 67.90 ? 118 ASN K CB 1 ATOM 5397 C CG . ASN C 3 92 ? 43.900 -49.571 19.319 1.00 69.27 ? 118 ASN K CG 1 ATOM 5398 O OD1 . ASN C 3 92 ? 42.735 -49.956 19.445 1.00 70.54 ? 118 ASN K OD1 1 ATOM 5399 N ND2 . ASN C 3 92 ? 44.528 -48.874 20.256 1.00 69.09 ? 118 ASN K ND2 1 ATOM 5400 N N . LEU C 3 93 ? 47.023 -52.023 16.531 1.00 60.40 ? 119 LEU K N 1 ATOM 5401 C CA . LEU C 3 93 ? 47.623 -52.327 15.249 1.00 59.83 ? 119 LEU K CA 1 ATOM 5402 C C . LEU C 3 93 ? 46.891 -53.521 14.638 1.00 60.29 ? 119 LEU K C 1 ATOM 5403 O O . LEU C 3 93 ? 46.864 -54.629 15.213 1.00 60.69 ? 119 LEU K O 1 ATOM 5404 C CB . LEU C 3 93 ? 49.103 -52.670 15.440 1.00 59.19 ? 119 LEU K CB 1 ATOM 5405 C CG . LEU C 3 93 ? 49.907 -53.080 14.208 1.00 58.45 ? 119 LEU K CG 1 ATOM 5406 C CD1 . LEU C 3 93 ? 50.450 -51.873 13.494 1.00 57.90 ? 119 LEU K CD1 1 ATOM 5407 C CD2 . LEU C 3 93 ? 51.032 -53.992 14.592 1.00 58.32 ? 119 LEU K CD2 1 ATOM 5408 N N . VAL C 3 94 ? 46.269 -53.253 13.482 1.00 60.87 ? 120 VAL K N 1 ATOM 5409 C CA . VAL C 3 94 ? 45.641 -54.258 12.620 1.00 61.17 ? 120 VAL K CA 1 ATOM 5410 C C . VAL C 3 94 ? 46.591 -54.907 11.617 1.00 60.52 ? 120 VAL K C 1 ATOM 5411 O O . VAL C 3 94 ? 46.483 -56.097 11.350 1.00 60.72 ? 120 VAL K O 1 ATOM 5412 C CB . VAL C 3 94 ? 44.352 -53.737 11.939 1.00 61.66 ? 120 VAL K CB 1 ATOM 5413 C CG1 . VAL C 3 94 ? 44.359 -52.255 11.861 1.00 61.98 ? 120 VAL K CG1 1 ATOM 5414 C CG2 . VAL C 3 94 ? 44.181 -54.323 10.567 1.00 61.25 ? 120 VAL K CG2 1 ATOM 5415 N N . SER C 3 95 ? 47.523 -54.140 11.059 1.00 72.04 ? 121 SER K N 1 ATOM 5416 C CA . SER C 3 95 ? 48.430 -54.690 10.043 1.00 70.96 ? 121 SER K CA 1 ATOM 5417 C C . SER C 3 95 ? 49.887 -54.279 10.252 1.00 69.90 ? 121 SER K C 1 ATOM 5418 O O . SER C 3 95 ? 50.180 -53.099 10.424 1.00 69.54 ? 121 SER K O 1 ATOM 5419 C CB . SER C 3 95 ? 47.966 -54.285 8.640 1.00 70.48 ? 121 SER K CB 1 ATOM 5420 O OG . SER C 3 95 ? 48.941 -54.588 7.663 1.00 69.38 ? 121 SER K OG 1 ATOM 5421 N N . LEU C 3 96 ? 50.793 -55.255 10.265 1.00 69.80 ? 122 LEU K N 1 ATOM 5422 C CA . LEU C 3 96 ? 52.220 -54.962 10.311 1.00 68.78 ? 122 LEU K CA 1 ATOM 5423 C C . LEU C 3 96 ? 52.933 -55.577 9.120 1.00 67.88 ? 122 LEU K C 1 ATOM 5424 O O . LEU C 3 96 ? 53.142 -56.787 9.076 1.00 68.06 ? 122 LEU K O 1 ATOM 5425 C CB . LEU C 3 96 ? 52.818 -55.482 11.624 1.00 69.29 ? 122 LEU K CB 1 ATOM 5426 C CG . LEU C 3 96 ? 54.325 -55.675 11.837 1.00 68.46 ? 122 LEU K CG 1 ATOM 5427 C CD1 . LEU C 3 96 ? 55.106 -54.400 11.759 1.00 67.39 ? 122 LEU K CD1 1 ATOM 5428 C CD2 . LEU C 3 96 ? 54.546 -56.280 13.185 1.00 69.37 ? 122 LEU K CD2 1 ATOM 5429 N N . ASP C 3 97 ? 53.343 -54.730 8.176 1.00 69.13 ? 123 ASP K N 1 ATOM 5430 C CA . ASP C 3 97 ? 54.085 -55.187 7.005 1.00 68.39 ? 123 ASP K CA 1 ATOM 5431 C C . ASP C 3 97 ? 55.505 -54.623 7.001 1.00 67.54 ? 123 ASP K C 1 ATOM 5432 O O . ASP C 3 97 ? 55.709 -53.436 6.747 1.00 67.08 ? 123 ASP K O 1 ATOM 5433 C CB . ASP C 3 97 ? 53.383 -54.725 5.729 1.00 68.22 ? 123 ASP K CB 1 ATOM 5434 C CG . ASP C 3 97 ? 51.961 -55.247 5.603 1.00 69.06 ? 123 ASP K CG 1 ATOM 5435 O OD1 . ASP C 3 97 ? 51.085 -54.803 6.378 1.00 69.70 ? 123 ASP K OD1 1 ATOM 5436 O OD2 . ASP C 3 97 ? 51.714 -56.070 4.697 1.00 69.13 ? 123 ASP K OD2 1 ATOM 5437 N N . LEU C 3 98 ? 56.470 -55.477 7.328 1.00 58.26 ? 124 LEU K N 1 ATOM 5438 C CA . LEU C 3 98 ? 57.896 -55.157 7.272 1.00 57.70 ? 124 LEU K CA 1 ATOM 5439 C C . LEU C 3 98 ? 58.616 -55.806 6.114 1.00 57.52 ? 124 LEU K C 1 ATOM 5440 O O . LEU C 3 98 ? 59.842 -55.728 6.024 1.00 57.15 ? 124 LEU K O 1 ATOM 5441 C CB . LEU C 3 98 ? 58.584 -55.537 8.576 1.00 57.83 ? 124 LEU K CB 1 ATOM 5442 C CG . LEU C 3 98 ? 58.114 -54.681 9.735 1.00 57.91 ? 124 LEU K CG 1 ATOM 5443 C CD1 . LEU C 3 98 ? 58.595 -55.271 11.001 1.00 58.17 ? 124 LEU K CD1 1 ATOM 5444 C CD2 . LEU C 3 98 ? 58.678 -53.316 9.548 1.00 57.26 ? 124 LEU K CD2 1 ATOM 5445 N N . TYR C 3 99 ? 57.864 -56.511 5.277 1.00 62.43 ? 125 TYR K N 1 ATOM 5446 C CA . TYR C 3 99 ? 58.459 -57.433 4.313 1.00 62.29 ? 125 TYR K CA 1 ATOM 5447 C C . TYR C 3 99 ? 59.313 -56.783 3.223 1.00 61.69 ? 125 TYR K C 1 ATOM 5448 O O . TYR C 3 99 ? 59.165 -55.597 2.914 1.00 61.45 ? 125 TYR K O 1 ATOM 5449 C CB . TYR C 3 99 ? 57.395 -58.332 3.701 1.00 62.73 ? 125 TYR K CB 1 ATOM 5450 C CG . TYR C 3 99 ? 56.337 -57.614 2.905 1.00 62.69 ? 125 TYR K CG 1 ATOM 5451 C CD1 . TYR C 3 99 ? 55.269 -57.014 3.536 1.00 63.12 ? 125 TYR K CD1 1 ATOM 5452 C CD2 . TYR C 3 99 ? 56.386 -57.571 1.524 1.00 62.31 ? 125 TYR K CD2 1 ATOM 5453 C CE1 . TYR C 3 99 ? 54.286 -56.377 2.820 1.00 63.18 ? 125 TYR K CE1 1 ATOM 5454 C CE2 . TYR C 3 99 ? 55.407 -56.935 0.802 1.00 62.33 ? 125 TYR K CE2 1 ATOM 5455 C CZ . TYR C 3 99 ? 54.360 -56.339 1.460 1.00 62.77 ? 125 TYR K CZ 1 ATOM 5456 O OH . TYR C 3 99 ? 53.364 -55.706 0.763 1.00 62.90 ? 125 TYR K OH 1 ATOM 5457 N N . LEU C 3 100 ? 60.202 -57.589 2.645 1.00 62.67 ? 126 LEU K N 1 ATOM 5458 C CA . LEU C 3 100 ? 61.219 -57.112 1.707 1.00 62.20 ? 126 LEU K CA 1 ATOM 5459 C C . LEU C 3 100 ? 62.134 -56.076 2.336 1.00 61.84 ? 126 LEU K C 1 ATOM 5460 O O . LEU C 3 100 ? 62.067 -54.896 1.992 1.00 61.59 ? 126 LEU K O 1 ATOM 5461 C CB . LEU C 3 100 ? 60.602 -56.543 0.431 1.00 62.10 ? 126 LEU K CB 1 ATOM 5462 C CG . LEU C 3 100 ? 60.088 -57.576 -0.550 1.00 62.38 ? 126 LEU K CG 1 ATOM 5463 C CD1 . LEU C 3 100 ? 59.411 -56.830 -1.658 1.00 62.43 ? 126 LEU K CD1 1 ATOM 5464 C CD2 . LEU C 3 100 ? 61.216 -58.443 -1.084 1.00 62.41 ? 126 LEU K CD2 1 ATOM 5465 N N . ASN C 3 101 ? 62.967 -56.525 3.272 1.00 60.92 ? 127 ASN K N 1 ATOM 5466 C CA . ASN C 3 101 ? 64.015 -55.693 3.847 1.00 60.60 ? 127 ASN K CA 1 ATOM 5467 C C . ASN C 3 101 ? 65.230 -56.514 4.270 1.00 60.70 ? 127 ASN K C 1 ATOM 5468 O O . ASN C 3 101 ? 65.352 -57.688 3.907 1.00 60.97 ? 127 ASN K O 1 ATOM 5469 C CB . ASN C 3 101 ? 63.485 -54.877 5.015 1.00 60.64 ? 127 ASN K CB 1 ATOM 5470 C CG . ASN C 3 101 ? 62.679 -53.684 4.566 1.00 60.56 ? 127 ASN K CG 1 ATOM 5471 O OD1 . ASN C 3 101 ? 63.192 -52.568 4.472 1.00 60.19 ? 127 ASN K OD1 1 ATOM 5472 N ND2 . ASN C 3 101 ? 61.407 -53.911 4.273 1.00 60.99 ? 127 ASN K ND2 1 ATOM 5473 N N . SER C 3 102 ? 66.159 -55.866 4.968 1.00 77.95 ? 128 SER K N 1 ATOM 5474 C CA . SER C 3 102 ? 67.334 -56.528 5.547 1.00 78.13 ? 128 SER K CA 1 ATOM 5475 C C . SER C 3 102 ? 67.311 -56.872 7.058 1.00 78.47 ? 128 SER K C 1 ATOM 5476 O O . SER C 3 102 ? 68.353 -57.203 7.627 1.00 78.60 ? 128 SER K O 1 ATOM 5477 C CB . SER C 3 102 ? 68.641 -55.880 5.085 1.00 77.75 ? 128 SER K CB 1 ATOM 5478 O OG . SER C 3 102 ? 68.896 -56.224 3.733 1.00 77.74 ? 128 SER K OG 1 ATOM 5479 N N . PHE C 3 103 ? 66.144 -56.759 7.698 1.00 60.31 ? 129 PHE K N 1 ATOM 5480 C CA . PHE C 3 103 ? 65.988 -57.017 9.135 1.00 60.62 ? 129 PHE K CA 1 ATOM 5481 C C . PHE C 3 103 ? 66.643 -58.291 9.645 1.00 61.19 ? 129 PHE K C 1 ATOM 5482 O O . PHE C 3 103 ? 66.556 -59.337 9.027 1.00 61.63 ? 129 PHE K O 1 ATOM 5483 C CB . PHE C 3 103 ? 64.514 -57.172 9.468 1.00 61.03 ? 129 PHE K CB 1 ATOM 5484 C CG . PHE C 3 103 ? 63.771 -55.902 9.493 1.00 60.59 ? 129 PHE K CG 1 ATOM 5485 C CD1 . PHE C 3 103 ? 63.283 -55.354 8.338 1.00 60.68 ? 129 PHE K CD1 1 ATOM 5486 C CD2 . PHE C 3 103 ? 63.547 -55.254 10.678 1.00 60.17 ? 129 PHE K CD2 1 ATOM 5487 C CE1 . PHE C 3 103 ? 62.587 -54.172 8.363 1.00 60.39 ? 129 PHE K CE1 1 ATOM 5488 C CE2 . PHE C 3 103 ? 62.861 -54.068 10.706 1.00 59.85 ? 129 PHE K CE2 1 ATOM 5489 C CZ . PHE C 3 103 ? 62.379 -53.525 9.548 1.00 59.97 ? 129 PHE K CZ 1 ATOM 5490 N N . THR C 3 104 ? 67.276 -58.197 10.806 1.00 76.86 ? 130 THR K N 1 ATOM 5491 C CA . THR C 3 104 ? 67.895 -59.353 11.426 1.00 77.48 ? 130 THR K CA 1 ATOM 5492 C C . THR C 3 104 ? 67.368 -59.549 12.826 1.00 78.11 ? 130 THR K C 1 ATOM 5493 O O . THR C 3 104 ? 66.714 -58.672 13.386 1.00 78.02 ? 130 THR K O 1 ATOM 5494 C CB . THR C 3 104 ? 69.396 -59.184 11.534 1.00 77.27 ? 130 THR K CB 1 ATOM 5495 O OG1 . THR C 3 104 ? 69.801 -58.074 10.723 1.00 77.05 ? 130 THR K OG1 1 ATOM 5496 C CG2 . THR C 3 104 ? 70.104 -60.472 11.094 1.00 77.25 ? 130 THR K CG2 1 ATOM 5497 N N . GLY C 3 105 ? 67.641 -60.717 13.387 1.00 84.24 ? 131 GLY K N 1 ATOM 5498 C CA . GLY C 3 105 ? 67.311 -60.954 14.773 1.00 85.01 ? 131 GLY K CA 1 ATOM 5499 C C . GLY C 3 105 ? 66.066 -61.783 14.941 1.00 85.71 ? 131 GLY K C 1 ATOM 5500 O O . GLY C 3 105 ? 65.562 -62.353 13.982 1.00 85.57 ? 131 GLY K O 1 ATOM 5501 N N . PRO C 3 106 ? 65.571 -61.864 16.174 1.00 75.38 ? 132 PRO K N 1 ATOM 5502 C CA . PRO C 3 106 ? 64.453 -62.719 16.545 1.00 76.26 ? 132 PRO K CA 1 ATOM 5503 C C . PRO C 3 106 ? 63.144 -62.068 16.164 1.00 76.14 ? 132 PRO K C 1 ATOM 5504 O O . PRO C 3 106 ? 63.099 -60.855 15.959 1.00 75.36 ? 132 PRO K O 1 ATOM 5505 C CB . PRO C 3 106 ? 64.570 -62.763 18.062 1.00 77.12 ? 132 PRO K CB 1 ATOM 5506 C CG . PRO C 3 106 ? 65.010 -61.376 18.405 1.00 76.53 ? 132 PRO K CG 1 ATOM 5507 C CD . PRO C 3 106 ? 65.928 -60.945 17.268 1.00 75.44 ? 132 PRO K CD 1 ATOM 5508 N N . ILE C 3 107 ? 62.095 -62.872 16.057 1.00 59.76 ? 133 ILE K N 1 ATOM 5509 C CA . ILE C 3 107 ? 60.748 -62.331 16.039 1.00 59.73 ? 133 ILE K CA 1 ATOM 5510 C C . ILE C 3 107 ? 60.240 -62.235 17.481 1.00 60.55 ? 133 ILE K C 1 ATOM 5511 O O . ILE C 3 107 ? 59.927 -63.252 18.110 1.00 61.47 ? 133 ILE K O 1 ATOM 5512 C CB . ILE C 3 107 ? 59.793 -63.207 15.202 1.00 60.13 ? 133 ILE K CB 1 ATOM 5513 C CG1 . ILE C 3 107 ? 60.343 -63.417 13.798 1.00 59.65 ? 133 ILE K CG1 1 ATOM 5514 C CG2 . ILE C 3 107 ? 58.400 -62.593 15.127 1.00 60.23 ? 133 ILE K CG2 1 ATOM 5515 C CD1 . ILE C 3 107 ? 59.485 -64.324 12.970 1.00 60.02 ? 133 ILE K CD1 1 ATOM 5516 N N . PRO C 3 108 ? 60.133 -61.004 17.995 1.00 60.24 ? 134 PRO K N 1 ATOM 5517 C CA . PRO C 3 108 ? 59.801 -60.641 19.372 1.00 60.90 ? 134 PRO K CA 1 ATOM 5518 C C . PRO C 3 108 ? 58.557 -61.332 19.891 1.00 61.92 ? 134 PRO K C 1 ATOM 5519 O O . PRO C 3 108 ? 57.547 -61.245 19.228 1.00 61.84 ? 134 PRO K O 1 ATOM 5520 C CB . PRO C 3 108 ? 59.472 -59.162 19.235 1.00 60.28 ? 134 PRO K CB 1 ATOM 5521 C CG . PRO C 3 108 ? 60.337 -58.709 18.162 1.00 59.20 ? 134 PRO K CG 1 ATOM 5522 C CD . PRO C 3 108 ? 60.398 -59.814 17.180 1.00 59.22 ? 134 PRO K CD 1 ATOM 5523 N N . ASP C 3 109 ? 58.601 -61.951 21.064 1.00 79.92 ? 135 ASP K N 1 ATOM 5524 C CA . ASP C 3 109 ? 57.407 -62.592 21.602 1.00 81.26 ? 135 ASP K CA 1 ATOM 5525 C C . ASP C 3 109 ? 56.335 -61.572 21.897 1.00 81.95 ? 135 ASP K C 1 ATOM 5526 O O . ASP C 3 109 ? 55.163 -61.911 22.036 1.00 82.82 ? 135 ASP K O 1 ATOM 5527 C CB . ASP C 3 109 ? 57.711 -63.339 22.892 1.00 82.28 ? 135 ASP K CB 1 ATOM 5528 C CG . ASP C 3 109 ? 58.602 -64.533 22.674 1.00 81.99 ? 135 ASP K CG 1 ATOM 5529 O OD1 . ASP C 3 109 ? 58.750 -64.943 21.502 1.00 81.04 ? 135 ASP K OD1 1 ATOM 5530 O OD2 . ASP C 3 109 ? 59.151 -65.060 23.673 1.00 82.72 ? 135 ASP K OD2 1 ATOM 5531 N N . SER C 3 110 ? 56.751 -60.318 22.013 1.00 84.07 ? 136 SER K N 1 ATOM 5532 C CA . SER C 3 110 ? 55.838 -59.231 22.320 1.00 84.81 ? 136 SER K CA 1 ATOM 5533 C C . SER C 3 110 ? 54.854 -59.016 21.179 1.00 84.57 ? 136 SER K C 1 ATOM 5534 O O . SER C 3 110 ? 53.791 -58.430 21.367 1.00 85.34 ? 136 SER K O 1 ATOM 5535 C CB . SER C 3 110 ? 56.628 -57.961 22.540 1.00 83.91 ? 136 SER K CB 1 ATOM 5536 O OG . SER C 3 110 ? 57.387 -57.696 21.381 1.00 81.94 ? 136 SER K OG 1 ATOM 5537 N N . LEU C 3 111 ? 55.223 -59.481 19.988 1.00 60.62 ? 137 LEU K N 1 ATOM 5538 C CA . LEU C 3 111 ? 54.308 -59.496 18.843 1.00 60.46 ? 137 LEU K CA 1 ATOM 5539 C C . LEU C 3 111 ? 53.078 -60.333 19.116 1.00 61.27 ? 137 LEU K C 1 ATOM 5540 O O . LEU C 3 111 ? 52.041 -60.120 18.508 1.00 61.39 ? 137 LEU K O 1 ATOM 5541 C CB . LEU C 3 111 ? 55.009 -60.041 17.611 1.00 59.84 ? 137 LEU K CB 1 ATOM 5542 C CG . LEU C 3 111 ? 55.860 -58.968 16.981 1.00 58.94 ? 137 LEU K CG 1 ATOM 5543 C CD1 . LEU C 3 111 ? 56.815 -59.577 16.017 1.00 58.59 ? 137 LEU K CD1 1 ATOM 5544 C CD2 . LEU C 3 111 ? 54.917 -58.057 16.279 1.00 58.78 ? 137 LEU K CD2 1 ATOM 5545 N N . GLY C 3 112 ? 53.192 -61.278 20.041 1.00 69.32 ? 138 GLY K N 1 ATOM 5546 C CA . GLY C 3 112 ? 52.057 -62.080 20.433 1.00 70.06 ? 138 GLY K CA 1 ATOM 5547 C C . GLY C 3 112 ? 51.025 -61.261 21.191 1.00 70.40 ? 138 GLY K C 1 ATOM 5548 O O . GLY C 3 112 ? 49.986 -61.785 21.628 1.00 70.70 ? 138 GLY K O 1 ATOM 5549 N N . LYS C 3 113 ? 51.321 -59.977 21.372 1.00 74.25 ? 139 LYS K N 1 ATOM 5550 C CA . LYS C 3 113 ? 50.453 -59.111 22.150 1.00 74.30 ? 139 LYS K CA 1 ATOM 5551 C C . LYS C 3 113 ? 49.508 -58.270 21.317 1.00 73.80 ? 139 LYS K C 1 ATOM 5552 O O . LYS C 3 113 ? 48.776 -57.467 21.881 1.00 73.92 ? 139 LYS K O 1 ATOM 5553 C CB . LYS C 3 113 ? 51.264 -58.223 23.100 1.00 74.36 ? 139 LYS K CB 1 ATOM 5554 C CG . LYS C 3 113 ? 52.070 -58.992 24.154 1.00 75.00 ? 139 LYS K CG 1 ATOM 5555 C CD . LYS C 3 113 ? 53.086 -58.093 24.847 1.00 75.01 ? 139 LYS K CD 1 ATOM 5556 C CE . LYS C 3 113 ? 52.426 -56.831 25.410 1.00 74.78 ? 139 LYS K CE 1 ATOM 5557 N NZ . LYS C 3 113 ? 53.385 -55.934 26.137 1.00 74.51 ? 139 LYS K NZ 1 ATOM 5558 N N . LEU C 3 114 ? 49.514 -58.432 19.993 1.00 61.40 ? 140 LEU K N 1 ATOM 5559 C CA . LEU C 3 114 ? 48.640 -57.602 19.145 1.00 61.07 ? 140 LEU K CA 1 ATOM 5560 C C . LEU C 3 114 ? 47.410 -58.401 18.742 1.00 61.45 ? 140 LEU K C 1 ATOM 5561 O O . LEU C 3 114 ? 47.491 -59.285 17.894 1.00 61.58 ? 140 LEU K O 1 ATOM 5562 C CB . LEU C 3 114 ? 49.373 -57.114 17.892 1.00 60.66 ? 140 LEU K CB 1 ATOM 5563 C CG . LEU C 3 114 ? 50.901 -57.061 17.921 1.00 60.45 ? 140 LEU K CG 1 ATOM 5564 C CD1 . LEU C 3 114 ? 51.442 -57.040 16.528 1.00 59.82 ? 140 LEU K CD1 1 ATOM 5565 C CD2 . LEU C 3 114 ? 51.381 -55.851 18.655 1.00 59.91 ? 140 LEU K CD2 1 ATOM 5566 N N . PHE C 3 115 ? 46.280 -58.070 19.366 1.00 89.84 ? 141 PHE K N 1 ATOM 5567 C CA . PHE C 3 115 ? 45.052 -58.849 19.241 1.00 90.41 ? 141 PHE K CA 1 ATOM 5568 C C . PHE C 3 115 ? 44.024 -58.274 18.285 1.00 90.39 ? 141 PHE K C 1 ATOM 5569 O O . PHE C 3 115 ? 42.957 -58.852 18.089 1.00 90.91 ? 141 PHE K O 1 ATOM 5570 C CB . PHE C 3 115 ? 44.433 -59.065 20.614 1.00 91.39 ? 141 PHE K CB 1 ATOM 5571 C CG . PHE C 3 115 ? 45.348 -59.763 21.578 1.00 91.46 ? 141 PHE K CG 1 ATOM 5572 C CD1 . PHE C 3 115 ? 45.451 -61.145 21.582 1.00 91.58 ? 141 PHE K CD1 1 ATOM 5573 C CD2 . PHE C 3 115 ? 46.116 -59.041 22.474 1.00 91.47 ? 141 PHE K CD2 1 ATOM 5574 C CE1 . PHE C 3 115 ? 46.306 -61.795 22.471 1.00 91.74 ? 141 PHE K CE1 1 ATOM 5575 C CE2 . PHE C 3 115 ? 46.969 -59.686 23.363 1.00 91.67 ? 141 PHE K CE2 1 ATOM 5576 C CZ . PHE C 3 115 ? 47.062 -61.062 23.359 1.00 91.82 ? 141 PHE K CZ 1 ATOM 5577 N N . LYS C 3 116 ? 44.324 -57.110 17.726 1.00 75.18 ? 142 LYS K N 1 ATOM 5578 C CA . LYS C 3 116 ? 43.531 -56.590 16.624 1.00 75.09 ? 142 LYS K CA 1 ATOM 5579 C C . LYS C 3 116 ? 44.235 -56.919 15.318 1.00 74.07 ? 142 LYS K C 1 ATOM 5580 O O . LYS C 3 116 ? 43.771 -56.527 14.258 1.00 73.84 ? 142 LYS K O 1 ATOM 5581 C CB . LYS C 3 116 ? 43.282 -55.084 16.770 1.00 75.37 ? 142 LYS K CB 1 ATOM 5582 C CG . LYS C 3 116 ? 41.878 -54.734 17.281 1.00 76.93 ? 142 LYS K CG 1 ATOM 5583 C CD . LYS C 3 116 ? 41.894 -53.640 18.349 1.00 77.36 ? 142 LYS K CD 1 ATOM 5584 C CE . LYS C 3 116 ? 42.286 -54.191 19.717 1.00 77.88 ? 142 LYS K CE 1 ATOM 5585 N NZ . LYS C 3 116 ? 42.495 -53.106 20.715 1.00 78.06 ? 142 LYS K NZ 1 ATOM 5586 N N . LEU C 3 117 ? 45.352 -57.645 15.408 1.00 62.08 ? 143 LEU K N 1 ATOM 5587 C CA . LEU C 3 117 ? 46.207 -57.903 14.249 1.00 61.71 ? 143 LEU K CA 1 ATOM 5588 C C . LEU C 3 117 ? 45.587 -58.896 13.303 1.00 61.92 ? 143 LEU K C 1 ATOM 5589 O O . LEU C 3 117 ? 45.133 -59.951 13.723 1.00 62.30 ? 143 LEU K O 1 ATOM 5590 C CB . LEU C 3 117 ? 47.587 -58.420 14.641 1.00 61.80 ? 143 LEU K CB 1 ATOM 5591 C CG . LEU C 3 117 ? 48.592 -58.241 13.502 1.00 60.98 ? 143 LEU K CG 1 ATOM 5592 C CD1 . LEU C 3 117 ? 49.037 -56.812 13.477 1.00 60.08 ? 143 LEU K CD1 1 ATOM 5593 C CD2 . LEU C 3 117 ? 49.780 -59.153 13.621 1.00 60.90 ? 143 LEU K CD2 1 ATOM 5594 N N . ARG C 3 118 ? 45.613 -58.535 12.022 1.00 77.51 ? 144 ARG K N 1 ATOM 5595 C CA . ARG C 3 118 ? 45.013 -59.272 10.915 1.00 77.47 ? 144 ARG K CA 1 ATOM 5596 C C . ARG C 3 118 ? 46.093 -59.718 9.944 1.00 76.43 ? 144 ARG K C 1 ATOM 5597 O O . ARG C 3 118 ? 46.169 -60.889 9.591 1.00 76.40 ? 144 ARG K O 1 ATOM 5598 C CB . ARG C 3 118 ? 43.957 -58.436 10.204 1.00 77.35 ? 144 ARG K CB 1 ATOM 5599 C CG . ARG C 3 118 ? 42.795 -58.059 11.099 1.00 78.20 ? 144 ARG K CG 1 ATOM 5600 C CD . ARG C 3 118 ? 41.636 -57.516 10.304 1.00 78.56 ? 144 ARG K CD 1 ATOM 5601 N NE . ARG C 3 118 ? 41.271 -58.441 9.246 1.00 78.51 ? 144 ARG K NE 1 ATOM 5602 C CZ . ARG C 3 118 ? 41.054 -58.078 7.991 1.00 78.11 ? 144 ARG K CZ 1 ATOM 5603 N NH1 . ARG C 3 118 ? 40.732 -58.983 7.083 1.00 78.08 ? 144 ARG K NH1 1 ATOM 5604 N NH2 . ARG C 3 118 ? 41.158 -56.806 7.648 1.00 77.72 ? 144 ARG K NH2 1 ATOM 5605 N N . PHE C 3 119 ? 46.870 -58.761 9.444 1.00 72.87 ? 145 PHE K N 1 ATOM 5606 C CA . PHE C 3 119 ? 47.967 -59.052 8.518 1.00 71.69 ? 145 PHE K CA 1 ATOM 5607 C C . PHE C 3 119 ? 49.373 -58.918 9.109 1.00 71.11 ? 145 PHE K C 1 ATOM 5608 O O . PHE C 3 119 ? 49.746 -57.870 9.627 1.00 70.75 ? 145 PHE K O 1 ATOM 5609 C CB . PHE C 3 119 ? 47.863 -58.145 7.305 1.00 70.82 ? 145 PHE K CB 1 ATOM 5610 C CG . PHE C 3 119 ? 46.478 -58.033 6.760 1.00 71.45 ? 145 PHE K CG 1 ATOM 5611 C CD1 . PHE C 3 119 ? 45.612 -57.062 7.233 1.00 72.10 ? 145 PHE K CD1 1 ATOM 5612 C CD2 . PHE C 3 119 ? 46.042 -58.895 5.776 1.00 71.42 ? 145 PHE K CD2 1 ATOM 5613 C CE1 . PHE C 3 119 ? 44.338 -56.952 6.735 1.00 72.75 ? 145 PHE K CE1 1 ATOM 5614 C CE2 . PHE C 3 119 ? 44.767 -58.790 5.266 1.00 71.97 ? 145 PHE K CE2 1 ATOM 5615 C CZ . PHE C 3 119 ? 43.912 -57.818 5.747 1.00 72.68 ? 145 PHE K CZ 1 ATOM 5616 N N . LEU C 3 120 ? 50.149 -59.992 9.005 1.00 59.25 ? 146 LEU K N 1 ATOM 5617 C CA . LEU C 3 120 ? 51.542 -59.998 9.429 1.00 58.85 ? 146 LEU K CA 1 ATOM 5618 C C . LEU C 3 120 ? 52.437 -60.524 8.308 1.00 58.65 ? 146 LEU K C 1 ATOM 5619 O O . LEU C 3 120 ? 52.386 -61.700 7.945 1.00 58.98 ? 146 LEU K O 1 ATOM 5620 C CB . LEU C 3 120 ? 51.719 -60.867 10.682 1.00 59.19 ? 146 LEU K CB 1 ATOM 5621 C CG . LEU C 3 120 ? 53.078 -60.835 11.388 1.00 58.89 ? 146 LEU K CG 1 ATOM 5622 C CD1 . LEU C 3 120 ? 53.339 -59.455 11.923 1.00 58.34 ? 146 LEU K CD1 1 ATOM 5623 C CD2 . LEU C 3 120 ? 53.134 -61.831 12.503 1.00 59.46 ? 146 LEU K CD2 1 ATOM 5624 N N . ARG C 3 121 ? 53.257 -59.644 7.754 1.00 67.07 ? 147 ARG K N 1 ATOM 5625 C CA . ARG C 3 121 ? 54.182 -60.059 6.724 1.00 66.26 ? 147 ARG K CA 1 ATOM 5626 C C . ARG C 3 121 ? 55.582 -59.587 7.024 1.00 65.61 ? 147 ARG K C 1 ATOM 5627 O O . ARG C 3 121 ? 55.885 -58.402 6.943 1.00 64.96 ? 147 ARG K O 1 ATOM 5628 C CB . ARG C 3 121 ? 53.734 -59.500 5.383 1.00 65.77 ? 147 ARG K CB 1 ATOM 5629 C CG . ARG C 3 121 ? 52.669 -60.324 4.730 1.00 66.16 ? 147 ARG K CG 1 ATOM 5630 C CD . ARG C 3 121 ? 52.069 -59.590 3.575 1.00 65.91 ? 147 ARG K CD 1 ATOM 5631 N NE . ARG C 3 121 ? 51.079 -58.610 4.008 1.00 66.35 ? 147 ARG K NE 1 ATOM 5632 C CZ . ARG C 3 121 ? 49.791 -58.672 3.687 1.00 66.99 ? 147 ARG K CZ 1 ATOM 5633 N NH1 . ARG C 3 121 ? 49.351 -59.671 2.930 1.00 67.18 ? 147 ARG K NH1 1 ATOM 5634 N NH2 . ARG C 3 121 ? 48.945 -57.738 4.112 1.00 67.47 ? 147 ARG K NH2 1 ATOM 5635 N N . LEU C 3 122 ? 56.427 -60.535 7.387 1.00 71.06 ? 148 LEU K N 1 ATOM 5636 C CA . LEU C 3 122 ? 57.855 -60.315 7.519 1.00 70.55 ? 148 LEU K CA 1 ATOM 5637 C C . LEU C 3 122 ? 58.640 -60.887 6.338 1.00 70.15 ? 148 LEU K C 1 ATOM 5638 O O . LEU C 3 122 ? 59.858 -60.946 6.367 1.00 69.93 ? 148 LEU K O 1 ATOM 5639 C CB . LEU C 3 122 ? 58.351 -60.867 8.849 1.00 71.22 ? 148 LEU K CB 1 ATOM 5640 C CG . LEU C 3 122 ? 57.374 -60.531 9.966 1.00 71.90 ? 148 LEU K CG 1 ATOM 5641 C CD1 . LEU C 3 122 ? 57.848 -61.134 11.256 1.00 72.68 ? 148 LEU K CD1 1 ATOM 5642 C CD2 . LEU C 3 122 ? 57.209 -59.035 10.102 1.00 71.26 ? 148 LEU K CD2 1 ATOM 5643 N N . ASN C 3 123 ? 57.946 -61.365 5.325 1.00 68.39 ? 149 ASN K N 1 ATOM 5644 C CA . ASN C 3 123 ? 58.603 -62.183 4.327 1.00 68.26 ? 149 ASN K CA 1 ATOM 5645 C C . ASN C 3 123 ? 59.715 -61.483 3.554 1.00 67.56 ? 149 ASN K C 1 ATOM 5646 O O . ASN C 3 123 ? 59.796 -60.258 3.535 1.00 67.08 ? 149 ASN K O 1 ATOM 5647 C CB . ASN C 3 123 ? 57.579 -62.748 3.358 1.00 68.46 ? 149 ASN K CB 1 ATOM 5648 C CG . ASN C 3 123 ? 56.706 -61.675 2.745 1.00 68.02 ? 149 ASN K CG 1 ATOM 5649 O OD1 . ASN C 3 123 ? 55.822 -61.130 3.410 1.00 68.22 ? 149 ASN K OD1 1 ATOM 5650 N ND2 . ASN C 3 123 ? 56.935 -61.378 1.462 1.00 67.52 ? 149 ASN K ND2 1 ATOM 5651 N N . ASN C 3 124 ? 60.584 -62.291 2.949 1.00 69.07 ? 150 ASN K N 1 ATOM 5652 C CA . ASN C 3 124 ? 61.777 -61.831 2.226 1.00 68.55 ? 150 ASN K CA 1 ATOM 5653 C C . ASN C 3 124 ? 62.680 -60.850 3.003 1.00 68.11 ? 150 ASN K C 1 ATOM 5654 O O . ASN C 3 124 ? 63.033 -59.778 2.509 1.00 67.53 ? 150 ASN K O 1 ATOM 5655 C CB . ASN C 3 124 ? 61.428 -61.335 0.813 1.00 68.30 ? 150 ASN K CB 1 ATOM 5656 C CG . ASN C 3 124 ? 61.355 -62.478 -0.217 1.00 68.62 ? 150 ASN K CG 1 ATOM 5657 O OD1 . ASN C 3 124 ? 60.498 -63.362 -0.111 1.00 68.02 ? 150 ASN K OD1 1 ATOM 5658 N ND2 . ASN C 3 124 ? 62.257 -62.445 -1.228 1.00 69.60 ? 150 ASN K ND2 1 ATOM 5659 N N . ASN C 3 125 ? 63.041 -61.260 4.223 1.00 59.23 ? 151 ASN K N 1 ATOM 5660 C CA . ASN C 3 125 ? 63.942 -60.540 5.133 1.00 58.90 ? 151 ASN K CA 1 ATOM 5661 C C . ASN C 3 125 ? 65.074 -61.469 5.563 1.00 59.43 ? 151 ASN K C 1 ATOM 5662 O O . ASN C 3 125 ? 65.224 -62.573 5.013 1.00 60.09 ? 151 ASN K O 1 ATOM 5663 C CB . ASN C 3 125 ? 63.198 -60.040 6.375 1.00 58.31 ? 151 ASN K CB 1 ATOM 5664 C CG . ASN C 3 125 ? 62.704 -58.618 6.229 1.00 57.73 ? 151 ASN K CG 1 ATOM 5665 O OD1 . ASN C 3 125 ? 63.411 -57.679 6.551 1.00 57.50 ? 151 ASN K OD1 1 ATOM 5666 N ND2 . ASN C 3 125 ? 61.485 -58.452 5.746 1.00 57.56 ? 151 ASN K ND2 1 ATOM 5667 N N . SER C 3 126 ? 65.899 -60.992 6.497 1.00 65.35 ? 152 SER K N 1 ATOM 5668 C CA . SER C 3 126 ? 67.023 -61.753 7.069 1.00 65.74 ? 152 SER K CA 1 ATOM 5669 C C . SER C 3 126 ? 66.809 -62.394 8.446 1.00 66.46 ? 152 SER K C 1 ATOM 5670 O O . SER C 3 126 ? 67.764 -62.890 9.034 1.00 66.84 ? 152 SER K O 1 ATOM 5671 C CB . SER C 3 126 ? 68.308 -60.927 7.056 1.00 65.28 ? 152 SER K CB 1 ATOM 5672 O OG . SER C 3 126 ? 68.638 -60.529 5.734 1.00 64.69 ? 152 SER K OG 1 ATOM 5673 N N . LEU C 3 127 ? 65.579 -62.337 8.961 1.00 60.64 ? 153 LEU K N 1 ATOM 5674 C CA . LEU C 3 127 ? 65.225 -62.781 10.327 1.00 60.71 ? 153 LEU K CA 1 ATOM 5675 C C . LEU C 3 127 ? 65.640 -64.191 10.728 1.00 61.60 ? 153 LEU K C 1 ATOM 5676 O O . LEU C 3 127 ? 65.623 -65.128 9.922 1.00 62.20 ? 153 LEU K O 1 ATOM 5677 C CB . LEU C 3 127 ? 63.722 -62.686 10.559 1.00 60.47 ? 153 LEU K CB 1 ATOM 5678 C CG . LEU C 3 127 ? 63.134 -61.299 10.691 1.00 59.80 ? 153 LEU K CG 1 ATOM 5679 C CD1 . LEU C 3 127 ? 61.652 -61.412 10.871 1.00 60.29 ? 153 LEU K CD1 1 ATOM 5680 C CD2 . LEU C 3 127 ? 63.753 -60.624 11.872 1.00 59.41 ? 153 LEU K CD2 1 ATOM 5681 N N . THR C 3 128 ? 66.000 -64.331 11.998 1.00 100.77 ? 154 THR K N 1 ATOM 5682 C CA . THR C 3 128 ? 66.485 -65.589 12.540 1.00 101.75 ? 154 THR K CA 1 ATOM 5683 C C . THR C 3 128 ? 65.734 -65.899 13.824 1.00 102.53 ? 154 THR K C 1 ATOM 5684 O O . THR C 3 128 ? 64.968 -65.073 14.329 1.00 102.34 ? 154 THR K O 1 ATOM 5685 C CB . THR C 3 128 ? 67.977 -65.503 12.879 1.00 101.79 ? 154 THR K CB 1 ATOM 5686 O OG1 . THR C 3 128 ? 68.160 -64.578 13.959 1.00 101.35 ? 154 THR K OG1 1 ATOM 5687 C CG2 . THR C 3 128 ? 68.771 -65.024 11.674 1.00 100.87 ? 154 THR K CG2 1 ATOM 5688 N N . GLY C 3 129 ? 65.941 -67.104 14.338 1.00 77.68 ? 155 GLY K N 1 ATOM 5689 C CA . GLY C 3 129 ? 65.328 -67.503 15.585 1.00 78.56 ? 155 GLY K CA 1 ATOM 5690 C C . GLY C 3 129 ? 64.054 -68.272 15.348 1.00 79.08 ? 155 GLY K C 1 ATOM 5691 O O . GLY C 3 129 ? 63.759 -68.661 14.226 1.00 78.81 ? 155 GLY K O 1 ATOM 5692 N N . PRO C 3 130 ? 63.307 -68.526 16.424 1.00 66.13 ? 156 PRO K N 1 ATOM 5693 C CA . PRO C 3 130 ? 62.061 -69.293 16.344 1.00 66.72 ? 156 PRO K CA 1 ATOM 5694 C C . PRO C 3 130 ? 60.834 -68.433 16.135 1.00 66.38 ? 156 PRO K C 1 ATOM 5695 O O . PRO C 3 130 ? 60.913 -67.202 16.276 1.00 66.04 ? 156 PRO K O 1 ATOM 5696 C CB . PRO C 3 130 ? 61.953 -69.886 17.742 1.00 75.96 ? 156 PRO K CB 1 ATOM 5697 C CG . PRO C 3 130 ? 62.494 -68.741 18.623 1.00 75.32 ? 156 PRO K CG 1 ATOM 5698 C CD . PRO C 3 130 ? 63.695 -68.240 17.820 1.00 75.49 ? 156 PRO K CD 1 ATOM 5699 N N . ILE C 3 131 ? 59.710 -69.119 15.913 1.00 67.20 ? 157 ILE K N 1 ATOM 5700 C CA . ILE C 3 131 ? 58.427 -68.505 15.627 1.00 67.15 ? 157 ILE K CA 1 ATOM 5701 C C . ILE C 3 131 ? 57.693 -68.500 16.953 1.00 68.12 ? 157 ILE K C 1 ATOM 5702 O O . ILE C 3 131 ? 57.342 -69.570 17.469 1.00 68.94 ? 157 ILE K O 1 ATOM 5703 C CB . ILE C 3 131 ? 57.657 -69.332 14.575 1.00 67.20 ? 157 ILE K CB 1 ATOM 5704 C CG1 . ILE C 3 131 ? 58.567 -69.712 13.412 1.00 66.66 ? 157 ILE K CG1 1 ATOM 5705 C CG2 . ILE C 3 131 ? 56.450 -68.582 14.061 1.00 67.08 ? 157 ILE K CG2 1 ATOM 5706 C CD1 . ILE C 3 131 ? 57.851 -70.416 12.318 1.00 66.68 ? 157 ILE K CD1 1 ATOM 5707 N N . PRO C 3 132 ? 57.460 -67.303 17.506 1.00 62.33 ? 158 PRO K N 1 ATOM 5708 C CA . PRO C 3 132 ? 56.924 -67.161 18.860 1.00 62.74 ? 158 PRO K CA 1 ATOM 5709 C C . PRO C 3 132 ? 55.510 -67.695 18.955 1.00 63.13 ? 158 PRO K C 1 ATOM 5710 O O . PRO C 3 132 ? 54.710 -67.443 18.052 1.00 62.85 ? 158 PRO K O 1 ATOM 5711 C CB . PRO C 3 132 ? 56.955 -65.651 19.110 1.00 62.12 ? 158 PRO K CB 1 ATOM 5712 C CG . PRO C 3 132 ? 57.033 -65.041 17.782 1.00 61.20 ? 158 PRO K CG 1 ATOM 5713 C CD . PRO C 3 132 ? 57.699 -66.005 16.869 1.00 61.45 ? 158 PRO K CD 1 ATOM 5714 N N . MET C 3 133 ? 55.233 -68.455 20.010 1.00 69.08 ? 159 MET K N 1 ATOM 5715 C CA . MET C 3 133 ? 54.010 -69.229 20.101 1.00 69.91 ? 159 MET K CA 1 ATOM 5716 C C . MET C 3 133 ? 52.854 -68.329 20.411 1.00 70.22 ? 159 MET K C 1 ATOM 5717 O O . MET C 3 133 ? 51.721 -68.630 20.078 1.00 70.43 ? 159 MET K O 1 ATOM 5718 C CB . MET C 3 133 ? 54.148 -70.264 21.196 1.00 70.67 ? 159 MET K CB 1 ATOM 5719 C CG . MET C 3 133 ? 54.621 -71.581 20.700 1.00 70.69 ? 159 MET K CG 1 ATOM 5720 S SD . MET C 3 133 ? 53.195 -72.326 19.934 1.00 70.88 ? 159 MET K SD 1 ATOM 5721 C CE . MET C 3 133 ? 53.824 -73.983 19.588 1.00 71.15 ? 159 MET K CE 1 ATOM 5722 N N . SER C 3 134 ? 53.160 -67.207 21.041 1.00 87.79 ? 160 SER K N 1 ATOM 5723 C CA . SER C 3 134 ? 52.131 -66.292 21.477 1.00 88.21 ? 160 SER K CA 1 ATOM 5724 C C . SER C 3 134 ? 51.433 -65.724 20.270 1.00 87.65 ? 160 SER K C 1 ATOM 5725 O O . SER C 3 134 ? 50.312 -65.253 20.372 1.00 87.86 ? 160 SER K O 1 ATOM 5726 C CB . SER C 3 134 ? 52.728 -65.179 22.330 1.00 71.39 ? 160 SER K CB 1 ATOM 5727 O OG . SER C 3 134 ? 53.987 -64.747 21.805 1.00 71.11 ? 160 SER K OG 1 ATOM 5728 N N . LEU C 3 135 ? 52.109 -65.774 19.127 1.00 68.04 ? 161 LEU K N 1 ATOM 5729 C CA . LEU C 3 135 ? 51.495 -65.371 17.872 1.00 67.48 ? 161 LEU K CA 1 ATOM 5730 C C . LEU C 3 135 ? 50.166 -66.111 17.663 1.00 67.89 ? 161 LEU K C 1 ATOM 5731 O O . LEU C 3 135 ? 49.199 -65.538 17.146 1.00 67.80 ? 161 LEU K O 1 ATOM 5732 C CB . LEU C 3 135 ? 52.441 -65.574 16.667 1.00 66.29 ? 161 LEU K CB 1 ATOM 5733 C CG . LEU C 3 135 ? 53.369 -64.430 16.236 1.00 65.25 ? 161 LEU K CG 1 ATOM 5734 C CD1 . LEU C 3 135 ? 54.288 -64.868 15.129 1.00 64.27 ? 161 LEU K CD1 1 ATOM 5735 C CD2 . LEU C 3 135 ? 52.560 -63.234 15.788 1.00 65.17 ? 161 LEU K CD2 1 ATOM 5736 N N . THR C 3 136 ? 50.104 -67.363 18.104 1.00 64.50 ? 162 THR K N 1 ATOM 5737 C CA . THR C 3 136 ? 48.903 -68.162 17.922 1.00 64.76 ? 162 THR K CA 1 ATOM 5738 C C . THR C 3 136 ? 47.714 -67.670 18.752 1.00 65.14 ? 162 THR K C 1 ATOM 5739 O O . THR C 3 136 ? 46.593 -68.133 18.574 1.00 65.24 ? 162 THR K O 1 ATOM 5740 C CB . THR C 3 136 ? 49.167 -69.645 18.212 1.00 65.14 ? 162 THR K CB 1 ATOM 5741 O OG1 . THR C 3 136 ? 49.137 -69.888 19.623 1.00 65.38 ? 162 THR K OG1 1 ATOM 5742 C CG2 . THR C 3 136 ? 50.516 -70.038 17.668 1.00 64.69 ? 162 THR K CG2 1 ATOM 5743 N N . ASN C 3 137 ? 47.946 -66.722 19.648 1.00 84.85 ? 163 ASN K N 1 ATOM 5744 C CA . ASN C 3 137 ? 46.851 -66.188 20.440 1.00 85.19 ? 163 ASN K CA 1 ATOM 5745 C C . ASN C 3 137 ? 46.119 -65.037 19.751 1.00 84.90 ? 163 ASN K C 1 ATOM 5746 O O . ASN C 3 137 ? 45.178 -64.478 20.315 1.00 85.19 ? 163 ASN K O 1 ATOM 5747 C CB . ASN C 3 137 ? 47.335 -65.776 21.833 1.00 85.60 ? 163 ASN K CB 1 ATOM 5748 C CG . ASN C 3 137 ? 47.754 -66.964 22.677 1.00 86.07 ? 163 ASN K CG 1 ATOM 5749 O OD1 . ASN C 3 137 ? 48.935 -67.177 22.913 1.00 85.91 ? 163 ASN K OD1 1 ATOM 5750 N ND2 . ASN C 3 137 ? 46.784 -67.735 23.148 1.00 86.59 ? 163 ASN K ND2 1 ATOM 5751 N N . ILE C 3 138 ? 46.556 -64.671 18.547 1.00 67.90 ? 164 ILE K N 1 ATOM 5752 C CA . ILE C 3 138 ? 45.852 -63.648 17.785 1.00 67.53 ? 164 ILE K CA 1 ATOM 5753 C C . ILE C 3 138 ? 44.883 -64.330 16.844 1.00 67.53 ? 164 ILE K C 1 ATOM 5754 O O . ILE C 3 138 ? 45.284 -64.836 15.803 1.00 67.39 ? 164 ILE K O 1 ATOM 5755 C CB . ILE C 3 138 ? 46.821 -62.862 16.888 1.00 67.17 ? 164 ILE K CB 1 ATOM 5756 C CG1 . ILE C 3 138 ? 48.163 -62.615 17.594 1.00 67.27 ? 164 ILE K CG1 1 ATOM 5757 C CG2 . ILE C 3 138 ? 46.142 -61.576 16.385 1.00 66.79 ? 164 ILE K CG2 1 ATOM 5758 C CD1 . ILE C 3 138 ? 49.275 -62.125 16.692 1.00 66.91 ? 164 ILE K CD1 1 ATOM 5759 N N . MET C 3 139 ? 43.598 -64.278 17.160 1.00 94.51 ? 165 MET K N 1 ATOM 5760 C CA . MET C 3 139 ? 42.635 -65.068 16.411 1.00 94.54 ? 165 MET K CA 1 ATOM 5761 C C . MET C 3 139 ? 42.031 -64.194 15.344 1.00 94.23 ? 165 MET K C 1 ATOM 5762 O O . MET C 3 139 ? 41.181 -64.623 14.564 1.00 94.20 ? 165 MET K O 1 ATOM 5763 C CB . MET C 3 139 ? 41.546 -65.626 17.325 1.00 95.29 ? 165 MET K CB 1 ATOM 5764 C CG . MET C 3 139 ? 41.985 -65.892 18.749 1.00 95.54 ? 165 MET K CG 1 ATOM 5765 S SD . MET C 3 139 ? 40.970 -64.948 19.904 1.00 95.68 ? 165 MET K SD 1 ATOM 5766 C CE . MET C 3 139 ? 41.546 -63.264 19.621 1.00 95.17 ? 165 MET K CE 1 ATOM 5767 N N . THR C 3 140 ? 42.472 -62.949 15.325 1.00 65.94 ? 166 THR K N 1 ATOM 5768 C CA . THR C 3 140 ? 42.065 -62.050 14.269 1.00 65.71 ? 166 THR K CA 1 ATOM 5769 C C . THR C 3 140 ? 43.009 -62.186 13.064 1.00 65.24 ? 166 THR K C 1 ATOM 5770 O O . THR C 3 140 ? 42.722 -61.682 11.970 1.00 65.04 ? 166 THR K O 1 ATOM 5771 C CB . THR C 3 140 ? 41.933 -60.580 14.769 1.00 65.75 ? 166 THR K CB 1 ATOM 5772 O OG1 . THR C 3 140 ? 43.221 -60.033 15.108 1.00 65.33 ? 166 THR K OG1 1 ATOM 5773 C CG2 . THR C 3 140 ? 41.008 -60.525 15.985 1.00 66.53 ? 166 THR K CG2 1 ATOM 5774 N N . LEU C 3 141 ? 44.110 -62.908 13.265 1.00 62.36 ? 167 LEU K N 1 ATOM 5775 C CA . LEU C 3 141 ? 45.092 -63.137 12.203 1.00 62.08 ? 167 LEU K CA 1 ATOM 5776 C C . LEU C 3 141 ? 44.551 -63.929 10.981 1.00 62.12 ? 167 LEU K C 1 ATOM 5777 O O . LEU C 3 141 ? 44.042 -65.054 11.102 1.00 62.33 ? 167 LEU K O 1 ATOM 5778 C CB . LEU C 3 141 ? 46.345 -63.810 12.782 1.00 62.10 ? 167 LEU K CB 1 ATOM 5779 C CG . LEU C 3 141 ? 47.665 -63.771 12.006 1.00 61.49 ? 167 LEU K CG 1 ATOM 5780 C CD1 . LEU C 3 141 ? 48.364 -62.429 12.151 1.00 61.09 ? 167 LEU K CD1 1 ATOM 5781 C CD2 . LEU C 3 141 ? 48.571 -64.895 12.455 1.00 61.51 ? 167 LEU K CD2 1 ATOM 5782 N N . GLN C 3 142 ? 44.712 -63.324 9.806 1.00 61.93 ? 168 GLN K N 1 ATOM 5783 C CA . GLN C 3 142 ? 44.191 -63.820 8.537 1.00 61.91 ? 168 GLN K CA 1 ATOM 5784 C C . GLN C 3 142 ? 45.307 -64.231 7.617 1.00 61.46 ? 168 GLN K C 1 ATOM 5785 O O . GLN C 3 142 ? 45.269 -65.312 7.043 1.00 61.56 ? 168 GLN K O 1 ATOM 5786 C CB . GLN C 3 142 ? 43.368 -62.763 7.837 1.00 61.98 ? 168 GLN K CB 1 ATOM 5787 C CG . GLN C 3 142 ? 41.934 -63.150 7.644 1.00 62.41 ? 168 GLN K CG 1 ATOM 5788 C CD . GLN C 3 142 ? 41.001 -62.149 8.279 1.00 62.72 ? 168 GLN K CD 1 ATOM 5789 O OE1 . GLN C 3 142 ? 40.704 -61.103 7.690 1.00 62.80 ? 168 GLN K OE1 1 ATOM 5790 N NE2 . GLN C 3 142 ? 40.548 -62.449 9.504 1.00 62.90 ? 168 GLN K NE2 1 ATOM 5791 N N . VAL C 3 143 ? 46.221 -63.295 7.367 1.00 62.12 ? 169 VAL K N 1 ATOM 5792 C CA . VAL C 3 143 ? 47.384 -63.537 6.511 1.00 61.18 ? 169 VAL K CA 1 ATOM 5793 C C . VAL C 3 143 ? 48.732 -63.474 7.218 1.00 60.71 ? 169 VAL K C 1 ATOM 5794 O O . VAL C 3 143 ? 49.179 -62.403 7.618 1.00 60.44 ? 169 VAL K O 1 ATOM 5795 C CB . VAL C 3 143 ? 47.472 -62.485 5.435 1.00 60.70 ? 169 VAL K CB 1 ATOM 5796 C CG1 . VAL C 3 143 ? 48.585 -62.843 4.484 1.00 60.04 ? 169 VAL K CG1 1 ATOM 5797 C CG2 . VAL C 3 143 ? 46.160 -62.384 4.711 1.00 61.08 ? 169 VAL K CG2 1 ATOM 5798 N N . LEU C 3 144 ? 49.405 -64.607 7.338 1.00 67.07 ? 170 LEU K N 1 ATOM 5799 C CA . LEU C 3 144 ? 50.729 -64.585 7.923 1.00 66.68 ? 170 LEU K CA 1 ATOM 5800 C C . LEU C 3 144 ? 51.742 -65.028 6.909 1.00 65.73 ? 170 LEU K C 1 ATOM 5801 O O . LEU C 3 144 ? 51.692 -66.162 6.440 1.00 65.78 ? 170 LEU K O 1 ATOM 5802 C CB . LEU C 3 144 ? 50.817 -65.512 9.121 1.00 67.42 ? 170 LEU K CB 1 ATOM 5803 C CG . LEU C 3 144 ? 52.250 -65.678 9.608 1.00 67.25 ? 170 LEU K CG 1 ATOM 5804 C CD1 . LEU C 3 144 ? 52.677 -64.421 10.280 1.00 67.34 ? 170 LEU K CD1 1 ATOM 5805 C CD2 . LEU C 3 144 ? 52.375 -66.835 10.544 1.00 67.95 ? 170 LEU K CD2 1 ATOM 5806 N N . ASP C 3 145 ? 52.662 -64.140 6.552 1.00 63.80 ? 171 ASP K N 1 ATOM 5807 C CA . ASP C 3 145 ? 53.768 -64.584 5.727 1.00 63.23 ? 171 ASP K CA 1 ATOM 5808 C C . ASP C 3 145 ? 55.127 -64.362 6.357 1.00 62.97 ? 171 ASP K C 1 ATOM 5809 O O . ASP C 3 145 ? 55.630 -63.253 6.396 1.00 62.54 ? 171 ASP K O 1 ATOM 5810 C CB . ASP C 3 145 ? 53.727 -63.902 4.381 1.00 62.57 ? 171 ASP K CB 1 ATOM 5811 C CG . ASP C 3 145 ? 54.699 -64.498 3.439 1.00 62.21 ? 171 ASP K CG 1 ATOM 5812 O OD1 . ASP C 3 145 ? 55.218 -65.577 3.748 1.00 62.57 ? 171 ASP K OD1 1 ATOM 5813 O OD2 . ASP C 3 145 ? 54.944 -63.910 2.382 1.00 61.67 ? 171 ASP K OD2 1 ATOM 5814 N N . LEU C 3 146 ? 55.714 -65.459 6.814 1.00 59.90 ? 172 LEU K N 1 ATOM 5815 C CA . LEU C 3 146 ? 57.054 -65.512 7.389 1.00 59.93 ? 172 LEU K CA 1 ATOM 5816 C C . LEU C 3 146 ? 58.108 -66.047 6.413 1.00 60.28 ? 172 LEU K C 1 ATOM 5817 O O . LEU C 3 146 ? 59.240 -66.329 6.811 1.00 60.49 ? 172 LEU K O 1 ATOM 5818 C CB . LEU C 3 146 ? 57.046 -66.327 8.690 1.00 60.33 ? 172 LEU K CB 1 ATOM 5819 C CG . LEU C 3 146 ? 56.139 -65.813 9.814 1.00 60.16 ? 172 LEU K CG 1 ATOM 5820 C CD1 . LEU C 3 146 ? 56.059 -66.799 10.955 1.00 60.71 ? 172 LEU K CD1 1 ATOM 5821 C CD2 . LEU C 3 146 ? 56.629 -64.480 10.313 1.00 59.65 ? 172 LEU K CD2 1 ATOM 5822 N N . SER C 3 147 ? 57.704 -66.259 5.160 1.00 68.98 ? 173 SER K N 1 ATOM 5823 C CA . SER C 3 147 ? 58.517 -66.976 4.166 1.00 68.88 ? 173 SER K CA 1 ATOM 5824 C C . SER C 3 147 ? 59.784 -66.251 3.749 1.00 68.19 ? 173 SER K C 1 ATOM 5825 O O . SER C 3 147 ? 59.865 -65.032 3.830 1.00 67.66 ? 173 SER K O 1 ATOM 5826 C CB . SER C 3 147 ? 57.695 -67.288 2.915 1.00 68.87 ? 173 SER K CB 1 ATOM 5827 O OG . SER C 3 147 ? 57.338 -66.091 2.244 1.00 68.35 ? 173 SER K OG 1 ATOM 5828 N N . ASN C 3 148 ? 60.758 -67.020 3.275 1.00 63.41 ? 174 ASN K N 1 ATOM 5829 C CA . ASN C 3 148 ? 62.061 -66.494 2.876 1.00 63.11 ? 174 ASN K CA 1 ATOM 5830 C C . ASN C 3 148 ? 62.854 -65.797 3.993 1.00 62.84 ? 174 ASN K C 1 ATOM 5831 O O . ASN C 3 148 ? 63.103 -64.596 3.950 1.00 62.17 ? 174 ASN K O 1 ATOM 5832 C CB . ASN C 3 148 ? 61.919 -65.583 1.649 1.00 62.67 ? 174 ASN K CB 1 ATOM 5833 C CG . ASN C 3 148 ? 61.830 -66.364 0.350 1.00 63.24 ? 174 ASN K CG 1 ATOM 5834 O OD1 . ASN C 3 148 ? 62.842 -66.850 -0.153 1.00 64.51 ? 174 ASN K OD1 1 ATOM 5835 N ND2 . ASN C 3 148 ? 60.622 -66.488 -0.200 1.00 62.48 ? 174 ASN K ND2 1 ATOM 5836 N N . ASN C 3 149 ? 63.271 -66.566 4.986 1.00 77.91 ? 175 ASN K N 1 ATOM 5837 C CA . ASN C 3 149 ? 64.071 -66.020 6.067 1.00 77.87 ? 175 ASN K CA 1 ATOM 5838 C C . ASN C 3 149 ? 65.096 -67.027 6.557 1.00 78.58 ? 175 ASN K C 1 ATOM 5839 O O . ASN C 3 149 ? 65.272 -68.091 5.959 1.00 79.03 ? 175 ASN K O 1 ATOM 5840 C CB . ASN C 3 149 ? 63.179 -65.570 7.222 1.00 78.03 ? 175 ASN K CB 1 ATOM 5841 C CG . ASN C 3 149 ? 62.502 -64.237 6.954 1.00 77.31 ? 175 ASN K CG 1 ATOM 5842 O OD1 . ASN C 3 149 ? 63.087 -63.175 7.169 1.00 76.71 ? 175 ASN K OD1 1 ATOM 5843 N ND2 . ASN C 3 149 ? 61.259 -64.285 6.493 1.00 77.41 ? 175 ASN K ND2 1 ATOM 5844 N N . ARG C 3 150 ? 65.780 -66.682 7.637 1.00 78.08 ? 176 ARG K N 1 ATOM 5845 C CA . ARG C 3 150 ? 66.758 -67.571 8.222 1.00 78.84 ? 176 ARG K CA 1 ATOM 5846 C C . ARG C 3 150 ? 66.152 -68.400 9.346 1.00 79.84 ? 176 ARG K C 1 ATOM 5847 O O . ARG C 3 150 ? 66.858 -69.151 10.003 1.00 80.64 ? 176 ARG K O 1 ATOM 5848 C CB . ARG C 3 150 ? 67.967 -66.779 8.714 1.00 78.41 ? 176 ARG K CB 1 ATOM 5849 C CG . ARG C 3 150 ? 69.123 -66.709 7.716 1.00 78.00 ? 176 ARG K CG 1 ATOM 5850 C CD . ARG C 3 150 ? 70.291 -67.559 8.204 1.00 78.70 ? 176 ARG K CD 1 ATOM 5851 N NE . ARG C 3 150 ? 71.373 -67.704 7.227 1.00 78.39 ? 176 ARG K NE 1 ATOM 5852 C CZ . ARG C 3 150 ? 71.507 -68.724 6.371 1.00 78.70 ? 176 ARG K CZ 1 ATOM 5853 N NH1 . ARG C 3 150 ? 70.611 -69.716 6.331 1.00 79.37 ? 176 ARG K NH1 1 ATOM 5854 N NH2 . ARG C 3 150 ? 72.545 -68.753 5.539 1.00 78.34 ? 176 ARG K NH2 1 ATOM 5855 N N . LEU C 3 151 ? 64.840 -68.282 9.541 1.00 63.65 ? 177 LEU K N 1 ATOM 5856 C CA . LEU C 3 151 ? 64.167 -68.799 10.740 1.00 64.31 ? 177 LEU K CA 1 ATOM 5857 C C . LEU C 3 151 ? 64.511 -70.231 11.070 1.00 65.47 ? 177 LEU K C 1 ATOM 5858 O O . LEU C 3 151 ? 64.463 -71.116 10.210 1.00 65.84 ? 177 LEU K O 1 ATOM 5859 C CB . LEU C 3 151 ? 62.643 -68.683 10.627 1.00 64.17 ? 177 LEU K CB 1 ATOM 5860 C CG . LEU C 3 151 ? 62.073 -67.271 10.729 1.00 63.19 ? 177 LEU K CG 1 ATOM 5861 C CD1 . LEU C 3 151 ? 60.588 -67.306 11.014 1.00 63.32 ? 177 LEU K CD1 1 ATOM 5862 C CD2 . LEU C 3 151 ? 62.818 -66.474 11.794 1.00 63.06 ? 177 LEU K CD2 1 ATOM 5863 N N . SER C 3 152 ? 64.882 -70.434 12.333 1.00 80.74 ? 178 SER K N 1 ATOM 5864 C CA . SER C 3 152 ? 65.144 -71.760 12.873 1.00 81.92 ? 178 SER K CA 1 ATOM 5865 C C . SER C 3 152 ? 63.977 -72.107 13.771 1.00 82.50 ? 178 SER K C 1 ATOM 5866 O O . SER C 3 152 ? 63.425 -71.243 14.438 1.00 82.21 ? 178 SER K O 1 ATOM 5867 C CB . SER C 3 152 ? 66.451 -71.793 13.680 1.00 82.33 ? 178 SER K CB 1 ATOM 5868 O OG . SER C 3 152 ? 67.559 -71.302 12.939 1.00 81.92 ? 178 SER K OG 1 ATOM 5869 N N . GLY C 3 153 ? 63.561 -73.357 13.776 1.00 70.02 ? 179 GLY K N 1 ATOM 5870 C CA . GLY C 3 153 ? 62.526 -73.694 14.717 1.00 70.36 ? 179 GLY K CA 1 ATOM 5871 C C . GLY C 3 153 ? 61.529 -74.753 14.329 1.00 70.81 ? 179 GLY K C 1 ATOM 5872 O O . GLY C 3 153 ? 61.763 -75.617 13.485 1.00 71.20 ? 179 GLY K O 1 ATOM 5873 N N . SER C 3 154 ? 60.397 -74.678 15.002 1.00 72.92 ? 180 SER K N 1 ATOM 5874 C CA . SER C 3 154 ? 59.320 -75.586 14.767 1.00 73.31 ? 180 SER K CA 1 ATOM 5875 C C . SER C 3 154 ? 58.112 -74.736 14.564 1.00 72.79 ? 180 SER K C 1 ATOM 5876 O O . SER C 3 154 ? 57.919 -73.759 15.263 1.00 72.66 ? 180 SER K O 1 ATOM 5877 C CB . SER C 3 154 ? 59.113 -76.480 15.975 1.00 74.03 ? 180 SER K CB 1 ATOM 5878 O OG . SER C 3 154 ? 57.969 -77.288 15.788 1.00 73.42 ? 180 SER K OG 1 ATOM 5879 N N . VAL C 3 155 ? 57.287 -75.105 13.608 1.00 69.79 ? 181 VAL K N 1 ATOM 5880 C CA . VAL C 3 155 ? 56.158 -74.271 13.282 1.00 69.26 ? 181 VAL K CA 1 ATOM 5881 C C . VAL C 3 155 ? 54.911 -74.710 14.006 1.00 69.80 ? 181 VAL K C 1 ATOM 5882 O O . VAL C 3 155 ? 54.510 -75.862 13.907 1.00 70.33 ? 181 VAL K O 1 ATOM 5883 C CB . VAL C 3 155 ? 55.882 -74.285 11.785 1.00 68.79 ? 181 VAL K CB 1 ATOM 5884 C CG1 . VAL C 3 155 ? 54.643 -73.457 11.470 1.00 68.36 ? 181 VAL K CG1 1 ATOM 5885 C CG2 . VAL C 3 155 ? 57.099 -73.767 11.027 1.00 68.26 ? 181 VAL K CG2 1 ATOM 5886 N N . PRO C 3 156 ? 54.286 -73.777 14.730 1.00 67.32 ? 182 PRO K N 1 ATOM 5887 C CA . PRO C 3 156 ? 52.984 -73.968 15.374 1.00 67.75 ? 182 PRO K CA 1 ATOM 5888 C C . PRO C 3 156 ? 51.854 -74.298 14.395 1.00 67.62 ? 182 PRO K C 1 ATOM 5889 O O . PRO C 3 156 ? 51.717 -73.667 13.341 1.00 66.98 ? 182 PRO K O 1 ATOM 5890 C CB . PRO C 3 156 ? 52.716 -72.609 16.037 1.00 67.59 ? 182 PRO K CB 1 ATOM 5891 C CG . PRO C 3 156 ? 53.643 -71.664 15.394 1.00 66.90 ? 182 PRO K CG 1 ATOM 5892 C CD . PRO C 3 156 ? 54.845 -72.449 15.016 1.00 66.84 ? 182 PRO K CD 1 ATOM 5893 N N . ASP C 3 157 ? 51.089 -75.338 14.709 1.00 87.69 ? 183 ASP K N 1 ATOM 5894 C CA . ASP C 3 157 ? 49.809 -75.556 14.043 1.00 87.67 ? 183 ASP K CA 1 ATOM 5895 C C . ASP C 3 157 ? 48.542 -75.166 14.824 1.00 88.11 ? 183 ASP K C 1 ATOM 5896 O O . ASP C 3 157 ? 47.449 -75.219 14.260 1.00 88.07 ? 183 ASP K O 1 ATOM 5897 C CB . ASP C 3 157 ? 49.700 -76.992 13.521 1.00 87.87 ? 183 ASP K CB 1 ATOM 5898 C CG . ASP C 3 157 ? 50.511 -77.975 14.339 1.00 88.41 ? 183 ASP K CG 1 ATOM 5899 O OD1 . ASP C 3 157 ? 51.462 -77.535 15.027 1.00 88.46 ? 183 ASP K OD1 1 ATOM 5900 O OD2 . ASP C 3 157 ? 50.201 -79.188 14.283 1.00 88.79 ? 183 ASP K OD2 1 ATOM 5901 N N . ASN C 3 158 ? 48.671 -74.758 16.092 1.00 87.67 ? 184 ASN K N 1 ATOM 5902 C CA . ASN C 3 158 ? 47.470 -74.449 16.885 1.00 88.11 ? 184 ASN K CA 1 ATOM 5903 C C . ASN C 3 158 ? 47.062 -72.984 16.833 1.00 87.93 ? 184 ASN K C 1 ATOM 5904 O O . ASN C 3 158 ? 47.773 -72.151 16.284 1.00 87.40 ? 184 ASN K O 1 ATOM 5905 C CB . ASN C 3 158 ? 47.546 -74.973 18.344 1.00 88.79 ? 184 ASN K CB 1 ATOM 5906 C CG . ASN C 3 158 ? 48.689 -74.350 19.170 1.00 88.91 ? 184 ASN K CG 1 ATOM 5907 O OD1 . ASN C 3 158 ? 49.338 -73.402 18.730 1.00 88.29 ? 184 ASN K OD1 1 ATOM 5908 N ND2 . ASN C 3 158 ? 48.941 -74.918 20.379 1.00 89.65 ? 184 ASN K ND2 1 ATOM 5909 N N . GLY C 3 159 ? 45.920 -72.671 17.425 1.00 72.77 ? 185 GLY K N 1 ATOM 5910 C CA . GLY C 3 159 ? 45.385 -71.325 17.352 1.00 72.65 ? 185 GLY K CA 1 ATOM 5911 C C . GLY C 3 159 ? 45.134 -70.855 15.934 1.00 72.12 ? 185 GLY K C 1 ATOM 5912 O O . GLY C 3 159 ? 44.643 -71.606 15.096 1.00 71.97 ? 185 GLY K O 1 ATOM 5913 N N . SER C 3 160 ? 45.479 -69.605 15.660 1.00 64.08 ? 186 SER K N 1 ATOM 5914 C CA . SER C 3 160 ? 45.270 -69.020 14.341 1.00 63.65 ? 186 SER K CA 1 ATOM 5915 C C . SER C 3 160 ? 46.056 -69.763 13.278 1.00 63.52 ? 186 SER K C 1 ATOM 5916 O O . SER C 3 160 ? 45.596 -69.950 12.144 1.00 63.42 ? 186 SER K O 1 ATOM 5917 C CB . SER C 3 160 ? 45.702 -67.566 14.362 1.00 63.22 ? 186 SER K CB 1 ATOM 5918 O OG . SER C 3 160 ? 46.786 -67.388 15.257 1.00 63.14 ? 186 SER K OG 1 ATOM 5919 N N . PHE C 3 161 ? 47.228 -70.231 13.678 1.00 68.17 ? 187 PHE K N 1 ATOM 5920 C CA . PHE C 3 161 ? 48.093 -71.020 12.824 1.00 67.65 ? 187 PHE K CA 1 ATOM 5921 C C . PHE C 3 161 ? 47.435 -72.319 12.307 1.00 67.79 ? 187 PHE K C 1 ATOM 5922 O O . PHE C 3 161 ? 48.010 -73.005 11.442 1.00 67.46 ? 187 PHE K O 1 ATOM 5923 C CB . PHE C 3 161 ? 49.388 -71.332 13.562 1.00 67.63 ? 187 PHE K CB 1 ATOM 5924 C CG . PHE C 3 161 ? 50.328 -70.186 13.626 1.00 67.12 ? 187 PHE K CG 1 ATOM 5925 C CD1 . PHE C 3 161 ? 49.952 -69.006 14.228 1.00 67.35 ? 187 PHE K CD1 1 ATOM 5926 C CD2 . PHE C 3 161 ? 51.593 -70.286 13.079 1.00 66.41 ? 187 PHE K CD2 1 ATOM 5927 C CE1 . PHE C 3 161 ? 50.816 -67.941 14.289 1.00 66.85 ? 187 PHE K CE1 1 ATOM 5928 C CE2 . PHE C 3 161 ? 52.466 -69.231 13.136 1.00 65.82 ? 187 PHE K CE2 1 ATOM 5929 C CZ . PHE C 3 161 ? 52.073 -68.050 13.747 1.00 65.99 ? 187 PHE K CZ 1 ATOM 5930 N N . SER C 3 162 ? 46.259 -72.669 12.847 1.00 71.71 ? 188 SER K N 1 ATOM 5931 C CA . SER C 3 162 ? 45.428 -73.725 12.262 1.00 71.78 ? 188 SER K CA 1 ATOM 5932 C C . SER C 3 162 ? 45.235 -73.516 10.755 1.00 71.13 ? 188 SER K C 1 ATOM 5933 O O . SER C 3 162 ? 45.391 -74.459 9.965 1.00 70.90 ? 188 SER K O 1 ATOM 5934 C CB . SER C 3 162 ? 44.062 -73.790 12.955 1.00 72.30 ? 188 SER K CB 1 ATOM 5935 O OG . SER C 3 162 ? 43.256 -72.675 12.614 1.00 72.09 ? 188 SER K OG 1 ATOM 5936 N N . LEU C 3 163 ? 44.944 -72.277 10.349 1.00 83.77 ? 189 LEU K N 1 ATOM 5937 C CA . LEU C 3 163 ? 44.549 -72.028 8.957 1.00 83.19 ? 189 LEU K CA 1 ATOM 5938 C C . LEU C 3 163 ? 45.687 -71.868 7.934 1.00 82.35 ? 189 LEU K C 1 ATOM 5939 O O . LEU C 3 163 ? 45.430 -71.670 6.755 1.00 81.66 ? 189 LEU K O 1 ATOM 5940 C CB . LEU C 3 163 ? 43.565 -70.847 8.867 1.00 83.21 ? 189 LEU K CB 1 ATOM 5941 C CG . LEU C 3 163 ? 43.967 -69.396 9.137 1.00 83.36 ? 189 LEU K CG 1 ATOM 5942 C CD1 . LEU C 3 163 ? 43.603 -68.514 7.948 1.00 83.16 ? 189 LEU K CD1 1 ATOM 5943 C CD2 . LEU C 3 163 ? 43.289 -68.881 10.398 1.00 83.80 ? 189 LEU K CD2 1 ATOM 5944 N N . PHE C 3 164 ? 46.937 -71.985 8.358 1.00 66.67 ? 190 PHE K N 1 ATOM 5945 C CA . PHE C 3 164 ? 48.036 -71.582 7.480 1.00 65.82 ? 190 PHE K CA 1 ATOM 5946 C C . PHE C 3 164 ? 48.722 -72.675 6.652 1.00 65.69 ? 190 PHE K C 1 ATOM 5947 O O . PHE C 3 164 ? 49.366 -73.568 7.190 1.00 66.18 ? 190 PHE K O 1 ATOM 5948 C CB . PHE C 3 164 ? 49.089 -70.809 8.276 1.00 65.62 ? 190 PHE K CB 1 ATOM 5949 C CG . PHE C 3 164 ? 48.578 -69.537 8.872 1.00 65.81 ? 190 PHE K CG 1 ATOM 5950 C CD1 . PHE C 3 164 ? 47.480 -68.900 8.337 1.00 65.56 ? 190 PHE K CD1 1 ATOM 5951 C CD2 . PHE C 3 164 ? 49.193 -68.977 9.964 1.00 66.30 ? 190 PHE K CD2 1 ATOM 5952 C CE1 . PHE C 3 164 ? 47.005 -67.724 8.884 1.00 65.88 ? 190 PHE K CE1 1 ATOM 5953 C CE2 . PHE C 3 164 ? 48.715 -67.807 10.515 1.00 66.58 ? 190 PHE K CE2 1 ATOM 5954 C CZ . PHE C 3 164 ? 47.621 -67.179 9.972 1.00 66.41 ? 190 PHE K CZ 1 ATOM 5955 N N . THR C 3 165 ? 48.611 -72.569 5.333 1.00 71.98 ? 191 THR K N 1 ATOM 5956 C CA . THR C 3 165 ? 49.346 -73.443 4.427 1.00 71.80 ? 191 THR K CA 1 ATOM 5957 C C . THR C 3 165 ? 50.828 -73.072 4.468 1.00 71.17 ? 191 THR K C 1 ATOM 5958 O O . THR C 3 165 ? 51.163 -71.946 4.838 1.00 70.55 ? 191 THR K O 1 ATOM 5959 C CB . THR C 3 165 ? 48.849 -73.279 2.976 1.00 71.45 ? 191 THR K CB 1 ATOM 5960 O OG1 . THR C 3 165 ? 49.096 -71.934 2.540 1.00 70.35 ? 191 THR K OG1 1 ATOM 5961 C CG2 . THR C 3 165 ? 47.363 -73.605 2.868 1.00 72.12 ? 191 THR K CG2 1 ATOM 5962 N N . PRO C 3 166 ? 51.714 -74.012 4.070 1.00 63.82 ? 192 PRO K N 1 ATOM 5963 C CA . PRO C 3 166 ? 53.176 -73.870 4.035 1.00 63.91 ? 192 PRO K CA 1 ATOM 5964 C C . PRO C 3 166 ? 53.694 -72.678 3.263 1.00 63.37 ? 192 PRO K C 1 ATOM 5965 O O . PRO C 3 166 ? 54.833 -72.272 3.479 1.00 63.35 ? 192 PRO K O 1 ATOM 5966 C CB . PRO C 3 166 ? 53.638 -75.151 3.325 1.00 64.74 ? 192 PRO K CB 1 ATOM 5967 C CG . PRO C 3 166 ? 52.421 -75.720 2.715 1.00 64.90 ? 192 PRO K CG 1 ATOM 5968 C CD . PRO C 3 166 ? 51.338 -75.373 3.670 1.00 64.51 ? 192 PRO K CD 1 ATOM 5969 N N . ILE C 3 167 ? 52.884 -72.127 2.372 1.00 63.88 ? 193 ILE K N 1 ATOM 5970 C CA . ILE C 3 167 ? 53.358 -71.041 1.535 1.00 63.19 ? 193 ILE K CA 1 ATOM 5971 C C . ILE C 3 167 ? 53.668 -69.849 2.440 1.00 62.84 ? 193 ILE K C 1 ATOM 5972 O O . ILE C 3 167 ? 54.406 -68.938 2.064 1.00 62.25 ? 193 ILE K O 1 ATOM 5973 C CB . ILE C 3 167 ? 52.356 -70.710 0.392 1.00 62.95 ? 193 ILE K CB 1 ATOM 5974 C CG1 . ILE C 3 167 ? 53.063 -69.981 -0.761 1.00 62.74 ? 193 ILE K CG1 1 ATOM 5975 C CG2 . ILE C 3 167 ? 51.136 -69.963 0.924 1.00 62.93 ? 193 ILE K CG2 1 ATOM 5976 C CD1 . ILE C 3 167 ? 52.133 -69.521 -1.918 1.00 62.59 ? 193 ILE K CD1 1 ATOM 5977 N N . SER C 3 168 ? 53.130 -69.899 3.660 1.00 64.58 ? 194 SER K N 1 ATOM 5978 C CA . SER C 3 168 ? 53.354 -68.874 4.681 1.00 64.44 ? 194 SER K CA 1 ATOM 5979 C C . SER C 3 168 ? 54.771 -68.951 5.250 1.00 64.41 ? 194 SER K C 1 ATOM 5980 O O . SER C 3 168 ? 55.425 -67.941 5.435 1.00 63.90 ? 194 SER K O 1 ATOM 5981 C CB . SER C 3 168 ? 52.337 -69.030 5.823 1.00 65.25 ? 194 SER K CB 1 ATOM 5982 O OG . SER C 3 168 ? 50.993 -69.075 5.360 1.00 65.39 ? 194 SER K OG 1 ATOM 5983 N N . PHE C 3 169 ? 55.213 -70.156 5.576 1.00 68.35 ? 195 PHE K N 1 ATOM 5984 C CA . PHE C 3 169 ? 56.504 -70.380 6.219 1.00 68.48 ? 195 PHE K CA 1 ATOM 5985 C C . PHE C 3 169 ? 57.634 -70.837 5.290 1.00 68.27 ? 195 PHE K C 1 ATOM 5986 O O . PHE C 3 169 ? 58.702 -71.231 5.766 1.00 68.57 ? 195 PHE K O 1 ATOM 5987 C CB . PHE C 3 169 ? 56.348 -71.341 7.398 1.00 69.44 ? 195 PHE K CB 1 ATOM 5988 C CG . PHE C 3 169 ? 55.077 -71.143 8.159 1.00 69.87 ? 195 PHE K CG 1 ATOM 5989 C CD1 . PHE C 3 169 ? 54.971 -70.144 9.097 1.00 69.90 ? 195 PHE K CD1 1 ATOM 5990 C CD2 . PHE C 3 169 ? 53.985 -71.941 7.920 1.00 70.31 ? 195 PHE K CD2 1 ATOM 5991 C CE1 . PHE C 3 169 ? 53.801 -69.959 9.796 1.00 70.44 ? 195 PHE K CE1 1 ATOM 5992 C CE2 . PHE C 3 169 ? 52.822 -71.752 8.603 1.00 70.78 ? 195 PHE K CE2 1 ATOM 5993 C CZ . PHE C 3 169 ? 52.728 -70.761 9.546 1.00 70.89 ? 195 PHE K CZ 1 ATOM 5994 N N . ALA C 3 170 ? 57.389 -70.849 3.981 1.00 65.37 ? 196 ALA K N 1 ATOM 5995 C CA . ALA C 3 170 ? 58.312 -71.514 3.039 1.00 65.44 ? 196 ALA K CA 1 ATOM 5996 C C . ALA C 3 170 ? 59.746 -70.957 2.901 1.00 65.02 ? 196 ALA K C 1 ATOM 5997 O O . ALA C 3 170 ? 59.980 -69.754 3.023 1.00 64.33 ? 196 ALA K O 1 ATOM 5998 C CB . ALA C 3 170 ? 57.657 -71.674 1.653 1.00 65.20 ? 196 ALA K CB 1 ATOM 5999 N N . ASN C 3 171 ? 60.683 -71.857 2.604 1.00 81.48 ? 197 ASN K N 1 ATOM 6000 C CA . ASN C 3 171 ? 62.081 -71.502 2.371 1.00 81.11 ? 197 ASN K CA 1 ATOM 6001 C C . ASN C 3 171 ? 62.836 -70.856 3.537 1.00 80.92 ? 197 ASN K C 1 ATOM 6002 O O . ASN C 3 171 ? 63.132 -69.662 3.528 1.00 80.05 ? 197 ASN K O 1 ATOM 6003 C CB . ASN C 3 171 ? 62.206 -70.628 1.130 1.00 80.17 ? 197 ASN K CB 1 ATOM 6004 C CG . ASN C 3 171 ? 63.634 -70.282 0.821 1.00 79.86 ? 197 ASN K CG 1 ATOM 6005 O OD1 . ASN C 3 171 ? 64.082 -69.164 1.083 1.00 79.23 ? 197 ASN K OD1 1 ATOM 6006 N ND2 . ASN C 3 171 ? 64.378 -71.253 0.291 1.00 80.31 ? 197 ASN K ND2 1 ATOM 6007 N N . ASN C 3 172 ? 63.139 -71.658 4.549 1.00 94.59 ? 198 ASN K N 1 ATOM 6008 C CA . ASN C 3 172 ? 63.937 -71.189 5.668 1.00 94.64 ? 198 ASN K CA 1 ATOM 6009 C C . ASN C 3 172 ? 65.101 -72.103 5.989 1.00 95.40 ? 198 ASN K C 1 ATOM 6010 O O . ASN C 3 172 ? 65.379 -73.083 5.289 1.00 95.81 ? 198 ASN K O 1 ATOM 6011 C CB . ASN C 3 172 ? 63.078 -71.043 6.922 1.00 94.97 ? 198 ASN K CB 1 ATOM 6012 C CG . ASN C 3 172 ? 62.163 -69.843 6.865 1.00 94.16 ? 198 ASN K CG 1 ATOM 6013 O OD1 . ASN C 3 172 ? 62.431 -68.807 7.472 1.00 93.70 ? 198 ASN K OD1 1 ATOM 6014 N ND2 . ASN C 3 172 ? 61.071 -69.976 6.131 1.00 94.00 ? 198 ASN K ND2 1 ATOM 6015 N N . LEU C 3 173 ? 65.741 -71.784 7.105 1.00 92.69 ? 199 LEU K N 1 ATOM 6016 C CA . LEU C 3 173 ? 66.761 -72.620 7.712 1.00 93.51 ? 199 LEU K CA 1 ATOM 6017 C C . LEU C 3 173 ? 65.993 -73.787 8.317 1.00 94.55 ? 199 LEU K C 1 ATOM 6018 O O . LEU C 3 173 ? 64.849 -74.039 7.931 1.00 94.44 ? 199 LEU K O 1 ATOM 6019 C CB . LEU C 3 173 ? 67.499 -71.835 8.793 1.00 93.43 ? 199 LEU K CB 1 ATOM 6020 C CG . LEU C 3 173 ? 68.899 -72.271 9.209 1.00 93.83 ? 199 LEU K CG 1 ATOM 6021 C CD1 . LEU C 3 173 ? 69.846 -72.205 8.034 1.00 93.40 ? 199 LEU K CD1 1 ATOM 6022 C CD2 . LEU C 3 173 ? 69.379 -71.387 10.324 1.00 93.95 ? 199 LEU K CD2 1 ATOM 6023 N N . ASP C 3 174 ? 66.619 -74.558 9.194 1.00 100.20 ? 200 ASP K N 1 ATOM 6024 C CA . ASP C 3 174 ? 65.866 -75.637 9.794 1.00 101.31 ? 200 ASP K CA 1 ATOM 6025 C C . ASP C 3 174 ? 64.583 -75.095 10.443 1.00 100.99 ? 200 ASP K C 1 ATOM 6026 O O . ASP C 3 174 ? 64.620 -74.236 11.309 1.00 100.63 ? 200 ASP K O 1 ATOM 6027 C CB . ASP C 3 174 ? 66.717 -76.387 10.822 1.00 102.40 ? 200 ASP K CB 1 ATOM 6028 C CG . ASP C 3 174 ? 66.097 -77.724 11.235 1.00 103.38 ? 200 ASP K CG 1 ATOM 6029 O OD1 . ASP C 3 174 ? 65.259 -77.733 12.168 1.00 103.05 ? 200 ASP K OD1 1 ATOM 6030 O OD2 . ASP C 3 174 ? 66.446 -78.766 10.626 1.00 104.37 ? 200 ASP K OD2 1 ATOM 6031 N N . LEU C 3 175 ? 63.453 -75.618 9.980 1.00 77.41 ? 201 LEU K N 1 ATOM 6032 C CA . LEU C 3 175 ? 62.131 -75.346 10.523 1.00 77.25 ? 201 LEU K CA 1 ATOM 6033 C C . LEU C 3 175 ? 61.421 -76.698 10.506 1.00 78.08 ? 201 LEU K C 1 ATOM 6034 O O . LEU C 3 175 ? 61.444 -77.391 9.495 1.00 78.26 ? 201 LEU K O 1 ATOM 6035 C CB . LEU C 3 175 ? 61.362 -74.338 9.649 1.00 76.20 ? 201 LEU K CB 1 ATOM 6036 C CG . LEU C 3 175 ? 61.069 -72.888 10.086 1.00 75.32 ? 201 LEU K CG 1 ATOM 6037 C CD1 . LEU C 3 175 ? 59.941 -72.288 9.266 1.00 74.56 ? 201 LEU K CD1 1 ATOM 6038 C CD2 . LEU C 3 175 ? 60.732 -72.782 11.554 1.00 75.88 ? 201 LEU K CD2 1 ATOM 6039 N N . CYS C 3 176 ? 60.801 -77.095 11.609 1.00 98.48 ? 202 CYS K N 1 ATOM 6040 C CA . CYS C 3 176 ? 60.172 -78.409 11.637 1.00 99.21 ? 202 CYS K CA 1 ATOM 6041 C C . CYS C 3 176 ? 58.688 -78.360 11.989 1.00 99.15 ? 202 CYS K C 1 ATOM 6042 O O . CYS C 3 176 ? 58.268 -77.558 12.808 1.00 98.95 ? 202 CYS K O 1 ATOM 6043 C CB . CYS C 3 176 ? 60.931 -79.349 12.579 1.00 99.92 ? 202 CYS K CB 1 ATOM 6044 S SG . CYS C 3 176 ? 60.441 -79.280 14.308 1.00 100.02 ? 202 CYS K SG 1 ATOM 6045 N N . GLY C 3 177 ? 57.885 -79.201 11.349 1.00 99.06 ? 203 GLY K N 1 ATOM 6046 C CA . GLY C 3 177 ? 56.478 -79.297 11.707 1.00 99.12 ? 203 GLY K CA 1 ATOM 6047 C C . GLY C 3 177 ? 55.573 -79.942 10.668 1.00 99.10 ? 203 GLY K C 1 ATOM 6048 O O . GLY C 3 177 ? 55.988 -80.162 9.534 1.00 98.89 ? 203 GLY K O 1 ATOM 6049 N N . PRO C 3 178 ? 54.329 -80.261 11.060 1.00 104.48 ? 204 PRO K N 1 ATOM 6050 C CA . PRO C 3 178 ? 53.263 -80.778 10.194 1.00 104.41 ? 204 PRO K CA 1 ATOM 6051 C C . PRO C 3 178 ? 52.711 -79.688 9.287 1.00 103.46 ? 204 PRO K C 1 ATOM 6052 O O . PRO C 3 178 ? 52.077 -79.984 8.272 1.00 103.06 ? 204 PRO K O 1 ATOM 6053 C CB . PRO C 3 178 ? 52.193 -81.202 11.189 1.00 104.98 ? 204 PRO K CB 1 ATOM 6054 C CG . PRO C 3 178 ? 52.360 -80.255 12.305 1.00 104.93 ? 204 PRO K CG 1 ATOM 6055 C CD . PRO C 3 178 ? 53.842 -80.027 12.429 1.00 104.85 ? 204 PRO K CD 1 ATOM 6056 N N . VAL C 3 179 ? 52.932 -78.435 9.681 1.00 99.88 ? 205 VAL K N 1 ATOM 6057 C CA . VAL C 3 179 ? 52.590 -77.279 8.864 1.00 98.96 ? 205 VAL K CA 1 ATOM 6058 C C . VAL C 3 179 ? 53.605 -77.189 7.733 1.00 98.46 ? 205 VAL K C 1 ATOM 6059 O O . VAL C 3 179 ? 53.415 -76.461 6.767 1.00 97.56 ? 205 VAL K O 1 ATOM 6060 C CB . VAL C 3 179 ? 52.611 -75.979 9.700 1.00 98.68 ? 205 VAL K CB 1 ATOM 6061 N N . THR C 3 180 ? 54.671 -77.973 7.873 1.00 87.26 ? 206 THR K N 1 ATOM 6062 C CA . THR C 3 180 ? 55.811 -78.004 6.965 1.00 87.01 ? 206 THR K CA 1 ATOM 6063 C C . THR C 3 180 ? 56.088 -79.431 6.484 1.00 87.78 ? 206 THR K C 1 ATOM 6064 O O . THR C 3 180 ? 55.267 -80.331 6.674 1.00 88.35 ? 206 THR K O 1 ATOM 6065 C CB . THR C 3 180 ? 57.080 -77.465 7.647 1.00 86.94 ? 206 THR K CB 1 ATOM 6066 O OG1 . THR C 3 180 ? 57.819 -78.545 8.230 1.00 87.92 ? 206 THR K OG1 1 ATOM 6067 C CG2 . THR C 3 180 ? 56.718 -76.468 8.730 1.00 86.62 ? 206 THR K CG2 1 ATOM 6068 N N . SER C 3 181 ? 57.225 -79.625 5.821 1.00 127.96 ? 207 SER K N 1 ATOM 6069 C CA . SER C 3 181 ? 57.632 -80.949 5.344 1.00 128.78 ? 207 SER K CA 1 ATOM 6070 C C . SER C 3 181 ? 58.243 -81.883 6.406 1.00 129.76 ? 207 SER K C 1 ATOM 6071 O O . SER C 3 181 ? 57.839 -83.042 6.528 1.00 130.46 ? 207 SER K O 1 ATOM 6072 C CB . SER C 3 181 ? 58.613 -80.801 4.179 1.00 128.49 ? 207 SER K CB 1 ATOM 6073 O OG . SER C 3 181 ? 59.785 -80.117 4.587 1.00 128.09 ? 207 SER K OG 1 ATOM 6074 N N . ARG C 3 182 ? 59.202 -81.367 7.175 1.00 114.67 ? 208 ARG K N 1 ATOM 6075 C CA . ARG C 3 182 ? 60.083 -82.203 8.000 1.00 115.72 ? 208 ARG K CA 1 ATOM 6076 C C . ARG C 3 182 ? 59.885 -82.076 9.512 1.00 115.79 ? 208 ARG K C 1 ATOM 6077 O O . ARG C 3 182 ? 60.232 -81.054 10.088 1.00 115.29 ? 208 ARG K O 1 ATOM 6078 C CB . ARG C 3 182 ? 61.548 -81.901 7.654 1.00 115.83 ? 208 ARG K CB 1 ATOM 6079 C CG . ARG C 3 182 ? 61.808 -80.472 7.171 1.00 114.23 ? 208 ARG K CG 1 ATOM 6080 C CD . ARG C 3 182 ? 62.729 -80.466 5.950 1.00 114.15 ? 208 ARG K CD 1 ATOM 6081 N NE . ARG C 3 182 ? 62.249 -81.366 4.895 1.00 114.32 ? 208 ARG K NE 1 ATOM 6082 C CZ . ARG C 3 182 ? 62.960 -81.749 3.833 1.00 114.33 ? 208 ARG K CZ 1 ATOM 6083 N NH1 . ARG C 3 182 ? 64.203 -81.319 3.659 1.00 114.09 ? 208 ARG K NH1 1 ATOM 6084 N NH2 . ARG C 3 182 ? 62.426 -82.572 2.939 1.00 114.35 ? 208 ARG K NH2 1 ATOM 6085 N N . PRO C 3 183 ? 59.338 -83.126 10.153 1.00 105.08 ? 209 PRO K N 1 ATOM 6086 C CA . PRO C 3 183 ? 59.158 -83.235 11.613 1.00 105.19 ? 209 PRO K CA 1 ATOM 6087 C C . PRO C 3 183 ? 60.449 -83.247 12.458 1.00 105.34 ? 209 PRO K C 1 ATOM 6088 O O . PRO C 3 183 ? 61.559 -83.233 11.919 1.00 105.19 ? 209 PRO K O 1 ATOM 6089 C CB . PRO C 3 183 ? 58.407 -84.560 11.768 1.00 105.72 ? 209 PRO K CB 1 ATOM 6090 C CG . PRO C 3 183 ? 57.619 -84.665 10.505 1.00 105.60 ? 209 PRO K CG 1 ATOM 6091 C CD . PRO C 3 183 ? 58.525 -84.121 9.433 1.00 105.43 ? 209 PRO K CD 1 ATOM 6092 N N . CYS C 3 184 ? 60.284 -83.300 13.779 1.00 118.50 ? 210 CYS K N 1 ATOM 6093 C CA . CYS C 3 184 ? 61.361 -82.971 14.710 1.00 118.34 ? 210 CYS K CA 1 ATOM 6094 C C . CYS C 3 184 ? 61.245 -83.772 16.026 1.00 118.72 ? 210 CYS K C 1 ATOM 6095 O O . CYS C 3 184 ? 60.288 -84.536 16.183 1.00 119.40 ? 210 CYS K O 1 ATOM 6096 C CB . CYS C 3 184 ? 61.331 -81.453 14.955 1.00 117.78 ? 210 CYS K CB 1 ATOM 6097 S SG . CYS C 3 184 ? 59.746 -80.770 15.515 1.00 117.65 ? 210 CYS K SG 1 ATOM 6098 N N . PRO C 3 185 ? 62.221 -83.617 16.961 1.00 101.95 ? 211 PRO K N 1 ATOM 6099 C CA . PRO C 3 185 ? 62.233 -84.251 18.294 1.00 102.02 ? 211 PRO K CA 1 ATOM 6100 C C . PRO C 3 185 ? 60.879 -84.485 18.975 1.00 102.11 ? 211 PRO K C 1 ATOM 6101 O O . PRO C 3 185 ? 60.810 -85.352 19.855 1.00 102.91 ? 211 PRO K O 1 ATOM 6102 C CB . PRO C 3 185 ? 63.071 -83.266 19.131 1.00 101.80 ? 211 PRO K CB 1 ATOM 6103 C CG . PRO C 3 185 ? 63.759 -82.336 18.103 1.00 101.22 ? 211 PRO K CG 1 ATOM 6104 C CD . PRO C 3 185 ? 63.511 -82.939 16.751 1.00 101.65 ? 211 PRO K CD 1 HETATM 6105 C C1 . NAG D 4 . ? 64.417 0.633 17.131 1.00 100.26 ? 701 NAG B C1 1 HETATM 6106 C C2 . NAG D 4 . ? 65.002 1.675 18.083 1.00 100.65 ? 701 NAG B C2 1 HETATM 6107 C C3 . NAG D 4 . ? 66.210 2.428 17.531 1.00 101.55 ? 701 NAG B C3 1 HETATM 6108 C C4 . NAG D 4 . ? 67.166 1.550 16.726 1.00 100.52 ? 701 NAG B C4 1 HETATM 6109 C C5 . NAG D 4 . ? 66.454 0.497 15.876 1.00 100.11 ? 701 NAG B C5 1 HETATM 6110 C C6 . NAG D 4 . ? 67.450 -0.577 15.462 1.00 98.58 ? 701 NAG B C6 1 HETATM 6111 C C7 . NAG D 4 . ? 63.358 2.604 19.577 1.00 101.82 ? 701 NAG B C7 1 HETATM 6112 C C8 . NAG D 4 . ? 61.906 2.974 19.569 1.00 103.33 ? 701 NAG B C8 1 HETATM 6113 N N2 . NAG D 4 . ? 63.977 2.640 18.407 1.00 102.38 ? 701 NAG B N2 1 HETATM 6114 O O3 . NAG D 4 . ? 66.927 2.996 18.614 1.00 101.09 ? 701 NAG B O3 1 HETATM 6115 O O4 . NAG D 4 . ? 67.962 2.378 15.891 1.00 102.09 ? 701 NAG B O4 1 HETATM 6116 O O5 . NAG D 4 . ? 65.446 -0.172 16.599 1.00 99.04 ? 701 NAG B O5 1 HETATM 6117 O O6 . NAG D 4 . ? 67.841 -1.303 16.611 1.00 96.44 ? 701 NAG B O6 1 HETATM 6118 O O7 . NAG D 4 . ? 63.924 2.283 20.620 1.00 100.25 ? 701 NAG B O7 1 HETATM 6119 C C1 . NAG E 4 . ? 85.443 -19.543 24.086 1.00 70.41 ? 702 NAG B C1 1 HETATM 6120 C C2 . NAG E 4 . ? 84.550 -18.324 23.826 1.00 70.68 ? 702 NAG B C2 1 HETATM 6121 C C3 . NAG E 4 . ? 83.398 -18.643 22.863 1.00 70.74 ? 702 NAG B C3 1 HETATM 6122 C C4 . NAG E 4 . ? 83.924 -19.314 21.588 1.00 71.15 ? 702 NAG B C4 1 HETATM 6123 C C5 . NAG E 4 . ? 84.717 -20.544 22.004 1.00 70.78 ? 702 NAG B C5 1 HETATM 6124 C C6 . NAG E 4 . ? 85.385 -21.186 20.805 1.00 71.20 ? 702 NAG B C6 1 HETATM 6125 C C7 . NAG E 4 . ? 84.372 -16.585 25.598 1.00 70.43 ? 702 NAG B C7 1 HETATM 6126 C C8 . NAG E 4 . ? 83.249 -15.825 26.259 1.00 70.21 ? 702 NAG B C8 1 HETATM 6127 N N2 . NAG E 4 . ? 84.063 -17.789 25.092 1.00 70.24 ? 702 NAG B N2 1 HETATM 6128 O O3 . NAG E 4 . ? 82.719 -17.449 22.541 1.00 71.08 ? 702 NAG B O3 1 HETATM 6129 O O4 . NAG E 4 . ? 82.927 -19.661 20.625 1.00 71.27 ? 702 NAG B O4 1 HETATM 6130 O O5 . NAG E 4 . ? 85.772 -20.175 22.864 1.00 70.77 ? 702 NAG B O5 1 HETATM 6131 O O6 . NAG E 4 . ? 86.752 -20.819 20.818 1.00 71.49 ? 702 NAG B O6 1 HETATM 6132 O O7 . NAG E 4 . ? 85.502 -16.098 25.551 1.00 70.80 ? 702 NAG B O7 1 HETATM 6133 C C1 . NAG F 4 . ? 49.085 -74.239 21.683 1.00 90.07 ? 301 NAG K C1 1 HETATM 6134 C C2 . NAG F 4 . ? 50.331 -73.873 22.477 1.00 90.53 ? 301 NAG K C2 1 HETATM 6135 C C3 . NAG F 4 . ? 49.961 -72.944 23.608 1.00 90.51 ? 301 NAG K C3 1 HETATM 6136 C C4 . NAG F 4 . ? 49.235 -71.744 23.064 1.00 90.09 ? 301 NAG K C4 1 HETATM 6137 C C5 . NAG F 4 . ? 48.003 -72.229 22.351 1.00 89.92 ? 301 NAG K C5 1 HETATM 6138 C C6 . NAG F 4 . ? 47.201 -71.058 21.845 1.00 89.53 ? 301 NAG K C6 1 HETATM 6139 C C7 . NAG F 4 . ? 50.605 -76.275 23.120 1.00 91.43 ? 301 NAG K C7 1 HETATM 6140 C C8 . NAG F 4 . ? 51.611 -77.354 22.875 1.00 91.83 ? 301 NAG K C8 1 HETATM 6141 N N2 . NAG F 4 . ? 51.058 -75.029 22.985 1.00 90.99 ? 301 NAG K N2 1 HETATM 6142 O O3 . NAG F 4 . ? 51.147 -72.505 24.249 1.00 90.49 ? 301 NAG K O3 1 HETATM 6143 O O4 . NAG F 4 . ? 48.835 -70.916 24.149 1.00 90.22 ? 301 NAG K O4 1 HETATM 6144 O O5 . NAG F 4 . ? 48.378 -73.071 21.275 1.00 89.71 ? 301 NAG K O5 1 HETATM 6145 O O6 . NAG F 4 . ? 45.862 -71.502 21.676 1.00 89.74 ? 301 NAG K O6 1 HETATM 6146 O O7 . NAG F 4 . ? 49.466 -76.543 23.440 1.00 91.52 ? 301 NAG K O7 1 HETATM 6147 C C1 . NAG G 4 . ? 62.333 -63.657 -2.052 1.00 80.51 ? 302 NAG K C1 1 HETATM 6148 C C2 . NAG G 4 . ? 62.490 -63.018 -3.443 1.00 81.50 ? 302 NAG K C2 1 HETATM 6149 C C3 . NAG G 4 . ? 63.095 -63.978 -4.505 1.00 83.10 ? 302 NAG K C3 1 HETATM 6150 C C4 . NAG G 4 . ? 64.458 -64.493 -3.998 1.00 83.78 ? 302 NAG K C4 1 HETATM 6151 C C5 . NAG G 4 . ? 64.081 -65.324 -2.756 1.00 82.83 ? 302 NAG K C5 1 HETATM 6152 C C6 . NAG G 4 . ? 65.288 -66.080 -2.147 1.00 83.54 ? 302 NAG K C6 1 HETATM 6153 C C7 . NAG G 4 . ? 61.103 -61.120 -4.290 1.00 80.88 ? 302 NAG K C7 1 HETATM 6154 C C8 . NAG G 4 . ? 59.766 -60.452 -3.961 1.00 79.76 ? 302 NAG K C8 1 HETATM 6155 N N2 . NAG G 4 . ? 61.207 -62.410 -3.849 1.00 80.90 ? 302 NAG K N2 1 HETATM 6156 O O3 . NAG G 4 . ? 63.184 -63.370 -5.797 1.00 84.11 ? 302 NAG K O3 1 HETATM 6157 O O4 . NAG G 4 . ? 65.258 -65.211 -4.971 1.00 85.50 ? 302 NAG K O4 1 HETATM 6158 O O5 . NAG G 4 . ? 63.426 -64.530 -1.741 1.00 81.27 ? 302 NAG K O5 1 HETATM 6159 O O6 . NAG G 4 . ? 66.287 -65.182 -1.647 1.00 83.44 ? 302 NAG K O6 1 HETATM 6160 O O7 . NAG G 4 . ? 62.020 -60.507 -4.940 1.00 81.82 ? 302 NAG K O7 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . PHE A 1 ? 1.6238 1.4047 1.7188 -0.0587 0.1553 -0.4330 32 PHE B N 2 C CA . PHE A 1 ? 1.5772 1.3440 1.6207 -0.0768 0.1638 -0.4221 32 PHE B CA 3 C C . PHE A 1 ? 1.5838 1.3222 1.5902 -0.0655 0.1488 -0.3927 32 PHE B C 4 O O . PHE A 1 ? 1.6167 1.3483 1.6366 -0.0453 0.1333 -0.3816 32 PHE B O 5 C CB . PHE A 1 ? 1.5843 1.3533 1.6112 -0.0924 0.1789 -0.4297 32 PHE B CB 6 C CG . PHE A 1 ? 1.6374 1.4344 1.6871 -0.1120 0.1982 -0.4592 32 PHE B CG 7 C CD1 . PHE A 1 ? 1.6781 1.4919 1.7435 -0.1218 0.2038 -0.4735 32 PHE B CD1 8 C CD2 . PHE A 1 ? 1.6351 1.4424 1.6901 -0.1214 0.2111 -0.4734 32 PHE B CD2 9 C CE1 . PHE A 1 ? 1.6710 1.5128 1.7577 -0.1410 0.2224 -0.5022 32 PHE B CE1 10 C CE2 . PHE A 1 ? 1.6342 1.4692 1.7101 -0.1405 0.2297 -0.5022 32 PHE B CE2 11 C CZ . PHE A 1 ? 1.6574 1.5104 1.7494 -0.1505 0.2356 -0.5169 32 PHE B CZ 12 N N . SER A 2 ? 1.1371 0.8591 1.0969 -0.0796 0.1530 -0.3808 33 SER B N 13 C CA . SER A 2 ? 1.1404 0.8369 1.0641 -0.0717 0.1398 -0.3557 33 SER B CA 14 C C . SER A 2 ? 1.1409 0.8237 1.0583 -0.0545 0.1293 -0.3399 33 SER B C 15 O O . SER A 2 ? 1.1443 0.8304 1.0657 -0.0562 0.1354 -0.3448 33 SER B O 16 C CB . SER A 2 ? 1.1874 0.8691 1.0641 -0.0923 0.1469 -0.3488 33 SER B CB 17 O OG . SER A 2 ? 1.1753 0.8366 1.0230 -0.0877 0.1349 -0.3300 33 SER B OG 18 N N . PRO A 3 ? 1.0678 0.7357 0.9739 -0.0391 0.1137 -0.3213 34 PRO B N 19 C CA . PRO A 3 ? 1.0419 0.6968 0.9393 -0.0233 0.1028 -0.3051 34 PRO B CA 20 C C . PRO A 3 ? 1.0978 0.7384 0.9589 -0.0321 0.1081 -0.2966 34 PRO B C 21 O O . PRO A 3 ? 1.1233 0.7589 0.9827 -0.0237 0.1047 -0.2897 34 PRO B O 22 C CB . PRO A 3 ? 1.0588 0.7011 0.9420 -0.0121 0.0884 -0.2886 34 PRO B CB 23 C CG . PRO A 3 ? 1.0586 0.7087 0.9512 -0.0187 0.0902 -0.2971 34 PRO B CG 24 C CD . PRO A 3 ? 1.0624 0.7240 0.9573 -0.0387 0.1067 -0.3143 34 PRO B CD 25 N N . GLN A 4 ? 1.1112 0.7441 0.9427 -0.0494 0.1151 -0.2964 35 GLN B N 26 C CA . GLN A 4 ? 1.1407 0.7606 0.9385 -0.0614 0.1209 -0.2907 35 GLN B CA 27 C C . GLN A 4 ? 1.1033 0.7366 0.9192 -0.0666 0.1322 -0.3044 35 GLN B C 28 O O . GLN A 4 ? 1.1158 0.7405 0.9186 -0.0641 0.1317 -0.2972 35 GLN B O 29 C CB . GLN A 4 ? 1.1905 0.8036 0.9597 -0.0833 0.1278 -0.2929 35 GLN B CB 30 C CG . GLN A 4 ? 1.1600 0.7595 0.9111 -0.0806 0.1172 -0.2815 35 GLN B CG 31 C CD . GLN A 4 ? 1.1608 0.7410 0.8919 -0.0645 0.1024 -0.2616 35 GLN B CD 32 O OE1 . GLN A 4 ? 1.2487 0.8122 0.9499 -0.0690 0.1006 -0.2518 35 GLN B OE1 33 N NE2 . GLN A 4 ? 1.1118 0.6947 0.8599 -0.0463 0.0917 -0.2563 35 GLN B NE2 34 N N . LEU A 5 ? 1.1801 0.8353 1.0277 -0.0736 0.1424 -0.3250 36 LEU B N 35 C CA . LEU A 5 ? 1.2016 0.8727 1.0700 -0.0804 0.1548 -0.3422 36 LEU B CA 36 C C . LEU A 5 ? 1.1814 0.8570 1.0797 -0.0604 0.1471 -0.3415 36 LEU B C 37 O O . LEU A 5 ? 1.2157 0.8918 1.1138 -0.0620 0.1522 -0.3444 36 LEU B O 38 C CB . LEU A 5 ? 1.1870 0.8825 1.0832 -0.0940 0.1679 -0.3668 36 LEU B CB 39 C CG . LEU A 5 ? 1.2062 0.9140 1.0975 -0.1173 0.1870 -0.3848 36 LEU B CG 40 C CD1 . LEU A 5 ? 1.2408 0.9764 1.1654 -0.1288 0.1992 -0.4109 36 LEU B CD1 41 C CD2 . LEU A 5 ? 1.2275 0.9379 1.1282 -0.1129 0.1904 -0.3886 36 LEU B CD2 42 N N . LEU A 6 ? 1.3481 1.0262 1.2710 -0.0426 0.1343 -0.3376 37 LEU B N 43 C CA . LEU A 6 ? 1.3561 1.0353 1.3048 -0.0237 0.1238 -0.3341 37 LEU B CA 44 C C . LEU A 6 ? 1.3694 1.0291 1.2857 -0.0182 0.1176 -0.3142 37 LEU B C 45 O O . LEU A 6 ? 1.3775 1.0370 1.3031 -0.0116 0.1160 -0.3134 37 LEU B O 46 C CB . LEU A 6 ? 1.3524 1.0330 1.3235 -0.0076 0.1089 -0.3289 37 LEU B CB 47 C CG . LEU A 6 ? 1.3392 1.0358 1.3375 -0.0113 0.1113 -0.3442 37 LEU B CG 48 C CD1 . LEU A 6 ? 1.3271 1.0209 1.3426 0.0059 0.0939 -0.3351 37 LEU B CD1 49 C CD2 . LEU A 6 ? 1.3043 1.0243 1.3425 -0.0179 0.1228 -0.3709 37 LEU B CD2 50 N N . SER A 7 ? 1.0141 0.6577 0.8932 -0.0213 0.1139 -0.2987 38 SER B N 51 C CA . SER A 7 ? 1.0274 0.6524 0.8742 -0.0162 0.1072 -0.2797 38 SER B CA 52 C C . SER A 7 ? 1.0360 0.6566 0.8639 -0.0279 0.1174 -0.2817 38 SER B C 53 O O . SER A 7 ? 1.0457 0.6617 0.8724 -0.0204 0.1140 -0.2752 38 SER B O 54 C CB . SER A 7 ? 1.0577 0.6675 0.8720 -0.0180 0.1010 -0.2661 38 SER B CB 55 O OG . SER A 7 ? 1.1242 0.7201 0.9202 -0.0055 0.0895 -0.2482 38 SER B OG 56 N N . LEU A 8 ? 1.1105 0.7320 0.9222 -0.0475 0.1294 -0.2903 39 LEU B N 57 C CA . LEU A 8 ? 1.1464 0.7636 0.9374 -0.0620 0.1396 -0.2929 39 LEU B CA 58 C C . LEU A 8 ? 1.1239 0.7568 0.9453 -0.0604 0.1471 -0.3077 39 LEU B C 59 O O . LEU A 8 ? 1.0770 0.7040 0.8872 -0.0616 0.1492 -0.3040 39 LEU B O 60 C CB . LEU A 8 ? 1.1590 0.7763 0.9290 -0.0857 0.1510 -0.3011 39 LEU B CB 61 C CG . LEU A 8 ? 1.1739 0.7704 0.9058 -0.0904 0.1432 -0.2851 39 LEU B CG 62 C CD1 . LEU A 8 ? 1.2147 0.8151 0.9357 -0.1123 0.1528 -0.2953 39 LEU B CD1 63 C CD2 . LEU A 8 ? 1.1589 0.7353 0.8557 -0.0933 0.1394 -0.2708 39 LEU B CD2 64 N N . LEU A 9 ? 1.1860 0.8388 1.0470 -0.0579 0.1507 -0.3250 40 LEU B N 65 C CA . LEU A 9 ? 1.1821 0.8511 1.0779 -0.0554 0.1568 -0.3417 40 LEU B CA 66 C C . LEU A 9 ? 1.1707 0.8324 1.0773 -0.0356 0.1438 -0.3298 40 LEU B C 67 O O . LEU A 9 ? 1.1873 0.8491 1.0964 -0.0358 0.1473 -0.3325 40 LEU B O 68 C CB . LEU A 9 ? 1.1408 0.8325 1.0797 -0.0552 0.1610 -0.3631 40 LEU B CB 69 C CG . LEU A 9 ? 1.1836 0.8903 1.1207 -0.0786 0.1793 -0.3833 40 LEU B CG 70 C CD1 . LEU A 9 ? 1.1274 0.8590 1.1117 -0.0770 0.1830 -0.4062 40 LEU B CD1 71 C CD2 . LEU A 9 ? 1.2016 0.9114 1.1290 -0.0920 0.1923 -0.3923 40 LEU B CD2 72 N N . SER A 10 ? 1.0001 0.6551 0.9113 -0.0196 0.1288 -0.3164 41 SER B N 73 C CA . SER A 10 ? 1.0010 0.6485 0.9199 -0.0019 0.1149 -0.3033 41 SER B CA 74 C C . SER A 10 ? 1.0469 0.6779 0.9295 -0.0027 0.1136 -0.2869 41 SER B C 75 O O . SER A 10 ? 1.0753 0.7027 0.9631 0.0061 0.1081 -0.2811 41 SER B O 76 C CB . SER A 10 ? 0.9978 0.6409 0.9213 0.0115 0.1002 -0.2915 41 SER B CB 77 O OG . SER A 10 ? 1.0197 0.6564 0.9162 0.0040 0.1021 -0.2856 41 SER B OG 78 N N . LEU A 11 ? 0.9342 0.5546 0.7805 -0.0136 0.1179 -0.2796 42 LEU B N 79 C CA . LEU A 11 ? 0.9397 0.5442 0.7508 -0.0161 0.1169 -0.2655 42 LEU B CA 80 C C . LEU A 11 ? 0.9469 0.5548 0.7562 -0.0275 0.1288 -0.2754 42 LEU B C 81 O O . LEU A 11 ? 0.9453 0.5451 0.7432 -0.0236 0.1261 -0.2666 42 LEU B O 82 C CB . LEU A 11 ? 0.9515 0.5431 0.7268 -0.0254 0.1167 -0.2566 42 LEU B CB 83 C CG . LEU A 11 ? 0.9475 0.5239 0.7006 -0.0136 0.1031 -0.2366 42 LEU B CG 84 C CD1 . LEU A 11 ? 0.9592 0.5249 0.6857 -0.0216 0.1015 -0.2313 42 LEU B CD1 85 C CD2 . LEU A 11 ? 0.9484 0.5147 0.6827 -0.0119 0.1015 -0.2268 42 LEU B CD2 86 N N . LYS A 12 ? 0.9933 0.6140 0.8137 -0.0423 0.1423 -0.2942 43 LYS B N 87 C CA . LYS A 12 ? 1.0110 0.6392 0.8336 -0.0556 0.1558 -0.3082 43 LYS B CA 88 C C . LYS A 12 ? 0.9914 0.6263 0.8435 -0.0430 0.1525 -0.3127 43 LYS B C 89 O O . LYS A 12 ? 1.0084 0.6370 0.8482 -0.0448 0.1545 -0.3088 43 LYS B O 90 C CB . LYS A 12 ? 1.0050 0.6515 0.8446 -0.0716 0.1703 -0.3311 43 LYS B CB 91 C CG . LYS A 12 ? 1.0081 0.6681 0.8593 -0.0848 0.1854 -0.3507 43 LYS B CG 92 C CD . LYS A 12 ? 1.0337 0.7177 0.9143 -0.0963 0.1983 -0.3767 43 LYS B CD 93 C CE . LYS A 12 ? 1.0658 0.7632 0.9475 -0.1158 0.2162 -0.3968 43 LYS B CE 94 N NZ . LYS A 12 ? 1.0582 0.7559 0.9547 -0.1064 0.2148 -0.3989 43 LYS B NZ 95 N N . THR A 13 ? 0.9966 0.6435 0.8881 -0.0305 0.1465 -0.3207 44 THR B N 96 C CA . THR A 13 ? 1.0150 0.6691 0.9406 -0.0192 0.1423 -0.3280 44 THR B CA 97 C C . THR A 13 ? 1.0307 0.6707 0.9493 -0.0029 0.1268 -0.3075 44 THR B C 98 O O . THR A 13 ? 1.0417 0.6820 0.9742 0.0026 0.1244 -0.3094 44 THR B O 99 C CB . THR A 13 ? 1.0237 0.6952 0.9966 -0.0120 0.1396 -0.3450 44 THR B CB 100 O OG1 . THR A 13 ? 0.9920 0.6564 0.9731 0.0048 0.1222 -0.3306 44 THR B OG1 101 C CG2 . THR A 13 ? 1.0325 0.7176 1.0092 -0.0265 0.1521 -0.3614 44 THR B CG2 102 N N . SER A 14 ? 1.1154 0.7437 1.0132 0.0043 0.1162 -0.2889 45 SER B N 103 C CA . SER A 14 ? 1.0981 0.7149 0.9880 0.0182 0.1020 -0.2700 45 SER B CA 104 C C . SER A 14 ? 1.1033 0.7080 0.9604 0.0138 0.1046 -0.2586 45 SER B C 105 O O . SER A 14 ? 1.0933 0.6911 0.9470 0.0232 0.0956 -0.2466 45 SER B O 106 C CB . SER A 14 ? 1.1106 0.7210 0.9893 0.0265 0.0907 -0.2555 45 SER B CB 107 O OG . SER A 14 ? 1.1293 0.7258 0.9746 0.0292 0.0853 -0.2369 45 SER B OG 108 N N . LEU A 15 ? 1.2100 0.8117 1.0420 -0.0012 0.1163 -0.2621 46 LEU B N 109 C CA . LEU A 15 ? 1.2455 0.8353 1.0464 -0.0068 0.1187 -0.2525 46 LEU B CA 110 C C . LEU A 15 ? 1.2445 0.8407 1.0549 -0.0159 0.1298 -0.2663 46 LEU B C 111 O O . LEU A 15 ? 1.2428 0.8474 1.0554 -0.0306 0.1430 -0.2822 46 LEU B O 112 C CB . LEU A 15 ? 1.2667 0.8460 1.0313 -0.0183 0.1221 -0.2460 46 LEU B CB 113 C CG . LEU A 15 ? 1.2515 0.8197 0.9991 -0.0068 0.1088 -0.2274 46 LEU B CG 114 C CD1 . LEU A 15 ? 1.2419 0.8017 0.9636 -0.0155 0.1094 -0.2235 46 LEU B CD1 115 C CD2 . LEU A 15 ? 1.2814 0.8397 1.0114 -0.0022 0.1039 -0.2148 46 LEU B CD2 116 N N . SER A 16 ? 1.3729 0.9660 1.1887 -0.0079 0.1248 -0.2609 47 SER B N 117 C CA . SER A 16 ? 1.3543 0.9532 1.1797 -0.0157 0.1346 -0.2741 47 SER B CA 118 C C . SER A 16 ? 1.3806 0.9692 1.1672 -0.0304 0.1427 -0.2690 47 SER B C 119 O O . SER A 16 ? 1.4144 0.9891 1.1746 -0.0267 0.1356 -0.2515 47 SER B O 120 C CB . SER A 16 ? 1.3354 0.9332 1.1798 -0.0026 0.1255 -0.2698 47 SER B CB 121 O OG . SER A 16 ? 1.3698 0.9751 1.2498 0.0102 0.1160 -0.2739 47 SER B OG 122 N N . GLY A 17 ? 1.3223 0.9179 1.1055 -0.0479 0.1572 -0.2847 48 GLY B N 123 C CA . GLY A 17 ? 1.3415 0.9271 1.0885 -0.0644 0.1649 -0.2814 48 GLY B CA 124 C C . GLY A 17 ? 1.3691 0.9676 1.1247 -0.0819 0.1815 -0.3032 48 GLY B C 125 O O . GLY A 17 ? 1.3837 0.9999 1.1721 -0.0825 0.1880 -0.3221 48 GLY B O 126 N N . PRO A 18 ? 1.3610 0.9514 1.0878 -0.0966 0.1884 -0.3016 49 PRO B N 127 C CA . PRO A 18 ? 1.3700 0.9718 1.0967 -0.1177 0.2055 -0.3220 49 PRO B CA 128 C C . PRO A 18 ? 1.3954 1.0083 1.1244 -0.1316 0.2147 -0.3352 49 PRO B C 129 O O . PRO A 18 ? 1.4210 1.0222 1.1240 -0.1359 0.2099 -0.3229 49 PRO B O 130 C CB . PRO A 18 ? 1.3912 0.9752 1.0729 -0.1321 0.2067 -0.3097 49 PRO B CB 131 C CG . PRO A 18 ? 1.3748 0.9444 1.0502 -0.1135 0.1918 -0.2892 49 PRO B CG 132 C CD . PRO A 18 ? 1.3555 0.9268 1.0514 -0.0934 0.1799 -0.2815 49 PRO B CD 133 N N . PRO A 19 ? 1.8475 1.4831 1.6080 -0.1389 0.2278 -0.3608 50 PRO B N 134 C CA . PRO A 19 ? 1.8527 1.5038 1.6240 -0.1509 0.2373 -0.3770 50 PRO B CA 135 C C . PRO A 19 ? 1.8675 1.5090 1.5941 -0.1762 0.2446 -0.3727 50 PRO B C 136 O O . PRO A 19 ? 1.8923 1.5405 1.6183 -0.1854 0.2487 -0.3788 50 PRO B O 137 C CB . PRO A 19 ? 1.8248 1.5013 1.6334 -0.1572 0.2517 -0.4066 50 PRO B CB 138 C CG . PRO A 19 ? 1.8202 1.4947 1.6529 -0.1373 0.2429 -0.4036 50 PRO B CG 139 C CD . PRO A 19 ? 1.8297 1.4787 1.6221 -0.1342 0.2331 -0.3770 50 PRO B CD 140 N N . SER A 20 ? 1.4725 1.0979 1.1619 -0.1877 0.2451 -0.3619 51 SER B N 141 C CA . SER A 20 ? 1.5313 1.1411 1.1731 -0.2104 0.2472 -0.3526 51 SER B CA 142 C C . SER A 20 ? 1.5372 1.1313 1.1635 -0.2019 0.2334 -0.3339 51 SER B C 143 O O . SER A 20 ? 1.5213 1.1102 1.1230 -0.2199 0.2362 -0.3331 51 SER B O 144 C CB . SER A 20 ? 1.5345 1.1255 1.1413 -0.2180 0.2447 -0.3397 51 SER B CB 145 O OG . SER A 20 ? 1.4848 1.0683 1.1043 -0.1937 0.2327 -0.3271 51 SER B OG 146 N N . ALA A 21 ? 1.4618 1.0491 1.1029 -0.1753 0.2185 -0.3197 52 ALA B N 147 C CA . ALA A 21 ? 1.4344 1.0069 1.0628 -0.1641 0.2041 -0.3015 52 ALA B CA 148 C C . ALA A 21 ? 1.4494 1.0334 1.0932 -0.1664 0.2068 -0.3106 52 ALA B C 149 O O . ALA A 21 ? 1.4642 1.0358 1.0816 -0.1753 0.2026 -0.3018 52 ALA B O 150 C CB . ALA A 21 ? 1.3901 0.9569 1.0338 -0.1365 0.1895 -0.2873 52 ALA B CB 151 N N . PHE A 22 ? 1.3390 0.9460 1.0263 -0.1578 0.2126 -0.3281 53 PHE B N 152 C CA . PHE A 22 ? 1.3103 0.9303 1.0172 -0.1584 0.2149 -0.3381 53 PHE B CA 153 C C . PHE A 22 ? 1.3533 0.9933 1.0672 -0.1824 0.2332 -0.3622 53 PHE B C 154 O O . PHE A 22 ? 1.3559 1.0115 1.0938 -0.1824 0.2368 -0.3746 53 PHE B O 155 C CB . PHE A 22 ? 1.2509 0.8808 0.9998 -0.1323 0.2055 -0.3390 53 PHE B CB 156 C CG . PHE A 22 ? 1.1825 0.7935 0.9191 -0.1125 0.1873 -0.3146 53 PHE B CG 157 C CD1 . PHE A 22 ? 1.1280 0.7280 0.8586 -0.0998 0.1789 -0.3014 53 PHE B CD1 158 C CD2 . PHE A 22 ? 1.1518 0.7571 0.8829 -0.1073 0.1790 -0.3059 53 PHE B CD2 159 C CE1 . PHE A 22 ? 1.1097 0.6952 0.8299 -0.0829 0.1633 -0.2809 53 PHE B CE1 160 C CE2 . PHE A 22 ? 1.1430 0.7331 0.8635 -0.0899 0.1631 -0.2855 53 PHE B CE2 161 C CZ . PHE A 22 ? 1.1381 0.7191 0.8536 -0.0780 0.1556 -0.2735 53 PHE B CZ 162 N N . GLN A 23 ? 1.4239 1.0636 1.1162 -0.2035 0.2447 -0.3690 54 GLN B N 163 C CA . GLN A 23 ? 1.4500 1.1123 1.1521 -0.2267 0.2643 -0.3951 54 GLN B CA 164 C C . GLN A 23 ? 1.4595 1.1342 1.1649 -0.2407 0.2713 -0.4063 54 GLN B C 165 O O . GLN A 23 ? 1.5039 1.2058 1.2395 -0.2496 0.2856 -0.4322 54 GLN B O 166 C CB . GLN A 23 ? 1.5206 1.1719 1.1805 -0.2518 0.2724 -0.3927 54 GLN B CB 167 C CG . GLN A 23 ? 1.5739 1.2523 1.2489 -0.2724 0.2921 -0.4181 54 GLN B CG 168 C CD . GLN A 23 ? 1.5880 1.2801 1.2969 -0.2576 0.2938 -0.4265 54 GLN B CD 169 O OE1 . GLN A 23 ? 1.5951 1.3125 1.3542 -0.2445 0.2967 -0.4434 54 GLN B OE1 170 N NE2 . GLN A 23 ? 1.5822 1.2567 1.2639 -0.2599 0.2908 -0.4146 54 GLN B NE2 171 N N . ASP A 24 ? 1.4357 1.0913 1.1114 -0.2431 0.2614 -0.3883 55 ASP B N 172 C CA . ASP A 24 ? 1.4585 1.1245 1.1330 -0.2594 0.2684 -0.3984 55 ASP B CA 173 C C . ASP A 24 ? 1.3565 1.0319 1.0647 -0.2401 0.2610 -0.4001 55 ASP B C 174 O O . ASP A 24 ? 1.3796 1.0607 1.0839 -0.2526 0.2647 -0.4055 55 ASP B O 175 C CB . ASP A 24 ? 1.4879 1.1302 1.1071 -0.2829 0.2656 -0.3831 55 ASP B CB 176 C CG . ASP A 24 ? 1.4920 1.1022 1.0833 -0.2674 0.2453 -0.3537 55 ASP B CG 177 O OD1 . ASP A 24 ? 1.4759 1.0781 1.0719 -0.2495 0.2378 -0.3441 55 ASP B OD1 178 O OD2 . ASP A 24 ? 1.5023 1.0962 1.0679 -0.2735 0.2369 -0.3411 55 ASP B OD2 179 N N . TRP A 25 ? 1.6194 1.2957 1.3590 -0.2109 0.2498 -0.3948 56 TRP B N 180 C CA . TRP A 25 ? 1.5910 1.2690 1.3535 -0.1916 0.2386 -0.3898 56 TRP B CA 181 C C . TRP A 25 ? 1.5766 1.2842 1.3901 -0.1865 0.2456 -0.4140 56 TRP B C 182 O O . TRP A 25 ? 1.5805 1.2895 1.4164 -0.1684 0.2349 -0.4097 56 TRP B O 183 C CB . TRP A 25 ? 1.5556 1.2174 1.3225 -0.1633 0.2205 -0.3692 56 TRP B CB 184 C CG . TRP A 25 ? 1.5725 1.2051 1.2936 -0.1638 0.2096 -0.3439 56 TRP B CG 185 C CD1 . TRP A 25 ? 1.5838 1.2018 1.2636 -0.1840 0.2140 -0.3379 56 TRP B CD1 186 C CD2 . TRP A 25 ? 1.5515 1.1660 1.2640 -0.1433 0.1918 -0.3220 56 TRP B CD2 187 N NE1 . TRP A 25 ? 1.5659 1.1574 1.2140 -0.1762 0.1991 -0.3138 56 TRP B NE1 188 C CE2 . TRP A 25 ? 1.5500 1.1401 1.2180 -0.1512 0.1860 -0.3045 56 TRP B CE2 189 C CE3 . TRP A 25 ? 1.5012 1.1182 1.2395 -0.1196 0.1798 -0.3161 56 TRP B CE3 190 C CZ2 . TRP A 25 ? 1.5259 1.0961 1.1769 -0.1357 0.1696 -0.2830 56 TRP B CZ2 191 C CZ3 . TRP A 25 ? 1.5019 1.0993 1.2207 -0.1056 0.1643 -0.2943 56 TRP B CZ3 192 C CH2 . TRP A 25 ? 1.5077 1.0828 1.1845 -0.1132 0.1597 -0.2788 56 TRP B CH2 193 N N . LYS A 26 ? 1.2904 1.0222 1.1249 -0.2013 0.2627 -0.4400 57 LYS B N 194 C CA . LYS A 26 ? 1.2904 1.0510 1.1783 -0.1940 0.2675 -0.4641 57 LYS B CA 195 C C . LYS A 26 ? 1.2831 1.0520 1.1718 -0.2038 0.2701 -0.4694 57 LYS B C 196 O O . LYS A 26 ? 1.3203 1.0796 1.1687 -0.2256 0.2752 -0.4631 57 LYS B O 197 C CB . LYS A 26 ? 1.3065 1.0938 1.2242 -0.2043 0.2844 -0.4935 57 LYS B CB 198 C CG . LYS A 26 ? 1.2906 1.0807 1.2426 -0.1812 0.2766 -0.4951 57 LYS B CG 199 C CD . LYS A 26 ? 1.2875 1.1117 1.2760 -0.1889 0.2888 -0.5170 57 LYS B CD 200 C CE . LYS A 26 ? 1.3184 1.1465 1.2704 -0.2181 0.3044 -0.5185 57 LYS B CE 201 N NZ . LYS A 26 ? 1.3189 1.1206 1.2338 -0.2173 0.3003 -0.5009 57 LYS B NZ 202 N N . VAL A 27 ? 1.0616 0.8463 0.9957 -0.1870 0.2647 -0.4797 58 VAL B N 203 C CA . VAL A 27 ? 1.0923 0.8880 1.0359 -0.1932 0.2664 -0.4870 58 VAL B CA 204 C C . VAL A 27 ? 1.1249 0.9572 1.1096 -0.2062 0.2834 -0.5221 58 VAL B C 205 O O . VAL A 27 ? 1.0977 0.9507 1.1301 -0.1934 0.2841 -0.5388 58 VAL B O 206 C CB . VAL A 27 ? 1.0537 0.8416 1.0191 -0.1658 0.2472 -0.4735 58 VAL B CB 207 C CG1 . VAL A 27 ? 1.0750 0.8697 1.0837 -0.1416 0.2390 -0.4790 58 VAL B CG1 208 C CG2 . VAL A 27 ? 1.0408 0.8451 1.0271 -0.1700 0.2494 -0.4857 58 VAL B CG2 209 N N . PRO A 28 ? 1.6383 1.4806 1.6061 -0.2314 0.2958 -0.5317 59 PRO B N 210 C CA . PRO A 28 ? 1.6521 1.5351 1.6602 -0.2437 0.3097 -0.5583 59 PRO B CA 211 C C . PRO A 28 ? 1.6450 1.5473 1.7142 -0.2196 0.3011 -0.5717 59 PRO B C 212 O O . PRO A 28 ? 1.6420 1.5681 1.7354 -0.2275 0.3073 -0.5875 59 PRO B O 213 C CB . PRO A 28 ? 1.6742 1.5542 1.6469 -0.2693 0.3172 -0.5568 59 PRO B CB 214 C CG . PRO A 28 ? 1.7068 1.5486 1.6155 -0.2792 0.3125 -0.5325 59 PRO B CG 215 C CD . PRO A 28 ? 1.6931 1.5114 1.6041 -0.2486 0.2937 -0.5105 59 PRO B CD 216 N N . ASP A 34 ? 1.6925 1.4784 1.5655 -0.2460 0.2584 -0.4690 65 ASP B N 217 C CA . ASP A 34 ? 1.7463 1.5108 1.5907 -0.2459 0.2464 -0.4496 65 ASP B CA 218 C C . ASP A 34 ? 1.7878 1.5173 1.5745 -0.2538 0.2386 -0.4240 65 ASP B C 219 O O . ASP A 34 ? 1.8417 1.5663 1.5940 -0.2812 0.2486 -0.4258 65 ASP B O 220 C CB . ASP A 34 ? 1.7827 1.5646 1.6286 -0.2694 0.2575 -0.4653 65 ASP B CB 221 C CG . ASP A 34 ? 1.7899 1.6060 1.6951 -0.2600 0.2629 -0.4903 65 ASP B CG 222 O OD1 . ASP A 34 ? 1.7865 1.6007 1.7109 -0.2416 0.2503 -0.4841 65 ASP B OD1 223 O OD2 . ASP A 34 ? 1.7646 1.6100 1.6981 -0.2710 0.2794 -0.5167 65 ASP B OD2 224 N N . ALA A 35 ? 1.5789 1.2845 1.3561 -0.2301 0.2202 -0.4011 66 ALA B N 225 C CA . ALA A 35 ? 1.5451 1.2172 1.2736 -0.2320 0.2099 -0.3767 66 ALA B CA 226 C C . ALA A 35 ? 1.5531 1.2232 1.2653 -0.2437 0.2190 -0.3792 66 ALA B C 227 O O . ALA A 35 ? 1.5657 1.2123 1.2334 -0.2576 0.2159 -0.3652 66 ALA B O 228 C CB . ALA A 35 ? 1.5600 1.2140 1.2481 -0.2522 0.2065 -0.3670 66 ALA B CB 229 N N . VAL A 36 ? 1.6515 1.3456 1.4010 -0.2373 0.2289 -0.3971 67 VAL B N 230 C CA . VAL A 36 ? 1.6691 1.3669 1.4096 -0.2497 0.2402 -0.4044 67 VAL B CA 231 C C . VAL A 36 ? 1.6932 1.3637 1.4063 -0.2377 0.2282 -0.3819 67 VAL B C 232 O O . VAL A 36 ? 1.7166 1.3722 1.3917 -0.2555 0.2314 -0.3752 67 VAL B O 233 C CB . VAL A 36 ? 1.6347 1.3648 1.4279 -0.2412 0.2512 -0.4294 67 VAL B CB 234 C CG1 . VAL A 36 ? 1.5977 1.3350 1.4341 -0.2107 0.2388 -0.4285 67 VAL B CG1 235 C CG2 . VAL A 36 ? 1.6478 1.3758 1.4370 -0.2405 0.2557 -0.4302 67 VAL B CG2 236 N N . TRP A 37 ? 1.5174 1.1814 1.2494 -0.2081 0.2139 -0.3702 68 TRP B N 237 C CA . TRP A 37 ? 1.4634 1.1073 1.1795 -0.1931 0.2032 -0.3520 68 TRP B CA 238 C C . TRP A 37 ? 1.4502 1.0632 1.1138 -0.2036 0.1947 -0.3311 68 TRP B C 239 O O . TRP A 37 ? 1.4675 1.0646 1.1117 -0.1992 0.1894 -0.3188 68 TRP B O 240 C CB . TRP A 37 ? 1.3836 1.0261 1.1264 -0.1621 0.1884 -0.3425 68 TRP B CB 241 C CG . TRP A 37 ? 1.3701 1.0031 1.1059 -0.1560 0.1773 -0.3322 68 TRP B CG 242 C CD1 . TRP A 37 ? 1.3913 0.9985 1.0957 -0.1493 0.1629 -0.3105 68 TRP B CD1 243 C CD2 . TRP A 37 ? 1.3194 0.9690 1.0815 -0.1559 0.1794 -0.3439 68 TRP B CD2 244 N NE1 . TRP A 37 ? 1.3683 0.9747 1.0771 -0.1450 0.1560 -0.3079 68 TRP B NE1 245 C CE2 . TRP A 37 ? 1.3280 0.9598 1.0712 -0.1491 0.1658 -0.3276 68 TRP B CE2 246 C CE3 . TRP A 37 ? 1.3068 0.9852 1.1080 -0.1606 0.1910 -0.3676 68 TRP B CE3 247 C CZ2 . TRP A 37 ? 1.3571 0.9981 1.1174 -0.1473 0.1637 -0.3331 68 TRP B CZ2 248 C CZ3 . TRP A 37 ? 1.3136 1.0017 1.1329 -0.1586 0.1886 -0.3732 68 TRP B CZ3 249 C CH2 . TRP A 37 ? 1.3398 1.0087 1.1376 -0.1523 0.1751 -0.3554 68 TRP B CH2 250 N N . CYS A 38 ? 1.3561 0.9603 0.9978 -0.2177 0.1925 -0.3273 69 CYS B N 251 C CA . CYS A 38 ? 1.3611 0.9341 0.9538 -0.2284 0.1821 -0.3080 69 CYS B CA 252 C C . CYS A 38 ? 1.3792 0.9437 0.9380 -0.2547 0.1907 -0.3090 69 CYS B C 253 O O . CYS A 38 ? 1.4293 0.9658 0.9472 -0.2634 0.1806 -0.2923 69 CYS B O 254 C CB . CYS A 38 ? 1.3485 0.9146 0.9279 -0.2382 0.1774 -0.3051 69 CYS B CB 255 S SG . CYS A 38 ? 1.8043 1.3652 1.4036 -0.2073 0.1600 -0.2935 69 CYS B SG 256 N N . SER A 39 ? 1.5382 1.1266 1.1142 -0.2681 0.2086 -0.3292 70 SER B N 257 C CA . SER A 39 ? 1.5757 1.1584 1.1205 -0.2944 0.2180 -0.3318 70 SER B CA 258 C C . SER A 39 ? 1.5592 1.1315 1.1001 -0.2807 0.2130 -0.3223 70 SER B C 259 O O . SER A 39 ? 1.5578 1.1120 1.0622 -0.2963 0.2119 -0.3137 70 SER B O 260 C CB . SER A 39 ? 1.5901 1.2050 1.1563 -0.3146 0.2403 -0.3594 70 SER B CB 261 O OG . SER A 39 ? 1.6298 1.2584 1.2072 -0.3240 0.2452 -0.3700 70 SER B OG 262 N N . TRP A 40 ? 1.6201 1.2023 1.1974 -0.2515 0.2084 -0.3226 71 TRP B N 263 C CA . TRP A 40 ? 1.5989 1.1821 1.1851 -0.2398 0.2090 -0.3215 71 TRP B CA 264 C C . TRP A 40 ? 1.5889 1.1417 1.1354 -0.2393 0.1965 -0.2996 71 TRP B C 265 O O . TRP A 40 ? 1.6187 1.1482 1.1365 -0.2403 0.1833 -0.2832 71 TRP B O 266 C CB . TRP A 40 ? 1.5602 1.1568 1.1910 -0.2085 0.2035 -0.3235 71 TRP B CB 267 C CG . TRP A 40 ? 1.5171 1.1444 1.1922 -0.2072 0.2147 -0.3466 71 TRP B CG 268 C CD1 . TRP A 40 ? 1.4952 1.1416 1.1759 -0.2304 0.2308 -0.3670 71 TRP B CD1 269 C CD2 . TRP A 40 ? 1.4698 1.1123 1.1905 -0.1818 0.2099 -0.3521 71 TRP B CD2 270 N NE1 . TRP A 40 ? 1.4784 1.1520 1.2081 -0.2198 0.2364 -0.3860 71 TRP B NE1 271 C CE2 . TRP A 40 ? 1.4588 1.1292 1.2133 -0.1900 0.2229 -0.3766 71 TRP B CE2 272 C CE3 . TRP A 40 ? 1.4417 1.0769 1.1775 -0.1541 0.1954 -0.3389 71 TRP B CE3 273 C CZ2 . TRP A 40 ? 1.4401 1.1295 1.2436 -0.1703 0.2202 -0.3876 71 TRP B CZ2 274 C CZ3 . TRP A 40 ? 1.4436 1.0970 1.2252 -0.1361 0.1931 -0.3489 71 TRP B CZ3 275 C CH2 . TRP A 40 ? 1.4406 1.1199 1.2561 -0.1437 0.2047 -0.3728 71 TRP B CH2 276 N N . SER A 41 ? 1.2533 0.8068 0.7993 -0.2383 0.2005 -0.3007 72 SER B N 277 C CA . SER A 41 ? 1.2831 0.8099 0.7933 -0.2393 0.1900 -0.2821 72 SER B CA 278 C C . SER A 41 ? 1.2747 0.7894 0.7927 -0.2093 0.1728 -0.2650 72 SER B C 279 O O . SER A 41 ? 1.2358 0.7631 0.7844 -0.1893 0.1731 -0.2682 72 SER B O 280 C CB . SER A 41 ? 1.2788 0.8125 0.7881 -0.2483 0.2009 -0.2903 72 SER B CB 281 O OG . SER A 41 ? 1.2678 0.8167 0.8150 -0.2244 0.2017 -0.2953 72 SER B OG 282 N N . GLY A 42 ? 1.2286 0.7181 0.7174 -0.2077 0.1574 -0.2471 73 GLY B N 283 C CA . GLY A 42 ? 1.1860 0.6639 0.6791 -0.1813 0.1409 -0.2315 73 GLY B CA 284 C C . GLY A 42 ? 1.2016 0.6800 0.7050 -0.1708 0.1331 -0.2289 73 GLY B C 285 O O . GLY A 42 ? 1.2228 0.6877 0.7209 -0.1543 0.1180 -0.2152 73 GLY B O 286 N N . VAL A 43 ? 1.1989 0.6938 0.7172 -0.1815 0.1438 -0.2431 74 VAL B N 287 C CA . VAL A 43 ? 1.2112 0.7090 0.7415 -0.1732 0.1380 -0.2427 74 VAL B CA 288 C C . VAL A 43 ? 1.2561 0.7353 0.7519 -0.1935 0.1334 -0.2371 74 VAL B C 289 O O . VAL A 43 ? 1.2854 0.7618 0.7593 -0.2199 0.1423 -0.2426 74 VAL B O 290 C CB . VAL A 43 ? 1.1950 0.7225 0.7652 -0.1717 0.1511 -0.2619 74 VAL B CB 291 C CG1 . VAL A 43 ? 1.1486 0.6792 0.7307 -0.1644 0.1451 -0.2617 74 VAL B CG1 292 C CG2 . VAL A 43 ? 1.1264 0.6697 0.7308 -0.1515 0.1531 -0.2667 74 VAL B CG2 293 N N . VAL A 44 ? 1.2532 0.7189 0.7431 -0.1818 0.1189 -0.2259 75 VAL B N 294 C CA . VAL A 44 ? 1.2502 0.6983 0.7118 -0.1985 0.1125 -0.2207 75 VAL B CA 295 C C . VAL A 44 ? 1.2424 0.6989 0.7255 -0.1852 0.1081 -0.2227 75 VAL B C 296 O O . VAL A 44 ? 1.2418 0.7002 0.7428 -0.1601 0.0990 -0.2167 75 VAL B O 297 C CB . VAL A 44 ? 1.3087 0.7244 0.7354 -0.1974 0.0944 -0.2023 75 VAL B CB 298 C CG1 . VAL A 44 ? 1.3011 0.6977 0.7041 -0.2089 0.0839 -0.1960 75 VAL B CG1 299 C CG2 . VAL A 44 ? 1.2523 0.6566 0.6529 -0.2142 0.0975 -0.1995 75 VAL B CG2 300 N N . CYS A 45 ? 1.3837 0.8462 0.8649 -0.2024 0.1146 -0.2311 76 CYS B N 301 C CA . CYS A 45 ? 1.3653 0.8375 0.8689 -0.1901 0.1112 -0.2341 76 CYS B CA 302 C C . CYS A 45 ? 1.4366 0.8858 0.9113 -0.1998 0.0990 -0.2243 76 CYS B C 303 O O . CYS A 45 ? 1.5292 0.9589 0.9685 -0.2219 0.0966 -0.2191 76 CYS B O 304 C CB . CYS A 45 ? 1.3813 0.8837 0.9160 -0.1979 0.1282 -0.2540 76 CYS B CB 305 S SG . CYS A 45 ? 1.4559 0.9876 1.0343 -0.1827 0.1404 -0.2679 76 CYS B SG 306 N N . ASP A 46 ? 1.4276 0.8780 0.9170 -0.1832 0.0901 -0.2214 77 ASP B N 307 C CA . ASP A 46 ? 1.4666 0.8960 0.9326 -0.1898 0.0777 -0.2130 77 ASP B CA 308 C C . ASP A 46 ? 1.4778 0.9184 0.9437 -0.2132 0.0892 -0.2249 77 ASP B C 309 O O . ASP A 46 ? 1.5061 0.9713 1.0041 -0.2072 0.0980 -0.2369 77 ASP B O 310 C CB . ASP A 46 ? 1.4942 0.9242 0.9789 -0.1630 0.0655 -0.2075 77 ASP B CB 311 C CG . ASP A 46 ? 1.5478 0.9569 1.0119 -0.1671 0.0518 -0.1996 77 ASP B CG 312 O OD1 . ASP A 46 ? 1.5296 0.9469 0.9997 -0.1773 0.0566 -0.2068 77 ASP B OD1 313 O OD2 . ASP A 46 ? 1.6002 0.9851 1.0437 -0.1599 0.0357 -0.1869 77 ASP B OD2 314 N N . ASN A 47 ? 1.5360 0.9580 0.9656 -0.2403 0.0880 -0.2214 78 ASN B N 315 C CA . ASN A 47 ? 1.5243 0.9599 0.9505 -0.2685 0.1029 -0.2347 78 ASN B CA 316 C C . ASN A 47 ? 1.4878 0.9391 0.9359 -0.2667 0.1058 -0.2434 78 ASN B C 317 O O . ASN A 47 ? 1.5235 0.9967 0.9830 -0.2845 0.1215 -0.2590 78 ASN B O 318 C CB . ASN A 47 ? 1.5949 1.0046 0.9731 -0.3001 0.0991 -0.2273 78 ASN B CB 319 C CG . ASN A 47 ? 1.6489 1.0655 1.0158 -0.3197 0.1132 -0.2340 78 ASN B CG 320 O OD1 . ASN A 47 ? 1.6572 1.1046 1.0526 -0.3206 0.1317 -0.2509 78 ASN B OD1 321 N ND2 . ASN A 47 ? 1.7131 1.1007 1.0388 -0.3356 0.1036 -0.2213 78 ASN B ND2 322 N N . VAL A 48 ? 1.5544 0.9960 1.0093 -0.2457 0.0909 -0.2344 79 VAL B N 323 C CA . VAL A 48 ? 1.5496 1.0074 1.0288 -0.2409 0.0931 -0.2425 79 VAL B CA 324 C C . VAL A 48 ? 1.5496 1.0389 1.0764 -0.2197 0.1024 -0.2546 79 VAL B C 325 O O . VAL A 48 ? 1.5357 1.0499 1.0883 -0.2256 0.1144 -0.2700 79 VAL B O 326 C CB . VAL A 48 ? 1.5305 0.9668 1.0004 -0.2259 0.0734 -0.2291 79 VAL B CB 327 C CG1 . VAL A 48 ? 1.5250 0.9764 1.0156 -0.2253 0.0759 -0.2375 79 VAL B CG1 328 C CG2 . VAL A 48 ? 1.5686 0.9692 0.9926 -0.2423 0.0595 -0.2152 79 VAL B CG2 329 N N . THR A 49 ? 1.5720 1.0593 1.1103 -0.1951 0.0956 -0.2474 80 THR B N 330 C CA . THR A 49 ? 1.5096 1.0197 1.0898 -0.1710 0.0978 -0.2539 80 THR B CA 331 C C . THR A 49 ? 1.4972 1.0294 1.1031 -0.1679 0.1111 -0.2653 80 THR B C 332 O O . THR A 49 ? 1.4918 1.0426 1.1337 -0.1494 0.1122 -0.2713 80 THR B O 333 C CB . THR A 49 ? 1.4760 0.9719 1.0554 -0.1446 0.0809 -0.2390 80 THR B CB 334 O OG1 . THR A 49 ? 1.4579 0.9480 1.0311 -0.1368 0.0798 -0.2328 80 THR B OG1 335 C CG2 . THR A 49 ? 1.4915 0.9599 1.0391 -0.1484 0.0660 -0.2264 80 THR B CG2 336 N N . ALA A 50 ? 1.3579 0.8869 0.9452 -0.1858 0.1199 -0.2679 81 ALA B N 337 C CA . ALA A 50 ? 1.3389 0.8874 0.9485 -0.1841 0.1325 -0.2792 81 ALA B CA 338 C C . ALA A 50 ? 1.3094 0.8556 0.9322 -0.1580 0.1245 -0.2704 81 ALA B C 339 O O . ALA A 50 ? 1.3014 0.8618 0.9432 -0.1544 0.1330 -0.2784 81 ALA B O 340 C CB . ALA A 50 ? 1.3074 0.8881 0.9564 -0.1878 0.1467 -0.3007 81 ALA B CB 341 N N . GLN A 51 ? 1.3102 0.8398 0.9244 -0.1401 0.1084 -0.2550 82 GLN B N 342 C CA . GLN A 51 ? 1.2618 0.7903 0.8881 -0.1157 0.1002 -0.2466 82 GLN B CA 343 C C . GLN A 51 ? 1.2631 0.7752 0.8631 -0.1188 0.0980 -0.2371 82 GLN B C 344 O O . GLN A 51 ? 1.2899 0.7822 0.8557 -0.1344 0.0950 -0.2306 82 GLN B O 345 C CB . GLN A 51 ? 1.2357 0.7553 0.8630 -0.0971 0.0849 -0.2356 82 GLN B CB 346 C CG . GLN A 51 ? 1.2268 0.7611 0.8783 -0.0947 0.0859 -0.2441 82 GLN B CG 347 C CD . GLN A 51 ? 1.2667 0.8275 0.9603 -0.0859 0.0938 -0.2572 82 GLN B CD 348 O OE1 . GLN A 51 ? 1.2749 0.8524 0.9839 -0.0994 0.1071 -0.2725 82 GLN B OE1 349 N NE2 . GLN A 51 ? 1.2737 0.8387 0.9866 -0.0638 0.0851 -0.2517 82 GLN B NE2 350 N N . VAL A 52 ? 1.2250 0.7440 0.8405 -0.1042 0.0984 -0.2360 83 VAL B N 351 C CA . VAL A 52 ? 1.2240 0.7317 0.8184 -0.1100 0.0997 -0.2305 83 VAL B CA 352 C C . VAL A 52 ? 1.2626 0.7488 0.8357 -0.0972 0.0837 -0.2135 83 VAL B C 353 O O . VAL A 52 ? 1.2712 0.7613 0.8593 -0.0761 0.0765 -0.2081 83 VAL B O 354 C CB . VAL A 52 ? 1.1820 0.7065 0.8025 -0.1002 0.1070 -0.2370 83 VAL B CB 355 C CG1 . VAL A 52 ? 1.1898 0.7011 0.7875 -0.1039 0.1064 -0.2293 83 VAL B CG1 356 C CG2 . VAL A 52 ? 1.1774 0.7253 0.8236 -0.1118 0.1229 -0.2564 83 VAL B CG2 357 N N . ILE A 53 ? 1.1290 0.5925 0.6670 -0.1108 0.0776 -0.2056 84 ILE B N 358 C CA . ILE A 53 ? 1.1646 0.6066 0.6827 -0.0996 0.0610 -0.1910 84 ILE B CA 359 C C . ILE A 53 ? 1.1636 0.5943 0.6658 -0.0983 0.0579 -0.1835 84 ILE B C 360 O O . ILE A 53 ? 1.1599 0.5768 0.6518 -0.0859 0.0446 -0.1730 84 ILE B O 361 C CB . ILE A 53 ? 1.2116 0.6320 0.7021 -0.1118 0.0513 -0.1853 84 ILE B CB 362 C CG1 . ILE A 53 ? 1.2508 0.6586 0.7127 -0.1395 0.0568 -0.1865 84 ILE B CG1 363 C CG2 . ILE A 53 ? 1.1550 0.5859 0.6611 -0.1114 0.0530 -0.1917 84 ILE B CG2 364 C CD1 . ILE A 53 ? 1.2560 0.6459 0.6940 -0.1555 0.0495 -0.1833 84 ILE B CD1 365 N N . SER A 54 ? 1.2202 0.6573 0.7210 -0.1112 0.0700 -0.1897 85 SER B N 366 C CA . SER A 54 ? 1.2228 0.6493 0.7088 -0.1102 0.0670 -0.1825 85 SER B CA 367 C C . SER A 54 ? 1.2091 0.6542 0.7134 -0.1116 0.0813 -0.1916 85 SER B C 368 O O . SER A 54 ? 1.2118 0.6685 0.7212 -0.1282 0.0951 -0.2036 85 SER B O 369 C CB . SER A 54 ? 1.2515 0.6526 0.6985 -0.1313 0.0617 -0.1760 85 SER B CB 370 O OG . SER A 54 ? 1.2555 0.6440 0.6875 -0.1287 0.0558 -0.1677 85 SER B OG 371 N N . LEU A 55 ? 1.2079 0.6562 0.7222 -0.0949 0.0779 -0.1867 86 LEU B N 372 C CA . LEU A 55 ? 1.1952 0.6589 0.7264 -0.0951 0.0896 -0.1945 86 LEU B CA 373 C C . LEU A 55 ? 1.1989 0.6501 0.7126 -0.0931 0.0847 -0.1853 86 LEU B C 374 O O . LEU A 55 ? 1.1898 0.6378 0.7070 -0.0751 0.0748 -0.1764 86 LEU B O 375 C CB . LEU A 55 ? 1.1706 0.6547 0.7388 -0.0751 0.0907 -0.1989 86 LEU B CB 376 C CG . LEU A 55 ? 1.1560 0.6614 0.7528 -0.0761 0.1039 -0.2124 86 LEU B CG 377 C CD1 . LEU A 55 ? 1.1650 0.6776 0.7597 -0.0990 0.1181 -0.2265 86 LEU B CD1 378 C CD2 . LEU A 55 ? 1.1367 0.6585 0.7681 -0.0586 0.1015 -0.2163 86 LEU B CD2 379 N N . ASP A 56 ? 1.3800 0.8253 0.8753 -0.1122 0.0922 -0.1882 87 ASP B N 380 C CA . ASP A 56 ? 1.3836 0.8178 0.8636 -0.1109 0.0880 -0.1802 87 ASP B CA 381 C C . ASP A 56 ? 1.3729 0.8229 0.8677 -0.1157 0.1022 -0.1902 87 ASP B C 382 O O . ASP A 56 ? 1.3798 0.8353 0.8702 -0.1356 0.1147 -0.2009 87 ASP B O 383 C CB . ASP A 56 ? 1.4111 0.8197 0.8515 -0.1294 0.0811 -0.1722 87 ASP B CB 384 C CG . ASP A 56 ? 1.4163 0.8134 0.8408 -0.1295 0.0769 -0.1645 87 ASP B CG 385 O OD1 . ASP A 56 ? 1.3999 0.8044 0.8408 -0.1103 0.0740 -0.1612 87 ASP B OD1 386 O OD2 . ASP A 56 ? 1.4375 0.8180 0.8323 -0.1496 0.0762 -0.1616 87 ASP B OD2 387 N N . LEU A 57 ? 1.0738 0.5322 0.5873 -0.0978 0.1005 -0.1879 88 LEU B N 388 C CA . LEU A 57 ? 1.0678 0.5367 0.5914 -0.1019 0.1114 -0.1955 88 LEU B CA 389 C C . LEU A 57 ? 1.0619 0.5239 0.5804 -0.0898 0.1040 -0.1849 88 LEU B C 390 O O . LEU A 57 ? 1.0435 0.5127 0.5809 -0.0701 0.0981 -0.1807 88 LEU B O 391 C CB . LEU A 57 ? 1.0468 0.5400 0.6095 -0.0933 0.1203 -0.2086 88 LEU B CB 392 C CG . LEU A 57 ? 1.0302 0.5301 0.6144 -0.0735 0.1117 -0.2051 88 LEU B CG 393 C CD1 . LEU A 57 ? 1.0082 0.5247 0.6257 -0.0585 0.1137 -0.2098 88 LEU B CD1 394 C CD2 . LEU A 57 ? 1.0345 0.5411 0.6262 -0.0810 0.1157 -0.2137 88 LEU B CD2 395 N N . SER A 58 ? 1.1142 0.5638 0.6083 -0.1026 0.1050 -0.1816 89 SER B N 396 C CA . SER A 58 ? 1.1131 0.5542 0.5995 -0.0919 0.0963 -0.1707 89 SER B CA 397 C C . SER A 58 ? 1.1209 0.5583 0.5935 -0.1067 0.1040 -0.1734 89 SER B C 398 O O . SER A 58 ? 1.1332 0.5679 0.5912 -0.1283 0.1129 -0.1806 89 SER B O 399 C CB . SER A 58 ? 1.1278 0.5482 0.5900 -0.0887 0.0804 -0.1573 89 SER B CB 400 O OG . SER A 58 ? 1.1468 0.5564 0.5910 -0.1043 0.0797 -0.1587 89 SER B OG 401 N N . HIS A 59 ? 1.6526 1.0905 1.1293 -0.0961 0.1010 -0.1681 90 HIS B N 402 C CA . HIS A 59 ? 1.6580 1.0941 1.1247 -0.1083 0.1085 -0.1712 90 HIS B CA 403 C C . HIS A 59 ? 1.6494 1.1033 1.1344 -0.1195 0.1257 -0.1885 90 HIS B C 404 O O . HIS A 59 ? 1.6588 1.1111 1.1298 -0.1387 0.1351 -0.1952 90 HIS B O 405 C CB . HIS A 59 ? 1.6841 1.0973 1.1119 -0.1268 0.1032 -0.1639 90 HIS B CB 406 C CG . HIS A 59 ? 1.6944 1.0893 1.1058 -0.1167 0.0851 -0.1489 90 HIS B CG 407 N ND1 . HIS A 59 ? 1.6970 1.0864 1.1075 -0.1103 0.0759 -0.1448 90 HIS B ND1 408 C CD2 . HIS A 59 ? 1.7020 1.0838 1.0993 -0.1114 0.0743 -0.1381 90 HIS B CD2 409 C CE1 . HIS A 59 ? 1.7053 1.0793 1.1025 -0.1013 0.0601 -0.1329 90 HIS B CE1 410 N NE2 . HIS A 59 ? 1.7084 1.0778 1.0979 -0.1017 0.0587 -0.1288 90 HIS B NE2 411 N N . ARG A 60 ? 1.4709 0.9423 0.9877 -0.1078 0.1291 -0.1964 91 ARG B N 412 C CA . ARG A 60 ? 1.4594 0.9504 1.0010 -0.1149 0.1439 -0.2147 91 ARG B CA 413 C C . ARG A 60 ? 1.4428 0.9464 1.0104 -0.1041 0.1478 -0.2202 91 ARG B C 414 O O . ARG A 60 ? 1.4298 0.9511 1.0250 -0.1056 0.1582 -0.2362 91 ARG B O 415 C CB . ARG A 60 ? 1.4487 0.9514 1.0125 -0.1087 0.1445 -0.2213 91 ARG B CB 416 C CG . ARG A 60 ? 1.4678 0.9614 1.0089 -0.1240 0.1444 -0.2208 91 ARG B CG 417 C CD . ARG A 60 ? 1.4552 0.9649 1.0221 -0.1218 0.1493 -0.2323 91 ARG B CD 418 N NE . ARG A 60 ? 1.4765 0.9804 1.0225 -0.1415 0.1530 -0.2355 91 ARG B NE 419 C CZ . ARG A 60 ? 1.4707 0.9868 1.0332 -0.1442 0.1578 -0.2456 91 ARG B CZ 420 N NH1 . ARG A 60 ? 1.4439 0.9781 1.0446 -0.1278 0.1587 -0.2533 91 ARG B NH1 421 N NH2 . ARG A 60 ? 1.4928 1.0024 1.0331 -0.1639 0.1608 -0.2476 91 ARG B NH2 422 N N . ASN A 61 ? 1.4195 0.9141 0.9794 -0.0930 0.1388 -0.2073 92 ASN B N 423 C CA . ASN A 61 ? 1.4059 0.9100 0.9888 -0.0815 0.1398 -0.2097 92 ASN B CA 424 C C . ASN A 61 ? 1.3877 0.9080 1.0086 -0.0662 0.1388 -0.2165 92 ASN B C 425 O O . ASN A 61 ? 1.3769 0.9089 1.0240 -0.0614 0.1431 -0.2256 92 ASN B O 426 C CB . ASN A 61 ? 1.4127 0.9218 0.9950 -0.0968 0.1528 -0.2223 92 ASN B CB 427 C CG . ASN A 61 ? 1.4283 0.9204 0.9755 -0.1079 0.1508 -0.2127 92 ASN B CG 428 O OD1 . ASN A 61 ? 1.4402 0.9159 0.9606 -0.1087 0.1410 -0.1989 92 ASN B OD1 429 N ND2 . ASN A 61 ? 1.4288 0.9248 0.9772 -0.1165 0.1595 -0.2206 92 ASN B ND2 430 N N . LEU A 62 ? 1.1807 0.7006 0.8041 -0.0588 0.1320 -0.2117 93 LEU B N 431 C CA . LEU A 62 ? 1.1650 0.6991 0.8223 -0.0467 0.1305 -0.2183 93 LEU B CA 432 C C . LEU A 62 ? 1.1570 0.6905 0.8249 -0.0260 0.1168 -0.2054 93 LEU B C 433 O O . LEU A 62 ? 1.1610 0.6851 0.8110 -0.0200 0.1074 -0.1922 93 LEU B O 434 C CB . LEU A 62 ? 1.1607 0.6986 0.8187 -0.0547 0.1345 -0.2259 93 LEU B CB 435 C CG . LEU A 62 ? 1.1545 0.6899 0.8135 -0.0439 0.1243 -0.2174 93 LEU B CG 436 C CD1 . LEU A 62 ? 1.1491 0.6940 0.8203 -0.0517 0.1310 -0.2300 93 LEU B CD1 437 C CD2 . LEU A 62 ? 1.1719 0.6892 0.7961 -0.0459 0.1162 -0.2025 93 LEU B CD2 438 N N . SER A 63 ? 1.3770 0.9209 1.0745 -0.0161 0.1155 -0.2101 94 SER B N 439 C CA . SER A 63 ? 1.3703 0.9144 1.0781 0.0009 0.1032 -0.1987 94 SER B CA 440 C C . SER A 63 ? 1.3625 0.9179 1.1029 0.0097 0.0997 -0.2055 94 SER B C 441 O O . SER A 63 ? 1.3627 0.9276 1.1230 0.0038 0.1076 -0.2211 94 SER B O 442 C CB . SER A 63 ? 1.3615 0.9052 1.0743 0.0041 0.1023 -0.1965 94 SER B CB 443 O OG . SER A 63 ? 1.3599 0.9138 1.1009 0.0015 0.1092 -0.2121 94 SER B OG 444 N N . GLY A 64 ? 1.1493 0.7043 0.8954 0.0231 0.0876 -0.1944 95 GLY B N 445 C CA . GLY A 64 ? 1.1425 0.7065 0.9184 0.0312 0.0822 -0.1995 95 GLY B CA 446 C C . GLY A 64 ? 1.1456 0.7076 0.9158 0.0406 0.0711 -0.1876 95 GLY B C 447 O O . GLY A 64 ? 1.1506 0.7055 0.8972 0.0437 0.0657 -0.1744 95 GLY B O 448 N N . ARG A 65 ? 1.2649 0.8342 1.0587 0.0451 0.0675 -0.1935 96 ARG B N 449 C CA . ARG A 65 ? 1.2670 0.8360 1.0582 0.0528 0.0577 -0.1846 96 ARG B CA 450 C C . ARG A 65 ? 1.2682 0.8376 1.0515 0.0462 0.0637 -0.1906 96 ARG B C 451 O O . ARG A 65 ? 1.2666 0.8412 1.0607 0.0376 0.0735 -0.2046 96 ARG B O 452 C CB . ARG A 65 ? 1.2668 0.8422 1.0892 0.0618 0.0478 -0.1863 96 ARG B CB 453 C CG . ARG A 65 ? 1.2669 0.8442 1.0923 0.0676 0.0393 -0.1817 96 ARG B CG 454 C CD . ARG A 65 ? 1.2677 0.8507 1.1267 0.0747 0.0292 -0.1855 96 ARG B CD 455 N NE . ARG A 65 ? 1.2606 0.8512 1.1498 0.0713 0.0358 -0.2034 96 ARG B NE 456 C CZ . ARG A 65 ? 1.2568 0.8548 1.1618 0.0684 0.0405 -0.2159 96 ARG B CZ 457 N NH1 . ARG A 65 ? 1.2606 0.8580 1.1533 0.0685 0.0389 -0.2114 96 ARG B NH1 458 N NH2 . ARG A 65 ? 1.2474 0.8546 1.1817 0.0651 0.0470 -0.2339 96 ARG B NH2 459 N N . ILE A 66 ? 0.9818 0.5463 0.7464 0.0496 0.0578 -0.1806 97 ILE B N 460 C CA . ILE A 66 ? 0.9845 0.5475 0.7398 0.0438 0.0615 -0.1845 97 ILE B CA 461 C C . ILE A 66 ? 0.9814 0.5522 0.7591 0.0499 0.0557 -0.1880 97 ILE B C 462 O O . ILE A 66 ? 0.9813 0.5521 0.7599 0.0595 0.0450 -0.1787 97 ILE B O 463 C CB . ILE A 66 ? 0.9906 0.5420 0.7112 0.0422 0.0590 -0.1737 97 ILE B CB 464 C CG1 . ILE A 66 ? 0.9944 0.5430 0.7065 0.0396 0.0580 -0.1747 97 ILE B CG1 465 C CG2 . ILE A 66 ? 0.9889 0.5378 0.7002 0.0525 0.0492 -0.1603 97 ILE B CG2 466 C CD1 . ILE A 66 ? 0.9913 0.5413 0.7041 0.0509 0.0469 -0.1663 97 ILE B CD1 467 N N . PRO A 67 ? 1.1201 0.6981 0.9154 0.0432 0.0631 -0.2022 98 PRO B N 468 C CA . PRO A 67 ? 1.1162 0.7039 0.9407 0.0475 0.0595 -0.2100 98 PRO B CA 469 C C . PRO A 67 ? 1.1190 0.7041 0.9364 0.0547 0.0494 -0.2004 98 PRO B C 470 O O . PRO A 67 ? 1.1226 0.6993 0.9121 0.0539 0.0479 -0.1912 98 PRO B O 471 C CB . PRO A 67 ? 1.1161 0.7094 0.9449 0.0350 0.0719 -0.2251 98 PRO B CB 472 C CG . PRO A 67 ? 1.1187 0.7085 0.9320 0.0244 0.0824 -0.2286 98 PRO B CG 473 C CD . PRO A 67 ? 1.1233 0.7006 0.9088 0.0288 0.0766 -0.2123 98 PRO B CD 474 N N . ILE A 68 ? 1.3370 0.9290 1.1803 0.0619 0.0415 -0.2027 99 ILE B N 475 C CA . ILE A 68 ? 1.3385 0.9292 1.1771 0.0680 0.0319 -0.1949 99 ILE B CA 476 C C . ILE A 68 ? 1.3382 0.9340 1.1854 0.0624 0.0369 -0.2054 99 ILE B C 477 O O . ILE A 68 ? 1.3394 0.9345 1.1835 0.0660 0.0304 -0.2012 99 ILE B O 478 C CB . ILE A 68 ? 1.3364 0.9302 1.1955 0.0782 0.0183 -0.1895 99 ILE B CB 479 C CG1 . ILE A 68 ? 1.3375 0.9309 1.2069 0.0806 0.0163 -0.1882 99 ILE B CG1 480 C CG2 . ILE A 68 ? 1.3386 0.9278 1.1777 0.0841 0.0082 -0.1751 99 ILE B CG2 481 C CD1 . ILE A 68 ? 1.3337 0.9349 1.2386 0.0794 0.0194 -0.2037 99 ILE B CD1 482 N N . GLN A 69 ? 1.0487 0.6501 0.9060 0.0528 0.0489 -0.2197 100 GLN B N 483 C CA . GLN A 69 ? 1.0492 0.6566 0.9139 0.0453 0.0551 -0.2309 100 GLN B CA 484 C C . GLN A 69 ? 1.0579 0.6563 0.8889 0.0346 0.0620 -0.2279 100 GLN B C 485 O O . GLN A 69 ? 1.0615 0.6638 0.8938 0.0249 0.0691 -0.2374 100 GLN B O 486 C CB . GLN A 69 ? 1.0414 0.6626 0.9383 0.0395 0.0640 -0.2502 100 GLN B CB 487 C CG . GLN A 69 ? 1.0328 0.6632 0.9686 0.0502 0.0541 -0.2553 100 GLN B CG 488 C CD . GLN A 69 ? 1.0289 0.6591 0.9795 0.0565 0.0499 -0.2546 100 GLN B CD 489 O OE1 . GLN A 69 ? 1.0329 0.6563 0.9633 0.0538 0.0543 -0.2488 100 GLN B OE1 490 N NE2 . GLN A 69 ? 1.0217 0.6585 1.0082 0.0648 0.0404 -0.2604 100 GLN B NE2 491 N N . ILE A 70 ? 1.0335 0.6196 0.8350 0.0358 0.0595 -0.2152 101 ILE B N 492 C CA . ILE A 70 ? 1.0427 0.6166 0.8114 0.0296 0.0600 -0.2085 101 ILE B CA 493 C C . ILE A 70 ? 1.0424 0.6148 0.8096 0.0381 0.0495 -0.2017 101 ILE B C 494 O O . ILE A 70 ? 1.0368 0.6171 0.8260 0.0476 0.0424 -0.2014 101 ILE B O 495 C CB . ILE A 70 ? 1.0456 0.6071 0.7861 0.0307 0.0577 -0.1969 101 ILE B CB 496 C CG1 . ILE A 70 ? 1.0412 0.6054 0.7880 0.0291 0.0633 -0.1995 101 ILE B CG1 497 C CG2 . ILE A 70 ? 1.0582 0.6070 0.7686 0.0192 0.0612 -0.1951 101 ILE B CG2 498 C CD1 . ILE A 70 ? 1.0463 0.5980 0.7638 0.0266 0.0630 -0.1903 101 ILE B CD1 499 N N . ARG A 71 ? 1.6084 1.1698 1.3496 0.0343 0.0476 -0.1963 102 ARG B N 500 C CA . ARG A 71 ? 1.6088 1.1685 1.3471 0.0400 0.0391 -0.1921 102 ARG B CA 501 C C . ARG A 71 ? 1.6111 1.1803 1.3702 0.0348 0.0430 -0.2033 102 ARG B C 502 O O . ARG A 71 ? 1.6134 1.1817 1.3714 0.0369 0.0377 -0.2021 102 ARG B O 503 C CB . ARG A 71 ? 1.5996 1.1615 1.3417 0.0548 0.0276 -0.1822 102 ARG B CB 504 C CG . ARG A 71 ? 1.5938 1.1675 1.3651 0.0621 0.0224 -0.1850 102 ARG B CG 505 C CD . ARG A 71 ? 1.5878 1.1643 1.3649 0.0720 0.0149 -0.1768 102 ARG B CD 506 N NE . ARG A 71 ? 1.5871 1.1615 1.3517 0.0801 0.0046 -0.1666 102 ARG B NE 507 C CZ . ARG A 71 ? 1.5867 1.1622 1.3471 0.0868 -0.0020 -0.1578 102 ARG B CZ 508 N NH1 . ARG A 71 ? 1.5886 1.1643 1.3375 0.0925 -0.0103 -0.1504 102 ARG B NH1 509 N NH2 . ARG A 71 ? 1.5862 1.1632 1.3537 0.0870 -0.0001 -0.1569 102 ARG B NH2 510 N N . TYR A 72 ? 1.2187 0.7977 0.9972 0.0278 0.0526 -0.2151 103 TYR B N 511 C CA . TYR A 72 ? 1.2209 0.8099 1.0173 0.0191 0.0594 -0.2287 103 TYR B CA 512 C C . TYR A 72 ? 1.2349 0.8152 1.0051 0.0026 0.0673 -0.2312 103 TYR B C 513 O O . TYR A 72 ? 1.2410 0.8253 1.0153 -0.0053 0.0705 -0.2386 103 TYR B O 514 C CB . TYR A 72 ? 1.2124 0.8160 1.0398 0.0171 0.0671 -0.2423 103 TYR B CB 515 C CG . TYR A 72 ? 1.2026 0.8191 1.0668 0.0272 0.0606 -0.2482 103 TYR B CG 516 C CD1 . TYR A 72 ? 1.2037 0.8207 1.0722 0.0325 0.0522 -0.2451 103 TYR B CD1 517 C CD2 . TYR A 72 ? 1.1925 0.8201 1.0879 0.0312 0.0618 -0.2573 103 TYR B CD2 518 C CE1 . TYR A 72 ? 1.1957 0.8233 1.0978 0.0412 0.0448 -0.2501 103 TYR B CE1 519 C CE2 . TYR A 72 ? 1.1837 0.8214 1.1141 0.0404 0.0536 -0.2628 103 TYR B CE2 520 C CZ . TYR A 72 ? 1.1856 0.8232 1.1190 0.0452 0.0449 -0.2588 103 TYR B CZ 521 O OH . TYR A 72 ? 1.1777 0.8242 1.1459 0.0540 0.0353 -0.2638 103 TYR B OH 522 N N . LEU A 73 ? 1.0467 0.6143 0.7892 -0.0033 0.0695 -0.2247 104 LEU B N 523 C CA . LEU A 73 ? 1.0635 0.6182 0.7764 -0.0184 0.0726 -0.2236 104 LEU B CA 524 C C . LEU A 73 ? 1.0674 0.6060 0.7568 -0.0095 0.0598 -0.2092 104 LEU B C 525 O O . LEU A 73 ? 1.0681 0.5955 0.7390 -0.0054 0.0551 -0.1997 104 LEU B O 526 C CB . LEU A 73 ? 1.0718 0.6211 0.7675 -0.0329 0.0822 -0.2263 104 LEU B CB 527 C CG . LEU A 73 ? 1.0608 0.6167 0.7688 -0.0275 0.0861 -0.2278 104 LEU B CG 528 C CD1 . LEU A 73 ? 1.0561 0.6023 0.7534 -0.0125 0.0751 -0.2132 104 LEU B CD1 529 C CD2 . LEU A 73 ? 1.0707 0.6245 0.7646 -0.0454 0.0979 -0.2342 104 LEU B CD2 530 N N . SER A 74 ? 1.2918 0.8296 0.9826 -0.0075 0.0543 -0.2089 105 SER B N 531 C CA . SER A 74 ? 1.2903 0.8177 0.9675 0.0039 0.0415 -0.1978 105 SER B CA 532 C C . SER A 74 ? 1.3066 0.8136 0.9502 -0.0048 0.0377 -0.1915 105 SER B C 533 O O . SER A 74 ? 1.3050 0.8015 0.9333 0.0030 0.0297 -0.1824 105 SER B O 534 C CB . SER A 74 ? 1.2865 0.8212 0.9793 0.0099 0.0365 -0.2001 105 SER B CB 535 O OG . SER A 74 ? 1.2813 0.8099 0.9657 0.0232 0.0244 -0.1905 105 SER B OG 536 N N . SER A 75 ? 1.1953 0.6965 0.8275 -0.0220 0.0430 -0.1967 106 SER B N 537 C CA . SER A 75 ? 1.2140 0.6930 0.8132 -0.0311 0.0370 -0.1897 106 SER B CA 538 C C . SER A 75 ? 1.2194 0.6947 0.8077 -0.0409 0.0442 -0.1900 106 SER B C 539 O O . SER A 75 ? 1.2279 0.7081 0.8161 -0.0575 0.0556 -0.1983 106 SER B O 540 C CB . SER A 75 ? 1.2326 0.7052 0.8211 -0.0476 0.0388 -0.1941 106 SER B CB 541 O OG . SER A 75 ? 1.2266 0.7192 0.8405 -0.0524 0.0492 -0.2060 106 SER B OG 542 N N . LEU A 76 ? 1.0340 0.5021 0.6139 -0.0304 0.0376 -0.1816 107 LEU B N 543 C CA . LEU A 76 ? 1.0401 0.5024 0.6076 -0.0372 0.0420 -0.1797 107 LEU B CA 544 C C . LEU A 76 ? 1.0474 0.4908 0.5927 -0.0300 0.0285 -0.1685 107 LEU B C 545 O O . LEU A 76 ? 1.0334 0.4804 0.5870 -0.0123 0.0204 -0.1638 107 LEU B O 546 C CB . LEU A 76 ? 1.0197 0.5000 0.6115 -0.0277 0.0490 -0.1833 107 LEU B CB 547 C CG . LEU A 76 ? 1.0237 0.4984 0.6035 -0.0319 0.0523 -0.1803 107 LEU B CG 548 C CD1 . LEU A 76 ? 1.0334 0.5138 0.6138 -0.0507 0.0665 -0.1904 107 LEU B CD1 549 C CD2 . LEU A 76 ? 1.0034 0.4883 0.5999 -0.0150 0.0504 -0.1770 107 LEU B CD2 550 N N . LEU A 77 ? 1.0707 0.4940 0.5879 -0.0441 0.0250 -0.1645 108 LEU B N 551 C CA . LEU A 77 ? 1.0792 0.4837 0.5776 -0.0369 0.0104 -0.1549 108 LEU B CA 552 C C . LEU A 77 ? 1.0805 0.4796 0.5694 -0.0366 0.0103 -0.1504 108 LEU B C 553 O O . LEU A 77 ? 1.0851 0.4713 0.5624 -0.0285 -0.0019 -0.1434 108 LEU B O 554 C CB . LEU A 77 ? 1.1062 0.4878 0.5794 -0.0498 0.0011 -0.1517 108 LEU B CB 555 C CG . LEU A 77 ? 1.1110 0.4998 0.5899 -0.0622 0.0092 -0.1590 108 LEU B CG 556 C CD1 . LEU A 77 ? 1.1430 0.5081 0.5921 -0.0825 0.0032 -0.1559 108 LEU B CD1 557 C CD2 . LEU A 77 ? 1.0946 0.4952 0.5940 -0.0473 0.0058 -0.1614 108 LEU B CD2 558 N N . TYR A 78 ? 1.1701 0.5796 0.6651 -0.0450 0.0234 -0.1552 109 TYR B N 559 C CA . TYR A 78 ? 1.1741 0.5764 0.6571 -0.0474 0.0233 -0.1509 109 TYR B CA 560 C C . TYR A 78 ? 1.1567 0.5791 0.6608 -0.0437 0.0360 -0.1564 109 TYR B C 561 O O . TYR A 78 ? 1.1537 0.5892 0.6706 -0.0528 0.0485 -0.1656 109 TYR B O 562 C CB . TYR A 78 ? 1.2005 0.5831 0.6540 -0.0706 0.0235 -0.1494 109 TYR B CB 563 C CG . TYR A 78 ? 1.2074 0.5812 0.6461 -0.0760 0.0236 -0.1451 109 TYR B CG 564 C CD1 . TYR A 78 ? 1.2020 0.5887 0.6480 -0.0842 0.0383 -0.1513 109 TYR B CD1 565 C CD2 . TYR A 78 ? 1.2196 0.5720 0.6379 -0.0733 0.0084 -0.1355 109 TYR B CD2 566 C CE1 . TYR A 78 ? 1.2086 0.5871 0.6404 -0.0898 0.0384 -0.1474 109 TYR B CE1 567 C CE2 . TYR A 78 ? 1.2269 0.5707 0.6314 -0.0787 0.0079 -0.1314 109 TYR B CE2 568 C CZ . TYR A 78 ? 1.2213 0.5782 0.6319 -0.0872 0.0232 -0.1370 109 TYR B CZ 569 O OH . TYR A 78 ? 1.2284 0.5769 0.6251 -0.0929 0.0228 -0.1330 109 TYR B OH 570 N N . LEU A 79 ? 1.0873 0.5123 0.5956 -0.0308 0.0324 -0.1514 110 LEU B N 571 C CA . LEU A 79 ? 1.0723 0.5134 0.5984 -0.0279 0.0428 -0.1556 110 LEU B CA 572 C C . LEU A 79 ? 1.0757 0.5085 0.5884 -0.0278 0.0404 -0.1496 110 LEU B C 573 O O . LEU A 79 ? 1.0710 0.4995 0.5804 -0.0150 0.0302 -0.1424 110 LEU B O 574 C CB . LEU A 79 ? 1.0488 0.5080 0.6023 -0.0093 0.0418 -0.1564 110 LEU B CB 575 C CG . LEU A 79 ? 1.0355 0.5126 0.6132 -0.0094 0.0534 -0.1642 110 LEU B CG 576 C CD1 . LEU A 79 ? 1.0382 0.5239 0.6286 -0.0185 0.0615 -0.1745 110 LEU B CD1 577 C CD2 . LEU A 79 ? 1.0154 0.5057 0.6142 0.0085 0.0497 -0.1612 110 LEU B CD2 578 N N . ASN A 80 ? 1.1282 0.5604 0.6345 -0.0421 0.0501 -0.1535 111 ASN B N 579 C CA . ASN A 80 ? 1.1330 0.5569 0.6260 -0.0432 0.0480 -0.1480 111 ASN B CA 580 C C . ASN A 80 ? 1.1198 0.5598 0.6308 -0.0433 0.0603 -0.1544 111 ASN B C 581 O O . ASN A 80 ? 1.1217 0.5688 0.6378 -0.0566 0.0723 -0.1640 111 ASN B O 582 C CB . ASN A 80 ? 1.1591 0.5614 0.6203 -0.0632 0.0456 -0.1452 111 ASN B CB 583 C CG . ASN A 80 ? 1.1678 0.5558 0.6109 -0.0625 0.0375 -0.1367 111 ASN B CG 584 O OD1 . ASN A 80 ? 1.1554 0.5530 0.6093 -0.0544 0.0411 -0.1363 111 ASN B OD1 585 N ND2 . ASN A 80 ? 1.1905 0.5545 0.6061 -0.0713 0.0254 -0.1297 111 ASN B ND2 586 N N . LEU A 81 ? 1.0429 0.4899 0.5653 -0.0285 0.0572 -0.1501 112 LEU B N 587 C CA . LEU A 81 ? 1.0335 0.4915 0.5688 -0.0289 0.0665 -0.1544 112 LEU B CA 588 C C . LEU A 81 ? 1.0354 0.4854 0.5581 -0.0245 0.0606 -0.1458 112 LEU B C 589 O O . LEU A 81 ? 1.0230 0.4780 0.5540 -0.0088 0.0534 -0.1399 112 LEU B O 590 C CB . LEU A 81 ? 1.0110 0.4882 0.5781 -0.0144 0.0685 -0.1580 112 LEU B CB 591 C CG . LEU A 81 ? 1.0048 0.4888 0.5854 -0.0094 0.0665 -0.1613 112 LEU B CG 592 C CD1 . LEU A 81 ? 0.9858 0.4829 0.5897 0.0079 0.0617 -0.1591 112 LEU B CD1 593 C CD2 . LEU A 81 ? 1.0084 0.4998 0.5995 -0.0222 0.0778 -0.1738 112 LEU B CD2 594 N N . SER A 82 ? 1.0849 0.5249 0.5893 -0.0387 0.0646 -0.1459 113 SER B N 595 C CA . SER A 82 ? 1.0901 0.5206 0.5804 -0.0356 0.0579 -0.1376 113 SER B CA 596 C C . SER A 82 ? 1.0880 0.5230 0.5804 -0.0419 0.0671 -0.1407 113 SER B C 597 O O . SER A 82 ? 1.0921 0.5296 0.5835 -0.0568 0.0785 -0.1493 113 SER B O 598 C CB . SER A 82 ? 1.1123 0.5200 0.5725 -0.0448 0.0477 -0.1308 113 SER B CB 599 O OG . SER A 82 ? 1.1127 0.5160 0.5725 -0.0367 0.0377 -0.1277 113 SER B OG 600 N N . GLY A 83 ? 1.4659 0.9034 0.9622 -0.0304 0.0623 -0.1346 114 GLY B N 601 C CA . GLY A 83 ? 1.4669 0.9047 0.9603 -0.0359 0.0679 -0.1352 114 GLY B CA 602 C C . GLY A 83 ? 1.4510 0.9063 0.9704 -0.0340 0.0792 -0.1443 114 GLY B C 603 O O . GLY A 83 ? 1.4461 0.9057 0.9712 -0.0323 0.0823 -0.1444 114 GLY B O 604 N N . ASN A 84 ? 1.2548 0.7200 0.7912 -0.0336 0.0841 -0.1522 115 ASN B N 605 C CA . ASN A 84 ? 1.2404 0.7224 0.8059 -0.0301 0.0926 -0.1620 115 ASN B CA 606 C C . ASN A 84 ? 1.2285 0.7180 0.8101 -0.0124 0.0854 -0.1552 115 ASN B C 607 O O . ASN A 84 ? 1.2256 0.7150 0.8071 -0.0011 0.0760 -0.1476 115 ASN B O 608 C CB . ASN A 84 ? 1.2364 0.7263 0.8163 -0.0310 0.0958 -0.1701 115 ASN B CB 609 C CG . ASN A 84 ? 1.2523 0.7317 0.8100 -0.0475 0.0988 -0.1727 115 ASN B CG 610 O OD1 . ASN A 84 ? 1.2664 0.7375 0.8045 -0.0634 0.1042 -0.1747 115 ASN B OD1 611 N ND2 . ASN A 84 ? 1.2517 0.7309 0.8110 -0.0448 0.0947 -0.1723 115 ASN B ND2 612 N N . SER A 85 ? 1.4897 0.9859 1.0845 -0.0107 0.0895 -0.1581 116 SER B N 613 C CA . SER A 85 ? 1.4820 0.9834 1.0877 0.0040 0.0816 -0.1500 116 SER B CA 614 C C . SER A 85 ? 1.4715 0.9856 1.1062 0.0127 0.0808 -0.1549 116 SER B C 615 O O . SER A 85 ? 1.4678 0.9895 1.1231 0.0102 0.0873 -0.1651 116 SER B O 616 C CB . SER A 85 ? 1.4834 0.9845 1.0890 0.0020 0.0845 -0.1494 116 SER B CB 617 O OG . SER A 85 ? 1.4794 0.9840 1.0904 0.0145 0.0761 -0.1400 116 SER B OG 618 N N . LEU A 86 ? 1.0553 0.5715 0.6920 0.0228 0.0722 -0.1484 117 LEU B N 619 C CA . LEU A 86 ? 1.0472 0.5739 0.7091 0.0317 0.0687 -0.1506 117 LEU B CA 620 C C . LEU A 86 ? 1.0461 0.5745 0.7045 0.0435 0.0575 -0.1390 117 LEU B C 621 O O . LEU A 86 ? 1.0495 0.5726 0.6892 0.0449 0.0531 -0.1329 117 LEU B O 622 C CB . LEU A 86 ? 1.0460 0.5757 0.7168 0.0272 0.0730 -0.1600 117 LEU B CB 623 C CG . LEU A 86 ? 1.0465 0.5719 0.7046 0.0267 0.0699 -0.1578 117 LEU B CG 624 C CD1 . LEU A 86 ? 1.0502 0.5776 0.7140 0.0159 0.0787 -0.1700 117 LEU B CD1 625 C CD2 . LEU A 86 ? 1.0516 0.5649 0.6806 0.0239 0.0664 -0.1495 117 LEU B CD2 626 N N . GLU A 87 ? 1.1878 0.7235 0.8639 0.0511 0.0524 -0.1363 118 GLU B N 627 C CA . GLU A 87 ? 1.1897 0.7284 0.8606 0.0600 0.0426 -0.1253 118 GLU B CA 628 C C . GLU A 87 ? 1.1841 0.7299 0.8730 0.0661 0.0367 -0.1256 118 GLU B C 629 O O . GLU A 87 ? 1.1804 0.7288 0.8885 0.0645 0.0396 -0.1341 118 GLU B O 630 C CB . GLU A 87 ? 1.1964 0.7358 0.8663 0.0614 0.0404 -0.1194 118 GLU B CB 631 C CG . GLU A 87 ? 1.2011 0.7473 0.8826 0.0684 0.0314 -0.1122 118 GLU B CG 632 C CD . GLU A 87 ? 1.2055 0.7555 0.8714 0.0732 0.0244 -0.1022 118 GLU B CD 633 O OE1 . GLU A 87 ? 1.2114 0.7618 0.8673 0.0730 0.0231 -0.0964 118 GLU B OE1 634 O OE2 . GLU A 87 ? 1.2036 0.7573 0.8684 0.0769 0.0202 -0.1010 118 GLU B OE2 635 N N . GLY A 88 ? 1.1695 0.7189 0.8515 0.0726 0.0285 -0.1171 119 GLY B N 636 C CA . GLY A 88 ? 1.1674 0.7231 0.8632 0.0779 0.0212 -0.1154 119 GLY B CA 637 C C . GLY A 88 ? 1.1738 0.7331 0.8543 0.0826 0.0146 -0.1074 119 GLY B C 638 O O . GLY A 88 ? 1.1766 0.7344 0.8394 0.0825 0.0153 -0.1037 119 GLY B O 639 N N . SER A 89 ? 1.3527 0.9175 1.0410 0.0865 0.0079 -0.1052 120 SER B N 640 C CA . SER A 89 ? 1.3594 0.9279 1.0344 0.0900 0.0038 -0.1019 120 SER B CA 641 C C . SER A 89 ? 1.3516 0.9145 1.0260 0.0880 0.0089 -0.1095 120 SER B C 642 O O . SER A 89 ? 1.3517 0.9124 1.0408 0.0851 0.0128 -0.1160 120 SER B O 643 C CB . SER A 89 ? 1.3674 0.9432 1.0508 0.0932 -0.0048 -0.0975 120 SER B CB 644 O OG . SER A 89 ? 1.3614 0.9356 1.0621 0.0932 -0.0052 -0.1030 120 SER B OG 645 N N . PHE A 90 ? 1.1390 0.6995 0.7971 0.0890 0.0088 -0.1094 121 PHE B N 646 C CA . PHE A 90 ? 1.1335 0.6872 0.7886 0.0861 0.0123 -0.1157 121 PHE B CA 647 C C . PHE A 90 ? 1.1298 0.6881 0.8001 0.0880 0.0096 -0.1185 121 PHE B C 648 O O . PHE A 90 ? 1.1335 0.6993 0.8079 0.0929 0.0027 -0.1141 121 PHE B O 649 C CB . PHE A 90 ? 1.1363 0.6860 0.7724 0.0881 0.0093 -0.1143 121 PHE B CB 650 C CG . PHE A 90 ? 1.1345 0.6755 0.7649 0.0847 0.0108 -0.1195 121 PHE B CG 651 C CD1 . PHE A 90 ? 1.1388 0.6707 0.7676 0.0760 0.0178 -0.1243 121 PHE B CD1 652 C CD2 . PHE A 90 ? 1.1309 0.6728 0.7564 0.0892 0.0051 -0.1197 121 PHE B CD2 653 C CE1 . PHE A 90 ? 1.1405 0.6640 0.7623 0.0711 0.0188 -0.1285 121 PHE B CE1 654 C CE2 . PHE A 90 ? 1.1333 0.6659 0.7528 0.0855 0.0055 -0.1238 121 PHE B CE2 655 C CZ . PHE A 90 ? 1.1387 0.6617 0.7557 0.0761 0.0122 -0.1278 121 PHE B CZ 656 N N . PRO A 91 ? 1.1396 0.6941 0.8186 0.0832 0.0150 -0.1260 122 PRO B N 657 C CA . PRO A 91 ? 1.1377 0.6962 0.8318 0.0844 0.0129 -0.1301 122 PRO B CA 658 C C . PRO A 91 ? 1.1386 0.6972 0.8221 0.0880 0.0076 -0.1281 122 PRO B C 659 O O . PRO A 91 ? 1.1407 0.6922 0.8075 0.0861 0.0089 -0.1288 122 PRO B O 660 C CB . PRO A 91 ? 1.1363 0.6903 0.8356 0.0763 0.0218 -0.1397 122 PRO B CB 661 C CG . PRO A 91 ? 1.1392 0.6844 0.8187 0.0705 0.0271 -0.1391 122 PRO B CG 662 C CD . PRO A 91 ? 1.1389 0.6866 0.8156 0.0750 0.0240 -0.1320 122 PRO B CD 663 N N . THR A 92 ? 1.0682 0.6339 0.7615 0.0928 0.0008 -0.1259 123 THR B N 664 C CA . THR A 92 ? 1.0683 0.6350 0.7527 0.0962 -0.0042 -0.1250 123 THR B CA 665 C C . THR A 92 ? 1.0648 0.6282 0.7569 0.0928 -0.0013 -0.1320 123 THR B C 666 O O . THR A 92 ? 1.0640 0.6259 0.7494 0.0942 -0.0043 -0.1330 123 THR B O 667 C CB . THR A 92 ? 1.0739 0.6499 0.7636 0.1012 -0.0127 -0.1195 123 THR B CB 668 O OG1 . THR A 92 ? 1.0803 0.6600 0.7787 0.1011 -0.0146 -0.1149 123 THR B OG1 669 C CG2 . THR A 92 ? 1.0767 0.6562 0.7487 0.1051 -0.0169 -0.1161 123 THR B CG2 670 N N . SER A 93 ? 1.0637 0.6267 0.7709 0.0880 0.0047 -0.1378 124 SER B N 671 C CA . SER A 93 ? 1.0627 0.6250 0.7806 0.0832 0.0088 -0.1463 124 SER B CA 672 C C . SER A 93 ? 1.0661 0.6189 0.7649 0.0772 0.0131 -0.1490 124 SER B C 673 O O . SER A 93 ? 1.0674 0.6187 0.7662 0.0752 0.0125 -0.1526 124 SER B O 674 C CB . SER A 93 ? 1.0619 0.6272 0.7994 0.0785 0.0156 -0.1537 124 SER B CB 675 O OG . SER A 93 ? 1.0633 0.6272 0.7962 0.0785 0.0175 -0.1500 124 SER B OG 676 N N . ILE A 94 ? 0.9624 0.5078 0.6446 0.0739 0.0164 -0.1468 125 ILE B N 677 C CA . ILE A 94 ? 0.9699 0.5033 0.6321 0.0667 0.0189 -0.1483 125 ILE B CA 678 C C . ILE A 94 ? 0.9714 0.5002 0.6206 0.0716 0.0108 -0.1450 125 ILE B C 679 O O . ILE A 94 ? 0.9789 0.4981 0.6168 0.0657 0.0108 -0.1475 125 ILE B O 680 C CB . ILE A 94 ? 0.9748 0.5008 0.6220 0.0629 0.0219 -0.1455 125 ILE B CB 681 C CG1 . ILE A 94 ? 0.9810 0.5032 0.6289 0.0503 0.0321 -0.1525 125 ILE B CG1 682 C CG2 . ILE A 94 ? 0.9805 0.4956 0.6047 0.0646 0.0155 -0.1405 125 ILE B CG2 683 C CD1 . ILE A 94 ? 0.9804 0.5033 0.6285 0.0485 0.0366 -0.1515 125 ILE B CD1 684 N N . PHE A 95 ? 0.9804 0.5163 0.6311 0.0816 0.0036 -0.1400 126 PHE B N 685 C CA . PHE A 95 ? 0.9810 0.5150 0.6216 0.0870 -0.0042 -0.1383 126 PHE B CA 686 C C . PHE A 95 ? 0.9814 0.5162 0.6298 0.0856 -0.0052 -0.1425 126 PHE B C 687 O O . PHE A 95 ? 0.9837 0.5141 0.6233 0.0879 -0.0106 -0.1429 126 PHE B O 688 C CB . PHE A 95 ? 0.9768 0.5217 0.6190 0.0964 -0.0104 -0.1335 126 PHE B CB 689 C CG . PHE A 95 ? 0.9775 0.5233 0.6117 0.0984 -0.0102 -0.1296 126 PHE B CG 690 C CD1 . PHE A 95 ? 0.9817 0.5162 0.6018 0.0950 -0.0089 -0.1299 126 PHE B CD1 691 C CD2 . PHE A 95 ? 0.9766 0.5342 0.6169 0.1028 -0.0122 -0.1252 126 PHE B CD2 692 C CE1 . PHE A 95 ? 0.9825 0.5184 0.5963 0.0970 -0.0091 -0.1265 126 PHE B CE1 693 C CE2 . PHE A 95 ? 0.9783 0.5378 0.6116 0.1041 -0.0119 -0.1218 126 PHE B CE2 694 C CZ . PHE A 95 ? 0.9799 0.5290 0.6007 0.1017 -0.0102 -0.1227 126 PHE B CZ 695 N N . ASP A 96 ? 1.2598 0.8007 0.9263 0.0824 -0.0005 -0.1462 127 ASP B N 696 C CA . ASP A 96 ? 1.2606 0.8037 0.9366 0.0812 -0.0017 -0.1505 127 ASP B CA 697 C C . ASP A 96 ? 1.2684 0.8032 0.9403 0.0702 0.0048 -0.1568 127 ASP B C 698 O O . ASP A 96 ? 1.2701 0.8077 0.9522 0.0672 0.0058 -0.1619 127 ASP B O 699 C CB . ASP A 96 ? 1.2562 0.8116 0.9556 0.0852 -0.0035 -0.1511 127 ASP B CB 700 C CG . ASP A 96 ? 1.2554 0.8177 0.9538 0.0943 -0.0125 -0.1442 127 ASP B CG 701 O OD1 . ASP A 96 ? 1.2587 0.8222 0.9535 0.0976 -0.0183 -0.1437 127 ASP B OD1 702 O OD2 . ASP A 96 ? 1.2535 0.8202 0.9535 0.0972 -0.0136 -0.1394 127 ASP B OD2 703 N N . LEU A 97 ? 1.1336 0.6585 0.7902 0.0632 0.0091 -0.1566 128 LEU B N 704 C CA . LEU A 97 ? 1.1464 0.6606 0.7917 0.0504 0.0141 -0.1612 128 LEU B CA 705 C C . LEU A 97 ? 1.1546 0.6569 0.7829 0.0500 0.0065 -0.1593 128 LEU B C 706 O O . LEU A 97 ? 1.1618 0.6618 0.7910 0.0430 0.0080 -0.1638 128 LEU B O 707 C CB . LEU A 97 ? 1.1541 0.6596 0.7853 0.0421 0.0194 -0.1604 128 LEU B CB 708 C CG . LEU A 97 ? 1.1567 0.6680 0.7988 0.0314 0.0313 -0.1677 128 LEU B CG 709 C CD1 . LEU A 97 ? 1.1564 0.6778 0.8182 0.0264 0.0369 -0.1771 128 LEU B CD1 710 C CD2 . LEU A 97 ? 1.1467 0.6667 0.8008 0.0375 0.0338 -0.1662 128 LEU B CD2 711 N N . THR A 98 ? 1.2676 0.7627 0.8814 0.0571 -0.0018 -0.1536 129 THR B N 712 C CA . THR A 98 ? 1.2711 0.7579 0.8741 0.0615 -0.0117 -0.1523 129 THR B CA 713 C C . THR A 98 ? 1.2888 0.7578 0.8745 0.0509 -0.0145 -0.1536 129 THR B C 714 O O . THR A 98 ? 1.2928 0.7525 0.8682 0.0554 -0.0243 -0.1521 129 THR B O 715 C CB . THR A 98 ? 1.2609 0.7595 0.8788 0.0692 -0.0150 -0.1540 129 THR B CB 716 O OG1 . THR A 98 ? 1.2671 0.7650 0.8912 0.0605 -0.0109 -0.1590 129 THR B OG1 717 C CG2 . THR A 98 ? 1.2471 0.7628 0.8830 0.0772 -0.0132 -0.1525 129 THR B CG2 718 N N . LYS A 99 ? 1.3877 0.8515 0.9696 0.0363 -0.0066 -0.1567 130 LYS B N 719 C CA . LYS A 99 ? 1.4084 0.8524 0.9689 0.0245 -0.0109 -0.1561 130 LYS B CA 720 C C . LYS A 99 ? 1.4197 0.8503 0.9619 0.0178 -0.0114 -0.1522 130 LYS B C 721 O O . LYS A 99 ? 1.4392 0.8498 0.9599 0.0080 -0.0175 -0.1497 130 LYS B O 722 C CB . LYS A 99 ? 1.4195 0.8643 0.9826 0.0101 -0.0034 -0.1620 130 LYS B CB 723 C CG . LYS A 99 ? 1.4426 0.8660 0.9824 -0.0020 -0.0104 -0.1604 130 LYS B CG 724 C CD . LYS A 99 ? 1.4427 0.8541 0.9733 0.0097 -0.0259 -0.1557 130 LYS B CD 725 C CE . LYS A 99 ? 1.4612 0.8480 0.9660 0.0039 -0.0361 -0.1502 130 LYS B CE 726 N NZ . LYS A 99 ? 1.4860 0.8567 0.9710 -0.0182 -0.0334 -0.1499 130 LYS B NZ 727 N N . LEU A 100 ? 1.2203 0.6611 0.7709 0.0232 -0.0062 -0.1511 131 LEU B N 728 C CA . LEU A 100 ? 1.2288 0.6587 0.7640 0.0185 -0.0069 -0.1472 131 LEU B CA 729 C C . LEU A 100 ? 1.2383 0.6503 0.7557 0.0231 -0.0214 -0.1421 131 LEU B C 730 O O . LEU A 100 ? 1.2273 0.6441 0.7512 0.0377 -0.0296 -0.1414 131 LEU B O 731 C CB . LEU A 100 ? 1.2117 0.6561 0.7602 0.0288 -0.0028 -0.1458 131 LEU B CB 732 C CG . LEU A 100 ? 1.2011 0.6624 0.7688 0.0266 0.0098 -0.1503 131 LEU B CG 733 C CD1 . LEU A 100 ? 1.1841 0.6580 0.7642 0.0407 0.0084 -0.1470 131 LEU B CD1 734 C CD2 . LEU A 100 ? 1.2141 0.6685 0.7713 0.0105 0.0185 -0.1525 131 LEU B CD2 735 N N . THR A 101 ? 1.0843 0.4755 0.5793 0.0100 -0.0254 -0.1393 132 THR B N 736 C CA . THR A 101 ? 1.0958 0.4698 0.5758 0.0150 -0.0398 -0.1344 132 THR B CA 737 C C . THR A 101 ? 1.0958 0.4679 0.5702 0.0150 -0.0386 -0.1309 132 THR B C 738 O O . THR A 101 ? 1.0987 0.4631 0.5680 0.0239 -0.0499 -0.1280 132 THR B O 739 C CB . THR A 101 ? 1.1236 0.4713 0.5812 0.0029 -0.0510 -0.1321 132 THR B CB 740 O OG1 . THR A 101 ? 1.1401 0.4802 0.5843 -0.0186 -0.0423 -0.1324 132 THR B OG1 741 C CG2 . THR A 101 ? 1.1216 0.4705 0.5861 0.0093 -0.0571 -0.1349 132 THR B CG2 742 N N . THR A 102 ? 1.0695 0.4507 0.5476 0.0064 -0.0250 -0.1323 133 THR B N 743 C CA . THR A 102 ? 1.0717 0.4491 0.5419 0.0037 -0.0234 -0.1289 133 THR B CA 744 C C . THR A 102 ? 1.0513 0.4495 0.5389 0.0064 -0.0094 -0.1316 133 THR B C 745 O O . THR A 102 ? 1.0471 0.4553 0.5437 -0.0018 0.0027 -0.1368 133 THR B O 746 C CB . THR A 102 ? 1.0993 0.4549 0.5437 -0.0172 -0.0242 -0.1264 133 THR B CB 747 O OG1 . THR A 102 ? 1.1215 0.4550 0.5487 -0.0216 -0.0385 -0.1233 133 THR B OG1 748 C CG2 . THR A 102 ? 1.1038 0.4526 0.5381 -0.0188 -0.0259 -0.1220 133 THR B CG2 749 N N . LEU A 103 ? 1.0422 0.4471 0.5352 0.0176 -0.0114 -0.1288 134 LEU B N 750 C CA . LEU A 103 ? 1.0251 0.4480 0.5344 0.0202 0.0002 -0.1308 134 LEU B CA 751 C C . LEU A 103 ? 1.0262 0.4464 0.5287 0.0205 0.0001 -0.1269 134 LEU B C 752 O O . LEU A 103 ? 1.0217 0.4428 0.5244 0.0321 -0.0081 -0.1233 134 LEU B O 753 C CB . LEU A 103 ? 1.0036 0.4454 0.5342 0.0362 -0.0006 -0.1318 134 LEU B CB 754 C CG . LEU A 103 ? 0.9865 0.4467 0.5369 0.0395 0.0095 -0.1339 134 LEU B CG 755 C CD1 . LEU A 103 ? 0.9841 0.4512 0.5471 0.0326 0.0179 -0.1404 134 LEU B CD1 756 C CD2 . LEU A 103 ? 0.9706 0.4445 0.5335 0.0553 0.0042 -0.1315 134 LEU B CD2 757 N N . ASP A 104 ? 1.1532 0.5721 0.6514 0.0080 0.0098 -0.1285 135 ASP B N 758 C CA . ASP A 104 ? 1.1548 0.5713 0.6469 0.0084 0.0096 -0.1247 135 ASP B CA 759 C C . ASP A 104 ? 1.1385 0.5736 0.6500 0.0112 0.0213 -0.1281 135 ASP B C 760 O O . ASP A 104 ? 1.1392 0.5786 0.6556 0.0006 0.0323 -0.1338 135 ASP B O 761 C CB . ASP A 104 ? 1.1779 0.5739 0.6447 -0.0090 0.0086 -0.1227 135 ASP B CB 762 C CG . ASP A 104 ? 1.1816 0.5724 0.6399 -0.0079 0.0054 -0.1178 135 ASP B CG 763 O OD1 . ASP A 104 ? 1.1649 0.5711 0.6388 0.0032 0.0090 -0.1177 135 ASP B OD1 764 O OD2 . ASP A 104 ? 1.2022 0.5729 0.6376 -0.0187 -0.0011 -0.1137 135 ASP B OD2 765 N N . ILE A 105 ? 1.1183 0.5652 0.6421 0.0255 0.0185 -0.1252 136 ILE B N 766 C CA . ILE A 105 ? 1.1056 0.5672 0.6459 0.0285 0.0267 -0.1267 136 ILE B CA 767 C C . ILE A 105 ? 1.1094 0.5673 0.6412 0.0273 0.0268 -0.1227 136 ILE B C 768 O O . ILE A 105 ? 1.0987 0.5685 0.6434 0.0332 0.0302 -0.1219 136 ILE B O 769 C CB . ILE A 105 ? 1.0886 0.5676 0.6503 0.0422 0.0253 -0.1266 136 ILE B CB 770 C CG1 . ILE A 105 ? 1.0856 0.5666 0.6436 0.0545 0.0148 -0.1213 136 ILE B CG1 771 C CG2 . ILE A 105 ? 1.0854 0.5684 0.6573 0.0413 0.0272 -0.1316 136 ILE B CG2 772 C CD1 . ILE A 105 ? 1.0708 0.5692 0.6464 0.0656 0.0138 -0.1201 136 ILE B CD1 773 N N . SER A 106 ? 1.0466 0.4875 0.5567 0.0206 0.0210 -0.1193 137 SER B N 774 C CA . SER A 106 ? 1.0514 0.4874 0.5521 0.0213 0.0178 -0.1145 137 SER B CA 775 C C . SER A 106 ? 1.0523 0.4898 0.5525 0.0123 0.0276 -0.1158 137 SER B C 776 O O . SER A 106 ? 1.0559 0.4926 0.5558 0.0000 0.0373 -0.1213 137 SER B O 777 C CB . SER A 106 ? 1.0707 0.4861 0.5486 0.0164 0.0067 -0.1105 137 SER B CB 778 O OG . SER A 106 ? 1.0871 0.4882 0.5498 -0.0004 0.0100 -0.1125 137 SER B OG 779 N N . ARG A 107 ? 1.2377 0.6777 0.7374 0.0182 0.0247 -0.1114 138 ARG B N 780 C CA . ARG A 107 ? 1.2392 0.6797 0.7373 0.0113 0.0321 -0.1117 138 ARG B CA 781 C C . ARG A 107 ? 1.2247 0.6813 0.7446 0.0127 0.0429 -0.1169 138 ARG B C 782 O O . ARG A 107 ? 1.2269 0.6836 0.7471 0.0040 0.0513 -0.1203 138 ARG B O 783 C CB . ARG A 107 ? 1.2582 0.6809 0.7339 -0.0064 0.0343 -0.1125 138 ARG B CB 784 C CG . ARG A 107 ? 1.2761 0.6796 0.7297 -0.0083 0.0208 -0.1064 138 ARG B CG 785 C CD . ARG A 107 ? 1.2978 0.6821 0.7264 -0.0274 0.0214 -0.1053 138 ARG B CD 786 N NE . ARG A 107 ? 1.3159 0.6807 0.7252 -0.0277 0.0058 -0.0985 138 ARG B NE 787 C CZ . ARG A 107 ? 1.3200 0.6807 0.7246 -0.0226 -0.0019 -0.0934 138 ARG B CZ 788 N NH1 . ARG A 107 ? 1.3078 0.6824 0.7241 -0.0175 0.0054 -0.0939 138 ARG B NH1 789 N NH2 . ARG A 107 ? 1.3368 0.6791 0.7260 -0.0225 -0.0177 -0.0882 138 ARG B NH2 790 N N . ASN A 108 ? 1.1708 0.6406 0.7092 0.0237 0.0418 -0.1176 139 ASN B N 791 C CA . ASN A 108 ? 1.1591 0.6422 0.7198 0.0253 0.0494 -0.1228 139 ASN B CA 792 C C . ASN A 108 ? 1.1509 0.6452 0.7236 0.0372 0.0452 -0.1175 139 ASN B C 793 O O . ASN A 108 ? 1.1541 0.6468 0.7170 0.0421 0.0388 -0.1111 139 ASN B O 794 C CB . ASN A 108 ? 1.1533 0.6414 0.7260 0.0258 0.0513 -0.1283 139 ASN B CB 795 C CG . ASN A 108 ? 1.1639 0.6421 0.7247 0.0117 0.0567 -0.1343 139 ASN B CG 796 O OD1 . ASN A 108 ? 1.1605 0.6446 0.7337 0.0069 0.0635 -0.1424 139 ASN B OD1 797 N ND2 . ASN A 108 ? 1.1789 0.6419 0.7154 0.0041 0.0531 -0.1304 139 ASN B ND2 798 N N . SER A 109 ? 1.0414 0.5468 0.6352 0.0408 0.0484 -0.1204 140 SER B N 799 C CA . SER A 109 ? 1.0377 0.5525 0.6411 0.0498 0.0437 -0.1146 140 SER B CA 800 C C . SER A 109 ? 1.0336 0.5585 0.6472 0.0600 0.0365 -0.1108 140 SER B C 801 O O . SER A 109 ? 1.0345 0.5671 0.6555 0.0652 0.0329 -0.1060 140 SER B O 802 C CB . SER A 109 ? 1.0365 0.5545 0.6531 0.0467 0.0492 -0.1175 140 SER B CB 803 O OG . SER A 109 ? 1.0411 0.5526 0.6438 0.0418 0.0512 -0.1151 140 SER B OG 804 N N . PHE A 110 ? 1.0768 0.6015 0.6899 0.0619 0.0342 -0.1127 141 PHE B N 805 C CA . PHE A 110 ? 1.0734 0.6077 0.6967 0.0701 0.0281 -0.1103 141 PHE B CA 806 C C . PHE A 110 ? 1.0773 0.6195 0.6965 0.0768 0.0215 -0.1029 141 PHE B C 807 O O . PHE A 110 ? 1.0809 0.6203 0.6860 0.0772 0.0197 -0.1003 141 PHE B O 808 C CB . PHE A 110 ? 1.0719 0.6031 0.6883 0.0714 0.0253 -0.1123 141 PHE B CB 809 C CG . PHE A 110 ? 1.0698 0.5961 0.6915 0.0649 0.0309 -0.1197 141 PHE B CG 810 C CD1 . PHE A 110 ? 1.0758 0.5912 0.6859 0.0551 0.0368 -0.1236 141 PHE B CD1 811 C CD2 . PHE A 110 ? 1.0642 0.5970 0.7016 0.0676 0.0301 -0.1228 141 PHE B CD2 812 C CE1 . PHE A 110 ? 1.0765 0.5891 0.6907 0.0473 0.0427 -0.1312 141 PHE B CE1 813 C CE2 . PHE A 110 ? 1.0632 0.5932 0.7067 0.0612 0.0357 -0.1307 141 PHE B CE2 814 C CZ . PHE A 110 ? 1.0696 0.5902 0.7014 0.0507 0.0425 -0.1352 141 PHE B CZ 815 N N . ASP A 111 ? 1.1646 0.7167 0.7956 0.0811 0.0173 -0.0996 142 ASP B N 816 C CA . ASP A 111 ? 1.1724 0.7334 0.7980 0.0851 0.0118 -0.0929 142 ASP B CA 817 C C . ASP A 111 ? 1.1783 0.7499 0.8083 0.0897 0.0053 -0.0898 142 ASP B C 818 O O . ASP A 111 ? 1.1745 0.7461 0.8099 0.0912 0.0040 -0.0928 142 ASP B O 819 C CB . ASP A 111 ? 1.1790 0.7406 0.8076 0.0825 0.0130 -0.0891 142 ASP B CB 820 C CG . ASP A 111 ? 1.1905 0.7590 0.8322 0.0836 0.0080 -0.0847 142 ASP B CG 821 O OD1 . ASP A 111 ? 1.1902 0.7582 0.8457 0.0842 0.0067 -0.0874 142 ASP B OD1 822 O OD2 . ASP A 111 ? 1.2028 0.7773 0.8404 0.0835 0.0045 -0.0784 142 ASP B OD2 823 N N . SER A 112 ? 1.3442 0.9253 0.9706 0.0908 0.0012 -0.0840 143 SER B N 824 C CA . SER A 112 ? 1.3561 0.9488 0.9830 0.0929 -0.0050 -0.0804 143 SER B CA 825 C C . SER A 112 ? 1.3479 0.9441 0.9667 0.0969 -0.0061 -0.0846 143 SER B C 826 O O . SER A 112 ? 1.3399 0.9332 0.9495 0.0983 -0.0043 -0.0877 143 SER B O 827 C CB . SER A 112 ? 1.3632 0.9551 1.0048 0.0921 -0.0085 -0.0791 143 SER B CB 828 O OG . SER A 112 ? 1.3492 0.9348 0.9969 0.0935 -0.0061 -0.0854 143 SER B OG 829 N N . SER A 113 ? 1.1045 0.7059 0.7272 0.0986 -0.0099 -0.0850 144 SER B N 830 C CA . SER A 113 ? 1.0988 0.7047 0.7140 0.1026 -0.0115 -0.0895 144 SER B CA 831 C C . SER A 113 ? 1.0843 0.6788 0.7015 0.1039 -0.0096 -0.0950 144 SER B C 832 O O . SER A 113 ? 1.0786 0.6637 0.7037 0.1010 -0.0063 -0.0960 144 SER B O 833 C CB . SER A 113 ? 1.1122 0.7314 0.7276 0.1032 -0.0168 -0.0877 144 SER B CB 834 O OG . SER A 113 ? 1.1235 0.7564 0.7302 0.1032 -0.0180 -0.0871 144 SER B OG 835 N N . PHE A 114 ? 0.9187 0.5149 0.5290 0.1077 -0.0119 -0.0995 145 PHE B N 836 C CA . PHE A 114 ? 0.9159 0.5016 0.5265 0.1084 -0.0115 -0.1042 145 PHE B CA 837 C C . PHE A 114 ? 0.9155 0.5078 0.5314 0.1106 -0.0151 -0.1054 145 PHE B C 838 O O . PHE A 114 ? 0.9174 0.5202 0.5292 0.1141 -0.0192 -0.1070 145 PHE B O 839 C CB . PHE A 114 ? 0.9175 0.4960 0.5174 0.1107 -0.0131 -0.1085 145 PHE B CB 840 C CG . PHE A 114 ? 0.9185 0.4814 0.5162 0.1081 -0.0119 -0.1118 145 PHE B CG 841 C CD1 . PHE A 114 ? 0.9182 0.4801 0.5175 0.1101 -0.0148 -0.1153 145 PHE B CD1 842 C CD2 . PHE A 114 ? 0.9213 0.4710 0.5150 0.1022 -0.0075 -0.1115 145 PHE B CD2 843 C CE1 . PHE A 114 ? 0.9211 0.4688 0.5177 0.1063 -0.0137 -0.1181 145 PHE B CE1 844 C CE2 . PHE A 114 ? 0.9251 0.4611 0.5153 0.0974 -0.0060 -0.1146 145 PHE B CE2 845 C CZ . PHE A 114 ? 0.9252 0.4602 0.5169 0.0993 -0.0092 -0.1177 145 PHE B CZ 846 N N . PRO A 115 ? 1.1357 0.7227 0.7617 0.1081 -0.0137 -0.1055 146 PRO B N 847 C CA . PRO A 115 ? 1.1367 0.7280 0.7700 0.1092 -0.0172 -0.1061 146 PRO B CA 848 C C . PRO A 115 ? 1.1326 0.7247 0.7586 0.1131 -0.0203 -0.1108 146 PRO B C 849 O O . PRO A 115 ? 1.1265 0.7092 0.7453 0.1137 -0.0192 -0.1147 146 PRO B O 850 C CB . PRO A 115 ? 1.1299 0.7116 0.7747 0.1058 -0.0134 -0.1084 146 PRO B CB 851 C CG . PRO A 115 ? 1.1269 0.6984 0.7661 0.1025 -0.0076 -0.1105 146 PRO B CG 852 C CD . PRO A 115 ? 1.1324 0.7082 0.7638 0.1035 -0.0080 -0.1065 146 PRO B CD 853 N N . PRO A 116 ? 1.1414 0.7438 0.7689 0.1151 -0.0249 -0.1105 147 PRO B N 854 C CA . PRO A 116 ? 1.1384 0.7451 0.7589 0.1193 -0.0285 -0.1157 147 PRO B CA 855 C C . PRO A 116 ? 1.1287 0.7238 0.7499 0.1202 -0.0289 -0.1206 147 PRO B C 856 O O . PRO A 116 ? 1.1252 0.7179 0.7391 0.1238 -0.0315 -0.1256 147 PRO B O 857 C CB . PRO A 116 ? 1.1495 0.7706 0.7720 0.1189 -0.0327 -0.1132 147 PRO B CB 858 C CG . PRO A 116 ? 1.1628 0.7795 0.7967 0.1151 -0.0328 -0.1081 147 PRO B CG 859 C CD . PRO A 116 ? 1.1533 0.7617 0.7904 0.1129 -0.0279 -0.1059 147 PRO B CD 860 N N . GLY A 117 ? 1.2908 0.8784 0.9209 0.1168 -0.0267 -0.1200 148 GLY B N 861 C CA . GLY A 117 ? 1.2857 0.8660 0.9174 0.1167 -0.0278 -0.1244 148 GLY B CA 862 C C . GLY A 117 ? 1.2824 0.8482 0.9051 0.1157 -0.0271 -0.1287 148 GLY B C 863 O O . GLY A 117 ? 1.2811 0.8394 0.9045 0.1140 -0.0278 -0.1320 148 GLY B O 864 N N . ILE A 118 ? 0.9165 0.4777 0.5300 0.1161 -0.0267 -0.1285 149 ILE B N 865 C CA . ILE A 118 ? 0.9228 0.4673 0.5263 0.1131 -0.0269 -0.1309 149 ILE B CA 866 C C . ILE A 118 ? 0.9287 0.4652 0.5257 0.1156 -0.0335 -0.1355 149 ILE B C 867 O O . ILE A 118 ? 0.9378 0.4582 0.5277 0.1105 -0.0341 -0.1368 149 ILE B O 868 C CB . ILE A 118 ? 0.9251 0.4669 0.5207 0.1135 -0.0267 -0.1291 149 ILE B CB 869 C CG1 . ILE A 118 ? 0.9353 0.4607 0.5182 0.1130 -0.0321 -0.1317 149 ILE B CG1 870 C CG2 . ILE A 118 ? 0.9204 0.4800 0.5188 0.1195 -0.0283 -0.1276 149 ILE B CG2 871 C CD1 . ILE A 118 ? 0.9435 0.4509 0.5191 0.1030 -0.0283 -0.1306 149 ILE B CD1 872 N N . SER A 119 ? 1.1316 0.6791 0.7307 0.1225 -0.0387 -0.1382 150 SER B N 873 C CA . SER A 119 ? 1.1333 0.6733 0.7274 0.1257 -0.0457 -0.1434 150 SER B CA 874 C C . SER A 119 ? 1.1337 0.6661 0.7305 0.1209 -0.0447 -0.1440 150 SER B C 875 O O . SER A 119 ? 1.1371 0.6592 0.7288 0.1214 -0.0503 -0.1476 150 SER B O 876 C CB . SER A 119 ? 1.1310 0.6864 0.7272 0.1340 -0.0510 -0.1481 150 SER B CB 877 O OG . SER A 119 ? 1.1290 0.6988 0.7328 0.1341 -0.0490 -0.1468 150 SER B OG 878 N N . LYS A 120 ? 1.1822 0.7195 0.7883 0.1163 -0.0380 -0.1409 151 LYS B N 879 C CA . LYS A 120 ? 1.1827 0.7159 0.7945 0.1117 -0.0365 -0.1424 151 LYS B CA 880 C C . LYS A 120 ? 1.1912 0.7057 0.7942 0.1035 -0.0352 -0.1440 151 LYS B C 881 O O . LYS A 120 ? 1.1948 0.7034 0.7983 0.0999 -0.0361 -0.1465 151 LYS B O 882 C CB . LYS A 120 ? 1.1792 0.7228 0.8059 0.1093 -0.0308 -0.1399 151 LYS B CB 883 C CG . LYS A 120 ? 1.1782 0.7239 0.8156 0.1072 -0.0308 -0.1421 151 LYS B CG 884 C CD . LYS A 120 ? 1.1759 0.7353 0.8288 0.1090 -0.0305 -0.1393 151 LYS B CD 885 C CE . LYS A 120 ? 1.1753 0.7390 0.8314 0.1085 -0.0269 -0.1352 151 LYS B CE 886 N NZ . LYS A 120 ? 1.1748 0.7503 0.8432 0.1105 -0.0297 -0.1311 151 LYS B NZ 887 N N . LEU A 121 ? 0.9938 0.4988 0.5877 0.0995 -0.0333 -0.1422 152 LEU B N 888 C CA . LEU A 121 ? 1.0071 0.4931 0.5886 0.0896 -0.0329 -0.1428 152 LEU B CA 889 C C . LEU A 121 ? 1.0177 0.4897 0.5878 0.0907 -0.0431 -0.1449 152 LEU B C 890 O O . LEU A 121 ? 1.0265 0.4892 0.5933 0.0838 -0.0435 -0.1466 152 LEU B O 891 C CB . LEU A 121 ? 1.0121 0.4912 0.5848 0.0856 -0.0305 -0.1399 152 LEU B CB 892 C CG . LEU A 121 ? 1.0097 0.4939 0.5890 0.0787 -0.0195 -0.1387 152 LEU B CG 893 C CD1 . LEU A 121 ? 1.0062 0.4976 0.5995 0.0735 -0.0123 -0.1421 152 LEU B CD1 894 C CD2 . LEU A 121 ? 0.9994 0.4967 0.5859 0.0859 -0.0179 -0.1358 152 LEU B CD2 895 N N . LYS A 122 ? 1.1689 0.6387 0.7332 0.0988 -0.0516 -0.1454 153 LYS B N 896 C CA . LYS A 122 ? 1.1729 0.6346 0.7321 0.1045 -0.0631 -0.1491 153 LYS B CA 897 C C . LYS A 122 ? 1.1907 0.6274 0.7348 0.0964 -0.0705 -0.1487 153 LYS B C 898 O O . LYS A 122 ? 1.1966 0.6222 0.7340 0.1014 -0.0823 -0.1508 153 LYS B O 899 C CB . LYS A 122 ? 1.1655 0.6381 0.7347 0.1081 -0.0628 -0.1522 153 LYS B CB 900 C CG . LYS A 122 ? 1.1709 0.6344 0.7357 0.1122 -0.0738 -0.1567 153 LYS B CG 901 C CD . LYS A 122 ? 1.1665 0.6354 0.7322 0.1241 -0.0827 -0.1614 153 LYS B CD 902 C CE . LYS A 122 ? 1.1491 0.6431 0.7253 0.1314 -0.0771 -0.1619 153 LYS B CE 903 N NZ . LYS A 122 ? 1.1435 0.6548 0.7296 0.1326 -0.0718 -0.1620 153 LYS B NZ 904 N N . PHE A 123 ? 1.2966 0.7235 0.8344 0.0831 -0.0642 -0.1462 154 PHE B N 905 C CA . PHE A 123 ? 1.3178 0.7196 0.8379 0.0724 -0.0713 -0.1447 154 PHE B CA 906 C C . PHE A 123 ? 1.3273 0.7198 0.8367 0.0656 -0.0696 -0.1406 154 PHE B C 907 O O . PHE A 123 ? 1.3476 0.7179 0.8392 0.0544 -0.0754 -0.1378 154 PHE B O 908 C CB . PHE A 123 ? 1.3265 0.7239 0.8445 0.0596 -0.0652 -0.1453 154 PHE B CB 909 C CG . PHE A 123 ? 1.3273 0.7212 0.8468 0.0630 -0.0729 -0.1484 154 PHE B CG 910 C CD1 . PHE A 123 ? 1.3150 0.7174 0.8430 0.0783 -0.0807 -0.1516 154 PHE B CD1 911 C CD2 . PHE A 123 ? 1.3409 0.7237 0.8529 0.0502 -0.0721 -0.1487 154 PHE B CD2 912 C CE1 . PHE A 123 ? 1.3154 0.7146 0.8449 0.0815 -0.0879 -0.1551 154 PHE B CE1 913 C CE2 . PHE A 123 ? 1.3417 0.7206 0.8549 0.0534 -0.0797 -0.1515 154 PHE B CE2 914 C CZ . PHE A 123 ? 1.3285 0.7154 0.8506 0.0694 -0.0877 -0.1546 154 PHE B CZ 915 N N . LEU A 124 ? 1.0340 0.4436 0.5537 0.0719 -0.0622 -0.1400 155 LEU B N 916 C CA . LEU A 124 ? 1.0363 0.4415 0.5488 0.0667 -0.0588 -0.1363 155 LEU B CA 917 C C . LEU A 124 ? 1.0541 0.4396 0.5520 0.0678 -0.0727 -0.1344 155 LEU B C 918 O O . LEU A 124 ? 1.0533 0.4404 0.5557 0.0803 -0.0834 -0.1373 155 LEU B O 919 C CB . LEU A 124 ? 1.0140 0.4418 0.5416 0.0758 -0.0509 -0.1363 155 LEU B CB 920 C CG . LEU A 124 ? 1.0131 0.4399 0.5362 0.0704 -0.0448 -0.1329 155 LEU B CG 921 C CD1 . LEU A 124 ? 1.0111 0.4407 0.5368 0.0582 -0.0318 -0.1331 155 LEU B CD1 922 C CD2 . LEU A 124 ? 0.9955 0.4408 0.5303 0.0822 -0.0432 -0.1326 155 LEU B CD2 923 N N . LYS A 125 ? 1.1486 0.5157 0.6296 0.0541 -0.0730 -0.1303 156 LYS B N 924 C CA . LYS A 125 ? 1.1646 0.5106 0.6309 0.0532 -0.0871 -0.1274 156 LYS B CA 925 C C . LYS A 125 ? 1.1613 0.5130 0.6279 0.0546 -0.0831 -0.1248 156 LYS B C 926 O O . LYS A 125 ? 1.1556 0.5109 0.6277 0.0667 -0.0912 -0.1260 156 LYS B O 927 C CB . LYS A 125 ? 1.1916 0.5095 0.6350 0.0353 -0.0937 -0.1235 156 LYS B CB 928 C CG . LYS A 125 ? 1.1998 0.5085 0.6407 0.0333 -0.1005 -0.1256 156 LYS B CG 929 C CD . LYS A 125 ? 1.2291 0.5045 0.6470 0.0223 -0.1176 -0.1214 156 LYS B CD 930 C CE . LYS A 125 ? 1.2304 0.4968 0.6489 0.0254 -0.1285 -0.1242 156 LYS B CE 931 N NZ . LYS A 125 ? 1.2122 0.4898 0.6492 0.0473 -0.1376 -0.1305 156 LYS B NZ 932 N N . VAL A 126 ? 1.1056 0.4587 0.5670 0.0421 -0.0705 -0.1222 157 VAL B N 933 C CA . VAL A 126 ? 1.1034 0.4592 0.5625 0.0407 -0.0661 -0.1193 157 VAL B CA 934 C C . VAL A 126 ? 1.0787 0.4606 0.5559 0.0466 -0.0513 -0.1210 157 VAL B C 935 O O . VAL A 126 ? 1.0725 0.4630 0.5556 0.0396 -0.0391 -0.1228 157 VAL B O 936 C CB . VAL A 126 ? 1.1230 0.4621 0.5626 0.0203 -0.0614 -0.1156 157 VAL B CB 937 C CG1 . VAL A 126 ? 1.1323 0.4615 0.5613 0.0184 -0.0665 -0.1113 157 VAL B CG1 938 C CG2 . VAL A 126 ? 1.1471 0.4634 0.5690 0.0077 -0.0699 -0.1143 157 VAL B CG2 939 N N . PHE A 127 ? 1.1349 0.5292 0.6212 0.0585 -0.0525 -0.1207 158 PHE B N 940 C CA . PHE A 127 ? 1.1179 0.5336 0.6186 0.0618 -0.0398 -0.1209 158 PHE B CA 941 C C . PHE A 127 ? 1.1214 0.5356 0.6169 0.0600 -0.0384 -0.1176 158 PHE B C 942 O O . PHE A 127 ? 1.1219 0.5358 0.6169 0.0685 -0.0472 -0.1169 158 PHE B O 943 C CB . PHE A 127 ? 1.0988 0.5359 0.6173 0.0768 -0.0402 -0.1237 158 PHE B CB 944 C CG . PHE A 127 ? 1.0842 0.5414 0.6162 0.0804 -0.0301 -0.1227 158 PHE B CG 945 C CD1 . PHE A 127 ? 1.0783 0.5428 0.6187 0.0743 -0.0189 -0.1231 158 PHE B CD1 946 C CD2 . PHE A 127 ? 1.0776 0.5466 0.6146 0.0897 -0.0326 -0.1219 158 PHE B CD2 947 C CE1 . PHE A 127 ? 1.0668 0.5474 0.6199 0.0777 -0.0119 -0.1219 158 PHE B CE1 948 C CE2 . PHE A 127 ? 1.0673 0.5529 0.6149 0.0918 -0.0247 -0.1201 158 PHE B CE2 949 C CZ . PHE A 127 ? 1.0622 0.5525 0.6176 0.0860 -0.0151 -0.1197 158 PHE B CZ 950 N N . ASN A 128 ? 1.1595 0.5731 0.6520 0.0488 -0.0275 -0.1164 159 ASN B N 951 C CA . ASN A 128 ? 1.1615 0.5750 0.6500 0.0473 -0.0255 -0.1133 159 ASN B CA 952 C C . ASN A 128 ? 1.1459 0.5789 0.6496 0.0500 -0.0135 -0.1138 159 ASN B C 953 O O . ASN A 128 ? 1.1450 0.5803 0.6516 0.0407 -0.0027 -0.1157 159 ASN B O 954 C CB . ASN A 128 ? 1.1823 0.5748 0.6500 0.0308 -0.0255 -0.1109 159 ASN B CB 955 C CG . ASN A 128 ? 1.1903 0.5763 0.6493 0.0307 -0.0302 -0.1069 159 ASN B CG 956 O OD1 . ASN A 128 ? 1.1773 0.5784 0.6477 0.0390 -0.0262 -0.1065 159 ASN B OD1 957 N ND2 . ASN A 128 ? 1.2131 0.5756 0.6513 0.0210 -0.0398 -0.1035 159 ASN B ND2 958 N N . ALA A 129 ? 1.0762 0.5230 0.5898 0.0622 -0.0161 -0.1128 160 ALA B N 959 C CA . ALA A 129 ? 1.0635 0.5277 0.5906 0.0657 -0.0077 -0.1120 160 ALA B CA 960 C C . ALA A 129 ? 1.0687 0.5302 0.5893 0.0636 -0.0073 -0.1086 160 ALA B C 961 O O . ALA A 129 ? 1.0602 0.5354 0.5906 0.0679 -0.0029 -0.1072 160 ALA B O 962 C CB . ALA A 129 ? 1.0501 0.5327 0.5914 0.0784 -0.0103 -0.1126 160 ALA B CB 963 N N . PHE A 130 ? 1.0901 0.5335 0.5937 0.0575 -0.0135 -0.1069 161 PHE B N 964 C CA . PHE A 130 ? 1.0969 0.5364 0.5933 0.0567 -0.0159 -0.1036 161 PHE B CA 965 C C . PHE A 130 ? 1.0941 0.5382 0.5927 0.0494 -0.0045 -0.1025 161 PHE B C 966 O O . PHE A 130 ? 1.0960 0.5358 0.5927 0.0387 0.0041 -0.1047 161 PHE B O 967 C CB . PHE A 130 ? 1.1169 0.5333 0.5939 0.0501 -0.0265 -0.1016 161 PHE B CB 968 C CG . PHE A 130 ? 1.1267 0.5360 0.5941 0.0459 -0.0283 -0.0980 161 PHE B CG 969 C CD1 . PHE A 130 ? 1.1236 0.5411 0.5969 0.0566 -0.0349 -0.0973 161 PHE B CD1 970 C CD2 . PHE A 130 ? 1.1396 0.5353 0.5924 0.0306 -0.0229 -0.0961 161 PHE B CD2 971 C CE1 . PHE A 130 ? 1.1332 0.5445 0.5984 0.0528 -0.0368 -0.0939 161 PHE B CE1 972 C CE2 . PHE A 130 ? 1.1493 0.5381 0.5927 0.0262 -0.0247 -0.0926 161 PHE B CE2 973 C CZ . PHE A 130 ? 1.1460 0.5422 0.5958 0.0377 -0.0320 -0.0912 161 PHE B CZ 974 N N . SER A 131 ? 1.2514 0.7047 0.7545 0.0549 -0.0046 -0.1001 162 SER B N 975 C CA . SER A 131 ? 1.2477 0.7068 0.7550 0.0500 0.0050 -0.0991 162 SER B CA 976 C C . SER A 131 ? 1.2341 0.7074 0.7589 0.0510 0.0146 -0.1016 162 SER B C 977 O O . SER A 131 ? 1.2356 0.7056 0.7619 0.0419 0.0229 -0.1049 162 SER B O 978 C CB . SER A 131 ? 1.2614 0.7035 0.7525 0.0357 0.0083 -0.0986 162 SER B CB 979 O OG . SER A 131 ? 1.2562 0.7048 0.7529 0.0315 0.0177 -0.0989 162 SER B OG 980 N N . ASN A 132 ? 0.9588 0.4481 0.4972 0.0616 0.0126 -0.1006 163 ASN B N 981 C CA . ASN A 132 ? 0.9475 0.4495 0.5031 0.0636 0.0186 -0.1018 163 ASN B CA 982 C C . ASN A 132 ? 0.9404 0.4565 0.5037 0.0708 0.0165 -0.0976 163 ASN B C 983 O O . ASN A 132 ? 0.9437 0.4605 0.4993 0.0736 0.0120 -0.0949 163 ASN B O 984 C CB . ASN A 132 ? 0.9433 0.4492 0.5064 0.0673 0.0170 -0.1047 163 ASN B CB 985 C CG . ASN A 132 ? 0.9488 0.4443 0.5095 0.0581 0.0221 -0.1097 163 ASN B CG 986 O OD1 . ASN A 132 ? 0.9489 0.4432 0.5141 0.0505 0.0301 -0.1128 163 ASN B OD1 987 N ND2 . ASN A 132 ? 0.9541 0.4432 0.5083 0.0585 0.0175 -0.1112 163 ASN B ND2 988 N N . ASN A 133 ? 1.1110 0.6377 0.6892 0.0729 0.0191 -0.0972 164 ASN B N 989 C CA . ASN A 133 ? 1.1129 0.6526 0.6974 0.0777 0.0166 -0.0924 164 ASN B CA 990 C C . ASN A 133 ? 1.1132 0.6660 0.7020 0.0850 0.0107 -0.0909 164 ASN B C 991 O O . ASN A 133 ? 1.1185 0.6824 0.7135 0.0868 0.0090 -0.0869 164 ASN B O 992 C CB . ASN A 133 ? 1.1123 0.6540 0.7090 0.0743 0.0212 -0.0916 164 ASN B CB 993 C CG . ASN A 133 ? 1.1143 0.6452 0.7063 0.0666 0.0275 -0.0942 164 ASN B CG 994 O OD1 . ASN A 133 ? 1.1211 0.6446 0.6985 0.0640 0.0271 -0.0933 164 ASN B OD1 995 N ND2 . ASN A 133 ? 1.1096 0.6395 0.7144 0.0626 0.0329 -0.0980 164 ASN B ND2 996 N N . PHE A 134 ? 0.9811 0.5320 0.5664 0.0880 0.0077 -0.0941 165 PHE B N 997 C CA . PHE A 134 ? 0.9813 0.5447 0.5696 0.0943 0.0025 -0.0941 165 PHE B CA 998 C C . PHE A 134 ? 0.9877 0.5644 0.5730 0.0975 -0.0008 -0.0914 165 PHE B C 999 O O . PHE A 134 ? 0.9898 0.5643 0.5677 0.0977 -0.0017 -0.0916 165 PHE B O 1000 C CB . PHE A 134 ? 0.9780 0.5363 0.5606 0.0974 -0.0013 -0.0987 165 PHE B CB 1001 C CG . PHE A 134 ? 0.9735 0.5223 0.5595 0.0942 0.0013 -0.1016 165 PHE B CG 1002 C CD1 . PHE A 134 ? 0.9705 0.5239 0.5692 0.0929 0.0043 -0.1011 165 PHE B CD1 1003 C CD2 . PHE A 134 ? 0.9748 0.5095 0.5517 0.0917 0.0002 -0.1049 165 PHE B CD2 1004 C CE1 . PHE A 134 ? 0.9664 0.5127 0.5702 0.0896 0.0072 -0.1051 165 PHE B CE1 1005 C CE2 . PHE A 134 ? 0.9728 0.4997 0.5523 0.0871 0.0034 -0.1080 165 PHE B CE2 1006 C CZ . PHE A 134 ? 0.9675 0.5012 0.5612 0.0863 0.0074 -0.1086 165 PHE B CZ 1007 N N . GLU A 135 ? 1.1771 0.7678 0.7683 0.0991 -0.0028 -0.0890 166 GLU B N 1008 C CA . GLU A 135 ? 1.1860 0.7933 0.7742 0.1013 -0.0060 -0.0881 166 GLU B CA 1009 C C . GLU A 135 ? 1.1863 0.8038 0.7763 0.1049 -0.0095 -0.0913 166 GLU B C 1010 O O . GLU A 135 ? 1.1785 0.7889 0.7721 0.1058 -0.0098 -0.0932 166 GLU B O 1011 C CB . GLU A 135 ? 1.2000 0.8148 0.7910 0.0969 -0.0053 -0.0813 166 GLU B CB 1012 C CG . GLU A 135 ? 1.2115 0.8222 0.8120 0.0939 -0.0054 -0.0774 166 GLU B CG 1013 C CD . GLU A 135 ? 1.2181 0.8285 0.8224 0.0890 -0.0054 -0.0708 166 GLU B CD 1014 O OE1 . GLU A 135 ? 1.2152 0.8169 0.8189 0.0871 -0.0017 -0.0707 166 GLU B OE1 1015 O OE2 . GLU A 135 ? 1.2275 0.8456 0.8349 0.0865 -0.0098 -0.0657 166 GLU B OE2 1016 N N . GLY A 136 ? 1.1362 0.7711 0.7236 0.1063 -0.0120 -0.0926 167 GLY B N 1017 C CA . GLY A 136 ? 1.1381 0.7846 0.7263 0.1088 -0.0150 -0.0965 167 GLY B CA 1018 C C . GLY A 136 ? 1.1276 0.7754 0.7138 0.1154 -0.0176 -0.1057 167 GLY B C 1019 O O . GLY A 136 ? 1.1218 0.7583 0.7057 0.1177 -0.0181 -0.1082 167 GLY B O 1020 N N . LEU A 137 ? 0.9834 0.6443 0.5707 0.1179 -0.0202 -0.1109 168 LEU B N 1021 C CA . LEU A 137 ? 0.9753 0.6385 0.5629 0.1249 -0.0240 -0.1211 168 LEU B CA 1022 C C . LEU A 137 ? 0.9641 0.6059 0.5517 0.1276 -0.0259 -0.1223 168 LEU B C 1023 O O . LEU A 137 ? 0.9617 0.5932 0.5507 0.1243 -0.0238 -0.1173 168 LEU B O 1024 C CB . LEU A 137 ? 0.9802 0.6624 0.5692 0.1261 -0.0257 -0.1269 168 LEU B CB 1025 C CG . LEU A 137 ? 0.9863 0.6948 0.5738 0.1221 -0.0243 -0.1287 168 LEU B CG 1026 C CD1 . LEU A 137 ? 0.9914 0.7100 0.5793 0.1235 -0.0237 -0.1334 168 LEU B CD1 1027 C CD2 . LEU A 137 ? 0.9984 0.7099 0.5828 0.1131 -0.0223 -0.1175 168 LEU B CD2 1028 N N . LEU A 138 ? 0.9260 0.5609 0.5126 0.1331 -0.0306 -0.1294 169 LEU B N 1029 C CA . LEU A 138 ? 0.9270 0.5411 0.5116 0.1345 -0.0338 -0.1309 169 LEU B CA 1030 C C . LEU A 138 ? 0.9243 0.5432 0.5121 0.1352 -0.0340 -0.1325 169 LEU B C 1031 O O . LEU A 138 ? 0.9235 0.5610 0.5143 0.1379 -0.0353 -0.1374 169 LEU B O 1032 C CB . LEU A 138 ? 0.9321 0.5409 0.5160 0.1410 -0.0418 -0.1393 169 LEU B CB 1033 C CG . LEU A 138 ? 0.9379 0.5265 0.5157 0.1399 -0.0454 -0.1375 169 LEU B CG 1034 C CD1 . LEU A 138 ? 0.9367 0.5183 0.5101 0.1322 -0.0382 -0.1283 169 LEU B CD1 1035 C CD2 . LEU A 138 ? 0.9409 0.5379 0.5222 0.1461 -0.0518 -0.1448 169 LEU B CD2 1036 N N . PRO A 139 ? 0.9625 0.5663 0.5498 0.1319 -0.0324 -0.1288 170 PRO B N 1037 C CA . PRO A 139 ? 0.9609 0.5693 0.5519 0.1328 -0.0333 -0.1305 170 PRO B CA 1038 C C . PRO A 139 ? 0.9587 0.5701 0.5496 0.1396 -0.0399 -0.1399 170 PRO B C 1039 O O . PRO A 139 ? 0.9583 0.5552 0.5459 0.1420 -0.0447 -0.1433 170 PRO B O 1040 C CB . PRO A 139 ? 0.9595 0.5490 0.5503 0.1284 -0.0311 -0.1270 170 PRO B CB 1041 C CG . PRO A 139 ? 0.9603 0.5339 0.5450 0.1256 -0.0302 -0.1253 170 PRO B CG 1042 C CD . PRO A 139 ? 0.9613 0.5452 0.5452 0.1265 -0.0293 -0.1238 170 PRO B CD 1043 N N . SER A 140 ? 1.1849 0.8146 0.7791 0.1420 -0.0410 -0.1444 171 SER B N 1044 C CA . SER A 140 ? 1.1812 0.8150 0.7772 0.1488 -0.0473 -0.1551 171 SER B CA 1045 C C . SER A 140 ? 1.1776 0.7939 0.7726 0.1489 -0.0501 -0.1550 171 SER B C 1046 O O . SER A 140 ? 1.1756 0.7810 0.7700 0.1534 -0.0569 -0.1613 171 SER B O 1047 C CB . SER A 140 ? 1.1837 0.8432 0.7828 0.1497 -0.0465 -0.1607 171 SER B CB 1048 O OG . SER A 140 ? 1.1796 0.8453 0.7824 0.1570 -0.0525 -0.1734 171 SER B OG 1049 N N . ASP A 141 ? 1.2478 0.8607 0.8434 0.1434 -0.0455 -0.1476 172 ASP B N 1050 C CA . ASP A 141 ? 1.2452 0.8455 0.8413 0.1422 -0.0469 -0.1474 172 ASP B CA 1051 C C . ASP A 141 ? 1.2445 0.8218 0.8356 0.1424 -0.0513 -0.1493 172 ASP B C 1052 O O . ASP A 141 ? 1.2437 0.8139 0.8343 0.1445 -0.0562 -0.1537 172 ASP B O 1053 C CB . ASP A 141 ? 1.2469 0.8457 0.8464 0.1357 -0.0410 -0.1390 172 ASP B CB 1054 C CG . ASP A 141 ? 1.2440 0.8329 0.8460 0.1338 -0.0417 -0.1392 172 ASP B CG 1055 O OD1 . ASP A 141 ? 1.2466 0.8440 0.8509 0.1362 -0.0446 -0.1424 172 ASP B OD1 1056 O OD2 . ASP A 141 ? 1.2409 0.8144 0.8423 0.1293 -0.0390 -0.1367 172 ASP B OD2 1057 N N . VAL A 142 ? 1.1699 0.7352 0.7561 0.1395 -0.0502 -0.1459 173 VAL B N 1058 C CA . VAL A 142 ? 1.1751 0.7167 0.7536 0.1370 -0.0550 -0.1462 173 VAL B CA 1059 C C . VAL A 142 ? 1.1773 0.7140 0.7546 0.1442 -0.0660 -0.1544 173 VAL B C 1060 O O . VAL A 142 ? 1.1837 0.7005 0.7549 0.1424 -0.0724 -0.1554 173 VAL B O 1061 C CB . VAL A 142 ? 1.1805 0.7118 0.7528 0.1321 -0.0525 -0.1412 173 VAL B CB 1062 C CG1 . VAL A 142 ? 1.1789 0.7280 0.7556 0.1344 -0.0484 -0.1397 173 VAL B CG1 1063 C CG2 . VAL A 142 ? 1.1924 0.7052 0.7563 0.1331 -0.0621 -0.1438 173 VAL B CG2 1064 N N . SER A 143 ? 1.1683 0.7240 0.7521 0.1519 -0.0685 -0.1611 174 SER B N 1065 C CA . SER A 143 ? 1.1686 0.7236 0.7553 0.1601 -0.0791 -0.1714 174 SER B CA 1066 C C . SER A 143 ? 1.1676 0.7158 0.7547 0.1612 -0.0835 -0.1750 174 SER B C 1067 O O . SER A 143 ? 1.1688 0.7115 0.7581 0.1676 -0.0938 -0.1835 174 SER B O 1068 C CB . SER A 143 ? 1.1634 0.7456 0.7591 0.1669 -0.0785 -0.1796 174 SER B CB 1069 O OG . SER A 143 ? 1.1615 0.7483 0.7632 0.1747 -0.0868 -0.1915 174 SER B OG 1070 N N . ARG A 144 ? 1.1999 0.7490 0.7862 0.1556 -0.0766 -0.1694 175 ARG B N 1071 C CA . ARG A 144 ? 1.1996 0.7428 0.7864 0.1563 -0.0806 -0.1726 175 ARG B CA 1072 C C . ARG A 144 ? 1.2074 0.7249 0.7861 0.1494 -0.0830 -0.1681 175 ARG B C 1073 O O . ARG A 144 ? 1.2077 0.7207 0.7868 0.1490 -0.0857 -0.1703 175 ARG B O 1074 C CB . ARG A 144 ? 1.1938 0.7576 0.7868 0.1565 -0.0747 -0.1730 175 ARG B CB 1075 C CG . ARG A 144 ? 1.1905 0.7770 0.7895 0.1639 -0.0770 -0.1825 175 ARG B CG 1076 C CD . ARG A 144 ? 1.1903 0.7913 0.7926 0.1639 -0.0753 -0.1849 175 ARG B CD 1077 N NE . ARG A 144 ? 1.1946 0.7986 0.7966 0.1566 -0.0676 -0.1747 175 ARG B NE 1078 C CZ . ARG A 144 ? 1.1959 0.8143 0.7988 0.1534 -0.0616 -0.1695 175 ARG B CZ 1079 N NH1 . ARG A 144 ? 1.1922 0.8248 0.7954 0.1561 -0.0611 -0.1736 175 ARG B NH1 1080 N NH2 . ARG A 144 ? 1.2022 0.8207 0.8066 0.1473 -0.0567 -0.1606 175 ARG B NH2 1081 N N . LEU A 145 ? 1.1793 0.6803 0.7500 0.1429 -0.0822 -0.1622 176 LEU B N 1082 C CA . LEU A 145 ? 1.1910 0.6676 0.7519 0.1344 -0.0850 -0.1588 176 LEU B CA 1083 C C . LEU A 145 ? 1.2010 0.6600 0.7560 0.1383 -0.0995 -0.1634 176 LEU B C 1084 O O . LEU A 145 ? 1.2072 0.6582 0.7579 0.1387 -0.1042 -0.1625 176 LEU B O 1085 C CB . LEU A 145 ? 1.1978 0.6646 0.7512 0.1240 -0.0777 -0.1512 176 LEU B CB 1086 C CG . LEU A 145 ? 1.1877 0.6731 0.7489 0.1230 -0.0655 -0.1474 176 LEU B CG 1087 C CD1 . LEU A 145 ? 1.1937 0.6728 0.7487 0.1187 -0.0630 -0.1431 176 LEU B CD1 1088 C CD2 . LEU A 145 ? 1.1839 0.6708 0.7489 0.1156 -0.0569 -0.1446 176 LEU B CD2 1089 N N . ARG A 146 ? 1.3882 0.8395 0.9432 0.1408 -0.1078 -0.1682 177 ARG B N 1090 C CA . ARG A 146 ? 1.3969 0.8323 0.9493 0.1464 -0.1238 -0.1739 177 ARG B CA 1091 C C . ARG A 146 ? 1.4163 0.8219 0.9529 0.1362 -0.1307 -0.1671 177 ARG B C 1092 O O . ARG A 146 ? 1.4246 0.8169 0.9585 0.1396 -0.1433 -0.1692 177 ARG B O 1093 C CB . ARG A 146 ? 1.3958 0.8296 0.9525 0.1517 -0.1319 -0.1812 177 ARG B CB 1094 C CG . ARG A 146 ? 1.3901 0.8323 0.9483 0.1468 -0.1221 -0.1787 177 ARG B CG 1095 C CD . ARG A 146 ? 1.3748 0.8414 0.9459 0.1567 -0.1206 -0.1871 177 ARG B CD 1096 N NE . ARG A 146 ? 1.3763 0.8347 0.9488 0.1612 -0.1315 -0.1945 177 ARG B NE 1097 C CZ . ARG A 146 ? 1.3786 0.8420 0.9589 0.1722 -0.1419 -0.2059 177 ARG B CZ 1098 N NH1 . ARG A 146 ? 1.3767 0.8542 0.9644 0.1794 -0.1424 -0.2114 177 ARG B NH1 1099 N NH2 . ARG A 146 ? 1.3835 0.8387 0.9656 0.1759 -0.1518 -0.2128 177 ARG B NH2 1100 N N . PHE A 147 ? 1.1621 0.5583 0.6887 0.1229 -0.1223 -0.1593 178 PHE B N 1101 C CA . PHE A 147 ? 1.1840 0.5512 0.6926 0.1099 -0.1284 -0.1529 178 PHE B CA 1102 C C . PHE A 147 ? 1.1894 0.5535 0.6907 0.1031 -0.1228 -0.1469 178 PHE B C 1103 O O . PHE A 147 ? 1.2090 0.5495 0.6934 0.0908 -0.1275 -0.1412 178 PHE B O 1104 C CB . PHE A 147 ? 1.1917 0.5509 0.6923 0.0969 -0.1216 -0.1491 178 PHE B CB 1105 C CG . PHE A 147 ? 1.1905 0.5475 0.6947 0.1008 -0.1282 -0.1538 178 PHE B CG 1106 C CD1 . PHE A 147 ? 1.1979 0.5394 0.7000 0.1072 -0.1459 -0.1582 178 PHE B CD1 1107 C CD2 . PHE A 147 ? 1.1819 0.5524 0.6929 0.0983 -0.1175 -0.1544 178 PHE B CD2 1108 C CE1 . PHE A 147 ? 1.1968 0.5360 0.7024 0.1107 -0.1522 -0.1630 178 PHE B CE1 1109 C CE2 . PHE A 147 ? 1.1813 0.5498 0.6954 0.1015 -0.1236 -0.1587 178 PHE B CE2 1110 C CZ . PHE A 147 ? 1.1887 0.5416 0.6996 0.1076 -0.1406 -0.1630 178 PHE B CZ 1111 N N . LEU A 148 ? 1.1182 0.5055 0.6308 0.1098 -0.1129 -0.1477 179 LEU B N 1112 C CA . LEU A 148 ? 1.1210 0.5074 0.6283 0.1044 -0.1072 -0.1424 179 LEU B CA 1113 C C . LEU A 148 ? 1.1376 0.5024 0.6345 0.1040 -0.1223 -0.1414 179 LEU B C 1114 O O . LEU A 148 ? 1.1355 0.5020 0.6403 0.1161 -0.1343 -0.1477 179 LEU B O 1115 C CB . LEU A 148 ? 1.1016 0.5159 0.6238 0.1142 -0.0984 -0.1447 179 LEU B CB 1116 C CG . LEU A 148 ? 1.1036 0.5196 0.6218 0.1089 -0.0909 -0.1393 179 LEU B CG 1117 C CD1 . LEU A 148 ? 1.1015 0.5203 0.6177 0.0975 -0.0763 -0.1345 179 LEU B CD1 1118 C CD2 . LEU A 148 ? 1.0893 0.5289 0.6205 0.1199 -0.0879 -0.1424 179 LEU B CD2 1119 N N . GLU A 149 ? 1.2040 0.5491 0.6838 0.0898 -0.1219 -0.1343 180 GLU B N 1120 C CA . GLU A 149 ? 1.2232 0.5434 0.6899 0.0865 -0.1376 -0.1315 180 GLU B CA 1121 C C . GLU A 149 ? 1.2222 0.5483 0.6888 0.0868 -0.1335 -0.1286 180 GLU B C 1122 O O . GLU A 149 ? 1.2231 0.5474 0.6946 0.0961 -0.1451 -0.1315 180 GLU B O 1123 C CB . GLU A 149 ? 1.2489 0.5386 0.6926 0.0684 -0.1439 -0.1251 180 GLU B CB 1124 C CG . GLU A 149 ? 1.2564 0.5326 0.6979 0.0690 -0.1554 -0.1278 180 GLU B CG 1125 C CD . GLU A 149 ? 1.2839 0.5252 0.7000 0.0510 -0.1671 -0.1210 180 GLU B CD 1126 O OE1 . GLU A 149 ? 1.2870 0.5192 0.6974 0.0446 -0.1693 -0.1211 180 GLU B OE1 1127 O OE2 . GLU A 149 ? 1.3031 0.5257 0.7041 0.0424 -0.1746 -0.1153 180 GLU B OE2 1128 N N . GLU A 150 ? 1.4301 0.7616 0.8911 0.0758 -0.1180 -0.1235 181 GLU B N 1129 C CA . GLU A 150 ? 1.4291 0.7665 0.8891 0.0744 -0.1121 -0.1203 181 GLU B CA 1130 C C . GLU A 150 ? 1.4063 0.7742 0.8829 0.0806 -0.0949 -0.1221 181 GLU B C 1131 O O . GLU A 150 ? 1.3995 0.7762 0.8790 0.0749 -0.0821 -0.1216 181 GLU B O 1132 C CB . GLU A 150 ? 1.4497 0.7662 0.8879 0.0547 -0.1091 -0.1131 181 GLU B CB 1133 C CG . GLU A 150 ? 1.4469 0.7732 0.8847 0.0504 -0.0970 -0.1100 181 GLU B CG 1134 C CD . GLU A 150 ? 1.4669 0.7742 0.8828 0.0295 -0.0929 -0.1042 181 GLU B CD 1135 O OE1 . GLU A 150 ? 1.4847 0.7707 0.8846 0.0181 -0.1003 -0.1022 181 GLU B OE1 1136 O OE2 . GLU A 150 ? 1.4652 0.7789 0.8792 0.0239 -0.0825 -0.1021 181 GLU B OE2 1137 N N . LEU A 151 ? 1.0535 0.4369 0.5411 0.0917 -0.0955 -0.1243 182 LEU B N 1138 C CA . LEU A 151 ? 1.0299 0.4398 0.5307 0.0962 -0.0811 -0.1246 182 LEU B CA 1139 C C . LEU A 151 ? 1.0285 0.4423 0.5280 0.0953 -0.0781 -0.1214 182 LEU B C 1140 O O . LEU A 151 ? 1.0304 0.4465 0.5335 0.1036 -0.0870 -0.1239 182 LEU B O 1141 C CB . LEU A 151 ? 1.0141 0.4464 0.5320 0.1106 -0.0824 -0.1313 182 LEU B CB 1142 C CG . LEU A 151 ? 0.9952 0.4546 0.5262 0.1172 -0.0730 -0.1322 182 LEU B CG 1143 C CD1 . LEU A 151 ? 0.9850 0.4522 0.5176 0.1097 -0.0584 -0.1273 182 LEU B CD1 1144 C CD2 . LEU A 151 ? 0.9846 0.4632 0.5287 0.1286 -0.0756 -0.1395 182 LEU B CD2 1145 N N . ASN A 152 ? 1.1288 0.5445 0.6246 0.0857 -0.0654 -0.1169 183 ASN B N 1146 C CA . ASN A 152 ? 1.1301 0.5489 0.6240 0.0836 -0.0615 -0.1136 183 ASN B CA 1147 C C . ASN A 152 ? 1.1123 0.5561 0.6208 0.0881 -0.0490 -0.1139 183 ASN B C 1148 O O . ASN A 152 ? 1.1074 0.5546 0.6181 0.0815 -0.0382 -0.1126 183 ASN B O 1149 C CB . ASN A 152 ? 1.1440 0.5448 0.6216 0.0672 -0.0564 -0.1088 183 ASN B CB 1150 C CG . ASN A 152 ? 1.1626 0.5472 0.6267 0.0625 -0.0646 -0.1051 183 ASN B CG 1151 O OD1 . ASN A 152 ? 1.1586 0.5529 0.6270 0.0659 -0.0616 -0.1039 183 ASN B OD1 1152 N ND2 . ASN A 152 ? 1.1846 0.5433 0.6311 0.0535 -0.0755 -0.1028 183 ASN B ND2 1153 N N . PHE A 153 ? 1.0933 0.5546 0.6123 0.0989 -0.0510 -0.1161 184 PHE B N 1154 C CA . PHE A 153 ? 1.0803 0.5636 0.6109 0.1016 -0.0407 -0.1149 184 PHE B CA 1155 C C . PHE A 153 ? 1.0829 0.5700 0.6121 0.1000 -0.0376 -0.1116 184 PHE B C 1156 O O . PHE A 153 ? 1.0747 0.5788 0.6125 0.1017 -0.0305 -0.1100 184 PHE B O 1157 C CB . PHE A 153 ? 1.0693 0.5736 0.6126 0.1123 -0.0424 -0.1195 184 PHE B CB 1158 C CG . PHE A 153 ? 1.0594 0.5734 0.6104 0.1113 -0.0350 -0.1191 184 PHE B CG 1159 C CD1 . PHE A 153 ? 1.0566 0.5730 0.6105 0.1049 -0.0251 -0.1148 184 PHE B CD1 1160 C CD2 . PHE A 153 ? 1.0538 0.5738 0.6101 0.1169 -0.0387 -0.1235 184 PHE B CD2 1161 C CE1 . PHE A 153 ? 1.0488 0.5735 0.6117 0.1043 -0.0199 -0.1147 184 PHE B CE1 1162 C CE2 . PHE A 153 ? 1.0462 0.5743 0.6096 0.1157 -0.0330 -0.1228 184 PHE B CE2 1163 C CZ . PHE A 153 ? 1.0440 0.5742 0.6112 0.1096 -0.0239 -0.1183 184 PHE B CZ 1164 N N . GLY A 154 ? 1.0516 0.5221 0.5695 0.0962 -0.0442 -0.1101 185 GLY B N 1165 C CA . GLY A 154 ? 1.0558 0.5284 0.5715 0.0950 -0.0432 -0.1072 185 GLY B CA 1166 C C . GLY A 154 ? 1.0537 0.5269 0.5676 0.0859 -0.0309 -0.1027 185 GLY B C 1167 O O . GLY A 154 ? 1.0473 0.5216 0.5643 0.0812 -0.0228 -0.1026 185 GLY B O 1168 N N . GLY A 155 ? 1.1835 0.6570 0.6942 0.0838 -0.0299 -0.0998 186 GLY B N 1169 C CA . GLY A 155 ? 1.1824 0.6561 0.6920 0.0755 -0.0191 -0.0963 186 GLY B CA 1170 C C . GLY A 155 ? 1.1679 0.6602 0.6920 0.0782 -0.0100 -0.0962 186 GLY B C 1171 O O . GLY A 155 ? 1.1632 0.6544 0.6894 0.0713 -0.0012 -0.0952 186 GLY B O 1172 N N . SER A 156 ? 0.9911 0.5004 0.5255 0.0877 -0.0127 -0.0978 187 SER B N 1173 C CA . SER A 156 ? 0.9819 0.5083 0.5288 0.0898 -0.0066 -0.0965 187 SER B CA 1174 C C . SER A 156 ? 0.9847 0.5277 0.5355 0.0957 -0.0093 -0.0956 187 SER B C 1175 O O . SER A 156 ? 0.9917 0.5323 0.5370 0.0973 -0.0142 -0.0963 187 SER B O 1176 C CB . SER A 156 ? 0.9744 0.5062 0.5286 0.0932 -0.0068 -0.0992 187 SER B CB 1177 O OG . SER A 156 ? 0.9745 0.4929 0.5265 0.0867 -0.0030 -0.1005 187 SER B OG 1178 N N . TYR A 157 ? 1.1360 0.6956 0.6961 0.0977 -0.0064 -0.0939 188 TYR B N 1179 C CA . TYR A 157 ? 1.1412 0.7191 0.7041 0.1023 -0.0092 -0.0942 188 TYR B CA 1180 C C . TYR A 157 ? 1.1379 0.7298 0.7066 0.1072 -0.0116 -0.0975 188 TYR B C 1181 O O . TYR A 157 ? 1.1398 0.7410 0.7139 0.1055 -0.0089 -0.0943 188 TYR B O 1182 C CB . TYR A 157 ? 1.1468 0.7328 0.7129 0.0981 -0.0046 -0.0884 188 TYR B CB 1183 C CG . TYR A 157 ? 1.1462 0.7171 0.7097 0.0915 0.0003 -0.0851 188 TYR B CG 1184 C CD1 . TYR A 157 ? 1.1402 0.7028 0.7086 0.0877 0.0048 -0.0846 188 TYR B CD1 1185 C CD2 . TYR A 157 ? 1.1513 0.7172 0.7084 0.0890 0.0004 -0.0835 188 TYR B CD2 1186 C CE1 . TYR A 157 ? 1.1392 0.6900 0.7064 0.0812 0.0101 -0.0837 188 TYR B CE1 1187 C CE2 . TYR A 157 ? 1.1511 0.7038 0.7052 0.0822 0.0054 -0.0813 188 TYR B CE2 1188 C CZ . TYR A 157 ? 1.1449 0.6907 0.7043 0.0782 0.0105 -0.0820 188 TYR B CZ 1189 O OH . TYR A 157 ? 1.1445 0.6792 0.7023 0.0710 0.0162 -0.0819 188 TYR B OH 1190 N N . PHE A 158 ? 0.9411 0.5358 0.5092 0.1132 -0.0175 -0.1040 189 PHE B N 1191 C CA . PHE A 158 ? 0.9380 0.5447 0.5111 0.1174 -0.0195 -0.1082 189 PHE B CA 1192 C C . PHE A 158 ? 0.9392 0.5688 0.5156 0.1209 -0.0215 -0.1125 189 PHE B C 1193 O O . PHE A 158 ? 0.9415 0.5742 0.5180 0.1250 -0.0257 -0.1181 189 PHE B O 1194 C CB . PHE A 158 ? 0.9398 0.5340 0.5112 0.1214 -0.0248 -0.1138 189 PHE B CB 1195 C CG . PHE A 158 ? 0.9376 0.5198 0.5091 0.1179 -0.0219 -0.1114 189 PHE B CG 1196 C CD1 . PHE A 158 ? 0.9327 0.5254 0.5103 0.1187 -0.0204 -0.1114 189 PHE B CD1 1197 C CD2 . PHE A 158 ? 0.9419 0.5030 0.5073 0.1130 -0.0209 -0.1096 189 PHE B CD2 1198 C CE1 . PHE A 158 ? 0.9307 0.5132 0.5102 0.1157 -0.0180 -0.1100 189 PHE B CE1 1199 C CE2 . PHE A 158 ? 0.9402 0.4924 0.5069 0.1091 -0.0175 -0.1088 189 PHE B CE2 1200 C CZ . PHE A 158 ? 0.9339 0.4969 0.5087 0.1111 -0.0162 -0.1092 189 PHE B CZ 1201 N N . GLU A 159 ? 1.1456 0.7919 0.7248 0.1185 -0.0187 -0.1103 190 GLU B N 1202 C CA . GLU A 159 ? 1.1519 0.8226 0.7330 0.1194 -0.0193 -0.1148 190 GLU B CA 1203 C C . GLU A 159 ? 1.1463 0.8280 0.7312 0.1256 -0.0233 -0.1253 190 GLU B C 1204 O O . GLU A 159 ? 1.1380 0.8104 0.7237 0.1280 -0.0251 -0.1268 190 GLU B O 1205 C CB . GLU A 159 ? 1.1640 0.8471 0.7442 0.1121 -0.0158 -0.1075 190 GLU B CB 1206 C CG . GLU A 159 ? 1.1691 0.8386 0.7476 0.1065 -0.0127 -0.0974 190 GLU B CG 1207 C CD . GLU A 159 ? 1.1839 0.8608 0.7625 0.0996 -0.0118 -0.0895 190 GLU B CD 1208 O OE1 . GLU A 159 ? 1.1923 0.8887 0.7690 0.0970 -0.0129 -0.0909 190 GLU B OE1 1209 O OE2 . GLU A 159 ? 1.1885 0.8516 0.7693 0.0962 -0.0106 -0.0825 190 GLU B OE2 1210 N N . GLY A 160 ? 1.2160 0.9187 0.8042 0.1280 -0.0246 -0.1337 191 GLY B N 1211 C CA . GLY A 160 ? 1.2106 0.9298 0.8039 0.1327 -0.0272 -0.1451 191 GLY B CA 1212 C C . GLY A 160 ? 1.2024 0.9133 0.8013 0.1422 -0.0344 -0.1557 191 GLY B C 1213 O O . GLY A 160 ? 1.2030 0.8951 0.8005 0.1442 -0.0378 -0.1534 191 GLY B O 1214 N N . GLU A 161 ? 1.0375 0.7617 0.6427 0.1474 -0.0376 -0.1675 192 GLU B N 1215 C CA . GLU A 161 ? 1.0313 0.7485 0.6441 0.1572 -0.0464 -0.1790 192 GLU B CA 1216 C C . GLU A 161 ? 1.0263 0.7161 0.6355 0.1599 -0.0515 -0.1758 192 GLU B C 1217 O O . GLU A 161 ? 1.0257 0.7042 0.6281 0.1546 -0.0473 -0.1660 192 GLU B O 1218 C CB . GLU A 161 ? 1.0268 0.7712 0.6500 0.1622 -0.0482 -0.1954 192 GLU B CB 1219 C CG . GLU A 161 ? 1.0327 0.8064 0.6612 0.1598 -0.0441 -0.2023 192 GLU B CG 1220 C CD . GLU A 161 ? 1.0292 0.8333 0.6674 0.1625 -0.0437 -0.2194 192 GLU B CD 1221 O OE1 . GLU A 161 ? 1.0281 0.8437 0.6610 0.1568 -0.0387 -0.2181 192 GLU B OE1 1222 O OE2 . GLU A 161 ? 1.0278 0.8441 0.6795 0.1700 -0.0488 -0.2348 192 GLU B OE2 1223 N N . ILE A 162 ? 1.0364 0.7158 0.6512 0.1679 -0.0614 -0.1849 193 ILE B N 1224 C CA . ILE A 162 ? 1.0342 0.6870 0.6451 0.1701 -0.0681 -0.1830 193 ILE B CA 1225 C C . ILE A 162 ? 1.0277 0.6917 0.6446 0.1745 -0.0700 -0.1925 193 ILE B C 1226 O O . ILE A 162 ? 1.0251 0.7039 0.6531 0.1821 -0.0757 -0.2069 193 ILE B O 1227 C CB . ILE A 162 ? 1.0389 0.6728 0.6522 0.1760 -0.0806 -0.1880 193 ILE B CB 1228 C CG1 . ILE A 162 ? 1.0470 0.6704 0.6541 0.1714 -0.0794 -0.1793 193 ILE B CG1 1229 C CG2 . ILE A 162 ? 1.0399 0.6463 0.6476 0.1767 -0.0884 -0.1860 193 ILE B CG2 1230 C CD1 . ILE A 162 ? 1.0560 0.6526 0.6601 0.1739 -0.0922 -0.1795 193 ILE B CD1 1231 N N . PRO A 163 ? 0.9694 0.6271 0.5802 0.1701 -0.0654 -0.1856 194 PRO B N 1232 C CA . PRO A 163 ? 0.9646 0.6346 0.5804 0.1735 -0.0666 -0.1942 194 PRO B CA 1233 C C . PRO A 163 ? 0.9639 0.6253 0.5872 0.1829 -0.0786 -0.2066 194 PRO B C 1234 O O . PRO A 163 ? 0.9679 0.6017 0.5866 0.1838 -0.0860 -0.2027 194 PRO B O 1235 C CB . PRO A 163 ? 0.9630 0.6173 0.5706 0.1677 -0.0628 -0.1833 194 PRO B CB 1236 C CG . PRO A 163 ? 0.9739 0.6031 0.5740 0.1636 -0.0629 -0.1730 194 PRO B CG 1237 C CD . PRO A 163 ? 0.9726 0.6093 0.5732 0.1626 -0.0609 -0.1715 194 PRO B CD 1238 N N . ALA A 164 ? 0.9353 0.6201 0.5701 0.1892 -0.0810 -0.2220 195 ALA B N 1239 C CA . ALA A 164 ? 0.9423 0.6195 0.5870 0.1992 -0.0938 -0.2355 195 ALA B CA 1240 C C . ALA A 164 ? 0.9489 0.6050 0.5880 0.1993 -0.0982 -0.2322 195 ALA B C 1241 O O . ALA A 164 ? 0.9612 0.5967 0.6028 0.2049 -0.1105 -0.2367 195 ALA B O 1242 C CB . ALA A 164 ? 0.9404 0.6496 0.5997 0.2052 -0.0939 -0.2540 195 ALA B CB 1243 N N . ALA A 165 ? 1.0068 0.6669 0.6381 0.1923 -0.0889 -0.2236 196 ALA B N 1244 C CA . ALA A 165 ? 1.0063 0.6484 0.6322 0.1910 -0.0915 -0.2197 196 ALA B CA 1245 C C . ALA A 165 ? 1.0131 0.6203 0.6316 0.1901 -0.0997 -0.2124 196 ALA B C 1246 O O . ALA A 165 ? 1.0158 0.6057 0.6332 0.1924 -0.1080 -0.2150 196 ALA B O 1247 C CB . ALA A 165 ? 1.0063 0.6544 0.6245 0.1822 -0.0802 -0.2083 196 ALA B CB 1248 N N . TYR A 166 ? 1.1248 0.7213 0.7373 0.1858 -0.0979 -0.2035 197 TYR B N 1249 C CA . TYR A 166 ? 1.1340 0.6978 0.7365 0.1819 -0.1046 -0.1954 197 TYR B CA 1250 C C . TYR A 166 ? 1.1398 0.6854 0.7457 0.1890 -0.1215 -0.2042 197 TYR B C 1251 O O . TYR A 166 ? 1.1481 0.6656 0.7442 0.1848 -0.1284 -0.1985 197 TYR B O 1252 C CB . TYR A 166 ? 1.1403 0.6982 0.7366 0.1766 -0.1007 -0.1866 197 TYR B CB 1253 C CG . TYR A 166 ? 1.1388 0.6995 0.7276 0.1668 -0.0867 -0.1742 197 TYR B CG 1254 C CD1 . TYR A 166 ? 1.1340 0.7017 0.7224 0.1633 -0.0790 -0.1709 197 TYR B CD1 1255 C CD2 . TYR A 166 ? 1.1430 0.6987 0.7261 0.1614 -0.0823 -0.1663 197 TYR B CD2 1256 C CE1 . TYR A 166 ? 1.1333 0.7029 0.7177 0.1554 -0.0681 -0.1607 197 TYR B CE1 1257 C CE2 . TYR A 166 ? 1.1414 0.6994 0.7199 0.1534 -0.0707 -0.1564 197 TYR B CE2 1258 C CZ . TYR A 166 ? 1.1364 0.7013 0.7164 0.1506 -0.0641 -0.1540 197 TYR B CZ 1259 O OH . TYR A 166 ? 1.1355 0.7022 0.7136 0.1434 -0.0541 -0.1452 197 TYR B OH 1260 N N . GLY A 167 ? 0.9906 0.5523 0.6110 0.1993 -0.1287 -0.2189 198 GLY B N 1261 C CA . GLY A 167 ? 1.0062 0.5504 0.6327 0.2071 -0.1466 -0.2283 198 GLY B CA 1262 C C . GLY A 167 ? 1.0156 0.5446 0.6388 0.2073 -0.1527 -0.2295 198 GLY B C 1263 O O . GLY A 167 ? 1.0324 0.5433 0.6595 0.2130 -0.1690 -0.2363 198 GLY B O 1264 N N . GLY A 168 ? 1.0439 0.5798 0.6606 0.2010 -0.1406 -0.2228 199 GLY B N 1265 C CA . GLY A 168 ? 1.0440 0.5682 0.6579 0.2007 -0.1449 -0.2239 199 GLY B CA 1266 C C . GLY A 168 ? 1.0555 0.5505 0.6525 0.1899 -0.1446 -0.2100 199 GLY B C 1267 O O . GLY A 168 ? 1.0542 0.5440 0.6479 0.1872 -0.1437 -0.2088 199 GLY B O 1268 N N . LEU A 169 ? 1.1474 0.6238 0.7336 0.1828 -0.1455 -0.2001 200 LEU B N 1269 C CA . LEU A 169 ? 1.1605 0.6094 0.7304 0.1712 -0.1460 -0.1888 200 LEU B CA 1270 C C . LEU A 169 ? 1.1765 0.5949 0.7404 0.1717 -0.1654 -0.1904 200 LEU B C 1271 O O . LEU A 169 ? 1.1874 0.5901 0.7448 0.1687 -0.1725 -0.1863 200 LEU B O 1272 C CB . LEU A 169 ? 1.1648 0.6107 0.7244 0.1607 -0.1346 -0.1770 200 LEU B CB 1273 C CG . LEU A 169 ? 1.1501 0.6259 0.7176 0.1619 -0.1187 -0.1760 200 LEU B CG 1274 C CD1 . LEU A 169 ? 1.1560 0.6297 0.7178 0.1564 -0.1132 -0.1686 200 LEU B CD1 1275 C CD2 . LEU A 169 ? 1.1393 0.6227 0.7057 0.1561 -0.1068 -0.1712 200 LEU B CD2 1276 N N . GLN A 170 ? 1.5248 0.9325 1.0891 0.1737 -0.1745 -0.1949 201 GLN B N 1277 C CA . GLN A 170 ? 1.5399 0.9226 1.1038 0.1778 -0.1960 -0.1999 201 GLN B CA 1278 C C . GLN A 170 ? 1.5598 0.9099 1.1033 0.1644 -0.2023 -0.1873 201 GLN B C 1279 O O . GLN A 170 ? 1.5750 0.9039 1.1156 0.1656 -0.2193 -0.1878 201 GLN B O 1280 C CB . GLN A 170 ? 1.5455 0.9210 1.1118 0.1809 -0.2040 -0.2059 201 GLN B CB 1281 C CG . GLN A 170 ? 1.5637 0.9153 1.1337 0.1877 -0.2286 -0.2134 201 GLN B CG 1282 C CD . GLN A 170 ? 1.5770 0.9088 1.1418 0.1854 -0.2390 -0.2144 201 GLN B CD 1283 O OE1 . GLN A 170 ? 1.5756 0.9068 1.1302 0.1761 -0.2281 -0.2072 201 GLN B OE1 1284 N NE2 . GLN A 170 ? 1.5909 0.9062 1.1637 0.1941 -0.2610 -0.2239 201 GLN B NE2 1285 N N . ARG A 171 ? 1.4205 0.7671 0.9499 0.1509 -0.1884 -0.1763 202 ARG B N 1286 C CA . ARG A 171 ? 1.4423 0.7580 0.9497 0.1351 -0.1930 -0.1649 202 ARG B CA 1287 C C . ARG A 171 ? 1.4469 0.7624 0.9465 0.1279 -0.1856 -0.1572 202 ARG B C 1288 O O . ARG A 171 ? 1.4653 0.7575 0.9453 0.1129 -0.1872 -0.1477 202 ARG B O 1289 C CB . ARG A 171 ? 1.4473 0.7568 0.9438 0.1229 -0.1840 -0.1590 202 ARG B CB 1290 C CG . ARG A 171 ? 1.4519 0.7514 0.9514 0.1276 -0.1966 -0.1651 202 ARG B CG 1291 C CD . ARG A 171 ? 1.4468 0.7533 0.9440 0.1209 -0.1844 -0.1631 202 ARG B CD 1292 N NE . ARG A 171 ? 1.4550 0.7532 0.9560 0.1264 -0.1966 -0.1696 202 ARG B NE 1293 C CZ . ARG A 171 ? 1.4390 0.7589 0.9581 0.1405 -0.1959 -0.1801 202 ARG B CZ 1294 N NH1 . ARG A 171 ? 1.4152 0.7663 0.9491 0.1498 -0.1838 -0.1849 202 ARG B NH1 1295 N NH2 . ARG A 171 ? 1.4480 0.7582 0.9695 0.1444 -0.2075 -0.1859 202 ARG B NH2 1296 N N . LEU A 172 ? 1.1129 0.4538 0.6268 0.1378 -0.1782 -0.1617 203 LEU B N 1297 C CA . LEU A 172 ? 1.1073 0.4508 0.6149 0.1314 -0.1695 -0.1547 203 LEU B CA 1298 C C . LEU A 172 ? 1.1299 0.4482 0.6280 0.1287 -0.1863 -0.1518 203 LEU B C 1299 O O . LEU A 172 ? 1.1350 0.4537 0.6451 0.1408 -0.2007 -0.1598 203 LEU B O 1300 C CB . LEU A 172 ? 1.0808 0.4586 0.6060 0.1421 -0.1578 -0.1602 203 LEU B CB 1301 C CG . LEU A 172 ? 1.0754 0.4561 0.5958 0.1370 -0.1505 -0.1538 203 LEU B CG 1302 C CD1 . LEU A 172 ? 1.0618 0.4513 0.5763 0.1267 -0.1314 -0.1462 203 LEU B CD1 1303 C CD2 . LEU A 172 ? 1.0603 0.4663 0.5977 0.1496 -0.1495 -0.1615 203 LEU B CD2 1304 N N . LYS A 173 ? 1.1819 0.4785 0.6588 0.1122 -0.1847 -0.1408 204 LYS B N 1305 C CA . LYS A 173 ? 1.2026 0.4729 0.6661 0.1058 -0.1997 -0.1355 204 LYS B CA 1306 C C . LYS A 173 ? 1.1994 0.4814 0.6657 0.1071 -0.1931 -0.1335 204 LYS B C 1307 O O . LYS A 173 ? 1.2082 0.4787 0.6752 0.1111 -0.2080 -0.1343 204 LYS B O 1308 C CB . LYS A 173 ? 1.2271 0.4666 0.6633 0.0849 -0.2023 -0.1248 204 LYS B CB 1309 C CG . LYS A 173 ? 1.2436 0.4566 0.6714 0.0819 -0.2206 -0.1252 204 LYS B CG 1310 C CD . LYS A 173 ? 1.2651 0.4546 0.6656 0.0587 -0.2174 -0.1150 204 LYS B CD 1311 C CE . LYS A 173 ? 1.2861 0.4421 0.6732 0.0526 -0.2398 -0.1130 204 LYS B CE 1312 N NZ . LYS A 173 ? 1.3050 0.4426 0.6660 0.0289 -0.2343 -0.1043 204 LYS B NZ 1313 N N . PHE A 174 ? 1.1351 0.4385 0.6030 0.1032 -0.1715 -0.1305 205 PHE B N 1314 C CA . PHE A 174 ? 1.1308 0.4397 0.5948 0.0986 -0.1633 -0.1256 205 PHE B CA 1315 C C . PHE A 174 ? 1.1026 0.4467 0.5837 0.1069 -0.1451 -0.1292 205 PHE B C 1316 O O . PHE A 174 ? 1.0897 0.4472 0.5740 0.1046 -0.1312 -0.1289 205 PHE B O 1317 C CB . PHE A 174 ? 1.1444 0.4356 0.5854 0.0782 -0.1551 -0.1155 205 PHE B CB 1318 C CG . PHE A 174 ? 1.1408 0.4382 0.5771 0.0721 -0.1446 -0.1106 205 PHE B CG 1319 C CD1 . PHE A 174 ? 1.1168 0.4416 0.5645 0.0747 -0.1250 -0.1116 205 PHE B CD1 1320 C CD2 . PHE A 174 ? 1.1629 0.4370 0.5825 0.0627 -0.1552 -0.1046 205 PHE B CD2 1321 C CE1 . PHE A 174 ? 1.1139 0.4435 0.5577 0.0691 -0.1160 -0.1074 205 PHE B CE1 1322 C CE2 . PHE A 174 ? 1.1602 0.4396 0.5750 0.0566 -0.1455 -0.1004 205 PHE B CE2 1323 C CZ . PHE A 174 ? 1.1351 0.4426 0.5625 0.0602 -0.1257 -0.1021 205 PHE B CZ 1324 N N . ILE A 175 ? 1.0872 0.4456 0.5786 0.1153 -0.1455 -0.1320 206 ILE B N 1325 C CA . ILE A 175 ? 1.0595 0.4508 0.5661 0.1223 -0.1299 -0.1351 206 ILE B CA 1326 C C . ILE A 175 ? 1.0561 0.4543 0.5611 0.1194 -0.1231 -0.1308 206 ILE B C 1327 O O . ILE A 175 ? 1.0622 0.4585 0.5707 0.1247 -0.1332 -0.1332 206 ILE B O 1328 C CB . ILE A 175 ? 1.0494 0.4617 0.5760 0.1385 -0.1354 -0.1466 206 ILE B CB 1329 C CG1 . ILE A 175 ? 1.0256 0.4713 0.5654 0.1438 -0.1205 -0.1492 206 ILE B CG1 1330 C CG2 . ILE A 175 ? 1.0636 0.4664 0.5954 0.1463 -0.1538 -0.1526 206 ILE B CG2 1331 C CD1 . ILE A 175 ? 1.0129 0.4702 0.5535 0.1401 -0.1065 -0.1466 206 ILE B CD1 1332 N N . HIS A 176 ? 1.0757 0.4825 0.5770 0.1113 -0.1065 -0.1250 207 HIS B N 1333 C CA . HIS A 176 ? 1.0748 0.4889 0.5752 0.1085 -0.0995 -0.1211 207 HIS B CA 1334 C C . HIS A 176 ? 1.0547 0.4989 0.5690 0.1136 -0.0848 -0.1225 207 HIS B C 1335 O O . HIS A 176 ? 1.0468 0.4968 0.5611 0.1081 -0.0726 -0.1195 207 HIS B O 1336 C CB . HIS A 176 ? 1.0885 0.4819 0.5699 0.0921 -0.0944 -0.1126 207 HIS B CB 1337 C CG . HIS A 176 ? 1.0901 0.4865 0.5680 0.0879 -0.0888 -0.1084 207 HIS B CG 1338 N ND1 . HIS A 176 ? 1.0749 0.4933 0.5623 0.0893 -0.0743 -0.1077 207 HIS B ND1 1339 C CD2 . HIS A 176 ? 1.1060 0.4850 0.5715 0.0816 -0.0964 -0.1043 207 HIS B CD2 1340 C CE1 . HIS A 176 ? 1.0807 0.4959 0.5622 0.0846 -0.0727 -0.1037 207 HIS B CE1 1341 N NE2 . HIS A 176 ? 1.0993 0.4911 0.5674 0.0798 -0.0856 -0.1017 207 HIS B NE2 1342 N N . LEU A 177 ? 1.0649 0.5281 0.5916 0.1238 -0.0873 -0.1277 208 LEU B N 1343 C CA . LEU A 177 ? 1.0520 0.5426 0.5894 0.1270 -0.0755 -0.1280 208 LEU B CA 1344 C C . LEU A 177 ? 1.0567 0.5505 0.5919 0.1241 -0.0723 -0.1240 208 LEU B C 1345 O O . LEU A 177 ? 1.0490 0.5651 0.5927 0.1268 -0.0648 -0.1244 208 LEU B O 1346 C CB . LEU A 177 ? 1.0423 0.5566 0.5951 0.1388 -0.0785 -0.1375 208 LEU B CB 1347 C CG . LEU A 177 ? 1.0382 0.5497 0.5938 0.1427 -0.0830 -0.1427 208 LEU B CG 1348 C CD1 . LEU A 177 ? 1.0294 0.5663 0.6001 0.1535 -0.0852 -0.1534 208 LEU B CD1 1349 C CD2 . LEU A 177 ? 1.0326 0.5420 0.5838 0.1353 -0.0723 -0.1367 208 LEU B CD2 1350 N N . ALA A 178 ? 1.0102 0.4815 0.5335 0.1184 -0.0794 -0.1203 209 ALA B N 1351 C CA . ALA A 178 ? 1.0142 0.4857 0.5353 0.1168 -0.0804 -0.1176 209 ALA B CA 1352 C C . ALA A 178 ? 1.0058 0.4847 0.5241 0.1092 -0.0661 -0.1111 209 ALA B C 1353 O O . ALA A 178 ? 1.0039 0.4758 0.5159 0.1010 -0.0573 -0.1068 209 ALA B O 1354 C CB . ALA A 178 ? 1.0355 0.4781 0.5424 0.1110 -0.0930 -0.1146 209 ALA B CB 1355 N N . GLY A 179 ? 1.0014 0.4944 0.5251 0.1120 -0.0642 -0.1110 210 GLY B N 1356 C CA . GLY A 179 ? 0.9937 0.4946 0.5163 0.1057 -0.0518 -0.1052 210 GLY B CA 1357 C C . GLY A 179 ? 0.9783 0.4978 0.5099 0.1066 -0.0409 -0.1047 210 GLY B C 1358 O O . GLY A 179 ? 0.9745 0.4893 0.5033 0.0996 -0.0320 -0.1005 210 GLY B O 1359 N N . ASN A 180 ? 0.9843 0.5252 0.5272 0.1150 -0.0422 -0.1100 211 ASN B N 1360 C CA . ASN A 180 ? 0.9743 0.5342 0.5251 0.1155 -0.0339 -0.1091 211 ASN B CA 1361 C C . ASN A 180 ? 0.9745 0.5579 0.5326 0.1193 -0.0334 -0.1114 211 ASN B C 1362 O O . ASN A 180 ? 0.9808 0.5643 0.5379 0.1202 -0.0371 -0.1123 211 ASN B O 1363 C CB . ASN A 180 ? 0.9679 0.5308 0.5231 0.1196 -0.0356 -0.1135 211 ASN B CB 1364 C CG . ASN A 180 ? 0.9670 0.5121 0.5166 0.1135 -0.0320 -0.1099 211 ASN B CG 1365 O OD1 . ASN A 180 ? 0.9615 0.5122 0.5151 0.1107 -0.0248 -0.1072 211 ASN B OD1 1366 N ND2 . ASN A 180 ? 0.9775 0.5009 0.5178 0.1107 -0.0377 -0.1102 211 ASN B ND2 1367 N N . VAL A 181 ? 1.0260 0.6292 0.5905 0.1200 -0.0284 -0.1116 212 VAL B N 1368 C CA . VAL A 181 ? 1.0302 0.6581 0.6008 0.1224 -0.0282 -0.1152 212 VAL B CA 1369 C C . VAL A 181 ? 1.0268 0.6715 0.6053 0.1301 -0.0333 -0.1262 212 VAL B C 1370 O O . VAL A 181 ? 1.0299 0.6987 0.6139 0.1310 -0.0319 -0.1308 212 VAL B O 1371 C CB . VAL A 181 ? 1.0337 0.6748 0.6049 0.1164 -0.0206 -0.1085 212 VAL B CB 1372 C CG1 . VAL A 181 ? 1.0423 0.6836 0.6105 0.1120 -0.0183 -0.1035 212 VAL B CG1 1373 C CG2 . VAL A 181 ? 1.0293 0.6582 0.5989 0.1123 -0.0164 -0.1022 212 VAL B CG2 1374 N N . LEU A 182 ? 1.0149 0.6479 0.5941 0.1348 -0.0390 -0.1310 213 LEU B N 1375 C CA . LEU A 182 ? 1.0099 0.6588 0.5974 0.1418 -0.0431 -0.1419 213 LEU B CA 1376 C C . LEU A 182 ? 1.0134 0.6821 0.6104 0.1478 -0.0478 -0.1531 213 LEU B C 1377 O O . LEU A 182 ? 1.0198 0.6835 0.6168 0.1482 -0.0511 -0.1528 213 LEU B O 1378 C CB . LEU A 182 ? 1.0055 0.6349 0.5917 0.1458 -0.0499 -0.1450 213 LEU B CB 1379 C CG . LEU A 182 ? 1.0023 0.6161 0.5815 0.1401 -0.0449 -0.1365 213 LEU B CG 1380 C CD1 . LEU A 182 ? 1.0051 0.5920 0.5785 0.1405 -0.0518 -0.1366 213 LEU B CD1 1381 C CD2 . LEU A 182 ? 0.9964 0.6269 0.5803 0.1407 -0.0409 -0.1385 213 LEU B CD2 1382 N N . GLY A 183 ? 0.9417 0.6345 0.5473 0.1516 -0.0476 -0.1634 214 GLY B N 1383 C CA . GLY A 183 ? 0.9424 0.6607 0.5588 0.1556 -0.0495 -0.1754 214 GLY B CA 1384 C C . GLY A 183 ? 0.9407 0.6800 0.5704 0.1635 -0.0540 -0.1928 214 GLY B C 1385 O O . GLY A 183 ? 0.9392 0.6749 0.5699 0.1666 -0.0561 -0.1966 214 GLY B O 1386 N N . GLY A 184 ? 1.3452 1.1072 0.9863 0.1667 -0.0555 -0.2046 215 GLY B N 1387 C CA . GLY A 184 ? 1.3383 1.1265 0.9943 0.1732 -0.0581 -0.2236 215 GLY B CA 1388 C C . GLY A 184 ? 1.3325 1.1099 1.0021 0.1857 -0.0719 -0.2370 215 GLY B C 1389 O O . GLY A 184 ? 1.3363 1.0920 1.0070 0.1897 -0.0811 -0.2345 215 GLY B O 1390 N N . LYS A 185 ? 1.1970 0.9896 0.8772 0.1914 -0.0742 -0.2516 216 LYS B N 1391 C CA . LYS A 185 ? 1.1916 0.9763 0.8874 0.2038 -0.0884 -0.2666 216 LYS B CA 1392 C C . LYS A 185 ? 1.1914 0.9396 0.8762 0.2050 -0.0951 -0.2560 216 LYS B C 1393 O O . LYS A 185 ? 1.1892 0.9324 0.8610 0.1984 -0.0871 -0.2455 216 LYS B O 1394 C CB . LYS A 185 ? 1.1806 0.9984 0.8925 0.2086 -0.0870 -0.2876 216 LYS B CB 1395 C CG . LYS A 185 ? 1.1815 1.0409 0.9013 0.2036 -0.0768 -0.2981 216 LYS B CG 1396 C CD . LYS A 185 ? 1.1875 1.0542 0.9235 0.2097 -0.0839 -0.3083 216 LYS B CD 1397 C CE . LYS A 185 ? 1.1807 1.0502 0.9413 0.2244 -0.0984 -0.3307 216 LYS B CE 1398 N NZ . LYS A 185 ? 1.1683 1.0834 0.9490 0.2262 -0.0932 -0.3554 216 LYS B NZ 1399 N N . LEU A 186 ? 0.9555 0.6776 0.6448 0.2125 -0.1103 -0.2584 217 LEU B N 1400 C CA . LEU A 186 ? 0.9620 0.6492 0.6405 0.2128 -0.1180 -0.2496 217 LEU B CA 1401 C C . LEU A 186 ? 0.9597 0.6548 0.6492 0.2203 -0.1232 -0.2639 217 LEU B C 1402 O O . LEU A 186 ? 0.9614 0.6681 0.6704 0.2305 -0.1333 -0.2822 217 LEU B O 1403 C CB . LEU A 186 ? 0.9757 0.6306 0.6530 0.2163 -0.1340 -0.2464 217 LEU B CB 1404 C CG . LEU A 186 ? 0.9821 0.6278 0.6543 0.2125 -0.1354 -0.2380 217 LEU B CG 1405 C CD1 . LEU A 186 ? 0.9970 0.6198 0.6771 0.2201 -0.1561 -0.2440 217 LEU B CD1 1406 C CD2 . LEU A 186 ? 0.9840 0.6075 0.6328 0.2003 -0.1266 -0.2170 217 LEU B CD2 1407 N N . PRO A 187 ? 0.9732 0.6625 0.6517 0.2157 -0.1168 -0.2566 218 PRO B N 1408 C CA . PRO A 187 ? 0.9695 0.6722 0.6583 0.2218 -0.1191 -0.2708 218 PRO B CA 1409 C C . PRO A 187 ? 0.9792 0.6588 0.6774 0.2319 -0.1380 -0.2800 218 PRO B C 1410 O O . PRO A 187 ? 0.9886 0.6328 0.6742 0.2295 -0.1458 -0.2678 218 PRO B O 1411 C CB . PRO A 187 ? 0.9651 0.6610 0.6376 0.2132 -0.1089 -0.2573 218 PRO B CB 1412 C CG . PRO A 187 ? 0.9717 0.6357 0.6277 0.2065 -0.1093 -0.2386 218 PRO B CG 1413 C CD . PRO A 187 ? 0.9769 0.6413 0.6347 0.2061 -0.1107 -0.2367 218 PRO B CD 1414 N N . PRO A 188 ? 0.9769 0.6765 0.6970 0.2426 -0.1456 -0.3019 219 PRO B N 1415 C CA . PRO A 188 ? 0.9912 0.6710 0.7243 0.2537 -0.1658 -0.3135 219 PRO B CA 1416 C C . PRO A 188 ? 1.0006 0.6507 0.7210 0.2520 -0.1716 -0.3050 219 PRO B C 1417 O O . PRO A 188 ? 1.0179 0.6359 0.7379 0.2561 -0.1891 -0.3036 219 PRO B O 1418 C CB . PRO A 188 ? 0.9883 0.7052 0.7468 0.2631 -0.1661 -0.3395 219 PRO B CB 1419 C CG . PRO A 188 ? 0.9744 0.7248 0.7360 0.2581 -0.1519 -0.3418 219 PRO B CG 1420 C CD . PRO A 188 ? 0.9673 0.7106 0.7028 0.2442 -0.1363 -0.3181 219 PRO B CD 1421 N N . ARG A 189 ? 1.1634 0.8229 0.8726 0.2451 -0.1576 -0.2983 220 ARG B N 1422 C CA . ARG A 189 ? 1.1645 0.8013 0.8633 0.2432 -0.1613 -0.2921 220 ARG B CA 1423 C C . ARG A 189 ? 1.1797 0.7738 0.8612 0.2376 -0.1700 -0.2747 220 ARG B C 1424 O O . ARG A 189 ? 1.1847 0.7531 0.8593 0.2372 -0.1790 -0.2712 220 ARG B O 1425 C CB . ARG A 189 ? 1.1582 0.8119 0.8464 0.2349 -0.1438 -0.2849 220 ARG B CB 1426 C CG . ARG A 189 ? 1.1596 0.7906 0.8364 0.2319 -0.1461 -0.2771 220 ARG B CG 1427 C CD . ARG A 189 ? 1.1503 0.8011 0.8365 0.2364 -0.1447 -0.2910 220 ARG B CD 1428 N NE . ARG A 189 ? 1.1476 0.8125 0.8228 0.2274 -0.1291 -0.2819 220 ARG B NE 1429 C CZ . ARG A 189 ? 1.1440 0.8409 0.8205 0.2231 -0.1160 -0.2841 220 ARG B CZ 1430 N NH1 . ARG A 189 ? 1.1413 0.8616 0.8299 0.2268 -0.1152 -0.2958 220 ARG B NH1 1431 N NH2 . ARG A 189 ? 1.1439 0.8493 0.8097 0.2146 -0.1045 -0.2748 220 ARG B NH2 1432 N N . LEU A 190 ? 1.0090 0.5960 0.6832 0.2326 -0.1678 -0.2645 221 LEU B N 1433 C CA . LEU A 190 ? 1.0221 0.5710 0.6786 0.2253 -0.1750 -0.2484 221 LEU B CA 1434 C C . LEU A 190 ? 1.0460 0.5638 0.7054 0.2310 -0.1980 -0.2530 221 LEU B C 1435 O O . LEU A 190 ? 1.0602 0.5448 0.7022 0.2235 -0.2044 -0.2407 221 LEU B O 1436 C CB . LEU A 190 ? 1.0166 0.5665 0.6668 0.2196 -0.1690 -0.2391 221 LEU B CB 1437 C CG . LEU A 190 ? 0.9983 0.5633 0.6370 0.2096 -0.1479 -0.2271 221 LEU B CG 1438 C CD1 . LEU A 190 ? 0.9922 0.5613 0.6267 0.2047 -0.1418 -0.2195 221 LEU B CD1 1439 C CD2 . LEU A 190 ? 1.0024 0.5434 0.6230 0.2003 -0.1442 -0.2134 221 LEU B CD2 1440 N N . GLY A 191 ? 1.0521 0.5804 0.7336 0.2437 -0.2112 -0.2712 222 GLY B N 1441 C CA . GLY A 191 ? 1.0770 0.5740 0.7627 0.2496 -0.2357 -0.2758 222 GLY B CA 1442 C C . GLY A 191 ? 1.0875 0.5665 0.7669 0.2490 -0.2417 -0.2754 222 GLY B C 1443 O O . GLY A 191 ? 1.1101 0.5614 0.7922 0.2533 -0.2632 -0.2791 222 GLY B O 1444 N N . LEU A 192 ? 1.1373 0.6315 0.8087 0.2433 -0.2238 -0.2706 223 LEU B N 1445 C CA . LEU A 192 ? 1.1403 0.6211 0.8064 0.2424 -0.2277 -0.2705 223 LEU B CA 1446 C C . LEU A 192 ? 1.1515 0.6003 0.7908 0.2281 -0.2253 -0.2502 223 LEU B C 1447 O O . LEU A 192 ? 1.1541 0.5911 0.7873 0.2258 -0.2275 -0.2487 223 LEU B O 1448 C CB . LEU A 192 ? 1.1220 0.6382 0.7984 0.2462 -0.2130 -0.2810 223 LEU B CB 1449 C CG . LEU A 192 ? 1.1107 0.6619 0.8134 0.2587 -0.2140 -0.3030 223 LEU B CG 1450 C CD1 . LEU A 192 ? 1.0966 0.6787 0.8069 0.2609 -0.2020 -0.3138 223 LEU B CD1 1451 C CD2 . LEU A 192 ? 1.1255 0.6626 0.8461 0.2706 -0.2376 -0.3179 223 LEU B CD2 1452 N N . LEU A 193 ? 1.0896 0.5245 0.7133 0.2180 -0.2211 -0.2355 224 LEU B N 1453 C CA . LEU A 193 ? 1.1013 0.5053 0.7003 0.2036 -0.2204 -0.2185 224 LEU B CA 1454 C C . LEU A 193 ? 1.1305 0.4987 0.7247 0.2036 -0.2446 -0.2178 224 LEU B C 1455 O O . LEU A 193 ? 1.1398 0.4959 0.7308 0.2020 -0.2527 -0.2141 224 LEU B O 1456 C CB . LEU A 193 ? 1.0921 0.4966 0.6767 0.1922 -0.2059 -0.2044 224 LEU B CB 1457 C CG . LEU A 193 ? 1.0640 0.5048 0.6558 0.1932 -0.1842 -0.2056 224 LEU B CG 1458 C CD1 . LEU A 193 ? 1.0552 0.5066 0.6476 0.1918 -0.1778 -0.2020 224 LEU B CD1 1459 C CD2 . LEU A 193 ? 1.0564 0.4951 0.6346 0.1822 -0.1696 -0.1947 224 LEU B CD2 1460 N N . THR A 194 ? 1.3786 0.7278 0.9705 0.2043 -0.2569 -0.2203 225 THR B N 1461 C CA . THR A 194 ? 1.4036 0.7198 0.9950 0.2068 -0.2838 -0.2226 225 THR B CA 1462 C C . THR A 194 ? 1.4254 0.7051 0.9881 0.1891 -0.2888 -0.2041 225 THR B C 1463 O O . THR A 194 ? 1.4457 0.7013 1.0035 0.1873 -0.3063 -0.2009 225 THR B O 1464 C CB . THR A 194 ? 1.4109 0.7204 1.0104 0.2136 -0.2953 -0.2323 225 THR B CB 1465 O OG1 . THR A 194 ? 1.3983 0.7163 0.9872 0.2058 -0.2777 -0.2261 225 THR B OG1 1466 C CG2 . THR A 194 ? 1.3965 0.7375 1.0274 0.2322 -0.2980 -0.2538 225 THR B CG2 1467 N N . GLU A 195 ? 1.3706 0.6482 0.9148 0.1755 -0.2724 -0.1925 226 GLU B N 1468 C CA . GLU A 195 ? 1.3924 0.6388 0.9078 0.1561 -0.2735 -0.1758 226 GLU B CA 1469 C C . GLU A 195 ? 1.3928 0.6412 0.8991 0.1484 -0.2648 -0.1671 226 GLU B C 1470 O O . GLU A 195 ? 1.4124 0.6353 0.8945 0.1316 -0.2664 -0.1541 226 GLU B O 1471 C CB . GLU A 195 ? 1.3885 0.6381 0.8914 0.1448 -0.2567 -0.1690 226 GLU B CB 1472 C CG . GLU A 195 ? 1.3979 0.6334 0.9012 0.1466 -0.2687 -0.1734 226 GLU B CG 1473 C CD . GLU A 195 ? 1.4299 0.6216 0.9143 0.1363 -0.2923 -0.1662 226 GLU B CD 1474 O OE1 . GLU A 195 ? 1.4443 0.6163 0.9059 0.1195 -0.2912 -0.1533 226 GLU B OE1 1475 O OE2 . GLU A 195 ? 1.4441 0.6208 0.9361 0.1443 -0.3127 -0.1736 226 GLU B OE2 1476 N N . LEU A 196 ? 1.1819 0.4610 0.7069 0.1600 -0.2556 -0.1747 227 LEU B N 1477 C CA . LEU A 196 ? 1.1718 0.4590 0.6909 0.1541 -0.2441 -0.1675 227 LEU B CA 1478 C C . LEU A 196 ? 1.1974 0.4551 0.7048 0.1483 -0.2622 -0.1613 227 LEU B C 1479 O O . LEU A 196 ? 1.2107 0.4601 0.7310 0.1592 -0.2829 -0.1696 227 LEU B O 1480 C CB . LEU A 196 ? 1.1436 0.4700 0.6858 0.1678 -0.2323 -0.1778 227 LEU B CB 1481 C CG . LEU A 196 ? 1.1313 0.4672 0.6663 0.1606 -0.2179 -0.1693 227 LEU B CG 1482 C CD1 . LEU A 196 ? 1.1166 0.4610 0.6398 0.1492 -0.1960 -0.1602 227 LEU B CD1 1483 C CD2 . LEU A 196 ? 1.1116 0.4794 0.6679 0.1732 -0.2128 -0.1792 227 LEU B CD2 1484 N N . GLN A 197 ? 1.2039 0.4473 0.6880 0.1311 -0.2541 -0.1475 228 GLN B N 1485 C CA . GLN A 197 ? 1.2306 0.4431 0.6969 0.1205 -0.2691 -0.1386 228 GLN B CA 1486 C C . GLN A 197 ? 1.2149 0.4443 0.6837 0.1205 -0.2574 -0.1362 228 GLN B C 1487 O O . GLN A 197 ? 1.2230 0.4474 0.6988 0.1268 -0.2713 -0.1388 228 GLN B O 1488 C CB . GLN A 197 ? 1.2541 0.4360 0.6889 0.0981 -0.2692 -0.1250 228 GLN B CB 1489 C CG . GLN A 197 ? 1.2678 0.4350 0.6984 0.0961 -0.2775 -0.1265 228 GLN B CG 1490 C CD . GLN A 197 ? 1.3059 0.4311 0.7052 0.0749 -0.2916 -0.1144 228 GLN B CD 1491 O OE1 . GLN A 197 ? 1.3233 0.4297 0.7021 0.0603 -0.2948 -0.1046 228 GLN B OE1 1492 N NE2 . GLN A 197 ? 1.3203 0.4306 0.7146 0.0722 -0.3002 -0.1151 228 GLN B NE2 1493 N N . HIS A 198 ? 1.2573 0.5053 0.7203 0.1127 -0.2328 -0.1309 229 HIS B N 1494 C CA . HIS A 198 ? 1.2543 0.5162 0.7162 0.1097 -0.2199 -0.1268 229 HIS B CA 1495 C C . HIS A 198 ? 1.2285 0.5312 0.7127 0.1223 -0.2018 -0.1346 229 HIS B C 1496 O O . HIS A 198 ? 1.2140 0.5345 0.7023 0.1223 -0.1860 -0.1357 229 HIS B O 1497 C CB . HIS A 198 ? 1.2659 0.5156 0.7026 0.0888 -0.2061 -0.1146 229 HIS B CB 1498 C CG . HIS A 198 ? 1.2647 0.5251 0.6982 0.0840 -0.1935 -0.1099 229 HIS B CG 1499 N ND1 . HIS A 198 ? 1.2855 0.5220 0.6989 0.0707 -0.2008 -0.1014 229 HIS B ND1 1500 C CD2 . HIS A 198 ? 1.2459 0.5373 0.6926 0.0897 -0.1746 -0.1123 229 HIS B CD2 1501 C CE1 . HIS A 198 ? 1.2790 0.5322 0.6944 0.0692 -0.1864 -0.0994 229 HIS B CE1 1502 N NE2 . HIS A 198 ? 1.2551 0.5412 0.6907 0.0807 -0.1707 -0.1057 229 HIS B NE2 1503 N N . MET A 199 ? 1.2261 0.5431 0.7240 0.1318 -0.2048 -0.1396 230 MET B N 1504 C CA . MET A 199 ? 1.2045 0.5595 0.7207 0.1412 -0.1881 -0.1458 230 MET B CA 1505 C C . MET A 199 ? 1.2066 0.5695 0.7204 0.1376 -0.1805 -0.1410 230 MET B C 1506 O O . MET A 199 ? 1.2134 0.5729 0.7334 0.1431 -0.1930 -0.1442 230 MET B O 1507 C CB . MET A 199 ? 1.1924 0.5658 0.7336 0.1591 -0.1981 -0.1610 230 MET B CB 1508 C CG . MET A 199 ? 1.1738 0.5863 0.7343 0.1688 -0.1849 -0.1692 230 MET B CG 1509 S SD . MET A 199 ? 1.1586 0.5950 0.7482 0.1879 -0.1950 -0.1897 230 MET B SD 1510 C CE . MET A 199 ? 1.1441 0.6219 0.7495 0.1932 -0.1799 -0.1960 230 MET B CE 1511 N N . GLU A 200 ? 1.2601 0.6342 0.7666 0.1290 -0.1605 -0.1339 231 GLU B N 1512 C CA . GLU A 200 ? 1.2592 0.6445 0.7653 0.1263 -0.1515 -0.1300 231 GLU B CA 1513 C C . GLU A 200 ? 1.2383 0.6584 0.7584 0.1317 -0.1331 -0.1333 231 GLU B C 1514 O O . GLU A 200 ? 1.2307 0.6559 0.7461 0.1253 -0.1189 -0.1288 231 GLU B O 1515 C CB . GLU A 200 ? 1.2735 0.6363 0.7560 0.1087 -0.1460 -0.1179 231 GLU B CB 1516 C CG . GLU A 200 ? 1.2755 0.6432 0.7546 0.1045 -0.1399 -0.1133 231 GLU B CG 1517 C CD . GLU A 200 ? 1.2900 0.6348 0.7451 0.0862 -0.1353 -0.1028 231 GLU B CD 1518 O OE1 . GLU A 200 ? 1.2928 0.6402 0.7434 0.0813 -0.1296 -0.0987 231 GLU B OE1 1519 O OE2 . GLU A 200 ? 1.2988 0.6239 0.7393 0.0761 -0.1373 -0.0993 231 GLU B OE2 1520 N N . ILE A 201 ? 1.0475 0.4912 0.5856 0.1435 -0.1350 -0.1421 232 ILE B N 1521 C CA . ILE A 201 ? 1.0266 0.5044 0.5776 0.1481 -0.1201 -0.1455 232 ILE B CA 1522 C C . ILE A 201 ? 1.0218 0.5143 0.5760 0.1475 -0.1141 -0.1436 232 ILE B C 1523 O O . ILE A 201 ? 1.0078 0.5292 0.5742 0.1523 -0.1057 -0.1484 232 ILE B O 1524 C CB . ILE A 201 ? 1.0158 0.5172 0.5850 0.1601 -0.1218 -0.1581 232 ILE B CB 1525 C CG1 . ILE A 201 ? 1.0210 0.5274 0.6051 0.1714 -0.1371 -0.1702 232 ILE B CG1 1526 C CG2 . ILE A 201 ? 1.0182 0.5079 0.5835 0.1595 -0.1239 -0.1585 232 ILE B CG2 1527 C CD1 . ILE A 201 ? 1.0081 0.5440 0.6116 0.1823 -0.1359 -0.1845 232 ILE B CD1 1528 N N . GLY A 202 ? 1.1724 0.6458 0.7163 0.1416 -0.1202 -0.1377 233 GLY B N 1529 C CA . GLY A 202 ? 1.1747 0.6611 0.7224 0.1418 -0.1166 -0.1368 233 GLY B CA 1530 C C . GLY A 202 ? 1.1681 0.6686 0.7119 0.1346 -0.0987 -0.1294 233 GLY B C 1531 O O . GLY A 202 ? 1.1607 0.6601 0.6982 0.1284 -0.0875 -0.1239 233 GLY B O 1532 N N . TYR A 203 ? 1.1266 0.6401 0.6753 0.1356 -0.0969 -0.1297 234 TYR B N 1533 C CA . TYR A 203 ? 1.1235 0.6461 0.6674 0.1282 -0.0826 -0.1219 234 TYR B CA 1534 C C . TYR A 203 ? 1.1099 0.6608 0.6636 0.1304 -0.0702 -0.1238 234 TYR B C 1535 O O . TYR A 203 ? 1.1072 0.6666 0.6585 0.1246 -0.0593 -0.1176 234 TYR B O 1536 C CB . TYR A 203 ? 1.1286 0.6255 0.6539 0.1155 -0.0780 -0.1113 234 TYR B CB 1537 C CG . TYR A 203 ? 1.1465 0.6159 0.6600 0.1116 -0.0916 -0.1090 234 TYR B CG 1538 C CD1 . TYR A 203 ? 1.1572 0.6251 0.6695 0.1108 -0.0963 -0.1075 234 TYR B CD1 1539 C CD2 . TYR A 203 ? 1.1542 0.5987 0.6573 0.1082 -0.1009 -0.1081 234 TYR B CD2 1540 C CE1 . TYR A 203 ? 1.1751 0.6169 0.6763 0.1069 -0.1107 -0.1050 234 TYR B CE1 1541 C CE2 . TYR A 203 ? 1.1731 0.5909 0.6640 0.1035 -0.1155 -0.1051 234 TYR B CE2 1542 C CZ . TYR A 203 ? 1.1833 0.5997 0.6733 0.1029 -0.1206 -0.1035 234 TYR B CZ 1543 O OH . TYR A 203 ? 1.2030 0.5917 0.6802 0.0976 -0.1364 -0.1000 234 TYR B OH 1544 N N . ASN A 204 ? 1.0433 0.6076 0.6075 0.1382 -0.0730 -0.1324 235 ASN B N 1545 C CA . ASN A 204 ? 1.0325 0.6268 0.6068 0.1409 -0.0642 -0.1364 235 ASN B CA 1546 C C . ASN A 204 ? 1.0339 0.6534 0.6216 0.1476 -0.0676 -0.1465 235 ASN B C 1547 O O . ASN A 204 ? 1.0429 0.6558 0.6330 0.1505 -0.0765 -0.1496 235 ASN B O 1548 C CB . ASN A 204 ? 1.0248 0.6211 0.6024 0.1445 -0.0645 -0.1408 235 ASN B CB 1549 C CG . ASN A 204 ? 1.0253 0.5961 0.5911 0.1384 -0.0630 -0.1330 235 ASN B CG 1550 O OD1 . ASN A 204 ? 1.0334 0.5820 0.5884 0.1324 -0.0650 -0.1266 235 ASN B OD1 1551 N ND2 . ASN A 204 ? 1.0176 0.5921 0.5851 0.1389 -0.0593 -0.1338 235 ASN B ND2 1552 N N . HIS A 205 ? 1.3427 0.9912 0.9389 0.1490 -0.0608 -0.1517 236 HIS B N 1553 C CA . HIS A 205 ? 1.3450 1.0207 0.9545 0.1541 -0.0630 -0.1632 236 HIS B CA 1554 C C . HIS A 205 ? 1.3369 1.0312 0.9598 0.1623 -0.0671 -0.1781 236 HIS B C 1555 O O . HIS A 205 ? 1.3307 1.0446 0.9549 0.1601 -0.0594 -0.1801 236 HIS B O 1556 C CB . HIS A 205 ? 1.3475 1.0466 0.9558 0.1469 -0.0517 -0.1589 236 HIS B CB 1557 C CG . HIS A 205 ? 1.3516 1.0347 0.9465 0.1376 -0.0445 -0.1433 236 HIS B CG 1558 N ND1 . HIS A 205 ? 1.3575 1.0195 0.9451 0.1348 -0.0471 -0.1363 236 HIS B ND1 1559 C CD2 . HIS A 205 ? 1.3509 1.0360 0.9391 0.1304 -0.0354 -0.1342 236 HIS B CD2 1560 C CE1 . HIS A 205 ? 1.3584 1.0113 0.9364 0.1265 -0.0390 -0.1246 236 HIS B CE1 1561 N NE2 . HIS A 205 ? 1.3547 1.0209 0.9337 0.1242 -0.0325 -0.1231 236 HIS B NE2 1562 N N . PHE A 206 ? 1.0219 0.7118 0.6556 0.1715 -0.0797 -0.1895 237 PHE B N 1563 C CA . PHE A 206 ? 1.0122 0.7198 0.6611 0.1803 -0.0847 -0.2060 237 PHE B CA 1564 C C . PHE A 206 ? 1.0128 0.7451 0.6801 0.1867 -0.0895 -0.2215 237 PHE B C 1565 O O . PHE A 206 ? 1.0223 0.7491 0.6900 0.1859 -0.0931 -0.2187 237 PHE B O 1566 C CB . PHE A 206 ? 1.0123 0.6927 0.6615 0.1869 -0.0977 -0.2086 237 PHE B CB 1567 C CG . PHE A 206 ? 1.0118 0.6677 0.6442 0.1806 -0.0937 -0.1951 237 PHE B CG 1568 C CD1 . PHE A 206 ? 1.0024 0.6695 0.6330 0.1785 -0.0853 -0.1948 237 PHE B CD1 1569 C CD2 . PHE A 206 ? 1.0215 0.6437 0.6403 0.1762 -0.0989 -0.1836 237 PHE B CD2 1570 C CE1 . PHE A 206 ? 1.0018 0.6475 0.6193 0.1731 -0.0821 -0.1836 237 PHE B CE1 1571 C CE2 . PHE A 206 ? 1.0207 0.6228 0.6256 0.1698 -0.0946 -0.1730 237 PHE B CE2 1572 C CZ . PHE A 206 ? 1.0103 0.6246 0.6157 0.1689 -0.0863 -0.1734 237 PHE B CZ 1573 N N . ASN A 207 ? 1.1649 0.9256 0.8480 0.1924 -0.0893 -0.2386 238 ASN B N 1574 C CA . ASN A 207 ? 1.1660 0.9519 0.8708 0.1998 -0.0951 -0.2574 238 ASN B CA 1575 C C . ASN A 207 ? 1.1567 0.9506 0.8807 0.2116 -0.1053 -0.2772 238 ASN B C 1576 O O . ASN A 207 ? 1.1483 0.9289 0.8675 0.2135 -0.1074 -0.2759 238 ASN B O 1577 C CB . ASN A 207 ? 1.1591 0.9839 0.8669 0.1925 -0.0814 -0.2617 238 ASN B CB 1578 C CG . ASN A 207 ? 1.1672 1.0005 0.8586 0.1813 -0.0668 -0.2505 238 ASN B CG 1579 O OD1 . ASN A 207 ? 1.1711 1.0183 0.8650 0.1819 -0.0636 -0.2580 238 ASN B OD1 1580 N ND2 . ASN A 207 ? 1.1711 0.9960 0.8461 0.1711 -0.0589 -0.2329 238 ASN B ND2 1581 N N . GLY A 208 ? 1.2774 1.0937 1.0245 0.2196 -0.1120 -0.2966 239 GLY B N 1582 C CA . GLY A 208 ? 1.2685 1.0930 1.0376 0.2319 -0.1233 -0.3179 239 GLY B CA 1583 C C . GLY A 208 ? 1.2741 1.0634 1.0497 0.2418 -0.1445 -0.3184 239 GLY B C 1584 O O . GLY A 208 ? 1.2850 1.0540 1.0540 0.2398 -0.1504 -0.3077 239 GLY B O 1585 N N . ASN A 209 ? 1.2322 1.0134 1.0201 0.2517 -0.1568 -0.3307 240 ASN B N 1586 C CA . ASN A 209 ? 1.2376 0.9839 1.0319 0.2607 -0.1795 -0.3317 240 ASN B CA 1587 C C . ASN A 209 ? 1.2404 0.9457 1.0105 0.2559 -0.1834 -0.3129 240 ASN B C 1588 O O . ASN A 209 ? 1.2361 0.9420 0.9873 0.2467 -0.1682 -0.3004 240 ASN B O 1589 C CB . ASN A 209 ? 1.2286 0.9897 1.0541 0.2754 -0.1937 -0.3586 240 ASN B CB 1590 C CG . ASN A 209 ? 1.2146 1.0180 1.0684 0.2810 -0.1914 -0.3810 240 ASN B CG 1591 O OD1 . ASN A 209 ? 1.2239 1.0266 1.0828 0.2812 -0.1960 -0.3796 240 ASN B OD1 1592 N ND2 . ASN A 209 ? 1.1920 1.0333 1.0643 0.2850 -0.1841 -0.4026 240 ASN B ND2 1593 N N . ILE A 210 ? 1.0088 0.6783 0.7798 0.2614 -0.2045 -0.3112 241 ILE B N 1594 C CA . ILE A 210 ? 1.0207 0.6544 0.7743 0.2587 -0.2115 -0.2997 241 ILE B CA 1595 C C . ILE A 210 ? 1.0246 0.6693 0.7976 0.2696 -0.2190 -0.3188 241 ILE B C 1596 O O . ILE A 210 ? 1.0347 0.6840 0.8331 0.2818 -0.2358 -0.3375 241 ILE B O 1597 C CB . ILE A 210 ? 1.0435 0.6327 0.7881 0.2584 -0.2327 -0.2897 241 ILE B CB 1598 C CG1 . ILE A 210 ? 1.0416 0.6172 0.7651 0.2467 -0.2257 -0.2704 241 ILE B CG1 1599 C CG2 . ILE A 210 ? 1.0576 0.6130 0.7865 0.2556 -0.2408 -0.2810 241 ILE B CG2 1600 C CD1 . ILE A 210 ? 1.0633 0.5908 0.7643 0.2393 -0.2397 -0.2533 241 ILE B CD1 1601 N N . PRO A 211 ? 1.0171 0.6665 0.7795 0.2654 -0.2072 -0.3151 242 PRO B N 1602 C CA . PRO A 211 ? 1.0190 0.6825 0.7985 0.2745 -0.2114 -0.3335 242 PRO B CA 1603 C C . PRO A 211 ? 1.0419 0.6758 0.8334 0.2851 -0.2378 -0.3419 242 PRO B C 1604 O O . PRO A 211 ? 1.0563 0.6496 0.8285 0.2799 -0.2478 -0.3254 242 PRO B O 1605 C CB . PRO A 211 ? 1.0124 0.6680 0.7692 0.2652 -0.1981 -0.3191 242 PRO B CB 1606 C CG . PRO A 211 ? 0.9978 0.6607 0.7356 0.2527 -0.1794 -0.3018 242 PRO B CG 1607 C CD . PRO A 211 ? 1.0049 0.6513 0.7407 0.2517 -0.1878 -0.2949 242 PRO B CD 1608 N N . SER A 212 ? 1.1401 0.7942 0.9629 0.2987 -0.2489 -0.3673 243 SER B N 1609 C CA . SER A 212 ? 1.1583 0.7842 0.9961 0.3100 -0.2767 -0.3771 243 SER B CA 1610 C C . SER A 212 ? 1.1675 0.7607 0.9867 0.3064 -0.2824 -0.3660 243 SER B C 1611 O O . SER A 212 ? 1.1878 0.7394 0.9998 0.3071 -0.3035 -0.3582 243 SER B O 1612 C CB . SER A 212 ? 1.1536 0.8140 1.0311 0.3248 -0.2841 -0.4084 243 SER B CB 1613 O OG . SER A 212 ? 1.1352 0.8361 1.0182 0.3239 -0.2638 -0.4205 243 SER B OG 1614 N N . GLU A 213 ? 1.0912 0.7032 0.9007 0.3010 -0.2630 -0.3638 244 GLU B N 1615 C CA . GLU A 213 ? 1.0962 0.6845 0.8890 0.2969 -0.2643 -0.3545 244 GLU B CA 1616 C C . GLU A 213 ? 1.1106 0.6532 0.8723 0.2850 -0.2694 -0.3280 244 GLU B C 1617 O O . GLU A 213 ? 1.1225 0.6358 0.8717 0.2823 -0.2782 -0.3207 244 GLU B O 1618 C CB . GLU A 213 ? 1.0764 0.6969 0.8634 0.2915 -0.2401 -0.3554 244 GLU B CB 1619 C CG . GLU A 213 ? 1.0590 0.7239 0.8530 0.2887 -0.2200 -0.3615 244 GLU B CG 1620 C CD . GLU A 213 ? 1.0513 0.7594 0.8766 0.2993 -0.2187 -0.3911 244 GLU B CD 1621 O OE1 . GLU A 213 ? 1.0470 0.7808 0.8880 0.3021 -0.2161 -0.4018 244 GLU B OE1 1622 O OE2 . GLU A 213 ? 1.0492 0.7681 0.8833 0.3040 -0.2191 -0.4042 244 GLU B OE2 1623 N N . PHE A 214 ? 1.0985 0.6354 0.8480 0.2773 -0.2643 -0.3144 245 PHE B N 1624 C CA . PHE A 214 ? 1.1140 0.6106 0.8341 0.2646 -0.2679 -0.2906 245 PHE B CA 1625 C C . PHE A 214 ? 1.1395 0.5942 0.8589 0.2677 -0.2967 -0.2897 245 PHE B C 1626 O O . PHE A 214 ? 1.1550 0.5729 0.8485 0.2561 -0.3022 -0.2712 245 PHE B O 1627 C CB . PHE A 214 ? 1.1170 0.6177 0.8267 0.2566 -0.2578 -0.2787 245 PHE B CB 1628 C CG . PHE A 214 ? 1.1099 0.6319 0.8050 0.2464 -0.2308 -0.2677 245 PHE B CG 1629 C CD1 . PHE A 214 ? 1.0931 0.6437 0.7939 0.2480 -0.2158 -0.2749 245 PHE B CD1 1630 C CD2 . PHE A 214 ? 1.1206 0.6330 0.7963 0.2348 -0.2213 -0.2503 245 PHE B CD2 1631 C CE1 . PHE A 214 ? 1.0877 0.6556 0.7753 0.2383 -0.1932 -0.2641 245 PHE B CE1 1632 C CE2 . PHE A 214 ? 1.1138 0.6445 0.7778 0.2259 -0.1981 -0.2407 245 PHE B CE2 1633 C CZ . PHE A 214 ? 1.0977 0.6551 0.7677 0.2277 -0.1849 -0.2472 245 PHE B CZ 1634 N N . ALA A 215 ? 1.1358 0.5955 0.8834 0.2825 -0.3158 -0.3100 246 ALA B N 1635 C CA . ALA A 215 ? 1.1656 0.5876 0.9149 0.2842 -0.3447 -0.3071 246 ALA B CA 1636 C C . ALA A 215 ? 1.1760 0.5797 0.9151 0.2796 -0.3493 -0.3004 246 ALA B C 1637 O O . ALA A 215 ? 1.2010 0.5738 0.9367 0.2765 -0.3713 -0.2926 246 ALA B O 1638 C CB . ALA A 215 ? 1.1701 0.6132 0.9585 0.2982 -0.3619 -0.3259 246 ALA B CB 1639 N N . LEU A 216 ? 1.1580 0.5807 0.8916 0.2785 -0.3293 -0.3032 247 LEU B N 1640 C CA . LEU A 216 ? 1.1659 0.5746 0.8913 0.2746 -0.3321 -0.2982 247 LEU B CA 1641 C C . LEU A 216 ? 1.1791 0.5473 0.8666 0.2585 -0.3307 -0.2759 247 LEU B C 1642 O O . LEU A 216 ? 1.1895 0.5420 0.8693 0.2542 -0.3359 -0.2708 247 LEU B O 1643 C CB . LEU A 216 ? 1.1435 0.5889 0.8797 0.2798 -0.3132 -0.3109 247 LEU B CB 1644 C CG . LEU A 216 ? 1.1434 0.6166 0.9163 0.2931 -0.3233 -0.3317 247 LEU B CG 1645 C CD1 . LEU A 216 ? 1.1251 0.6418 0.9235 0.3024 -0.3135 -0.3503 247 LEU B CD1 1646 C CD2 . LEU A 216 ? 1.1395 0.6215 0.9140 0.2934 -0.3176 -0.3358 247 LEU B CD2 1647 N N . LEU A 217 ? 1.1783 0.5337 0.8442 0.2479 -0.3230 -0.2614 248 LEU B N 1648 C CA . LEU A 217 ? 1.1885 0.5133 0.8207 0.2296 -0.3184 -0.2393 248 LEU B CA 1649 C C . LEU A 217 ? 1.2237 0.5033 0.8441 0.2246 -0.3459 -0.2318 248 LEU B C 1650 O O . LEU A 217 ? 1.2312 0.5015 0.8485 0.2221 -0.3528 -0.2269 248 LEU B O 1651 C CB . LEU A 217 ? 1.1697 0.5081 0.7872 0.2188 -0.2959 -0.2263 248 LEU B CB 1652 C CG . LEU A 217 ? 1.1368 0.5223 0.7708 0.2256 -0.2731 -0.2353 248 LEU B CG 1653 C CD1 . LEU A 217 ? 1.1262 0.5226 0.7572 0.2215 -0.2636 -0.2292 248 LEU B CD1 1654 C CD2 . LEU A 217 ? 1.1203 0.5180 0.7432 0.2184 -0.2523 -0.2289 248 LEU B CD2 1655 N N . SER A 218 ? 1.5005 0.7575 1.1147 0.2201 -0.3596 -0.2271 249 SER B N 1656 C CA . SER A 218 ? 1.5316 0.7556 1.1410 0.2146 -0.3872 -0.2186 249 SER B CA 1657 C C . SER A 218 ? 1.5504 0.7376 1.1213 0.1939 -0.3869 -0.1978 249 SER B C 1658 O O . SER A 218 ? 1.5713 0.7363 1.1341 0.1878 -0.4031 -0.1896 249 SER B O 1659 C CB . SER A 218 ? 1.5455 0.7614 1.1612 0.2160 -0.4005 -0.2204 249 SER B CB 1660 O OG . SER A 218 ? 1.5405 0.7494 1.1333 0.2050 -0.3842 -0.2122 249 SER B OG 1661 N N . ASN A 219 ? 1.3489 0.5311 0.8962 0.1822 -0.3678 -0.1897 250 ASN B N 1662 C CA . ASN A 219 ? 1.3689 0.5177 0.8793 0.1601 -0.3663 -0.1709 250 ASN B CA 1663 C C . ASN A 219 ? 1.3573 0.5193 0.8602 0.1534 -0.3501 -0.1633 250 ASN B C 1664 O O . ASN A 219 ? 1.3705 0.5124 0.8451 0.1343 -0.3455 -0.1479 250 ASN B O 1665 C CB . ASN A 219 ? 1.3627 0.5128 0.8568 0.1487 -0.3492 -0.1641 250 ASN B CB 1666 C CG . ASN A 219 ? 1.3721 0.5148 0.8753 0.1546 -0.3630 -0.1704 250 ASN B CG 1667 O OD1 . ASN A 219 ? 1.3750 0.5273 0.9049 0.1691 -0.3800 -0.1806 250 ASN B OD1 1668 N ND2 . ASN A 219 ? 1.3757 0.5075 0.8599 0.1425 -0.3543 -0.1637 250 ASN B ND2 1669 N N . LEU A 220 ? 1.2668 0.4632 0.7950 0.1685 -0.3414 -0.1747 251 LEU B N 1670 C CA . LEU A 220 ? 1.2495 0.4627 0.7732 0.1636 -0.3243 -0.1686 251 LEU B CA 1671 C C . LEU A 220 ? 1.2767 0.4571 0.7813 0.1519 -0.3402 -0.1571 251 LEU B C 1672 O O . LEU A 220 ? 1.3015 0.4593 0.8127 0.1578 -0.3675 -0.1611 251 LEU B O 1673 C CB . LEU A 220 ? 1.2222 0.4757 0.7770 0.1816 -0.3165 -0.1838 251 LEU B CB 1674 C CG . LEU A 220 ? 1.2022 0.4761 0.7537 0.1770 -0.2976 -0.1780 251 LEU B CG 1675 C CD1 . LEU A 220 ? 1.1773 0.4723 0.7191 0.1688 -0.2688 -0.1713 251 LEU B CD1 1676 C CD2 . LEU A 220 ? 1.1856 0.4905 0.7657 0.1930 -0.2978 -0.1924 251 LEU B CD2 1677 N N . LYS A 221 ? 1.3815 0.5599 0.8634 0.1356 -0.3233 -0.1435 252 LYS B N 1678 C CA . LYS A 221 ? 1.4046 0.5549 0.8647 0.1217 -0.3338 -0.1314 252 LYS B CA 1679 C C . LYS A 221 ? 1.3904 0.5650 0.8558 0.1230 -0.3177 -0.1305 252 LYS B C 1680 O O . LYS A 221 ? 1.3934 0.5650 0.8684 0.1295 -0.3315 -0.1335 252 LYS B O 1681 C CB . LYS A 221 ? 1.4251 0.5474 0.8493 0.0974 -0.3294 -0.1157 252 LYS B CB 1682 C CG . LYS A 221 ? 1.4484 0.5396 0.8612 0.0918 -0.3482 -0.1136 252 LYS B CG 1683 C CD . LYS A 221 ? 1.4875 0.5331 0.8654 0.0691 -0.3660 -0.0985 252 LYS B CD 1684 C CE . LYS A 221 ? 1.4883 0.5325 0.8366 0.0454 -0.3432 -0.0860 252 LYS B CE 1685 N NZ . LYS A 221 ? 1.5175 0.5292 0.8348 0.0243 -0.3543 -0.0724 252 LYS B NZ 1686 N N . TYR A 222 ? 1.2485 0.4463 0.7082 0.1165 -0.2894 -0.1264 253 TYR B N 1687 C CA . TYR A 222 ? 1.2287 0.4473 0.6895 0.1147 -0.2723 -0.1236 253 TYR B CA 1688 C C . TYR A 222 ? 1.1943 0.4558 0.6847 0.1325 -0.2583 -0.1363 253 TYR B C 1689 O O . TYR A 222 ? 1.1752 0.4571 0.6731 0.1363 -0.2437 -0.1405 253 TYR B O 1690 C CB . TYR A 222 ? 1.2245 0.4406 0.6607 0.0954 -0.2508 -0.1114 253 TYR B CB 1691 C CG . TYR A 222 ? 1.2119 0.4403 0.6432 0.0895 -0.2361 -0.1061 253 TYR B CG 1692 C CD1 . TYR A 222 ? 1.1825 0.4477 0.6307 0.0978 -0.2148 -0.1109 253 TYR B CD1 1693 C CD2 . TYR A 222 ? 1.2353 0.4375 0.6435 0.0741 -0.2436 -0.0957 253 TYR B CD2 1694 C CE1 . TYR A 222 ? 1.1759 0.4517 0.6198 0.0921 -0.2016 -0.1060 253 TYR B CE1 1695 C CE2 . TYR A 222 ? 1.2271 0.4409 0.6310 0.0685 -0.2296 -0.0912 253 TYR B CE2 1696 C CZ . TYR A 222 ? 1.1975 0.4482 0.6200 0.0781 -0.2087 -0.0966 253 TYR B CZ 1697 O OH . TYR A 222 ? 1.1904 0.4521 0.6095 0.0730 -0.1957 -0.0925 253 TYR B OH 1698 N N . PHE A 223 ? 1.1880 0.4630 0.6948 0.1426 -0.2636 -0.1426 254 PHE B N 1699 C CA . PHE A 223 ? 1.1576 0.4742 0.6907 0.1572 -0.2505 -0.1547 254 PHE B CA 1700 C C . PHE A 223 ? 1.1461 0.4768 0.6788 0.1544 -0.2401 -0.1508 254 PHE B C 1701 O O . PHE A 223 ? 1.1584 0.4790 0.6944 0.1567 -0.2549 -0.1516 254 PHE B O 1702 C CB . PHE A 223 ? 1.1631 0.4859 0.7228 0.1750 -0.2700 -0.1710 254 PHE B CB 1703 C CG . PHE A 223 ? 1.1348 0.5018 0.7224 0.1896 -0.2578 -0.1861 254 PHE B CG 1704 C CD1 . PHE A 223 ? 1.1121 0.5048 0.7032 0.1905 -0.2377 -0.1885 254 PHE B CD1 1705 C CD2 . PHE A 223 ? 1.1325 0.5157 0.7435 0.2019 -0.2675 -0.1987 254 PHE B CD2 1706 C CE1 . PHE A 223 ? 1.0889 0.5219 0.7031 0.2018 -0.2269 -0.2021 254 PHE B CE1 1707 C CE2 . PHE A 223 ? 1.1080 0.5337 0.7437 0.2134 -0.2556 -0.2135 254 PHE B CE2 1708 C CZ . PHE A 223 ? 1.0870 0.5371 0.7230 0.2127 -0.2354 -0.2148 254 PHE B CZ 1709 N N . ASP A 224 ? 1.1570 0.5103 0.6865 0.1496 -0.2157 -0.1465 255 ASP B N 1710 C CA . ASP A 224 ? 1.1560 0.5244 0.6855 0.1468 -0.2045 -0.1429 255 ASP B CA 1711 C C . ASP A 224 ? 1.1346 0.5441 0.6822 0.1550 -0.1856 -0.1503 255 ASP B C 1712 O O . ASP A 224 ? 1.1241 0.5440 0.6667 0.1503 -0.1687 -0.1464 255 ASP B O 1713 C CB . ASP A 224 ? 1.1669 0.5159 0.6691 0.1283 -0.1941 -0.1276 255 ASP B CB 1714 C CG . ASP A 224 ? 1.1639 0.5272 0.6645 0.1242 -0.1812 -0.1230 255 ASP B CG 1715 O OD1 . ASP A 224 ? 1.1579 0.5445 0.6773 0.1349 -0.1813 -0.1307 255 ASP B OD1 1716 O OD2 . ASP A 224 ? 1.1683 0.5197 0.6490 0.1095 -0.1709 -0.1123 255 ASP B OD2 1717 N N . VAL A 225 ? 1.2927 0.7252 0.8615 0.1667 -0.1895 -0.1613 256 VAL B N 1718 C CA . VAL A 225 ? 1.2766 0.7489 0.8612 0.1726 -0.1730 -0.1682 256 VAL B CA 1719 C C . VAL A 225 ? 1.2790 0.7642 0.8619 0.1682 -0.1633 -0.1632 256 VAL B C 1720 O O . VAL A 225 ? 1.2697 0.7873 0.8667 0.1732 -0.1533 -0.1700 256 VAL B O 1721 C CB . VAL A 225 ? 1.2670 0.7639 0.8781 0.1878 -0.1805 -0.1865 256 VAL B CB 1722 C CG1 . VAL A 225 ? 1.2505 0.7776 0.8691 0.1901 -0.1639 -0.1915 256 VAL B CG1 1723 C CG2 . VAL A 225 ? 1.2733 0.7467 0.8888 0.1942 -0.2021 -0.1928 256 VAL B CG2 1724 N N . SER A 226 ? 1.3197 0.7795 0.8854 0.1585 -0.1675 -0.1521 257 SER B N 1725 C CA . SER A 226 ? 1.3256 0.7927 0.8906 0.1554 -0.1638 -0.1485 257 SER B CA 1726 C C . SER A 226 ? 1.3154 0.8075 0.8794 0.1506 -0.1417 -0.1440 257 SER B C 1727 O O . SER A 226 ? 1.3055 0.8027 0.8638 0.1462 -0.1284 -0.1398 257 SER B O 1728 C CB . SER A 226 ? 1.3439 0.7753 0.8873 0.1441 -0.1731 -0.1368 257 SER B CB 1729 O OG . SER A 226 ? 1.3557 0.7602 0.8969 0.1464 -0.1944 -0.1390 257 SER B OG 1730 N N . ASN A 227 ? 1.3409 0.8478 0.9113 0.1515 -0.1395 -0.1450 258 ASN B N 1731 C CA . ASN A 227 ? 1.3335 0.8656 0.9053 0.1478 -0.1215 -0.1419 258 ASN B CA 1732 C C . ASN A 227 ? 1.3183 0.8792 0.9019 0.1528 -0.1107 -0.1488 258 ASN B C 1733 O O . ASN A 227 ? 1.3129 0.8754 0.8887 0.1470 -0.0983 -0.1422 258 ASN B O 1734 C CB . ASN A 227 ? 1.3364 0.8518 0.8876 0.1342 -0.1106 -0.1273 258 ASN B CB 1735 C CG . ASN A 227 ? 1.3361 0.8702 0.8887 0.1305 -0.0990 -0.1237 258 ASN B CG 1736 O OD1 . ASN A 227 ? 1.3364 0.8933 0.9035 0.1368 -0.1006 -0.1312 258 ASN B OD1 1737 N ND2 . ASN A 227 ? 1.3356 0.8606 0.8741 0.1197 -0.0876 -0.1130 258 ASN B ND2 1738 N N . CYS A 228 ? 1.2126 0.7961 0.8160 0.1634 -0.1167 -0.1630 259 CYS B N 1739 C CA . CYS A 228 ? 1.1999 0.8146 0.8156 0.1679 -0.1077 -0.1719 259 CYS B CA 1740 C C . CYS A 228 ? 1.2007 0.8456 0.8351 0.1742 -0.1093 -0.1845 259 CYS B C 1741 O O . CYS A 228 ? 1.2112 0.8519 0.8475 0.1741 -0.1154 -0.1840 259 CYS B O 1742 C CB . CYS A 228 ? 1.1929 0.8031 0.8151 0.1751 -0.1154 -0.1803 259 CYS B CB 1743 S SG . CYS A 228 ? 1.1886 0.7761 0.7927 0.1678 -0.1088 -0.1685 259 CYS B SG 1744 N N . SER A 229 ? 1.2217 0.8983 0.8692 0.1781 -0.1029 -0.1957 260 SER B N 1745 C CA . SER A 229 ? 1.2218 0.9303 0.8895 0.1842 -0.1047 -0.2113 260 SER B CA 1746 C C . SER A 229 ? 1.2158 0.9350 0.9053 0.1968 -0.1170 -0.2312 260 SER B C 1747 O O . SER A 229 ? 1.2133 0.9638 0.9220 0.2017 -0.1169 -0.2469 260 SER B O 1748 C CB . SER A 229 ? 1.2179 0.9594 0.8851 0.1770 -0.0882 -0.2107 260 SER B CB 1749 O OG . SER A 229 ? 1.2283 0.9625 0.8836 0.1684 -0.0827 -0.1974 260 SER B OG 1750 N N . LEU A 230 ? 1.2430 0.9371 0.9301 0.2015 -0.1275 -0.2312 261 LEU B N 1751 C CA . LEU A 230 ? 1.2361 0.9373 0.9440 0.2139 -0.1403 -0.2501 261 LEU B CA 1752 C C . LEU A 230 ? 1.2407 0.9537 0.9716 0.2231 -0.1532 -0.2658 261 LEU B C 1753 O O . LEU A 230 ? 1.2527 0.9505 0.9799 0.2213 -0.1600 -0.2591 261 LEU B O 1754 C CB . LEU A 230 ? 1.2386 0.9019 0.9379 0.2165 -0.1538 -0.2447 261 LEU B CB 1755 C CG . LEU A 230 ? 1.2328 0.8866 0.9161 0.2107 -0.1443 -0.2352 261 LEU B CG 1756 C CD1 . LEU A 230 ? 1.2364 0.8520 0.9115 0.2124 -0.1594 -0.2304 261 LEU B CD1 1757 C CD2 . LEU A 230 ? 1.2222 0.9091 0.9191 0.2153 -0.1365 -0.2494 261 LEU B CD2 1758 N N . SER A 231 ? 1.0559 0.7972 0.8115 0.2328 -0.1566 -0.2877 262 SER B N 1759 C CA . SER A 231 ? 1.0574 0.8173 0.8391 0.2417 -0.1670 -0.3055 262 SER B CA 1760 C C . SER A 231 ? 1.0501 0.8176 0.8599 0.2563 -0.1828 -0.3291 262 SER B C 1761 O O . SER A 231 ? 1.0471 0.7985 0.8552 0.2605 -0.1893 -0.3305 262 SER B O 1762 C CB . SER A 231 ? 1.0503 0.8541 0.8394 0.2363 -0.1501 -0.3126 262 SER B CB 1763 O OG . SER A 231 ? 1.0358 0.8742 0.8364 0.2378 -0.1403 -0.3283 262 SER B OG 1764 N N . GLY A 232 ? 1.2118 1.0041 1.0490 0.2643 -0.1896 -0.3482 263 GLY B N 1765 C CA . GLY A 232 ? 1.2001 1.0057 1.0694 0.2789 -0.2043 -0.3743 263 GLY B CA 1766 C C . GLY A 232 ? 1.2081 0.9716 1.0826 0.2880 -0.2314 -0.3727 263 GLY B C 1767 O O . GLY A 232 ? 1.2235 0.9541 1.0804 0.2829 -0.2390 -0.3544 263 GLY B O 1768 N N . SER A 233 ? 1.1249 0.8892 1.0232 0.3010 -0.2467 -0.3923 264 SER B N 1769 C CA . SER A 233 ? 1.1324 0.8579 1.0394 0.3105 -0.2757 -0.3936 264 SER B CA 1770 C C . SER A 233 ? 1.1413 0.8186 1.0176 0.3042 -0.2823 -0.3712 264 SER B C 1771 O O . SER A 233 ? 1.1341 0.8128 0.9908 0.2968 -0.2661 -0.3617 264 SER B O 1772 C CB . SER A 233 ? 1.1177 0.8634 1.0654 0.3276 -0.2912 -0.4251 264 SER B CB 1773 O OG . SER A 233 ? 1.1095 0.8997 1.0873 0.3329 -0.2862 -0.4471 264 SER B OG 1774 N N . LEU A 234 ? 1.1041 0.7388 0.9755 0.3062 -0.3064 -0.3626 265 LEU B N 1775 C CA . LEU A 234 ? 1.1147 0.7017 0.9618 0.3015 -0.3188 -0.3457 265 LEU B CA 1776 C C . LEU A 234 ? 1.1104 0.6951 0.9804 0.3148 -0.3355 -0.3648 265 LEU B C 1777 O O . LEU A 234 ? 1.1204 0.7087 1.0222 0.3285 -0.3565 -0.3846 265 LEU B O 1778 C CB . LEU A 234 ? 1.1380 0.6823 0.9732 0.2979 -0.3406 -0.3316 265 LEU B CB 1779 C CG . LEU A 234 ? 1.1557 0.6676 0.9494 0.2801 -0.3325 -0.3020 265 LEU B CG 1780 C CD1 . LEU A 234 ? 1.1462 0.6891 0.9272 0.2707 -0.3011 -0.2944 265 LEU B CD1 1781 C CD2 . LEU A 234 ? 1.1789 0.6638 0.9690 0.2780 -0.3517 -0.2943 265 LEU B CD2 1782 N N . PRO A 235 ? 1.1038 0.6836 0.9596 0.3113 -0.3265 -0.3600 266 PRO B N 1783 C CA . PRO A 235 ? 1.1121 0.6946 0.9894 0.3235 -0.3387 -0.3791 266 PRO B CA 1784 C C . PRO A 235 ? 1.1435 0.6819 1.0255 0.3291 -0.3720 -0.3775 266 PRO B C 1785 O O . PRO A 235 ? 1.1599 0.6534 1.0105 0.3190 -0.3798 -0.3556 266 PRO B O 1786 C CB . PRO A 235 ? 1.1005 0.6841 0.9537 0.3143 -0.3189 -0.3677 266 PRO B CB 1787 C CG . PRO A 235 ? 1.0812 0.6756 0.9084 0.2996 -0.2933 -0.3484 266 PRO B CG 1788 C CD . PRO A 235 ? 1.0911 0.6650 0.9116 0.2958 -0.3036 -0.3374 266 PRO B CD 1789 N N . GLN A 236 ? 1.2930 0.8508 1.2143 0.3410 -0.3888 -0.3960 267 GLN B N 1790 C CA . GLN A 236 ? 1.3200 0.8448 1.2502 0.3436 -0.4207 -0.3908 267 GLN B CA 1791 C C . GLN A 236 ? 1.3334 0.8227 1.2358 0.3350 -0.4248 -0.3731 267 GLN B C 1792 O O . GLN A 236 ? 1.3580 0.8026 1.2394 0.3272 -0.4435 -0.3545 267 GLN B O 1793 C CB . GLN A 236 ? 1.3230 0.8801 1.3015 0.3581 -0.4353 -0.4160 267 GLN B CB 1794 C CG . GLN A 236 ? 1.3546 0.8787 1.3431 0.3610 -0.4697 -0.4115 267 GLN B CG 1795 C CD . GLN A 236 ? 1.3584 0.8992 1.3722 0.3689 -0.4769 -0.4262 267 GLN B CD 1796 O OE1 . GLN A 236 ? 1.3390 0.9070 1.3535 0.3692 -0.4552 -0.4343 267 GLN B OE1 1797 N NE2 . GLN A 236 ? 1.3849 0.9084 1.4189 0.3746 -0.5086 -0.4294 267 GLN B NE2 1798 N N . GLU A 237 ? 1.3223 0.8336 1.2238 0.3353 -0.4061 -0.3792 268 GLU B N 1799 C CA . GLU A 237 ? 1.3316 0.8196 1.2148 0.3295 -0.4083 -0.3681 268 GLU B CA 1800 C C . GLU A 237 ? 1.3457 0.7845 1.1839 0.3139 -0.4096 -0.3401 268 GLU B C 1801 O O . GLU A 237 ? 1.3645 0.7721 1.1881 0.3079 -0.4223 -0.3282 268 GLU B O 1802 C CB . GLU A 237 ? 1.3072 0.8313 1.1938 0.3310 -0.3828 -0.3789 268 GLU B CB 1803 C CG . GLU A 237 ? 1.2816 0.8436 1.1687 0.3310 -0.3561 -0.3877 268 GLU B CG 1804 C CD . GLU A 237 ? 1.2692 0.8803 1.1988 0.3430 -0.3552 -0.4147 268 GLU B CD 1805 O OE1 . GLU A 237 ? 1.2774 0.9017 1.2381 0.3521 -0.3696 -0.4298 268 GLU B OE1 1806 O OE2 . GLU A 237 ? 1.2554 0.8924 1.1871 0.3426 -0.3399 -0.4211 268 GLU B OE2 1807 N N . LEU A 238 ? 1.1913 0.6236 1.0077 0.3067 -0.3969 -0.3303 269 LEU B N 1808 C CA . LEU A 238 ? 1.2036 0.5928 0.9767 0.2904 -0.3950 -0.3049 269 LEU B CA 1809 C C . LEU A 238 ? 1.2375 0.5829 1.0008 0.2841 -0.4241 -0.2908 269 LEU B C 1810 O O . LEU A 238 ? 1.2530 0.5616 0.9819 0.2693 -0.4258 -0.2707 269 LEU B O 1811 C CB . LEU A 238 ? 1.1881 0.5873 0.9467 0.2831 -0.3768 -0.2964 269 LEU B CB 1812 C CG . LEU A 238 ? 1.1553 0.5941 0.9101 0.2794 -0.3436 -0.2966 269 LEU B CG 1813 C CD1 . LEU A 238 ? 1.1365 0.5989 0.8885 0.2742 -0.3260 -0.2915 269 LEU B CD1 1814 C CD2 . LEU A 238 ? 1.1569 0.5736 0.8795 0.2656 -0.3330 -0.2777 269 LEU B CD2 1815 N N . GLY A 239 ? 1.4241 0.7750 1.2183 0.2946 -0.4474 -0.3022 270 GLY B N 1816 C CA . GLY A 239 ? 1.4584 0.7699 1.2458 0.2891 -0.4779 -0.2900 270 GLY B CA 1817 C C . GLY A 239 ? 1.4761 0.7642 1.2511 0.2831 -0.4882 -0.2813 270 GLY B C 1818 O O . GLY A 239 ? 1.5073 0.7605 1.2720 0.2762 -0.5138 -0.2694 270 GLY B O 1819 N N . ASN A 240 ? 1.4600 0.7674 1.2355 0.2852 -0.4692 -0.2872 271 ASN B N 1820 C CA . ASN A 240 ? 1.4755 0.7628 1.2405 0.2800 -0.4781 -0.2802 271 ASN B CA 1821 C C . ASN A 240 ? 1.4808 0.7373 1.2010 0.2614 -0.4655 -0.2583 271 ASN B C 1822 O O . ASN A 240 ? 1.4937 0.7337 1.2041 0.2563 -0.4721 -0.2523 271 ASN B O 1823 C CB . ASN A 240 ? 1.4590 0.7828 1.2558 0.2940 -0.4720 -0.3010 271 ASN B CB 1824 C CG . ASN A 240 ? 1.4721 0.8089 1.3097 0.3085 -0.4977 -0.3185 271 ASN B CG 1825 O OD1 . ASN A 240 ? 1.4898 0.8155 1.3352 0.3105 -0.5153 -0.3199 271 ASN B OD1 1826 N ND2 . ASN A 240 ? 1.4643 0.8252 1.3286 0.3185 -0.5003 -0.3324 271 ASN B ND2 1827 N N . LEU A 241 ? 1.2958 0.5441 0.9890 0.2507 -0.4484 -0.2466 272 LEU B N 1828 C CA . LEU A 241 ? 1.3019 0.5228 0.9548 0.2326 -0.4367 -0.2275 272 LEU B CA 1829 C C . LEU A 241 ? 1.3377 0.5142 0.9655 0.2173 -0.4592 -0.2086 272 LEU B C 1830 O O . LEU A 241 ? 1.3442 0.5069 0.9564 0.2092 -0.4598 -0.1993 272 LEU B O 1831 C CB . LEU A 241 ? 1.2780 0.5100 0.9119 0.2265 -0.4074 -0.2234 272 LEU B CB 1832 C CG . LEU A 241 ? 1.2437 0.5218 0.9019 0.2410 -0.3864 -0.2418 272 LEU B CG 1833 C CD1 . LEU A 241 ? 1.2285 0.5231 0.8840 0.2373 -0.3728 -0.2368 272 LEU B CD1 1834 C CD2 . LEU A 241 ? 1.2213 0.5200 0.8720 0.2375 -0.3613 -0.2406 272 LEU B CD2 1835 N N . SER A 242 ? 1.4595 0.6131 1.0801 0.2115 -0.4767 -0.2019 273 SER B N 1836 C CA . SER A 242 ? 1.4973 0.6118 1.0991 0.1986 -0.5032 -0.1864 273 SER B CA 1837 C C . SER A 242 ? 1.5099 0.5938 1.0654 0.1744 -0.4926 -0.1649 273 SER B C 1838 O O . SER A 242 ? 1.5415 0.5923 1.0735 0.1591 -0.5104 -0.1494 273 SER B O 1839 C CB . SER A 242 ? 1.5210 0.6235 1.1341 0.2018 -0.5284 -0.1884 273 SER B CB 1840 O OG . SER A 242 ? 1.5597 0.6203 1.1433 0.1836 -0.5502 -0.1691 273 SER B OG 1841 N N . ASN A 243 ? 1.5443 0.6402 1.0864 0.1700 -0.4638 -0.1642 274 ASN B N 1842 C CA . ASN A 243 ? 1.5559 0.6254 1.0558 0.1465 -0.4524 -0.1457 274 ASN B CA 1843 C C . ASN A 243 ? 1.5442 0.6159 1.0286 0.1393 -0.4347 -0.1406 274 ASN B C 1844 O O . ASN A 243 ? 1.5533 0.6061 1.0035 0.1193 -0.4227 -0.1267 274 ASN B O 1845 C CB . ASN A 243 ? 1.5448 0.6192 1.0350 0.1420 -0.4347 -0.1456 274 ASN B CB 1846 C CG . ASN A 243 ? 1.5667 0.6272 1.0608 0.1419 -0.4550 -0.1447 274 ASN B CG 1847 O OD1 . ASN A 243 ? 1.6006 0.6328 1.0844 0.1331 -0.4805 -0.1349 274 ASN B OD1 1848 N ND2 . ASN A 243 ? 1.5485 0.6289 1.0572 0.1514 -0.4444 -0.1549 274 ASN B ND2 1849 N N . LEU A 244 ? 1.3711 0.4655 0.8806 0.1549 -0.4339 -0.1523 275 LEU B N 1850 C CA . LEU A 244 ? 1.3489 0.4597 0.8512 0.1520 -0.4108 -0.1506 275 LEU B CA 1851 C C . LEU A 244 ? 1.3712 0.4548 0.8485 0.1359 -0.4192 -0.1356 275 LEU B C 1852 O O . LEU A 244 ? 1.3874 0.4597 0.8752 0.1416 -0.4414 -0.1380 275 LEU B O 1853 C CB . LEU A 244 ? 1.3200 0.4721 0.8609 0.1742 -0.4051 -0.1691 275 LEU B CB 1854 C CG . LEU A 244 ? 1.2872 0.4754 0.8324 0.1744 -0.3779 -0.1687 275 LEU B CG 1855 C CD1 . LEU A 244 ? 1.2521 0.4816 0.8139 0.1835 -0.3528 -0.1788 275 LEU B CD1 1856 C CD2 . LEU A 244 ? 1.2865 0.4853 0.8550 0.1869 -0.3904 -0.1785 275 LEU B CD2 1857 N N . GLU A 245 ? 1.3995 0.4773 0.8458 0.1154 -0.3999 -0.1206 276 GLU B N 1858 C CA . GLU A 245 ? 1.4202 0.4735 0.8391 0.0972 -0.4045 -0.1059 276 GLU B CA 1859 C C . GLU A 245 ? 1.3964 0.4793 0.8207 0.0984 -0.3826 -0.1057 276 GLU B C 1860 O O . GLU A 245 ? 1.4117 0.4779 0.8189 0.0869 -0.3880 -0.0962 276 GLU B O 1861 C CB . GLU A 245 ? 1.4414 0.4668 0.8207 0.0711 -0.3991 -0.0900 276 GLU B CB 1862 C CG . GLU A 245 ? 1.4719 0.4622 0.8408 0.0661 -0.4241 -0.0874 276 GLU B CG 1863 C CD . GLU A 245 ? 1.4937 0.4593 0.8231 0.0386 -0.4175 -0.0722 276 GLU B CD 1864 O OE1 . GLU A 245 ? 1.4856 0.4603 0.7960 0.0235 -0.3935 -0.0650 276 GLU B OE1 1865 O OE2 . GLU A 245 ? 1.5160 0.4645 0.8382 0.0320 -0.4340 -0.0667 276 GLU B OE2 1866 N N . THR A 246 ? 1.3238 0.4496 0.7709 0.1116 -0.3588 -0.1159 277 THR B N 1867 C CA . THR A 246 ? 1.2976 0.4516 0.7497 0.1124 -0.3379 -0.1155 277 THR B CA 1868 C C . THR A 246 ? 1.2640 0.4611 0.7522 0.1341 -0.3278 -0.1317 277 THR B C 1869 O O . THR A 246 ? 1.2439 0.4638 0.7457 0.1424 -0.3156 -0.1398 277 THR B O 1870 C CB . THR A 246 ? 1.2820 0.4459 0.7135 0.0969 -0.3090 -0.1059 277 THR B CB 1871 O OG1 . THR A 246 ? 1.3126 0.4403 0.7087 0.0739 -0.3149 -0.0911 277 THR B OG1 1872 C CG2 . THR A 246 ? 1.2523 0.4485 0.6934 0.1004 -0.2874 -0.1073 277 THR B CG2 1873 N N . LEU A 247 ? 1.2581 0.4675 0.7610 0.1418 -0.3320 -0.1364 278 LEU B N 1874 C CA . LEU A 247 ? 1.2264 0.4793 0.7613 0.1595 -0.3201 -0.1515 278 LEU B CA 1875 C C . LEU A 247 ? 1.2091 0.4815 0.7433 0.1563 -0.3046 -0.1478 278 LEU B C 1876 O O . LEU A 247 ? 1.2224 0.4837 0.7578 0.1564 -0.3189 -0.1465 278 LEU B O 1877 C CB . LEU A 247 ? 1.2380 0.4900 0.8011 0.1769 -0.3459 -0.1668 278 LEU B CB 1878 C CG . LEU A 247 ? 1.2106 0.5071 0.8098 0.1956 -0.3382 -0.1858 278 LEU B CG 1879 C CD1 . LEU A 247 ? 1.1859 0.5116 0.7940 0.2008 -0.3181 -0.1932 278 LEU B CD1 1880 C CD2 . LEU A 247 ? 1.2285 0.5177 0.8544 0.2109 -0.3674 -0.2008 278 LEU B CD2 1881 N N . PHE A 248 ? 1.1885 0.4899 0.7221 0.1540 -0.2769 -0.1463 279 PHE B N 1882 C CA . PHE A 248 ? 1.1778 0.4993 0.7128 0.1518 -0.2625 -0.1437 279 PHE B CA 1883 C C . PHE A 248 ? 1.1509 0.5174 0.7139 0.1661 -0.2486 -0.1574 279 PHE B C 1884 O O . PHE A 248 ? 1.1327 0.5199 0.6960 0.1653 -0.2288 -0.1575 279 PHE B O 1885 C CB . PHE A 248 ? 1.1753 0.4918 0.6840 0.1345 -0.2416 -0.1290 279 PHE B CB 1886 C CG . PHE A 248 ? 1.2018 0.4770 0.6797 0.1169 -0.2513 -0.1155 279 PHE B CG 1887 C CD1 . PHE A 248 ? 1.2284 0.4728 0.6987 0.1141 -0.2766 -0.1124 279 PHE B CD1 1888 C CD2 . PHE A 248 ? 1.2011 0.4687 0.6574 0.1023 -0.2355 -0.1062 279 PHE B CD2 1889 C CE1 . PHE A 248 ? 1.2546 0.4610 0.6939 0.0957 -0.2857 -0.0994 279 PHE B CE1 1890 C CE2 . PHE A 248 ? 1.2263 0.4584 0.6535 0.0843 -0.2433 -0.0947 279 PHE B CE2 1891 C CZ . PHE A 248 ? 1.2537 0.4547 0.6709 0.0802 -0.2683 -0.0908 279 PHE B CZ 1892 N N . LEU A 249 ? 1.1405 0.5223 0.7267 0.1781 -0.2590 -0.1691 280 LEU B N 1893 C CA . LEU A 249 ? 1.1173 0.5438 0.7298 0.1900 -0.2463 -0.1833 280 LEU B CA 1894 C C . LEU A 249 ? 1.1095 0.5553 0.7222 0.1863 -0.2335 -0.1798 280 LEU B C 1895 O O . LEU A 249 ? 1.0942 0.5758 0.7285 0.1950 -0.2258 -0.1917 280 LEU B O 1896 C CB . LEU A 249 ? 1.1177 0.5560 0.7611 0.2070 -0.2647 -0.2029 280 LEU B CB 1897 C CG . LEU A 249 ? 1.1241 0.5474 0.7734 0.2137 -0.2793 -0.2101 280 LEU B CG 1898 C CD1 . LEU A 249 ? 1.1151 0.5685 0.8005 0.2314 -0.2866 -0.2333 280 LEU B CD1 1899 C CD2 . LEU A 249 ? 1.1140 0.5394 0.7479 0.2066 -0.2615 -0.2029 280 LEU B CD2 1900 N N . PHE A 250 ? 1.1524 0.5741 0.7415 0.1731 -0.2328 -0.1644 281 PHE B N 1901 C CA . PHE A 250 ? 1.1550 0.5886 0.7439 0.1696 -0.2258 -0.1608 281 PHE B CA 1902 C C . PHE A 250 ? 1.1389 0.6081 0.7318 0.1680 -0.2004 -0.1607 281 PHE B C 1903 O O . PHE A 250 ? 1.1282 0.6038 0.7122 0.1630 -0.1840 -0.1558 281 PHE B O 1904 C CB . PHE A 250 ? 1.1743 0.5722 0.7356 0.1548 -0.2317 -0.1447 281 PHE B CB 1905 C CG . PHE A 250 ? 1.1758 0.5576 0.7097 0.1397 -0.2170 -0.1307 281 PHE B CG 1906 C CD1 . PHE A 250 ? 1.1682 0.5645 0.6930 0.1313 -0.1948 -0.1235 281 PHE B CD1 1907 C CD2 . PHE A 250 ? 1.1859 0.5375 0.7036 0.1332 -0.2264 -0.1254 281 PHE B CD2 1908 C CE1 . PHE A 250 ? 1.1688 0.5517 0.6716 0.1179 -0.1818 -0.1127 281 PHE B CE1 1909 C CE2 . PHE A 250 ? 1.1875 0.5265 0.6816 0.1187 -0.2125 -0.1142 281 PHE B CE2 1910 C CZ . PHE A 250 ? 1.1783 0.5336 0.6660 0.1115 -0.1900 -0.1086 281 PHE B CZ 1911 N N . GLN A 251 ? 1.1720 0.6623 0.7778 0.1716 -0.1987 -0.1657 282 GLN B N 1912 C CA . GLN A 251 ? 1.1617 0.6865 0.7732 0.1703 -0.1777 -0.1667 282 GLN B CA 1913 C C . GLN A 251 ? 1.1446 0.7028 0.7739 0.1786 -0.1681 -0.1791 282 GLN B C 1914 O O . GLN A 251 ? 1.1348 0.7019 0.7556 0.1733 -0.1517 -0.1737 282 GLN B O 1915 C CB . GLN A 251 ? 1.1614 0.6759 0.7483 0.1561 -0.1607 -0.1503 282 GLN B CB 1916 C CG . GLN A 251 ? 1.1721 0.6639 0.7416 0.1460 -0.1637 -0.1386 282 GLN B CG 1917 C CD . GLN A 251 ? 1.1721 0.6623 0.7232 0.1335 -0.1445 -0.1260 282 GLN B CD 1918 O OE1 . GLN A 251 ? 1.1789 0.6450 0.7108 0.1241 -0.1421 -0.1169 282 GLN B OE1 1919 N NE2 . GLN A 251 ? 1.1644 0.6813 0.7222 0.1330 -0.1308 -0.1263 282 GLN B NE2 1920 N N . ASN A 252 ? 1.2378 0.8149 0.8924 0.1911 -0.1786 -0.1965 283 ASN B N 1921 C CA . ASN A 252 ? 1.2217 0.8341 0.8950 0.1986 -0.1702 -0.2110 283 ASN B CA 1922 C C . ASN A 252 ? 1.2210 0.8640 0.9223 0.2085 -0.1761 -0.2295 283 ASN B C 1923 O O . ASN A 252 ? 1.2335 0.8729 0.9382 0.2083 -0.1833 -0.2287 283 ASN B O 1924 C CB . ASN A 252 ? 1.2138 0.8140 0.8892 0.2042 -0.1779 -0.2162 283 ASN B CB 1925 C CG . ASN A 252 ? 1.2082 0.7959 0.8615 0.1947 -0.1644 -0.2023 283 ASN B CG 1926 O OD1 . ASN A 252 ? 1.1981 0.8088 0.8545 0.1947 -0.1509 -0.2056 283 ASN B OD1 1927 N ND2 . ASN A 252 ? 1.2150 0.7666 0.8460 0.1859 -0.1685 -0.1872 283 ASN B ND2 1928 N N . GLY A 253 ? 1.0930 0.7677 0.8147 0.2165 -0.1725 -0.2467 284 GLY B N 1929 C CA . GLY A 253 ? 1.0893 0.7993 0.8395 0.2249 -0.1753 -0.2669 284 GLY B CA 1930 C C . GLY A 253 ? 1.0849 0.7964 0.8627 0.2397 -0.1954 -0.2875 284 GLY B C 1931 O O . GLY A 253 ? 1.0761 0.8235 0.8807 0.2473 -0.1951 -0.3082 284 GLY B O 1932 N N . PHE A 254 ? 1.0588 0.7315 0.8302 0.2432 -0.2133 -0.2825 285 PHE B N 1933 C CA . PHE A 254 ? 1.0556 0.7243 0.8523 0.2575 -0.2347 -0.3011 285 PHE B CA 1934 C C . PHE A 254 ? 1.0606 0.7430 0.8858 0.2671 -0.2495 -0.3174 285 PHE B C 1935 O O . PHE A 254 ? 1.0699 0.7449 0.8883 0.2620 -0.2510 -0.3084 285 PHE B O 1936 C CB . PHE A 254 ? 1.0724 0.6918 0.8521 0.2565 -0.2523 -0.2887 285 PHE B CB 1937 C CG . PHE A 254 ? 1.0670 0.6755 0.8247 0.2494 -0.2401 -0.2772 285 PHE B CG 1938 C CD1 . PHE A 254 ? 1.0547 0.6854 0.8254 0.2558 -0.2343 -0.2909 285 PHE B CD1 1939 C CD2 . PHE A 254 ? 1.0742 0.6517 0.7992 0.2360 -0.2342 -0.2538 285 PHE B CD2 1940 C CE1 . PHE A 254 ? 1.0499 0.6708 0.8013 0.2493 -0.2236 -0.2804 285 PHE B CE1 1941 C CE2 . PHE A 254 ? 1.0688 0.6380 0.7759 0.2297 -0.2230 -0.2446 285 PHE B CE2 1942 C CZ . PHE A 254 ? 1.0568 0.6472 0.7771 0.2365 -0.2180 -0.2574 285 PHE B CZ 1943 N N . THR A 255 ? 1.0974 0.7998 0.9555 0.2811 -0.2607 -0.3424 286 THR B N 1944 C CA . THR A 255 ? 1.0953 0.8212 0.9872 0.2915 -0.2721 -0.3632 286 THR B CA 1945 C C . THR A 255 ? 1.0906 0.8030 1.0112 0.3074 -0.3003 -0.3819 286 THR B C 1946 O O . THR A 255 ? 1.0900 0.7738 1.0026 0.3099 -0.3110 -0.3779 286 THR B O 1947 C CB . THR A 255 ? 1.0803 0.8636 0.9919 0.2920 -0.2515 -0.3821 286 THR B CB 1948 O OG1 . THR A 255 ? 1.0676 0.8624 0.9635 0.2857 -0.2324 -0.3778 286 THR B OG1 1949 C CG2 . THR A 255 ? 1.0906 0.8910 0.9933 0.2821 -0.2373 -0.3733 286 THR B CG2 1950 N N . GLY A 256 ? 1.3369 1.0697 1.2918 0.3182 -0.3130 -0.4028 287 GLY B N 1951 C CA . GLY A 256 ? 1.3306 1.0546 1.3186 0.3348 -0.3409 -0.4239 287 GLY B CA 1952 C C . GLY A 256 ? 1.3498 1.0142 1.3215 0.3346 -0.3684 -0.4065 287 GLY B C 1953 O O . GLY A 256 ? 1.3658 0.9983 1.2997 0.3207 -0.3635 -0.3788 287 GLY B O 1954 N N . GLU A 257 ? 1.3779 1.0268 1.3777 0.3491 -0.3979 -0.4229 288 GLU B N 1955 C CA . GLU A 257 ? 1.4005 0.9907 1.3850 0.3481 -0.4275 -0.4069 288 GLU B CA 1956 C C . GLU A 257 ? 1.4066 0.9600 1.3536 0.3380 -0.4243 -0.3853 288 GLU B C 1957 O O . GLU A 257 ? 1.3901 0.9637 1.3326 0.3367 -0.4048 -0.3886 288 GLU B O 1958 C CB . GLU A 257 ? 1.4165 0.9983 1.4425 0.3667 -0.4623 -0.4308 288 GLU B CB 1959 C CG . GLU A 257 ? 1.4249 1.0134 1.4781 0.3739 -0.4797 -0.4415 288 GLU B CG 1960 C CD . GLU A 257 ? 1.4495 1.0064 1.5196 0.3785 -0.5184 -0.4377 288 GLU B CD 1961 O OE1 . GLU A 257 ? 1.4572 1.0214 1.5554 0.3855 -0.5365 -0.4480 288 GLU B OE1 1962 O OE2 . GLU A 257 ? 1.4622 0.9869 1.5165 0.3743 -0.5314 -0.4241 288 GLU B OE2 1963 N N . ILE A 258 ? 1.1901 0.6905 1.1092 0.3293 -0.4429 -0.3630 289 ILE B N 1964 C CA . ILE A 258 ? 1.2044 0.6647 1.0905 0.3200 -0.4461 -0.3441 289 ILE B CA 1965 C C . ILE A 258 ? 1.2249 0.6716 1.1360 0.3332 -0.4730 -0.3595 289 ILE B C 1966 O O . ILE A 258 ? 1.2454 0.6816 1.1779 0.3386 -0.5007 -0.3628 289 ILE B O 1967 C CB . ILE A 258 ? 1.2297 0.6375 1.0789 0.3050 -0.4602 -0.3165 289 ILE B CB 1968 C CG1 . ILE A 258 ? 1.2179 0.6374 1.0563 0.2961 -0.4466 -0.3062 289 ILE B CG1 1969 C CG2 . ILE A 258 ? 1.2364 0.6129 1.0453 0.2901 -0.4519 -0.2946 289 ILE B CG2 1970 C CD1 . ILE A 258 ? 1.2350 0.6474 1.0971 0.3043 -0.4727 -0.3151 289 ILE B CD1 1971 N N . PRO A 259 ? 1.4797 0.9377 1.3904 0.3342 -0.4622 -0.3631 290 PRO B N 1972 C CA . PRO A 259 ? 1.4865 0.9481 1.4242 0.3426 -0.4816 -0.3731 290 PRO B CA 1973 C C . PRO A 259 ? 1.5210 0.9327 1.4452 0.3363 -0.5135 -0.3552 290 PRO B C 1974 O O . PRO A 259 ? 1.5340 0.9050 1.4162 0.3212 -0.5130 -0.3307 290 PRO B O 1975 C CB . PRO A 259 ? 1.4712 0.9443 1.3959 0.3397 -0.4600 -0.3728 290 PRO B CB 1976 C CG . PRO A 259 ? 1.4489 0.9486 1.3606 0.3365 -0.4280 -0.3755 290 PRO B CG 1977 C CD . PRO A 259 ? 1.4585 0.9361 1.3473 0.3266 -0.4290 -0.3579 290 PRO B CD 1978 N N . GLU A 260 ? 1.4396 0.8557 1.3989 0.3466 -0.5411 -0.3679 291 GLU B N 1979 C CA . GLU A 260 ? 1.4765 0.8472 1.4249 0.3405 -0.5741 -0.3522 291 GLU B CA 1980 C C . GLU A 260 ? 1.4889 0.8298 1.4070 0.3300 -0.5747 -0.3356 291 GLU B C 1981 O O . GLU A 260 ? 1.5187 0.8149 1.4096 0.3179 -0.5947 -0.3150 291 GLU B O 1982 C CB . GLU A 260 ? 1.4914 0.8776 1.4871 0.3548 -0.6032 -0.3722 291 GLU B CB 1983 C CG . GLU A 260 ? 1.4902 0.8929 1.5119 0.3623 -0.6118 -0.3838 291 GLU B CG 1984 C CD . GLU A 260 ? 1.5268 0.9014 1.5615 0.3633 -0.6524 -0.3805 291 GLU B CD 1985 O OE1 . GLU A 260 ? 1.5359 0.9288 1.6114 0.3757 -0.6723 -0.4002 291 GLU B OE1 1986 O OE2 . GLU A 260 ? 1.5477 0.8819 1.5511 0.3508 -0.6649 -0.3583 291 GLU B OE2 1987 N N . SER A 261 ? 1.3717 0.7384 1.2933 0.3336 -0.5521 -0.3446 292 SER B N 1988 C CA . SER A 261 ? 1.3813 0.7260 1.2810 0.3260 -0.5524 -0.3330 292 SER B CA 1989 C C . SER A 261 ? 1.3932 0.6940 1.2402 0.3061 -0.5466 -0.3040 292 SER B C 1990 O O . SER A 261 ? 1.4128 0.6830 1.2373 0.2964 -0.5562 -0.2896 292 SER B O 1991 C CB . SER A 261 ? 1.3526 0.7356 1.2647 0.3329 -0.5264 -0.3481 292 SER B CB 1992 O OG . SER A 261 ? 1.3259 0.7228 1.2162 0.3271 -0.4939 -0.3440 292 SER B OG 1993 N N . TYR A 262 ? 1.3679 0.6662 1.1954 0.2994 -0.5311 -0.2959 293 TYR B N 1994 C CA . TYR A 262 ? 1.3769 0.6379 1.1548 0.2796 -0.5220 -0.2701 293 TYR B CA 1995 C C . TYR A 262 ? 1.4165 0.6309 1.1739 0.2673 -0.5519 -0.2513 293 TYR B C 1996 O O . TYR A 262 ? 1.4311 0.6120 1.1483 0.2494 -0.5493 -0.2302 293 TYR B O 1997 C CB . TYR A 262 ? 1.3588 0.6284 1.1215 0.2753 -0.4994 -0.2669 293 TYR B CB 1998 C CG . TYR A 262 ? 1.3261 0.6353 1.0964 0.2820 -0.4675 -0.2802 293 TYR B CG 1999 C CD1 . TYR A 262 ? 1.3038 0.6598 1.1146 0.2990 -0.4612 -0.3053 293 TYR B CD1 2000 C CD2 . TYR A 262 ? 1.3188 0.6214 1.0566 0.2703 -0.4440 -0.2678 293 TYR B CD2 2001 C CE1 . TYR A 262 ? 1.2773 0.6703 1.0929 0.3033 -0.4328 -0.3169 293 TYR B CE1 2002 C CE2 . TYR A 262 ? 1.2882 0.6354 1.0344 0.2735 -0.4139 -0.2758 293 TYR B CE2 2003 C CZ . TYR A 262 ? 1.2684 0.6599 1.0522 0.2894 -0.4087 -0.2998 293 TYR B CZ 2004 O OH . TYR A 262 ? 1.2403 0.6751 1.0298 0.2905 -0.3795 -0.3069 293 TYR B OH 2005 N N . SER A 263 ? 1.5427 0.7568 1.3291 0.2766 -0.5812 -0.2601 294 SER B N 2006 C CA . SER A 263 ? 1.5834 0.7546 1.3520 0.2649 -0.6129 -0.2432 294 SER B CA 2007 C C . SER A 263 ? 1.6003 0.7480 1.3476 0.2553 -0.6183 -0.2320 294 SER B C 2008 O O . SER A 263 ? 1.6362 0.7467 1.3628 0.2427 -0.6430 -0.2163 294 SER B O 2009 C CB . SER A 263 ? 1.5999 0.7792 1.4092 0.2789 -0.6446 -0.2581 294 SER B CB 2010 O OG . SER A 263 ? 1.5858 0.7859 1.4144 0.2869 -0.6404 -0.2681 294 SER B OG 2011 N N . ASN A 264 ? 1.4652 0.6360 1.2178 0.2608 -0.5955 -0.2407 295 ASN B N 2012 C CA . ASN A 264 ? 1.4776 0.6316 1.2151 0.2540 -0.5990 -0.2333 295 ASN B CA 2013 C C . ASN A 264 ? 1.4775 0.6076 1.1674 0.2339 -0.5788 -0.2124 295 ASN B C 2014 O O . ASN A 264 ? 1.4905 0.6041 1.1656 0.2265 -0.5828 -0.2050 295 ASN B O 2015 C CB . ASN A 264 ? 1.4558 0.6475 1.2300 0.2719 -0.5913 -0.2559 295 ASN B CB 2016 C CG . ASN A 264 ? 1.4597 0.6751 1.2828 0.2906 -0.6134 -0.2779 295 ASN B CG 2017 O OD1 . ASN A 264 ? 1.4905 0.6861 1.3229 0.2913 -0.6454 -0.2767 295 ASN B OD1 2018 N ND2 . ASN A 264 ? 1.4295 0.6884 1.2842 0.3053 -0.5967 -0.2987 295 ASN B ND2 2019 N N . LEU A 265 ? 1.4226 0.5501 1.0881 0.2242 -0.5578 -0.2031 296 LEU B N 2020 C CA . LEU A 265 ? 1.4256 0.5302 1.0475 0.2043 -0.5405 -0.1844 296 LEU B CA 2021 C C . LEU A 265 ? 1.4638 0.5252 1.0524 0.1842 -0.5611 -0.1628 296 LEU B C 2022 O O . LEU A 265 ? 1.4684 0.5199 1.0427 0.1764 -0.5602 -0.1547 296 LEU B O 2023 C CB . LEU A 265 ? 1.3951 0.5168 1.0046 0.2018 -0.5074 -0.1844 296 LEU B CB 2024 C CG . LEU A 265 ? 1.3589 0.5276 1.0055 0.2230 -0.4907 -0.2077 296 LEU B CG 2025 C CD1 . LEU A 265 ? 1.3459 0.5287 1.0003 0.2275 -0.4839 -0.2125 296 LEU B CD1 2026 C CD2 . LEU A 265 ? 1.3331 0.5190 0.9698 0.2218 -0.4613 -0.2098 296 LEU B CD2 2027 N N . LYS A 266 ? 1.7319 0.7671 1.3052 0.1741 -0.5787 -0.1528 297 LYS B N 2028 C CA . LYS A 266 ? 1.7725 0.7678 1.3153 0.1546 -0.6021 -0.1332 297 LYS B CA 2029 C C . LYS A 266 ? 1.7781 0.7514 1.2726 0.1295 -0.5824 -0.1136 297 LYS B C 2030 O O . LYS A 266 ? 1.8084 0.7511 1.2703 0.1091 -0.5939 -0.0959 297 LYS B O 2031 C CB . LYS A 266 ? 1.8044 0.7817 1.3537 0.1549 -0.6334 -0.1321 297 LYS B CB 2032 C CG . LYS A 266 ? 1.8141 0.8017 1.4045 0.1735 -0.6626 -0.1468 297 LYS B CG 2033 C CD . LYS A 266 ? 1.8448 0.8070 1.4215 0.1629 -0.6863 -0.1350 297 LYS B CD 2034 C CE . LYS A 266 ? 1.8613 0.8290 1.4776 0.1795 -0.7204 -0.1488 297 LYS B CE 2035 N NZ . LYS A 266 ? 1.8245 0.8369 1.4901 0.2056 -0.7089 -0.1747 297 LYS B NZ 2036 N N . SER A 267 ? 1.6125 0.6038 1.1034 0.1307 -0.5521 -0.1179 298 SER B N 2037 C CA . SER A 267 ? 1.6142 0.5897 1.0635 0.1082 -0.5306 -0.1025 298 SER B CA 2038 C C . SER A 267 ? 1.5910 0.5792 1.0337 0.1066 -0.5070 -0.1028 298 SER B C 2039 O O . SER A 267 ? 1.5903 0.5682 1.0003 0.0880 -0.4873 -0.0915 298 SER B O 2040 C CB . SER A 267 ? 1.5965 0.5840 1.0463 0.1102 -0.5122 -0.1075 298 SER B CB 2041 O OG . SER A 267 ? 1.5632 0.5878 1.0529 0.1354 -0.5030 -0.1282 298 SER B OG 2042 N N . LEU A 268 ? 1.6045 0.6156 1.0788 0.1256 -0.5092 -0.1164 299 LEU B N 2043 C CA . LEU A 268 ? 1.5806 0.6069 1.0525 0.1267 -0.4870 -0.1188 299 LEU B CA 2044 C C . LEU A 268 ? 1.6036 0.6016 1.0404 0.1048 -0.4902 -0.1008 299 LEU B C 2045 O O . LEU A 268 ? 1.6337 0.6103 1.0662 0.0991 -0.5168 -0.0931 299 LEU B O 2046 C CB . LEU A 268 ? 1.5609 0.6172 1.0743 0.1507 -0.4916 -0.1375 299 LEU B CB 2047 C CG . LEU A 268 ? 1.5328 0.6151 1.0488 0.1548 -0.4642 -0.1429 299 LEU B CG 2048 C CD1 . LEU A 268 ? 1.5081 0.6141 1.0121 0.1478 -0.4301 -0.1392 299 LEU B CD1 2049 C CD2 . LEU A 268 ? 1.5099 0.6295 1.0704 0.1794 -0.4655 -0.1645 299 LEU B CD2 2050 N N . LYS A 269 ? 1.4728 0.4718 0.8848 0.0922 -0.4632 -0.0947 300 LYS B N 2051 C CA . LYS A 269 ? 1.4921 0.4680 0.8694 0.0696 -0.4614 -0.0783 300 LYS B CA 2052 C C . LYS A 269 ? 1.4638 0.4716 0.8533 0.0753 -0.4426 -0.0812 300 LYS B C 2053 O O . LYS A 269 ? 1.4781 0.4731 0.8666 0.0742 -0.4581 -0.0781 300 LYS B O 2054 C CB . LYS A 269 ? 1.4971 0.4631 0.8383 0.0457 -0.4416 -0.0653 300 LYS B CB 2055 C CG . LYS A 269 ? 1.5248 0.4662 0.8512 0.0355 -0.4570 -0.0587 300 LYS B CG 2056 C CD . LYS A 269 ? 1.5385 0.4624 0.8230 0.0070 -0.4405 -0.0449 300 LYS B CD 2057 C CE . LYS A 269 ? 1.5518 0.4659 0.8270 -0.0004 -0.4444 -0.0416 300 LYS B CE 2058 N NZ . LYS A 269 ? 1.5904 0.4796 0.8596 -0.0063 -0.4777 -0.0330 300 LYS B NZ 2059 N N . LEU A 270 ? 1.4014 0.4494 0.8014 0.0806 -0.4097 -0.0865 301 LEU B N 2060 C CA . LEU A 270 ? 1.3726 0.4526 0.7835 0.0853 -0.3895 -0.0890 301 LEU B CA 2061 C C . LEU A 270 ? 1.3491 0.4690 0.8023 0.1112 -0.3850 -0.1075 301 LEU B C 2062 O O . LEU A 270 ? 1.3346 0.4752 0.8034 0.1213 -0.3747 -0.1167 301 LEU B O 2063 C CB . LEU A 270 ? 1.3636 0.4614 0.7567 0.0721 -0.3557 -0.0820 301 LEU B CB 2064 C CG . LEU A 270 ? 1.3814 0.4512 0.7401 0.0500 -0.3532 -0.0700 301 LEU B CG 2065 C CD1 . LEU A 270 ? 1.3662 0.4626 0.7196 0.0436 -0.3189 -0.0690 301 LEU B CD1 2066 C CD2 . LEU A 270 ? 1.4116 0.4434 0.7364 0.0279 -0.3677 -0.0556 301 LEU B CD2 2067 N N . LEU A 271 ? 1.3977 0.5292 0.8689 0.1208 -0.3919 -0.1132 302 LEU B N 2068 C CA . LEU A 271 ? 1.3776 0.5500 0.8883 0.1433 -0.3861 -0.1315 302 LEU B CA 2069 C C . LEU A 271 ? 1.3727 0.5717 0.8876 0.1429 -0.3680 -0.1306 302 LEU B C 2070 O O . LEU A 271 ? 1.3871 0.5697 0.8941 0.1372 -0.3803 -0.1245 302 LEU B O 2071 C CB . LEU A 271 ? 1.3821 0.5425 0.9183 0.1587 -0.4189 -0.1437 302 LEU B CB 2072 C CG . LEU A 271 ? 1.3620 0.5611 0.9416 0.1827 -0.4178 -0.1665 302 LEU B CG 2073 C CD1 . LEU A 271 ? 1.3762 0.5539 0.9763 0.1949 -0.4531 -0.1772 302 LEU B CD1 2074 C CD2 . LEU A 271 ? 1.3461 0.5826 0.9457 0.1907 -0.4036 -0.1745 302 LEU B CD2 2075 N N . ASP A 272 ? 1.2468 0.4855 0.7729 0.1480 -0.3397 -0.1361 303 ASP B N 2076 C CA . ASP A 272 ? 1.2275 0.4931 0.7597 0.1484 -0.3231 -0.1362 303 ASP B CA 2077 C C . ASP A 272 ? 1.1995 0.5122 0.7666 0.1665 -0.3110 -0.1536 303 ASP B C 2078 O O . ASP A 272 ? 1.1792 0.5164 0.7510 0.1690 -0.2910 -0.1573 303 ASP B O 2079 C CB . ASP A 272 ? 1.2232 0.4876 0.7265 0.1304 -0.2983 -0.1213 303 ASP B CB 2080 C CG . ASP A 272 ? 1.2164 0.4962 0.7190 0.1270 -0.2867 -0.1177 303 ASP B CG 2081 O OD1 . ASP A 272 ? 1.1992 0.5116 0.7284 0.1405 -0.2821 -0.1292 303 ASP B OD1 2082 O OD2 . ASP A 272 ? 1.2288 0.4889 0.7042 0.1100 -0.2821 -0.1041 303 ASP B OD2 2083 N N . PHE A 273 ? 1.2939 0.6188 0.8848 0.1780 -0.3237 -0.1645 304 PHE B N 2084 C CA . PHE A 273 ? 1.2749 0.6452 0.8997 0.1939 -0.3144 -0.1826 304 PHE B CA 2085 C C . PHE A 273 ? 1.2713 0.6708 0.8998 0.1917 -0.2959 -0.1817 304 PHE B C 2086 O O . PHE A 273 ? 1.2592 0.6959 0.9151 0.2033 -0.2900 -0.1969 304 PHE B O 2087 C CB . PHE A 273 ? 1.2740 0.6448 0.9299 0.2104 -0.3407 -0.2002 304 PHE B CB 2088 C CG . PHE A 273 ? 1.2687 0.6284 0.9326 0.2179 -0.3533 -0.2082 304 PHE B CG 2089 C CD1 . PHE A 273 ? 1.2647 0.6174 0.9088 0.2099 -0.3397 -0.1998 304 PHE B CD1 2090 C CD2 . PHE A 273 ? 1.2671 0.6241 0.9599 0.2332 -0.3789 -0.2251 304 PHE B CD2 2091 C CE1 . PHE A 273 ? 1.2602 0.6026 0.9113 0.2165 -0.3512 -0.2070 304 PHE B CE1 2092 C CE2 . PHE A 273 ? 1.2618 0.6081 0.9624 0.2402 -0.3909 -0.2327 304 PHE B CE2 2093 C CZ . PHE A 273 ? 1.2589 0.5975 0.9377 0.2315 -0.3770 -0.2232 304 PHE B CZ 2094 N N . SER A 274 ? 1.2475 0.6295 0.8482 0.1763 -0.2878 -0.1645 305 SER B N 2095 C CA . SER A 274 ? 1.2499 0.6488 0.8510 0.1726 -0.2771 -0.1614 305 SER B CA 2096 C C . SER A 274 ? 1.2338 0.6772 0.8477 0.1760 -0.2515 -0.1675 305 SER B C 2097 O O . SER A 274 ? 1.2206 0.6785 0.8314 0.1748 -0.2342 -0.1671 305 SER B O 2098 C CB . SER A 274 ? 1.2655 0.6342 0.8318 0.1540 -0.2730 -0.1417 305 SER B CB 2099 O OG . SER A 274 ? 1.2636 0.6222 0.8087 0.1440 -0.2591 -0.1326 305 SER B OG 2100 N N . SER A 275 ? 1.2394 0.7026 0.8662 0.1790 -0.2502 -0.1721 306 SER B N 2101 C CA . SER A 275 ? 1.2273 0.7334 0.8676 0.1817 -0.2289 -0.1786 306 SER B CA 2102 C C . SER A 275 ? 1.2111 0.7507 0.8779 0.1945 -0.2251 -0.1968 306 SER B C 2103 O O . SER A 275 ? 1.1990 0.7610 0.8637 0.1922 -0.2053 -0.1967 306 SER B O 2104 C CB . SER A 275 ? 1.2237 0.7309 0.8397 0.1680 -0.2050 -0.1634 306 SER B CB 2105 O OG . SER A 275 ? 1.2307 0.7371 0.8369 0.1597 -0.1995 -0.1546 306 SER B OG 2106 N N . ASN A 276 ? 1.2252 0.7672 0.9168 0.2076 -0.2450 -0.2128 307 ASN B N 2107 C CA . ASN A 276 ? 1.2097 0.7863 0.9307 0.2206 -0.2434 -0.2338 307 ASN B CA 2108 C C . ASN A 276 ? 1.2094 0.8110 0.9625 0.2317 -0.2542 -0.2525 307 ASN B C 2109 O O . ASN A 276 ? 1.2220 0.8142 0.9741 0.2294 -0.2627 -0.2482 307 ASN B O 2110 C CB . ASN A 276 ? 1.2058 0.7622 0.9306 0.2276 -0.2584 -0.2394 307 ASN B CB 2111 C CG . ASN A 276 ? 1.2010 0.7449 0.9015 0.2188 -0.2444 -0.2266 307 ASN B CG 2112 O OD1 . ASN A 276 ? 1.1893 0.7603 0.8957 0.2208 -0.2285 -0.2329 307 ASN B OD1 2113 N ND2 . ASN A 276 ? 1.2101 0.7130 0.8832 0.2086 -0.2509 -0.2091 307 ASN B ND2 2114 N N . GLN A 277 ? 1.2530 0.8880 1.0352 0.2434 -0.2536 -0.2743 308 GLN B N 2115 C CA . GLN A 277 ? 1.2504 0.9140 1.0679 0.2551 -0.2636 -0.2962 308 GLN B CA 2116 C C . GLN A 277 ? 1.2503 0.8968 1.0922 0.2693 -0.2930 -0.3113 308 GLN B C 2117 O O . GLN A 277 ? 1.2435 0.9174 1.1203 0.2811 -0.3016 -0.3339 308 GLN B O 2118 C CB . GLN A 277 ? 1.2332 0.9499 1.0710 0.2584 -0.2443 -0.3143 308 GLN B CB 2119 C CG . GLN A 277 ? 1.2285 0.9621 1.0430 0.2447 -0.2166 -0.3004 308 GLN B CG 2120 C CD . GLN A 277 ? 1.2377 0.9906 1.0519 0.2380 -0.2071 -0.2971 308 GLN B CD 2121 O OE1 . GLN A 277 ? 1.2560 0.9865 1.0645 0.2361 -0.2182 -0.2884 308 GLN B OE1 2122 N NE2 . GLN A 277 ? 1.2255 1.0202 1.0450 0.2334 -0.1869 -0.3041 308 GLN B NE2 2123 N N . LEU A 278 ? 1.2122 0.8156 1.0375 0.2682 -0.3082 -0.3004 309 LEU B N 2124 C CA . LEU A 278 ? 1.2111 0.7967 1.0592 0.2816 -0.3371 -0.3146 309 LEU B CA 2125 C C . LEU A 278 ? 1.2193 0.8045 1.0937 0.2906 -0.3596 -0.3264 309 LEU B C 2126 O O . LEU A 278 ? 1.2364 0.8067 1.0964 0.2826 -0.3621 -0.3128 309 LEU B O 2127 C CB . LEU A 278 ? 1.2224 0.7555 1.0422 0.2752 -0.3514 -0.2965 309 LEU B CB 2128 C CG . LEU A 278 ? 1.2146 0.7447 1.0101 0.2670 -0.3320 -0.2855 309 LEU B CG 2129 C CD1 . LEU A 278 ? 1.2253 0.7062 1.0006 0.2631 -0.3509 -0.2734 309 LEU B CD1 2130 C CD2 . LEU A 278 ? 1.1924 0.7646 1.0123 0.2767 -0.3190 -0.3060 309 LEU B CD2 2131 N N . SER A 279 ? 1.2578 0.8604 1.1719 0.3073 -0.3761 -0.3525 310 SER B N 2132 C CA . SER A 279 ? 1.2617 0.8728 1.2085 0.3180 -0.3964 -0.3687 310 SER B CA 2133 C C . SER A 279 ? 1.2637 0.8433 1.2314 0.3310 -0.4327 -0.3792 310 SER B C 2134 O O . SER A 279 ? 1.2620 0.8154 1.2193 0.3318 -0.4413 -0.3750 310 SER B O 2135 C CB . SER A 279 ? 1.2465 0.9190 1.2304 0.3269 -0.3811 -0.3962 310 SER B CB 2136 O OG . SER A 279 ? 1.2154 0.9184 1.1832 0.3178 -0.3483 -0.3921 310 SER B OG 2137 N N . GLY A 280 ? 1.2464 0.8287 1.2446 0.3411 -0.4548 -0.3934 311 GLY B N 2138 C CA . GLY A 280 ? 1.2562 0.8082 1.2781 0.3543 -0.4927 -0.4046 311 GLY B CA 2139 C C . GLY A 280 ? 1.2839 0.7703 1.2694 0.3440 -0.5153 -0.3774 311 GLY B C 2140 O O . GLY A 280 ? 1.2907 0.7563 1.2321 0.3264 -0.4996 -0.3505 311 GLY B O 2141 N N . SER A 281 ? 1.3135 0.7671 1.3173 0.3542 -0.5526 -0.3847 312 SER B N 2142 C CA . SER A 281 ? 1.3451 0.7385 1.3153 0.3419 -0.5770 -0.3579 312 SER B CA 2143 C C . SER A 281 ? 1.3510 0.7138 1.2812 0.3292 -0.5694 -0.3376 312 SER B C 2144 O O . SER A 281 ? 1.3306 0.7162 1.2597 0.3314 -0.5463 -0.3447 312 SER B O 2145 C CB . SER A 281 ? 1.3667 0.7504 1.3688 0.3496 -0.6157 -0.3641 312 SER B CB 2146 O OG . SER A 281 ? 1.3642 0.7709 1.4007 0.3596 -0.6252 -0.3805 312 SER B OG 2147 N N . ILE A 282 ? 1.3768 0.6887 1.2737 0.3149 -0.5890 -0.3124 313 ILE B N 2148 C CA . ILE A 282 ? 1.3879 0.6675 1.2480 0.3014 -0.5871 -0.2926 313 ILE B CA 2149 C C . ILE A 282 ? 1.4038 0.6794 1.2875 0.3084 -0.6135 -0.2990 313 ILE B C 2150 O O . ILE A 282 ? 1.4238 0.6968 1.3348 0.3155 -0.6431 -0.3062 313 ILE B O 2151 C CB . ILE A 282 ? 1.4142 0.6421 1.2248 0.2797 -0.5952 -0.2622 313 ILE B CB 2152 C CG1 . ILE A 282 ? 1.3992 0.6367 1.1854 0.2695 -0.5667 -0.2527 313 ILE B CG1 2153 C CG2 . ILE A 282 ? 1.4292 0.6246 1.2038 0.2648 -0.5958 -0.2428 313 ILE B CG2 2154 C CD1 . ILE A 282 ? 1.4226 0.6151 1.1596 0.2461 -0.5704 -0.2234 313 ILE B CD1 2155 N N . PRO A 283 ? 1.4346 0.7105 1.3089 0.3067 -0.6036 -0.2973 314 PRO B N 2156 C CA . PRO A 283 ? 1.4540 0.7242 1.3471 0.3121 -0.6275 -0.3026 314 PRO B CA 2157 C C . PRO A 283 ? 1.4964 0.7216 1.3748 0.3018 -0.6637 -0.2853 314 PRO B C 2158 O O . PRO A 283 ? 1.5140 0.7000 1.3469 0.2827 -0.6642 -0.2599 314 PRO B O 2159 C CB . PRO A 283 ? 1.4457 0.7082 1.3105 0.3038 -0.6077 -0.2927 314 PRO B CB 2160 C CG . PRO A 283 ? 1.4094 0.7014 1.2684 0.3054 -0.5709 -0.2990 314 PRO B CG 2161 C CD . PRO A 283 ? 1.4082 0.6972 1.2603 0.3021 -0.5682 -0.2950 314 PRO B CD 2162 N N . SER A 284 ? 1.4452 0.6768 1.3613 0.3133 -0.6939 -0.2995 315 SER B N 2163 C CA . SER A 284 ? 1.4881 0.6777 1.3908 0.3032 -0.7307 -0.2842 315 SER B CA 2164 C C . SER A 284 ? 1.5081 0.6615 1.3699 0.2868 -0.7331 -0.2627 315 SER B C 2165 O O . SER A 284 ? 1.5420 0.6529 1.3699 0.2695 -0.7527 -0.2407 315 SER B O 2166 C CB . SER A 284 ? 1.5035 0.7088 1.4569 0.3193 -0.7629 -0.3059 315 SER B CB 2167 O OG . SER A 284 ? 1.5399 0.7133 1.4879 0.3119 -0.7971 -0.2955 315 SER B OG 2168 N N . GLY A 285 ? 1.6735 0.8452 1.5376 0.2914 -0.7121 -0.2695 316 GLY B N 2169 C CA . GLY A 285 ? 1.6903 0.8333 1.5224 0.2784 -0.7142 -0.2532 316 GLY B CA 2170 C C . GLY A 285 ? 1.6899 0.8051 1.4668 0.2567 -0.6927 -0.2277 316 GLY B C 2171 O O . GLY A 285 ? 1.7091 0.7950 1.4530 0.2418 -0.6959 -0.2108 316 GLY B O 2172 N N . PHE A 286 ? 1.4916 0.6162 1.2583 0.2543 -0.6708 -0.2254 317 PHE B N 2173 C CA . PHE A 286 ? 1.4921 0.5913 1.2076 0.2332 -0.6506 -0.2023 317 PHE B CA 2174 C C . PHE A 286 ? 1.5345 0.5855 1.2107 0.2109 -0.6738 -0.1773 317 PHE B C 2175 O O . PHE A 286 ? 1.5412 0.5682 1.1726 0.1905 -0.6598 -0.1575 317 PHE B O 2176 C CB . PHE A 286 ? 1.4654 0.5829 1.1794 0.2350 -0.6263 -0.2055 317 PHE B CB 2177 C CG . PHE A 286 ? 1.4288 0.5727 1.1389 0.2384 -0.5895 -0.2122 317 PHE B CG 2178 C CD1 . PHE A 286 ? 1.4281 0.5594 1.1102 0.2274 -0.5755 -0.2015 317 PHE B CD1 2179 C CD2 . PHE A 286 ? 1.3962 0.5782 1.1307 0.2521 -0.5694 -0.2298 317 PHE B CD2 2180 C CE1 . PHE A 286 ? 1.3956 0.5510 1.0740 0.2302 -0.5427 -0.2077 317 PHE B CE1 2181 C CE2 . PHE A 286 ? 1.3643 0.5709 1.0936 0.2542 -0.5365 -0.2359 317 PHE B CE2 2182 C CZ . PHE A 286 ? 1.3641 0.5569 1.0655 0.2435 -0.5235 -0.2246 317 PHE B CZ 2183 N N . SER A 287 ? 1.5551 0.5936 1.2484 0.2141 -0.7094 -0.1792 318 SER B N 2184 C CA . SER A 287 ? 1.5998 0.5939 1.2585 0.1932 -0.7364 -0.1572 318 SER B CA 2185 C C . SER A 287 ? 1.6198 0.5896 1.2493 0.1790 -0.7398 -0.1439 318 SER B C 2186 O O . SER A 287 ? 1.6556 0.5883 1.2466 0.1571 -0.7554 -0.1231 318 SER B O 2187 C CB . SER A 287 ? 1.6270 0.6166 1.3169 0.2024 -0.7761 -0.1660 318 SER B CB 2188 O OG . SER A 287 ? 1.6046 0.6255 1.3342 0.2209 -0.7737 -0.1850 318 SER B OG 2189 N N . THR A 288 ? 1.6381 0.6299 1.2855 0.1909 -0.7253 -0.1562 319 THR B N 2190 C CA . THR A 288 ? 1.6572 0.6292 1.2852 0.1811 -0.7322 -0.1473 319 THR B CA 2191 C C . THR A 288 ? 1.6480 0.6088 1.2330 0.1631 -0.7026 -0.1316 319 THR B C 2192 O O . THR A 288 ? 1.6660 0.6083 1.2315 0.1527 -0.7084 -0.1227 319 THR B O 2193 C CB . THR A 288 ? 1.6448 0.6434 1.3166 0.2029 -0.7384 -0.1692 319 THR B CB 2194 O OG1 . THR A 288 ? 1.5998 0.6363 1.2896 0.2164 -0.7039 -0.1841 319 THR B OG1 2195 C CG2 . THR A 288 ? 1.6567 0.6672 1.3738 0.2203 -0.7697 -0.1866 319 THR B CG2 2196 N N . LEU A 289 ? 1.5838 0.5551 1.1536 0.1586 -0.6719 -0.1285 320 LEU B N 2197 C CA . LEU A 289 ? 1.5742 0.5378 1.1078 0.1428 -0.6441 -0.1165 320 LEU B CA 2198 C C . LEU A 289 ? 1.6070 0.5327 1.0909 0.1140 -0.6498 -0.0918 320 LEU B C 2199 O O . LEU A 289 ? 1.6041 0.5258 1.0711 0.1050 -0.6398 -0.0845 320 LEU B O 2200 C CB . LEU A 289 ? 1.5308 0.5245 1.0705 0.1505 -0.6071 -0.1254 320 LEU B CB 2201 C CG . LEU A 289 ? 1.4975 0.5332 1.0865 0.1780 -0.6004 -0.1506 320 LEU B CG 2202 C CD1 . LEU A 289 ? 1.4598 0.5198 1.0445 0.1804 -0.5635 -0.1556 320 LEU B CD1 2203 C CD2 . LEU A 289 ? 1.4925 0.5457 1.1133 0.1940 -0.6089 -0.1661 320 LEU B CD2 2204 N N . LYS A 290 ? 1.9689 0.8681 1.4280 0.0986 -0.6640 -0.0793 321 LYS B N 2205 C CA . LYS A 290 ? 2.0070 0.8700 1.4198 0.0703 -0.6751 -0.0568 321 LYS B CA 2206 C C . LYS A 290 ? 1.9981 0.8554 1.3719 0.0502 -0.6437 -0.0449 321 LYS B C 2207 O O . LYS A 290 ? 2.0269 0.8575 1.3582 0.0237 -0.6459 -0.0266 321 LYS B O 2208 C CB . LYS A 290 ? 2.0502 0.8867 1.4558 0.0627 -0.7106 -0.0496 321 LYS B CB 2209 C CG . LYS A 290 ? 2.0633 0.9038 1.5082 0.0814 -0.7450 -0.0619 321 LYS B CG 2210 C CD . LYS A 290 ? 2.0858 0.9110 1.5211 0.0729 -0.7632 -0.0540 321 LYS B CD 2211 C CE . LYS A 290 ? 2.1162 0.9325 1.5790 0.0830 -0.8063 -0.0609 321 LYS B CE 2212 N NZ . LYS A 290 ? 2.1467 0.9423 1.5952 0.0711 -0.8293 -0.0509 321 LYS B NZ 2213 N N . ASN A 291 ? 1.6626 0.5459 1.0509 0.0620 -0.6147 -0.0562 322 ASN B N 2214 C CA . ASN A 291 ? 1.6501 0.5319 1.0054 0.0444 -0.5827 -0.0473 322 ASN B CA 2215 C C . ASN A 291 ? 1.6197 0.5200 0.9771 0.0478 -0.5566 -0.0515 322 ASN B C 2216 O O . ASN A 291 ? 1.6073 0.5088 0.9400 0.0342 -0.5289 -0.0459 322 ASN B O 2217 C CB . ASN A 291 ? 1.6358 0.5265 0.9928 0.0469 -0.5676 -0.0520 322 ASN B CB 2218 C CG . ASN A 291 ? 1.6722 0.5325 0.9919 0.0222 -0.5775 -0.0354 322 ASN B CG 2219 O OD1 . ASN A 291 ? 1.7096 0.5429 1.0031 0.0039 -0.5976 -0.0211 322 ASN B OD1 2220 N ND2 . ASN A 291 ? 1.6628 0.5279 0.9790 0.0210 -0.5637 -0.0376 322 ASN B ND2 2221 N N . LEU A 292 ? 1.5728 0.4869 0.9596 0.0652 -0.5664 -0.0616 323 LEU B N 2222 C CA . LEU A 292 ? 1.5430 0.4773 0.9372 0.0719 -0.5440 -0.0679 323 LEU B CA 2223 C C . LEU A 292 ? 1.5571 0.4723 0.9133 0.0484 -0.5359 -0.0517 323 LEU B C 2224 O O . LEU A 292 ? 1.5881 0.4816 0.9312 0.0377 -0.5587 -0.0413 323 LEU B O 2225 C CB . LEU A 292 ? 1.5320 0.4862 0.9693 0.0965 -0.5595 -0.0839 323 LEU B CB 2226 C CG . LEU A 292 ? 1.4982 0.4791 0.9517 0.1085 -0.5380 -0.0947 323 LEU B CG 2227 C CD1 . LEU A 292 ? 1.4605 0.4712 0.9274 0.1204 -0.5088 -0.1078 323 LEU B CD1 2228 C CD2 . LEU A 292 ? 1.4960 0.4921 0.9893 0.1290 -0.5586 -0.1088 323 LEU B CD2 2229 N N . THR A 293 ? 1.5476 0.4724 0.8873 0.0408 -0.5038 -0.0506 324 THR B N 2230 C CA . THR A 293 ? 1.5600 0.4687 0.8628 0.0169 -0.4929 -0.0362 324 THR B CA 2231 C C . THR A 293 ? 1.5347 0.4678 0.8529 0.0271 -0.4772 -0.0429 324 THR B C 2232 O O . THR A 293 ? 1.5508 0.4694 0.8590 0.0200 -0.4886 -0.0364 324 THR B O 2233 C CB . THR A 293 ? 1.5601 0.4622 0.8281 -0.0052 -0.4674 -0.0274 324 THR B CB 2234 O OG1 . THR A 293 ? 1.5177 0.4630 0.8011 0.0037 -0.4316 -0.0354 324 THR B OG1 2235 C CG2 . THR A 293 ? 1.5717 0.4660 0.8362 -0.0081 -0.4745 -0.0260 324 THR B CG2 2236 N N . TRP A 294 ? 1.5361 0.5146 0.8790 0.0419 -0.4483 -0.0542 325 TRP B N 2237 C CA . TRP A 294 ? 1.5066 0.5225 0.8700 0.0529 -0.4291 -0.0609 325 TRP B CA 2238 C C . TRP A 294 ? 1.4873 0.5303 0.8967 0.0815 -0.4388 -0.0792 325 TRP B C 2239 O O . TRP A 294 ? 1.4707 0.5331 0.9024 0.0961 -0.4341 -0.0909 325 TRP B O 2240 C CB . TRP A 294 ? 1.4863 0.5359 0.8473 0.0499 -0.3907 -0.0616 325 TRP B CB 2241 C CG . TRP A 294 ? 1.4713 0.5572 0.8465 0.0564 -0.3679 -0.0656 325 TRP B CG 2242 C CD1 . TRP A 294 ? 1.4558 0.5747 0.8669 0.0780 -0.3659 -0.0790 325 TRP B CD1 2243 C CD2 . TRP A 294 ? 1.4708 0.5645 0.8248 0.0405 -0.3431 -0.0567 325 TRP B CD2 2244 N NE1 . TRP A 294 ? 1.4470 0.5917 0.8585 0.0757 -0.3423 -0.0776 325 TRP B NE1 2245 C CE2 . TRP A 294 ? 1.4553 0.5847 0.8329 0.0536 -0.3284 -0.0642 325 TRP B CE2 2246 C CE3 . TRP A 294 ? 1.4820 0.5563 0.7997 0.0160 -0.3322 -0.0441 325 TRP B CE3 2247 C CZ2 . TRP A 294 ? 1.4506 0.5949 0.8171 0.0437 -0.3047 -0.0588 325 TRP B CZ2 2248 C CZ3 . TRP A 294 ? 1.4766 0.5672 0.7849 0.0067 -0.3080 -0.0403 325 TRP B CZ3 2249 C CH2 . TRP A 294 ? 1.4608 0.5852 0.7934 0.0209 -0.2950 -0.0472 325 TRP B CH2 2250 N N . LEU A 295 ? 1.4209 0.4672 0.8451 0.0891 -0.4513 -0.0827 326 LEU B N 2251 C CA . LEU A 295 ? 1.3973 0.4770 0.8668 0.1152 -0.4551 -0.1021 326 LEU B CA 2252 C C . LEU A 295 ? 1.3663 0.4825 0.8492 0.1203 -0.4341 -0.1061 326 LEU B C 2253 O O . LEU A 295 ? 1.3799 0.4838 0.8559 0.1146 -0.4445 -0.1002 326 LEU B O 2254 C CB . LEU A 295 ? 1.4296 0.4820 0.9146 0.1243 -0.4950 -0.1074 326 LEU B CB 2255 C CG . LEU A 295 ? 1.4105 0.4955 0.9437 0.1503 -0.5028 -0.1288 326 LEU B CG 2256 C CD1 . LEU A 295 ? 1.3774 0.5016 0.9385 0.1668 -0.4845 -0.1454 326 LEU B CD1 2257 C CD2 . LEU A 295 ? 1.4466 0.4999 0.9946 0.1583 -0.5448 -0.1338 326 LEU B CD2 2258 N N . SER A 296 ? 1.3265 0.4867 0.8286 0.1307 -0.4063 -0.1160 327 SER B N 2259 C CA . SER A 296 ? 1.2986 0.4925 0.8115 0.1340 -0.3865 -0.1189 327 SER B CA 2260 C C . SER A 296 ? 1.2685 0.5075 0.8235 0.1561 -0.3798 -0.1391 327 SER B C 2261 O O . SER A 296 ? 1.2466 0.5131 0.8133 0.1631 -0.3617 -0.1470 327 SER B O 2262 C CB . SER A 296 ? 1.2829 0.4869 0.7706 0.1187 -0.3547 -0.1074 327 SER B CB 2263 O OG . SER A 296 ? 1.2589 0.5015 0.7620 0.1247 -0.3331 -0.1126 327 SER B OG 2264 N N . LEU A 297 ? 1.3014 0.5479 0.8786 0.1660 -0.3949 -0.1477 328 LEU B N 2265 C CA . LEU A 297 ? 1.2840 0.5745 0.9018 0.1856 -0.3899 -0.1683 328 LEU B CA 2266 C C . LEU A 297 ? 1.2782 0.6030 0.9009 0.1843 -0.3669 -0.1686 328 LEU B C 2267 O O . LEU A 297 ? 1.2684 0.6279 0.9234 0.1981 -0.3655 -0.1849 328 LEU B O 2268 C CB . LEU A 297 ? 1.2876 0.5700 0.9355 0.2008 -0.4225 -0.1828 328 LEU B CB 2269 C CG . LEU A 297 ? 1.2825 0.5470 0.9385 0.2084 -0.4407 -0.1900 328 LEU B CG 2270 C CD1 . LEU A 297 ? 1.2853 0.5648 0.9858 0.2299 -0.4632 -0.2134 328 LEU B CD1 2271 C CD2 . LEU A 297 ? 1.2628 0.5473 0.9138 0.2078 -0.4156 -0.1912 328 LEU B CD2 2272 N N . ILE A 298 ? 1.3137 0.6278 0.9045 0.1670 -0.3504 -0.1510 329 ILE B N 2273 C CA . ILE A 298 ? 1.3141 0.6487 0.9032 0.1625 -0.3342 -0.1475 329 ILE B CA 2274 C C . ILE A 298 ? 1.2963 0.6818 0.9150 0.1750 -0.3158 -0.1627 329 ILE B C 2275 O O . ILE A 298 ? 1.2814 0.6889 0.9078 0.1798 -0.3007 -0.1691 329 ILE B O 2276 C CB . ILE A 298 ? 1.3158 0.6412 0.8702 0.1440 -0.3114 -0.1300 329 ILE B CB 2277 C CG1 . ILE A 298 ? 1.3348 0.6120 0.8553 0.1275 -0.3256 -0.1142 329 ILE B CG1 2278 C CG2 . ILE A 298 ? 1.3158 0.6618 0.8681 0.1391 -0.2942 -0.1261 329 ILE B CG2 2279 C CD1 . ILE A 298 ? 1.3347 0.6052 0.8241 0.1100 -0.3025 -0.1003 329 ILE B CD1 2280 N N . SER A 299 ? 1.2135 0.6175 0.8480 0.1793 -0.3174 -0.1684 330 SER B N 2281 C CA . SER A 299 ? 1.1991 0.6509 0.8535 0.1853 -0.2958 -0.1787 330 SER B CA 2282 C C . SER A 299 ? 1.1819 0.6669 0.8681 0.2009 -0.2939 -0.1992 330 SER B C 2283 O O . SER A 299 ? 1.1680 0.6745 0.8528 0.2003 -0.2736 -0.2007 330 SER B O 2284 C CB . SER A 299 ? 1.1947 0.6540 0.8243 0.1719 -0.2672 -0.1648 330 SER B CB 2285 O OG . SER A 299 ? 1.1851 0.6859 0.8296 0.1748 -0.2484 -0.1718 330 SER B OG 2286 N N . ASN A 300 ? 1.2130 0.7018 0.9284 0.2146 -0.3160 -0.2156 331 ASN B N 2287 C CA . ASN A 300 ? 1.1962 0.7165 0.9451 0.2302 -0.3174 -0.2381 331 ASN B CA 2288 C C . ASN A 300 ? 1.1962 0.7418 0.9805 0.2421 -0.3293 -0.2570 331 ASN B C 2289 O O . ASN A 300 ? 1.2086 0.7519 0.9893 0.2373 -0.3315 -0.2512 331 ASN B O 2290 C CB . ASN A 300 ? 1.1950 0.6867 0.9457 0.2362 -0.3377 -0.2413 331 ASN B CB 2291 C CG . ASN A 300 ? 1.1843 0.6763 0.9187 0.2317 -0.3208 -0.2357 331 ASN B CG 2292 O OD1 . ASN A 300 ? 1.1681 0.6832 0.9230 0.2419 -0.3175 -0.2513 331 ASN B OD1 2293 N ND2 . ASN A 300 ? 1.1926 0.6598 0.8907 0.2159 -0.3096 -0.2141 331 ASN B ND2 2294 N N . ASN A 301 ? 1.4401 1.0121 1.2594 0.2573 -0.3359 -0.2807 332 ASN B N 2295 C CA . ASN A 301 ? 1.4371 1.0323 1.2946 0.2701 -0.3505 -0.3019 332 ASN B CA 2296 C C . ASN A 301 ? 1.4434 1.0048 1.3162 0.2802 -0.3865 -0.3083 332 ASN B C 2297 O O . ASN A 301 ? 1.4396 1.0185 1.3496 0.2936 -0.4028 -0.3292 332 ASN B O 2298 C CB . ASN A 301 ? 1.4190 1.0686 1.3098 0.2805 -0.3364 -0.3274 332 ASN B CB 2299 C CG . ASN A 301 ? 1.4259 1.1116 1.3480 0.2867 -0.3376 -0.3449 332 ASN B CG 2300 O OD1 . ASN A 301 ? 1.4287 1.1117 1.3385 0.2783 -0.3332 -0.3333 332 ASN B OD1 2301 N ND2 . ASN A 301 ? 1.4290 1.1492 1.3926 0.3014 -0.3438 -0.3740 332 ASN B ND2 2302 N N . LEU A 302 ? 1.2743 0.7876 1.1188 0.2733 -0.3993 -0.2907 333 LEU B N 2303 C CA . LEU A 302 ? 1.2809 0.7578 1.1365 0.2819 -0.4343 -0.2956 333 LEU B CA 2304 C C . LEU A 302 ? 1.2932 0.7602 1.1726 0.2898 -0.4631 -0.3040 333 LEU B C 2305 O O . LEU A 302 ? 1.3054 0.7719 1.1751 0.2823 -0.4599 -0.2946 333 LEU B O 2306 C CB . LEU A 302 ? 1.2945 0.7187 1.1076 0.2677 -0.4415 -0.2705 333 LEU B CB 2307 C CG . LEU A 302 ? 1.2855 0.7006 1.0922 0.2694 -0.4393 -0.2715 333 LEU B CG 2308 C CD1 . LEU A 302 ? 1.2608 0.7209 1.1074 0.2866 -0.4326 -0.2990 333 LEU B CD1 2309 C CD2 . LEU A 302 ? 1.2878 0.6954 1.0538 0.2523 -0.4123 -0.2502 333 LEU B CD2 2310 N N . SER A 303 ? 1.2780 0.7376 1.1898 0.3055 -0.4917 -0.3224 334 SER B N 2311 C CA . SER A 303 ? 1.2864 0.7399 1.2286 0.3160 -0.5215 -0.3347 334 SER B CA 2312 C C . SER A 303 ? 1.3042 0.7084 1.2525 0.3223 -0.5633 -0.3347 334 SER B C 2313 O O . SER A 303 ? 1.3171 0.6857 1.2408 0.3165 -0.5708 -0.3222 334 SER B O 2314 C CB . SER A 303 ? 1.2640 0.7750 1.2579 0.3333 -0.5154 -0.3674 334 SER B CB 2315 O OG . SER A 303 ? 1.2670 0.7705 1.2966 0.3465 -0.5485 -0.3833 334 SER B OG 2316 N N . GLY A 304 ? 1.4072 0.8088 1.3882 0.3338 -0.5915 -0.3486 335 GLY B N 2317 C CA . GLY A 304 ? 1.4374 0.7958 1.4308 0.3415 -0.6341 -0.3513 335 GLY B CA 2318 C C . GLY A 304 ? 1.4679 0.7660 1.4130 0.3219 -0.6512 -0.3183 335 GLY B C 2319 O O . GLY A 304 ? 1.4653 0.7499 1.3662 0.3041 -0.6295 -0.2958 335 GLY B O 2320 N N . GLU A 305 ? 1.5716 0.8448 1.5252 0.3211 -0.6867 -0.3128 336 GLU B N 2321 C CA . GLU A 305 ? 1.6068 0.8243 1.5150 0.3007 -0.7059 -0.2822 336 GLU B CA 2322 C C . GLU A 305 ? 1.6102 0.8026 1.4746 0.2857 -0.6916 -0.2628 336 GLU B C 2323 O O . GLU A 305 ? 1.5892 0.8047 1.4633 0.2931 -0.6735 -0.2736 336 GLU B O 2324 C CB . GLU A 305 ? 1.6431 0.8426 1.5724 0.3031 -0.7490 -0.2834 336 GLU B CB 2325 C CG . GLU A 305 ? 1.6493 0.8612 1.6127 0.3125 -0.7686 -0.2963 336 GLU B CG 2326 C CD . GLU A 305 ? 1.6914 0.8778 1.6682 0.3109 -0.8138 -0.2941 336 GLU B CD 2327 O OE1 . GLU A 305 ? 1.7064 0.8845 1.6911 0.3097 -0.8325 -0.2932 336 GLU B OE1 2328 O OE2 . GLU A 305 ? 1.7104 0.8850 1.6901 0.3103 -0.8314 -0.2939 336 GLU B OE2 2329 N N . VAL A 306 ? 1.4903 0.6370 1.3058 0.2637 -0.6984 -0.2343 337 VAL B N 2330 C CA . VAL A 306 ? 1.4990 0.6189 1.2718 0.2471 -0.6885 -0.2148 337 VAL B CA 2331 C C . VAL A 306 ? 1.5352 0.6296 1.3086 0.2429 -0.7224 -0.2084 337 VAL B C 2332 O O . VAL A 306 ? 1.5666 0.6383 1.3390 0.2372 -0.7525 -0.2012 337 VAL B O 2333 C CB . VAL A 306 ? 1.5099 0.5955 1.2274 0.2226 -0.6765 -0.1879 337 VAL B CB 2334 C CG1 . VAL A 306 ? 1.5303 0.5831 1.2049 0.2029 -0.6759 -0.1667 337 VAL B CG1 2335 C CG2 . VAL A 306 ? 1.4791 0.5873 1.1896 0.2243 -0.6398 -0.1928 337 VAL B CG2 2336 N N . PRO A 307 ? 1.5182 0.6159 1.2926 0.2452 -0.7184 -0.2113 338 PRO B N 2337 C CA . PRO A 307 ? 1.5513 0.6291 1.3320 0.2437 -0.7513 -0.2091 338 PRO B CA 2338 C C . PRO A 307 ? 1.5949 0.6230 1.3315 0.2195 -0.7747 -0.1821 338 PRO B C 2339 O O . PRO A 307 ? 1.5993 0.6038 1.2875 0.1990 -0.7579 -0.1607 338 PRO B O 2340 C CB . PRO A 307 ? 1.5372 0.6225 1.3110 0.2446 -0.7331 -0.2106 338 PRO B CB 2341 C CG . PRO A 307 ? 1.4916 0.6184 1.2833 0.2578 -0.6972 -0.2271 338 PRO B CG 2342 C CD . PRO A 307 ? 1.4836 0.6062 1.2565 0.2502 -0.6838 -0.2187 338 PRO B CD 2343 N N . GLU A 308 ? 1.8754 0.8893 1.6290 0.2210 -0.8131 -0.1843 339 GLU B N 2344 C CA . GLU A 308 ? 1.9203 0.8889 1.6347 0.1978 -0.8390 -0.1607 339 GLU B CA 2345 C C . GLU A 308 ? 1.9384 0.8785 1.6085 0.1782 -0.8351 -0.1412 339 GLU B C 2346 O O . GLU A 308 ? 1.9656 0.8712 1.5873 0.1531 -0.8388 -0.1175 339 GLU B O 2347 C CB . GLU A 308 ? 1.9531 0.9143 1.6996 0.2052 -0.8832 -0.1707 339 GLU B CB 2348 C CG . GLU A 308 ? 2.0027 0.9188 1.7128 0.1817 -0.9142 -0.1489 339 GLU B CG 2349 C CD . GLU A 308 ? 2.0395 0.9447 1.7790 0.1876 -0.9598 -0.1591 339 GLU B CD 2350 O OE1 . GLU A 308 ? 2.0780 0.9540 1.8027 0.1738 -0.9896 -0.1486 339 GLU B OE1 2351 O OE2 . GLU A 308 ? 2.0306 0.9566 1.8084 0.2056 -0.9660 -0.1782 339 GLU B OE2 2352 N N . GLY A 309 ? 1.7500 0.7074 1.4375 0.1895 -0.8256 -0.1524 340 GLY B N 2353 C CA . GLY A 309 ? 1.7661 0.7006 1.4194 0.1743 -0.8237 -0.1377 340 GLY B CA 2354 C C . GLY A 309 ? 1.7563 0.6776 1.3590 0.1537 -0.7913 -0.1179 340 GLY B C 2355 O O . GLY A 309 ? 1.7750 0.6724 1.3420 0.1361 -0.7907 -0.1024 340 GLY B O 2356 N N . ILE A 310 ? 1.6520 0.5890 1.2514 0.1553 -0.7644 -0.1190 341 ILE B N 2357 C CA . ILE A 310 ? 1.6424 0.5683 1.1955 0.1356 -0.7331 -0.1018 341 ILE B CA 2358 C C . ILE A 310 ? 1.6815 0.5686 1.1876 0.1075 -0.7472 -0.0775 341 ILE B C 2359 O O . ILE A 310 ? 1.6834 0.5557 1.1455 0.0861 -0.7261 -0.0608 341 ILE B O 2360 C CB . ILE A 310 ? 1.5992 0.5548 1.1625 0.1455 -0.6983 -0.1113 341 ILE B CB 2361 C CG1 . ILE A 310 ? 1.5645 0.5620 1.1798 0.1743 -0.6898 -0.1383 341 ILE B CG1 2362 C CG2 . ILE A 310 ? 1.5861 0.5347 1.1078 0.1280 -0.6647 -0.0977 341 ILE B CG2 2363 C CD1 . ILE A 310 ? 1.5243 0.5532 1.1526 0.1850 -0.6587 -0.1501 341 ILE B CD1 2364 N N . GLY A 311 ? 1.9363 0.8083 1.4527 0.1073 -0.7835 -0.0768 342 GLY B N 2365 C CA . GLY A 311 ? 1.9776 0.8136 1.4520 0.0809 -0.8018 -0.0556 342 GLY B CA 2366 C C . GLY A 311 ? 2.0023 0.8108 1.4273 0.0548 -0.7977 -0.0360 342 GLY B C 2367 O O . GLY A 311 ? 2.0121 0.8041 1.3923 0.0307 -0.7832 -0.0186 342 GLY B O 2368 N N . GLU A 312 ? 2.0438 0.8484 1.4769 0.0590 -0.8102 -0.0395 343 GLU B N 2369 C CA . GLU A 312 ? 2.0615 0.8452 1.4511 0.0364 -0.8017 -0.0235 343 GLU B CA 2370 C C . GLU A 312 ? 2.0301 0.8340 1.4335 0.0486 -0.7778 -0.0330 343 GLU B C 2371 O O . GLU A 312 ? 2.0311 0.8423 1.4639 0.0642 -0.7929 -0.0447 343 GLU B O 2372 C CB . GLU A 312 ? 2.1148 0.8654 1.4859 0.0211 -0.8410 -0.0127 343 GLU B CB 2373 C CG . GLU A 312 ? 2.1256 0.8817 1.5434 0.0431 -0.8755 -0.0290 343 GLU B CG 2374 C CD . GLU A 312 ? 2.1362 0.8938 1.5803 0.0524 -0.9008 -0.0365 343 GLU B CD 2375 O OE1 . GLU A 312 ? 2.1114 0.8970 1.6080 0.0801 -0.9045 -0.0582 343 GLU B OE1 2376 O OE2 . GLU A 312 ? 2.1700 0.9015 1.5825 0.0314 -0.9169 -0.0216 343 GLU B OE2 2377 N N . LEU A 313 ? 1.8381 0.6506 1.2191 0.0403 -0.7404 -0.0280 344 LEU B N 2378 C CA . LEU A 313 ? 1.8188 0.6400 1.1943 0.0406 -0.7172 -0.0299 344 LEU B CA 2379 C C . LEU A 313 ? 1.8428 0.6378 1.1618 0.0079 -0.7068 -0.0082 344 LEU B C 2380 O O . LEU A 313 ? 1.8345 0.6297 1.1315 -0.0042 -0.6868 -0.0011 344 LEU B O 2381 C CB . LEU A 313 ? 1.7677 0.6228 1.1641 0.0571 -0.6806 -0.0434 344 LEU B CB 2382 C CG . LEU A 313 ? 1.7373 0.6241 1.1840 0.0861 -0.6805 -0.0646 344 LEU B CG 2383 C CD1 . LEU A 313 ? 1.6911 0.6099 1.1538 0.1000 -0.6449 -0.0778 344 LEU B CD1 2384 C CD2 . LEU A 313 ? 1.7507 0.6421 1.2368 0.1045 -0.7136 -0.0779 344 LEU B CD2 2385 N N . PRO A 314 ? 2.1512 0.9247 1.4466 -0.0072 -0.7201 0.0017 345 PRO B N 2386 C CA . PRO A 314 ? 2.1814 0.9288 1.4214 -0.0409 -0.7147 0.0222 345 PRO B CA 2387 C C . PRO A 314 ? 2.1527 0.9121 1.3706 -0.0519 -0.6726 0.0256 345 PRO B C 2388 O O . PRO A 314 ? 2.1717 0.9160 1.3485 -0.0782 -0.6644 0.0399 345 PRO B O 2389 C CB . PRO A 314 ? 2.2014 0.9361 1.4325 -0.0465 -0.7259 0.0254 345 PRO B CB 2390 C CG . PRO A 314 ? 2.1999 0.9434 1.4780 -0.0195 -0.7530 0.0103 345 PRO B CG 2391 C CD . PRO A 314 ? 2.1558 0.9317 1.4765 0.0073 -0.7376 -0.0075 345 PRO B CD 2392 N N . GLU A 315 ? 2.0707 0.8578 1.3162 -0.0322 -0.6468 0.0115 346 GLU B N 2393 C CA . GLU A 315 ? 2.0422 0.8420 1.2705 -0.0407 -0.6072 0.0126 346 GLU B CA 2394 C C . GLU A 315 ? 2.0084 0.8293 1.2511 -0.0301 -0.5854 0.0049 346 GLU B C 2395 O O . GLU A 315 ? 1.9865 0.8173 1.2143 -0.0381 -0.5534 0.0056 346 GLU B O 2396 C CB . GLU A 315 ? 2.0189 0.8331 1.2591 -0.0314 -0.5897 0.0041 346 GLU B CB 2397 C CG . GLU A 315 ? 2.0445 0.8388 1.2457 -0.0570 -0.5862 0.0173 346 GLU B CG 2398 C CD . GLU A 315 ? 2.0966 0.8594 1.2711 -0.0763 -0.6194 0.0319 346 GLU B CD 2399 O OE1 . GLU A 315 ? 2.1138 0.8692 1.3066 -0.0653 -0.6482 0.0286 346 GLU B OE1 2400 O OE2 . GLU A 315 ? 2.1214 0.8674 1.2564 -0.1029 -0.6170 0.0460 346 GLU B OE2 2401 N N . LEU A 316 ? 1.7298 0.5581 1.0017 -0.0126 -0.6026 -0.0029 347 LEU B N 2402 C CA . LEU A 316 ? 1.6953 0.5465 0.9860 0.0007 -0.5826 -0.0125 347 LEU B CA 2403 C C . LEU A 316 ? 1.6997 0.5418 0.9532 -0.0224 -0.5636 0.0002 347 LEU B C 2404 O O . LEU A 316 ? 1.7344 0.5531 0.9587 -0.0432 -0.5791 0.0144 347 LEU B O 2405 C CB . LEU A 316 ? 1.6928 0.5539 1.0224 0.0230 -0.6060 -0.0238 347 LEU B CB 2406 C CG . LEU A 316 ? 1.6588 0.5440 1.0083 0.0369 -0.5867 -0.0343 347 LEU B CG 2407 C CD1 . LEU A 316 ? 1.6180 0.5300 0.9800 0.0486 -0.5540 -0.0462 347 LEU B CD1 2408 C CD2 . LEU A 316 ? 1.6547 0.5536 1.0477 0.0608 -0.6095 -0.0486 347 LEU B CD2 2409 N N . THR A 317 ? 1.8026 0.6645 1.0577 -0.0190 -0.5304 -0.0060 348 THR B N 2410 C CA . THR A 317 ? 1.8032 0.6597 1.0241 -0.0411 -0.5078 0.0041 348 THR B CA 2411 C C . THR A 317 ? 1.7718 0.6505 1.0118 -0.0273 -0.4908 -0.0053 348 THR B C 2412 O O . THR A 317 ? 1.7823 0.6528 1.0115 -0.0354 -0.4959 0.0010 348 THR B O 2413 C CB . THR A 317 ? 1.7973 0.6540 0.9923 -0.0577 -0.4810 0.0080 348 THR B CB 2414 O OG1 . THR A 317 ? 1.8371 0.6680 0.9981 -0.0824 -0.4951 0.0226 348 THR B OG1 2415 C CG2 . THR A 317 ? 1.7775 0.6490 0.9565 -0.0695 -0.4484 0.0098 348 THR B CG2 2416 N N . THR A 318 ? 1.5348 0.4572 0.8076 -0.0067 -0.4672 -0.0191 349 THR B N 2417 C CA . THR A 318 ? 1.4960 0.4588 0.7924 0.0065 -0.4457 -0.0270 349 THR B CA 2418 C C . THR A 318 ? 1.4790 0.4632 0.8212 0.0355 -0.4600 -0.0431 349 THR B C 2419 O O . THR A 318 ? 1.4618 0.4637 0.8299 0.0526 -0.4588 -0.0551 349 THR B O 2420 C CB . THR A 318 ? 1.4557 0.4558 0.7557 0.0074 -0.4066 -0.0311 349 THR B CB 2421 O OG1 . THR A 318 ? 1.4684 0.4542 0.7293 -0.0193 -0.3906 -0.0183 349 THR B OG1 2422 C CG2 . THR A 318 ? 1.4150 0.4582 0.7436 0.0236 -0.3866 -0.0406 349 THR B CG2 2423 N N . LEU A 319 ? 1.4847 0.4678 0.8372 0.0405 -0.4738 -0.0441 350 LEU B N 2424 C CA . LEU A 319 ? 1.4674 0.4750 0.8656 0.0674 -0.4858 -0.0612 350 LEU B CA 2425 C C . LEU A 319 ? 1.4313 0.4803 0.8503 0.0771 -0.4642 -0.0684 350 LEU B C 2426 O O . LEU A 319 ? 1.4418 0.4819 0.8507 0.0693 -0.4695 -0.0617 350 LEU B O 2427 C CB . LEU A 319 ? 1.5078 0.4785 0.9091 0.0691 -0.5275 -0.0597 350 LEU B CB 2428 C CG . LEU A 319 ? 1.4916 0.4886 0.9421 0.0964 -0.5407 -0.0790 350 LEU B CG 2429 C CD1 . LEU A 319 ? 1.4789 0.4916 0.9599 0.1156 -0.5440 -0.0950 350 LEU B CD1 2430 C CD2 . LEU A 319 ? 1.5298 0.4924 0.9817 0.0956 -0.5791 -0.0758 350 LEU B CD2 2431 N N . PHE A 320 ? 1.3971 0.4905 0.8445 0.0935 -0.4410 -0.0820 351 PHE B N 2432 C CA . PHE A 320 ? 1.3823 0.5154 0.8493 0.1021 -0.4211 -0.0890 351 PHE B CA 2433 C C . PHE A 320 ? 1.3680 0.5315 0.8815 0.1275 -0.4302 -0.1095 351 PHE B C 2434 O O . PHE A 320 ? 1.3507 0.5398 0.8856 0.1404 -0.4203 -0.1217 351 PHE B O 2435 C CB . PHE A 320 ? 1.3637 0.5276 0.8246 0.0982 -0.3836 -0.0879 351 PHE B CB 2436 C CG . PHE A 320 ? 1.3751 0.5178 0.7945 0.0740 -0.3690 -0.0707 351 PHE B CG 2437 C CD1 . PHE A 320 ? 1.3996 0.5019 0.7878 0.0555 -0.3860 -0.0570 351 PHE B CD1 2438 C CD2 . PHE A 320 ? 1.3617 0.5265 0.7743 0.0692 -0.3379 -0.0693 351 PHE B CD2 2439 C CE1 . PHE A 320 ? 1.4096 0.4959 0.7607 0.0323 -0.3708 -0.0434 351 PHE B CE1 2440 C CE2 . PHE A 320 ? 1.3705 0.5192 0.7485 0.0475 -0.3233 -0.0562 351 PHE B CE2 2441 C CZ . PHE A 320 ? 1.3939 0.5045 0.7411 0.0288 -0.3390 -0.0438 351 PHE B CZ 2442 N N . LEU A 321 ? 1.3506 0.5118 0.8803 0.1342 -0.4498 -0.1141 352 LEU B N 2443 C CA . LEU A 321 ? 1.3326 0.5279 0.9087 0.1574 -0.4563 -0.1354 352 LEU B CA 2444 C C . LEU A 321 ? 1.3093 0.5444 0.9011 0.1620 -0.4360 -0.1412 352 LEU B C 2445 O O . LEU A 321 ? 1.2980 0.5625 0.9277 0.1793 -0.4417 -0.1591 352 LEU B O 2446 C CB . LEU A 321 ? 1.3658 0.5334 0.9585 0.1658 -0.4964 -0.1412 352 LEU B CB 2447 C CG . LEU A 321 ? 1.3969 0.5251 0.9766 0.1624 -0.5189 -0.1366 352 LEU B CG 2448 C CD1 . LEU A 321 ? 1.4298 0.5317 1.0303 0.1724 -0.5607 -0.1439 352 LEU B CD1 2449 C CD2 . LEU A 321 ? 1.3728 0.5270 0.9685 0.1733 -0.5024 -0.1484 352 LEU B CD2 2450 N N . TRP A 322 ? 1.3130 0.5484 0.8762 0.1458 -0.4139 -0.1266 353 TRP B N 2451 C CA . TRP A 322 ? 1.3007 0.5646 0.8734 0.1469 -0.3998 -0.1287 353 TRP B CA 2452 C C . TRP A 322 ? 1.2695 0.5870 0.8743 0.1615 -0.3776 -0.1452 353 TRP B C 2453 O O . TRP A 322 ? 1.2530 0.5882 0.8643 0.1667 -0.3635 -0.1513 353 TRP B O 2454 C CB . TRP A 322 ? 1.3069 0.5557 0.8413 0.1256 -0.3836 -0.1094 353 TRP B CB 2455 C CG . TRP A 322 ? 1.2971 0.5446 0.8044 0.1127 -0.3578 -0.0992 353 TRP B CG 2456 C CD1 . TRP A 322 ? 1.3110 0.5269 0.7919 0.1010 -0.3621 -0.0894 353 TRP B CD1 2457 C CD2 . TRP A 322 ? 1.2770 0.5551 0.7811 0.1091 -0.3251 -0.0976 353 TRP B CD2 2458 N NE1 . TRP A 322 ? 1.2960 0.5227 0.7596 0.0914 -0.3335 -0.0832 353 TRP B NE1 2459 C CE2 . TRP A 322 ? 1.2747 0.5386 0.7525 0.0966 -0.3113 -0.0879 353 TRP B CE2 2460 C CE3 . TRP A 322 ? 1.2645 0.5802 0.7857 0.1151 -0.3071 -0.1036 353 TRP B CE3 2461 C CZ2 . TRP A 322 ? 1.2594 0.5452 0.7301 0.0912 -0.2816 -0.0849 353 TRP B CZ2 2462 C CZ3 . TRP A 322 ? 1.2502 0.5858 0.7620 0.1089 -0.2781 -0.0993 353 TRP B CZ3 2463 C CH2 . TRP A 322 ? 1.2473 0.5676 0.7351 0.0977 -0.2661 -0.0903 353 TRP B CH2 2464 N N . ASN A 323 ? 1.3744 0.7169 0.9982 0.1671 -0.3754 -0.1522 354 ASN B N 2465 C CA . ASN A 323 ? 1.3586 0.7532 1.0130 0.1792 -0.3563 -0.1685 354 ASN B CA 2466 C C . ASN A 323 ? 1.3452 0.7666 1.0393 0.1989 -0.3646 -0.1917 354 ASN B C 2467 O O . ASN A 323 ? 1.3304 0.7855 1.0362 0.2043 -0.3444 -0.2009 354 ASN B O 2468 C CB . ASN A 323 ? 1.3473 0.7623 0.9838 0.1698 -0.3223 -0.1602 354 ASN B CB 2469 C CG . ASN A 323 ? 1.3595 0.7678 0.9722 0.1552 -0.3106 -0.1452 354 ASN B CG 2470 O OD1 . ASN A 323 ? 1.3804 0.7552 0.9748 0.1462 -0.3264 -0.1344 354 ASN B OD1 2471 N ND2 . ASN A 323 ? 1.3468 0.7866 0.9594 0.1523 -0.2840 -0.1447 354 ASN B ND2 2472 N N . ASN A 324 ? 1.2983 0.7045 1.0132 0.2091 -0.3951 -0.2015 355 ASN B N 2473 C CA . ASN A 324 ? 1.2859 0.7197 1.0441 0.2288 -0.4059 -0.2266 355 ASN B CA 2474 C C . ASN A 324 ? 1.2939 0.7319 1.0792 0.2375 -0.4278 -0.2376 355 ASN B C 2475 O O . ASN A 324 ? 1.3071 0.7326 1.0764 0.2276 -0.4290 -0.2251 355 ASN B O 2476 C CB . ASN A 324 ? 1.2841 0.6905 1.0436 0.2345 -0.4253 -0.2296 355 ASN B CB 2477 C CG . ASN A 324 ? 1.2737 0.6784 1.0093 0.2268 -0.4038 -0.2205 355 ASN B CG 2478 O OD1 . ASN A 324 ? 1.2621 0.6992 0.9947 0.2239 -0.3745 -0.2206 355 ASN B OD1 2479 N ND2 . ASN A 324 ? 1.2785 0.6446 0.9971 0.2231 -0.4194 -0.2124 355 ASN B ND2 2480 N N . ASN A 325 ? 1.2313 0.6896 1.0592 0.2558 -0.4439 -0.2619 356 ASN B N 2481 C CA . ASN A 325 ? 1.2455 0.6986 1.1010 0.2653 -0.4723 -0.2729 356 ASN B CA 2482 C C . ASN A 325 ? 1.2641 0.6810 1.1301 0.2741 -0.5067 -0.2780 356 ASN B C 2483 O O . ASN A 325 ? 1.2542 0.6905 1.1522 0.2893 -0.5122 -0.2991 356 ASN B O 2484 C CB . ASN A 325 ? 1.2260 0.7363 1.1280 0.2801 -0.4638 -0.3006 356 ASN B CB 2485 C CG . ASN A 325 ? 1.2296 0.7495 1.1437 0.2796 -0.4704 -0.3024 356 ASN B CG 2486 O OD1 . ASN A 325 ? 1.2504 0.7327 1.1579 0.2774 -0.4971 -0.2935 356 ASN B OD1 2487 N ND2 . ASN A 325 ? 1.2104 0.7803 1.1409 0.2807 -0.4464 -0.3137 356 ASN B ND2 2488 N N . PHE A 326 ? 1.4779 0.8420 1.3175 0.2642 -0.5310 -0.2594 357 PHE B N 2489 C CA . PHE A 326 ? 1.4843 0.8065 1.3271 0.2694 -0.5658 -0.2602 357 PHE B CA 2490 C C . PHE A 326 ? 1.4973 0.7974 1.3581 0.2747 -0.6014 -0.2637 357 PHE B C 2491 O O . PHE A 326 ? 1.5018 0.8082 1.3578 0.2687 -0.5971 -0.2578 357 PHE B O 2492 C CB . PHE A 326 ? 1.5011 0.7745 1.2918 0.2497 -0.5659 -0.2327 357 PHE B CB 2493 C CG . PHE A 326 ? 1.4842 0.7653 1.2639 0.2487 -0.5460 -0.2323 357 PHE B CG 2494 C CD1 . PHE A 326 ? 1.4565 0.7635 1.2724 0.2667 -0.5479 -0.2552 357 PHE B CD1 2495 C CD2 . PHE A 326 ? 1.4959 0.7578 1.2294 0.2291 -0.5259 -0.2095 357 PHE B CD2 2496 C CE1 . PHE A 326 ? 1.4425 0.7553 1.2471 0.2651 -0.5303 -0.2541 357 PHE B CE1 2497 C CE2 . PHE A 326 ? 1.4810 0.7492 1.2049 0.2280 -0.5085 -0.2089 357 PHE B CE2 2498 C CZ . PHE A 326 ? 1.4545 0.7475 1.2132 0.2459 -0.5110 -0.2306 357 PHE B CZ 2499 N N . THR A 327 ? 1.4887 0.7619 1.3704 0.2858 -0.6378 -0.2732 358 THR B N 2500 C CA . THR A 327 ? 1.5110 0.7615 1.4105 0.2908 -0.6738 -0.2762 358 THR B CA 2501 C C . THR A 327 ? 1.5505 0.7406 1.4327 0.2848 -0.7133 -0.2625 358 THR B C 2502 O O . THR A 327 ? 1.5546 0.7320 1.4214 0.2797 -0.7133 -0.2550 358 THR B O 2503 C CB . THR A 327 ? 1.4982 0.7932 1.4610 0.3151 -0.6829 -0.3101 358 THR B CB 2504 O OG1 . THR A 327 ? 1.4694 0.8214 1.4505 0.3224 -0.6469 -0.3270 358 THR B OG1 2505 C CG2 . THR A 327 ? 1.5013 0.8060 1.4772 0.3151 -0.6902 -0.3118 358 THR B CG2 2506 N N . GLY A 328 ? 1.7285 0.8968 1.6122 0.2803 -0.7421 -0.2548 359 GLY B N 2507 C CA . GLY A 328 ? 1.7668 0.8978 1.6381 0.2699 -0.7776 -0.2400 359 GLY B CA 2508 C C . GLY A 328 ? 1.7935 0.8751 1.6011 0.2418 -0.7781 -0.2062 359 GLY B C 2509 O O . GLY A 328 ? 1.7803 0.8553 1.5526 0.2299 -0.7503 -0.1933 359 GLY B O 2510 N N . VAL A 329 ? 1.6508 0.6987 1.4436 0.2300 -0.8101 -0.1929 360 VAL B N 2511 C CA . VAL A 329 ? 1.6806 0.6831 1.4131 0.2013 -0.8130 -0.1619 360 VAL B CA 2512 C C . VAL A 329 ? 1.6674 0.6649 1.3660 0.1913 -0.7845 -0.1512 360 VAL B C 2513 O O . VAL A 329 ? 1.6463 0.6675 1.3683 0.2056 -0.7735 -0.1662 360 VAL B O 2514 C CB . VAL A 329 ? 1.7285 0.6982 1.4538 0.1905 -0.8547 -0.1527 360 VAL B CB 2515 C CG1 . VAL A 329 ? 1.7622 0.6938 1.4429 0.1650 -0.8678 -0.1283 360 VAL B CG1 2516 C CG2 . VAL A 329 ? 1.7341 0.7245 1.5189 0.2125 -0.8849 -0.1779 360 VAL B CG2 2517 N N . LEU A 330 ? 1.7711 0.7388 1.4147 0.1660 -0.7721 -0.1262 361 LEU B N 2518 C CA . LEU A 330 ? 1.7704 0.7254 1.3781 0.1521 -0.7534 -0.1134 361 LEU B CA 2519 C C . LEU A 330 ? 1.8069 0.7396 1.4125 0.1465 -0.7857 -0.1085 361 LEU B C 2520 O O . LEU A 330 ? 1.8391 0.7552 1.4515 0.1435 -0.8197 -0.1064 361 LEU B O 2521 C CB . LEU A 330 ? 1.7790 0.7083 1.3294 0.1245 -0.7344 -0.0889 361 LEU B CB 2522 C CG . LEU A 330 ? 1.7436 0.6915 1.2877 0.1261 -0.6982 -0.0915 361 LEU B CG 2523 C CD1 . LEU A 330 ? 1.7522 0.6761 1.2388 0.0977 -0.6769 -0.0685 361 LEU B CD1 2524 C CD2 . LEU A 330 ? 1.7037 0.6881 1.2791 0.1475 -0.6737 -0.1124 361 LEU B CD2 2525 N N . PRO A 331 ? 1.7276 0.6598 1.3246 0.1451 -0.7764 -0.1075 362 PRO B N 2526 C CA . PRO A 331 ? 1.7640 0.6720 1.3528 0.1370 -0.8056 -0.1009 362 PRO B CA 2527 C C . PRO A 331 ? 1.8067 0.6745 1.3487 0.1086 -0.8237 -0.0768 362 PRO B C 2528 O O . PRO A 331 ? 1.8061 0.6607 1.3043 0.0883 -0.8016 -0.0597 362 PRO B O 2529 C CB . PRO A 331 ? 1.7496 0.6593 1.3186 0.1321 -0.7810 -0.0967 362 PRO B CB 2530 C CG . PRO A 331 ? 1.7010 0.6486 1.2953 0.1506 -0.7473 -0.1133 362 PRO B CG 2531 C CD . PRO A 331 ? 1.6898 0.6442 1.2849 0.1510 -0.7388 -0.1133 362 PRO B CD 2532 N N . HIS A 332 ? 1.7739 0.6230 1.3247 0.1062 -0.8635 -0.0764 363 HIS B N 2533 C CA . HIS A 332 ? 1.8113 0.6280 1.3241 0.0815 -0.8808 -0.0572 363 HIS B CA 2534 C C . HIS A 332 ? 1.8441 0.6269 1.2993 0.0509 -0.8814 -0.0339 363 HIS B C 2535 O O . HIS A 332 ? 1.8643 0.6258 1.2772 0.0266 -0.8789 -0.0162 363 HIS B O 2536 C CB . HIS A 332 ? 1.8401 0.6494 1.3830 0.0888 -0.9228 -0.0660 363 HIS B CB 2537 C CG . HIS A 332 ? 1.8686 0.6671 1.4293 0.0932 -0.9561 -0.0726 363 HIS B CG 2538 N ND1 . HIS A 332 ? 1.9152 0.6763 1.4368 0.0689 -0.9795 -0.0551 363 HIS B ND1 2539 C CD2 . HIS A 332 ? 1.8583 0.6790 1.4721 0.1186 -0.9704 -0.0955 363 HIS B CD2 2540 C CE1 . HIS A 332 ? 1.9330 0.6918 1.4825 0.0794 -1.0078 -0.0662 363 HIS B CE1 2541 N NE2 . HIS A 332 ? 1.8989 0.6938 1.5049 0.1096 -1.0028 -0.0911 363 HIS B NE2 2542 N N . LYS A 333 ? 2.0033 0.7825 1.4558 0.0510 -0.8830 -0.0342 364 LYS B N 2543 C CA . LYS A 333 ? 2.0341 0.7830 1.4317 0.0214 -0.8821 -0.0129 364 LYS B CA 2544 C C . LYS A 333 ? 2.0041 0.7622 1.3720 0.0119 -0.8375 -0.0051 364 LYS B C 2545 O O . LYS A 333 ? 2.0212 0.7614 1.3484 -0.0097 -0.8299 0.0093 364 LYS B O 2546 C CB . LYS A 333 ? 2.0643 0.7974 1.4650 0.0203 -0.9102 -0.0134 364 LYS B CB 2547 C CG . LYS A 333 ? 2.1177 0.8107 1.4648 -0.0133 -0.9308 0.0085 364 LYS B CG 2548 C CD . LYS A 333 ? 2.1473 0.8243 1.4948 -0.0152 -0.9566 0.0087 364 LYS B CD 2549 C CE . LYS A 333 ? 2.1998 0.8384 1.4899 -0.0505 -0.9735 0.0308 364 LYS B CE 2550 N NZ . LYS A 333 ? 2.2292 0.8515 1.5184 -0.0527 -0.9986 0.0314 364 LYS B NZ 2551 N N . LEU A 334 ? 1.9316 0.7187 1.3219 0.0286 -0.8086 -0.0159 365 LEU B N 2552 C CA . LEU A 334 ? 1.8998 0.6986 1.2679 0.0222 -0.7658 -0.0115 365 LEU B CA 2553 C C . LEU A 334 ? 1.9232 0.6972 1.2320 -0.0119 -0.7543 0.0108 365 LEU B C 2554 O O . LEU A 334 ? 1.9482 0.7058 1.2373 -0.0268 -0.7679 0.0206 365 LEU B O 2555 C CB . LEU A 334 ? 1.8575 0.6862 1.2546 0.0414 -0.7429 -0.0249 365 LEU B CB 2556 C CG . LEU A 334 ? 1.8112 0.6672 1.2164 0.0522 -0.7027 -0.0339 365 LEU B CG 2557 C CD1 . LEU A 334 ? 1.7765 0.6626 1.2208 0.0755 -0.6921 -0.0513 365 LEU B CD1 2558 C CD2 . LEU A 334 ? 1.8095 0.6542 1.1656 0.0269 -0.6729 -0.0175 365 LEU B CD2 2559 N N . GLY A 335 ? 1.7888 0.5613 1.0701 -0.0246 -0.7291 0.0176 366 GLY B N 2560 C CA . GLY A 335 ? 1.8061 0.5610 1.0334 -0.0564 -0.7126 0.0358 366 GLY B CA 2561 C C . GLY A 335 ? 1.8545 0.5792 1.0461 -0.0808 -0.7360 0.0500 366 GLY B C 2562 O O . GLY A 335 ? 1.8703 0.5820 1.0166 -0.1082 -0.7213 0.0635 366 GLY B O 2563 N N . SER A 336 ? 1.9376 0.6522 1.1506 -0.0711 -0.7729 0.0457 367 SER B N 2564 C CA . SER A 336 ? 1.9883 0.6723 1.1703 -0.0929 -0.8015 0.0581 367 SER B CA 2565 C C . SER A 336 ? 1.9896 0.6699 1.1507 -0.1029 -0.7873 0.0629 367 SER B C 2566 O O . SER A 336 ? 2.0299 0.6854 1.1526 -0.1279 -0.8008 0.0762 367 SER B O 2567 C CB . SER A 336 ? 2.0102 0.6871 1.2271 -0.0765 -0.8442 0.0494 367 SER B CB 2568 O OG . SER A 336 ? 1.9772 0.6780 1.2414 -0.0463 -0.8401 0.0317 367 SER B OG 2569 N N . ASN A 337 ? 1.8978 0.6028 1.0837 -0.0839 -0.7604 0.0516 368 ASN B N 2570 C CA . ASN A 337 ? 1.8952 0.5987 1.0618 -0.0932 -0.7431 0.0555 368 ASN B CA 2571 C C . ASN A 337 ? 1.9041 0.5985 1.0190 -0.1246 -0.7171 0.0702 368 ASN B C 2572 O O . ASN A 337 ? 1.9107 0.5996 1.0008 -0.1393 -0.7045 0.0761 368 ASN B O 2573 C CB . ASN A 337 ? 1.8465 0.5797 1.0519 -0.0660 -0.7196 0.0390 368 ASN B CB 2574 C CG . ASN A 337 ? 1.8030 0.5611 1.0210 -0.0557 -0.6865 0.0315 368 ASN B CG 2575 O OD1 . ASN A 337 ? 1.7865 0.5502 0.9807 -0.0683 -0.6540 0.0361 368 ASN B OD1 2576 N ND2 . ASN A 337 ? 1.7847 0.5589 1.0416 -0.0326 -0.6948 0.0190 368 ASN B ND2 2577 N N . GLY A 338 ? 1.8940 0.5883 0.9941 -0.1348 -0.7088 0.0750 369 GLY B N 2578 C CA . GLY A 338 ? 1.9103 0.5945 0.9601 -0.1671 -0.6895 0.0886 369 GLY B CA 2579 C C . GLY A 338 ? 1.8754 0.5780 0.9163 -0.1709 -0.6460 0.0863 369 GLY B C 2580 O O . GLY A 338 ? 1.8848 0.5833 0.8872 -0.1969 -0.6261 0.0952 369 GLY B O 2581 N N . LYS A 339 ? 1.9995 0.7226 1.0757 -0.1459 -0.6318 0.0733 370 LYS B N 2582 C CA . LYS A 339 ? 1.9634 0.7058 1.0369 -0.1464 -0.5915 0.0687 370 LYS B CA 2583 C C . LYS A 339 ? 1.9201 0.6871 1.0213 -0.1270 -0.5694 0.0576 370 LYS B C 2584 O O . LYS A 339 ? 1.8878 0.6724 0.9910 -0.1247 -0.5365 0.0518 370 LYS B O 2585 C CB . LYS A 339 ? 1.9518 0.6999 1.0383 -0.1368 -0.5867 0.0627 370 LYS B CB 2586 C CG . LYS A 339 ? 1.9950 0.7187 1.0492 -0.1591 -0.6050 0.0746 370 LYS B CG 2587 C CD . LYS A 339 ? 1.9848 0.7137 1.0580 -0.1456 -0.6060 0.0676 370 LYS B CD 2588 C CE . LYS A 339 ? 1.9411 0.6941 1.0247 -0.1379 -0.5670 0.0584 370 LYS B CE 2589 N NZ . LYS A 339 ? 1.9244 0.6869 1.0336 -0.1199 -0.5670 0.0487 370 LYS B NZ 2590 N N . LEU A 340 ? 1.8879 0.6558 1.0105 -0.1134 -0.5883 0.0542 371 LEU B N 2591 C CA . LEU A 340 ? 1.8489 0.6401 1.0010 -0.0929 -0.5714 0.0427 371 LEU B CA 2592 C C . LEU A 340 ? 1.8386 0.6339 0.9632 -0.1109 -0.5413 0.0483 371 LEU B C 2593 O O . LEU A 340 ? 1.8668 0.6462 0.9587 -0.1343 -0.5465 0.0605 371 LEU B O 2594 C CB . LEU A 340 ? 1.8562 0.6464 1.0351 -0.0771 -0.5998 0.0384 371 LEU B CB 2595 C CG . LEU A 340 ? 1.8165 0.6320 1.0283 -0.0546 -0.5838 0.0251 371 LEU B CG 2596 C CD1 . LEU A 340 ? 1.7796 0.6198 1.0267 -0.0295 -0.5698 0.0086 371 LEU B CD1 2597 C CD2 . LEU A 340 ? 1.8270 0.6407 1.0633 -0.0415 -0.6123 0.0212 371 LEU B CD2 2598 N N . GLU A 341 ? 1.8844 0.7024 1.0235 -0.0996 -0.5103 0.0382 372 GLU B N 2599 C CA . GLU A 341 ? 1.8709 0.6957 0.9876 -0.1150 -0.4790 0.0410 372 GLU B CA 2600 C C . GLU A 341 ? 1.8418 0.6871 0.9830 -0.0981 -0.4694 0.0327 372 GLU B C 2601 O O . GLU A 341 ? 1.8523 0.6909 0.9763 -0.1108 -0.4685 0.0396 372 GLU B O 2602 C CB . GLU A 341 ? 1.8478 0.6855 0.9597 -0.1180 -0.4485 0.0358 372 GLU B CB 2603 C CG . GLU A 341 ? 1.8739 0.6966 0.9596 -0.1374 -0.4522 0.0441 372 GLU B CG 2604 C CD . GLU A 341 ? 1.8523 0.6881 0.9302 -0.1439 -0.4196 0.0391 372 GLU B CD 2605 O OE1 . GLU A 341 ? 1.8096 0.6858 0.9114 -0.1298 -0.3914 0.0299 372 GLU B OE1 2606 O OE2 . GLU A 341 ? 1.8714 0.6972 0.9277 -0.1607 -0.4190 0.0449 372 GLU B OE2 2607 N N . THR A 342 ? 1.7120 0.5949 0.8967 -0.0694 -0.4590 0.0179 373 THR B N 2608 C CA . THR A 342 ? 1.6793 0.5994 0.8926 -0.0524 -0.4434 0.0092 373 THR B CA 2609 C C . THR A 342 ? 1.6642 0.6017 0.9235 -0.0222 -0.4606 -0.0048 373 THR B C 2610 O O . THR A 342 ? 1.6535 0.6005 0.9351 -0.0066 -0.4640 -0.0142 373 THR B O 2611 C CB . THR A 342 ? 1.6501 0.6105 0.8706 -0.0498 -0.4029 0.0034 373 THR B CB 2612 O OG1 . THR A 342 ? 1.6274 0.6286 0.8885 -0.0246 -0.3918 -0.0095 373 THR B OG1 2613 C CG2 . THR A 342 ? 1.6459 0.6076 0.8645 -0.0501 -0.3943 0.0009 373 THR B CG2 2614 N N . MET A 343 ? 1.5725 0.5152 0.8464 -0.0143 -0.4711 -0.0070 374 MET B N 2615 C CA . MET A 343 ? 1.5559 0.5217 0.8764 0.0142 -0.4839 -0.0227 374 MET B CA 2616 C C . MET A 343 ? 1.5414 0.5451 0.8836 0.0247 -0.4656 -0.0295 374 MET B C 2617 O O . MET A 343 ? 1.5521 0.5460 0.8753 0.0115 -0.4651 -0.0205 374 MET B O 2618 C CB . MET A 343 ? 1.5904 0.5196 0.9153 0.0172 -0.5272 -0.0213 374 MET B CB 2619 C CG . MET A 343 ? 1.5744 0.5291 0.9455 0.0431 -0.5390 -0.0371 374 MET B CG 2620 S SD . MET A 343 ? 1.6140 0.5293 0.9994 0.0509 -0.5915 -0.0391 374 MET B SD 2621 C CE . MET A 343 ? 1.6538 0.5294 0.9922 0.0208 -0.6055 -0.0163 374 MET B CE 2622 N N . ASP A 344 ? 1.4374 0.4842 0.8179 0.0472 -0.4503 -0.0454 375 ASP B N 2623 C CA . ASP A 344 ? 1.4101 0.4925 0.8152 0.0589 -0.4378 -0.0535 375 ASP B CA 2624 C C . ASP A 344 ? 1.3961 0.5039 0.8490 0.0858 -0.4514 -0.0727 375 ASP B C 2625 O O . ASP A 344 ? 1.3744 0.5095 0.8502 0.0999 -0.4397 -0.0848 375 ASP B O 2626 C CB . ASP A 344 ? 1.3867 0.5034 0.7883 0.0560 -0.3986 -0.0537 375 ASP B CB 2627 C CG . ASP A 344 ? 1.3757 0.5270 0.7969 0.0643 -0.3840 -0.0597 375 ASP B CG 2628 O OD1 . ASP A 344 ? 1.3802 0.5355 0.8239 0.0755 -0.4026 -0.0667 375 ASP B OD1 2629 O OD2 . ASP A 344 ? 1.3627 0.5375 0.7777 0.0594 -0.3540 -0.0577 375 ASP B OD2 2630 N N . VAL A 345 ? 1.4095 0.5084 0.8773 0.0922 -0.4765 -0.0761 376 VAL B N 2631 C CA . VAL A 345 ? 1.3972 0.5216 0.9127 0.1171 -0.4907 -0.0961 376 VAL B CA 2632 C C . VAL A 345 ? 1.3707 0.5362 0.9123 0.1273 -0.4766 -0.1060 376 VAL B C 2633 O O . VAL A 345 ? 1.3656 0.5501 0.9459 0.1456 -0.4912 -0.1226 376 VAL B O 2634 C CB . VAL A 345 ? 1.4373 0.5243 0.9601 0.1211 -0.5333 -0.0973 376 VAL B CB 2635 C CG1 . VAL A 345 ? 1.4631 0.5149 0.9642 0.1129 -0.5457 -0.0897 376 VAL B CG1 2636 C CG2 . VAL A 345 ? 1.4663 0.5228 0.9661 0.1063 -0.5502 -0.0833 376 VAL B CG2 2637 N N . SER A 346 ? 1.4623 0.6401 0.9830 0.1146 -0.4499 -0.0962 377 SER B N 2638 C CA . SER A 346 ? 1.4595 0.6670 0.9957 0.1188 -0.4390 -0.1008 377 SER B CA 2639 C C . SER A 346 ? 1.4404 0.7003 1.0202 0.1397 -0.4258 -0.1217 377 SER B C 2640 O O . SER A 346 ? 1.4268 0.7052 1.0211 0.1492 -0.4166 -0.1314 377 SER B O 2641 C CB . SER A 346 ? 1.4610 0.6702 0.9642 0.1003 -0.4111 -0.0860 377 SER B CB 2642 O OG . SER A 346 ? 1.4441 0.6838 0.9502 0.1026 -0.3804 -0.0896 377 SER B OG 2643 N N . ASN A 347 ? 1.3367 0.6202 0.9366 0.1456 -0.4252 -0.1286 378 ASN B N 2644 C CA . ASN A 347 ? 1.3171 0.6530 0.9564 0.1624 -0.4111 -0.1483 378 ASN B CA 2645 C C . ASN A 347 ? 1.3093 0.6586 0.9897 0.1830 -0.4312 -0.1698 378 ASN B C 2646 O O . ASN A 347 ? 1.2868 0.6775 0.9953 0.1955 -0.4167 -0.1866 378 ASN B O 2647 C CB . ASN A 347 ? 1.3002 0.6664 0.9319 0.1592 -0.3752 -0.1471 378 ASN B CB 2648 C CG . ASN A 347 ? 1.2817 0.7015 0.9450 0.1702 -0.3569 -0.1630 378 ASN B CG 2649 O OD1 . ASN A 347 ? 1.2843 0.7183 0.9636 0.1736 -0.3625 -0.1687 378 ASN B OD1 2650 N ND2 . ASN A 347 ? 1.2634 0.7126 0.9342 0.1745 -0.3351 -0.1699 378 ASN B ND2 2651 N N . ASN A 348 ? 1.4121 0.7263 1.0962 0.1860 -0.4655 -0.1698 379 ASN B N 2652 C CA . ASN A 348 ? 1.4043 0.7269 1.1287 0.2058 -0.4882 -0.1910 379 ASN B CA 2653 C C . ASN A 348 ? 1.4115 0.7348 1.1662 0.2161 -0.5154 -0.2023 379 ASN B C 2654 O O . ASN A 348 ? 1.4220 0.7450 1.1684 0.2086 -0.5140 -0.1948 379 ASN B O 2655 C CB . ASN A 348 ? 1.4085 0.6896 1.1185 0.2039 -0.5088 -0.1850 379 ASN B CB 2656 C CG . ASN A 348 ? 1.3938 0.6884 1.0955 0.2036 -0.4853 -0.1856 379 ASN B CG 2657 O OD1 . ASN A 348 ? 1.3867 0.7014 1.1181 0.2191 -0.4882 -0.2036 379 ASN B OD1 2658 N ND2 . ASN A 348 ? 1.3885 0.6727 1.0506 0.1858 -0.4623 -0.1667 379 ASN B ND2 2659 N N . SER A 349 ? 1.3490 0.6769 1.1419 0.2342 -0.5393 -0.2223 380 SER B N 2660 C CA . SER A 349 ? 1.3559 0.6771 1.1801 0.2453 -0.5721 -0.2341 380 SER B CA 2661 C C . SER A 349 ? 1.3816 0.6433 1.1921 0.2417 -0.6123 -0.2235 380 SER B C 2662 O O . SER A 349 ? 1.4006 0.6539 1.2428 0.2541 -0.6449 -0.2362 380 SER B O 2663 C CB . SER A 349 ? 1.3351 0.7051 1.2172 0.2686 -0.5739 -0.2666 380 SER B CB 2664 O OG . SER A 349 ? 1.3269 0.7471 1.2227 0.2694 -0.5456 -0.2751 380 SER B OG 2665 N N . PHE A 350 ? 1.4557 0.6777 1.2215 0.2252 -0.6107 -0.2019 381 PHE B N 2666 C CA . PHE A 350 ? 1.4756 0.6383 1.2217 0.2181 -0.6477 -0.1893 381 PHE B CA 2667 C C . PHE A 350 ? 1.4983 0.6335 1.2453 0.2147 -0.6786 -0.1836 381 PHE B C 2668 O O . PHE A 350 ? 1.5001 0.6437 1.2330 0.2050 -0.6652 -0.1748 381 PHE B O 2669 C CB . PHE A 350 ? 1.4877 0.6151 1.1763 0.1938 -0.6347 -0.1627 381 PHE B CB 2670 C CG . PHE A 350 ? 1.4788 0.6032 1.1611 0.1953 -0.6265 -0.1641 381 PHE B CG 2671 C CD1 . PHE A 350 ? 1.4902 0.6020 1.1989 0.2100 -0.6543 -0.1774 381 PHE B CD1 2672 C CD2 . PHE A 350 ? 1.4684 0.6022 1.1193 0.1821 -0.5917 -0.1524 381 PHE B CD2 2673 C CE1 . PHE A 350 ? 1.4851 0.5938 1.1872 0.2109 -0.6466 -0.1784 381 PHE B CE1 2674 C CE2 . PHE A 350 ? 1.4592 0.5904 1.1043 0.1831 -0.5842 -0.1535 381 PHE B CE2 2675 C CZ . PHE A 350 ? 1.4668 0.5856 1.1366 0.1972 -0.6111 -0.1662 381 PHE B CZ 2676 N N . THR A 351 ? 1.6789 0.7805 1.4427 0.2227 -0.7209 -0.1887 382 THR B N 2677 C CA . THR A 351 ? 1.7078 0.7810 1.4741 0.2200 -0.7538 -0.1835 382 THR B CA 2678 C C . THR A 351 ? 1.7504 0.7733 1.4835 0.2015 -0.7848 -0.1616 382 THR B C 2679 O O . THR A 351 ? 1.7586 0.7665 1.4668 0.1916 -0.7808 -0.1513 382 THR B O 2680 C CB . THR A 351 ? 1.7027 0.8042 1.5330 0.2463 -0.7761 -0.2127 382 THR B CB 2681 O OG1 . THR A 351 ? 1.7127 0.8181 1.5700 0.2562 -0.7978 -0.2236 382 THR B OG1 2682 C CG2 . THR A 351 ? 1.6583 0.8294 1.5234 0.2601 -0.7399 -0.2342 382 THR B CG2 2683 N N . GLY A 352 ? 1.7422 0.7460 1.4756 0.1951 -0.8142 -0.1549 383 GLY B N 2684 C CA . GLY A 352 ? 1.7884 0.7530 1.4947 0.1763 -0.8458 -0.1370 383 GLY B CA 2685 C C . GLY A 352 ? 1.8129 0.7386 1.4540 0.1445 -0.8399 -0.1064 383 GLY B C 2686 O O . GLY A 352 ? 1.8043 0.7274 1.4240 0.1356 -0.8228 -0.0973 383 GLY B O 2687 N N . THR A 353 ? 1.7876 0.6837 1.3976 0.1266 -0.8552 -0.0916 384 THR B N 2688 C CA . THR A 353 ? 1.8165 0.6764 1.3645 0.0941 -0.8528 -0.0640 384 THR B CA 2689 C C . THR A 353 ? 1.8064 0.6609 1.3171 0.0811 -0.8238 -0.0524 384 THR B C 2690 O O . THR A 353 ? 1.7965 0.6612 1.3231 0.0919 -0.8211 -0.0612 384 THR B O 2691 C CB . THR A 353 ? 1.8685 0.6951 1.4029 0.0784 -0.8940 -0.0549 384 THR B CB 2692 O OG1 . THR A 353 ? 1.8798 0.7116 1.4551 0.0921 -0.9247 -0.0689 384 THR B OG1 2693 C CG2 . THR A 353 ? 1.9001 0.6923 1.3717 0.0435 -0.8924 -0.0285 384 THR B CG2 2694 N N . ILE A 354 ? 1.7794 0.6185 1.2411 0.0573 -0.8022 -0.0333 385 ILE B N 2695 C CA . ILE A 354 ? 1.7772 0.6068 1.1980 0.0397 -0.7774 -0.0203 385 ILE B CA 2696 C C . ILE A 354 ? 1.8195 0.6207 1.2168 0.0227 -0.8038 -0.0093 385 ILE B C 2697 O O . ILE A 354 ? 1.8583 0.6359 1.2426 0.0089 -0.8338 -0.0011 385 ILE B O 2698 C CB . ILE A 354 ? 1.7755 0.5951 1.1492 0.0157 -0.7504 -0.0033 385 ILE B CB 2699 C CG1 . ILE A 354 ? 1.7347 0.5807 1.1288 0.0310 -0.7235 -0.0137 385 ILE B CG1 2700 C CG2 . ILE A 354 ? 1.7760 0.5863 1.1084 -0.0039 -0.7262 0.0089 385 ILE B CG2 2701 C CD1 . ILE A 354 ? 1.7357 0.5719 1.0877 0.0083 -0.7013 0.0017 385 ILE B CD1 2702 N N . PRO A 355 ? 1.8668 0.6701 1.2595 0.0235 -0.7935 -0.0101 386 PRO B N 2703 C CA . PRO A 355 ? 1.9049 0.6818 1.2713 0.0061 -0.8141 0.0008 386 PRO B CA 2704 C C . PRO A 355 ? 1.9388 0.6863 1.2454 -0.0297 -0.8125 0.0235 386 PRO B C 2705 O O . PRO A 355 ? 1.9232 0.6737 1.1990 -0.0436 -0.7798 0.0323 386 PRO B O 2706 C CB . PRO A 355 ? 1.8791 0.6700 1.2487 0.0137 -0.7900 -0.0041 386 PRO B CB 2707 C CG . PRO A 355 ? 1.8327 0.6601 1.2513 0.0446 -0.7730 -0.0254 386 PRO B CG 2708 C CD . PRO A 355 ? 1.8216 0.6554 1.2408 0.0446 -0.7644 -0.0248 386 PRO B CD 2709 N N . SER A 356 ? 2.1896 0.9095 1.4809 -0.0449 -0.8483 0.0315 387 SER B N 2710 C CA . SER A 356 ? 2.2287 0.9199 1.4643 -0.0801 -0.8528 0.0512 387 SER B CA 2711 C C . SER A 356 ? 2.2344 0.9170 1.4284 -0.1008 -0.8319 0.0627 387 SER B C 2712 O O . SER A 356 ? 2.2509 0.9205 1.3976 -0.1291 -0.8181 0.0769 387 SER B O 2713 C CB . SER A 356 ? 2.2798 0.9437 1.5139 -0.0894 -0.8998 0.0543 387 SER B CB 2714 O OG . SER A 356 ? 2.2730 0.9481 1.5593 -0.0635 -0.9238 0.0382 387 SER B OG 2715 N N . SER A 357 ? 2.3227 1.0138 1.5358 -0.0865 -0.8297 0.0552 388 SER B N 2716 C CA . SER A 357 ? 2.3338 1.0145 1.5114 -0.1051 -0.8169 0.0650 388 SER B CA 2717 C C . SER A 357 ? 2.2919 0.9935 1.4625 -0.1029 -0.7712 0.0636 388 SER B C 2718 O O . SER A 357 ? 2.2961 0.9928 1.4441 -0.1146 -0.7593 0.0690 388 SER B O 2719 C CB . SER A 357 ? 2.3531 1.0250 1.5487 -0.0959 -0.8451 0.0601 388 SER B CB 2720 O OG . SER A 357 ? 2.3206 1.0171 1.5732 -0.0611 -0.8483 0.0407 388 SER B OG 2721 N N . LEU A 358 ? 1.9598 0.6845 1.1505 -0.0882 -0.7468 0.0557 389 LEU B N 2722 C CA . LEU A 358 ? 1.9182 0.6642 1.1085 -0.0831 -0.7052 0.0516 389 LEU B CA 2723 C C . LEU A 358 ? 1.9315 0.6656 1.0712 -0.1131 -0.6836 0.0655 389 LEU B C 2724 O O . LEU A 358 ? 1.9138 0.6563 1.0508 -0.1121 -0.6625 0.0632 389 LEU B O 2725 C CB . LEU A 358 ? 1.8849 0.6505 1.0894 -0.0728 -0.6831 0.0457 389 LEU B CB 2726 C CG . LEU A 358 ? 1.8579 0.6453 1.1168 -0.0397 -0.6921 0.0279 389 LEU B CG 2727 C CD1 . LEU A 358 ? 1.8274 0.6321 1.0920 -0.0343 -0.6669 0.0241 389 LEU B CD1 2728 C CD2 . LEU A 358 ? 1.8314 0.6382 1.1252 -0.0160 -0.6864 0.0128 389 LEU B CD2 2729 N N . CYS A 359 ? 1.9894 0.7047 1.0898 -0.1405 -0.6895 0.0789 390 CYS B N 2730 C CA . CYS A 359 ? 2.0051 0.7106 1.0564 -0.1714 -0.6694 0.0909 390 CYS B CA 2731 C C . CYS A 359 ? 2.0511 0.7315 1.0726 -0.1923 -0.6931 0.1007 390 CYS B C 2732 O O . CYS A 359 ? 2.0710 0.7419 1.0489 -0.2210 -0.6799 0.1107 390 CYS B O 2733 C CB . CYS A 359 ? 2.0112 0.7147 1.0331 -0.1918 -0.6552 0.0984 390 CYS B CB 2734 S SG . CYS A 359 ? 1.9856 0.7040 0.9794 -0.2084 -0.6057 0.1003 390 CYS B SG 2735 N N . HIS A 360 ? 2.3078 0.9787 1.3532 -0.1784 -0.7275 0.0969 391 HIS B N 2736 C CA . HIS A 360 ? 2.3588 1.0020 1.3780 -0.1977 -0.7590 0.1064 391 HIS B CA 2737 C C . HIS A 360 ? 2.3696 1.0071 1.3473 -0.2226 -0.7377 0.1153 391 HIS B C 2738 O O . HIS A 360 ? 2.4151 1.0294 1.3538 -0.2497 -0.7543 0.1264 391 HIS B O 2739 C CB . HIS A 360 ? 2.3606 1.0028 1.4205 -0.1725 -0.7884 0.0969 391 HIS B CB 2740 C CG . HIS A 360 ? 2.4148 1.0275 1.4569 -0.1876 -0.8289 0.1047 391 HIS B CG 2741 N ND1 . HIS A 360 ? 2.4396 1.0378 1.4528 -0.2048 -0.8319 0.1125 391 HIS B ND1 2742 C CD2 . HIS A 360 ? 2.4489 1.0441 1.5012 -0.1865 -0.8698 0.1046 391 HIS B CD2 2743 C CE1 . HIS A 360 ? 2.4878 1.0600 1.4916 -0.2148 -0.8726 0.1178 391 HIS B CE1 2744 N NE2 . HIS A 360 ? 2.4945 1.0641 1.5221 -0.2040 -0.8966 0.1129 391 HIS B NE2 2745 N N . GLY A 361 ? 1.9627 0.6219 0.9490 -0.2138 -0.7010 0.1095 392 GLY B N 2746 C CA . GLY A 361 ? 1.9664 0.6248 0.9172 -0.2360 -0.6758 0.1157 392 GLY B CA 2747 C C . GLY A 361 ? 1.9512 0.6208 0.8752 -0.2541 -0.6387 0.1185 392 GLY B C 2748 O O . GLY A 361 ? 1.9544 0.6252 0.8497 -0.2736 -0.6164 0.1224 392 GLY B O 2749 N N . ASN A 362 ? 1.9344 0.6133 0.8691 -0.2477 -0.6317 0.1158 393 ASN B N 2750 C CA . ASN A 362 ? 1.9227 0.6118 0.8321 -0.2657 -0.5987 0.1181 393 ASN B CA 2751 C C . ASN A 362 ? 1.8833 0.5939 0.7981 -0.2614 -0.5586 0.1116 393 ASN B C 2752 O O . ASN A 362 ? 1.8832 0.5990 0.7687 -0.2833 -0.5316 0.1144 393 ASN B O 2753 C CB . ASN A 362 ? 1.9698 0.6399 0.8260 -0.3041 -0.6040 0.1300 393 ASN B CB 2754 C CG . ASN A 362 ? 1.9930 0.6526 0.8376 -0.3143 -0.6215 0.1345 393 ASN B CG 2755 O OD1 . ASN A 362 ? 1.9964 0.6598 0.8143 -0.3346 -0.6021 0.1371 393 ASN B OD1 2756 N ND2 . ASN A 362 ? 2.0093 0.6561 0.8752 -0.3003 -0.6583 0.1344 393 ASN B ND2 2757 N N . LYS A 363 ? 1.8870 0.6103 0.8392 -0.2339 -0.5553 0.1018 394 LYS B N 2758 C CA . LYS A 363 ? 1.8469 0.5915 0.8101 -0.2262 -0.5191 0.0935 394 LYS B CA 2759 C C . LYS A 363 ? 1.8026 0.5693 0.8005 -0.2016 -0.5020 0.0824 394 LYS B C 2760 O O . LYS A 363 ? 1.7686 0.5538 0.7763 -0.1949 -0.4719 0.0745 394 LYS B O 2761 C CB . LYS A 363 ? 1.8410 0.5864 0.8194 -0.2146 -0.5233 0.0891 394 LYS B CB 2762 C CG . LYS A 363 ? 1.8799 0.6069 0.8199 -0.2419 -0.5305 0.0995 394 LYS B CG 2763 C CD . LYS A 363 ? 1.8607 0.5981 0.8036 -0.2406 -0.5082 0.0944 394 LYS B CD 2764 C CE . LYS A 363 ? 1.8609 0.5941 0.8301 -0.2204 -0.5303 0.0902 394 LYS B CE 2765 N NZ . LYS A 363 ? 1.9107 0.6173 0.8595 -0.2339 -0.5670 0.1009 394 LYS B NZ 2766 N N . LEU A 364 ? 1.7885 0.5530 0.8037 -0.1893 -0.5217 0.0816 395 LEU B N 2767 C CA . LEU A 364 ? 1.7496 0.5343 0.8004 -0.1640 -0.5107 0.0704 395 LEU B CA 2768 C C . LEU A 364 ? 1.7367 0.5301 0.7710 -0.1763 -0.4840 0.0722 395 LEU B C 2769 O O . LEU A 364 ? 1.7637 0.5445 0.7702 -0.1969 -0.4911 0.0819 395 LEU B O 2770 C CB . LEU A 364 ? 1.7587 0.5384 0.8381 -0.1448 -0.5449 0.0675 395 LEU B CB 2771 C CG . LEU A 364 ? 1.7249 0.5240 0.8478 -0.1148 -0.5442 0.0544 395 LEU B CG 2772 C CD1 . LEU A 364 ? 1.7386 0.5323 0.8925 -0.0959 -0.5815 0.0494 395 LEU B CD1 2773 C CD2 . LEU A 364 ? 1.7202 0.5223 0.8335 -0.1220 -0.5337 0.0575 395 LEU B CD2 2774 N N . TYR A 365 ? 1.8625 0.6775 0.9141 -0.1638 -0.4544 0.0620 396 TYR B N 2775 C CA . TYR A 365 ? 1.8438 0.6757 0.8867 -0.1721 -0.4267 0.0615 396 TYR B CA 2776 C C . TYR A 365 ? 1.8061 0.6734 0.8895 -0.1454 -0.4191 0.0514 396 TYR B C 2777 O O . TYR A 365 ? 1.8124 0.6768 0.8891 -0.1508 -0.4220 0.0554 396 TYR B O 2778 C CB . TYR A 365 ? 1.8244 0.6774 0.8540 -0.1849 -0.3900 0.0589 396 TYR B CB 2779 C CG . TYR A 365 ? 1.7815 0.6720 0.8472 -0.1610 -0.3691 0.0460 396 TYR B CG 2780 C CD1 . TYR A 365 ? 1.7856 0.6680 0.8570 -0.1552 -0.3783 0.0438 396 TYR B CD1 2781 C CD2 . TYR A 365 ? 1.7466 0.6794 0.8392 -0.1455 -0.3409 0.0365 396 TYR B CD2 2782 C CE1 . TYR A 365 ? 1.7512 0.6671 0.8538 -0.1346 -0.3597 0.0324 396 TYR B CE1 2783 C CE2 . TYR A 365 ? 1.7219 0.6873 0.8453 -0.1253 -0.3231 0.0256 396 TYR B CE2 2784 C CZ . TYR A 365 ? 1.7217 0.6787 0.8497 -0.1201 -0.3324 0.0236 396 TYR B CZ 2785 O OH . TYR A 365 ? 1.6981 0.6868 0.8553 -0.1011 -0.3153 0.0130 396 TYR B OH 2786 N N . LYS A 366 ? 1.8048 0.7067 0.9283 -0.1184 -0.4074 0.0385 397 LYS B N 2787 C CA . LYS A 366 ? 1.7797 0.7176 0.9416 -0.0940 -0.3989 0.0281 397 LYS B CA 2788 C C . LYS A 366 ? 1.7798 0.7124 0.9724 -0.0721 -0.4304 0.0222 397 LYS B C 2789 O O . LYS A 366 ? 1.7725 0.7072 0.9864 -0.0567 -0.4412 0.0149 397 LYS B O 2790 C CB . LYS A 366 ? 1.7517 0.7333 0.9392 -0.0788 -0.3663 0.0170 397 LYS B CB 2791 C CG . LYS A 366 ? 1.7318 0.7532 0.9569 -0.0557 -0.3546 0.0064 397 LYS B CG 2792 C CD . LYS A 366 ? 1.7075 0.7679 0.9464 -0.0491 -0.3190 -0.0008 397 LYS B CD 2793 C CE . LYS A 366 ? 1.6985 0.7682 0.9508 -0.0390 -0.3143 -0.0074 397 LYS B CE 2794 N NZ . LYS A 366 ? 1.6705 0.7770 0.9367 -0.0326 -0.2818 -0.0139 397 LYS B NZ 2795 N N . LEU A 367 ? 1.5559 0.4817 0.7516 -0.0711 -0.4456 0.0246 398 LEU B N 2796 C CA . LEU A 367 ? 1.5582 0.4842 0.7881 -0.0490 -0.4741 0.0165 398 LEU B CA 2797 C C . LEU A 367 ? 1.5231 0.4873 0.7860 -0.0309 -0.4626 0.0066 398 LEU B C 2798 O O . LEU A 367 ? 1.5284 0.4900 0.7784 -0.0409 -0.4600 0.0127 398 LEU B O 2799 C CB . LEU A 367 ? 1.6109 0.4879 0.8184 -0.0624 -0.5128 0.0278 398 LEU B CB 2800 C CG . LEU A 367 ? 1.6169 0.4919 0.8603 -0.0407 -0.5448 0.0192 398 LEU B CG 2801 C CD1 . LEU A 367 ? 1.5888 0.4913 0.8764 -0.0126 -0.5451 0.0020 398 LEU B CD1 2802 C CD2 . LEU A 367 ? 1.6699 0.4990 0.8919 -0.0545 -0.5840 0.0308 398 LEU B CD2 2803 N N . ILE A 368 ? 1.5213 0.5210 0.8262 -0.0050 -0.4560 -0.0091 399 ILE B N 2804 C CA . ILE A 368 ? 1.5065 0.5451 0.8450 0.0126 -0.4453 -0.0200 399 ILE B CA 2805 C C . ILE A 368 ? 1.5087 0.5512 0.8862 0.0351 -0.4742 -0.0328 399 ILE B C 2806 O O . ILE A 368 ? 1.4989 0.5584 0.9051 0.0531 -0.4764 -0.0456 399 ILE B O 2807 C CB . ILE A 368 ? 1.4837 0.5673 0.8400 0.0230 -0.4096 -0.0293 399 ILE B CB 2808 C CG1 . ILE A 368 ? 1.4804 0.5551 0.8049 0.0052 -0.3880 -0.0204 399 ILE B CG1 2809 C CG2 . ILE A 368 ? 1.4664 0.5818 0.8344 0.0267 -0.3899 -0.0323 399 ILE B CG2 2810 C CD1 . ILE A 368 ? 1.5050 0.5696 0.7952 -0.0176 -0.3724 -0.0083 399 ILE B CD1 2811 N N . LEU A 369 ? 1.5536 0.5812 0.9329 0.0339 -0.4963 -0.0302 400 LEU B N 2812 C CA . LEU A 369 ? 1.5558 0.5871 0.9739 0.0547 -0.5250 -0.0432 400 LEU B CA 2813 C C . LEU A 369 ? 1.5434 0.6195 0.9978 0.0716 -0.5126 -0.0568 400 LEU B C 2814 O O . LEU A 369 ? 1.5451 0.6291 1.0343 0.0885 -0.5347 -0.0693 400 LEU B O 2815 C CB . LEU A 369 ? 1.5833 0.5645 0.9827 0.0435 -0.5642 -0.0323 400 LEU B CB 2816 C CG . LEU A 369 ? 1.6075 0.5442 0.9783 0.0302 -0.5835 -0.0219 400 LEU B CG 2817 C CD1 . LEU A 369 ? 1.6543 0.5403 0.9846 0.0060 -0.6085 -0.0033 400 LEU B CD1 2818 C CD2 . LEU A 369 ? 1.6118 0.5451 1.0172 0.0511 -0.6098 -0.0355 400 LEU B CD2 2819 N N . PHE A 370 ? 1.4284 0.5335 0.8750 0.0662 -0.4781 -0.0547 401 PHE B N 2820 C CA . PHE A 370 ? 1.4128 0.5511 0.8810 0.0741 -0.4675 -0.0616 401 PHE B CA 2821 C C . PHE A 370 ? 1.3888 0.5723 0.9076 0.0994 -0.4649 -0.0833 401 PHE B C 2822 O O . PHE A 370 ? 1.3746 0.5752 0.9136 0.1122 -0.4606 -0.0947 401 PHE B O 2823 C CB . PHE A 370 ? 1.4005 0.5518 0.8430 0.0588 -0.4346 -0.0515 401 PHE B CB 2824 C CG . PHE A 370 ? 1.3749 0.5613 0.8239 0.0634 -0.4006 -0.0569 401 PHE B CG 2825 C CD1 . PHE A 370 ? 1.3571 0.5889 0.8441 0.0826 -0.3880 -0.0730 401 PHE B CD1 2826 C CD2 . PHE A 370 ? 1.3702 0.5452 0.7863 0.0468 -0.3805 -0.0457 401 PHE B CD2 2827 C CE1 . PHE A 370 ? 1.3360 0.5977 0.8264 0.0850 -0.3580 -0.0765 401 PHE B CE1 2828 C CE2 . PHE A 370 ? 1.3484 0.5541 0.7706 0.0506 -0.3506 -0.0501 401 PHE B CE2 2829 C CZ . PHE A 370 ? 1.3316 0.5794 0.7901 0.0695 -0.3401 -0.0647 401 PHE B CZ 2830 N N . SER A 371 ? 1.4836 0.6869 1.0216 0.1053 -0.4668 -0.0891 402 SER B N 2831 C CA . SER A 371 ? 1.4691 0.7189 1.0543 0.1269 -0.4624 -0.1103 402 SER B CA 2832 C C . SER A 371 ? 1.4647 0.7124 1.0836 0.1452 -0.4891 -0.1265 402 SER B C 2833 O O . SER A 371 ? 1.4474 0.7255 1.0920 0.1591 -0.4785 -0.1415 402 SER B O 2834 C CB . SER A 371 ? 1.4508 0.7434 1.0413 0.1295 -0.4246 -0.1154 402 SER B CB 2835 O OG . SER A 371 ? 1.4524 0.7557 1.0244 0.1173 -0.4023 -0.1056 402 SER B OG 2836 N N . ASN A 372 ? 1.5474 0.7575 1.1649 0.1442 -0.5247 -0.1229 403 ASN B N 2837 C CA . ASN A 372 ? 1.5456 0.7483 1.1955 0.1613 -0.5549 -0.1379 403 ASN B CA 2838 C C . ASN A 372 ? 1.5584 0.7534 1.2346 0.1700 -0.5872 -0.1458 403 ASN B C 2839 O O . ASN A 372 ? 1.5698 0.7692 1.2405 0.1636 -0.5842 -0.1404 403 ASN B O 2840 C CB . ASN A 372 ? 1.5528 0.7082 1.1741 0.1517 -0.5722 -0.1256 403 ASN B CB 2841 C CG . ASN A 372 ? 1.5359 0.7078 1.1570 0.1556 -0.5505 -0.1302 403 ASN B CG 2842 O OD1 . ASN A 372 ? 1.5260 0.7200 1.1834 0.1745 -0.5555 -0.1493 403 ASN B OD1 2843 N ND2 . ASN A 372 ? 1.5324 0.6935 1.1132 0.1375 -0.5270 -0.1136 403 ASN B ND2 2844 N N . MET A 373 ? 1.7058 0.8913 1.4133 0.1858 -0.6180 -0.1600 404 MET B N 2845 C CA . MET A 373 ? 1.7166 0.8904 1.4522 0.1954 -0.6540 -0.1686 404 MET B CA 2846 C C . MET A 373 ? 1.7396 0.8490 1.4473 0.1831 -0.6928 -0.1512 404 MET B C 2847 O O . MET A 373 ? 1.7522 0.8455 1.4853 0.1926 -0.7289 -0.1590 404 MET B O 2848 C CB . MET A 373 ? 1.6996 0.9103 1.4958 0.2224 -0.6646 -0.1993 404 MET B CB 2849 C CG . MET A 373 ? 1.6862 0.9591 1.5155 0.2331 -0.6371 -0.2175 404 MET B CG 2850 S SD . MET A 373 ? 1.7022 0.9784 1.5431 0.2315 -0.6508 -0.2172 404 MET B SD 2851 C CE . MET A 373 ? 1.7033 0.9741 1.4884 0.2055 -0.6167 -0.1896 404 MET B CE 2852 N N . PHE A 374 ? 1.5887 0.6619 1.2456 0.1619 -0.6861 -0.1288 405 PHE B N 2853 C CA . PHE A 374 ? 1.6312 0.6414 1.2541 0.1461 -0.7205 -0.1102 405 PHE B CA 2854 C C . PHE A 374 ? 1.6581 0.6445 1.2783 0.1401 -0.7480 -0.1031 405 PHE B C 2855 O O . PHE A 374 ? 1.6455 0.6478 1.2539 0.1317 -0.7288 -0.0971 405 PHE B O 2856 C CB . PHE A 374 ? 1.6388 0.6229 1.2022 0.1192 -0.6993 -0.0860 405 PHE B CB 2857 C CG . PHE A 374 ? 1.6207 0.6167 1.1794 0.1214 -0.6775 -0.0890 405 PHE B CG 2858 C CD1 . PHE A 374 ? 1.6268 0.6175 1.2117 0.1370 -0.6974 -0.1018 405 PHE B CD1 2859 C CD2 . PHE A 374 ? 1.5984 0.6101 1.1268 0.1076 -0.6380 -0.0792 405 PHE B CD2 2860 C CE1 . PHE A 374 ? 1.6104 0.6118 1.1903 0.1385 -0.6773 -0.1043 405 PHE B CE1 2861 C CE2 . PHE A 374 ? 1.5820 0.6045 1.1067 0.1094 -0.6185 -0.0819 405 PHE B CE2 2862 C CZ . PHE A 374 ? 1.5881 0.6053 1.1377 0.1246 -0.6381 -0.0940 405 PHE B CZ 2863 N N . GLU A 375 ? 1.7760 0.7258 1.4073 0.1441 -0.7928 -0.1038 406 GLU B N 2864 C CA . GLU A 375 ? 1.8043 0.7351 1.4304 0.1348 -0.8193 -0.0950 406 GLU B CA 2865 C C . GLU A 375 ? 1.8502 0.7396 1.4303 0.1065 -0.8406 -0.0716 406 GLU B C 2866 O O . GLU A 375 ? 1.8578 0.7337 1.4079 0.0937 -0.8321 -0.0610 406 GLU B O 2867 C CB . GLU A 375 ? 1.8042 0.7570 1.4917 0.1594 -0.8480 -0.1189 406 GLU B CB 2868 C CG . GLU A 375 ? 1.8069 0.7732 1.5334 0.1762 -0.8664 -0.1370 406 GLU B CG 2869 C CD . GLU A 375 ? 1.8188 0.7992 1.6005 0.1942 -0.9011 -0.1584 406 GLU B CD 2870 O OE1 . GLU A 375 ? 1.8401 0.8058 1.6193 0.1868 -0.9205 -0.1530 406 GLU B OE1 2871 O OE2 . GLU A 375 ? 1.8074 0.8142 1.6354 0.2150 -0.9086 -0.1817 406 GLU B OE2 2872 N N . GLY A 376 ? 2.0612 0.9307 1.6345 0.0955 -0.8675 -0.0642 407 GLY B N 2873 C CA . GLY A 376 ? 2.1087 0.9393 1.6414 0.0681 -0.8912 -0.0455 407 GLY B CA 2874 C C . GLY A 376 ? 2.1192 0.9274 1.5876 0.0370 -0.8689 -0.0205 407 GLY B C 2875 O O . GLY A 376 ? 2.0886 0.9104 1.5431 0.0366 -0.8337 -0.0171 407 GLY B O 2876 N N . GLU A 377 ? 1.9645 0.7387 1.3942 0.0100 -0.8895 -0.0045 408 GLU B N 2877 C CA . GLU A 377 ? 1.9807 0.7337 1.3493 -0.0225 -0.8718 0.0176 408 GLU B CA 2878 C C . GLU A 377 ? 1.9631 0.7204 1.3036 -0.0301 -0.8396 0.0246 408 GLU B C 2879 O O . GLU A 377 ? 1.9413 0.7149 1.3079 -0.0112 -0.8332 0.0134 408 GLU B O 2880 C CB . GLU A 377 ? 2.0366 0.7530 1.3744 -0.0495 -0.9052 0.0299 408 GLU B CB 2881 C CG . GLU A 377 ? 2.0583 0.7552 1.3454 -0.0808 -0.8965 0.0477 408 GLU B CG 2882 C CD . GLU A 377 ? 2.1142 0.7765 1.3829 -0.1032 -0.9353 0.0549 408 GLU B CD 2883 O OE1 . GLU A 377 ? 2.1430 0.7891 1.4160 -0.1052 -0.9632 0.0532 408 GLU B OE1 2884 O OE2 . GLU A 377 ? 2.1303 0.7809 1.3805 -0.1191 -0.9385 0.0620 408 GLU B OE2 2885 N N . LEU A 378 ? 1.8607 0.6039 1.1486 -0.0585 -0.8193 0.0420 409 LEU B N 2886 C CA . LEU A 378 ? 1.8439 0.5916 1.1029 -0.0684 -0.7857 0.0486 409 LEU B CA 2887 C C . LEU A 378 ? 1.8843 0.6054 1.1055 -0.0936 -0.8003 0.0606 409 LEU B C 2888 O O . LEU A 378 ? 1.9225 0.6200 1.1116 -0.1185 -0.8167 0.0719 409 LEU B O 2889 C CB . LEU A 378 ? 1.8276 0.5805 1.0552 -0.0836 -0.7516 0.0577 409 LEU B CB 2890 C CG . LEU A 378 ? 1.8134 0.5695 1.0049 -0.0998 -0.7142 0.0656 409 LEU B CG 2891 C CD1 . LEU A 378 ? 1.7692 0.5507 0.9901 -0.0756 -0.6893 0.0529 409 LEU B CD1 2892 C CD2 . LEU A 378 ? 1.8110 0.5666 0.9689 -0.1202 -0.6905 0.0754 409 LEU B CD2 2893 N N . PRO A 379 ? 1.9414 0.6658 1.1657 -0.0881 -0.7947 0.0577 410 PRO B N 2894 C CA . PRO A 379 ? 1.9820 0.6812 1.1766 -0.1088 -0.8140 0.0673 410 PRO B CA 2895 C C . PRO A 379 ? 2.0110 0.6900 1.1465 -0.1461 -0.8043 0.0846 410 PRO B C 2896 O O . PRO A 379 ? 1.9898 0.6790 1.1013 -0.1563 -0.7681 0.0894 410 PRO B O 2897 C CB . PRO A 379 ? 1.9571 0.6696 1.1598 -0.0978 -0.7943 0.0622 410 PRO B CB 2898 C CG . PRO A 379 ? 1.9137 0.6555 1.1685 -0.0636 -0.7850 0.0446 410 PRO B CG 2899 C CD . PRO A 379 ? 1.8973 0.6489 1.1554 -0.0617 -0.7727 0.0443 410 PRO B CD 2900 N N . LYS A 380 ? 1.9973 0.6484 1.1107 -0.1666 -0.8368 0.0925 411 LYS B N 2901 C CA . LYS A 380 ? 2.0296 0.6615 1.0875 -0.2034 -0.8308 0.1072 411 LYS B CA 2902 C C . LYS A 380 ? 2.0296 0.6608 1.0556 -0.2186 -0.8085 0.1134 411 LYS B C 2903 O O . LYS A 380 ? 2.0284 0.6611 1.0163 -0.2410 -0.7801 0.1208 411 LYS B O 2904 C CB . LYS A 380 ? 2.0849 0.6859 1.1289 -0.2213 -0.8737 0.1128 411 LYS B CB 2905 C CG . LYS A 380 ? 2.0867 0.6875 1.1587 -0.2101 -0.8936 0.1071 411 LYS B CG 2906 C CD . LYS A 380 ? 2.1442 0.7119 1.2000 -0.2309 -0.9357 0.1128 411 LYS B CD 2907 C CE . LYS A 380 ? 2.1440 0.7119 1.2244 -0.2224 -0.9503 0.1077 411 LYS B CE 2908 N NZ . LYS A 380 ? 2.1988 0.7341 1.2715 -0.2394 -0.9937 0.1110 411 LYS B NZ 2909 N N . SER A 381 ? 2.0266 0.6582 1.0721 -0.2044 -0.8196 0.1084 412 SER B N 2910 C CA . SER A 381 ? 2.0274 0.6578 1.0466 -0.2167 -0.8013 0.1134 412 SER B CA 2911 C C . SER A 381 ? 1.9849 0.6386 0.9963 -0.2159 -0.7538 0.1123 412 SER B C 2912 O O . SER A 381 ? 1.9893 0.6412 0.9669 -0.2356 -0.7328 0.1185 412 SER B O 2913 C CB . SER A 381 ? 2.0235 0.6555 1.0740 -0.1956 -0.8182 0.1057 412 SER B CB 2914 O OG . SER A 381 ? 1.9722 0.6328 1.0649 -0.1642 -0.7968 0.0928 412 SER B OG 2915 N N . LEU A 382 ? 2.0555 0.7311 1.0984 -0.1938 -0.7375 0.1038 413 LEU B N 2916 C CA . LEU A 382 ? 2.0135 0.7118 1.0544 -0.1900 -0.6940 0.1011 413 LEU B CA 2917 C C . LEU A 382 ? 2.0237 0.7182 1.0182 -0.2210 -0.6700 0.1108 413 LEU B C 2918 O O . LEU A 382 ? 1.9970 0.7065 0.9811 -0.2248 -0.6340 0.1099 413 LEU B O 2919 C CB . LEU A 382 ? 1.9697 0.6921 1.0564 -0.1585 -0.6837 0.0886 413 LEU B CB 2920 C CG . LEU A 382 ? 1.9312 0.6743 1.0520 -0.1323 -0.6682 0.0765 413 LEU B CG 2921 C CD1 . LEU A 382 ? 1.8921 0.6589 1.0578 -0.1024 -0.6607 0.0628 413 LEU B CD1 2922 C CD2 . LEU A 382 ? 1.9153 0.6652 1.0089 -0.1461 -0.6316 0.0802 413 LEU B CD2 2923 N N . THR A 383 ? 2.0534 0.7283 1.0209 -0.2435 -0.6900 0.1189 414 THR B N 2924 C CA . THR A 383 ? 2.0667 0.7384 0.9898 -0.2746 -0.6686 0.1266 414 THR B CA 2925 C C . THR A 383 ? 2.0970 0.7553 0.9796 -0.3020 -0.6660 0.1335 414 THR B C 2926 O O . THR A 383 ? 2.1097 0.7667 0.9536 -0.3300 -0.6462 0.1381 414 THR B O 2927 C CB . THR A 383 ? 2.0981 0.7543 1.0071 -0.2897 -0.6900 0.1315 414 THR B CB 2928 O OG1 . THR A 383 ? 2.1369 0.7701 1.0506 -0.2904 -0.7332 0.1338 414 THR B OG1 2929 C CG2 . THR A 383 ? 2.0668 0.7387 1.0075 -0.2685 -0.6841 0.1256 414 THR B CG2 2930 N N . ARG A 384 ? 2.1687 0.8177 1.0616 -0.2938 -0.6868 0.1331 415 ARG B N 2931 C CA . ARG A 384 ? 2.1985 0.8340 1.0564 -0.3171 -0.6881 0.1395 415 ARG B CA 2932 C C . ARG A 384 ? 2.1642 0.8180 1.0282 -0.3086 -0.6560 0.1352 415 ARG B C 2933 O O . ARG A 384 ? 2.1834 0.8290 1.0234 -0.3242 -0.6547 0.1392 415 ARG B O 2934 C CB . ARG A 384 ? 2.2371 0.8492 1.0998 -0.3157 -0.7318 0.1424 415 ARG B CB 2935 C CG . ARG A 384 ? 2.2641 0.8600 1.1376 -0.3137 -0.7686 0.1433 415 ARG B CG 2936 C CD . ARG A 384 ? 2.3143 0.8820 1.1782 -0.3235 -0.8113 0.1482 415 ARG B CD 2937 N NE . ARG A 384 ? 2.3018 0.8729 1.2010 -0.2977 -0.8252 0.1419 415 ARG B NE 2938 C CZ . ARG A 384 ? 2.3134 0.8759 1.2476 -0.2784 -0.8620 0.1364 415 ARG B CZ 2939 N NH1 . ARG A 384 ? 2.3378 0.8868 1.2764 -0.2821 -0.8893 0.1370 415 ARG B NH1 2940 N NH2 . ARG A 384 ? 2.3010 0.8688 1.2669 -0.2558 -0.8717 0.1294 415 ARG B NH2 2941 N N . CYS A 385 ? 1.9798 0.6576 0.8756 -0.2844 -0.6308 0.1267 416 CYS B N 2942 C CA . CYS A 385 ? 1.9465 0.6412 0.8523 -0.2743 -0.6022 0.1214 416 CYS B CA 2943 C C . CYS A 385 ? 1.9365 0.6422 0.8115 -0.2963 -0.5638 0.1229 416 CYS B C 2944 O O . CYS A 385 ? 1.9118 0.6318 0.7928 -0.2926 -0.5428 0.1196 416 CYS B O 2945 C CB . CYS A 385 ? 1.8998 0.6150 0.8563 -0.2375 -0.5951 0.1099 416 CYS B CB 2946 S SG . CYS A 385 ? 1.8596 0.5942 0.8368 -0.2202 -0.5670 0.1010 416 CYS B SG 2947 N N . GLU A 386 ? 2.0692 0.7691 0.9124 -0.3187 -0.5543 0.1270 417 GLU B N 2948 C CA . GLU A 386 ? 2.0645 0.7749 0.8773 -0.3423 -0.5191 0.1271 417 GLU B CA 2949 C C . GLU A 386 ? 2.0132 0.7491 0.8514 -0.3239 -0.4838 0.1181 417 GLU B C 2950 O O . GLU A 386 ? 1.9954 0.7451 0.8279 -0.3303 -0.4572 0.1151 417 GLU B O 2951 C CB . GLU A 386 ? 2.0943 0.7949 0.8721 -0.3677 -0.5171 0.1318 417 GLU B CB 2952 C CG . GLU A 386 ? 2.1427 0.8268 0.8746 -0.4034 -0.5275 0.1389 417 GLU B CG 2953 C CD . GLU A 386 ? 2.1714 0.8362 0.9061 -0.4016 -0.5654 0.1438 417 GLU B CD 2954 O OE1 . GLU A 386 ? 2.1873 0.8372 0.9362 -0.3894 -0.5974 0.1466 417 GLU B OE1 2955 O OE2 . GLU A 386 ? 2.1779 0.8427 0.9023 -0.4121 -0.5633 0.1441 417 GLU B OE2 2956 N N . SER A 387 ? 1.8749 0.6167 0.7421 -0.3011 -0.4846 0.1129 418 SER B N 2957 C CA . SER A 387 ? 1.8297 0.5937 0.7197 -0.2851 -0.4527 0.1034 418 SER B CA 2958 C C . SER A 387 ? 1.7932 0.5733 0.7142 -0.2626 -0.4422 0.0961 418 SER B C 2959 O O . SER A 387 ? 1.7573 0.5564 0.6926 -0.2535 -0.4128 0.0878 418 SER B O 2960 C CB . SER A 387 ? 1.8188 0.5833 0.7321 -0.2666 -0.4608 0.0990 418 SER B CB 2961 O OG . SER A 387 ? 1.8554 0.5987 0.7629 -0.2691 -0.4974 0.1057 418 SER B OG 2962 N N . LEU A 388 ? 1.7958 0.5683 0.7271 -0.2545 -0.4665 0.0986 419 LEU B N 2963 C CA . LEU A 388 ? 1.7627 0.5499 0.7264 -0.2309 -0.4605 0.0915 419 LEU B CA 2964 C C . LEU A 388 ? 1.7409 0.5434 0.6939 -0.2404 -0.4254 0.0890 419 LEU B C 2965 O O . LEU A 388 ? 1.7614 0.5591 0.6810 -0.2666 -0.4172 0.0952 419 LEU B O 2966 C CB . LEU A 388 ? 1.7809 0.5570 0.7547 -0.2239 -0.4924 0.0948 419 LEU B CB 2967 C CG . LEU A 388 ? 1.7476 0.5387 0.7617 -0.1949 -0.4920 0.0858 419 LEU B CG 2968 C CD1 . LEU A 388 ? 1.7260 0.5257 0.7817 -0.1644 -0.5025 0.0750 419 LEU B CD1 2969 C CD2 . LEU A 388 ? 1.7680 0.5489 0.7828 -0.1961 -0.5169 0.0903 419 LEU B CD2 2970 N N . TRP A 389 ? 1.6908 0.5185 0.6758 -0.2179 -0.4041 0.0779 420 TRP B N 2971 C CA . TRP A 389 ? 1.6566 0.5192 0.6457 -0.2196 -0.3664 0.0714 420 TRP B CA 2972 C C . TRP A 389 ? 1.6207 0.5180 0.6509 -0.1919 -0.3585 0.0624 420 TRP B C 2973 O O . TRP A 389 ? 1.6157 0.5238 0.6420 -0.1970 -0.3463 0.0629 420 TRP B O 2974 C CB . TRP A 389 ? 1.6366 0.5183 0.6282 -0.2206 -0.3404 0.0648 420 TRP B CB 2975 C CG . TRP A 389 ? 1.6034 0.5257 0.6133 -0.2126 -0.3050 0.0554 420 TRP B CG 2976 C CD1 . TRP A 389 ? 1.6050 0.5348 0.5957 -0.2309 -0.2830 0.0558 420 TRP B CD1 2977 C CD2 . TRP A 389 ? 1.5712 0.5322 0.6232 -0.1845 -0.2881 0.0437 420 TRP B CD2 2978 N NE1 . TRP A 389 ? 1.5769 0.5468 0.5963 -0.2150 -0.2543 0.0452 420 TRP B NE1 2979 C CE2 . TRP A 389 ? 1.5578 0.5470 0.6139 -0.1871 -0.2571 0.0383 420 TRP B CE2 2980 C CE3 . TRP A 389 ? 1.5560 0.5304 0.6421 -0.1582 -0.2965 0.0369 420 TRP B CE3 2981 C CZ2 . TRP A 389 ? 1.5302 0.5584 0.6220 -0.1648 -0.2357 0.0278 420 TRP B CZ2 2982 C CZ3 . TRP A 389 ? 1.5288 0.5434 0.6491 -0.1369 -0.2739 0.0261 420 TRP B CZ3 2983 C CH2 . TRP A 389 ? 1.5167 0.5568 0.6390 -0.1406 -0.2446 0.0224 420 TRP B CH2 2984 N N . ARG A 390 ? 1.5772 0.4942 0.6468 -0.1634 -0.3632 0.0533 421 ARG B N 2985 C CA . ARG A 390 ? 1.5399 0.4898 0.6493 -0.1373 -0.3582 0.0441 421 ARG B CA 2986 C C . ARG A 390 ? 1.5529 0.4896 0.6836 -0.1205 -0.3926 0.0429 421 ARG B C 2987 O O . ARG A 390 ? 1.5605 0.4873 0.7020 -0.1109 -0.4092 0.0402 421 ARG B O 2988 C CB . ARG A 390 ? 1.4936 0.4833 0.6352 -0.1170 -0.3334 0.0321 421 ARG B CB 2989 C CG . ARG A 390 ? 1.4579 0.4850 0.6152 -0.1103 -0.3035 0.0261 421 ARG B CG 2990 C CD . ARG A 390 ? 1.4269 0.4918 0.6267 -0.0823 -0.2931 0.0138 421 ARG B CD 2991 N NE . ARG A 390 ? 1.4141 0.5078 0.6353 -0.0708 -0.2817 0.0091 421 ARG B NE 2992 C CZ . ARG A 390 ? 1.3888 0.5200 0.6373 -0.0550 -0.2606 0.0002 421 ARG B CZ 2993 N NH1 . ARG A 390 ? 1.3738 0.5176 0.6318 -0.0484 -0.2491 -0.0049 421 ARG B NH1 2994 N NH2 . ARG A 390 ? 1.3795 0.5348 0.6450 -0.0467 -0.2517 -0.0031 421 ARG B NH2 2995 N N . PHE A 391 ? 1.5938 0.5306 0.7319 -0.1165 -0.4038 0.0440 422 PHE B N 2996 C CA . PHE A 391 ? 1.5989 0.5275 0.7631 -0.0984 -0.4361 0.0404 422 PHE B CA 2997 C C . PHE A 391 ? 1.5853 0.5474 0.7830 -0.0795 -0.4293 0.0317 422 PHE B C 2998 O O . PHE A 391 ? 1.5910 0.5528 0.7751 -0.0901 -0.4234 0.0369 422 PHE B O 2999 C CB . PHE A 391 ? 1.6367 0.5145 0.7683 -0.1181 -0.4706 0.0538 422 PHE B CB 3000 C CG . PHE A 391 ? 1.6515 0.5157 0.8093 -0.1009 -0.5081 0.0504 422 PHE B CG 3001 C CD1 . PHE A 391 ? 1.6224 0.5160 0.8287 -0.0703 -0.5113 0.0350 422 PHE B CD1 3002 C CD2 . PHE A 391 ? 1.6979 0.5192 0.8311 -0.1164 -0.5409 0.0622 422 PHE B CD2 3003 C CE1 . PHE A 391 ? 1.6366 0.5191 0.8692 -0.0546 -0.5458 0.0299 422 PHE B CE1 3004 C CE2 . PHE A 391 ? 1.7129 0.5230 0.8727 -0.1003 -0.5764 0.0582 422 PHE B CE2 3005 C CZ . PHE A 391 ? 1.6815 0.5207 0.8914 -0.0691 -0.5791 0.0416 422 PHE B CZ 3006 N N . ARG A 392 ? 1.5548 0.5463 0.7959 -0.0521 -0.4304 0.0179 423 ARG B N 3007 C CA . ARG A 392 ? 1.5430 0.5675 0.8167 -0.0348 -0.4250 0.0087 423 ARG B CA 3008 C C . ARG A 392 ? 1.5440 0.5698 0.8540 -0.0130 -0.4549 -0.0014 423 ARG B C 3009 O O . ARG A 392 ? 1.5322 0.5741 0.8705 0.0052 -0.4570 -0.0129 423 ARG B O 3010 C CB . ARG A 392 ? 1.5199 0.5904 0.8146 -0.0230 -0.3896 -0.0009 423 ARG B CB 3011 C CG . ARG A 392 ? 1.5159 0.5866 0.7804 -0.0415 -0.3605 0.0062 423 ARG B CG 3012 C CD . ARG A 392 ? 1.4921 0.6047 0.7801 -0.0280 -0.3305 -0.0036 423 ARG B CD 3013 N NE . ARG A 392 ? 1.4829 0.6281 0.7940 -0.0169 -0.3187 -0.0097 423 ARG B NE 3014 C CZ . ARG A 392 ? 1.4637 0.6481 0.8053 0.0005 -0.3017 -0.0205 423 ARG B CZ 3015 N NH1 . ARG A 392 ? 1.4506 0.6470 0.8042 0.0096 -0.2944 -0.0268 423 ARG B NH1 3016 N NH2 . ARG A 392 ? 1.4583 0.6697 0.8175 0.0077 -0.2925 -0.0248 423 ARG B NH2 3017 N N . SER A 393 ? 1.5220 0.5302 0.8311 -0.0156 -0.4785 0.0024 424 SER B N 3018 C CA . SER A 393 ? 1.5264 0.5340 0.8709 0.0040 -0.5097 -0.0077 424 SER B CA 3019 C C . SER A 393 ? 1.5176 0.5625 0.9001 0.0220 -0.5060 -0.0201 424 SER B C 3020 O O . SER A 393 ? 1.5229 0.5647 0.9329 0.0357 -0.5337 -0.0281 424 SER B O 3021 C CB . SER A 393 ? 1.5637 0.5194 0.8859 -0.0088 -0.5487 0.0036 424 SER B CB 3022 O OG . SER A 393 ? 1.5714 0.5250 0.9306 0.0122 -0.5790 -0.0082 424 SER B OG 3023 N N . GLN A 394 ? 1.4571 0.5352 0.8401 0.0207 -0.4732 -0.0213 425 GLN B N 3024 C CA . GLN A 394 ? 1.4411 0.5527 0.8529 0.0328 -0.4675 -0.0305 425 GLN B CA 3025 C C . GLN A 394 ? 1.4263 0.5697 0.8900 0.0598 -0.4780 -0.0506 425 GLN B C 3026 O O . GLN A 394 ? 1.4160 0.5716 0.8990 0.0726 -0.4769 -0.0608 425 GLN B O 3027 C CB . GLN A 394 ? 1.4156 0.5592 0.8207 0.0279 -0.4289 -0.0294 425 GLN B CB 3028 C CG . GLN A 394 ? 1.3878 0.5645 0.8096 0.0390 -0.4036 -0.0388 425 GLN B CG 3029 C CD . GLN A 394 ? 1.3889 0.5484 0.7763 0.0227 -0.3867 -0.0282 425 GLN B CD 3030 O OE1 . GLN A 394 ? 1.4118 0.5338 0.7748 0.0112 -0.4032 -0.0196 425 GLN B OE1 3031 N NE2 . GLN A 394 ? 1.3652 0.5516 0.7502 0.0207 -0.3544 -0.0288 425 GLN B NE2 3032 N N . ASN A 395 ? 1.4569 0.6146 0.9429 0.0675 -0.4877 -0.0569 426 ASN B N 3033 C CA . ASN A 395 ? 1.4488 0.6392 0.9859 0.0917 -0.4986 -0.0777 426 ASN B CA 3034 C C . ASN A 395 ? 1.4527 0.6234 1.0132 0.1049 -0.5348 -0.0870 426 ASN B C 3035 O O . ASN A 395 ? 1.4397 0.6372 1.0359 0.1237 -0.5346 -0.1047 426 ASN B O 3036 C CB . ASN A 395 ? 1.4279 0.6690 0.9897 0.1044 -0.4672 -0.0914 426 ASN B CB 3037 C CG . ASN A 395 ? 1.4218 0.6823 0.9633 0.0925 -0.4331 -0.0830 426 ASN B CG 3038 O OD1 . ASN A 395 ? 1.4240 0.7023 0.9727 0.0918 -0.4272 -0.0840 426 ASN B OD1 3039 N ND2 . ASN A 395 ? 1.4136 0.6708 0.9306 0.0832 -0.4110 -0.0751 426 ASN B ND2 3040 N N . ASN A 396 ? 1.5145 0.6383 1.0553 0.0947 -0.5665 -0.0756 427 ASN B N 3041 C CA . ASN A 396 ? 1.5220 0.6231 1.0848 0.1066 -0.6043 -0.0836 427 ASN B CA 3042 C C . ASN A 396 ? 1.5398 0.6184 1.1117 0.1072 -0.6389 -0.0824 427 ASN B C 3043 O O . ASN A 396 ? 1.5447 0.6283 1.1072 0.0990 -0.6322 -0.0762 427 ASN B O 3044 C CB . ASN A 396 ? 1.5324 0.5896 1.0607 0.0935 -0.6153 -0.0700 427 ASN B CB 3045 C CG . ASN A 396 ? 1.5122 0.5918 1.0412 0.0978 -0.5875 -0.0752 427 ASN B CG 3046 O OD1 . ASN A 396 ? 1.5044 0.5837 1.0548 0.1113 -0.5999 -0.0860 427 ASN B OD1 3047 N ND2 . ASN A 396 ? 1.5035 0.6023 1.0099 0.0867 -0.5504 -0.0678 427 ASN B ND2 3048 N N . ARG A 397 ? 1.7560 0.8104 1.3484 0.1177 -0.6767 -0.0893 428 ARG B N 3049 C CA . ARG A 397 ? 1.7739 0.8017 1.3770 0.1191 -0.7155 -0.0885 428 ARG B CA 3050 C C . ARG A 397 ? 1.8131 0.7753 1.3702 0.0968 -0.7458 -0.0654 428 ARG B C 3051 O O . ARG A 397 ? 1.8443 0.7784 1.4117 0.0990 -0.7844 -0.0649 428 ARG B O 3052 C CB . ARG A 397 ? 1.7651 0.8120 1.4281 0.1468 -0.7411 -0.1138 428 ARG B CB 3053 C CG . ARG A 397 ? 1.7431 0.8555 1.4500 0.1657 -0.7130 -0.1366 428 ARG B CG 3054 C CD . ARG A 397 ? 1.7337 0.8675 1.5014 0.1921 -0.7381 -0.1636 428 ARG B CD 3055 N NE . ARG A 397 ? 1.7123 0.9114 1.5193 0.2080 -0.7080 -0.1860 428 ARG B NE 3056 C CZ . ARG A 397 ? 1.7009 0.9347 1.5654 0.2308 -0.7201 -0.2136 428 ARG B CZ 3057 N NH1 . ARG A 397 ? 1.7076 0.9165 1.5998 0.2421 -0.7631 -0.2228 428 ARG B NH1 3058 N NH2 . ARG A 397 ? 1.6836 0.9773 1.5779 0.2415 -0.6896 -0.2325 428 ARG B NH2 3059 N N . LEU A 398 ? 1.7510 0.6892 1.2595 0.0756 -0.7301 -0.0475 429 LEU B N 3060 C CA . LEU A 398 ? 1.7997 0.6761 1.2595 0.0508 -0.7561 -0.0249 429 LEU B CA 3061 C C . LEU A 398 ? 1.8275 0.6793 1.2694 0.0371 -0.7754 -0.0129 429 LEU B C 3062 O O . LEU A 398 ? 1.8062 0.6832 1.2435 0.0325 -0.7508 -0.0114 429 LEU B O 3063 C CB . LEU A 398 ? 1.7981 0.6639 1.2074 0.0277 -0.7261 -0.0088 429 LEU B CB 3064 C CG . LEU A 398 ? 1.7625 0.6615 1.1852 0.0387 -0.6956 -0.0193 429 LEU B CG 3065 C CD1 . LEU A 398 ? 1.7675 0.6512 1.1393 0.0140 -0.6700 -0.0027 429 LEU B CD1 3066 C CD2 . LEU A 398 ? 1.7704 0.6605 1.2230 0.0566 -0.7219 -0.0314 429 LEU B CD2 3067 N N . ASN A 399 ? 1.8503 0.6779 1.2875 0.0272 -0.8117 -0.0073 430 ASN B N 3068 C CA . ASN A 399 ? 1.8752 0.6887 1.3071 0.0171 -0.8330 -0.0012 430 ASN B CA 3069 C C . ASN A 399 ? 1.9197 0.6975 1.2979 -0.0186 -0.8445 0.0196 430 ASN B C 3070 O O . ASN A 399 ? 1.9312 0.6951 1.2696 -0.0386 -0.8326 0.0317 430 ASN B O 3071 C CB . ASN A 399 ? 1.8823 0.7050 1.3702 0.0402 -0.8686 -0.0202 430 ASN B CB 3072 C CG . ASN A 399 ? 1.9173 0.7209 1.4123 0.0367 -0.9025 -0.0231 430 ASN B CG 3073 O OD1 . ASN A 399 ? 1.9276 0.7185 1.3944 0.0241 -0.8971 -0.0142 430 ASN B OD1 3074 N ND2 . ASN A 399 ? 1.9367 0.7378 1.4703 0.0476 -0.9379 -0.0363 430 ASN B ND2 3075 N N . GLY A 400 ? 2.2544 1.0184 1.6322 -0.0270 -0.8665 0.0225 431 GLY B N 3076 C CA . GLY A 400 ? 2.3018 1.0307 1.6362 -0.0596 -0.8844 0.0381 431 GLY B CA 3077 C C . GLY A 400 ? 2.3032 1.0238 1.5802 -0.0883 -0.8534 0.0562 431 GLY B C 3078 O O . GLY A 400 ? 2.2671 1.0081 1.5385 -0.0829 -0.8183 0.0571 431 GLY B O 3079 N N . THR A 401 ? 2.0433 0.7338 1.2781 -0.1196 -0.8668 0.0694 432 THR B N 3080 C CA . THR A 401 ? 2.0497 0.7323 1.2294 -0.1497 -0.8392 0.0847 432 THR B CA 3081 C C . THR A 401 ? 2.0291 0.7225 1.1933 -0.1501 -0.8114 0.0866 432 THR B C 3082 O O . THR A 401 ? 2.0254 0.7219 1.2110 -0.1352 -0.8216 0.0796 432 THR B O 3083 C CB . THR A 401 ? 2.1044 0.7524 1.2438 -0.1836 -0.8623 0.0962 432 THR B CB 3084 O OG1 . THR A 401 ? 2.1305 0.7631 1.2918 -0.1809 -0.8975 0.0923 432 THR B OG1 3085 C CG2 . THR A 401 ? 2.1099 0.7536 1.1981 -0.2140 -0.8339 0.1089 432 THR B CG2 3086 N N . ILE A 402 ? 2.0352 0.7345 1.1634 -0.1674 -0.7760 0.0951 433 ILE B N 3087 C CA . ILE A 402 ? 2.0180 0.7257 1.1277 -0.1717 -0.7476 0.0973 433 ILE B CA 3088 C C . ILE A 402 ? 2.0596 0.7428 1.1240 -0.2036 -0.7554 0.1079 433 ILE B C 3089 O O . ILE A 402 ? 2.0913 0.7571 1.1230 -0.2302 -0.7621 0.1163 433 ILE B O 3090 C CB . ILE A 402 ? 1.9827 0.7103 1.0784 -0.1744 -0.7044 0.0992 433 ILE B CB 3091 C CG1 . ILE A 402 ? 1.9405 0.6932 1.0814 -0.1415 -0.6954 0.0878 433 ILE B CG1 3092 C CG2 . ILE A 402 ? 1.9716 0.7042 1.0428 -0.1846 -0.6756 0.1021 433 ILE B CG2 3093 C CD1 . ILE A 402 ? 1.9024 0.6755 1.0361 -0.1392 -0.6534 0.0873 433 ILE B CD1 3094 N N . PRO A 403 ? 2.0503 0.7319 1.1136 -0.2011 -0.7561 0.1069 434 PRO B N 3095 C CA . PRO A 403 ? 2.0859 0.7474 1.1060 -0.2303 -0.7595 0.1163 434 PRO B CA 3096 C C . PRO A 403 ? 2.0903 0.7515 1.0623 -0.2608 -0.7281 0.1248 434 PRO B C 3097 O O . PRO A 403 ? 2.0550 0.7369 1.0264 -0.2569 -0.6928 0.1230 434 PRO B O 3098 C CB . PRO A 403 ? 2.0684 0.7386 1.1053 -0.2140 -0.7545 0.1111 434 PRO B CB 3099 C CG . PRO A 403 ? 2.0493 0.7305 1.1417 -0.1791 -0.7748 0.0986 434 PRO B CG 3100 C CD . PRO A 403 ? 2.0256 0.7212 1.1353 -0.1684 -0.7644 0.0949 434 PRO B CD 3101 N N . ILE A 404 ? 2.1756 0.8127 1.1082 -0.2920 -0.7433 0.1332 435 ILE B N 3102 C CA . ILE A 404 ? 2.1926 0.8247 1.0808 -0.3246 -0.7243 0.1400 435 ILE B CA 3103 C C . ILE A 404 ? 2.1968 0.8312 1.0465 -0.3479 -0.6968 0.1434 435 ILE B C 3104 O O . ILE A 404 ? 2.2152 0.8451 1.0277 -0.3770 -0.6827 0.1474 435 ILE B O 3105 C CB . ILE A 404 ? 2.2444 0.8480 1.1119 -0.3477 -0.7582 0.1460 435 ILE B CB 3106 C CG1 . ILE A 404 ? 2.2540 0.8475 1.1614 -0.3249 -0.7984 0.1419 435 ILE B CG1 3107 C CG2 . ILE A 404 ? 2.2447 0.8513 1.0919 -0.3654 -0.7406 0.1485 435 ILE B CG2 3108 C CD1 . ILE A 404 ? 2.2947 0.8638 1.1994 -0.3301 -0.8359 0.1440 435 ILE B CD1 3109 N N . GLY A 405 ? 2.2375 0.8789 1.0963 -0.3364 -0.6898 0.1411 436 GLY B N 3110 C CA . GLY A 405 ? 2.2504 0.8895 1.0719 -0.3606 -0.6711 0.1445 436 GLY B CA 3111 C C . GLY A 405 ? 2.2086 0.8730 1.0308 -0.3555 -0.6273 0.1400 436 GLY B C 3112 O O . GLY A 405 ? 2.2146 0.8796 1.0135 -0.3704 -0.6120 0.1410 436 GLY B O 3113 N N . PHE A 406 ? 2.0162 0.7013 0.8651 -0.3350 -0.6074 0.1346 437 PHE B N 3114 C CA . PHE A 406 ? 1.9725 0.6819 0.8318 -0.3233 -0.5695 0.1291 437 PHE B CA 3115 C C . PHE A 406 ? 1.9730 0.6903 0.7965 -0.3506 -0.5350 0.1294 437 PHE B C 3116 O O . PHE A 406 ? 1.9458 0.6790 0.7721 -0.3461 -0.5065 0.1252 437 PHE B O 3117 C CB . PHE A 406 ? 1.9310 0.6593 0.8280 -0.2947 -0.5594 0.1232 437 PHE B CB 3118 C CG . PHE A 406 ? 1.9154 0.6459 0.8564 -0.2617 -0.5815 0.1179 437 PHE B CG 3119 C CD1 . PHE A 406 ? 1.9072 0.6393 0.8614 -0.2494 -0.5832 0.1146 437 PHE B CD1 3120 C CD2 . PHE A 406 ? 1.9095 0.6411 0.8797 -0.2431 -0.6006 0.1150 437 PHE B CD2 3121 C CE1 . PHE A 406 ? 1.8927 0.6287 0.8896 -0.2190 -0.6030 0.1074 437 PHE B CE1 3122 C CE2 . PHE A 406 ? 1.8953 0.6312 0.9087 -0.2126 -0.6206 0.1075 437 PHE B CE2 3123 C CZ . PHE A 406 ? 1.8869 0.6254 0.9139 -0.2005 -0.6216 0.1032 437 PHE B CZ 3124 N N . GLY A 407 ? 2.1476 0.8539 0.9391 -0.3789 -0.5381 0.1331 438 GLY B N 3125 C CA . GLY A 407 ? 2.1476 0.8633 0.9089 -0.4048 -0.5054 0.1308 438 GLY B CA 3126 C C . GLY A 407 ? 2.1719 0.8814 0.9011 -0.4293 -0.4983 0.1314 438 GLY B C 3127 O O . GLY A 407 ? 2.1714 0.8906 0.8779 -0.4506 -0.4694 0.1272 438 GLY B O 3128 N N . SER A 408 ? 2.0017 0.6952 0.7305 -0.4262 -0.5252 0.1358 439 SER B N 3129 C CA . SER A 408 ? 2.0259 0.7121 0.7263 -0.4469 -0.5226 0.1374 439 SER B CA 3130 C C . SER A 408 ? 1.9903 0.6977 0.6989 -0.4384 -0.4886 0.1315 439 SER B C 3131 O O . SER A 408 ? 2.0041 0.7136 0.6839 -0.4623 -0.4712 0.1298 439 SER B O 3132 C CB . SER A 408 ? 2.0559 0.7198 0.7592 -0.4415 -0.5623 0.1437 439 SER B CB 3133 O OG . SER A 408 ? 2.0786 0.7354 0.7555 -0.4596 -0.5607 0.1458 439 SER B OG 3134 N N . LEU A 409 ? 1.9646 0.6878 0.7126 -0.4052 -0.4793 0.1277 440 LEU B N 3135 C CA . LEU A 409 ? 1.9334 0.6715 0.6965 -0.3911 -0.4574 0.1232 440 LEU B CA 3136 C C . LEU A 409 ? 1.9065 0.6668 0.6628 -0.3997 -0.4146 0.1161 440 LEU B C 3137 O O . LEU A 409 ? 1.8792 0.6538 0.6502 -0.3902 -0.3974 0.1120 440 LEU B O 3138 C CB . LEU A 409 ? 1.8994 0.6441 0.7091 -0.3527 -0.4674 0.1205 440 LEU B CB 3139 C CG . LEU A 409 ? 1.9213 0.6483 0.7443 -0.3422 -0.5081 0.1249 440 LEU B CG 3140 C CD1 . LEU A 409 ? 1.8860 0.6235 0.7566 -0.3054 -0.5148 0.1194 440 LEU B CD1 3141 C CD2 . LEU A 409 ? 1.9595 0.6651 0.7689 -0.3513 -0.5380 0.1305 440 LEU B CD2 3142 N N . ARG A 410 ? 2.0168 0.7801 0.7518 -0.4171 -0.3980 0.1143 441 ARG B N 3143 C CA . ARG A 410 ? 1.9959 0.7798 0.7231 -0.4283 -0.3582 0.1063 441 ARG B CA 3144 C C . ARG A 410 ? 1.9456 0.7494 0.7089 -0.3998 -0.3355 0.1002 441 ARG B C 3145 O O . ARG A 410 ? 1.9226 0.7449 0.6875 -0.4035 -0.3032 0.0929 441 ARG B O 3146 C CB . ARG A 410 ? 2.0219 0.8040 0.7159 -0.4567 -0.3473 0.1051 441 ARG B CB 3147 C CG . ARG A 410 ? 2.0731 0.8383 0.7264 -0.4920 -0.3619 0.1078 441 ARG B CG 3148 C CD . ARG A 410 ? 2.1098 0.8497 0.7527 -0.4935 -0.4009 0.1179 441 ARG B CD 3149 N NE . ARG A 410 ? 2.1611 0.8855 0.7603 -0.5303 -0.4109 0.1202 441 ARG B NE 3150 C CZ . ARG A 410 ? 2.1993 0.9072 0.7747 -0.5526 -0.4296 0.1230 441 ARG B CZ 3151 N NH1 . ARG A 410 ? 2.1911 0.8966 0.7822 -0.5414 -0.4394 0.1242 441 ARG B NH1 3152 N NH2 . ARG A 410 ? 2.2467 0.9404 0.7820 -0.5868 -0.4383 0.1244 441 ARG B NH2 3153 N N . ASN A 411 ? 1.8816 0.6814 0.6742 -0.3727 -0.3524 0.1017 442 ASN B N 3154 C CA . ASN A 411 ? 1.8360 0.6531 0.6639 -0.3466 -0.3329 0.0937 442 ASN B CA 3155 C C . ASN A 411 ? 1.8038 0.6291 0.6681 -0.3173 -0.3362 0.0901 442 ASN B C 3156 O O . ASN A 411 ? 1.7631 0.6109 0.6598 -0.2948 -0.3189 0.0805 442 ASN B O 3157 C CB . ASN A 411 ? 1.8331 0.6470 0.6712 -0.3373 -0.3387 0.0926 442 ASN B CB 3158 C CG . ASN A 411 ? 1.8388 0.6594 0.6542 -0.3594 -0.3141 0.0897 442 ASN B CG 3159 O OD1 . ASN A 411 ? 1.8355 0.6679 0.6356 -0.3766 -0.2878 0.0856 442 ASN B OD1 3160 N ND2 . ASN A 411 ? 1.8475 0.6615 0.6623 -0.3585 -0.3223 0.0910 442 ASN B ND2 3161 N N . LEU A 412 ? 1.7457 0.5625 0.6089 -0.3162 -0.3560 0.0953 443 LEU B N 3162 C CA . LEU A 412 ? 1.7200 0.5420 0.6197 -0.2865 -0.3661 0.0924 443 LEU B CA 3163 C C . LEU A 412 ? 1.6850 0.5359 0.6002 -0.2788 -0.3393 0.0856 443 LEU B C 3164 O O . LEU A 412 ? 1.7014 0.5437 0.5962 -0.2943 -0.3392 0.0905 443 LEU B O 3165 C CB . LEU A 412 ? 1.7494 0.5539 0.6468 -0.2864 -0.4023 0.0997 443 LEU B CB 3166 C CG . LEU A 412 ? 1.7347 0.5422 0.6605 -0.2644 -0.4159 0.0983 443 LEU B CG 3167 C CD1 . LEU A 412 ? 1.7115 0.5237 0.6785 -0.2320 -0.4287 0.0916 443 LEU B CD1 3168 C CD2 . LEU A 412 ? 1.7723 0.5614 0.6824 -0.2771 -0.4460 0.1060 443 LEU B CD2 3169 N N . THR A 413 ? 1.6353 0.5256 0.5889 -0.2540 -0.3169 0.0736 444 THR B N 3170 C CA . THR A 413 ? 1.5996 0.5234 0.5711 -0.2456 -0.2911 0.0664 444 THR B CA 3171 C C . THR A 413 ? 1.5648 0.5140 0.5775 -0.2160 -0.2942 0.0607 444 THR B C 3172 O O . THR A 413 ? 1.5412 0.5137 0.5633 -0.2129 -0.2747 0.0565 444 THR B O 3173 C CB . THR A 413 ? 1.5711 0.5232 0.5477 -0.2479 -0.2556 0.0572 444 THR B CB 3174 O OG1 . THR A 413 ? 1.5338 0.5116 0.5482 -0.2209 -0.2492 0.0486 444 THR B OG1 3175 C CG2 . THR A 413 ? 1.6049 0.5351 0.5425 -0.2777 -0.2514 0.0611 444 THR B CG2 3176 N N . PHE A 414 ? 1.5923 0.5386 0.6299 -0.1949 -0.3176 0.0596 445 PHE B N 3177 C CA . PHE A 414 ? 1.5759 0.5510 0.6539 -0.1677 -0.3177 0.0521 445 PHE B CA 3178 C C . PHE A 414 ? 1.5873 0.5443 0.6784 -0.1556 -0.3532 0.0545 445 PHE B C 3179 O O . PHE A 414 ? 1.5888 0.5339 0.6884 -0.1472 -0.3712 0.0535 445 PHE B O 3180 C CB . PHE A 414 ? 1.5513 0.5619 0.6641 -0.1450 -0.2988 0.0407 445 PHE B CB 3181 C CG . PHE A 414 ? 1.5313 0.5798 0.6809 -0.1225 -0.2863 0.0320 445 PHE B CG 3182 C CD1 . PHE A 414 ? 1.5311 0.5854 0.7076 -0.1035 -0.3064 0.0287 445 PHE B CD1 3183 C CD2 . PHE A 414 ? 1.5135 0.5925 0.6721 -0.1203 -0.2550 0.0265 445 PHE B CD2 3184 C CE1 . PHE A 414 ? 1.5155 0.6058 0.7244 -0.0847 -0.2943 0.0204 445 PHE B CE1 3185 C CE2 . PHE A 414 ? 1.4978 0.6100 0.6877 -0.1016 -0.2444 0.0194 445 PHE B CE2 3186 C CZ . PHE A 414 ? 1.4993 0.6178 0.7136 -0.0843 -0.2635 0.0165 445 PHE B CZ 3187 N N . VAL A 415 ? 1.5487 0.5056 0.6452 -0.1529 -0.3634 0.0564 446 VAL B N 3188 C CA . VAL A 415 ? 1.5670 0.5073 0.6790 -0.1409 -0.3988 0.0574 446 VAL B CA 3189 C C . VAL A 415 ? 1.5387 0.5079 0.6875 -0.1192 -0.3994 0.0494 446 VAL B C 3190 O O . VAL A 415 ? 1.5347 0.5108 0.6759 -0.1265 -0.3896 0.0520 446 VAL B O 3191 C CB . VAL A 415 ? 1.6205 0.5144 0.6938 -0.1653 -0.4260 0.0714 446 VAL B CB 3192 C CG1 . VAL A 415 ? 1.6372 0.5160 0.7318 -0.1503 -0.4633 0.0710 446 VAL B CG1 3193 C CG2 . VAL A 415 ? 1.6553 0.5169 0.6903 -0.1887 -0.4306 0.0801 446 VAL B CG2 3194 N N . ASP A 416 ? 1.5490 0.5354 0.7376 -0.0932 -0.4113 0.0391 447 ASP B N 3195 C CA . ASP A 416 ? 1.5412 0.5547 0.7654 -0.0735 -0.4146 0.0304 447 ASP B CA 3196 C C . ASP A 416 ? 1.5519 0.5484 0.7963 -0.0608 -0.4526 0.0276 447 ASP B C 3197 O O . ASP A 416 ? 1.5452 0.5476 0.8156 -0.0436 -0.4638 0.0187 447 ASP B O 3198 C CB . ASP A 416 ? 1.5167 0.5777 0.7771 -0.0520 -0.3888 0.0168 447 ASP B CB 3199 C CG . ASP A 416 ? 1.5096 0.6033 0.8036 -0.0350 -0.3860 0.0078 447 ASP B CG 3200 O OD1 . ASP A 416 ? 1.5192 0.6042 0.8272 -0.0280 -0.4120 0.0060 447 ASP B OD1 3201 O OD2 . ASP A 416 ? 1.4942 0.6233 0.8016 -0.0287 -0.3579 0.0021 447 ASP B OD2 3202 N N . LEU A 417 ? 1.5564 0.5330 0.7906 -0.0689 -0.4723 0.0343 448 LEU B N 3203 C CA . LEU A 417 ? 1.5669 0.5302 0.8245 -0.0560 -0.5089 0.0305 448 LEU B CA 3204 C C . LEU A 417 ? 1.5565 0.5546 0.8538 -0.0363 -0.5079 0.0189 448 LEU B C 3205 O O . LEU A 417 ? 1.5658 0.5542 0.8831 -0.0267 -0.5379 0.0153 448 LEU B O 3206 C CB . LEU A 417 ? 1.6173 0.5288 0.8373 -0.0783 -0.5389 0.0461 448 LEU B CB 3207 C CG . LEU A 417 ? 1.6466 0.5245 0.8393 -0.0914 -0.5492 0.0538 448 LEU B CG 3208 C CD1 . LEU A 417 ? 1.7022 0.5280 0.8482 -0.1197 -0.5740 0.0715 448 LEU B CD1 3209 C CD2 . LEU A 417 ? 1.6450 0.5243 0.8738 -0.0682 -0.5719 0.0428 448 LEU B CD2 3210 N N . SER A 418 ? 1.5527 0.5901 0.8603 -0.0317 -0.4743 0.0134 449 SER B N 3211 C CA . SER A 418 ? 1.5472 0.6189 0.8867 -0.0174 -0.4688 0.0039 449 SER B CA 3212 C C . SER A 418 ? 1.5425 0.6368 0.9315 0.0092 -0.4864 -0.0130 449 SER B C 3213 O O . SER A 418 ? 1.5329 0.6365 0.9409 0.0222 -0.4874 -0.0220 449 SER B O 3214 C CB . SER A 418 ? 1.5303 0.6406 0.8729 -0.0165 -0.4290 0.0004 449 SER B CB 3215 O OG . SER A 418 ? 1.5149 0.6492 0.8753 -0.0040 -0.4126 -0.0087 449 SER B OG 3216 N N . ASN A 419 ? 1.6520 0.7573 1.0626 0.0169 -0.4989 -0.0182 450 ASN B N 3217 C CA . ASN A 419 ? 1.6499 0.7789 1.1102 0.0414 -0.5165 -0.0362 450 ASN B CA 3218 C C . ASN A 419 ? 1.6583 0.7566 1.1279 0.0483 -0.5526 -0.0389 450 ASN B C 3219 O O . ASN A 419 ? 1.6491 0.7620 1.1444 0.0640 -0.5538 -0.0513 450 ASN B O 3220 C CB . ASN A 419 ? 1.6282 0.8093 1.1222 0.0591 -0.4890 -0.0525 450 ASN B CB 3221 C CG . ASN A 419 ? 1.6269 0.8383 1.1732 0.0830 -0.5041 -0.0732 450 ASN B CG 3222 O OD1 . ASN A 419 ? 1.6384 0.8372 1.1989 0.0871 -0.5323 -0.0760 450 ASN B OD1 3223 N ND2 . ASN A 419 ? 1.6122 0.8644 1.1880 0.0984 -0.4857 -0.0887 450 ASN B ND2 3224 N N . ASN A 420 ? 1.7221 0.7768 1.1704 0.0360 -0.5830 -0.0271 451 ASN B N 3225 C CA . ASN A 420 ? 1.7315 0.7550 1.1915 0.0431 -0.6221 -0.0298 451 ASN B CA 3226 C C . ASN A 420 ? 1.7470 0.7503 1.2148 0.0427 -0.6552 -0.0279 451 ASN B C 3227 O O . ASN A 420 ? 1.7471 0.7653 1.2142 0.0388 -0.6454 -0.0261 451 ASN B O 3228 C CB . ASN A 420 ? 1.7425 0.7205 1.1584 0.0238 -0.6298 -0.0136 451 ASN B CB 3229 C CG . ASN A 420 ? 1.7272 0.7249 1.1405 0.0266 -0.6006 -0.0174 451 ASN B CG 3230 O OD1 . ASN A 420 ? 1.7149 0.7227 1.1565 0.0438 -0.6079 -0.0299 451 ASN B OD1 3231 N ND2 . ASN A 420 ? 1.7276 0.7305 1.1077 0.0096 -0.5683 -0.0071 451 ASN B ND2 3232 N N . ARG A 421 ? 1.7225 0.6926 1.2000 0.0478 -0.6955 -0.0289 452 ARG B N 3233 C CA . ARG A 421 ? 1.7406 0.6844 1.2232 0.0461 -0.7320 -0.0255 452 ARG B CA 3234 C C . ARG A 421 ? 1.7869 0.6702 1.2135 0.0170 -0.7536 -0.0005 452 ARG B C 3235 O O . ARG A 421 ? 1.8216 0.6721 1.2494 0.0146 -0.7920 0.0041 452 ARG B O 3236 C CB . ARG A 421 ? 1.7423 0.6939 1.2802 0.0725 -0.7650 -0.0456 452 ARG B CB 3237 C CG . ARG A 421 ? 1.7147 0.7306 1.3072 0.0975 -0.7434 -0.0705 452 ARG B CG 3238 C CD . ARG A 421 ? 1.7062 0.7357 1.3564 0.1247 -0.7717 -0.0943 452 ARG B CD 3239 N NE . ARG A 421 ? 1.6828 0.7756 1.3792 0.1461 -0.7442 -0.1186 452 ARG B NE 3240 C CZ . ARG A 421 ? 1.6705 0.7865 1.4166 0.1699 -0.7561 -0.1424 452 ARG B CZ 3241 N NH1 . ARG A 421 ? 1.6787 0.7592 1.4373 0.1771 -0.7960 -0.1456 452 ARG B NH1 3242 N NH2 . ARG A 421 ? 1.6504 0.8251 1.4335 0.1859 -0.7283 -0.1635 452 ARG B NH2 3243 N N . PHE A 422 ? 1.8054 0.6735 1.1842 -0.0050 -0.7304 0.0148 453 PHE B N 3244 C CA . PHE A 422 ? 1.8511 0.6652 1.1719 -0.0362 -0.7454 0.0382 453 PHE B CA 3245 C C . PHE A 422 ? 1.8705 0.6717 1.1788 -0.0475 -0.7580 0.0468 453 PHE B C 3246 O O . PHE A 422 ? 1.8399 0.6757 1.1577 -0.0444 -0.7324 0.0423 453 PHE B O 3247 C CB . PHE A 422 ? 1.8417 0.6561 1.1171 -0.0583 -0.7082 0.0500 453 PHE B CB 3248 C CG . PHE A 422 ? 1.8342 0.6490 1.1080 -0.0548 -0.6987 0.0469 453 PHE B CG 3249 C CD1 . PHE A 422 ? 1.8674 0.6579 1.1339 -0.0613 -0.7259 0.0502 453 PHE B CD1 3250 C CD2 . PHE A 422 ? 1.7908 0.6477 1.0749 -0.0468 -0.6576 0.0382 453 PHE B CD2 3251 C CE1 . PHE A 422 ? 1.8596 0.6528 1.1248 -0.0583 -0.7163 0.0475 453 PHE B CE1 3252 C CE2 . PHE A 422 ? 1.7836 0.6413 1.0665 -0.0438 -0.6488 0.0354 453 PHE B CE2 3253 C CZ . PHE A 422 ? 1.8202 0.6362 1.0904 -0.0492 -0.6804 0.0414 453 PHE B CZ 3254 N N . THR A 423 ? 1.8497 0.6244 1.1447 -0.0644 -0.7888 0.0529 454 THR B N 3255 C CA . THR A 423 ? 1.8720 0.6340 1.1578 -0.0773 -0.8037 0.0589 454 THR B CA 3256 C C . THR A 423 ? 1.9072 0.6418 1.1356 -0.1157 -0.7997 0.0760 454 THR B C 3257 O O . THR A 423 ? 1.9109 0.6399 1.1069 -0.1315 -0.7830 0.0830 454 THR B O 3258 C CB . THR A 423 ? 1.8969 0.6488 1.2216 -0.0651 -0.8468 0.0482 454 THR B CB 3259 O OG1 . THR A 423 ? 1.9259 0.6583 1.2468 -0.0719 -0.8693 0.0476 454 THR B OG1 3260 C CG2 . THR A 423 ? 1.8622 0.6461 1.2479 -0.0273 -0.8514 0.0287 454 THR B CG2 3261 N N . ASP A 424 ? 2.0498 0.7684 1.2680 -0.1303 -0.8150 0.0814 455 ASP B N 3262 C CA . ASP A 424 ? 2.0898 0.7803 1.2582 -0.1674 -0.8180 0.0953 455 ASP B CA 3263 C C . ASP A 424 ? 2.0783 0.7748 1.2003 -0.1897 -0.7785 0.1057 455 ASP B C 3264 O O . ASP A 424 ? 2.0425 0.7621 1.1666 -0.1812 -0.7484 0.1051 455 ASP B O 3265 C CB . ASP A 424 ? 2.1308 0.7947 1.2894 -0.1798 -0.8479 0.0968 455 ASP B CB 3266 C CG . ASP A 424 ? 2.1783 0.8110 1.3306 -0.1972 -0.8833 0.1005 455 ASP B CG 3267 O OD1 . ASP A 424 ? 2.1781 0.8105 1.3387 -0.1967 -0.8857 0.1009 455 ASP B OD1 3268 O OD2 . ASP A 424 ? 2.2176 0.8252 1.3569 -0.2114 -0.9094 0.1032 455 ASP B OD2 3269 N N . GLN A 425 ? 2.3151 0.9911 1.3959 -0.2186 -0.7796 0.1143 456 GLN B N 3270 C CA . GLN A 425 ? 2.3118 0.9910 1.3479 -0.2438 -0.7454 0.1226 456 GLN B CA 3271 C C . GLN A 425 ? 2.2779 0.9774 1.3124 -0.2347 -0.7141 0.1201 456 GLN B C 3272 O O . GLN A 425 ? 2.2687 0.9721 1.3258 -0.2165 -0.7226 0.1143 456 GLN B O 3273 C CB . GLN A 425 ? 2.3616 1.0121 1.3538 -0.2797 -0.7586 0.1315 456 GLN B CB 3274 C CG . GLN A 425 ? 2.3999 1.0269 1.3866 -0.2946 -0.7873 0.1354 456 GLN B CG 3275 C CD . GLN A 425 ? 2.4246 1.0337 1.4432 -0.2807 -0.8316 0.1306 456 GLN B CD 3276 O OE1 . GLN A 425 ? 2.4238 1.0328 1.4585 -0.2676 -0.8438 0.1260 456 GLN B OE1 3277 N NE2 . GLN A 425 ? 2.4470 1.0406 1.4763 -0.2834 -0.8559 0.1310 456 GLN B NE2 3278 N N . ILE A 426 ? 2.0349 0.7469 1.0435 -0.2479 -0.6778 0.1238 457 ILE B N 3279 C CA . ILE A 426 ? 2.0099 0.7369 1.0069 -0.2482 -0.6452 0.1228 457 ILE B CA 3280 C C . ILE A 426 ? 2.0455 0.7541 0.9987 -0.2812 -0.6444 0.1293 457 ILE B C 3281 O O . ILE A 426 ? 2.0749 0.7695 0.9990 -0.3074 -0.6482 0.1348 457 ILE B O 3282 C CB . ILE A 426 ? 1.9753 0.7251 0.9668 -0.2476 -0.6069 0.1225 457 ILE B CB 3283 C CG1 . ILE A 426 ? 1.9454 0.7120 0.9763 -0.2182 -0.6101 0.1171 457 ILE B CG1 3284 C CG2 . ILE A 426 ? 1.9498 0.7146 0.9314 -0.2479 -0.5732 0.1206 457 ILE B CG2 3285 C CD1 . ILE A 426 ? 1.9234 0.7069 0.9451 -0.2222 -0.5820 0.1190 457 ILE B CD1 3286 N N . PRO A 427 ? 2.0500 0.7581 0.9984 -0.2806 -0.6404 0.1283 458 PRO B N 3287 C CA . PRO A 427 ? 2.0849 0.7762 0.9919 -0.3117 -0.6405 0.1339 458 PRO B CA 3288 C C . PRO A 427 ? 2.0858 0.7830 0.9559 -0.3392 -0.6080 0.1364 458 PRO B C 3289 O O . PRO A 427 ? 2.0490 0.7688 0.9247 -0.3314 -0.5745 0.1329 458 PRO B O 3290 C CB . PRO A 427 ? 2.0696 0.7676 0.9854 -0.2995 -0.6334 0.1308 458 PRO B CB 3291 C CG . PRO A 427 ? 2.0455 0.7524 1.0095 -0.2638 -0.6494 0.1240 458 PRO B CG 3292 C CD . PRO A 427 ? 2.0212 0.7421 1.0048 -0.2506 -0.6410 0.1213 458 PRO B CD 3293 N N . ALA A 428 ? 2.0147 0.6915 0.8481 -0.3713 -0.6185 0.1416 459 ALA B N 3294 C CA . ALA A 428 ? 2.0214 0.7021 0.8211 -0.3995 -0.5918 0.1425 459 ALA B CA 3295 C C . ALA A 428 ? 2.0096 0.7026 0.7892 -0.4115 -0.5591 0.1395 459 ALA B C 3296 O O . ALA A 428 ? 1.9876 0.6983 0.7596 -0.4181 -0.5252 0.1358 459 ALA B O 3297 C CB . ALA A 428 ? 2.0740 0.7279 0.8425 -0.4301 -0.6158 0.1481 459 ALA B CB 3298 N N . ASP A 429 ? 2.2877 0.9714 1.0603 -0.4139 -0.5701 0.1406 460 ASP B N 3299 C CA . ASP A 429 ? 2.2827 0.9750 1.0348 -0.4274 -0.5433 0.1379 460 ASP B CA 3300 C C . ASP A 429 ? 2.2303 0.9504 1.0065 -0.4042 -0.5101 0.1317 460 ASP B C 3301 O O . ASP A 429 ? 2.2204 0.9510 0.9833 -0.4138 -0.4836 0.1282 460 ASP B O 3302 C CB . ASP A 429 ? 2.3111 0.9860 1.0537 -0.4319 -0.5671 0.1414 460 ASP B CB 3303 C CG . ASP A 429 ? 2.2920 0.9680 1.0740 -0.3974 -0.5876 0.1409 460 ASP B CG 3304 O OD1 . ASP A 429 ? 2.2663 0.9517 1.0809 -0.3729 -0.5913 0.1385 460 ASP B OD1 3305 O OD2 . ASP A 429 ? 2.3031 0.9712 1.0842 -0.3951 -0.6001 0.1421 460 ASP B OD2 3306 N N . PHE A 430 ? 1.9348 0.6661 0.7470 -0.3742 -0.5128 0.1301 461 PHE B N 3307 C CA . PHE A 430 ? 1.8862 0.6422 0.7247 -0.3497 -0.4857 0.1244 461 PHE B CA 3308 C C . PHE A 430 ? 1.8667 0.6410 0.6893 -0.3633 -0.4448 0.1201 461 PHE B C 3309 O O . PHE A 430 ? 1.8403 0.6293 0.6700 -0.3549 -0.4215 0.1158 461 PHE B O 3310 C CB . PHE A 430 ? 1.8611 0.6254 0.7353 -0.3213 -0.4948 0.1232 461 PHE B CB 3311 C CG . PHE A 430 ? 1.8427 0.6096 0.7535 -0.2900 -0.5108 0.1202 461 PHE B CG 3312 C CD1 . PHE A 430 ? 1.8229 0.5986 0.7416 -0.2801 -0.4962 0.1164 461 PHE B CD1 3313 C CD2 . PHE A 430 ? 1.8453 0.6064 0.7846 -0.2704 -0.5404 0.1197 461 PHE B CD2 3314 C CE1 . PHE A 430 ? 1.8062 0.5847 0.7602 -0.2516 -0.5104 0.1119 461 PHE B CE1 3315 C CE2 . PHE A 430 ? 1.8285 0.5935 0.8042 -0.2415 -0.5547 0.1144 461 PHE B CE2 3316 C CZ . PHE A 430 ? 1.8089 0.5827 0.7919 -0.2322 -0.5394 0.1103 461 PHE B CZ 3317 N N . ALA A 431 ? 2.0759 0.8494 0.8786 -0.3843 -0.4362 0.1204 462 ALA B N 3318 C CA . ALA A 431 ? 2.0584 0.8501 0.8490 -0.3973 -0.3979 0.1147 462 ALA B CA 3319 C C . ALA A 431 ? 2.0866 0.8714 0.8429 -0.4297 -0.3870 0.1125 462 ALA B C 3320 O O . ALA A 431 ? 2.0755 0.8746 0.8222 -0.4431 -0.3553 0.1061 462 ALA B O 3321 C CB . ALA A 431 ? 2.0539 0.8516 0.8445 -0.4017 -0.3906 0.1145 462 ALA B CB 3322 N N . THR A 432 ? 2.0156 0.7785 0.7546 -0.4426 -0.4139 0.1173 463 THR B N 3323 C CA . THR A 432 ? 2.0442 0.7997 0.7510 -0.4724 -0.4065 0.1153 463 THR B CA 3324 C C . THR A 432 ? 2.0257 0.7910 0.7388 -0.4630 -0.3926 0.1121 463 THR B C 3325 O O . THR A 432 ? 2.0332 0.8032 0.7263 -0.4842 -0.3714 0.1068 463 THR B O 3326 C CB . THR A 432 ? 2.0954 0.8226 0.7782 -0.4917 -0.4421 0.1223 463 THR B CB 3327 O OG1 . THR A 432 ? 2.0957 0.8128 0.7982 -0.4682 -0.4717 0.1278 463 THR B OG1 3328 C CG2 . THR A 432 ? 2.1162 0.8327 0.7909 -0.5035 -0.4555 0.1254 463 THR B CG2 3329 N N . ALA A 433 ? 1.9845 0.7521 0.7264 -0.4319 -0.4050 0.1145 464 ALA B N 3330 C CA . ALA A 433 ? 1.9631 0.7399 0.7163 -0.4182 -0.3934 0.1119 464 ALA B CA 3331 C C . ALA A 433 ? 1.9289 0.7300 0.6865 -0.4180 -0.3520 0.1035 464 ALA B C 3332 O O . ALA A 433 ? 1.8975 0.7143 0.6748 -0.4027 -0.3361 0.1005 464 ALA B O 3333 C CB . ALA A 433 ? 1.9410 0.7179 0.7302 -0.3833 -0.4123 0.1144 464 ALA B CB 3334 N N . PRO A 434 ? 1.8487 0.6528 0.5886 -0.4348 -0.3354 0.0994 465 PRO B N 3335 C CA . PRO A 434 ? 1.8312 0.6542 0.5658 -0.4474 -0.2970 0.0899 465 PRO B CA 3336 C C . PRO A 434 ? 1.7834 0.6286 0.5472 -0.4213 -0.2724 0.0849 465 PRO B C 3337 O O . PRO A 434 ? 1.7639 0.6264 0.5315 -0.4261 -0.2429 0.0779 465 PRO B O 3338 C CB . PRO A 434 ? 1.8570 0.6730 0.5670 -0.4700 -0.2951 0.0880 465 PRO B CB 3339 C CG . PRO A 434 ? 1.8670 0.6687 0.5822 -0.4542 -0.3254 0.0966 465 PRO B CG 3340 C CD . PRO A 434 ? 1.8727 0.6622 0.6011 -0.4392 -0.3549 0.1038 465 PRO B CD 3341 N N . VAL A 435 ? 1.7659 0.6104 0.5512 -0.3955 -0.2834 0.0881 466 VAL B N 3342 C CA . VAL A 435 ? 1.7231 0.5862 0.5358 -0.3724 -0.2606 0.0828 466 VAL B CA 3343 C C . VAL A 435 ? 1.6871 0.5671 0.5403 -0.3393 -0.2659 0.0808 466 VAL B C 3344 O O . VAL A 435 ? 1.6410 0.5560 0.5309 -0.3158 -0.2457 0.0701 466 VAL B O 3345 C CB . VAL A 435 ? 1.7180 0.5789 0.5383 -0.3654 -0.2611 0.0812 466 VAL B CB 3346 C CG1 . VAL A 435 ? 1.7261 0.5949 0.5236 -0.3898 -0.2357 0.0752 466 VAL B CG1 3347 C CG2 . VAL A 435 ? 1.7474 0.5871 0.5618 -0.3644 -0.2971 0.0895 466 VAL B CG2 3348 N N . LEU A 436 ? 1.7701 0.6301 0.6196 -0.3370 -0.2922 0.0893 467 LEU B N 3349 C CA . LEU A 436 ? 1.7390 0.6151 0.6313 -0.3034 -0.3040 0.0863 467 LEU B CA 3350 C C . LEU A 436 ? 1.7046 0.6174 0.6232 -0.2889 -0.2793 0.0775 467 LEU B C 3351 O O . LEU A 436 ? 1.7125 0.6219 0.6165 -0.3009 -0.2766 0.0803 467 LEU B O 3352 C CB . LEU A 436 ? 1.7733 0.6175 0.6544 -0.3063 -0.3399 0.0972 467 LEU B CB 3353 C CG . LEU A 436 ? 1.7432 0.6070 0.6677 -0.2744 -0.3501 0.0926 467 LEU B CG 3354 C CD1 . LEU A 436 ? 1.7241 0.5989 0.6834 -0.2479 -0.3587 0.0863 467 LEU B CD1 3355 C CD2 . LEU A 436 ? 1.7755 0.6110 0.6885 -0.2798 -0.3817 0.1022 467 LEU B CD2 3356 N N . GLN A 437 ? 1.5881 0.5346 0.5456 -0.2630 -0.2632 0.0672 468 GLN B N 3357 C CA . GLN A 437 ? 1.5463 0.5298 0.5296 -0.2496 -0.2366 0.0581 468 GLN B CA 3358 C C . GLN A 437 ? 1.5187 0.5213 0.5379 -0.2230 -0.2447 0.0555 468 GLN B C 3359 O O . GLN A 437 ? 1.4912 0.5193 0.5262 -0.2158 -0.2262 0.0502 468 GLN B O 3360 C CB . GLN A 437 ? 1.5140 0.5241 0.5169 -0.2395 -0.2123 0.0482 468 GLN B CB 3361 C CG . GLN A 437 ? 1.4987 0.5288 0.4969 -0.2506 -0.1799 0.0409 468 GLN B CG 3362 C CD . GLN A 437 ? 1.4847 0.5274 0.4893 -0.2497 -0.1626 0.0337 468 GLN B CD 3363 O OE1 . GLN A 437 ? 1.4471 0.5206 0.4799 -0.2342 -0.1419 0.0245 468 GLN B OE1 3364 N NE2 . GLN A 437 ? 1.5167 0.5346 0.4943 -0.2674 -0.1721 0.0382 468 GLN B NE2 3365 N N . TYR A 438 ? 1.5263 0.5176 0.5594 -0.2087 -0.2722 0.0584 469 TYR B N 3366 C CA . TYR A 438 ? 1.5005 0.5124 0.5697 -0.1836 -0.2800 0.0541 469 TYR B CA 3367 C C . TYR A 438 ? 1.5305 0.5152 0.5971 -0.1818 -0.3157 0.0608 469 TYR B C 3368 O O . TYR A 438 ? 1.5504 0.5145 0.6139 -0.1807 -0.3362 0.0634 469 TYR B O 3369 C CB . TYR A 438 ? 1.4630 0.5056 0.5716 -0.1568 -0.2713 0.0440 469 TYR B CB 3370 C CG . TYR A 438 ? 1.4452 0.5110 0.5922 -0.1312 -0.2800 0.0380 469 TYR B CG 3371 C CD1 . TYR A 438 ? 1.4577 0.5107 0.6184 -0.1195 -0.3098 0.0383 469 TYR B CD1 3372 C CD2 . TYR A 438 ? 1.4169 0.5176 0.5870 -0.1194 -0.2586 0.0314 469 TYR B CD2 3373 C CE1 . TYR A 438 ? 1.4419 0.5187 0.6390 -0.0970 -0.3168 0.0310 469 TYR B CE1 3374 C CE2 . TYR A 438 ? 1.4022 0.5257 0.6061 -0.0981 -0.2656 0.0254 469 TYR B CE2 3375 C CZ . TYR A 438 ? 1.4145 0.5271 0.6323 -0.0870 -0.2940 0.0246 469 TYR B CZ 3376 O OH . TYR A 438 ? 1.4004 0.5380 0.6534 -0.0663 -0.3004 0.0167 469 TYR B OH 3377 N N . LEU A 439 ? 1.5404 0.5256 0.6115 -0.1798 -0.3247 0.0629 470 LEU B N 3378 C CA . LEU A 439 ? 1.5604 0.5212 0.6341 -0.1757 -0.3606 0.0681 470 LEU B CA 3379 C C . LEU A 439 ? 1.5492 0.5348 0.6605 -0.1528 -0.3665 0.0615 470 LEU B C 3380 O O . LEU A 439 ? 1.5464 0.5432 0.6556 -0.1569 -0.3556 0.0621 470 LEU B O 3381 C CB . LEU A 439 ? 1.6088 0.5300 0.6372 -0.2052 -0.3756 0.0810 470 LEU B CB 3382 C CG . LEU A 439 ? 1.6456 0.5337 0.6705 -0.2053 -0.4162 0.0884 470 LEU B CG 3383 C CD1 . LEU A 439 ? 1.6468 0.5289 0.6919 -0.1892 -0.4349 0.0847 470 LEU B CD1 3384 C CD2 . LEU A 439 ? 1.6979 0.5433 0.6711 -0.2388 -0.4297 0.1024 470 LEU B CD2 3385 N N . ASN A 440 ? 1.5449 0.5401 0.6909 -0.1293 -0.3834 0.0542 471 ASN B N 3386 C CA . ASN A 440 ? 1.5382 0.5577 0.7203 -0.1088 -0.3902 0.0468 471 ASN B CA 3387 C C . ASN A 440 ? 1.5552 0.5503 0.7468 -0.1023 -0.4295 0.0483 471 ASN B C 3388 O O . ASN A 440 ? 1.5528 0.5454 0.7643 -0.0882 -0.4456 0.0427 471 ASN B O 3389 C CB . ASN A 440 ? 1.5132 0.5772 0.7365 -0.0838 -0.3709 0.0329 471 ASN B CB 3390 C CG . ASN A 440 ? 1.5076 0.6047 0.7627 -0.0681 -0.3659 0.0250 471 ASN B CG 3391 O OD1 . ASN A 440 ? 1.5208 0.6068 0.7723 -0.0724 -0.3814 0.0290 471 ASN B OD1 3392 N ND2 . ASN A 440 ? 1.4883 0.6259 0.7740 -0.0507 -0.3449 0.0141 471 ASN B ND2 3393 N N . LEU A 441 ? 1.5554 0.5322 0.7334 -0.1126 -0.4455 0.0555 472 LEU B N 3394 C CA . LEU A 441 ? 1.5838 0.5377 0.7729 -0.1064 -0.4844 0.0568 472 LEU B CA 3395 C C . LEU A 441 ? 1.5594 0.5437 0.7894 -0.0854 -0.4887 0.0463 472 LEU B C 3396 O O . LEU A 441 ? 1.5820 0.5499 0.8223 -0.0811 -0.5197 0.0469 472 LEU B O 3397 C CB . LEU A 441 ? 1.6352 0.5416 0.7791 -0.1339 -0.5056 0.0729 472 LEU B CB 3398 C CG . LEU A 441 ? 1.6576 0.5387 0.7592 -0.1572 -0.4965 0.0823 472 LEU B CG 3399 C CD1 . LEU A 441 ? 1.7126 0.5453 0.7686 -0.1857 -0.5205 0.0982 472 LEU B CD1 3400 C CD2 . LEU A 441 ? 1.6552 0.5338 0.7719 -0.1449 -0.5047 0.0771 472 LEU B CD2 3401 N N . SER A 442 ? 1.5537 0.5811 0.8050 -0.0743 -0.4578 0.0373 473 SER B N 3402 C CA . SER A 442 ? 1.5418 0.6006 0.8258 -0.0593 -0.4558 0.0286 473 SER B CA 3403 C C . SER A 442 ? 1.5399 0.6126 0.8694 -0.0346 -0.4801 0.0153 473 SER B C 3404 O O . SER A 442 ? 1.5384 0.6071 0.8823 -0.0239 -0.4917 0.0094 473 SER B O 3405 C CB . SER A 442 ? 1.5207 0.6222 0.8174 -0.0530 -0.4179 0.0217 473 SER B CB 3406 O OG . SER A 442 ? 1.5103 0.6504 0.8531 -0.0291 -0.4171 0.0069 473 SER B OG 3407 N N . THR A 443 ? 1.5887 0.6784 0.9413 -0.0261 -0.4875 0.0098 474 THR B N 3408 C CA . THR A 443 ? 1.5849 0.6964 0.9861 -0.0020 -0.5070 -0.0060 474 THR B CA 3409 C C . THR A 443 ? 1.5978 0.6745 1.0052 0.0021 -0.5480 -0.0059 474 THR B C 3410 O O . THR A 443 ? 1.5912 0.6824 1.0360 0.0224 -0.5608 -0.0204 474 THR B O 3411 C CB . THR A 443 ? 1.5674 0.7243 1.0053 0.0185 -0.4861 -0.0226 474 THR B CB 3412 O OG1 . THR A 443 ? 1.5545 0.7280 0.9732 0.0099 -0.4496 -0.0182 474 THR B OG1 3413 C CG2 . THR A 443 ? 1.5607 0.7585 1.0438 0.0372 -0.4869 -0.0388 474 THR B CG2 3414 N N . ASN A 444 ? 1.8145 0.8451 1.1854 -0.0177 -0.5694 0.0099 475 ASN B N 3415 C CA . ASN A 444 ? 1.8297 0.8209 1.2010 -0.0170 -0.6109 0.0128 475 ASN B CA 3416 C C . ASN A 444 ? 1.8435 0.8174 1.2221 -0.0177 -0.6421 0.0150 475 ASN B C 3417 O O . ASN A 444 ? 1.8400 0.8370 1.2294 -0.0159 -0.6320 0.0121 475 ASN B O 3418 C CB . ASN A 444 ? 1.8435 0.7881 1.1645 -0.0408 -0.6168 0.0301 475 ASN B CB 3419 C CG . ASN A 444 ? 1.8317 0.7849 1.1553 -0.0348 -0.6019 0.0253 475 ASN B CG 3420 O OD1 . ASN A 444 ? 1.8338 0.7659 1.1649 -0.0286 -0.6264 0.0233 475 ASN B OD1 3421 N ND2 . ASN A 444 ? 1.8188 0.8033 1.1379 -0.0360 -0.5622 0.0230 475 ASN B ND2 3422 N N . PHE A 445 ? 1.9150 0.8482 1.2903 -0.0193 -0.6818 0.0195 476 PHE B N 3423 C CA . PHE A 445 ? 1.9316 0.8409 1.3119 -0.0211 -0.7173 0.0230 476 PHE B CA 3424 C C . PHE A 445 ? 1.9767 0.8327 1.3028 -0.0510 -0.7362 0.0458 476 PHE B C 3425 O O . PHE A 445 ? 2.0084 0.8364 1.3383 -0.0523 -0.7732 0.0495 476 PHE B O 3426 C CB . PHE A 445 ? 1.9326 0.8485 1.3660 0.0050 -0.7503 0.0057 476 PHE B CB 3427 C CG . PHE A 445 ? 1.9062 0.8822 1.3935 0.0304 -0.7309 -0.0169 476 PHE B CG 3428 C CD1 . PHE A 445 ? 1.8910 0.9067 1.3981 0.0436 -0.7004 -0.0296 476 PHE B CD1 3429 C CD2 . PHE A 445 ? 1.9008 0.8948 1.4158 0.0386 -0.7410 -0.0246 476 PHE B CD2 3430 C CE1 . PHE A 445 ? 1.8722 0.9436 1.4253 0.0641 -0.6815 -0.0498 476 PHE B CE1 3431 C CE2 . PHE A 445 ? 1.8811 0.9321 1.4436 0.0596 -0.7216 -0.0455 476 PHE B CE2 3432 C CZ . PHE A 445 ? 1.8673 0.9569 1.4480 0.0717 -0.6917 -0.0579 476 PHE B CZ 3433 N N . PHE A 446 ? 2.0068 0.8497 1.2837 -0.0752 -0.7111 0.0601 477 PHE B N 3434 C CA . PHE A 446 ? 2.0545 0.8444 1.2737 -0.1070 -0.7269 0.0818 477 PHE B CA 3435 C C . PHE A 446 ? 2.0860 0.8573 1.3026 -0.1182 -0.7533 0.0861 477 PHE B C 3436 O O . PHE A 446 ? 2.1238 0.8687 1.3380 -0.1294 -0.7823 0.0871 477 PHE B O 3437 C CB . PHE A 446 ? 2.0428 0.8396 1.2195 -0.1296 -0.6867 0.0912 477 PHE B CB 3438 C CG . PHE A 446 ? 2.0188 0.8323 1.1920 -0.1275 -0.6580 0.0870 477 PHE B CG 3439 C CD1 . PHE A 446 ? 2.0278 0.8272 1.2108 -0.1189 -0.6749 0.0839 477 PHE B CD1 3440 C CD2 . PHE A 446 ? 1.9882 0.8310 1.1493 -0.1337 -0.6150 0.0859 477 PHE B CD2 3441 C CE1 . PHE A 446 ? 2.0056 0.8207 1.1857 -0.1169 -0.6485 0.0800 477 PHE B CE1 3442 C CE2 . PHE A 446 ? 1.9663 0.8246 1.1257 -0.1314 -0.5892 0.0818 477 PHE B CE2 3443 C CZ . PHE A 446 ? 1.9748 0.8196 1.1433 -0.1232 -0.6056 0.0790 477 PHE B CZ 3444 N N . HIS A 447 ? 1.9041 0.6903 1.1207 -0.1168 -0.7427 0.0883 478 HIS B N 3445 C CA . HIS A 447 ? 1.9319 0.7017 1.1446 -0.1296 -0.7626 0.0927 478 HIS B CA 3446 C C . HIS A 447 ? 1.9722 0.7092 1.1351 -0.1678 -0.7616 0.1058 478 HIS B C 3447 O O . HIS A 447 ? 2.0116 0.7210 1.1713 -0.1809 -0.7905 0.1084 478 HIS B O 3448 C CB . HIS A 447 ? 1.9470 0.7109 1.2063 -0.1101 -0.8026 0.0817 478 HIS B CB 3449 C CG . HIS A 447 ? 1.9085 0.7125 1.2185 -0.0756 -0.8054 0.0665 478 HIS B CG 3450 N ND1 . HIS A 447 ? 1.8994 0.7175 1.2616 -0.0481 -0.8263 0.0489 478 HIS B ND1 3451 C CD2 . HIS A 447 ? 1.8716 0.7195 1.2010 -0.0680 -0.7775 0.0580 478 HIS B CD2 3452 C CE1 . HIS A 447 ? 1.8581 0.7278 1.2685 -0.0257 -0.8105 0.0302 478 HIS B CE1 3453 N NE2 . HIS A 447 ? 1.8421 0.7302 1.2331 -0.0375 -0.7813 0.0359 478 HIS B NE2 3454 N N . ARG A 448 ? 1.9836 0.7256 1.1086 -0.1855 -0.7282 0.1127 479 ARG B N 3455 C CA . ARG A 448 ? 2.0163 0.7357 1.0927 -0.2222 -0.7213 0.1230 479 ARG B CA 3456 C C . ARG A 448 ? 1.9899 0.7286 1.0382 -0.2332 -0.6781 0.1270 479 ARG B C 3457 O O . ARG A 448 ? 1.9518 0.7173 1.0176 -0.2140 -0.6586 0.1233 479 ARG B O 3458 C CB . ARG A 448 ? 2.0450 0.7436 1.1063 -0.2346 -0.7362 0.1241 479 ARG B CB 3459 C CG . ARG A 448 ? 2.0978 0.7630 1.1290 -0.2655 -0.7599 0.1316 479 ARG B CG 3460 C CD . ARG A 448 ? 2.1197 0.7695 1.1773 -0.2582 -0.7951 0.1299 479 ARG B CD 3461 N NE . ARG A 448 ? 2.1198 0.7677 1.2215 -0.2318 -0.8250 0.1202 479 ARG B NE 3462 C CZ . ARG A 448 ? 2.1611 0.7808 1.2688 -0.2379 -0.8628 0.1194 479 ARG B CZ 3463 N NH1 . ARG A 448 ? 2.2071 0.7968 1.2775 -0.2705 -0.8766 0.1289 479 ARG B NH1 3464 N NH2 . ARG A 448 ? 2.1573 0.7791 1.3091 -0.2118 -0.8876 0.1083 479 ARG B NH2 3465 N N . LYS A 449 ? 2.1421 0.8684 1.1476 -0.2644 -0.6637 0.1333 480 LYS B N 3466 C CA . LYS A 449 ? 2.1216 0.8648 1.1011 -0.2778 -0.6238 0.1356 480 LYS B CA 3467 C C . LYS A 449 ? 2.1193 0.8648 1.0722 -0.2924 -0.5995 0.1358 480 LYS B C 3468 O O . LYS A 449 ? 2.1437 0.8724 1.0873 -0.3007 -0.6151 0.1366 480 LYS B O 3469 C CB . LYS A 449 ? 2.1463 0.8782 1.1002 -0.3034 -0.6236 0.1413 480 LYS B CB 3470 C CG . LYS A 449 ? 2.1825 0.8892 1.1461 -0.3062 -0.6637 0.1439 480 LYS B CG 3471 C CD . LYS A 449 ? 2.1853 0.8933 1.1459 -0.3131 -0.6621 0.1472 480 LYS B CD 3472 C CE . LYS A 449 ? 2.2158 0.9014 1.1951 -0.3098 -0.7025 0.1488 480 LYS B CE 3473 N NZ . LYS A 449 ? 2.2187 0.9055 1.1951 -0.3165 -0.7007 0.1525 480 LYS B NZ 3474 N N . LEU A 450 ? 1.8631 0.6298 0.8044 -0.2958 -0.5619 0.1346 481 LEU B N 3475 C CA . LEU A 450 ? 1.8564 0.6291 0.7755 -0.3085 -0.5347 0.1332 481 LEU B CA 3476 C C . LEU A 450 ? 1.8971 0.6495 0.7764 -0.3443 -0.5367 0.1369 481 LEU B C 3477 O O . LEU A 450 ? 1.9252 0.6631 0.7895 -0.3621 -0.5496 0.1406 481 LEU B O 3478 C CB . LEU A 450 ? 1.8187 0.6187 0.7369 -0.3045 -0.4956 0.1302 481 LEU B CB 3479 C CG . LEU A 450 ? 1.7778 0.6003 0.7311 -0.2707 -0.4899 0.1264 481 LEU B CG 3480 C CD1 . LEU A 450 ? 1.7720 0.6020 0.7408 -0.2603 -0.4987 0.1273 481 LEU B CD1 3481 C CD2 . LEU A 450 ? 1.7437 0.5926 0.6964 -0.2667 -0.4512 0.1211 481 LEU B CD2 3482 N N . PRO A 451 ? 1.9466 0.6973 0.8082 -0.3554 -0.5250 0.1356 482 PRO B N 3483 C CA . PRO A 451 ? 1.9857 0.7192 0.8078 -0.3910 -0.5251 0.1381 482 PRO B CA 3484 C C . PRO A 451 ? 1.9797 0.7256 0.7789 -0.4121 -0.4914 0.1356 482 PRO B C 3485 O O . PRO A 451 ? 1.9417 0.7116 0.7538 -0.3990 -0.4633 0.1315 482 PRO B O 3486 C CB . PRO A 451 ? 1.9896 0.7201 0.8043 -0.3928 -0.5232 0.1367 482 PRO B CB 3487 C CG . PRO A 451 ? 1.9431 0.6967 0.7877 -0.3627 -0.5053 0.1320 482 PRO B CG 3488 C CD . PRO A 451 ? 1.9233 0.6838 0.8010 -0.3366 -0.5181 0.1320 482 PRO B CD 3489 N N . GLU A 452 ? 2.1596 0.8891 0.9255 -0.4446 -0.4950 0.1376 483 GLU B N 3490 C CA . GLU A 452 ? 2.1579 0.8982 0.9014 -0.4673 -0.4632 0.1335 483 GLU B CA 3491 C C . GLU A 452 ? 2.1378 0.8939 0.8769 -0.4687 -0.4336 0.1273 483 GLU B C 3492 O O . GLU A 452 ? 2.1159 0.8916 0.8524 -0.4737 -0.4001 0.1213 483 GLU B O 3493 C CB . GLU A 452 ? 2.2086 0.9255 0.9168 -0.5033 -0.4765 0.1365 483 GLU B CB 3494 C CG . GLU A 452 ? 2.2115 0.9367 0.9017 -0.5253 -0.4513 0.1328 483 GLU B CG 3495 C CD . GLU A 452 ? 2.2623 0.9619 0.9237 -0.5561 -0.4724 0.1373 483 GLU B CD 3496 O OE1 . GLU A 452 ? 2.2647 0.9676 0.9201 -0.5666 -0.4633 0.1367 483 GLU B OE1 3497 O OE2 . GLU A 452 ? 2.3009 0.9767 0.9451 -0.5703 -0.4987 0.1416 483 GLU B OE2 3498 N N . ASN A 453 ? 2.0973 0.8446 0.8373 -0.4636 -0.4473 0.1286 484 ASN B N 3499 C CA . ASN A 453 ? 2.0828 0.8414 0.8183 -0.4650 -0.4243 0.1234 484 ASN B CA 3500 C C . ASN A 453 ? 2.0315 0.8179 0.7941 -0.4388 -0.3966 0.1183 484 ASN B C 3501 O O . ASN A 453 ? 2.0149 0.8160 0.7731 -0.4435 -0.3679 0.1123 484 ASN B O 3502 C CB . ASN A 453 ? 2.1013 0.8439 0.8363 -0.4606 -0.4497 0.1269 484 ASN B CB 3503 C CG . ASN A 453 ? 2.1547 0.8717 0.8545 -0.4933 -0.4695 0.1305 484 ASN B CG 3504 O OD1 . ASN A 453 ? 2.1813 0.8888 0.8601 -0.5170 -0.4717 0.1316 484 ASN B OD1 3505 N ND2 . ASN A 453 ? 2.1720 0.8776 0.8645 -0.4953 -0.4842 0.1323 484 ASN B ND2 3506 N N . ILE A 454 ? 1.8548 0.6483 0.6452 -0.4124 -0.4057 0.1205 485 ILE B N 3507 C CA . ILE A 454 ? 1.8095 0.6250 0.6296 -0.3819 -0.3903 0.1173 485 ILE B CA 3508 C C . ILE A 454 ? 1.7789 0.6189 0.5979 -0.3831 -0.3500 0.1103 485 ILE B C 3509 O O . ILE A 454 ? 1.7552 0.6067 0.5859 -0.3690 -0.3370 0.1071 485 ILE B O 3510 C CB . ILE A 454 ? 1.7919 0.6122 0.6400 -0.3566 -0.4053 0.1200 485 ILE B CB 3511 C CG1 . ILE A 454 ? 1.7504 0.5902 0.6289 -0.3249 -0.3949 0.1170 485 ILE B CG1 3512 C CG2 . ILE A 454 ? 1.7885 0.6171 0.6307 -0.3655 -0.3929 0.1197 485 ILE B CG2 3513 C CD1 . ILE A 454 ? 1.7514 0.5837 0.6394 -0.3136 -0.4072 0.1167 485 ILE B CD1 3514 N N . TRP A 455 ? 1.8123 0.6601 0.6182 -0.4002 -0.3307 0.1072 486 TRP B N 3515 C CA . TRP A 455 ? 1.7819 0.6548 0.5912 -0.3991 -0.2936 0.0995 486 TRP B CA 3516 C C . TRP A 455 ? 1.7952 0.6681 0.5832 -0.4237 -0.2736 0.0936 486 TRP B C 3517 O O . TRP A 455 ? 1.7750 0.6677 0.5643 -0.4271 -0.2425 0.0858 486 TRP B O 3518 C CB . TRP A 455 ? 1.7709 0.6562 0.5826 -0.4008 -0.2809 0.0976 486 TRP B CB 3519 C CG . TRP A 455 ? 1.7644 0.6472 0.5940 -0.3811 -0.3031 0.1038 486 TRP B CG 3520 C CD1 . TRP A 455 ? 1.7859 0.6566 0.6085 -0.3908 -0.3198 0.1081 486 TRP B CD1 3521 C CD2 . TRP A 455 ? 1.7354 0.6282 0.5935 -0.3489 -0.3111 0.1056 486 TRP B CD2 3522 N NE1 . TRP A 455 ? 1.7717 0.6447 0.6175 -0.3667 -0.3375 0.1124 486 TRP B NE1 3523 C CE2 . TRP A 455 ? 1.7412 0.6280 0.6092 -0.3409 -0.3325 0.1107 486 TRP B CE2 3524 C CE3 . TRP A 455 ? 1.7080 0.6162 0.5866 -0.3263 -0.3019 0.1022 486 TRP B CE3 3525 C CZ2 . TRP A 455 ? 1.7208 0.6178 0.6193 -0.3112 -0.3446 0.1115 486 TRP B CZ2 3526 C CZ3 . TRP A 455 ? 1.6823 0.6112 0.6047 -0.2954 -0.3111 0.0982 486 TRP B CZ3 3527 C CH2 . TRP A 455 ? 1.6892 0.6131 0.6214 -0.2883 -0.3318 0.1023 486 TRP B CH2 3528 N N . LYS A 456 ? 1.9307 0.7817 0.7000 -0.4408 -0.2925 0.0969 487 LYS B N 3529 C CA . LYS A 456 ? 1.9505 0.7983 0.6972 -0.4679 -0.2775 0.0919 487 LYS B CA 3530 C C . LYS A 456 ? 1.9370 0.7895 0.6904 -0.4579 -0.2710 0.0896 487 LYS B C 3531 O O . LYS A 456 ? 1.9514 0.8021 0.6887 -0.4783 -0.2586 0.0854 487 LYS B O 3532 C CB . LYS A 456 ? 2.0004 0.8213 0.7190 -0.4956 -0.3020 0.0966 487 LYS B CB 3533 C CG . LYS A 456 ? 2.0198 0.8343 0.7266 -0.5118 -0.3064 0.0981 487 LYS B CG 3534 C CD . LYS A 456 ? 2.0526 0.8607 0.7299 -0.5501 -0.2931 0.0937 487 LYS B CD 3535 C CE . LYS A 456 ? 2.0303 0.8607 0.7117 -0.5565 -0.2537 0.0840 487 LYS B CE 3536 N NZ . LYS A 456 ? 2.0596 0.8870 0.7173 -0.5933 -0.2379 0.0793 487 LYS B NZ 3537 N N . ALA A 457 ? 1.8349 0.6936 0.6128 -0.4268 -0.2792 0.0922 488 ALA B N 3538 C CA . ALA A 457 ? 1.8229 0.6837 0.6089 -0.4144 -0.2778 0.0913 488 ALA B CA 3539 C C . ALA A 457 ? 1.8037 0.6834 0.5885 -0.4203 -0.2429 0.0824 488 ALA B C 3540 O O . ALA A 457 ? 1.7710 0.6740 0.5703 -0.4080 -0.2189 0.0769 488 ALA B O 3541 C CB . ALA A 457 ? 1.9613 0.8271 0.7769 -0.3797 -0.2906 0.0949 488 ALA B CB 3542 N N . PRO A 458 ? 1.8400 0.7108 0.6085 -0.4380 -0.2416 0.0808 489 PRO B N 3543 C CA . PRO A 458 ? 1.8331 0.7185 0.5958 -0.4535 -0.2092 0.0724 489 PRO B CA 3544 C C . PRO A 458 ? 1.7888 0.7012 0.5748 -0.4288 -0.1856 0.0659 489 PRO B C 3545 O O . PRO A 458 ? 1.7698 0.7052 0.5615 -0.4315 -0.1580 0.0571 489 PRO B O 3546 C CB . PRO A 458 ? 1.8609 0.7291 0.6067 -0.4688 -0.2209 0.0739 489 PRO B CB 3547 C CG . PRO A 458 ? 1.8922 0.7355 0.6265 -0.4699 -0.2600 0.0825 489 PRO B CG 3548 C CD . PRO A 458 ? 1.8691 0.7168 0.6269 -0.4411 -0.2724 0.0871 489 PRO B CD 3549 N N . ASN A 459 ? 1.9735 0.8850 0.7737 -0.4041 -0.1974 0.0687 490 ASN B N 3550 C CA . ASN A 459 ? 1.9250 0.8690 0.7612 -0.3747 -0.1795 0.0598 490 ASN B CA 3551 C C . ASN A 459 ? 1.9130 0.8564 0.7783 -0.3460 -0.2029 0.0652 490 ASN B C 3552 O O . ASN A 459 ? 1.9179 0.8499 0.7903 -0.3359 -0.2212 0.0692 490 ASN B O 3553 C CB . ASN A 459 ? 1.9107 0.8693 0.7590 -0.3699 -0.1641 0.0517 490 ASN B CB 3554 C CG . ASN A 459 ? 1.9271 0.8864 0.7467 -0.3998 -0.1420 0.0450 490 ASN B CG 3555 O OD1 . ASN A 459 ? 1.9075 0.8925 0.7383 -0.4007 -0.1149 0.0332 490 ASN B OD1 3556 N ND2 . ASN A 459 ? 1.9629 0.8988 0.7571 -0.4229 -0.1522 0.0518 490 ASN B ND2 3557 N N . LEU A 460 ? 1.6149 0.5716 0.4981 -0.3333 -0.2020 0.0644 491 LEU B N 3558 C CA . LEU A 460 ? 1.5949 0.5577 0.5104 -0.3049 -0.2207 0.0667 491 LEU B CA 3559 C C . LEU A 460 ? 1.5532 0.5506 0.4999 -0.2871 -0.2003 0.0583 491 LEU B C 3560 O O . LEU A 460 ? 1.5583 0.5573 0.4930 -0.2988 -0.1914 0.0582 491 LEU B O 3561 C CB . LEU A 460 ? 1.6306 0.5627 0.5266 -0.3137 -0.2511 0.0784 491 LEU B CB 3562 C CG . LEU A 460 ? 1.6120 0.5523 0.5413 -0.2869 -0.2697 0.0794 491 LEU B CG 3563 C CD1 . LEU A 460 ? 1.5819 0.5399 0.5488 -0.2586 -0.2732 0.0735 491 LEU B CD1 3564 C CD2 . LEU A 460 ? 1.6535 0.5579 0.5625 -0.2966 -0.3045 0.0912 491 LEU B CD2 3565 N N . GLN A 461 ? 1.5268 0.5509 0.5127 -0.2593 -0.1944 0.0517 492 GLN B N 3566 C CA . GLN A 461 ? 1.5029 0.5609 0.5196 -0.2420 -0.1749 0.0439 492 GLN B CA 3567 C C . GLN A 461 ? 1.5002 0.5659 0.5407 -0.2225 -0.1908 0.0462 492 GLN B C 3568 O O . GLN A 461 ? 1.4989 0.5707 0.5389 -0.2252 -0.1861 0.0466 492 GLN B O 3569 C CB . GLN A 461 ? 1.4803 0.5660 0.5230 -0.2272 -0.1538 0.0342 492 GLN B CB 3570 C CG . GLN A 461 ? 1.4839 0.5646 0.5046 -0.2475 -0.1364 0.0303 492 GLN B CG 3571 C CD . GLN A 461 ? 1.4576 0.5662 0.5050 -0.2334 -0.1151 0.0203 492 GLN B CD 3572 O OE1 . GLN A 461 ? 1.4404 0.5708 0.5009 -0.2308 -0.0939 0.0129 492 GLN B OE1 3573 N NE2 . GLN A 461 ? 1.4543 0.5615 0.5100 -0.2244 -0.1216 0.0200 492 GLN B NE2 3574 N N . ILE A 462 ? 1.4822 0.5491 0.5446 -0.2030 -0.2092 0.0466 493 ILE B N 3575 C CA . ILE A 462 ? 1.4770 0.5549 0.5656 -0.1839 -0.2235 0.0466 493 ILE B CA 3576 C C . ILE A 462 ? 1.5023 0.5497 0.5783 -0.1883 -0.2569 0.0550 493 ILE B C 3577 O O . ILE A 462 ? 1.5206 0.5443 0.5844 -0.1930 -0.2746 0.0590 493 ILE B O 3578 C CB . ILE A 462 ? 1.4531 0.5617 0.5833 -0.1556 -0.2193 0.0381 493 ILE B CB 3579 C CG1 . ILE A 462 ? 1.4313 0.5629 0.5700 -0.1531 -0.1907 0.0311 493 ILE B CG1 3580 C CG2 . ILE A 462 ? 1.4427 0.5740 0.6014 -0.1381 -0.2224 0.0350 493 ILE B CG2 3581 C CD1 . ILE A 462 ? 1.4096 0.5689 0.5846 -0.1283 -0.1868 0.0237 493 ILE B CD1 3582 N N . PHE A 463 ? 1.5370 0.5841 0.6163 -0.1870 -0.2665 0.0577 494 PHE B N 3583 C CA . PHE A 463 ? 1.5566 0.5762 0.6284 -0.1892 -0.3000 0.0650 494 PHE B CA 3584 C C . PHE A 463 ? 1.5531 0.5908 0.6575 -0.1690 -0.3113 0.0614 494 PHE B C 3585 O O . PHE A 463 ? 1.5489 0.6011 0.6562 -0.1703 -0.2997 0.0607 494 PHE B O 3586 C CB . PHE A 463 ? 1.5762 0.5626 0.6033 -0.2191 -0.3068 0.0754 494 PHE B CB 3587 C CG . PHE A 463 ? 1.5964 0.5531 0.6142 -0.2230 -0.3420 0.0839 494 PHE B CG 3588 C CD1 . PHE A 463 ? 1.6193 0.5446 0.6244 -0.2278 -0.3691 0.0900 494 PHE B CD1 3589 C CD2 . PHE A 463 ? 1.6007 0.5592 0.6219 -0.2227 -0.3490 0.0861 494 PHE B CD2 3590 C CE1 . PHE A 463 ? 1.6539 0.5497 0.6511 -0.2315 -0.4038 0.0981 494 PHE B CE1 3591 C CE2 . PHE A 463 ? 1.6222 0.5525 0.6356 -0.2264 -0.3827 0.0939 494 PHE B CE2 3592 C CZ . PHE A 463 ? 1.6551 0.5537 0.6570 -0.2306 -0.4107 0.0999 494 PHE B CZ 3593 N N . SER A 464 ? 1.5212 0.5585 0.6505 -0.1509 -0.3342 0.0585 495 SER B N 3594 C CA . SER A 464 ? 1.5116 0.5679 0.6737 -0.1322 -0.3455 0.0533 495 SER B CA 3595 C C . SER A 464 ? 1.5368 0.5676 0.7030 -0.1286 -0.3834 0.0567 495 SER B C 3596 O O . SER A 464 ? 1.5396 0.5659 0.7228 -0.1159 -0.4004 0.0527 495 SER B O 3597 C CB . SER A 464 ? 1.4777 0.5759 0.6823 -0.1065 -0.3305 0.0406 495 SER B CB 3598 O OG . SER A 464 ? 1.4642 0.5887 0.6989 -0.0914 -0.3323 0.0344 495 SER B OG 3599 N N . ALA A 465 ? 1.6603 0.6757 0.8133 -0.1389 -0.3969 0.0632 496 ALA B N 3600 C CA . ALA A 465 ? 1.6767 0.6710 0.8383 -0.1339 -0.4337 0.0656 496 ALA B CA 3601 C C . ALA A 465 ? 1.6702 0.6958 0.8734 -0.1124 -0.4376 0.0559 496 ALA B C 3602 O O . ALA A 465 ? 1.6827 0.6949 0.8967 -0.1077 -0.4669 0.0565 496 ALA B O 3603 C CB . ALA A 465 ? 1.6978 0.6498 0.8159 -0.1608 -0.4510 0.0801 496 ALA B CB 3604 N N . SER A 466 ? 1.5045 0.5714 0.7299 -0.1009 -0.4083 0.0471 497 SER B N 3605 C CA . SER A 466 ? 1.4869 0.5878 0.7477 -0.0842 -0.4056 0.0381 497 SER B CA 3606 C C . SER A 466 ? 1.4880 0.5975 0.7882 -0.0628 -0.4326 0.0280 497 SER B C 3607 O O . SER A 466 ? 1.4824 0.5970 0.8017 -0.0494 -0.4388 0.0206 497 SER B O 3608 C CB . SER A 466 ? 1.4525 0.5958 0.7321 -0.0742 -0.3712 0.0296 497 SER B CB 3609 O OG . SER A 466 ? 1.4369 0.5968 0.7393 -0.0584 -0.3672 0.0206 497 SER B OG 3610 N N . PHE A 467 ? 1.4949 0.6072 0.8084 -0.0595 -0.4481 0.0268 498 PHE B N 3611 C CA . PHE A 467 ? 1.4951 0.6193 0.8501 -0.0389 -0.4736 0.0152 498 PHE B CA 3612 C C . PHE A 467 ? 1.5205 0.6089 0.8746 -0.0371 -0.5097 0.0171 498 PHE B C 3613 O O . PHE A 467 ? 1.5158 0.6177 0.9089 -0.0168 -0.5274 0.0041 498 PHE B O 3614 C CB . PHE A 467 ? 1.4630 0.6360 0.8614 -0.0160 -0.4562 -0.0020 498 PHE B CB 3615 C CG . PHE A 467 ? 1.4409 0.6510 0.8495 -0.0144 -0.4293 -0.0059 498 PHE B CG 3616 C CD1 . PHE A 467 ? 1.4428 0.6661 0.8690 -0.0106 -0.4384 -0.0095 498 PHE B CD1 3617 C CD2 . PHE A 467 ? 1.4197 0.6501 0.8194 -0.0176 -0.3960 -0.0053 498 PHE B CD2 3618 C CE1 . PHE A 467 ? 1.4239 0.6802 0.8578 -0.0106 -0.4141 -0.0123 498 PHE B CE1 3619 C CE2 . PHE A 467 ? 1.4011 0.6633 0.8089 -0.0173 -0.3727 -0.0079 498 PHE B CE2 3620 C CZ . PHE A 467 ? 1.4034 0.6785 0.8276 -0.0141 -0.3816 -0.0111 498 PHE B CZ 3621 N N . SER A 468 ? 1.8793 0.9224 1.1899 -0.0588 -0.5217 0.0326 499 SER B N 3622 C CA . SER A 468 ? 1.8964 0.9021 1.2059 -0.0589 -0.5617 0.0361 499 SER B CA 3623 C C . SER A 468 ? 1.9127 0.8885 1.1979 -0.0757 -0.5817 0.0481 499 SER B C 3624 O O . SER A 468 ? 1.9236 0.8642 1.1609 -0.1011 -0.5822 0.0638 499 SER B O 3625 C CB . SER A 468 ? 1.9050 0.8760 1.1784 -0.0742 -0.5642 0.0465 499 SER B CB 3626 O OG . SER A 468 ? 1.9163 0.8640 1.1395 -0.1023 -0.5509 0.0619 499 SER B OG 3627 N N . ASN A 469 ? 1.7726 0.7631 1.0901 -0.0624 -0.5977 0.0402 500 ASN B N 3628 C CA . ASN A 469 ? 1.7926 0.7484 1.1001 -0.0711 -0.6334 0.0486 500 ASN B CA 3629 C C . ASN A 469 ? 1.8124 0.7218 1.0597 -0.1034 -0.6383 0.0696 500 ASN B C 3630 O O . ASN A 469 ? 1.8425 0.7083 1.0709 -0.1143 -0.6731 0.0797 500 ASN B O 3631 C CB . ASN A 469 ? 1.7965 0.7388 1.1372 -0.0537 -0.6731 0.0402 500 ASN B CB 3632 C CG . ASN A 469 ? 1.7750 0.7673 1.1779 -0.0232 -0.6695 0.0174 500 ASN B CG 3633 O OD1 . ASN A 469 ? 1.7251 0.7610 1.1449 -0.0137 -0.6350 0.0076 500 ASN B OD1 3634 N ND2 . ASN A 469 ? 1.8128 0.7996 1.2503 -0.0087 -0.7053 0.0085 500 ASN B ND2 3635 N N . LEU A 470 ? 1.6827 0.6019 0.9002 -0.1190 -0.6032 0.0757 501 LEU B N 3636 C CA . LEU A 470 ? 1.7110 0.5921 0.8710 -0.1510 -0.6018 0.0934 501 LEU B CA 3637 C C . LEU A 470 ? 1.7291 0.5998 0.8771 -0.1622 -0.6127 0.1003 501 LEU B C 3638 O O . LEU A 470 ? 1.7033 0.6049 0.8859 -0.1461 -0.6098 0.0910 501 LEU B O 3639 C CB . LEU A 470 ? 1.6870 0.5849 0.8234 -0.1624 -0.5595 0.0947 501 LEU B CB 3640 C CG . LEU A 470 ? 1.6907 0.5776 0.8100 -0.1680 -0.5504 0.0964 501 LEU B CG 3641 C CD1 . LEU A 470 ? 1.6661 0.5767 0.7704 -0.1761 -0.5075 0.0949 501 LEU B CD1 3642 C CD2 . LEU A 470 ? 1.7471 0.5802 0.8211 -0.1933 -0.5768 0.1118 501 LEU B CD2 3643 N N . ILE A 471 ? 1.8951 0.7223 0.9934 -0.1909 -0.6258 0.1167 502 ILE B N 3644 C CA . ILE A 471 ? 1.9150 0.7286 0.9959 -0.2049 -0.6361 0.1248 502 ILE B CA 3645 C C . ILE A 471 ? 1.9387 0.7314 0.9716 -0.2406 -0.6189 0.1341 502 ILE B C 3646 O O . ILE A 471 ? 1.9488 0.7309 0.9620 -0.2535 -0.6106 0.1353 502 ILE B O 3647 C CB . ILE A 471 ? 1.9420 0.7354 1.0475 -0.1973 -0.6794 0.1238 502 ILE B CB 3648 C CG1 . ILE A 471 ? 1.9662 0.7453 1.0578 -0.2157 -0.6877 0.1305 502 ILE B CG1 3649 C CG2 . ILE A 471 ? 1.9742 0.7378 1.0773 -0.2045 -0.7019 0.1244 502 ILE B CG2 3650 C CD1 . ILE A 471 ? 1.9388 0.7478 1.0382 -0.2069 -0.6722 0.1284 502 ILE B CD1 3651 N N . GLY A 472 ? 1.9471 0.7392 0.9635 -0.2562 -0.6112 0.1385 503 GLY B N 3652 C CA . GLY A 472 ? 1.9750 0.7492 0.9508 -0.2907 -0.5994 0.1444 503 GLY B CA 3653 C C . GLY A 472 ? 1.9519 0.7461 0.9048 -0.3023 -0.5580 0.1437 503 GLY B C 3654 O O . GLY A 472 ? 1.9137 0.7348 0.8800 -0.2841 -0.5364 0.1394 503 GLY B O 3655 N N . GLU A 473 ? 2.0340 0.8152 0.9527 -0.3332 -0.5478 0.1470 504 GLU B N 3656 C CA . GLU A 473 ? 2.0173 0.8154 0.9140 -0.3476 -0.5094 0.1447 504 GLU B CA 3657 C C . GLU A 473 ? 1.9965 0.8067 0.8913 -0.3424 -0.4873 0.1402 504 GLU B C 3658 O O . GLU A 473 ? 2.0072 0.8054 0.9058 -0.3381 -0.5026 0.1402 504 GLU B O 3659 C CB . GLU A 473 ? 2.0542 0.8337 0.9154 -0.3829 -0.5074 0.1475 504 GLU B CB 3660 C CG . GLU A 473 ? 2.0946 0.8466 0.9524 -0.3937 -0.5427 0.1536 504 GLU B CG 3661 C CD . GLU A 473 ? 2.0915 0.8492 0.9532 -0.3943 -0.5419 0.1557 504 GLU B CD 3662 O OE1 . GLU A 473 ? 2.1235 0.8592 0.9828 -0.4035 -0.5692 0.1607 504 GLU B OE1 3663 O OE2 . GLU A 473 ? 2.0579 0.8416 0.9250 -0.3861 -0.5144 0.1523 504 GLU B OE2 3664 N N . ILE A 474 ? 1.7925 0.6264 0.6826 -0.3423 -0.4522 0.1359 505 ILE B N 3665 C CA . ILE A 474 ? 1.7729 0.6189 0.6601 -0.3394 -0.4286 0.1312 505 ILE B CA 3666 C C . ILE A 474 ? 1.7940 0.6323 0.6486 -0.3705 -0.4110 0.1294 505 ILE B C 3667 O O . ILE A 474 ? 1.7892 0.6378 0.6310 -0.3842 -0.3881 0.1266 505 ILE B O 3668 C CB . ILE A 474 ? 1.7300 0.6075 0.6325 -0.3209 -0.4000 0.1263 505 ILE B CB 3669 C CG1 . ILE A 474 ? 1.7062 0.6011 0.6493 -0.2880 -0.4133 0.1233 505 ILE B CG1 3670 C CG2 . ILE A 474 ? 1.7139 0.6031 0.6091 -0.3235 -0.3722 0.1210 505 ILE B CG2 3671 C CD1 . ILE A 474 ? 1.6736 0.6145 0.6509 -0.2686 -0.3813 0.1112 505 ILE B CD1 3672 N N . PRO A 475 ? 1.8166 0.6378 0.6583 -0.3815 -0.4215 0.1302 506 PRO B N 3673 C CA . PRO A 475 ? 1.8438 0.6545 0.6530 -0.4130 -0.4105 0.1285 506 PRO B CA 3674 C C . PRO A 475 ? 1.8220 0.6545 0.6221 -0.4220 -0.3706 0.1212 506 PRO B C 3675 O O . PRO A 475 ? 1.7871 0.6400 0.6034 -0.4037 -0.3512 0.1170 506 PRO B O 3676 C CB . PRO A 475 ? 1.8549 0.6539 0.6626 -0.4110 -0.4230 0.1291 506 PRO B CB 3677 C CG . PRO A 475 ? 1.8250 0.6340 0.6667 -0.3764 -0.4325 0.1294 506 PRO B CG 3678 C CD . PRO A 475 ? 1.8185 0.6301 0.6776 -0.3634 -0.4457 0.1322 506 PRO B CD 3679 N N . ASN A 476 ? 2.1202 0.9478 0.8956 -0.4501 -0.3597 0.1192 507 ASN B N 3680 C CA . ASN A 476 ? 2.1028 0.9504 0.8712 -0.4603 -0.3230 0.1110 507 ASN B CA 3681 C C . ASN A 476 ? 2.0909 0.9471 0.8580 -0.4604 -0.3042 0.1053 507 ASN B C 3682 O O . ASN A 476 ? 2.1159 0.9556 0.8689 -0.4727 -0.3161 0.1070 507 ASN B O 3683 C CB . ASN A 476 ? 2.1352 0.9725 0.8763 -0.4932 -0.3180 0.1094 507 ASN B CB 3684 C CG . ASN A 476 ? 2.1441 0.9759 0.8866 -0.4938 -0.3319 0.1141 507 ASN B CG 3685 O OD1 . ASN A 476 ? 2.1484 0.9696 0.9032 -0.4791 -0.3597 0.1212 507 ASN B OD1 3686 N ND2 . ASN A 476 ? 2.1471 0.9862 0.8782 -0.5107 -0.3126 0.1096 507 ASN B ND2 3687 N N . TYR A 477 ? 1.9454 0.8273 0.7269 -0.4472 -0.2752 0.0985 508 TYR B N 3688 C CA . TYR A 477 ? 1.9287 0.8213 0.7139 -0.4424 -0.2572 0.0931 508 TYR B CA 3689 C C . TYR A 477 ? 1.9514 0.8407 0.7128 -0.4736 -0.2393 0.0871 508 TYR B C 3690 O O . TYR A 477 ? 1.9470 0.8487 0.7042 -0.4856 -0.2164 0.0807 508 TYR B O 3691 C CB . TYR A 477 ? 1.8837 0.8050 0.6912 -0.4198 -0.2323 0.0871 508 TYR B CB 3692 C CG . TYR A 477 ? 1.8599 0.7881 0.6916 -0.3901 -0.2466 0.0921 508 TYR B CG 3693 C CD1 . TYR A 477 ? 1.8575 0.7886 0.6943 -0.3868 -0.2519 0.0946 508 TYR B CD1 3694 C CD2 . TYR A 477 ? 1.8424 0.7747 0.6922 -0.3659 -0.2542 0.0940 508 TYR B CD2 3695 C CE1 . TYR A 477 ? 1.8401 0.7784 0.6993 -0.3608 -0.2648 0.0988 508 TYR B CE1 3696 C CE2 . TYR A 477 ? 1.8242 0.7650 0.6988 -0.3394 -0.2666 0.0971 508 TYR B CE2 3697 C CZ . TYR A 477 ? 1.8233 0.7680 0.7032 -0.3372 -0.2716 0.0991 508 TYR B CZ 3698 O OH . TYR A 477 ? 1.8119 0.7757 0.7310 -0.3100 -0.2812 0.0972 508 TYR B OH 3699 N N . VAL A 478 ? 2.4729 1.3463 1.2198 -0.4868 -0.2494 0.0887 509 VAL B N 3700 C CA . VAL A 478 ? 2.5002 1.3682 1.2231 -0.5194 -0.2357 0.0838 509 VAL B CA 3701 C C . VAL A 478 ? 2.4821 1.3639 1.2107 -0.5165 -0.2132 0.0772 509 VAL B C 3702 O O . VAL A 478 ? 2.4855 1.3587 1.2145 -0.5099 -0.2255 0.0800 509 VAL B O 3703 C CB . VAL A 478 ? 2.5491 1.3867 1.2465 -0.5425 -0.2653 0.0905 509 VAL B CB 3704 C CG1 . VAL A 478 ? 2.5525 1.3753 1.2591 -0.5222 -0.2986 0.0989 509 VAL B CG1 3705 C CG2 . VAL A 478 ? 2.5761 1.4071 1.2504 -0.5727 -0.2539 0.0860 509 VAL B CG2 3706 N N . GLY A 479 ? 2.0759 0.9804 0.8105 -0.5203 -0.1804 0.0681 510 GLY B N 3707 C CA . GLY A 479 ? 2.0547 0.9770 0.7982 -0.5160 -0.1559 0.0606 510 GLY B CA 3708 C C . GLY A 479 ? 2.0219 0.9529 0.7872 -0.4831 -0.1609 0.0620 510 GLY B C 3709 O O . GLY A 479 ? 2.0226 0.9498 0.7876 -0.4803 -0.1633 0.0624 510 GLY B O 3710 N N . CYS A 480 ? 1.9049 0.8472 0.6887 -0.4588 -0.1629 0.0630 511 CYS B N 3711 C CA . CYS A 480 ? 1.8729 0.8256 0.6784 -0.4276 -0.1663 0.0639 511 CYS B CA 3712 C C . CYS A 480 ? 1.8525 0.8249 0.6645 -0.4258 -0.1392 0.0535 511 CYS B C 3713 O O . CYS A 480 ? 1.8401 0.8319 0.6559 -0.4323 -0.1132 0.0432 511 CYS B O 3714 C CB . CYS A 480 ? 1.8454 0.8130 0.6691 -0.4062 -0.1646 0.0639 511 CYS B CB 3715 S SG . CYS A 480 ? 1.8161 0.7931 0.6693 -0.3678 -0.1780 0.0678 511 CYS B SG 3716 N N . LYS A 481 ? 1.7751 0.7431 0.5898 -0.4170 -0.1457 0.0551 512 LYS B N 3717 C CA . LYS A 481 ? 1.7604 0.7455 0.5795 -0.4188 -0.1213 0.0446 512 LYS B CA 3718 C C . LYS A 481 ? 1.7223 0.7303 0.5707 -0.3881 -0.1126 0.0381 512 LYS B C 3719 O O . LYS A 481 ? 1.6965 0.7320 0.5680 -0.3789 -0.0896 0.0269 512 LYS B O 3720 C CB . LYS A 481 ? 1.7876 0.7553 0.5903 -0.4361 -0.1289 0.0482 512 LYS B CB 3721 C CG . LYS A 481 ? 1.7714 0.7586 0.5809 -0.4372 -0.1038 0.0370 512 LYS B CG 3722 C CD . LYS A 481 ? 1.8037 0.7765 0.5930 -0.4638 -0.1045 0.0393 512 LYS B CD 3723 C CE . LYS A 481 ? 1.7852 0.7766 0.5847 -0.4593 -0.0846 0.0294 512 LYS B CE 3724 N NZ . LYS A 481 ? 1.8155 0.7887 0.5963 -0.4789 -0.0929 0.0350 512 LYS B NZ 3725 N N . SER A 482 ? 1.6277 0.6301 0.4908 -0.3705 -0.1305 0.0441 513 SER B N 3726 C CA . SER A 482 ? 1.5949 0.6244 0.4988 -0.3423 -0.1205 0.0368 513 SER B CA 3727 C C . SER A 482 ? 1.5788 0.6253 0.5207 -0.3112 -0.1290 0.0383 513 SER B C 3728 O O . SER A 482 ? 1.5590 0.6294 0.5347 -0.2880 -0.1204 0.0323 513 SER B O 3729 C CB . SER A 482 ? 1.6035 0.6206 0.5013 -0.3432 -0.1301 0.0395 513 SER B CB 3730 O OG . SER A 482 ? 1.6311 0.6281 0.4882 -0.3757 -0.1265 0.0403 513 SER B OG 3731 N N . PHE A 483 ? 1.5344 0.5696 0.4700 -0.3119 -0.1450 0.0457 514 PHE B N 3732 C CA . PHE A 483 ? 1.5251 0.5725 0.4929 -0.2851 -0.1580 0.0480 514 PHE B CA 3733 C C . PHE A 483 ? 1.4979 0.5804 0.4995 -0.2666 -0.1366 0.0390 514 PHE B C 3734 O O . PHE A 483 ? 1.4936 0.5828 0.4886 -0.2765 -0.1215 0.0354 514 PHE B O 3735 C CB . PHE A 483 ? 1.5431 0.5710 0.4941 -0.2939 -0.1776 0.0570 514 PHE B CB 3736 C CG . PHE A 483 ? 1.5709 0.5643 0.4987 -0.3036 -0.2080 0.0679 514 PHE B CG 3737 C CD1 . PHE A 483 ? 1.6056 0.5742 0.4989 -0.3272 -0.2115 0.0717 514 PHE B CD1 3738 C CD2 . PHE A 483 ? 1.5742 0.5598 0.5153 -0.2898 -0.2341 0.0742 514 PHE B CD2 3739 C CE1 . PHE A 483 ? 1.6438 0.5783 0.5151 -0.3368 -0.2415 0.0827 514 PHE B CE1 3740 C CE2 . PHE A 483 ? 1.6113 0.5637 0.5331 -0.2980 -0.2642 0.0840 514 PHE B CE2 3741 C CZ . PHE A 483 ? 1.6470 0.5725 0.5330 -0.3217 -0.2686 0.0890 514 PHE B CZ 3742 N N . TYR A 484 ? 1.5533 0.6578 0.5901 -0.2409 -0.1349 0.0350 515 TYR B N 3743 C CA . TYR A 484 ? 1.5330 0.6680 0.6018 -0.2224 -0.1213 0.0292 515 TYR B CA 3744 C C . TYR A 484 ? 1.5316 0.6773 0.6253 -0.2021 -0.1365 0.0323 515 TYR B C 3745 O O . TYR A 484 ? 1.5204 0.6871 0.6325 -0.1930 -0.1262 0.0291 515 TYR B O 3746 C CB . TYR A 484 ? 1.5124 0.6721 0.6040 -0.2110 -0.1001 0.0200 515 TYR B CB 3747 C CG . TYR A 484 ? 1.5036 0.6737 0.6193 -0.1904 -0.1074 0.0190 515 TYR B CG 3748 C CD1 . TYR A 484 ? 1.4932 0.6818 0.6386 -0.1680 -0.1147 0.0189 515 TYR B CD1 3749 C CD2 . TYR A 484 ? 1.5054 0.6687 0.6148 -0.1939 -0.1056 0.0172 515 TYR B CD2 3750 C CE1 . TYR A 484 ? 1.4851 0.6846 0.6525 -0.1500 -0.1205 0.0166 515 TYR B CE1 3751 C CE2 . TYR A 484 ? 1.4970 0.6700 0.6284 -0.1753 -0.1118 0.0157 515 TYR B CE2 3752 C CZ . TYR A 484 ? 1.4867 0.6779 0.6470 -0.1533 -0.1192 0.0152 515 TYR B CZ 3753 O OH . TYR A 484 ? 1.4781 0.6805 0.6606 -0.1353 -0.1250 0.0125 515 TYR B OH 3754 N N . ARG A 485 ? 1.5253 0.6573 0.6203 -0.1955 -0.1611 0.0377 516 ARG B N 3755 C CA . ARG A 485 ? 1.5238 0.6696 0.6464 -0.1753 -0.1748 0.0380 516 ARG B CA 3756 C C . ARG A 485 ? 1.5452 0.6642 0.6540 -0.1806 -0.2040 0.0458 516 ARG B C 3757 O O . ARG A 485 ? 1.5567 0.6535 0.6527 -0.1853 -0.2202 0.0496 516 ARG B O 3758 C CB . ARG A 485 ? 1.5095 0.6796 0.6665 -0.1512 -0.1731 0.0317 516 ARG B CB 3759 C CG . ARG A 485 ? 1.4990 0.6978 0.6901 -0.1304 -0.1741 0.0278 516 ARG B CG 3760 C CD . ARG A 485 ? 1.4780 0.7073 0.6998 -0.1112 -0.1610 0.0200 516 ARG B CD 3761 N NE . ARG A 485 ? 1.4685 0.7277 0.7130 -0.1009 -0.1479 0.0161 516 ARG B NE 3762 C CZ . ARG A 485 ? 1.4677 0.7382 0.7107 -0.1062 -0.1265 0.0145 516 ARG B CZ 3763 N NH1 . ARG A 485 ? 1.4736 0.7303 0.6950 -0.1215 -0.1143 0.0149 516 ARG B NH1 3764 N NH2 . ARG A 485 ? 1.4622 0.7581 0.7254 -0.0971 -0.1175 0.0120 516 ARG B NH2 3765 N N . ILE A 486 ? 1.4285 0.5487 0.5399 -0.1802 -0.2118 0.0485 517 ILE B N 3766 C CA . ILE A 486 ? 1.4557 0.5495 0.5543 -0.1859 -0.2410 0.0562 517 ILE B CA 3767 C C . ILE A 486 ? 1.4470 0.5576 0.5771 -0.1662 -0.2550 0.0539 517 ILE B C 3768 O O . ILE A 486 ? 1.4360 0.5639 0.5753 -0.1638 -0.2453 0.0523 517 ILE B O 3769 C CB . ILE A 486 ? 1.4807 0.5493 0.5409 -0.2125 -0.2418 0.0636 517 ILE B CB 3770 C CG1 . ILE A 486 ? 1.4910 0.5454 0.5198 -0.2341 -0.2267 0.0641 517 ILE B CG1 3771 C CG2 . ILE A 486 ? 1.5101 0.5488 0.5558 -0.2193 -0.2739 0.0724 517 ILE B CG2 3772 C CD1 . ILE A 486 ? 1.5202 0.5542 0.5115 -0.2613 -0.2234 0.0691 517 ILE B CD1 3773 N N . GLU A 487 ? 1.5584 0.6648 0.7060 -0.1523 -0.2779 0.0529 518 GLU B N 3774 C CA . GLU A 487 ? 1.5604 0.6836 0.7383 -0.1351 -0.2916 0.0492 518 GLU B CA 3775 C C . GLU A 487 ? 1.5822 0.6746 0.7491 -0.1409 -0.3248 0.0560 518 GLU B C 3776 O O . GLU A 487 ? 1.5911 0.6670 0.7616 -0.1358 -0.3463 0.0564 518 GLU B O 3777 C CB . GLU A 487 ? 1.5488 0.7018 0.7665 -0.1099 -0.2900 0.0388 518 GLU B CB 3778 C CG . GLU A 487 ? 1.5285 0.7142 0.7607 -0.1025 -0.2594 0.0323 518 GLU B CG 3779 C CD . GLU A 487 ? 1.5190 0.7195 0.7728 -0.0868 -0.2568 0.0249 518 GLU B CD 3780 O OE1 . GLU A 487 ? 1.5261 0.7194 0.7930 -0.0767 -0.2789 0.0224 518 GLU B OE1 3781 O OE2 . GLU A 487 ? 1.5041 0.7229 0.7621 -0.0847 -0.2332 0.0214 518 GLU B OE2 3782 N N . LEU A 488 ? 1.5595 0.6430 0.7129 -0.1519 -0.3297 0.0614 519 LEU B N 3783 C CA . LEU A 488 ? 1.5802 0.6350 0.7239 -0.1578 -0.3621 0.0683 519 LEU B CA 3784 C C . LEU A 488 ? 1.5815 0.6564 0.7601 -0.1399 -0.3757 0.0626 519 LEU B C 3785 O O . LEU A 488 ? 1.5974 0.6510 0.7714 -0.1438 -0.4026 0.0675 519 LEU B O 3786 C CB . LEU A 488 ? 1.5944 0.6161 0.6914 -0.1870 -0.3639 0.0799 519 LEU B CB 3787 C CG . LEU A 488 ? 1.6030 0.5967 0.6658 -0.2051 -0.3632 0.0857 519 LEU B CG 3788 C CD1 . LEU A 488 ? 1.6132 0.5836 0.6306 -0.2351 -0.3550 0.0941 519 LEU B CD1 3789 C CD2 . LEU A 488 ? 1.6233 0.5881 0.6847 -0.2030 -0.3976 0.0902 519 LEU B CD2 3790 N N . GLN A 489 ? 1.6367 0.7528 0.8497 -0.1214 -0.3572 0.0521 520 GLN B N 3791 C CA . GLN A 489 ? 1.6347 0.7771 0.8802 -0.1066 -0.3625 0.0454 520 GLN B CA 3792 C C . GLN A 489 ? 1.6451 0.7874 0.9208 -0.0899 -0.3932 0.0393 520 GLN B C 3793 O O . GLN A 489 ? 1.6528 0.7800 0.9318 -0.0847 -0.4093 0.0380 520 GLN B O 3794 C CB . GLN A 489 ? 1.6153 0.8012 0.8876 -0.0927 -0.3343 0.0357 520 GLN B CB 3795 C CG . GLN A 489 ? 1.6064 0.7931 0.8658 -0.0967 -0.3127 0.0360 520 GLN B CG 3796 C CD . GLN A 489 ? 1.5897 0.8003 0.8800 -0.0770 -0.3097 0.0258 520 GLN B CD 3797 O OE1 . GLN A 489 ? 1.5892 0.8100 0.9081 -0.0613 -0.3278 0.0185 520 GLN B OE1 3798 N NE2 . GLN A 489 ? 1.5757 0.7965 0.8618 -0.0775 -0.2869 0.0242 520 GLN B NE2 3799 N N . GLY A 490 ? 1.6923 0.8508 0.9901 -0.0822 -0.4018 0.0350 521 GLY B N 3800 C CA . GLY A 490 ? 1.6930 0.8645 1.0303 -0.0625 -0.4259 0.0245 521 GLY B CA 3801 C C . GLY A 490 ? 1.7087 0.8429 1.0392 -0.0664 -0.4642 0.0298 521 GLY B C 3802 O O . GLY A 490 ? 1.7076 0.8450 1.0691 -0.0499 -0.4873 0.0207 521 GLY B O 3803 N N . ASN A 491 ? 1.5343 0.6335 0.8253 -0.0885 -0.4718 0.0441 522 ASN B N 3804 C CA . ASN A 491 ? 1.5637 0.6185 0.8368 -0.0978 -0.5080 0.0529 522 ASN B CA 3805 C C . ASN A 491 ? 1.5825 0.6222 0.8465 -0.1075 -0.5259 0.0596 522 ASN B C 3806 O O . ASN A 491 ? 1.5678 0.6355 0.8480 -0.1027 -0.5133 0.0548 522 ASN B O 3807 C CB . ASN A 491 ? 1.5825 0.5995 0.8087 -0.1195 -0.5058 0.0658 522 ASN B CB 3808 C CG . ASN A 491 ? 1.5689 0.5947 0.8052 -0.1093 -0.4960 0.0596 522 ASN B CG 3809 O OD1 . ASN A 491 ? 1.5600 0.5961 0.8311 -0.0892 -0.5118 0.0495 522 ASN B OD1 3810 N ND2 . ASN A 491 ? 1.5666 0.5895 0.7743 -0.1229 -0.4699 0.0646 522 ASN B ND2 3811 N N . SER A 492 ? 1.6748 0.6699 0.9152 -0.1202 -0.5580 0.0701 523 SER B N 3812 C CA . SER A 492 ? 1.6896 0.6622 0.9110 -0.1346 -0.5757 0.0796 523 SER B CA 3813 C C . SER A 492 ? 1.7020 0.6408 0.8647 -0.1666 -0.5672 0.0964 523 SER B C 3814 O O . SER A 492 ? 1.7195 0.6309 0.8609 -0.1814 -0.5875 0.1061 523 SER B O 3815 C CB . SER A 492 ? 1.7026 0.6545 0.9452 -0.1254 -0.6198 0.0782 523 SER B CB 3816 O OG . SER A 492 ? 1.6894 0.6834 0.9874 -0.0990 -0.6207 0.0610 523 SER B OG 3817 N N . LEU A 493 ? 1.6662 0.6061 0.8035 -0.1776 -0.5389 0.0991 524 LEU B N 3818 C CA . LEU A 493 ? 1.6932 0.6053 0.7762 -0.2084 -0.5272 0.1123 524 LEU B CA 3819 C C . LEU A 493 ? 1.6939 0.6109 0.7646 -0.2198 -0.5186 0.1161 524 LEU B C 3820 O O . LEU A 493 ? 1.6552 0.6102 0.7509 -0.2075 -0.4955 0.1075 524 LEU B O 3821 C CB . LEU A 493 ? 1.6700 0.5972 0.7393 -0.2138 -0.4907 0.1098 524 LEU B CB 3822 C CG . LEU A 493 ? 1.6609 0.5899 0.7374 -0.2053 -0.4861 0.1054 524 LEU B CG 3823 C CD1 . LEU A 493 ? 1.6398 0.5838 0.6992 -0.2143 -0.4482 0.1037 524 LEU B CD1 3824 C CD2 . LEU A 493 ? 1.7083 0.5916 0.7572 -0.2191 -0.5163 0.1155 524 LEU B CD2 3825 N N . ASN A 494 ? 1.9714 0.8488 1.0013 -0.2447 -0.5369 0.1293 525 ASN B N 3826 C CA . ASN A 494 ? 1.9791 0.8548 0.9904 -0.2595 -0.5309 0.1345 525 ASN B CA 3827 C C . ASN A 494 ? 1.9942 0.8538 0.9581 -0.2898 -0.5083 0.1413 525 ASN B C 3828 O O . ASN A 494 ? 1.9938 0.8496 0.9443 -0.2975 -0.4943 0.1402 525 ASN B O 3829 C CB . ASN A 494 ? 2.0122 0.8612 1.0230 -0.2628 -0.5702 0.1416 525 ASN B CB 3830 C CG . ASN A 494 ? 2.0530 0.8639 1.0470 -0.2831 -0.5912 0.1474 525 ASN B CG 3831 O OD1 . ASN A 494 ? 2.0595 0.8611 1.0401 -0.2907 -0.5846 0.1473 525 ASN B OD1 3832 N ND2 . ASN A 494 ? 2.0848 0.8740 1.0794 -0.2923 -0.6175 0.1519 525 ASN B ND2 3833 N N . GLY A 495 ? 2.2452 1.1033 1.1939 -0.3064 -0.5005 0.1439 526 GLY B N 3834 C CA . GLY A 495 ? 2.2558 1.1073 1.1717 -0.3350 -0.4765 0.1446 526 GLY B CA 3835 C C . GLY A 495 ? 2.2226 1.1028 1.1364 -0.3313 -0.4388 0.1390 526 GLY B C 3836 O O . GLY A 495 ? 2.1953 1.0999 1.1309 -0.3100 -0.4324 0.1358 526 GLY B O 3837 N N . THR A 496 ? 1.8594 0.7385 0.7492 -0.3521 -0.4142 0.1363 527 THR B N 3838 C CA . THR A 496 ? 1.8314 0.7360 0.7188 -0.3517 -0.3781 0.1300 527 THR B CA 3839 C C . THR A 496 ? 1.8178 0.7305 0.7005 -0.3520 -0.3559 0.1247 527 THR B C 3840 O O . THR A 496 ? 1.8363 0.7320 0.7078 -0.3620 -0.3643 0.1257 527 THR B O 3841 C CB . THR A 496 ? 1.8431 0.7455 0.7092 -0.3764 -0.3633 0.1288 527 THR B CB 3842 O OG1 . THR A 496 ? 1.8757 0.7581 0.7156 -0.4029 -0.3635 0.1287 527 THR B OG1 3843 C CG2 . THR A 496 ? 1.8566 0.7512 0.7269 -0.3766 -0.3841 0.1342 527 THR B CG2 3844 N N . ILE A 497 ? 1.6788 0.6174 0.5700 -0.3415 -0.3281 0.1187 528 ILE B N 3845 C CA . ILE A 497 ? 1.6626 0.6118 0.5510 -0.3411 -0.3042 0.1126 528 ILE B CA 3846 C C . ILE A 497 ? 1.6813 0.6239 0.5445 -0.3695 -0.2858 0.1083 528 ILE B C 3847 O O . ILE A 497 ? 1.6784 0.6297 0.5347 -0.3804 -0.2685 0.1045 528 ILE B O 3848 C CB . ILE A 497 ? 1.6323 0.6223 0.5557 -0.3205 -0.2763 0.1018 528 ILE B CB 3849 C CG1 . ILE A 497 ? 1.6209 0.6346 0.5903 -0.2899 -0.2871 0.0984 528 ILE B CG1 3850 C CG2 . ILE A 497 ? 1.6223 0.6231 0.5449 -0.3216 -0.2520 0.0945 528 ILE B CG2 3851 C CD1 . ILE A 497 ? 1.6383 0.6609 0.6220 -0.2836 -0.2962 0.0999 528 ILE B CD1 3852 N N . PRO A 498 ? 1.7006 0.6289 0.5504 -0.3817 -0.2890 0.1081 529 PRO B N 3853 C CA . PRO A 498 ? 1.7261 0.6447 0.5499 -0.4116 -0.2770 0.1044 529 PRO B CA 3854 C C . PRO A 498 ? 1.7113 0.6486 0.5299 -0.4216 -0.2431 0.0949 529 PRO B C 3855 O O . PRO A 498 ? 1.6796 0.6385 0.5117 -0.4078 -0.2213 0.0887 529 PRO B O 3856 C CB . PRO A 498 ? 1.7365 0.6448 0.5541 -0.4148 -0.2814 0.1043 529 PRO B CB 3857 C CG . PRO A 498 ? 1.7383 0.6357 0.5712 -0.3954 -0.3117 0.1118 529 PRO B CG 3858 C CD . PRO A 498 ? 1.7056 0.6224 0.5634 -0.3696 -0.3099 0.1123 529 PRO B CD 3859 N N . TRP A 499 ? 2.0881 1.0147 0.8857 -0.4479 -0.2407 0.0937 530 TRP B N 3860 C CA . TRP A 499 ? 2.0865 1.0246 0.8743 -0.4651 -0.2122 0.0845 530 TRP B CA 3861 C C . TRP A 499 ? 2.0699 1.0222 0.8605 -0.4647 -0.1869 0.0756 530 TRP B C 3862 O O . TRP A 499 ? 2.0466 1.0195 0.8459 -0.4607 -0.1611 0.0669 530 TRP B O 3863 C CB . TRP A 499 ? 2.1299 1.0464 0.8905 -0.4970 -0.2209 0.0863 530 TRP B CB 3864 C CG . TRP A 499 ? 2.1370 1.0610 0.8852 -0.5189 -0.1958 0.0777 530 TRP B CG 3865 C CD1 . TRP A 499 ? 2.1639 1.0799 0.8915 -0.5469 -0.1856 0.0735 530 TRP B CD1 3866 C CD2 . TRP A 499 ? 2.1183 1.0596 0.8747 -0.5156 -0.1773 0.0721 530 TRP B CD2 3867 N NE1 . TRP A 499 ? 2.1628 1.0909 0.8864 -0.5610 -0.1612 0.0654 530 TRP B NE1 3868 C CE2 . TRP A 499 ? 2.1349 1.0781 0.8758 -0.5418 -0.1561 0.0642 530 TRP B CE2 3869 C CE3 . TRP A 499 ? 2.0898 1.0455 0.8654 -0.4934 -0.1766 0.0729 530 TRP B CE3 3870 C CZ2 . TRP A 499 ? 2.1240 1.0826 0.8688 -0.5456 -0.1348 0.0568 530 TRP B CZ2 3871 C CZ3 . TRP A 499 ? 2.0795 1.0494 0.8573 -0.4979 -0.1561 0.0657 530 TRP B CZ3 3872 C CH2 . TRP A 499 ? 2.0966 1.0675 0.8593 -0.5233 -0.1357 0.0575 530 TRP B CH2 3873 N N . ASP A 500 ? 1.9877 0.9288 0.7723 -0.4678 -0.1954 0.0777 531 ASP B N 3874 C CA . ASP A 500 ? 1.9811 0.9316 0.7633 -0.4743 -0.1730 0.0696 531 ASP B CA 3875 C C . ASP A 500 ? 1.9450 0.9128 0.7488 -0.4474 -0.1642 0.0668 531 ASP B C 3876 O O . ASP A 500 ? 1.9392 0.9142 0.7425 -0.4509 -0.1481 0.0604 531 ASP B O 3877 C CB . ASP A 500 ? 2.0180 0.9467 0.7781 -0.4977 -0.1842 0.0723 531 ASP B CB 3878 C CG . ASP A 500 ? 2.0335 0.9412 0.7928 -0.4890 -0.2182 0.0829 531 ASP B CG 3879 O OD1 . ASP A 500 ? 2.0102 0.9237 0.7900 -0.4617 -0.2295 0.0872 531 ASP B OD1 3880 O OD2 . ASP A 500 ? 2.0703 0.9559 0.8090 -0.5098 -0.2342 0.0866 531 ASP B OD2 3881 N N . ILE A 501 ? 1.6664 0.6416 0.4893 -0.4214 -0.1743 0.0712 532 ILE B N 3882 C CA . ILE A 501 ? 1.6352 0.6243 0.4779 -0.3952 -0.1708 0.0702 532 ILE B CA 3883 C C . ILE A 501 ? 1.6108 0.6224 0.4605 -0.3929 -0.1394 0.0580 532 ILE B C 3884 O O . ILE A 501 ? 1.5885 0.6116 0.4541 -0.3763 -0.1340 0.0548 532 ILE B O 3885 C CB . ILE A 501 ? 1.6126 0.6103 0.4756 -0.3696 -0.1826 0.0754 532 ILE B CB 3886 C CG1 . ILE A 501 ? 1.6040 0.6085 0.4956 -0.3447 -0.1957 0.0771 532 ILE B CG1 3887 C CG2 . ILE A 501 ? 1.5881 0.6166 0.4759 -0.3582 -0.1574 0.0653 532 ILE B CG2 3888 C CD1 . ILE A 501 ? 1.5730 0.6135 0.5055 -0.3195 -0.1753 0.0670 532 ILE B CD1 3889 N N . GLY A 502 ? 1.7937 0.8133 0.6367 -0.4094 -0.1190 0.0496 533 GLY B N 3890 C CA . GLY A 502 ? 1.7740 0.8147 0.6255 -0.4084 -0.0901 0.0361 533 GLY B CA 3891 C C . GLY A 502 ? 1.7837 0.8209 0.6265 -0.4214 -0.0824 0.0319 533 GLY B C 3892 O O . GLY A 502 ? 1.7735 0.8267 0.6215 -0.4268 -0.0583 0.0196 533 GLY B O 3893 N N . HIS A 503 ? 1.6409 0.6569 0.4715 -0.4272 -0.1038 0.0418 534 HIS B N 3894 C CA . HIS A 503 ? 1.6558 0.6652 0.4762 -0.4405 -0.1002 0.0399 534 HIS B CA 3895 C C . HIS A 503 ? 1.6315 0.6497 0.4666 -0.4186 -0.0991 0.0382 534 HIS B C 3896 O O . HIS A 503 ? 1.6357 0.6552 0.4669 -0.4265 -0.0900 0.0337 534 HIS B O 3897 C CB . HIS A 503 ? 1.6954 0.6756 0.4941 -0.4591 -0.1254 0.0507 534 HIS B CB 3898 C CG . HIS A 503 ? 1.7272 0.6993 0.5049 -0.4917 -0.1181 0.0483 534 HIS B CG 3899 N ND1 . HIS A 503 ? 1.7605 0.7157 0.5178 -0.5163 -0.1235 0.0505 534 HIS B ND1 3900 C CD2 . HIS A 503 ? 1.7318 0.7106 0.5055 -0.5046 -0.1053 0.0438 534 HIS B CD2 3901 C CE1 . HIS A 503 ? 1.7847 0.7371 0.5260 -0.5434 -0.1141 0.0475 534 HIS B CE1 3902 N NE2 . HIS A 503 ? 1.7675 0.7342 0.5188 -0.5365 -0.1028 0.0434 534 HIS B NE2 3903 N N . CYS A 504 ? 1.6160 0.6411 0.4681 -0.3918 -0.1080 0.0416 535 CYS B N 3904 C CA . CYS A 504 ? 1.5940 0.6345 0.4763 -0.3682 -0.1063 0.0388 535 CYS B CA 3905 C C . CYS A 504 ? 1.5648 0.6381 0.4788 -0.3537 -0.0801 0.0259 535 CYS B C 3906 O O . CYS A 504 ? 1.5513 0.6411 0.4921 -0.3347 -0.0796 0.0256 535 CYS B O 3907 C CB . CYS A 504 ? 1.5922 0.6314 0.4970 -0.3443 -0.1301 0.0479 535 CYS B CB 3908 S SG . CYS A 504 ? 1.6259 0.6252 0.4969 -0.3598 -0.1653 0.0636 535 CYS B SG 3909 N N . GLU A 505 ? 1.5791 0.6620 0.4918 -0.3620 -0.0595 0.0151 536 GLU B N 3910 C CA . GLU A 505 ? 1.5558 0.6672 0.4963 -0.3516 -0.0347 0.0017 536 GLU B CA 3911 C C . GLU A 505 ? 1.5370 0.6689 0.5173 -0.3209 -0.0351 0.0010 536 GLU B C 3912 O O . GLU A 505 ? 1.5191 0.6736 0.5295 -0.3038 -0.0244 -0.0045 536 GLU B O 3913 C CB . GLU A 505 ? 1.5592 0.6740 0.4851 -0.3723 -0.0133 -0.0111 536 GLU B CB 3914 C CG . GLU A 505 ? 1.5897 0.6845 0.4739 -0.4059 -0.0129 -0.0105 536 GLU B CG 3915 C CD . GLU A 505 ? 1.5846 0.6928 0.4739 -0.4154 0.0048 -0.0201 536 GLU B CD 3916 O OE1 . GLU A 505 ? 1.5616 0.6895 0.4750 -0.3998 0.0187 -0.0307 536 GLU B OE1 3917 O OE2 . GLU A 505 ? 1.6093 0.7083 0.4805 -0.4391 0.0046 -0.0169 536 GLU B OE2 3918 N N . LYS A 506 ? 1.6007 0.7231 0.5797 -0.3151 -0.0490 0.0073 537 LYS B N 3919 C CA . LYS A 506 ? 1.5842 0.7246 0.5971 -0.2891 -0.0489 0.0057 537 LYS B CA 3920 C C . LYS A 506 ? 1.5832 0.7281 0.6171 -0.2670 -0.0670 0.0139 537 LYS B C 3921 O O . LYS A 506 ? 1.5732 0.7322 0.6339 -0.2457 -0.0698 0.0135 537 LYS B O 3922 C CB . LYS A 506 ? 1.5903 0.7203 0.5927 -0.2942 -0.0529 0.0064 537 LYS B CB 3923 C CG . LYS A 506 ? 1.5951 0.7206 0.5743 -0.3188 -0.0358 -0.0021 537 LYS B CG 3924 C CD . LYS A 506 ? 1.5834 0.7156 0.5716 -0.3144 -0.0288 -0.0074 537 LYS B CD 3925 C CE . LYS A 506 ? 1.5845 0.7166 0.5529 -0.3391 -0.0094 -0.0183 537 LYS B CE 3926 N NZ . LYS A 506 ? 1.5728 0.7122 0.5506 -0.3352 -0.0023 -0.0239 537 LYS B NZ 3927 N N . LEU A 507 ? 1.4186 0.5522 0.4405 -0.2728 -0.0791 0.0206 538 LEU B N 3928 C CA . LEU A 507 ? 1.4115 0.5494 0.4525 -0.2538 -0.0970 0.0273 538 LEU B CA 3929 C C . LEU A 507 ? 1.3798 0.5487 0.4576 -0.2319 -0.0850 0.0219 538 LEU B C 3930 O O . LEU A 507 ? 1.3703 0.5504 0.4514 -0.2361 -0.0682 0.0164 538 LEU B O 3931 C CB . LEU A 507 ? 1.4358 0.5536 0.4535 -0.2677 -0.1120 0.0352 538 LEU B CB 3932 C CG . LEU A 507 ? 1.4361 0.5544 0.4689 -0.2526 -0.1332 0.0422 538 LEU B CG 3933 C CD1 . LEU A 507 ? 1.4322 0.5511 0.4826 -0.2352 -0.1493 0.0443 538 LEU B CD1 3934 C CD2 . LEU A 507 ? 1.4677 0.5578 0.4686 -0.2723 -0.1503 0.0507 538 LEU B CD2 3935 N N . LEU A 508 ? 1.4019 0.5840 0.5065 -0.2097 -0.0945 0.0233 539 LEU B N 3936 C CA . LEU A 508 ? 1.3823 0.5945 0.5219 -0.1886 -0.0850 0.0188 539 LEU B CA 3937 C C . LEU A 508 ? 1.3854 0.6071 0.5427 -0.1743 -0.0994 0.0230 539 LEU B C 3938 O O . LEU A 508 ? 1.3806 0.6162 0.5486 -0.1709 -0.0928 0.0221 539 LEU B O 3939 C CB . LEU A 508 ? 1.3693 0.5946 0.5284 -0.1741 -0.0809 0.0148 539 LEU B CB 3940 C CG . LEU A 508 ? 1.3607 0.5854 0.5124 -0.1834 -0.0633 0.0083 539 LEU B CG 3941 C CD1 . LEU A 508 ? 1.3412 0.5844 0.5187 -0.1653 -0.0585 0.0042 539 LEU B CD1 3942 C CD2 . LEU A 508 ? 1.3580 0.5908 0.5089 -0.1919 -0.0446 0.0027 539 LEU B CD2 3943 N N . CYS A 509 ? 1.4571 0.6732 0.6202 -0.1651 -0.1187 0.0264 540 CYS B N 3944 C CA . CYS A 509 ? 1.4633 0.6875 0.6429 -0.1529 -0.1345 0.0290 540 CYS B CA 3945 C C . CYS A 509 ? 1.4833 0.6795 0.6422 -0.1626 -0.1582 0.0361 540 CYS B C 3946 O O . CYS A 509 ? 1.4922 0.6695 0.6400 -0.1658 -0.1715 0.0386 540 CYS B O 3947 C CB . CYS A 509 ? 1.4529 0.6999 0.6645 -0.1304 -0.1381 0.0247 540 CYS B CB 3948 S SG . CYS A 509 ? 1.4731 0.7133 0.6959 -0.1191 -0.1682 0.0269 540 CYS B SG 3949 N N . LEU A 510 ? 1.3907 0.5835 0.5441 -0.1681 -0.1641 0.0396 541 LEU B N 3950 C CA . LEU A 510 ? 1.4141 0.5816 0.5502 -0.1769 -0.1883 0.0468 541 LEU B CA 3951 C C . LEU A 510 ? 1.4138 0.5963 0.5756 -0.1613 -0.2025 0.0465 541 LEU B C 3952 O O . LEU A 510 ? 1.4109 0.6058 0.5780 -0.1618 -0.1954 0.0462 541 LEU B O 3953 C CB . LEU A 510 ? 1.4282 0.5754 0.5304 -0.2011 -0.1831 0.0513 541 LEU B CB 3954 C CG . LEU A 510 ? 1.4584 0.5769 0.5372 -0.2144 -0.2071 0.0600 541 LEU B CG 3955 C CD1 . LEU A 510 ? 1.4743 0.5721 0.5486 -0.2123 -0.2309 0.0640 541 LEU B CD1 3956 C CD2 . LEU A 510 ? 1.4797 0.5761 0.5195 -0.2418 -0.1997 0.0637 541 LEU B CD2 3957 N N . ASN A 511 ? 1.4609 0.6417 0.6385 -0.1485 -0.2234 0.0459 542 ASN B N 3958 C CA . ASN A 511 ? 1.4661 0.6614 0.6692 -0.1344 -0.2383 0.0439 542 ASN B CA 3959 C C . ASN A 511 ? 1.4861 0.6504 0.6717 -0.1440 -0.2664 0.0511 542 ASN B C 3960 O O . ASN A 511 ? 1.4968 0.6403 0.6772 -0.1438 -0.2862 0.0533 542 ASN B O 3961 C CB . ASN A 511 ? 1.4578 0.6793 0.6976 -0.1111 -0.2413 0.0354 542 ASN B CB 3962 C CG . ASN A 511 ? 1.4600 0.7085 0.7315 -0.0961 -0.2478 0.0299 542 ASN B CG 3963 O OD1 . ASN A 511 ? 1.4735 0.7131 0.7410 -0.1008 -0.2616 0.0333 542 ASN B OD1 3964 N ND2 . ASN A 511 ? 1.4472 0.7295 0.7501 -0.0788 -0.2379 0.0210 542 ASN B ND2 3965 N N . LEU A 512 ? 1.4711 0.6301 0.6453 -0.1542 -0.2682 0.0555 543 LEU B N 3966 C CA . LEU A 512 ? 1.4930 0.6235 0.6503 -0.1644 -0.2946 0.0630 543 LEU B CA 3967 C C . LEU A 512 ? 1.4971 0.6418 0.6832 -0.1500 -0.3124 0.0600 543 LEU B C 3968 O O . LEU A 512 ? 1.5146 0.6371 0.6878 -0.1588 -0.3336 0.0662 543 LEU B O 3969 C CB . LEU A 512 ? 1.5047 0.6127 0.6229 -0.1898 -0.2874 0.0707 543 LEU B CB 3970 C CG . LEU A 512 ? 1.5119 0.5961 0.5956 -0.2087 -0.2791 0.0745 543 LEU B CG 3971 C CD1 . LEU A 512 ? 1.5297 0.5889 0.5738 -0.2352 -0.2776 0.0817 543 LEU B CD1 3972 C CD2 . LEU A 512 ? 1.5258 0.5873 0.6046 -0.2074 -0.3021 0.0777 543 LEU B CD2 3973 N N . SER A 513 ? 1.6626 0.8448 0.8867 -0.1295 -0.3034 0.0503 544 SER B N 3974 C CA . SER A 513 ? 1.6658 0.8695 0.9181 -0.1177 -0.3129 0.0457 544 SER B CA 3975 C C . SER A 513 ? 1.6777 0.8741 0.9499 -0.1066 -0.3452 0.0429 544 SER B C 3976 O O . SER A 513 ? 1.6843 0.8572 0.9501 -0.1065 -0.3634 0.0447 544 SER B O 3977 C CB . SER A 513 ? 1.6507 0.8983 0.9351 -0.1019 -0.2912 0.0360 544 SER B CB 3978 O OG . SER A 513 ? 1.6424 0.9045 0.9481 -0.0869 -0.2899 0.0283 544 SER B OG 3979 N N . GLN A 514 ? 1.5967 0.8140 0.8944 -0.0973 -0.3524 0.0378 545 GLN B N 3980 C CA . GLN A 514 ? 1.6078 0.8230 0.9303 -0.0857 -0.3830 0.0329 545 GLN B CA 3981 C C . GLN A 514 ? 1.6257 0.7946 0.9215 -0.0986 -0.4127 0.0431 545 GLN B C 3982 O O . GLN A 514 ? 1.6320 0.7871 0.9392 -0.0904 -0.4368 0.0405 545 GLN B O 3983 C CB . GLN A 514 ? 1.5996 0.8392 0.9598 -0.0638 -0.3870 0.0197 545 GLN B CB 3984 C CG . GLN A 514 ? 1.5863 0.8758 0.9829 -0.0485 -0.3683 0.0071 545 GLN B CG 3985 C CD . GLN A 514 ? 1.5894 0.9029 1.0271 -0.0270 -0.3794 -0.0079 545 GLN B CD 3986 O OE1 . GLN A 514 ? 1.6014 0.8994 1.0516 -0.0203 -0.4082 -0.0112 545 GLN B OE1 3987 N NE2 . GLN A 514 ? 1.5788 0.9298 1.0379 -0.0164 -0.3573 -0.0175 545 GLN B NE2 3988 N N . ASN A 515 ? 1.7695 0.9144 1.0301 -0.1193 -0.4116 0.0545 546 ASN B N 3989 C CA . ASN A 515 ? 1.7876 0.8860 1.0153 -0.1363 -0.4376 0.0662 546 ASN B CA 3990 C C . ASN A 515 ? 1.8000 0.8838 1.0134 -0.1487 -0.4504 0.0734 546 ASN B C 3991 O O . ASN A 515 ? 1.7948 0.9050 1.0250 -0.1437 -0.4398 0.0691 546 ASN B O 3992 C CB . ASN A 515 ? 1.7879 0.8589 0.9725 -0.1564 -0.4250 0.0755 546 ASN B CB 3993 C CG . ASN A 515 ? 1.7803 0.8461 0.9709 -0.1482 -0.4289 0.0722 546 ASN B CG 3994 O OD1 . ASN A 515 ? 1.7979 0.8288 0.9708 -0.1559 -0.4533 0.0788 546 ASN B OD1 3995 N ND2 . ASN A 515 ? 1.7548 0.8545 0.9700 -0.1330 -0.4058 0.0624 546 ASN B ND2 3996 N N . HIS A 516 ? 1.7174 0.7577 0.8988 -0.1656 -0.4749 0.0847 547 HIS B N 3997 C CA . HIS A 516 ? 1.7323 0.7508 0.8944 -0.1801 -0.4918 0.0934 547 HIS B CA 3998 C C . HIS A 516 ? 1.7374 0.7349 0.8500 -0.2082 -0.4745 0.1045 547 HIS B C 3999 O O . HIS A 516 ? 1.7529 0.7221 0.8385 -0.2258 -0.4911 0.1143 547 HIS B O 4000 C CB . HIS A 516 ? 1.7509 0.7370 0.9149 -0.1793 -0.5342 0.0977 547 HIS B CB 4001 C CG . HIS A 516 ? 1.7443 0.7555 0.9618 -0.1509 -0.5506 0.0840 547 HIS B CG 4002 N ND1 . HIS A 516 ? 1.7247 0.7851 0.9831 -0.1302 -0.5288 0.0696 547 HIS B ND1 4003 C CD2 . HIS A 516 ? 1.7545 0.7489 0.9918 -0.1404 -0.5868 0.0815 547 HIS B CD2 4004 C CE1 . HIS A 516 ? 1.7223 0.7974 1.0237 -0.1084 -0.5494 0.0578 547 HIS B CE1 4005 N NE2 . HIS A 516 ? 1.7395 0.7752 1.0305 -0.1132 -0.5850 0.0643 547 HIS B NE2 4006 N N . LEU A 517 ? 1.6157 0.6252 0.7162 -0.2129 -0.4429 0.1026 548 LEU B N 4007 C CA . LEU A 517 ? 1.6202 0.6166 0.6789 -0.2377 -0.4216 0.1094 548 LEU B CA 4008 C C . LEU A 517 ? 1.6180 0.6236 0.6718 -0.2452 -0.4126 0.1109 548 LEU B C 4009 O O . LEU A 517 ? 1.6048 0.6413 0.6925 -0.2286 -0.4082 0.1039 548 LEU B O 4010 C CB . LEU A 517 ? 1.5967 0.6144 0.6563 -0.2353 -0.3876 0.1033 548 LEU B CB 4011 C CG . LEU A 517 ? 1.5918 0.6081 0.6589 -0.2265 -0.3882 0.1000 548 LEU B CG 4012 C CD1 . LEU A 517 ? 1.5700 0.6142 0.6450 -0.2212 -0.3531 0.0926 548 LEU B CD1 4013 C CD2 . LEU A 517 ? 1.6280 0.6003 0.6530 -0.2490 -0.4049 0.1105 548 LEU B CD2 4014 N N . ASN A 518 ? 1.8281 0.8071 0.8379 -0.2719 -0.4087 0.1196 549 ASN B N 4015 C CA . ASN A 518 ? 1.8303 0.8107 0.8278 -0.2835 -0.4025 0.1224 549 ASN B CA 4016 C C . ASN A 518 ? 1.8289 0.7970 0.7850 -0.3087 -0.3787 0.1254 549 ASN B C 4017 O O . ASN A 518 ? 1.8206 0.7893 0.7667 -0.3126 -0.3615 0.1226 549 ASN B O 4018 C CB . ASN A 518 ? 1.8523 0.8049 0.8394 -0.2914 -0.4373 0.1311 549 ASN B CB 4019 C CG . ASN A 518 ? 1.8781 0.7864 0.8303 -0.3091 -0.4624 0.1415 549 ASN B CG 4020 O OD1 . ASN A 518 ? 1.8856 0.7849 0.8545 -0.2969 -0.4863 0.1415 549 ASN B OD1 4021 N ND2 . ASN A 518 ? 1.8969 0.7876 0.8175 -0.3370 -0.4517 0.1447 549 ASN B ND2 4022 N N . GLY A 519 ? 1.8511 0.8105 0.7856 -0.3253 -0.3767 0.1297 550 GLY B N 4023 C CA . GLY A 519 ? 1.8508 0.8026 0.7521 -0.3493 -0.3531 0.1294 550 GLY B CA 4024 C C . GLY A 519 ? 1.8267 0.8113 0.7445 -0.3389 -0.3197 0.1199 550 GLY B C 4025 O O . GLY A 519 ? 1.8132 0.8280 0.7696 -0.3164 -0.3149 0.1141 550 GLY B O 4026 N N . ILE A 520 ? 1.6522 0.6338 0.5459 -0.3550 -0.2960 0.1167 551 ILE B N 4027 C CA . ILE A 520 ? 1.6137 0.6266 0.5272 -0.3450 -0.2643 0.1063 551 ILE B CA 4028 C C . ILE A 520 ? 1.5956 0.6184 0.5198 -0.3359 -0.2514 0.1005 551 ILE B C 4029 O O . ILE A 520 ? 1.6140 0.6185 0.5279 -0.3385 -0.2662 0.1046 551 ILE B O 4030 C CB . ILE A 520 ? 1.6241 0.6337 0.5109 -0.3664 -0.2429 0.1033 551 ILE B CB 4031 C CG1 . ILE A 520 ? 1.6561 0.6456 0.5186 -0.3922 -0.2422 0.1019 551 ILE B CG1 4032 C CG2 . ILE A 520 ? 1.6280 0.6390 0.5157 -0.3691 -0.2493 0.1063 551 ILE B CG2 4033 C CD1 . ILE A 520 ? 1.6494 0.6439 0.5066 -0.3969 -0.2211 0.0944 551 ILE B CD1 4034 N N . ILE A 521 ? 1.5715 0.6223 0.5158 -0.3260 -0.2244 0.0912 552 ILE B N 4035 C CA . ILE A 521 ? 1.5548 0.6208 0.5143 -0.3153 -0.2080 0.0842 552 ILE B CA 4036 C C . ILE A 521 ? 1.5531 0.6130 0.4863 -0.3355 -0.1851 0.0788 552 ILE B C 4037 O O . ILE A 521 ? 1.5415 0.6164 0.4800 -0.3371 -0.1651 0.0724 552 ILE B O 4038 C CB . ILE A 521 ? 1.5324 0.6350 0.5333 -0.2913 -0.1935 0.0770 552 ILE B CB 4039 C CG1 . ILE A 521 ? 1.5348 0.6492 0.5650 -0.2713 -0.2134 0.0798 552 ILE B CG1 4040 C CG2 . ILE A 521 ? 1.5161 0.6351 0.5323 -0.2812 -0.1750 0.0696 552 ILE B CG2 4041 C CD1 . ILE A 521 ? 1.5181 0.6667 0.5829 -0.2532 -0.2003 0.0740 552 ILE B CD1 4042 N N . PRO A 522 ? 1.5743 0.6130 0.4804 -0.3510 -0.1878 0.0806 553 PRO B N 4043 C CA . PRO A 522 ? 1.5958 0.6236 0.4694 -0.3764 -0.1699 0.0758 553 PRO B CA 4044 C C . PRO A 522 ? 1.5653 0.6192 0.4571 -0.3703 -0.1393 0.0628 553 PRO B C 4045 O O . PRO A 522 ? 1.5354 0.6078 0.4556 -0.3506 -0.1328 0.0587 553 PRO B O 4046 C CB . PRO A 522 ? 1.6164 0.6275 0.4784 -0.3856 -0.1795 0.0779 553 PRO B CB 4047 C CG . PRO A 522 ? 1.6002 0.6145 0.4822 -0.3618 -0.1952 0.0828 553 PRO B CG 4048 C CD . PRO A 522 ? 1.5855 0.6101 0.4914 -0.3454 -0.2084 0.0864 553 PRO B CD 4049 N N . TRP A 523 ? 1.8601 0.9146 0.7360 -0.3872 -0.1219 0.0562 554 TRP B N 4050 C CA . TRP A 523 ? 1.8417 0.9201 0.7368 -0.3815 -0.0943 0.0429 554 TRP B CA 4051 C C . TRP A 523 ? 1.8361 0.9186 0.7320 -0.3826 -0.0813 0.0355 554 TRP B C 4052 O O . TRP A 523 ? 1.8191 0.9233 0.7391 -0.3716 -0.0619 0.0251 554 TRP B O 4053 C CB . TRP A 523 ? 1.8455 0.9209 0.7209 -0.4021 -0.0798 0.0360 554 TRP B CB 4054 C CG . TRP A 523 ? 1.8580 0.9275 0.7151 -0.4267 -0.0649 0.0271 554 TRP B CG 4055 C CD1 . TRP A 523 ? 1.8483 0.9298 0.7109 -0.4281 -0.0438 0.0147 554 TRP B CD1 4056 C CD2 . TRP A 523 ? 1.8882 0.9420 0.7243 -0.4531 -0.0691 0.0291 554 TRP B CD2 4057 N NE1 . TRP A 523 ? 1.8698 0.9454 0.7171 -0.4535 -0.0343 0.0097 554 TRP B NE1 4058 C CE2 . TRP A 523 ? 1.8964 0.9546 0.7262 -0.4697 -0.0493 0.0187 554 TRP B CE2 4059 C CE3 . TRP A 523 ? 1.9118 0.9485 0.7344 -0.4646 -0.0880 0.0386 554 TRP B CE3 4060 C CZ2 . TRP A 523 ? 1.9293 0.9759 0.7387 -0.4980 -0.0471 0.0185 554 TRP B CZ2 4061 C CZ3 . TRP A 523 ? 1.9452 0.9685 0.7466 -0.4927 -0.0869 0.0378 554 TRP B CZ3 4062 C CH2 . TRP A 523 ? 1.9540 0.9823 0.7485 -0.5096 -0.0662 0.0283 554 TRP B CH2 4063 N N . GLU A 524 ? 1.8675 0.9279 0.7361 -0.3969 -0.0933 0.0413 555 GLU B N 4064 C CA . GLU A 524 ? 1.8667 0.9275 0.7319 -0.4017 -0.0834 0.0354 555 GLU B CA 4065 C C . GLU A 524 ? 1.8463 0.9293 0.7488 -0.3739 -0.0779 0.0318 555 GLU B C 4066 O O . GLU A 524 ? 1.8352 0.9302 0.7459 -0.3734 -0.0596 0.0217 555 GLU B O 4067 C CB . GLU A 524 ? 1.8936 0.9311 0.7404 -0.4178 -0.1021 0.0439 555 GLU B CB 4068 C CG . GLU A 524 ? 1.9237 0.9487 0.7483 -0.4493 -0.0980 0.0418 555 GLU B CG 4069 C CD . GLU A 524 ? 1.9408 0.9557 0.7568 -0.4585 -0.1104 0.0476 555 GLU B CD 4070 O OE1 . GLU A 524 ? 1.9315 0.9450 0.7569 -0.4421 -0.1274 0.0554 555 GLU B OE1 4071 O OE2 . GLU A 524 ? 1.9647 0.9735 0.7645 -0.4832 -0.1028 0.0442 555 GLU B OE2 4072 N N . ILE A 525 ? 1.5136 0.6040 0.4414 -0.3511 -0.0932 0.0391 556 ILE B N 4073 C CA . ILE A 525 ? 1.4823 0.5962 0.4481 -0.3244 -0.0884 0.0358 556 ILE B CA 4074 C C . ILE A 525 ? 1.4554 0.5956 0.4470 -0.3145 -0.0647 0.0247 556 ILE B C 4075 O O . ILE A 525 ? 1.4342 0.5913 0.4497 -0.2994 -0.0554 0.0194 556 ILE B O 4076 C CB . ILE A 525 ? 1.4739 0.5944 0.4630 -0.3032 -0.1077 0.0437 556 ILE B CB 4077 C CG1 . ILE A 525 ? 1.5010 0.5949 0.4679 -0.3120 -0.1344 0.0548 556 ILE B CG1 4078 C CG2 . ILE A 525 ? 1.4518 0.5910 0.4721 -0.2801 -0.1063 0.0412 556 ILE B CG2 4079 C CD1 . ILE A 525 ? 1.4910 0.5932 0.4855 -0.2887 -0.1538 0.0599 556 ILE B CD1 4080 N N . SER A 526 ? 1.5095 0.6526 0.4970 -0.3227 -0.0558 0.0211 557 SER B N 4081 C CA . SER A 526 ? 1.4923 0.6571 0.5028 -0.3152 -0.0345 0.0101 557 SER B CA 4082 C C . SER A 526 ? 1.4826 0.6508 0.4909 -0.3222 -0.0170 -0.0012 557 SER B C 4083 O O . SER A 526 ? 1.4639 0.6513 0.4979 -0.3107 -0.0018 -0.0103 557 SER B O 4084 C CB . SER A 526 ? 1.5004 0.6631 0.5008 -0.3277 -0.0278 0.0068 557 SER B CB 4085 O OG . SER A 526 ? 1.4824 0.6505 0.4804 -0.3387 -0.0064 -0.0071 557 SER B OG 4086 N N . THR A 527 ? 1.4515 0.6006 0.4288 -0.3419 -0.0199 -0.0004 558 THR B N 4087 C CA . THR A 527 ? 1.4574 0.6084 0.4280 -0.3528 -0.0037 -0.0115 558 THR B CA 4088 C C . THR A 527 ? 1.4511 0.6019 0.4273 -0.3445 -0.0081 -0.0093 558 THR B C 4089 O O . THR A 527 ? 1.4591 0.6102 0.4271 -0.3556 0.0044 -0.0181 558 THR B O 4090 C CB . THR A 527 ? 1.4973 0.6295 0.4279 -0.3840 -0.0002 -0.0145 558 THR B CB 4091 O OG1 . THR A 527 ? 1.5254 0.6330 0.4281 -0.3938 -0.0232 0.0002 558 THR B OG1 4092 C CG2 . THR A 527 ? 1.4998 0.6382 0.4295 -0.3931 0.0131 -0.0235 558 THR B CG2 4093 N N . LEU A 528 ? 1.6560 0.8064 0.6455 -0.3263 -0.0257 0.0014 559 LEU B N 4094 C CA . LEU A 528 ? 1.6500 0.8040 0.6510 -0.3148 -0.0286 0.0021 559 LEU B CA 4095 C C . LEU A 528 ? 1.6264 0.8066 0.6618 -0.2974 -0.0107 -0.0081 559 LEU B C 4096 O O . LEU A 528 ? 1.6152 0.8118 0.6774 -0.2792 -0.0105 -0.0073 559 LEU B O 4097 C CB . LEU A 528 ? 1.6552 0.8040 0.6648 -0.2988 -0.0519 0.0143 559 LEU B CB 4098 C CG . LEU A 528 ? 1.6779 0.7983 0.6559 -0.3139 -0.0740 0.0254 559 LEU B CG 4099 C CD1 . LEU A 528 ? 1.6812 0.7973 0.6710 -0.2975 -0.0954 0.0338 559 LEU B CD1 4100 C CD2 . LEU A 528 ? 1.6931 0.7932 0.6337 -0.3420 -0.0694 0.0234 559 LEU B CD2 4101 N N . PRO A 529 ? 1.4088 0.5928 0.4429 -0.3041 0.0038 -0.0179 560 PRO B N 4102 C CA . PRO A 529 ? 1.3859 0.5922 0.4486 -0.2933 0.0228 -0.0302 560 PRO B CA 4103 C C . PRO A 529 ? 1.3681 0.5919 0.4649 -0.2664 0.0200 -0.0278 560 PRO B C 4104 O O . PRO A 529 ? 1.3514 0.5939 0.4752 -0.2541 0.0312 -0.0347 560 PRO B O 4105 C CB . PRO A 529 ? 1.3887 0.5898 0.4344 -0.3113 0.0348 -0.0398 560 PRO B CB 4106 C CG . PRO A 529 ? 1.4231 0.6001 0.4279 -0.3367 0.0265 -0.0345 560 PRO B CG 4107 C CD . PRO A 529 ? 1.4264 0.5912 0.4271 -0.3271 0.0027 -0.0182 560 PRO B CD 4108 N N . SER A 530 ? 1.4300 0.6478 0.5255 -0.2583 0.0055 -0.0192 561 SER B N 4109 C CA . SER A 530 ? 1.4166 0.6517 0.5432 -0.2337 0.0022 -0.0171 561 SER B CA 4110 C C . SER A 530 ? 1.4203 0.6594 0.5589 -0.2182 -0.0144 -0.0069 561 SER B C 4111 O O . SER A 530 ? 1.4107 0.6657 0.5744 -0.1989 -0.0167 -0.0059 561 SER B O 4112 C CB . SER A 530 ? 1.4127 0.6463 0.5401 -0.2309 0.0021 -0.0186 561 SER B CB 4113 O OG . SER A 530 ? 1.4040 0.6434 0.5326 -0.2395 0.0206 -0.0305 561 SER B OG 4114 N N . ILE A 531 ? 1.3910 0.6170 0.5123 -0.2271 -0.0254 -0.0005 562 ILE B N 4115 C CA . ILE A 531 ? 1.3970 0.6233 0.5257 -0.2153 -0.0443 0.0089 562 ILE B CA 4116 C C . ILE A 531 ? 1.3836 0.6349 0.5458 -0.1933 -0.0437 0.0090 562 ILE B C 4117 O O . ILE A 531 ? 1.3743 0.6388 0.5487 -0.1909 -0.0322 0.0053 562 ILE B O 4118 C CB . ILE A 531 ? 1.4121 0.6234 0.5198 -0.2289 -0.0530 0.0142 562 ILE B CB 4119 C CG1 . ILE A 531 ? 1.4188 0.6285 0.5335 -0.2179 -0.0746 0.0230 562 ILE B CG1 4120 C CG2 . ILE A 531 ? 1.4050 0.6272 0.5192 -0.2319 -0.0386 0.0091 562 ILE B CG2 4121 C CD1 . ILE A 531 ? 1.4331 0.6233 0.5330 -0.2213 -0.0925 0.0285 562 ILE B CD1 4122 N N . ALA A 532 ? 1.3249 0.5826 0.5015 -0.1780 -0.0568 0.0130 563 ALA B N 4123 C CA . ALA A 532 ? 1.3109 0.5944 0.5186 -0.1583 -0.0554 0.0122 563 ALA B CA 4124 C C . ALA A 532 ? 1.3188 0.6083 0.5356 -0.1500 -0.0709 0.0175 563 ALA B C 4125 O O . ALA A 532 ? 1.3141 0.6168 0.5417 -0.1467 -0.0673 0.0178 563 ALA B O 4126 C CB . ALA A 532 ? 1.2995 0.5939 0.5235 -0.1454 -0.0536 0.0092 563 ALA B CB 4127 N N . ASP A 533 ? 1.4279 0.7082 0.6418 -0.1463 -0.0886 0.0209 564 ASP B N 4128 C CA . ASP A 533 ? 1.4394 0.7271 0.6660 -0.1367 -0.1048 0.0240 564 ASP B CA 4129 C C . ASP A 533 ? 1.4588 0.7216 0.6622 -0.1496 -0.1208 0.0299 564 ASP B C 4130 O O . ASP A 533 ? 1.4735 0.7127 0.6556 -0.1598 -0.1284 0.0324 564 ASP B O 4131 C CB . ASP A 533 ? 1.4456 0.7426 0.6908 -0.1209 -0.1157 0.0221 564 ASP B CB 4132 C CG . ASP A 533 ? 1.4277 0.7544 0.7003 -0.1057 -0.1039 0.0170 564 ASP B CG 4133 O OD1 . ASP A 533 ? 1.4077 0.7449 0.6835 -0.1081 -0.0870 0.0154 564 ASP B OD1 4134 O OD2 . ASP A 533 ? 1.4350 0.7737 0.7258 -0.0919 -0.1123 0.0143 564 ASP B OD2 4135 N N . VAL A 534 ? 1.3569 0.6241 0.5636 -0.1499 -0.1268 0.0324 565 VAL B N 4136 C CA . VAL A 534 ? 1.3764 0.6206 0.5636 -0.1606 -0.1451 0.0385 565 VAL B CA 4137 C C . VAL A 534 ? 1.3807 0.6386 0.5892 -0.1482 -0.1606 0.0392 565 VAL B C 4138 O O . VAL A 534 ? 1.3736 0.6506 0.5956 -0.1441 -0.1533 0.0379 565 VAL B O 4139 C CB . VAL A 534 ? 1.3793 0.6096 0.5414 -0.1799 -0.1361 0.0409 565 VAL B CB 4140 C CG1 . VAL A 534 ? 1.3970 0.6092 0.5440 -0.1888 -0.1550 0.0473 565 VAL B CG1 4141 C CG2 . VAL A 534 ? 1.3835 0.5959 0.5204 -0.1958 -0.1250 0.0395 565 VAL B CG2 4142 N N . ASP A 535 ? 1.3939 0.6429 0.6069 -0.1421 -0.1823 0.0405 566 ASP B N 4143 C CA . ASP A 535 ? 1.4003 0.6642 0.6361 -0.1303 -0.1970 0.0392 566 ASP B CA 4144 C C . ASP A 535 ? 1.4172 0.6539 0.6348 -0.1407 -0.2197 0.0456 566 ASP B C 4145 O O . ASP A 535 ? 1.4263 0.6422 0.6364 -0.1416 -0.2385 0.0480 566 ASP B O 4146 C CB . ASP A 535 ? 1.3986 0.6826 0.6651 -0.1103 -0.2044 0.0325 566 ASP B CB 4147 C CG . ASP A 535 ? 1.4043 0.7112 0.6994 -0.0972 -0.2159 0.0280 566 ASP B CG 4148 O OD1 . ASP A 535 ? 1.4017 0.7262 0.7039 -0.0979 -0.2064 0.0277 566 ASP B OD1 4149 O OD2 . ASP A 535 ? 1.4114 0.7193 0.7231 -0.0862 -0.2349 0.0241 566 ASP B OD2 4150 N N . LEU A 536 ? 1.4681 0.7043 0.6784 -0.1489 -0.2186 0.0488 567 LEU B N 4151 C CA . LEU A 536 ? 1.4853 0.6968 0.6777 -0.1602 -0.2394 0.0555 567 LEU B CA 4152 C C . LEU A 536 ? 1.4949 0.7197 0.7117 -0.1489 -0.2573 0.0537 567 LEU B C 4153 O O . LEU A 536 ? 1.5076 0.7139 0.7098 -0.1591 -0.2723 0.0594 567 LEU B O 4154 C CB . LEU A 536 ? 1.4868 0.6809 0.6469 -0.1816 -0.2283 0.0609 567 LEU B CB 4155 C CG . LEU A 536 ? 1.4796 0.6601 0.6153 -0.1945 -0.2117 0.0610 567 LEU B CG 4156 C CD1 . LEU A 536 ? 1.4836 0.6471 0.5878 -0.2166 -0.2020 0.0646 567 LEU B CD1 4157 C CD2 . LEU A 536 ? 1.4894 0.6464 0.6118 -0.1977 -0.2269 0.0638 567 LEU B CD2 4158 N N . SER A 537 ? 1.3999 0.6580 0.6531 -0.1295 -0.2547 0.0455 568 SER B N 4159 C CA . SER A 537 ? 1.3985 0.6766 0.6776 -0.1196 -0.2664 0.0417 568 SER B CA 4160 C C . SER A 537 ? 1.4179 0.6817 0.7055 -0.1150 -0.2983 0.0417 568 SER B C 4161 O O . SER A 537 ? 1.4321 0.6729 0.7121 -0.1151 -0.3149 0.0435 568 SER B O 4162 C CB . SER A 537 ? 1.3735 0.6943 0.6879 -0.1026 -0.2520 0.0319 568 SER B CB 4163 O OG . SER A 537 ? 1.3617 0.6904 0.6833 -0.0944 -0.2422 0.0276 568 SER B OG 4164 N N . HIS A 538 ? 1.5386 0.8160 0.8424 -0.1114 -0.3072 0.0397 569 HIS B N 4165 C CA . HIS A 538 ? 1.5501 0.8200 0.8691 -0.1051 -0.3374 0.0377 569 HIS B CA 4166 C C . HIS A 538 ? 1.5640 0.7887 0.8517 -0.1202 -0.3609 0.0483 569 HIS B C 4167 O O . HIS A 538 ? 1.5714 0.7786 0.8647 -0.1150 -0.3861 0.0477 569 HIS B O 4168 C CB . HIS A 538 ? 1.5467 0.8376 0.9025 -0.0843 -0.3472 0.0259 569 HIS B CB 4169 C CG . HIS A 538 ? 1.5369 0.8749 0.9273 -0.0702 -0.3305 0.0145 569 HIS B CG 4170 N ND1 . HIS A 538 ? 1.5244 0.8836 0.9187 -0.0664 -0.3052 0.0112 569 HIS B ND1 4171 C CD2 . HIS A 538 ? 1.5382 0.9063 0.9593 -0.0610 -0.3349 0.0060 569 HIS B CD2 4172 C CE1 . HIS A 538 ? 1.5194 0.9188 0.9437 -0.0559 -0.2954 0.0017 569 HIS B CE1 4173 N NE2 . HIS A 538 ? 1.5275 0.9341 0.9688 -0.0527 -0.3124 -0.0021 569 HIS B NE2 4174 N N . ASN A 539 ? 1.6412 0.8468 0.8956 -0.1395 -0.3534 0.0578 570 ASN B N 4175 C CA . ASN A 539 ? 1.6563 0.8188 0.8756 -0.1578 -0.3734 0.0689 570 ASN B CA 4176 C C . ASN A 539 ? 1.6652 0.8199 0.8711 -0.1701 -0.3783 0.0747 570 ASN B C 4177 O O . ASN A 539 ? 1.6605 0.8438 0.8874 -0.1631 -0.3689 0.0698 570 ASN B O 4178 C CB . ASN A 539 ? 1.6549 0.7919 0.8356 -0.1749 -0.3601 0.0758 570 ASN B CB 4179 C CG . ASN A 539 ? 1.6516 0.7823 0.8377 -0.1667 -0.3656 0.0731 570 ASN B CG 4180 O OD1 . ASN A 539 ? 1.6659 0.7622 0.8285 -0.1772 -0.3843 0.0800 570 ASN B OD1 4181 N ND2 . ASN A 539 ? 1.6329 0.7966 0.8496 -0.1487 -0.3502 0.0633 570 ASN B ND2 4182 N N . LEU A 540 ? 1.7413 0.8561 0.9110 -0.1893 -0.3946 0.0854 571 LEU B N 4183 C CA . LEU A 540 ? 1.7527 0.8529 0.9019 -0.2048 -0.4009 0.0926 571 LEU B CA 4184 C C . LEU A 540 ? 1.7500 0.8395 0.8615 -0.2260 -0.3761 0.0981 571 LEU B C 4185 O O . LEU A 540 ? 1.7603 0.8331 0.8472 -0.2428 -0.3796 0.1048 571 LEU B O 4186 C CB . LEU A 540 ? 1.7734 0.8363 0.9069 -0.2137 -0.4371 0.1008 571 LEU B CB 4187 C CG . LEU A 540 ? 1.7758 0.8517 0.9513 -0.1926 -0.4639 0.0937 571 LEU B CG 4188 C CD1 . LEU A 540 ? 1.7633 0.8833 0.9764 -0.1773 -0.4505 0.0838 571 LEU B CD1 4189 C CD2 . LEU A 540 ? 1.7721 0.8502 0.9688 -0.1766 -0.4736 0.0874 571 LEU B CD2 4190 N N . LEU A 541 ? 1.6288 0.7280 0.7368 -0.2251 -0.3519 0.0945 572 LEU B N 4191 C CA . LEU A 541 ? 1.6213 0.7140 0.6984 -0.2434 -0.3265 0.0969 572 LEU B CA 4192 C C . LEU A 541 ? 1.6168 0.7232 0.6943 -0.2482 -0.3140 0.0966 572 LEU B C 4193 O O . LEU A 541 ? 1.6073 0.7454 0.7170 -0.2324 -0.3067 0.0905 572 LEU B O 4194 C CB . LEU A 541 ? 1.6008 0.7152 0.6902 -0.2341 -0.3003 0.0896 572 LEU B CB 4195 C CG . LEU A 541 ? 1.6043 0.7013 0.6770 -0.2393 -0.2991 0.0905 572 LEU B CG 4196 C CD1 . LEU A 541 ? 1.5811 0.7069 0.6791 -0.2229 -0.2778 0.0818 572 LEU B CD1 4197 C CD2 . LEU A 541 ? 1.6058 0.6758 0.6338 -0.2663 -0.2897 0.0959 572 LEU B CD2 4198 N N . THR A 542 ? 1.7656 0.8482 0.8062 -0.2713 -0.3112 0.1028 573 THR B N 4199 C CA . THR A 542 ? 1.7612 0.8545 0.7993 -0.2775 -0.2985 0.1023 573 THR B CA 4200 C C . THR A 542 ? 1.7590 0.8360 0.7600 -0.3003 -0.2792 0.1036 573 THR B C 4201 O O . THR A 542 ? 1.7698 0.8184 0.7387 -0.3172 -0.2850 0.1081 573 THR B O 4202 C CB . THR A 542 ? 1.7787 0.8607 0.8150 -0.2815 -0.3228 0.1082 573 THR B CB 4203 O OG1 . THR A 542 ? 1.7717 0.8670 0.8082 -0.2863 -0.3090 0.1071 573 THR B OG1 4204 C CG2 . THR A 542 ? 1.8009 0.8397 0.7969 -0.3034 -0.3446 0.1182 573 THR B CG2 4205 N N . GLY A 543 ? 1.5444 0.6399 0.5502 -0.3013 -0.2562 0.0989 574 GLY B N 4206 C CA . GLY A 543 ? 1.5481 0.6335 0.5251 -0.3202 -0.2350 0.0967 574 GLY B CA 4207 C C . GLY A 543 ? 1.5199 0.6351 0.5200 -0.3094 -0.2088 0.0883 574 GLY B C 4208 O O . GLY A 543 ? 1.5030 0.6428 0.5337 -0.2929 -0.2083 0.0864 574 GLY B O 4209 N N . THR A 544 ? 1.6406 0.7539 0.6266 -0.3193 -0.1874 0.0828 575 THR B N 4210 C CA . THR A 544 ? 1.6244 0.7630 0.6314 -0.3099 -0.1632 0.0746 575 THR B CA 4211 C C . THR A 544 ? 1.6114 0.7600 0.6314 -0.2995 -0.1521 0.0692 575 THR B C 4212 O O . THR A 544 ? 1.6189 0.7508 0.6226 -0.3058 -0.1583 0.0708 575 THR B O 4213 C CB . THR A 544 ? 1.6289 0.7595 0.6131 -0.3290 -0.1456 0.0700 575 THR B CB 4214 O OG1 . THR A 544 ? 1.6164 0.7652 0.6168 -0.3220 -0.1224 0.0607 575 THR B OG1 4215 C CG2 . THR A 544 ? 1.6474 0.7481 0.5912 -0.3531 -0.1496 0.0720 575 THR B CG2 4216 N N . ILE A 545 ? 1.5408 0.7160 0.5895 -0.2841 -0.1368 0.0633 576 ILE B N 4217 C CA . ILE A 545 ? 1.5277 0.7136 0.5887 -0.2753 -0.1231 0.0572 576 ILE B CA 4218 C C . ILE A 545 ? 1.5231 0.7036 0.5683 -0.2895 -0.1019 0.0497 576 ILE B C 4219 O O . ILE A 545 ? 1.5169 0.7069 0.5685 -0.2910 -0.0898 0.0457 576 ILE B O 4220 C CB . ILE A 545 ? 1.5133 0.7296 0.6118 -0.2530 -0.1176 0.0545 576 ILE B CB 4221 C CG1 . ILE A 545 ? 1.5205 0.7447 0.6366 -0.2388 -0.1376 0.0592 576 ILE B CG1 4222 C CG2 . ILE A 545 ? 1.5004 0.7263 0.6096 -0.2458 -0.1026 0.0481 576 ILE B CG2 4223 C CD1 . ILE A 545 ? 1.5103 0.7653 0.6615 -0.2186 -0.1329 0.0560 576 ILE B CD1 4224 N N . PRO A 546 ? 1.5212 0.6873 0.5473 -0.3001 -0.0978 0.0471 577 PRO B N 4225 C CA . PRO A 546 ? 1.5222 0.6790 0.5269 -0.3185 -0.0804 0.0391 577 PRO B CA 4226 C C . PRO A 546 ? 1.5076 0.6831 0.5315 -0.3133 -0.0587 0.0289 577 PRO B C 4227 O O . PRO A 546 ? 1.4931 0.6881 0.5456 -0.2952 -0.0526 0.0262 577 PRO B O 4228 C CB . PRO A 546 ? 1.5231 0.6723 0.5197 -0.3205 -0.0799 0.0376 577 PRO B CB 4229 C CG . PRO A 546 ? 1.5334 0.6738 0.5300 -0.3131 -0.1035 0.0478 577 PRO B CG 4230 C CD . PRO A 546 ? 1.5265 0.6853 0.5519 -0.2942 -0.1114 0.0513 577 PRO B CD 4231 N N . SER A 547 ? 1.5272 0.6957 0.5346 -0.3300 -0.0478 0.0228 578 SER B N 4232 C CA . SER A 547 ? 1.5178 0.7010 0.5421 -0.3271 -0.0291 0.0123 578 SER B CA 4233 C C . SER A 547 ? 1.5022 0.7003 0.5491 -0.3147 -0.0159 0.0042 578 SER B C 4234 O O . SER A 547 ? 1.4897 0.7061 0.5662 -0.2965 -0.0132 0.0041 578 SER B O 4235 C CB . SER A 547 ? 1.5286 0.6989 0.5268 -0.3508 -0.0182 0.0038 578 SER B CB 4236 O OG . SER A 547 ? 1.5210 0.7039 0.5362 -0.3485 -0.0017 -0.0074 578 SER B OG 4237 N N . ASP A 548 ? 1.6466 0.8364 0.6783 -0.3254 -0.0089 -0.0019 579 ASP B N 4238 C CA . ASP A 548 ? 1.6328 0.8344 0.6812 -0.3198 0.0075 -0.0134 579 ASP B CA 4239 C C . ASP A 548 ? 1.6211 0.8344 0.6918 -0.2999 0.0033 -0.0094 579 ASP B C 4240 O O . ASP A 548 ? 1.6088 0.8326 0.6956 -0.2933 0.0154 -0.0180 579 ASP B O 4241 C CB . ASP A 548 ? 1.6394 0.8286 0.6612 -0.3422 0.0183 -0.0232 579 ASP B CB 4242 C CG . ASP A 548 ? 1.6603 0.8264 0.6446 -0.3607 0.0044 -0.0141 579 ASP B CG 4243 O OD1 . ASP A 548 ? 1.6673 0.8276 0.6507 -0.3522 -0.0143 -0.0008 579 ASP B OD1 4244 O OD2 . ASP A 548 ? 1.6705 0.8242 0.6263 -0.3843 0.0116 -0.0207 579 ASP B OD2 4245 N N . PHE A 549 ? 1.3796 0.5918 0.4527 -0.2900 -0.0142 0.0027 580 PHE B N 4246 C CA . PHE A 549 ? 1.3667 0.5904 0.4607 -0.2711 -0.0200 0.0067 580 PHE B CA 4247 C C . PHE A 549 ? 1.3479 0.5944 0.4754 -0.2530 -0.0101 0.0022 580 PHE B C 4248 O O . PHE A 549 ? 1.3366 0.5920 0.4786 -0.2420 -0.0073 0.0003 580 PHE B O 4249 C CB . PHE A 549 ? 1.3745 0.5959 0.4692 -0.2632 -0.0406 0.0185 580 PHE B CB 4250 C CG . PHE A 549 ? 1.3792 0.5917 0.4669 -0.2608 -0.0523 0.0230 580 PHE B CG 4251 C CD1 . PHE A 549 ? 1.3671 0.5936 0.4767 -0.2443 -0.0504 0.0214 580 PHE B CD1 4252 C CD2 . PHE A 549 ? 1.4006 0.5895 0.4590 -0.2758 -0.0659 0.0289 580 PHE B CD2 4253 C CE1 . PHE A 549 ? 1.3719 0.5897 0.4757 -0.2418 -0.0617 0.0251 580 PHE B CE1 4254 C CE2 . PHE A 549 ? 1.4082 0.5868 0.4601 -0.2739 -0.0784 0.0332 580 PHE B CE2 4255 C CZ . PHE A 549 ? 1.3899 0.5834 0.4653 -0.2563 -0.0760 0.0310 580 PHE B CZ 4256 N N . GLY A 550 ? 1.4655 0.7205 0.6046 -0.2505 -0.0058 0.0010 581 GLY B N 4257 C CA . GLY A 550 ? 1.4535 0.7278 0.6224 -0.2353 0.0017 -0.0022 581 GLY B CA 4258 C C . GLY A 550 ? 1.4441 0.7214 0.6210 -0.2365 0.0176 -0.0141 581 GLY B C 4259 O O . GLY A 550 ? 1.4342 0.7259 0.6360 -0.2239 0.0230 -0.0169 581 GLY B O 4260 N N . SER A 551 ? 1.6846 0.9487 0.8408 -0.2525 0.0247 -0.0215 582 SER B N 4261 C CA . SER A 551 ? 1.6754 0.9436 0.8402 -0.2552 0.0407 -0.0353 582 SER B CA 4262 C C . SER A 551 ? 1.6679 0.9394 0.8377 -0.2486 0.0420 -0.0365 582 SER B C 4263 O O . SER A 551 ? 1.6613 0.9362 0.8376 -0.2511 0.0546 -0.0481 582 SER B O 4264 C CB . SER A 551 ? 1.6823 0.9381 0.8243 -0.2770 0.0505 -0.0457 582 SER B CB 4265 O OG . SER A 551 ? 1.6628 0.9268 0.8221 -0.2773 0.0652 -0.0602 582 SER B OG 4266 N N . SER A 552 ? 1.3037 0.5748 0.4718 -0.2400 0.0288 -0.0253 583 SER B N 4267 C CA . SER A 552 ? 1.2987 0.5708 0.4688 -0.2346 0.0281 -0.0255 583 SER B CA 4268 C C . SER A 552 ? 1.2847 0.5751 0.4850 -0.2141 0.0286 -0.0244 583 SER B C 4269 O O . SER A 552 ? 1.2826 0.5820 0.4953 -0.2017 0.0192 -0.0161 583 SER B O 4270 C CB . SER A 552 ? 1.3108 0.5700 0.4610 -0.2378 0.0122 -0.0150 583 SER B CB 4271 O OG . SER A 552 ? 1.3057 0.5657 0.4588 -0.2318 0.0105 -0.0149 583 SER B OG 4272 N N . LYS A 553 ? 1.5507 0.8469 0.7623 -0.2114 0.0394 -0.0333 584 LYS B N 4273 C CA . LYS A 553 ? 1.5401 0.8527 0.7794 -0.1932 0.0401 -0.0326 584 LYS B CA 4274 C C . LYS A 553 ? 1.5395 0.8551 0.7803 -0.1827 0.0295 -0.0246 584 LYS B C 4275 O O . LYS A 553 ? 1.5331 0.8629 0.7951 -0.1677 0.0282 -0.0225 584 LYS B O 4276 C CB . LYS A 553 ? 1.5294 0.8476 0.7832 -0.1932 0.0546 -0.0456 584 LYS B CB 4277 C CG . LYS A 553 ? 1.5251 0.8405 0.7736 -0.1963 0.0596 -0.0512 584 LYS B CG 4278 C CD . LYS A 553 ? 1.5358 0.8340 0.7521 -0.2143 0.0578 -0.0509 584 LYS B CD 4279 C CE . LYS A 553 ? 1.5428 0.8319 0.7423 -0.2329 0.0657 -0.0587 584 LYS B CE 4280 N NZ . LYS A 553 ? 1.5577 0.8285 0.7224 -0.2508 0.0596 -0.0542 584 LYS B NZ 4281 N N . THR A 554 ? 1.2973 0.5988 0.5156 -0.1911 0.0214 -0.0204 585 THR B N 4282 C CA . THR A 554 ? 1.2960 0.5985 0.5161 -0.1814 0.0104 -0.0141 585 THR B CA 4283 C C . THR A 554 ? 1.3042 0.6073 0.5237 -0.1743 -0.0068 -0.0038 585 THR B C 4284 O O . THR A 554 ? 1.3036 0.6101 0.5293 -0.1643 -0.0157 -0.0004 585 THR B O 4285 C CB . THR A 554 ? 1.3017 0.5882 0.5003 -0.1931 0.0100 -0.0162 585 THR B CB 4286 O OG1 . THR A 554 ? 1.3190 0.5860 0.4888 -0.2101 0.0030 -0.0125 585 THR B OG1 4287 C CG2 . THR A 554 ? 1.2931 0.5820 0.4949 -0.1991 0.0269 -0.0279 585 THR B CG2 4288 N N . ILE A 555 ? 1.3645 0.6649 0.5783 -0.1786 -0.0121 0.0004 586 ILE B N 4289 C CA . ILE A 555 ? 1.3738 0.6755 0.5890 -0.1715 -0.0290 0.0086 586 ILE B CA 4290 C C . ILE A 555 ? 1.3669 0.6924 0.6096 -0.1550 -0.0294 0.0100 586 ILE B C 4291 O O . ILE A 555 ? 1.3636 0.6983 0.6152 -0.1546 -0.0226 0.0092 586 ILE B O 4292 C CB . ILE A 555 ? 1.3890 0.6779 0.5865 -0.1827 -0.0379 0.0135 586 ILE B CB 4293 C CG1 . ILE A 555 ? 1.3885 0.6642 0.5667 -0.2007 -0.0266 0.0087 586 ILE B CG1 4294 C CG2 . ILE A 555 ? 1.4074 0.6819 0.5912 -0.1847 -0.0560 0.0195 586 ILE B CG2 4295 C CD1 . ILE A 555 ? 1.3762 0.6641 0.5681 -0.1987 -0.0163 0.0054 586 ILE B CD1 4296 N N . THR A 556 ? 1.2818 0.6177 0.5378 -0.1419 -0.0369 0.0116 587 THR B N 4297 C CA . THR A 556 ? 1.2806 0.6395 0.5596 -0.1284 -0.0396 0.0134 587 THR B CA 4298 C C . THR A 556 ? 1.2928 0.6550 0.5738 -0.1245 -0.0556 0.0180 587 THR B C 4299 O O . THR A 556 ? 1.2919 0.6738 0.5899 -0.1165 -0.0574 0.0190 587 THR B O 4300 C CB . THR A 556 ? 1.2713 0.6459 0.5689 -0.1156 -0.0354 0.0105 587 THR B CB 4301 O OG1 . THR A 556 ? 1.2742 0.6412 0.5671 -0.1123 -0.0443 0.0104 587 THR B OG1 4302 C CG2 . THR A 556 ? 1.2603 0.6333 0.5593 -0.1191 -0.0199 0.0055 587 THR B CG2 4303 N N . THR A 557 ? 1.3470 0.6900 0.6107 -0.1312 -0.0676 0.0205 588 THR B N 4304 C CA . THR A 557 ? 1.3598 0.7047 0.6274 -0.1268 -0.0849 0.0238 588 THR B CA 4305 C C . THR A 557 ? 1.3716 0.6925 0.6152 -0.1409 -0.0952 0.0283 588 THR B C 4306 O O . THR A 557 ? 1.3760 0.6735 0.5971 -0.1521 -0.0977 0.0295 588 THR B O 4307 C CB . THR A 557 ? 1.3669 0.7177 0.6472 -0.1141 -0.0966 0.0222 588 THR B CB 4308 O OG1 . THR A 557 ? 1.3628 0.7431 0.6703 -0.0999 -0.0955 0.0194 588 THR B OG1 4309 C CG2 . THR A 557 ? 1.3785 0.7129 0.6497 -0.1164 -0.1174 0.0254 588 THR B CG2 4310 N N . PHE A 558 ? 1.4027 0.7297 0.6502 -0.1415 -0.1008 0.0309 589 PHE B N 4311 C CA . PHE A 558 ? 1.4155 0.7224 0.6438 -0.1527 -0.1141 0.0356 589 PHE B CA 4312 C C . PHE A 558 ? 1.4246 0.7473 0.6723 -0.1421 -0.1285 0.0366 589 PHE B C 4313 O O . PHE A 558 ? 1.4220 0.7642 0.6837 -0.1384 -0.1226 0.0359 589 PHE B O 4314 C CB . PHE A 558 ? 1.4113 0.7113 0.6247 -0.1665 -0.1023 0.0365 589 PHE B CB 4315 C CG . PHE A 558 ? 1.4244 0.6963 0.6075 -0.1843 -0.1101 0.0405 589 PHE B CG 4316 C CD1 . PHE A 558 ? 1.4256 0.6755 0.5847 -0.1971 -0.1074 0.0401 589 PHE B CD1 4317 C CD2 . PHE A 558 ? 1.4359 0.7040 0.6138 -0.1897 -0.1194 0.0447 589 PHE B CD2 4318 C CE1 . PHE A 558 ? 1.4390 0.6633 0.5681 -0.2155 -0.1143 0.0439 589 PHE B CE1 4319 C CE2 . PHE A 558 ? 1.4482 0.6902 0.5971 -0.2071 -0.1268 0.0487 589 PHE B CE2 4320 C CZ . PHE A 558 ? 1.4502 0.6701 0.5739 -0.2205 -0.1243 0.0485 589 PHE B CZ 4321 N N . ASN A 559 ? 1.3994 0.7142 0.6489 -0.1377 -0.1479 0.0376 590 ASN B N 4322 C CA . ASN A 559 ? 1.4089 0.7401 0.6788 -0.1281 -0.1614 0.0367 590 ASN B CA 4323 C C . ASN A 559 ? 1.4248 0.7326 0.6780 -0.1378 -0.1804 0.0419 590 ASN B C 4324 O O . ASN A 559 ? 1.4351 0.7250 0.6820 -0.1376 -0.1976 0.0433 590 ASN B O 4325 C CB . ASN A 559 ? 1.4119 0.7611 0.7078 -0.1108 -0.1695 0.0308 590 ASN B CB 4326 C CG . ASN A 559 ? 1.4162 0.7923 0.7399 -0.0994 -0.1783 0.0264 590 ASN B CG 4327 O OD1 . ASN A 559 ? 1.4174 0.8004 0.7417 -0.1041 -0.1770 0.0284 590 ASN B OD1 4328 N ND2 . ASN A 559 ? 1.4180 0.8108 0.7659 -0.0846 -0.1869 0.0195 590 ASN B ND2 4329 N N . VAL A 560 ? 1.3548 0.6622 0.6010 -0.1461 -0.1784 0.0450 591 VAL B N 4330 C CA . VAL A 560 ? 1.3772 0.6621 0.6058 -0.1571 -0.1959 0.0506 591 VAL B CA 4331 C C . VAL A 560 ? 1.3798 0.6800 0.6306 -0.1479 -0.2122 0.0492 591 VAL B C 4332 O O . VAL A 560 ? 1.3968 0.6815 0.6353 -0.1568 -0.2255 0.0539 591 VAL B O 4333 C CB . VAL A 560 ? 1.3866 0.6528 0.5856 -0.1764 -0.1854 0.0553 591 VAL B CB 4334 C CG1 . VAL A 560 ? 1.3958 0.6358 0.5665 -0.1894 -0.1807 0.0571 591 VAL B CG1 4335 C CG2 . VAL A 560 ? 1.3683 0.6564 0.5777 -0.1748 -0.1638 0.0523 591 VAL B CG2 4336 N N . SER A 561 ? 1.3630 0.6952 0.6465 -0.1310 -0.2099 0.0421 592 SER B N 4337 C CA . SER A 561 ? 1.3613 0.7166 0.6712 -0.1214 -0.2211 0.0380 592 SER B CA 4338 C C . SER A 561 ? 1.3800 0.7211 0.6938 -0.1190 -0.2489 0.0382 592 SER B C 4339 O O . SER A 561 ? 1.3915 0.7110 0.6971 -0.1186 -0.2623 0.0395 592 SER B O 4340 C CB . SER A 561 ? 1.3395 0.7330 0.6828 -0.1050 -0.2122 0.0289 592 SER B CB 4341 O OG . SER A 561 ? 1.3312 0.7233 0.6753 -0.0991 -0.2059 0.0263 592 SER B OG 4342 N N . TYR A 562 ? 1.5543 0.9076 0.8814 -0.1176 -0.2582 0.0370 593 TYR B N 4343 C CA . TYR A 562 ? 1.5677 0.9085 0.9011 -0.1154 -0.2858 0.0368 593 TYR B CA 4344 C C . TYR A 562 ? 1.5765 0.8728 0.8725 -0.1318 -0.2981 0.0473 593 TYR B C 4345 O O . TYR A 562 ? 1.5826 0.8569 0.8730 -0.1306 -0.3158 0.0486 593 TYR B O 4346 C CB . TYR A 562 ? 1.5684 0.9227 0.9316 -0.0977 -0.2996 0.0272 593 TYR B CB 4347 C CG . TYR A 562 ? 1.5612 0.9613 0.9610 -0.0830 -0.2881 0.0156 593 TYR B CG 4348 C CD1 . TYR A 562 ? 1.5487 0.9674 0.9525 -0.0789 -0.2657 0.0127 593 TYR B CD1 4349 C CD2 . TYR A 562 ? 1.5673 0.9924 0.9973 -0.0741 -0.2998 0.0073 593 TYR B CD2 4350 C CE1 . TYR A 562 ? 1.5435 1.0037 0.9781 -0.0676 -0.2553 0.0026 593 TYR B CE1 4351 C CE2 . TYR A 562 ? 1.5618 1.0304 1.0239 -0.0628 -0.2885 -0.0040 593 TYR B CE2 4352 C CZ . TYR A 562 ? 1.5505 1.0360 1.0134 -0.0602 -0.2662 -0.0058 593 TYR B CZ 4353 O OH . TYR A 562 ? 1.5463 1.0746 1.0385 -0.0509 -0.2551 -0.0166 593 TYR B OH 4354 N N . ASN A 563 ? 1.6384 0.9217 0.9084 -0.1480 -0.2886 0.0546 594 ASN B N 4355 C CA . ASN A 563 ? 1.6473 0.8900 0.8794 -0.1667 -0.2991 0.0645 594 ASN B CA 4356 C C . ASN A 563 ? 1.6524 0.8911 0.8725 -0.1785 -0.2994 0.0692 594 ASN B C 4357 O O . ASN A 563 ? 1.6493 0.9162 0.8914 -0.1715 -0.2923 0.0650 594 ASN B O 4358 C CB . ASN A 563 ? 1.6403 0.8653 0.8432 -0.1785 -0.2815 0.0680 594 ASN B CB 4359 C CG . ASN A 563 ? 1.6357 0.8517 0.8408 -0.1718 -0.2883 0.0662 594 ASN B CG 4360 O OD1 . ASN A 563 ? 1.6451 0.8290 0.8276 -0.1814 -0.3053 0.0720 594 ASN B OD1 4361 N ND2 . ASN A 563 ? 1.6219 0.8658 0.8536 -0.1557 -0.2762 0.0583 594 ASN B ND2 4362 N N . GLN A 564 ? 1.5724 0.7759 0.7567 -0.1974 -0.3080 0.0780 595 GLN B N 4363 C CA . GLN A 564 ? 1.5787 0.7735 0.7473 -0.2107 -0.3104 0.0833 595 GLN B CA 4364 C C . GLN A 564 ? 1.5677 0.7604 0.7126 -0.2251 -0.2840 0.0851 595 GLN B C 4365 O O . GLN A 564 ? 1.5743 0.7567 0.7013 -0.2387 -0.2838 0.0895 595 GLN B O 4366 C CB . GLN A 564 ? 1.5965 0.7538 0.7397 -0.2241 -0.3375 0.0917 595 GLN B CB 4367 C CG . GLN A 564 ? 1.6082 0.7613 0.7727 -0.2109 -0.3664 0.0899 595 GLN B CG 4368 C CD . GLN A 564 ? 1.6199 0.7878 0.8115 -0.2017 -0.3845 0.0870 595 GLN B CD 4369 O OE1 . GLN A 564 ? 1.6176 0.8162 0.8298 -0.1950 -0.3707 0.0819 595 GLN B OE1 4370 N NE2 . GLN A 564 ? 1.6332 0.7787 0.8250 -0.2018 -0.4164 0.0903 595 GLN B NE2 4371 N N . LEU A 565 ? 1.5423 0.7449 0.6885 -0.2218 -0.2625 0.0811 596 LEU B N 4372 C CA . LEU A 565 ? 1.5306 0.7291 0.6554 -0.2352 -0.2383 0.0812 596 LEU B CA 4373 C C . LEU A 565 ? 1.5284 0.7414 0.6580 -0.2382 -0.2279 0.0808 596 LEU B C 4374 O O . LEU A 565 ? 1.5305 0.7679 0.6876 -0.2259 -0.2315 0.0784 596 LEU B O 4375 C CB . LEU A 565 ? 1.5127 0.7272 0.6489 -0.2264 -0.2176 0.0752 596 LEU B CB 4376 C CG . LEU A 565 ? 1.5146 0.7096 0.6330 -0.2315 -0.2168 0.0756 596 LEU B CG 4377 C CD1 . LEU A 565 ? 1.4975 0.7149 0.6361 -0.2184 -0.1984 0.0689 596 LEU B CD1 4378 C CD2 . LEU A 565 ? 1.5158 0.6833 0.5950 -0.2550 -0.2092 0.0788 596 LEU B CD2 4379 N N . ILE A 566 ? 1.5583 0.7556 0.6601 -0.2558 -0.2154 0.0827 597 ILE B N 4380 C CA . ILE A 566 ? 1.5561 0.7625 0.6580 -0.2613 -0.2052 0.0825 597 ILE B CA 4381 C C . ILE A 566 ? 1.5455 0.7469 0.6302 -0.2727 -0.1815 0.0791 597 ILE B C 4382 O O . ILE A 566 ? 1.5471 0.7321 0.6123 -0.2813 -0.1759 0.0779 597 ILE B O 4383 C CB . ILE A 566 ? 1.5729 0.7595 0.6553 -0.2750 -0.2224 0.0890 597 ILE B CB 4384 C CG1 . ILE A 566 ? 1.5830 0.7342 0.6241 -0.2968 -0.2253 0.0931 597 ILE B CG1 4385 C CG2 . ILE A 566 ? 1.5850 0.7765 0.6871 -0.2635 -0.2478 0.0913 597 ILE B CG2 4386 C CD1 . ILE A 566 ? 1.5950 0.7272 0.6095 -0.3160 -0.2309 0.0980 597 ILE B CD1 4387 N N . GLY A 567 ? 1.5501 0.7659 0.6429 -0.2730 -0.1682 0.0768 598 GLY B N 4388 C CA . GLY A 567 ? 1.5410 0.7538 0.6222 -0.2823 -0.1465 0.0718 598 GLY B CA 4389 C C . GLY A 567 ? 1.5239 0.7612 0.6316 -0.2675 -0.1304 0.0662 598 GLY B C 4390 O O . GLY A 567 ? 1.5207 0.7781 0.6540 -0.2511 -0.1353 0.0663 598 GLY B O 4391 N N . PRO A 568 ? 1.4102 0.6464 0.5124 -0.2736 -0.1115 0.0605 599 PRO B N 4392 C CA . PRO A 568 ? 1.3875 0.6443 0.5133 -0.2614 -0.0964 0.0553 599 PRO B CA 4393 C C . PRO A 568 ? 1.3793 0.6389 0.5117 -0.2530 -0.0921 0.0520 599 PRO B C 4394 O O . PRO A 568 ? 1.3914 0.6332 0.5046 -0.2611 -0.0946 0.0516 599 PRO B O 4395 C CB . PRO A 568 ? 1.3880 0.6379 0.5033 -0.2731 -0.0803 0.0496 599 PRO B CB 4396 C CG . PRO A 568 ? 1.4077 0.6387 0.4978 -0.2898 -0.0876 0.0526 599 PRO B CG 4397 C CD . PRO A 568 ? 1.4241 0.6408 0.4992 -0.2931 -0.1041 0.0582 599 PRO B CD 4398 N N . ILE A 569 ? 1.3594 0.6415 0.5182 -0.2379 -0.0856 0.0499 600 ILE B N 4399 C CA . ILE A 569 ? 1.3481 0.6363 0.5168 -0.2285 -0.0797 0.0463 600 ILE B CA 4400 C C . ILE A 569 ? 1.3403 0.6266 0.5078 -0.2329 -0.0610 0.0391 600 ILE B C 4401 O O . ILE A 569 ? 1.3362 0.6274 0.5090 -0.2353 -0.0531 0.0373 600 ILE B O 4402 C CB . ILE A 569 ? 1.3323 0.6468 0.5302 -0.2104 -0.0837 0.0476 600 ILE B CB 4403 C CG1 . ILE A 569 ? 1.3424 0.6573 0.5430 -0.2048 -0.1024 0.0515 600 ILE B CG1 4404 C CG2 . ILE A 569 ? 1.3165 0.6409 0.5277 -0.2009 -0.0731 0.0431 600 ILE B CG2 4405 C CD1 . ILE A 569 ? 1.3341 0.6759 0.5613 -0.1913 -0.1089 0.0524 600 ILE B CD1 4406 N N . PRO A 570 ? 1.3396 0.6179 0.5003 -0.2345 -0.0545 0.0344 601 PRO B N 4407 C CA . PRO A 570 ? 1.3347 0.6106 0.4948 -0.2396 -0.0371 0.0257 601 PRO B CA 4408 C C . PRO A 570 ? 1.3150 0.6103 0.5021 -0.2269 -0.0274 0.0224 601 PRO B C 4409 O O . PRO A 570 ? 1.3022 0.6123 0.5072 -0.2131 -0.0301 0.0246 601 PRO B O 4410 C CB . PRO A 570 ? 1.3386 0.6032 0.4858 -0.2437 -0.0351 0.0223 601 PRO B CB 4411 C CG . PRO A 570 ? 1.3582 0.6102 0.4888 -0.2480 -0.0519 0.0298 601 PRO B CG 4412 C CD . PRO A 570 ? 1.3473 0.6144 0.4964 -0.2352 -0.0639 0.0366 601 PRO B CD 4413 N N . SER A 571 ? 1.9013 1.1959 1.0913 -0.2321 -0.0169 0.0169 602 SER B N 4414 C CA . SER A 571 ? 1.8928 1.2007 1.1059 -0.2224 -0.0078 0.0126 602 SER B CA 4415 C C . SER A 571 ? 1.8858 1.1889 1.0983 -0.2234 0.0027 0.0036 602 SER B C 4416 O O . SER A 571 ? 1.8880 1.1774 1.0841 -0.2364 0.0098 -0.0040 602 SER B O 4417 C CB . SER A 571 ? 1.8967 1.2048 1.1154 -0.2268 -0.0027 0.0100 602 SER B CB 4418 O OG . SER A 571 ? 1.9017 1.1940 1.1033 -0.2416 0.0044 0.0021 602 SER B OG 4419 N N . GLY A 572 ? 1.2798 0.5950 0.5098 -0.2104 0.0039 0.0038 603 GLY B N 4420 C CA . GLY A 572 ? 1.2763 0.5880 0.5049 -0.2102 0.0110 -0.0030 603 GLY B CA 4421 C C . GLY A 572 ? 1.2617 0.5880 0.5088 -0.1947 0.0084 0.0002 603 GLY B C 4422 O O . GLY A 572 ? 1.2516 0.5923 0.5173 -0.1846 0.0063 0.0041 603 GLY B O 4423 N N . SER A 573 ? 1.4885 0.8108 0.7299 -0.1938 0.0091 -0.0019 604 SER B N 4424 C CA . SER A 573 ? 1.4829 0.8179 0.7383 -0.1798 0.0042 0.0020 604 SER B CA 4425 C C . SER A 573 ? 1.4886 0.8327 0.7474 -0.1733 -0.0089 0.0114 604 SER B C 4426 O O . SER A 573 ? 1.4861 0.8470 0.7624 -0.1609 -0.0124 0.0146 604 SER B O 4427 C CB . SER A 573 ? 1.4816 0.8072 0.7248 -0.1824 0.0038 -0.0003 604 SER B CB 4428 O OG . SER A 573 ? 1.4790 0.7965 0.7170 -0.1909 0.0164 -0.0102 604 SER B OG 4429 N N . PHE A 574 ? 1.3936 0.7272 0.6360 -0.1825 -0.0160 0.0150 605 PHE B N 4430 C CA . PHE A 574 ? 1.3992 0.7413 0.6456 -0.1773 -0.0288 0.0224 605 PHE B CA 4431 C C . PHE A 574 ? 1.3956 0.7573 0.6619 -0.1697 -0.0281 0.0252 605 PHE B C 4432 O O . PHE A 574 ? 1.3983 0.7730 0.6729 -0.1635 -0.0375 0.0300 605 PHE B O 4433 C CB . PHE A 574 ? 1.4093 0.7351 0.6342 -0.1900 -0.0364 0.0254 605 PHE B CB 4434 C CG . PHE A 574 ? 1.4169 0.7285 0.6257 -0.1935 -0.0471 0.0277 605 PHE B CG 4435 C CD1 . PHE A 574 ? 1.4148 0.7134 0.6110 -0.1992 -0.0420 0.0236 605 PHE B CD1 4436 C CD2 . PHE A 574 ? 1.4272 0.7383 0.6340 -0.1916 -0.0632 0.0338 605 PHE B CD2 4437 C CE1 . PHE A 574 ? 1.4232 0.7067 0.6030 -0.2037 -0.0533 0.0266 605 PHE B CE1 4438 C CE2 . PHE A 574 ? 1.4359 0.7317 0.6283 -0.1949 -0.0755 0.0363 605 PHE B CE2 4439 C CZ . PHE A 574 ? 1.4339 0.7150 0.6118 -0.2014 -0.0708 0.0333 605 PHE B CZ 4440 N N . ALA A 575 ? 1.2500 0.6141 0.5243 -0.1706 -0.0177 0.0217 606 ALA B N 4441 C CA . ALA A 575 ? 1.2414 0.6221 0.5327 -0.1651 -0.0178 0.0252 606 ALA B CA 4442 C C . ALA A 575 ? 1.2304 0.6307 0.5391 -0.1523 -0.0203 0.0273 606 ALA B C 4443 O O . ALA A 575 ? 1.2259 0.6434 0.5457 -0.1478 -0.0249 0.0318 606 ALA B O 4444 C CB . ALA A 575 ? 1.2382 0.6142 0.5347 -0.1688 -0.0079 0.0207 606 ALA B CB 4445 N N . HIS A 576 ? 1.5802 0.9785 0.8903 -0.1473 -0.0172 0.0236 607 HIS B N 4446 C CA . HIS A 576 ? 1.5768 0.9930 0.9032 -0.1355 -0.0182 0.0244 607 HIS B CA 4447 C C . HIS A 576 ? 1.5826 1.0073 0.9099 -0.1296 -0.0286 0.0266 607 HIS B C 4448 O O . HIS A 576 ? 1.5807 1.0197 0.9200 -0.1199 -0.0301 0.0259 607 HIS B O 4449 C CB . HIS A 576 ? 1.5706 0.9814 0.8999 -0.1324 -0.0101 0.0189 607 HIS B CB 4450 C CG . HIS A 576 ? 1.5658 0.9706 0.8997 -0.1363 -0.0008 0.0151 607 HIS B CG 4451 N ND1 . HIS A 576 ? 1.5640 0.9793 0.9115 -0.1338 0.0000 0.0179 607 HIS B ND1 4452 C CD2 . HIS A 576 ? 1.5636 0.9533 0.8912 -0.1427 0.0075 0.0078 607 HIS B CD2 4453 C CE1 . HIS A 576 ? 1.5623 0.9678 0.9130 -0.1375 0.0071 0.0126 607 HIS B CE1 4454 N NE2 . HIS A 576 ? 1.5616 0.9528 0.9014 -0.1426 0.0125 0.0055 607 HIS B NE2 4455 N N . LEU A 577 ? 1.2599 0.6753 0.5748 -0.1354 -0.0365 0.0286 608 LEU B N 4456 C CA . LEU A 577 ? 1.2676 0.6869 0.5832 -0.1302 -0.0486 0.0295 608 LEU B CA 4457 C C . LEU A 577 ? 1.2686 0.7117 0.6001 -0.1236 -0.0559 0.0315 608 LEU B C 4458 O O . LEU A 577 ? 1.2648 0.7202 0.6033 -0.1254 -0.0524 0.0337 608 LEU B O 4459 C CB . LEU A 577 ? 1.2793 0.6760 0.5740 -0.1401 -0.0561 0.0309 608 LEU B CB 4460 C CG . LEU A 577 ? 1.2785 0.6521 0.5548 -0.1465 -0.0550 0.0287 608 LEU B CG 4461 C CD1 . LEU A 577 ? 1.2865 0.6498 0.5535 -0.1474 -0.0706 0.0312 608 LEU B CD1 4462 C CD2 . LEU A 577 ? 1.2690 0.6471 0.5535 -0.1392 -0.0475 0.0247 608 LEU B CD2 4463 N N . ASN A 578 ? 1.2709 0.7199 0.6077 -0.1170 -0.0671 0.0302 609 ASN B N 4464 C CA . ASN A 578 ? 1.2757 0.7500 0.6302 -0.1101 -0.0742 0.0295 609 ASN B CA 4465 C C . ASN A 578 ? 1.2891 0.7581 0.6379 -0.1153 -0.0851 0.0316 609 ASN B C 4466 O O . ASN A 578 ? 1.2964 0.7474 0.6346 -0.1171 -0.0950 0.0318 609 ASN B O 4467 C CB . ASN A 578 ? 1.2783 0.7653 0.6467 -0.0983 -0.0806 0.0246 609 ASN B CB 4468 C CG . ASN A 578 ? 1.2899 0.7982 0.6746 -0.0924 -0.0920 0.0216 609 ASN B CG 4469 O OD1 . ASN A 578 ? 1.3002 0.7986 0.6820 -0.0921 -0.1051 0.0209 609 ASN B OD1 4470 N ND2 . ASN A 578 ? 1.2895 0.8274 0.6915 -0.0886 -0.0874 0.0194 609 ASN B ND2 4471 N N . PRO A 579 ? 1.2421 0.7268 0.5981 -0.1180 -0.0845 0.0334 610 PRO B N 4472 C CA . PRO A 579 ? 1.2548 0.7348 0.6056 -0.1238 -0.0943 0.0356 610 PRO B CA 4473 C C . PRO A 579 ? 1.2635 0.7435 0.6202 -0.1175 -0.1103 0.0325 610 PRO B C 4474 O O . PRO A 579 ? 1.2790 0.7384 0.6220 -0.1233 -0.1203 0.0349 610 PRO B O 4475 C CB . PRO A 579 ? 1.2477 0.7543 0.6129 -0.1241 -0.0912 0.0362 610 PRO B CB 4476 C CG . PRO A 579 ? 1.2343 0.7486 0.6030 -0.1236 -0.0779 0.0369 610 PRO B CG 4477 C CD . PRO A 579 ? 1.2293 0.7380 0.5990 -0.1162 -0.0755 0.0336 610 PRO B CD 4478 N N . SER A 580 ? 1.5062 1.0077 0.8830 -0.1058 -0.1134 0.0267 611 SER B N 4479 C CA . SER A 580 ? 1.5175 1.0227 0.9054 -0.0984 -0.1301 0.0221 611 SER B CA 4480 C C . SER A 580 ? 1.5184 0.9917 0.8895 -0.1000 -0.1403 0.0239 611 SER B C 4481 O O . SER A 580 ? 1.5268 0.9965 0.9043 -0.0950 -0.1571 0.0212 611 SER B O 4482 C CB . SER A 580 ? 1.5131 1.0514 0.9284 -0.0857 -0.1304 0.0136 611 SER B CB 4483 O OG . SER A 580 ? 1.5157 1.0833 0.9443 -0.0872 -0.1235 0.0122 611 SER B OG 4484 N N . PHE A 581 ? 1.3036 0.7540 0.6535 -0.1076 -0.1307 0.0281 612 PHE B N 4485 C CA . PHE A 581 ? 1.3091 0.7265 0.6367 -0.1140 -0.1385 0.0311 612 PHE B CA 4486 C C . PHE A 581 ? 1.3230 0.7214 0.6353 -0.1241 -0.1508 0.0358 612 PHE B C 4487 O O . PHE A 581 ? 1.3328 0.7113 0.6357 -0.1258 -0.1665 0.0372 612 PHE B O 4488 C CB . PHE A 581 ? 1.3000 0.6996 0.6078 -0.1228 -0.1233 0.0336 612 PHE B CB 4489 C CG . PHE A 581 ? 1.2908 0.6960 0.6059 -0.1148 -0.1159 0.0299 612 PHE B CG 4490 C CD1 . PHE A 581 ? 1.2951 0.7059 0.6228 -0.1038 -0.1267 0.0261 612 PHE B CD1 4491 C CD2 . PHE A 581 ? 1.2779 0.6828 0.5887 -0.1178 -0.0988 0.0296 612 PHE B CD2 4492 C CE1 . PHE A 581 ? 1.2862 0.7023 0.6206 -0.0965 -0.1200 0.0227 612 PHE B CE1 4493 C CE2 . PHE A 581 ? 1.2692 0.6793 0.5872 -0.1105 -0.0924 0.0262 612 PHE B CE2 4494 C CZ . PHE A 581 ? 1.2732 0.6889 0.6022 -0.1001 -0.1027 0.0231 612 PHE B CZ 4495 N N . PHE A 582 ? 1.3794 0.7820 0.6876 -0.1317 -0.1441 0.0386 613 PHE B N 4496 C CA . PHE A 582 ? 1.3901 0.7736 0.6809 -0.1432 -0.1535 0.0435 613 PHE B CA 4497 C C . PHE A 582 ? 1.4024 0.8020 0.7104 -0.1385 -0.1675 0.0424 613 PHE B C 4498 O O . PHE A 582 ? 1.4116 0.7977 0.7073 -0.1476 -0.1760 0.0465 613 PHE B O 4499 C CB . PHE A 582 ? 1.3832 0.7586 0.6575 -0.1557 -0.1385 0.0469 613 PHE B CB 4500 C CG . PHE A 582 ? 1.3707 0.7365 0.6341 -0.1592 -0.1226 0.0457 613 PHE B CG 4501 C CD1 . PHE A 582 ? 1.3704 0.7078 0.6086 -0.1698 -0.1229 0.0472 613 PHE B CD1 4502 C CD2 . PHE A 582 ? 1.3584 0.7435 0.6363 -0.1531 -0.1077 0.0430 613 PHE B CD2 4503 C CE1 . PHE A 582 ? 1.3582 0.6888 0.5882 -0.1734 -0.1077 0.0446 613 PHE B CE1 4504 C CE2 . PHE A 582 ? 1.3477 0.7243 0.6178 -0.1559 -0.0940 0.0412 613 PHE B CE2 4505 C CZ . PHE A 582 ? 1.3469 0.6972 0.5941 -0.1657 -0.0935 0.0413 613 PHE B CZ 4506 N N . SER A 583 ? 1.4316 0.8612 0.7684 -0.1248 -0.1695 0.0360 614 SER B N 4507 C CA . SER A 583 ? 1.4427 0.8929 0.7998 -0.1199 -0.1811 0.0326 614 SER B CA 4508 C C . SER A 583 ? 1.4560 0.8884 0.8113 -0.1191 -0.2047 0.0328 614 SER B C 4509 O O . SER A 583 ? 1.4579 0.8647 0.7989 -0.1206 -0.2128 0.0350 614 SER B O 4510 C CB . SER A 583 ? 1.4394 0.9283 0.8281 -0.1067 -0.1765 0.0240 614 SER B CB 4511 O OG . SER A 583 ? 1.4308 0.9205 0.8248 -0.0980 -0.1739 0.0201 614 SER B OG 4512 N N . SER A 584 ? 1.5449 0.9893 0.9135 -0.1182 -0.2162 0.0309 615 SER B N 4513 C CA . SER A 584 ? 1.5567 0.9848 0.9262 -0.1174 -0.2409 0.0310 615 SER B CA 4514 C C . SER A 584 ? 1.5610 0.9466 0.8936 -0.1326 -0.2468 0.0412 615 SER B C 4515 O O . SER A 584 ? 1.5698 0.9320 0.8950 -0.1340 -0.2678 0.0434 615 SER B O 4516 C CB . SER A 584 ? 1.5585 0.9928 0.9493 -0.1028 -0.2546 0.0230 615 SER B CB 4517 O OG . SER A 584 ? 1.5494 1.0249 0.9752 -0.0895 -0.2499 0.0118 615 SER B OG 4518 N N . ASN A 585 ? 1.6372 1.0130 0.9468 -0.1447 -0.2286 0.0470 616 ASN B N 4519 C CA . ASN A 585 ? 1.6426 0.9845 0.9180 -0.1621 -0.2315 0.0555 616 ASN B CA 4520 C C . ASN A 585 ? 1.6456 0.9976 0.9200 -0.1692 -0.2240 0.0576 616 ASN B C 4521 O O . ASN A 585 ? 1.6376 1.0040 0.9138 -0.1706 -0.2045 0.0570 616 ASN B O 4522 C CB . ASN A 585 ? 1.6326 0.9533 0.8819 -0.1712 -0.2172 0.0586 616 ASN B CB 4523 C CG . ASN A 585 ? 1.6365 0.9363 0.8772 -0.1696 -0.2296 0.0592 616 ASN B CG 4524 O OD1 . ASN A 585 ? 1.6471 0.9523 0.9066 -0.1583 -0.2474 0.0559 616 ASN B OD1 4525 N ND2 . ASN A 585 ? 1.6281 0.9044 0.8412 -0.1812 -0.2209 0.0625 616 ASN B ND2 4526 N N . GLU A 586 ? 1.7165 1.0604 0.9891 -0.1735 -0.2416 0.0602 617 GLU B N 4527 C CA . GLU A 586 ? 1.7192 1.0790 1.0000 -0.1765 -0.2400 0.0606 617 GLU B CA 4528 C C . GLU A 586 ? 1.7136 1.0515 0.9631 -0.1941 -0.2297 0.0676 617 GLU B C 4529 O O . GLU A 586 ? 1.7113 1.0601 0.9630 -0.1987 -0.2235 0.0686 617 GLU B O 4530 C CB . GLU A 586 ? 1.7385 1.0984 1.0323 -0.1729 -0.2650 0.0595 617 GLU B CB 4531 C CG . GLU A 586 ? 1.7557 1.0888 1.0418 -0.1715 -0.2872 0.0611 617 GLU B CG 4532 C CD . GLU A 586 ? 1.7576 1.1091 1.0732 -0.1532 -0.2935 0.0522 617 GLU B CD 4533 O OE1 . GLU A 586 ? 1.7475 1.1353 1.0913 -0.1414 -0.2818 0.0440 617 GLU B OE1 4534 O OE2 . GLU A 586 ? 1.7697 1.0989 1.0795 -0.1514 -0.3109 0.0533 617 GLU B OE2 4535 N N . GLY A 587 ? 1.5950 0.9027 0.8155 -0.2045 -0.2277 0.0716 618 GLY B N 4536 C CA . GLY A 587 ? 1.5913 0.8760 0.7803 -0.2228 -0.2194 0.0768 618 GLY B CA 4537 C C . GLY A 587 ? 1.5750 0.8595 0.7538 -0.2275 -0.1950 0.0749 618 GLY B C 4538 O O . GLY A 587 ? 1.5726 0.8393 0.7266 -0.2426 -0.1865 0.0771 618 GLY B O 4539 N N . LEU A 588 ? 1.4068 0.7112 0.6053 -0.2148 -0.1842 0.0701 619 LEU B N 4540 C CA . LEU A 588 ? 1.3939 0.6980 0.5855 -0.2179 -0.1628 0.0677 619 LEU B CA 4541 C C . LEU A 588 ? 1.3818 0.7042 0.5839 -0.2181 -0.1500 0.0669 619 LEU B C 4542 O O . LEU A 588 ? 1.3778 0.7226 0.6009 -0.2105 -0.1551 0.0667 619 LEU B O 4543 C CB . LEU A 588 ? 1.3812 0.6977 0.5887 -0.2048 -0.1573 0.0634 619 LEU B CB 4544 C CG . LEU A 588 ? 1.3860 0.6805 0.5749 -0.2093 -0.1558 0.0629 619 LEU B CG 4545 C CD1 . LEU A 588 ? 1.4076 0.6695 0.5626 -0.2279 -0.1621 0.0672 619 LEU B CD1 4546 C CD2 . LEU A 588 ? 1.3875 0.6875 0.5915 -0.1962 -0.1688 0.0614 619 LEU B CD2 4547 N N . CYS A 589 ? 1.3899 0.7026 0.5778 -0.2276 -0.1342 0.0659 620 CYS B N 4548 C CA . CYS A 589 ? 1.3796 0.7073 0.5776 -0.2276 -0.1213 0.0649 620 CYS B CA 4549 C C . CYS A 589 ? 1.3645 0.6949 0.5661 -0.2247 -0.1039 0.0604 620 CYS B C 4550 O O . CYS A 589 ? 1.3615 0.6783 0.5522 -0.2266 -0.1003 0.0579 620 CYS B O 4551 C CB . CYS A 589 ? 1.3869 0.6992 0.5658 -0.2426 -0.1208 0.0673 620 CYS B CB 4552 S SG . CYS A 589 ? 1.3835 0.6715 0.5367 -0.2577 -0.1050 0.0632 620 CYS B SG 4553 N N . GLY A 590 ? 1.6548 1.0028 0.8723 -0.2203 -0.0942 0.0595 621 GLY B N 4554 C CA . GLY A 590 ? 1.6432 0.9926 0.8653 -0.2178 -0.0793 0.0553 621 GLY B CA 4555 C C . GLY A 590 ? 1.6380 1.0138 0.8848 -0.2068 -0.0758 0.0558 621 GLY B C 4556 O O . GLY A 590 ? 1.6456 1.0385 0.9039 -0.2037 -0.0829 0.0589 621 GLY B O 4557 N N . ASP A 591 ? 1.3627 0.7428 0.6178 -0.2018 -0.0651 0.0526 622 ASP B N 4558 C CA . ASP A 591 ? 1.3573 0.7620 0.6340 -0.1923 -0.0628 0.0537 622 ASP B CA 4559 C C . ASP A 591 ? 1.3610 0.7831 0.6506 -0.1812 -0.0703 0.0535 622 ASP B C 4560 O O . ASP A 591 ? 1.3672 0.8104 0.6702 -0.1772 -0.0759 0.0552 622 ASP B O 4561 C CB . ASP A 591 ? 1.3457 0.7490 0.6281 -0.1900 -0.0509 0.0506 622 ASP B CB 4562 C CG . ASP A 591 ? 1.3433 0.7357 0.6206 -0.1988 -0.0444 0.0501 622 ASP B CG 4563 O OD1 . ASP A 591 ? 1.3482 0.7289 0.6124 -0.2082 -0.0475 0.0511 622 ASP B OD1 4564 O OD2 . ASP A 591 ? 1.3376 0.7325 0.6246 -0.1963 -0.0372 0.0484 622 ASP B OD2 4565 N N . LEU A 592 ? 1.3579 0.7715 0.6437 -0.1769 -0.0707 0.0505 623 LEU B N 4566 C CA . LEU A 592 ? 1.3605 0.7909 0.6610 -0.1650 -0.0766 0.0488 623 LEU B CA 4567 C C . LEU A 592 ? 1.3751 0.8145 0.6813 -0.1621 -0.0912 0.0495 623 LEU B C 4568 O O . LEU A 592 ? 1.3800 0.8385 0.7031 -0.1517 -0.0965 0.0467 623 LEU B O 4569 C CB . LEU A 592 ? 1.3556 0.7728 0.6498 -0.1616 -0.0744 0.0455 623 LEU B CB 4570 C CG . LEU A 592 ? 1.3431 0.7561 0.6375 -0.1614 -0.0606 0.0430 623 LEU B CG 4571 C CD1 . LEU A 592 ? 1.3417 0.7284 0.6153 -0.1733 -0.0543 0.0412 623 LEU B CD1 4572 C CD2 . LEU A 592 ? 1.3384 0.7584 0.6420 -0.1511 -0.0598 0.0399 623 LEU B CD2 4573 N N . VAL A 593 ? 1.3743 0.7999 0.6673 -0.1711 -0.0983 0.0523 624 VAL B N 4574 C CA . VAL A 593 ? 1.3882 0.8235 0.6891 -0.1686 -0.1131 0.0527 624 VAL B CA 4575 C C . VAL A 593 ? 1.3899 0.8455 0.7019 -0.1709 -0.1128 0.0544 624 VAL B C 4576 O O . VAL A 593 ? 1.4014 0.8727 0.7259 -0.1675 -0.1235 0.0532 624 VAL B O 4577 C CB . VAL A 593 ? 1.3999 0.8082 0.6804 -0.1768 -0.1244 0.0552 624 VAL B CB 4578 C CG1 . VAL A 593 ? 1.4027 0.8024 0.6709 -0.1889 -0.1246 0.0591 624 VAL B CG1 4579 C CG2 . VAL A 593 ? 1.4123 0.8265 0.7041 -0.1686 -0.1422 0.0533 624 VAL B CG2 4580 N N . GLY A 594 ? 1.2950 0.7505 0.6032 -0.1769 -0.1009 0.0567 625 GLY B N 4581 C CA . GLY A 594 ? 1.2908 0.7665 0.6096 -0.1795 -0.0990 0.0588 625 GLY B CA 4582 C C . GLY A 594 ? 1.3016 0.7642 0.6071 -0.1909 -0.1022 0.0627 625 GLY B C 4583 O O . GLY A 594 ? 1.2987 0.7695 0.6066 -0.1963 -0.0978 0.0654 625 GLY B O 4584 N N . LYS A 595 ? 1.5544 0.9953 0.8445 -0.1955 -0.1104 0.0633 626 LYS B N 4585 C CA . LYS A 595 ? 1.5602 0.9870 0.8359 -0.2068 -0.1151 0.0668 626 LYS B CA 4586 C C . LYS A 595 ? 1.5500 0.9490 0.8034 -0.2169 -0.1058 0.0673 626 LYS B C 4587 O O . LYS A 595 ? 1.5453 0.9277 0.7876 -0.2171 -0.1038 0.0651 626 LYS B O 4588 C CB . LYS A 595 ? 1.5765 0.9961 0.8486 -0.2066 -0.1317 0.0671 626 LYS B CB 4589 C CG . LYS A 595 ? 1.5849 1.0262 0.8795 -0.1930 -0.1413 0.0629 626 LYS B CG 4590 C CD . LYS A 595 ? 1.5976 1.0212 0.8849 -0.1916 -0.1577 0.0625 626 LYS B CD 4591 C CE . LYS A 595 ? 1.6037 1.0484 0.9159 -0.1770 -0.1675 0.0567 626 LYS B CE 4592 N NZ . LYS A 595 ? 1.6123 1.0364 0.9174 -0.1747 -0.1838 0.0564 626 LYS B NZ 4593 N N . PRO A 596 ? 1.4284 0.8231 0.6759 -0.2256 -0.0997 0.0692 627 PRO B N 4594 C CA . PRO A 596 ? 1.4219 0.7928 0.6512 -0.2351 -0.0901 0.0673 627 PRO B CA 4595 C C . PRO A 596 ? 1.4312 0.7774 0.6364 -0.2468 -0.0960 0.0679 627 PRO B C 4596 O O . PRO A 596 ? 1.4428 0.7889 0.6449 -0.2493 -0.1085 0.0713 627 PRO B O 4597 C CB . PRO A 596 ? 1.4195 0.7965 0.6540 -0.2398 -0.0840 0.0690 627 PRO B CB 4598 C CG . PRO A 596 ? 1.4134 0.8188 0.6689 -0.2319 -0.0877 0.0718 627 PRO B CG 4599 C CD . PRO A 596 ? 1.4293 0.8434 0.6893 -0.2266 -0.0999 0.0720 627 PRO B CD 4600 N N . CYS A 597 ? 1.6424 0.9680 0.8309 -0.2545 -0.0871 0.0638 628 CYS B N 4601 C CA . CYS A 597 ? 1.6523 0.9535 0.8146 -0.2689 -0.0898 0.0635 628 CYS B CA 4602 C C . CYS A 597 ? 1.6521 0.9494 0.8106 -0.2778 -0.0831 0.0625 628 CYS B C 4603 O O . CYS A 597 ? 1.6450 0.9579 0.8212 -0.2720 -0.0786 0.0631 628 CYS B O 4604 C CB . CYS A 597 ? 1.6500 0.9344 0.7977 -0.2733 -0.0819 0.0579 628 CYS B CB 4605 S SG . CYS A 597 ? 1.6438 0.9405 0.8075 -0.2577 -0.0820 0.0568 628 CYS B SG 4606 N N . ASN A 598 ? 1.3906 0.6673 0.5258 -0.2925 -0.0830 0.0611 629 ASN B N 4607 C CA . ASN A 598 ? 1.3936 0.6650 0.5246 -0.3016 -0.0765 0.0588 629 ASN B CA 4608 C C . ASN A 598 ? 1.3890 0.6752 0.5331 -0.2989 -0.0836 0.0652 629 ASN B C 4609 O O . ASN A 598 ? 1.3768 0.6800 0.5411 -0.2905 -0.0798 0.0660 629 ASN B O 4610 C CB . ASN A 598 ? 1.3841 0.6559 0.5240 -0.2996 -0.0610 0.0507 629 ASN B CB 4611 C CG . ASN A 598 ? 1.3905 0.6477 0.5166 -0.3052 -0.0520 0.0423 629 ASN B CG 4612 O OD1 . ASN A 598 ? 1.4067 0.6481 0.5096 -0.3161 -0.0556 0.0421 629 ASN B OD1 4613 N ND2 . ASN A 598 ? 1.3790 0.6411 0.5188 -0.2986 -0.0405 0.0353 629 ASN B ND2 4614 N N . HIS B 1 ? 1.2534 0.7364 0.7758 0.0495 0.0196 -0.0915 93 HIS C N 4615 C CA . HIS B 1 ? 1.2617 0.7425 0.7751 0.0545 0.0101 -0.0885 93 HIS C CA 4616 C C . HIS B 1 ? 1.2747 0.7368 0.7717 0.0493 0.0035 -0.0891 93 HIS C C 4617 O O . HIS B 1 ? 1.2745 0.7319 0.7704 0.0497 0.0011 -0.0915 93 HIS C O 4618 C CB . HIS B 1 ? 1.2539 0.7510 0.7782 0.0665 0.0049 -0.0885 93 HIS C CB 4619 C CG . HIS B 1 ? 1.2620 0.7624 0.7823 0.0729 -0.0040 -0.0876 93 HIS C CG 4620 N ND1 . HIS B 1 ? 1.2588 0.7722 0.7861 0.0826 -0.0100 -0.0900 93 HIS C ND1 4621 C CD2 . HIS B 1 ? 1.2738 0.7672 0.7852 0.0708 -0.0081 -0.0857 93 HIS C CD2 4622 C CE1 . HIS B 1 ? 1.2678 0.7832 0.7924 0.0866 -0.0171 -0.0905 93 HIS C CE1 4623 N NE2 . HIS B 1 ? 1.2772 0.7800 0.7922 0.0799 -0.0167 -0.0875 93 HIS C NE2 4624 N N . GLU B 2 ? 1.2940 0.7440 0.7775 0.0437 -0.0002 -0.0865 94 GLU C N 4625 C CA . GLU B 2 ? 1.3098 0.7402 0.7766 0.0391 -0.0099 -0.0857 94 GLU C CA 4626 C C . GLU B 2 ? 1.3162 0.7474 0.7824 0.0479 -0.0220 -0.0841 94 GLU C C 4627 O O . GLU B 2 ? 1.3136 0.7560 0.7857 0.0520 -0.0209 -0.0826 94 GLU C O 4628 C CB . GLU B 2 ? 1.3242 0.7362 0.7730 0.0229 -0.0063 -0.0844 94 GLU C CB 4629 C CG . GLU B 2 ? 1.3287 0.7308 0.7700 0.0112 -0.0003 -0.0875 94 GLU C CG 4630 C CD . GLU B 2 ? 1.3508 0.7288 0.7668 -0.0054 -0.0042 -0.0853 94 GLU C CD 4631 O OE1 . GLU B 2 ? 1.3640 0.7273 0.7685 -0.0090 -0.0131 -0.0844 94 GLU C OE1 4632 O OE2 . GLU B 2 ? 1.3561 0.7291 0.7627 -0.0157 0.0011 -0.0843 94 GLU C OE2 4633 N N . VAL B 3 ? 1.1531 0.5722 0.6126 0.0502 -0.0342 -0.0849 95 VAL C N 4634 C CA . VAL B 3 ? 1.1574 0.5793 0.6213 0.0609 -0.0474 -0.0861 95 VAL C CA 4635 C C . VAL B 3 ? 1.1785 0.5753 0.6251 0.0542 -0.0604 -0.0833 95 VAL C C 4636 O O . VAL B 3 ? 1.1898 0.5661 0.6213 0.0438 -0.0632 -0.0816 95 VAL C O 4637 C CB . VAL B 3 ? 1.1512 0.5794 0.6248 0.0711 -0.0536 -0.0910 95 VAL C CB 4638 C CG1 . VAL B 3 ? 1.1543 0.5883 0.6360 0.0832 -0.0672 -0.0951 95 VAL C CG1 4639 C CG2 . VAL B 3 ? 1.1335 0.5830 0.6216 0.0759 -0.0422 -0.0932 95 VAL C CG2 4640 N N . PRO B 4 ? 1.0687 0.4668 0.5172 0.0594 -0.0693 -0.0829 96 PRO C N 4641 C CA . PRO B 4 ? 1.0920 0.4660 0.5260 0.0545 -0.0849 -0.0801 96 PRO C CA 4642 C C . PRO B 4 ? 1.1036 0.4628 0.5351 0.0577 -0.0993 -0.0825 96 PRO C C 4643 O O . PRO B 4 ? 1.0900 0.4650 0.5376 0.0698 -0.0998 -0.0885 96 PRO C O 4644 C CB . PRO B 4 ? 1.0879 0.4756 0.5350 0.0660 -0.0922 -0.0828 96 PRO C CB 4645 C CG . PRO B 4 ? 1.0673 0.4809 0.5272 0.0700 -0.0776 -0.0837 96 PRO C CG 4646 C CD . PRO B 4 ? 1.0533 0.4761 0.5178 0.0694 -0.0653 -0.0849 96 PRO C CD 4647 N N . SER B 5 ? 1.2574 0.5871 0.6690 0.0469 -0.1115 -0.0781 97 SER C N 4648 C CA . SER B 5 ? 1.2654 0.5795 0.6764 0.0518 -0.1298 -0.0804 97 SER C CA 4649 C C . SER B 5 ? 1.2910 0.5757 0.6865 0.0457 -0.1504 -0.0761 97 SER C C 4650 O O . SER B 5 ? 1.3152 0.5792 0.6878 0.0288 -0.1505 -0.0687 97 SER C O 4651 C CB . SER B 5 ? 1.2644 0.5697 0.6677 0.0451 -0.1259 -0.0803 97 SER C CB 4652 O OG . SER B 5 ? 1.2932 0.5714 0.6698 0.0252 -0.1271 -0.0733 97 SER C OG 4653 N N . GLY B 6 ? 1.2731 0.5556 0.6812 0.0587 -0.1688 -0.0811 98 GLY C N 4654 C CA . GLY B 6 ? 1.2972 0.5473 0.6905 0.0525 -0.1918 -0.0768 98 GLY C CA 4655 C C . GLY B 6 ? 1.2980 0.5563 0.7102 0.0673 -0.2060 -0.0827 98 GLY C C 4656 O O . GLY B 6 ? 1.2805 0.5688 0.7183 0.0835 -0.2004 -0.0920 98 GLY C O 4657 N N . HYP B 7 ? 1.4384 0.6691 0.8379 0.0611 -0.2260 -0.0777 99 HYP C N 4658 C CA . HYP B 7 ? 1.4385 0.6750 0.8547 0.0730 -0.2402 -0.0826 99 HYP C CA 4659 C C . HYP B 7 ? 1.4171 0.6773 0.8386 0.0731 -0.2233 -0.0819 99 HYP C C 4660 O O . HYP B 7 ? 1.4096 0.6728 0.8156 0.0602 -0.2034 -0.0751 99 HYP C O 4661 C CB . HYP B 7 ? 1.4752 0.6744 0.8752 0.0650 -0.2664 -0.0765 99 HYP C CB 4662 C CG . HYP B 7 ? 1.4947 0.6686 0.8605 0.0420 -0.2600 -0.0644 99 HYP C CG 4663 C CD . HYP B 7 ? 1.4686 0.6659 0.8364 0.0403 -0.2327 -0.0661 99 HYP C CD 4664 O OD1 . HYP B 7 ? 1.5273 0.6674 0.8790 0.0357 -0.2823 -0.0608 99 HYP C OD1 4665 N N . ASN B 8 ? 1.2548 0.5336 0.6990 0.0872 -0.2297 -0.0896 100 ASN C N 4666 C CA . ASN B 8 ? 1.2499 0.5492 0.6986 0.0868 -0.2163 -0.0885 100 ASN C CA 4667 C C . ASN B 8 ? 1.2687 0.5413 0.6933 0.0714 -0.2232 -0.0777 100 ASN C C 4668 O O . ASN B 8 ? 1.2840 0.5330 0.7047 0.0710 -0.2465 -0.0763 100 ASN C O 4669 C CB . ASN B 8 ? 1.2420 0.5677 0.7208 0.1046 -0.2228 -0.1003 100 ASN C CB 4670 C CG . ASN B 8 ? 1.2368 0.5868 0.7207 0.1039 -0.2071 -0.0992 100 ASN C CG 4671 O OD1 . ASN B 8 ? 1.2409 0.5829 0.7053 0.0904 -0.1954 -0.0893 100 ASN C OD1 4672 N ND2 . ASN B 8 ? 1.2280 0.6082 0.7386 0.1181 -0.2069 -0.1104 100 ASN C ND2 4673 N N . PRO B 9 ? 1.3102 0.5855 0.7185 0.0582 -0.2037 -0.0702 101 PRO C N 4674 C CA . PRO B 9 ? 1.3271 0.5797 0.7099 0.0408 -0.2054 -0.0598 101 PRO C CA 4675 C C . PRO B 9 ? 1.3311 0.5884 0.7196 0.0436 -0.2116 -0.0594 101 PRO C C 4676 O O . PRO B 9 ? 1.3489 0.5785 0.7172 0.0315 -0.2248 -0.0518 101 PRO C O 4677 C CB . PRO B 9 ? 1.3206 0.5829 0.6917 0.0292 -0.1793 -0.0559 101 PRO C CB 4678 C CG . PRO B 9 ? 1.2973 0.5939 0.6934 0.0439 -0.1644 -0.0640 101 PRO C CG 4679 C CD . PRO B 9 ? 1.2941 0.5911 0.7055 0.0574 -0.1792 -0.0712 101 PRO C CD 4680 N N . ILE B 10 ? 1.2728 0.5632 0.6871 0.0581 -0.2036 -0.0672 102 ILE C N 4681 C CA . ILE B 10 ? 1.2760 0.5749 0.6932 0.0576 -0.2024 -0.0657 102 ILE C CA 4682 C C . ILE B 10 ? 1.2962 0.5678 0.7053 0.0543 -0.2274 -0.0624 102 ILE C C 4683 O O . ILE B 10 ? 1.3035 0.5592 0.7183 0.0608 -0.2494 -0.0659 102 ILE C O 4684 C CB . ILE B 10 ? 1.2611 0.5995 0.7084 0.0738 -0.1936 -0.0756 102 ILE C CB 4685 C CG1 . ILE B 10 ? 1.2644 0.6090 0.7345 0.0883 -0.2143 -0.0851 102 ILE C CG1 4686 C CG2 . ILE B 10 ? 1.2435 0.6071 0.7032 0.0806 -0.1762 -0.0811 102 ILE C CG2 4687 C CD1 . ILE B 10 ? 1.2527 0.6368 0.7491 0.1004 -0.2044 -0.0945 102 ILE C CD1 4688 N N . SER B 11 ? 1.3061 0.5697 0.7002 0.0431 -0.2247 -0.0550 103 SER C N 4689 C CA . SER B 11 ? 1.3273 0.5595 0.7058 0.0347 -0.2473 -0.0487 103 SER C CA 4690 C C . SER B 11 ? 1.3334 0.5721 0.7140 0.0335 -0.2479 -0.0468 103 SER C C 4691 O O . SER B 11 ? 1.3209 0.5887 0.7138 0.0381 -0.2296 -0.0499 103 SER C O 4692 C CB . SER B 11 ? 1.3401 0.5389 0.6820 0.0125 -0.2468 -0.0374 103 SER C CB 4693 O OG . SER B 11 ? 1.3256 0.5391 0.6604 0.0054 -0.2197 -0.0363 103 SER C OG 4694 N N . ASN B 12 ? 1.4456 0.6550 0.8130 0.0265 -0.2706 -0.0412 104 ASN C N 4695 C CA . ASN B 12 ? 1.4546 0.6635 0.8195 0.0227 -0.2746 -0.0378 104 ASN C CA 4696 C C . ASN B 12 ? 1.4710 0.6458 0.7968 -0.0016 -0.2767 -0.0242 104 ASN C C 4697 O O . ASN B 12 ? 1.4742 0.6319 0.7760 -0.0159 -0.2700 -0.0185 104 ASN C O 4698 C CB . ASN B 12 ? 1.4633 0.6705 0.8511 0.0369 -0.3014 -0.0446 104 ASN C CB 4699 C CG . ASN B 12 ? 1.4434 0.6924 0.8708 0.0589 -0.2945 -0.0593 104 ASN C CG 4700 O OD1 . ASN B 12 ? 1.4272 0.7065 0.8623 0.0613 -0.2698 -0.0620 104 ASN C OD1 4701 N ND2 . ASN B 12 ? 1.4448 0.6956 0.8975 0.0741 -0.3167 -0.0695 104 ASN C ND2 4702 O OXT . ASN B 12 ? 1.4813 0.6464 0.7985 -0.0083 -0.2845 -0.0194 104 ASN C OXT 4703 N N . ASN C 1 ? 1.1514 0.6281 0.6234 0.0577 -0.0962 -0.0624 27 ASN K N 4704 C CA . ASN C 1 ? 1.1484 0.6063 0.6078 0.0528 -0.0930 -0.0596 27 ASN K CA 4705 C C . ASN C 1 ? 1.1306 0.6046 0.5957 0.0538 -0.0767 -0.0602 27 ASN K C 4706 O O . ASN C 1 ? 1.1248 0.5889 0.5842 0.0519 -0.0734 -0.0598 27 ASN K O 4707 C CB . ASN C 1 ? 1.1569 0.6031 0.6191 0.0594 -0.1086 -0.0643 27 ASN K CB 4708 N N . MET C 2 ? 1.5975 1.0965 1.0743 0.0567 -0.0677 -0.0612 28 MET K N 4709 C CA . MET C 2 ? 1.5843 1.0942 1.0632 0.0545 -0.0528 -0.0592 28 MET K CA 4710 C C . MET C 2 ? 1.5860 1.0802 1.0502 0.0425 -0.0450 -0.0522 28 MET K C 4711 O O . MET C 2 ? 1.5788 1.0625 1.0356 0.0364 -0.0365 -0.0501 28 MET K O 4712 C CB . MET C 2 ? 1.5811 1.1220 1.0760 0.0601 -0.0479 -0.0621 28 MET K CB 4713 C CG . MET C 2 ? 1.5694 1.1233 1.0691 0.0597 -0.0360 -0.0608 28 MET K CG 4714 S SD . MET C 2 ? 1.5694 1.1225 1.0633 0.0498 -0.0243 -0.0529 28 MET K SD 4715 C CE . MET C 2 ? 1.5783 1.1544 1.0805 0.0512 -0.0269 -0.0537 28 MET K CE 4716 N N . GLU C 3 ? 1.4254 0.9185 0.8862 0.0391 -0.0483 -0.0498 29 GLU K N 4717 C CA . GLU C 3 ? 1.4277 0.9071 0.8751 0.0277 -0.0420 -0.0441 29 GLU K CA 4718 C C . GLU C 3 ? 1.4315 0.8825 0.8604 0.0189 -0.0455 -0.0422 29 GLU K C 4719 O O . GLU C 3 ? 1.4308 0.8686 0.8469 0.0079 -0.0380 -0.0391 29 GLU K O 4720 C CB . GLU C 3 ? 1.4368 0.9212 0.8849 0.0267 -0.0472 -0.0425 29 GLU K CB 4721 C CG . GLU C 3 ? 1.4619 0.9442 0.9135 0.0330 -0.0632 -0.0459 29 GLU K CG 4722 C CD . GLU C 3 ? 1.4696 0.9581 0.9236 0.0322 -0.0685 -0.0449 29 GLU K CD 4723 O OE1 . GLU C 3 ? 1.4794 0.9584 0.9324 0.0343 -0.0830 -0.0465 29 GLU K OE1 4724 O OE2 . GLU C 3 ? 1.4660 0.9681 0.9232 0.0293 -0.0593 -0.0426 29 GLU K OE2 4725 N N . GLY C 4 ? 1.1255 0.5671 0.5528 0.0231 -0.0574 -0.0445 30 GLY K N 4726 C CA . GLY C 4 ? 1.1346 0.5487 0.5428 0.0136 -0.0617 -0.0422 30 GLY K CA 4727 C C . GLY C 4 ? 1.1230 0.5362 0.5293 0.0096 -0.0488 -0.0432 30 GLY K C 4728 O O . GLY C 4 ? 1.1264 0.5243 0.5176 -0.0029 -0.0419 -0.0412 30 GLY K O 4729 N N . ASP C 5 ? 1.2593 0.6904 0.6818 0.0201 -0.0454 -0.0470 31 ASP K N 4730 C CA . ASP C 5 ? 1.2471 0.6789 0.6707 0.0179 -0.0345 -0.0485 31 ASP K CA 4731 C C . ASP C 5 ? 1.2396 0.6752 0.6628 0.0105 -0.0205 -0.0470 31 ASP K C 4732 O O . ASP C 5 ? 1.2343 0.6603 0.6505 0.0022 -0.0120 -0.0480 31 ASP K O 4733 C CB . ASP C 5 ? 1.2374 0.6893 0.6791 0.0306 -0.0342 -0.0526 31 ASP K CB 4734 C CG . ASP C 5 ? 1.2422 0.6929 0.6878 0.0394 -0.0488 -0.0560 31 ASP K CG 4735 O OD1 . ASP C 5 ? 1.2509 0.6792 0.6830 0.0344 -0.0585 -0.0548 31 ASP K OD1 4736 O OD2 . ASP C 5 ? 1.2386 0.7107 0.7006 0.0505 -0.0513 -0.0601 31 ASP K OD2 4737 N N . ALA C 6 ? 1.1234 0.5729 0.5544 0.0133 -0.0185 -0.0453 32 ALA K N 4738 C CA . ALA C 6 ? 1.1177 0.5706 0.5500 0.0070 -0.0070 -0.0439 32 ALA K CA 4739 C C . ALA C 6 ? 1.1258 0.5581 0.5400 -0.0069 -0.0041 -0.0427 32 ALA K C 4740 O O . ALA C 6 ? 1.1194 0.5468 0.5313 -0.0146 0.0064 -0.0449 32 ALA K O 4741 C CB . ALA C 6 ? 1.1193 0.5900 0.5619 0.0120 -0.0075 -0.0417 32 ALA K CB 4742 N N . LEU C 7 ? 1.2367 0.6574 0.6386 -0.0105 -0.0139 -0.0399 33 LEU K N 4743 C CA . LEU C 7 ? 1.2460 0.6467 0.6282 -0.0251 -0.0125 -0.0383 33 LEU K CA 4744 C C . LEU C 7 ? 1.2445 0.6303 0.6149 -0.0339 -0.0086 -0.0410 33 LEU K C 4745 O O . LEU C 7 ? 1.2453 0.6212 0.6042 -0.0470 0.0002 -0.0428 33 LEU K O 4746 C CB . LEU C 7 ? 1.2632 0.6524 0.6339 -0.0269 -0.0266 -0.0344 33 LEU K CB 4747 C CG . LEU C 7 ? 1.2668 0.6667 0.6435 -0.0246 -0.0274 -0.0319 33 LEU K CG 4748 C CD1 . LEU C 7 ? 1.2841 0.6735 0.6524 -0.0249 -0.0430 -0.0288 33 LEU K CD1 4749 C CD2 . LEU C 7 ? 1.2631 0.6591 0.6329 -0.0358 -0.0152 -0.0316 33 LEU K CD2 4750 N N . HIS C 8 ? 1.2337 0.6192 0.6075 -0.0272 -0.0147 -0.0422 34 HIS K N 4751 C CA . HIS C 8 ? 1.2336 0.6060 0.5966 -0.0357 -0.0114 -0.0446 34 HIS K CA 4752 C C . HIS C 8 ? 1.2168 0.6005 0.5915 -0.0362 0.0041 -0.0499 34 HIS K C 4753 O O . HIS C 8 ? 1.2166 0.5909 0.5818 -0.0474 0.0113 -0.0534 34 HIS K O 4754 C CB . HIS C 8 ? 1.2376 0.6054 0.6012 -0.0285 -0.0230 -0.0445 34 HIS K CB 4755 C CG . HIS C 8 ? 1.2368 0.5938 0.5913 -0.0366 -0.0186 -0.0472 34 HIS K CG 4756 N ND1 . HIS C 8 ? 1.2522 0.5861 0.5822 -0.0533 -0.0213 -0.0456 34 HIS K ND1 4757 C CD2 . HIS C 8 ? 1.2236 0.5901 0.5897 -0.0319 -0.0112 -0.0515 34 HIS K CD2 4758 C CE1 . HIS C 8 ? 1.2491 0.5794 0.5760 -0.0585 -0.0155 -0.0491 34 HIS K CE1 4759 N NE2 . HIS C 8 ? 1.2311 0.5811 0.5805 -0.0451 -0.0094 -0.0529 34 HIS K NE2 4760 N N . SER C 9 ? 1.2233 0.6273 0.6189 -0.0247 0.0085 -0.0508 35 SER K N 4761 C CA . SER C 9 ? 1.2084 0.6225 0.6173 -0.0245 0.0212 -0.0556 35 SER K CA 4762 C C . SER C 9 ? 1.2096 0.6176 0.6120 -0.0368 0.0308 -0.0582 35 SER K C 4763 O O . SER C 9 ? 1.2042 0.6091 0.6063 -0.0450 0.0406 -0.0645 35 SER K O 4764 C CB . SER C 9 ? 1.1990 0.6339 0.6290 -0.0115 0.0221 -0.0545 35 SER K CB 4765 O OG . SER C 9 ? 1.2017 0.6441 0.6354 -0.0011 0.0114 -0.0514 35 SER K OG 4766 N N . LEU C 10 ? 1.0779 0.4855 0.4763 -0.0382 0.0279 -0.0543 36 LEU K N 4767 C CA . LEU C 10 ? 1.0838 0.4852 0.4749 -0.0501 0.0359 -0.0567 36 LEU K CA 4768 C C . LEU C 10 ? 1.0996 0.4833 0.4696 -0.0660 0.0388 -0.0601 36 LEU K C 4769 O O . LEU C 10 ? 1.0996 0.4824 0.4697 -0.0757 0.0505 -0.0674 36 LEU K O 4770 C CB . LEU C 10 ? 1.0899 0.4906 0.4757 -0.0501 0.0299 -0.0510 36 LEU K CB 4771 C CG . LEU C 10 ? 1.1012 0.4907 0.4727 -0.0648 0.0355 -0.0527 36 LEU K CG 4772 C CD1 . LEU C 10 ? 1.0914 0.4893 0.4769 -0.0668 0.0483 -0.0593 36 LEU K CD1 4773 C CD2 . LEU C 10 ? 1.1093 0.4956 0.4728 -0.0647 0.0267 -0.0460 36 LEU K CD2 4774 N N . ARG C 11 ? 1.1616 0.5315 0.5142 -0.0691 0.0276 -0.0552 37 ARG K N 4775 C CA . ARG C 11 ? 1.1746 0.5251 0.5031 -0.0857 0.0272 -0.0563 37 ARG K CA 4776 C C . ARG C 11 ? 1.1655 0.5184 0.4977 -0.0910 0.0382 -0.0643 37 ARG K C 4777 O O . ARG C 11 ? 1.1685 0.5150 0.4891 -0.1071 0.0480 -0.0703 37 ARG K O 4778 C CB . ARG C 11 ? 1.1891 0.5260 0.5046 -0.0833 0.0101 -0.0493 37 ARG K CB 4779 C CG . ARG C 11 ? 1.2084 0.5209 0.4939 -0.1018 0.0043 -0.0468 37 ARG K CG 4780 C CD . ARG C 11 ? 1.2113 0.5178 0.4881 -0.1131 0.0119 -0.0521 37 ARG K CD 4781 N NE . ARG C 11 ? 1.2329 0.5148 0.4782 -0.1326 0.0049 -0.0486 37 ARG K NE 4782 C CZ . ARG C 11 ? 1.2483 0.5130 0.4803 -0.1326 -0.0125 -0.0418 37 ARG K CZ 4783 N NH1 . ARG C 11 ? 1.2431 0.5150 0.4929 -0.1132 -0.0230 -0.0393 37 ARG K NH1 4784 N NH2 . ARG C 11 ? 1.2691 0.5095 0.4703 -0.1524 -0.0199 -0.0377 37 ARG K NH2 4785 N N . ALA C 12 ? 1.2259 0.5889 0.5744 -0.0780 0.0366 -0.0650 38 ALA K N 4786 C CA . ALA C 12 ? 1.2178 0.5834 0.5711 -0.0813 0.0448 -0.0719 38 ALA K CA 4787 C C . ALA C 12 ? 1.2044 0.5819 0.5728 -0.0847 0.0605 -0.0815 38 ALA K C 4788 O O . ALA C 12 ? 1.2051 0.5795 0.5678 -0.0976 0.0701 -0.0896 38 ALA K O 4789 C CB . ALA C 12 ? 1.2082 0.5830 0.5769 -0.0655 0.0389 -0.0702 38 ALA K CB 4790 N N . ASN C 13 ? 1.2172 0.6084 0.6052 -0.0738 0.0626 -0.0812 39 ASN K N 4791 C CA . ASN C 13 ? 1.2062 0.6072 0.6103 -0.0765 0.0753 -0.0904 39 ASN K CA 4792 C C . ASN C 13 ? 1.2164 0.6085 0.6048 -0.0938 0.0828 -0.0955 39 ASN K C 4793 O O . ASN C 13 ? 1.2093 0.6081 0.6093 -0.0992 0.0944 -0.1061 39 ASN K O 4794 C CB . ASN C 13 ? 1.1972 0.6117 0.6227 -0.0622 0.0732 -0.0871 39 ASN K CB 4795 C CG . ASN C 13 ? 1.1852 0.6102 0.6331 -0.0613 0.0834 -0.0966 39 ASN K CG 4796 O OD1 . ASN C 13 ? 1.1738 0.6102 0.6431 -0.0493 0.0820 -0.0963 39 ASN K OD1 4797 N ND2 . ASN C 13 ? 1.1889 0.6100 0.6325 -0.0743 0.0929 -0.1055 39 ASN K ND2 4798 N N . LEU C 14 ? 1.3701 0.7473 0.7332 -0.1027 0.0755 -0.0887 40 LEU K N 4799 C CA . LEU C 14 ? 1.3805 0.7485 0.7261 -0.1194 0.0808 -0.0917 40 LEU K CA 4800 C C . LEU C 14 ? 1.3909 0.7474 0.7142 -0.1400 0.0869 -0.0979 40 LEU K C 4801 O O . LEU C 14 ? 1.3988 0.7462 0.7090 -0.1435 0.0811 -0.0946 40 LEU K O 4802 C CB . LEU C 14 ? 1.3943 0.7521 0.7241 -0.1191 0.0689 -0.0807 40 LEU K CB 4803 C CG . LEU C 14 ? 1.3897 0.7564 0.7328 -0.1111 0.0692 -0.0786 40 LEU K CG 4804 C CD1 . LEU C 14 ? 1.4040 0.7606 0.7311 -0.1111 0.0564 -0.0679 40 LEU K CD1 4805 C CD2 . LEU C 14 ? 1.3865 0.7555 0.7315 -0.1229 0.0827 -0.0890 40 LEU K CD2 4806 N N . VAL C 15 ? 1.1471 0.5045 0.4661 -0.1543 0.0988 -0.1074 41 VAL K N 4807 C CA . VAL C 15 ? 1.1739 0.5208 0.4680 -0.1777 0.1055 -0.1137 41 VAL K CA 4808 C C . VAL C 15 ? 1.1970 0.5253 0.4599 -0.1908 0.0971 -0.1047 41 VAL K C 4809 O O . VAL C 15 ? 1.1959 0.5256 0.4600 -0.1914 0.0987 -0.1047 41 VAL K O 4810 C CB . VAL C 15 ? 1.1739 0.5337 0.4813 -0.1869 0.1236 -0.1309 41 VAL K CB 4811 C CG1 . VAL C 15 ? 1.2046 0.5546 0.4829 -0.2143 0.1315 -0.1380 41 VAL K CG1 4812 C CG2 . VAL C 15 ? 1.1543 0.5309 0.4919 -0.1754 0.1307 -0.1404 41 VAL K CG2 4813 N N . ASP C 16 ? 1.3473 0.6573 0.5826 -0.2014 0.0868 -0.0968 42 ASP K N 4814 C CA . ASP C 16 ? 1.3676 0.6579 0.5736 -0.2132 0.0757 -0.0870 42 ASP K CA 4815 C C . ASP C 16 ? 1.3861 0.6598 0.5574 -0.2415 0.0784 -0.0894 42 ASP K C 4816 O O . ASP C 16 ? 1.4037 0.6585 0.5521 -0.2486 0.0649 -0.0801 42 ASP K O 4817 C CB . ASP C 16 ? 1.3761 0.6563 0.5800 -0.1984 0.0552 -0.0724 42 ASP K CB 4818 C CG . ASP C 16 ? 1.3986 0.6574 0.5744 -0.2092 0.0411 -0.0620 42 ASP K CG 4819 O OD1 . ASP C 16 ? 1.4068 0.6599 0.5655 -0.2266 0.0475 -0.0649 42 ASP K OD1 4820 O OD2 . ASP C 16 ? 1.4078 0.6558 0.5795 -0.2001 0.0229 -0.0514 42 ASP K OD2 4821 N N . PRO C 17 ? 1.3289 0.6091 0.4955 -0.2588 0.0951 -0.1021 43 PRO K N 4822 C CA . PRO C 17 ? 1.3471 0.6167 0.4826 -0.2884 0.1021 -0.1080 43 PRO K CA 4823 C C . PRO C 17 ? 1.3777 0.6193 0.4729 -0.3056 0.0861 -0.0944 43 PRO K C 4824 O O . PRO C 17 ? 1.4015 0.6293 0.4672 -0.3287 0.0856 -0.0944 43 PRO K O 4825 C CB . PRO C 17 ? 1.3422 0.6266 0.4852 -0.2994 0.1216 -0.1242 43 PRO K CB 4826 C CG . PRO C 17 ? 1.3270 0.6179 0.4899 -0.2808 0.1180 -0.1202 43 PRO K CG 4827 C CD . PRO C 17 ? 1.3139 0.6101 0.5016 -0.2529 0.1067 -0.1109 43 PRO K CD 4828 N N . ASN C 18 ? 1.4710 0.7043 0.5646 -0.2958 0.0729 -0.0833 44 ASN K N 4829 C CA . ASN C 18 ? 1.4993 0.7049 0.5578 -0.3091 0.0541 -0.0692 44 ASN K CA 4830 C C . ASN C 18 ? 1.5060 0.6972 0.5648 -0.2930 0.0305 -0.0541 44 ASN K C 4831 O O . ASN C 18 ? 1.5283 0.6954 0.5605 -0.3025 0.0124 -0.0424 44 ASN K O 4832 C CB . ASN C 18 ? 1.5058 0.7078 0.5547 -0.3160 0.0544 -0.0677 44 ASN K CB 4833 C CG . ASN C 18 ? 1.5147 0.7223 0.5497 -0.3406 0.0739 -0.0814 44 ASN K CG 4834 O OD1 . ASN C 18 ? 1.5282 0.7330 0.5456 -0.3611 0.0821 -0.0883 44 ASN K OD1 4835 N ND2 . ASN C 18 ? 1.5077 0.7243 0.5510 -0.3396 0.0819 -0.0865 44 ASN K ND2 4836 N N . ASN C 19 ? 1.5250 0.7310 0.6145 -0.2688 0.0300 -0.0550 45 ASN K N 4837 C CA . ASN C 19 ? 1.5309 0.7271 0.6253 -0.2521 0.0091 -0.0437 45 ASN K CA 4838 C C . ASN C 19 ? 1.5396 0.7263 0.6331 -0.2418 -0.0090 -0.0327 45 ASN K C 4839 O O . ASN C 19 ? 1.5597 0.7234 0.6335 -0.2464 -0.0294 -0.0223 45 ASN K O 4840 C CB . ASN C 19 ? 1.5511 0.7250 0.6182 -0.2679 -0.0016 -0.0387 45 ASN K CB 4841 C CG . ASN C 19 ? 1.5478 0.7296 0.6102 -0.2837 0.0169 -0.0501 45 ASN K CG 4842 O OD1 . ASN C 19 ? 1.5312 0.7300 0.6182 -0.2701 0.0252 -0.0566 45 ASN K OD1 4843 N ND2 . ASN C 19 ? 1.5666 0.7366 0.5969 -0.3134 0.0232 -0.0529 45 ASN K ND2 4844 N N . VAL C 20 ? 1.3220 0.5261 0.4370 -0.2285 -0.0022 -0.0353 46 VAL K N 4845 C CA . VAL C 20 ? 1.3165 0.5172 0.4374 -0.2154 -0.0180 -0.0263 46 VAL K CA 4846 C C . VAL C 20 ? 1.2963 0.5083 0.4446 -0.1893 -0.0276 -0.0237 46 VAL K C 4847 O O . VAL C 20 ? 1.3044 0.5061 0.4519 -0.1807 -0.0474 -0.0157 46 VAL K O 4848 C CB . VAL C 20 ? 1.3016 0.5171 0.4349 -0.2116 -0.0073 -0.0299 46 VAL K CB 4849 C CG1 . VAL C 20 ? 1.3315 0.5296 0.4338 -0.2353 -0.0079 -0.0278 46 VAL K CG1 4850 C CG2 . VAL C 20 ? 1.2773 0.5174 0.4352 -0.2054 0.0146 -0.0419 46 VAL K CG2 4851 N N . LEU C 21 ? 1.3455 0.5790 0.5185 -0.1775 -0.0134 -0.0315 47 LEU K N 4852 C CA . LEU C 21 ? 1.3332 0.5805 0.5324 -0.1545 -0.0187 -0.0311 47 LEU K CA 4853 C C . LEU C 21 ? 1.3466 0.5771 0.5342 -0.1560 -0.0333 -0.0268 47 LEU K C 4854 O O . LEU C 21 ? 1.3408 0.5782 0.5460 -0.1383 -0.0419 -0.0256 47 LEU K O 4855 C CB . LEU C 21 ? 1.3094 0.5801 0.5328 -0.1466 0.0003 -0.0406 47 LEU K CB 4856 C CG . LEU C 21 ? 1.2987 0.5835 0.5334 -0.1459 0.0130 -0.0448 47 LEU K CG 4857 C CD1 . LEU C 21 ? 1.2812 0.5843 0.5353 -0.1437 0.0316 -0.0554 47 LEU K CD1 4858 C CD2 . LEU C 21 ? 1.2931 0.5890 0.5459 -0.1275 0.0044 -0.0395 47 LEU K CD2 4859 N N . GLN C 22 ? 1.4119 0.6196 0.5683 -0.1784 -0.0366 -0.0245 48 GLN K N 4860 C CA . GLN C 22 ? 1.4270 0.6150 0.5673 -0.1846 -0.0502 -0.0202 48 GLN K CA 4861 C C . GLN C 22 ? 1.4377 0.6153 0.5834 -0.1699 -0.0748 -0.0122 48 GLN K C 4862 O O . GLN C 22 ? 1.4477 0.6138 0.5903 -0.1672 -0.0873 -0.0097 48 GLN K O 4863 C CB . GLN C 22 ? 1.4495 0.6132 0.5510 -0.2148 -0.0507 -0.0177 48 GLN K CB 4864 C CG . GLN C 22 ? 1.4586 0.6077 0.5425 -0.2277 -0.0538 -0.0174 48 GLN K CG 4865 C CD . GLN C 22 ? 1.4857 0.6039 0.5466 -0.2340 -0.0808 -0.0059 48 GLN K CD 4866 O OE1 . GLN C 22 ? 1.4987 0.6012 0.5456 -0.2390 -0.0947 0.0015 48 GLN K OE1 4867 N NE2 . GLN C 22 ? 1.4951 0.6031 0.5525 -0.2335 -0.0896 -0.0042 48 GLN K NE2 4868 N N . SER C 23 ? 1.4525 0.6348 0.6076 -0.1600 -0.0819 -0.0092 49 SER K N 4869 C CA . SER C 23 ? 1.4598 0.6360 0.6249 -0.1446 -0.1046 -0.0040 49 SER K CA 4870 C C . SER C 23 ? 1.4385 0.6424 0.6402 -0.1182 -0.1013 -0.0094 49 SER K C 4871 O O . SER C 23 ? 1.4404 0.6444 0.6555 -0.1033 -0.1183 -0.0079 49 SER K O 4872 C CB . SER C 23 ? 1.4737 0.6405 0.6304 -0.1479 -0.1162 0.0017 49 SER K CB 4873 O OG . SER C 23 ? 1.4653 0.6471 0.6251 -0.1518 -0.0984 -0.0014 49 SER K OG 4874 N N . TRP C 24 ? 1.2983 0.5253 0.5160 -0.1133 -0.0801 -0.0161 50 TRP K N 4875 C CA . TRP C 24 ? 1.2780 0.5328 0.5287 -0.0905 -0.0752 -0.0207 50 TRP K CA 4876 C C . TRP C 24 ? 1.2715 0.5288 0.5316 -0.0817 -0.0783 -0.0235 50 TRP K C 4877 O O . TRP C 24 ? 1.2615 0.5247 0.5228 -0.0855 -0.0643 -0.0278 50 TRP K O 4878 C CB . TRP C 24 ? 1.2591 0.5357 0.5226 -0.0899 -0.0527 -0.0262 50 TRP K CB 4879 C CG . TRP C 24 ? 1.2600 0.5405 0.5220 -0.0935 -0.0488 -0.0246 50 TRP K CG 4880 C CD1 . TRP C 24 ? 1.2773 0.5402 0.5205 -0.1036 -0.0596 -0.0191 50 TRP K CD1 4881 C CD2 . TRP C 24 ? 1.2437 0.5464 0.5240 -0.0868 -0.0343 -0.0282 50 TRP K CD2 4882 N NE1 . TRP C 24 ? 1.2722 0.5458 0.5207 -0.1037 -0.0518 -0.0194 50 TRP K NE1 4883 C CE2 . TRP C 24 ? 1.2520 0.5496 0.5232 -0.0935 -0.0365 -0.0249 50 TRP K CE2 4884 C CE3 . TRP C 24 ? 1.2236 0.5487 0.5267 -0.0762 -0.0210 -0.0335 50 TRP K CE3 4885 C CZ2 . TRP C 24 ? 1.2411 0.5552 0.5253 -0.0899 -0.0255 -0.0268 50 TRP K CZ2 4886 C CZ3 . TRP C 24 ? 1.2136 0.5540 0.5292 -0.0730 -0.0111 -0.0350 50 TRP K CZ3 4887 C CH2 . TRP C 24 ? 1.2224 0.5574 0.5287 -0.0798 -0.0133 -0.0318 50 TRP K CH2 4888 N N . ASP C 25 ? 1.5035 0.7598 0.7746 -0.0678 -0.0958 -0.0224 51 ASP K N 4889 C CA . ASP C 25 ? 1.5055 0.7546 0.7787 -0.0625 -0.1053 -0.0236 51 ASP K CA 4890 C C . ASP C 25 ? 1.4890 0.7636 0.7932 -0.0399 -0.1052 -0.0293 51 ASP K C 4891 O O . ASP C 25 ? 1.4947 0.7716 0.8111 -0.0275 -0.1209 -0.0300 51 ASP K O 4892 C CB . ASP C 25 ? 1.5284 0.7489 0.7851 -0.0676 -0.1303 -0.0179 51 ASP K CB 4893 C CG . ASP C 25 ? 1.5327 0.7448 0.7937 -0.0605 -0.1430 -0.0193 51 ASP K CG 4894 O OD1 . ASP C 25 ? 1.5269 0.7416 0.7857 -0.0642 -0.1319 -0.0218 51 ASP K OD1 4895 O OD2 . ASP C 25 ? 1.5413 0.7447 0.8091 -0.0509 -0.1645 -0.0187 51 ASP K OD2 4896 N N . PRO C 26 ? 1.2050 0.4988 0.5223 -0.0351 -0.0882 -0.0341 52 PRO K N 4897 C CA . PRO C 26 ? 1.1842 0.5064 0.5301 -0.0160 -0.0833 -0.0395 52 PRO K CA 4898 C C . PRO C 26 ? 1.1873 0.5108 0.5459 -0.0018 -0.1006 -0.0422 52 PRO K C 4899 O O . PRO C 26 ? 1.1755 0.5226 0.5564 0.0131 -0.1001 -0.0466 52 PRO K O 4900 C CB . PRO C 26 ? 1.1693 0.4995 0.5186 -0.0181 -0.0677 -0.0429 52 PRO K CB 4901 C CG . PRO C 26 ? 1.1769 0.4933 0.5058 -0.0369 -0.0577 -0.0408 52 PRO K CG 4902 C CD . PRO C 26 ? 1.2019 0.4914 0.5067 -0.0493 -0.0721 -0.0351 52 PRO K CD 4903 N N . THR C 27 ? 1.3069 0.6056 0.6513 -0.0070 -0.1158 -0.0400 53 THR K N 4904 C CA . THR C 27 ? 1.3107 0.6078 0.6677 0.0063 -0.1340 -0.0435 53 THR K CA 4905 C C . THR C 27 ? 1.3239 0.6154 0.6854 0.0117 -0.1527 -0.0430 53 THR K C 4906 O O . THR C 27 ? 1.3286 0.6167 0.7015 0.0226 -0.1706 -0.0470 53 THR K O 4907 C CB . THR C 27 ? 1.3216 0.5927 0.6621 -0.0016 -0.1444 -0.0413 53 THR K CB 4908 O OG1 . THR C 27 ? 1.3352 0.5889 0.6764 0.0037 -0.1697 -0.0410 53 THR K OG1 4909 C CG2 . THR C 27 ? 1.3341 0.5827 0.6441 -0.0246 -0.1376 -0.0344 53 THR K CG2 4910 N N . LEU C 28 ? 1.2450 0.5352 0.5982 0.0041 -0.1491 -0.0388 54 LEU K N 4911 C CA . LEU C 28 ? 1.2562 0.5442 0.6158 0.0096 -0.1653 -0.0388 54 LEU K CA 4912 C C . LEU C 28 ? 1.2405 0.5636 0.6316 0.0281 -0.1613 -0.0471 54 LEU K C 4913 O O . LEU C 28 ? 1.2225 0.5704 0.6241 0.0317 -0.1424 -0.0496 54 LEU K O 4914 C CB . LEU C 28 ? 1.2678 0.5428 0.6070 -0.0058 -0.1621 -0.0314 54 LEU K CB 4915 C CG . LEU C 28 ? 1.2884 0.5407 0.6189 -0.0090 -0.1858 -0.0274 54 LEU K CG 4916 C CD1 . LEU C 28 ? 1.3061 0.5242 0.6143 -0.0200 -0.2014 -0.0224 54 LEU K CD1 4917 C CD2 . LEU C 28 ? 1.2956 0.5433 0.6114 -0.0212 -0.1801 -0.0216 54 LEU K CD2 4918 N N . VAL C 29 ? 1.2898 0.6148 0.6957 0.0388 -0.1798 -0.0516 55 VAL K N 4919 C CA . VAL C 29 ? 1.2803 0.6393 0.7167 0.0556 -0.1780 -0.0615 55 VAL K CA 4920 C C . VAL C 29 ? 1.2738 0.6567 0.7151 0.0541 -0.1605 -0.0604 55 VAL K C 4921 O O . VAL C 29 ? 1.2647 0.6788 0.7285 0.0652 -0.1541 -0.0678 55 VAL K O 4922 C CB . VAL C 29 ? 1.2925 0.6476 0.7439 0.0658 -0.2023 -0.0675 55 VAL K CB 4923 N N . ASN C 30 ? 1.3145 0.6824 0.7341 0.0393 -0.1531 -0.0514 56 ASN K N 4924 C CA . ASN C 30 ? 1.3085 0.6939 0.7294 0.0356 -0.1369 -0.0492 56 ASN K CA 4925 C C . ASN C 30 ? 1.3169 0.6774 0.7106 0.0180 -0.1336 -0.0400 56 ASN K C 4926 O O . ASN C 30 ? 1.3306 0.6625 0.7063 0.0095 -0.1471 -0.0357 56 ASN K O 4927 C CB . ASN C 30 ? 1.3140 0.7181 0.7529 0.0443 -0.1440 -0.0536 56 ASN K CB 4928 C CG . ASN C 30 ? 1.3318 0.7131 0.7632 0.0414 -0.1652 -0.0512 56 ASN K CG 4929 O OD1 . ASN C 30 ? 1.3338 0.6937 0.7435 0.0279 -0.1664 -0.0429 56 ASN K OD1 4930 N ND2 . ASN C 30 ? 1.3451 0.7310 0.7952 0.0539 -0.1828 -0.0591 56 ASN K ND2 4931 N N . PRO C 31 ? 1.3027 0.6730 0.6925 0.0114 -0.1163 -0.0372 57 PRO K N 4932 C CA . PRO C 31 ? 1.3115 0.6569 0.6747 -0.0062 -0.1141 -0.0300 57 PRO K CA 4933 C C . PRO C 31 ? 1.3257 0.6630 0.6819 -0.0113 -0.1235 -0.0261 57 PRO K C 4934 O O . PRO C 31 ? 1.3270 0.6577 0.6684 -0.0237 -0.1142 -0.0217 57 PRO K O 4935 C CB . PRO C 31 ? 1.2959 0.6545 0.6594 -0.0110 -0.0915 -0.0300 57 PRO K CB 4936 C CG . PRO C 31 ? 1.2859 0.6759 0.6743 0.0025 -0.0859 -0.0341 57 PRO K CG 4937 C CD . PRO C 31 ? 1.2883 0.6877 0.6937 0.0169 -0.0994 -0.0397 57 PRO K CD 4938 N N . CYS C 32 ? 1.3851 0.7209 0.7510 -0.0029 -0.1425 -0.0280 58 CYS K N 4939 C CA . CYS C 32 ? 1.3984 0.7289 0.7599 -0.0070 -0.1511 -0.0246 58 CYS K CA 4940 C C . CYS C 32 ? 1.4165 0.7107 0.7514 -0.0211 -0.1667 -0.0175 58 CYS K C 4941 O O . CYS C 32 ? 1.4283 0.7120 0.7532 -0.0285 -0.1739 -0.0131 58 CYS K O 4942 C CB . CYS C 32 ? 1.3996 0.7511 0.7883 0.0091 -0.1628 -0.0315 58 CYS K CB 4943 S SG . CYS C 32 ? 1.3845 0.7800 0.8001 0.0209 -0.1438 -0.0383 58 CYS K SG 4944 N N . THR C 33 ? 1.2873 0.5621 0.6103 -0.0255 -0.1728 -0.0163 59 THR K N 4945 C CA . THR C 33 ? 1.3073 0.5453 0.6007 -0.0419 -0.1872 -0.0086 59 THR K CA 4946 C C . THR C 33 ? 1.3061 0.5331 0.5736 -0.0608 -0.1693 -0.0044 59 THR K C 4947 O O . THR C 33 ? 1.3230 0.5209 0.5621 -0.0781 -0.1765 0.0017 59 THR K O 4948 C CB . THR C 33 ? 1.3178 0.5370 0.6121 -0.0369 -0.2096 -0.0092 59 THR K CB 4949 O OG1 . THR C 33 ? 1.3212 0.5220 0.5938 -0.0495 -0.2047 -0.0059 59 THR K OG1 4950 C CG2 . THR C 33 ? 1.3042 0.5502 0.6336 -0.0138 -0.2127 -0.0194 59 THR K CG2 4951 N N . TRP C 34 ? 1.4483 0.6993 0.7263 -0.0578 -0.1461 -0.0083 60 TRP K N 4952 C CA . TRP C 34 ? 1.4449 0.6891 0.7029 -0.0747 -0.1282 -0.0067 60 TRP K CA 4953 C C . TRP C 34 ? 1.4551 0.6890 0.6942 -0.0899 -0.1253 -0.0021 60 TRP K C 4954 O O . TRP C 34 ? 1.4593 0.7001 0.7069 -0.0844 -0.1314 -0.0009 60 TRP K O 4955 C CB . TRP C 34 ? 1.4217 0.6936 0.6989 -0.0662 -0.1063 -0.0128 60 TRP K CB 4956 C CG . TRP C 34 ? 1.4131 0.6912 0.7024 -0.0561 -0.1070 -0.0168 60 TRP K CG 4957 C CD1 . TRP C 34 ? 1.4219 0.6873 0.7112 -0.0508 -0.1251 -0.0164 60 TRP K CD1 4958 C CD2 . TRP C 34 ? 1.3939 0.6915 0.6973 -0.0500 -0.0898 -0.0219 60 TRP K CD2 4959 N NE1 . TRP C 34 ? 1.4091 0.6858 0.7114 -0.0418 -0.1192 -0.0212 60 TRP K NE1 4960 C CE2 . TRP C 34 ? 1.3917 0.6884 0.7026 -0.0413 -0.0976 -0.0244 60 TRP K CE2 4961 C CE3 . TRP C 34 ? 1.3781 0.6933 0.6895 -0.0507 -0.0697 -0.0248 60 TRP K CE3 4962 C CZ2 . TRP C 34 ? 1.3743 0.6873 0.6991 -0.0340 -0.0854 -0.0292 60 TRP K CZ2 4963 C CZ3 . TRP C 34 ? 1.3615 0.6920 0.6874 -0.0433 -0.0587 -0.0294 60 TRP K CZ3 4964 C CH2 . TRP C 34 ? 1.3597 0.6892 0.6916 -0.0353 -0.0662 -0.0314 60 TRP K CH2 4965 N N . PHE C 35 ? 1.2913 0.5089 0.5044 -0.1100 -0.1162 -0.0001 61 PHE K N 4966 C CA . PHE C 35 ? 1.3010 0.5114 0.4962 -0.1256 -0.1098 0.0026 61 PHE K CA 4967 C C . PHE C 35 ? 1.2758 0.5127 0.4887 -0.1199 -0.0878 -0.0030 61 PHE K C 4968 O O . PHE C 35 ? 1.2553 0.5105 0.4865 -0.1098 -0.0759 -0.0084 61 PHE K O 4969 C CB . PHE C 35 ? 1.3251 0.5095 0.4856 -0.1506 -0.1082 0.0055 61 PHE K CB 4970 C CG . PHE C 35 ? 1.3548 0.5089 0.4936 -0.1595 -0.1328 0.0133 61 PHE K CG 4971 C CD1 . PHE C 35 ? 1.3644 0.5113 0.5059 -0.1538 -0.1520 0.0183 61 PHE K CD1 4972 C CD2 . PHE C 35 ? 1.3736 0.5065 0.4908 -0.1729 -0.1384 0.0156 61 PHE K CD2 4973 C CE1 . PHE C 35 ? 1.3925 0.5099 0.5158 -0.1611 -0.1774 0.0256 61 PHE K CE1 4974 C CE2 . PHE C 35 ? 1.4026 0.5053 0.4997 -0.1811 -0.1637 0.0237 61 PHE K CE2 4975 C CZ . PHE C 35 ? 1.4121 0.5064 0.5126 -0.1749 -0.1838 0.0287 61 PHE K CZ 4976 N N . HIS C 36 ? 1.3439 0.5825 0.5524 -0.1256 -0.0841 -0.0015 62 HIS K N 4977 C CA . HIS C 36 ? 1.3260 0.5869 0.5500 -0.1216 -0.0650 -0.0063 62 HIS K CA 4978 C C . HIS C 36 ? 1.3109 0.5991 0.5674 -0.0993 -0.0637 -0.0089 62 HIS K C 4979 O O . HIS C 36 ? 1.2981 0.6050 0.5692 -0.0945 -0.0510 -0.0116 62 HIS K O 4980 C CB . HIS C 36 ? 1.3161 0.5780 0.5336 -0.1323 -0.0462 -0.0121 62 HIS K CB 4981 C CG . HIS C 36 ? 1.3331 0.5695 0.5181 -0.1549 -0.0480 -0.0105 62 HIS K CG 4982 N ND1 . HIS C 36 ? 1.3495 0.5675 0.5104 -0.1706 -0.0553 -0.0056 62 HIS K ND1 4983 C CD2 . HIS C 36 ? 1.3374 0.5637 0.5088 -0.1659 -0.0438 -0.0131 62 HIS K CD2 4984 C CE1 . HIS C 36 ? 1.3637 0.5611 0.4961 -0.1912 -0.0553 -0.0050 62 HIS K CE1 4985 N NE2 . HIS C 36 ? 1.3569 0.5593 0.4953 -0.1889 -0.0482 -0.0096 62 HIS K NE2 4986 N N . VAL C 37 ? 1.2698 0.5602 0.5374 -0.0865 -0.0774 -0.0084 63 VAL K N 4987 C CA . VAL C 37 ? 1.2591 0.5754 0.5554 -0.0672 -0.0782 -0.0112 63 VAL K CA 4988 C C . VAL C 37 ? 1.2741 0.5879 0.5734 -0.0622 -0.0960 -0.0083 63 VAL K C 4989 O O . VAL C 37 ? 1.2912 0.5818 0.5745 -0.0690 -0.1122 -0.0044 63 VAL K O 4990 C CB . VAL C 37 ? 1.2491 0.5738 0.5594 -0.0553 -0.0797 -0.0150 63 VAL K CB 4991 C CG1 . VAL C 37 ? 1.2407 0.5924 0.5789 -0.0369 -0.0817 -0.0185 63 VAL K CG1 4992 C CG2 . VAL C 37 ? 1.2327 0.5607 0.5416 -0.0601 -0.0621 -0.0184 63 VAL K CG2 4993 N N . THR C 38 ? 1.2485 0.5854 0.5677 -0.0516 -0.0937 -0.0100 64 THR K N 4994 C CA . THR C 38 ? 1.2615 0.6005 0.5879 -0.0458 -0.1096 -0.0089 64 THR K CA 4995 C C . THR C 38 ? 1.2532 0.6229 0.6091 -0.0282 -0.1086 -0.0147 64 THR K C 4996 O O . THR C 38 ? 1.2417 0.6321 0.6087 -0.0250 -0.0935 -0.0165 64 THR K O 4997 C CB . THR C 38 ? 1.2682 0.6045 0.5853 -0.0552 -0.1066 -0.0050 64 THR K CB 4998 O OG1 . THR C 38 ? 1.2774 0.5853 0.5649 -0.0736 -0.1073 -0.0001 64 THR K OG1 4999 C CG2 . THR C 38 ? 1.2814 0.6240 0.6099 -0.0477 -0.1226 -0.0049 64 THR K CG2 5000 N N . CYS C 39 ? 1.3219 0.6948 0.6908 -0.0174 -0.1251 -0.0182 65 CYS K N 5001 C CA . CYS C 39 ? 1.3145 0.7187 0.7119 -0.0014 -0.1242 -0.0255 65 CYS K CA 5002 C C . CYS C 39 ? 1.3253 0.7406 0.7353 0.0036 -0.1355 -0.0277 65 CYS K C 5003 O O . CYS C 39 ? 1.3378 0.7339 0.7346 -0.0040 -0.1462 -0.0231 65 CYS K O 5004 C CB . CYS C 39 ? 1.3113 0.7160 0.7193 0.0090 -0.1335 -0.0312 65 CYS K CB 5005 S SG . CYS C 39 ? 1.2966 0.6980 0.6982 0.0071 -0.1191 -0.0312 65 CYS K SG 5006 N N . ASN C 40 ? 1.3492 0.7959 0.7846 0.0160 -0.1335 -0.0352 66 ASN K N 5007 C CA . ASN C 40 ? 1.3590 0.8220 0.8111 0.0221 -0.1435 -0.0397 66 ASN K CA 5008 C C . ASN C 40 ? 1.3677 0.8298 0.8356 0.0333 -0.1638 -0.0477 66 ASN K C 5009 O O . ASN C 40 ? 1.3706 0.8101 0.8297 0.0333 -0.1734 -0.0467 66 ASN K O 5010 C CB . ASN C 40 ? 1.3517 0.8511 0.8220 0.0268 -0.1300 -0.0441 66 ASN K CB 5011 C CG . ASN C 40 ? 1.3382 0.8576 0.8204 0.0340 -0.1192 -0.0493 66 ASN K CG 5012 O OD1 . ASN C 40 ? 1.3377 0.8536 0.8257 0.0413 -0.1259 -0.0543 66 ASN K OD1 5013 N ND2 . ASN C 40 ? 1.3282 0.8675 0.8134 0.0315 -0.1031 -0.0478 66 ASN K ND2 5014 N N . ASN C 41 ? 1.4025 0.8875 0.8932 0.0421 -0.1716 -0.0558 67 ASN K N 5015 C CA . ASN C 41 ? 1.4088 0.8982 0.9208 0.0548 -0.1906 -0.0664 67 ASN K CA 5016 C C . ASN C 41 ? 1.3956 0.9123 0.9288 0.0665 -0.1836 -0.0773 67 ASN K C 5017 O O . ASN C 41 ? 1.3964 0.9182 0.9488 0.0780 -0.1978 -0.0877 67 ASN K O 5018 C CB . ASN C 41 ? 1.4226 0.9249 0.9524 0.0594 -0.2035 -0.0725 67 ASN K CB 5019 C CG . ASN C 41 ? 1.4397 0.9066 0.9552 0.0536 -0.2248 -0.0659 67 ASN K CG 5020 O OD1 . ASN C 41 ? 1.4420 0.8750 0.9284 0.0420 -0.2258 -0.0545 67 ASN K OD1 5021 N ND2 . ASN C 41 ? 1.4521 0.9270 0.9879 0.0609 -0.2423 -0.0736 67 ASN K ND2 5022 N N . GLU C 42 ? 1.2761 0.8100 0.8060 0.0633 -0.1625 -0.0749 68 GLU K N 5023 C CA . GLU C 42 ? 1.2623 0.8191 0.8070 0.0718 -0.1539 -0.0832 68 GLU K CA 5024 C C . GLU C 42 ? 1.2531 0.7857 0.7803 0.0686 -0.1503 -0.0771 68 GLU K C 5025 O O . GLU C 42 ? 1.2408 0.7863 0.7766 0.0747 -0.1442 -0.0824 68 GLU K O 5026 C CB . GLU C 42 ? 1.2536 0.8435 0.8053 0.0697 -0.1347 -0.0842 68 GLU K CB 5027 N N . ASN C 43 ? 1.2620 0.7601 0.7642 0.0581 -0.1542 -0.0663 69 ASN K N 5028 C CA . ASN C 43 ? 1.2552 0.7286 0.7383 0.0523 -0.1505 -0.0602 69 ASN K CA 5029 C C . ASN C 43 ? 1.2397 0.7233 0.7169 0.0480 -0.1289 -0.0567 69 ASN K C 5030 O O . ASN C 43 ? 1.2317 0.7071 0.7036 0.0483 -0.1251 -0.0564 69 ASN K O 5031 C CB . ASN C 43 ? 1.2549 0.7199 0.7464 0.0615 -0.1651 -0.0668 69 ASN K CB 5032 C CG . ASN C 43 ? 1.2709 0.7199 0.7671 0.0651 -0.1895 -0.0695 69 ASN K CG 5033 O OD1 . ASN C 43 ? 1.2830 0.6991 0.7576 0.0551 -0.2001 -0.0607 69 ASN K OD1 5034 N ND2 . ASN C 43 ? 1.2714 0.7437 0.7964 0.0789 -0.1993 -0.0822 69 ASN K ND2 5035 N N . SER C 44 ? 1.3515 0.8516 0.8296 0.0438 -0.1158 -0.0540 70 SER K N 5036 C CA . SER C 44 ? 1.3396 0.8428 0.8092 0.0374 -0.0973 -0.0489 70 SER K CA 5037 C C . SER C 44 ? 1.3438 0.8243 0.7914 0.0238 -0.0926 -0.0398 70 SER K C 5038 O O . SER C 44 ? 1.3548 0.8287 0.7977 0.0196 -0.0997 -0.0373 70 SER K O 5039 C CB . SER C 44 ? 1.3345 0.8702 0.8191 0.0405 -0.0862 -0.0516 70 SER K CB 5040 O OG . SER C 44 ? 1.3292 0.8607 0.8022 0.0312 -0.0718 -0.0442 70 SER K OG 5041 N N . VAL C 45 ? 1.2081 0.6779 0.6434 0.0166 -0.0805 -0.0356 71 VAL K N 5042 C CA . VAL C 45 ? 1.2107 0.6596 0.6255 0.0029 -0.0749 -0.0289 71 VAL K CA 5043 C C . VAL C 45 ? 1.2112 0.6733 0.6290 -0.0008 -0.0669 -0.0262 71 VAL K C 5044 O O . VAL C 45 ? 1.2024 0.6851 0.6318 0.0026 -0.0567 -0.0272 71 VAL K O 5045 C CB . VAL C 45 ? 1.1982 0.6368 0.6034 -0.0031 -0.0629 -0.0276 71 VAL K CB 5046 C CG1 . VAL C 45 ? 1.1991 0.6220 0.5867 -0.0173 -0.0541 -0.0230 71 VAL K CG1 5047 C CG2 . VAL C 45 ? 1.1992 0.6214 0.5978 -0.0020 -0.0711 -0.0292 71 VAL K CG2 5048 N N . ILE C 46 ? 1.1471 0.5974 0.5545 -0.0079 -0.0728 -0.0226 72 ILE K N 5049 C CA . ILE C 46 ? 1.1441 0.6023 0.5507 -0.0137 -0.0643 -0.0193 72 ILE K CA 5050 C C . ILE C 46 ? 1.1504 0.5871 0.5368 -0.0276 -0.0561 -0.0148 72 ILE K C 5051 O O . ILE C 46 ? 1.1468 0.5888 0.5329 -0.0326 -0.0474 -0.0127 72 ILE K O 5052 C CB . ILE C 46 ? 1.1506 0.6182 0.5642 -0.0112 -0.0746 -0.0196 72 ILE K CB 5053 C CG1 . ILE C 46 ? 1.1687 0.6104 0.5637 -0.0207 -0.0845 -0.0153 72 ILE K CG1 5054 C CG2 . ILE C 46 ? 1.1489 0.6345 0.5819 0.0019 -0.0851 -0.0265 72 ILE K CG2 5055 C CD1 . ILE C 46 ? 1.1848 0.6094 0.5751 -0.0182 -0.1002 -0.0166 72 ILE K CD1 5056 N N . ARG C 47 ? 1.3661 0.7795 0.7361 -0.0345 -0.0586 -0.0141 73 ARG K N 5057 C CA . ARG C 47 ? 1.3667 0.7602 0.7165 -0.0494 -0.0511 -0.0115 73 ARG K CA 5058 C C . ARG C 47 ? 1.3600 0.7395 0.6995 -0.0547 -0.0459 -0.0134 73 ARG K C 5059 O O . ARG C 47 ? 1.3639 0.7365 0.7019 -0.0508 -0.0549 -0.0142 73 ARG K O 5060 C CB . ARG C 47 ? 1.3840 0.7572 0.7155 -0.0590 -0.0628 -0.0075 73 ARG K CB 5061 C CG . ARG C 47 ? 1.3923 0.7750 0.7306 -0.0562 -0.0696 -0.0055 73 ARG K CG 5062 C CD . ARG C 47 ? 1.4075 0.7664 0.7237 -0.0691 -0.0788 -0.0010 73 ARG K CD 5063 N NE . ARG C 47 ? 1.4012 0.7470 0.6993 -0.0840 -0.0661 0.0001 73 ARG K NE 5064 C CZ . ARG C 47 ? 1.3930 0.7469 0.6933 -0.0878 -0.0560 0.0004 73 ARG K CZ 5065 N NH1 . ARG C 47 ? 1.3908 0.7648 0.7085 -0.0788 -0.0573 0.0009 73 ARG K NH1 5066 N NH2 . ARG C 47 ? 1.3876 0.7299 0.6730 -0.1012 -0.0446 -0.0005 73 ARG K NH2 5067 N N . VAL C 48 ? 1.1794 0.5549 0.5125 -0.0637 -0.0317 -0.0149 74 VAL K N 5068 C CA . VAL C 48 ? 1.1792 0.5388 0.4982 -0.0733 -0.0263 -0.0173 74 VAL K CA 5069 C C . VAL C 48 ? 1.1850 0.5302 0.4855 -0.0903 -0.0183 -0.0178 74 VAL K C 5070 O O . VAL C 48 ? 1.1753 0.5295 0.4835 -0.0918 -0.0059 -0.0208 74 VAL K O 5071 C CB . VAL C 48 ? 1.1612 0.5346 0.4958 -0.0667 -0.0144 -0.0221 74 VAL K CB 5072 C CG1 . VAL C 48 ? 1.1605 0.5198 0.4821 -0.0775 -0.0071 -0.0259 74 VAL K CG1 5073 C CG2 . VAL C 48 ? 1.1558 0.5437 0.5073 -0.0513 -0.0214 -0.0223 74 VAL K CG2 5074 N N . ASP C 49 ? 1.5874 0.9102 0.8635 -0.1038 -0.0253 -0.0153 75 ASP K N 5075 C CA . ASP C 49 ? 1.5913 0.9024 0.8494 -0.1211 -0.0166 -0.0168 75 ASP K CA 5076 C C . ASP C 49 ? 1.5921 0.8893 0.8326 -0.1358 -0.0089 -0.0213 75 ASP K C 5077 O O . ASP C 49 ? 1.6068 0.8840 0.8246 -0.1472 -0.0181 -0.0180 75 ASP K O 5078 C CB . ASP C 49 ? 1.6095 0.9057 0.8497 -0.1295 -0.0292 -0.0105 75 ASP K CB 5079 C CG . ASP C 49 ? 1.6113 0.9215 0.8685 -0.1158 -0.0381 -0.0066 75 ASP K CG 5080 O OD1 . ASP C 49 ? 1.6150 0.9290 0.8817 -0.1041 -0.0513 -0.0043 75 ASP K OD1 5081 O OD2 . ASP C 49 ? 1.6103 0.9279 0.8715 -0.1174 -0.0322 -0.0066 75 ASP K OD2 5082 N N . LEU C 50 ? 1.2079 0.5159 0.4593 -0.1365 0.0075 -0.0291 76 LEU K N 5083 C CA . LEU C 50 ? 1.2142 0.5141 0.4529 -0.1511 0.0185 -0.0362 76 LEU K CA 5084 C C . LEU C 50 ? 1.2199 0.5175 0.4496 -0.1668 0.0320 -0.0432 76 LEU K C 5085 O O . LEU C 50 ? 1.2205 0.5179 0.4466 -0.1772 0.0444 -0.0522 76 LEU K O 5086 C CB . LEU C 50 ? 1.1968 0.5093 0.4543 -0.1411 0.0258 -0.0418 76 LEU K CB 5087 C CG . LEU C 50 ? 1.1970 0.5072 0.4567 -0.1304 0.0126 -0.0362 76 LEU K CG 5088 C CD1 . LEU C 50 ? 1.1747 0.5030 0.4598 -0.1151 0.0184 -0.0402 76 LEU K CD1 5089 C CD2 . LEU C 50 ? 1.2187 0.5077 0.4521 -0.1455 0.0071 -0.0350 76 LEU K CD2 5090 N N . GLY C 51 ? 1.3595 0.6581 0.5890 -0.1674 0.0307 -0.0406 77 GLY K N 5091 C CA . GLY C 51 ? 1.3596 0.6572 0.5826 -0.1814 0.0433 -0.0482 77 GLY K CA 5092 C C . GLY C 51 ? 1.3713 0.6520 0.5649 -0.2046 0.0476 -0.0524 77 GLY K C 5093 O O . GLY C 51 ? 1.3888 0.6517 0.5579 -0.2138 0.0352 -0.0445 77 GLY K O 5094 N N . ASN C 52 ? 1.2823 0.5689 0.4787 -0.2147 0.0646 -0.0654 78 ASN K N 5095 C CA . ASN C 52 ? 1.2933 0.5677 0.4625 -0.2392 0.0719 -0.0722 78 ASN K CA 5096 C C . ASN C 52 ? 1.3008 0.5647 0.4542 -0.2458 0.0668 -0.0696 78 ASN K C 5097 O O . ASN C 52 ? 1.3203 0.5659 0.4415 -0.2662 0.0624 -0.0667 78 ASN K O 5098 C CB . ASN C 52 ? 1.3137 0.5714 0.4532 -0.2574 0.0668 -0.0677 78 ASN K CB 5099 C CG . ASN C 52 ? 1.3016 0.5681 0.4512 -0.2583 0.0762 -0.0743 78 ASN K CG 5100 O OD1 . ASN C 52 ? 1.2977 0.5658 0.4553 -0.2473 0.0679 -0.0665 78 ASN K OD1 5101 N ND2 . ASN C 52 ? 1.2983 0.5715 0.4489 -0.2713 0.0936 -0.0897 78 ASN K ND2 5102 N N . ALA C 53 ? 1.4406 0.7147 0.6148 -0.2300 0.0665 -0.0701 79 ALA K N 5103 C CA . ALA C 53 ? 1.4477 0.7117 0.6079 -0.2356 0.0610 -0.0674 79 ALA K CA 5104 C C . ALA C 53 ? 1.4390 0.7104 0.6011 -0.2467 0.0778 -0.0813 79 ALA K C 5105 O O . ALA C 53 ? 1.4434 0.7087 0.5964 -0.2511 0.0750 -0.0803 79 ALA K O 5106 C CB . ALA C 53 ? 1.4419 0.7105 0.6201 -0.2132 0.0486 -0.0590 79 ALA K CB 5107 N N . ASP C 54 ? 1.3919 0.6771 0.5674 -0.2507 0.0945 -0.0948 80 ASP K N 5108 C CA . ASP C 54 ? 1.3807 0.6771 0.5640 -0.2600 0.1118 -0.1110 80 ASP K CA 5109 C C . ASP C 54 ? 1.3632 0.6728 0.5744 -0.2409 0.1125 -0.1127 80 ASP K C 5110 O O . ASP C 54 ? 1.3574 0.6724 0.5708 -0.2482 0.1220 -0.1226 80 ASP K O 5111 C CB . ASP C 54 ? 1.3989 0.6804 0.5462 -0.2878 0.1143 -0.1134 80 ASP K CB 5112 C CG . ASP C 54 ? 1.4112 0.6936 0.5431 -0.3115 0.1287 -0.1262 80 ASP K CG 5113 O OD1 . ASP C 54 ? 1.3961 0.6966 0.5477 -0.3139 0.1464 -0.1442 80 ASP K OD1 5114 O OD2 . ASP C 54 ? 1.4369 0.7021 0.5371 -0.3285 0.1220 -0.1191 80 ASP K OD2 5115 N N . LEU C 55 ? 1.2486 0.5641 0.4808 -0.2174 0.1025 -0.1035 81 LEU K N 5116 C CA . LEU C 55 ? 1.2308 0.5585 0.4886 -0.1988 0.1015 -0.1036 81 LEU K CA 5117 C C . LEU C 55 ? 1.2119 0.5587 0.4994 -0.1938 0.1169 -0.1190 81 LEU K C 5118 O O . LEU C 55 ? 1.2068 0.5604 0.5058 -0.1936 0.1234 -0.1253 81 LEU K O 5119 C CB . LEU C 55 ? 1.2260 0.5566 0.4975 -0.1769 0.0875 -0.0907 81 LEU K CB 5120 C CG . LEU C 55 ? 1.2431 0.5572 0.4923 -0.1776 0.0702 -0.0763 81 LEU K CG 5121 C CD1 . LEU C 55 ? 1.2352 0.5577 0.5024 -0.1575 0.0605 -0.0677 81 LEU K CD1 5122 C CD2 . LEU C 55 ? 1.2546 0.5575 0.4899 -0.1800 0.0614 -0.0715 81 LEU K CD2 5123 N N . SER C 56 ? 1.4103 0.7652 0.7111 -0.1899 0.1219 -0.1254 82 SER K N 5124 C CA . SER C 56 ? 1.3925 0.7656 0.7252 -0.1829 0.1341 -0.1399 82 SER K CA 5125 C C . SER C 56 ? 1.3809 0.7633 0.7386 -0.1608 0.1275 -0.1344 82 SER K C 5126 O O . SER C 56 ? 1.3865 0.7626 0.7364 -0.1518 0.1149 -0.1209 82 SER K O 5127 C CB . SER C 56 ? 1.3914 0.7685 0.7201 -0.2004 0.1485 -0.1562 82 SER K CB 5128 O OG . SER C 56 ? 1.3714 0.7665 0.7337 -0.1938 0.1599 -0.1722 82 SER K OG 5129 N N . GLY C 57 ? 1.4959 0.8934 0.8841 -0.1522 0.1353 -0.1456 83 GLY K N 5130 C CA . GLY C 57 ? 1.4846 0.8908 0.8954 -0.1330 0.1291 -0.1408 83 GLY K CA 5131 C C . GLY C 57 ? 1.4823 0.8923 0.9071 -0.1167 0.1199 -0.1307 83 GLY K C 5132 O O . GLY C 57 ? 1.4827 0.8945 0.9144 -0.1177 0.1225 -0.1338 83 GLY K O 5133 N N . GLN C 58 ? 1.3702 0.7819 0.7990 -0.1025 0.1093 -0.1191 84 GLN K N 5134 C CA . GLN C 58 ? 1.3667 0.7854 0.8120 -0.0872 0.1017 -0.1110 84 GLN K CA 5135 C C . GLN C 58 ? 1.3735 0.7893 0.8075 -0.0789 0.0890 -0.0961 84 GLN K C 5136 O O . GLN C 58 ? 1.3832 0.7887 0.7950 -0.0848 0.0842 -0.0909 84 GLN K O 5137 C CB . GLN C 58 ? 1.3534 0.7845 0.8280 -0.0750 0.1028 -0.1156 84 GLN K CB 5138 C CG . GLN C 58 ? 1.3512 0.7881 0.8465 -0.0779 0.1119 -0.1296 84 GLN K CG 5139 C CD . GLN C 58 ? 1.3345 0.7794 0.8495 -0.0750 0.1172 -0.1402 84 GLN K CD 5140 O OE1 . GLN C 58 ? 1.3314 0.7744 0.8360 -0.0797 0.1197 -0.1420 84 GLN K OE1 5141 N NE2 . GLN C 58 ? 1.3240 0.7770 0.8681 -0.0672 0.1178 -0.1472 84 GLN K NE2 5142 N N . LEU C 59 ? 1.0595 0.4845 0.5099 -0.0656 0.0830 -0.0899 85 LEU K N 5143 C CA . LEU C 59 ? 1.0586 0.4857 0.5037 -0.0565 0.0717 -0.0775 85 LEU K CA 5144 C C . LEU C 59 ? 1.0463 0.4846 0.5079 -0.0432 0.0676 -0.0749 85 LEU K C 5145 O O . LEU C 59 ? 1.0378 0.4824 0.5177 -0.0399 0.0723 -0.0810 85 LEU K O 5146 C CB . LEU C 59 ? 1.0596 0.4898 0.5084 -0.0544 0.0687 -0.0724 85 LEU K CB 5147 C CG . LEU C 59 ? 1.0729 0.4927 0.5042 -0.0659 0.0701 -0.0723 85 LEU K CG 5148 C CD1 . LEU C 59 ? 1.0728 0.4972 0.5156 -0.0646 0.0712 -0.0721 85 LEU K CD1 5149 C CD2 . LEU C 59 ? 1.0795 0.4942 0.4934 -0.0652 0.0601 -0.0627 85 LEU K CD2 5150 N N . VAL C 60 ? 1.3952 0.8362 0.8513 -0.0358 0.0584 -0.0665 86 VAL K N 5151 C CA . VAL C 60 ? 1.3895 0.8428 0.8603 -0.0237 0.0541 -0.0635 86 VAL K CA 5152 C C . VAL C 60 ? 1.3976 0.8608 0.8729 -0.0168 0.0472 -0.0554 86 VAL K C 5153 O O . VAL C 60 ? 1.4079 0.8676 0.8719 -0.0199 0.0437 -0.0513 86 VAL K O 5154 C CB . VAL C 60 ? 1.3888 0.8395 0.8513 -0.0208 0.0496 -0.0625 86 VAL K CB 5155 C CG1 . VAL C 60 ? 1.3825 0.8247 0.8410 -0.0287 0.0567 -0.0704 86 VAL K CG1 5156 C CG2 . VAL C 60 ? 1.4021 0.8455 0.8468 -0.0227 0.0416 -0.0570 86 VAL K CG2 5157 N N . PRO C 61 ? 1.2319 0.7076 0.7232 -0.0084 0.0450 -0.0530 87 PRO K N 5158 C CA . PRO C 61 ? 1.2430 0.7301 0.7382 -0.0034 0.0389 -0.0456 87 PRO K CA 5159 C C . PRO C 61 ? 1.2488 0.7417 0.7354 0.0011 0.0319 -0.0414 87 PRO K C 5160 O O . PRO C 61 ? 1.2597 0.7629 0.7473 0.0036 0.0273 -0.0364 87 PRO K O 5161 C CB . PRO C 61 ? 1.2401 0.7372 0.7523 0.0026 0.0381 -0.0449 87 PRO K CB 5162 C CG . PRO C 61 ? 1.2254 0.7194 0.7410 0.0044 0.0413 -0.0507 87 PRO K CG 5163 C CD . PRO C 61 ? 1.2202 0.7003 0.7258 -0.0040 0.0476 -0.0572 87 PRO K CD 5164 N N . GLN C 62 ? 1.2941 0.7811 0.7733 0.0020 0.0306 -0.0442 88 GLN K N 5165 C CA . GLN C 62 ? 1.2989 0.7897 0.7716 0.0068 0.0226 -0.0420 88 GLN K CA 5166 C C . GLN C 62 ? 1.3114 0.8002 0.7750 0.0037 0.0180 -0.0386 88 GLN K C 5167 O O . GLN C 62 ? 1.3177 0.8151 0.7815 0.0091 0.0106 -0.0370 88 GLN K O 5168 C CB . GLN C 62 ? 1.2933 0.7723 0.7571 0.0058 0.0210 -0.0455 88 GLN K CB 5169 C CG . GLN C 62 ? 1.2864 0.7750 0.7577 0.0150 0.0170 -0.0467 88 GLN K CG 5170 C CD . GLN C 62 ? 1.2796 0.7629 0.7543 0.0141 0.0225 -0.0510 88 GLN K CD 5171 O OE1 . GLN C 62 ? 1.2775 0.7575 0.7567 0.0091 0.0303 -0.0534 88 GLN K OE1 5172 N NE2 . GLN C 62 ? 1.2764 0.7593 0.7501 0.0189 0.0181 -0.0528 88 GLN K NE2 5173 N N . LEU C 63 ? 1.1926 0.6707 0.6495 -0.0050 0.0223 -0.0385 89 LEU K N 5174 C CA . LEU C 63 ? 1.2046 0.6794 0.6524 -0.0092 0.0185 -0.0351 89 LEU K CA 5175 C C . LEU C 63 ? 1.2130 0.7057 0.6699 -0.0038 0.0146 -0.0308 89 LEU K C 5176 O O . LEU C 63 ? 1.2234 0.7176 0.6750 -0.0047 0.0092 -0.0284 89 LEU K O 5177 C CB . LEU C 63 ? 1.2055 0.6676 0.6462 -0.0199 0.0252 -0.0365 89 LEU K CB 5178 C CG . LEU C 63 ? 1.2061 0.6490 0.6295 -0.0296 0.0266 -0.0395 89 LEU K CG 5179 C CD1 . LEU C 63 ? 1.2072 0.6407 0.6246 -0.0407 0.0341 -0.0422 89 LEU K CD1 5180 C CD2 . LEU C 63 ? 1.2174 0.6534 0.6274 -0.0298 0.0159 -0.0359 89 LEU K CD2 5181 N N . GLY C 64 ? 1.0451 0.5513 0.5150 0.0009 0.0169 -0.0300 90 GLY K N 5182 C CA . GLY C 64 ? 1.0498 0.5748 0.5270 0.0047 0.0132 -0.0263 90 GLY K CA 5183 C C . GLY C 64 ? 1.0505 0.5865 0.5275 0.0109 0.0059 -0.0275 90 GLY K C 5184 O O . GLY C 64 ? 1.0569 0.6040 0.5347 0.0111 0.0020 -0.0257 90 GLY K O 5185 N N . GLN C 65 ? 1.2906 0.8237 0.7674 0.0158 0.0036 -0.0314 91 GLN K N 5186 C CA . GLN C 65 ? 1.2922 0.8381 0.7730 0.0233 -0.0039 -0.0343 91 GLN K CA 5187 C C . GLN C 65 ? 1.3011 0.8432 0.7763 0.0229 -0.0115 -0.0349 91 GLN K C 5188 O O . GLN C 65 ? 1.3039 0.8586 0.7855 0.0296 -0.0185 -0.0387 91 GLN K O 5189 C CB . GLN C 65 ? 1.2831 0.8249 0.7652 0.0288 -0.0057 -0.0386 91 GLN K CB 5190 C CG . GLN C 65 ? 1.2726 0.8252 0.7639 0.0320 -0.0010 -0.0391 91 GLN K CG 5191 C CD . GLN C 65 ? 1.2649 0.8027 0.7532 0.0319 0.0016 -0.0414 91 GLN K CD 5192 O OE1 . GLN C 65 ? 1.2569 0.7859 0.7448 0.0271 0.0083 -0.0403 91 GLN K OE1 5193 N NE2 . GLN C 65 ? 1.2679 0.8026 0.7547 0.0369 -0.0041 -0.0453 91 GLN K NE2 5194 N N . LEU C 66 ? 1.1137 0.6396 0.5779 0.0152 -0.0107 -0.0319 92 LEU K N 5195 C CA . LEU C 66 ? 1.1243 0.6464 0.5834 0.0145 -0.0193 -0.0319 92 LEU K CA 5196 C C . LEU C 66 ? 1.1310 0.6723 0.5975 0.0143 -0.0184 -0.0299 92 LEU K C 5197 O O . LEU C 66 ? 1.1329 0.6708 0.5956 0.0074 -0.0130 -0.0256 92 LEU K O 5198 C CB . LEU C 66 ? 1.1278 0.6251 0.5704 0.0046 -0.0187 -0.0292 92 LEU K CB 5199 C CG . LEU C 66 ? 1.1228 0.5995 0.5545 0.0013 -0.0189 -0.0308 92 LEU K CG 5200 C CD1 . LEU C 66 ? 1.1212 0.5837 0.5434 -0.0091 -0.0090 -0.0297 92 LEU K CD1 5201 C CD2 . LEU C 66 ? 1.1333 0.5951 0.5544 -0.0001 -0.0310 -0.0307 92 LEU K CD2 5202 N N . LYS C 67 ? 1.0634 0.6256 0.5410 0.0214 -0.0239 -0.0337 93 LYS K N 5203 C CA . LYS C 67 ? 1.0611 0.6459 0.5466 0.0205 -0.0219 -0.0326 93 LYS K CA 5204 C C . LYS C 67 ? 1.0704 0.6520 0.5514 0.0161 -0.0263 -0.0306 93 LYS K C 5205 O O . LYS C 67 ? 1.0709 0.6611 0.5522 0.0107 -0.0226 -0.0267 93 LYS K O 5206 C CB . LYS C 67 ? 1.0555 0.6669 0.5551 0.0283 -0.0245 -0.0391 93 LYS K CB 5207 N N . ASN C 68 ? 1.1432 0.7106 0.6192 0.0176 -0.0351 -0.0328 94 ASN K N 5208 C CA . ASN C 68 ? 1.1551 0.7183 0.6269 0.0137 -0.0410 -0.0311 94 ASN K CA 5209 C C . ASN C 68 ? 1.1601 0.6960 0.6141 0.0039 -0.0395 -0.0252 94 ASN K C 5210 O O . ASN C 68 ? 1.1713 0.7010 0.6198 -0.0002 -0.0451 -0.0233 94 ASN K O 5211 C CB . ASN C 68 ? 1.1631 0.7314 0.6430 0.0213 -0.0539 -0.0376 94 ASN K CB 5212 C CG . ASN C 68 ? 1.1619 0.7619 0.6609 0.0295 -0.0544 -0.0452 94 ASN K CG 5213 O OD1 . ASN C 68 ? 1.1645 0.7864 0.6716 0.0282 -0.0524 -0.0464 94 ASN K OD1 5214 N ND2 . ASN C 68 ? 1.1592 0.7627 0.6652 0.0372 -0.0566 -0.0510 94 ASN K ND2 5215 N N . LEU C 69 ? 1.1427 0.6636 0.5885 -0.0003 -0.0318 -0.0231 95 LEU K N 5216 C CA . LEU C 69 ? 1.1472 0.6441 0.5766 -0.0106 -0.0282 -0.0195 95 LEU K CA 5217 C C . LEU C 69 ? 1.1522 0.6517 0.5793 -0.0172 -0.0248 -0.0155 95 LEU K C 5218 O O . LEU C 69 ? 1.1476 0.6613 0.5830 -0.0171 -0.0184 -0.0140 95 LEU K O 5219 C CB . LEU C 69 ? 1.1371 0.6254 0.5638 -0.0134 -0.0182 -0.0199 95 LEU K CB 5220 C CG . LEU C 69 ? 1.1410 0.6058 0.5511 -0.0248 -0.0141 -0.0186 95 LEU K CG 5221 C CD1 . LEU C 69 ? 1.1508 0.5973 0.5468 -0.0279 -0.0237 -0.0188 95 LEU K CD1 5222 C CD2 . LEU C 69 ? 1.1307 0.5903 0.5416 -0.0274 -0.0036 -0.0210 95 LEU K CD2 5223 N N . GLN C 70 ? 1.1703 0.6546 0.5850 -0.0239 -0.0299 -0.0135 96 GLN K N 5224 C CA . GLN C 70 ? 1.1759 0.6616 0.5876 -0.0304 -0.0280 -0.0099 96 GLN K CA 5225 C C . GLN C 70 ? 1.1754 0.6401 0.5724 -0.0415 -0.0207 -0.0083 96 GLN K C 5226 O O . GLN C 70 ? 1.1724 0.6400 0.5721 -0.0452 -0.0123 -0.0071 96 GLN K O 5227 C CB . GLN C 70 ? 1.1879 0.6735 0.5976 -0.0300 -0.0398 -0.0094 96 GLN K CB 5228 C CG . GLN C 70 ? 1.1909 0.7025 0.6184 -0.0202 -0.0459 -0.0127 96 GLN K CG 5229 C CD . GLN C 70 ? 1.2034 0.7137 0.6309 -0.0193 -0.0589 -0.0136 96 GLN K CD 5230 O OE1 . GLN C 70 ? 1.2095 0.6968 0.6218 -0.0260 -0.0647 -0.0108 96 GLN K OE1 5231 N NE2 . GLN C 70 ? 1.2079 0.7432 0.6525 -0.0119 -0.0639 -0.0180 96 GLN K NE2 5232 N N . TYR C 71 ? 1.2739 0.7172 0.6550 -0.0476 -0.0247 -0.0086 97 TYR K N 5233 C CA . TYR C 71 ? 1.2717 0.6958 0.6373 -0.0599 -0.0173 -0.0087 97 TYR K CA 5234 C C . TYR C 71 ? 1.2620 0.6762 0.6232 -0.0618 -0.0114 -0.0125 97 TYR K C 5235 O O . TYR C 71 ? 1.2622 0.6679 0.6171 -0.0606 -0.0181 -0.0131 97 TYR K O 5236 C CB . TYR C 71 ? 1.2834 0.6895 0.6305 -0.0695 -0.0253 -0.0060 97 TYR K CB 5237 C CG . TYR C 71 ? 1.2919 0.7074 0.6433 -0.0683 -0.0314 -0.0026 97 TYR K CG 5238 C CD1 . TYR C 71 ? 1.2984 0.7278 0.6614 -0.0584 -0.0424 -0.0022 97 TYR K CD1 5239 C CD2 . TYR C 71 ? 1.2938 0.7053 0.6390 -0.0770 -0.0261 -0.0007 97 TYR K CD2 5240 C CE1 . TYR C 71 ? 1.3064 0.7465 0.6749 -0.0576 -0.0476 -0.0001 97 TYR K CE1 5241 C CE2 . TYR C 71 ? 1.3016 0.7222 0.6509 -0.0763 -0.0317 0.0025 97 TYR K CE2 5242 C CZ . TYR C 71 ? 1.3079 0.7432 0.6689 -0.0666 -0.0423 0.0028 97 TYR K CZ 5243 O OH . TYR C 71 ? 1.3155 0.7622 0.6822 -0.0660 -0.0478 0.0050 97 TYR K OH 5244 N N . LEU C 72 ? 1.1354 0.5512 0.5014 -0.0646 0.0007 -0.0155 98 LEU K N 5245 C CA . LEU C 72 ? 1.1321 0.5395 0.4951 -0.0680 0.0082 -0.0205 98 LEU K CA 5246 C C . LEU C 72 ? 1.1399 0.5329 0.4900 -0.0820 0.0168 -0.0241 98 LEU K C 5247 O O . LEU C 72 ? 1.1350 0.5327 0.4934 -0.0838 0.0248 -0.0266 98 LEU K O 5248 C CB . LEU C 72 ? 1.1160 0.5390 0.4988 -0.0591 0.0149 -0.0229 98 LEU K CB 5249 C CG . LEU C 72 ? 1.1102 0.5280 0.4945 -0.0609 0.0230 -0.0290 98 LEU K CG 5250 C CD1 . LEU C 72 ? 1.1066 0.5259 0.4917 -0.0539 0.0173 -0.0289 98 LEU K CD1 5251 C CD2 . LEU C 72 ? 1.0985 0.5273 0.5009 -0.0567 0.0307 -0.0316 98 LEU K CD2 5252 N N . GLU C 73 ? 1.2609 0.6359 0.5906 -0.0929 0.0149 -0.0251 99 GLU K N 5253 C CA . GLU C 73 ? 1.2619 0.6243 0.5775 -0.1081 0.0235 -0.0296 99 GLU K CA 5254 C C . GLU C 73 ? 1.2550 0.6107 0.5654 -0.1150 0.0320 -0.0368 99 GLU K C 5255 O O . GLU C 73 ? 1.2622 0.6057 0.5566 -0.1210 0.0270 -0.0357 99 GLU K O 5256 C CB . GLU C 73 ? 1.2781 0.6242 0.5704 -0.1190 0.0146 -0.0248 99 GLU K CB 5257 C CG . GLU C 73 ? 1.2871 0.6399 0.5846 -0.1115 0.0038 -0.0177 99 GLU K CG 5258 C CD . GLU C 73 ? 1.2821 0.6478 0.5939 -0.1085 0.0107 -0.0184 99 GLU K CD 5259 O OE1 . GLU C 73 ? 1.2803 0.6400 0.5865 -0.1187 0.0201 -0.0229 99 GLU K OE1 5260 O OE2 . GLU C 73 ? 1.2810 0.6629 0.6094 -0.0966 0.0067 -0.0149 99 GLU K OE2 5261 N N . LEU C 74 ? 1.2154 0.5795 0.5406 -0.1142 0.0442 -0.0445 100 LEU K N 5262 C CA . LEU C 74 ? 1.2090 0.5688 0.5315 -0.1224 0.0546 -0.0540 100 LEU K CA 5263 C C . LEU C 74 ? 1.2102 0.5640 0.5249 -0.1380 0.0664 -0.0636 100 LEU K C 5264 O O . LEU C 74 ? 1.2031 0.5574 0.5201 -0.1445 0.0768 -0.0738 100 LEU K O 5265 C CB . LEU C 74 ? 1.1935 0.5671 0.5396 -0.1100 0.0589 -0.0578 100 LEU K CB 5266 C CG . LEU C 74 ? 1.1929 0.5715 0.5436 -0.0975 0.0491 -0.0511 100 LEU K CG 5267 C CD1 . LEU C 74 ? 1.1844 0.5713 0.5512 -0.0915 0.0558 -0.0573 100 LEU K CD1 5268 C CD2 . LEU C 74 ? 1.2031 0.5674 0.5318 -0.1035 0.0401 -0.0466 100 LEU K CD2 5269 N N . TYR C 75 ? 1.1988 0.5485 0.5060 -0.1439 0.0653 -0.0615 101 TYR K N 5270 C CA . TYR C 75 ? 1.1995 0.5467 0.5042 -0.1567 0.0769 -0.0718 101 TYR K CA 5271 C C . TYR C 75 ? 1.2100 0.5457 0.4923 -0.1764 0.0848 -0.0801 101 TYR K C 5272 O O . TYR C 75 ? 1.2219 0.5457 0.4820 -0.1840 0.0783 -0.0748 101 TYR K O 5273 C CB . TYR C 75 ? 1.2082 0.5523 0.5073 -0.1594 0.0729 -0.0669 101 TYR K CB 5274 C CG . TYR C 75 ? 1.2252 0.5552 0.4976 -0.1675 0.0619 -0.0572 101 TYR K CG 5275 C CD1 . TYR C 75 ? 1.2290 0.5600 0.5019 -0.1564 0.0481 -0.0459 101 TYR K CD1 5276 C CD2 . TYR C 75 ? 1.2394 0.5554 0.4868 -0.1865 0.0647 -0.0600 101 TYR K CD2 5277 C CE1 . TYR C 75 ? 1.2450 0.5627 0.4964 -0.1627 0.0362 -0.0376 101 TYR K CE1 5278 C CE2 . TYR C 75 ? 1.2566 0.5579 0.4795 -0.1942 0.0525 -0.0503 101 TYR K CE2 5279 C CZ . TYR C 75 ? 1.2584 0.5604 0.4845 -0.1815 0.0376 -0.0391 101 TYR K CZ 5280 O OH . TYR C 75 ? 1.2754 0.5627 0.4805 -0.1873 0.0233 -0.0298 101 TYR K OH 5281 N N . SER C 76 ? 1.2087 0.5482 0.4974 -0.1852 0.0984 -0.0939 102 SER K N 5282 C CA . SER C 76 ? 1.2145 0.5465 0.4833 -0.2062 0.1086 -0.1047 102 SER K CA 5283 C C . SER C 76 ? 1.2136 0.5443 0.4769 -0.2087 0.1098 -0.1064 102 SER K C 5284 O O . SER C 76 ? 1.2282 0.5449 0.4643 -0.2194 0.1031 -0.0996 102 SER K O 5285 C CB . SER C 76 ? 1.2328 0.5483 0.4685 -0.2233 0.1034 -0.0987 102 SER K CB 5286 O OG . SER C 76 ? 1.2422 0.5576 0.4721 -0.2391 0.1157 -0.1114 102 SER K OG 5287 N N . ASN C 77 ? 1.2325 0.5769 0.5223 -0.1983 0.1169 -0.1151 103 ASN K N 5288 C CA . ASN C 77 ? 1.2281 0.5737 0.5171 -0.1996 0.1196 -0.1185 103 ASN K CA 5289 C C . ASN C 77 ? 1.2117 0.5730 0.5291 -0.1962 0.1333 -0.1354 103 ASN K C 5290 O O . ASN C 77 ? 1.2049 0.5748 0.5427 -0.1919 0.1390 -0.1436 103 ASN K O 5291 C CB . ASN C 77 ? 1.2265 0.5717 0.5200 -0.1828 0.1058 -0.1044 103 ASN K CB 5292 C CG . ASN C 77 ? 1.2451 0.5732 0.5091 -0.1891 0.0922 -0.0907 103 ASN K CG 5293 O OD1 . ASN C 77 ? 1.2531 0.5704 0.4969 -0.1996 0.0898 -0.0894 103 ASN K OD1 5294 N ND2 . ASN C 77 ? 1.2533 0.5782 0.5148 -0.1830 0.0823 -0.0807 103 ASN K ND2 5295 N N . ASN C 78 ? 1.5616 0.9262 0.8810 -0.1983 0.1378 -0.1411 104 ASN K N 5296 C CA . ASN C 78 ? 1.5457 0.9257 0.8937 -0.1946 0.1499 -0.1578 104 ASN K CA 5297 C C . ASN C 78 ? 1.5329 0.9228 0.9096 -0.1720 0.1435 -0.1528 104 ASN K C 5298 O O . ASN C 78 ? 1.5203 0.9219 0.9211 -0.1672 0.1508 -0.1648 104 ASN K O 5299 C CB . ASN C 78 ? 1.5468 0.9275 0.8827 -0.2126 0.1612 -0.1705 104 ASN K CB 5300 C CG . ASN C 78 ? 1.5346 0.9313 0.8965 -0.2163 0.1771 -0.1934 104 ASN K CG 5301 O OD1 . ASN C 78 ? 1.5239 0.9289 0.9118 -0.2061 0.1787 -0.1996 104 ASN K OD1 5302 N ND2 . ASN C 78 ? 1.5379 0.9391 0.8935 -0.2314 0.1883 -0.2067 104 ASN K ND2 5303 N N . ILE C 79 ? 1.2075 0.5928 0.5805 -0.1592 0.1297 -0.1356 105 ILE K N 5304 C CA . ILE C 79 ? 1.1972 0.5916 0.5939 -0.1388 0.1225 -0.1291 105 ILE K CA 5305 C C . ILE C 79 ? 1.1849 0.5918 0.6149 -0.1295 0.1277 -0.1391 105 ILE K C 5306 O O . ILE C 79 ? 1.1874 0.5947 0.6237 -0.1309 0.1295 -0.1424 105 ILE K O 5307 C CB . ILE C 79 ? 1.2043 0.5948 0.5941 -0.1276 0.1080 -0.1112 105 ILE K CB 5308 C CG1 . ILE C 79 ? 1.2161 0.5937 0.5770 -0.1346 0.1004 -0.1018 105 ILE K CG1 5309 C CG2 . ILE C 79 ? 1.1940 0.5957 0.6080 -0.1083 0.1018 -0.1058 105 ILE K CG2 5310 C CD1 . ILE C 79 ? 1.2219 0.5981 0.5797 -0.1226 0.0861 -0.0868 105 ILE K CD1 5311 N N . THR C 80 ? 1.2187 0.6347 0.6702 -0.1203 0.1292 -0.1442 106 THR K N 5312 C CA . THR C 80 ? 1.2087 0.6350 0.6931 -0.1109 0.1316 -0.1533 106 THR K CA 5313 C C . THR C 80 ? 1.2029 0.6347 0.7029 -0.0933 0.1213 -0.1425 106 THR K C 5314 O O . THR C 80 ? 1.2067 0.6352 0.6921 -0.0883 0.1128 -0.1283 106 THR K O 5315 C CB . THR C 80 ? 1.1990 0.6329 0.6988 -0.1182 0.1444 -0.1736 106 THR K CB 5316 O OG1 . THR C 80 ? 1.1889 0.6321 0.7244 -0.1063 0.1435 -0.1816 106 THR K OG1 5317 C CG2 . THR C 80 ? 1.1957 0.6308 0.6881 -0.1204 0.1465 -0.1742 106 THR K CG2 5318 N N . GLY C 81 ? 1.0547 0.4948 0.5850 -0.0840 0.1213 -0.1495 107 GLY K N 5319 C CA . GLY C 81 ? 1.0443 0.4896 0.5891 -0.0689 0.1116 -0.1400 107 GLY K CA 5320 C C . GLY C 81 ? 1.0437 0.4891 0.5967 -0.0607 0.1022 -0.1300 107 GLY K C 5321 O O . GLY C 81 ? 1.0491 0.4916 0.6054 -0.0649 0.1039 -0.1342 107 GLY K O 5322 N N . PRO C 82 ? 1.1147 0.5640 0.6727 -0.0494 0.0924 -0.1180 108 PRO K N 5323 C CA . PRO C 82 ? 1.1236 0.5734 0.6858 -0.0432 0.0827 -0.1067 108 PRO K CA 5324 C C . PRO C 82 ? 1.1341 0.5820 0.6724 -0.0439 0.0773 -0.0926 108 PRO K C 5325 O O . PRO C 82 ? 1.1338 0.5789 0.6527 -0.0480 0.0793 -0.0906 108 PRO K O 5326 C CB . PRO C 82 ? 1.1207 0.5772 0.7024 -0.0319 0.0753 -0.1028 108 PRO K CB 5327 C CG . PRO C 82 ? 1.1110 0.5705 0.6883 -0.0309 0.0789 -0.1055 108 PRO K CG 5328 C CD . PRO C 82 ? 1.1062 0.5612 0.6738 -0.0419 0.0905 -0.1178 108 PRO K CD 5329 N N . VAL C 83 ? 1.1116 0.5613 0.6530 -0.0400 0.0695 -0.0832 109 VAL K N 5330 C CA . VAL C 83 ? 1.1230 0.5740 0.6469 -0.0395 0.0632 -0.0703 109 VAL K CA 5331 C C . VAL C 83 ? 1.1282 0.5890 0.6580 -0.0299 0.0546 -0.0601 109 VAL K C 5332 O O . VAL C 83 ? 1.1334 0.5978 0.6780 -0.0258 0.0491 -0.0568 109 VAL K O 5333 C CB . VAL C 83 ? 1.1322 0.5799 0.6547 -0.0434 0.0608 -0.0670 109 VAL K CB 5334 C CG1 . VAL C 83 ? 1.1315 0.5753 0.6307 -0.0494 0.0606 -0.0617 109 VAL K CG1 5335 C CG2 . VAL C 83 ? 1.1323 0.5740 0.6685 -0.0482 0.0669 -0.0796 109 VAL K CG2 5336 N N . PRO C 84 ? 1.0455 0.5104 0.5636 -0.0270 0.0528 -0.0555 110 PRO K N 5337 C CA . PRO C 84 ? 1.0421 0.5180 0.5648 -0.0186 0.0459 -0.0479 110 PRO K CA 5338 C C . PRO C 84 ? 1.0479 0.5322 0.5706 -0.0166 0.0382 -0.0375 110 PRO K C 5339 O O . PRO C 84 ? 1.0531 0.5387 0.5632 -0.0191 0.0364 -0.0329 110 PRO K O 5340 C CB . PRO C 84 ? 1.0411 0.5176 0.5487 -0.0177 0.0459 -0.0469 110 PRO K CB 5341 C CG . PRO C 84 ? 1.0416 0.5067 0.5425 -0.0248 0.0536 -0.0560 110 PRO K CG 5342 C CD . PRO C 84 ? 1.0468 0.5052 0.5486 -0.0321 0.0575 -0.0596 110 PRO K CD 5343 N N . SER C 85 ? 1.2473 0.7379 0.7831 -0.0126 0.0331 -0.0337 111 SER K N 5344 C CA . SER C 85 ? 1.2678 0.7669 0.8021 -0.0128 0.0259 -0.0237 111 SER K CA 5345 C C . SER C 85 ? 1.2752 0.7864 0.7973 -0.0105 0.0235 -0.0186 111 SER K C 5346 O O . SER C 85 ? 1.2926 0.8120 0.8096 -0.0126 0.0195 -0.0120 111 SER K O 5347 C CB . SER C 85 ? 1.2756 0.7786 0.8239 -0.0100 0.0197 -0.0199 111 SER K CB 5348 O OG . SER C 85 ? 1.2749 0.7921 0.8185 -0.0073 0.0150 -0.0129 111 SER K OG 5349 N N . ASP C 86 ? 1.3484 0.8611 0.8670 -0.0065 0.0259 -0.0225 112 ASP K N 5350 C CA . ASP C 86 ? 1.3511 0.8746 0.8607 -0.0034 0.0231 -0.0199 112 ASP K CA 5351 C C . ASP C 86 ? 1.3548 0.8752 0.8522 -0.0072 0.0227 -0.0191 112 ASP K C 5352 O O . ASP C 86 ? 1.3580 0.8874 0.8497 -0.0045 0.0192 -0.0179 112 ASP K O 5353 C CB . ASP C 86 ? 1.3335 0.8567 0.8425 0.0017 0.0246 -0.0248 112 ASP K CB 5354 C CG . ASP C 86 ? 1.3333 0.8656 0.8527 0.0066 0.0226 -0.0239 112 ASP K CG 5355 O OD1 . ASP C 86 ? 1.3447 0.8853 0.8696 0.0058 0.0188 -0.0183 112 ASP K OD1 5356 O OD2 . ASP C 86 ? 1.3221 0.8525 0.8431 0.0105 0.0244 -0.0283 112 ASP K OD2 5357 N N . LEU C 87 ? 1.0556 0.5632 0.5496 -0.0134 0.0261 -0.0209 113 LEU K N 5358 C CA . LEU C 87 ? 1.0615 0.5656 0.5438 -0.0180 0.0249 -0.0191 113 LEU K CA 5359 C C . LEU C 87 ? 1.0693 0.5862 0.5530 -0.0187 0.0200 -0.0122 113 LEU K C 5360 O O . LEU C 87 ? 1.0739 0.5948 0.5499 -0.0202 0.0171 -0.0100 113 LEU K O 5361 C CB . LEU C 87 ? 1.0645 0.5524 0.5423 -0.0255 0.0302 -0.0233 113 LEU K CB 5362 C CG . LEU C 87 ? 1.0647 0.5394 0.5305 -0.0295 0.0340 -0.0291 113 LEU K CG 5363 C CD1 . LEU C 87 ? 1.0586 0.5364 0.5232 -0.0238 0.0322 -0.0305 113 LEU K CD1 5364 C CD2 . LEU C 87 ? 1.0638 0.5268 0.5329 -0.0354 0.0419 -0.0368 113 LEU K CD2 5365 N N . GLY C 88 ? 1.1842 0.7075 0.6777 -0.0184 0.0184 -0.0086 114 GLY K N 5366 C CA . GLY C 88 ? 1.2021 0.7403 0.6963 -0.0199 0.0134 -0.0016 114 GLY K CA 5367 C C . GLY C 88 ? 1.1991 0.7549 0.6910 -0.0153 0.0107 -0.0015 114 GLY K C 5368 O O . GLY C 88 ? 1.2030 0.7729 0.6926 -0.0173 0.0076 0.0018 114 GLY K O 5369 N N . ASN C 89 ? 1.4415 0.9973 0.9349 -0.0092 0.0120 -0.0062 115 ASN K N 5370 C CA . ASN C 89 ? 1.4364 1.0086 0.9297 -0.0040 0.0091 -0.0081 115 ASN K CA 5371 C C . ASN C 89 ? 1.4333 1.0054 0.9196 -0.0034 0.0066 -0.0105 115 ASN K C 5372 O O . ASN C 89 ? 1.4301 1.0157 0.9181 0.0015 0.0031 -0.0136 115 ASN K O 5373 C CB . ASN C 89 ? 1.4260 0.9982 0.9236 0.0025 0.0101 -0.0124 115 ASN K CB 5374 C CG . ASN C 89 ? 1.4319 1.0142 0.9373 0.0030 0.0095 -0.0094 115 ASN K CG 5375 O OD1 . ASN C 89 ? 1.4433 1.0306 0.9502 -0.0022 0.0078 -0.0036 115 ASN K OD1 5376 N ND2 . ASN C 89 ? 1.4256 1.0098 0.9351 0.0085 0.0100 -0.0128 115 ASN K ND2 5377 N N . LEU C 90 ? 1.2067 0.7636 0.6858 -0.0085 0.0076 -0.0098 116 LEU K N 5378 C CA . LEU C 90 ? 1.2066 0.7615 0.6784 -0.0088 0.0037 -0.0112 116 LEU K CA 5379 C C . LEU C 90 ? 1.2163 0.7811 0.6875 -0.0135 0.0015 -0.0072 116 LEU K C 5380 O O . LEU C 90 ? 1.2221 0.7760 0.6887 -0.0200 0.0036 -0.0041 116 LEU K O 5381 C CB . LEU C 90 ? 1.2037 0.7350 0.6653 -0.0133 0.0059 -0.0129 116 LEU K CB 5382 C CG . LEU C 90 ? 1.1911 0.7079 0.6503 -0.0124 0.0096 -0.0171 116 LEU K CG 5383 C CD1 . LEU C 90 ? 1.1881 0.6861 0.6402 -0.0206 0.0153 -0.0182 116 LEU K CD1 5384 C CD2 . LEU C 90 ? 1.1887 0.7013 0.6419 -0.0086 0.0041 -0.0202 116 LEU K CD2 5385 N N . THR C 91 ? 1.4004 0.9861 0.8764 -0.0104 -0.0026 -0.0082 117 THR K N 5386 C CA . THR C 91 ? 1.4087 1.0082 0.8854 -0.0155 -0.0042 -0.0046 117 THR K CA 5387 C C . THR C 91 ? 1.4140 1.0068 0.8846 -0.0181 -0.0079 -0.0049 117 THR K C 5388 O O . THR C 91 ? 1.4202 1.0096 0.8868 -0.0251 -0.0072 -0.0004 117 THR K O 5389 C CB . THR C 91 ? 1.4102 1.0384 0.8955 -0.0128 -0.0061 -0.0070 117 THR K CB 5390 O OG1 . THR C 91 ? 1.4111 1.0471 0.9005 -0.0057 -0.0108 -0.0144 117 THR K OG1 5391 C CG2 . THR C 91 ? 1.4040 1.0381 0.8938 -0.0110 -0.0032 -0.0065 117 THR K CG2 5392 N N . ASN C 92 ? 1.1635 0.7525 0.6332 -0.0128 -0.0127 -0.0099 118 ASN K N 5393 C CA . ASN C 92 ? 1.1716 0.7556 0.6366 -0.0145 -0.0186 -0.0105 118 ASN K CA 5394 C C . ASN C 92 ? 1.1720 0.7280 0.6233 -0.0207 -0.0172 -0.0077 118 ASN K C 5395 O O . ASN C 92 ? 1.1800 0.7263 0.6243 -0.0231 -0.0228 -0.0077 118 ASN K O 5396 C CB . ASN C 92 ? 1.1729 0.7633 0.6436 -0.0063 -0.0268 -0.0173 118 ASN K CB 5397 C CG . ASN C 92 ? 1.1750 0.7966 0.6605 -0.0009 -0.0284 -0.0224 118 ASN K CG 5398 O OD1 . ASN C 92 ? 1.1835 0.8222 0.6745 -0.0028 -0.0309 -0.0236 118 ASN K OD1 5399 N ND2 . ASN C 92 ? 1.1676 0.7976 0.6598 0.0052 -0.0268 -0.0265 118 ASN K ND2 5400 N N . LEU C 93 ? 1.1012 0.6446 0.5492 -0.0237 -0.0101 -0.0061 119 LEU K N 5401 C CA . LEU C 93 ? 1.1061 0.6253 0.5419 -0.0307 -0.0071 -0.0053 119 LEU K CA 5402 C C . LEU C 93 ? 1.1140 0.6313 0.5454 -0.0383 -0.0066 -0.0013 119 LEU K C 5403 O O . LEU C 93 ? 1.1143 0.6402 0.5516 -0.0406 -0.0033 0.0019 119 LEU K O 5404 C CB . LEU C 93 ? 1.1004 0.6107 0.5378 -0.0318 0.0010 -0.0065 119 LEU K CB 5405 C CG . LEU C 93 ? 1.1018 0.5899 0.5289 -0.0399 0.0064 -0.0081 119 LEU K CG 5406 C CD1 . LEU C 93 ? 1.1032 0.5766 0.5202 -0.0406 0.0054 -0.0118 119 LEU K CD1 5407 C CD2 . LEU C 93 ? 1.0982 0.5845 0.5333 -0.0411 0.0138 -0.0092 119 LEU K CD2 5408 N N . VAL C 94 ? 1.1290 0.6342 0.5496 -0.0425 -0.0112 -0.0011 120 VAL K N 5409 C CA . VAL C 94 ? 1.1374 0.6359 0.5508 -0.0508 -0.0110 0.0022 120 VAL K CA 5410 C C . VAL C 94 ? 1.1397 0.6170 0.5428 -0.0593 -0.0040 0.0014 120 VAL K C 5411 O O . VAL C 94 ? 1.1430 0.6183 0.5457 -0.0650 -0.0006 0.0035 120 VAL K O 5412 C CB . VAL C 94 ? 1.1455 0.6437 0.5535 -0.0515 -0.0206 0.0028 120 VAL K CB 5413 C CG1 . VAL C 94 ? 1.1514 0.6455 0.5580 -0.0457 -0.0278 -0.0006 120 VAL K CG1 5414 C CG2 . VAL C 94 ? 1.1516 0.6308 0.5448 -0.0617 -0.0203 0.0049 120 VAL K CG2 5415 N N . SER C 95 ? 1.2932 0.7555 0.6885 -0.0607 -0.0017 -0.0023 121 SER K N 5416 C CA . SER C 95 ? 1.2889 0.7329 0.6746 -0.0701 0.0059 -0.0052 121 SER K CA 5417 C C . SER C 95 ? 1.2763 0.7148 0.6647 -0.0689 0.0128 -0.0105 121 SER K C 5418 O O . SER C 95 ? 1.2731 0.7099 0.6591 -0.0651 0.0100 -0.0120 121 SER K O 5419 C CB . SER C 95 ? 1.2949 0.7216 0.6615 -0.0791 0.0018 -0.0049 121 SER K CB 5420 O OG . SER C 95 ? 1.2900 0.7002 0.6459 -0.0892 0.0100 -0.0095 121 SER K OG 5421 N N . LEU C 96 ? 1.2736 0.7098 0.6686 -0.0717 0.0212 -0.0139 122 LEU K N 5422 C CA . LEU C 96 ? 1.2614 0.6920 0.6599 -0.0718 0.0285 -0.0206 122 LEU K CA 5423 C C . LEU C 96 ? 1.2572 0.6735 0.6483 -0.0829 0.0367 -0.0273 122 LEU K C 5424 O O . LEU C 96 ? 1.2564 0.6733 0.6561 -0.0850 0.0409 -0.0295 122 LEU K O 5425 C CB . LEU C 96 ? 1.2570 0.7005 0.6751 -0.0635 0.0305 -0.0206 122 LEU K CB 5426 C CG . LEU C 96 ? 1.2441 0.6845 0.6727 -0.0628 0.0381 -0.0279 122 LEU K CG 5427 C CD1 . LEU C 96 ? 1.2336 0.6697 0.6572 -0.0618 0.0402 -0.0322 122 LEU K CD1 5428 C CD2 . LEU C 96 ? 1.2453 0.6983 0.6920 -0.0549 0.0362 -0.0250 122 LEU K CD2 5429 N N . ASP C 97 ? 1.2827 0.6862 0.6579 -0.0906 0.0388 -0.0312 123 ASP K N 5430 C CA . ASP C 97 ? 1.2802 0.6715 0.6467 -0.1031 0.0478 -0.0394 123 ASP K CA 5431 C C . ASP C 97 ? 1.2695 0.6582 0.6385 -0.1050 0.0557 -0.0482 123 ASP K C 5432 O O . ASP C 97 ? 1.2701 0.6522 0.6262 -0.1079 0.0536 -0.0478 123 ASP K O 5433 C CB . ASP C 97 ? 1.2911 0.6682 0.6328 -0.1148 0.0441 -0.0371 123 ASP K CB 5434 C CG . ASP C 97 ? 1.3021 0.6812 0.6406 -0.1140 0.0361 -0.0291 123 ASP K CG 5435 O OD1 . ASP C 97 ? 1.3055 0.6937 0.6492 -0.1045 0.0268 -0.0219 123 ASP K OD1 5436 O OD2 . ASP C 97 ? 1.3080 0.6800 0.6386 -0.1235 0.0392 -0.0310 123 ASP K OD2 5437 N N . LEU C 98 ? 1.1443 0.5382 0.5312 -0.1030 0.0636 -0.0560 124 LEU K N 5438 C CA . LEU C 98 ? 1.1354 0.5286 0.5283 -0.1055 0.0725 -0.0667 124 LEU K CA 5439 C C . LEU C 98 ? 1.1364 0.5230 0.5259 -0.1185 0.0834 -0.0792 124 LEU K C 5440 O O . LEU C 98 ? 1.1285 0.5167 0.5263 -0.1213 0.0921 -0.0905 124 LEU K O 5441 C CB . LEU C 98 ? 1.1245 0.5297 0.5432 -0.0929 0.0728 -0.0681 124 LEU K CB 5442 C CG . LEU C 98 ? 1.1221 0.5351 0.5432 -0.0814 0.0640 -0.0583 124 LEU K CG 5443 C CD1 . LEU C 98 ? 1.1137 0.5379 0.5583 -0.0707 0.0629 -0.0580 124 LEU K CD1 5444 C CD2 . LEU C 98 ? 1.1191 0.5273 0.5293 -0.0838 0.0652 -0.0606 124 LEU K CD2 5445 N N . TYR C 99 ? 1.2039 0.5846 0.5834 -0.1263 0.0831 -0.0781 125 TYR K N 5446 C CA . TYR C 99 ? 1.2027 0.5799 0.5841 -0.1371 0.0934 -0.0911 125 TYR K CA 5447 C C . TYR C 99 ? 1.2029 0.5732 0.5679 -0.1527 0.1032 -0.1021 125 TYR K C 5448 O O . TYR C 99 ? 1.2093 0.5723 0.5531 -0.1585 0.1001 -0.0969 125 TYR K O 5449 C CB . TYR C 99 ? 1.2123 0.5848 0.5861 -0.1419 0.0902 -0.0868 125 TYR K CB 5450 C CG . TYR C 99 ? 1.2248 0.5870 0.5700 -0.1506 0.0840 -0.0777 125 TYR K CG 5451 C CD1 . TYR C 99 ? 1.2313 0.5951 0.5718 -0.1420 0.0719 -0.0637 125 TYR K CD1 5452 C CD2 . TYR C 99 ? 1.2309 0.5820 0.5544 -0.1679 0.0895 -0.0836 125 TYR K CD2 5453 C CE1 . TYR C 99 ? 1.2432 0.5971 0.5602 -0.1491 0.0644 -0.0558 125 TYR K CE1 5454 C CE2 . TYR C 99 ? 1.2438 0.5837 0.5409 -0.1762 0.0818 -0.0745 125 TYR K CE2 5455 C CZ . TYR C 99 ? 1.2497 0.5906 0.5447 -0.1661 0.0687 -0.0606 125 TYR K CZ 5456 O OH . TYR C 99 ? 1.2629 0.5924 0.5344 -0.1734 0.0592 -0.0519 125 TYR K OH 5457 N N . LEU C 100 ? 1.2111 0.5837 0.5863 -0.1600 0.1146 -0.1179 126 LEU K N 5458 C CA . LEU C 100 ? 1.2096 0.5797 0.5739 -0.1755 0.1264 -0.1319 126 LEU K CA 5459 C C . LEU C 100 ? 1.2020 0.5765 0.5710 -0.1714 0.1280 -0.1337 126 LEU K C 5460 O O . LEU C 100 ? 1.2093 0.5761 0.5548 -0.1793 0.1259 -0.1285 126 LEU K O 5461 C CB . LEU C 100 ? 1.2248 0.5815 0.5533 -0.1938 0.1262 -0.1283 126 LEU K CB 5462 C CG . LEU C 100 ? 1.2321 0.5845 0.5536 -0.2041 0.1297 -0.1330 126 LEU K CG 5463 C CD1 . LEU C 100 ? 1.2501 0.5878 0.5343 -0.2213 0.1265 -0.1263 126 LEU K CD1 5464 C CD2 . LEU C 100 ? 1.2246 0.5847 0.5621 -0.2119 0.1448 -0.1548 126 LEU K CD2 5465 N N . ASN C 101 ? 1.1765 0.5624 0.5759 -0.1590 0.1304 -0.1405 127 ASN K N 5466 C CA . ASN C 101 ? 1.1677 0.5593 0.5756 -0.1554 0.1337 -0.1452 127 ASN K CA 5467 C C . ASN C 101 ? 1.1537 0.5572 0.5952 -0.1494 0.1415 -0.1615 127 ASN K C 5468 O O . ASN C 101 ? 1.1513 0.5576 0.6076 -0.1508 0.1457 -0.1717 127 ASN K O 5469 C CB . ASN C 101 ? 1.1680 0.5601 0.5758 -0.1411 0.1216 -0.1290 127 ASN K CB 5470 C CG . ASN C 101 ? 1.1813 0.5621 0.5576 -0.1482 0.1148 -0.1171 127 ASN K CG 5471 O OD1 . ASN C 101 ? 1.1818 0.5590 0.5461 -0.1533 0.1158 -0.1176 127 ASN K OD1 5472 N ND2 . ASN C 101 ? 1.1934 0.5676 0.5565 -0.1487 0.1068 -0.1063 127 ASN K ND2 5473 N N . SER C 102 ? 1.3660 0.7760 0.8195 -0.1436 0.1431 -0.1651 128 SER K N 5474 C CA . SER C 102 ? 1.3530 0.7745 0.8413 -0.1356 0.1480 -0.1795 128 SER K CA 5475 C C . SER C 102 ? 1.3470 0.7739 0.8607 -0.1155 0.1371 -0.1706 128 SER K C 5476 O O . SER C 102 ? 1.3366 0.7718 0.8781 -0.1086 0.1393 -0.1812 128 SER K O 5477 C CB . SER C 102 ? 1.3457 0.7731 0.8354 -0.1459 0.1603 -0.1960 128 SER K CB 5478 O OG . SER C 102 ? 1.3492 0.7762 0.8286 -0.1640 0.1724 -0.2111 128 SER K OG 5479 N N . PHE C 103 ? 1.1216 0.5443 0.6255 -0.1073 0.1253 -0.1517 129 PHE K N 5480 C CA . PHE C 103 ? 1.1176 0.5453 0.6403 -0.0907 0.1146 -0.1415 129 PHE K CA 5481 C C . PHE C 103 ? 1.1121 0.5448 0.6679 -0.0829 0.1132 -0.1503 129 PHE K C 5482 O O . PHE C 103 ? 1.1159 0.5465 0.6792 -0.0870 0.1155 -0.1580 129 PHE K O 5483 C CB . PHE C 103 ? 1.1286 0.5524 0.6379 -0.0864 0.1040 -0.1237 129 PHE K CB 5484 C CG . PHE C 103 ? 1.1325 0.5530 0.6167 -0.0876 0.0998 -0.1117 129 PHE K CG 5485 C CD1 . PHE C 103 ? 1.1453 0.5570 0.6032 -0.1002 0.1030 -0.1113 129 PHE K CD1 5486 C CD2 . PHE C 103 ? 1.1244 0.5500 0.6117 -0.0765 0.0918 -0.1011 129 PHE K CD2 5487 C CE1 . PHE C 103 ? 1.1504 0.5574 0.5867 -0.1008 0.0969 -0.1004 129 PHE K CE1 5488 C CE2 . PHE C 103 ? 1.1282 0.5508 0.5949 -0.0768 0.0870 -0.0916 129 PHE K CE2 5489 C CZ . PHE C 103 ? 1.1414 0.5541 0.5833 -0.0885 0.0889 -0.0912 129 PHE K CZ 5490 N N . THR C 104 ? 1.3021 0.7407 0.8777 -0.0716 0.1080 -0.1489 130 THR K N 5491 C CA . THR C 104 ? 1.2981 0.7397 0.9061 -0.0632 0.1033 -0.1556 130 THR K CA 5492 C C . THR C 104 ? 1.3038 0.7461 0.9181 -0.0511 0.0893 -0.1390 130 THR K C 5493 O O . THR C 104 ? 1.3080 0.7515 0.9049 -0.0484 0.0850 -0.1251 130 THR K O 5494 C CB . THR C 104 ? 1.2855 0.7340 0.9166 -0.0617 0.1097 -0.1725 130 THR K CB 5495 O OG1 . THR C 104 ? 1.2882 0.7383 0.9010 -0.0723 0.1215 -0.1797 130 THR K OG1 5496 C CG2 . THR C 104 ? 1.2751 0.7250 0.9352 -0.0621 0.1123 -0.1905 130 THR K CG2 5497 N N . GLY C 105 ? 1.3733 0.8148 1.0125 -0.0446 0.0816 -0.1410 131 GLY K N 5498 C CA . GLY C 105 ? 1.3804 0.8227 1.0268 -0.0349 0.0680 -0.1263 131 GLY K CA 5499 C C . GLY C 105 ? 1.3938 0.8313 1.0314 -0.0353 0.0591 -0.1129 131 GLY K C 5500 O O . GLY C 105 ? 1.3959 0.8286 1.0269 -0.0420 0.0628 -0.1165 131 GLY K O 5501 N N . PRO C 106 ? 1.2625 0.7018 0.8998 -0.0292 0.0474 -0.0977 132 PRO K N 5502 C CA . PRO C 106 ? 1.2768 0.7128 0.9080 -0.0299 0.0375 -0.0844 132 PRO K CA 5503 C C . PRO C 106 ? 1.2839 0.7226 0.8863 -0.0347 0.0406 -0.0741 132 PRO K C 5504 O O . PRO C 106 ? 1.2773 0.7204 0.8655 -0.0353 0.0470 -0.0742 132 PRO K O 5505 C CB . PRO C 106 ? 1.2838 0.7232 0.9232 -0.0230 0.0256 -0.0732 132 PRO K CB 5506 C CG . PRO C 106 ? 1.2760 0.7232 0.9087 -0.0198 0.0312 -0.0740 132 PRO K CG 5507 C CD . PRO C 106 ? 1.2610 0.7069 0.8984 -0.0228 0.0441 -0.0914 132 PRO K CD 5508 N N . ILE C 107 ? 1.0799 0.5156 0.6750 -0.0380 0.0351 -0.0657 133 ILE K N 5509 C CA . ILE C 107 ? 1.0860 0.5263 0.6573 -0.0409 0.0344 -0.0537 133 ILE K CA 5510 C C . ILE C 107 ? 1.0940 0.5426 0.6643 -0.0363 0.0244 -0.0396 133 ILE K C 5511 O O . ILE C 107 ? 1.1040 0.5508 0.6808 -0.0368 0.0150 -0.0323 133 ILE K O 5512 C CB . ILE C 107 ? 1.0958 0.5303 0.6585 -0.0477 0.0339 -0.0515 133 ILE K CB 5513 C CG1 . ILE C 107 ? 1.0917 0.5184 0.6561 -0.0535 0.0439 -0.0665 133 ILE K CG1 5514 C CG2 . ILE C 107 ? 1.1029 0.5431 0.6426 -0.0504 0.0331 -0.0404 133 ILE K CG2 5515 C CD1 . ILE C 107 ? 1.1010 0.5214 0.6581 -0.0603 0.0433 -0.0653 133 ILE K CD1 5516 N N . PRO C 108 ? 1.0901 0.5476 0.6511 -0.0329 0.0261 -0.0360 134 PRO K N 5517 C CA . PRO C 108 ? 1.0955 0.5634 0.6550 -0.0287 0.0188 -0.0254 134 PRO K CA 5518 C C . PRO C 108 ? 1.1094 0.5823 0.6611 -0.0324 0.0110 -0.0132 134 PRO K C 5519 O O . PRO C 108 ? 1.1124 0.5867 0.6506 -0.0363 0.0134 -0.0109 134 PRO K O 5520 C CB . PRO C 108 ? 1.0899 0.5653 0.6351 -0.0268 0.0244 -0.0257 134 PRO K CB 5521 C CG . PRO C 108 ? 1.0786 0.5459 0.6249 -0.0281 0.0334 -0.0377 134 PRO K CG 5522 C CD . PRO C 108 ? 1.0807 0.5380 0.6314 -0.0337 0.0357 -0.0434 134 PRO K CD 5523 N N . ASP C 109 ? 1.3341 0.8098 0.8928 -0.0319 0.0016 -0.0052 135 ASP K N 5524 C CA . ASP C 109 ? 1.3520 0.8338 0.9016 -0.0374 -0.0056 0.0066 135 ASP K CA 5525 C C . ASP C 109 ? 1.3607 0.8585 0.8945 -0.0374 -0.0029 0.0113 135 ASP K C 5526 O O . ASP C 109 ? 1.3725 0.8777 0.8966 -0.0426 -0.0059 0.0186 135 ASP K O 5527 C CB . ASP C 109 ? 1.3623 0.8440 0.9199 -0.0386 -0.0171 0.0148 135 ASP K CB 5528 C CG . ASP C 109 ? 1.3584 0.8234 0.9334 -0.0388 -0.0233 0.0112 135 ASP K CG 5529 O OD1 . ASP C 109 ? 1.3482 0.8035 0.9276 -0.0394 -0.0183 0.0028 135 ASP K OD1 5530 O OD2 . ASP C 109 ? 1.3657 0.8271 0.9504 -0.0387 -0.0338 0.0163 135 ASP K OD2 5531 N N . SER C 110 ? 1.3860 0.8895 0.9186 -0.0317 0.0022 0.0065 136 SER K N 5532 C CA . SER C 110 ? 1.3943 0.9130 0.9151 -0.0301 0.0040 0.0088 136 SER K CA 5533 C C . SER C 110 ? 1.3953 0.9130 0.9049 -0.0329 0.0080 0.0072 136 SER K C 5534 O O . SER C 110 ? 1.4036 0.9342 0.9046 -0.0330 0.0072 0.0100 136 SER K O 5535 C CB . SER C 110 ? 1.3812 0.9025 0.9044 -0.0232 0.0081 0.0028 136 SER K CB 5536 O OG . SER C 110 ? 1.3601 0.8681 0.8852 -0.0222 0.0147 -0.0062 136 SER K OG 5537 N N . LEU C 111 ? 1.0968 0.5994 0.6071 -0.0354 0.0119 0.0018 137 LEU K N 5538 C CA . LEU C 111 ? 1.0998 0.5988 0.5987 -0.0398 0.0145 0.0010 137 LEU K CA 5539 C C . LEU C 111 ? 1.1091 0.6154 0.6034 -0.0450 0.0091 0.0095 137 LEU K C 5540 O O . LEU C 111 ? 1.1130 0.6225 0.5972 -0.0476 0.0095 0.0106 137 LEU K O 5541 C CB . LEU C 111 ? 1.0968 0.5788 0.5981 -0.0431 0.0196 -0.0067 137 LEU K CB 5542 C CG . LEU C 111 ? 1.0879 0.5642 0.5872 -0.0408 0.0266 -0.0157 137 LEU K CG 5543 C CD1 . LEU C 111 ? 1.0859 0.5486 0.5916 -0.0445 0.0323 -0.0252 137 LEU K CD1 5544 C CD2 . LEU C 111 ? 1.0908 0.5685 0.5739 -0.0426 0.0277 -0.0147 137 LEU K CD2 5545 N N . GLY C 112 ? 1.2081 0.7166 0.7093 -0.0471 0.0031 0.0156 138 GLY K N 5546 C CA . GLY C 112 ? 1.2165 0.7330 0.7124 -0.0536 -0.0025 0.0243 138 GLY K CA 5547 C C . GLY C 112 ? 1.2161 0.7540 0.7048 -0.0530 -0.0034 0.0279 138 GLY K C 5548 O O . GLY C 112 ? 1.2178 0.7669 0.7015 -0.0591 -0.0074 0.0345 138 GLY K O 5549 N N . LYS C 113 ? 1.2625 0.8069 0.7515 -0.0461 0.0000 0.0228 139 LYS K N 5550 C CA . LYS C 113 ? 1.2574 0.8231 0.7427 -0.0443 -0.0009 0.0238 139 LYS K CA 5551 C C . LYS C 113 ? 1.2516 0.8220 0.7304 -0.0422 0.0011 0.0197 139 LYS K C 5552 O O . LYS C 113 ? 1.2473 0.8358 0.7257 -0.0396 0.0000 0.0182 139 LYS K O 5553 C CB . LYS C 113 ? 1.2540 0.8265 0.7448 -0.0379 -0.0003 0.0212 139 LYS K CB 5554 C CG . LYS C 113 ? 1.2606 0.8314 0.7576 -0.0404 -0.0045 0.0265 139 LYS K CG 5555 C CD . LYS C 113 ? 1.2581 0.8308 0.7610 -0.0335 -0.0033 0.0227 139 LYS K CD 5556 C CE . LYS C 113 ? 1.2497 0.8424 0.7492 -0.0294 -0.0016 0.0195 139 LYS K CE 5557 N NZ . LYS C 113 ? 1.2438 0.8389 0.7485 -0.0228 -0.0007 0.0159 139 LYS K NZ 5558 N N . LEU C 114 ? 1.1014 0.6558 0.5758 -0.0437 0.0034 0.0171 140 LEU K N 5559 C CA . LEU C 114 ? 1.0991 0.6550 0.5664 -0.0423 0.0034 0.0137 140 LEU K CA 5560 C C . LEU C 114 ? 1.1039 0.6643 0.5664 -0.0489 0.0008 0.0179 140 LEU K C 5561 O O . LEU C 114 ? 1.1116 0.6575 0.5705 -0.0543 0.0017 0.0193 140 LEU K O 5562 C CB . LEU C 114 ? 1.1023 0.6377 0.5646 -0.0412 0.0071 0.0081 140 LEU K CB 5563 C CG . LEU C 114 ? 1.1020 0.6251 0.5696 -0.0389 0.0115 0.0042 140 LEU K CG 5564 C CD1 . LEU C 114 ? 1.1027 0.6062 0.5637 -0.0425 0.0160 -0.0009 140 LEU K CD1 5565 C CD2 . LEU C 114 ? 1.0915 0.6222 0.5626 -0.0316 0.0115 0.0012 140 LEU K CD2 5566 N N . PHE C 115 ? 1.4562 1.0378 0.9195 -0.0487 -0.0024 0.0188 141 PHE K N 5567 C CA . PHE C 115 ? 1.4613 1.0521 0.9216 -0.0556 -0.0051 0.0229 141 PHE K CA 5568 C C . PHE C 115 ? 1.4621 1.0539 0.9182 -0.0546 -0.0072 0.0196 141 PHE K C 5569 O O . PHE C 115 ? 1.4667 1.0664 0.9208 -0.0601 -0.0096 0.0223 141 PHE K O 5570 C CB . PHE C 115 ? 1.4639 1.0800 0.9283 -0.0585 -0.0070 0.0259 141 PHE K CB 5571 C CG . PHE C 115 ? 1.4647 1.0786 0.9316 -0.0615 -0.0070 0.0310 141 PHE K CG 5572 C CD1 . PHE C 115 ? 1.4702 1.0748 0.9347 -0.0699 -0.0093 0.0383 141 PHE K CD1 5573 C CD2 . PHE C 115 ? 1.4614 1.0811 0.9331 -0.0559 -0.0060 0.0285 141 PHE K CD2 5574 C CE1 . PHE C 115 ? 1.4727 1.0730 0.9401 -0.0727 -0.0117 0.0434 141 PHE K CE1 5575 C CE2 . PHE C 115 ? 1.4643 1.0807 0.9382 -0.0589 -0.0075 0.0336 141 PHE K CE2 5576 C CZ . PHE C 115 ? 1.4702 1.0764 0.9421 -0.0673 -0.0109 0.0412 141 PHE K CZ 5577 N N . LYS C 116 ? 1.2726 0.8564 0.7274 -0.0481 -0.0075 0.0140 142 LYS K N 5578 C CA . LYS C 116 ? 1.2755 0.8531 0.7247 -0.0480 -0.0112 0.0115 142 LYS K CA 5579 C C . LYS C 116 ? 1.2751 0.8253 0.7140 -0.0523 -0.0086 0.0121 142 LYS K C 5580 O O . LYS C 116 ? 1.2783 0.8181 0.7094 -0.0539 -0.0117 0.0107 142 LYS K O 5581 C CB . LYS C 116 ? 1.2752 0.8601 0.7284 -0.0394 -0.0154 0.0052 142 LYS K CB 5582 C CG . LYS C 116 ? 1.2837 0.8940 0.7453 -0.0371 -0.0208 0.0021 142 LYS K CG 5583 C CD . LYS C 116 ? 1.2792 0.9084 0.7518 -0.0285 -0.0222 -0.0044 142 LYS K CD 5584 C CE . LYS C 116 ? 1.2783 0.9247 0.7562 -0.0304 -0.0170 -0.0024 142 LYS K CE 5585 N NZ . LYS C 116 ? 1.2721 0.9344 0.7593 -0.0224 -0.0174 -0.0091 142 LYS K NZ 5586 N N . LEU C 117 ? 1.1267 0.6659 0.5662 -0.0547 -0.0033 0.0133 143 LEU K N 5587 C CA . LEU C 117 ? 1.1325 0.6479 0.5644 -0.0588 0.0009 0.0112 143 LEU K CA 5588 C C . LEU C 117 ? 1.1404 0.6471 0.5651 -0.0670 0.0005 0.0138 143 LEU K C 5589 O O . LEU C 117 ? 1.1416 0.6554 0.5700 -0.0706 -0.0005 0.0184 143 LEU K O 5590 C CB . LEU C 117 ? 1.1341 0.6419 0.5723 -0.0583 0.0063 0.0098 143 LEU K CB 5591 C CG . LEU C 117 ? 1.1328 0.6197 0.5646 -0.0612 0.0116 0.0041 143 LEU K CG 5592 C CD1 . LEU C 117 ? 1.1230 0.6080 0.5517 -0.0562 0.0117 0.0000 143 LEU K CD1 5593 C CD2 . LEU C 117 ? 1.1318 0.6104 0.5718 -0.0628 0.0167 0.0015 143 LEU K CD2 5594 N N . ARG C 118 ? 1.3472 0.8374 0.7605 -0.0708 0.0009 0.0111 144 ARG K N 5595 C CA . ARG C 118 ? 1.3534 0.8330 0.7572 -0.0791 0.0002 0.0126 144 ARG K CA 5596 C C . ARG C 118 ? 1.3491 0.8083 0.7466 -0.0853 0.0071 0.0080 144 ARG K C 5597 O O . ARG C 118 ? 1.3505 0.8038 0.7486 -0.0910 0.0098 0.0084 144 ARG K O 5598 C CB . ARG C 118 ? 1.3553 0.8339 0.7498 -0.0798 -0.0066 0.0131 144 ARG K CB 5599 C CG . ARG C 118 ? 1.3555 0.8568 0.7589 -0.0740 -0.0133 0.0153 144 ARG K CG 5600 C CD . ARG C 118 ? 1.3628 0.8626 0.7595 -0.0755 -0.0215 0.0156 144 ARG K CD 5601 N NE . ARG C 118 ? 1.3699 0.8569 0.7562 -0.0850 -0.0210 0.0182 144 ARG K NE 5602 C CZ . ARG C 118 ? 1.3753 0.8448 0.7477 -0.0904 -0.0247 0.0178 144 ARG K CZ 5603 N NH1 . ARG C 118 ? 1.3816 0.8405 0.7445 -0.0995 -0.0237 0.0200 144 ARG K NH1 5604 N NH2 . ARG C 118 ? 1.3748 0.8365 0.7417 -0.0875 -0.0301 0.0155 144 ARG K NH2 5605 N N . PHE C 119 ? 1.3097 0.7583 0.7007 -0.0850 0.0097 0.0031 145 PHE K N 5606 C CA . PHE C 119 ? 1.3025 0.7340 0.6876 -0.0919 0.0175 -0.0034 145 PHE K CA 5607 C C . PHE C 119 ? 1.2915 0.7231 0.6873 -0.0875 0.0238 -0.0089 145 PHE K C 5608 O O . PHE C 119 ? 1.2850 0.7205 0.6825 -0.0816 0.0229 -0.0097 145 PHE K O 5609 C CB . PHE C 119 ? 1.3025 0.7195 0.6690 -0.0986 0.0163 -0.0055 145 PHE K CB 5610 C CG . PHE C 119 ? 1.3139 0.7305 0.6703 -0.1017 0.0080 -0.0001 145 PHE K CG 5611 C CD1 . PHE C 119 ? 1.3187 0.7445 0.6764 -0.0949 -0.0013 0.0037 145 PHE K CD1 5612 C CD2 . PHE C 119 ? 1.3197 0.7270 0.6667 -0.1113 0.0089 0.0003 145 PHE K CD2 5613 C CE1 . PHE C 119 ? 1.3290 0.7551 0.6800 -0.0972 -0.0099 0.0077 145 PHE K CE1 5614 C CE2 . PHE C 119 ? 1.3299 0.7366 0.6681 -0.1142 0.0006 0.0054 145 PHE K CE2 5615 C CZ . PHE C 119 ? 1.3349 0.7511 0.6756 -0.1070 -0.0091 0.0090 145 PHE K CZ 5616 N N . LEU C 120 ? 1.1401 0.5670 0.5442 -0.0904 0.0297 -0.0133 146 LEU K N 5617 C CA . LEU C 120 ? 1.1315 0.5572 0.5475 -0.0871 0.0356 -0.0202 146 LEU K CA 5618 C C . LEU C 120 ? 1.1342 0.5465 0.5479 -0.0956 0.0441 -0.0305 146 LEU K C 5619 O O . LEU C 120 ? 1.1380 0.5464 0.5565 -0.0998 0.0455 -0.0327 146 LEU K O 5620 C CB . LEU C 120 ? 1.1263 0.5621 0.5607 -0.0806 0.0328 -0.0166 146 LEU K CB 5621 C CG . LEU C 120 ? 1.1169 0.5538 0.5667 -0.0751 0.0363 -0.0222 146 LEU K CG 5622 C CD1 . LEU C 120 ? 1.1088 0.5518 0.5561 -0.0692 0.0360 -0.0218 146 LEU K CD1 5623 C CD2 . LEU C 120 ? 1.1168 0.5603 0.5822 -0.0710 0.0312 -0.0174 146 LEU K CD2 5624 N N . ARG C 121 ? 1.2453 0.6512 0.6519 -0.0989 0.0498 -0.0376 147 ARG K N 5625 C CA . ARG C 121 ? 1.2390 0.6349 0.6439 -0.1081 0.0592 -0.0495 147 ARG K CA 5626 C C . ARG C 121 ? 1.2267 0.6241 0.6419 -0.1055 0.0659 -0.0587 147 ARG K C 5627 O O . ARG C 121 ? 1.2224 0.6181 0.6277 -0.1063 0.0668 -0.0591 147 ARG K O 5628 C CB . ARG C 121 ? 1.2448 0.6294 0.6249 -0.1202 0.0607 -0.0504 147 ARG K CB 5629 C CG . ARG C 121 ? 1.2539 0.6343 0.6256 -0.1261 0.0574 -0.0462 147 ARG K CG 5630 C CD . ARG C 121 ? 1.2631 0.6323 0.6089 -0.1370 0.0556 -0.0442 147 ARG K CD 5631 N NE . ARG C 121 ? 1.2703 0.6425 0.6084 -0.1312 0.0449 -0.0332 147 ARG K NE 5632 C CZ . ARG C 121 ? 1.2821 0.6529 0.6104 -0.1331 0.0366 -0.0253 147 ARG K CZ 5633 N NH1 . ARG C 121 ? 1.2880 0.6535 0.6112 -0.1410 0.0383 -0.0262 147 ARG K NH1 5634 N NH2 . ARG C 121 ? 1.2879 0.6629 0.6127 -0.1270 0.0265 -0.0175 147 ARG K NH2 5635 N N . LEU C 122 ? 1.2879 0.6879 0.7240 -0.1024 0.0695 -0.0661 148 LEU K N 5636 C CA . LEU C 122 ? 1.2766 0.6780 0.7258 -0.1011 0.0768 -0.0778 148 LEU K CA 5637 C C . LEU C 122 ? 1.2733 0.6685 0.7238 -0.1119 0.0874 -0.0937 148 LEU K C 5638 O O . LEU C 122 ? 1.2646 0.6624 0.7300 -0.1116 0.0943 -0.1062 148 LEU K O 5639 C CB . LEU C 122 ? 1.2740 0.6835 0.7484 -0.0893 0.0722 -0.0762 148 LEU K CB 5640 C CG . LEU C 122 ? 1.2809 0.6980 0.7528 -0.0809 0.0619 -0.0608 148 LEU K CG 5641 C CD1 . LEU C 122 ? 1.2813 0.7050 0.7752 -0.0715 0.0566 -0.0584 148 LEU K CD1 5642 C CD2 . LEU C 122 ? 1.2768 0.6963 0.7345 -0.0793 0.0613 -0.0566 148 LEU K CD2 5643 N N . ASN C 123 ? 1.2579 0.6462 0.6944 -0.1215 0.0887 -0.0940 149 ASN K N 5644 C CA . ASN C 123 ? 1.2559 0.6402 0.6975 -0.1310 0.0982 -0.1098 149 ASN K CA 5645 C C . ASN C 123 ? 1.2493 0.6329 0.6849 -0.1408 0.1100 -0.1243 149 ASN K C 5646 O O . ASN C 123 ? 1.2488 0.6312 0.6687 -0.1433 0.1103 -0.1202 149 ASN K O 5647 C CB . ASN C 123 ? 1.2666 0.6433 0.6913 -0.1405 0.0971 -0.1067 149 ASN K CB 5648 C CG . ASN C 123 ? 1.2734 0.6438 0.6673 -0.1483 0.0943 -0.0969 149 ASN K CG 5649 O OD1 . ASN C 123 ? 1.2773 0.6497 0.6652 -0.1410 0.0846 -0.0825 149 ASN K OD1 5650 N ND2 . ASN C 123 ? 1.2762 0.6388 0.6506 -0.1638 0.1022 -0.1053 149 ASN K ND2 5651 N N . ASN C 124 ? 1.2632 0.6482 0.7131 -0.1466 0.1194 -0.1421 150 ASN K N 5652 C CA . ASN C 124 ? 1.2560 0.6434 0.7050 -0.1570 0.1324 -0.1597 150 ASN K CA 5653 C C . ASN C 124 ? 1.2457 0.6395 0.7026 -0.1505 0.1336 -0.1607 150 ASN K C 5654 O O . ASN C 124 ? 1.2452 0.6373 0.6834 -0.1601 0.1393 -0.1630 150 ASN K O 5655 C CB . ASN C 124 ? 1.2666 0.6458 0.6828 -0.1763 0.1392 -0.1624 150 ASN K CB 5656 C CG . ASN C 124 ? 1.2708 0.6480 0.6886 -0.1867 0.1459 -0.1751 150 ASN K CG 5657 O OD1 . ASN C 124 ? 1.2630 0.6368 0.6848 -0.1819 0.1388 -0.1680 150 ASN K OD1 5658 N ND2 . ASN C 124 ? 1.2835 0.6633 0.6976 -0.2019 0.1600 -0.1946 150 ASN K ND2 5659 N N . ASN C 125 ? 1.1219 0.5222 0.6064 -0.1348 0.1274 -0.1586 151 ASN K N 5660 C CA . ASN C 125 ? 1.1109 0.5182 0.6087 -0.1263 0.1273 -0.1599 151 ASN K CA 5661 C C . ASN C 125 ? 1.1031 0.5178 0.6374 -0.1192 0.1299 -0.1755 151 ASN K C 5662 O O . ASN C 125 ? 1.1070 0.5213 0.6547 -0.1224 0.1331 -0.1873 151 ASN K O 5663 C CB . ASN C 125 ? 1.1040 0.5120 0.5995 -0.1133 0.1146 -0.1400 151 ASN K CB 5664 C CG . ASN C 125 ? 1.1072 0.5115 0.5748 -0.1174 0.1131 -0.1295 151 ASN K CG 5665 O OD1 . ASN C 125 ? 1.1033 0.5105 0.5708 -0.1162 0.1155 -0.1316 151 ASN K OD1 5666 N ND2 . ASN C 125 ? 1.1150 0.5123 0.5597 -0.1223 0.1081 -0.1184 151 ASN K ND2 5667 N N . SER C 126 ? 1.1705 0.5917 0.7210 -0.1100 0.1283 -0.1765 152 SER K N 5668 C CA . SER C 126 ? 1.1608 0.5889 0.7483 -0.1014 0.1283 -0.1903 152 SER K CA 5669 C C . SER C 126 ? 1.1630 0.5909 0.7713 -0.0856 0.1137 -0.1786 152 SER K C 5670 O O . SER C 126 ? 1.1564 0.5886 0.7948 -0.0777 0.1112 -0.1882 152 SER K O 5671 C CB . SER C 126 ? 1.1496 0.5857 0.7451 -0.1037 0.1376 -0.2038 152 SER K CB 5672 O OG . SER C 126 ? 1.1474 0.5844 0.7263 -0.1206 0.1518 -0.2176 152 SER K OG 5673 N N . LEU C 127 ? 1.0964 0.5197 0.6882 -0.0818 0.1037 -0.1582 153 LEU K N 5674 C CA . LEU C 127 ? 1.0929 0.5165 0.6975 -0.0693 0.0895 -0.1441 153 LEU K CA 5675 C C . LEU C 127 ? 1.0948 0.5160 0.7297 -0.0632 0.0820 -0.1503 153 LEU K C 5676 O O . LEU C 127 ? 1.1014 0.5185 0.7435 -0.0681 0.0847 -0.1605 153 LEU K O 5677 C CB . LEU C 127 ? 1.0986 0.5189 0.6801 -0.0694 0.0817 -0.1243 153 LEU K CB 5678 C CG . LEU C 127 ? 1.0978 0.5204 0.6540 -0.0704 0.0824 -0.1131 153 LEU K CG 5679 C CD1 . LEU C 127 ? 1.1102 0.5312 0.6491 -0.0704 0.0745 -0.0966 153 LEU K CD1 5680 C CD2 . LEU C 127 ? 1.0872 0.5163 0.6537 -0.0610 0.0785 -0.1094 153 LEU K CD2 5681 N N . THR C 128 ? 1.5845 1.0075 1.2367 -0.0527 0.0715 -0.1437 154 THR K N 5682 C CA . THR C 128 ? 1.5882 1.0073 1.2705 -0.0461 0.0612 -0.1483 154 THR K CA 5683 C C . THR C 128 ? 1.6000 1.0161 1.2796 -0.0397 0.0455 -0.1275 154 THR K C 5684 O O . THR C 128 ? 1.6036 1.0237 1.2612 -0.0395 0.0441 -0.1122 154 THR K O 5685 C CB . THR C 128 ? 1.5773 1.0012 1.2888 -0.0403 0.0628 -0.1639 154 THR K CB 5686 O OG1 . THR C 128 ? 1.5716 1.0003 1.2789 -0.0340 0.0585 -0.1529 154 THR K OG1 5687 C CG2 . THR C 128 ? 1.5635 0.9934 1.2758 -0.0482 0.0799 -0.1850 154 THR K CG2 5688 N N . GLY C 129 ? 1.2800 0.6894 0.9821 -0.0353 0.0331 -0.1276 155 GLY K N 5689 C CA . GLY C 129 ? 1.2929 0.6990 0.9930 -0.0312 0.0172 -0.1085 155 GLY K CA 5690 C C . GLY C 129 ? 1.3066 0.7065 0.9916 -0.0367 0.0118 -0.0972 155 GLY K C 5691 O O . GLY C 129 ? 1.3056 0.7023 0.9865 -0.0424 0.0189 -0.1054 155 GLY K O 5692 N N . PRO C 130 ? 1.1456 0.5445 0.8227 -0.0357 -0.0010 -0.0785 156 PRO K N 5693 C CA . PRO C 130 ? 1.1593 0.5532 0.8223 -0.0415 -0.0076 -0.0663 156 PRO K CA 5694 C C . PRO C 130 ? 1.1624 0.5651 0.7947 -0.0463 -0.0006 -0.0552 156 PRO K C 5695 O O . PRO C 130 ? 1.1586 0.5706 0.7801 -0.0443 0.0068 -0.0545 156 PRO K O 5696 C CB . PRO C 130 ? 1.2757 0.6658 0.9448 -0.0392 -0.0251 -0.0517 156 PRO K CB 5697 C CG . PRO C 130 ? 1.2646 0.6648 0.9324 -0.0339 -0.0232 -0.0488 156 PRO K CG 5698 C CD . PRO C 130 ? 1.2611 0.6627 0.9445 -0.0300 -0.0112 -0.0689 156 PRO K CD 5699 N N . ILE C 131 ? 1.1780 0.5772 0.7980 -0.0521 -0.0050 -0.0461 157 ILE K N 5700 C CA . ILE C 131 ? 1.1837 0.5904 0.7771 -0.0570 -0.0001 -0.0364 157 ILE K CA 5701 C C . ILE C 131 ? 1.1964 0.6100 0.7818 -0.0570 -0.0107 -0.0190 157 ILE K C 5702 O O . ILE C 131 ? 1.2074 0.6151 0.7970 -0.0600 -0.0224 -0.0108 157 ILE K O 5703 C CB . ILE C 131 ? 1.1891 0.5887 0.7755 -0.0641 0.0014 -0.0380 157 ILE K CB 5704 C CG1 . ILE C 131 ? 1.1803 0.5718 0.7807 -0.0649 0.0094 -0.0570 157 ILE K CG1 5705 C CG2 . ILE C 131 ? 1.1938 0.6007 0.7543 -0.0689 0.0077 -0.0312 157 ILE K CG2 5706 C CD1 . ILE C 131 ? 1.1855 0.5704 0.7776 -0.0723 0.0121 -0.0598 157 ILE K CD1 5707 N N . PRO C 132 ? 1.1228 0.5489 0.6966 -0.0545 -0.0071 -0.0138 158 PRO K N 5708 C CA . PRO C 132 ? 1.1269 0.5624 0.6944 -0.0545 -0.0158 0.0004 158 PRO K CA 5709 C C . PRO C 132 ? 1.1355 0.5751 0.6880 -0.0619 -0.0206 0.0122 158 PRO K C 5710 O O . PRO C 132 ? 1.1354 0.5774 0.6754 -0.0650 -0.0138 0.0108 158 PRO K O 5711 C CB . PRO C 132 ? 1.1178 0.5663 0.6762 -0.0501 -0.0080 -0.0005 158 PRO K CB 5712 C CG . PRO C 132 ? 1.1091 0.5548 0.6616 -0.0503 0.0037 -0.0111 158 PRO K CG 5713 C CD . PRO C 132 ? 1.1124 0.5444 0.6779 -0.0522 0.0052 -0.0216 158 PRO K CD 5714 N N . MET C 133 ? 1.2105 0.6501 0.7642 -0.0656 -0.0326 0.0235 159 MET K N 5715 C CA . MET C 133 ? 1.2243 0.6656 0.7662 -0.0743 -0.0386 0.0341 159 MET K CA 5716 C C . MET C 133 ? 1.2279 0.6886 0.7517 -0.0766 -0.0339 0.0406 159 MET K C 5717 O O . MET C 133 ? 1.2327 0.6980 0.7451 -0.0829 -0.0339 0.0455 159 MET K O 5718 C CB . MET C 133 ? 1.2343 0.6691 0.7818 -0.0790 -0.0538 0.0445 159 MET K CB 5719 C CG . MET C 133 ? 1.2365 0.6512 0.7981 -0.0806 -0.0618 0.0412 159 MET K CG 5720 S SD . MET C 133 ? 1.2441 0.6582 0.7907 -0.0901 -0.0616 0.0469 159 MET K SD 5721 C CE . MET C 133 ? 1.2498 0.6384 0.8150 -0.0921 -0.0746 0.0440 159 MET K CE 5722 N N . SER C 134 ? 1.4469 0.9193 0.9696 -0.0713 -0.0302 0.0395 160 SER K N 5723 C CA . SER C 134 ? 1.4501 0.9426 0.9590 -0.0725 -0.0267 0.0440 160 SER K CA 5724 C C . SER C 134 ? 1.4450 0.9397 0.9454 -0.0716 -0.0180 0.0383 160 SER K C 5725 O O . SER C 134 ? 1.4464 0.9559 0.9361 -0.0740 -0.0166 0.0418 160 SER K O 5726 C CB . SER C 134 ? 1.2328 0.7356 0.7442 -0.0660 -0.0245 0.0421 160 SER K CB 5727 O OG . SER C 134 ? 1.2291 0.7209 0.7517 -0.0582 -0.0195 0.0319 160 SER K OG 5728 N N . LEU C 135 ? 1.1999 0.6800 0.7054 -0.0689 -0.0125 0.0289 161 LEU K N 5729 C CA . LEU C 135 ? 1.1965 0.6749 0.6924 -0.0701 -0.0055 0.0240 161 LEU K CA 5730 C C . LEU C 135 ? 1.2037 0.6857 0.6901 -0.0778 -0.0094 0.0315 161 LEU K C 5731 O O . LEU C 135 ? 1.2036 0.6934 0.6792 -0.0791 -0.0063 0.0317 161 LEU K O 5732 C CB . LEU C 135 ? 1.1851 0.6464 0.6871 -0.0690 0.0006 0.0127 161 LEU K CB 5733 C CG . LEU C 135 ? 1.1721 0.6316 0.6757 -0.0635 0.0088 0.0028 161 LEU K CG 5734 C CD1 . LEU C 135 ? 1.1622 0.6068 0.6730 -0.0650 0.0146 -0.0090 161 LEU K CD1 5735 C CD2 . LEU C 135 ? 1.1735 0.6409 0.6618 -0.0632 0.0131 0.0031 161 LEU K CD2 5736 N N . THR C 136 ? 1.1612 0.6376 0.6518 -0.0832 -0.0172 0.0378 162 THR K N 5737 C CA . THR C 136 ? 1.1665 0.6455 0.6485 -0.0916 -0.0213 0.0451 162 THR K CA 5738 C C . THR C 136 ? 1.1672 0.6685 0.6392 -0.0949 -0.0230 0.0528 162 THR K C 5739 O O . THR C 136 ? 1.1692 0.6765 0.6332 -0.1018 -0.0251 0.0579 162 THR K O 5740 C CB . THR C 136 ? 1.1735 0.6392 0.6625 -0.0973 -0.0308 0.0503 162 THR K CB 5741 O OG1 . THR C 136 ? 1.1736 0.6473 0.6631 -0.1005 -0.0393 0.0600 162 THR K OG1 5742 C CG2 . THR C 136 ? 1.1690 0.6159 0.6730 -0.0924 -0.0300 0.0407 162 THR K CG2 5743 N N . ASN C 137 ? 1.4120 0.9268 0.8852 -0.0901 -0.0217 0.0527 163 ASN K N 5744 C CA . ASN C 137 ? 1.4108 0.9493 0.8766 -0.0930 -0.0224 0.0573 163 ASN K CA 5745 C C . ASN C 137 ? 1.4054 0.9543 0.8661 -0.0883 -0.0161 0.0511 163 ASN K C 5746 O O . ASN C 137 ? 1.4031 0.9733 0.8603 -0.0894 -0.0162 0.0523 163 ASN K O 5747 C CB . ASN C 137 ? 1.4112 0.9610 0.8802 -0.0915 -0.0249 0.0601 163 ASN K CB 5748 C CG . ASN C 137 ? 1.4191 0.9609 0.8903 -0.0989 -0.0342 0.0689 163 ASN K CG 5749 O OD1 . ASN C 137 ? 1.4187 0.9467 0.8989 -0.0951 -0.0372 0.0678 163 ASN K OD1 5750 N ND2 . ASN C 137 ? 1.4255 0.9759 0.8887 -0.1100 -0.0396 0.0776 163 ASN K ND2 5751 N N . ILE C 138 ? 1.1950 0.7292 0.6557 -0.0837 -0.0112 0.0440 164 ILE K N 5752 C CA . ILE C 138 ? 1.1905 0.7304 0.6451 -0.0805 -0.0076 0.0391 164 ILE K CA 5753 C C . ILE C 138 ? 1.1942 0.7297 0.6418 -0.0871 -0.0088 0.0411 164 ILE K C 5754 O O . ILE C 138 ? 1.1993 0.7162 0.6451 -0.0891 -0.0069 0.0384 164 ILE K O 5755 C CB . ILE C 138 ? 1.1908 0.7155 0.6458 -0.0743 -0.0022 0.0308 164 ILE K CB 5756 C CG1 . ILE C 138 ? 1.1904 0.7113 0.6544 -0.0689 -0.0008 0.0283 164 ILE K CG1 5757 C CG2 . ILE C 138 ? 1.1858 0.7175 0.6346 -0.0703 -0.0010 0.0267 164 ILE K CG2 5758 C CD1 . ILE C 138 ? 1.1909 0.6953 0.6562 -0.0652 0.0050 0.0198 164 ILE K CD1 5759 N N . MET C 139 ? 1.5311 1.0848 0.9751 -0.0907 -0.0115 0.0445 165 MET K N 5760 C CA . MET C 139 ? 1.5344 1.0852 0.9723 -0.0981 -0.0135 0.0476 165 MET K CA 5761 C C . MET C 139 ? 1.5327 1.0823 0.9653 -0.0951 -0.0120 0.0424 165 MET K C 5762 O O . MET C 139 ? 1.5351 1.0821 0.9620 -0.1002 -0.0137 0.0438 165 MET K O 5763 C CB . MET C 139 ? 1.5373 1.1089 0.9744 -0.1055 -0.0177 0.0543 165 MET K CB 5764 C CG . MET C 139 ? 1.5359 1.1174 0.9769 -0.1075 -0.0200 0.0590 165 MET K CG 5765 S SD . MET C 139 ? 1.5254 1.1422 0.9679 -0.1073 -0.0196 0.0574 165 MET K SD 5766 C CE . MET C 139 ? 1.5171 1.1340 0.9650 -0.0931 -0.0153 0.0471 165 MET K CE 5767 N N . THR C 140 ? 1.1735 0.7241 0.6078 -0.0870 -0.0099 0.0366 166 THR K N 5768 C CA . THR C 140 ? 1.1745 0.7193 0.6028 -0.0844 -0.0101 0.0319 166 THR K CA 5769 C C . THR C 140 ? 1.1794 0.6981 0.6011 -0.0860 -0.0062 0.0285 166 THR K C 5770 O O . THR C 140 ? 1.1832 0.6918 0.5963 -0.0871 -0.0068 0.0258 166 THR K O 5771 C CB . THR C 140 ? 1.1691 0.7274 0.6017 -0.0757 -0.0115 0.0272 166 THR K CB 5772 O OG1 . THR C 140 ? 1.1653 0.7160 0.6010 -0.0701 -0.0078 0.0241 166 THR K OG1 5773 C CG2 . THR C 140 ? 1.1669 0.7537 0.6071 -0.0753 -0.0141 0.0286 166 THR K CG2 5774 N N . LEU C 141 ? 1.1450 0.6533 0.5711 -0.0869 -0.0028 0.0283 167 LEU K N 5775 C CA . LEU C 141 ? 1.1500 0.6363 0.5725 -0.0892 0.0021 0.0230 167 LEU K CA 5776 C C . LEU C 141 ? 1.1576 0.6315 0.5710 -0.0974 0.0021 0.0232 167 LEU K C 5777 O O . LEU C 141 ? 1.1593 0.6345 0.5743 -0.1025 -0.0005 0.0279 167 LEU K O 5778 C CB . LEU C 141 ? 1.1487 0.6288 0.5818 -0.0877 0.0046 0.0216 167 LEU K CB 5779 C CG . LEU C 141 ? 1.1464 0.6090 0.5811 -0.0876 0.0111 0.0129 167 LEU K CG 5780 C CD1 . LEU C 141 ? 1.1409 0.6049 0.5752 -0.0814 0.0143 0.0081 167 LEU K CD1 5781 C CD2 . LEU C 141 ? 1.1444 0.6006 0.5921 -0.0879 0.0109 0.0119 167 LEU K CD2 5782 N N . GLN C 142 ? 1.1631 0.6240 0.5661 -0.0996 0.0048 0.0182 168 GLN K N 5783 C CA . GLN C 142 ? 1.1707 0.6194 0.5623 -0.1080 0.0049 0.0176 168 GLN K CA 5784 C C . GLN C 142 ? 1.1720 0.6023 0.5609 -0.1129 0.0120 0.0099 168 GLN K C 5785 O O . GLN C 142 ? 1.1763 0.5982 0.5644 -0.1192 0.0134 0.0088 168 GLN K O 5786 C CB . GLN C 142 ? 1.1758 0.6239 0.5553 -0.1087 0.0009 0.0180 168 GLN K CB 5787 C CG . GLN C 142 ? 1.1800 0.6355 0.5559 -0.1123 -0.0055 0.0235 168 GLN K CG 5788 C CD . GLN C 142 ? 1.1768 0.6498 0.5563 -0.1058 -0.0122 0.0258 168 GLN K CD 5789 O OE1 . GLN C 142 ? 1.1819 0.6502 0.5542 -0.1046 -0.0163 0.0240 168 GLN K OE1 5790 N NE2 . GLN C 142 ? 1.1684 0.6618 0.5596 -0.1021 -0.0140 0.0292 168 GLN K NE2 5791 N N . VAL C 143 ? 1.1833 0.6076 0.5695 -0.1108 0.0165 0.0038 169 VAL K N 5792 C CA . VAL C 143 ? 1.1769 0.5863 0.5611 -0.1160 0.0247 -0.0058 169 VAL K CA 5793 C C . VAL C 143 ? 1.1656 0.5766 0.5644 -0.1101 0.0296 -0.0116 169 VAL K C 5794 O O . VAL C 143 ? 1.1610 0.5756 0.5598 -0.1050 0.0304 -0.0127 169 VAL K O 5795 C CB . VAL C 143 ? 1.1802 0.5792 0.5468 -0.1217 0.0268 -0.0096 169 VAL K CB 5796 C CG1 . VAL C 143 ? 1.1773 0.5631 0.5407 -0.1297 0.0363 -0.0206 169 VAL K CG1 5797 C CG2 . VAL C 143 ? 1.1909 0.5872 0.5427 -0.1273 0.0204 -0.0038 169 VAL K CG2 5798 N N . LEU C 144 ? 1.2432 0.6505 0.6549 -0.1108 0.0323 -0.0161 170 LEU K N 5799 C CA . LEU C 144 ? 1.2329 0.6406 0.6599 -0.1054 0.0363 -0.0228 170 LEU K CA 5800 C C . LEU C 144 ? 1.2239 0.6200 0.6534 -0.1116 0.0449 -0.0362 170 LEU K C 5801 O O . LEU C 144 ? 1.2251 0.6150 0.6591 -0.1162 0.0454 -0.0397 170 LEU K O 5802 C CB . LEU C 144 ? 1.2344 0.6485 0.6790 -0.0998 0.0305 -0.0177 170 LEU K CB 5803 C CG . LEU C 144 ? 1.2268 0.6389 0.6895 -0.0948 0.0336 -0.0259 170 LEU K CG 5804 C CD1 . LEU C 144 ? 1.2255 0.6454 0.6879 -0.0883 0.0347 -0.0251 170 LEU K CD1 5805 C CD2 . LEU C 144 ? 1.2298 0.6428 0.7090 -0.0917 0.0263 -0.0216 170 LEU K CD2 5806 N N . ASP C 145 ? 1.2013 0.5949 0.6279 -0.1125 0.0519 -0.0445 171 ASP K N 5807 C CA . ASP C 145 ? 1.1947 0.5805 0.6272 -0.1184 0.0612 -0.0595 171 ASP K CA 5808 C C . ASP C 145 ? 1.1840 0.5737 0.6349 -0.1120 0.0653 -0.0681 171 ASP K C 5809 O O . ASP C 145 ? 1.1798 0.5714 0.6249 -0.1112 0.0689 -0.0702 171 ASP K O 5810 C CB . ASP C 145 ? 1.1965 0.5742 0.6068 -0.1300 0.0679 -0.0652 171 ASP K CB 5811 C CG . ASP C 145 ? 1.1922 0.5640 0.6074 -0.1384 0.0782 -0.0817 171 ASP K CG 5812 O OD1 . ASP C 145 ? 1.1892 0.5622 0.6260 -0.1346 0.0787 -0.0884 171 ASP K OD1 5813 O OD2 . ASP C 145 ? 1.1932 0.5590 0.5910 -0.1495 0.0853 -0.0886 171 ASP K OD2 5814 N N . LEU C 146 ? 1.1375 0.5274 0.6109 -0.1077 0.0638 -0.0732 172 LEU K N 5815 C CA . LEU C 146 ? 1.1296 0.5223 0.6252 -0.1015 0.0665 -0.0830 172 LEU K CA 5816 C C . LEU C 146 ? 1.1319 0.5199 0.6384 -0.1077 0.0764 -0.1026 172 LEU K C 5817 O O . LEU C 146 ? 1.1262 0.5166 0.6557 -0.1026 0.0781 -0.1132 172 LEU K O 5818 C CB . LEU C 146 ? 1.1269 0.5228 0.6425 -0.0920 0.0558 -0.0753 172 LEU K CB 5819 C CG . LEU C 146 ? 1.1248 0.5287 0.6324 -0.0863 0.0468 -0.0579 172 LEU K CG 5820 C CD1 . LEU C 146 ? 1.1259 0.5311 0.6497 -0.0808 0.0360 -0.0502 172 LEU K CD1 5821 C CD2 . LEU C 146 ? 1.1171 0.5278 0.6215 -0.0814 0.0497 -0.0574 172 LEU K CD2 5822 N N . SER C 147 ? 1.2493 0.6312 0.7405 -0.1189 0.0822 -0.1080 173 SER K N 5823 C CA . SER C 147 ? 1.2458 0.6243 0.7472 -0.1263 0.0916 -0.1275 173 SER K CA 5824 C C . SER C 147 ? 1.2343 0.6169 0.7395 -0.1303 0.1034 -0.1436 173 SER K C 5825 O O . SER C 147 ? 1.2320 0.6168 0.7221 -0.1316 0.1058 -0.1390 173 SER K O 5826 C CB . SER C 147 ? 1.2550 0.6264 0.7352 -0.1389 0.0952 -0.1285 173 SER K CB 5827 O OG . SER C 147 ? 1.2587 0.6283 0.7101 -0.1478 0.0998 -0.1244 173 SER K OG 5828 N N . ASN C 148 ? 1.1665 0.5502 0.6925 -0.1328 0.1104 -0.1634 174 ASN K N 5829 C CA . ASN C 148 ? 1.1579 0.5478 0.6921 -0.1372 0.1225 -0.1820 174 ASN K CA 5830 C C . ASN C 148 ? 1.1473 0.5442 0.6963 -0.1262 0.1198 -0.1797 174 ASN K C 5831 O O . ASN C 148 ? 1.1430 0.5426 0.6766 -0.1295 0.1247 -0.1776 174 ASN K O 5832 C CB . ASN C 148 ? 1.1637 0.5515 0.6660 -0.1538 0.1336 -0.1858 174 ASN K CB 5833 C CG . ASN C 148 ? 1.1738 0.5582 0.6707 -0.1674 0.1419 -0.1998 174 ASN K CG 5834 O OD1 . ASN C 148 ? 1.1820 0.5721 0.6972 -0.1719 0.1518 -0.2221 174 ASN K OD1 5835 N ND2 . ASN C 148 ? 1.1752 0.5512 0.6477 -0.1741 0.1378 -0.1880 174 ASN K ND2 5836 N N . ASN C 149 ? 1.3276 0.7263 0.9063 -0.1136 0.1113 -0.1802 175 ASN K N 5837 C CA . ASN C 149 ? 1.3196 0.7245 0.9145 -0.1032 0.1080 -0.1789 175 ASN K CA 5838 C C . ASN C 149 ? 1.3149 0.7220 0.9488 -0.0946 0.1042 -0.1929 175 ASN K C 5839 O O . ASN C 149 ? 1.3163 0.7209 0.9657 -0.0973 0.1055 -0.2063 175 ASN K O 5840 C CB . ASN C 149 ? 1.3256 0.7296 0.9095 -0.0944 0.0956 -0.1550 175 ASN K CB 5841 C CG . ASN C 149 ? 1.3273 0.7315 0.8787 -0.0999 0.0989 -0.1437 175 ASN K CG 5842 O OD1 . ASN C 149 ? 1.3196 0.7282 0.8669 -0.0992 0.1031 -0.1452 175 ASN K OD1 5843 N ND2 . ASN C 149 ? 1.3378 0.7367 0.8666 -0.1054 0.0960 -0.1325 175 ASN K ND2 5844 N N . ARG C 150 ? 1.3015 0.7131 0.9521 -0.0843 0.0987 -0.1904 176 ARG K N 5845 C CA . ARG C 150 ? 1.2981 0.7107 0.9869 -0.0750 0.0923 -0.2023 176 ARG K CA 5846 C C . ARG C 150 ? 1.3100 0.7151 1.0084 -0.0653 0.0739 -0.1853 176 ARG K C 5847 O O . ARG C 150 ? 1.3106 0.7138 1.0396 -0.0569 0.0645 -0.1911 176 ARG K O 5848 C CB . ARG C 150 ? 1.2846 0.7062 0.9884 -0.0703 0.0966 -0.2112 176 ARG K CB 5849 C CG . ARG C 150 ? 1.2718 0.7018 0.9900 -0.0776 0.1120 -0.2387 176 ARG K CG 5850 C CD . ARG C 150 ? 1.2646 0.6980 1.0275 -0.0679 0.1064 -0.2558 176 ARG K CD 5851 N NE . ARG C 150 ? 1.2509 0.6945 1.0332 -0.0747 0.1209 -0.2854 176 ARG K NE 5852 C CZ . ARG C 150 ? 1.2494 0.6930 1.0478 -0.0792 0.1247 -0.3039 176 ARG K CZ 5853 N NH1 . ARG C 150 ? 1.2622 0.6945 1.0590 -0.0775 0.1147 -0.2951 176 ARG K NH1 5854 N NH2 . ARG C 150 ? 1.2347 0.6906 1.0513 -0.0860 0.1391 -0.3324 176 ARG K NH2 5855 N N . LEU C 151 ? 1.1152 0.5159 0.7873 -0.0674 0.0684 -0.1648 177 LEU K N 5856 C CA . LEU C 151 ? 1.1244 0.5203 0.7988 -0.0601 0.0516 -0.1455 177 LEU K CA 5857 C C . LEU C 151 ? 1.1321 0.5197 0.8356 -0.0553 0.0394 -0.1507 177 LEU K C 5858 O O . LEU C 151 ? 1.1361 0.5184 0.8473 -0.0596 0.0414 -0.1619 177 LEU K O 5859 C CB . LEU C 151 ? 1.1336 0.5270 0.7776 -0.0654 0.0490 -0.1270 177 LEU K CB 5860 C CG . LEU C 151 ? 1.1282 0.5285 0.7443 -0.0673 0.0545 -0.1157 177 LEU K CG 5861 C CD1 . LEU C 151 ? 1.1375 0.5369 0.7316 -0.0693 0.0474 -0.0963 177 LEU K CD1 5862 C CD2 . LEU C 151 ? 1.1214 0.5283 0.7463 -0.0592 0.0521 -0.1131 177 LEU K CD2 5863 N N . SER C 152 ? 1.3209 0.7067 1.0403 -0.0466 0.0260 -0.1426 178 SER K N 5864 C CA . SER C 152 ? 1.3305 0.7058 1.0764 -0.0416 0.0098 -0.1434 178 SER K CA 5865 C C . SER C 152 ? 1.3454 0.7150 1.0741 -0.0424 -0.0043 -0.1187 178 SER K C 5866 O O . SER C 152 ? 1.3465 0.7227 1.0543 -0.0425 -0.0041 -0.1031 178 SER K O 5867 C CB . SER C 152 ? 1.3250 0.7011 1.1020 -0.0323 0.0027 -0.1520 178 SER K CB 5868 O OG . SER C 152 ? 1.3119 0.6967 1.1040 -0.0320 0.0170 -0.1749 178 SER K OG 5869 N N . GLY C 153 ? 1.1885 0.5465 0.9254 -0.0438 -0.0162 -0.1154 179 GLY K N 5870 C CA . GLY C 153 ? 1.1996 0.5530 0.9206 -0.0458 -0.0301 -0.0921 179 GLY K CA 5871 C C . GLY C 153 ? 1.2113 0.5549 0.9244 -0.0522 -0.0369 -0.0853 179 GLY K C 5872 O O . GLY C 153 ? 1.2138 0.5494 0.9418 -0.0534 -0.0366 -0.0990 179 GLY K O 5873 N N . SER C 154 ? 1.2452 0.5904 0.9351 -0.0566 -0.0434 -0.0642 180 SER K N 5874 C CA . SER C 154 ? 1.2564 0.5939 0.9350 -0.0637 -0.0503 -0.0546 180 SER K CA 5875 C C . SER C 154 ? 1.2566 0.6060 0.9030 -0.0695 -0.0406 -0.0430 180 SER K C 5876 O O . SER C 154 ? 1.2554 0.6161 0.8892 -0.0680 -0.0382 -0.0339 180 SER K O 5877 C CB . SER C 154 ? 1.2672 0.5946 0.9511 -0.0646 -0.0715 -0.0389 180 SER K CB 5878 O OG . SER C 154 ? 1.2663 0.5874 0.9359 -0.0728 -0.0778 -0.0280 180 SER K OG 5879 N N . VAL C 155 ? 1.2235 0.5705 0.8576 -0.0760 -0.0357 -0.0439 181 VAL K N 5880 C CA . VAL C 155 ? 1.2227 0.5808 0.8283 -0.0811 -0.0266 -0.0350 181 VAL K CA 5881 C C . VAL C 155 ? 1.2343 0.5938 0.8242 -0.0868 -0.0372 -0.0154 181 VAL K C 5882 O O . VAL C 155 ? 1.2433 0.5922 0.8365 -0.0914 -0.0465 -0.0118 181 VAL K O 5883 C CB . VAL C 155 ? 1.2200 0.5761 0.8176 -0.0862 -0.0144 -0.0465 181 VAL K CB 5884 C CG1 . VAL C 155 ? 1.2209 0.5869 0.7896 -0.0915 -0.0076 -0.0362 181 VAL K CG1 5885 C CG2 . VAL C 155 ? 1.2087 0.5657 0.8191 -0.0828 -0.0021 -0.0667 181 VAL K CG2 5886 N N . PRO C 156 ? 1.2037 0.5772 0.7769 -0.0870 -0.0356 -0.0035 182 PRO K N 5887 C CA . PRO C 156 ? 1.2128 0.5931 0.7683 -0.0937 -0.0426 0.0138 182 PRO K CA 5888 C C . PRO C 156 ? 1.2162 0.5960 0.7568 -0.1009 -0.0386 0.0153 182 PRO K C 5889 O O . PRO C 156 ? 1.2099 0.5924 0.7426 -0.1009 -0.0267 0.0070 182 PRO K O 5890 C CB . PRO C 156 ? 1.2089 0.6071 0.7521 -0.0908 -0.0368 0.0194 182 PRO K CB 5891 C CG . PRO C 156 ? 1.1979 0.5971 0.7468 -0.0841 -0.0250 0.0054 182 PRO K CG 5892 C CD . PRO C 156 ? 1.1944 0.5791 0.7660 -0.0809 -0.0271 -0.0072 182 PRO K CD 5893 N N . ASP C 157 ? 1.4734 0.8482 1.0102 -0.1080 -0.0494 0.0259 183 ASP K N 5894 C CA . ASP C 157 ? 1.4778 0.8558 0.9976 -0.1156 -0.0470 0.0310 183 ASP K CA 5895 C C . ASP C 157 ? 1.4836 0.8786 0.9854 -0.1211 -0.0495 0.0460 183 ASP K C 5896 O O . ASP C 157 ? 1.4860 0.8860 0.9744 -0.1269 -0.0468 0.0494 183 ASP K O 5897 C CB . ASP C 157 ? 1.4836 0.8446 1.0103 -0.1209 -0.0550 0.0298 183 ASP K CB 5898 C CG . ASP C 157 ? 1.4890 0.8361 1.0342 -0.1196 -0.0696 0.0318 183 ASP K CG 5899 O OD1 . ASP C 157 ? 1.4853 0.8337 1.0421 -0.1129 -0.0711 0.0292 183 ASP K OD1 5900 O OD2 . ASP C 157 ? 1.4970 0.8310 1.0454 -0.1254 -0.0806 0.0361 183 ASP K OD2 5901 N N . ASN C 158 ? 1.4747 0.8797 0.9765 -0.1198 -0.0543 0.0539 184 ASN K N 5902 C CA . ASN C 158 ? 1.4795 0.9029 0.9655 -0.1262 -0.0564 0.0665 184 ASN K CA 5903 C C . ASN C 158 ? 1.4737 0.9164 0.9508 -0.1215 -0.0455 0.0636 184 ASN K C 5904 O O . ASN C 158 ? 1.4661 0.9071 0.9477 -0.1135 -0.0370 0.0534 184 ASN K O 5905 C CB . ASN C 158 ? 1.4872 0.9124 0.9741 -0.1314 -0.0691 0.0786 184 ASN K CB 5906 C CG . ASN C 158 ? 1.4849 0.9110 0.9822 -0.1237 -0.0698 0.0760 184 ASN K CG 5907 O OD1 . ASN C 158 ? 1.4745 0.9031 0.9772 -0.1143 -0.0599 0.0655 184 ASN K OD1 5908 N ND2 . ASN C 158 ? 1.4947 0.9176 0.9938 -0.1286 -0.0826 0.0861 184 ASN K ND2 5909 N N . GLY C 159 ? 1.2795 0.7410 0.7445 -0.1269 -0.0463 0.0721 185 GLY K N 5910 C CA . GLY C 159 ? 1.2740 0.7542 0.7320 -0.1225 -0.0377 0.0689 185 GLY K CA 5911 C C . GLY C 159 ? 1.2704 0.7457 0.7242 -0.1195 -0.0295 0.0604 185 GLY K C 5912 O O . GLY C 159 ? 1.2729 0.7391 0.7228 -0.1249 -0.0304 0.0606 185 GLY K O 5913 N N . SER C 160 ? 1.1670 0.6472 0.6205 -0.1118 -0.0221 0.0532 186 SER K N 5914 C CA . SER C 160 ? 1.1654 0.6403 0.6126 -0.1101 -0.0152 0.0457 186 SER K CA 5915 C C . SER C 160 ? 1.1696 0.6228 0.6210 -0.1114 -0.0128 0.0386 186 SER K C 5916 O O . SER C 160 ? 1.1732 0.6192 0.6172 -0.1155 -0.0100 0.0355 186 SER K O 5917 C CB . SER C 160 ? 1.1580 0.6393 0.6049 -0.1020 -0.0094 0.0398 186 SER K CB 5918 O OG . SER C 160 ? 1.1536 0.6349 0.6106 -0.0967 -0.0099 0.0387 186 SER K OG 5919 N N . PHE C 161 ? 1.2275 0.6710 0.6918 -0.1084 -0.0145 0.0354 187 PHE K N 5920 C CA . PHE C 161 ? 1.2242 0.6489 0.6971 -0.1091 -0.0128 0.0266 187 PHE K CA 5921 C C . PHE C 161 ? 1.2299 0.6453 0.7006 -0.1171 -0.0179 0.0299 187 PHE K C 5922 O O . PHE C 161 ? 1.2285 0.6288 0.7060 -0.1184 -0.0161 0.0210 187 PHE K O 5923 C CB . PHE C 161 ? 1.2204 0.6386 0.7107 -0.1039 -0.0162 0.0233 187 PHE K CB 5924 C CG . PHE C 161 ? 1.2113 0.6330 0.7058 -0.0964 -0.0090 0.0154 187 PHE K CG 5925 C CD1 . PHE C 161 ? 1.2119 0.6489 0.6983 -0.0930 -0.0069 0.0199 187 PHE K CD1 5926 C CD2 . PHE C 161 ? 1.2017 0.6122 0.7093 -0.0929 -0.0043 0.0026 187 PHE K CD2 5927 C CE1 . PHE C 161 ? 1.2036 0.6429 0.6934 -0.0863 -0.0008 0.0130 187 PHE K CE1 5928 C CE2 . PHE C 161 ? 1.1919 0.6060 0.7029 -0.0869 0.0025 -0.0046 187 PHE K CE2 5929 C CZ . PHE C 161 ? 1.1927 0.6205 0.6941 -0.0837 0.0040 0.0012 187 PHE K CZ 5930 N N . SER C 162 ? 1.2791 0.7041 0.7414 -0.1228 -0.0242 0.0415 188 SER K N 5931 C CA . SER C 162 ? 1.2842 0.7022 0.7409 -0.1311 -0.0283 0.0453 188 SER K CA 5932 C C . SER C 162 ? 1.2810 0.6915 0.7301 -0.1328 -0.0203 0.0365 188 SER K C 5933 O O . SER C 162 ? 1.2820 0.6780 0.7340 -0.1368 -0.0210 0.0318 188 SER K O 5934 C CB . SER C 162 ? 1.2890 0.7233 0.7349 -0.1374 -0.0336 0.0578 188 SER K CB 5935 O OG . SER C 162 ? 1.2849 0.7339 0.7204 -0.1359 -0.0276 0.0569 188 SER K OG 5936 N N . LEU C 163 ? 1.4413 0.8607 0.8808 -0.1300 -0.0134 0.0338 189 LEU K N 5937 C CA . LEU C 163 ? 1.4400 0.8528 0.8681 -0.1339 -0.0076 0.0279 189 LEU K CA 5938 C C . LEU C 163 ? 1.4331 0.8317 0.8641 -0.1329 0.0007 0.0142 189 LEU K C 5939 O O . LEU C 163 ? 1.4303 0.8224 0.8501 -0.1378 0.0056 0.0091 189 LEU K O 5940 C CB . LEU C 163 ? 1.4399 0.8666 0.8552 -0.1331 -0.0063 0.0317 189 LEU K CB 5941 C CG . LEU C 163 ? 1.4395 0.8742 0.8537 -0.1258 -0.0022 0.0286 189 LEU K CG 5942 C CD1 . LEU C 163 ? 1.4430 0.8732 0.8435 -0.1278 0.0017 0.0242 189 LEU K CD1 5943 C CD2 . LEU C 163 ? 1.4375 0.8927 0.8538 -0.1221 -0.0069 0.0367 189 LEU K CD2 5944 N N . PHE C 164 ? 1.2311 0.6250 0.6769 -0.1277 0.0021 0.0077 190 PHE K N 5945 C CA . PHE C 164 ? 1.2224 0.6075 0.6710 -0.1268 0.0115 -0.0065 190 PHE K CA 5946 C C . PHE C 164 ? 1.2223 0.5929 0.6808 -0.1307 0.0140 -0.0182 190 PHE K C 5947 O O . PHE C 164 ? 1.2242 0.5896 0.7008 -0.1278 0.0089 -0.0206 190 PHE K O 5948 C CB . PHE C 164 ? 1.2146 0.6049 0.6739 -0.1186 0.0137 -0.0099 190 PHE K CB 5949 C CG . PHE C 164 ? 1.2157 0.6195 0.6652 -0.1146 0.0135 -0.0024 190 PHE K CG 5950 C CD1 . PHE C 164 ? 1.2168 0.6253 0.6489 -0.1182 0.0139 0.0023 190 PHE K CD1 5951 C CD2 . PHE C 164 ? 1.2162 0.6280 0.6749 -0.1071 0.0121 -0.0007 190 PHE K CD2 5952 C CE1 . PHE C 164 ? 1.2187 0.6399 0.6447 -0.1137 0.0127 0.0076 190 PHE K CE1 5953 C CE2 . PHE C 164 ? 1.2180 0.6427 0.6689 -0.1032 0.0118 0.0050 190 PHE K CE2 5954 C CZ . PHE C 164 ? 1.2194 0.6490 0.6548 -0.1062 0.0120 0.0086 190 PHE K CZ 5955 N N . THR C 165 ? 1.3080 0.6719 0.7549 -0.1376 0.0213 -0.0263 191 THR K N 5956 C CA . THR C 165 ? 1.3067 0.6587 0.7627 -0.1419 0.0261 -0.0409 191 THR K CA 5957 C C . THR C 165 ? 1.2938 0.6453 0.7650 -0.1371 0.0332 -0.0551 191 THR K C 5958 O O . THR C 165 ? 1.2848 0.6436 0.7522 -0.1331 0.0367 -0.0538 191 THR K O 5959 C CB . THR C 165 ? 1.3107 0.6570 0.7471 -0.1522 0.0332 -0.0463 191 THR K CB 5960 O OG1 . THR C 165 ? 1.3003 0.6500 0.7227 -0.1536 0.0409 -0.0494 191 THR K OG1 5961 C CG2 . THR C 165 ? 1.3238 0.6710 0.7455 -0.1571 0.0262 -0.0329 191 THR K CG2 5962 N N . PRO C 166 ? 1.1972 0.5407 0.6869 -0.1377 0.0353 -0.0696 192 PRO K N 5963 C CA . PRO C 166 ? 1.1920 0.5355 0.7007 -0.1337 0.0420 -0.0862 192 PRO K CA 5964 C C . PRO C 166 ? 1.1881 0.5357 0.6839 -0.1380 0.0552 -0.0958 192 PRO K C 5965 O O . PRO C 166 ? 1.1821 0.5333 0.6916 -0.1338 0.0604 -0.1064 192 PRO K O 5966 C CB . PRO C 166 ? 1.2000 0.5342 0.7255 -0.1370 0.0427 -0.1015 192 PRO K CB 5967 C CG . PRO C 166 ? 1.2095 0.5382 0.7181 -0.1450 0.0396 -0.0937 192 PRO K CG 5968 C CD . PRO C 166 ? 1.2071 0.5411 0.7030 -0.1420 0.0300 -0.0716 192 PRO K CD 5969 N N . ILE C 167 ? 1.2037 0.5501 0.6733 -0.1471 0.0598 -0.0920 193 ILE K N 5970 C CA . ILE C 167 ? 1.1997 0.5473 0.6541 -0.1538 0.0712 -0.1008 193 ILE K CA 5971 C C . ILE C 167 ? 1.1928 0.5483 0.6464 -0.1459 0.0702 -0.0936 193 ILE K C 5972 O O . ILE C 167 ? 1.1867 0.5440 0.6347 -0.1489 0.0787 -0.1019 193 ILE K O 5973 C CB . ILE C 167 ? 1.2083 0.5506 0.6330 -0.1660 0.0738 -0.0966 193 ILE K CB 5974 C CG1 . ILE C 167 ? 1.2111 0.5510 0.6216 -0.1774 0.0867 -0.1107 193 ILE K CG1 5975 C CG2 . ILE C 167 ? 1.2125 0.5584 0.6202 -0.1630 0.0651 -0.0767 193 ILE K CG2 5976 C CD1 . ILE C 167 ? 1.2223 0.5552 0.6006 -0.1910 0.0881 -0.1059 193 ILE K CD1 5977 N N . SER C 168 ? 1.2111 0.5717 0.6709 -0.1366 0.0596 -0.0788 194 SER K N 5978 C CA . SER C 168 ? 1.2060 0.5751 0.6673 -0.1281 0.0572 -0.0714 194 SER K CA 5979 C C . SER C 168 ? 1.1969 0.5683 0.6821 -0.1212 0.0600 -0.0824 194 SER K C 5980 O O . SER C 168 ? 1.1893 0.5653 0.6734 -0.1188 0.0648 -0.0856 194 SER K O 5981 C CB . SER C 168 ? 1.2141 0.5895 0.6754 -0.1218 0.0454 -0.0536 194 SER K CB 5982 O OG . SER C 168 ? 1.2224 0.5971 0.6652 -0.1276 0.0418 -0.0440 194 SER K OG 5983 N N . PHE C 169 ? 1.2405 0.6084 0.7483 -0.1178 0.0555 -0.0876 195 PHE K N 5984 C CA . PHE C 169 ? 1.2327 0.6022 0.7671 -0.1101 0.0552 -0.0976 195 PHE K CA 5985 C C . PHE C 169 ? 1.2259 0.5921 0.7759 -0.1141 0.0649 -0.1204 195 PHE K C 5986 O O . PHE C 169 ? 1.2206 0.5877 0.7972 -0.1074 0.0634 -0.1307 195 PHE K O 5987 C CB . PHE C 169 ? 1.2395 0.6072 0.7916 -0.1026 0.0411 -0.0879 195 PHE K CB 5988 C CG . PHE C 169 ? 1.2490 0.6208 0.7850 -0.1018 0.0322 -0.0671 195 PHE K CG 5989 C CD1 . PHE C 169 ? 1.2481 0.6294 0.7782 -0.0964 0.0302 -0.0570 195 PHE K CD1 5990 C CD2 . PHE C 169 ? 1.2589 0.6264 0.7860 -0.1070 0.0264 -0.0587 195 PHE K CD2 5991 C CE1 . PHE C 169 ? 1.2573 0.6449 0.7741 -0.0962 0.0229 -0.0401 195 PHE K CE1 5992 C CE2 . PHE C 169 ? 1.2674 0.6411 0.7807 -0.1071 0.0191 -0.0413 195 PHE K CE2 5993 C CZ . PHE C 169 ? 1.2668 0.6513 0.7755 -0.1018 0.0176 -0.0325 195 PHE K CZ 5994 N N . ALA C 170 ? 1.1954 0.5583 0.7302 -0.1252 0.0742 -0.1290 196 ALA K N 5995 C CA . ALA C 170 ? 1.1918 0.5525 0.7420 -0.1306 0.0833 -0.1521 196 ALA K CA 5996 C C . ALA C 170 ? 1.1792 0.5470 0.7443 -0.1300 0.0939 -0.1707 196 ALA K C 5997 O O . ALA C 170 ? 1.1730 0.5461 0.7250 -0.1308 0.0990 -0.1674 196 ALA K O 5998 C CB . ALA C 170 ? 1.1979 0.5537 0.7259 -0.1445 0.0908 -0.1567 196 ALA K CB 5999 N N . ASN C 171 ? 1.3783 0.7463 0.9714 -0.1291 0.0969 -0.1911 197 ASN K N 6000 C CA . ASN C 171 ? 1.3648 0.7411 0.9760 -0.1294 0.1077 -0.2125 197 ASN K CA 6001 C C . ASN C 171 ? 1.3554 0.7378 0.9816 -0.1181 0.1035 -0.2085 197 ASN K C 6002 O O . ASN C 171 ? 1.3472 0.7355 0.9590 -0.1207 0.1109 -0.2070 197 ASN K O 6003 C CB . ASN C 171 ? 1.3601 0.7404 0.9457 -0.1448 0.1242 -0.2224 197 ASN K CB 6004 C CG . ASN C 171 ? 1.3469 0.7374 0.9501 -0.1475 0.1367 -0.2459 197 ASN K CG 6005 O OD1 . ASN C 171 ? 1.3399 0.7361 0.9345 -0.1478 0.1413 -0.2435 197 ASN K OD1 6006 N ND2 . ASN C 171 ? 1.3426 0.7364 0.9726 -0.1491 0.1418 -0.2696 197 ASN K ND2 6007 N N . ASN C 172 ? 1.5199 0.8997 1.1745 -0.1058 0.0905 -0.2062 198 ASN K N 6008 C CA . ASN C 172 ? 1.5131 0.8978 1.1851 -0.0950 0.0854 -0.2039 198 ASN K CA 6009 C C . ASN C 172 ? 1.5085 0.8937 1.2226 -0.0869 0.0805 -0.2222 198 ASN K C 6010 O O . ASN C 172 ? 1.5085 0.8911 1.2407 -0.0895 0.0822 -0.2395 198 ASN K O 6011 C CB . ASN C 172 ? 1.5217 0.9027 1.1839 -0.0872 0.0706 -0.1775 198 ASN K CB 6012 C CG . ASN C 172 ? 1.5225 0.9065 1.1487 -0.0921 0.0747 -0.1609 198 ASN K CG 6013 O OD1 . ASN C 172 ? 1.5165 0.9065 1.1370 -0.0882 0.0758 -0.1549 198 ASN K OD1 6014 N ND2 . ASN C 172 ? 1.5298 0.9093 1.1325 -0.1004 0.0763 -0.1539 198 ASN K ND2 6015 N N . LEU C 173 ? 1.4677 0.8558 1.1982 -0.0766 0.0730 -0.2179 199 LEU K N 6016 C CA . LEU C 173 ? 1.4651 0.8515 1.2365 -0.0664 0.0632 -0.2303 199 LEU K CA 6017 C C . LEU C 173 ? 1.4807 0.8534 1.2582 -0.0618 0.0444 -0.2160 199 LEU K C 6018 O O . LEU C 173 ? 1.4892 0.8562 1.2430 -0.0682 0.0436 -0.2040 199 LEU K O 6019 C CB . LEU C 173 ? 1.4590 0.8512 1.2399 -0.0578 0.0594 -0.2254 199 LEU K CB 6020 C CG . LEU C 173 ? 1.4487 0.8441 1.2725 -0.0487 0.0547 -0.2445 199 LEU K CG 6021 C CD1 . LEU C 173 ? 1.4345 0.8408 1.2734 -0.0550 0.0722 -0.2746 199 LEU K CD1 6022 C CD2 . LEU C 173 ? 1.4482 0.8482 1.2732 -0.0413 0.0503 -0.2344 199 LEU K CD2 6023 N N . ASP C 174 ? 1.5436 0.9102 1.3531 -0.0518 0.0288 -0.2180 200 ASP K N 6024 C CA . ASP C 174 ? 1.5616 0.9137 1.3738 -0.0492 0.0098 -0.2026 200 ASP K CA 6025 C C . ASP C 174 ? 1.5702 0.9210 1.3459 -0.0523 0.0053 -0.1732 200 ASP K C 6026 O O . ASP C 174 ? 1.5671 0.9233 1.3332 -0.0488 0.0037 -0.1607 200 ASP K O 6027 C CB . ASP C 174 ? 1.5660 0.9101 1.4146 -0.0382 -0.0092 -0.2052 200 ASP K CB 6028 C CG . ASP C 174 ? 1.5817 0.9083 1.4381 -0.0372 -0.0298 -0.1942 200 ASP K CG 6029 O OD1 . ASP C 174 ? 1.5861 0.9062 1.4230 -0.0379 -0.0421 -0.1687 200 ASP K OD1 6030 O OD2 . ASP C 174 ? 1.5881 0.9076 1.4699 -0.0363 -0.0336 -0.2117 200 ASP K OD2 6031 N N . LEU C 175 ? 1.2800 0.6244 1.0368 -0.0591 0.0036 -0.1639 201 LEU K N 6032 C CA . LEU C 175 ? 1.2888 0.6320 1.0144 -0.0627 -0.0020 -0.1379 201 LEU K CA 6033 C C . LEU C 175 ? 1.3026 0.6322 1.0321 -0.0653 -0.0156 -0.1315 201 LEU K C 6034 O O . LEU C 175 ? 1.3039 0.6287 1.0408 -0.0691 -0.0113 -0.1457 201 LEU K O 6035 C CB . LEU C 175 ? 1.2837 0.6357 0.9758 -0.0711 0.0145 -0.1349 201 LEU K CB 6036 C CG . LEU C 175 ? 1.2769 0.6398 0.9453 -0.0709 0.0211 -0.1228 201 LEU K CG 6037 C CD1 . LEU C 175 ? 1.2772 0.6433 0.9126 -0.0798 0.0304 -0.1155 201 LEU K CD1 6038 C CD2 . LEU C 175 ? 1.2843 0.6478 0.9508 -0.0652 0.0072 -0.1029 201 LEU K CD2 6039 N N . CYS C 176 ? 1.5649 0.8881 1.2889 -0.0642 -0.0321 -0.1107 202 CYS K N 6040 C CA . CYS C 176 ? 1.5776 0.8864 1.3053 -0.0675 -0.0465 -0.1041 202 CYS K CA 6041 C C . CYS C 176 ? 1.5872 0.8970 1.2831 -0.0749 -0.0506 -0.0804 202 CYS K C 6042 O O . CYS C 176 ? 1.5875 0.9061 1.2661 -0.0749 -0.0510 -0.0650 202 CYS K O 6043 C CB . CYS C 176 ? 1.5810 0.8767 1.3389 -0.0608 -0.0671 -0.1042 202 CYS K CB 6044 S SG . CYS C 176 ? 1.5874 0.8800 1.3329 -0.0608 -0.0858 -0.0758 202 CYS K SG 6045 N N . GLY C 177 ? 1.5911 0.8930 1.2798 -0.0814 -0.0531 -0.0787 203 GLY K N 6046 C CA . GLY C 177 ? 1.6006 0.9033 1.2621 -0.0889 -0.0585 -0.0570 203 GLY K CA 6047 C C . GLY C 177 ? 1.6061 0.9036 1.2557 -0.0969 -0.0552 -0.0583 203 GLY K C 6048 O O . GLY C 177 ? 1.6012 0.8961 1.2599 -0.0974 -0.0458 -0.0767 203 GLY K O 6049 N N . PRO C 178 ? 1.6812 0.9780 1.3106 -0.1038 -0.0630 -0.0392 204 PRO K N 6050 C CA . PRO C 178 ? 1.6866 0.9802 1.3003 -0.1123 -0.0605 -0.0365 204 PRO K CA 6051 C C . PRO C 178 ? 1.6777 0.9845 1.2687 -0.1157 -0.0424 -0.0393 204 PRO K C 6052 O O . PRO C 178 ? 1.6772 0.9813 1.2574 -0.1221 -0.0369 -0.0428 204 PRO K O 6053 C CB . PRO C 178 ? 1.6990 0.9918 1.2978 -0.1183 -0.0745 -0.0135 204 PRO K CB 6054 C CG . PRO C 178 ? 1.6961 1.0010 1.2896 -0.1145 -0.0749 -0.0037 204 PRO K CG 6055 C CD . PRO C 178 ? 1.6879 0.9896 1.3064 -0.1048 -0.0736 -0.0185 204 PRO K CD 6056 N N . VAL C 179 ? 1.6306 0.9506 1.2138 -0.1118 -0.0345 -0.0371 205 VAL K N 6057 C CA . VAL C 179 ? 1.6218 0.9528 1.1855 -0.1141 -0.0187 -0.0407 205 VAL K CA 6058 C C . VAL C 179 ? 1.6127 0.9402 1.1880 -0.1134 -0.0067 -0.0631 205 VAL K C 6059 O O . VAL C 179 ? 1.6050 0.9373 1.1646 -0.1179 0.0062 -0.0693 205 VAL K O 6060 C CB . VAL C 179 ? 1.6166 0.9616 1.1711 -0.1096 -0.0155 -0.0324 205 VAL K CB 6061 N N . THR C 180 ? 1.4645 0.7834 1.0676 -0.1085 -0.0119 -0.0755 206 THR K N 6062 C CA . THR C 180 ? 1.4559 0.7734 1.0767 -0.1072 -0.0015 -0.0995 206 THR K CA 6063 C C . THR C 180 ? 1.4630 0.7672 1.1053 -0.1081 -0.0084 -0.1117 206 THR K C 6064 O O . THR C 180 ? 1.4745 0.7697 1.1129 -0.1113 -0.0200 -0.1005 206 THR K O 6065 C CB . THR C 180 ? 1.4466 0.7690 1.0877 -0.0982 -0.0007 -0.1075 206 THR K CB 6066 O OG1 . THR C 180 ? 1.4522 0.7642 1.1242 -0.0920 -0.0146 -0.1131 206 THR K OG1 6067 C CG2 . THR C 180 ? 1.4444 0.7760 1.0706 -0.0949 -0.0035 -0.0892 206 THR K CG2 6068 N N . SER C 181 ? 1.9644 1.2681 1.6294 -0.1059 -0.0010 -0.1356 207 SER K N 6069 C CA . SER C 181 ? 1.9701 1.2623 1.6606 -0.1055 -0.0073 -0.1511 207 SER K CA 6070 C C . SER C 181 ? 1.9759 1.2569 1.6975 -0.0964 -0.0272 -0.1497 207 SER K C 6071 O O . SER C 181 ? 1.9867 1.2539 1.7164 -0.0974 -0.0416 -0.1453 207 SER K O 6072 C CB . SER C 181 ? 1.9598 1.2580 1.6641 -0.1075 0.0091 -0.1799 207 SER K CB 6073 O OG . SER C 181 ? 1.9460 1.2529 1.6677 -0.1005 0.0140 -0.1905 207 SER K OG 6074 N N . ARG C 182 ? 1.7777 1.0637 1.5158 -0.0881 -0.0290 -0.1527 208 ARG K N 6075 C CA . ARG C 182 ? 1.7827 1.0580 1.5560 -0.0790 -0.0468 -0.1576 208 ARG K CA 6076 C C . ARG C 182 ? 1.7862 1.0577 1.5554 -0.0749 -0.0634 -0.1342 208 ARG K C 6077 O O . ARG C 182 ? 1.7783 1.0605 1.5417 -0.0714 -0.0582 -0.1294 208 ARG K O 6078 C CB . ARG C 182 ? 1.7715 1.0546 1.5748 -0.0723 -0.0375 -0.1844 208 ARG K CB 6079 C CG . ARG C 182 ? 1.7512 1.0526 1.5365 -0.0752 -0.0154 -0.1902 208 ARG K CG 6080 C CD . ARG C 182 ? 1.7415 1.0509 1.5446 -0.0774 0.0012 -0.2215 208 ARG K CD 6081 N NE . ARG C 182 ? 1.7461 1.0489 1.5484 -0.0845 0.0037 -0.2317 208 ARG K NE 6082 C CZ . ARG C 182 ? 1.7383 1.0455 1.5604 -0.0871 0.0147 -0.2605 208 ARG K CZ 6083 N NH1 . ARG C 182 ? 1.7236 1.0426 1.5688 -0.0836 0.0246 -0.2829 208 ARG K NH1 6084 N NH2 . ARG C 182 ? 1.7416 1.0424 1.5608 -0.0939 0.0160 -0.2677 208 ARG K NH2 6085 N N . PRO C 183 ? 1.6551 0.9109 1.4266 -0.0764 -0.0839 -0.1197 209 PRO K N 6086 C CA . PRO C 183 ? 1.6597 0.9091 1.4281 -0.0748 -0.1027 -0.0975 209 PRO K CA 6087 C C . PRO C 183 ? 1.6526 0.8981 1.4517 -0.0647 -0.1137 -0.1046 209 PRO K C 6088 O O . PRO C 183 ? 1.6405 0.8885 1.4678 -0.0578 -0.1073 -0.1285 209 PRO K O 6089 C CB . PRO C 183 ? 1.6727 0.9036 1.4404 -0.0804 -0.1214 -0.0864 209 PRO K CB 6090 C CG . PRO C 183 ? 1.6755 0.9100 1.4269 -0.0876 -0.1073 -0.0925 209 PRO K CG 6091 C CD . PRO C 183 ? 1.6650 0.9101 1.4306 -0.0834 -0.0877 -0.1193 209 PRO K CD 6092 N N . CYS C 184 ? 1.8231 1.0628 1.6167 -0.0647 -0.1306 -0.0840 210 CYS K N 6093 C CA . CYS C 184 ? 1.8143 1.0539 1.6283 -0.0563 -0.1389 -0.0859 210 CYS K CA 6094 C C . CYS C 184 ? 1.8239 1.0457 1.6412 -0.0580 -0.1668 -0.0662 210 CYS K C 6095 O O . CYS C 184 ? 1.8412 1.0521 1.6432 -0.0666 -0.1782 -0.0509 210 CYS K O 6096 C CB . CYS C 184 ? 1.8073 1.0679 1.6001 -0.0556 -0.1212 -0.0809 210 CYS K CB 6097 S SG . CYS C 184 ? 1.8178 1.0888 1.5636 -0.0660 -0.1173 -0.0522 210 CYS K SG 6098 N N . PRO C 185 ? 1.6062 0.8245 1.4430 -0.0510 -0.1785 -0.0664 211 PRO K N 6099 C CA . PRO C 185 ? 1.6121 0.8133 1.4509 -0.0534 -0.2057 -0.0472 211 PRO K CA 6100 C C . PRO C 185 ? 1.6265 0.8242 1.4290 -0.0668 -0.2145 -0.0189 211 PRO K C 6101 O O . PRO C 185 ? 1.6421 0.8208 1.4471 -0.0716 -0.2396 -0.0045 211 PRO K O 6102 C CB . PRO C 185 ? 1.6041 0.8157 1.4481 -0.0469 -0.2036 -0.0466 211 PRO K CB 6103 C CG . PRO C 185 ? 1.5866 0.8172 1.4420 -0.0389 -0.1775 -0.0710 211 PRO K CG 6104 C CD . PRO C 185 ? 1.5904 0.8188 1.4529 -0.0402 -0.1682 -0.0875 211 PRO K CD 6105 C C1 . NAG D . ? 1.8983 0.7337 1.1773 -0.0043 -0.5746 -0.0213 701 NAG B C1 6106 C C2 . NAG D . ? 1.8963 0.7361 1.1920 0.0063 -0.5809 -0.0285 701 NAG B C2 6107 C C3 . NAG D . ? 1.9286 0.7427 1.1871 -0.0188 -0.5854 -0.0138 701 NAG B C3 6108 C C4 . NAG D . ? 1.9325 0.7379 1.1488 -0.0468 -0.5601 -0.0012 701 NAG B C4 6109 C C5 . NAG D . ? 1.9313 0.7361 1.1365 -0.0540 -0.5540 0.0036 701 NAG B C5 6110 C C6 . NAG D . ? 1.9211 0.7288 1.0955 -0.0755 -0.5208 0.0096 701 NAG B C6 6111 C C7 . NAG D . ? 1.8752 0.7456 1.2480 0.0540 -0.6088 -0.0568 701 NAG B C7 6112 C C8 . NAG D . ? 1.8812 0.7575 1.2874 0.0722 -0.6354 -0.0664 701 NAG B C8 6113 N N2 . NAG D . ? 1.9069 0.7478 1.2355 0.0258 -0.6121 -0.0373 701 NAG B N2 6114 O O3 . NAG D . ? 1.9136 0.7391 1.1883 -0.0080 -0.5791 -0.0227 701 NAG B O3 6115 O O4 . NAG D . ? 1.9741 0.7513 1.1533 -0.0729 -0.5731 0.0143 701 NAG B O4 6116 O O5 . NAG D . ? 1.8969 0.7267 1.1395 -0.0278 -0.5482 -0.0111 701 NAG B O5 6117 O O6 . NAG D . ? 1.8771 0.7128 1.0744 -0.0592 -0.4928 -0.0044 701 NAG B O6 6118 O O7 . NAG D . ? 1.8430 0.7363 1.2296 0.0644 -0.5854 -0.0672 701 NAG B O7 6119 C C1 . NAG E . ? 1.3093 0.6592 0.7067 -0.0751 0.0193 -0.1230 702 NAG B C1 6120 C C2 . NAG E . ? 1.3297 0.6530 0.7029 -0.0766 0.0002 -0.1136 702 NAG B C2 6121 C C3 . NAG E . ? 1.3405 0.6507 0.6967 -0.0818 -0.0051 -0.1076 702 NAG B C3 6122 C C4 . NAG E . ? 1.3498 0.6602 0.6933 -0.1040 0.0091 -0.1115 702 NAG B C4 6123 C C5 . NAG E . ? 1.3263 0.6653 0.6978 -0.0987 0.0277 -0.1216 702 NAG B C5 6124 C C6 . NAG E . ? 1.3334 0.6760 0.6961 -0.1206 0.0432 -0.1287 702 NAG B C6 6125 C C7 . NAG E . ? 1.3262 0.6417 0.7082 -0.0537 -0.0223 -0.1100 702 NAG B C7 6126 C C8 . NAG E . ? 1.3264 0.6323 0.7088 -0.0374 -0.0408 -0.1051 702 NAG B C8 6127 N N2 . NAG E . ? 1.3187 0.6448 0.7054 -0.0555 -0.0116 -0.1112 702 NAG B N2 6128 O O3 . NAG E . ? 1.3611 0.6446 0.6949 -0.0854 -0.0240 -0.0997 702 NAG B O3 6129 O O4 . NAG E . ? 1.3611 0.6593 0.6876 -0.1109 0.0051 -0.1061 702 NAG B O4 6130 O O5 . NAG E . ? 1.3174 0.6672 0.7043 -0.0941 0.0312 -0.1270 702 NAG B O5 6131 O O6 . NAG E . ? 1.3337 0.6831 0.6995 -0.1322 0.0522 -0.1369 702 NAG B O6 6132 O O7 . NAG E . ? 1.3325 0.6467 0.7110 -0.0646 -0.0177 -0.1134 702 NAG B O7 6133 C C1 . NAG F . ? 1.4960 0.9299 0.9962 -0.1248 -0.0825 0.0879 301 NAG K C1 6134 C C2 . NAG F . ? 1.5014 0.9272 1.0110 -0.1241 -0.0942 0.0926 301 NAG K C2 6135 C C3 . NAG F . ? 1.4967 0.9413 1.0008 -0.1218 -0.0906 0.0951 301 NAG K C3 6136 C C4 . NAG F . ? 1.4871 0.9551 0.9808 -0.1181 -0.0754 0.0902 301 NAG K C4 6137 C C5 . NAG F . ? 1.4869 0.9612 0.9685 -0.1260 -0.0728 0.0935 301 NAG K C5 6138 C C6 . NAG F . ? 1.4773 0.9755 0.9488 -0.1240 -0.0610 0.0899 301 NAG K C6 6139 C C7 . NAG F . ? 1.5215 0.9118 1.0407 -0.1369 -0.1263 0.1076 301 NAG K C7 6140 C C8 . NAG F . ? 1.5321 0.9148 1.0423 -0.1511 -0.1450 0.1243 301 NAG K C8 6141 N N2 . NAG F . ? 1.5124 0.9267 1.0181 -0.1361 -0.1111 0.1057 301 NAG K N2 6142 O O3 . NAG F . ? 1.4943 0.9289 1.0149 -0.1120 -0.0919 0.0880 301 NAG K O3 6143 O O4 . NAG F . ? 1.4848 0.9726 0.9706 -0.1199 -0.0744 0.0948 301 NAG K O4 6144 O O5 . NAG F . ? 1.4875 0.9442 0.9770 -0.1222 -0.0707 0.0859 301 NAG K O5 6145 O O6 . NAG F . ? 1.4823 0.9800 0.9475 -0.1282 -0.0582 0.0895 301 NAG K O6 6146 O O7 . NAG F . ? 1.5214 0.8958 1.0603 -0.1274 -0.1262 0.0959 301 NAG K O7 6147 C C1 . NAG G . ? 1.4185 0.7990 0.8414 -0.2094 0.1668 -0.2099 302 NAG K C1 6148 C C2 . NAG G . ? 1.4430 0.8197 0.8339 -0.2331 0.1781 -0.2185 302 NAG K C2 6149 C C3 . NAG G . ? 1.4586 0.8408 0.8581 -0.2464 0.1919 -0.2433 302 NAG K C3 6150 C C4 . NAG G . ? 1.4486 0.8458 0.8888 -0.2376 0.1995 -0.2648 302 NAG K C4 6151 C C5 . NAG G . ? 1.4268 0.8234 0.8971 -0.2143 0.1854 -0.2541 302 NAG K C5 6152 C C6 . NAG G . ? 1.4167 0.8253 0.9321 -0.2026 0.1883 -0.2736 302 NAG K C6 6153 C C7 . NAG G . ? 1.4647 0.8204 0.7878 -0.2519 0.1690 -0.1909 302 NAG K C7 6154 C C8 . NAG G . ? 1.4615 0.8056 0.7633 -0.2463 0.1532 -0.1658 302 NAG K C8 6155 N N2 . NAG G . ? 1.4519 0.8150 0.8069 -0.2399 0.1693 -0.1985 302 NAG K N2 6156 O O3 . NAG G . ? 1.4837 0.8622 0.8497 -0.2707 0.2022 -0.2503 302 NAG K O3 6157 O O4 . NAG G . ? 1.4635 0.8697 0.9154 -0.2506 0.2143 -0.2926 302 NAG K O4 6158 O O5 . NAG G . ? 1.4121 0.8034 0.8725 -0.2024 0.1726 -0.2296 302 NAG K O5 6159 O O6 . NAG G . ? 1.4099 0.8272 0.9334 -0.1999 0.1928 -0.2786 302 NAG K O6 6160 O O7 . NAG G . ? 1.4796 0.8378 0.7914 -0.2673 0.1804 -0.2038 302 NAG K O7 # 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 32 32 PHE PHE B . n A 1 2 SER 2 33 33 SER SER B . n A 1 3 PRO 3 34 34 PRO PRO B . n A 1 4 GLN 4 35 35 GLN GLN B . n A 1 5 LEU 5 36 36 LEU LEU B . n A 1 6 LEU 6 37 37 LEU LEU B . n A 1 7 SER 7 38 38 SER SER B . n A 1 8 LEU 8 39 39 LEU LEU B . n A 1 9 LEU 9 40 40 LEU LEU B . n A 1 10 SER 10 41 41 SER SER B . n A 1 11 LEU 11 42 42 LEU LEU B . n A 1 12 LYS 12 43 43 LYS LYS B . n A 1 13 THR 13 44 44 THR THR B . n A 1 14 SER 14 45 45 SER SER B . n A 1 15 LEU 15 46 46 LEU LEU B . n A 1 16 SER 16 47 47 SER SER B . n A 1 17 GLY 17 48 48 GLY GLY B . n A 1 18 PRO 18 49 49 PRO PRO B . n A 1 19 PRO 19 50 50 PRO PRO B . n A 1 20 SER 20 51 51 SER SER B . n A 1 21 ALA 21 52 52 ALA ALA B . n A 1 22 PHE 22 53 53 PHE PHE B . n A 1 23 GLN 23 54 54 GLN GLN B . n A 1 24 ASP 24 55 55 ASP ASP B . n A 1 25 TRP 25 56 56 TRP TRP B . n A 1 26 LYS 26 57 57 LYS LYS B . n A 1 27 VAL 27 58 58 VAL VAL B . n A 1 28 PRO 28 59 59 PRO PRO B . n A 1 29 VAL 29 60 ? ? ? B . n A 1 30 ASN 30 61 ? ? ? B . n A 1 31 GLY 31 62 ? ? ? B . n A 1 32 GLN 32 63 ? ? ? B . n A 1 33 ASN 33 64 ? ? ? B . n A 1 34 ASP 34 65 65 ASP ASP B . n A 1 35 ALA 35 66 66 ALA ALA B . n A 1 36 VAL 36 67 67 VAL VAL B . n A 1 37 TRP 37 68 68 TRP TRP B . n A 1 38 CYS 38 69 69 CYS CYS B . n A 1 39 SER 39 70 70 SER SER B . n A 1 40 TRP 40 71 71 TRP TRP B . n A 1 41 SER 41 72 72 SER SER B . n A 1 42 GLY 42 73 73 GLY GLY B . n A 1 43 VAL 43 74 74 VAL VAL B . n A 1 44 VAL 44 75 75 VAL VAL B . n A 1 45 CYS 45 76 76 CYS CYS B . n A 1 46 ASP 46 77 77 ASP ASP B . n A 1 47 ASN 47 78 78 ASN ASN B . n A 1 48 VAL 48 79 79 VAL VAL B . n A 1 49 THR 49 80 80 THR THR B . n A 1 50 ALA 50 81 81 ALA ALA B . n A 1 51 GLN 51 82 82 GLN GLN B . n A 1 52 VAL 52 83 83 VAL VAL B . n A 1 53 ILE 53 84 84 ILE ILE B . n A 1 54 SER 54 85 85 SER SER B . n A 1 55 LEU 55 86 86 LEU LEU B . n A 1 56 ASP 56 87 87 ASP ASP B . n A 1 57 LEU 57 88 88 LEU LEU B . n A 1 58 SER 58 89 89 SER SER B . n A 1 59 HIS 59 90 90 HIS HIS B . n A 1 60 ARG 60 91 91 ARG ARG B . n A 1 61 ASN 61 92 92 ASN ASN B . n A 1 62 LEU 62 93 93 LEU LEU B . n A 1 63 SER 63 94 94 SER SER B . n A 1 64 GLY 64 95 95 GLY GLY B . n A 1 65 ARG 65 96 96 ARG ARG B . n A 1 66 ILE 66 97 97 ILE ILE B . n A 1 67 PRO 67 98 98 PRO PRO B . n A 1 68 ILE 68 99 99 ILE ILE B . n A 1 69 GLN 69 100 100 GLN GLN B . n A 1 70 ILE 70 101 101 ILE ILE B . n A 1 71 ARG 71 102 102 ARG ARG B . n A 1 72 TYR 72 103 103 TYR TYR B . n A 1 73 LEU 73 104 104 LEU LEU B . n A 1 74 SER 74 105 105 SER SER B . n A 1 75 SER 75 106 106 SER SER B . n A 1 76 LEU 76 107 107 LEU LEU B . n A 1 77 LEU 77 108 108 LEU LEU B . n A 1 78 TYR 78 109 109 TYR TYR B . n A 1 79 LEU 79 110 110 LEU LEU B . n A 1 80 ASN 80 111 111 ASN ASN B . n A 1 81 LEU 81 112 112 LEU LEU B . n A 1 82 SER 82 113 113 SER SER B . n A 1 83 GLY 83 114 114 GLY GLY B . n A 1 84 ASN 84 115 115 ASN ASN B . n A 1 85 SER 85 116 116 SER SER B . n A 1 86 LEU 86 117 117 LEU LEU B . n A 1 87 GLU 87 118 118 GLU GLU B . n A 1 88 GLY 88 119 119 GLY GLY B . n A 1 89 SER 89 120 120 SER SER B . n A 1 90 PHE 90 121 121 PHE PHE B . n A 1 91 PRO 91 122 122 PRO PRO B . n A 1 92 THR 92 123 123 THR THR B . n A 1 93 SER 93 124 124 SER SER B . n A 1 94 ILE 94 125 125 ILE ILE B . n A 1 95 PHE 95 126 126 PHE PHE B . n A 1 96 ASP 96 127 127 ASP ASP B . n A 1 97 LEU 97 128 128 LEU LEU B . n A 1 98 THR 98 129 129 THR THR B . n A 1 99 LYS 99 130 130 LYS LYS B . n A 1 100 LEU 100 131 131 LEU LEU B . n A 1 101 THR 101 132 132 THR THR B . n A 1 102 THR 102 133 133 THR THR B . n A 1 103 LEU 103 134 134 LEU LEU B . n A 1 104 ASP 104 135 135 ASP ASP B . n A 1 105 ILE 105 136 136 ILE ILE B . n A 1 106 SER 106 137 137 SER SER B . n A 1 107 ARG 107 138 138 ARG ARG B . n A 1 108 ASN 108 139 139 ASN ASN B . n A 1 109 SER 109 140 140 SER SER B . n A 1 110 PHE 110 141 141 PHE PHE B . n A 1 111 ASP 111 142 142 ASP ASP B . n A 1 112 SER 112 143 143 SER SER B . n A 1 113 SER 113 144 144 SER SER B . n A 1 114 PHE 114 145 145 PHE PHE B . n A 1 115 PRO 115 146 146 PRO PRO B . n A 1 116 PRO 116 147 147 PRO PRO B . n A 1 117 GLY 117 148 148 GLY GLY B . n A 1 118 ILE 118 149 149 ILE ILE B . n A 1 119 SER 119 150 150 SER SER B . n A 1 120 LYS 120 151 151 LYS LYS B . n A 1 121 LEU 121 152 152 LEU LEU B . n A 1 122 LYS 122 153 153 LYS LYS B . n A 1 123 PHE 123 154 154 PHE PHE B . n A 1 124 LEU 124 155 155 LEU LEU B . n A 1 125 LYS 125 156 156 LYS LYS B . n A 1 126 VAL 126 157 157 VAL VAL B . n A 1 127 PHE 127 158 158 PHE PHE B . n A 1 128 ASN 128 159 159 ASN ASN B . n A 1 129 ALA 129 160 160 ALA ALA B . n A 1 130 PHE 130 161 161 PHE PHE B . n A 1 131 SER 131 162 162 SER SER B . n A 1 132 ASN 132 163 163 ASN ASN B . n A 1 133 ASN 133 164 164 ASN ASN B . n A 1 134 PHE 134 165 165 PHE PHE B . n A 1 135 GLU 135 166 166 GLU GLU B . n A 1 136 GLY 136 167 167 GLY GLY B . n A 1 137 LEU 137 168 168 LEU LEU B . n A 1 138 LEU 138 169 169 LEU LEU B . n A 1 139 PRO 139 170 170 PRO PRO B . n A 1 140 SER 140 171 171 SER SER B . n A 1 141 ASP 141 172 172 ASP ASP B . n A 1 142 VAL 142 173 173 VAL VAL B . n A 1 143 SER 143 174 174 SER SER B . n A 1 144 ARG 144 175 175 ARG ARG B . n A 1 145 LEU 145 176 176 LEU LEU B . n A 1 146 ARG 146 177 177 ARG ARG B . n A 1 147 PHE 147 178 178 PHE PHE B . n A 1 148 LEU 148 179 179 LEU LEU B . n A 1 149 GLU 149 180 180 GLU GLU B . n A 1 150 GLU 150 181 181 GLU GLU B . n A 1 151 LEU 151 182 182 LEU LEU B . n A 1 152 ASN 152 183 183 ASN ASN B . n A 1 153 PHE 153 184 184 PHE PHE B . n A 1 154 GLY 154 185 185 GLY GLY B . n A 1 155 GLY 155 186 186 GLY GLY B . n A 1 156 SER 156 187 187 SER SER B . n A 1 157 TYR 157 188 188 TYR TYR B . n A 1 158 PHE 158 189 189 PHE PHE B . n A 1 159 GLU 159 190 190 GLU GLU B . n A 1 160 GLY 160 191 191 GLY GLY B . n A 1 161 GLU 161 192 192 GLU GLU B . n A 1 162 ILE 162 193 193 ILE ILE B . n A 1 163 PRO 163 194 194 PRO PRO B . n A 1 164 ALA 164 195 195 ALA ALA B . n A 1 165 ALA 165 196 196 ALA ALA B . n A 1 166 TYR 166 197 197 TYR TYR B . n A 1 167 GLY 167 198 198 GLY GLY B . n A 1 168 GLY 168 199 199 GLY GLY B . n A 1 169 LEU 169 200 200 LEU LEU B . n A 1 170 GLN 170 201 201 GLN GLN B . n A 1 171 ARG 171 202 202 ARG ARG B . n A 1 172 LEU 172 203 203 LEU LEU B . n A 1 173 LYS 173 204 204 LYS LYS B . n A 1 174 PHE 174 205 205 PHE PHE B . n A 1 175 ILE 175 206 206 ILE ILE B . n A 1 176 HIS 176 207 207 HIS HIS B . n A 1 177 LEU 177 208 208 LEU LEU B . n A 1 178 ALA 178 209 209 ALA ALA B . n A 1 179 GLY 179 210 210 GLY GLY B . n A 1 180 ASN 180 211 211 ASN ASN B . n A 1 181 VAL 181 212 212 VAL VAL B . n A 1 182 LEU 182 213 213 LEU LEU B . n A 1 183 GLY 183 214 214 GLY GLY B . n A 1 184 GLY 184 215 215 GLY GLY B . n A 1 185 LYS 185 216 216 LYS LYS B . n A 1 186 LEU 186 217 217 LEU LEU B . n A 1 187 PRO 187 218 218 PRO PRO B . n A 1 188 PRO 188 219 219 PRO PRO B . n A 1 189 ARG 189 220 220 ARG ARG B . n A 1 190 LEU 190 221 221 LEU LEU B . n A 1 191 GLY 191 222 222 GLY GLY B . n A 1 192 LEU 192 223 223 LEU LEU B . n A 1 193 LEU 193 224 224 LEU LEU B . n A 1 194 THR 194 225 225 THR THR B . n A 1 195 GLU 195 226 226 GLU GLU B . n A 1 196 LEU 196 227 227 LEU LEU B . n A 1 197 GLN 197 228 228 GLN GLN B . n A 1 198 HIS 198 229 229 HIS HIS B . n A 1 199 MET 199 230 230 MET MET B . n A 1 200 GLU 200 231 231 GLU GLU B . n A 1 201 ILE 201 232 232 ILE ILE B . n A 1 202 GLY 202 233 233 GLY GLY B . n A 1 203 TYR 203 234 234 TYR TYR B . n A 1 204 ASN 204 235 235 ASN ASN B . n A 1 205 HIS 205 236 236 HIS HIS B . n A 1 206 PHE 206 237 237 PHE PHE B . n A 1 207 ASN 207 238 238 ASN ASN B . n A 1 208 GLY 208 239 239 GLY GLY B . n A 1 209 ASN 209 240 240 ASN ASN B . n A 1 210 ILE 210 241 241 ILE ILE B . n A 1 211 PRO 211 242 242 PRO PRO B . n A 1 212 SER 212 243 243 SER SER B . n A 1 213 GLU 213 244 244 GLU GLU B . n A 1 214 PHE 214 245 245 PHE PHE B . n A 1 215 ALA 215 246 246 ALA ALA B . n A 1 216 LEU 216 247 247 LEU LEU B . n A 1 217 LEU 217 248 248 LEU LEU B . n A 1 218 SER 218 249 249 SER SER B . n A 1 219 ASN 219 250 250 ASN ASN B . n A 1 220 LEU 220 251 251 LEU LEU B . n A 1 221 LYS 221 252 252 LYS LYS B . n A 1 222 TYR 222 253 253 TYR TYR B . n A 1 223 PHE 223 254 254 PHE PHE B . n A 1 224 ASP 224 255 255 ASP ASP B . n A 1 225 VAL 225 256 256 VAL VAL B . n A 1 226 SER 226 257 257 SER SER B . n A 1 227 ASN 227 258 258 ASN ASN B . n A 1 228 CYS 228 259 259 CYS CYS B . n A 1 229 SER 229 260 260 SER SER B . n A 1 230 LEU 230 261 261 LEU LEU B . n A 1 231 SER 231 262 262 SER SER B . n A 1 232 GLY 232 263 263 GLY GLY B . n A 1 233 SER 233 264 264 SER SER B . n A 1 234 LEU 234 265 265 LEU LEU B . n A 1 235 PRO 235 266 266 PRO PRO B . n A 1 236 GLN 236 267 267 GLN GLN B . n A 1 237 GLU 237 268 268 GLU GLU B . n A 1 238 LEU 238 269 269 LEU LEU B . n A 1 239 GLY 239 270 270 GLY GLY B . n A 1 240 ASN 240 271 271 ASN ASN B . n A 1 241 LEU 241 272 272 LEU LEU B . n A 1 242 SER 242 273 273 SER SER B . n A 1 243 ASN 243 274 274 ASN ASN B . n A 1 244 LEU 244 275 275 LEU LEU B . n A 1 245 GLU 245 276 276 GLU GLU B . n A 1 246 THR 246 277 277 THR THR B . n A 1 247 LEU 247 278 278 LEU LEU B . n A 1 248 PHE 248 279 279 PHE PHE B . n A 1 249 LEU 249 280 280 LEU LEU B . n A 1 250 PHE 250 281 281 PHE PHE B . n A 1 251 GLN 251 282 282 GLN GLN B . n A 1 252 ASN 252 283 283 ASN ASN B . n A 1 253 GLY 253 284 284 GLY GLY B . n A 1 254 PHE 254 285 285 PHE PHE B . n A 1 255 THR 255 286 286 THR THR B . n A 1 256 GLY 256 287 287 GLY GLY B . n A 1 257 GLU 257 288 288 GLU GLU B . n A 1 258 ILE 258 289 289 ILE ILE B . n A 1 259 PRO 259 290 290 PRO PRO B . n A 1 260 GLU 260 291 291 GLU GLU B . n A 1 261 SER 261 292 292 SER SER B . n A 1 262 TYR 262 293 293 TYR TYR B . n A 1 263 SER 263 294 294 SER SER B . n A 1 264 ASN 264 295 295 ASN ASN B . n A 1 265 LEU 265 296 296 LEU LEU B . n A 1 266 LYS 266 297 297 LYS LYS B . n A 1 267 SER 267 298 298 SER SER B . n A 1 268 LEU 268 299 299 LEU LEU B . n A 1 269 LYS 269 300 300 LYS LYS B . n A 1 270 LEU 270 301 301 LEU LEU B . n A 1 271 LEU 271 302 302 LEU LEU B . n A 1 272 ASP 272 303 303 ASP ASP B . n A 1 273 PHE 273 304 304 PHE PHE B . n A 1 274 SER 274 305 305 SER SER B . n A 1 275 SER 275 306 306 SER SER B . n A 1 276 ASN 276 307 307 ASN ASN B . n A 1 277 GLN 277 308 308 GLN GLN B . n A 1 278 LEU 278 309 309 LEU LEU B . n A 1 279 SER 279 310 310 SER SER B . n A 1 280 GLY 280 311 311 GLY GLY B . n A 1 281 SER 281 312 312 SER SER B . n A 1 282 ILE 282 313 313 ILE ILE B . n A 1 283 PRO 283 314 314 PRO PRO B . n A 1 284 SER 284 315 315 SER SER B . n A 1 285 GLY 285 316 316 GLY GLY B . n A 1 286 PHE 286 317 317 PHE PHE B . n A 1 287 SER 287 318 318 SER SER B . n A 1 288 THR 288 319 319 THR THR B . n A 1 289 LEU 289 320 320 LEU LEU B . n A 1 290 LYS 290 321 321 LYS LYS B . n A 1 291 ASN 291 322 322 ASN ASN B . n A 1 292 LEU 292 323 323 LEU LEU B . n A 1 293 THR 293 324 324 THR THR B . n A 1 294 TRP 294 325 325 TRP TRP B . n A 1 295 LEU 295 326 326 LEU LEU B . n A 1 296 SER 296 327 327 SER SER B . n A 1 297 LEU 297 328 328 LEU LEU B . n A 1 298 ILE 298 329 329 ILE ILE B . n A 1 299 SER 299 330 330 SER SER B . n A 1 300 ASN 300 331 331 ASN ASN B . n A 1 301 ASN 301 332 332 ASN ASN B . n A 1 302 LEU 302 333 333 LEU LEU B . n A 1 303 SER 303 334 334 SER SER B . n A 1 304 GLY 304 335 335 GLY GLY B . n A 1 305 GLU 305 336 336 GLU GLU B . n A 1 306 VAL 306 337 337 VAL VAL B . n A 1 307 PRO 307 338 338 PRO PRO B . n A 1 308 GLU 308 339 339 GLU GLU B . n A 1 309 GLY 309 340 340 GLY GLY B . n A 1 310 ILE 310 341 341 ILE ILE B . n A 1 311 GLY 311 342 342 GLY GLY B . n A 1 312 GLU 312 343 343 GLU GLU B . n A 1 313 LEU 313 344 344 LEU LEU B . n A 1 314 PRO 314 345 345 PRO PRO B . n A 1 315 GLU 315 346 346 GLU GLU B . n A 1 316 LEU 316 347 347 LEU LEU B . n A 1 317 THR 317 348 348 THR THR B . n A 1 318 THR 318 349 349 THR THR B . n A 1 319 LEU 319 350 350 LEU LEU B . n A 1 320 PHE 320 351 351 PHE PHE B . n A 1 321 LEU 321 352 352 LEU LEU B . n A 1 322 TRP 322 353 353 TRP TRP B . n A 1 323 ASN 323 354 354 ASN ASN B . n A 1 324 ASN 324 355 355 ASN ASN B . n A 1 325 ASN 325 356 356 ASN ASN B . n A 1 326 PHE 326 357 357 PHE PHE B . n A 1 327 THR 327 358 358 THR THR B . n A 1 328 GLY 328 359 359 GLY GLY B . n A 1 329 VAL 329 360 360 VAL VAL B . n A 1 330 LEU 330 361 361 LEU LEU B . n A 1 331 PRO 331 362 362 PRO PRO B . n A 1 332 HIS 332 363 363 HIS HIS B . n A 1 333 LYS 333 364 364 LYS LYS B . n A 1 334 LEU 334 365 365 LEU LEU B . n A 1 335 GLY 335 366 366 GLY GLY B . n A 1 336 SER 336 367 367 SER SER B . n A 1 337 ASN 337 368 368 ASN ASN B . n A 1 338 GLY 338 369 369 GLY GLY B . n A 1 339 LYS 339 370 370 LYS LYS B . n A 1 340 LEU 340 371 371 LEU LEU B . n A 1 341 GLU 341 372 372 GLU GLU B . n A 1 342 THR 342 373 373 THR THR B . n A 1 343 MET 343 374 374 MET MET B . n A 1 344 ASP 344 375 375 ASP ASP B . n A 1 345 VAL 345 376 376 VAL VAL B . n A 1 346 SER 346 377 377 SER SER B . n A 1 347 ASN 347 378 378 ASN ASN B . n A 1 348 ASN 348 379 379 ASN ASN B . n A 1 349 SER 349 380 380 SER SER B . n A 1 350 PHE 350 381 381 PHE PHE B . n A 1 351 THR 351 382 382 THR THR B . n A 1 352 GLY 352 383 383 GLY GLY B . n A 1 353 THR 353 384 384 THR THR B . n A 1 354 ILE 354 385 385 ILE ILE B . n A 1 355 PRO 355 386 386 PRO PRO B . n A 1 356 SER 356 387 387 SER SER B . n A 1 357 SER 357 388 388 SER SER B . n A 1 358 LEU 358 389 389 LEU LEU B . n A 1 359 CYS 359 390 390 CYS CYS B . n A 1 360 HIS 360 391 391 HIS HIS B . n A 1 361 GLY 361 392 392 GLY GLY B . n A 1 362 ASN 362 393 393 ASN ASN B . n A 1 363 LYS 363 394 394 LYS LYS B . n A 1 364 LEU 364 395 395 LEU LEU B . n A 1 365 TYR 365 396 396 TYR TYR B . n A 1 366 LYS 366 397 397 LYS LYS B . n A 1 367 LEU 367 398 398 LEU LEU B . n A 1 368 ILE 368 399 399 ILE ILE B . n A 1 369 LEU 369 400 400 LEU LEU B . n A 1 370 PHE 370 401 401 PHE PHE B . n A 1 371 SER 371 402 402 SER SER B . n A 1 372 ASN 372 403 403 ASN ASN B . n A 1 373 MET 373 404 404 MET MET B . n A 1 374 PHE 374 405 405 PHE PHE B . n A 1 375 GLU 375 406 406 GLU GLU B . n A 1 376 GLY 376 407 407 GLY GLY B . n A 1 377 GLU 377 408 408 GLU GLU B . n A 1 378 LEU 378 409 409 LEU LEU B . n A 1 379 PRO 379 410 410 PRO PRO B . n A 1 380 LYS 380 411 411 LYS LYS B . n A 1 381 SER 381 412 412 SER SER B . n A 1 382 LEU 382 413 413 LEU LEU B . n A 1 383 THR 383 414 414 THR THR B . n A 1 384 ARG 384 415 415 ARG ARG B . n A 1 385 CYS 385 416 416 CYS CYS B . n A 1 386 GLU 386 417 417 GLU GLU B . n A 1 387 SER 387 418 418 SER SER B . n A 1 388 LEU 388 419 419 LEU LEU B . n A 1 389 TRP 389 420 420 TRP TRP B . n A 1 390 ARG 390 421 421 ARG ARG B . n A 1 391 PHE 391 422 422 PHE PHE B . n A 1 392 ARG 392 423 423 ARG ARG B . n A 1 393 SER 393 424 424 SER SER B . n A 1 394 GLN 394 425 425 GLN GLN B . n A 1 395 ASN 395 426 426 ASN ASN B . n A 1 396 ASN 396 427 427 ASN ASN B . n A 1 397 ARG 397 428 428 ARG ARG B . n A 1 398 LEU 398 429 429 LEU LEU B . n A 1 399 ASN 399 430 430 ASN ASN B . n A 1 400 GLY 400 431 431 GLY GLY B . n A 1 401 THR 401 432 432 THR THR B . n A 1 402 ILE 402 433 433 ILE ILE B . n A 1 403 PRO 403 434 434 PRO PRO B . n A 1 404 ILE 404 435 435 ILE ILE B . n A 1 405 GLY 405 436 436 GLY GLY B . n A 1 406 PHE 406 437 437 PHE PHE B . n A 1 407 GLY 407 438 438 GLY GLY B . n A 1 408 SER 408 439 439 SER SER B . n A 1 409 LEU 409 440 440 LEU LEU B . n A 1 410 ARG 410 441 441 ARG ARG B . n A 1 411 ASN 411 442 442 ASN ASN B . n A 1 412 LEU 412 443 443 LEU LEU B . n A 1 413 THR 413 444 444 THR THR B . n A 1 414 PHE 414 445 445 PHE PHE B . n A 1 415 VAL 415 446 446 VAL VAL B . n A 1 416 ASP 416 447 447 ASP ASP B . n A 1 417 LEU 417 448 448 LEU LEU B . n A 1 418 SER 418 449 449 SER SER B . n A 1 419 ASN 419 450 450 ASN ASN B . n A 1 420 ASN 420 451 451 ASN ASN B . n A 1 421 ARG 421 452 452 ARG ARG B . n A 1 422 PHE 422 453 453 PHE PHE B . n A 1 423 THR 423 454 454 THR THR B . n A 1 424 ASP 424 455 455 ASP ASP B . n A 1 425 GLN 425 456 456 GLN GLN B . n A 1 426 ILE 426 457 457 ILE ILE B . n A 1 427 PRO 427 458 458 PRO PRO B . n A 1 428 ALA 428 459 459 ALA ALA B . n A 1 429 ASP 429 460 460 ASP ASP B . n A 1 430 PHE 430 461 461 PHE PHE B . n A 1 431 ALA 431 462 462 ALA ALA B . n A 1 432 THR 432 463 463 THR THR B . n A 1 433 ALA 433 464 464 ALA ALA B . n A 1 434 PRO 434 465 465 PRO PRO B . n A 1 435 VAL 435 466 466 VAL VAL B . n A 1 436 LEU 436 467 467 LEU LEU B . n A 1 437 GLN 437 468 468 GLN GLN B . n A 1 438 TYR 438 469 469 TYR TYR B . n A 1 439 LEU 439 470 470 LEU LEU B . n A 1 440 ASN 440 471 471 ASN ASN B . n A 1 441 LEU 441 472 472 LEU LEU B . n A 1 442 SER 442 473 473 SER SER B . n A 1 443 THR 443 474 474 THR THR B . n A 1 444 ASN 444 475 475 ASN ASN B . n A 1 445 PHE 445 476 476 PHE PHE B . n A 1 446 PHE 446 477 477 PHE PHE B . n A 1 447 HIS 447 478 478 HIS HIS B . n A 1 448 ARG 448 479 479 ARG ARG B . n A 1 449 LYS 449 480 480 LYS LYS B . n A 1 450 LEU 450 481 481 LEU LEU B . n A 1 451 PRO 451 482 482 PRO PRO B . n A 1 452 GLU 452 483 483 GLU GLU B . n A 1 453 ASN 453 484 484 ASN ASN B . n A 1 454 ILE 454 485 485 ILE ILE B . n A 1 455 TRP 455 486 486 TRP TRP B . n A 1 456 LYS 456 487 487 LYS LYS B . n A 1 457 ALA 457 488 488 ALA ALA B . n A 1 458 PRO 458 489 489 PRO PRO B . n A 1 459 ASN 459 490 490 ASN ASN B . n A 1 460 LEU 460 491 491 LEU LEU B . n A 1 461 GLN 461 492 492 GLN GLN B . n A 1 462 ILE 462 493 493 ILE ILE B . n A 1 463 PHE 463 494 494 PHE PHE B . n A 1 464 SER 464 495 495 SER SER B . n A 1 465 ALA 465 496 496 ALA ALA B . n A 1 466 SER 466 497 497 SER SER B . n A 1 467 PHE 467 498 498 PHE PHE B . n A 1 468 SER 468 499 499 SER SER B . n A 1 469 ASN 469 500 500 ASN ASN B . n A 1 470 LEU 470 501 501 LEU LEU B . n A 1 471 ILE 471 502 502 ILE ILE B . n A 1 472 GLY 472 503 503 GLY GLY B . n A 1 473 GLU 473 504 504 GLU GLU B . n A 1 474 ILE 474 505 505 ILE ILE B . n A 1 475 PRO 475 506 506 PRO PRO B . n A 1 476 ASN 476 507 507 ASN ASN B . n A 1 477 TYR 477 508 508 TYR TYR B . n A 1 478 VAL 478 509 509 VAL VAL B . n A 1 479 GLY 479 510 510 GLY GLY B . n A 1 480 CYS 480 511 511 CYS CYS B . n A 1 481 LYS 481 512 512 LYS LYS B . n A 1 482 SER 482 513 513 SER SER B . n A 1 483 PHE 483 514 514 PHE PHE B . n A 1 484 TYR 484 515 515 TYR TYR B . n A 1 485 ARG 485 516 516 ARG ARG B . n A 1 486 ILE 486 517 517 ILE ILE B . n A 1 487 GLU 487 518 518 GLU GLU B . n A 1 488 LEU 488 519 519 LEU LEU B . n A 1 489 GLN 489 520 520 GLN GLN B . n A 1 490 GLY 490 521 521 GLY GLY B . n A 1 491 ASN 491 522 522 ASN ASN B . n A 1 492 SER 492 523 523 SER SER B . n A 1 493 LEU 493 524 524 LEU LEU B . n A 1 494 ASN 494 525 525 ASN ASN B . n A 1 495 GLY 495 526 526 GLY GLY B . n A 1 496 THR 496 527 527 THR THR B . n A 1 497 ILE 497 528 528 ILE ILE B . n A 1 498 PRO 498 529 529 PRO PRO B . n A 1 499 TRP 499 530 530 TRP TRP B . n A 1 500 ASP 500 531 531 ASP ASP B . n A 1 501 ILE 501 532 532 ILE ILE B . n A 1 502 GLY 502 533 533 GLY GLY B . n A 1 503 HIS 503 534 534 HIS HIS B . n A 1 504 CYS 504 535 535 CYS CYS B . n A 1 505 GLU 505 536 536 GLU GLU B . n A 1 506 LYS 506 537 537 LYS LYS B . n A 1 507 LEU 507 538 538 LEU LEU B . n A 1 508 LEU 508 539 539 LEU LEU B . n A 1 509 CYS 509 540 540 CYS CYS B . n A 1 510 LEU 510 541 541 LEU LEU B . n A 1 511 ASN 511 542 542 ASN ASN B . n A 1 512 LEU 512 543 543 LEU LEU B . n A 1 513 SER 513 544 544 SER SER B . n A 1 514 GLN 514 545 545 GLN GLN B . n A 1 515 ASN 515 546 546 ASN ASN B . n A 1 516 HIS 516 547 547 HIS HIS B . n A 1 517 LEU 517 548 548 LEU LEU B . n A 1 518 ASN 518 549 549 ASN ASN B . n A 1 519 GLY 519 550 550 GLY GLY B . n A 1 520 ILE 520 551 551 ILE ILE B . n A 1 521 ILE 521 552 552 ILE ILE B . n A 1 522 PRO 522 553 553 PRO PRO B . n A 1 523 TRP 523 554 554 TRP TRP B . n A 1 524 GLU 524 555 555 GLU GLU B . n A 1 525 ILE 525 556 556 ILE ILE B . n A 1 526 SER 526 557 557 SER SER B . n A 1 527 THR 527 558 558 THR THR B . n A 1 528 LEU 528 559 559 LEU LEU B . n A 1 529 PRO 529 560 560 PRO PRO B . n A 1 530 SER 530 561 561 SER SER B . n A 1 531 ILE 531 562 562 ILE ILE B . n A 1 532 ALA 532 563 563 ALA ALA B . n A 1 533 ASP 533 564 564 ASP ASP B . n A 1 534 VAL 534 565 565 VAL VAL B . n A 1 535 ASP 535 566 566 ASP ASP B . n A 1 536 LEU 536 567 567 LEU LEU B . n A 1 537 SER 537 568 568 SER SER B . n A 1 538 HIS 538 569 569 HIS HIS B . n A 1 539 ASN 539 570 570 ASN ASN B . n A 1 540 LEU 540 571 571 LEU LEU B . n A 1 541 LEU 541 572 572 LEU LEU B . n A 1 542 THR 542 573 573 THR THR B . n A 1 543 GLY 543 574 574 GLY GLY B . n A 1 544 THR 544 575 575 THR THR B . n A 1 545 ILE 545 576 576 ILE ILE B . n A 1 546 PRO 546 577 577 PRO PRO B . n A 1 547 SER 547 578 578 SER SER B . n A 1 548 ASP 548 579 579 ASP ASP B . n A 1 549 PHE 549 580 580 PHE PHE B . n A 1 550 GLY 550 581 581 GLY GLY B . n A 1 551 SER 551 582 582 SER SER B . n A 1 552 SER 552 583 583 SER SER B . n A 1 553 LYS 553 584 584 LYS LYS B . n A 1 554 THR 554 585 585 THR THR B . n A 1 555 ILE 555 586 586 ILE ILE B . n A 1 556 THR 556 587 587 THR THR B . n A 1 557 THR 557 588 588 THR THR B . n A 1 558 PHE 558 589 589 PHE PHE B . n A 1 559 ASN 559 590 590 ASN ASN B . n A 1 560 VAL 560 591 591 VAL VAL B . n A 1 561 SER 561 592 592 SER SER B . n A 1 562 TYR 562 593 593 TYR TYR B . n A 1 563 ASN 563 594 594 ASN ASN B . n A 1 564 GLN 564 595 595 GLN GLN B . n A 1 565 LEU 565 596 596 LEU LEU B . n A 1 566 ILE 566 597 597 ILE ILE B . n A 1 567 GLY 567 598 598 GLY GLY B . n A 1 568 PRO 568 599 599 PRO PRO B . n A 1 569 ILE 569 600 600 ILE ILE B . n A 1 570 PRO 570 601 601 PRO PRO B . n A 1 571 SER 571 602 602 SER SER B . n A 1 572 GLY 572 603 603 GLY GLY B . n A 1 573 SER 573 604 604 SER SER B . n A 1 574 PHE 574 605 605 PHE PHE B . n A 1 575 ALA 575 606 606 ALA ALA B . n A 1 576 HIS 576 607 607 HIS HIS B . n A 1 577 LEU 577 608 608 LEU LEU B . n A 1 578 ASN 578 609 609 ASN ASN B . n A 1 579 PRO 579 610 610 PRO PRO B . n A 1 580 SER 580 611 611 SER SER B . n A 1 581 PHE 581 612 612 PHE PHE B . n A 1 582 PHE 582 613 613 PHE PHE B . n A 1 583 SER 583 614 614 SER SER B . n A 1 584 SER 584 615 615 SER SER B . n A 1 585 ASN 585 616 616 ASN ASN B . n A 1 586 GLU 586 617 617 GLU GLU B . n A 1 587 GLY 587 618 618 GLY GLY B . n A 1 588 LEU 588 619 619 LEU LEU B . n A 1 589 CYS 589 620 620 CYS CYS B . n A 1 590 GLY 590 621 621 GLY GLY B . n A 1 591 ASP 591 622 622 ASP ASP B . n A 1 592 LEU 592 623 623 LEU LEU B . n A 1 593 VAL 593 624 624 VAL VAL B . n A 1 594 GLY 594 625 625 GLY GLY B . n A 1 595 LYS 595 626 626 LYS LYS B . n A 1 596 PRO 596 627 627 PRO PRO B . n A 1 597 CYS 597 628 628 CYS CYS B . n A 1 598 ASN 598 629 629 ASN ASN B . n B 2 1 HIS 1 93 93 HIS HIS C . n B 2 2 GLU 2 94 94 GLU GLU C . n B 2 3 VAL 3 95 95 VAL VAL C . n B 2 4 PRO 4 96 96 PRO PRO C . n B 2 5 SER 5 97 97 SER SER C . n B 2 6 GLY 6 98 98 GLY GLY C . n B 2 7 HYP 7 99 99 HYP HPY C . n B 2 8 ASN 8 100 100 ASN ASN C . n B 2 9 PRO 9 101 101 PRO PRO C . n B 2 10 ILE 10 102 102 ILE ILE C . n B 2 11 SER 11 103 103 SER SER C . n B 2 12 ASN 12 104 104 ASN ASN C . n C 3 1 ASN 1 27 27 ASN ASN K . n C 3 2 MET 2 28 28 MET MET K . n C 3 3 GLU 3 29 29 GLU GLU K . n C 3 4 GLY 4 30 30 GLY GLY K . n C 3 5 ASP 5 31 31 ASP ASP K . n C 3 6 ALA 6 32 32 ALA ALA K . n C 3 7 LEU 7 33 33 LEU LEU K . n C 3 8 HIS 8 34 34 HIS HIS K . n C 3 9 SER 9 35 35 SER SER K . n C 3 10 LEU 10 36 36 LEU LEU K . n C 3 11 ARG 11 37 37 ARG ARG K . n C 3 12 ALA 12 38 38 ALA ALA K . n C 3 13 ASN 13 39 39 ASN ASN K . n C 3 14 LEU 14 40 40 LEU LEU K . n C 3 15 VAL 15 41 41 VAL VAL K . n C 3 16 ASP 16 42 42 ASP ASP K . n C 3 17 PRO 17 43 43 PRO PRO K . n C 3 18 ASN 18 44 44 ASN ASN K . n C 3 19 ASN 19 45 45 ASN ASN K . n C 3 20 VAL 20 46 46 VAL VAL K . n C 3 21 LEU 21 47 47 LEU LEU K . n C 3 22 GLN 22 48 48 GLN GLN K . n C 3 23 SER 23 49 49 SER SER K . n C 3 24 TRP 24 50 50 TRP TRP K . n C 3 25 ASP 25 51 51 ASP ASP K . n C 3 26 PRO 26 52 52 PRO PRO K . n C 3 27 THR 27 53 53 THR THR K . n C 3 28 LEU 28 54 54 LEU LEU K . n C 3 29 VAL 29 55 55 VAL VAL K . n C 3 30 ASN 30 56 56 ASN ASN K . n C 3 31 PRO 31 57 57 PRO PRO K . n C 3 32 CYS 32 58 58 CYS CYS K . n C 3 33 THR 33 59 59 THR THR K . n C 3 34 TRP 34 60 60 TRP TRP K . n C 3 35 PHE 35 61 61 PHE PHE K . n C 3 36 HIS 36 62 62 HIS HIS K . n C 3 37 VAL 37 63 63 VAL VAL K . n C 3 38 THR 38 64 64 THR THR K . n C 3 39 CYS 39 65 65 CYS CYS K . n C 3 40 ASN 40 66 66 ASN ASN K . n C 3 41 ASN 41 67 67 ASN ASN K . n C 3 42 GLU 42 68 68 GLU GLU K . n C 3 43 ASN 43 69 69 ASN ASN K . n C 3 44 SER 44 70 70 SER SER K . n C 3 45 VAL 45 71 71 VAL VAL K . n C 3 46 ILE 46 72 72 ILE ILE K . n C 3 47 ARG 47 73 73 ARG ARG K . n C 3 48 VAL 48 74 74 VAL VAL K . n C 3 49 ASP 49 75 75 ASP ASP K . n C 3 50 LEU 50 76 76 LEU LEU K . n C 3 51 GLY 51 77 77 GLY GLY K . n C 3 52 ASN 52 78 78 ASN ASN K . n C 3 53 ALA 53 79 79 ALA ALA K . n C 3 54 ASP 54 80 80 ASP ASP K . n C 3 55 LEU 55 81 81 LEU LEU K . n C 3 56 SER 56 82 82 SER SER K . n C 3 57 GLY 57 83 83 GLY GLY K . n C 3 58 GLN 58 84 84 GLN GLN K . n C 3 59 LEU 59 85 85 LEU LEU K . n C 3 60 VAL 60 86 86 VAL VAL K . n C 3 61 PRO 61 87 87 PRO PRO K . n C 3 62 GLN 62 88 88 GLN GLN K . n C 3 63 LEU 63 89 89 LEU LEU K . n C 3 64 GLY 64 90 90 GLY GLY K . n C 3 65 GLN 65 91 91 GLN GLN K . n C 3 66 LEU 66 92 92 LEU LEU K . n C 3 67 LYS 67 93 93 LYS LYS K . n C 3 68 ASN 68 94 94 ASN ASN K . n C 3 69 LEU 69 95 95 LEU LEU K . n C 3 70 GLN 70 96 96 GLN GLN K . n C 3 71 TYR 71 97 97 TYR TYR K . n C 3 72 LEU 72 98 98 LEU LEU K . n C 3 73 GLU 73 99 99 GLU GLU K . n C 3 74 LEU 74 100 100 LEU LEU K . n C 3 75 TYR 75 101 101 TYR TYR K . n C 3 76 SER 76 102 102 SER SER K . n C 3 77 ASN 77 103 103 ASN ASN K . n C 3 78 ASN 78 104 104 ASN ASN K . n C 3 79 ILE 79 105 105 ILE ILE K . n C 3 80 THR 80 106 106 THR THR K . n C 3 81 GLY 81 107 107 GLY GLY K . n C 3 82 PRO 82 108 108 PRO PRO K . n C 3 83 VAL 83 109 109 VAL VAL K . n C 3 84 PRO 84 110 110 PRO PRO K . n C 3 85 SER 85 111 111 SER SER K . n C 3 86 ASP 86 112 112 ASP ASP K . n C 3 87 LEU 87 113 113 LEU LEU K . n C 3 88 GLY 88 114 114 GLY GLY K . n C 3 89 ASN 89 115 115 ASN ASN K . n C 3 90 LEU 90 116 116 LEU LEU K . n C 3 91 THR 91 117 117 THR THR K . n C 3 92 ASN 92 118 118 ASN ASN K . n C 3 93 LEU 93 119 119 LEU LEU K . n C 3 94 VAL 94 120 120 VAL VAL K . n C 3 95 SER 95 121 121 SER SER K . n C 3 96 LEU 96 122 122 LEU LEU K . n C 3 97 ASP 97 123 123 ASP ASP K . n C 3 98 LEU 98 124 124 LEU LEU K . n C 3 99 TYR 99 125 125 TYR TYR K . n C 3 100 LEU 100 126 126 LEU LEU K . n C 3 101 ASN 101 127 127 ASN ASN K . n C 3 102 SER 102 128 128 SER SER K . n C 3 103 PHE 103 129 129 PHE PHE K . n C 3 104 THR 104 130 130 THR THR K . n C 3 105 GLY 105 131 131 GLY GLY K . n C 3 106 PRO 106 132 132 PRO PRO K . n C 3 107 ILE 107 133 133 ILE ILE K . n C 3 108 PRO 108 134 134 PRO PRO K . n C 3 109 ASP 109 135 135 ASP ASP K . n C 3 110 SER 110 136 136 SER SER K . n C 3 111 LEU 111 137 137 LEU LEU K . n C 3 112 GLY 112 138 138 GLY GLY K . n C 3 113 LYS 113 139 139 LYS LYS K . n C 3 114 LEU 114 140 140 LEU LEU K . n C 3 115 PHE 115 141 141 PHE PHE K . n C 3 116 LYS 116 142 142 LYS LYS K . n C 3 117 LEU 117 143 143 LEU LEU K . n C 3 118 ARG 118 144 144 ARG ARG K . n C 3 119 PHE 119 145 145 PHE PHE K . n C 3 120 LEU 120 146 146 LEU LEU K . n C 3 121 ARG 121 147 147 ARG ARG K . n C 3 122 LEU 122 148 148 LEU LEU K . n C 3 123 ASN 123 149 149 ASN ASN K . n C 3 124 ASN 124 150 150 ASN ASN K . n C 3 125 ASN 125 151 151 ASN ASN K . n C 3 126 SER 126 152 152 SER SER K . n C 3 127 LEU 127 153 153 LEU LEU K . n C 3 128 THR 128 154 154 THR THR K . n C 3 129 GLY 129 155 155 GLY GLY K . n C 3 130 PRO 130 156 156 PRO PRO K . n C 3 131 ILE 131 157 157 ILE ILE K . n C 3 132 PRO 132 158 158 PRO PRO K . n C 3 133 MET 133 159 159 MET MET K . n C 3 134 SER 134 160 160 SER SER K . n C 3 135 LEU 135 161 161 LEU LEU K . n C 3 136 THR 136 162 162 THR THR K . n C 3 137 ASN 137 163 163 ASN ASN K . n C 3 138 ILE 138 164 164 ILE ILE K . n C 3 139 MET 139 165 165 MET MET K . n C 3 140 THR 140 166 166 THR THR K . n C 3 141 LEU 141 167 167 LEU LEU K . n C 3 142 GLN 142 168 168 GLN GLN K . n C 3 143 VAL 143 169 169 VAL VAL K . n C 3 144 LEU 144 170 170 LEU LEU K . n C 3 145 ASP 145 171 171 ASP ASP K . n C 3 146 LEU 146 172 172 LEU LEU K . n C 3 147 SER 147 173 173 SER SER K . n C 3 148 ASN 148 174 174 ASN ASN K . n C 3 149 ASN 149 175 175 ASN ASN K . n C 3 150 ARG 150 176 176 ARG ARG K . n C 3 151 LEU 151 177 177 LEU LEU K . n C 3 152 SER 152 178 178 SER SER K . n C 3 153 GLY 153 179 179 GLY GLY K . n C 3 154 SER 154 180 180 SER SER K . n C 3 155 VAL 155 181 181 VAL VAL K . n C 3 156 PRO 156 182 182 PRO PRO K . n C 3 157 ASP 157 183 183 ASP ASP K . n C 3 158 ASN 158 184 184 ASN ASN K . n C 3 159 GLY 159 185 185 GLY GLY K . n C 3 160 SER 160 186 186 SER SER K . n C 3 161 PHE 161 187 187 PHE PHE K . n C 3 162 SER 162 188 188 SER SER K . n C 3 163 LEU 163 189 189 LEU LEU K . n C 3 164 PHE 164 190 190 PHE PHE K . n C 3 165 THR 165 191 191 THR THR K . n C 3 166 PRO 166 192 192 PRO PRO K . n C 3 167 ILE 167 193 193 ILE ILE K . n C 3 168 SER 168 194 194 SER SER K . n C 3 169 PHE 169 195 195 PHE PHE K . n C 3 170 ALA 170 196 196 ALA ALA K . n C 3 171 ASN 171 197 197 ASN ASN K . n C 3 172 ASN 172 198 198 ASN ASN K . n C 3 173 LEU 173 199 199 LEU LEU K . n C 3 174 ASP 174 200 200 ASP ASP K . n C 3 175 LEU 175 201 201 LEU LEU K . n C 3 176 CYS 176 202 202 CYS CYS K . n C 3 177 GLY 177 203 203 GLY GLY K . n C 3 178 PRO 178 204 204 PRO PRO K . n C 3 179 VAL 179 205 205 VAL VAL K . n C 3 180 THR 180 206 206 THR THR K . n C 3 181 SER 181 207 207 SER SER K . n C 3 182 ARG 182 208 208 ARG ARG K . n C 3 183 PRO 183 209 209 PRO PRO K . n C 3 184 CYS 184 210 210 CYS CYS K . n C 3 185 PRO 185 211 211 PRO PRO K . 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 1 701 3221 NAG NAG B . E 4 NAG 1 702 1111 NAG NAG B . F 4 NAG 1 301 1841 NAG NAG K . G 4 NAG 1 302 1501 NAG NAG K . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G # 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)' 4250 ? 1 MORE 5 ? 1 'SSA (A^2)' 31270 ? # _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_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 2016-12-14 2 'Structure model' 1 1 2017-09-27 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Data collection' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 2 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category diffrn_detector # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 2 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_diffrn_detector.detector' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 58.0206 _pdbx_refine_tls.origin_y -31.8570 _pdbx_refine_tls.origin_z 14.2508 _pdbx_refine_tls.T[1][1] 1.1368 _pdbx_refine_tls.T[2][2] 0.4522 _pdbx_refine_tls.T[3][3] 0.4786 _pdbx_refine_tls.T[1][2] -0.0167 _pdbx_refine_tls.T[1][3] -0.0932 _pdbx_refine_tls.T[2][3] -0.0370 _pdbx_refine_tls.L[1][1] 1.1001 _pdbx_refine_tls.L[2][2] 1.0532 _pdbx_refine_tls.L[3][3] 0.8501 _pdbx_refine_tls.L[1][2] 0.9227 _pdbx_refine_tls.L[1][3] 0.7969 _pdbx_refine_tls.L[2][3] 0.6576 _pdbx_refine_tls.S[1][1] -0.4574 _pdbx_refine_tls.S[1][2] 0.0110 _pdbx_refine_tls.S[1][3] 0.2322 _pdbx_refine_tls.S[2][1] -0.5223 _pdbx_refine_tls.S[2][2] 0.2445 _pdbx_refine_tls.S[2][3] 0.1644 _pdbx_refine_tls.S[3][1] -0.3409 _pdbx_refine_tls.S[3][2] -0.0719 _pdbx_refine_tls.S[3][3] 0.2108 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _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 all # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.8_1069 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? . 4 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 ND2 K ASN 184 ? ? O5 K NAG 301 ? ? 2.13 2 1 O B GLU 555 ? ? OG1 B THR 558 ? ? 2.14 3 1 O B ASP 460 ? ? OG1 B THR 463 ? ? 2.17 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 C _pdbx_validate_rmsd_angle.auth_asym_id_1 B _pdbx_validate_rmsd_angle.auth_comp_id_1 ILE _pdbx_validate_rmsd_angle.auth_seq_id_1 97 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 N _pdbx_validate_rmsd_angle.auth_asym_id_2 B _pdbx_validate_rmsd_angle.auth_comp_id_2 PRO _pdbx_validate_rmsd_angle.auth_seq_id_2 98 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 CA _pdbx_validate_rmsd_angle.auth_asym_id_3 B _pdbx_validate_rmsd_angle.auth_comp_id_3 PRO _pdbx_validate_rmsd_angle.auth_seq_id_3 98 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 128.45 _pdbx_validate_rmsd_angle.angle_target_value 119.30 _pdbx_validate_rmsd_angle.angle_deviation 9.15 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.50 _pdbx_validate_rmsd_angle.linker_flag 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 ALA B 81 ? ? 64.73 -2.02 2 1 ARG B 102 ? ? 67.15 -5.98 3 1 THR B 129 ? ? 67.29 -16.05 4 1 SER B 143 ? ? 63.16 -138.09 5 1 LYS B 153 ? ? 73.94 -31.89 6 1 LYS B 156 ? ? -102.26 -60.89 7 1 SER B 162 ? ? 63.17 70.74 8 1 TYR B 234 ? ? 77.11 -0.60 9 1 GLN B 282 ? ? 63.31 67.25 10 1 SER B 330 ? ? 60.87 68.85 11 1 THR B 348 ? ? -127.37 -61.76 12 1 GLU B 372 ? ? -106.74 -62.03 13 1 TRP B 420 ? ? -131.22 -57.72 14 1 ASN B 450 ? ? 60.15 66.94 15 1 ASP B 455 ? ? 58.47 -139.77 16 1 ASN B 500 ? ? 30.73 37.95 17 1 LYS B 512 ? ? -107.35 -74.87 18 1 ASN K 56 ? ? 177.62 160.37 19 1 PRO K 57 ? ? -90.16 42.97 20 1 HIS K 62 ? ? 65.56 -6.41 21 1 GLN K 96 ? ? -108.47 -61.13 22 1 SER K 102 ? ? 56.96 70.49 23 1 THR K 106 ? ? -126.13 -168.88 24 1 ASN K 174 ? ? 60.49 66.60 25 1 PHE K 187 ? ? -58.82 -9.78 26 1 ASN K 197 ? ? 61.74 71.94 27 1 LEU K 199 ? ? -73.17 -165.05 28 1 THR K 206 ? ? -126.60 -169.76 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 K ASN 27 ? CG ? C ASN 1 CG 2 1 Y 1 K ASN 27 ? OD1 ? C ASN 1 OD1 3 1 Y 1 K ASN 27 ? ND2 ? C ASN 1 ND2 4 1 Y 1 K VAL 55 ? CG1 ? C VAL 29 CG1 5 1 Y 1 K VAL 55 ? CG2 ? C VAL 29 CG2 6 1 Y 1 K GLU 68 ? CG ? C GLU 42 CG 7 1 Y 1 K GLU 68 ? CD ? C GLU 42 CD 8 1 Y 1 K GLU 68 ? OE1 ? C GLU 42 OE1 9 1 Y 1 K GLU 68 ? OE2 ? C GLU 42 OE2 10 1 Y 1 K LYS 93 ? CG ? C LYS 67 CG 11 1 Y 1 K LYS 93 ? CD ? C LYS 67 CD 12 1 Y 1 K LYS 93 ? CE ? C LYS 67 CE 13 1 Y 1 K LYS 93 ? NZ ? C LYS 67 NZ 14 1 Y 1 K VAL 205 ? CG1 ? C VAL 179 CG1 15 1 Y 1 K VAL 205 ? CG2 ? C VAL 179 CG2 # 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 B VAL 60 ? A VAL 29 2 1 Y 1 B ASN 61 ? A ASN 30 3 1 Y 1 B GLY 62 ? A GLY 31 4 1 Y 1 B GLN 63 ? A GLN 32 5 1 Y 1 B ASN 64 ? A ASN 33 # _pdbx_entity_nonpoly.entity_id 4 _pdbx_entity_nonpoly.name N-ACETYL-D-GLUCOSAMINE _pdbx_entity_nonpoly.comp_id NAG #