data_3WLJ # _entry.id 3WLJ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3WLJ RCSB RCSB096486 WWPDB D_1000096486 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1EX1 . unspecified PDB 1IEQ . unspecified PDB 1IEV . unspecified PDB 1IEW . unspecified PDB 1IEX . unspecified PDB 1J8V . unspecified PDB 3WLH . unspecified PDB 3WLI . unspecified PDB 3WLK . unspecified PDB 3WLL . unspecified PDB 3WLM . unspecified PDB 3WLN . unspecified PDB 3WLO . unspecified PDB 3WLP . unspecified PDB 3WLQ . unspecified PDB 3WLR . unspecified PDB 3WLS . unspecified PDB 3WLT . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3WLJ _pdbx_database_status.recvd_initial_deposition_date 2013-11-12 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.methods_development_category ? _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Streltsov, V.A.' 1 'Hrmova, M.' 2 # _citation.id primary _citation.title 'A landscape of the product and substrate trajectories in a glycoside hydrolase' _citation.journal_abbrev 'To be Published' _citation.journal_volume ? _citation.page_first ? _citation.page_last ? _citation.year ? _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Streltsov, V.A.' 1 primary 'Luang, S.' 2 primary 'Ketudat-Cairns, J.R.' 3 primary 'Raab, M.' 4 primary 'Tvaroska, I.' 5 primary 'Fort, S.' 6 primary 'Jimenez-Barbero, J.' 7 primary 'Peisley, A.' 8 primary 'Varghese, J.N.' 9 primary 'Hrmova, M.' 10 # _cell.entry_id 3WLJ _cell.length_a 100.816 _cell.length_b 100.816 _cell.length_c 181.646 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3WLJ _symmetry.space_group_name_H-M 'P 43 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 96 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'Beta-D-glucan exohydrolase isoenzyme ExoI' 65475.617 1 3.2.1.- ? 'UNP RESIDUES 26-630' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 3 ? ? ? ? 4 non-polymer man BETA-L-FUCOSE 164.156 2 ? ? ? ? 5 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 6 non-polymer man BETA-D-XYLOPYRANOSE 150.130 1 ? ? ? ? 7 non-polymer man BETA-D-GLUCOSE 180.156 1 ? ? ? ? 8 non-polymer man 3-deoxy-beta-D-ribo-hexopyranose 164.156 1 ? ? ? ? 9 non-polymer syn GLYCEROL 92.094 3 ? ? ? ? 10 non-polymer syn 'SULFATE ION' 96.063 1 ? ? ? ? 11 water nat water 18.015 830 ? ? ? ? # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDGFQKA CMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRWGRCY ESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKN AMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIMVPNK YQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGGFSYA IVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDALFGD FGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _entity_poly.pdbx_seq_one_letter_code_can ;DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDGFQKA CMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRWGRCY ESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKN AMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIMVPNK YQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGGFSYA IVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDALFGD FGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 TYR n 1 3 VAL n 1 4 LEU n 1 5 TYR n 1 6 LYS n 1 7 ASP n 1 8 ALA n 1 9 THR n 1 10 LYS n 1 11 PRO n 1 12 VAL n 1 13 GLU n 1 14 ASP n 1 15 ARG n 1 16 VAL n 1 17 ALA n 1 18 ASP n 1 19 LEU n 1 20 LEU n 1 21 GLY n 1 22 ARG n 1 23 MET n 1 24 THR n 1 25 LEU n 1 26 ALA n 1 27 GLU n 1 28 LYS n 1 29 ILE n 1 30 GLY n 1 31 GLN n 1 32 MET n 1 33 THR n 1 34 GLN n 1 35 ILE n 1 36 GLU n 1 37 ARG n 1 38 LEU n 1 39 VAL n 1 40 ALA n 1 41 THR n 1 42 PRO n 1 43 ASP n 1 44 VAL n 1 45 LEU n 1 46 ARG n 1 47 ASP n 1 48 ASN n 1 49 PHE n 1 50 ILE n 1 51 GLY n 1 52 SER n 1 53 LEU n 1 54 LEU n 1 55 SER n 1 56 GLY n 1 57 GLY n 1 58 GLY n 1 59 SER n 1 60 VAL n 1 61 PRO n 1 62 ARG n 1 63 LYS n 1 64 GLY n 1 65 ALA n 1 66 THR n 1 67 ALA n 1 68 LYS n 1 69 GLU n 1 70 TRP n 1 71 GLN n 1 72 ASP n 1 73 MET n 1 74 VAL n 1 75 ASP n 1 76 GLY n 1 77 PHE n 1 78 GLN n 1 79 LYS n 1 80 ALA n 1 81 CYS n 1 82 MET n 1 83 SER n 1 84 THR n 1 85 ARG n 1 86 LEU n 1 87 GLY n 1 88 ILE n 1 89 PRO n 1 90 MET n 1 91 ILE n 1 92 TYR n 1 93 GLY n 1 94 ILE n 1 95 ASP n 1 96 ALA n 1 97 VAL n 1 98 HIS n 1 99 GLY n 1 100 GLN n 1 101 ASN n 1 102 ASN n 1 103 VAL n 1 104 TYR n 1 105 GLY n 1 106 ALA n 1 107 THR n 1 108 ILE n 1 109 PHE n 1 110 PRO n 1 111 HIS n 1 112 ASN n 1 113 VAL n 1 114 GLY n 1 115 LEU n 1 116 GLY n 1 117 ALA n 1 118 THR n 1 119 ARG n 1 120 ASP n 1 121 PRO n 1 122 TYR n 1 123 LEU n 1 124 VAL n 1 125 LYS n 1 126 ARG n 1 127 ILE n 1 128 GLY n 1 129 GLU n 1 130 ALA n 1 131 THR n 1 132 ALA n 1 133 LEU n 1 134 GLU n 1 135 VAL n 1 136 ARG n 1 137 ALA n 1 138 THR n 1 139 GLY n 1 140 ILE n 1 141 GLN n 1 142 TYR n 1 143 ALA n 1 144 PHE n 1 145 ALA n 1 146 PRO n 1 147 CYS n 1 148 ILE n 1 149 ALA n 1 150 VAL n 1 151 CYS n 1 152 ARG n 1 153 ASP n 1 154 PRO n 1 155 ARG n 1 156 TRP n 1 157 GLY n 1 158 ARG n 1 159 CYS n 1 160 TYR n 1 161 GLU n 1 162 SER n 1 163 TYR n 1 164 SER n 1 165 GLU n 1 166 ASP n 1 167 ARG n 1 168 ARG n 1 169 ILE n 1 170 VAL n 1 171 GLN n 1 172 SER n 1 173 MET n 1 174 THR n 1 175 GLU n 1 176 LEU n 1 177 ILE n 1 178 PRO n 1 179 GLY n 1 180 LEU n 1 181 GLN n 1 182 GLY n 1 183 ASP n 1 184 VAL n 1 185 PRO n 1 186 LYS n 1 187 ASP n 1 188 PHE n 1 189 THR n 1 190 SER n 1 191 GLY n 1 192 MET n 1 193 PRO n 1 194 PHE n 1 195 VAL n 1 196 ALA n 1 197 GLY n 1 198 LYS n 1 199 ASN n 1 200 LYS n 1 201 VAL n 1 202 ALA n 1 203 ALA n 1 204 CYS n 1 205 ALA n 1 206 LYS n 1 207 HIS n 1 208 PHE n 1 209 VAL n 1 210 GLY n 1 211 ASP n 1 212 GLY n 1 213 GLY n 1 214 THR n 1 215 VAL n 1 216 ASP n 1 217 GLY n 1 218 ILE n 1 219 ASN n 1 220 GLU n 1 221 ASN n 1 222 ASN n 1 223 THR n 1 224 ILE n 1 225 ILE n 1 226 ASN n 1 227 ARG n 1 228 GLU n 1 229 GLY n 1 230 LEU n 1 231 MET n 1 232 ASN n 1 233 ILE n 1 234 HIS n 1 235 MET n 1 236 PRO n 1 237 ALA n 1 238 TYR n 1 239 LYS n 1 240 ASN n 1 241 ALA n 1 242 MET n 1 243 ASP n 1 244 LYS n 1 245 GLY n 1 246 VAL n 1 247 SER n 1 248 THR n 1 249 VAL n 1 250 MET n 1 251 ILE n 1 252 SER n 1 253 TYR n 1 254 SER n 1 255 SER n 1 256 TRP n 1 257 ASN n 1 258 GLY n 1 259 VAL n 1 260 LYS n 1 261 MET n 1 262 HIS n 1 263 ALA n 1 264 ASN n 1 265 GLN n 1 266 ASP n 1 267 LEU n 1 268 VAL n 1 269 THR n 1 270 GLY n 1 271 TYR n 1 272 LEU n 1 273 LYS n 1 274 ASP n 1 275 THR n 1 276 LEU n 1 277 LYS n 1 278 PHE n 1 279 LYS n 1 280 GLY n 1 281 PHE n 1 282 VAL n 1 283 ILE n 1 284 SER n 1 285 ASP n 1 286 TRP n 1 287 GLU n 1 288 GLY n 1 289 ILE n 1 290 ASP n 1 291 ARG n 1 292 ILE n 1 293 THR n 1 294 THR n 1 295 PRO n 1 296 ALA n 1 297 GLY n 1 298 SER n 1 299 ASP n 1 300 TYR n 1 301 SER n 1 302 TYR n 1 303 SER n 1 304 VAL n 1 305 LYS n 1 306 ALA n 1 307 SER n 1 308 ILE n 1 309 LEU n 1 310 ALA n 1 311 GLY n 1 312 LEU n 1 313 ASP n 1 314 MET n 1 315 ILE n 1 316 MET n 1 317 VAL n 1 318 PRO n 1 319 ASN n 1 320 LYS n 1 321 TYR n 1 322 GLN n 1 323 GLN n 1 324 PHE n 1 325 ILE n 1 326 SER n 1 327 ILE n 1 328 LEU n 1 329 THR n 1 330 GLY n 1 331 HIS n 1 332 VAL n 1 333 ASN n 1 334 GLY n 1 335 GLY n 1 336 VAL n 1 337 ILE n 1 338 PRO n 1 339 MET n 1 340 SER n 1 341 ARG n 1 342 ILE n 1 343 ASP n 1 344 ASP n 1 345 ALA n 1 346 VAL n 1 347 THR n 1 348 ARG n 1 349 ILE n 1 350 LEU n 1 351 ARG n 1 352 VAL n 1 353 LYS n 1 354 PHE n 1 355 THR n 1 356 MET n 1 357 GLY n 1 358 LEU n 1 359 PHE n 1 360 GLU n 1 361 ASN n 1 362 PRO n 1 363 TYR n 1 364 ALA n 1 365 ASP n 1 366 PRO n 1 367 ALA n 1 368 MET n 1 369 ALA n 1 370 GLU n 1 371 GLN n 1 372 LEU n 1 373 GLY n 1 374 LYS n 1 375 GLN n 1 376 GLU n 1 377 HIS n 1 378 ARG n 1 379 ASP n 1 380 LEU n 1 381 ALA n 1 382 ARG n 1 383 GLU n 1 384 ALA n 1 385 ALA n 1 386 ARG n 1 387 LYS n 1 388 SER n 1 389 LEU n 1 390 VAL n 1 391 LEU n 1 392 LEU n 1 393 LYS n 1 394 ASN n 1 395 GLY n 1 396 LYS n 1 397 THR n 1 398 SER n 1 399 THR n 1 400 ASP n 1 401 ALA n 1 402 PRO n 1 403 LEU n 1 404 LEU n 1 405 PRO n 1 406 LEU n 1 407 PRO n 1 408 LYS n 1 409 LYS n 1 410 ALA n 1 411 PRO n 1 412 LYS n 1 413 ILE n 1 414 LEU n 1 415 VAL n 1 416 ALA n 1 417 GLY n 1 418 SER n 1 419 HIS n 1 420 ALA n 1 421 ASP n 1 422 ASN n 1 423 LEU n 1 424 GLY n 1 425 TYR n 1 426 GLN n 1 427 CYS n 1 428 GLY n 1 429 GLY n 1 430 TRP n 1 431 THR n 1 432 ILE n 1 433 GLU n 1 434 TRP n 1 435 GLN n 1 436 GLY n 1 437 ASP n 1 438 THR n 1 439 GLY n 1 440 ARG n 1 441 THR n 1 442 THR n 1 443 VAL n 1 444 GLY n 1 445 THR n 1 446 THR n 1 447 ILE n 1 448 LEU n 1 449 GLU n 1 450 ALA n 1 451 VAL n 1 452 LYS n 1 453 ALA n 1 454 ALA n 1 455 VAL n 1 456 ASP n 1 457 PRO n 1 458 SER n 1 459 THR n 1 460 VAL n 1 461 VAL n 1 462 VAL n 1 463 PHE n 1 464 ALA n 1 465 GLU n 1 466 ASN n 1 467 PRO n 1 468 ASP n 1 469 ALA n 1 470 GLU n 1 471 PHE n 1 472 VAL n 1 473 LYS n 1 474 SER n 1 475 GLY n 1 476 GLY n 1 477 PHE n 1 478 SER n 1 479 TYR n 1 480 ALA n 1 481 ILE n 1 482 VAL n 1 483 ALA n 1 484 VAL n 1 485 GLY n 1 486 GLU n 1 487 HIS n 1 488 PRO n 1 489 TYR n 1 490 THR n 1 491 GLU n 1 492 THR n 1 493 LYS n 1 494 GLY n 1 495 ASP n 1 496 ASN n 1 497 LEU n 1 498 ASN n 1 499 LEU n 1 500 THR n 1 501 ILE n 1 502 PRO n 1 503 GLU n 1 504 PRO n 1 505 GLY n 1 506 LEU n 1 507 SER n 1 508 THR n 1 509 VAL n 1 510 GLN n 1 511 ALA n 1 512 VAL n 1 513 CYS n 1 514 GLY n 1 515 GLY n 1 516 VAL n 1 517 ARG n 1 518 CYS n 1 519 ALA n 1 520 THR n 1 521 VAL n 1 522 LEU n 1 523 ILE n 1 524 SER n 1 525 GLY n 1 526 ARG n 1 527 PRO n 1 528 VAL n 1 529 VAL n 1 530 VAL n 1 531 GLN n 1 532 PRO n 1 533 LEU n 1 534 LEU n 1 535 ALA n 1 536 ALA n 1 537 SER n 1 538 ASP n 1 539 ALA n 1 540 LEU n 1 541 VAL n 1 542 ALA n 1 543 ALA n 1 544 TRP n 1 545 LEU n 1 546 PRO n 1 547 GLY n 1 548 SER n 1 549 GLU n 1 550 GLY n 1 551 GLN n 1 552 GLY n 1 553 VAL n 1 554 THR n 1 555 ASP n 1 556 ALA n 1 557 LEU n 1 558 PHE n 1 559 GLY n 1 560 ASP n 1 561 PHE n 1 562 GLY n 1 563 PHE n 1 564 THR n 1 565 GLY n 1 566 ARG n 1 567 LEU n 1 568 PRO n 1 569 ARG n 1 570 THR n 1 571 TRP n 1 572 PHE n 1 573 LYS n 1 574 SER n 1 575 VAL n 1 576 ASP n 1 577 GLN n 1 578 LEU n 1 579 PRO n 1 580 MET n 1 581 ASN n 1 582 VAL n 1 583 GLY n 1 584 ASP n 1 585 ALA n 1 586 HIS n 1 587 TYR n 1 588 ASP n 1 589 PRO n 1 590 LEU n 1 591 PHE n 1 592 ARG n 1 593 LEU n 1 594 GLY n 1 595 TYR n 1 596 GLY n 1 597 LEU n 1 598 THR n 1 599 THR n 1 600 ASN n 1 601 ALA n 1 602 THR n 1 603 LYS n 1 604 LYS n 1 605 TYR n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'barley,two-rowed barley' _entity_src_nat.pdbx_organism_scientific 'Hordeum vulgare subsp. vulgare' _entity_src_nat.pdbx_ncbi_taxonomy_id 112509 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code Q9XEI3_HORVD _struct_ref.pdbx_db_accession Q9XEI3 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDGFQKA CMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRWGRCY ESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKN AMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIMVPNN YQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGGFSYA IVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDALFGD FGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _struct_ref.pdbx_align_begin 26 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3WLJ _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 605 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q9XEI3 _struct_ref_seq.db_align_beg 26 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 630 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 605 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 3WLJ _struct_ref_seq_dif.mon_id LYS _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 320 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code Q9XEI3 _struct_ref_seq_dif.db_mon_id ASN _struct_ref_seq_dif.pdbx_seq_db_seq_num 345 _struct_ref_seq_dif.details 'SEE REMARK 999' _struct_ref_seq_dif.pdbx_auth_seq_num 320 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 3DO saccharide . 3-deoxy-beta-D-ribo-hexopyranose ? 'C6 H12 O5' 164.156 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 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FUL L-saccharide . BETA-L-FUCOSE 6-DEOXY-BETA-L-GALACTOSE 'C6 H12 O5' 164.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 XYP D-saccharide . BETA-D-XYLOPYRANOSE ? 'C5 H10 O5' 150.130 # _exptl.entry_id 3WLJ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.55 _exptl_crystal.density_percent_sol 65.33 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.00 _exptl_crystal_grow.pdbx_details ;75mM HEPES-NaOH pH7.0 buffer, 1.2% PEG 400, 1.7M ammonium sulphate , pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 277K ; _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2005-11-20 _diffrn_detector.details 'RH COATED SI MIRROR' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'C(111) DOUBLE CRYSTAL' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.12714 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 14-ID-B' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 14-ID-B _diffrn_source.pdbx_wavelength 1.12714 _diffrn_source.pdbx_wavelength_list 1.12714 # _reflns.entry_id 3WLJ _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 34.18 _reflns.d_resolution_high 1.670 _reflns.number_obs 101919 _reflns.number_all ? _reflns.percent_possible_obs 99.0 _reflns.pdbx_Rmerge_I_obs 0.052 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 57.8 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 13.3 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.67 _reflns_shell.d_res_low 1.72 _reflns_shell.percent_possible_all 94.7 _reflns_shell.Rmerge_I_obs 0.619 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.11 _reflns_shell.pdbx_redundancy 7.1 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3WLJ _refine.ls_number_reflns_obs 101919 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 34.18 _refine.ls_d_res_high 1.67 _refine.ls_percent_reflns_obs 98.96 _refine.ls_R_factor_obs 0.16009 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.15879 _refine.ls_R_factor_R_free 0.18478 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 5362 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.972 _refine.correlation_coeff_Fo_to_Fc_free 0.966 _refine.B_iso_mean 26.369 _refine.aniso_B[1][1] 0.30 _refine.aniso_B[2][2] 0.30 _refine.aniso_B[3][3] -0.60 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB ENTRY 1X39' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.090 _refine.pdbx_overall_ESU_R_Free 0.074 _refine.overall_SU_ML 0.046 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 3.007 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _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 4566 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 217 _refine_hist.number_atoms_solvent 830 _refine_hist.number_atoms_total 5613 _refine_hist.d_res_high 1.67 _refine_hist.d_res_low 34.18 # 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_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.013 0.022 ? 4938 ? 'X-RAY DIFFRACTION' r_bond_other_d ? ? ? ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.408 2.011 ? 6727 ? 'X-RAY DIFFRACTION' r_angle_other_deg ? ? ? ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 5.983 5.000 ? 601 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 38.021 24.061 ? 197 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 13.357 15.000 ? 781 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 13.005 15.000 ? 29 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.098 0.200 ? 798 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.005 0.020 ? 3598 ? 'X-RAY DIFFRACTION' r_gen_planes_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_refined 0.200 0.200 ? 2629 ? 'X-RAY DIFFRACTION' r_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_refined 0.308 0.200 ? 3461 ? 'X-RAY DIFFRACTION' r_nbtor_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_refined 0.146 0.200 ? 612 ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_refined 0.234 0.200 ? 62 ? 'X-RAY DIFFRACTION' r_symmetry_vdw_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_refined 0.217 0.200 ? 47 ? 'X-RAY DIFFRACTION' r_symmetry_hbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcbond_it 1.024 1.500 ? 3070 ? 'X-RAY DIFFRACTION' r_mcbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcangle_it 1.518 2.000 ? 4822 ? 'X-RAY DIFFRACTION' r_mcangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scbond_it 4.696 3.000 ? 2091 ? 'X-RAY DIFFRACTION' r_scbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scangle_it 4.193 4.500 ? 1905 ? 'X-RAY DIFFRACTION' r_scangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_rigid_bond_restr 5.169 3.000 ? 5161 ? 'X-RAY DIFFRACTION' r_sphericity_free 4.546 3.000 ? 830 ? 'X-RAY DIFFRACTION' r_sphericity_bonded 4.463 3.000 ? 4827 ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.672 _refine_ls_shell.d_res_low 1.716 _refine_ls_shell.number_reflns_R_work 7095 _refine_ls_shell.R_factor_R_work 0.277 _refine_ls_shell.percent_reflns_obs 94.67 _refine_ls_shell.R_factor_R_free 0.351 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 389 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? # _struct.entry_id 3WLJ _struct.title 'Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with 3-deoxy-glucose' _struct.pdbx_descriptor 'Beta-D-glucan exohydrolase isoenzyme ExoI (E.C.3.2.1.-)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3WLJ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'BETA BARREL, HYDROLASE, GRAIN DEVELOPMENT, Enzyme Function Initiative, Tim Barrel/Beta sheet, N-glycosylation, plant apoplast' # 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 2 ? D N N 3 ? E N N 2 ? F N N 2 ? G N N 3 ? H N N 4 ? I N N 5 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 3 ? N N N 4 ? O N N 6 ? P N N 7 ? Q N N 8 ? R N N 9 ? S N N 9 ? T N N 9 ? U N N 10 ? V N N 11 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 VAL A 3 ? ASP A 7 ? VAL A 3 ASP A 7 5 ? 5 HELX_P HELX_P2 2 PRO A 11 ? GLY A 21 ? PRO A 11 GLY A 21 1 ? 11 HELX_P HELX_P3 3 THR A 24 ? MET A 32 ? THR A 24 MET A 32 1 ? 9 HELX_P HELX_P4 4 LEU A 38 ? ALA A 40 ? LEU A 38 ALA A 40 5 ? 3 HELX_P HELX_P5 5 THR A 41 ? ASN A 48 ? THR A 41 ASN A 48 1 ? 8 HELX_P HELX_P6 6 THR A 66 ? SER A 83 ? THR A 66 SER A 83 1 ? 18 HELX_P HELX_P7 7 HIS A 111 ? THR A 118 ? HIS A 111 THR A 118 1 ? 8 HELX_P HELX_P8 8 ASP A 120 ? ALA A 137 ? ASP A 120 ALA A 137 1 ? 18 HELX_P HELX_P9 9 ARG A 158 ? SER A 162 ? ARG A 158 SER A 162 5 ? 5 HELX_P HELX_P10 10 ASP A 166 ? THR A 174 ? ASP A 166 THR A 174 1 ? 9 HELX_P HELX_P11 11 GLU A 175 ? GLY A 182 ? GLU A 175 GLY A 182 1 ? 8 HELX_P HELX_P12 12 GLY A 210 ? ILE A 218 ? GLY A 210 ILE A 218 5 ? 9 HELX_P HELX_P13 13 ASN A 226 ? HIS A 234 ? ASN A 226 HIS A 234 1 ? 9 HELX_P HELX_P14 14 MET A 235 ? LYS A 244 ? MET A 235 LYS A 244 1 ? 10 HELX_P HELX_P15 15 ASN A 264 ? THR A 269 ? ASN A 264 THR A 269 1 ? 6 HELX_P HELX_P16 16 ILE A 289 ? THR A 293 ? ILE A 289 THR A 293 5 ? 5 HELX_P HELX_P17 17 ASP A 299 ? GLY A 311 ? ASP A 299 GLY A 311 1 ? 13 HELX_P HELX_P18 18 LYS A 320 ? GLY A 334 ? LYS A 320 GLY A 334 1 ? 15 HELX_P HELX_P19 19 PRO A 338 ? MET A 356 ? PRO A 338 MET A 356 1 ? 19 HELX_P HELX_P20 20 ASP A 365 ? LEU A 372 ? ASP A 365 LEU A 372 5 ? 8 HELX_P HELX_P21 21 LYS A 374 ? LEU A 389 ? LYS A 374 LEU A 389 1 ? 16 HELX_P HELX_P22 22 ASN A 422 ? GLY A 428 ? ASN A 422 GLY A 428 1 ? 7 HELX_P HELX_P23 23 THR A 446 ? VAL A 455 ? THR A 446 VAL A 455 1 ? 10 HELX_P HELX_P24 24 ASP A 468 ? GLY A 475 ? ASP A 468 GLY A 475 1 ? 8 HELX_P HELX_P25 25 THR A 490 ? ASP A 495 ? THR A 490 ASP A 495 5 ? 6 HELX_P HELX_P26 26 GLY A 505 ? VAL A 516 ? GLY A 505 VAL A 516 1 ? 12 HELX_P HELX_P27 27 VAL A 530 ? SER A 537 ? VAL A 530 SER A 537 1 ? 8 HELX_P HELX_P28 28 GLY A 550 ? PHE A 558 ? GLY A 550 PHE A 558 1 ? 9 HELX_P HELX_P29 29 SER A 574 ? LEU A 578 ? SER A 574 LEU A 578 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 151 SG ? ? ? 1_555 A CYS 159 SG ? ? A CYS 151 A CYS 159 1_555 ? ? ? ? ? ? ? 2.189 ? disulf2 disulf ? ? A CYS 513 SG ? ? ? 1_555 A CYS 518 SG A ? A CYS 513 A CYS 518 1_555 ? ? ? ? ? ? ? 2.011 ? disulf3 disulf ? ? A CYS 513 SG ? ? ? 1_555 A CYS 518 SG B ? A CYS 513 A CYS 518 1_555 ? ? ? ? ? ? ? 2.082 ? covale1 covale ? ? I MAN . O2 ? ? ? 1_555 J NAG . C1 ? ? A MAN 708 A NAG 709 1_555 ? ? ? ? ? ? ? 1.442 ? covale2 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 701 A NAG 702 1_555 ? ? ? ? ? ? ? 1.442 ? covale3 covale ? ? A ASN 221 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 221 A NAG 701 1_555 ? ? ? ? ? ? ? 1.443 ? covale4 covale ? ? A ASN 600 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 600 A NAG 710 1_555 ? ? ? ? ? ? ? 1.444 ? covale5 covale ? ? A ASN 498 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 498 A NAG 704 1_555 ? ? ? ? ? ? ? 1.450 ? covale6 covale ? ? K NAG . O4 ? ? ? 1_555 L NAG . C1 ? ? A NAG 710 A NAG 711 1_555 ? ? ? ? ? ? ? 1.450 ? covale7 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 704 A NAG 705 1_555 ? ? ? ? ? ? ? 1.453 ? covale8 covale ? ? G BMA . O6 ? ? ? 1_555 I MAN . C1 ? ? A BMA 706 A MAN 708 1_555 ? ? ? ? ? ? ? 1.440 ? covale9 covale ? ? M BMA . O2 ? ? ? 1_555 O XYP . C1B ? ? A BMA 712 A XYP 714 1_555 ? ? ? ? ? ? ? 1.442 ? covale10 covale ? ? C NAG . O4 ? ? ? 1_555 D BMA . C1 ? ? A NAG 702 A BMA 703 1_555 ? ? ? ? ? ? ? 1.446 ? covale11 covale ? ? L NAG . O4 ? ? ? 1_555 M BMA . C1 ? ? A NAG 711 A BMA 712 1_555 ? ? ? ? ? ? ? 1.447 ? covale12 covale ? ? F NAG . O4 ? ? ? 1_555 G BMA . C1 ? ? A NAG 705 A BMA 706 1_555 ? ? ? ? ? ? ? 1.447 ? covale13 covale ? ? K NAG . O3 ? ? ? 1_555 N FUL . C1 ? ? A NAG 710 A FUL 713 1_555 ? ? ? ? ? ? ? 1.452 ? covale14 covale ? ? E NAG . O3 ? ? ? 1_555 H FUL . C1 ? ? A NAG 704 A FUL 707 1_555 ? ? ? ? ? ? ? 1.453 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ALA 145 A . ? ALA 145 A PRO 146 A ? PRO 146 A 1 5.18 2 LYS 206 A . ? LYS 206 A HIS 207 A ? HIS 207 A 1 -6.57 3 PHE 208 A . ? PHE 208 A VAL 209 A ? VAL 209 A 1 -7.74 4 THR 294 A . ? THR 294 A PRO 295 A ? PRO 295 A 1 -4.90 5 VAL 317 A . ? VAL 317 A PRO 318 A ? PRO 318 A 1 -14.28 6 LEU 404 A . ? LEU 404 A PRO 405 A ? PRO 405 A 1 0.62 7 GLU 503 A . ? GLU 503 A PRO 504 A ? PRO 504 A 1 -1.60 8 LEU 578 A . ? LEU 578 A PRO 579 A ? PRO 579 A 1 -3.08 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 3 ? C ? 3 ? D ? 6 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel B 1 2 ? parallel B 2 3 ? parallel C 1 2 ? parallel C 2 3 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? parallel D 3 4 ? parallel D 4 5 ? parallel D 5 6 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 TYR A 142 ? ALA A 143 ? TYR A 142 ALA A 143 A 2 ILE A 91 ? ILE A 94 ? ILE A 91 ILE A 94 A 3 SER A 52 ? SER A 55 ? SER A 52 SER A 55 A 4 THR A 33 ? GLU A 36 ? THR A 33 GLU A 36 A 5 ILE A 315 ? MET A 316 ? ILE A 315 MET A 316 B 1 CYS A 204 ? PHE A 208 ? CYS A 204 PHE A 208 B 2 THR A 248 ? ILE A 251 ? THR A 248 ILE A 251 B 3 PHE A 281 ? ILE A 283 ? PHE A 281 ILE A 283 C 1 ASN A 222 ? THR A 223 ? ASN A 222 THR A 223 C 2 SER A 255 ? TRP A 256 ? SER A 255 TRP A 256 C 3 VAL A 259 ? LYS A 260 ? VAL A 259 LYS A 260 D 1 VAL A 390 ? ASN A 394 ? VAL A 390 ASN A 394 D 2 ALA A 539 ? TRP A 544 ? ALA A 539 TRP A 544 D 3 CYS A 518 ? ILE A 523 ? CYS A 518 ILE A 523 D 4 ALA A 480 ? GLY A 485 ? ALA A 480 GLY A 485 D 5 LYS A 412 ? ALA A 416 ? LYS A 412 ALA A 416 D 6 VAL A 460 ? ALA A 464 ? VAL A 460 ALA A 464 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O TYR A 142 ? O TYR A 142 N ILE A 94 ? N ILE A 94 A 2 3 O GLY A 93 ? O GLY A 93 N LEU A 53 ? N LEU A 53 A 3 4 O SER A 52 ? O SER A 52 N ILE A 35 ? N ILE A 35 A 4 5 N GLN A 34 ? N GLN A 34 O ILE A 315 ? O ILE A 315 B 1 2 N PHE A 208 ? N PHE A 208 O MET A 250 ? O MET A 250 B 2 3 N VAL A 249 ? N VAL A 249 O ILE A 283 ? O ILE A 283 C 1 2 N THR A 223 ? N THR A 223 O SER A 255 ? O SER A 255 C 2 3 N TRP A 256 ? N TRP A 256 O VAL A 259 ? O VAL A 259 D 1 2 N VAL A 390 ? N VAL A 390 O ALA A 542 ? O ALA A 542 D 2 3 O VAL A 541 ? O VAL A 541 N LEU A 522 ? N LEU A 522 D 3 4 O ILE A 523 ? O ILE A 523 N VAL A 484 ? N VAL A 484 D 4 5 O ALA A 483 ? O ALA A 483 N ALA A 416 ? N ALA A 416 D 5 6 N VAL A 415 ? N VAL A 415 O VAL A 462 ? O VAL A 462 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE BGC A 715' AC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE 3DO A 716' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE GOL A 717' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 718' AC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 719' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 720' AC7 Software ? ? ? ? 9 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 221 RESIDUES 701 TO 703' AC8 Software ? ? ? ? 19 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 498 RESIDUES 704 TO 709' AC9 Software ? ? ? ? 12 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 600 RESIDUES 710 TO 714' # 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 10 ASP A 95 ? ASP A 95 . ? 1_555 ? 2 AC1 10 ARG A 158 ? ARG A 158 . ? 1_555 ? 3 AC1 10 LYS A 206 ? LYS A 206 . ? 1_555 ? 4 AC1 10 HIS A 207 ? HIS A 207 . ? 1_555 ? 5 AC1 10 MET A 250 ? MET A 250 . ? 1_555 ? 6 AC1 10 TYR A 253 ? TYR A 253 . ? 1_555 ? 7 AC1 10 ASP A 285 ? ASP A 285 . ? 1_555 ? 8 AC1 10 GLU A 491 ? GLU A 491 . ? 1_555 ? 9 AC1 10 3DO Q . ? 3DO A 716 . ? 1_555 ? 10 AC1 10 HOH V . ? HOH A 1427 . ? 1_555 ? 11 AC2 10 GLY A 56 ? GLY A 56 . ? 1_555 ? 12 AC2 10 GLY A 57 ? GLY A 57 . ? 1_555 ? 13 AC2 10 TRP A 286 ? TRP A 286 . ? 1_555 ? 14 AC2 10 TRP A 430 ? TRP A 430 . ? 1_555 ? 15 AC2 10 TRP A 434 ? TRP A 434 . ? 1_555 ? 16 AC2 10 GLU A 491 ? GLU A 491 . ? 1_555 ? 17 AC2 10 BGC P . ? BGC A 715 . ? 1_555 ? 18 AC2 10 HOH V . ? HOH A 1492 . ? 1_555 ? 19 AC2 10 HOH V . ? HOH A 1588 . ? 1_555 ? 20 AC2 10 HOH V . ? HOH A 1589 . ? 1_555 ? 21 AC3 2 ARG A 386 ? ARG A 386 . ? 1_555 ? 22 AC3 2 LYS A 387 ? LYS A 387 . ? 1_555 ? 23 AC4 5 ARG A 119 ? ARG A 119 . ? 1_555 ? 24 AC4 5 ARG A 566 ? ARG A 566 . ? 1_555 ? 25 AC4 5 ARG A 592 ? ARG A 592 . ? 1_555 ? 26 AC4 5 GLY A 594 ? GLY A 594 . ? 1_555 ? 27 AC4 5 HOH V . ? HOH A 1557 . ? 1_555 ? 28 AC5 8 GLY A 21 ? GLY A 21 . ? 1_555 ? 29 AC5 8 ARG A 22 ? ARG A 22 . ? 1_555 ? 30 AC5 8 MET A 23 ? MET A 23 . ? 1_555 ? 31 AC5 8 THR A 24 ? THR A 24 . ? 1_555 ? 32 AC5 8 LYS A 452 ? LYS A 452 . ? 6_555 ? 33 AC5 8 ALA A 453 ? ALA A 453 . ? 6_555 ? 34 AC5 8 HOH V . ? HOH A 894 . ? 6_555 ? 35 AC5 8 HOH V . ? HOH A 1556 . ? 1_555 ? 36 AC6 5 PRO A 338 ? PRO A 338 . ? 1_555 ? 37 AC6 5 MET A 339 ? MET A 339 . ? 1_555 ? 38 AC6 5 SER A 340 ? SER A 340 . ? 1_555 ? 39 AC6 5 HOH V . ? HOH A 1434 . ? 1_555 ? 40 AC6 5 HOH V . ? HOH A 1441 . ? 1_555 ? 41 AC7 9 GLU A 220 ? GLU A 220 . ? 1_555 ? 42 AC7 9 ASN A 221 ? ASN A 221 . ? 1_555 ? 43 AC7 9 THR A 294 ? THR A 294 . ? 1_555 ? 44 AC7 9 HOH V . ? HOH A 948 . ? 1_555 ? 45 AC7 9 HOH V . ? HOH A 1124 . ? 1_555 ? 46 AC7 9 HOH V . ? HOH A 1178 . ? 1_555 ? 47 AC7 9 HOH V . ? HOH A 1206 . ? 1_555 ? 48 AC7 9 HOH V . ? HOH A 1270 . ? 1_555 ? 49 AC7 9 HOH V . ? HOH A 1607 . ? 1_555 ? 50 AC8 19 TYR A 425 ? TYR A 425 . ? 1_555 ? 51 AC8 19 HIS A 487 ? HIS A 487 . ? 1_555 ? 52 AC8 19 ASN A 496 ? ASN A 496 . ? 1_555 ? 53 AC8 19 ASN A 498 ? ASN A 498 . ? 1_555 ? 54 AC8 19 THR A 500 ? THR A 500 . ? 1_555 ? 55 AC8 19 GLU A 503 ? GLU A 503 . ? 1_555 ? 56 AC8 19 HOH V . ? HOH A 916 . ? 1_555 ? 57 AC8 19 HOH V . ? HOH A 921 . ? 1_555 ? 58 AC8 19 HOH V . ? HOH A 939 . ? 1_555 ? 59 AC8 19 HOH V . ? HOH A 1047 . ? 1_555 ? 60 AC8 19 HOH V . ? HOH A 1216 . ? 1_555 ? 61 AC8 19 HOH V . ? HOH A 1236 . ? 1_555 ? 62 AC8 19 HOH V . ? HOH A 1371 . ? 1_555 ? 63 AC8 19 HOH V . ? HOH A 1481 . ? 1_555 ? 64 AC8 19 HOH V . ? HOH A 1506 . ? 1_555 ? 65 AC8 19 HOH V . ? HOH A 1603 . ? 1_555 ? 66 AC8 19 HOH V . ? HOH A 1610 . ? 1_555 ? 67 AC8 19 HOH V . ? HOH A 1620 . ? 1_555 ? 68 AC8 19 HOH V . ? HOH A 1628 . ? 1_555 ? 69 AC9 12 THR A 118 ? THR A 118 . ? 1_555 ? 70 AC9 12 ARG A 119 ? ARG A 119 . ? 1_555 ? 71 AC9 12 ASP A 120 ? ASP A 120 . ? 1_555 ? 72 AC9 12 ARG A 566 ? ARG A 566 . ? 1_555 ? 73 AC9 12 THR A 598 ? THR A 598 . ? 1_555 ? 74 AC9 12 ASN A 600 ? ASN A 600 . ? 1_555 ? 75 AC9 12 HOH V . ? HOH A 1034 . ? 1_555 ? 76 AC9 12 HOH V . ? HOH A 1042 . ? 1_555 ? 77 AC9 12 HOH V . ? HOH A 1131 . ? 1_555 ? 78 AC9 12 HOH V . ? HOH A 1171 . ? 1_555 ? 79 AC9 12 HOH V . ? HOH A 1239 . ? 1_555 ? 80 AC9 12 HOH V . ? HOH A 1254 . ? 1_555 ? # _database_PDB_matrix.entry_id 3WLJ _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 3WLJ _atom_sites.fract_transf_matrix[1][1] 0.009919 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.009919 _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] 0.005505 _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 . ASP A 1 1 ? 30.445 5.245 -2.199 1.00 34.12 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 29.676 4.018 -1.843 1.00 33.99 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 28.602 4.329 -0.797 1.00 33.80 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 28.335 5.496 -0.492 1.00 33.74 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 30.613 2.897 -1.365 1.00 34.40 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 31.489 3.303 -0.174 1.00 35.54 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 31.464 4.484 0.263 1.00 35.94 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 32.219 2.419 0.327 1.00 36.59 ? 1 ASP A OD2 1 ATOM 9 N N . TYR A 1 2 ? 27.986 3.270 -0.284 1.00 33.35 ? 2 TYR A N 1 ATOM 10 C CA . TYR A 1 2 ? 26.962 3.369 0.744 1.00 32.36 ? 2 TYR A CA 1 ATOM 11 C C . TYR A 1 2 ? 27.592 3.827 2.071 1.00 31.58 ? 2 TYR A C 1 ATOM 12 O O . TYR A 1 2 ? 28.648 3.313 2.480 1.00 31.64 ? 2 TYR A O 1 ATOM 13 C CB . TYR A 1 2 ? 26.278 2.014 0.885 1.00 32.64 ? 2 TYR A CB 1 ATOM 14 C CG . TYR A 1 2 ? 25.460 1.826 2.140 1.00 32.83 ? 2 TYR A CG 1 ATOM 15 C CD1 . TYR A 1 2 ? 24.178 2.378 2.255 1.00 32.76 ? 2 TYR A CD1 1 ATOM 16 C CD2 . TYR A 1 2 ? 25.954 1.060 3.196 1.00 33.31 ? 2 TYR A CD2 1 ATOM 17 C CE1 . TYR A 1 2 ? 23.421 2.188 3.406 1.00 31.73 ? 2 TYR A CE1 1 ATOM 18 C CE2 . TYR A 1 2 ? 25.201 0.855 4.342 1.00 33.36 ? 2 TYR A CE2 1 ATOM 19 C CZ . TYR A 1 2 ? 23.943 1.429 4.437 1.00 32.69 ? 2 TYR A CZ 1 ATOM 20 O OH . TYR A 1 2 ? 23.228 1.208 5.577 1.00 32.55 ? 2 TYR A OH 1 ATOM 21 N N . VAL A 1 3 ? 26.933 4.792 2.722 1.00 29.84 ? 3 VAL A N 1 ATOM 22 C CA . VAL A 1 3 ? 27.423 5.369 3.976 1.00 28.73 ? 3 VAL A CA 1 ATOM 23 C C . VAL A 1 3 ? 26.467 4.961 5.098 1.00 28.41 ? 3 VAL A C 1 ATOM 24 O O . VAL A 1 3 ? 25.372 5.522 5.232 1.00 28.38 ? 3 VAL A O 1 ATOM 25 C CB . VAL A 1 3 ? 27.571 6.907 3.874 1.00 28.53 ? 3 VAL A CB 1 ATOM 26 C CG1 . VAL A 1 3 ? 27.986 7.531 5.223 1.00 27.90 ? 3 VAL A CG1 1 ATOM 27 C CG2 . VAL A 1 3 ? 28.594 7.273 2.799 1.00 28.63 ? 3 VAL A CG2 1 ATOM 28 N N . LEU A 1 4 ? 26.896 3.974 5.881 1.00 27.59 ? 4 LEU A N 1 ATOM 29 C CA . LEU A 1 4 ? 26.033 3.329 6.859 1.00 27.47 ? 4 LEU A CA 1 ATOM 30 C C . LEU A 1 4 ? 25.492 4.313 7.900 1.00 26.85 ? 4 LEU A C 1 ATOM 31 O O . LEU A 1 4 ? 24.320 4.236 8.247 1.00 26.27 ? 4 LEU A O 1 ATOM 32 C CB . LEU A 1 4 ? 26.739 2.144 7.528 1.00 27.93 ? 4 LEU A CB 1 ATOM 33 C CG . LEU A 1 4 ? 25.922 1.171 8.384 1.00 28.51 ? 4 LEU A CG 1 ATOM 34 C CD1 . LEU A 1 4 ? 26.621 -0.184 8.443 1.00 31.05 ? 4 LEU A CD1 1 ATOM 35 C CD2 . LEU A 1 4 ? 25.670 1.691 9.806 1.00 29.13 ? 4 LEU A CD2 1 ATOM 36 N N . TYR A 1 5 ? 26.311 5.252 8.370 1.00 25.75 ? 5 TYR A N 1 ATOM 37 C CA . TYR A 1 5 ? 25.827 6.109 9.472 1.00 25.14 ? 5 TYR A CA 1 ATOM 38 C C . TYR A 1 5 ? 24.672 7.029 9.067 1.00 25.28 ? 5 TYR A C 1 ATOM 39 O O . TYR A 1 5 ? 23.927 7.523 9.934 1.00 25.23 ? 5 TYR A O 1 ATOM 40 C CB . TYR A 1 5 ? 26.966 6.892 10.135 1.00 24.08 ? 5 TYR A CB 1 ATOM 41 C CG . TYR A 1 5 ? 27.424 8.164 9.433 1.00 23.84 ? 5 TYR A CG 1 ATOM 42 C CD1 . TYR A 1 5 ? 26.770 9.390 9.651 1.00 22.86 ? 5 TYR A CD1 1 ATOM 43 C CD2 . TYR A 1 5 ? 28.548 8.156 8.584 1.00 24.30 ? 5 TYR A CD2 1 ATOM 44 C CE1 . TYR A 1 5 ? 27.208 10.579 9.027 1.00 21.88 ? 5 TYR A CE1 1 ATOM 45 C CE2 . TYR A 1 5 ? 29.000 9.325 7.968 1.00 22.58 ? 5 TYR A CE2 1 ATOM 46 C CZ . TYR A 1 5 ? 28.329 10.529 8.184 1.00 22.87 ? 5 TYR A CZ 1 ATOM 47 O OH . TYR A 1 5 ? 28.773 11.677 7.583 1.00 22.62 ? 5 TYR A OH 1 ATOM 48 N N . LYS A 1 6 ? 24.521 7.264 7.763 1.00 25.95 ? 6 LYS A N 1 ATOM 49 C CA . LYS A 1 6 ? 23.450 8.120 7.261 1.00 27.01 ? 6 LYS A CA 1 ATOM 50 C C . LYS A 1 6 ? 22.163 7.340 7.022 1.00 27.40 ? 6 LYS A C 1 ATOM 51 O O . LYS A 1 6 ? 21.158 7.918 6.619 1.00 28.32 ? 6 LYS A O 1 ATOM 52 C CB . LYS A 1 6 ? 23.873 8.824 5.971 1.00 27.29 ? 6 LYS A CB 1 ATOM 53 C CG . LYS A 1 6 ? 24.928 9.888 6.212 1.00 27.71 ? 6 LYS A CG 1 ATOM 54 C CD . LYS A 1 6 ? 25.249 10.682 4.969 1.00 29.82 ? 6 LYS A CD 1 ATOM 55 C CE . LYS A 1 6 ? 26.324 11.728 5.318 1.00 31.16 ? 6 LYS A CE 1 ATOM 56 N NZ . LYS A 1 6 ? 26.677 12.579 4.166 1.00 33.00 ? 6 LYS A NZ 1 ATOM 57 N N . ASP A 1 7 ? 22.203 6.038 7.270 1.00 27.33 ? 7 ASP A N 1 ATOM 58 C CA . ASP A 1 7 ? 21.047 5.180 7.012 1.00 27.69 ? 7 ASP A CA 1 ATOM 59 C C . ASP A 1 7 ? 20.191 5.032 8.274 1.00 27.60 ? 7 ASP A C 1 ATOM 60 O O . ASP A 1 7 ? 20.564 4.326 9.201 1.00 27.35 ? 7 ASP A O 1 ATOM 61 C CB . ASP A 1 7 ? 21.528 3.819 6.496 1.00 27.69 ? 7 ASP A CB 1 ATOM 62 C CG . ASP A 1 7 ? 20.378 2.878 6.094 1.00 29.10 ? 7 ASP A CG 1 ATOM 63 O OD1 . ASP A 1 7 ? 20.692 1.817 5.502 1.00 28.77 ? 7 ASP A OD1 1 ATOM 64 O OD2 . ASP A 1 7 ? 19.188 3.173 6.373 1.00 30.03 ? 7 ASP A OD2 1 ATOM 65 N N . ALA A 1 8 ? 19.040 5.696 8.280 1.00 28.42 ? 8 ALA A N 1 ATOM 66 C CA . ALA A 1 8 ? 18.130 5.702 9.438 1.00 29.24 ? 8 ALA A CA 1 ATOM 67 C C . ALA A 1 8 ? 17.578 4.329 9.846 1.00 29.83 ? 8 ALA A C 1 ATOM 68 O O . ALA A 1 8 ? 17.115 4.158 10.973 1.00 30.07 ? 8 ALA A O 1 ATOM 69 C CB . ALA A 1 8 ? 16.998 6.671 9.201 1.00 29.29 ? 8 ALA A CB 1 ATOM 70 N N . THR A 1 9 ? 17.637 3.353 8.939 1.00 30.49 ? 9 THR A N 1 ATOM 71 C CA . THR A 1 9 ? 17.127 2.005 9.227 1.00 30.93 ? 9 THR A CA 1 ATOM 72 C C . THR A 1 9 ? 18.125 1.124 9.991 1.00 31.01 ? 9 THR A C 1 ATOM 73 O O . THR A 1 9 ? 17.790 0.001 10.392 1.00 32.06 ? 9 THR A O 1 ATOM 74 C CB . THR A 1 9 ? 16.712 1.269 7.933 1.00 30.86 ? 9 THR A CB 1 ATOM 75 O OG1 . THR A 1 9 ? 17.881 0.925 7.175 1.00 31.26 ? 9 THR A OG1 1 ATOM 76 C CG2 . THR A 1 9 ? 15.772 2.125 7.091 1.00 30.95 ? 9 THR A CG2 1 ATOM 77 N N . LYS A 1 10 ? 19.351 1.618 10.174 1.00 30.48 ? 10 LYS A N 1 ATOM 78 C CA . LYS A 1 10 ? 20.418 0.831 10.793 1.00 30.12 ? 10 LYS A CA 1 ATOM 79 C C . LYS A 1 10 ? 20.455 0.990 12.320 1.00 29.38 ? 10 LYS A C 1 ATOM 80 O O . LYS A 1 10 ? 20.133 2.070 12.827 1.00 29.03 ? 10 LYS A O 1 ATOM 81 C CB . LYS A 1 10 ? 21.783 1.212 10.194 1.00 30.74 ? 10 LYS A CB 1 ATOM 82 C CG . LYS A 1 10 ? 22.021 0.687 8.777 1.00 32.84 ? 10 LYS A CG 1 ATOM 83 C CD . LYS A 1 10 ? 22.339 -0.813 8.801 1.00 36.34 ? 10 LYS A CD 1 ATOM 84 C CE . LYS A 1 10 ? 21.565 -1.565 7.725 1.00 40.14 ? 10 LYS A CE 1 ATOM 85 N NZ . LYS A 1 10 ? 21.682 -0.972 6.375 1.00 42.16 ? 10 LYS A NZ 1 ATOM 86 N N . PRO A 1 11 ? 20.856 -0.074 13.049 1.00 28.57 ? 11 PRO A N 1 ATOM 87 C CA . PRO A 1 11 ? 20.973 -0.001 14.507 1.00 28.01 ? 11 PRO A CA 1 ATOM 88 C C . PRO A 1 11 ? 21.899 1.115 14.944 1.00 26.90 ? 11 PRO A C 1 ATOM 89 O O . PRO A 1 11 ? 22.919 1.368 14.292 1.00 25.98 ? 11 PRO A O 1 ATOM 90 C CB . PRO A 1 11 ? 21.612 -1.340 14.878 1.00 28.40 ? 11 PRO A CB 1 ATOM 91 C CG . PRO A 1 11 ? 21.172 -2.266 13.783 1.00 29.17 ? 11 PRO A CG 1 ATOM 92 C CD . PRO A 1 11 ? 21.208 -1.422 12.550 1.00 29.31 ? 11 PRO A CD 1 ATOM 93 N N . VAL A 1 12 ? 21.541 1.777 16.044 1.00 25.80 ? 12 VAL A N 1 ATOM 94 C CA . VAL A 1 12 ? 22.360 2.852 16.584 1.00 25.25 ? 12 VAL A CA 1 ATOM 95 C C . VAL A 1 12 ? 23.838 2.469 16.734 1.00 24.96 ? 12 VAL A C 1 ATOM 96 O O . VAL A 1 12 ? 24.711 3.207 16.289 1.00 24.68 ? 12 VAL A O 1 ATOM 97 C CB . VAL A 1 12 ? 21.769 3.384 17.930 1.00 24.95 ? 12 VAL A CB 1 ATOM 98 C CG1 . VAL A 1 12 ? 22.745 4.356 18.620 1.00 24.39 ? 12 VAL A CG1 1 ATOM 99 C CG2 . VAL A 1 12 ? 20.426 4.062 17.671 1.00 26.07 ? 12 VAL A CG2 1 ATOM 100 N N . GLU A 1 13 ? 24.134 1.322 17.345 1.00 25.10 ? 13 GLU A N 1 ATOM 101 C CA . GLU A 1 13 ? 25.545 0.966 17.564 1.00 25.64 ? 13 GLU A CA 1 ATOM 102 C C . GLU A 1 13 ? 26.348 0.861 16.253 1.00 25.81 ? 13 GLU A C 1 ATOM 103 O O . GLU A 1 13 ? 27.510 1.257 16.205 1.00 25.49 ? 13 GLU A O 1 ATOM 104 C CB . GLU A 1 13 ? 25.677 -0.312 18.384 1.00 26.34 ? 13 GLU A CB 1 ATOM 105 C CG . GLU A 1 13 ? 25.134 -0.194 19.812 1.00 26.95 ? 13 GLU A CG 1 ATOM 106 C CD . GLU A 1 13 ? 25.751 0.964 20.607 1.00 30.51 ? 13 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 13 ? 24.967 1.746 21.193 1.00 31.26 ? 13 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 13 ? 27.006 1.095 20.651 1.00 29.10 ? 13 GLU A OE2 1 ATOM 109 N N . ASP A 1 14 ? 25.715 0.343 15.205 1.00 26.05 ? 14 ASP A N 1 ATOM 110 C CA . ASP A 1 14 ? 26.353 0.264 13.882 1.00 26.51 ? 14 ASP A CA 1 ATOM 111 C C . ASP A 1 14 ? 26.601 1.649 13.289 1.00 25.36 ? 14 ASP A C 1 ATOM 112 O O . ASP A 1 14 ? 27.672 1.923 12.728 1.00 25.71 ? 14 ASP A O 1 ATOM 113 C CB . ASP A 1 14 ? 25.508 -0.573 12.921 1.00 27.19 ? 14 ASP A CB 1 ATOM 114 C CG . ASP A 1 14 ? 25.396 -2.036 13.347 1.00 32.41 ? 14 ASP A CG 1 ATOM 115 O OD1 . ASP A 1 14 ? 26.277 -2.547 14.075 1.00 35.42 ? 14 ASP A OD1 1 ATOM 116 O OD2 . ASP A 1 14 ? 24.416 -2.682 12.935 1.00 37.11 ? 14 ASP A OD2 1 ATOM 117 N N . ARG A 1 15 ? 25.617 2.530 13.425 1.00 24.49 ? 15 ARG A N 1 ATOM 118 C CA . ARG A 1 15 ? 25.757 3.906 12.939 1.00 22.95 ? 15 ARG A CA 1 ATOM 119 C C . ARG A 1 15 ? 26.865 4.641 13.684 1.00 22.85 ? 15 ARG A C 1 ATOM 120 O O . ARG A 1 15 ? 27.675 5.352 13.065 1.00 22.62 ? 15 ARG A O 1 ATOM 121 C CB . ARG A 1 15 ? 24.426 4.658 13.052 1.00 23.03 ? 15 ARG A CB 1 ATOM 122 C CG . ARG A 1 15 ? 23.314 4.026 12.208 1.00 23.02 ? 15 ARG A CG 1 ATOM 123 C CD . ARG A 1 15 ? 22.010 4.811 12.326 1.00 22.64 ? 15 ARG A CD 1 ATOM 124 N NE . ARG A 1 15 ? 22.035 6.068 11.582 1.00 22.54 ? 15 ARG A NE 1 ATOM 125 C CZ . ARG A 1 15 ? 21.064 6.985 11.616 1.00 22.37 ? 15 ARG A CZ 1 ATOM 126 N NH1 . ARG A 1 15 ? 19.980 6.799 12.388 1.00 22.89 ? 15 ARG A NH1 1 ATOM 127 N NH2 . ARG A 1 15 ? 21.176 8.096 10.899 1.00 22.36 ? 15 ARG A NH2 1 ATOM 128 N N . VAL A 1 16 ? 26.877 4.495 15.010 1.00 22.34 ? 16 VAL A N 1 ATOM 129 C CA . VAL A 1 16 ? 27.960 5.057 15.832 1.00 22.88 ? 16 VAL A CA 1 ATOM 130 C C . VAL A 1 16 ? 29.336 4.596 15.343 1.00 23.02 ? 16 VAL A C 1 ATOM 131 O O . VAL A 1 16 ? 30.201 5.431 15.102 1.00 23.30 ? 16 VAL A O 1 ATOM 132 C CB . VAL A 1 16 ? 27.802 4.724 17.335 1.00 22.84 ? 16 VAL A CB 1 ATOM 133 C CG1 . VAL A 1 16 ? 29.035 5.139 18.107 1.00 23.08 ? 16 VAL A CG1 1 ATOM 134 C CG2 . VAL A 1 16 ? 26.566 5.439 17.912 1.00 22.72 ? 16 VAL A CG2 1 ATOM 135 N N . ALA A 1 17 ? 29.528 3.281 15.217 1.00 23.08 ? 17 ALA A N 1 ATOM 136 C CA . ALA A 1 17 ? 30.842 2.725 14.846 1.00 23.27 ? 17 ALA A CA 1 ATOM 137 C C . ALA A 1 17 ? 31.241 3.182 13.444 1.00 23.75 ? 17 ALA A C 1 ATOM 138 O O . ALA A 1 17 ? 32.407 3.549 13.205 1.00 24.32 ? 17 ALA A O 1 ATOM 139 C CB . ALA A 1 17 ? 30.842 1.204 14.947 1.00 24.00 ? 17 ALA A CB 1 ATOM 140 N N . ASP A 1 18 ? 30.270 3.202 12.539 1.00 23.31 ? 18 ASP A N 1 ATOM 141 C CA . ASP A 1 18 ? 30.543 3.599 11.157 1.00 23.68 ? 18 ASP A CA 1 ATOM 142 C C . ASP A 1 18 ? 30.984 5.050 11.072 1.00 23.46 ? 18 ASP A C 1 ATOM 143 O O . ASP A 1 18 ? 31.931 5.390 10.355 1.00 24.27 ? 18 ASP A O 1 ATOM 144 C CB . ASP A 1 18 ? 29.333 3.375 10.265 1.00 23.77 ? 18 ASP A CB 1 ATOM 145 C CG . ASP A 1 18 ? 29.634 3.696 8.824 1.00 24.93 ? 18 ASP A CG 1 ATOM 146 O OD1 . ASP A 1 18 ? 30.246 2.835 8.158 1.00 28.87 ? 18 ASP A OD1 1 ATOM 147 O OD2 . ASP A 1 18 ? 29.285 4.800 8.370 1.00 25.71 ? 18 ASP A OD2 1 ATOM 148 N N . LEU A 1 19 ? 30.301 5.922 11.807 1.00 22.51 ? 19 LEU A N 1 ATOM 149 C CA . LEU A 1 19 ? 30.672 7.326 11.802 1.00 21.61 ? 19 LEU A CA 1 ATOM 150 C C . LEU A 1 19 ? 32.016 7.551 12.503 1.00 21.58 ? 19 LEU A C 1 ATOM 151 O O . LEU A 1 19 ? 32.857 8.276 11.993 1.00 21.71 ? 19 LEU A O 1 ATOM 152 C CB . LEU A 1 19 ? 29.577 8.182 12.447 1.00 21.89 ? 19 LEU A CB 1 ATOM 153 C CG . LEU A 1 19 ? 29.839 9.675 12.614 1.00 21.05 ? 19 LEU A CG 1 ATOM 154 C CD1 . LEU A 1 19 ? 30.284 10.327 11.288 1.00 22.77 ? 19 LEU A CD1 1 ATOM 155 C CD2 . LEU A 1 19 ? 28.605 10.387 13.165 1.00 21.02 ? 19 LEU A CD2 1 ATOM 156 N N . LEU A 1 20 ? 32.207 6.937 13.668 1.00 21.54 ? 20 LEU A N 1 ATOM 157 C CA . LEU A 1 20 ? 33.425 7.127 14.459 1.00 22.08 ? 20 LEU A CA 1 ATOM 158 C C . LEU A 1 20 ? 34.666 6.793 13.618 1.00 22.68 ? 20 LEU A C 1 ATOM 159 O O . LEU A 1 20 ? 35.659 7.509 13.658 1.00 22.26 ? 20 LEU A O 1 ATOM 160 C CB . LEU A 1 20 ? 33.396 6.242 15.707 1.00 22.25 ? 20 LEU A CB 1 ATOM 161 C CG . LEU A 1 20 ? 34.569 6.362 16.686 1.00 22.27 ? 20 LEU A CG 1 ATOM 162 C CD1 . LEU A 1 20 ? 34.605 7.763 17.382 1.00 23.28 ? 20 LEU A CD1 1 ATOM 163 C CD2 . LEU A 1 20 ? 34.528 5.205 17.716 1.00 23.69 ? 20 LEU A CD2 1 ATOM 164 N N . GLY A 1 21 ? 34.567 5.706 12.861 1.00 23.33 ? 21 GLY A N 1 ATOM 165 C CA . GLY A 1 21 ? 35.686 5.214 12.056 1.00 24.31 ? 21 GLY A CA 1 ATOM 166 C C . GLY A 1 21 ? 36.117 6.151 10.946 1.00 24.87 ? 21 GLY A C 1 ATOM 167 O O . GLY A 1 21 ? 37.207 5.976 10.384 1.00 26.39 ? 21 GLY A O 1 ATOM 168 N N . ARG A 1 22 ? 35.283 7.143 10.636 1.00 24.35 ? 22 ARG A N 1 ATOM 169 C CA . ARG A 1 22 ? 35.548 8.112 9.562 1.00 23.73 ? 22 ARG A CA 1 ATOM 170 C C . ARG A 1 22 ? 36.127 9.441 10.057 1.00 23.34 ? 22 ARG A C 1 ATOM 171 O O . ARG A 1 22 ? 36.558 10.282 9.253 1.00 23.99 ? 22 ARG A O 1 ATOM 172 C CB . ARG A 1 22 ? 34.259 8.412 8.794 1.00 23.54 ? 22 ARG A CB 1 ATOM 173 C CG . ARG A 1 22 ? 33.573 7.199 8.186 1.00 24.20 ? 22 ARG A CG 1 ATOM 174 C CD . ARG A 1 22 ? 32.210 7.562 7.674 1.00 26.14 ? 22 ARG A CD 1 ATOM 175 N NE . ARG A 1 22 ? 31.466 6.384 7.253 1.00 26.75 ? 22 ARG A NE 1 ATOM 176 C CZ . ARG A 1 22 ? 31.501 5.878 6.029 1.00 28.81 ? 22 ARG A CZ 1 ATOM 177 N NH1 . ARG A 1 22 ? 32.271 6.440 5.102 1.00 30.21 ? 22 ARG A NH1 1 ATOM 178 N NH2 . ARG A 1 22 ? 30.778 4.803 5.737 1.00 30.36 ? 22 ARG A NH2 1 ATOM 179 N N . MET A 1 23 ? 36.123 9.652 11.374 1.00 22.51 ? 23 MET A N 1 ATOM 180 C CA . MET A 1 23 ? 36.367 10.982 11.917 1.00 21.67 ? 23 MET A CA 1 ATOM 181 C C . MET A 1 23 ? 37.841 11.291 12.139 1.00 21.37 ? 23 MET A C 1 ATOM 182 O O . MET A 1 23 ? 38.601 10.443 12.622 1.00 22.58 ? 23 MET A O 1 ATOM 183 C CB . MET A 1 23 ? 35.611 11.150 13.254 1.00 21.33 ? 23 MET A CB 1 ATOM 184 C CG . MET A 1 23 ? 34.089 11.131 13.077 1.00 21.41 ? 23 MET A CG 1 ATOM 185 S SD . MET A 1 23 ? 33.191 11.079 14.647 1.00 21.16 ? 23 MET A SD 1 ATOM 186 C CE . MET A 1 23 ? 33.444 12.765 15.209 1.00 21.31 ? 23 MET A CE 1 ATOM 187 N N . THR A 1 24 ? 38.230 12.520 11.818 1.00 21.62 ? 24 THR A N 1 ATOM 188 C CA . THR A 1 24 ? 39.549 13.032 12.182 1.00 21.80 ? 24 THR A CA 1 ATOM 189 C C . THR A 1 24 ? 39.617 13.378 13.672 1.00 21.81 ? 24 THR A C 1 ATOM 190 O O . THR A 1 24 ? 38.571 13.473 14.360 1.00 20.90 ? 24 THR A O 1 ATOM 191 C CB . THR A 1 24 ? 39.902 14.316 11.402 1.00 22.06 ? 24 THR A CB 1 ATOM 192 O OG1 . THR A 1 24 ? 39.060 15.391 11.841 1.00 21.30 ? 24 THR A OG1 1 ATOM 193 C CG2 . THR A 1 24 ? 39.757 14.109 9.868 1.00 21.93 ? 24 THR A CG2 1 ATOM 194 N N . LEU A 1 25 ? 40.832 13.612 14.167 1.00 22.18 ? 25 LEU A N 1 ATOM 195 C CA . LEU A 1 25 ? 40.985 14.063 15.544 1.00 22.61 ? 25 LEU A CA 1 ATOM 196 C C . LEU A 1 25 ? 40.220 15.354 15.800 1.00 22.23 ? 25 LEU A C 1 ATOM 197 O O . LEU A 1 25 ? 39.549 15.470 16.831 1.00 20.78 ? 25 LEU A O 1 ATOM 198 C CB . LEU A 1 25 ? 42.469 14.219 15.926 1.00 23.14 ? 25 LEU A CB 1 ATOM 199 C CG . LEU A 1 25 ? 42.732 14.691 17.364 1.00 22.89 ? 25 LEU A CG 1 ATOM 200 C CD1 . LEU A 1 25 ? 42.072 13.743 18.384 1.00 25.73 ? 25 LEU A CD1 1 ATOM 201 C CD2 . LEU A 1 25 ? 44.239 14.811 17.592 1.00 23.69 ? 25 LEU A CD2 1 ATOM 202 N N . ALA A 1 26 ? 40.309 16.308 14.868 1.00 21.91 ? 26 ALA A N 1 ATOM 203 C CA . ALA A 1 26 ? 39.638 17.591 14.998 1.00 21.50 ? 26 ALA A CA 1 ATOM 204 C C . ALA A 1 26 ? 38.121 17.374 15.087 1.00 20.93 ? 26 ALA A C 1 ATOM 205 O O . ALA A 1 26 ? 37.430 18.036 15.878 1.00 20.89 ? 26 ALA A O 1 ATOM 206 C CB . ALA A 1 26 ? 39.986 18.501 13.821 1.00 22.52 ? 26 ALA A CB 1 ATOM 207 N N . GLU A 1 27 ? 37.617 16.416 14.307 1.00 19.47 ? 27 GLU A N 1 ATOM 208 C CA . GLU A 1 27 ? 36.172 16.149 14.269 1.00 19.45 ? 27 GLU A CA 1 ATOM 209 C C . GLU A 1 27 ? 35.731 15.495 15.583 1.00 18.79 ? 27 GLU A C 1 ATOM 210 O O . GLU A 1 27 ? 34.647 15.820 16.113 1.00 18.50 ? 27 GLU A O 1 ATOM 211 C CB . GLU A 1 27 ? 35.841 15.291 13.057 1.00 18.76 ? 27 GLU A CB 1 ATOM 212 C CG . GLU A 1 27 ? 35.835 16.122 11.754 1.00 19.60 ? 27 GLU A CG 1 ATOM 213 C CD . GLU A 1 27 ? 35.823 15.252 10.475 1.00 19.41 ? 27 GLU A CD 1 ATOM 214 O OE1 . GLU A 1 27 ? 36.205 14.061 10.541 1.00 21.00 ? 27 GLU A OE1 1 ATOM 215 O OE2 . GLU A 1 27 ? 35.463 15.792 9.399 1.00 20.28 ? 27 GLU A OE2 1 ATOM 216 N N . LYS A 1 28 ? 36.595 14.630 16.128 1.00 18.44 ? 28 LYS A N 1 ATOM 217 C CA . LYS A 1 28 ? 36.322 13.978 17.430 1.00 18.46 ? 28 LYS A CA 1 ATOM 218 C C . LYS A 1 28 ? 36.309 14.977 18.590 1.00 18.35 ? 28 LYS A C 1 ATOM 219 O O . LYS A 1 28 ? 35.350 15.039 19.395 1.00 17.07 ? 28 LYS A O 1 ATOM 220 C CB . LYS A 1 28 ? 37.320 12.840 17.685 1.00 19.94 ? 28 LYS A CB 1 ATOM 221 C CG . LYS A 1 28 ? 37.112 11.666 16.765 1.00 19.12 ? 28 LYS A CG 1 ATOM 222 C CD . LYS A 1 28 ? 38.124 10.566 17.050 1.00 21.37 ? 28 LYS A CD 1 ATOM 223 C CE . LYS A 1 28 ? 38.065 9.534 15.961 1.00 22.41 ? 28 LYS A CE 1 ATOM 224 N NZ . LYS A 1 28 ? 39.033 8.405 16.194 1.00 22.74 ? 28 LYS A NZ 1 ATOM 225 N N . ILE A 1 29 ? 37.369 15.773 18.686 1.00 18.09 ? 29 ILE A N 1 ATOM 226 C CA . ILE A 1 29 ? 37.460 16.770 19.764 1.00 18.63 ? 29 ILE A CA 1 ATOM 227 C C . ILE A 1 29 ? 36.319 17.800 19.634 1.00 18.61 ? 29 ILE A C 1 ATOM 228 O O . ILE A 1 29 ? 35.762 18.270 20.639 1.00 18.39 ? 29 ILE A O 1 ATOM 229 C CB . ILE A 1 29 ? 38.875 17.416 19.802 1.00 18.14 ? 29 ILE A CB 1 ATOM 230 C CG1 . ILE A 1 29 ? 39.883 16.367 20.294 1.00 19.77 ? 29 ILE A CG1 1 ATOM 231 C CG2 . ILE A 1 29 ? 38.871 18.691 20.663 1.00 19.50 ? 29 ILE A CG2 1 ATOM 232 C CD1 . ILE A 1 29 ? 41.352 16.817 20.160 1.00 20.44 ? 29 ILE A CD1 1 ATOM 233 N N . GLY A 1 30 ? 35.946 18.119 18.391 1.00 18.55 ? 30 GLY A N 1 ATOM 234 C CA . GLY A 1 30 ? 34.842 19.040 18.149 1.00 18.11 ? 30 GLY A CA 1 ATOM 235 C C . GLY A 1 30 ? 33.555 18.505 18.778 1.00 17.95 ? 30 GLY A C 1 ATOM 236 O O . GLY A 1 30 ? 32.817 19.267 19.417 1.00 17.89 ? 30 GLY A O 1 ATOM 237 N N . GLN A 1 31 ? 33.293 17.205 18.634 1.00 17.65 ? 31 GLN A N 1 ATOM 238 C CA . GLN A 1 31 ? 32.068 16.615 19.240 1.00 17.83 ? 31 GLN A CA 1 ATOM 239 C C . GLN A 1 31 ? 32.041 16.795 20.755 1.00 18.01 ? 31 GLN A C 1 ATOM 240 O O . GLN A 1 31 ? 30.969 16.935 21.352 1.00 18.38 ? 31 GLN A O 1 ATOM 241 C CB . GLN A 1 31 ? 31.924 15.127 18.933 1.00 18.14 ? 31 GLN A CB 1 ATOM 242 C CG . GLN A 1 31 ? 31.409 14.843 17.529 1.00 17.54 ? 31 GLN A CG 1 ATOM 243 C CD . GLN A 1 31 ? 30.050 15.498 17.272 1.00 18.15 ? 31 GLN A CD 1 ATOM 244 O OE1 . GLN A 1 31 ? 29.050 15.142 17.908 1.00 19.58 ? 31 GLN A OE1 1 ATOM 245 N NE2 . GLN A 1 31 ? 30.015 16.463 16.360 1.00 17.81 ? 31 GLN A NE2 1 ATOM 246 N N . MET A 1 32 ? 33.230 16.777 21.361 1.00 17.94 ? 32 MET A N 1 ATOM 247 C CA . MET A 1 32 ? 33.377 16.841 22.816 1.00 18.40 ? 32 MET A CA 1 ATOM 248 C C . MET A 1 32 ? 33.264 18.264 23.338 1.00 18.33 ? 32 MET A C 1 ATOM 249 O O . MET A 1 32 ? 33.357 18.506 24.555 1.00 18.47 ? 32 MET A O 1 ATOM 250 C CB . MET A 1 32 ? 34.750 16.274 23.196 1.00 17.88 ? 32 MET A CB 1 ATOM 251 C CG . MET A 1 32 ? 34.905 14.775 22.869 1.00 19.07 ? 32 MET A CG 1 ATOM 252 S SD . MET A 1 32 ? 36.612 14.197 23.134 1.00 20.22 ? 32 MET A SD 1 ATOM 253 C CE . MET A 1 32 ? 36.717 14.331 24.928 1.00 21.76 ? 32 MET A CE 1 ATOM 254 N N . THR A 1 33 ? 33.104 19.211 22.411 1.00 16.96 ? 33 THR A N 1 ATOM 255 C CA . THR A 1 33 ? 33.123 20.628 22.754 1.00 17.10 ? 33 THR A CA 1 ATOM 256 C C . THR A 1 33 ? 31.717 21.238 22.723 1.00 17.16 ? 33 THR A C 1 ATOM 257 O O . THR A 1 33 ? 31.046 21.247 21.670 1.00 17.26 ? 33 THR A O 1 ATOM 258 C CB . THR A 1 33 ? 34.083 21.418 21.784 1.00 17.26 ? 33 THR A CB 1 ATOM 259 O OG1 . THR A 1 33 ? 35.378 20.794 21.774 1.00 18.56 ? 33 THR A OG1 1 ATOM 260 C CG2 . THR A 1 33 ? 34.244 22.855 22.225 1.00 18.01 ? 33 THR A CG2 1 ATOM 261 N N . GLN A 1 34 ? 31.289 21.770 23.873 1.00 16.23 ? 34 GLN A N 1 ATOM 262 C CA . GLN A 1 34 ? 30.043 22.521 23.951 1.00 15.92 ? 34 GLN A CA 1 ATOM 263 C C . GLN A 1 34 ? 30.322 24.008 24.195 1.00 16.58 ? 34 GLN A C 1 ATOM 264 O O . GLN A 1 34 ? 31.054 24.368 25.130 1.00 16.58 ? 34 GLN A O 1 ATOM 265 C CB . GLN A 1 34 ? 29.134 21.967 25.045 1.00 15.81 ? 34 GLN A CB 1 ATOM 266 C CG . GLN A 1 34 ? 27.782 22.685 25.110 1.00 15.68 ? 34 GLN A CG 1 ATOM 267 C CD . GLN A 1 34 ? 26.915 22.228 26.295 1.00 14.93 ? 34 GLN A CD 1 ATOM 268 O OE1 . GLN A 1 34 ? 27.160 22.621 27.445 1.00 16.00 ? 34 GLN A OE1 1 ATOM 269 N NE2 . GLN A 1 34 ? 25.902 21.415 26.015 1.00 15.53 ? 34 GLN A NE2 1 ATOM 270 N N . ILE A 1 35 ? 29.733 24.869 23.361 1.00 16.70 ? 35 ILE A N 1 ATOM 271 C CA . ILE A 1 35 ? 29.990 26.306 23.472 1.00 16.73 ? 35 ILE A CA 1 ATOM 272 C C . ILE A 1 35 ? 28.714 27.131 23.663 1.00 16.50 ? 35 ILE A C 1 ATOM 273 O O . ILE A 1 35 ? 27.630 26.732 23.249 1.00 16.79 ? 35 ILE A O 1 ATOM 274 C CB . ILE A 1 35 ? 30.808 26.862 22.263 1.00 17.16 ? 35 ILE A CB 1 ATOM 275 C CG1 . ILE A 1 35 ? 29.953 26.910 20.976 1.00 17.37 ? 35 ILE A CG1 1 ATOM 276 C CG2 . ILE A 1 35 ? 32.044 26.014 22.055 1.00 17.93 ? 35 ILE A CG2 1 ATOM 277 C CD1 . ILE A 1 35 ? 30.733 27.482 19.755 1.00 17.43 ? 35 ILE A CD1 1 ATOM 278 N N . GLU A 1 36 ? 28.864 28.284 24.292 1.00 17.14 ? 36 GLU A N 1 ATOM 279 C CA . GLU A 1 36 ? 27.761 29.229 24.460 1.00 17.45 ? 36 GLU A CA 1 ATOM 280 C C . GLU A 1 36 ? 27.333 29.793 23.112 1.00 17.53 ? 36 GLU A C 1 ATOM 281 O O . GLU A 1 36 ? 28.186 30.135 22.254 1.00 18.20 ? 36 GLU A O 1 ATOM 282 C CB . GLU A 1 36 ? 28.221 30.394 25.341 1.00 18.04 ? 36 GLU A CB 1 ATOM 283 C CG . GLU A 1 36 ? 27.435 30.556 26.643 1.00 18.18 ? 36 GLU A CG 1 ATOM 284 C CD . GLU A 1 36 ? 26.050 31.206 26.473 1.00 20.29 ? 36 GLU A CD 1 ATOM 285 O OE1 . GLU A 1 36 ? 25.754 31.778 25.404 1.00 21.77 ? 36 GLU A OE1 1 ATOM 286 O OE2 . GLU A 1 36 ? 25.250 31.166 27.432 1.00 21.15 ? 36 GLU A OE2 1 ATOM 287 N N . ARG A 1 37 ? 26.028 29.931 22.921 1.00 17.05 ? 37 ARG A N 1 ATOM 288 C CA . ARG A 1 37 ? 25.544 30.665 21.732 1.00 17.29 ? 37 ARG A CA 1 ATOM 289 C C . ARG A 1 37 ? 26.213 32.044 21.606 1.00 18.55 ? 37 ARG A C 1 ATOM 290 O O . ARG A 1 37 ? 26.386 32.538 20.488 1.00 19.03 ? 37 ARG A O 1 ATOM 291 C CB . ARG A 1 37 ? 24.021 30.819 21.721 1.00 16.93 ? 37 ARG A CB 1 ATOM 292 C CG . ARG A 1 37 ? 23.466 31.466 22.974 1.00 16.59 ? 37 ARG A CG 1 ATOM 293 C CD . ARG A 1 37 ? 22.071 32.038 22.725 1.00 15.69 ? 37 ARG A CD 1 ATOM 294 N NE . ARG A 1 37 ? 22.088 33.263 21.887 1.00 16.47 ? 37 ARG A NE 1 ATOM 295 C CZ . ARG A 1 37 ? 22.220 34.504 22.359 1.00 17.05 ? 37 ARG A CZ 1 ATOM 296 N NH1 . ARG A 1 37 ? 22.388 34.741 23.668 1.00 18.03 ? 37 ARG A NH1 1 ATOM 297 N NH2 . ARG A 1 37 ? 22.181 35.530 21.515 1.00 19.11 ? 37 ARG A NH2 1 ATOM 298 N N . LEU A 1 38 ? 26.601 32.650 22.736 1.00 19.09 ? 38 LEU A N 1 ATOM 299 C CA . LEU A 1 38 ? 27.209 33.996 22.698 1.00 19.84 ? 38 LEU A CA 1 ATOM 300 C C . LEU A 1 38 ? 28.558 34.055 21.975 1.00 20.99 ? 38 LEU A C 1 ATOM 301 O O . LEU A 1 38 ? 28.948 35.146 21.493 1.00 22.57 ? 38 LEU A O 1 ATOM 302 C CB . LEU A 1 38 ? 27.310 34.608 24.098 1.00 19.96 ? 38 LEU A CB 1 ATOM 303 C CG . LEU A 1 38 ? 25.965 35.064 24.673 1.00 22.61 ? 38 LEU A CG 1 ATOM 304 C CD1 . LEU A 1 38 ? 26.081 35.250 26.186 1.00 23.56 ? 38 LEU A CD1 1 ATOM 305 C CD2 . LEU A 1 38 ? 25.447 36.331 24.000 1.00 25.15 ? 38 LEU A CD2 1 ATOM 306 N N . VAL A 1 39 ? 29.250 32.914 21.877 1.00 20.68 ? 39 VAL A N 1 ATOM 307 C CA . VAL A 1 39 ? 30.537 32.848 21.151 1.00 21.00 ? 39 VAL A CA 1 ATOM 308 C C . VAL A 1 39 ? 30.446 32.101 19.810 1.00 20.99 ? 39 VAL A C 1 ATOM 309 O O . VAL A 1 39 ? 31.440 31.960 19.090 1.00 21.42 ? 39 VAL A O 1 ATOM 310 C CB . VAL A 1 39 ? 31.679 32.272 22.026 1.00 20.89 ? 39 VAL A CB 1 ATOM 311 C CG1 . VAL A 1 39 ? 31.846 33.095 23.296 1.00 22.33 ? 39 VAL A CG1 1 ATOM 312 C CG2 . VAL A 1 39 ? 31.448 30.796 22.333 1.00 20.38 ? 39 VAL A CG2 1 ATOM 313 N N . ALA A 1 40 ? 29.243 31.640 19.466 1.00 21.25 ? 40 ALA A N 1 ATOM 314 C CA . ALA A 1 40 ? 29.046 30.848 18.254 1.00 21.21 ? 40 ALA A CA 1 ATOM 315 C C . ALA A 1 40 ? 28.811 31.720 17.020 1.00 22.16 ? 40 ALA A C 1 ATOM 316 O O . ALA A 1 40 ? 28.137 32.742 17.091 1.00 22.64 ? 40 ALA A O 1 ATOM 317 C CB . ALA A 1 40 ? 27.876 29.893 18.437 1.00 21.55 ? 40 ALA A CB 1 ATOM 318 N N . THR A 1 41 ? 29.379 31.296 15.896 1.00 22.50 ? 41 THR A N 1 ATOM 319 C CA . THR A 1 41 ? 29.040 31.850 14.581 1.00 23.10 ? 41 THR A CA 1 ATOM 320 C C . THR A 1 41 ? 29.045 30.674 13.615 1.00 23.08 ? 41 THR A C 1 ATOM 321 O O . THR A 1 41 ? 29.600 29.610 13.926 1.00 21.94 ? 41 THR A O 1 ATOM 322 C CB . THR A 1 41 ? 30.113 32.852 14.079 1.00 23.22 ? 41 THR A CB 1 ATOM 323 O OG1 . THR A 1 41 ? 31.319 32.137 13.792 1.00 22.96 ? 41 THR A OG1 1 ATOM 324 C CG2 . THR A 1 41 ? 30.386 33.958 15.093 1.00 24.52 ? 41 THR A CG2 1 ATOM 325 N N . PRO A 1 42 ? 28.437 30.844 12.421 1.00 23.51 ? 42 PRO A N 1 ATOM 326 C CA . PRO A 1 42 ? 28.539 29.752 11.459 1.00 23.77 ? 42 PRO A CA 1 ATOM 327 C C . PRO A 1 42 ? 29.966 29.250 11.178 1.00 23.28 ? 42 PRO A C 1 ATOM 328 O O . PRO A 1 42 ? 30.186 28.043 11.152 1.00 21.99 ? 42 PRO A O 1 ATOM 329 C CB . PRO A 1 42 ? 27.879 30.338 10.205 1.00 24.59 ? 42 PRO A CB 1 ATOM 330 C CG . PRO A 1 42 ? 26.871 31.304 10.744 1.00 25.31 ? 42 PRO A CG 1 ATOM 331 C CD . PRO A 1 42 ? 27.580 31.941 11.926 1.00 24.40 ? 42 PRO A CD 1 ATOM 332 N N . ASP A 1 43 ? 30.931 30.160 11.004 1.00 24.23 ? 43 ASP A N 1 ATOM 333 C CA . ASP A 1 43 ? 32.310 29.739 10.725 1.00 24.55 ? 43 ASP A CA 1 ATOM 334 C C . ASP A 1 43 ? 32.927 28.981 11.899 1.00 23.29 ? 43 ASP A C 1 ATOM 335 O O . ASP A 1 43 ? 33.623 27.990 11.711 1.00 23.16 ? 43 ASP A O 1 ATOM 336 C CB . ASP A 1 43 ? 33.198 30.937 10.349 1.00 26.39 ? 43 ASP A CB 1 ATOM 337 C CG . ASP A 1 43 ? 32.979 31.403 8.920 1.00 30.37 ? 43 ASP A CG 1 ATOM 338 O OD1 . ASP A 1 43 ? 32.440 30.624 8.095 1.00 33.30 ? 43 ASP A OD1 1 ATOM 339 O OD2 . ASP A 1 43 ? 33.352 32.559 8.624 1.00 34.09 ? 43 ASP A OD2 1 ATOM 340 N N . VAL A 1 44 ? 32.675 29.469 13.114 1.00 21.72 ? 44 VAL A N 1 ATOM 341 C CA . VAL A 1 44 ? 33.207 28.825 14.308 1.00 20.53 ? 44 VAL A CA 1 ATOM 342 C C . VAL A 1 44 ? 32.694 27.389 14.413 1.00 19.70 ? 44 VAL A C 1 ATOM 343 O O . VAL A 1 44 ? 33.459 26.453 14.703 1.00 19.78 ? 44 VAL A O 1 ATOM 344 C CB . VAL A 1 44 ? 32.848 29.649 15.575 1.00 20.12 ? 44 VAL A CB 1 ATOM 345 C CG1 . VAL A 1 44 ? 33.077 28.821 16.833 1.00 20.79 ? 44 VAL A CG1 1 ATOM 346 C CG2 . VAL A 1 44 ? 33.682 30.941 15.585 1.00 21.46 ? 44 VAL A CG2 1 ATOM 347 N N . LEU A 1 45 ? 31.390 27.212 14.177 1.00 19.54 ? 45 LEU A N 1 ATOM 348 C CA . LEU A 1 45 ? 30.764 25.893 14.321 1.00 19.63 ? 45 LEU A CA 1 ATOM 349 C C . LEU A 1 45 ? 31.248 24.912 13.271 1.00 20.04 ? 45 LEU A C 1 ATOM 350 O O . LEU A 1 45 ? 31.461 23.738 13.563 1.00 19.16 ? 45 LEU A O 1 ATOM 351 C CB . LEU A 1 45 ? 29.235 26.029 14.233 1.00 19.56 ? 45 LEU A CB 1 ATOM 352 C CG . LEU A 1 45 ? 28.604 26.788 15.399 1.00 20.63 ? 45 LEU A CG 1 ATOM 353 C CD1 . LEU A 1 45 ? 27.123 27.039 15.125 1.00 21.59 ? 45 LEU A CD1 1 ATOM 354 C CD2 . LEU A 1 45 ? 28.838 25.987 16.714 1.00 21.23 ? 45 LEU A CD2 1 ATOM 355 N N . ARG A 1 46 ? 31.385 25.404 12.036 1.00 21.14 ? 46 ARG A N 1 ATOM 356 C CA . ARG A 1 46 ? 31.870 24.606 10.938 1.00 22.78 ? 46 ARG A CA 1 ATOM 357 C C . ARG A 1 46 ? 33.372 24.323 11.105 1.00 22.41 ? 46 ARG A C 1 ATOM 358 O O . ARG A 1 46 ? 33.797 23.171 11.056 1.00 22.59 ? 46 ARG A O 1 ATOM 359 C CB . ARG A 1 46 ? 31.579 25.345 9.619 1.00 24.35 ? 46 ARG A CB 1 ATOM 360 C CG . ARG A 1 46 ? 31.818 24.552 8.377 1.00 29.14 ? 46 ARG A CG 1 ATOM 361 C CD . ARG A 1 46 ? 31.607 25.437 7.149 1.00 29.70 ? 46 ARG A CD 1 ATOM 362 N NE . ARG A 1 46 ? 30.243 25.969 7.121 1.00 43.40 ? 46 ARG A NE 1 ATOM 363 C CZ . ARG A 1 46 ? 29.887 27.244 7.322 1.00 33.38 ? 46 ARG A CZ 1 ATOM 364 N NH1 . ARG A 1 46 ? 28.601 27.576 7.269 1.00 42.65 ? 46 ARG A NH1 1 ATOM 365 N NH2 . ARG A 1 46 ? 30.793 28.189 7.570 1.00 44.79 ? 46 ARG A NH2 1 ATOM 366 N N . ASP A 1 47 ? 34.170 25.370 11.328 1.00 22.21 ? 47 ASP A N 1 ATOM 367 C CA . ASP A 1 47 ? 35.639 25.206 11.335 1.00 22.48 ? 47 ASP A CA 1 ATOM 368 C C . ASP A 1 47 ? 36.164 24.341 12.477 1.00 21.84 ? 47 ASP A C 1 ATOM 369 O O . ASP A 1 47 ? 37.186 23.660 12.335 1.00 22.35 ? 47 ASP A O 1 ATOM 370 C CB . ASP A 1 47 ? 36.356 26.551 11.353 1.00 22.63 ? 47 ASP A CB 1 ATOM 371 C CG . ASP A 1 47 ? 36.120 27.372 10.091 1.00 25.18 ? 47 ASP A CG 1 ATOM 372 O OD1 . ASP A 1 47 ? 36.391 28.583 10.146 1.00 27.55 ? 47 ASP A OD1 1 ATOM 373 O OD2 . ASP A 1 47 ? 35.653 26.824 9.068 1.00 26.24 ? 47 ASP A OD2 1 ATOM 374 N N . ASN A 1 48 ? 35.471 24.393 13.617 1.00 20.35 ? 48 ASN A N 1 ATOM 375 C CA . ASN A 1 48 ? 35.822 23.603 14.792 1.00 19.81 ? 48 ASN A CA 1 ATOM 376 C C . ASN A 1 48 ? 34.982 22.324 14.994 1.00 19.19 ? 48 ASN A C 1 ATOM 377 O O . ASN A 1 48 ? 35.159 21.609 15.986 1.00 19.35 ? 48 ASN A O 1 ATOM 378 C CB . ASN A 1 48 ? 35.784 24.500 16.031 1.00 20.35 ? 48 ASN A CB 1 ATOM 379 C CG . ASN A 1 48 ? 36.781 25.618 15.922 1.00 20.59 ? 48 ASN A CG 1 ATOM 380 O OD1 . ASN A 1 48 ? 37.987 25.401 16.117 1.00 21.95 ? 48 ASN A OD1 1 ATOM 381 N ND2 . ASN A 1 48 ? 36.304 26.802 15.548 1.00 20.69 ? 48 ASN A ND2 1 ATOM 382 N N . PHE A 1 49 ? 34.112 22.019 14.028 1.00 18.21 ? 49 PHE A N 1 ATOM 383 C CA . PHE A 1 49 ? 33.332 20.784 14.060 1.00 18.18 ? 49 PHE A CA 1 ATOM 384 C C . PHE A 1 49 ? 32.584 20.631 15.401 1.00 17.40 ? 49 PHE A C 1 ATOM 385 O O . PHE A 1 49 ? 32.554 19.547 15.986 1.00 17.31 ? 49 PHE A O 1 ATOM 386 C CB . PHE A 1 49 ? 34.244 19.580 13.836 1.00 18.90 ? 49 PHE A CB 1 ATOM 387 C CG . PHE A 1 49 ? 35.082 19.676 12.584 1.00 20.18 ? 49 PHE A CG 1 ATOM 388 C CD1 . PHE A 1 49 ? 34.488 19.505 11.324 1.00 20.04 ? 49 PHE A CD1 1 ATOM 389 C CD2 . PHE A 1 49 ? 36.446 19.936 12.670 1.00 21.56 ? 49 PHE A CD2 1 ATOM 390 C CE1 . PHE A 1 49 ? 35.269 19.580 10.140 1.00 21.25 ? 49 PHE A CE1 1 ATOM 391 C CE2 . PHE A 1 49 ? 37.238 20.022 11.504 1.00 21.37 ? 49 PHE A CE2 1 ATOM 392 C CZ . PHE A 1 49 ? 36.655 19.842 10.250 1.00 21.33 ? 49 PHE A CZ 1 ATOM 393 N N . ILE A 1 50 ? 32.022 21.738 15.881 1.00 17.30 ? 50 ILE A N 1 ATOM 394 C CA . ILE A 1 50 ? 31.467 21.819 17.254 1.00 16.97 ? 50 ILE A CA 1 ATOM 395 C C . ILE A 1 50 ? 30.304 20.838 17.439 1.00 17.27 ? 50 ILE A C 1 ATOM 396 O O . ILE A 1 50 ? 29.432 20.739 16.563 1.00 17.83 ? 50 ILE A O 1 ATOM 397 C CB . ILE A 1 50 ? 31.031 23.271 17.597 1.00 17.04 ? 50 ILE A CB 1 ATOM 398 C CG1 . ILE A 1 50 ? 32.245 24.239 17.636 1.00 17.42 ? 50 ILE A CG1 1 ATOM 399 C CG2 . ILE A 1 50 ? 30.189 23.305 18.913 1.00 16.90 ? 50 ILE A CG2 1 ATOM 400 C CD1 . ILE A 1 50 ? 33.355 23.868 18.656 1.00 17.40 ? 50 ILE A CD1 1 ATOM 401 N N . GLY A 1 51 ? 30.285 20.147 18.585 1.00 16.37 ? 51 GLY A N 1 ATOM 402 C CA . GLY A 1 51 ? 29.276 19.116 18.855 1.00 17.06 ? 51 GLY A CA 1 ATOM 403 C C . GLY A 1 51 ? 28.013 19.607 19.558 1.00 16.10 ? 51 GLY A C 1 ATOM 404 O O . GLY A 1 51 ? 26.942 18.985 19.454 1.00 15.80 ? 51 GLY A O 1 ATOM 405 N N . SER A 1 52 ? 28.112 20.717 20.276 1.00 15.50 ? 52 SER A N 1 ATOM 406 C CA . SER A 1 52 ? 26.967 21.155 21.081 1.00 15.69 ? 52 SER A CA 1 ATOM 407 C C . SER A 1 52 ? 27.008 22.644 21.346 1.00 15.89 ? 52 SER A C 1 ATOM 408 O O . SER A 1 52 ? 28.087 23.239 21.411 1.00 15.17 ? 52 SER A O 1 ATOM 409 C CB . SER A 1 52 ? 26.940 20.367 22.404 1.00 16.19 ? 52 SER A CB 1 ATOM 410 O OG . SER A 1 52 ? 25.811 20.720 23.199 1.00 16.13 ? 52 SER A OG 1 ATOM 411 N N . LEU A 1 53 ? 25.830 23.252 21.498 1.00 15.46 ? 53 LEU A N 1 ATOM 412 C CA . LEU A 1 53 ? 25.734 24.612 21.998 1.00 16.01 ? 53 LEU A CA 1 ATOM 413 C C . LEU A 1 53 ? 24.832 24.610 23.217 1.00 16.18 ? 53 LEU A C 1 ATOM 414 O O . LEU A 1 53 ? 24.051 23.679 23.412 1.00 17.00 ? 53 LEU A O 1 ATOM 415 C CB . LEU A 1 53 ? 25.100 25.531 20.970 1.00 16.61 ? 53 LEU A CB 1 ATOM 416 C CG . LEU A 1 53 ? 26.061 25.878 19.815 1.00 18.50 ? 53 LEU A CG 1 ATOM 417 C CD1 . LEU A 1 53 ? 25.905 24.917 18.688 1.00 23.29 ? 53 LEU A CD1 1 ATOM 418 C CD2 . LEU A 1 53 ? 25.755 27.286 19.392 1.00 24.22 ? 53 LEU A CD2 1 ATOM 419 N N . LEU A 1 54 ? 24.939 25.665 24.012 1.00 16.08 ? 54 LEU A N 1 ATOM 420 C CA . LEU A 1 54 ? 23.970 25.904 25.075 1.00 15.88 ? 54 LEU A CA 1 ATOM 421 C C . LEU A 1 54 ? 23.655 27.382 25.214 1.00 16.31 ? 54 LEU A C 1 ATOM 422 O O . LEU A 1 54 ? 24.423 28.250 24.776 1.00 16.43 ? 54 LEU A O 1 ATOM 423 C CB . LEU A 1 54 ? 24.455 25.359 26.436 1.00 15.82 ? 54 LEU A CB 1 ATOM 424 C CG . LEU A 1 54 ? 25.382 26.266 27.256 1.00 16.29 ? 54 LEU A CG 1 ATOM 425 C CD1 . LEU A 1 54 ? 25.271 25.899 28.758 1.00 17.43 ? 54 LEU A CD1 1 ATOM 426 C CD2 . LEU A 1 54 ? 26.826 26.201 26.774 1.00 17.74 ? 54 LEU A CD2 1 ATOM 427 N N . SER A 1 55 ? 22.503 27.633 25.835 1.00 15.58 ? 55 SER A N 1 ATOM 428 C CA . SER A 1 55 ? 22.203 28.893 26.475 1.00 16.35 ? 55 SER A CA 1 ATOM 429 C C . SER A 1 55 ? 22.429 28.713 27.967 1.00 16.62 ? 55 SER A C 1 ATOM 430 O O . SER A 1 55 ? 21.772 27.873 28.595 1.00 16.45 ? 55 SER A O 1 ATOM 431 C CB . SER A 1 55 ? 20.737 29.270 26.255 1.00 16.69 ? 55 SER A CB 1 ATOM 432 O OG . SER A 1 55 ? 20.535 29.869 24.983 1.00 17.64 ? 55 SER A OG 1 ATOM 433 N N . GLY A 1 56 ? 23.331 29.503 28.542 1.00 16.63 ? 56 GLY A N 1 ATOM 434 C CA . GLY A 1 56 ? 23.386 29.601 30.010 1.00 17.71 ? 56 GLY A CA 1 ATOM 435 C C . GLY A 1 56 ? 22.172 30.409 30.479 1.00 17.78 ? 56 GLY A C 1 ATOM 436 O O . GLY A 1 56 ? 21.401 30.926 29.647 1.00 17.67 ? 56 GLY A O 1 ATOM 437 N N . GLY A 1 57 ? 21.982 30.521 31.795 1.00 18.03 ? 57 GLY A N 1 ATOM 438 C CA . GLY A 1 57 ? 20.859 31.304 32.333 1.00 18.36 ? 57 GLY A CA 1 ATOM 439 C C . GLY A 1 57 ? 20.863 32.717 31.738 1.00 18.89 ? 57 GLY A C 1 ATOM 440 O O . GLY A 1 57 ? 21.905 33.404 31.744 1.00 19.45 ? 57 GLY A O 1 ATOM 441 N N . GLY A 1 58 ? 19.710 33.130 31.205 1.00 18.92 ? 58 GLY A N 1 ATOM 442 C CA . GLY A 1 58 ? 19.521 34.463 30.609 1.00 19.56 ? 58 GLY A CA 1 ATOM 443 C C . GLY A 1 58 ? 20.162 34.669 29.236 1.00 19.32 ? 58 GLY A C 1 ATOM 444 O O . GLY A 1 58 ? 20.138 35.794 28.706 1.00 20.95 ? 58 GLY A O 1 ATOM 445 N N . SER A 1 59 ? 20.742 33.610 28.653 1.00 18.77 ? 59 SER A N 1 ATOM 446 C CA . SER A 1 59 ? 21.360 33.731 27.319 1.00 18.29 ? 59 SER A CA 1 ATOM 447 C C . SER A 1 59 ? 20.292 33.512 26.239 1.00 18.07 ? 59 SER A C 1 ATOM 448 O O . SER A 1 59 ? 19.985 32.379 25.853 1.00 18.43 ? 59 SER A O 1 ATOM 449 C CB . SER A 1 59 ? 22.558 32.784 27.135 1.00 17.97 ? 59 SER A CB 1 ATOM 450 O OG . SER A 1 59 ? 23.154 32.988 25.845 1.00 18.52 ? 59 SER A OG 1 ATOM 451 N N . VAL A 1 60 ? 19.712 34.614 25.777 1.00 17.80 ? 60 VAL A N 1 ATOM 452 C CA . VAL A 1 60 ? 18.551 34.561 24.887 1.00 17.93 ? 60 VAL A CA 1 ATOM 453 C C . VAL A 1 60 ? 18.794 35.419 23.627 1.00 18.59 ? 60 VAL A C 1 ATOM 454 O O . VAL A 1 60 ? 19.592 36.351 23.660 1.00 18.97 ? 60 VAL A O 1 ATOM 455 C CB . VAL A 1 60 ? 17.275 35.023 25.639 1.00 17.58 ? 60 VAL A CB 1 ATOM 456 C CG1 . VAL A 1 60 ? 17.042 34.130 26.916 1.00 17.60 ? 60 VAL A CG1 1 ATOM 457 C CG2 . VAL A 1 60 ? 17.358 36.518 26.043 1.00 19.02 ? 60 VAL A CG2 1 ATOM 458 N N . PRO A 1 61 ? 18.131 35.080 22.510 1.00 19.39 ? 61 PRO A N 1 ATOM 459 C CA . PRO A 1 61 ? 18.375 35.884 21.274 1.00 19.99 ? 61 PRO A CA 1 ATOM 460 C C . PRO A 1 61 ? 17.934 37.354 21.380 1.00 21.01 ? 61 PRO A C 1 ATOM 461 O O . PRO A 1 61 ? 18.564 38.244 20.770 1.00 21.54 ? 61 PRO A O 1 ATOM 462 C CB . PRO A 1 61 ? 17.572 35.139 20.193 1.00 20.94 ? 61 PRO A CB 1 ATOM 463 C CG . PRO A 1 61 ? 16.594 34.270 20.939 1.00 19.71 ? 61 PRO A CG 1 ATOM 464 C CD . PRO A 1 61 ? 17.235 33.939 22.264 1.00 19.72 ? 61 PRO A CD 1 ATOM 465 N N . ARG A 1 62 ? 16.895 37.610 22.165 1.00 22.36 ? 62 ARG A N 1 ATOM 466 C CA . ARG A 1 62 ? 16.323 38.940 22.335 1.00 24.41 ? 62 ARG A CA 1 ATOM 467 C C . ARG A 1 62 ? 15.419 38.853 23.561 1.00 24.49 ? 62 ARG A C 1 ATOM 468 O O . ARG A 1 62 ? 14.815 37.807 23.808 1.00 23.02 ? 62 ARG A O 1 ATOM 469 C CB . ARG A 1 62 ? 15.471 39.241 21.086 1.00 25.73 ? 62 ARG A CB 1 ATOM 470 C CG . ARG A 1 62 ? 14.734 40.523 21.057 1.00 28.90 ? 62 ARG A CG 1 ATOM 471 C CD . ARG A 1 62 ? 14.262 40.762 19.642 1.00 31.72 ? 62 ARG A CD 1 ATOM 472 N NE . ARG A 1 62 ? 13.002 40.086 19.364 1.00 32.66 ? 62 ARG A NE 1 ATOM 473 C CZ . ARG A 1 62 ? 11.833 40.714 19.354 1.00 34.61 ? 62 ARG A CZ 1 ATOM 474 N NH1 . ARG A 1 62 ? 11.801 42.011 19.610 1.00 34.71 ? 62 ARG A NH1 1 ATOM 475 N NH2 . ARG A 1 62 ? 10.712 40.053 19.092 1.00 35.29 ? 62 ARG A NH2 1 ATOM 476 N N . LYS A 1 63 ? 15.304 39.938 24.323 1.00 24.89 ? 63 LYS A N 1 ATOM 477 C CA . LYS A 1 63 ? 14.278 39.966 25.355 1.00 26.05 ? 63 LYS A CA 1 ATOM 478 C C . LYS A 1 63 ? 12.924 39.839 24.681 1.00 24.78 ? 63 LYS A C 1 ATOM 479 O O . LYS A 1 63 ? 12.670 40.489 23.663 1.00 25.46 ? 63 LYS A O 1 ATOM 480 C CB . LYS A 1 63 ? 14.332 41.260 26.154 1.00 27.45 ? 63 LYS A CB 1 ATOM 481 C CG . LYS A 1 63 ? 14.372 40.978 27.630 1.00 32.83 ? 63 LYS A CG 1 ATOM 482 C CD . LYS A 1 63 ? 15.690 40.305 28.003 1.00 35.79 ? 63 LYS A CD 1 ATOM 483 C CE . LYS A 1 63 ? 15.578 39.491 29.283 1.00 40.70 ? 63 LYS A CE 1 ATOM 484 N NZ . LYS A 1 63 ? 15.301 40.289 30.503 1.00 41.05 ? 63 LYS A NZ 1 ATOM 485 N N . GLY A 1 64 ? 12.063 38.983 25.225 1.00 23.48 ? 64 GLY A N 1 ATOM 486 C CA . GLY A 1 64 ? 10.736 38.795 24.672 1.00 22.64 ? 64 GLY A CA 1 ATOM 487 C C . GLY A 1 64 ? 10.678 38.018 23.364 1.00 21.80 ? 64 GLY A C 1 ATOM 488 O O . GLY A 1 64 ? 9.654 38.041 22.688 1.00 22.38 ? 64 GLY A O 1 ATOM 489 N N . ALA A 1 65 ? 11.755 37.310 23.012 1.00 21.13 ? 65 ALA A N 1 ATOM 490 C CA . ALA A 1 65 ? 11.785 36.535 21.754 1.00 20.28 ? 65 ALA A CA 1 ATOM 491 C C . ALA A 1 65 ? 10.647 35.514 21.682 1.00 20.37 ? 65 ALA A C 1 ATOM 492 O O . ALA A 1 65 ? 10.337 34.846 22.679 1.00 20.12 ? 65 ALA A O 1 ATOM 493 C CB . ALA A 1 65 ? 13.138 35.833 21.590 1.00 20.87 ? 65 ALA A CB 1 ATOM 494 N N . THR A 1 66 ? 10.024 35.394 20.510 1.00 19.92 ? 66 THR A N 1 ATOM 495 C CA . THR A 1 66 ? 8.971 34.396 20.282 1.00 19.92 ? 66 THR A CA 1 ATOM 496 C C . THR A 1 66 ? 9.582 32.997 20.149 1.00 19.68 ? 66 THR A C 1 ATOM 497 O O . THR A 1 66 ? 10.805 32.865 19.921 1.00 19.12 ? 66 THR A O 1 ATOM 498 C CB . THR A 1 66 ? 8.215 34.697 18.974 1.00 20.14 ? 66 THR A CB 1 ATOM 499 O OG1 . THR A 1 66 ? 9.130 34.557 17.865 1.00 20.47 ? 66 THR A OG1 1 ATOM 500 C CG2 . THR A 1 66 ? 7.645 36.112 19.019 1.00 20.63 ? 66 THR A CG2 1 ATOM 501 N N . ALA A 1 67 ? 8.740 31.966 20.248 1.00 19.71 ? 67 ALA A N 1 ATOM 502 C CA . ALA A 1 67 ? 9.183 30.596 20.004 1.00 19.50 ? 67 ALA A CA 1 ATOM 503 C C . ALA A 1 67 ? 9.863 30.498 18.634 1.00 19.55 ? 67 ALA A C 1 ATOM 504 O O . ALA A 1 67 ? 10.916 29.864 18.507 1.00 18.91 ? 67 ALA A O 1 ATOM 505 C CB . ALA A 1 67 ? 8.022 29.591 20.102 1.00 19.77 ? 67 ALA A CB 1 ATOM 506 N N . LYS A 1 68 ? 9.282 31.141 17.619 1.00 18.90 ? 68 LYS A N 1 ATOM 507 C CA . LYS A 1 68 ? 9.883 31.059 16.274 1.00 20.27 ? 68 LYS A CA 1 ATOM 508 C C . LYS A 1 68 ? 11.272 31.717 16.217 1.00 19.38 ? 68 LYS A C 1 ATOM 509 O O . LYS A 1 68 ? 12.166 31.212 15.514 1.00 19.57 ? 68 LYS A O 1 ATOM 510 C CB A LYS A 1 68 ? 8.924 31.572 15.195 0.50 20.22 ? 68 LYS A CB 1 ATOM 511 C CB B LYS A 1 68 ? 8.954 31.746 15.266 0.50 19.95 ? 68 LYS A CB 1 ATOM 512 C CG A LYS A 1 68 ? 9.413 31.352 13.754 0.50 21.81 ? 68 LYS A CG 1 ATOM 513 C CG B LYS A 1 68 ? 9.635 32.153 13.955 0.50 21.26 ? 68 LYS A CG 1 ATOM 514 C CD A LYS A 1 68 ? 9.253 29.926 13.251 0.50 25.53 ? 68 LYS A CD 1 ATOM 515 C CD B LYS A 1 68 ? 8.700 32.939 13.047 0.50 21.43 ? 68 LYS A CD 1 ATOM 516 C CE A LYS A 1 68 ? 9.646 29.877 11.775 0.50 25.50 ? 68 LYS A CE 1 ATOM 517 C CE B LYS A 1 68 ? 9.126 32.830 11.582 0.50 22.33 ? 68 LYS A CE 1 ATOM 518 N NZ A LYS A 1 68 ? 8.959 28.818 10.998 0.50 28.70 ? 68 LYS A NZ 1 ATOM 519 N NZ B LYS A 1 68 ? 10.560 33.111 11.324 0.50 24.43 ? 68 LYS A NZ 1 ATOM 520 N N . GLU A 1 69 ? 11.462 32.827 16.937 1.00 19.16 ? 69 GLU A N 1 ATOM 521 C CA . GLU A 1 69 ? 12.806 33.437 17.039 1.00 19.07 ? 69 GLU A CA 1 ATOM 522 C C . GLU A 1 69 ? 13.842 32.456 17.596 1.00 18.52 ? 69 GLU A C 1 ATOM 523 O O . GLU A 1 69 ? 14.972 32.374 17.091 1.00 18.20 ? 69 GLU A O 1 ATOM 524 C CB . GLU A 1 69 ? 12.813 34.708 17.876 1.00 19.63 ? 69 GLU A CB 1 ATOM 525 C CG . GLU A 1 69 ? 12.212 35.926 17.168 1.00 20.39 ? 69 GLU A CG 1 ATOM 526 C CD . GLU A 1 69 ? 12.206 37.116 18.086 1.00 23.28 ? 69 GLU A CD 1 ATOM 527 O OE1 . GLU A 1 69 ? 11.097 37.507 18.531 1.00 23.53 ? 69 GLU A OE1 1 ATOM 528 O OE2 . GLU A 1 69 ? 13.305 37.639 18.392 1.00 24.83 ? 69 GLU A OE2 1 ATOM 529 N N . TRP A 1 70 ? 13.449 31.698 18.622 1.00 17.68 ? 70 TRP A N 1 ATOM 530 C CA . TRP A 1 70 ? 14.344 30.679 19.163 1.00 17.25 ? 70 TRP A CA 1 ATOM 531 C C . TRP A 1 70 ? 14.600 29.608 18.124 1.00 17.14 ? 70 TRP A C 1 ATOM 532 O O . TRP A 1 70 ? 15.746 29.197 17.923 1.00 17.16 ? 70 TRP A O 1 ATOM 533 C CB . TRP A 1 70 ? 13.738 30.057 20.430 1.00 17.06 ? 70 TRP A CB 1 ATOM 534 C CG . TRP A 1 70 ? 13.915 30.888 21.667 1.00 15.77 ? 70 TRP A CG 1 ATOM 535 C CD1 . TRP A 1 70 ? 13.083 31.878 22.134 1.00 16.99 ? 70 TRP A CD1 1 ATOM 536 C CD2 . TRP A 1 70 ? 14.993 30.786 22.611 1.00 16.36 ? 70 TRP A CD2 1 ATOM 537 N NE1 . TRP A 1 70 ? 13.580 32.398 23.322 1.00 17.80 ? 70 TRP A NE1 1 ATOM 538 C CE2 . TRP A 1 70 ? 14.741 31.735 23.640 1.00 16.76 ? 70 TRP A CE2 1 ATOM 539 C CE3 . TRP A 1 70 ? 16.150 29.969 22.699 1.00 17.17 ? 70 TRP A CE3 1 ATOM 540 C CZ2 . TRP A 1 70 ? 15.614 31.912 24.734 1.00 16.52 ? 70 TRP A CZ2 1 ATOM 541 C CZ3 . TRP A 1 70 ? 17.014 30.142 23.801 1.00 17.07 ? 70 TRP A CZ3 1 ATOM 542 C CH2 . TRP A 1 70 ? 16.735 31.108 24.801 1.00 16.27 ? 70 TRP A CH2 1 ATOM 543 N N . GLN A 1 71 ? 13.540 29.149 17.453 1.00 17.37 ? 71 GLN A N 1 ATOM 544 C CA . GLN A 1 71 ? 13.697 28.112 16.436 1.00 18.21 ? 71 GLN A CA 1 ATOM 545 C C . GLN A 1 71 ? 14.652 28.566 15.331 1.00 18.40 ? 71 GLN A C 1 ATOM 546 O O . GLN A 1 71 ? 15.521 27.791 14.900 1.00 19.50 ? 71 GLN A O 1 ATOM 547 C CB . GLN A 1 71 ? 12.341 27.742 15.825 1.00 18.30 ? 71 GLN A CB 1 ATOM 548 C CG . GLN A 1 71 ? 11.438 26.946 16.793 1.00 18.83 ? 71 GLN A CG 1 ATOM 549 C CD . GLN A 1 71 ? 10.324 26.191 16.090 1.00 20.31 ? 71 GLN A CD 1 ATOM 550 O OE1 . GLN A 1 71 ? 9.444 25.612 16.739 1.00 23.27 ? 71 GLN A OE1 1 ATOM 551 N NE2 . GLN A 1 71 ? 10.355 26.182 14.769 1.00 19.31 ? 71 GLN A NE2 1 ATOM 552 N N . ASP A 1 72 ? 14.498 29.815 14.899 1.00 19.45 ? 72 ASP A N 1 ATOM 553 C CA . ASP A 1 72 ? 15.356 30.363 13.827 1.00 20.21 ? 72 ASP A CA 1 ATOM 554 C C . ASP A 1 72 ? 16.812 30.436 14.275 1.00 20.30 ? 72 ASP A C 1 ATOM 555 O O . ASP A 1 72 ? 17.717 30.153 13.486 1.00 20.06 ? 72 ASP A O 1 ATOM 556 C CB . ASP A 1 72 ? 14.875 31.749 13.398 1.00 21.21 ? 72 ASP A CB 1 ATOM 557 C CG . ASP A 1 72 ? 13.535 31.705 12.652 1.00 23.48 ? 72 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 72 ? 13.104 30.613 12.221 1.00 25.75 ? 72 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 72 ? 12.926 32.790 12.489 1.00 27.38 ? 72 ASP A OD2 1 ATOM 560 N N . MET A 1 73 ? 17.029 30.805 15.540 1.00 19.29 ? 73 MET A N 1 ATOM 561 C CA . MET A 1 73 ? 18.379 30.846 16.086 1.00 18.93 ? 73 MET A CA 1 ATOM 562 C C . MET A 1 73 ? 19.022 29.459 16.092 1.00 18.12 ? 73 MET A C 1 ATOM 563 O O . MET A 1 73 ? 20.133 29.285 15.581 1.00 17.49 ? 73 MET A O 1 ATOM 564 C CB . MET A 1 73 ? 18.371 31.417 17.504 1.00 18.51 ? 73 MET A CB 1 ATOM 565 C CG . MET A 1 73 ? 19.772 31.413 18.124 1.00 19.24 ? 73 MET A CG 1 ATOM 566 S SD . MET A 1 73 ? 19.734 31.796 19.876 1.00 21.32 ? 73 MET A SD 1 ATOM 567 C CE . MET A 1 73 ? 19.069 30.254 20.528 1.00 22.17 ? 73 MET A CE 1 ATOM 568 N N . VAL A 1 74 ? 18.308 28.472 16.653 1.00 17.28 ? 74 VAL A N 1 ATOM 569 C CA . VAL A 1 74 ? 18.837 27.123 16.777 1.00 18.08 ? 74 VAL A CA 1 ATOM 570 C C . VAL A 1 74 ? 19.076 26.533 15.373 1.00 18.24 ? 74 VAL A C 1 ATOM 571 O O . VAL A 1 74 ? 20.146 25.973 15.101 1.00 18.25 ? 74 VAL A O 1 ATOM 572 C CB . VAL A 1 74 ? 17.927 26.233 17.656 1.00 18.95 ? 74 VAL A CB 1 ATOM 573 C CG1 . VAL A 1 74 ? 18.489 24.839 17.743 1.00 19.50 ? 74 VAL A CG1 1 ATOM 574 C CG2 . VAL A 1 74 ? 17.793 26.855 19.063 1.00 18.03 ? 74 VAL A CG2 1 ATOM 575 N N . ASP A 1 75 ? 18.103 26.711 14.471 1.00 18.65 ? 75 ASP A N 1 ATOM 576 C CA . ASP A 1 75 ? 18.267 26.209 13.093 1.00 19.17 ? 75 ASP A CA 1 ATOM 577 C C . ASP A 1 75 ? 19.471 26.834 12.356 1.00 19.67 ? 75 ASP A C 1 ATOM 578 O O . ASP A 1 75 ? 20.113 26.145 11.566 1.00 19.42 ? 75 ASP A O 1 ATOM 579 C CB . ASP A 1 75 ? 17.015 26.453 12.263 1.00 19.51 ? 75 ASP A CB 1 ATOM 580 C CG . ASP A 1 75 ? 15.873 25.500 12.586 1.00 20.97 ? 75 ASP A CG 1 ATOM 581 O OD1 . ASP A 1 75 ? 16.087 24.431 13.202 1.00 21.11 ? 75 ASP A OD1 1 ATOM 582 O OD2 . ASP A 1 75 ? 14.742 25.831 12.161 1.00 24.14 ? 75 ASP A OD2 1 ATOM 583 N N . GLY A 1 76 ? 19.733 28.124 12.585 1.00 19.60 ? 76 GLY A N 1 ATOM 584 C CA . GLY A 1 76 ? 20.913 28.823 12.019 1.00 20.53 ? 76 GLY A CA 1 ATOM 585 C C . GLY A 1 76 ? 22.227 28.163 12.427 1.00 20.58 ? 76 GLY A C 1 ATOM 586 O O . GLY A 1 76 ? 23.145 27.939 11.602 1.00 20.99 ? 76 GLY A O 1 ATOM 587 N N . PHE A 1 77 ? 22.320 27.843 13.714 1.00 19.64 ? 77 PHE A N 1 ATOM 588 C CA . PHE A 1 77 ? 23.465 27.109 14.218 1.00 19.50 ? 77 PHE A CA 1 ATOM 589 C C . PHE A 1 77 ? 23.516 25.711 13.600 1.00 18.93 ? 77 PHE A C 1 ATOM 590 O O . PHE A 1 77 ? 24.580 25.247 13.199 1.00 19.31 ? 77 PHE A O 1 ATOM 591 C CB . PHE A 1 77 ? 23.404 27.023 15.749 1.00 19.18 ? 77 PHE A CB 1 ATOM 592 C CG . PHE A 1 77 ? 23.530 28.363 16.442 1.00 20.12 ? 77 PHE A CG 1 ATOM 593 C CD1 . PHE A 1 77 ? 24.430 29.346 15.976 1.00 20.78 ? 77 PHE A CD1 1 ATOM 594 C CD2 . PHE A 1 77 ? 22.760 28.638 17.591 1.00 20.22 ? 77 PHE A CD2 1 ATOM 595 C CE1 . PHE A 1 77 ? 24.556 30.593 16.655 1.00 21.92 ? 77 PHE A CE1 1 ATOM 596 C CE2 . PHE A 1 77 ? 22.888 29.869 18.264 1.00 20.78 ? 77 PHE A CE2 1 ATOM 597 C CZ . PHE A 1 77 ? 23.780 30.850 17.791 1.00 21.17 ? 77 PHE A CZ 1 ATOM 598 N N . GLN A 1 78 ? 22.372 25.040 13.529 1.00 18.85 ? 78 GLN A N 1 ATOM 599 C CA . GLN A 1 78 ? 22.312 23.675 13.015 1.00 18.55 ? 78 GLN A CA 1 ATOM 600 C C . GLN A 1 78 ? 22.756 23.638 11.554 1.00 19.00 ? 78 GLN A C 1 ATOM 601 O O . GLN A 1 78 ? 23.488 22.736 11.156 1.00 18.99 ? 78 GLN A O 1 ATOM 602 C CB . GLN A 1 78 ? 20.914 23.058 13.175 1.00 18.65 ? 78 GLN A CB 1 ATOM 603 C CG . GLN A 1 78 ? 20.878 21.555 12.889 1.00 19.07 ? 78 GLN A CG 1 ATOM 604 C CD . GLN A 1 78 ? 21.664 20.743 13.918 1.00 19.13 ? 78 GLN A CD 1 ATOM 605 O OE1 . GLN A 1 78 ? 22.897 20.724 13.893 1.00 18.06 ? 78 GLN A OE1 1 ATOM 606 N NE2 . GLN A 1 78 ? 20.948 20.075 14.839 1.00 20.41 ? 78 GLN A NE2 1 ATOM 607 N N . LYS A 1 79 ? 22.347 24.642 10.784 1.00 19.65 ? 79 LYS A N 1 ATOM 608 C CA . LYS A 1 79 ? 22.693 24.670 9.346 1.00 23.33 ? 79 LYS A CA 1 ATOM 609 C C . LYS A 1 79 ? 24.223 24.696 9.170 1.00 21.72 ? 79 LYS A C 1 ATOM 610 O O . LYS A 1 79 ? 24.765 24.018 8.280 1.00 22.09 ? 79 LYS A O 1 ATOM 611 C CB . LYS A 1 79 ? 22.042 25.870 8.667 1.00 22.85 ? 79 LYS A CB 1 ATOM 612 C CG . LYS A 1 79 ? 20.554 25.696 8.448 1.00 28.15 ? 79 LYS A CG 1 ATOM 613 C CD . LYS A 1 79 ? 19.977 26.837 7.599 1.00 28.14 ? 79 LYS A CD 1 ATOM 614 C CE . LYS A 1 79 ? 18.470 26.649 7.351 1.00 30.05 ? 79 LYS A CE 1 ATOM 615 N NZ . LYS A 1 79 ? 18.182 25.507 6.407 1.00 48.27 ? 79 LYS A NZ 1 ATOM 616 N N . ALA A 1 80 ? 24.914 25.439 10.044 1.00 21.21 ? 80 ALA A N 1 ATOM 617 C CA . ALA A 1 80 ? 26.376 25.509 10.011 1.00 21.53 ? 80 ALA A CA 1 ATOM 618 C C . ALA A 1 80 ? 26.979 24.132 10.327 1.00 21.34 ? 80 ALA A C 1 ATOM 619 O O . ALA A 1 80 ? 27.855 23.645 9.617 1.00 22.12 ? 80 ALA A O 1 ATOM 620 C CB . ALA A 1 80 ? 26.879 26.563 10.977 1.00 21.18 ? 80 ALA A CB 1 ATOM 621 N N . CYS A 1 81 ? 26.491 23.483 11.386 1.00 21.09 ? 81 CYS A N 1 ATOM 622 C CA . CYS A 1 81 ? 26.992 22.174 11.748 1.00 21.13 ? 81 CYS A CA 1 ATOM 623 C C . CYS A 1 81 ? 26.714 21.128 10.652 1.00 21.39 ? 81 CYS A C 1 ATOM 624 O O . CYS A 1 81 ? 27.555 20.275 10.375 1.00 22.35 ? 81 CYS A O 1 ATOM 625 C CB . CYS A 1 81 ? 26.375 21.737 13.076 1.00 20.98 ? 81 CYS A CB 1 ATOM 626 S SG . CYS A 1 81 ? 26.885 22.831 14.412 1.00 20.97 ? 81 CYS A SG 1 ATOM 627 N N . MET A 1 82 ? 25.538 21.199 10.035 1.00 21.13 ? 82 MET A N 1 ATOM 628 C CA . MET A 1 82 ? 25.167 20.228 9.014 1.00 21.67 ? 82 MET A CA 1 ATOM 629 C C . MET A 1 82 ? 25.982 20.415 7.727 1.00 21.94 ? 82 MET A C 1 ATOM 630 O O . MET A 1 82 ? 26.000 19.521 6.877 1.00 23.47 ? 82 MET A O 1 ATOM 631 C CB . MET A 1 82 ? 23.661 20.288 8.719 1.00 22.27 ? 82 MET A CB 1 ATOM 632 C CG . MET A 1 82 ? 22.790 19.802 9.896 1.00 24.47 ? 82 MET A CG 1 ATOM 633 S SD . MET A 1 82 ? 23.174 18.116 10.410 1.00 31.73 ? 82 MET A SD 1 ATOM 634 C CE . MET A 1 82 ? 22.408 17.192 9.098 1.00 30.18 ? 82 MET A CE 1 ATOM 635 N N . SER A 1 83 ? 26.633 21.566 7.603 1.00 22.11 ? 83 SER A N 1 ATOM 636 C CA . SER A 1 83 ? 27.467 21.904 6.419 1.00 22.58 ? 83 SER A CA 1 ATOM 637 C C . SER A 1 83 ? 28.917 21.408 6.499 1.00 22.65 ? 83 SER A C 1 ATOM 638 O O . SER A 1 83 ? 29.694 21.594 5.546 1.00 22.86 ? 83 SER A O 1 ATOM 639 C CB . SER A 1 83 ? 27.455 23.409 6.179 1.00 23.33 ? 83 SER A CB 1 ATOM 640 O OG . SER A 1 83 ? 28.358 24.092 7.047 1.00 24.85 ? 83 SER A OG 1 ATOM 641 N N . THR A 1 84 ? 29.292 20.799 7.625 1.00 21.71 ? 84 THR A N 1 ATOM 642 C CA . THR A 1 84 ? 30.603 20.145 7.745 1.00 21.16 ? 84 THR A CA 1 ATOM 643 C C . THR A 1 84 ? 30.701 18.915 6.834 1.00 21.27 ? 84 THR A C 1 ATOM 644 O O . THR A 1 84 ? 29.687 18.407 6.323 1.00 20.99 ? 84 THR A O 1 ATOM 645 C CB . THR A 1 84 ? 30.904 19.693 9.208 1.00 20.63 ? 84 THR A CB 1 ATOM 646 O OG1 . THR A 1 84 ? 29.951 18.688 9.610 1.00 20.00 ? 84 THR A OG1 1 ATOM 647 C CG2 . THR A 1 84 ? 30.889 20.885 10.175 1.00 21.15 ? 84 THR A CG2 1 ATOM 648 N N . ARG A 1 85 ? 31.931 18.430 6.651 1.00 21.35 ? 85 ARG A N 1 ATOM 649 C CA . ARG A 1 85 ? 32.208 17.259 5.827 1.00 21.45 ? 85 ARG A CA 1 ATOM 650 C C . ARG A 1 85 ? 31.319 16.060 6.177 1.00 21.53 ? 85 ARG A C 1 ATOM 651 O O . ARG A 1 85 ? 30.760 15.411 5.282 1.00 22.25 ? 85 ARG A O 1 ATOM 652 C CB . ARG A 1 85 ? 33.672 16.880 6.018 1.00 22.07 ? 85 ARG A CB 1 ATOM 653 C CG . ARG A 1 85 ? 34.127 15.717 5.170 1.00 21.12 ? 85 ARG A CG 1 ATOM 654 C CD . ARG A 1 85 ? 35.566 15.440 5.482 1.00 23.42 ? 85 ARG A CD 1 ATOM 655 N NE . ARG A 1 85 ? 35.753 14.685 6.723 1.00 21.67 ? 85 ARG A NE 1 ATOM 656 C CZ . ARG A 1 85 ? 35.982 13.383 6.788 1.00 23.03 ? 85 ARG A CZ 1 ATOM 657 N NH1 . ARG A 1 85 ? 36.007 12.642 5.679 1.00 24.65 ? 85 ARG A NH1 1 ATOM 658 N NH2 . ARG A 1 85 ? 36.191 12.819 7.967 1.00 24.55 ? 85 ARG A NH2 1 ATOM 659 N N . LEU A 1 86 ? 31.181 15.787 7.477 1.00 20.43 ? 86 LEU A N 1 ATOM 660 C CA . LEU A 1 86 ? 30.407 14.646 7.956 1.00 20.43 ? 86 LEU A CA 1 ATOM 661 C C . LEU A 1 86 ? 28.947 14.995 8.281 1.00 20.25 ? 86 LEU A C 1 ATOM 662 O O . LEU A 1 86 ? 28.122 14.084 8.420 1.00 20.64 ? 86 LEU A O 1 ATOM 663 C CB . LEU A 1 86 ? 31.085 14.005 9.170 1.00 20.23 ? 86 LEU A CB 1 ATOM 664 C CG . LEU A 1 86 ? 32.482 13.387 8.927 1.00 20.13 ? 86 LEU A CG 1 ATOM 665 C CD1 . LEU A 1 86 ? 32.994 12.862 10.242 1.00 20.70 ? 86 LEU A CD1 1 ATOM 666 C CD2 . LEU A 1 86 ? 32.445 12.289 7.881 1.00 22.16 ? 86 LEU A CD2 1 ATOM 667 N N . GLY A 1 87 ? 28.648 16.289 8.425 1.00 19.95 ? 87 GLY A N 1 ATOM 668 C CA . GLY A 1 87 ? 27.276 16.764 8.677 1.00 20.96 ? 87 GLY A CA 1 ATOM 669 C C . GLY A 1 87 ? 26.696 16.214 9.973 1.00 20.79 ? 87 GLY A C 1 ATOM 670 O O . GLY A 1 87 ? 25.519 15.794 10.025 1.00 22.11 ? 87 GLY A O 1 ATOM 671 N N . ILE A 1 88 ? 27.503 16.211 11.025 1.00 20.15 ? 88 ILE A N 1 ATOM 672 C CA . ILE A 1 88 ? 27.021 15.742 12.328 1.00 18.76 ? 88 ILE A CA 1 ATOM 673 C C . ILE A 1 88 ? 26.217 16.876 12.977 1.00 18.64 ? 88 ILE A C 1 ATOM 674 O O . ILE A 1 88 ? 26.764 17.956 13.224 1.00 18.68 ? 88 ILE A O 1 ATOM 675 C CB . ILE A 1 88 ? 28.176 15.319 13.273 1.00 18.63 ? 88 ILE A CB 1 ATOM 676 C CG1 . ILE A 1 88 ? 29.030 14.209 12.633 1.00 19.22 ? 88 ILE A CG1 1 ATOM 677 C CG2 . ILE A 1 88 ? 27.596 14.825 14.615 1.00 18.82 ? 88 ILE A CG2 1 ATOM 678 C CD1 . ILE A 1 88 ? 30.323 13.918 13.413 1.00 19.47 ? 88 ILE A CD1 1 ATOM 679 N N . PRO A 1 89 ? 24.909 16.642 13.250 1.00 18.64 ? 89 PRO A N 1 ATOM 680 C CA . PRO A 1 89 ? 24.107 17.729 13.833 1.00 17.93 ? 89 PRO A CA 1 ATOM 681 C C . PRO A 1 89 ? 24.546 18.032 15.271 1.00 17.74 ? 89 PRO A C 1 ATOM 682 O O . PRO A 1 89 ? 24.937 17.111 16.002 1.00 17.27 ? 89 PRO A O 1 ATOM 683 C CB . PRO A 1 89 ? 22.683 17.153 13.835 1.00 18.33 ? 89 PRO A CB 1 ATOM 684 C CG . PRO A 1 89 ? 22.876 15.670 13.923 1.00 19.14 ? 89 PRO A CG 1 ATOM 685 C CD . PRO A 1 89 ? 24.112 15.407 13.071 1.00 18.67 ? 89 PRO A CD 1 ATOM 686 N N . MET A 1 90 ? 24.500 19.310 15.641 1.00 17.17 ? 90 MET A N 1 ATOM 687 C CA . MET A 1 90 ? 24.749 19.705 17.038 1.00 16.52 ? 90 MET A CA 1 ATOM 688 C C . MET A 1 90 ? 23.505 19.426 17.890 1.00 17.21 ? 90 MET A C 1 ATOM 689 O O . MET A 1 90 ? 22.383 19.363 17.377 1.00 16.74 ? 90 MET A O 1 ATOM 690 C CB . MET A 1 90 ? 25.213 21.173 17.146 1.00 17.37 ? 90 MET A CB 1 ATOM 691 C CG . MET A 1 90 ? 24.178 22.240 16.781 1.00 17.31 ? 90 MET A CG 1 ATOM 692 S SD . MET A 1 90 ? 22.989 22.574 18.102 1.00 18.52 ? 90 MET A SD 1 ATOM 693 C CE . MET A 1 90 ? 21.494 22.906 17.175 1.00 21.25 ? 90 MET A CE 1 ATOM 694 N N . ILE A 1 91 ? 23.734 19.238 19.183 1.00 16.55 ? 91 ILE A N 1 ATOM 695 C CA . ILE A 1 91 ? 22.639 19.191 20.167 1.00 16.26 ? 91 ILE A CA 1 ATOM 696 C C . ILE A 1 91 ? 22.690 20.496 20.966 1.00 16.49 ? 91 ILE A C 1 ATOM 697 O O . ILE A 1 91 ? 23.792 20.942 21.376 1.00 16.06 ? 91 ILE A O 1 ATOM 698 C CB . ILE A 1 91 ? 22.745 17.905 21.055 1.00 16.88 ? 91 ILE A CB 1 ATOM 699 C CG1 . ILE A 1 91 ? 21.509 17.733 21.955 1.00 15.56 ? 91 ILE A CG1 1 ATOM 700 C CG2 . ILE A 1 91 ? 24.063 17.840 21.857 1.00 16.87 ? 91 ILE A CG2 1 ATOM 701 C CD1 . ILE A 1 91 ? 21.494 16.404 22.709 1.00 16.82 ? 91 ILE A CD1 1 ATOM 702 N N . TYR A 1 92 ? 21.521 21.112 21.182 1.00 16.31 ? 92 TYR A N 1 ATOM 703 C CA . TYR A 1 92 ? 21.453 22.405 21.874 1.00 15.79 ? 92 TYR A CA 1 ATOM 704 C C . TYR A 1 92 ? 20.841 22.186 23.239 1.00 15.61 ? 92 TYR A C 1 ATOM 705 O O . TYR A 1 92 ? 19.731 21.662 23.321 1.00 15.56 ? 92 TYR A O 1 ATOM 706 C CB . TYR A 1 92 ? 20.616 23.414 21.073 1.00 16.01 ? 92 TYR A CB 1 ATOM 707 C CG . TYR A 1 92 ? 20.808 24.848 21.495 1.00 15.87 ? 92 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 92 ? 20.306 25.332 22.716 1.00 15.10 ? 92 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 92 ? 21.492 25.745 20.656 1.00 15.29 ? 92 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 92 ? 20.504 26.648 23.102 1.00 15.50 ? 92 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 92 ? 21.660 27.082 21.009 1.00 16.58 ? 92 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 92 ? 21.187 27.526 22.235 1.00 16.42 ? 92 TYR A CZ 1 ATOM 713 O OH . TYR A 1 92 ? 21.376 28.832 22.581 1.00 17.74 ? 92 TYR A OH 1 ATOM 714 N N . GLY A 1 93 ? 21.569 22.575 24.292 1.00 15.21 ? 93 GLY A N 1 ATOM 715 C CA . GLY A 1 93 ? 21.116 22.380 25.685 1.00 15.56 ? 93 GLY A CA 1 ATOM 716 C C . GLY A 1 93 ? 20.701 23.681 26.355 1.00 15.30 ? 93 GLY A C 1 ATOM 717 O O . GLY A 1 93 ? 21.166 24.789 26.001 1.00 15.49 ? 93 GLY A O 1 ATOM 718 N N . ILE A 1 94 ? 19.843 23.559 27.371 1.00 15.42 ? 94 ILE A N 1 ATOM 719 C CA . ILE A 1 94 ? 19.411 24.716 28.126 1.00 15.32 ? 94 ILE A CA 1 ATOM 720 C C . ILE A 1 94 ? 18.911 24.264 29.508 1.00 15.17 ? 94 ILE A C 1 ATOM 721 O O . ILE A 1 94 ? 18.471 23.119 29.667 1.00 15.32 ? 94 ILE A O 1 ATOM 722 C CB . ILE A 1 94 ? 18.271 25.462 27.367 1.00 15.15 ? 94 ILE A CB 1 ATOM 723 C CG1 . ILE A 1 94 ? 18.132 26.913 27.873 1.00 15.43 ? 94 ILE A CG1 1 ATOM 724 C CG2 . ILE A 1 94 ? 16.936 24.666 27.428 1.00 16.64 ? 94 ILE A CG2 1 ATOM 725 C CD1 . ILE A 1 94 ? 17.307 27.788 26.957 1.00 15.91 ? 94 ILE A CD1 1 ATOM 726 N N . ASP A 1 95 ? 18.976 25.162 30.488 1.00 15.68 ? 95 ASP A N 1 ATOM 727 C CA . ASP A 1 95 ? 18.390 24.875 31.818 1.00 15.19 ? 95 ASP A CA 1 ATOM 728 C C . ASP A 1 95 ? 16.880 25.093 31.755 1.00 15.71 ? 95 ASP A C 1 ATOM 729 O O . ASP A 1 95 ? 16.382 26.192 32.019 1.00 16.68 ? 95 ASP A O 1 ATOM 730 C CB . ASP A 1 95 ? 19.013 25.752 32.887 1.00 16.17 ? 95 ASP A CB 1 ATOM 731 C CG . ASP A 1 95 ? 20.468 25.446 33.056 1.00 17.88 ? 95 ASP A CG 1 ATOM 732 O OD1 . ASP A 1 95 ? 20.750 24.379 33.668 1.00 20.95 ? 95 ASP A OD1 1 ATOM 733 O OD2 . ASP A 1 95 ? 21.299 26.222 32.520 1.00 18.32 ? 95 ASP A OD2 1 ATOM 734 N N . ALA A 1 96 ? 16.168 24.039 31.382 1.00 16.18 ? 96 ALA A N 1 ATOM 735 C CA . ALA A 1 96 ? 14.709 24.017 31.474 1.00 15.87 ? 96 ALA A CA 1 ATOM 736 C C . ALA A 1 96 ? 14.438 23.203 32.724 1.00 16.52 ? 96 ALA A C 1 ATOM 737 O O . ALA A 1 96 ? 14.309 21.968 32.660 1.00 17.40 ? 96 ALA A O 1 ATOM 738 C CB . ALA A 1 96 ? 14.088 23.363 30.218 1.00 15.55 ? 96 ALA A CB 1 ATOM 739 N N . VAL A 1 97 ? 14.438 23.893 33.870 1.00 16.06 ? 97 VAL A N 1 ATOM 740 C CA . VAL A 1 97 ? 14.424 23.214 35.164 1.00 15.88 ? 97 VAL A CA 1 ATOM 741 C C . VAL A 1 97 ? 13.126 23.420 35.958 1.00 16.40 ? 97 VAL A C 1 ATOM 742 O O . VAL A 1 97 ? 12.940 22.785 36.993 1.00 17.15 ? 97 VAL A O 1 ATOM 743 C CB . VAL A 1 97 ? 15.617 23.615 36.063 1.00 15.94 ? 97 VAL A CB 1 ATOM 744 C CG1 . VAL A 1 97 ? 16.955 23.182 35.428 1.00 17.45 ? 97 VAL A CG1 1 ATOM 745 C CG2 . VAL A 1 97 ? 15.578 25.123 36.400 1.00 17.13 ? 97 VAL A CG2 1 ATOM 746 N N . HIS A 1 98 ? 12.264 24.334 35.498 1.00 15.40 ? 98 HIS A N 1 ATOM 747 C CA . HIS A 1 98 ? 10.878 24.384 36.008 1.00 15.29 ? 98 HIS A CA 1 ATOM 748 C C . HIS A 1 98 ? 9.994 24.967 34.913 1.00 15.12 ? 98 HIS A C 1 ATOM 749 O O . HIS A 1 98 ? 9.436 26.057 35.034 1.00 16.07 ? 98 HIS A O 1 ATOM 750 C CB . HIS A 1 98 ? 10.767 25.118 37.371 1.00 14.89 ? 98 HIS A CB 1 ATOM 751 C CG . HIS A 1 98 ? 11.143 26.573 37.360 1.00 14.86 ? 98 HIS A CG 1 ATOM 752 N ND1 . HIS A 1 98 ? 10.515 27.493 38.175 1.00 14.86 ? 98 HIS A ND1 1 ATOM 753 C CD2 . HIS A 1 98 ? 12.108 27.256 36.694 1.00 14.54 ? 98 HIS A CD2 1 ATOM 754 C CE1 . HIS A 1 98 ? 11.063 28.686 37.996 1.00 14.15 ? 98 HIS A CE1 1 ATOM 755 N NE2 . HIS A 1 98 ? 12.041 28.564 37.114 1.00 16.00 ? 98 HIS A NE2 1 ATOM 756 N N . GLY A 1 99 ? 9.874 24.192 33.838 1.00 15.09 ? 99 GLY A N 1 ATOM 757 C CA . GLY A 1 99 ? 9.432 24.732 32.568 1.00 15.47 ? 99 GLY A CA 1 ATOM 758 C C . GLY A 1 99 ? 10.639 25.168 31.739 1.00 15.49 ? 99 GLY A C 1 ATOM 759 O O . GLY A 1 99 ? 11.808 25.036 32.166 1.00 16.21 ? 99 GLY A O 1 ATOM 760 N N . GLN A 1 100 ? 10.343 25.693 30.555 1.00 15.30 ? 100 GLN A N 1 ATOM 761 C CA . GLN A 1 100 ? 11.368 26.224 29.632 1.00 15.44 ? 100 GLN A CA 1 ATOM 762 C C . GLN A 1 100 ? 11.696 27.669 30.078 1.00 15.27 ? 100 GLN A C 1 ATOM 763 O O . GLN A 1 100 ? 11.346 28.662 29.411 1.00 16.07 ? 100 GLN A O 1 ATOM 764 C CB . GLN A 1 100 ? 10.849 26.101 28.174 1.00 15.36 ? 100 GLN A CB 1 ATOM 765 C CG . GLN A 1 100 ? 11.666 26.792 27.046 1.00 15.86 ? 100 GLN A CG 1 ATOM 766 C CD . GLN A 1 100 ? 13.133 26.360 26.900 1.00 18.59 ? 100 GLN A CD 1 ATOM 767 O OE1 . GLN A 1 100 ? 13.689 26.257 25.759 1.00 20.10 ? 100 GLN A OE1 1 ATOM 768 N NE2 . GLN A 1 100 ? 13.779 26.150 28.016 1.00 14.73 ? 100 GLN A NE2 1 ATOM 769 N N . ASN A 1 101 ? 12.338 27.777 31.250 1.00 15.49 ? 101 ASN A N 1 ATOM 770 C CA . ASN A 1 101 ? 12.243 28.994 32.062 1.00 15.68 ? 101 ASN A CA 1 ATOM 771 C C . ASN A 1 101 ? 13.006 30.227 31.572 1.00 16.10 ? 101 ASN A C 1 ATOM 772 O O . ASN A 1 101 ? 12.759 31.321 32.082 1.00 16.93 ? 101 ASN A O 1 ATOM 773 C CB . ASN A 1 101 ? 12.640 28.680 33.508 1.00 15.83 ? 101 ASN A CB 1 ATOM 774 C CG . ASN A 1 101 ? 13.947 27.910 33.577 1.00 15.72 ? 101 ASN A CG 1 ATOM 775 O OD1 . ASN A 1 101 ? 15.063 28.460 33.361 1.00 18.93 ? 101 ASN A OD1 1 ATOM 776 N ND2 . ASN A 1 101 ? 13.825 26.638 33.821 1.00 12.74 ? 101 ASN A ND2 1 ATOM 777 N N . ASN A 1 102 ? 13.945 30.072 30.629 1.00 16.24 ? 102 ASN A N 1 ATOM 778 C CA . ASN A 1 102 ? 14.651 31.251 30.067 1.00 16.57 ? 102 ASN A CA 1 ATOM 779 C C . ASN A 1 102 ? 13.758 31.996 29.078 1.00 17.09 ? 102 ASN A C 1 ATOM 780 O O . ASN A 1 102 ? 14.053 33.132 28.694 1.00 17.56 ? 102 ASN A O 1 ATOM 781 C CB . ASN A 1 102 ? 15.922 30.842 29.319 1.00 16.52 ? 102 ASN A CB 1 ATOM 782 C CG . ASN A 1 102 ? 17.063 30.482 30.244 1.00 17.55 ? 102 ASN A CG 1 ATOM 783 O OD1 . ASN A 1 102 ? 17.599 29.364 30.183 1.00 22.07 ? 102 ASN A OD1 1 ATOM 784 N ND2 . ASN A 1 102 ? 17.466 31.424 31.074 1.00 14.63 ? 102 ASN A ND2 1 ATOM 785 N N . VAL A 1 103 ? 12.676 31.351 28.669 1.00 16.63 ? 103 VAL A N 1 ATOM 786 C CA . VAL A 1 103 ? 11.912 31.829 27.496 1.00 16.90 ? 103 VAL A CA 1 ATOM 787 C C . VAL A 1 103 ? 10.681 32.642 27.908 1.00 17.50 ? 103 VAL A C 1 ATOM 788 O O . VAL A 1 103 ? 9.882 32.200 28.749 1.00 18.39 ? 103 VAL A O 1 ATOM 789 C CB . VAL A 1 103 ? 11.511 30.630 26.594 1.00 17.04 ? 103 VAL A CB 1 ATOM 790 C CG1 . VAL A 1 103 ? 10.690 31.107 25.363 1.00 18.17 ? 103 VAL A CG1 1 ATOM 791 C CG2 . VAL A 1 103 ? 12.759 29.876 26.113 1.00 17.47 ? 103 VAL A CG2 1 ATOM 792 N N . TYR A 1 104 ? 10.511 33.812 27.289 1.00 18.11 ? 104 TYR A N 1 ATOM 793 C CA . TYR A 1 104 ? 9.380 34.669 27.573 1.00 19.12 ? 104 TYR A CA 1 ATOM 794 C C . TYR A 1 104 ? 8.089 33.944 27.201 1.00 18.52 ? 104 TYR A C 1 ATOM 795 O O . TYR A 1 104 ? 7.981 33.371 26.109 1.00 18.99 ? 104 TYR A O 1 ATOM 796 C CB . TYR A 1 104 ? 9.491 35.989 26.797 1.00 20.22 ? 104 TYR A CB 1 ATOM 797 C CG . TYR A 1 104 ? 8.319 36.884 27.081 1.00 22.50 ? 104 TYR A CG 1 ATOM 798 C CD1 . TYR A 1 104 ? 8.307 37.709 28.208 1.00 23.46 ? 104 TYR A CD1 1 ATOM 799 C CD2 . TYR A 1 104 ? 7.197 36.862 26.256 1.00 24.05 ? 104 TYR A CD2 1 ATOM 800 C CE1 . TYR A 1 104 ? 7.206 38.526 28.487 1.00 25.09 ? 104 TYR A CE1 1 ATOM 801 C CE2 . TYR A 1 104 ? 6.085 37.676 26.531 1.00 25.55 ? 104 TYR A CE2 1 ATOM 802 C CZ . TYR A 1 104 ? 6.106 38.491 27.649 1.00 24.81 ? 104 TYR A CZ 1 ATOM 803 O OH . TYR A 1 104 ? 5.002 39.289 27.900 1.00 28.05 ? 104 TYR A OH 1 ATOM 804 N N . GLY A 1 105 ? 7.120 33.933 28.109 1.00 18.26 ? 105 GLY A N 1 ATOM 805 C CA . GLY A 1 105 ? 5.852 33.278 27.823 1.00 18.30 ? 105 GLY A CA 1 ATOM 806 C C . GLY A 1 105 ? 5.825 31.779 28.039 1.00 17.88 ? 105 GLY A C 1 ATOM 807 O O . GLY A 1 105 ? 4.758 31.153 27.868 1.00 19.11 ? 105 GLY A O 1 ATOM 808 N N . ALA A 1 106 ? 6.961 31.184 28.442 1.00 16.96 ? 106 ALA A N 1 ATOM 809 C CA . ALA A 1 106 ? 6.945 29.768 28.800 1.00 16.87 ? 106 ALA A CA 1 ATOM 810 C C . ALA A 1 106 ? 6.207 29.547 30.126 1.00 16.04 ? 106 ALA A C 1 ATOM 811 O O . ALA A 1 106 ? 6.336 30.343 31.061 1.00 16.44 ? 106 ALA A O 1 ATOM 812 C CB . ALA A 1 106 ? 8.343 29.237 28.939 1.00 16.54 ? 106 ALA A CB 1 ATOM 813 N N . THR A 1 107 ? 5.489 28.437 30.218 1.00 15.72 ? 107 THR A N 1 ATOM 814 C CA . THR A 1 107 ? 4.852 28.056 31.487 1.00 16.22 ? 107 THR A CA 1 ATOM 815 C C . THR A 1 107 ? 5.942 27.866 32.539 1.00 16.00 ? 107 THR A C 1 ATOM 816 O O . THR A 1 107 ? 6.926 27.159 32.284 1.00 16.64 ? 107 THR A O 1 ATOM 817 C CB . THR A 1 107 ? 4.087 26.737 31.323 1.00 16.13 ? 107 THR A CB 1 ATOM 818 O OG1 . THR A 1 107 ? 3.140 26.860 30.239 1.00 16.98 ? 107 THR A OG1 1 ATOM 819 C CG2 . THR A 1 107 ? 3.379 26.355 32.623 1.00 17.51 ? 107 THR A CG2 1 ATOM 820 N N . ILE A 1 108 ? 5.784 28.490 33.711 1.00 15.41 ? 108 ILE A N 1 ATOM 821 C CA . ILE A 1 108 ? 6.775 28.310 34.783 1.00 14.91 ? 108 ILE A CA 1 ATOM 822 C C . ILE A 1 108 ? 6.153 27.453 35.883 1.00 15.64 ? 108 ILE A C 1 ATOM 823 O O . ILE A 1 108 ? 5.182 27.866 36.547 1.00 15.31 ? 108 ILE A O 1 ATOM 824 C CB . ILE A 1 108 ? 7.295 29.649 35.351 1.00 15.78 ? 108 ILE A CB 1 ATOM 825 C CG1 . ILE A 1 108 ? 7.876 30.536 34.225 1.00 15.51 ? 108 ILE A CG1 1 ATOM 826 C CG2 . ILE A 1 108 ? 8.311 29.345 36.468 1.00 15.22 ? 108 ILE A CG2 1 ATOM 827 C CD1 . ILE A 1 108 ? 9.066 29.892 33.457 1.00 16.85 ? 108 ILE A CD1 1 ATOM 828 N N . PHE A 1 109 ? 6.699 26.257 36.045 1.00 14.98 ? 109 PHE A N 1 ATOM 829 C CA . PHE A 1 109 ? 6.219 25.315 37.071 1.00 14.62 ? 109 PHE A CA 1 ATOM 830 C C . PHE A 1 109 ? 6.841 25.600 38.445 1.00 14.77 ? 109 PHE A C 1 ATOM 831 O O . PHE A 1 109 ? 7.867 26.284 38.526 1.00 15.06 ? 109 PHE A O 1 ATOM 832 C CB . PHE A 1 109 ? 6.520 23.866 36.645 1.00 14.79 ? 109 PHE A CB 1 ATOM 833 C CG . PHE A 1 109 ? 5.799 23.455 35.392 1.00 14.69 ? 109 PHE A CG 1 ATOM 834 C CD1 . PHE A 1 109 ? 4.523 22.884 35.478 1.00 16.39 ? 109 PHE A CD1 1 ATOM 835 C CD2 . PHE A 1 109 ? 6.379 23.656 34.133 1.00 16.64 ? 109 PHE A CD2 1 ATOM 836 C CE1 . PHE A 1 109 ? 3.814 22.514 34.327 1.00 17.15 ? 109 PHE A CE1 1 ATOM 837 C CE2 . PHE A 1 109 ? 5.684 23.295 32.955 1.00 17.20 ? 109 PHE A CE2 1 ATOM 838 C CZ . PHE A 1 109 ? 4.403 22.727 33.046 1.00 17.75 ? 109 PHE A CZ 1 ATOM 839 N N . PRO A 1 110 ? 6.227 25.069 39.534 1.00 15.47 ? 110 PRO A N 1 ATOM 840 C CA . PRO A 1 110 ? 6.866 25.192 40.842 1.00 15.10 ? 110 PRO A CA 1 ATOM 841 C C . PRO A 1 110 ? 8.273 24.627 40.827 1.00 15.00 ? 110 PRO A C 1 ATOM 842 O O . PRO A 1 110 ? 8.520 23.615 40.143 1.00 15.02 ? 110 PRO A O 1 ATOM 843 C CB . PRO A 1 110 ? 5.961 24.341 41.768 1.00 15.64 ? 110 PRO A CB 1 ATOM 844 C CG . PRO A 1 110 ? 4.597 24.423 41.099 1.00 15.16 ? 110 PRO A CG 1 ATOM 845 C CD . PRO A 1 110 ? 4.956 24.318 39.613 1.00 15.59 ? 110 PRO A CD 1 ATOM 846 N N . HIS A 1 111 ? 9.188 25.252 41.572 1.00 14.90 ? 111 HIS A N 1 ATOM 847 C CA . HIS A 1 111 ? 10.520 24.662 41.733 1.00 14.64 ? 111 HIS A CA 1 ATOM 848 C C . HIS A 1 111 ? 10.483 23.313 42.474 1.00 15.33 ? 111 HIS A C 1 ATOM 849 O O . HIS A 1 111 ? 9.472 22.960 43.115 1.00 15.34 ? 111 HIS A O 1 ATOM 850 C CB . HIS A 1 111 ? 11.468 25.649 42.418 1.00 14.52 ? 111 HIS A CB 1 ATOM 851 C CG . HIS A 1 111 ? 12.168 26.589 41.470 1.00 15.19 ? 111 HIS A CG 1 ATOM 852 N ND1 . HIS A 1 111 ? 12.996 26.149 40.451 1.00 15.98 ? 111 HIS A ND1 1 ATOM 853 C CD2 . HIS A 1 111 ? 12.177 27.944 41.399 1.00 15.27 ? 111 HIS A CD2 1 ATOM 854 C CE1 . HIS A 1 111 ? 13.493 27.193 39.808 1.00 14.50 ? 111 HIS A CE1 1 ATOM 855 N NE2 . HIS A 1 111 ? 13.011 28.294 40.356 1.00 14.79 ? 111 HIS A NE2 1 ATOM 856 N N . ASN A 1 112 ? 11.586 22.563 42.365 1.00 15.13 ? 112 ASN A N 1 ATOM 857 C CA . ASN A 1 112 ? 11.640 21.185 42.864 1.00 15.49 ? 112 ASN A CA 1 ATOM 858 C C . ASN A 1 112 ? 11.191 20.987 44.314 1.00 15.97 ? 112 ASN A C 1 ATOM 859 O O . ASN A 1 112 ? 10.463 20.031 44.595 1.00 16.29 ? 112 ASN A O 1 ATOM 860 C CB . ASN A 1 112 ? 13.040 20.582 42.642 1.00 16.07 ? 112 ASN A CB 1 ATOM 861 C CG . ASN A 1 112 ? 13.282 20.156 41.192 1.00 16.51 ? 112 ASN A CG 1 ATOM 862 O OD1 . ASN A 1 112 ? 14.360 19.625 40.858 1.00 20.97 ? 112 ASN A OD1 1 ATOM 863 N ND2 . ASN A 1 112 ? 12.285 20.336 40.343 1.00 13.80 ? 112 ASN A ND2 1 ATOM 864 N N . VAL A 1 113 ? 11.597 21.876 45.218 1.00 15.89 ? 113 VAL A N 1 ATOM 865 C CA . VAL A 1 113 ? 11.223 21.691 46.645 1.00 16.56 ? 113 VAL A CA 1 ATOM 866 C C . VAL A 1 113 ? 9.689 21.567 46.797 1.00 16.25 ? 113 VAL A C 1 ATOM 867 O O . VAL A 1 113 ? 9.199 20.659 47.479 1.00 17.05 ? 113 VAL A O 1 ATOM 868 C CB . VAL A 1 113 ? 11.838 22.774 47.585 1.00 16.41 ? 113 VAL A CB 1 ATOM 869 C CG1 . VAL A 1 113 ? 11.415 24.190 47.183 1.00 17.80 ? 113 VAL A CG1 1 ATOM 870 C CG2 . VAL A 1 113 ? 11.510 22.463 49.075 1.00 16.91 ? 113 VAL A CG2 1 ATOM 871 N N . GLY A 1 114 ? 8.938 22.423 46.099 1.00 16.03 ? 114 GLY A N 1 ATOM 872 C CA . GLY A 1 114 ? 7.468 22.345 46.128 1.00 16.32 ? 114 GLY A CA 1 ATOM 873 C C . GLY A 1 114 ? 6.940 21.095 45.474 1.00 16.86 ? 114 GLY A C 1 ATOM 874 O O . GLY A 1 114 ? 5.961 20.501 45.945 1.00 16.44 ? 114 GLY A O 1 ATOM 875 N N . LEU A 1 115 ? 7.584 20.669 44.381 1.00 16.40 ? 115 LEU A N 1 ATOM 876 C CA . LEU A 1 115 ? 7.197 19.402 43.765 1.00 16.98 ? 115 LEU A CA 1 ATOM 877 C C . LEU A 1 115 ? 7.385 18.247 44.770 1.00 16.52 ? 115 LEU A C 1 ATOM 878 O O . LEU A 1 115 ? 6.552 17.337 44.829 1.00 17.51 ? 115 LEU A O 1 ATOM 879 C CB . LEU A 1 115 ? 7.963 19.161 42.453 1.00 16.18 ? 115 LEU A CB 1 ATOM 880 C CG . LEU A 1 115 ? 7.641 20.236 41.386 1.00 16.22 ? 115 LEU A CG 1 ATOM 881 C CD1 . LEU A 1 115 ? 8.396 19.848 40.102 1.00 16.66 ? 115 LEU A CD1 1 ATOM 882 C CD2 . LEU A 1 115 ? 6.116 20.390 41.127 1.00 16.42 ? 115 LEU A CD2 1 ATOM 883 N N . GLY A 1 116 ? 8.458 18.295 45.559 1.00 17.61 ? 116 GLY A N 1 ATOM 884 C CA . GLY A 1 116 ? 8.674 17.281 46.603 1.00 17.65 ? 116 GLY A CA 1 ATOM 885 C C . GLY A 1 116 ? 7.507 17.260 47.581 1.00 18.55 ? 116 GLY A C 1 ATOM 886 O O . GLY A 1 116 ? 7.083 16.192 48.024 1.00 18.98 ? 116 GLY A O 1 ATOM 887 N N . ALA A 1 117 ? 6.985 18.439 47.910 1.00 18.29 ? 117 ALA A N 1 ATOM 888 C CA . ALA A 1 117 ? 5.844 18.549 48.852 1.00 18.86 ? 117 ALA A CA 1 ATOM 889 C C . ALA A 1 117 ? 4.584 17.838 48.340 1.00 19.15 ? 117 ALA A C 1 ATOM 890 O O . ALA A 1 117 ? 3.699 17.453 49.121 1.00 19.41 ? 117 ALA A O 1 ATOM 891 C CB . ALA A 1 117 ? 5.556 20.006 49.164 1.00 18.99 ? 117 ALA A CB 1 ATOM 892 N N . THR A 1 118 ? 4.480 17.669 47.020 1.00 18.93 ? 118 THR A N 1 ATOM 893 C CA . THR A 1 118 ? 3.285 17.063 46.445 1.00 19.76 ? 118 THR A CA 1 ATOM 894 C C . THR A 1 118 ? 3.231 15.553 46.654 1.00 20.03 ? 118 THR A C 1 ATOM 895 O O . THR A 1 118 ? 2.148 14.965 46.556 1.00 21.32 ? 118 THR A O 1 ATOM 896 C CB . THR A 1 118 ? 3.148 17.328 44.912 1.00 19.57 ? 118 THR A CB 1 ATOM 897 O OG1 . THR A 1 118 ? 4.083 16.490 44.204 1.00 19.05 ? 118 THR A OG1 1 ATOM 898 C CG2 . THR A 1 118 ? 3.341 18.832 44.564 1.00 18.92 ? 118 THR A CG2 1 ATOM 899 N N . ARG A 1 119 ? 4.394 14.928 46.892 1.00 20.46 ? 119 ARG A N 1 ATOM 900 C CA . ARG A 1 119 ? 4.521 13.457 46.929 1.00 21.27 ? 119 ARG A CA 1 ATOM 901 C C . ARG A 1 119 ? 3.823 12.775 45.733 1.00 22.02 ? 119 ARG A C 1 ATOM 902 O O . ARG A 1 119 ? 3.230 11.700 45.873 1.00 23.05 ? 119 ARG A O 1 ATOM 903 C CB . ARG A 1 119 ? 3.960 12.906 48.259 1.00 21.23 ? 119 ARG A CB 1 ATOM 904 C CG . ARG A 1 119 ? 4.621 13.489 49.480 1.00 21.91 ? 119 ARG A CG 1 ATOM 905 C CD . ARG A 1 119 ? 6.121 13.196 49.602 1.00 22.35 ? 119 ARG A CD 1 ATOM 906 N NE . ARG A 1 119 ? 6.503 13.325 51.008 1.00 22.54 ? 119 ARG A NE 1 ATOM 907 C CZ . ARG A 1 119 ? 6.734 14.475 51.630 1.00 21.92 ? 119 ARG A CZ 1 ATOM 908 N NH1 . ARG A 1 119 ? 6.717 15.628 50.941 1.00 19.69 ? 119 ARG A NH1 1 ATOM 909 N NH2 . ARG A 1 119 ? 7.033 14.472 52.940 1.00 22.55 ? 119 ARG A NH2 1 ATOM 910 N N . ASP A 1 120 ? 3.873 13.410 44.558 1.00 21.69 ? 120 ASP A N 1 ATOM 911 C CA . ASP A 1 120 ? 3.109 12.937 43.407 1.00 22.20 ? 120 ASP A CA 1 ATOM 912 C C . ASP A 1 120 ? 4.014 12.753 42.175 1.00 22.01 ? 120 ASP A C 1 ATOM 913 O O . ASP A 1 120 ? 4.112 13.657 41.339 1.00 21.37 ? 120 ASP A O 1 ATOM 914 C CB . ASP A 1 120 ? 1.964 13.911 43.126 1.00 22.97 ? 120 ASP A CB 1 ATOM 915 C CG . ASP A 1 120 ? 0.962 13.388 42.095 1.00 25.56 ? 120 ASP A CG 1 ATOM 916 O OD1 . ASP A 1 120 ? 1.238 12.395 41.375 1.00 28.09 ? 120 ASP A OD1 1 ATOM 917 O OD2 . ASP A 1 120 ? -0.113 14.014 41.989 1.00 27.98 ? 120 ASP A OD2 1 ATOM 918 N N . PRO A 1 121 ? 4.708 11.605 42.088 1.00 21.93 ? 121 PRO A N 1 ATOM 919 C CA . PRO A 1 121 ? 5.613 11.369 40.947 1.00 21.87 ? 121 PRO A CA 1 ATOM 920 C C . PRO A 1 121 ? 4.932 11.448 39.573 1.00 21.59 ? 121 PRO A C 1 ATOM 921 O O . PRO A 1 121 ? 5.570 11.860 38.592 1.00 21.09 ? 121 PRO A O 1 ATOM 922 C CB . PRO A 1 121 ? 6.154 9.960 41.213 1.00 22.19 ? 121 PRO A CB 1 ATOM 923 C CG . PRO A 1 121 ? 6.027 9.787 42.719 1.00 22.90 ? 121 PRO A CG 1 ATOM 924 C CD . PRO A 1 121 ? 4.760 10.498 43.072 1.00 22.15 ? 121 PRO A CD 1 ATOM 925 N N . TYR A 1 122 ? 3.658 11.059 39.480 1.00 21.41 ? 122 TYR A N 1 ATOM 926 C CA . TYR A 1 122 ? 2.959 11.115 38.205 1.00 21.95 ? 122 TYR A CA 1 ATOM 927 C C . TYR A 1 122 ? 2.728 12.558 37.761 1.00 20.81 ? 122 TYR A C 1 ATOM 928 O O . TYR A 1 122 ? 2.844 12.884 36.578 1.00 20.29 ? 122 TYR A O 1 ATOM 929 C CB . TYR A 1 122 ? 1.643 10.329 38.225 1.00 24.01 ? 122 TYR A CB 1 ATOM 930 C CG . TYR A 1 122 ? 0.964 10.334 36.875 1.00 25.31 ? 122 TYR A CG 1 ATOM 931 C CD1 . TYR A 1 122 ? 1.658 9.930 35.721 1.00 27.19 ? 122 TYR A CD1 1 ATOM 932 C CD2 . TYR A 1 122 ? -0.348 10.779 36.737 1.00 25.90 ? 122 TYR A CD2 1 ATOM 933 C CE1 . TYR A 1 122 ? 1.042 9.961 34.471 1.00 28.28 ? 122 TYR A CE1 1 ATOM 934 C CE2 . TYR A 1 122 ? -0.981 10.803 35.489 1.00 27.26 ? 122 TYR A CE2 1 ATOM 935 C CZ . TYR A 1 122 ? -0.285 10.391 34.370 1.00 27.66 ? 122 TYR A CZ 1 ATOM 936 O OH . TYR A 1 122 ? -0.902 10.427 33.137 1.00 29.76 ? 122 TYR A OH 1 ATOM 937 N N . LEU A 1 123 ? 2.433 13.432 38.723 1.00 20.13 ? 123 LEU A N 1 ATOM 938 C CA . LEU A 1 123 ? 2.345 14.866 38.449 1.00 19.39 ? 123 LEU A CA 1 ATOM 939 C C . LEU A 1 123 ? 3.679 15.347 37.851 1.00 18.87 ? 123 LEU A C 1 ATOM 940 O O . LEU A 1 123 ? 3.708 16.075 36.846 1.00 18.74 ? 123 LEU A O 1 ATOM 941 C CB . LEU A 1 123 ? 2.071 15.628 39.753 1.00 19.42 ? 123 LEU A CB 1 ATOM 942 C CG . LEU A 1 123 ? 2.120 17.155 39.683 1.00 19.35 ? 123 LEU A CG 1 ATOM 943 C CD1 . LEU A 1 123 ? 0.939 17.721 38.874 1.00 21.45 ? 123 LEU A CD1 1 ATOM 944 C CD2 . LEU A 1 123 ? 2.185 17.733 41.114 1.00 20.83 ? 123 LEU A CD2 1 ATOM 945 N N . VAL A 1 124 ? 4.780 14.955 38.487 1.00 18.58 ? 124 VAL A N 1 ATOM 946 C CA . VAL A 1 124 ? 6.114 15.377 38.027 1.00 17.82 ? 124 VAL A CA 1 ATOM 947 C C . VAL A 1 124 ? 6.395 14.809 36.613 1.00 17.71 ? 124 VAL A C 1 ATOM 948 O O . VAL A 1 124 ? 6.940 15.506 35.740 1.00 17.08 ? 124 VAL A O 1 ATOM 949 C CB . VAL A 1 124 ? 7.206 15.035 39.084 1.00 17.87 ? 124 VAL A CB 1 ATOM 950 C CG1 . VAL A 1 124 ? 8.606 15.293 38.548 1.00 18.14 ? 124 VAL A CG1 1 ATOM 951 C CG2 . VAL A 1 124 ? 6.962 15.879 40.383 1.00 17.79 ? 124 VAL A CG2 1 ATOM 952 N N . LYS A 1 125 ? 5.981 13.568 36.368 1.00 17.95 ? 125 LYS A N 1 ATOM 953 C CA . LYS A 1 125 ? 6.129 13.003 35.013 1.00 18.43 ? 125 LYS A CA 1 ATOM 954 C C . LYS A 1 125 ? 5.400 13.887 34.007 1.00 18.27 ? 125 LYS A C 1 ATOM 955 O O . LYS A 1 125 ? 5.955 14.245 32.967 1.00 18.13 ? 125 LYS A O 1 ATOM 956 C CB . LYS A 1 125 ? 5.586 11.576 34.940 1.00 18.15 ? 125 LYS A CB 1 ATOM 957 C CG . LYS A 1 125 ? 5.959 10.872 33.620 1.00 19.38 ? 125 LYS A CG 1 ATOM 958 C CD . LYS A 1 125 ? 5.316 9.500 33.513 1.00 21.84 ? 125 LYS A CD 1 ATOM 959 C CE . LYS A 1 125 ? 5.559 8.876 32.146 1.00 23.72 ? 125 LYS A CE 1 ATOM 960 N NZ . LYS A 1 125 ? 5.094 7.446 32.155 1.00 25.67 ? 125 LYS A NZ 1 ATOM 961 N N . ARG A 1 126 ? 4.153 14.258 34.317 1.00 17.82 ? 126 ARG A N 1 ATOM 962 C CA . ARG A 1 126 ? 3.383 15.094 33.405 1.00 20.68 ? 126 ARG A CA 1 ATOM 963 C C . ARG A 1 126 ? 4.021 16.473 33.210 1.00 16.95 ? 126 ARG A C 1 ATOM 964 O O . ARG A 1 126 ? 3.985 17.038 32.107 1.00 16.96 ? 126 ARG A O 1 ATOM 965 C CB . ARG A 1 126 ? 1.957 15.236 33.935 1.00 18.03 ? 126 ARG A CB 1 ATOM 966 C CG . ARG A 1 126 ? 1.175 13.905 33.852 1.00 23.38 ? 126 ARG A CG 1 ATOM 967 C CD . ARG A 1 126 ? 0.068 13.821 34.948 1.00 18.40 ? 126 ARG A CD 1 ATOM 968 N NE . ARG A 1 126 ? -0.838 14.969 34.960 1.00 42.74 ? 126 ARG A NE 1 ATOM 969 C CZ . ARG A 1 126 ? -1.446 15.501 36.030 1.00 21.31 ? 126 ARG A CZ 1 ATOM 970 N NH1 . ARG A 1 126 ? -1.284 15.027 37.278 1.00 34.75 ? 126 ARG A NH1 1 ATOM 971 N NH2 . ARG A 1 126 ? -2.235 16.554 35.837 1.00 41.88 ? 126 ARG A NH2 1 ATOM 972 N N . ILE A 1 127 ? 4.617 17.008 34.274 1.00 16.85 ? 127 ILE A N 1 ATOM 973 C CA . ILE A 1 127 ? 5.412 18.245 34.152 1.00 16.19 ? 127 ILE A CA 1 ATOM 974 C C . ILE A 1 127 ? 6.594 18.035 33.178 1.00 16.46 ? 127 ILE A C 1 ATOM 975 O O . ILE A 1 127 ? 6.830 18.889 32.325 1.00 16.68 ? 127 ILE A O 1 ATOM 976 C CB . ILE A 1 127 ? 5.900 18.775 35.514 1.00 15.76 ? 127 ILE A CB 1 ATOM 977 C CG1 . ILE A 1 127 ? 4.701 19.229 36.353 1.00 16.08 ? 127 ILE A CG1 1 ATOM 978 C CG2 . ILE A 1 127 ? 6.929 19.929 35.318 1.00 17.02 ? 127 ILE A CG2 1 ATOM 979 C CD1 . ILE A 1 127 ? 5.049 19.628 37.781 1.00 15.36 ? 127 ILE A CD1 1 ATOM 980 N N . GLY A 1 128 ? 7.304 16.907 33.294 1.00 15.88 ? 128 GLY A N 1 ATOM 981 C CA . GLY A 1 128 ? 8.373 16.550 32.325 1.00 16.79 ? 128 GLY A CA 1 ATOM 982 C C . GLY A 1 128 ? 7.826 16.541 30.902 1.00 17.35 ? 128 GLY A C 1 ATOM 983 O O . GLY A 1 128 ? 8.447 17.091 29.980 1.00 17.31 ? 128 GLY A O 1 ATOM 984 N N . GLU A 1 129 ? 6.665 15.906 30.713 1.00 17.86 ? 129 GLU A N 1 ATOM 985 C CA . GLU A 1 129 ? 6.021 15.862 29.383 1.00 19.24 ? 129 GLU A CA 1 ATOM 986 C C . GLU A 1 129 ? 5.739 17.253 28.806 1.00 18.33 ? 129 GLU A C 1 ATOM 987 O O . GLU A 1 129 ? 6.068 17.547 27.637 1.00 18.09 ? 129 GLU A O 1 ATOM 988 C CB . GLU A 1 129 ? 4.760 14.999 29.440 1.00 19.58 ? 129 GLU A CB 1 ATOM 989 C CG . GLU A 1 129 ? 5.067 13.590 29.914 1.00 21.13 ? 129 GLU A CG 1 ATOM 990 C CD . GLU A 1 129 ? 3.835 12.700 30.075 1.00 23.17 ? 129 GLU A CD 1 ATOM 991 O OE1 . GLU A 1 129 ? 4.034 11.475 30.246 1.00 27.74 ? 129 GLU A OE1 1 ATOM 992 O OE2 . GLU A 1 129 ? 2.689 13.208 30.010 1.00 27.04 ? 129 GLU A OE2 1 ATOM 993 N N . ALA A 1 130 ? 5.159 18.124 29.634 1.00 17.52 ? 130 ALA A N 1 ATOM 994 C CA . ALA A 1 130 ? 4.807 19.477 29.200 1.00 17.45 ? 130 ALA A CA 1 ATOM 995 C C . ALA A 1 130 ? 6.086 20.280 28.917 1.00 16.86 ? 130 ALA A C 1 ATOM 996 O O . ALA A 1 130 ? 6.159 21.057 27.955 1.00 17.43 ? 130 ALA A O 1 ATOM 997 C CB . ALA A 1 130 ? 3.945 20.170 30.259 1.00 17.95 ? 130 ALA A CB 1 ATOM 998 N N . THR A 1 131 ? 7.092 20.076 29.762 1.00 16.61 ? 131 THR A N 1 ATOM 999 C CA . THR A 1 131 ? 8.354 20.802 29.634 1.00 16.62 ? 131 THR A CA 1 ATOM 1000 C C . THR A 1 131 ? 9.045 20.415 28.320 1.00 16.48 ? 131 THR A C 1 ATOM 1001 O O . THR A 1 131 ? 9.511 21.299 27.594 1.00 16.88 ? 131 THR A O 1 ATOM 1002 C CB . THR A 1 131 ? 9.266 20.558 30.849 1.00 16.54 ? 131 THR A CB 1 ATOM 1003 O OG1 . THR A 1 131 ? 8.616 21.066 32.028 1.00 16.72 ? 131 THR A OG1 1 ATOM 1004 C CG2 . THR A 1 131 ? 10.598 21.299 30.663 1.00 16.64 ? 131 THR A CG2 1 ATOM 1005 N N . ALA A 1 132 ? 9.067 19.120 27.993 1.00 16.60 ? 132 ALA A N 1 ATOM 1006 C CA . ALA A 1 132 ? 9.667 18.656 26.711 1.00 17.07 ? 132 ALA A CA 1 ATOM 1007 C C . ALA A 1 132 ? 9.018 19.375 25.526 1.00 17.59 ? 132 ALA A C 1 ATOM 1008 O O . ALA A 1 132 ? 9.716 19.804 24.591 1.00 18.23 ? 132 ALA A O 1 ATOM 1009 C CB . ALA A 1 132 ? 9.531 17.148 26.549 1.00 17.65 ? 132 ALA A CB 1 ATOM 1010 N N . LEU A 1 133 ? 7.691 19.536 25.576 1.00 17.34 ? 133 LEU A N 1 ATOM 1011 C CA . LEU A 1 133 ? 6.958 20.192 24.475 1.00 17.80 ? 133 LEU A CA 1 ATOM 1012 C C . LEU A 1 133 ? 7.320 21.665 24.354 1.00 17.80 ? 133 LEU A C 1 ATOM 1013 O O . LEU A 1 133 ? 7.495 22.182 23.238 1.00 18.10 ? 133 LEU A O 1 ATOM 1014 C CB . LEU A 1 133 ? 5.444 20.021 24.629 1.00 18.03 ? 133 LEU A CB 1 ATOM 1015 C CG . LEU A 1 133 ? 4.927 18.580 24.483 1.00 19.64 ? 133 LEU A CG 1 ATOM 1016 C CD1 . LEU A 1 133 ? 3.444 18.526 24.893 1.00 20.85 ? 133 LEU A CD1 1 ATOM 1017 C CD2 . LEU A 1 133 ? 5.105 18.061 23.052 1.00 21.54 ? 133 LEU A CD2 1 ATOM 1018 N N . GLU A 1 134 ? 7.453 22.336 25.500 1.00 16.75 ? 134 GLU A N 1 ATOM 1019 C CA . GLU A 1 134 ? 7.768 23.757 25.484 1.00 17.04 ? 134 GLU A CA 1 ATOM 1020 C C . GLU A 1 134 ? 9.235 23.995 25.098 1.00 16.66 ? 134 GLU A C 1 ATOM 1021 O O . GLU A 1 134 ? 9.543 25.008 24.474 1.00 16.63 ? 134 GLU A O 1 ATOM 1022 C CB . GLU A 1 134 ? 7.378 24.453 26.791 1.00 17.71 ? 134 GLU A CB 1 ATOM 1023 C CG . GLU A 1 134 ? 5.875 24.284 27.086 1.00 17.40 ? 134 GLU A CG 1 ATOM 1024 C CD . GLU A 1 134 ? 5.236 25.456 27.853 1.00 17.65 ? 134 GLU A CD 1 ATOM 1025 O OE1 . GLU A 1 134 ? 5.857 26.521 28.001 1.00 17.87 ? 134 GLU A OE1 1 ATOM 1026 O OE2 . GLU A 1 134 ? 4.081 25.287 28.282 1.00 19.00 ? 134 GLU A OE2 1 ATOM 1027 N N . VAL A 1 135 ? 10.117 23.055 25.453 1.00 16.16 ? 135 VAL A N 1 ATOM 1028 C CA . VAL A 1 135 ? 11.520 23.125 25.024 1.00 16.03 ? 135 VAL A CA 1 ATOM 1029 C C . VAL A 1 135 ? 11.595 22.895 23.497 1.00 16.22 ? 135 VAL A C 1 ATOM 1030 O O . VAL A 1 135 ? 12.238 23.673 22.787 1.00 16.65 ? 135 VAL A O 1 ATOM 1031 C CB . VAL A 1 135 ? 12.401 22.147 25.809 1.00 15.24 ? 135 VAL A CB 1 ATOM 1032 C CG1 . VAL A 1 135 ? 13.845 22.108 25.230 1.00 15.00 ? 135 VAL A CG1 1 ATOM 1033 C CG2 . VAL A 1 135 ? 12.432 22.593 27.301 1.00 15.15 ? 135 VAL A CG2 1 ATOM 1034 N N . ARG A 1 136 ? 10.927 21.847 22.997 1.00 16.60 ? 136 ARG A N 1 ATOM 1035 C CA . ARG A 1 136 ? 10.873 21.615 21.534 1.00 17.38 ? 136 ARG A CA 1 ATOM 1036 C C . ARG A 1 136 ? 10.170 22.757 20.756 1.00 17.53 ? 136 ARG A C 1 ATOM 1037 O O . ARG A 1 136 ? 10.491 23.017 19.576 1.00 17.61 ? 136 ARG A O 1 ATOM 1038 C CB . ARG A 1 136 ? 10.249 20.256 21.204 1.00 16.95 ? 136 ARG A CB 1 ATOM 1039 C CG . ARG A 1 136 ? 11.193 19.104 21.519 1.00 16.23 ? 136 ARG A CG 1 ATOM 1040 C CD . ARG A 1 136 ? 12.373 19.054 20.516 1.00 17.56 ? 136 ARG A CD 1 ATOM 1041 N NE . ARG A 1 136 ? 13.062 17.774 20.623 1.00 18.02 ? 136 ARG A NE 1 ATOM 1042 C CZ . ARG A 1 136 ? 13.867 17.255 19.691 1.00 19.44 ? 136 ARG A CZ 1 ATOM 1043 N NH1 . ARG A 1 136 ? 14.139 17.936 18.573 1.00 19.24 ? 136 ARG A NH1 1 ATOM 1044 N NH2 . ARG A 1 136 ? 14.403 16.051 19.887 1.00 20.61 ? 136 ARG A NH2 1 ATOM 1045 N N . ALA A 1 137 ? 9.240 23.456 21.414 1.00 17.74 ? 137 ALA A N 1 ATOM 1046 C CA . ALA A 1 137 ? 8.611 24.646 20.810 1.00 17.68 ? 137 ALA A CA 1 ATOM 1047 C C . ALA A 1 137 ? 9.641 25.702 20.394 1.00 17.97 ? 137 ALA A C 1 ATOM 1048 O O . ALA A 1 137 ? 9.395 26.498 19.489 1.00 17.45 ? 137 ALA A O 1 ATOM 1049 C CB . ALA A 1 137 ? 7.602 25.280 21.787 1.00 17.75 ? 137 ALA A CB 1 ATOM 1050 N N . THR A 1 138 ? 10.770 25.717 21.111 1.00 16.95 ? 138 THR A N 1 ATOM 1051 C CA . THR A 1 138 ? 11.844 26.680 20.897 1.00 17.25 ? 138 THR A CA 1 ATOM 1052 C C . THR A 1 138 ? 13.005 26.079 20.078 1.00 17.14 ? 138 THR A C 1 ATOM 1053 O O . THR A 1 138 ? 14.043 26.721 19.890 1.00 18.28 ? 138 THR A O 1 ATOM 1054 C CB . THR A 1 138 ? 12.339 27.275 22.243 1.00 16.72 ? 138 THR A CB 1 ATOM 1055 O OG1 . THR A 1 138 ? 12.956 26.248 23.040 1.00 17.48 ? 138 THR A OG1 1 ATOM 1056 C CG2 . THR A 1 138 ? 11.162 27.912 23.017 1.00 17.62 ? 138 THR A CG2 1 ATOM 1057 N N . GLY A 1 139 ? 12.824 24.857 19.584 1.00 18.06 ? 139 GLY A N 1 ATOM 1058 C CA . GLY A 1 139 ? 13.844 24.200 18.735 1.00 17.67 ? 139 GLY A CA 1 ATOM 1059 C C . GLY A 1 139 ? 14.957 23.507 19.509 1.00 18.58 ? 139 GLY A C 1 ATOM 1060 O O . GLY A 1 139 ? 15.881 22.940 18.922 1.00 20.27 ? 139 GLY A O 1 ATOM 1061 N N . ILE A 1 140 ? 14.858 23.518 20.832 1.00 16.86 ? 140 ILE A N 1 ATOM 1062 C CA . ILE A 1 140 ? 15.926 22.985 21.664 1.00 16.73 ? 140 ILE A CA 1 ATOM 1063 C C . ILE A 1 140 ? 15.662 21.504 21.968 1.00 16.86 ? 140 ILE A C 1 ATOM 1064 O O . ILE A 1 140 ? 14.489 21.099 22.128 1.00 17.69 ? 140 ILE A O 1 ATOM 1065 C CB . ILE A 1 140 ? 16.105 23.879 22.921 1.00 15.58 ? 140 ILE A CB 1 ATOM 1066 C CG1 . ILE A 1 140 ? 16.647 25.248 22.458 1.00 16.64 ? 140 ILE A CG1 1 ATOM 1067 C CG2 . ILE A 1 140 ? 17.051 23.224 23.950 1.00 15.99 ? 140 ILE A CG2 1 ATOM 1068 C CD1 . ILE A 1 140 ? 16.648 26.360 23.499 1.00 18.48 ? 140 ILE A CD1 1 ATOM 1069 N N . GLN A 1 141 ? 16.736 20.709 22.008 1.00 16.43 ? 141 GLN A N 1 ATOM 1070 C CA . GLN A 1 141 ? 16.610 19.249 22.058 1.00 16.11 ? 141 GLN A CA 1 ATOM 1071 C C . GLN A 1 141 ? 17.069 18.597 23.365 1.00 15.60 ? 141 GLN A C 1 ATOM 1072 O O . GLN A 1 141 ? 16.993 17.375 23.495 1.00 15.82 ? 141 GLN A O 1 ATOM 1073 C CB . GLN A 1 141 ? 17.378 18.581 20.895 1.00 17.02 ? 141 GLN A CB 1 ATOM 1074 C CG . GLN A 1 141 ? 17.124 19.205 19.530 1.00 17.26 ? 141 GLN A CG 1 ATOM 1075 C CD . GLN A 1 141 ? 18.211 20.204 19.135 1.00 19.57 ? 141 GLN A CD 1 ATOM 1076 O OE1 . GLN A 1 141 ? 18.941 20.735 19.990 1.00 18.83 ? 141 GLN A OE1 1 ATOM 1077 N NE2 . GLN A 1 141 ? 18.299 20.487 17.838 1.00 20.31 ? 141 GLN A NE2 1 ATOM 1078 N N . TYR A 1 142 ? 17.559 19.413 24.308 1.00 14.94 ? 142 TYR A N 1 ATOM 1079 C CA . TYR A 1 142 ? 18.299 18.893 25.469 1.00 15.24 ? 142 TYR A CA 1 ATOM 1080 C C . TYR A 1 142 ? 18.082 19.805 26.673 1.00 15.17 ? 142 TYR A C 1 ATOM 1081 O O . TYR A 1 142 ? 18.370 21.015 26.611 1.00 15.82 ? 142 TYR A O 1 ATOM 1082 C CB . TYR A 1 142 ? 19.779 18.835 25.066 1.00 15.06 ? 142 TYR A CB 1 ATOM 1083 C CG . TYR A 1 142 ? 20.785 18.372 26.103 1.00 16.03 ? 142 TYR A CG 1 ATOM 1084 C CD1 . TYR A 1 142 ? 20.414 17.566 27.195 1.00 15.73 ? 142 TYR A CD1 1 ATOM 1085 C CD2 . TYR A 1 142 ? 22.140 18.674 25.929 1.00 16.88 ? 142 TYR A CD2 1 ATOM 1086 C CE1 . TYR A 1 142 ? 21.388 17.136 28.130 1.00 17.22 ? 142 TYR A CE1 1 ATOM 1087 C CE2 . TYR A 1 142 ? 23.107 18.241 26.834 1.00 16.93 ? 142 TYR A CE2 1 ATOM 1088 C CZ . TYR A 1 142 ? 22.726 17.470 27.922 1.00 16.81 ? 142 TYR A CZ 1 ATOM 1089 O OH . TYR A 1 142 ? 23.703 17.067 28.802 1.00 17.86 ? 142 TYR A OH 1 ATOM 1090 N N . ALA A 1 143 ? 17.541 19.233 27.755 1.00 15.27 ? 143 ALA A N 1 ATOM 1091 C CA . ALA A 1 143 ? 17.278 19.985 29.003 1.00 14.82 ? 143 ALA A CA 1 ATOM 1092 C C . ALA A 1 143 ? 18.225 19.507 30.109 1.00 15.05 ? 143 ALA A C 1 ATOM 1093 O O . ALA A 1 143 ? 18.364 18.281 30.337 1.00 15.81 ? 143 ALA A O 1 ATOM 1094 C CB . ALA A 1 143 ? 15.812 19.771 29.451 1.00 15.61 ? 143 ALA A CB 1 ATOM 1095 N N . PHE A 1 144 ? 18.835 20.461 30.821 1.00 14.84 ? 144 PHE A N 1 ATOM 1096 C CA . PHE A 1 144 ? 19.753 20.127 31.928 1.00 14.73 ? 144 PHE A CA 1 ATOM 1097 C C . PHE A 1 144 ? 18.936 19.865 33.203 1.00 14.94 ? 144 PHE A C 1 ATOM 1098 O O . PHE A 1 144 ? 18.993 20.636 34.173 1.00 15.84 ? 144 PHE A O 1 ATOM 1099 C CB . PHE A 1 144 ? 20.762 21.244 32.183 1.00 15.32 ? 144 PHE A CB 1 ATOM 1100 C CG . PHE A 1 144 ? 21.659 21.554 31.000 1.00 16.14 ? 144 PHE A CG 1 ATOM 1101 C CD1 . PHE A 1 144 ? 22.346 20.547 30.330 1.00 15.86 ? 144 PHE A CD1 1 ATOM 1102 C CD2 . PHE A 1 144 ? 21.822 22.879 30.591 1.00 16.52 ? 144 PHE A CD2 1 ATOM 1103 C CE1 . PHE A 1 144 ? 23.199 20.850 29.227 1.00 18.52 ? 144 PHE A CE1 1 ATOM 1104 C CE2 . PHE A 1 144 ? 22.661 23.200 29.493 1.00 19.95 ? 144 PHE A CE2 1 ATOM 1105 C CZ . PHE A 1 144 ? 23.345 22.175 28.815 1.00 16.79 ? 144 PHE A CZ 1 ATOM 1106 N N . ALA A 1 145 ? 18.170 18.780 33.186 1.00 15.03 ? 145 ALA A N 1 ATOM 1107 C CA . ALA A 1 145 ? 17.261 18.442 34.300 1.00 15.29 ? 145 ALA A CA 1 ATOM 1108 C C . ALA A 1 145 ? 16.977 16.945 34.225 1.00 15.52 ? 145 ALA A C 1 ATOM 1109 O O . ALA A 1 145 ? 16.977 16.377 33.126 1.00 15.45 ? 145 ALA A O 1 ATOM 1110 C CB . ALA A 1 145 ? 15.953 19.234 34.165 1.00 15.79 ? 145 ALA A CB 1 ATOM 1111 N N . PRO A 1 146 ? 16.678 16.302 35.374 1.00 16.21 ? 146 PRO A N 1 ATOM 1112 C CA . PRO A 1 146 ? 16.485 16.878 36.705 1.00 16.53 ? 146 PRO A CA 1 ATOM 1113 C C . PRO A 1 146 ? 17.732 17.046 37.559 1.00 17.16 ? 146 PRO A C 1 ATOM 1114 O O . PRO A 1 146 ? 18.672 16.210 37.513 1.00 17.28 ? 146 PRO A O 1 ATOM 1115 C CB . PRO A 1 146 ? 15.605 15.832 37.404 1.00 16.83 ? 146 PRO A CB 1 ATOM 1116 C CG . PRO A 1 146 ? 16.111 14.507 36.826 1.00 16.78 ? 146 PRO A CG 1 ATOM 1117 C CD . PRO A 1 146 ? 16.472 14.842 35.359 1.00 16.37 ? 146 PRO A CD 1 ATOM 1118 N N . CYS A 1 147 ? 17.697 18.086 38.389 1.00 17.56 ? 147 CYS A N 1 ATOM 1119 C CA . CYS A 1 147 ? 18.586 18.139 39.545 1.00 18.01 ? 147 CYS A CA 1 ATOM 1120 C C . CYS A 1 147 ? 18.080 17.109 40.552 1.00 18.17 ? 147 CYS A C 1 ATOM 1121 O O . CYS A 1 147 ? 16.975 17.257 41.096 1.00 17.87 ? 147 CYS A O 1 ATOM 1122 C CB . CYS A 1 147 ? 18.579 19.534 40.196 1.00 18.29 ? 147 CYS A CB 1 ATOM 1123 S SG . CYS A 1 147 ? 19.656 19.584 41.629 1.00 21.37 ? 147 CYS A SG 1 ATOM 1124 N N . ILE A 1 148 ? 18.890 16.073 40.768 1.00 17.44 ? 148 ILE A N 1 ATOM 1125 C CA . ILE A 1 148 ? 18.591 15.038 41.772 1.00 18.56 ? 148 ILE A CA 1 ATOM 1126 C C . ILE A 1 148 ? 19.494 15.143 43.008 1.00 18.75 ? 148 ILE A C 1 ATOM 1127 O O . ILE A 1 148 ? 19.721 14.150 43.716 1.00 19.56 ? 148 ILE A O 1 ATOM 1128 C CB . ILE A 1 148 ? 18.537 13.600 41.156 1.00 18.66 ? 148 ILE A CB 1 ATOM 1129 C CG1 . ILE A 1 148 ? 19.856 13.217 40.434 1.00 18.51 ? 148 ILE A CG1 1 ATOM 1130 C CG2 . ILE A 1 148 ? 17.314 13.448 40.250 1.00 19.18 ? 148 ILE A CG2 1 ATOM 1131 C CD1 . ILE A 1 148 ? 19.963 11.712 40.085 1.00 19.90 ? 148 ILE A CD1 1 ATOM 1132 N N . ALA A 1 149 ? 19.959 16.356 43.296 1.00 18.67 ? 149 ALA A N 1 ATOM 1133 C CA . ALA A 1 149 ? 20.638 16.664 44.561 1.00 19.06 ? 149 ALA A CA 1 ATOM 1134 C C . ALA A 1 149 ? 19.696 16.316 45.709 1.00 19.05 ? 149 ALA A C 1 ATOM 1135 O O . ALA A 1 149 ? 18.480 16.518 45.608 1.00 18.61 ? 149 ALA A O 1 ATOM 1136 C CB . ALA A 1 149 ? 20.995 18.146 44.651 1.00 19.30 ? 149 ALA A CB 1 ATOM 1137 N N . VAL A 1 150 ? 20.272 15.779 46.781 1.00 18.68 ? 150 VAL A N 1 ATOM 1138 C CA . VAL A 1 150 ? 19.552 15.571 48.043 1.00 20.10 ? 150 VAL A CA 1 ATOM 1139 C C . VAL A 1 150 ? 20.107 16.641 48.989 1.00 20.18 ? 150 VAL A C 1 ATOM 1140 O O . VAL A 1 150 ? 21.216 16.495 49.539 1.00 19.85 ? 150 VAL A O 1 ATOM 1141 C CB . VAL A 1 150 ? 19.809 14.142 48.594 1.00 19.46 ? 150 VAL A CB 1 ATOM 1142 C CG1 . VAL A 1 150 ? 18.986 13.913 49.888 1.00 21.15 ? 150 VAL A CG1 1 ATOM 1143 C CG2 . VAL A 1 150 ? 19.528 13.069 47.526 1.00 20.65 ? 150 VAL A CG2 1 ATOM 1144 N N . CYS A 1 151 ? 19.398 17.762 49.108 1.00 20.77 ? 151 CYS A N 1 ATOM 1145 C CA . CYS A 1 151 ? 19.920 18.887 49.899 1.00 21.56 ? 151 CYS A CA 1 ATOM 1146 C C . CYS A 1 151 ? 19.818 18.584 51.382 1.00 20.99 ? 151 CYS A C 1 ATOM 1147 O O . CYS A 1 151 ? 18.720 18.365 51.903 1.00 22.05 ? 151 CYS A O 1 ATOM 1148 C CB . CYS A 1 151 ? 19.177 20.195 49.574 1.00 21.70 ? 151 CYS A CB 1 ATOM 1149 S SG . CYS A 1 151 ? 19.489 21.579 50.701 1.00 23.12 ? 151 CYS A SG 1 ATOM 1150 N N . ARG A 1 152 ? 20.973 18.558 52.045 1.00 21.68 ? 152 ARG A N 1 ATOM 1151 C CA . ARG A 1 152 ? 21.035 18.160 53.462 1.00 21.45 ? 152 ARG A CA 1 ATOM 1152 C C . ARG A 1 152 ? 21.214 19.335 54.401 1.00 21.93 ? 152 ARG A C 1 ATOM 1153 O O . ARG A 1 152 ? 21.379 19.151 55.624 1.00 22.54 ? 152 ARG A O 1 ATOM 1154 C CB . ARG A 1 152 ? 22.169 17.127 53.656 1.00 21.67 ? 152 ARG A CB 1 ATOM 1155 C CG . ARG A 1 152 ? 22.023 15.886 52.767 1.00 20.55 ? 152 ARG A CG 1 ATOM 1156 C CD . ARG A 1 152 ? 20.812 15.052 53.116 1.00 27.72 ? 152 ARG A CD 1 ATOM 1157 N NE . ARG A 1 152 ? 21.096 14.377 54.397 1.00 17.80 ? 152 ARG A NE 1 ATOM 1158 C CZ . ARG A 1 152 ? 20.235 13.634 55.118 1.00 33.00 ? 152 ARG A CZ 1 ATOM 1159 N NH1 . ARG A 1 152 ? 20.652 13.070 56.251 1.00 20.80 ? 152 ARG A NH1 1 ATOM 1160 N NH2 . ARG A 1 152 ? 18.972 13.449 54.728 1.00 22.06 ? 152 ARG A NH2 1 ATOM 1161 N N . ASP A 1 153 ? 21.198 20.542 53.838 1.00 21.81 ? 153 ASP A N 1 ATOM 1162 C CA . ASP A 1 153 ? 21.373 21.787 54.584 1.00 21.31 ? 153 ASP A CA 1 ATOM 1163 C C . ASP A 1 153 ? 20.745 22.949 53.797 1.00 21.29 ? 153 ASP A C 1 ATOM 1164 O O . ASP A 1 153 ? 21.290 23.358 52.753 1.00 20.77 ? 153 ASP A O 1 ATOM 1165 C CB . ASP A 1 153 ? 22.870 22.043 54.845 1.00 21.82 ? 153 ASP A CB 1 ATOM 1166 C CG . ASP A 1 153 ? 23.119 23.114 55.912 1.00 23.79 ? 153 ASP A CG 1 ATOM 1167 O OD1 . ASP A 1 153 ? 22.369 24.114 55.977 1.00 21.27 ? 153 ASP A OD1 1 ATOM 1168 O OD2 . ASP A 1 153 ? 24.104 22.969 56.691 1.00 25.13 ? 153 ASP A OD2 1 ATOM 1169 N N . PRO A 1 154 ? 19.628 23.510 54.317 1.00 20.53 ? 154 PRO A N 1 ATOM 1170 C CA . PRO A 1 154 ? 18.893 24.540 53.566 1.00 20.06 ? 154 PRO A CA 1 ATOM 1171 C C . PRO A 1 154 ? 19.643 25.866 53.469 1.00 19.84 ? 154 PRO A C 1 ATOM 1172 O O . PRO A 1 154 ? 19.180 26.783 52.780 1.00 20.93 ? 154 PRO A O 1 ATOM 1173 C CB . PRO A 1 154 ? 17.569 24.678 54.339 1.00 19.67 ? 154 PRO A CB 1 ATOM 1174 C CG . PRO A 1 154 ? 17.975 24.345 55.788 1.00 20.34 ? 154 PRO A CG 1 ATOM 1175 C CD . PRO A 1 154 ? 19.014 23.240 55.639 1.00 19.86 ? 154 PRO A CD 1 ATOM 1176 N N . ARG A 1 155 ? 20.810 25.979 54.117 1.00 20.55 ? 155 ARG A N 1 ATOM 1177 C CA . ARG A 1 155 ? 21.656 27.156 53.902 1.00 20.02 ? 155 ARG A CA 1 ATOM 1178 C C . ARG A 1 155 ? 22.216 27.217 52.451 1.00 19.98 ? 155 ARG A C 1 ATOM 1179 O O . ARG A 1 155 ? 22.672 28.266 51.999 1.00 21.44 ? 155 ARG A O 1 ATOM 1180 C CB . ARG A 1 155 ? 22.752 27.259 54.974 1.00 20.63 ? 155 ARG A CB 1 ATOM 1181 C CG . ARG A 1 155 ? 22.156 27.521 56.396 1.00 18.27 ? 155 ARG A CG 1 ATOM 1182 C CD . ARG A 1 155 ? 23.212 27.483 57.535 1.00 25.03 ? 155 ARG A CD 1 ATOM 1183 N NE . ARG A 1 155 ? 23.664 26.110 57.778 1.00 17.47 ? 155 ARG A NE 1 ATOM 1184 C CZ . ARG A 1 155 ? 24.626 25.785 58.650 1.00 29.52 ? 155 ARG A CZ 1 ATOM 1185 N NH1 . ARG A 1 155 ? 25.192 26.750 59.372 1.00 21.57 ? 155 ARG A NH1 1 ATOM 1186 N NH2 . ARG A 1 155 ? 24.982 24.507 58.768 1.00 21.74 ? 155 ARG A NH2 1 ATOM 1187 N N . TRP A 1 156 ? 22.142 26.094 51.744 1.00 20.57 ? 156 TRP A N 1 ATOM 1188 C CA . TRP A 1 156 ? 22.567 25.999 50.335 1.00 19.88 ? 156 TRP A CA 1 ATOM 1189 C C . TRP A 1 156 ? 21.664 26.809 49.415 1.00 20.14 ? 156 TRP A C 1 ATOM 1190 O O . TRP A 1 156 ? 20.445 26.686 49.476 1.00 19.06 ? 156 TRP A O 1 ATOM 1191 C CB . TRP A 1 156 ? 22.508 24.549 49.897 1.00 20.79 ? 156 TRP A CB 1 ATOM 1192 C CG . TRP A 1 156 ? 23.176 24.213 48.570 1.00 19.79 ? 156 TRP A CG 1 ATOM 1193 C CD1 . TRP A 1 156 ? 24.283 24.812 48.016 1.00 21.24 ? 156 TRP A CD1 1 ATOM 1194 C CD2 . TRP A 1 156 ? 22.805 23.146 47.679 1.00 21.41 ? 156 TRP A CD2 1 ATOM 1195 N NE1 . TRP A 1 156 ? 24.611 24.186 46.820 1.00 21.85 ? 156 TRP A NE1 1 ATOM 1196 C CE2 . TRP A 1 156 ? 23.731 23.158 46.596 1.00 21.79 ? 156 TRP A CE2 1 ATOM 1197 C CE3 . TRP A 1 156 ? 21.775 22.188 47.680 1.00 21.06 ? 156 TRP A CE3 1 ATOM 1198 C CZ2 . TRP A 1 156 ? 23.646 22.256 45.520 1.00 21.31 ? 156 TRP A CZ2 1 ATOM 1199 C CZ3 . TRP A 1 156 ? 21.694 21.276 46.616 1.00 21.06 ? 156 TRP A CZ3 1 ATOM 1200 C CH2 . TRP A 1 156 ? 22.632 21.318 45.546 1.00 20.48 ? 156 TRP A CH2 1 ATOM 1201 N N . GLY A 1 157 ? 22.276 27.617 48.554 1.00 20.04 ? 157 GLY A N 1 ATOM 1202 C CA . GLY A 1 157 ? 21.528 28.426 47.584 1.00 19.86 ? 157 GLY A CA 1 ATOM 1203 C C . GLY A 1 157 ? 20.744 27.635 46.548 1.00 19.68 ? 157 GLY A C 1 ATOM 1204 O O . GLY A 1 157 ? 19.918 28.213 45.840 1.00 20.41 ? 157 GLY A O 1 ATOM 1205 N N . ARG A 1 158 ? 21.024 26.340 46.418 1.00 19.34 ? 158 ARG A N 1 ATOM 1206 C CA . ARG A 1 158 ? 20.299 25.484 45.471 1.00 19.09 ? 158 ARG A CA 1 ATOM 1207 C C . ARG A 1 158 ? 19.340 24.548 46.168 1.00 19.39 ? 158 ARG A C 1 ATOM 1208 O O . ARG A 1 158 ? 18.825 23.627 45.540 1.00 19.34 ? 158 ARG A O 1 ATOM 1209 C CB . ARG A 1 158 ? 21.268 24.680 44.589 1.00 19.14 ? 158 ARG A CB 1 ATOM 1210 C CG . ARG A 1 158 ? 22.400 25.538 44.068 1.00 18.95 ? 158 ARG A CG 1 ATOM 1211 C CD . ARG A 1 158 ? 23.132 24.888 42.923 1.00 20.10 ? 158 ARG A CD 1 ATOM 1212 N NE . ARG A 1 158 ? 22.340 24.886 41.684 1.00 19.84 ? 158 ARG A NE 1 ATOM 1213 C CZ . ARG A 1 158 ? 22.852 24.626 40.480 1.00 21.97 ? 158 ARG A CZ 1 ATOM 1214 N NH1 . ARG A 1 158 ? 24.158 24.345 40.361 1.00 21.31 ? 158 ARG A NH1 1 ATOM 1215 N NH2 . ARG A 1 158 ? 22.061 24.642 39.400 1.00 19.11 ? 158 ARG A NH2 1 ATOM 1216 N N . CYS A 1 159 ? 19.051 24.796 47.454 1.00 20.80 ? 159 CYS A N 1 ATOM 1217 C CA . CYS A 1 159 ? 18.140 23.898 48.160 1.00 20.59 ? 159 CYS A CA 1 ATOM 1218 C C . CYS A 1 159 ? 16.783 23.779 47.433 1.00 19.19 ? 159 CYS A C 1 ATOM 1219 O O . CYS A 1 159 ? 16.203 22.685 47.348 1.00 18.06 ? 159 CYS A O 1 ATOM 1220 C CB . CYS A 1 159 ? 18.012 24.245 49.649 1.00 21.59 ? 159 CYS A CB 1 ATOM 1221 S SG . CYS A 1 159 ? 17.624 22.724 50.634 1.00 28.20 ? 159 CYS A SG 1 ATOM 1222 N N . TYR A 1 160 ? 16.314 24.876 46.826 1.00 17.48 ? 160 TYR A N 1 ATOM 1223 C CA . TYR A 1 160 ? 15.027 24.797 46.116 1.00 17.35 ? 160 TYR A CA 1 ATOM 1224 C C . TYR A 1 160 ? 15.036 23.889 44.870 1.00 17.21 ? 160 TYR A C 1 ATOM 1225 O O . TYR A 1 160 ? 13.966 23.450 44.397 1.00 17.75 ? 160 TYR A O 1 ATOM 1226 C CB . TYR A 1 160 ? 14.511 26.189 45.778 1.00 16.86 ? 160 TYR A CB 1 ATOM 1227 C CG . TYR A 1 160 ? 15.282 26.947 44.720 1.00 16.86 ? 160 TYR A CG 1 ATOM 1228 C CD1 . TYR A 1 160 ? 15.073 26.689 43.352 1.00 16.74 ? 160 TYR A CD1 1 ATOM 1229 C CD2 . TYR A 1 160 ? 16.154 27.973 45.075 1.00 17.19 ? 160 TYR A CD2 1 ATOM 1230 C CE1 . TYR A 1 160 ? 15.734 27.432 42.361 1.00 14.80 ? 160 TYR A CE1 1 ATOM 1231 C CE2 . TYR A 1 160 ? 16.840 28.718 44.093 1.00 17.33 ? 160 TYR A CE2 1 ATOM 1232 C CZ . TYR A 1 160 ? 16.620 28.436 42.738 1.00 16.53 ? 160 TYR A CZ 1 ATOM 1233 O OH . TYR A 1 160 ? 17.265 29.179 41.783 1.00 16.83 ? 160 TYR A OH 1 ATOM 1234 N N . GLU A 1 161 ? 16.238 23.616 44.351 1.00 17.17 ? 161 GLU A N 1 ATOM 1235 C CA . GLU A 1 161 ? 16.420 22.734 43.197 1.00 17.79 ? 161 GLU A CA 1 ATOM 1236 C C . GLU A 1 161 ? 16.411 21.240 43.574 1.00 18.17 ? 161 GLU A C 1 ATOM 1237 O O . GLU A 1 161 ? 16.419 20.357 42.696 1.00 18.24 ? 161 GLU A O 1 ATOM 1238 C CB . GLU A 1 161 ? 17.705 23.099 42.441 1.00 17.60 ? 161 GLU A CB 1 ATOM 1239 C CG . GLU A 1 161 ? 17.704 24.524 41.910 1.00 18.48 ? 161 GLU A CG 1 ATOM 1240 C CD . GLU A 1 161 ? 18.705 24.703 40.792 1.00 21.95 ? 161 GLU A CD 1 ATOM 1241 O OE1 . GLU A 1 161 ? 19.660 25.476 40.991 1.00 22.17 ? 161 GLU A OE1 1 ATOM 1242 O OE2 . GLU A 1 161 ? 18.501 24.061 39.725 1.00 23.69 ? 161 GLU A OE2 1 ATOM 1243 N N . SER A 1 162 ? 16.365 20.960 44.885 1.00 18.03 ? 162 SER A N 1 ATOM 1244 C CA . SER A 1 162 ? 16.301 19.599 45.387 1.00 17.66 ? 162 SER A CA 1 ATOM 1245 C C . SER A 1 162 ? 14.866 19.261 45.800 1.00 17.13 ? 162 SER A C 1 ATOM 1246 O O . SER A 1 162 ? 14.229 20.032 46.517 1.00 18.74 ? 162 SER A O 1 ATOM 1247 C CB . SER A 1 162 ? 17.217 19.452 46.613 1.00 17.91 ? 162 SER A CB 1 ATOM 1248 O OG . SER A 1 162 ? 17.024 18.191 47.229 1.00 19.61 ? 162 SER A OG 1 ATOM 1249 N N . TYR A 1 163 ? 14.361 18.109 45.382 1.00 17.34 ? 163 TYR A N 1 ATOM 1250 C CA . TYR A 1 163 ? 12.990 17.728 45.762 1.00 17.99 ? 163 TYR A CA 1 ATOM 1251 C C . TYR A 1 163 ? 12.850 17.498 47.267 1.00 18.54 ? 163 TYR A C 1 ATOM 1252 O O . TYR A 1 163 ? 11.764 17.679 47.807 1.00 18.79 ? 163 TYR A O 1 ATOM 1253 C CB . TYR A 1 163 ? 12.522 16.462 45.047 1.00 18.01 ? 163 TYR A CB 1 ATOM 1254 C CG . TYR A 1 163 ? 12.536 16.518 43.533 1.00 17.61 ? 163 TYR A CG 1 ATOM 1255 C CD1 . TYR A 1 163 ? 11.524 17.193 42.827 1.00 18.22 ? 163 TYR A CD1 1 ATOM 1256 C CD2 . TYR A 1 163 ? 13.534 15.841 42.807 1.00 17.55 ? 163 TYR A CD2 1 ATOM 1257 C CE1 . TYR A 1 163 ? 11.523 17.216 41.417 1.00 16.94 ? 163 TYR A CE1 1 ATOM 1258 C CE2 . TYR A 1 163 ? 13.549 15.863 41.423 1.00 17.76 ? 163 TYR A CE2 1 ATOM 1259 C CZ . TYR A 1 163 ? 12.540 16.558 40.730 1.00 17.47 ? 163 TYR A CZ 1 ATOM 1260 O OH . TYR A 1 163 ? 12.550 16.582 39.359 1.00 18.43 ? 163 TYR A OH 1 ATOM 1261 N N . SER A 1 164 ? 13.927 17.091 47.938 1.00 18.96 ? 164 SER A N 1 ATOM 1262 C CA . SER A 1 164 ? 13.810 16.691 49.362 1.00 19.43 ? 164 SER A CA 1 ATOM 1263 C C . SER A 1 164 ? 15.162 16.429 49.982 1.00 20.07 ? 164 SER A C 1 ATOM 1264 O O . SER A 1 164 ? 16.132 16.127 49.272 1.00 20.16 ? 164 SER A O 1 ATOM 1265 C CB . SER A 1 164 ? 12.980 15.407 49.453 1.00 19.39 ? 164 SER A CB 1 ATOM 1266 O OG . SER A 1 164 ? 12.738 14.997 50.808 1.00 19.91 ? 164 SER A OG 1 ATOM 1267 N N . GLU A 1 165 ? 15.204 16.501 51.315 1.00 20.05 ? 165 GLU A N 1 ATOM 1268 C CA . GLU A 1 165 ? 16.366 16.053 52.092 1.00 21.76 ? 165 GLU A CA 1 ATOM 1269 C C . GLU A 1 165 ? 16.348 14.532 52.204 1.00 21.63 ? 165 GLU A C 1 ATOM 1270 O O . GLU A 1 165 ? 17.359 13.940 52.613 1.00 21.88 ? 165 GLU A O 1 ATOM 1271 C CB . GLU A 1 165 ? 16.372 16.681 53.498 1.00 21.30 ? 165 GLU A CB 1 ATOM 1272 C CG . GLU A 1 165 ? 15.322 16.093 54.466 1.00 22.97 ? 165 GLU A CG 1 ATOM 1273 C CD . GLU A 1 165 ? 15.120 16.930 55.730 1.00 23.14 ? 165 GLU A CD 1 ATOM 1274 O OE1 . GLU A 1 165 ? 15.201 18.178 55.666 1.00 24.53 ? 165 GLU A OE1 1 ATOM 1275 O OE2 . GLU A 1 165 ? 14.849 16.325 56.799 1.00 26.53 ? 165 GLU A OE2 1 ATOM 1276 N N . ASP A 1 166 ? 15.202 13.930 51.864 1.00 22.04 ? 166 ASP A N 1 ATOM 1277 C CA . ASP A 1 166 ? 14.993 12.484 51.921 1.00 23.17 ? 166 ASP A CA 1 ATOM 1278 C C . ASP A 1 166 ? 15.220 11.884 50.533 1.00 22.59 ? 166 ASP A C 1 ATOM 1279 O O . ASP A 1 166 ? 14.427 12.099 49.605 1.00 21.86 ? 166 ASP A O 1 ATOM 1280 C CB . ASP A 1 166 ? 13.577 12.161 52.431 1.00 23.80 ? 166 ASP A CB 1 ATOM 1281 C CG . ASP A 1 166 ? 13.313 10.661 52.613 1.00 27.15 ? 166 ASP A CG 1 ATOM 1282 O OD1 . ASP A 1 166 ? 14.085 9.796 52.129 1.00 26.71 ? 166 ASP A OD1 1 ATOM 1283 O OD2 . ASP A 1 166 ? 12.271 10.342 53.257 1.00 30.05 ? 166 ASP A OD2 1 ATOM 1284 N N . ARG A 1 167 ? 16.301 11.117 50.395 1.00 22.18 ? 167 ARG A N 1 ATOM 1285 C CA . ARG A 1 167 ? 16.610 10.460 49.110 1.00 21.91 ? 167 ARG A CA 1 ATOM 1286 C C . ARG A 1 167 ? 15.460 9.643 48.509 1.00 21.65 ? 167 ARG A C 1 ATOM 1287 O O . ARG A 1 167 ? 15.321 9.547 47.289 1.00 20.75 ? 167 ARG A O 1 ATOM 1288 C CB . ARG A 1 167 ? 17.914 9.638 49.214 1.00 22.61 ? 167 ARG A CB 1 ATOM 1289 C CG . ARG A 1 167 ? 17.869 8.509 50.229 1.00 24.91 ? 167 ARG A CG 1 ATOM 1290 C CD . ARG A 1 167 ? 17.483 7.153 49.632 1.00 26.77 ? 167 ARG A CD 1 ATOM 1291 N NE . ARG A 1 167 ? 17.502 6.102 50.665 1.00 35.72 ? 167 ARG A NE 1 ATOM 1292 C CZ . ARG A 1 167 ? 16.960 4.892 50.530 1.00 27.39 ? 167 ARG A CZ 1 ATOM 1293 N NH1 . ARG A 1 167 ? 17.032 4.012 51.536 1.00 41.92 ? 167 ARG A NH1 1 ATOM 1294 N NH2 . ARG A 1 167 ? 16.358 4.547 49.396 1.00 37.93 ? 167 ARG A NH2 1 ATOM 1295 N N . ARG A 1 168 ? 14.623 9.033 49.360 1.00 21.71 ? 168 ARG A N 1 ATOM 1296 C CA . ARG A 1 168 ? 13.468 8.287 48.860 1.00 21.85 ? 168 ARG A CA 1 ATOM 1297 C C . ARG A 1 168 ? 12.507 9.161 48.047 1.00 21.30 ? 168 ARG A C 1 ATOM 1298 O O . ARG A 1 168 ? 11.943 8.722 47.024 1.00 21.57 ? 168 ARG A O 1 ATOM 1299 C CB . ARG A 1 168 ? 12.745 7.588 50.020 1.00 23.26 ? 168 ARG A CB 1 ATOM 1300 C CG . ARG A 1 168 ? 13.597 6.495 50.651 1.00 29.05 ? 168 ARG A CG 1 ATOM 1301 C CD . ARG A 1 168 ? 12.820 5.774 51.744 1.00 29.88 ? 168 ARG A CD 1 ATOM 1302 N NE . ARG A 1 168 ? 13.466 4.518 52.146 1.00 50.33 ? 168 ARG A NE 1 ATOM 1303 C CZ . ARG A 1 168 ? 14.375 4.410 53.112 1.00 35.17 ? 168 ARG A CZ 1 ATOM 1304 N NH1 . ARG A 1 168 ? 14.777 5.488 53.784 1.00 52.66 ? 168 ARG A NH1 1 ATOM 1305 N NH2 . ARG A 1 168 ? 14.884 3.217 53.405 1.00 50.92 ? 168 ARG A NH2 1 ATOM 1306 N N . ILE A 1 169 ? 12.323 10.397 48.496 1.00 20.34 ? 169 ILE A N 1 ATOM 1307 C CA . ILE A 1 169 ? 11.451 11.314 47.760 1.00 20.07 ? 169 ILE A CA 1 ATOM 1308 C C . ILE A 1 169 ? 12.129 11.703 46.427 1.00 19.57 ? 169 ILE A C 1 ATOM 1309 O O . ILE A 1 169 ? 11.500 11.683 45.365 1.00 18.81 ? 169 ILE A O 1 ATOM 1310 C CB . ILE A 1 169 ? 11.040 12.529 48.617 1.00 19.86 ? 169 ILE A CB 1 ATOM 1311 C CG1 . ILE A 1 169 ? 10.167 12.045 49.789 1.00 20.84 ? 169 ILE A CG1 1 ATOM 1312 C CG2 . ILE A 1 169 ? 10.262 13.551 47.774 1.00 20.07 ? 169 ILE A CG2 1 ATOM 1313 C CD1 . ILE A 1 169 ? 9.871 13.147 50.815 1.00 21.03 ? 169 ILE A CD1 1 ATOM 1314 N N . VAL A 1 170 ? 13.419 12.010 46.500 1.00 19.60 ? 170 VAL A N 1 ATOM 1315 C CA . VAL A 1 170 ? 14.185 12.343 45.279 1.00 19.07 ? 170 VAL A CA 1 ATOM 1316 C C . VAL A 1 170 ? 14.115 11.182 44.272 1.00 20.07 ? 170 VAL A C 1 ATOM 1317 O O . VAL A 1 170 ? 13.849 11.393 43.076 1.00 19.58 ? 170 VAL A O 1 ATOM 1318 C CB . VAL A 1 170 ? 15.651 12.740 45.587 1.00 19.30 ? 170 VAL A CB 1 ATOM 1319 C CG1 . VAL A 1 170 ? 16.436 13.008 44.269 1.00 18.06 ? 170 VAL A CG1 1 ATOM 1320 C CG2 . VAL A 1 170 ? 15.694 13.972 46.489 1.00 18.77 ? 170 VAL A CG2 1 ATOM 1321 N N . GLN A 1 171 ? 14.326 9.953 44.759 1.00 20.24 ? 171 GLN A N 1 ATOM 1322 C CA . GLN A 1 171 ? 14.204 8.770 43.896 1.00 21.06 ? 171 GLN A CA 1 ATOM 1323 C C . GLN A 1 171 ? 12.840 8.719 43.220 1.00 20.73 ? 171 GLN A C 1 ATOM 1324 O O . GLN A 1 171 ? 12.749 8.476 42.021 1.00 21.06 ? 171 GLN A O 1 ATOM 1325 C CB . GLN A 1 171 ? 14.428 7.475 44.695 1.00 20.88 ? 171 GLN A CB 1 ATOM 1326 C CG . GLN A 1 171 ? 15.864 7.224 45.108 1.00 22.33 ? 171 GLN A CG 1 ATOM 1327 C CD . GLN A 1 171 ? 15.989 5.926 45.886 1.00 22.89 ? 171 GLN A CD 1 ATOM 1328 O OE1 . GLN A 1 171 ? 16.342 4.868 45.330 1.00 27.05 ? 171 GLN A OE1 1 ATOM 1329 N NE2 . GLN A 1 171 ? 15.658 5.986 47.158 1.00 22.23 ? 171 GLN A NE2 1 ATOM 1330 N N . SER A 1 172 ? 11.766 8.926 43.985 1.00 21.09 ? 172 SER A N 1 ATOM 1331 C CA . SER A 1 172 ? 10.437 8.878 43.389 1.00 21.38 ? 172 SER A CA 1 ATOM 1332 C C . SER A 1 172 ? 10.256 9.909 42.263 1.00 21.14 ? 172 SER A C 1 ATOM 1333 O O . SER A 1 172 ? 9.535 9.647 41.301 1.00 22.23 ? 172 SER A O 1 ATOM 1334 C CB . SER A 1 172 ? 9.329 9.037 44.444 1.00 22.38 ? 172 SER A CB 1 ATOM 1335 O OG . SER A 1 172 ? 9.243 10.354 44.927 1.00 24.12 ? 172 SER A OG 1 ATOM 1336 N N . MET A 1 173 ? 10.904 11.067 42.401 1.00 20.66 ? 173 MET A N 1 ATOM 1337 C CA . MET A 1 173 ? 10.693 12.195 41.466 1.00 20.78 ? 173 MET A CA 1 ATOM 1338 C C . MET A 1 173 ? 11.549 12.097 40.203 1.00 20.78 ? 173 MET A C 1 ATOM 1339 O O . MET A 1 173 ? 11.433 12.944 39.282 1.00 20.45 ? 173 MET A O 1 ATOM 1340 C CB . MET A 1 173 ? 10.911 13.552 42.165 1.00 22.12 ? 173 MET A CB 1 ATOM 1341 C CG . MET A 1 173 ? 9.987 13.785 43.363 1.00 24.68 ? 173 MET A CG 1 ATOM 1342 S SD . MET A 1 173 ? 8.282 13.666 42.829 1.00 28.56 ? 173 MET A SD 1 ATOM 1343 C CE . MET A 1 173 ? 7.379 13.913 44.367 1.00 26.10 ? 173 MET A CE 1 ATOM 1344 N N . THR A 1 174 ? 12.391 11.066 40.150 1.00 20.29 ? 174 THR A N 1 ATOM 1345 C CA . THR A 1 174 ? 13.091 10.727 38.894 1.00 19.98 ? 174 THR A CA 1 ATOM 1346 C C . THR A 1 174 ? 12.136 10.422 37.732 1.00 19.90 ? 174 THR A C 1 ATOM 1347 O O . THR A 1 174 ? 12.573 10.306 36.587 1.00 19.64 ? 174 THR A O 1 ATOM 1348 C CB . THR A 1 174 ? 14.132 9.587 39.049 1.00 20.20 ? 174 THR A CB 1 ATOM 1349 O OG1 . THR A 1 174 ? 13.479 8.368 39.461 1.00 21.13 ? 174 THR A OG1 1 ATOM 1350 C CG2 . THR A 1 174 ? 15.247 10.002 39.989 1.00 20.50 ? 174 THR A CG2 1 ATOM 1351 N N . GLU A 1 175 ? 10.837 10.279 38.033 1.00 20.05 ? 175 GLU A N 1 ATOM 1352 C CA . GLU A 1 175 ? 9.797 10.228 36.996 1.00 20.09 ? 175 GLU A CA 1 ATOM 1353 C C . GLU A 1 175 ? 9.843 11.422 36.033 1.00 18.97 ? 175 GLU A C 1 ATOM 1354 O O . GLU A 1 175 ? 9.261 11.359 34.946 1.00 19.60 ? 175 GLU A O 1 ATOM 1355 C CB . GLU A 1 175 ? 8.393 10.106 37.618 1.00 20.54 ? 175 GLU A CB 1 ATOM 1356 C CG . GLU A 1 175 ? 8.126 8.706 38.146 1.00 23.84 ? 175 GLU A CG 1 ATOM 1357 C CD . GLU A 1 175 ? 8.144 7.671 37.026 1.00 25.27 ? 175 GLU A CD 1 ATOM 1358 O OE1 . GLU A 1 175 ? 9.176 7.002 36.878 1.00 27.30 ? 175 GLU A OE1 1 ATOM 1359 O OE2 . GLU A 1 175 ? 7.153 7.552 36.269 1.00 28.65 ? 175 GLU A OE2 1 ATOM 1360 N N . LEU A 1 176 ? 10.486 12.515 36.434 1.00 17.93 ? 176 LEU A N 1 ATOM 1361 C CA . LEU A 1 176 ? 10.654 13.640 35.482 1.00 17.16 ? 176 LEU A CA 1 ATOM 1362 C C . LEU A 1 176 ? 11.296 13.127 34.195 1.00 17.34 ? 176 LEU A C 1 ATOM 1363 O O . LEU A 1 176 ? 10.963 13.594 33.107 1.00 17.61 ? 176 LEU A O 1 ATOM 1364 C CB . LEU A 1 176 ? 11.509 14.767 36.065 1.00 16.24 ? 176 LEU A CB 1 ATOM 1365 C CG . LEU A 1 176 ? 11.486 16.032 35.175 1.00 16.76 ? 176 LEU A CG 1 ATOM 1366 C CD1 . LEU A 1 176 ? 10.183 16.825 35.422 1.00 18.44 ? 176 LEU A CD1 1 ATOM 1367 C CD2 . LEU A 1 176 ? 12.697 16.904 35.406 1.00 18.32 ? 176 LEU A CD2 1 ATOM 1368 N N . ILE A 1 177 ? 12.216 12.173 34.349 1.00 16.73 ? 177 ILE A N 1 ATOM 1369 C CA . ILE A 1 177 ? 13.073 11.693 33.227 1.00 17.23 ? 177 ILE A CA 1 ATOM 1370 C C . ILE A 1 177 ? 12.241 11.085 32.075 1.00 17.88 ? 177 ILE A C 1 ATOM 1371 O O . ILE A 1 177 ? 12.322 11.564 30.949 1.00 17.87 ? 177 ILE A O 1 ATOM 1372 C CB . ILE A 1 177 ? 14.208 10.778 33.744 1.00 16.53 ? 177 ILE A CB 1 ATOM 1373 C CG1 . ILE A 1 177 ? 15.213 11.618 34.566 1.00 18.31 ? 177 ILE A CG1 1 ATOM 1374 C CG2 . ILE A 1 177 ? 14.916 10.089 32.576 1.00 17.45 ? 177 ILE A CG2 1 ATOM 1375 C CD1 . ILE A 1 177 ? 16.164 10.801 35.445 1.00 18.54 ? 177 ILE A CD1 1 ATOM 1376 N N . PRO A 1 178 ? 11.412 10.043 32.350 1.00 18.57 ? 178 PRO A N 1 ATOM 1377 C CA . PRO A 1 178 ? 10.547 9.545 31.272 1.00 18.82 ? 178 PRO A CA 1 ATOM 1378 C C . PRO A 1 178 ? 9.486 10.531 30.809 1.00 18.78 ? 178 PRO A C 1 ATOM 1379 O O . PRO A 1 178 ? 8.954 10.385 29.709 1.00 18.98 ? 178 PRO A O 1 ATOM 1380 C CB . PRO A 1 178 ? 9.907 8.282 31.873 1.00 19.78 ? 178 PRO A CB 1 ATOM 1381 C CG . PRO A 1 178 ? 9.993 8.475 33.354 1.00 18.98 ? 178 PRO A CG 1 ATOM 1382 C CD . PRO A 1 178 ? 11.275 9.238 33.579 1.00 19.02 ? 178 PRO A CD 1 ATOM 1383 N N . GLY A 1 179 ? 9.175 11.538 31.631 1.00 18.25 ? 179 GLY A N 1 ATOM 1384 C CA . GLY A 1 179 ? 8.330 12.636 31.159 1.00 17.97 ? 179 GLY A CA 1 ATOM 1385 C C . GLY A 1 179 ? 9.040 13.424 30.053 1.00 17.65 ? 179 GLY A C 1 ATOM 1386 O O . GLY A 1 179 ? 8.475 13.651 28.970 1.00 17.96 ? 179 GLY A O 1 ATOM 1387 N N . LEU A 1 180 ? 10.271 13.846 30.334 1.00 16.75 ? 180 LEU A N 1 ATOM 1388 C CA . LEU A 1 180 ? 11.057 14.637 29.366 1.00 15.87 ? 180 LEU A CA 1 ATOM 1389 C C . LEU A 1 180 ? 11.432 13.831 28.115 1.00 16.44 ? 180 LEU A C 1 ATOM 1390 O O . LEU A 1 180 ? 11.380 14.356 26.990 1.00 16.64 ? 180 LEU A O 1 ATOM 1391 C CB . LEU A 1 180 ? 12.358 15.114 30.009 1.00 15.79 ? 180 LEU A CB 1 ATOM 1392 C CG . LEU A 1 180 ? 12.244 16.226 31.064 1.00 15.38 ? 180 LEU A CG 1 ATOM 1393 C CD1 . LEU A 1 180 ? 13.540 16.365 31.861 1.00 17.51 ? 180 LEU A CD1 1 ATOM 1394 C CD2 . LEU A 1 180 ? 11.848 17.570 30.434 1.00 16.61 ? 180 LEU A CD2 1 ATOM 1395 N N . GLN A 1 181 ? 11.833 12.578 28.330 1.00 16.45 ? 181 GLN A N 1 ATOM 1396 C CA . GLN A 1 181 ? 12.438 11.735 27.269 1.00 17.54 ? 181 GLN A CA 1 ATOM 1397 C C . GLN A 1 181 ? 11.473 10.762 26.600 1.00 18.93 ? 181 GLN A C 1 ATOM 1398 O O . GLN A 1 181 ? 11.743 10.286 25.480 1.00 19.62 ? 181 GLN A O 1 ATOM 1399 C CB . GLN A 1 181 ? 13.587 10.897 27.846 1.00 17.25 ? 181 GLN A CB 1 ATOM 1400 C CG . GLN A 1 181 ? 14.732 11.708 28.461 1.00 17.33 ? 181 GLN A CG 1 ATOM 1401 C CD . GLN A 1 181 ? 15.939 10.843 28.761 1.00 18.05 ? 181 GLN A CD 1 ATOM 1402 O OE1 . GLN A 1 181 ? 15.815 9.670 29.185 1.00 19.24 ? 181 GLN A OE1 1 ATOM 1403 N NE2 . GLN A 1 181 ? 17.110 11.399 28.547 1.00 13.45 ? 181 GLN A NE2 1 ATOM 1404 N N . GLY A 1 182 ? 10.377 10.428 27.287 1.00 19.59 ? 182 GLY A N 1 ATOM 1405 C CA . GLY A 1 182 ? 9.533 9.285 26.881 1.00 21.12 ? 182 GLY A CA 1 ATOM 1406 C C . GLY A 1 182 ? 9.836 8.044 27.707 1.00 21.89 ? 182 GLY A C 1 ATOM 1407 O O . GLY A 1 182 ? 10.925 7.884 28.255 1.00 21.95 ? 182 GLY A O 1 ATOM 1408 N N . ASP A 1 183 ? 8.849 7.160 27.835 1.00 23.62 ? 183 ASP A N 1 ATOM 1409 C CA . ASP A 1 183 ? 9.049 5.925 28.587 1.00 25.39 ? 183 ASP A CA 1 ATOM 1410 C C . ASP A 1 183 ? 9.955 4.966 27.823 1.00 26.12 ? 183 ASP A C 1 ATOM 1411 O O . ASP A 1 183 ? 9.864 4.877 26.610 1.00 26.43 ? 183 ASP A O 1 ATOM 1412 C CB . ASP A 1 183 ? 7.705 5.239 28.845 1.00 26.57 ? 183 ASP A CB 1 ATOM 1413 C CG . ASP A 1 183 ? 6.886 5.950 29.899 1.00 28.83 ? 183 ASP A CG 1 ATOM 1414 O OD1 . ASP A 1 183 ? 7.431 6.253 30.979 1.00 31.30 ? 183 ASP A OD1 1 ATOM 1415 O OD2 . ASP A 1 183 ? 5.689 6.185 29.652 1.00 33.49 ? 183 ASP A OD2 1 ATOM 1416 N N . VAL A 1 184 ? 10.818 4.265 28.543 1.00 27.79 ? 184 VAL A N 1 ATOM 1417 C CA . VAL A 1 184 ? 11.719 3.299 27.917 1.00 30.03 ? 184 VAL A CA 1 ATOM 1418 C C . VAL A 1 184 ? 10.942 2.027 27.536 1.00 32.53 ? 184 VAL A C 1 ATOM 1419 O O . VAL A 1 184 ? 9.896 1.743 28.136 1.00 32.57 ? 184 VAL A O 1 ATOM 1420 C CB . VAL A 1 184 ? 12.946 2.967 28.812 1.00 29.66 ? 184 VAL A CB 1 ATOM 1421 C CG1 . VAL A 1 184 ? 13.737 4.249 29.128 1.00 29.50 ? 184 VAL A CG1 1 ATOM 1422 C CG2 . VAL A 1 184 ? 12.529 2.224 30.101 1.00 29.90 ? 184 VAL A CG2 1 ATOM 1423 N N . PRO A 1 185 ? 11.419 1.293 26.511 1.00 35.03 ? 185 PRO A N 1 ATOM 1424 C CA . PRO A 1 185 ? 10.801 0.020 26.102 1.00 36.95 ? 185 PRO A CA 1 ATOM 1425 C C . PRO A 1 185 ? 10.839 -1.061 27.184 1.00 38.52 ? 185 PRO A C 1 ATOM 1426 O O . PRO A 1 185 ? 11.623 -0.968 28.134 1.00 38.44 ? 185 PRO A O 1 ATOM 1427 C CB . PRO A 1 185 ? 11.662 -0.415 24.914 1.00 37.26 ? 185 PRO A CB 1 ATOM 1428 C CG . PRO A 1 185 ? 12.277 0.817 24.410 1.00 36.72 ? 185 PRO A CG 1 ATOM 1429 C CD . PRO A 1 185 ? 12.544 1.649 25.628 1.00 35.35 ? 185 PRO A CD 1 ATOM 1430 N N . LYS A 1 186 ? 9.993 -2.085 27.036 1.00 40.62 ? 186 LYS A N 1 ATOM 1431 C CA . LYS A 1 186 ? 9.985 -3.217 27.977 1.00 42.35 ? 186 LYS A CA 1 ATOM 1432 C C . LYS A 1 186 ? 11.343 -3.928 28.029 1.00 42.41 ? 186 LYS A C 1 ATOM 1433 O O . LYS A 1 186 ? 11.775 -4.386 29.089 1.00 43.08 ? 186 LYS A O 1 ATOM 1434 C CB . LYS A 1 186 ? 8.855 -4.211 27.646 1.00 42.60 ? 186 LYS A CB 1 ATOM 1435 C CG . LYS A 1 186 ? 8.815 -5.448 28.561 1.00 44.24 ? 186 LYS A CG 1 ATOM 1436 C CD . LYS A 1 186 ? 7.400 -5.778 29.048 1.00 55.33 ? 186 LYS A CD 1 ATOM 1437 C CE . LYS A 1 186 ? 6.951 -4.812 30.150 1.00 40.67 ? 186 LYS A CE 1 ATOM 1438 N NZ . LYS A 1 186 ? 5.725 -5.303 30.850 1.00 58.96 ? 186 LYS A NZ 1 ATOM 1439 N N . ASP A 1 187 ? 12.017 -3.991 26.885 1.00 42.55 ? 187 ASP A N 1 ATOM 1440 C CA . ASP A 1 187 ? 13.323 -4.658 26.777 1.00 42.88 ? 187 ASP A CA 1 ATOM 1441 C C . ASP A 1 187 ? 14.472 -3.968 27.540 1.00 41.34 ? 187 ASP A C 1 ATOM 1442 O O . ASP A 1 187 ? 15.528 -4.562 27.747 1.00 42.01 ? 187 ASP A O 1 ATOM 1443 C CB . ASP A 1 187 ? 13.714 -4.800 25.297 1.00 43.74 ? 187 ASP A CB 1 ATOM 1444 C CG . ASP A 1 187 ? 13.203 -3.646 24.443 1.00 46.55 ? 187 ASP A CG 1 ATOM 1445 O OD1 . ASP A 1 187 ? 14.000 -2.722 24.127 1.00 48.93 ? 187 ASP A OD1 1 ATOM 1446 O OD2 . ASP A 1 187 ? 11.994 -3.660 24.102 1.00 49.41 ? 187 ASP A OD2 1 ATOM 1447 N N . PHE A 1 188 ? 14.239 -2.738 27.988 1.00 39.34 ? 188 PHE A N 1 ATOM 1448 C CA . PHE A 1 188 ? 15.313 -1.781 28.263 1.00 36.66 ? 188 PHE A CA 1 ATOM 1449 C C . PHE A 1 188 ? 16.418 -2.175 29.249 1.00 35.20 ? 188 PHE A C 1 ATOM 1450 O O . PHE A 1 188 ? 16.141 -2.620 30.370 1.00 35.26 ? 188 PHE A O 1 ATOM 1451 C CB . PHE A 1 188 ? 14.712 -0.436 28.683 1.00 36.46 ? 188 PHE A CB 1 ATOM 1452 C CG . PHE A 1 188 ? 15.653 0.710 28.511 1.00 35.77 ? 188 PHE A CG 1 ATOM 1453 C CD1 . PHE A 1 188 ? 15.910 1.218 27.241 1.00 35.66 ? 188 PHE A CD1 1 ATOM 1454 C CD2 . PHE A 1 188 ? 16.300 1.265 29.607 1.00 35.33 ? 188 PHE A CD2 1 ATOM 1455 C CE1 . PHE A 1 188 ? 16.786 2.273 27.066 1.00 34.89 ? 188 PHE A CE1 1 ATOM 1456 C CE2 . PHE A 1 188 ? 17.193 2.325 29.435 1.00 34.69 ? 188 PHE A CE2 1 ATOM 1457 C CZ . PHE A 1 188 ? 17.418 2.826 28.167 1.00 34.77 ? 188 PHE A CZ 1 ATOM 1458 N N . THR A 1 189 ? 17.671 -1.969 28.829 1.00 32.61 ? 189 THR A N 1 ATOM 1459 C CA . THR A 1 189 ? 18.833 -2.212 29.683 1.00 31.00 ? 189 THR A CA 1 ATOM 1460 C C . THR A 1 189 ? 19.224 -0.963 30.483 1.00 29.44 ? 189 THR A C 1 ATOM 1461 O O . THR A 1 189 ? 19.593 0.055 29.896 1.00 28.19 ? 189 THR A O 1 ATOM 1462 C CB . THR A 1 189 ? 20.060 -2.680 28.856 1.00 31.35 ? 189 THR A CB 1 ATOM 1463 O OG1 . THR A 1 189 ? 19.710 -3.847 28.100 1.00 32.66 ? 189 THR A OG1 1 ATOM 1464 C CG2 . THR A 1 189 ? 21.246 -2.988 29.767 1.00 31.34 ? 189 THR A CG2 1 ATOM 1465 N N . SER A 1 190 ? 19.164 -1.065 31.812 1.00 27.63 ? 190 SER A N 1 ATOM 1466 C CA . SER A 1 190 ? 19.549 0.034 32.700 1.00 26.46 ? 190 SER A CA 1 ATOM 1467 C C . SER A 1 190 ? 20.908 0.644 32.330 1.00 26.05 ? 190 SER A C 1 ATOM 1468 O O . SER A 1 190 ? 21.903 -0.078 32.154 1.00 25.79 ? 190 SER A O 1 ATOM 1469 C CB . SER A 1 190 ? 19.573 -0.430 34.157 1.00 26.79 ? 190 SER A CB 1 ATOM 1470 O OG . SER A 1 190 ? 19.951 0.628 35.025 1.00 24.66 ? 190 SER A OG 1 ATOM 1471 N N . GLY A 1 191 ? 20.937 1.970 32.204 1.00 24.80 ? 191 GLY A N 1 ATOM 1472 C CA . GLY A 1 191 ? 22.180 2.682 31.884 1.00 24.09 ? 191 GLY A CA 1 ATOM 1473 C C . GLY A 1 191 ? 22.270 3.122 30.435 1.00 23.53 ? 191 GLY A C 1 ATOM 1474 O O . GLY A 1 191 ? 23.050 4.010 30.111 1.00 22.64 ? 191 GLY A O 1 ATOM 1475 N N . MET A 1 192 ? 21.472 2.511 29.564 1.00 23.32 ? 192 MET A N 1 ATOM 1476 C CA . MET A 1 192 ? 21.398 2.957 28.169 1.00 23.18 ? 192 MET A CA 1 ATOM 1477 C C . MET A 1 192 ? 20.675 4.297 28.064 1.00 22.52 ? 192 MET A C 1 ATOM 1478 O O . MET A 1 192 ? 19.735 4.544 28.820 1.00 22.57 ? 192 MET A O 1 ATOM 1479 C CB . MET A 1 192 ? 20.719 1.906 27.290 1.00 23.91 ? 192 MET A CB 1 ATOM 1480 C CG . MET A 1 192 ? 21.617 0.674 27.040 1.00 25.46 ? 192 MET A CG 1 ATOM 1481 S SD . MET A 1 192 ? 23.042 1.082 25.971 1.00 30.38 ? 192 MET A SD 1 ATOM 1482 C CE . MET A 1 192 ? 22.232 1.175 24.372 1.00 28.66 ? 192 MET A CE 1 ATOM 1483 N N . PRO A 1 193 ? 21.114 5.176 27.140 1.00 21.91 ? 193 PRO A N 1 ATOM 1484 C CA . PRO A 1 193 ? 20.371 6.430 26.940 1.00 21.11 ? 193 PRO A CA 1 ATOM 1485 C C . PRO A 1 193 ? 19.079 6.179 26.140 1.00 21.22 ? 193 PRO A C 1 ATOM 1486 O O . PRO A 1 193 ? 18.993 5.215 25.364 1.00 21.91 ? 193 PRO A O 1 ATOM 1487 C CB . PRO A 1 193 ? 21.349 7.285 26.122 1.00 20.81 ? 193 PRO A CB 1 ATOM 1488 C CG . PRO A 1 193 ? 22.121 6.239 25.298 1.00 20.25 ? 193 PRO A CG 1 ATOM 1489 C CD . PRO A 1 193 ? 22.303 5.075 26.253 1.00 22.06 ? 193 PRO A CD 1 ATOM 1490 N N . PHE A 1 194 ? 18.085 7.041 26.319 1.00 20.98 ? 194 PHE A N 1 ATOM 1491 C CA . PHE A 1 194 ? 16.836 6.914 25.595 1.00 21.01 ? 194 PHE A CA 1 ATOM 1492 C C . PHE A 1 194 ? 16.188 8.286 25.411 1.00 20.43 ? 194 PHE A C 1 ATOM 1493 O O . PHE A 1 194 ? 16.135 9.074 26.363 1.00 19.85 ? 194 PHE A O 1 ATOM 1494 C CB . PHE A 1 194 ? 15.838 5.995 26.339 1.00 21.72 ? 194 PHE A CB 1 ATOM 1495 C CG . PHE A 1 194 ? 14.544 5.832 25.613 1.00 22.58 ? 194 PHE A CG 1 ATOM 1496 C CD1 . PHE A 1 194 ? 14.438 4.930 24.544 1.00 24.03 ? 194 PHE A CD1 1 ATOM 1497 C CD2 . PHE A 1 194 ? 13.443 6.634 25.935 1.00 23.18 ? 194 PHE A CD2 1 ATOM 1498 C CE1 . PHE A 1 194 ? 13.230 4.809 23.830 1.00 25.05 ? 194 PHE A CE1 1 ATOM 1499 C CE2 . PHE A 1 194 ? 12.231 6.525 25.228 1.00 23.28 ? 194 PHE A CE2 1 ATOM 1500 C CZ . PHE A 1 194 ? 12.124 5.615 24.179 1.00 23.90 ? 194 PHE A CZ 1 ATOM 1501 N N . VAL A 1 195 ? 15.718 8.557 24.194 1.00 19.61 ? 195 VAL A N 1 ATOM 1502 C CA . VAL A 1 195 ? 14.794 9.661 23.901 1.00 19.68 ? 195 VAL A CA 1 ATOM 1503 C C . VAL A 1 195 ? 13.851 9.149 22.809 1.00 20.29 ? 195 VAL A C 1 ATOM 1504 O O . VAL A 1 195 ? 14.308 8.573 21.797 1.00 20.36 ? 195 VAL A O 1 ATOM 1505 C CB . VAL A 1 195 ? 15.512 10.957 23.401 1.00 19.27 ? 195 VAL A CB 1 ATOM 1506 C CG1 . VAL A 1 195 ? 14.488 12.056 23.098 1.00 20.63 ? 195 VAL A CG1 1 ATOM 1507 C CG2 . VAL A 1 195 ? 16.541 11.468 24.399 1.00 19.21 ? 195 VAL A CG2 1 ATOM 1508 N N . ALA A 1 196 ? 12.549 9.339 23.002 1.00 20.26 ? 196 ALA A N 1 ATOM 1509 C CA . ALA A 1 196 ? 11.559 8.716 22.110 1.00 21.63 ? 196 ALA A CA 1 ATOM 1510 C C . ALA A 1 196 ? 11.550 9.237 20.668 1.00 23.02 ? 196 ALA A C 1 ATOM 1511 O O . ALA A 1 196 ? 11.157 8.511 19.731 1.00 24.98 ? 196 ALA A O 1 ATOM 1512 C CB . ALA A 1 196 ? 10.145 8.748 22.735 1.00 21.79 ? 196 ALA A CB 1 ATOM 1513 N N . GLY A 1 197 ? 11.992 10.469 20.474 1.00 22.79 ? 197 GLY A N 1 ATOM 1514 C CA . GLY A 1 197 ? 11.896 11.111 19.167 1.00 22.58 ? 197 GLY A CA 1 ATOM 1515 C C . GLY A 1 197 ? 11.801 12.624 19.266 1.00 22.58 ? 197 GLY A C 1 ATOM 1516 O O . GLY A 1 197 ? 12.150 13.236 20.312 1.00 22.29 ? 197 GLY A O 1 ATOM 1517 N N . LYS A 1 198 ? 11.323 13.230 18.182 1.00 22.46 ? 198 LYS A N 1 ATOM 1518 C CA . LYS A 1 198 ? 11.459 14.671 17.971 1.00 22.62 ? 198 LYS A CA 1 ATOM 1519 C C . LYS A 1 198 ? 10.543 15.516 18.857 1.00 22.43 ? 198 LYS A C 1 ATOM 1520 O O . LYS A 1 198 ? 10.725 16.733 18.953 1.00 22.89 ? 198 LYS A O 1 ATOM 1521 C CB . LYS A 1 198 ? 11.229 15.016 16.494 1.00 22.49 ? 198 LYS A CB 1 ATOM 1522 C CG . LYS A 1 198 ? 9.796 14.734 16.002 1.00 23.47 ? 198 LYS A CG 1 ATOM 1523 C CD . LYS A 1 198 ? 9.628 15.140 14.551 1.00 24.67 ? 198 LYS A CD 1 ATOM 1524 C CE . LYS A 1 198 ? 8.147 15.152 14.215 1.00 29.48 ? 198 LYS A CE 1 ATOM 1525 N NZ . LYS A 1 198 ? 7.892 15.020 12.755 1.00 33.47 ? 198 LYS A NZ 1 ATOM 1526 N N . ASN A 1 199 ? 9.581 14.873 19.519 1.00 21.89 ? 199 ASN A N 1 ATOM 1527 C CA . ASN A 1 199 ? 8.702 15.591 20.438 1.00 22.10 ? 199 ASN A CA 1 ATOM 1528 C C . ASN A 1 199 ? 9.161 15.472 21.900 1.00 21.41 ? 199 ASN A C 1 ATOM 1529 O O . ASN A 1 199 ? 8.489 15.964 22.817 1.00 21.51 ? 199 ASN A O 1 ATOM 1530 C CB . ASN A 1 199 ? 7.247 15.125 20.264 1.00 23.14 ? 199 ASN A CB 1 ATOM 1531 C CG . ASN A 1 199 ? 6.718 15.366 18.847 1.00 26.57 ? 199 ASN A CG 1 ATOM 1532 O OD1 . ASN A 1 199 ? 6.161 14.454 18.230 1.00 33.28 ? 199 ASN A OD1 1 ATOM 1533 N ND2 . ASN A 1 199 ? 6.896 16.573 18.329 1.00 26.87 ? 199 ASN A ND2 1 ATOM 1534 N N . LYS A 1 200 ? 10.306 14.823 22.103 1.00 20.02 ? 200 LYS A N 1 ATOM 1535 C CA . LYS A 1 200 ? 10.886 14.658 23.438 1.00 19.11 ? 200 LYS A CA 1 ATOM 1536 C C . LYS A 1 200 ? 12.285 15.288 23.458 1.00 18.35 ? 200 LYS A C 1 ATOM 1537 O O . LYS A 1 200 ? 12.805 15.702 22.405 1.00 18.07 ? 200 LYS A O 1 ATOM 1538 C CB . LYS A 1 200 ? 10.943 13.175 23.826 1.00 19.66 ? 200 LYS A CB 1 ATOM 1539 C CG . LYS A 1 200 ? 9.549 12.505 24.040 1.00 19.88 ? 200 LYS A CG 1 ATOM 1540 C CD . LYS A 1 200 ? 8.778 13.150 25.205 1.00 21.44 ? 200 LYS A CD 1 ATOM 1541 C CE . LYS A 1 200 ? 7.514 12.373 25.475 1.00 22.46 ? 200 LYS A CE 1 ATOM 1542 N NZ . LYS A 1 200 ? 6.808 12.938 26.682 1.00 20.21 ? 200 LYS A NZ 1 ATOM 1543 N N . VAL A 1 201 ? 12.877 15.383 24.640 1.00 17.37 ? 201 VAL A N 1 ATOM 1544 C CA . VAL A 1 201 ? 14.215 15.958 24.773 1.00 16.69 ? 201 VAL A CA 1 ATOM 1545 C C . VAL A 1 201 ? 15.136 15.014 25.543 1.00 16.83 ? 201 VAL A C 1 ATOM 1546 O O . VAL A 1 201 ? 14.668 14.166 26.322 1.00 17.40 ? 201 VAL A O 1 ATOM 1547 C CB . VAL A 1 201 ? 14.190 17.367 25.458 1.00 16.30 ? 201 VAL A CB 1 ATOM 1548 C CG1 . VAL A 1 201 ? 13.349 18.365 24.648 1.00 16.58 ? 201 VAL A CG1 1 ATOM 1549 C CG2 . VAL A 1 201 ? 13.697 17.254 26.923 1.00 17.19 ? 201 VAL A CG2 1 ATOM 1550 N N . ALA A 1 202 ? 16.442 15.130 25.297 1.00 16.68 ? 202 ALA A N 1 ATOM 1551 C CA . ALA A 1 202 ? 17.431 14.489 26.159 1.00 16.30 ? 202 ALA A CA 1 ATOM 1552 C C . ALA A 1 202 ? 17.388 15.137 27.550 1.00 16.61 ? 202 ALA A C 1 ATOM 1553 O O . ALA A 1 202 ? 17.273 16.348 27.662 1.00 16.97 ? 202 ALA A O 1 ATOM 1554 C CB . ALA A 1 202 ? 18.846 14.618 25.561 1.00 16.33 ? 202 ALA A CB 1 ATOM 1555 N N . ALA A 1 203 ? 17.456 14.308 28.593 1.00 16.22 ? 203 ALA A N 1 ATOM 1556 C CA . ALA A 1 203 ? 17.510 14.764 29.974 1.00 16.21 ? 203 ALA A CA 1 ATOM 1557 C C . ALA A 1 203 ? 18.926 14.648 30.531 1.00 17.23 ? 203 ALA A C 1 ATOM 1558 O O . ALA A 1 203 ? 19.840 14.118 29.865 1.00 18.05 ? 203 ALA A O 1 ATOM 1559 C CB . ALA A 1 203 ? 16.499 13.964 30.847 1.00 16.02 ? 203 ALA A CB 1 ATOM 1560 N N . CYS A 1 204 ? 19.095 15.133 31.757 1.00 17.17 ? 204 CYS A N 1 ATOM 1561 C CA . CYS A 1 204 ? 20.405 15.211 32.394 1.00 17.20 ? 204 CYS A CA 1 ATOM 1562 C C . CYS A 1 204 ? 20.249 15.088 33.901 1.00 17.80 ? 204 CYS A C 1 ATOM 1563 O O . CYS A 1 204 ? 19.738 16.005 34.543 1.00 17.99 ? 204 CYS A O 1 ATOM 1564 C CB . CYS A 1 204 ? 21.056 16.565 32.082 1.00 17.16 ? 204 CYS A CB 1 ATOM 1565 S SG . CYS A 1 204 ? 22.678 16.800 32.822 1.00 18.31 ? 204 CYS A SG 1 ATOM 1566 N N . ALA A 1 205 ? 20.683 13.960 34.457 1.00 17.19 ? 205 ALA A N 1 ATOM 1567 C CA . ALA A 1 205 ? 20.692 13.816 35.910 1.00 17.24 ? 205 ALA A CA 1 ATOM 1568 C C . ALA A 1 205 ? 21.898 14.593 36.443 1.00 17.62 ? 205 ALA A C 1 ATOM 1569 O O . ALA A 1 205 ? 23.043 14.349 36.019 1.00 18.08 ? 205 ALA A O 1 ATOM 1570 C CB . ALA A 1 205 ? 20.786 12.324 36.281 1.00 16.71 ? 205 ALA A CB 1 ATOM 1571 N N . LYS A 1 206 ? 21.659 15.519 37.375 1.00 17.22 ? 206 LYS A N 1 ATOM 1572 C CA . LYS A 1 206 ? 22.732 16.364 37.893 1.00 17.60 ? 206 LYS A CA 1 ATOM 1573 C C . LYS A 1 206 ? 22.563 16.663 39.395 1.00 18.26 ? 206 LYS A C 1 ATOM 1574 O O . LYS A 1 206 ? 21.446 16.555 39.920 1.00 19.12 ? 206 LYS A O 1 ATOM 1575 C CB . LYS A 1 206 ? 22.791 17.676 37.077 1.00 17.56 ? 206 LYS A CB 1 ATOM 1576 C CG . LYS A 1 206 ? 21.613 18.642 37.327 1.00 18.38 ? 206 LYS A CG 1 ATOM 1577 C CD . LYS A 1 206 ? 21.626 19.838 36.348 1.00 18.07 ? 206 LYS A CD 1 ATOM 1578 C CE . LYS A 1 206 ? 20.633 20.919 36.812 1.00 18.52 ? 206 LYS A CE 1 ATOM 1579 N NZ . LYS A 1 206 ? 20.686 22.097 35.869 1.00 19.09 ? 206 LYS A NZ 1 ATOM 1580 N N . HIS A 1 207 ? 23.629 17.057 40.097 1.00 18.34 ? 207 HIS A N 1 ATOM 1581 C CA . HIS A 1 207 ? 25.019 17.108 39.592 1.00 18.74 ? 207 HIS A CA 1 ATOM 1582 C C . HIS A 1 207 ? 25.782 16.008 40.324 1.00 19.30 ? 207 HIS A C 1 ATOM 1583 O O . HIS A 1 207 ? 25.739 15.916 41.562 1.00 19.28 ? 207 HIS A O 1 ATOM 1584 C CB . HIS A 1 207 ? 25.674 18.479 39.896 1.00 19.20 ? 207 HIS A CB 1 ATOM 1585 C CG . HIS A 1 207 ? 24.824 19.663 39.525 1.00 19.59 ? 207 HIS A CG 1 ATOM 1586 N ND1 . HIS A 1 207 ? 23.836 20.164 40.354 1.00 21.00 ? 207 HIS A ND1 1 ATOM 1587 C CD2 . HIS A 1 207 ? 24.825 20.456 38.422 1.00 21.57 ? 207 HIS A CD2 1 ATOM 1588 C CE1 . HIS A 1 207 ? 23.258 21.204 39.771 1.00 21.58 ? 207 HIS A CE1 1 ATOM 1589 N NE2 . HIS A 1 207 ? 23.836 21.399 38.598 1.00 20.77 ? 207 HIS A NE2 1 ATOM 1590 N N . PHE A 1 208 ? 26.440 15.150 39.557 1.00 19.33 ? 208 PHE A N 1 ATOM 1591 C CA . PHE A 1 208 ? 27.016 13.913 40.095 1.00 19.44 ? 208 PHE A CA 1 ATOM 1592 C C . PHE A 1 208 ? 28.352 14.232 40.787 1.00 20.45 ? 208 PHE A C 1 ATOM 1593 O O . PHE A 1 208 ? 29.253 14.794 40.154 1.00 19.84 ? 208 PHE A O 1 ATOM 1594 C CB . PHE A 1 208 ? 27.226 12.947 38.920 1.00 19.45 ? 208 PHE A CB 1 ATOM 1595 C CG . PHE A 1 208 ? 27.837 11.622 39.301 1.00 19.77 ? 208 PHE A CG 1 ATOM 1596 C CD1 . PHE A 1 208 ? 27.022 10.547 39.631 1.00 19.95 ? 208 PHE A CD1 1 ATOM 1597 C CD2 . PHE A 1 208 ? 29.230 11.430 39.244 1.00 21.33 ? 208 PHE A CD2 1 ATOM 1598 C CE1 . PHE A 1 208 ? 27.575 9.298 39.981 1.00 21.07 ? 208 PHE A CE1 1 ATOM 1599 C CE2 . PHE A 1 208 ? 29.802 10.173 39.601 1.00 21.60 ? 208 PHE A CE2 1 ATOM 1600 C CZ . PHE A 1 208 ? 28.969 9.112 39.947 1.00 20.54 ? 208 PHE A CZ 1 ATOM 1601 N N . VAL A 1 209 ? 28.520 13.901 42.077 1.00 20.89 ? 209 VAL A N 1 ATOM 1602 C CA . VAL A 1 209 ? 27.500 13.384 43.008 1.00 21.45 ? 209 VAL A CA 1 ATOM 1603 C C . VAL A 1 209 ? 27.753 14.057 44.373 1.00 21.69 ? 209 VAL A C 1 ATOM 1604 O O . VAL A 1 209 ? 28.887 14.451 44.685 1.00 21.93 ? 209 VAL A O 1 ATOM 1605 C CB . VAL A 1 209 ? 27.553 11.817 43.101 1.00 21.57 ? 209 VAL A CB 1 ATOM 1606 C CG1 . VAL A 1 209 ? 28.961 11.318 43.536 1.00 22.06 ? 209 VAL A CG1 1 ATOM 1607 C CG2 . VAL A 1 209 ? 26.431 11.234 44.006 1.00 21.79 ? 209 VAL A CG2 1 ATOM 1608 N N . GLY A 1 210 ? 26.703 14.190 45.188 1.00 21.64 ? 210 GLY A N 1 ATOM 1609 C CA . GLY A 1 210 ? 26.833 14.785 46.539 1.00 21.80 ? 210 GLY A CA 1 ATOM 1610 C C . GLY A 1 210 ? 26.799 16.308 46.539 1.00 21.91 ? 210 GLY A C 1 ATOM 1611 O O . GLY A 1 210 ? 27.242 16.963 47.507 1.00 21.21 ? 210 GLY A O 1 ATOM 1612 N N . ASP A 1 211 ? 26.233 16.892 45.468 1.00 21.27 ? 211 ASP A N 1 ATOM 1613 C CA . ASP A 1 211 ? 26.106 18.349 45.415 1.00 21.55 ? 211 ASP A CA 1 ATOM 1614 C C . ASP A 1 211 ? 25.285 18.930 46.572 1.00 21.14 ? 211 ASP A C 1 ATOM 1615 O O . ASP A 1 211 ? 25.488 20.079 46.975 1.00 21.41 ? 211 ASP A O 1 ATOM 1616 C CB . ASP A 1 211 ? 25.557 18.855 44.054 1.00 21.25 ? 211 ASP A CB 1 ATOM 1617 C CG . ASP A 1 211 ? 24.351 18.068 43.539 1.00 21.64 ? 211 ASP A CG 1 ATOM 1618 O OD1 . ASP A 1 211 ? 24.041 16.960 44.014 1.00 21.53 ? 211 ASP A OD1 1 ATOM 1619 O OD2 . ASP A 1 211 ? 23.686 18.572 42.601 1.00 22.88 ? 211 ASP A OD2 1 ATOM 1620 N N . GLY A 1 212 ? 24.363 18.127 47.094 1.00 21.52 ? 212 GLY A N 1 ATOM 1621 C CA . GLY A 1 212 ? 23.501 18.550 48.208 1.00 21.57 ? 212 GLY A CA 1 ATOM 1622 C C . GLY A 1 212 ? 24.067 18.263 49.594 1.00 22.68 ? 212 GLY A C 1 ATOM 1623 O O . GLY A 1 212 ? 23.382 18.483 50.598 1.00 22.81 ? 212 GLY A O 1 ATOM 1624 N N . GLY A 1 213 ? 25.313 17.794 49.648 1.00 22.52 ? 213 GLY A N 1 ATOM 1625 C CA . GLY A 1 213 ? 25.930 17.366 50.929 1.00 23.54 ? 213 GLY A CA 1 ATOM 1626 C C . GLY A 1 213 ? 27.091 18.226 51.401 1.00 24.38 ? 213 GLY A C 1 ATOM 1627 O O . GLY A 1 213 ? 27.857 17.824 52.303 1.00 24.92 ? 213 GLY A O 1 ATOM 1628 N N . THR A 1 214 ? 27.253 19.405 50.812 1.00 24.70 ? 214 THR A N 1 ATOM 1629 C CA . THR A 1 214 ? 28.434 20.215 51.107 1.00 25.50 ? 214 THR A CA 1 ATOM 1630 C C . THR A 1 214 ? 28.382 20.836 52.520 1.00 26.25 ? 214 THR A C 1 ATOM 1631 O O . THR A 1 214 ? 27.302 21.164 53.036 1.00 25.94 ? 214 THR A O 1 ATOM 1632 C CB . THR A 1 214 ? 28.666 21.339 50.058 1.00 26.13 ? 214 THR A CB 1 ATOM 1633 O OG1 . THR A 1 214 ? 27.625 22.314 50.170 1.00 24.98 ? 214 THR A OG1 1 ATOM 1634 C CG2 . THR A 1 214 ? 28.709 20.779 48.632 1.00 25.23 ? 214 THR A CG2 1 ATOM 1635 N N . VAL A 1 215 ? 29.556 21.000 53.124 1.00 26.30 ? 215 VAL A N 1 ATOM 1636 C CA . VAL A 1 215 ? 29.686 21.618 54.464 1.00 27.64 ? 215 VAL A CA 1 ATOM 1637 C C . VAL A 1 215 ? 28.951 22.953 54.569 1.00 27.10 ? 215 VAL A C 1 ATOM 1638 O O . VAL A 1 215 ? 29.216 23.864 53.784 1.00 26.70 ? 215 VAL A O 1 ATOM 1639 C CB . VAL A 1 215 ? 31.178 21.850 54.824 1.00 27.87 ? 215 VAL A CB 1 ATOM 1640 C CG1 . VAL A 1 215 ? 31.319 22.500 56.223 1.00 29.81 ? 215 VAL A CG1 1 ATOM 1641 C CG2 . VAL A 1 215 ? 31.925 20.543 54.769 1.00 29.36 ? 215 VAL A CG2 1 ATOM 1642 N N . ASP A 1 216 ? 28.032 23.045 55.543 1.00 26.99 ? 216 ASP A N 1 ATOM 1643 C CA . ASP A 1 216 ? 27.267 24.269 55.835 1.00 27.07 ? 216 ASP A CA 1 ATOM 1644 C C . ASP A 1 216 ? 26.461 24.749 54.628 1.00 26.18 ? 216 ASP A C 1 ATOM 1645 O O . ASP A 1 216 ? 26.124 25.931 54.539 1.00 25.77 ? 216 ASP A O 1 ATOM 1646 C CB . ASP A 1 216 ? 28.178 25.397 56.326 1.00 28.08 ? 216 ASP A CB 1 ATOM 1647 C CG . ASP A 1 216 ? 28.801 25.096 57.692 1.00 30.09 ? 216 ASP A CG 1 ATOM 1648 O OD1 . ASP A 1 216 ? 28.328 24.162 58.388 1.00 32.66 ? 216 ASP A OD1 1 ATOM 1649 O OD2 . ASP A 1 216 ? 29.764 25.800 58.053 1.00 33.31 ? 216 ASP A OD2 1 ATOM 1650 N N . GLY A 1 217 ? 26.175 23.822 53.711 1.00 25.54 ? 217 GLY A N 1 ATOM 1651 C CA . GLY A 1 217 ? 25.485 24.156 52.458 1.00 24.95 ? 217 GLY A CA 1 ATOM 1652 C C . GLY A 1 217 ? 26.236 25.156 51.588 1.00 25.05 ? 217 GLY A C 1 ATOM 1653 O O . GLY A 1 217 ? 25.621 25.855 50.774 1.00 25.53 ? 217 GLY A O 1 ATOM 1654 N N . ILE A 1 218 ? 27.564 25.234 51.732 1.00 24.31 ? 218 ILE A N 1 ATOM 1655 C CA . ILE A 1 218 ? 28.356 26.145 50.891 1.00 24.09 ? 218 ILE A CA 1 ATOM 1656 C C . ILE A 1 218 ? 28.371 25.607 49.457 1.00 23.88 ? 218 ILE A C 1 ATOM 1657 O O . ILE A 1 218 ? 28.814 24.487 49.202 1.00 23.79 ? 218 ILE A O 1 ATOM 1658 C CB . ILE A 1 218 ? 29.789 26.350 51.428 1.00 24.19 ? 218 ILE A CB 1 ATOM 1659 C CG1 . ILE A 1 218 ? 29.762 26.947 52.840 1.00 25.20 ? 218 ILE A CG1 1 ATOM 1660 C CG2 . ILE A 1 218 ? 30.577 27.297 50.503 1.00 24.42 ? 218 ILE A CG2 1 ATOM 1661 C CD1 . ILE A 1 218 ? 31.074 26.710 53.594 1.00 25.99 ? 218 ILE A CD1 1 ATOM 1662 N N . ASN A 1 219 ? 27.849 26.406 48.529 1.00 23.22 ? 219 ASN A N 1 ATOM 1663 C CA . ASN A 1 219 ? 27.704 25.960 47.136 1.00 22.99 ? 219 ASN A CA 1 ATOM 1664 C C . ASN A 1 219 ? 29.077 25.643 46.535 1.00 22.81 ? 219 ASN A C 1 ATOM 1665 O O . ASN A 1 219 ? 30.030 26.394 46.747 1.00 22.41 ? 219 ASN A O 1 ATOM 1666 C CB . ASN A 1 219 ? 27.015 27.061 46.317 1.00 22.91 ? 219 ASN A CB 1 ATOM 1667 C CG . ASN A 1 219 ? 26.645 26.614 44.907 1.00 22.55 ? 219 ASN A CG 1 ATOM 1668 O OD1 . ASN A 1 219 ? 26.787 27.390 43.941 1.00 25.58 ? 219 ASN A OD1 1 ATOM 1669 N ND2 . ASN A 1 219 ? 26.168 25.394 44.775 1.00 18.79 ? 219 ASN A ND2 1 ATOM 1670 N N . GLU A 1 220 ? 29.166 24.519 45.818 1.00 22.78 ? 220 GLU A N 1 ATOM 1671 C CA . GLU A 1 220 ? 30.393 24.102 45.106 1.00 23.42 ? 220 GLU A CA 1 ATOM 1672 C C . GLU A 1 220 ? 31.500 23.614 46.051 1.00 24.23 ? 220 GLU A C 1 ATOM 1673 O O . GLU A 1 220 ? 32.638 23.415 45.616 1.00 24.25 ? 220 GLU A O 1 ATOM 1674 C CB . GLU A 1 220 ? 30.945 25.241 44.212 1.00 23.41 ? 220 GLU A CB 1 ATOM 1675 C CG . GLU A 1 220 ? 29.862 25.878 43.306 1.00 25.02 ? 220 GLU A CG 1 ATOM 1676 C CD . GLU A 1 220 ? 30.399 26.776 42.191 1.00 24.72 ? 220 GLU A CD 1 ATOM 1677 O OE1 . GLU A 1 220 ? 31.639 26.821 41.936 1.00 26.63 ? 220 GLU A OE1 1 ATOM 1678 O OE2 . GLU A 1 220 ? 29.542 27.435 41.550 1.00 25.69 ? 220 GLU A OE2 1 ATOM 1679 N N . ASN A 1 221 ? 31.162 23.429 47.331 1.00 24.51 ? 221 ASN A N 1 ATOM 1680 C CA . ASN A 1 221 ? 32.190 23.175 48.355 1.00 25.24 ? 221 ASN A CA 1 ATOM 1681 C C . ASN A 1 221 ? 32.478 21.685 48.565 1.00 25.17 ? 221 ASN A C 1 ATOM 1682 O O . ASN A 1 221 ? 32.291 20.878 47.648 1.00 24.26 ? 221 ASN A O 1 ATOM 1683 C CB . ASN A 1 221 ? 31.851 23.887 49.674 1.00 25.78 ? 221 ASN A CB 1 ATOM 1684 C CG . ASN A 1 221 ? 33.101 24.281 50.443 1.00 27.61 ? 221 ASN A CG 1 ATOM 1685 O OD1 . ASN A 1 221 ? 33.448 23.653 51.461 1.00 30.01 ? 221 ASN A OD1 1 ATOM 1686 N ND2 . ASN A 1 221 ? 33.820 25.271 49.908 1.00 29.78 ? 221 ASN A ND2 1 ATOM 1687 N N . ASN A 1 222 ? 32.920 21.314 49.771 1.00 25.41 ? 222 ASN A N 1 ATOM 1688 C CA . ASN A 1 222 ? 33.350 19.952 50.045 1.00 26.34 ? 222 ASN A CA 1 ATOM 1689 C C . ASN A 1 222 ? 32.253 19.137 50.726 1.00 26.40 ? 222 ASN A C 1 ATOM 1690 O O . ASN A 1 222 ? 31.693 19.572 51.739 1.00 27.24 ? 222 ASN A O 1 ATOM 1691 C CB . ASN A 1 222 ? 34.595 19.996 50.946 1.00 26.27 ? 222 ASN A CB 1 ATOM 1692 C CG . ASN A 1 222 ? 35.359 18.668 50.979 1.00 28.15 ? 222 ASN A CG 1 ATOM 1693 O OD1 . ASN A 1 222 ? 35.136 17.758 50.162 1.00 28.56 ? 222 ASN A OD1 1 ATOM 1694 N ND2 . ASN A 1 222 ? 36.274 18.560 51.941 1.00 28.50 ? 222 ASN A ND2 1 ATOM 1695 N N . THR A 1 223 ? 31.957 17.960 50.185 1.00 26.79 ? 223 THR A N 1 ATOM 1696 C CA . THR A 1 223 ? 31.025 17.035 50.804 1.00 27.53 ? 223 THR A CA 1 ATOM 1697 C C . THR A 1 223 ? 31.837 16.001 51.593 1.00 28.28 ? 223 THR A C 1 ATOM 1698 O O . THR A 1 223 ? 32.514 15.146 51.011 1.00 27.74 ? 223 THR A O 1 ATOM 1699 C CB . THR A 1 223 ? 30.103 16.381 49.750 1.00 27.86 ? 223 THR A CB 1 ATOM 1700 O OG1 . THR A 1 223 ? 29.252 17.401 49.184 1.00 29.10 ? 223 THR A OG1 1 ATOM 1701 C CG2 . THR A 1 223 ? 29.242 15.281 50.359 1.00 28.15 ? 223 THR A CG2 1 ATOM 1702 N N . ILE A 1 224 ? 31.783 16.120 52.918 1.00 29.19 ? 224 ILE A N 1 ATOM 1703 C CA . ILE A 1 224 ? 32.589 15.269 53.808 1.00 30.55 ? 224 ILE A CA 1 ATOM 1704 C C . ILE A 1 224 ? 31.694 14.187 54.407 1.00 30.97 ? 224 ILE A C 1 ATOM 1705 O O . ILE A 1 224 ? 30.898 14.462 55.310 1.00 31.92 ? 224 ILE A O 1 ATOM 1706 C CB . ILE A 1 224 ? 33.256 16.093 54.933 1.00 30.36 ? 224 ILE A CB 1 ATOM 1707 C CG1 . ILE A 1 224 ? 34.091 17.238 54.355 1.00 30.75 ? 224 ILE A CG1 1 ATOM 1708 C CG2 . ILE A 1 224 ? 34.104 15.164 55.840 1.00 30.66 ? 224 ILE A CG2 1 ATOM 1709 C CD1 . ILE A 1 224 ? 34.495 18.303 55.373 1.00 31.24 ? 224 ILE A CD1 1 ATOM 1710 N N . ILE A 1 225 ? 31.800 12.978 53.866 1.00 31.40 ? 225 ILE A N 1 ATOM 1711 C CA . ILE A 1 225 ? 30.953 11.838 54.233 1.00 32.11 ? 225 ILE A CA 1 ATOM 1712 C C . ILE A 1 225 ? 31.672 10.572 53.786 1.00 32.82 ? 225 ILE A C 1 ATOM 1713 O O . ILE A 1 225 ? 32.358 10.571 52.748 1.00 31.95 ? 225 ILE A O 1 ATOM 1714 C CB . ILE A 1 225 ? 29.532 11.919 53.577 1.00 32.20 ? 225 ILE A CB 1 ATOM 1715 C CG1 . ILE A 1 225 ? 28.542 10.942 54.232 1.00 32.45 ? 225 ILE A CG1 1 ATOM 1716 C CG2 . ILE A 1 225 ? 29.599 11.687 52.057 1.00 32.55 ? 225 ILE A CG2 1 ATOM 1717 C CD1 . ILE A 1 225 ? 27.068 11.317 54.037 1.00 32.25 ? 225 ILE A CD1 1 ATOM 1718 N N . ASN A 1 226 ? 31.546 9.494 54.565 1.00 33.58 ? 226 ASN A N 1 ATOM 1719 C CA . ASN A 1 226 ? 32.144 8.223 54.142 1.00 34.47 ? 226 ASN A CA 1 ATOM 1720 C C . ASN A 1 226 ? 31.412 7.622 52.937 1.00 34.65 ? 226 ASN A C 1 ATOM 1721 O O . ASN A 1 226 ? 30.319 8.090 52.564 1.00 34.25 ? 226 ASN A O 1 ATOM 1722 C CB . ASN A 1 226 ? 32.294 7.229 55.319 1.00 34.61 ? 226 ASN A CB 1 ATOM 1723 C CG . ASN A 1 226 ? 30.957 6.756 55.901 1.00 36.91 ? 226 ASN A CG 1 ATOM 1724 O OD1 . ASN A 1 226 ? 29.875 6.986 55.343 1.00 37.66 ? 226 ASN A OD1 1 ATOM 1725 N ND2 . ASN A 1 226 ? 31.038 6.062 57.048 1.00 37.78 ? 226 ASN A ND2 1 ATOM 1726 N N . ARG A 1 227 ? 32.021 6.619 52.309 1.00 34.94 ? 227 ARG A N 1 ATOM 1727 C CA . ARG A 1 227 ? 31.425 5.982 51.131 1.00 35.29 ? 227 ARG A CA 1 ATOM 1728 C C . ARG A 1 227 ? 30.027 5.445 51.418 1.00 35.39 ? 227 ARG A C 1 ATOM 1729 O O . ARG A 1 227 ? 29.122 5.587 50.594 1.00 34.97 ? 227 ARG A O 1 ATOM 1730 C CB . ARG A 1 227 ? 32.324 4.876 50.575 1.00 36.16 ? 227 ARG A CB 1 ATOM 1731 C CG . ARG A 1 227 ? 31.894 4.364 49.197 1.00 36.80 ? 227 ARG A CG 1 ATOM 1732 C CD . ARG A 1 227 ? 32.823 3.254 48.713 1.00 38.10 ? 227 ARG A CD 1 ATOM 1733 N NE . ARG A 1 227 ? 32.612 2.871 47.310 1.00 48.36 ? 227 ARG A NE 1 ATOM 1734 C CZ . ARG A 1 227 ? 31.710 1.986 46.883 1.00 33.50 ? 227 ARG A CZ 1 ATOM 1735 N NH1 . ARG A 1 227 ? 30.883 1.392 47.739 1.00 51.66 ? 227 ARG A NH1 1 ATOM 1736 N NH2 . ARG A 1 227 ? 31.622 1.704 45.586 1.00 47.57 ? 227 ARG A NH2 1 ATOM 1737 N N . GLU A 1 228 ? 29.844 4.847 52.596 1.00 35.05 ? 228 GLU A N 1 ATOM 1738 C CA . GLU A 1 228 ? 28.539 4.313 52.968 1.00 36.31 ? 228 GLU A CA 1 ATOM 1739 C C . GLU A 1 228 ? 27.466 5.414 52.910 1.00 34.18 ? 228 GLU A C 1 ATOM 1740 O O . GLU A 1 228 ? 26.395 5.189 52.374 1.00 34.42 ? 228 GLU A O 1 ATOM 1741 C CB . GLU A 1 228 ? 28.571 3.656 54.355 1.00 35.67 ? 228 GLU A CB 1 ATOM 1742 C CG . GLU A 1 228 ? 27.275 2.936 54.698 1.00 38.99 ? 228 GLU A CG 1 ATOM 1743 C CD . GLU A 1 228 ? 27.397 1.995 55.902 1.00 37.33 ? 228 GLU A CD 1 ATOM 1744 O OE1 . GLU A 1 228 ? 28.390 2.087 56.661 1.00 44.65 ? 228 GLU A OE1 1 ATOM 1745 O OE2 . GLU A 1 228 ? 26.478 1.167 56.090 1.00 45.10 ? 228 GLU A OE2 1 ATOM 1746 N N . GLY A 1 229 ? 27.782 6.590 53.445 1.00 33.30 ? 229 GLY A N 1 ATOM 1747 C CA . GLY A 1 229 ? 26.857 7.726 53.455 1.00 32.45 ? 229 GLY A CA 1 ATOM 1748 C C . GLY A 1 229 ? 26.604 8.263 52.054 1.00 31.82 ? 229 GLY A C 1 ATOM 1749 O O . GLY A 1 229 ? 25.455 8.539 51.673 1.00 31.87 ? 229 GLY A O 1 ATOM 1750 N N . LEU A 1 230 ? 27.673 8.390 51.273 1.00 30.43 ? 230 LEU A N 1 ATOM 1751 C CA . LEU A 1 230 ? 27.534 8.836 49.881 1.00 29.67 ? 230 LEU A CA 1 ATOM 1752 C C . LEU A 1 230 ? 26.591 7.902 49.121 1.00 29.40 ? 230 LEU A C 1 ATOM 1753 O O . LEU A 1 230 ? 25.695 8.354 48.402 1.00 29.31 ? 230 LEU A O 1 ATOM 1754 C CB . LEU A 1 230 ? 28.896 8.899 49.179 1.00 29.12 ? 230 LEU A CB 1 ATOM 1755 C CG . LEU A 1 230 ? 28.812 9.547 47.786 1.00 28.69 ? 230 LEU A CG 1 ATOM 1756 C CD1 . LEU A 1 230 ? 28.836 11.079 47.899 1.00 27.93 ? 230 LEU A CD1 1 ATOM 1757 C CD2 . LEU A 1 230 ? 29.954 9.035 46.906 1.00 29.65 ? 230 LEU A CD2 1 ATOM 1758 N N . MET A 1 231 ? 26.790 6.594 49.286 1.00 28.82 ? 231 MET A N 1 ATOM 1759 C CA . MET A 1 231 ? 26.003 5.609 48.560 1.00 28.91 ? 231 MET A CA 1 ATOM 1760 C C . MET A 1 231 ? 24.569 5.478 49.078 1.00 28.63 ? 231 MET A C 1 ATOM 1761 O O . MET A 1 231 ? 23.682 5.052 48.337 1.00 29.04 ? 231 MET A O 1 ATOM 1762 C CB . MET A 1 231 ? 26.702 4.238 48.563 1.00 29.56 ? 231 MET A CB 1 ATOM 1763 C CG . MET A 1 231 ? 28.071 4.236 47.866 1.00 29.78 ? 231 MET A CG 1 ATOM 1764 S SD . MET A 1 231 ? 27.893 4.668 46.123 1.00 32.83 ? 231 MET A SD 1 ATOM 1765 C CE . MET A 1 231 ? 29.604 4.712 45.580 1.00 31.59 ? 231 MET A CE 1 ATOM 1766 N N . ASN A 1 232 ? 24.353 5.830 50.346 1.00 28.57 ? 232 ASN A N 1 ATOM 1767 C CA . ASN A 1 232 ? 23.053 5.661 50.992 1.00 28.96 ? 232 ASN A CA 1 ATOM 1768 C C . ASN A 1 232 ? 22.152 6.889 50.807 1.00 27.74 ? 232 ASN A C 1 ATOM 1769 O O . ASN A 1 232 ? 20.920 6.774 50.808 1.00 27.60 ? 232 ASN A O 1 ATOM 1770 C CB . ASN A 1 232 ? 23.238 5.363 52.496 1.00 30.29 ? 232 ASN A CB 1 ATOM 1771 C CG . ASN A 1 232 ? 21.917 5.092 53.220 1.00 34.89 ? 232 ASN A CG 1 ATOM 1772 O OD1 . ASN A 1 232 ? 21.158 4.185 52.851 1.00 40.40 ? 232 ASN A OD1 1 ATOM 1773 N ND2 . ASN A 1 232 ? 21.644 5.873 54.270 1.00 38.89 ? 232 ASN A ND2 1 ATOM 1774 N N . ILE A 1 233 ? 22.779 8.050 50.644 1.00 26.18 ? 233 ILE A N 1 ATOM 1775 C CA . ILE A 1 233 ? 22.040 9.317 50.595 1.00 24.83 ? 233 ILE A CA 1 ATOM 1776 C C . ILE A 1 233 ? 22.087 9.924 49.195 1.00 24.44 ? 233 ILE A C 1 ATOM 1777 O O . ILE A 1 233 ? 21.048 10.163 48.588 1.00 23.94 ? 233 ILE A O 1 ATOM 1778 C CB . ILE A 1 233 ? 22.576 10.359 51.612 1.00 24.73 ? 233 ILE A CB 1 ATOM 1779 C CG1 . ILE A 1 233 ? 22.390 9.865 53.065 1.00 24.54 ? 233 ILE A CG1 1 ATOM 1780 C CG2 . ILE A 1 233 ? 21.881 11.735 51.426 1.00 24.31 ? 233 ILE A CG2 1 ATOM 1781 C CD1 . ILE A 1 233 ? 23.065 10.764 54.097 1.00 25.68 ? 233 ILE A CD1 1 ATOM 1782 N N . HIS A 1 234 ? 23.301 10.118 48.690 1.00 24.06 ? 234 HIS A N 1 ATOM 1783 C CA . HIS A 1 234 ? 23.509 10.991 47.524 1.00 23.50 ? 234 HIS A CA 1 ATOM 1784 C C . HIS A 1 234 ? 23.481 10.265 46.174 1.00 23.76 ? 234 HIS A C 1 ATOM 1785 O O . HIS A 1 234 ? 23.204 10.885 45.114 1.00 23.23 ? 234 HIS A O 1 ATOM 1786 C CB . HIS A 1 234 ? 24.791 11.793 47.727 1.00 23.13 ? 234 HIS A CB 1 ATOM 1787 C CG . HIS A 1 234 ? 24.677 12.807 48.818 1.00 23.71 ? 234 HIS A CG 1 ATOM 1788 N ND1 . HIS A 1 234 ? 25.306 12.680 50.041 1.00 25.11 ? 234 HIS A ND1 1 ATOM 1789 C CD2 . HIS A 1 234 ? 23.942 13.940 48.889 1.00 20.38 ? 234 HIS A CD2 1 ATOM 1790 C CE1 . HIS A 1 234 ? 25.004 13.721 50.798 1.00 21.04 ? 234 HIS A CE1 1 ATOM 1791 N NE2 . HIS A 1 234 ? 24.175 14.500 50.120 1.00 25.68 ? 234 HIS A NE2 1 ATOM 1792 N N . MET A 1 235 ? 23.774 8.965 46.216 1.00 23.08 ? 235 MET A N 1 ATOM 1793 C CA . MET A 1 235 ? 23.849 8.123 45.026 1.00 23.25 ? 235 MET A CA 1 ATOM 1794 C C . MET A 1 235 ? 22.550 7.438 44.537 1.00 23.24 ? 235 MET A C 1 ATOM 1795 O O . MET A 1 235 ? 22.377 7.279 43.329 1.00 23.58 ? 235 MET A O 1 ATOM 1796 C CB . MET A 1 235 ? 24.962 7.068 45.194 1.00 23.30 ? 235 MET A CB 1 ATOM 1797 C CG . MET A 1 235 ? 25.309 6.298 43.917 1.00 22.94 ? 235 MET A CG 1 ATOM 1798 S SD . MET A 1 235 ? 26.054 7.401 42.667 1.00 24.63 ? 235 MET A SD 1 ATOM 1799 C CE . MET A 1 235 ? 27.703 7.604 43.338 1.00 24.10 ? 235 MET A CE 1 ATOM 1800 N N . PRO A 1 236 ? 21.661 6.971 45.456 1.00 23.59 ? 236 PRO A N 1 ATOM 1801 C CA . PRO A 1 236 ? 20.544 6.128 44.984 1.00 23.01 ? 236 PRO A CA 1 ATOM 1802 C C . PRO A 1 236 ? 19.743 6.620 43.771 1.00 22.47 ? 236 PRO A C 1 ATOM 1803 O O . PRO A 1 236 ? 19.395 5.821 42.891 1.00 22.61 ? 236 PRO A O 1 ATOM 1804 C CB . PRO A 1 236 ? 19.633 6.035 46.221 1.00 23.60 ? 236 PRO A CB 1 ATOM 1805 C CG . PRO A 1 236 ? 20.616 6.089 47.374 1.00 23.32 ? 236 PRO A CG 1 ATOM 1806 C CD . PRO A 1 236 ? 21.641 7.120 46.929 1.00 24.26 ? 236 PRO A CD 1 ATOM 1807 N N . ALA A 1 237 ? 19.420 7.913 43.739 1.00 21.84 ? 237 ALA A N 1 ATOM 1808 C CA . ALA A 1 237 ? 18.581 8.420 42.653 1.00 21.90 ? 237 ALA A CA 1 ATOM 1809 C C . ALA A 1 237 ? 19.293 8.317 41.281 1.00 21.58 ? 237 ALA A C 1 ATOM 1810 O O . ALA A 1 237 ? 18.624 8.205 40.246 1.00 21.53 ? 237 ALA A O 1 ATOM 1811 C CB . ALA A 1 237 ? 18.098 9.835 42.938 1.00 21.80 ? 237 ALA A CB 1 ATOM 1812 N N . TYR A 1 238 ? 20.627 8.302 41.282 1.00 21.10 ? 238 TYR A N 1 ATOM 1813 C CA . TYR A 1 238 ? 21.355 8.046 40.017 1.00 21.09 ? 238 TYR A CA 1 ATOM 1814 C C . TYR A 1 238 ? 21.067 6.661 39.461 1.00 21.78 ? 238 TYR A C 1 ATOM 1815 O O . TYR A 1 238 ? 20.939 6.495 38.255 1.00 21.00 ? 238 TYR A O 1 ATOM 1816 C CB . TYR A 1 238 ? 22.864 8.332 40.139 1.00 20.90 ? 238 TYR A CB 1 ATOM 1817 C CG . TYR A 1 238 ? 23.122 9.809 40.149 1.00 19.67 ? 238 TYR A CG 1 ATOM 1818 C CD1 . TYR A 1 238 ? 23.243 10.527 38.932 1.00 18.71 ? 238 TYR A CD1 1 ATOM 1819 C CD2 . TYR A 1 238 ? 23.215 10.511 41.352 1.00 20.10 ? 238 TYR A CD2 1 ATOM 1820 C CE1 . TYR A 1 238 ? 23.450 11.908 38.937 1.00 19.49 ? 238 TYR A CE1 1 ATOM 1821 C CE2 . TYR A 1 238 ? 23.430 11.904 41.372 1.00 20.46 ? 238 TYR A CE2 1 ATOM 1822 C CZ . TYR A 1 238 ? 23.539 12.591 40.162 1.00 19.75 ? 238 TYR A CZ 1 ATOM 1823 O OH . TYR A 1 238 ? 23.730 13.946 40.198 1.00 20.77 ? 238 TYR A OH 1 ATOM 1824 N N . LYS A 1 239 ? 20.905 5.676 40.348 1.00 22.53 ? 239 LYS A N 1 ATOM 1825 C CA . LYS A 1 239 ? 20.509 4.351 39.890 1.00 23.13 ? 239 LYS A CA 1 ATOM 1826 C C . LYS A 1 239 ? 19.104 4.332 39.269 1.00 22.64 ? 239 LYS A C 1 ATOM 1827 O O . LYS A 1 239 ? 18.899 3.725 38.210 1.00 22.07 ? 239 LYS A O 1 ATOM 1828 C CB . LYS A 1 239 ? 20.674 3.308 41.006 1.00 25.11 ? 239 LYS A CB 1 ATOM 1829 C CG . LYS A 1 239 ? 20.320 1.888 40.580 1.00 27.42 ? 239 LYS A CG 1 ATOM 1830 C CD . LYS A 1 239 ? 21.236 1.310 39.478 1.00 32.40 ? 239 LYS A CD 1 ATOM 1831 C CE . LYS A 1 239 ? 21.013 -0.206 39.303 1.00 31.90 ? 239 LYS A CE 1 ATOM 1832 N NZ . LYS A 1 239 ? 19.584 -0.552 38.956 1.00 37.20 ? 239 LYS A NZ 1 ATOM 1833 N N . ASN A 1 240 ? 18.141 5.024 39.885 1.00 21.92 ? 240 ASN A N 1 ATOM 1834 C CA . ASN A 1 240 ? 16.818 5.128 39.272 1.00 21.93 ? 240 ASN A CA 1 ATOM 1835 C C . ASN A 1 240 ? 16.899 5.819 37.903 1.00 21.09 ? 240 ASN A C 1 ATOM 1836 O O . ASN A 1 240 ? 16.186 5.454 36.970 1.00 20.60 ? 240 ASN A O 1 ATOM 1837 C CB . ASN A 1 240 ? 15.861 5.901 40.185 1.00 22.19 ? 240 ASN A CB 1 ATOM 1838 C CG . ASN A 1 240 ? 15.663 5.207 41.522 1.00 24.37 ? 240 ASN A CG 1 ATOM 1839 O OD1 . ASN A 1 240 ? 16.439 5.393 42.450 1.00 23.59 ? 240 ASN A OD1 1 ATOM 1840 N ND2 . ASN A 1 240 ? 14.623 4.399 41.613 1.00 28.89 ? 240 ASN A ND2 1 ATOM 1841 N N . ALA A 1 241 ? 17.777 6.816 37.804 1.00 21.09 ? 241 ALA A N 1 ATOM 1842 C CA . ALA A 1 241 ? 17.966 7.551 36.554 1.00 20.59 ? 241 ALA A CA 1 ATOM 1843 C C . ALA A 1 241 ? 18.489 6.604 35.455 1.00 20.94 ? 241 ALA A C 1 ATOM 1844 O O . ALA A 1 241 ? 18.008 6.642 34.317 1.00 20.75 ? 241 ALA A O 1 ATOM 1845 C CB . ALA A 1 241 ? 18.908 8.759 36.768 1.00 20.47 ? 241 ALA A CB 1 ATOM 1846 N N . MET A 1 242 ? 19.443 5.737 35.807 1.00 20.82 ? 242 MET A N 1 ATOM 1847 C CA . MET A 1 242 ? 19.948 4.707 34.869 1.00 21.36 ? 242 MET A CA 1 ATOM 1848 C C . MET A 1 242 ? 18.812 3.789 34.415 1.00 21.76 ? 242 MET A C 1 ATOM 1849 O O . MET A 1 242 ? 18.692 3.427 33.245 1.00 21.54 ? 242 MET A O 1 ATOM 1850 C CB . MET A 1 242 ? 21.019 3.825 35.533 1.00 21.32 ? 242 MET A CB 1 ATOM 1851 C CG . MET A 1 242 ? 22.258 4.538 36.059 1.00 21.91 ? 242 MET A CG 1 ATOM 1852 S SD . MET A 1 242 ? 23.273 5.296 34.786 1.00 24.22 ? 242 MET A SD 1 ATOM 1853 C CE . MET A 1 242 ? 22.697 6.994 34.945 1.00 25.20 ? 242 MET A CE 1 ATOM 1854 N N . ASP A 1 243 ? 17.985 3.385 35.375 1.00 22.58 ? 243 ASP A N 1 ATOM 1855 C CA . ASP A 1 243 ? 16.877 2.484 35.087 1.00 22.83 ? 243 ASP A CA 1 ATOM 1856 C C . ASP A 1 243 ? 15.862 3.101 34.141 1.00 23.14 ? 243 ASP A C 1 ATOM 1857 O O . ASP A 1 243 ? 15.155 2.376 33.424 1.00 23.96 ? 243 ASP A O 1 ATOM 1858 C CB . ASP A 1 243 ? 16.156 2.110 36.384 1.00 23.32 ? 243 ASP A CB 1 ATOM 1859 C CG . ASP A 1 243 ? 16.940 1.156 37.250 1.00 25.74 ? 243 ASP A CG 1 ATOM 1860 O OD1 . ASP A 1 243 ? 17.971 0.587 36.819 1.00 26.95 ? 243 ASP A OD1 1 ATOM 1861 O OD2 . ASP A 1 243 ? 16.494 0.954 38.397 1.00 27.12 ? 243 ASP A OD2 1 ATOM 1862 N N . LYS A 1 244 ? 15.789 4.439 34.160 1.00 22.02 ? 244 LYS A N 1 ATOM 1863 C CA . LYS A 1 244 ? 14.847 5.185 33.336 1.00 22.42 ? 244 LYS A CA 1 ATOM 1864 C C . LYS A 1 244 ? 15.471 5.737 32.039 1.00 21.69 ? 244 LYS A C 1 ATOM 1865 O O . LYS A 1 244 ? 14.817 6.475 31.282 1.00 23.10 ? 244 LYS A O 1 ATOM 1866 C CB . LYS A 1 244 ? 14.171 6.281 34.185 1.00 21.74 ? 244 LYS A CB 1 ATOM 1867 C CG . LYS A 1 244 ? 13.297 5.651 35.305 1.00 22.98 ? 244 LYS A CG 1 ATOM 1868 C CD . LYS A 1 244 ? 12.811 6.628 36.348 1.00 23.25 ? 244 LYS A CD 1 ATOM 1869 C CE . LYS A 1 244 ? 12.158 5.837 37.493 1.00 23.72 ? 244 LYS A CE 1 ATOM 1870 N NZ . LYS A 1 244 ? 11.356 6.706 38.361 1.00 25.92 ? 244 LYS A NZ 1 ATOM 1871 N N . GLY A 1 245 ? 16.725 5.364 31.782 1.00 20.95 ? 245 GLY A N 1 ATOM 1872 C CA . GLY A 1 245 ? 17.371 5.693 30.517 1.00 20.17 ? 245 GLY A CA 1 ATOM 1873 C C . GLY A 1 245 ? 17.802 7.154 30.381 1.00 19.07 ? 245 GLY A C 1 ATOM 1874 O O . GLY A 1 245 ? 17.864 7.686 29.262 1.00 19.49 ? 245 GLY A O 1 ATOM 1875 N N . VAL A 1 246 ? 18.126 7.812 31.491 1.00 18.66 ? 246 VAL A N 1 ATOM 1876 C CA . VAL A 1 246 ? 18.611 9.204 31.392 1.00 18.41 ? 246 VAL A CA 1 ATOM 1877 C C . VAL A 1 246 ? 19.778 9.290 30.360 1.00 18.33 ? 246 VAL A C 1 ATOM 1878 O O . VAL A 1 246 ? 20.682 8.439 30.353 1.00 18.56 ? 246 VAL A O 1 ATOM 1879 C CB . VAL A 1 246 ? 19.010 9.798 32.765 1.00 17.92 ? 246 VAL A CB 1 ATOM 1880 C CG1 . VAL A 1 246 ? 20.359 9.237 33.276 1.00 18.96 ? 246 VAL A CG1 1 ATOM 1881 C CG2 . VAL A 1 246 ? 18.999 11.334 32.711 1.00 19.35 ? 246 VAL A CG2 1 ATOM 1882 N N . SER A 1 247 ? 19.725 10.283 29.477 1.00 17.63 ? 247 SER A N 1 ATOM 1883 C CA . SER A 1 247 ? 20.661 10.327 28.323 1.00 18.36 ? 247 SER A CA 1 ATOM 1884 C C . SER A 1 247 ? 22.037 10.846 28.685 1.00 17.81 ? 247 SER A C 1 ATOM 1885 O O . SER A 1 247 ? 23.055 10.456 28.067 1.00 18.26 ? 247 SER A O 1 ATOM 1886 C CB . SER A 1 247 ? 20.084 11.163 27.181 1.00 18.37 ? 247 SER A CB 1 ATOM 1887 O OG . SER A 1 247 ? 19.024 10.457 26.556 1.00 20.52 ? 247 SER A OG 1 ATOM 1888 N N . THR A 1 248 ? 22.063 11.761 29.647 1.00 16.84 ? 248 THR A N 1 ATOM 1889 C CA . THR A 1 248 ? 23.305 12.395 30.080 1.00 16.71 ? 248 THR A CA 1 ATOM 1890 C C . THR A 1 248 ? 23.358 12.557 31.606 1.00 17.39 ? 248 THR A C 1 ATOM 1891 O O . THR A 1 248 ? 22.321 12.499 32.311 1.00 17.31 ? 248 THR A O 1 ATOM 1892 C CB . THR A 1 248 ? 23.509 13.792 29.420 1.00 16.93 ? 248 THR A CB 1 ATOM 1893 O OG1 . THR A 1 248 ? 22.639 14.769 30.038 1.00 16.07 ? 248 THR A OG1 1 ATOM 1894 C CG2 . THR A 1 248 ? 23.231 13.731 27.919 1.00 17.07 ? 248 THR A CG2 1 ATOM 1895 N N . VAL A 1 249 ? 24.575 12.755 32.095 1.00 16.84 ? 249 VAL A N 1 ATOM 1896 C CA . VAL A 1 249 ? 24.828 13.059 33.491 1.00 17.30 ? 249 VAL A CA 1 ATOM 1897 C C . VAL A 1 249 ? 25.802 14.242 33.550 1.00 17.98 ? 249 VAL A C 1 ATOM 1898 O O . VAL A 1 249 ? 26.842 14.223 32.888 1.00 18.12 ? 249 VAL A O 1 ATOM 1899 C CB . VAL A 1 249 ? 25.437 11.847 34.256 1.00 17.28 ? 249 VAL A CB 1 ATOM 1900 C CG1 . VAL A 1 249 ? 25.881 12.289 35.656 1.00 17.84 ? 249 VAL A CG1 1 ATOM 1901 C CG2 . VAL A 1 249 ? 24.446 10.682 34.326 1.00 18.19 ? 249 VAL A CG2 1 ATOM 1902 N N . MET A 1 250 ? 25.470 15.260 34.337 1.00 17.43 ? 250 MET A N 1 ATOM 1903 C CA . MET A 1 250 ? 26.375 16.390 34.543 1.00 17.68 ? 250 MET A CA 1 ATOM 1904 C C . MET A 1 250 ? 27.123 16.267 35.858 1.00 17.57 ? 250 MET A C 1 ATOM 1905 O O . MET A 1 250 ? 26.528 15.966 36.903 1.00 17.45 ? 250 MET A O 1 ATOM 1906 C CB . MET A 1 250 ? 25.605 17.705 34.534 1.00 17.65 ? 250 MET A CB 1 ATOM 1907 C CG . MET A 1 250 ? 26.503 18.942 34.584 1.00 18.53 ? 250 MET A CG 1 ATOM 1908 S SD . MET A 1 250 ? 25.556 20.486 34.653 1.00 18.90 ? 250 MET A SD 1 ATOM 1909 C CE . MET A 1 250 ? 24.691 20.454 33.072 1.00 20.18 ? 250 MET A CE 1 ATOM 1910 N N . ILE A 1 251 ? 28.419 16.537 35.800 1.00 17.29 ? 251 ILE A N 1 ATOM 1911 C CA . ILE A 1 251 ? 29.287 16.455 36.971 1.00 18.15 ? 251 ILE A CA 1 ATOM 1912 C C . ILE A 1 251 ? 29.176 17.701 37.868 1.00 18.21 ? 251 ILE A C 1 ATOM 1913 O O . ILE A 1 251 ? 29.003 18.826 37.384 1.00 18.38 ? 251 ILE A O 1 ATOM 1914 C CB . ILE A 1 251 ? 30.756 16.180 36.540 1.00 18.79 ? 251 ILE A CB 1 ATOM 1915 C CG1 . ILE A 1 251 ? 30.820 14.939 35.633 1.00 18.75 ? 251 ILE A CG1 1 ATOM 1916 C CG2 . ILE A 1 251 ? 31.680 16.047 37.774 1.00 19.51 ? 251 ILE A CG2 1 ATOM 1917 C CD1 . ILE A 1 251 ? 30.174 13.649 36.243 1.00 19.48 ? 251 ILE A CD1 1 ATOM 1918 N N . SER A 1 252 ? 29.263 17.478 39.182 1.00 18.16 ? 252 SER A N 1 ATOM 1919 C CA . SER A 1 252 ? 29.179 18.537 40.181 1.00 18.78 ? 252 SER A CA 1 ATOM 1920 C C . SER A 1 252 ? 30.459 19.364 40.345 1.00 19.12 ? 252 SER A C 1 ATOM 1921 O O . SER A 1 252 ? 31.575 18.834 40.250 1.00 19.55 ? 252 SER A O 1 ATOM 1922 C CB . SER A 1 252 ? 28.779 17.930 41.539 1.00 18.59 ? 252 SER A CB 1 ATOM 1923 O OG . SER A 1 252 ? 28.600 18.974 42.481 1.00 19.94 ? 252 SER A OG 1 ATOM 1924 N N . TYR A 1 253 ? 30.302 20.658 40.625 1.00 19.28 ? 253 TYR A N 1 ATOM 1925 C CA . TYR A 1 253 ? 31.444 21.495 41.022 1.00 19.91 ? 253 TYR A CA 1 ATOM 1926 C C . TYR A 1 253 ? 32.041 21.012 42.351 1.00 20.37 ? 253 TYR A C 1 ATOM 1927 O O . TYR A 1 253 ? 33.214 21.266 42.668 1.00 20.84 ? 253 TYR A O 1 ATOM 1928 C CB . TYR A 1 253 ? 30.987 22.919 41.250 1.00 19.83 ? 253 TYR A CB 1 ATOM 1929 C CG . TYR A 1 253 ? 30.583 23.713 40.037 1.00 20.29 ? 253 TYR A CG 1 ATOM 1930 C CD1 . TYR A 1 253 ? 31.461 23.892 38.963 1.00 19.80 ? 253 TYR A CD1 1 ATOM 1931 C CD2 . TYR A 1 253 ? 29.346 24.358 40.004 1.00 21.23 ? 253 TYR A CD2 1 ATOM 1932 C CE1 . TYR A 1 253 ? 31.094 24.681 37.860 1.00 19.41 ? 253 TYR A CE1 1 ATOM 1933 C CE2 . TYR A 1 253 ? 28.973 25.150 38.920 1.00 21.63 ? 253 TYR A CE2 1 ATOM 1934 C CZ . TYR A 1 253 ? 29.844 25.300 37.853 1.00 20.12 ? 253 TYR A CZ 1 ATOM 1935 O OH . TYR A 1 253 ? 29.461 26.099 36.801 1.00 20.72 ? 253 TYR A OH 1 ATOM 1936 N N . SER A 1 254 ? 31.209 20.362 43.157 1.00 20.82 ? 254 SER A N 1 ATOM 1937 C CA . SER A 1 254 ? 31.598 20.018 44.524 1.00 21.79 ? 254 SER A CA 1 ATOM 1938 C C . SER A 1 254 ? 32.702 18.965 44.570 1.00 22.63 ? 254 SER A C 1 ATOM 1939 O O . SER A 1 254 ? 33.077 18.383 43.548 1.00 22.11 ? 254 SER A O 1 ATOM 1940 C CB . SER A 1 254 ? 30.365 19.586 45.343 1.00 21.48 ? 254 SER A CB 1 ATOM 1941 O OG . SER A 1 254 ? 29.707 18.463 44.778 1.00 22.07 ? 254 SER A OG 1 ATOM 1942 N N . SER A 1 255 ? 33.245 18.766 45.766 1.00 23.65 ? 255 SER A N 1 ATOM 1943 C CA . SER A 1 255 ? 34.281 17.765 45.996 1.00 24.75 ? 255 SER A CA 1 ATOM 1944 C C . SER A 1 255 ? 33.712 16.720 46.949 1.00 25.67 ? 255 SER A C 1 ATOM 1945 O O . SER A 1 255 ? 32.735 16.987 47.665 1.00 24.91 ? 255 SER A O 1 ATOM 1946 C CB . SER A 1 255 ? 35.523 18.436 46.608 1.00 24.76 ? 255 SER A CB 1 ATOM 1947 O OG . SER A 1 255 ? 36.062 19.436 45.746 1.00 25.31 ? 255 SER A OG 1 ATOM 1948 N N . TRP A 1 256 ? 34.290 15.524 46.931 1.00 26.68 ? 256 TRP A N 1 ATOM 1949 C CA . TRP A 1 256 ? 33.940 14.503 47.904 1.00 27.45 ? 256 TRP A CA 1 ATOM 1950 C C . TRP A 1 256 ? 35.206 14.185 48.684 1.00 27.94 ? 256 TRP A C 1 ATOM 1951 O O . TRP A 1 256 ? 36.186 13.699 48.100 1.00 27.17 ? 256 TRP A O 1 ATOM 1952 C CB . TRP A 1 256 ? 33.412 13.250 47.223 1.00 28.50 ? 256 TRP A CB 1 ATOM 1953 C CG . TRP A 1 256 ? 33.121 12.137 48.194 1.00 29.20 ? 256 TRP A CG 1 ATOM 1954 C CD1 . TRP A 1 256 ? 32.458 12.244 49.396 1.00 31.76 ? 256 TRP A CD1 1 ATOM 1955 C CD2 . TRP A 1 256 ? 33.460 10.751 48.042 1.00 29.86 ? 256 TRP A CD2 1 ATOM 1956 N NE1 . TRP A 1 256 ? 32.374 11.006 50.000 1.00 30.71 ? 256 TRP A NE1 1 ATOM 1957 C CE2 . TRP A 1 256 ? 32.977 10.073 49.194 1.00 30.18 ? 256 TRP A CE2 1 ATOM 1958 C CE3 . TRP A 1 256 ? 34.129 10.014 47.051 1.00 31.17 ? 256 TRP A CE3 1 ATOM 1959 C CZ2 . TRP A 1 256 ? 33.150 8.691 49.382 1.00 30.69 ? 256 TRP A CZ2 1 ATOM 1960 C CZ3 . TRP A 1 256 ? 34.298 8.637 47.233 1.00 29.53 ? 256 TRP A CZ3 1 ATOM 1961 C CH2 . TRP A 1 256 ? 33.804 7.989 48.396 1.00 30.40 ? 256 TRP A CH2 1 ATOM 1962 N N . ASN A 1 257 ? 35.187 14.495 49.983 1.00 28.55 ? 257 ASN A N 1 ATOM 1963 C CA . ASN A 1 257 ? 36.351 14.292 50.843 1.00 29.40 ? 257 ASN A CA 1 ATOM 1964 C C . ASN A 1 257 ? 37.613 14.927 50.235 1.00 29.74 ? 257 ASN A C 1 ATOM 1965 O O . ASN A 1 257 ? 38.712 14.331 50.231 1.00 30.30 ? 257 ASN A O 1 ATOM 1966 C CB . ASN A 1 257 ? 36.528 12.798 51.146 1.00 29.58 ? 257 ASN A CB 1 ATOM 1967 C CG . ASN A 1 257 ? 35.382 12.224 51.985 1.00 29.61 ? 257 ASN A CG 1 ATOM 1968 O OD1 . ASN A 1 257 ? 34.800 12.918 52.834 1.00 31.39 ? 257 ASN A OD1 1 ATOM 1969 N ND2 . ASN A 1 257 ? 35.047 10.960 51.742 1.00 28.80 ? 257 ASN A ND2 1 ATOM 1970 N N . GLY A 1 258 ? 37.430 16.135 49.700 1.00 29.09 ? 258 GLY A N 1 ATOM 1971 C CA . GLY A 1 258 ? 38.510 16.947 49.154 1.00 28.84 ? 258 GLY A CA 1 ATOM 1972 C C . GLY A 1 258 ? 38.929 16.668 47.720 1.00 28.48 ? 258 GLY A C 1 ATOM 1973 O O . GLY A 1 258 ? 39.824 17.348 47.212 1.00 29.56 ? 258 GLY A O 1 ATOM 1974 N N . VAL A 1 259 ? 38.317 15.671 47.081 1.00 27.45 ? 259 VAL A N 1 ATOM 1975 C CA . VAL A 1 259 ? 38.615 15.357 45.672 1.00 26.76 ? 259 VAL A CA 1 ATOM 1976 C C . VAL A 1 259 ? 37.540 15.987 44.783 1.00 26.10 ? 259 VAL A C 1 ATOM 1977 O O . VAL A 1 259 ? 36.356 15.656 44.913 1.00 26.19 ? 259 VAL A O 1 ATOM 1978 C CB . VAL A 1 259 ? 38.674 13.834 45.411 1.00 27.26 ? 259 VAL A CB 1 ATOM 1979 C CG1 . VAL A 1 259 ? 38.898 13.529 43.920 1.00 26.65 ? 259 VAL A CG1 1 ATOM 1980 C CG2 . VAL A 1 259 ? 39.789 13.201 46.244 1.00 27.74 ? 259 VAL A CG2 1 ATOM 1981 N N . LYS A 1 260 ? 37.965 16.880 43.889 1.00 25.07 ? 260 LYS A N 1 ATOM 1982 C CA . LYS A 1 260 ? 37.051 17.499 42.916 1.00 23.72 ? 260 LYS A CA 1 ATOM 1983 C C . LYS A 1 260 ? 36.321 16.431 42.091 1.00 23.02 ? 260 LYS A C 1 ATOM 1984 O O . LYS A 1 260 ? 36.947 15.525 41.514 1.00 21.89 ? 260 LYS A O 1 ATOM 1985 C CB . LYS A 1 260 ? 37.818 18.470 41.984 1.00 23.40 ? 260 LYS A CB 1 ATOM 1986 C CG . LYS A 1 260 ? 38.376 19.742 42.658 1.00 23.94 ? 260 LYS A CG 1 ATOM 1987 C CD . LYS A 1 260 ? 37.306 20.817 42.843 1.00 22.90 ? 260 LYS A CD 1 ATOM 1988 C CE . LYS A 1 260 ? 37.868 22.078 43.494 1.00 23.31 ? 260 LYS A CE 1 ATOM 1989 N NZ . LYS A 1 260 ? 36.850 23.177 43.644 1.00 24.11 ? 260 LYS A NZ 1 ATOM 1990 N N . MET A 1 261 ? 34.987 16.533 42.015 1.00 21.73 ? 261 MET A N 1 ATOM 1991 C CA . MET A 1 261 ? 34.217 15.605 41.192 1.00 21.62 ? 261 MET A CA 1 ATOM 1992 C C . MET A 1 261 ? 34.666 15.612 39.718 1.00 21.08 ? 261 MET A C 1 ATOM 1993 O O . MET A 1 261 ? 34.684 14.573 39.077 1.00 21.18 ? 261 MET A O 1 ATOM 1994 C CB . MET A 1 261 ? 32.712 15.916 41.272 1.00 21.29 ? 261 MET A CB 1 ATOM 1995 C CG . MET A 1 261 ? 32.025 15.428 42.562 1.00 22.58 ? 261 MET A CG 1 ATOM 1996 S SD . MET A 1 261 ? 32.205 13.656 42.903 1.00 24.69 ? 261 MET A SD 1 ATOM 1997 C CE . MET A 1 261 ? 31.928 12.869 41.311 1.00 24.47 ? 261 MET A CE 1 ATOM 1998 N N . HIS A 1 262 ? 35.022 16.785 39.199 1.00 21.14 ? 262 HIS A N 1 ATOM 1999 C CA . HIS A 1 262 ? 35.453 16.916 37.797 1.00 20.96 ? 262 HIS A CA 1 ATOM 2000 C C . HIS A 1 262 ? 36.796 16.225 37.519 1.00 21.87 ? 262 HIS A C 1 ATOM 2001 O O . HIS A 1 262 ? 37.179 16.078 36.360 1.00 22.09 ? 262 HIS A O 1 ATOM 2002 C CB . HIS A 1 262 ? 35.499 18.380 37.355 1.00 20.63 ? 262 HIS A CB 1 ATOM 2003 C CG . HIS A 1 262 ? 34.151 18.960 37.085 1.00 20.28 ? 262 HIS A CG 1 ATOM 2004 N ND1 . HIS A 1 262 ? 33.675 19.198 35.807 1.00 20.82 ? 262 HIS A ND1 1 ATOM 2005 C CD2 . HIS A 1 262 ? 33.171 19.350 37.934 1.00 17.55 ? 262 HIS A CD2 1 ATOM 2006 C CE1 . HIS A 1 262 ? 32.447 19.691 35.885 1.00 16.96 ? 262 HIS A CE1 1 ATOM 2007 N NE2 . HIS A 1 262 ? 32.119 19.797 37.162 1.00 21.61 ? 262 HIS A NE2 1 ATOM 2008 N N . ALA A 1 263 ? 37.478 15.786 38.584 1.00 22.10 ? 263 ALA A N 1 ATOM 2009 C CA . ALA A 1 263 ? 38.767 15.071 38.468 1.00 22.95 ? 263 ALA A CA 1 ATOM 2010 C C . ALA A 1 263 ? 38.733 13.639 39.039 1.00 23.48 ? 263 ALA A C 1 ATOM 2011 O O . ALA A 1 263 ? 39.775 12.950 39.138 1.00 24.74 ? 263 ALA A O 1 ATOM 2012 C CB . ALA A 1 263 ? 39.884 15.897 39.115 1.00 23.11 ? 263 ALA A CB 1 ATOM 2013 N N . ASN A 1 264 ? 37.538 13.169 39.380 1.00 23.17 ? 264 ASN A N 1 ATOM 2014 C CA . ASN A 1 264 ? 37.397 11.903 40.093 1.00 23.28 ? 264 ASN A CA 1 ATOM 2015 C C . ASN A 1 264 ? 37.145 10.708 39.195 1.00 23.04 ? 264 ASN A C 1 ATOM 2016 O O . ASN A 1 264 ? 36.005 10.354 38.901 1.00 23.19 ? 264 ASN A O 1 ATOM 2017 C CB . ASN A 1 264 ? 36.338 11.995 41.207 1.00 23.28 ? 264 ASN A CB 1 ATOM 2018 C CG . ASN A 1 264 ? 36.466 10.853 42.213 1.00 24.62 ? 264 ASN A CG 1 ATOM 2019 O OD1 . ASN A 1 264 ? 36.819 9.723 41.846 1.00 25.51 ? 264 ASN A OD1 1 ATOM 2020 N ND2 . ASN A 1 264 ? 36.205 11.146 43.478 1.00 25.69 ? 264 ASN A ND2 1 ATOM 2021 N N . GLN A 1 265 ? 38.237 10.077 38.763 1.00 23.95 ? 265 GLN A N 1 ATOM 2022 C CA . GLN A 1 265 ? 38.150 8.918 37.891 1.00 23.97 ? 265 GLN A CA 1 ATOM 2023 C C . GLN A 1 265 ? 37.433 7.746 38.551 1.00 24.04 ? 265 GLN A C 1 ATOM 2024 O O . GLN A 1 265 ? 36.662 7.025 37.895 1.00 23.54 ? 265 GLN A O 1 ATOM 2025 C CB . GLN A 1 265 ? 39.553 8.516 37.420 1.00 24.59 ? 265 GLN A CB 1 ATOM 2026 C CG . GLN A 1 265 ? 39.554 7.465 36.344 1.00 27.03 ? 265 GLN A CG 1 ATOM 2027 C CD . GLN A 1 265 ? 40.974 7.072 35.975 1.00 31.66 ? 265 GLN A CD 1 ATOM 2028 O OE1 . GLN A 1 265 ? 41.556 7.592 35.028 1.00 35.66 ? 265 GLN A OE1 1 ATOM 2029 N NE2 . GLN A 1 265 ? 41.545 6.181 36.755 1.00 34.78 ? 265 GLN A NE2 1 ATOM 2030 N N . ASP A 1 266 ? 37.669 7.560 39.852 1.00 24.68 ? 266 ASP A N 1 ATOM 2031 C CA . ASP A 1 266 ? 37.056 6.454 40.576 1.00 25.59 ? 266 ASP A CA 1 ATOM 2032 C C . ASP A 1 266 ? 35.529 6.512 40.502 1.00 24.49 ? 266 ASP A C 1 ATOM 2033 O O . ASP A 1 266 ? 34.869 5.509 40.245 1.00 24.47 ? 266 ASP A O 1 ATOM 2034 C CB . ASP A 1 266 ? 37.501 6.455 42.049 1.00 26.85 ? 266 ASP A CB 1 ATOM 2035 C CG . ASP A 1 266 ? 38.942 6.009 42.235 1.00 31.70 ? 266 ASP A CG 1 ATOM 2036 O OD1 . ASP A 1 266 ? 39.499 6.267 43.334 1.00 37.06 ? 266 ASP A OD1 1 ATOM 2037 O OD2 . ASP A 1 266 ? 39.524 5.394 41.304 1.00 36.59 ? 266 ASP A OD2 1 ATOM 2038 N N . LEU A 1 267 ? 34.972 7.703 40.701 1.00 24.08 ? 267 LEU A N 1 ATOM 2039 C CA . LEU A 1 267 ? 33.522 7.845 40.692 1.00 23.43 ? 267 LEU A CA 1 ATOM 2040 C C . LEU A 1 267 ? 32.945 7.977 39.278 1.00 22.69 ? 267 LEU A C 1 ATOM 2041 O O . LEU A 1 267 ? 31.952 7.341 38.966 1.00 22.63 ? 267 LEU A O 1 ATOM 2042 C CB . LEU A 1 267 ? 33.081 9.019 41.581 1.00 23.74 ? 267 LEU A CB 1 ATOM 2043 C CG . LEU A 1 267 ? 33.117 8.794 43.100 1.00 24.73 ? 267 LEU A CG 1 ATOM 2044 C CD1 . LEU A 1 267 ? 32.613 10.014 43.814 1.00 25.47 ? 267 LEU A CD1 1 ATOM 2045 C CD2 . LEU A 1 267 ? 32.295 7.564 43.489 1.00 27.00 ? 267 LEU A CD2 1 ATOM 2046 N N . VAL A 1 268 ? 33.584 8.767 38.416 1.00 22.59 ? 268 VAL A N 1 ATOM 2047 C CA . VAL A 1 268 ? 32.997 9.009 37.077 1.00 22.19 ? 268 VAL A CA 1 ATOM 2048 C C . VAL A 1 268 ? 33.176 7.775 36.192 1.00 22.61 ? 268 VAL A C 1 ATOM 2049 O O . VAL A 1 268 ? 32.224 7.289 35.580 1.00 22.44 ? 268 VAL A O 1 ATOM 2050 C CB . VAL A 1 268 ? 33.588 10.282 36.407 1.00 21.96 ? 268 VAL A CB 1 ATOM 2051 C CG1 . VAL A 1 268 ? 33.066 10.439 34.965 1.00 22.09 ? 268 VAL A CG1 1 ATOM 2052 C CG2 . VAL A 1 268 ? 33.284 11.521 37.241 1.00 22.62 ? 268 VAL A CG2 1 ATOM 2053 N N . THR A 1 269 ? 34.399 7.239 36.152 1.00 22.70 ? 269 THR A N 1 ATOM 2054 C CA . THR A 1 269 ? 34.645 6.047 35.343 1.00 23.43 ? 269 THR A CA 1 ATOM 2055 C C . THR A 1 269 ? 34.380 4.751 36.114 1.00 23.60 ? 269 THR A C 1 ATOM 2056 O O . THR A 1 269 ? 33.626 3.898 35.645 1.00 23.23 ? 269 THR A O 1 ATOM 2057 C CB . THR A 1 269 ? 36.062 6.059 34.705 1.00 23.54 ? 269 THR A CB 1 ATOM 2058 O OG1 . THR A 1 269 ? 36.191 7.221 33.862 1.00 24.42 ? 269 THR A OG1 1 ATOM 2059 C CG2 . THR A 1 269 ? 36.288 4.802 33.861 1.00 24.59 ? 269 THR A CG2 1 ATOM 2060 N N . GLY A 1 270 ? 34.985 4.611 37.289 1.00 24.29 ? 270 GLY A N 1 ATOM 2061 C CA . GLY A 1 270 ? 34.850 3.368 38.076 1.00 25.31 ? 270 GLY A CA 1 ATOM 2062 C C . GLY A 1 270 ? 33.422 3.041 38.484 1.00 26.02 ? 270 GLY A C 1 ATOM 2063 O O . GLY A 1 270 ? 32.979 1.881 38.394 1.00 27.45 ? 270 GLY A O 1 ATOM 2064 N N . TYR A 1 271 ? 32.685 4.066 38.913 1.00 25.34 ? 271 TYR A N 1 ATOM 2065 C CA . TYR A 1 271 ? 31.332 3.834 39.399 1.00 25.33 ? 271 TYR A CA 1 ATOM 2066 C C . TYR A 1 271 ? 30.250 4.104 38.347 1.00 24.41 ? 271 TYR A C 1 ATOM 2067 O O . TYR A 1 271 ? 29.513 3.193 37.955 1.00 24.30 ? 271 TYR A O 1 ATOM 2068 C CB . TYR A 1 271 ? 31.060 4.592 40.704 1.00 26.62 ? 271 TYR A CB 1 ATOM 2069 C CG . TYR A 1 271 ? 29.854 4.029 41.421 1.00 27.93 ? 271 TYR A CG 1 ATOM 2070 C CD1 . TYR A 1 271 ? 29.956 2.856 42.174 1.00 28.91 ? 271 TYR A CD1 1 ATOM 2071 C CD2 . TYR A 1 271 ? 28.598 4.639 41.311 1.00 28.12 ? 271 TYR A CD2 1 ATOM 2072 C CE1 . TYR A 1 271 ? 28.854 2.313 42.801 1.00 29.10 ? 271 TYR A CE1 1 ATOM 2073 C CE2 . TYR A 1 271 ? 27.479 4.104 41.949 1.00 29.19 ? 271 TYR A CE2 1 ATOM 2074 C CZ . TYR A 1 271 ? 27.621 2.939 42.696 1.00 29.16 ? 271 TYR A CZ 1 ATOM 2075 O OH . TYR A 1 271 ? 26.532 2.387 43.332 1.00 30.54 ? 271 TYR A OH 1 ATOM 2076 N N . LEU A 1 272 ? 30.165 5.343 37.876 1.00 23.10 ? 272 LEU A N 1 ATOM 2077 C CA . LEU A 1 272 ? 29.081 5.699 36.979 1.00 22.48 ? 272 LEU A CA 1 ATOM 2078 C C . LEU A 1 272 ? 29.131 4.861 35.705 1.00 22.56 ? 272 LEU A C 1 ATOM 2079 O O . LEU A 1 272 ? 28.143 4.213 35.336 1.00 21.56 ? 272 LEU A O 1 ATOM 2080 C CB . LEU A 1 272 ? 29.102 7.195 36.669 1.00 22.08 ? 272 LEU A CB 1 ATOM 2081 C CG . LEU A 1 272 ? 28.052 7.717 35.685 1.00 21.52 ? 272 LEU A CG 1 ATOM 2082 C CD1 . LEU A 1 272 ? 26.615 7.478 36.149 1.00 21.84 ? 272 LEU A CD1 1 ATOM 2083 C CD2 . LEU A 1 272 ? 28.366 9.190 35.474 1.00 21.14 ? 272 LEU A CD2 1 ATOM 2084 N N . LYS A 1 273 ? 30.292 4.852 35.040 1.00 22.28 ? 273 LYS A N 1 ATOM 2085 C CA . LYS A 1 273 ? 30.394 4.122 33.786 1.00 23.07 ? 273 LYS A CA 1 ATOM 2086 C C . LYS A 1 273 ? 30.538 2.614 34.009 1.00 24.43 ? 273 LYS A C 1 ATOM 2087 O O . LYS A 1 273 ? 29.800 1.831 33.417 1.00 24.55 ? 273 LYS A O 1 ATOM 2088 C CB . LYS A 1 273 ? 31.524 4.675 32.911 1.00 22.57 ? 273 LYS A CB 1 ATOM 2089 C CG . LYS A 1 273 ? 31.256 6.106 32.395 1.00 21.97 ? 273 LYS A CG 1 ATOM 2090 C CD . LYS A 1 273 ? 32.344 6.548 31.427 1.00 22.23 ? 273 LYS A CD 1 ATOM 2091 C CE . LYS A 1 273 ? 31.964 7.859 30.696 1.00 22.19 ? 273 LYS A CE 1 ATOM 2092 N NZ . LYS A 1 273 ? 33.045 8.208 29.721 1.00 21.71 ? 273 LYS A NZ 1 ATOM 2093 N N . ASP A 1 274 ? 31.458 2.215 34.885 1.00 25.90 ? 274 ASP A N 1 ATOM 2094 C CA . ASP A 1 274 ? 31.842 0.790 34.977 1.00 27.15 ? 274 ASP A CA 1 ATOM 2095 C C . ASP A 1 274 ? 30.991 -0.059 35.917 1.00 27.90 ? 274 ASP A C 1 ATOM 2096 O O . ASP A 1 274 ? 30.974 -1.288 35.779 1.00 29.38 ? 274 ASP A O 1 ATOM 2097 C CB . ASP A 1 274 ? 33.317 0.638 35.375 1.00 27.46 ? 274 ASP A CB 1 ATOM 2098 C CG . ASP A 1 274 ? 34.291 1.089 34.288 1.00 28.88 ? 274 ASP A CG 1 ATOM 2099 O OD1 . ASP A 1 274 ? 33.877 1.344 33.141 1.00 31.57 ? 274 ASP A OD1 1 ATOM 2100 O OD2 . ASP A 1 274 ? 35.497 1.187 34.598 1.00 31.34 ? 274 ASP A OD2 1 ATOM 2101 N N . THR A 1 275 ? 30.328 0.573 36.884 1.00 26.96 ? 275 THR A N 1 ATOM 2102 C CA . THR A 1 275 ? 29.508 -0.157 37.866 1.00 27.14 ? 275 THR A CA 1 ATOM 2103 C C . THR A 1 275 ? 28.021 0.003 37.540 1.00 27.20 ? 275 THR A C 1 ATOM 2104 O O . THR A 1 275 ? 27.294 -0.994 37.404 1.00 28.31 ? 275 THR A O 1 ATOM 2105 C CB . THR A 1 275 ? 29.842 0.270 39.328 1.00 27.07 ? 275 THR A CB 1 ATOM 2106 O OG1 . THR A 1 275 ? 31.247 0.096 39.574 1.00 27.61 ? 275 THR A OG1 1 ATOM 2107 C CG2 . THR A 1 275 ? 29.038 -0.563 40.363 1.00 28.02 ? 275 THR A CG2 1 ATOM 2108 N N . LEU A 1 276 ? 27.579 1.251 37.362 1.00 26.58 ? 276 LEU A N 1 ATOM 2109 C CA . LEU A 1 276 ? 26.190 1.527 36.955 1.00 25.93 ? 276 LEU A CA 1 ATOM 2110 C C . LEU A 1 276 ? 25.924 1.271 35.466 1.00 25.65 ? 276 LEU A C 1 ATOM 2111 O O . LEU A 1 276 ? 24.773 1.280 35.029 1.00 25.15 ? 276 LEU A O 1 ATOM 2112 C CB . LEU A 1 276 ? 25.795 2.962 37.322 1.00 26.26 ? 276 LEU A CB 1 ATOM 2113 C CG . LEU A 1 276 ? 25.795 3.313 38.809 1.00 26.83 ? 276 LEU A CG 1 ATOM 2114 C CD1 . LEU A 1 276 ? 25.307 4.751 39.006 1.00 25.97 ? 276 LEU A CD1 1 ATOM 2115 C CD2 . LEU A 1 276 ? 24.940 2.312 39.612 1.00 28.62 ? 276 LEU A CD2 1 ATOM 2116 N N . LYS A 1 277 ? 26.995 1.045 34.696 1.00 24.88 ? 277 LYS A N 1 ATOM 2117 C CA . LYS A 1 277 ? 26.906 0.728 33.259 1.00 24.92 ? 277 LYS A CA 1 ATOM 2118 C C . LYS A 1 277 ? 26.262 1.880 32.477 1.00 23.54 ? 277 LYS A C 1 ATOM 2119 O O . LYS A 1 277 ? 25.544 1.668 31.500 1.00 23.64 ? 277 LYS A O 1 ATOM 2120 C CB . LYS A 1 277 ? 26.158 -0.592 33.010 1.00 27.31 ? 277 LYS A CB 1 ATOM 2121 C CG . LYS A 1 277 ? 26.727 -1.793 33.784 1.00 27.28 ? 277 LYS A CG 1 ATOM 2122 C CD . LYS A 1 277 ? 28.186 -2.025 33.412 1.00 33.29 ? 277 LYS A CD 1 ATOM 2123 C CE . LYS A 1 277 ? 28.797 -3.219 34.169 1.00 27.38 ? 277 LYS A CE 1 ATOM 2124 N NZ . LYS A 1 277 ? 30.279 -3.307 33.920 1.00 34.83 ? 277 LYS A NZ 1 ATOM 2125 N N . PHE A 1 278 ? 26.531 3.106 32.913 1.00 23.14 ? 278 PHE A N 1 ATOM 2126 C CA . PHE A 1 278 ? 26.011 4.260 32.187 1.00 22.07 ? 278 PHE A CA 1 ATOM 2127 C C . PHE A 1 278 ? 26.635 4.307 30.796 1.00 21.88 ? 278 PHE A C 1 ATOM 2128 O O . PHE A 1 278 ? 27.870 4.345 30.678 1.00 22.19 ? 278 PHE A O 1 ATOM 2129 C CB . PHE A 1 278 ? 26.314 5.546 32.923 1.00 21.73 ? 278 PHE A CB 1 ATOM 2130 C CG . PHE A 1 278 ? 25.802 6.778 32.212 1.00 20.78 ? 278 PHE A CG 1 ATOM 2131 C CD1 . PHE A 1 278 ? 24.454 6.876 31.839 1.00 20.70 ? 278 PHE A CD1 1 ATOM 2132 C CD2 . PHE A 1 278 ? 26.662 7.830 31.929 1.00 20.47 ? 278 PHE A CD2 1 ATOM 2133 C CE1 . PHE A 1 278 ? 23.962 8.036 31.177 1.00 19.20 ? 278 PHE A CE1 1 ATOM 2134 C CE2 . PHE A 1 278 ? 26.190 8.995 31.280 1.00 19.94 ? 278 PHE A CE2 1 ATOM 2135 C CZ . PHE A 1 278 ? 24.848 9.095 30.908 1.00 20.74 ? 278 PHE A CZ 1 ATOM 2136 N N . LYS A 1 279 ? 25.780 4.325 29.775 1.00 21.73 ? 279 LYS A N 1 ATOM 2137 C CA . LYS A 1 279 ? 26.216 4.369 28.357 1.00 21.67 ? 279 LYS A CA 1 ATOM 2138 C C . LYS A 1 279 ? 25.865 5.665 27.617 1.00 21.07 ? 279 LYS A C 1 ATOM 2139 O O . LYS A 1 279 ? 26.121 5.775 26.404 1.00 21.09 ? 279 LYS A O 1 ATOM 2140 C CB . LYS A 1 279 ? 25.641 3.179 27.580 1.00 22.27 ? 279 LYS A CB 1 ATOM 2141 C CG . LYS A 1 279 ? 25.968 1.799 28.151 1.00 24.99 ? 279 LYS A CG 1 ATOM 2142 C CD . LYS A 1 279 ? 27.432 1.485 28.115 1.00 27.97 ? 279 LYS A CD 1 ATOM 2143 C CE . LYS A 1 279 ? 27.659 0.032 28.569 1.00 30.87 ? 279 LYS A CE 1 ATOM 2144 N NZ . LYS A 1 279 ? 29.087 -0.147 28.946 1.00 32.51 ? 279 LYS A NZ 1 ATOM 2145 N N . GLY A 1 280 ? 25.271 6.641 28.315 1.00 20.92 ? 280 GLY A N 1 ATOM 2146 C CA . GLY A 1 280 ? 25.058 7.949 27.689 1.00 20.13 ? 280 GLY A CA 1 ATOM 2147 C C . GLY A 1 280 ? 26.342 8.756 27.829 1.00 19.75 ? 280 GLY A C 1 ATOM 2148 O O . GLY A 1 280 ? 27.415 8.194 28.067 1.00 19.90 ? 280 GLY A O 1 ATOM 2149 N N . PHE A 1 281 ? 26.248 10.069 27.680 1.00 19.37 ? 281 PHE A N 1 ATOM 2150 C CA . PHE A 1 281 ? 27.429 10.908 27.865 1.00 19.01 ? 281 PHE A CA 1 ATOM 2151 C C . PHE A 1 281 ? 27.442 11.729 29.137 1.00 18.94 ? 281 PHE A C 1 ATOM 2152 O O . PHE A 1 281 ? 26.385 12.159 29.632 1.00 18.52 ? 281 PHE A O 1 ATOM 2153 C CB . PHE A 1 281 ? 27.801 11.732 26.614 1.00 19.25 ? 281 PHE A CB 1 ATOM 2154 C CG . PHE A 1 281 ? 26.889 12.917 26.292 1.00 18.11 ? 281 PHE A CG 1 ATOM 2155 C CD1 . PHE A 1 281 ? 27.015 14.142 26.963 1.00 18.55 ? 281 PHE A CD1 1 ATOM 2156 C CD2 . PHE A 1 281 ? 25.952 12.818 25.249 1.00 18.81 ? 281 PHE A CD2 1 ATOM 2157 C CE1 . PHE A 1 281 ? 26.205 15.255 26.636 1.00 18.44 ? 281 PHE A CE1 1 ATOM 2158 C CE2 . PHE A 1 281 ? 25.156 13.934 24.877 1.00 19.30 ? 281 PHE A CE2 1 ATOM 2159 C CZ . PHE A 1 281 ? 25.273 15.156 25.576 1.00 19.12 ? 281 PHE A CZ 1 ATOM 2160 N N . VAL A 1 282 ? 28.660 11.948 29.625 1.00 18.23 ? 282 VAL A N 1 ATOM 2161 C CA . VAL A 1 282 ? 28.921 12.692 30.835 1.00 18.07 ? 282 VAL A CA 1 ATOM 2162 C C . VAL A 1 282 ? 29.399 14.084 30.444 1.00 18.16 ? 282 VAL A C 1 ATOM 2163 O O . VAL A 1 282 ? 30.393 14.232 29.697 1.00 18.40 ? 282 VAL A O 1 ATOM 2164 C CB . VAL A 1 282 ? 30.006 11.981 31.678 1.00 18.05 ? 282 VAL A CB 1 ATOM 2165 C CG1 . VAL A 1 282 ? 30.346 12.806 32.903 1.00 18.34 ? 282 VAL A CG1 1 ATOM 2166 C CG2 . VAL A 1 282 ? 29.551 10.551 32.043 1.00 19.13 ? 282 VAL A CG2 1 ATOM 2167 N N . ILE A 1 283 ? 28.701 15.105 30.942 1.00 17.31 ? 283 ILE A N 1 ATOM 2168 C CA . ILE A 1 283 ? 29.037 16.480 30.603 1.00 16.39 ? 283 ILE A CA 1 ATOM 2169 C C . ILE A 1 283 ? 29.564 17.223 31.838 1.00 16.76 ? 283 ILE A C 1 ATOM 2170 O O . ILE A 1 283 ? 29.080 16.985 32.960 1.00 16.33 ? 283 ILE A O 1 ATOM 2171 C CB . ILE A 1 283 ? 27.816 17.203 29.949 1.00 16.39 ? 283 ILE A CB 1 ATOM 2172 C CG1 . ILE A 1 283 ? 28.212 18.604 29.448 1.00 15.44 ? 283 ILE A CG1 1 ATOM 2173 C CG2 . ILE A 1 283 ? 26.601 17.233 30.933 1.00 15.69 ? 283 ILE A CG2 1 ATOM 2174 C CD1 . ILE A 1 283 ? 27.114 19.273 28.598 1.00 16.45 ? 283 ILE A CD1 1 ATOM 2175 N N . SER A 1 284 ? 30.543 18.114 31.637 1.00 17.01 ? 284 SER A N 1 ATOM 2176 C CA . SER A 1 284 ? 31.004 18.990 32.724 1.00 16.60 ? 284 SER A CA 1 ATOM 2177 C C . SER A 1 284 ? 29.924 20.010 33.089 1.00 16.57 ? 284 SER A C 1 ATOM 2178 O O . SER A 1 284 ? 28.980 20.240 32.313 1.00 16.81 ? 284 SER A O 1 ATOM 2179 C CB . SER A 1 284 ? 32.287 19.752 32.341 1.00 16.71 ? 284 SER A CB 1 ATOM 2180 O OG . SER A 1 284 ? 32.016 20.903 31.551 1.00 17.35 ? 284 SER A OG 1 ATOM 2181 N N . ASP A 1 285 ? 30.091 20.649 34.238 1.00 17.49 ? 285 ASP A N 1 ATOM 2182 C CA . ASP A 1 285 ? 29.334 21.853 34.536 1.00 17.44 ? 285 ASP A CA 1 ATOM 2183 C C . ASP A 1 285 ? 30.083 23.043 33.902 1.00 18.08 ? 285 ASP A C 1 ATOM 2184 O O . ASP A 1 285 ? 31.151 22.862 33.289 1.00 18.28 ? 285 ASP A O 1 ATOM 2185 C CB . ASP A 1 285 ? 29.097 22.007 36.055 1.00 18.40 ? 285 ASP A CB 1 ATOM 2186 C CG . ASP A 1 285 ? 27.838 22.815 36.380 1.00 19.32 ? 285 ASP A CG 1 ATOM 2187 O OD1 . ASP A 1 285 ? 27.359 23.602 35.517 1.00 19.03 ? 285 ASP A OD1 1 ATOM 2188 O OD2 . ASP A 1 285 ? 27.302 22.657 37.505 1.00 20.56 ? 285 ASP A OD2 1 ATOM 2189 N N . TRP A 1 286 ? 29.499 24.230 34.016 1.00 17.92 ? 286 TRP A N 1 ATOM 2190 C CA . TRP A 1 286 ? 29.941 25.453 33.338 1.00 18.32 ? 286 TRP A CA 1 ATOM 2191 C C . TRP A 1 286 ? 31.285 25.898 33.915 1.00 18.89 ? 286 TRP A C 1 ATOM 2192 O O . TRP A 1 286 ? 31.364 26.327 35.083 1.00 19.27 ? 286 TRP A O 1 ATOM 2193 C CB . TRP A 1 286 ? 28.871 26.517 33.596 1.00 18.85 ? 286 TRP A CB 1 ATOM 2194 C CG . TRP A 1 286 ? 29.128 27.938 33.159 1.00 19.72 ? 286 TRP A CG 1 ATOM 2195 C CD1 . TRP A 1 286 ? 29.935 28.862 33.763 1.00 20.97 ? 286 TRP A CD1 1 ATOM 2196 C CD2 . TRP A 1 286 ? 28.480 28.615 32.077 1.00 19.27 ? 286 TRP A CD2 1 ATOM 2197 N NE1 . TRP A 1 286 ? 29.861 30.065 33.101 1.00 21.13 ? 286 TRP A NE1 1 ATOM 2198 C CE2 . TRP A 1 286 ? 28.970 29.944 32.060 1.00 20.35 ? 286 TRP A CE2 1 ATOM 2199 C CE3 . TRP A 1 286 ? 27.542 28.216 31.105 1.00 19.16 ? 286 TRP A CE3 1 ATOM 2200 C CZ2 . TRP A 1 286 ? 28.548 30.891 31.104 1.00 20.65 ? 286 TRP A CZ2 1 ATOM 2201 C CZ3 . TRP A 1 286 ? 27.111 29.159 30.152 1.00 20.29 ? 286 TRP A CZ3 1 ATOM 2202 C CH2 . TRP A 1 286 ? 27.621 30.480 30.160 1.00 19.99 ? 286 TRP A CH2 1 ATOM 2203 N N . GLU A 1 287 ? 32.341 25.792 33.109 1.00 19.13 ? 287 GLU A N 1 ATOM 2204 C CA . GLU A 1 287 ? 33.723 26.061 33.595 1.00 20.31 ? 287 GLU A CA 1 ATOM 2205 C C . GLU A 1 287 ? 34.074 25.132 34.758 1.00 19.61 ? 287 GLU A C 1 ATOM 2206 O O . GLU A 1 287 ? 34.939 25.456 35.597 1.00 19.91 ? 287 GLU A O 1 ATOM 2207 C CB . GLU A 1 287 ? 33.920 27.529 34.027 1.00 20.74 ? 287 GLU A CB 1 ATOM 2208 C CG . GLU A 1 287 ? 33.633 28.583 32.935 1.00 22.57 ? 287 GLU A CG 1 ATOM 2209 C CD . GLU A 1 287 ? 33.602 30.027 33.459 1.00 23.80 ? 287 GLU A CD 1 ATOM 2210 O OE1 . GLU A 1 287 ? 33.532 30.265 34.695 1.00 27.27 ? 287 GLU A OE1 1 ATOM 2211 O OE2 . GLU A 1 287 ? 33.617 30.943 32.615 1.00 27.65 ? 287 GLU A OE2 1 ATOM 2212 N N . GLY A 1 288 ? 33.416 23.978 34.804 1.00 19.31 ? 288 GLY A N 1 ATOM 2213 C CA . GLY A 1 288 ? 33.662 22.998 35.871 1.00 19.65 ? 288 GLY A CA 1 ATOM 2214 C C . GLY A 1 288 ? 35.108 22.513 35.886 1.00 20.41 ? 288 GLY A C 1 ATOM 2215 O O . GLY A 1 288 ? 35.705 22.365 36.965 1.00 20.68 ? 288 GLY A O 1 ATOM 2216 N N . ILE A 1 289 ? 35.687 22.272 34.705 1.00 19.87 ? 289 ILE A N 1 ATOM 2217 C CA . ILE A 1 289 ? 37.077 21.809 34.671 1.00 20.39 ? 289 ILE A CA 1 ATOM 2218 C C . ILE A 1 289 ? 38.041 22.907 35.128 1.00 20.78 ? 289 ILE A C 1 ATOM 2219 O O . ILE A 1 289 ? 39.036 22.595 35.799 1.00 20.90 ? 289 ILE A O 1 ATOM 2220 C CB . ILE A 1 289 ? 37.482 21.136 33.315 1.00 20.39 ? 289 ILE A CB 1 ATOM 2221 C CG1 . ILE A 1 289 ? 37.759 22.178 32.213 1.00 20.02 ? 289 ILE A CG1 1 ATOM 2222 C CG2 . ILE A 1 289 ? 36.406 20.137 32.882 1.00 19.86 ? 289 ILE A CG2 1 ATOM 2223 C CD1 . ILE A 1 289 ? 38.427 21.552 30.951 1.00 20.68 ? 289 ILE A CD1 1 ATOM 2224 N N . ASP A 1 290 ? 37.721 24.172 34.823 1.00 21.05 ? 290 ASP A N 1 ATOM 2225 C CA . ASP A 1 290 ? 38.516 25.343 35.275 1.00 21.75 ? 290 ASP A CA 1 ATOM 2226 C C . ASP A 1 290 ? 38.619 25.360 36.794 1.00 22.63 ? 290 ASP A C 1 ATOM 2227 O O . ASP A 1 290 ? 39.677 25.700 37.378 1.00 23.01 ? 290 ASP A O 1 ATOM 2228 C CB . ASP A 1 290 ? 37.854 26.667 34.854 1.00 22.00 ? 290 ASP A CB 1 ATOM 2229 C CG . ASP A 1 290 ? 37.500 26.719 33.369 1.00 22.55 ? 290 ASP A CG 1 ATOM 2230 O OD1 . ASP A 1 290 ? 36.862 25.778 32.869 1.00 24.24 ? 290 ASP A OD1 1 ATOM 2231 O OD2 . ASP A 1 290 ? 37.839 27.725 32.715 1.00 23.83 ? 290 ASP A OD2 1 ATOM 2232 N N . ARG A 1 291 ? 37.512 24.990 37.429 1.00 22.02 ? 291 ARG A N 1 ATOM 2233 C CA . ARG A 1 291 ? 37.374 25.129 38.882 1.00 23.03 ? 291 ARG A CA 1 ATOM 2234 C C . ARG A 1 291 ? 37.994 23.974 39.658 1.00 23.74 ? 291 ARG A C 1 ATOM 2235 O O . ARG A 1 291 ? 37.917 23.931 40.904 1.00 24.50 ? 291 ARG A O 1 ATOM 2236 C CB . ARG A 1 291 ? 35.906 25.370 39.247 1.00 22.58 ? 291 ARG A CB 1 ATOM 2237 C CG . ARG A 1 291 ? 35.414 26.694 38.662 1.00 21.94 ? 291 ARG A CG 1 ATOM 2238 C CD . ARG A 1 291 ? 33.961 27.002 39.012 1.00 23.23 ? 291 ARG A CD 1 ATOM 2239 N NE . ARG A 1 291 ? 33.442 28.028 38.105 1.00 23.30 ? 291 ARG A NE 1 ATOM 2240 C CZ . ARG A 1 291 ? 32.190 28.475 38.107 1.00 25.06 ? 291 ARG A CZ 1 ATOM 2241 N NH1 . ARG A 1 291 ? 31.311 28.008 39.001 1.00 24.17 ? 291 ARG A NH1 1 ATOM 2242 N NH2 . ARG A 1 291 ? 31.816 29.389 37.205 1.00 24.46 ? 291 ARG A NH2 1 ATOM 2243 N N . ILE A 1 292 ? 38.630 23.050 38.940 1.00 24.24 ? 292 ILE A N 1 ATOM 2244 C CA . ILE A 1 292 ? 39.407 21.976 39.578 1.00 25.48 ? 292 ILE A CA 1 ATOM 2245 C C . ILE A 1 292 ? 40.570 22.600 40.360 1.00 26.34 ? 292 ILE A C 1 ATOM 2246 O O . ILE A 1 292 ? 40.934 22.118 41.451 1.00 26.70 ? 292 ILE A O 1 ATOM 2247 C CB . ILE A 1 292 ? 39.935 20.961 38.530 1.00 25.37 ? 292 ILE A CB 1 ATOM 2248 C CG1 . ILE A 1 292 ? 38.787 20.097 38.004 1.00 24.28 ? 292 ILE A CG1 1 ATOM 2249 C CG2 . ILE A 1 292 ? 41.057 20.070 39.103 1.00 25.27 ? 292 ILE A CG2 1 ATOM 2250 C CD1 . ILE A 1 292 ? 39.124 19.320 36.708 1.00 24.85 ? 292 ILE A CD1 1 ATOM 2251 N N . THR A 1 293 ? 41.128 23.676 39.804 1.00 26.90 ? 293 THR A N 1 ATOM 2252 C CA . THR A 1 293 ? 42.305 24.339 40.385 1.00 27.80 ? 293 THR A CA 1 ATOM 2253 C C . THR A 1 293 ? 41.907 25.547 41.225 1.00 28.93 ? 293 THR A C 1 ATOM 2254 O O . THR A 1 293 ? 40.796 26.072 41.093 1.00 28.61 ? 293 THR A O 1 ATOM 2255 C CB . THR A 1 293 ? 43.285 24.800 39.270 1.00 27.02 ? 293 THR A CB 1 ATOM 2256 O OG1 . THR A 1 293 ? 42.638 25.777 38.452 1.00 26.63 ? 293 THR A OG1 1 ATOM 2257 C CG2 . THR A 1 293 ? 43.741 23.608 38.403 1.00 26.61 ? 293 THR A CG2 1 ATOM 2258 N N . THR A 1 294 ? 42.818 25.977 42.106 1.00 30.69 ? 294 THR A N 1 ATOM 2259 C CA . THR A 1 294 ? 42.687 27.236 42.844 1.00 32.58 ? 294 THR A CA 1 ATOM 2260 C C . THR A 1 294 ? 43.949 28.054 42.569 1.00 32.85 ? 294 THR A C 1 ATOM 2261 O O . THR A 1 294 ? 45.049 27.563 42.814 1.00 33.55 ? 294 THR A O 1 ATOM 2262 C CB . THR A 1 294 ? 42.583 27.019 44.380 1.00 33.10 ? 294 THR A CB 1 ATOM 2263 O OG1 . THR A 1 294 ? 41.540 26.078 44.680 1.00 34.67 ? 294 THR A OG1 1 ATOM 2264 C CG2 . THR A 1 294 ? 42.297 28.343 45.083 1.00 34.26 ? 294 THR A CG2 1 ATOM 2265 N N . PRO A 1 295 ? 43.805 29.272 42.009 1.00 32.81 ? 295 PRO A N 1 ATOM 2266 C CA . PRO A 1 295 ? 42.554 29.860 41.540 1.00 32.47 ? 295 PRO A CA 1 ATOM 2267 C C . PRO A 1 295 ? 41.974 29.080 40.349 1.00 31.82 ? 295 PRO A C 1 ATOM 2268 O O . PRO A 1 295 ? 42.695 28.328 39.679 1.00 31.37 ? 295 PRO A O 1 ATOM 2269 C CB . PRO A 1 295 ? 42.955 31.275 41.105 1.00 33.12 ? 295 PRO A CB 1 ATOM 2270 C CG . PRO A 1 295 ? 44.342 31.503 41.648 1.00 33.53 ? 295 PRO A CG 1 ATOM 2271 C CD . PRO A 1 295 ? 44.961 30.166 41.800 1.00 33.11 ? 295 PRO A CD 1 ATOM 2272 N N . ALA A 1 296 ? 40.677 29.240 40.104 1.00 30.89 ? 296 ALA A N 1 ATOM 2273 C CA . ALA A 1 296 ? 40.061 28.604 38.944 1.00 30.45 ? 296 ALA A CA 1 ATOM 2274 C C . ALA A 1 296 ? 40.759 29.068 37.670 1.00 30.30 ? 296 ALA A C 1 ATOM 2275 O O . ALA A 1 296 ? 41.052 30.259 37.510 1.00 30.51 ? 296 ALA A O 1 ATOM 2276 C CB . ALA A 1 296 ? 38.569 28.914 38.886 1.00 30.12 ? 296 ALA A CB 1 ATOM 2277 N N . GLY A 1 297 ? 41.036 28.120 36.782 1.00 30.00 ? 297 GLY A N 1 ATOM 2278 C CA . GLY A 1 297 ? 41.566 28.425 35.457 1.00 30.06 ? 297 GLY A CA 1 ATOM 2279 C C . GLY A 1 297 ? 43.057 28.732 35.426 1.00 30.15 ? 297 GLY A C 1 ATOM 2280 O O . GLY A 1 297 ? 43.584 29.130 34.382 1.00 30.22 ? 297 GLY A O 1 ATOM 2281 N N . SER A 1 298 ? 43.743 28.526 36.552 1.00 29.78 ? 298 SER A N 1 ATOM 2282 C CA . SER A 1 298 ? 45.170 28.863 36.644 1.00 29.49 ? 298 SER A CA 1 ATOM 2283 C C . SER A 1 298 ? 46.085 27.782 36.050 1.00 29.22 ? 298 SER A C 1 ATOM 2284 O O . SER A 1 298 ? 47.307 27.991 35.913 1.00 29.91 ? 298 SER A O 1 ATOM 2285 C CB . SER A 1 298 ? 45.548 29.141 38.101 1.00 29.65 ? 298 SER A CB 1 ATOM 2286 O OG . SER A 1 298 ? 45.390 27.979 38.889 1.00 30.17 ? 298 SER A OG 1 ATOM 2287 N N . ASP A 1 299 ? 45.517 26.628 35.707 1.00 27.69 ? 299 ASP A N 1 ATOM 2288 C CA . ASP A 1 299 ? 46.271 25.581 35.023 1.00 27.00 ? 299 ASP A CA 1 ATOM 2289 C C . ASP A 1 299 ? 45.330 24.795 34.125 1.00 26.02 ? 299 ASP A C 1 ATOM 2290 O O . ASP A 1 299 ? 44.981 23.637 34.401 1.00 25.34 ? 299 ASP A O 1 ATOM 2291 C CB . ASP A 1 299 ? 47.015 24.667 36.010 1.00 27.53 ? 299 ASP A CB 1 ATOM 2292 C CG . ASP A 1 299 ? 48.027 23.749 35.320 1.00 29.26 ? 299 ASP A CG 1 ATOM 2293 O OD1 . ASP A 1 299 ? 47.989 23.593 34.081 1.00 30.18 ? 299 ASP A OD1 1 ATOM 2294 O OD2 . ASP A 1 299 ? 48.863 23.148 36.026 1.00 30.89 ? 299 ASP A OD2 1 ATOM 2295 N N . TYR A 1 300 ? 44.930 25.446 33.039 1.00 25.07 ? 300 TYR A N 1 ATOM 2296 C CA . TYR A 1 300 ? 43.901 24.879 32.180 1.00 24.42 ? 300 TYR A CA 1 ATOM 2297 C C . TYR A 1 300 ? 44.378 23.608 31.495 1.00 24.33 ? 300 TYR A C 1 ATOM 2298 O O . TYR A 1 300 ? 43.591 22.690 31.243 1.00 23.75 ? 300 TYR A O 1 ATOM 2299 C CB . TYR A 1 300 ? 43.399 25.914 31.189 1.00 24.34 ? 300 TYR A CB 1 ATOM 2300 C CG . TYR A 1 300 ? 42.044 25.560 30.598 1.00 24.64 ? 300 TYR A CG 1 ATOM 2301 C CD1 . TYR A 1 300 ? 40.882 25.604 31.383 1.00 24.73 ? 300 TYR A CD1 1 ATOM 2302 C CD2 . TYR A 1 300 ? 41.922 25.201 29.259 1.00 25.45 ? 300 TYR A CD2 1 ATOM 2303 C CE1 . TYR A 1 300 ? 39.615 25.287 30.844 1.00 23.97 ? 300 TYR A CE1 1 ATOM 2304 C CE2 . TYR A 1 300 ? 40.672 24.883 28.702 1.00 25.56 ? 300 TYR A CE2 1 ATOM 2305 C CZ . TYR A 1 300 ? 39.521 24.927 29.505 1.00 24.86 ? 300 TYR A CZ 1 ATOM 2306 O OH . TYR A 1 300 ? 38.289 24.626 28.953 1.00 23.14 ? 300 TYR A OH 1 ATOM 2307 N N . SER A 1 301 ? 45.681 23.526 31.224 1.00 24.41 ? 301 SER A N 1 ATOM 2308 C CA . SER A 1 301 ? 46.216 22.291 30.687 1.00 24.50 ? 301 SER A CA 1 ATOM 2309 C C . SER A 1 301 ? 45.962 21.126 31.648 1.00 24.25 ? 301 SER A C 1 ATOM 2310 O O . SER A 1 301 ? 45.553 20.047 31.225 1.00 23.23 ? 301 SER A O 1 ATOM 2311 C CB . SER A 1 301 ? 47.720 22.411 30.384 1.00 25.11 ? 301 SER A CB 1 ATOM 2312 O OG . SER A 1 301 ? 48.221 21.118 30.121 1.00 27.70 ? 301 SER A OG 1 ATOM 2313 N N . TYR A 1 302 ? 46.203 21.343 32.943 1.00 24.04 ? 302 TYR A N 1 ATOM 2314 C CA . TYR A 1 302 ? 45.893 20.324 33.942 1.00 24.68 ? 302 TYR A CA 1 ATOM 2315 C C . TYR A 1 302 ? 44.388 20.024 34.002 1.00 23.57 ? 302 TYR A C 1 ATOM 2316 O O . TYR A 1 302 ? 43.991 18.860 34.061 1.00 22.95 ? 302 TYR A O 1 ATOM 2317 C CB . TYR A 1 302 ? 46.389 20.748 35.336 1.00 26.32 ? 302 TYR A CB 1 ATOM 2318 C CG . TYR A 1 302 ? 45.979 19.757 36.394 1.00 30.11 ? 302 TYR A CG 1 ATOM 2319 C CD1 . TYR A 1 302 ? 46.542 18.475 36.429 1.00 30.62 ? 302 TYR A CD1 1 ATOM 2320 C CD2 . TYR A 1 302 ? 44.990 20.076 37.330 1.00 30.19 ? 302 TYR A CD2 1 ATOM 2321 C CE1 . TYR A 1 302 ? 46.160 17.544 37.388 1.00 32.23 ? 302 TYR A CE1 1 ATOM 2322 C CE2 . TYR A 1 302 ? 44.601 19.155 38.298 1.00 31.54 ? 302 TYR A CE2 1 ATOM 2323 C CZ . TYR A 1 302 ? 45.187 17.892 38.317 1.00 33.60 ? 302 TYR A CZ 1 ATOM 2324 O OH . TYR A 1 302 ? 44.809 16.975 39.275 1.00 32.42 ? 302 TYR A OH 1 ATOM 2325 N N . SER A 1 303 ? 43.568 21.078 33.972 1.00 22.72 ? 303 SER A N 1 ATOM 2326 C CA . SER A 1 303 ? 42.094 20.933 33.982 1.00 21.98 ? 303 SER A CA 1 ATOM 2327 C C . SER A 1 303 ? 41.622 19.974 32.876 1.00 21.88 ? 303 SER A C 1 ATOM 2328 O O . SER A 1 303 ? 40.797 19.093 33.114 1.00 21.10 ? 303 SER A O 1 ATOM 2329 C CB . SER A 1 303 ? 41.427 22.301 33.807 1.00 21.70 ? 303 SER A CB 1 ATOM 2330 O OG . SER A 1 303 ? 41.527 23.098 34.985 1.00 23.28 ? 303 SER A OG 1 ATOM 2331 N N . VAL A 1 304 ? 42.171 20.135 31.663 1.00 21.72 ? 304 VAL A N 1 ATOM 2332 C CA . VAL A 1 304 ? 41.768 19.294 30.528 1.00 20.98 ? 304 VAL A CA 1 ATOM 2333 C C . VAL A 1 304 ? 42.235 17.859 30.728 1.00 21.68 ? 304 VAL A C 1 ATOM 2334 O O . VAL A 1 304 ? 41.469 16.919 30.572 1.00 20.98 ? 304 VAL A O 1 ATOM 2335 C CB . VAL A 1 304 ? 42.307 19.861 29.198 1.00 21.20 ? 304 VAL A CB 1 ATOM 2336 C CG1 . VAL A 1 304 ? 42.011 18.921 28.038 1.00 21.24 ? 304 VAL A CG1 1 ATOM 2337 C CG2 . VAL A 1 304 ? 41.713 21.220 28.962 1.00 19.36 ? 304 VAL A CG2 1 ATOM 2338 N N . LYS A 1 305 ? 43.501 17.694 31.107 1.00 21.98 ? 305 LYS A N 1 ATOM 2339 C CA . LYS A 1 305 ? 43.997 16.364 31.371 1.00 24.98 ? 305 LYS A CA 1 ATOM 2340 C C . LYS A 1 305 ? 43.214 15.625 32.467 1.00 22.61 ? 305 LYS A C 1 ATOM 2341 O O . LYS A 1 305 ? 42.802 14.487 32.268 1.00 22.12 ? 305 LYS A O 1 ATOM 2342 C CB . LYS A 1 305 ? 45.478 16.435 31.757 1.00 22.59 ? 305 LYS A CB 1 ATOM 2343 C CG . LYS A 1 305 ? 46.024 15.088 32.039 1.00 33.26 ? 305 LYS A CG 1 ATOM 2344 C CD . LYS A 1 305 ? 47.496 15.193 32.567 1.00 21.77 ? 305 LYS A CD 1 ATOM 2345 C CE . LYS A 1 305 ? 47.901 14.102 33.626 1.00 38.06 ? 305 LYS A CE 1 ATOM 2346 N NZ . LYS A 1 305 ? 49.296 14.228 34.158 1.00 25.50 ? 305 LYS A NZ 1 ATOM 2347 N N . ALA A 1 306 ? 43.036 16.283 33.616 1.00 22.58 ? 306 ALA A N 1 ATOM 2348 C CA . ALA A 1 306 ? 42.382 15.669 34.775 1.00 22.33 ? 306 ALA A CA 1 ATOM 2349 C C . ALA A 1 306 ? 40.950 15.252 34.463 1.00 22.37 ? 306 ALA A C 1 ATOM 2350 O O . ALA A 1 306 ? 40.546 14.122 34.748 1.00 22.30 ? 306 ALA A O 1 ATOM 2351 C CB . ALA A 1 306 ? 42.432 16.614 35.983 1.00 22.57 ? 306 ALA A CB 1 ATOM 2352 N N . SER A 1 307 ? 40.204 16.154 33.828 1.00 21.50 ? 307 SER A N 1 ATOM 2353 C CA . SER A 1 307 ? 38.784 15.915 33.556 1.00 20.66 ? 307 SER A CA 1 ATOM 2354 C C . SER A 1 307 ? 38.558 14.831 32.480 1.00 20.12 ? 307 SER A C 1 ATOM 2355 O O . SER A 1 307 ? 37.713 13.938 32.633 1.00 19.97 ? 307 SER A O 1 ATOM 2356 C CB . SER A 1 307 ? 38.100 17.234 33.199 1.00 20.62 ? 307 SER A CB 1 ATOM 2357 O OG . SER A 1 307 ? 38.619 17.794 32.002 1.00 21.88 ? 307 SER A OG 1 ATOM 2358 N N . ILE A 1 308 ? 39.334 14.892 31.397 1.00 20.14 ? 308 ILE A N 1 ATOM 2359 C CA . ILE A 1 308 ? 39.165 13.927 30.322 1.00 20.24 ? 308 ILE A CA 1 ATOM 2360 C C . ILE A 1 308 ? 39.635 12.531 30.784 1.00 20.70 ? 308 ILE A C 1 ATOM 2361 O O . ILE A 1 308 ? 38.978 11.530 30.520 1.00 20.24 ? 308 ILE A O 1 ATOM 2362 C CB . ILE A 1 308 ? 39.808 14.415 28.988 1.00 20.70 ? 308 ILE A CB 1 ATOM 2363 C CG1 . ILE A 1 308 ? 39.117 15.709 28.501 1.00 19.81 ? 308 ILE A CG1 1 ATOM 2364 C CG2 . ILE A 1 308 ? 39.697 13.319 27.918 1.00 21.53 ? 308 ILE A CG2 1 ATOM 2365 C CD1 . ILE A 1 308 ? 37.571 15.628 28.353 1.00 20.31 ? 308 ILE A CD1 1 ATOM 2366 N N . LEU A 1 309 ? 40.755 12.472 31.500 1.00 21.31 ? 309 LEU A N 1 ATOM 2367 C CA . LEU A 1 309 ? 41.195 11.198 32.070 1.00 21.64 ? 309 LEU A CA 1 ATOM 2368 C C . LEU A 1 309 ? 40.230 10.650 33.135 1.00 21.35 ? 309 LEU A C 1 ATOM 2369 O O . LEU A 1 309 ? 40.090 9.432 33.265 1.00 22.53 ? 309 LEU A O 1 ATOM 2370 C CB . LEU A 1 309 ? 42.635 11.279 32.596 1.00 21.59 ? 309 LEU A CB 1 ATOM 2371 C CG . LEU A 1 309 ? 43.678 11.447 31.466 1.00 22.28 ? 309 LEU A CG 1 ATOM 2372 C CD1 . LEU A 1 309 ? 45.070 11.522 32.098 1.00 23.19 ? 309 LEU A CD1 1 ATOM 2373 C CD2 . LEU A 1 309 ? 43.581 10.312 30.427 1.00 22.09 ? 309 LEU A CD2 1 ATOM 2374 N N . ALA A 1 310 ? 39.552 11.540 33.860 1.00 21.39 ? 310 ALA A N 1 ATOM 2375 C CA . ALA A 1 310 ? 38.543 11.127 34.842 1.00 20.99 ? 310 ALA A CA 1 ATOM 2376 C C . ALA A 1 310 ? 37.365 10.413 34.189 1.00 21.13 ? 310 ALA A C 1 ATOM 2377 O O . ALA A 1 310 ? 36.691 9.604 34.837 1.00 21.65 ? 310 ALA A O 1 ATOM 2378 C CB . ALA A 1 310 ? 38.050 12.333 35.654 1.00 21.77 ? 310 ALA A CB 1 ATOM 2379 N N . GLY A 1 311 ? 37.098 10.728 32.913 1.00 20.44 ? 311 GLY A N 1 ATOM 2380 C CA . GLY A 1 311 ? 36.026 10.068 32.177 1.00 19.89 ? 311 GLY A CA 1 ATOM 2381 C C . GLY A 1 311 ? 34.944 10.991 31.619 1.00 19.50 ? 311 GLY A C 1 ATOM 2382 O O . GLY A 1 311 ? 33.952 10.505 31.065 1.00 19.48 ? 311 GLY A O 1 ATOM 2383 N N . LEU A 1 312 ? 35.132 12.307 31.740 1.00 19.33 ? 312 LEU A N 1 ATOM 2384 C CA . LEU A 1 312 ? 34.136 13.253 31.189 1.00 18.95 ? 312 LEU A CA 1 ATOM 2385 C C . LEU A 1 312 ? 34.162 13.170 29.670 1.00 18.58 ? 312 LEU A C 1 ATOM 2386 O O . LEU A 1 312 ? 35.226 12.963 29.078 1.00 18.83 ? 312 LEU A O 1 ATOM 2387 C CB . LEU A 1 312 ? 34.340 14.691 31.693 1.00 18.60 ? 312 LEU A CB 1 ATOM 2388 C CG . LEU A 1 312 ? 33.772 15.012 33.091 1.00 19.35 ? 312 LEU A CG 1 ATOM 2389 C CD1 . LEU A 1 312 ? 34.632 14.360 34.188 1.00 19.25 ? 312 LEU A CD1 1 ATOM 2390 C CD2 . LEU A 1 312 ? 33.701 16.514 33.290 1.00 19.81 ? 312 LEU A CD2 1 ATOM 2391 N N . ASP A 1 313 ? 32.984 13.286 29.045 1.00 17.70 ? 313 ASP A N 1 ATOM 2392 C CA . ASP A 1 313 ? 32.869 13.108 27.592 1.00 17.85 ? 313 ASP A CA 1 ATOM 2393 C C . ASP A 1 313 ? 32.695 14.412 26.827 1.00 17.48 ? 313 ASP A C 1 ATOM 2394 O O . ASP A 1 313 ? 33.245 14.581 25.726 1.00 18.15 ? 313 ASP A O 1 ATOM 2395 C CB . ASP A 1 313 ? 31.689 12.175 27.271 1.00 18.31 ? 313 ASP A CB 1 ATOM 2396 C CG . ASP A 1 313 ? 31.784 10.842 28.001 1.00 18.45 ? 313 ASP A CG 1 ATOM 2397 O OD1 . ASP A 1 313 ? 32.866 10.203 27.969 1.00 19.70 ? 313 ASP A OD1 1 ATOM 2398 O OD2 . ASP A 1 313 ? 30.775 10.433 28.619 1.00 18.74 ? 313 ASP A OD2 1 ATOM 2399 N N . MET A 1 314 ? 31.874 15.311 27.379 1.00 17.04 ? 314 MET A N 1 ATOM 2400 C CA . MET A 1 314 ? 31.618 16.598 26.753 1.00 17.35 ? 314 MET A CA 1 ATOM 2401 C C . MET A 1 314 ? 31.929 17.713 27.750 1.00 17.51 ? 314 MET A C 1 ATOM 2402 O O . MET A 1 314 ? 31.539 17.637 28.918 1.00 18.19 ? 314 MET A O 1 ATOM 2403 C CB . MET A 1 314 ? 30.149 16.698 26.284 1.00 17.45 ? 314 MET A CB 1 ATOM 2404 C CG . MET A 1 314 ? 29.833 18.026 25.535 1.00 18.05 ? 314 MET A CG 1 ATOM 2405 S SD . MET A 1 314 ? 28.132 18.158 24.971 1.00 18.97 ? 314 MET A SD 1 ATOM 2406 C CE . MET A 1 314 ? 28.131 16.959 23.625 1.00 19.94 ? 314 MET A CE 1 ATOM 2407 N N . ILE A 1 315 ? 32.615 18.743 27.283 1.00 16.15 ? 315 ILE A N 1 ATOM 2408 C CA . ILE A 1 315 ? 32.996 19.848 28.134 1.00 16.85 ? 315 ILE A CA 1 ATOM 2409 C C . ILE A 1 315 ? 32.171 21.070 27.810 1.00 17.08 ? 315 ILE A C 1 ATOM 2410 O O . ILE A 1 315 ? 32.159 21.571 26.676 1.00 17.61 ? 315 ILE A O 1 ATOM 2411 C CB . ILE A 1 315 ? 34.533 20.137 28.067 1.00 16.99 ? 315 ILE A CB 1 ATOM 2412 C CG1 . ILE A 1 315 ? 35.338 18.866 28.435 1.00 16.93 ? 315 ILE A CG1 1 ATOM 2413 C CG2 . ILE A 1 315 ? 34.897 21.359 28.940 1.00 18.21 ? 315 ILE A CG2 1 ATOM 2414 C CD1 . ILE A 1 315 ? 34.934 18.177 29.774 1.00 17.88 ? 315 ILE A CD1 1 ATOM 2415 N N . MET A 1 316 ? 31.472 21.549 28.826 1.00 16.64 ? 316 MET A N 1 ATOM 2416 C CA . MET A 1 316 ? 30.764 22.824 28.741 1.00 16.82 ? 316 MET A CA 1 ATOM 2417 C C . MET A 1 316 ? 31.808 23.913 28.986 1.00 16.93 ? 316 MET A C 1 ATOM 2418 O O . MET A 1 316 ? 32.083 24.281 30.142 1.00 16.92 ? 316 MET A O 1 ATOM 2419 C CB . MET A 1 316 ? 29.644 22.848 29.804 1.00 17.05 ? 316 MET A CB 1 ATOM 2420 C CG . MET A 1 316 ? 28.775 24.104 29.780 1.00 17.00 ? 316 MET A CG 1 ATOM 2421 S SD . MET A 1 316 ? 27.525 24.122 31.112 1.00 18.55 ? 316 MET A SD 1 ATOM 2422 C CE . MET A 1 316 ? 26.643 22.586 30.838 1.00 19.23 ? 316 MET A CE 1 ATOM 2423 N N . VAL A 1 317 ? 32.412 24.411 27.902 1.00 17.33 ? 317 VAL A N 1 ATOM 2424 C CA . VAL A 1 317 ? 33.642 25.218 28.022 1.00 18.45 ? 317 VAL A CA 1 ATOM 2425 C C . VAL A 1 317 ? 33.447 26.493 28.892 1.00 18.49 ? 317 VAL A C 1 ATOM 2426 O O . VAL A 1 317 ? 34.193 26.682 29.873 1.00 19.12 ? 317 VAL A O 1 ATOM 2427 C CB . VAL A 1 317 ? 34.318 25.488 26.645 1.00 18.41 ? 317 VAL A CB 1 ATOM 2428 C CG1 . VAL A 1 317 ? 35.628 26.270 26.827 1.00 19.93 ? 317 VAL A CG1 1 ATOM 2429 C CG2 . VAL A 1 317 ? 34.562 24.171 25.906 1.00 18.36 ? 317 VAL A CG2 1 ATOM 2430 N N . PRO A 1 318 ? 32.419 27.324 28.603 1.00 18.61 ? 318 PRO A N 1 ATOM 2431 C CA . PRO A 1 318 ? 31.582 27.377 27.400 1.00 18.46 ? 318 PRO A CA 1 ATOM 2432 C C . PRO A 1 318 ? 32.075 28.446 26.401 1.00 19.64 ? 318 PRO A C 1 ATOM 2433 O O . PRO A 1 318 ? 31.541 28.538 25.299 1.00 19.35 ? 318 PRO A O 1 ATOM 2434 C CB . PRO A 1 318 ? 30.219 27.812 27.975 1.00 18.74 ? 318 PRO A CB 1 ATOM 2435 C CG . PRO A 1 318 ? 30.618 28.837 29.019 1.00 18.93 ? 318 PRO A CG 1 ATOM 2436 C CD . PRO A 1 318 ? 31.939 28.288 29.620 1.00 18.32 ? 318 PRO A CD 1 ATOM 2437 N N . ASN A 1 319 ? 33.067 29.247 26.800 1.00 20.41 ? 319 ASN A N 1 ATOM 2438 C CA . ASN A 1 319 ? 33.484 30.400 25.998 1.00 21.33 ? 319 ASN A CA 1 ATOM 2439 C C . ASN A 1 319 ? 34.800 30.207 25.252 1.00 22.33 ? 319 ASN A C 1 ATOM 2440 O O . ASN A 1 319 ? 34.870 30.448 24.033 1.00 22.74 ? 319 ASN A O 1 ATOM 2441 C CB . ASN A 1 319 ? 33.516 31.677 26.851 1.00 21.61 ? 319 ASN A CB 1 ATOM 2442 C CG . ASN A 1 319 ? 32.180 32.000 27.452 1.00 22.33 ? 319 ASN A CG 1 ATOM 2443 O OD1 . ASN A 1 319 ? 31.155 31.890 26.794 1.00 23.08 ? 319 ASN A OD1 1 ATOM 2444 N ND2 . ASN A 1 319 ? 32.178 32.391 28.721 1.00 23.98 ? 319 ASN A ND2 1 ATOM 2445 N N . LYS A 1 320 ? 35.838 29.775 25.969 1.00 22.66 ? 320 LYS A N 1 ATOM 2446 C CA . LYS A 1 320 ? 37.173 29.727 25.362 1.00 23.00 ? 320 LYS A CA 1 ATOM 2447 C C . LYS A 1 320 ? 37.441 28.393 24.669 1.00 22.37 ? 320 LYS A C 1 ATOM 2448 O O . LYS A 1 320 ? 38.336 27.619 25.046 1.00 22.34 ? 320 LYS A O 1 ATOM 2449 C CB A LYS A 1 320 ? 38.230 30.079 26.413 0.50 23.69 ? 320 LYS A CB 1 ATOM 2450 C CB B LYS A 1 320 ? 38.272 30.105 26.375 0.50 25.81 ? 320 LYS A CB 1 ATOM 2451 C CG A LYS A 1 320 ? 38.341 31.578 26.633 0.50 25.11 ? 320 LYS A CG 1 ATOM 2452 C CG B LYS A 1 320 ? 39.682 30.376 25.764 0.50 22.40 ? 320 LYS A CG 1 ATOM 2453 C CD A LYS A 1 320 ? 37.674 32.023 27.904 0.50 28.30 ? 320 LYS A CD 1 ATOM 2454 C CD B LYS A 1 320 ? 39.718 30.499 24.221 0.50 29.71 ? 320 LYS A CD 1 ATOM 2455 C CE A LYS A 1 320 ? 37.693 33.540 28.030 0.50 30.59 ? 320 LYS A CE 1 ATOM 2456 C CE B LYS A 1 320 ? 40.761 31.543 23.746 0.50 18.95 ? 320 LYS A CE 1 ATOM 2457 N NZ A LYS A 1 320 ? 36.521 34.186 27.375 0.50 29.08 ? 320 LYS A NZ 1 ATOM 2458 N NZ B LYS A 1 320 ? 42.174 31.064 23.460 0.50 31.51 ? 320 LYS A NZ 1 ATOM 2459 N N . TYR A 1 321 ? 36.642 28.128 23.627 1.00 22.22 ? 321 TYR A N 1 ATOM 2460 C CA . TYR A 1 321 ? 36.725 26.852 22.907 1.00 21.99 ? 321 TYR A CA 1 ATOM 2461 C C . TYR A 1 321 ? 38.072 26.702 22.201 1.00 21.72 ? 321 TYR A C 1 ATOM 2462 O O . TYR A 1 321 ? 38.543 25.586 22.015 1.00 21.57 ? 321 TYR A O 1 ATOM 2463 C CB . TYR A 1 321 ? 35.558 26.684 21.892 1.00 22.47 ? 321 TYR A CB 1 ATOM 2464 C CG . TYR A 1 321 ? 35.516 27.814 20.898 1.00 22.57 ? 321 TYR A CG 1 ATOM 2465 C CD1 . TYR A 1 321 ? 36.308 27.775 19.739 1.00 22.19 ? 321 TYR A CD1 1 ATOM 2466 C CD2 . TYR A 1 321 ? 34.726 28.947 21.129 1.00 22.10 ? 321 TYR A CD2 1 ATOM 2467 C CE1 . TYR A 1 321 ? 36.331 28.845 18.856 1.00 22.16 ? 321 TYR A CE1 1 ATOM 2468 C CE2 . TYR A 1 321 ? 34.726 30.023 20.236 1.00 23.81 ? 321 TYR A CE2 1 ATOM 2469 C CZ . TYR A 1 321 ? 35.544 29.964 19.108 1.00 23.53 ? 321 TYR A CZ 1 ATOM 2470 O OH . TYR A 1 321 ? 35.557 31.014 18.218 1.00 25.96 ? 321 TYR A OH 1 ATOM 2471 N N . GLN A 1 322 ? 38.688 27.820 21.808 1.00 21.49 ? 322 GLN A N 1 ATOM 2472 C CA . GLN A 1 322 ? 39.965 27.739 21.089 1.00 22.66 ? 322 GLN A CA 1 ATOM 2473 C C . GLN A 1 322 ? 41.004 27.115 22.009 1.00 22.19 ? 322 GLN A C 1 ATOM 2474 O O . GLN A 1 322 ? 41.678 26.164 21.623 1.00 23.15 ? 322 GLN A O 1 ATOM 2475 C CB A GLN A 1 322 ? 40.434 29.108 20.600 0.50 22.25 ? 322 GLN A CB 1 ATOM 2476 C CB B GLN A 1 322 ? 40.434 29.126 20.642 0.50 22.35 ? 322 GLN A CB 1 ATOM 2477 C CG A GLN A 1 322 ? 41.689 29.030 19.729 0.50 23.05 ? 322 GLN A CG 1 ATOM 2478 C CG B GLN A 1 322 ? 39.404 29.932 19.869 0.50 23.18 ? 322 GLN A CG 1 ATOM 2479 C CD A GLN A 1 322 ? 42.118 30.378 19.185 0.50 23.02 ? 322 GLN A CD 1 ATOM 2480 C CD B GLN A 1 322 ? 38.719 30.991 20.727 0.50 25.60 ? 322 GLN A CD 1 ATOM 2481 O OE1 A GLN A 1 322 ? 41.288 31.165 18.733 0.50 24.58 ? 322 GLN A OE1 1 ATOM 2482 O OE1 B GLN A 1 322 ? 38.046 30.689 21.728 0.50 22.39 ? 322 GLN A OE1 1 ATOM 2483 N NE2 A GLN A 1 322 ? 43.416 30.655 19.233 0.50 23.02 ? 322 GLN A NE2 1 ATOM 2484 N NE2 B GLN A 1 322 ? 38.898 32.255 20.334 0.50 26.91 ? 322 GLN A NE2 1 ATOM 2485 N N . GLN A 1 323 ? 41.080 27.627 23.236 1.00 23.15 ? 323 GLN A N 1 ATOM 2486 C CA . GLN A 1 323 ? 42.017 27.099 24.227 1.00 23.56 ? 323 GLN A CA 1 ATOM 2487 C C . GLN A 1 323 ? 41.725 25.640 24.543 1.00 22.61 ? 323 GLN A C 1 ATOM 2488 O O . GLN A 1 323 ? 42.645 24.810 24.549 1.00 22.84 ? 323 GLN A O 1 ATOM 2489 C CB . GLN A 1 323 ? 41.993 27.953 25.485 1.00 25.23 ? 323 GLN A CB 1 ATOM 2490 C CG . GLN A 1 323 ? 42.994 27.506 26.545 1.00 31.23 ? 323 GLN A CG 1 ATOM 2491 C CD . GLN A 1 323 ? 42.797 28.210 27.874 1.00 29.98 ? 323 GLN A CD 1 ATOM 2492 O OE1 . GLN A 1 323 ? 41.676 28.565 28.261 1.00 42.66 ? 323 GLN A OE1 1 ATOM 2493 N NE2 . GLN A 1 323 ? 43.885 28.395 28.593 1.00 39.95 ? 323 GLN A NE2 1 ATOM 2494 N N . PHE A 1 324 ? 40.452 25.308 24.784 1.00 21.00 ? 324 PHE A N 1 ATOM 2495 C CA . PHE A 1 324 ? 40.094 23.919 25.062 1.00 19.99 ? 324 PHE A CA 1 ATOM 2496 C C . PHE A 1 324 ? 40.528 22.973 23.944 1.00 19.22 ? 324 PHE A C 1 ATOM 2497 O O . PHE A 1 324 ? 41.181 21.958 24.195 1.00 18.61 ? 324 PHE A O 1 ATOM 2498 C CB . PHE A 1 324 ? 38.579 23.759 25.329 1.00 19.98 ? 324 PHE A CB 1 ATOM 2499 C CG . PHE A 1 324 ? 38.160 22.328 25.521 1.00 19.99 ? 324 PHE A CG 1 ATOM 2500 C CD1 . PHE A 1 324 ? 38.504 21.639 26.690 1.00 19.22 ? 324 PHE A CD1 1 ATOM 2501 C CD2 . PHE A 1 324 ? 37.462 21.649 24.524 1.00 19.03 ? 324 PHE A CD2 1 ATOM 2502 C CE1 . PHE A 1 324 ? 38.149 20.306 26.855 1.00 19.07 ? 324 PHE A CE1 1 ATOM 2503 C CE2 . PHE A 1 324 ? 37.108 20.311 24.675 1.00 19.47 ? 324 PHE A CE2 1 ATOM 2504 C CZ . PHE A 1 324 ? 37.447 19.634 25.850 1.00 19.82 ? 324 PHE A CZ 1 ATOM 2505 N N . ILE A 1 325 ? 40.131 23.287 22.711 1.00 19.77 ? 325 ILE A N 1 ATOM 2506 C CA . ILE A 1 325 ? 40.430 22.416 21.587 1.00 19.75 ? 325 ILE A CA 1 ATOM 2507 C C . ILE A 1 325 ? 41.941 22.301 21.369 1.00 19.80 ? 325 ILE A C 1 ATOM 2508 O O . ILE A 1 325 ? 42.455 21.199 21.164 1.00 18.90 ? 325 ILE A O 1 ATOM 2509 C CB . ILE A 1 325 ? 39.714 22.885 20.280 1.00 19.61 ? 325 ILE A CB 1 ATOM 2510 C CG1 . ILE A 1 325 ? 38.190 22.771 20.459 1.00 19.92 ? 325 ILE A CG1 1 ATOM 2511 C CG2 . ILE A 1 325 ? 40.186 22.058 19.081 1.00 20.82 ? 325 ILE A CG2 1 ATOM 2512 C CD1 . ILE A 1 325 ? 37.404 23.403 19.307 1.00 20.19 ? 325 ILE A CD1 1 ATOM 2513 N N . SER A 1 326 ? 42.642 23.424 21.483 1.00 20.13 ? 326 SER A N 1 ATOM 2514 C CA . SER A 1 326 ? 44.097 23.417 21.285 1.00 20.44 ? 326 SER A CA 1 ATOM 2515 C C . SER A 1 326 ? 44.806 22.533 22.330 1.00 20.74 ? 326 SER A C 1 ATOM 2516 O O . SER A 1 326 ? 45.648 21.685 21.990 1.00 21.17 ? 326 SER A O 1 ATOM 2517 C CB . SER A 1 326 ? 44.641 24.843 21.294 1.00 20.85 ? 326 SER A CB 1 ATOM 2518 O OG . SER A 1 326 ? 46.041 24.805 21.053 1.00 22.29 ? 326 SER A OG 1 ATOM 2519 N N . ILE A 1 327 ? 44.429 22.703 23.597 1.00 20.74 ? 327 ILE A N 1 ATOM 2520 C CA . ILE A 1 327 ? 45.061 21.947 24.674 1.00 21.13 ? 327 ILE A CA 1 ATOM 2521 C C . ILE A 1 327 ? 44.768 20.455 24.556 1.00 20.84 ? 327 ILE A C 1 ATOM 2522 O O . ILE A 1 327 ? 45.668 19.617 24.681 1.00 21.26 ? 327 ILE A O 1 ATOM 2523 C CB . ILE A 1 327 ? 44.626 22.482 26.047 1.00 21.41 ? 327 ILE A CB 1 ATOM 2524 C CG1 . ILE A 1 327 ? 45.290 23.842 26.288 1.00 22.73 ? 327 ILE A CG1 1 ATOM 2525 C CG2 . ILE A 1 327 ? 44.954 21.472 27.158 1.00 22.02 ? 327 ILE A CG2 1 ATOM 2526 C CD1 . ILE A 1 327 ? 44.841 24.546 27.536 1.00 26.96 ? 327 ILE A CD1 1 ATOM 2527 N N . LEU A 1 328 ? 43.501 20.115 24.324 1.00 20.02 ? 328 LEU A N 1 ATOM 2528 C CA . LEU A 1 328 ? 43.137 18.719 24.193 1.00 19.70 ? 328 LEU A CA 1 ATOM 2529 C C . LEU A 1 328 ? 43.848 18.069 22.990 1.00 20.16 ? 328 LEU A C 1 ATOM 2530 O O . LEU A 1 328 ? 44.343 16.937 23.092 1.00 20.01 ? 328 LEU A O 1 ATOM 2531 C CB . LEU A 1 328 ? 41.610 18.542 24.124 1.00 19.41 ? 328 LEU A CB 1 ATOM 2532 C CG . LEU A 1 328 ? 41.109 17.098 24.085 1.00 19.21 ? 328 LEU A CG 1 ATOM 2533 C CD1 . LEU A 1 328 ? 41.752 16.201 25.193 1.00 21.35 ? 328 LEU A CD1 1 ATOM 2534 C CD2 . LEU A 1 328 ? 39.563 17.096 24.217 1.00 20.22 ? 328 LEU A CD2 1 ATOM 2535 N N . THR A 1 329 ? 43.909 18.800 21.878 1.00 19.75 ? 329 THR A N 1 ATOM 2536 C CA . THR A 1 329 ? 44.593 18.283 20.693 1.00 20.79 ? 329 THR A CA 1 ATOM 2537 C C . THR A 1 329 ? 46.073 18.002 21.033 1.00 20.94 ? 329 THR A C 1 ATOM 2538 O O . THR A 1 329 ? 46.588 16.947 20.684 1.00 21.33 ? 329 THR A O 1 ATOM 2539 C CB . THR A 1 329 ? 44.471 19.250 19.514 1.00 20.63 ? 329 THR A CB 1 ATOM 2540 O OG1 . THR A 1 329 ? 43.084 19.399 19.197 1.00 21.12 ? 329 THR A OG1 1 ATOM 2541 C CG2 . THR A 1 329 ? 45.220 18.709 18.276 1.00 21.39 ? 329 THR A CG2 1 ATOM 2542 N N . GLY A 1 330 ? 46.701 18.933 21.751 1.00 21.25 ? 330 GLY A N 1 ATOM 2543 C CA . GLY A 1 330 ? 48.111 18.782 22.198 1.00 22.20 ? 330 GLY A CA 1 ATOM 2544 C C . GLY A 1 330 ? 48.297 17.538 23.067 1.00 22.73 ? 330 GLY A C 1 ATOM 2545 O O . GLY A 1 330 ? 49.243 16.757 22.874 1.00 22.72 ? 330 GLY A O 1 ATOM 2546 N N . HIS A 1 331 ? 47.386 17.324 24.014 1.00 22.69 ? 331 HIS A N 1 ATOM 2547 C CA . HIS A 1 331 ? 47.493 16.171 24.911 1.00 23.42 ? 331 HIS A CA 1 ATOM 2548 C C . HIS A 1 331 ? 47.385 14.852 24.143 1.00 22.90 ? 331 HIS A C 1 ATOM 2549 O O . HIS A 1 331 ? 48.100 13.895 24.435 1.00 23.90 ? 331 HIS A O 1 ATOM 2550 C CB . HIS A 1 331 ? 46.445 16.245 26.041 1.00 23.37 ? 331 HIS A CB 1 ATOM 2551 C CG . HIS A 1 331 ? 46.806 17.215 27.126 1.00 25.59 ? 331 HIS A CG 1 ATOM 2552 N ND1 . HIS A 1 331 ? 45.869 17.920 27.852 1.00 27.87 ? 331 HIS A ND1 1 ATOM 2553 C CD2 . HIS A 1 331 ? 48.015 17.610 27.593 1.00 26.45 ? 331 HIS A CD2 1 ATOM 2554 C CE1 . HIS A 1 331 ? 46.484 18.694 28.732 1.00 25.90 ? 331 HIS A CE1 1 ATOM 2555 N NE2 . HIS A 1 331 ? 47.788 18.533 28.587 1.00 30.01 ? 331 HIS A NE2 1 ATOM 2556 N N . VAL A 1 332 ? 46.498 14.804 23.151 1.00 22.06 ? 332 VAL A N 1 ATOM 2557 C CA . VAL A 1 332 ? 46.341 13.591 22.362 1.00 22.29 ? 332 VAL A CA 1 ATOM 2558 C C . VAL A 1 332 ? 47.584 13.357 21.477 1.00 22.84 ? 332 VAL A C 1 ATOM 2559 O O . VAL A 1 332 ? 48.094 12.226 21.398 1.00 23.33 ? 332 VAL A O 1 ATOM 2560 C CB . VAL A 1 332 ? 45.052 13.644 21.518 1.00 22.21 ? 332 VAL A CB 1 ATOM 2561 C CG1 . VAL A 1 332 ? 44.950 12.430 20.644 1.00 22.83 ? 332 VAL A CG1 1 ATOM 2562 C CG2 . VAL A 1 332 ? 43.844 13.719 22.458 1.00 20.83 ? 332 VAL A CG2 1 ATOM 2563 N N . ASN A 1 333 ? 48.051 14.422 20.832 1.00 23.97 ? 333 ASN A N 1 ATOM 2564 C CA . ASN A 1 333 ? 49.248 14.350 19.966 1.00 25.44 ? 333 ASN A CA 1 ATOM 2565 C C . ASN A 1 333 ? 50.489 13.913 20.753 1.00 26.64 ? 333 ASN A C 1 ATOM 2566 O O . ASN A 1 333 ? 51.364 13.213 20.211 1.00 27.22 ? 333 ASN A O 1 ATOM 2567 C CB . ASN A 1 333 ? 49.490 15.679 19.239 1.00 25.56 ? 333 ASN A CB 1 ATOM 2568 C CG . ASN A 1 333 ? 48.516 15.906 18.088 1.00 25.39 ? 333 ASN A CG 1 ATOM 2569 O OD1 . ASN A 1 333 ? 47.897 14.960 17.584 1.00 25.69 ? 333 ASN A OD1 1 ATOM 2570 N ND2 . ASN A 1 333 ? 48.361 17.162 17.680 1.00 24.61 ? 333 ASN A ND2 1 ATOM 2571 N N . GLY A 1 334 ? 50.540 14.306 22.026 1.00 27.07 ? 334 GLY A N 1 ATOM 2572 C CA . GLY A 1 334 ? 51.643 13.963 22.933 1.00 28.00 ? 334 GLY A CA 1 ATOM 2573 C C . GLY A 1 334 ? 51.493 12.653 23.689 1.00 29.16 ? 334 GLY A C 1 ATOM 2574 O O . GLY A 1 334 ? 52.351 12.307 24.528 1.00 29.85 ? 334 GLY A O 1 ATOM 2575 N N . GLY A 1 335 ? 50.403 11.926 23.423 1.00 28.88 ? 335 GLY A N 1 ATOM 2576 C CA . GLY A 1 335 ? 50.133 10.636 24.057 1.00 29.43 ? 335 GLY A CA 1 ATOM 2577 C C . GLY A 1 335 ? 49.728 10.663 25.523 1.00 29.42 ? 335 GLY A C 1 ATOM 2578 O O . GLY A 1 335 ? 49.669 9.608 26.168 1.00 30.63 ? 335 GLY A O 1 ATOM 2579 N N . VAL A 1 336 ? 49.440 11.852 26.055 1.00 28.55 ? 336 VAL A N 1 ATOM 2580 C CA . VAL A 1 336 ? 49.044 12.026 27.461 1.00 28.45 ? 336 VAL A CA 1 ATOM 2581 C C . VAL A 1 336 ? 47.598 11.565 27.685 1.00 27.47 ? 336 VAL A C 1 ATOM 2582 O O . VAL A 1 336 ? 47.234 11.085 28.770 1.00 27.13 ? 336 VAL A O 1 ATOM 2583 C CB . VAL A 1 336 ? 49.232 13.498 27.917 1.00 28.91 ? 336 VAL A CB 1 ATOM 2584 C CG1 . VAL A 1 336 ? 48.529 13.777 29.255 1.00 30.44 ? 336 VAL A CG1 1 ATOM 2585 C CG2 . VAL A 1 336 ? 50.715 13.844 27.997 1.00 31.10 ? 336 VAL A CG2 1 ATOM 2586 N N . ILE A 1 337 ? 46.774 11.744 26.651 1.00 25.83 ? 337 ILE A N 1 ATOM 2587 C CA . ILE A 1 337 ? 45.404 11.228 26.629 1.00 25.01 ? 337 ILE A CA 1 ATOM 2588 C C . ILE A 1 337 ? 45.318 10.264 25.441 1.00 24.06 ? 337 ILE A C 1 ATOM 2589 O O . ILE A 1 337 ? 45.608 10.660 24.313 1.00 24.44 ? 337 ILE A O 1 ATOM 2590 C CB . ILE A 1 337 ? 44.357 12.372 26.508 1.00 23.97 ? 337 ILE A CB 1 ATOM 2591 C CG1 . ILE A 1 337 ? 44.366 13.243 27.783 1.00 24.53 ? 337 ILE A CG1 1 ATOM 2592 C CG2 . ILE A 1 337 ? 42.965 11.779 26.225 1.00 24.48 ? 337 ILE A CG2 1 ATOM 2593 C CD1 . ILE A 1 337 ? 43.610 14.547 27.651 1.00 25.43 ? 337 ILE A CD1 1 ATOM 2594 N N . PRO A 1 338 ? 44.954 8.995 25.691 1.00 23.87 ? 338 PRO A N 1 ATOM 2595 C CA . PRO A 1 338 ? 44.937 8.001 24.617 1.00 24.05 ? 338 PRO A CA 1 ATOM 2596 C C . PRO A 1 338 ? 43.747 8.169 23.670 1.00 24.31 ? 338 PRO A C 1 ATOM 2597 O O . PRO A 1 338 ? 42.690 8.683 24.080 1.00 23.49 ? 338 PRO A O 1 ATOM 2598 C CB . PRO A 1 338 ? 44.815 6.670 25.364 1.00 23.97 ? 338 PRO A CB 1 ATOM 2599 C CG . PRO A 1 338 ? 44.145 7.005 26.647 1.00 24.39 ? 338 PRO A CG 1 ATOM 2600 C CD . PRO A 1 338 ? 44.533 8.426 26.990 1.00 23.70 ? 338 PRO A CD 1 ATOM 2601 N N . MET A 1 339 ? 43.910 7.728 22.423 1.00 24.79 ? 339 MET A N 1 ATOM 2602 C CA . MET A 1 339 ? 42.789 7.717 21.478 1.00 25.89 ? 339 MET A CA 1 ATOM 2603 C C . MET A 1 339 ? 41.588 6.950 22.016 1.00 24.89 ? 339 MET A C 1 ATOM 2604 O O . MET A 1 339 ? 40.448 7.296 21.697 1.00 24.95 ? 339 MET A O 1 ATOM 2605 C CB . MET A 1 339 ? 43.176 7.088 20.146 1.00 26.80 ? 339 MET A CB 1 ATOM 2606 C CG . MET A 1 339 ? 43.276 8.016 18.962 1.00 31.44 ? 339 MET A CG 1 ATOM 2607 S SD . MET A 1 339 ? 41.994 9.287 18.696 1.00 36.66 ? 339 MET A SD 1 ATOM 2608 C CE . MET A 1 339 ? 42.957 10.590 19.364 1.00 33.64 ? 339 MET A CE 1 ATOM 2609 N N . SER A 1 340 ? 41.835 5.891 22.787 1.00 24.67 ? 340 SER A N 1 ATOM 2610 C CA . SER A 1 340 ? 40.734 5.100 23.352 1.00 24.46 ? 340 SER A CA 1 ATOM 2611 C C . SER A 1 340 ? 39.784 5.977 24.194 1.00 24.01 ? 340 SER A C 1 ATOM 2612 O O . SER A 1 340 ? 38.566 5.779 24.165 1.00 24.58 ? 340 SER A O 1 ATOM 2613 C CB . SER A 1 340 ? 41.265 3.911 24.167 1.00 24.32 ? 340 SER A CB 1 ATOM 2614 O OG . SER A 1 340 ? 42.039 4.344 25.269 1.00 25.16 ? 340 SER A OG 1 ATOM 2615 N N . ARG A 1 341 ? 40.349 6.947 24.913 1.00 23.38 ? 341 ARG A N 1 ATOM 2616 C CA . ARG A 1 341 ? 39.563 7.851 25.759 1.00 22.74 ? 341 ARG A CA 1 ATOM 2617 C C . ARG A 1 341 ? 38.716 8.782 24.889 1.00 22.22 ? 341 ARG A C 1 ATOM 2618 O O . ARG A 1 341 ? 37.501 8.918 25.099 1.00 22.18 ? 341 ARG A O 1 ATOM 2619 C CB . ARG A 1 341 ? 40.485 8.623 26.709 1.00 23.06 ? 341 ARG A CB 1 ATOM 2620 C CG . ARG A 1 341 ? 39.780 9.537 27.714 1.00 22.47 ? 341 ARG A CG 1 ATOM 2621 C CD . ARG A 1 341 ? 38.950 8.737 28.758 1.00 21.99 ? 341 ARG A CD 1 ATOM 2622 N NE . ARG A 1 341 ? 37.572 8.522 28.312 1.00 22.67 ? 341 ARG A NE 1 ATOM 2623 C CZ . ARG A 1 341 ? 36.643 9.481 28.289 1.00 21.69 ? 341 ARG A CZ 1 ATOM 2624 N NH1 . ARG A 1 341 ? 36.952 10.714 28.675 1.00 20.77 ? 341 ARG A NH1 1 ATOM 2625 N NH2 . ARG A 1 341 ? 35.419 9.204 27.877 1.00 21.16 ? 341 ARG A NH2 1 ATOM 2626 N N . ILE A 1 342 ? 39.349 9.379 23.876 1.00 21.76 ? 342 ILE A N 1 ATOM 2627 C CA . ILE A 1 342 ? 38.642 10.230 22.909 1.00 20.75 ? 342 ILE A CA 1 ATOM 2628 C C . ILE A 1 342 ? 37.538 9.433 22.218 1.00 20.76 ? 342 ILE A C 1 ATOM 2629 O O . ILE A 1 342 ? 36.397 9.917 22.108 1.00 20.13 ? 342 ILE A O 1 ATOM 2630 C CB . ILE A 1 342 ? 39.614 10.848 21.832 1.00 20.60 ? 342 ILE A CB 1 ATOM 2631 C CG1 . ILE A 1 342 ? 40.745 11.654 22.503 1.00 20.74 ? 342 ILE A CG1 1 ATOM 2632 C CG2 . ILE A 1 342 ? 38.842 11.676 20.791 1.00 20.86 ? 342 ILE A CG2 1 ATOM 2633 C CD1 . ILE A 1 342 ? 40.305 12.833 23.371 1.00 21.58 ? 342 ILE A CD1 1 ATOM 2634 N N . ASP A 1 343 ? 37.856 8.217 21.768 1.00 20.59 ? 343 ASP A N 1 ATOM 2635 C CA . ASP A 1 343 ? 36.871 7.400 21.045 1.00 21.17 ? 343 ASP A CA 1 ATOM 2636 C C . ASP A 1 343 ? 35.681 7.034 21.937 1.00 21.47 ? 343 ASP A C 1 ATOM 2637 O O . ASP A 1 343 ? 34.542 6.977 21.452 1.00 21.38 ? 343 ASP A O 1 ATOM 2638 C CB . ASP A 1 343 ? 37.510 6.131 20.468 1.00 22.05 ? 343 ASP A CB 1 ATOM 2639 C CG . ASP A 1 343 ? 38.379 6.415 19.240 1.00 22.88 ? 343 ASP A CG 1 ATOM 2640 O OD1 . ASP A 1 343 ? 38.376 7.571 18.757 1.00 22.73 ? 343 ASP A OD1 1 ATOM 2641 O OD2 . ASP A 1 343 ? 39.050 5.458 18.750 1.00 24.20 ? 343 ASP A OD2 1 ATOM 2642 N N . ASP A 1 344 ? 35.950 6.795 23.225 1.00 21.03 ? 344 ASP A N 1 ATOM 2643 C CA . ASP A 1 344 ? 34.876 6.494 24.170 1.00 21.33 ? 344 ASP A CA 1 ATOM 2644 C C . ASP A 1 344 ? 33.935 7.699 24.309 1.00 21.10 ? 344 ASP A C 1 ATOM 2645 O O . ASP A 1 344 ? 32.700 7.543 24.239 1.00 21.46 ? 344 ASP A O 1 ATOM 2646 C CB . ASP A 1 344 ? 35.442 6.076 25.532 1.00 21.44 ? 344 ASP A CB 1 ATOM 2647 C CG . ASP A 1 344 ? 34.350 5.891 26.581 1.00 22.20 ? 344 ASP A CG 1 ATOM 2648 O OD1 . ASP A 1 344 ? 33.486 5.003 26.407 1.00 23.13 ? 344 ASP A OD1 1 ATOM 2649 O OD2 . ASP A 1 344 ? 34.363 6.639 27.573 1.00 22.82 ? 344 ASP A OD2 1 ATOM 2650 N N . ALA A 1 345 ? 34.516 8.885 24.494 1.00 20.56 ? 345 ALA A N 1 ATOM 2651 C CA . ALA A 1 345 ? 33.720 10.114 24.679 1.00 19.71 ? 345 ALA A CA 1 ATOM 2652 C C . ALA A 1 345 ? 32.845 10.344 23.445 1.00 19.10 ? 345 ALA A C 1 ATOM 2653 O O . ALA A 1 345 ? 31.633 10.615 23.551 1.00 18.80 ? 345 ALA A O 1 ATOM 2654 C CB . ALA A 1 345 ? 34.623 11.320 24.918 1.00 19.67 ? 345 ALA A CB 1 ATOM 2655 N N . VAL A 1 346 ? 33.457 10.230 22.265 1.00 18.70 ? 346 VAL A N 1 ATOM 2656 C CA . VAL A 1 346 ? 32.713 10.449 21.025 1.00 18.46 ? 346 VAL A CA 1 ATOM 2657 C C . VAL A 1 346 ? 31.655 9.368 20.794 1.00 19.02 ? 346 VAL A C 1 ATOM 2658 O O . VAL A 1 346 ? 30.549 9.671 20.349 1.00 19.09 ? 346 VAL A O 1 ATOM 2659 C CB . VAL A 1 346 ? 33.663 10.616 19.797 1.00 18.39 ? 346 VAL A CB 1 ATOM 2660 C CG1 . VAL A 1 346 ? 32.834 10.726 18.513 1.00 18.81 ? 346 VAL A CG1 1 ATOM 2661 C CG2 . VAL A 1 346 ? 34.533 11.870 19.995 1.00 18.12 ? 346 VAL A CG2 1 ATOM 2662 N N . THR A 1 347 ? 31.973 8.121 21.128 1.00 18.54 ? 347 THR A N 1 ATOM 2663 C CA . THR A 1 347 ? 31.010 7.023 21.001 1.00 19.15 ? 347 THR A CA 1 ATOM 2664 C C . THR A 1 347 ? 29.731 7.364 21.782 1.00 19.08 ? 347 THR A C 1 ATOM 2665 O O . THR A 1 347 ? 28.628 7.211 21.274 1.00 19.12 ? 347 THR A O 1 ATOM 2666 C CB . THR A 1 347 ? 31.613 5.683 21.505 1.00 19.05 ? 347 THR A CB 1 ATOM 2667 O OG1 . THR A 1 347 ? 32.584 5.222 20.554 1.00 20.50 ? 347 THR A OG1 1 ATOM 2668 C CG2 . THR A 1 347 ? 30.533 4.602 21.677 1.00 19.61 ? 347 THR A CG2 1 ATOM 2669 N N . ARG A 1 348 ? 29.912 7.843 23.004 1.00 18.87 ? 348 ARG A N 1 ATOM 2670 C CA . ARG A 1 348 ? 28.780 8.147 23.906 1.00 18.30 ? 348 ARG A CA 1 ATOM 2671 C C . ARG A 1 348 ? 27.960 9.341 23.406 1.00 18.48 ? 348 ARG A C 1 ATOM 2672 O O . ARG A 1 348 ? 26.716 9.310 23.425 1.00 18.58 ? 348 ARG A O 1 ATOM 2673 C CB . ARG A 1 348 ? 29.331 8.406 25.302 1.00 18.30 ? 348 ARG A CB 1 ATOM 2674 C CG . ARG A 1 348 ? 29.848 7.119 25.959 1.00 19.33 ? 348 ARG A CG 1 ATOM 2675 C CD . ARG A 1 348 ? 30.815 7.389 27.097 1.00 19.06 ? 348 ARG A CD 1 ATOM 2676 N NE . ARG A 1 348 ? 31.135 6.114 27.739 1.00 20.81 ? 348 ARG A NE 1 ATOM 2677 C CZ . ARG A 1 348 ? 30.341 5.527 28.637 1.00 22.03 ? 348 ARG A CZ 1 ATOM 2678 N NH1 . ARG A 1 348 ? 29.202 6.122 29.017 1.00 21.33 ? 348 ARG A NH1 1 ATOM 2679 N NH2 . ARG A 1 348 ? 30.688 4.362 29.163 1.00 22.47 ? 348 ARG A NH2 1 ATOM 2680 N N . ILE A 1 349 ? 28.654 10.383 22.938 1.00 17.60 ? 349 ILE A N 1 ATOM 2681 C CA . ILE A 1 349 ? 27.976 11.560 22.397 1.00 17.64 ? 349 ILE A CA 1 ATOM 2682 C C . ILE A 1 349 ? 27.169 11.165 21.156 1.00 17.28 ? 349 ILE A C 1 ATOM 2683 O O . ILE A 1 349 ? 25.978 11.475 21.044 1.00 17.63 ? 349 ILE A O 1 ATOM 2684 C CB . ILE A 1 349 ? 28.979 12.698 22.087 1.00 17.23 ? 349 ILE A CB 1 ATOM 2685 C CG1 . ILE A 1 349 ? 29.622 13.190 23.411 1.00 16.66 ? 349 ILE A CG1 1 ATOM 2686 C CG2 . ILE A 1 349 ? 28.298 13.835 21.313 1.00 18.44 ? 349 ILE A CG2 1 ATOM 2687 C CD1 . ILE A 1 349 ? 30.917 14.023 23.217 1.00 17.69 ? 349 ILE A CD1 1 ATOM 2688 N N . LEU A 1 350 ? 27.815 10.481 20.212 1.00 17.62 ? 350 LEU A N 1 ATOM 2689 C CA . LEU A 1 350 ? 27.097 10.010 19.033 1.00 18.08 ? 350 LEU A CA 1 ATOM 2690 C C . LEU A 1 350 ? 25.954 9.059 19.394 1.00 18.33 ? 350 LEU A C 1 ATOM 2691 O O . LEU A 1 350 ? 24.880 9.116 18.782 1.00 18.98 ? 350 LEU A O 1 ATOM 2692 C CB . LEU A 1 350 ? 28.059 9.316 18.058 1.00 18.44 ? 350 LEU A CB 1 ATOM 2693 C CG . LEU A 1 350 ? 29.124 10.242 17.458 1.00 17.67 ? 350 LEU A CG 1 ATOM 2694 C CD1 . LEU A 1 350 ? 29.995 9.385 16.545 1.00 18.96 ? 350 LEU A CD1 1 ATOM 2695 C CD2 . LEU A 1 350 ? 28.529 11.428 16.693 1.00 18.37 ? 350 LEU A CD2 1 ATOM 2696 N N . ARG A 1 351 ? 26.188 8.166 20.356 1.00 18.77 ? 351 ARG A N 1 ATOM 2697 C CA . ARG A 1 351 ? 25.129 7.247 20.783 1.00 18.35 ? 351 ARG A CA 1 ATOM 2698 C C . ARG A 1 351 ? 23.866 8.044 21.180 1.00 18.06 ? 351 ARG A C 1 ATOM 2699 O O . ARG A 1 351 ? 22.770 7.743 20.720 1.00 18.27 ? 351 ARG A O 1 ATOM 2700 C CB . ARG A 1 351 ? 25.588 6.349 21.932 1.00 18.44 ? 351 ARG A CB 1 ATOM 2701 C CG . ARG A 1 351 ? 24.492 5.378 22.405 1.00 18.76 ? 351 ARG A CG 1 ATOM 2702 C CD . ARG A 1 351 ? 24.960 4.463 23.517 1.00 19.23 ? 351 ARG A CD 1 ATOM 2703 N NE . ARG A 1 351 ? 25.981 3.519 23.048 1.00 20.98 ? 351 ARG A NE 1 ATOM 2704 C CZ . ARG A 1 351 ? 27.220 3.407 23.530 1.00 20.66 ? 351 ARG A CZ 1 ATOM 2705 N NH1 . ARG A 1 351 ? 27.665 4.157 24.546 1.00 21.44 ? 351 ARG A NH1 1 ATOM 2706 N NH2 . ARG A 1 351 ? 28.043 2.523 22.969 1.00 23.46 ? 351 ARG A NH2 1 ATOM 2707 N N . VAL A 1 352 ? 24.033 9.084 21.985 1.00 17.02 ? 352 VAL A N 1 ATOM 2708 C CA . VAL A 1 352 ? 22.865 9.870 22.399 1.00 17.52 ? 352 VAL A CA 1 ATOM 2709 C C . VAL A 1 352 ? 22.203 10.533 21.186 1.00 17.57 ? 352 VAL A C 1 ATOM 2710 O O . VAL A 1 352 ? 20.970 10.477 21.021 1.00 18.61 ? 352 VAL A O 1 ATOM 2711 C CB . VAL A 1 352 ? 23.220 10.876 23.509 1.00 17.17 ? 352 VAL A CB 1 ATOM 2712 C CG1 . VAL A 1 352 ? 22.044 11.844 23.765 1.00 17.19 ? 352 VAL A CG1 1 ATOM 2713 C CG2 . VAL A 1 352 ? 23.652 10.107 24.783 1.00 17.66 ? 352 VAL A CG2 1 ATOM 2714 N N . LYS A 1 353 ? 23.025 11.128 20.316 1.00 17.42 ? 353 LYS A N 1 ATOM 2715 C CA . LYS A 1 353 ? 22.499 11.832 19.134 1.00 17.34 ? 353 LYS A CA 1 ATOM 2716 C C . LYS A 1 353 ? 21.733 10.900 18.185 1.00 17.91 ? 353 LYS A C 1 ATOM 2717 O O . LYS A 1 353 ? 20.636 11.240 17.728 1.00 17.61 ? 353 LYS A O 1 ATOM 2718 C CB . LYS A 1 353 ? 23.637 12.552 18.391 1.00 17.12 ? 353 LYS A CB 1 ATOM 2719 C CG . LYS A 1 353 ? 24.156 13.771 19.155 1.00 16.35 ? 353 LYS A CG 1 ATOM 2720 C CD . LYS A 1 353 ? 25.221 14.501 18.309 1.00 17.11 ? 353 LYS A CD 1 ATOM 2721 C CE . LYS A 1 353 ? 25.680 15.780 18.990 1.00 17.25 ? 353 LYS A CE 1 ATOM 2722 N NZ . LYS A 1 353 ? 26.661 16.547 18.132 1.00 16.22 ? 353 LYS A NZ 1 ATOM 2723 N N . PHE A 1 354 ? 22.292 9.731 17.872 1.00 19.23 ? 354 PHE A N 1 ATOM 2724 C CA . PHE A 1 354 ? 21.583 8.812 16.982 1.00 19.28 ? 354 PHE A CA 1 ATOM 2725 C C . PHE A 1 354 ? 20.299 8.293 17.650 1.00 19.48 ? 354 PHE A C 1 ATOM 2726 O O . PHE A 1 354 ? 19.245 8.227 17.015 1.00 19.81 ? 354 PHE A O 1 ATOM 2727 C CB . PHE A 1 354 ? 22.472 7.621 16.599 1.00 19.31 ? 354 PHE A CB 1 ATOM 2728 C CG . PHE A 1 354 ? 23.463 7.919 15.513 1.00 19.79 ? 354 PHE A CG 1 ATOM 2729 C CD1 . PHE A 1 354 ? 23.024 8.207 14.199 1.00 20.58 ? 354 PHE A CD1 1 ATOM 2730 C CD2 . PHE A 1 354 ? 24.834 7.897 15.785 1.00 19.97 ? 354 PHE A CD2 1 ATOM 2731 C CE1 . PHE A 1 354 ? 23.967 8.474 13.167 1.00 21.48 ? 354 PHE A CE1 1 ATOM 2732 C CE2 . PHE A 1 354 ? 25.766 8.157 14.762 1.00 21.21 ? 354 PHE A CE2 1 ATOM 2733 C CZ . PHE A 1 354 ? 25.325 8.444 13.469 1.00 20.15 ? 354 PHE A CZ 1 ATOM 2734 N N . THR A 1 355 ? 20.411 7.934 18.926 1.00 19.84 ? 355 THR A N 1 ATOM 2735 C CA . THR A 1 355 ? 19.287 7.320 19.671 1.00 20.32 ? 355 THR A CA 1 ATOM 2736 C C . THR A 1 355 ? 18.068 8.247 19.661 1.00 20.22 ? 355 THR A C 1 ATOM 2737 O O . THR A 1 355 ? 16.928 7.809 19.422 1.00 20.75 ? 355 THR A O 1 ATOM 2738 C CB . THR A 1 355 ? 19.715 6.945 21.118 1.00 20.00 ? 355 THR A CB 1 ATOM 2739 O OG1 . THR A 1 355 ? 20.718 5.925 21.046 1.00 21.78 ? 355 THR A OG1 1 ATOM 2740 C CG2 . THR A 1 355 ? 18.531 6.391 21.972 1.00 21.44 ? 355 THR A CG2 1 ATOM 2741 N N . MET A 1 356 ? 18.320 9.530 19.903 1.00 19.34 ? 356 MET A N 1 ATOM 2742 C CA . MET A 1 356 ? 17.240 10.504 20.038 1.00 19.30 ? 356 MET A CA 1 ATOM 2743 C C . MET A 1 356 ? 16.639 10.943 18.703 1.00 19.53 ? 356 MET A C 1 ATOM 2744 O O . MET A 1 356 ? 15.672 11.705 18.685 1.00 20.17 ? 356 MET A O 1 ATOM 2745 C CB . MET A 1 356 ? 17.746 11.716 20.849 1.00 19.12 ? 356 MET A CB 1 ATOM 2746 C CG . MET A 1 356 ? 18.668 12.644 20.065 1.00 18.34 ? 356 MET A CG 1 ATOM 2747 S SD . MET A 1 356 ? 19.426 13.872 21.149 1.00 19.57 ? 356 MET A SD 1 ATOM 2748 C CE . MET A 1 356 ? 18.010 14.925 21.508 1.00 20.73 ? 356 MET A CE 1 ATOM 2749 N N . GLY A 1 357 ? 17.222 10.492 17.590 1.00 19.37 ? 357 GLY A N 1 ATOM 2750 C CA . GLY A 1 357 ? 16.702 10.823 16.258 1.00 19.76 ? 357 GLY A CA 1 ATOM 2751 C C . GLY A 1 357 ? 17.248 12.118 15.671 1.00 19.60 ? 357 GLY A C 1 ATOM 2752 O O . GLY A 1 357 ? 16.716 12.632 14.681 1.00 20.13 ? 357 GLY A O 1 ATOM 2753 N N . LEU A 1 358 ? 18.317 12.648 16.276 1.00 19.10 ? 358 LEU A N 1 ATOM 2754 C CA . LEU A 1 358 ? 18.837 13.960 15.877 1.00 19.26 ? 358 LEU A CA 1 ATOM 2755 C C . LEU A 1 358 ? 19.336 13.990 14.418 1.00 19.50 ? 358 LEU A C 1 ATOM 2756 O O . LEU A 1 358 ? 19.258 15.029 13.776 1.00 19.72 ? 358 LEU A O 1 ATOM 2757 C CB . LEU A 1 358 ? 19.993 14.369 16.785 1.00 18.85 ? 358 LEU A CB 1 ATOM 2758 C CG . LEU A 1 358 ? 20.120 15.729 17.463 1.00 23.06 ? 358 LEU A CG 1 ATOM 2759 C CD1 . LEU A 1 358 ? 21.609 16.088 17.637 1.00 18.67 ? 358 LEU A CD1 1 ATOM 2760 C CD2 . LEU A 1 358 ? 19.222 16.893 17.024 1.00 21.06 ? 358 LEU A CD2 1 ATOM 2761 N N . PHE A 1 359 ? 19.851 12.862 13.924 1.00 20.15 ? 359 PHE A N 1 ATOM 2762 C CA . PHE A 1 359 ? 20.326 12.784 12.527 1.00 20.87 ? 359 PHE A CA 1 ATOM 2763 C C . PHE A 1 359 ? 19.146 12.786 11.547 1.00 21.74 ? 359 PHE A C 1 ATOM 2764 O O . PHE A 1 359 ? 19.309 13.162 10.377 1.00 22.68 ? 359 PHE A O 1 ATOM 2765 C CB . PHE A 1 359 ? 21.191 11.544 12.299 1.00 21.15 ? 359 PHE A CB 1 ATOM 2766 C CG . PHE A 1 359 ? 22.613 11.672 12.806 1.00 20.62 ? 359 PHE A CG 1 ATOM 2767 C CD1 . PHE A 1 359 ? 22.892 11.591 14.175 1.00 21.09 ? 359 PHE A CD1 1 ATOM 2768 C CD2 . PHE A 1 359 ? 23.678 11.858 11.908 1.00 21.55 ? 359 PHE A CD2 1 ATOM 2769 C CE1 . PHE A 1 359 ? 24.219 11.695 14.653 1.00 21.69 ? 359 PHE A CE1 1 ATOM 2770 C CE2 . PHE A 1 359 ? 24.997 11.963 12.367 1.00 20.75 ? 359 PHE A CE2 1 ATOM 2771 C CZ . PHE A 1 359 ? 25.273 11.876 13.750 1.00 21.29 ? 359 PHE A CZ 1 ATOM 2772 N N . GLU A 1 360 ? 17.974 12.365 12.023 1.00 22.29 ? 360 GLU A N 1 ATOM 2773 C CA . GLU A 1 360 ? 16.767 12.325 11.189 1.00 22.46 ? 360 GLU A CA 1 ATOM 2774 C C . GLU A 1 360 ? 15.968 13.616 11.260 1.00 22.62 ? 360 GLU A C 1 ATOM 2775 O O . GLU A 1 360 ? 15.331 14.029 10.279 1.00 23.58 ? 360 GLU A O 1 ATOM 2776 C CB . GLU A 1 360 ? 15.896 11.117 11.547 1.00 22.11 ? 360 GLU A CB 1 ATOM 2777 C CG . GLU A 1 360 ? 16.386 9.807 10.903 1.00 22.70 ? 360 GLU A CG 1 ATOM 2778 C CD . GLU A 1 360 ? 17.793 9.409 11.335 1.00 23.54 ? 360 GLU A CD 1 ATOM 2779 O OE1 . GLU A 1 360 ? 17.961 8.948 12.481 1.00 23.68 ? 360 GLU A OE1 1 ATOM 2780 O OE2 . GLU A 1 360 ? 18.727 9.534 10.510 1.00 24.99 ? 360 GLU A OE2 1 ATOM 2781 N N . ASN A 1 361 ? 16.003 14.264 12.421 1.00 22.29 ? 361 ASN A N 1 ATOM 2782 C CA . ASN A 1 361 ? 15.310 15.523 12.625 1.00 22.31 ? 361 ASN A CA 1 ATOM 2783 C C . ASN A 1 361 ? 16.212 16.547 13.289 1.00 21.75 ? 361 ASN A C 1 ATOM 2784 O O . ASN A 1 361 ? 16.008 16.902 14.457 1.00 22.08 ? 361 ASN A O 1 ATOM 2785 C CB . ASN A 1 361 ? 14.038 15.302 13.444 1.00 23.15 ? 361 ASN A CB 1 ATOM 2786 C CG . ASN A 1 361 ? 12.953 14.599 12.625 1.00 24.32 ? 361 ASN A CG 1 ATOM 2787 O OD1 . ASN A 1 361 ? 12.182 15.246 11.911 1.00 29.28 ? 361 ASN A OD1 1 ATOM 2788 N ND2 . ASN A 1 361 ? 12.924 13.289 12.695 1.00 24.35 ? 361 ASN A ND2 1 ATOM 2789 N N . PRO A 1 362 ? 17.213 17.034 12.540 1.00 21.44 ? 362 PRO A N 1 ATOM 2790 C CA . PRO A 1 362 ? 18.150 18.012 13.099 1.00 20.44 ? 362 PRO A CA 1 ATOM 2791 C C . PRO A 1 362 ? 17.552 19.415 13.250 1.00 20.45 ? 362 PRO A C 1 ATOM 2792 O O . PRO A 1 362 ? 18.105 20.248 13.986 1.00 20.33 ? 362 PRO A O 1 ATOM 2793 C CB . PRO A 1 362 ? 19.309 18.017 12.083 1.00 21.05 ? 362 PRO A CB 1 ATOM 2794 C CG . PRO A 1 362 ? 18.694 17.566 10.799 1.00 21.38 ? 362 PRO A CG 1 ATOM 2795 C CD . PRO A 1 362 ? 17.552 16.646 11.154 1.00 21.24 ? 362 PRO A CD 1 ATOM 2796 N N . TYR A 1 363 ? 16.438 19.688 12.568 1.00 20.53 ? 363 TYR A N 1 ATOM 2797 C CA . TYR A 1 363 ? 15.872 21.048 12.569 1.00 20.33 ? 363 TYR A CA 1 ATOM 2798 C C . TYR A 1 363 ? 14.564 21.159 13.361 1.00 20.53 ? 363 TYR A C 1 ATOM 2799 O O . TYR A 1 363 ? 13.898 20.158 13.618 1.00 21.04 ? 363 TYR A O 1 ATOM 2800 C CB . TYR A 1 363 ? 15.657 21.573 11.140 1.00 21.44 ? 363 TYR A CB 1 ATOM 2801 C CG . TYR A 1 363 ? 16.950 21.678 10.353 1.00 21.29 ? 363 TYR A CG 1 ATOM 2802 C CD1 . TYR A 1 363 ? 17.876 22.684 10.634 1.00 22.24 ? 363 TYR A CD1 1 ATOM 2803 C CD2 . TYR A 1 363 ? 17.247 20.765 9.355 1.00 23.54 ? 363 TYR A CD2 1 ATOM 2804 C CE1 . TYR A 1 363 ? 19.062 22.793 9.920 1.00 23.05 ? 363 TYR A CE1 1 ATOM 2805 C CE2 . TYR A 1 363 ? 18.439 20.851 8.641 1.00 23.73 ? 363 TYR A CE2 1 ATOM 2806 C CZ . TYR A 1 363 ? 19.335 21.865 8.926 1.00 23.89 ? 363 TYR A CZ 1 ATOM 2807 O OH . TYR A 1 363 ? 20.520 21.949 8.217 1.00 23.98 ? 363 TYR A OH 1 ATOM 2808 N N . ALA A 1 364 ? 14.233 22.386 13.739 1.00 20.08 ? 364 ALA A N 1 ATOM 2809 C CA . ALA A 1 364 ? 13.037 22.656 14.540 1.00 20.28 ? 364 ALA A CA 1 ATOM 2810 C C . ALA A 1 364 ? 11.763 22.393 13.739 1.00 20.77 ? 364 ALA A C 1 ATOM 2811 O O . ALA A 1 364 ? 11.758 22.432 12.495 1.00 21.31 ? 364 ALA A O 1 ATOM 2812 C CB . ALA A 1 364 ? 13.066 24.069 15.065 1.00 20.27 ? 364 ALA A CB 1 ATOM 2813 N N . ASP A 1 365 ? 10.684 22.104 14.466 1.00 21.04 ? 365 ASP A N 1 ATOM 2814 C CA . ASP A 1 365 ? 9.370 21.919 13.848 1.00 22.02 ? 365 ASP A CA 1 ATOM 2815 C C . ASP A 1 365 ? 8.522 23.157 14.104 1.00 22.35 ? 365 ASP A C 1 ATOM 2816 O O . ASP A 1 365 ? 8.109 23.391 15.240 1.00 21.59 ? 365 ASP A O 1 ATOM 2817 C CB . ASP A 1 365 ? 8.720 20.646 14.401 1.00 22.22 ? 365 ASP A CB 1 ATOM 2818 C CG . ASP A 1 365 ? 7.310 20.396 13.841 1.00 23.41 ? 365 ASP A CG 1 ATOM 2819 O OD1 . ASP A 1 365 ? 6.830 21.194 12.991 1.00 23.40 ? 365 ASP A OD1 1 ATOM 2820 O OD2 . ASP A 1 365 ? 6.685 19.393 14.280 1.00 26.10 ? 365 ASP A OD2 1 ATOM 2821 N N . PRO A 1 366 ? 8.238 23.950 13.051 1.00 23.34 ? 366 PRO A N 1 ATOM 2822 C CA . PRO A 1 366 ? 7.494 25.210 13.240 1.00 23.72 ? 366 PRO A CA 1 ATOM 2823 C C . PRO A 1 366 ? 6.110 24.996 13.865 1.00 23.42 ? 366 PRO A C 1 ATOM 2824 O O . PRO A 1 366 ? 5.609 25.890 14.581 1.00 23.99 ? 366 PRO A O 1 ATOM 2825 C CB . PRO A 1 366 ? 7.400 25.795 11.823 1.00 24.60 ? 366 PRO A CB 1 ATOM 2826 C CG . PRO A 1 366 ? 7.697 24.648 10.894 1.00 25.04 ? 366 PRO A CG 1 ATOM 2827 C CD . PRO A 1 366 ? 8.592 23.706 11.632 1.00 23.80 ? 366 PRO A CD 1 ATOM 2828 N N . ALA A 1 367 ? 5.528 23.819 13.626 1.00 23.33 ? 367 ALA A N 1 ATOM 2829 C CA . ALA A 1 367 ? 4.226 23.439 14.209 1.00 23.74 ? 367 ALA A CA 1 ATOM 2830 C C . ALA A 1 367 ? 4.260 23.313 15.734 1.00 23.84 ? 367 ALA A C 1 ATOM 2831 O O . ALA A 1 367 ? 3.212 23.294 16.384 1.00 24.68 ? 367 ALA A O 1 ATOM 2832 C CB . ALA A 1 367 ? 3.734 22.149 13.609 1.00 24.46 ? 367 ALA A CB 1 ATOM 2833 N N . MET A 1 368 ? 5.452 23.172 16.300 1.00 22.60 ? 368 MET A N 1 ATOM 2834 C CA . MET A 1 368 ? 5.580 23.048 17.758 1.00 22.42 ? 368 MET A CA 1 ATOM 2835 C C . MET A 1 368 ? 5.575 24.386 18.494 1.00 22.05 ? 368 MET A C 1 ATOM 2836 O O . MET A 1 368 ? 5.446 24.403 19.731 1.00 21.52 ? 368 MET A O 1 ATOM 2837 C CB . MET A 1 368 ? 6.821 22.227 18.118 1.00 22.44 ? 368 MET A CB 1 ATOM 2838 C CG . MET A 1 368 ? 6.722 20.782 17.678 1.00 25.99 ? 368 MET A CG 1 ATOM 2839 S SD . MET A 1 368 ? 5.564 19.855 18.729 1.00 32.58 ? 368 MET A SD 1 ATOM 2840 C CE . MET A 1 368 ? 6.579 19.732 20.227 1.00 30.27 ? 368 MET A CE 1 ATOM 2841 N N . ALA A 1 369 ? 5.715 25.501 17.765 1.00 21.34 ? 369 ALA A N 1 ATOM 2842 C CA . ALA A 1 369 ? 5.919 26.807 18.411 1.00 21.54 ? 369 ALA A CA 1 ATOM 2843 C C . ALA A 1 369 ? 4.779 27.118 19.372 1.00 21.87 ? 369 ALA A C 1 ATOM 2844 O O . ALA A 1 369 ? 5.005 27.662 20.449 1.00 21.68 ? 369 ALA A O 1 ATOM 2845 C CB . ALA A 1 369 ? 6.070 27.921 17.383 1.00 21.47 ? 369 ALA A CB 1 ATOM 2846 N N . GLU A 1 370 ? 3.569 26.723 18.984 1.00 22.41 ? 370 GLU A N 1 ATOM 2847 C CA . GLU A 1 370 ? 2.383 27.023 19.802 1.00 23.59 ? 370 GLU A CA 1 ATOM 2848 C C . GLU A 1 370 ? 2.270 26.220 21.102 1.00 22.75 ? 370 GLU A C 1 ATOM 2849 O O . GLU A 1 370 ? 1.381 26.489 21.917 1.00 23.75 ? 370 GLU A O 1 ATOM 2850 C CB A GLU A 1 370 ? 1.110 26.752 18.965 0.50 23.27 ? 370 GLU A CB 1 ATOM 2851 C CB B GLU A 1 370 ? 1.107 27.138 18.965 0.50 23.33 ? 370 GLU A CB 1 ATOM 2852 C CG A GLU A 1 370 ? 0.945 25.271 18.555 0.50 24.41 ? 370 GLU A CG 1 ATOM 2853 C CG B GLU A 1 370 ? 1.162 28.431 18.175 0.50 24.49 ? 370 GLU A CG 1 ATOM 2854 C CD A GLU A 1 370 ? -0.434 24.899 17.990 0.50 24.89 ? 370 GLU A CD 1 ATOM 2855 C CD B GLU A 1 370 ? -0.113 28.795 17.456 0.50 27.44 ? 370 GLU A CD 1 ATOM 2856 O OE1 A GLU A 1 370 ? -0.951 23.835 18.390 0.50 29.08 ? 370 GLU A OE1 1 ATOM 2857 O OE1 B GLU A 1 370 ? 0.019 29.449 16.397 0.50 28.05 ? 370 GLU A OE1 1 ATOM 2858 O OE2 A GLU A 1 370 ? -0.991 25.637 17.144 0.50 27.71 ? 370 GLU A OE2 1 ATOM 2859 O OE2 B GLU A 1 370 ? -1.219 28.463 17.940 0.50 24.91 ? 370 GLU A OE2 1 ATOM 2860 N N . GLN A 1 371 ? 3.170 25.249 21.304 1.00 21.08 ? 371 GLN A N 1 ATOM 2861 C CA . GLN A 1 371 ? 3.270 24.530 22.591 1.00 20.57 ? 371 GLN A CA 1 ATOM 2862 C C . GLN A 1 371 ? 3.743 25.441 23.728 1.00 20.60 ? 371 GLN A C 1 ATOM 2863 O O . GLN A 1 371 ? 3.492 25.156 24.917 1.00 20.69 ? 371 GLN A O 1 ATOM 2864 C CB . GLN A 1 371 ? 4.218 23.320 22.489 1.00 20.30 ? 371 GLN A CB 1 ATOM 2865 C CG . GLN A 1 371 ? 3.676 22.202 21.604 1.00 22.81 ? 371 GLN A CG 1 ATOM 2866 C CD . GLN A 1 371 ? 2.423 21.553 22.171 1.00 25.68 ? 371 GLN A CD 1 ATOM 2867 O OE1 . GLN A 1 371 ? 2.216 21.500 23.393 1.00 23.95 ? 371 GLN A OE1 1 ATOM 2868 N NE2 . GLN A 1 371 ? 1.553 21.076 21.273 1.00 29.67 ? 371 GLN A NE2 1 ATOM 2869 N N . LEU A 1 372 ? 4.428 26.523 23.365 1.00 20.39 ? 372 LEU A N 1 ATOM 2870 C CA . LEU A 1 372 ? 4.988 27.455 24.343 1.00 20.38 ? 372 LEU A CA 1 ATOM 2871 C C . LEU A 1 372 ? 3.880 28.184 25.117 1.00 20.76 ? 372 LEU A C 1 ATOM 2872 O O . LEU A 1 372 ? 3.025 28.865 24.523 1.00 21.55 ? 372 LEU A O 1 ATOM 2873 C CB . LEU A 1 372 ? 5.913 28.459 23.678 1.00 20.67 ? 372 LEU A CB 1 ATOM 2874 C CG . LEU A 1 372 ? 6.665 29.345 24.672 1.00 20.84 ? 372 LEU A CG 1 ATOM 2875 C CD1 . LEU A 1 372 ? 7.738 28.562 25.438 1.00 20.80 ? 372 LEU A CD1 1 ATOM 2876 C CD2 . LEU A 1 372 ? 7.273 30.566 23.974 1.00 22.38 ? 372 LEU A CD2 1 ATOM 2877 N N . GLY A 1 373 ? 3.873 28.010 26.440 1.00 19.95 ? 373 GLY A N 1 ATOM 2878 C CA . GLY A 1 373 ? 2.875 28.683 27.271 1.00 19.82 ? 373 GLY A CA 1 ATOM 2879 C C . GLY A 1 373 ? 1.462 28.178 27.022 1.00 20.11 ? 373 GLY A C 1 ATOM 2880 O O . GLY A 1 373 ? 0.489 28.874 27.343 1.00 20.61 ? 373 GLY A O 1 ATOM 2881 N N . LYS A 1 374 ? 1.333 26.977 26.464 1.00 20.68 ? 374 LYS A N 1 ATOM 2882 C CA . LYS A 1 374 ? 0.006 26.432 26.123 1.00 21.47 ? 374 LYS A CA 1 ATOM 2883 C C . LYS A 1 374 ? -0.883 26.348 27.381 1.00 20.69 ? 374 LYS A C 1 ATOM 2884 O O . LYS A 1 374 ? -0.435 25.920 28.448 1.00 19.92 ? 374 LYS A O 1 ATOM 2885 C CB . LYS A 1 374 ? 0.138 25.052 25.484 1.00 22.34 ? 374 LYS A CB 1 ATOM 2886 C CG . LYS A 1 374 ? -0.967 24.712 24.502 1.00 26.11 ? 374 LYS A CG 1 ATOM 2887 C CD . LYS A 1 374 ? -0.677 23.399 23.781 1.00 30.48 ? 374 LYS A CD 1 ATOM 2888 C CE . LYS A 1 374 ? -1.622 22.295 24.229 1.00 35.37 ? 374 LYS A CE 1 ATOM 2889 N NZ . LYS A 1 374 ? -1.580 21.089 23.339 1.00 37.92 ? 374 LYS A NZ 1 ATOM 2890 N N . GLN A 1 375 ? -2.139 26.760 27.257 1.00 20.03 ? 375 GLN A N 1 ATOM 2891 C CA . GLN A 1 375 ? -3.019 26.820 28.420 1.00 19.91 ? 375 GLN A CA 1 ATOM 2892 C C . GLN A 1 375 ? -3.132 25.503 29.197 1.00 20.03 ? 375 GLN A C 1 ATOM 2893 O O . GLN A 1 375 ? -3.163 25.506 30.427 1.00 20.20 ? 375 GLN A O 1 ATOM 2894 C CB . GLN A 1 375 ? -4.407 27.368 28.037 1.00 20.35 ? 375 GLN A CB 1 ATOM 2895 C CG . GLN A 1 375 ? -5.270 27.712 29.251 1.00 20.43 ? 375 GLN A CG 1 ATOM 2896 C CD . GLN A 1 375 ? -4.575 28.693 30.205 1.00 22.74 ? 375 GLN A CD 1 ATOM 2897 O OE1 . GLN A 1 375 ? -3.960 29.668 29.772 1.00 23.95 ? 375 GLN A OE1 1 ATOM 2898 N NE2 . GLN A 1 375 ? -4.694 28.438 31.514 1.00 23.50 ? 375 GLN A NE2 1 ATOM 2899 N N . GLU A 1 376 ? -3.160 24.369 28.496 1.00 19.62 ? 376 GLU A N 1 ATOM 2900 C CA . GLU A 1 376 ? -3.202 23.076 29.176 1.00 20.03 ? 376 GLU A CA 1 ATOM 2901 C C . GLU A 1 376 ? -1.991 22.898 30.110 1.00 19.25 ? 376 GLU A C 1 ATOM 2902 O O . GLU A 1 376 ? -2.108 22.288 31.189 1.00 19.37 ? 376 GLU A O 1 ATOM 2903 C CB . GLU A 1 376 ? -3.217 21.930 28.176 1.00 20.70 ? 376 GLU A CB 1 ATOM 2904 C CG . GLU A 1 376 ? -4.521 21.773 27.417 1.00 22.59 ? 376 GLU A CG 1 ATOM 2905 C CD . GLU A 1 376 ? -4.650 22.655 26.191 1.00 24.46 ? 376 GLU A CD 1 ATOM 2906 O OE1 . GLU A 1 376 ? -3.875 23.628 25.986 1.00 23.62 ? 376 GLU A OE1 1 ATOM 2907 O OE2 . GLU A 1 376 ? -5.570 22.361 25.399 1.00 29.64 ? 376 GLU A OE2 1 ATOM 2908 N N . HIS A 1 377 ? -0.830 23.413 29.689 1.00 18.28 ? 377 HIS A N 1 ATOM 2909 C CA . HIS A 1 377 ? 0.389 23.268 30.497 1.00 17.77 ? 377 HIS A CA 1 ATOM 2910 C C . HIS A 1 377 ? 0.265 24.184 31.719 1.00 17.85 ? 377 HIS A C 1 ATOM 2911 O O . HIS A 1 377 ? 0.725 23.861 32.824 1.00 17.83 ? 377 HIS A O 1 ATOM 2912 C CB . HIS A 1 377 ? 1.637 23.678 29.697 1.00 17.85 ? 377 HIS A CB 1 ATOM 2913 C CG . HIS A 1 377 ? 1.847 22.923 28.413 1.00 18.91 ? 377 HIS A CG 1 ATOM 2914 N ND1 . HIS A 1 377 ? 1.166 21.770 28.087 1.00 21.86 ? 377 HIS A ND1 1 ATOM 2915 C CD2 . HIS A 1 377 ? 2.705 23.155 27.387 1.00 16.28 ? 377 HIS A CD2 1 ATOM 2916 C CE1 . HIS A 1 377 ? 1.568 21.342 26.899 1.00 19.59 ? 377 HIS A CE1 1 ATOM 2917 N NE2 . HIS A 1 377 ? 2.509 22.160 26.460 1.00 22.59 ? 377 HIS A NE2 1 ATOM 2918 N N . ARG A 1 378 ? -0.333 25.353 31.511 1.00 17.77 ? 378 ARG A N 1 ATOM 2919 C CA . ARG A 1 378 ? -0.582 26.279 32.627 1.00 18.01 ? 378 ARG A CA 1 ATOM 2920 C C . ARG A 1 378 ? -1.560 25.661 33.631 1.00 18.27 ? 378 ARG A C 1 ATOM 2921 O O . ARG A 1 378 ? -1.379 25.793 34.857 1.00 18.36 ? 378 ARG A O 1 ATOM 2922 C CB . ARG A 1 378 ? -1.101 27.607 32.106 1.00 18.32 ? 378 ARG A CB 1 ATOM 2923 C CG . ARG A 1 378 ? -0.075 28.359 31.263 1.00 18.99 ? 378 ARG A CG 1 ATOM 2924 C CD . ARG A 1 378 ? -0.560 29.770 30.952 1.00 18.73 ? 378 ARG A CD 1 ATOM 2925 N NE . ARG A 1 378 ? 0.347 30.431 30.012 1.00 19.47 ? 378 ARG A NE 1 ATOM 2926 C CZ . ARG A 1 378 ? 1.459 31.074 30.347 1.00 19.71 ? 378 ARG A CZ 1 ATOM 2927 N NH1 . ARG A 1 378 ? 1.829 31.168 31.630 1.00 18.30 ? 378 ARG A NH1 1 ATOM 2928 N NH2 . ARG A 1 378 ? 2.203 31.635 29.393 1.00 20.32 ? 378 ARG A NH2 1 ATOM 2929 N N . ASP A 1 379 ? -2.586 24.974 33.125 1.00 18.15 ? 379 ASP A N 1 ATOM 2930 C CA . ASP A 1 379 ? -3.530 24.278 34.012 1.00 18.12 ? 379 ASP A CA 1 ATOM 2931 C C . ASP A 1 379 ? -2.790 23.233 34.859 1.00 18.21 ? 379 ASP A C 1 ATOM 2932 O O . ASP A 1 379 ? -3.075 23.064 36.048 1.00 18.17 ? 379 ASP A O 1 ATOM 2933 C CB . ASP A 1 379 ? -4.652 23.609 33.212 1.00 18.85 ? 379 ASP A CB 1 ATOM 2934 C CG . ASP A 1 379 ? -5.559 24.612 32.507 1.00 21.52 ? 379 ASP A CG 1 ATOM 2935 O OD1 . ASP A 1 379 ? -5.548 25.815 32.859 1.00 23.45 ? 379 ASP A OD1 1 ATOM 2936 O OD2 . ASP A 1 379 ? -6.298 24.172 31.577 1.00 26.72 ? 379 ASP A OD2 1 ATOM 2937 N N . LEU A 1 380 ? -1.815 22.557 34.246 1.00 17.61 ? 380 LEU A N 1 ATOM 2938 C CA . LEU A 1 380 ? -0.982 21.590 34.953 1.00 17.19 ? 380 LEU A CA 1 ATOM 2939 C C . LEU A 1 380 ? -0.114 22.274 36.020 1.00 16.96 ? 380 LEU A C 1 ATOM 2940 O O . LEU A 1 380 ? -0.032 21.784 37.152 1.00 16.58 ? 380 LEU A O 1 ATOM 2941 C CB . LEU A 1 380 ? -0.094 20.817 33.973 1.00 17.75 ? 380 LEU A CB 1 ATOM 2942 C CG . LEU A 1 380 ? 0.899 19.812 34.570 1.00 17.54 ? 380 LEU A CG 1 ATOM 2943 C CD1 . LEU A 1 380 ? 0.184 18.710 35.309 1.00 19.25 ? 380 LEU A CD1 1 ATOM 2944 C CD2 . LEU A 1 380 ? 1.804 19.222 33.465 1.00 18.33 ? 380 LEU A CD2 1 ATOM 2945 N N . ALA A 1 381 ? 0.505 23.401 35.660 1.00 16.44 ? 381 ALA A N 1 ATOM 2946 C CA . ALA A 1 381 ? 1.343 24.167 36.604 1.00 16.52 ? 381 ALA A CA 1 ATOM 2947 C C . ALA A 1 381 ? 0.485 24.627 37.787 1.00 16.70 ? 381 ALA A C 1 ATOM 2948 O O . ALA A 1 381 ? 0.931 24.626 38.935 1.00 17.11 ? 381 ALA A O 1 ATOM 2949 C CB . ALA A 1 381 ? 1.972 25.357 35.917 1.00 16.52 ? 381 ALA A CB 1 ATOM 2950 N N . ARG A 1 382 ? -0.739 25.046 37.480 1.00 16.75 ? 382 ARG A N 1 ATOM 2951 C CA . ARG A 1 382 ? -1.688 25.492 38.500 1.00 16.82 ? 382 ARG A CA 1 ATOM 2952 C C . ARG A 1 382 ? -2.034 24.360 39.484 1.00 17.14 ? 382 ARG A C 1 ATOM 2953 O O . ARG A 1 382 ? -2.067 24.573 40.700 1.00 17.42 ? 382 ARG A O 1 ATOM 2954 C CB . ARG A 1 382 ? -2.926 26.048 37.791 1.00 15.72 ? 382 ARG A CB 1 ATOM 2955 C CG . ARG A 1 382 ? -4.077 26.443 38.718 1.00 16.23 ? 382 ARG A CG 1 ATOM 2956 C CD . ARG A 1 382 ? -5.172 27.053 37.874 1.00 18.02 ? 382 ARG A CD 1 ATOM 2957 N NE . ARG A 1 382 ? -6.310 27.400 38.716 1.00 19.37 ? 382 ARG A NE 1 ATOM 2958 C CZ . ARG A 1 382 ? -7.375 28.049 38.273 1.00 23.48 ? 382 ARG A CZ 1 ATOM 2959 N NH1 . ARG A 1 382 ? -7.447 28.412 36.980 1.00 24.39 ? 382 ARG A NH1 1 ATOM 2960 N NH2 . ARG A 1 382 ? -8.367 28.335 39.114 1.00 25.15 ? 382 ARG A NH2 1 ATOM 2961 N N . GLU A 1 383 ? -2.295 23.164 38.953 1.00 17.73 ? 383 GLU A N 1 ATOM 2962 C CA . GLU A 1 383 ? -2.494 21.954 39.764 1.00 18.41 ? 383 GLU A CA 1 ATOM 2963 C C . GLU A 1 383 ? -1.259 21.689 40.644 1.00 17.18 ? 383 GLU A C 1 ATOM 2964 O O . GLU A 1 383 ? -1.384 21.455 41.857 1.00 17.41 ? 383 GLU A O 1 ATOM 2965 C CB . GLU A 1 383 ? -2.756 20.740 38.853 1.00 18.47 ? 383 GLU A CB 1 ATOM 2966 C CG . GLU A 1 383 ? -2.839 19.403 39.601 1.00 20.07 ? 383 GLU A CG 1 ATOM 2967 C CD . GLU A 1 383 ? -2.929 18.205 38.671 1.00 21.73 ? 383 GLU A CD 1 ATOM 2968 O OE1 . GLU A 1 383 ? -3.249 18.399 37.474 1.00 26.30 ? 383 GLU A OE1 1 ATOM 2969 O OE2 . GLU A 1 383 ? -2.688 17.077 39.137 1.00 25.61 ? 383 GLU A OE2 1 ATOM 2970 N N . ALA A 1 384 ? -0.066 21.744 40.048 1.00 16.79 ? 384 ALA A N 1 ATOM 2971 C CA . ALA A 1 384 ? 1.182 21.484 40.789 1.00 16.83 ? 384 ALA A CA 1 ATOM 2972 C C . ALA A 1 384 ? 1.392 22.506 41.917 1.00 16.44 ? 384 ALA A C 1 ATOM 2973 O O . ALA A 1 384 ? 1.758 22.137 43.042 1.00 16.42 ? 384 ALA A O 1 ATOM 2974 C CB . ALA A 1 384 ? 2.375 21.499 39.830 1.00 17.18 ? 384 ALA A CB 1 ATOM 2975 N N . ALA A 1 385 ? 1.160 23.781 41.611 1.00 16.43 ? 385 ALA A N 1 ATOM 2976 C CA . ALA A 1 385 ? 1.337 24.867 42.600 1.00 16.31 ? 385 ALA A CA 1 ATOM 2977 C C . ALA A 1 385 ? 0.418 24.577 43.791 1.00 16.66 ? 385 ALA A C 1 ATOM 2978 O O . ALA A 1 385 ? 0.847 24.621 44.947 1.00 17.33 ? 385 ALA A O 1 ATOM 2979 C CB . ALA A 1 385 ? 0.992 26.220 41.987 1.00 16.49 ? 385 ALA A CB 1 ATOM 2980 N N . ARG A 1 386 ? -0.838 24.258 43.495 1.00 16.12 ? 386 ARG A N 1 ATOM 2981 C CA . ARG A 1 386 ? -1.819 24.013 44.559 1.00 16.80 ? 386 ARG A CA 1 ATOM 2982 C C . ARG A 1 386 ? -1.430 22.803 45.403 1.00 16.75 ? 386 ARG A C 1 ATOM 2983 O O . ARG A 1 386 ? -1.488 22.861 46.641 1.00 18.27 ? 386 ARG A O 1 ATOM 2984 C CB . ARG A 1 386 ? -3.205 23.846 43.946 1.00 16.70 ? 386 ARG A CB 1 ATOM 2985 C CG . ARG A 1 386 ? -4.319 23.553 44.962 1.00 20.34 ? 386 ARG A CG 1 ATOM 2986 C CD . ARG A 1 386 ? -4.700 22.069 44.926 1.00 25.95 ? 386 ARG A CD 1 ATOM 2987 N NE . ARG A 1 386 ? -5.164 21.607 43.612 1.00 27.94 ? 386 ARG A NE 1 ATOM 2988 C CZ . ARG A 1 386 ? -5.476 20.341 43.337 1.00 29.91 ? 386 ARG A CZ 1 ATOM 2989 N NH1 . ARG A 1 386 ? -5.396 19.410 44.286 1.00 30.76 ? 386 ARG A NH1 1 ATOM 2990 N NH2 . ARG A 1 386 ? -5.879 20.010 42.116 1.00 30.68 ? 386 ARG A NH2 1 ATOM 2991 N N . LYS A 1 387 ? -0.980 21.732 44.746 1.00 16.93 ? 387 LYS A N 1 ATOM 2992 C CA . LYS A 1 387 ? -0.576 20.521 45.462 1.00 17.62 ? 387 LYS A CA 1 ATOM 2993 C C . LYS A 1 387 ? 0.704 20.702 46.283 1.00 16.83 ? 387 LYS A C 1 ATOM 2994 O O . LYS A 1 387 ? 0.944 19.951 47.234 1.00 17.81 ? 387 LYS A O 1 ATOM 2995 C CB . LYS A 1 387 ? -0.410 19.358 44.482 1.00 18.16 ? 387 LYS A CB 1 ATOM 2996 C CG . LYS A 1 387 ? -1.755 18.835 43.995 1.00 18.53 ? 387 LYS A CG 1 ATOM 2997 C CD . LYS A 1 387 ? -1.602 17.721 42.982 1.00 21.06 ? 387 LYS A CD 1 ATOM 2998 C CE . LYS A 1 387 ? -2.963 17.104 42.685 1.00 23.68 ? 387 LYS A CE 1 ATOM 2999 N NZ . LYS A 1 387 ? -2.814 15.937 41.742 1.00 25.02 ? 387 LYS A NZ 1 ATOM 3000 N N . SER A 1 388 ? 1.531 21.675 45.905 1.00 16.24 ? 388 SER A N 1 ATOM 3001 C CA . SER A 1 388 ? 2.826 21.885 46.576 1.00 16.19 ? 388 SER A CA 1 ATOM 3002 C C . SER A 1 388 ? 2.664 22.633 47.903 1.00 16.34 ? 388 SER A C 1 ATOM 3003 O O . SER A 1 388 ? 3.579 22.646 48.729 1.00 17.03 ? 388 SER A O 1 ATOM 3004 C CB . SER A 1 388 ? 3.785 22.682 45.680 1.00 16.42 ? 388 SER A CB 1 ATOM 3005 O OG . SER A 1 388 ? 3.404 24.047 45.616 1.00 15.66 ? 388 SER A OG 1 ATOM 3006 N N . LEU A 1 389 ? 1.534 23.323 48.067 1.00 16.31 ? 389 LEU A N 1 ATOM 3007 C CA . LEU A 1 389 ? 1.351 24.208 49.238 1.00 16.23 ? 389 LEU A CA 1 ATOM 3008 C C . LEU A 1 389 ? 1.286 23.389 50.521 1.00 16.13 ? 389 LEU A C 1 ATOM 3009 O O . LEU A 1 389 ? 0.565 22.378 50.585 1.00 17.08 ? 389 LEU A O 1 ATOM 3010 C CB . LEU A 1 389 ? 0.056 25.012 49.121 1.00 16.28 ? 389 LEU A CB 1 ATOM 3011 C CG . LEU A 1 389 ? -0.220 25.791 47.835 1.00 16.09 ? 389 LEU A CG 1 ATOM 3012 C CD1 . LEU A 1 389 ? -1.617 26.436 47.907 1.00 17.40 ? 389 LEU A CD1 1 ATOM 3013 C CD2 . LEU A 1 389 ? 0.887 26.831 47.563 1.00 15.85 ? 389 LEU A CD2 1 ATOM 3014 N N . VAL A 1 390 ? 2.022 23.825 51.537 1.00 15.95 ? 390 VAL A N 1 ATOM 3015 C CA . VAL A 1 390 ? 1.941 23.145 52.843 1.00 16.43 ? 390 VAL A CA 1 ATOM 3016 C C . VAL A 1 390 ? 1.334 24.087 53.881 1.00 16.76 ? 390 VAL A C 1 ATOM 3017 O O . VAL A 1 390 ? 1.869 25.156 54.171 1.00 17.22 ? 390 VAL A O 1 ATOM 3018 C CB . VAL A 1 390 ? 3.316 22.589 53.327 1.00 16.62 ? 390 VAL A CB 1 ATOM 3019 C CG1 . VAL A 1 390 ? 3.156 21.910 54.715 1.00 17.26 ? 390 VAL A CG1 1 ATOM 3020 C CG2 . VAL A 1 390 ? 3.901 21.583 52.299 1.00 16.70 ? 390 VAL A CG2 1 ATOM 3021 N N . LEU A 1 391 ? 0.196 23.686 54.416 1.00 17.22 ? 391 LEU A N 1 ATOM 3022 C CA . LEU A 1 391 ? -0.507 24.487 55.424 1.00 17.23 ? 391 LEU A CA 1 ATOM 3023 C C . LEU A 1 391 ? 0.146 24.208 56.788 1.00 18.18 ? 391 LEU A C 1 ATOM 3024 O O . LEU A 1 391 ? 0.100 23.062 57.289 1.00 19.16 ? 391 LEU A O 1 ATOM 3025 C CB . LEU A 1 391 ? -1.979 24.077 55.437 1.00 17.41 ? 391 LEU A CB 1 ATOM 3026 C CG . LEU A 1 391 ? -2.922 24.833 56.380 1.00 18.09 ? 391 LEU A CG 1 ATOM 3027 C CD1 . LEU A 1 391 ? -2.899 26.327 56.063 1.00 19.13 ? 391 LEU A CD1 1 ATOM 3028 C CD2 . LEU A 1 391 ? -4.334 24.280 56.261 1.00 17.60 ? 391 LEU A CD2 1 ATOM 3029 N N . LEU A 1 392 ? 0.762 25.231 57.368 1.00 18.16 ? 392 LEU A N 1 ATOM 3030 C CA . LEU A 1 392 ? 1.494 25.069 58.633 1.00 19.01 ? 392 LEU A CA 1 ATOM 3031 C C . LEU A 1 392 ? 0.671 25.463 59.856 1.00 19.61 ? 392 LEU A C 1 ATOM 3032 O O . LEU A 1 392 ? 0.942 25.003 60.961 1.00 21.03 ? 392 LEU A O 1 ATOM 3033 C CB . LEU A 1 392 ? 2.797 25.868 58.607 1.00 19.05 ? 392 LEU A CB 1 ATOM 3034 C CG . LEU A 1 392 ? 3.877 25.437 57.591 1.00 19.65 ? 392 LEU A CG 1 ATOM 3035 C CD1 . LEU A 1 392 ? 5.087 26.360 57.685 1.00 22.93 ? 392 LEU A CD1 1 ATOM 3036 C CD2 . LEU A 1 392 ? 4.267 23.948 57.785 1.00 21.93 ? 392 LEU A CD2 1 ATOM 3037 N N . LYS A 1 393 ? -0.319 26.323 59.649 1.00 18.96 ? 393 LYS A N 1 ATOM 3038 C CA . LYS A 1 393 ? -1.154 26.848 60.746 1.00 19.20 ? 393 LYS A CA 1 ATOM 3039 C C . LYS A 1 393 ? -2.498 27.227 60.155 1.00 19.28 ? 393 LYS A C 1 ATOM 3040 O O . LYS A 1 393 ? -2.557 27.780 59.059 1.00 19.11 ? 393 LYS A O 1 ATOM 3041 C CB . LYS A 1 393 ? -0.497 28.089 61.354 1.00 19.24 ? 393 LYS A CB 1 ATOM 3042 C CG . LYS A 1 393 ? -1.204 28.637 62.593 1.00 20.02 ? 393 LYS A CG 1 ATOM 3043 C CD . LYS A 1 393 ? -0.478 29.826 63.182 1.00 20.03 ? 393 LYS A CD 1 ATOM 3044 C CE . LYS A 1 393 ? -1.230 30.342 64.400 1.00 20.80 ? 393 LYS A CE 1 ATOM 3045 N NZ . LYS A 1 393 ? -0.481 31.418 65.100 1.00 21.00 ? 393 LYS A NZ 1 ATOM 3046 N N . ASN A 1 394 ? -3.574 26.968 60.893 1.00 19.54 ? 394 ASN A N 1 ATOM 3047 C CA . ASN A 1 394 ? -4.910 27.348 60.428 1.00 20.35 ? 394 ASN A CA 1 ATOM 3048 C C . ASN A 1 394 ? -5.800 27.629 61.640 1.00 21.39 ? 394 ASN A C 1 ATOM 3049 O O . ASN A 1 394 ? -6.754 26.896 61.882 1.00 23.92 ? 394 ASN A O 1 ATOM 3050 C CB . ASN A 1 394 ? -5.513 26.234 59.549 1.00 20.53 ? 394 ASN A CB 1 ATOM 3051 C CG . ASN A 1 394 ? -6.759 26.677 58.782 1.00 20.67 ? 394 ASN A CG 1 ATOM 3052 O OD1 . ASN A 1 394 ? -7.513 25.834 58.249 1.00 23.47 ? 394 ASN A OD1 1 ATOM 3053 N ND2 . ASN A 1 394 ? -6.983 27.982 58.709 1.00 19.26 ? 394 ASN A ND2 1 ATOM 3054 N N . GLY A 1 395 ? -5.444 28.663 62.392 1.00 22.33 ? 395 GLY A N 1 ATOM 3055 C CA . GLY A 1 395 ? -6.136 29.065 63.629 1.00 23.41 ? 395 GLY A CA 1 ATOM 3056 C C . GLY A 1 395 ? -5.129 29.238 64.758 1.00 24.65 ? 395 GLY A C 1 ATOM 3057 O O . GLY A 1 395 ? -4.223 28.430 64.909 1.00 25.07 ? 395 GLY A O 1 ATOM 3058 N N . LYS A 1 396 ? -5.299 30.280 65.568 1.00 26.01 ? 396 LYS A N 1 ATOM 3059 C CA . LYS A 1 396 ? -4.329 30.586 66.636 1.00 27.54 ? 396 LYS A CA 1 ATOM 3060 C C . LYS A 1 396 ? -4.448 29.701 67.873 1.00 28.36 ? 396 LYS A C 1 ATOM 3061 O O . LYS A 1 396 ? -3.490 29.565 68.636 1.00 29.02 ? 396 LYS A O 1 ATOM 3062 C CB . LYS A 1 396 ? -4.440 32.056 67.047 1.00 27.80 ? 396 LYS A CB 1 ATOM 3063 C CG . LYS A 1 396 ? -4.003 33.027 65.958 1.00 28.47 ? 396 LYS A CG 1 ATOM 3064 C CD . LYS A 1 396 ? -3.871 34.456 66.455 1.00 29.02 ? 396 LYS A CD 1 ATOM 3065 C CE . LYS A 1 396 ? -3.311 35.371 65.366 1.00 30.58 ? 396 LYS A CE 1 ATOM 3066 N NZ . LYS A 1 396 ? -3.341 36.813 65.769 1.00 31.79 ? 396 LYS A NZ 1 ATOM 3067 N N . THR A 1 397 ? -5.634 29.139 68.089 1.00 28.49 ? 397 THR A N 1 ATOM 3068 C CA . THR A 1 397 ? -5.894 28.278 69.233 1.00 29.34 ? 397 THR A CA 1 ATOM 3069 C C . THR A 1 397 ? -6.767 27.120 68.772 1.00 30.51 ? 397 THR A C 1 ATOM 3070 O O . THR A 1 397 ? -7.400 27.187 67.701 1.00 30.90 ? 397 THR A O 1 ATOM 3071 C CB . THR A 1 397 ? -6.612 29.045 70.399 1.00 29.02 ? 397 THR A CB 1 ATOM 3072 O OG1 . THR A 1 397 ? -8.021 29.108 70.149 1.00 28.86 ? 397 THR A OG1 1 ATOM 3073 C CG2 . THR A 1 397 ? -6.070 30.473 70.564 1.00 29.41 ? 397 THR A CG2 1 ATOM 3074 N N . SER A 1 398 ? -6.828 26.073 69.586 1.00 31.11 ? 398 SER A N 1 ATOM 3075 C CA . SER A 1 398 ? -7.676 24.921 69.306 1.00 31.68 ? 398 SER A CA 1 ATOM 3076 C C . SER A 1 398 ? -9.174 25.259 69.348 1.00 31.61 ? 398 SER A C 1 ATOM 3077 O O . SER A 1 398 ? -9.994 24.455 68.900 1.00 33.12 ? 398 SER A O 1 ATOM 3078 C CB . SER A 1 398 ? -7.368 23.804 70.306 1.00 32.46 ? 398 SER A CB 1 ATOM 3079 O OG . SER A 1 398 ? -7.651 24.233 71.631 1.00 34.09 ? 398 SER A OG 1 ATOM 3080 N N . THR A 1 399 ? -9.522 26.420 69.911 1.00 30.08 ? 399 THR A N 1 ATOM 3081 C CA . THR A 1 399 ? -10.920 26.874 70.021 1.00 29.10 ? 399 THR A CA 1 ATOM 3082 C C . THR A 1 399 ? -11.330 27.705 68.797 1.00 26.35 ? 399 THR A C 1 ATOM 3083 O O . THR A 1 399 ? -12.518 27.867 68.533 1.00 25.26 ? 399 THR A O 1 ATOM 3084 C CB . THR A 1 399 ? -11.178 27.710 71.326 1.00 29.59 ? 399 THR A CB 1 ATOM 3085 O OG1 . THR A 1 399 ? -10.898 26.902 72.466 1.00 34.77 ? 399 THR A OG1 1 ATOM 3086 C CG2 . THR A 1 399 ? -12.683 28.219 71.440 1.00 30.34 ? 399 THR A CG2 1 ATOM 3087 N N . ASP A 1 400 ? -10.355 28.242 68.060 1.00 24.03 ? 400 ASP A N 1 ATOM 3088 C CA . ASP A 1 400 ? -10.676 29.176 66.972 1.00 22.17 ? 400 ASP A CA 1 ATOM 3089 C C . ASP A 1 400 ? -11.343 28.493 65.781 1.00 21.69 ? 400 ASP A C 1 ATOM 3090 O O . ASP A 1 400 ? -11.046 27.334 65.481 1.00 21.69 ? 400 ASP A O 1 ATOM 3091 C CB . ASP A 1 400 ? -9.398 29.864 66.461 1.00 22.12 ? 400 ASP A CB 1 ATOM 3092 C CG . ASP A 1 400 ? -8.872 30.944 67.410 1.00 23.73 ? 400 ASP A CG 1 ATOM 3093 O OD1 . ASP A 1 400 ? -9.311 31.022 68.580 1.00 24.73 ? 400 ASP A OD1 1 ATOM 3094 O OD2 . ASP A 1 400 ? -8.004 31.725 66.982 1.00 24.67 ? 400 ASP A OD2 1 ATOM 3095 N N . ALA A 1 401 ? -12.233 29.217 65.103 1.00 20.84 ? 401 ALA A N 1 ATOM 3096 C CA . ALA A 1 401 ? -12.744 28.785 63.800 1.00 20.91 ? 401 ALA A CA 1 ATOM 3097 C C . ALA A 1 401 ? -11.541 28.711 62.836 1.00 21.69 ? 401 ALA A C 1 ATOM 3098 O O . ALA A 1 401 ? -10.699 29.610 62.839 1.00 21.47 ? 401 ALA A O 1 ATOM 3099 C CB . ALA A 1 401 ? -13.766 29.797 63.265 1.00 21.10 ? 401 ALA A CB 1 ATOM 3100 N N . PRO A 1 402 ? -11.460 27.648 62.026 1.00 22.30 ? 402 PRO A N 1 ATOM 3101 C CA . PRO A 1 402 ? -10.393 27.629 60.991 1.00 22.88 ? 402 PRO A CA 1 ATOM 3102 C C . PRO A 1 402 ? -10.560 28.818 60.039 1.00 22.65 ? 402 PRO A C 1 ATOM 3103 O O . PRO A 1 402 ? -11.674 29.082 59.582 1.00 22.78 ? 402 PRO A O 1 ATOM 3104 C CB . PRO A 1 402 ? -10.632 26.303 60.247 1.00 23.59 ? 402 PRO A CB 1 ATOM 3105 C CG . PRO A 1 402 ? -12.032 25.874 60.607 1.00 25.07 ? 402 PRO A CG 1 ATOM 3106 C CD . PRO A 1 402 ? -12.314 26.445 61.986 1.00 23.54 ? 402 PRO A CD 1 ATOM 3107 N N . LEU A 1 403 ? -9.468 29.526 59.742 1.00 21.63 ? 403 LEU A N 1 ATOM 3108 C CA . LEU A 1 403 ? -9.527 30.667 58.813 1.00 21.93 ? 403 LEU A CA 1 ATOM 3109 C C . LEU A 1 403 ? -9.726 30.178 57.369 1.00 20.82 ? 403 LEU A C 1 ATOM 3110 O O . LEU A 1 403 ? -10.540 30.739 56.606 1.00 19.95 ? 403 LEU A O 1 ATOM 3111 C CB . LEU A 1 403 ? -8.264 31.547 58.904 1.00 21.76 ? 403 LEU A CB 1 ATOM 3112 C CG . LEU A 1 403 ? -8.302 32.778 57.962 1.00 23.43 ? 403 LEU A CG 1 ATOM 3113 C CD1 . LEU A 1 403 ? -9.522 33.733 58.212 1.00 24.37 ? 403 LEU A CD1 1 ATOM 3114 C CD2 . LEU A 1 403 ? -6.999 33.570 57.984 1.00 23.99 ? 403 LEU A CD2 1 ATOM 3115 N N . LEU A 1 404 ? -8.964 29.148 57.005 1.00 20.52 ? 404 LEU A N 1 ATOM 3116 C CA . LEU A 1 404 ? -9.042 28.578 55.652 1.00 20.38 ? 404 LEU A CA 1 ATOM 3117 C C . LEU A 1 404 ? -9.932 27.342 55.633 1.00 20.84 ? 404 LEU A C 1 ATOM 3118 O O . LEU A 1 404 ? -9.864 26.531 56.547 1.00 20.87 ? 404 LEU A O 1 ATOM 3119 C CB . LEU A 1 404 ? -7.637 28.215 55.139 1.00 20.22 ? 404 LEU A CB 1 ATOM 3120 C CG . LEU A 1 404 ? -6.614 29.356 55.186 1.00 20.24 ? 404 LEU A CG 1 ATOM 3121 C CD1 . LEU A 1 404 ? -5.227 28.843 54.691 1.00 20.70 ? 404 LEU A CD1 1 ATOM 3122 C CD2 . LEU A 1 404 ? -7.052 30.591 54.408 1.00 19.89 ? 404 LEU A CD2 1 ATOM 3123 N N . PRO A 1 405 ? -10.748 27.177 54.578 1.00 21.79 ? 405 PRO A N 1 ATOM 3124 C CA . PRO A 1 405 ? -10.855 28.086 53.415 1.00 21.93 ? 405 PRO A CA 1 ATOM 3125 C C . PRO A 1 405 ? -11.618 29.399 53.641 1.00 21.44 ? 405 PRO A C 1 ATOM 3126 O O . PRO A 1 405 ? -12.586 29.463 54.428 1.00 22.10 ? 405 PRO A O 1 ATOM 3127 C CB . PRO A 1 405 ? -11.564 27.232 52.340 1.00 22.37 ? 405 PRO A CB 1 ATOM 3128 C CG . PRO A 1 405 ? -12.146 26.055 53.058 1.00 24.14 ? 405 PRO A CG 1 ATOM 3129 C CD . PRO A 1 405 ? -11.628 25.994 54.477 1.00 22.24 ? 405 PRO A CD 1 ATOM 3130 N N . LEU A 1 406 ? -11.165 30.439 52.945 1.00 20.63 ? 406 LEU A N 1 ATOM 3131 C CA . LEU A 1 406 ? -11.772 31.755 52.985 1.00 20.74 ? 406 LEU A CA 1 ATOM 3132 C C . LEU A 1 406 ? -13.014 31.800 52.103 1.00 20.75 ? 406 LEU A C 1 ATOM 3133 O O . LEU A 1 406 ? -13.050 31.142 51.067 1.00 20.76 ? 406 LEU A O 1 ATOM 3134 C CB . LEU A 1 406 ? -10.775 32.790 52.466 1.00 21.00 ? 406 LEU A CB 1 ATOM 3135 C CG . LEU A 1 406 ? -9.475 32.962 53.263 1.00 23.24 ? 406 LEU A CG 1 ATOM 3136 C CD1 . LEU A 1 406 ? -8.464 33.788 52.447 1.00 24.92 ? 406 LEU A CD1 1 ATOM 3137 C CD2 . LEU A 1 406 ? -9.768 33.619 54.586 1.00 23.91 ? 406 LEU A CD2 1 ATOM 3138 N N . PRO A 1 407 ? -14.016 32.616 52.489 1.00 20.93 ? 407 PRO A N 1 ATOM 3139 C CA . PRO A 1 407 ? -15.184 32.814 51.620 1.00 20.37 ? 407 PRO A CA 1 ATOM 3140 C C . PRO A 1 407 ? -14.858 33.722 50.420 1.00 20.20 ? 407 PRO A C 1 ATOM 3141 O O . PRO A 1 407 ? -14.189 34.751 50.561 1.00 20.14 ? 407 PRO A O 1 ATOM 3142 C CB . PRO A 1 407 ? -16.207 33.483 52.553 1.00 20.71 ? 407 PRO A CB 1 ATOM 3143 C CG . PRO A 1 407 ? -15.369 34.252 53.523 1.00 21.26 ? 407 PRO A CG 1 ATOM 3144 C CD . PRO A 1 407 ? -14.111 33.401 53.734 1.00 20.96 ? 407 PRO A CD 1 ATOM 3145 N N . LYS A 1 408 ? -15.332 33.327 49.237 1.00 20.31 ? 408 LYS A N 1 ATOM 3146 C CA . LYS A 1 408 ? -15.193 34.153 48.040 1.00 19.90 ? 408 LYS A CA 1 ATOM 3147 C C . LYS A 1 408 ? -16.065 35.421 48.043 1.00 19.86 ? 408 LYS A C 1 ATOM 3148 O O . LYS A 1 408 ? -15.761 36.388 47.338 1.00 19.80 ? 408 LYS A O 1 ATOM 3149 C CB . LYS A 1 408 ? -15.483 33.330 46.781 1.00 20.24 ? 408 LYS A CB 1 ATOM 3150 C CG . LYS A 1 408 ? -14.493 32.192 46.553 1.00 20.23 ? 408 LYS A CG 1 ATOM 3151 C CD . LYS A 1 408 ? -14.893 31.416 45.292 1.00 21.55 ? 408 LYS A CD 1 ATOM 3152 C CE . LYS A 1 408 ? -13.959 30.262 45.045 1.00 23.43 ? 408 LYS A CE 1 ATOM 3153 N NZ . LYS A 1 408 ? -14.412 29.453 43.861 1.00 23.70 ? 408 LYS A NZ 1 ATOM 3154 N N . LYS A 1 409 ? -17.131 35.402 48.835 1.00 20.00 ? 409 LYS A N 1 ATOM 3155 C CA . LYS A 1 409 ? -18.026 36.548 48.961 1.00 21.14 ? 409 LYS A CA 1 ATOM 3156 C C . LYS A 1 409 ? -17.825 37.207 50.329 1.00 20.89 ? 409 LYS A C 1 ATOM 3157 O O . LYS A 1 409 ? -18.109 36.607 51.372 1.00 22.12 ? 409 LYS A O 1 ATOM 3158 C CB . LYS A 1 409 ? -19.489 36.121 48.803 1.00 21.93 ? 409 LYS A CB 1 ATOM 3159 C CG . LYS A 1 409 ? -20.437 37.325 48.689 1.00 23.92 ? 409 LYS A CG 1 ATOM 3160 C CD . LYS A 1 409 ? -21.837 36.913 48.242 1.00 28.39 ? 409 LYS A CD 1 ATOM 3161 C CE . LYS A 1 409 ? -22.679 38.160 48.151 1.00 31.18 ? 409 LYS A CE 1 ATOM 3162 N NZ . LYS A 1 409 ? -24.118 37.885 47.850 1.00 34.61 ? 409 LYS A NZ 1 ATOM 3163 N N . ALA A 1 410 ? -17.341 38.440 50.299 1.00 21.08 ? 410 ALA A N 1 ATOM 3164 C CA . ALA A 1 410 ? -17.146 39.265 51.496 1.00 21.03 ? 410 ALA A CA 1 ATOM 3165 C C . ALA A 1 410 ? -17.216 40.728 51.046 1.00 21.52 ? 410 ALA A C 1 ATOM 3166 O O . ALA A 1 410 ? -16.896 41.040 49.903 1.00 21.36 ? 410 ALA A O 1 ATOM 3167 C CB . ALA A 1 410 ? -15.790 38.957 52.150 1.00 20.88 ? 410 ALA A CB 1 ATOM 3168 N N . PRO A 1 411 ? -17.671 41.638 51.921 1.00 21.11 ? 411 PRO A N 1 ATOM 3169 C CA . PRO A 1 411 ? -17.791 43.026 51.456 1.00 21.05 ? 411 PRO A CA 1 ATOM 3170 C C . PRO A 1 411 ? -16.479 43.626 50.960 1.00 20.67 ? 411 PRO A C 1 ATOM 3171 O O . PRO A 1 411 ? -16.453 44.282 49.925 1.00 21.19 ? 411 PRO A O 1 ATOM 3172 C CB . PRO A 1 411 ? -18.296 43.768 52.708 1.00 21.38 ? 411 PRO A CB 1 ATOM 3173 C CG . PRO A 1 411 ? -19.050 42.688 53.471 1.00 22.29 ? 411 PRO A CG 1 ATOM 3174 C CD . PRO A 1 411 ? -18.167 41.470 53.304 1.00 21.65 ? 411 PRO A CD 1 ATOM 3175 N N . LYS A 1 412 ? -15.391 43.391 51.685 1.00 20.96 ? 412 LYS A N 1 ATOM 3176 C CA . LYS A 1 412 ? -14.131 44.036 51.354 1.00 20.26 ? 412 LYS A CA 1 ATOM 3177 C C . LYS A 1 412 ? -13.021 43.197 51.934 1.00 20.11 ? 412 LYS A C 1 ATOM 3178 O O . LYS A 1 412 ? -13.117 42.740 53.089 1.00 19.67 ? 412 LYS A O 1 ATOM 3179 C CB . LYS A 1 412 ? -14.095 45.433 51.958 1.00 21.58 ? 412 LYS A CB 1 ATOM 3180 C CG . LYS A 1 412 ? -13.010 46.341 51.451 1.00 23.82 ? 412 LYS A CG 1 ATOM 3181 C CD . LYS A 1 412 ? -13.276 47.714 52.077 1.00 26.37 ? 412 LYS A CD 1 ATOM 3182 C CE . LYS A 1 412 ? -12.184 48.691 51.811 1.00 28.58 ? 412 LYS A CE 1 ATOM 3183 N NZ . LYS A 1 412 ? -12.463 49.925 52.598 1.00 29.00 ? 412 LYS A NZ 1 ATOM 3184 N N . ILE A 1 413 ? -11.989 42.961 51.121 1.00 18.94 ? 413 ILE A N 1 ATOM 3185 C CA . ILE A 1 413 ? -10.834 42.163 51.573 1.00 18.67 ? 413 ILE A CA 1 ATOM 3186 C C . ILE A 1 413 ? -9.528 42.884 51.228 1.00 18.53 ? 413 ILE A C 1 ATOM 3187 O O . ILE A 1 413 ? -9.488 43.744 50.334 1.00 19.02 ? 413 ILE A O 1 ATOM 3188 C CB . ILE A 1 413 ? -10.848 40.706 51.019 1.00 18.26 ? 413 ILE A CB 1 ATOM 3189 C CG1 . ILE A 1 413 ? -10.585 40.701 49.506 1.00 17.62 ? 413 ILE A CG1 1 ATOM 3190 C CG2 . ILE A 1 413 ? -12.185 39.963 51.346 1.00 18.74 ? 413 ILE A CG2 1 ATOM 3191 C CD1 . ILE A 1 413 ? -10.423 39.306 48.923 1.00 19.03 ? 413 ILE A CD1 1 ATOM 3192 N N . LEU A 1 414 ? -8.465 42.564 51.967 1.00 17.88 ? 414 LEU A N 1 ATOM 3193 C CA . LEU A 1 414 ? -7.165 43.175 51.744 1.00 18.17 ? 414 LEU A CA 1 ATOM 3194 C C . LEU A 1 414 ? -6.159 42.155 51.239 1.00 17.94 ? 414 LEU A C 1 ATOM 3195 O O . LEU A 1 414 ? -6.059 41.049 51.796 1.00 17.71 ? 414 LEU A O 1 ATOM 3196 C CB . LEU A 1 414 ? -6.633 43.751 53.064 1.00 18.23 ? 414 LEU A CB 1 ATOM 3197 C CG . LEU A 1 414 ? -5.235 44.375 53.026 1.00 18.81 ? 414 LEU A CG 1 ATOM 3198 C CD1 . LEU A 1 414 ? -5.142 45.579 52.075 1.00 18.58 ? 414 LEU A CD1 1 ATOM 3199 C CD2 . LEU A 1 414 ? -4.819 44.769 54.472 1.00 18.80 ? 414 LEU A CD2 1 ATOM 3200 N N . VAL A 1 415 ? -5.425 42.523 50.190 1.00 17.42 ? 415 VAL A N 1 ATOM 3201 C CA . VAL A 1 415 ? -4.303 41.700 49.714 1.00 17.89 ? 415 VAL A CA 1 ATOM 3202 C C . VAL A 1 415 ? -3.073 42.578 49.911 1.00 17.65 ? 415 VAL A C 1 ATOM 3203 O O . VAL A 1 415 ? -3.054 43.736 49.488 1.00 18.66 ? 415 VAL A O 1 ATOM 3204 C CB . VAL A 1 415 ? -4.485 41.247 48.228 1.00 17.75 ? 415 VAL A CB 1 ATOM 3205 C CG1 . VAL A 1 415 ? -3.221 40.556 47.708 1.00 18.24 ? 415 VAL A CG1 1 ATOM 3206 C CG2 . VAL A 1 415 ? -5.712 40.318 48.079 1.00 17.98 ? 415 VAL A CG2 1 ATOM 3207 N N . ALA A 1 416 ? -2.050 42.056 50.579 1.00 17.24 ? 416 ALA A N 1 ATOM 3208 C CA . ALA A 1 416 ? -0.908 42.888 50.947 1.00 16.89 ? 416 ALA A CA 1 ATOM 3209 C C . ALA A 1 416 ? 0.406 42.115 50.877 1.00 16.85 ? 416 ALA A C 1 ATOM 3210 O O . ALA A 1 416 ? 0.415 40.879 50.804 1.00 17.31 ? 416 ALA A O 1 ATOM 3211 C CB . ALA A 1 416 ? -1.086 43.450 52.383 1.00 17.43 ? 416 ALA A CB 1 ATOM 3212 N N . GLY A 1 417 ? 1.510 42.852 50.978 1.00 17.31 ? 417 GLY A N 1 ATOM 3213 C CA . GLY A 1 417 ? 2.833 42.235 51.075 1.00 17.35 ? 417 GLY A CA 1 ATOM 3214 C C . GLY A 1 417 ? 3.620 42.370 49.773 1.00 18.35 ? 417 GLY A C 1 ATOM 3215 O O . GLY A 1 417 ? 3.041 42.483 48.674 1.00 18.17 ? 417 GLY A O 1 ATOM 3216 N N . SER A 1 418 ? 4.943 42.355 49.918 1.00 17.91 ? 418 SER A N 1 ATOM 3217 C CA . SER A 1 418 ? 5.901 42.480 48.811 1.00 18.52 ? 418 SER A CA 1 ATOM 3218 C C . SER A 1 418 ? 5.762 41.368 47.775 1.00 18.19 ? 418 SER A C 1 ATOM 3219 O O . SER A 1 418 ? 6.214 41.529 46.644 1.00 19.92 ? 418 SER A O 1 ATOM 3220 C CB . SER A 1 418 ? 7.334 42.418 49.370 1.00 19.16 ? 418 SER A CB 1 ATOM 3221 O OG . SER A 1 418 ? 7.498 41.224 50.110 1.00 20.63 ? 418 SER A OG 1 ATOM 3222 N N . HIS A 1 419 ? 5.176 40.235 48.169 1.00 17.62 ? 419 HIS A N 1 ATOM 3223 C CA . HIS A 1 419 ? 5.092 39.083 47.265 1.00 17.57 ? 419 HIS A CA 1 ATOM 3224 C C . HIS A 1 419 ? 3.678 38.853 46.725 1.00 17.75 ? 419 HIS A C 1 ATOM 3225 O O . HIS A 1 419 ? 3.434 37.859 46.037 1.00 17.80 ? 419 HIS A O 1 ATOM 3226 C CB . HIS A 1 419 ? 5.632 37.819 47.944 1.00 17.52 ? 419 HIS A CB 1 ATOM 3227 C CG . HIS A 1 419 ? 7.122 37.828 48.140 1.00 17.36 ? 419 HIS A CG 1 ATOM 3228 N ND1 . HIS A 1 419 ? 7.794 38.833 48.816 1.00 18.16 ? 419 HIS A ND1 1 ATOM 3229 C CD2 . HIS A 1 419 ? 8.069 36.937 47.752 1.00 17.32 ? 419 HIS A CD2 1 ATOM 3230 C CE1 . HIS A 1 419 ? 9.091 38.559 48.830 1.00 18.65 ? 419 HIS A CE1 1 ATOM 3231 N NE2 . HIS A 1 419 ? 9.283 37.410 48.204 1.00 17.84 ? 419 HIS A NE2 1 ATOM 3232 N N . ALA A 1 420 ? 2.743 39.754 47.054 1.00 17.69 ? 420 ALA A N 1 ATOM 3233 C CA . ALA A 1 420 ? 1.344 39.583 46.608 1.00 17.45 ? 420 ALA A CA 1 ATOM 3234 C C . ALA A 1 420 ? 1.135 39.889 45.125 1.00 17.80 ? 420 ALA A C 1 ATOM 3235 O O . ALA A 1 420 ? 0.240 39.307 44.483 1.00 18.06 ? 420 ALA A O 1 ATOM 3236 C CB . ALA A 1 420 ? 0.388 40.429 47.452 1.00 18.11 ? 420 ALA A CB 1 ATOM 3237 N N . ASP A 1 421 ? 1.953 40.782 44.576 1.00 17.52 ? 421 ASP A N 1 ATOM 3238 C CA . ASP A 1 421 ? 1.777 41.203 43.174 1.00 18.58 ? 421 ASP A CA 1 ATOM 3239 C C . ASP A 1 421 ? 3.135 41.337 42.517 1.00 18.90 ? 421 ASP A C 1 ATOM 3240 O O . ASP A 1 421 ? 3.499 42.395 42.004 1.00 20.11 ? 421 ASP A O 1 ATOM 3241 C CB . ASP A 1 421 ? 1.001 42.525 43.094 1.00 18.85 ? 421 ASP A CB 1 ATOM 3242 C CG . ASP A 1 421 ? 0.523 42.843 41.668 1.00 19.71 ? 421 ASP A CG 1 ATOM 3243 O OD1 . ASP A 1 421 ? 0.164 41.908 40.909 1.00 21.44 ? 421 ASP A OD1 1 ATOM 3244 O OD2 . ASP A 1 421 ? 0.512 44.031 41.307 1.00 23.54 ? 421 ASP A OD2 1 ATOM 3245 N N . ASN A 1 422 ? 3.881 40.245 42.540 1.00 18.05 ? 422 ASN A N 1 ATOM 3246 C CA . ASN A 1 422 ? 5.241 40.247 42.011 1.00 17.50 ? 422 ASN A CA 1 ATOM 3247 C C . ASN A 1 422 ? 5.532 38.886 41.390 1.00 17.27 ? 422 ASN A C 1 ATOM 3248 O O . ASN A 1 422 ? 5.872 37.914 42.077 1.00 17.25 ? 422 ASN A O 1 ATOM 3249 C CB . ASN A 1 422 ? 6.280 40.627 43.080 1.00 17.15 ? 422 ASN A CB 1 ATOM 3250 C CG . ASN A 1 422 ? 7.644 40.910 42.472 1.00 17.90 ? 422 ASN A CG 1 ATOM 3251 O OD1 . ASN A 1 422 ? 8.057 40.231 41.537 1.00 16.51 ? 422 ASN A OD1 1 ATOM 3252 N ND2 . ASN A 1 422 ? 8.346 41.935 42.987 1.00 17.82 ? 422 ASN A ND2 1 ATOM 3253 N N . LEU A 1 423 ? 5.328 38.822 40.077 1.00 17.12 ? 423 LEU A N 1 ATOM 3254 C CA . LEU A 1 423 ? 5.439 37.559 39.350 1.00 16.96 ? 423 LEU A CA 1 ATOM 3255 C C . LEU A 1 423 ? 6.857 37.000 39.449 1.00 16.56 ? 423 LEU A C 1 ATOM 3256 O O . LEU A 1 423 ? 7.041 35.797 39.692 1.00 16.45 ? 423 LEU A O 1 ATOM 3257 C CB . LEU A 1 423 ? 5.041 37.768 37.877 1.00 16.93 ? 423 LEU A CB 1 ATOM 3258 C CG . LEU A 1 423 ? 4.957 36.490 37.054 1.00 18.24 ? 423 LEU A CG 1 ATOM 3259 C CD1 . LEU A 1 423 ? 3.918 35.549 37.611 1.00 20.43 ? 423 LEU A CD1 1 ATOM 3260 C CD2 . LEU A 1 423 ? 4.624 36.836 35.599 1.00 18.42 ? 423 LEU A CD2 1 ATOM 3261 N N . GLY A 1 424 ? 7.861 37.862 39.278 1.00 16.67 ? 424 GLY A N 1 ATOM 3262 C CA . GLY A 1 424 ? 9.260 37.431 39.395 1.00 17.13 ? 424 GLY A CA 1 ATOM 3263 C C . GLY A 1 424 ? 9.554 36.806 40.764 1.00 16.56 ? 424 GLY A C 1 ATOM 3264 O O . GLY A 1 424 ? 10.199 35.753 40.851 1.00 17.18 ? 424 GLY A O 1 ATOM 3265 N N . TYR A 1 425 ? 9.022 37.411 41.831 1.00 16.24 ? 425 TYR A N 1 ATOM 3266 C CA . TYR A 1 425 ? 9.272 36.869 43.175 1.00 15.88 ? 425 TYR A CA 1 ATOM 3267 C C . TYR A 1 425 ? 8.630 35.500 43.336 1.00 16.79 ? 425 TYR A C 1 ATOM 3268 O O . TYR A 1 425 ? 9.198 34.618 43.986 1.00 17.35 ? 425 TYR A O 1 ATOM 3269 C CB . TYR A 1 425 ? 8.723 37.812 44.241 1.00 17.14 ? 425 TYR A CB 1 ATOM 3270 C CG . TYR A 1 425 ? 9.588 39.002 44.559 1.00 17.10 ? 425 TYR A CG 1 ATOM 3271 C CD1 . TYR A 1 425 ? 10.739 39.323 43.801 1.00 17.38 ? 425 TYR A CD1 1 ATOM 3272 C CD2 . TYR A 1 425 ? 9.249 39.830 45.633 1.00 18.76 ? 425 TYR A CD2 1 ATOM 3273 C CE1 . TYR A 1 425 ? 11.534 40.436 44.124 1.00 19.58 ? 425 TYR A CE1 1 ATOM 3274 C CE2 . TYR A 1 425 ? 10.011 40.957 45.943 1.00 20.54 ? 425 TYR A CE2 1 ATOM 3275 C CZ . TYR A 1 425 ? 11.154 41.243 45.196 1.00 19.00 ? 425 TYR A CZ 1 ATOM 3276 O OH . TYR A 1 425 ? 11.918 42.334 45.534 1.00 21.28 ? 425 TYR A OH 1 ATOM 3277 N N . GLN A 1 426 ? 7.437 35.318 42.763 1.00 16.26 ? 426 GLN A N 1 ATOM 3278 C CA . GLN A 1 426 ? 6.778 34.032 42.956 1.00 17.55 ? 426 GLN A CA 1 ATOM 3279 C C . GLN A 1 426 ? 7.425 32.917 42.126 1.00 16.40 ? 426 GLN A C 1 ATOM 3280 O O . GLN A 1 426 ? 7.231 31.738 42.425 1.00 16.87 ? 426 GLN A O 1 ATOM 3281 C CB . GLN A 1 426 ? 5.263 34.091 42.766 1.00 19.35 ? 426 GLN A CB 1 ATOM 3282 C CG . GLN A 1 426 ? 4.789 34.223 41.395 1.00 20.52 ? 426 GLN A CG 1 ATOM 3283 C CD . GLN A 1 426 ? 3.256 34.373 41.347 1.00 20.82 ? 426 GLN A CD 1 ATOM 3284 O OE1 . GLN A 1 426 ? 2.674 35.209 42.058 1.00 21.21 ? 426 GLN A OE1 1 ATOM 3285 N NE2 . GLN A 1 426 ? 2.609 33.571 40.521 1.00 18.62 ? 426 GLN A NE2 1 ATOM 3286 N N . CYS A 1 427 ? 8.193 33.294 41.101 1.00 15.70 ? 427 CYS A N 1 ATOM 3287 C CA . CYS A 1 427 ? 8.896 32.294 40.277 1.00 15.83 ? 427 CYS A CA 1 ATOM 3288 C C . CYS A 1 427 ? 10.290 31.943 40.826 1.00 15.84 ? 427 CYS A C 1 ATOM 3289 O O . CYS A 1 427 ? 10.782 30.818 40.634 1.00 15.87 ? 427 CYS A O 1 ATOM 3290 C CB . CYS A 1 427 ? 9.039 32.814 38.830 1.00 16.41 ? 427 CYS A CB 1 ATOM 3291 S SG . CYS A 1 427 ? 7.452 32.865 37.933 1.00 18.25 ? 427 CYS A SG 1 ATOM 3292 N N . GLY A 1 428 ? 10.941 32.916 41.472 1.00 15.56 ? 428 GLY A N 1 ATOM 3293 C CA . GLY A 1 428 ? 12.284 32.694 42.030 1.00 16.03 ? 428 GLY A CA 1 ATOM 3294 C C . GLY A 1 428 ? 13.360 32.586 40.933 1.00 16.08 ? 428 GLY A C 1 ATOM 3295 O O . GLY A 1 428 ? 13.167 33.048 39.783 1.00 16.37 ? 428 GLY A O 1 ATOM 3296 N N . GLY A 1 429 ? 14.504 31.999 41.291 1.00 16.22 ? 429 GLY A N 1 ATOM 3297 C CA . GLY A 1 429 ? 15.656 31.942 40.380 1.00 16.12 ? 429 GLY A CA 1 ATOM 3298 C C . GLY A 1 429 ? 15.377 31.097 39.138 1.00 16.01 ? 429 GLY A C 1 ATOM 3299 O O . GLY A 1 429 ? 14.349 30.397 39.058 1.00 15.28 ? 429 GLY A O 1 ATOM 3300 N N . TRP A 1 430 ? 16.302 31.157 38.176 1.00 15.64 ? 430 TRP A N 1 ATOM 3301 C CA . TRP A 1 430 ? 16.166 30.437 36.909 1.00 16.10 ? 430 TRP A CA 1 ATOM 3302 C C . TRP A 1 430 ? 14.818 30.777 36.268 1.00 16.27 ? 430 TRP A C 1 ATOM 3303 O O . TRP A 1 430 ? 14.070 29.883 35.874 1.00 15.61 ? 430 TRP A O 1 ATOM 3304 C CB . TRP A 1 430 ? 16.238 28.907 37.094 1.00 16.98 ? 430 TRP A CB 1 ATOM 3305 C CG . TRP A 1 430 ? 17.551 28.356 37.485 1.00 17.19 ? 430 TRP A CG 1 ATOM 3306 C CD1 . TRP A 1 430 ? 17.877 27.756 38.678 1.00 18.27 ? 430 TRP A CD1 1 ATOM 3307 C CD2 . TRP A 1 430 ? 18.728 28.278 36.663 1.00 16.99 ? 430 TRP A CD2 1 ATOM 3308 N NE1 . TRP A 1 430 ? 19.198 27.338 38.656 1.00 18.04 ? 430 TRP A NE1 1 ATOM 3309 C CE2 . TRP A 1 430 ? 19.745 27.648 37.438 1.00 18.27 ? 430 TRP A CE2 1 ATOM 3310 C CE3 . TRP A 1 430 ? 19.037 28.711 35.362 1.00 18.03 ? 430 TRP A CE3 1 ATOM 3311 C CZ2 . TRP A 1 430 ? 21.045 27.434 36.943 1.00 19.32 ? 430 TRP A CZ2 1 ATOM 3312 C CZ3 . TRP A 1 430 ? 20.328 28.492 34.868 1.00 17.84 ? 430 TRP A CZ3 1 ATOM 3313 C CH2 . TRP A 1 430 ? 21.315 27.856 35.659 1.00 18.30 ? 430 TRP A CH2 1 ATOM 3314 N N . THR A 1 431 ? 14.493 32.063 36.207 1.00 16.12 ? 431 THR A N 1 ATOM 3315 C CA . THR A 1 431 ? 13.278 32.492 35.497 1.00 16.15 ? 431 THR A CA 1 ATOM 3316 C C . THR A 1 431 ? 13.606 33.763 34.731 1.00 16.65 ? 431 THR A C 1 ATOM 3317 O O . THR A 1 431 ? 13.802 34.817 35.342 1.00 16.57 ? 431 THR A O 1 ATOM 3318 C CB . THR A 1 431 ? 12.086 32.760 36.474 1.00 15.54 ? 431 THR A CB 1 ATOM 3319 O OG1 . THR A 1 431 ? 11.953 31.658 37.400 1.00 16.00 ? 431 THR A OG1 1 ATOM 3320 C CG2 . THR A 1 431 ? 10.781 32.929 35.648 1.00 16.35 ? 431 THR A CG2 1 ATOM 3321 N N . ILE A 1 432 ? 13.668 33.618 33.398 1.00 16.07 ? 432 ILE A N 1 ATOM 3322 C CA . ILE A 1 432 ? 13.985 34.684 32.436 1.00 17.29 ? 432 ILE A CA 1 ATOM 3323 C C . ILE A 1 432 ? 15.462 35.078 32.533 1.00 17.40 ? 432 ILE A C 1 ATOM 3324 O O . ILE A 1 432 ? 16.201 34.984 31.543 1.00 19.23 ? 432 ILE A O 1 ATOM 3325 C CB . ILE A 1 432 ? 13.046 35.896 32.549 1.00 17.33 ? 432 ILE A CB 1 ATOM 3326 C CG1 . ILE A 1 432 ? 11.581 35.474 32.322 1.00 17.49 ? 432 ILE A CG1 1 ATOM 3327 C CG2 . ILE A 1 432 ? 13.474 36.994 31.576 1.00 18.14 ? 432 ILE A CG2 1 ATOM 3328 C CD1 . ILE A 1 432 ? 11.229 34.819 30.967 1.00 18.81 ? 432 ILE A CD1 1 ATOM 3329 N N . GLU A 1 433 ? 15.887 35.493 33.725 1.00 17.61 ? 433 GLU A N 1 ATOM 3330 C CA . GLU A 1 433 ? 17.298 35.697 34.014 1.00 18.33 ? 433 GLU A CA 1 ATOM 3331 C C . GLU A 1 433 ? 17.819 34.509 34.823 1.00 18.16 ? 433 GLU A C 1 ATOM 3332 O O . GLU A 1 433 ? 17.056 33.753 35.460 1.00 18.46 ? 433 GLU A O 1 ATOM 3333 C CB . GLU A 1 433 ? 17.515 36.985 34.826 1.00 18.81 ? 433 GLU A CB 1 ATOM 3334 C CG . GLU A 1 433 ? 16.912 38.271 34.226 1.00 22.37 ? 433 GLU A CG 1 ATOM 3335 C CD . GLU A 1 433 ? 17.604 38.748 32.959 1.00 26.76 ? 433 GLU A CD 1 ATOM 3336 O OE1 . GLU A 1 433 ? 18.646 38.183 32.547 1.00 27.34 ? 433 GLU A OE1 1 ATOM 3337 O OE2 . GLU A 1 433 ? 17.080 39.719 32.353 1.00 32.21 ? 433 GLU A OE2 1 ATOM 3338 N N . TRP A 1 434 ? 19.133 34.385 34.849 1.00 18.17 ? 434 TRP A N 1 ATOM 3339 C CA . TRP A 1 434 ? 19.778 33.344 35.644 1.00 17.81 ? 434 TRP A CA 1 ATOM 3340 C C . TRP A 1 434 ? 19.323 33.425 37.112 1.00 17.94 ? 434 TRP A C 1 ATOM 3341 O O . TRP A 1 434 ? 18.921 32.415 37.702 1.00 17.63 ? 434 TRP A O 1 ATOM 3342 C CB . TRP A 1 434 ? 21.289 33.532 35.530 1.00 19.07 ? 434 TRP A CB 1 ATOM 3343 C CG . TRP A 1 434 ? 22.105 32.621 36.369 1.00 18.28 ? 434 TRP A CG 1 ATOM 3344 C CD1 . TRP A 1 434 ? 21.919 31.280 36.563 1.00 19.23 ? 434 TRP A CD1 1 ATOM 3345 C CD2 . TRP A 1 434 ? 23.274 32.989 37.122 1.00 18.68 ? 434 TRP A CD2 1 ATOM 3346 N NE1 . TRP A 1 434 ? 22.913 30.787 37.400 1.00 20.43 ? 434 TRP A NE1 1 ATOM 3347 C CE2 . TRP A 1 434 ? 23.756 31.810 37.747 1.00 18.82 ? 434 TRP A CE2 1 ATOM 3348 C CE3 . TRP A 1 434 ? 23.963 34.201 37.317 1.00 20.05 ? 434 TRP A CE3 1 ATOM 3349 C CZ2 . TRP A 1 434 ? 24.900 31.806 38.573 1.00 20.47 ? 434 TRP A CZ2 1 ATOM 3350 C CZ3 . TRP A 1 434 ? 25.099 34.205 38.125 1.00 20.28 ? 434 TRP A CZ3 1 ATOM 3351 C CH2 . TRP A 1 434 ? 25.563 33.008 38.737 1.00 20.26 ? 434 TRP A CH2 1 ATOM 3352 N N . GLN A 1 435 ? 19.408 34.635 37.681 1.00 18.32 ? 435 GLN A N 1 ATOM 3353 C CA . GLN A 1 435 ? 19.134 34.869 39.112 1.00 18.75 ? 435 GLN A CA 1 ATOM 3354 C C . GLN A 1 435 ? 17.647 35.114 39.366 1.00 18.98 ? 435 GLN A C 1 ATOM 3355 O O . GLN A 1 435 ? 17.234 35.442 40.488 1.00 20.09 ? 435 GLN A O 1 ATOM 3356 C CB . GLN A 1 435 ? 19.960 36.074 39.610 1.00 19.15 ? 435 GLN A CB 1 ATOM 3357 C CG . GLN A 1 435 ? 21.462 35.790 39.754 1.00 19.53 ? 435 GLN A CG 1 ATOM 3358 C CD . GLN A 1 435 ? 21.771 34.783 40.864 1.00 19.36 ? 435 GLN A CD 1 ATOM 3359 O OE1 . GLN A 1 435 ? 21.135 34.806 41.933 1.00 20.38 ? 435 GLN A OE1 1 ATOM 3360 N NE2 . GLN A 1 435 ? 22.740 33.895 40.621 1.00 19.48 ? 435 GLN A NE2 1 ATOM 3361 N N . GLY A 1 436 ? 16.838 34.968 38.318 1.00 18.84 ? 436 GLY A N 1 ATOM 3362 C CA . GLY A 1 436 ? 15.457 35.438 38.387 1.00 18.82 ? 436 GLY A CA 1 ATOM 3363 C C . GLY A 1 436 ? 15.451 36.960 38.414 1.00 19.32 ? 436 GLY A C 1 ATOM 3364 O O . GLY A 1 436 ? 16.492 37.612 38.171 1.00 18.89 ? 436 GLY A O 1 ATOM 3365 N N . ASP A 1 437 ? 14.293 37.542 38.720 1.00 19.78 ? 437 ASP A N 1 ATOM 3366 C CA . ASP A 1 437 ? 14.158 38.984 38.651 1.00 20.50 ? 437 ASP A CA 1 ATOM 3367 C C . ASP A 1 437 ? 12.877 39.419 39.368 1.00 20.66 ? 437 ASP A C 1 ATOM 3368 O O . ASP A 1 437 ? 12.104 38.582 39.861 1.00 20.00 ? 437 ASP A O 1 ATOM 3369 C CB . ASP A 1 437 ? 14.155 39.413 37.161 1.00 21.34 ? 437 ASP A CB 1 ATOM 3370 C CG . ASP A 1 437 ? 14.501 40.892 36.938 1.00 24.04 ? 437 ASP A CG 1 ATOM 3371 O OD1 . ASP A 1 437 ? 14.818 41.684 37.887 1.00 24.58 ? 437 ASP A OD1 1 ATOM 3372 O OD2 . ASP A 1 437 ? 14.421 41.276 35.747 1.00 28.15 ? 437 ASP A OD2 1 ATOM 3373 N N . THR A 1 438 ? 12.677 40.728 39.435 1.00 20.85 ? 438 THR A N 1 ATOM 3374 C CA . THR A 1 438 ? 11.516 41.321 40.092 1.00 20.62 ? 438 THR A CA 1 ATOM 3375 C C . THR A 1 438 ? 10.478 41.818 39.078 1.00 20.87 ? 438 THR A C 1 ATOM 3376 O O . THR A 1 438 ? 10.820 42.274 37.969 1.00 22.09 ? 438 THR A O 1 ATOM 3377 C CB . THR A 1 438 ? 11.951 42.479 41.038 1.00 20.97 ? 438 THR A CB 1 ATOM 3378 O OG1 . THR A 1 438 ? 10.812 42.983 41.736 1.00 21.04 ? 438 THR A OG1 1 ATOM 3379 C CG2 . THR A 1 438 ? 12.621 43.617 40.232 1.00 21.16 ? 438 THR A CG2 1 ATOM 3380 N N . GLY A 1 439 ? 9.210 41.694 39.449 1.00 20.16 ? 439 GLY A N 1 ATOM 3381 C CA . GLY A 1 439 ? 8.118 42.285 38.667 1.00 20.48 ? 439 GLY A CA 1 ATOM 3382 C C . GLY A 1 439 ? 7.572 41.399 37.563 1.00 20.97 ? 439 GLY A C 1 ATOM 3383 O O . GLY A 1 439 ? 7.674 40.170 37.628 1.00 20.64 ? 439 GLY A O 1 ATOM 3384 N N . ARG A 1 440 ? 6.977 42.033 36.550 1.00 20.91 ? 440 ARG A N 1 ATOM 3385 C CA . ARG A 1 440 ? 6.242 41.305 35.532 1.00 21.88 ? 440 ARG A CA 1 ATOM 3386 C C . ARG A 1 440 ? 7.207 40.924 34.384 1.00 22.31 ? 440 ARG A C 1 ATOM 3387 O O . ARG A 1 440 ? 7.292 41.594 33.341 1.00 23.37 ? 440 ARG A O 1 ATOM 3388 C CB . ARG A 1 440 ? 5.029 42.126 35.066 1.00 22.70 ? 440 ARG A CB 1 ATOM 3389 C CG . ARG A 1 440 ? 4.192 41.437 34.015 1.00 25.94 ? 440 ARG A CG 1 ATOM 3390 C CD . ARG A 1 440 ? 2.733 41.847 34.109 1.00 35.85 ? 440 ARG A CD 1 ATOM 3391 N NE . ARG A 1 440 ? 1.964 40.663 34.511 1.00 32.38 ? 440 ARG A NE 1 ATOM 3392 C CZ . ARG A 1 440 ? 1.719 40.263 35.766 1.00 47.69 ? 440 ARG A CZ 1 ATOM 3393 N NH1 . ARG A 1 440 ? 2.148 40.980 36.825 1.00 33.98 ? 440 ARG A NH1 1 ATOM 3394 N NH2 . ARG A 1 440 ? 1.038 39.130 35.950 1.00 32.20 ? 440 ARG A NH2 1 ATOM 3395 N N . THR A 1 441 ? 7.944 39.836 34.609 1.00 21.62 ? 441 THR A N 1 ATOM 3396 C CA . THR A 1 441 ? 9.038 39.428 33.735 1.00 21.44 ? 441 THR A CA 1 ATOM 3397 C C . THR A 1 441 ? 8.574 38.479 32.633 1.00 20.70 ? 441 THR A C 1 ATOM 3398 O O . THR A 1 441 ? 9.316 38.218 31.682 1.00 21.40 ? 441 THR A O 1 ATOM 3399 C CB . THR A 1 441 ? 10.133 38.691 34.553 1.00 21.56 ? 441 THR A CB 1 ATOM 3400 O OG1 . THR A 1 441 ? 9.518 37.588 35.233 1.00 23.13 ? 441 THR A OG1 1 ATOM 3401 C CG2 . THR A 1 441 ? 10.783 39.644 35.586 1.00 23.16 ? 441 THR A CG2 1 ATOM 3402 N N . THR A 1 442 ? 7.366 37.935 32.776 1.00 19.92 ? 442 THR A N 1 ATOM 3403 C CA . THR A 1 442 ? 6.835 36.962 31.799 1.00 18.54 ? 442 THR A CA 1 ATOM 3404 C C . THR A 1 442 ? 5.309 36.948 31.876 1.00 18.50 ? 442 THR A C 1 ATOM 3405 O O . THR A 1 442 ? 4.718 37.839 32.513 1.00 19.10 ? 442 THR A O 1 ATOM 3406 C CB . THR A 1 442 ? 7.508 35.558 31.972 1.00 18.71 ? 442 THR A CB 1 ATOM 3407 O OG1 . THR A 1 442 ? 7.131 34.689 30.905 1.00 18.64 ? 442 THR A OG1 1 ATOM 3408 C CG2 . THR A 1 442 ? 7.151 34.913 33.338 1.00 17.89 ? 442 THR A CG2 1 ATOM 3409 N N . VAL A 1 443 ? 4.676 35.993 31.202 1.00 17.76 ? 443 VAL A N 1 ATOM 3410 C CA . VAL A 1 443 ? 3.234 35.849 31.249 1.00 17.86 ? 443 VAL A CA 1 ATOM 3411 C C . VAL A 1 443 ? 2.873 34.999 32.467 1.00 17.48 ? 443 VAL A C 1 ATOM 3412 O O . VAL A 1 443 ? 3.415 33.910 32.668 1.00 18.95 ? 443 VAL A O 1 ATOM 3413 C CB . VAL A 1 443 ? 2.712 35.186 29.941 1.00 18.33 ? 443 VAL A CB 1 ATOM 3414 C CG1 . VAL A 1 443 ? 1.208 34.918 30.006 1.00 18.99 ? 443 VAL A CG1 1 ATOM 3415 C CG2 . VAL A 1 443 ? 3.066 36.055 28.754 1.00 20.40 ? 443 VAL A CG2 1 ATOM 3416 N N . GLY A 1 444 ? 1.952 35.490 33.280 1.00 17.04 ? 444 GLY A N 1 ATOM 3417 C CA . GLY A 1 444 ? 1.573 34.734 34.472 1.00 16.86 ? 444 GLY A CA 1 ATOM 3418 C C . GLY A 1 444 ? 0.473 35.441 35.225 1.00 17.12 ? 444 GLY A C 1 ATOM 3419 O O . GLY A 1 444 ? -0.082 36.460 34.759 1.00 18.44 ? 444 GLY A O 1 ATOM 3420 N N . THR A 1 445 ? 0.165 34.905 36.399 1.00 16.17 ? 445 THR A N 1 ATOM 3421 C CA . THR A 1 445 ? -0.886 35.469 37.248 1.00 16.91 ? 445 THR A CA 1 ATOM 3422 C C . THR A 1 445 ? -0.320 35.578 38.663 1.00 16.83 ? 445 THR A C 1 ATOM 3423 O O . THR A 1 445 ? 0.049 34.569 39.250 1.00 15.48 ? 445 THR A O 1 ATOM 3424 C CB . THR A 1 445 ? -2.149 34.570 37.242 1.00 17.66 ? 445 THR A CB 1 ATOM 3425 O OG1 . THR A 1 445 ? -2.666 34.478 35.907 1.00 18.55 ? 445 THR A OG1 1 ATOM 3426 C CG2 . THR A 1 445 ? -3.226 35.153 38.140 1.00 17.64 ? 445 THR A CG2 1 ATOM 3427 N N . THR A 1 446 ? -0.260 36.799 39.200 1.00 16.51 ? 446 THR A N 1 ATOM 3428 C CA . THR A 1 446 ? 0.250 37.008 40.574 1.00 16.62 ? 446 THR A CA 1 ATOM 3429 C C . THR A 1 446 ? -0.834 36.592 41.581 1.00 15.99 ? 446 THR A C 1 ATOM 3430 O O . THR A 1 446 ? -1.979 36.320 41.193 1.00 16.11 ? 446 THR A O 1 ATOM 3431 C CB . THR A 1 446 ? 0.601 38.467 40.810 1.00 16.56 ? 446 THR A CB 1 ATOM 3432 O OG1 . THR A 1 446 ? -0.600 39.259 40.713 1.00 17.73 ? 446 THR A OG1 1 ATOM 3433 C CG2 . THR A 1 446 ? 1.677 38.969 39.792 1.00 18.15 ? 446 THR A CG2 1 ATOM 3434 N N . ILE A 1 447 ? -0.481 36.553 42.866 1.00 15.47 ? 447 ILE A N 1 ATOM 3435 C CA . ILE A 1 447 ? -1.464 36.226 43.910 1.00 15.82 ? 447 ILE A CA 1 ATOM 3436 C C . ILE A 1 447 ? -2.623 37.234 43.908 1.00 16.10 ? 447 ILE A C 1 ATOM 3437 O O . ILE A 1 447 ? -3.792 36.840 43.961 1.00 16.66 ? 447 ILE A O 1 ATOM 3438 C CB . ILE A 1 447 ? -0.774 36.116 45.284 1.00 15.44 ? 447 ILE A CB 1 ATOM 3439 C CG1 . ILE A 1 447 ? 0.157 34.883 45.259 1.00 17.24 ? 447 ILE A CG1 1 ATOM 3440 C CG2 . ILE A 1 447 ? -1.815 35.912 46.376 1.00 16.63 ? 447 ILE A CG2 1 ATOM 3441 C CD1 . ILE A 1 447 ? 1.164 34.855 46.425 1.00 18.51 ? 447 ILE A CD1 1 ATOM 3442 N N . LEU A 1 448 ? -2.304 38.518 43.773 1.00 16.50 ? 448 LEU A N 1 ATOM 3443 C CA . LEU A 1 448 ? -3.337 39.561 43.716 1.00 17.21 ? 448 LEU A CA 1 ATOM 3444 C C . LEU A 1 448 ? -4.282 39.319 42.537 1.00 17.73 ? 448 LEU A C 1 ATOM 3445 O O . LEU A 1 448 ? -5.500 39.350 42.694 1.00 17.70 ? 448 LEU A O 1 ATOM 3446 C CB . LEU A 1 448 ? -2.713 40.948 43.592 1.00 17.61 ? 448 LEU A CB 1 ATOM 3447 C CG . LEU A 1 448 ? -3.672 42.108 43.304 1.00 17.58 ? 448 LEU A CG 1 ATOM 3448 C CD1 . LEU A 1 448 ? -4.680 42.262 44.481 1.00 19.43 ? 448 LEU A CD1 1 ATOM 3449 C CD2 . LEU A 1 448 ? -2.887 43.380 43.057 1.00 19.57 ? 448 LEU A CD2 1 ATOM 3450 N N . GLU A 1 449 ? -3.706 39.098 41.358 1.00 17.54 ? 449 GLU A N 1 ATOM 3451 C CA . GLU A 1 449 ? -4.523 38.818 40.160 1.00 18.92 ? 449 GLU A CA 1 ATOM 3452 C C . GLU A 1 449 ? -5.394 37.564 40.344 1.00 18.17 ? 449 GLU A C 1 ATOM 3453 O O . GLU A 1 449 ? -6.576 37.561 39.948 1.00 17.90 ? 449 GLU A O 1 ATOM 3454 C CB . GLU A 1 449 ? -3.620 38.696 38.917 1.00 18.40 ? 449 GLU A CB 1 ATOM 3455 C CG . GLU A 1 449 ? -2.959 40.013 38.542 1.00 21.29 ? 449 GLU A CG 1 ATOM 3456 C CD . GLU A 1 449 ? -1.844 39.891 37.463 1.00 22.95 ? 449 GLU A CD 1 ATOM 3457 O OE1 . GLU A 1 449 ? -1.171 38.842 37.281 1.00 21.74 ? 449 GLU A OE1 1 ATOM 3458 O OE2 . GLU A 1 449 ? -1.621 40.926 36.794 1.00 31.96 ? 449 GLU A OE2 1 ATOM 3459 N N . ALA A 1 450 ? -4.835 36.524 40.968 1.00 17.17 ? 450 ALA A N 1 ATOM 3460 C CA . ALA A 1 450 ? -5.558 35.284 41.264 1.00 17.47 ? 450 ALA A CA 1 ATOM 3461 C C . ALA A 1 450 ? -6.722 35.552 42.219 1.00 17.35 ? 450 ALA A C 1 ATOM 3462 O O . ALA A 1 450 ? -7.817 35.019 42.028 1.00 17.17 ? 450 ALA A O 1 ATOM 3463 C CB . ALA A 1 450 ? -4.620 34.240 41.858 1.00 17.41 ? 450 ALA A CB 1 ATOM 3464 N N . VAL A 1 451 ? -6.487 36.395 43.229 1.00 17.05 ? 451 VAL A N 1 ATOM 3465 C CA . VAL A 1 451 ? -7.560 36.737 44.174 1.00 16.82 ? 451 VAL A CA 1 ATOM 3466 C C . VAL A 1 451 ? -8.711 37.436 43.421 1.00 17.71 ? 451 VAL A C 1 ATOM 3467 O O . VAL A 1 451 ? -9.902 37.062 43.578 1.00 18.02 ? 451 VAL A O 1 ATOM 3468 C CB . VAL A 1 451 ? -7.024 37.626 45.325 1.00 16.17 ? 451 VAL A CB 1 ATOM 3469 C CG1 . VAL A 1 451 ? -8.177 38.185 46.153 1.00 16.81 ? 451 VAL A CG1 1 ATOM 3470 C CG2 . VAL A 1 451 ? -6.103 36.778 46.252 1.00 17.12 ? 451 VAL A CG2 1 ATOM 3471 N N . LYS A 1 452 ? -8.357 38.430 42.605 1.00 18.16 ? 452 LYS A N 1 ATOM 3472 C CA . LYS A 1 452 ? -9.374 39.187 41.859 1.00 18.88 ? 452 LYS A CA 1 ATOM 3473 C C . LYS A 1 452 ? -10.160 38.268 40.908 1.00 19.42 ? 452 LYS A C 1 ATOM 3474 O O . LYS A 1 452 ? -11.344 38.495 40.674 1.00 19.80 ? 452 LYS A O 1 ATOM 3475 C CB . LYS A 1 452 ? -8.737 40.316 41.075 1.00 17.99 ? 452 LYS A CB 1 ATOM 3476 C CG . LYS A 1 452 ? -8.143 41.420 41.948 1.00 21.06 ? 452 LYS A CG 1 ATOM 3477 C CD . LYS A 1 452 ? -7.348 42.361 41.054 1.00 25.64 ? 452 LYS A CD 1 ATOM 3478 C CE . LYS A 1 452 ? -6.921 43.587 41.792 1.00 31.45 ? 452 LYS A CE 1 ATOM 3479 N NZ . LYS A 1 452 ? -6.313 44.595 40.864 1.00 34.62 ? 452 LYS A NZ 1 ATOM 3480 N N . ALA A 1 453 ? -9.496 37.225 40.394 1.00 18.96 ? 453 ALA A N 1 ATOM 3481 C CA . ALA A 1 453 ? -10.103 36.275 39.452 1.00 19.42 ? 453 ALA A CA 1 ATOM 3482 C C . ALA A 1 453 ? -10.984 35.246 40.151 1.00 19.83 ? 453 ALA A C 1 ATOM 3483 O O . ALA A 1 453 ? -11.805 34.587 39.504 1.00 20.54 ? 453 ALA A O 1 ATOM 3484 C CB . ALA A 1 453 ? -9.016 35.569 38.629 1.00 19.74 ? 453 ALA A CB 1 ATOM 3485 N N . ALA A 1 454 ? -10.813 35.103 41.474 1.00 19.04 ? 454 ALA A N 1 ATOM 3486 C CA . ALA A 1 454 ? -11.482 34.064 42.233 1.00 19.33 ? 454 ALA A CA 1 ATOM 3487 C C . ALA A 1 454 ? -12.731 34.544 42.947 1.00 19.45 ? 454 ALA A C 1 ATOM 3488 O O . ALA A 1 454 ? -13.706 33.794 43.085 1.00 20.92 ? 454 ALA A O 1 ATOM 3489 C CB . ALA A 1 454 ? -10.527 33.473 43.271 1.00 19.62 ? 454 ALA A CB 1 ATOM 3490 N N . VAL A 1 455 ? -12.678 35.768 43.462 1.00 19.21 ? 455 VAL A N 1 ATOM 3491 C CA . VAL A 1 455 ? -13.730 36.231 44.387 1.00 19.35 ? 455 VAL A CA 1 ATOM 3492 C C . VAL A 1 455 ? -15.056 36.580 43.674 1.00 19.77 ? 455 VAL A C 1 ATOM 3493 O O . VAL A 1 455 ? -15.083 36.885 42.477 1.00 20.29 ? 455 VAL A O 1 ATOM 3494 C CB . VAL A 1 455 ? -13.240 37.411 45.271 1.00 19.05 ? 455 VAL A CB 1 ATOM 3495 C CG1 . VAL A 1 455 ? -12.081 36.959 46.206 1.00 20.11 ? 455 VAL A CG1 1 ATOM 3496 C CG2 . VAL A 1 455 ? -12.870 38.632 44.419 1.00 19.73 ? 455 VAL A CG2 1 ATOM 3497 N N . ASP A 1 456 ? -16.144 36.559 44.441 1.00 20.18 ? 456 ASP A N 1 ATOM 3498 C CA . ASP A 1 456 ? -17.456 37.010 43.979 1.00 20.50 ? 456 ASP A CA 1 ATOM 3499 C C . ASP A 1 456 ? -17.355 38.449 43.434 1.00 20.94 ? 456 ASP A C 1 ATOM 3500 O O . ASP A 1 456 ? -16.558 39.257 43.927 1.00 20.39 ? 456 ASP A O 1 ATOM 3501 C CB . ASP A 1 456 ? -18.435 36.939 45.163 1.00 20.85 ? 456 ASP A CB 1 ATOM 3502 C CG . ASP A 1 456 ? -19.885 37.147 44.750 1.00 22.99 ? 456 ASP A CG 1 ATOM 3503 O OD1 . ASP A 1 456 ? -20.361 38.301 44.775 1.00 25.08 ? 456 ASP A OD1 1 ATOM 3504 O OD2 . ASP A 1 456 ? -20.534 36.143 44.414 1.00 26.04 ? 456 ASP A OD2 1 ATOM 3505 N N . PRO A 1 457 ? -18.156 38.787 42.405 1.00 20.69 ? 457 PRO A N 1 ATOM 3506 C CA . PRO A 1 457 ? -18.125 40.154 41.872 1.00 21.49 ? 457 PRO A CA 1 ATOM 3507 C C . PRO A 1 457 ? -18.462 41.240 42.894 1.00 21.28 ? 457 PRO A C 1 ATOM 3508 O O . PRO A 1 457 ? -18.039 42.380 42.716 1.00 22.97 ? 457 PRO A O 1 ATOM 3509 C CB . PRO A 1 457 ? -19.185 40.129 40.740 1.00 21.19 ? 457 PRO A CB 1 ATOM 3510 C CG . PRO A 1 457 ? -20.002 38.918 40.998 1.00 21.63 ? 457 PRO A CG 1 ATOM 3511 C CD . PRO A 1 457 ? -19.071 37.924 41.634 1.00 21.49 ? 457 PRO A CD 1 ATOM 3512 N N . SER A 1 458 ? -19.195 40.894 43.949 1.00 21.46 ? 458 SER A N 1 ATOM 3513 C CA . SER A 1 458 ? -19.532 41.879 44.994 1.00 21.69 ? 458 SER A CA 1 ATOM 3514 C C . SER A 1 458 ? -18.386 42.142 45.982 1.00 21.69 ? 458 SER A C 1 ATOM 3515 O O . SER A 1 458 ? -18.464 43.060 46.804 1.00 22.62 ? 458 SER A O 1 ATOM 3516 C CB . SER A 1 458 ? -20.791 41.458 45.751 1.00 22.15 ? 458 SER A CB 1 ATOM 3517 O OG . SER A 1 458 ? -20.548 40.334 46.563 1.00 23.59 ? 458 SER A OG 1 ATOM 3518 N N . THR A 1 459 ? -17.343 41.318 45.911 1.00 20.54 ? 459 THR A N 1 ATOM 3519 C CA . THR A 1 459 ? -16.214 41.442 46.835 1.00 20.14 ? 459 THR A CA 1 ATOM 3520 C C . THR A 1 459 ? -15.258 42.535 46.382 1.00 20.37 ? 459 THR A C 1 ATOM 3521 O O . THR A 1 459 ? -14.663 42.463 45.296 1.00 21.64 ? 459 THR A O 1 ATOM 3522 C CB . THR A 1 459 ? -15.465 40.098 46.980 1.00 19.44 ? 459 THR A CB 1 ATOM 3523 O OG1 . THR A 1 459 ? -16.374 39.089 47.440 1.00 20.06 ? 459 THR A OG1 1 ATOM 3524 C CG2 . THR A 1 459 ? -14.260 40.229 47.965 1.00 19.40 ? 459 THR A CG2 1 ATOM 3525 N N . VAL A 1 460 ? -15.088 43.554 47.214 1.00 20.27 ? 460 VAL A N 1 ATOM 3526 C CA . VAL A 1 460 ? -14.127 44.599 46.901 1.00 20.13 ? 460 VAL A CA 1 ATOM 3527 C C . VAL A 1 460 ? -12.748 44.143 47.337 1.00 20.62 ? 460 VAL A C 1 ATOM 3528 O O . VAL A 1 460 ? -12.552 43.757 48.491 1.00 20.70 ? 460 VAL A O 1 ATOM 3529 C CB . VAL A 1 460 ? -14.482 45.935 47.579 1.00 20.14 ? 460 VAL A CB 1 ATOM 3530 C CG1 . VAL A 1 460 ? -13.404 46.974 47.302 1.00 21.27 ? 460 VAL A CG1 1 ATOM 3531 C CG2 . VAL A 1 460 ? -15.849 46.428 47.059 1.00 19.70 ? 460 VAL A CG2 1 ATOM 3532 N N . VAL A 1 461 ? -11.803 44.176 46.401 1.00 19.90 ? 461 VAL A N 1 ATOM 3533 C CA . VAL A 1 461 ? -10.423 43.772 46.682 1.00 20.03 ? 461 VAL A CA 1 ATOM 3534 C C . VAL A 1 461 ? -9.539 45.003 46.737 1.00 20.43 ? 461 VAL A C 1 ATOM 3535 O O . VAL A 1 461 ? -9.435 45.763 45.769 1.00 20.94 ? 461 VAL A O 1 ATOM 3536 C CB . VAL A 1 461 ? -9.887 42.774 45.627 1.00 20.26 ? 461 VAL A CB 1 ATOM 3537 C CG1 . VAL A 1 461 ? -8.433 42.385 45.954 1.00 19.31 ? 461 VAL A CG1 1 ATOM 3538 C CG2 . VAL A 1 461 ? -10.792 41.542 45.566 1.00 18.58 ? 461 VAL A CG2 1 ATOM 3539 N N . VAL A 1 462 ? -8.885 45.201 47.871 1.00 19.85 ? 462 VAL A N 1 ATOM 3540 C CA . VAL A 1 462 ? -7.949 46.312 48.013 1.00 19.77 ? 462 VAL A CA 1 ATOM 3541 C C . VAL A 1 462 ? -6.516 45.768 48.070 1.00 19.82 ? 462 VAL A C 1 ATOM 3542 O O . VAL A 1 462 ? -6.248 44.822 48.808 1.00 20.01 ? 462 VAL A O 1 ATOM 3543 C CB . VAL A 1 462 ? -8.240 47.110 49.304 1.00 20.26 ? 462 VAL A CB 1 ATOM 3544 C CG1 . VAL A 1 462 ? -7.179 48.216 49.511 1.00 21.01 ? 462 VAL A CG1 1 ATOM 3545 C CG2 . VAL A 1 462 ? -9.655 47.718 49.245 1.00 20.47 ? 462 VAL A CG2 1 ATOM 3546 N N . PHE A 1 463 ? -5.615 46.375 47.302 1.00 19.58 ? 463 PHE A N 1 ATOM 3547 C CA . PHE A 1 463 ? -4.196 46.030 47.350 1.00 20.39 ? 463 PHE A CA 1 ATOM 3548 C C . PHE A 1 463 ? -3.414 47.130 48.056 1.00 20.75 ? 463 PHE A C 1 ATOM 3549 O O . PHE A 1 463 ? -3.540 48.311 47.717 1.00 21.26 ? 463 PHE A O 1 ATOM 3550 C CB . PHE A 1 463 ? -3.607 45.802 45.953 1.00 21.19 ? 463 PHE A CB 1 ATOM 3551 C CG . PHE A 1 463 ? -2.117 45.577 45.971 1.00 21.49 ? 463 PHE A CG 1 ATOM 3552 C CD1 . PHE A 1 463 ? -1.575 44.464 46.606 1.00 22.14 ? 463 PHE A CD1 1 ATOM 3553 C CD2 . PHE A 1 463 ? -1.257 46.498 45.382 1.00 24.03 ? 463 PHE A CD2 1 ATOM 3554 C CE1 . PHE A 1 463 ? -0.186 44.259 46.639 1.00 22.51 ? 463 PHE A CE1 1 ATOM 3555 C CE2 . PHE A 1 463 ? 0.132 46.306 45.415 1.00 24.43 ? 463 PHE A CE2 1 ATOM 3556 C CZ . PHE A 1 463 ? 0.664 45.179 46.040 1.00 23.48 ? 463 PHE A CZ 1 ATOM 3557 N N . ALA A 1 464 ? -2.592 46.744 49.026 1.00 21.16 ? 464 ALA A N 1 ATOM 3558 C CA . ALA A 1 464 ? -1.624 47.679 49.601 1.00 22.37 ? 464 ALA A CA 1 ATOM 3559 C C . ALA A 1 464 ? -0.343 46.908 49.866 1.00 22.73 ? 464 ALA A C 1 ATOM 3560 O O . ALA A 1 464 ? -0.360 45.896 50.558 1.00 22.28 ? 464 ALA A O 1 ATOM 3561 C CB . ALA A 1 464 ? -2.156 48.306 50.883 1.00 22.37 ? 464 ALA A CB 1 ATOM 3562 N N . GLU A 1 465 ? 0.764 47.349 49.286 1.00 23.67 ? 465 GLU A N 1 ATOM 3563 C CA . GLU A 1 465 ? 1.976 46.553 49.385 1.00 24.48 ? 465 GLU A CA 1 ATOM 3564 C C . GLU A 1 465 ? 2.499 46.463 50.820 1.00 24.47 ? 465 GLU A C 1 ATOM 3565 O O . GLU A 1 465 ? 2.891 45.387 51.281 1.00 24.84 ? 465 GLU A O 1 ATOM 3566 C CB . GLU A 1 465 ? 3.067 47.081 48.461 1.00 25.21 ? 465 GLU A CB 1 ATOM 3567 C CG . GLU A 1 465 ? 4.229 46.103 48.388 1.00 28.39 ? 465 GLU A CG 1 ATOM 3568 C CD . GLU A 1 465 ? 5.309 46.508 47.421 1.00 33.50 ? 465 GLU A CD 1 ATOM 3569 O OE1 . GLU A 1 465 ? 5.025 47.251 46.443 1.00 35.75 ? 465 GLU A OE1 1 ATOM 3570 O OE2 . GLU A 1 465 ? 6.451 46.045 47.641 1.00 36.96 ? 465 GLU A OE2 1 ATOM 3571 N N . ASN A 1 466 ? 2.520 47.596 51.519 1.00 24.37 ? 466 ASN A N 1 ATOM 3572 C CA . ASN A 1 466 ? 3.027 47.627 52.877 1.00 24.78 ? 466 ASN A CA 1 ATOM 3573 C C . ASN A 1 466 ? 2.199 48.577 53.732 1.00 24.96 ? 466 ASN A C 1 ATOM 3574 O O . ASN A 1 466 ? 2.680 49.646 54.129 1.00 25.70 ? 466 ASN A O 1 ATOM 3575 C CB A ASN A 1 466 ? 4.498 48.045 52.885 0.50 25.09 ? 466 ASN A CB 1 ATOM 3576 C CB B ASN A 1 466 ? 4.508 48.033 52.922 0.50 24.96 ? 466 ASN A CB 1 ATOM 3577 C CG A ASN A 1 466 ? 5.173 47.769 54.208 0.50 25.15 ? 466 ASN A CG 1 ATOM 3578 C CG B ASN A 1 466 ? 5.440 46.926 52.456 0.50 24.62 ? 466 ASN A CG 1 ATOM 3579 O OD1 A ASN A 1 466 ? 6.223 48.334 54.505 0.50 27.68 ? 466 ASN A OD1 1 ATOM 3580 O OD1 B ASN A 1 466 ? 5.480 45.828 53.031 0.50 22.87 ? 466 ASN A OD1 1 ATOM 3581 N ND2 A ASN A 1 466 ? 4.572 46.899 55.015 0.50 24.52 ? 466 ASN A ND2 1 ATOM 3582 N ND2 B ASN A 1 466 ? 6.202 47.214 51.407 0.50 25.61 ? 466 ASN A ND2 1 ATOM 3583 N N . PRO A 1 467 ? 0.960 48.170 54.034 1.00 24.80 ? 467 PRO A N 1 ATOM 3584 C CA . PRO A 1 467 ? 0.058 49.072 54.758 1.00 25.00 ? 467 PRO A CA 1 ATOM 3585 C C . PRO A 1 467 ? 0.474 49.187 56.223 1.00 25.98 ? 467 PRO A C 1 ATOM 3586 O O . PRO A 1 467 ? 1.034 48.236 56.796 1.00 25.30 ? 467 PRO A O 1 ATOM 3587 C CB . PRO A 1 467 ? -1.294 48.362 54.651 1.00 25.09 ? 467 PRO A CB 1 ATOM 3588 C CG . PRO A 1 467 ? -0.934 46.893 54.595 1.00 24.62 ? 467 PRO A CG 1 ATOM 3589 C CD . PRO A 1 467 ? 0.336 46.855 53.761 1.00 24.17 ? 467 PRO A CD 1 ATOM 3590 N N . ASP A 1 468 ? 0.206 50.337 56.831 1.00 26.96 ? 468 ASP A N 1 ATOM 3591 C CA . ASP A 1 468 ? 0.403 50.430 58.270 1.00 27.74 ? 468 ASP A CA 1 ATOM 3592 C C . ASP A 1 468 ? -0.804 49.927 59.055 1.00 27.27 ? 468 ASP A C 1 ATOM 3593 O O . ASP A 1 468 ? -1.873 49.659 58.483 1.00 26.45 ? 468 ASP A O 1 ATOM 3594 C CB . ASP A 1 468 ? 0.878 51.821 58.716 1.00 29.00 ? 468 ASP A CB 1 ATOM 3595 C CG . ASP A 1 468 ? -0.167 52.913 58.550 1.00 30.95 ? 468 ASP A CG 1 ATOM 3596 O OD1 . ASP A 1 468 ? 0.261 54.086 58.530 1.00 34.99 ? 468 ASP A OD1 1 ATOM 3597 O OD2 . ASP A 1 468 ? -1.386 52.652 58.465 1.00 30.25 ? 468 ASP A OD2 1 ATOM 3598 N N . ALA A 1 469 ? -0.611 49.768 60.363 1.00 26.84 ? 469 ALA A N 1 ATOM 3599 C CA . ALA A 1 469 ? -1.607 49.154 61.226 1.00 26.82 ? 469 ALA A CA 1 ATOM 3600 C C . ALA A 1 469 ? -2.936 49.911 61.177 1.00 26.22 ? 469 ALA A C 1 ATOM 3601 O O . ALA A 1 469 ? -4.008 49.304 61.194 1.00 25.41 ? 469 ALA A O 1 ATOM 3602 C CB . ALA A 1 469 ? -1.077 49.061 62.672 1.00 27.68 ? 469 ALA A CB 1 ATOM 3603 N N . GLU A 1 470 ? -2.852 51.239 61.112 1.00 26.31 ? 470 GLU A N 1 ATOM 3604 C CA . GLU A 1 470 ? -4.052 52.071 61.097 1.00 26.58 ? 470 GLU A CA 1 ATOM 3605 C C . GLU A 1 470 ? -4.869 51.871 59.826 1.00 25.34 ? 470 GLU A C 1 ATOM 3606 O O . GLU A 1 470 ? -6.109 51.806 59.874 1.00 25.09 ? 470 GLU A O 1 ATOM 3607 C CB . GLU A 1 470 ? -3.692 53.549 61.266 1.00 27.44 ? 470 GLU A CB 1 ATOM 3608 C CG . GLU A 1 470 ? -4.901 54.451 61.205 1.00 30.25 ? 470 GLU A CG 1 ATOM 3609 C CD . GLU A 1 470 ? -4.559 55.929 61.191 1.00 35.23 ? 470 GLU A CD 1 ATOM 3610 O OE1 . GLU A 1 470 ? -5.414 56.702 60.700 1.00 35.98 ? 470 GLU A OE1 1 ATOM 3611 O OE2 . GLU A 1 470 ? -3.455 56.312 61.664 1.00 36.34 ? 470 GLU A OE2 1 ATOM 3612 N N . PHE A 1 471 ? -4.173 51.788 58.694 1.00 24.61 ? 471 PHE A N 1 ATOM 3613 C CA . PHE A 1 471 ? -4.824 51.535 57.411 1.00 24.17 ? 471 PHE A CA 1 ATOM 3614 C C . PHE A 1 471 ? -5.680 50.266 57.499 1.00 23.22 ? 471 PHE A C 1 ATOM 3615 O O . PHE A 1 471 ? -6.852 50.262 57.094 1.00 23.34 ? 471 PHE A O 1 ATOM 3616 C CB . PHE A 1 471 ? -3.765 51.422 56.305 1.00 24.98 ? 471 PHE A CB 1 ATOM 3617 C CG . PHE A 1 471 ? -4.320 51.074 54.955 1.00 25.39 ? 471 PHE A CG 1 ATOM 3618 C CD1 . PHE A 1 471 ? -4.536 49.745 54.594 1.00 25.49 ? 471 PHE A CD1 1 ATOM 3619 C CD2 . PHE A 1 471 ? -4.589 52.073 54.027 1.00 27.98 ? 471 PHE A CD2 1 ATOM 3620 C CE1 . PHE A 1 471 ? -5.029 49.420 53.335 1.00 26.22 ? 471 PHE A CE1 1 ATOM 3621 C CE2 . PHE A 1 471 ? -5.098 51.750 52.763 1.00 28.76 ? 471 PHE A CE2 1 ATOM 3622 C CZ . PHE A 1 471 ? -5.307 50.421 52.421 1.00 26.70 ? 471 PHE A CZ 1 ATOM 3623 N N . VAL A 1 472 ? -5.105 49.198 58.058 1.00 22.43 ? 472 VAL A N 1 ATOM 3624 C CA . VAL A 1 472 ? -5.813 47.938 58.200 1.00 22.13 ? 472 VAL A CA 1 ATOM 3625 C C . VAL A 1 472 ? -6.998 48.041 59.166 1.00 21.89 ? 472 VAL A C 1 ATOM 3626 O O . VAL A 1 472 ? -8.096 47.630 58.822 1.00 21.99 ? 472 VAL A O 1 ATOM 3627 C CB . VAL A 1 472 ? -4.874 46.793 58.626 1.00 21.18 ? 472 VAL A CB 1 ATOM 3628 C CG1 . VAL A 1 472 ? -5.611 45.464 58.621 1.00 22.53 ? 472 VAL A CG1 1 ATOM 3629 C CG2 . VAL A 1 472 ? -3.643 46.756 57.675 1.00 21.66 ? 472 VAL A CG2 1 ATOM 3630 N N . LYS A 1 473 ? -6.770 48.610 60.358 1.00 22.10 ? 473 LYS A N 1 ATOM 3631 C CA . LYS A 1 473 ? -7.827 48.701 61.371 1.00 24.52 ? 473 LYS A CA 1 ATOM 3632 C C . LYS A 1 473 ? -9.010 49.547 60.905 1.00 22.73 ? 473 LYS A C 1 ATOM 3633 O O . LYS A 1 473 ? -10.150 49.271 61.272 1.00 22.35 ? 473 LYS A O 1 ATOM 3634 C CB . LYS A 1 473 ? -7.282 49.262 62.695 1.00 22.68 ? 473 LYS A CB 1 ATOM 3635 C CG . LYS A 1 473 ? -6.389 48.300 63.444 1.00 32.97 ? 473 LYS A CG 1 ATOM 3636 C CD . LYS A 1 473 ? -6.088 48.798 64.890 1.00 23.97 ? 473 LYS A CD 1 ATOM 3637 C CE . LYS A 1 473 ? -5.438 47.692 65.777 1.00 38.63 ? 473 LYS A CE 1 ATOM 3638 N NZ . LYS A 1 473 ? -4.895 48.204 67.089 1.00 28.52 ? 473 LYS A NZ 1 ATOM 3639 N N . SER A 1 474 ? -8.730 50.563 60.089 1.00 22.34 ? 474 SER A N 1 ATOM 3640 C CA . SER A 1 474 ? -9.762 51.484 59.597 1.00 23.52 ? 474 SER A CA 1 ATOM 3641 C C . SER A 1 474 ? -10.416 51.023 58.298 1.00 23.57 ? 474 SER A C 1 ATOM 3642 O O . SER A 1 474 ? -11.392 51.618 57.847 1.00 24.07 ? 474 SER A O 1 ATOM 3643 C CB . SER A 1 474 ? -9.163 52.882 59.387 1.00 23.53 ? 474 SER A CB 1 ATOM 3644 O OG . SER A 1 474 ? -8.803 53.455 60.632 1.00 25.88 ? 474 SER A OG 1 ATOM 3645 N N . GLY A 1 475 ? -9.893 49.956 57.694 1.00 23.29 ? 475 GLY A N 1 ATOM 3646 C CA . GLY A 1 475 ? -10.289 49.626 56.331 1.00 23.00 ? 475 GLY A CA 1 ATOM 3647 C C . GLY A 1 475 ? -11.600 48.897 56.125 1.00 23.25 ? 475 GLY A C 1 ATOM 3648 O O . GLY A 1 475 ? -12.055 48.763 54.987 1.00 24.07 ? 475 GLY A O 1 ATOM 3649 N N . GLY A 1 476 ? -12.201 48.386 57.199 1.00 22.28 ? 476 GLY A N 1 ATOM 3650 C CA . GLY A 1 476 ? -13.440 47.618 57.083 1.00 22.85 ? 476 GLY A CA 1 ATOM 3651 C C . GLY A 1 476 ? -13.262 46.302 56.330 1.00 22.12 ? 476 GLY A C 1 ATOM 3652 O O . GLY A 1 476 ? -14.144 45.884 55.562 1.00 23.05 ? 476 GLY A O 1 ATOM 3653 N N . PHE A 1 477 ? -12.122 45.650 56.562 1.00 21.58 ? 477 PHE A N 1 ATOM 3654 C CA . PHE A 1 477 ? -11.811 44.366 55.907 1.00 20.94 ? 477 PHE A CA 1 ATOM 3655 C C . PHE A 1 477 ? -12.372 43.132 56.623 1.00 21.39 ? 477 PHE A C 1 ATOM 3656 O O . PHE A 1 477 ? -12.384 43.060 57.872 1.00 21.88 ? 477 PHE A O 1 ATOM 3657 C CB . PHE A 1 477 ? -10.303 44.207 55.758 1.00 20.68 ? 477 PHE A CB 1 ATOM 3658 C CG . PHE A 1 477 ? -9.668 45.274 54.928 1.00 19.82 ? 477 PHE A CG 1 ATOM 3659 C CD1 . PHE A 1 477 ? -9.989 45.406 53.560 1.00 20.64 ? 477 PHE A CD1 1 ATOM 3660 C CD2 . PHE A 1 477 ? -8.744 46.149 55.493 1.00 20.29 ? 477 PHE A CD2 1 ATOM 3661 C CE1 . PHE A 1 477 ? -9.395 46.405 52.779 1.00 20.26 ? 477 PHE A CE1 1 ATOM 3662 C CE2 . PHE A 1 477 ? -8.141 47.143 54.726 1.00 20.47 ? 477 PHE A CE2 1 ATOM 3663 C CZ . PHE A 1 477 ? -8.470 47.282 53.362 1.00 21.18 ? 477 PHE A CZ 1 ATOM 3664 N N . SER A 1 478 ? -12.834 42.161 55.838 1.00 20.39 ? 478 SER A N 1 ATOM 3665 C CA . SER A 1 478 ? -13.302 40.881 56.371 1.00 20.76 ? 478 SER A CA 1 ATOM 3666 C C . SER A 1 478 ? -12.143 39.976 56.774 1.00 20.89 ? 478 SER A C 1 ATOM 3667 O O . SER A 1 478 ? -12.229 39.224 57.755 1.00 21.88 ? 478 SER A O 1 ATOM 3668 C CB . SER A 1 478 ? -14.175 40.155 55.340 1.00 20.94 ? 478 SER A CB 1 ATOM 3669 O OG . SER A 1 478 ? -15.393 40.856 55.181 1.00 23.52 ? 478 SER A OG 1 ATOM 3670 N N . TYR A 1 479 ? -11.080 40.043 55.979 1.00 20.33 ? 479 TYR A N 1 ATOM 3671 C CA . TYR A 1 479 ? -9.852 39.278 56.197 1.00 19.37 ? 479 TYR A CA 1 ATOM 3672 C C . TYR A 1 479 ? -8.794 39.837 55.261 1.00 19.32 ? 479 TYR A C 1 ATOM 3673 O O . TYR A 1 479 ? -9.081 40.705 54.424 1.00 18.74 ? 479 TYR A O 1 ATOM 3674 C CB . TYR A 1 479 ? -10.052 37.775 55.958 1.00 20.20 ? 479 TYR A CB 1 ATOM 3675 C CG . TYR A 1 479 ? -10.602 37.430 54.592 1.00 20.22 ? 479 TYR A CG 1 ATOM 3676 C CD1 . TYR A 1 479 ? -9.762 37.394 53.460 1.00 20.54 ? 479 TYR A CD1 1 ATOM 3677 C CD2 . TYR A 1 479 ? -11.964 37.111 54.425 1.00 21.70 ? 479 TYR A CD2 1 ATOM 3678 C CE1 . TYR A 1 479 ? -10.281 37.066 52.194 1.00 20.62 ? 479 TYR A CE1 1 ATOM 3679 C CE2 . TYR A 1 479 ? -12.482 36.776 53.170 1.00 21.71 ? 479 TYR A CE2 1 ATOM 3680 C CZ . TYR A 1 479 ? -11.630 36.755 52.056 1.00 21.95 ? 479 TYR A CZ 1 ATOM 3681 O OH . TYR A 1 479 ? -12.121 36.427 50.799 1.00 21.86 ? 479 TYR A OH 1 ATOM 3682 N N . ALA A 1 480 ? -7.566 39.361 55.449 1.00 19.02 ? 480 ALA A N 1 ATOM 3683 C CA . ALA A 1 480 ? -6.457 39.740 54.592 1.00 19.02 ? 480 ALA A CA 1 ATOM 3684 C C . ALA A 1 480 ? -5.674 38.526 54.162 1.00 18.91 ? 480 ALA A C 1 ATOM 3685 O O . ALA A 1 480 ? -5.564 37.531 54.897 1.00 18.93 ? 480 ALA A O 1 ATOM 3686 C CB . ALA A 1 480 ? -5.537 40.713 55.287 1.00 19.55 ? 480 ALA A CB 1 ATOM 3687 N N . ILE A 1 481 ? -5.130 38.627 52.955 1.00 18.09 ? 481 ILE A N 1 ATOM 3688 C CA . ILE A 1 481 ? -4.157 37.665 52.462 1.00 17.81 ? 481 ILE A CA 1 ATOM 3689 C C . ILE A 1 481 ? -2.864 38.449 52.306 1.00 17.70 ? 481 ILE A C 1 ATOM 3690 O O . ILE A 1 481 ? -2.815 39.470 51.615 1.00 18.22 ? 481 ILE A O 1 ATOM 3691 C CB . ILE A 1 481 ? -4.594 37.053 51.111 1.00 17.64 ? 481 ILE A CB 1 ATOM 3692 C CG1 . ILE A 1 481 ? -5.859 36.193 51.309 1.00 17.30 ? 481 ILE A CG1 1 ATOM 3693 C CG2 . ILE A 1 481 ? -3.442 36.214 50.515 1.00 18.42 ? 481 ILE A CG2 1 ATOM 3694 C CD1 . ILE A 1 481 ? -6.639 35.936 49.985 1.00 17.92 ? 481 ILE A CD1 1 ATOM 3695 N N . VAL A 1 482 ? -1.812 37.988 52.971 1.00 17.84 ? 482 VAL A N 1 ATOM 3696 C CA . VAL A 1 482 ? -0.555 38.733 52.966 1.00 18.19 ? 482 VAL A CA 1 ATOM 3697 C C . VAL A 1 482 ? 0.588 37.818 52.516 1.00 17.65 ? 482 VAL A C 1 ATOM 3698 O O . VAL A 1 482 ? 0.784 36.748 53.089 1.00 18.74 ? 482 VAL A O 1 ATOM 3699 C CB . VAL A 1 482 ? -0.293 39.428 54.341 1.00 18.97 ? 482 VAL A CB 1 ATOM 3700 C CG1 . VAL A 1 482 ? -0.468 38.447 55.488 1.00 21.89 ? 482 VAL A CG1 1 ATOM 3701 C CG2 . VAL A 1 482 ? 1.072 40.124 54.361 1.00 19.36 ? 482 VAL A CG2 1 ATOM 3702 N N . ALA A 1 483 ? 1.324 38.239 51.483 1.00 17.11 ? 483 ALA A N 1 ATOM 3703 C CA . ALA A 1 483 ? 2.352 37.381 50.883 1.00 17.56 ? 483 ALA A CA 1 ATOM 3704 C C . ALA A 1 483 ? 3.709 38.042 51.015 1.00 17.41 ? 483 ALA A C 1 ATOM 3705 O O . ALA A 1 483 ? 3.890 39.197 50.601 1.00 17.92 ? 483 ALA A O 1 ATOM 3706 C CB . ALA A 1 483 ? 2.048 37.099 49.402 1.00 18.08 ? 483 ALA A CB 1 ATOM 3707 N N . VAL A 1 484 ? 4.658 37.302 51.587 1.00 17.45 ? 484 VAL A N 1 ATOM 3708 C CA . VAL A 1 484 ? 5.999 37.803 51.851 1.00 17.35 ? 484 VAL A CA 1 ATOM 3709 C C . VAL A 1 484 ? 6.996 36.659 51.640 1.00 16.99 ? 484 VAL A C 1 ATOM 3710 O O . VAL A 1 484 ? 6.599 35.496 51.478 1.00 16.90 ? 484 VAL A O 1 ATOM 3711 C CB . VAL A 1 484 ? 6.146 38.346 53.310 1.00 16.91 ? 484 VAL A CB 1 ATOM 3712 C CG1 . VAL A 1 484 ? 5.227 39.552 53.544 1.00 18.29 ? 484 VAL A CG1 1 ATOM 3713 C CG2 . VAL A 1 484 ? 5.860 37.237 54.339 1.00 17.20 ? 484 VAL A CG2 1 ATOM 3714 N N . GLY A 1 485 ? 8.291 36.984 51.638 1.00 16.96 ? 485 GLY A N 1 ATOM 3715 C CA . GLY A 1 485 ? 9.286 35.916 51.569 1.00 17.01 ? 485 GLY A CA 1 ATOM 3716 C C . GLY A 1 485 ? 10.615 36.306 50.954 1.00 16.59 ? 485 GLY A C 1 ATOM 3717 O O . GLY A 1 485 ? 11.049 37.468 51.030 1.00 17.15 ? 485 GLY A O 1 ATOM 3718 N N . GLU A 1 486 ? 11.281 35.304 50.383 1.00 16.23 ? 486 GLU A N 1 ATOM 3719 C CA . GLU A 1 486 ? 12.634 35.481 49.857 1.00 16.76 ? 486 GLU A CA 1 ATOM 3720 C C . GLU A 1 486 ? 12.597 36.150 48.493 1.00 17.89 ? 486 GLU A C 1 ATOM 3721 O O . GLU A 1 486 ? 11.616 36.007 47.760 1.00 17.87 ? 486 GLU A O 1 ATOM 3722 C CB . GLU A 1 486 ? 13.317 34.116 49.715 1.00 16.97 ? 486 GLU A CB 1 ATOM 3723 C CG . GLU A 1 486 ? 13.596 33.396 51.046 1.00 18.70 ? 486 GLU A CG 1 ATOM 3724 C CD . GLU A 1 486 ? 14.577 32.250 50.851 1.00 18.82 ? 486 GLU A CD 1 ATOM 3725 O OE1 . GLU A 1 486 ? 14.254 31.293 50.114 1.00 19.68 ? 486 GLU A OE1 1 ATOM 3726 O OE2 . GLU A 1 486 ? 15.684 32.315 51.434 1.00 21.21 ? 486 GLU A OE2 1 ATOM 3727 N N . HIS A 1 487 ? 13.678 36.847 48.159 1.00 18.20 ? 487 HIS A N 1 ATOM 3728 C CA . HIS A 1 487 ? 13.876 37.371 46.802 1.00 18.32 ? 487 HIS A CA 1 ATOM 3729 C C . HIS A 1 487 ? 14.500 36.266 45.938 1.00 17.94 ? 487 HIS A C 1 ATOM 3730 O O . HIS A 1 487 ? 15.037 35.295 46.477 1.00 18.23 ? 487 HIS A O 1 ATOM 3731 C CB . HIS A 1 487 ? 14.729 38.641 46.846 1.00 19.64 ? 487 HIS A CB 1 ATOM 3732 C CG . HIS A 1 487 ? 14.072 39.761 47.599 1.00 22.43 ? 487 HIS A CG 1 ATOM 3733 N ND1 . HIS A 1 487 ? 14.754 40.865 48.062 1.00 27.47 ? 487 HIS A ND1 1 ATOM 3734 C CD2 . HIS A 1 487 ? 12.789 39.915 48.008 1.00 26.08 ? 487 HIS A CD2 1 ATOM 3735 C CE1 . HIS A 1 487 ? 13.914 41.664 48.699 1.00 26.42 ? 487 HIS A CE1 1 ATOM 3736 N NE2 . HIS A 1 487 ? 12.715 41.110 48.682 1.00 27.01 ? 487 HIS A NE2 1 ATOM 3737 N N . PRO A 1 488 ? 14.368 36.366 44.602 1.00 17.71 ? 488 PRO A N 1 ATOM 3738 C CA . PRO A 1 488 ? 14.955 35.330 43.728 1.00 17.30 ? 488 PRO A CA 1 ATOM 3739 C C . PRO A 1 488 ? 16.478 35.222 43.859 1.00 17.45 ? 488 PRO A C 1 ATOM 3740 O O . PRO A 1 488 ? 17.174 36.229 44.044 1.00 17.79 ? 488 PRO A O 1 ATOM 3741 C CB . PRO A 1 488 ? 14.573 35.802 42.308 1.00 16.79 ? 488 PRO A CB 1 ATOM 3742 C CG . PRO A 1 488 ? 13.295 36.608 42.532 1.00 17.55 ? 488 PRO A CG 1 ATOM 3743 C CD . PRO A 1 488 ? 13.590 37.362 43.833 1.00 17.46 ? 488 PRO A CD 1 ATOM 3744 N N . TYR A 1 489 ? 16.981 34.000 43.752 1.00 16.90 ? 489 TYR A N 1 ATOM 3745 C CA . TYR A 1 489 ? 18.431 33.761 43.805 1.00 17.56 ? 489 TYR A CA 1 ATOM 3746 C C . TYR A 1 489 ? 18.726 32.432 43.156 1.00 17.29 ? 489 TYR A C 1 ATOM 3747 O O . TYR A 1 489 ? 17.841 31.563 43.047 1.00 17.05 ? 489 TYR A O 1 ATOM 3748 C CB . TYR A 1 489 ? 18.948 33.767 45.261 1.00 17.81 ? 489 TYR A CB 1 ATOM 3749 C CG . TYR A 1 489 ? 18.220 32.775 46.156 1.00 17.79 ? 489 TYR A CG 1 ATOM 3750 C CD1 . TYR A 1 489 ? 18.516 31.409 46.114 1.00 15.98 ? 489 TYR A CD1 1 ATOM 3751 C CD2 . TYR A 1 489 ? 17.202 33.209 47.029 1.00 16.87 ? 489 TYR A CD2 1 ATOM 3752 C CE1 . TYR A 1 489 ? 17.828 30.482 46.922 1.00 17.56 ? 489 TYR A CE1 1 ATOM 3753 C CE2 . TYR A 1 489 ? 16.499 32.300 47.826 1.00 17.70 ? 489 TYR A CE2 1 ATOM 3754 C CZ . TYR A 1 489 ? 16.824 30.950 47.779 1.00 17.95 ? 489 TYR A CZ 1 ATOM 3755 O OH . TYR A 1 489 ? 16.121 30.070 48.572 1.00 19.20 ? 489 TYR A OH 1 ATOM 3756 N N . THR A 1 490 ? 19.988 32.256 42.779 1.00 17.46 ? 490 THR A N 1 ATOM 3757 C CA . THR A 1 490 ? 20.444 31.035 42.127 1.00 18.51 ? 490 THR A CA 1 ATOM 3758 C C . THR A 1 490 ? 21.895 30.782 42.544 1.00 18.84 ? 490 THR A C 1 ATOM 3759 O O . THR A 1 490 ? 22.683 31.724 42.655 1.00 18.39 ? 490 THR A O 1 ATOM 3760 C CB . THR A 1 490 ? 20.345 31.197 40.589 1.00 18.83 ? 490 THR A CB 1 ATOM 3761 O OG1 . THR A 1 490 ? 18.989 31.529 40.248 1.00 19.03 ? 490 THR A OG1 1 ATOM 3762 C CG2 . THR A 1 490 ? 20.738 29.912 39.876 1.00 20.07 ? 490 THR A CG2 1 ATOM 3763 N N . GLU A 1 491 ? 22.218 29.511 42.773 1.00 19.30 ? 491 GLU A N 1 ATOM 3764 C CA . GLU A 1 491 ? 23.601 29.075 43.041 1.00 20.41 ? 491 GLU A CA 1 ATOM 3765 C C . GLU A 1 491 ? 24.186 29.881 44.225 1.00 20.71 ? 491 GLU A C 1 ATOM 3766 O O . GLU A 1 491 ? 23.482 30.080 45.228 1.00 20.53 ? 491 GLU A O 1 ATOM 3767 C CB . GLU A 1 491 ? 24.441 29.102 41.746 1.00 20.37 ? 491 GLU A CB 1 ATOM 3768 C CG . GLU A 1 491 ? 23.951 28.042 40.737 1.00 21.20 ? 491 GLU A CG 1 ATOM 3769 C CD . GLU A 1 491 ? 24.670 28.072 39.398 1.00 21.57 ? 491 GLU A CD 1 ATOM 3770 O OE1 . GLU A 1 491 ? 25.877 27.744 39.372 1.00 24.63 ? 491 GLU A OE1 1 ATOM 3771 O OE2 . GLU A 1 491 ? 24.028 28.377 38.364 1.00 23.01 ? 491 GLU A OE2 1 ATOM 3772 N N . THR A 1 492 ? 25.423 30.370 44.120 1.00 21.00 ? 492 THR A N 1 ATOM 3773 C CA . THR A 1 492 ? 26.106 30.941 45.303 1.00 21.98 ? 492 THR A CA 1 ATOM 3774 C C . THR A 1 492 ? 25.407 32.164 45.894 1.00 21.91 ? 492 THR A C 1 ATOM 3775 O O . THR A 1 492 ? 25.397 32.352 47.126 1.00 21.87 ? 492 THR A O 1 ATOM 3776 C CB . THR A 1 492 ? 27.614 31.181 45.029 1.00 22.15 ? 492 THR A CB 1 ATOM 3777 O OG1 . THR A 1 492 ? 28.177 29.950 44.571 1.00 22.83 ? 492 THR A OG1 1 ATOM 3778 C CG2 . THR A 1 492 ? 28.353 31.612 46.308 1.00 23.03 ? 492 THR A CG2 1 ATOM 3779 N N . LYS A 1 493 ? 24.769 32.966 45.040 1.00 21.98 ? 493 LYS A N 1 ATOM 3780 C CA . LYS A 1 493 ? 24.014 34.124 45.519 1.00 23.58 ? 493 LYS A CA 1 ATOM 3781 C C . LYS A 1 493 ? 22.930 33.757 46.535 1.00 22.92 ? 493 LYS A C 1 ATOM 3782 O O . LYS A 1 493 ? 22.510 34.609 47.319 1.00 24.34 ? 493 LYS A O 1 ATOM 3783 C CB . LYS A 1 493 ? 23.401 34.910 44.357 1.00 23.81 ? 493 LYS A CB 1 ATOM 3784 C CG . LYS A 1 493 ? 24.424 35.684 43.532 1.00 29.37 ? 493 LYS A CG 1 ATOM 3785 C CD . LYS A 1 493 ? 24.782 37.014 44.170 1.00 35.77 ? 493 LYS A CD 1 ATOM 3786 C CE . LYS A 1 493 ? 25.276 38.016 43.122 1.00 38.56 ? 493 LYS A CE 1 ATOM 3787 N NZ . LYS A 1 493 ? 25.717 39.285 43.797 1.00 42.58 ? 493 LYS A NZ 1 ATOM 3788 N N . GLY A 1 494 ? 22.491 32.500 46.529 1.00 21.74 ? 494 GLY A N 1 ATOM 3789 C CA . GLY A 1 494 ? 21.467 32.035 47.469 1.00 22.39 ? 494 GLY A CA 1 ATOM 3790 C C . GLY A 1 494 ? 21.987 31.442 48.771 1.00 21.70 ? 494 GLY A C 1 ATOM 3791 O O . GLY A 1 494 ? 21.191 31.144 49.686 1.00 21.94 ? 494 GLY A O 1 ATOM 3792 N N . ASP A 1 495 ? 23.299 31.198 48.852 1.00 22.02 ? 495 ASP A N 1 ATOM 3793 C CA . ASP A 1 495 ? 23.899 30.694 50.103 1.00 21.92 ? 495 ASP A CA 1 ATOM 3794 C C . ASP A 1 495 ? 23.594 31.706 51.209 1.00 21.98 ? 495 ASP A C 1 ATOM 3795 O O . ASP A 1 495 ? 23.791 32.902 51.033 1.00 22.56 ? 495 ASP A O 1 ATOM 3796 C CB . ASP A 1 495 ? 25.428 30.526 49.970 1.00 21.69 ? 495 ASP A CB 1 ATOM 3797 C CG . ASP A 1 495 ? 25.834 29.326 49.107 1.00 22.21 ? 495 ASP A CG 1 ATOM 3798 O OD1 . ASP A 1 495 ? 24.958 28.558 48.643 1.00 21.75 ? 495 ASP A OD1 1 ATOM 3799 O OD2 . ASP A 1 495 ? 27.073 29.138 48.907 1.00 22.85 ? 495 ASP A OD2 1 ATOM 3800 N N . ASN A 1 496 ? 23.094 31.226 52.341 1.00 22.31 ? 496 ASN A N 1 ATOM 3801 C CA . ASN A 1 496 ? 22.543 32.127 53.351 1.00 22.43 ? 496 ASN A CA 1 ATOM 3802 C C . ASN A 1 496 ? 22.626 31.458 54.717 1.00 22.66 ? 496 ASN A C 1 ATOM 3803 O O . ASN A 1 496 ? 22.000 30.423 54.942 1.00 21.90 ? 496 ASN A O 1 ATOM 3804 C CB . ASN A 1 496 ? 21.081 32.419 52.980 1.00 22.50 ? 496 ASN A CB 1 ATOM 3805 C CG . ASN A 1 496 ? 20.434 33.470 53.852 1.00 23.71 ? 496 ASN A CG 1 ATOM 3806 O OD1 . ASN A 1 496 ? 20.781 33.652 55.029 1.00 23.81 ? 496 ASN A OD1 1 ATOM 3807 N ND2 . ASN A 1 496 ? 19.461 34.176 53.270 1.00 24.96 ? 496 ASN A ND2 1 ATOM 3808 N N . LEU A 1 497 ? 23.417 32.051 55.616 1.00 23.86 ? 497 LEU A N 1 ATOM 3809 C CA . LEU A 1 497 ? 23.642 31.449 56.930 1.00 25.18 ? 497 LEU A CA 1 ATOM 3810 C C . LEU A 1 497 ? 22.591 31.825 57.979 1.00 25.73 ? 497 LEU A C 1 ATOM 3811 O O . LEU A 1 497 ? 22.537 31.193 59.043 1.00 26.89 ? 497 LEU A O 1 ATOM 3812 C CB . LEU A 1 497 ? 25.039 31.811 57.456 1.00 25.54 ? 497 LEU A CB 1 ATOM 3813 C CG . LEU A 1 497 ? 26.249 31.307 56.666 1.00 25.44 ? 497 LEU A CG 1 ATOM 3814 C CD1 . LEU A 1 497 ? 27.511 31.824 57.367 1.00 27.54 ? 497 LEU A CD1 1 ATOM 3815 C CD2 . LEU A 1 497 ? 26.256 29.783 56.535 1.00 25.85 ? 497 LEU A CD2 1 ATOM 3816 N N . ASN A 1 498 ? 21.766 32.834 57.693 1.00 25.25 ? 498 ASN A N 1 ATOM 3817 C CA . ASN A 1 498 ? 20.791 33.318 58.683 1.00 26.02 ? 498 ASN A CA 1 ATOM 3818 C C . ASN A 1 498 ? 19.343 32.921 58.381 1.00 24.36 ? 498 ASN A C 1 ATOM 3819 O O . ASN A 1 498 ? 18.513 32.802 59.298 1.00 23.59 ? 498 ASN A O 1 ATOM 3820 C CB . ASN A 1 498 ? 20.905 34.834 58.862 1.00 27.83 ? 498 ASN A CB 1 ATOM 3821 C CG . ASN A 1 498 ? 20.538 35.610 57.608 1.00 35.01 ? 498 ASN A CG 1 ATOM 3822 O OD1 . ASN A 1 498 ? 19.348 35.712 57.246 1.00 38.07 ? 498 ASN A OD1 1 ATOM 3823 N ND2 . ASN A 1 498 ? 21.558 36.206 56.957 1.00 44.91 ? 498 ASN A ND2 1 ATOM 3824 N N . LEU A 1 499 ? 19.047 32.721 57.096 1.00 23.38 ? 499 LEU A N 1 ATOM 3825 C CA . LEU A 1 499 ? 17.720 32.242 56.657 1.00 23.22 ? 499 LEU A CA 1 ATOM 3826 C C . LEU A 1 499 ? 16.544 33.019 57.250 1.00 23.33 ? 499 LEU A C 1 ATOM 3827 O O . LEU A 1 499 ? 15.521 32.432 57.627 1.00 22.96 ? 499 LEU A O 1 ATOM 3828 C CB . LEU A 1 499 ? 17.574 30.750 56.940 1.00 22.70 ? 499 LEU A CB 1 ATOM 3829 C CG . LEU A 1 499 ? 17.946 29.719 55.869 1.00 26.64 ? 499 LEU A CG 1 ATOM 3830 C CD1 . LEU A 1 499 ? 18.684 30.262 54.639 1.00 25.72 ? 499 LEU A CD1 1 ATOM 3831 C CD2 . LEU A 1 499 ? 18.479 28.412 56.396 1.00 23.47 ? 499 LEU A CD2 1 ATOM 3832 N N . THR A 1 500 ? 16.698 34.334 57.316 1.00 23.39 ? 500 THR A N 1 ATOM 3833 C CA . THR A 1 500 ? 15.618 35.223 57.742 1.00 25.18 ? 500 THR A CA 1 ATOM 3834 C C . THR A 1 500 ? 15.119 35.961 56.507 1.00 25.26 ? 500 THR A C 1 ATOM 3835 O O . THR A 1 500 ? 15.916 36.354 55.644 1.00 25.42 ? 500 THR A O 1 ATOM 3836 C CB . THR A 1 500 ? 16.099 36.217 58.822 1.00 25.89 ? 500 THR A CB 1 ATOM 3837 O OG1 . THR A 1 500 ? 17.178 37.007 58.302 1.00 29.39 ? 500 THR A OG1 1 ATOM 3838 C CG2 . THR A 1 500 ? 16.592 35.441 60.017 1.00 25.23 ? 500 THR A CG2 1 ATOM 3839 N N . ILE A 1 501 ? 13.813 36.144 56.391 1.00 25.89 ? 501 ILE A N 1 ATOM 3840 C CA . ILE A 1 501 ? 13.331 36.779 55.161 1.00 27.20 ? 501 ILE A CA 1 ATOM 3841 C C . ILE A 1 501 ? 13.627 38.281 55.167 1.00 28.31 ? 501 ILE A C 1 ATOM 3842 O O . ILE A 1 501 ? 13.706 38.885 56.245 1.00 28.04 ? 501 ILE A O 1 ATOM 3843 C CB . ILE A 1 501 ? 11.834 36.518 54.895 1.00 27.22 ? 501 ILE A CB 1 ATOM 3844 C CG1 . ILE A 1 501 ? 10.969 37.102 56.011 1.00 26.76 ? 501 ILE A CG1 1 ATOM 3845 C CG2 . ILE A 1 501 ? 11.582 35.029 54.664 1.00 26.67 ? 501 ILE A CG2 1 ATOM 3846 C CD1 . ILE A 1 501 ? 9.532 37.348 55.587 1.00 29.25 ? 501 ILE A CD1 1 ATOM 3847 N N . PRO A 1 502 ? 13.822 38.886 53.973 1.00 29.71 ? 502 PRO A N 1 ATOM 3848 C CA . PRO A 1 502 ? 14.054 40.328 53.958 1.00 31.13 ? 502 PRO A CA 1 ATOM 3849 C C . PRO A 1 502 ? 12.859 41.144 54.468 1.00 32.02 ? 502 PRO A C 1 ATOM 3850 O O . PRO A 1 502 ? 11.704 40.698 54.415 1.00 32.10 ? 502 PRO A O 1 ATOM 3851 C CB . PRO A 1 502 ? 14.319 40.641 52.474 1.00 31.11 ? 502 PRO A CB 1 ATOM 3852 C CG . PRO A 1 502 ? 13.710 39.512 51.709 1.00 30.93 ? 502 PRO A CG 1 ATOM 3853 C CD . PRO A 1 502 ? 13.840 38.305 52.612 1.00 30.12 ? 502 PRO A CD 1 ATOM 3854 N N . GLU A 1 503 ? 13.166 42.328 54.975 1.00 32.74 ? 503 GLU A N 1 ATOM 3855 C CA . GLU A 1 503 ? 12.151 43.290 55.377 1.00 33.18 ? 503 GLU A CA 1 ATOM 3856 C C . GLU A 1 503 ? 11.977 44.357 54.304 1.00 33.33 ? 503 GLU A C 1 ATOM 3857 O O . GLU A 1 503 ? 12.920 44.627 53.548 1.00 34.21 ? 503 GLU A O 1 ATOM 3858 C CB . GLU A 1 503 ? 12.514 43.897 56.730 1.00 33.22 ? 503 GLU A CB 1 ATOM 3859 C CG . GLU A 1 503 ? 12.421 42.880 57.852 1.00 34.65 ? 503 GLU A CG 1 ATOM 3860 C CD . GLU A 1 503 ? 11.015 42.309 58.006 1.00 33.97 ? 503 GLU A CD 1 ATOM 3861 O OE1 . GLU A 1 503 ? 10.089 43.132 58.232 1.00 33.37 ? 503 GLU A OE1 1 ATOM 3862 O OE2 . GLU A 1 503 ? 10.853 41.049 57.895 1.00 35.74 ? 503 GLU A OE2 1 ATOM 3863 N N . PRO A 1 504 ? 10.760 44.944 54.202 1.00 32.56 ? 504 PRO A N 1 ATOM 3864 C CA . PRO A 1 504 ? 9.605 44.595 55.029 1.00 31.76 ? 504 PRO A CA 1 ATOM 3865 C C . PRO A 1 504 ? 8.988 43.244 54.615 1.00 30.53 ? 504 PRO A C 1 ATOM 3866 O O . PRO A 1 504 ? 8.781 42.950 53.410 1.00 30.98 ? 504 PRO A O 1 ATOM 3867 C CB . PRO A 1 504 ? 8.641 45.764 54.803 1.00 31.83 ? 504 PRO A CB 1 ATOM 3868 C CG . PRO A 1 504 ? 8.963 46.253 53.440 1.00 32.58 ? 504 PRO A CG 1 ATOM 3869 C CD . PRO A 1 504 ? 10.450 46.027 53.251 1.00 33.30 ? 504 PRO A CD 1 ATOM 3870 N N . GLY A 1 505 ? 8.750 42.414 55.621 1.00 28.75 ? 505 GLY A N 1 ATOM 3871 C CA . GLY A 1 505 ? 8.034 41.155 55.449 1.00 26.07 ? 505 GLY A CA 1 ATOM 3872 C C . GLY A 1 505 ? 7.319 40.886 56.753 1.00 24.57 ? 505 GLY A C 1 ATOM 3873 O O . GLY A 1 505 ? 6.084 40.960 56.832 1.00 23.04 ? 505 GLY A O 1 ATOM 3874 N N . LEU A 1 506 ? 8.097 40.584 57.795 1.00 23.77 ? 506 LEU A N 1 ATOM 3875 C CA . LEU A 1 506 ? 7.514 40.394 59.120 1.00 24.02 ? 506 LEU A CA 1 ATOM 3876 C C . LEU A 1 506 ? 6.726 41.623 59.591 1.00 23.85 ? 506 LEU A C 1 ATOM 3877 O O . LEU A 1 506 ? 5.631 41.477 60.148 1.00 23.63 ? 506 LEU A O 1 ATOM 3878 C CB . LEU A 1 506 ? 8.611 40.039 60.144 1.00 23.86 ? 506 LEU A CB 1 ATOM 3879 C CG . LEU A 1 506 ? 8.134 39.825 61.579 1.00 24.04 ? 506 LEU A CG 1 ATOM 3880 C CD1 . LEU A 1 506 ? 7.114 38.701 61.720 1.00 24.08 ? 506 LEU A CD1 1 ATOM 3881 C CD2 . LEU A 1 506 ? 9.369 39.544 62.439 1.00 24.68 ? 506 LEU A CD2 1 ATOM 3882 N N . SER A 1 507 ? 7.264 42.824 59.360 1.00 24.43 ? 507 SER A N 1 ATOM 3883 C CA . SER A 1 507 ? 6.579 44.043 59.826 1.00 25.06 ? 507 SER A CA 1 ATOM 3884 C C . SER A 1 507 ? 5.203 44.203 59.158 1.00 24.31 ? 507 SER A C 1 ATOM 3885 O O . SER A 1 507 ? 4.241 44.585 59.821 1.00 24.52 ? 507 SER A O 1 ATOM 3886 C CB . SER A 1 507 ? 7.433 45.298 59.635 1.00 25.85 ? 507 SER A CB 1 ATOM 3887 O OG . SER A 1 507 ? 7.745 45.479 58.267 1.00 28.19 ? 507 SER A OG 1 ATOM 3888 N N . THR A 1 508 ? 5.120 43.879 57.863 1.00 23.66 ? 508 THR A N 1 ATOM 3889 C CA . THR A 1 508 ? 3.844 43.901 57.136 1.00 22.84 ? 508 THR A CA 1 ATOM 3890 C C . THR A 1 508 ? 2.853 42.876 57.702 1.00 21.53 ? 508 THR A C 1 ATOM 3891 O O . THR A 1 508 ? 1.689 43.194 57.926 1.00 20.72 ? 508 THR A O 1 ATOM 3892 C CB . THR A 1 508 ? 4.073 43.670 55.618 1.00 23.18 ? 508 THR A CB 1 ATOM 3893 O OG1 . THR A 1 508 ? 4.996 44.659 55.163 1.00 27.43 ? 508 THR A OG1 1 ATOM 3894 C CG2 . THR A 1 508 ? 2.783 43.814 54.825 1.00 22.75 ? 508 THR A CG2 1 ATOM 3895 N N . VAL A 1 509 ? 3.316 41.642 57.914 1.00 20.59 ? 509 VAL A N 1 ATOM 3896 C CA . VAL A 1 509 ? 2.471 40.609 58.494 1.00 20.04 ? 509 VAL A CA 1 ATOM 3897 C C . VAL A 1 509 ? 1.937 41.071 59.849 1.00 20.88 ? 509 VAL A C 1 ATOM 3898 O O . VAL A 1 509 ? 0.751 40.948 60.109 1.00 19.92 ? 509 VAL A O 1 ATOM 3899 C CB . VAL A 1 509 ? 3.207 39.248 58.559 1.00 19.90 ? 509 VAL A CB 1 ATOM 3900 C CG1 . VAL A 1 509 ? 2.406 38.201 59.339 1.00 20.35 ? 509 VAL A CG1 1 ATOM 3901 C CG2 . VAL A 1 509 ? 3.498 38.759 57.118 1.00 20.79 ? 509 VAL A CG2 1 ATOM 3902 N N . GLN A 1 510 ? 2.814 41.605 60.698 1.00 21.47 ? 510 GLN A N 1 ATOM 3903 C CA . GLN A 1 510 ? 2.385 42.081 62.013 1.00 23.09 ? 510 GLN A CA 1 ATOM 3904 C C . GLN A 1 510 ? 1.358 43.210 61.937 1.00 23.18 ? 510 GLN A C 1 ATOM 3905 O O . GLN A 1 510 ? 0.372 43.185 62.674 1.00 24.30 ? 510 GLN A O 1 ATOM 3906 C CB . GLN A 1 510 ? 3.599 42.493 62.844 1.00 22.70 ? 510 GLN A CB 1 ATOM 3907 C CG . GLN A 1 510 ? 4.496 41.302 63.209 1.00 23.20 ? 510 GLN A CG 1 ATOM 3908 C CD . GLN A 1 510 ? 5.824 41.728 63.833 1.00 24.44 ? 510 GLN A CD 1 ATOM 3909 O OE1 . GLN A 1 510 ? 6.363 42.808 63.542 1.00 28.50 ? 510 GLN A OE1 1 ATOM 3910 N NE2 . GLN A 1 510 ? 6.369 40.865 64.672 1.00 26.28 ? 510 GLN A NE2 1 ATOM 3911 N N . ALA A 1 511 ? 1.562 44.169 61.034 1.00 23.11 ? 511 ALA A N 1 ATOM 3912 C CA . ALA A 1 511 ? 0.616 45.299 60.879 1.00 23.39 ? 511 ALA A CA 1 ATOM 3913 C C . ALA A 1 511 ? -0.740 44.816 60.373 1.00 23.32 ? 511 ALA A C 1 ATOM 3914 O O . ALA A 1 511 ? -1.798 45.223 60.867 1.00 23.85 ? 511 ALA A O 1 ATOM 3915 C CB . ALA A 1 511 ? 1.198 46.359 59.948 1.00 23.73 ? 511 ALA A CB 1 ATOM 3916 N N . VAL A 1 512 ? -0.712 43.903 59.409 1.00 22.60 ? 512 VAL A N 1 ATOM 3917 C CA . VAL A 1 512 ? -1.947 43.393 58.835 1.00 22.53 ? 512 VAL A CA 1 ATOM 3918 C C . VAL A 1 512 ? -2.700 42.506 59.822 1.00 22.83 ? 512 VAL A C 1 ATOM 3919 O O . VAL A 1 512 ? -3.888 42.726 60.091 1.00 22.47 ? 512 VAL A O 1 ATOM 3920 C CB . VAL A 1 512 ? -1.676 42.659 57.507 1.00 22.24 ? 512 VAL A CB 1 ATOM 3921 C CG1 . VAL A 1 512 ? -2.948 41.923 57.008 1.00 23.67 ? 512 VAL A CG1 1 ATOM 3922 C CG2 . VAL A 1 512 ? -1.130 43.647 56.482 1.00 22.32 ? 512 VAL A CG2 1 ATOM 3923 N N . CYS A 1 513 ? -2.023 41.492 60.354 1.00 22.69 ? 513 CYS A N 1 ATOM 3924 C CA . CYS A 1 513 ? -2.705 40.537 61.195 1.00 23.41 ? 513 CYS A CA 1 ATOM 3925 C C . CYS A 1 513 ? -3.113 41.161 62.551 1.00 23.57 ? 513 CYS A C 1 ATOM 3926 O O . CYS A 1 513 ? -4.042 40.685 63.200 1.00 24.53 ? 513 CYS A O 1 ATOM 3927 C CB . CYS A 1 513 ? -1.834 39.323 61.412 1.00 23.45 ? 513 CYS A CB 1 ATOM 3928 S SG . CYS A 1 513 ? -1.141 38.465 59.952 1.00 26.57 ? 513 CYS A SG 1 ATOM 3929 N N . GLY A 1 514 ? -2.435 42.234 62.952 1.00 23.93 ? 514 GLY A N 1 ATOM 3930 C CA . GLY A 1 514 ? -2.849 42.996 64.144 1.00 25.34 ? 514 GLY A CA 1 ATOM 3931 C C . GLY A 1 514 ? -4.205 43.675 63.987 1.00 25.98 ? 514 GLY A C 1 ATOM 3932 O O . GLY A 1 514 ? -4.875 43.992 64.991 1.00 27.28 ? 514 GLY A O 1 ATOM 3933 N N . GLY A 1 515 ? -4.622 43.885 62.737 1.00 25.70 ? 515 GLY A N 1 ATOM 3934 C CA . GLY A 1 515 ? -5.859 44.613 62.422 1.00 25.35 ? 515 GLY A CA 1 ATOM 3935 C C . GLY A 1 515 ? -7.028 43.772 61.951 1.00 25.15 ? 515 GLY A C 1 ATOM 3936 O O . GLY A 1 515 ? -8.194 44.169 62.111 1.00 25.60 ? 515 GLY A O 1 ATOM 3937 N N . VAL A 1 516 ? -6.737 42.606 61.373 1.00 23.91 ? 516 VAL A N 1 ATOM 3938 C CA . VAL A 1 516 ? -7.771 41.767 60.780 1.00 23.60 ? 516 VAL A CA 1 ATOM 3939 C C . VAL A 1 516 ? -7.240 40.339 60.713 1.00 22.87 ? 516 VAL A C 1 ATOM 3940 O O . VAL A 1 516 ? -6.014 40.145 60.717 1.00 22.63 ? 516 VAL A O 1 ATOM 3941 C CB . VAL A 1 516 ? -8.175 42.291 59.362 1.00 24.05 ? 516 VAL A CB 1 ATOM 3942 C CG1 . VAL A 1 516 ? -7.068 42.007 58.360 1.00 24.32 ? 516 VAL A CG1 1 ATOM 3943 C CG2 . VAL A 1 516 ? -9.485 41.693 58.897 1.00 25.70 ? 516 VAL A CG2 1 ATOM 3944 N N . ARG A 1 517 ? -8.142 39.356 60.701 1.00 22.13 ? 517 ARG A N 1 ATOM 3945 C CA . ARG A 1 517 ? -7.740 37.951 60.547 1.00 22.40 ? 517 ARG A CA 1 ATOM 3946 C C . ARG A 1 517 ? -7.006 37.803 59.227 1.00 22.37 ? 517 ARG A C 1 ATOM 3947 O O . ARG A 1 517 ? -7.384 38.416 58.244 1.00 20.85 ? 517 ARG A O 1 ATOM 3948 C CB A ARG A 1 517 ? -8.961 37.019 60.639 0.50 23.06 ? 517 ARG A CB 1 ATOM 3949 C CB B ARG A 1 517 ? -8.936 37.018 60.558 0.50 22.79 ? 517 ARG A CB 1 ATOM 3950 C CG A ARG A 1 517 ? -10.102 37.295 59.645 0.50 24.29 ? 517 ARG A CG 1 ATOM 3951 C CG B ARG A 1 517 ? -9.423 36.732 61.931 0.50 22.48 ? 517 ARG A CG 1 ATOM 3952 C CD A ARG A 1 517 ? -11.478 37.114 60.304 0.50 22.71 ? 517 ARG A CD 1 ATOM 3953 C CD B ARG A 1 517 ? -10.367 35.545 61.940 0.50 24.14 ? 517 ARG A CD 1 ATOM 3954 N NE A ARG A 1 517 ? -12.361 36.288 59.486 0.50 31.37 ? 517 ARG A NE 1 ATOM 3955 N NE B ARG A 1 517 ? -9.697 34.293 62.307 0.50 23.13 ? 517 ARG A NE 1 ATOM 3956 C CZ A ARG A 1 517 ? -12.542 34.982 59.675 0.50 18.53 ? 517 ARG A CZ 1 ATOM 3957 C CZ B ARG A 1 517 ? -10.237 33.085 62.135 0.50 21.96 ? 517 ARG A CZ 1 ATOM 3958 N NH1 A ARG A 1 517 ? -11.924 34.330 60.662 0.50 37.81 ? 517 ARG A NH1 1 ATOM 3959 N NH1 B ARG A 1 517 ? -11.459 32.974 61.573 0.50 18.04 ? 517 ARG A NH1 1 ATOM 3960 N NH2 A ARG A 1 517 ? -13.344 34.309 58.870 0.50 39.77 ? 517 ARG A NH2 1 ATOM 3961 N NH2 B ARG A 1 517 ? -9.546 32.002 62.495 0.50 18.04 ? 517 ARG A NH2 1 ATOM 3962 N N . CYS A 1 518 ? -5.962 36.989 59.219 1.00 22.99 ? 518 CYS A N 1 ATOM 3963 C CA . CYS A 1 518 ? -4.969 37.093 58.157 1.00 22.24 ? 518 CYS A CA 1 ATOM 3964 C C . CYS A 1 518 ? -4.425 35.709 57.792 1.00 21.33 ? 518 CYS A C 1 ATOM 3965 O O . CYS A 1 518 ? -4.130 34.872 58.670 1.00 20.89 ? 518 CYS A O 1 ATOM 3966 C CB A CYS A 1 518 ? -3.805 38.016 58.504 0.50 21.42 ? 518 CYS A CB 1 ATOM 3967 C CB B CYS A 1 518 ? -3.954 38.055 58.789 0.50 23.48 ? 518 CYS A CB 1 ATOM 3968 S SG A CYS A 1 518 ? -2.678 37.203 59.656 0.50 20.85 ? 518 CYS A SG 1 ATOM 3969 S SG B CYS A 1 518 ? -2.331 38.312 58.251 0.50 28.47 ? 518 CYS A SG 1 ATOM 3970 N N . ALA A 1 519 ? -4.355 35.452 56.482 1.00 19.51 ? 519 ALA A N 1 ATOM 3971 C CA . ALA A 1 519 ? -3.720 34.255 55.945 1.00 18.36 ? 519 ALA A CA 1 ATOM 3972 C C . ALA A 1 519 ? -2.397 34.711 55.341 1.00 17.44 ? 519 ALA A C 1 ATOM 3973 O O . ALA A 1 519 ? -2.384 35.502 54.390 1.00 18.05 ? 519 ALA A O 1 ATOM 3974 C CB . ALA A 1 519 ? -4.607 33.620 54.852 1.00 17.77 ? 519 ALA A CB 1 ATOM 3975 N N . THR A 1 520 ? -1.291 34.237 55.904 1.00 16.94 ? 520 THR A N 1 ATOM 3976 C CA . THR A 1 520 ? 0.044 34.579 55.408 1.00 17.39 ? 520 THR A CA 1 ATOM 3977 C C . THR A 1 520 ? 0.530 33.517 54.426 1.00 17.10 ? 520 THR A C 1 ATOM 3978 O O . THR A 1 520 ? 0.548 32.320 54.733 1.00 17.84 ? 520 THR A O 1 ATOM 3979 C CB . THR A 1 520 ? 1.037 34.715 56.590 1.00 17.82 ? 520 THR A CB 1 ATOM 3980 O OG1 . THR A 1 520 ? 0.622 35.820 57.399 1.00 19.29 ? 520 THR A OG1 1 ATOM 3981 C CG2 . THR A 1 520 ? 2.463 34.957 56.097 1.00 18.75 ? 520 THR A CG2 1 ATOM 3982 N N . VAL A 1 521 ? 0.913 33.973 53.235 1.00 16.82 ? 521 VAL A N 1 ATOM 3983 C CA . VAL A 1 521 ? 1.498 33.106 52.223 1.00 16.91 ? 521 VAL A CA 1 ATOM 3984 C C . VAL A 1 521 ? 3.003 33.391 52.173 1.00 16.57 ? 521 VAL A C 1 ATOM 3985 O O . VAL A 1 521 ? 3.444 34.497 51.802 1.00 16.98 ? 521 VAL A O 1 ATOM 3986 C CB . VAL A 1 521 ? 0.850 33.328 50.838 1.00 16.69 ? 521 VAL A CB 1 ATOM 3987 C CG1 . VAL A 1 521 ? 1.490 32.382 49.794 1.00 16.89 ? 521 VAL A CG1 1 ATOM 3988 C CG2 . VAL A 1 521 ? -0.670 33.112 50.893 1.00 17.53 ? 521 VAL A CG2 1 ATOM 3989 N N . LEU A 1 522 ? 3.787 32.383 52.543 1.00 16.19 ? 522 LEU A N 1 ATOM 3990 C CA . LEU A 1 522 ? 5.236 32.524 52.595 1.00 16.23 ? 522 LEU A CA 1 ATOM 3991 C C . LEU A 1 522 ? 5.848 31.967 51.307 1.00 15.90 ? 522 LEU A C 1 ATOM 3992 O O . LEU A 1 522 ? 5.693 30.782 51.006 1.00 16.20 ? 522 LEU A O 1 ATOM 3993 C CB . LEU A 1 522 ? 5.772 31.763 53.820 1.00 16.04 ? 522 LEU A CB 1 ATOM 3994 C CG . LEU A 1 522 ? 7.296 31.726 53.973 1.00 16.57 ? 522 LEU A CG 1 ATOM 3995 C CD1 . LEU A 1 522 ? 7.945 33.118 54.052 1.00 18.55 ? 522 LEU A CD1 1 ATOM 3996 C CD2 . LEU A 1 522 ? 7.641 30.883 55.229 1.00 18.66 ? 522 LEU A CD2 1 ATOM 3997 N N . ILE A 1 523 ? 6.507 32.837 50.545 1.00 15.91 ? 523 ILE A N 1 ATOM 3998 C CA . ILE A 1 523 ? 7.188 32.444 49.301 1.00 16.15 ? 523 ILE A CA 1 ATOM 3999 C C . ILE A 1 523 ? 8.672 32.277 49.613 1.00 16.88 ? 523 ILE A C 1 ATOM 4000 O O . ILE A 1 523 ? 9.341 33.236 50.020 1.00 17.35 ? 523 ILE A O 1 ATOM 4001 C CB . ILE A 1 523 ? 6.995 33.537 48.206 1.00 16.77 ? 523 ILE A CB 1 ATOM 4002 C CG1 . ILE A 1 523 ? 5.508 33.747 47.888 1.00 17.92 ? 523 ILE A CG1 1 ATOM 4003 C CG2 . ILE A 1 523 ? 7.827 33.199 46.961 1.00 15.94 ? 523 ILE A CG2 1 ATOM 4004 C CD1 . ILE A 1 523 ? 4.851 32.574 47.082 1.00 19.58 ? 523 ILE A CD1 1 ATOM 4005 N N . SER A 1 524 ? 9.185 31.057 49.477 1.00 16.98 ? 524 SER A N 1 ATOM 4006 C CA . SER A 1 524 ? 10.602 30.823 49.793 1.00 17.35 ? 524 SER A CA 1 ATOM 4007 C C . SER A 1 524 ? 11.116 29.605 49.038 1.00 17.23 ? 524 SER A C 1 ATOM 4008 O O . SER A 1 524 ? 10.332 28.789 48.563 1.00 17.25 ? 524 SER A O 1 ATOM 4009 C CB . SER A 1 524 ? 10.773 30.617 51.309 1.00 17.22 ? 524 SER A CB 1 ATOM 4010 O OG . SER A 1 524 ? 10.236 29.371 51.713 1.00 17.59 ? 524 SER A OG 1 ATOM 4011 N N . GLY A 1 525 ? 12.433 29.467 48.951 1.00 17.90 ? 525 GLY A N 1 ATOM 4012 C CA . GLY A 1 525 ? 13.024 28.302 48.291 1.00 17.70 ? 525 GLY A CA 1 ATOM 4013 C C . GLY A 1 525 ? 13.302 27.162 49.272 1.00 18.15 ? 525 GLY A C 1 ATOM 4014 O O . GLY A 1 525 ? 13.870 26.134 48.898 1.00 18.61 ? 525 GLY A O 1 ATOM 4015 N N . ARG A 1 526 ? 12.898 27.357 50.534 1.00 18.20 ? 526 ARG A N 1 ATOM 4016 C CA . ARG A 1 526 ? 13.412 26.538 51.636 1.00 17.80 ? 526 ARG A CA 1 ATOM 4017 C C . ARG A 1 526 ? 12.755 26.983 52.947 1.00 17.94 ? 526 ARG A C 1 ATOM 4018 O O . ARG A 1 526 ? 12.216 28.097 53.036 1.00 17.93 ? 526 ARG A O 1 ATOM 4019 C CB . ARG A 1 526 ? 14.921 26.761 51.786 1.00 17.70 ? 526 ARG A CB 1 ATOM 4020 C CG . ARG A 1 526 ? 15.297 28.212 51.946 1.00 18.89 ? 526 ARG A CG 1 ATOM 4021 C CD . ARG A 1 526 ? 16.818 28.421 51.935 1.00 19.03 ? 526 ARG A CD 1 ATOM 4022 N NE . ARG A 1 526 ? 17.147 29.783 51.547 1.00 19.94 ? 526 ARG A NE 1 ATOM 4023 C CZ . ARG A 1 526 ? 18.358 30.177 51.142 1.00 19.57 ? 526 ARG A CZ 1 ATOM 4024 N NH1 . ARG A 1 526 ? 19.362 29.308 51.083 1.00 19.59 ? 526 ARG A NH1 1 ATOM 4025 N NH2 . ARG A 1 526 ? 18.554 31.430 50.769 1.00 20.07 ? 526 ARG A NH2 1 ATOM 4026 N N . PRO A 1 527 ? 12.848 26.137 53.982 1.00 18.56 ? 527 PRO A N 1 ATOM 4027 C CA . PRO A 1 527 ? 12.475 26.632 55.305 1.00 19.02 ? 527 PRO A CA 1 ATOM 4028 C C . PRO A 1 527 ? 13.313 27.857 55.675 1.00 18.79 ? 527 PRO A C 1 ATOM 4029 O O . PRO A 1 527 ? 14.529 27.923 55.366 1.00 19.67 ? 527 PRO A O 1 ATOM 4030 C CB . PRO A 1 527 ? 12.788 25.460 56.253 1.00 19.03 ? 527 PRO A CB 1 ATOM 4031 C CG . PRO A 1 527 ? 12.948 24.284 55.416 1.00 21.49 ? 527 PRO A CG 1 ATOM 4032 C CD . PRO A 1 527 ? 13.281 24.733 54.000 1.00 18.53 ? 527 PRO A CD 1 ATOM 4033 N N . VAL A 1 528 ? 12.653 28.826 56.304 1.00 18.69 ? 528 VAL A N 1 ATOM 4034 C CA . VAL A 1 528 ? 13.276 30.049 56.804 1.00 18.98 ? 528 VAL A CA 1 ATOM 4035 C C . VAL A 1 528 ? 12.777 30.275 58.232 1.00 19.31 ? 528 VAL A C 1 ATOM 4036 O O . VAL A 1 528 ? 11.777 29.662 58.634 1.00 19.64 ? 528 VAL A O 1 ATOM 4037 C CB . VAL A 1 528 ? 12.916 31.269 55.926 1.00 18.77 ? 528 VAL A CB 1 ATOM 4038 C CG1 . VAL A 1 528 ? 13.618 31.129 54.535 1.00 19.15 ? 528 VAL A CG1 1 ATOM 4039 C CG2 . VAL A 1 528 ? 11.365 31.430 55.802 1.00 19.55 ? 528 VAL A CG2 1 ATOM 4040 N N . VAL A 1 529 ? 13.442 31.152 58.984 1.00 20.25 ? 529 VAL A N 1 ATOM 4041 C CA . VAL A 1 529 ? 13.011 31.431 60.372 1.00 20.30 ? 529 VAL A CA 1 ATOM 4042 C C . VAL A 1 529 ? 11.537 31.852 60.346 1.00 20.23 ? 529 VAL A C 1 ATOM 4043 O O . VAL A 1 529 ? 11.198 32.850 59.717 1.00 20.60 ? 529 VAL A O 1 ATOM 4044 C CB . VAL A 1 529 ? 13.879 32.502 61.058 1.00 20.68 ? 529 VAL A CB 1 ATOM 4045 C CG1 . VAL A 1 529 ? 13.306 32.847 62.453 1.00 21.88 ? 529 VAL A CG1 1 ATOM 4046 C CG2 . VAL A 1 529 ? 15.324 32.019 61.179 1.00 21.67 ? 529 VAL A CG2 1 ATOM 4047 N N . VAL A 1 530 ? 10.668 31.090 61.016 1.00 19.72 ? 530 VAL A N 1 ATOM 4048 C CA . VAL A 1 530 ? 9.220 31.302 60.819 1.00 20.28 ? 530 VAL A CA 1 ATOM 4049 C C . VAL A 1 530 ? 8.401 31.531 62.106 1.00 20.98 ? 530 VAL A C 1 ATOM 4050 O O . VAL A 1 530 ? 7.230 31.917 62.025 1.00 20.66 ? 530 VAL A O 1 ATOM 4051 C CB . VAL A 1 530 ? 8.630 30.140 59.962 1.00 20.61 ? 530 VAL A CB 1 ATOM 4052 C CG1 . VAL A 1 530 ? 8.431 28.887 60.804 1.00 20.45 ? 530 VAL A CG1 1 ATOM 4053 C CG2 . VAL A 1 530 ? 7.322 30.553 59.250 1.00 20.18 ? 530 VAL A CG2 1 ATOM 4054 N N . GLN A 1 531 ? 8.998 31.312 63.282 1.00 20.89 ? 531 GLN A N 1 ATOM 4055 C CA . GLN A 1 531 ? 8.223 31.537 64.525 1.00 20.83 ? 531 GLN A CA 1 ATOM 4056 C C . GLN A 1 531 ? 7.537 32.918 64.618 1.00 20.67 ? 531 GLN A C 1 ATOM 4057 O O . GLN A 1 531 ? 6.350 32.977 64.966 1.00 20.58 ? 531 GLN A O 1 ATOM 4058 C CB . GLN A 1 531 ? 9.027 31.212 65.805 1.00 20.51 ? 531 GLN A CB 1 ATOM 4059 C CG . GLN A 1 531 ? 9.474 29.746 65.905 1.00 21.60 ? 531 GLN A CG 1 ATOM 4060 C CD . GLN A 1 531 ? 10.880 29.528 65.354 1.00 23.21 ? 531 GLN A CD 1 ATOM 4061 O OE1 . GLN A 1 531 ? 11.295 30.177 64.379 1.00 24.58 ? 531 GLN A OE1 1 ATOM 4062 N NE2 . GLN A 1 531 ? 11.626 28.624 65.984 1.00 24.18 ? 531 GLN A NE2 1 ATOM 4063 N N . PRO A 1 532 ? 8.263 34.030 64.330 1.00 21.30 ? 532 PRO A N 1 ATOM 4064 C CA . PRO A 1 532 ? 7.603 35.343 64.396 1.00 21.09 ? 532 PRO A CA 1 ATOM 4065 C C . PRO A 1 532 ? 6.440 35.476 63.410 1.00 20.84 ? 532 PRO A C 1 ATOM 4066 O O . PRO A 1 532 ? 5.402 36.039 63.759 1.00 21.19 ? 532 PRO A O 1 ATOM 4067 C CB . PRO A 1 532 ? 8.720 36.319 64.044 1.00 21.49 ? 532 PRO A CB 1 ATOM 4068 C CG . PRO A 1 532 ? 9.994 35.587 64.438 1.00 22.71 ? 532 PRO A CG 1 ATOM 4069 C CD . PRO A 1 532 ? 9.713 34.170 64.053 1.00 21.74 ? 532 PRO A CD 1 ATOM 4070 N N . LEU A 1 533 ? 6.604 34.938 62.202 1.00 20.01 ? 533 LEU A N 1 ATOM 4071 C CA . LEU A 1 533 ? 5.505 34.962 61.232 1.00 19.85 ? 533 LEU A CA 1 ATOM 4072 C C . LEU A 1 533 ? 4.306 34.138 61.735 1.00 19.86 ? 533 LEU A C 1 ATOM 4073 O O . LEU A 1 533 ? 3.155 34.576 61.652 1.00 20.54 ? 533 LEU A O 1 ATOM 4074 C CB . LEU A 1 533 ? 5.986 34.438 59.873 1.00 19.77 ? 533 LEU A CB 1 ATOM 4075 C CG . LEU A 1 533 ? 6.873 35.411 59.093 1.00 20.29 ? 533 LEU A CG 1 ATOM 4076 C CD1 . LEU A 1 533 ? 7.577 34.645 57.965 1.00 20.34 ? 533 LEU A CD1 1 ATOM 4077 C CD2 . LEU A 1 533 ? 6.076 36.592 58.525 1.00 21.09 ? 533 LEU A CD2 1 ATOM 4078 N N . LEU A 1 534 ? 4.576 32.938 62.236 1.00 20.16 ? 534 LEU A N 1 ATOM 4079 C CA . LEU A 1 534 ? 3.552 32.097 62.834 1.00 21.06 ? 534 LEU A CA 1 ATOM 4080 C C . LEU A 1 534 ? 2.814 32.823 63.964 1.00 21.61 ? 534 LEU A C 1 ATOM 4081 O O . LEU A 1 534 ? 1.570 32.807 64.011 1.00 22.19 ? 534 LEU A O 1 ATOM 4082 C CB . LEU A 1 534 ? 4.204 30.843 63.392 1.00 21.52 ? 534 LEU A CB 1 ATOM 4083 C CG . LEU A 1 534 ? 4.053 29.441 62.802 1.00 25.29 ? 534 LEU A CG 1 ATOM 4084 C CD1 . LEU A 1 534 ? 3.337 29.259 61.450 1.00 23.69 ? 534 LEU A CD1 1 ATOM 4085 C CD2 . LEU A 1 534 ? 5.344 28.638 62.905 1.00 23.68 ? 534 LEU A CD2 1 ATOM 4086 N N . ALA A 1 535 ? 3.575 33.476 64.852 1.00 21.97 ? 535 ALA A N 1 ATOM 4087 C CA . ALA A 1 535 ? 2.974 34.099 66.043 1.00 22.68 ? 535 ALA A CA 1 ATOM 4088 C C . ALA A 1 535 ? 1.937 35.173 65.669 1.00 22.67 ? 535 ALA A C 1 ATOM 4089 O O . ALA A 1 535 ? 0.895 35.311 66.335 1.00 22.87 ? 535 ALA A O 1 ATOM 4090 C CB . ALA A 1 535 ? 4.057 34.675 66.956 1.00 22.11 ? 535 ALA A CB 1 ATOM 4091 N N . ALA A 1 536 ? 2.217 35.900 64.586 1.00 21.88 ? 536 ALA A N 1 ATOM 4092 C CA . ALA A 1 536 ? 1.360 36.985 64.115 1.00 22.08 ? 536 ALA A CA 1 ATOM 4093 C C . ALA A 1 536 ? 0.111 36.465 63.373 1.00 22.10 ? 536 ALA A C 1 ATOM 4094 O O . ALA A 1 536 ? -0.949 37.086 63.425 1.00 22.67 ? 536 ALA A O 1 ATOM 4095 C CB . ALA A 1 536 ? 2.176 37.920 63.205 1.00 22.00 ? 536 ALA A CB 1 ATOM 4096 N N . SER A 1 537 ? 0.240 35.318 62.708 1.00 20.78 ? 537 SER A N 1 ATOM 4097 C CA . SER A 1 537 ? -0.736 34.909 61.690 1.00 20.13 ? 537 SER A CA 1 ATOM 4098 C C . SER A 1 537 ? -1.848 33.998 62.200 1.00 20.31 ? 537 SER A C 1 ATOM 4099 O O . SER A 1 537 ? -1.598 33.104 63.012 1.00 20.61 ? 537 SER A O 1 ATOM 4100 C CB . SER A 1 537 ? -0.005 34.166 60.560 1.00 20.12 ? 537 SER A CB 1 ATOM 4101 O OG . SER A 1 537 ? 1.002 34.971 59.967 1.00 21.17 ? 537 SER A OG 1 ATOM 4102 N N . ASP A 1 538 ? -3.061 34.173 61.671 1.00 19.40 ? 538 ASP A N 1 ATOM 4103 C CA . ASP A 1 538 ? -4.118 33.202 61.921 1.00 19.65 ? 538 ASP A CA 1 ATOM 4104 C C . ASP A 1 538 ? -3.871 31.926 61.155 1.00 19.33 ? 538 ASP A C 1 ATOM 4105 O O . ASP A 1 538 ? -3.975 30.850 61.719 1.00 20.10 ? 538 ASP A O 1 ATOM 4106 C CB . ASP A 1 538 ? -5.478 33.773 61.556 1.00 19.46 ? 538 ASP A CB 1 ATOM 4107 C CG . ASP A 1 538 ? -5.838 34.945 62.419 1.00 21.26 ? 538 ASP A CG 1 ATOM 4108 O OD1 . ASP A 1 538 ? -5.466 36.073 62.036 1.00 21.53 ? 538 ASP A OD1 1 ATOM 4109 O OD2 . ASP A 1 538 ? -6.451 34.720 63.499 1.00 23.80 ? 538 ASP A OD2 1 ATOM 4110 N N . ALA A 1 539 ? -3.532 32.053 59.867 1.00 19.03 ? 539 ALA A N 1 ATOM 4111 C CA . ALA A 1 539 ? -3.134 30.886 59.075 1.00 17.32 ? 539 ALA A CA 1 ATOM 4112 C C . ALA A 1 539 ? -1.828 31.218 58.364 1.00 17.45 ? 539 ALA A C 1 ATOM 4113 O O . ALA A 1 539 ? -1.543 32.395 58.095 1.00 17.19 ? 539 ALA A O 1 ATOM 4114 C CB . ALA A 1 539 ? -4.216 30.512 58.056 1.00 18.20 ? 539 ALA A CB 1 ATOM 4115 N N . LEU A 1 540 ? -1.034 30.183 58.089 1.00 16.93 ? 540 LEU A N 1 ATOM 4116 C CA . LEU A 1 540 ? 0.225 30.366 57.359 1.00 16.79 ? 540 LEU A CA 1 ATOM 4117 C C . LEU A 1 540 ? 0.456 29.194 56.425 1.00 16.82 ? 540 LEU A C 1 ATOM 4118 O O . LEU A 1 540 ? 0.343 28.025 56.828 1.00 17.06 ? 540 LEU A O 1 ATOM 4119 C CB . LEU A 1 540 ? 1.428 30.568 58.325 1.00 17.50 ? 540 LEU A CB 1 ATOM 4120 C CG . LEU A 1 540 ? 2.721 31.035 57.635 1.00 18.82 ? 540 LEU A CG 1 ATOM 4121 C CD1 . LEU A 1 540 ? 3.491 32.036 58.510 1.00 20.65 ? 540 LEU A CD1 1 ATOM 4122 C CD2 . LEU A 1 540 ? 3.598 29.845 57.237 1.00 20.81 ? 540 LEU A CD2 1 ATOM 4123 N N . VAL A 1 541 ? 0.781 29.534 55.174 1.00 16.32 ? 541 VAL A N 1 ATOM 4124 C CA . VAL A 1 541 ? 0.994 28.562 54.113 1.00 16.77 ? 541 VAL A CA 1 ATOM 4125 C C . VAL A 1 541 ? 2.426 28.712 53.588 1.00 16.92 ? 541 VAL A C 1 ATOM 4126 O O . VAL A 1 541 ? 2.853 29.833 53.247 1.00 16.62 ? 541 VAL A O 1 ATOM 4127 C CB . VAL A 1 541 ? 0.011 28.828 52.933 1.00 17.21 ? 541 VAL A CB 1 ATOM 4128 C CG1 . VAL A 1 541 ? 0.354 27.930 51.755 1.00 17.63 ? 541 VAL A CG1 1 ATOM 4129 C CG2 . VAL A 1 541 ? -1.466 28.634 53.361 1.00 18.43 ? 541 VAL A CG2 1 ATOM 4130 N N . ALA A 1 542 ? 3.158 27.594 53.531 1.00 16.29 ? 542 ALA A N 1 ATOM 4131 C CA . ALA A 1 542 ? 4.469 27.572 52.856 1.00 16.09 ? 542 ALA A CA 1 ATOM 4132 C C . ALA A 1 542 ? 4.160 27.266 51.393 1.00 15.88 ? 542 ALA A C 1 ATOM 4133 O O . ALA A 1 542 ? 3.750 26.146 51.062 1.00 17.01 ? 542 ALA A O 1 ATOM 4134 C CB . ALA A 1 542 ? 5.380 26.490 53.455 1.00 16.34 ? 542 ALA A CB 1 ATOM 4135 N N . ALA A 1 543 ? 4.321 28.270 50.525 1.00 15.52 ? 543 ALA A N 1 ATOM 4136 C CA . ALA A 1 543 ? 3.988 28.106 49.106 1.00 15.45 ? 543 ALA A CA 1 ATOM 4137 C C . ALA A 1 543 ? 5.229 27.843 48.236 1.00 15.37 ? 543 ALA A C 1 ATOM 4138 O O . ALA A 1 543 ? 5.089 27.646 47.019 1.00 16.07 ? 543 ALA A O 1 ATOM 4139 C CB . ALA A 1 543 ? 3.255 29.362 48.603 1.00 15.55 ? 543 ALA A CB 1 ATOM 4140 N N . TRP A 1 544 ? 6.422 27.836 48.851 1.00 15.53 ? 544 TRP A N 1 ATOM 4141 C CA . TRP A 1 544 ? 7.686 27.581 48.132 1.00 15.22 ? 544 TRP A CA 1 ATOM 4142 C C . TRP A 1 544 ? 7.838 28.618 46.996 1.00 15.26 ? 544 TRP A C 1 ATOM 4143 O O . TRP A 1 544 ? 7.626 29.809 47.227 1.00 15.46 ? 544 TRP A O 1 ATOM 4144 C CB . TRP A 1 544 ? 7.773 26.133 47.630 1.00 16.25 ? 544 TRP A CB 1 ATOM 4145 C CG . TRP A 1 544 ? 7.347 25.152 48.685 1.00 15.00 ? 544 TRP A CG 1 ATOM 4146 C CD1 . TRP A 1 544 ? 6.205 24.417 48.692 1.00 17.68 ? 544 TRP A CD1 1 ATOM 4147 C CD2 . TRP A 1 544 ? 8.035 24.850 49.914 1.00 16.86 ? 544 TRP A CD2 1 ATOM 4148 N NE1 . TRP A 1 544 ? 6.126 23.655 49.854 1.00 16.73 ? 544 TRP A NE1 1 ATOM 4149 C CE2 . TRP A 1 544 ? 7.238 23.904 50.618 1.00 17.07 ? 544 TRP A CE2 1 ATOM 4150 C CE3 . TRP A 1 544 ? 9.235 25.291 50.489 1.00 18.17 ? 544 TRP A CE3 1 ATOM 4151 C CZ2 . TRP A 1 544 ? 7.612 23.375 51.869 1.00 17.74 ? 544 TRP A CZ2 1 ATOM 4152 C CZ3 . TRP A 1 544 ? 9.613 24.777 51.761 1.00 18.49 ? 544 TRP A CZ3 1 ATOM 4153 C CH2 . TRP A 1 544 ? 8.801 23.815 52.422 1.00 17.77 ? 544 TRP A CH2 1 ATOM 4154 N N . LEU A 1 545 ? 8.205 28.166 45.794 1.00 15.17 ? 545 LEU A N 1 ATOM 4155 C CA . LEU A 1 545 ? 8.354 29.078 44.635 1.00 15.18 ? 545 LEU A CA 1 ATOM 4156 C C . LEU A 1 545 ? 7.393 28.554 43.564 1.00 15.45 ? 545 LEU A C 1 ATOM 4157 O O . LEU A 1 545 ? 7.787 27.743 42.700 1.00 15.77 ? 545 LEU A O 1 ATOM 4158 C CB . LEU A 1 545 ? 9.808 29.099 44.145 1.00 16.04 ? 545 LEU A CB 1 ATOM 4159 C CG . LEU A 1 545 ? 10.807 29.607 45.198 1.00 15.99 ? 545 LEU A CG 1 ATOM 4160 C CD1 . LEU A 1 545 ? 12.258 29.383 44.734 1.00 17.03 ? 545 LEU A CD1 1 ATOM 4161 C CD2 . LEU A 1 545 ? 10.558 31.080 45.493 1.00 16.56 ? 545 LEU A CD2 1 ATOM 4162 N N . PRO A 1 546 ? 6.117 28.963 43.664 1.00 15.39 ? 546 PRO A N 1 ATOM 4163 C CA . PRO A 1 546 ? 5.073 28.252 42.902 1.00 15.39 ? 546 PRO A CA 1 ATOM 4164 C C . PRO A 1 546 ? 5.019 28.458 41.392 1.00 15.40 ? 546 PRO A C 1 ATOM 4165 O O . PRO A 1 546 ? 4.287 27.714 40.711 1.00 15.52 ? 546 PRO A O 1 ATOM 4166 C CB . PRO A 1 546 ? 3.762 28.705 43.593 1.00 15.82 ? 546 PRO A CB 1 ATOM 4167 C CG . PRO A 1 546 ? 4.093 30.095 44.123 1.00 16.22 ? 546 PRO A CG 1 ATOM 4168 C CD . PRO A 1 546 ? 5.555 30.010 44.554 1.00 15.15 ? 546 PRO A CD 1 ATOM 4169 N N . GLY A 1 547 ? 5.782 29.410 40.859 1.00 14.95 ? 547 GLY A N 1 ATOM 4170 C CA . GLY A 1 547 ? 5.838 29.594 39.384 1.00 15.16 ? 547 GLY A CA 1 ATOM 4171 C C . GLY A 1 547 ? 4.845 30.616 38.858 1.00 15.63 ? 547 GLY A C 1 ATOM 4172 O O . GLY A 1 547 ? 4.336 31.479 39.597 1.00 16.10 ? 547 GLY A O 1 ATOM 4173 N N . SER A 1 548 ? 4.554 30.515 37.567 1.00 15.79 ? 548 SER A N 1 ATOM 4174 C CA . SER A 1 548 ? 3.762 31.572 36.912 1.00 15.90 ? 548 SER A CA 1 ATOM 4175 C C . SER A 1 548 ? 2.258 31.527 37.234 1.00 16.31 ? 548 SER A C 1 ATOM 4176 O O . SER A 1 548 ? 1.562 32.536 37.025 1.00 17.10 ? 548 SER A O 1 ATOM 4177 C CB . SER A 1 548 ? 3.977 31.543 35.391 1.00 15.79 ? 548 SER A CB 1 ATOM 4178 O OG . SER A 1 548 ? 3.642 30.277 34.846 1.00 16.64 ? 548 SER A OG 1 ATOM 4179 N N . GLU A 1 549 ? 1.761 30.388 37.724 1.00 16.39 ? 549 GLU A N 1 ATOM 4180 C CA . GLU A 1 549 ? 0.295 30.189 37.859 1.00 17.14 ? 549 GLU A CA 1 ATOM 4181 C C . GLU A 1 549 ? -0.179 30.409 39.305 1.00 17.21 ? 549 GLU A C 1 ATOM 4182 O O . GLU A 1 549 ? -0.439 29.456 40.058 1.00 17.70 ? 549 GLU A O 1 ATOM 4183 C CB . GLU A 1 549 ? -0.134 28.824 37.303 1.00 17.65 ? 549 GLU A CB 1 ATOM 4184 C CG . GLU A 1 549 ? 0.375 28.595 35.856 1.00 17.82 ? 549 GLU A CG 1 ATOM 4185 C CD . GLU A 1 549 ? 0.049 29.778 34.930 1.00 20.55 ? 549 GLU A CD 1 ATOM 4186 O OE1 . GLU A 1 549 ? -1.116 30.274 34.963 1.00 19.35 ? 549 GLU A OE1 1 ATOM 4187 O OE2 . GLU A 1 549 ? 0.953 30.206 34.174 1.00 19.93 ? 549 GLU A OE2 1 ATOM 4188 N N . GLY A 1 550 ? -0.301 31.689 39.659 1.00 17.35 ? 550 GLY A N 1 ATOM 4189 C CA . GLY A 1 550 ? -0.688 32.103 41.016 1.00 16.99 ? 550 GLY A CA 1 ATOM 4190 C C . GLY A 1 550 ? -2.073 31.637 41.444 1.00 18.04 ? 550 GLY A C 1 ATOM 4191 O O . GLY A 1 550 ? -2.360 31.561 42.645 1.00 18.01 ? 550 GLY A O 1 ATOM 4192 N N . GLN A 1 551 ? -2.939 31.302 40.483 1.00 18.17 ? 551 GLN A N 1 ATOM 4193 C CA . GLN A 1 551 ? -4.241 30.719 40.833 1.00 19.12 ? 551 GLN A CA 1 ATOM 4194 C C . GLN A 1 551 ? -4.152 29.388 41.594 1.00 18.89 ? 551 GLN A C 1 ATOM 4195 O O . GLN A 1 551 ? -5.115 28.993 42.266 1.00 19.02 ? 551 GLN A O 1 ATOM 4196 C CB . GLN A 1 551 ? -5.147 30.621 39.599 1.00 19.40 ? 551 GLN A CB 1 ATOM 4197 C CG . GLN A 1 551 ? -5.549 32.020 39.139 1.00 21.68 ? 551 GLN A CG 1 ATOM 4198 C CD . GLN A 1 551 ? -6.182 32.036 37.776 1.00 24.64 ? 551 GLN A CD 1 ATOM 4199 O OE1 . GLN A 1 551 ? -7.393 32.296 37.637 1.00 28.56 ? 551 GLN A OE1 1 ATOM 4200 N NE2 . GLN A 1 551 ? -5.375 31.758 36.748 1.00 24.47 ? 551 GLN A NE2 1 ATOM 4201 N N . GLY A 1 552 ? -3.005 28.698 41.504 1.00 18.31 ? 552 GLY A N 1 ATOM 4202 C CA . GLY A 1 552 ? -2.804 27.498 42.313 1.00 18.07 ? 552 GLY A CA 1 ATOM 4203 C C . GLY A 1 552 ? -2.895 27.823 43.802 1.00 18.00 ? 552 GLY A C 1 ATOM 4204 O O . GLY A 1 552 ? -3.381 27.018 44.610 1.00 18.51 ? 552 GLY A O 1 ATOM 4205 N N . VAL A 1 553 ? -2.420 29.010 44.159 1.00 17.42 ? 553 VAL A N 1 ATOM 4206 C CA . VAL A 1 553 ? -2.451 29.450 45.561 1.00 17.29 ? 553 VAL A CA 1 ATOM 4207 C C . VAL A 1 553 ? -3.889 29.698 46.013 1.00 18.02 ? 553 VAL A C 1 ATOM 4208 O O . VAL A 1 553 ? -4.331 29.196 47.059 1.00 18.33 ? 553 VAL A O 1 ATOM 4209 C CB . VAL A 1 553 ? -1.602 30.707 45.780 1.00 16.59 ? 553 VAL A CB 1 ATOM 4210 C CG1 . VAL A 1 553 ? -1.735 31.189 47.251 1.00 17.42 ? 553 VAL A CG1 1 ATOM 4211 C CG2 . VAL A 1 553 ? -0.116 30.429 45.402 1.00 16.84 ? 553 VAL A CG2 1 ATOM 4212 N N . THR A 1 554 ? -4.626 30.455 45.212 1.00 18.51 ? 554 THR A N 1 ATOM 4213 C CA . THR A 1 554 ? -6.018 30.792 45.569 1.00 19.04 ? 554 THR A CA 1 ATOM 4214 C C . THR A 1 554 ? -6.981 29.606 45.453 1.00 19.48 ? 554 THR A C 1 ATOM 4215 O O . THR A 1 554 ? -7.995 29.564 46.166 1.00 19.61 ? 554 THR A O 1 ATOM 4216 C CB . THR A 1 554 ? -6.535 31.991 44.758 1.00 19.43 ? 554 THR A CB 1 ATOM 4217 O OG1 . THR A 1 554 ? -6.319 31.748 43.363 1.00 19.43 ? 554 THR A OG1 1 ATOM 4218 C CG2 . THR A 1 554 ? -5.795 33.271 45.160 1.00 19.74 ? 554 THR A CG2 1 ATOM 4219 N N . ASP A 1 555 ? -6.648 28.622 44.598 1.00 18.94 ? 555 ASP A N 1 ATOM 4220 C CA . ASP A 1 555 ? -7.420 27.370 44.518 1.00 19.90 ? 555 ASP A CA 1 ATOM 4221 C C . ASP A 1 555 ? -7.537 26.700 45.889 1.00 20.20 ? 555 ASP A C 1 ATOM 4222 O O . ASP A 1 555 ? -8.571 26.123 46.210 1.00 21.14 ? 555 ASP A O 1 ATOM 4223 C CB . ASP A 1 555 ? -6.809 26.389 43.514 1.00 19.94 ? 555 ASP A CB 1 ATOM 4224 C CG . ASP A 1 555 ? -7.098 26.771 42.062 1.00 19.95 ? 555 ASP A CG 1 ATOM 4225 O OD1 . ASP A 1 555 ? -7.922 27.682 41.788 1.00 20.13 ? 555 ASP A OD1 1 ATOM 4226 O OD2 . ASP A 1 555 ? -6.468 26.158 41.180 1.00 20.73 ? 555 ASP A OD2 1 ATOM 4227 N N . ALA A 1 556 ? -6.477 26.800 46.699 1.00 19.15 ? 556 ALA A N 1 ATOM 4228 C CA . ALA A 1 556 ? -6.499 26.245 48.054 1.00 19.14 ? 556 ALA A CA 1 ATOM 4229 C C . ALA A 1 556 ? -7.019 27.274 49.085 1.00 18.89 ? 556 ALA A C 1 ATOM 4230 O O . ALA A 1 556 ? -7.798 26.913 49.988 1.00 19.17 ? 556 ALA A O 1 ATOM 4231 C CB . ALA A 1 556 ? -5.114 25.705 48.446 1.00 19.07 ? 556 ALA A CB 1 ATOM 4232 N N . LEU A 1 557 ? -6.623 28.539 48.958 1.00 18.42 ? 557 LEU A N 1 ATOM 4233 C CA . LEU A 1 557 ? -7.061 29.538 49.954 1.00 18.04 ? 557 LEU A CA 1 ATOM 4234 C C . LEU A 1 557 ? -8.587 29.627 50.043 1.00 18.85 ? 557 LEU A C 1 ATOM 4235 O O . LEU A 1 557 ? -9.135 29.773 51.146 1.00 18.61 ? 557 LEU A O 1 ATOM 4236 C CB . LEU A 1 557 ? -6.490 30.921 49.650 1.00 17.83 ? 557 LEU A CB 1 ATOM 4237 C CG . LEU A 1 557 ? -4.983 31.094 49.818 1.00 18.29 ? 557 LEU A CG 1 ATOM 4238 C CD1 . LEU A 1 557 ? -4.598 32.511 49.400 1.00 20.49 ? 557 LEU A CD1 1 ATOM 4239 C CD2 . LEU A 1 557 ? -4.553 30.823 51.269 1.00 19.69 ? 557 LEU A CD2 1 ATOM 4240 N N . PHE A 1 558 ? -9.250 29.547 48.886 1.00 19.05 ? 558 PHE A N 1 ATOM 4241 C CA . PHE A 1 558 ? -10.710 29.685 48.802 1.00 19.91 ? 558 PHE A CA 1 ATOM 4242 C C . PHE A 1 558 ? -11.482 28.358 48.786 1.00 20.72 ? 558 PHE A C 1 ATOM 4243 O O . PHE A 1 558 ? -12.711 28.339 48.581 1.00 21.43 ? 558 PHE A O 1 ATOM 4244 C CB . PHE A 1 558 ? -11.089 30.583 47.614 1.00 19.56 ? 558 PHE A CB 1 ATOM 4245 C CG . PHE A 1 558 ? -10.624 32.006 47.767 1.00 19.98 ? 558 PHE A CG 1 ATOM 4246 C CD1 . PHE A 1 558 ? -11.240 32.872 48.676 1.00 19.26 ? 558 PHE A CD1 1 ATOM 4247 C CD2 . PHE A 1 558 ? -9.562 32.475 47.019 1.00 21.94 ? 558 PHE A CD2 1 ATOM 4248 C CE1 . PHE A 1 558 ? -10.805 34.185 48.820 1.00 20.70 ? 558 PHE A CE1 1 ATOM 4249 C CE2 . PHE A 1 558 ? -9.089 33.783 47.163 1.00 21.99 ? 558 PHE A CE2 1 ATOM 4250 C CZ . PHE A 1 558 ? -9.717 34.652 48.067 1.00 21.54 ? 558 PHE A CZ 1 ATOM 4251 N N . GLY A 1 559 ? -10.778 27.251 48.995 1.00 21.04 ? 559 GLY A N 1 ATOM 4252 C CA . GLY A 1 559 ? -11.431 25.961 49.194 1.00 22.66 ? 559 GLY A CA 1 ATOM 4253 C C . GLY A 1 559 ? -11.930 25.245 47.949 1.00 23.27 ? 559 GLY A C 1 ATOM 4254 O O . GLY A 1 559 ? -12.679 24.274 48.066 1.00 24.27 ? 559 GLY A O 1 ATOM 4255 N N . ASP A 1 560 ? -11.515 25.680 46.756 1.00 23.94 ? 560 ASP A N 1 ATOM 4256 C CA . ASP A 1 560 ? -11.823 24.878 45.555 1.00 24.73 ? 560 ASP A CA 1 ATOM 4257 C C . ASP A 1 560 ? -11.221 23.482 45.656 1.00 24.35 ? 560 ASP A C 1 ATOM 4258 O O . ASP A 1 560 ? -11.822 22.494 45.191 1.00 25.01 ? 560 ASP A O 1 ATOM 4259 C CB . ASP A 1 560 ? -11.395 25.595 44.286 1.00 25.10 ? 560 ASP A CB 1 ATOM 4260 C CG . ASP A 1 560 ? -12.299 26.785 43.977 1.00 27.97 ? 560 ASP A CG 1 ATOM 4261 O OD1 . ASP A 1 560 ? -13.404 26.859 44.559 1.00 30.87 ? 560 ASP A OD1 1 ATOM 4262 O OD2 . ASP A 1 560 ? -11.909 27.640 43.170 1.00 33.92 ? 560 ASP A OD2 1 ATOM 4263 N N . PHE A 1 561 ? -10.062 23.401 46.310 1.00 23.95 ? 561 PHE A N 1 ATOM 4264 C CA . PHE A 1 561 ? -9.404 22.138 46.624 1.00 24.24 ? 561 PHE A CA 1 ATOM 4265 C C . PHE A 1 561 ? -8.909 22.201 48.046 1.00 24.14 ? 561 PHE A C 1 ATOM 4266 O O . PHE A 1 561 ? -8.656 23.290 48.565 1.00 25.15 ? 561 PHE A O 1 ATOM 4267 C CB . PHE A 1 561 ? -8.212 21.921 45.693 1.00 24.30 ? 561 PHE A CB 1 ATOM 4268 C CG . PHE A 1 561 ? -8.611 21.780 44.269 1.00 24.44 ? 561 PHE A CG 1 ATOM 4269 C CD1 . PHE A 1 561 ? -8.734 22.911 43.449 1.00 25.60 ? 561 PHE A CD1 1 ATOM 4270 C CD2 . PHE A 1 561 ? -8.940 20.527 43.758 1.00 25.39 ? 561 PHE A CD2 1 ATOM 4271 C CE1 . PHE A 1 561 ? -9.148 22.780 42.127 1.00 26.50 ? 561 PHE A CE1 1 ATOM 4272 C CE2 . PHE A 1 561 ? -9.350 20.397 42.437 1.00 25.39 ? 561 PHE A CE2 1 ATOM 4273 C CZ . PHE A 1 561 ? -9.454 21.518 41.629 1.00 26.11 ? 561 PHE A CZ 1 ATOM 4274 N N . GLY A 1 562 ? -8.779 21.044 48.686 1.00 24.07 ? 562 GLY A N 1 ATOM 4275 C CA . GLY A 1 562 ? -8.221 21.020 50.033 1.00 22.84 ? 562 GLY A CA 1 ATOM 4276 C C . GLY A 1 562 ? -6.701 21.058 49.980 1.00 22.67 ? 562 GLY A C 1 ATOM 4277 O O . GLY A 1 562 ? -6.102 20.664 48.969 1.00 23.55 ? 562 GLY A O 1 ATOM 4278 N N . PHE A 1 563 ? -6.076 21.547 51.052 1.00 21.98 ? 563 PHE A N 1 ATOM 4279 C CA . PHE A 1 563 ? -4.613 21.480 51.188 1.00 21.00 ? 563 PHE A CA 1 ATOM 4280 C C . PHE A 1 563 ? -4.194 20.025 51.382 1.00 21.37 ? 563 PHE A C 1 ATOM 4281 O O . PHE A 1 563 ? -4.816 19.297 52.172 1.00 21.13 ? 563 PHE A O 1 ATOM 4282 C CB . PHE A 1 563 ? -4.138 22.301 52.393 1.00 20.87 ? 563 PHE A CB 1 ATOM 4283 C CG . PHE A 1 563 ? -4.123 23.780 52.163 1.00 19.39 ? 563 PHE A CG 1 ATOM 4284 C CD1 . PHE A 1 563 ? -5.243 24.570 52.460 1.00 20.82 ? 563 PHE A CD1 1 ATOM 4285 C CD2 . PHE A 1 563 ? -2.966 24.408 51.676 1.00 19.48 ? 563 PHE A CD2 1 ATOM 4286 C CE1 . PHE A 1 563 ? -5.215 25.951 52.260 1.00 20.29 ? 563 PHE A CE1 1 ATOM 4287 C CE2 . PHE A 1 563 ? -2.932 25.779 51.481 1.00 19.72 ? 563 PHE A CE2 1 ATOM 4288 C CZ . PHE A 1 563 ? -4.060 26.555 51.773 1.00 20.42 ? 563 PHE A CZ 1 ATOM 4289 N N . THR A 1 564 ? -3.141 19.607 50.674 1.00 20.60 ? 564 THR A N 1 ATOM 4290 C CA . THR A 1 564 ? -2.640 18.223 50.772 1.00 20.87 ? 564 THR A CA 1 ATOM 4291 C C . THR A 1 564 ? -1.116 18.131 50.863 1.00 20.45 ? 564 THR A C 1 ATOM 4292 O O . THR A 1 564 ? -0.582 17.069 51.218 1.00 20.00 ? 564 THR A O 1 ATOM 4293 C CB . THR A 1 564 ? -3.124 17.337 49.590 1.00 21.21 ? 564 THR A CB 1 ATOM 4294 O OG1 . THR A 1 564 ? -2.755 17.954 48.359 1.00 22.76 ? 564 THR A OG1 1 ATOM 4295 C CG2 . THR A 1 564 ? -4.652 17.147 49.612 1.00 22.79 ? 564 THR A CG2 1 ATOM 4296 N N . GLY A 1 565 ? -0.414 19.228 50.557 1.00 19.43 ? 565 GLY A N 1 ATOM 4297 C CA . GLY A 1 565 ? 1.066 19.213 50.569 1.00 19.66 ? 565 GLY A CA 1 ATOM 4298 C C . GLY A 1 565 ? 1.631 18.856 51.954 1.00 19.89 ? 565 GLY A C 1 ATOM 4299 O O . GLY A 1 565 ? 1.035 19.190 52.995 1.00 20.27 ? 565 GLY A O 1 ATOM 4300 N N . ARG A 1 566 ? 2.751 18.138 51.968 1.00 19.74 ? 566 ARG A N 1 ATOM 4301 C CA . ARG A 1 566 ? 3.455 17.777 53.200 1.00 20.41 ? 566 ARG A CA 1 ATOM 4302 C C . ARG A 1 566 ? 4.929 18.185 53.092 1.00 20.18 ? 566 ARG A C 1 ATOM 4303 O O . ARG A 1 566 ? 5.521 18.068 52.005 1.00 19.62 ? 566 ARG A O 1 ATOM 4304 C CB . ARG A 1 566 ? 3.326 16.271 53.445 1.00 20.78 ? 566 ARG A CB 1 ATOM 4305 C CG . ARG A 1 566 ? 1.863 15.844 53.627 1.00 23.90 ? 566 ARG A CG 1 ATOM 4306 C CD . ARG A 1 566 ? 1.737 14.434 54.203 1.00 29.94 ? 566 ARG A CD 1 ATOM 4307 N NE . ARG A 1 566 ? 2.162 13.395 53.261 1.00 32.18 ? 566 ARG A NE 1 ATOM 4308 C CZ . ARG A 1 566 ? 1.406 12.894 52.280 1.00 38.33 ? 566 ARG A CZ 1 ATOM 4309 N NH1 . ARG A 1 566 ? 0.159 13.335 52.086 1.00 36.96 ? 566 ARG A NH1 1 ATOM 4310 N NH2 . ARG A 1 566 ? 1.893 11.937 51.485 1.00 36.04 ? 566 ARG A NH2 1 ATOM 4311 N N . LEU A 1 567 ? 5.509 18.695 54.182 1.00 19.49 ? 567 LEU A N 1 ATOM 4312 C CA . LEU A 1 567 ? 6.892 19.177 54.129 1.00 19.10 ? 567 LEU A CA 1 ATOM 4313 C C . LEU A 1 567 ? 7.829 18.111 53.553 1.00 19.51 ? 567 LEU A C 1 ATOM 4314 O O . LEU A 1 567 ? 7.840 16.970 54.035 1.00 19.73 ? 567 LEU A O 1 ATOM 4315 C CB . LEU A 1 567 ? 7.388 19.601 55.508 1.00 18.57 ? 567 LEU A CB 1 ATOM 4316 C CG . LEU A 1 567 ? 6.823 20.863 56.165 1.00 18.10 ? 567 LEU A CG 1 ATOM 4317 C CD1 . LEU A 1 567 ? 7.555 21.047 57.490 1.00 18.61 ? 567 LEU A CD1 1 ATOM 4318 C CD2 . LEU A 1 567 ? 7.002 22.120 55.270 1.00 18.65 ? 567 LEU A CD2 1 ATOM 4319 N N . PRO A 1 568 ? 8.581 18.458 52.481 1.00 19.48 ? 568 PRO A N 1 ATOM 4320 C CA . PRO A 1 568 ? 9.609 17.549 51.956 1.00 20.36 ? 568 PRO A CA 1 ATOM 4321 C C . PRO A 1 568 ? 10.972 17.772 52.628 1.00 20.84 ? 568 PRO A C 1 ATOM 4322 O O . PRO A 1 568 ? 11.991 17.174 52.207 1.00 21.91 ? 568 PRO A O 1 ATOM 4323 C CB . PRO A 1 568 ? 9.695 17.954 50.472 1.00 19.88 ? 568 PRO A CB 1 ATOM 4324 C CG . PRO A 1 568 ? 9.478 19.456 50.510 1.00 19.82 ? 568 PRO A CG 1 ATOM 4325 C CD . PRO A 1 568 ? 8.466 19.692 51.666 1.00 19.36 ? 568 PRO A CD 1 ATOM 4326 N N . ARG A 1 569 ? 10.998 18.660 53.614 1.00 21.26 ? 569 ARG A N 1 ATOM 4327 C CA . ARG A 1 569 ? 12.222 19.005 54.349 1.00 21.99 ? 569 ARG A CA 1 ATOM 4328 C C . ARG A 1 569 ? 11.841 19.223 55.799 1.00 21.95 ? 569 ARG A C 1 ATOM 4329 O O . ARG A 1 569 ? 10.700 19.564 56.098 1.00 21.71 ? 569 ARG A O 1 ATOM 4330 C CB . ARG A 1 569 ? 12.811 20.351 53.893 1.00 22.30 ? 569 ARG A CB 1 ATOM 4331 C CG . ARG A 1 569 ? 13.257 20.469 52.471 1.00 24.55 ? 569 ARG A CG 1 ATOM 4332 C CD . ARG A 1 569 ? 14.243 21.591 52.373 1.00 24.26 ? 569 ARG A CD 1 ATOM 4333 N NE . ARG A 1 569 ? 15.433 21.312 53.176 1.00 25.51 ? 569 ARG A NE 1 ATOM 4334 C CZ . ARG A 1 569 ? 16.409 20.480 52.815 1.00 24.77 ? 569 ARG A CZ 1 ATOM 4335 N NH1 . ARG A 1 569 ? 16.384 19.872 51.631 1.00 24.87 ? 569 ARG A NH1 1 ATOM 4336 N NH2 . ARG A 1 569 ? 17.429 20.281 53.636 1.00 25.98 ? 569 ARG A NH2 1 ATOM 4337 N N . THR A 1 570 ? 12.823 19.072 56.679 1.00 22.11 ? 570 THR A N 1 ATOM 4338 C CA . THR A 1 570 ? 12.676 19.466 58.070 1.00 21.90 ? 570 THR A CA 1 ATOM 4339 C C . THR A 1 570 ? 12.558 20.982 58.190 1.00 21.92 ? 570 THR A C 1 ATOM 4340 O O . THR A 1 570 ? 13.317 21.732 57.558 1.00 22.55 ? 570 THR A O 1 ATOM 4341 C CB . THR A 1 570 ? 13.908 18.975 58.872 1.00 21.90 ? 570 THR A CB 1 ATOM 4342 O OG1 . THR A 1 570 ? 13.911 17.549 58.849 1.00 22.13 ? 570 THR A OG1 1 ATOM 4343 C CG2 . THR A 1 570 ? 13.898 19.506 60.312 1.00 23.22 ? 570 THR A CG2 1 ATOM 4344 N N . TRP A 1 571 ? 11.602 21.444 58.999 1.00 21.13 ? 571 TRP A N 1 ATOM 4345 C CA . TRP A 1 571 ? 11.586 22.855 59.353 1.00 20.54 ? 571 TRP A CA 1 ATOM 4346 C C . TRP A 1 571 ? 12.263 23.025 60.708 1.00 21.60 ? 571 TRP A C 1 ATOM 4347 O O . TRP A 1 571 ? 11.716 22.604 61.746 1.00 22.03 ? 571 TRP A O 1 ATOM 4348 C CB . TRP A 1 571 ? 10.159 23.432 59.374 1.00 20.57 ? 571 TRP A CB 1 ATOM 4349 C CG . TRP A 1 571 ? 10.154 24.891 59.037 1.00 19.79 ? 571 TRP A CG 1 ATOM 4350 C CD1 . TRP A 1 571 ? 10.755 25.901 59.733 1.00 20.12 ? 571 TRP A CD1 1 ATOM 4351 C CD2 . TRP A 1 571 ? 9.559 25.496 57.880 1.00 20.64 ? 571 TRP A CD2 1 ATOM 4352 N NE1 . TRP A 1 571 ? 10.568 27.106 59.089 1.00 20.65 ? 571 TRP A NE1 1 ATOM 4353 C CE2 . TRP A 1 571 ? 9.830 26.889 57.951 1.00 20.49 ? 571 TRP A CE2 1 ATOM 4354 C CE3 . TRP A 1 571 ? 8.823 24.996 56.797 1.00 20.31 ? 571 TRP A CE3 1 ATOM 4355 C CZ2 . TRP A 1 571 ? 9.393 27.800 56.969 1.00 19.64 ? 571 TRP A CZ2 1 ATOM 4356 C CZ3 . TRP A 1 571 ? 8.384 25.904 55.805 1.00 19.72 ? 571 TRP A CZ3 1 ATOM 4357 C CH2 . TRP A 1 571 ? 8.675 27.290 55.904 1.00 19.56 ? 571 TRP A CH2 1 ATOM 4358 N N . PHE A 1 572 ? 13.429 23.654 60.685 1.00 21.88 ? 572 PHE A N 1 ATOM 4359 C CA . PHE A 1 572 ? 14.260 23.873 61.880 1.00 22.13 ? 572 PHE A CA 1 ATOM 4360 C C . PHE A 1 572 ? 13.649 24.924 62.828 1.00 22.72 ? 572 PHE A C 1 ATOM 4361 O O . PHE A 1 572 ? 12.904 25.805 62.412 1.00 21.45 ? 572 PHE A O 1 ATOM 4362 C CB . PHE A 1 572 ? 15.681 24.307 61.466 1.00 22.93 ? 572 PHE A CB 1 ATOM 4363 C CG . PHE A 1 572 ? 15.702 25.514 60.567 1.00 21.62 ? 572 PHE A CG 1 ATOM 4364 C CD1 . PHE A 1 572 ? 15.618 26.806 61.097 1.00 21.58 ? 572 PHE A CD1 1 ATOM 4365 C CD2 . PHE A 1 572 ? 15.772 25.360 59.175 1.00 21.94 ? 572 PHE A CD2 1 ATOM 4366 C CE1 . PHE A 1 572 ? 15.617 27.929 60.271 1.00 22.95 ? 572 PHE A CE1 1 ATOM 4367 C CE2 . PHE A 1 572 ? 15.744 26.470 58.339 1.00 21.15 ? 572 PHE A CE2 1 ATOM 4368 C CZ . PHE A 1 572 ? 15.684 27.748 58.872 1.00 21.64 ? 572 PHE A CZ 1 ATOM 4369 N N . LYS A 1 573 ? 13.977 24.824 64.118 1.00 23.17 ? 573 LYS A N 1 ATOM 4370 C CA . LYS A 1 573 ? 13.660 25.897 65.056 1.00 23.86 ? 573 LYS A CA 1 ATOM 4371 C C . LYS A 1 573 ? 14.653 27.051 64.933 1.00 24.33 ? 573 LYS A C 1 ATOM 4372 O O . LYS A 1 573 ? 14.290 28.213 65.081 1.00 25.19 ? 573 LYS A O 1 ATOM 4373 C CB . LYS A 1 573 ? 13.685 25.357 66.501 1.00 24.05 ? 573 LYS A CB 1 ATOM 4374 C CG . LYS A 1 573 ? 12.640 24.280 66.775 1.00 23.45 ? 573 LYS A CG 1 ATOM 4375 C CD . LYS A 1 573 ? 12.719 23.781 68.243 1.00 25.06 ? 573 LYS A CD 1 ATOM 4376 C CE . LYS A 1 573 ? 11.554 22.852 68.563 1.00 27.72 ? 573 LYS A CE 1 ATOM 4377 N NZ . LYS A 1 573 ? 11.624 22.373 70.000 1.00 29.77 ? 573 LYS A NZ 1 ATOM 4378 N N . SER A 1 574 ? 15.924 26.724 64.688 1.00 24.48 ? 574 SER A N 1 ATOM 4379 C CA . SER A 1 574 ? 16.974 27.725 64.644 1.00 25.42 ? 574 SER A CA 1 ATOM 4380 C C . SER A 1 574 ? 18.068 27.263 63.678 1.00 24.64 ? 574 SER A C 1 ATOM 4381 O O . SER A 1 574 ? 18.293 26.070 63.554 1.00 23.70 ? 574 SER A O 1 ATOM 4382 C CB . SER A 1 574 ? 17.567 27.904 66.056 1.00 26.52 ? 574 SER A CB 1 ATOM 4383 O OG . SER A 1 574 ? 18.839 28.510 65.964 1.00 31.64 ? 574 SER A OG 1 ATOM 4384 N N . VAL A 1 575 ? 18.753 28.201 63.027 1.00 24.74 ? 575 VAL A N 1 ATOM 4385 C CA . VAL A 1 575 ? 19.851 27.850 62.095 1.00 25.55 ? 575 VAL A CA 1 ATOM 4386 C C . VAL A 1 575 ? 21.046 27.221 62.829 1.00 26.24 ? 575 VAL A C 1 ATOM 4387 O O . VAL A 1 575 ? 21.823 26.477 62.223 1.00 25.37 ? 575 VAL A O 1 ATOM 4388 C CB . VAL A 1 575 ? 20.337 29.038 61.218 1.00 25.62 ? 575 VAL A CB 1 ATOM 4389 C CG1 . VAL A 1 575 ? 19.218 29.508 60.273 1.00 25.70 ? 575 VAL A CG1 1 ATOM 4390 C CG2 . VAL A 1 575 ? 20.852 30.206 62.051 1.00 26.56 ? 575 VAL A CG2 1 ATOM 4391 N N . ASP A 1 576 ? 21.158 27.488 64.140 1.00 26.97 ? 576 ASP A N 1 ATOM 4392 C CA . ASP A 1 576 ? 22.235 26.872 64.942 1.00 27.70 ? 576 ASP A CA 1 ATOM 4393 C C . ASP A 1 576 ? 22.083 25.352 65.067 1.00 27.32 ? 576 ASP A C 1 ATOM 4394 O O . ASP A 1 576 ? 23.031 24.651 65.447 1.00 28.11 ? 576 ASP A O 1 ATOM 4395 C CB A ASP A 1 576 ? 22.212 27.439 66.367 0.50 27.87 ? 576 ASP A CB 1 ATOM 4396 C CB B ASP A 1 576 ? 22.442 27.582 66.292 0.50 28.24 ? 576 ASP A CB 1 ATOM 4397 C CG A ASP A 1 576 ? 22.573 28.905 66.431 0.50 29.90 ? 576 ASP A CG 1 ATOM 4398 C CG B ASP A 1 576 ? 21.257 27.459 67.216 0.50 30.15 ? 576 ASP A CG 1 ATOM 4399 O OD1 A ASP A 1 576 ? 22.414 29.493 67.523 0.50 31.44 ? 576 ASP A OD1 1 ATOM 4400 O OD1 B ASP A 1 576 ? 20.375 26.610 66.973 0.50 32.18 ? 576 ASP A OD1 1 ATOM 4401 O OD2 A ASP A 1 576 ? 23.023 29.477 65.416 0.50 31.18 ? 576 ASP A OD2 1 ATOM 4402 O OD2 B ASP A 1 576 ? 21.215 28.212 68.214 0.50 33.10 ? 576 ASP A OD2 1 ATOM 4403 N N . GLN A 1 577 ? 20.894 24.844 64.750 1.00 25.69 ? 577 GLN A N 1 ATOM 4404 C CA . GLN A 1 577 ? 20.647 23.406 64.738 1.00 25.38 ? 577 GLN A CA 1 ATOM 4405 C C . GLN A 1 577 ? 21.227 22.720 63.500 1.00 25.25 ? 577 GLN A C 1 ATOM 4406 O O . GLN A 1 577 ? 21.366 21.490 63.455 1.00 25.58 ? 577 GLN A O 1 ATOM 4407 C CB . GLN A 1 577 ? 19.149 23.119 64.764 1.00 25.63 ? 577 GLN A CB 1 ATOM 4408 C CG . GLN A 1 577 ? 18.408 23.606 66.001 1.00 25.69 ? 577 GLN A CG 1 ATOM 4409 C CD . GLN A 1 577 ? 16.958 23.224 65.908 1.00 25.74 ? 577 GLN A CD 1 ATOM 4410 O OE1 . GLN A 1 577 ? 16.253 23.653 64.972 1.00 26.92 ? 577 GLN A OE1 1 ATOM 4411 N NE2 . GLN A 1 577 ? 16.503 22.378 66.827 1.00 27.91 ? 577 GLN A NE2 1 ATOM 4412 N N . LEU A 1 578 ? 21.511 23.506 62.469 1.00 24.88 ? 578 LEU A N 1 ATOM 4413 C CA . LEU A 1 578 ? 21.812 22.927 61.161 1.00 24.88 ? 578 LEU A CA 1 ATOM 4414 C C . LEU A 1 578 ? 23.240 22.366 61.042 1.00 25.41 ? 578 LEU A C 1 ATOM 4415 O O . LEU A 1 578 ? 24.165 22.953 61.610 1.00 26.58 ? 578 LEU A O 1 ATOM 4416 C CB . LEU A 1 578 ? 21.553 23.958 60.070 1.00 24.04 ? 578 LEU A CB 1 ATOM 4417 C CG . LEU A 1 578 ? 20.093 24.455 59.964 1.00 23.60 ? 578 LEU A CG 1 ATOM 4418 C CD1 . LEU A 1 578 ? 20.019 25.514 58.859 1.00 24.64 ? 578 LEU A CD1 1 ATOM 4419 C CD2 . LEU A 1 578 ? 19.127 23.306 59.672 1.00 23.52 ? 578 LEU A CD2 1 ATOM 4420 N N . PRO A 1 579 ? 23.425 21.270 60.265 1.00 25.90 ? 579 PRO A N 1 ATOM 4421 C CA . PRO A 1 579 ? 22.394 20.496 59.553 1.00 26.43 ? 579 PRO A CA 1 ATOM 4422 C C . PRO A 1 579 ? 21.583 19.604 60.477 1.00 26.92 ? 579 PRO A C 1 ATOM 4423 O O . PRO A 1 579 ? 22.116 19.060 61.456 1.00 27.01 ? 579 PRO A O 1 ATOM 4424 C CB . PRO A 1 579 ? 23.203 19.646 58.553 1.00 26.56 ? 579 PRO A CB 1 ATOM 4425 C CG . PRO A 1 579 ? 24.536 19.447 59.265 1.00 26.48 ? 579 PRO A CG 1 ATOM 4426 C CD . PRO A 1 579 ? 24.783 20.726 60.032 1.00 26.40 ? 579 PRO A CD 1 ATOM 4427 N N . MET A 1 580 ? 20.298 19.475 60.176 1.00 26.86 ? 580 MET A N 1 ATOM 4428 C CA . MET A 1 580 ? 19.394 18.636 60.945 1.00 27.19 ? 580 MET A CA 1 ATOM 4429 C C . MET A 1 580 ? 18.340 18.031 60.017 1.00 27.80 ? 580 MET A C 1 ATOM 4430 O O . MET A 1 580 ? 17.457 18.737 59.494 1.00 27.74 ? 580 MET A O 1 ATOM 4431 C CB . MET A 1 580 ? 18.761 19.452 62.085 1.00 27.16 ? 580 MET A CB 1 ATOM 4432 C CG . MET A 1 580 ? 17.833 18.639 62.992 1.00 27.47 ? 580 MET A CG 1 ATOM 4433 S SD . MET A 1 580 ? 17.137 19.618 64.332 1.00 27.72 ? 580 MET A SD 1 ATOM 4434 C CE . MET A 1 580 ? 15.905 20.583 63.423 1.00 25.78 ? 580 MET A CE 1 ATOM 4435 N N . ASN A 1 581 ? 18.457 16.728 59.795 1.00 28.62 ? 581 ASN A N 1 ATOM 4436 C CA . ASN A 1 581 ? 17.611 16.019 58.844 1.00 29.23 ? 581 ASN A CA 1 ATOM 4437 C C . ASN A 1 581 ? 16.855 14.894 59.517 1.00 30.60 ? 581 ASN A C 1 ATOM 4438 O O . ASN A 1 581 ? 17.323 14.343 60.518 1.00 30.23 ? 581 ASN A O 1 ATOM 4439 C CB . ASN A 1 581 ? 18.467 15.441 57.707 1.00 29.17 ? 581 ASN A CB 1 ATOM 4440 C CG . ASN A 1 581 ? 19.136 16.525 56.869 1.00 28.82 ? 581 ASN A CG 1 ATOM 4441 O OD1 . ASN A 1 581 ? 18.489 17.161 56.035 1.00 28.53 ? 581 ASN A OD1 1 ATOM 4442 N ND2 . ASN A 1 581 ? 20.418 16.752 57.103 1.00 27.35 ? 581 ASN A ND2 1 ATOM 4443 N N . VAL A 1 582 ? 15.710 14.529 58.941 1.00 31.50 ? 582 VAL A N 1 ATOM 4444 C CA . VAL A 1 582 ? 14.898 13.444 59.474 1.00 33.26 ? 582 VAL A CA 1 ATOM 4445 C C . VAL A 1 582 ? 15.745 12.174 59.612 1.00 34.08 ? 582 VAL A C 1 ATOM 4446 O O . VAL A 1 582 ? 16.520 11.818 58.713 1.00 34.11 ? 582 VAL A O 1 ATOM 4447 C CB . VAL A 1 582 ? 13.579 13.236 58.669 1.00 33.48 ? 582 VAL A CB 1 ATOM 4448 C CG1 . VAL A 1 582 ? 13.832 12.625 57.281 1.00 33.49 ? 582 VAL A CG1 1 ATOM 4449 C CG2 . VAL A 1 582 ? 12.569 12.416 59.478 1.00 34.52 ? 582 VAL A CG2 1 ATOM 4450 N N . GLY A 1 583 ? 15.639 11.532 60.771 1.00 35.10 ? 583 GLY A N 1 ATOM 4451 C CA . GLY A 1 583 ? 16.437 10.338 61.047 1.00 35.77 ? 583 GLY A CA 1 ATOM 4452 C C . GLY A 1 583 ? 17.710 10.595 61.829 1.00 36.60 ? 583 GLY A C 1 ATOM 4453 O O . GLY A 1 583 ? 18.397 9.638 62.218 1.00 36.87 ? 583 GLY A O 1 ATOM 4454 N N . ASP A 1 584 ? 18.041 11.870 62.046 1.00 36.93 ? 584 ASP A N 1 ATOM 4455 C CA . ASP A 1 584 ? 19.199 12.269 62.855 1.00 37.74 ? 584 ASP A CA 1 ATOM 4456 C C . ASP A 1 584 ? 18.962 11.898 64.313 1.00 38.73 ? 584 ASP A C 1 ATOM 4457 O O . ASP A 1 584 ? 17.808 11.778 64.744 1.00 38.50 ? 584 ASP A O 1 ATOM 4458 C CB . ASP A 1 584 ? 19.429 13.780 62.785 1.00 37.60 ? 584 ASP A CB 1 ATOM 4459 C CG . ASP A 1 584 ? 20.194 14.220 61.530 1.00 36.83 ? 584 ASP A CG 1 ATOM 4460 O OD1 . ASP A 1 584 ? 20.535 15.424 61.462 1.00 37.06 ? 584 ASP A OD1 1 ATOM 4461 O OD2 . ASP A 1 584 ? 20.458 13.384 60.632 1.00 34.68 ? 584 ASP A OD2 1 ATOM 4462 N N . ALA A 1 585 ? 20.050 11.743 65.068 1.00 39.93 ? 585 ALA A N 1 ATOM 4463 C CA . ALA A 1 585 ? 19.956 11.442 66.498 1.00 40.87 ? 585 ALA A CA 1 ATOM 4464 C C . ALA A 1 585 ? 19.402 12.621 67.306 1.00 41.30 ? 585 ALA A C 1 ATOM 4465 O O . ALA A 1 585 ? 18.547 12.421 68.177 1.00 42.30 ? 585 ALA A O 1 ATOM 4466 C CB . ALA A 1 585 ? 21.312 10.996 67.049 1.00 41.19 ? 585 ALA A CB 1 ATOM 4467 N N . HIS A 1 586 ? 19.868 13.838 67.011 1.00 40.96 ? 586 HIS A N 1 ATOM 4468 C CA . HIS A 1 586 ? 19.492 15.037 67.787 1.00 40.84 ? 586 HIS A CA 1 ATOM 4469 C C . HIS A 1 586 ? 18.184 15.740 67.316 1.00 39.52 ? 586 HIS A C 1 ATOM 4470 O O . HIS A 1 586 ? 17.979 16.929 67.601 1.00 40.68 ? 586 HIS A O 1 ATOM 4471 C CB A HIS A 1 586 ? 20.661 16.034 67.837 0.50 41.29 ? 586 HIS A CB 1 ATOM 4472 C CB B HIS A 1 586 ? 20.664 16.045 67.813 0.50 41.14 ? 586 HIS A CB 1 ATOM 4473 C CG A HIS A 1 586 ? 21.707 15.702 68.859 0.50 42.50 ? 586 HIS A CG 1 ATOM 4474 C CG B HIS A 1 586 ? 20.691 17.001 66.651 0.50 42.00 ? 586 HIS A CG 1 ATOM 4475 N ND1 A HIS A 1 586 ? 22.251 16.650 69.700 0.50 43.79 ? 586 HIS A ND1 1 ATOM 4476 N ND1 B HIS A 1 586 ? 20.832 16.589 65.341 0.50 43.25 ? 586 HIS A ND1 1 ATOM 4477 C CD2 A HIS A 1 586 ? 22.310 14.530 69.174 0.50 43.40 ? 586 HIS A CD2 1 ATOM 4478 C CD2 B HIS A 1 586 ? 20.613 18.355 66.611 0.50 42.38 ? 586 HIS A CD2 1 ATOM 4479 C CE1 A HIS A 1 586 ? 23.144 16.077 70.487 0.50 43.60 ? 586 HIS A CE1 1 ATOM 4480 C CE1 B HIS A 1 586 ? 20.832 17.645 64.545 0.50 42.61 ? 586 HIS A CE1 1 ATOM 4481 N NE2 A HIS A 1 586 ? 23.198 14.791 70.190 0.50 44.25 ? 586 HIS A NE2 1 ATOM 4482 N NE2 B HIS A 1 586 ? 20.699 18.729 65.290 0.50 42.54 ? 586 HIS A NE2 1 ATOM 4483 N N . TYR A 1 587 ? 17.294 14.995 66.659 1.00 36.80 ? 587 TYR A N 1 ATOM 4484 C CA . TYR A 1 587 ? 16.216 15.583 65.839 1.00 33.81 ? 587 TYR A CA 1 ATOM 4485 C C . TYR A 1 587 ? 15.158 16.386 66.620 1.00 32.85 ? 587 TYR A C 1 ATOM 4486 O O . TYR A 1 587 ? 14.275 15.800 67.266 1.00 33.26 ? 587 TYR A O 1 ATOM 4487 C CB . TYR A 1 587 ? 15.547 14.489 65.011 1.00 32.58 ? 587 TYR A CB 1 ATOM 4488 C CG . TYR A 1 587 ? 14.717 14.989 63.846 1.00 31.25 ? 587 TYR A CG 1 ATOM 4489 C CD1 . TYR A 1 587 ? 15.306 15.711 62.806 1.00 30.19 ? 587 TYR A CD1 1 ATOM 4490 C CD2 . TYR A 1 587 ? 13.362 14.690 63.761 1.00 30.21 ? 587 TYR A CD2 1 ATOM 4491 C CE1 . TYR A 1 587 ? 14.539 16.152 61.715 1.00 29.41 ? 587 TYR A CE1 1 ATOM 4492 C CE2 . TYR A 1 587 ? 12.581 15.126 62.678 1.00 30.02 ? 587 TYR A CE2 1 ATOM 4493 C CZ . TYR A 1 587 ? 13.184 15.855 61.660 1.00 30.74 ? 587 TYR A CZ 1 ATOM 4494 O OH . TYR A 1 587 ? 12.414 16.275 60.592 1.00 29.82 ? 587 TYR A OH 1 ATOM 4495 N N . ASP A 1 588 ? 15.247 17.717 66.530 1.00 30.68 ? 588 ASP A N 1 ATOM 4496 C CA . ASP A 1 588 ? 14.378 18.633 67.277 1.00 28.96 ? 588 ASP A CA 1 ATOM 4497 C C . ASP A 1 588 ? 13.736 19.692 66.346 1.00 27.32 ? 588 ASP A C 1 ATOM 4498 O O . ASP A 1 588 ? 14.036 20.880 66.465 1.00 25.79 ? 588 ASP A O 1 ATOM 4499 C CB . ASP A 1 588 ? 15.187 19.308 68.389 1.00 29.36 ? 588 ASP A CB 1 ATOM 4500 C CG . ASP A 1 588 ? 14.338 20.193 69.298 1.00 30.87 ? 588 ASP A CG 1 ATOM 4501 O OD1 . ASP A 1 588 ? 13.121 19.960 69.428 1.00 32.75 ? 588 ASP A OD1 1 ATOM 4502 O OD2 . ASP A 1 588 ? 14.901 21.137 69.886 1.00 34.97 ? 588 ASP A OD2 1 ATOM 4503 N N . PRO A 1 589 ? 12.853 19.247 65.430 1.00 26.26 ? 589 PRO A N 1 ATOM 4504 C CA . PRO A 1 589 ? 12.310 20.196 64.444 1.00 25.74 ? 589 PRO A CA 1 ATOM 4505 C C . PRO A 1 589 ? 11.192 21.090 65.004 1.00 25.43 ? 589 PRO A C 1 ATOM 4506 O O . PRO A 1 589 ? 10.506 20.697 65.969 1.00 25.19 ? 589 PRO A O 1 ATOM 4507 C CB . PRO A 1 589 ? 11.727 19.268 63.383 1.00 26.11 ? 589 PRO A CB 1 ATOM 4508 C CG . PRO A 1 589 ? 11.227 18.082 64.170 1.00 26.29 ? 589 PRO A CG 1 ATOM 4509 C CD . PRO A 1 589 ? 12.297 17.889 65.238 1.00 26.00 ? 589 PRO A CD 1 ATOM 4510 N N . LEU A 1 590 ? 11.010 22.265 64.392 1.00 24.31 ? 590 LEU A N 1 ATOM 4511 C CA . LEU A 1 590 ? 9.774 23.037 64.557 1.00 23.59 ? 590 LEU A CA 1 ATOM 4512 C C . LEU A 1 590 ? 8.620 22.265 63.915 1.00 23.67 ? 590 LEU A C 1 ATOM 4513 O O . LEU A 1 590 ? 7.562 22.103 64.526 1.00 24.07 ? 590 LEU A O 1 ATOM 4514 C CB . LEU A 1 590 ? 9.893 24.436 63.950 1.00 23.66 ? 590 LEU A CB 1 ATOM 4515 C CG . LEU A 1 590 ? 8.717 25.394 64.221 1.00 23.41 ? 590 LEU A CG 1 ATOM 4516 C CD1 . LEU A 1 590 ? 8.637 25.776 65.715 1.00 25.22 ? 590 LEU A CD1 1 ATOM 4517 C CD2 . LEU A 1 590 ? 8.861 26.651 63.385 1.00 22.99 ? 590 LEU A CD2 1 ATOM 4518 N N . PHE A 1 591 ? 8.820 21.808 62.674 1.00 22.73 ? 591 PHE A N 1 ATOM 4519 C CA . PHE A 1 591 ? 7.887 20.902 62.018 1.00 22.76 ? 591 PHE A CA 1 ATOM 4520 C C . PHE A 1 591 ? 8.719 19.798 61.394 1.00 23.12 ? 591 PHE A C 1 ATOM 4521 O O . PHE A 1 591 ? 9.654 20.081 60.628 1.00 22.94 ? 591 PHE A O 1 ATOM 4522 C CB . PHE A 1 591 ? 7.094 21.605 60.896 1.00 22.80 ? 591 PHE A CB 1 ATOM 4523 C CG . PHE A 1 591 ? 6.289 22.793 61.347 1.00 23.65 ? 591 PHE A CG 1 ATOM 4524 C CD1 . PHE A 1 591 ? 5.057 22.624 61.988 1.00 23.97 ? 591 PHE A CD1 1 ATOM 4525 C CD2 . PHE A 1 591 ? 6.748 24.084 61.096 1.00 22.96 ? 591 PHE A CD2 1 ATOM 4526 C CE1 . PHE A 1 591 ? 4.302 23.742 62.396 1.00 24.28 ? 591 PHE A CE1 1 ATOM 4527 C CE2 . PHE A 1 591 ? 6.019 25.206 61.498 1.00 23.09 ? 591 PHE A CE2 1 ATOM 4528 C CZ . PHE A 1 591 ? 4.783 25.039 62.149 1.00 22.39 ? 591 PHE A CZ 1 ATOM 4529 N N . ARG A 1 592 ? 8.384 18.547 61.701 1.00 23.77 ? 592 ARG A N 1 ATOM 4530 C CA . ARG A 1 592 ? 9.097 17.396 61.114 1.00 25.65 ? 592 ARG A CA 1 ATOM 4531 C C . ARG A 1 592 ? 8.823 17.292 59.610 1.00 23.93 ? 592 ARG A C 1 ATOM 4532 O O . ARG A 1 592 ? 7.773 17.746 59.118 1.00 23.55 ? 592 ARG A O 1 ATOM 4533 C CB . ARG A 1 592 ? 8.662 16.077 61.776 1.00 25.50 ? 592 ARG A CB 1 ATOM 4534 C CG . ARG A 1 592 ? 7.175 15.832 61.727 1.00 27.55 ? 592 ARG A CG 1 ATOM 4535 C CD . ARG A 1 592 ? 6.768 14.429 62.198 1.00 28.29 ? 592 ARG A CD 1 ATOM 4536 N NE . ARG A 1 592 ? 6.327 13.674 61.023 1.00 44.58 ? 592 ARG A NE 1 ATOM 4537 C CZ . ARG A 1 592 ? 5.128 13.771 60.439 1.00 31.40 ? 592 ARG A CZ 1 ATOM 4538 N NH1 . ARG A 1 592 ? 4.888 13.035 59.360 1.00 49.36 ? 592 ARG A NH1 1 ATOM 4539 N NH2 . ARG A 1 592 ? 4.172 14.587 60.912 1.00 51.51 ? 592 ARG A NH2 1 ATOM 4540 N N . LEU A 1 593 ? 9.750 16.655 58.899 1.00 23.54 ? 593 LEU A N 1 ATOM 4541 C CA . LEU A 1 593 ? 9.498 16.234 57.523 1.00 23.65 ? 593 LEU A CA 1 ATOM 4542 C C . LEU A 1 593 ? 8.187 15.457 57.484 1.00 23.50 ? 593 LEU A C 1 ATOM 4543 O O . LEU A 1 593 ? 7.924 14.592 58.352 1.00 24.01 ? 593 LEU A O 1 ATOM 4544 C CB . LEU A 1 593 ? 10.665 15.374 56.975 1.00 23.97 ? 593 LEU A CB 1 ATOM 4545 C CG . LEU A 1 593 ? 10.547 14.961 55.494 1.00 24.53 ? 593 LEU A CG 1 ATOM 4546 C CD1 . LEU A 1 593 ? 11.927 14.934 54.832 1.00 25.24 ? 593 LEU A CD1 1 ATOM 4547 C CD2 . LEU A 1 593 ? 9.830 13.632 55.318 1.00 25.93 ? 593 LEU A CD2 1 ATOM 4548 N N . GLY A 1 594 ? 7.345 15.781 56.505 1.00 22.25 ? 594 GLY A N 1 ATOM 4549 C CA . GLY A 1 594 ? 6.075 15.105 56.340 1.00 21.96 ? 594 GLY A CA 1 ATOM 4550 C C . GLY A 1 594 ? 4.892 15.802 57.003 1.00 21.33 ? 594 GLY A C 1 ATOM 4551 O O . GLY A 1 594 ? 3.757 15.431 56.763 1.00 21.85 ? 594 GLY A O 1 ATOM 4552 N N . TYR A 1 595 ? 5.159 16.813 57.823 1.00 21.35 ? 595 TYR A N 1 ATOM 4553 C CA . TYR A 1 595 ? 4.089 17.616 58.444 1.00 21.97 ? 595 TYR A CA 1 ATOM 4554 C C . TYR A 1 595 ? 3.284 18.410 57.403 1.00 21.84 ? 595 TYR A C 1 ATOM 4555 O O . TYR A 1 595 ? 3.854 18.977 56.450 1.00 20.87 ? 595 TYR A O 1 ATOM 4556 C CB . TYR A 1 595 ? 4.701 18.582 59.448 1.00 22.78 ? 595 TYR A CB 1 ATOM 4557 C CG . TYR A 1 595 ? 3.698 19.486 60.127 1.00 23.74 ? 595 TYR A CG 1 ATOM 4558 C CD1 . TYR A 1 595 ? 3.347 20.710 59.553 1.00 25.68 ? 595 TYR A CD1 1 ATOM 4559 C CD2 . TYR A 1 595 ? 3.128 19.139 61.349 1.00 26.41 ? 595 TYR A CD2 1 ATOM 4560 C CE1 . TYR A 1 595 ? 2.445 21.549 60.149 1.00 27.03 ? 595 TYR A CE1 1 ATOM 4561 C CE2 . TYR A 1 595 ? 2.199 20.004 61.970 1.00 27.37 ? 595 TYR A CE2 1 ATOM 4562 C CZ . TYR A 1 595 ? 1.875 21.199 61.343 1.00 27.17 ? 595 TYR A CZ 1 ATOM 4563 O OH . TYR A 1 595 ? 0.984 22.095 61.892 1.00 29.27 ? 595 TYR A OH 1 ATOM 4564 N N . GLY A 1 596 ? 1.965 18.435 57.571 1.00 21.40 ? 596 GLY A N 1 ATOM 4565 C CA . GLY A 1 596 ? 1.127 19.367 56.818 1.00 21.68 ? 596 GLY A CA 1 ATOM 4566 C C . GLY A 1 596 ? -0.312 19.250 57.280 1.00 21.86 ? 596 GLY A C 1 ATOM 4567 O O . GLY A 1 596 ? -0.863 18.145 57.355 1.00 22.76 ? 596 GLY A O 1 ATOM 4568 N N . LEU A 1 597 ? -0.913 20.386 57.601 1.00 21.67 ? 597 LEU A N 1 ATOM 4569 C CA . LEU A 1 597 ? -2.334 20.421 57.956 1.00 22.08 ? 597 LEU A CA 1 ATOM 4570 C C . LEU A 1 597 ? -3.158 20.246 56.688 1.00 22.60 ? 597 LEU A C 1 ATOM 4571 O O . LEU A 1 597 ? -2.670 20.506 55.581 1.00 23.12 ? 597 LEU A O 1 ATOM 4572 C CB . LEU A 1 597 ? -2.681 21.756 58.636 1.00 22.36 ? 597 LEU A CB 1 ATOM 4573 C CG . LEU A 1 597 ? -1.929 22.019 59.940 1.00 22.64 ? 597 LEU A CG 1 ATOM 4574 C CD1 . LEU A 1 597 ? -2.313 23.371 60.531 1.00 22.08 ? 597 LEU A CD1 1 ATOM 4575 C CD2 . LEU A 1 597 ? -2.147 20.862 60.954 1.00 25.42 ? 597 LEU A CD2 1 ATOM 4576 N N . THR A 1 598 ? -4.407 19.808 56.831 1.00 23.26 ? 598 THR A N 1 ATOM 4577 C CA . THR A 1 598 ? -5.270 19.684 55.661 1.00 24.35 ? 598 THR A CA 1 ATOM 4578 C C . THR A 1 598 ? -6.550 20.510 55.797 1.00 24.59 ? 598 THR A C 1 ATOM 4579 O O . THR A 1 598 ? -6.906 20.962 56.890 1.00 24.58 ? 598 THR A O 1 ATOM 4580 C CB . THR A 1 598 ? -5.641 18.220 55.390 1.00 25.13 ? 598 THR A CB 1 ATOM 4581 O OG1 . THR A 1 598 ? -6.350 17.678 56.526 1.00 25.96 ? 598 THR A OG1 1 ATOM 4582 C CG2 . THR A 1 598 ? -4.373 17.388 55.121 1.00 25.92 ? 598 THR A CG2 1 ATOM 4583 N N . THR A 1 599 ? -7.228 20.704 54.673 1.00 25.31 ? 599 THR A N 1 ATOM 4584 C CA . THR A 1 599 ? -8.564 21.270 54.656 1.00 25.70 ? 599 THR A CA 1 ATOM 4585 C C . THR A 1 599 ? -9.340 20.431 53.656 1.00 27.64 ? 599 THR A C 1 ATOM 4586 O O . THR A 1 599 ? -8.762 19.625 52.924 1.00 27.31 ? 599 THR A O 1 ATOM 4587 C CB . THR A 1 599 ? -8.588 22.736 54.177 1.00 25.57 ? 599 THR A CB 1 ATOM 4588 O OG1 . THR A 1 599 ? -8.013 22.806 52.862 1.00 24.14 ? 599 THR A OG1 1 ATOM 4589 C CG2 . THR A 1 599 ? -7.833 23.660 55.138 1.00 24.27 ? 599 THR A CG2 1 ATOM 4590 N N . ASN A 1 600 ? -10.654 20.604 53.641 1.00 29.67 ? 600 ASN A N 1 ATOM 4591 C CA . ASN A 1 600 ? -11.482 20.000 52.609 1.00 31.95 ? 600 ASN A CA 1 ATOM 4592 C C . ASN A 1 600 ? -12.096 21.055 51.704 1.00 32.58 ? 600 ASN A C 1 ATOM 4593 O O . ASN A 1 600 ? -12.370 22.176 52.151 1.00 32.49 ? 600 ASN A O 1 ATOM 4594 C CB . ASN A 1 600 ? -12.547 19.120 53.262 1.00 32.49 ? 600 ASN A CB 1 ATOM 4595 C CG . ASN A 1 600 ? -11.947 17.863 53.848 1.00 36.60 ? 600 ASN A CG 1 ATOM 4596 O OD1 . ASN A 1 600 ? -11.854 17.718 55.068 1.00 39.53 ? 600 ASN A OD1 1 ATOM 4597 N ND2 . ASN A 1 600 ? -11.488 16.963 52.970 1.00 41.34 ? 600 ASN A ND2 1 ATOM 4598 N N . ALA A 1 601 ? -12.287 20.692 50.435 1.00 34.05 ? 601 ALA A N 1 ATOM 4599 C CA . ALA A 1 601 ? -12.931 21.563 49.456 1.00 35.75 ? 601 ALA A CA 1 ATOM 4600 C C . ALA A 1 601 ? -14.305 22.022 49.950 1.00 37.53 ? 601 ALA A C 1 ATOM 4601 O O . ALA A 1 601 ? -15.023 21.260 50.603 1.00 37.85 ? 601 ALA A O 1 ATOM 4602 C CB . ALA A 1 601 ? -13.054 20.860 48.109 1.00 35.47 ? 601 ALA A CB 1 ATOM 4603 N N . THR A 1 602 ? -14.654 23.271 49.664 1.00 39.23 ? 602 THR A N 1 ATOM 4604 C CA . THR A 1 602 ? -15.961 23.809 50.040 1.00 40.99 ? 602 THR A CA 1 ATOM 4605 C C . THR A 1 602 ? -17.059 23.170 49.195 1.00 42.15 ? 602 THR A C 1 ATOM 4606 O O . THR A 1 602 ? -18.215 23.064 49.643 1.00 43.29 ? 602 THR A O 1 ATOM 4607 C CB . THR A 1 602 ? -16.032 25.310 49.825 1.00 41.16 ? 602 THR A CB 1 ATOM 4608 O OG1 . THR A 1 602 ? -15.872 25.575 48.425 1.00 43.71 ? 602 THR A OG1 1 ATOM 4609 C CG2 . THR A 1 602 ? -14.948 26.028 50.622 1.00 39.98 ? 602 THR A CG2 1 HETATM 4610 C C1 . NAG B 2 . ? 34.940 25.782 50.661 1.00 33.88 ? 701 NAG A C1 1 HETATM 4611 C C2 . NAG B 2 . ? 36.155 25.621 49.732 1.00 35.92 ? 701 NAG A C2 1 HETATM 4612 C C3 . NAG B 2 . ? 37.375 26.369 50.305 1.00 38.99 ? 701 NAG A C3 1 HETATM 4613 C C4 . NAG B 2 . ? 37.046 27.816 50.675 1.00 41.52 ? 701 NAG A C4 1 HETATM 4614 C C5 . NAG B 2 . ? 35.780 27.839 51.548 1.00 39.34 ? 701 NAG A C5 1 HETATM 4615 C C6 . NAG B 2 . ? 35.299 29.244 51.913 1.00 39.97 ? 701 NAG A C6 1 HETATM 4616 C C7 . NAG B 2 . ? 36.217 23.524 48.437 1.00 35.06 ? 701 NAG A C7 1 HETATM 4617 C C8 . NAG B 2 . ? 36.631 22.081 48.425 1.00 36.27 ? 701 NAG A C8 1 HETATM 4618 N N2 . NAG B 2 . ? 36.482 24.218 49.548 1.00 34.55 ? 701 NAG A N2 1 HETATM 4619 O O3 . NAG B 2 . ? 38.460 26.360 49.396 1.00 39.25 ? 701 NAG A O3 1 HETATM 4620 O O4 . NAG B 2 . ? 38.159 28.345 51.370 1.00 47.05 ? 701 NAG A O4 1 HETATM 4621 O O5 . NAG B 2 . ? 34.729 27.161 50.871 1.00 36.25 ? 701 NAG A O5 1 HETATM 4622 O O6 . NAG B 2 . ? 35.170 30.041 50.748 1.00 40.19 ? 701 NAG A O6 1 HETATM 4623 O O7 . NAG B 2 . ? 35.659 24.009 47.452 1.00 34.54 ? 701 NAG A O7 1 HETATM 4624 C C1 . NAG C 2 . ? 38.613 29.593 50.807 1.00 51.81 ? 702 NAG A C1 1 HETATM 4625 C C2 . NAG C 2 . ? 39.378 30.363 51.892 1.00 52.64 ? 702 NAG A C2 1 HETATM 4626 C C3 . NAG C 2 . ? 39.923 31.683 51.356 1.00 55.95 ? 702 NAG A C3 1 HETATM 4627 C C4 . NAG C 2 . ? 40.673 31.508 50.035 1.00 58.39 ? 702 NAG A C4 1 HETATM 4628 C C5 . NAG C 2 . ? 39.881 30.619 49.057 1.00 56.91 ? 702 NAG A C5 1 HETATM 4629 C C6 . NAG C 2 . ? 40.714 30.251 47.832 1.00 56.75 ? 702 NAG A C6 1 HETATM 4630 C C7 . NAG C 2 . ? 38.534 29.876 54.150 1.00 44.83 ? 702 NAG A C7 1 HETATM 4631 C C8 . NAG C 2 . ? 37.593 30.306 55.236 1.00 61.60 ? 702 NAG A C8 1 HETATM 4632 N N2 . NAG C 2 . ? 38.535 30.626 53.048 1.00 59.47 ? 702 NAG A N2 1 HETATM 4633 O O3 . NAG C 2 . ? 40.786 32.262 52.314 1.00 56.86 ? 702 NAG A O3 1 HETATM 4634 O O4 . NAG C 2 . ? 40.862 32.800 49.490 1.00 61.83 ? 702 NAG A O4 1 HETATM 4635 O O5 . NAG C 2 . ? 39.428 29.414 49.663 1.00 54.30 ? 702 NAG A O5 1 HETATM 4636 O O6 . NAG C 2 . ? 39.871 29.709 46.840 1.00 58.57 ? 702 NAG A O6 1 HETATM 4637 O O7 . NAG C 2 . ? 39.245 28.883 54.301 1.00 61.23 ? 702 NAG A O7 1 HETATM 4638 C C1 . BMA D 3 . ? 42.257 33.150 49.337 1.00 64.75 ? 703 BMA A C1 1 HETATM 4639 C C2 . BMA D 3 . ? 42.393 33.982 48.060 1.00 65.95 ? 703 BMA A C2 1 HETATM 4640 C C3 . BMA D 3 . ? 43.835 34.452 47.836 1.00 66.90 ? 703 BMA A C3 1 HETATM 4641 C C4 . BMA D 3 . ? 44.466 35.035 49.107 1.00 67.24 ? 703 BMA A C4 1 HETATM 4642 C C5 . BMA D 3 . ? 44.160 34.211 50.365 1.00 67.29 ? 703 BMA A C5 1 HETATM 4643 C C6 . BMA D 3 . ? 44.559 35.011 51.606 1.00 67.33 ? 703 BMA A C6 1 HETATM 4644 O O2 . BMA D 3 . ? 41.510 35.084 48.130 1.00 66.37 ? 703 BMA A O2 1 HETATM 4645 O O3 . BMA D 3 . ? 43.881 35.413 46.795 1.00 66.49 ? 703 BMA A O3 1 HETATM 4646 O O4 . BMA D 3 . ? 45.867 35.133 48.937 1.00 68.05 ? 703 BMA A O4 1 HETATM 4647 O O5 . BMA D 3 . ? 42.780 33.861 50.450 1.00 66.43 ? 703 BMA A O5 1 HETATM 4648 O O6 . BMA D 3 . ? 44.667 34.150 52.717 1.00 67.79 ? 703 BMA A O6 1 HETATM 4649 C C1 . NAG E 2 . ? 21.188 36.822 55.698 1.00 53.54 ? 704 NAG A C1 1 HETATM 4650 C C2 . NAG E 2 . ? 21.071 38.345 55.766 1.00 62.08 ? 704 NAG A C2 1 HETATM 4651 C C3 . NAG E 2 . ? 20.720 39.011 54.428 1.00 61.38 ? 704 NAG A C3 1 HETATM 4652 C C4 . NAG E 2 . ? 21.538 38.430 53.260 1.00 61.77 ? 704 NAG A C4 1 HETATM 4653 C C5 . NAG E 2 . ? 21.688 36.902 53.375 1.00 60.36 ? 704 NAG A C5 1 HETATM 4654 C C6 . NAG E 2 . ? 22.663 36.319 52.348 1.00 59.12 ? 704 NAG A C6 1 HETATM 4655 C C7 . NAG E 2 . ? 20.526 39.319 57.957 1.00 68.85 ? 704 NAG A C7 1 HETATM 4656 C C8 . NAG E 2 . ? 21.997 39.571 58.186 1.00 59.70 ? 704 NAG A C8 1 HETATM 4657 N N2 . NAG E 2 . ? 20.139 38.745 56.809 1.00 54.97 ? 704 NAG A N2 1 HETATM 4658 O O3 . NAG E 2 . ? 21.058 40.363 54.661 1.00 64.62 ? 704 NAG A O3 1 HETATM 4659 O O4 . NAG E 2 . ? 20.931 38.765 52.016 1.00 64.19 ? 704 NAG A O4 1 HETATM 4660 O O5 . NAG E 2 . ? 22.109 36.505 54.673 1.00 56.72 ? 704 NAG A O5 1 HETATM 4661 O O6 . NAG E 2 . ? 24.001 36.610 52.693 1.00 60.53 ? 704 NAG A O6 1 HETATM 4662 O O7 . NAG E 2 . ? 19.707 39.645 58.823 1.00 55.96 ? 704 NAG A O7 1 HETATM 4663 C C1 . NAG F 2 . ? 21.851 39.448 51.123 1.00 67.09 ? 705 NAG A C1 1 HETATM 4664 C C2 . NAG F 2 . ? 21.227 39.664 49.733 1.00 70.18 ? 705 NAG A C2 1 HETATM 4665 C C3 . NAG F 2 . ? 22.173 40.456 48.819 1.00 68.17 ? 705 NAG A C3 1 HETATM 4666 C C4 . NAG F 2 . ? 22.832 41.663 49.507 1.00 68.81 ? 705 NAG A C4 1 HETATM 4667 C C5 . NAG F 2 . ? 23.351 41.285 50.903 1.00 70.83 ? 705 NAG A C5 1 HETATM 4668 C C6 . NAG F 2 . ? 23.918 42.474 51.690 1.00 62.54 ? 705 NAG A C6 1 HETATM 4669 C C7 . NAG F 2 . ? 19.662 37.881 48.917 1.00 77.88 ? 705 NAG A C7 1 HETATM 4670 C C8 . NAG F 2 . ? 18.489 38.653 49.448 1.00 63.99 ? 705 NAG A C8 1 HETATM 4671 N N2 . NAG F 2 . ? 20.893 38.398 49.084 1.00 63.97 ? 705 NAG A N2 1 HETATM 4672 O O3 . NAG F 2 . ? 21.482 40.871 47.656 1.00 67.99 ? 705 NAG A O3 1 HETATM 4673 O O4 . NAG F 2 . ? 23.907 42.114 48.705 1.00 68.69 ? 705 NAG A O4 1 HETATM 4674 O O5 . NAG F 2 . ? 22.311 40.680 51.650 1.00 67.69 ? 705 NAG A O5 1 HETATM 4675 O O6 . NAG F 2 . ? 22.898 43.387 52.049 1.00 76.12 ? 705 NAG A O6 1 HETATM 4676 O O7 . NAG F 2 . ? 19.462 36.798 48.351 1.00 65.44 ? 705 NAG A O7 1 HETATM 4677 C C1 . BMA G 3 . ? 23.669 43.430 48.152 1.00 69.15 ? 706 BMA A C1 1 HETATM 4678 C C2 . BMA G 3 . ? 24.954 43.927 47.475 1.00 69.52 ? 706 BMA A C2 1 HETATM 4679 C C3 . BMA G 3 . ? 24.740 45.280 46.776 1.00 69.45 ? 706 BMA A C3 1 HETATM 4680 C C4 . BMA G 3 . ? 23.455 45.294 45.937 1.00 68.90 ? 706 BMA A C4 1 HETATM 4681 C C5 . BMA G 3 . ? 22.287 44.794 46.789 1.00 68.09 ? 706 BMA A C5 1 HETATM 4682 C C6 . BMA G 3 . ? 20.963 44.789 46.034 1.00 66.50 ? 706 BMA A C6 1 HETATM 4683 O O2 . BMA G 3 . ? 25.416 42.952 46.556 1.00 69.76 ? 706 BMA A O2 1 HETATM 4684 O O3 . BMA G 3 . ? 25.858 45.608 45.973 1.00 69.39 ? 706 BMA A O3 1 HETATM 4685 O O4 . BMA G 3 . ? 23.190 46.592 45.451 1.00 69.55 ? 706 BMA A O4 1 HETATM 4686 O O5 . BMA G 3 . ? 22.576 43.481 47.245 1.00 68.54 ? 706 BMA A O5 1 HETATM 4687 O O6 . BMA G 3 . ? 20.156 43.819 46.662 1.00 64.19 ? 706 BMA A O6 1 HETATM 4688 C C1 . FUL H 4 . ? 20.351 41.425 53.965 1.00 67.15 ? 707 FUL A C1 1 HETATM 4689 C C2 . FUL H 4 . ? 20.190 42.642 54.867 1.00 68.05 ? 707 FUL A C2 1 HETATM 4690 O O2 . FUL H 4 . ? 21.271 42.754 55.765 1.00 68.93 ? 707 FUL A O2 1 HETATM 4691 C C3 . FUL H 4 . ? 20.134 43.834 53.916 1.00 68.53 ? 707 FUL A C3 1 HETATM 4692 O O3 . FUL H 4 . ? 20.038 45.044 54.643 1.00 68.83 ? 707 FUL A O3 1 HETATM 4693 C C4 . FUL H 4 . ? 18.992 43.655 52.893 1.00 68.46 ? 707 FUL A C4 1 HETATM 4694 O O4 . FUL H 4 . ? 17.743 43.960 53.484 1.00 68.58 ? 707 FUL A O4 1 HETATM 4695 C C5 . FUL H 4 . ? 18.971 42.231 52.285 1.00 68.17 ? 707 FUL A C5 1 HETATM 4696 C C6 . FUL H 4 . ? 17.744 41.991 51.402 1.00 67.91 ? 707 FUL A C6 1 HETATM 4697 O O5 . FUL H 4 . ? 19.110 41.221 53.292 1.00 67.63 ? 707 FUL A O5 1 HETATM 4698 C C1 . MAN I 5 . ? 18.804 43.847 46.167 1.00 62.54 ? 708 MAN A C1 1 HETATM 4699 C C2 . MAN I 5 . ? 17.913 43.141 47.191 1.00 61.33 ? 708 MAN A C2 1 HETATM 4700 C C3 . MAN I 5 . ? 18.279 41.656 47.229 1.00 60.51 ? 708 MAN A C3 1 HETATM 4701 C C4 . MAN I 5 . ? 18.164 41.040 45.833 1.00 59.85 ? 708 MAN A C4 1 HETATM 4702 C C5 . MAN I 5 . ? 19.005 41.856 44.838 1.00 60.64 ? 708 MAN A C5 1 HETATM 4703 C C6 . MAN I 5 . ? 18.880 41.370 43.397 1.00 60.01 ? 708 MAN A C6 1 HETATM 4704 O O2 . MAN I 5 . ? 16.558 43.225 46.806 1.00 60.73 ? 708 MAN A O2 1 HETATM 4705 O O3 . MAN I 5 . ? 17.441 40.976 48.132 1.00 59.70 ? 708 MAN A O3 1 HETATM 4706 O O4 . MAN I 5 . ? 18.579 39.696 45.887 1.00 59.18 ? 708 MAN A O4 1 HETATM 4707 O O5 . MAN I 5 . ? 18.644 43.235 44.891 1.00 61.59 ? 708 MAN A O5 1 HETATM 4708 O O6 . MAN I 5 . ? 19.708 42.158 42.568 1.00 58.57 ? 708 MAN A O6 1 HETATM 4709 C C1 . NAG J 2 . ? 15.881 44.380 47.341 1.00 61.42 ? 709 NAG A C1 1 HETATM 4710 C C2 . NAG J 2 . ? 14.634 44.584 46.472 1.00 61.15 ? 709 NAG A C2 1 HETATM 4711 C C3 . NAG J 2 . ? 13.764 45.726 47.004 1.00 60.99 ? 709 NAG A C3 1 HETATM 4712 C C4 . NAG J 2 . ? 13.485 45.533 48.501 1.00 60.47 ? 709 NAG A C4 1 HETATM 4713 C C5 . NAG J 2 . ? 14.790 45.301 49.286 1.00 60.03 ? 709 NAG A C5 1 HETATM 4714 C C6 . NAG J 2 . ? 14.543 44.997 50.770 1.00 68.01 ? 709 NAG A C6 1 HETATM 4715 C C7 . NAG J 2 . ? 14.875 43.817 44.132 1.00 65.45 ? 709 NAG A C7 1 HETATM 4716 C C8 . NAG J 2 . ? 15.353 44.187 42.757 1.00 54.71 ? 709 NAG A C8 1 HETATM 4717 N N2 . NAG J 2 . ? 15.026 44.761 45.074 1.00 55.55 ? 709 NAG A N2 1 HETATM 4718 O O3 . NAG J 2 . ? 12.548 45.764 46.289 1.00 60.47 ? 709 NAG A O3 1 HETATM 4719 O O4 . NAG J 2 . ? 12.788 46.646 49.023 1.00 61.99 ? 709 NAG A O4 1 HETATM 4720 O O5 . NAG J 2 . ? 15.551 44.241 48.718 1.00 60.75 ? 709 NAG A O5 1 HETATM 4721 O O6 . NAG J 2 . ? 13.592 43.965 50.946 1.00 55.28 ? 709 NAG A O6 1 HETATM 4722 O O7 . NAG J 2 . ? 14.381 42.702 44.332 1.00 52.72 ? 709 NAG A O7 1 HETATM 4723 C C1 . NAG K 2 . ? -10.834 15.818 53.559 1.00 48.21 ? 710 NAG A C1 1 HETATM 4724 C C2 . NAG K 2 . ? -11.297 14.735 52.577 1.00 52.70 ? 710 NAG A C2 1 HETATM 4725 C C3 . NAG K 2 . ? -10.539 13.413 52.744 1.00 54.42 ? 710 NAG A C3 1 HETATM 4726 C C4 . NAG K 2 . ? -9.031 13.625 52.978 1.00 52.88 ? 710 NAG A C4 1 HETATM 4727 C C5 . NAG K 2 . ? -8.765 14.767 53.978 1.00 50.35 ? 710 NAG A C5 1 HETATM 4728 C C6 . NAG K 2 . ? -7.279 15.082 54.181 1.00 49.96 ? 710 NAG A C6 1 HETATM 4729 C C7 . NAG K 2 . ? -13.576 14.710 51.718 1.00 60.34 ? 710 NAG A C7 1 HETATM 4730 C C8 . NAG K 2 . ? -15.029 14.449 52.005 1.00 52.44 ? 710 NAG A C8 1 HETATM 4731 N N2 . NAG K 2 . ? -12.728 14.513 52.729 1.00 50.03 ? 710 NAG A N2 1 HETATM 4732 O O3 . NAG K 2 . ? -10.716 12.614 51.580 1.00 57.97 ? 710 NAG A O3 1 HETATM 4733 O O4 . NAG K 2 . ? -8.451 12.410 53.423 1.00 53.91 ? 710 NAG A O4 1 HETATM 4734 O O5 . NAG K 2 . ? -9.423 15.938 53.532 1.00 49.24 ? 710 NAG A O5 1 HETATM 4735 O O6 . NAG K 2 . ? -6.652 15.326 52.938 1.00 47.08 ? 710 NAG A O6 1 HETATM 4736 O O7 . NAG K 2 . ? -13.219 15.081 50.593 1.00 52.25 ? 710 NAG A O7 1 HETATM 4737 C C1 . NAG L 2 . ? -7.323 12.006 52.606 1.00 54.59 ? 711 NAG A C1 1 HETATM 4738 C C2 . NAG L 2 . ? -6.551 10.886 53.315 1.00 54.78 ? 711 NAG A C2 1 HETATM 4739 C C3 . NAG L 2 . ? -5.342 10.429 52.499 1.00 55.64 ? 711 NAG A C3 1 HETATM 4740 C C4 . NAG L 2 . ? -5.709 10.175 51.033 1.00 56.50 ? 711 NAG A C4 1 HETATM 4741 C C5 . NAG L 2 . ? -6.520 11.357 50.471 1.00 57.37 ? 711 NAG A C5 1 HETATM 4742 C C6 . NAG L 2 . ? -6.965 11.149 49.024 1.00 50.38 ? 711 NAG A C6 1 HETATM 4743 C C7 . NAG L 2 . ? -6.816 10.993 55.743 1.00 48.12 ? 711 NAG A C7 1 HETATM 4744 C C8 . NAG L 2 . ? -6.233 11.465 57.042 1.00 60.76 ? 711 NAG A C8 1 HETATM 4745 N N2 . NAG L 2 . ? -6.115 11.281 54.646 1.00 59.33 ? 711 NAG A N2 1 HETATM 4746 O O3 . NAG L 2 . ? -4.808 9.260 53.082 1.00 55.60 ? 711 NAG A O3 1 HETATM 4747 O O4 . NAG L 2 . ? -4.523 9.983 50.284 1.00 55.53 ? 711 NAG A O4 1 HETATM 4748 O O5 . NAG L 2 . ? -7.660 11.608 51.283 1.00 55.76 ? 711 NAG A O5 1 HETATM 4749 O O6 . NAG L 2 . ? -7.883 10.078 48.966 1.00 63.29 ? 711 NAG A O6 1 HETATM 4750 O O7 . NAG L 2 . ? -7.889 10.382 55.725 1.00 62.27 ? 711 NAG A O7 1 HETATM 4751 C C1 . BMA M 3 . ? -4.327 8.601 49.902 1.00 55.81 ? 712 BMA A C1 1 HETATM 4752 C C2 . BMA M 3 . ? -3.440 8.579 48.657 1.00 55.11 ? 712 BMA A C2 1 HETATM 4753 C C3 . BMA M 3 . ? -3.158 7.133 48.222 1.00 56.06 ? 712 BMA A C3 1 HETATM 4754 C C4 . BMA M 3 . ? -2.619 6.307 49.395 1.00 56.97 ? 712 BMA A C4 1 HETATM 4755 C C5 . BMA M 3 . ? -3.571 6.439 50.598 1.00 57.73 ? 712 BMA A C5 1 HETATM 4756 C C6 . BMA M 3 . ? -3.170 5.599 51.822 1.00 55.26 ? 712 BMA A C6 1 HETATM 4757 O O2 . BMA M 3 . ? -2.222 9.203 49.013 1.00 52.82 ? 712 BMA A O2 1 HETATM 4758 O O3 . BMA M 3 . ? -2.234 7.098 47.149 1.00 56.59 ? 712 BMA A O3 1 HETATM 4759 O O4 . BMA M 3 . ? -2.451 4.959 48.999 1.00 57.86 ? 712 BMA A O4 1 HETATM 4760 O O5 . BMA M 3 . ? -3.734 7.817 50.936 1.00 56.81 ? 712 BMA A O5 1 HETATM 4761 O O6 . BMA M 3 . ? -1.789 5.685 52.107 1.00 60.61 ? 712 BMA A O6 1 HETATM 4762 C C1 . FUL N 4 . ? -11.631 11.499 51.745 1.00 61.37 ? 713 FUL A C1 1 HETATM 4763 C C2 . FUL N 4 . ? -10.922 10.375 52.529 1.00 62.57 ? 713 FUL A C2 1 HETATM 4764 O O2 . FUL N 4 . ? -11.485 10.301 53.818 1.00 63.33 ? 713 FUL A O2 1 HETATM 4765 C C3 . FUL N 4 . ? -10.907 8.961 51.939 1.00 63.59 ? 713 FUL A C3 1 HETATM 4766 O O3 . FUL N 4 . ? -9.583 8.482 52.016 1.00 64.14 ? 713 FUL A O3 1 HETATM 4767 C C4 . FUL N 4 . ? -11.436 8.862 50.508 1.00 64.02 ? 713 FUL A C4 1 HETATM 4768 O O4 . FUL N 4 . ? -10.431 9.227 49.584 1.00 64.37 ? 713 FUL A O4 1 HETATM 4769 C C5 . FUL N 4 . ? -12.636 9.793 50.362 1.00 63.96 ? 713 FUL A C5 1 HETATM 4770 C C6 . FUL N 4 . ? -13.356 9.579 49.030 1.00 64.35 ? 713 FUL A C6 1 HETATM 4771 O O5 . FUL N 4 . ? -12.190 11.133 50.484 1.00 62.79 ? 713 FUL A O5 1 HETATM 4772 C C1B . XYP O 6 . ? -1.984 10.439 48.310 1.00 51.18 ? 714 XYP A C1B 1 HETATM 4773 C C2B . XYP O 6 . ? -0.966 11.185 49.136 1.00 49.80 ? 714 XYP A C2B 1 HETATM 4774 C C3B . XYP O 6 . ? -0.538 12.472 48.431 1.00 49.04 ? 714 XYP A C3B 1 HETATM 4775 C C4B . XYP O 6 . ? -0.117 12.156 46.998 1.00 49.19 ? 714 XYP A C4B 1 HETATM 4776 C C5B . XYP O 6 . ? -1.252 11.417 46.296 1.00 50.10 ? 714 XYP A C5B 1 HETATM 4777 O O2B . XYP O 6 . ? -1.480 11.473 50.421 1.00 49.01 ? 714 XYP A O2B 1 HETATM 4778 O O3B . XYP O 6 . ? 0.541 13.040 49.131 1.00 47.36 ? 714 XYP A O3B 1 HETATM 4779 O O4B . XYP O 6 . ? 0.188 13.348 46.318 1.00 48.19 ? 714 XYP A O4B 1 HETATM 4780 O O5B . XYP O 6 . ? -1.527 10.240 47.039 1.00 50.68 ? 714 XYP A O5B 1 HETATM 4781 C C2 . BGC P 7 . ? 24.866 25.162 36.951 1.00 26.93 ? 715 BGC A C2 1 HETATM 4782 C C3 . BGC P 7 . ? 24.151 24.018 36.214 1.00 25.76 ? 715 BGC A C3 1 HETATM 4783 C C4 . BGC P 7 . ? 23.662 24.520 34.857 1.00 27.60 ? 715 BGC A C4 1 HETATM 4784 C C5 . BGC P 7 . ? 24.830 25.181 34.083 1.00 29.18 ? 715 BGC A C5 1 HETATM 4785 C C6 . BGC P 7 . ? 24.459 25.633 32.665 1.00 29.18 ? 715 BGC A C6 1 HETATM 4786 C C1 . BGC P 7 . ? 25.929 25.842 36.077 1.00 30.29 ? 715 BGC A C1 1 HETATM 4787 O O1 . BGC P 7 . ? 26.553 26.912 36.797 1.00 31.24 ? 715 BGC A O1 1 HETATM 4788 O O2 . BGC P 7 . ? 25.573 24.635 38.046 1.00 25.18 ? 715 BGC A O2 1 HETATM 4789 O O3 . BGC P 7 . ? 23.046 23.486 36.960 1.00 23.18 ? 715 BGC A O3 1 HETATM 4790 O O4 . BGC P 7 . ? 23.099 23.429 34.165 1.00 25.61 ? 715 BGC A O4 1 HETATM 4791 O O5 . BGC P 7 . ? 25.360 26.279 34.841 1.00 30.95 ? 715 BGC A O5 1 HETATM 4792 O O6 . BGC P 7 . ? 23.706 26.814 32.721 1.00 28.86 ? 715 BGC A O6 1 HETATM 4793 C C2 . 3DO Q 8 . ? 25.522 32.178 32.476 1.00 42.45 ? 716 3DO A C2 1 HETATM 4794 C C3 . 3DO Q 8 . ? 25.431 30.661 32.319 1.00 40.53 ? 716 3DO A C3 1 HETATM 4795 C C4 . 3DO Q 8 . ? 25.228 29.789 33.539 1.00 40.35 ? 716 3DO A C4 1 HETATM 4796 C C5 . 3DO Q 8 . ? 25.380 30.537 34.856 1.00 44.39 ? 716 3DO A C5 1 HETATM 4797 C C6 . 3DO Q 8 . ? 25.907 29.578 35.892 1.00 35.89 ? 716 3DO A C6 1 HETATM 4798 O O1 . 3DO Q 8 . ? 26.531 33.815 33.923 1.00 46.31 ? 716 3DO A O1 1 HETATM 4799 O O6 . 3DO Q 8 . ? 24.915 28.555 36.029 1.00 51.83 ? 716 3DO A O6 1 HETATM 4800 O O5 . 3DO Q 8 . ? 26.259 31.651 34.717 1.00 44.41 ? 716 3DO A O5 1 HETATM 4801 O O4 . 3DO Q 8 . ? 23.902 29.292 33.445 1.00 31.37 ? 716 3DO A O4 1 HETATM 4802 O O2 . 3DO Q 8 . ? 24.408 32.761 31.800 1.00 37.12 ? 716 3DO A O2 1 HETATM 4803 C C1 . 3DO Q 8 . ? 25.664 32.675 33.917 1.00 43.13 ? 716 3DO A C1 1 HETATM 4804 C C1 . GOL R 9 . ? -7.534 17.249 40.446 1.00 57.62 ? 717 GOL A C1 1 HETATM 4805 O O1 . GOL R 9 . ? -6.386 18.011 40.126 1.00 71.10 ? 717 GOL A O1 1 HETATM 4806 C C2 . GOL R 9 . ? -7.239 16.322 41.624 1.00 74.60 ? 717 GOL A C2 1 HETATM 4807 O O2 . GOL R 9 . ? -6.825 17.079 42.737 1.00 60.95 ? 717 GOL A O2 1 HETATM 4808 C C3 . GOL R 9 . ? -6.161 15.315 41.224 1.00 56.62 ? 717 GOL A C3 1 HETATM 4809 O O3 . GOL R 9 . ? -5.693 14.606 42.354 1.00 74.08 ? 717 GOL A O3 1 HETATM 4810 C C1 . GOL S 9 . ? 4.535 12.320 55.176 1.00 50.59 ? 718 GOL A C1 1 HETATM 4811 O O1 . GOL S 9 . ? 4.054 11.698 56.353 1.00 62.62 ? 718 GOL A O1 1 HETATM 4812 C C2 . GOL S 9 . ? 5.304 11.336 54.297 1.00 62.81 ? 718 GOL A C2 1 HETATM 4813 O O2 . GOL S 9 . ? 6.640 11.768 54.143 1.00 53.45 ? 718 GOL A O2 1 HETATM 4814 C C3 . GOL S 9 . ? 4.607 11.256 52.947 1.00 49.03 ? 718 GOL A C3 1 HETATM 4815 O O3 . GOL S 9 . ? 4.792 9.980 52.378 1.00 60.69 ? 718 GOL A O3 1 HETATM 4816 C C1 . GOL T 9 . ? 40.470 10.562 8.933 1.00 54.40 ? 719 GOL A C1 1 HETATM 4817 O O1 . GOL T 9 . ? 40.060 11.273 7.792 1.00 63.20 ? 719 GOL A O1 1 HETATM 4818 C C2 . GOL T 9 . ? 40.369 9.077 8.644 1.00 54.66 ? 719 GOL A C2 1 HETATM 4819 O O2 . GOL T 9 . ? 39.387 8.814 7.661 1.00 58.46 ? 719 GOL A O2 1 HETATM 4820 C C3 . GOL T 9 . ? 39.993 8.398 9.947 1.00 58.57 ? 719 GOL A C3 1 HETATM 4821 O O3 . GOL T 9 . ? 39.807 7.027 9.703 1.00 60.18 ? 719 GOL A O3 1 HETATM 4822 S S . SO4 U 10 . ? 45.612 4.564 22.003 1.00 56.32 ? 720 SO4 A S 1 HETATM 4823 O O1 . SO4 U 10 . ? 45.557 3.978 20.660 1.00 55.64 ? 720 SO4 A O1 1 HETATM 4824 O O2 . SO4 U 10 . ? 46.072 5.958 21.890 1.00 54.40 ? 720 SO4 A O2 1 HETATM 4825 O O3 . SO4 U 10 . ? 44.280 4.483 22.607 1.00 53.57 ? 720 SO4 A O3 1 HETATM 4826 O O4 . SO4 U 10 . ? 46.557 3.801 22.836 1.00 55.24 ? 720 SO4 A O4 1 HETATM 4827 O O . HOH V 11 . ? 9.799 20.666 36.936 1.00 18.34 ? 801 HOH A O 1 HETATM 4828 O O . HOH V 11 . ? 32.512 16.980 14.937 1.00 17.39 ? 802 HOH A O 1 HETATM 4829 O O . HOH V 11 . ? 10.687 22.284 39.053 1.00 16.53 ? 803 HOH A O 1 HETATM 4830 O O . HOH V 11 . ? 13.491 23.374 40.212 1.00 16.95 ? 804 HOH A O 1 HETATM 4831 O O . HOH V 11 . ? 13.284 20.110 36.601 1.00 16.37 ? 805 HOH A O 1 HETATM 4832 O O . HOH V 11 . ? 8.296 25.148 44.641 1.00 16.37 ? 806 HOH A O 1 HETATM 4833 O O . HOH V 11 . ? 27.847 18.322 15.903 1.00 18.33 ? 807 HOH A O 1 HETATM 4834 O O . HOH V 11 . ? 11.724 36.428 36.451 1.00 20.82 ? 808 HOH A O 1 HETATM 4835 O O . HOH V 11 . ? 4.688 32.520 30.800 1.00 22.07 ? 809 HOH A O 1 HETATM 4836 O O . HOH V 11 . ? 16.345 16.694 43.807 1.00 18.70 ? 810 HOH A O 1 HETATM 4837 O O . HOH V 11 . ? 37.681 20.713 16.646 1.00 21.57 ? 811 HOH A O 1 HETATM 4838 O O . HOH V 11 . ? -7.644 33.921 68.485 1.00 39.85 ? 812 HOH A O 1 HETATM 4839 O O . HOH V 11 . ? -0.252 17.573 47.651 1.00 23.94 ? 813 HOH A O 1 HETATM 4840 O O . HOH V 11 . ? 14.980 31.675 44.090 1.00 17.02 ? 814 HOH A O 1 HETATM 4841 O O . HOH V 11 . ? 11.036 21.404 17.326 1.00 20.34 ? 815 HOH A O 1 HETATM 4842 O O . HOH V 11 . ? 50.620 17.340 26.584 1.00 37.13 ? 816 HOH A O 1 HETATM 4843 O O . HOH V 11 . ? -16.671 28.723 61.681 1.00 22.74 ? 817 HOH A O 1 HETATM 4844 O O . HOH V 11 . ? 10.310 21.317 34.270 1.00 16.51 ? 818 HOH A O 1 HETATM 4845 O O . HOH V 11 . ? -14.864 41.151 42.888 1.00 23.01 ? 819 HOH A O 1 HETATM 4846 O O . HOH V 11 . ? 17.442 27.352 48.518 1.00 19.46 ? 820 HOH A O 1 HETATM 4847 O O . HOH V 11 . ? 23.135 15.495 46.700 1.00 20.84 ? 821 HOH A O 1 HETATM 4848 O O . HOH V 11 . ? 5.487 25.758 45.033 1.00 15.91 ? 822 HOH A O 1 HETATM 4849 O O . HOH V 11 . ? 12.412 35.076 58.725 1.00 27.58 ? 823 HOH A O 1 HETATM 4850 O O . HOH V 11 . ? -7.368 32.306 64.335 1.00 26.62 ? 824 HOH A O 1 HETATM 4851 O O . HOH V 11 . ? 34.152 20.414 6.908 1.00 21.32 ? 825 HOH A O 1 HETATM 4852 O O . HOH V 11 . ? 6.409 10.611 28.594 1.00 24.11 ? 826 HOH A O 1 HETATM 4853 O O . HOH V 11 . ? -0.871 21.157 53.683 1.00 19.95 ? 827 HOH A O 1 HETATM 4854 O O . HOH V 11 . ? 4.431 41.233 38.675 1.00 21.28 ? 828 HOH A O 1 HETATM 4855 O O . HOH V 11 . ? -8.421 30.376 42.325 1.00 21.69 ? 829 HOH A O 1 HETATM 4856 O O . HOH V 11 . ? 8.341 32.309 31.133 1.00 18.55 ? 830 HOH A O 1 HETATM 4857 O O . HOH V 11 . ? -11.320 30.681 70.120 1.00 29.30 ? 831 HOH A O 1 HETATM 4858 O O . HOH V 11 . ? 16.233 36.734 29.421 1.00 24.43 ? 832 HOH A O 1 HETATM 4859 O O . HOH V 11 . ? 14.115 35.849 28.140 1.00 20.03 ? 833 HOH A O 1 HETATM 4860 O O . HOH V 11 . ? 16.055 19.081 16.281 1.00 22.34 ? 834 HOH A O 1 HETATM 4861 O O . HOH V 11 . ? 2.491 37.496 43.373 1.00 19.57 ? 835 HOH A O 1 HETATM 4862 O O . HOH V 11 . ? 35.230 29.455 28.766 1.00 22.60 ? 836 HOH A O 1 HETATM 4863 O O . HOH V 11 . ? 19.797 20.442 57.516 1.00 24.40 ? 837 HOH A O 1 HETATM 4864 O O . HOH V 11 . ? -2.060 29.720 20.289 1.00 30.17 ? 838 HOH A O 1 HETATM 4865 O O . HOH V 11 . ? 30.845 16.293 2.715 1.00 31.67 ? 839 HOH A O 1 HETATM 4866 O O . HOH V 11 . ? 13.731 20.656 17.838 1.00 22.90 ? 840 HOH A O 1 HETATM 4867 O O . HOH V 11 . ? -14.056 34.979 56.920 1.00 37.88 ? 841 HOH A O 1 HETATM 4868 O O . HOH V 11 . ? 16.231 34.506 16.198 1.00 30.52 ? 842 HOH A O 1 HETATM 4869 O O . HOH V 11 . ? 21.685 31.384 14.624 1.00 23.13 ? 843 HOH A O 1 HETATM 4870 O O . HOH V 11 . ? 5.351 38.208 65.486 1.00 26.36 ? 844 HOH A O 1 HETATM 4871 O O . HOH V 11 . ? 21.309 33.877 62.474 1.00 50.33 ? 845 HOH A O 1 HETATM 4872 O O . HOH V 11 . ? 15.607 21.838 56.066 1.00 25.00 ? 846 HOH A O 1 HETATM 4873 O O . HOH V 11 . ? 4.832 15.148 15.553 1.00 57.52 ? 847 HOH A O 1 HETATM 4874 O O . HOH V 11 . ? 16.984 38.962 56.538 1.00 44.18 ? 848 HOH A O 1 HETATM 4875 O O . HOH V 11 . ? -4.764 38.113 63.586 1.00 26.10 ? 849 HOH A O 1 HETATM 4876 O O . HOH V 11 . ? 10.844 17.907 12.527 1.00 33.42 ? 850 HOH A O 1 HETATM 4877 O O . HOH V 11 . ? 6.296 34.476 15.574 1.00 52.84 ? 851 HOH A O 1 HETATM 4878 O O . HOH V 11 . ? 19.737 9.852 45.998 1.00 24.69 ? 852 HOH A O 1 HETATM 4879 O O . HOH V 11 . ? -8.081 33.440 35.074 1.00 38.36 ? 853 HOH A O 1 HETATM 4880 O O . HOH V 11 . ? 12.088 18.426 14.839 1.00 27.33 ? 854 HOH A O 1 HETATM 4881 O O . HOH V 11 . ? -10.318 31.796 39.192 1.00 37.05 ? 855 HOH A O 1 HETATM 4882 O O . HOH V 11 . ? 20.687 11.604 44.076 1.00 21.33 ? 856 HOH A O 1 HETATM 4883 O O . HOH V 11 . ? 47.036 13.858 15.454 1.00 49.81 ? 857 HOH A O 1 HETATM 4884 O O . HOH V 11 . ? -15.611 36.985 55.799 1.00 34.39 ? 858 HOH A O 1 HETATM 4885 O O . HOH V 11 . ? -0.750 51.456 52.193 1.00 41.10 ? 859 HOH A O 1 HETATM 4886 O O . HOH V 11 . ? -4.278 19.920 47.145 1.00 30.02 ? 860 HOH A O 1 HETATM 4887 O O . HOH V 11 . ? -5.290 23.688 41.439 1.00 25.18 ? 861 HOH A O 1 HETATM 4888 O O . HOH V 11 . ? 6.452 32.071 17.579 1.00 25.15 ? 862 HOH A O 1 HETATM 4889 O O . HOH V 11 . ? 34.456 2.503 14.800 1.00 34.95 ? 863 HOH A O 1 HETATM 4890 O O . HOH V 11 . ? 12.960 24.268 10.883 1.00 27.12 ? 864 HOH A O 1 HETATM 4891 O O . HOH V 11 . ? -2.831 24.685 14.505 1.00 38.20 ? 865 HOH A O 1 HETATM 4892 O O . HOH V 11 . ? 27.069 33.128 53.201 1.00 40.51 ? 866 HOH A O 1 HETATM 4893 O O . HOH V 11 . ? 19.315 0.621 17.480 1.00 35.36 ? 867 HOH A O 1 HETATM 4894 O O . HOH V 11 . ? -11.100 24.228 57.375 1.00 25.00 ? 868 HOH A O 1 HETATM 4895 O O . HOH V 11 . ? 42.982 12.711 12.473 1.00 27.68 ? 869 HOH A O 1 HETATM 4896 O O . HOH V 11 . ? 25.159 34.564 18.984 1.00 25.87 ? 870 HOH A O 1 HETATM 4897 O O . HOH V 11 . ? -3.487 25.856 63.493 1.00 25.62 ? 871 HOH A O 1 HETATM 4898 O O . HOH V 11 . ? 25.442 14.505 53.405 1.00 29.49 ? 872 HOH A O 1 HETATM 4899 O O . HOH V 11 . ? 35.776 6.987 30.908 1.00 34.13 ? 873 HOH A O 1 HETATM 4900 O O . HOH V 11 . ? 24.263 29.389 60.220 1.00 26.62 ? 874 HOH A O 1 HETATM 4901 O O . HOH V 11 . ? -1.079 27.807 22.231 1.00 28.76 ? 875 HOH A O 1 HETATM 4902 O O . HOH V 11 . ? 24.570 13.444 8.480 1.00 36.19 ? 876 HOH A O 1 HETATM 4903 O O . HOH V 11 . ? 39.468 17.589 10.223 1.00 24.35 ? 877 HOH A O 1 HETATM 4904 O O . HOH V 11 . ? 7.555 34.084 23.601 1.00 27.90 ? 878 HOH A O 1 HETATM 4905 O O . HOH V 11 . ? 42.563 16.367 12.925 1.00 24.10 ? 879 HOH A O 1 HETATM 4906 O O . HOH V 11 . ? 27.655 30.232 52.988 1.00 28.88 ? 880 HOH A O 1 HETATM 4907 O O . HOH V 11 . ? -10.404 46.162 58.731 1.00 24.49 ? 881 HOH A O 1 HETATM 4908 O O . HOH V 11 . ? 35.160 13.579 44.147 1.00 31.58 ? 882 HOH A O 1 HETATM 4909 O O . HOH V 11 . ? 34.800 22.469 8.590 1.00 29.17 ? 883 HOH A O 1 HETATM 4910 O O . HOH V 11 . ? 1.959 38.459 33.232 1.00 29.39 ? 884 HOH A O 1 HETATM 4911 O O . HOH V 11 . ? 17.942 30.905 63.690 1.00 30.66 ? 885 HOH A O 1 HETATM 4912 O O . HOH V 11 . ? -16.133 33.267 56.803 1.00 36.05 ? 886 HOH A O 1 HETATM 4913 O O . HOH V 11 . ? 12.447 38.971 58.604 1.00 30.36 ? 887 HOH A O 1 HETATM 4914 O O . HOH V 11 . ? 9.261 4.891 35.199 1.00 37.31 ? 888 HOH A O 1 HETATM 4915 O O . HOH V 11 . ? 11.089 26.862 12.263 1.00 41.63 ? 889 HOH A O 1 HETATM 4916 O O . HOH V 11 . ? -1.350 39.418 64.969 1.00 36.54 ? 890 HOH A O 1 HETATM 4917 O O . HOH V 11 . ? 13.330 34.802 13.678 1.00 35.67 ? 891 HOH A O 1 HETATM 4918 O O . HOH V 11 . ? -6.506 48.601 45.617 1.00 29.25 ? 892 HOH A O 1 HETATM 4919 O O . HOH V 11 . ? 9.725 43.509 18.742 1.00 33.35 ? 893 HOH A O 1 HETATM 4920 O O . HOH V 11 . ? -7.253 38.823 37.623 1.00 31.26 ? 894 HOH A O 1 HETATM 4921 O O . HOH V 11 . ? 0.128 45.505 64.826 1.00 57.21 ? 895 HOH A O 1 HETATM 4922 O O . HOH V 11 . ? -7.622 46.115 43.614 1.00 52.47 ? 896 HOH A O 1 HETATM 4923 O O . HOH V 11 . ? -5.622 28.040 34.697 1.00 26.94 ? 897 HOH A O 1 HETATM 4924 O O . HOH V 11 . ? -5.548 33.854 70.301 1.00 41.67 ? 898 HOH A O 1 HETATM 4925 O O . HOH V 11 . ? 6.972 44.972 36.579 1.00 33.78 ? 899 HOH A O 1 HETATM 4926 O O . HOH V 11 . ? 32.944 3.427 24.278 1.00 32.72 ? 900 HOH A O 1 HETATM 4927 O O . HOH V 11 . ? 21.987 -0.450 18.415 1.00 31.41 ? 901 HOH A O 1 HETATM 4928 O O . HOH V 11 . ? -7.433 36.292 68.210 1.00 44.80 ? 902 HOH A O 1 HETATM 4929 O O . HOH V 11 . ? -3.202 33.025 32.526 1.00 38.31 ? 903 HOH A O 1 HETATM 4930 O O . HOH V 11 . ? 15.242 27.611 29.795 1.00 16.77 ? 904 HOH A O 1 HETATM 4931 O O . HOH V 11 . ? -22.607 37.415 53.932 1.00 56.32 ? 905 HOH A O 1 HETATM 4932 O O . HOH V 11 . ? 19.181 -3.180 9.092 1.00 61.15 ? 906 HOH A O 1 HETATM 4933 O O . HOH V 11 . ? 15.914 31.756 9.823 1.00 34.45 ? 907 HOH A O 1 HETATM 4934 O O . HOH V 11 . ? 8.633 12.083 19.675 1.00 30.47 ? 908 HOH A O 1 HETATM 4935 O O . HOH V 11 . ? 37.846 5.583 27.973 1.00 27.00 ? 909 HOH A O 1 HETATM 4936 O O . HOH V 11 . ? 47.154 25.998 39.901 1.00 55.76 ? 910 HOH A O 1 HETATM 4937 O O . HOH V 11 . ? 24.185 13.453 2.994 1.00 51.78 ? 911 HOH A O 1 HETATM 4938 O O . HOH V 11 . ? 21.335 -4.160 10.367 1.00 49.07 ? 912 HOH A O 1 HETATM 4939 O O . HOH V 11 . ? 12.183 35.448 39.065 1.00 17.62 ? 913 HOH A O 1 HETATM 4940 O O . HOH V 11 . ? 5.626 20.906 10.641 1.00 39.35 ? 914 HOH A O 1 HETATM 4941 O O . HOH V 11 . ? 1.061 25.523 63.641 1.00 37.63 ? 915 HOH A O 1 HETATM 4942 O O . HOH V 11 . ? 10.275 44.410 46.944 1.00 48.18 ? 916 HOH A O 1 HETATM 4943 O O . HOH V 11 . ? 8.970 11.587 13.906 1.00 51.91 ? 917 HOH A O 1 HETATM 4944 O O . HOH V 11 . ? 9.652 9.236 52.210 1.00 51.75 ? 918 HOH A O 1 HETATM 4945 O O . HOH V 11 . ? 44.414 15.745 10.594 1.00 66.30 ? 919 HOH A O 1 HETATM 4946 O O . HOH V 11 . ? -8.698 42.259 65.285 1.00 77.74 ? 920 HOH A O 1 HETATM 4947 O O . HOH V 11 . ? 18.424 36.006 55.380 1.00 40.77 ? 921 HOH A O 1 HETATM 4948 O O . HOH V 11 . ? 33.759 27.883 7.431 1.00 36.87 ? 922 HOH A O 1 HETATM 4949 O O . HOH V 11 . ? 30.416 9.743 57.245 1.00 41.23 ? 923 HOH A O 1 HETATM 4950 O O . HOH V 11 . ? 30.574 0.437 26.394 1.00 51.50 ? 924 HOH A O 1 HETATM 4951 O O . HOH V 11 . ? 15.604 19.936 38.118 1.00 18.75 ? 925 HOH A O 1 HETATM 4952 O O . HOH V 11 . ? 0.609 25.606 15.026 1.00 51.06 ? 926 HOH A O 1 HETATM 4953 O O . HOH V 11 . ? -1.191 37.622 31.792 1.00 60.33 ? 927 HOH A O 1 HETATM 4954 O O . HOH V 11 . ? 36.485 9.754 6.492 1.00 31.56 ? 928 HOH A O 1 HETATM 4955 O O . HOH V 11 . ? 24.605 37.680 39.721 1.00 43.46 ? 929 HOH A O 1 HETATM 4956 O O . HOH V 11 . ? -15.802 31.357 60.760 1.00 25.91 ? 930 HOH A O 1 HETATM 4957 O O . HOH V 11 . ? 22.070 15.065 58.989 1.00 34.07 ? 931 HOH A O 1 HETATM 4958 O O . HOH V 11 . ? 2.981 38.467 66.788 1.00 34.61 ? 932 HOH A O 1 HETATM 4959 O O . HOH V 11 . ? -11.813 22.161 55.654 1.00 33.88 ? 933 HOH A O 1 HETATM 4960 O O . HOH V 11 . ? 35.125 21.773 39.527 1.00 26.92 ? 934 HOH A O 1 HETATM 4961 O O . HOH V 11 . ? 13.372 11.751 14.971 1.00 30.77 ? 935 HOH A O 1 HETATM 4962 O O . HOH V 11 . ? 40.614 5.631 16.625 1.00 33.31 ? 936 HOH A O 1 HETATM 4963 O O . HOH V 11 . ? 1.877 50.357 50.741 1.00 35.98 ? 937 HOH A O 1 HETATM 4964 O O . HOH V 11 . ? 9.520 41.950 22.578 1.00 64.77 ? 938 HOH A O 1 HETATM 4965 O O . HOH V 11 . ? 19.207 37.531 60.306 1.00 58.00 ? 939 HOH A O 1 HETATM 4966 O O . HOH V 11 . ? -22.988 35.997 43.830 1.00 46.90 ? 940 HOH A O 1 HETATM 4967 O O . HOH V 11 . ? -0.550 52.451 54.892 1.00 35.60 ? 941 HOH A O 1 HETATM 4968 O O . HOH V 11 . ? 6.379 -8.334 30.981 1.00 107.86 ? 942 HOH A O 1 HETATM 4969 O O . HOH V 11 . ? 34.791 4.517 54.837 1.00 60.06 ? 943 HOH A O 1 HETATM 4970 O O . HOH V 11 . ? -8.118 52.402 55.800 1.00 42.37 ? 944 HOH A O 1 HETATM 4971 O O . HOH V 11 . ? 18.959 39.821 27.254 1.00 33.22 ? 945 HOH A O 1 HETATM 4972 O O . HOH V 11 . ? 34.749 6.187 53.001 1.00 39.30 ? 946 HOH A O 1 HETATM 4973 O O . HOH V 11 . ? 39.126 22.880 15.661 1.00 27.37 ? 947 HOH A O 1 HETATM 4974 O O . HOH V 11 . ? 39.378 24.473 47.630 1.00 49.77 ? 948 HOH A O 1 HETATM 4975 O O . HOH V 11 . ? -6.400 33.240 73.032 1.00 75.35 ? 949 HOH A O 1 HETATM 4976 O O . HOH V 11 . ? 19.327 9.965 14.637 1.00 21.44 ? 950 HOH A O 1 HETATM 4977 O O . HOH V 11 . ? 0.178 19.654 25.168 1.00 33.72 ? 951 HOH A O 1 HETATM 4978 O O . HOH V 11 . ? 10.662 11.387 15.868 1.00 27.59 ? 952 HOH A O 1 HETATM 4979 O O . HOH V 11 . ? 39.149 31.139 42.064 1.00 45.39 ? 953 HOH A O 1 HETATM 4980 O O . HOH V 11 . ? -1.681 21.611 49.178 1.00 19.12 ? 954 HOH A O 1 HETATM 4981 O O . HOH V 11 . ? 2.024 8.829 30.820 1.00 47.87 ? 955 HOH A O 1 HETATM 4982 O O . HOH V 11 . ? 31.288 -2.103 31.350 1.00 62.32 ? 956 HOH A O 1 HETATM 4983 O O . HOH V 11 . ? -10.334 19.839 57.813 1.00 50.33 ? 957 HOH A O 1 HETATM 4984 O O . HOH V 11 . ? -9.778 22.874 59.265 1.00 35.97 ? 958 HOH A O 1 HETATM 4985 O O . HOH V 11 . ? 23.909 35.571 29.305 1.00 42.18 ? 959 HOH A O 1 HETATM 4986 O O . HOH V 11 . ? 37.374 28.203 30.105 1.00 27.76 ? 960 HOH A O 1 HETATM 4987 O O . HOH V 11 . ? -7.491 26.090 27.398 1.00 27.08 ? 961 HOH A O 1 HETATM 4988 O O . HOH V 11 . ? 15.124 1.324 50.382 1.00 61.53 ? 962 HOH A O 1 HETATM 4989 O O . HOH V 11 . ? 49.880 15.872 36.050 1.00 55.29 ? 963 HOH A O 1 HETATM 4990 O O . HOH V 11 . ? 7.542 25.659 30.100 1.00 16.58 ? 964 HOH A O 1 HETATM 4991 O O . HOH V 11 . ? 29.950 30.361 54.616 1.00 32.48 ? 965 HOH A O 1 HETATM 4992 O O . HOH V 11 . ? 19.709 24.255 37.279 1.00 23.33 ? 966 HOH A O 1 HETATM 4993 O O . HOH V 11 . ? 41.326 23.411 43.914 1.00 37.91 ? 967 HOH A O 1 HETATM 4994 O O . HOH V 11 . ? -1.311 32.835 34.152 1.00 22.80 ? 968 HOH A O 1 HETATM 4995 O O . HOH V 11 . ? 7.403 28.601 51.506 1.00 17.84 ? 969 HOH A O 1 HETATM 4996 O O . HOH V 11 . ? 8.857 28.773 40.205 1.00 15.61 ? 970 HOH A O 1 HETATM 4997 O O . HOH V 11 . ? 2.948 27.750 38.272 1.00 16.56 ? 971 HOH A O 1 HETATM 4998 O O . HOH V 11 . ? 34.662 19.291 40.616 1.00 19.97 ? 972 HOH A O 1 HETATM 4999 O O . HOH V 11 . ? 32.852 16.927 9.616 1.00 19.13 ? 973 HOH A O 1 HETATM 5000 O O . HOH V 11 . ? 11.453 18.823 38.203 1.00 16.98 ? 974 HOH A O 1 HETATM 5001 O O . HOH V 11 . ? 13.506 32.849 46.106 1.00 17.60 ? 975 HOH A O 1 HETATM 5002 O O . HOH V 11 . ? 12.740 20.054 33.869 1.00 16.83 ? 976 HOH A O 1 HETATM 5003 O O . HOH V 11 . ? 12.005 28.579 62.118 1.00 21.07 ? 977 HOH A O 1 HETATM 5004 O O . HOH V 11 . ? 22.450 34.067 19.039 1.00 21.95 ? 978 HOH A O 1 HETATM 5005 O O . HOH V 11 . ? 11.939 34.303 24.858 1.00 18.81 ? 979 HOH A O 1 HETATM 5006 O O . HOH V 11 . ? 29.785 21.199 13.760 1.00 18.50 ? 980 HOH A O 1 HETATM 5007 O O . HOH V 11 . ? 31.689 17.125 12.148 1.00 20.30 ? 981 HOH A O 1 HETATM 5008 O O . HOH V 11 . ? 36.134 24.929 30.551 1.00 20.75 ? 982 HOH A O 1 HETATM 5009 O O . HOH V 11 . ? 16.290 31.283 33.569 1.00 21.08 ? 983 HOH A O 1 HETATM 5010 O O . HOH V 11 . ? 20.073 27.907 30.736 1.00 16.58 ? 984 HOH A O 1 HETATM 5011 O O . HOH V 11 . ? 20.798 36.959 36.506 1.00 21.15 ? 985 HOH A O 1 HETATM 5012 O O . HOH V 11 . ? -8.810 24.608 50.997 1.00 23.56 ? 986 HOH A O 1 HETATM 5013 O O . HOH V 11 . ? 20.662 36.429 33.475 1.00 23.03 ? 987 HOH A O 1 HETATM 5014 O O . HOH V 11 . ? 13.327 8.086 29.724 1.00 20.23 ? 988 HOH A O 1 HETATM 5015 O O . HOH V 11 . ? 7.952 17.903 16.107 1.00 25.50 ? 989 HOH A O 1 HETATM 5016 O O . HOH V 11 . ? 16.069 22.335 39.490 1.00 20.67 ? 990 HOH A O 1 HETATM 5017 O O . HOH V 11 . ? 27.006 26.504 41.293 1.00 22.74 ? 991 HOH A O 1 HETATM 5018 O O . HOH V 11 . ? 29.324 18.662 12.389 1.00 19.24 ? 992 HOH A O 1 HETATM 5019 O O . HOH V 11 . ? 11.667 34.698 45.157 1.00 18.06 ? 993 HOH A O 1 HETATM 5020 O O . HOH V 11 . ? 5.530 15.306 26.038 1.00 23.62 ? 994 HOH A O 1 HETATM 5021 O O . HOH V 11 . ? 19.946 27.722 42.811 1.00 21.32 ? 995 HOH A O 1 HETATM 5022 O O . HOH V 11 . ? 3.363 42.864 45.894 1.00 23.08 ? 996 HOH A O 1 HETATM 5023 O O . HOH V 11 . ? 22.829 15.074 42.494 1.00 23.91 ? 997 HOH A O 1 HETATM 5024 O O . HOH V 11 . ? 34.729 23.311 41.709 1.00 23.08 ? 998 HOH A O 1 HETATM 5025 O O . HOH V 11 . ? 10.380 18.728 17.015 1.00 23.81 ? 999 HOH A O 1 HETATM 5026 O O . HOH V 11 . ? -8.268 32.615 40.588 1.00 22.96 ? 1000 HOH A O 1 HETATM 5027 O O . HOH V 11 . ? 23.948 13.686 44.662 1.00 22.86 ? 1001 HOH A O 1 HETATM 5028 O O . HOH V 11 . ? 14.006 35.904 25.452 1.00 22.54 ? 1002 HOH A O 1 HETATM 5029 O O . HOH V 11 . ? -2.815 31.050 37.453 1.00 21.76 ? 1003 HOH A O 1 HETATM 5030 O O . HOH V 11 . ? 18.308 11.204 52.309 1.00 24.36 ? 1004 HOH A O 1 HETATM 5031 O O . HOH V 11 . ? 42.721 25.569 35.655 1.00 24.16 ? 1005 HOH A O 1 HETATM 5032 O O . HOH V 11 . ? 6.025 43.009 52.556 1.00 22.51 ? 1006 HOH A O 1 HETATM 5033 O O . HOH V 11 . ? 34.298 23.070 31.982 1.00 19.07 ? 1007 HOH A O 1 HETATM 5034 O O . HOH V 11 . ? 25.137 21.213 49.533 1.00 22.59 ? 1008 HOH A O 1 HETATM 5035 O O . HOH V 11 . ? 12.322 38.024 27.864 1.00 23.24 ? 1009 HOH A O 1 HETATM 5036 O O . HOH V 11 . ? 14.977 20.804 49.129 1.00 22.29 ? 1010 HOH A O 1 HETATM 5037 O O . HOH V 11 . ? -3.488 46.744 62.218 1.00 30.97 ? 1011 HOH A O 1 HETATM 5038 O O . HOH V 11 . ? 9.660 34.922 60.834 1.00 26.16 ? 1012 HOH A O 1 HETATM 5039 O O . HOH V 11 . ? -12.813 33.262 37.308 1.00 22.60 ? 1013 HOH A O 1 HETATM 5040 O O . HOH V 11 . ? -14.823 29.027 50.645 1.00 30.25 ? 1014 HOH A O 1 HETATM 5041 O O . HOH V 11 . ? 18.757 33.100 61.963 1.00 26.06 ? 1015 HOH A O 1 HETATM 5042 O O . HOH V 11 . ? 24.853 19.840 53.113 1.00 25.41 ? 1016 HOH A O 1 HETATM 5043 O O . HOH V 11 . ? 34.075 25.907 42.627 1.00 25.28 ? 1017 HOH A O 1 HETATM 5044 O O . HOH V 11 . ? 20.914 5.843 31.477 1.00 24.64 ? 1018 HOH A O 1 HETATM 5045 O O . HOH V 11 . ? 18.847 38.028 29.337 1.00 25.09 ? 1019 HOH A O 1 HETATM 5046 O O . HOH V 11 . ? 27.632 21.585 39.974 1.00 23.03 ? 1020 HOH A O 1 HETATM 5047 O O . HOH V 11 . ? 25.816 28.266 53.045 1.00 25.31 ? 1021 HOH A O 1 HETATM 5048 O O . HOH V 11 . ? 26.398 24.023 42.314 1.00 23.86 ? 1022 HOH A O 1 HETATM 5049 O O . HOH V 11 . ? 26.076 21.058 56.613 1.00 27.02 ? 1023 HOH A O 1 HETATM 5050 O O . HOH V 11 . ? 35.470 29.506 36.661 1.00 30.05 ? 1024 HOH A O 1 HETATM 5051 O O . HOH V 11 . ? 36.711 19.191 6.419 1.00 25.81 ? 1025 HOH A O 1 HETATM 5052 O O . HOH V 11 . ? -12.313 49.006 59.964 1.00 26.85 ? 1026 HOH A O 1 HETATM 5053 O O . HOH V 11 . ? 17.801 22.933 14.875 1.00 25.32 ? 1027 HOH A O 1 HETATM 5054 O O . HOH V 11 . ? 28.733 30.697 50.343 1.00 26.86 ? 1028 HOH A O 1 HETATM 5055 O O . HOH V 11 . ? -15.754 43.520 54.993 1.00 24.14 ? 1029 HOH A O 1 HETATM 5056 O O . HOH V 11 . ? 6.283 18.302 63.731 1.00 32.75 ? 1030 HOH A O 1 HETATM 5057 O O . HOH V 11 . ? 9.518 39.700 52.454 1.00 28.22 ? 1031 HOH A O 1 HETATM 5058 O O . HOH V 11 . ? 27.866 21.832 43.029 1.00 23.79 ? 1032 HOH A O 1 HETATM 5059 O O . HOH V 11 . ? 14.299 13.303 17.091 1.00 25.02 ? 1033 HOH A O 1 HETATM 5060 O O . HOH V 11 . ? -7.208 17.726 51.927 1.00 30.22 ? 1034 HOH A O 1 HETATM 5061 O O . HOH V 11 . ? 27.362 22.210 45.705 1.00 23.34 ? 1035 HOH A O 1 HETATM 5062 O O . HOH V 11 . ? -12.432 44.980 43.639 1.00 26.13 ? 1036 HOH A O 1 HETATM 5063 O O . HOH V 11 . ? 47.838 21.881 20.443 1.00 24.01 ? 1037 HOH A O 1 HETATM 5064 O O . HOH V 11 . ? -16.701 30.754 48.989 1.00 29.83 ? 1038 HOH A O 1 HETATM 5065 O O . HOH V 11 . ? -13.193 31.376 59.996 1.00 25.74 ? 1039 HOH A O 1 HETATM 5066 O O . HOH V 11 . ? 23.726 14.297 55.559 1.00 30.47 ? 1040 HOH A O 1 HETATM 5067 O O . HOH V 11 . ? -12.974 31.882 57.031 1.00 23.52 ? 1041 HOH A O 1 HETATM 5068 O O . HOH V 11 . ? 1.250 15.568 49.583 1.00 27.49 ? 1042 HOH A O 1 HETATM 5069 O O . HOH V 11 . ? 27.112 31.083 41.671 1.00 28.45 ? 1043 HOH A O 1 HETATM 5070 O O . HOH V 11 . ? 23.917 -0.180 30.172 1.00 25.90 ? 1044 HOH A O 1 HETATM 5071 O O . HOH V 11 . ? 2.966 26.468 16.132 1.00 33.44 ? 1045 HOH A O 1 HETATM 5072 O O . HOH V 11 . ? 15.672 22.017 16.510 1.00 25.58 ? 1046 HOH A O 1 HETATM 5073 O O . HOH V 11 . ? 16.687 38.873 43.708 1.00 31.04 ? 1047 HOH A O 1 HETATM 5074 O O . HOH V 11 . ? 6.004 32.623 20.973 1.00 26.74 ? 1048 HOH A O 1 HETATM 5075 O O . HOH V 11 . ? -18.512 33.096 49.980 1.00 30.97 ? 1049 HOH A O 1 HETATM 5076 O O . HOH V 11 . ? 22.985 21.337 51.357 1.00 27.94 ? 1050 HOH A O 1 HETATM 5077 O O . HOH V 11 . ? -12.506 40.812 41.517 1.00 24.36 ? 1051 HOH A O 1 HETATM 5078 O O . HOH V 11 . ? 30.237 3.065 25.178 1.00 31.96 ? 1052 HOH A O 1 HETATM 5079 O O . HOH V 11 . ? 34.947 21.843 45.346 1.00 29.42 ? 1053 HOH A O 1 HETATM 5080 O O . HOH V 11 . ? 44.744 28.665 22.475 1.00 35.91 ? 1054 HOH A O 1 HETATM 5081 O O . HOH V 11 . ? 6.112 8.147 27.021 1.00 32.65 ? 1055 HOH A O 1 HETATM 5082 O O . HOH V 11 . ? 43.214 26.484 16.529 1.00 55.51 ? 1056 HOH A O 1 HETATM 5083 O O . HOH V 11 . ? 15.878 36.956 49.926 1.00 25.76 ? 1057 HOH A O 1 HETATM 5084 O O . HOH V 11 . ? 14.297 18.275 11.180 1.00 30.00 ? 1058 HOH A O 1 HETATM 5085 O O . HOH V 11 . ? -19.830 40.967 49.111 1.00 27.59 ? 1059 HOH A O 1 HETATM 5086 O O . HOH V 11 . ? -17.850 36.633 54.098 1.00 25.58 ? 1060 HOH A O 1 HETATM 5087 O O . HOH V 11 . ? 7.250 43.528 45.163 1.00 24.30 ? 1061 HOH A O 1 HETATM 5088 O O . HOH V 11 . ? 27.984 14.739 5.009 1.00 27.00 ? 1062 HOH A O 1 HETATM 5089 O O . HOH V 11 . ? 22.394 0.705 36.207 1.00 27.46 ? 1063 HOH A O 1 HETATM 5090 O O . HOH V 11 . ? -4.309 42.980 39.632 1.00 32.41 ? 1064 HOH A O 1 HETATM 5091 O O . HOH V 11 . ? 14.492 23.758 50.109 1.00 28.34 ? 1065 HOH A O 1 HETATM 5092 O O . HOH V 11 . ? 15.595 15.816 17.015 1.00 24.14 ? 1066 HOH A O 1 HETATM 5093 O O . HOH V 11 . ? 17.057 19.665 56.766 1.00 31.51 ? 1067 HOH A O 1 HETATM 5094 O O . HOH V 11 . ? 30.454 33.015 10.429 1.00 31.57 ? 1068 HOH A O 1 HETATM 5095 O O . HOH V 11 . ? 23.755 23.015 5.939 1.00 32.35 ? 1069 HOH A O 1 HETATM 5096 O O . HOH V 11 . ? 6.102 14.774 23.401 1.00 26.17 ? 1070 HOH A O 1 HETATM 5097 O O . HOH V 11 . ? -1.611 15.540 53.163 1.00 28.59 ? 1071 HOH A O 1 HETATM 5098 O O . HOH V 11 . ? 22.371 1.426 21.062 1.00 31.06 ? 1072 HOH A O 1 HETATM 5099 O O . HOH V 11 . ? 17.000 11.929 56.130 1.00 37.15 ? 1073 HOH A O 1 HETATM 5100 O O . HOH V 11 . ? 45.899 2.808 33.001 1.00 39.26 ? 1074 HOH A O 1 HETATM 5101 O O . HOH V 11 . ? 47.454 24.721 23.426 1.00 32.82 ? 1075 HOH A O 1 HETATM 5102 O O . HOH V 11 . ? 37.427 3.463 23.374 1.00 31.77 ? 1076 HOH A O 1 HETATM 5103 O O . HOH V 11 . ? 31.964 4.442 -4.260 1.00 30.09 ? 1077 HOH A O 1 HETATM 5104 O O . HOH V 11 . ? 25.256 18.752 55.509 1.00 33.22 ? 1078 HOH A O 1 HETATM 5105 O O . HOH V 11 . ? 33.985 3.626 9.539 1.00 33.16 ? 1079 HOH A O 1 HETATM 5106 O O . HOH V 11 . ? 11.108 39.446 29.961 1.00 27.30 ? 1080 HOH A O 1 HETATM 5107 O O . HOH V 11 . ? 29.211 -0.258 11.656 1.00 32.77 ? 1081 HOH A O 1 HETATM 5108 O O . HOH V 11 . ? 40.795 17.183 43.386 1.00 31.49 ? 1082 HOH A O 1 HETATM 5109 O O . HOH V 11 . ? 33.842 33.142 18.716 1.00 27.87 ? 1083 HOH A O 1 HETATM 5110 O O . HOH V 11 . ? 47.215 9.885 22.295 1.00 26.75 ? 1084 HOH A O 1 HETATM 5111 O O . HOH V 11 . ? 15.841 36.878 17.487 1.00 26.99 ? 1085 HOH A O 1 HETATM 5112 O O . HOH V 11 . ? -9.653 50.896 51.698 1.00 47.12 ? 1086 HOH A O 1 HETATM 5113 O O . HOH V 11 . ? 32.797 26.590 47.632 1.00 28.07 ? 1087 HOH A O 1 HETATM 5114 O O . HOH V 11 . ? -11.382 17.777 49.927 1.00 49.63 ? 1088 HOH A O 1 HETATM 5115 O O . HOH V 11 . ? 1.720 16.981 30.492 1.00 29.28 ? 1089 HOH A O 1 HETATM 5116 O O . HOH V 11 . ? -15.008 39.537 59.105 1.00 36.54 ? 1090 HOH A O 1 HETATM 5117 O O . HOH V 11 . ? 8.692 35.572 15.366 1.00 27.09 ? 1091 HOH A O 1 HETATM 5118 O O . HOH V 11 . ? 18.657 3.248 43.853 1.00 30.64 ? 1092 HOH A O 1 HETATM 5119 O O . HOH V 11 . ? -0.491 52.874 61.891 1.00 33.85 ? 1093 HOH A O 1 HETATM 5120 O O . HOH V 11 . ? -6.615 31.945 30.761 1.00 26.64 ? 1094 HOH A O 1 HETATM 5121 O O . HOH V 11 . ? -13.256 28.211 56.991 1.00 31.46 ? 1095 HOH A O 1 HETATM 5122 O O . HOH V 11 . ? 25.654 33.040 42.239 1.00 31.63 ? 1096 HOH A O 1 HETATM 5123 O O . HOH V 11 . ? 16.134 7.859 14.080 1.00 32.51 ? 1097 HOH A O 1 HETATM 5124 O O . HOH V 11 . ? 35.861 32.540 22.633 1.00 33.50 ? 1098 HOH A O 1 HETATM 5125 O O . HOH V 11 . ? -5.313 19.250 59.497 1.00 37.01 ? 1099 HOH A O 1 HETATM 5126 O O . HOH V 11 . ? 36.156 30.008 12.697 1.00 34.48 ? 1100 HOH A O 1 HETATM 5127 O O . HOH V 11 . ? 42.233 19.503 16.500 1.00 24.65 ? 1101 HOH A O 1 HETATM 5128 O O . HOH V 11 . ? 29.849 17.906 54.227 1.00 31.65 ? 1102 HOH A O 1 HETATM 5129 O O . HOH V 11 . ? 20.134 36.967 43.202 1.00 31.25 ? 1103 HOH A O 1 HETATM 5130 O O . HOH V 11 . ? 41.030 18.984 10.093 1.00 30.59 ? 1104 HOH A O 1 HETATM 5131 O O . HOH V 11 . ? -1.032 15.805 56.021 1.00 31.52 ? 1105 HOH A O 1 HETATM 5132 O O . HOH V 11 . ? -11.088 30.191 43.065 1.00 33.53 ? 1106 HOH A O 1 HETATM 5133 O O . HOH V 11 . ? 0.757 49.549 47.421 1.00 33.69 ? 1107 HOH A O 1 HETATM 5134 O O . HOH V 11 . ? 4.240 11.853 26.437 1.00 37.69 ? 1108 HOH A O 1 HETATM 5135 O O . HOH V 11 . ? 6.330 28.586 66.577 1.00 33.19 ? 1109 HOH A O 1 HETATM 5136 O O . HOH V 11 . ? -6.957 58.725 61.381 1.00 32.49 ? 1110 HOH A O 1 HETATM 5137 O O . HOH V 11 . ? 36.013 27.738 41.936 1.00 27.49 ? 1111 HOH A O 1 HETATM 5138 O O . HOH V 11 . ? 33.336 3.273 28.537 1.00 28.53 ? 1112 HOH A O 1 HETATM 5139 O O . HOH V 11 . ? 0.916 16.633 59.780 1.00 31.37 ? 1113 HOH A O 1 HETATM 5140 O O . HOH V 11 . ? 19.398 34.339 50.271 1.00 32.55 ? 1114 HOH A O 1 HETATM 5141 O O . HOH V 11 . ? 8.538 6.173 24.627 1.00 31.16 ? 1115 HOH A O 1 HETATM 5142 O O . HOH V 11 . ? 4.420 30.347 20.602 1.00 33.45 ? 1116 HOH A O 1 HETATM 5143 O O . HOH V 11 . ? -7.529 52.734 63.064 1.00 35.27 ? 1117 HOH A O 1 HETATM 5144 O O . HOH V 11 . ? 34.692 8.256 5.049 1.00 31.71 ? 1118 HOH A O 1 HETATM 5145 O O . HOH V 11 . ? 28.080 34.279 29.289 1.00 30.67 ? 1119 HOH A O 1 HETATM 5146 O O . HOH V 11 . ? -6.814 23.096 58.748 1.00 26.44 ? 1120 HOH A O 1 HETATM 5147 O O . HOH V 11 . ? 20.428 3.309 21.588 1.00 29.28 ? 1121 HOH A O 1 HETATM 5148 O O . HOH V 11 . ? 36.951 3.695 15.185 1.00 35.04 ? 1122 HOH A O 1 HETATM 5149 O O . HOH V 11 . ? 6.943 11.056 46.554 1.00 31.93 ? 1123 HOH A O 1 HETATM 5150 O O . HOH V 11 . ? 34.670 25.750 45.396 1.00 31.84 ? 1124 HOH A O 1 HETATM 5151 O O . HOH V 11 . ? 14.272 8.637 18.830 1.00 33.59 ? 1125 HOH A O 1 HETATM 5152 O O . HOH V 11 . ? 39.009 29.886 33.532 1.00 35.41 ? 1126 HOH A O 1 HETATM 5153 O O . HOH V 11 . ? 4.500 46.240 61.882 1.00 31.61 ? 1127 HOH A O 1 HETATM 5154 O O . HOH V 11 . ? 29.199 1.631 18.703 1.00 33.04 ? 1128 HOH A O 1 HETATM 5155 O O . HOH V 11 . ? 7.439 39.602 17.372 1.00 49.27 ? 1129 HOH A O 1 HETATM 5156 O O . HOH V 11 . ? 2.863 14.953 26.164 1.00 31.81 ? 1130 HOH A O 1 HETATM 5157 O O . HOH V 11 . ? -4.164 14.611 52.625 1.00 35.69 ? 1131 HOH A O 1 HETATM 5158 O O . HOH V 11 . ? 29.866 1.893 30.644 1.00 29.46 ? 1132 HOH A O 1 HETATM 5159 O O . HOH V 11 . ? 24.105 31.499 13.261 1.00 29.28 ? 1133 HOH A O 1 HETATM 5160 O O . HOH V 11 . ? -22.698 38.976 43.599 1.00 34.03 ? 1134 HOH A O 1 HETATM 5161 O O . HOH V 11 . ? 29.213 2.352 5.263 1.00 36.87 ? 1135 HOH A O 1 HETATM 5162 O O . HOH V 11 . ? 8.335 7.136 41.309 1.00 32.51 ? 1136 HOH A O 1 HETATM 5163 O O . HOH V 11 . ? 19.303 11.664 58.522 1.00 32.76 ? 1137 HOH A O 1 HETATM 5164 O O . HOH V 11 . ? 18.555 -3.599 33.040 1.00 37.63 ? 1138 HOH A O 1 HETATM 5165 O O . HOH V 11 . ? 38.766 19.999 46.473 1.00 30.36 ? 1139 HOH A O 1 HETATM 5166 O O . HOH V 11 . ? 11.500 36.883 60.332 1.00 34.27 ? 1140 HOH A O 1 HETATM 5167 O O . HOH V 11 . ? 40.467 3.662 20.357 1.00 36.60 ? 1141 HOH A O 1 HETATM 5168 O O . HOH V 11 . ? 24.776 -2.284 29.094 1.00 39.02 ? 1142 HOH A O 1 HETATM 5169 O O . HOH V 11 . ? 18.668 39.051 37.383 1.00 36.88 ? 1143 HOH A O 1 HETATM 5170 O O . HOH V 11 . ? -3.547 29.635 33.963 1.00 29.63 ? 1144 HOH A O 1 HETATM 5171 O O . HOH V 11 . ? 37.309 9.474 45.557 1.00 35.25 ? 1145 HOH A O 1 HETATM 5172 O O . HOH V 11 . ? 13.995 39.967 33.459 1.00 36.10 ? 1146 HOH A O 1 HETATM 5173 O O . HOH V 11 . ? 38.303 16.706 52.914 1.00 38.93 ? 1147 HOH A O 1 HETATM 5174 O O . HOH V 11 . ? 4.429 44.909 44.435 1.00 32.73 ? 1148 HOH A O 1 HETATM 5175 O O . HOH V 11 . ? 10.787 27.430 68.446 1.00 32.64 ? 1149 HOH A O 1 HETATM 5176 O O . HOH V 11 . ? -11.033 44.730 60.734 1.00 45.54 ? 1150 HOH A O 1 HETATM 5177 O O . HOH V 11 . ? 2.098 50.065 61.495 1.00 36.90 ? 1151 HOH A O 1 HETATM 5178 O O . HOH V 11 . ? -12.288 19.952 44.488 1.00 37.91 ? 1152 HOH A O 1 HETATM 5179 O O . HOH V 11 . ? 5.465 31.243 66.895 1.00 30.90 ? 1153 HOH A O 1 HETATM 5180 O O . HOH V 11 . ? -17.088 44.660 43.861 1.00 36.33 ? 1154 HOH A O 1 HETATM 5181 O O . HOH V 11 . ? 19.495 9.391 23.744 1.00 31.89 ? 1155 HOH A O 1 HETATM 5182 O O . HOH V 11 . ? 41.067 9.987 14.927 1.00 34.80 ? 1156 HOH A O 1 HETATM 5183 O O . HOH V 11 . ? 18.918 4.363 13.567 1.00 39.56 ? 1157 HOH A O 1 HETATM 5184 O O . HOH V 11 . ? 37.725 29.137 14.794 1.00 30.03 ? 1158 HOH A O 1 HETATM 5185 O O . HOH V 11 . ? 1.767 30.013 66.170 1.00 34.91 ? 1159 HOH A O 1 HETATM 5186 O O . HOH V 11 . ? 31.961 3.893 54.438 1.00 36.36 ? 1160 HOH A O 1 HETATM 5187 O O . HOH V 11 . ? -8.509 28.040 29.337 1.00 31.20 ? 1161 HOH A O 1 HETATM 5188 O O . HOH V 11 . ? -5.688 23.296 36.984 1.00 34.83 ? 1162 HOH A O 1 HETATM 5189 O O . HOH V 11 . ? 43.606 13.554 9.861 1.00 39.97 ? 1163 HOH A O 1 HETATM 5190 O O . HOH V 11 . ? 30.534 16.227 45.951 1.00 31.26 ? 1164 HOH A O 1 HETATM 5191 O O . HOH V 11 . ? 37.734 3.327 17.857 1.00 41.85 ? 1165 HOH A O 1 HETATM 5192 O O . HOH V 11 . ? -17.875 44.266 56.539 1.00 38.31 ? 1166 HOH A O 1 HETATM 5193 O O . HOH V 11 . ? 20.893 20.636 6.032 1.00 38.45 ? 1167 HOH A O 1 HETATM 5194 O O . HOH V 11 . ? 23.223 6.263 3.369 1.00 43.87 ? 1168 HOH A O 1 HETATM 5195 O O . HOH V 11 . ? 4.539 8.242 37.043 1.00 31.05 ? 1169 HOH A O 1 HETATM 5196 O O . HOH V 11 . ? 23.905 16.605 56.920 1.00 34.43 ? 1170 HOH A O 1 HETATM 5197 O O . HOH V 11 . ? -3.503 13.356 50.224 1.00 38.00 ? 1171 HOH A O 1 HETATM 5198 O O . HOH V 11 . ? 18.862 3.019 23.889 1.00 30.15 ? 1172 HOH A O 1 HETATM 5199 O O . HOH V 11 . ? 46.679 17.920 15.297 1.00 32.84 ? 1173 HOH A O 1 HETATM 5200 O O . HOH V 11 . ? 36.745 9.244 49.927 1.00 37.77 ? 1174 HOH A O 1 HETATM 5201 O O . HOH V 11 . ? 23.661 29.356 9.337 1.00 39.31 ? 1175 HOH A O 1 HETATM 5202 O O . HOH V 11 . ? 29.252 33.695 26.826 1.00 32.57 ? 1176 HOH A O 1 HETATM 5203 O O . HOH V 11 . ? -5.355 52.559 64.649 1.00 36.77 ? 1177 HOH A O 1 HETATM 5204 O O . HOH V 11 . ? 36.398 32.565 53.003 1.00 64.99 ? 1178 HOH A O 1 HETATM 5205 O O . HOH V 11 . ? 4.396 34.693 20.262 1.00 38.65 ? 1179 HOH A O 1 HETATM 5206 O O . HOH V 11 . ? 24.930 34.353 54.854 1.00 39.32 ? 1180 HOH A O 1 HETATM 5207 O O . HOH V 11 . ? 11.334 5.129 40.855 1.00 44.01 ? 1181 HOH A O 1 HETATM 5208 O O . HOH V 11 . ? -9.669 18.691 47.203 1.00 42.72 ? 1182 HOH A O 1 HETATM 5209 O O . HOH V 11 . ? -9.269 51.994 53.711 1.00 54.44 ? 1183 HOH A O 1 HETATM 5210 O O . HOH V 11 . ? 40.613 5.007 27.579 1.00 34.45 ? 1184 HOH A O 1 HETATM 5211 O O . HOH V 11 . ? 31.737 2.958 18.649 1.00 37.96 ? 1185 HOH A O 1 HETATM 5212 O O . HOH V 11 . ? 26.061 -0.989 24.199 1.00 53.99 ? 1186 HOH A O 1 HETATM 5213 O O . HOH V 11 . ? 41.663 12.716 36.750 1.00 35.31 ? 1187 HOH A O 1 HETATM 5214 O O . HOH V 11 . ? -0.928 37.123 67.295 1.00 34.43 ? 1188 HOH A O 1 HETATM 5215 O O . HOH V 11 . ? -14.024 31.460 41.826 1.00 29.82 ? 1189 HOH A O 1 HETATM 5216 O O . HOH V 11 . ? 25.478 34.135 49.267 1.00 33.67 ? 1190 HOH A O 1 HETATM 5217 O O . HOH V 11 . ? 18.309 -1.452 26.151 1.00 44.66 ? 1191 HOH A O 1 HETATM 5218 O O . HOH V 11 . ? -6.014 41.730 37.866 1.00 40.87 ? 1192 HOH A O 1 HETATM 5219 O O . HOH V 11 . ? -4.706 26.001 71.910 1.00 49.70 ? 1193 HOH A O 1 HETATM 5220 O O . HOH V 11 . ? -3.178 14.276 56.993 1.00 43.33 ? 1194 HOH A O 1 HETATM 5221 O O . HOH V 11 . ? -20.821 39.898 51.469 1.00 37.71 ? 1195 HOH A O 1 HETATM 5222 O O . HOH V 11 . ? 38.536 26.706 42.310 1.00 37.09 ? 1196 HOH A O 1 HETATM 5223 O O . HOH V 11 . ? 31.396 36.225 18.224 1.00 51.20 ? 1197 HOH A O 1 HETATM 5224 O O . HOH V 11 . ? 17.821 38.429 41.376 1.00 40.71 ? 1198 HOH A O 1 HETATM 5225 O O . HOH V 11 . ? 46.299 13.902 10.644 1.00 38.97 ? 1199 HOH A O 1 HETATM 5226 O O . HOH V 11 . ? -10.516 47.675 63.510 1.00 39.69 ? 1200 HOH A O 1 HETATM 5227 O O . HOH V 11 . ? 1.149 14.695 57.750 1.00 39.82 ? 1201 HOH A O 1 HETATM 5228 O O . HOH V 11 . ? 11.424 6.086 46.744 1.00 38.61 ? 1202 HOH A O 1 HETATM 5229 O O . HOH V 11 . ? 39.873 8.957 41.227 1.00 36.05 ? 1203 HOH A O 1 HETATM 5230 O O . HOH V 11 . ? -17.035 45.318 58.848 1.00 43.66 ? 1204 HOH A O 1 HETATM 5231 O O . HOH V 11 . ? -6.480 36.303 65.712 1.00 38.06 ? 1205 HOH A O 1 HETATM 5232 O O . HOH V 11 . ? 33.204 29.187 48.761 1.00 38.80 ? 1206 HOH A O 1 HETATM 5233 O O . HOH V 11 . ? 32.641 29.528 42.047 1.00 46.36 ? 1207 HOH A O 1 HETATM 5234 O O . HOH V 11 . ? 24.297 29.039 62.985 1.00 37.28 ? 1208 HOH A O 1 HETATM 5235 O O . HOH V 11 . ? 16.271 2.245 46.750 1.00 39.37 ? 1209 HOH A O 1 HETATM 5236 O O . HOH V 11 . ? -0.327 19.403 30.144 1.00 38.83 ? 1210 HOH A O 1 HETATM 5237 O O . HOH V 11 . ? 17.978 7.376 6.070 1.00 42.80 ? 1211 HOH A O 1 HETATM 5238 O O . HOH V 11 . ? -8.374 26.277 65.259 1.00 40.89 ? 1212 HOH A O 1 HETATM 5239 O O . HOH V 11 . ? 40.004 26.747 17.371 1.00 36.69 ? 1213 HOH A O 1 HETATM 5240 O O . HOH V 11 . ? 1.865 21.766 18.406 1.00 36.93 ? 1214 HOH A O 1 HETATM 5241 O O . HOH V 11 . ? 22.646 -2.615 33.205 1.00 37.24 ? 1215 HOH A O 1 HETATM 5242 O O . HOH V 11 . ? 21.073 38.399 45.414 1.00 36.28 ? 1216 HOH A O 1 HETATM 5243 O O . HOH V 11 . ? 45.195 24.009 42.179 1.00 41.96 ? 1217 HOH A O 1 HETATM 5244 O O . HOH V 11 . ? 2.576 32.441 26.349 1.00 39.98 ? 1218 HOH A O 1 HETATM 5245 O O . HOH V 11 . ? 14.278 2.280 39.278 1.00 37.82 ? 1219 HOH A O 1 HETATM 5246 O O . HOH V 11 . ? 15.319 31.214 65.336 1.00 56.64 ? 1220 HOH A O 1 HETATM 5247 O O . HOH V 11 . ? 23.976 19.731 63.415 1.00 33.95 ? 1221 HOH A O 1 HETATM 5248 O O . HOH V 11 . ? 12.862 37.219 62.710 1.00 43.77 ? 1222 HOH A O 1 HETATM 5249 O O . HOH V 11 . ? 6.620 6.215 33.999 1.00 37.46 ? 1223 HOH A O 1 HETATM 5250 O O . HOH V 11 . ? 45.341 14.752 13.132 1.00 33.30 ? 1224 HOH A O 1 HETATM 5251 O O . HOH V 11 . ? 9.163 45.121 40.639 1.00 39.49 ? 1225 HOH A O 1 HETATM 5252 O O . HOH V 11 . ? 4.588 26.397 66.237 1.00 39.72 ? 1226 HOH A O 1 HETATM 5253 O O . HOH V 11 . ? 34.995 34.310 20.955 1.00 32.39 ? 1227 HOH A O 1 HETATM 5254 O O . HOH V 11 . ? 26.069 34.623 16.519 1.00 33.39 ? 1228 HOH A O 1 HETATM 5255 O O . HOH V 11 . ? -1.705 43.234 39.102 1.00 44.33 ? 1229 HOH A O 1 HETATM 5256 O O . HOH V 11 . ? 8.047 34.325 67.784 1.00 42.19 ? 1230 HOH A O 1 HETATM 5257 O O . HOH V 11 . ? -11.322 43.256 41.882 1.00 28.01 ? 1231 HOH A O 1 HETATM 5258 O O . HOH V 11 . ? 31.228 32.632 33.072 1.00 38.49 ? 1232 HOH A O 1 HETATM 5259 O O . HOH V 11 . ? 1.671 17.618 27.833 1.00 44.18 ? 1233 HOH A O 1 HETATM 5260 O O . HOH V 11 . ? 0.379 41.638 64.927 1.00 30.89 ? 1234 HOH A O 1 HETATM 5261 O O . HOH V 11 . ? 28.039 0.764 -1.953 1.00 45.06 ? 1235 HOH A O 1 HETATM 5262 O O . HOH V 11 . ? 16.012 43.046 55.117 1.00 42.17 ? 1236 HOH A O 1 HETATM 5263 O O . HOH V 11 . ? 54.960 13.258 24.468 1.00 40.84 ? 1237 HOH A O 1 HETATM 5264 O O . HOH V 11 . ? -7.419 55.569 59.561 1.00 56.47 ? 1238 HOH A O 1 HETATM 5265 O O . HOH V 11 . ? -3.817 12.920 54.815 1.00 47.30 ? 1239 HOH A O 1 HETATM 5266 O O . HOH V 11 . ? 30.270 28.565 57.064 1.00 44.29 ? 1240 HOH A O 1 HETATM 5267 O O . HOH V 11 . ? 18.717 1.863 20.058 1.00 39.26 ? 1241 HOH A O 1 HETATM 5268 O O . HOH V 11 . ? 23.172 31.898 10.736 1.00 41.46 ? 1242 HOH A O 1 HETATM 5269 O O . HOH V 11 . ? 5.791 43.626 41.138 1.00 40.12 ? 1243 HOH A O 1 HETATM 5270 O O . HOH V 11 . ? 34.429 23.472 53.970 1.00 46.28 ? 1244 HOH A O 1 HETATM 5271 O O . HOH V 11 . ? 18.545 10.297 8.019 1.00 37.53 ? 1245 HOH A O 1 HETATM 5272 O O . HOH V 11 . ? 7.659 28.035 68.843 1.00 39.52 ? 1246 HOH A O 1 HETATM 5273 O O . HOH V 11 . ? 35.419 8.932 54.792 1.00 45.98 ? 1247 HOH A O 1 HETATM 5274 O O . HOH V 11 . ? -18.971 23.117 52.295 1.00 39.59 ? 1248 HOH A O 1 HETATM 5275 O O . HOH V 11 . ? -7.676 27.275 31.963 1.00 34.61 ? 1249 HOH A O 1 HETATM 5276 O O . HOH V 11 . ? 18.126 20.948 68.787 1.00 43.99 ? 1250 HOH A O 1 HETATM 5277 O O . HOH V 11 . ? 37.448 11.185 47.913 1.00 34.43 ? 1251 HOH A O 1 HETATM 5278 O O . HOH V 11 . ? 47.921 21.862 39.162 1.00 56.78 ? 1252 HOH A O 1 HETATM 5279 O O . HOH V 11 . ? -1.180 12.847 39.612 1.00 36.62 ? 1253 HOH A O 1 HETATM 5280 O O . HOH V 11 . ? -0.543 15.787 45.692 1.00 36.93 ? 1254 HOH A O 1 HETATM 5281 O O . HOH V 11 . ? 37.640 31.352 16.433 1.00 39.68 ? 1255 HOH A O 1 HETATM 5282 O O . HOH V 11 . ? -5.214 31.672 34.117 1.00 35.43 ? 1256 HOH A O 1 HETATM 5283 O O . HOH V 11 . ? 2.843 17.084 19.836 1.00 68.21 ? 1257 HOH A O 1 HETATM 5284 O O . HOH V 11 . ? 43.765 28.811 14.380 1.00 41.17 ? 1258 HOH A O 1 HETATM 5285 O O . HOH V 11 . ? 33.351 33.905 13.105 1.00 34.66 ? 1259 HOH A O 1 HETATM 5286 O O . HOH V 11 . ? 5.572 36.932 44.697 1.00 29.12 ? 1260 HOH A O 1 HETATM 5287 O O . HOH V 11 . ? 24.496 25.629 62.389 1.00 32.25 ? 1261 HOH A O 1 HETATM 5288 O O . HOH V 11 . ? 18.733 9.248 54.206 1.00 37.55 ? 1262 HOH A O 1 HETATM 5289 O O . HOH V 11 . ? 33.740 1.768 17.333 1.00 36.51 ? 1263 HOH A O 1 HETATM 5290 O O . HOH V 11 . ? 7.037 37.333 67.511 1.00 40.10 ? 1264 HOH A O 1 HETATM 5291 O O . HOH V 11 . ? 3.473 47.754 57.413 1.00 41.91 ? 1265 HOH A O 1 HETATM 5292 O O . HOH V 11 . ? 30.738 0.504 9.437 1.00 40.45 ? 1266 HOH A O 1 HETATM 5293 O O . HOH V 11 . ? 30.500 33.844 30.659 1.00 34.93 ? 1267 HOH A O 1 HETATM 5294 O O . HOH V 11 . ? -9.103 18.065 56.071 1.00 36.41 ? 1268 HOH A O 1 HETATM 5295 O O . HOH V 11 . ? -12.295 41.222 61.918 1.00 32.38 ? 1269 HOH A O 1 HETATM 5296 O O . HOH V 11 . ? 37.622 22.509 51.799 1.00 54.62 ? 1270 HOH A O 1 HETATM 5297 O O . HOH V 11 . ? 2.588 45.721 42.262 1.00 35.04 ? 1271 HOH A O 1 HETATM 5298 O O . HOH V 11 . ? 22.907 36.062 31.831 1.00 43.51 ? 1272 HOH A O 1 HETATM 5299 O O . HOH V 11 . ? 33.260 19.538 3.166 1.00 38.16 ? 1273 HOH A O 1 HETATM 5300 O O . HOH V 11 . ? -7.327 30.187 33.000 1.00 31.15 ? 1274 HOH A O 1 HETATM 5301 O O . HOH V 11 . ? 22.708 -2.632 4.172 1.00 60.01 ? 1275 HOH A O 1 HETATM 5302 O O . HOH V 11 . ? 20.698 2.647 45.913 1.00 43.87 ? 1276 HOH A O 1 HETATM 5303 O O . HOH V 11 . ? 23.201 3.775 45.980 1.00 35.60 ? 1277 HOH A O 1 HETATM 5304 O O . HOH V 11 . ? -0.608 33.026 67.500 1.00 41.62 ? 1278 HOH A O 1 HETATM 5305 O O . HOH V 11 . ? 23.545 7.243 55.703 1.00 51.48 ? 1279 HOH A O 1 HETATM 5306 O O . HOH V 11 . ? 2.866 48.960 45.490 1.00 38.69 ? 1280 HOH A O 1 HETATM 5307 O O . HOH V 11 . ? 12.758 8.194 16.863 1.00 45.59 ? 1281 HOH A O 1 HETATM 5308 O O . HOH V 11 . ? -10.314 24.519 32.580 1.00 63.61 ? 1282 HOH A O 1 HETATM 5309 O O . HOH V 11 . ? 45.847 28.010 32.656 1.00 37.98 ? 1283 HOH A O 1 HETATM 5310 O O . HOH V 11 . ? -4.260 19.767 35.298 1.00 43.06 ? 1284 HOH A O 1 HETATM 5311 O O . HOH V 11 . ? 12.286 2.198 33.680 1.00 39.51 ? 1285 HOH A O 1 HETATM 5312 O O . HOH V 11 . ? -2.467 38.515 34.574 1.00 57.78 ? 1286 HOH A O 1 HETATM 5313 O O . HOH V 11 . ? 9.827 4.711 31.703 1.00 47.27 ? 1287 HOH A O 1 HETATM 5314 O O . HOH V 11 . ? 27.168 35.732 46.539 1.00 43.99 ? 1288 HOH A O 1 HETATM 5315 O O . HOH V 11 . ? 22.642 14.192 65.450 1.00 55.00 ? 1289 HOH A O 1 HETATM 5316 O O . HOH V 11 . ? 2.980 6.816 34.976 1.00 52.52 ? 1290 HOH A O 1 HETATM 5317 O O . HOH V 11 . ? 35.645 32.685 12.607 1.00 39.34 ? 1291 HOH A O 1 HETATM 5318 O O . HOH V 11 . ? -19.285 38.734 55.082 1.00 45.71 ? 1292 HOH A O 1 HETATM 5319 O O . HOH V 11 . ? -16.315 47.315 54.896 1.00 33.41 ? 1293 HOH A O 1 HETATM 5320 O O . HOH V 11 . ? 22.932 42.467 42.974 1.00 71.93 ? 1294 HOH A O 1 HETATM 5321 O O . HOH V 11 . ? 38.250 6.254 14.434 1.00 39.04 ? 1295 HOH A O 1 HETATM 5322 O O . HOH V 11 . ? 31.398 4.075 3.034 1.00 41.35 ? 1296 HOH A O 1 HETATM 5323 O O . HOH V 11 . ? 6.050 45.464 63.767 1.00 48.42 ? 1297 HOH A O 1 HETATM 5324 O O . HOH V 11 . ? 23.163 37.910 37.262 1.00 39.89 ? 1298 HOH A O 1 HETATM 5325 O O . HOH V 11 . ? 29.065 30.771 37.366 1.00 42.79 ? 1299 HOH A O 1 HETATM 5326 O O . HOH V 11 . ? -3.330 56.041 64.393 1.00 62.02 ? 1300 HOH A O 1 HETATM 5327 O O . HOH V 11 . ? -8.421 16.942 49.731 1.00 49.62 ? 1301 HOH A O 1 HETATM 5328 O O . HOH V 11 . ? 13.253 4.282 47.438 1.00 39.30 ? 1302 HOH A O 1 HETATM 5329 O O . HOH V 11 . ? 23.106 12.151 63.801 1.00 51.98 ? 1303 HOH A O 1 HETATM 5330 O O . HOH V 11 . ? 27.002 30.131 60.605 1.00 49.13 ? 1304 HOH A O 1 HETATM 5331 O O . HOH V 11 . ? 34.835 3.508 22.028 1.00 37.15 ? 1305 HOH A O 1 HETATM 5332 O O . HOH V 11 . ? -1.374 30.480 26.263 1.00 38.20 ? 1306 HOH A O 1 HETATM 5333 O O . HOH V 11 . ? 10.917 19.154 68.069 1.00 43.98 ? 1307 HOH A O 1 HETATM 5334 O O . HOH V 11 . ? 12.399 8.993 12.204 1.00 51.36 ? 1308 HOH A O 1 HETATM 5335 O O . HOH V 11 . ? 8.845 43.705 62.845 1.00 45.44 ? 1309 HOH A O 1 HETATM 5336 O O . HOH V 11 . ? 12.074 25.140 71.839 1.00 54.96 ? 1310 HOH A O 1 HETATM 5337 O O . HOH V 11 . ? 51.086 16.777 30.259 1.00 53.00 ? 1311 HOH A O 1 HETATM 5338 O O . HOH V 11 . ? 47.323 10.972 17.549 1.00 57.02 ? 1312 HOH A O 1 HETATM 5339 O O . HOH V 11 . ? 2.449 40.926 66.366 1.00 43.47 ? 1313 HOH A O 1 HETATM 5340 O O . HOH V 11 . ? 8.788 5.305 22.108 1.00 37.66 ? 1314 HOH A O 1 HETATM 5341 O O . HOH V 11 . ? 4.357 18.433 13.743 1.00 44.53 ? 1315 HOH A O 1 HETATM 5342 O O . HOH V 11 . ? 9.117 41.087 65.979 1.00 43.11 ? 1316 HOH A O 1 HETATM 5343 O O . HOH V 11 . ? -5.953 22.122 61.240 1.00 44.47 ? 1317 HOH A O 1 HETATM 5344 O O . HOH V 11 . ? 10.272 12.359 62.358 1.00 49.86 ? 1318 HOH A O 1 HETATM 5345 O O . HOH V 11 . ? -2.288 52.147 50.200 1.00 52.15 ? 1319 HOH A O 1 HETATM 5346 O O . HOH V 11 . ? 16.678 25.730 68.740 1.00 49.76 ? 1320 HOH A O 1 HETATM 5347 O O . HOH V 11 . ? -15.675 29.373 53.330 1.00 47.79 ? 1321 HOH A O 1 HETATM 5348 O O . HOH V 11 . ? -20.358 34.667 51.996 1.00 42.28 ? 1322 HOH A O 1 HETATM 5349 O O . HOH V 11 . ? 39.142 1.824 21.923 1.00 40.95 ? 1323 HOH A O 1 HETATM 5350 O O . HOH V 11 . ? 6.811 32.420 68.968 1.00 42.83 ? 1324 HOH A O 1 HETATM 5351 O O . HOH V 11 . ? -14.236 53.168 51.079 1.00 63.28 ? 1325 HOH A O 1 HETATM 5352 O O . HOH V 11 . ? 42.717 10.223 36.418 1.00 53.79 ? 1326 HOH A O 1 HETATM 5353 O O . HOH V 11 . ? -16.582 21.568 53.548 1.00 52.43 ? 1327 HOH A O 1 HETATM 5354 O O . HOH V 11 . ? 29.893 2.004 50.612 1.00 47.98 ? 1328 HOH A O 1 HETATM 5355 O O . HOH V 11 . ? 46.952 6.542 18.815 1.00 46.71 ? 1329 HOH A O 1 HETATM 5356 O O . HOH V 11 . ? 18.133 4.323 54.978 1.00 72.06 ? 1330 HOH A O 1 HETATM 5357 O O . HOH V 11 . ? 3.689 25.591 11.175 1.00 54.45 ? 1331 HOH A O 1 HETATM 5358 O O . HOH V 11 . ? 28.142 20.603 58.176 1.00 44.47 ? 1332 HOH A O 1 HETATM 5359 O O . HOH V 11 . ? 21.716 13.311 8.824 1.00 42.75 ? 1333 HOH A O 1 HETATM 5360 O O . HOH V 11 . ? 4.877 40.415 30.491 1.00 54.09 ? 1334 HOH A O 1 HETATM 5361 O O . HOH V 11 . ? 22.928 2.083 49.608 1.00 54.29 ? 1335 HOH A O 1 HETATM 5362 O O . HOH V 11 . ? -13.061 25.117 65.524 1.00 39.46 ? 1336 HOH A O 1 HETATM 5363 O O . HOH V 11 . ? -12.218 52.240 54.454 1.00 45.71 ? 1337 HOH A O 1 HETATM 5364 O O . HOH V 11 . ? 9.710 41.400 28.704 1.00 52.73 ? 1338 HOH A O 1 HETATM 5365 O O . HOH V 11 . ? 11.825 20.199 10.788 1.00 45.23 ? 1339 HOH A O 1 HETATM 5366 O O . HOH V 11 . ? 14.419 28.234 10.963 1.00 38.14 ? 1340 HOH A O 1 HETATM 5367 O O . HOH V 11 . ? 31.701 16.809 0.280 1.00 58.38 ? 1341 HOH A O 1 HETATM 5368 O O . HOH V 11 . ? 7.398 9.602 48.923 1.00 42.30 ? 1342 HOH A O 1 HETATM 5369 O O . HOH V 11 . ? 31.536 29.613 44.429 1.00 61.03 ? 1343 HOH A O 1 HETATM 5370 O O . HOH V 11 . ? 40.084 5.027 38.719 1.00 47.28 ? 1344 HOH A O 1 HETATM 5371 O O . HOH V 11 . ? -1.340 25.017 64.644 1.00 35.59 ? 1345 HOH A O 1 HETATM 5372 O O . HOH V 11 . ? 24.365 17.292 5.963 1.00 50.33 ? 1346 HOH A O 1 HETATM 5373 O O . HOH V 11 . ? 3.785 50.976 56.895 1.00 55.79 ? 1347 HOH A O 1 HETATM 5374 O O . HOH V 11 . ? 6.172 47.321 57.184 1.00 43.71 ? 1348 HOH A O 1 HETATM 5375 O O . HOH V 11 . ? 25.879 28.288 7.580 1.00 44.33 ? 1349 HOH A O 1 HETATM 5376 O O . HOH V 11 . ? 34.210 34.678 16.381 1.00 42.65 ? 1350 HOH A O 1 HETATM 5377 O O . HOH V 11 . ? 5.651 12.382 22.070 1.00 45.07 ? 1351 HOH A O 1 HETATM 5378 O O . HOH V 11 . ? 6.426 29.689 11.177 1.00 37.53 ? 1352 HOH A O 1 HETATM 5379 O O . HOH V 11 . ? 6.195 28.674 13.795 1.00 34.58 ? 1353 HOH A O 1 HETATM 5380 O O . HOH V 11 . ? 34.764 31.522 30.236 1.00 35.03 ? 1354 HOH A O 1 HETATM 5381 O O . HOH V 11 . ? 18.633 6.745 53.245 1.00 51.81 ? 1355 HOH A O 1 HETATM 5382 O O . HOH V 11 . ? 17.052 29.611 10.503 1.00 37.07 ? 1356 HOH A O 1 HETATM 5383 O O . HOH V 11 . ? 26.394 7.277 -0.289 1.00 44.64 ? 1357 HOH A O 1 HETATM 5384 O O . HOH V 11 . ? 7.998 45.939 49.788 1.00 42.21 ? 1358 HOH A O 1 HETATM 5385 O O . HOH V 11 . ? 5.102 30.791 15.352 1.00 33.38 ? 1359 HOH A O 1 HETATM 5386 O O . HOH V 11 . ? 9.415 12.803 59.638 1.00 45.76 ? 1360 HOH A O 1 HETATM 5387 O O . HOH V 11 . ? 2.247 27.422 65.023 1.00 35.89 ? 1361 HOH A O 1 HETATM 5388 O O . HOH V 11 . ? 25.367 2.464 51.429 1.00 50.33 ? 1362 HOH A O 1 HETATM 5389 O O . HOH V 11 . ? 20.298 30.538 65.373 1.00 44.62 ? 1363 HOH A O 1 HETATM 5390 O O . HOH V 11 . ? 32.709 -0.864 17.112 1.00 53.53 ? 1364 HOH A O 1 HETATM 5391 O O . HOH V 11 . ? 16.955 1.343 42.532 1.00 64.02 ? 1365 HOH A O 1 HETATM 5392 O O . HOH V 11 . ? 12.573 33.352 66.128 1.00 45.66 ? 1366 HOH A O 1 HETATM 5393 O O . HOH V 11 . ? 10.802 43.550 35.611 1.00 51.24 ? 1367 HOH A O 1 HETATM 5394 O O . HOH V 11 . ? 2.294 47.083 63.424 1.00 53.88 ? 1368 HOH A O 1 HETATM 5395 O O . HOH V 11 . ? 16.301 41.546 40.277 1.00 39.24 ? 1369 HOH A O 1 HETATM 5396 O O . HOH V 11 . ? 3.984 15.882 63.356 1.00 48.06 ? 1370 HOH A O 1 HETATM 5397 O O . HOH V 11 . ? 22.765 41.036 45.120 1.00 47.78 ? 1371 HOH A O 1 HETATM 5398 O O . HOH V 11 . ? 5.349 23.842 65.911 1.00 45.58 ? 1372 HOH A O 1 HETATM 5399 O O . HOH V 11 . ? -17.571 30.943 58.394 1.00 43.33 ? 1373 HOH A O 1 HETATM 5400 O O . HOH V 11 . ? 1.969 30.111 22.505 1.00 40.40 ? 1374 HOH A O 1 HETATM 5401 O O . HOH V 11 . ? 31.220 33.163 47.853 1.00 52.57 ? 1375 HOH A O 1 HETATM 5402 O O . HOH V 11 . ? 38.398 25.137 44.784 1.00 43.36 ? 1376 HOH A O 1 HETATM 5403 O O . HOH V 11 . ? 35.739 5.345 5.568 1.00 48.19 ? 1377 HOH A O 1 HETATM 5404 O O . HOH V 11 . ? 24.348 -4.033 31.423 1.00 45.68 ? 1378 HOH A O 1 HETATM 5405 O O . HOH V 11 . ? -15.338 30.817 55.814 1.00 43.84 ? 1379 HOH A O 1 HETATM 5406 O O . HOH V 11 . ? 28.385 -2.284 15.868 1.00 56.80 ? 1380 HOH A O 1 HETATM 5407 O O . HOH V 11 . ? -6.376 21.807 39.576 1.00 43.16 ? 1381 HOH A O 1 HETATM 5408 O O . HOH V 11 . ? 8.500 -1.730 23.465 1.00 68.60 ? 1382 HOH A O 1 HETATM 5409 O O . HOH V 11 . ? 24.401 22.011 64.845 1.00 47.87 ? 1383 HOH A O 1 HETATM 5410 O O . HOH V 11 . ? 38.083 23.358 9.471 1.00 50.36 ? 1384 HOH A O 1 HETATM 5411 O O . HOH V 11 . ? 9.147 41.914 26.256 1.00 60.63 ? 1385 HOH A O 1 HETATM 5412 O O . HOH V 11 . ? -0.652 17.712 62.284 1.00 64.03 ? 1386 HOH A O 1 HETATM 5413 O O . HOH V 11 . ? -0.972 41.280 34.076 1.00 52.57 ? 1387 HOH A O 1 HETATM 5414 O O . HOH V 11 . ? 36.117 6.445 50.318 1.00 51.84 ? 1388 HOH A O 1 HETATM 5415 O O . HOH V 11 . ? 27.180 24.730 60.787 1.00 42.93 ? 1389 HOH A O 1 HETATM 5416 O O . HOH V 11 . ? -8.340 27.567 73.155 1.00 49.18 ? 1390 HOH A O 1 HETATM 5417 O O . HOH V 11 . ? 27.283 17.679 4.964 1.00 38.83 ? 1391 HOH A O 1 HETATM 5418 O O . HOH V 11 . ? 28.680 35.245 39.479 1.00 54.58 ? 1392 HOH A O 1 HETATM 5419 O O . HOH V 11 . ? 14.952 5.812 20.846 1.00 52.43 ? 1393 HOH A O 1 HETATM 5420 O O . HOH V 11 . ? 13.163 40.427 60.744 1.00 44.48 ? 1394 HOH A O 1 HETATM 5421 O O . HOH V 11 . ? -10.642 27.867 32.552 1.00 44.01 ? 1395 HOH A O 1 HETATM 5422 O O . HOH V 11 . ? 21.324 24.078 68.548 1.00 53.13 ? 1396 HOH A O 1 HETATM 5423 O O . HOH V 11 . ? -17.074 28.903 47.049 1.00 43.82 ? 1397 HOH A O 1 HETATM 5424 O O . HOH V 11 . ? 23.443 2.578 43.165 1.00 46.92 ? 1398 HOH A O 1 HETATM 5425 O O . HOH V 11 . ? -14.323 23.152 53.935 1.00 47.36 ? 1399 HOH A O 1 HETATM 5426 O O . HOH V 11 . ? 26.794 19.011 62.605 1.00 49.95 ? 1400 HOH A O 1 HETATM 5427 O O . HOH V 11 . ? 40.046 20.511 50.007 1.00 65.31 ? 1401 HOH A O 1 HETATM 5428 O O . HOH V 11 . ? -1.094 30.722 67.853 1.00 41.07 ? 1402 HOH A O 1 HETATM 5429 O O . HOH V 11 . ? 33.278 3.769 44.720 1.00 61.18 ? 1403 HOH A O 1 HETATM 5430 O O . HOH V 11 . ? 52.870 8.898 22.369 1.00 64.46 ? 1404 HOH A O 1 HETATM 5431 O O . HOH V 11 . ? 15.711 -0.493 33.155 1.00 48.55 ? 1405 HOH A O 1 HETATM 5432 O O . HOH V 11 . ? 30.905 35.868 26.023 1.00 50.58 ? 1406 HOH A O 1 HETATM 5433 O O . HOH V 11 . ? 18.716 0.373 24.330 1.00 42.63 ? 1407 HOH A O 1 HETATM 5434 O O . HOH V 11 . ? -2.263 16.683 32.961 1.00 40.83 ? 1408 HOH A O 1 HETATM 5435 O O . HOH V 11 . ? 39.738 9.418 43.877 1.00 49.98 ? 1409 HOH A O 1 HETATM 5436 O O . HOH V 11 . ? 3.848 7.173 39.330 1.00 44.12 ? 1410 HOH A O 1 HETATM 5437 O O . HOH V 11 . ? 36.288 3.354 27.843 1.00 45.72 ? 1411 HOH A O 1 HETATM 5438 O O . HOH V 11 . ? 26.598 35.789 40.955 1.00 58.71 ? 1412 HOH A O 1 HETATM 5439 O O . HOH V 11 . ? 9.007 1.991 31.083 1.00 45.30 ? 1413 HOH A O 1 HETATM 5440 O O . HOH V 11 . ? -13.050 23.272 40.999 1.00 71.24 ? 1414 HOH A O 1 HETATM 5441 O O . HOH V 11 . ? -15.620 49.370 49.426 1.00 56.03 ? 1415 HOH A O 1 HETATM 5442 O O . HOH V 11 . ? 10.402 5.988 19.965 1.00 46.24 ? 1416 HOH A O 1 HETATM 5443 O O . HOH V 11 . ? 5.916 49.654 50.198 1.00 54.83 ? 1417 HOH A O 1 HETATM 5444 O O . HOH V 11 . ? 23.389 12.737 57.780 1.00 52.49 ? 1418 HOH A O 1 HETATM 5445 O O . HOH V 11 . ? 5.190 8.522 45.999 1.00 52.12 ? 1419 HOH A O 1 HETATM 5446 O O . HOH V 11 . ? 27.499 7.532 57.002 1.00 48.33 ? 1420 HOH A O 1 HETATM 5447 O O . HOH V 11 . ? 32.340 22.011 59.432 1.00 67.92 ? 1421 HOH A O 1 HETATM 5448 O O . HOH V 11 . ? 34.098 2.663 42.102 1.00 60.77 ? 1422 HOH A O 1 HETATM 5449 O O . HOH V 11 . ? -0.966 46.993 41.584 1.00 63.86 ? 1423 HOH A O 1 HETATM 5450 O O . HOH V 11 . ? 34.008 1.449 11.081 1.00 51.00 ? 1424 HOH A O 1 HETATM 5451 O O . HOH V 11 . ? 29.944 1.047 1.681 1.00 51.23 ? 1425 HOH A O 1 HETATM 5452 O O . HOH V 11 . ? -3.966 25.383 67.559 1.00 60.55 ? 1426 HOH A O 1 HETATM 5453 O O . HOH V 11 . ? 28.393 28.484 37.551 1.00 60.23 ? 1427 HOH A O 1 HETATM 5454 O O . HOH V 11 . ? 49.046 18.854 31.977 1.00 43.93 ? 1428 HOH A O 1 HETATM 5455 O O . HOH V 11 . ? -5.315 46.477 42.573 1.00 47.88 ? 1429 HOH A O 1 HETATM 5456 O O . HOH V 11 . ? 19.897 4.119 50.340 1.00 61.24 ? 1430 HOH A O 1 HETATM 5457 O O . HOH V 11 . ? 35.295 24.757 7.520 1.00 42.11 ? 1431 HOH A O 1 HETATM 5458 O O . HOH V 11 . ? 2.409 8.707 41.203 1.00 53.31 ? 1432 HOH A O 1 HETATM 5459 O O . HOH V 11 . ? 9.446 2.970 24.502 1.00 47.29 ? 1433 HOH A O 1 HETATM 5460 O O . HOH V 11 . ? 43.048 3.514 19.689 1.00 51.46 ? 1434 HOH A O 1 HETATM 5461 O O . HOH V 11 . ? 45.221 13.473 36.141 1.00 68.97 ? 1435 HOH A O 1 HETATM 5462 O O . HOH V 11 . ? 1.827 33.576 20.755 1.00 44.83 ? 1436 HOH A O 1 HETATM 5463 O O . HOH V 11 . ? 31.101 2.457 56.485 1.00 55.22 ? 1437 HOH A O 1 HETATM 5464 O O . HOH V 11 . ? 50.865 11.642 17.757 1.00 52.70 ? 1438 HOH A O 1 HETATM 5465 O O . HOH V 11 . ? 31.488 1.526 52.691 1.00 63.19 ? 1439 HOH A O 1 HETATM 5466 O O . HOH V 11 . ? 41.687 17.529 51.881 1.00 80.34 ? 1440 HOH A O 1 HETATM 5467 O O . HOH V 11 . ? 44.133 1.987 23.534 1.00 58.46 ? 1441 HOH A O 1 HETATM 5468 O O . HOH V 11 . ? -5.319 23.867 63.412 1.00 55.25 ? 1442 HOH A O 1 HETATM 5469 O O . HOH V 11 . ? 7.389 -2.055 25.785 1.00 69.28 ? 1443 HOH A O 1 HETATM 5470 O O . HOH V 11 . ? -4.079 50.774 48.785 1.00 35.80 ? 1444 HOH A O 1 HETATM 5471 O O . HOH V 11 . ? 23.952 -1.235 40.613 1.00 72.35 ? 1445 HOH A O 1 HETATM 5472 O O . HOH V 11 . ? 41.713 29.810 31.569 1.00 59.81 ? 1446 HOH A O 1 HETATM 5473 O O . HOH V 11 . ? 18.263 -2.060 37.186 1.00 48.57 ? 1447 HOH A O 1 HETATM 5474 O O . HOH V 11 . ? 1.402 32.496 23.829 1.00 52.86 ? 1448 HOH A O 1 HETATM 5475 O O . HOH V 11 . ? -0.051 29.302 24.129 1.00 45.78 ? 1449 HOH A O 1 HETATM 5476 O O . HOH V 11 . ? -24.327 40.824 44.521 1.00 48.22 ? 1450 HOH A O 1 HETATM 5477 O O . HOH V 11 . ? 33.476 35.390 26.144 1.00 51.55 ? 1451 HOH A O 1 HETATM 5478 O O . HOH V 11 . ? -1.091 27.361 67.019 1.00 57.90 ? 1452 HOH A O 1 HETATM 5479 O O . HOH V 11 . ? 4.098 34.941 17.232 1.00 47.02 ? 1453 HOH A O 1 HETATM 5480 O O . HOH V 11 . ? 2.918 21.652 65.962 1.00 67.63 ? 1454 HOH A O 1 HETATM 5481 O O . HOH V 11 . ? -8.852 32.877 70.546 1.00 49.99 ? 1455 HOH A O 1 HETATM 5482 O O . HOH V 11 . ? 21.036 10.785 7.146 1.00 46.30 ? 1456 HOH A O 1 HETATM 5483 O O . HOH V 11 . ? 29.829 -2.080 13.527 1.00 70.78 ? 1457 HOH A O 1 HETATM 5484 O O . HOH V 11 . ? 36.975 2.007 25.765 1.00 56.55 ? 1458 HOH A O 1 HETATM 5485 O O . HOH V 11 . ? 48.571 6.987 23.679 1.00 50.87 ? 1459 HOH A O 1 HETATM 5486 O O . HOH V 11 . ? 6.933 41.093 24.883 1.00 55.49 ? 1460 HOH A O 1 HETATM 5487 O O . HOH V 11 . ? 7.226 6.408 43.824 1.00 50.74 ? 1461 HOH A O 1 HETATM 5488 O O . HOH V 11 . ? 43.533 10.737 14.244 1.00 58.79 ? 1462 HOH A O 1 HETATM 5489 O O . HOH V 11 . ? 29.141 -3.135 29.576 1.00 69.32 ? 1463 HOH A O 1 HETATM 5490 O O . HOH V 11 . ? -17.031 28.637 44.198 1.00 45.87 ? 1464 HOH A O 1 HETATM 5491 O O . HOH V 11 . ? 40.037 21.045 8.664 1.00 49.08 ? 1465 HOH A O 1 HETATM 5492 O O . HOH V 11 . ? 6.292 6.399 39.975 1.00 55.88 ? 1466 HOH A O 1 HETATM 5493 O O . HOH V 11 . ? 6.960 38.452 22.734 1.00 53.59 ? 1467 HOH A O 1 HETATM 5494 O O . HOH V 11 . ? 19.250 16.696 7.019 1.00 56.43 ? 1468 HOH A O 1 HETATM 5495 O O . HOH V 11 . ? 4.393 48.632 59.998 1.00 54.92 ? 1469 HOH A O 1 HETATM 5496 O O . HOH V 11 . ? 36.395 33.243 50.702 1.00 59.57 ? 1470 HOH A O 1 HETATM 5497 O O . HOH V 11 . ? 7.202 44.006 56.465 1.00 48.48 ? 1471 HOH A O 1 HETATM 5498 O O . HOH V 11 . ? 33.798 5.688 58.232 1.00 65.59 ? 1472 HOH A O 1 HETATM 5499 O O . HOH V 11 . ? -12.612 22.929 66.551 1.00 52.35 ? 1473 HOH A O 1 HETATM 5500 O O . HOH V 11 . ? 41.986 38.432 52.606 1.00 80.82 ? 1474 HOH A O 1 HETATM 5501 O O . HOH V 11 . ? -9.303 46.289 39.201 1.00 66.43 ? 1475 HOH A O 1 HETATM 5502 O O . HOH V 11 . ? 20.644 5.176 3.425 1.00 54.67 ? 1476 HOH A O 1 HETATM 5503 O O . HOH V 11 . ? 13.809 9.230 8.632 1.00 60.45 ? 1477 HOH A O 1 HETATM 5504 O O . HOH V 11 . ? -10.503 48.530 45.533 1.00 44.81 ? 1478 HOH A O 1 HETATM 5505 O O . HOH V 11 . ? 38.773 27.253 27.896 1.00 40.03 ? 1479 HOH A O 1 HETATM 5506 O O . HOH V 11 . ? 1.461 39.466 30.754 1.00 61.08 ? 1480 HOH A O 1 HETATM 5507 O O . HOH V 11 . ? 21.980 34.914 49.928 1.00 42.00 ? 1481 HOH A O 1 HETATM 5508 O O . HOH V 11 . ? 15.219 16.838 71.399 1.00 68.70 ? 1482 HOH A O 1 HETATM 5509 O O . HOH V 11 . ? 8.448 11.168 16.547 1.00 49.20 ? 1483 HOH A O 1 HETATM 5510 O O . HOH V 11 . ? 11.476 44.948 43.478 1.00 30.03 ? 1484 HOH A O 1 HETATM 5511 O O . HOH V 11 . ? 35.192 34.148 29.869 1.00 86.37 ? 1485 HOH A O 1 HETATM 5512 O O . HOH V 11 . ? 10.058 9.023 16.402 1.00 42.27 ? 1486 HOH A O 1 HETATM 5513 O O . HOH V 11 . ? 15.989 24.552 7.468 1.00 56.10 ? 1487 HOH A O 1 HETATM 5514 O O . HOH V 11 . ? -3.670 39.788 66.852 1.00 51.21 ? 1488 HOH A O 1 HETATM 5515 O O . HOH V 11 . ? -14.674 27.170 47.146 1.00 34.75 ? 1489 HOH A O 1 HETATM 5516 O O . HOH V 11 . ? 11.181 5.365 43.469 1.00 49.12 ? 1490 HOH A O 1 HETATM 5517 O O . HOH V 11 . ? -10.605 28.201 45.704 1.00 43.68 ? 1491 HOH A O 1 HETATM 5518 O O . HOH V 11 . ? 25.558 33.256 29.316 1.00 23.69 ? 1492 HOH A O 1 HETATM 5519 O O . HOH V 11 . ? 10.326 44.720 49.723 1.00 73.41 ? 1493 HOH A O 1 HETATM 5520 O O . HOH V 11 . ? -16.857 48.219 58.538 1.00 72.07 ? 1494 HOH A O 1 HETATM 5521 O O . HOH V 11 . ? 24.630 5.950 1.442 1.00 41.09 ? 1495 HOH A O 1 HETATM 5522 O O . HOH V 11 . ? 13.894 9.200 14.483 1.00 35.15 ? 1496 HOH A O 1 HETATM 5523 O O . HOH V 11 . ? 3.214 31.188 67.845 1.00 42.51 ? 1497 HOH A O 1 HETATM 5524 O O . HOH V 11 . ? 37.210 6.890 45.578 1.00 52.83 ? 1498 HOH A O 1 HETATM 5525 O O . HOH V 11 . ? 35.446 4.724 2.405 1.00 36.64 ? 1499 HOH A O 1 HETATM 5526 O O . HOH V 11 . ? 17.195 6.077 16.263 1.00 48.13 ? 1500 HOH A O 1 HETATM 5527 O O . HOH V 11 . ? 36.596 20.864 53.633 1.00 40.69 ? 1501 HOH A O 1 HETATM 5528 O O . HOH V 11 . ? 9.715 14.119 64.812 1.00 55.02 ? 1502 HOH A O 1 HETATM 5529 O O . HOH V 11 . ? 10.619 43.114 61.039 1.00 49.74 ? 1503 HOH A O 1 HETATM 5530 O O . HOH V 11 . ? 3.645 33.871 24.646 1.00 60.95 ? 1504 HOH A O 1 HETATM 5531 O O . HOH V 11 . ? 23.404 -2.348 35.707 1.00 55.30 ? 1505 HOH A O 1 HETATM 5532 O O . HOH V 11 . ? 15.060 40.540 42.542 1.00 33.59 ? 1506 HOH A O 1 HETATM 5533 O O . HOH V 11 . ? 7.119 8.699 24.444 1.00 36.21 ? 1507 HOH A O 1 HETATM 5534 O O . HOH V 11 . ? 40.419 7.206 31.647 1.00 33.49 ? 1508 HOH A O 1 HETATM 5535 O O . HOH V 11 . ? 27.927 33.212 50.265 1.00 38.12 ? 1509 HOH A O 1 HETATM 5536 O O . HOH V 11 . ? 36.489 30.437 8.304 1.00 49.86 ? 1510 HOH A O 1 HETATM 5537 O O . HOH V 11 . ? 28.575 -1.140 20.691 1.00 48.48 ? 1511 HOH A O 1 HETATM 5538 O O . HOH V 11 . ? 27.761 17.996 60.369 1.00 53.48 ? 1512 HOH A O 1 HETATM 5539 O O . HOH V 11 . ? 30.965 30.660 48.821 1.00 44.01 ? 1513 HOH A O 1 HETATM 5540 O O . HOH V 11 . ? -14.830 50.113 58.896 1.00 51.28 ? 1514 HOH A O 1 HETATM 5541 O O . HOH V 11 . ? 27.994 35.055 44.171 1.00 48.69 ? 1515 HOH A O 1 HETATM 5542 O O . HOH V 11 . ? 33.590 17.074 2.139 1.00 50.43 ? 1516 HOH A O 1 HETATM 5543 O O . HOH V 11 . ? 16.158 3.594 21.903 1.00 48.60 ? 1517 HOH A O 1 HETATM 5544 O O . HOH V 11 . ? 29.019 6.996 -3.739 1.00 43.72 ? 1518 HOH A O 1 HETATM 5545 O O . HOH V 11 . ? -2.205 19.507 26.023 1.00 49.62 ? 1519 HOH A O 1 HETATM 5546 O O . HOH V 11 . ? -3.637 15.910 46.248 1.00 47.32 ? 1520 HOH A O 1 HETATM 5547 O O . HOH V 11 . ? 34.707 11.465 55.440 1.00 58.89 ? 1521 HOH A O 1 HETATM 5548 O O . HOH V 11 . ? -1.838 16.880 60.040 1.00 55.09 ? 1522 HOH A O 1 HETATM 5549 O O . HOH V 11 . ? -14.459 22.653 44.371 1.00 55.73 ? 1523 HOH A O 1 HETATM 5550 O O . HOH V 11 . ? -6.546 51.916 48.801 1.00 53.06 ? 1524 HOH A O 1 HETATM 5551 O O . HOH V 11 . ? 29.787 19.183 3.174 1.00 66.83 ? 1525 HOH A O 1 HETATM 5552 O O . HOH V 11 . ? 11.987 -1.400 31.028 1.00 49.42 ? 1526 HOH A O 1 HETATM 5553 O O . HOH V 11 . ? 21.937 21.176 67.373 1.00 64.57 ? 1527 HOH A O 1 HETATM 5554 O O . HOH V 11 . ? 35.209 4.321 30.347 1.00 57.38 ? 1528 HOH A O 1 HETATM 5555 O O . HOH V 11 . ? -4.469 13.739 47.807 1.00 51.19 ? 1529 HOH A O 1 HETATM 5556 O O . HOH V 11 . ? 34.064 20.478 58.079 1.00 52.06 ? 1530 HOH A O 1 HETATM 5557 O O . HOH V 11 . ? 17.440 4.360 4.482 1.00 57.69 ? 1531 HOH A O 1 HETATM 5558 O O . HOH V 11 . ? -6.653 21.073 35.757 1.00 59.13 ? 1532 HOH A O 1 HETATM 5559 O O . HOH V 11 . ? 25.465 29.286 12.736 1.00 57.35 ? 1533 HOH A O 1 HETATM 5560 O O . HOH V 11 . ? -4.759 37.471 68.201 1.00 51.61 ? 1534 HOH A O 1 HETATM 5561 O O . HOH V 11 . ? 34.002 3.440 6.837 1.00 50.71 ? 1535 HOH A O 1 HETATM 5562 O O . HOH V 11 . ? 17.598 36.515 53.459 1.00 44.44 ? 1536 HOH A O 1 HETATM 5563 O O . HOH V 11 . ? -10.496 26.529 41.134 1.00 47.82 ? 1537 HOH A O 1 HETATM 5564 O O . HOH V 11 . ? 0.503 31.686 26.760 1.00 37.45 ? 1538 HOH A O 1 HETATM 5565 O O . HOH V 11 . ? 27.264 16.238 54.449 1.00 47.01 ? 1539 HOH A O 1 HETATM 5566 O O . HOH V 11 . ? 28.696 -0.375 5.275 1.00 46.24 ? 1540 HOH A O 1 HETATM 5567 O O . HOH V 11 . ? 12.342 2.078 37.016 1.00 46.62 ? 1541 HOH A O 1 HETATM 5568 O O . HOH V 11 . ? 46.435 30.303 13.910 1.00 47.92 ? 1542 HOH A O 1 HETATM 5569 O O . HOH V 11 . ? 28.896 35.647 18.467 1.00 48.30 ? 1543 HOH A O 1 HETATM 5570 O O . HOH V 11 . ? 13.853 11.399 62.811 1.00 50.57 ? 1544 HOH A O 1 HETATM 5571 O O . HOH V 11 . ? -7.314 18.064 47.396 1.00 52.22 ? 1545 HOH A O 1 HETATM 5572 O O . HOH V 11 . ? 28.203 -3.521 37.985 1.00 48.30 ? 1546 HOH A O 1 HETATM 5573 O O . HOH V 11 . ? 7.293 10.316 22.147 1.00 46.24 ? 1547 HOH A O 1 HETATM 5574 O O . HOH V 11 . ? 22.978 -3.072 18.076 1.00 52.88 ? 1548 HOH A O 1 HETATM 5575 O O . HOH V 11 . ? -1.810 54.720 55.167 1.00 46.04 ? 1549 HOH A O 1 HETATM 5576 O O . HOH V 11 . ? 25.088 5.141 56.085 1.00 69.53 ? 1550 HOH A O 1 HETATM 5577 O O . HOH V 11 . ? 30.037 33.567 43.341 1.00 65.39 ? 1551 HOH A O 1 HETATM 5578 O O . HOH V 11 . ? -3.409 49.724 45.325 1.00 50.88 ? 1552 HOH A O 1 HETATM 5579 O O . HOH V 11 . ? 17.378 34.836 63.281 1.00 55.53 ? 1553 HOH A O 1 HETATM 5580 O O . HOH V 11 . ? 31.965 30.597 52.931 1.00 55.92 ? 1554 HOH A O 1 HETATM 5581 O O . HOH V 11 . ? 32.182 0.588 31.196 1.00 41.50 ? 1555 HOH A O 1 HETATM 5582 O O . HOH V 11 . ? 38.109 5.925 7.385 1.00 53.77 ? 1556 HOH A O 1 HETATM 5583 O O . HOH V 11 . ? 7.218 10.438 51.596 1.00 47.67 ? 1557 HOH A O 1 HETATM 5584 O O . HOH V 11 . ? -11.719 42.528 32.522 1.00 55.42 ? 1558 HOH A O 1 HETATM 5585 O O . HOH V 11 . ? -3.279 50.740 64.675 1.00 62.81 ? 1559 HOH A O 1 HETATM 5586 O O . HOH V 11 . ? 35.693 3.357 51.626 1.00 65.22 ? 1560 HOH A O 1 HETATM 5587 O O . HOH V 11 . ? 27.213 35.279 13.584 1.00 54.30 ? 1561 HOH A O 1 HETATM 5588 O O . HOH V 11 . ? 31.690 35.607 11.376 1.00 57.41 ? 1562 HOH A O 1 HETATM 5589 O O . HOH V 11 . ? 43.271 5.263 17.065 1.00 66.06 ? 1563 HOH A O 1 HETATM 5590 O O . HOH V 11 . ? 39.720 11.956 49.495 1.00 56.26 ? 1564 HOH A O 1 HETATM 5591 O O . HOH V 11 . ? -18.597 31.146 49.742 1.00 54.16 ? 1565 HOH A O 1 HETATM 5592 O O . HOH V 11 . ? 22.896 -3.053 26.223 1.00 65.49 ? 1566 HOH A O 1 HETATM 5593 O O . HOH V 11 . ? 19.795 15.075 8.847 1.00 116.71 ? 1567 HOH A O 1 HETATM 5594 O O . HOH V 11 . ? -0.525 6.854 37.653 1.00 71.57 ? 1568 HOH A O 1 HETATM 5595 O O . HOH V 11 . ? 5.334 19.703 65.535 1.00 72.44 ? 1569 HOH A O 1 HETATM 5596 O O . HOH V 11 . ? 12.667 8.776 61.275 1.00 58.11 ? 1570 HOH A O 1 HETATM 5597 O O . HOH V 11 . ? 49.368 18.301 34.310 1.00 55.02 ? 1571 HOH A O 1 HETATM 5598 O O . HOH V 11 . ? -14.306 27.543 41.096 1.00 53.60 ? 1572 HOH A O 1 HETATM 5599 O O . HOH V 11 . ? 1.009 10.999 30.922 1.00 45.40 ? 1573 HOH A O 1 HETATM 5600 O O . HOH V 11 . ? 39.571 29.503 43.420 1.00 50.58 ? 1574 HOH A O 1 HETATM 5601 O O . HOH V 11 . ? 15.794 41.033 56.873 1.00 56.38 ? 1575 HOH A O 1 HETATM 5602 O O . HOH V 11 . ? 17.913 -1.298 16.593 1.00 52.27 ? 1576 HOH A O 1 HETATM 5603 O O . HOH V 11 . ? 16.244 16.919 7.548 1.00 72.88 ? 1577 HOH A O 1 HETATM 5604 O O . HOH V 11 . ? 35.224 -0.978 -7.063 1.00 49.34 ? 1578 HOH A O 1 HETATM 5605 O O . HOH V 11 . ? -1.815 14.254 44.051 1.00 46.15 ? 1579 HOH A O 1 HETATM 5606 O O . HOH V 11 . ? 28.909 0.174 46.484 1.00 79.56 ? 1580 HOH A O 1 HETATM 5607 O O . HOH V 11 . ? -2.353 30.121 28.089 1.00 32.98 ? 1581 HOH A O 1 HETATM 5608 O O . HOH V 11 . ? -10.285 29.405 29.877 1.00 48.88 ? 1582 HOH A O 1 HETATM 5609 O O . HOH V 11 . ? -9.665 29.662 34.139 1.00 58.77 ? 1583 HOH A O 1 HETATM 5610 O O . HOH V 11 . ? -8.540 24.303 26.711 1.00 59.61 ? 1584 HOH A O 1 HETATM 5611 O O . HOH V 11 . ? 17.027 34.977 51.362 1.00 43.78 ? 1585 HOH A O 1 HETATM 5612 O O . HOH V 11 . ? 28.035 29.519 39.738 1.00 52.11 ? 1586 HOH A O 1 HETATM 5613 O O . HOH V 11 . ? 29.775 30.118 41.596 1.00 46.19 ? 1587 HOH A O 1 HETATM 5614 O O . HOH V 11 . ? 24.619 35.807 33.746 1.00 66.80 ? 1588 HOH A O 1 HETATM 5615 O O . HOH V 11 . ? 28.567 32.744 35.697 1.00 72.95 ? 1589 HOH A O 1 HETATM 5616 O O . HOH V 11 . ? 10.603 41.954 50.090 1.00 40.57 ? 1590 HOH A O 1 HETATM 5617 O O . HOH V 11 . ? 11.998 40.754 31.971 1.00 46.42 ? 1591 HOH A O 1 HETATM 5618 O O . HOH V 11 . ? 38.321 5.742 30.681 1.00 46.24 ? 1592 HOH A O 1 HETATM 5619 O O . HOH V 11 . ? 3.840 14.778 21.658 1.00 49.31 ? 1593 HOH A O 1 HETATM 5620 O O . HOH V 11 . ? 8.831 30.710 69.596 1.00 53.15 ? 1594 HOH A O 1 HETATM 5621 O O . HOH V 11 . ? 35.658 2.273 19.433 1.00 45.21 ? 1595 HOH A O 1 HETATM 5622 O O . HOH V 11 . ? 38.294 3.577 37.544 1.00 52.93 ? 1596 HOH A O 1 HETATM 5623 O O . HOH V 11 . ? -11.917 50.717 48.662 1.00 58.37 ? 1597 HOH A O 1 HETATM 5624 O O . HOH V 11 . ? 45.793 27.207 24.320 1.00 52.38 ? 1598 HOH A O 1 HETATM 5625 O O . HOH V 11 . ? 9.141 25.587 69.171 1.00 48.88 ? 1599 HOH A O 1 HETATM 5626 O O . HOH V 11 . ? -2.485 46.439 64.764 1.00 66.56 ? 1600 HOH A O 1 HETATM 5627 O O . HOH V 11 . ? 35.405 31.245 38.682 1.00 45.64 ? 1601 HOH A O 1 HETATM 5628 O O . HOH V 11 . ? 40.138 22.289 46.307 1.00 47.10 ? 1602 HOH A O 1 HETATM 5629 O O . HOH V 11 . ? 19.769 45.071 49.378 1.00 78.51 ? 1603 HOH A O 1 HETATM 5630 O O . HOH V 11 . ? 53.528 11.696 20.269 1.00 49.22 ? 1604 HOH A O 1 HETATM 5631 O O . HOH V 11 . ? 31.138 -4.153 37.363 1.00 55.57 ? 1605 HOH A O 1 HETATM 5632 O O . HOH V 11 . ? 56.542 11.285 25.512 1.00 42.25 ? 1606 HOH A O 1 HETATM 5633 O O . HOH V 11 . ? 41.312 27.040 48.950 1.00 62.03 ? 1607 HOH A O 1 HETATM 5634 O O . HOH V 11 . ? 32.731 21.540 4.801 1.00 52.49 ? 1608 HOH A O 1 HETATM 5635 O O . HOH V 11 . ? -7.969 24.952 63.208 1.00 46.42 ? 1609 HOH A O 1 HETATM 5636 O O . HOH V 11 . ? 17.769 38.836 52.475 1.00 54.97 ? 1610 HOH A O 1 HETATM 5637 O O . HOH V 11 . ? 35.775 30.350 41.072 1.00 52.40 ? 1611 HOH A O 1 HETATM 5638 O O . HOH V 11 . ? 14.143 12.068 8.076 1.00 58.92 ? 1612 HOH A O 1 HETATM 5639 O O . HOH V 11 . ? -24.711 36.318 50.072 1.00 62.93 ? 1613 HOH A O 1 HETATM 5640 O O . HOH V 11 . ? 0.296 30.859 20.646 1.00 54.83 ? 1614 HOH A O 1 HETATM 5641 O O . HOH V 11 . ? 5.102 33.939 70.445 1.00 54.08 ? 1615 HOH A O 1 HETATM 5642 O O . HOH V 11 . ? 29.632 18.611 56.863 1.00 58.18 ? 1616 HOH A O 1 HETATM 5643 O O . HOH V 11 . ? 23.816 34.878 15.185 1.00 55.41 ? 1617 HOH A O 1 HETATM 5644 O O . HOH V 11 . ? 34.137 -0.360 13.548 1.00 59.87 ? 1618 HOH A O 1 HETATM 5645 O O . HOH V 11 . ? 10.699 33.831 67.922 1.00 50.47 ? 1619 HOH A O 1 HETATM 5646 O O . HOH V 11 . ? 16.944 47.020 44.561 1.00 71.60 ? 1620 HOH A O 1 HETATM 5647 O O . HOH V 11 . ? 42.147 15.112 42.375 1.00 61.58 ? 1621 HOH A O 1 HETATM 5648 O O . HOH V 11 . ? 14.209 8.567 58.360 1.00 59.66 ? 1622 HOH A O 1 HETATM 5649 O O . HOH V 11 . ? 53.794 9.030 25.171 1.00 71.28 ? 1623 HOH A O 1 HETATM 5650 O O . HOH V 11 . ? -4.637 11.582 46.176 1.00 60.71 ? 1624 HOH A O 1 HETATM 5651 O O . HOH V 11 . ? 45.706 37.583 53.402 1.00 77.08 ? 1625 HOH A O 1 HETATM 5652 O O . HOH V 11 . ? 45.868 5.828 33.758 1.00 65.40 ? 1626 HOH A O 1 HETATM 5653 O O . HOH V 11 . ? -0.887 55.417 60.986 1.00 55.92 ? 1627 HOH A O 1 HETATM 5654 O O . HOH V 11 . ? 22.681 37.235 47.419 1.00 45.01 ? 1628 HOH A O 1 HETATM 5655 O O . HOH V 11 . ? 35.023 5.595 45.438 1.00 65.81 ? 1629 HOH A O 1 HETATM 5656 O O . HOH V 11 . ? 41.116 10.453 39.855 1.00 45.80 ? 1630 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASP A 1 ? 0.4363 0.4370 0.4231 -0.0095 0.0073 -0.0051 1 ASP A N 2 C CA . ASP A 1 ? 0.4309 0.4427 0.4179 -0.0048 0.0113 -0.0062 1 ASP A CA 3 C C . ASP A 1 ? 0.4294 0.4386 0.4159 -0.0077 0.0099 -0.0075 1 ASP A C 4 O O . ASP A 1 ? 0.4245 0.4435 0.4139 -0.0028 0.0161 -0.0099 1 ASP A O 5 C CB . ASP A 1 ? 0.4359 0.4458 0.4252 -0.0052 0.0095 -0.0066 1 ASP A CB 6 C CG . ASP A 1 ? 0.4455 0.4613 0.4436 -0.0015 0.0096 -0.0038 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.4491 0.4567 0.4595 -0.0179 0.0112 -0.0057 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.4586 0.4715 0.4601 0.0110 0.0118 0.0030 1 ASP A OD2 9 N N . TYR A 2 ? 0.4264 0.4389 0.4018 -0.0083 0.0116 -0.0088 2 TYR A N 10 C CA . TYR A 2 ? 0.4150 0.4236 0.3907 -0.0104 0.0067 -0.0135 2 TYR A CA 11 C C . TYR A 2 ? 0.4021 0.4165 0.3810 -0.0098 0.0031 -0.0137 2 TYR A C 12 O O . TYR A 2 ? 0.4042 0.4207 0.3772 -0.0087 0.0038 -0.0197 2 TYR A O 13 C CB . TYR A 2 ? 0.4170 0.4249 0.3982 -0.0119 0.0089 -0.0123 2 TYR A CB 14 C CG . TYR A 2 ? 0.4228 0.4164 0.4082 -0.0077 0.0049 -0.0155 2 TYR A CG 15 C CD1 . TYR A 2 ? 0.4136 0.4195 0.4115 -0.0095 0.0071 -0.0200 2 TYR A CD1 16 C CD2 . TYR A 2 ? 0.4317 0.4298 0.4039 -0.0135 0.0053 -0.0133 2 TYR A CD2 17 C CE1 . TYR A 2 ? 0.4101 0.3990 0.3962 -0.0104 0.0028 -0.0168 2 TYR A CE1 18 C CE2 . TYR A 2 ? 0.4202 0.4277 0.4195 -0.0076 0.0073 -0.0185 2 TYR A CE2 19 C CZ . TYR A 2 ? 0.4219 0.4095 0.4106 -0.0128 0.0016 -0.0178 2 TYR A CZ 20 O OH . TYR A 2 ? 0.4136 0.4225 0.4004 -0.0057 0.0144 -0.0294 2 TYR A OH 21 N N . VAL A 3 ? 0.3778 0.3992 0.3566 -0.0163 0.0033 -0.0169 3 VAL A N 22 C CA . VAL A 3 ? 0.3633 0.3878 0.3402 -0.0158 0.0052 -0.0136 3 VAL A CA 23 C C . VAL A 3 ? 0.3626 0.3780 0.3386 -0.0124 0.0025 -0.0192 3 VAL A C 24 O O . VAL A 3 ? 0.3584 0.3832 0.3366 -0.0172 0.0008 -0.0240 3 VAL A O 25 C CB . VAL A 3 ? 0.3625 0.3882 0.3333 -0.0172 0.0021 -0.0132 3 VAL A CB 26 C CG1 . VAL A 3 ? 0.3485 0.3856 0.3258 -0.0225 0.0011 -0.0112 3 VAL A CG1 27 C CG2 . VAL A 3 ? 0.3580 0.3934 0.3361 -0.0192 0.0010 -0.0063 3 VAL A CG2 28 N N . LEU A 4 ? 0.3566 0.3631 0.3286 -0.0173 0.0092 -0.0230 4 LEU A N 29 C CA . LEU A 4 ? 0.3540 0.3584 0.3309 -0.0087 0.0125 -0.0233 4 LEU A CA 30 C C . LEU A 4 ? 0.3434 0.3499 0.3269 -0.0119 0.0124 -0.0278 4 LEU A C 31 O O . LEU A 4 ? 0.3290 0.3433 0.3257 -0.0141 0.0192 -0.0366 4 LEU A O 32 C CB . LEU A 4 ? 0.3623 0.3629 0.3360 -0.0073 0.0083 -0.0202 4 LEU A CB 33 C CG . LEU A 4 ? 0.3658 0.3633 0.3540 -0.0045 0.0095 -0.0107 4 LEU A CG 34 C CD1 . LEU A 4 ? 0.4060 0.3826 0.3909 0.0050 0.0078 -0.0049 4 LEU A CD1 35 C CD2 . LEU A 4 ? 0.3679 0.3787 0.3599 0.0024 0.0017 -0.0110 4 LEU A CD2 36 N N . TYR A 5 ? 0.3265 0.3378 0.3139 -0.0128 0.0152 -0.0262 5 TYR A N 37 C CA . TYR A 5 ? 0.3136 0.3296 0.3119 -0.0126 0.0138 -0.0235 5 TYR A CA 38 C C . TYR A 5 ? 0.3141 0.3321 0.3143 -0.0132 0.0107 -0.0161 5 TYR A C 39 O O . TYR A 5 ? 0.3007 0.3414 0.3163 -0.0146 0.0228 -0.0174 5 TYR A O 40 C CB . TYR A 5 ? 0.3021 0.3229 0.2899 -0.0102 0.0095 -0.0182 5 TYR A CB 41 C CG . TYR A 5 ? 0.2983 0.3085 0.2989 -0.0089 0.0078 -0.0138 5 TYR A CG 42 C CD1 . TYR A 5 ? 0.2907 0.3045 0.2731 0.0034 0.0052 -0.0108 5 TYR A CD1 43 C CD2 . TYR A 5 ? 0.3178 0.3078 0.2974 0.0016 0.0112 -0.0123 5 TYR A CD2 44 C CE1 . TYR A 5 ? 0.2572 0.3112 0.2627 -0.0040 -0.0008 -0.0119 5 TYR A CE1 45 C CE2 . TYR A 5 ? 0.2720 0.3096 0.2761 -0.0067 0.0097 -0.0100 5 TYR A CE2 46 C CZ . TYR A 5 ? 0.2850 0.3142 0.2695 -0.0049 -0.0001 -0.0077 5 TYR A CZ 47 O OH . TYR A 5 ? 0.2779 0.3157 0.2656 -0.0174 0.0066 -0.0147 5 TYR A OH 48 N N . LYS A 6 ? 0.3181 0.3419 0.3260 -0.0165 0.0112 -0.0115 6 LYS A N 49 C CA . LYS A 6 ? 0.3284 0.3589 0.3388 -0.0204 0.0035 -0.0031 6 LYS A CA 50 C C . LYS A 6 ? 0.3283 0.3646 0.3481 -0.0182 0.0047 -0.0036 6 LYS A C 51 O O . LYS A 6 ? 0.3299 0.3808 0.3651 -0.0161 -0.0005 -0.0008 6 LYS A O 52 C CB . LYS A 6 ? 0.3342 0.3609 0.3418 -0.0191 0.0080 -0.0006 6 LYS A CB 53 C CG . LYS A 6 ? 0.3365 0.3677 0.3483 -0.0246 -0.0040 0.0001 6 LYS A CG 54 C CD . LYS A 6 ? 0.3697 0.3903 0.3729 -0.0182 0.0046 0.0047 6 LYS A CD 55 C CE . LYS A 6 ? 0.3795 0.4070 0.3973 -0.0207 -0.0096 0.0078 6 LYS A CE 56 N NZ . LYS A 6 ? 0.4104 0.4293 0.4139 -0.0090 0.0069 -0.0015 6 LYS A NZ 57 N N . ASP A 7 ? 0.3280 0.3620 0.3483 -0.0180 0.0064 -0.0100 7 ASP A N 58 C CA . ASP A 7 ? 0.3380 0.3617 0.3521 -0.0210 0.0069 -0.0137 7 ASP A CA 59 C C . ASP A 7 ? 0.3407 0.3595 0.3485 -0.0177 0.0063 -0.0163 7 ASP A C 60 O O . ASP A 7 ? 0.3355 0.3603 0.3431 -0.0216 0.0163 -0.0189 7 ASP A O 61 C CB . ASP A 7 ? 0.3370 0.3605 0.3545 -0.0183 0.0088 -0.0141 7 ASP A CB 62 C CG . ASP A 7 ? 0.3567 0.3731 0.3759 -0.0155 0.0009 -0.0214 7 ASP A CG 63 O OD1 . ASP A 7 ? 0.3634 0.3673 0.3624 -0.0345 0.0080 -0.0188 7 ASP A OD1 64 O OD2 . ASP A 7 ? 0.3683 0.3883 0.3843 -0.0082 0.0009 -0.0283 7 ASP A OD2 65 N N . ALA A 8 ? 0.3536 0.3706 0.3553 -0.0173 0.0073 -0.0210 8 ALA A N 66 C CA . ALA A 8 ? 0.3650 0.3769 0.3689 -0.0160 0.0078 -0.0148 8 ALA A CA 67 C C . ALA A 8 ? 0.3747 0.3810 0.3776 -0.0161 0.0081 -0.0145 8 ALA A C 68 O O . ALA A 8 ? 0.3735 0.3834 0.3853 -0.0223 0.0107 -0.0160 8 ALA A O 69 C CB . ALA A 8 ? 0.3690 0.3762 0.3677 -0.0110 0.0102 -0.0153 8 ALA A CB 70 N N . THR A 9 ? 0.3812 0.3858 0.3912 -0.0182 0.0082 -0.0142 9 THR A N 71 C CA . THR A 9 ? 0.3899 0.3892 0.3959 -0.0168 0.0068 -0.0127 9 THR A CA 72 C C . THR A 9 ? 0.3937 0.3909 0.3935 -0.0137 0.0086 -0.0118 9 THR A C 73 O O . THR A 9 ? 0.4053 0.4071 0.4056 -0.0219 0.0118 -0.0111 9 THR A O 74 C CB . THR A 9 ? 0.3905 0.3858 0.3962 -0.0174 0.0051 -0.0128 9 THR A CB 75 O OG1 . THR A 9 ? 0.3897 0.3853 0.4128 -0.0362 0.0052 -0.0242 9 THR A OG1 76 C CG2 . THR A 9 ? 0.3863 0.3900 0.3996 -0.0162 0.0023 -0.0090 9 THR A CG2 77 N N . LYS A 10 ? 0.3847 0.3864 0.3871 -0.0138 0.0082 -0.0165 10 LYS A N 78 C CA . LYS A 10 ? 0.3827 0.3834 0.3781 -0.0108 0.0059 -0.0130 10 LYS A CA 79 C C . LYS A 10 ? 0.3687 0.3745 0.3731 -0.0111 0.0106 -0.0122 10 LYS A C 80 O O . LYS A 10 ? 0.3641 0.3697 0.3692 -0.0164 0.0130 -0.0154 10 LYS A O 81 C CB . LYS A 10 ? 0.3921 0.3919 0.3840 -0.0070 0.0070 -0.0096 10 LYS A CB 82 C CG . LYS A 10 ? 0.4270 0.4157 0.4048 0.0004 0.0066 -0.0126 10 LYS A CG 83 C CD . LYS A 10 ? 0.4821 0.4426 0.4559 -0.0007 0.0026 -0.0066 10 LYS A CD 84 C CE . LYS A 10 ? 0.5118 0.5027 0.5103 -0.0032 -0.0038 -0.0022 10 LYS A CE 85 N NZ . LYS A 10 ? 0.5637 0.5271 0.5109 -0.0020 0.0051 0.0062 10 LYS A NZ 86 N N . PRO A 11 ? 0.3611 0.3636 0.3606 -0.0113 0.0097 -0.0155 11 PRO A N 87 C CA . PRO A 11 ? 0.3572 0.3538 0.3531 -0.0099 0.0095 -0.0180 11 PRO A CA 88 C C . PRO A 11 ? 0.3466 0.3407 0.3346 -0.0069 0.0142 -0.0235 11 PRO A C 89 O O . PRO A 11 ? 0.3326 0.3336 0.3207 -0.0071 0.0213 -0.0294 11 PRO A O 90 C CB . PRO A 11 ? 0.3622 0.3556 0.3610 -0.0082 0.0092 -0.0166 11 PRO A CB 91 C CG . PRO A 11 ? 0.3804 0.3683 0.3594 -0.0107 0.0036 -0.0196 11 PRO A CG 92 C CD . PRO A 11 ? 0.3721 0.3679 0.3733 -0.0080 0.0063 -0.0116 11 PRO A CD 93 N N . VAL A 12 ? 0.3291 0.3318 0.3194 -0.0034 0.0175 -0.0257 12 VAL A N 94 C CA . VAL A 12 ? 0.3250 0.3213 0.3128 -0.0008 0.0162 -0.0252 12 VAL A CA 95 C C . VAL A 12 ? 0.3278 0.3152 0.3053 0.0036 0.0191 -0.0256 12 VAL A C 96 O O . VAL A 12 ? 0.3254 0.2982 0.3140 0.0061 0.0278 -0.0283 12 VAL A O 97 C CB . VAL A 12 ? 0.3217 0.3167 0.3096 0.0004 0.0145 -0.0300 12 VAL A CB 98 C CG1 . VAL A 12 ? 0.2990 0.3210 0.3063 -0.0087 0.0106 -0.0249 12 VAL A CG1 99 C CG2 . VAL A 12 ? 0.3209 0.3315 0.3382 -0.0039 0.0083 -0.0189 12 VAL A CG2 100 N N . GLU A 13 ? 0.3274 0.3177 0.3084 0.0019 0.0183 -0.0222 13 GLU A N 101 C CA . GLU A 13 ? 0.3322 0.3288 0.3129 0.0059 0.0190 -0.0169 13 GLU A CA 102 C C . GLU A 13 ? 0.3326 0.3307 0.3174 0.0040 0.0172 -0.0151 13 GLU A C 103 O O . GLU A 13 ? 0.3308 0.3220 0.3158 0.0048 0.0254 -0.0233 13 GLU A O 104 C CB . GLU A 13 ? 0.3416 0.3366 0.3224 0.0022 0.0151 -0.0122 13 GLU A CB 105 C CG . GLU A 13 ? 0.3507 0.3459 0.3273 0.0038 0.0148 -0.0141 13 GLU A CG 106 C CD . GLU A 13 ? 0.3900 0.3841 0.3849 -0.0073 0.0024 -0.0123 13 GLU A CD 107 O OE1 . GLU A 13 ? 0.3817 0.3995 0.4064 0.0109 0.0161 -0.0168 13 GLU A OE1 108 O OE2 . GLU A 13 ? 0.3531 0.3746 0.3778 0.0077 0.0154 -0.0227 13 GLU A OE2 109 N N . ASP A 14 ? 0.3349 0.3334 0.3215 0.0048 0.0177 -0.0169 14 ASP A N 110 C CA . ASP A 14 ? 0.3396 0.3399 0.3276 0.0018 0.0146 -0.0105 14 ASP A CA 111 C C . ASP A 14 ? 0.3185 0.3284 0.3164 0.0007 0.0116 -0.0157 14 ASP A C 112 O O . ASP A 14 ? 0.3219 0.3352 0.3196 -0.0003 0.0254 -0.0192 14 ASP A O 113 C CB . ASP A 14 ? 0.3448 0.3452 0.3429 -0.0018 0.0114 -0.0110 14 ASP A CB 114 C CG . ASP A 14 ? 0.4219 0.3946 0.4147 -0.0017 0.0023 -0.0003 14 ASP A CG 115 O OD1 . ASP A 14 ? 0.4587 0.4180 0.4692 0.0070 -0.0083 0.0139 14 ASP A OD1 116 O OD2 . ASP A 14 ? 0.4608 0.4489 0.5002 -0.0215 -0.0063 -0.0074 14 ASP A OD2 117 N N . ARG A 15 ? 0.3061 0.3188 0.3054 0.0010 0.0134 -0.0111 15 ARG A N 118 C CA . ARG A 15 ? 0.2809 0.3017 0.2891 0.0021 0.0064 -0.0148 15 ARG A CA 119 C C . ARG A 15 ? 0.2807 0.3049 0.2826 -0.0009 0.0075 -0.0098 15 ARG A C 120 O O . ARG A 15 ? 0.2744 0.3181 0.2666 -0.0061 0.0121 -0.0183 15 ARG A O 121 C CB . ARG A 15 ? 0.2753 0.3103 0.2894 0.0033 0.0043 -0.0109 15 ARG A CB 122 C CG . ARG A 15 ? 0.2789 0.2964 0.2991 0.0036 -0.0020 -0.0127 15 ARG A CG 123 C CD . ARG A 15 ? 0.2764 0.3002 0.2836 0.0064 0.0025 -0.0181 15 ARG A CD 124 N NE . ARG A 15 ? 0.2649 0.3193 0.2720 -0.0123 0.0136 -0.0199 15 ARG A NE 125 C CZ . ARG A 15 ? 0.2727 0.3056 0.2714 -0.0051 0.0142 -0.0082 15 ARG A CZ 126 N NH1 . ARG A 15 ? 0.2619 0.3312 0.2767 -0.0172 0.0079 -0.0275 15 ARG A NH1 127 N NH2 . ARG A 15 ? 0.2812 0.3064 0.2620 -0.0110 0.0052 -0.0250 15 ARG A NH2 128 N N . VAL A 16 ? 0.2719 0.3026 0.2740 -0.0046 0.0054 -0.0082 16 VAL A N 129 C CA . VAL A 16 ? 0.2792 0.3091 0.2808 -0.0004 0.0097 -0.0077 16 VAL A CA 130 C C . VAL A 16 ? 0.2839 0.3111 0.2795 -0.0030 0.0119 -0.0057 16 VAL A C 131 O O . VAL A 16 ? 0.2824 0.3171 0.2856 -0.0114 0.0170 -0.0041 16 VAL A O 132 C CB . VAL A 16 ? 0.2814 0.3059 0.2803 0.0023 0.0069 -0.0054 16 VAL A CB 133 C CG1 . VAL A 16 ? 0.2820 0.3088 0.2861 -0.0047 0.0108 -0.0065 16 VAL A CG1 134 C CG2 . VAL A 16 ? 0.2751 0.3010 0.2871 0.0038 0.0195 -0.0055 16 VAL A CG2 135 N N . ALA A 17 ? 0.2820 0.3095 0.2851 0.0005 0.0164 -0.0104 17 ALA A N 136 C CA . ALA A 17 ? 0.2878 0.3073 0.2891 0.0007 0.0219 -0.0080 17 ALA A CA 137 C C . ALA A 17 ? 0.2964 0.3164 0.2894 0.0003 0.0219 -0.0103 17 ALA A C 138 O O . ALA A 17 ? 0.3038 0.3288 0.2913 -0.0077 0.0263 -0.0142 17 ALA A O 139 C CB . ALA A 17 ? 0.2949 0.3111 0.3056 0.0026 0.0247 -0.0089 17 ALA A CB 140 N N . ASP A 18 ? 0.2933 0.3087 0.2834 -0.0001 0.0244 -0.0063 18 ASP A N 141 C CA . ASP A 18 ? 0.2972 0.3183 0.2839 0.0032 0.0206 -0.0110 18 ASP A CA 142 C C . ASP A 18 ? 0.2919 0.3167 0.2827 0.0048 0.0251 -0.0098 18 ASP A C 143 O O . ASP A 18 ? 0.2997 0.3389 0.2835 0.0022 0.0393 -0.0161 18 ASP A O 144 C CB . ASP A 18 ? 0.2951 0.3245 0.2834 0.0020 0.0186 -0.0118 18 ASP A CB 145 C CG . ASP A 18 ? 0.3065 0.3360 0.3045 -0.0024 0.0135 -0.0038 18 ASP A CG 146 O OD1 . ASP A 18 ? 0.3765 0.3771 0.3432 0.0061 0.0343 -0.0182 18 ASP A OD1 147 O OD2 . ASP A 18 ? 0.3161 0.3462 0.3144 -0.0057 0.0237 -0.0068 18 ASP A OD2 148 N N . LEU A 19 ? 0.2778 0.3047 0.2729 0.0061 0.0242 -0.0180 19 LEU A N 149 C CA . LEU A 19 ? 0.2644 0.2918 0.2648 0.0064 0.0206 -0.0101 19 LEU A CA 150 C C . LEU A 19 ? 0.2610 0.2945 0.2642 0.0104 0.0226 -0.0123 19 LEU A C 151 O O . LEU A 19 ? 0.2614 0.2970 0.2662 0.0073 0.0211 -0.0061 19 LEU A O 152 C CB . LEU A 19 ? 0.2699 0.2948 0.2668 0.0073 0.0216 -0.0130 19 LEU A CB 153 C CG . LEU A 19 ? 0.2651 0.2720 0.2627 0.0042 0.0176 -0.0023 19 LEU A CG 154 C CD1 . LEU A 19 ? 0.2913 0.3008 0.2730 0.0094 0.0170 -0.0027 19 LEU A CD1 155 C CD2 . LEU A 19 ? 0.2584 0.2884 0.2517 0.0012 0.0067 -0.0140 19 LEU A CD2 156 N N . LEU A 20 ? 0.2552 0.3018 0.2612 0.0114 0.0231 -0.0091 20 LEU A N 157 C CA . LEU A 20 ? 0.2649 0.3127 0.2613 0.0050 0.0234 -0.0095 20 LEU A CA 158 C C . LEU A 20 ? 0.2694 0.3180 0.2743 0.0061 0.0243 -0.0099 20 LEU A C 159 O O . LEU A 20 ? 0.2649 0.3194 0.2613 0.0040 0.0416 -0.0131 20 LEU A O 160 C CB . LEU A 20 ? 0.2661 0.3072 0.2720 0.0014 0.0164 -0.0056 20 LEU A CB 161 C CG . LEU A 20 ? 0.2730 0.3046 0.2685 0.0027 0.0092 -0.0060 20 LEU A CG 162 C CD1 . LEU A 20 ? 0.2776 0.3197 0.2873 -0.0048 -0.0071 -0.0186 20 LEU A CD1 163 C CD2 . LEU A 20 ? 0.2967 0.3187 0.2847 -0.0022 0.0085 -0.0032 20 LEU A CD2 164 N N . GLY A 21 ? 0.2812 0.3247 0.2803 0.0086 0.0322 -0.0107 21 GLY A N 165 C CA . GLY A 21 ? 0.2955 0.3319 0.2960 0.0144 0.0313 -0.0097 21 GLY A CA 166 C C . GLY A 21 ? 0.3009 0.3365 0.3074 0.0091 0.0259 -0.0075 21 GLY A C 167 O O . GLY A 21 ? 0.3156 0.3619 0.3252 0.0102 0.0272 0.0001 21 GLY A O 168 N N . ARG A 22 ? 0.2956 0.3344 0.2950 0.0059 0.0194 -0.0038 22 ARG A N 169 C CA . ARG A 22 ? 0.2876 0.3309 0.2831 0.0045 0.0223 -0.0080 22 ARG A CA 170 C C . ARG A 22 ? 0.2823 0.3310 0.2734 0.0025 0.0208 -0.0060 22 ARG A C 171 O O . ARG A 22 ? 0.2907 0.3469 0.2735 -0.0021 0.0282 -0.0104 22 ARG A O 172 C CB . ARG A 22 ? 0.2856 0.3257 0.2831 0.0007 0.0183 -0.0110 22 ARG A CB 173 C CG . ARG A 22 ? 0.2902 0.3327 0.2963 0.0050 0.0187 -0.0168 22 ARG A CG 174 C CD . ARG A 22 ? 0.3206 0.3492 0.3233 0.0034 0.0099 -0.0084 22 ARG A CD 175 N NE . ARG A 22 ? 0.3095 0.3755 0.3313 -0.0145 0.0103 0.0024 22 ARG A NE 176 C CZ . ARG A 22 ? 0.3605 0.3809 0.3532 -0.0135 0.0113 -0.0059 22 ARG A CZ 177 N NH1 . ARG A 22 ? 0.3741 0.4209 0.3528 -0.0053 0.0115 0.0054 22 ARG A NH1 178 N NH2 . ARG A 22 ? 0.3757 0.4135 0.3642 -0.0157 0.0063 -0.0002 22 ARG A NH2 179 N N . MET A 23 ? 0.2698 0.3271 0.2583 0.0039 0.0251 -0.0082 23 MET A N 180 C CA . MET A 23 ? 0.2474 0.3304 0.2453 -0.0005 0.0291 -0.0115 23 MET A CA 181 C C . MET A 23 ? 0.2453 0.3201 0.2465 0.0032 0.0261 -0.0096 23 MET A C 182 O O . MET A 23 ? 0.2569 0.3423 0.2584 -0.0014 0.0231 -0.0105 23 MET A O 183 C CB . MET A 23 ? 0.2345 0.3276 0.2482 0.0011 0.0334 -0.0145 23 MET A CB 184 C CG . MET A 23 ? 0.2345 0.3331 0.2457 0.0021 0.0297 -0.0151 23 MET A CG 185 S SD . MET A 23 ? 0.2161 0.3538 0.2341 -0.0008 0.0408 -0.0191 23 MET A SD 186 C CE . MET A 23 ? 0.2386 0.3183 0.2528 0.0034 0.0148 -0.0037 23 MET A CE 187 N N . THR A 24 ? 0.2467 0.3306 0.2441 -0.0001 0.0220 -0.0100 24 THR A N 188 C CA . THR A 24 ? 0.2506 0.3292 0.2483 -0.0034 0.0127 -0.0083 24 THR A CA 189 C C . THR A 24 ? 0.2480 0.3315 0.2493 -0.0043 0.0075 -0.0077 24 THR A C 190 O O . THR A 24 ? 0.2241 0.3322 0.2378 0.0049 0.0101 -0.0110 24 THR A O 191 C CB . THR A 24 ? 0.2648 0.3211 0.2523 -0.0030 0.0066 -0.0045 24 THR A CB 192 O OG1 . THR A 24 ? 0.2335 0.3310 0.2448 -0.0060 0.0172 -0.0086 24 THR A OG1 193 C CG2 . THR A 24 ? 0.2641 0.3265 0.2425 -0.0066 0.0121 -0.0051 24 THR A CG2 194 N N . LEU A 25 ? 0.2459 0.3429 0.2537 0.0010 0.0052 -0.0063 25 LEU A N 195 C CA . LEU A 25 ? 0.2496 0.3417 0.2674 -0.0026 -0.0014 -0.0077 25 LEU A CA 196 C C . LEU A 25 ? 0.2463 0.3376 0.2605 -0.0039 -0.0028 0.0022 25 LEU A C 197 O O . LEU A 25 ? 0.2192 0.3273 0.2429 0.0059 0.0137 0.0009 25 LEU A O 198 C CB . LEU A 25 ? 0.2542 0.3494 0.2755 -0.0004 -0.0122 -0.0093 25 LEU A CB 199 C CG . LEU A 25 ? 0.2667 0.3370 0.2658 0.0065 0.0005 -0.0009 25 LEU A CG 200 C CD1 . LEU A 25 ? 0.2971 0.3664 0.3140 -0.0016 0.0018 0.0040 25 LEU A CD1 201 C CD2 . LEU A 25 ? 0.2689 0.3452 0.2858 -0.0054 -0.0080 -0.0080 25 LEU A CD2 202 N N . ALA A 26 ? 0.2360 0.3303 0.2662 -0.0114 0.0017 0.0056 26 ALA A N 203 C CA . ALA A 26 ? 0.2350 0.3257 0.2561 -0.0105 0.0044 0.0097 26 ALA A CA 204 C C . ALA A 26 ? 0.2268 0.3150 0.2533 -0.0088 0.0005 0.0044 26 ALA A C 205 O O . ALA A 26 ? 0.2261 0.3248 0.2427 -0.0121 0.0006 -0.0003 26 ALA A O 206 C CB . ALA A 26 ? 0.2535 0.3301 0.2720 -0.0169 0.0048 0.0156 26 ALA A CB 207 N N . GLU A 27 ? 0.2025 0.3059 0.2314 -0.0057 0.0029 0.0051 27 GLU A N 208 C CA . GLU A 27 ? 0.2121 0.3021 0.2248 -0.0048 0.0056 0.0054 27 GLU A CA 209 C C . GLU A 27 ? 0.2061 0.2843 0.2235 -0.0020 0.0080 0.0095 27 GLU A C 210 O O . GLU A 27 ? 0.1882 0.3013 0.2132 -0.0070 0.0061 0.0141 27 GLU A O 211 C CB . GLU A 27 ? 0.1981 0.2868 0.2277 -0.0024 -0.0015 0.0027 27 GLU A CB 212 C CG . GLU A 27 ? 0.2240 0.3053 0.2152 0.0051 0.0058 0.0017 27 GLU A CG 213 C CD . GLU A 27 ? 0.2186 0.2929 0.2258 -0.0012 0.0009 0.0017 27 GLU A CD 214 O OE1 . GLU A 27 ? 0.2405 0.3229 0.2345 -0.0035 0.0242 -0.0202 27 GLU A OE1 215 O OE2 . GLU A 27 ? 0.1925 0.3591 0.2189 -0.0044 0.0147 -0.0052 27 GLU A OE2 216 N N . LYS A 28 ? 0.1984 0.2841 0.2181 -0.0042 0.0062 0.0097 28 LYS A N 217 C CA . LYS A 28 ? 0.2085 0.2661 0.2265 0.0007 0.0015 0.0081 28 LYS A CA 218 C C . LYS A 28 ? 0.2029 0.2682 0.2258 -0.0048 0.0015 0.0042 28 LYS A C 219 O O . LYS A 28 ? 0.1826 0.2534 0.2123 -0.0148 0.0022 0.0000 28 LYS A O 220 C CB . LYS A 28 ? 0.2339 0.2755 0.2480 0.0054 0.0023 0.0019 28 LYS A CB 221 C CG . LYS A 28 ? 0.2299 0.2519 0.2447 -0.0014 0.0085 0.0041 28 LYS A CG 222 C CD . LYS A 28 ? 0.2677 0.2732 0.2709 0.0145 0.0031 0.0053 28 LYS A CD 223 C CE . LYS A 28 ? 0.2879 0.3017 0.2616 0.0119 0.0039 -0.0005 28 LYS A CE 224 N NZ . LYS A 28 ? 0.2921 0.3074 0.2644 0.0213 0.0177 0.0006 28 LYS A NZ 225 N N . ILE A 29 ? 0.1986 0.2670 0.2215 -0.0046 -0.0005 0.0047 29 ILE A N 226 C CA . ILE A 29 ? 0.1980 0.2835 0.2261 -0.0052 0.0002 0.0016 29 ILE A CA 227 C C . ILE A 29 ? 0.2073 0.2822 0.2176 -0.0008 -0.0013 0.0038 29 ILE A C 228 O O . ILE A 29 ? 0.1935 0.2985 0.2064 -0.0010 -0.0029 0.0012 29 ILE A O 229 C CB . ILE A 29 ? 0.1996 0.2695 0.2201 -0.0082 0.0006 0.0064 29 ILE A CB 230 C CG1 . ILE A 29 ? 0.1978 0.3042 0.2491 -0.0057 -0.0004 0.0025 29 ILE A CG1 231 C CG2 . ILE A 29 ? 0.2237 0.2880 0.2290 -0.0006 -0.0027 -0.0069 29 ILE A CG2 232 C CD1 . ILE A 29 ? 0.2056 0.3107 0.2602 -0.0067 0.0045 0.0084 29 ILE A CD1 233 N N . GLY A 30 ? 0.2025 0.2858 0.2163 -0.0079 0.0048 0.0130 30 GLY A N 234 C CA . GLY A 30 ? 0.1986 0.2763 0.2130 -0.0060 0.0059 0.0100 30 GLY A CA 235 C C . GLY A 30 ? 0.1968 0.2709 0.2142 -0.0020 0.0095 0.0072 30 GLY A C 236 O O . GLY A 30 ? 0.1910 0.2678 0.2206 0.0063 0.0107 0.0087 30 GLY A O 237 N N . GLN A 31 ? 0.1946 0.2682 0.2077 0.0025 0.0088 0.0035 31 GLN A N 238 C CA . GLN A 31 ? 0.1974 0.2655 0.2145 0.0008 0.0052 -0.0003 31 GLN A CA 239 C C . GLN A 31 ? 0.1999 0.2668 0.2174 0.0067 0.0077 0.0024 31 GLN A C 240 O O . GLN A 31 ? 0.1957 0.2786 0.2241 0.0199 0.0109 0.0022 31 GLN A O 241 C CB . GLN A 31 ? 0.2022 0.2675 0.2194 0.0073 0.0039 0.0038 31 GLN A CB 242 C CG . GLN A 31 ? 0.2052 0.2413 0.2197 0.0035 -0.0103 -0.0092 31 GLN A CG 243 C CD . GLN A 31 ? 0.1982 0.2570 0.2344 0.0011 0.0009 -0.0017 31 GLN A CD 244 O OE1 . GLN A 31 ? 0.2037 0.3155 0.2246 0.0040 0.0080 -0.0009 31 GLN A OE1 245 N NE2 . GLN A 31 ? 0.1957 0.2652 0.2155 0.0099 0.0121 -0.0085 31 GLN A NE2 246 N N . MET A 32 ? 0.2000 0.2676 0.2139 0.0087 0.0001 0.0054 32 MET A N 247 C CA . MET A 32 ? 0.1999 0.2772 0.2217 0.0112 0.0023 0.0110 32 MET A CA 248 C C . MET A 32 ? 0.2018 0.2716 0.2227 0.0013 0.0016 0.0095 32 MET A C 249 O O . MET A 32 ? 0.2121 0.2692 0.2203 -0.0045 0.0138 0.0105 32 MET A O 250 C CB . MET A 32 ? 0.1862 0.2637 0.2293 0.0174 0.0020 0.0147 32 MET A CB 251 C CG . MET A 32 ? 0.2066 0.2771 0.2408 0.0080 -0.0030 -0.0032 32 MET A CG 252 S SD . MET A 32 ? 0.2028 0.3290 0.2363 0.0260 0.0118 0.0123 32 MET A SD 253 C CE . MET A 32 ? 0.2529 0.3308 0.2430 0.0016 0.0006 0.0138 32 MET A CE 254 N N . THR A 33 ? 0.1810 0.2562 0.2071 -0.0024 0.0085 0.0143 33 THR A N 255 C CA . THR A 33 ? 0.1888 0.2551 0.2055 -0.0015 0.0139 0.0129 33 THR A CA 256 C C . THR A 33 ? 0.1951 0.2591 0.1977 -0.0042 0.0153 0.0067 33 THR A C 257 O O . THR A 33 ? 0.1937 0.2725 0.1896 0.0026 0.0154 0.0138 33 THR A O 258 C CB . THR A 33 ? 0.1935 0.2579 0.2041 0.0004 0.0172 0.0132 33 THR A CB 259 O OG1 . THR A 33 ? 0.2015 0.2811 0.2224 0.0114 0.0133 0.0050 33 THR A OG1 260 C CG2 . THR A 33 ? 0.2217 0.2622 0.2002 -0.0105 0.0195 0.0136 33 THR A CG2 261 N N . GLN A 34 ? 0.1898 0.2521 0.1746 -0.0085 0.0215 0.0095 34 GLN A N 262 C CA . GLN A 34 ? 0.1999 0.2345 0.1705 -0.0067 0.0161 0.0095 34 GLN A CA 263 C C . GLN A 34 ? 0.2084 0.2384 0.1830 -0.0065 0.0108 0.0092 34 GLN A C 264 O O . GLN A 34 ? 0.2132 0.2376 0.1789 0.0009 0.0042 0.0104 34 GLN A O 265 C CB . GLN A 34 ? 0.1927 0.2400 0.1679 -0.0056 0.0201 0.0054 34 GLN A CB 266 C CG . GLN A 34 ? 0.1722 0.2449 0.1787 -0.0101 0.0188 0.0167 34 GLN A CG 267 C CD . GLN A 34 ? 0.1880 0.2152 0.1640 -0.0070 0.0165 0.0047 34 GLN A CD 268 O OE1 . GLN A 34 ? 0.2230 0.2278 0.1569 -0.0192 0.0120 0.0232 34 GLN A OE1 269 N NE2 . GLN A 34 ? 0.1820 0.2308 0.1770 -0.0062 0.0091 0.0063 34 GLN A NE2 270 N N . ILE A 35 ? 0.2090 0.2480 0.1774 -0.0043 0.0136 0.0122 35 ILE A N 271 C CA . ILE A 35 ? 0.2044 0.2490 0.1822 -0.0038 0.0163 0.0103 35 ILE A CA 272 C C . ILE A 35 ? 0.2012 0.2437 0.1819 -0.0015 0.0129 0.0071 35 ILE A C 273 O O . ILE A 35 ? 0.1903 0.2449 0.2025 0.0016 0.0228 0.0022 35 ILE A O 274 C CB . ILE A 35 ? 0.2054 0.2640 0.1824 -0.0068 0.0075 0.0122 35 ILE A CB 275 C CG1 . ILE A 35 ? 0.2121 0.2722 0.1754 -0.0150 0.0102 0.0149 35 ILE A CG1 276 C CG2 . ILE A 35 ? 0.2222 0.2527 0.2062 0.0009 0.0178 -0.0040 35 ILE A CG2 277 C CD1 . ILE A 35 ? 0.2039 0.2827 0.1755 -0.0132 0.0211 0.0218 35 ILE A CD1 278 N N . GLU A 36 ? 0.2129 0.2397 0.1984 0.0030 0.0137 0.0092 36 GLU A N 279 C CA . GLU A 36 ? 0.2143 0.2446 0.2039 0.0038 0.0072 0.0100 36 GLU A CA 280 C C . GLU A 36 ? 0.2144 0.2454 0.2059 0.0028 0.0060 0.0123 36 GLU A C 281 O O . GLU A 36 ? 0.2099 0.2600 0.2214 -0.0007 0.0114 0.0146 36 GLU A O 282 C CB . GLU A 36 ? 0.2244 0.2461 0.2148 0.0007 0.0038 0.0022 36 GLU A CB 283 C CG . GLU A 36 ? 0.2339 0.2534 0.2034 0.0069 0.0052 0.0020 36 GLU A CG 284 C CD . GLU A 36 ? 0.2565 0.2747 0.2397 -0.0005 0.0002 0.0017 36 GLU A CD 285 O OE1 . GLU A 36 ? 0.2615 0.3070 0.2586 0.0263 -0.0078 0.0229 36 GLU A OE1 286 O OE2 . GLU A 36 ? 0.2524 0.2887 0.2623 -0.0082 0.0153 0.0014 36 GLU A OE2 287 N N . ARG A 37 ? 0.2063 0.2388 0.2025 0.0010 0.0024 0.0183 37 ARG A N 288 C CA . ARG A 37 ? 0.2091 0.2356 0.2121 -0.0013 -0.0017 0.0195 37 ARG A CA 289 C C . ARG A 37 ? 0.2302 0.2478 0.2265 -0.0075 -0.0028 0.0115 37 ARG A C 290 O O . ARG A 37 ? 0.2367 0.2591 0.2270 -0.0176 0.0058 0.0213 37 ARG A O 291 C CB . ARG A 37 ? 0.2078 0.2226 0.2128 0.0050 0.0062 0.0118 37 ARG A CB 292 C CG . ARG A 37 ? 0.1930 0.2353 0.2017 0.0161 0.0117 0.0099 37 ARG A CG 293 C CD . ARG A 37 ? 0.1960 0.1964 0.2034 0.0083 -0.0047 0.0304 37 ARG A CD 294 N NE . ARG A 37 ? 0.2142 0.1998 0.2118 0.0084 -0.0011 0.0394 37 ARG A NE 295 C CZ . ARG A 37 ? 0.2179 0.2164 0.2133 -0.0002 0.0050 0.0210 37 ARG A CZ 296 N NH1 . ARG A 37 ? 0.2481 0.2190 0.2178 -0.0036 -0.0121 0.0326 37 ARG A NH1 297 N NH2 . ARG A 37 ? 0.2695 0.2215 0.2351 -0.0033 0.0086 0.0153 37 ARG A NH2 298 N N . LEU A 38 ? 0.2377 0.2525 0.2351 -0.0084 -0.0023 0.0094 38 LEU A N 299 C CA . LEU A 38 ? 0.2470 0.2607 0.2462 -0.0142 0.0004 0.0014 38 LEU A CA 300 C C . LEU A 38 ? 0.2628 0.2725 0.2619 -0.0128 0.0030 0.0054 38 LEU A C 301 O O . LEU A 38 ? 0.2846 0.2832 0.2897 -0.0178 0.0091 0.0099 38 LEU A O 302 C CB . LEU A 38 ? 0.2530 0.2586 0.2468 -0.0108 0.0037 0.0021 38 LEU A CB 303 C CG . LEU A 38 ? 0.2731 0.2966 0.2892 -0.0067 -0.0002 0.0028 38 LEU A CG 304 C CD1 . LEU A 38 ? 0.2776 0.3259 0.2914 -0.0074 0.0019 -0.0077 38 LEU A CD1 305 C CD2 . LEU A 38 ? 0.3122 0.3014 0.3418 -0.0142 -0.0003 0.0095 38 LEU A CD2 306 N N . VAL A 39 ? 0.2556 0.2814 0.2486 -0.0115 -0.0038 0.0067 39 VAL A N 307 C CA . VAL A 39 ? 0.2634 0.2815 0.2528 -0.0102 -0.0008 0.0106 39 VAL A CA 308 C C . VAL A 39 ? 0.2640 0.2812 0.2520 -0.0098 -0.0002 0.0121 39 VAL A C 309 O O . VAL A 39 ? 0.2610 0.2999 0.2526 -0.0198 -0.0037 0.0117 39 VAL A O 310 C CB . VAL A 39 ? 0.2615 0.2813 0.2509 -0.0101 0.0000 0.0092 39 VAL A CB 311 C CG1 . VAL A 39 ? 0.2870 0.2941 0.2670 -0.0198 0.0060 0.0004 39 VAL A CG1 312 C CG2 . VAL A 39 ? 0.2636 0.2674 0.2432 -0.0072 -0.0078 0.0122 39 VAL A CG2 313 N N . ALA A 40 ? 0.2703 0.2844 0.2526 -0.0140 -0.0020 0.0165 40 ALA A N 314 C CA . ALA A 40 ? 0.2744 0.2856 0.2458 -0.0082 0.0032 0.0176 40 ALA A CA 315 C C . ALA A 40 ? 0.2869 0.2943 0.2607 -0.0046 0.0045 0.0176 40 ALA A C 316 O O . ALA A 40 ? 0.3029 0.2985 0.2587 0.0010 0.0080 0.0273 40 ALA A O 317 C CB . ALA A 40 ? 0.2715 0.2924 0.2548 -0.0105 0.0034 0.0148 40 ALA A CB 318 N N . THR A 41 ? 0.2913 0.3074 0.2560 -0.0043 0.0017 0.0237 41 THR A N 319 C CA . THR A 41 ? 0.2980 0.3184 0.2611 -0.0087 0.0019 0.0214 41 THR A CA 320 C C . THR A 41 ? 0.2963 0.3183 0.2622 -0.0095 -0.0036 0.0177 41 THR A C 321 O O . THR A 41 ? 0.2836 0.3141 0.2359 -0.0048 -0.0010 0.0148 41 THR A O 322 C CB . THR A 41 ? 0.3018 0.3106 0.2695 -0.0080 -0.0028 0.0232 41 THR A CB 323 O OG1 . THR A 41 ? 0.2999 0.3041 0.2681 -0.0102 0.0157 0.0311 41 THR A OG1 324 C CG2 . THR A 41 ? 0.3214 0.3282 0.2819 -0.0062 -0.0055 0.0184 41 THR A CG2 325 N N . PRO A 42 ? 0.3054 0.3267 0.2608 -0.0062 -0.0038 0.0169 42 PRO A N 326 C CA . PRO A 42 ? 0.3080 0.3348 0.2603 -0.0084 -0.0056 0.0154 42 PRO A CA 327 C C . PRO A 42 ? 0.3022 0.3286 0.2538 -0.0135 -0.0008 0.0140 42 PRO A C 328 O O . PRO A 42 ? 0.2734 0.3241 0.2380 -0.0265 0.0030 0.0174 42 PRO A O 329 C CB . PRO A 42 ? 0.3204 0.3437 0.2701 0.0029 -0.0112 0.0194 42 PRO A CB 330 C CG . PRO A 42 ? 0.3353 0.3489 0.2774 -0.0015 -0.0114 0.0088 42 PRO A CG 331 C CD . PRO A 42 ? 0.3188 0.3356 0.2724 -0.0064 -0.0085 0.0126 42 PRO A CD 332 N N . ASP A 43 ? 0.3106 0.3398 0.2702 -0.0166 0.0028 0.0140 43 ASP A N 333 C CA . ASP A 43 ? 0.3149 0.3381 0.2797 -0.0179 0.0047 0.0122 43 ASP A CA 334 C C . ASP A 43 ? 0.2950 0.3224 0.2673 -0.0166 0.0094 0.0095 43 ASP A C 335 O O . ASP A 43 ? 0.2961 0.3268 0.2569 -0.0218 0.0256 0.0089 43 ASP A O 336 C CB . ASP A 43 ? 0.3437 0.3538 0.3051 -0.0175 0.0065 0.0177 43 ASP A CB 337 C CG . ASP A 43 ? 0.4083 0.4017 0.3436 -0.0158 -0.0005 0.0162 43 ASP A CG 338 O OD1 . ASP A 43 ? 0.4613 0.4253 0.3786 -0.0266 -0.0010 0.0150 43 ASP A OD1 339 O OD2 . ASP A 43 ? 0.4726 0.4126 0.4100 -0.0209 0.0027 0.0218 43 ASP A OD2 340 N N . VAL A 44 ? 0.2653 0.3130 0.2467 -0.0156 0.0091 0.0114 44 VAL A N 341 C CA . VAL A 44 ? 0.2527 0.2978 0.2296 -0.0185 0.0068 -0.0010 44 VAL A CA 342 C C . VAL A 44 ? 0.2404 0.2893 0.2188 -0.0120 0.0103 0.0014 44 VAL A C 343 O O . VAL A 44 ? 0.2170 0.3070 0.2274 -0.0190 0.0150 -0.0012 44 VAL A O 344 C CB . VAL A 44 ? 0.2472 0.2860 0.2312 -0.0203 0.0056 -0.0010 44 VAL A CB 345 C CG1 . VAL A 44 ? 0.2581 0.2923 0.2396 -0.0277 -0.0015 0.0056 44 VAL A CG1 346 C CG2 . VAL A 44 ? 0.2824 0.2877 0.2452 -0.0283 -0.0020 -0.0071 44 VAL A CG2 347 N N . LEU A 45 ? 0.2374 0.2874 0.2173 -0.0121 0.0041 -0.0001 45 LEU A N 348 C CA . LEU A 45 ? 0.2334 0.2881 0.2241 -0.0105 0.0091 0.0031 45 LEU A CA 349 C C . LEU A 45 ? 0.2438 0.2860 0.2315 -0.0098 0.0054 0.0056 45 LEU A C 350 O O . LEU A 45 ? 0.2299 0.2857 0.2122 -0.0018 0.0126 0.0056 45 LEU A O 351 C CB . LEU A 45 ? 0.2289 0.2873 0.2269 -0.0037 0.0065 0.0042 45 LEU A CB 352 C CG . LEU A 45 ? 0.2542 0.2936 0.2358 0.0010 0.0030 0.0118 45 LEU A CG 353 C CD1 . LEU A 45 ? 0.2558 0.3062 0.2581 0.0073 0.0138 0.0182 45 LEU A CD1 354 C CD2 . LEU A 45 ? 0.2696 0.3143 0.2224 0.0056 0.0027 0.0110 45 LEU A CD2 355 N N . ARG A 46 ? 0.2707 0.2928 0.2396 -0.0151 0.0129 0.0114 46 ARG A N 356 C CA . ARG A 46 ? 0.2951 0.3139 0.2563 -0.0146 0.0085 0.0108 46 ARG A CA 357 C C . ARG A 46 ? 0.2885 0.3122 0.2505 -0.0167 0.0176 0.0088 46 ARG A C 358 O O . ARG A 46 ? 0.2820 0.3316 0.2444 -0.0286 0.0245 0.0026 46 ARG A O 359 C CB . ARG A 46 ? 0.3242 0.3277 0.2730 -0.0133 0.0100 0.0140 46 ARG A CB 360 C CG . ARG A 46 ? 0.3823 0.3773 0.3475 -0.0148 0.0049 -0.0104 46 ARG A CG 361 C CD . ARG A 46 ? 0.3525 0.3988 0.3769 0.0325 -0.0123 0.0219 46 ARG A CD 362 N NE . ARG A 46 ? 0.5510 0.6233 0.4745 -0.0450 0.0040 0.0237 46 ARG A NE 363 C CZ . ARG A 46 ? 0.3803 0.3754 0.5124 0.0004 -0.0156 -0.0369 46 ARG A CZ 364 N NH1 . ARG A 46 ? 0.5823 0.5449 0.4933 -0.0209 0.0024 0.0092 46 ARG A NH1 365 N NH2 . ARG A 46 ? 0.6094 0.6087 0.4837 0.0341 0.0170 0.0236 46 ARG A NH2 366 N N . ASP A 47 ? 0.2766 0.3224 0.2448 -0.0203 0.0147 0.0008 47 ASP A N 367 C CA . ASP A 47 ? 0.2783 0.3169 0.2587 -0.0161 0.0169 0.0007 47 ASP A CA 368 C C . ASP A 47 ? 0.2661 0.3083 0.2553 -0.0185 0.0147 -0.0026 47 ASP A C 369 O O . ASP A 47 ? 0.2854 0.3129 0.2510 -0.0159 0.0379 -0.0003 47 ASP A O 370 C CB . ASP A 47 ? 0.2816 0.3162 0.2620 -0.0126 0.0141 -0.0009 47 ASP A CB 371 C CG . ASP A 47 ? 0.3268 0.3465 0.2832 -0.0194 0.0130 0.0007 47 ASP A CG 372 O OD1 . ASP A 47 ? 0.3750 0.3600 0.3114 -0.0305 0.0289 0.0186 47 ASP A OD1 373 O OD2 . ASP A 47 ? 0.3644 0.3909 0.2415 -0.0238 0.0209 0.0121 47 ASP A OD2 374 N N . ASN A 48 ? 0.2442 0.2874 0.2414 -0.0260 0.0198 -0.0075 48 ASN A N 375 C CA . ASN A 48 ? 0.2407 0.2771 0.2346 -0.0238 0.0112 -0.0117 48 ASN A CA 376 C C . ASN A 48 ? 0.2300 0.2739 0.2251 -0.0219 0.0119 -0.0054 48 ASN A C 377 O O . ASN A 48 ? 0.2250 0.2849 0.2250 -0.0325 0.0047 -0.0035 48 ASN A O 378 C CB . ASN A 48 ? 0.2520 0.2789 0.2422 -0.0266 0.0093 -0.0082 48 ASN A CB 379 C CG . ASN A 48 ? 0.2456 0.2839 0.2525 -0.0206 0.0127 -0.0014 48 ASN A CG 380 O OD1 . ASN A 48 ? 0.2460 0.3119 0.2762 -0.0219 0.0260 0.0026 48 ASN A OD1 381 N ND2 . ASN A 48 ? 0.2603 0.2785 0.2470 -0.0224 0.0248 0.0021 48 ASN A ND2 382 N N . PHE A 49 ? 0.2147 0.2716 0.2054 -0.0163 0.0173 -0.0066 49 PHE A N 383 C CA . PHE A 49 ? 0.2164 0.2699 0.2043 -0.0161 0.0148 -0.0096 49 PHE A CA 384 C C . PHE A 49 ? 0.2028 0.2603 0.1978 -0.0171 0.0096 -0.0062 49 PHE A C 385 O O . PHE A 49 ? 0.1896 0.2663 0.2015 -0.0178 0.0110 -0.0121 49 PHE A O 386 C CB . PHE A 49 ? 0.2243 0.2833 0.2103 -0.0114 0.0167 -0.0007 49 PHE A CB 387 C CG . PHE A 49 ? 0.2411 0.3062 0.2194 -0.0131 0.0186 -0.0061 49 PHE A CG 388 C CD1 . PHE A 49 ? 0.2502 0.3010 0.2100 -0.0164 0.0189 0.0000 49 PHE A CD1 389 C CD2 . PHE A 49 ? 0.2585 0.3292 0.2312 -0.0154 0.0264 -0.0019 49 PHE A CD2 390 C CE1 . PHE A 49 ? 0.2483 0.3278 0.2311 -0.0155 0.0176 -0.0020 49 PHE A CE1 391 C CE2 . PHE A 49 ? 0.2464 0.3252 0.2402 -0.0110 0.0313 -0.0008 49 PHE A CE2 392 C CZ . PHE A 49 ? 0.2414 0.3264 0.2426 -0.0118 0.0223 -0.0026 49 PHE A CZ 393 N N . ILE A 50 ? 0.2027 0.2650 0.1894 -0.0166 0.0174 -0.0091 50 ILE A N 394 C CA . ILE A 50 ? 0.2039 0.2515 0.1894 -0.0185 0.0192 -0.0068 50 ILE A CA 395 C C . ILE A 50 ? 0.1994 0.2557 0.2009 -0.0138 0.0198 -0.0042 50 ILE A C 396 O O . ILE A 50 ? 0.2077 0.2699 0.1998 -0.0271 0.0152 0.0054 50 ILE A O 397 C CB . ILE A 50 ? 0.2008 0.2545 0.1920 -0.0139 0.0185 -0.0042 50 ILE A CB 398 C CG1 . ILE A 50 ? 0.2077 0.2586 0.1953 -0.0175 0.0057 0.0033 50 ILE A CG1 399 C CG2 . ILE A 50 ? 0.2119 0.2556 0.1745 -0.0105 0.0291 -0.0069 50 ILE A CG2 400 C CD1 . ILE A 50 ? 0.2116 0.2583 0.1912 -0.0123 0.0009 0.0064 50 ILE A CD1 401 N N . GLY A 51 ? 0.1963 0.2332 0.1923 -0.0184 0.0237 -0.0006 51 GLY A N 402 C CA . GLY A 51 ? 0.2002 0.2406 0.2072 -0.0136 0.0299 -0.0015 51 GLY A CA 403 C C . GLY A 51 ? 0.1963 0.2281 0.1872 -0.0132 0.0283 -0.0054 51 GLY A C 404 O O . GLY A 51 ? 0.1801 0.2361 0.1838 -0.0097 0.0196 -0.0134 51 GLY A O 405 N N . SER A 52 ? 0.1948 0.2250 0.1690 -0.0093 0.0305 0.0014 52 SER A N 406 C CA . SER A 52 ? 0.1953 0.2264 0.1743 -0.0015 0.0239 0.0029 52 SER A CA 407 C C . SER A 52 ? 0.1975 0.2321 0.1742 -0.0012 0.0195 0.0042 52 SER A C 408 O O . SER A 52 ? 0.1726 0.2327 0.1711 -0.0098 0.0115 -0.0028 52 SER A O 409 C CB . SER A 52 ? 0.2024 0.2365 0.1760 0.0043 0.0260 0.0033 52 SER A CB 410 O OG . SER A 52 ? 0.1997 0.2502 0.1629 -0.0106 0.0292 0.0125 52 SER A OG 411 N N . LEU A 53 ? 0.1819 0.2333 0.1721 -0.0029 0.0195 0.0079 53 LEU A N 412 C CA . LEU A 53 ? 0.1934 0.2440 0.1708 -0.0003 0.0221 0.0056 53 LEU A CA 413 C C . LEU A 53 ? 0.1983 0.2449 0.1716 0.0004 0.0195 0.0049 53 LEU A C 414 O O . LEU A 53 ? 0.2121 0.2482 0.1855 -0.0012 0.0204 -0.0092 53 LEU A O 415 C CB . LEU A 53 ? 0.2247 0.2339 0.1725 0.0000 0.0314 0.0116 53 LEU A CB 416 C CG . LEU A 53 ? 0.2348 0.2685 0.1995 -0.0085 0.0299 0.0187 53 LEU A CG 417 C CD1 . LEU A 53 ? 0.3184 0.3181 0.2482 -0.0147 0.0179 0.0032 53 LEU A CD1 418 C CD2 . LEU A 53 ? 0.3291 0.2892 0.3017 0.0075 0.0265 0.0206 53 LEU A CD2 419 N N . LEU A 54 ? 0.1947 0.2445 0.1716 0.0065 0.0144 0.0075 54 LEU A N 420 C CA . LEU A 54 ? 0.2018 0.2405 0.1610 0.0090 0.0102 0.0114 54 LEU A CA 421 C C . LEU A 54 ? 0.2099 0.2391 0.1707 0.0049 0.0037 0.0156 54 LEU A C 422 O O . LEU A 54 ? 0.2217 0.2310 0.1713 0.0091 0.0071 0.0195 54 LEU A O 423 C CB . LEU A 54 ? 0.1934 0.2474 0.1602 -0.0001 0.0054 0.0072 54 LEU A CB 424 C CG . LEU A 54 ? 0.2131 0.2538 0.1518 -0.0028 0.0018 0.0101 54 LEU A CG 425 C CD1 . LEU A 54 ? 0.2427 0.2671 0.1524 -0.0062 0.0062 0.0296 54 LEU A CD1 426 C CD2 . LEU A 54 ? 0.2196 0.2670 0.1872 0.0058 0.0040 -0.0007 54 LEU A CD2 427 N N . SER A 55 ? 0.2021 0.2303 0.1593 0.0091 0.0071 0.0178 55 SER A N 428 C CA . SER A 55 ? 0.2209 0.2295 0.1706 -0.0005 0.0026 0.0168 55 SER A CA 429 C C . SER A 55 ? 0.2278 0.2274 0.1762 0.0013 -0.0009 0.0095 55 SER A C 430 O O . SER A 55 ? 0.2288 0.2337 0.1623 -0.0113 0.0000 0.0172 55 SER A O 431 C CB . SER A 55 ? 0.2225 0.2358 0.1758 0.0077 -0.0009 0.0162 55 SER A CB 432 O OG . SER A 55 ? 0.2582 0.2351 0.1768 0.0086 0.0003 0.0305 55 SER A OG 433 N N . GLY A 56 ? 0.2144 0.2402 0.1773 0.0049 -0.0065 0.0102 56 GLY A N 434 C CA . GLY A 56 ? 0.2365 0.2446 0.1917 0.0051 0.0076 0.0000 56 GLY A CA 435 C C . GLY A 56 ? 0.2384 0.2372 0.1996 0.0060 0.0044 -0.0021 56 GLY A C 436 O O . GLY A 56 ? 0.2460 0.2413 0.1840 0.0063 0.0123 -0.0017 56 GLY A O 437 N N . GLY A 57 ? 0.2460 0.2369 0.2020 0.0059 0.0098 -0.0001 57 GLY A N 438 C CA . GLY A 57 ? 0.2473 0.2411 0.2092 0.0051 0.0076 0.0003 57 GLY A CA 439 C C . GLY A 57 ? 0.2596 0.2494 0.2085 -0.0002 0.0099 -0.0003 57 GLY A C 440 O O . GLY A 57 ? 0.2583 0.2646 0.2159 -0.0038 0.0093 -0.0006 57 GLY A O 441 N N . GLY A 58 ? 0.2644 0.2485 0.2058 0.0035 0.0118 0.0017 58 GLY A N 442 C CA . GLY A 58 ? 0.2727 0.2542 0.2159 0.0068 0.0100 0.0013 58 GLY A CA 443 C C . GLY A 58 ? 0.2659 0.2519 0.2162 0.0034 0.0106 0.0063 58 GLY A C 444 O O . GLY A 58 ? 0.2978 0.2637 0.2343 0.0116 0.0060 0.0012 58 GLY A O 445 N N . SER A 59 ? 0.2638 0.2455 0.2039 0.0032 0.0061 0.0072 59 SER A N 446 C CA . SER A 59 ? 0.2462 0.2475 0.2011 0.0082 0.0078 0.0044 59 SER A CA 447 C C . SER A 59 ? 0.2463 0.2393 0.2009 0.0037 0.0052 0.0077 59 SER A C 448 O O . SER A 59 ? 0.2583 0.2342 0.2075 0.0034 -0.0032 0.0130 59 SER A O 449 C CB . SER A 59 ? 0.2386 0.2544 0.1899 0.0091 0.0128 0.0061 59 SER A CB 450 O OG . SER A 59 ? 0.2313 0.2752 0.1970 0.0105 0.0225 0.0281 59 SER A OG 451 N N . VAL A 60 ? 0.2476 0.2329 0.1956 -0.0005 0.0049 0.0175 60 VAL A N 452 C CA . VAL A 60 ? 0.2534 0.2286 0.1991 -0.0029 0.0001 0.0238 60 VAL A CA 453 C C . VAL A 60 ? 0.2631 0.2373 0.2059 -0.0057 0.0048 0.0196 60 VAL A C 454 O O . VAL A 60 ? 0.2662 0.2426 0.2118 -0.0052 -0.0002 0.0225 60 VAL A O 455 C CB . VAL A 60 ? 0.2480 0.2201 0.1998 -0.0065 0.0060 0.0239 60 VAL A CB 456 C CG1 . VAL A 60 ? 0.2445 0.2521 0.1719 -0.0043 0.0103 0.0295 60 VAL A CG1 457 C CG2 . VAL A 60 ? 0.2602 0.2300 0.2322 0.0002 0.0002 0.0102 60 VAL A CG2 458 N N . PRO A 61 ? 0.2735 0.2472 0.2159 -0.0061 -0.0026 0.0240 61 PRO A N 459 C CA . PRO A 61 ? 0.2863 0.2526 0.2205 -0.0100 -0.0027 0.0254 61 PRO A CA 460 C C . PRO A 61 ? 0.2909 0.2644 0.2427 -0.0034 0.0007 0.0204 61 PRO A C 461 O O . PRO A 61 ? 0.2923 0.2665 0.2595 -0.0080 0.0115 0.0271 61 PRO A O 462 C CB . PRO A 61 ? 0.2920 0.2540 0.2495 -0.0143 -0.0048 0.0190 61 PRO A CB 463 C CG . PRO A 61 ? 0.2711 0.2604 0.2173 -0.0105 -0.0020 0.0161 61 PRO A CG 464 C CD . PRO A 61 ? 0.2784 0.2512 0.2193 -0.0091 -0.0015 0.0200 61 PRO A CD 465 N N . ARG A 62 ? 0.3045 0.2808 0.2642 0.0031 0.0038 0.0194 62 ARG A N 466 C CA . ARG A 62 ? 0.3235 0.3111 0.2930 0.0044 0.0090 0.0094 62 ARG A CA 467 C C . ARG A 62 ? 0.3259 0.3086 0.2958 0.0065 0.0093 0.0062 62 ARG A C 468 O O . ARG A 62 ? 0.3087 0.2832 0.2826 0.0089 0.0148 0.0104 62 ARG A O 469 C CB . ARG A 62 ? 0.3460 0.3229 0.3084 0.0090 0.0042 0.0145 62 ARG A CB 470 C CG . ARG A 62 ? 0.3786 0.3668 0.3524 0.0053 0.0038 0.0088 62 ARG A CG 471 C CD . ARG A 62 ? 0.4129 0.3921 0.4001 0.0077 -0.0123 0.0080 62 ARG A CD 472 N NE . ARG A 62 ? 0.4052 0.4190 0.4166 0.0043 -0.0159 -0.0026 62 ARG A NE 473 C CZ . ARG A 62 ? 0.4275 0.4493 0.4382 0.0065 -0.0033 -0.0046 62 ARG A CZ 474 N NH1 . ARG A 62 ? 0.4421 0.4367 0.4398 0.0227 -0.0134 -0.0053 62 ARG A NH1 475 N NH2 . ARG A 62 ? 0.4282 0.4647 0.4479 0.0064 0.0015 -0.0176 62 ARG A NH2 476 N N . LYS A 63 ? 0.3288 0.3135 0.3031 0.0012 0.0119 0.0027 63 LYS A N 477 C CA . LYS A 63 ? 0.3393 0.3283 0.3221 0.0041 0.0114 -0.0008 63 LYS A CA 478 C C . LYS A 63 ? 0.3262 0.3097 0.3053 0.0061 0.0127 0.0011 63 LYS A C 479 O O . LYS A 63 ? 0.3384 0.3086 0.3203 0.0069 0.0207 0.0106 63 LYS A O 480 C CB . LYS A 63 ? 0.3569 0.3472 0.3388 0.0023 0.0077 -0.0051 63 LYS A CB 481 C CG . LYS A 63 ? 0.4340 0.4209 0.3926 -0.0023 0.0107 0.0020 63 LYS A CG 482 C CD . LYS A 63 ? 0.4550 0.4591 0.4456 0.0151 -0.0054 0.0144 63 LYS A CD 483 C CE . LYS A 63 ? 0.5092 0.5097 0.5272 -0.0043 0.0017 0.0090 63 LYS A CE 484 N NZ . LYS A 63 ? 0.5366 0.5145 0.5085 0.0072 0.0097 -0.0095 63 LYS A NZ 485 N N . GLY A 64 ? 0.3155 0.2905 0.2860 0.0109 0.0156 0.0036 64 GLY A N 486 C CA . GLY A 64 ? 0.3053 0.2820 0.2728 0.0082 0.0149 0.0097 64 GLY A CA 487 C C . GLY A 64 ? 0.2894 0.2757 0.2631 0.0117 0.0132 0.0112 64 GLY A C 488 O O . GLY A 64 ? 0.2972 0.2827 0.2701 0.0299 0.0136 0.0179 64 GLY A O 489 N N . ALA A 65 ? 0.2827 0.2680 0.2520 0.0172 0.0101 0.0167 65 ALA A N 490 C CA . ALA A 65 ? 0.2620 0.2691 0.2393 0.0140 0.0058 0.0149 65 ALA A CA 491 C C . ALA A 65 ? 0.2669 0.2705 0.2362 0.0129 -0.0011 0.0117 65 ALA A C 492 O O . ALA A 65 ? 0.2630 0.2686 0.2328 0.0019 -0.0056 0.0177 65 ALA A O 493 C CB . ALA A 65 ? 0.2715 0.2758 0.2457 0.0179 0.0123 0.0098 65 ALA A CB 494 N N . THR A 66 ? 0.2571 0.2718 0.2279 0.0172 -0.0004 0.0158 66 THR A N 495 C CA . THR A 66 ? 0.2579 0.2738 0.2249 0.0192 -0.0068 0.0160 66 THR A CA 496 C C . THR A 66 ? 0.2531 0.2761 0.2185 0.0135 -0.0048 0.0159 66 THR A C 497 O O . THR A 66 ? 0.2396 0.2759 0.2109 0.0194 -0.0096 0.0270 66 THR A O 498 C CB . THR A 66 ? 0.2620 0.2776 0.2255 0.0215 -0.0004 0.0137 66 THR A CB 499 O OG1 . THR A 66 ? 0.2656 0.2964 0.2157 0.0422 -0.0042 0.0355 66 THR A OG1 500 C CG2 . THR A 66 ? 0.2667 0.2700 0.2469 0.0236 -0.0117 0.0250 66 THR A CG2 501 N N . ALA A 67 ? 0.2485 0.2857 0.2145 0.0140 -0.0071 0.0165 67 ALA A N 502 C CA . ALA A 67 ? 0.2389 0.2835 0.2182 0.0080 0.0042 0.0102 67 ALA A CA 503 C C . ALA A 67 ? 0.2375 0.2867 0.2184 0.0100 0.0044 0.0135 67 ALA A C 504 O O . ALA A 67 ? 0.2131 0.2972 0.2081 0.0093 0.0006 0.0145 67 ALA A O 505 C CB . ALA A 67 ? 0.2281 0.2824 0.2406 0.0111 0.0036 0.0078 67 ALA A CB 506 N N . LYS A 68 ? 0.2293 0.2880 0.2006 0.0056 0.0053 0.0144 68 LYS A N 507 C CA . LYS A 68 ? 0.2545 0.2934 0.2221 0.0074 0.0007 0.0185 68 LYS A CA 508 C C . LYS A 68 ? 0.2477 0.2781 0.2101 0.0150 -0.0012 0.0266 68 LYS A C 509 O O . LYS A 68 ? 0.2465 0.2915 0.2054 0.0225 -0.0031 0.0297 68 LYS A O 510 C CB A LYS A 68 ? 0.2507 0.2974 0.2198 0.0095 -0.0008 0.0155 68 LYS A CB 511 C CB B LYS A 68 ? 0.2460 0.2976 0.2143 0.0082 -0.0010 0.0143 68 LYS A CB 512 C CG A LYS A 68 ? 0.2853 0.3004 0.2427 0.0073 0.0069 0.0063 68 LYS A CG 513 C CG B LYS A 68 ? 0.2700 0.3007 0.2368 0.0000 0.0022 0.0152 68 LYS A CG 514 C CD A LYS A 68 ? 0.3235 0.3276 0.3187 0.0082 -0.0027 0.0014 68 LYS A CD 515 C CD B LYS A 68 ? 0.2729 0.2960 0.2452 0.0066 -0.0033 0.0148 68 LYS A CD 516 C CE A LYS A 68 ? 0.3451 0.3133 0.3106 -0.0052 -0.0002 -0.0108 68 LYS A CE 517 C CE B LYS A 68 ? 0.2895 0.2990 0.2597 -0.0002 -0.0032 0.0028 68 LYS A CE 518 N NZ A LYS A 68 ? 0.3515 0.3729 0.3660 0.0137 -0.0061 0.0100 68 LYS A NZ 519 N NZ B LYS A 68 ? 0.3191 0.3095 0.2996 -0.0052 -0.0105 0.0137 68 LYS A NZ 520 N N . GLU A 69 ? 0.2471 0.2710 0.2098 0.0131 -0.0035 0.0309 69 GLU A N 521 C CA . GLU A 69 ? 0.2506 0.2561 0.2176 0.0107 0.0008 0.0271 69 GLU A CA 522 C C . GLU A 69 ? 0.2431 0.2557 0.2048 0.0064 -0.0007 0.0283 69 GLU A C 523 O O . GLU A 69 ? 0.2428 0.2518 0.1966 0.0085 0.0102 0.0325 69 GLU A O 524 C CB . GLU A 69 ? 0.2614 0.2536 0.2306 0.0153 -0.0051 0.0286 69 GLU A CB 525 C CG . GLU A 69 ? 0.2843 0.2545 0.2357 0.0072 0.0246 0.0505 69 GLU A CG 526 C CD . GLU A 69 ? 0.3218 0.2920 0.2704 0.0047 0.0032 0.0413 69 GLU A CD 527 O OE1 . GLU A 69 ? 0.3273 0.3235 0.2432 0.0285 0.0171 0.0577 69 GLU A OE1 528 O OE2 . GLU A 69 ? 0.3293 0.3302 0.2837 0.0074 -0.0128 0.0570 69 GLU A OE2 529 N N . TRP A 70 ? 0.2358 0.2471 0.1888 0.0061 -0.0040 0.0261 70 TRP A N 530 C CA . TRP A 70 ? 0.2233 0.2437 0.1882 0.0013 0.0037 0.0239 70 TRP A CA 531 C C . TRP A 70 ? 0.2183 0.2450 0.1878 -0.0025 -0.0025 0.0204 70 TRP A C 532 O O . TRP A 70 ? 0.2109 0.2658 0.1753 0.0031 -0.0021 0.0087 70 TRP A O 533 C CB . TRP A 70 ? 0.2212 0.2399 0.1870 -0.0025 0.0068 0.0234 70 TRP A CB 534 C CG . TRP A 70 ? 0.1961 0.2156 0.1874 -0.0160 0.0136 0.0172 70 TRP A CG 535 C CD1 . TRP A 70 ? 0.2252 0.2165 0.2037 -0.0139 -0.0063 0.0177 70 TRP A CD1 536 C CD2 . TRP A 70 ? 0.2055 0.2244 0.1917 -0.0007 -0.0002 0.0149 70 TRP A CD2 537 N NE1 . TRP A 70 ? 0.2270 0.2500 0.1991 -0.0024 0.0066 0.0132 70 TRP A NE1 538 C CE2 . TRP A 70 ? 0.2185 0.2143 0.2039 -0.0152 -0.0024 0.0183 70 TRP A CE2 539 C CE3 . TRP A 70 ? 0.2250 0.2292 0.1981 -0.0086 0.0028 0.0071 70 TRP A CE3 540 C CZ2 . TRP A 70 ? 0.2061 0.2292 0.1923 -0.0132 -0.0016 0.0306 70 TRP A CZ2 541 C CZ3 . TRP A 70 ? 0.2224 0.2268 0.1992 -0.0036 0.0045 0.0180 70 TRP A CZ3 542 C CH2 . TRP A 70 ? 0.2245 0.2069 0.1866 -0.0038 0.0065 0.0250 70 TRP A CH2 543 N N . GLN A 71 ? 0.2187 0.2606 0.1804 -0.0007 -0.0110 0.0157 71 GLN A N 544 C CA . GLN A 71 ? 0.2193 0.2740 0.1986 -0.0103 -0.0048 0.0134 71 GLN A CA 545 C C . GLN A 71 ? 0.2233 0.2839 0.1916 -0.0056 -0.0051 0.0141 71 GLN A C 546 O O . GLN A 71 ? 0.2411 0.3043 0.1954 -0.0076 -0.0028 0.0235 71 GLN A O 547 C CB . GLN A 71 ? 0.2118 0.2823 0.2012 -0.0113 -0.0097 0.0089 71 GLN A CB 548 C CG . GLN A 71 ? 0.2100 0.2817 0.2235 -0.0185 0.0040 0.0027 71 GLN A CG 549 C CD . GLN A 71 ? 0.2384 0.3020 0.2312 -0.0131 0.0000 -0.0072 71 GLN A CD 550 O OE1 . GLN A 71 ? 0.2684 0.3668 0.2489 -0.0359 0.0128 -0.0052 71 GLN A OE1 551 N NE2 . GLN A 71 ? 0.2108 0.3292 0.1936 -0.0050 -0.0060 -0.0051 71 GLN A NE2 552 N N . ASP A 72 ? 0.2384 0.3024 0.1981 -0.0096 0.0008 0.0175 72 ASP A N 553 C CA . ASP A 72 ? 0.2395 0.3089 0.2192 -0.0028 0.0046 0.0226 72 ASP A CA 554 C C . ASP A 72 ? 0.2478 0.3106 0.2125 -0.0011 -0.0003 0.0126 72 ASP A C 555 O O . ASP A 72 ? 0.2408 0.3311 0.1900 0.0053 0.0026 0.0179 72 ASP A O 556 C CB . ASP A 72 ? 0.2618 0.3157 0.2283 0.0014 0.0066 0.0241 72 ASP A CB 557 C CG . ASP A 72 ? 0.2931 0.3420 0.2567 0.0017 0.0033 0.0209 72 ASP A CG 558 O OD1 . ASP A 72 ? 0.3196 0.3733 0.2853 -0.0090 -0.0373 0.0264 72 ASP A OD1 559 O OD2 . ASP A 72 ? 0.3375 0.3964 0.3062 0.0326 -0.0020 0.0346 72 ASP A OD2 560 N N . MET A 73 ? 0.2394 0.2949 0.1986 -0.0015 -0.0023 0.0115 73 MET A N 561 C CA . MET A 73 ? 0.2452 0.2825 0.1915 -0.0020 -0.0037 0.0055 73 MET A CA 562 C C . MET A 73 ? 0.2352 0.2707 0.1824 -0.0029 -0.0012 0.0043 73 MET A C 563 O O . MET A 73 ? 0.2329 0.2602 0.1711 -0.0007 0.0065 0.0101 73 MET A O 564 C CB . MET A 73 ? 0.2350 0.2791 0.1890 0.0044 -0.0051 0.0025 73 MET A CB 565 C CG . MET A 73 ? 0.2415 0.2892 0.2003 -0.0123 -0.0024 -0.0032 73 MET A CG 566 S SD . MET A 73 ? 0.2875 0.3279 0.1944 -0.0072 -0.0047 0.0096 73 MET A SD 567 C CE . MET A 73 ? 0.2708 0.3197 0.2517 -0.0008 -0.0123 0.0117 73 MET A CE 568 N N . VAL A 74 ? 0.2313 0.2580 0.1671 -0.0032 0.0036 0.0030 74 VAL A N 569 C CA . VAL A 74 ? 0.2386 0.2623 0.1861 -0.0080 0.0113 0.0032 74 VAL A CA 570 C C . VAL A 74 ? 0.2374 0.2713 0.1842 -0.0049 0.0051 0.0021 74 VAL A C 571 O O . VAL A 74 ? 0.2363 0.2732 0.1839 -0.0133 -0.0011 0.0052 74 VAL A O 572 C CB . VAL A 74 ? 0.2595 0.2585 0.2019 -0.0080 0.0101 0.0011 74 VAL A CB 573 C CG1 . VAL A 74 ? 0.2551 0.2561 0.2294 -0.0022 0.0287 0.0080 74 VAL A CG1 574 C CG2 . VAL A 74 ? 0.2493 0.2518 0.1838 0.0100 0.0155 0.0118 74 VAL A CG2 575 N N . ASP A 75 ? 0.2309 0.2907 0.1869 -0.0055 0.0070 0.0005 75 ASP A N 576 C CA . ASP A 75 ? 0.2404 0.2894 0.1983 -0.0027 0.0066 0.0018 75 ASP A CA 577 C C . ASP A 75 ? 0.2417 0.2981 0.2075 -0.0004 0.0030 0.0059 75 ASP A C 578 O O . ASP A 75 ? 0.2409 0.2845 0.2124 0.0061 0.0055 0.0041 75 ASP A O 579 C CB . ASP A 75 ? 0.2392 0.2972 0.2048 -0.0021 0.0068 0.0042 75 ASP A CB 580 C CG . ASP A 75 ? 0.2580 0.2953 0.2433 -0.0039 -0.0007 -0.0009 75 ASP A CG 581 O OD1 . ASP A 75 ? 0.2497 0.3003 0.2519 -0.0249 0.0002 0.0112 75 ASP A OD1 582 O OD2 . ASP A 75 ? 0.2661 0.3559 0.2952 -0.0050 -0.0011 -0.0007 75 ASP A OD2 583 N N . GLY A 76 ? 0.2426 0.2982 0.2038 0.0001 0.0035 0.0142 76 GLY A N 584 C CA . GLY A 76 ? 0.2483 0.3125 0.2191 -0.0009 -0.0013 0.0140 76 GLY A CA 585 C C . GLY A 76 ? 0.2530 0.3106 0.2182 0.0034 0.0029 0.0098 76 GLY A C 586 O O . GLY A 76 ? 0.2567 0.3278 0.2129 0.0057 0.0015 0.0165 76 GLY A O 587 N N . PHE A 77 ? 0.2435 0.2952 0.2075 0.0003 0.0022 0.0151 77 PHE A N 588 C CA . PHE A 77 ? 0.2466 0.2871 0.2070 -0.0004 0.0039 0.0068 77 PHE A CA 589 C C . PHE A 77 ? 0.2370 0.2843 0.1977 -0.0030 0.0086 0.0052 77 PHE A C 590 O O . PHE A 77 ? 0.2234 0.2965 0.2138 -0.0044 0.0049 -0.0048 77 PHE A O 591 C CB . PHE A 77 ? 0.2460 0.2797 0.2029 0.0005 0.0077 0.0067 77 PHE A CB 592 C CG . PHE A 77 ? 0.2516 0.2941 0.2187 -0.0082 -0.0078 -0.0061 77 PHE A CG 593 C CD1 . PHE A 77 ? 0.2715 0.2655 0.2523 -0.0010 -0.0183 0.0047 77 PHE A CD1 594 C CD2 . PHE A 77 ? 0.2359 0.2986 0.2337 0.0100 -0.0078 -0.0083 77 PHE A CD2 595 C CE1 . PHE A 77 ? 0.2834 0.2940 0.2554 0.0011 -0.0014 -0.0017 77 PHE A CE1 596 C CE2 . PHE A 77 ? 0.2514 0.2829 0.2552 0.0000 -0.0101 0.0034 77 PHE A CE2 597 C CZ . PHE A 77 ? 0.2648 0.2868 0.2526 -0.0010 -0.0063 -0.0001 77 PHE A CZ 598 N N . GLN A 78 ? 0.2238 0.2944 0.1980 -0.0027 0.0084 0.0008 78 GLN A N 599 C CA . GLN A 78 ? 0.2152 0.2885 0.2008 -0.0038 0.0100 0.0053 78 GLN A CA 600 C C . GLN A 78 ? 0.2213 0.2955 0.2051 -0.0027 0.0061 0.0007 78 GLN A C 601 O O . GLN A 78 ? 0.2233 0.3001 0.1979 0.0019 0.0066 0.0022 78 GLN A O 602 C CB . GLN A 78 ? 0.2164 0.2789 0.2132 -0.0070 0.0027 0.0001 78 GLN A CB 603 C CG . GLN A 78 ? 0.2244 0.2781 0.2222 0.0014 0.0115 0.0041 78 GLN A CG 604 C CD . GLN A 78 ? 0.2214 0.2893 0.2161 -0.0028 0.0164 0.0126 78 GLN A CD 605 O OE1 . GLN A 78 ? 0.2087 0.2684 0.2091 0.0103 0.0049 0.0161 78 GLN A OE1 606 N NE2 . GLN A 78 ? 0.2477 0.2979 0.2299 -0.0280 0.0084 0.0115 78 GLN A NE2 607 N N . LYS A 79 ? 0.2332 0.3064 0.2069 -0.0041 0.0147 0.0112 79 LYS A N 608 C CA . LYS A 79 ? 0.2883 0.3407 0.2572 -0.0073 0.0112 0.0051 79 LYS A CA 609 C C . LYS A 79 ? 0.2660 0.3199 0.2391 -0.0059 0.0132 0.0070 79 LYS A C 610 O O . LYS A 79 ? 0.2729 0.3326 0.2338 -0.0070 0.0097 0.0018 79 LYS A O 611 C CB . LYS A 79 ? 0.2703 0.3412 0.2564 0.0019 0.0098 0.0147 79 LYS A CB 612 C CG . LYS A 79 ? 0.3263 0.4043 0.3388 -0.0083 0.0054 0.0038 79 LYS A CG 613 C CD . LYS A 79 ? 0.3496 0.3804 0.3392 0.0232 -0.0070 0.0337 79 LYS A CD 614 C CE . LYS A 79 ? 0.4412 0.3589 0.3414 -0.0533 -0.0488 -0.1333 79 LYS A CE 615 N NZ . LYS A 79 ? 0.5408 0.6506 0.6424 0.0547 0.0255 0.1104 79 LYS A NZ 616 N N . ALA A 80 ? 0.2586 0.3161 0.2309 -0.0082 0.0122 0.0098 80 ALA A N 617 C CA . ALA A 80 ? 0.2654 0.3155 0.2370 -0.0109 0.0098 0.0059 80 ALA A CA 618 C C . ALA A 80 ? 0.2630 0.3157 0.2320 -0.0097 0.0150 0.0066 80 ALA A C 619 O O . ALA A 80 ? 0.2737 0.3259 0.2405 -0.0105 0.0221 0.0096 80 ALA A O 620 C CB . ALA A 80 ? 0.2574 0.3072 0.2401 -0.0112 0.0118 0.0036 80 ALA A CB 621 N N . CYS A 81 ? 0.2610 0.3142 0.2258 -0.0152 0.0165 0.0086 81 CYS A N 622 C CA . CYS A 81 ? 0.2632 0.3192 0.2206 -0.0133 0.0203 0.0049 81 CYS A CA 623 C C . CYS A 81 ? 0.2643 0.3174 0.2307 -0.0084 0.0195 0.0015 81 CYS A C 624 O O . CYS A 81 ? 0.2732 0.3435 0.2323 -0.0020 0.0237 -0.0005 81 CYS A O 625 C CB . CYS A 81 ? 0.2628 0.3146 0.2197 -0.0145 0.0174 0.0087 81 CYS A CB 626 S SG . CYS A 81 ? 0.2562 0.3427 0.1978 -0.0302 0.0260 0.0144 81 CYS A SG 627 N N . MET A 82 ? 0.2541 0.3243 0.2244 -0.0080 0.0207 -0.0015 82 MET A N 628 C CA . MET A 82 ? 0.2593 0.3259 0.2379 -0.0051 0.0209 -0.0068 82 MET A CA 629 C C . MET A 82 ? 0.2597 0.3297 0.2442 -0.0023 0.0192 -0.0040 82 MET A C 630 O O . MET A 82 ? 0.2822 0.3561 0.2533 -0.0021 0.0270 -0.0080 82 MET A O 631 C CB . MET A 82 ? 0.2640 0.3365 0.2457 -0.0062 0.0143 -0.0089 82 MET A CB 632 C CG . MET A 82 ? 0.3075 0.3589 0.2633 -0.0050 0.0310 -0.0185 82 MET A CG 633 S SD . MET A 82 ? 0.4242 0.4241 0.3573 -0.0050 0.0524 -0.0165 82 MET A SD 634 C CE . MET A 82 ? 0.3827 0.4118 0.3520 -0.0193 0.0164 0.0080 82 MET A CE 635 N N . SER A 83 ? 0.2598 0.3323 0.2478 0.0028 0.0185 0.0038 83 SER A N 636 C CA . SER A 83 ? 0.2631 0.3376 0.2570 0.0004 0.0158 0.0066 83 SER A CA 637 C C . SER A 83 ? 0.2703 0.3295 0.2606 0.0034 0.0130 0.0084 83 SER A C 638 O O . SER A 83 ? 0.2742 0.3386 0.2555 0.0032 0.0206 0.0126 83 SER A O 639 C CB . SER A 83 ? 0.2788 0.3427 0.2648 0.0021 0.0145 0.0046 83 SER A CB 640 O OG . SER A 83 ? 0.2857 0.3651 0.2932 -0.0056 0.0189 0.0054 83 SER A OG 641 N N . THR A 84 ? 0.2564 0.3203 0.2481 0.0046 0.0029 0.0063 84 THR A N 642 C CA . THR A 84 ? 0.2519 0.3040 0.2479 0.0033 0.0000 0.0033 84 THR A CA 643 C C . THR A 84 ? 0.2474 0.3105 0.2503 0.0067 0.0017 -0.0030 84 THR A C 644 O O . THR A 84 ? 0.2321 0.3100 0.2552 0.0035 0.0028 -0.0084 84 THR A O 645 C CB . THR A 84 ? 0.2508 0.2935 0.2394 0.0000 -0.0055 0.0031 84 THR A CB 646 O OG1 . THR A 84 ? 0.2464 0.2952 0.2181 -0.0007 -0.0102 0.0012 84 THR A OG1 647 C CG2 . THR A 84 ? 0.2544 0.2948 0.2540 0.0129 -0.0004 0.0021 84 THR A CG2 648 N N . ARG A 85 ? 0.2419 0.3078 0.2612 0.0015 0.0075 -0.0085 85 ARG A N 649 C CA . ARG A 85 ? 0.2402 0.3116 0.2631 0.0028 0.0117 -0.0062 85 ARG A CA 650 C C . ARG A 85 ? 0.2423 0.3131 0.2625 0.0005 0.0098 -0.0126 85 ARG A C 651 O O . ARG A 85 ? 0.2537 0.3329 0.2587 -0.0064 0.0175 -0.0195 85 ARG A O 652 C CB . ARG A 85 ? 0.2457 0.3128 0.2798 0.0117 0.0080 -0.0078 85 ARG A CB 653 C CG . ARG A 85 ? 0.2368 0.3197 0.2460 0.0077 0.0021 -0.0169 85 ARG A CG 654 C CD . ARG A 85 ? 0.2684 0.3379 0.2834 0.0093 -0.0014 0.0028 85 ARG A CD 655 N NE . ARG A 85 ? 0.2417 0.3254 0.2562 -0.0037 -0.0027 -0.0108 85 ARG A NE 656 C CZ . ARG A 85 ? 0.2855 0.3211 0.2683 -0.0026 0.0050 -0.0082 85 ARG A CZ 657 N NH1 . ARG A 85 ? 0.3170 0.3273 0.2921 0.0018 -0.0011 -0.0118 85 ARG A NH1 658 N NH2 . ARG A 85 ? 0.3012 0.3528 0.2785 0.0043 0.0133 -0.0167 85 ARG A NH2 659 N N . LEU A 86 ? 0.2278 0.3037 0.2447 -0.0005 0.0112 -0.0091 86 LEU A N 660 C CA . LEU A 86 ? 0.2333 0.3028 0.2401 0.0055 0.0114 -0.0088 86 LEU A CA 661 C C . LEU A 86 ? 0.2296 0.3040 0.2357 0.0016 0.0116 -0.0085 86 LEU A C 662 O O . LEU A 86 ? 0.2351 0.3098 0.2391 0.0030 0.0219 -0.0212 86 LEU A O 663 C CB . LEU A 86 ? 0.2231 0.3030 0.2422 0.0113 0.0105 -0.0052 86 LEU A CB 664 C CG . LEU A 86 ? 0.2299 0.2955 0.2394 0.0164 0.0092 -0.0060 86 LEU A CG 665 C CD1 . LEU A 86 ? 0.2406 0.3084 0.2375 0.0221 0.0069 0.0056 86 LEU A CD1 666 C CD2 . LEU A 86 ? 0.2673 0.3104 0.2641 0.0063 0.0145 -0.0094 86 LEU A CD2 667 N N . GLY A 87 ? 0.2208 0.3120 0.2250 0.0037 0.0107 -0.0089 87 GLY A N 668 C CA . GLY A 87 ? 0.2374 0.3291 0.2298 0.0025 0.0125 -0.0014 87 GLY A CA 669 C C . GLY A 87 ? 0.2320 0.3303 0.2273 -0.0023 0.0117 -0.0053 87 GLY A C 670 O O . GLY A 87 ? 0.2435 0.3598 0.2365 -0.0154 0.0053 -0.0042 87 GLY A O 671 N N . ILE A 88 ? 0.2208 0.3175 0.2273 0.0038 0.0140 -0.0070 88 ILE A N 672 C CA . ILE A 88 ? 0.2128 0.2847 0.2152 0.0029 0.0071 -0.0056 88 ILE A CA 673 C C . ILE A 88 ? 0.2107 0.2765 0.2209 -0.0030 0.0108 -0.0100 88 ILE A C 674 O O . ILE A 88 ? 0.2076 0.2798 0.2224 -0.0076 0.0100 -0.0057 88 ILE A O 675 C CB . ILE A 88 ? 0.2175 0.2765 0.2138 0.0083 0.0092 -0.0026 88 ILE A CB 676 C CG1 . ILE A 88 ? 0.2138 0.2865 0.2297 0.0160 0.0049 -0.0125 88 ILE A CG1 677 C CG2 . ILE A 88 ? 0.2443 0.2663 0.2042 -0.0018 0.0171 -0.0044 88 ILE A CG2 678 C CD1 . ILE A 88 ? 0.2157 0.2998 0.2239 0.0119 -0.0013 -0.0115 88 ILE A CD1 679 N N . PRO A 89 ? 0.2126 0.2725 0.2228 -0.0074 0.0112 -0.0113 89 PRO A N 680 C CA . PRO A 89 ? 0.2013 0.2680 0.2119 -0.0085 0.0088 -0.0122 89 PRO A CA 681 C C . PRO A 89 ? 0.2053 0.2625 0.2061 -0.0095 0.0108 -0.0093 89 PRO A C 682 O O . PRO A 89 ? 0.2026 0.2642 0.1893 -0.0090 -0.0003 -0.0095 89 PRO A O 683 C CB . PRO A 89 ? 0.2063 0.2708 0.2191 -0.0117 0.0118 -0.0082 89 PRO A CB 684 C CG . PRO A 89 ? 0.2109 0.2734 0.2430 -0.0083 0.0119 -0.0158 89 PRO A CG 685 C CD . PRO A 89 ? 0.2076 0.2729 0.2286 -0.0075 0.0174 -0.0137 89 PRO A CD 686 N N . MET A 90 ? 0.2015 0.2555 0.1952 -0.0123 0.0140 -0.0109 90 MET A N 687 C CA . MET A 90 ? 0.1934 0.2476 0.1867 -0.0147 0.0241 -0.0051 90 MET A CA 688 C C . MET A 90 ? 0.2038 0.2553 0.1946 -0.0099 0.0174 -0.0022 90 MET A C 689 O O . MET A 90 ? 0.1991 0.2545 0.1823 -0.0216 0.0180 -0.0022 90 MET A O 690 C CB . MET A 90 ? 0.2128 0.2497 0.1975 -0.0004 0.0197 -0.0053 90 MET A CB 691 C CG . MET A 90 ? 0.1970 0.2515 0.2092 -0.0049 0.0256 0.0094 90 MET A CG 692 S SD . MET A 90 ? 0.2080 0.2885 0.2070 -0.0091 0.0212 -0.0166 90 MET A SD 693 C CE . MET A 90 ? 0.2482 0.3215 0.2376 0.0211 0.0021 -0.0108 90 MET A CE 694 N N . ILE A 91 ? 0.1957 0.2528 0.1803 -0.0119 0.0199 0.0035 91 ILE A N 695 C CA . ILE A 91 ? 0.1903 0.2386 0.1889 -0.0124 0.0194 0.0051 91 ILE A CA 696 C C . ILE A 91 ? 0.1940 0.2407 0.1915 -0.0076 0.0159 0.0044 91 ILE A C 697 O O . ILE A 91 ? 0.1858 0.2455 0.1789 -0.0088 0.0200 -0.0007 91 ILE A O 698 C CB . ILE A 91 ? 0.1916 0.2444 0.2051 -0.0116 0.0207 0.0113 91 ILE A CB 699 C CG1 . ILE A 91 ? 0.1846 0.2212 0.1854 -0.0083 0.0231 0.0015 91 ILE A CG1 700 C CG2 . ILE A 91 ? 0.2048 0.2493 0.1869 -0.0066 0.0126 0.0127 91 ILE A CG2 701 C CD1 . ILE A 91 ? 0.1990 0.2342 0.2056 -0.0038 0.0258 0.0140 91 ILE A CD1 702 N N . TYR A 92 ? 0.2035 0.2314 0.1848 -0.0080 0.0094 0.0011 92 TYR A N 703 C CA . TYR A 92 ? 0.1993 0.2293 0.1710 -0.0030 0.0123 0.0068 92 TYR A CA 704 C C . TYR A 92 ? 0.1924 0.2339 0.1666 -0.0050 0.0103 0.0087 92 TYR A C 705 O O . TYR A 92 ? 0.1925 0.2496 0.1488 -0.0096 0.0174 0.0138 92 TYR A O 706 C CB . TYR A 92 ? 0.2022 0.2285 0.1773 -0.0043 0.0077 0.0098 92 TYR A CB 707 C CG . TYR A 92 ? 0.1959 0.2274 0.1794 -0.0094 0.0093 0.0112 92 TYR A CG 708 C CD1 . TYR A 92 ? 0.1734 0.2139 0.1864 -0.0017 0.0102 0.0045 92 TYR A CD1 709 C CD2 . TYR A 92 ? 0.1843 0.2003 0.1961 -0.0160 0.0075 0.0266 92 TYR A CD2 710 C CE1 . TYR A 92 ? 0.1956 0.1984 0.1948 0.0073 0.0154 0.0168 92 TYR A CE1 711 C CE2 . TYR A 92 ? 0.2294 0.2131 0.1871 -0.0005 -0.0004 -0.0005 92 TYR A CE2 712 C CZ . TYR A 92 ? 0.2054 0.2145 0.2038 0.0066 0.0074 0.0137 92 TYR A CZ 713 O OH . TYR A 92 ? 0.2430 0.2303 0.2004 -0.0117 0.0062 0.0144 92 TYR A OH 714 N N . GLY A 93 ? 0.1964 0.2339 0.1475 -0.0037 0.0182 0.0067 93 GLY A N 715 C CA . GLY A 93 ? 0.1953 0.2317 0.1639 -0.0071 0.0153 0.0059 93 GLY A CA 716 C C . GLY A 93 ? 0.1963 0.2211 0.1637 -0.0048 0.0198 0.0115 93 GLY A C 717 O O . GLY A 93 ? 0.1919 0.2202 0.1761 -0.0073 0.0150 0.0113 93 GLY A O 718 N N . ILE A 94 ? 0.1890 0.2199 0.1769 0.0031 0.0119 0.0115 94 ILE A N 719 C CA . ILE A 94 ? 0.1916 0.2131 0.1771 0.0023 0.0107 0.0130 94 ILE A CA 720 C C . ILE A 94 ? 0.1990 0.2121 0.1651 0.0049 0.0089 0.0110 94 ILE A C 721 O O . ILE A 94 ? 0.2031 0.2111 0.1679 0.0065 0.0198 0.0079 94 ILE A O 722 C CB . ILE A 94 ? 0.1852 0.2082 0.1820 0.0056 0.0048 0.0162 94 ILE A CB 723 C CG1 . ILE A 94 ? 0.1975 0.2163 0.1724 0.0048 0.0108 0.0145 94 ILE A CG1 724 C CG2 . ILE A 94 ? 0.2098 0.2169 0.2055 -0.0097 0.0096 0.0128 94 ILE A CG2 725 C CD1 . ILE A 94 ? 0.1899 0.2183 0.1963 0.0101 0.0002 0.0220 94 ILE A CD1 726 N N . ASP A 95 ? 0.1992 0.2206 0.1757 0.0001 0.0129 0.0083 95 ASP A N 727 C CA . ASP A 95 ? 0.1912 0.2201 0.1657 -0.0014 0.0022 0.0090 95 ASP A CA 728 C C . ASP A 95 ? 0.1962 0.2224 0.1781 0.0049 0.0066 0.0086 95 ASP A C 729 O O . ASP A 95 ? 0.1984 0.2391 0.1959 0.0141 -0.0042 0.0099 95 ASP A O 730 C CB . ASP A 95 ? 0.2049 0.2304 0.1789 0.0023 0.0057 0.0141 95 ASP A CB 731 C CG . ASP A 95 ? 0.2227 0.2553 0.2012 -0.0033 -0.0035 0.0087 95 ASP A CG 732 O OD1 . ASP A 95 ? 0.2753 0.3016 0.2191 0.0196 -0.0022 0.0256 95 ASP A OD1 733 O OD2 . ASP A 95 ? 0.2203 0.2606 0.2150 -0.0076 0.0092 -0.0051 95 ASP A OD2 734 N N . ALA A 96 ? 0.1973 0.2316 0.1858 0.0049 0.0012 0.0031 96 ALA A N 735 C CA . ALA A 96 ? 0.2011 0.2229 0.1789 0.0026 0.0038 0.0030 96 ALA A CA 736 C C . ALA A 96 ? 0.2114 0.2248 0.1915 0.0021 0.0083 0.0029 96 ALA A C 737 O O . ALA A 96 ? 0.2402 0.2229 0.1978 0.0084 0.0133 0.0168 96 ALA A O 738 C CB . ALA A 96 ? 0.2045 0.2155 0.1705 -0.0003 -0.0002 0.0033 96 ALA A CB 739 N N . VAL A 97 ? 0.1960 0.2327 0.1813 0.0133 0.0117 0.0035 97 VAL A N 740 C CA . VAL A 97 ? 0.1900 0.2238 0.1893 0.0141 0.0097 0.0118 97 VAL A CA 741 C C . VAL A 97 ? 0.2021 0.2298 0.1910 0.0171 0.0156 0.0144 97 VAL A C 742 O O . VAL A 97 ? 0.2209 0.2377 0.1930 0.0167 0.0180 0.0229 97 VAL A O 743 C CB . VAL A 97 ? 0.1902 0.2196 0.1958 0.0107 0.0078 0.0062 97 VAL A CB 744 C CG1 . VAL A 97 ? 0.1975 0.2533 0.2122 0.0169 0.0164 0.0106 97 VAL A CG1 745 C CG2 . VAL A 97 ? 0.2182 0.2264 0.2061 0.0083 -0.0051 -0.0014 97 VAL A CG2 746 N N . HIS A 98 ? 0.1889 0.2136 0.1826 0.0134 0.0101 0.0056 98 HIS A N 747 C CA . HIS A 98 ? 0.1920 0.2134 0.1752 0.0106 0.0055 0.0061 98 HIS A CA 748 C C . HIS A 98 ? 0.2009 0.2082 0.1650 0.0051 0.0092 0.0137 98 HIS A C 749 O O . HIS A 98 ? 0.2050 0.2286 0.1769 0.0109 0.0085 0.0188 98 HIS A O 750 C CB . HIS A 98 ? 0.1992 0.1931 0.1735 0.0027 0.0072 0.0035 98 HIS A CB 751 C CG . HIS A 98 ? 0.2056 0.2036 0.1553 -0.0021 -0.0002 0.0159 98 HIS A CG 752 N ND1 . HIS A 98 ? 0.1978 0.1808 0.1858 -0.0132 0.0147 0.0206 98 HIS A ND1 753 C CD2 . HIS A 98 ? 0.2043 0.1821 0.1658 -0.0230 -0.0007 0.0056 98 HIS A CD2 754 C CE1 . HIS A 98 ? 0.1976 0.1878 0.1520 -0.0146 0.0071 0.0169 98 HIS A CE1 755 N NE2 . HIS A 98 ? 0.2215 0.2105 0.1756 0.0068 0.0184 0.0175 98 HIS A NE2 756 N N . GLY A 99 ? 0.1952 0.2094 0.1687 0.0034 0.0070 0.0154 99 GLY A N 757 C CA . GLY A 99 ? 0.2026 0.2279 0.1570 0.0000 0.0120 0.0139 99 GLY A CA 758 C C . GLY A 99 ? 0.1939 0.2162 0.1782 -0.0024 0.0054 0.0156 99 GLY A C 759 O O . GLY A 99 ? 0.2075 0.2286 0.1798 -0.0010 -0.0005 0.0188 99 GLY A O 760 N N . GLN A 100 ? 0.2006 0.2151 0.1655 -0.0031 0.0087 0.0107 100 GLN A N 761 C CA . GLN A 100 ? 0.2020 0.2166 0.1680 -0.0052 0.0076 0.0128 100 GLN A CA 762 C C . GLN A 100 ? 0.2025 0.2100 0.1675 -0.0025 0.0021 0.0138 100 GLN A C 763 O O . GLN A 100 ? 0.2214 0.2103 0.1788 -0.0025 0.0051 0.0167 100 GLN A O 764 C CB . GLN A 100 ? 0.1910 0.2150 0.1773 -0.0005 -0.0048 0.0170 100 GLN A CB 765 C CG . GLN A 100 ? 0.1955 0.2295 0.1777 -0.0016 0.0104 0.0180 100 GLN A CG 766 C CD . GLN A 100 ? 0.2285 0.2644 0.2133 0.0045 0.0074 0.0120 100 GLN A CD 767 O OE1 . GLN A 100 ? 0.2681 0.2927 0.2027 -0.0011 0.0231 0.0180 100 GLN A OE1 768 N NE2 . GLN A 100 ? 0.2014 0.2213 0.1370 -0.0120 0.0350 0.0229 100 GLN A NE2 769 N N . ASN A 101 ? 0.2012 0.2064 0.1806 -0.0049 0.0018 0.0095 101 ASN A N 770 C CA . ASN A 101 ? 0.2147 0.2088 0.1721 -0.0020 -0.0029 0.0111 101 ASN A CA 771 C C . ASN A 101 ? 0.2125 0.2158 0.1834 -0.0006 -0.0015 0.0128 101 ASN A C 772 O O . ASN A 101 ? 0.2289 0.2158 0.1982 0.0021 0.0140 0.0175 101 ASN A O 773 C CB . ASN A 101 ? 0.2132 0.2103 0.1777 -0.0048 -0.0061 0.0102 101 ASN A CB 774 C CG . ASN A 101 ? 0.2110 0.2139 0.1721 -0.0040 -0.0022 0.0025 101 ASN A CG 775 O OD1 . ASN A 101 ? 0.2258 0.2637 0.2296 -0.0052 0.0164 0.0113 101 ASN A OD1 776 N ND2 . ASN A 101 ? 0.1626 0.1961 0.1250 -0.0001 0.0198 0.0076 101 ASN A ND2 777 N N . ASN A 102 ? 0.2087 0.2215 0.1865 0.0042 -0.0024 0.0186 102 ASN A N 778 C CA . ASN A 102 ? 0.2162 0.2242 0.1889 0.0069 -0.0073 0.0159 102 ASN A CA 779 C C . ASN A 102 ? 0.2304 0.2290 0.1898 0.0066 -0.0090 0.0166 102 ASN A C 780 O O . ASN A 102 ? 0.2490 0.2236 0.1946 0.0029 -0.0137 0.0211 102 ASN A O 781 C CB . ASN A 102 ? 0.2035 0.2281 0.1959 0.0073 -0.0033 0.0220 102 ASN A CB 782 C CG . ASN A 102 ? 0.2279 0.2393 0.1995 0.0022 0.0007 0.0107 102 ASN A CG 783 O OD1 . ASN A 102 ? 0.2824 0.2825 0.2734 0.0226 -0.0013 0.0205 102 ASN A OD1 784 N ND2 . ASN A 102 ? 0.1744 0.2099 0.1714 -0.0027 0.0030 0.0095 102 ASN A ND2 785 N N . VAL A 103 ? 0.2242 0.2204 0.1870 0.0103 -0.0048 0.0130 103 VAL A N 786 C CA . VAL A 103 ? 0.2228 0.2305 0.1886 0.0090 -0.0034 0.0159 103 VAL A CA 787 C C . VAL A 103 ? 0.2344 0.2274 0.2029 0.0089 -0.0030 0.0203 103 VAL A C 788 O O . VAL A 103 ? 0.2464 0.2449 0.2072 0.0093 0.0028 0.0276 103 VAL A O 789 C CB . VAL A 103 ? 0.2217 0.2300 0.1957 0.0179 -0.0089 0.0077 103 VAL A CB 790 C CG1 . VAL A 103 ? 0.2491 0.2552 0.1859 0.0200 -0.0142 0.0137 103 VAL A CG1 791 C CG2 . VAL A 103 ? 0.2286 0.2350 0.2000 0.0275 0.0009 0.0165 103 VAL A CG2 792 N N . TYR A 104 ? 0.2428 0.2324 0.2128 0.0074 0.0046 0.0204 104 TYR A N 793 C CA . TYR A 104 ? 0.2554 0.2406 0.2302 0.0086 0.0017 0.0245 104 TYR A CA 794 C C . TYR A 104 ? 0.2451 0.2377 0.2206 0.0064 0.0045 0.0223 104 TYR A C 795 O O . TYR A 104 ? 0.2427 0.2547 0.2240 0.0023 0.0091 0.0123 104 TYR A O 796 C CB . TYR A 104 ? 0.2744 0.2542 0.2397 0.0024 0.0129 0.0279 104 TYR A CB 797 C CG . TYR A 104 ? 0.3065 0.2681 0.2801 0.0067 0.0124 0.0275 104 TYR A CG 798 C CD1 . TYR A 104 ? 0.3221 0.2911 0.2781 0.0071 0.0141 0.0275 104 TYR A CD1 799 C CD2 . TYR A 104 ? 0.2987 0.3025 0.3122 0.0117 0.0141 0.0229 104 TYR A CD2 800 C CE1 . TYR A 104 ? 0.3315 0.3131 0.3085 0.0083 0.0239 0.0231 104 TYR A CE1 801 C CE2 . TYR A 104 ? 0.3236 0.3054 0.3417 0.0193 0.0139 0.0110 104 TYR A CE2 802 C CZ . TYR A 104 ? 0.3125 0.3086 0.3215 0.0170 0.0248 0.0271 104 TYR A CZ 803 O OH . TYR A 104 ? 0.3535 0.3343 0.3780 0.0359 0.0453 0.0254 104 TYR A OH 804 N N . GLY A 105 ? 0.2386 0.2425 0.2124 0.0110 -0.0034 0.0236 105 GLY A N 805 C CA . GLY A 105 ? 0.2395 0.2517 0.2040 0.0026 0.0051 0.0189 105 GLY A CA 806 C C . GLY A 105 ? 0.2270 0.2532 0.1989 0.0094 0.0030 0.0141 105 GLY A C 807 O O . GLY A 105 ? 0.2458 0.2671 0.2129 0.0081 0.0099 0.0167 105 GLY A O 808 N N . ALA A 106 ? 0.2211 0.2486 0.1745 0.0144 0.0123 0.0176 106 ALA A N 809 C CA . ALA A 106 ? 0.2124 0.2484 0.1799 0.0094 0.0142 0.0152 106 ALA A CA 810 C C . ALA A 106 ? 0.2042 0.2382 0.1669 0.0029 0.0097 0.0170 106 ALA A C 811 O O . ALA A 106 ? 0.2164 0.2288 0.1793 0.0039 0.0128 0.0165 106 ALA A O 812 C CB . ALA A 106 ? 0.1988 0.2490 0.1804 0.0182 0.0105 0.0226 106 ALA A CB 813 N N . THR A 107 ? 0.1962 0.2416 0.1595 0.0000 0.0012 0.0171 107 THR A N 814 C CA . THR A 107 ? 0.2042 0.2437 0.1682 -0.0019 -0.0005 0.0130 107 THR A CA 815 C C . THR A 107 ? 0.2038 0.2363 0.1678 0.0042 -0.0018 0.0102 107 THR A C 816 O O . THR A 107 ? 0.2107 0.2522 0.1691 0.0232 -0.0133 0.0020 107 THR A O 817 C CB . THR A 107 ? 0.1956 0.2467 0.1706 -0.0089 -0.0048 0.0145 107 THR A CB 818 O OG1 . THR A 107 ? 0.1988 0.2763 0.1698 -0.0047 -0.0112 0.0164 107 THR A OG1 819 C CG2 . THR A 107 ? 0.2123 0.2615 0.1914 -0.0139 0.0149 0.0105 107 THR A CG2 820 N N . ILE A 108 ? 0.2002 0.2226 0.1625 0.0067 -0.0039 0.0126 108 ILE A N 821 C CA . ILE A 108 ? 0.2024 0.2081 0.1558 -0.0056 0.0042 0.0092 108 ILE A CA 822 C C . ILE A 108 ? 0.2124 0.2122 0.1696 0.0017 0.0017 0.0135 108 ILE A C 823 O O . ILE A 108 ? 0.2134 0.2064 0.1618 0.0084 0.0232 0.0094 108 ILE A O 824 C CB . ILE A 108 ? 0.2105 0.2235 0.1655 -0.0106 -0.0040 0.0190 108 ILE A CB 825 C CG1 . ILE A 108 ? 0.2146 0.2148 0.1597 -0.0024 0.0146 0.0101 108 ILE A CG1 826 C CG2 . ILE A 108 ? 0.2047 0.2201 0.1534 -0.0172 -0.0265 0.0001 108 ILE A CG2 827 C CD1 . ILE A 108 ? 0.2466 0.2252 0.1682 0.0089 0.0367 0.0098 108 ILE A CD1 828 N N . PHE A 109 ? 0.2050 0.1993 0.1649 0.0004 0.0033 0.0087 109 PHE A N 829 C CA . PHE A 109 ? 0.2034 0.1928 0.1593 -0.0069 0.0078 0.0065 109 PHE A CA 830 C C . PHE A 109 ? 0.2014 0.1969 0.1627 -0.0022 0.0086 0.0118 109 PHE A C 831 O O . PHE A 109 ? 0.2147 0.1997 0.1575 -0.0015 0.0092 0.0112 109 PHE A O 832 C CB . PHE A 109 ? 0.1904 0.2038 0.1675 -0.0004 0.0047 -0.0024 109 PHE A CB 833 C CG . PHE A 109 ? 0.2035 0.1970 0.1574 -0.0140 -0.0008 -0.0031 109 PHE A CG 834 C CD1 . PHE A 109 ? 0.2021 0.2316 0.1888 0.0037 0.0010 -0.0025 109 PHE A CD1 835 C CD2 . PHE A 109 ? 0.2252 0.2230 0.1839 -0.0019 -0.0006 -0.0057 109 PHE A CD2 836 C CE1 . PHE A 109 ? 0.2012 0.2522 0.1981 -0.0023 -0.0075 -0.0148 109 PHE A CE1 837 C CE2 . PHE A 109 ? 0.2076 0.2518 0.1941 -0.0120 -0.0185 -0.0021 109 PHE A CE2 838 C CZ . PHE A 109 ? 0.2150 0.2541 0.2050 -0.0015 -0.0071 0.0066 109 PHE A CZ 839 N N . PRO A 110 ? 0.2071 0.2120 0.1684 -0.0055 0.0141 0.0044 110 PRO A N 840 C CA . PRO A 110 ? 0.2019 0.2124 0.1594 -0.0008 0.0180 0.0119 110 PRO A CA 841 C C . PRO A 110 ? 0.2051 0.2079 0.1567 0.0005 0.0105 0.0142 110 PRO A C 842 O O . PRO A 110 ? 0.2057 0.2076 0.1573 0.0134 0.0208 0.0057 110 PRO A O 843 C CB . PRO A 110 ? 0.2002 0.2308 0.1630 -0.0021 0.0202 0.0136 110 PRO A CB 844 C CG . PRO A 110 ? 0.2018 0.2217 0.1524 -0.0028 0.0145 0.0077 110 PRO A CG 845 C CD . PRO A 110 ? 0.1983 0.2271 0.1668 -0.0059 0.0251 0.0127 110 PRO A CD 846 N N . HIS A 111 ? 0.1986 0.2071 0.1601 0.0034 0.0136 0.0131 111 HIS A N 847 C CA . HIS A 111 ? 0.1909 0.2037 0.1616 0.0068 0.0045 0.0170 111 HIS A CA 848 C C . HIS A 111 ? 0.1957 0.2166 0.1701 0.0106 0.0099 0.0154 111 HIS A C 849 O O . HIS A 111 ? 0.1947 0.2177 0.1705 0.0204 0.0141 0.0228 111 HIS A O 850 C CB . HIS A 111 ? 0.1968 0.1966 0.1580 -0.0019 -0.0012 0.0132 111 HIS A CB 851 C CG . HIS A 111 ? 0.1870 0.2122 0.1777 -0.0087 0.0092 0.0059 111 HIS A CG 852 N ND1 . HIS A 111 ? 0.1970 0.2288 0.1813 0.0009 0.0047 0.0090 111 HIS A ND1 853 C CD2 . HIS A 111 ? 0.1809 0.2112 0.1881 0.0085 -0.0016 0.0075 111 HIS A CD2 854 C CE1 . HIS A 111 ? 0.1748 0.2157 0.1604 0.0139 -0.0054 0.0078 111 HIS A CE1 855 N NE2 . HIS A 111 ? 0.1909 0.1881 0.1828 0.0000 0.0059 0.0005 111 HIS A NE2 856 N N . ASN A 112 ? 0.2016 0.2069 0.1663 0.0232 0.0072 0.0138 112 ASN A N 857 C CA . ASN A 112 ? 0.1960 0.2215 0.1709 0.0187 0.0103 0.0121 112 ASN A CA 858 C C . ASN A 112 ? 0.2008 0.2245 0.1811 0.0165 0.0082 0.0163 112 ASN A C 859 O O . ASN A 112 ? 0.2029 0.2414 0.1746 0.0064 0.0255 0.0193 112 ASN A O 860 C CB . ASN A 112 ? 0.1981 0.2307 0.1818 0.0255 0.0159 0.0105 112 ASN A CB 861 C CG . ASN A 112 ? 0.2086 0.2302 0.1883 0.0081 0.0054 0.0062 112 ASN A CG 862 O OD1 . ASN A 112 ? 0.2546 0.3276 0.2144 0.0185 0.0207 -0.0052 112 ASN A OD1 863 N ND2 . ASN A 112 ? 0.1673 0.2191 0.1378 0.0129 0.0311 0.0211 112 ASN A ND2 864 N N . VAL A 113 ? 0.2039 0.2327 0.1668 0.0187 0.0087 0.0148 113 VAL A N 865 C CA . VAL A 113 ? 0.2145 0.2356 0.1789 0.0111 0.0078 0.0161 113 VAL A CA 866 C C . VAL A 113 ? 0.2097 0.2240 0.1837 0.0126 0.0086 0.0166 113 VAL A C 867 O O . VAL A 113 ? 0.2214 0.2407 0.1854 0.0102 0.0064 0.0224 113 VAL A O 868 C CB . VAL A 113 ? 0.2167 0.2335 0.1730 0.0103 0.0019 0.0203 113 VAL A CB 869 C CG1 . VAL A 113 ? 0.2477 0.2290 0.1996 0.0120 0.0071 -0.0020 113 VAL A CG1 870 C CG2 . VAL A 113 ? 0.2230 0.2509 0.1686 0.0021 0.0048 0.0126 113 VAL A CG2 871 N N . GLY A 114 ? 0.1978 0.2310 0.1801 0.0163 0.0080 0.0191 114 GLY A N 872 C CA . GLY A 114 ? 0.2054 0.2285 0.1860 0.0172 0.0036 0.0184 114 GLY A CA 873 C C . GLY A 114 ? 0.2228 0.2250 0.1928 0.0218 0.0156 0.0149 114 GLY A C 874 O O . GLY A 114 ? 0.2264 0.2184 0.1798 0.0265 0.0261 0.0057 114 GLY A O 875 N N . LEU A 115 ? 0.2270 0.2209 0.1749 0.0159 0.0198 0.0154 115 LEU A N 876 C CA . LEU A 115 ? 0.2389 0.2285 0.1777 0.0159 0.0228 0.0160 115 LEU A CA 877 C C . LEU A 115 ? 0.2302 0.2246 0.1725 0.0132 0.0193 0.0176 115 LEU A C 878 O O . LEU A 115 ? 0.2423 0.2400 0.1828 0.0138 0.0267 0.0207 115 LEU A O 879 C CB . LEU A 115 ? 0.2282 0.2226 0.1639 0.0151 0.0236 0.0241 115 LEU A CB 880 C CG . LEU A 115 ? 0.2156 0.2413 0.1592 0.0170 0.0200 0.0265 115 LEU A CG 881 C CD1 . LEU A 115 ? 0.2398 0.2436 0.1495 0.0090 0.0174 0.0127 115 LEU A CD1 882 C CD2 . LEU A 115 ? 0.2227 0.2285 0.1724 0.0067 0.0143 0.0187 115 LEU A CD2 883 N N . GLY A 116 ? 0.2473 0.2375 0.1842 0.0131 0.0228 0.0133 116 GLY A N 884 C CA . GLY A 116 ? 0.2417 0.2378 0.1909 0.0108 0.0197 0.0135 116 GLY A CA 885 C C . GLY A 116 ? 0.2523 0.2479 0.2043 0.0098 0.0173 0.0101 116 GLY A C 886 O O . GLY A 116 ? 0.2544 0.2502 0.2163 0.0133 0.0291 0.0194 116 GLY A O 887 N N . ALA A 117 ? 0.2504 0.2490 0.1952 0.0163 0.0206 0.0115 117 ALA A N 888 C CA . ALA A 117 ? 0.2564 0.2501 0.2099 0.0122 0.0178 0.0105 117 ALA A CA 889 C C . ALA A 117 ? 0.2572 0.2523 0.2180 0.0124 0.0180 0.0105 117 ALA A C 890 O O . ALA A 117 ? 0.2686 0.2631 0.2055 0.0041 0.0254 0.0169 117 ALA A O 891 C CB . ALA A 117 ? 0.2599 0.2478 0.2137 0.0120 0.0133 0.0057 117 ALA A CB 892 N N . THR A 118 ? 0.2565 0.2529 0.2098 0.0099 0.0190 0.0086 118 THR A N 893 C CA . THR A 118 ? 0.2656 0.2624 0.2228 0.0064 0.0164 0.0069 118 THR A CA 894 C C . THR A 118 ? 0.2658 0.2675 0.2278 0.0008 0.0183 0.0066 118 THR A C 895 O O . THR A 118 ? 0.2635 0.2878 0.2585 0.0084 0.0227 0.0103 118 THR A O 896 C CB . THR A 118 ? 0.2676 0.2528 0.2231 0.0045 0.0147 0.0117 118 THR A CB 897 O OG1 . THR A 118 ? 0.2708 0.2556 0.1974 0.0038 0.0206 0.0109 118 THR A OG1 898 C CG2 . THR A 118 ? 0.2463 0.2448 0.2277 0.0007 0.0124 0.0122 118 THR A CG2 899 N N . ARG A 119 ? 0.2752 0.2734 0.2287 0.0006 0.0212 0.0093 119 ARG A N 900 C CA . ARG A 119 ? 0.2898 0.2809 0.2374 -0.0046 0.0215 0.0140 119 ARG A CA 901 C C . ARG A 119 ? 0.2956 0.2848 0.2560 -0.0090 0.0196 0.0096 119 ARG A C 902 O O . ARG A 119 ? 0.3199 0.2937 0.2622 -0.0108 0.0268 0.0173 119 ARG A O 903 C CB . ARG A 119 ? 0.2869 0.2736 0.2460 -0.0059 0.0233 0.0127 119 ARG A CB 904 C CG . ARG A 119 ? 0.2960 0.2838 0.2525 -0.0080 0.0204 0.0052 119 ARG A CG 905 C CD . ARG A 119 ? 0.3065 0.2695 0.2730 0.0018 0.0058 0.0054 119 ARG A CD 906 N NE . ARG A 119 ? 0.3036 0.2847 0.2681 0.0085 0.0166 0.0031 119 ARG A NE 907 C CZ . ARG A 119 ? 0.3010 0.2762 0.2557 0.0042 0.0009 0.0081 119 ARG A CZ 908 N NH1 . ARG A 119 ? 0.2708 0.2710 0.2061 0.0171 0.0315 0.0145 119 ARG A NH1 909 N NH2 . ARG A 119 ? 0.3078 0.3086 0.2403 0.0121 0.0275 0.0022 119 ARG A NH2 910 N N . ASP A 120 ? 0.2888 0.2855 0.2498 -0.0082 0.0295 0.0114 120 ASP A N 911 C CA . ASP A 120 ? 0.2847 0.2971 0.2614 -0.0038 0.0261 0.0137 120 ASP A CA 912 C C . ASP A 120 ? 0.2792 0.2927 0.2644 0.0024 0.0220 0.0086 120 ASP A C 913 O O . ASP A 120 ? 0.2709 0.2804 0.2606 0.0023 0.0297 0.0097 120 ASP A O 914 C CB . ASP A 120 ? 0.2954 0.3086 0.2688 0.0000 0.0242 0.0140 120 ASP A CB 915 C CG . ASP A 120 ? 0.3227 0.3356 0.3129 -0.0071 0.0196 0.0163 120 ASP A CG 916 O OD1 . ASP A 120 ? 0.3681 0.3668 0.3322 -0.0322 0.0200 0.0076 120 ASP A OD1 917 O OD2 . ASP A 120 ? 0.3221 0.4103 0.3307 -0.0023 0.0162 0.0384 120 ASP A OD2 918 N N . PRO A 121 ? 0.2803 0.2857 0.2671 0.0017 0.0215 0.0071 121 PRO A N 919 C CA . PRO A 121 ? 0.2756 0.2849 0.2704 0.0030 0.0232 0.0066 121 PRO A CA 920 C C . PRO A 121 ? 0.2692 0.2783 0.2726 0.0000 0.0219 0.0031 121 PRO A C 921 O O . PRO A 121 ? 0.2545 0.2755 0.2713 -0.0081 0.0266 0.0146 121 PRO A O 922 C CB . PRO A 121 ? 0.2811 0.2926 0.2694 0.0037 0.0176 0.0086 121 PRO A CB 923 C CG . PRO A 121 ? 0.2897 0.2978 0.2823 0.0094 0.0189 0.0015 121 PRO A CG 924 C CD . PRO A 121 ? 0.2749 0.2881 0.2785 0.0075 0.0203 0.0082 121 PRO A CD 925 N N . TYR A 122 ? 0.2668 0.2736 0.2732 -0.0022 0.0194 -0.0002 122 TYR A N 926 C CA . TYR A 122 ? 0.2807 0.2767 0.2766 -0.0078 0.0171 -0.0027 122 TYR A CA 927 C C . TYR A 122 ? 0.2654 0.2658 0.2592 0.0001 0.0144 -0.0050 122 TYR A C 928 O O . TYR A 122 ? 0.2628 0.2611 0.2470 -0.0011 0.0235 -0.0145 122 TYR A O 929 C CB . TYR A 122 ? 0.2991 0.3018 0.3114 -0.0121 0.0141 0.0010 122 TYR A CB 930 C CG . TYR A 122 ? 0.3235 0.3146 0.3234 -0.0158 0.0053 -0.0016 122 TYR A CG 931 C CD1 . TYR A 122 ? 0.3518 0.3436 0.3375 -0.0191 0.0019 -0.0024 122 TYR A CD1 932 C CD2 . TYR A 122 ? 0.3348 0.3186 0.3304 -0.0193 0.0050 0.0093 122 TYR A CD2 933 C CE1 . TYR A 122 ? 0.3531 0.3701 0.3511 -0.0097 -0.0077 0.0033 122 TYR A CE1 934 C CE2 . TYR A 122 ? 0.3453 0.3470 0.3435 -0.0195 0.0012 0.0002 122 TYR A CE2 935 C CZ . TYR A 122 ? 0.3538 0.3549 0.3420 -0.0081 -0.0059 0.0005 122 TYR A CZ 936 O OH . TYR A 122 ? 0.3752 0.3949 0.3607 -0.0118 -0.0179 -0.0087 122 TYR A OH 937 N N . LEU A 123 ? 0.2624 0.2565 0.2459 -0.0061 0.0177 -0.0077 123 LEU A N 938 C CA . LEU A 123 ? 0.2499 0.2531 0.2337 0.0025 0.0149 -0.0092 123 LEU A CA 939 C C . LEU A 123 ? 0.2391 0.2468 0.2311 -0.0021 0.0137 -0.0030 123 LEU A C 940 O O . LEU A 123 ? 0.2336 0.2562 0.2222 0.0013 0.0237 -0.0093 123 LEU A O 941 C CB . LEU A 123 ? 0.2545 0.2519 0.2311 0.0021 0.0168 -0.0076 123 LEU A CB 942 C CG . LEU A 123 ? 0.2470 0.2576 0.2304 0.0006 0.0008 -0.0106 123 LEU A CG 943 C CD1 . LEU A 123 ? 0.2552 0.2893 0.2705 0.0020 0.0044 0.0086 123 LEU A CD1 944 C CD2 . LEU A 123 ? 0.2771 0.2695 0.2447 0.0102 0.0082 -0.0126 123 LEU A CD2 945 N N . VAL A 124 ? 0.2269 0.2479 0.2311 -0.0057 0.0199 -0.0058 124 VAL A N 946 C CA . VAL A 124 ? 0.2172 0.2365 0.2233 -0.0081 0.0152 -0.0029 124 VAL A CA 947 C C . VAL A 124 ? 0.2204 0.2267 0.2255 -0.0066 0.0180 -0.0057 124 VAL A C 948 O O . VAL A 124 ? 0.2153 0.2055 0.2281 -0.0080 0.0193 -0.0025 124 VAL A O 949 C CB . VAL A 124 ? 0.2176 0.2371 0.2240 -0.0060 0.0164 -0.0048 124 VAL A CB 950 C CG1 . VAL A 124 ? 0.2091 0.2476 0.2325 -0.0073 0.0070 0.0124 124 VAL A CG1 951 C CG2 . VAL A 124 ? 0.2273 0.2416 0.2070 -0.0182 0.0064 -0.0067 124 VAL A CG2 952 N N . LYS A 125 ? 0.2238 0.2362 0.2218 -0.0110 0.0150 -0.0181 125 LYS A N 953 C CA . LYS A 125 ? 0.2328 0.2376 0.2295 -0.0128 0.0157 -0.0131 125 LYS A CA 954 C C . LYS A 125 ? 0.2264 0.2347 0.2331 -0.0151 0.0163 -0.0125 125 LYS A C 955 O O . LYS A 125 ? 0.2214 0.2474 0.2197 -0.0147 0.0234 0.0004 125 LYS A O 956 C CB . LYS A 125 ? 0.2341 0.2246 0.2310 -0.0064 0.0163 -0.0153 125 LYS A CB 957 C CG . LYS A 125 ? 0.2668 0.2379 0.2314 -0.0026 0.0188 -0.0139 125 LYS A CG 958 C CD . LYS A 125 ? 0.2826 0.2600 0.2872 -0.0126 0.0216 -0.0171 125 LYS A CD 959 C CE . LYS A 125 ? 0.3193 0.2762 0.3056 -0.0256 0.0246 -0.0133 125 LYS A CE 960 N NZ . LYS A 125 ? 0.3490 0.2875 0.3389 -0.0223 0.0291 -0.0284 125 LYS A NZ 961 N N . ARG A 126 ? 0.2044 0.2377 0.2346 -0.0133 0.0142 -0.0089 126 ARG A N 962 C CA . ARG A 126 ? 0.2520 0.2675 0.2661 -0.0174 0.0107 -0.0088 126 ARG A CA 963 C C . ARG A 126 ? 0.1969 0.2299 0.2169 -0.0095 0.0177 -0.0122 126 ARG A C 964 O O . ARG A 126 ? 0.2025 0.2349 0.2067 -0.0116 0.0149 -0.0208 126 ARG A O 965 C CB . ARG A 126 ? 0.1872 0.2522 0.2457 -0.0160 0.0337 -0.0073 126 ARG A CB 966 C CG . ARG A 126 ? 0.2993 0.2848 0.3043 -0.0185 -0.0084 0.0027 126 ARG A CG 967 C CD . ARG A 126 ? 0.1913 0.2155 0.2920 0.0256 0.0594 -0.0112 126 ARG A CD 968 N NE . ARG A 126 ? 0.5075 0.5456 0.5707 -0.1422 -0.1319 0.0907 126 ARG A NE 969 C CZ . ARG A 126 ? 0.2493 0.2855 0.2746 0.1184 0.0571 -0.0160 126 ARG A CZ 970 N NH1 . ARG A 126 ? 0.3734 0.4388 0.5078 -0.0211 0.0038 -0.0334 126 ARG A NH1 971 N NH2 . ARG A 126 ? 0.5502 0.5551 0.4857 -0.1223 0.0039 -0.0097 126 ARG A NH2 972 N N . ILE A 127 ? 0.2053 0.2277 0.2071 -0.0079 0.0216 -0.0123 127 ILE A N 973 C CA . ILE A 127 ? 0.1991 0.2262 0.1897 -0.0114 0.0175 -0.0152 127 ILE A CA 974 C C . ILE A 127 ? 0.2005 0.2261 0.1986 -0.0078 0.0166 -0.0107 127 ILE A C 975 O O . ILE A 127 ? 0.2184 0.2149 0.2003 -0.0059 0.0263 0.0026 127 ILE A O 976 C CB . ILE A 127 ? 0.1902 0.2193 0.1890 -0.0078 0.0110 -0.0154 127 ILE A CB 977 C CG1 . ILE A 127 ? 0.2086 0.2272 0.1751 -0.0103 0.0145 -0.0268 127 ILE A CG1 978 C CG2 . ILE A 127 ? 0.1987 0.2389 0.2090 -0.0176 0.0018 -0.0123 127 ILE A CG2 979 C CD1 . ILE A 127 ? 0.1958 0.2190 0.1688 -0.0046 0.0084 -0.0191 127 ILE A CD1 980 N N . GLY A 128 ? 0.1923 0.2170 0.1939 -0.0053 0.0219 -0.0041 128 GLY A N 981 C CA . GLY A 128 ? 0.2095 0.2312 0.1969 -0.0007 0.0152 -0.0078 128 GLY A CA 982 C C . GLY A 128 ? 0.2194 0.2347 0.2049 -0.0079 0.0130 -0.0110 128 GLY A C 983 O O . GLY A 128 ? 0.2147 0.2393 0.2036 -0.0175 0.0091 -0.0010 128 GLY A O 984 N N . GLU A 129 ? 0.2182 0.2513 0.2089 -0.0046 0.0134 -0.0123 129 GLU A N 985 C CA . GLU A 129 ? 0.2275 0.2629 0.2404 -0.0067 0.0030 -0.0125 129 GLU A CA 986 C C . GLU A 129 ? 0.2137 0.2583 0.2243 -0.0013 0.0067 -0.0132 129 GLU A C 987 O O . GLU A 129 ? 0.2191 0.2532 0.2149 0.0051 0.0139 -0.0231 129 GLU A O 988 C CB . GLU A 129 ? 0.2354 0.2632 0.2453 -0.0125 0.0073 -0.0102 129 GLU A CB 989 C CG . GLU A 129 ? 0.2612 0.2698 0.2718 -0.0116 0.0030 -0.0065 129 GLU A CG 990 C CD . GLU A 129 ? 0.2674 0.2958 0.3169 -0.0146 0.0010 -0.0028 129 GLU A CD 991 O OE1 . GLU A 129 ? 0.3406 0.3319 0.3812 -0.0343 -0.0040 0.0147 129 GLU A OE1 992 O OE2 . GLU A 129 ? 0.2716 0.3680 0.3878 -0.0224 0.0116 -0.0137 129 GLU A OE2 993 N N . ALA A 130 ? 0.2152 0.2464 0.2038 -0.0072 0.0099 -0.0185 130 ALA A N 994 C CA . ALA A 130 ? 0.2078 0.2483 0.2068 -0.0021 0.0122 -0.0188 130 ALA A CA 995 C C . ALA A 130 ? 0.2006 0.2436 0.1962 -0.0023 0.0122 -0.0120 130 ALA A C 996 O O . ALA A 130 ? 0.1978 0.2571 0.2073 -0.0019 0.0053 -0.0110 130 ALA A O 997 C CB . ALA A 130 ? 0.2234 0.2487 0.2099 0.0000 0.0230 -0.0224 130 ALA A CB 998 N N . THR A 131 ? 0.1869 0.2473 0.1966 -0.0020 0.0160 -0.0140 131 THR A N 999 C CA . THR A 131 ? 0.1942 0.2444 0.1927 -0.0048 0.0038 -0.0041 131 THR A CA 1000 C C . THR A 131 ? 0.1912 0.2438 0.1912 -0.0029 0.0062 -0.0022 131 THR A C 1001 O O . THR A 131 ? 0.2009 0.2457 0.1947 -0.0128 0.0047 -0.0036 131 THR A O 1002 C CB . THR A 131 ? 0.1920 0.2522 0.1840 -0.0061 0.0027 -0.0083 131 THR A CB 1003 O OG1 . THR A 131 ? 0.1984 0.2447 0.1922 -0.0084 0.0132 0.0033 131 THR A OG1 1004 C CG2 . THR A 131 ? 0.2026 0.2388 0.1907 -0.0230 0.0025 0.0074 131 THR A CG2 1005 N N . ALA A 132 ? 0.2028 0.2418 0.1861 -0.0041 0.0120 -0.0079 132 ALA A N 1006 C CA . ALA A 132 ? 0.2114 0.2421 0.1949 -0.0019 0.0140 -0.0031 132 ALA A CA 1007 C C . ALA A 132 ? 0.2185 0.2505 0.1993 -0.0039 0.0092 -0.0044 132 ALA A C 1008 O O . ALA A 132 ? 0.2320 0.2552 0.2053 -0.0033 0.0124 0.0043 132 ALA A O 1009 C CB . ALA A 132 ? 0.2266 0.2436 0.2002 -0.0037 0.0189 -0.0031 132 ALA A CB 1010 N N . LEU A 133 ? 0.2071 0.2542 0.1974 -0.0022 0.0136 0.0018 133 LEU A N 1011 C CA . LEU A 133 ? 0.2101 0.2523 0.2139 -0.0028 0.0082 -0.0048 133 LEU A CA 1012 C C . LEU A 133 ? 0.2088 0.2530 0.2142 -0.0031 0.0101 -0.0012 133 LEU A C 1013 O O . LEU A 133 ? 0.2137 0.2632 0.2105 -0.0077 0.0101 -0.0037 133 LEU A O 1014 C CB . LEU A 133 ? 0.2091 0.2575 0.2183 -0.0110 0.0096 -0.0050 133 LEU A CB 1015 C CG . LEU A 133 ? 0.2382 0.2651 0.2426 -0.0055 0.0182 -0.0090 133 LEU A CG 1016 C CD1 . LEU A 133 ? 0.2328 0.3002 0.2590 -0.0141 0.0153 -0.0069 133 LEU A CD1 1017 C CD2 . LEU A 133 ? 0.2869 0.2870 0.2444 -0.0109 0.0000 -0.0174 133 LEU A CD2 1018 N N . GLU A 134 ? 0.1952 0.2391 0.2019 -0.0005 0.0122 -0.0042 134 GLU A N 1019 C CA . GLU A 134 ? 0.1957 0.2413 0.2102 0.0008 0.0124 -0.0114 134 GLU A CA 1020 C C . GLU A 134 ? 0.1955 0.2339 0.2037 0.0014 0.0142 -0.0067 134 GLU A C 1021 O O . GLU A 134 ? 0.1970 0.2350 0.1998 0.0068 0.0092 0.0028 134 GLU A O 1022 C CB . GLU A 134 ? 0.2040 0.2575 0.2113 0.0005 0.0150 -0.0079 134 GLU A CB 1023 C CG . GLU A 134 ? 0.1903 0.2509 0.2197 0.0237 0.0170 -0.0190 134 GLU A CG 1024 C CD . GLU A 134 ? 0.2258 0.2444 0.2001 0.0070 0.0040 -0.0089 134 GLU A CD 1025 O OE1 . GLU A 134 ? 0.2580 0.2377 0.1831 0.0100 0.0129 -0.0088 134 GLU A OE1 1026 O OE2 . GLU A 134 ? 0.2069 0.2967 0.2181 0.0243 0.0052 -0.0128 134 GLU A OE2 1027 N N . VAL A 135 ? 0.1922 0.2337 0.1880 -0.0007 0.0105 -0.0017 135 VAL A N 1028 C CA . VAL A 135 ? 0.1965 0.2288 0.1837 0.0076 0.0039 -0.0019 135 VAL A CA 1029 C C . VAL A 135 ? 0.2035 0.2304 0.1821 -0.0009 0.0064 -0.0053 135 VAL A C 1030 O O . VAL A 135 ? 0.2245 0.2356 0.1722 -0.0058 -0.0037 -0.0035 135 VAL A O 1031 C CB . VAL A 135 ? 0.1811 0.2244 0.1733 0.0058 0.0068 0.0034 135 VAL A CB 1032 C CG1 . VAL A 135 ? 0.1703 0.2078 0.1918 0.0110 0.0039 0.0097 135 VAL A CG1 1033 C CG2 . VAL A 135 ? 0.1842 0.2143 0.1769 0.0102 0.0055 -0.0019 135 VAL A CG2 1034 N N . ARG A 136 ? 0.2130 0.2316 0.1861 0.0035 0.0055 -0.0102 136 ARG A N 1035 C CA . ARG A 136 ? 0.2193 0.2394 0.2017 0.0022 0.0084 -0.0073 136 ARG A CA 1036 C C . ARG A 136 ? 0.2160 0.2423 0.2075 0.0054 0.0068 -0.0051 136 ARG A C 1037 O O . ARG A 136 ? 0.2149 0.2458 0.2083 0.0028 0.0105 -0.0080 136 ARG A O 1038 C CB . ARG A 136 ? 0.2143 0.2324 0.1971 0.0035 0.0116 -0.0052 136 ARG A CB 1039 C CG . ARG A 136 ? 0.1982 0.2181 0.2001 0.0024 0.0335 -0.0145 136 ARG A CG 1040 C CD . ARG A 136 ? 0.1991 0.2427 0.2251 -0.0075 0.0381 -0.0288 136 ARG A CD 1041 N NE . ARG A 136 ? 0.2108 0.2569 0.2168 -0.0024 0.0039 -0.0025 136 ARG A NE 1042 C CZ . ARG A 136 ? 0.2306 0.2738 0.2341 0.0046 0.0002 -0.0090 136 ARG A CZ 1043 N NH1 . ARG A 136 ? 0.2287 0.2884 0.2138 -0.0189 -0.0067 -0.0247 136 ARG A NH1 1044 N NH2 . ARG A 136 ? 0.2693 0.2827 0.2311 0.0068 -0.0030 -0.0123 136 ARG A NH2 1045 N N . ALA A 137 ? 0.2077 0.2477 0.2186 0.0062 0.0069 -0.0035 137 ALA A N 1046 C CA . ALA A 137 ? 0.2118 0.2488 0.2108 0.0084 0.0016 -0.0021 137 ALA A CA 1047 C C . ALA A 137 ? 0.2163 0.2586 0.2078 0.0132 0.0037 -0.0003 137 ALA A C 1048 O O . ALA A 137 ? 0.2126 0.2611 0.1893 0.0123 0.0002 -0.0003 137 ALA A O 1049 C CB . ALA A 137 ? 0.2054 0.2496 0.2191 0.0198 0.0051 0.0025 137 ALA A CB 1050 N N . THR A 138 ? 0.2032 0.2512 0.1893 0.0104 -0.0053 -0.0082 138 THR A N 1051 C CA . THR A 138 ? 0.2191 0.2466 0.1896 0.0091 -0.0065 0.0015 138 THR A CA 1052 C C . THR A 138 ? 0.2191 0.2483 0.1838 0.0116 -0.0089 0.0081 138 THR A C 1053 O O . THR A 138 ? 0.2269 0.2678 0.1998 0.0047 -0.0087 0.0054 138 THR A O 1054 C CB . THR A 138 ? 0.2093 0.2345 0.1912 0.0166 -0.0073 0.0007 138 THR A CB 1055 O OG1 . THR A 138 ? 0.2397 0.2436 0.1809 -0.0010 -0.0234 0.0176 138 THR A OG1 1056 C CG2 . THR A 138 ? 0.2191 0.2530 0.1972 0.0070 -0.0088 -0.0186 138 THR A CG2 1057 N N . GLY A 139 ? 0.2350 0.2649 0.1863 0.0179 -0.0084 0.0065 139 GLY A N 1058 C CA . GLY A 139 ? 0.2213 0.2597 0.1903 0.0174 -0.0054 0.0083 139 GLY A CA 1059 C C . GLY A 139 ? 0.2376 0.2709 0.1974 0.0225 -0.0026 0.0037 139 GLY A C 1060 O O . GLY A 139 ? 0.2562 0.3031 0.2105 0.0239 0.0030 0.0025 139 GLY A O 1061 N N . ILE A 140 ? 0.2171 0.2462 0.1773 0.0073 -0.0020 0.0014 140 ILE A N 1062 C CA . ILE A 140 ? 0.2296 0.2254 0.1806 0.0034 -0.0028 0.0048 140 ILE A CA 1063 C C . ILE A 140 ? 0.2273 0.2303 0.1827 0.0011 -0.0013 -0.0063 140 ILE A C 1064 O O . ILE A 140 ? 0.2324 0.2500 0.1896 -0.0051 0.0106 -0.0011 140 ILE A O 1065 C CB . ILE A 140 ? 0.2132 0.2086 0.1698 0.0071 -0.0074 0.0004 140 ILE A CB 1066 C CG1 . ILE A 140 ? 0.2309 0.2096 0.1917 -0.0003 0.0051 0.0104 140 ILE A CG1 1067 C CG2 . ILE A 140 ? 0.2140 0.2122 0.1812 0.0128 -0.0138 0.0094 140 ILE A CG2 1068 C CD1 . ILE A 140 ? 0.2568 0.2225 0.2226 0.0025 -0.0034 0.0029 140 ILE A CD1 1069 N N . GLN A 141 ? 0.2151 0.2373 0.1716 -0.0006 0.0067 -0.0056 141 GLN A N 1070 C CA . GLN A 141 ? 0.2179 0.2295 0.1646 0.0084 0.0115 -0.0047 141 GLN A CA 1071 C C . GLN A 141 ? 0.2029 0.2266 0.1632 0.0057 0.0128 -0.0042 141 GLN A C 1072 O O . GLN A 141 ? 0.2013 0.2392 0.1605 -0.0113 0.0247 -0.0082 141 GLN A O 1073 C CB . GLN A 141 ? 0.2228 0.2436 0.1803 0.0107 0.0158 -0.0072 141 GLN A CB 1074 C CG . GLN A 141 ? 0.2280 0.2477 0.1799 -0.0026 0.0206 -0.0053 141 GLN A CG 1075 C CD . GLN A 141 ? 0.2380 0.2698 0.2358 -0.0111 0.0084 -0.0034 141 GLN A CD 1076 O OE1 . GLN A 141 ? 0.1909 0.3092 0.2151 -0.0241 0.0185 -0.0106 141 GLN A OE1 1077 N NE2 . GLN A 141 ? 0.2443 0.2974 0.2299 -0.0178 0.0232 -0.0121 141 GLN A NE2 1078 N N . TYR A 142 ? 0.1845 0.2258 0.1574 0.0014 0.0032 0.0012 142 TYR A N 1079 C CA . TYR A 142 ? 0.1827 0.2245 0.1716 -0.0016 0.0074 0.0020 142 TYR A CA 1080 C C . TYR A 142 ? 0.1846 0.2168 0.1750 -0.0020 0.0146 0.0017 142 TYR A C 1081 O O . TYR A 142 ? 0.2006 0.2231 0.1773 -0.0140 0.0245 0.0127 142 TYR A O 1082 C CB . TYR A 142 ? 0.1732 0.2233 0.1756 0.0046 0.0106 0.0072 142 TYR A CB 1083 C CG . TYR A 142 ? 0.1933 0.2327 0.1829 -0.0049 -0.0013 0.0089 142 TYR A CG 1084 C CD1 . TYR A 142 ? 0.1840 0.2364 0.1772 -0.0044 -0.0060 0.0167 142 TYR A CD1 1085 C CD2 . TYR A 142 ? 0.1913 0.2394 0.2105 0.0069 -0.0023 0.0011 142 TYR A CD2 1086 C CE1 . TYR A 142 ? 0.1950 0.2464 0.2128 0.0032 -0.0104 0.0056 142 TYR A CE1 1087 C CE2 . TYR A 142 ? 0.2239 0.2388 0.1804 0.0006 -0.0057 0.0026 142 TYR A CE2 1088 C CZ . TYR A 142 ? 0.2057 0.2346 0.1982 -0.0123 -0.0124 0.0136 142 TYR A CZ 1089 O OH . TYR A 142 ? 0.1990 0.2600 0.2197 0.0138 0.0009 0.0191 142 TYR A OH 1090 N N . ALA A 143 ? 0.1933 0.2165 0.1701 0.0003 0.0101 0.0054 143 ALA A N 1091 C CA . ALA A 143 ? 0.1724 0.2174 0.1730 -0.0030 0.0127 0.0031 143 ALA A CA 1092 C C . ALA A 143 ? 0.1845 0.2143 0.1729 -0.0014 0.0126 0.0086 143 ALA A C 1093 O O . ALA A 143 ? 0.1980 0.2246 0.1779 -0.0015 0.0093 0.0105 143 ALA A O 1094 C CB . ALA A 143 ? 0.1734 0.2225 0.1972 -0.0021 0.0147 0.0010 143 ALA A CB 1095 N N . PHE A 144 ? 0.1747 0.2230 0.1661 -0.0033 0.0072 0.0144 144 PHE A N 1096 C CA . PHE A 144 ? 0.1856 0.2154 0.1583 -0.0069 0.0133 0.0144 144 PHE A CA 1097 C C . PHE A 144 ? 0.1853 0.2182 0.1639 -0.0058 0.0151 0.0078 144 PHE A C 1098 O O . PHE A 144 ? 0.2035 0.2148 0.1834 -0.0120 0.0160 0.0013 144 PHE A O 1099 C CB . PHE A 144 ? 0.1876 0.2219 0.1725 -0.0044 0.0166 0.0149 144 PHE A CB 1100 C CG . PHE A 144 ? 0.2018 0.2219 0.1895 -0.0134 0.0196 0.0097 144 PHE A CG 1101 C CD1 . PHE A 144 ? 0.2112 0.2117 0.1797 -0.0160 0.0313 0.0194 144 PHE A CD1 1102 C CD2 . PHE A 144 ? 0.2144 0.2204 0.1929 -0.0095 0.0232 0.0263 144 PHE A CD2 1103 C CE1 . PHE A 144 ? 0.2288 0.2640 0.2106 -0.0038 0.0090 0.0011 144 PHE A CE1 1104 C CE2 . PHE A 144 ? 0.2533 0.2626 0.2420 -0.0098 0.0229 0.0045 144 PHE A CE2 1105 C CZ . PHE A 144 ? 0.2079 0.2427 0.1872 -0.0126 0.0241 0.0010 144 PHE A CZ 1106 N N . ALA A 145 ? 0.1910 0.2151 0.1648 -0.0020 0.0167 0.0165 145 ALA A N 1107 C CA . ALA A 145 ? 0.1880 0.2154 0.1772 -0.0022 0.0182 0.0096 145 ALA A CA 1108 C C . ALA A 145 ? 0.1987 0.2120 0.1787 0.0023 0.0157 0.0112 145 ALA A C 1109 O O . ALA A 145 ? 0.1974 0.2168 0.1728 -0.0037 0.0196 0.0087 145 ALA A O 1110 C CB . ALA A 145 ? 0.1930 0.2236 0.1831 0.0080 0.0135 0.0102 145 ALA A CB 1111 N N . PRO A 146 ? 0.2120 0.2168 0.1869 0.0031 0.0109 0.0113 146 PRO A N 1112 C CA . PRO A 146 ? 0.2206 0.2217 0.1854 -0.0018 0.0121 0.0097 146 PRO A CA 1113 C C . PRO A 146 ? 0.2254 0.2291 0.1972 0.0004 0.0120 0.0151 146 PRO A C 1114 O O . PRO A 146 ? 0.2213 0.2460 0.1892 0.0024 0.0137 0.0063 146 PRO A O 1115 C CB . PRO A 146 ? 0.2228 0.2224 0.1940 -0.0026 0.0127 0.0130 146 PRO A CB 1116 C CG . PRO A 146 ? 0.2253 0.2301 0.1820 -0.0010 0.0117 0.0015 146 PRO A CG 1117 C CD . PRO A 146 ? 0.2103 0.2184 0.1931 -0.0066 0.0085 0.0176 146 PRO A CD 1118 N N . CYS A 147 ? 0.2365 0.2348 0.1959 0.0023 0.0074 0.0127 147 CYS A N 1119 C CA . CYS A 147 ? 0.2517 0.2348 0.1976 0.0058 0.0064 0.0213 147 CYS A CA 1120 C C . CYS A 147 ? 0.2439 0.2448 0.2014 0.0066 0.0090 0.0209 147 CYS A C 1121 O O . CYS A 147 ? 0.2473 0.2523 0.1794 0.0130 0.0134 0.0368 147 CYS A O 1122 C CB . CYS A 147 ? 0.2519 0.2392 0.2037 -0.0014 0.0027 0.0044 147 CYS A CB 1123 S SG . CYS A 147 ? 0.3006 0.2821 0.2291 0.0140 -0.0102 0.0358 147 CYS A SG 1124 N N . ILE A 148 ? 0.2432 0.2266 0.1926 0.0108 0.0144 0.0300 148 ILE A N 1125 C CA . ILE A 148 ? 0.2514 0.2399 0.2137 0.0100 0.0159 0.0230 148 ILE A CA 1126 C C . ILE A 148 ? 0.2507 0.2461 0.2154 0.0145 0.0225 0.0235 148 ILE A C 1127 O O . ILE A 148 ? 0.2683 0.2588 0.2160 0.0221 0.0177 0.0282 148 ILE A O 1128 C CB . ILE A 148 ? 0.2450 0.2450 0.2190 0.0082 0.0117 0.0219 148 ILE A CB 1129 C CG1 . ILE A 148 ? 0.2540 0.2267 0.2226 0.0046 0.0245 0.0128 148 ILE A CG1 1130 C CG2 . ILE A 148 ? 0.2457 0.2583 0.2247 -0.0013 0.0125 0.0130 148 ILE A CG2 1131 C CD1 . ILE A 148 ? 0.2733 0.2422 0.2406 0.0113 0.0164 0.0221 148 ILE A CD1 1132 N N . ALA A 149 ? 0.2525 0.2522 0.2046 0.0105 0.0203 0.0224 149 ALA A N 1133 C CA . ALA A 149 ? 0.2549 0.2604 0.2088 0.0073 0.0207 0.0286 149 ALA A CA 1134 C C . ALA A 149 ? 0.2509 0.2663 0.2064 0.0103 0.0213 0.0304 149 ALA A C 1135 O O . ALA A 149 ? 0.2419 0.2686 0.1963 0.0112 0.0160 0.0512 149 ALA A O 1136 C CB . ALA A 149 ? 0.2614 0.2589 0.2128 0.0042 0.0162 0.0246 149 ALA A CB 1137 N N . VAL A 150 ? 0.2459 0.2695 0.1941 0.0149 0.0247 0.0378 150 VAL A N 1138 C CA . VAL A 150 ? 0.2704 0.2748 0.2183 0.0128 0.0204 0.0363 150 VAL A CA 1139 C C . VAL A 150 ? 0.2759 0.2838 0.2067 0.0145 0.0138 0.0362 150 VAL A C 1140 O O . VAL A 150 ? 0.2687 0.2871 0.1982 0.0227 0.0098 0.0351 150 VAL A O 1141 C CB . VAL A 150 ? 0.2690 0.2639 0.2064 0.0106 0.0214 0.0361 150 VAL A CB 1142 C CG1 . VAL A 150 ? 0.2779 0.2860 0.2394 0.0165 0.0269 0.0426 150 VAL A CG1 1143 C CG2 . VAL A 150 ? 0.2791 0.2699 0.2355 0.0111 0.0168 0.0350 150 VAL A CG2 1144 N N . CYS A 151 ? 0.2823 0.2873 0.2195 0.0220 0.0124 0.0297 151 CYS A N 1145 C CA . CYS A 151 ? 0.2950 0.2949 0.2290 0.0249 0.0042 0.0273 151 CYS A CA 1146 C C . CYS A 151 ? 0.2844 0.2859 0.2271 0.0238 0.0021 0.0276 151 CYS A C 1147 O O . CYS A 151 ? 0.3018 0.3098 0.2260 0.0366 0.0045 0.0267 151 CYS A O 1148 C CB . CYS A 151 ? 0.2991 0.2817 0.2435 0.0250 0.0100 0.0367 151 CYS A CB 1149 S SG . CYS A 151 ? 0.3316 0.3281 0.2188 0.0257 -0.0002 0.0435 151 CYS A SG 1150 N N . ARG A 152 ? 0.2900 0.3081 0.2253 0.0294 -0.0005 0.0223 152 ARG A N 1151 C CA . ARG A 152 ? 0.2796 0.3030 0.2321 0.0316 -0.0023 0.0255 152 ARG A CA 1152 C C . ARG A 152 ? 0.2779 0.3129 0.2422 0.0269 -0.0009 0.0218 152 ARG A C 1153 O O . ARG A 152 ? 0.2939 0.3261 0.2361 0.0344 0.0045 0.0289 152 ARG A O 1154 C CB . ARG A 152 ? 0.2941 0.2989 0.2302 0.0366 -0.0107 0.0324 152 ARG A CB 1155 C CG . ARG A 152 ? 0.2761 0.2920 0.2124 0.0172 -0.0015 0.0345 152 ARG A CG 1156 C CD . ARG A 152 ? 0.3231 0.3648 0.3654 0.0184 -0.0002 -0.0335 152 ARG A CD 1157 N NE . ARG A 152 ? 0.2577 0.2548 0.1639 -0.0103 0.0250 0.1191 152 ARG A NE 1158 C CZ . ARG A 152 ? 0.3991 0.4363 0.4183 0.0022 0.0353 -0.0732 152 ARG A CZ 1159 N NH1 . ARG A 152 ? 0.3156 0.3058 0.1688 0.0456 -0.0452 0.0931 152 ARG A NH1 1160 N NH2 . ARG A 152 ? 0.2529 0.3361 0.2489 0.0067 -0.0576 0.0390 152 ARG A NH2 1161 N N . ASP A 153 ? 0.2793 0.3104 0.2390 0.0281 -0.0071 0.0236 153 ASP A N 1162 C CA . ASP A 153 ? 0.2682 0.3034 0.2379 0.0239 -0.0099 0.0197 153 ASP A CA 1163 C C . ASP A 153 ? 0.2680 0.3087 0.2322 0.0250 -0.0044 0.0151 153 ASP A C 1164 O O . ASP A 153 ? 0.2625 0.3007 0.2257 0.0214 -0.0012 0.0158 153 ASP A O 1165 C CB . ASP A 153 ? 0.2728 0.3081 0.2482 0.0113 -0.0099 0.0161 153 ASP A CB 1166 C CG . ASP A 153 ? 0.3001 0.3359 0.2679 0.0208 -0.0039 0.0019 153 ASP A CG 1167 O OD1 . ASP A 153 ? 0.2522 0.3395 0.2162 0.0275 -0.0333 0.0191 153 ASP A OD1 1168 O OD2 . ASP A 153 ? 0.3045 0.3713 0.2789 0.0319 -0.0349 -0.0119 153 ASP A OD2 1169 N N . PRO A 154 ? 0.2574 0.3029 0.2194 0.0304 -0.0049 0.0154 154 PRO A N 1170 C CA . PRO A 154 ? 0.2491 0.3018 0.2113 0.0302 -0.0079 0.0087 154 PRO A CA 1171 C C . PRO A 154 ? 0.2470 0.3011 0.2056 0.0274 -0.0095 0.0033 154 PRO A C 1172 O O . PRO A 154 ? 0.2564 0.3187 0.2199 0.0302 -0.0108 0.0059 154 PRO A O 1173 C CB . PRO A 154 ? 0.2567 0.2956 0.1951 0.0244 -0.0055 0.0064 154 PRO A CB 1174 C CG . PRO A 154 ? 0.2595 0.3079 0.2052 0.0393 -0.0031 0.0168 154 PRO A CG 1175 C CD . PRO A 154 ? 0.2481 0.2970 0.2093 0.0376 -0.0067 0.0151 154 PRO A CD 1176 N N . ARG A 155 ? 0.2606 0.3085 0.2115 0.0246 -0.0034 0.0016 155 ARG A N 1177 C CA . ARG A 155 ? 0.2526 0.3040 0.2040 0.0140 -0.0146 -0.0009 155 ARG A CA 1178 C C . ARG A 155 ? 0.2482 0.3028 0.2078 0.0148 -0.0120 0.0055 155 ARG A C 1179 O O . ARG A 155 ? 0.2755 0.3178 0.2212 0.0170 -0.0126 0.0074 155 ARG A O 1180 C CB . ARG A 155 ? 0.2555 0.2982 0.2298 0.0254 -0.0049 -0.0008 155 ARG A CB 1181 C CG . ARG A 155 ? 0.2291 0.3072 0.1579 0.0261 -0.0451 0.0023 155 ARG A CG 1182 C CD . ARG A 155 ? 0.3229 0.3696 0.2585 -0.0072 0.0096 -0.0294 155 ARG A CD 1183 N NE . ARG A 155 ? 0.2057 0.3043 0.1535 0.0662 -0.0934 0.0220 155 ARG A NE 1184 C CZ . ARG A 155 ? 0.3716 0.3934 0.3565 -0.0017 0.0504 0.0013 155 ARG A CZ 1185 N NH1 . ARG A 155 ? 0.2723 0.3269 0.2202 -0.0078 -0.0528 -0.0362 155 ARG A NH1 1186 N NH2 . ARG A 155 ? 0.2851 0.3015 0.2394 0.0526 -0.0263 0.0271 155 ARG A NH2 1187 N N . TRP A 156 ? 0.2497 0.3135 0.2184 0.0219 -0.0080 0.0047 156 TRP A N 1188 C CA . TRP A 156 ? 0.2496 0.2973 0.2082 0.0176 -0.0085 0.0095 156 TRP A CA 1189 C C . TRP A 156 ? 0.2523 0.2977 0.2150 0.0096 -0.0091 0.0087 156 TRP A C 1190 O O . TRP A 156 ? 0.2419 0.2909 0.1912 0.0120 0.0006 0.0172 156 TRP A O 1191 C CB . TRP A 156 ? 0.2515 0.3023 0.2360 0.0142 -0.0065 0.0065 156 TRP A CB 1192 C CG . TRP A 156 ? 0.2389 0.2867 0.2260 0.0182 -0.0067 0.0108 156 TRP A CG 1193 C CD1 . TRP A 156 ? 0.2605 0.3046 0.2419 0.0159 -0.0127 0.0106 156 TRP A CD1 1194 C CD2 . TRP A 156 ? 0.2635 0.3057 0.2441 0.0103 -0.0086 0.0048 156 TRP A CD2 1195 N NE1 . TRP A 156 ? 0.2659 0.3103 0.2539 0.0124 -0.0151 -0.0019 156 TRP A NE1 1196 C CE2 . TRP A 156 ? 0.2732 0.3035 0.2512 0.0099 -0.0038 0.0054 156 TRP A CE2 1197 C CE3 . TRP A 156 ? 0.2835 0.2682 0.2483 0.0167 -0.0090 0.0123 156 TRP A CE3 1198 C CZ2 . TRP A 156 ? 0.2688 0.2828 0.2581 0.0133 -0.0100 -0.0003 156 TRP A CZ2 1199 C CZ3 . TRP A 156 ? 0.2753 0.2956 0.2292 0.0153 -0.0120 0.0119 156 TRP A CZ3 1200 C CH2 . TRP A 156 ? 0.2416 0.2915 0.2448 0.0183 -0.0064 0.0097 156 TRP A CH2 1201 N N . GLY A 157 ? 0.2534 0.2942 0.2138 0.0069 -0.0108 0.0154 157 GLY A N 1202 C CA . GLY A 157 ? 0.2573 0.2845 0.2126 0.0059 -0.0090 0.0090 157 GLY A CA 1203 C C . GLY A 157 ? 0.2509 0.2784 0.2184 0.0051 -0.0033 0.0086 157 GLY A C 1204 O O . GLY A 157 ? 0.2638 0.2895 0.2221 0.0088 -0.0137 0.0060 157 GLY A O 1205 N N . ARG A 158 ? 0.2515 0.2711 0.2119 0.0003 -0.0015 0.0139 158 ARG A N 1206 C CA . ARG A 158 ? 0.2506 0.2687 0.2059 0.0107 0.0053 0.0103 158 ARG A CA 1207 C C . ARG A 158 ? 0.2499 0.2681 0.2187 0.0104 0.0032 0.0069 158 ARG A C 1208 O O . ARG A 158 ? 0.2469 0.2766 0.2111 0.0140 0.0159 0.0072 158 ARG A O 1209 C CB . ARG A 158 ? 0.2505 0.2718 0.2048 0.0083 0.0049 0.0082 158 ARG A CB 1210 C CG . ARG A 158 ? 0.2538 0.2734 0.1927 -0.0019 0.0127 0.0114 158 ARG A CG 1211 C CD . ARG A 158 ? 0.2605 0.2938 0.2094 0.0132 0.0041 0.0021 158 ARG A CD 1212 N NE . ARG A 158 ? 0.2379 0.3024 0.2133 -0.0019 0.0010 -0.0017 158 ARG A NE 1213 C CZ . ARG A 158 ? 0.2639 0.3215 0.2492 -0.0056 -0.0045 0.0049 158 ARG A CZ 1214 N NH1 . ARG A 158 ? 0.2386 0.3143 0.2566 0.0216 0.0117 0.0101 158 ARG A NH1 1215 N NH2 . ARG A 158 ? 0.2069 0.3023 0.2167 -0.0074 -0.0118 0.0084 158 ARG A NH2 1216 N N . CYS A 159 ? 0.2733 0.2883 0.2285 0.0096 0.0041 0.0104 159 CYS A N 1217 C CA . CYS A 159 ? 0.2731 0.2830 0.2261 0.0094 0.0000 0.0118 159 CYS A CA 1218 C C . CYS A 159 ? 0.2538 0.2609 0.2145 0.0087 0.0055 0.0124 159 CYS A C 1219 O O . CYS A 159 ? 0.2453 0.2422 0.1987 0.0130 0.0020 0.0226 159 CYS A O 1220 C CB . CYS A 159 ? 0.2851 0.2951 0.2400 -0.0013 -0.0014 0.0079 159 CYS A CB 1221 S SG . CYS A 159 ? 0.3925 0.3919 0.2869 -0.0178 0.0057 0.0282 159 CYS A SG 1222 N N . TYR A 160 ? 0.2327 0.2443 0.1869 0.0092 0.0128 0.0150 160 TYR A N 1223 C CA . TYR A 160 ? 0.2343 0.2331 0.1916 0.0087 0.0108 0.0132 160 TYR A CA 1224 C C . TYR A 160 ? 0.2312 0.2299 0.1928 0.0046 0.0067 0.0130 160 TYR A C 1225 O O . TYR A 160 ? 0.2343 0.2333 0.2067 0.0064 0.0187 0.0100 160 TYR A O 1226 C CB . TYR A 160 ? 0.2262 0.2298 0.1845 0.0070 0.0073 0.0137 160 TYR A CB 1227 C CG . TYR A 160 ? 0.2161 0.2300 0.1945 0.0019 0.0064 0.0066 160 TYR A CG 1228 C CD1 . TYR A 160 ? 0.2130 0.2348 0.1883 0.0057 0.0103 0.0086 160 TYR A CD1 1229 C CD2 . TYR A 160 ? 0.2048 0.2435 0.2048 -0.0003 0.0136 0.0068 160 TYR A CD2 1230 C CE1 . TYR A 160 ? 0.1764 0.1862 0.1994 0.0012 0.0126 0.0125 160 TYR A CE1 1231 C CE2 . TYR A 160 ? 0.2259 0.2459 0.1865 -0.0130 0.0058 0.0163 160 TYR A CE2 1232 C CZ . TYR A 160 ? 0.1979 0.2333 0.1968 -0.0016 0.0016 -0.0024 160 TYR A CZ 1233 O OH . TYR A 160 ? 0.2082 0.2565 0.1749 -0.0035 0.0050 -0.0011 160 TYR A OH 1234 N N . GLU A 161 ? 0.2304 0.2317 0.1900 0.0047 0.0106 0.0208 161 GLU A N 1235 C CA . GLU A 161 ? 0.2351 0.2398 0.2011 0.0037 0.0139 0.0189 161 GLU A CA 1236 C C . GLU A 161 ? 0.2469 0.2423 0.2011 0.0088 0.0076 0.0176 161 GLU A C 1237 O O . GLU A 161 ? 0.2547 0.2484 0.1897 0.0051 0.0120 0.0206 161 GLU A O 1238 C CB . GLU A 161 ? 0.2249 0.2372 0.2064 0.0014 0.0098 0.0204 161 GLU A CB 1239 C CG . GLU A 161 ? 0.2538 0.2523 0.1958 0.0028 0.0189 0.0177 161 GLU A CG 1240 C CD . GLU A 161 ? 0.2832 0.2949 0.2559 -0.0059 0.0149 0.0274 161 GLU A CD 1241 O OE1 . GLU A 161 ? 0.2308 0.3399 0.2717 -0.0042 0.0069 0.0322 161 GLU A OE1 1242 O OE2 . GLU A 161 ? 0.3255 0.3302 0.2441 -0.0072 0.0274 0.0258 161 GLU A OE2 1243 N N . SER A 162 ? 0.2399 0.2492 0.1957 0.0151 0.0068 0.0180 162 SER A N 1244 C CA . SER A 162 ? 0.2324 0.2414 0.1972 0.0094 0.0011 0.0198 162 SER A CA 1245 C C . SER A 162 ? 0.2246 0.2397 0.1864 0.0153 -0.0024 0.0241 162 SER A C 1246 O O . SER A 162 ? 0.2489 0.2424 0.2204 0.0129 0.0095 0.0208 162 SER A O 1247 C CB . SER A 162 ? 0.2294 0.2423 0.2085 0.0111 -0.0030 0.0203 162 SER A CB 1248 O OG . SER A 162 ? 0.2547 0.2618 0.2282 0.0203 0.0054 0.0356 162 SER A OG 1249 N N . TYR A 163 ? 0.2232 0.2459 0.1896 0.0140 -0.0034 0.0271 163 TYR A N 1250 C CA . TYR A 163 ? 0.2371 0.2608 0.1855 0.0093 0.0069 0.0223 163 TYR A CA 1251 C C . TYR A 163 ? 0.2431 0.2672 0.1940 0.0141 0.0051 0.0266 163 TYR A C 1252 O O . TYR A 163 ? 0.2387 0.2776 0.1976 0.0113 0.0092 0.0320 163 TYR A O 1253 C CB . TYR A 163 ? 0.2371 0.2603 0.1867 0.0084 0.0029 0.0188 163 TYR A CB 1254 C CG . TYR A 163 ? 0.2242 0.2586 0.1862 0.0189 0.0084 0.0198 163 TYR A CG 1255 C CD1 . TYR A 163 ? 0.2432 0.2596 0.1895 0.0150 0.0018 0.0173 163 TYR A CD1 1256 C CD2 . TYR A 163 ? 0.2407 0.2474 0.1784 0.0091 0.0080 -0.0007 163 TYR A CD2 1257 C CE1 . TYR A 163 ? 0.2400 0.2190 0.1845 0.0179 0.0067 0.0127 163 TYR A CE1 1258 C CE2 . TYR A 163 ? 0.2381 0.2463 0.1903 0.0186 0.0125 0.0093 163 TYR A CE2 1259 C CZ . TYR A 163 ? 0.2210 0.2540 0.1885 0.0135 -0.0009 0.0092 163 TYR A CZ 1260 O OH . TYR A 163 ? 0.2405 0.2618 0.1978 0.0142 0.0167 0.0132 163 TYR A OH 1261 N N . SER A 164 ? 0.2489 0.2761 0.1951 0.0107 0.0083 0.0280 164 SER A N 1262 C CA . SER A 164 ? 0.2586 0.2778 0.2016 0.0161 0.0100 0.0246 164 SER A CA 1263 C C . SER A 164 ? 0.2678 0.2797 0.2151 0.0175 0.0057 0.0254 164 SER A C 1264 O O . SER A 164 ? 0.2783 0.2853 0.2022 0.0264 0.0027 0.0353 164 SER A O 1265 C CB . SER A 164 ? 0.2657 0.2695 0.2013 0.0163 0.0237 0.0244 164 SER A CB 1266 O OG . SER A 164 ? 0.2784 0.2781 0.2000 0.0300 0.0284 0.0361 164 SER A OG 1267 N N . GLU A 165 ? 0.2669 0.2786 0.2163 0.0134 0.0045 0.0194 165 GLU A N 1268 C CA . GLU A 165 ? 0.2862 0.2910 0.2496 0.0150 0.0104 0.0165 165 GLU A CA 1269 C C . GLU A 165 ? 0.2844 0.2918 0.2457 0.0188 0.0121 0.0187 165 GLU A C 1270 O O . GLU A 165 ? 0.2908 0.2892 0.2513 0.0325 0.0228 0.0247 165 GLU A O 1271 C CB . GLU A 165 ? 0.2782 0.2914 0.2394 0.0113 0.0111 0.0190 165 GLU A CB 1272 C CG . GLU A 165 ? 0.3041 0.3049 0.2637 0.0015 0.0177 0.0149 165 GLU A CG 1273 C CD . GLU A 165 ? 0.3110 0.3091 0.2591 0.0086 0.0156 0.0159 165 GLU A CD 1274 O OE1 . GLU A 165 ? 0.3378 0.3356 0.2586 0.0023 0.0255 0.0156 165 GLU A OE1 1275 O OE2 . GLU A 165 ? 0.3631 0.3701 0.2745 0.0085 0.0174 0.0369 165 GLU A OE2 1276 N N . ASP A 166 ? 0.2900 0.2929 0.2542 0.0219 0.0177 0.0158 166 ASP A N 1277 C CA . ASP A 166 ? 0.2979 0.3031 0.2794 0.0148 0.0161 0.0139 166 ASP A CA 1278 C C . ASP A 166 ? 0.2916 0.2956 0.2711 0.0182 0.0176 0.0175 166 ASP A C 1279 O O . ASP A 166 ? 0.2750 0.2869 0.2687 0.0304 0.0151 0.0250 166 ASP A O 1280 C CB . ASP A 166 ? 0.3052 0.3072 0.2917 0.0125 0.0167 0.0183 166 ASP A CB 1281 C CG . ASP A 166 ? 0.3543 0.3390 0.3382 0.0037 0.0162 0.0143 166 ASP A CG 1282 O OD1 . ASP A 166 ? 0.3669 0.3312 0.3168 0.0129 0.0428 0.0324 166 ASP A OD1 1283 O OD2 . ASP A 166 ? 0.3711 0.3966 0.3740 -0.0132 0.0386 0.0226 166 ASP A OD2 1284 N N . ARG A 167 ? 0.2904 0.2853 0.2670 0.0250 0.0143 0.0273 167 ARG A N 1285 C CA . ARG A 167 ? 0.2866 0.2754 0.2702 0.0267 0.0209 0.0245 167 ARG A CA 1286 C C . ARG A 167 ? 0.2835 0.2724 0.2666 0.0285 0.0238 0.0276 167 ARG A C 1287 O O . ARG A 167 ? 0.2672 0.2638 0.2575 0.0348 0.0277 0.0390 167 ARG A O 1288 C CB . ARG A 167 ? 0.2975 0.2828 0.2787 0.0259 0.0098 0.0248 167 ARG A CB 1289 C CG . ARG A 167 ? 0.3328 0.3035 0.3099 0.0090 0.0061 0.0233 167 ARG A CG 1290 C CD . ARG A 167 ? 0.3930 0.2981 0.3260 -0.0066 0.0012 0.0364 167 ARG A CD 1291 N NE . ARG A 167 ? 0.4582 0.4724 0.4265 0.0388 -0.0004 0.0150 167 ARG A NE 1292 C CZ . ARG A 167 ? 0.4454 0.2841 0.3111 -0.0433 -0.0738 0.0513 167 ARG A CZ 1293 N NH1 . ARG A 167 ? 0.5258 0.5181 0.5487 -0.0089 0.0077 -0.0282 167 ARG A NH1 1294 N NH2 . ARG A 167 ? 0.5127 0.4045 0.5237 0.0224 0.0281 0.0411 167 ARG A NH2 1295 N N . ARG A 168 ? 0.2809 0.2753 0.2684 0.0176 0.0315 0.0292 168 ARG A N 1296 C CA . ARG A 168 ? 0.2889 0.2777 0.2634 0.0139 0.0279 0.0325 168 ARG A CA 1297 C C . ARG A 168 ? 0.2802 0.2717 0.2572 0.0102 0.0296 0.0237 168 ARG A C 1298 O O . ARG A 168 ? 0.2948 0.2652 0.2594 0.0204 0.0273 0.0350 168 ARG A O 1299 C CB . ARG A 168 ? 0.2974 0.3037 0.2826 0.0078 0.0353 0.0329 168 ARG A CB 1300 C CG . ARG A 168 ? 0.3683 0.3739 0.3613 0.0176 -0.0019 0.0088 168 ARG A CG 1301 C CD . ARG A 168 ? 0.3986 0.3322 0.4045 0.0559 0.0002 0.0915 168 ARG A CD 1302 N NE . ARG A 168 ? 0.6558 0.6085 0.6477 -0.0622 0.1295 -0.0297 168 ARG A NE 1303 C CZ . ARG A 168 ? 0.4400 0.4488 0.4473 0.0254 -0.1390 -0.0308 168 ARG A CZ 1304 N NH1 . ARG A 168 ? 0.6336 0.6937 0.6736 0.0464 0.0386 0.0700 168 ARG A NH1 1305 N NH2 . ARG A 168 ? 0.6460 0.6766 0.6121 -0.0472 0.0200 -0.0222 168 ARG A NH2 1306 N N . ILE A 169 ? 0.2755 0.2581 0.2392 0.0122 0.0292 0.0318 169 ILE A N 1307 C CA . ILE A 169 ? 0.2679 0.2570 0.2377 0.0128 0.0322 0.0234 169 ILE A CA 1308 C C . ILE A 169 ? 0.2595 0.2516 0.2324 0.0087 0.0297 0.0192 169 ILE A C 1309 O O . ILE A 169 ? 0.2442 0.2399 0.2303 0.0176 0.0368 0.0123 169 ILE A O 1310 C CB . ILE A 169 ? 0.2670 0.2577 0.2297 0.0079 0.0278 0.0208 169 ILE A CB 1311 C CG1 . ILE A 169 ? 0.2858 0.2716 0.2341 0.0119 0.0368 0.0100 169 ILE A CG1 1312 C CG2 . ILE A 169 ? 0.2686 0.2573 0.2364 0.0129 0.0336 0.0283 169 ILE A CG2 1313 C CD1 . ILE A 169 ? 0.2793 0.2563 0.2633 0.0192 0.0291 -0.0033 169 ILE A CD1 1314 N N . VAL A 170 ? 0.2519 0.2529 0.2398 0.0111 0.0309 0.0215 170 VAL A N 1315 C CA . VAL A 170 ? 0.2520 0.2439 0.2287 0.0062 0.0249 0.0253 170 VAL A CA 1316 C C . VAL A 170 ? 0.2646 0.2486 0.2491 0.0099 0.0236 0.0260 170 VAL A C 1317 O O . VAL A 170 ? 0.2595 0.2448 0.2395 0.0100 0.0264 0.0267 170 VAL A O 1318 C CB . VAL A 170 ? 0.2554 0.2473 0.2305 0.0076 0.0227 0.0257 170 VAL A CB 1319 C CG1 . VAL A 170 ? 0.2325 0.2411 0.2123 0.0114 0.0275 0.0217 170 VAL A CG1 1320 C CG2 . VAL A 170 ? 0.2378 0.2459 0.2293 0.0145 0.0154 0.0184 170 VAL A CG2 1321 N N . GLN A 171 ? 0.2781 0.2375 0.2533 0.0070 0.0265 0.0300 171 GLN A N 1322 C CA . GLN A 171 ? 0.2877 0.2462 0.2661 0.0049 0.0219 0.0266 171 GLN A CA 1323 C C . GLN A 171 ? 0.2874 0.2408 0.2593 0.0053 0.0230 0.0264 171 GLN A C 1324 O O . GLN A 171 ? 0.2916 0.2419 0.2664 0.0085 0.0340 0.0285 171 GLN A O 1325 C CB . GLN A 171 ? 0.2896 0.2476 0.2558 0.0049 0.0143 0.0320 171 GLN A CB 1326 C CG . GLN A 171 ? 0.3069 0.2626 0.2788 0.0096 0.0162 0.0322 171 GLN A CG 1327 C CD . GLN A 171 ? 0.3212 0.2640 0.2842 0.0155 0.0128 0.0290 171 GLN A CD 1328 O OE1 . GLN A 171 ? 0.3929 0.2946 0.3399 0.0097 0.0233 0.0218 171 GLN A OE1 1329 N NE2 . GLN A 171 ? 0.3249 0.2405 0.2792 0.0227 0.0256 0.0256 171 GLN A NE2 1330 N N . SER A 172 ? 0.2888 0.2488 0.2635 0.0045 0.0287 0.0237 172 SER A N 1331 C CA . SER A 172 ? 0.2826 0.2633 0.2662 0.0032 0.0313 0.0208 172 SER A CA 1332 C C . SER A 172 ? 0.2819 0.2621 0.2591 0.0059 0.0257 0.0165 172 SER A C 1333 O O . SER A 172 ? 0.3026 0.2621 0.2798 -0.0010 0.0224 0.0193 172 SER A O 1334 C CB . SER A 172 ? 0.2989 0.2807 0.2705 0.0005 0.0370 0.0176 172 SER A CB 1335 O OG . SER A 172 ? 0.3152 0.3088 0.2924 -0.0033 0.0347 0.0191 172 SER A OG 1336 N N . MET A 173 ? 0.2679 0.2634 0.2534 0.0048 0.0294 0.0134 173 MET A N 1337 C CA . MET A 173 ? 0.2714 0.2650 0.2529 0.0057 0.0251 0.0132 173 MET A CA 1338 C C . MET A 173 ? 0.2745 0.2606 0.2543 0.0094 0.0261 0.0125 173 MET A C 1339 O O . MET A 173 ? 0.2740 0.2736 0.2292 0.0054 0.0317 0.0145 173 MET A O 1340 C CB . MET A 173 ? 0.2851 0.2841 0.2711 0.0053 0.0202 0.0064 173 MET A CB 1341 C CG . MET A 173 ? 0.3232 0.3280 0.2863 0.0025 0.0264 0.0181 173 MET A CG 1342 S SD . MET A 173 ? 0.3395 0.4183 0.3273 0.0143 0.0567 0.0491 173 MET A SD 1343 C CE . MET A 173 ? 0.3098 0.3640 0.3179 0.0060 0.0358 0.0034 173 MET A CE 1344 N N . THR A 174 ? 0.2612 0.2602 0.2492 0.0081 0.0248 0.0155 174 THR A N 1345 C CA . THR A 174 ? 0.2581 0.2505 0.2505 0.0075 0.0258 0.0122 174 THR A CA 1346 C C . THR A 174 ? 0.2568 0.2475 0.2517 0.0079 0.0229 0.0142 174 THR A C 1347 O O . THR A 174 ? 0.2588 0.2429 0.2444 0.0187 0.0280 0.0131 174 THR A O 1348 C CB . THR A 174 ? 0.2659 0.2472 0.2543 0.0032 0.0216 0.0141 174 THR A CB 1349 O OG1 . THR A 174 ? 0.3043 0.2319 0.2664 0.0195 0.0393 0.0220 174 THR A OG1 1350 C CG2 . THR A 174 ? 0.2619 0.2564 0.2606 0.0036 0.0219 0.0167 174 THR A CG2 1351 N N . GLU A 175 ? 0.2549 0.2503 0.2563 0.0013 0.0213 0.0144 175 GLU A N 1352 C CA . GLU A 175 ? 0.2526 0.2517 0.2590 0.0015 0.0237 0.0181 175 GLU A CA 1353 C C . GLU A 175 ? 0.2416 0.2360 0.2428 0.0002 0.0251 0.0131 175 GLU A C 1354 O O . GLU A 175 ? 0.2515 0.2454 0.2477 -0.0070 0.0238 0.0220 175 GLU A O 1355 C CB . GLU A 175 ? 0.2599 0.2557 0.2644 -0.0027 0.0234 0.0160 175 GLU A CB 1356 C CG . GLU A 175 ? 0.3116 0.2818 0.3121 -0.0130 0.0176 0.0174 175 GLU A CG 1357 C CD . GLU A 175 ? 0.3195 0.2969 0.3435 -0.0003 0.0089 0.0000 175 GLU A CD 1358 O OE1 . GLU A 175 ? 0.3663 0.2818 0.3890 -0.0058 0.0287 0.0036 175 GLU A OE1 1359 O OE2 . GLU A 175 ? 0.3734 0.3514 0.3636 -0.0081 0.0093 0.0093 175 GLU A OE2 1360 N N . LEU A 176 ? 0.2319 0.2173 0.2319 0.0021 0.0274 0.0195 176 LEU A N 1361 C CA . LEU A 176 ? 0.2316 0.2080 0.2122 0.0010 0.0209 0.0113 176 LEU A CA 1362 C C . LEU A 176 ? 0.2269 0.2165 0.2154 -0.0007 0.0205 0.0082 176 LEU A C 1363 O O . LEU A 176 ? 0.2402 0.2203 0.2086 0.0054 0.0145 -0.0004 176 LEU A O 1364 C CB . LEU A 176 ? 0.2252 0.1862 0.2056 -0.0010 0.0231 0.0204 176 LEU A CB 1365 C CG . LEU A 176 ? 0.2168 0.1929 0.2270 0.0095 0.0056 0.0242 176 LEU A CG 1366 C CD1 . LEU A 176 ? 0.2141 0.2443 0.2422 0.0189 0.0147 0.0175 176 LEU A CD1 1367 C CD2 . LEU A 176 ? 0.2263 0.2389 0.2307 -0.0028 0.0056 0.0073 176 LEU A CD2 1368 N N . ILE A 177 ? 0.2225 0.2013 0.2118 0.0009 0.0257 -0.0018 177 ILE A N 1369 C CA . ILE A 177 ? 0.2209 0.2143 0.2194 -0.0010 0.0220 -0.0032 177 ILE A CA 1370 C C . ILE A 177 ? 0.2302 0.2221 0.2267 -0.0066 0.0213 0.0007 177 ILE A C 1371 O O . ILE A 177 ? 0.2276 0.2135 0.2376 -0.0153 0.0256 0.0064 177 ILE A O 1372 C CB . ILE A 177 ? 0.2168 0.2024 0.2088 -0.0058 0.0144 -0.0142 177 ILE A CB 1373 C CG1 . ILE A 177 ? 0.2287 0.2333 0.2337 -0.0042 0.0035 -0.0106 177 ILE A CG1 1374 C CG2 . ILE A 177 ? 0.2218 0.2133 0.2276 0.0097 0.0380 -0.0008 177 ILE A CG2 1375 C CD1 . ILE A 177 ? 0.2316 0.2434 0.2292 0.0103 0.0141 -0.0052 177 ILE A CD1 1376 N N . PRO A 178 ? 0.2360 0.2321 0.2372 -0.0155 0.0238 0.0034 178 PRO A N 1377 C CA . PRO A 178 ? 0.2396 0.2352 0.2400 -0.0173 0.0287 0.0032 178 PRO A CA 1378 C C . PRO A 178 ? 0.2365 0.2368 0.2401 -0.0189 0.0288 -0.0012 178 PRO A C 1379 O O . PRO A 178 ? 0.2384 0.2401 0.2426 -0.0101 0.0382 -0.0018 178 PRO A O 1380 C CB . PRO A 178 ? 0.2579 0.2376 0.2560 -0.0221 0.0255 0.0047 178 PRO A CB 1381 C CG . PRO A 178 ? 0.2370 0.2442 0.2397 -0.0164 0.0199 0.0025 178 PRO A CG 1382 C CD . PRO A 178 ? 0.2381 0.2415 0.2431 -0.0108 0.0215 0.0061 178 PRO A CD 1383 N N . GLY A 179 ? 0.2260 0.2328 0.2344 -0.0175 0.0367 -0.0028 179 GLY A N 1384 C CA . GLY A 179 ? 0.2273 0.2322 0.2233 -0.0118 0.0302 0.0029 179 GLY A CA 1385 C C . GLY A 179 ? 0.2258 0.2289 0.2158 -0.0128 0.0245 -0.0024 179 GLY A C 1386 O O . GLY A 179 ? 0.2229 0.2422 0.2170 -0.0124 0.0210 0.0014 179 GLY A O 1387 N N . LEU A 180 ? 0.2074 0.2244 0.2044 -0.0031 0.0285 -0.0056 180 LEU A N 1388 C CA . LEU A 180 ? 0.2031 0.2045 0.1954 -0.0109 0.0228 -0.0101 180 LEU A CA 1389 C C . LEU A 180 ? 0.2071 0.2192 0.1983 -0.0077 0.0191 -0.0114 180 LEU A C 1390 O O . LEU A 180 ? 0.2132 0.2219 0.1968 0.0041 0.0155 -0.0205 180 LEU A O 1391 C CB . LEU A 180 ? 0.2019 0.2084 0.1895 -0.0089 0.0168 -0.0105 180 LEU A CB 1392 C CG . LEU A 180 ? 0.1929 0.1982 0.1931 -0.0124 0.0160 -0.0178 180 LEU A CG 1393 C CD1 . LEU A 180 ? 0.2235 0.2413 0.2004 0.0110 -0.0117 -0.0009 180 LEU A CD1 1394 C CD2 . LEU A 180 ? 0.2167 0.2247 0.1894 -0.0009 0.0100 0.0131 180 LEU A CD2 1395 N N . GLN A 181 ? 0.2087 0.2147 0.2016 -0.0067 0.0181 -0.0103 181 GLN A N 1396 C CA . GLN A 181 ? 0.2171 0.2317 0.2174 -0.0058 0.0138 -0.0145 181 GLN A CA 1397 C C . GLN A 181 ? 0.2367 0.2514 0.2311 -0.0133 0.0163 -0.0152 181 GLN A C 1398 O O . GLN A 181 ? 0.2356 0.2680 0.2416 -0.0160 0.0197 -0.0281 181 GLN A O 1399 C CB . GLN A 181 ? 0.2192 0.2264 0.2096 -0.0089 0.0100 -0.0121 181 GLN A CB 1400 C CG . GLN A 181 ? 0.2087 0.2270 0.2224 -0.0065 -0.0011 -0.0069 181 GLN A CG 1401 C CD . GLN A 181 ? 0.2202 0.2281 0.2375 -0.0073 0.0083 -0.0107 181 GLN A CD 1402 O OE1 . GLN A 181 ? 0.2466 0.2231 0.2610 0.0044 0.0214 -0.0035 181 GLN A OE1 1403 N NE2 . GLN A 181 ? 0.1670 0.1728 0.1712 -0.0082 0.0338 -0.0018 181 GLN A NE2 1404 N N . GLY A 182 ? 0.2348 0.2602 0.2491 -0.0195 0.0183 -0.0206 182 GLY A N 1405 C CA . GLY A 182 ? 0.2567 0.2725 0.2731 -0.0228 0.0208 -0.0147 182 GLY A CA 1406 C C . GLY A 182 ? 0.2622 0.2800 0.2895 -0.0156 0.0195 -0.0134 182 GLY A C 1407 O O . GLY A 182 ? 0.2657 0.2745 0.2936 -0.0252 0.0197 -0.0160 182 GLY A O 1408 N N . ASP A 183 ? 0.2871 0.2940 0.3162 -0.0233 0.0204 -0.0138 183 ASP A N 1409 C CA . ASP A 183 ? 0.3056 0.3179 0.3411 -0.0129 0.0195 -0.0065 183 ASP A CA 1410 C C . ASP A 183 ? 0.3154 0.3228 0.3541 -0.0163 0.0182 -0.0087 183 ASP A C 1411 O O . ASP A 183 ? 0.3175 0.3305 0.3560 -0.0062 0.0223 -0.0106 183 ASP A O 1412 C CB . ASP A 183 ? 0.3182 0.3274 0.3639 -0.0185 0.0212 -0.0067 183 ASP A CB 1413 C CG . ASP A 183 ? 0.3528 0.3651 0.3773 -0.0110 0.0257 -0.0015 183 ASP A CG 1414 O OD1 . ASP A 183 ? 0.3757 0.4011 0.4124 -0.0233 0.0257 -0.0175 183 ASP A OD1 1415 O OD2 . ASP A 183 ? 0.3984 0.4252 0.4486 0.0051 0.0087 0.0003 183 ASP A OD2 1416 N N . VAL A 184 ? 0.3420 0.3424 0.3713 -0.0168 0.0143 -0.0016 184 VAL A N 1417 C CA . VAL A 184 ? 0.3765 0.3661 0.3982 -0.0099 0.0073 -0.0047 184 VAL A CA 1418 C C . VAL A 184 ? 0.4089 0.3969 0.4300 -0.0117 0.0037 -0.0061 184 VAL A C 1419 O O . VAL A 184 ? 0.4150 0.3854 0.4368 -0.0183 0.0054 -0.0042 184 VAL A O 1420 C CB . VAL A 184 ? 0.3721 0.3640 0.3906 -0.0147 0.0064 -0.0033 184 VAL A CB 1421 C CG1 . VAL A 184 ? 0.3649 0.3674 0.3885 -0.0143 0.0035 -0.0050 184 VAL A CG1 1422 C CG2 . VAL A 184 ? 0.3767 0.3721 0.3872 -0.0109 0.0036 0.0017 184 VAL A CG2 1423 N N . PRO A 185 ? 0.4437 0.4291 0.4580 -0.0077 0.0033 -0.0073 185 PRO A N 1424 C CA . PRO A 185 ? 0.4709 0.4515 0.4816 -0.0080 0.0011 -0.0093 185 PRO A CA 1425 C C . PRO A 185 ? 0.4906 0.4697 0.5032 -0.0075 -0.0007 -0.0036 185 PRO A C 1426 O O . PRO A 185 ? 0.4879 0.4633 0.5090 -0.0110 -0.0028 -0.0088 185 PRO A O 1427 C CB . PRO A 185 ? 0.4759 0.4589 0.4809 -0.0067 0.0027 -0.0072 185 PRO A CB 1428 C CG . PRO A 185 ? 0.4721 0.4519 0.4710 -0.0076 0.0000 -0.0096 185 PRO A CG 1429 C CD . PRO A 185 ? 0.4504 0.4343 0.4584 -0.0047 0.0032 -0.0074 185 PRO A CD 1430 N N . LYS A 186 ? 0.5122 0.4981 0.5331 -0.0097 -0.0033 -0.0044 186 LYS A N 1431 C CA . LYS A 186 ? 0.5370 0.5198 0.5521 -0.0080 -0.0027 0.0015 186 LYS A CA 1432 C C . LYS A 186 ? 0.5357 0.5214 0.5543 -0.0071 -0.0031 -0.0022 186 LYS A C 1433 O O . LYS A 186 ? 0.5471 0.5250 0.5646 -0.0096 -0.0050 0.0001 186 LYS A O 1434 C CB . LYS A 186 ? 0.5398 0.5262 0.5525 -0.0081 -0.0004 -0.0044 186 LYS A CB 1435 C CG . LYS A 186 ? 0.5545 0.5567 0.5694 -0.0028 0.0091 0.0003 186 LYS A CG 1436 C CD . LYS A 186 ? 0.6347 0.7278 0.7396 -0.0333 -0.0545 0.0996 186 LYS A CD 1437 C CE . LYS A 186 ? 0.5202 0.5153 0.5095 -0.0320 0.1397 -0.0298 186 LYS A CE 1438 N NZ . LYS A 186 ? 0.7785 0.7038 0.7577 0.0785 -0.0876 -0.0347 186 LYS A NZ 1439 N N . ASP A 187 ? 0.5339 0.5231 0.5595 -0.0045 -0.0006 -0.0045 187 ASP A N 1440 C CA . ASP A 187 ? 0.5374 0.5285 0.5631 -0.0016 -0.0036 -0.0044 187 ASP A CA 1441 C C . ASP A 187 ? 0.5184 0.5042 0.5481 0.0000 -0.0024 -0.0063 187 ASP A C 1442 O O . ASP A 187 ? 0.5284 0.5097 0.5581 0.0017 -0.0069 -0.0053 187 ASP A O 1443 C CB . ASP A 187 ? 0.5494 0.5446 0.5678 -0.0020 -0.0007 -0.0009 187 ASP A CB 1444 C CG . ASP A 187 ? 0.5842 0.5753 0.6090 0.0029 -0.0041 0.0056 187 ASP A CG 1445 O OD1 . ASP A 187 ? 0.6091 0.6090 0.6407 -0.0042 0.0057 0.0065 187 ASP A OD1 1446 O OD2 . ASP A 187 ? 0.6087 0.6156 0.6529 -0.0025 -0.0040 0.0015 187 ASP A OD2 1447 N N . PHE A 188 ? 0.4906 0.4790 0.5249 -0.0025 -0.0015 -0.0047 188 PHE A N 1448 C CA . PHE A 188 ? 0.4607 0.4455 0.4865 -0.0006 0.0019 -0.0030 188 PHE A CA 1449 C C . PHE A 188 ? 0.4440 0.4261 0.4672 -0.0012 0.0070 -0.0011 188 PHE A C 1450 O O . PHE A 188 ? 0.4394 0.4322 0.4679 -0.0020 0.0085 0.0029 188 PHE A O 1451 C CB . PHE A 188 ? 0.4583 0.4411 0.4857 -0.0014 0.0022 -0.0025 188 PHE A CB 1452 C CG . PHE A 188 ? 0.4534 0.4320 0.4734 0.0013 0.0020 -0.0004 188 PHE A CG 1453 C CD1 . PHE A 188 ? 0.4488 0.4342 0.4717 -0.0012 0.0031 0.0008 188 PHE A CD1 1454 C CD2 . PHE A 188 ? 0.4425 0.4238 0.4760 0.0019 -0.0006 0.0031 188 PHE A CD2 1455 C CE1 . PHE A 188 ? 0.4354 0.4269 0.4633 0.0082 0.0032 0.0069 188 PHE A CE1 1456 C CE2 . PHE A 188 ? 0.4334 0.4189 0.4657 0.0048 0.0091 -0.0030 188 PHE A CE2 1457 C CZ . PHE A 188 ? 0.4410 0.4197 0.4603 0.0067 0.0007 -0.0026 188 PHE A CZ 1458 N N . THR A 189 ? 0.4137 0.3929 0.4323 0.0007 0.0108 -0.0040 189 THR A N 1459 C CA . THR A 189 ? 0.4005 0.3680 0.4092 -0.0010 0.0147 -0.0067 189 THR A CA 1460 C C . THR A 189 ? 0.3773 0.3548 0.3864 0.0010 0.0137 -0.0025 189 THR A C 1461 O O . THR A 189 ? 0.3668 0.3276 0.3764 0.0035 0.0231 -0.0047 189 THR A O 1462 C CB . THR A 189 ? 0.4028 0.3786 0.4098 -0.0008 0.0111 -0.0070 189 THR A CB 1463 O OG1 . THR A 189 ? 0.4299 0.3761 0.4347 0.0025 0.0171 -0.0082 189 THR A OG1 1464 C CG2 . THR A 189 ? 0.3968 0.3829 0.4108 0.0033 0.0147 -0.0119 189 THR A CG2 1465 N N . SER A 190 ? 0.3548 0.3298 0.3653 -0.0012 0.0189 0.0010 190 SER A N 1466 C CA . SER A 190 ? 0.3356 0.3223 0.3472 -0.0021 0.0192 0.0063 190 SER A CA 1467 C C . SER A 190 ? 0.3283 0.3142 0.3472 -0.0008 0.0211 0.0076 190 SER A C 1468 O O . SER A 190 ? 0.3222 0.3063 0.3512 -0.0015 0.0248 0.0123 190 SER A O 1469 C CB . SER A 190 ? 0.3444 0.3279 0.3453 -0.0049 0.0177 0.0065 190 SER A CB 1470 O OG . SER A 190 ? 0.3369 0.2854 0.3144 -0.0026 0.0342 0.0230 190 SER A OG 1471 N N . GLY A 191 ? 0.3075 0.3015 0.3329 -0.0016 0.0220 0.0038 191 GLY A N 1472 C CA . GLY A 191 ? 0.3041 0.2898 0.3212 0.0055 0.0237 0.0046 191 GLY A CA 1473 C C . GLY A 191 ? 0.2957 0.2830 0.3151 0.0114 0.0210 0.0010 191 GLY A C 1474 O O . GLY A 191 ? 0.2710 0.2845 0.3047 0.0142 0.0354 0.0021 191 GLY A O 1475 N N . MET A 192 ? 0.2961 0.2857 0.3040 0.0140 0.0233 -0.0001 192 MET A N 1476 C CA . MET A 192 ? 0.3008 0.2769 0.3028 0.0145 0.0252 0.0028 192 MET A CA 1477 C C . MET A 192 ? 0.2902 0.2731 0.2920 0.0131 0.0274 0.0079 192 MET A C 1478 O O . MET A 192 ? 0.3056 0.2645 0.2873 0.0199 0.0424 0.0104 192 MET A O 1479 C CB . MET A 192 ? 0.3032 0.2914 0.3136 0.0122 0.0217 -0.0015 192 MET A CB 1480 C CG . MET A 192 ? 0.3291 0.2969 0.3412 0.0191 0.0179 -0.0073 192 MET A CG 1481 S SD . MET A 192 ? 0.3985 0.3682 0.3873 0.0270 0.0419 -0.0317 192 MET A SD 1482 C CE . MET A 192 ? 0.3533 0.3613 0.3743 0.0046 0.0224 -0.0107 192 MET A CE 1483 N N . PRO A 193 ? 0.2771 0.2725 0.2829 0.0103 0.0352 0.0058 193 PRO A N 1484 C CA . PRO A 193 ? 0.2672 0.2659 0.2686 0.0047 0.0271 0.0041 193 PRO A CA 1485 C C . PRO A 193 ? 0.2650 0.2673 0.2737 0.0045 0.0220 0.0007 193 PRO A C 1486 O O . PRO A 193 ? 0.2724 0.2862 0.2736 0.0094 0.0202 -0.0066 193 PRO A O 1487 C CB . PRO A 193 ? 0.2668 0.2578 0.2658 0.0044 0.0290 0.0032 193 PRO A CB 1488 C CG . PRO A 193 ? 0.2581 0.2533 0.2578 0.0023 0.0367 0.0041 193 PRO A CG 1489 C CD . PRO A 193 ? 0.2785 0.2794 0.2800 0.0102 0.0304 0.0049 193 PRO A CD 1490 N N . PHE A 194 ? 0.2633 0.2642 0.2696 0.0023 0.0200 0.0000 194 PHE A N 1491 C CA . PHE A 194 ? 0.2637 0.2624 0.2720 -0.0019 0.0143 0.0001 194 PHE A CA 1492 C C . PHE A 194 ? 0.2528 0.2560 0.2674 -0.0045 0.0119 -0.0006 194 PHE A C 1493 O O . PHE A 194 ? 0.2396 0.2553 0.2591 -0.0048 0.0208 0.0000 194 PHE A O 1494 C CB . PHE A 194 ? 0.2695 0.2731 0.2824 -0.0017 0.0144 0.0007 194 PHE A CB 1495 C CG . PHE A 194 ? 0.2775 0.2864 0.2937 -0.0104 0.0073 -0.0018 194 PHE A CG 1496 C CD1 . PHE A 194 ? 0.2957 0.3078 0.3094 -0.0099 0.0097 -0.0099 194 PHE A CD1 1497 C CD2 . PHE A 194 ? 0.2802 0.3023 0.2981 -0.0036 0.0080 -0.0091 194 PHE A CD2 1498 C CE1 . PHE A 194 ? 0.2964 0.3303 0.3248 -0.0044 0.0039 -0.0065 194 PHE A CE1 1499 C CE2 . PHE A 194 ? 0.2884 0.3005 0.2953 -0.0255 0.0092 0.0006 194 PHE A CE2 1500 C CZ . PHE A 194 ? 0.2980 0.3026 0.3072 -0.0061 0.0038 -0.0062 194 PHE A CZ 1501 N N . VAL A 195 ? 0.2481 0.2488 0.2479 -0.0110 0.0174 -0.0067 195 VAL A N 1502 C CA . VAL A 195 ? 0.2436 0.2600 0.2440 -0.0127 0.0086 -0.0085 195 VAL A CA 1503 C C . VAL A 195 ? 0.2539 0.2680 0.2489 -0.0132 0.0089 -0.0152 195 VAL A C 1504 O O . VAL A 195 ? 0.2408 0.2791 0.2534 -0.0144 0.0183 -0.0340 195 VAL A O 1505 C CB . VAL A 195 ? 0.2508 0.2455 0.2357 -0.0097 0.0026 -0.0051 195 VAL A CB 1506 C CG1 . VAL A 195 ? 0.2508 0.2683 0.2646 -0.0002 0.0107 0.0031 195 VAL A CG1 1507 C CG2 . VAL A 195 ? 0.2437 0.2594 0.2267 -0.0083 0.0085 -0.0126 195 VAL A CG2 1508 N N . ALA A 196 ? 0.2503 0.2738 0.2457 -0.0125 0.0108 -0.0212 196 ALA A N 1509 C CA . ALA A 196 ? 0.2651 0.2889 0.2678 -0.0129 0.0048 -0.0196 196 ALA A CA 1510 C C . ALA A 196 ? 0.2874 0.3027 0.2846 -0.0139 0.0000 -0.0187 196 ALA A C 1511 O O . ALA A 196 ? 0.3261 0.3232 0.2998 -0.0210 -0.0019 -0.0278 196 ALA A O 1512 C CB . ALA A 196 ? 0.2608 0.2929 0.2742 -0.0134 0.0041 -0.0210 196 ALA A CB 1513 N N . GLY A 197 ? 0.2873 0.2959 0.2825 -0.0115 0.0003 -0.0075 197 GLY A N 1514 C CA . GLY A 197 ? 0.2843 0.3025 0.2709 -0.0104 -0.0029 -0.0146 197 GLY A CA 1515 C C . GLY A 197 ? 0.2819 0.3047 0.2711 -0.0052 -0.0016 -0.0069 197 GLY A C 1516 O O . GLY A 197 ? 0.2755 0.3103 0.2609 -0.0043 0.0012 -0.0181 197 GLY A O 1517 N N . LYS A 198 ? 0.2807 0.3097 0.2630 -0.0068 -0.0019 -0.0083 198 LYS A N 1518 C CA . LYS A 198 ? 0.2833 0.3127 0.2632 -0.0011 -0.0052 -0.0028 198 LYS A CA 1519 C C . LYS A 198 ? 0.2803 0.3133 0.2586 -0.0034 -0.0049 -0.0025 198 LYS A C 1520 O O . LYS A 198 ? 0.2843 0.3237 0.2615 -0.0089 -0.0075 0.0000 198 LYS A O 1521 C CB . LYS A 198 ? 0.2787 0.3218 0.2539 -0.0048 -0.0083 -0.0056 198 LYS A CB 1522 C CG . LYS A 198 ? 0.2836 0.3348 0.2731 0.0016 -0.0095 -0.0005 198 LYS A CG 1523 C CD . LYS A 198 ? 0.3140 0.3394 0.2838 -0.0018 -0.0099 -0.0022 198 LYS A CD 1524 C CE . LYS A 198 ? 0.3523 0.4159 0.3516 -0.0012 -0.0149 -0.0092 198 LYS A CE 1525 N NZ . LYS A 198 ? 0.4276 0.4621 0.3817 0.0038 -0.0163 0.0000 198 LYS A NZ 1526 N N . ASN A 199 ? 0.2548 0.3101 0.2667 -0.0077 -0.0098 -0.0107 199 ASN A N 1527 C CA . ASN A 199 ? 0.2574 0.3153 0.2668 -0.0074 -0.0033 -0.0085 199 ASN A CA 1528 C C . ASN A 199 ? 0.2487 0.3012 0.2633 -0.0096 -0.0005 -0.0062 199 ASN A C 1529 O O . ASN A 199 ? 0.2581 0.3067 0.2523 -0.0064 0.0004 -0.0073 199 ASN A O 1530 C CB . ASN A 199 ? 0.2660 0.3283 0.2846 -0.0055 -0.0034 -0.0125 199 ASN A CB 1531 C CG . ASN A 199 ? 0.3156 0.3674 0.3266 -0.0069 -0.0074 -0.0064 199 ASN A CG 1532 O OD1 . ASN A 199 ? 0.4051 0.4505 0.4088 -0.0125 -0.0242 -0.0291 199 ASN A OD1 1533 N ND2 . ASN A 199 ? 0.3252 0.3793 0.3163 0.0177 -0.0161 0.0111 199 ASN A ND2 1534 N N . LYS A 200 ? 0.2346 0.2831 0.2430 -0.0113 0.0040 -0.0058 200 LYS A N 1535 C CA . LYS A 200 ? 0.2121 0.2701 0.2437 -0.0130 0.0078 0.0001 200 LYS A CA 1536 C C . LYS A 200 ? 0.2084 0.2583 0.2305 -0.0148 0.0059 -0.0016 200 LYS A C 1537 O O . LYS A 200 ? 0.1930 0.2637 0.2298 -0.0193 0.0106 0.0000 200 LYS A O 1538 C CB . LYS A 200 ? 0.2255 0.2723 0.2491 -0.0220 0.0084 -0.0056 200 LYS A CB 1539 C CG . LYS A 200 ? 0.2148 0.2721 0.2684 -0.0188 0.0337 -0.0097 200 LYS A CG 1540 C CD . LYS A 200 ? 0.2658 0.2710 0.2776 -0.0190 0.0277 -0.0061 200 LYS A CD 1541 C CE . LYS A 200 ? 0.2525 0.2989 0.3016 -0.0067 0.0315 -0.0049 200 LYS A CE 1542 N NZ . LYS A 200 ? 0.2536 0.2535 0.2607 -0.0089 0.0314 -0.0160 200 LYS A NZ 1543 N N . VAL A 201 ? 0.1968 0.2432 0.2197 -0.0075 0.0126 0.0037 201 VAL A N 1544 C CA . VAL A 201 ? 0.1951 0.2314 0.2076 -0.0037 0.0104 0.0033 201 VAL A CA 1545 C C . VAL A 201 ? 0.1950 0.2316 0.2128 -0.0035 0.0127 0.0054 201 VAL A C 1546 O O . VAL A 201 ? 0.2024 0.2302 0.2283 -0.0085 0.0195 0.0056 201 VAL A O 1547 C CB . VAL A 201 ? 0.1951 0.2266 0.1975 0.0003 0.0084 0.0079 201 VAL A CB 1548 C CG1 . VAL A 201 ? 0.1967 0.2314 0.2018 0.0048 0.0080 0.0120 201 VAL A CG1 1549 C CG2 . VAL A 201 ? 0.2037 0.2535 0.1958 -0.0013 0.0183 0.0040 201 VAL A CG2 1550 N N . ALA A 202 ? 0.1913 0.2306 0.2115 -0.0092 0.0156 0.0015 202 ALA A N 1551 C CA . ALA A 202 ? 0.1859 0.2311 0.2022 -0.0020 0.0193 0.0012 202 ALA A CA 1552 C C . ALA A 202 ? 0.1971 0.2262 0.2076 -0.0045 0.0197 0.0010 202 ALA A C 1553 O O . ALA A 202 ? 0.2171 0.2210 0.2064 -0.0047 0.0241 0.0042 202 ALA A O 1554 C CB . ALA A 202 ? 0.1768 0.2388 0.2049 -0.0057 0.0238 -0.0054 202 ALA A CB 1555 N N . ALA A 203 ? 0.1947 0.2248 0.1968 -0.0019 0.0176 0.0065 203 ALA A N 1556 C CA . ALA A 203 ? 0.1862 0.2282 0.2011 -0.0047 0.0132 0.0088 203 ALA A CA 1557 C C . ALA A 203 ? 0.2053 0.2395 0.2095 -0.0031 0.0071 0.0057 203 ALA A C 1558 O O . ALA A 203 ? 0.2154 0.2615 0.2088 -0.0057 0.0142 0.0041 203 ALA A O 1559 C CB . ALA A 203 ? 0.1932 0.2215 0.1938 -0.0145 0.0152 0.0146 203 ALA A CB 1560 N N . CYS A 204 ? 0.2091 0.2381 0.2050 -0.0058 0.0106 0.0128 204 CYS A N 1561 C CA . CYS A 204 ? 0.2128 0.2404 0.2003 -0.0016 0.0071 0.0145 204 CYS A CA 1562 C C . CYS A 204 ? 0.2306 0.2390 0.2066 0.0040 0.0036 0.0114 204 CYS A C 1563 O O . CYS A 204 ? 0.2325 0.2475 0.2035 0.0144 0.0040 0.0087 204 CYS A O 1564 C CB . CYS A 204 ? 0.2154 0.2292 0.2072 -0.0016 0.0058 0.0071 204 CYS A CB 1565 S SG . CYS A 204 ? 0.2043 0.2660 0.2253 -0.0024 0.0140 0.0119 204 CYS A SG 1566 N N . ALA A 205 ? 0.2245 0.2353 0.1931 0.0056 0.0017 0.0234 205 ALA A N 1567 C CA . ALA A 205 ? 0.2306 0.2277 0.1965 0.0101 0.0042 0.0192 205 ALA A CA 1568 C C . ALA A 205 ? 0.2351 0.2364 0.1980 0.0118 0.0045 0.0159 205 ALA A C 1569 O O . ALA A 205 ? 0.2400 0.2569 0.1899 0.0198 0.0105 0.0062 205 ALA A O 1570 C CB . ALA A 205 ? 0.2204 0.2159 0.1986 0.0067 0.0130 0.0283 205 ALA A CB 1571 N N . LYS A 206 ? 0.2285 0.2269 0.1987 0.0180 0.0089 0.0164 206 LYS A N 1572 C CA . LYS A 206 ? 0.2295 0.2279 0.2110 0.0129 0.0063 0.0178 206 LYS A CA 1573 C C . LYS A 206 ? 0.2280 0.2440 0.2217 0.0080 0.0100 0.0170 206 LYS A C 1574 O O . LYS A 206 ? 0.2304 0.2645 0.2315 0.0064 0.0146 0.0189 206 LYS A O 1575 C CB . LYS A 206 ? 0.2242 0.2219 0.2210 0.0094 0.0125 0.0233 206 LYS A CB 1576 C CG . LYS A 206 ? 0.2401 0.2234 0.2345 0.0229 -0.0005 0.0244 206 LYS A CG 1577 C CD . LYS A 206 ? 0.2370 0.2327 0.2167 0.0228 0.0067 0.0194 206 LYS A CD 1578 C CE . LYS A 206 ? 0.2567 0.2468 0.2002 0.0238 -0.0010 0.0125 206 LYS A CE 1579 N NZ . LYS A 206 ? 0.2622 0.2431 0.2200 0.0204 -0.0237 0.0111 206 LYS A NZ 1580 N N . HIS A 207 ? 0.2214 0.2518 0.2236 0.0125 0.0034 0.0253 207 HIS A N 1581 C CA . HIS A 207 ? 0.2309 0.2487 0.2323 0.0187 0.0083 0.0191 207 HIS A CA 1582 C C . HIS A 207 ? 0.2413 0.2605 0.2312 0.0186 0.0071 0.0191 207 HIS A C 1583 O O . HIS A 207 ? 0.2436 0.2765 0.2121 0.0227 0.0012 0.0169 207 HIS A O 1584 C CB . HIS A 207 ? 0.2369 0.2559 0.2366 0.0149 0.0018 0.0146 207 HIS A CB 1585 C CG . HIS A 207 ? 0.2560 0.2473 0.2407 0.0138 0.0016 0.0113 207 HIS A CG 1586 N ND1 . HIS A 207 ? 0.2758 0.2608 0.2611 0.0260 0.0011 0.0099 207 HIS A ND1 1587 C CD2 . HIS A 207 ? 0.2833 0.2691 0.2670 0.0024 -0.0134 0.0062 207 HIS A CD2 1588 C CE1 . HIS A 207 ? 0.2850 0.2582 0.2768 0.0059 0.0011 0.0081 207 HIS A CE1 1589 N NE2 . HIS A 207 ? 0.2918 0.2485 0.2487 0.0102 -0.0136 0.0062 207 HIS A NE2 1590 N N . PHE A 208 ? 0.2472 0.2501 0.2372 0.0227 0.0059 0.0197 208 PHE A N 1591 C CA . PHE A 208 ? 0.2513 0.2508 0.2363 0.0233 0.0059 0.0185 208 PHE A CA 1592 C C . PHE A 208 ? 0.2630 0.2646 0.2493 0.0154 0.0028 0.0185 208 PHE A C 1593 O O . PHE A 208 ? 0.2543 0.2603 0.2392 0.0242 0.0074 0.0341 208 PHE A O 1594 C CB . PHE A 208 ? 0.2541 0.2432 0.2413 0.0150 0.0067 0.0110 208 PHE A CB 1595 C CG . PHE A 208 ? 0.2492 0.2615 0.2405 0.0231 -0.0019 0.0067 208 PHE A CG 1596 C CD1 . PHE A 208 ? 0.2713 0.2474 0.2391 0.0235 0.0050 0.0094 208 PHE A CD1 1597 C CD2 . PHE A 208 ? 0.2621 0.2748 0.2736 0.0307 0.0056 0.0034 208 PHE A CD2 1598 C CE1 . PHE A 208 ? 0.2684 0.2650 0.2669 0.0189 0.0068 0.0168 208 PHE A CE1 1599 C CE2 . PHE A 208 ? 0.2796 0.2595 0.2815 0.0089 0.0131 0.0109 208 PHE A CE2 1600 C CZ . PHE A 208 ? 0.2573 0.2623 0.2609 0.0128 0.0032 0.0181 208 PHE A CZ 1601 N N . VAL A 209 ? 0.2703 0.2771 0.2461 0.0139 0.0103 0.0262 209 VAL A N 1602 C CA . VAL A 209 ? 0.2689 0.2885 0.2576 0.0131 0.0093 0.0205 209 VAL A CA 1603 C C . VAL A 209 ? 0.2759 0.2958 0.2523 0.0115 0.0070 0.0237 209 VAL A C 1604 O O . VAL A 209 ? 0.2771 0.3146 0.2413 0.0159 0.0169 0.0217 209 VAL A O 1605 C CB . VAL A 209 ? 0.2650 0.2909 0.2637 0.0095 0.0087 0.0223 209 VAL A CB 1606 C CG1 . VAL A 209 ? 0.2708 0.2908 0.2763 0.0206 -0.0005 0.0161 209 VAL A CG1 1607 C CG2 . VAL A 209 ? 0.2675 0.2927 0.2675 0.0091 0.0175 0.0255 209 VAL A CG2 1608 N N . GLY A 210 ? 0.2719 0.3028 0.2472 0.0220 0.0038 0.0157 210 GLY A N 1609 C CA . GLY A 210 ? 0.2782 0.3027 0.2472 0.0203 -0.0059 0.0211 210 GLY A CA 1610 C C . GLY A 210 ? 0.2770 0.3057 0.2497 0.0157 -0.0077 0.0163 210 GLY A C 1611 O O . GLY A 210 ? 0.2556 0.3153 0.2349 0.0164 -0.0170 0.0321 210 GLY A O 1612 N N . ASP A 211 ? 0.2691 0.3039 0.2350 0.0196 -0.0089 0.0249 211 ASP A N 1613 C CA . ASP A 211 ? 0.2723 0.3061 0.2403 0.0169 -0.0058 0.0227 211 ASP A CA 1614 C C . ASP A 211 ? 0.2645 0.3051 0.2334 0.0183 -0.0098 0.0178 211 ASP A C 1615 O O . ASP A 211 ? 0.2591 0.3155 0.2385 0.0120 -0.0032 0.0193 211 ASP A O 1616 C CB . ASP A 211 ? 0.2693 0.3055 0.2323 0.0161 -0.0202 0.0235 211 ASP A CB 1617 C CG . ASP A 211 ? 0.2709 0.2940 0.2571 0.0096 -0.0009 0.0265 211 ASP A CG 1618 O OD1 . ASP A 211 ? 0.2633 0.2935 0.2613 0.0369 0.0011 0.0223 211 ASP A OD1 1619 O OD2 . ASP A 211 ? 0.2899 0.3221 0.2571 0.0137 -0.0118 0.0323 211 ASP A OD2 1620 N N . GLY A 212 ? 0.2656 0.3110 0.2407 0.0182 -0.0053 0.0188 212 GLY A N 1621 C CA . GLY A 212 ? 0.2648 0.3217 0.2328 0.0227 -0.0100 0.0179 212 GLY A CA 1622 C C . GLY A 212 ? 0.2831 0.3394 0.2390 0.0209 -0.0072 0.0164 212 GLY A C 1623 O O . GLY A 212 ? 0.2750 0.3490 0.2427 0.0273 -0.0094 0.0190 212 GLY A O 1624 N N . GLY A 213 ? 0.2792 0.3370 0.2393 0.0190 -0.0103 0.0192 213 GLY A N 1625 C CA . GLY A 213 ? 0.2897 0.3430 0.2615 0.0228 -0.0142 0.0153 213 GLY A CA 1626 C C . GLY A 213 ? 0.3036 0.3503 0.2722 0.0199 -0.0074 0.0100 213 GLY A C 1627 O O . GLY A 213 ? 0.3101 0.3566 0.2800 0.0339 -0.0137 0.0174 213 GLY A O 1628 N N . THR A 214 ? 0.3105 0.3484 0.2793 0.0210 -0.0081 0.0097 214 THR A N 1629 C CA . THR A 214 ? 0.3238 0.3593 0.2856 0.0157 -0.0066 0.0048 214 THR A CA 1630 C C . THR A 214 ? 0.3321 0.3709 0.2942 0.0155 -0.0059 0.0000 214 THR A C 1631 O O . THR A 214 ? 0.3162 0.3841 0.2851 0.0227 -0.0081 -0.0001 214 THR A O 1632 C CB . THR A 214 ? 0.3379 0.3540 0.3007 0.0164 -0.0038 0.0053 214 THR A CB 1633 O OG1 . THR A 214 ? 0.3005 0.3705 0.2782 0.0182 -0.0114 0.0138 214 THR A OG1 1634 C CG2 . THR A 214 ? 0.3212 0.3507 0.2866 0.0219 -0.0061 0.0014 214 THR A CG2 1635 N N . VAL A 215 ? 0.3241 0.3766 0.2984 0.0119 -0.0080 -0.0025 215 VAL A N 1636 C CA . VAL A 215 ? 0.3448 0.3835 0.3217 0.0115 -0.0134 -0.0066 215 VAL A CA 1637 C C . VAL A 215 ? 0.3346 0.3804 0.3143 0.0111 -0.0138 -0.0021 215 VAL A C 1638 O O . VAL A 215 ? 0.3214 0.3729 0.3200 0.0157 -0.0123 -0.0002 215 VAL A O 1639 C CB . VAL A 215 ? 0.3444 0.3886 0.3257 0.0104 -0.0129 -0.0092 215 VAL A CB 1640 C CG1 . VAL A 215 ? 0.3718 0.4052 0.3557 0.0040 -0.0160 -0.0151 215 VAL A CG1 1641 C CG2 . VAL A 215 ? 0.3761 0.3841 0.3551 0.0054 -0.0152 -0.0048 215 VAL A CG2 1642 N N . ASP A 216 ? 0.3345 0.3826 0.3080 0.0159 -0.0176 0.0032 216 ASP A N 1643 C CA . ASP A 216 ? 0.3408 0.3821 0.3057 0.0119 -0.0184 0.0031 216 ASP A CA 1644 C C . ASP A 216 ? 0.3335 0.3711 0.2901 0.0138 -0.0147 0.0057 216 ASP A C 1645 O O . ASP A 216 ? 0.3265 0.3754 0.2772 0.0237 -0.0152 0.0062 216 ASP A O 1646 C CB . ASP A 216 ? 0.3569 0.3890 0.3207 0.0088 -0.0176 0.0047 216 ASP A CB 1647 C CG . ASP A 216 ? 0.3893 0.4174 0.3365 -0.0038 -0.0191 0.0056 216 ASP A CG 1648 O OD1 . ASP A 216 ? 0.4357 0.4477 0.3575 0.0008 -0.0182 0.0103 216 ASP A OD1 1649 O OD2 . ASP A 216 ? 0.4154 0.4829 0.3670 -0.0011 -0.0341 -0.0004 216 ASP A OD2 1650 N N . GLY A 217 ? 0.3171 0.3698 0.2832 0.0147 -0.0123 0.0070 217 GLY A N 1651 C CA . GLY A 217 ? 0.3062 0.3655 0.2762 0.0124 -0.0143 0.0078 217 GLY A CA 1652 C C . GLY A 217 ? 0.3057 0.3617 0.2843 0.0123 -0.0157 0.0059 217 GLY A C 1653 O O . GLY A 217 ? 0.3171 0.3726 0.2801 0.0175 -0.0240 0.0108 217 GLY A O 1654 N N . ILE A 218 ? 0.2903 0.3603 0.2730 0.0038 -0.0150 0.0061 218 ILE A N 1655 C CA . ILE A 218 ? 0.2860 0.3587 0.2706 0.0063 -0.0148 0.0030 218 ILE A CA 1656 C C . ILE A 218 ? 0.2854 0.3528 0.2689 0.0101 -0.0100 0.0059 218 ILE A C 1657 O O . ILE A 218 ? 0.2956 0.3558 0.2524 0.0145 -0.0171 0.0026 218 ILE A O 1658 C CB . ILE A 218 ? 0.2861 0.3596 0.2733 -0.0018 -0.0101 0.0036 218 ILE A CB 1659 C CG1 . ILE A 218 ? 0.3013 0.3707 0.2851 0.0055 -0.0167 -0.0050 218 ILE A CG1 1660 C CG2 . ILE A 218 ? 0.2782 0.3616 0.2881 -0.0090 -0.0098 0.0124 218 ILE A CG2 1661 C CD1 . ILE A 218 ? 0.3013 0.3758 0.3104 0.0071 -0.0297 -0.0100 218 ILE A CD1 1662 N N . ASN A 219 ? 0.2726 0.3507 0.2588 0.0144 -0.0085 0.0076 219 ASN A N 1663 C CA . ASN A 219 ? 0.2722 0.3406 0.2603 0.0153 -0.0045 0.0041 219 ASN A CA 1664 C C . ASN A 219 ? 0.2713 0.3355 0.2598 0.0150 -0.0073 0.0047 219 ASN A C 1665 O O . ASN A 219 ? 0.2648 0.3338 0.2527 0.0114 -0.0084 -0.0010 219 ASN A O 1666 C CB . ASN A 219 ? 0.2777 0.3372 0.2553 0.0125 -0.0089 0.0089 219 ASN A CB 1667 C CG . ASN A 219 ? 0.2727 0.3267 0.2574 0.0101 -0.0001 0.0056 219 ASN A CG 1668 O OD1 . ASN A 219 ? 0.3233 0.3833 0.2652 0.0001 -0.0013 0.0225 219 ASN A OD1 1669 N ND2 . ASN A 219 ? 0.2185 0.2995 0.1957 0.0203 -0.0031 0.0189 219 ASN A ND2 1670 N N . GLU A 220 ? 0.2729 0.3349 0.2574 0.0160 -0.0137 0.0049 220 GLU A N 1671 C CA . GLU A 220 ? 0.2767 0.3460 0.2671 0.0196 -0.0112 0.0057 220 GLU A CA 1672 C C . GLU A 220 ? 0.2865 0.3590 0.2749 0.0192 -0.0124 0.0025 220 GLU A C 1673 O O . GLU A 220 ? 0.2818 0.3704 0.2689 0.0246 -0.0159 0.0030 220 GLU A O 1674 C CB . GLU A 220 ? 0.2772 0.3434 0.2689 0.0154 -0.0093 0.0046 220 GLU A CB 1675 C CG . GLU A 220 ? 0.3004 0.3627 0.2874 0.0197 -0.0076 0.0151 220 GLU A CG 1676 C CD . GLU A 220 ? 0.2951 0.3517 0.2925 0.0142 -0.0046 0.0121 220 GLU A CD 1677 O OE1 . GLU A 220 ? 0.3023 0.3908 0.3187 -0.0062 -0.0120 0.0155 220 GLU A OE1 1678 O OE2 . GLU A 220 ? 0.2987 0.3814 0.2958 0.0118 -0.0050 0.0130 220 GLU A OE2 1679 N N . ASN A 221 ? 0.2908 0.3622 0.2782 0.0225 -0.0175 0.0059 221 ASN A N 1680 C CA . ASN A 221 ? 0.3091 0.3633 0.2863 0.0170 -0.0205 -0.0007 221 ASN A CA 1681 C C . ASN A 221 ? 0.3054 0.3592 0.2915 0.0210 -0.0210 0.0037 221 ASN A C 1682 O O . ASN A 221 ? 0.2929 0.3540 0.2746 0.0255 -0.0241 0.0033 221 ASN A O 1683 C CB . ASN A 221 ? 0.3076 0.3708 0.3008 0.0165 -0.0129 -0.0010 221 ASN A CB 1684 C CG . ASN A 221 ? 0.3458 0.3900 0.3132 0.0089 -0.0210 -0.0090 221 ASN A CG 1685 O OD1 . ASN A 221 ? 0.3658 0.4366 0.3376 0.0235 -0.0143 -0.0002 221 ASN A OD1 1686 N ND2 . ASN A 221 ? 0.3614 0.4126 0.3574 -0.0008 -0.0048 -0.0103 221 ASN A ND2 1687 N N . ASN A 222 ? 0.3108 0.3598 0.2948 0.0189 -0.0219 0.0068 222 ASN A N 1688 C CA . ASN A 222 ? 0.3206 0.3687 0.3113 0.0218 -0.0226 0.0076 222 ASN A CA 1689 C C . ASN A 222 ? 0.3249 0.3660 0.3119 0.0253 -0.0248 0.0133 222 ASN A C 1690 O O . ASN A 222 ? 0.3293 0.3829 0.3226 0.0349 -0.0195 0.0110 222 ASN A O 1691 C CB . ASN A 222 ? 0.3152 0.3673 0.3152 0.0229 -0.0221 0.0093 222 ASN A CB 1692 C CG . ASN A 222 ? 0.3396 0.3844 0.3454 0.0204 -0.0145 0.0071 222 ASN A CG 1693 O OD1 . ASN A 222 ? 0.3463 0.3889 0.3500 0.0283 -0.0203 0.0103 222 ASN A OD1 1694 N ND2 . ASN A 222 ? 0.3393 0.4246 0.3188 0.0117 -0.0234 0.0083 222 ASN A ND2 1695 N N . THR A 223 ? 0.3330 0.3688 0.3160 0.0266 -0.0277 0.0164 223 THR A N 1696 C CA . THR A 223 ? 0.3452 0.3723 0.3282 0.0235 -0.0242 0.0185 223 THR A CA 1697 C C . THR A 223 ? 0.3599 0.3783 0.3361 0.0240 -0.0200 0.0185 223 THR A C 1698 O O . THR A 223 ? 0.3539 0.3783 0.3216 0.0350 -0.0227 0.0287 223 THR A O 1699 C CB . THR A 223 ? 0.3483 0.3704 0.3399 0.0178 -0.0183 0.0146 223 THR A CB 1700 O OG1 . THR A 223 ? 0.3650 0.3865 0.3540 0.0204 -0.0334 0.0220 223 THR A OG1 1701 C CG2 . THR A 223 ? 0.3550 0.3738 0.3408 0.0184 -0.0189 0.0180 223 THR A CG2 1702 N N . ILE A 224 ? 0.3693 0.3965 0.3430 0.0215 -0.0191 0.0211 224 ILE A N 1703 C CA . ILE A 224 ? 0.3884 0.4068 0.3653 0.0175 -0.0182 0.0174 224 ILE A CA 1704 C C . ILE A 224 ? 0.3954 0.4136 0.3676 0.0164 -0.0144 0.0195 224 ILE A C 1705 O O . ILE A 224 ? 0.4113 0.4307 0.3706 0.0195 -0.0081 0.0189 224 ILE A O 1706 C CB . ILE A 224 ? 0.3850 0.4040 0.3643 0.0162 -0.0160 0.0145 224 ILE A CB 1707 C CG1 . ILE A 224 ? 0.3908 0.4105 0.3670 0.0130 -0.0231 0.0140 224 ILE A CG1 1708 C CG2 . ILE A 224 ? 0.3911 0.4108 0.3627 0.0171 -0.0219 0.0155 224 ILE A CG2 1709 C CD1 . ILE A 224 ? 0.3961 0.4093 0.3816 0.0140 -0.0151 0.0115 224 ILE A CD1 1710 N N . ILE A 225 ? 0.4038 0.4153 0.3739 0.0161 -0.0106 0.0172 225 ILE A N 1711 C CA . ILE A 225 ? 0.4103 0.4234 0.3862 0.0114 -0.0057 0.0160 225 ILE A CA 1712 C C . ILE A 225 ? 0.4233 0.4250 0.3986 0.0142 -0.0034 0.0191 225 ILE A C 1713 O O . ILE A 225 ? 0.4173 0.4151 0.3815 0.0211 -0.0092 0.0301 225 ILE A O 1714 C CB . ILE A 225 ? 0.4099 0.4240 0.3892 0.0080 -0.0041 0.0139 225 ILE A CB 1715 C CG1 . ILE A 225 ? 0.4097 0.4250 0.3978 0.0110 -0.0020 0.0136 225 ILE A CG1 1716 C CG2 . ILE A 225 ? 0.4213 0.4273 0.3879 0.0088 -0.0083 0.0068 225 ILE A CG2 1717 C CD1 . ILE A 225 ? 0.4038 0.4311 0.3902 0.0042 -0.0054 0.0161 225 ILE A CD1 1718 N N . ASN A 226 ? 0.4366 0.4330 0.4061 0.0127 -0.0017 0.0222 226 ASN A N 1719 C CA . ASN A 226 ? 0.4464 0.4429 0.4201 0.0111 -0.0010 0.0172 226 ASN A CA 1720 C C . ASN A 226 ? 0.4476 0.4471 0.4215 0.0110 -0.0007 0.0126 226 ASN A C 1721 O O . ASN A 226 ? 0.4374 0.4494 0.4143 0.0166 0.0025 0.0104 226 ASN A O 1722 C CB . ASN A 226 ? 0.4481 0.4456 0.4213 0.0118 -0.0027 0.0208 226 ASN A CB 1723 C CG . ASN A 226 ? 0.4728 0.4792 0.4504 0.0058 0.0036 0.0197 226 ASN A CG 1724 O OD1 . ASN A 226 ? 0.4858 0.5042 0.4409 0.0047 -0.0057 0.0277 226 ASN A OD1 1725 N ND2 . ASN A 226 ? 0.4918 0.4989 0.4445 0.0117 -0.0021 0.0322 226 ASN A ND2 1726 N N . ARG A 227 ? 0.4477 0.4479 0.4319 0.0135 -0.0008 0.0130 227 ARG A N 1727 C CA . ARG A 227 ? 0.4543 0.4522 0.4343 0.0122 0.0000 0.0085 227 ARG A CA 1728 C C . ARG A 227 ? 0.4551 0.4544 0.4349 0.0121 -0.0010 0.0108 227 ARG A C 1729 O O . ARG A 227 ? 0.4520 0.4546 0.4221 0.0125 -0.0004 0.0126 227 ARG A O 1730 C CB . ARG A 227 ? 0.4651 0.4593 0.4492 0.0113 -0.0010 0.0066 227 ARG A CB 1731 C CG . ARG A 227 ? 0.4704 0.4662 0.4612 0.0092 -0.0062 -0.0029 227 ARG A CG 1732 C CD . ARG A 227 ? 0.5018 0.4902 0.4556 0.0070 -0.0202 -0.0209 227 ARG A CD 1733 N NE . ARG A 227 ? 0.6408 0.6418 0.5548 0.1160 0.0384 0.0384 227 ARG A NE 1734 C CZ . ARG A 227 ? 0.4163 0.4216 0.4347 -0.1195 0.0177 -0.0180 227 ARG A CZ 1735 N NH1 . ARG A 227 ? 0.6742 0.6202 0.6685 0.0759 -0.0651 -0.0317 227 ARG A NH1 1736 N NH2 . ARG A 227 ? 0.5679 0.5920 0.6475 0.0183 0.0066 0.0220 227 ARG A NH2 1737 N N . GLU A 228 ? 0.4470 0.4523 0.4323 0.0131 0.0008 0.0166 228 GLU A N 1738 C CA . GLU A 228 ? 0.4635 0.4679 0.4480 0.0157 0.0012 0.0133 228 GLU A CA 1739 C C . GLU A 228 ? 0.4362 0.4462 0.4162 0.0118 0.0039 0.0179 228 GLU A C 1740 O O . GLU A 228 ? 0.4347 0.4477 0.4253 0.0102 0.0057 0.0232 228 GLU A O 1741 C CB . GLU A 228 ? 0.4583 0.4588 0.4379 0.0084 0.0013 0.0195 228 GLU A CB 1742 C CG . GLU A 228 ? 0.4929 0.5041 0.4844 0.0029 0.0029 0.0098 228 GLU A CG 1743 C CD . GLU A 228 ? 0.4735 0.4795 0.4654 -0.0117 -0.0013 0.0295 228 GLU A CD 1744 O OE1 . GLU A 228 ? 0.5675 0.5727 0.5560 0.0059 -0.0015 0.0125 228 GLU A OE1 1745 O OE2 . GLU A 228 ? 0.5858 0.5749 0.5527 0.0038 -0.0022 0.0033 228 GLU A OE2 1746 N N . GLY A 229 ? 0.4268 0.4368 0.4015 0.0170 0.0079 0.0238 229 GLY A N 1747 C CA . GLY A 229 ? 0.4138 0.4340 0.3851 0.0181 0.0078 0.0186 229 GLY A CA 1748 C C . GLY A 229 ? 0.4029 0.4259 0.3801 0.0193 0.0078 0.0195 229 GLY A C 1749 O O . GLY A 229 ? 0.3990 0.4348 0.3771 0.0224 0.0091 0.0148 229 GLY A O 1750 N N . LEU A 230 ? 0.3860 0.4097 0.3604 0.0225 0.0081 0.0201 230 LEU A N 1751 C CA . LEU A 230 ? 0.3791 0.3917 0.3563 0.0196 0.0100 0.0202 230 LEU A CA 1752 C C . LEU A 230 ? 0.3766 0.3852 0.3552 0.0224 0.0106 0.0178 230 LEU A C 1753 O O . LEU A 230 ? 0.3693 0.3812 0.3628 0.0368 0.0133 0.0209 230 LEU A O 1754 C CB . LEU A 230 ? 0.3791 0.3833 0.3439 0.0184 0.0120 0.0183 230 LEU A CB 1755 C CG . LEU A 230 ? 0.3728 0.3779 0.3392 0.0141 0.0117 0.0133 230 LEU A CG 1756 C CD1 . LEU A 230 ? 0.3698 0.3765 0.3148 0.0192 0.0079 0.0168 230 LEU A CD1 1757 C CD2 . LEU A 230 ? 0.3886 0.3973 0.3404 0.0213 0.0108 0.0092 230 LEU A CD2 1758 N N . MET A 231 ? 0.3667 0.3711 0.3571 0.0259 0.0072 0.0258 231 MET A N 1759 C CA . MET A 231 ? 0.3700 0.3688 0.3592 0.0250 0.0068 0.0240 231 MET A CA 1760 C C . MET A 231 ? 0.3669 0.3610 0.3596 0.0243 0.0023 0.0221 231 MET A C 1761 O O . MET A 231 ? 0.3764 0.3638 0.3631 0.0323 0.0005 0.0271 231 MET A O 1762 C CB . MET A 231 ? 0.3718 0.3796 0.3716 0.0242 0.0098 0.0246 231 MET A CB 1763 C CG . MET A 231 ? 0.3721 0.3954 0.3638 0.0298 0.0132 0.0280 231 MET A CG 1764 S SD . MET A 231 ? 0.4035 0.4654 0.3784 0.0535 0.0252 0.0585 231 MET A SD 1765 C CE . MET A 231 ? 0.3887 0.4219 0.3894 0.0222 0.0159 0.0272 231 MET A CE 1766 N N . ASN A 232 ? 0.3693 0.3575 0.3584 0.0281 0.0013 0.0284 232 ASN A N 1767 C CA . ASN A 232 ? 0.3739 0.3654 0.3609 0.0239 0.0023 0.0260 232 ASN A CA 1768 C C . ASN A 232 ? 0.3615 0.3506 0.3419 0.0200 0.0036 0.0300 232 ASN A C 1769 O O . ASN A 232 ? 0.3597 0.3480 0.3409 0.0238 -0.0029 0.0438 232 ASN A O 1770 C CB . ASN A 232 ? 0.3925 0.3865 0.3719 0.0211 0.0017 0.0249 232 ASN A CB 1771 C CG . ASN A 232 ? 0.4394 0.4457 0.4404 0.0061 0.0057 0.0095 232 ASN A CG 1772 O OD1 . ASN A 232 ? 0.5084 0.5044 0.5221 -0.0082 -0.0060 -0.0019 232 ASN A OD1 1773 N ND2 . ASN A 232 ? 0.5027 0.4836 0.4911 0.0126 0.0095 -0.0090 232 ASN A ND2 1774 N N . ILE A 233 ? 0.3433 0.3363 0.3150 0.0202 0.0097 0.0315 233 ILE A N 1775 C CA . ILE A 233 ? 0.3337 0.3251 0.2845 0.0177 0.0132 0.0358 233 ILE A CA 1776 C C . ILE A 233 ? 0.3207 0.3283 0.2794 0.0157 0.0139 0.0349 233 ILE A C 1777 O O . ILE A 233 ? 0.3121 0.3370 0.2605 0.0251 0.0285 0.0451 233 ILE A O 1778 C CB . ILE A 233 ? 0.3315 0.3210 0.2870 0.0204 0.0083 0.0354 233 ILE A CB 1779 C CG1 . ILE A 233 ? 0.3443 0.3115 0.2763 0.0172 0.0079 0.0302 233 ILE A CG1 1780 C CG2 . ILE A 233 ? 0.3247 0.3166 0.2821 0.0258 0.0134 0.0374 233 ILE A CG2 1781 C CD1 . ILE A 233 ? 0.3355 0.3408 0.2993 0.0128 0.0042 0.0312 233 ILE A CD1 1782 N N . HIS A 234 ? 0.3191 0.3220 0.2730 0.0149 0.0189 0.0360 234 HIS A N 1783 C CA . HIS A 234 ? 0.3111 0.3067 0.2750 0.0151 0.0138 0.0309 234 HIS A CA 1784 C C . HIS A 234 ? 0.3095 0.3095 0.2838 0.0167 0.0131 0.0239 234 HIS A C 1785 O O . HIS A 234 ? 0.2940 0.3080 0.2803 0.0239 0.0159 0.0311 234 HIS A O 1786 C CB . HIS A 234 ? 0.3127 0.2948 0.2712 0.0192 0.0085 0.0257 234 HIS A CB 1787 C CG . HIS A 234 ? 0.3167 0.3124 0.2715 0.0071 0.0041 0.0202 234 HIS A CG 1788 N ND1 . HIS A 234 ? 0.3381 0.3246 0.2910 0.0205 -0.0146 0.0239 234 HIS A ND1 1789 C CD2 . HIS A 234 ? 0.2677 0.2738 0.2327 0.0244 -0.0037 0.0354 234 HIS A CD2 1790 C CE1 . HIS A 234 ? 0.2813 0.2908 0.2270 0.0317 -0.0065 0.0306 234 HIS A CE1 1791 N NE2 . HIS A 234 ? 0.3324 0.3402 0.3032 0.0108 -0.0025 0.0168 234 HIS A NE2 1792 N N . MET A 235 ? 0.2983 0.2978 0.2808 0.0161 0.0146 0.0257 235 MET A N 1793 C CA . MET A 235 ? 0.2995 0.3002 0.2834 0.0173 0.0122 0.0222 235 MET A CA 1794 C C . MET A 235 ? 0.2916 0.3050 0.2864 0.0202 0.0116 0.0220 235 MET A C 1795 O O . MET A 235 ? 0.2873 0.3156 0.2926 0.0249 0.0133 0.0221 235 MET A O 1796 C CB . MET A 235 ? 0.3012 0.3037 0.2802 0.0202 0.0141 0.0200 235 MET A CB 1797 C CG . MET A 235 ? 0.2944 0.3052 0.2720 0.0131 0.0243 0.0261 235 MET A CG 1798 S SD . MET A 235 ? 0.3354 0.3220 0.2782 0.0365 0.0452 0.0605 235 MET A SD 1799 C CE . MET A 235 ? 0.3236 0.3175 0.2744 0.0151 0.0327 0.0075 235 MET A CE 1800 N N . PRO A 236 ? 0.3019 0.3056 0.2887 0.0173 0.0116 0.0223 236 PRO A N 1801 C CA . PRO A 236 ? 0.2983 0.2936 0.2820 0.0131 0.0174 0.0203 236 PRO A CA 1802 C C . PRO A 236 ? 0.3008 0.2826 0.2704 0.0090 0.0244 0.0177 236 PRO A C 1803 O O . PRO A 236 ? 0.3104 0.2801 0.2686 0.0145 0.0275 0.0348 236 PRO A O 1804 C CB . PRO A 236 ? 0.3092 0.3052 0.2822 0.0070 0.0165 0.0116 236 PRO A CB 1805 C CG . PRO A 236 ? 0.2966 0.3043 0.2852 0.0085 0.0087 0.0184 236 PRO A CG 1806 C CD . PRO A 236 ? 0.3106 0.3121 0.2988 0.0085 0.0121 0.0144 236 PRO A CD 1807 N N . ALA A 237 ? 0.2934 0.2729 0.2634 0.0174 0.0295 0.0268 237 ALA A N 1808 C CA . ALA A 237 ? 0.2992 0.2738 0.2589 0.0119 0.0262 0.0159 237 ALA A CA 1809 C C . ALA A 237 ? 0.2924 0.2651 0.2625 0.0086 0.0259 0.0204 237 ALA A C 1810 O O . ALA A 237 ? 0.2932 0.2603 0.2642 0.0074 0.0288 0.0187 237 ALA A O 1811 C CB . ALA A 237 ? 0.3009 0.2665 0.2605 0.0136 0.0250 0.0176 237 ALA A CB 1812 N N . TYR A 238 ? 0.2894 0.2532 0.2589 0.0072 0.0278 0.0213 238 TYR A N 1813 C CA . TYR A 238 ? 0.2798 0.2555 0.2657 0.0072 0.0235 0.0135 238 TYR A CA 1814 C C . TYR A 238 ? 0.2915 0.2615 0.2744 0.0079 0.0229 0.0166 238 TYR A C 1815 O O . TYR A 238 ? 0.2823 0.2466 0.2690 0.0137 0.0273 0.0180 238 TYR A O 1816 C CB . TYR A 238 ? 0.2738 0.2616 0.2588 0.0023 0.0200 0.0137 238 TYR A CB 1817 C CG . TYR A 238 ? 0.2516 0.2527 0.2428 0.0158 0.0161 0.0158 238 TYR A CG 1818 C CD1 . TYR A 238 ? 0.2356 0.2433 0.2318 0.0020 0.0275 0.0241 238 TYR A CD1 1819 C CD2 . TYR A 238 ? 0.2598 0.2466 0.2571 0.0112 0.0025 0.0061 238 TYR A CD2 1820 C CE1 . TYR A 238 ? 0.2611 0.2368 0.2426 0.0132 0.0131 0.0130 238 TYR A CE1 1821 C CE2 . TYR A 238 ? 0.2763 0.2598 0.2412 0.0068 0.0146 0.0163 238 TYR A CE2 1822 C CZ . TYR A 238 ? 0.2618 0.2454 0.2429 0.0037 0.0051 0.0161 238 TYR A CZ 1823 O OH . TYR A 238 ? 0.2707 0.2663 0.2522 0.0070 0.0120 0.0165 238 TYR A OH 1824 N N . LYS A 239 ? 0.3037 0.2683 0.2838 0.0083 0.0251 0.0233 239 LYS A N 1825 C CA . LYS A 239 ? 0.3145 0.2748 0.2896 0.0022 0.0192 0.0245 239 LYS A CA 1826 C C . LYS A 239 ? 0.3111 0.2665 0.2826 0.0050 0.0227 0.0263 239 LYS A C 1827 O O . LYS A 239 ? 0.3009 0.2593 0.2784 0.0094 0.0232 0.0308 239 LYS A O 1828 C CB . LYS A 239 ? 0.3361 0.3076 0.3103 0.0044 0.0133 0.0304 239 LYS A CB 1829 C CG . LYS A 239 ? 0.3758 0.3196 0.3463 -0.0003 0.0131 0.0115 239 LYS A CG 1830 C CD . LYS A 239 ? 0.4246 0.3902 0.4162 0.0043 0.0141 0.0030 239 LYS A CD 1831 C CE . LYS A 239 ? 0.4194 0.3706 0.4216 -0.0122 -0.0009 -0.0136 239 LYS A CE 1832 N NZ . LYS A 239 ? 0.4691 0.4655 0.4787 -0.0024 0.0017 0.0080 239 LYS A NZ 1833 N N . ASN A 240 ? 0.2974 0.2636 0.2717 0.0035 0.0231 0.0330 240 ASN A N 1834 C CA . ASN A 240 ? 0.2970 0.2689 0.2672 0.0007 0.0225 0.0264 240 ASN A CA 1835 C C . ASN A 240 ? 0.2847 0.2585 0.2580 -0.0005 0.0200 0.0224 240 ASN A C 1836 O O . ASN A 240 ? 0.2809 0.2450 0.2567 -0.0092 0.0276 0.0300 240 ASN A O 1837 C CB . ASN A 240 ? 0.2936 0.2807 0.2687 0.0038 0.0214 0.0247 240 ASN A CB 1838 C CG . ASN A 240 ? 0.3261 0.3131 0.2867 -0.0087 0.0136 0.0219 240 ASN A CG 1839 O OD1 . ASN A 240 ? 0.3022 0.3193 0.2747 -0.0020 0.0189 0.0525 240 ASN A OD1 1840 N ND2 . ASN A 240 ? 0.3726 0.3670 0.3581 -0.0320 0.0097 0.0323 240 ASN A ND2 1841 N N . ALA A 241 ? 0.2784 0.2572 0.2656 0.0043 0.0215 0.0172 241 ALA A N 1842 C CA . ALA A 241 ? 0.2735 0.2529 0.2557 0.0021 0.0197 0.0105 241 ALA A CA 1843 C C . ALA A 241 ? 0.2786 0.2549 0.2619 0.0043 0.0169 0.0079 241 ALA A C 1844 O O . ALA A 241 ? 0.2742 0.2419 0.2722 0.0034 0.0054 0.0082 241 ALA A O 1845 C CB . ALA A 241 ? 0.2721 0.2535 0.2520 -0.0007 0.0209 0.0094 241 ALA A CB 1846 N N . MET A 242 ? 0.2758 0.2519 0.2630 0.0045 0.0230 0.0170 242 MET A N 1847 C CA . MET A 242 ? 0.2769 0.2619 0.2727 0.0066 0.0218 0.0125 242 MET A CA 1848 C C . MET A 242 ? 0.2843 0.2659 0.2763 0.0030 0.0232 0.0146 242 MET A C 1849 O O . MET A 242 ? 0.2786 0.2637 0.2759 0.0047 0.0339 0.0173 242 MET A O 1850 C CB . MET A 242 ? 0.2777 0.2641 0.2680 0.0039 0.0192 0.0150 242 MET A CB 1851 C CG . MET A 242 ? 0.2753 0.2689 0.2879 -0.0019 0.0286 0.0146 242 MET A CG 1852 S SD . MET A 242 ? 0.3111 0.3028 0.3063 0.0113 0.0598 0.0453 242 MET A SD 1853 C CE . MET A 242 ? 0.3193 0.3088 0.3294 0.0139 0.0175 0.0238 242 MET A CE 1854 N N . ASP A 243 ? 0.2882 0.2784 0.2910 0.0069 0.0338 0.0126 243 ASP A N 1855 C CA . ASP A 243 ? 0.2943 0.2837 0.2892 -0.0012 0.0247 0.0093 243 ASP A CA 1856 C C . ASP A 243 ? 0.3028 0.2875 0.2887 -0.0055 0.0258 0.0081 243 ASP A C 1857 O O . ASP A 243 ? 0.3123 0.2921 0.3057 -0.0141 0.0215 0.0076 243 ASP A O 1858 C CB . ASP A 243 ? 0.2981 0.2996 0.2881 -0.0006 0.0271 0.0165 243 ASP A CB 1859 C CG . ASP A 243 ? 0.3287 0.3212 0.3281 0.0025 0.0175 0.0100 243 ASP A CG 1860 O OD1 . ASP A 243 ? 0.3553 0.3289 0.3398 0.0008 0.0459 0.0180 243 ASP A OD1 1861 O OD2 . ASP A 243 ? 0.3518 0.3591 0.3195 0.0105 0.0327 0.0293 243 ASP A OD2 1862 N N . LYS A 244 ? 0.2894 0.2724 0.2747 0.0011 0.0323 0.0109 244 LYS A N 1863 C CA . LYS A 244 ? 0.2926 0.2773 0.2817 -0.0006 0.0263 0.0078 244 LYS A CA 1864 C C . LYS A 244 ? 0.2866 0.2684 0.2688 0.0058 0.0223 0.0085 244 LYS A C 1865 O O . LYS A 244 ? 0.3057 0.2830 0.2890 0.0104 0.0224 0.0067 244 LYS A O 1866 C CB . LYS A 244 ? 0.2910 0.2660 0.2688 0.0005 0.0274 0.0051 244 LYS A CB 1867 C CG . LYS A 244 ? 0.3040 0.2979 0.2712 -0.0026 0.0223 0.0068 244 LYS A CG 1868 C CD . LYS A 244 ? 0.3085 0.2865 0.2884 -0.0037 0.0250 0.0070 244 LYS A CD 1869 C CE . LYS A 244 ? 0.3190 0.2996 0.2823 0.0003 0.0171 0.0057 244 LYS A CE 1870 N NZ . LYS A 244 ? 0.3401 0.3259 0.3186 -0.0064 0.0162 -0.0032 244 LYS A NZ 1871 N N . GLY A 245 ? 0.2779 0.2539 0.2641 -0.0044 0.0248 0.0128 245 GLY A N 1872 C CA . GLY A 245 ? 0.2573 0.2511 0.2577 -0.0024 0.0278 0.0052 245 GLY A CA 1873 C C . GLY A 245 ? 0.2402 0.2373 0.2470 0.0028 0.0214 0.0018 245 GLY A C 1874 O O . GLY A 245 ? 0.2397 0.2449 0.2556 0.0043 0.0287 0.0024 245 GLY A O 1875 N N . VAL A 246 ? 0.2292 0.2416 0.2383 -0.0016 0.0257 0.0089 246 VAL A N 1876 C CA . VAL A 246 ? 0.2327 0.2384 0.2283 -0.0043 0.0205 0.0001 246 VAL A CA 1877 C C . VAL A 246 ? 0.2291 0.2431 0.2243 0.0044 0.0241 -0.0011 246 VAL A C 1878 O O . VAL A 246 ? 0.2310 0.2496 0.2243 0.0082 0.0227 0.0069 246 VAL A O 1879 C CB . VAL A 246 ? 0.2231 0.2348 0.2229 0.0009 0.0233 -0.0041 246 VAL A CB 1880 C CG1 . VAL A 246 ? 0.2480 0.2502 0.2221 0.0009 0.0071 0.0048 246 VAL A CG1 1881 C CG2 . VAL A 246 ? 0.2507 0.2377 0.2466 -0.0047 0.0125 0.0060 246 VAL A CG2 1882 N N . SER A 247 ? 0.2201 0.2434 0.2064 -0.0018 0.0267 -0.0002 247 SER A N 1883 C CA . SER A 247 ? 0.2273 0.2540 0.2161 -0.0012 0.0188 0.0029 247 SER A CA 1884 C C . SER A 247 ? 0.2213 0.2463 0.2091 0.0000 0.0184 0.0088 247 SER A C 1885 O O . SER A 247 ? 0.2199 0.2587 0.2150 0.0144 0.0192 0.0041 247 SER A O 1886 C CB . SER A 247 ? 0.2206 0.2572 0.2199 -0.0027 0.0145 0.0054 247 SER A CB 1887 O OG . SER A 247 ? 0.2454 0.2897 0.2445 -0.0120 0.0058 -0.0212 247 SER A OG 1888 N N . THR A 248 ? 0.2134 0.2286 0.1978 0.0032 0.0178 0.0064 248 THR A N 1889 C CA . THR A 248 ? 0.2208 0.2186 0.1955 -0.0023 0.0130 0.0031 248 THR A CA 1890 C C . THR A 248 ? 0.2246 0.2328 0.2031 0.0001 0.0134 0.0106 248 THR A C 1891 O O . THR A 248 ? 0.2097 0.2390 0.2088 -0.0037 0.0235 0.0055 248 THR A O 1892 C CB . THR A 248 ? 0.2291 0.2188 0.1952 0.0048 0.0160 0.0004 248 THR A CB 1893 O OG1 . THR A 248 ? 0.2015 0.2029 0.2060 0.0111 0.0214 0.0066 248 THR A OG1 1894 C CG2 . THR A 248 ? 0.2302 0.2187 0.1995 0.0062 0.0053 0.0106 248 THR A CG2 1895 N N . VAL A 249 ? 0.2192 0.2201 0.2005 -0.0026 0.0054 0.0088 249 VAL A N 1896 C CA . VAL A 249 ? 0.2219 0.2331 0.2022 0.0043 0.0001 0.0121 249 VAL A CA 1897 C C . VAL A 249 ? 0.2360 0.2372 0.2096 0.0051 0.0026 0.0159 249 VAL A C 1898 O O . VAL A 249 ? 0.2229 0.2462 0.2191 0.0135 0.0077 0.0102 249 VAL A O 1899 C CB . VAL A 249 ? 0.2315 0.2219 0.2030 0.0024 -0.0001 0.0098 249 VAL A CB 1900 C CG1 . VAL A 249 ? 0.2244 0.2430 0.2102 0.0201 -0.0042 0.0103 249 VAL A CG1 1901 C CG2 . VAL A 249 ? 0.2310 0.2413 0.2186 0.0084 0.0084 0.0128 249 VAL A CG2 1902 N N . MET A 250 ? 0.2296 0.2308 0.2018 0.0069 0.0074 0.0145 250 MET A N 1903 C CA . MET A 250 ? 0.2207 0.2429 0.2079 0.0088 0.0004 0.0116 250 MET A CA 1904 C C . MET A 250 ? 0.2166 0.2450 0.2058 0.0099 0.0020 0.0105 250 MET A C 1905 O O . MET A 250 ? 0.2009 0.2574 0.2043 0.0137 0.0119 0.0179 250 MET A O 1906 C CB . MET A 250 ? 0.2318 0.2264 0.2123 0.0051 -0.0016 0.0157 250 MET A CB 1907 C CG . MET A 250 ? 0.2289 0.2419 0.2329 -0.0053 -0.0045 0.0042 250 MET A CG 1908 S SD . MET A 250 ? 0.2339 0.2571 0.2269 0.0124 0.0012 0.0185 250 MET A SD 1909 C CE . MET A 250 ? 0.2572 0.2556 0.2538 -0.0039 -0.0186 0.0117 250 MET A CE 1910 N N . ILE A 251 ? 0.2002 0.2585 0.1981 0.0148 0.0008 0.0100 251 ILE A N 1911 C CA . ILE A 251 ? 0.2077 0.2698 0.2122 0.0135 -0.0004 0.0057 251 ILE A CA 1912 C C . ILE A 251 ? 0.2131 0.2673 0.2115 0.0102 0.0017 0.0083 251 ILE A C 1913 O O . ILE A 251 ? 0.2210 0.2771 0.2001 0.0105 0.0000 0.0198 251 ILE A O 1914 C CB . ILE A 251 ? 0.2108 0.2798 0.2231 0.0146 -0.0029 -0.0009 251 ILE A CB 1915 C CG1 . ILE A 251 ? 0.2091 0.2558 0.2475 0.0107 -0.0004 0.0020 251 ILE A CG1 1916 C CG2 . ILE A 251 ? 0.2229 0.2926 0.2257 0.0301 -0.0111 0.0116 251 ILE A CG2 1917 C CD1 . ILE A 251 ? 0.2535 0.2368 0.2498 0.0070 -0.0036 -0.0084 251 ILE A CD1 1918 N N . SER A 252 ? 0.2191 0.2699 0.2009 0.0117 0.0015 0.0075 252 SER A N 1919 C CA . SER A 252 ? 0.2351 0.2740 0.2044 0.0111 0.0079 0.0070 252 SER A CA 1920 C C . SER A 252 ? 0.2401 0.2831 0.2030 0.0112 0.0027 0.0065 252 SER A C 1921 O O . SER A 252 ? 0.2310 0.3011 0.2106 0.0095 0.0047 0.0116 252 SER A O 1922 C CB . SER A 252 ? 0.2411 0.2694 0.1957 0.0118 0.0065 0.0045 252 SER A CB 1923 O OG . SER A 252 ? 0.2461 0.2912 0.2203 0.0135 0.0079 -0.0138 252 SER A OG 1924 N N . TYR A 253 ? 0.2383 0.2850 0.2090 0.0038 0.0008 0.0164 253 TYR A N 1925 C CA . TYR A 253 ? 0.2500 0.2926 0.2138 0.0061 0.0001 0.0119 253 TYR A CA 1926 C C . TYR A 253 ? 0.2502 0.3028 0.2207 0.0074 -0.0004 0.0178 253 TYR A C 1927 O O . TYR A 253 ? 0.2534 0.3239 0.2142 0.0087 0.0102 0.0212 253 TYR A O 1928 C CB . TYR A 253 ? 0.2466 0.2895 0.2172 0.0092 0.0000 0.0144 253 TYR A CB 1929 C CG . TYR A 253 ? 0.2548 0.2864 0.2295 0.0063 0.0040 0.0113 253 TYR A CG 1930 C CD1 . TYR A 253 ? 0.2382 0.2864 0.2275 -0.0029 0.0042 0.0186 253 TYR A CD1 1931 C CD2 . TYR A 253 ? 0.2598 0.3123 0.2345 0.0149 -0.0056 0.0092 253 TYR A CD2 1932 C CE1 . TYR A 253 ? 0.2474 0.2649 0.2250 0.0143 -0.0036 0.0090 253 TYR A CE1 1933 C CE2 . TYR A 253 ? 0.2621 0.3048 0.2549 0.0071 0.0020 0.0155 253 TYR A CE2 1934 C CZ . TYR A 253 ? 0.2493 0.2929 0.2220 0.0107 -0.0032 0.0070 253 TYR A CZ 1935 O OH . TYR A 253 ? 0.2484 0.2991 0.2396 0.0175 0.0060 0.0142 253 TYR A OH 1936 N N . SER A 254 ? 0.2519 0.3150 0.2238 0.0123 0.0004 0.0189 254 SER A N 1937 C CA . SER A 254 ? 0.2670 0.3195 0.2415 0.0175 -0.0023 0.0238 254 SER A CA 1938 C C . SER A 254 ? 0.2797 0.3230 0.2568 0.0189 -0.0040 0.0184 254 SER A C 1939 O O . SER A 254 ? 0.2852 0.3141 0.2406 0.0260 -0.0098 0.0235 254 SER A O 1940 C CB . SER A 254 ? 0.2636 0.3156 0.2369 0.0136 0.0017 0.0254 254 SER A CB 1941 O OG . SER A 254 ? 0.2856 0.3189 0.2339 0.0070 -0.0004 0.0284 254 SER A OG 1942 N N . SER A 255 ? 0.2921 0.3380 0.2685 0.0216 -0.0081 0.0208 255 SER A N 1943 C CA . SER A 255 ? 0.2983 0.3464 0.2956 0.0148 -0.0115 0.0199 255 SER A CA 1944 C C . SER A 255 ? 0.3135 0.3541 0.3078 0.0170 -0.0105 0.0195 255 SER A C 1945 O O . SER A 255 ? 0.2996 0.3525 0.2942 0.0199 -0.0142 0.0292 255 SER A O 1946 C CB . SER A 255 ? 0.2952 0.3448 0.3006 0.0109 -0.0145 0.0165 255 SER A CB 1947 O OG . SER A 255 ? 0.2845 0.3762 0.3008 0.0047 -0.0269 0.0175 255 SER A OG 1948 N N . TRP A 256 ? 0.3252 0.3625 0.3259 0.0219 -0.0101 0.0219 256 TRP A N 1949 C CA . TRP A 256 ? 0.3331 0.3774 0.3323 0.0227 -0.0111 0.0227 256 TRP A CA 1950 C C . TRP A 256 ? 0.3393 0.3868 0.3355 0.0249 -0.0116 0.0199 256 TRP A C 1951 O O . TRP A 256 ? 0.3279 0.3862 0.3182 0.0432 -0.0195 0.0353 256 TRP A O 1952 C CB . TRP A 256 ? 0.3497 0.3900 0.3431 0.0172 -0.0053 0.0175 256 TRP A CB 1953 C CG . TRP A 256 ? 0.3699 0.3881 0.3514 0.0118 0.0051 0.0169 256 TRP A CG 1954 C CD1 . TRP A 256 ? 0.3949 0.4308 0.3809 0.0002 0.0016 0.0216 256 TRP A CD1 1955 C CD2 . TRP A 256 ? 0.3908 0.3836 0.3601 0.0148 0.0025 0.0091 256 TRP A CD2 1956 N NE1 . TRP A 256 ? 0.3976 0.3833 0.3857 0.0093 0.0044 0.0310 256 TRP A NE1 1957 C CE2 . TRP A 256 ? 0.4046 0.3771 0.3650 0.0094 0.0099 0.0058 256 TRP A CE2 1958 C CE3 . TRP A 256 ? 0.4026 0.4111 0.3705 0.0056 -0.0025 0.0120 256 TRP A CE3 1959 C CZ2 . TRP A 256 ? 0.4057 0.3897 0.3705 0.0045 0.0009 0.0153 256 TRP A CZ2 1960 C CZ3 . TRP A 256 ? 0.3916 0.3695 0.3608 0.0198 0.0115 0.0042 256 TRP A CZ3 1961 C CH2 . TRP A 256 ? 0.3984 0.3798 0.3767 0.0181 0.0062 0.0099 256 TRP A CH2 1962 N N . ASN A 257 ? 0.3430 0.4009 0.3407 0.0258 -0.0115 0.0190 257 ASN A N 1963 C CA . ASN A 257 ? 0.3552 0.4067 0.3548 0.0195 -0.0089 0.0117 257 ASN A CA 1964 C C . ASN A 257 ? 0.3603 0.4077 0.3617 0.0199 -0.0083 0.0132 257 ASN A C 1965 O O . ASN A 257 ? 0.3598 0.4187 0.3727 0.0305 -0.0069 0.0182 257 ASN A O 1966 C CB . ASN A 257 ? 0.3570 0.4058 0.3608 0.0185 -0.0098 0.0139 257 ASN A CB 1967 C CG . ASN A 257 ? 0.3680 0.4070 0.3500 0.0197 -0.0085 0.0123 257 ASN A CG 1968 O OD1 . ASN A 257 ? 0.4073 0.4250 0.3603 0.0430 -0.0146 0.0202 257 ASN A OD1 1969 N ND2 . ASN A 257 ? 0.3405 0.4055 0.3483 0.0247 -0.0039 0.0168 257 ASN A ND2 1970 N N . GLY A 258 ? 0.3538 0.4000 0.3514 0.0197 -0.0135 0.0111 258 GLY A N 1971 C CA . GLY A 258 ? 0.3541 0.3996 0.3418 0.0186 -0.0097 0.0117 258 GLY A CA 1972 C C . GLY A 258 ? 0.3484 0.3909 0.3426 0.0169 -0.0086 0.0111 258 GLY A C 1973 O O . GLY A 258 ? 0.3676 0.4044 0.3509 0.0139 -0.0066 0.0106 258 GLY A O 1974 N N . VAL A 259 ? 0.3310 0.3849 0.3269 0.0253 -0.0138 0.0137 259 VAL A N 1975 C CA . VAL A 259 ? 0.3219 0.3733 0.3214 0.0250 -0.0199 0.0206 259 VAL A CA 1976 C C . VAL A 259 ? 0.3108 0.3686 0.3120 0.0169 -0.0203 0.0269 259 VAL A C 1977 O O . VAL A 259 ? 0.3095 0.3764 0.3090 0.0234 -0.0174 0.0349 259 VAL A O 1978 C CB . VAL A 259 ? 0.3303 0.3784 0.3269 0.0235 -0.0189 0.0151 259 VAL A CB 1979 C CG1 . VAL A 259 ? 0.3266 0.3656 0.3200 0.0286 -0.0111 0.0175 259 VAL A CG1 1980 C CG2 . VAL A 259 ? 0.3286 0.3866 0.3387 0.0322 -0.0222 0.0217 259 VAL A CG2 1981 N N . LYS A 260 ? 0.2969 0.3579 0.2974 0.0149 -0.0219 0.0252 260 LYS A N 1982 C CA . LYS A 260 ? 0.2810 0.3359 0.2841 0.0160 -0.0156 0.0258 260 LYS A CA 1983 C C . LYS A 260 ? 0.2687 0.3334 0.2724 0.0184 -0.0129 0.0246 260 LYS A C 1984 O O . LYS A 260 ? 0.2409 0.3267 0.2640 0.0313 -0.0267 0.0314 260 LYS A O 1985 C CB . LYS A 260 ? 0.2814 0.3250 0.2827 0.0078 -0.0162 0.0190 260 LYS A CB 1986 C CG . LYS A 260 ? 0.2960 0.3281 0.2856 0.0107 -0.0087 0.0161 260 LYS A CG 1987 C CD . LYS A 260 ? 0.2911 0.3078 0.2712 0.0095 0.0013 0.0102 260 LYS A CD 1988 C CE . LYS A 260 ? 0.2841 0.3142 0.2874 0.0131 -0.0130 0.0085 260 LYS A CE 1989 N NZ . LYS A 260 ? 0.2858 0.3440 0.2861 0.0160 -0.0095 0.0033 260 LYS A NZ 1990 N N . MET A 261 ? 0.2452 0.3284 0.2519 0.0187 -0.0059 0.0233 261 MET A N 1991 C CA . MET A 261 ? 0.2476 0.3213 0.2523 0.0162 0.0035 0.0200 261 MET A CA 1992 C C . MET A 261 ? 0.2410 0.3123 0.2475 0.0184 -0.0009 0.0140 261 MET A C 1993 O O . MET A 261 ? 0.2500 0.3158 0.2386 0.0255 0.0006 0.0157 261 MET A O 1994 C CB . MET A 261 ? 0.2429 0.3142 0.2517 0.0174 0.0025 0.0251 261 MET A CB 1995 C CG . MET A 261 ? 0.2627 0.3354 0.2596 0.0147 0.0140 0.0183 261 MET A CG 1996 S SD . MET A 261 ? 0.3031 0.3740 0.2610 0.0322 -0.0096 0.0530 261 MET A SD 1997 C CE . MET A 261 ? 0.2762 0.3444 0.3092 0.0135 0.0008 0.0042 261 MET A CE 1998 N N . HIS A 262 ? 0.2381 0.3147 0.2502 0.0223 0.0012 0.0149 262 HIS A N 1999 C CA . HIS A 262 ? 0.2391 0.3080 0.2491 0.0273 0.0043 0.0133 262 HIS A CA 2000 C C . HIS A 262 ? 0.2455 0.3214 0.2639 0.0253 0.0079 0.0120 262 HIS A C 2001 O O . HIS A 262 ? 0.2552 0.3290 0.2549 0.0336 0.0006 0.0193 262 HIS A O 2002 C CB . HIS A 262 ? 0.2309 0.3042 0.2487 0.0199 0.0093 0.0087 262 HIS A CB 2003 C CG . HIS A 262 ? 0.2370 0.3014 0.2319 0.0230 -0.0095 0.0113 262 HIS A CG 2004 N ND1 . HIS A 262 ? 0.2449 0.3024 0.2436 0.0286 -0.0164 0.0111 262 HIS A ND1 2005 C CD2 . HIS A 262 ? 0.1945 0.2763 0.1961 0.0093 0.0010 0.0163 262 HIS A CD2 2006 C CE1 . HIS A 262 ? 0.1999 0.2568 0.1877 0.0159 -0.0090 0.0204 262 HIS A CE1 2007 N NE2 . HIS A 262 ? 0.2521 0.3172 0.2518 0.0128 -0.0125 0.0095 262 HIS A NE2 2008 N N . ALA A 263 ? 0.2446 0.3222 0.2725 0.0290 0.0022 0.0140 263 ALA A N 2009 C CA . ALA A 263 ? 0.2555 0.3246 0.2919 0.0242 0.0041 0.0069 263 ALA A CA 2010 C C . ALA A 263 ? 0.2642 0.3278 0.3001 0.0274 0.0015 0.0125 263 ALA A C 2011 O O . ALA A 263 ? 0.2721 0.3412 0.3264 0.0384 -0.0003 0.0098 263 ALA A O 2012 C CB . ALA A 263 ? 0.2561 0.3295 0.2923 0.0225 -0.0006 0.0031 263 ALA A CB 2013 N N . ASN A 264 ? 0.2678 0.3214 0.2911 0.0241 0.0023 0.0190 264 ASN A N 2014 C CA . ASN A 264 ? 0.2763 0.3185 0.2896 0.0213 0.0062 0.0189 264 ASN A CA 2015 C C . ASN A 264 ? 0.2726 0.3212 0.2815 0.0214 0.0066 0.0217 264 ASN A C 2016 O O . ASN A 264 ? 0.2732 0.3239 0.2839 0.0188 0.0072 0.0269 264 ASN A O 2017 C CB . ASN A 264 ? 0.2785 0.3212 0.2845 0.0245 0.0086 0.0225 264 ASN A CB 2018 C CG . ASN A 264 ? 0.3145 0.3186 0.3023 0.0204 0.0034 0.0168 264 ASN A CG 2019 O OD1 . ASN A 264 ? 0.3409 0.3198 0.3085 0.0323 -0.0089 0.0292 264 ASN A OD1 2020 N ND2 . ASN A 264 ? 0.3289 0.3458 0.3012 0.0309 0.0024 0.0299 264 ASN A ND2 2021 N N . GLN A 265 ? 0.2823 0.3313 0.2963 0.0290 0.0035 0.0147 265 GLN A N 2022 C CA . GLN A 265 ? 0.2757 0.3306 0.3044 0.0297 0.0043 0.0100 265 GLN A CA 2023 C C . GLN A 265 ? 0.2799 0.3349 0.2986 0.0320 0.0017 0.0106 265 GLN A C 2024 O O . GLN A 265 ? 0.2772 0.3332 0.2839 0.0311 0.0000 0.0132 265 GLN A O 2025 C CB . GLN A 265 ? 0.2782 0.3408 0.3153 0.0290 0.0015 0.0152 265 GLN A CB 2026 C CG . GLN A 265 ? 0.3185 0.3602 0.3482 0.0281 0.0021 0.0036 265 GLN A CG 2027 C CD . GLN A 265 ? 0.3580 0.4295 0.4154 0.0312 0.0113 0.0175 265 GLN A CD 2028 O OE1 . GLN A 265 ? 0.4172 0.4640 0.4738 0.0213 0.0100 0.0173 265 GLN A OE1 2029 N NE2 . GLN A 265 ? 0.3995 0.4571 0.4649 0.0289 0.0066 0.0122 265 GLN A NE2 2030 N N . ASP A 266 ? 0.2920 0.3457 0.3001 0.0332 0.0049 0.0092 266 ASP A N 2031 C CA . ASP A 266 ? 0.3173 0.3449 0.3101 0.0245 0.0005 0.0102 266 ASP A CA 2032 C C . ASP A 266 ? 0.3136 0.3274 0.2892 0.0239 0.0048 0.0105 266 ASP A C 2033 O O . ASP A 266 ? 0.3166 0.3254 0.2876 0.0322 0.0030 0.0091 266 ASP A O 2034 C CB . ASP A 266 ? 0.3383 0.3636 0.3181 0.0199 -0.0030 0.0061 266 ASP A CB 2035 C CG . ASP A 266 ? 0.3870 0.4268 0.3904 0.0203 -0.0045 0.0001 266 ASP A CG 2036 O OD1 . ASP A 266 ? 0.4738 0.4985 0.4357 0.0155 -0.0136 -0.0105 266 ASP A OD1 2037 O OD2 . ASP A 266 ? 0.4512 0.4901 0.4489 0.0312 0.0036 -0.0066 266 ASP A OD2 2038 N N . LEU A 267 ? 0.3150 0.3211 0.2789 0.0281 0.0051 0.0137 267 LEU A N 2039 C CA . LEU A 267 ? 0.3110 0.3085 0.2708 0.0237 0.0029 0.0143 267 LEU A CA 2040 C C . LEU A 267 ? 0.2965 0.2967 0.2689 0.0268 0.0012 0.0168 267 LEU A C 2041 O O . LEU A 267 ? 0.3086 0.2902 0.2611 0.0310 0.0042 0.0202 267 LEU A O 2042 C CB . LEU A 267 ? 0.3202 0.3128 0.2690 0.0254 0.0071 0.0103 267 LEU A CB 2043 C CG . LEU A 267 ? 0.3313 0.3207 0.2875 0.0205 -0.0012 0.0153 267 LEU A CG 2044 C CD1 . LEU A 267 ? 0.3511 0.3320 0.2844 0.0203 0.0017 0.0118 267 LEU A CD1 2045 C CD2 . LEU A 267 ? 0.3444 0.3512 0.3300 0.0045 0.0067 0.0134 267 LEU A CD2 2046 N N . VAL A 268 ? 0.2919 0.2974 0.2689 0.0290 0.0019 0.0204 268 VAL A N 2047 C CA . VAL A 268 ? 0.2778 0.2954 0.2697 0.0201 0.0032 0.0179 268 VAL A CA 2048 C C . VAL A 268 ? 0.2813 0.3026 0.2752 0.0166 0.0055 0.0182 268 VAL A C 2049 O O . VAL A 268 ? 0.2725 0.2962 0.2839 0.0172 0.0153 0.0175 268 VAL A O 2050 C CB . VAL A 268 ? 0.2768 0.2911 0.2663 0.0188 -0.0012 0.0151 268 VAL A CB 2051 C CG1 . VAL A 268 ? 0.2807 0.2987 0.2598 0.0188 0.0054 0.0143 268 VAL A CG1 2052 C CG2 . VAL A 268 ? 0.2764 0.2972 0.2859 0.0231 0.0058 0.0110 268 VAL A CG2 2053 N N . THR A 269 ? 0.2804 0.2988 0.2831 0.0232 0.0096 0.0192 269 THR A N 2054 C CA . THR A 269 ? 0.2944 0.2997 0.2958 0.0152 0.0077 0.0147 269 THR A CA 2055 C C . THR A 269 ? 0.2950 0.2992 0.3023 0.0182 0.0097 0.0119 269 THR A C 2056 O O . THR A 269 ? 0.2910 0.2882 0.3033 0.0149 0.0053 0.0165 269 THR A O 2057 C CB . THR A 269 ? 0.2949 0.2984 0.3012 0.0164 0.0113 0.0145 269 THR A CB 2058 O OG1 . THR A 269 ? 0.3058 0.3249 0.2972 0.0113 0.0203 0.0218 269 THR A OG1 2059 C CG2 . THR A 269 ? 0.3103 0.3132 0.3105 0.0177 0.0011 0.0118 269 THR A CG2 2060 N N . GLY A 270 ? 0.3064 0.3063 0.3098 0.0235 0.0103 0.0120 270 GLY A N 2061 C CA . GLY A 270 ? 0.3199 0.3151 0.3265 0.0205 0.0119 0.0177 270 GLY A CA 2062 C C . GLY A 270 ? 0.3353 0.3238 0.3293 0.0141 0.0095 0.0152 270 GLY A C 2063 O O . GLY A 270 ? 0.3479 0.3435 0.3514 0.0169 0.0169 0.0158 270 GLY A O 2064 N N . TYR A 271 ? 0.3229 0.3212 0.3186 0.0249 0.0058 0.0245 271 TYR A N 2065 C CA . TYR A 271 ? 0.3253 0.3168 0.3201 0.0152 0.0045 0.0239 271 TYR A CA 2066 C C . TYR A 271 ? 0.3112 0.3047 0.3115 0.0142 0.0096 0.0206 271 TYR A C 2067 O O . TYR A 271 ? 0.3182 0.2984 0.3065 0.0211 0.0028 0.0298 271 TYR A O 2068 C CB . TYR A 271 ? 0.3402 0.3324 0.3387 0.0178 0.0037 0.0207 271 TYR A CB 2069 C CG . TYR A 271 ? 0.3565 0.3488 0.3559 0.0094 0.0084 0.0235 271 TYR A CG 2070 C CD1 . TYR A 271 ? 0.3637 0.3632 0.3715 0.0156 0.0007 0.0244 271 TYR A CD1 2071 C CD2 . TYR A 271 ? 0.3488 0.3620 0.3573 0.0081 0.0104 0.0159 271 TYR A CD2 2072 C CE1 . TYR A 271 ? 0.3586 0.3676 0.3794 0.0104 0.0062 0.0240 271 TYR A CE1 2073 C CE2 . TYR A 271 ? 0.3669 0.3691 0.3730 0.0078 0.0093 0.0155 271 TYR A CE2 2074 C CZ . TYR A 271 ? 0.3599 0.3661 0.3817 0.0045 0.0154 0.0213 271 TYR A CZ 2075 O OH . TYR A 271 ? 0.3774 0.3875 0.3951 0.0018 0.0274 0.0281 271 TYR A OH 2076 N N . LEU A 272 ? 0.2938 0.2941 0.2897 0.0167 0.0154 0.0226 272 LEU A N 2077 C CA . LEU A 272 ? 0.2839 0.2818 0.2885 0.0113 0.0175 0.0222 272 LEU A CA 2078 C C . LEU A 272 ? 0.2868 0.2791 0.2910 0.0096 0.0125 0.0242 272 LEU A C 2079 O O . LEU A 272 ? 0.2594 0.2741 0.2855 0.0156 0.0204 0.0368 272 LEU A O 2080 C CB . LEU A 272 ? 0.2830 0.2778 0.2781 0.0144 0.0117 0.0201 272 LEU A CB 2081 C CG . LEU A 272 ? 0.2699 0.2647 0.2830 0.0169 0.0149 0.0119 272 LEU A CG 2082 C CD1 . LEU A 272 ? 0.2884 0.2592 0.2821 0.0104 0.0107 0.0302 272 LEU A CD1 2083 C CD2 . LEU A 272 ? 0.2818 0.2515 0.2700 0.0116 0.0106 0.0028 272 LEU A CD2 2084 N N . LYS A 273 ? 0.2825 0.2702 0.2939 0.0133 0.0199 0.0245 273 LYS A N 2085 C CA . LYS A 273 ? 0.2938 0.2798 0.3026 0.0064 0.0184 0.0239 273 LYS A CA 2086 C C . LYS A 273 ? 0.3120 0.2943 0.3218 0.0074 0.0159 0.0150 273 LYS A C 2087 O O . LYS A 273 ? 0.3180 0.2890 0.3258 0.0009 0.0198 0.0208 273 LYS A O 2088 C CB . LYS A 273 ? 0.2831 0.2751 0.2991 0.0066 0.0178 0.0245 273 LYS A CB 2089 C CG . LYS A 273 ? 0.2822 0.2663 0.2860 0.0099 0.0280 0.0266 273 LYS A CG 2090 C CD . LYS A 273 ? 0.2771 0.2686 0.2989 0.0099 0.0209 0.0237 273 LYS A CD 2091 C CE . LYS A 273 ? 0.2846 0.2861 0.2724 0.0035 0.0236 0.0283 273 LYS A CE 2092 N NZ . LYS A 273 ? 0.2525 0.2817 0.2905 0.0069 0.0169 0.0259 273 LYS A NZ 2093 N N . ASP A 274 ? 0.3316 0.3117 0.3405 0.0141 0.0115 0.0169 274 ASP A N 2094 C CA . ASP A 274 ? 0.3528 0.3200 0.3586 0.0073 0.0135 0.0169 274 ASP A CA 2095 C C . ASP A 274 ? 0.3619 0.3293 0.3689 0.0074 0.0149 0.0163 274 ASP A C 2096 O O . ASP A 274 ? 0.3846 0.3385 0.3930 0.0005 0.0226 0.0155 274 ASP A O 2097 C CB . ASP A 274 ? 0.3510 0.3254 0.3669 0.0118 0.0112 0.0141 274 ASP A CB 2098 C CG . ASP A 274 ? 0.3709 0.3533 0.3731 0.0116 0.0109 0.0027 274 ASP A CG 2099 O OD1 . ASP A 274 ? 0.4033 0.4021 0.3938 0.0325 0.0205 0.0029 274 ASP A OD1 2100 O OD2 . ASP A 274 ? 0.3830 0.3873 0.4203 0.0104 0.0142 0.0050 274 ASP A OD2 2101 N N . THR A 275 ? 0.3461 0.3225 0.3558 0.0118 0.0151 0.0198 275 THR A N 2102 C CA . THR A 275 ? 0.3477 0.3239 0.3594 0.0087 0.0135 0.0233 275 THR A CA 2103 C C . THR A 275 ? 0.3448 0.3274 0.3611 0.0038 0.0145 0.0184 275 THR A C 2104 O O . THR A 275 ? 0.3600 0.3338 0.3814 0.0073 0.0155 0.0277 275 THR A O 2105 C CB . THR A 275 ? 0.3409 0.3273 0.3600 -0.0002 0.0126 0.0204 275 THR A CB 2106 O OG1 . THR A 275 ? 0.3617 0.3185 0.3687 0.0160 0.0087 0.0401 275 THR A OG1 2107 C CG2 . THR A 275 ? 0.3631 0.3399 0.3616 0.0118 0.0196 0.0259 275 THR A CG2 2108 N N . LEU A 276 ? 0.3349 0.3241 0.3507 0.0103 0.0168 0.0214 276 LEU A N 2109 C CA . LEU A 276 ? 0.3309 0.3178 0.3364 0.0063 0.0143 0.0157 276 LEU A CA 2110 C C . LEU A 276 ? 0.3268 0.3147 0.3327 0.0063 0.0108 0.0204 276 LEU A C 2111 O O . LEU A 276 ? 0.3123 0.3187 0.3245 0.0029 0.0227 0.0245 276 LEU A O 2112 C CB . LEU A 276 ? 0.3356 0.3209 0.3412 0.0069 0.0155 0.0116 276 LEU A CB 2113 C CG . LEU A 276 ? 0.3483 0.3294 0.3415 0.0036 0.0101 0.0112 276 LEU A CG 2114 C CD1 . LEU A 276 ? 0.3283 0.3323 0.3260 0.0100 0.0154 -0.0076 276 LEU A CD1 2115 C CD2 . LEU A 276 ? 0.3568 0.3614 0.3692 -0.0003 0.0217 0.0088 276 LEU A CD2 2116 N N . LYS A 277 ? 0.3220 0.3045 0.3187 0.0111 0.0100 0.0226 277 LYS A N 2117 C CA . LYS A 277 ? 0.3199 0.3041 0.3228 0.0080 0.0100 0.0191 277 LYS A CA 2118 C C . LYS A 277 ? 0.2972 0.2908 0.3063 0.0082 0.0157 0.0158 277 LYS A C 2119 O O . LYS A 277 ? 0.2947 0.2998 0.3036 0.0039 0.0273 0.0214 277 LYS A O 2120 C CB . LYS A 277 ? 0.3564 0.3369 0.3442 -0.0075 0.0131 0.0040 277 LYS A CB 2121 C CG . LYS A 277 ? 0.3518 0.3203 0.3645 0.0211 0.0010 0.0236 277 LYS A CG 2122 C CD . LYS A 277 ? 0.4028 0.4263 0.4359 -0.0154 0.0066 -0.0130 277 LYS A CD 2123 C CE . LYS A 277 ? 0.3138 0.3269 0.3993 0.0513 -0.0161 0.0494 277 LYS A CE 2124 N NZ . LYS A 277 ? 0.4399 0.4226 0.4607 0.0170 -0.0053 0.0045 277 LYS A NZ 2125 N N . PHE A 278 ? 0.2962 0.2865 0.2965 0.0108 0.0116 0.0165 278 PHE A N 2126 C CA . PHE A 278 ? 0.2884 0.2666 0.2834 0.0114 0.0164 0.0129 278 PHE A CA 2127 C C . PHE A 278 ? 0.2884 0.2625 0.2803 0.0089 0.0160 0.0158 278 PHE A C 2128 O O . PHE A 278 ? 0.2887 0.2671 0.2871 0.0180 0.0307 0.0165 278 PHE A O 2129 C CB . PHE A 278 ? 0.2859 0.2568 0.2827 0.0136 0.0130 0.0161 278 PHE A CB 2130 C CG . PHE A 278 ? 0.2725 0.2543 0.2626 0.0176 0.0078 0.0139 278 PHE A CG 2131 C CD1 . PHE A 278 ? 0.2632 0.2598 0.2632 0.0177 0.0167 0.0189 278 PHE A CD1 2132 C CD2 . PHE A 278 ? 0.2579 0.2491 0.2706 0.0235 0.0180 0.0129 278 PHE A CD2 2133 C CE1 . PHE A 278 ? 0.2457 0.2165 0.2671 0.0203 0.0142 0.0062 278 PHE A CE1 2134 C CE2 . PHE A 278 ? 0.2556 0.2321 0.2697 0.0228 0.0123 0.0142 278 PHE A CE2 2135 C CZ . PHE A 278 ? 0.2606 0.2544 0.2730 0.0086 0.0143 0.0049 278 PHE A CZ 2136 N N . LYS A 279 ? 0.2922 0.2571 0.2761 0.0064 0.0210 0.0102 279 LYS A N 2137 C CA . LYS A 279 ? 0.2896 0.2620 0.2714 0.0104 0.0126 0.0129 279 LYS A CA 2138 C C . LYS A 279 ? 0.2760 0.2529 0.2716 0.0063 0.0154 0.0060 279 LYS A C 2139 O O . LYS A 279 ? 0.2742 0.2484 0.2787 0.0131 0.0129 0.0106 279 LYS A O 2140 C CB . LYS A 279 ? 0.2998 0.2666 0.2798 0.0060 0.0157 0.0137 279 LYS A CB 2141 C CG . LYS A 279 ? 0.3363 0.2991 0.3140 0.0149 0.0069 0.0192 279 LYS A CG 2142 C CD . LYS A 279 ? 0.3523 0.3436 0.3665 0.0100 -0.0044 0.0175 279 LYS A CD 2143 C CE . LYS A 279 ? 0.3975 0.3636 0.4118 0.0052 -0.0004 0.0097 279 LYS A CE 2144 N NZ . LYS A 279 ? 0.4145 0.3921 0.4284 0.0262 -0.0070 -0.0007 279 LYS A NZ 2145 N N . GLY A 280 ? 0.2678 0.2540 0.2729 0.0071 0.0168 0.0118 280 GLY A N 2146 C CA . GLY A 280 ? 0.2502 0.2490 0.2655 0.0080 0.0161 0.0041 280 GLY A CA 2147 C C . GLY A 280 ? 0.2387 0.2572 0.2544 0.0094 0.0181 0.0107 280 GLY A C 2148 O O . GLY A 280 ? 0.2391 0.2616 0.2551 0.0117 0.0166 0.0147 280 GLY A O 2149 N N . PHE A 281 ? 0.2334 0.2531 0.2493 0.0075 0.0193 0.0024 281 PHE A N 2150 C CA . PHE A 281 ? 0.2327 0.2507 0.2386 0.0097 0.0179 0.0020 281 PHE A CA 2151 C C . PHE A 281 ? 0.2308 0.2563 0.2325 0.0098 0.0143 0.0057 281 PHE A C 2152 O O . PHE A 281 ? 0.2167 0.2623 0.2246 0.0144 0.0329 0.0116 281 PHE A O 2153 C CB . PHE A 281 ? 0.2381 0.2548 0.2385 0.0136 0.0107 0.0086 281 PHE A CB 2154 C CG . PHE A 281 ? 0.2223 0.2482 0.2175 0.0061 0.0145 0.0059 281 PHE A CG 2155 C CD1 . PHE A 281 ? 0.2390 0.2529 0.2126 0.0039 0.0044 0.0083 281 PHE A CD1 2156 C CD2 . PHE A 281 ? 0.2201 0.2796 0.2148 0.0106 0.0109 0.0045 281 PHE A CD2 2157 C CE1 . PHE A 281 ? 0.2235 0.2669 0.2100 0.0065 0.0003 -0.0024 281 PHE A CE1 2158 C CE2 . PHE A 281 ? 0.2273 0.2713 0.2346 0.0073 0.0156 0.0073 281 PHE A CE2 2159 C CZ . PHE A 281 ? 0.2223 0.2768 0.2271 0.0048 0.0014 0.0131 281 PHE A CZ 2160 N N . VAL A 282 ? 0.2248 0.2441 0.2237 0.0108 0.0150 0.0099 282 VAL A N 2161 C CA . VAL A 282 ? 0.2207 0.2402 0.2256 0.0081 0.0033 0.0121 282 VAL A CA 2162 C C . VAL A 282 ? 0.2211 0.2431 0.2258 0.0084 0.0080 0.0076 282 VAL A C 2163 O O . VAL A 282 ? 0.2181 0.2529 0.2280 0.0012 0.0199 0.0113 282 VAL A O 2164 C CB . VAL A 282 ? 0.2274 0.2346 0.2236 0.0112 -0.0008 0.0092 282 VAL A CB 2165 C CG1 . VAL A 282 ? 0.2357 0.2387 0.2224 0.0098 -0.0014 0.0037 282 VAL A CG1 2166 C CG2 . VAL A 282 ? 0.2475 0.2447 0.2347 0.0094 0.0018 0.0220 282 VAL A CG2 2167 N N . ILE A 283 ? 0.2064 0.2353 0.2158 0.0121 0.0118 0.0149 283 ILE A N 2168 C CA . ILE A 283 ? 0.1935 0.2271 0.2019 0.0088 0.0052 0.0085 283 ILE A CA 2169 C C . ILE A 283 ? 0.1930 0.2324 0.2112 0.0043 0.0002 0.0116 283 ILE A C 2170 O O . ILE A 283 ? 0.1955 0.2336 0.1912 -0.0009 -0.0029 0.0117 283 ILE A O 2171 C CB . ILE A 283 ? 0.1932 0.2282 0.2010 0.0081 0.0123 0.0136 283 ILE A CB 2172 C CG1 . ILE A 283 ? 0.1883 0.2074 0.1909 0.0054 -0.0056 0.0086 283 ILE A CG1 2173 C CG2 . ILE A 283 ? 0.1736 0.2394 0.1830 -0.0016 0.0149 0.0109 283 ILE A CG2 2174 C CD1 . ILE A 283 ? 0.1908 0.2309 0.2033 0.0153 0.0032 0.0102 283 ILE A CD1 2175 N N . SER A 284 ? 0.1923 0.2385 0.2153 0.0033 0.0011 0.0091 284 SER A N 2176 C CA . SER A 284 ? 0.1904 0.2366 0.2038 0.0027 0.0041 0.0045 284 SER A CA 2177 C C . SER A 284 ? 0.1914 0.2357 0.2023 0.0011 0.0059 0.0058 284 SER A C 2178 O O . SER A 284 ? 0.1816 0.2554 0.2016 0.0147 0.0069 0.0025 284 SER A O 2179 C CB . SER A 284 ? 0.1971 0.2276 0.2099 0.0029 -0.0002 0.0068 284 SER A CB 2180 O OG . SER A 284 ? 0.2177 0.2372 0.2043 -0.0072 -0.0061 0.0137 284 SER A OG 2181 N N . ASP A 285 ? 0.2067 0.2557 0.2021 0.0060 0.0135 0.0053 285 ASP A N 2182 C CA . ASP A 285 ? 0.2165 0.2478 0.1981 0.0067 0.0063 0.0067 285 ASP A CA 2183 C C . ASP A 285 ? 0.2183 0.2568 0.2117 0.0045 0.0057 0.0072 285 ASP A C 2184 O O . ASP A 285 ? 0.2187 0.2613 0.2143 0.0047 0.0025 0.0139 285 ASP A O 2185 C CB . ASP A 285 ? 0.2273 0.2643 0.2074 0.0066 0.0052 -0.0005 285 ASP A CB 2186 C CG . ASP A 285 ? 0.2454 0.2784 0.2100 0.0090 0.0127 0.0037 285 ASP A CG 2187 O OD1 . ASP A 285 ? 0.2252 0.2698 0.2280 0.0170 0.0211 0.0046 285 ASP A OD1 2188 O OD2 . ASP A 285 ? 0.2739 0.2890 0.2180 0.0197 0.0355 0.0075 285 ASP A OD2 2189 N N . TRP A 286 ? 0.2181 0.2519 0.2106 0.0013 0.0052 0.0072 286 TRP A N 2190 C CA . TRP A 286 ? 0.2164 0.2541 0.2255 0.0032 -0.0022 0.0074 286 TRP A CA 2191 C C . TRP A 286 ? 0.2203 0.2643 0.2330 -0.0009 -0.0016 0.0070 286 TRP A C 2192 O O . TRP A 286 ? 0.2156 0.2879 0.2284 -0.0014 0.0012 0.0072 286 TRP A O 2193 C CB . TRP A 286 ? 0.2275 0.2553 0.2332 0.0046 -0.0012 0.0062 286 TRP A CB 2194 C CG . TRP A 286 ? 0.2471 0.2675 0.2344 -0.0014 -0.0029 0.0062 286 TRP A CG 2195 C CD1 . TRP A 286 ? 0.2659 0.2766 0.2539 -0.0029 -0.0088 0.0071 286 TRP A CD1 2196 C CD2 . TRP A 286 ? 0.2428 0.2503 0.2389 0.0110 0.0043 0.0084 286 TRP A CD2 2197 N NE1 . TRP A 286 ? 0.2713 0.2763 0.2553 0.0048 -0.0112 0.0050 286 TRP A NE1 2198 C CE2 . TRP A 286 ? 0.2533 0.2794 0.2403 -0.0033 -0.0072 0.0041 286 TRP A CE2 2199 C CE3 . TRP A 286 ? 0.2363 0.2713 0.2203 -0.0051 0.0087 0.0171 286 TRP A CE3 2200 C CZ2 . TRP A 286 ? 0.2672 0.2589 0.2585 0.0019 0.0009 0.0018 286 TRP A CZ2 2201 C CZ3 . TRP A 286 ? 0.2518 0.2658 0.2531 0.0056 0.0007 0.0130 286 TRP A CZ3 2202 C CH2 . TRP A 286 ? 0.2551 0.2590 0.2454 -0.0021 0.0020 0.0100 286 TRP A CH2 2203 N N . GLU A 287 ? 0.2185 0.2779 0.2302 0.0020 -0.0011 0.0081 287 GLU A N 2204 C CA . GLU A 287 ? 0.2377 0.2845 0.2495 0.0011 -0.0032 0.0108 287 GLU A CA 2205 C C . GLU A 287 ? 0.2272 0.2818 0.2360 0.0046 0.0035 0.0065 287 GLU A C 2206 O O . GLU A 287 ? 0.2348 0.2844 0.2370 0.0028 -0.0060 0.0139 287 GLU A O 2207 C CB . GLU A 287 ? 0.2438 0.2891 0.2549 -0.0049 -0.0031 0.0140 287 GLU A CB 2208 C CG . GLU A 287 ? 0.2833 0.2877 0.2864 -0.0060 -0.0060 0.0207 287 GLU A CG 2209 C CD . GLU A 287 ? 0.3055 0.3044 0.2941 -0.0002 0.0001 0.0097 287 GLU A CD 2210 O OE1 . GLU A 287 ? 0.3873 0.3212 0.3276 -0.0058 -0.0237 -0.0070 287 GLU A OE1 2211 O OE2 . GLU A 287 ? 0.3661 0.3271 0.3573 -0.0136 -0.0121 0.0295 287 GLU A OE2 2212 N N . GLY A 288 ? 0.2198 0.2806 0.2331 0.0093 0.0022 0.0073 288 GLY A N 2213 C CA . GLY A 288 ? 0.2200 0.2917 0.2347 0.0069 0.0015 0.0082 288 GLY A CA 2214 C C . GLY A 288 ? 0.2299 0.3068 0.2388 0.0078 -0.0002 0.0040 288 GLY A C 2215 O O . GLY A 288 ? 0.2226 0.3251 0.2379 0.0165 -0.0043 0.0086 288 GLY A O 2216 N N . ILE A 289 ? 0.2239 0.2963 0.2348 0.0063 -0.0006 0.0011 289 ILE A N 2217 C CA . ILE A 289 ? 0.2376 0.2996 0.2375 0.0037 0.0041 -0.0022 289 ILE A CA 2218 C C . ILE A 289 ? 0.2465 0.3083 0.2346 0.0024 0.0022 -0.0022 289 ILE A C 2219 O O . ILE A 289 ? 0.2364 0.3227 0.2349 0.0022 -0.0028 -0.0009 289 ILE A O 2220 C CB . ILE A 289 ? 0.2392 0.2924 0.2428 0.0041 0.0026 -0.0029 289 ILE A CB 2221 C CG1 . ILE A 289 ? 0.2488 0.2803 0.2315 0.0082 0.0035 -0.0010 289 ILE A CG1 2222 C CG2 . ILE A 289 ? 0.2347 0.2766 0.2434 0.0086 -0.0011 -0.0097 289 ILE A CG2 2223 C CD1 . ILE A 289 ? 0.2304 0.3075 0.2477 0.0070 0.0091 -0.0033 289 ILE A CD1 2224 N N . ASP A 290 ? 0.2558 0.3115 0.2322 -0.0025 -0.0013 0.0030 290 ASP A N 2225 C CA . ASP A 290 ? 0.2687 0.3182 0.2393 -0.0072 -0.0057 0.0020 290 ASP A CA 2226 C C . ASP A 290 ? 0.2730 0.3339 0.2528 -0.0074 -0.0090 0.0038 290 ASP A C 2227 O O . ASP A 290 ? 0.2713 0.3495 0.2533 -0.0176 -0.0129 0.0019 290 ASP A O 2228 C CB . ASP A 290 ? 0.2691 0.3218 0.2447 -0.0053 -0.0104 0.0016 290 ASP A CB 2229 C CG . ASP A 290 ? 0.2870 0.3197 0.2501 -0.0084 -0.0070 0.0054 290 ASP A CG 2230 O OD1 . ASP A 290 ? 0.2986 0.3617 0.2607 -0.0147 -0.0134 -0.0067 290 ASP A OD1 2231 O OD2 . ASP A 290 ? 0.2903 0.3426 0.2722 -0.0091 -0.0262 0.0031 290 ASP A OD2 2232 N N . ARG A 291 ? 0.2592 0.3284 0.2490 -0.0067 -0.0081 0.0048 291 ARG A N 2233 C CA . ARG A 291 ? 0.2763 0.3347 0.2637 -0.0004 -0.0053 0.0030 291 ARG A CA 2234 C C . ARG A 291 ? 0.2866 0.3406 0.2747 0.0026 -0.0088 0.0044 291 ARG A C 2235 O O . ARG A 291 ? 0.2967 0.3624 0.2715 0.0040 -0.0102 0.0048 291 ARG A O 2236 C CB . ARG A 291 ? 0.2688 0.3231 0.2658 0.0015 -0.0023 0.0046 291 ARG A CB 2237 C CG . ARG A 291 ? 0.2539 0.3108 0.2688 0.0060 -0.0042 0.0041 291 ARG A CG 2238 C CD . ARG A 291 ? 0.2672 0.3252 0.2901 0.0120 -0.0081 0.0074 291 ARG A CD 2239 N NE . ARG A 291 ? 0.2878 0.3257 0.2715 0.0069 -0.0029 0.0256 291 ARG A NE 2240 C CZ . ARG A 291 ? 0.3164 0.3311 0.3046 0.0107 0.0003 0.0091 291 ARG A CZ 2241 N NH1 . ARG A 291 ? 0.2805 0.3467 0.2909 -0.0051 -0.0091 0.0077 291 ARG A NH1 2242 N NH2 . ARG A 291 ? 0.3195 0.3295 0.2804 0.0167 -0.0197 0.0136 291 ARG A NH2 2243 N N . ILE A 292 ? 0.2922 0.3479 0.2807 0.0000 -0.0149 0.0045 292 ILE A N 2244 C CA . ILE A 292 ? 0.3095 0.3519 0.3067 0.0022 -0.0108 0.0023 292 ILE A CA 2245 C C . ILE A 292 ? 0.3178 0.3701 0.3128 -0.0018 -0.0128 0.0039 292 ILE A C 2246 O O . ILE A 292 ? 0.3170 0.3958 0.3015 -0.0044 -0.0143 0.0053 292 ILE A O 2247 C CB . ILE A 292 ? 0.3109 0.3484 0.3044 0.0043 -0.0076 0.0052 292 ILE A CB 2248 C CG1 . ILE A 292 ? 0.2998 0.3341 0.2884 0.0029 -0.0100 0.0042 292 ILE A CG1 2249 C CG2 . ILE A 292 ? 0.3029 0.3533 0.3040 0.0069 -0.0118 0.0064 292 ILE A CG2 2250 C CD1 . ILE A 292 ? 0.2916 0.3425 0.3100 0.0138 -0.0047 0.0016 292 ILE A CD1 2251 N N . THR A 293 ? 0.3243 0.3789 0.3188 -0.0113 -0.0100 0.0021 293 THR A N 2252 C CA . THR A 293 ? 0.3347 0.3891 0.3323 -0.0111 -0.0058 -0.0005 293 THR A CA 2253 C C . THR A 293 ? 0.3547 0.3991 0.3451 -0.0060 -0.0065 -0.0032 293 THR A C 2254 O O . THR A 293 ? 0.3452 0.4115 0.3301 -0.0087 -0.0141 -0.0117 293 THR A O 2255 C CB . THR A 293 ? 0.3245 0.3723 0.3296 -0.0097 -0.0045 -0.0004 293 THR A CB 2256 O OG1 . THR A 293 ? 0.3134 0.3845 0.3138 -0.0097 0.0000 -0.0053 293 THR A OG1 2257 C CG2 . THR A 293 ? 0.3064 0.3779 0.3266 -0.0128 0.0030 -0.0005 293 THR A CG2 2258 N N . THR A 294 ? 0.3748 0.4207 0.3703 -0.0062 -0.0108 -0.0072 294 THR A N 2259 C CA . THR A 294 ? 0.4059 0.4329 0.3989 -0.0071 -0.0065 -0.0057 294 THR A CA 2260 C C . THR A 294 ? 0.4064 0.4357 0.4057 -0.0062 -0.0072 -0.0080 294 THR A C 2261 O O . THR A 294 ? 0.4144 0.4490 0.4113 -0.0035 -0.0166 -0.0105 294 THR A O 2262 C CB . THR A 294 ? 0.4169 0.4363 0.4041 -0.0070 -0.0010 -0.0073 294 THR A CB 2263 O OG1 . THR A 294 ? 0.4312 0.4657 0.4201 -0.0123 0.0024 0.0018 294 THR A OG1 2264 C CG2 . THR A 294 ? 0.4379 0.4446 0.4191 -0.0038 -0.0038 -0.0090 294 THR A CG2 2265 N N . PRO A 295 ? 0.4023 0.4330 0.4111 -0.0081 -0.0072 -0.0076 295 PRO A N 2266 C CA . PRO A 295 ? 0.3954 0.4308 0.4072 -0.0102 -0.0073 -0.0097 295 PRO A CA 2267 C C . PRO A 295 ? 0.3799 0.4257 0.4033 -0.0103 -0.0082 -0.0110 295 PRO A C 2268 O O . PRO A 295 ? 0.3612 0.4260 0.4045 -0.0197 -0.0118 -0.0167 295 PRO A O 2269 C CB . PRO A 295 ? 0.4038 0.4379 0.4165 -0.0095 -0.0084 -0.0085 295 PRO A CB 2270 C CG . PRO A 295 ? 0.4084 0.4403 0.4249 -0.0064 -0.0065 -0.0105 295 PRO A CG 2271 C CD . PRO A 295 ? 0.4084 0.4343 0.4150 -0.0080 -0.0057 -0.0061 295 PRO A CD 2272 N N . ALA A 296 ? 0.3661 0.4178 0.3897 -0.0098 -0.0066 -0.0109 296 ALA A N 2273 C CA . ALA A 296 ? 0.3585 0.4135 0.3847 -0.0089 -0.0048 -0.0060 296 ALA A CA 2274 C C . ALA A 296 ? 0.3549 0.4121 0.3839 -0.0089 -0.0060 -0.0037 296 ALA A C 2275 O O . ALA A 296 ? 0.3600 0.4171 0.3821 -0.0117 0.0008 -0.0052 296 ALA A O 2276 C CB . ALA A 296 ? 0.3498 0.4096 0.3848 -0.0065 -0.0050 -0.0048 296 ALA A CB 2277 N N . GLY A 297 ? 0.3471 0.4102 0.3825 -0.0081 -0.0035 -0.0028 297 GLY A N 2278 C CA . GLY A 297 ? 0.3458 0.4110 0.3852 -0.0119 -0.0013 0.0003 297 GLY A CA 2279 C C . GLY A 297 ? 0.3474 0.4125 0.3856 -0.0106 -0.0048 0.0005 297 GLY A C 2280 O O . GLY A 297 ? 0.3418 0.4139 0.3925 -0.0151 -0.0003 0.0076 297 GLY A O 2281 N N . SER A 298 ? 0.3389 0.4083 0.3841 -0.0132 -0.0078 -0.0025 298 SER A N 2282 C CA . SER A 298 ? 0.3361 0.4077 0.3765 -0.0122 -0.0068 -0.0036 298 SER A CA 2283 C C . SER A 298 ? 0.3334 0.3995 0.3771 -0.0127 -0.0071 -0.0055 298 SER A C 2284 O O . SER A 298 ? 0.3284 0.4192 0.3886 -0.0189 -0.0051 -0.0132 298 SER A O 2285 C CB . SER A 298 ? 0.3403 0.4076 0.3785 -0.0147 -0.0129 -0.0046 298 SER A CB 2286 O OG . SER A 298 ? 0.3627 0.4222 0.3612 -0.0203 -0.0258 -0.0001 298 SER A OG 2287 N N . ASP A 299 ? 0.3107 0.3854 0.3561 -0.0115 -0.0129 -0.0046 299 ASP A N 2288 C CA . ASP A 299 ? 0.3082 0.3761 0.3416 -0.0102 -0.0142 -0.0052 299 ASP A CA 2289 C C . ASP A 299 ? 0.2957 0.3675 0.3253 -0.0065 -0.0136 -0.0023 299 ASP A C 2290 O O . ASP A 299 ? 0.2893 0.3622 0.3113 -0.0035 -0.0278 -0.0132 299 ASP A O 2291 C CB . ASP A 299 ? 0.3159 0.3813 0.3485 -0.0073 -0.0117 -0.0008 299 ASP A CB 2292 C CG . ASP A 299 ? 0.3432 0.4006 0.3680 -0.0012 -0.0126 -0.0014 299 ASP A CG 2293 O OD1 . ASP A 299 ? 0.3277 0.4453 0.3735 -0.0038 -0.0043 -0.0093 299 ASP A OD1 2294 O OD2 . ASP A 299 ? 0.3318 0.4400 0.4016 0.0065 -0.0331 0.0002 299 ASP A OD2 2295 N N . TYR A 300 ? 0.2761 0.3648 0.3113 -0.0067 -0.0130 -0.0059 300 TYR A N 2296 C CA . TYR A 300 ? 0.2683 0.3575 0.3017 -0.0058 -0.0094 -0.0032 300 TYR A CA 2297 C C . TYR A 300 ? 0.2686 0.3570 0.2987 -0.0052 -0.0084 -0.0001 300 TYR A C 2298 O O . TYR A 300 ? 0.2551 0.3545 0.2928 -0.0063 -0.0064 0.0116 300 TYR A O 2299 C CB . TYR A 300 ? 0.2705 0.3612 0.2931 -0.0093 -0.0057 -0.0021 300 TYR A CB 2300 C CG . TYR A 300 ? 0.2730 0.3697 0.2933 -0.0105 -0.0104 -0.0050 300 TYR A CG 2301 C CD1 . TYR A 300 ? 0.2795 0.3644 0.2954 -0.0139 -0.0077 -0.0065 300 TYR A CD1 2302 C CD2 . TYR A 300 ? 0.3019 0.3707 0.2941 -0.0092 0.0055 -0.0088 300 TYR A CD2 2303 C CE1 . TYR A 300 ? 0.2695 0.3518 0.2892 -0.0123 -0.0070 -0.0068 300 TYR A CE1 2304 C CE2 . TYR A 300 ? 0.2855 0.3940 0.2914 -0.0053 0.0080 -0.0089 300 TYR A CE2 2305 C CZ . TYR A 300 ? 0.2743 0.3747 0.2955 -0.0148 0.0016 -0.0095 300 TYR A CZ 2306 O OH . TYR A 300 ? 0.2500 0.3712 0.2578 0.0029 0.0021 -0.0010 300 TYR A OH 2307 N N . SER A 301 ? 0.2633 0.3599 0.3040 -0.0010 -0.0116 -0.0009 301 SER A N 2308 C CA . SER A 301 ? 0.2617 0.3590 0.3102 0.0032 -0.0069 -0.0018 301 SER A CA 2309 C C . SER A 301 ? 0.2603 0.3572 0.3037 0.0008 -0.0033 -0.0043 301 SER A C 2310 O O . SER A 301 ? 0.2473 0.3484 0.2866 0.0001 -0.0060 -0.0030 301 SER A O 2311 C CB . SER A 301 ? 0.2693 0.3620 0.3227 0.0013 -0.0047 -0.0030 301 SER A CB 2312 O OG . SER A 301 ? 0.2994 0.3913 0.3616 0.0042 -0.0084 -0.0083 301 SER A OG 2313 N N . TYR A 302 ? 0.2624 0.3549 0.2961 0.0002 -0.0082 -0.0043 302 TYR A N 2314 C CA . TYR A 302 ? 0.2766 0.3593 0.3017 0.0000 -0.0123 -0.0025 302 TYR A CA 2315 C C . TYR A 302 ? 0.2664 0.3422 0.2868 0.0051 -0.0080 0.0015 302 TYR A C 2316 O O . TYR A 302 ? 0.2466 0.3412 0.2840 0.0041 -0.0130 0.0087 302 TYR A O 2317 C CB . TYR A 302 ? 0.3078 0.3746 0.3176 0.0019 -0.0153 -0.0041 302 TYR A CB 2318 C CG . TYR A 302 ? 0.3543 0.4260 0.3635 -0.0005 -0.0191 -0.0130 302 TYR A CG 2319 C CD1 . TYR A 302 ? 0.3881 0.4006 0.3746 0.0000 -0.0065 0.0087 302 TYR A CD1 2320 C CD2 . TYR A 302 ? 0.3642 0.4238 0.3589 -0.0037 -0.0080 -0.0040 302 TYR A CD2 2321 C CE1 . TYR A 302 ? 0.3973 0.4423 0.3849 -0.0020 0.0051 0.0049 302 TYR A CE1 2322 C CE2 . TYR A 302 ? 0.3996 0.4037 0.3949 -0.0027 -0.0064 0.0077 302 TYR A CE2 2323 C CZ . TYR A 302 ? 0.4121 0.4568 0.4076 -0.0019 -0.0138 -0.0017 302 TYR A CZ 2324 O OH . TYR A 302 ? 0.4261 0.4272 0.3781 -0.0259 0.0045 0.0392 302 TYR A OH 2325 N N . SER A 303 ? 0.2528 0.3401 0.2702 0.0051 -0.0053 -0.0038 303 SER A N 2326 C CA . SER A 303 ? 0.2511 0.3259 0.2579 0.0000 -0.0006 0.0014 303 SER A CA 2327 C C . SER A 303 ? 0.2513 0.3251 0.2549 0.0013 -0.0011 0.0048 303 SER A C 2328 O O . SER A 303 ? 0.2549 0.3159 0.2309 0.0065 -0.0048 0.0052 303 SER A O 2329 C CB . SER A 303 ? 0.2409 0.3232 0.2603 -0.0007 0.0024 -0.0075 303 SER A CB 2330 O OG . SER A 303 ? 0.2688 0.3384 0.2773 -0.0059 0.0028 -0.0203 303 SER A OG 2331 N N . VAL A 304 ? 0.2471 0.3240 0.2541 0.0046 0.0030 0.0039 304 VAL A N 2332 C CA . VAL A 304 ? 0.2356 0.3127 0.2486 0.0066 0.0003 0.0083 304 VAL A CA 2333 C C . VAL A 304 ? 0.2409 0.3186 0.2642 0.0053 -0.0010 0.0038 304 VAL A C 2334 O O . VAL A 304 ? 0.2185 0.3254 0.2532 0.0059 -0.0076 0.0083 304 VAL A O 2335 C CB . VAL A 304 ? 0.2410 0.3102 0.2540 0.0006 0.0010 0.0076 304 VAL A CB 2336 C CG1 . VAL A 304 ? 0.2549 0.3050 0.2470 0.0095 0.0022 0.0047 304 VAL A CG1 2337 C CG2 . VAL A 304 ? 0.2138 0.2901 0.2315 0.0098 0.0006 0.0056 304 VAL A CG2 2338 N N . LYS A 305 ? 0.2312 0.3281 0.2759 0.0084 -0.0064 0.0011 305 LYS A N 2339 C CA . LYS A 305 ? 0.2775 0.3467 0.3248 0.0026 0.0034 -0.0006 305 LYS A CA 2340 C C . LYS A 305 ? 0.2370 0.3223 0.2998 0.0111 -0.0041 0.0034 305 LYS A C 2341 O O . LYS A 305 ? 0.2278 0.3133 0.2992 0.0166 0.0000 0.0061 305 LYS A O 2342 C CB . LYS A 305 ? 0.2252 0.3177 0.3154 0.0218 -0.0222 0.0093 305 LYS A CB 2343 C CG . LYS A 305 ? 0.4132 0.4006 0.4497 -0.0239 0.0941 -0.0193 305 LYS A CG 2344 C CD . LYS A 305 ? 0.2065 0.3157 0.3050 0.0292 -0.0646 0.0508 305 LYS A CD 2345 C CE . LYS A 305 ? 0.4789 0.4657 0.5013 -0.0184 0.0912 -0.0264 305 LYS A CE 2346 N NZ . LYS A 305 ? 0.2373 0.4114 0.3200 0.0425 -0.1370 0.0215 305 LYS A NZ 2347 N N . ALA A 306 ? 0.2447 0.3288 0.2843 0.0179 -0.0067 0.0113 306 ALA A N 2348 C CA . ALA A 306 ? 0.2515 0.3170 0.2798 0.0110 -0.0051 0.0075 306 ALA A CA 2349 C C . ALA A 306 ? 0.2553 0.3192 0.2754 0.0131 -0.0042 0.0115 306 ALA A C 2350 O O . ALA A 306 ? 0.2491 0.3184 0.2798 0.0095 -0.0123 0.0147 306 ALA A O 2351 C CB . ALA A 306 ? 0.2581 0.3252 0.2742 0.0099 -0.0081 0.0077 306 ALA A CB 2352 N N . SER A 307 ? 0.2416 0.3125 0.2625 0.0117 -0.0046 0.0137 307 SER A N 2353 C CA . SER A 307 ? 0.2300 0.3034 0.2516 0.0111 -0.0023 0.0139 307 SER A CA 2354 C C . SER A 307 ? 0.2261 0.2917 0.2464 0.0104 0.0021 0.0131 307 SER A C 2355 O O . SER A 307 ? 0.2324 0.2893 0.2368 0.0144 0.0000 0.0175 307 SER A O 2356 C CB . SER A 307 ? 0.2296 0.2930 0.2608 0.0067 -0.0002 0.0139 307 SER A CB 2357 O OG . SER A 307 ? 0.2345 0.3304 0.2664 0.0215 -0.0029 0.0136 307 SER A OG 2358 N N . ILE A 308 ? 0.2253 0.2917 0.2483 0.0145 0.0025 0.0092 308 ILE A N 2359 C CA . ILE A 308 ? 0.2334 0.2913 0.2440 0.0110 0.0097 0.0108 308 ILE A CA 2360 C C . ILE A 308 ? 0.2377 0.3000 0.2488 0.0102 0.0110 0.0118 308 ILE A C 2361 O O . ILE A 308 ? 0.2178 0.3016 0.2496 0.0116 0.0014 0.0174 308 ILE A O 2362 C CB . ILE A 308 ? 0.2448 0.2879 0.2537 0.0081 0.0081 0.0103 308 ILE A CB 2363 C CG1 . ILE A 308 ? 0.2149 0.2846 0.2529 0.0035 0.0046 0.0119 308 ILE A CG1 2364 C CG2 . ILE A 308 ? 0.2666 0.3024 0.2490 0.0155 0.0057 -0.0012 308 ILE A CG2 2365 C CD1 . ILE A 308 ? 0.2241 0.2850 0.2626 -0.0036 0.0046 0.0245 308 ILE A CD1 2366 N N . LEU A 309 ? 0.2461 0.3069 0.2566 0.0095 0.0066 0.0152 309 LEU A N 2367 C CA . LEU A 309 ? 0.2456 0.3062 0.2702 0.0092 0.0070 0.0153 309 LEU A CA 2368 C C . LEU A 309 ? 0.2473 0.2996 0.2643 0.0108 0.0050 0.0129 309 LEU A C 2369 O O . LEU A 309 ? 0.2539 0.3109 0.2908 0.0220 0.0153 0.0141 309 LEU A O 2370 C CB . LEU A 309 ? 0.2423 0.3085 0.2694 0.0076 0.0094 0.0163 309 LEU A CB 2371 C CG . LEU A 309 ? 0.2505 0.3095 0.2865 0.0124 0.0123 0.0051 309 LEU A CG 2372 C CD1 . LEU A 309 ? 0.2650 0.3311 0.2847 0.0133 -0.0046 0.0132 309 LEU A CD1 2373 C CD2 . LEU A 309 ? 0.2594 0.3092 0.2707 0.0096 -0.0095 0.0118 309 LEU A CD2 2374 N N . ALA A 310 ? 0.2478 0.3025 0.2622 0.0151 0.0017 0.0166 310 ALA A N 2375 C CA . ALA A 310 ? 0.2538 0.2894 0.2540 0.0157 0.0049 0.0106 310 ALA A CA 2376 C C . ALA A 310 ? 0.2528 0.2902 0.2598 0.0159 0.0046 0.0143 310 ALA A C 2377 O O . ALA A 310 ? 0.2595 0.3042 0.2588 0.0200 0.0005 0.0183 310 ALA A O 2378 C CB . ALA A 310 ? 0.2668 0.2935 0.2667 0.0143 0.0127 0.0088 310 ALA A CB 2379 N N . GLY A 311 ? 0.2425 0.2833 0.2508 0.0196 0.0050 0.0104 311 GLY A N 2380 C CA . GLY A 311 ? 0.2447 0.2718 0.2393 0.0244 0.0021 0.0113 311 GLY A CA 2381 C C . GLY A 311 ? 0.2371 0.2698 0.2340 0.0198 0.0038 0.0120 311 GLY A C 2382 O O . GLY A 311 ? 0.2510 0.2610 0.2280 0.0180 0.0047 0.0141 311 GLY A O 2383 N N . LEU A 312 ? 0.2340 0.2738 0.2265 0.0248 0.0053 0.0106 312 LEU A N 2384 C CA . LEU A 312 ? 0.2365 0.2662 0.2173 0.0196 0.0018 0.0110 312 LEU A CA 2385 C C . LEU A 312 ? 0.2195 0.2685 0.2177 0.0184 0.0067 0.0079 312 LEU A C 2386 O O . LEU A 312 ? 0.2021 0.2951 0.2180 0.0231 0.0081 0.0205 312 LEU A O 2387 C CB . LEU A 312 ? 0.2373 0.2652 0.2042 0.0138 0.0097 0.0134 312 LEU A CB 2388 C CG . LEU A 312 ? 0.2483 0.2592 0.2275 0.0307 0.0086 -0.0039 312 LEU A CG 2389 C CD1 . LEU A 312 ? 0.2470 0.2828 0.2012 0.0128 0.0069 0.0021 312 LEU A CD1 2390 C CD2 . LEU A 312 ? 0.2631 0.2648 0.2249 0.0131 0.0038 0.0091 312 LEU A CD2 2391 N N . ASP A 313 ? 0.2015 0.2566 0.2144 0.0188 0.0007 0.0037 313 ASP A N 2392 C CA . ASP A 313 ? 0.2072 0.2480 0.2229 0.0154 0.0027 0.0019 313 ASP A CA 2393 C C . ASP A 313 ? 0.2006 0.2471 0.2163 0.0110 0.0080 0.0076 313 ASP A C 2394 O O . ASP A 313 ? 0.1972 0.2599 0.2322 0.0196 0.0114 0.0111 313 ASP A O 2395 C CB . ASP A 313 ? 0.2111 0.2502 0.2340 0.0069 0.0123 0.0062 313 ASP A CB 2396 C CG . ASP A 313 ? 0.2207 0.2464 0.2338 0.0182 0.0107 -0.0005 313 ASP A CG 2397 O OD1 . ASP A 313 ? 0.2268 0.2781 0.2434 0.0290 0.0095 -0.0011 313 ASP A OD1 2398 O OD2 . ASP A 313 ? 0.2092 0.2572 0.2453 0.0226 0.0290 0.0129 313 ASP A OD2 2399 N N . MET A 314 ? 0.1973 0.2420 0.2080 0.0093 0.0053 0.0042 314 MET A N 2400 C CA . MET A 314 ? 0.2054 0.2451 0.2084 0.0020 0.0086 0.0072 314 MET A CA 2401 C C . MET A 314 ? 0.2086 0.2523 0.2044 0.0023 0.0073 0.0087 314 MET A C 2402 O O . MET A 314 ? 0.2242 0.2659 0.2010 0.0037 0.0121 0.0102 314 MET A O 2403 C CB . MET A 314 ? 0.2109 0.2451 0.2068 0.0069 0.0014 0.0212 314 MET A CB 2404 C CG . MET A 314 ? 0.2273 0.2277 0.2308 0.0006 -0.0044 0.0110 314 MET A CG 2405 S SD . MET A 314 ? 0.2194 0.2775 0.2235 -0.0117 0.0089 0.0141 314 MET A SD 2406 C CE . MET A 314 ? 0.2634 0.2588 0.2351 -0.0179 -0.0065 0.0073 314 MET A CE 2407 N N . ILE A 315 ? 0.1873 0.2365 0.1897 0.0045 0.0098 0.0040 315 ILE A N 2408 C CA . ILE A 315 ? 0.1981 0.2391 0.2028 -0.0015 0.0093 0.0089 315 ILE A CA 2409 C C . ILE A 315 ? 0.1994 0.2453 0.2040 0.0004 0.0081 0.0042 315 ILE A C 2410 O O . ILE A 315 ? 0.2192 0.2516 0.1983 0.0045 0.0154 0.0084 315 ILE A O 2411 C CB . ILE A 315 ? 0.1999 0.2430 0.2024 0.0049 0.0130 0.0048 315 ILE A CB 2412 C CG1 . ILE A 315 ? 0.2097 0.2548 0.1787 -0.0016 -0.0060 0.0175 315 ILE A CG1 2413 C CG2 . ILE A 315 ? 0.2248 0.2439 0.2231 -0.0090 0.0059 0.0066 315 ILE A CG2 2414 C CD1 . ILE A 315 ? 0.2405 0.2478 0.1908 -0.0029 0.0049 0.0204 315 ILE A CD1 2415 N N . MET A 316 ? 0.1940 0.2451 0.1930 0.0019 0.0157 0.0042 316 MET A N 2416 C CA . MET A 316 ? 0.1954 0.2469 0.1967 0.0000 0.0139 0.0047 316 MET A CA 2417 C C . MET A 316 ? 0.1988 0.2486 0.1958 -0.0064 0.0089 -0.0001 316 MET A C 2418 O O . MET A 316 ? 0.1867 0.2539 0.2022 -0.0097 0.0038 0.0087 316 MET A O 2419 C CB . MET A 316 ? 0.2074 0.2548 0.1855 0.0076 0.0185 0.0006 316 MET A CB 2420 C CG . MET A 316 ? 0.2111 0.2379 0.1968 0.0066 0.0095 0.0088 316 MET A CG 2421 S SD . MET A 316 ? 0.2163 0.2914 0.1969 0.0104 0.0091 0.0015 316 MET A SD 2422 C CE . MET A 316 ? 0.2184 0.2799 0.2322 -0.0033 0.0145 0.0032 316 MET A CE 2423 N N . VAL A 317 ? 0.2078 0.2465 0.2040 -0.0191 0.0011 0.0051 317 VAL A N 2424 C CA . VAL A 317 ? 0.2274 0.2577 0.2158 -0.0197 0.0029 0.0057 317 VAL A CA 2425 C C . VAL A 317 ? 0.2239 0.2582 0.2204 -0.0125 0.0021 0.0075 317 VAL A C 2426 O O . VAL A 317 ? 0.2376 0.2641 0.2247 -0.0193 -0.0073 0.0056 317 VAL A O 2427 C CB . VAL A 317 ? 0.2237 0.2542 0.2216 -0.0202 0.0102 0.0030 317 VAL A CB 2428 C CG1 . VAL A 317 ? 0.2395 0.2742 0.2435 -0.0296 0.0072 0.0041 317 VAL A CG1 2429 C CG2 . VAL A 317 ? 0.2353 0.2535 0.2088 -0.0172 0.0085 -0.0058 317 VAL A CG2 2430 N N . PRO A 318 ? 0.2340 0.2528 0.2202 -0.0083 -0.0065 0.0143 318 PRO A N 2431 C CA . PRO A 318 ? 0.2231 0.2553 0.2228 -0.0082 -0.0058 0.0183 318 PRO A CA 2432 C C . PRO A 318 ? 0.2300 0.2809 0.2350 -0.0149 0.0004 0.0184 318 PRO A C 2433 O O . PRO A 318 ? 0.2329 0.2798 0.2223 -0.0254 0.0074 0.0180 318 PRO A O 2434 C CB . PRO A 318 ? 0.2305 0.2612 0.2203 -0.0029 -0.0028 0.0086 318 PRO A CB 2435 C CG . PRO A 318 ? 0.2280 0.2644 0.2268 0.0075 -0.0092 0.0056 318 PRO A CG 2436 C CD . PRO A 318 ? 0.2202 0.2622 0.2133 -0.0008 -0.0030 0.0157 318 PRO A CD 2437 N N . ASN A 319 ? 0.2532 0.2766 0.2455 -0.0185 -0.0033 0.0116 319 ASN A N 2438 C CA . ASN A 319 ? 0.2522 0.2910 0.2670 -0.0125 0.0000 0.0117 319 ASN A CA 2439 C C . ASN A 319 ? 0.2664 0.3071 0.2747 -0.0087 0.0023 0.0079 319 ASN A C 2440 O O . ASN A 319 ? 0.2684 0.3192 0.2762 -0.0055 -0.0017 0.0121 319 ASN A O 2441 C CB . ASN A 319 ? 0.2614 0.2930 0.2666 -0.0098 0.0045 0.0116 319 ASN A CB 2442 C CG . ASN A 319 ? 0.2840 0.2834 0.2808 -0.0027 -0.0031 0.0103 319 ASN A CG 2443 O OD1 . ASN A 319 ? 0.2699 0.3047 0.3021 -0.0156 -0.0084 0.0050 319 ASN A OD1 2444 N ND2 . ASN A 319 ? 0.3177 0.3127 0.2806 -0.0096 0.0020 -0.0015 319 ASN A ND2 2445 N N . LYS A 320 ? 0.2622 0.3146 0.2840 -0.0079 -0.0006 0.0036 320 LYS A N 2446 C CA . LYS A 320 ? 0.2591 0.3253 0.2894 -0.0138 -0.0051 0.0022 320 LYS A CA 2447 C C . LYS A 320 ? 0.2499 0.3215 0.2783 -0.0139 0.0007 0.0065 320 LYS A C 2448 O O . LYS A 320 ? 0.2574 0.3306 0.2607 -0.0182 -0.0099 0.0124 320 LYS A O 2449 C CB A LYS A 320 ? 0.2718 0.3314 0.2966 -0.0124 -0.0021 0.0026 320 LYS A CB 2450 C CB B LYS A 320 ? 0.3097 0.3419 0.3288 0.0036 -0.0273 -0.0104 320 LYS A CB 2451 C CG A LYS A 320 ? 0.3054 0.3282 0.3202 -0.0079 -0.0070 -0.0012 320 LYS A CG 2452 C CG B LYS A 320 ? 0.2576 0.3146 0.2788 -0.0145 0.0115 0.0133 320 LYS A CG 2453 C CD A LYS A 320 ? 0.3507 0.3698 0.3547 -0.0035 0.0073 -0.0064 320 LYS A CD 2454 C CD B LYS A 320 ? 0.3815 0.4046 0.3427 0.0835 -0.0573 -0.0389 320 LYS A CD 2455 C CE A LYS A 320 ? 0.4014 0.3777 0.3830 -0.0132 0.0106 -0.0051 320 LYS A CE 2456 C CE B LYS A 320 ? 0.2000 0.2233 0.2965 -0.0673 0.0775 0.0389 320 LYS A CE 2457 N NZ A LYS A 320 ? 0.3536 0.3799 0.3713 0.0103 -0.0139 0.0067 320 LYS A NZ 2458 N NZ B LYS A 320 ? 0.4133 0.3930 0.3909 -0.0303 -0.0367 0.0053 320 LYS A NZ 2459 N N . TYR A 321 ? 0.2503 0.3230 0.2708 -0.0154 -0.0027 0.0029 321 TYR A N 2460 C CA . TYR A 321 ? 0.2482 0.3128 0.2745 -0.0150 -0.0051 0.0035 321 TYR A CA 2461 C C . TYR A 321 ? 0.2467 0.3071 0.2715 -0.0114 -0.0073 0.0072 321 TYR A C 2462 O O . TYR A 321 ? 0.2346 0.3104 0.2742 -0.0146 -0.0024 0.0158 321 TYR A O 2463 C CB . TYR A 321 ? 0.2523 0.3212 0.2801 -0.0120 -0.0100 0.0038 321 TYR A CB 2464 C CG . TYR A 321 ? 0.2604 0.3199 0.2771 -0.0209 -0.0066 -0.0009 321 TYR A CG 2465 C CD1 . TYR A 321 ? 0.2516 0.3270 0.2644 -0.0110 -0.0087 -0.0046 321 TYR A CD1 2466 C CD2 . TYR A 321 ? 0.2564 0.3064 0.2767 -0.0153 -0.0102 0.0054 321 TYR A CD2 2467 C CE1 . TYR A 321 ? 0.2519 0.3142 0.2756 -0.0115 -0.0246 -0.0014 321 TYR A CE1 2468 C CE2 . TYR A 321 ? 0.2939 0.3275 0.2829 -0.0138 -0.0163 -0.0016 321 TYR A CE2 2469 C CZ . TYR A 321 ? 0.2888 0.3205 0.2846 -0.0078 -0.0089 0.0005 321 TYR A CZ 2470 O OH . TYR A 321 ? 0.3193 0.3625 0.3043 -0.0170 0.0038 0.0210 321 TYR A OH 2471 N N . GLN A 322 ? 0.2338 0.3092 0.2735 -0.0119 -0.0043 0.0147 322 GLN A N 2472 C CA . GLN A 322 ? 0.2570 0.3088 0.2950 -0.0079 -0.0009 0.0166 322 GLN A CA 2473 C C . GLN A 322 ? 0.2478 0.3083 0.2867 -0.0131 -0.0003 0.0172 322 GLN A C 2474 O O . GLN A 322 ? 0.2529 0.3230 0.3034 -0.0135 -0.0124 0.0340 322 GLN A O 2475 C CB A GLN A 322 ? 0.2540 0.3025 0.2888 -0.0042 0.0039 0.0159 322 GLN A CB 2476 C CB B GLN A 322 ? 0.2559 0.3037 0.2895 -0.0051 0.0051 0.0144 322 GLN A CB 2477 C CG A GLN A 322 ? 0.2648 0.3075 0.3033 -0.0018 0.0094 0.0184 322 GLN A CG 2478 C CG B GLN A 322 ? 0.2725 0.3070 0.3011 -0.0042 0.0019 0.0132 322 GLN A CG 2479 C CD A GLN A 322 ? 0.2725 0.2996 0.3024 -0.0058 0.0013 0.0153 322 GLN A CD 2480 C CD B GLN A 322 ? 0.3163 0.3255 0.3308 0.0002 0.0049 0.0098 322 GLN A CD 2481 O OE1 A GLN A 322 ? 0.3014 0.3150 0.3173 0.0077 0.0098 0.0189 322 GLN A OE1 2482 O OE1 B GLN A 322 ? 0.2450 0.3031 0.3023 -0.0073 -0.0010 0.0117 322 GLN A OE1 2483 N NE2 A GLN A 322 ? 0.2728 0.3005 0.3010 0.0092 0.0256 0.0031 322 GLN A NE2 2484 N NE2 B GLN A 322 ? 0.3435 0.3190 0.3600 0.0033 0.0032 0.0174 322 GLN A NE2 2485 N N . GLN A 323 ? 0.2548 0.3216 0.3033 -0.0171 -0.0101 0.0147 323 GLN A N 2486 C CA . GLN A 323 ? 0.2740 0.3306 0.2906 -0.0091 -0.0091 0.0063 323 GLN A CA 2487 C C . GLN A 323 ? 0.2551 0.3257 0.2779 -0.0085 -0.0092 0.0003 323 GLN A C 2488 O O . GLN A 323 ? 0.2426 0.3340 0.2910 -0.0119 -0.0056 -0.0015 323 GLN A O 2489 C CB . GLN A 323 ? 0.3010 0.3444 0.3129 -0.0119 -0.0154 0.0040 323 GLN A CB 2490 C CG . GLN A 323 ? 0.3653 0.4091 0.4121 0.0017 -0.0219 0.0284 323 GLN A CG 2491 C CD . GLN A 323 ? 0.3157 0.4583 0.3648 0.0252 -0.0231 -0.0486 323 GLN A CD 2492 O OE1 . GLN A 323 ? 0.5500 0.5378 0.5328 -0.0215 -0.0346 0.0044 323 GLN A OE1 2493 N NE2 . GLN A 323 ? 0.5234 0.4842 0.5103 0.0045 0.0241 -0.0004 323 GLN A NE2 2494 N N . PHE A 324 ? 0.2329 0.3096 0.2553 -0.0098 -0.0034 -0.0003 324 PHE A N 2495 C CA . PHE A 324 ? 0.2159 0.3008 0.2426 -0.0063 -0.0005 0.0035 324 PHE A CA 2496 C C . PHE A 324 ? 0.2025 0.2965 0.2311 -0.0045 -0.0006 0.0075 324 PHE A C 2497 O O . PHE A 324 ? 0.2030 0.2924 0.2116 -0.0033 0.0035 0.0035 324 PHE A O 2498 C CB . PHE A 324 ? 0.2138 0.2943 0.2508 -0.0054 0.0016 0.0043 324 PHE A CB 2499 C CG . PHE A 324 ? 0.2207 0.2909 0.2477 0.0001 0.0082 0.0078 324 PHE A CG 2500 C CD1 . PHE A 324 ? 0.2038 0.2813 0.2449 0.0089 0.0141 0.0124 324 PHE A CD1 2501 C CD2 . PHE A 324 ? 0.2252 0.2687 0.2291 -0.0057 0.0046 0.0005 324 PHE A CD2 2502 C CE1 . PHE A 324 ? 0.2141 0.2806 0.2296 -0.0049 0.0169 0.0069 324 PHE A CE1 2503 C CE2 . PHE A 324 ? 0.2233 0.2859 0.2306 -0.0020 0.0121 0.0088 324 PHE A CE2 2504 C CZ . PHE A 324 ? 0.2244 0.2876 0.2411 -0.0062 0.0082 0.0098 324 PHE A CZ 2505 N N . ILE A 325 ? 0.2077 0.3080 0.2356 -0.0065 0.0007 0.0084 325 ILE A N 2506 C CA . ILE A 325 ? 0.2041 0.3145 0.2318 0.0031 0.0000 0.0074 325 ILE A CA 2507 C C . ILE A 325 ? 0.2085 0.3105 0.2333 -0.0034 0.0063 0.0099 325 ILE A C 2508 O O . ILE A 325 ? 0.1859 0.3197 0.2123 0.0032 0.0183 0.0028 325 ILE A O 2509 C CB . ILE A 325 ? 0.1999 0.3112 0.2338 0.0005 -0.0065 0.0054 325 ILE A CB 2510 C CG1 . ILE A 325 ? 0.2031 0.3230 0.2304 0.0056 0.0008 0.0096 325 ILE A CG1 2511 C CG2 . ILE A 325 ? 0.2138 0.3271 0.2499 -0.0069 -0.0039 -0.0024 325 ILE A CG2 2512 C CD1 . ILE A 325 ? 0.2169 0.3094 0.2406 0.0091 -0.0078 0.0118 325 ILE A CD1 2513 N N . SER A 326 ? 0.2121 0.3201 0.2324 -0.0045 0.0108 0.0078 326 SER A N 2514 C CA . SER A 326 ? 0.2101 0.3167 0.2496 -0.0079 0.0040 0.0107 326 SER A CA 2515 C C . SER A 326 ? 0.2217 0.3205 0.2456 -0.0038 0.0028 0.0055 326 SER A C 2516 O O . SER A 326 ? 0.2394 0.3278 0.2371 0.0008 -0.0005 0.0175 326 SER A O 2517 C CB . SER A 326 ? 0.2047 0.3186 0.2689 -0.0057 0.0099 0.0118 326 SER A CB 2518 O OG . SER A 326 ? 0.1987 0.3530 0.2950 -0.0167 0.0146 0.0174 326 SER A OG 2519 N N . ILE A 327 ? 0.2228 0.3230 0.2422 -0.0044 0.0027 0.0097 327 ILE A N 2520 C CA . ILE A 327 ? 0.2360 0.3204 0.2463 -0.0009 0.0035 0.0048 327 ILE A CA 2521 C C . ILE A 327 ? 0.2299 0.3188 0.2431 0.0019 0.0035 0.0010 327 ILE A C 2522 O O . ILE A 327 ? 0.2242 0.3292 0.2541 0.0002 -0.0002 0.0005 327 ILE A O 2523 C CB . ILE A 327 ? 0.2462 0.3169 0.2502 0.0033 0.0058 0.0035 327 ILE A CB 2524 C CG1 . ILE A 327 ? 0.2728 0.3161 0.2748 -0.0008 0.0039 -0.0075 327 ILE A CG1 2525 C CG2 . ILE A 327 ? 0.2566 0.3207 0.2591 0.0047 -0.0042 0.0079 327 ILE A CG2 2526 C CD1 . ILE A 327 ? 0.3423 0.3709 0.3109 0.0062 0.0098 -0.0051 327 ILE A CD1 2527 N N . LEU A 328 ? 0.2124 0.3132 0.2349 -0.0049 -0.0001 -0.0007 328 LEU A N 2528 C CA . LEU A 328 ? 0.2011 0.3090 0.2383 -0.0009 0.0040 -0.0007 328 LEU A CA 2529 C C . LEU A 328 ? 0.2145 0.3125 0.2390 -0.0010 0.0016 0.0022 328 LEU A C 2530 O O . LEU A 328 ? 0.2085 0.3210 0.2306 0.0058 0.0064 0.0044 328 LEU A O 2531 C CB . LEU A 328 ? 0.1983 0.3028 0.2361 -0.0002 -0.0111 0.0007 328 LEU A CB 2532 C CG . LEU A 328 ? 0.1921 0.2967 0.2411 0.0030 -0.0024 0.0103 328 LEU A CG 2533 C CD1 . LEU A 328 ? 0.2193 0.3335 0.2582 0.0134 -0.0086 0.0226 328 LEU A CD1 2534 C CD2 . LEU A 328 ? 0.1954 0.3189 0.2537 -0.0133 -0.0070 -0.0044 328 LEU A CD2 2535 N N . THR A 329 ? 0.2003 0.3235 0.2265 -0.0013 -0.0007 0.0037 329 THR A N 2536 C CA . THR A 329 ? 0.2138 0.3309 0.2450 0.0053 0.0031 0.0094 329 THR A CA 2537 C C . THR A 329 ? 0.2147 0.3283 0.2524 0.0027 0.0055 0.0121 329 THR A C 2538 O O . THR A 329 ? 0.2211 0.3341 0.2549 0.0004 0.0070 0.0214 329 THR A O 2539 C CB . THR A 329 ? 0.2161 0.3286 0.2389 0.0103 0.0018 0.0067 329 THR A CB 2540 O OG1 . THR A 329 ? 0.2073 0.3505 0.2445 -0.0030 0.0064 0.0136 329 THR A OG1 2541 C CG2 . THR A 329 ? 0.2311 0.3307 0.2508 0.0029 0.0143 0.0010 329 THR A CG2 2542 N N . GLY A 330 ? 0.2174 0.3373 0.2523 -0.0047 -0.0003 0.0188 330 GLY A N 2543 C CA . GLY A 330 ? 0.2262 0.3388 0.2784 0.0021 -0.0006 0.0137 330 GLY A CA 2544 C C . GLY A 330 ? 0.2402 0.3389 0.2844 0.0037 0.0011 0.0099 330 GLY A C 2545 O O . GLY A 330 ? 0.2251 0.3447 0.2931 0.0055 0.0089 0.0134 330 GLY A O 2546 N N . HIS A 331 ? 0.2342 0.3393 0.2884 0.0024 0.0051 0.0095 331 HIS A N 2547 C CA . HIS A 331 ? 0.2541 0.3422 0.2933 0.0012 0.0055 0.0008 331 HIS A CA 2548 C C . HIS A 331 ? 0.2456 0.3368 0.2876 0.0050 0.0097 0.0000 331 HIS A C 2549 O O . HIS A 331 ? 0.2579 0.3554 0.2946 0.0075 -0.0026 0.0023 331 HIS A O 2550 C CB . HIS A 331 ? 0.2566 0.3395 0.2918 0.0026 0.0052 -0.0012 331 HIS A CB 2551 C CG . HIS A 331 ? 0.3085 0.3577 0.3059 0.0034 0.0051 -0.0079 331 HIS A CG 2552 N ND1 . HIS A 331 ? 0.3350 0.3732 0.3508 0.0023 0.0020 -0.0132 331 HIS A ND1 2553 C CD2 . HIS A 331 ? 0.3126 0.3773 0.3149 0.0044 -0.0016 -0.0135 331 HIS A CD2 2554 C CE1 . HIS A 331 ? 0.3042 0.3641 0.3157 0.0084 -0.0015 -0.0099 331 HIS A CE1 2555 N NE2 . HIS A 331 ? 0.3656 0.4137 0.3610 0.0049 -0.0015 -0.0148 331 HIS A NE2 2556 N N . VAL A 332 ? 0.2284 0.3326 0.2770 0.0068 0.0134 -0.0015 332 VAL A N 2557 C CA . VAL A 332 ? 0.2265 0.3376 0.2828 0.0047 0.0119 -0.0028 332 VAL A CA 2558 C C . VAL A 332 ? 0.2348 0.3397 0.2932 0.0103 0.0121 -0.0044 332 VAL A C 2559 O O . VAL A 332 ? 0.2310 0.3542 0.3009 0.0082 0.0152 0.0079 332 VAL A O 2560 C CB . VAL A 332 ? 0.2320 0.3354 0.2761 0.0065 0.0077 -0.0076 332 VAL A CB 2561 C CG1 . VAL A 332 ? 0.2460 0.3289 0.2922 0.0050 0.0050 -0.0097 332 VAL A CG1 2562 C CG2 . VAL A 332 ? 0.2088 0.3171 0.2655 -0.0030 0.0088 0.0047 332 VAL A CG2 2563 N N . ASN A 333 ? 0.2510 0.3566 0.3030 0.0108 0.0101 -0.0039 333 ASN A N 2564 C CA . ASN A 333 ? 0.2720 0.3688 0.3257 0.0091 0.0117 0.0003 333 ASN A CA 2565 C C . ASN A 333 ? 0.2879 0.3819 0.3424 0.0135 0.0054 -0.0036 333 ASN A C 2566 O O . ASN A 333 ? 0.2912 0.3936 0.3492 0.0217 0.0123 -0.0041 333 ASN A O 2567 C CB . ASN A 333 ? 0.2808 0.3654 0.3247 0.0111 0.0084 -0.0022 333 ASN A CB 2568 C CG . ASN A 333 ? 0.2901 0.3562 0.3181 0.0016 0.0193 -0.0077 333 ASN A CG 2569 O OD1 . ASN A 333 ? 0.3137 0.3581 0.3042 -0.0063 0.0185 -0.0229 333 ASN A OD1 2570 N ND2 . ASN A 333 ? 0.2881 0.3392 0.3076 -0.0128 0.0320 0.0008 333 ASN A ND2 2571 N N . GLY A 334 ? 0.2935 0.3875 0.3475 0.0071 0.0053 -0.0022 334 GLY A N 2572 C CA . GLY A 334 ? 0.3086 0.3898 0.3654 0.0070 -0.0045 0.0004 334 GLY A CA 2573 C C . GLY A 334 ? 0.3254 0.4000 0.3824 0.0047 -0.0098 0.0038 334 GLY A C 2574 O O . GLY A 334 ? 0.3191 0.4094 0.4053 -0.0003 -0.0215 0.0036 334 GLY A O 2575 N N . GLY A 335 ? 0.3199 0.3964 0.3810 0.0025 -0.0108 0.0055 335 GLY A N 2576 C CA . GLY A 335 ? 0.3306 0.3943 0.3931 0.0070 -0.0110 0.0068 335 GLY A CA 2577 C C . GLY A 335 ? 0.3366 0.3915 0.3893 0.0039 -0.0145 0.0091 335 GLY A C 2578 O O . GLY A 335 ? 0.3516 0.3999 0.4119 0.0092 -0.0191 0.0136 335 GLY A O 2579 N N . VAL A 336 ? 0.3194 0.3892 0.3761 0.0080 -0.0144 0.0084 336 VAL A N 2580 C CA . VAL A 336 ? 0.3270 0.3881 0.3655 0.0060 -0.0149 0.0122 336 VAL A CA 2581 C C . VAL A 336 ? 0.3146 0.3812 0.3479 0.0118 -0.0104 0.0134 336 VAL A C 2582 O O . VAL A 336 ? 0.3064 0.3852 0.3390 0.0164 -0.0189 0.0221 336 VAL A O 2583 C CB . VAL A 336 ? 0.3389 0.3949 0.3645 0.0059 -0.0125 0.0079 336 VAL A CB 2584 C CG1 . VAL A 336 ? 0.3650 0.4025 0.3889 0.0009 -0.0072 0.0028 336 VAL A CG1 2585 C CG2 . VAL A 336 ? 0.3697 0.4157 0.3961 -0.0090 -0.0145 0.0107 336 VAL A CG2 2586 N N . ILE A 337 ? 0.2932 0.3649 0.3232 0.0058 -0.0114 0.0112 337 ILE A N 2587 C CA . ILE A 337 ? 0.2893 0.3474 0.3136 0.0099 -0.0089 0.0071 337 ILE A CA 2588 C C . ILE A 337 ? 0.2662 0.3405 0.3073 0.0116 -0.0067 0.0062 337 ILE A C 2589 O O . ILE A 337 ? 0.2716 0.3567 0.3001 0.0136 -0.0168 0.0097 337 ILE A O 2590 C CB . ILE A 337 ? 0.2807 0.3335 0.2966 0.0075 -0.0043 0.0037 337 ILE A CB 2591 C CG1 . ILE A 337 ? 0.2818 0.3264 0.3238 0.0032 -0.0131 -0.0045 337 ILE A CG1 2592 C CG2 . ILE A 337 ? 0.2830 0.3432 0.3036 0.0088 -0.0033 0.0085 337 ILE A CG2 2593 C CD1 . ILE A 337 ? 0.3105 0.3342 0.3212 0.0062 -0.0125 -0.0033 337 ILE A CD1 2594 N N . PRO A 338 ? 0.2663 0.3367 0.3040 0.0165 -0.0048 0.0074 338 PRO A N 2595 C CA . PRO A 338 ? 0.2758 0.3372 0.3007 0.0115 0.0023 0.0023 338 PRO A CA 2596 C C . PRO A 338 ? 0.2877 0.3366 0.2993 0.0095 0.0006 0.0015 338 PRO A C 2597 O O . PRO A 338 ? 0.2795 0.3319 0.2811 0.0046 0.0018 -0.0098 338 PRO A O 2598 C CB . PRO A 338 ? 0.2777 0.3334 0.2996 0.0147 0.0046 0.0036 338 PRO A CB 2599 C CG . PRO A 338 ? 0.2904 0.3344 0.3017 0.0117 0.0000 0.0002 338 PRO A CG 2600 C CD . PRO A 338 ? 0.2725 0.3298 0.2979 0.0121 0.0029 0.0063 338 PRO A CD 2601 N N . MET A 339 ? 0.2911 0.3474 0.3031 0.0099 0.0091 -0.0024 339 MET A N 2602 C CA . MET A 339 ? 0.3117 0.3531 0.3187 0.0090 0.0091 -0.0014 339 MET A CA 2603 C C . MET A 339 ? 0.3011 0.3391 0.3055 0.0105 0.0148 0.0016 339 MET A C 2604 O O . MET A 339 ? 0.2924 0.3453 0.3099 0.0110 0.0245 -0.0015 339 MET A O 2605 C CB . MET A 339 ? 0.3237 0.3665 0.3281 0.0115 0.0172 -0.0057 339 MET A CB 2606 C CG . MET A 339 ? 0.4066 0.4106 0.3771 0.0148 0.0134 0.0075 339 MET A CG 2607 S SD . MET A 339 ? 0.4890 0.4724 0.4315 0.0491 0.0385 -0.0013 339 MET A SD 2608 C CE . MET A 339 ? 0.4291 0.4545 0.3944 0.0158 0.0197 0.0128 339 MET A CE 2609 N N . SER A 340 ? 0.2942 0.3312 0.3118 0.0134 0.0158 0.0000 340 SER A N 2610 C CA . SER A 340 ? 0.2998 0.3207 0.3088 0.0158 0.0138 0.0022 340 SER A CA 2611 C C . SER A 340 ? 0.2955 0.3148 0.3020 0.0132 0.0093 -0.0018 340 SER A C 2612 O O . SER A 340 ? 0.2957 0.3234 0.3145 0.0223 0.0138 -0.0064 340 SER A O 2613 C CB . SER A 340 ? 0.3016 0.3075 0.3148 0.0134 0.0091 -0.0011 340 SER A CB 2614 O OG . SER A 340 ? 0.3070 0.3353 0.3134 0.0251 0.0138 0.0068 340 SER A OG 2615 N N . ARG A 341 ? 0.2899 0.3051 0.2934 0.0187 0.0099 0.0018 341 ARG A N 2616 C CA . ARG A 341 ? 0.2800 0.3068 0.2771 0.0120 0.0105 0.0017 341 ARG A CA 2617 C C . ARG A 341 ? 0.2700 0.3014 0.2728 0.0100 0.0145 0.0067 341 ARG A C 2618 O O . ARG A 341 ? 0.2674 0.3137 0.2614 0.0067 0.0121 0.0134 341 ARG A O 2619 C CB . ARG A 341 ? 0.2887 0.3009 0.2863 0.0128 0.0081 -0.0028 341 ARG A CB 2620 C CG . ARG A 341 ? 0.2797 0.3006 0.2735 0.0076 0.0107 -0.0003 341 ARG A CG 2621 C CD . ARG A 341 ? 0.2700 0.2895 0.2758 0.0083 0.0016 0.0030 341 ARG A CD 2622 N NE . ARG A 341 ? 0.2647 0.3155 0.2811 0.0219 0.0152 0.0126 341 ARG A NE 2623 C CZ . ARG A 341 ? 0.2635 0.3054 0.2551 0.0140 0.0102 0.0077 341 ARG A CZ 2624 N NH1 . ARG A 341 ? 0.2470 0.2924 0.2497 0.0462 0.0214 0.0120 341 ARG A NH1 2625 N NH2 . ARG A 341 ? 0.2365 0.3136 0.2539 0.0237 0.0245 0.0155 341 ARG A NH2 2626 N N . ILE A 342 ? 0.2574 0.3030 0.2665 0.0078 0.0137 0.0097 342 ILE A N 2627 C CA . ILE A 342 ? 0.2381 0.2882 0.2618 0.0052 0.0163 0.0098 342 ILE A CA 2628 C C . ILE A 342 ? 0.2447 0.2824 0.2615 0.0029 0.0178 0.0068 342 ILE A C 2629 O O . ILE A 342 ? 0.2153 0.2797 0.2698 0.0016 0.0216 0.0035 342 ILE A O 2630 C CB . ILE A 342 ? 0.2437 0.2842 0.2547 0.0028 0.0153 0.0078 342 ILE A CB 2631 C CG1 . ILE A 342 ? 0.2378 0.2895 0.2605 -0.0045 0.0226 -0.0026 342 ILE A CG1 2632 C CG2 . ILE A 342 ? 0.2463 0.2870 0.2590 0.0097 0.0099 0.0056 342 ILE A CG2 2633 C CD1 . ILE A 342 ? 0.2584 0.2950 0.2665 -0.0128 0.0131 -0.0075 342 ILE A CD1 2634 N N . ASP A 343 ? 0.2354 0.2861 0.2606 0.0088 0.0250 0.0038 343 ASP A N 2635 C CA . ASP A 343 ? 0.2420 0.2955 0.2667 0.0072 0.0246 0.0012 343 ASP A CA 2636 C C . ASP A 343 ? 0.2459 0.3035 0.2664 0.0092 0.0212 0.0038 343 ASP A C 2637 O O . ASP A 343 ? 0.2344 0.3154 0.2622 0.0011 0.0262 0.0036 343 ASP A O 2638 C CB . ASP A 343 ? 0.2559 0.3044 0.2772 0.0111 0.0246 0.0008 343 ASP A CB 2639 C CG . ASP A 343 ? 0.2670 0.3161 0.2860 0.0165 0.0247 0.0000 343 ASP A CG 2640 O OD1 . ASP A 343 ? 0.2625 0.3229 0.2781 0.0144 0.0526 -0.0037 343 ASP A OD1 2641 O OD2 . ASP A 343 ? 0.2734 0.3401 0.3058 0.0260 0.0319 -0.0199 343 ASP A OD2 2642 N N . ASP A 344 ? 0.2471 0.2946 0.2573 0.0099 0.0286 0.0008 344 ASP A N 2643 C CA . ASP A 344 ? 0.2558 0.2923 0.2623 0.0107 0.0211 0.0036 344 ASP A CA 2644 C C . ASP A 344 ? 0.2551 0.2876 0.2591 0.0093 0.0140 0.0022 344 ASP A C 2645 O O . ASP A 344 ? 0.2532 0.2929 0.2693 0.0193 0.0108 0.0050 344 ASP A O 2646 C CB . ASP A 344 ? 0.2524 0.2951 0.2671 0.0148 0.0226 0.0035 344 ASP A CB 2647 C CG . ASP A 344 ? 0.2738 0.2981 0.2713 -0.0009 0.0161 0.0101 344 ASP A CG 2648 O OD1 . ASP A 344 ? 0.2793 0.3033 0.2960 -0.0081 0.0291 -0.0037 344 ASP A OD1 2649 O OD2 . ASP A 344 ? 0.2635 0.3065 0.2969 0.0209 0.0287 0.0028 344 ASP A OD2 2650 N N . ALA A 345 ? 0.2520 0.2773 0.2518 0.0132 0.0155 0.0103 345 ALA A N 2651 C CA . ALA A 345 ? 0.2453 0.2604 0.2432 0.0090 0.0122 0.0033 345 ALA A CA 2652 C C . ALA A 345 ? 0.2325 0.2610 0.2318 0.0052 0.0155 0.0016 345 ALA A C 2653 O O . ALA A 345 ? 0.2237 0.2599 0.2306 0.0015 0.0220 0.0017 345 ALA A O 2654 C CB . ALA A 345 ? 0.2347 0.2732 0.2393 0.0051 0.0093 0.0042 345 ALA A CB 2655 N N . VAL A 346 ? 0.2307 0.2552 0.2244 0.0026 0.0225 0.0018 346 VAL A N 2656 C CA . VAL A 346 ? 0.2230 0.2599 0.2183 -0.0008 0.0270 0.0012 346 VAL A CA 2657 C C . VAL A 346 ? 0.2320 0.2645 0.2258 0.0040 0.0235 -0.0015 346 VAL A C 2658 O O . VAL A 346 ? 0.2156 0.2668 0.2429 -0.0015 0.0244 0.0040 346 VAL A O 2659 C CB . VAL A 346 ? 0.2211 0.2599 0.2177 -0.0095 0.0244 0.0083 346 VAL A CB 2660 C CG1 . VAL A 346 ? 0.2248 0.2691 0.2206 -0.0060 0.0158 0.0068 346 VAL A CG1 2661 C CG2 . VAL A 346 ? 0.2168 0.2485 0.2229 -0.0145 0.0097 0.0001 346 VAL A CG2 2662 N N . THR A 347 ? 0.2276 0.2542 0.2225 0.0103 0.0284 -0.0039 347 THR A N 2663 C CA . THR A 347 ? 0.2301 0.2580 0.2394 0.0136 0.0296 -0.0039 347 THR A CA 2664 C C . THR A 347 ? 0.2281 0.2601 0.2367 0.0076 0.0267 -0.0009 347 THR A C 2665 O O . THR A 347 ? 0.2183 0.2634 0.2445 0.0176 0.0267 -0.0025 347 THR A O 2666 C CB . THR A 347 ? 0.2316 0.2491 0.2429 0.0100 0.0274 -0.0048 347 THR A CB 2667 O OG1 . THR A 347 ? 0.2502 0.2733 0.2554 0.0119 0.0456 -0.0121 347 THR A OG1 2668 C CG2 . THR A 347 ? 0.2396 0.2490 0.2564 0.0044 0.0151 -0.0052 347 THR A CG2 2669 N N . ARG A 348 ? 0.2228 0.2605 0.2336 0.0066 0.0258 -0.0006 348 ARG A N 2670 C CA . ARG A 348 ? 0.2266 0.2489 0.2196 0.0081 0.0245 0.0059 348 ARG A CA 2671 C C . ARG A 348 ? 0.2218 0.2520 0.2283 0.0057 0.0197 0.0045 348 ARG A C 2672 O O . ARG A 348 ? 0.2250 0.2548 0.2259 0.0064 0.0229 0.0160 348 ARG A O 2673 C CB . ARG A 348 ? 0.2275 0.2434 0.2244 0.0057 0.0166 0.0093 348 ARG A CB 2674 C CG . ARG A 348 ? 0.2487 0.2511 0.2343 0.0015 0.0189 0.0201 348 ARG A CG 2675 C CD . ARG A 348 ? 0.2378 0.2397 0.2463 -0.0005 0.0129 0.0197 348 ARG A CD 2676 N NE . ARG A 348 ? 0.2660 0.2601 0.2646 0.0083 0.0105 0.0183 348 ARG A NE 2677 C CZ . ARG A 348 ? 0.2777 0.2731 0.2860 0.0095 0.0190 0.0194 348 ARG A CZ 2678 N NH1 . ARG A 348 ? 0.2734 0.2848 0.2523 0.0165 0.0323 0.0031 348 ARG A NH1 2679 N NH2 . ARG A 348 ? 0.2994 0.2709 0.2832 0.0182 0.0089 0.0089 348 ARG A NH2 2680 N N . ILE A 349 ? 0.2101 0.2381 0.2204 0.0068 0.0177 0.0007 349 ILE A N 2681 C CA . ILE A 349 ? 0.2116 0.2383 0.2203 -0.0038 0.0152 -0.0047 349 ILE A CA 2682 C C . ILE A 349 ? 0.2022 0.2374 0.2167 -0.0034 0.0148 -0.0065 349 ILE A C 2683 O O . ILE A 349 ? 0.1988 0.2551 0.2157 -0.0037 0.0301 -0.0132 349 ILE A O 2684 C CB . ILE A 349 ? 0.2056 0.2294 0.2195 -0.0069 0.0070 -0.0064 349 ILE A CB 2685 C CG1 . ILE A 349 ? 0.1980 0.2228 0.2123 -0.0166 0.0019 -0.0100 349 ILE A CG1 2686 C CG2 . ILE A 349 ? 0.2197 0.2459 0.2347 -0.0024 0.0208 0.0068 349 ILE A CG2 2687 C CD1 . ILE A 349 ? 0.2046 0.2375 0.2300 -0.0120 0.0061 -0.0008 349 ILE A CD1 2688 N N . LEU A 350 ? 0.2008 0.2493 0.2191 -0.0055 0.0202 -0.0106 350 LEU A N 2689 C CA . LEU A 350 ? 0.2131 0.2513 0.2224 -0.0028 0.0227 -0.0123 350 LEU A CA 2690 C C . LEU A 350 ? 0.2160 0.2522 0.2279 0.0011 0.0214 -0.0050 350 LEU A C 2691 O O . LEU A 350 ? 0.2180 0.2685 0.2345 -0.0013 0.0248 -0.0032 350 LEU A O 2692 C CB . LEU A 350 ? 0.2132 0.2597 0.2276 0.0029 0.0268 -0.0094 350 LEU A CB 2693 C CG . LEU A 350 ? 0.2108 0.2419 0.2187 -0.0019 0.0171 -0.0092 350 LEU A CG 2694 C CD1 . LEU A 350 ? 0.2296 0.2437 0.2469 0.0077 0.0320 -0.0174 350 LEU A CD1 2695 C CD2 . LEU A 350 ? 0.2339 0.2371 0.2269 0.0058 0.0144 -0.0045 350 LEU A CD2 2696 N N . ARG A 351 ? 0.2249 0.2526 0.2356 0.0017 0.0260 -0.0010 351 ARG A N 2697 C CA . ARG A 351 ? 0.2188 0.2370 0.2414 0.0088 0.0217 -0.0008 351 ARG A CA 2698 C C . ARG A 351 ? 0.2164 0.2375 0.2322 0.0068 0.0219 -0.0079 351 ARG A C 2699 O O . ARG A 351 ? 0.2096 0.2409 0.2433 0.0144 0.0220 -0.0150 351 ARG A O 2700 C CB . ARG A 351 ? 0.2246 0.2338 0.2420 0.0062 0.0193 0.0003 351 ARG A CB 2701 C CG . ARG A 351 ? 0.2283 0.2300 0.2542 0.0130 0.0275 0.0040 351 ARG A CG 2702 C CD . ARG A 351 ? 0.2418 0.2474 0.2411 0.0184 0.0246 0.0065 351 ARG A CD 2703 N NE . ARG A 351 ? 0.2611 0.2551 0.2807 0.0200 0.0466 0.0098 351 ARG A NE 2704 C CZ . ARG A 351 ? 0.2665 0.2553 0.2631 0.0086 0.0160 -0.0084 351 ARG A CZ 2705 N NH1 . ARG A 351 ? 0.2711 0.2734 0.2701 -0.0029 0.0325 -0.0039 351 ARG A NH1 2706 N NH2 . ARG A 351 ? 0.3088 0.2847 0.2976 0.0159 0.0295 -0.0046 351 ARG A NH2 2707 N N . VAL A 352 ? 0.2041 0.2270 0.2155 0.0056 0.0205 -0.0027 352 VAL A N 2708 C CA . VAL A 352 ? 0.2113 0.2322 0.2218 0.0003 0.0210 -0.0078 352 VAL A CA 2709 C C . VAL A 352 ? 0.2090 0.2376 0.2209 -0.0038 0.0213 -0.0111 352 VAL A C 2710 O O . VAL A 352 ? 0.2147 0.2663 0.2259 -0.0108 0.0244 -0.0160 352 VAL A O 2711 C CB . VAL A 352 ? 0.2030 0.2322 0.2172 0.0067 0.0191 -0.0087 352 VAL A CB 2712 C CG1 . VAL A 352 ? 0.2216 0.2231 0.2085 0.0141 0.0183 -0.0204 352 VAL A CG1 2713 C CG2 . VAL A 352 ? 0.2125 0.2333 0.2249 0.0049 0.0184 0.0015 352 VAL A CG2 2714 N N . LYS A 353 ? 0.2112 0.2382 0.2122 -0.0148 0.0237 -0.0034 353 LYS A N 2715 C CA . LYS A 353 ? 0.2050 0.2330 0.2207 -0.0211 0.0241 0.0017 353 LYS A CA 2716 C C . LYS A 353 ? 0.2165 0.2354 0.2285 -0.0123 0.0232 -0.0064 353 LYS A C 2717 O O . LYS A 353 ? 0.2078 0.2272 0.2339 -0.0112 0.0140 -0.0185 353 LYS A O 2718 C CB . LYS A 353 ? 0.2011 0.2273 0.2220 -0.0256 0.0233 -0.0036 353 LYS A CB 2719 C CG . LYS A 353 ? 0.1948 0.2177 0.2085 -0.0242 0.0248 -0.0021 353 LYS A CG 2720 C CD . LYS A 353 ? 0.2022 0.2304 0.2172 -0.0264 0.0261 0.0098 353 LYS A CD 2721 C CE . LYS A 353 ? 0.2212 0.2309 0.2032 -0.0213 0.0161 0.0181 353 LYS A CE 2722 N NZ . LYS A 353 ? 0.1755 0.2598 0.1808 -0.0078 0.0253 0.0266 353 LYS A NZ 2723 N N . PHE A 354 ? 0.2308 0.2526 0.2470 -0.0159 0.0245 -0.0062 354 PHE A N 2724 C CA . PHE A 354 ? 0.2282 0.2571 0.2470 -0.0144 0.0276 -0.0058 354 PHE A CA 2725 C C . PHE A 354 ? 0.2259 0.2660 0.2483 -0.0102 0.0253 -0.0058 354 PHE A C 2726 O O . PHE A 354 ? 0.2274 0.2937 0.2312 -0.0167 0.0229 -0.0112 354 PHE A O 2727 C CB . PHE A 354 ? 0.2331 0.2537 0.2468 -0.0078 0.0267 -0.0069 354 PHE A CB 2728 C CG . PHE A 354 ? 0.2418 0.2730 0.2371 -0.0039 0.0232 -0.0124 354 PHE A CG 2729 C CD1 . PHE A 354 ? 0.2550 0.2909 0.2359 -0.0014 0.0286 -0.0071 354 PHE A CD1 2730 C CD2 . PHE A 354 ? 0.2589 0.2760 0.2237 -0.0092 0.0188 -0.0090 354 PHE A CD2 2731 C CE1 . PHE A 354 ? 0.2547 0.2910 0.2701 -0.0008 0.0156 -0.0114 354 PHE A CE1 2732 C CE2 . PHE A 354 ? 0.2571 0.2951 0.2535 -0.0072 0.0270 -0.0069 354 PHE A CE2 2733 C CZ . PHE A 354 ? 0.2327 0.2856 0.2473 -0.0008 0.0224 -0.0129 354 PHE A CZ 2734 N N . THR A 355 ? 0.2357 0.2700 0.2480 -0.0163 0.0284 -0.0045 355 THR A N 2735 C CA . THR A 355 ? 0.2369 0.2712 0.2637 -0.0153 0.0241 -0.0015 355 THR A CA 2736 C C . THR A 355 ? 0.2419 0.2662 0.2598 -0.0109 0.0175 -0.0087 355 THR A C 2737 O O . THR A 355 ? 0.2490 0.2622 0.2769 -0.0179 0.0101 -0.0135 355 THR A O 2738 C CB . THR A 355 ? 0.2276 0.2731 0.2590 -0.0219 0.0234 0.0004 355 THR A CB 2739 O OG1 . THR A 355 ? 0.2572 0.2802 0.2900 -0.0278 0.0309 0.0059 355 THR A OG1 2740 C CG2 . THR A 355 ? 0.2530 0.2881 0.2732 -0.0154 0.0311 0.0057 355 THR A CG2 2741 N N . MET A 356 ? 0.2377 0.2484 0.2484 -0.0049 0.0189 -0.0033 356 MET A N 2742 C CA . MET A 356 ? 0.2415 0.2482 0.2437 -0.0072 0.0147 -0.0131 356 MET A CA 2743 C C . MET A 356 ? 0.2403 0.2609 0.2406 -0.0057 0.0093 -0.0148 356 MET A C 2744 O O . MET A 356 ? 0.2485 0.2889 0.2287 0.0036 0.0131 -0.0162 356 MET A O 2745 C CB . MET A 356 ? 0.2300 0.2439 0.2525 -0.0169 0.0136 -0.0131 356 MET A CB 2746 C CG . MET A 356 ? 0.2332 0.2256 0.2380 -0.0105 0.0319 -0.0092 356 MET A CG 2747 S SD . MET A 356 ? 0.2349 0.2544 0.2541 -0.0069 0.0163 -0.0236 356 MET A SD 2748 C CE . MET A 356 ? 0.2576 0.2624 0.2676 0.0121 0.0106 -0.0149 356 MET A CE 2749 N N . GLY A 357 ? 0.2393 0.2658 0.2309 -0.0048 0.0107 -0.0150 357 GLY A N 2750 C CA . GLY A 357 ? 0.2438 0.2749 0.2317 -0.0121 0.0054 -0.0175 357 GLY A CA 2751 C C . GLY A 357 ? 0.2378 0.2781 0.2287 -0.0106 0.0071 -0.0174 357 GLY A C 2752 O O . GLY A 357 ? 0.2334 0.2986 0.2329 -0.0192 0.0038 -0.0171 357 GLY A O 2753 N N . LEU A 358 ? 0.2269 0.2767 0.2219 -0.0140 0.0085 -0.0226 358 LEU A N 2754 C CA . LEU A 358 ? 0.2253 0.2788 0.2275 -0.0152 0.0041 -0.0175 358 LEU A CA 2755 C C . LEU A 358 ? 0.2256 0.2852 0.2299 -0.0098 0.0018 -0.0157 358 LEU A C 2756 O O . LEU A 358 ? 0.2219 0.2973 0.2300 -0.0109 0.0119 -0.0153 358 LEU A O 2757 C CB . LEU A 358 ? 0.2176 0.2756 0.2229 -0.0067 -0.0003 -0.0266 358 LEU A CB 2758 C CG . LEU A 358 ? 0.2657 0.2879 0.3223 -0.0053 -0.0172 -0.0093 358 LEU A CG 2759 C CD1 . LEU A 358 ? 0.2091 0.2246 0.2753 -0.0139 0.0031 0.0005 358 LEU A CD1 2760 C CD2 . LEU A 358 ? 0.2787 0.2593 0.2619 -0.0065 -0.0166 0.0107 358 LEU A CD2 2761 N N . PHE A 359 ? 0.2344 0.2946 0.2364 -0.0171 -0.0048 -0.0223 359 PHE A N 2762 C CA . PHE A 359 ? 0.2464 0.2991 0.2476 -0.0084 -0.0031 -0.0142 359 PHE A CA 2763 C C . PHE A 359 ? 0.2622 0.3110 0.2528 -0.0131 -0.0039 -0.0127 359 PHE A C 2764 O O . PHE A 359 ? 0.2688 0.3294 0.2635 -0.0123 -0.0153 -0.0050 359 PHE A O 2765 C CB . PHE A 359 ? 0.2541 0.2951 0.2543 -0.0074 -0.0021 -0.0135 359 PHE A CB 2766 C CG . PHE A 359 ? 0.2407 0.2968 0.2459 -0.0002 0.0017 -0.0154 359 PHE A CG 2767 C CD1 . PHE A 359 ? 0.2499 0.2972 0.2541 0.0095 -0.0067 -0.0145 359 PHE A CD1 2768 C CD2 . PHE A 359 ? 0.2538 0.3015 0.2633 -0.0070 -0.0002 -0.0128 359 PHE A CD2 2769 C CE1 . PHE A 359 ? 0.2518 0.3146 0.2578 -0.0026 0.0015 -0.0180 359 PHE A CE1 2770 C CE2 . PHE A 359 ? 0.2463 0.2972 0.2446 0.0087 -0.0011 -0.0117 359 PHE A CE2 2771 C CZ . PHE A 359 ? 0.2636 0.2946 0.2508 -0.0144 0.0038 -0.0164 359 PHE A CZ 2772 N N . GLU A 360 ? 0.2683 0.3152 0.2632 -0.0092 -0.0063 -0.0174 360 GLU A N 2773 C CA . GLU A 360 ? 0.2745 0.3122 0.2665 -0.0117 -0.0040 -0.0145 360 GLU A CA 2774 C C . GLU A 360 ? 0.2709 0.3214 0.2670 -0.0098 -0.0018 -0.0120 360 GLU A C 2775 O O . GLU A 360 ? 0.2992 0.3421 0.2546 -0.0162 -0.0072 -0.0236 360 GLU A O 2776 C CB . GLU A 360 ? 0.2719 0.3012 0.2667 -0.0078 -0.0053 -0.0137 360 GLU A CB 2777 C CG . GLU A 360 ? 0.2754 0.3026 0.2843 -0.0031 -0.0004 -0.0165 360 GLU A CG 2778 C CD . GLU A 360 ? 0.2872 0.3123 0.2950 -0.0135 -0.0094 -0.0080 360 GLU A CD 2779 O OE1 . GLU A 360 ? 0.2750 0.3185 0.3060 -0.0278 -0.0055 -0.0118 360 GLU A OE1 2780 O OE2 . GLU A 360 ? 0.2787 0.3473 0.3235 -0.0173 -0.0113 -0.0069 360 GLU A OE2 2781 N N . ASN A 361 ? 0.2653 0.3203 0.2612 -0.0211 0.0007 -0.0149 361 ASN A N 2782 C CA . ASN A 361 ? 0.2583 0.3209 0.2683 -0.0199 0.0017 -0.0133 361 ASN A CA 2783 C C . ASN A 361 ? 0.2514 0.3165 0.2583 -0.0186 0.0040 -0.0119 361 ASN A C 2784 O O . ASN A 361 ? 0.2535 0.3379 0.2473 -0.0307 0.0027 -0.0129 361 ASN A O 2785 C CB . ASN A 361 ? 0.2713 0.3362 0.2720 -0.0195 0.0020 -0.0149 361 ASN A CB 2786 C CG . ASN A 361 ? 0.2825 0.3360 0.3054 -0.0133 -0.0078 -0.0173 361 ASN A CG 2787 O OD1 . ASN A 361 ? 0.3633 0.4222 0.3270 0.0032 -0.0321 -0.0141 361 ASN A OD1 2788 N ND2 . ASN A 361 ? 0.2780 0.3378 0.3094 -0.0434 -0.0121 -0.0117 361 ASN A ND2 2789 N N . PRO A 362 ? 0.2521 0.3085 0.2538 -0.0124 0.0085 -0.0093 362 PRO A N 2790 C CA . PRO A 362 ? 0.2342 0.3018 0.2404 -0.0138 0.0076 -0.0078 362 PRO A CA 2791 C C . PRO A 362 ? 0.2350 0.3030 0.2388 -0.0095 0.0092 -0.0024 362 PRO A C 2792 O O . PRO A 362 ? 0.2259 0.3126 0.2338 -0.0100 0.0050 -0.0049 362 PRO A O 2793 C CB . PRO A 362 ? 0.2457 0.3087 0.2451 -0.0104 0.0069 -0.0059 362 PRO A CB 2794 C CG . PRO A 362 ? 0.2533 0.3094 0.2494 -0.0206 0.0094 -0.0119 362 PRO A CG 2795 C CD . PRO A 362 ? 0.2503 0.3082 0.2483 -0.0160 0.0091 -0.0087 362 PRO A CD 2796 N N . TYR A 363 ? 0.2313 0.3109 0.2379 -0.0038 0.0103 -0.0029 363 TYR A N 2797 C CA . TYR A 363 ? 0.2233 0.3075 0.2415 -0.0020 0.0136 -0.0005 363 TYR A CA 2798 C C . TYR A 363 ? 0.2259 0.3100 0.2439 0.0005 0.0118 -0.0012 363 TYR A C 2799 O O . TYR A 363 ? 0.2251 0.3186 0.2558 0.0029 0.0249 -0.0039 363 TYR A O 2800 C CB . TYR A 363 ? 0.2435 0.3243 0.2467 -0.0033 0.0103 0.0003 363 TYR A CB 2801 C CG . TYR A 363 ? 0.2459 0.3218 0.2410 0.0031 0.0129 0.0046 363 TYR A CG 2802 C CD1 . TYR A 363 ? 0.2588 0.3418 0.2443 0.0042 0.0044 0.0075 363 TYR A CD1 2803 C CD2 . TYR A 363 ? 0.2712 0.3476 0.2754 -0.0026 0.0052 -0.0029 363 TYR A CD2 2804 C CE1 . TYR A 363 ? 0.2670 0.3484 0.2602 -0.0082 0.0166 -0.0030 363 TYR A CE1 2805 C CE2 . TYR A 363 ? 0.2770 0.3558 0.2689 -0.0101 0.0187 -0.0112 363 TYR A CE2 2806 C CZ . TYR A 363 ? 0.2761 0.3528 0.2785 -0.0068 0.0225 -0.0026 363 TYR A CZ 2807 O OH . TYR A 363 ? 0.2683 0.3910 0.2515 -0.0015 0.0256 0.0020 363 TYR A OH 2808 N N . ALA A 364 ? 0.2111 0.3121 0.2398 0.0055 0.0064 0.0004 364 ALA A N 2809 C CA . ALA A 364 ? 0.2175 0.3119 0.2410 0.0012 0.0077 -0.0050 364 ALA A CA 2810 C C . ALA A 364 ? 0.2239 0.3243 0.2407 0.0000 0.0048 -0.0031 364 ALA A C 2811 O O . ALA A 364 ? 0.2173 0.3392 0.2529 -0.0057 0.0172 -0.0063 364 ALA A O 2812 C CB . ALA A 364 ? 0.2274 0.3035 0.2393 0.0088 0.0017 -0.0019 364 ALA A CB 2813 N N . ASP A 365 ? 0.2191 0.3326 0.2476 -0.0039 0.0038 -0.0103 365 ASP A N 2814 C CA . ASP A 365 ? 0.2459 0.3338 0.2567 -0.0014 -0.0004 -0.0118 365 ASP A CA 2815 C C . ASP A 365 ? 0.2502 0.3414 0.2576 -0.0009 -0.0017 -0.0066 365 ASP A C 2816 O O . ASP A 365 ? 0.2374 0.3508 0.2320 0.0010 0.0014 -0.0130 365 ASP A O 2817 C CB . ASP A 365 ? 0.2475 0.3375 0.2593 -0.0044 0.0023 -0.0072 365 ASP A CB 2818 C CG . ASP A 365 ? 0.2667 0.3380 0.2847 -0.0057 -0.0036 -0.0064 365 ASP A CG 2819 O OD1 . ASP A 365 ? 0.2714 0.3443 0.2732 -0.0101 -0.0015 -0.0102 365 ASP A OD1 2820 O OD2 . ASP A 365 ? 0.3038 0.3690 0.3186 -0.0228 -0.0139 -0.0195 365 ASP A OD2 2821 N N . PRO A 366 ? 0.2786 0.3447 0.2633 0.0082 0.0027 -0.0053 366 PRO A N 2822 C CA . PRO A 366 ? 0.2858 0.3443 0.2709 0.0076 -0.0028 0.0003 366 PRO A CA 2823 C C . PRO A 366 ? 0.2814 0.3419 0.2664 0.0084 -0.0019 -0.0002 366 PRO A C 2824 O O . PRO A 366 ? 0.2754 0.3580 0.2780 0.0060 -0.0056 0.0007 366 PRO A O 2825 C CB . PRO A 366 ? 0.3064 0.3474 0.2806 0.0070 0.0000 -0.0027 366 PRO A CB 2826 C CG . PRO A 366 ? 0.3152 0.3518 0.2842 0.0184 -0.0042 -0.0041 366 PRO A CG 2827 C CD . PRO A 366 ? 0.2901 0.3529 0.2614 0.0126 -0.0022 0.0012 366 PRO A CD 2828 N N . ALA A 367 ? 0.2739 0.3477 0.2645 0.0033 0.0048 0.0024 367 ALA A N 2829 C CA . ALA A 367 ? 0.2782 0.3502 0.2734 0.0015 0.0044 -0.0005 367 ALA A CA 2830 C C . ALA A 367 ? 0.2781 0.3535 0.2741 0.0055 0.0036 -0.0075 367 ALA A C 2831 O O . ALA A 367 ? 0.2821 0.3737 0.2816 0.0037 0.0050 -0.0070 367 ALA A O 2832 C CB . ALA A 367 ? 0.2904 0.3526 0.2861 -0.0010 0.0055 -0.0057 367 ALA A CB 2833 N N . MET A 368 ? 0.2601 0.3396 0.2588 0.0102 0.0025 -0.0068 368 MET A N 2834 C CA . MET A 368 ? 0.2562 0.3316 0.2640 0.0097 0.0036 -0.0027 368 MET A CA 2835 C C . MET A 368 ? 0.2479 0.3252 0.2644 0.0116 0.0031 0.0010 368 MET A C 2836 O O . MET A 368 ? 0.2412 0.3280 0.2484 0.0171 0.0069 -0.0079 368 MET A O 2837 C CB . MET A 368 ? 0.2610 0.3243 0.2672 0.0096 0.0033 0.0037 368 MET A CB 2838 C CG . MET A 368 ? 0.3158 0.3576 0.3140 0.0028 0.0096 -0.0154 368 MET A CG 2839 S SD . MET A 368 ? 0.3764 0.4467 0.4147 -0.0043 0.0150 0.0059 368 MET A SD 2840 C CE . MET A 368 ? 0.3831 0.4048 0.3621 -0.0070 0.0117 0.0016 368 MET A CE 2841 N N . ALA A 369 ? 0.2419 0.3106 0.2582 0.0108 0.0052 0.0000 369 ALA A N 2842 C CA . ALA A 369 ? 0.2494 0.3084 0.2606 0.0126 0.0121 0.0029 369 ALA A CA 2843 C C . ALA A 369 ? 0.2600 0.3063 0.2643 0.0116 0.0085 0.0016 369 ALA A C 2844 O O . ALA A 369 ? 0.2566 0.3037 0.2632 0.0184 0.0153 0.0031 369 ALA A O 2845 C CB . ALA A 369 ? 0.2582 0.2969 0.2604 0.0151 0.0069 0.0031 369 ALA A CB 2846 N N . GLU A 370 ? 0.2605 0.3190 0.2719 0.0151 0.0110 0.0038 370 GLU A N 2847 C CA . GLU A 370 ? 0.2786 0.3308 0.2866 0.0121 0.0089 0.0004 370 GLU A CA 2848 C C . GLU A 370 ? 0.2715 0.3198 0.2731 0.0125 0.0079 -0.0019 370 GLU A C 2849 O O . GLU A 370 ? 0.2711 0.3453 0.2858 0.0264 0.0072 -0.0082 370 GLU A O 2850 C CB A GLU A 370 ? 0.2755 0.3264 0.2820 0.0076 0.0051 -0.0008 370 GLU A CB 2851 C CB B GLU A 370 ? 0.2774 0.3272 0.2817 0.0092 0.0035 0.0000 370 GLU A CB 2852 C CG A GLU A 370 ? 0.2933 0.3301 0.3039 0.0072 0.0074 0.0006 370 GLU A CG 2853 C CG B GLU A 370 ? 0.2915 0.3354 0.3035 0.0052 -0.0039 0.0022 370 GLU A CG 2854 C CD A GLU A 370 ? 0.3006 0.3324 0.3127 -0.0023 -0.0054 0.0066 370 GLU A CD 2855 C CD B GLU A 370 ? 0.3309 0.3631 0.3487 0.0062 -0.0081 -0.0013 370 GLU A CD 2856 O OE1 A GLU A 370 ? 0.3542 0.3737 0.3769 -0.0133 -0.0061 -0.0068 370 GLU A OE1 2857 O OE1 B GLU A 370 ? 0.3484 0.3793 0.3378 0.0077 -0.0019 0.0184 370 GLU A OE1 2858 O OE2 A GLU A 370 ? 0.3153 0.3791 0.3582 0.0199 -0.0128 0.0038 370 GLU A OE2 2859 O OE2 B GLU A 370 ? 0.2861 0.3510 0.3092 -0.0008 -0.0099 0.0028 370 GLU A OE2 2860 N N . GLN A 371 ? 0.2532 0.2962 0.2515 0.0124 0.0067 -0.0050 371 GLN A N 2861 C CA . GLN A 371 ? 0.2565 0.2805 0.2443 0.0047 0.0115 -0.0027 371 GLN A CA 2862 C C . GLN A 371 ? 0.2588 0.2822 0.2416 0.0042 0.0113 0.0000 371 GLN A C 2863 O O . GLN A 371 ? 0.2635 0.2871 0.2354 0.0027 0.0212 0.0032 371 GLN A O 2864 C CB . GLN A 371 ? 0.2553 0.2730 0.2429 0.0012 0.0095 -0.0062 371 GLN A CB 2865 C CG . GLN A 371 ? 0.2940 0.2954 0.2770 -0.0073 0.0000 -0.0065 371 GLN A CG 2866 C CD . GLN A 371 ? 0.3107 0.3572 0.3076 -0.0154 0.0027 -0.0059 371 GLN A CD 2867 O OE1 . GLN A 371 ? 0.2899 0.3201 0.2997 -0.0073 -0.0054 0.0055 371 GLN A OE1 2868 N NE2 . GLN A 371 ? 0.3755 0.4121 0.3395 -0.0295 0.0014 -0.0243 371 GLN A NE2 2869 N N . LEU A 372 ? 0.2528 0.2812 0.2406 0.0075 0.0111 -0.0011 372 LEU A N 2870 C CA . LEU A 372 ? 0.2546 0.2889 0.2307 0.0062 0.0066 0.0034 372 LEU A CA 2871 C C . LEU A 372 ? 0.2627 0.2928 0.2333 0.0150 0.0042 0.0001 372 LEU A C 2872 O O . LEU A 372 ? 0.2838 0.3141 0.2208 0.0243 0.0082 0.0079 372 LEU A O 2873 C CB . LEU A 372 ? 0.2592 0.2846 0.2412 0.0018 0.0051 -0.0003 372 LEU A CB 2874 C CG . LEU A 372 ? 0.2625 0.2864 0.2428 -0.0076 -0.0024 0.0049 372 LEU A CG 2875 C CD1 . LEU A 372 ? 0.2797 0.2774 0.2331 0.0004 0.0065 0.0108 372 LEU A CD1 2876 C CD2 . LEU A 372 ? 0.2907 0.2974 0.2623 -0.0127 0.0086 0.0086 372 LEU A CD2 2877 N N . GLY A 373 ? 0.2467 0.2905 0.2206 0.0107 0.0015 0.0048 373 GLY A N 2878 C CA . GLY A 373 ? 0.2386 0.2886 0.2259 0.0030 0.0002 -0.0031 373 GLY A CA 2879 C C . GLY A 373 ? 0.2432 0.2898 0.2308 0.0059 -0.0045 -0.0014 373 GLY A C 2880 O O . GLY A 373 ? 0.2396 0.3019 0.2414 0.0117 -0.0104 -0.0038 373 GLY A O 2881 N N . LYS A 374 ? 0.2498 0.2969 0.2390 0.0089 -0.0006 -0.0033 374 LYS A N 2882 C CA . LYS A 374 ? 0.2579 0.3018 0.2561 0.0076 -0.0043 -0.0088 374 LYS A CA 2883 C C . LYS A 374 ? 0.2478 0.2936 0.2445 0.0110 -0.0055 -0.0076 374 LYS A C 2884 O O . LYS A 374 ? 0.2260 0.2937 0.2371 0.0122 -0.0151 -0.0080 374 LYS A O 2885 C CB . LYS A 374 ? 0.2806 0.3066 0.2614 0.0027 -0.0075 -0.0139 374 LYS A CB 2886 C CG . LYS A 374 ? 0.2881 0.3605 0.3433 0.0004 -0.0121 -0.0223 374 LYS A CG 2887 C CD . LYS A 374 ? 0.3714 0.3818 0.4046 0.0037 0.0015 -0.0292 374 LYS A CD 2888 C CE . LYS A 374 ? 0.4510 0.4327 0.4602 -0.0065 0.0107 -0.0075 374 LYS A CE 2889 N NZ . LYS A 374 ? 0.4884 0.4698 0.4824 -0.0004 -0.0023 -0.0173 374 LYS A NZ 2890 N N . GLN A 375 ? 0.2378 0.2920 0.2313 0.0097 -0.0118 -0.0109 375 GLN A N 2891 C CA . GLN A 375 ? 0.2329 0.2878 0.2355 0.0155 -0.0089 -0.0159 375 GLN A CA 2892 C C . GLN A 375 ? 0.2339 0.2898 0.2373 0.0107 -0.0106 -0.0150 375 GLN A C 2893 O O . GLN A 375 ? 0.2456 0.2937 0.2281 0.0173 -0.0140 -0.0206 375 GLN A O 2894 C CB . GLN A 375 ? 0.2369 0.2993 0.2369 0.0174 -0.0102 -0.0121 375 GLN A CB 2895 C CG . GLN A 375 ? 0.2624 0.2901 0.2235 0.0080 -0.0097 -0.0181 375 GLN A CG 2896 C CD . GLN A 375 ? 0.3010 0.3048 0.2582 -0.0053 -0.0131 -0.0121 375 GLN A CD 2897 O OE1 . GLN A 375 ? 0.3254 0.3285 0.2560 0.0018 -0.0088 -0.0121 375 GLN A OE1 2898 N NE2 . GLN A 375 ? 0.3128 0.3314 0.2486 0.0146 -0.0079 -0.0093 375 GLN A NE2 2899 N N . GLU A 376 ? 0.2298 0.2824 0.2332 0.0126 -0.0148 -0.0165 376 GLU A N 2900 C CA . GLU A 376 ? 0.2334 0.2854 0.2420 0.0081 -0.0133 -0.0174 376 GLU A CA 2901 C C . GLU A 376 ? 0.2151 0.2802 0.2360 0.0101 -0.0073 -0.0132 376 GLU A C 2902 O O . GLU A 376 ? 0.2073 0.2891 0.2396 0.0064 0.0013 -0.0163 376 GLU A O 2903 C CB . GLU A 376 ? 0.2468 0.2875 0.2522 0.0006 -0.0187 -0.0216 376 GLU A CB 2904 C CG . GLU A 376 ? 0.2502 0.3130 0.2949 0.0092 -0.0145 -0.0193 376 GLU A CG 2905 C CD . GLU A 376 ? 0.2938 0.3202 0.3151 -0.0072 -0.0294 -0.0086 376 GLU A CD 2906 O OE1 . GLU A 376 ? 0.2748 0.3488 0.2736 -0.0014 -0.0392 -0.0142 376 GLU A OE1 2907 O OE2 . GLU A 376 ? 0.3565 0.3769 0.3925 -0.0019 -0.0444 -0.0284 376 GLU A OE2 2908 N N . HIS A 377 ? 0.2055 0.2692 0.2198 0.0083 -0.0032 -0.0175 377 HIS A N 2909 C CA . HIS A 377 ? 0.2070 0.2621 0.2058 0.0072 -0.0013 -0.0159 377 HIS A CA 2910 C C . HIS A 377 ? 0.2146 0.2539 0.2096 0.0075 -0.0012 -0.0118 377 HIS A C 2911 O O . HIS A 377 ? 0.2219 0.2486 0.2069 0.0193 0.0050 0.0006 377 HIS A O 2912 C CB . HIS A 377 ? 0.2035 0.2743 0.2001 0.0029 0.0034 -0.0170 377 HIS A CB 2913 C CG . HIS A 377 ? 0.2270 0.2707 0.2204 0.0034 -0.0040 -0.0180 377 HIS A CG 2914 N ND1 . HIS A 377 ? 0.2626 0.3104 0.2576 0.0046 0.0088 -0.0184 377 HIS A ND1 2915 C CD2 . HIS A 377 ? 0.1752 0.2309 0.2125 -0.0010 0.0124 -0.0261 377 HIS A CD2 2916 C CE1 . HIS A 377 ? 0.2312 0.2871 0.2260 -0.0057 0.0108 -0.0219 377 HIS A CE1 2917 N NE2 . HIS A 377 ? 0.2871 0.3151 0.2562 -0.0026 0.0033 -0.0186 377 HIS A NE2 2918 N N . ARG A 378 ? 0.2258 0.2461 0.2031 0.0114 -0.0075 -0.0115 378 ARG A N 2919 C CA . ARG A 378 ? 0.2283 0.2414 0.2145 0.0086 -0.0040 -0.0089 378 ARG A CA 2920 C C . ARG A 378 ? 0.2245 0.2479 0.2215 0.0071 -0.0056 -0.0099 378 ARG A C 2921 O O . ARG A 378 ? 0.2239 0.2606 0.2129 0.0012 -0.0105 -0.0028 378 ARG A O 2922 C CB . ARG A 378 ? 0.2358 0.2459 0.2143 0.0004 -0.0074 0.0023 378 ARG A CB 2923 C CG . ARG A 378 ? 0.2340 0.2476 0.2399 0.0033 0.0035 0.0047 378 ARG A CG 2924 C CD . ARG A 378 ? 0.2453 0.2378 0.2286 -0.0031 -0.0059 0.0072 378 ARG A CD 2925 N NE . ARG A 378 ? 0.2668 0.2496 0.2232 0.0135 -0.0008 -0.0013 378 ARG A NE 2926 C CZ . ARG A 378 ? 0.2512 0.2585 0.2391 0.0091 0.0069 0.0016 378 ARG A CZ 2927 N NH1 . ARG A 378 ? 0.1976 0.2677 0.2297 0.0094 0.0008 -0.0119 378 ARG A NH1 2928 N NH2 . ARG A 378 ? 0.2750 0.2456 0.2512 0.0220 0.0134 0.0207 378 ARG A NH2 2929 N N . ASP A 379 ? 0.2235 0.2442 0.2219 0.0021 -0.0031 -0.0118 379 ASP A N 2930 C CA . ASP A 379 ? 0.2162 0.2515 0.2207 0.0008 -0.0033 -0.0084 379 ASP A CA 2931 C C . ASP A 379 ? 0.2236 0.2449 0.2232 0.0054 0.0061 -0.0098 379 ASP A C 2932 O O . ASP A 379 ? 0.2172 0.2605 0.2125 0.0213 0.0097 -0.0216 379 ASP A O 2933 C CB . ASP A 379 ? 0.2300 0.2652 0.2208 -0.0023 -0.0094 -0.0097 379 ASP A CB 2934 C CG . ASP A 379 ? 0.2534 0.2936 0.2707 -0.0009 -0.0096 -0.0060 379 ASP A CG 2935 O OD1 . ASP A 379 ? 0.2826 0.3133 0.2950 0.0127 -0.0090 -0.0051 379 ASP A OD1 2936 O OD2 . ASP A 379 ? 0.3198 0.3828 0.3124 -0.0059 -0.0358 -0.0054 379 ASP A OD2 2937 N N . LEU A 380 ? 0.2118 0.2421 0.2150 0.0065 0.0091 -0.0183 380 LEU A N 2938 C CA . LEU A 380 ? 0.2127 0.2335 0.2067 0.0030 0.0097 -0.0161 380 LEU A CA 2939 C C . LEU A 380 ? 0.2026 0.2377 0.2040 0.0034 0.0011 -0.0097 380 LEU A C 2940 O O . LEU A 380 ? 0.2078 0.2357 0.1862 -0.0038 0.0013 -0.0154 380 LEU A O 2941 C CB . LEU A 380 ? 0.2175 0.2366 0.2201 0.0068 0.0063 -0.0155 380 LEU A CB 2942 C CG . LEU A 380 ? 0.2182 0.2264 0.2216 0.0084 0.0153 -0.0086 380 LEU A CG 2943 C CD1 . LEU A 380 ? 0.2512 0.2272 0.2527 0.0007 0.0220 0.0012 380 LEU A CD1 2944 C CD2 . LEU A 380 ? 0.2183 0.2530 0.2250 0.0106 0.0212 -0.0198 380 LEU A CD2 2945 N N . ALA A 381 ? 0.2026 0.2321 0.1896 0.0041 -0.0001 -0.0116 381 ALA A N 2946 C CA . ALA A 381 ? 0.1954 0.2382 0.1940 0.0045 0.0046 -0.0128 381 ALA A CA 2947 C C . ALA A 381 ? 0.1901 0.2459 0.1983 0.0104 0.0064 -0.0120 381 ALA A C 2948 O O . ALA A 381 ? 0.2002 0.2574 0.1925 0.0153 0.0220 -0.0152 381 ALA A O 2949 C CB . ALA A 381 ? 0.1989 0.2353 0.1934 0.0026 0.0027 -0.0097 381 ALA A CB 2950 N N . ARG A 382 ? 0.1869 0.2542 0.1951 0.0139 0.0048 -0.0159 382 ARG A N 2951 C CA . ARG A 382 ? 0.1848 0.2499 0.2041 0.0150 0.0015 -0.0109 382 ARG A CA 2952 C C . ARG A 382 ? 0.1986 0.2475 0.2051 0.0117 0.0011 -0.0108 382 ARG A C 2953 O O . ARG A 382 ? 0.2170 0.2486 0.1963 0.0051 -0.0123 0.0001 382 ARG A O 2954 C CB . ARG A 382 ? 0.1704 0.2452 0.1814 0.0221 0.0034 -0.0095 382 ARG A CB 2955 C CG . ARG A 382 ? 0.1714 0.2467 0.1984 0.0389 0.0013 -0.0139 382 ARG A CG 2956 C CD . ARG A 382 ? 0.1829 0.2668 0.2350 0.0183 -0.0075 -0.0065 382 ARG A CD 2957 N NE . ARG A 382 ? 0.2166 0.2886 0.2307 0.0143 0.0131 -0.0098 382 ARG A NE 2958 C CZ . ARG A 382 ? 0.2710 0.3430 0.2780 0.0208 -0.0021 0.0039 382 ARG A CZ 2959 N NH1 . ARG A 382 ? 0.2815 0.3837 0.2614 0.0359 0.0091 -0.0007 382 ARG A NH1 2960 N NH2 . ARG A 382 ? 0.2851 0.3774 0.2929 0.0185 0.0020 -0.0143 382 ARG A NH2 2961 N N . GLU A 383 ? 0.2053 0.2463 0.2218 0.0117 -0.0013 -0.0086 383 GLU A N 2962 C CA . GLU A 383 ? 0.2239 0.2506 0.2249 0.0013 0.0033 -0.0114 383 GLU A CA 2963 C C . GLU A 383 ? 0.2041 0.2389 0.2096 0.0038 0.0076 -0.0088 383 GLU A C 2964 O O . GLU A 383 ? 0.1969 0.2593 0.2052 -0.0039 0.0130 -0.0089 383 GLU A O 2965 C CB . GLU A 383 ? 0.2197 0.2521 0.2299 -0.0007 -0.0008 -0.0142 383 GLU A CB 2966 C CG . GLU A 383 ? 0.2537 0.2613 0.2474 -0.0004 0.0017 -0.0105 383 GLU A CG 2967 C CD . GLU A 383 ? 0.2810 0.2715 0.2728 -0.0043 0.0002 -0.0087 383 GLU A CD 2968 O OE1 . GLU A 383 ? 0.3688 0.3089 0.3214 -0.0170 -0.0184 -0.0178 383 GLU A OE1 2969 O OE2 . GLU A 383 ? 0.3215 0.3256 0.3257 0.0014 0.0063 0.0000 383 GLU A OE2 2970 N N . ALA A 384 ? 0.1939 0.2398 0.2041 -0.0042 0.0064 -0.0148 384 ALA A N 2971 C CA . ALA A 384 ? 0.1994 0.2399 0.1998 0.0098 0.0170 -0.0110 384 ALA A CA 2972 C C . ALA A 384 ? 0.1925 0.2348 0.1974 0.0011 0.0102 -0.0080 384 ALA A C 2973 O O . ALA A 384 ? 0.2049 0.2325 0.1863 0.0066 0.0211 -0.0084 384 ALA A O 2974 C CB . ALA A 384 ? 0.1905 0.2558 0.2063 0.0065 0.0214 -0.0102 384 ALA A CB 2975 N N . ALA A 385 ? 0.2014 0.2276 0.1952 0.0047 0.0175 -0.0114 385 ALA A N 2976 C CA . ALA A 385 ? 0.2049 0.2247 0.1899 -0.0001 0.0171 -0.0055 385 ALA A CA 2977 C C . ALA A 385 ? 0.2026 0.2339 0.1963 0.0023 0.0141 -0.0001 385 ALA A C 2978 O O . ALA A 385 ? 0.2046 0.2516 0.2020 0.0102 0.0090 0.0038 385 ALA A O 2979 C CB . ALA A 385 ? 0.2041 0.2320 0.1902 -0.0023 0.0121 -0.0001 385 ALA A CB 2980 N N . ARG A 386 ? 0.1924 0.2280 0.1920 -0.0017 0.0199 0.0090 386 ARG A N 2981 C CA . ARG A 386 ? 0.1953 0.2431 0.1998 0.0028 0.0196 0.0006 386 ARG A CA 2982 C C . ARG A 386 ? 0.1988 0.2373 0.2002 -0.0033 0.0175 -0.0007 386 ARG A C 2983 O O . ARG A 386 ? 0.2279 0.2516 0.2145 0.0023 0.0139 0.0053 386 ARG A O 2984 C CB . ARG A 386 ? 0.1844 0.2439 0.2059 -0.0093 0.0156 0.0010 386 ARG A CB 2985 C CG . ARG A 386 ? 0.2476 0.2826 0.2423 -0.0023 0.0340 -0.0046 386 ARG A CG 2986 C CD . ARG A 386 ? 0.3259 0.3267 0.3331 -0.0135 0.0176 0.0022 386 ARG A CD 2987 N NE . ARG A 386 ? 0.3137 0.3781 0.3695 -0.0100 0.0274 -0.0143 386 ARG A NE 2988 C CZ . ARG A 386 ? 0.3382 0.3990 0.3991 -0.0055 0.0135 -0.0110 386 ARG A CZ 2989 N NH1 . ARG A 386 ? 0.3384 0.3994 0.4307 -0.0081 0.0192 -0.0079 386 ARG A NH1 2990 N NH2 . ARG A 386 ? 0.3259 0.4328 0.4070 -0.0090 0.0189 -0.0211 386 ARG A NH2 2991 N N . LYS A 387 ? 0.2089 0.2342 0.2001 0.0013 0.0145 -0.0006 387 LYS A N 2992 C CA . LYS A 387 ? 0.2191 0.2381 0.2123 -0.0004 0.0100 -0.0095 387 LYS A CA 2993 C C . LYS A 387 ? 0.2040 0.2362 0.1991 0.0079 0.0131 -0.0028 387 LYS A C 2994 O O . LYS A 387 ? 0.2186 0.2615 0.1963 -0.0066 0.0188 0.0029 387 LYS A O 2995 C CB . LYS A 387 ? 0.2338 0.2490 0.2072 0.0004 0.0107 -0.0144 387 LYS A CB 2996 C CG . LYS A 387 ? 0.2311 0.2417 0.2313 -0.0120 0.0157 -0.0147 387 LYS A CG 2997 C CD . LYS A 387 ? 0.2868 0.2588 0.2543 0.0009 0.0017 -0.0230 387 LYS A CD 2998 C CE . LYS A 387 ? 0.3117 0.3040 0.2838 -0.0184 0.0083 -0.0145 387 LYS A CE 2999 N NZ . LYS A 387 ? 0.3533 0.2904 0.3067 -0.0102 0.0051 -0.0178 387 LYS A NZ 3000 N N . SER A 388 ? 0.1988 0.2287 0.1893 0.0034 0.0096 -0.0004 388 SER A N 3001 C CA . SER A 388 ? 0.2016 0.2272 0.1863 0.0026 0.0104 0.0027 388 SER A CA 3002 C C . SER A 388 ? 0.2087 0.2308 0.1810 0.0089 0.0109 0.0062 388 SER A C 3003 O O . SER A 388 ? 0.2113 0.2497 0.1857 0.0138 0.0119 0.0077 388 SER A O 3004 C CB . SER A 388 ? 0.2082 0.2242 0.1914 0.0048 0.0138 0.0059 388 SER A CB 3005 O OG . SER A 388 ? 0.1784 0.2161 0.2005 -0.0040 0.0146 -0.0074 388 SER A OG 3006 N N . LEU A 389 ? 0.2087 0.2320 0.1787 0.0126 0.0165 0.0063 389 LEU A N 3007 C CA . LEU A 389 ? 0.2163 0.2252 0.1749 0.0130 0.0118 0.0092 389 LEU A CA 3008 C C . LEU A 389 ? 0.2164 0.2231 0.1731 0.0090 0.0151 0.0101 389 LEU A C 3009 O O . LEU A 389 ? 0.2441 0.2218 0.1828 0.0026 0.0211 0.0123 389 LEU A O 3010 C CB . LEU A 389 ? 0.2120 0.2230 0.1835 0.0171 -0.0009 0.0141 389 LEU A CB 3011 C CG . LEU A 389 ? 0.1977 0.2316 0.1821 0.0098 0.0048 0.0177 389 LEU A CG 3012 C CD1 . LEU A 389 ? 0.2017 0.2485 0.2106 0.0206 0.0034 0.0231 389 LEU A CD1 3013 C CD2 . LEU A 389 ? 0.2043 0.2112 0.1865 0.0039 -0.0168 0.0196 389 LEU A CD2 3014 N N . VAL A 390 ? 0.2163 0.2252 0.1644 0.0102 0.0163 0.0145 390 VAL A N 3015 C CA . VAL A 390 ? 0.2257 0.2298 0.1688 0.0124 0.0136 0.0102 390 VAL A CA 3016 C C . VAL A 390 ? 0.2256 0.2290 0.1822 0.0115 0.0118 0.0079 390 VAL A C 3017 O O . VAL A 390 ? 0.2329 0.2410 0.1803 0.0002 0.0104 -0.0096 390 VAL A O 3018 C CB . VAL A 390 ? 0.2273 0.2293 0.1746 0.0186 0.0174 0.0119 390 VAL A CB 3019 C CG1 . VAL A 390 ? 0.2481 0.2362 0.1711 0.0125 0.0251 0.0177 390 VAL A CG1 3020 C CG2 . VAL A 390 ? 0.2378 0.2339 0.1627 0.0116 0.0239 0.0088 390 VAL A CG2 3021 N N . LEU A 391 ? 0.2228 0.2419 0.1894 0.0131 0.0145 0.0026 391 LEU A N 3022 C CA . LEU A 391 ? 0.2214 0.2413 0.1917 0.0105 0.0145 0.0005 391 LEU A CA 3023 C C . LEU A 391 ? 0.2328 0.2571 0.2007 0.0107 0.0147 0.0028 391 LEU A C 3024 O O . LEU A 391 ? 0.2492 0.2695 0.2091 0.0063 0.0147 0.0134 391 LEU A O 3025 C CB . LEU A 391 ? 0.2211 0.2460 0.1943 0.0109 0.0077 0.0004 391 LEU A CB 3026 C CG . LEU A 391 ? 0.2268 0.2510 0.2093 0.0114 0.0130 -0.0043 391 LEU A CG 3027 C CD1 . LEU A 391 ? 0.2592 0.2385 0.2290 0.0040 0.0059 -0.0045 391 LEU A CD1 3028 C CD2 . LEU A 391 ? 0.2231 0.2448 0.2007 0.0047 0.0178 -0.0049 391 LEU A CD2 3029 N N . LEU A 392 ? 0.2223 0.2703 0.1972 0.0099 0.0142 0.0032 392 LEU A N 3030 C CA . LEU A 392 ? 0.2337 0.2844 0.2042 0.0134 0.0154 -0.0026 392 LEU A CA 3031 C C . LEU A 392 ? 0.2410 0.2973 0.2069 0.0162 0.0168 0.0045 392 LEU A C 3032 O O . LEU A 392 ? 0.2604 0.3222 0.2164 0.0267 0.0116 0.0118 392 LEU A O 3033 C CB . LEU A 392 ? 0.2340 0.2775 0.2121 0.0076 0.0142 -0.0021 392 LEU A CB 3034 C CG . LEU A 392 ? 0.2515 0.2735 0.2214 0.0028 0.0114 -0.0119 392 LEU A CG 3035 C CD1 . LEU A 392 ? 0.2667 0.3242 0.2804 -0.0055 0.0110 0.0033 392 LEU A CD1 3036 C CD2 . LEU A 392 ? 0.2850 0.2970 0.2511 0.0192 0.0089 -0.0005 392 LEU A CD2 3037 N N . LYS A 393 ? 0.2310 0.2900 0.1992 0.0196 0.0221 0.0004 393 LYS A N 3038 C CA . LYS A 393 ? 0.2315 0.2881 0.2100 0.0157 0.0166 -0.0043 393 LYS A CA 3039 C C . LYS A 393 ? 0.2303 0.2857 0.2165 0.0123 0.0174 -0.0026 393 LYS A C 3040 O O . LYS A 393 ? 0.2297 0.2920 0.2043 0.0096 0.0133 0.0000 393 LYS A O 3041 C CB . LYS A 393 ? 0.2351 0.2853 0.2107 0.0206 0.0152 -0.0124 393 LYS A CB 3042 C CG . LYS A 393 ? 0.2413 0.2925 0.2266 0.0143 0.0194 -0.0071 393 LYS A CG 3043 C CD . LYS A 393 ? 0.2530 0.2920 0.2159 0.0116 0.0186 -0.0071 393 LYS A CD 3044 C CE . LYS A 393 ? 0.2663 0.2797 0.2441 0.0023 0.0209 -0.0186 393 LYS A CE 3045 N NZ . LYS A 393 ? 0.2541 0.2945 0.2492 -0.0030 0.0203 -0.0106 393 LYS A NZ 3046 N N . ASN A 394 ? 0.2375 0.2923 0.2124 0.0024 0.0253 -0.0028 394 ASN A N 3047 C CA . ASN A 394 ? 0.2445 0.2999 0.2285 -0.0002 0.0283 -0.0060 394 ASN A CA 3048 C C . ASN A 394 ? 0.2612 0.3149 0.2363 -0.0092 0.0329 -0.0082 394 ASN A C 3049 O O . ASN A 394 ? 0.2953 0.3446 0.2688 -0.0138 0.0405 -0.0121 394 ASN A O 3050 C CB . ASN A 394 ? 0.2516 0.3032 0.2252 0.0010 0.0240 -0.0066 394 ASN A CB 3051 C CG . ASN A 394 ? 0.2538 0.2981 0.2335 0.0000 0.0283 -0.0035 394 ASN A CG 3052 O OD1 . ASN A 394 ? 0.3129 0.3393 0.2395 -0.0027 0.0275 -0.0143 394 ASN A OD1 3053 N ND2 . ASN A 394 ? 0.2378 0.2857 0.2080 -0.0019 0.0117 0.0084 394 ASN A ND2 3054 N N . GLY A 395 ? 0.2764 0.3230 0.2490 -0.0066 0.0370 -0.0080 395 GLY A N 3055 C CA . GLY A 395 ? 0.2924 0.3362 0.2609 -0.0050 0.0256 -0.0159 395 GLY A CA 3056 C C . GLY A 395 ? 0.3055 0.3450 0.2859 -0.0071 0.0202 -0.0101 395 GLY A C 3057 O O . GLY A 395 ? 0.3166 0.3555 0.2803 -0.0026 0.0144 -0.0149 395 GLY A O 3058 N N . LYS A 396 ? 0.3239 0.3579 0.3064 -0.0091 0.0172 -0.0132 396 LYS A N 3059 C CA . LYS A 396 ? 0.3488 0.3738 0.3238 -0.0072 0.0081 -0.0040 396 LYS A CA 3060 C C . LYS A 396 ? 0.3536 0.3835 0.3403 -0.0023 0.0020 -0.0030 396 LYS A C 3061 O O . LYS A 396 ? 0.3624 0.4024 0.3375 -0.0075 0.0031 0.0018 396 LYS A O 3062 C CB . LYS A 396 ? 0.3538 0.3719 0.3303 -0.0074 0.0100 -0.0065 396 LYS A CB 3063 C CG . LYS A 396 ? 0.3784 0.3732 0.3298 -0.0056 0.0048 0.0045 396 LYS A CG 3064 C CD . LYS A 396 ? 0.3773 0.3802 0.3448 -0.0084 0.0056 -0.0018 396 LYS A CD 3065 C CE . LYS A 396 ? 0.4104 0.3924 0.3588 -0.0098 0.0017 0.0006 396 LYS A CE 3066 N NZ . LYS A 396 ? 0.4305 0.3982 0.3789 0.0024 -0.0175 0.0028 396 LYS A NZ 3067 N N . THR A 397 ? 0.3530 0.3884 0.3410 -0.0072 0.0005 -0.0025 397 THR A N 3068 C CA . THR A 397 ? 0.3627 0.3979 0.3541 -0.0010 -0.0040 0.0009 397 THR A CA 3069 C C . THR A 397 ? 0.3817 0.4090 0.3684 -0.0022 -0.0059 0.0044 397 THR A C 3070 O O . THR A 397 ? 0.3777 0.4294 0.3670 -0.0042 -0.0118 0.0052 397 THR A O 3071 C CB . THR A 397 ? 0.3576 0.3933 0.3515 -0.0013 -0.0024 0.0006 397 THR A CB 3072 O OG1 . THR A 397 ? 0.3448 0.3996 0.3521 -0.0057 0.0094 -0.0043 397 THR A OG1 3073 C CG2 . THR A 397 ? 0.3706 0.3988 0.3479 -0.0025 -0.0050 0.0006 397 THR A CG2 3074 N N . SER A 398 ? 0.3885 0.4145 0.3789 0.0024 -0.0069 0.0081 398 SER A N 3075 C CA . SER A 398 ? 0.4047 0.4137 0.3851 0.0022 -0.0048 0.0072 398 SER A CA 3076 C C . SER A 398 ? 0.4029 0.4146 0.3833 -0.0033 -0.0086 0.0092 398 SER A C 3077 O O . SER A 398 ? 0.4243 0.4315 0.4023 -0.0064 -0.0164 0.0113 398 SER A O 3078 C CB . SER A 398 ? 0.4186 0.4206 0.3939 -0.0002 -0.0046 0.0077 398 SER A CB 3079 O OG . SER A 398 ? 0.4415 0.4426 0.4111 0.0118 0.0020 0.0066 398 SER A OG 3080 N N . THR A 399 ? 0.3792 0.4008 0.3628 0.0018 -0.0022 0.0134 399 THR A N 3081 C CA . THR A 399 ? 0.3643 0.3912 0.3499 -0.0017 -0.0001 0.0143 399 THR A CA 3082 C C . THR A 399 ? 0.3274 0.3605 0.3132 -0.0072 0.0070 0.0167 399 THR A C 3083 O O . THR A 399 ? 0.3114 0.3530 0.2951 -0.0157 0.0157 0.0219 399 THR A O 3084 C CB . THR A 399 ? 0.3725 0.4002 0.3514 0.0013 0.0065 0.0175 399 THR A CB 3085 O OG1 . THR A 399 ? 0.4338 0.4682 0.4190 0.0124 -0.0059 0.0150 399 THR A OG1 3086 C CG2 . THR A 399 ? 0.3859 0.4093 0.3574 -0.0029 0.0030 0.0078 399 THR A CG2 3087 N N . ASP A 400 ? 0.2935 0.3322 0.2872 -0.0091 0.0071 0.0070 400 ASP A N 3088 C CA . ASP A 400 ? 0.2691 0.3062 0.2669 -0.0091 0.0104 0.0031 400 ASP A CA 3089 C C . ASP A 400 ? 0.2613 0.3032 0.2596 -0.0070 0.0126 0.0043 400 ASP A C 3090 O O . ASP A 400 ? 0.2620 0.3087 0.2534 -0.0072 0.0054 -0.0003 400 ASP A O 3091 C CB . ASP A 400 ? 0.2681 0.3093 0.2629 -0.0189 0.0149 0.0022 400 ASP A CB 3092 C CG . ASP A 400 ? 0.2920 0.3313 0.2781 -0.0149 0.0114 -0.0027 400 ASP A CG 3093 O OD1 . ASP A 400 ? 0.3010 0.3656 0.2730 -0.0170 0.0212 -0.0236 400 ASP A OD1 3094 O OD2 . ASP A 400 ? 0.3016 0.3454 0.2903 -0.0302 0.0166 -0.0159 400 ASP A OD2 3095 N N . ALA A 401 ? 0.2460 0.3020 0.2436 -0.0057 0.0184 0.0014 401 ALA A N 3096 C CA . ALA A 401 ? 0.2464 0.3040 0.2439 -0.0029 0.0236 -0.0033 401 ALA A CA 3097 C C . ALA A 401 ? 0.2672 0.3111 0.2456 -0.0099 0.0283 -0.0059 401 ALA A C 3098 O O . ALA A 401 ? 0.2606 0.3168 0.2381 -0.0121 0.0395 -0.0138 401 ALA A O 3099 C CB . ALA A 401 ? 0.2468 0.3042 0.2505 -0.0026 0.0195 0.0028 401 ALA A CB 3100 N N . PRO A 402 ? 0.2789 0.3099 0.2583 -0.0068 0.0317 -0.0063 402 PRO A N 3101 C CA . PRO A 402 ? 0.2882 0.3150 0.2658 -0.0070 0.0289 -0.0051 402 PRO A CA 3102 C C . PRO A 402 ? 0.2805 0.3129 0.2670 -0.0051 0.0220 -0.0049 402 PRO A C 3103 O O . PRO A 402 ? 0.2740 0.3182 0.2732 -0.0041 0.0288 0.0002 402 PRO A O 3104 C CB . PRO A 402 ? 0.2967 0.3209 0.2786 -0.0053 0.0332 -0.0081 402 PRO A CB 3105 C CG . PRO A 402 ? 0.3249 0.3362 0.2915 -0.0138 0.0238 -0.0169 402 PRO A CG 3106 C CD . PRO A 402 ? 0.3046 0.3215 0.2683 -0.0109 0.0296 -0.0141 402 PRO A CD 3107 N N . LEU A 403 ? 0.2618 0.3096 0.2505 -0.0017 0.0230 -0.0050 403 LEU A N 3108 C CA . LEU A 403 ? 0.2644 0.3076 0.2611 -0.0022 0.0170 -0.0132 403 LEU A CA 3109 C C . LEU A 403 ? 0.2496 0.3001 0.2414 0.0029 0.0174 -0.0129 403 LEU A C 3110 O O . LEU A 403 ? 0.2242 0.3075 0.2260 0.0009 0.0295 -0.0267 403 LEU A O 3111 C CB . LEU A 403 ? 0.2677 0.3034 0.2556 -0.0033 0.0118 -0.0129 403 LEU A CB 3112 C CG . LEU A 403 ? 0.2799 0.3026 0.3077 -0.0047 0.0143 -0.0062 403 LEU A CG 3113 C CD1 . LEU A 403 ? 0.3080 0.2942 0.3237 0.0051 0.0202 0.0013 403 LEU A CD1 3114 C CD2 . LEU A 403 ? 0.2854 0.3293 0.2966 -0.0108 0.0106 -0.0149 403 LEU A CD2 3115 N N . LEU A 404 ? 0.2438 0.2979 0.2377 -0.0006 0.0197 -0.0148 404 LEU A N 3116 C CA . LEU A 404 ? 0.2412 0.2884 0.2444 0.0012 0.0169 -0.0129 404 LEU A CA 3117 C C . LEU A 404 ? 0.2496 0.2916 0.2503 0.0013 0.0122 -0.0101 404 LEU A C 3118 O O . LEU A 404 ? 0.2568 0.2850 0.2511 0.0033 0.0115 -0.0106 404 LEU A O 3119 C CB . LEU A 404 ? 0.2341 0.2886 0.2455 0.0077 0.0147 -0.0104 404 LEU A CB 3120 C CG . LEU A 404 ? 0.2443 0.2754 0.2492 0.0087 0.0181 -0.0099 404 LEU A CG 3121 C CD1 . LEU A 404 ? 0.2391 0.2834 0.2641 0.0180 0.0193 -0.0032 404 LEU A CD1 3122 C CD2 . LEU A 404 ? 0.2438 0.2685 0.2432 0.0095 0.0125 -0.0044 404 LEU A CD2 3123 N N . PRO A 405 ? 0.2648 0.3028 0.2601 -0.0062 0.0059 -0.0074 405 PRO A N 3124 C CA . PRO A 405 ? 0.2708 0.3013 0.2609 -0.0084 0.0010 -0.0080 405 PRO A CA 3125 C C . PRO A 405 ? 0.2612 0.2960 0.2573 -0.0100 0.0025 -0.0080 405 PRO A C 3126 O O . PRO A 405 ? 0.2687 0.3026 0.2683 -0.0167 0.0112 -0.0172 405 PRO A O 3127 C CB . PRO A 405 ? 0.2854 0.3030 0.2615 -0.0144 0.0033 -0.0132 405 PRO A CB 3128 C CG . PRO A 405 ? 0.3070 0.3284 0.2817 -0.0151 -0.0087 -0.0005 405 PRO A CG 3129 C CD . PRO A 405 ? 0.2817 0.3025 0.2608 -0.0042 -0.0015 -0.0082 405 PRO A CD 3130 N N . LEU A 406 ? 0.2500 0.2857 0.2481 -0.0065 -0.0013 -0.0082 406 LEU A N 3131 C CA . LEU A 406 ? 0.2494 0.2923 0.2462 0.0001 -0.0007 -0.0076 406 LEU A CA 3132 C C . LEU A 406 ? 0.2472 0.2905 0.2505 0.0035 0.0021 -0.0109 406 LEU A C 3133 O O . LEU A 406 ? 0.2462 0.3093 0.2330 0.0023 0.0114 -0.0174 406 LEU A O 3134 C CB . LEU A 406 ? 0.2583 0.2872 0.2523 -0.0059 -0.0060 -0.0070 406 LEU A CB 3135 C CG . LEU A 406 ? 0.2714 0.3151 0.2963 0.0072 -0.0065 -0.0036 406 LEU A CG 3136 C CD1 . LEU A 406 ? 0.3018 0.3147 0.3301 -0.0047 -0.0001 -0.0041 406 LEU A CD1 3137 C CD2 . LEU A 406 ? 0.3155 0.3101 0.2827 -0.0034 -0.0312 -0.0144 406 LEU A CD2 3138 N N . PRO A 407 ? 0.2506 0.2987 0.2458 0.0072 0.0059 -0.0100 407 PRO A N 3139 C CA . PRO A 407 ? 0.2425 0.2901 0.2413 0.0130 0.0041 -0.0141 407 PRO A CA 3140 C C . PRO A 407 ? 0.2430 0.2835 0.2407 0.0099 0.0005 -0.0150 407 PRO A C 3141 O O . PRO A 407 ? 0.2394 0.2877 0.2381 0.0164 -0.0011 -0.0230 407 PRO A O 3142 C CB . PRO A 407 ? 0.2493 0.2933 0.2441 0.0122 0.0071 -0.0122 407 PRO A CB 3143 C CG . PRO A 407 ? 0.2530 0.2977 0.2568 0.0158 0.0065 -0.0155 407 PRO A CG 3144 C CD . PRO A 407 ? 0.2495 0.2973 0.2494 0.0121 0.0060 -0.0161 407 PRO A CD 3145 N N . LYS A 408 ? 0.2476 0.2824 0.2417 0.0070 -0.0031 -0.0232 408 LYS A N 3146 C CA . LYS A 408 ? 0.2491 0.2725 0.2345 0.0103 -0.0074 -0.0240 408 LYS A CA 3147 C C . LYS A 408 ? 0.2430 0.2719 0.2396 0.0067 -0.0124 -0.0209 408 LYS A C 3148 O O . LYS A 408 ? 0.2372 0.2779 0.2371 0.0070 -0.0098 -0.0228 408 LYS A O 3149 C CB . LYS A 408 ? 0.2566 0.2699 0.2424 0.0062 -0.0070 -0.0337 408 LYS A CB 3150 C CG . LYS A 408 ? 0.2610 0.2738 0.2338 0.0180 -0.0118 -0.0258 408 LYS A CG 3151 C CD . LYS A 408 ? 0.2827 0.2840 0.2519 0.0122 -0.0113 -0.0374 408 LYS A CD 3152 C CE . LYS A 408 ? 0.3056 0.2949 0.2895 0.0176 -0.0166 -0.0516 408 LYS A CE 3153 N NZ . LYS A 408 ? 0.3159 0.2995 0.2851 0.0050 -0.0120 -0.0472 408 LYS A NZ 3154 N N . LYS A 409 ? 0.2394 0.2727 0.2475 0.0058 -0.0145 -0.0230 409 LYS A N 3155 C CA . LYS A 409 ? 0.2503 0.2901 0.2626 0.0047 -0.0096 -0.0200 409 LYS A CA 3156 C C . LYS A 409 ? 0.2564 0.2869 0.2504 0.0082 -0.0030 -0.0146 409 LYS A C 3157 O O . LYS A 409 ? 0.2728 0.2993 0.2681 0.0092 0.0040 -0.0103 409 LYS A O 3158 C CB . LYS A 409 ? 0.2514 0.3023 0.2793 0.0065 -0.0108 -0.0150 409 LYS A CB 3159 C CG . LYS A 409 ? 0.2733 0.3203 0.3152 0.0073 -0.0101 -0.0099 409 LYS A CG 3160 C CD . LYS A 409 ? 0.3117 0.3943 0.3726 -0.0024 -0.0088 -0.0012 409 LYS A CD 3161 C CE . LYS A 409 ? 0.3647 0.3977 0.4220 0.0002 -0.0082 -0.0045 409 LYS A CE 3162 N NZ . LYS A 409 ? 0.3796 0.4624 0.4730 -0.0106 -0.0054 -0.0043 409 LYS A NZ 3163 N N . ALA A 410 ? 0.2613 0.2953 0.2442 0.0013 0.0000 -0.0131 410 ALA A N 3164 C CA . ALA A 410 ? 0.2641 0.2901 0.2445 0.0048 0.0044 -0.0141 410 ALA A CA 3165 C C . ALA A 410 ? 0.2707 0.2949 0.2519 0.0088 0.0068 -0.0129 410 ALA A C 3166 O O . ALA A 410 ? 0.2794 0.2974 0.2347 0.0177 0.0150 -0.0230 410 ALA A O 3167 C CB . ALA A 410 ? 0.2622 0.2896 0.2413 0.0033 0.0046 -0.0036 410 ALA A CB 3168 N N . PRO A 411 ? 0.2702 0.2883 0.2434 0.0061 0.0080 -0.0191 411 PRO A N 3169 C CA . PRO A 411 ? 0.2663 0.2898 0.2436 0.0104 0.0067 -0.0151 411 PRO A CA 3170 C C . PRO A 411 ? 0.2608 0.2813 0.2432 0.0105 0.0022 -0.0128 411 PRO A C 3171 O O . PRO A 411 ? 0.2528 0.3042 0.2479 0.0136 0.0092 -0.0093 411 PRO A O 3172 C CB . PRO A 411 ? 0.2847 0.2828 0.2446 0.0076 0.0080 -0.0184 411 PRO A CB 3173 C CG . PRO A 411 ? 0.2875 0.2974 0.2618 0.0100 0.0140 -0.0128 411 PRO A CG 3174 C CD . PRO A 411 ? 0.2799 0.2941 0.2483 0.0070 0.0053 -0.0179 411 PRO A CD 3175 N N . LYS A 412 ? 0.2555 0.2879 0.2530 0.0128 0.0049 -0.0105 412 LYS A N 3176 C CA . LYS A 412 ? 0.2441 0.2762 0.2491 0.0141 -0.0004 -0.0097 412 LYS A CA 3177 C C . LYS A 412 ? 0.2450 0.2779 0.2410 0.0148 0.0010 -0.0075 412 LYS A C 3178 O O . LYS A 412 ? 0.2331 0.2902 0.2238 0.0291 0.0044 -0.0088 412 LYS A O 3179 C CB . LYS A 412 ? 0.2637 0.2871 0.2690 0.0108 -0.0009 -0.0071 412 LYS A CB 3180 C CG . LYS A 412 ? 0.3002 0.3008 0.3039 0.0094 -0.0035 -0.0031 412 LYS A CG 3181 C CD . LYS A 412 ? 0.3668 0.3122 0.3230 -0.0015 -0.0067 -0.0111 412 LYS A CD 3182 C CE . LYS A 412 ? 0.3823 0.3548 0.3486 0.0001 0.0009 -0.0150 412 LYS A CE 3183 N NZ . LYS A 412 ? 0.4120 0.3302 0.3595 0.0115 0.0026 -0.0052 412 LYS A NZ 3184 N N . ILE A 413 ? 0.2228 0.2691 0.2277 0.0162 0.0000 -0.0133 413 ILE A N 3185 C CA . ILE A 413 ? 0.2281 0.2564 0.2248 0.0074 -0.0023 -0.0130 413 ILE A CA 3186 C C . ILE A 413 ? 0.2262 0.2550 0.2228 0.0114 -0.0017 -0.0145 413 ILE A C 3187 O O . ILE A 413 ? 0.2309 0.2669 0.2246 0.0132 -0.0099 -0.0171 413 ILE A O 3188 C CB . ILE A 413 ? 0.2164 0.2565 0.2208 0.0026 0.0038 -0.0085 413 ILE A CB 3189 C CG1 . ILE A 413 ? 0.2281 0.2443 0.1970 -0.0088 -0.0014 -0.0092 413 ILE A CG1 3190 C CG2 . ILE A 413 ? 0.2192 0.2588 0.2339 -0.0060 -0.0040 -0.0070 413 ILE A CG2 3191 C CD1 . ILE A 413 ? 0.2427 0.2479 0.2324 0.0061 0.0072 -0.0159 413 ILE A CD1 3192 N N . LEU A 414 ? 0.2200 0.2467 0.2127 0.0105 -0.0104 -0.0180 414 LEU A N 3193 C CA . LEU A 414 ? 0.2242 0.2508 0.2152 0.0089 -0.0061 -0.0186 414 LEU A CA 3194 C C . LEU A 414 ? 0.2215 0.2472 0.2126 0.0111 -0.0001 -0.0166 414 LEU A C 3195 O O . LEU A 414 ? 0.2228 0.2452 0.2046 0.0222 0.0061 -0.0111 414 LEU A O 3196 C CB . LEU A 414 ? 0.2237 0.2557 0.2132 -0.0003 -0.0070 -0.0292 414 LEU A CB 3197 C CG . LEU A 414 ? 0.2276 0.2603 0.2265 0.0000 -0.0046 -0.0171 414 LEU A CG 3198 C CD1 . LEU A 414 ? 0.2329 0.2397 0.2331 0.0132 0.0026 -0.0081 414 LEU A CD1 3199 C CD2 . LEU A 414 ? 0.2327 0.2683 0.2132 0.0013 -0.0102 -0.0225 414 LEU A CD2 3200 N N . VAL A 415 ? 0.2068 0.2400 0.2151 0.0117 -0.0023 -0.0128 415 VAL A N 3201 C CA . VAL A 415 ? 0.2152 0.2489 0.2157 0.0085 0.0005 -0.0128 415 VAL A CA 3202 C C . VAL A 415 ? 0.2122 0.2483 0.2101 0.0087 -0.0020 -0.0095 415 VAL A C 3203 O O . VAL A 415 ? 0.2237 0.2593 0.2260 0.0094 -0.0173 0.0009 415 VAL A O 3204 C CB . VAL A 415 ? 0.2140 0.2407 0.2196 0.0039 0.0016 -0.0145 415 VAL A CB 3205 C CG1 . VAL A 415 ? 0.2236 0.2365 0.2329 0.0132 0.0052 -0.0122 415 VAL A CG1 3206 C CG2 . VAL A 415 ? 0.2039 0.2648 0.2144 0.0018 -0.0029 -0.0176 415 VAL A CG2 3207 N N . ALA A 416 ? 0.2020 0.2484 0.2043 0.0163 -0.0038 -0.0082 416 ALA A N 3208 C CA . ALA A 416 ? 0.2033 0.2396 0.1987 0.0092 0.0039 -0.0124 416 ALA A CA 3209 C C . ALA A 416 ? 0.1986 0.2430 0.1986 0.0108 0.0006 -0.0145 416 ALA A C 3210 O O . ALA A 416 ? 0.2068 0.2503 0.2005 0.0151 0.0034 -0.0107 416 ALA A O 3211 C CB . ALA A 416 ? 0.2040 0.2499 0.2082 0.0146 0.0109 -0.0206 416 ALA A CB 3212 N N . GLY A 417 ? 0.2069 0.2468 0.2041 0.0049 0.0098 -0.0069 417 GLY A N 3213 C CA . GLY A 417 ? 0.2036 0.2454 0.2101 0.0071 0.0032 -0.0094 417 GLY A CA 3214 C C . GLY A 417 ? 0.2198 0.2548 0.2224 0.0040 0.0008 -0.0056 417 GLY A C 3215 O O . GLY A 417 ? 0.2153 0.2517 0.2233 0.0037 -0.0031 -0.0157 417 GLY A O 3216 N N . SER A 418 ? 0.2098 0.2454 0.2250 0.0012 -0.0023 -0.0059 418 SER A N 3217 C CA . SER A 418 ? 0.2159 0.2539 0.2339 -0.0011 -0.0066 -0.0146 418 SER A CA 3218 C C . SER A 418 ? 0.2146 0.2489 0.2275 -0.0025 -0.0103 -0.0100 418 SER A C 3219 O O . SER A 418 ? 0.2490 0.2655 0.2423 -0.0105 -0.0159 -0.0137 418 SER A O 3220 C CB . SER A 418 ? 0.2276 0.2613 0.2388 -0.0016 -0.0104 -0.0073 418 SER A CB 3221 O OG . SER A 418 ? 0.2397 0.2740 0.2702 0.0112 -0.0189 -0.0193 418 SER A OG 3222 N N . HIS A 419 ? 0.2158 0.2349 0.2187 0.0011 -0.0132 -0.0088 419 HIS A N 3223 C CA . HIS A 419 ? 0.2140 0.2373 0.2159 0.0087 -0.0106 -0.0040 419 HIS A CA 3224 C C . HIS A 419 ? 0.2166 0.2403 0.2175 0.0091 -0.0144 -0.0103 419 HIS A C 3225 O O . HIS A 419 ? 0.2202 0.2446 0.2114 0.0171 -0.0100 -0.0097 419 HIS A O 3226 C CB . HIS A 419 ? 0.2128 0.2354 0.2175 0.0070 -0.0149 0.0001 419 HIS A CB 3227 C CG . HIS A 419 ? 0.2093 0.2399 0.2102 0.0089 -0.0129 0.0071 419 HIS A CG 3228 N ND1 . HIS A 419 ? 0.2117 0.2510 0.2270 0.0123 -0.0050 0.0062 419 HIS A ND1 3229 C CD2 . HIS A 419 ? 0.2077 0.2490 0.2012 0.0074 0.0019 0.0101 419 HIS A CD2 3230 C CE1 . HIS A 419 ? 0.2430 0.2552 0.2103 0.0096 -0.0017 0.0039 419 HIS A CE1 3231 N NE2 . HIS A 419 ? 0.2161 0.2398 0.2219 0.0026 -0.0109 -0.0082 419 HIS A NE2 3232 N N . ALA A 420 ? 0.2125 0.2486 0.2108 0.0134 -0.0138 -0.0044 420 ALA A N 3233 C CA . ALA A 420 ? 0.2086 0.2490 0.2053 0.0084 -0.0087 -0.0039 420 ALA A CA 3234 C C . ALA A 420 ? 0.2211 0.2454 0.2095 0.0058 -0.0094 0.0008 420 ALA A C 3235 O O . ALA A 420 ? 0.2291 0.2393 0.2176 -0.0059 -0.0114 0.0013 420 ALA A O 3236 C CB . ALA A 420 ? 0.2209 0.2638 0.2031 0.0161 -0.0046 -0.0089 420 ALA A CB 3237 N N . ASP A 421 ? 0.2204 0.2421 0.2029 0.0041 -0.0097 0.0011 421 ASP A N 3238 C CA . ASP A 421 ? 0.2301 0.2525 0.2231 0.0082 0.0014 0.0077 421 ASP A CA 3239 C C . ASP A 421 ? 0.2333 0.2549 0.2299 0.0101 0.0038 0.0044 421 ASP A C 3240 O O . ASP A 421 ? 0.2363 0.2614 0.2664 0.0184 0.0252 0.0090 421 ASP A O 3241 C CB . ASP A 421 ? 0.2426 0.2474 0.2262 0.0060 -0.0060 -0.0026 421 ASP A CB 3242 C CG . ASP A 421 ? 0.2535 0.2558 0.2397 0.0102 -0.0002 0.0044 421 ASP A CG 3243 O OD1 . ASP A 421 ? 0.3035 0.2865 0.2245 0.0035 -0.0113 -0.0093 421 ASP A OD1 3244 O OD2 . ASP A 421 ? 0.3284 0.2853 0.2804 0.0065 -0.0061 0.0049 421 ASP A OD2 3245 N N . ASN A 422 ? 0.2192 0.2504 0.2160 0.0089 0.0042 0.0000 422 ASN A N 3246 C CA . ASN A 422 ? 0.2139 0.2427 0.2080 0.0041 -0.0016 -0.0074 422 ASN A CA 3247 C C . ASN A 422 ? 0.2169 0.2356 0.2033 0.0025 -0.0031 -0.0037 422 ASN A C 3248 O O . ASN A 422 ? 0.2122 0.2490 0.1942 0.0105 -0.0096 -0.0038 422 ASN A O 3249 C CB . ASN A 422 ? 0.2154 0.2273 0.2090 0.0007 -0.0090 -0.0050 422 ASN A CB 3250 C CG . ASN A 422 ? 0.2306 0.2301 0.2192 0.0083 -0.0034 -0.0037 422 ASN A CG 3251 O OD1 . ASN A 422 ? 0.2276 0.1826 0.2169 0.0060 0.0029 0.0017 422 ASN A OD1 3252 N ND2 . ASN A 422 ? 0.2194 0.2110 0.2466 -0.0022 -0.0120 0.0014 422 ASN A ND2 3253 N N . LEU A 423 ? 0.2232 0.2374 0.1896 0.0049 0.0040 -0.0004 423 LEU A N 3254 C CA . LEU A 423 ? 0.2323 0.2337 0.1782 0.0026 -0.0049 0.0023 423 LEU A CA 3255 C C . LEU A 423 ? 0.2254 0.2260 0.1777 0.0000 -0.0051 0.0035 423 LEU A C 3256 O O . LEU A 423 ? 0.2128 0.2177 0.1943 0.0008 -0.0079 0.0090 423 LEU A O 3257 C CB . LEU A 423 ? 0.2376 0.2310 0.1745 0.0068 -0.0115 0.0008 423 LEU A CB 3258 C CG . LEU A 423 ? 0.2640 0.2367 0.1922 0.0101 -0.0109 0.0013 423 LEU A CG 3259 C CD1 . LEU A 423 ? 0.2719 0.2659 0.2381 -0.0026 -0.0012 0.0052 423 LEU A CD1 3260 C CD2 . LEU A 423 ? 0.2568 0.2584 0.1845 0.0041 -0.0192 0.0131 423 LEU A CD2 3261 N N . GLY A 424 ? 0.2183 0.2390 0.1758 0.0042 0.0061 0.0072 424 GLY A N 3262 C CA . GLY A 424 ? 0.2236 0.2418 0.1854 0.0021 -0.0029 0.0112 424 GLY A CA 3263 C C . GLY A 424 ? 0.2184 0.2338 0.1768 0.0062 0.0008 0.0094 424 GLY A C 3264 O O . GLY A 424 ? 0.2305 0.2468 0.1752 0.0035 0.0036 0.0147 424 GLY A O 3265 N N . TYR A 425 ? 0.2073 0.2303 0.1794 0.0006 -0.0049 0.0051 425 TYR A N 3266 C CA . TYR A 425 ? 0.2071 0.2158 0.1804 -0.0013 -0.0003 0.0021 425 TYR A CA 3267 C C . TYR A 425 ? 0.2112 0.2268 0.1999 0.0013 -0.0053 0.0010 425 TYR A C 3268 O O . TYR A 425 ? 0.2200 0.2222 0.2168 -0.0102 -0.0155 -0.0004 425 TYR A O 3269 C CB . TYR A 425 ? 0.2276 0.2259 0.1975 0.0048 0.0009 -0.0064 425 TYR A CB 3270 C CG . TYR A 425 ? 0.2227 0.2263 0.2008 0.0015 0.0064 -0.0048 425 TYR A CG 3271 C CD1 . TYR A 425 ? 0.2249 0.2255 0.2098 0.0028 -0.0154 0.0084 425 TYR A CD1 3272 C CD2 . TYR A 425 ? 0.2509 0.2403 0.2215 -0.0024 0.0037 -0.0166 425 TYR A CD2 3273 C CE1 . TYR A 425 ? 0.2589 0.2537 0.2311 0.0029 -0.0127 -0.0087 425 TYR A CE1 3274 C CE2 . TYR A 425 ? 0.2818 0.2573 0.2413 -0.0211 -0.0006 -0.0060 425 TYR A CE2 3275 C CZ . TYR A 425 ? 0.2442 0.2386 0.2390 -0.0073 -0.0026 -0.0119 425 TYR A CZ 3276 O OH . TYR A 425 ? 0.2872 0.2530 0.2682 -0.0179 -0.0011 -0.0145 425 TYR A OH 3277 N N . GLN A 426 ? 0.2024 0.2255 0.1899 -0.0014 -0.0104 0.0010 426 GLN A N 3278 C CA . GLN A 426 ? 0.2120 0.2455 0.2093 0.0013 -0.0086 -0.0045 426 GLN A CA 3279 C C . GLN A 426 ? 0.1972 0.2368 0.1888 0.0112 -0.0040 -0.0004 426 GLN A C 3280 O O . GLN A 426 ? 0.2112 0.2538 0.1757 -0.0087 0.0028 -0.0012 426 GLN A O 3281 C CB . GLN A 426 ? 0.2314 0.2717 0.2319 0.0156 -0.0078 -0.0064 426 GLN A CB 3282 C CG . GLN A 426 ? 0.2420 0.2954 0.2421 0.0135 -0.0127 -0.0039 426 GLN A CG 3283 C CD . GLN A 426 ? 0.2264 0.2948 0.2697 0.0258 -0.0096 -0.0299 426 GLN A CD 3284 O OE1 . GLN A 426 ? 0.2480 0.3122 0.2455 0.0333 -0.0363 -0.0523 426 GLN A OE1 3285 N NE2 . GLN A 426 ? 0.2072 0.2589 0.2414 0.0276 -0.0151 -0.0137 426 GLN A NE2 3286 N N . CYS A 427 ? 0.1882 0.2271 0.1811 0.0038 -0.0095 0.0016 427 CYS A N 3287 C CA . CYS A 427 ? 0.1969 0.2353 0.1690 0.0107 -0.0063 0.0057 427 CYS A CA 3288 C C . CYS A 427 ? 0.1964 0.2253 0.1799 0.0041 -0.0069 0.0057 427 CYS A C 3289 O O . CYS A 427 ? 0.1908 0.2264 0.1856 0.0106 -0.0122 0.0018 427 CYS A O 3290 C CB . CYS A 427 ? 0.2098 0.2365 0.1770 0.0026 -0.0025 0.0080 427 CYS A CB 3291 S SG . CYS A 427 ? 0.2414 0.2768 0.1752 0.0277 -0.0164 0.0167 427 CYS A SG 3292 N N . GLY A 428 ? 0.1877 0.2328 0.1707 0.0018 -0.0046 0.0050 428 GLY A N 3293 C CA . GLY A 428 ? 0.1864 0.2395 0.1830 0.0056 -0.0011 0.0041 428 GLY A CA 3294 C C . GLY A 428 ? 0.1843 0.2396 0.1868 0.0020 0.0013 0.0027 428 GLY A C 3295 O O . GLY A 428 ? 0.1932 0.2371 0.1916 -0.0024 -0.0074 0.0000 428 GLY A O 3296 N N . GLY A 429 ? 0.1911 0.2384 0.1864 0.0071 0.0007 0.0007 429 GLY A N 3297 C CA . GLY A 429 ? 0.1965 0.2404 0.1753 0.0093 0.0019 -0.0072 429 GLY A CA 3298 C C . GLY A 429 ? 0.2015 0.2302 0.1766 0.0069 -0.0004 -0.0045 429 GLY A C 3299 O O . GLY A 429 ? 0.2023 0.2204 0.1576 0.0062 0.0078 -0.0026 429 GLY A O 3300 N N . TRP A 430 ? 0.1935 0.2225 0.1781 0.0013 0.0012 0.0030 430 TRP A N 3301 C CA . TRP A 430 ? 0.2032 0.2236 0.1848 0.0074 0.0015 0.0046 430 TRP A CA 3302 C C . TRP A 430 ? 0.2069 0.2261 0.1850 0.0087 0.0025 0.0056 430 TRP A C 3303 O O . TRP A 430 ? 0.2016 0.2173 0.1742 0.0110 0.0041 0.0032 430 TRP A O 3304 C CB . TRP A 430 ? 0.2156 0.2304 0.1988 0.0044 0.0012 0.0044 430 TRP A CB 3305 C CG . TRP A 430 ? 0.2133 0.2364 0.2035 0.0059 -0.0043 0.0042 430 TRP A CG 3306 C CD1 . TRP A 430 ? 0.2249 0.2561 0.2129 0.0057 0.0018 0.0138 430 TRP A CD1 3307 C CD2 . TRP A 430 ? 0.1951 0.2456 0.2046 0.0062 -0.0016 0.0089 430 TRP A CD2 3308 N NE1 . TRP A 430 ? 0.2205 0.2523 0.2126 -0.0002 -0.0046 0.0084 430 TRP A NE1 3309 C CE2 . TRP A 430 ? 0.2177 0.2670 0.2095 0.0058 -0.0004 0.0072 430 TRP A CE2 3310 C CE3 . TRP A 430 ? 0.2178 0.2600 0.2073 0.0019 0.0020 0.0040 430 TRP A CE3 3311 C CZ2 . TRP A 430 ? 0.2280 0.2803 0.2256 0.0121 -0.0035 0.0018 430 TRP A CZ2 3312 C CZ3 . TRP A 430 ? 0.2068 0.2540 0.2167 0.0020 -0.0015 0.0020 430 TRP A CZ3 3313 C CH2 . TRP A 430 ? 0.2174 0.2548 0.2230 0.0051 0.0022 0.0157 430 TRP A CH2 3314 N N . THR A 431 ? 0.2085 0.2221 0.1816 0.0141 -0.0013 0.0162 431 THR A N 3315 C CA . THR A 431 ? 0.2046 0.2172 0.1916 0.0098 0.0064 0.0214 431 THR A CA 3316 C C . THR A 431 ? 0.2172 0.2181 0.1973 0.0026 0.0041 0.0141 431 THR A C 3317 O O . THR A 431 ? 0.2364 0.2115 0.1816 0.0068 0.0040 0.0110 431 THR A O 3318 C CB . THR A 431 ? 0.1892 0.2163 0.1848 0.0032 0.0043 0.0296 431 THR A CB 3319 O OG1 . THR A 431 ? 0.2103 0.1872 0.2103 0.0065 0.0077 0.0199 431 THR A OG1 3320 C CG2 . THR A 431 ? 0.1970 0.2304 0.1936 0.0171 0.0018 0.0239 431 THR A CG2 3321 N N . ILE A 432 ? 0.2117 0.2221 0.1767 -0.0018 0.0054 0.0213 432 ILE A N 3322 C CA . ILE A 432 ? 0.2263 0.2323 0.1983 -0.0007 0.0002 0.0182 432 ILE A CA 3323 C C . ILE A 432 ? 0.2212 0.2398 0.2000 -0.0002 0.0067 0.0122 432 ILE A C 3324 O O . ILE A 432 ? 0.2442 0.2782 0.2082 -0.0200 0.0060 0.0163 432 ILE A O 3325 C CB . ILE A 432 ? 0.2334 0.2391 0.1860 0.0032 0.0037 0.0206 432 ILE A CB 3326 C CG1 . ILE A 432 ? 0.2280 0.2353 0.2009 0.0010 -0.0003 0.0096 432 ILE A CG1 3327 C CG2 . ILE A 432 ? 0.2486 0.2238 0.2165 -0.0077 0.0061 0.0323 432 ILE A CG2 3328 C CD1 . ILE A 432 ? 0.2437 0.2591 0.2116 0.0013 -0.0168 0.0025 432 ILE A CD1 3329 N N . GLU A 433 ? 0.2179 0.2382 0.2129 -0.0045 0.0013 0.0063 433 GLU A N 3330 C CA . GLU A 433 ? 0.2320 0.2428 0.2215 0.0003 -0.0105 0.0046 433 GLU A CA 3331 C C . GLU A 433 ? 0.2265 0.2415 0.2219 -0.0026 -0.0045 0.0026 433 GLU A C 3332 O O . GLU A 433 ? 0.2333 0.2523 0.2156 -0.0072 -0.0046 0.0003 433 GLU A O 3333 C CB . GLU A 433 ? 0.2336 0.2297 0.2512 -0.0027 -0.0058 0.0069 433 GLU A CB 3334 C CG . GLU A 433 ? 0.2864 0.2679 0.2956 0.0032 -0.0156 0.0151 433 GLU A CG 3335 C CD . GLU A 433 ? 0.3510 0.3256 0.3400 0.0151 0.0037 0.0297 433 GLU A CD 3336 O OE1 . GLU A 433 ? 0.3602 0.3332 0.3451 -0.0041 0.0054 0.0396 433 GLU A OE1 3337 O OE2 . GLU A 433 ? 0.4394 0.3819 0.4024 0.0177 -0.0059 0.0309 433 GLU A OE2 3338 N N . TRP A 434 ? 0.2249 0.2498 0.2157 0.0036 -0.0028 0.0020 434 TRP A N 3339 C CA . TRP A 434 ? 0.2117 0.2526 0.2122 0.0055 -0.0022 0.0021 434 TRP A CA 3340 C C . TRP A 434 ? 0.2135 0.2531 0.2149 -0.0007 -0.0014 0.0009 434 TRP A C 3341 O O . TRP A 434 ? 0.2060 0.2530 0.2108 -0.0053 -0.0043 -0.0055 434 TRP A O 3342 C CB . TRP A 434 ? 0.2310 0.2603 0.2329 -0.0026 -0.0020 0.0080 434 TRP A CB 3343 C CG . TRP A 434 ? 0.2199 0.2533 0.2212 0.0083 -0.0008 0.0031 434 TRP A CG 3344 C CD1 . TRP A 434 ? 0.2363 0.2607 0.2334 0.0033 0.0008 0.0129 434 TRP A CD1 3345 C CD2 . TRP A 434 ? 0.2183 0.2639 0.2275 -0.0077 0.0039 0.0067 434 TRP A CD2 3346 N NE1 . TRP A 434 ? 0.2372 0.2879 0.2510 0.0028 -0.0101 0.0050 434 TRP A NE1 3347 C CE2 . TRP A 434 ? 0.2197 0.2718 0.2235 0.0002 -0.0009 0.0048 434 TRP A CE2 3348 C CE3 . TRP A 434 ? 0.2477 0.2852 0.2289 0.0014 0.0012 0.0043 434 TRP A CE3 3349 C CZ2 . TRP A 434 ? 0.2421 0.2834 0.2519 -0.0059 -0.0151 0.0047 434 TRP A CZ2 3350 C CZ3 . TRP A 434 ? 0.2392 0.2814 0.2497 -0.0129 -0.0098 0.0079 434 TRP A CZ3 3351 C CH2 . TRP A 434 ? 0.2410 0.2734 0.2551 -0.0061 -0.0144 0.0099 434 TRP A CH2 3352 N N . GLN A 435 ? 0.2188 0.2627 0.2144 -0.0012 0.0044 -0.0056 435 GLN A N 3353 C CA . GLN A 435 ? 0.2213 0.2705 0.2206 -0.0055 -0.0020 -0.0042 435 GLN A CA 3354 C C . GLN A 435 ? 0.2239 0.2713 0.2256 0.0001 0.0002 -0.0013 435 GLN A C 3355 O O . GLN A 435 ? 0.2110 0.3050 0.2472 -0.0001 -0.0076 -0.0025 435 GLN A O 3356 C CB . GLN A 435 ? 0.2313 0.2682 0.2280 -0.0059 0.0020 -0.0012 435 GLN A CB 3357 C CG . GLN A 435 ? 0.2279 0.2839 0.2302 -0.0135 -0.0033 0.0013 435 GLN A CG 3358 C CD . GLN A 435 ? 0.2262 0.2654 0.2438 -0.0071 -0.0059 -0.0022 435 GLN A CD 3359 O OE1 . GLN A 435 ? 0.2441 0.2983 0.2317 -0.0123 -0.0065 0.0047 435 GLN A OE1 3360 N NE2 . GLN A 435 ? 0.2288 0.2531 0.2581 -0.0156 -0.0043 -0.0030 435 GLN A NE2 3361 N N . GLY A 436 ? 0.2147 0.2699 0.2310 -0.0005 -0.0032 -0.0022 436 GLY A N 3362 C CA . GLY A 436 ? 0.2280 0.2569 0.2299 0.0004 0.0038 0.0014 436 GLY A CA 3363 C C . GLY A 436 ? 0.2387 0.2627 0.2325 -0.0049 0.0056 0.0006 436 GLY A C 3364 O O . GLY A 436 ? 0.2357 0.2522 0.2297 -0.0156 0.0046 -0.0080 436 GLY A O 3365 N N . ASP A 437 ? 0.2476 0.2660 0.2377 -0.0056 0.0066 0.0032 437 ASP A N 3366 C CA . ASP A 437 ? 0.2566 0.2716 0.2505 0.0035 0.0088 0.0051 437 ASP A CA 3367 C C . ASP A 437 ? 0.2605 0.2713 0.2531 -0.0004 0.0078 0.0033 437 ASP A C 3368 O O . ASP A 437 ? 0.2486 0.2617 0.2496 0.0050 0.0148 0.0095 437 ASP A O 3369 C CB . ASP A 437 ? 0.2688 0.2843 0.2575 0.0024 0.0106 0.0096 437 ASP A CB 3370 C CG . ASP A 437 ? 0.3164 0.3134 0.2836 -0.0034 0.0098 0.0059 437 ASP A CG 3371 O OD1 . ASP A 437 ? 0.3294 0.3023 0.3020 -0.0241 0.0211 0.0152 437 ASP A OD1 3372 O OD2 . ASP A 437 ? 0.3951 0.3499 0.3243 -0.0121 0.0202 0.0310 437 ASP A OD2 3373 N N . THR A 438 ? 0.2649 0.2674 0.2598 0.0032 0.0056 0.0063 438 THR A N 3374 C CA . THR A 438 ? 0.2636 0.2612 0.2584 0.0009 0.0044 0.0038 438 THR A CA 3375 C C . THR A 438 ? 0.2716 0.2708 0.2502 0.0017 0.0024 0.0036 438 THR A C 3376 O O . THR A 438 ? 0.2863 0.2865 0.2664 0.0025 0.0042 0.0118 438 THR A O 3377 C CB . THR A 438 ? 0.2706 0.2727 0.2534 0.0002 0.0039 0.0038 438 THR A CB 3378 O OG1 . THR A 438 ? 0.2723 0.2516 0.2755 0.0026 0.0100 0.0065 438 THR A OG1 3379 C CG2 . THR A 438 ? 0.2733 0.2621 0.2684 -0.0119 0.0025 -0.0056 438 THR A CG2 3380 N N . GLY A 439 ? 0.2584 0.2701 0.2375 0.0090 -0.0021 0.0009 439 GLY A N 3381 C CA . GLY A 439 ? 0.2674 0.2658 0.2448 0.0088 -0.0074 0.0066 439 GLY A CA 3382 C C . GLY A 439 ? 0.2783 0.2706 0.2477 0.0125 -0.0065 0.0040 439 GLY A C 3383 O O . GLY A 439 ? 0.2814 0.2656 0.2369 -0.0022 -0.0132 0.0128 439 GLY A O 3384 N N . ARG A 440 ? 0.2741 0.2715 0.2486 0.0136 -0.0078 0.0092 440 ARG A N 3385 C CA . ARG A 440 ? 0.2870 0.2800 0.2643 0.0180 -0.0059 0.0043 440 ARG A CA 3386 C C . ARG A 440 ? 0.2884 0.2839 0.2753 0.0206 -0.0015 0.0103 440 ARG A C 3387 O O . ARG A 440 ? 0.3005 0.2967 0.2906 0.0303 0.0039 0.0158 440 ARG A O 3388 C CB . ARG A 440 ? 0.2958 0.2905 0.2761 0.0166 -0.0108 0.0053 440 ARG A CB 3389 C CG . ARG A 440 ? 0.3304 0.3344 0.3205 0.0018 -0.0110 -0.0034 440 ARG A CG 3390 C CD . ARG A 440 ? 0.4047 0.5086 0.4488 0.0382 -0.0310 -0.0401 440 ARG A CD 3391 N NE . ARG A 440 ? 0.4696 0.4240 0.3365 -0.0534 0.0375 0.0658 440 ARG A NE 3392 C CZ . ARG A 440 ? 0.5886 0.6346 0.5887 0.1041 0.0032 -0.0032 440 ARG A CZ 3393 N NH1 . ARG A 440 ? 0.4900 0.4261 0.3747 -0.0401 -0.0357 -0.0484 440 ARG A NH1 3394 N NH2 . ARG A 440 ? 0.4112 0.3444 0.4676 -0.0815 0.0223 0.0024 440 ARG A NH2 3395 N N . THR A 441 ? 0.2814 0.2737 0.2663 0.0180 -0.0074 0.0103 441 THR A N 3396 C CA . THR A 441 ? 0.2755 0.2709 0.2680 0.0153 -0.0108 0.0070 441 THR A CA 3397 C C . THR A 441 ? 0.2680 0.2604 0.2579 0.0121 -0.0048 0.0101 441 THR A C 3398 O O . THR A 441 ? 0.2767 0.2700 0.2664 0.0158 0.0030 0.0164 441 THR A O 3399 C CB . THR A 441 ? 0.2787 0.2736 0.2668 0.0134 -0.0166 0.0033 441 THR A CB 3400 O OG1 . THR A 441 ? 0.2897 0.2868 0.3023 0.0192 -0.0152 0.0148 441 THR A OG1 3401 C CG2 . THR A 441 ? 0.2907 0.2897 0.2994 0.0012 -0.0169 -0.0058 441 THR A CG2 3402 N N . THR A 442 ? 0.2588 0.2544 0.2435 0.0130 -0.0047 0.0072 442 THR A N 3403 C CA . THR A 442 ? 0.2414 0.2430 0.2200 0.0084 -0.0003 0.0090 442 THR A CA 3404 C C . THR A 442 ? 0.2448 0.2418 0.2161 0.0048 -0.0012 0.0081 442 THR A C 3405 O O . THR A 442 ? 0.2428 0.2595 0.2234 0.0065 0.0029 0.0005 442 THR A O 3406 C CB . THR A 442 ? 0.2475 0.2402 0.2230 0.0032 0.0035 0.0084 442 THR A CB 3407 O OG1 . THR A 442 ? 0.2485 0.2537 0.2059 0.0145 -0.0041 0.0151 442 THR A OG1 3408 C CG2 . THR A 442 ? 0.2412 0.2372 0.2014 0.0058 0.0100 0.0202 442 THR A CG2 3409 N N . VAL A 443 ? 0.2291 0.2474 0.1982 0.0040 -0.0023 0.0151 443 VAL A N 3410 C CA . VAL A 443 ? 0.2309 0.2475 0.2001 0.0020 0.0013 0.0083 443 VAL A CA 3411 C C . VAL A 443 ? 0.2218 0.2483 0.1938 0.0084 0.0034 0.0079 443 VAL A C 3412 O O . VAL A 443 ? 0.2445 0.2661 0.2093 0.0154 0.0126 0.0121 443 VAL A O 3413 C CB . VAL A 443 ? 0.2341 0.2547 0.2076 -0.0036 0.0041 0.0068 443 VAL A CB 3414 C CG1 . VAL A 443 ? 0.2185 0.2737 0.2292 -0.0006 -0.0034 0.0019 443 VAL A CG1 3415 C CG2 . VAL A 443 ? 0.2894 0.2690 0.2166 0.0123 0.0037 0.0166 443 VAL A CG2 3416 N N . GLY A 444 ? 0.2275 0.2445 0.1753 0.0121 0.0050 0.0080 444 GLY A N 3417 C CA . GLY A 444 ? 0.2167 0.2418 0.1818 0.0146 0.0225 0.0091 444 GLY A CA 3418 C C . GLY A 444 ? 0.2182 0.2406 0.1915 0.0246 0.0138 0.0075 444 GLY A C 3419 O O . GLY A 444 ? 0.2496 0.2490 0.2020 0.0372 0.0238 0.0136 444 GLY A O 3420 N N . THR A 445 ? 0.2022 0.2326 0.1794 0.0186 0.0120 0.0038 445 THR A N 3421 C CA . THR A 445 ? 0.2081 0.2453 0.1889 0.0164 -0.0015 -0.0051 445 THR A CA 3422 C C . THR A 445 ? 0.2135 0.2368 0.1890 0.0109 -0.0036 -0.0069 445 THR A C 3423 O O . THR A 445 ? 0.1986 0.2163 0.1733 0.0110 -0.0214 -0.0090 445 THR A O 3424 C CB . THR A 445 ? 0.2221 0.2501 0.1987 0.0156 -0.0024 -0.0057 445 THR A CB 3425 O OG1 . THR A 445 ? 0.2147 0.2820 0.2080 0.0237 -0.0110 -0.0160 445 THR A OG1 3426 C CG2 . THR A 445 ? 0.2007 0.2688 0.2005 0.0101 0.0045 -0.0026 445 THR A CG2 3427 N N . THR A 446 ? 0.2082 0.2307 0.1883 0.0075 -0.0086 -0.0077 446 THR A N 3428 C CA . THR A 446 ? 0.2057 0.2327 0.1931 0.0078 0.0071 -0.0045 446 THR A CA 3429 C C . THR A 446 ? 0.2029 0.2261 0.1785 0.0035 0.0009 -0.0030 446 THR A C 3430 O O . THR A 446 ? 0.2024 0.2374 0.1723 0.0046 0.0077 -0.0072 446 THR A O 3431 C CB . THR A 446 ? 0.1933 0.2317 0.2040 0.0029 0.0071 -0.0036 446 THR A CB 3432 O OG1 . THR A 446 ? 0.2167 0.2219 0.2348 0.0194 0.0027 -0.0050 446 THR A OG1 3433 C CG2 . THR A 446 ? 0.2169 0.2457 0.2270 -0.0001 0.0231 0.0076 446 THR A CG2 3434 N N . ILE A 447 ? 0.1976 0.2224 0.1676 0.0066 0.0006 0.0031 447 ILE A N 3435 C CA . ILE A 447 ? 0.1994 0.2322 0.1694 0.0055 -0.0097 0.0027 447 ILE A CA 3436 C C . ILE A 447 ? 0.2024 0.2346 0.1747 0.0028 -0.0070 -0.0064 447 ILE A C 3437 O O . ILE A 447 ? 0.2023 0.2418 0.1888 0.0081 -0.0051 -0.0055 447 ILE A O 3438 C CB . ILE A 447 ? 0.1977 0.2302 0.1584 0.0080 -0.0074 0.0112 447 ILE A CB 3439 C CG1 . ILE A 447 ? 0.2112 0.2455 0.1982 0.0176 -0.0278 -0.0038 447 ILE A CG1 3440 C CG2 . ILE A 447 ? 0.2013 0.2511 0.1793 0.0072 0.0058 0.0108 447 ILE A CG2 3441 C CD1 . ILE A 447 ? 0.2498 0.2609 0.1926 0.0372 -0.0327 0.0247 447 ILE A CD1 3442 N N . LEU A 448 ? 0.2100 0.2281 0.1889 0.0089 -0.0127 -0.0045 448 LEU A N 3443 C CA . LEU A 448 ? 0.2176 0.2381 0.1980 0.0090 -0.0110 -0.0065 448 LEU A CA 3444 C C . LEU A 448 ? 0.2234 0.2468 0.2034 0.0097 -0.0096 -0.0094 448 LEU A C 3445 O O . LEU A 448 ? 0.2214 0.2508 0.2001 0.0055 -0.0036 -0.0149 448 LEU A O 3446 C CB . LEU A 448 ? 0.2250 0.2307 0.2132 0.0113 -0.0062 -0.0061 448 LEU A CB 3447 C CG . LEU A 448 ? 0.2214 0.2360 0.2105 0.0109 0.0021 -0.0002 448 LEU A CG 3448 C CD1 . LEU A 448 ? 0.2409 0.2628 0.2343 0.0231 0.0152 -0.0099 448 LEU A CD1 3449 C CD2 . LEU A 448 ? 0.2571 0.2467 0.2396 0.0035 -0.0109 -0.0009 448 LEU A CD2 3450 N N . GLU A 449 ? 0.2266 0.2516 0.1882 0.0143 -0.0096 -0.0095 449 GLU A N 3451 C CA . GLU A 449 ? 0.2374 0.2737 0.2077 0.0122 -0.0068 -0.0084 449 GLU A CA 3452 C C . GLU A 449 ? 0.2218 0.2690 0.1994 0.0150 -0.0033 -0.0085 449 GLU A C 3453 O O . GLU A 449 ? 0.2050 0.2745 0.2005 0.0206 -0.0138 -0.0045 449 GLU A O 3454 C CB . GLU A 449 ? 0.2198 0.2770 0.2022 0.0065 0.0019 -0.0020 449 GLU A CB 3455 C CG . GLU A 449 ? 0.2853 0.2866 0.2367 0.0048 0.0004 0.0007 449 GLU A CG 3456 C CD . GLU A 449 ? 0.3018 0.3017 0.2682 0.0085 0.0185 0.0111 449 GLU A CD 3457 O OE1 . GLU A 449 ? 0.3256 0.2619 0.2386 0.0155 0.0003 0.0077 449 GLU A OE1 3458 O OE2 . GLU A 449 ? 0.4500 0.3761 0.3882 0.0005 0.0344 0.0412 449 GLU A OE2 3459 N N . ALA A 450 ? 0.2092 0.2582 0.1848 0.0139 -0.0016 -0.0082 450 ALA A N 3460 C CA . ALA A 450 ? 0.2118 0.2570 0.1948 0.0189 -0.0022 -0.0062 450 ALA A CA 3461 C C . ALA A 450 ? 0.2123 0.2525 0.1944 0.0135 -0.0011 -0.0109 450 ALA A C 3462 O O . ALA A 450 ? 0.2087 0.2496 0.1938 0.0071 -0.0053 -0.0219 450 ALA A O 3463 C CB . ALA A 450 ? 0.2225 0.2350 0.2039 0.0139 -0.0030 0.0013 450 ALA A CB 3464 N N . VAL A 451 ? 0.2087 0.2571 0.1819 0.0200 -0.0074 -0.0128 451 VAL A N 3465 C CA . VAL A 451 ? 0.1973 0.2523 0.1894 0.0152 -0.0065 -0.0112 451 VAL A CA 3466 C C . VAL A 451 ? 0.2125 0.2579 0.2024 0.0091 -0.0090 -0.0124 451 VAL A C 3467 O O . VAL A 451 ? 0.2002 0.2818 0.2025 0.0120 -0.0161 -0.0088 451 VAL A O 3468 C CB . VAL A 451 ? 0.1953 0.2459 0.1732 0.0172 -0.0031 -0.0114 451 VAL A CB 3469 C CG1 . VAL A 451 ? 0.1903 0.2577 0.1908 0.0207 -0.0083 -0.0209 451 VAL A CG1 3470 C CG2 . VAL A 451 ? 0.1937 0.2570 0.1996 0.0108 -0.0110 -0.0061 451 VAL A CG2 3471 N N . LYS A 452 ? 0.2207 0.2624 0.2068 0.0169 -0.0137 -0.0115 452 LYS A N 3472 C CA . LYS A 452 ? 0.2273 0.2627 0.2274 0.0151 -0.0167 -0.0147 452 LYS A CA 3473 C C . LYS A 452 ? 0.2286 0.2736 0.2354 0.0153 -0.0158 -0.0174 452 LYS A C 3474 O O . LYS A 452 ? 0.2206 0.2864 0.2452 0.0225 -0.0135 -0.0263 452 LYS A O 3475 C CB . LYS A 452 ? 0.2105 0.2519 0.2209 0.0120 -0.0088 -0.0125 452 LYS A CB 3476 C CG . LYS A 452 ? 0.2623 0.2696 0.2681 0.0076 -0.0071 -0.0129 452 LYS A CG 3477 C CD . LYS A 452 ? 0.3129 0.3245 0.3366 -0.0091 0.0139 0.0012 452 LYS A CD 3478 C CE . LYS A 452 ? 0.3988 0.3944 0.4018 -0.0075 0.0040 -0.0092 452 LYS A CE 3479 N NZ . LYS A 452 ? 0.4398 0.4368 0.4388 -0.0050 0.0079 0.0191 452 LYS A NZ 3480 N N . ALA A 453 ? 0.2200 0.2769 0.2235 0.0199 -0.0146 -0.0183 453 ALA A N 3481 C CA . ALA A 453 ? 0.2219 0.2815 0.2342 0.0172 -0.0076 -0.0167 453 ALA A CA 3482 C C . ALA A 453 ? 0.2265 0.2886 0.2381 0.0123 -0.0078 -0.0192 453 ALA A C 3483 O O . ALA A 453 ? 0.2206 0.3267 0.2332 0.0058 -0.0074 -0.0230 453 ALA A O 3484 C CB . ALA A 453 ? 0.2266 0.2890 0.2344 0.0134 -0.0048 -0.0175 453 ALA A CB 3485 N N . ALA A 454 ? 0.2158 0.2843 0.2233 0.0169 -0.0089 -0.0194 454 ALA A N 3486 C CA . ALA A 454 ? 0.2235 0.2811 0.2296 0.0154 -0.0068 -0.0193 454 ALA A CA 3487 C C . ALA A 454 ? 0.2197 0.2787 0.2404 0.0123 -0.0056 -0.0164 454 ALA A C 3488 O O . ALA A 454 ? 0.2387 0.2997 0.2561 0.0077 -0.0068 -0.0321 454 ALA A O 3489 C CB . ALA A 454 ? 0.2182 0.2893 0.2378 0.0175 -0.0122 -0.0081 454 ALA A CB 3490 N N . VAL A 455 ? 0.2177 0.2778 0.2340 0.0119 -0.0045 -0.0228 455 VAL A N 3491 C CA . VAL A 455 ? 0.2158 0.2840 0.2353 0.0130 -0.0075 -0.0157 455 VAL A CA 3492 C C . VAL A 455 ? 0.2221 0.2917 0.2374 0.0163 -0.0036 -0.0074 455 VAL A C 3493 O O . VAL A 455 ? 0.2282 0.3158 0.2269 0.0210 -0.0089 -0.0178 455 VAL A O 3494 C CB . VAL A 455 ? 0.2163 0.2687 0.2387 0.0119 -0.0082 -0.0091 455 VAL A CB 3495 C CG1 . VAL A 455 ? 0.2348 0.2904 0.2386 0.0156 -0.0163 -0.0055 455 VAL A CG1 3496 C CG2 . VAL A 455 ? 0.2308 0.2797 0.2391 0.0011 -0.0020 -0.0157 455 VAL A CG2 3497 N N . ASP A 456 ? 0.2169 0.3097 0.2399 0.0119 -0.0041 -0.0078 456 ASP A N 3498 C CA . ASP A 456 ? 0.2249 0.3095 0.2441 0.0158 -0.0058 -0.0076 456 ASP A CA 3499 C C . ASP A 456 ? 0.2336 0.3130 0.2491 0.0115 -0.0032 -0.0115 456 ASP A C 3500 O O . ASP A 456 ? 0.2218 0.3125 0.2404 0.0119 -0.0092 -0.0174 456 ASP A O 3501 C CB . ASP A 456 ? 0.2187 0.3182 0.2551 0.0105 -0.0010 -0.0042 456 ASP A CB 3502 C CG . ASP A 456 ? 0.2567 0.3326 0.2841 0.0089 -0.0081 -0.0049 456 ASP A CG 3503 O OD1 . ASP A 456 ? 0.2940 0.3450 0.3136 0.0104 -0.0107 -0.0109 456 ASP A OD1 3504 O OD2 . ASP A 456 ? 0.2738 0.3785 0.3368 -0.0068 -0.0121 -0.0208 456 ASP A OD2 3505 N N . PRO A 457 ? 0.2364 0.3058 0.2438 0.0131 -0.0129 -0.0131 457 PRO A N 3506 C CA . PRO A 457 ? 0.2489 0.3115 0.2561 0.0104 -0.0196 -0.0138 457 PRO A CA 3507 C C . PRO A 457 ? 0.2451 0.3078 0.2555 0.0138 -0.0217 -0.0112 457 PRO A C 3508 O O . PRO A 457 ? 0.2701 0.3308 0.2716 0.0133 -0.0223 -0.0174 457 PRO A O 3509 C CB . PRO A 457 ? 0.2450 0.3083 0.2518 0.0113 -0.0219 -0.0099 457 PRO A CB 3510 C CG . PRO A 457 ? 0.2625 0.3033 0.2557 0.0101 -0.0185 -0.0069 457 PRO A CG 3511 C CD . PRO A 457 ? 0.2427 0.3155 0.2582 0.0099 -0.0135 -0.0155 457 PRO A CD 3512 N N . SER A 458 ? 0.2451 0.3144 0.2556 0.0172 -0.0226 -0.0126 458 SER A N 3513 C CA . SER A 458 ? 0.2492 0.3113 0.2635 0.0165 -0.0221 -0.0144 458 SER A CA 3514 C C . SER A 458 ? 0.2554 0.3080 0.2605 0.0165 -0.0217 -0.0190 458 SER A C 3515 O O . SER A 458 ? 0.2677 0.3223 0.2692 0.0285 -0.0325 -0.0214 458 SER A O 3516 C CB . SER A 458 ? 0.2591 0.3127 0.2696 0.0106 -0.0138 -0.0107 458 SER A CB 3517 O OG . SER A 458 ? 0.2685 0.3213 0.3065 0.0149 -0.0201 -0.0169 458 SER A OG 3518 N N . THR A 459 ? 0.2399 0.2999 0.2404 0.0177 -0.0250 -0.0153 459 THR A N 3519 C CA . THR A 459 ? 0.2342 0.2961 0.2347 0.0116 -0.0183 -0.0100 459 THR A CA 3520 C C . THR A 459 ? 0.2403 0.2971 0.2366 0.0096 -0.0142 -0.0106 459 THR A C 3521 O O . THR A 459 ? 0.2622 0.3179 0.2418 0.0040 -0.0097 -0.0105 459 THR A O 3522 C CB . THR A 459 ? 0.2306 0.2844 0.2236 0.0066 -0.0184 -0.0076 459 THR A CB 3523 O OG1 . THR A 459 ? 0.2233 0.3090 0.2295 0.0035 -0.0156 -0.0094 459 THR A OG1 3524 C CG2 . THR A 459 ? 0.2121 0.3063 0.2184 0.0137 -0.0182 -0.0037 459 THR A CG2 3525 N N . VAL A 460 ? 0.2439 0.2870 0.2392 0.0145 -0.0073 -0.0087 460 VAL A N 3526 C CA . VAL A 460 ? 0.2402 0.2848 0.2397 0.0145 -0.0041 -0.0070 460 VAL A CA 3527 C C . VAL A 460 ? 0.2496 0.2958 0.2379 0.0152 -0.0030 -0.0060 460 VAL A C 3528 O O . VAL A 460 ? 0.2506 0.3100 0.2258 0.0218 0.0021 0.0038 460 VAL A O 3529 C CB . VAL A 460 ? 0.2397 0.2805 0.2448 0.0151 -0.0012 -0.0099 460 VAL A CB 3530 C CG1 . VAL A 460 ? 0.2615 0.2843 0.2624 0.0093 -0.0042 -0.0040 460 VAL A CG1 3531 C CG2 . VAL A 460 ? 0.2309 0.2714 0.2459 0.0267 0.0028 -0.0065 460 VAL A CG2 3532 N N . VAL A 461 ? 0.2380 0.2881 0.2297 0.0097 -0.0013 -0.0083 461 VAL A N 3533 C CA . VAL A 461 ? 0.2497 0.2768 0.2346 0.0099 0.0027 -0.0154 461 VAL A CA 3534 C C . VAL A 461 ? 0.2538 0.2813 0.2409 0.0071 -0.0027 -0.0108 461 VAL A C 3535 O O . VAL A 461 ? 0.2763 0.2841 0.2352 0.0078 -0.0092 0.0001 461 VAL A O 3536 C CB . VAL A 461 ? 0.2497 0.2747 0.2454 0.0074 0.0003 -0.0213 461 VAL A CB 3537 C CG1 . VAL A 461 ? 0.2345 0.2725 0.2264 0.0164 0.0035 -0.0270 461 VAL A CG1 3538 C CG2 . VAL A 461 ? 0.2386 0.2450 0.2220 0.0050 0.0036 -0.0221 461 VAL A CG2 3539 N N . VAL A 462 ? 0.2474 0.2752 0.2316 0.0124 -0.0057 -0.0100 462 VAL A N 3540 C CA . VAL A 462 ? 0.2396 0.2692 0.2422 0.0115 -0.0050 -0.0119 462 VAL A CA 3541 C C . VAL A 462 ? 0.2473 0.2644 0.2412 0.0122 -0.0023 -0.0109 462 VAL A C 3542 O O . VAL A 462 ? 0.2518 0.2690 0.2394 0.0074 -0.0050 -0.0035 462 VAL A O 3543 C CB . VAL A 462 ? 0.2402 0.2757 0.2539 0.0107 -0.0047 -0.0175 462 VAL A CB 3544 C CG1 . VAL A 462 ? 0.2532 0.2688 0.2761 0.0042 -0.0052 -0.0221 462 VAL A CG1 3545 C CG2 . VAL A 462 ? 0.2423 0.2829 0.2525 0.0240 -0.0043 -0.0168 462 VAL A CG2 3546 N N . PHE A 463 ? 0.2420 0.2612 0.2404 0.0097 -0.0010 -0.0096 463 PHE A N 3547 C CA . PHE A 463 ? 0.2523 0.2761 0.2461 0.0047 0.0015 -0.0066 463 PHE A CA 3548 C C . PHE A 463 ? 0.2548 0.2785 0.2550 0.0037 0.0015 -0.0072 463 PHE A C 3549 O O . PHE A 463 ? 0.2671 0.2771 0.2632 0.0011 -0.0117 -0.0078 463 PHE A O 3550 C CB . PHE A 463 ? 0.2587 0.2840 0.2622 0.0079 0.0031 -0.0069 463 PHE A CB 3551 C CG . PHE A 463 ? 0.2600 0.2930 0.2634 -0.0007 0.0033 -0.0095 463 PHE A CG 3552 C CD1 . PHE A 463 ? 0.2745 0.2930 0.2734 0.0082 0.0038 -0.0153 463 PHE A CD1 3553 C CD2 . PHE A 463 ? 0.2843 0.3098 0.3190 0.0018 0.0044 0.0123 463 PHE A CD2 3554 C CE1 . PHE A 463 ? 0.2757 0.2886 0.2908 0.0123 -0.0025 -0.0073 463 PHE A CE1 3555 C CE2 . PHE A 463 ? 0.2853 0.3310 0.3119 0.0022 0.0041 0.0065 463 PHE A CE2 3556 C CZ . PHE A 463 ? 0.2767 0.3028 0.3127 0.0154 0.0076 -0.0027 463 PHE A CZ 3557 N N . ALA A 464 ? 0.2627 0.2836 0.2576 0.0044 0.0005 -0.0071 464 ALA A N 3558 C CA . ALA A 464 ? 0.2751 0.2982 0.2764 0.0051 -0.0011 -0.0107 464 ALA A CA 3559 C C . ALA A 464 ? 0.2829 0.3002 0.2805 0.0031 -0.0030 -0.0076 464 ALA A C 3560 O O . ALA A 464 ? 0.2833 0.2912 0.2719 0.0026 -0.0069 -0.0108 464 ALA A O 3561 C CB . ALA A 464 ? 0.2746 0.3038 0.2711 0.0059 0.0061 -0.0116 464 ALA A CB 3562 N N . GLU A 465 ? 0.2907 0.3100 0.2983 0.0000 -0.0028 -0.0062 465 GLU A N 3563 C CA . GLU A 465 ? 0.3030 0.3109 0.3159 0.0022 -0.0030 -0.0073 465 GLU A CA 3564 C C . GLU A 465 ? 0.3020 0.3093 0.3181 -0.0028 -0.0017 -0.0091 465 GLU A C 3565 O O . GLU A 465 ? 0.3168 0.3079 0.3191 -0.0079 -0.0137 -0.0142 465 GLU A O 3566 C CB . GLU A 465 ? 0.3160 0.3216 0.3201 0.0046 0.0023 -0.0072 465 GLU A CB 3567 C CG . GLU A 465 ? 0.3447 0.3601 0.3738 0.0130 -0.0057 -0.0040 465 GLU A CG 3568 C CD . GLU A 465 ? 0.4128 0.4356 0.4244 0.0030 0.0128 0.0042 465 GLU A CD 3569 O OE1 . GLU A 465 ? 0.4452 0.4458 0.4673 0.0125 0.0090 -0.0024 465 GLU A OE1 3570 O OE2 . GLU A 465 ? 0.4311 0.4848 0.4882 0.0041 0.0053 -0.0121 465 GLU A OE2 3571 N N . ASN A 466 ? 0.2962 0.3111 0.3184 -0.0002 0.0016 -0.0135 466 ASN A N 3572 C CA . ASN A 466 ? 0.3042 0.3163 0.3209 0.0010 0.0067 -0.0114 466 ASN A CA 3573 C C . ASN A 466 ? 0.3097 0.3180 0.3205 0.0021 0.0063 -0.0138 466 ASN A C 3574 O O . ASN A 466 ? 0.3189 0.3219 0.3354 -0.0005 0.0137 -0.0154 466 ASN A O 3575 C CB A ASN A 466 ? 0.3058 0.3238 0.3235 0.0021 0.0044 -0.0105 466 ASN A CB 3576 C CB B ASN A 466 ? 0.3042 0.3211 0.3229 0.0009 0.0052 -0.0100 466 ASN A CB 3577 C CG A ASN A 466 ? 0.3126 0.3255 0.3174 0.0062 0.0041 -0.0091 466 ASN A CG 3578 C CG B ASN A 466 ? 0.3092 0.3132 0.3130 0.0005 0.0073 -0.0060 466 ASN A CG 3579 O OD1 A ASN A 466 ? 0.3444 0.3659 0.3411 -0.0002 0.0022 -0.0101 466 ASN A OD1 3580 O OD1 B ASN A 466 ? 0.2741 0.3079 0.2870 -0.0035 0.0020 -0.0070 466 ASN A OD1 3581 N ND2 A ASN A 466 ? 0.2929 0.3342 0.3044 0.0077 -0.0040 -0.0120 466 ASN A ND2 3582 N ND2 B ASN A 466 ? 0.3083 0.3356 0.3291 -0.0078 0.0072 -0.0019 466 ASN A ND2 3583 N N . PRO A 467 ? 0.3086 0.3171 0.3165 0.0019 0.0056 -0.0138 467 PRO A N 3584 C CA . PRO A 467 ? 0.3139 0.3196 0.3163 0.0039 0.0028 -0.0165 467 PRO A CA 3585 C C . PRO A 467 ? 0.3291 0.3305 0.3272 0.0021 0.0001 -0.0150 467 PRO A C 3586 O O . PRO A 467 ? 0.3201 0.3217 0.3195 -0.0005 -0.0029 -0.0241 467 PRO A O 3587 C CB . PRO A 467 ? 0.3179 0.3164 0.3189 0.0018 0.0032 -0.0140 467 PRO A CB 3588 C CG . PRO A 467 ? 0.3012 0.3181 0.3160 0.0007 0.0001 -0.0118 467 PRO A CG 3589 C CD . PRO A 467 ? 0.3002 0.3122 0.3058 -0.0013 0.0049 -0.0135 467 PRO A CD 3590 N N . ASP A 468 ? 0.3473 0.3385 0.3383 -0.0013 -0.0035 -0.0163 468 ASP A N 3591 C CA . ASP A 468 ? 0.3585 0.3501 0.3454 0.0010 -0.0030 -0.0143 468 ASP A CA 3592 C C . ASP A 468 ? 0.3559 0.3435 0.3366 0.0043 -0.0033 -0.0129 468 ASP A C 3593 O O . ASP A 468 ? 0.3425 0.3445 0.3178 0.0048 0.0012 -0.0209 468 ASP A O 3594 C CB . ASP A 468 ? 0.3741 0.3592 0.3685 -0.0029 -0.0024 -0.0110 468 ASP A CB 3595 C CG . ASP A 468 ? 0.3932 0.3798 0.4029 0.0024 0.0012 -0.0112 468 ASP A CG 3596 O OD1 . ASP A 468 ? 0.4519 0.4120 0.4653 -0.0228 0.0018 -0.0146 468 ASP A OD1 3597 O OD2 . ASP A 468 ? 0.3866 0.3495 0.4130 -0.0084 0.0016 -0.0239 468 ASP A OD2 3598 N N . ALA A 469 ? 0.3543 0.3393 0.3262 0.0076 -0.0061 -0.0177 469 ALA A N 3599 C CA . ALA A 469 ? 0.3569 0.3365 0.3254 0.0078 -0.0088 -0.0098 469 ALA A CA 3600 C C . ALA A 469 ? 0.3512 0.3261 0.3187 0.0090 -0.0047 -0.0123 469 ALA A C 3601 O O . ALA A 469 ? 0.3417 0.3105 0.3131 0.0186 -0.0087 -0.0138 469 ALA A O 3602 C CB . ALA A 469 ? 0.3663 0.3542 0.3312 0.0053 -0.0066 -0.0122 469 ALA A CB 3603 N N . GLU A 470 ? 0.3518 0.3238 0.3239 0.0122 -0.0095 -0.0051 470 GLU A N 3604 C CA . GLU A 470 ? 0.3519 0.3220 0.3359 0.0084 -0.0071 -0.0103 470 GLU A CA 3605 C C . GLU A 470 ? 0.3371 0.3058 0.3199 0.0097 -0.0050 -0.0016 470 GLU A C 3606 O O . GLU A 470 ? 0.3397 0.2924 0.3213 0.0052 -0.0053 -0.0059 470 GLU A O 3607 C CB . GLU A 470 ? 0.3616 0.3281 0.3530 0.0022 -0.0090 -0.0015 470 GLU A CB 3608 C CG . GLU A 470 ? 0.3923 0.3640 0.3931 0.0117 -0.0021 -0.0102 470 GLU A CG 3609 C CD . GLU A 470 ? 0.4634 0.4141 0.4609 -0.0025 -0.0031 -0.0021 470 GLU A CD 3610 O OE1 . GLU A 470 ? 0.4753 0.4196 0.4722 0.0192 -0.0063 -0.0090 470 GLU A OE1 3611 O OE2 . GLU A 470 ? 0.4578 0.4358 0.4868 -0.0092 -0.0105 -0.0101 470 GLU A OE2 3612 N N . PHE A 471 ? 0.3253 0.2952 0.3143 0.0119 -0.0048 -0.0072 471 PHE A N 3613 C CA . PHE A 471 ? 0.3158 0.3024 0.3000 0.0107 -0.0007 -0.0032 471 PHE A CA 3614 C C . PHE A 471 ? 0.3061 0.2914 0.2846 0.0122 -0.0022 -0.0029 471 PHE A C 3615 O O . PHE A 471 ? 0.3058 0.2876 0.2931 0.0141 0.0006 0.0055 471 PHE A O 3616 C CB . PHE A 471 ? 0.3223 0.3180 0.3087 0.0020 0.0009 -0.0015 471 PHE A CB 3617 C CG . PHE A 471 ? 0.3269 0.3217 0.3158 0.0022 -0.0081 0.0014 471 PHE A CG 3618 C CD1 . PHE A 471 ? 0.3147 0.3318 0.3218 -0.0002 -0.0011 -0.0083 471 PHE A CD1 3619 C CD2 . PHE A 471 ? 0.3737 0.3468 0.3423 -0.0073 -0.0054 0.0039 471 PHE A CD2 3620 C CE1 . PHE A 471 ? 0.3193 0.3406 0.3363 0.0065 -0.0090 -0.0052 471 PHE A CE1 3621 C CE2 . PHE A 471 ? 0.3856 0.3594 0.3477 -0.0075 -0.0110 0.0070 471 PHE A CE2 3622 C CZ . PHE A 471 ? 0.3495 0.3431 0.3217 -0.0086 -0.0072 0.0013 471 PHE A CZ 3623 N N . VAL A 472 ? 0.2979 0.2842 0.2700 0.0118 -0.0023 -0.0063 472 VAL A N 3624 C CA . VAL A 472 ? 0.2919 0.2793 0.2694 0.0146 0.0002 -0.0074 472 VAL A CA 3625 C C . VAL A 472 ? 0.2902 0.2779 0.2635 0.0111 -0.0004 -0.0024 472 VAL A C 3626 O O . VAL A 472 ? 0.3070 0.2802 0.2480 0.0162 -0.0069 -0.0029 472 VAL A O 3627 C CB . VAL A 472 ? 0.2800 0.2640 0.2606 0.0141 0.0011 -0.0069 472 VAL A CB 3628 C CG1 . VAL A 472 ? 0.2784 0.2869 0.2906 0.0154 0.0038 -0.0080 472 VAL A CG1 3629 C CG2 . VAL A 472 ? 0.2807 0.2648 0.2772 0.0141 0.0083 -0.0032 472 VAL A CG2 3630 N N . LYS A 473 ? 0.2954 0.2822 0.2618 0.0155 -0.0038 -0.0078 473 LYS A N 3631 C CA . LYS A 473 ? 0.3279 0.3067 0.2970 0.0125 0.0022 -0.0064 473 LYS A CA 3632 C C . LYS A 473 ? 0.3082 0.2793 0.2761 0.0127 -0.0002 -0.0119 473 LYS A C 3633 O O . LYS A 473 ? 0.3074 0.2659 0.2756 0.0185 0.0038 -0.0014 473 LYS A O 3634 C CB . LYS A 473 ? 0.3091 0.2855 0.2668 0.0196 -0.0277 -0.0036 473 LYS A CB 3635 C CG . LYS A 473 ? 0.4239 0.3712 0.4572 0.0062 0.0490 0.0022 473 LYS A CG 3636 C CD . LYS A 473 ? 0.3503 0.3053 0.2550 0.0273 -0.0591 0.0028 473 LYS A CD 3637 C CE . LYS A 473 ? 0.4950 0.4692 0.5033 0.0134 0.0599 0.0208 473 LYS A CE 3638 N NZ . LYS A 473 ? 0.3928 0.4287 0.2622 -0.0070 -0.1243 -0.0283 473 LYS A NZ 3639 N N . SER A 474 ? 0.3072 0.2806 0.2609 0.0160 0.0000 -0.0075 474 SER A N 3640 C CA . SER A 474 ? 0.3246 0.2891 0.2797 0.0158 0.0016 -0.0087 474 SER A CA 3641 C C . SER A 474 ? 0.3217 0.2976 0.2760 0.0192 0.0026 -0.0112 474 SER A C 3642 O O . SER A 474 ? 0.3354 0.3099 0.2690 0.0293 0.0000 -0.0182 474 SER A O 3643 C CB . SER A 474 ? 0.3268 0.2818 0.2853 0.0151 -0.0064 -0.0062 474 SER A CB 3644 O OG . SER A 474 ? 0.3740 0.2887 0.3204 0.0120 0.0015 -0.0012 474 SER A OG 3645 N N . GLY A 475 ? 0.3168 0.2905 0.2775 0.0196 0.0060 -0.0162 475 GLY A N 3646 C CA . GLY A 475 ? 0.3089 0.2916 0.2733 0.0194 0.0060 -0.0131 475 GLY A CA 3647 C C . GLY A 475 ? 0.3128 0.2909 0.2795 0.0193 0.0037 -0.0177 475 GLY A C 3648 O O . GLY A 475 ? 0.3243 0.3039 0.2861 0.0164 0.0009 -0.0119 475 GLY A O 3649 N N . GLY A 476 ? 0.2930 0.2764 0.2771 0.0151 0.0098 -0.0256 476 GLY A N 3650 C CA . GLY A 476 ? 0.2917 0.2906 0.2857 0.0201 0.0022 -0.0293 476 GLY A CA 3651 C C . GLY A 476 ? 0.2805 0.2915 0.2681 0.0211 0.0049 -0.0290 476 GLY A C 3652 O O . GLY A 476 ? 0.2803 0.3172 0.2782 0.0286 0.0055 -0.0329 476 GLY A O 3653 N N . PHE A 477 ? 0.2734 0.2916 0.2547 0.0209 0.0038 -0.0248 477 PHE A N 3654 C CA . PHE A 477 ? 0.2647 0.2839 0.2468 0.0172 0.0036 -0.0208 477 PHE A CA 3655 C C . PHE A 477 ? 0.2703 0.2943 0.2478 0.0131 0.0074 -0.0149 477 PHE A C 3656 O O . PHE A 477 ? 0.2870 0.3080 0.2360 0.0105 0.0002 -0.0138 477 PHE A O 3657 C CB . PHE A 477 ? 0.2579 0.2832 0.2443 0.0140 0.0107 -0.0207 477 PHE A CB 3658 C CG . PHE A 477 ? 0.2413 0.2694 0.2421 0.0159 0.0128 -0.0177 477 PHE A CG 3659 C CD1 . PHE A 477 ? 0.2521 0.2831 0.2487 0.0159 0.0013 0.0030 477 PHE A CD1 3660 C CD2 . PHE A 477 ? 0.2587 0.2648 0.2473 0.0142 0.0151 -0.0254 477 PHE A CD2 3661 C CE1 . PHE A 477 ? 0.2463 0.2640 0.2592 -0.0005 -0.0027 -0.0061 477 PHE A CE1 3662 C CE2 . PHE A 477 ? 0.2629 0.2577 0.2572 0.0095 0.0097 -0.0078 477 PHE A CE2 3663 C CZ . PHE A 477 ? 0.2618 0.2748 0.2679 0.0069 -0.0026 -0.0183 477 PHE A CZ 3664 N N . SER A 478 ? 0.2505 0.2917 0.2325 0.0160 0.0055 -0.0143 478 SER A N 3665 C CA . SER A 478 ? 0.2499 0.2974 0.2414 0.0146 0.0091 -0.0124 478 SER A CA 3666 C C . SER A 478 ? 0.2552 0.2959 0.2425 0.0157 0.0127 -0.0038 478 SER A C 3667 O O . SER A 478 ? 0.2644 0.3143 0.2523 0.0250 0.0195 -0.0001 478 SER A O 3668 C CB . SER A 478 ? 0.2478 0.2995 0.2481 0.0090 0.0047 -0.0106 478 SER A CB 3669 O OG . SER A 478 ? 0.2841 0.3462 0.2629 0.0153 -0.0122 -0.0273 478 SER A OG 3670 N N . TYR A 479 ? 0.2449 0.2903 0.2370 0.0186 0.0140 -0.0065 479 TYR A N 3671 C CA . TYR A 479 ? 0.2307 0.2753 0.2299 0.0132 0.0160 -0.0134 479 TYR A CA 3672 C C . TYR A 479 ? 0.2354 0.2741 0.2245 0.0145 0.0129 -0.0127 479 TYR A C 3673 O O . TYR A 479 ? 0.2163 0.2773 0.2183 0.0267 0.0195 -0.0170 479 TYR A O 3674 C CB . TYR A 479 ? 0.2410 0.2831 0.2432 0.0087 0.0165 -0.0055 479 TYR A CB 3675 C CG . TYR A 479 ? 0.2467 0.2694 0.2519 0.0035 0.0155 -0.0160 479 TYR A CG 3676 C CD1 . TYR A 479 ? 0.2640 0.2766 0.2397 0.0141 0.0136 -0.0062 479 TYR A CD1 3677 C CD2 . TYR A 479 ? 0.2583 0.2873 0.2789 0.0093 0.0058 -0.0150 479 TYR A CD2 3678 C CE1 . TYR A 479 ? 0.2465 0.2861 0.2507 0.0111 0.0122 -0.0287 479 TYR A CE1 3679 C CE2 . TYR A 479 ? 0.2626 0.2901 0.2720 0.0085 0.0033 -0.0154 479 TYR A CE2 3680 C CZ . TYR A 479 ? 0.2720 0.2964 0.2654 0.0092 0.0039 -0.0186 479 TYR A CZ 3681 O OH . TYR A 479 ? 0.2746 0.2891 0.2667 0.0318 0.0020 -0.0276 479 TYR A OH 3682 N N . ALA A 480 ? 0.2281 0.2718 0.2225 0.0188 0.0177 -0.0182 480 ALA A N 3683 C CA . ALA A 480 ? 0.2314 0.2656 0.2254 0.0128 0.0148 -0.0137 480 ALA A CA 3684 C C . ALA A 480 ? 0.2313 0.2665 0.2207 0.0156 0.0094 -0.0086 480 ALA A C 3685 O O . ALA A 480 ? 0.2344 0.2660 0.2189 0.0200 0.0206 -0.0046 480 ALA A O 3686 C CB . ALA A 480 ? 0.2405 0.2621 0.2402 0.0151 0.0084 -0.0219 480 ALA A CB 3687 N N . ILE A 481 ? 0.2136 0.2651 0.2084 0.0152 0.0124 -0.0121 481 ILE A N 3688 C CA . ILE A 481 ? 0.2184 0.2505 0.2075 0.0121 0.0009 -0.0131 481 ILE A CA 3689 C C . ILE A 481 ? 0.2216 0.2502 0.2007 0.0101 0.0048 -0.0093 481 ILE A C 3690 O O . ILE A 481 ? 0.2276 0.2490 0.2154 0.0256 -0.0009 -0.0046 481 ILE A O 3691 C CB . ILE A 481 ? 0.2143 0.2425 0.2133 0.0047 0.0014 -0.0185 481 ILE A CB 3692 C CG1 . ILE A 481 ? 0.2056 0.2441 0.2075 0.0005 -0.0063 -0.0236 481 ILE A CG1 3693 C CG2 . ILE A 481 ? 0.2276 0.2558 0.2164 0.0136 0.0092 -0.0193 481 ILE A CG2 3694 C CD1 . ILE A 481 ? 0.2272 0.2476 0.2059 0.0114 -0.0133 -0.0117 481 ILE A CD1 3695 N N . VAL A 482 ? 0.2221 0.2537 0.2019 0.0138 0.0041 -0.0047 482 VAL A N 3696 C CA . VAL A 482 ? 0.2293 0.2578 0.2040 0.0060 0.0063 -0.0047 482 VAL A CA 3697 C C . VAL A 482 ? 0.2284 0.2474 0.1949 0.0123 0.0039 -0.0001 482 VAL A C 3698 O O . VAL A 482 ? 0.2483 0.2572 0.2063 0.0101 0.0223 0.0021 482 VAL A O 3699 C CB . VAL A 482 ? 0.2410 0.2645 0.2150 -0.0083 -0.0058 0.0030 482 VAL A CB 3700 C CG1 . VAL A 482 ? 0.2879 0.3091 0.2347 -0.0012 -0.0022 -0.0010 482 VAL A CG1 3701 C CG2 . VAL A 482 ? 0.2251 0.2827 0.2278 -0.0051 0.0044 -0.0117 482 VAL A CG2 3702 N N . ALA A 483 ? 0.2069 0.2465 0.1965 0.0102 0.0028 -0.0023 483 ALA A N 3703 C CA . ALA A 483 ? 0.2242 0.2437 0.1991 0.0074 0.0049 -0.0056 483 ALA A CA 3704 C C . ALA A 483 ? 0.2227 0.2410 0.1977 0.0065 0.0073 -0.0071 483 ALA A C 3705 O O . ALA A 483 ? 0.2260 0.2445 0.2103 0.0113 0.0175 -0.0033 483 ALA A O 3706 C CB . ALA A 483 ? 0.2387 0.2453 0.2027 -0.0021 0.0012 -0.0031 483 ALA A CB 3707 N N . VAL A 484 ? 0.2226 0.2416 0.1989 0.0046 0.0085 -0.0075 484 VAL A N 3708 C CA . VAL A 484 ? 0.2173 0.2481 0.1939 0.0093 -0.0019 -0.0092 484 VAL A CA 3709 C C . VAL A 484 ? 0.2106 0.2428 0.1921 0.0096 -0.0044 -0.0042 484 VAL A C 3710 O O . VAL A 484 ? 0.1854 0.2510 0.2057 0.0111 -0.0096 0.0042 484 VAL A O 3711 C CB . VAL A 484 ? 0.2249 0.2258 0.1916 0.0031 -0.0066 -0.0118 484 VAL A CB 3712 C CG1 . VAL A 484 ? 0.2350 0.2561 0.2038 0.0123 0.0018 -0.0323 484 VAL A CG1 3713 C CG2 . VAL A 484 ? 0.2257 0.2514 0.1764 0.0034 -0.0112 -0.0020 484 VAL A CG2 3714 N N . GLY A 485 ? 0.2031 0.2505 0.1906 0.0116 -0.0050 -0.0066 485 GLY A N 3715 C CA . GLY A 485 ? 0.2001 0.2571 0.1889 0.0103 -0.0076 -0.0053 485 GLY A CA 3716 C C . GLY A 485 ? 0.2002 0.2450 0.1849 0.0069 -0.0050 -0.0013 485 GLY A C 3717 O O . GLY A 485 ? 0.2043 0.2472 0.2001 0.0087 0.0000 -0.0087 485 GLY A O 3718 N N . GLU A 486 ? 0.2006 0.2461 0.1698 0.0041 -0.0101 -0.0059 486 GLU A N 3719 C CA . GLU A 486 ? 0.2078 0.2454 0.1833 0.0112 -0.0079 0.0005 486 GLU A CA 3720 C C . GLU A 486 ? 0.2201 0.2577 0.2017 0.0055 -0.0040 -0.0006 486 GLU A C 3721 O O . GLU A 486 ? 0.2208 0.2765 0.1816 0.0140 -0.0168 0.0021 486 GLU A O 3722 C CB . GLU A 486 ? 0.2112 0.2394 0.1940 0.0070 -0.0125 0.0018 486 GLU A CB 3723 C CG . GLU A 486 ? 0.2387 0.2657 0.2058 0.0168 -0.0117 0.0124 486 GLU A CG 3724 C CD . GLU A 486 ? 0.2328 0.2657 0.2166 0.0124 -0.0058 0.0077 486 GLU A CD 3725 O OE1 . GLU A 486 ? 0.2461 0.2918 0.2098 0.0058 0.0110 0.0126 486 GLU A OE1 3726 O OE2 . GLU A 486 ? 0.2296 0.3169 0.2593 0.0157 -0.0060 0.0000 486 GLU A OE2 3727 N N . HIS A 487 ? 0.2252 0.2568 0.2092 0.0047 0.0016 0.0032 487 HIS A N 3728 C CA . HIS A 487 ? 0.2300 0.2517 0.2141 0.0047 -0.0002 0.0016 487 HIS A CA 3729 C C . HIS A 487 ? 0.2245 0.2488 0.2082 0.0063 -0.0006 0.0040 487 HIS A C 3730 O O . HIS A 487 ? 0.2290 0.2568 0.2066 0.0054 -0.0061 0.0085 487 HIS A O 3731 C CB . HIS A 487 ? 0.2474 0.2593 0.2392 0.0011 0.0022 -0.0004 487 HIS A CB 3732 C CG . HIS A 487 ? 0.2917 0.2867 0.2737 0.0048 -0.0009 -0.0145 487 HIS A CG 3733 N ND1 . HIS A 487 ? 0.3383 0.3431 0.3622 -0.0019 0.0029 -0.0156 487 HIS A ND1 3734 C CD2 . HIS A 487 ? 0.3297 0.3306 0.3303 0.0089 -0.0003 -0.0181 487 HIS A CD2 3735 C CE1 . HIS A 487 ? 0.3302 0.3333 0.3403 -0.0032 0.0062 -0.0205 487 HIS A CE1 3736 N NE2 . HIS A 487 ? 0.3564 0.3318 0.3380 -0.0001 0.0039 -0.0256 487 HIS A NE2 3737 N N . PRO A 488 ? 0.2211 0.2493 0.2023 0.0116 -0.0058 -0.0007 488 PRO A N 3738 C CA . PRO A 488 ? 0.2145 0.2448 0.1980 0.0169 -0.0064 0.0011 488 PRO A CA 3739 C C . PRO A 488 ? 0.2139 0.2468 0.2023 0.0105 -0.0060 -0.0020 488 PRO A C 3740 O O . PRO A 488 ? 0.2069 0.2482 0.2209 0.0165 -0.0019 -0.0100 488 PRO A O 3741 C CB . PRO A 488 ? 0.2050 0.2503 0.1823 0.0141 -0.0044 0.0070 488 PRO A CB 3742 C CG . PRO A 488 ? 0.2274 0.2404 0.1987 0.0174 -0.0043 -0.0056 488 PRO A CG 3743 C CD . PRO A 488 ? 0.2244 0.2475 0.1912 0.0068 -0.0116 0.0045 488 PRO A CD 3744 N N . TYR A 489 ? 0.2051 0.2417 0.1953 0.0113 -0.0111 -0.0009 489 TYR A N 3745 C CA . TYR A 489 ? 0.2138 0.2544 0.1988 0.0124 -0.0078 0.0046 489 TYR A CA 3746 C C . TYR A 489 ? 0.2114 0.2531 0.1924 0.0102 -0.0129 0.0087 489 TYR A C 3747 O O . TYR A 489 ? 0.2036 0.2556 0.1886 0.0140 -0.0043 0.0145 489 TYR A O 3748 C CB . TYR A 489 ? 0.2203 0.2571 0.1991 0.0026 -0.0114 -0.0005 489 TYR A CB 3749 C CG . TYR A 489 ? 0.2216 0.2585 0.1959 0.0017 -0.0122 -0.0009 489 TYR A CG 3750 C CD1 . TYR A 489 ? 0.1862 0.2424 0.1785 0.0002 -0.0280 -0.0007 489 TYR A CD1 3751 C CD2 . TYR A 489 ? 0.2047 0.2432 0.1930 0.0006 0.0045 0.0056 489 TYR A CD2 3752 C CE1 . TYR A 489 ? 0.2142 0.2710 0.1818 -0.0017 -0.0120 0.0058 489 TYR A CE1 3753 C CE2 . TYR A 489 ? 0.2291 0.2551 0.1884 -0.0051 -0.0108 0.0080 489 TYR A CE2 3754 C CZ . TYR A 489 ? 0.2174 0.2594 0.2050 -0.0017 -0.0074 -0.0018 489 TYR A CZ 3755 O OH . TYR A 489 ? 0.2439 0.2727 0.2128 0.0012 -0.0086 0.0144 489 TYR A OH 3756 N N . THR A 490 ? 0.2075 0.2567 0.1992 0.0129 -0.0035 0.0067 490 THR A N 3757 C CA . THR A 490 ? 0.2085 0.2725 0.2222 0.0095 -0.0098 0.0039 490 THR A CA 3758 C C . THR A 490 ? 0.2122 0.2751 0.2286 0.0120 -0.0064 0.0014 490 THR A C 3759 O O . THR A 490 ? 0.2010 0.2705 0.2271 0.0140 -0.0080 0.0037 490 THR A O 3760 C CB . THR A 490 ? 0.2162 0.2747 0.2244 0.0124 -0.0090 -0.0023 490 THR A CB 3761 O OG1 . THR A 490 ? 0.2030 0.2909 0.2291 0.0008 -0.0090 0.0079 490 THR A OG1 3762 C CG2 . THR A 490 ? 0.2415 0.2779 0.2430 0.0128 -0.0026 -0.0023 490 THR A CG2 3763 N N . GLU A 491 ? 0.2138 0.2801 0.2393 0.0073 -0.0118 0.0112 491 GLU A N 3764 C CA . GLU A 491 ? 0.2292 0.2994 0.2469 0.0041 -0.0090 0.0049 491 GLU A CA 3765 C C . GLU A 491 ? 0.2354 0.2992 0.2519 0.0040 -0.0099 0.0052 491 GLU A C 3766 O O . GLU A 491 ? 0.2254 0.3135 0.2412 0.0083 -0.0094 0.0144 491 GLU A O 3767 C CB . GLU A 491 ? 0.2348 0.2945 0.2444 0.0000 -0.0134 -0.0001 491 GLU A CB 3768 C CG . GLU A 491 ? 0.2474 0.3105 0.2472 -0.0019 -0.0077 -0.0045 491 GLU A CG 3769 C CD . GLU A 491 ? 0.2489 0.3191 0.2516 0.0103 -0.0014 0.0080 491 GLU A CD 3770 O OE1 . GLU A 491 ? 0.2665 0.3820 0.2873 0.0118 -0.0017 0.0342 491 GLU A OE1 3771 O OE2 . GLU A 491 ? 0.2786 0.3162 0.2792 0.0106 -0.0232 -0.0022 491 GLU A OE2 3772 N N . THR A 492 ? 0.2326 0.3090 0.2561 0.0035 -0.0109 0.0006 492 THR A N 3773 C CA . THR A 492 ? 0.2441 0.3253 0.2657 -0.0045 -0.0076 -0.0032 492 THR A CA 3774 C C . THR A 492 ? 0.2435 0.3242 0.2646 -0.0043 -0.0067 -0.0004 492 THR A C 3775 O O . THR A 492 ? 0.2274 0.3408 0.2627 -0.0026 -0.0145 -0.0012 492 THR A O 3776 C CB . THR A 492 ? 0.2445 0.3269 0.2700 -0.0035 -0.0112 -0.0064 492 THR A CB 3777 O OG1 . THR A 492 ? 0.2612 0.3379 0.2682 -0.0036 -0.0096 -0.0041 492 THR A OG1 3778 C CG2 . THR A 492 ? 0.2688 0.3431 0.2631 -0.0051 -0.0046 -0.0160 492 THR A CG2 3779 N N . LYS A 493 ? 0.2528 0.3179 0.2643 0.0016 -0.0030 0.0036 493 LYS A N 3780 C CA . LYS A 493 ? 0.2819 0.3308 0.2831 0.0026 -0.0028 0.0041 493 LYS A CA 3781 C C . LYS A 493 ? 0.2725 0.3243 0.2740 0.0067 -0.0026 0.0028 493 LYS A C 3782 O O . LYS A 493 ? 0.2982 0.3370 0.2894 0.0015 0.0058 -0.0084 493 LYS A O 3783 C CB . LYS A 493 ? 0.2913 0.3291 0.2843 0.0043 -0.0027 0.0105 493 LYS A CB 3784 C CG . LYS A 493 ? 0.3590 0.3900 0.3668 -0.0115 0.0090 0.0095 493 LYS A CG 3785 C CD . LYS A 493 ? 0.4618 0.4410 0.4563 -0.0096 0.0000 -0.0062 493 LYS A CD 3786 C CE . LYS A 493 ? 0.4959 0.4776 0.4914 -0.0124 0.0077 0.0066 493 LYS A CE 3787 N NZ . LYS A 493 ? 0.5489 0.5169 0.5521 -0.0066 -0.0022 -0.0059 493 LYS A NZ 3788 N N . GLY A 494 ? 0.2588 0.3175 0.2496 0.0026 -0.0031 0.0067 494 GLY A N 3789 C CA . GLY A 494 ? 0.2584 0.3323 0.2599 0.0077 -0.0046 0.0122 494 GLY A CA 3790 C C . GLY A 494 ? 0.2481 0.3247 0.2514 0.0083 -0.0056 0.0128 494 GLY A C 3791 O O . GLY A 494 ? 0.2379 0.3390 0.2565 0.0094 -0.0037 0.0193 494 GLY A O 3792 N N . ASP A 495 ? 0.2488 0.3304 0.2573 0.0081 -0.0010 0.0099 495 ASP A N 3793 C CA . ASP A 495 ? 0.2494 0.3289 0.2545 0.0107 -0.0029 0.0037 495 ASP A CA 3794 C C . ASP A 495 ? 0.2511 0.3270 0.2568 0.0117 -0.0012 0.0023 495 ASP A C 3795 O O . ASP A 495 ? 0.2706 0.3326 0.2540 0.0103 0.0039 0.0019 495 ASP A O 3796 C CB . ASP A 495 ? 0.2391 0.3305 0.2546 0.0174 0.0022 0.0040 495 ASP A CB 3797 C CG . ASP A 495 ? 0.2602 0.3274 0.2562 0.0033 0.0024 0.0005 495 ASP A CG 3798 O OD1 . ASP A 495 ? 0.2448 0.3425 0.2391 0.0155 0.0000 -0.0062 495 ASP A OD1 3799 O OD2 . ASP A 495 ? 0.2497 0.3656 0.2527 0.0138 -0.0044 -0.0135 495 ASP A OD2 3800 N N . ASN A 496 ? 0.2630 0.3310 0.2535 0.0166 -0.0069 0.0033 496 ASN A N 3801 C CA . ASN A 496 ? 0.2670 0.3297 0.2555 0.0158 -0.0099 0.0010 496 ASN A CA 3802 C C . ASN A 496 ? 0.2657 0.3339 0.2613 0.0140 -0.0087 0.0013 496 ASN A C 3803 O O . ASN A 496 ? 0.2673 0.3235 0.2413 0.0151 -0.0208 -0.0005 496 ASN A O 3804 C CB . ASN A 496 ? 0.2616 0.3299 0.2631 0.0183 -0.0048 0.0011 496 ASN A CB 3805 C CG . ASN A 496 ? 0.2884 0.3316 0.2808 0.0156 -0.0067 -0.0044 496 ASN A CG 3806 O OD1 . ASN A 496 ? 0.2718 0.3546 0.2783 0.0290 0.0052 -0.0103 496 ASN A OD1 3807 N ND2 . ASN A 496 ? 0.2947 0.3425 0.3110 0.0239 0.0063 -0.0134 496 ASN A ND2 3808 N N . LEU A 497 ? 0.2805 0.3560 0.2701 0.0124 -0.0093 -0.0019 497 LEU A N 3809 C CA . LEU A 497 ? 0.2905 0.3733 0.2927 0.0110 -0.0071 0.0016 497 LEU A CA 3810 C C . LEU A 497 ? 0.3030 0.3765 0.2979 0.0117 -0.0035 -0.0002 497 LEU A C 3811 O O . LEU A 497 ? 0.3194 0.3926 0.3096 0.0164 -0.0004 0.0076 497 LEU A O 3812 C CB . LEU A 497 ? 0.2915 0.3822 0.2964 0.0081 -0.0068 -0.0032 497 LEU A CB 3813 C CG . LEU A 497 ? 0.2867 0.3672 0.3124 0.0066 -0.0067 -0.0063 497 LEU A CG 3814 C CD1 . LEU A 497 ? 0.3079 0.3875 0.3511 0.0092 -0.0206 0.0003 497 LEU A CD1 3815 C CD2 . LEU A 497 ? 0.2884 0.3701 0.3234 -0.0016 -0.0140 0.0002 497 LEU A CD2 3816 N N . ASN A 498 ? 0.2953 0.3739 0.2902 0.0092 -0.0125 -0.0027 498 ASN A N 3817 C CA . ASN A 498 ? 0.2995 0.3805 0.3084 0.0097 -0.0117 -0.0033 498 ASN A CA 3818 C C . ASN A 498 ? 0.2815 0.3628 0.2812 0.0076 -0.0108 -0.0048 498 ASN A C 3819 O O . ASN A 498 ? 0.2633 0.3727 0.2602 0.0069 -0.0260 -0.0005 498 ASN A O 3820 C CB . ASN A 498 ? 0.3251 0.3940 0.3383 0.0038 -0.0065 -0.0084 498 ASN A CB 3821 C CG . ASN A 498 ? 0.4351 0.4671 0.4279 0.0114 -0.0121 0.0042 498 ASN A CG 3822 O OD1 . ASN A 498 ? 0.4621 0.5109 0.4733 -0.0015 -0.0091 -0.0041 498 ASN A OD1 3823 N ND2 . ASN A 498 ? 0.5459 0.5794 0.5809 -0.0115 0.0221 -0.0026 498 ASN A ND2 3824 N N . LEU A 499 ? 0.2695 0.3546 0.2642 0.0107 -0.0085 -0.0063 499 LEU A N 3825 C CA . LEU A 499 ? 0.2786 0.3472 0.2562 0.0082 -0.0077 -0.0077 499 LEU A CA 3826 C C . LEU A 499 ? 0.2845 0.3433 0.2584 0.0066 -0.0102 -0.0030 499 LEU A C 3827 O O . LEU A 499 ? 0.2763 0.3459 0.2500 0.0087 -0.0115 -0.0023 499 LEU A O 3828 C CB . LEU A 499 ? 0.2812 0.3442 0.2371 0.0022 -0.0124 -0.0071 499 LEU A CB 3829 C CG . LEU A 499 ? 0.3392 0.3558 0.3171 0.0103 0.0109 -0.0053 499 LEU A CG 3830 C CD1 . LEU A 499 ? 0.2960 0.3608 0.3202 -0.0077 0.0139 0.0043 499 LEU A CD1 3831 C CD2 . LEU A 499 ? 0.2768 0.3537 0.2612 0.0204 -0.0119 -0.0008 499 LEU A CD2 3832 N N . THR A 500 ? 0.2886 0.3426 0.2574 0.0089 -0.0128 -0.0071 500 THR A N 3833 C CA . THR A 500 ? 0.3130 0.3540 0.2898 0.0079 -0.0144 -0.0020 500 THR A CA 3834 C C . THR A 500 ? 0.3128 0.3527 0.2940 0.0091 -0.0140 0.0030 500 THR A C 3835 O O . THR A 500 ? 0.3048 0.3682 0.2928 0.0167 -0.0173 0.0105 500 THR A O 3836 C CB . THR A 500 ? 0.3249 0.3568 0.3019 0.0024 -0.0095 -0.0018 500 THR A CB 3837 O OG1 . THR A 500 ? 0.3778 0.3903 0.3484 -0.0030 -0.0113 -0.0110 500 THR A OG1 3838 C CG2 . THR A 500 ? 0.3139 0.3544 0.2902 0.0057 -0.0197 -0.0042 500 THR A CG2 3839 N N . ILE A 501 ? 0.3200 0.3559 0.3076 0.0055 -0.0117 -0.0007 501 ILE A N 3840 C CA . ILE A 501 ? 0.3374 0.3640 0.3319 0.0041 -0.0147 0.0008 501 ILE A CA 3841 C C . ILE A 501 ? 0.3497 0.3724 0.3535 0.0028 -0.0110 -0.0011 501 ILE A C 3842 O O . ILE A 501 ? 0.3555 0.3629 0.3467 0.0053 -0.0078 -0.0029 501 ILE A O 3843 C CB . ILE A 501 ? 0.3312 0.3636 0.3392 -0.0001 -0.0152 -0.0007 501 ILE A CB 3844 C CG1 . ILE A 501 ? 0.3259 0.3601 0.3306 -0.0044 -0.0108 -0.0084 501 ILE A CG1 3845 C CG2 . ILE A 501 ? 0.3378 0.3457 0.3296 0.0054 -0.0274 0.0050 501 ILE A CG2 3846 C CD1 . ILE A 501 ? 0.3491 0.3895 0.3727 0.0135 -0.0078 -0.0026 501 ILE A CD1 3847 N N . PRO A 502 ? 0.3714 0.3871 0.3703 -0.0001 -0.0054 0.0000 502 PRO A N 3848 C CA . PRO A 502 ? 0.3872 0.4001 0.3954 0.0020 -0.0031 -0.0010 502 PRO A CA 3849 C C . PRO A 502 ? 0.3930 0.4104 0.4132 0.0011 -0.0014 -0.0017 502 PRO A C 3850 O O . PRO A 502 ? 0.3871 0.4120 0.4205 0.0025 0.0014 -0.0003 502 PRO A O 3851 C CB . PRO A 502 ? 0.3931 0.3966 0.3923 -0.0022 -0.0012 0.0007 502 PRO A CB 3852 C CG . PRO A 502 ? 0.3912 0.3973 0.3867 -0.0042 -0.0045 0.0039 502 PRO A CG 3853 C CD . PRO A 502 ? 0.3805 0.3888 0.3749 0.0029 -0.0046 0.0000 502 PRO A CD 3854 N N . GLU A 503 ? 0.4022 0.4169 0.4247 0.0022 -0.0024 -0.0041 503 GLU A N 3855 C CA . GLU A 503 ? 0.4031 0.4284 0.4290 0.0012 -0.0012 0.0010 503 GLU A CA 3856 C C . GLU A 503 ? 0.4027 0.4281 0.4355 0.0036 0.0006 0.0042 503 GLU A C 3857 O O . GLU A 503 ? 0.4075 0.4456 0.4464 0.0046 0.0008 0.0075 503 GLU A O 3858 C CB . GLU A 503 ? 0.4080 0.4247 0.4296 -0.0012 -0.0054 -0.0043 503 GLU A CB 3859 C CG . GLU A 503 ? 0.4260 0.4500 0.4406 -0.0088 -0.0091 0.0011 503 GLU A CG 3860 C CD . GLU A 503 ? 0.4162 0.4112 0.4631 0.0015 0.0054 -0.0074 503 GLU A CD 3861 O OE1 . GLU A 503 ? 0.3927 0.4363 0.4389 -0.0118 -0.0126 0.0031 503 GLU A OE1 3862 O OE2 . GLU A 503 ? 0.4270 0.4703 0.4604 -0.0117 -0.0070 0.0058 503 GLU A OE2 3863 N N . PRO A 504 ? 0.3879 0.4223 0.4270 0.0018 0.0010 0.0102 504 PRO A N 3864 C CA . PRO A 504 ? 0.3802 0.4113 0.4152 0.0035 -0.0016 0.0068 504 PRO A CA 3865 C C . PRO A 504 ? 0.3648 0.4008 0.3944 0.0004 -0.0025 0.0091 504 PRO A C 3866 O O . PRO A 504 ? 0.3610 0.4107 0.4055 -0.0001 0.0009 0.0079 504 PRO A O 3867 C CB . PRO A 504 ? 0.3835 0.4107 0.4151 0.0004 0.0006 0.0085 504 PRO A CB 3868 C CG . PRO A 504 ? 0.3894 0.4259 0.4224 0.0057 0.0029 0.0087 504 PRO A CG 3869 C CD . PRO A 504 ? 0.3963 0.4329 0.4359 0.0059 0.0005 0.0098 504 PRO A CD 3870 N N . GLY A 505 ? 0.3454 0.3824 0.3643 -0.0031 -0.0041 0.0048 505 GLY A N 3871 C CA . GLY A 505 ? 0.3229 0.3499 0.3176 0.0019 -0.0064 0.0019 505 GLY A CA 3872 C C . GLY A 505 ? 0.3037 0.3371 0.2927 0.0036 -0.0101 -0.0022 505 GLY A C 3873 O O . GLY A 505 ? 0.2895 0.3239 0.2617 0.0064 -0.0040 -0.0015 505 GLY A O 3874 N N . LEU A 506 ? 0.2956 0.3310 0.2765 0.0056 -0.0108 0.0025 506 LEU A N 3875 C CA . LEU A 506 ? 0.2982 0.3405 0.2737 0.0086 -0.0204 0.0019 506 LEU A CA 3876 C C . LEU A 506 ? 0.2952 0.3380 0.2727 0.0045 -0.0233 0.0024 506 LEU A C 3877 O O . LEU A 506 ? 0.2939 0.3399 0.2641 0.0093 -0.0193 -0.0007 506 LEU A O 3878 C CB . LEU A 506 ? 0.2932 0.3425 0.2708 0.0068 -0.0239 0.0061 506 LEU A CB 3879 C CG . LEU A 506 ? 0.2982 0.3387 0.2764 0.0014 -0.0187 0.0052 506 LEU A CG 3880 C CD1 . LEU A 506 ? 0.2947 0.3366 0.2832 0.0029 -0.0168 -0.0041 506 LEU A CD1 3881 C CD2 . LEU A 506 ? 0.2876 0.3510 0.2991 -0.0039 -0.0280 0.0024 506 LEU A CD2 3882 N N . SER A 507 ? 0.3001 0.3440 0.2841 0.0017 -0.0241 -0.0002 507 SER A N 3883 C CA . SER A 507 ? 0.3068 0.3430 0.3021 -0.0007 -0.0193 -0.0014 507 SER A CA 3884 C C . SER A 507 ? 0.3008 0.3376 0.2851 0.0009 -0.0176 -0.0047 507 SER A C 3885 O O . SER A 507 ? 0.2962 0.3436 0.2918 -0.0010 -0.0215 -0.0034 507 SER A O 3886 C CB . SER A 507 ? 0.3182 0.3540 0.3100 -0.0057 -0.0164 0.0003 507 SER A CB 3887 O OG . SER A 507 ? 0.3458 0.3878 0.3373 -0.0073 -0.0096 0.0089 507 SER A OG 3888 N N . THR A 508 ? 0.2968 0.3215 0.2806 -0.0036 -0.0173 -0.0029 508 THR A N 3889 C CA . THR A 508 ? 0.2923 0.3125 0.2629 -0.0027 -0.0114 -0.0075 508 THR A CA 3890 C C . THR A 508 ? 0.2815 0.2913 0.2452 0.0023 -0.0114 -0.0087 508 THR A C 3891 O O . THR A 508 ? 0.2768 0.2819 0.2282 0.0055 -0.0050 -0.0139 508 THR A O 3892 C CB . THR A 508 ? 0.2970 0.3193 0.2642 -0.0058 -0.0078 -0.0006 508 THR A CB 3893 O OG1 . THR A 508 ? 0.3371 0.3836 0.3214 -0.0255 -0.0124 0.0104 508 THR A OG1 3894 C CG2 . THR A 508 ? 0.2945 0.2993 0.2703 -0.0021 -0.0132 -0.0086 508 THR A CG2 3895 N N . VAL A 509 ? 0.2709 0.2752 0.2361 0.0019 -0.0104 -0.0111 509 VAL A N 3896 C CA . VAL A 509 ? 0.2673 0.2664 0.2275 0.0058 -0.0047 -0.0160 509 VAL A CA 3897 C C . VAL A 509 ? 0.2733 0.2810 0.2389 0.0038 -0.0076 -0.0150 509 VAL A C 3898 O O . VAL A 509 ? 0.2543 0.2761 0.2263 0.0136 -0.0061 -0.0285 509 VAL A O 3899 C CB . VAL A 509 ? 0.2642 0.2627 0.2290 0.0038 -0.0051 -0.0125 509 VAL A CB 3900 C CG1 . VAL A 509 ? 0.2744 0.2542 0.2446 0.0038 -0.0025 -0.0181 509 VAL A CG1 3901 C CG2 . VAL A 509 ? 0.2895 0.2739 0.2263 0.0059 -0.0057 -0.0125 509 VAL A CG2 3902 N N . GLN A 510 ? 0.2849 0.2865 0.2440 0.0019 -0.0109 -0.0218 510 GLN A N 3903 C CA . GLN A 510 ? 0.3021 0.3091 0.2660 0.0042 -0.0116 -0.0195 510 GLN A CA 3904 C C . GLN A 510 ? 0.3033 0.3111 0.2660 0.0027 -0.0137 -0.0217 510 GLN A C 3905 O O . GLN A 510 ? 0.3127 0.3332 0.2771 0.0092 -0.0119 -0.0230 510 GLN A O 3906 C CB . GLN A 510 ? 0.2935 0.3039 0.2651 0.0070 -0.0159 -0.0218 510 GLN A CB 3907 C CG . GLN A 510 ? 0.3030 0.3099 0.2685 0.0048 -0.0181 -0.0143 510 GLN A CG 3908 C CD . GLN A 510 ? 0.3128 0.3253 0.2904 -0.0022 -0.0169 -0.0042 510 GLN A CD 3909 O OE1 . GLN A 510 ? 0.3668 0.3616 0.3543 -0.0243 -0.0359 -0.0250 510 GLN A OE1 3910 N NE2 . GLN A 510 ? 0.3287 0.3539 0.3156 0.0141 -0.0276 -0.0095 510 GLN A NE2 3911 N N . ALA A 511 ? 0.3104 0.3014 0.2660 0.0085 -0.0115 -0.0217 511 ALA A N 3912 C CA . ALA A 511 ? 0.3138 0.3041 0.2708 0.0074 -0.0062 -0.0200 511 ALA A CA 3913 C C . ALA A 511 ? 0.3075 0.3034 0.2751 0.0141 -0.0021 -0.0163 511 ALA A C 3914 O O . ALA A 511 ? 0.3177 0.3143 0.2740 0.0157 0.0050 -0.0319 511 ALA A O 3915 C CB . ALA A 511 ? 0.3189 0.3040 0.2787 0.0044 -0.0050 -0.0181 511 ALA A CB 3916 N N . VAL A 512 ? 0.2987 0.2936 0.2663 0.0129 -0.0021 -0.0208 512 VAL A N 3917 C CA . VAL A 512 ? 0.2929 0.2896 0.2735 0.0128 0.0072 -0.0162 512 VAL A CA 3918 C C . VAL A 512 ? 0.2969 0.2905 0.2797 0.0140 0.0041 -0.0135 512 VAL A C 3919 O O . VAL A 512 ? 0.2867 0.2871 0.2797 0.0320 0.0123 -0.0071 512 VAL A O 3920 C CB . VAL A 512 ? 0.2907 0.2848 0.2693 0.0076 -0.0007 -0.0162 512 VAL A CB 3921 C CG1 . VAL A 512 ? 0.3029 0.3041 0.2924 -0.0018 -0.0061 -0.0036 512 VAL A CG1 3922 C CG2 . VAL A 512 ? 0.2826 0.2947 0.2706 0.0210 0.0191 -0.0189 512 VAL A CG2 3923 N N . CYS A 513 ? 0.2905 0.2970 0.2744 0.0171 0.0056 -0.0153 513 CYS A N 3924 C CA . CYS A 513 ? 0.3055 0.3031 0.2806 0.0186 0.0064 -0.0162 513 CYS A CA 3925 C C . CYS A 513 ? 0.3074 0.3075 0.2805 0.0155 0.0032 -0.0150 513 CYS A C 3926 O O . CYS A 513 ? 0.3155 0.3289 0.2873 0.0132 0.0018 -0.0272 513 CYS A O 3927 C CB . CYS A 513 ? 0.3049 0.3029 0.2832 0.0132 0.0027 -0.0126 513 CYS A CB 3928 S SG . CYS A 513 ? 0.3366 0.3424 0.3306 0.0222 0.0212 -0.0158 513 CYS A SG 3929 N N . GLY A 514 ? 0.3015 0.3215 0.2862 0.0175 -0.0014 -0.0194 514 GLY A N 3930 C CA . GLY A 514 ? 0.3230 0.3361 0.3034 0.0147 0.0049 -0.0188 514 GLY A CA 3931 C C . GLY A 514 ? 0.3295 0.3482 0.3091 0.0180 0.0065 -0.0186 514 GLY A C 3932 O O . GLY A 514 ? 0.3455 0.3745 0.3162 0.0251 0.0092 -0.0222 514 GLY A O 3933 N N . GLY A 515 ? 0.3217 0.3399 0.3146 0.0168 -0.0018 -0.0218 515 GLY A N 3934 C CA . GLY A 515 ? 0.3204 0.3311 0.3116 0.0188 0.0002 -0.0213 515 GLY A CA 3935 C C . GLY A 515 ? 0.3140 0.3343 0.3072 0.0198 0.0006 -0.0207 515 GLY A C 3936 O O . GLY A 515 ? 0.3107 0.3501 0.3118 0.0271 0.0016 -0.0398 515 GLY A O 3937 N N . VAL A 516 ? 0.3025 0.3191 0.2869 0.0183 0.0088 -0.0161 516 VAL A N 3938 C CA . VAL A 516 ? 0.3053 0.3139 0.2775 0.0172 0.0105 -0.0086 516 VAL A CA 3939 C C . VAL A 516 ? 0.2953 0.3078 0.2656 0.0146 0.0117 -0.0075 516 VAL A C 3940 O O . VAL A 516 ? 0.2881 0.3024 0.2694 0.0220 0.0227 -0.0197 516 VAL A O 3941 C CB . VAL A 516 ? 0.3117 0.3171 0.2850 0.0110 0.0089 0.0003 516 VAL A CB 3942 C CG1 . VAL A 516 ? 0.3246 0.3272 0.2721 0.0181 0.0100 0.0131 516 VAL A CG1 3943 C CG2 . VAL A 516 ? 0.3334 0.3418 0.3012 0.0136 -0.0030 0.0009 516 VAL A CG2 3944 N N . ARG A 517 ? 0.2899 0.3016 0.2491 0.0165 0.0136 -0.0078 517 ARG A N 3945 C CA . ARG A 517 ? 0.2891 0.3059 0.2559 0.0080 0.0183 -0.0032 517 ARG A CA 3946 C C . ARG A 517 ? 0.2913 0.3050 0.2536 0.0183 0.0171 -0.0036 517 ARG A C 3947 O O . ARG A 517 ? 0.2699 0.2882 0.2338 0.0377 0.0161 -0.0006 517 ARG A O 3948 C CB A ARG A 517 ? 0.2939 0.3138 0.2683 0.0057 0.0107 0.0009 517 ARG A CB 3949 C CB B ARG A 517 ? 0.2930 0.3098 0.2629 0.0046 0.0114 -0.0005 517 ARG A CB 3950 C CG A ARG A 517 ? 0.3149 0.3155 0.2925 0.0082 0.0072 0.0032 517 ARG A CG 3951 C CG B ARG A 517 ? 0.2904 0.3009 0.2628 -0.0046 0.0161 -0.0076 517 ARG A CG 3952 C CD A ARG A 517 ? 0.2804 0.2951 0.2872 -0.0328 0.0045 -0.0273 517 ARG A CD 3953 C CD B ARG A 517 ? 0.3101 0.3047 0.3022 -0.0071 0.0119 -0.0058 517 ARG A CD 3954 N NE A ARG A 517 ? 0.3580 0.4692 0.3645 0.0493 0.0434 -0.0027 517 ARG A NE 3955 N NE B ARG A 517 ? 0.2967 0.2872 0.2949 -0.0107 0.0053 -0.0083 517 ARG A NE 3956 C CZ A ARG A 517 ? 0.2317 0.2284 0.2437 -0.0518 -0.1180 0.0257 517 ARG A CZ 3957 C CZ B ARG A 517 ? 0.2850 0.2739 0.2753 -0.0057 0.0027 -0.0046 517 ARG A CZ 3958 N NH1 A ARG A 517 ? 0.4523 0.4782 0.5061 -0.0590 0.0673 -0.0811 517 ARG A NH1 3959 N NH1 B ARG A 517 ? 0.2330 0.2374 0.2148 -0.0161 0.0187 -0.0033 517 ARG A NH1 3960 N NH2 A ARG A 517 ? 0.5244 0.4820 0.5043 0.0761 0.0772 0.0520 517 ARG A NH2 3961 N NH2 B ARG A 517 ? 0.2423 0.2451 0.1979 -0.0286 0.0086 -0.0060 517 ARG A NH2 3962 N N . CYS A 518 ? 0.2932 0.3131 0.2670 0.0212 0.0173 -0.0001 518 CYS A N 3963 C CA . CYS A 518 ? 0.2808 0.3017 0.2624 0.0184 0.0138 -0.0011 518 CYS A CA 3964 C C . CYS A 518 ? 0.2739 0.2898 0.2466 0.0119 0.0134 -0.0021 518 CYS A C 3965 O O . CYS A 518 ? 0.2748 0.2906 0.2282 0.0134 0.0214 -0.0110 518 CYS A O 3966 C CB A CYS A 518 ? 0.2680 0.2936 0.2520 0.0152 0.0117 0.0027 518 CYS A CB 3967 C CB B CYS A 518 ? 0.3005 0.3085 0.2831 0.0126 0.0093 -0.0001 518 CYS A CB 3968 S SG A CYS A 518 ? 0.2489 0.2888 0.2544 0.0232 -0.0078 0.0089 518 CYS A SG 3969 S SG B CYS A 518 ? 0.3478 0.3701 0.3637 0.0113 0.0106 -0.0021 518 CYS A SG 3970 N N . ALA A 519 ? 0.2480 0.2682 0.2250 0.0165 0.0143 -0.0067 519 ALA A N 3971 C CA . ALA A 519 ? 0.2239 0.2553 0.2183 0.0014 0.0068 -0.0067 519 ALA A CA 3972 C C . ALA A 519 ? 0.2133 0.2471 0.2022 0.0012 0.0063 -0.0028 519 ALA A C 3973 O O . ALA A 519 ? 0.2167 0.2544 0.2146 -0.0001 -0.0093 0.0088 519 ALA A O 3974 C CB . ALA A 519 ? 0.2075 0.2492 0.2182 -0.0080 0.0011 -0.0053 519 ALA A CB 3975 N N . THR A 520 ? 0.2123 0.2479 0.1831 0.0015 0.0062 -0.0014 520 THR A N 3976 C CA . THR A 520 ? 0.2160 0.2519 0.1927 0.0022 -0.0002 -0.0048 520 THR A CA 3977 C C . THR A 520 ? 0.2143 0.2459 0.1894 0.0014 0.0054 -0.0006 520 THR A C 3978 O O . THR A 520 ? 0.2246 0.2654 0.1878 0.0009 0.0158 0.0042 520 THR A O 3979 C CB . THR A 520 ? 0.2207 0.2532 0.2031 -0.0025 -0.0023 -0.0095 520 THR A CB 3980 O OG1 . THR A 520 ? 0.2520 0.2801 0.2006 0.0071 -0.0052 -0.0176 520 THR A OG1 3981 C CG2 . THR A 520 ? 0.2239 0.2719 0.2165 0.0029 0.0092 -0.0110 520 THR A CG2 3982 N N . VAL A 521 ? 0.2078 0.2487 0.1824 0.0077 0.0020 -0.0010 521 VAL A N 3983 C CA . VAL A 521 ? 0.2088 0.2479 0.1857 0.0054 0.0003 0.0029 521 VAL A CA 3984 C C . VAL A 521 ? 0.2037 0.2405 0.1852 0.0107 0.0022 0.0061 521 VAL A C 3985 O O . VAL A 521 ? 0.1991 0.2339 0.2120 0.0054 0.0029 0.0022 521 VAL A O 3986 C CB . VAL A 521 ? 0.1998 0.2531 0.1813 0.0090 -0.0034 0.0000 521 VAL A CB 3987 C CG1 . VAL A 521 ? 0.2165 0.2383 0.1867 0.0093 0.0020 -0.0062 521 VAL A CG1 3988 C CG2 . VAL A 521 ? 0.2037 0.2648 0.1975 -0.0036 0.0050 0.0025 521 VAL A CG2 3989 N N . LEU A 522 ? 0.2003 0.2378 0.1770 0.0121 0.0002 0.0050 522 LEU A N 3990 C CA . LEU A 522 ? 0.2022 0.2320 0.1822 0.0108 -0.0038 0.0074 522 LEU A CA 3991 C C . LEU A 522 ? 0.1906 0.2302 0.1831 0.0085 -0.0008 0.0021 522 LEU A C 3992 O O . LEU A 522 ? 0.1914 0.2308 0.1932 0.0112 0.0044 -0.0013 522 LEU A O 3993 C CB . LEU A 522 ? 0.2027 0.2366 0.1701 0.0120 -0.0090 -0.0024 522 LEU A CB 3994 C CG . LEU A 522 ? 0.1991 0.2280 0.2024 0.0064 -0.0096 0.0163 522 LEU A CG 3995 C CD1 . LEU A 522 ? 0.2237 0.2493 0.2317 0.0061 -0.0090 0.0011 522 LEU A CD1 3996 C CD2 . LEU A 522 ? 0.2307 0.2654 0.2127 -0.0023 -0.0199 0.0241 522 LEU A CD2 3997 N N . ILE A 523 ? 0.1919 0.2393 0.1731 0.0112 0.0058 0.0033 523 ILE A N 3998 C CA . ILE A 523 ? 0.1970 0.2373 0.1793 0.0088 0.0027 0.0012 523 ILE A CA 3999 C C . ILE A 523 ? 0.2116 0.2421 0.1876 0.0094 0.0069 -0.0002 523 ILE A C 4000 O O . ILE A 523 ? 0.2141 0.2367 0.2084 0.0056 0.0020 -0.0072 523 ILE A O 4001 C CB . ILE A 523 ? 0.2020 0.2542 0.1810 0.0044 0.0094 0.0036 523 ILE A CB 4002 C CG1 . ILE A 523 ? 0.2217 0.2605 0.1986 0.0103 0.0019 -0.0001 523 ILE A CG1 4003 C CG2 . ILE A 523 ? 0.1919 0.2335 0.1803 0.0027 0.0160 -0.0053 523 ILE A CG2 4004 C CD1 . ILE A 523 ? 0.2281 0.2536 0.2622 -0.0174 -0.0055 0.0054 523 ILE A CD1 4005 N N . SER A 524 ? 0.2121 0.2489 0.1840 0.0218 -0.0060 0.0036 524 SER A N 4006 C CA . SER A 524 ? 0.2160 0.2525 0.1907 0.0176 -0.0013 0.0052 524 SER A CA 4007 C C . SER A 524 ? 0.2224 0.2444 0.1879 0.0187 -0.0024 0.0068 524 SER A C 4008 O O . SER A 524 ? 0.2186 0.2487 0.1881 0.0203 0.0031 0.0044 524 SER A O 4009 C CB . SER A 524 ? 0.2181 0.2460 0.1902 0.0126 -0.0036 0.0107 524 SER A CB 4010 O OG . SER A 524 ? 0.2239 0.2555 0.1890 0.0134 0.0033 0.0236 524 SER A OG 4011 N N . GLY A 525 ? 0.2378 0.2528 0.1895 0.0175 -0.0007 0.0102 525 GLY A N 4012 C CA . GLY A 525 ? 0.2325 0.2512 0.1888 0.0234 0.0026 0.0122 525 GLY A CA 4013 C C . GLY A 525 ? 0.2432 0.2601 0.1863 0.0204 -0.0010 0.0137 525 GLY A C 4014 O O . GLY A 525 ? 0.2507 0.2705 0.1858 0.0217 -0.0004 0.0205 525 GLY A O 4015 N N . ARG A 526 ? 0.2315 0.2776 0.1821 0.0172 -0.0026 0.0176 526 ARG A N 4016 C CA . ARG A 526 ? 0.2279 0.2656 0.1825 0.0108 0.0021 0.0152 526 ARG A CA 4017 C C . ARG A 526 ? 0.2363 0.2642 0.1810 0.0139 0.0009 0.0109 526 ARG A C 4018 O O . ARG A 526 ? 0.2411 0.2707 0.1695 0.0135 -0.0062 0.0153 526 ARG A O 4019 C CB . ARG A 526 ? 0.2254 0.2654 0.1814 0.0092 -0.0044 0.0190 526 ARG A CB 4020 C CG . ARG A 526 ? 0.2111 0.2874 0.2190 0.0007 -0.0061 -0.0003 526 ARG A CG 4021 C CD . ARG A 526 ? 0.2066 0.3023 0.2140 -0.0037 -0.0004 0.0130 526 ARG A CD 4022 N NE . ARG A 526 ? 0.2371 0.2938 0.2266 -0.0004 -0.0051 -0.0031 526 ARG A NE 4023 C CZ . ARG A 526 ? 0.2344 0.2848 0.2242 -0.0050 -0.0177 -0.0038 526 ARG A CZ 4024 N NH1 . ARG A 526 ? 0.2262 0.3073 0.2105 0.0107 -0.0094 -0.0048 526 ARG A NH1 4025 N NH2 . ARG A 526 ? 0.2594 0.2817 0.2215 -0.0058 -0.0257 -0.0147 526 ARG A NH2 4026 N N . PRO A 527 ? 0.2443 0.2677 0.1929 0.0152 0.0008 0.0138 527 PRO A N 4027 C CA . PRO A 527 ? 0.2546 0.2715 0.1966 0.0202 0.0000 0.0145 527 PRO A CA 4028 C C . PRO A 527 ? 0.2385 0.2776 0.1976 0.0167 -0.0018 0.0141 527 PRO A C 4029 O O . PRO A 527 ? 0.2451 0.3028 0.1993 0.0258 -0.0001 0.0200 527 PRO A O 4030 C CB . PRO A 527 ? 0.2640 0.2581 0.2007 0.0178 0.0016 0.0148 527 PRO A CB 4031 C CG . PRO A 527 ? 0.3045 0.2918 0.2201 0.0191 0.0092 0.0106 527 PRO A CG 4032 C CD . PRO A 527 ? 0.2572 0.2602 0.1865 0.0151 0.0005 0.0152 527 PRO A CD 4033 N N . VAL A 528 ? 0.2336 0.2803 0.1962 0.0226 -0.0092 0.0117 528 VAL A N 4034 C CA . VAL A 528 ? 0.2343 0.2843 0.2024 0.0140 0.0011 0.0044 528 VAL A CA 4035 C C . VAL A 528 ? 0.2375 0.2940 0.2019 0.0088 0.0015 -0.0004 528 VAL A C 4036 O O . VAL A 528 ? 0.2389 0.3077 0.1995 0.0096 0.0033 -0.0061 528 VAL A O 4037 C CB . VAL A 528 ? 0.2264 0.2806 0.2059 0.0164 0.0025 0.0012 528 VAL A CB 4038 C CG1 . VAL A 528 ? 0.2462 0.2890 0.1921 0.0127 0.0049 0.0186 528 VAL A CG1 4039 C CG2 . VAL A 528 ? 0.2343 0.2834 0.2251 0.0151 -0.0059 -0.0074 528 VAL A CG2 4040 N N . VAL A 529 ? 0.2440 0.3094 0.2160 0.0077 0.0070 -0.0048 529 VAL A N 4041 C CA . VAL A 529 ? 0.2402 0.3124 0.2186 0.0118 0.0048 -0.0115 529 VAL A CA 4042 C C . VAL A 529 ? 0.2418 0.3057 0.2211 0.0095 -0.0010 -0.0076 529 VAL A C 4043 O O . VAL A 529 ? 0.2392 0.3166 0.2268 0.0205 -0.0002 -0.0056 529 VAL A O 4044 C CB . VAL A 529 ? 0.2443 0.3100 0.2315 0.0100 0.0122 -0.0113 529 VAL A CB 4045 C CG1 . VAL A 529 ? 0.2609 0.3321 0.2381 0.0030 0.0066 -0.0174 529 VAL A CG1 4046 C CG2 . VAL A 529 ? 0.2552 0.3172 0.2506 0.0120 -0.0056 -0.0065 529 VAL A CG2 4047 N N . VAL A 530 ? 0.2329 0.3084 0.2078 0.0096 -0.0075 -0.0061 530 VAL A N 4048 C CA . VAL A 530 ? 0.2458 0.3111 0.2136 0.0147 0.0016 -0.0036 530 VAL A CA 4049 C C . VAL A 530 ? 0.2604 0.3228 0.2137 0.0186 -0.0035 -0.0056 530 VAL A C 4050 O O . VAL A 530 ? 0.2590 0.3333 0.1926 0.0334 0.0026 -0.0038 530 VAL A O 4051 C CB . VAL A 530 ? 0.2503 0.2991 0.2338 0.0118 -0.0058 0.0016 530 VAL A CB 4052 C CG1 . VAL A 530 ? 0.2515 0.2988 0.2265 0.0097 0.0106 0.0105 530 VAL A CG1 4053 C CG2 . VAL A 530 ? 0.2423 0.3046 0.2196 0.0063 -0.0182 -0.0035 530 VAL A CG2 4054 N N . GLN A 531 ? 0.2669 0.3159 0.2108 0.0219 -0.0039 0.0014 531 GLN A N 4055 C CA . GLN A 531 ? 0.2657 0.3160 0.2094 0.0162 -0.0064 -0.0009 531 GLN A CA 4056 C C . GLN A 531 ? 0.2637 0.3106 0.2111 0.0098 -0.0116 -0.0027 531 GLN A C 4057 O O . GLN A 531 ? 0.2637 0.3183 0.1998 0.0150 -0.0171 -0.0065 531 GLN A O 4058 C CB . GLN A 531 ? 0.2655 0.3091 0.2044 0.0176 -0.0064 0.0019 531 GLN A CB 4059 C CG . GLN A 531 ? 0.2800 0.3146 0.2261 0.0150 -0.0018 0.0011 531 GLN A CG 4060 C CD . GLN A 531 ? 0.2881 0.3165 0.2772 0.0135 0.0015 0.0089 531 GLN A CD 4061 O OE1 . GLN A 531 ? 0.2987 0.3588 0.2765 0.0415 0.0134 0.0020 531 GLN A OE1 4062 N NE2 . GLN A 531 ? 0.3123 0.3484 0.2579 0.0178 -0.0171 -0.0115 531 GLN A NE2 4063 N N . PRO A 532 ? 0.2682 0.3147 0.2263 0.0097 -0.0126 -0.0051 532 PRO A N 4064 C CA . PRO A 532 ? 0.2642 0.3085 0.2286 0.0110 -0.0166 -0.0027 532 PRO A CA 4065 C C . PRO A 532 ? 0.2623 0.3064 0.2228 0.0134 -0.0142 -0.0081 532 PRO A C 4066 O O . PRO A 532 ? 0.2706 0.3114 0.2230 0.0145 -0.0212 -0.0122 532 PRO A O 4067 C CB . PRO A 532 ? 0.2722 0.3080 0.2361 0.0125 -0.0182 -0.0021 532 PRO A CB 4068 C CG . PRO A 532 ? 0.2738 0.3190 0.2699 0.0108 -0.0100 -0.0038 532 PRO A CG 4069 C CD . PRO A 532 ? 0.2717 0.3083 0.2460 0.0044 -0.0056 -0.0019 532 PRO A CD 4070 N N . LEU A 533 ? 0.2533 0.2901 0.2167 0.0083 -0.0107 -0.0116 533 LEU A N 4071 C CA . LEU A 533 ? 0.2505 0.2952 0.2084 0.0109 -0.0035 -0.0083 533 LEU A CA 4072 C C . LEU A 533 ? 0.2519 0.2885 0.2139 0.0103 -0.0015 -0.0097 533 LEU A C 4073 O O . LEU A 533 ? 0.2567 0.3116 0.2118 0.0180 0.0065 0.0003 533 LEU A O 4074 C CB . LEU A 533 ? 0.2494 0.2886 0.2130 0.0084 0.0003 -0.0102 533 LEU A CB 4075 C CG . LEU A 533 ? 0.2631 0.2809 0.2269 0.0120 0.0127 -0.0084 533 LEU A CG 4076 C CD1 . LEU A 533 ? 0.2794 0.2804 0.2129 0.0002 0.0157 -0.0158 533 LEU A CD1 4077 C CD2 . LEU A 533 ? 0.2598 0.2902 0.2511 0.0140 0.0041 0.0004 533 LEU A CD2 4078 N N . LEU A 534 ? 0.2547 0.2931 0.2179 0.0115 -0.0019 -0.0043 534 LEU A N 4079 C CA . LEU A 534 ? 0.2675 0.2956 0.2371 0.0114 -0.0040 -0.0103 534 LEU A CA 4080 C C . LEU A 534 ? 0.2723 0.3065 0.2421 0.0101 0.0013 -0.0083 534 LEU A C 4081 O O . LEU A 534 ? 0.2832 0.3191 0.2406 0.0128 0.0005 -0.0124 534 LEU A O 4082 C CB . LEU A 534 ? 0.2734 0.2918 0.2524 0.0148 -0.0052 -0.0080 534 LEU A CB 4083 C CG . LEU A 534 ? 0.3193 0.3251 0.3163 0.0124 -0.0160 -0.0130 534 LEU A CG 4084 C CD1 . LEU A 534 ? 0.3087 0.3173 0.2739 0.0066 -0.0074 -0.0074 534 LEU A CD1 4085 C CD2 . LEU A 534 ? 0.2760 0.3188 0.3048 0.0109 0.0079 -0.0055 534 LEU A CD2 4086 N N . ALA A 535 ? 0.2807 0.3134 0.2407 0.0145 0.0025 -0.0090 535 ALA A N 4087 C CA . ALA A 535 ? 0.2902 0.3215 0.2499 0.0127 -0.0006 -0.0064 535 ALA A CA 4088 C C . ALA A 535 ? 0.2855 0.3229 0.2527 0.0117 -0.0021 -0.0039 535 ALA A C 4089 O O . ALA A 535 ? 0.2884 0.3377 0.2426 0.0173 -0.0010 0.0077 535 ALA A O 4090 C CB . ALA A 535 ? 0.2770 0.3208 0.2421 0.0101 -0.0016 -0.0099 535 ALA A CB 4091 N N . ALA A 536 ? 0.2810 0.3076 0.2427 0.0099 -0.0108 -0.0046 536 ALA A N 4092 C CA . ALA A 536 ? 0.2802 0.3088 0.2499 0.0069 -0.0116 -0.0124 536 ALA A CA 4093 C C . ALA A 536 ? 0.2807 0.3096 0.2491 0.0073 -0.0086 -0.0134 536 ALA A C 4094 O O . ALA A 536 ? 0.2908 0.3240 0.2464 0.0142 -0.0137 -0.0248 536 ALA A O 4095 C CB . ALA A 536 ? 0.2789 0.3061 0.2506 0.0076 -0.0169 -0.0072 536 ALA A CB 4096 N N . SER A 537 ? 0.2692 0.2919 0.2284 0.0003 -0.0037 -0.0123 537 SER A N 4097 C CA . SER A 537 ? 0.2577 0.2842 0.2226 0.0006 0.0025 -0.0089 537 SER A CA 4098 C C . SER A 537 ? 0.2573 0.2873 0.2270 0.0062 0.0039 -0.0091 537 SER A C 4099 O O . SER A 537 ? 0.2617 0.2987 0.2224 0.0148 -0.0004 0.0028 537 SER A O 4100 C CB . SER A 537 ? 0.2581 0.2857 0.2207 -0.0070 0.0064 -0.0154 537 SER A CB 4101 O OG . SER A 537 ? 0.2690 0.3127 0.2226 -0.0111 0.0069 0.0119 537 SER A OG 4102 N N . ASP A 538 ? 0.2462 0.2768 0.2141 0.0108 0.0101 -0.0099 538 ASP A N 4103 C CA . ASP A 538 ? 0.2500 0.2768 0.2196 0.0121 0.0089 -0.0124 538 ASP A CA 4104 C C . ASP A 538 ? 0.2523 0.2693 0.2126 0.0079 0.0112 -0.0095 538 ASP A C 4105 O O . ASP A 538 ? 0.2770 0.2836 0.2032 0.0121 0.0265 -0.0089 538 ASP A O 4106 C CB . ASP A 538 ? 0.2365 0.2752 0.2275 0.0182 0.0077 -0.0056 538 ASP A CB 4107 C CG . ASP A 538 ? 0.2657 0.3030 0.2389 0.0078 0.0059 -0.0130 538 ASP A CG 4108 O OD1 . ASP A 538 ? 0.2754 0.3193 0.2230 0.0244 0.0174 -0.0079 538 ASP A OD1 4109 O OD2 . ASP A 538 ? 0.2890 0.3566 0.2588 0.0072 0.0292 -0.0072 538 ASP A OD2 4110 N N . ALA A 539 ? 0.2459 0.2703 0.2067 0.0029 0.0153 -0.0083 539 ALA A N 4111 C CA . ALA A 539 ? 0.2116 0.2467 0.1995 0.0022 0.0105 -0.0034 539 ALA A CA 4112 C C . ALA A 539 ? 0.2163 0.2534 0.1931 0.0039 0.0128 -0.0005 539 ALA A C 4113 O O . ALA A 539 ? 0.2088 0.2561 0.1882 0.0036 0.0164 0.0030 539 ALA A O 4114 C CB . ALA A 539 ? 0.2297 0.2588 0.2029 -0.0052 0.0049 -0.0011 539 ALA A CB 4115 N N . LEU A 540 ? 0.2046 0.2553 0.1832 0.0045 0.0109 0.0030 540 LEU A N 4116 C CA . LEU A 540 ? 0.2043 0.2528 0.1806 0.0003 0.0072 -0.0042 540 LEU A CA 4117 C C . LEU A 540 ? 0.2056 0.2505 0.1827 0.0017 0.0097 -0.0012 540 LEU A C 4118 O O . LEU A 540 ? 0.2277 0.2505 0.1700 0.0110 0.0190 -0.0119 540 LEU A O 4119 C CB . LEU A 540 ? 0.2056 0.2635 0.1956 -0.0058 0.0002 -0.0028 540 LEU A CB 4120 C CG . LEU A 540 ? 0.2254 0.2691 0.2203 -0.0015 0.0016 -0.0141 540 LEU A CG 4121 C CD1 . LEU A 540 ? 0.2431 0.2929 0.2484 -0.0236 -0.0071 -0.0097 540 LEU A CD1 4122 C CD2 . LEU A 540 ? 0.2638 0.2741 0.2526 0.0110 0.0093 0.0080 540 LEU A CD2 4123 N N . VAL A 541 ? 0.2052 0.2450 0.1696 0.0043 0.0121 -0.0036 541 VAL A N 4124 C CA . VAL A 541 ? 0.2040 0.2498 0.1834 0.0012 0.0085 -0.0049 541 VAL A CA 4125 C C . VAL A 541 ? 0.2077 0.2441 0.1910 0.0029 0.0062 0.0007 541 VAL A C 4126 O O . VAL A 541 ? 0.1997 0.2403 0.1915 -0.0067 0.0075 0.0056 541 VAL A O 4127 C CB . VAL A 541 ? 0.2070 0.2588 0.1880 0.0005 0.0031 -0.0063 541 VAL A CB 4128 C CG1 . VAL A 541 ? 0.2248 0.2596 0.1852 -0.0077 0.0146 -0.0158 541 VAL A CG1 4129 C CG2 . VAL A 541 ? 0.2077 0.2698 0.2226 0.0063 0.0066 -0.0083 541 VAL A CG2 4130 N N . ALA A 542 ? 0.1971 0.2396 0.1821 0.0110 0.0131 0.0016 542 ALA A N 4131 C CA . ALA A 542 ? 0.2032 0.2289 0.1790 0.0145 0.0104 0.0041 542 ALA A CA 4132 C C . ALA A 542 ? 0.2040 0.2280 0.1713 0.0114 0.0136 0.0058 542 ALA A C 4133 O O . ALA A 542 ? 0.2300 0.2476 0.1687 0.0083 0.0101 0.0013 542 ALA A O 4134 C CB . ALA A 542 ? 0.2061 0.2331 0.1814 0.0096 0.0052 0.0075 542 ALA A CB 4135 N N . ALA A 543 ? 0.1962 0.2305 0.1629 0.0136 0.0136 0.0102 543 ALA A N 4136 C CA . ALA A 543 ? 0.1916 0.2277 0.1677 0.0128 0.0161 0.0093 543 ALA A CA 4137 C C . ALA A 543 ? 0.1851 0.2283 0.1706 0.0106 0.0104 0.0082 543 ALA A C 4138 O O . ALA A 543 ? 0.1888 0.2459 0.1758 0.0059 0.0179 0.0033 543 ALA A O 4139 C CB . ALA A 543 ? 0.1873 0.2294 0.1739 0.0219 0.0178 0.0095 543 ALA A CB 4140 N N . TRP A 544 ? 0.1910 0.2337 0.1651 0.0075 0.0103 0.0100 544 TRP A N 4141 C CA . TRP A 544 ? 0.1919 0.2253 0.1610 0.0061 0.0075 0.0178 544 TRP A CA 4142 C C . TRP A 544 ? 0.1956 0.2239 0.1603 0.0037 0.0054 0.0172 544 TRP A C 4143 O O . TRP A 544 ? 0.2037 0.2393 0.1443 0.0065 0.0015 0.0157 544 TRP A O 4144 C CB . TRP A 544 ? 0.1948 0.2368 0.1858 0.0029 0.0085 0.0155 544 TRP A CB 4145 C CG . TRP A 544 ? 0.1956 0.2015 0.1728 0.0107 0.0052 0.0119 544 TRP A CG 4146 C CD1 . TRP A 544 ? 0.2213 0.2416 0.2086 0.0091 0.0101 0.0164 544 TRP A CD1 4147 C CD2 . TRP A 544 ? 0.2212 0.2299 0.1895 0.0082 0.0021 0.0078 544 TRP A CD2 4148 N NE1 . TRP A 544 ? 0.2189 0.2417 0.1750 0.0112 -0.0027 0.0236 544 TRP A NE1 4149 C CE2 . TRP A 544 ? 0.2130 0.2348 0.2006 0.0048 0.0026 0.0100 544 TRP A CE2 4150 C CE3 . TRP A 544 ? 0.2319 0.2573 0.2012 0.0111 0.0001 0.0179 544 TRP A CE3 4151 C CZ2 . TRP A 544 ? 0.2154 0.2521 0.2063 0.0090 -0.0011 0.0212 544 TRP A CZ2 4152 C CZ3 . TRP A 544 ? 0.2377 0.2567 0.2081 0.0077 -0.0058 0.0254 544 TRP A CZ3 4153 C CH2 . TRP A 544 ? 0.2220 0.2548 0.1984 -0.0017 -0.0047 0.0222 544 TRP A CH2 4154 N N . LEU A 545 ? 0.1964 0.2232 0.1565 0.0015 -0.0001 0.0192 545 LEU A N 4155 C CA . LEU A 545 ? 0.1923 0.2224 0.1621 -0.0020 -0.0072 0.0151 545 LEU A CA 4156 C C . LEU A 545 ? 0.1997 0.2185 0.1686 0.0000 -0.0039 0.0115 545 LEU A C 4157 O O . LEU A 545 ? 0.2090 0.2310 0.1589 0.0018 -0.0089 0.0073 545 LEU A O 4158 C CB . LEU A 545 ? 0.2009 0.2333 0.1751 -0.0071 -0.0072 0.0108 545 LEU A CB 4159 C CG . LEU A 545 ? 0.1871 0.2328 0.1875 -0.0032 -0.0029 -0.0006 545 LEU A CG 4160 C CD1 . LEU A 545 ? 0.1740 0.2726 0.2003 -0.0003 0.0009 0.0161 545 LEU A CD1 4161 C CD2 . LEU A 545 ? 0.1841 0.2389 0.2060 0.0102 -0.0025 -0.0074 545 LEU A CD2 4162 N N . PRO A 546 ? 0.2016 0.2137 0.1694 0.0052 -0.0031 0.0112 546 PRO A N 4163 C CA . PRO A 546 ? 0.1875 0.2285 0.1687 0.0086 -0.0026 0.0114 546 PRO A CA 4164 C C . PRO A 546 ? 0.1930 0.2234 0.1684 0.0080 -0.0044 0.0093 546 PRO A C 4165 O O . PRO A 546 ? 0.2052 0.2254 0.1589 -0.0079 -0.0106 0.0208 546 PRO A O 4166 C CB . PRO A 546 ? 0.1949 0.2281 0.1780 0.0078 0.0138 0.0034 546 PRO A CB 4167 C CG . PRO A 546 ? 0.2019 0.2244 0.1897 0.0083 -0.0085 0.0088 546 PRO A CG 4168 C CD . PRO A 546 ? 0.1844 0.2119 0.1792 0.0133 0.0000 0.0109 546 PRO A CD 4169 N N . GLY A 547 ? 0.1965 0.2250 0.1464 0.0115 -0.0084 0.0161 547 GLY A N 4170 C CA . GLY A 547 ? 0.1917 0.2271 0.1569 0.0164 -0.0131 0.0148 547 GLY A CA 4171 C C . GLY A 547 ? 0.2027 0.2323 0.1588 0.0173 -0.0140 0.0093 547 GLY A C 4172 O O . GLY A 547 ? 0.2061 0.2448 0.1605 0.0232 -0.0133 0.0103 547 GLY A O 4173 N N . SER A 548 ? 0.2064 0.2359 0.1575 0.0213 -0.0086 0.0094 548 SER A N 4174 C CA . SER A 548 ? 0.2026 0.2343 0.1669 0.0184 -0.0047 0.0028 548 SER A CA 4175 C C . SER A 548 ? 0.2040 0.2333 0.1823 0.0108 -0.0018 -0.0024 548 SER A C 4176 O O . SER A 548 ? 0.2080 0.2418 0.1998 0.0130 -0.0025 -0.0036 548 SER A O 4177 C CB . SER A 548 ? 0.2108 0.2300 0.1590 0.0061 -0.0062 0.0083 548 SER A CB 4178 O OG . SER A 548 ? 0.2255 0.2389 0.1677 0.0125 0.0016 0.0049 548 SER A OG 4179 N N . GLU A 549 ? 0.2001 0.2430 0.1796 0.0096 0.0022 -0.0073 549 GLU A N 4180 C CA . GLU A 549 ? 0.2193 0.2421 0.1895 0.0061 0.0083 -0.0116 549 GLU A CA 4181 C C . GLU A 549 ? 0.2268 0.2397 0.1874 0.0076 0.0087 -0.0057 549 GLU A C 4182 O O . GLU A 549 ? 0.2330 0.2371 0.2023 0.0110 0.0108 -0.0103 549 GLU A O 4183 C CB . GLU A 549 ? 0.2213 0.2513 0.1980 0.0058 0.0082 -0.0106 549 GLU A CB 4184 C CG . GLU A 549 ? 0.2416 0.2480 0.1872 0.0100 0.0042 0.0014 549 GLU A CG 4185 C CD . GLU A 549 ? 0.2557 0.2846 0.2403 0.0136 -0.0082 0.0029 549 GLU A CD 4186 O OE1 . GLU A 549 ? 0.2181 0.2824 0.2346 0.0212 0.0043 -0.0068 549 GLU A OE1 4187 O OE2 . GLU A 549 ? 0.2257 0.2850 0.2464 0.0007 -0.0119 0.0118 549 GLU A OE2 4188 N N . GLY A 550 ? 0.2285 0.2485 0.1821 0.0105 0.0040 -0.0155 550 GLY A N 4189 C CA . GLY A 550 ? 0.2345 0.2378 0.1730 0.0114 0.0077 -0.0096 550 GLY A CA 4190 C C . GLY A 550 ? 0.2355 0.2517 0.1980 0.0121 -0.0005 -0.0112 550 GLY A C 4191 O O . GLY A 550 ? 0.2357 0.2630 0.1854 0.0101 -0.0019 -0.0109 550 GLY A O 4192 N N . GLN A 551 ? 0.2339 0.2474 0.2088 0.0125 -0.0034 -0.0091 551 GLN A N 4193 C CA . GLN A 551 ? 0.2458 0.2582 0.2223 0.0096 -0.0073 -0.0076 551 GLN A CA 4194 C C . GLN A 551 ? 0.2419 0.2550 0.2206 0.0083 -0.0054 -0.0093 551 GLN A C 4195 O O . GLN A 551 ? 0.2527 0.2536 0.2161 0.0111 -0.0013 -0.0042 551 GLN A O 4196 C CB . GLN A 551 ? 0.2469 0.2655 0.2247 0.0174 -0.0064 0.0006 551 GLN A CB 4197 C CG . GLN A 551 ? 0.2792 0.2890 0.2556 0.0246 -0.0009 0.0015 551 GLN A CG 4198 C CD . GLN A 551 ? 0.2941 0.3598 0.2822 0.0140 -0.0125 -0.0123 551 GLN A CD 4199 O OE1 . GLN A 551 ? 0.3379 0.3976 0.3494 0.0395 -0.0061 -0.0152 551 GLN A OE1 4200 N NE2 . GLN A 551 ? 0.2935 0.3710 0.2651 0.0215 -0.0131 -0.0068 551 GLN A NE2 4201 N N . GLY A 552 ? 0.2427 0.2489 0.2039 0.0070 -0.0058 -0.0208 552 GLY A N 4202 C CA . GLY A 552 ? 0.2442 0.2426 0.1998 0.0081 -0.0029 -0.0237 552 GLY A CA 4203 C C . GLY A 552 ? 0.2404 0.2424 0.2011 -0.0004 -0.0008 -0.0194 552 GLY A C 4204 O O . GLY A 552 ? 0.2599 0.2404 0.2028 -0.0065 -0.0056 -0.0259 552 GLY A O 4205 N N . VAL A 553 ? 0.2306 0.2374 0.1938 0.0094 0.0011 -0.0217 553 VAL A N 4206 C CA . VAL A 553 ? 0.2274 0.2375 0.1920 -0.0005 0.0007 -0.0201 553 VAL A CA 4207 C C . VAL A 553 ? 0.2365 0.2404 0.2075 0.0068 0.0018 -0.0163 553 VAL A C 4208 O O . VAL A 553 ? 0.2363 0.2511 0.2089 0.0110 -0.0029 -0.0131 553 VAL A O 4209 C CB . VAL A 553 ? 0.2214 0.2236 0.1851 0.0031 0.0177 -0.0167 553 VAL A CB 4210 C CG1 . VAL A 553 ? 0.2574 0.2295 0.1748 -0.0158 0.0003 -0.0178 553 VAL A CG1 4211 C CG2 . VAL A 553 ? 0.1868 0.2438 0.2091 -0.0203 0.0068 -0.0087 553 VAL A CG2 4212 N N . THR A 554 ? 0.2328 0.2494 0.2210 0.0127 -0.0048 -0.0112 554 THR A N 4213 C CA . THR A 554 ? 0.2432 0.2527 0.2276 0.0150 0.0059 -0.0084 554 THR A CA 4214 C C . THR A 554 ? 0.2417 0.2665 0.2316 0.0125 0.0000 -0.0063 554 THR A C 4215 O O . THR A 554 ? 0.2582 0.2703 0.2166 0.0179 0.0114 -0.0072 554 THR A O 4216 C CB . THR A 554 ? 0.2509 0.2572 0.2300 0.0089 0.0012 -0.0034 554 THR A CB 4217 O OG1 . THR A 554 ? 0.2537 0.2576 0.2269 0.0202 0.0106 -0.0013 554 THR A OG1 4218 C CG2 . THR A 554 ? 0.2605 0.2421 0.2475 0.0192 -0.0002 -0.0122 554 THR A CG2 4219 N N . ASP A 555 ? 0.2382 0.2647 0.2167 0.0066 -0.0001 -0.0080 555 ASP A N 4220 C CA . ASP A 555 ? 0.2503 0.2739 0.2318 0.0068 -0.0014 -0.0102 555 ASP A CA 4221 C C . ASP A 555 ? 0.2489 0.2775 0.2407 0.0028 0.0010 -0.0061 555 ASP A C 4222 O O . ASP A 555 ? 0.2477 0.2995 0.2560 -0.0013 -0.0022 -0.0091 555 ASP A O 4223 C CB . ASP A 555 ? 0.2507 0.2788 0.2280 -0.0011 0.0018 -0.0130 555 ASP A CB 4224 C CG . ASP A 555 ? 0.2439 0.2724 0.2415 0.0042 -0.0062 -0.0105 555 ASP A CG 4225 O OD1 . ASP A 555 ? 0.2546 0.2807 0.2294 0.0133 0.0140 -0.0191 555 ASP A OD1 4226 O OD2 . ASP A 555 ? 0.2631 0.2857 0.2389 0.0119 0.0055 -0.0350 555 ASP A OD2 4227 N N . ALA A 556 ? 0.2330 0.2690 0.2256 0.0090 -0.0022 -0.0079 556 ALA A N 4228 C CA . ALA A 556 ? 0.2295 0.2705 0.2269 0.0126 0.0011 -0.0092 556 ALA A CA 4229 C C . ALA A 556 ? 0.2298 0.2627 0.2249 0.0077 0.0041 -0.0096 556 ALA A C 4230 O O . ALA A 556 ? 0.2369 0.2698 0.2215 0.0109 0.0109 -0.0025 556 ALA A O 4231 C CB . ALA A 556 ? 0.2287 0.2663 0.2295 0.0114 -0.0090 -0.0060 556 ALA A CB 4232 N N . LEU A 557 ? 0.2281 0.2593 0.2123 0.0140 0.0037 -0.0130 557 LEU A N 4233 C CA . LEU A 557 ? 0.2182 0.2524 0.2149 0.0063 0.0048 -0.0117 557 LEU A CA 4234 C C . LEU A 557 ? 0.2283 0.2632 0.2244 0.0050 0.0052 -0.0123 557 LEU A C 4235 O O . LEU A 557 ? 0.2230 0.2708 0.2132 0.0014 0.0095 -0.0164 557 LEU A O 4236 C CB . LEU A 557 ? 0.2162 0.2510 0.2099 0.0038 0.0066 -0.0097 557 LEU A CB 4237 C CG . LEU A 557 ? 0.2233 0.2646 0.2068 -0.0035 -0.0048 -0.0038 557 LEU A CG 4238 C CD1 . LEU A 557 ? 0.2576 0.2728 0.2481 -0.0069 0.0179 -0.0035 557 LEU A CD1 4239 C CD2 . LEU A 557 ? 0.2301 0.3032 0.2147 -0.0176 -0.0102 0.0139 557 LEU A CD2 4240 N N . PHE A 558 ? 0.2281 0.2641 0.2313 0.0029 0.0021 -0.0140 558 PHE A N 4241 C CA . PHE A 558 ? 0.2376 0.2758 0.2428 0.0048 -0.0011 -0.0138 558 PHE A CA 4242 C C . PHE A 558 ? 0.2491 0.2893 0.2486 0.0005 0.0017 -0.0145 558 PHE A C 4243 O O . PHE A 558 ? 0.2473 0.3008 0.2661 0.0010 0.0020 -0.0254 558 PHE A O 4244 C CB . PHE A 558 ? 0.2362 0.2696 0.2371 -0.0012 0.0025 -0.0095 558 PHE A CB 4245 C CG . PHE A 558 ? 0.2389 0.2673 0.2527 0.0075 -0.0025 -0.0079 558 PHE A CG 4246 C CD1 . PHE A 558 ? 0.2386 0.2649 0.2281 -0.0005 -0.0082 -0.0099 558 PHE A CD1 4247 C CD2 . PHE A 558 ? 0.2627 0.2837 0.2872 0.0053 0.0116 -0.0047 558 PHE A CD2 4248 C CE1 . PHE A 558 ? 0.2712 0.2711 0.2443 -0.0068 0.0074 -0.0002 558 PHE A CE1 4249 C CE2 . PHE A 558 ? 0.2780 0.2688 0.2884 0.0052 0.0078 -0.0103 558 PHE A CE2 4250 C CZ . PHE A 558 ? 0.2808 0.2872 0.2502 0.0001 0.0064 -0.0037 558 PHE A CZ 4251 N N . GLY A 559 ? 0.2613 0.2871 0.2509 -0.0031 -0.0007 -0.0165 559 GLY A N 4252 C CA . GLY A 559 ? 0.2805 0.3084 0.2718 -0.0089 0.0015 -0.0132 559 GLY A CA 4253 C C . GLY A 559 ? 0.2919 0.3128 0.2791 -0.0120 0.0004 -0.0134 559 GLY A C 4254 O O . GLY A 559 ? 0.2974 0.3366 0.2880 -0.0181 -0.0008 -0.0190 559 GLY A O 4255 N N . ASP A 560 ? 0.2978 0.3226 0.2891 -0.0064 -0.0027 -0.0167 560 ASP A N 4256 C CA . ASP A 560 ? 0.3099 0.3314 0.2979 -0.0012 -0.0022 -0.0107 560 ASP A CA 4257 C C . ASP A 560 ? 0.3058 0.3252 0.2941 -0.0014 0.0017 -0.0139 560 ASP A C 4258 O O . ASP A 560 ? 0.3035 0.3359 0.3109 -0.0006 -0.0078 -0.0165 560 ASP A O 4259 C CB . ASP A 560 ? 0.3209 0.3313 0.3012 -0.0004 -0.0053 -0.0087 560 ASP A CB 4260 C CG . ASP A 560 ? 0.3521 0.3632 0.3474 0.0089 -0.0006 -0.0045 560 ASP A CG 4261 O OD1 . ASP A 560 ? 0.3818 0.4066 0.3843 0.0215 -0.0080 -0.0191 560 ASP A OD1 4262 O OD2 . ASP A 560 ? 0.4415 0.4254 0.4217 -0.0020 0.0065 0.0106 560 ASP A OD2 4263 N N . PHE A 561 ? 0.3000 0.3259 0.2841 -0.0018 0.0042 -0.0114 561 PHE A N 4264 C CA . PHE A 561 ? 0.3047 0.3289 0.2874 -0.0039 0.0033 -0.0064 561 PHE A CA 4265 C C . PHE A 561 ? 0.3048 0.3265 0.2855 -0.0019 0.0035 -0.0013 561 PHE A C 4266 O O . PHE A 561 ? 0.3323 0.3321 0.2910 -0.0074 -0.0028 -0.0001 561 PHE A O 4267 C CB . PHE A 561 ? 0.3024 0.3284 0.2922 -0.0038 0.0059 -0.0089 561 PHE A CB 4268 C CG . PHE A 561 ? 0.2981 0.3356 0.2948 -0.0056 0.0031 -0.0023 561 PHE A CG 4269 C CD1 . PHE A 561 ? 0.3022 0.3526 0.3178 -0.0053 -0.0020 0.0014 561 PHE A CD1 4270 C CD2 . PHE A 561 ? 0.3143 0.3468 0.3034 0.0023 0.0069 -0.0053 561 PHE A CD2 4271 C CE1 . PHE A 561 ? 0.3423 0.3481 0.3165 -0.0023 0.0071 -0.0095 561 PHE A CE1 4272 C CE2 . PHE A 561 ? 0.3176 0.3482 0.2989 -0.0061 0.0001 -0.0146 561 PHE A CE2 4273 C CZ . PHE A 561 ? 0.3269 0.3542 0.3109 -0.0038 0.0024 -0.0112 561 PHE A CZ 4274 N N . GLY A 562 ? 0.3000 0.3251 0.2893 0.0008 0.0050 -0.0041 562 GLY A N 4275 C CA . GLY A 562 ? 0.2763 0.3167 0.2745 -0.0009 0.0030 -0.0052 562 GLY A CA 4276 C C . GLY A 562 ? 0.2766 0.3118 0.2727 -0.0030 0.0068 -0.0058 562 GLY A C 4277 O O . GLY A 562 ? 0.2892 0.3238 0.2815 0.0024 0.0051 -0.0197 562 GLY A O 4278 N N . PHE A 563 ? 0.2643 0.3012 0.2694 -0.0070 0.0094 -0.0021 563 PHE A N 4279 C CA . PHE A 563 ? 0.2582 0.2807 0.2590 0.0023 0.0059 -0.0024 563 PHE A CA 4280 C C . PHE A 563 ? 0.2609 0.2818 0.2690 0.0001 0.0130 0.0042 563 PHE A C 4281 O O . PHE A 563 ? 0.2621 0.2819 0.2587 0.0127 0.0248 0.0153 563 PHE A O 4282 C CB . PHE A 563 ? 0.2572 0.2813 0.2544 -0.0087 0.0039 -0.0022 563 PHE A CB 4283 C CG . PHE A 563 ? 0.2350 0.2671 0.2344 -0.0006 -0.0035 -0.0078 563 PHE A CG 4284 C CD1 . PHE A 563 ? 0.2745 0.2722 0.2441 -0.0025 0.0154 -0.0088 563 PHE A CD1 4285 C CD2 . PHE A 563 ? 0.2537 0.2705 0.2156 -0.0071 0.0032 -0.0004 563 PHE A CD2 4286 C CE1 . PHE A 563 ? 0.2720 0.2727 0.2260 -0.0031 0.0109 -0.0025 563 PHE A CE1 4287 C CE2 . PHE A 563 ? 0.2597 0.2696 0.2198 0.0019 0.0002 -0.0075 563 PHE A CE2 4288 C CZ . PHE A 563 ? 0.2604 0.2765 0.2388 -0.0007 0.0014 -0.0053 563 PHE A CZ 4289 N N . THR A 564 ? 0.2531 0.2734 0.2559 -0.0021 0.0173 0.0045 564 THR A N 4290 C CA . THR A 564 ? 0.2523 0.2814 0.2591 -0.0021 0.0169 0.0037 564 THR A CA 4291 C C . THR A 564 ? 0.2501 0.2747 0.2522 -0.0014 0.0147 0.0052 564 THR A C 4292 O O . THR A 564 ? 0.2352 0.2686 0.2558 -0.0022 0.0264 0.0152 564 THR A O 4293 C CB . THR A 564 ? 0.2569 0.2803 0.2683 -0.0046 0.0094 0.0043 564 THR A CB 4294 O OG1 . THR A 564 ? 0.2824 0.3135 0.2685 -0.0071 0.0182 -0.0079 564 THR A OG1 4295 C CG2 . THR A 564 ? 0.2701 0.3054 0.2901 -0.0151 0.0154 0.0011 564 THR A CG2 4296 N N . GLY A 565 ? 0.2353 0.2639 0.2389 -0.0004 0.0142 0.0185 565 GLY A N 4297 C CA . GLY A 565 ? 0.2370 0.2694 0.2406 -0.0001 0.0149 0.0173 565 GLY A CA 4298 C C . GLY A 565 ? 0.2430 0.2730 0.2396 -0.0007 0.0101 0.0113 565 GLY A C 4299 O O . GLY A 565 ? 0.2484 0.2834 0.2383 0.0000 0.0112 0.0102 565 GLY A O 4300 N N . ARG A 566 ? 0.2461 0.2656 0.2380 0.0029 0.0127 0.0163 566 ARG A N 4301 C CA . ARG A 566 ? 0.2558 0.2762 0.2435 0.0021 0.0130 0.0136 566 ARG A CA 4302 C C . ARG A 566 ? 0.2574 0.2695 0.2396 0.0086 0.0116 0.0099 566 ARG A C 4303 O O . ARG A 566 ? 0.2513 0.2761 0.2178 0.0144 0.0276 0.0198 566 ARG A O 4304 C CB . ARG A 566 ? 0.2677 0.2719 0.2498 -0.0034 0.0096 0.0125 566 ARG A CB 4305 C CG . ARG A 566 ? 0.2980 0.3010 0.3091 -0.0114 0.0109 0.0150 566 ARG A CG 4306 C CD . ARG A 566 ? 0.3934 0.3578 0.3861 -0.0161 0.0068 0.0311 566 ARG A CD 4307 N NE . ARG A 566 ? 0.4187 0.3922 0.4119 -0.0224 0.0106 -0.0024 566 ARG A NE 4308 C CZ . ARG A 566 ? 0.4987 0.4766 0.4809 -0.0217 0.0096 0.0193 566 ARG A CZ 4309 N NH1 . ARG A 566 ? 0.4488 0.4664 0.4889 0.0072 0.0012 0.0058 566 ARG A NH1 4310 N NH2 . ARG A 566 ? 0.4603 0.4448 0.4643 -0.0035 0.0278 -0.0088 566 ARG A NH2 4311 N N . LEU A 567 ? 0.2515 0.2661 0.2229 0.0134 0.0094 0.0176 567 LEU A N 4312 C CA . LEU A 567 ? 0.2541 0.2536 0.2180 0.0154 0.0137 0.0131 567 LEU A CA 4313 C C . LEU A 567 ? 0.2614 0.2627 0.2171 0.0189 0.0172 0.0181 567 LEU A C 4314 O O . LEU A 567 ? 0.2711 0.2677 0.2108 0.0225 0.0297 0.0266 567 LEU A O 4315 C CB . LEU A 567 ? 0.2506 0.2460 0.2090 0.0254 0.0136 0.0141 567 LEU A CB 4316 C CG . LEU A 567 ? 0.2701 0.2297 0.1878 0.0111 0.0013 0.0136 567 LEU A CG 4317 C CD1 . LEU A 567 ? 0.2624 0.2512 0.1932 0.0134 -0.0067 -0.0001 567 LEU A CD1 4318 C CD2 . LEU A 567 ? 0.2704 0.2267 0.2115 0.0060 0.0154 0.0200 567 LEU A CD2 4319 N N . PRO A 568 ? 0.2570 0.2687 0.2141 0.0158 0.0212 0.0221 568 PRO A N 4320 C CA . PRO A 568 ? 0.2721 0.2832 0.2182 0.0177 0.0152 0.0177 568 PRO A CA 4321 C C . PRO A 568 ? 0.2728 0.2919 0.2269 0.0131 0.0106 0.0170 568 PRO A C 4322 O O . PRO A 568 ? 0.2891 0.3114 0.2319 0.0193 0.0112 0.0237 568 PRO A O 4323 C CB . PRO A 568 ? 0.2693 0.2771 0.2087 0.0203 0.0253 0.0223 568 PRO A CB 4324 C CG . PRO A 568 ? 0.2716 0.2693 0.2122 0.0086 0.0317 0.0121 568 PRO A CG 4325 C CD . PRO A 568 ? 0.2580 0.2712 0.2063 0.0209 0.0247 0.0266 568 PRO A CD 4326 N N . ARG A 569 ? 0.2752 0.3094 0.2229 0.0080 0.0155 0.0168 569 ARG A N 4327 C CA . ARG A 569 ? 0.2897 0.3219 0.2237 0.0102 0.0047 0.0110 569 ARG A CA 4328 C C . ARG A 569 ? 0.2860 0.3226 0.2251 0.0137 0.0041 0.0082 569 ARG A C 4329 O O . ARG A 569 ? 0.2839 0.3295 0.2115 0.0220 0.0025 0.0216 569 ARG A O 4330 C CB . ARG A 569 ? 0.2869 0.3257 0.2345 0.0003 0.0094 0.0037 569 ARG A CB 4331 C CG . ARG A 569 ? 0.3154 0.3527 0.2644 0.0050 -0.0060 0.0145 569 ARG A CG 4332 C CD . ARG A 569 ? 0.3098 0.3309 0.2809 0.0086 -0.0070 0.0114 569 ARG A CD 4333 N NE . ARG A 569 ? 0.3202 0.3669 0.2820 0.0163 0.0005 0.0201 569 ARG A NE 4334 C CZ . ARG A 569 ? 0.3083 0.3396 0.2933 0.0175 -0.0023 0.0030 569 ARG A CZ 4335 N NH1 . ARG A 569 ? 0.3114 0.3290 0.3044 0.0055 0.0015 0.0227 569 ARG A NH1 4336 N NH2 . ARG A 569 ? 0.3167 0.3614 0.3089 0.0113 0.0041 0.0011 569 ARG A NH2 4337 N N . THR A 570 ? 0.2927 0.3179 0.2294 0.0223 0.0010 0.0080 570 THR A N 4338 C CA . THR A 570 ? 0.2866 0.3144 0.2308 0.0214 0.0035 0.0092 570 THR A CA 4339 C C . THR A 570 ? 0.2819 0.3113 0.2396 0.0229 0.0069 0.0118 570 THR A C 4340 O O . THR A 570 ? 0.2882 0.3179 0.2506 0.0295 0.0133 0.0087 570 THR A O 4341 C CB . THR A 570 ? 0.2873 0.3102 0.2343 0.0222 0.0000 0.0114 570 THR A CB 4342 O OG1 . THR A 570 ? 0.2874 0.3220 0.2312 0.0256 0.0148 0.0250 570 THR A OG1 4343 C CG2 . THR A 570 ? 0.2992 0.3247 0.2583 0.0241 -0.0011 0.0098 570 THR A CG2 4344 N N . TRP A 571 ? 0.2778 0.3075 0.2174 0.0224 0.0100 0.0136 571 TRP A N 4345 C CA . TRP A 571 ? 0.2641 0.3041 0.2119 0.0129 0.0034 0.0125 571 TRP A CA 4346 C C . TRP A 571 ? 0.2745 0.3197 0.2265 0.0088 0.0019 0.0084 571 TRP A C 4347 O O . TRP A 571 ? 0.2809 0.3349 0.2212 0.0079 0.0013 0.0216 571 TRP A O 4348 C CB . TRP A 571 ? 0.2571 0.2965 0.2277 0.0111 0.0077 0.0096 571 TRP A CB 4349 C CG . TRP A 571 ? 0.2435 0.2883 0.2199 0.0100 0.0075 0.0125 571 TRP A CG 4350 C CD1 . TRP A 571 ? 0.2542 0.2898 0.2205 0.0139 0.0056 0.0087 571 TRP A CD1 4351 C CD2 . TRP A 571 ? 0.2530 0.2878 0.2433 0.0125 0.0008 0.0072 571 TRP A CD2 4352 N NE1 . TRP A 571 ? 0.2431 0.2986 0.2428 0.0188 -0.0032 0.0041 571 TRP A NE1 4353 C CE2 . TRP A 571 ? 0.2551 0.2881 0.2350 0.0057 0.0008 0.0021 571 TRP A CE2 4354 C CE3 . TRP A 571 ? 0.2447 0.2881 0.2387 0.0126 -0.0029 0.0026 571 TRP A CE3 4355 C CZ2 . TRP A 571 ? 0.2303 0.2811 0.2346 0.0099 0.0031 0.0015 571 TRP A CZ2 4356 C CZ3 . TRP A 571 ? 0.2442 0.2741 0.2308 0.0162 0.0046 0.0082 571 TRP A CZ3 4357 C CH2 . TRP A 571 ? 0.2384 0.2809 0.2237 0.0033 0.0037 -0.0021 571 TRP A CH2 4358 N N . PHE A 572 ? 0.2817 0.3240 0.2255 0.0075 -0.0012 0.0047 572 PHE A N 4359 C CA . PHE A 572 ? 0.2845 0.3263 0.2300 0.0064 -0.0063 0.0041 572 PHE A CA 4360 C C . PHE A 572 ? 0.2970 0.3377 0.2285 0.0132 -0.0065 0.0039 572 PHE A C 4361 O O . PHE A 572 ? 0.2887 0.3297 0.1963 0.0233 -0.0096 0.0009 572 PHE A O 4362 C CB . PHE A 572 ? 0.2884 0.3356 0.2471 0.0091 -0.0043 0.0048 572 PHE A CB 4363 C CG . PHE A 572 ? 0.2714 0.3083 0.2417 0.0041 -0.0046 0.0033 572 PHE A CG 4364 C CD1 . PHE A 572 ? 0.2565 0.3167 0.2466 0.0059 -0.0034 -0.0007 572 PHE A CD1 4365 C CD2 . PHE A 572 ? 0.2782 0.3072 0.2480 0.0086 -0.0031 -0.0011 572 PHE A CD2 4366 C CE1 . PHE A 572 ? 0.2846 0.3342 0.2532 -0.0018 0.0030 -0.0004 572 PHE A CE1 4367 C CE2 . PHE A 572 ? 0.2655 0.3039 0.2341 0.0008 -0.0064 0.0067 572 PHE A CE2 4368 C CZ . PHE A 572 ? 0.2733 0.3179 0.2310 0.0060 -0.0103 0.0010 572 PHE A CZ 4369 N N . LYS A 573 ? 0.3050 0.3491 0.2260 0.0173 -0.0130 0.0072 573 LYS A N 4370 C CA . LYS A 573 ? 0.3125 0.3553 0.2385 0.0149 -0.0066 0.0089 573 LYS A CA 4371 C C . LYS A 573 ? 0.3167 0.3600 0.2476 0.0170 -0.0085 0.0081 573 LYS A C 4372 O O . LYS A 573 ? 0.3137 0.3793 0.2640 0.0239 -0.0028 0.0023 573 LYS A O 4373 C CB . LYS A 573 ? 0.3212 0.3539 0.2385 0.0147 -0.0101 0.0129 573 LYS A CB 4374 C CG . LYS A 573 ? 0.3157 0.3447 0.2306 0.0079 0.0054 0.0183 573 LYS A CG 4375 C CD . LYS A 573 ? 0.3358 0.3650 0.2511 0.0086 -0.0093 0.0119 573 LYS A CD 4376 C CE . LYS A 573 ? 0.3674 0.3865 0.2992 0.0001 -0.0029 0.0248 573 LYS A CE 4377 N NZ . LYS A 573 ? 0.4034 0.4181 0.3095 0.0038 0.0176 0.0103 573 LYS A NZ 4378 N N . SER A 574 ? 0.3089 0.3679 0.2533 0.0147 -0.0062 0.0040 574 SER A N 4379 C CA . SER A 574 ? 0.3151 0.3797 0.2709 0.0140 -0.0142 -0.0016 574 SER A CA 4380 C C . SER A 574 ? 0.3039 0.3690 0.2632 0.0132 -0.0192 -0.0025 574 SER A C 4381 O O . SER A 574 ? 0.2906 0.3643 0.2455 0.0226 -0.0204 0.0042 574 SER A O 4382 C CB . SER A 574 ? 0.3284 0.3921 0.2869 0.0034 -0.0107 -0.0138 574 SER A CB 4383 O OG . SER A 574 ? 0.3844 0.4608 0.3569 -0.0011 -0.0192 -0.0045 574 SER A OG 4384 N N . VAL A 575 ? 0.2974 0.3763 0.2662 0.0175 -0.0214 0.0025 575 VAL A N 4385 C CA . VAL A 575 ? 0.3079 0.3787 0.2838 0.0181 -0.0219 0.0047 575 VAL A CA 4386 C C . VAL A 575 ? 0.3186 0.3865 0.2919 0.0183 -0.0194 0.0052 575 VAL A C 4387 O O . VAL A 575 ? 0.3047 0.3892 0.2701 0.0180 -0.0238 0.0082 575 VAL A O 4388 C CB . VAL A 575 ? 0.3109 0.3716 0.2908 0.0190 -0.0265 0.0060 575 VAL A CB 4389 C CG1 . VAL A 575 ? 0.3090 0.3797 0.2877 0.0178 -0.0411 0.0139 575 VAL A CG1 4390 C CG2 . VAL A 575 ? 0.3282 0.3673 0.3136 0.0069 -0.0179 0.0064 575 VAL A CG2 4391 N N . ASP A 576 ? 0.3335 0.3935 0.2976 0.0154 -0.0153 -0.0006 576 ASP A N 4392 C CA . ASP A 576 ? 0.3459 0.3916 0.3149 0.0148 -0.0092 0.0004 576 ASP A CA 4393 C C . ASP A 576 ? 0.3440 0.3910 0.3029 0.0172 -0.0042 0.0028 576 ASP A C 4394 O O . ASP A 576 ? 0.3471 0.4135 0.3071 0.0229 -0.0109 0.0053 576 ASP A O 4395 C CB A ASP A 576 ? 0.3474 0.3921 0.3193 0.0117 -0.0098 -0.0003 576 ASP A CB 4396 C CB B ASP A 576 ? 0.3541 0.3931 0.3257 0.0119 -0.0113 -0.0016 576 ASP A CB 4397 C CG A ASP A 576 ? 0.3694 0.3977 0.3687 0.0093 -0.0128 0.0010 576 ASP A CG 4398 C CG B ASP A 576 ? 0.3780 0.4073 0.3602 0.0044 -0.0020 0.0000 576 ASP A CG 4399 O OD1 A ASP A 576 ? 0.4071 0.4153 0.3720 0.0104 -0.0005 -0.0051 576 ASP A OD1 4400 O OD1 B ASP A 576 ? 0.4031 0.4223 0.3972 -0.0001 -0.0069 -0.0032 576 ASP A OD1 4401 O OD2 A ASP A 576 ? 0.3909 0.4248 0.3690 -0.0028 -0.0078 0.0029 576 ASP A OD2 4402 O OD2 B ASP A 576 ? 0.4276 0.4171 0.4127 0.0036 -0.0044 -0.0149 576 ASP A OD2 4403 N N . GLN A 577 ? 0.3269 0.3779 0.2711 0.0178 -0.0008 0.0034 577 GLN A N 4404 C CA . GLN A 577 ? 0.3211 0.3671 0.2758 0.0214 -0.0036 0.0113 577 GLN A CA 4405 C C . GLN A 577 ? 0.3213 0.3558 0.2823 0.0234 -0.0038 0.0104 577 GLN A C 4406 O O . GLN A 577 ? 0.3356 0.3590 0.2773 0.0320 -0.0116 0.0263 577 GLN A O 4407 C CB . GLN A 577 ? 0.3227 0.3718 0.2793 0.0244 0.0015 0.0098 577 GLN A CB 4408 C CG . GLN A 577 ? 0.3306 0.3736 0.2717 0.0228 -0.0076 0.0176 577 GLN A CG 4409 C CD . GLN A 577 ? 0.3134 0.3844 0.2801 0.0167 -0.0033 0.0313 577 GLN A CD 4410 O OE1 . GLN A 577 ? 0.3282 0.4118 0.2827 0.0306 0.0024 0.0066 577 GLN A OE1 4411 N NE2 . GLN A 577 ? 0.3563 0.4006 0.3034 0.0143 -0.0087 0.0169 577 GLN A NE2 4412 N N . LEU A 578 ? 0.3069 0.3550 0.2835 0.0282 -0.0019 0.0118 578 LEU A N 4413 C CA . LEU A 578 ? 0.3040 0.3542 0.2869 0.0262 -0.0017 0.0084 578 LEU A CA 4414 C C . LEU A 578 ? 0.3059 0.3604 0.2991 0.0217 -0.0022 0.0110 578 LEU A C 4415 O O . LEU A 578 ? 0.3189 0.3876 0.3032 0.0242 -0.0030 0.0070 578 LEU A O 4416 C CB . LEU A 578 ? 0.2914 0.3453 0.2766 0.0241 -0.0029 0.0112 578 LEU A CB 4417 C CG . LEU A 578 ? 0.2855 0.3271 0.2839 0.0207 -0.0009 0.0167 578 LEU A CG 4418 C CD1 . LEU A 578 ? 0.3210 0.3443 0.2708 0.0146 -0.0086 0.0162 578 LEU A CD1 4419 C CD2 . LEU A 578 ? 0.2938 0.3233 0.2763 0.0193 -0.0019 0.0222 578 LEU A CD2 4420 N N . PRO A 579 ? 0.3129 0.3632 0.3079 0.0228 -0.0029 0.0120 579 PRO A N 4421 C CA . PRO A 579 ? 0.3225 0.3679 0.3136 0.0231 -0.0010 0.0120 579 PRO A CA 4422 C C . PRO A 579 ? 0.3308 0.3771 0.3148 0.0226 -0.0006 0.0146 579 PRO A C 4423 O O . PRO A 579 ? 0.3305 0.3883 0.3074 0.0278 -0.0018 0.0247 579 PRO A O 4424 C CB . PRO A 579 ? 0.3230 0.3676 0.3185 0.0264 -0.0043 0.0114 579 PRO A CB 4425 C CG . PRO A 579 ? 0.3212 0.3629 0.3217 0.0200 -0.0109 0.0092 579 PRO A CG 4426 C CD . PRO A 579 ? 0.3189 0.3676 0.3164 0.0218 -0.0006 0.0073 579 PRO A CD 4427 N N . MET A 580 ? 0.3293 0.3819 0.3091 0.0211 -0.0014 0.0173 580 MET A N 4428 C CA . MET A 580 ? 0.3442 0.3836 0.3054 0.0260 0.0013 0.0216 580 MET A CA 4429 C C . MET A 580 ? 0.3508 0.3803 0.3249 0.0187 0.0074 0.0162 580 MET A C 4430 O O . MET A 580 ? 0.3474 0.3869 0.3195 0.0240 0.0054 0.0236 580 MET A O 4431 C CB . MET A 580 ? 0.3414 0.3787 0.3116 0.0218 0.0012 0.0151 580 MET A CB 4432 C CG . MET A 580 ? 0.3554 0.3717 0.3167 0.0285 0.0021 0.0210 580 MET A CG 4433 S SD . MET A 580 ? 0.3567 0.4332 0.2631 0.0618 -0.0104 0.0432 580 MET A SD 4434 C CE . MET A 580 ? 0.3307 0.3562 0.2924 0.0439 -0.0086 0.0212 580 MET A CE 4435 N N . ASN A 581 ? 0.3678 0.3805 0.3389 0.0181 0.0075 0.0171 581 ASN A N 4436 C CA . ASN A 581 ? 0.3752 0.3843 0.3511 0.0148 0.0070 0.0129 581 ASN A CA 4437 C C . ASN A 581 ? 0.3916 0.4009 0.3701 0.0154 0.0113 0.0098 581 ASN A C 4438 O O . ASN A 581 ? 0.3867 0.4027 0.3590 0.0125 0.0109 0.0137 581 ASN A O 4439 C CB . ASN A 581 ? 0.3773 0.3843 0.3465 0.0175 0.0078 0.0159 581 ASN A CB 4440 C CG . ASN A 581 ? 0.3682 0.3856 0.3410 0.0130 0.0121 0.0106 581 ASN A CG 4441 O OD1 . ASN A 581 ? 0.3648 0.4287 0.2903 0.0129 0.0037 0.0026 581 ASN A OD1 4442 N ND2 . ASN A 581 ? 0.3549 0.3833 0.3010 0.0136 0.0056 0.0260 581 ASN A ND2 4443 N N . VAL A 582 ? 0.4036 0.4085 0.3844 0.0113 0.0092 0.0074 582 VAL A N 4444 C CA . VAL A 582 ? 0.4317 0.4222 0.4096 0.0105 0.0092 0.0103 582 VAL A CA 4445 C C . VAL A 582 ? 0.4459 0.4298 0.4189 0.0134 0.0114 0.0124 582 VAL A C 4446 O O . VAL A 582 ? 0.4546 0.4259 0.4153 0.0156 0.0144 0.0171 582 VAL A O 4447 C CB . VAL A 582 ? 0.4337 0.4262 0.4123 0.0049 0.0066 0.0087 582 VAL A CB 4448 C CG1 . VAL A 582 ? 0.4301 0.4241 0.4183 0.0115 0.0042 0.0067 582 VAL A CG1 4449 C CG2 . VAL A 582 ? 0.4456 0.4363 0.4294 0.0037 0.0074 0.0083 582 VAL A CG2 4450 N N . GLY A 583 ? 0.4604 0.4450 0.4280 0.0119 0.0124 0.0135 583 GLY A N 4451 C CA . GLY A 583 ? 0.4642 0.4521 0.4425 0.0136 0.0096 0.0152 583 GLY A CA 4452 C C . GLY A 583 ? 0.4725 0.4674 0.4506 0.0103 0.0077 0.0136 583 GLY A C 4453 O O . GLY A 583 ? 0.4784 0.4657 0.4565 0.0135 0.0101 0.0177 583 GLY A O 4454 N N . ASP A 584 ? 0.4797 0.4726 0.4508 0.0112 0.0079 0.0127 584 ASP A N 4455 C CA . ASP A 584 ? 0.4861 0.4891 0.4584 0.0066 0.0059 0.0131 584 ASP A CA 4456 C C . ASP A 584 ? 0.4966 0.5051 0.4697 0.0077 0.0029 0.0148 584 ASP A C 4457 O O . ASP A 584 ? 0.4978 0.5044 0.4605 0.0115 0.0040 0.0227 584 ASP A O 4458 C CB . ASP A 584 ? 0.4829 0.4876 0.4578 0.0068 0.0072 0.0115 584 ASP A CB 4459 C CG . ASP A 584 ? 0.4767 0.4767 0.4458 0.0030 -0.0001 0.0117 584 ASP A CG 4460 O OD1 . ASP A 584 ? 0.4832 0.4790 0.4457 0.0144 -0.0048 0.0192 584 ASP A OD1 4461 O OD2 . ASP A 584 ? 0.4512 0.4511 0.4153 0.0155 0.0009 0.0316 584 ASP A OD2 4462 N N . ALA A 585 ? 0.5067 0.5230 0.4874 0.0087 0.0002 0.0107 585 ALA A N 4463 C CA . ALA A 585 ? 0.5173 0.5343 0.5010 0.0088 -0.0022 0.0083 585 ALA A CA 4464 C C . ALA A 585 ? 0.5210 0.5369 0.5111 0.0077 -0.0023 0.0067 585 ALA A C 4465 O O . ALA A 585 ? 0.5327 0.5558 0.5186 0.0068 0.0012 0.0070 585 ALA A O 4466 C CB . ALA A 585 ? 0.5183 0.5384 0.5080 0.0086 -0.0024 0.0092 585 ALA A CB 4467 N N . HIS A 586 ? 0.5159 0.5294 0.5109 0.0084 -0.0065 0.0058 586 HIS A N 4468 C CA . HIS A 586 ? 0.5148 0.5232 0.5138 0.0091 -0.0087 0.0063 586 HIS A CA 4469 C C . HIS A 586 ? 0.5027 0.5041 0.4947 0.0106 -0.0109 0.0070 586 HIS A C 4470 O O . HIS A 586 ? 0.5196 0.5187 0.5073 0.0153 -0.0118 0.0064 586 HIS A O 4471 C CB A HIS A 586 ? 0.5210 0.5281 0.5196 0.0056 -0.0060 0.0049 586 HIS A CB 4472 C CB B HIS A 586 ? 0.5181 0.5270 0.5178 0.0062 -0.0072 0.0049 586 HIS A CB 4473 C CG A HIS A 586 ? 0.5384 0.5434 0.5330 0.0045 -0.0081 0.0027 586 HIS A CG 4474 C CG B HIS A 586 ? 0.5350 0.5326 0.5279 0.0027 -0.0024 0.0068 586 HIS A CG 4475 N ND1 A HIS A 586 ? 0.5565 0.5569 0.5504 0.0003 -0.0046 -0.0034 586 HIS A ND1 4476 N ND1 B HIS A 586 ? 0.5506 0.5479 0.5447 0.0000 -0.0026 0.0000 586 HIS A ND1 4477 C CD2 A HIS A 586 ? 0.5514 0.5491 0.5483 0.0049 -0.0057 0.0010 586 HIS A CD2 4478 C CD2 B HIS A 586 ? 0.5406 0.5371 0.5324 0.0033 -0.0022 0.0024 586 HIS A CD2 4479 C CE1 A HIS A 586 ? 0.5580 0.5457 0.5527 0.0032 -0.0055 -0.0021 586 HIS A CE1 4480 C CE1 B HIS A 586 ? 0.5500 0.5401 0.5288 0.0017 -0.0053 0.0051 586 HIS A CE1 4481 N NE2 A HIS A 586 ? 0.5622 0.5620 0.5570 0.0032 -0.0046 0.0005 586 HIS A NE2 4482 N NE2 B HIS A 586 ? 0.5376 0.5421 0.5366 0.0062 -0.0049 0.0046 586 HIS A NE2 4483 N N . TYR A 587 ? 0.4698 0.4710 0.4571 0.0162 -0.0105 0.0142 587 TYR A N 4484 C CA . TYR A 587 ? 0.4357 0.4367 0.4123 0.0144 -0.0024 0.0152 587 TYR A CA 4485 C C . TYR A 587 ? 0.4265 0.4231 0.3985 0.0140 -0.0014 0.0178 587 TYR A C 4486 O O . TYR A 587 ? 0.4294 0.4307 0.4034 0.0203 0.0068 0.0222 587 TYR A O 4487 C CB . TYR A 587 ? 0.4240 0.4242 0.3896 0.0179 -0.0060 0.0222 587 TYR A CB 4488 C CG . TYR A 587 ? 0.4030 0.4064 0.3777 0.0119 -0.0021 0.0145 587 TYR A CG 4489 C CD1 . TYR A 587 ? 0.3885 0.3937 0.3648 0.0169 0.0009 0.0184 587 TYR A CD1 4490 C CD2 . TYR A 587 ? 0.3895 0.3950 0.3633 0.0209 0.0033 0.0151 587 TYR A CD2 4491 C CE1 . TYR A 587 ? 0.3854 0.3874 0.3445 0.0110 0.0016 0.0089 587 TYR A CE1 4492 C CE2 . TYR A 587 ? 0.3946 0.3897 0.3561 0.0154 -0.0008 0.0183 587 TYR A CE2 4493 C CZ . TYR A 587 ? 0.3973 0.3999 0.3705 0.0132 0.0023 0.0091 587 TYR A CZ 4494 O OH . TYR A 587 ? 0.3994 0.3774 0.3560 0.0227 0.0128 0.0278 587 TYR A OH 4495 N N . ASP A 588 ? 0.4045 0.4024 0.3585 0.0186 -0.0022 0.0205 588 ASP A N 4496 C CA . ASP A 588 ? 0.3835 0.3798 0.3370 0.0191 -0.0051 0.0274 588 ASP A CA 4497 C C . ASP A 588 ? 0.3563 0.3657 0.3159 0.0198 -0.0020 0.0230 588 ASP A C 4498 O O . ASP A 588 ? 0.3430 0.3521 0.2845 0.0310 -0.0105 0.0363 588 ASP A O 4499 C CB . ASP A 588 ? 0.3874 0.3853 0.3426 0.0136 -0.0033 0.0214 588 ASP A CB 4500 C CG . ASP A 588 ? 0.4109 0.4047 0.3573 0.0102 -0.0050 0.0197 588 ASP A CG 4501 O OD1 . ASP A 588 ? 0.4348 0.4558 0.3535 0.0081 0.0112 0.0225 588 ASP A OD1 4502 O OD2 . ASP A 588 ? 0.4693 0.4541 0.4051 0.0026 -0.0014 0.0112 588 ASP A OD2 4503 N N . PRO A 589 ? 0.3451 0.3549 0.2978 0.0228 0.0026 0.0230 589 PRO A N 4504 C CA . PRO A 589 ? 0.3362 0.3490 0.2925 0.0234 0.0039 0.0212 589 PRO A CA 4505 C C . PRO A 589 ? 0.3317 0.3460 0.2881 0.0218 0.0084 0.0203 589 PRO A C 4506 O O . PRO A 589 ? 0.3290 0.3549 0.2729 0.0276 0.0024 0.0254 589 PRO A O 4507 C CB . PRO A 589 ? 0.3437 0.3500 0.2981 0.0166 0.0051 0.0207 589 PRO A CB 4508 C CG . PRO A 589 ? 0.3431 0.3486 0.3069 0.0213 0.0040 0.0158 589 PRO A CG 4509 C CD . PRO A 589 ? 0.3397 0.3590 0.2892 0.0186 0.0031 0.0208 589 PRO A CD 4510 N N . LEU A 590 ? 0.3196 0.3346 0.2692 0.0259 0.0065 0.0128 590 LEU A N 4511 C CA . LEU A 590 ? 0.3148 0.3200 0.2615 0.0184 0.0116 0.0080 590 LEU A CA 4512 C C . LEU A 590 ? 0.3133 0.3240 0.2618 0.0166 0.0115 0.0122 590 LEU A C 4513 O O . LEU A 590 ? 0.3217 0.3360 0.2567 0.0102 0.0212 0.0153 590 LEU A O 4514 C CB . LEU A 590 ? 0.3147 0.3215 0.2628 0.0212 0.0122 0.0048 590 LEU A CB 4515 C CG . LEU A 590 ? 0.3079 0.3140 0.2673 0.0145 0.0047 0.0003 590 LEU A CG 4516 C CD1 . LEU A 590 ? 0.3352 0.3521 0.2707 0.0156 0.0192 -0.0012 590 LEU A CD1 4517 C CD2 . LEU A 590 ? 0.3105 0.3088 0.2540 0.0171 0.0091 0.0005 590 LEU A CD2 4518 N N . PHE A 591 ? 0.3064 0.3079 0.2490 0.0162 0.0083 0.0125 591 PHE A N 4519 C CA . PHE A 591 ? 0.3063 0.3065 0.2517 0.0164 0.0059 0.0153 591 PHE A CA 4520 C C . PHE A 591 ? 0.3058 0.3086 0.2638 0.0180 0.0032 0.0158 591 PHE A C 4521 O O . PHE A 591 ? 0.3072 0.3109 0.2532 0.0168 0.0034 0.0241 591 PHE A O 4522 C CB . PHE A 591 ? 0.2967 0.3105 0.2587 0.0186 0.0021 0.0145 591 PHE A CB 4523 C CG . PHE A 591 ? 0.3122 0.3112 0.2751 0.0094 0.0033 0.0075 591 PHE A CG 4524 C CD1 . PHE A 591 ? 0.3081 0.3158 0.2867 0.0129 0.0110 0.0076 591 PHE A CD1 4525 C CD2 . PHE A 591 ? 0.2921 0.3061 0.2741 0.0089 -0.0051 0.0105 591 PHE A CD2 4526 C CE1 . PHE A 591 ? 0.3280 0.3134 0.2810 0.0072 0.0149 0.0051 591 PHE A CE1 4527 C CE2 . PHE A 591 ? 0.2990 0.3085 0.2698 0.0165 -0.0038 0.0080 591 PHE A CE2 4528 C CZ . PHE A 591 ? 0.2921 0.3059 0.2525 0.0020 0.0033 0.0067 591 PHE A CZ 4529 N N . ARG A 592 ? 0.3267 0.3116 0.2646 0.0179 0.0108 0.0115 592 ARG A N 4530 C CA . ARG A 592 ? 0.3489 0.3236 0.3019 0.0217 0.0134 0.0119 592 ARG A CA 4531 C C . ARG A 592 ? 0.3261 0.3076 0.2754 0.0177 0.0139 0.0078 592 ARG A C 4532 O O . ARG A 592 ? 0.3311 0.3033 0.2601 0.0272 0.0257 0.0124 592 ARG A O 4533 C CB . ARG A 592 ? 0.3412 0.3229 0.3047 0.0105 0.0182 0.0124 592 ARG A CB 4534 C CG . ARG A 592 ? 0.3569 0.3557 0.3341 0.0071 0.0005 0.0101 592 ARG A CG 4535 C CD . ARG A 592 ? 0.3832 0.3532 0.3385 -0.0056 0.0000 0.0055 592 ARG A CD 4536 N NE . ARG A 592 ? 0.6280 0.5030 0.5626 -0.0208 0.0661 -0.0051 592 ARG A NE 4537 C CZ . ARG A 592 ? 0.4057 0.3917 0.3956 0.1059 -0.0471 -0.1356 592 ARG A CZ 4538 N NH1 . ARG A 592 ? 0.5712 0.6325 0.6717 0.0179 0.0235 0.0788 592 ARG A NH1 4539 N NH2 . ARG A 592 ? 0.6754 0.6896 0.5922 -0.1068 -0.0501 0.0644 592 ARG A NH2 4540 N N . LEU A 593 ? 0.3187 0.3017 0.2737 0.0212 0.0155 0.0139 593 LEU A N 4541 C CA . LEU A 593 ? 0.3167 0.3064 0.2753 0.0217 0.0138 0.0109 593 LEU A CA 4542 C C . LEU A 593 ? 0.3157 0.3057 0.2714 0.0185 0.0154 0.0177 593 LEU A C 4543 O O . LEU A 593 ? 0.3232 0.3135 0.2754 0.0084 0.0163 0.0330 593 LEU A O 4544 C CB . LEU A 593 ? 0.3193 0.3122 0.2791 0.0225 0.0183 0.0085 593 LEU A CB 4545 C CG . LEU A 593 ? 0.3135 0.3263 0.2919 0.0147 0.0065 0.0075 593 LEU A CG 4546 C CD1 . LEU A 593 ? 0.3242 0.3534 0.2813 0.0117 0.0155 0.0085 593 LEU A CD1 4547 C CD2 . LEU A 593 ? 0.3441 0.3434 0.2975 0.0012 0.0133 0.0036 593 LEU A CD2 4548 N N . GLY A 594 ? 0.3005 0.2941 0.2506 0.0202 0.0175 0.0192 594 GLY A N 4549 C CA . GLY A 594 ? 0.2960 0.2900 0.2483 0.0173 0.0182 0.0196 594 GLY A CA 4550 C C . GLY A 594 ? 0.2903 0.2805 0.2394 0.0144 0.0172 0.0238 594 GLY A C 4551 O O . GLY A 594 ? 0.2906 0.2934 0.2458 0.0175 0.0336 0.0252 594 GLY A O 4552 N N . TYR A 595 ? 0.2909 0.2841 0.2362 0.0185 0.0243 0.0248 595 TYR A N 4553 C CA . TYR A 595 ? 0.2889 0.2896 0.2560 0.0153 0.0188 0.0187 595 TYR A CA 4554 C C . TYR A 595 ? 0.2815 0.2921 0.2563 0.0154 0.0222 0.0164 595 TYR A C 4555 O O . TYR A 595 ? 0.2771 0.2787 0.2368 0.0150 0.0338 0.0279 595 TYR A O 4556 C CB . TYR A 595 ? 0.2991 0.3036 0.2627 0.0118 0.0191 0.0109 595 TYR A CB 4557 C CG . TYR A 595 ? 0.3044 0.3044 0.2932 0.0174 0.0082 0.0061 595 TYR A CG 4558 C CD1 . TYR A 595 ? 0.3340 0.3282 0.3133 0.0170 0.0073 0.0040 595 TYR A CD1 4559 C CD2 . TYR A 595 ? 0.3404 0.3390 0.3238 0.0123 0.0195 0.0005 595 TYR A CD2 4560 C CE1 . TYR A 595 ? 0.3477 0.3541 0.3252 0.0181 0.0195 -0.0010 595 TYR A CE1 4561 C CE2 . TYR A 595 ? 0.3473 0.3560 0.3365 0.0207 0.0214 0.0023 595 TYR A CE2 4562 C CZ . TYR A 595 ? 0.3405 0.3543 0.3375 0.0111 0.0156 -0.0072 595 TYR A CZ 4563 O OH . TYR A 595 ? 0.3608 0.3877 0.3635 0.0345 0.0194 -0.0294 595 TYR A OH 4564 N N . GLY A 596 ? 0.2735 0.2924 0.2469 0.0104 0.0222 0.0162 596 GLY A N 4565 C CA . GLY A 596 ? 0.2663 0.2943 0.2630 0.0138 0.0236 0.0129 596 GLY A CA 4566 C C . GLY A 596 ? 0.2710 0.2923 0.2673 0.0018 0.0200 0.0143 596 GLY A C 4567 O O . GLY A 596 ? 0.2828 0.2936 0.2883 0.0006 0.0319 0.0138 596 GLY A O 4568 N N . LEU A 597 ? 0.2668 0.2941 0.2623 0.0020 0.0217 0.0141 597 LEU A N 4569 C CA . LEU A 597 ? 0.2722 0.2977 0.2688 -0.0024 0.0158 0.0106 597 LEU A CA 4570 C C . LEU A 597 ? 0.2767 0.3067 0.2750 -0.0034 0.0134 0.0071 597 LEU A C 4571 O O . LEU A 597 ? 0.2817 0.3179 0.2786 -0.0118 0.0173 0.0109 597 LEU A O 4572 C CB . LEU A 597 ? 0.2766 0.3046 0.2683 -0.0013 0.0172 0.0047 597 LEU A CB 4573 C CG . LEU A 597 ? 0.2962 0.2964 0.2676 -0.0029 0.0032 0.0136 597 LEU A CG 4574 C CD1 . LEU A 597 ? 0.2896 0.3055 0.2438 0.0015 0.0134 0.0078 597 LEU A CD1 4575 C CD2 . LEU A 597 ? 0.3460 0.3309 0.2888 -0.0035 0.0048 0.0241 597 LEU A CD2 4576 N N . THR A 598 ? 0.2871 0.3108 0.2858 -0.0079 0.0144 0.0084 598 THR A N 4577 C CA . THR A 598 ? 0.3041 0.3212 0.2998 -0.0018 0.0138 0.0058 598 THR A CA 4578 C C . THR A 598 ? 0.3100 0.3209 0.3032 0.0017 0.0099 0.0063 598 THR A C 4579 O O . THR A 598 ? 0.3032 0.3259 0.3046 0.0036 0.0157 0.0079 598 THR A O 4580 C CB . THR A 598 ? 0.3181 0.3271 0.3094 -0.0034 0.0175 0.0108 598 THR A CB 4581 O OG1 . THR A 598 ? 0.3332 0.3352 0.3177 -0.0173 0.0413 0.0216 598 THR A OG1 4582 C CG2 . THR A 598 ? 0.3296 0.3267 0.3285 0.0071 0.0142 -0.0037 598 THR A CG2 4583 N N . THR A 599 ? 0.3194 0.3299 0.3124 -0.0011 0.0066 0.0047 599 THR A N 4584 C CA . THR A 599 ? 0.3216 0.3390 0.3156 -0.0032 0.0081 0.0049 599 THR A CA 4585 C C . THR A 599 ? 0.3452 0.3641 0.3408 -0.0026 0.0028 0.0040 599 THR A C 4586 O O . THR A 599 ? 0.3376 0.3701 0.3297 -0.0042 0.0082 0.0017 599 THR A O 4587 C CB . THR A 599 ? 0.3206 0.3377 0.3132 -0.0043 0.0094 -0.0016 599 THR A CB 4588 O OG1 . THR A 599 ? 0.3086 0.3197 0.2887 -0.0006 0.0056 0.0101 599 THR A OG1 4589 C CG2 . THR A 599 ? 0.3113 0.3216 0.2892 -0.0037 0.0135 -0.0012 599 THR A CG2 4590 N N . ASN A 600 ? 0.3606 0.3938 0.3726 -0.0049 0.0062 0.0033 600 ASN A N 4591 C CA . ASN A 600 ? 0.3903 0.4160 0.4076 -0.0092 0.0027 0.0029 600 ASN A CA 4592 C C . ASN A 600 ? 0.3940 0.4247 0.4189 -0.0100 0.0048 0.0057 600 ASN A C 4593 O O . ASN A 600 ? 0.3887 0.4278 0.4178 -0.0065 0.0067 0.0048 600 ASN A O 4594 C CB . ASN A 600 ? 0.3978 0.4246 0.4120 -0.0127 0.0058 0.0017 600 ASN A CB 4595 C CG . ASN A 600 ? 0.4603 0.4613 0.4688 -0.0115 -0.0012 0.0113 600 ASN A CG 4596 O OD1 . ASN A 600 ? 0.5255 0.4938 0.4827 -0.0041 0.0007 -0.0048 600 ASN A OD1 4597 N ND2 . ASN A 600 ? 0.5175 0.5349 0.5180 -0.0081 0.0099 -0.0082 600 ASN A ND2 4598 N N . ALA A 601 ? 0.4104 0.4463 0.4368 -0.0110 0.0074 0.0054 601 ALA A N 4599 C CA . ALA A 601 ? 0.4365 0.4638 0.4580 -0.0091 0.0045 0.0085 601 ALA A CA 4600 C C . ALA A 601 ? 0.4585 0.4887 0.4786 -0.0065 0.0054 0.0075 601 ALA A C 4601 O O . ALA A 601 ? 0.4581 0.4942 0.4858 -0.0120 0.0064 0.0139 601 ALA A O 4602 C CB . ALA A 601 ? 0.4309 0.4608 0.4559 -0.0091 0.0077 0.0066 601 ALA A CB 4603 N N . THR A 602 ? 0.4839 0.5095 0.4970 -0.0029 0.0040 0.0087 602 THR A N 4604 C CA . THR A 602 ? 0.5051 0.5371 0.5151 0.0010 0.0071 0.0046 602 THR A CA 4605 C C . THR A 602 ? 0.5183 0.5560 0.5271 0.0002 0.0058 0.0014 602 THR A C 4606 O O . THR A 602 ? 0.5301 0.5743 0.5402 0.0006 0.0074 0.0022 602 THR A O 4607 C CB . THR A 602 ? 0.5098 0.5385 0.5155 0.0018 0.0066 0.0035 602 THR A CB 4608 O OG1 . THR A 602 ? 0.5474 0.5675 0.5457 0.0058 0.0058 0.0118 602 THR A OG1 4609 C CG2 . THR A 602 ? 0.4939 0.5216 0.5033 0.0046 0.0081 0.0018 602 THR A CG2 4610 C C1 . NAG B . ? 0.4047 0.4568 0.4258 -0.0086 -0.0158 -0.0095 701 NAG A C1 4611 C C2 . NAG B . ? 0.4270 0.4809 0.4567 -0.0034 -0.0013 -0.0056 701 NAG A C2 4612 C C3 . NAG B . ? 0.4673 0.5182 0.4960 -0.0108 -0.0035 -0.0104 701 NAG A C3 4613 C C4 . NAG B . ? 0.5112 0.5349 0.5313 -0.0021 0.0021 -0.0093 701 NAG A C4 4614 C C5 . NAG B . ? 0.4797 0.5107 0.5043 -0.0084 -0.0093 -0.0086 701 NAG A C5 4615 C C6 . NAG B . ? 0.4962 0.5060 0.5162 -0.0038 -0.0053 -0.0081 701 NAG A C6 4616 C C7 . NAG B . ? 0.4275 0.4664 0.4379 0.0064 -0.0010 -0.0035 701 NAG A C7 4617 C C8 . NAG B . ? 0.4464 0.4737 0.4579 0.0037 -0.0006 0.0016 701 NAG A C8 4618 N N2 . NAG B . ? 0.4012 0.4771 0.4343 -0.0026 -0.0055 -0.0056 701 NAG A N2 4619 O O3 . NAG B . ? 0.4559 0.5346 0.5006 -0.0057 -0.0040 -0.0159 701 NAG A O3 4620 O O4 . NAG B . ? 0.5685 0.6186 0.6003 -0.0089 -0.0135 -0.0180 701 NAG A O4 4621 O O5 . NAG B . ? 0.4384 0.4768 0.4621 0.0030 -0.0006 -0.0074 701 NAG A O5 4622 O O6 . NAG B . ? 0.5004 0.5193 0.5074 -0.0037 0.0002 -0.0038 701 NAG A O6 4623 O O7 . NAG B . ? 0.4256 0.4828 0.4039 -0.0013 0.0059 -0.0031 701 NAG A O7 4624 C C1 . NAG C . ? 0.6595 0.6479 0.6611 -0.0068 0.0051 0.0117 702 NAG A C1 4625 C C2 . NAG C . ? 0.6707 0.6901 0.6390 -0.0095 0.0127 -0.0165 702 NAG A C2 4626 C C3 . NAG C . ? 0.7145 0.7095 0.7016 -0.0060 -0.0031 0.0012 702 NAG A C3 4627 C C4 . NAG C . ? 0.7385 0.7438 0.7360 -0.0043 -0.0023 -0.0059 702 NAG A C4 4628 C C5 . NAG C . ? 0.7252 0.7168 0.7203 -0.0037 0.0014 0.0025 702 NAG A C5 4629 C C6 . NAG C . ? 0.7191 0.7282 0.7089 -0.0064 -0.0004 -0.0065 702 NAG A C6 4630 C C7 . NAG C . ? 0.5704 0.5663 0.5665 0.1244 0.1001 0.0362 702 NAG A C7 4631 C C8 . NAG C . ? 0.8217 0.6988 0.8200 -0.0635 -0.0996 0.0326 702 NAG A C8 4632 N N2 . NAG C . ? 0.6988 0.7498 0.8108 -0.0186 -0.0391 -0.0677 702 NAG A N2 4633 O O3 . NAG C . ? 0.7171 0.7177 0.7255 -0.0038 -0.0026 -0.0027 702 NAG A O3 4634 O O4 . NAG C . ? 0.7930 0.7736 0.7825 -0.0035 -0.0008 0.0038 702 NAG A O4 4635 O O5 . NAG C . ? 0.6875 0.6937 0.6819 -0.0044 0.0026 -0.0072 702 NAG A O5 4636 O O6 . NAG C . ? 0.7470 0.7422 0.7359 -0.0007 0.0047 0.0038 702 NAG A O6 4637 O O7 . NAG C . ? 0.8189 0.8263 0.6812 -0.0973 -0.0026 -0.0308 702 NAG A O7 4638 C C1 . BMA D . ? 0.8130 0.8233 0.8239 -0.0054 0.0012 0.0001 703 BMA A C1 4639 C C2 . BMA D . ? 0.8362 0.8360 0.8336 -0.0028 0.0001 0.0018 703 BMA A C2 4640 C C3 . BMA D . ? 0.8419 0.8496 0.8503 -0.0028 0.0007 0.0002 703 BMA A C3 4641 C C4 . BMA D . ? 0.8481 0.8562 0.8503 -0.0031 -0.0002 0.0010 703 BMA A C4 4642 C C5 . BMA D . ? 0.8457 0.8592 0.8518 -0.0023 -0.0001 0.0005 703 BMA A C5 4643 C C6 . BMA D . ? 0.8485 0.8598 0.8500 -0.0013 -0.0034 -0.0001 703 BMA A C6 4644 O O2 . BMA D . ? 0.8383 0.8385 0.8446 -0.0006 -0.0001 0.0014 703 BMA A O2 4645 O O3 . BMA D . ? 0.8443 0.8408 0.8411 -0.0039 -0.0002 0.0018 703 BMA A O3 4646 O O4 . BMA D . ? 0.8514 0.8640 0.8700 0.0004 -0.0002 0.0035 703 BMA A O4 4647 O O5 . BMA D . ? 0.8400 0.8464 0.8377 -0.0065 -0.0021 -0.0018 703 BMA A O5 4648 O O6 . BMA D . ? 0.8501 0.8696 0.8558 0.0001 -0.0019 0.0002 703 BMA A O6 4649 C C1 . NAG E . ? 0.6880 0.6898 0.6563 0.0031 -0.0033 0.0175 704 NAG A C1 4650 C C2 . NAG E . ? 0.7903 0.7462 0.8222 -0.0118 -0.0225 0.0052 704 NAG A C2 4651 C C3 . NAG E . ? 0.7912 0.7854 0.7553 0.0078 -0.0009 0.0132 704 NAG A C3 4652 C C4 . NAG E . ? 0.7905 0.7778 0.7785 0.0040 0.0058 -0.0013 704 NAG A C4 4653 C C5 . NAG E . ? 0.7650 0.7707 0.7576 0.0002 -0.0010 0.0039 704 NAG A C5 4654 C C6 . NAG E . ? 0.7320 0.7668 0.7472 0.0000 0.0037 -0.0047 704 NAG A C6 4655 C C7 . NAG E . ? 0.9319 0.7971 0.8869 -0.0021 -0.0556 0.0844 704 NAG A C7 4656 C C8 . NAG E . ? 0.7203 0.7807 0.7672 -0.0202 -0.0119 -0.0140 704 NAG A C8 4657 N N2 . NAG E . ? 0.7309 0.7391 0.6184 0.0008 0.0030 -0.0690 704 NAG A N2 4658 O O3 . NAG E . ? 0.8321 0.8073 0.8158 -0.0021 0.0021 -0.0047 704 NAG A O3 4659 O O4 . NAG E . ? 0.8207 0.8134 0.8049 0.0024 -0.0022 -0.0013 704 NAG A O4 4660 O O5 . NAG E . ? 0.7145 0.7337 0.7065 0.0031 0.0116 -0.0040 704 NAG A O5 4661 O O6 . NAG E . ? 0.7722 0.7683 0.7592 0.0045 0.0109 0.0028 704 NAG A O6 4662 O O7 . NAG E . ? 0.6707 0.8043 0.6513 0.0417 0.0759 -0.0371 704 NAG A O7 4663 C C1 . NAG F . ? 0.8585 0.8488 0.8417 0.0010 0.0003 0.0020 705 NAG A C1 4664 C C2 . NAG F . ? 0.8782 0.9241 0.8642 0.0197 0.0068 0.0205 705 NAG A C2 4665 C C3 . NAG F . ? 0.8698 0.8601 0.8600 -0.0048 0.0041 0.0033 705 NAG A C3 4666 C C4 . NAG F . ? 0.8809 0.8711 0.8623 -0.0077 -0.0067 0.0015 705 NAG A C4 4667 C C5 . NAG F . ? 0.8923 0.9160 0.8827 0.0058 0.0082 0.0166 705 NAG A C5 4668 C C6 . NAG F . ? 0.7466 0.7471 0.8825 0.0896 0.0458 -0.0649 705 NAG A C6 4669 C C7 . NAG F . ? 1.0030 1.0175 0.9382 0.0147 -0.0147 0.1293 705 NAG A C7 4670 C C8 . NAG F . ? 0.7556 0.8171 0.8585 0.0630 0.0461 -0.0403 705 NAG A C8 4671 N N2 . NAG F . ? 0.7568 0.8126 0.8611 -0.0697 -0.0235 -0.0383 705 NAG A N2 4672 O O3 . NAG F . ? 0.8609 0.8602 0.8621 -0.0050 -0.0003 0.0006 705 NAG A O3 4673 O O4 . NAG F . ? 0.8715 0.8688 0.8696 -0.0031 0.0034 0.0022 705 NAG A O4 4674 O O5 . NAG F . ? 0.8648 0.8550 0.8518 -0.0146 -0.0005 -0.0014 705 NAG A O5 4675 O O6 . NAG F . ? 1.0292 0.9960 0.8670 -0.1050 -0.0594 0.0477 705 NAG A O6 4676 O O7 . NAG F . ? 0.9079 0.7626 0.8156 -0.0387 -0.0122 -0.0861 705 NAG A O7 4677 C C1 . BMA G . ? 0.8727 0.8770 0.8775 -0.0006 0.0006 0.0027 706 BMA A C1 4678 C C2 . BMA G . ? 0.8781 0.8799 0.8834 -0.0005 0.0018 0.0033 706 BMA A C2 4679 C C3 . BMA G . ? 0.8779 0.8773 0.8836 0.0000 0.0000 0.0027 706 BMA A C3 4680 C C4 . BMA G . ? 0.8689 0.8706 0.8781 -0.0014 0.0017 0.0042 706 BMA A C4 4681 C C5 . BMA G . ? 0.8565 0.8638 0.8667 -0.0004 -0.0029 0.0022 706 BMA A C5 4682 C C6 . BMA G . ? 0.8394 0.8404 0.8468 -0.0035 0.0040 0.0020 706 BMA A C6 4683 O O2 . BMA G . ? 0.8832 0.8825 0.8849 -0.0028 0.0041 0.0030 706 BMA A O2 4684 O O3 . BMA G . ? 0.8724 0.8794 0.8847 0.0000 0.0033 0.0029 706 BMA A O3 4685 O O4 . BMA G . ? 0.8774 0.8788 0.8864 0.0001 -0.0009 0.0042 706 BMA A O4 4686 O O5 . BMA G . ? 0.8654 0.8657 0.8728 -0.0018 0.0015 0.0038 706 BMA A O5 4687 O O6 . BMA G . ? 0.8068 0.8154 0.8167 -0.0010 -0.0037 -0.0028 706 BMA A O6 4688 C C1 . FUL H . ? 0.8574 0.8438 0.8501 0.0037 -0.0054 0.0018 707 FUL A C1 4689 C C2 . FUL H . ? 0.8681 0.8556 0.8620 0.0023 -0.0042 -0.0042 707 FUL A C2 4690 O O2 . FUL H . ? 0.8783 0.8697 0.8706 -0.0003 -0.0075 -0.0051 707 FUL A O2 4691 C C3 . FUL H . ? 0.8704 0.8640 0.8693 0.0010 -0.0029 -0.0010 707 FUL A C3 4692 O O3 . FUL H . ? 0.8725 0.8704 0.8723 -0.0007 -0.0017 -0.0041 707 FUL A O3 4693 C C4 . FUL H . ? 0.8703 0.8631 0.8676 0.0005 -0.0032 -0.0025 707 FUL A C4 4694 O O4 . FUL H . ? 0.8709 0.8671 0.8676 0.0015 -0.0019 -0.0043 707 FUL A O4 4695 C C5 . FUL H . ? 0.8669 0.8586 0.8646 0.0018 -0.0036 0.0000 707 FUL A C5 4696 C C6 . FUL H . ? 0.8629 0.8572 0.8599 -0.0012 -0.0015 0.0000 707 FUL A C6 4697 O O5 . FUL H . ? 0.8586 0.8504 0.8605 0.0001 -0.0067 -0.0027 707 FUL A O5 4698 C C1 . MAN I . ? 0.7939 0.7918 0.7906 -0.0026 0.0029 -0.0013 708 MAN A C1 4699 C C2 . MAN I . ? 0.7748 0.7781 0.7770 0.0012 0.0006 -0.0003 708 MAN A C2 4700 C C3 . MAN I . ? 0.7637 0.7696 0.7657 -0.0011 0.0009 0.0008 708 MAN A C3 4701 C C4 . MAN I . ? 0.7594 0.7559 0.7587 0.0001 0.0022 0.0002 708 MAN A C4 4702 C C5 . MAN I . ? 0.7698 0.7709 0.7633 -0.0018 0.0005 -0.0005 708 MAN A C5 4703 C C6 . MAN I . ? 0.7636 0.7588 0.7575 0.0001 0.0014 -0.0005 708 MAN A C6 4704 O O2 . MAN I . ? 0.7713 0.7673 0.7689 0.0062 0.0068 -0.0032 708 MAN A O2 4705 O O3 . MAN I . ? 0.7549 0.7561 0.7572 0.0000 -0.0022 -0.0008 708 MAN A O3 4706 O O4 . MAN I . ? 0.7472 0.7566 0.7445 -0.0062 0.0005 -0.0011 708 MAN A O4 4707 O O5 . MAN I . ? 0.7829 0.7786 0.7785 -0.0005 0.0007 -0.0001 708 MAN A O5 4708 O O6 . MAN I . ? 0.7381 0.7450 0.7423 -0.0026 0.0010 -0.0011 708 MAN A O6 4709 C C1 . NAG J . ? 0.7721 0.7835 0.7780 0.0006 -0.0028 0.0037 709 NAG A C1 4710 C C2 . NAG J . ? 0.7681 0.7710 0.7843 -0.0017 -0.0013 0.0042 709 NAG A C2 4711 C C3 . NAG J . ? 0.7725 0.7727 0.7720 0.0066 0.0003 0.0000 709 NAG A C3 4712 C C4 . NAG J . ? 0.7691 0.7566 0.7716 0.0024 0.0039 -0.0038 709 NAG A C4 4713 C C5 . NAG J . ? 0.7752 0.7704 0.7350 -0.0080 0.0046 0.0060 709 NAG A C5 4714 C C6 . NAG J . ? 0.9160 0.8885 0.7795 0.1237 -0.0286 -0.0362 709 NAG A C6 4715 C C7 . NAG J . ? 0.7659 0.8655 0.8551 0.0864 -0.0457 0.0137 709 NAG A C7 4716 C C8 . NAG J . ? 0.7264 0.7285 0.6235 -0.0265 0.0405 0.0282 709 NAG A C8 4717 N N2 . NAG J . ? 0.7671 0.6616 0.6820 -0.0169 0.0006 -0.0639 709 NAG A N2 4718 O O3 . NAG J . ? 0.7666 0.7699 0.7611 0.0026 -0.0020 -0.0045 709 NAG A O3 4719 O O4 . NAG J . ? 0.7843 0.7908 0.7800 0.0025 -0.0053 0.0003 709 NAG A O4 4720 O O5 . NAG J . ? 0.7689 0.7696 0.7696 -0.0029 0.0040 -0.0045 709 NAG A O5 4721 O O6 . NAG J . ? 0.6408 0.6498 0.8096 -0.1186 0.0373 0.0369 709 NAG A O6 4722 O O7 . NAG J . ? 0.6901 0.6094 0.7035 -0.0666 0.0116 0.0178 709 NAG A O7 4723 C C1 . NAG K . ? 0.6079 0.6041 0.6197 0.0049 0.0018 0.0092 710 NAG A C1 4724 C C2 . NAG K . ? 0.6766 0.6603 0.6655 -0.0012 0.0014 -0.0079 710 NAG A C2 4725 C C3 . NAG K . ? 0.6806 0.6832 0.7040 0.0030 0.0013 0.0035 710 NAG A C3 4726 C C4 . NAG K . ? 0.6674 0.6699 0.6718 -0.0017 0.0002 -0.0043 710 NAG A C4 4727 C C5 . NAG K . ? 0.6268 0.6408 0.6452 0.0017 0.0017 0.0025 710 NAG A C5 4728 C C6 . NAG K . ? 0.6296 0.6270 0.6417 0.0007 -0.0024 -0.0017 710 NAG A C6 4729 C C7 . NAG K . ? 0.8166 0.6720 0.8040 0.0203 -0.0030 -0.0533 710 NAG A C7 4730 C C8 . NAG K . ? 0.6033 0.7062 0.6828 -0.0253 0.0274 0.0088 710 NAG A C8 4731 N N2 . NAG K . ? 0.6333 0.6815 0.5860 0.0045 -0.0558 0.0112 710 NAG A N2 4732 O O3 . NAG K . ? 0.7402 0.7336 0.7287 -0.0015 -0.0051 -0.0103 710 NAG A O3 4733 O O4 . NAG K . ? 0.6798 0.6761 0.6924 -0.0033 -0.0040 0.0028 710 NAG A O4 4734 O O5 . NAG K . ? 0.6133 0.6323 0.6252 0.0030 0.0052 0.0002 710 NAG A O5 4735 O O6 . NAG K . ? 0.5749 0.6064 0.6073 -0.0084 0.0092 0.0061 710 NAG A O6 4736 O O7 . NAG K . ? 0.6846 0.7048 0.5956 -0.0162 0.0324 0.0365 710 NAG A O7 4737 C C1 . NAG L . ? 0.6878 0.6969 0.6892 -0.0019 0.0069 -0.0039 711 NAG A C1 4738 C C2 . NAG L . ? 0.7037 0.7036 0.6738 0.0019 -0.0016 -0.0039 711 NAG A C2 4739 C C3 . NAG L . ? 0.7039 0.7075 0.7026 0.0004 0.0042 0.0005 711 NAG A C3 4740 C C4 . NAG L . ? 0.7192 0.7164 0.7111 0.0074 0.0016 0.0005 711 NAG A C4 4741 C C5 . NAG L . ? 0.7216 0.7195 0.7386 0.0095 0.0079 0.0021 711 NAG A C5 4742 C C6 . NAG L . ? 0.5841 0.6081 0.7217 -0.1221 -0.0131 -0.0164 711 NAG A C6 4743 C C7 . NAG L . ? 0.5983 0.6440 0.5859 -0.1310 0.0038 -0.0213 711 NAG A C7 4744 C C8 . NAG L . ? 0.7537 0.7259 0.8288 0.0343 0.0436 0.0416 711 NAG A C8 4745 N N2 . NAG L . ? 0.7518 0.7082 0.7940 0.0242 -0.0337 -0.0036 711 NAG A N2 4746 O O3 . NAG L . ? 0.7074 0.7027 0.7023 0.0010 0.0070 0.0016 711 NAG A O3 4747 O O4 . NAG L . ? 0.7029 0.6991 0.7079 0.0029 0.0093 -0.0007 711 NAG A O4 4748 O O5 . NAG L . ? 0.7048 0.7113 0.7024 0.0049 0.0057 0.0000 711 NAG A O5 4749 O O6 . NAG L . ? 0.8655 0.8508 0.6884 0.1191 0.0116 0.0061 711 NAG A O6 4750 O O7 . NAG L . ? 0.8568 0.8012 0.7077 0.0804 0.0087 0.0124 711 NAG A O7 4751 C C1 . BMA M . ? 0.7042 0.7067 0.7093 0.0001 0.0081 0.0015 712 BMA A C1 4752 C C2 . BMA M . ? 0.6979 0.6962 0.6998 -0.0019 0.0041 -0.0008 712 BMA A C2 4753 C C3 . BMA M . ? 0.7149 0.7043 0.7107 -0.0023 0.0068 -0.0029 712 BMA A C3 4754 C C4 . BMA M . ? 0.7332 0.7115 0.7198 0.0016 0.0060 0.0005 712 BMA A C4 4755 C C5 . BMA M . ? 0.7423 0.7208 0.7302 0.0002 0.0059 -0.0016 712 BMA A C5 4756 C C6 . BMA M . ? 0.6119 0.7515 0.7359 -0.0090 -0.0301 -0.0004 712 BMA A C6 4757 O O2 . BMA M . ? 0.6788 0.6568 0.6710 -0.0045 0.0110 0.0025 712 BMA A O2 4758 O O3 . BMA M . ? 0.7222 0.7107 0.7173 0.0001 0.0085 -0.0034 712 BMA A O3 4759 O O4 . BMA M . ? 0.7320 0.7289 0.7372 -0.0005 0.0038 0.0008 712 BMA A O4 4760 O O5 . BMA M . ? 0.7292 0.7145 0.7147 0.0020 0.0082 0.0019 712 BMA A O5 4761 O O6 . BMA M . ? 0.8406 0.7253 0.7367 0.0109 0.0370 0.0021 712 BMA A O6 4762 C C1 . FUL N . ? 0.7749 0.7742 0.7824 -0.0064 0.0003 -0.0030 713 FUL A C1 4763 C C2 . FUL N . ? 0.7919 0.7899 0.7952 -0.0025 -0.0014 0.0006 713 FUL A C2 4764 O O2 . FUL N . ? 0.8017 0.8008 0.8038 -0.0058 0.0047 -0.0018 713 FUL A O2 4765 C C3 . FUL N . ? 0.8045 0.8025 0.8088 0.0010 0.0004 -0.0017 713 FUL A C3 4766 O O3 . FUL N . ? 0.8077 0.8104 0.8188 0.0011 0.0010 0.0000 713 FUL A O3 4767 C C4 . FUL N . ? 0.8096 0.8116 0.8112 0.0023 -0.0008 -0.0021 713 FUL A C4 4768 O O4 . FUL N . ? 0.8089 0.8156 0.8210 -0.0002 0.0038 -0.0009 713 FUL A O4 4769 C C5 . FUL N . ? 0.8100 0.8071 0.8128 -0.0006 -0.0023 -0.0023 713 FUL A C5 4770 C C6 . FUL N . ? 0.8151 0.8171 0.8128 0.0021 -0.0034 -0.0019 713 FUL A C6 4771 O O5 . FUL N . ? 0.7935 0.7952 0.7967 -0.0035 -0.0041 -0.0057 713 FUL A O5 4772 C C1B . XYP O . ? 0.6534 0.6445 0.6465 -0.0079 0.0002 -0.0034 714 XYP A C1B 4773 C C2B . XYP O . ? 0.6408 0.6232 0.6279 -0.0078 0.0061 0.0010 714 XYP A C2B 4774 C C3B . XYP O . ? 0.6279 0.6219 0.6132 -0.0085 0.0037 0.0018 714 XYP A C3B 4775 C C4B . XYP O . ? 0.6338 0.6201 0.6149 -0.0066 0.0025 0.0009 714 XYP A C4B 4776 C C5B . XYP O . ? 0.6404 0.6325 0.6307 -0.0088 -0.0006 0.0011 714 XYP A C5B 4777 O O2B . XYP O . ? 0.6252 0.6168 0.6201 -0.0141 0.0053 0.0050 714 XYP A O2B 4778 O O3B . XYP O . ? 0.6149 0.5894 0.5949 -0.0084 0.0095 0.0032 714 XYP A O3B 4779 O O4B . XYP O . ? 0.6220 0.6141 0.5949 -0.0103 0.0041 0.0037 714 XYP A O4B 4780 O O5B . XYP O . ? 0.6528 0.6329 0.6399 -0.0136 0.0018 0.0017 714 XYP A O5B 4781 C C2 . BGC P . ? 0.3410 0.3657 0.3163 -0.0110 -0.0077 0.0099 715 BGC A C2 4782 C C3 . BGC P . ? 0.3245 0.3498 0.3042 -0.0100 0.0005 0.0100 715 BGC A C3 4783 C C4 . BGC P . ? 0.3516 0.3708 0.3260 -0.0084 -0.0057 0.0042 715 BGC A C4 4784 C C5 . BGC P . ? 0.3655 0.3916 0.3514 -0.0193 -0.0003 0.0098 715 BGC A C5 4785 C C6 . BGC P . ? 0.3665 0.3828 0.3594 -0.0087 -0.0006 0.0072 715 BGC A C6 4786 C C1 . BGC P . ? 0.3862 0.4061 0.3584 -0.0109 -0.0013 0.0117 715 BGC A C1 4787 O O1 . BGC P . ? 0.4043 0.4114 0.3713 -0.0054 -0.0018 -0.0060 715 BGC A O1 4788 O O2 . BGC P . ? 0.3197 0.3523 0.2848 0.0124 0.0108 0.0058 715 BGC A O2 4789 O O3 . BGC P . ? 0.2618 0.3350 0.2838 0.0134 -0.0208 0.0234 715 BGC A O3 4790 O O4 . BGC P . ? 0.3168 0.3555 0.3004 0.0000 -0.0018 -0.0045 715 BGC A O4 4791 O O5 . BGC P . ? 0.3952 0.4311 0.3496 -0.0104 -0.0084 0.0043 715 BGC A O5 4792 O O6 . BGC P . ? 0.3601 0.3731 0.3631 -0.0177 -0.0026 0.0226 715 BGC A O6 4793 C C2 . 3DO Q . ? 0.5332 0.5346 0.5449 0.0027 0.0016 0.0025 716 3DO A C2 4794 C C3 . 3DO Q . ? 0.5174 0.5105 0.5121 -0.0033 0.0012 0.0081 716 3DO A C3 4795 C C4 . 3DO Q . ? 0.5299 0.5085 0.4945 0.0092 0.0004 -0.0035 716 3DO A C4 4796 C C5 . 3DO Q . ? 0.5511 0.5785 0.5571 -0.0108 0.0059 -0.0221 716 3DO A C5 4797 C C6 . 3DO Q . ? 0.4117 0.4147 0.5370 -0.0853 -0.0012 0.0527 716 3DO A C6 4798 O O1 . 3DO Q . ? 0.5940 0.5770 0.5885 0.0000 -0.0007 0.0041 716 3DO A O1 4799 O O6 . 3DO Q . ? 0.6847 0.7050 0.5794 0.1093 -0.0337 -0.0263 716 3DO A O6 4800 O O5 . 3DO Q . ? 0.5709 0.5583 0.5581 -0.0093 -0.0015 0.0073 716 3DO A O5 4801 O O4 . 3DO Q . ? 0.4065 0.4076 0.3777 0.0159 0.0012 0.0090 716 3DO A O4 4802 O O2 . 3DO Q . ? 0.4627 0.4866 0.4610 -0.0055 -0.0019 0.0029 716 3DO A O2 4803 C C1 . 3DO Q . ? 0.5532 0.5517 0.5339 0.0011 -0.0026 -0.0018 716 3DO A C1 4804 C C1 . GOL R . ? 0.6915 0.7043 0.7935 -0.1237 0.0393 0.0511 717 GOL A C1 4805 O O1 . GOL R . ? 0.9488 0.9601 0.7926 0.1190 -0.0536 -0.0477 717 GOL A O1 4806 C C2 . GOL R . ? 0.9257 0.9621 0.9466 -0.0527 0.0066 0.0323 717 GOL A C2 4807 O O2 . GOL R . ? 0.8294 0.7659 0.7202 -0.0152 -0.0244 -0.0604 717 GOL A O2 4808 C C3 . GOL R . ? 0.7089 0.7265 0.7158 0.1250 -0.0418 0.0633 717 GOL A C3 4809 O O3 . GOL R . ? 0.8760 0.9645 0.9739 -0.0781 0.0916 -0.1238 717 GOL A O3 4810 C C1 . GOL S . ? 0.6731 0.6561 0.5926 0.0022 0.0842 0.0441 718 GOL A C1 4811 O O1 . GOL S . ? 0.7373 0.7759 0.8660 0.0268 -0.0442 -0.0546 718 GOL A O1 4812 C C2 . GOL S . ? 0.8329 0.7575 0.7958 0.0001 0.0139 0.0383 718 GOL A C2 4813 O O2 . GOL S . ? 0.6258 0.7019 0.7029 -0.0288 0.0132 0.0134 718 GOL A O2 4814 C C3 . GOL S . ? 0.6950 0.5935 0.5741 0.0187 -0.0502 -0.0753 718 GOL A C3 4815 O O3 . GOL S . ? 0.6719 0.8412 0.7926 -0.0332 0.0055 0.0981 718 GOL A O3 4816 C C1 . GOL T . ? 0.7269 0.7296 0.6102 0.0400 -0.0448 0.0942 719 GOL A C1 4817 O O1 . GOL T . ? 0.7277 0.8142 0.8593 -0.0395 0.0425 -0.0824 719 GOL A O1 4818 C C2 . GOL T . ? 0.7216 0.6641 0.6911 -0.0113 0.0103 0.0098 719 GOL A C2 4819 O O2 . GOL T . ? 0.7237 0.7431 0.7542 0.0076 0.0137 0.0002 719 GOL A O2 4820 C C3 . GOL T . ? 0.7328 0.6506 0.8419 -0.0070 -0.0155 -0.0595 719 GOL A C3 4821 O O3 . GOL T . ? 0.7209 0.8469 0.7186 0.0236 0.0074 0.0369 719 GOL A O3 4822 S S . SO4 U . ? 0.7043 0.7247 0.7108 0.0117 -0.0021 -0.0018 720 SO4 A S 4823 O O1 . SO4 U . ? 0.6931 0.7150 0.7058 0.0062 -0.0040 -0.0055 720 SO4 A O1 4824 O O2 . SO4 U . ? 0.6713 0.7014 0.6939 0.0126 -0.0003 -0.0037 720 SO4 A O2 4825 O O3 . SO4 U . ? 0.6643 0.6889 0.6821 0.0054 -0.0011 0.0014 720 SO4 A O3 4826 O O4 . SO4 U . ? 0.6918 0.7041 0.7027 0.0052 -0.0005 -0.0003 720 SO4 A O4 4827 O O . HOH V . ? 0.2184 0.2734 0.2048 0.0076 0.0300 0.0167 801 HOH A O 4828 O O . HOH V . ? 0.1774 0.2972 0.1860 0.0016 0.0177 -0.0071 802 HOH A O 4829 O O . HOH V . ? 0.2168 0.2195 0.1917 -0.0033 0.0014 -0.0002 803 HOH A O 4830 O O . HOH V . ? 0.2141 0.2128 0.2168 0.0200 0.0095 0.0350 804 HOH A O 4831 O O . HOH V . ? 0.2172 0.2296 0.1752 0.0000 0.0238 -0.0054 805 HOH A O 4832 O O . HOH V . ? 0.2260 0.2230 0.1728 0.0249 0.0103 0.0151 806 HOH A O 4833 O O . HOH V . ? 0.1895 0.2910 0.2158 -0.0203 0.0364 0.0037 807 HOH A O 4834 O O . HOH V . ? 0.2952 0.2720 0.2237 0.0327 -0.0116 0.0189 808 HOH A O 4835 O O . HOH V . ? 0.2685 0.3076 0.2624 0.0360 -0.0190 -0.0246 809 HOH A O 4836 O O . HOH V . ? 0.2388 0.2763 0.1951 0.0378 0.0189 0.0331 810 HOH A O 4837 O O . HOH V . ? 0.2272 0.3393 0.2530 -0.0427 -0.0093 0.0139 811 HOH A O 4838 O O . HOH V . ? 0.5098 0.4829 0.5214 -0.0034 -0.0295 -0.0285 812 HOH A O 4839 O O . HOH V . ? 0.3072 0.3056 0.2967 -0.0059 0.0226 -0.0048 813 HOH A O 4840 O O . HOH V . ? 0.2077 0.2479 0.1909 0.0019 -0.0034 -0.0072 814 HOH A O 4841 O O . HOH V . ? 0.2408 0.3191 0.2128 -0.0156 0.0134 -0.0096 815 HOH A O 4842 O O . HOH V . ? 0.4215 0.4936 0.4957 -0.0072 0.0093 -0.0083 816 HOH A O 4843 O O . HOH V . ? 0.2663 0.3521 0.2456 0.0180 0.0297 -0.0059 817 HOH A O 4844 O O . HOH V . ? 0.2274 0.2124 0.1872 0.0248 0.0094 0.0034 818 HOH A O 4845 O O . HOH V . ? 0.2572 0.3911 0.2257 0.0186 -0.0100 -0.0042 819 HOH A O 4846 O O . HOH V . ? 0.2590 0.2508 0.2294 0.0143 0.0000 0.0172 820 HOH A O 4847 O O . HOH V . ? 0.2736 0.2922 0.2258 0.0483 0.0054 0.0220 821 HOH A O 4848 O O . HOH V . ? 0.1936 0.2393 0.1716 0.0245 0.0119 0.0245 822 HOH A O 4849 O O . HOH V . ? 0.3124 0.3812 0.3541 0.0273 -0.0001 0.0241 823 HOH A O 4850 O O . HOH V . ? 0.3350 0.3599 0.3164 -0.0272 0.0429 -0.0361 824 HOH A O 4851 O O . HOH V . ? 0.2587 0.3313 0.2198 -0.0042 0.0433 -0.0237 825 HOH A O 4852 O O . HOH V . ? 0.2909 0.2997 0.3253 -0.0089 0.0200 -0.0254 826 HOH A O 4853 O O . HOH V . ? 0.2672 0.2720 0.2187 -0.0101 0.0419 0.0222 827 HOH A O 4854 O O . HOH V . ? 0.2845 0.2686 0.2552 0.0393 -0.0316 0.0480 828 HOH A O 4855 O O . HOH V . ? 0.2563 0.3094 0.2583 0.0203 -0.0214 -0.0155 829 HOH A O 4856 O O . HOH V . ? 0.2439 0.2836 0.1773 0.0331 -0.0172 0.0150 830 HOH A O 4857 O O . HOH V . ? 0.3516 0.4493 0.3123 -0.0197 0.0148 -0.0196 831 HOH A O 4858 O O . HOH V . ? 0.3404 0.3348 0.2530 -0.0279 0.0310 0.0476 832 HOH A O 4859 O O . HOH V . ? 0.3209 0.2305 0.2093 0.0277 0.0117 0.0368 833 HOH A O 4860 O O . HOH V . ? 0.3149 0.3026 0.2310 -0.0037 0.0158 -0.0063 834 HOH A O 4861 O O . HOH V . ? 0.2358 0.2773 0.2303 0.0250 -0.0334 -0.0255 835 HOH A O 4862 O O . HOH V . ? 0.2434 0.3514 0.2637 -0.0303 -0.0260 0.0021 836 HOH A O 4863 O O . HOH V . ? 0.3189 0.3689 0.2390 0.0213 0.0035 0.0227 837 HOH A O 4864 O O . HOH V . ? 0.3120 0.4685 0.3657 0.0050 -0.0070 -0.0085 838 HOH A O 4865 O O . HOH V . ? 0.4257 0.4494 0.3281 -0.0165 -0.0316 -0.0005 839 HOH A O 4866 O O . HOH V . ? 0.2744 0.3341 0.2614 -0.0073 -0.0091 0.0148 840 HOH A O 4867 O O . HOH V . ? 0.4770 0.4975 0.4645 -0.0027 0.0073 -0.0082 841 HOH A O 4868 O O . HOH V . ? 0.3889 0.3611 0.4096 0.0026 0.0532 0.0159 842 HOH A O 4869 O O . HOH V . ? 0.3103 0.3264 0.2420 0.0098 0.0238 0.0068 843 HOH A O 4870 O O . HOH V . ? 0.3658 0.4001 0.2356 -0.0018 -0.0223 -0.0231 844 HOH A O 4871 O O . HOH V . ? 0.6315 0.6647 0.6161 -0.0072 -0.0019 -0.0134 845 HOH A O 4872 O O . HOH V . ? 0.3266 0.3576 0.2654 0.0141 0.0145 0.0402 846 HOH A O 4873 O O . HOH V . ? 0.7206 0.7408 0.7239 -0.0045 0.0045 0.0037 847 HOH A O 4874 O O . HOH V . ? 0.5711 0.5487 0.5586 -0.0049 -0.0119 -0.0060 848 HOH A O 4875 O O . HOH V . ? 0.3391 0.3748 0.2777 -0.0206 0.0073 -0.0155 849 HOH A O 4876 O O . HOH V . ? 0.5005 0.4245 0.3445 -0.0081 0.0039 -0.0262 850 HOH A O 4877 O O . HOH V . ? 0.6483 0.6685 0.6909 0.0011 -0.0025 -0.0052 851 HOH A O 4878 O O . HOH V . ? 0.3590 0.3029 0.2762 0.0432 0.0384 0.0305 852 HOH A O 4879 O O . HOH V . ? 0.4617 0.5369 0.4586 0.0286 0.0076 0.0047 853 HOH A O 4880 O O . HOH V . ? 0.3586 0.3607 0.3189 -0.0155 0.0404 -0.0112 854 HOH A O 4881 O O . HOH V . ? 0.4528 0.4892 0.4657 -0.0049 -0.0023 -0.0149 855 HOH A O 4882 O O . HOH V . ? 0.2678 0.2599 0.2827 0.0382 0.0097 0.0311 856 HOH A O 4883 O O . HOH V . ? 0.6302 0.6439 0.6182 -0.0088 -0.0060 -0.0097 857 HOH A O 4884 O O . HOH V . ? 0.4492 0.4488 0.4084 -0.0135 0.0102 -0.0237 858 HOH A O 4885 O O . HOH V . ? 0.5422 0.5092 0.5099 -0.0085 -0.0017 0.0005 859 HOH A O 4886 O O . HOH V . ? 0.3846 0.4153 0.3406 0.0298 0.0291 -0.0128 860 HOH A O 4887 O O . HOH V . ? 0.2762 0.3583 0.3222 0.0357 0.0102 -0.0169 861 HOH A O 4888 O O . HOH V . ? 0.3160 0.3549 0.2847 0.0419 -0.0111 0.0162 862 HOH A O 4889 O O . HOH V . ? 0.4309 0.4463 0.4506 0.0083 0.0103 -0.0200 863 HOH A O 4890 O O . HOH V . ? 0.3299 0.4200 0.2806 -0.0361 -0.0110 0.0341 864 HOH A O 4891 O O . HOH V . ? 0.4467 0.4855 0.5190 0.0202 -0.0269 -0.0070 865 HOH A O 4892 O O . HOH V . ? 0.5191 0.5333 0.4868 -0.0057 0.0053 0.0050 866 HOH A O 4893 O O . HOH V . ? 0.4754 0.4525 0.4156 -0.0184 0.0406 -0.0263 867 HOH A O 4894 O O . HOH V . ? 0.3388 0.3403 0.2707 -0.0049 0.0444 -0.0060 868 HOH A O 4895 O O . HOH V . ? 0.2905 0.4502 0.3107 0.0178 0.0593 0.0066 869 HOH A O 4896 O O . HOH V . ? 0.3594 0.3381 0.2852 0.0054 -0.0230 0.0564 870 HOH A O 4897 O O . HOH V . ? 0.3370 0.3907 0.2454 -0.0046 0.0226 0.0327 871 HOH A O 4898 O O . HOH V . ? 0.4020 0.4133 0.3049 0.0249 -0.0073 0.0371 872 HOH A O 4899 O O . HOH V . ? 0.4305 0.4462 0.4200 0.0123 0.0170 0.0095 873 HOH A O 4900 O O . HOH V . ? 0.3150 0.4184 0.2778 0.0130 -0.0538 -0.0057 874 HOH A O 4901 O O . HOH V . ? 0.3459 0.4094 0.3375 0.0094 0.0273 -0.0204 875 HOH A O 4902 O O . HOH V . ? 0.4674 0.4816 0.4258 -0.0233 -0.0065 -0.0148 876 HOH A O 4903 O O . HOH V . ? 0.2948 0.3836 0.2466 -0.0025 -0.0026 0.0085 877 HOH A O 4904 O O . HOH V . ? 0.4023 0.3840 0.2736 0.0022 -0.0326 0.0289 878 HOH A O 4905 O O . HOH V . ? 0.2243 0.4082 0.2829 -0.0127 0.0320 -0.0066 879 HOH A O 4906 O O . HOH V . ? 0.3470 0.3880 0.3622 -0.0135 -0.0177 0.0010 880 HOH A O 4907 O O . HOH V . ? 0.3205 0.3356 0.2742 -0.0045 0.0160 0.0090 881 HOH A O 4908 O O . HOH V . ? 0.3889 0.4456 0.3654 0.0333 0.0008 0.0218 882 HOH A O 4909 O O . HOH V . ? 0.4275 0.4065 0.2742 0.0187 0.0299 -0.0032 883 HOH A O 4910 O O . HOH V . ? 0.3624 0.3644 0.3898 0.0176 0.0417 -0.0088 884 HOH A O 4911 O O . HOH V . ? 0.3948 0.4324 0.3377 0.0212 0.0008 0.0073 885 HOH A O 4912 O O . HOH V . ? 0.4757 0.4840 0.4099 0.0083 0.0120 0.0002 886 HOH A O 4913 O O . HOH V . ? 0.3445 0.4116 0.3974 0.0022 -0.0371 -0.0016 887 HOH A O 4914 O O . HOH V . ? 0.4905 0.4490 0.4781 0.0016 0.0001 -0.0150 888 HOH A O 4915 O O . HOH V . ? 0.5413 0.5727 0.4677 -0.0073 0.0058 0.0110 889 HOH A O 4916 O O . HOH V . ? 0.4815 0.4729 0.4340 0.0094 -0.0109 -0.0034 890 HOH A O 4917 O O . HOH V . ? 0.4591 0.4443 0.4518 0.0190 -0.0150 0.0311 891 HOH A O 4918 O O . HOH V . ? 0.3673 0.3682 0.3758 0.0068 0.0013 0.0565 892 HOH A O 4919 O O . HOH V . ? 0.4559 0.3880 0.4232 -0.0143 -0.0042 0.0306 893 HOH A O 4920 O O . HOH V . ? 0.3735 0.4470 0.3670 0.0232 0.0063 0.0165 894 HOH A O 4921 O O . HOH V . ? 0.7235 0.7349 0.7150 -0.0041 -0.0002 -0.0039 895 HOH A O 4922 O O . HOH V . ? 0.6624 0.6837 0.6475 0.0035 0.0056 0.0000 896 HOH A O 4923 O O . HOH V . ? 0.3076 0.4264 0.2893 -0.0041 0.0024 -0.0055 897 HOH A O 4924 O O . HOH V . ? 0.5308 0.5224 0.5301 -0.0079 -0.0230 -0.0165 898 HOH A O 4925 O O . HOH V . ? 0.4615 0.4212 0.4006 0.0139 -0.0185 -0.0169 899 HOH A O 4926 O O . HOH V . ? 0.3700 0.4555 0.4176 -0.0186 0.0280 0.0156 900 HOH A O 4927 O O . HOH V . ? 0.4112 0.3768 0.4055 -0.0259 0.0041 0.0110 901 HOH A O 4928 O O . HOH V . ? 0.5460 0.5725 0.5837 -0.0024 -0.0014 -0.0031 902 HOH A O 4929 O O . HOH V . ? 0.5378 0.5061 0.4115 -0.0259 -0.0328 -0.0113 903 HOH A O 4930 O O . HOH V . ? 0.2181 0.2265 0.1924 0.0190 0.0083 0.0134 904 HOH A O 4931 O O . HOH V . ? 0.7115 0.7196 0.7085 -0.0039 0.0010 0.0071 905 HOH A O 4932 O O . HOH V . ? 0.7769 0.7670 0.7795 -0.0045 0.0017 -0.0035 906 HOH A O 4933 O O . HOH V . ? 0.4428 0.4655 0.4006 0.0071 0.0031 0.0261 907 HOH A O 4934 O O . HOH V . ? 0.3753 0.3809 0.4014 0.0088 0.0163 -0.0183 908 HOH A O 4935 O O . HOH V . ? 0.3263 0.3297 0.3696 0.0211 -0.0017 0.0044 909 HOH A O 4936 O O . HOH V . ? 0.7031 0.7093 0.7059 0.0000 -0.0030 0.0003 910 HOH A O 4937 O O . HOH V . ? 0.6446 0.6446 0.6782 -0.0020 -0.0011 0.0089 911 HOH A O 4938 O O . HOH V . ? 0.6401 0.6103 0.6138 -0.0016 0.0062 -0.0126 912 HOH A O 4939 O O . HOH V . ? 0.2065 0.2534 0.2093 0.0216 0.0145 0.0152 913 HOH A O 4940 O O . HOH V . ? 0.4869 0.5363 0.4716 0.0081 -0.0154 -0.0240 914 HOH A O 4941 O O . HOH V . ? 0.4795 0.5379 0.4122 0.0150 -0.0039 0.0144 915 HOH A O 4942 O O . HOH V . ? 0.6079 0.6107 0.6119 -0.0020 0.0148 -0.0078 916 HOH A O 4943 O O . HOH V . ? 0.6230 0.6749 0.6741 -0.0118 0.0012 -0.0063 917 HOH A O 4944 O O . HOH V . ? 0.6588 0.6518 0.6556 0.0000 0.0042 0.0152 918 HOH A O 4945 O O . HOH V . ? 0.8371 0.8347 0.8473 0.0084 -0.0017 0.0031 919 HOH A O 4946 O O . HOH V . ? 0.9874 0.9811 0.9851 -0.0014 0.0007 -0.0002 920 HOH A O 4947 O O . HOH V . ? 0.5030 0.5539 0.4921 0.0048 -0.0053 -0.0065 921 HOH A O 4948 O O . HOH V . ? 0.4370 0.5275 0.4363 0.0039 0.0052 0.0036 922 HOH A O 4949 O O . HOH V . ? 0.5197 0.5534 0.4934 0.0123 0.0105 0.0178 923 HOH A O 4950 O O . HOH V . ? 0.6504 0.6596 0.6467 0.0084 0.0105 0.0097 924 HOH A O 4951 O O . HOH V . ? 0.2342 0.2518 0.2265 0.0160 0.0075 -0.0026 925 HOH A O 4952 O O . HOH V . ? 0.6259 0.6745 0.6395 -0.0005 -0.0105 0.0061 926 HOH A O 4953 O O . HOH V . ? 0.7653 0.7614 0.7655 -0.0012 0.0005 -0.0052 927 HOH A O 4954 O O . HOH V . ? 0.4204 0.4406 0.3378 0.0117 0.0326 -0.0200 928 HOH A O 4955 O O . HOH V . ? 0.5431 0.5335 0.5747 -0.0198 0.0051 -0.0050 929 HOH A O 4956 O O . HOH V . ? 0.2954 0.3636 0.3253 0.0001 0.0168 -0.0144 930 HOH A O 4957 O O . HOH V . ? 0.4341 0.4577 0.4024 0.0416 -0.0255 0.0281 931 HOH A O 4958 O O . HOH V . ? 0.4181 0.4839 0.4129 0.0054 0.0130 -0.0150 932 HOH A O 4959 O O . HOH V . ? 0.4143 0.4364 0.4364 -0.0079 0.0232 -0.0178 933 HOH A O 4960 O O . HOH V . ? 0.3800 0.3805 0.2621 0.0107 0.0193 0.0024 934 HOH A O 4961 O O . HOH V . ? 0.3631 0.4132 0.3926 -0.0078 -0.0254 -0.0129 935 HOH A O 4962 O O . HOH V . ? 0.4420 0.4504 0.3730 0.0105 0.0418 0.0042 936 HOH A O 4963 O O . HOH V . ? 0.4870 0.4208 0.4591 -0.0080 -0.0246 -0.0230 937 HOH A O 4964 O O . HOH V . ? 0.8254 0.8120 0.8233 0.0051 -0.0008 0.0067 938 HOH A O 4965 O O . HOH V . ? 0.7270 0.7312 0.7455 0.0001 -0.0008 -0.0093 939 HOH A O 4966 O O . HOH V . ? 0.5585 0.6099 0.6135 0.0094 0.0000 0.0017 940 HOH A O 4967 O O . HOH V . ? 0.4442 0.4381 0.4701 0.0037 0.0070 -0.0122 941 HOH A O 4968 O O . HOH V . ? 1.3676 1.3628 1.3676 0.0004 -0.0010 -0.0001 942 HOH A O 4969 O O . HOH V . ? 0.7621 0.7477 0.7721 0.0052 -0.0006 -0.0005 943 HOH A O 4970 O O . HOH V . ? 0.5216 0.5469 0.5412 -0.0072 -0.0030 0.0086 944 HOH A O 4971 O O . HOH V . ? 0.4611 0.3933 0.4074 0.0100 0.0164 0.0239 945 HOH A O 4972 O O . HOH V . ? 0.4880 0.5202 0.4851 0.0234 -0.0077 0.0118 946 HOH A O 4973 O O . HOH V . ? 0.3278 0.3548 0.3572 -0.0047 0.0002 0.0117 947 HOH A O 4974 O O . HOH V . ? 0.6243 0.6238 0.6429 0.0092 0.0101 -0.0059 948 HOH A O 4975 O O . HOH V . ? 0.9528 0.9529 0.9572 0.0008 0.0020 -0.0039 949 HOH A O 4976 O O . HOH V . ? 0.2529 0.3195 0.2420 -0.0088 0.0267 -0.0349 950 HOH A O 4977 O O . HOH V . ? 0.3967 0.4545 0.4298 0.0105 0.0040 -0.0769 951 HOH A O 4978 O O . HOH V . ? 0.3733 0.3798 0.2950 0.0139 0.0130 -0.0156 952 HOH A O 4979 O O . HOH V . ? 0.5342 0.5841 0.6063 0.0085 -0.0032 -0.0063 953 HOH A O 4980 O O . HOH V . ? 0.2496 0.2833 0.1936 0.0118 0.0480 0.0115 954 HOH A O 4981 O O . HOH V . ? 0.6290 0.6019 0.5878 -0.0035 0.0007 -0.0126 955 HOH A O 4982 O O . HOH V . ? 0.7875 0.7898 0.7905 0.0080 -0.0014 -0.0015 956 HOH A O 4983 O O . HOH V . ? 0.6430 0.6380 0.6312 -0.0047 0.0265 0.0056 957 HOH A O 4984 O O . HOH V . ? 0.4354 0.4842 0.4470 0.0162 0.0186 0.0149 958 HOH A O 4985 O O . HOH V . ? 0.5578 0.5239 0.5207 0.0081 -0.0073 -0.0047 959 HOH A O 4986 O O . HOH V . ? 0.3109 0.4284 0.3152 0.0057 -0.0110 0.0041 960 HOH A O 4987 O O . HOH V . ? 0.3345 0.3928 0.3014 0.0226 0.0154 -0.0236 961 HOH A O 4988 O O . HOH V . ? 0.7823 0.7775 0.7780 -0.0054 0.0015 0.0027 962 HOH A O 4989 O O . HOH V . ? 0.7137 0.6918 0.6951 0.0023 0.0019 -0.0071 963 HOH A O 4990 O O . HOH V . ? 0.2080 0.2512 0.1707 0.0127 0.0014 0.0147 964 HOH A O 4991 O O . HOH V . ? 0.3779 0.4626 0.3933 0.0080 -0.0264 -0.0124 965 HOH A O 4992 O O . HOH V . ? 0.2719 0.3154 0.2991 -0.0034 0.0048 0.0154 966 HOH A O 4993 O O . HOH V . ? 0.5019 0.5311 0.4074 -0.0105 -0.0037 0.0049 967 HOH A O 4994 O O . HOH V . ? 0.2615 0.3139 0.2908 0.0157 0.0059 -0.0202 968 HOH A O 4995 O O . HOH V . ? 0.2261 0.2793 0.1725 -0.0017 -0.0185 0.0143 969 HOH A O 4996 O O . HOH V . ? 0.1934 0.2337 0.1658 0.0302 0.0283 -0.0052 970 HOH A O 4997 O O . HOH V . ? 0.2231 0.2147 0.1913 0.0056 -0.0016 0.0197 971 HOH A O 4998 O O . HOH V . ? 0.2437 0.3144 0.2006 0.0212 -0.0063 0.0309 972 HOH A O 4999 O O . HOH V . ? 0.2064 0.3016 0.2186 -0.0027 0.0230 -0.0051 973 HOH A O 5000 O O . HOH V . ? 0.2596 0.1988 0.1865 0.0004 0.0071 0.0220 974 HOH A O 5001 O O . HOH V . ? 0.2143 0.2770 0.1774 0.0028 0.0077 0.0192 975 HOH A O 5002 O O . HOH V . ? 0.2169 0.2346 0.1877 0.0085 0.0311 0.0313 976 HOH A O 5003 O O . HOH V . ? 0.2367 0.3362 0.2273 0.0106 0.0010 0.0147 977 HOH A O 5004 O O . HOH V . ? 0.3048 0.3062 0.2229 0.0025 0.0235 0.0300 978 HOH A O 5005 O O . HOH V . ? 0.2916 0.2330 0.1899 0.0319 0.0064 0.0438 979 HOH A O 5006 O O . HOH V . ? 0.2286 0.2893 0.1849 -0.0269 0.0149 -0.0111 980 HOH A O 5007 O O . HOH V . ? 0.2640 0.3145 0.1927 -0.0038 0.0296 -0.0273 981 HOH A O 5008 O O . HOH V . ? 0.2284 0.3364 0.2235 0.0000 0.0181 0.0094 982 HOH A O 5009 O O . HOH V . ? 0.2964 0.2791 0.2252 -0.0049 0.0120 0.0225 983 HOH A O 5010 O O . HOH V . ? 0.2261 0.2051 0.1985 0.0106 -0.0009 0.0522 984 HOH A O 5011 O O . HOH V . ? 0.3117 0.2783 0.2136 -0.0169 0.0055 0.0091 985 HOH A O 5012 O O . HOH V . ? 0.2836 0.3267 0.2848 -0.0061 0.0187 -0.0084 986 HOH A O 5013 O O . HOH V . ? 0.3154 0.2975 0.2620 -0.0241 -0.0062 0.0199 987 HOH A O 5014 O O . HOH V . ? 0.2332 0.2533 0.2819 -0.0187 0.0251 0.0389 988 HOH A O 5015 O O . HOH V . ? 0.3000 0.3649 0.3038 -0.0089 0.0002 0.0116 989 HOH A O 5016 O O . HOH V . ? 0.2472 0.2854 0.2525 0.0212 -0.0109 -0.0361 990 HOH A O 5017 O O . HOH V . ? 0.2718 0.3511 0.2408 0.0362 -0.0025 -0.0055 991 HOH A O 5018 O O . HOH V . ? 0.2177 0.3094 0.2038 -0.0087 -0.0101 -0.0076 992 HOH A O 5019 O O . HOH V . ? 0.2461 0.2460 0.1939 0.0128 0.0128 0.0065 993 HOH A O 5020 O O . HOH V . ? 0.3264 0.2858 0.2850 0.0037 0.0044 -0.0279 994 HOH A O 5021 O O . HOH V . ? 0.2273 0.3080 0.2747 0.0050 -0.0118 0.0474 995 HOH A O 5022 O O . HOH V . ? 0.2757 0.3058 0.2955 -0.0279 -0.0390 -0.0080 996 HOH A O 5023 O O . HOH V . ? 0.3114 0.3494 0.2474 0.0038 0.0316 0.0222 997 HOH A O 5024 O O . HOH V . ? 0.2509 0.3736 0.2522 0.0264 -0.0252 0.0159 998 HOH A O 5025 O O . HOH V . ? 0.2896 0.3534 0.2613 -0.0045 0.0125 -0.0168 999 HOH A O 5026 O O . HOH V . ? 0.3093 0.3085 0.2545 0.0194 0.0100 -0.0245 1000 HOH A O 5027 O O . HOH V . ? 0.3027 0.3033 0.2624 0.0384 0.0141 0.0221 1001 HOH A O 5028 O O . HOH V . ? 0.3013 0.3034 0.2514 -0.0035 0.0043 0.0312 1002 HOH A O 5029 O O . HOH V . ? 0.2651 0.3112 0.2505 -0.0160 -0.0159 -0.0012 1003 HOH A O 5030 O O . HOH V . ? 0.3018 0.3424 0.2811 0.0393 0.0061 0.0335 1004 HOH A O 5031 O O . HOH V . ? 0.2783 0.3457 0.2937 -0.0213 -0.0185 -0.0027 1005 HOH A O 5032 O O . HOH V . ? 0.2886 0.3193 0.2474 -0.0329 -0.0227 -0.0449 1006 HOH A O 5033 O O . HOH V . ? 0.2046 0.3098 0.2100 0.0045 0.0027 0.0046 1007 HOH A O 5034 O O . HOH V . ? 0.3121 0.3292 0.2167 0.0109 -0.0441 0.0285 1008 HOH A O 5035 O O . HOH V . ? 0.3170 0.3135 0.2523 0.0142 0.0067 0.0112 1009 HOH A O 5036 O O . HOH V . ? 0.3218 0.3034 0.2216 -0.0049 0.0181 0.0034 1010 HOH A O 5037 O O . HOH V . ? 0.3812 0.3920 0.4032 -0.0023 0.0057 -0.0172 1011 HOH A O 5038 O O . HOH V . ? 0.3065 0.3805 0.3067 0.0369 -0.0201 -0.0012 1012 HOH A O 5039 O O . HOH V . ? 0.2401 0.3794 0.2391 0.0144 -0.0171 -0.0055 1013 HOH A O 5040 O O . HOH V . ? 0.3178 0.4034 0.4279 -0.0113 0.0055 -0.0207 1014 HOH A O 5041 O O . HOH V . ? 0.3265 0.3986 0.2650 0.0043 -0.0201 0.0043 1015 HOH A O 5042 O O . HOH V . ? 0.2991 0.3996 0.2666 0.0195 -0.0110 0.0175 1016 HOH A O 5043 O O . HOH V . ? 0.2856 0.3596 0.3152 0.0252 -0.0085 0.0060 1017 HOH A O 5044 O O . HOH V . ? 0.3364 0.3118 0.2876 0.0192 0.0262 0.0120 1018 HOH A O 5045 O O . HOH V . ? 0.3536 0.2899 0.3097 0.0029 0.0051 0.0212 1019 HOH A O 5046 O O . HOH V . ? 0.2796 0.3047 0.2905 0.0030 -0.0036 -0.0131 1020 HOH A O 5047 O O . HOH V . ? 0.2995 0.3838 0.2782 0.0256 -0.0143 0.0071 1021 HOH A O 5048 O O . HOH V . ? 0.2676 0.3460 0.2927 0.0222 -0.0314 -0.0001 1022 HOH A O 5049 O O . HOH V . ? 0.3177 0.3761 0.3327 0.0267 0.0087 0.0415 1023 HOH A O 5050 O O . HOH V . ? 0.3938 0.4149 0.3329 -0.0084 0.0015 0.0066 1024 HOH A O 5051 O O . HOH V . ? 0.2960 0.3721 0.3124 0.0034 0.0071 -0.0035 1025 HOH A O 5052 O O . HOH V . ? 0.3682 0.3416 0.3104 0.0369 0.0015 -0.0322 1026 HOH A O 5053 O O . HOH V . ? 0.3321 0.3805 0.2492 -0.0093 0.0133 -0.0259 1027 HOH A O 5054 O O . HOH V . ? 0.3195 0.3564 0.3444 -0.0097 -0.0039 -0.0121 1028 HOH A O 5055 O O . HOH V . ? 0.2938 0.3179 0.3054 -0.0001 -0.0021 -0.0088 1029 HOH A O 5056 O O . HOH V . ? 0.4256 0.4059 0.4128 0.0111 0.0431 0.0115 1030 HOH A O 5057 O O . HOH V . ? 0.3932 0.3383 0.3405 -0.0117 0.0500 -0.0124 1031 HOH A O 5058 O O . HOH V . ? 0.3285 0.3265 0.2487 0.0402 0.0263 0.0338 1032 HOH A O 5059 O O . HOH V . ? 0.2768 0.3422 0.3314 -0.0281 0.0169 -0.0162 1033 HOH A O 5060 O O . HOH V . ? 0.3789 0.3989 0.3701 -0.0250 0.0154 0.0003 1034 HOH A O 5061 O O . HOH V . ? 0.2888 0.3547 0.2432 0.0310 -0.0042 0.0161 1035 HOH A O 5062 O O . HOH V . ? 0.3345 0.3848 0.2734 0.0134 -0.0044 0.0063 1036 HOH A O 5063 O O . HOH V . ? 0.2226 0.3487 0.3408 -0.0089 0.0464 0.0477 1037 HOH A O 5064 O O . HOH V . ? 0.3935 0.3761 0.3636 -0.0288 0.0023 -0.0098 1038 HOH A O 5065 O O . HOH V . ? 0.2965 0.3440 0.3375 -0.0171 0.0036 -0.0095 1039 HOH A O 5066 O O . HOH V . ? 0.3591 0.4279 0.3706 0.0203 -0.0097 0.0315 1040 HOH A O 5067 O O . HOH V . ? 0.2683 0.3444 0.2809 0.0330 0.0324 -0.0157 1041 HOH A O 5068 O O . HOH V . ? 0.3672 0.3693 0.3079 0.0095 0.0555 -0.0176 1042 HOH A O 5069 O O . HOH V . ? 0.3246 0.4215 0.3348 -0.0279 0.0019 0.0174 1043 HOH A O 5070 O O . HOH V . ? 0.3186 0.3339 0.3312 0.0324 0.0498 0.0023 1044 HOH A O 5071 O O . HOH V . ? 0.3842 0.4911 0.3952 -0.0019 -0.0330 -0.0127 1045 HOH A O 5072 O O . HOH V . ? 0.3287 0.3607 0.2823 -0.0113 -0.0056 -0.0124 1046 HOH A O 5073 O O . HOH V . ? 0.3984 0.3776 0.4031 0.0097 -0.0006 0.0185 1047 HOH A O 5074 O O . HOH V . ? 0.2798 0.3313 0.4047 0.0239 0.0364 0.0452 1048 HOH A O 5075 O O . HOH V . ? 0.3632 0.4145 0.3990 -0.0039 -0.0054 0.0289 1049 HOH A O 5076 O O . HOH V . ? 0.3751 0.3588 0.3276 0.0244 0.0477 0.0376 1050 HOH A O 5077 O O . HOH V . ? 0.2821 0.3730 0.2704 0.0331 0.0110 -0.0071 1051 HOH A O 5078 O O . HOH V . ? 0.3718 0.4057 0.4366 0.0310 0.0060 0.0043 1052 HOH A O 5079 O O . HOH V . ? 0.3254 0.4308 0.3616 0.0155 0.0102 0.0160 1053 HOH A O 5080 O O . HOH V . ? 0.4424 0.4887 0.4333 -0.0064 0.0137 -0.0100 1054 HOH A O 5081 O O . HOH V . ? 0.3471 0.4281 0.4651 -0.0278 -0.0153 -0.0045 1055 HOH A O 5082 O O . HOH V . ? 0.7154 0.7007 0.6927 0.0021 -0.0066 -0.0030 1056 HOH A O 5083 O O . HOH V . ? 0.3116 0.3802 0.2868 -0.0231 -0.0509 0.0025 1057 HOH A O 5084 O O . HOH V . ? 0.3810 0.4104 0.3482 0.0036 -0.0475 -0.0081 1058 HOH A O 5085 O O . HOH V . ? 0.3438 0.3651 0.3394 -0.0074 -0.0159 -0.0245 1059 HOH A O 5086 O O . HOH V . ? 0.3285 0.3820 0.2613 0.0114 0.0349 0.0162 1060 HOH A O 5087 O O . HOH V . ? 0.3579 0.2836 0.2816 -0.0056 0.0265 -0.0168 1061 HOH A O 5088 O O . HOH V . ? 0.2913 0.3987 0.3358 -0.0343 -0.0024 -0.0064 1062 HOH A O 5089 O O . HOH V . ? 0.3576 0.3231 0.3626 0.0098 0.0419 0.0360 1063 HOH A O 5090 O O . HOH V . ? 0.3849 0.4410 0.4054 0.0185 0.0000 0.0250 1064 HOH A O 5091 O O . HOH V . ? 0.3790 0.3591 0.3386 0.0190 -0.0049 -0.0039 1065 HOH A O 5092 O O . HOH V . ? 0.2948 0.3580 0.2642 -0.0150 0.0405 -0.0318 1066 HOH A O 5093 O O . HOH V . ? 0.3881 0.4119 0.3971 0.0299 -0.0228 0.0377 1067 HOH A O 5094 O O . HOH V . ? 0.4378 0.3906 0.3711 0.0062 -0.0231 0.0278 1068 HOH A O 5095 O O . HOH V . ? 0.3839 0.4855 0.3595 -0.0073 0.0341 0.0050 1069 HOH A O 5096 O O . HOH V . ? 0.2805 0.3997 0.3141 -0.0129 0.0160 0.0006 1070 HOH A O 5097 O O . HOH V . ? 0.3887 0.3737 0.3235 -0.0093 0.0271 0.0375 1071 HOH A O 5098 O O . HOH V . ? 0.3951 0.3919 0.3928 0.0060 0.0344 0.0080 1072 HOH A O 5099 O O . HOH V . ? 0.4995 0.4787 0.4332 0.0049 0.0136 0.0352 1073 HOH A O 5100 O O . HOH V . ? 0.4787 0.5136 0.4992 -0.0034 0.0114 -0.0035 1074 HOH A O 5101 O O . HOH V . ? 0.3674 0.5045 0.3749 0.0067 0.0052 0.0222 1075 HOH A O 5102 O O . HOH V . ? 0.3875 0.3697 0.4497 0.0129 0.0046 0.0056 1076 HOH A O 5103 O O . HOH V . ? 0.3637 0.3900 0.3892 -0.0351 -0.0092 0.0055 1077 HOH A O 5104 O O . HOH V . ? 0.4044 0.4846 0.3730 0.0144 -0.0260 0.0213 1078 HOH A O 5105 O O . HOH V . ? 0.3901 0.4328 0.4371 0.0119 0.0233 -0.0158 1079 HOH A O 5106 O O . HOH V . ? 0.3589 0.3418 0.3365 0.0407 -0.0066 -0.0016 1080 HOH A O 5107 O O . HOH V . ? 0.4090 0.4209 0.4149 0.0043 0.0250 -0.0031 1081 HOH A O 5108 O O . HOH V . ? 0.3448 0.4400 0.4115 0.0270 -0.0048 0.0302 1082 HOH A O 5109 O O . HOH V . ? 0.3519 0.4043 0.3025 -0.0349 0.0388 0.0140 1083 HOH A O 5110 O O . HOH V . ? 0.2541 0.3807 0.3812 0.0001 0.0324 0.0020 1084 HOH A O 5111 O O . HOH V . ? 0.3231 0.3215 0.3809 0.0096 0.0170 -0.0065 1085 HOH A O 5112 O O . HOH V . ? 0.6090 0.5694 0.6118 0.0038 0.0128 -0.0240 1086 HOH A O 5113 O O . HOH V . ? 0.3409 0.4017 0.3236 0.0044 0.0159 0.0131 1087 HOH A O 5114 O O . HOH V . ? 0.6283 0.6389 0.6186 0.0020 -0.0007 -0.0082 1088 HOH A O 5115 O O . HOH V . ? 0.3312 0.4321 0.3491 -0.0017 0.0036 -0.0206 1089 HOH A O 5116 O O . HOH V . ? 0.5119 0.4653 0.4111 -0.0160 0.0259 -0.0171 1090 HOH A O 5117 O O . HOH V . ? 0.3424 0.3573 0.3296 0.0165 -0.0168 0.0444 1091 HOH A O 5118 O O . HOH V . ? 0.4241 0.3773 0.3628 0.0244 0.0480 0.0246 1092 HOH A O 5119 O O . HOH V . ? 0.4328 0.4336 0.4195 -0.0154 -0.0160 -0.0303 1093 HOH A O 5120 O O . HOH V . ? 0.2938 0.4421 0.2761 0.0292 -0.0316 -0.0325 1094 HOH A O 5121 O O . HOH V . ? 0.4067 0.4090 0.3793 0.0116 0.0247 0.0260 1095 HOH A O 5122 O O . HOH V . ? 0.4204 0.4134 0.3679 0.0079 0.0036 0.0154 1096 HOH A O 5123 O O . HOH V . ? 0.3625 0.4388 0.4339 -0.0178 0.0283 -0.0340 1097 HOH A O 5124 O O . HOH V . ? 0.4220 0.4306 0.4201 -0.0462 0.0045 0.0304 1098 HOH A O 5125 O O . HOH V . ? 0.4557 0.5301 0.4203 -0.0277 0.0232 0.0173 1099 HOH A O 5126 O O . HOH V . ? 0.4532 0.4403 0.4165 -0.0239 0.0039 -0.0033 1100 HOH A O 5127 O O . HOH V . ? 0.2539 0.4021 0.2804 0.0221 0.0093 -0.0013 1101 HOH A O 5128 O O . HOH V . ? 0.3866 0.4689 0.3471 0.0237 -0.0054 0.0237 1102 HOH A O 5129 O O . HOH V . ? 0.4264 0.3859 0.3749 0.0102 0.0007 -0.0153 1103 HOH A O 5130 O O . HOH V . ? 0.3191 0.4246 0.4183 -0.0179 0.0197 -0.0018 1104 HOH A O 5131 O O . HOH V . ? 0.4063 0.3954 0.3956 0.0184 0.0227 0.0110 1105 HOH A O 5132 O O . HOH V . ? 0.3775 0.4484 0.4479 0.0146 0.0112 -0.0343 1106 HOH A O 5133 O O . HOH V . ? 0.4332 0.4129 0.4338 0.0022 -0.0123 0.0212 1107 HOH A O 5134 O O . HOH V . ? 0.4286 0.5195 0.4839 -0.0145 -0.0023 0.0055 1108 HOH A O 5135 O O . HOH V . ? 0.4235 0.4255 0.4119 0.0366 0.0150 0.0042 1109 HOH A O 5136 O O . HOH V . ? 0.4336 0.3923 0.4086 0.0467 0.0055 0.0056 1110 HOH A O 5137 O O . HOH V . ? 0.3245 0.4001 0.3199 -0.0319 -0.0079 -0.0120 1111 HOH A O 5138 O O . HOH V . ? 0.3758 0.3613 0.3469 0.0291 0.0469 0.0166 1112 HOH A O 5139 O O . HOH V . ? 0.4080 0.3894 0.3944 -0.0134 0.0193 0.0374 1113 HOH A O 5140 O O . HOH V . ? 0.4346 0.4413 0.3609 -0.0106 0.0286 -0.0329 1114 HOH A O 5141 O O . HOH V . ? 0.4097 0.4035 0.3707 -0.0306 0.0002 -0.0093 1115 HOH A O 5142 O O . HOH V . ? 0.3701 0.4500 0.4507 0.0077 -0.0068 -0.0024 1116 HOH A O 5143 O O . HOH V . ? 0.4714 0.4017 0.4669 0.0046 -0.0017 -0.0201 1117 HOH A O 5144 O O . HOH V . ? 0.3837 0.4633 0.3576 0.0096 -0.0049 0.0207 1118 HOH A O 5145 O O . HOH V . ? 0.3733 0.3984 0.3933 -0.0182 -0.0118 0.0009 1119 HOH A O 5146 O O . HOH V . ? 0.3758 0.3241 0.3047 -0.0001 0.0123 -0.0117 1120 HOH A O 5147 O O . HOH V . ? 0.3800 0.3522 0.3803 -0.0100 0.0444 0.0031 1121 HOH A O 5148 O O . HOH V . ? 0.4094 0.4835 0.4383 0.0042 0.0258 0.0071 1122 HOH A O 5149 O O . HOH V . ? 0.4031 0.4195 0.3905 0.0180 0.0355 0.0156 1123 HOH A O 5150 O O . HOH V . ? 0.3434 0.4658 0.4004 -0.0016 -0.0305 0.0192 1124 HOH A O 5151 O O . HOH V . ? 0.3743 0.4434 0.4582 -0.0143 0.0062 -0.0096 1125 HOH A O 5152 O O . HOH V . ? 0.4352 0.4569 0.4533 -0.0422 -0.0244 -0.0062 1126 HOH A O 5153 O O . HOH V . ? 0.4263 0.3822 0.3925 0.0074 -0.0263 -0.0426 1127 HOH A O 5154 O O . HOH V . ? 0.4141 0.4126 0.4284 0.0052 0.0145 -0.0013 1128 HOH A O 5155 O O . HOH V . ? 0.6159 0.6346 0.6214 0.0173 0.0144 0.0138 1129 HOH A O 5156 O O . HOH V . ? 0.3565 0.4583 0.3935 -0.0040 -0.0046 -0.0202 1130 HOH A O 5157 O O . HOH V . ? 0.4529 0.4415 0.4617 -0.0086 0.0259 0.0211 1131 HOH A O 5158 O O . HOH V . ? 0.4047 0.3645 0.3501 0.0166 0.0084 0.0430 1132 HOH A O 5159 O O . HOH V . ? 0.3656 0.4139 0.3329 -0.0185 0.0364 0.0220 1133 HOH A O 5160 O O . HOH V . ? 0.3680 0.4806 0.4443 -0.0005 -0.0093 -0.0322 1134 HOH A O 5161 O O . HOH V . ? 0.4467 0.4857 0.4683 -0.0029 0.0135 -0.0109 1135 HOH A O 5162 O O . HOH V . ? 0.4335 0.3836 0.4181 -0.0128 0.0088 0.0144 1136 HOH A O 5163 O O . HOH V . ? 0.4425 0.4080 0.3943 0.0410 0.0175 0.0266 1137 HOH A O 5164 O O . HOH V . ? 0.5104 0.4212 0.4980 -0.0003 0.0071 -0.0021 1138 HOH A O 5165 O O . HOH V . ? 0.3297 0.4521 0.3714 0.0177 -0.0239 0.0136 1139 HOH A O 5166 O O . HOH V . ? 0.4545 0.4444 0.4029 -0.0031 0.0213 0.0048 1140 HOH A O 5167 O O . HOH V . ? 0.4680 0.4609 0.4614 0.0236 0.0055 -0.0108 1141 HOH A O 5168 O O . HOH V . ? 0.4773 0.4610 0.5442 0.0023 0.0318 -0.0231 1142 HOH A O 5169 O O . HOH V . ? 0.4749 0.4774 0.4487 -0.0141 -0.0025 0.0069 1143 HOH A O 5170 O O . HOH V . ? 0.3626 0.4158 0.3472 0.0291 -0.0225 -0.0233 1144 HOH A O 5171 O O . HOH V . ? 0.4271 0.4718 0.4401 0.0190 0.0170 0.0181 1145 HOH A O 5172 O O . HOH V . ? 0.4819 0.4583 0.4314 0.0128 -0.0059 -0.0049 1146 HOH A O 5173 O O . HOH V . ? 0.4694 0.5229 0.4868 0.0273 -0.0369 0.0079 1147 HOH A O 5174 O O . HOH V . ? 0.4336 0.3997 0.4101 -0.0301 0.0045 -0.0005 1148 HOH A O 5175 O O . HOH V . ? 0.4372 0.4602 0.3427 0.0141 -0.0086 0.0150 1149 HOH A O 5176 O O . HOH V . ? 0.6089 0.5554 0.5658 0.0091 0.0236 -0.0081 1150 HOH A O 5177 O O . HOH V . ? 0.4495 0.4835 0.4688 0.0228 -0.0180 -0.0159 1151 HOH A O 5178 O O . HOH V . ? 0.4927 0.4504 0.4971 -0.0208 0.0007 -0.0283 1152 HOH A O 5179 O O . HOH V . ? 0.4163 0.4238 0.3340 0.0171 0.0386 0.0049 1153 HOH A O 5180 O O . HOH V . ? 0.4301 0.4946 0.4555 -0.0058 0.0017 -0.0113 1154 HOH A O 5181 O O . HOH V . ? 0.4064 0.4148 0.3904 -0.0049 0.0235 0.0029 1155 HOH A O 5182 O O . HOH V . ? 0.4354 0.4556 0.4311 -0.0199 0.0372 0.0017 1156 HOH A O 5183 O O . HOH V . ? 0.4914 0.4811 0.5305 -0.0015 0.0304 0.0013 1157 HOH A O 5184 O O . HOH V . ? 0.3508 0.3996 0.3903 -0.0426 0.0323 0.0346 1158 HOH A O 5185 O O . HOH V . ? 0.4516 0.4573 0.4173 0.0304 0.0053 0.0017 1159 HOH A O 5186 O O . HOH V . ? 0.4862 0.4669 0.4282 0.0205 -0.0206 0.0338 1160 HOH A O 5187 O O . HOH V . ? 0.3744 0.4379 0.3733 0.0253 -0.0175 -0.0048 1161 HOH A O 5188 O O . HOH V . ? 0.3828 0.4923 0.4483 0.0093 0.0013 0.0000 1162 HOH A O 5189 O O . HOH V . ? 0.4702 0.5530 0.4951 -0.0141 -0.0101 0.0058 1163 HOH A O 5190 O O . HOH V . ? 0.3986 0.4331 0.3557 0.0245 -0.0419 0.0153 1164 HOH A O 5191 O O . HOH V . ? 0.5100 0.5289 0.5510 0.0007 0.0025 -0.0118 1165 HOH A O 5192 O O . HOH V . ? 0.4658 0.5245 0.4652 -0.0127 0.0143 -0.0235 1166 HOH A O 5193 O O . HOH V . ? 0.4606 0.5335 0.4666 0.0223 0.0312 -0.0062 1167 HOH A O 5194 O O . HOH V . ? 0.5582 0.5530 0.5553 0.0041 -0.0004 -0.0128 1168 HOH A O 5195 O O . HOH V . ? 0.3958 0.3761 0.4077 -0.0070 0.0114 -0.0130 1169 HOH A O 5196 O O . HOH V . ? 0.4234 0.4959 0.3886 0.0195 0.0094 0.0199 1170 HOH A O 5197 O O . HOH V . ? 0.4606 0.5005 0.4827 0.0031 0.0022 -0.0030 1171 HOH A O 5198 O O . HOH V . ? 0.4679 0.3356 0.3418 -0.0103 0.0324 -0.0190 1172 HOH A O 5199 O O . HOH V . ? 0.4342 0.4356 0.3779 -0.0242 -0.0285 -0.0142 1173 HOH A O 5200 O O . HOH V . ? 0.4776 0.4964 0.4611 0.0239 -0.0018 0.0206 1174 HOH A O 5201 O O . HOH V . ? 0.5160 0.5295 0.4480 -0.0186 0.0112 0.0146 1175 HOH A O 5202 O O . HOH V . ? 0.4240 0.4376 0.3759 -0.0027 0.0056 0.0175 1176 HOH A O 5203 O O . HOH V . ? 0.4751 0.4470 0.4750 0.0180 -0.0175 -0.0149 1177 HOH A O 5204 O O . HOH V . ? 0.8245 0.8162 0.8286 -0.0038 -0.0027 -0.0056 1178 HOH A O 5205 O O . HOH V . ? 0.4434 0.5010 0.5237 0.0067 -0.0049 0.0105 1179 HOH A O 5206 O O . HOH V . ? 0.4965 0.5199 0.4776 -0.0206 -0.0196 -0.0051 1180 HOH A O 5207 O O . HOH V . ? 0.5951 0.5276 0.5494 0.0059 -0.0026 0.0038 1181 HOH A O 5208 O O . HOH V . ? 0.5621 0.5305 0.5303 -0.0103 0.0027 -0.0114 1182 HOH A O 5209 O O . HOH V . ? 0.6929 0.6917 0.6838 -0.0045 0.0006 0.0134 1183 HOH A O 5210 O O . HOH V . ? 0.4329 0.4630 0.4130 0.0279 0.0136 0.0315 1184 HOH A O 5211 O O . HOH V . ? 0.4652 0.4777 0.4992 -0.0067 0.0169 0.0109 1185 HOH A O 5212 O O . HOH V . ? 0.6929 0.6808 0.6777 0.0041 0.0117 -0.0026 1186 HOH A O 5213 O O . HOH V . ? 0.4205 0.4813 0.4399 0.0057 -0.0085 0.0284 1187 HOH A O 5214 O O . HOH V . ? 0.4302 0.4482 0.4296 0.0169 -0.0025 0.0068 1188 HOH A O 5215 O O . HOH V . ? 0.4388 0.3780 0.3161 -0.0178 0.0267 -0.0357 1189 HOH A O 5216 O O . HOH V . ? 0.4182 0.4508 0.4102 -0.0028 -0.0155 0.0009 1190 HOH A O 5217 O O . HOH V . ? 0.5827 0.5475 0.5663 0.0095 0.0102 0.0022 1191 HOH A O 5218 O O . HOH V . ? 0.5111 0.5545 0.4874 0.0097 0.0007 -0.0124 1192 HOH A O 5219 O O . HOH V . ? 0.6237 0.6281 0.6364 0.0020 -0.0071 0.0098 1193 HOH A O 5220 O O . HOH V . ? 0.5538 0.5619 0.5304 -0.0116 -0.0039 0.0143 1194 HOH A O 5221 O O . HOH V . ? 0.4693 0.4825 0.4809 -0.0080 -0.0011 -0.0183 1195 HOH A O 5222 O O . HOH V . ? 0.4333 0.5227 0.4533 0.0076 0.0123 -0.0001 1196 HOH A O 5223 O O . HOH V . ? 0.6580 0.6552 0.6322 0.0061 0.0042 0.0005 1197 HOH A O 5224 O O . HOH V . ? 0.5148 0.4947 0.5372 -0.0044 0.0106 -0.0186 1198 HOH A O 5225 O O . HOH V . ? 0.5162 0.4740 0.4905 -0.0230 0.0188 -0.0156 1199 HOH A O 5226 O O . HOH V . ? 0.5156 0.4776 0.5148 0.0057 0.0082 0.0176 1200 HOH A O 5227 O O . HOH V . ? 0.5089 0.5154 0.4884 -0.0015 0.0176 0.0024 1201 HOH A O 5228 O O . HOH V . ? 0.4994 0.4802 0.4873 0.0026 0.0261 0.0135 1202 HOH A O 5229 O O . HOH V . ? 0.4134 0.4878 0.4684 0.0268 -0.0230 0.0027 1203 HOH A O 5230 O O . HOH V . ? 0.5805 0.5352 0.5432 -0.0039 -0.0088 -0.0060 1204 HOH A O 5231 O O . HOH V . ? 0.4599 0.4996 0.4864 -0.0116 -0.0077 -0.0225 1205 HOH A O 5232 O O . HOH V . ? 0.4826 0.4966 0.4949 0.0024 -0.0133 -0.0005 1206 HOH A O 5233 O O . HOH V . ? 0.5907 0.5840 0.5867 -0.0016 -0.0047 0.0001 1207 HOH A O 5234 O O . HOH V . ? 0.4142 0.5375 0.4646 0.0018 -0.0259 0.0045 1208 HOH A O 5235 O O . HOH V . ? 0.5026 0.4933 0.4999 0.0197 0.0160 0.0034 1209 HOH A O 5236 O O . HOH V . ? 0.4949 0.4998 0.4805 0.0081 0.0118 0.0112 1210 HOH A O 5237 O O . HOH V . ? 0.5404 0.5502 0.5354 -0.0051 -0.0056 -0.0021 1211 HOH A O 5238 O O . HOH V . ? 0.5318 0.5261 0.4957 0.0099 -0.0095 -0.0190 1212 HOH A O 5239 O O . HOH V . ? 0.4363 0.4893 0.4684 -0.0460 -0.0267 -0.0130 1213 HOH A O 5240 O O . HOH V . ? 0.4273 0.5037 0.4719 -0.0303 -0.0018 0.0191 1214 HOH A O 5241 O O . HOH V . ? 0.4789 0.4314 0.5044 0.0091 0.0280 0.0120 1215 HOH A O 5242 O O . HOH V . ? 0.4504 0.4869 0.4410 0.0036 -0.0047 -0.0319 1216 HOH A O 5243 O O . HOH V . ? 0.4923 0.5662 0.5356 0.0022 -0.0195 -0.0056 1217 HOH A O 5244 O O . HOH V . ? 0.4921 0.5245 0.5022 0.0197 -0.0267 -0.0005 1218 HOH A O 5245 O O . HOH V . ? 0.5061 0.4614 0.4693 -0.0255 0.0257 -0.0186 1219 HOH A O 5246 O O . HOH V . ? 0.7388 0.7187 0.6945 0.0068 -0.0037 0.0046 1220 HOH A O 5247 O O . HOH V . ? 0.4215 0.4876 0.3805 0.0166 -0.0194 0.0331 1221 HOH A O 5248 O O . HOH V . ? 0.5693 0.5521 0.5413 -0.0063 0.0060 -0.0097 1222 HOH A O 5249 O O . HOH V . ? 0.4895 0.4421 0.4915 0.0038 0.0117 -0.0074 1223 HOH A O 5250 O O . HOH V . ? 0.4223 0.4530 0.3896 -0.0193 0.0110 -0.0442 1224 HOH A O 5251 O O . HOH V . ? 0.5145 0.4870 0.4988 0.0055 -0.0179 -0.0066 1225 HOH A O 5252 O O . HOH V . ? 0.5118 0.5220 0.4750 0.0012 0.0102 0.0098 1226 HOH A O 5253 O O . HOH V . ? 0.4317 0.3982 0.4006 -0.0381 -0.0230 0.0042 1227 HOH A O 5254 O O . HOH V . ? 0.4418 0.4426 0.3842 0.0075 0.0113 0.0382 1228 HOH A O 5255 O O . HOH V . ? 0.5541 0.5625 0.5674 0.0010 0.0020 0.0072 1229 HOH A O 5256 O O . HOH V . ? 0.5196 0.5645 0.5186 0.0046 -0.0193 -0.0030 1230 HOH A O 5257 O O . HOH V . ? 0.3210 0.3949 0.3482 0.0263 0.0064 0.0052 1231 HOH A O 5258 O O . HOH V . ? 0.4971 0.4720 0.4931 -0.0045 -0.0067 -0.0065 1232 HOH A O 5259 O O . HOH V . ? 0.5691 0.5810 0.5283 -0.0133 0.0076 0.0035 1233 HOH A O 5260 O O . HOH V . ? 0.4209 0.4182 0.3343 -0.0131 -0.0082 -0.0099 1234 HOH A O 5261 O O . HOH V . ? 0.5606 0.5881 0.5633 0.0085 0.0198 -0.0104 1235 HOH A O 5262 O O . HOH V . ? 0.5185 0.5261 0.5573 -0.0106 -0.0021 -0.0116 1236 HOH A O 5263 O O . HOH V . ? 0.4844 0.5160 0.5510 -0.0034 -0.0217 0.0046 1237 HOH A O 5264 O O . HOH V . ? 0.6904 0.7095 0.7454 -0.0071 0.0075 0.0063 1238 HOH A O 5265 O O . HOH V . ? 0.6189 0.5837 0.5942 -0.0073 -0.0020 0.0041 1239 HOH A O 5266 O O . HOH V . ? 0.5598 0.5871 0.5357 0.0047 -0.0227 -0.0059 1240 HOH A O 5267 O O . HOH V . ? 0.5094 0.5047 0.4773 -0.0227 0.0127 -0.0081 1241 HOH A O 5268 O O . HOH V . ? 0.5272 0.5471 0.5010 0.0065 0.0039 0.0150 1242 HOH A O 5269 O O . HOH V . ? 0.5030 0.4965 0.5246 0.0029 0.0195 0.0036 1243 HOH A O 5270 O O . HOH V . ? 0.5746 0.6260 0.5577 -0.0023 -0.0250 0.0087 1244 HOH A O 5271 O O . HOH V . ? 0.4850 0.4885 0.4522 -0.0155 0.0064 -0.0093 1245 HOH A O 5272 O O . HOH V . ? 0.5012 0.5285 0.4716 -0.0016 0.0048 0.0178 1246 HOH A O 5273 O O . HOH V . ? 0.5757 0.6092 0.5621 0.0053 -0.0110 0.0104 1247 HOH A O 5274 O O . HOH V . ? 0.5067 0.5492 0.4482 0.0086 0.0272 0.0107 1248 HOH A O 5275 O O . HOH V . ? 0.4481 0.4668 0.4002 0.0194 0.0016 0.0099 1249 HOH A O 5276 O O . HOH V . ? 0.5624 0.5806 0.5282 0.0020 -0.0297 0.0260 1250 HOH A O 5277 O O . HOH V . ? 0.4090 0.4708 0.4283 0.0316 0.0034 0.0221 1251 HOH A O 5278 O O . HOH V . ? 0.7132 0.7376 0.7065 0.0022 -0.0103 -0.0097 1252 HOH A O 5279 O O . HOH V . ? 0.4631 0.5088 0.4192 -0.0051 -0.0064 -0.0110 1253 HOH A O 5280 O O . HOH V . ? 0.5097 0.4437 0.4498 0.0086 0.0165 -0.0003 1254 HOH A O 5281 O O . HOH V . ? 0.4983 0.5185 0.4907 -0.0053 0.0220 0.0024 1255 HOH A O 5282 O O . HOH V . ? 0.4685 0.4659 0.4115 0.0203 0.0002 -0.0008 1256 HOH A O 5283 O O . HOH V . ? 0.8633 0.8689 0.8592 0.0018 -0.0025 -0.0032 1257 HOH A O 5284 O O . HOH V . ? 0.5041 0.5235 0.5365 -0.0092 0.0063 -0.0227 1258 HOH A O 5285 O O . HOH V . ? 0.4306 0.4363 0.4498 -0.0405 0.0520 0.0029 1259 HOH A O 5286 O O . HOH V . ? 0.3459 0.4089 0.3514 -0.0064 0.0139 -0.0054 1260 HOH A O 5287 O O . HOH V . ? 0.3870 0.4815 0.3567 0.0153 -0.0052 0.0122 1261 HOH A O 5288 O O . HOH V . ? 0.4952 0.4553 0.4759 0.0070 0.0043 0.0292 1262 HOH A O 5289 O O . HOH V . ? 0.4667 0.4505 0.4700 0.0138 0.0155 0.0049 1263 HOH A O 5290 O O . HOH V . ? 0.5122 0.5414 0.4701 0.0124 -0.0291 -0.0113 1264 HOH A O 5291 O O . HOH V . ? 0.4882 0.5581 0.5459 0.0099 0.0111 0.0277 1265 HOH A O 5292 O O . HOH V . ? 0.5279 0.4891 0.5197 0.0100 0.0114 0.0069 1266 HOH A O 5293 O O . HOH V . ? 0.4351 0.4487 0.4433 -0.0169 -0.0056 -0.0002 1267 HOH A O 5294 O O . HOH V . ? 0.4051 0.4784 0.4997 0.0046 0.0175 0.0152 1268 HOH A O 5295 O O . HOH V . ? 0.3915 0.4506 0.3882 -0.0076 0.0088 -0.0102 1269 HOH A O 5296 O O . HOH V . ? 0.6774 0.7011 0.6968 0.0043 -0.0062 -0.0015 1270 HOH A O 5297 O O . HOH V . ? 0.4676 0.4171 0.4464 -0.0091 0.0146 0.0147 1271 HOH A O 5298 O O . HOH V . ? 0.5123 0.5666 0.5743 -0.0067 0.0157 0.0094 1272 HOH A O 5299 O O . HOH V . ? 0.4517 0.5299 0.4680 0.0049 0.0234 -0.0273 1273 HOH A O 5300 O O . HOH V . ? 0.3829 0.4440 0.3564 -0.0017 -0.0224 -0.0269 1274 HOH A O 5301 O O . HOH V . ? 0.7744 0.7531 0.7526 0.0030 0.0034 -0.0075 1275 HOH A O 5302 O O . HOH V . ? 0.5670 0.5376 0.5620 0.0123 0.0084 0.0081 1276 HOH A O 5303 O O . HOH V . ? 0.4529 0.4182 0.4813 0.0162 0.0071 0.0117 1277 HOH A O 5304 O O . HOH V . ? 0.4930 0.5520 0.5363 0.0166 0.0121 -0.0171 1278 HOH A O 5305 O O . HOH V . ? 0.6589 0.6546 0.6422 0.0041 0.0140 0.0069 1279 HOH A O 5306 O O . HOH V . ? 0.4966 0.4897 0.4836 -0.0116 0.0011 0.0034 1280 HOH A O 5307 O O . HOH V . ? 0.5838 0.5985 0.5498 -0.0120 -0.0023 0.0059 1281 HOH A O 5308 O O . HOH V . ? 0.7997 0.8051 0.8118 0.0000 -0.0005 -0.0031 1282 HOH A O 5309 O O . HOH V . ? 0.4521 0.5030 0.4878 -0.0094 -0.0230 0.0086 1283 HOH A O 5310 O O . HOH V . ? 0.5479 0.5265 0.5614 -0.0181 -0.0212 0.0009 1284 HOH A O 5311 O O . HOH V . ? 0.4749 0.5175 0.5086 -0.0101 0.0100 -0.0122 1285 HOH A O 5312 O O . HOH V . ? 0.7275 0.7469 0.7208 0.0010 -0.0167 0.0113 1286 HOH A O 5313 O O . HOH V . ? 0.6255 0.5573 0.6130 0.0051 -0.0001 0.0093 1287 HOH A O 5314 O O . HOH V . ? 0.5435 0.5749 0.5528 -0.0048 -0.0120 -0.0031 1288 HOH A O 5315 O O . HOH V . ? 0.7073 0.7018 0.6803 0.0072 -0.0043 0.0082 1289 HOH A O 5316 O O . HOH V . ? 0.6616 0.6550 0.6786 -0.0101 -0.0018 0.0010 1290 HOH A O 5317 O O . HOH V . ? 0.4891 0.5159 0.4895 -0.0210 -0.0023 -0.0047 1291 HOH A O 5318 O O . HOH V . ? 0.5839 0.5693 0.5835 0.0106 0.0180 0.0224 1292 HOH A O 5319 O O . HOH V . ? 0.3830 0.4332 0.4530 0.0424 -0.0226 0.0079 1293 HOH A O 5320 O O . HOH V . ? 0.9127 0.9120 0.9083 -0.0019 -0.0010 -0.0015 1294 HOH A O 5321 O O . HOH V . ? 0.4624 0.5276 0.4933 0.0251 0.0201 -0.0132 1295 HOH A O 5322 O O . HOH V . ? 0.5285 0.5477 0.4946 -0.0148 0.0116 -0.0081 1296 HOH A O 5323 O O . HOH V . ? 0.6139 0.6086 0.6170 0.0038 -0.0145 -0.0083 1297 HOH A O 5324 O O . HOH V . ? 0.5198 0.4847 0.5110 -0.0143 -0.0040 0.0173 1298 HOH A O 5325 O O . HOH V . ? 0.5096 0.5521 0.5642 0.0001 -0.0036 0.0024 1299 HOH A O 5326 O O . HOH V . ? 0.7757 0.7936 0.7869 0.0054 0.0029 0.0029 1300 HOH A O 5327 O O . HOH V . ? 0.6216 0.6295 0.6341 -0.0155 -0.0069 -0.0084 1301 HOH A O 5328 O O . HOH V . ? 0.4996 0.4810 0.5126 -0.0154 0.0124 0.0228 1302 HOH A O 5329 O O . HOH V . ? 0.6640 0.6780 0.6327 0.0118 0.0053 0.0094 1303 HOH A O 5330 O O . HOH V . ? 0.6088 0.6463 0.6115 -0.0069 -0.0061 0.0053 1304 HOH A O 5331 O O . HOH V . ? 0.4548 0.4753 0.4812 0.0201 -0.0001 -0.0113 1305 HOH A O 5332 O O . HOH V . ? 0.4766 0.4998 0.4750 0.0073 -0.0066 -0.0131 1306 HOH A O 5333 O O . HOH V . ? 0.5599 0.5842 0.5267 -0.0036 0.0131 0.0022 1307 HOH A O 5334 O O . HOH V . ? 0.6440 0.6579 0.6494 -0.0079 -0.0024 -0.0051 1308 HOH A O 5335 O O . HOH V . ? 0.5660 0.5782 0.5823 -0.0235 -0.0086 -0.0059 1309 HOH A O 5336 O O . HOH V . ? 0.7171 0.6992 0.6716 0.0017 0.0026 0.0032 1310 HOH A O 5337 O O . HOH V . ? 0.6650 0.6700 0.6784 -0.0032 -0.0082 0.0000 1311 HOH A O 5338 O O . HOH V . ? 0.7301 0.7282 0.7081 0.0082 0.0139 -0.0056 1312 HOH A O 5339 O O . HOH V . ? 0.5259 0.5761 0.5495 0.0032 -0.0070 0.0058 1313 HOH A O 5340 O O . HOH V . ? 0.4755 0.4801 0.4754 -0.0201 -0.0035 -0.0097 1314 HOH A O 5341 O O . HOH V . ? 0.5237 0.5661 0.6022 -0.0098 -0.0112 -0.0033 1315 HOH A O 5342 O O . HOH V . ? 0.5248 0.5693 0.5439 -0.0137 -0.0254 -0.0048 1316 HOH A O 5343 O O . HOH V . ? 0.5677 0.5720 0.5499 0.0011 -0.0022 0.0014 1317 HOH A O 5344 O O . HOH V . ? 0.6450 0.6263 0.6230 0.0032 0.0037 0.0104 1318 HOH A O 5345 O O . HOH V . ? 0.6679 0.6497 0.6635 -0.0065 0.0004 0.0011 1319 HOH A O 5346 O O . HOH V . ? 0.6353 0.6345 0.6206 -0.0060 -0.0048 0.0060 1320 HOH A O 5347 O O . HOH V . ? 0.5975 0.6152 0.6030 -0.0073 0.0064 0.0113 1321 HOH A O 5348 O O . HOH V . ? 0.5395 0.5627 0.5041 -0.0157 0.0207 -0.0001 1322 HOH A O 5349 O O . HOH V . ? 0.5205 0.5092 0.5260 0.0198 0.0055 -0.0118 1323 HOH A O 5350 O O . HOH V . ? 0.5622 0.5648 0.5004 -0.0003 -0.0017 0.0032 1324 HOH A O 5351 O O . HOH V . ? 0.8030 0.7993 0.8020 0.0069 0.0048 -0.0017 1325 HOH A O 5352 O O . HOH V . ? 0.6816 0.6908 0.6711 0.0112 -0.0035 -0.0009 1326 HOH A O 5353 O O . HOH V . ? 0.6718 0.6743 0.6458 -0.0016 0.0076 0.0000 1327 HOH A O 5354 O O . HOH V . ? 0.6155 0.6090 0.5982 0.0038 0.0000 0.0004 1328 HOH A O 5355 O O . HOH V . ? 0.5772 0.6107 0.5867 0.0006 0.0050 -0.0159 1329 HOH A O 5356 O O . HOH V . ? 0.9065 0.9114 0.9200 0.0001 -0.0026 0.0015 1330 HOH A O 5357 O O . HOH V . ? 0.6905 0.6981 0.6802 0.0037 -0.0147 0.0020 1331 HOH A O 5358 O O . HOH V . ? 0.5462 0.5878 0.5555 0.0048 -0.0027 0.0021 1332 HOH A O 5359 O O . HOH V . ? 0.5208 0.5787 0.5245 -0.0256 0.0027 0.0049 1333 HOH A O 5360 O O . HOH V . ? 0.7065 0.6791 0.6693 0.0104 0.0053 0.0069 1334 HOH A O 5361 O O . HOH V . ? 0.6988 0.6779 0.6860 -0.0026 -0.0010 -0.0001 1335 HOH A O 5362 O O . HOH V . ? 0.5030 0.4949 0.5013 -0.0162 0.0232 0.0065 1336 HOH A O 5363 O O . HOH V . ? 0.5809 0.5683 0.5876 0.0019 -0.0076 -0.0026 1337 HOH A O 5364 O O . HOH V . ? 0.6828 0.6454 0.6751 0.0005 -0.0097 0.0012 1338 HOH A O 5365 O O . HOH V . ? 0.5880 0.5688 0.5615 -0.0063 -0.0022 -0.0282 1339 HOH A O 5366 O O . HOH V . ? 0.4858 0.4872 0.4758 -0.0031 -0.0273 0.0097 1340 HOH A O 5367 O O . HOH V . ? 0.7196 0.7498 0.7488 -0.0075 0.0038 0.0007 1341 HOH A O 5368 O O . HOH V . ? 0.5653 0.5111 0.5306 -0.0146 0.0121 0.0202 1342 HOH A O 5369 O O . HOH V . ? 0.7788 0.7755 0.7645 -0.0068 -0.0007 -0.0064 1343 HOH A O 5370 O O . HOH V . ? 0.6088 0.5937 0.5937 0.0206 0.0041 0.0000 1344 HOH A O 5371 O O . HOH V . ? 0.4429 0.4829 0.4261 0.0124 0.0108 0.0288 1345 HOH A O 5372 O O . HOH V . ? 0.6304 0.6739 0.6078 0.0025 0.0071 -0.0067 1346 HOH A O 5373 O O . HOH V . ? 0.7054 0.6946 0.7195 0.0072 0.0058 0.0009 1347 HOH A O 5374 O O . HOH V . ? 0.5850 0.5219 0.5538 0.0179 -0.0004 -0.0028 1348 HOH A O 5375 O O . HOH V . ? 0.5646 0.5834 0.5363 -0.0081 -0.0003 0.0137 1349 HOH A O 5376 O O . HOH V . ? 0.5474 0.5314 0.5415 -0.0064 0.0080 0.0032 1350 HOH A O 5377 O O . HOH V . ? 0.5905 0.5534 0.5683 -0.0154 -0.0036 0.0033 1351 HOH A O 5378 O O . HOH V . ? 0.5082 0.4637 0.4540 -0.0093 0.0198 0.0116 1352 HOH A O 5379 O O . HOH V . ? 0.4414 0.4662 0.4060 -0.0108 0.0038 0.0001 1353 HOH A O 5380 O O . HOH V . ? 0.4724 0.4388 0.4196 -0.0058 -0.0185 -0.0109 1354 HOH A O 5381 O O . HOH V . ? 0.6792 0.6440 0.6451 0.0039 -0.0022 0.0058 1355 HOH A O 5382 O O . HOH V . ? 0.4634 0.4848 0.4601 0.0085 0.0118 0.0172 1356 HOH A O 5383 O O . HOH V . ? 0.5486 0.5815 0.5659 -0.0117 -0.0097 -0.0003 1357 HOH A O 5384 O O . HOH V . ? 0.5288 0.5065 0.5683 -0.0051 0.0218 0.0062 1358 HOH A O 5385 O O . HOH V . ? 0.4097 0.4688 0.3895 0.0096 -0.0045 0.0081 1359 HOH A O 5386 O O . HOH V . ? 0.5792 0.5850 0.5744 0.0156 -0.0002 0.0240 1360 HOH A O 5387 O O . HOH V . ? 0.4719 0.4850 0.4065 0.0033 0.0079 0.0224 1361 HOH A O 5388 O O . HOH V . ? 0.6437 0.6351 0.6334 0.0023 0.0078 0.0146 1362 HOH A O 5389 O O . HOH V . ? 0.5754 0.5883 0.5315 0.0034 -0.0136 -0.0025 1363 HOH A O 5390 O O . HOH V . ? 0.6876 0.6726 0.6736 0.0108 0.0035 -0.0005 1364 HOH A O 5391 O O . HOH V . ? 0.8120 0.8066 0.8139 -0.0010 0.0001 0.0087 1365 HOH A O 5392 O O . HOH V . ? 0.5566 0.6133 0.5650 0.0104 -0.0169 -0.0004 1366 HOH A O 5393 O O . HOH V . ? 0.6622 0.6457 0.6389 -0.0020 0.0013 0.0070 1367 HOH A O 5394 O O . HOH V . ? 0.6771 0.6982 0.6720 0.0009 -0.0160 -0.0161 1368 HOH A O 5395 O O . HOH V . ? 0.4848 0.5026 0.5033 -0.0113 0.0073 -0.0138 1369 HOH A O 5396 O O . HOH V . ? 0.6223 0.6061 0.5975 0.0047 -0.0039 0.0147 1370 HOH A O 5397 O O . HOH V . ? 0.6032 0.6314 0.5805 -0.0007 -0.0026 0.0019 1371 HOH A O 5398 O O . HOH V . ? 0.5945 0.5921 0.5452 -0.0060 0.0033 0.0059 1372 HOH A O 5399 O O . HOH V . ? 0.5585 0.5662 0.5214 0.0154 0.0102 0.0001 1373 HOH A O 5400 O O . HOH V . ? 0.4999 0.5208 0.5142 0.0053 -0.0281 0.0137 1374 HOH A O 5401 O O . HOH V . ? 0.6742 0.6609 0.6623 -0.0052 -0.0027 0.0021 1375 HOH A O 5402 O O . HOH V . ? 0.5361 0.5517 0.5597 -0.0066 -0.0106 -0.0134 1376 HOH A O 5403 O O . HOH V . ? 0.6117 0.6101 0.6090 0.0076 0.0140 0.0050 1377 HOH A O 5404 O O . HOH V . ? 0.5615 0.5765 0.5974 0.0127 -0.0037 -0.0106 1378 HOH A O 5405 O O . HOH V . ? 0.5324 0.5653 0.5680 -0.0073 0.0087 -0.0012 1379 HOH A O 5406 O O . HOH V . ? 0.7200 0.7127 0.7254 0.0033 0.0035 -0.0076 1380 HOH A O 5407 O O . HOH V . ? 0.5209 0.5784 0.5405 -0.0089 0.0209 -0.0139 1381 HOH A O 5408 O O . HOH V . ? 0.8698 0.8680 0.8687 -0.0030 0.0002 -0.0006 1382 HOH A O 5409 O O . HOH V . ? 0.5790 0.6320 0.6078 0.0153 -0.0150 0.0108 1383 HOH A O 5410 O O . HOH V . ? 0.6300 0.6441 0.6393 0.0051 0.0072 0.0073 1384 HOH A O 5411 O O . HOH V . ? 0.7788 0.7547 0.7698 0.0047 0.0020 -0.0014 1385 HOH A O 5412 O O . HOH V . ? 0.8041 0.8118 0.8167 0.0036 -0.0049 0.0084 1386 HOH A O 5413 O O . HOH V . ? 0.6671 0.6753 0.6550 0.0045 0.0051 0.0067 1387 HOH A O 5414 O O . HOH V . ? 0.6485 0.6566 0.6645 0.0063 -0.0066 0.0081 1388 HOH A O 5415 O O . HOH V . ? 0.5365 0.6071 0.4873 0.0026 -0.0073 0.0132 1389 HOH A O 5416 O O . HOH V . ? 0.5986 0.6545 0.6153 -0.0021 0.0038 0.0071 1390 HOH A O 5417 O O . HOH V . ? 0.4697 0.5442 0.4611 0.0127 -0.0165 -0.0192 1391 HOH A O 5418 O O . HOH V . ? 0.6713 0.7019 0.7004 -0.0068 -0.0009 0.0019 1392 HOH A O 5419 O O . HOH V . ? 0.6688 0.6616 0.6614 0.0003 0.0075 -0.0012 1393 HOH A O 5420 O O . HOH V . ? 0.5862 0.5715 0.5320 0.0002 -0.0181 -0.0131 1394 HOH A O 5421 O O . HOH V . ? 0.5751 0.5832 0.5138 -0.0110 0.0078 -0.0067 1395 HOH A O 5422 O O . HOH V . ? 0.6720 0.6895 0.6571 0.0017 -0.0112 0.0084 1396 HOH A O 5423 O O . HOH V . ? 0.5538 0.5649 0.5461 0.0060 -0.0011 -0.0009 1397 HOH A O 5424 O O . HOH V . ? 0.6087 0.5932 0.5805 0.0125 0.0038 0.0086 1398 HOH A O 5425 O O . HOH V . ? 0.6006 0.5989 0.6000 -0.0005 0.0105 0.0009 1399 HOH A O 5426 O O . HOH V . ? 0.6329 0.6480 0.6167 0.0126 -0.0083 0.0072 1400 HOH A O 5427 O O . HOH V . ? 0.8266 0.8263 0.8283 0.0040 0.0032 0.0027 1401 HOH A O 5428 O O . HOH V . ? 0.4996 0.5810 0.4797 -0.0141 0.0071 -0.0012 1402 HOH A O 5429 O O . HOH V . ? 0.7714 0.7695 0.7834 0.0088 0.0014 0.0019 1403 HOH A O 5430 O O . HOH V . ? 0.8220 0.8226 0.8046 0.0014 0.0038 -0.0040 1404 HOH A O 5431 O O . HOH V . ? 0.6304 0.5906 0.6235 0.0027 -0.0040 -0.0095 1405 HOH A O 5432 O O . HOH V . ? 0.6509 0.6392 0.6315 -0.0051 0.0087 -0.0108 1406 HOH A O 5433 O O . HOH V . ? 0.5502 0.5278 0.5417 -0.0099 0.0047 0.0016 1407 HOH A O 5434 O O . HOH V . ? 0.5064 0.5443 0.5007 0.0119 -0.0102 0.0061 1408 HOH A O 5435 O O . HOH V . ? 0.6274 0.6461 0.6253 0.0153 -0.0021 0.0007 1409 HOH A O 5436 O O . HOH V . ? 0.5679 0.5458 0.5624 0.0038 0.0018 0.0049 1410 HOH A O 5437 O O . HOH V . ? 0.5717 0.5725 0.5929 0.0114 -0.0096 0.0004 1411 HOH A O 5438 O O . HOH V . ? 0.7524 0.7426 0.7356 -0.0086 -0.0033 -0.0069 1412 HOH A O 5439 O O . HOH V . ? 0.5751 0.5438 0.6021 -0.0038 0.0064 0.0025 1413 HOH A O 5440 O O . HOH V . ? 0.8964 0.9031 0.9072 0.0028 -0.0015 -0.0003 1414 HOH A O 5441 O O . HOH V . ? 0.7333 0.6971 0.6985 0.0159 -0.0038 -0.0069 1415 HOH A O 5442 O O . HOH V . ? 0.6246 0.5695 0.5625 -0.0063 -0.0012 -0.0075 1416 HOH A O 5443 O O . HOH V . ? 0.7048 0.6928 0.6853 -0.0037 0.0088 -0.0024 1417 HOH A O 5444 O O . HOH V . ? 0.6765 0.6678 0.6501 -0.0056 -0.0093 0.0062 1418 HOH A O 5445 O O . HOH V . ? 0.6691 0.6730 0.6380 -0.0057 0.0039 0.0241 1419 HOH A O 5446 O O . HOH V . ? 0.6124 0.6404 0.5832 0.0146 -0.0041 0.0005 1420 HOH A O 5447 O O . HOH V . ? 0.8596 0.8656 0.8554 0.0012 -0.0071 -0.0012 1421 HOH A O 5448 O O . HOH V . ? 0.7651 0.7802 0.7636 0.0005 -0.0003 -0.0012 1422 HOH A O 5449 O O . HOH V . ? 0.8049 0.8232 0.7982 0.0028 0.0015 0.0040 1423 HOH A O 5450 O O . HOH V . ? 0.6504 0.6512 0.6361 0.0112 0.0107 -0.0059 1424 HOH A O 5451 O O . HOH V . ? 0.6560 0.6586 0.6316 -0.0041 0.0083 -0.0001 1425 HOH A O 5452 O O . HOH V . ? 0.7680 0.7727 0.7599 0.0068 0.0060 -0.0044 1426 HOH A O 5453 O O . HOH V . ? 0.7637 0.7603 0.7643 0.0056 0.0080 0.0012 1427 HOH A O 5454 O O . HOH V . ? 0.5660 0.5615 0.5414 -0.0001 -0.0254 0.0100 1428 HOH A O 5455 O O . HOH V . ? 0.6199 0.6028 0.5963 0.0079 -0.0044 -0.0061 1429 HOH A O 5456 O O . HOH V . ? 0.7805 0.7777 0.7684 -0.0047 -0.0061 0.0064 1430 HOH A O 5457 O O . HOH V . ? 0.5464 0.5426 0.5109 -0.0166 0.0122 -0.0168 1431 HOH A O 5458 O O . HOH V . ? 0.6843 0.6871 0.6541 -0.0146 0.0030 0.0091 1432 HOH A O 5459 O O . HOH V . ? 0.5965 0.5986 0.6016 -0.0020 -0.0068 -0.0103 1433 HOH A O 5460 O O . HOH V . ? 0.6350 0.6479 0.6720 0.0022 -0.0043 -0.0049 1434 HOH A O 5461 O O . HOH V . ? 0.8701 0.8813 0.8690 -0.0001 -0.0057 0.0028 1435 HOH A O 5462 O O . HOH V . ? 0.5127 0.5936 0.5971 -0.0151 -0.0129 -0.0014 1436 HOH A O 5463 O O . HOH V . ? 0.7055 0.6934 0.6990 -0.0034 -0.0006 0.0133 1437 HOH A O 5464 O O . HOH V . ? 0.6711 0.6573 0.6737 -0.0042 0.0069 -0.0014 1438 HOH A O 5465 O O . HOH V . ? 0.8021 0.7984 0.8002 0.0026 -0.0008 0.0090 1439 HOH A O 5466 O O . HOH V . ? 1.0199 1.0173 1.0151 -0.0039 -0.0006 -0.0004 1440 HOH A O 5467 O O . HOH V . ? 0.7180 0.7521 0.7512 0.0024 0.0023 0.0078 1441 HOH A O 5468 O O . HOH V . ? 0.6901 0.7031 0.7058 -0.0054 -0.0067 0.0002 1442 HOH A O 5469 O O . HOH V . ? 0.8853 0.8703 0.8764 -0.0025 -0.0008 -0.0016 1443 HOH A O 5470 O O . HOH V . ? 0.4985 0.4065 0.4551 0.0169 -0.0075 -0.0188 1444 HOH A O 5471 O O . HOH V . ? 0.9249 0.9013 0.9225 -0.0025 0.0022 0.0021 1445 HOH A O 5472 O O . HOH V . ? 0.7538 0.7499 0.7687 -0.0064 -0.0032 0.0010 1446 HOH A O 5473 O O . HOH V . ? 0.6373 0.6019 0.6061 0.0087 0.0122 0.0141 1447 HOH A O 5474 O O . HOH V . ? 0.6699 0.6682 0.6702 0.0074 0.0021 -0.0045 1448 HOH A O 5475 O O . HOH V . ? 0.5599 0.5910 0.5886 0.0081 -0.0068 0.0092 1449 HOH A O 5476 O O . HOH V . ? 0.5947 0.6221 0.6151 -0.0013 -0.0031 -0.0080 1450 HOH A O 5477 O O . HOH V . ? 0.6598 0.6363 0.6626 -0.0167 -0.0042 -0.0021 1451 HOH A O 5478 O O . HOH V . ? 0.7432 0.7339 0.7226 0.0073 -0.0005 0.0069 1452 HOH A O 5479 O O . HOH V . ? 0.5823 0.6098 0.5943 -0.0041 0.0067 0.0056 1453 HOH A O 5480 O O . HOH V . ? 0.8546 0.8681 0.8467 -0.0001 0.0015 0.0007 1454 HOH A O 5481 O O . HOH V . ? 0.6276 0.6378 0.6339 0.0057 -0.0142 -0.0094 1455 HOH A O 5482 O O . HOH V . ? 0.5748 0.5800 0.6042 0.0085 0.0089 -0.0016 1456 HOH A O 5483 O O . HOH V . ? 0.9025 0.8901 0.8967 0.0036 0.0021 -0.0038 1457 HOH A O 5484 O O . HOH V . ? 0.7109 0.7218 0.7159 0.0059 0.0020 0.0063 1458 HOH A O 5485 O O . HOH V . ? 0.6276 0.6486 0.6563 -0.0012 -0.0054 -0.0031 1459 HOH A O 5486 O O . HOH V . ? 0.7168 0.6817 0.7096 -0.0003 0.0028 0.0112 1460 HOH A O 5487 O O . HOH V . ? 0.6460 0.6398 0.6419 -0.0001 0.0052 0.0099 1461 HOH A O 5488 O O . HOH V . ? 0.7378 0.7456 0.7503 0.0019 0.0010 -0.0049 1462 HOH A O 5489 O O . HOH V . ? 0.8785 0.8748 0.8805 0.0046 -0.0016 0.0015 1463 HOH A O 5490 O O . HOH V . ? 0.5680 0.5753 0.5995 -0.0137 -0.0031 -0.0065 1464 HOH A O 5491 O O . HOH V . ? 0.6091 0.6391 0.6163 -0.0162 0.0124 0.0103 1465 HOH A O 5492 O O . HOH V . ? 0.7218 0.6960 0.7052 -0.0047 0.0031 -0.0025 1466 HOH A O 5493 O O . HOH V . ? 0.6854 0.6889 0.6616 0.0046 0.0069 0.0062 1467 HOH A O 5494 O O . HOH V . ? 0.7226 0.7161 0.7050 -0.0029 -0.0041 -0.0071 1468 HOH A O 5495 O O . HOH V . ? 0.6916 0.6846 0.7102 -0.0072 -0.0024 -0.0003 1469 HOH A O 5496 O O . HOH V . ? 0.7572 0.7467 0.7595 0.0006 -0.0014 -0.0007 1470 HOH A O 5497 O O . HOH V . ? 0.6170 0.6066 0.6181 -0.0189 -0.0088 -0.0028 1471 HOH A O 5498 O O . HOH V . ? 0.8267 0.8365 0.8287 -0.0013 -0.0072 0.0063 1472 HOH A O 5499 O O . HOH V . ? 0.6549 0.6519 0.6823 0.0163 0.0001 -0.0086 1473 HOH A O 5500 O O . HOH V . ? 1.0209 1.0247 1.0251 -0.0010 0.0014 -0.0012 1474 HOH A O 5501 O O . HOH V . ? 0.8377 0.8419 0.8442 0.0013 -0.0052 0.0002 1475 HOH A O 5502 O O . HOH V . ? 0.6930 0.7073 0.6768 -0.0061 -0.0056 -0.0028 1476 HOH A O 5503 O O . HOH V . ? 0.7592 0.7736 0.7638 -0.0010 -0.0093 -0.0011 1477 HOH A O 5504 O O . HOH V . ? 0.5595 0.5575 0.5853 0.0112 -0.0068 0.0131 1478 HOH A O 5505 O O . HOH V . ? 0.5175 0.4947 0.5086 0.0009 0.0001 0.0054 1479 HOH A O 5506 O O . HOH V . ? 0.7723 0.7708 0.7775 0.0058 -0.0092 -0.0001 1480 HOH A O 5507 O O . HOH V . ? 0.5360 0.5504 0.5092 0.0112 0.0180 0.0076 1481 HOH A O 5508 O O . HOH V . ? 0.8817 0.8695 0.8588 0.0010 -0.0003 0.0040 1482 HOH A O 5509 O O . HOH V . ? 0.6287 0.6056 0.6350 -0.0158 -0.0196 -0.0012 1483 HOH A O 5510 O O . HOH V . ? 0.4104 0.3898 0.3407 -0.0082 0.0088 -0.0274 1484 HOH A O 5511 O O . HOH V . ? 1.0923 1.0975 1.0918 -0.0033 0.0000 -0.0015 1485 HOH A O 5512 O O . HOH V . ? 0.5172 0.5584 0.5304 -0.0310 -0.0009 -0.0261 1486 HOH A O 5513 O O . HOH V . ? 0.7038 0.7103 0.7171 -0.0026 -0.0047 0.0101 1487 HOH A O 5514 O O . HOH V . ? 0.6527 0.6434 0.6496 -0.0115 0.0049 -0.0038 1488 HOH A O 5515 O O . HOH V . ? 0.4187 0.4693 0.4322 -0.0213 0.0006 0.0011 1489 HOH A O 5516 O O . HOH V . ? 0.6325 0.5991 0.6344 -0.0118 0.0091 0.0132 1490 HOH A O 5517 O O . HOH V . ? 0.5355 0.5569 0.5672 0.0052 -0.0045 -0.0069 1491 HOH A O 5518 O O . HOH V . ? 0.3103 0.3164 0.2732 0.0008 -0.0214 0.0057 1492 HOH A O 5519 O O . HOH V . ? 0.9256 0.9235 0.9401 -0.0022 -0.0032 -0.0038 1493 HOH A O 5520 O O . HOH V . ? 0.9075 0.9094 0.9215 0.0048 0.0038 -0.0006 1494 HOH A O 5521 O O . HOH V . ? 0.4965 0.5464 0.5180 -0.0023 -0.0044 0.0020 1495 HOH A O 5522 O O . HOH V . ? 0.4251 0.4505 0.4600 -0.0100 0.0086 -0.0231 1496 HOH A O 5523 O O . HOH V . ? 0.5296 0.5511 0.5343 0.0082 0.0053 -0.0024 1497 HOH A O 5524 O O . HOH V . ? 0.6766 0.6660 0.6646 -0.0012 -0.0002 0.0059 1498 HOH A O 5525 O O . HOH V . ? 0.4268 0.5001 0.4651 -0.0193 0.0173 0.0120 1499 HOH A O 5526 O O . HOH V . ? 0.6023 0.6137 0.6127 -0.0135 0.0033 0.0062 1500 HOH A O 5527 O O . HOH V . ? 0.5256 0.5388 0.4816 0.0087 -0.0238 -0.0041 1501 HOH A O 5528 O O . HOH V . ? 0.6944 0.6977 0.6984 0.0036 -0.0006 0.0094 1502 HOH A O 5529 O O . HOH V . ? 0.6207 0.6309 0.6381 -0.0060 -0.0105 0.0006 1503 HOH A O 5530 O O . HOH V . ? 0.7733 0.7839 0.7583 0.0065 -0.0004 0.0065 1504 HOH A O 5531 O O . HOH V . ? 0.7096 0.6774 0.7139 -0.0016 0.0026 0.0012 1505 HOH A O 5532 O O . HOH V . ? 0.4349 0.3882 0.4530 -0.0128 -0.0109 0.0109 1506 HOH A O 5533 O O . HOH V . ? 0.4510 0.4605 0.4641 0.0034 0.0056 -0.0328 1507 HOH A O 5534 O O . HOH V . ? 0.4322 0.4450 0.3950 0.0260 0.0099 0.0176 1508 HOH A O 5535 O O . HOH V . ? 0.4646 0.4813 0.5023 -0.0060 -0.0205 -0.0155 1509 HOH A O 5536 O O . HOH V . ? 0.6484 0.6386 0.6075 -0.0044 0.0041 0.0103 1510 HOH A O 5537 O O . HOH V . ? 0.6039 0.6148 0.6233 0.0086 0.0090 -0.0130 1511 HOH A O 5538 O O . HOH V . ? 0.6659 0.6885 0.6774 0.0041 0.0016 -0.0044 1512 HOH A O 5539 O O . HOH V . ? 0.5293 0.5648 0.5780 0.0098 0.0024 -0.0044 1513 HOH A O 5540 O O . HOH V . ? 0.6575 0.6518 0.6390 0.0151 -0.0045 -0.0047 1514 HOH A O 5541 O O . HOH V . ? 0.6102 0.6308 0.6089 0.0004 -0.0115 -0.0009 1515 HOH A O 5542 O O . HOH V . ? 0.6399 0.6431 0.6331 -0.0082 0.0069 0.0001 1516 HOH A O 5543 O O . HOH V . ? 0.6069 0.6110 0.6287 -0.0104 0.0057 -0.0069 1517 HOH A O 5544 O O . HOH V . ? 0.5541 0.5307 0.5763 -0.0080 -0.0044 -0.0100 1518 HOH A O 5545 O O . HOH V . ? 0.6268 0.6255 0.6328 -0.0007 0.0077 -0.0165 1519 HOH A O 5546 O O . HOH V . ? 0.6210 0.5866 0.5902 -0.0089 0.0100 0.0047 1520 HOH A O 5547 O O . HOH V . ? 0.7439 0.7509 0.7427 0.0064 -0.0035 0.0016 1521 HOH A O 5548 O O . HOH V . ? 0.7067 0.6821 0.7041 0.0050 0.0161 0.0010 1522 HOH A O 5549 O O . HOH V . ? 0.6931 0.7098 0.7143 0.0000 -0.0056 -0.0037 1523 HOH A O 5550 O O . HOH V . ? 0.6709 0.6697 0.6755 0.0090 -0.0031 0.0041 1524 HOH A O 5551 O O . HOH V . ? 0.8559 0.8516 0.8317 0.0021 0.0003 -0.0015 1525 HOH A O 5552 O O . HOH V . ? 0.6217 0.6082 0.6477 -0.0085 0.0120 0.0069 1526 HOH A O 5553 O O . HOH V . ? 0.8166 0.8185 0.8182 0.0002 -0.0031 0.0121 1527 HOH A O 5554 O O . HOH V . ? 0.7135 0.7397 0.7270 0.0134 0.0021 -0.0048 1528 HOH A O 5555 O O . HOH V . ? 0.6744 0.6343 0.6362 -0.0037 0.0106 -0.0074 1529 HOH A O 5556 O O . HOH V . ? 0.6589 0.6556 0.6635 0.0072 -0.0052 0.0031 1530 HOH A O 5557 O O . HOH V . ? 0.7199 0.7489 0.7232 0.0002 -0.0071 0.0024 1531 HOH A O 5558 O O . HOH V . ? 0.7421 0.7505 0.7541 -0.0028 0.0091 0.0010 1532 HOH A O 5559 O O . HOH V . ? 0.7246 0.7323 0.7222 0.0021 0.0005 -0.0002 1533 HOH A O 5560 O O . HOH V . ? 0.6469 0.6576 0.6563 0.0012 0.0062 -0.0116 1534 HOH A O 5561 O O . HOH V . ? 0.6404 0.6368 0.6493 0.0024 0.0002 0.0005 1535 HOH A O 5562 O O . HOH V . ? 0.5584 0.5712 0.5589 0.0089 -0.0023 0.0040 1536 HOH A O 5563 O O . HOH V . ? 0.5917 0.6242 0.6009 -0.0065 -0.0014 0.0019 1537 HOH A O 5564 O O . HOH V . ? 0.4820 0.4826 0.4582 0.0091 0.0000 0.0039 1538 HOH A O 5565 O O . HOH V . ? 0.6084 0.5947 0.5828 -0.0086 0.0045 0.0143 1539 HOH A O 5566 O O . HOH V . ? 0.5953 0.5877 0.5737 0.0028 0.0087 -0.0138 1540 HOH A O 5567 O O . HOH V . ? 0.5710 0.5947 0.6053 -0.0151 0.0097 0.0074 1541 HOH A O 5568 O O . HOH V . ? 0.6100 0.5863 0.6242 0.0122 -0.0069 -0.0111 1542 HOH A O 5569 O O . HOH V . ? 0.6293 0.6165 0.5891 -0.0050 -0.0030 -0.0017 1543 HOH A O 5570 O O . HOH V . ? 0.6590 0.6457 0.6166 0.0045 0.0245 0.0046 1544 HOH A O 5571 O O . HOH V . ? 0.6672 0.6573 0.6596 0.0051 -0.0027 0.0028 1545 HOH A O 5572 O O . HOH V . ? 0.6224 0.5906 0.6222 0.0004 0.0037 0.0108 1546 HOH A O 5573 O O . HOH V . ? 0.5767 0.5937 0.5863 0.0002 -0.0056 -0.0118 1547 HOH A O 5574 O O . HOH V . ? 0.6733 0.6591 0.6765 -0.0066 0.0025 0.0047 1548 HOH A O 5575 O O . HOH V . ? 0.5847 0.5618 0.6027 0.0025 0.0047 -0.0058 1549 HOH A O 5576 O O . HOH V . ? 0.8874 0.8815 0.8726 0.0033 0.0017 0.0019 1550 HOH A O 5577 O O . HOH V . ? 0.8287 0.8239 0.8316 -0.0035 0.0023 0.0002 1551 HOH A O 5578 O O . HOH V . ? 0.6622 0.6281 0.6427 0.0109 0.0098 0.0080 1552 HOH A O 5579 O O . HOH V . ? 0.7054 0.7092 0.6953 0.0001 -0.0113 -0.0030 1553 HOH A O 5580 O O . HOH V . ? 0.7120 0.7116 0.7011 -0.0040 0.0004 -0.0062 1554 HOH A O 5581 O O . HOH V . ? 0.5094 0.5511 0.5162 0.0090 0.0069 0.0047 1555 HOH A O 5582 O O . HOH V . ? 0.6841 0.6746 0.6843 0.0054 0.0091 -0.0014 1556 HOH A O 5583 O O . HOH V . ? 0.6052 0.6014 0.6045 0.0027 0.0036 0.0157 1557 HOH A O 5584 O O . HOH V . ? 0.7085 0.6886 0.7085 -0.0036 0.0065 0.0015 1558 HOH A O 5585 O O . HOH V . ? 0.8040 0.7945 0.7878 0.0092 0.0041 -0.0011 1559 HOH A O 5586 O O . HOH V . ? 0.8158 0.8331 0.8291 0.0047 -0.0028 -0.0018 1560 HOH A O 5587 O O . HOH V . ? 0.6860 0.6890 0.6882 0.0036 -0.0002 0.0091 1561 HOH A O 5588 O O . HOH V . ? 0.7321 0.7246 0.7246 -0.0048 -0.0065 0.0042 1562 HOH A O 5589 O O . HOH V . ? 0.8362 0.8434 0.8302 0.0008 0.0005 -0.0057 1563 HOH A O 5590 O O . HOH V . ? 0.7052 0.7265 0.7057 0.0029 0.0013 0.0063 1564 HOH A O 5591 O O . HOH V . ? 0.6828 0.6899 0.6850 -0.0002 -0.0044 -0.0011 1565 HOH A O 5592 O O . HOH V . ? 0.8380 0.8291 0.8209 0.0025 0.0017 -0.0005 1566 HOH A O 5593 O O . HOH V . ? 1.4809 1.4738 1.4796 0.0006 0.0017 0.0004 1567 HOH A O 5594 O O . HOH V . ? 0.9077 0.8960 0.9156 -0.0071 0.0038 0.0016 1568 HOH A O 5595 O O . HOH V . ? 0.9204 0.9151 0.9169 -0.0030 0.0015 0.0001 1569 HOH A O 5596 O O . HOH V . ? 0.7420 0.7300 0.7358 0.0020 0.0028 0.0103 1570 HOH A O 5597 O O . HOH V . ? 0.6850 0.7046 0.7006 -0.0006 0.0033 0.0004 1571 HOH A O 5598 O O . HOH V . ? 0.6879 0.6840 0.6646 -0.0009 -0.0083 -0.0003 1572 HOH A O 5599 O O . HOH V . ? 0.5699 0.5933 0.5618 -0.0181 0.0237 -0.0045 1573 HOH A O 5600 O O . HOH V . ? 0.6179 0.6589 0.6450 -0.0173 0.0057 -0.0040 1574 HOH A O 5601 O O . HOH V . ? 0.7082 0.7268 0.7070 0.0042 0.0011 -0.0059 1575 HOH A O 5602 O O . HOH V . ? 0.6556 0.6632 0.6671 -0.0147 0.0070 0.0011 1576 HOH A O 5603 O O . HOH V . ? 0.9258 0.9280 0.9152 0.0003 -0.0035 0.0000 1577 HOH A O 5604 O O . HOH V . ? 0.6303 0.6064 0.6378 -0.0151 0.0076 0.0011 1578 HOH A O 5605 O O . HOH V . ? 0.5583 0.5797 0.6153 -0.0006 0.0036 0.0047 1579 HOH A O 5606 O O . HOH V . ? 1.0072 1.0061 1.0095 -0.0037 0.0000 0.0055 1580 HOH A O 5607 O O . HOH V . ? 0.4301 0.4073 0.4155 -0.0055 -0.0472 -0.0081 1581 HOH A O 5608 O O . HOH V . ? 0.6222 0.6264 0.6085 0.0036 -0.0064 -0.0084 1582 HOH A O 5609 O O . HOH V . ? 0.7299 0.7589 0.7442 -0.0002 0.0024 0.0023 1583 HOH A O 5610 O O . HOH V . ? 0.7472 0.7593 0.7584 -0.0035 0.0005 0.0038 1584 HOH A O 5611 O O . HOH V . ? 0.5532 0.5658 0.5442 0.0071 -0.0184 0.0065 1585 HOH A O 5612 O O . HOH V . ? 0.6463 0.6659 0.6677 -0.0073 -0.0065 -0.0019 1586 HOH A O 5613 O O . HOH V . ? 0.5508 0.5929 0.6110 0.0007 0.0019 0.0020 1587 HOH A O 5614 O O . HOH V . ? 0.8471 0.8448 0.8460 -0.0058 0.0034 0.0024 1588 HOH A O 5615 O O . HOH V . ? 0.9186 0.9273 0.9256 -0.0032 0.0025 -0.0034 1589 HOH A O 5616 O O . HOH V . ? 0.4764 0.5214 0.5435 0.0202 0.0068 -0.0131 1590 HOH A O 5617 O O . HOH V . ? 0.6088 0.5818 0.5729 0.0234 -0.0079 0.0034 1591 HOH A O 5618 O O . HOH V . ? 0.6210 0.5752 0.5608 -0.0203 0.0169 0.0173 1592 HOH A O 5619 O O . HOH V . ? 0.6234 0.6263 0.6237 -0.0186 0.0000 -0.0065 1593 HOH A O 5620 O O . HOH V . ? 0.6933 0.6726 0.6532 0.0016 0.0040 -0.0038 1594 HOH A O 5621 O O . HOH V . ? 0.5597 0.5608 0.5971 0.0027 -0.0016 -0.0017 1595 HOH A O 5622 O O . HOH V . ? 0.6438 0.6759 0.6912 0.0019 0.0020 0.0038 1596 HOH A O 5623 O O . HOH V . ? 0.7334 0.7327 0.7514 0.0075 -0.0052 0.0111 1597 HOH A O 5624 O O . HOH V . ? 0.6504 0.6547 0.6850 -0.0063 0.0071 0.0059 1598 HOH A O 5625 O O . HOH V . ? 0.6404 0.6263 0.5905 0.0101 0.0022 -0.0021 1599 HOH A O 5626 O O . HOH V . ? 0.8561 0.8329 0.8397 -0.0033 -0.0009 0.0068 1600 HOH A O 5627 O O . HOH V . ? 0.5867 0.5703 0.5768 -0.0034 -0.0157 -0.0065 1601 HOH A O 5628 O O . HOH V . ? 0.5954 0.6093 0.5847 -0.0036 -0.0077 -0.0111 1602 HOH A O 5629 O O . HOH V . ? 0.9968 0.9948 0.9912 -0.0023 0.0002 -0.0022 1603 HOH A O 5630 O O . HOH V . ? 0.5988 0.6426 0.6288 0.0039 0.0090 0.0025 1604 HOH A O 5631 O O . HOH V . ? 0.7039 0.6936 0.7138 0.0086 -0.0018 0.0048 1605 HOH A O 5632 O O . HOH V . ? 0.5281 0.5405 0.5366 -0.0039 0.0049 -0.0083 1606 HOH A O 5633 O O . HOH V . ? 0.7748 0.7893 0.7927 -0.0013 0.0006 0.0018 1607 HOH A O 5634 O O . HOH V . ? 0.6612 0.6713 0.6617 -0.0024 -0.0048 0.0023 1608 HOH A O 5635 O O . HOH V . ? 0.5949 0.5893 0.5794 -0.0112 0.0101 -0.0009 1609 HOH A O 5636 O O . HOH V . ? 0.7008 0.6832 0.7044 -0.0052 0.0099 -0.0085 1610 HOH A O 5637 O O . HOH V . ? 0.6630 0.6723 0.6555 0.0080 0.0083 0.0061 1611 HOH A O 5638 O O . HOH V . ? 0.7604 0.7457 0.7324 -0.0022 -0.0058 -0.0031 1612 HOH A O 5639 O O . HOH V . ? 0.7924 0.7982 0.8003 -0.0003 0.0035 0.0103 1613 HOH A O 5640 O O . HOH V . ? 0.6778 0.7057 0.6996 -0.0036 0.0050 0.0040 1614 HOH A O 5641 O O . HOH V . ? 0.6933 0.6934 0.6678 -0.0010 -0.0052 -0.0012 1615 HOH A O 5642 O O . HOH V . ? 0.7399 0.7481 0.7224 0.0087 -0.0006 0.0026 1616 HOH A O 5643 O O . HOH V . ? 0.7046 0.6931 0.7073 -0.0072 -0.0051 0.0012 1617 HOH A O 5644 O O . HOH V . ? 0.7556 0.7537 0.7652 0.0092 0.0039 -0.0059 1618 HOH A O 5645 O O . HOH V . ? 0.6441 0.6464 0.6270 -0.0014 -0.0006 0.0052 1619 HOH A O 5646 O O . HOH V . ? 0.9112 0.8960 0.9130 -0.0051 0.0001 -0.0014 1620 HOH A O 5647 O O . HOH V . ? 0.7706 0.7882 0.7809 0.0016 0.0018 -0.0029 1621 HOH A O 5648 O O . HOH V . ? 0.7558 0.7477 0.7630 0.0019 0.0023 -0.0023 1622 HOH A O 5649 O O . HOH V . ? 0.9022 0.9012 0.9047 0.0054 0.0004 0.0020 1623 HOH A O 5650 O O . HOH V . ? 0.7781 0.7648 0.7636 -0.0027 0.0042 -0.0041 1624 HOH A O 5651 O O . HOH V . ? 0.9751 0.9801 0.9732 0.0005 -0.0015 0.0008 1625 HOH A O 5652 O O . HOH V . ? 0.8216 0.8331 0.8302 -0.0009 0.0011 0.0018 1626 HOH A O 5653 O O . HOH V . ? 0.7091 0.7092 0.7063 -0.0006 -0.0029 -0.0073 1627 HOH A O 5654 O O . HOH V . ? 0.5594 0.5762 0.5744 -0.0116 -0.0038 -0.0111 1628 HOH A O 5655 O O . HOH V . ? 0.8283 0.8345 0.8375 0.0085 -0.0041 -0.0002 1629 HOH A O 5656 O O . HOH V . ? 0.5653 0.5912 0.5836 0.0109 -0.0098 -0.0060 1630 HOH A O # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'BMA 703, NAG 705, BMA 706, FUL 707 HAVE LOW CORRELATION AND (OR) HIGH REAL SPACE R VALUE.' # 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 ASP 1 1 1 ASP ASP A . n A 1 2 TYR 2 2 2 TYR TYR A . n A 1 3 VAL 3 3 3 VAL VAL A . n A 1 4 LEU 4 4 4 LEU LEU A . n A 1 5 TYR 5 5 5 TYR TYR A . n A 1 6 LYS 6 6 6 LYS LYS A . n A 1 7 ASP 7 7 7 ASP ASP A . n A 1 8 ALA 8 8 8 ALA ALA A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 LYS 10 10 10 LYS LYS A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 VAL 12 12 12 VAL VAL A . n A 1 13 GLU 13 13 13 GLU GLU A . n A 1 14 ASP 14 14 14 ASP ASP A . n A 1 15 ARG 15 15 15 ARG ARG A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ALA 17 17 17 ALA ALA A . n A 1 18 ASP 18 18 18 ASP ASP A . n A 1 19 LEU 19 19 19 LEU LEU A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 GLY 21 21 21 GLY GLY A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 MET 23 23 23 MET MET A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 LEU 25 25 25 LEU LEU A . n A 1 26 ALA 26 26 26 ALA ALA A . n A 1 27 GLU 27 27 27 GLU GLU A . n A 1 28 LYS 28 28 28 LYS LYS A . n A 1 29 ILE 29 29 29 ILE ILE A . n A 1 30 GLY 30 30 30 GLY GLY A . n A 1 31 GLN 31 31 31 GLN GLN A . n A 1 32 MET 32 32 32 MET MET A . n A 1 33 THR 33 33 33 THR THR A . n A 1 34 GLN 34 34 34 GLN GLN A . n A 1 35 ILE 35 35 35 ILE ILE A . n A 1 36 GLU 36 36 36 GLU GLU A . n A 1 37 ARG 37 37 37 ARG ARG A . n A 1 38 LEU 38 38 38 LEU LEU A . n A 1 39 VAL 39 39 39 VAL VAL A . n A 1 40 ALA 40 40 40 ALA ALA A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 PRO 42 42 42 PRO PRO A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 VAL 44 44 44 VAL VAL A . n A 1 45 LEU 45 45 45 LEU LEU A . n A 1 46 ARG 46 46 46 ARG ARG A . n A 1 47 ASP 47 47 47 ASP ASP A . n A 1 48 ASN 48 48 48 ASN ASN A . n A 1 49 PHE 49 49 49 PHE PHE A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 GLY 51 51 51 GLY GLY A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 LEU 53 53 53 LEU LEU A . n A 1 54 LEU 54 54 54 LEU LEU A . n A 1 55 SER 55 55 55 SER SER A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 SER 59 59 59 SER SER A . n A 1 60 VAL 60 60 60 VAL VAL A . n A 1 61 PRO 61 61 61 PRO PRO A . n A 1 62 ARG 62 62 62 ARG ARG A . n A 1 63 LYS 63 63 63 LYS LYS A . n A 1 64 GLY 64 64 64 GLY GLY A . n A 1 65 ALA 65 65 65 ALA ALA A . n A 1 66 THR 66 66 66 THR THR A . n A 1 67 ALA 67 67 67 ALA ALA A . n A 1 68 LYS 68 68 68 LYS LYS A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 TRP 70 70 70 TRP TRP A . n A 1 71 GLN 71 71 71 GLN GLN A . n A 1 72 ASP 72 72 72 ASP ASP A . n A 1 73 MET 73 73 73 MET MET A . n A 1 74 VAL 74 74 74 VAL VAL A . n A 1 75 ASP 75 75 75 ASP ASP A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 PHE 77 77 77 PHE PHE A . n A 1 78 GLN 78 78 78 GLN GLN A . n A 1 79 LYS 79 79 79 LYS LYS A . n A 1 80 ALA 80 80 80 ALA ALA A . n A 1 81 CYS 81 81 81 CYS CYS A . n A 1 82 MET 82 82 82 MET MET A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 THR 84 84 84 THR THR A . n A 1 85 ARG 85 85 85 ARG ARG A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 GLY 87 87 87 GLY GLY A . n A 1 88 ILE 88 88 88 ILE ILE A . n A 1 89 PRO 89 89 89 PRO PRO A . n A 1 90 MET 90 90 90 MET MET A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 TYR 92 92 92 TYR TYR A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ILE 94 94 94 ILE ILE A . n A 1 95 ASP 95 95 95 ASP ASP A . n A 1 96 ALA 96 96 96 ALA ALA A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 HIS 98 98 98 HIS HIS A . n A 1 99 GLY 99 99 99 GLY GLY A . n A 1 100 GLN 100 100 100 GLN GLN A . n A 1 101 ASN 101 101 101 ASN ASN A . n A 1 102 ASN 102 102 102 ASN ASN A . n A 1 103 VAL 103 103 103 VAL VAL A . n A 1 104 TYR 104 104 104 TYR TYR A . n A 1 105 GLY 105 105 105 GLY GLY A . n A 1 106 ALA 106 106 106 ALA ALA A . n A 1 107 THR 107 107 107 THR THR A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 PHE 109 109 109 PHE PHE A . n A 1 110 PRO 110 110 110 PRO PRO A . n A 1 111 HIS 111 111 111 HIS HIS A . n A 1 112 ASN 112 112 112 ASN ASN A . n A 1 113 VAL 113 113 113 VAL VAL A . n A 1 114 GLY 114 114 114 GLY GLY A . n A 1 115 LEU 115 115 115 LEU LEU A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 ALA 117 117 117 ALA ALA A . n A 1 118 THR 118 118 118 THR THR A . n A 1 119 ARG 119 119 119 ARG ARG A . n A 1 120 ASP 120 120 120 ASP ASP A . n A 1 121 PRO 121 121 121 PRO PRO A . n A 1 122 TYR 122 122 122 TYR TYR A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 VAL 124 124 124 VAL VAL A . n A 1 125 LYS 125 125 125 LYS LYS A . n A 1 126 ARG 126 126 126 ARG ARG A . n A 1 127 ILE 127 127 127 ILE ILE A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 GLU 129 129 129 GLU GLU A . n A 1 130 ALA 130 130 130 ALA ALA A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 ALA 132 132 132 ALA ALA A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 VAL 135 135 135 VAL VAL A . n A 1 136 ARG 136 136 136 ARG ARG A . n A 1 137 ALA 137 137 137 ALA ALA A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 ILE 140 140 140 ILE ILE A . n A 1 141 GLN 141 141 141 GLN GLN A . n A 1 142 TYR 142 142 142 TYR TYR A . n A 1 143 ALA 143 143 143 ALA ALA A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ALA 145 145 145 ALA ALA A . n A 1 146 PRO 146 146 146 PRO PRO A . n A 1 147 CYS 147 147 147 CYS CYS A . n A 1 148 ILE 148 148 148 ILE ILE A . n A 1 149 ALA 149 149 149 ALA ALA A . n A 1 150 VAL 150 150 150 VAL VAL A . n A 1 151 CYS 151 151 151 CYS CYS A . n A 1 152 ARG 152 152 152 ARG ARG A . n A 1 153 ASP 153 153 153 ASP ASP A . n A 1 154 PRO 154 154 154 PRO PRO A . n A 1 155 ARG 155 155 155 ARG ARG A . n A 1 156 TRP 156 156 156 TRP TRP A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 ARG 158 158 158 ARG ARG A . n A 1 159 CYS 159 159 159 CYS CYS A . n A 1 160 TYR 160 160 160 TYR TYR A . n A 1 161 GLU 161 161 161 GLU GLU A . n A 1 162 SER 162 162 162 SER SER A . n A 1 163 TYR 163 163 163 TYR TYR A . n A 1 164 SER 164 164 164 SER SER A . n A 1 165 GLU 165 165 165 GLU GLU A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 ARG 167 167 167 ARG ARG A . n A 1 168 ARG 168 168 168 ARG ARG A . n A 1 169 ILE 169 169 169 ILE ILE A . n A 1 170 VAL 170 170 170 VAL VAL A . n A 1 171 GLN 171 171 171 GLN GLN A . n A 1 172 SER 172 172 172 SER SER A . n A 1 173 MET 173 173 173 MET MET A . n A 1 174 THR 174 174 174 THR THR A . n A 1 175 GLU 175 175 175 GLU GLU A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 ILE 177 177 177 ILE ILE A . n A 1 178 PRO 178 178 178 PRO PRO A . n A 1 179 GLY 179 179 179 GLY GLY A . n A 1 180 LEU 180 180 180 LEU LEU A . n A 1 181 GLN 181 181 181 GLN GLN A . n A 1 182 GLY 182 182 182 GLY GLY A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 VAL 184 184 184 VAL VAL A . n A 1 185 PRO 185 185 185 PRO PRO A . n A 1 186 LYS 186 186 186 LYS LYS A . n A 1 187 ASP 187 187 187 ASP ASP A . n A 1 188 PHE 188 188 188 PHE PHE A . n A 1 189 THR 189 189 189 THR THR A . n A 1 190 SER 190 190 190 SER SER A . n A 1 191 GLY 191 191 191 GLY GLY A . n A 1 192 MET 192 192 192 MET MET A . n A 1 193 PRO 193 193 193 PRO PRO A . n A 1 194 PHE 194 194 194 PHE PHE A . n A 1 195 VAL 195 195 195 VAL VAL A . n A 1 196 ALA 196 196 196 ALA ALA A . n A 1 197 GLY 197 197 197 GLY GLY A . n A 1 198 LYS 198 198 198 LYS LYS A . n A 1 199 ASN 199 199 199 ASN ASN A . n A 1 200 LYS 200 200 200 LYS LYS A . n A 1 201 VAL 201 201 201 VAL VAL A . n A 1 202 ALA 202 202 202 ALA ALA A . n A 1 203 ALA 203 203 203 ALA ALA A . n A 1 204 CYS 204 204 204 CYS CYS A . n A 1 205 ALA 205 205 205 ALA ALA A . n A 1 206 LYS 206 206 206 LYS LYS A . n A 1 207 HIS 207 207 207 HIS HIS A . n A 1 208 PHE 208 208 208 PHE PHE A . n A 1 209 VAL 209 209 209 VAL VAL A . n A 1 210 GLY 210 210 210 GLY GLY A . n A 1 211 ASP 211 211 211 ASP ASP A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 GLY 213 213 213 GLY GLY A . n A 1 214 THR 214 214 214 THR THR A . n A 1 215 VAL 215 215 215 VAL VAL A . n A 1 216 ASP 216 216 216 ASP ASP A . n A 1 217 GLY 217 217 217 GLY GLY A . n A 1 218 ILE 218 218 218 ILE ILE A . n A 1 219 ASN 219 219 219 ASN ASN A . n A 1 220 GLU 220 220 220 GLU GLU A . n A 1 221 ASN 221 221 221 ASN ASN A . n A 1 222 ASN 222 222 222 ASN ASN A . n A 1 223 THR 223 223 223 THR THR A . n A 1 224 ILE 224 224 224 ILE ILE A . n A 1 225 ILE 225 225 225 ILE ILE A . n A 1 226 ASN 226 226 226 ASN ASN A . n A 1 227 ARG 227 227 227 ARG ARG A . n A 1 228 GLU 228 228 228 GLU GLU A . n A 1 229 GLY 229 229 229 GLY GLY A . n A 1 230 LEU 230 230 230 LEU LEU A . n A 1 231 MET 231 231 231 MET MET A . n A 1 232 ASN 232 232 232 ASN ASN A . n A 1 233 ILE 233 233 233 ILE ILE A . n A 1 234 HIS 234 234 234 HIS HIS A . n A 1 235 MET 235 235 235 MET MET A . n A 1 236 PRO 236 236 236 PRO PRO A . n A 1 237 ALA 237 237 237 ALA ALA A . n A 1 238 TYR 238 238 238 TYR TYR A . n A 1 239 LYS 239 239 239 LYS LYS A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 ALA 241 241 241 ALA ALA A . n A 1 242 MET 242 242 242 MET MET A . n A 1 243 ASP 243 243 243 ASP ASP A . n A 1 244 LYS 244 244 244 LYS LYS A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 VAL 246 246 246 VAL VAL A . n A 1 247 SER 247 247 247 SER SER A . n A 1 248 THR 248 248 248 THR THR A . n A 1 249 VAL 249 249 249 VAL VAL A . n A 1 250 MET 250 250 250 MET MET A . n A 1 251 ILE 251 251 251 ILE ILE A . n A 1 252 SER 252 252 252 SER SER A . n A 1 253 TYR 253 253 253 TYR TYR A . n A 1 254 SER 254 254 254 SER SER A . n A 1 255 SER 255 255 255 SER SER A . n A 1 256 TRP 256 256 256 TRP TRP A . n A 1 257 ASN 257 257 257 ASN ASN A . n A 1 258 GLY 258 258 258 GLY GLY A . n A 1 259 VAL 259 259 259 VAL VAL A . n A 1 260 LYS 260 260 260 LYS LYS A . n A 1 261 MET 261 261 261 MET MET A . n A 1 262 HIS 262 262 262 HIS HIS A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 ASN 264 264 264 ASN ASN A . n A 1 265 GLN 265 265 265 GLN GLN A . n A 1 266 ASP 266 266 266 ASP ASP A . n A 1 267 LEU 267 267 267 LEU LEU A . n A 1 268 VAL 268 268 268 VAL VAL A . n A 1 269 THR 269 269 269 THR THR A . n A 1 270 GLY 270 270 270 GLY GLY A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 LYS 273 273 273 LYS LYS A . n A 1 274 ASP 274 274 274 ASP ASP A . n A 1 275 THR 275 275 275 THR THR A . n A 1 276 LEU 276 276 276 LEU LEU A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 PHE 278 278 278 PHE PHE A . n A 1 279 LYS 279 279 279 LYS LYS A . n A 1 280 GLY 280 280 280 GLY GLY A . n A 1 281 PHE 281 281 281 PHE PHE A . n A 1 282 VAL 282 282 282 VAL VAL A . n A 1 283 ILE 283 283 283 ILE ILE A . n A 1 284 SER 284 284 284 SER SER A . n A 1 285 ASP 285 285 285 ASP ASP A . n A 1 286 TRP 286 286 286 TRP TRP A . n A 1 287 GLU 287 287 287 GLU GLU A . n A 1 288 GLY 288 288 288 GLY GLY A . n A 1 289 ILE 289 289 289 ILE ILE A . n A 1 290 ASP 290 290 290 ASP ASP A . n A 1 291 ARG 291 291 291 ARG ARG A . n A 1 292 ILE 292 292 292 ILE ILE A . n A 1 293 THR 293 293 293 THR THR A . n A 1 294 THR 294 294 294 THR THR A . n A 1 295 PRO 295 295 295 PRO PRO A . n A 1 296 ALA 296 296 296 ALA ALA A . n A 1 297 GLY 297 297 297 GLY GLY A . n A 1 298 SER 298 298 298 SER SER A . n A 1 299 ASP 299 299 299 ASP ASP A . n A 1 300 TYR 300 300 300 TYR TYR A . n A 1 301 SER 301 301 301 SER SER A . n A 1 302 TYR 302 302 302 TYR TYR A . n A 1 303 SER 303 303 303 SER SER A . n A 1 304 VAL 304 304 304 VAL VAL A . n A 1 305 LYS 305 305 305 LYS LYS A . n A 1 306 ALA 306 306 306 ALA ALA A . n A 1 307 SER 307 307 307 SER SER A . n A 1 308 ILE 308 308 308 ILE ILE A . n A 1 309 LEU 309 309 309 LEU LEU A . n A 1 310 ALA 310 310 310 ALA ALA A . n A 1 311 GLY 311 311 311 GLY GLY A . n A 1 312 LEU 312 312 312 LEU LEU A . n A 1 313 ASP 313 313 313 ASP ASP A . n A 1 314 MET 314 314 314 MET MET A . n A 1 315 ILE 315 315 315 ILE ILE A . n A 1 316 MET 316 316 316 MET MET A . n A 1 317 VAL 317 317 317 VAL VAL A . n A 1 318 PRO 318 318 318 PRO PRO A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 LYS 320 320 320 LYS LYS A . n A 1 321 TYR 321 321 321 TYR TYR A . n A 1 322 GLN 322 322 322 GLN GLN A . n A 1 323 GLN 323 323 323 GLN GLN A . n A 1 324 PHE 324 324 324 PHE PHE A . n A 1 325 ILE 325 325 325 ILE ILE A . n A 1 326 SER 326 326 326 SER SER A . n A 1 327 ILE 327 327 327 ILE ILE A . n A 1 328 LEU 328 328 328 LEU LEU A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 GLY 330 330 330 GLY GLY A . n A 1 331 HIS 331 331 331 HIS HIS A . n A 1 332 VAL 332 332 332 VAL VAL A . n A 1 333 ASN 333 333 333 ASN ASN A . n A 1 334 GLY 334 334 334 GLY GLY A . n A 1 335 GLY 335 335 335 GLY GLY A . n A 1 336 VAL 336 336 336 VAL VAL A . n A 1 337 ILE 337 337 337 ILE ILE A . n A 1 338 PRO 338 338 338 PRO PRO A . n A 1 339 MET 339 339 339 MET MET A . n A 1 340 SER 340 340 340 SER SER A . n A 1 341 ARG 341 341 341 ARG ARG A . n A 1 342 ILE 342 342 342 ILE ILE A . n A 1 343 ASP 343 343 343 ASP ASP A . n A 1 344 ASP 344 344 344 ASP ASP A . n A 1 345 ALA 345 345 345 ALA ALA A . n A 1 346 VAL 346 346 346 VAL VAL A . n A 1 347 THR 347 347 347 THR THR A . n A 1 348 ARG 348 348 348 ARG ARG A . n A 1 349 ILE 349 349 349 ILE ILE A . n A 1 350 LEU 350 350 350 LEU LEU A . n A 1 351 ARG 351 351 351 ARG ARG A . n A 1 352 VAL 352 352 352 VAL VAL A . n A 1 353 LYS 353 353 353 LYS LYS A . n A 1 354 PHE 354 354 354 PHE PHE A . n A 1 355 THR 355 355 355 THR THR A . n A 1 356 MET 356 356 356 MET MET A . n A 1 357 GLY 357 357 357 GLY GLY A . n A 1 358 LEU 358 358 358 LEU LEU A . n A 1 359 PHE 359 359 359 PHE PHE A . n A 1 360 GLU 360 360 360 GLU GLU A . n A 1 361 ASN 361 361 361 ASN ASN A . n A 1 362 PRO 362 362 362 PRO PRO A . n A 1 363 TYR 363 363 363 TYR TYR A . n A 1 364 ALA 364 364 364 ALA ALA A . n A 1 365 ASP 365 365 365 ASP ASP A . n A 1 366 PRO 366 366 366 PRO PRO A . n A 1 367 ALA 367 367 367 ALA ALA A . n A 1 368 MET 368 368 368 MET MET A . n A 1 369 ALA 369 369 369 ALA ALA A . n A 1 370 GLU 370 370 370 GLU GLU A . n A 1 371 GLN 371 371 371 GLN GLN A . n A 1 372 LEU 372 372 372 LEU LEU A . n A 1 373 GLY 373 373 373 GLY GLY A . n A 1 374 LYS 374 374 374 LYS LYS A . n A 1 375 GLN 375 375 375 GLN GLN A . n A 1 376 GLU 376 376 376 GLU GLU A . n A 1 377 HIS 377 377 377 HIS HIS A . n A 1 378 ARG 378 378 378 ARG ARG A . n A 1 379 ASP 379 379 379 ASP ASP A . n A 1 380 LEU 380 380 380 LEU LEU A . n A 1 381 ALA 381 381 381 ALA ALA A . n A 1 382 ARG 382 382 382 ARG ARG A . n A 1 383 GLU 383 383 383 GLU GLU A . n A 1 384 ALA 384 384 384 ALA ALA A . n A 1 385 ALA 385 385 385 ALA ALA A . n A 1 386 ARG 386 386 386 ARG ARG A . n A 1 387 LYS 387 387 387 LYS LYS A . n A 1 388 SER 388 388 388 SER SER A . n A 1 389 LEU 389 389 389 LEU LEU A . n A 1 390 VAL 390 390 390 VAL VAL A . n A 1 391 LEU 391 391 391 LEU LEU A . n A 1 392 LEU 392 392 392 LEU LEU A . n A 1 393 LYS 393 393 393 LYS LYS A . n A 1 394 ASN 394 394 394 ASN ASN A . n A 1 395 GLY 395 395 395 GLY GLY A . n A 1 396 LYS 396 396 396 LYS LYS A . n A 1 397 THR 397 397 397 THR THR A . n A 1 398 SER 398 398 398 SER SER A . n A 1 399 THR 399 399 399 THR THR A . n A 1 400 ASP 400 400 400 ASP ASP A . n A 1 401 ALA 401 401 401 ALA ALA A . n A 1 402 PRO 402 402 402 PRO PRO A . n A 1 403 LEU 403 403 403 LEU LEU A . n A 1 404 LEU 404 404 404 LEU LEU A . n A 1 405 PRO 405 405 405 PRO PRO A . n A 1 406 LEU 406 406 406 LEU LEU A . n A 1 407 PRO 407 407 407 PRO PRO A . n A 1 408 LYS 408 408 408 LYS LYS A . n A 1 409 LYS 409 409 409 LYS LYS A . n A 1 410 ALA 410 410 410 ALA ALA A . n A 1 411 PRO 411 411 411 PRO PRO A . n A 1 412 LYS 412 412 412 LYS LYS A . n A 1 413 ILE 413 413 413 ILE ILE A . n A 1 414 LEU 414 414 414 LEU LEU A . n A 1 415 VAL 415 415 415 VAL VAL A . n A 1 416 ALA 416 416 416 ALA ALA A . n A 1 417 GLY 417 417 417 GLY GLY A . n A 1 418 SER 418 418 418 SER SER A . n A 1 419 HIS 419 419 419 HIS HIS A . n A 1 420 ALA 420 420 420 ALA ALA A . n A 1 421 ASP 421 421 421 ASP ASP A . n A 1 422 ASN 422 422 422 ASN ASN A . n A 1 423 LEU 423 423 423 LEU LEU A . n A 1 424 GLY 424 424 424 GLY GLY A . n A 1 425 TYR 425 425 425 TYR TYR A . n A 1 426 GLN 426 426 426 GLN GLN A . n A 1 427 CYS 427 427 427 CYS CYS A . n A 1 428 GLY 428 428 428 GLY GLY A . n A 1 429 GLY 429 429 429 GLY GLY A . n A 1 430 TRP 430 430 430 TRP TRP A . n A 1 431 THR 431 431 431 THR THR A . n A 1 432 ILE 432 432 432 ILE ILE A . n A 1 433 GLU 433 433 433 GLU GLU A . n A 1 434 TRP 434 434 434 TRP TRP A . n A 1 435 GLN 435 435 435 GLN GLN A . n A 1 436 GLY 436 436 436 GLY GLY A . n A 1 437 ASP 437 437 437 ASP ASP A . n A 1 438 THR 438 438 438 THR THR A . n A 1 439 GLY 439 439 439 GLY GLY A . n A 1 440 ARG 440 440 440 ARG ARG A . n A 1 441 THR 441 441 441 THR THR A . n A 1 442 THR 442 442 442 THR THR A . n A 1 443 VAL 443 443 443 VAL VAL A . n A 1 444 GLY 444 444 444 GLY GLY A . n A 1 445 THR 445 445 445 THR THR A . n A 1 446 THR 446 446 446 THR THR A . n A 1 447 ILE 447 447 447 ILE ILE A . n A 1 448 LEU 448 448 448 LEU LEU A . n A 1 449 GLU 449 449 449 GLU GLU A . n A 1 450 ALA 450 450 450 ALA ALA A . n A 1 451 VAL 451 451 451 VAL VAL A . n A 1 452 LYS 452 452 452 LYS LYS A . n A 1 453 ALA 453 453 453 ALA ALA A . n A 1 454 ALA 454 454 454 ALA ALA A . n A 1 455 VAL 455 455 455 VAL VAL A . n A 1 456 ASP 456 456 456 ASP ASP A . n A 1 457 PRO 457 457 457 PRO PRO A . n A 1 458 SER 458 458 458 SER SER A . n A 1 459 THR 459 459 459 THR THR A . n A 1 460 VAL 460 460 460 VAL VAL A . n A 1 461 VAL 461 461 461 VAL VAL A . n A 1 462 VAL 462 462 462 VAL VAL A . n A 1 463 PHE 463 463 463 PHE PHE A . n A 1 464 ALA 464 464 464 ALA ALA A . n A 1 465 GLU 465 465 465 GLU GLU A . n A 1 466 ASN 466 466 466 ASN ASN A . n A 1 467 PRO 467 467 467 PRO PRO A . n A 1 468 ASP 468 468 468 ASP ASP A . n A 1 469 ALA 469 469 469 ALA ALA A . n A 1 470 GLU 470 470 470 GLU GLU A . n A 1 471 PHE 471 471 471 PHE PHE A . n A 1 472 VAL 472 472 472 VAL VAL A . n A 1 473 LYS 473 473 473 LYS LYS A . n A 1 474 SER 474 474 474 SER SER A . n A 1 475 GLY 475 475 475 GLY GLY A . n A 1 476 GLY 476 476 476 GLY GLY A . n A 1 477 PHE 477 477 477 PHE PHE A . n A 1 478 SER 478 478 478 SER SER A . n A 1 479 TYR 479 479 479 TYR TYR A . n A 1 480 ALA 480 480 480 ALA ALA A . n A 1 481 ILE 481 481 481 ILE ILE A . n A 1 482 VAL 482 482 482 VAL VAL A . n A 1 483 ALA 483 483 483 ALA ALA A . n A 1 484 VAL 484 484 484 VAL VAL A . n A 1 485 GLY 485 485 485 GLY GLY A . n A 1 486 GLU 486 486 486 GLU GLU A . n A 1 487 HIS 487 487 487 HIS HIS A . n A 1 488 PRO 488 488 488 PRO PRO A . n A 1 489 TYR 489 489 489 TYR TYR A . n A 1 490 THR 490 490 490 THR THR A . n A 1 491 GLU 491 491 491 GLU GLU A . n A 1 492 THR 492 492 492 THR THR A . n A 1 493 LYS 493 493 493 LYS LYS A . n A 1 494 GLY 494 494 494 GLY GLY A . n A 1 495 ASP 495 495 495 ASP ASP A . n A 1 496 ASN 496 496 496 ASN ASN A . n A 1 497 LEU 497 497 497 LEU LEU A . n A 1 498 ASN 498 498 498 ASN ASN A . n A 1 499 LEU 499 499 499 LEU LEU A . n A 1 500 THR 500 500 500 THR THR A . n A 1 501 ILE 501 501 501 ILE ILE A . n A 1 502 PRO 502 502 502 PRO PRO A . n A 1 503 GLU 503 503 503 GLU GLU A . n A 1 504 PRO 504 504 504 PRO PRO A . n A 1 505 GLY 505 505 505 GLY GLY A . n A 1 506 LEU 506 506 506 LEU LEU A . n A 1 507 SER 507 507 507 SER SER A . n A 1 508 THR 508 508 508 THR THR A . n A 1 509 VAL 509 509 509 VAL VAL A . n A 1 510 GLN 510 510 510 GLN GLN A . n A 1 511 ALA 511 511 511 ALA ALA A . n A 1 512 VAL 512 512 512 VAL VAL A . n A 1 513 CYS 513 513 513 CYS CYS A . n A 1 514 GLY 514 514 514 GLY GLY A . n A 1 515 GLY 515 515 515 GLY GLY A . n A 1 516 VAL 516 516 516 VAL VAL A . n A 1 517 ARG 517 517 517 ARG ARG A . n A 1 518 CYS 518 518 518 CYS CYS A . n A 1 519 ALA 519 519 519 ALA ALA A . n A 1 520 THR 520 520 520 THR THR A . n A 1 521 VAL 521 521 521 VAL VAL A . n A 1 522 LEU 522 522 522 LEU LEU A . n A 1 523 ILE 523 523 523 ILE ILE A . n A 1 524 SER 524 524 524 SER SER A . n A 1 525 GLY 525 525 525 GLY GLY A . n A 1 526 ARG 526 526 526 ARG ARG A . n A 1 527 PRO 527 527 527 PRO PRO A . n A 1 528 VAL 528 528 528 VAL VAL A . n A 1 529 VAL 529 529 529 VAL VAL A . n A 1 530 VAL 530 530 530 VAL VAL A . n A 1 531 GLN 531 531 531 GLN GLN A . n A 1 532 PRO 532 532 532 PRO PRO A . n A 1 533 LEU 533 533 533 LEU LEU A . n A 1 534 LEU 534 534 534 LEU LEU A . n A 1 535 ALA 535 535 535 ALA ALA A . n A 1 536 ALA 536 536 536 ALA ALA A . n A 1 537 SER 537 537 537 SER SER A . n A 1 538 ASP 538 538 538 ASP ASP A . n A 1 539 ALA 539 539 539 ALA ALA A . n A 1 540 LEU 540 540 540 LEU LEU A . n A 1 541 VAL 541 541 541 VAL VAL A . n A 1 542 ALA 542 542 542 ALA ALA A . n A 1 543 ALA 543 543 543 ALA ALA A . n A 1 544 TRP 544 544 544 TRP TRP A . n A 1 545 LEU 545 545 545 LEU LEU A . n A 1 546 PRO 546 546 546 PRO PRO A . n A 1 547 GLY 547 547 547 GLY GLY A . n A 1 548 SER 548 548 548 SER SER A . n A 1 549 GLU 549 549 549 GLU GLU A . n A 1 550 GLY 550 550 550 GLY GLY A . n A 1 551 GLN 551 551 551 GLN GLN A . n A 1 552 GLY 552 552 552 GLY GLY A . n A 1 553 VAL 553 553 553 VAL VAL A . n A 1 554 THR 554 554 554 THR THR A . n A 1 555 ASP 555 555 555 ASP ASP A . n A 1 556 ALA 556 556 556 ALA ALA A . n A 1 557 LEU 557 557 557 LEU LEU A . n A 1 558 PHE 558 558 558 PHE PHE A . n A 1 559 GLY 559 559 559 GLY GLY A . n A 1 560 ASP 560 560 560 ASP ASP A . n A 1 561 PHE 561 561 561 PHE PHE A . n A 1 562 GLY 562 562 562 GLY GLY A . n A 1 563 PHE 563 563 563 PHE PHE A . n A 1 564 THR 564 564 564 THR THR A . n A 1 565 GLY 565 565 565 GLY GLY A . n A 1 566 ARG 566 566 566 ARG ARG A . n A 1 567 LEU 567 567 567 LEU LEU A . n A 1 568 PRO 568 568 568 PRO PRO A . n A 1 569 ARG 569 569 569 ARG ARG A . n A 1 570 THR 570 570 570 THR THR A . n A 1 571 TRP 571 571 571 TRP TRP A . n A 1 572 PHE 572 572 572 PHE PHE A . n A 1 573 LYS 573 573 573 LYS LYS A . n A 1 574 SER 574 574 574 SER SER A . n A 1 575 VAL 575 575 575 VAL VAL A . n A 1 576 ASP 576 576 576 ASP ASP A . n A 1 577 GLN 577 577 577 GLN GLN A . n A 1 578 LEU 578 578 578 LEU LEU A . n A 1 579 PRO 579 579 579 PRO PRO A . n A 1 580 MET 580 580 580 MET MET A . n A 1 581 ASN 581 581 581 ASN ASN A . n A 1 582 VAL 582 582 582 VAL VAL A . n A 1 583 GLY 583 583 583 GLY GLY A . n A 1 584 ASP 584 584 584 ASP ASP A . n A 1 585 ALA 585 585 585 ALA ALA A . n A 1 586 HIS 586 586 586 HIS HIS A . n A 1 587 TYR 587 587 587 TYR TYR A . n A 1 588 ASP 588 588 588 ASP ASP A . n A 1 589 PRO 589 589 589 PRO PRO A . n A 1 590 LEU 590 590 590 LEU LEU A . n A 1 591 PHE 591 591 591 PHE PHE A . n A 1 592 ARG 592 592 592 ARG ARG A . n A 1 593 LEU 593 593 593 LEU LEU A . n A 1 594 GLY 594 594 594 GLY GLY A . n A 1 595 TYR 595 595 595 TYR TYR A . n A 1 596 GLY 596 596 596 GLY GLY A . n A 1 597 LEU 597 597 597 LEU LEU A . n A 1 598 THR 598 598 598 THR THR A . n A 1 599 THR 599 599 599 THR THR A . n A 1 600 ASN 600 600 600 ASN ASN A . n A 1 601 ALA 601 601 601 ALA ALA A . n A 1 602 THR 602 602 602 THR THR A . n A 1 603 LYS 603 603 ? ? ? A . n A 1 604 LYS 604 604 ? ? ? A . n A 1 605 TYR 605 605 ? ? ? A . 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 B 2 NAG 1 701 2211 NAG NAG A . C 2 NAG 2 702 2212 NAG NAG A . D 3 BMA 3 703 2213 BMA MAN A . E 2 NAG 1 704 4981 NAG NAG A . F 2 NAG 2 705 4982 NAG NAG A . G 3 BMA 3 706 4983 BMA MAN A . H 4 FUL 4 707 4984 FUL FCU A . I 5 MAN 5 708 4985 MAN MAN A . J 2 NAG 6 709 4986 NAG NAG A . K 2 NAG 1 710 6001 NAG NAG A . L 2 NAG 2 711 6002 NAG NAG A . M 3 BMA 3 712 6003 BMA MAN A . N 4 FUL 4 713 6004 FUL FCU A . O 6 XYP 5 714 6005 XYP XYS A . P 7 BGC 1 715 1 BGC GLC A . Q 8 3DO 1 716 2 3DO 3DO A . R 9 GOL 1 717 1 GOL GOL A . S 9 GOL 1 718 2 GOL GOL A . T 9 GOL 1 719 3 GOL GOL A . U 10 SO4 1 720 1 SO4 SO4 A . V 11 HOH 1 801 1 HOH HOH A . V 11 HOH 2 802 2 HOH HOH A . V 11 HOH 3 803 3 HOH HOH A . V 11 HOH 4 804 4 HOH HOH A . V 11 HOH 5 805 5 HOH HOH A . V 11 HOH 6 806 6 HOH HOH A . V 11 HOH 7 807 7 HOH HOH A . V 11 HOH 8 808 8 HOH HOH A . V 11 HOH 9 809 9 HOH HOH A . V 11 HOH 10 810 10 HOH HOH A . V 11 HOH 11 811 11 HOH HOH A . V 11 HOH 12 812 12 HOH HOH A . V 11 HOH 13 813 13 HOH HOH A . V 11 HOH 14 814 14 HOH HOH A . V 11 HOH 15 815 15 HOH HOH A . V 11 HOH 16 816 16 HOH HOH A . V 11 HOH 17 817 17 HOH HOH A . V 11 HOH 18 818 18 HOH HOH A . V 11 HOH 19 819 19 HOH HOH A . V 11 HOH 20 820 20 HOH HOH A . V 11 HOH 21 821 21 HOH HOH A . V 11 HOH 22 822 22 HOH HOH A . V 11 HOH 23 823 23 HOH HOH A . V 11 HOH 24 824 24 HOH HOH A . V 11 HOH 25 825 25 HOH HOH A . V 11 HOH 26 826 26 HOH HOH A . V 11 HOH 27 827 27 HOH HOH A . V 11 HOH 28 828 28 HOH HOH A . V 11 HOH 29 829 29 HOH HOH A . V 11 HOH 30 830 30 HOH HOH A . V 11 HOH 31 831 31 HOH HOH A . V 11 HOH 32 832 32 HOH HOH A . V 11 HOH 33 833 33 HOH HOH A . V 11 HOH 34 834 34 HOH HOH A . V 11 HOH 35 835 35 HOH HOH A . V 11 HOH 36 836 36 HOH HOH A . V 11 HOH 37 837 37 HOH HOH A . V 11 HOH 38 838 38 HOH HOH A . V 11 HOH 39 839 39 HOH HOH A . V 11 HOH 40 840 40 HOH HOH A . V 11 HOH 41 841 41 HOH HOH A . V 11 HOH 42 842 42 HOH HOH A . V 11 HOH 43 843 43 HOH HOH A . V 11 HOH 44 844 44 HOH HOH A . V 11 HOH 45 845 45 HOH HOH A . V 11 HOH 46 846 46 HOH HOH A . V 11 HOH 47 847 47 HOH HOH A . V 11 HOH 48 848 48 HOH HOH A . V 11 HOH 49 849 49 HOH HOH A . V 11 HOH 50 850 50 HOH HOH A . V 11 HOH 51 851 51 HOH HOH A . V 11 HOH 52 852 52 HOH HOH A . V 11 HOH 53 853 53 HOH HOH A . V 11 HOH 54 854 54 HOH HOH A . V 11 HOH 55 855 55 HOH HOH A . V 11 HOH 56 856 56 HOH HOH A . V 11 HOH 57 857 57 HOH HOH A . V 11 HOH 58 858 58 HOH HOH A . V 11 HOH 59 859 59 HOH HOH A . V 11 HOH 60 860 60 HOH HOH A . V 11 HOH 61 861 61 HOH HOH A . V 11 HOH 62 862 62 HOH HOH A . V 11 HOH 63 863 63 HOH HOH A . V 11 HOH 64 864 64 HOH HOH A . V 11 HOH 65 865 65 HOH HOH A . V 11 HOH 66 866 66 HOH HOH A . V 11 HOH 67 867 67 HOH HOH A . V 11 HOH 68 868 68 HOH HOH A . V 11 HOH 69 869 69 HOH HOH A . V 11 HOH 70 870 70 HOH HOH A . V 11 HOH 71 871 71 HOH HOH A . V 11 HOH 72 872 72 HOH HOH A . V 11 HOH 73 873 73 HOH HOH A . V 11 HOH 74 874 74 HOH HOH A . V 11 HOH 75 875 75 HOH HOH A . V 11 HOH 76 876 76 HOH HOH A . V 11 HOH 77 877 77 HOH HOH A . V 11 HOH 78 878 78 HOH HOH A . V 11 HOH 79 879 79 HOH HOH A . V 11 HOH 80 880 80 HOH HOH A . V 11 HOH 81 881 81 HOH HOH A . V 11 HOH 82 882 82 HOH HOH A . V 11 HOH 83 883 83 HOH HOH A . V 11 HOH 84 884 84 HOH HOH A . V 11 HOH 85 885 85 HOH HOH A . V 11 HOH 86 886 86 HOH HOH A . V 11 HOH 87 887 87 HOH HOH A . V 11 HOH 88 888 88 HOH HOH A . V 11 HOH 89 889 89 HOH HOH A . V 11 HOH 90 890 90 HOH HOH A . V 11 HOH 91 891 91 HOH HOH A . V 11 HOH 92 892 92 HOH HOH A . V 11 HOH 93 893 93 HOH HOH A . V 11 HOH 94 894 94 HOH HOH A . V 11 HOH 95 895 95 HOH HOH A . V 11 HOH 96 896 96 HOH HOH A . V 11 HOH 97 897 97 HOH HOH A . V 11 HOH 98 898 98 HOH HOH A . V 11 HOH 99 899 99 HOH HOH A . V 11 HOH 100 900 100 HOH HOH A . V 11 HOH 101 901 101 HOH HOH A . V 11 HOH 102 902 102 HOH HOH A . V 11 HOH 103 903 103 HOH HOH A . V 11 HOH 104 904 104 HOH HOH A . V 11 HOH 105 905 105 HOH HOH A . V 11 HOH 106 906 106 HOH HOH A . V 11 HOH 107 907 107 HOH HOH A . V 11 HOH 108 908 108 HOH HOH A . V 11 HOH 109 909 109 HOH HOH A . V 11 HOH 110 910 110 HOH HOH A . V 11 HOH 111 911 111 HOH HOH A . V 11 HOH 112 912 112 HOH HOH A . V 11 HOH 113 913 113 HOH HOH A . V 11 HOH 114 914 114 HOH HOH A . V 11 HOH 115 915 115 HOH HOH A . V 11 HOH 116 916 116 HOH HOH A . V 11 HOH 117 917 117 HOH HOH A . V 11 HOH 118 918 118 HOH HOH A . V 11 HOH 119 919 119 HOH HOH A . V 11 HOH 120 920 120 HOH HOH A . V 11 HOH 121 921 121 HOH HOH A . V 11 HOH 122 922 122 HOH HOH A . V 11 HOH 123 923 123 HOH HOH A . V 11 HOH 124 924 124 HOH HOH A . V 11 HOH 125 925 125 HOH HOH A . V 11 HOH 126 926 126 HOH HOH A . V 11 HOH 127 927 127 HOH HOH A . V 11 HOH 128 928 128 HOH HOH A . V 11 HOH 129 929 129 HOH HOH A . V 11 HOH 130 930 130 HOH HOH A . V 11 HOH 131 931 131 HOH HOH A . V 11 HOH 132 932 132 HOH HOH A . V 11 HOH 133 933 133 HOH HOH A . V 11 HOH 134 934 134 HOH HOH A . V 11 HOH 135 935 135 HOH HOH A . V 11 HOH 136 936 136 HOH HOH A . V 11 HOH 137 937 137 HOH HOH A . V 11 HOH 138 938 138 HOH HOH A . V 11 HOH 139 939 139 HOH HOH A . V 11 HOH 140 940 140 HOH HOH A . V 11 HOH 141 941 141 HOH HOH A . V 11 HOH 142 942 142 HOH HOH A . V 11 HOH 143 943 143 HOH HOH A . V 11 HOH 144 944 144 HOH HOH A . V 11 HOH 145 945 145 HOH HOH A . V 11 HOH 146 946 146 HOH HOH A . V 11 HOH 147 947 147 HOH HOH A . V 11 HOH 148 948 148 HOH HOH A . V 11 HOH 149 949 149 HOH HOH A . V 11 HOH 150 950 150 HOH HOH A . V 11 HOH 151 951 151 HOH HOH A . V 11 HOH 152 952 152 HOH HOH A . V 11 HOH 153 953 153 HOH HOH A . V 11 HOH 154 954 154 HOH HOH A . V 11 HOH 155 955 155 HOH HOH A . V 11 HOH 156 956 156 HOH HOH A . V 11 HOH 157 957 157 HOH HOH A . V 11 HOH 158 958 158 HOH HOH A . V 11 HOH 159 959 159 HOH HOH A . V 11 HOH 160 960 160 HOH HOH A . V 11 HOH 161 961 161 HOH HOH A . V 11 HOH 162 962 162 HOH HOH A . V 11 HOH 163 963 163 HOH HOH A . V 11 HOH 164 964 164 HOH HOH A . V 11 HOH 165 965 165 HOH HOH A . V 11 HOH 166 966 166 HOH HOH A . V 11 HOH 167 967 167 HOH HOH A . V 11 HOH 168 968 168 HOH HOH A . V 11 HOH 169 969 169 HOH HOH A . V 11 HOH 170 970 170 HOH HOH A . V 11 HOH 171 971 171 HOH HOH A . V 11 HOH 172 972 172 HOH HOH A . V 11 HOH 173 973 173 HOH HOH A . V 11 HOH 174 974 174 HOH HOH A . V 11 HOH 175 975 175 HOH HOH A . V 11 HOH 176 976 176 HOH HOH A . V 11 HOH 177 977 177 HOH HOH A . V 11 HOH 178 978 178 HOH HOH A . V 11 HOH 179 979 179 HOH HOH A . V 11 HOH 180 980 180 HOH HOH A . V 11 HOH 181 981 181 HOH HOH A . V 11 HOH 182 982 182 HOH HOH A . V 11 HOH 183 983 183 HOH HOH A . V 11 HOH 184 984 184 HOH HOH A . V 11 HOH 185 985 185 HOH HOH A . V 11 HOH 186 986 186 HOH HOH A . V 11 HOH 187 987 187 HOH HOH A . V 11 HOH 188 988 188 HOH HOH A . V 11 HOH 189 989 189 HOH HOH A . V 11 HOH 190 990 190 HOH HOH A . V 11 HOH 191 991 191 HOH HOH A . V 11 HOH 192 992 192 HOH HOH A . V 11 HOH 193 993 193 HOH HOH A . V 11 HOH 194 994 194 HOH HOH A . V 11 HOH 195 995 195 HOH HOH A . V 11 HOH 196 996 196 HOH HOH A . V 11 HOH 197 997 197 HOH HOH A . V 11 HOH 198 998 198 HOH HOH A . V 11 HOH 199 999 199 HOH HOH A . V 11 HOH 200 1000 200 HOH HOH A . V 11 HOH 201 1001 201 HOH HOH A . V 11 HOH 202 1002 202 HOH HOH A . V 11 HOH 203 1003 203 HOH HOH A . V 11 HOH 204 1004 204 HOH HOH A . V 11 HOH 205 1005 205 HOH HOH A . V 11 HOH 206 1006 206 HOH HOH A . V 11 HOH 207 1007 207 HOH HOH A . V 11 HOH 208 1008 208 HOH HOH A . V 11 HOH 209 1009 209 HOH HOH A . V 11 HOH 210 1010 210 HOH HOH A . V 11 HOH 211 1011 211 HOH HOH A . V 11 HOH 212 1012 212 HOH HOH A . V 11 HOH 213 1013 213 HOH HOH A . V 11 HOH 214 1014 214 HOH HOH A . V 11 HOH 215 1015 215 HOH HOH A . V 11 HOH 216 1016 216 HOH HOH A . V 11 HOH 217 1017 217 HOH HOH A . V 11 HOH 218 1018 218 HOH HOH A . V 11 HOH 219 1019 219 HOH HOH A . V 11 HOH 220 1020 220 HOH HOH A . V 11 HOH 221 1021 221 HOH HOH A . V 11 HOH 222 1022 222 HOH HOH A . V 11 HOH 223 1023 223 HOH HOH A . V 11 HOH 224 1024 224 HOH HOH A . V 11 HOH 225 1025 225 HOH HOH A . V 11 HOH 226 1026 226 HOH HOH A . V 11 HOH 227 1027 227 HOH HOH A . V 11 HOH 228 1028 228 HOH HOH A . V 11 HOH 229 1029 229 HOH HOH A . V 11 HOH 230 1030 230 HOH HOH A . V 11 HOH 231 1031 231 HOH HOH A . V 11 HOH 232 1032 232 HOH HOH A . V 11 HOH 233 1033 233 HOH HOH A . V 11 HOH 234 1034 234 HOH HOH A . V 11 HOH 235 1035 235 HOH HOH A . V 11 HOH 236 1036 236 HOH HOH A . V 11 HOH 237 1037 237 HOH HOH A . V 11 HOH 238 1038 238 HOH HOH A . V 11 HOH 239 1039 239 HOH HOH A . V 11 HOH 240 1040 240 HOH HOH A . V 11 HOH 241 1041 241 HOH HOH A . V 11 HOH 242 1042 242 HOH HOH A . V 11 HOH 243 1043 243 HOH HOH A . V 11 HOH 244 1044 244 HOH HOH A . V 11 HOH 245 1045 245 HOH HOH A . V 11 HOH 246 1046 246 HOH HOH A . V 11 HOH 247 1047 247 HOH HOH A . V 11 HOH 248 1048 248 HOH HOH A . V 11 HOH 249 1049 249 HOH HOH A . V 11 HOH 250 1050 250 HOH HOH A . V 11 HOH 251 1051 251 HOH HOH A . V 11 HOH 252 1052 252 HOH HOH A . V 11 HOH 253 1053 253 HOH HOH A . V 11 HOH 254 1054 254 HOH HOH A . V 11 HOH 255 1055 255 HOH HOH A . V 11 HOH 256 1056 256 HOH HOH A . V 11 HOH 257 1057 257 HOH HOH A . V 11 HOH 258 1058 258 HOH HOH A . V 11 HOH 259 1059 259 HOH HOH A . V 11 HOH 260 1060 260 HOH HOH A . V 11 HOH 261 1061 261 HOH HOH A . V 11 HOH 262 1062 262 HOH HOH A . V 11 HOH 263 1063 263 HOH HOH A . V 11 HOH 264 1064 264 HOH HOH A . V 11 HOH 265 1065 265 HOH HOH A . V 11 HOH 266 1066 266 HOH HOH A . V 11 HOH 267 1067 267 HOH HOH A . V 11 HOH 268 1068 268 HOH HOH A . V 11 HOH 269 1069 269 HOH HOH A . V 11 HOH 270 1070 270 HOH HOH A . V 11 HOH 271 1071 271 HOH HOH A . V 11 HOH 272 1072 272 HOH HOH A . V 11 HOH 273 1073 273 HOH HOH A . V 11 HOH 274 1074 274 HOH HOH A . V 11 HOH 275 1075 275 HOH HOH A . V 11 HOH 276 1076 276 HOH HOH A . V 11 HOH 277 1077 277 HOH HOH A . V 11 HOH 278 1078 278 HOH HOH A . V 11 HOH 279 1079 279 HOH HOH A . V 11 HOH 280 1080 280 HOH HOH A . V 11 HOH 281 1081 281 HOH HOH A . V 11 HOH 282 1082 282 HOH HOH A . V 11 HOH 283 1083 283 HOH HOH A . V 11 HOH 284 1084 284 HOH HOH A . V 11 HOH 285 1085 285 HOH HOH A . V 11 HOH 286 1086 286 HOH HOH A . V 11 HOH 287 1087 287 HOH HOH A . V 11 HOH 288 1088 288 HOH HOH A . V 11 HOH 289 1089 289 HOH HOH A . V 11 HOH 290 1090 290 HOH HOH A . V 11 HOH 291 1091 291 HOH HOH A . V 11 HOH 292 1092 292 HOH HOH A . V 11 HOH 293 1093 293 HOH HOH A . V 11 HOH 294 1094 294 HOH HOH A . V 11 HOH 295 1095 295 HOH HOH A . V 11 HOH 296 1096 296 HOH HOH A . V 11 HOH 297 1097 297 HOH HOH A . V 11 HOH 298 1098 298 HOH HOH A . V 11 HOH 299 1099 299 HOH HOH A . V 11 HOH 300 1100 300 HOH HOH A . V 11 HOH 301 1101 301 HOH HOH A . V 11 HOH 302 1102 302 HOH HOH A . V 11 HOH 303 1103 303 HOH HOH A . V 11 HOH 304 1104 304 HOH HOH A . V 11 HOH 305 1105 305 HOH HOH A . V 11 HOH 306 1106 306 HOH HOH A . V 11 HOH 307 1107 307 HOH HOH A . V 11 HOH 308 1108 308 HOH HOH A . V 11 HOH 309 1109 309 HOH HOH A . V 11 HOH 310 1110 310 HOH HOH A . V 11 HOH 311 1111 311 HOH HOH A . V 11 HOH 312 1112 312 HOH HOH A . V 11 HOH 313 1113 313 HOH HOH A . V 11 HOH 314 1114 314 HOH HOH A . V 11 HOH 315 1115 315 HOH HOH A . V 11 HOH 316 1116 316 HOH HOH A . V 11 HOH 317 1117 317 HOH HOH A . V 11 HOH 318 1118 318 HOH HOH A . V 11 HOH 319 1119 319 HOH HOH A . V 11 HOH 320 1120 320 HOH HOH A . V 11 HOH 321 1121 321 HOH HOH A . V 11 HOH 322 1122 322 HOH HOH A . V 11 HOH 323 1123 323 HOH HOH A . V 11 HOH 324 1124 324 HOH HOH A . V 11 HOH 325 1125 325 HOH HOH A . V 11 HOH 326 1126 326 HOH HOH A . V 11 HOH 327 1127 327 HOH HOH A . V 11 HOH 328 1128 328 HOH HOH A . V 11 HOH 329 1129 329 HOH HOH A . V 11 HOH 330 1130 330 HOH HOH A . V 11 HOH 331 1131 331 HOH HOH A . V 11 HOH 332 1132 332 HOH HOH A . V 11 HOH 333 1133 333 HOH HOH A . V 11 HOH 334 1134 334 HOH HOH A . V 11 HOH 335 1135 335 HOH HOH A . V 11 HOH 336 1136 336 HOH HOH A . V 11 HOH 337 1137 337 HOH HOH A . V 11 HOH 338 1138 338 HOH HOH A . V 11 HOH 339 1139 339 HOH HOH A . V 11 HOH 340 1140 340 HOH HOH A . V 11 HOH 341 1141 341 HOH HOH A . V 11 HOH 342 1142 342 HOH HOH A . V 11 HOH 343 1143 343 HOH HOH A . V 11 HOH 344 1144 344 HOH HOH A . V 11 HOH 345 1145 345 HOH HOH A . V 11 HOH 346 1146 346 HOH HOH A . V 11 HOH 347 1147 347 HOH HOH A . V 11 HOH 348 1148 348 HOH HOH A . V 11 HOH 349 1149 349 HOH HOH A . V 11 HOH 350 1150 350 HOH HOH A . V 11 HOH 351 1151 351 HOH HOH A . V 11 HOH 352 1152 352 HOH HOH A . V 11 HOH 353 1153 353 HOH HOH A . V 11 HOH 354 1154 354 HOH HOH A . V 11 HOH 355 1155 355 HOH HOH A . V 11 HOH 356 1156 356 HOH HOH A . V 11 HOH 357 1157 357 HOH HOH A . V 11 HOH 358 1158 358 HOH HOH A . V 11 HOH 359 1159 359 HOH HOH A . V 11 HOH 360 1160 360 HOH HOH A . V 11 HOH 361 1161 361 HOH HOH A . V 11 HOH 362 1162 362 HOH HOH A . V 11 HOH 363 1163 363 HOH HOH A . V 11 HOH 364 1164 364 HOH HOH A . V 11 HOH 365 1165 365 HOH HOH A . V 11 HOH 366 1166 366 HOH HOH A . V 11 HOH 367 1167 367 HOH HOH A . V 11 HOH 368 1168 368 HOH HOH A . V 11 HOH 369 1169 369 HOH HOH A . V 11 HOH 370 1170 370 HOH HOH A . V 11 HOH 371 1171 371 HOH HOH A . V 11 HOH 372 1172 372 HOH HOH A . V 11 HOH 373 1173 373 HOH HOH A . V 11 HOH 374 1174 374 HOH HOH A . V 11 HOH 375 1175 375 HOH HOH A . V 11 HOH 376 1176 376 HOH HOH A . V 11 HOH 377 1177 377 HOH HOH A . V 11 HOH 378 1178 378 HOH HOH A . V 11 HOH 379 1179 379 HOH HOH A . V 11 HOH 380 1180 380 HOH HOH A . V 11 HOH 381 1181 381 HOH HOH A . V 11 HOH 382 1182 382 HOH HOH A . V 11 HOH 383 1183 383 HOH HOH A . V 11 HOH 384 1184 384 HOH HOH A . V 11 HOH 385 1185 385 HOH HOH A . V 11 HOH 386 1186 386 HOH HOH A . V 11 HOH 387 1187 387 HOH HOH A . V 11 HOH 388 1188 388 HOH HOH A . V 11 HOH 389 1189 389 HOH HOH A . V 11 HOH 390 1190 390 HOH HOH A . V 11 HOH 391 1191 391 HOH HOH A . V 11 HOH 392 1192 392 HOH HOH A . V 11 HOH 393 1193 393 HOH HOH A . V 11 HOH 394 1194 394 HOH HOH A . V 11 HOH 395 1195 395 HOH HOH A . V 11 HOH 396 1196 396 HOH HOH A . V 11 HOH 397 1197 397 HOH HOH A . V 11 HOH 398 1198 398 HOH HOH A . V 11 HOH 399 1199 399 HOH HOH A . V 11 HOH 400 1200 400 HOH HOH A . V 11 HOH 401 1201 401 HOH HOH A . V 11 HOH 402 1202 402 HOH HOH A . V 11 HOH 403 1203 403 HOH HOH A . V 11 HOH 404 1204 404 HOH HOH A . V 11 HOH 405 1205 405 HOH HOH A . V 11 HOH 406 1206 406 HOH HOH A . V 11 HOH 407 1207 407 HOH HOH A . V 11 HOH 408 1208 408 HOH HOH A . V 11 HOH 409 1209 409 HOH HOH A . V 11 HOH 410 1210 410 HOH HOH A . V 11 HOH 411 1211 411 HOH HOH A . V 11 HOH 412 1212 412 HOH HOH A . V 11 HOH 413 1213 413 HOH HOH A . V 11 HOH 414 1214 414 HOH HOH A . V 11 HOH 415 1215 415 HOH HOH A . V 11 HOH 416 1216 416 HOH HOH A . V 11 HOH 417 1217 417 HOH HOH A . V 11 HOH 418 1218 418 HOH HOH A . V 11 HOH 419 1219 419 HOH HOH A . V 11 HOH 420 1220 420 HOH HOH A . V 11 HOH 421 1221 421 HOH HOH A . V 11 HOH 422 1222 422 HOH HOH A . V 11 HOH 423 1223 423 HOH HOH A . V 11 HOH 424 1224 424 HOH HOH A . V 11 HOH 425 1225 425 HOH HOH A . V 11 HOH 426 1226 426 HOH HOH A . V 11 HOH 427 1227 427 HOH HOH A . V 11 HOH 428 1228 428 HOH HOH A . V 11 HOH 429 1229 429 HOH HOH A . V 11 HOH 430 1230 430 HOH HOH A . V 11 HOH 431 1231 431 HOH HOH A . V 11 HOH 432 1232 432 HOH HOH A . V 11 HOH 433 1233 433 HOH HOH A . V 11 HOH 434 1234 434 HOH HOH A . V 11 HOH 435 1235 435 HOH HOH A . V 11 HOH 436 1236 436 HOH HOH A . V 11 HOH 437 1237 437 HOH HOH A . V 11 HOH 438 1238 438 HOH HOH A . V 11 HOH 439 1239 439 HOH HOH A . V 11 HOH 440 1240 440 HOH HOH A . V 11 HOH 441 1241 441 HOH HOH A . V 11 HOH 442 1242 442 HOH HOH A . V 11 HOH 443 1243 443 HOH HOH A . V 11 HOH 444 1244 444 HOH HOH A . V 11 HOH 445 1245 445 HOH HOH A . V 11 HOH 446 1246 446 HOH HOH A . V 11 HOH 447 1247 447 HOH HOH A . V 11 HOH 448 1248 448 HOH HOH A . V 11 HOH 449 1249 449 HOH HOH A . V 11 HOH 450 1250 450 HOH HOH A . V 11 HOH 451 1251 451 HOH HOH A . V 11 HOH 452 1252 452 HOH HOH A . V 11 HOH 453 1253 453 HOH HOH A . V 11 HOH 454 1254 454 HOH HOH A . V 11 HOH 455 1255 455 HOH HOH A . V 11 HOH 456 1256 456 HOH HOH A . V 11 HOH 457 1257 457 HOH HOH A . V 11 HOH 458 1258 458 HOH HOH A . V 11 HOH 459 1259 459 HOH HOH A . V 11 HOH 460 1260 460 HOH HOH A . V 11 HOH 461 1261 461 HOH HOH A . V 11 HOH 462 1262 462 HOH HOH A . V 11 HOH 463 1263 463 HOH HOH A . V 11 HOH 464 1264 464 HOH HOH A . V 11 HOH 465 1265 465 HOH HOH A . V 11 HOH 466 1266 466 HOH HOH A . V 11 HOH 467 1267 467 HOH HOH A . V 11 HOH 468 1268 468 HOH HOH A . V 11 HOH 469 1269 469 HOH HOH A . V 11 HOH 470 1270 470 HOH HOH A . V 11 HOH 471 1271 471 HOH HOH A . V 11 HOH 472 1272 472 HOH HOH A . V 11 HOH 473 1273 473 HOH HOH A . V 11 HOH 474 1274 474 HOH HOH A . V 11 HOH 475 1275 475 HOH HOH A . V 11 HOH 476 1276 476 HOH HOH A . V 11 HOH 477 1277 477 HOH HOH A . V 11 HOH 478 1278 478 HOH HOH A . V 11 HOH 479 1279 479 HOH HOH A . V 11 HOH 480 1280 480 HOH HOH A . V 11 HOH 481 1281 481 HOH HOH A . V 11 HOH 482 1282 482 HOH HOH A . V 11 HOH 483 1283 483 HOH HOH A . V 11 HOH 484 1284 484 HOH HOH A . V 11 HOH 485 1285 485 HOH HOH A . V 11 HOH 486 1286 486 HOH HOH A . V 11 HOH 487 1287 487 HOH HOH A . V 11 HOH 488 1288 488 HOH HOH A . V 11 HOH 489 1289 489 HOH HOH A . V 11 HOH 490 1290 490 HOH HOH A . V 11 HOH 491 1291 491 HOH HOH A . V 11 HOH 492 1292 492 HOH HOH A . V 11 HOH 493 1293 493 HOH HOH A . V 11 HOH 494 1294 494 HOH HOH A . V 11 HOH 495 1295 495 HOH HOH A . V 11 HOH 496 1296 496 HOH HOH A . V 11 HOH 497 1297 497 HOH HOH A . V 11 HOH 498 1298 498 HOH HOH A . V 11 HOH 499 1299 499 HOH HOH A . V 11 HOH 500 1300 500 HOH HOH A . V 11 HOH 501 1301 501 HOH HOH A . V 11 HOH 502 1302 502 HOH HOH A . V 11 HOH 503 1303 503 HOH HOH A . V 11 HOH 504 1304 504 HOH HOH A . V 11 HOH 505 1305 505 HOH HOH A . V 11 HOH 506 1306 506 HOH HOH A . V 11 HOH 507 1307 507 HOH HOH A . V 11 HOH 508 1308 508 HOH HOH A . V 11 HOH 509 1309 509 HOH HOH A . V 11 HOH 510 1310 510 HOH HOH A . V 11 HOH 511 1311 511 HOH HOH A . V 11 HOH 512 1312 512 HOH HOH A . V 11 HOH 513 1313 513 HOH HOH A . V 11 HOH 514 1314 514 HOH HOH A . V 11 HOH 515 1315 515 HOH HOH A . V 11 HOH 516 1316 516 HOH HOH A . V 11 HOH 517 1317 517 HOH HOH A . V 11 HOH 518 1318 518 HOH HOH A . V 11 HOH 519 1319 519 HOH HOH A . V 11 HOH 520 1320 520 HOH HOH A . V 11 HOH 521 1321 521 HOH HOH A . V 11 HOH 522 1322 522 HOH HOH A . V 11 HOH 523 1323 523 HOH HOH A . V 11 HOH 524 1324 524 HOH HOH A . V 11 HOH 525 1325 525 HOH HOH A . V 11 HOH 526 1326 526 HOH HOH A . V 11 HOH 527 1327 527 HOH HOH A . V 11 HOH 528 1328 528 HOH HOH A . V 11 HOH 529 1329 529 HOH HOH A . V 11 HOH 530 1330 530 HOH HOH A . V 11 HOH 531 1331 531 HOH HOH A . V 11 HOH 532 1332 532 HOH HOH A . V 11 HOH 533 1333 533 HOH HOH A . V 11 HOH 534 1334 534 HOH HOH A . V 11 HOH 535 1335 535 HOH HOH A . V 11 HOH 536 1336 536 HOH HOH A . V 11 HOH 537 1337 537 HOH HOH A . V 11 HOH 538 1338 538 HOH HOH A . V 11 HOH 539 1339 539 HOH HOH A . V 11 HOH 540 1340 540 HOH HOH A . V 11 HOH 541 1341 541 HOH HOH A . V 11 HOH 542 1342 542 HOH HOH A . V 11 HOH 543 1343 543 HOH HOH A . V 11 HOH 544 1344 544 HOH HOH A . V 11 HOH 545 1345 545 HOH HOH A . V 11 HOH 546 1346 546 HOH HOH A . V 11 HOH 547 1347 547 HOH HOH A . V 11 HOH 548 1348 548 HOH HOH A . V 11 HOH 549 1349 549 HOH HOH A . V 11 HOH 550 1350 550 HOH HOH A . V 11 HOH 551 1351 551 HOH HOH A . V 11 HOH 552 1352 552 HOH HOH A . V 11 HOH 553 1353 553 HOH HOH A . V 11 HOH 554 1354 554 HOH HOH A . V 11 HOH 555 1355 555 HOH HOH A . V 11 HOH 556 1356 556 HOH HOH A . V 11 HOH 557 1357 557 HOH HOH A . V 11 HOH 558 1358 558 HOH HOH A . V 11 HOH 559 1359 559 HOH HOH A . V 11 HOH 560 1360 560 HOH HOH A . V 11 HOH 561 1361 561 HOH HOH A . V 11 HOH 562 1362 562 HOH HOH A . V 11 HOH 563 1363 563 HOH HOH A . V 11 HOH 564 1364 564 HOH HOH A . V 11 HOH 565 1365 565 HOH HOH A . V 11 HOH 566 1366 566 HOH HOH A . V 11 HOH 567 1367 567 HOH HOH A . V 11 HOH 568 1368 568 HOH HOH A . V 11 HOH 569 1369 569 HOH HOH A . V 11 HOH 570 1370 570 HOH HOH A . V 11 HOH 571 1371 571 HOH HOH A . V 11 HOH 572 1372 572 HOH HOH A . V 11 HOH 573 1373 573 HOH HOH A . V 11 HOH 574 1374 574 HOH HOH A . V 11 HOH 575 1375 575 HOH HOH A . V 11 HOH 576 1376 576 HOH HOH A . V 11 HOH 577 1377 577 HOH HOH A . V 11 HOH 578 1378 578 HOH HOH A . V 11 HOH 579 1379 579 HOH HOH A . V 11 HOH 580 1380 580 HOH HOH A . V 11 HOH 581 1381 581 HOH HOH A . V 11 HOH 582 1382 582 HOH HOH A . V 11 HOH 583 1383 583 HOH HOH A . V 11 HOH 584 1384 584 HOH HOH A . V 11 HOH 585 1385 585 HOH HOH A . V 11 HOH 586 1386 586 HOH HOH A . V 11 HOH 587 1387 587 HOH HOH A . V 11 HOH 588 1388 588 HOH HOH A . V 11 HOH 589 1389 589 HOH HOH A . V 11 HOH 590 1390 590 HOH HOH A . V 11 HOH 591 1391 591 HOH HOH A . V 11 HOH 592 1392 592 HOH HOH A . V 11 HOH 593 1393 593 HOH HOH A . V 11 HOH 594 1394 594 HOH HOH A . V 11 HOH 595 1395 595 HOH HOH A . V 11 HOH 596 1396 596 HOH HOH A . V 11 HOH 597 1397 597 HOH HOH A . V 11 HOH 598 1398 598 HOH HOH A . V 11 HOH 599 1399 599 HOH HOH A . V 11 HOH 600 1400 600 HOH HOH A . V 11 HOH 601 1401 601 HOH HOH A . V 11 HOH 602 1402 602 HOH HOH A . V 11 HOH 603 1403 603 HOH HOH A . V 11 HOH 604 1404 604 HOH HOH A . V 11 HOH 605 1405 605 HOH HOH A . V 11 HOH 606 1406 606 HOH HOH A . V 11 HOH 607 1407 607 HOH HOH A . V 11 HOH 608 1408 608 HOH HOH A . V 11 HOH 609 1409 609 HOH HOH A . V 11 HOH 610 1410 610 HOH HOH A . V 11 HOH 611 1411 611 HOH HOH A . V 11 HOH 612 1412 612 HOH HOH A . V 11 HOH 613 1413 613 HOH HOH A . V 11 HOH 614 1414 614 HOH HOH A . V 11 HOH 615 1415 615 HOH HOH A . V 11 HOH 616 1416 616 HOH HOH A . V 11 HOH 617 1417 617 HOH HOH A . V 11 HOH 618 1418 618 HOH HOH A . V 11 HOH 619 1419 619 HOH HOH A . V 11 HOH 620 1420 620 HOH HOH A . V 11 HOH 621 1421 621 HOH HOH A . V 11 HOH 622 1422 622 HOH HOH A . V 11 HOH 623 1423 623 HOH HOH A . V 11 HOH 624 1424 624 HOH HOH A . V 11 HOH 625 1425 625 HOH HOH A . V 11 HOH 626 1426 626 HOH HOH A . V 11 HOH 627 1427 627 HOH HOH A . V 11 HOH 628 1428 628 HOH HOH A . V 11 HOH 629 1429 629 HOH HOH A . V 11 HOH 630 1430 630 HOH HOH A . V 11 HOH 631 1431 631 HOH HOH A . V 11 HOH 632 1432 632 HOH HOH A . V 11 HOH 633 1433 633 HOH HOH A . V 11 HOH 634 1434 634 HOH HOH A . V 11 HOH 635 1435 635 HOH HOH A . V 11 HOH 636 1436 636 HOH HOH A . V 11 HOH 637 1437 637 HOH HOH A . V 11 HOH 638 1438 638 HOH HOH A . V 11 HOH 639 1439 639 HOH HOH A . V 11 HOH 640 1440 640 HOH HOH A . V 11 HOH 641 1441 641 HOH HOH A . V 11 HOH 642 1442 642 HOH HOH A . V 11 HOH 643 1443 643 HOH HOH A . V 11 HOH 644 1444 644 HOH HOH A . V 11 HOH 645 1445 645 HOH HOH A . V 11 HOH 646 1446 646 HOH HOH A . V 11 HOH 647 1447 647 HOH HOH A . V 11 HOH 648 1448 648 HOH HOH A . V 11 HOH 649 1449 649 HOH HOH A . V 11 HOH 650 1450 650 HOH HOH A . V 11 HOH 651 1451 651 HOH HOH A . V 11 HOH 652 1452 652 HOH HOH A . V 11 HOH 653 1453 653 HOH HOH A . V 11 HOH 654 1454 654 HOH HOH A . V 11 HOH 655 1455 655 HOH HOH A . V 11 HOH 656 1456 656 HOH HOH A . V 11 HOH 657 1457 657 HOH HOH A . V 11 HOH 658 1458 658 HOH HOH A . V 11 HOH 659 1459 659 HOH HOH A . V 11 HOH 660 1460 660 HOH HOH A . V 11 HOH 661 1461 661 HOH HOH A . V 11 HOH 662 1462 662 HOH HOH A . V 11 HOH 663 1463 663 HOH HOH A . V 11 HOH 664 1464 664 HOH HOH A . V 11 HOH 665 1465 665 HOH HOH A . V 11 HOH 666 1466 666 HOH HOH A . V 11 HOH 667 1467 667 HOH HOH A . V 11 HOH 668 1468 668 HOH HOH A . V 11 HOH 669 1469 669 HOH HOH A . V 11 HOH 670 1470 670 HOH HOH A . V 11 HOH 671 1471 671 HOH HOH A . V 11 HOH 672 1472 672 HOH HOH A . V 11 HOH 673 1473 673 HOH HOH A . V 11 HOH 674 1474 674 HOH HOH A . V 11 HOH 675 1475 675 HOH HOH A . V 11 HOH 676 1476 676 HOH HOH A . V 11 HOH 677 1477 677 HOH HOH A . V 11 HOH 678 1478 678 HOH HOH A . V 11 HOH 679 1479 679 HOH HOH A . V 11 HOH 680 1480 680 HOH HOH A . V 11 HOH 681 1481 681 HOH HOH A . V 11 HOH 682 1482 682 HOH HOH A . V 11 HOH 683 1483 683 HOH HOH A . V 11 HOH 684 1484 684 HOH HOH A . V 11 HOH 685 1485 685 HOH HOH A . V 11 HOH 686 1486 686 HOH HOH A . V 11 HOH 687 1487 687 HOH HOH A . V 11 HOH 688 1488 688 HOH HOH A . V 11 HOH 689 1489 689 HOH HOH A . V 11 HOH 690 1490 690 HOH HOH A . V 11 HOH 691 1491 691 HOH HOH A . V 11 HOH 692 1492 692 HOH HOH A . V 11 HOH 693 1493 693 HOH HOH A . V 11 HOH 694 1494 694 HOH HOH A . V 11 HOH 695 1495 695 HOH HOH A . V 11 HOH 696 1496 696 HOH HOH A . V 11 HOH 697 1497 697 HOH HOH A . V 11 HOH 698 1498 698 HOH HOH A . V 11 HOH 699 1499 699 HOH HOH A . V 11 HOH 700 1500 700 HOH HOH A . V 11 HOH 701 1501 701 HOH HOH A . V 11 HOH 702 1502 702 HOH HOH A . V 11 HOH 703 1503 703 HOH HOH A . V 11 HOH 704 1504 704 HOH HOH A . V 11 HOH 705 1505 705 HOH HOH A . V 11 HOH 706 1506 706 HOH HOH A . V 11 HOH 707 1507 707 HOH HOH A . V 11 HOH 708 1508 708 HOH HOH A . V 11 HOH 709 1509 709 HOH HOH A . V 11 HOH 710 1510 710 HOH HOH A . V 11 HOH 711 1511 711 HOH HOH A . V 11 HOH 712 1512 712 HOH HOH A . V 11 HOH 713 1513 713 HOH HOH A . V 11 HOH 714 1514 714 HOH HOH A . V 11 HOH 715 1515 715 HOH HOH A . V 11 HOH 716 1516 716 HOH HOH A . V 11 HOH 717 1517 717 HOH HOH A . V 11 HOH 718 1518 718 HOH HOH A . V 11 HOH 719 1519 719 HOH HOH A . V 11 HOH 720 1520 720 HOH HOH A . V 11 HOH 721 1521 721 HOH HOH A . V 11 HOH 722 1522 722 HOH HOH A . V 11 HOH 723 1523 723 HOH HOH A . V 11 HOH 724 1524 724 HOH HOH A . V 11 HOH 725 1525 725 HOH HOH A . V 11 HOH 726 1526 726 HOH HOH A . V 11 HOH 727 1527 727 HOH HOH A . V 11 HOH 728 1528 728 HOH HOH A . V 11 HOH 729 1529 729 HOH HOH A . V 11 HOH 730 1530 730 HOH HOH A . V 11 HOH 731 1531 731 HOH HOH A . V 11 HOH 732 1532 732 HOH HOH A . V 11 HOH 733 1533 733 HOH HOH A . V 11 HOH 734 1534 734 HOH HOH A . V 11 HOH 735 1535 735 HOH HOH A . V 11 HOH 736 1536 736 HOH HOH A . V 11 HOH 737 1537 737 HOH HOH A . V 11 HOH 738 1538 738 HOH HOH A . V 11 HOH 739 1539 739 HOH HOH A . V 11 HOH 740 1540 740 HOH HOH A . V 11 HOH 741 1541 741 HOH HOH A . V 11 HOH 742 1542 742 HOH HOH A . V 11 HOH 743 1543 743 HOH HOH A . V 11 HOH 744 1544 744 HOH HOH A . V 11 HOH 745 1545 745 HOH HOH A . V 11 HOH 746 1546 746 HOH HOH A . V 11 HOH 747 1547 747 HOH HOH A . V 11 HOH 748 1548 748 HOH HOH A . V 11 HOH 749 1549 749 HOH HOH A . V 11 HOH 750 1550 750 HOH HOH A . V 11 HOH 751 1551 751 HOH HOH A . V 11 HOH 752 1552 752 HOH HOH A . V 11 HOH 753 1553 753 HOH HOH A . V 11 HOH 754 1554 754 HOH HOH A . V 11 HOH 755 1555 755 HOH HOH A . V 11 HOH 756 1556 756 HOH HOH A . V 11 HOH 757 1557 757 HOH HOH A . V 11 HOH 758 1558 758 HOH HOH A . V 11 HOH 759 1559 759 HOH HOH A . V 11 HOH 760 1560 760 HOH HOH A . V 11 HOH 761 1561 761 HOH HOH A . V 11 HOH 762 1562 762 HOH HOH A . V 11 HOH 763 1563 763 HOH HOH A . V 11 HOH 764 1564 764 HOH HOH A . V 11 HOH 765 1565 765 HOH HOH A . V 11 HOH 766 1566 766 HOH HOH A . V 11 HOH 767 1567 767 HOH HOH A . V 11 HOH 768 1568 768 HOH HOH A . V 11 HOH 769 1569 769 HOH HOH A . V 11 HOH 770 1570 770 HOH HOH A . V 11 HOH 771 1571 771 HOH HOH A . V 11 HOH 772 1572 772 HOH HOH A . V 11 HOH 773 1573 773 HOH HOH A . V 11 HOH 774 1574 774 HOH HOH A . V 11 HOH 775 1575 775 HOH HOH A . V 11 HOH 776 1576 776 HOH HOH A . V 11 HOH 777 1577 777 HOH HOH A . V 11 HOH 778 1578 778 HOH HOH A . V 11 HOH 779 1579 779 HOH HOH A . V 11 HOH 780 1580 780 HOH HOH A . V 11 HOH 781 1581 781 HOH HOH A . V 11 HOH 782 1582 782 HOH HOH A . V 11 HOH 783 1583 783 HOH HOH A . V 11 HOH 784 1584 784 HOH HOH A . V 11 HOH 785 1585 785 HOH HOH A . V 11 HOH 786 1586 786 HOH HOH A . V 11 HOH 787 1587 787 HOH HOH A . V 11 HOH 788 1588 788 HOH HOH A . V 11 HOH 789 1589 789 HOH HOH A . V 11 HOH 790 1590 790 HOH HOH A . V 11 HOH 791 1591 791 HOH HOH A . V 11 HOH 792 1592 792 HOH HOH A . V 11 HOH 793 1593 793 HOH HOH A . V 11 HOH 794 1594 794 HOH HOH A . V 11 HOH 795 1595 795 HOH HOH A . V 11 HOH 796 1596 796 HOH HOH A . V 11 HOH 797 1597 797 HOH HOH A . V 11 HOH 798 1598 798 HOH HOH A . V 11 HOH 799 1599 799 HOH HOH A . V 11 HOH 800 1600 800 HOH HOH A . V 11 HOH 801 1601 801 HOH HOH A . V 11 HOH 802 1602 802 HOH HOH A . V 11 HOH 803 1603 803 HOH HOH A . V 11 HOH 804 1604 804 HOH HOH A . V 11 HOH 805 1605 805 HOH HOH A . V 11 HOH 806 1606 806 HOH HOH A . V 11 HOH 807 1607 807 HOH HOH A . V 11 HOH 808 1608 808 HOH HOH A . V 11 HOH 809 1609 809 HOH HOH A . V 11 HOH 810 1610 810 HOH HOH A . V 11 HOH 811 1611 811 HOH HOH A . V 11 HOH 812 1612 812 HOH HOH A . V 11 HOH 813 1613 813 HOH HOH A . V 11 HOH 814 1614 814 HOH HOH A . V 11 HOH 815 1615 815 HOH HOH A . V 11 HOH 816 1616 816 HOH HOH A . V 11 HOH 817 1617 817 HOH HOH A . V 11 HOH 818 1618 818 HOH HOH A . V 11 HOH 819 1619 819 HOH HOH A . V 11 HOH 820 1620 820 HOH HOH A . V 11 HOH 821 1621 821 HOH HOH A . V 11 HOH 822 1622 822 HOH HOH A . V 11 HOH 823 1623 823 HOH HOH A . V 11 HOH 824 1624 824 HOH HOH A . V 11 HOH 825 1625 825 HOH HOH A . V 11 HOH 826 1626 826 HOH HOH A . V 11 HOH 827 1627 827 HOH HOH A . V 11 HOH 828 1628 828 HOH HOH A . V 11 HOH 829 1629 829 HOH HOH A . V 11 HOH 830 1630 830 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 221 A ASN 221 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 600 A ASN 600 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 498 A ASN 498 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V # _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 # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2015-03-25 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CCP4 'model building' . ? 1 REFMAC refinement 5.3.0040 ? 2 DENZO 'data reduction' . ? 3 SCALEPACK 'data scaling' . ? 4 CCP4 phasing . ? 5 # _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THE AUTHORS STATE THERE IS AN ERROR IN THE CDNA SEQUENCING OF AF102868 (GENBANK ACCESSION NUMBER). RESIDUE 320 (SEQUENCE DATABASE RESIDUE 345) IS LYS AND IS NOT ASN. ; _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.entry_id 3WLJ # 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 O A HOH 1049 ? ? O A HOH 1565 ? ? 1.97 2 1 O A HOH 1038 ? ? O A HOH 1565 ? ? 2.08 3 1 O A HOH 877 ? ? O A HOH 1104 ? ? 2.10 4 1 O A HOH 1306 ? ? O A HOH 1581 ? ? 2.10 5 1 OD1 A ASN 498 ? ? O A HOH 921 ? ? 2.10 6 1 O A HOH 921 ? ? O A HOH 1536 ? ? 2.15 7 1 O A HOH 953 ? ? O A HOH 1574 ? ? 2.17 8 1 NH2 A ARG 517 ? A O A HOH 841 ? ? 2.18 9 1 O A HOH 961 ? ? O A HOH 1584 ? ? 2.18 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 947 ? ? 1_555 O A HOH 1582 ? ? 6_555 2.13 2 1 O A HOH 1104 ? ? 1_555 O A HOH 1583 ? ? 6_555 2.14 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 CA _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 CYS _pdbx_validate_rmsd_angle.auth_seq_id_1 518 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CB _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 CYS _pdbx_validate_rmsd_angle.auth_seq_id_2 518 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 B _pdbx_validate_rmsd_angle.auth_atom_id_3 SG _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 CYS _pdbx_validate_rmsd_angle.auth_seq_id_3 518 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 B _pdbx_validate_rmsd_angle.angle_value 125.86 _pdbx_validate_rmsd_angle.angle_target_value 114.20 _pdbx_validate_rmsd_angle.angle_deviation 11.66 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.10 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 98 ? ? -152.35 66.87 2 1 ASN A 221 ? ? -91.17 -152.56 3 1 TYR A 271 ? ? -97.66 -61.67 4 1 ASN A 394 ? ? -150.56 64.59 5 1 ILE A 432 ? ? 70.73 -57.71 6 1 GLU A 491 ? ? 54.64 -135.04 7 1 TRP A 544 ? ? 57.44 -133.90 8 1 GLU A 549 ? ? -100.64 78.53 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A LYS 603 ? A LYS 603 2 1 Y 1 A LYS 604 ? A LYS 604 3 1 Y 1 A TYR 605 ? A TYR 605 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 BETA-L-FUCOSE FUL 5 ALPHA-D-MANNOSE MAN 6 BETA-D-XYLOPYRANOSE XYP 7 BETA-D-GLUCOSE BGC 8 3-deoxy-beta-D-ribo-hexopyranose 3DO 9 GLYCEROL GOL 10 'SULFATE ION' SO4 11 water HOH #