data_4CA7 # _entry.id 4CA7 # _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 4CA7 PDBE EBI-58646 WWPDB D_1290058646 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4CA5 unspecified 'HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH A PHOSPHINIC TRIPEPTIDE FI' PDB 4CA6 unspecified 'HUMAN ANGIOTENSIN CONVERTING ENZYME N-DOMAIN IN COMPLEX WITH A PHOSPHINIC TRIPEPTIDE FI' PDB 4CA8 unspecified 'DROSOPHILA ANGIOTENSIN CONVERTING ENZYME (ANCE) IN COMPLEX WITH A PHOSPHINIC TRIPEPTIDE FII' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4CA7 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2013-10-07 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Masuyer, G.' 1 'Akif, M.' 2 'Czarny, B.' 3 'Beau, F.' 4 'Schwager, S.L.U.' 5 'Sturrock, E.D.' 6 'Isaac, R.E.' 7 'Dive, V.' 8 'Acharya, K.R.' 9 # _citation.id primary _citation.title 'Crystal Structures of Highly Specific Phosphinic Tripeptide Enantiomers in Complex with the Angiotensin-I Converting Enzyme.' _citation.journal_abbrev 'FEBS J.' _citation.journal_volume 281 _citation.page_first 943 _citation.page_last ? _citation.year 2014 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 1742-464X _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24289879 _citation.pdbx_database_id_DOI 10.1111/FEBS.12660 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Masuyer, G.' 1 primary 'Akif, M.' 2 primary 'Czarny, B.' 3 primary 'Beau, F.' 4 primary 'Schwager, S.L.' 5 primary 'Sturrock, E.D.' 6 primary 'Isaac, R.E.' 7 primary 'Dive, V.' 8 primary 'Acharya, K.R.' 9 # _cell.entry_id 4CA7 _cell.length_a 173.743 _cell.length_b 173.743 _cell.length_c 102.178 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 9 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4CA7 _symmetry.space_group_name_H-M 'H 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 146 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'ANGIOTENSIN-CONVERTING ENZYME' 69152.602 1 3.4.15.1 ? 'RESIDUES 17-614' ? 2 non-polymer syn 'ZINC ION' 65.409 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 4 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 5 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 6 non-polymer syn ;N-{(2S)-3-[(S)-[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl]-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tyrosine ; 711.697 1 ? ? ? ? 7 water nat water 18.015 576 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II,' # _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 ;ALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEVASDTTKFQWRSYQSEDLKRQ FKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTA VRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPM HLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLPQDFWDKSIIEKPTDGRDLVC HASAWDFYLTDDVRIKQCTRVTQDQLFTVHHELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGL LKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWNCAFWKLRDEYSGIEPPVVRSEKDFDAPAKY HISADVEYLRYLVSFIIQFQFYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPDALEAFNGERI MSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVS ; _entity_poly.pdbx_seq_one_letter_code_can ;ALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEVASDTTKFQWRSYQSEDLKRQ FKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTA VRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPM HLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLPQDFWDKSIIEKPTDGRDLVC HASAWDFYLTDDVRIKQCTRVTQDQLFTVHHELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGL LKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWNCAFWKLRDEYSGIEPPVVRSEKDFDAPAKY HISADVEYLRYLVSFIIQFQFYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPDALEAFNGERI MSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVS ; _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 ALA n 1 2 LEU n 1 3 VAL n 1 4 LYS n 1 5 GLU n 1 6 GLU n 1 7 ILE n 1 8 GLN n 1 9 ALA n 1 10 LYS n 1 11 GLU n 1 12 TYR n 1 13 LEU n 1 14 GLU n 1 15 ASN n 1 16 LEU n 1 17 ASN n 1 18 LYS n 1 19 GLU n 1 20 LEU n 1 21 ALA n 1 22 LYS n 1 23 ARG n 1 24 THR n 1 25 ASN n 1 26 VAL n 1 27 GLU n 1 28 THR n 1 29 GLU n 1 30 ALA n 1 31 ALA n 1 32 TRP n 1 33 ALA n 1 34 TYR n 1 35 GLY n 1 36 SER n 1 37 ASN n 1 38 ILE n 1 39 THR n 1 40 ASP n 1 41 GLU n 1 42 ASN n 1 43 GLU n 1 44 LYS n 1 45 LYS n 1 46 LYS n 1 47 ASN n 1 48 GLU n 1 49 ILE n 1 50 SER n 1 51 ALA n 1 52 GLU n 1 53 LEU n 1 54 ALA n 1 55 LYS n 1 56 PHE n 1 57 MET n 1 58 LYS n 1 59 GLU n 1 60 VAL n 1 61 ALA n 1 62 SER n 1 63 ASP n 1 64 THR n 1 65 THR n 1 66 LYS n 1 67 PHE n 1 68 GLN n 1 69 TRP n 1 70 ARG n 1 71 SER n 1 72 TYR n 1 73 GLN n 1 74 SER n 1 75 GLU n 1 76 ASP n 1 77 LEU n 1 78 LYS n 1 79 ARG n 1 80 GLN n 1 81 PHE n 1 82 LYS n 1 83 ALA n 1 84 LEU n 1 85 THR n 1 86 LYS n 1 87 LEU n 1 88 GLY n 1 89 TYR n 1 90 ALA n 1 91 ALA n 1 92 LEU n 1 93 PRO n 1 94 GLU n 1 95 ASP n 1 96 ASP n 1 97 TYR n 1 98 ALA n 1 99 GLU n 1 100 LEU n 1 101 LEU n 1 102 ASP n 1 103 THR n 1 104 LEU n 1 105 SER n 1 106 ALA n 1 107 MET n 1 108 GLU n 1 109 SER n 1 110 ASN n 1 111 PHE n 1 112 ALA n 1 113 LYS n 1 114 VAL n 1 115 LYS n 1 116 VAL n 1 117 CYS n 1 118 ASP n 1 119 TYR n 1 120 LYS n 1 121 ASP n 1 122 SER n 1 123 THR n 1 124 LYS n 1 125 CYS n 1 126 ASP n 1 127 LEU n 1 128 ALA n 1 129 LEU n 1 130 ASP n 1 131 PRO n 1 132 GLU n 1 133 ILE n 1 134 GLU n 1 135 GLU n 1 136 VAL n 1 137 ILE n 1 138 SER n 1 139 LYS n 1 140 SER n 1 141 ARG n 1 142 ASP n 1 143 HIS n 1 144 GLU n 1 145 GLU n 1 146 LEU n 1 147 ALA n 1 148 TYR n 1 149 TYR n 1 150 TRP n 1 151 ARG n 1 152 GLU n 1 153 PHE n 1 154 TYR n 1 155 ASP n 1 156 LYS n 1 157 ALA n 1 158 GLY n 1 159 THR n 1 160 ALA n 1 161 VAL n 1 162 ARG n 1 163 SER n 1 164 GLN n 1 165 PHE n 1 166 GLU n 1 167 ARG n 1 168 TYR n 1 169 VAL n 1 170 GLU n 1 171 LEU n 1 172 ASN n 1 173 THR n 1 174 LYS n 1 175 ALA n 1 176 ALA n 1 177 LYS n 1 178 LEU n 1 179 ASN n 1 180 ASN n 1 181 PHE n 1 182 THR n 1 183 SER n 1 184 GLY n 1 185 ALA n 1 186 GLU n 1 187 ALA n 1 188 TRP n 1 189 LEU n 1 190 ASP n 1 191 GLU n 1 192 TYR n 1 193 GLU n 1 194 ASP n 1 195 ASP n 1 196 THR n 1 197 PHE n 1 198 GLU n 1 199 GLN n 1 200 GLN n 1 201 LEU n 1 202 GLU n 1 203 ASP n 1 204 ILE n 1 205 PHE n 1 206 ALA n 1 207 ASP n 1 208 ILE n 1 209 ARG n 1 210 PRO n 1 211 LEU n 1 212 TYR n 1 213 GLN n 1 214 GLN n 1 215 ILE n 1 216 HIS n 1 217 GLY n 1 218 TYR n 1 219 VAL n 1 220 ARG n 1 221 PHE n 1 222 ARG n 1 223 LEU n 1 224 ARG n 1 225 LYS n 1 226 HIS n 1 227 TYR n 1 228 GLY n 1 229 ASP n 1 230 ALA n 1 231 VAL n 1 232 VAL n 1 233 SER n 1 234 GLU n 1 235 THR n 1 236 GLY n 1 237 PRO n 1 238 ILE n 1 239 PRO n 1 240 MET n 1 241 HIS n 1 242 LEU n 1 243 LEU n 1 244 GLY n 1 245 ASN n 1 246 MET n 1 247 TRP n 1 248 ALA n 1 249 GLN n 1 250 GLN n 1 251 TRP n 1 252 SER n 1 253 GLU n 1 254 ILE n 1 255 ALA n 1 256 ASP n 1 257 ILE n 1 258 VAL n 1 259 SER n 1 260 PRO n 1 261 PHE n 1 262 PRO n 1 263 GLU n 1 264 LYS n 1 265 PRO n 1 266 LEU n 1 267 VAL n 1 268 ASP n 1 269 VAL n 1 270 SER n 1 271 ALA n 1 272 GLU n 1 273 MET n 1 274 GLU n 1 275 LYS n 1 276 GLN n 1 277 GLY n 1 278 TYR n 1 279 THR n 1 280 PRO n 1 281 LEU n 1 282 LYS n 1 283 MET n 1 284 PHE n 1 285 GLN n 1 286 MET n 1 287 GLY n 1 288 ASP n 1 289 ASP n 1 290 PHE n 1 291 PHE n 1 292 THR n 1 293 SER n 1 294 MET n 1 295 ASN n 1 296 LEU n 1 297 THR n 1 298 LYS n 1 299 LEU n 1 300 PRO n 1 301 GLN n 1 302 ASP n 1 303 PHE n 1 304 TRP n 1 305 ASP n 1 306 LYS n 1 307 SER n 1 308 ILE n 1 309 ILE n 1 310 GLU n 1 311 LYS n 1 312 PRO n 1 313 THR n 1 314 ASP n 1 315 GLY n 1 316 ARG n 1 317 ASP n 1 318 LEU n 1 319 VAL n 1 320 CYS n 1 321 HIS n 1 322 ALA n 1 323 SER n 1 324 ALA n 1 325 TRP n 1 326 ASP n 1 327 PHE n 1 328 TYR n 1 329 LEU n 1 330 THR n 1 331 ASP n 1 332 ASP n 1 333 VAL n 1 334 ARG n 1 335 ILE n 1 336 LYS n 1 337 GLN n 1 338 CYS n 1 339 THR n 1 340 ARG n 1 341 VAL n 1 342 THR n 1 343 GLN n 1 344 ASP n 1 345 GLN n 1 346 LEU n 1 347 PHE n 1 348 THR n 1 349 VAL n 1 350 HIS n 1 351 HIS n 1 352 GLU n 1 353 LEU n 1 354 GLY n 1 355 HIS n 1 356 ILE n 1 357 GLN n 1 358 TYR n 1 359 PHE n 1 360 LEU n 1 361 GLN n 1 362 TYR n 1 363 GLN n 1 364 HIS n 1 365 GLN n 1 366 PRO n 1 367 PHE n 1 368 VAL n 1 369 TYR n 1 370 ARG n 1 371 THR n 1 372 GLY n 1 373 ALA n 1 374 ASN n 1 375 PRO n 1 376 GLY n 1 377 PHE n 1 378 HIS n 1 379 GLU n 1 380 ALA n 1 381 VAL n 1 382 GLY n 1 383 ASP n 1 384 VAL n 1 385 LEU n 1 386 SER n 1 387 LEU n 1 388 SER n 1 389 VAL n 1 390 SER n 1 391 THR n 1 392 PRO n 1 393 LYS n 1 394 HIS n 1 395 LEU n 1 396 GLU n 1 397 LYS n 1 398 ILE n 1 399 GLY n 1 400 LEU n 1 401 LEU n 1 402 LYS n 1 403 ASP n 1 404 TYR n 1 405 VAL n 1 406 ARG n 1 407 ASP n 1 408 ASP n 1 409 GLU n 1 410 ALA n 1 411 ARG n 1 412 ILE n 1 413 ASN n 1 414 GLN n 1 415 LEU n 1 416 PHE n 1 417 LEU n 1 418 THR n 1 419 ALA n 1 420 LEU n 1 421 ASP n 1 422 LYS n 1 423 ILE n 1 424 VAL n 1 425 PHE n 1 426 LEU n 1 427 PRO n 1 428 PHE n 1 429 ALA n 1 430 PHE n 1 431 THR n 1 432 MET n 1 433 ASP n 1 434 LYS n 1 435 TYR n 1 436 ARG n 1 437 TRP n 1 438 SER n 1 439 LEU n 1 440 PHE n 1 441 ARG n 1 442 GLY n 1 443 GLU n 1 444 VAL n 1 445 ASP n 1 446 LYS n 1 447 ALA n 1 448 ASN n 1 449 TRP n 1 450 ASN n 1 451 CYS n 1 452 ALA n 1 453 PHE n 1 454 TRP n 1 455 LYS n 1 456 LEU n 1 457 ARG n 1 458 ASP n 1 459 GLU n 1 460 TYR n 1 461 SER n 1 462 GLY n 1 463 ILE n 1 464 GLU n 1 465 PRO n 1 466 PRO n 1 467 VAL n 1 468 VAL n 1 469 ARG n 1 470 SER n 1 471 GLU n 1 472 LYS n 1 473 ASP n 1 474 PHE n 1 475 ASP n 1 476 ALA n 1 477 PRO n 1 478 ALA n 1 479 LYS n 1 480 TYR n 1 481 HIS n 1 482 ILE n 1 483 SER n 1 484 ALA n 1 485 ASP n 1 486 VAL n 1 487 GLU n 1 488 TYR n 1 489 LEU n 1 490 ARG n 1 491 TYR n 1 492 LEU n 1 493 VAL n 1 494 SER n 1 495 PHE n 1 496 ILE n 1 497 ILE n 1 498 GLN n 1 499 PHE n 1 500 GLN n 1 501 PHE n 1 502 TYR n 1 503 LYS n 1 504 SER n 1 505 ALA n 1 506 CYS n 1 507 ILE n 1 508 LYS n 1 509 ALA n 1 510 GLY n 1 511 GLN n 1 512 TYR n 1 513 ASP n 1 514 PRO n 1 515 ASP n 1 516 ASN n 1 517 VAL n 1 518 GLU n 1 519 LEU n 1 520 PRO n 1 521 LEU n 1 522 ASP n 1 523 ASN n 1 524 CYS n 1 525 ASP n 1 526 ILE n 1 527 TYR n 1 528 GLY n 1 529 SER n 1 530 ALA n 1 531 ALA n 1 532 ALA n 1 533 GLY n 1 534 ALA n 1 535 ALA n 1 536 PHE n 1 537 HIS n 1 538 ASN n 1 539 MET n 1 540 LEU n 1 541 SER n 1 542 MET n 1 543 GLY n 1 544 ALA n 1 545 SER n 1 546 LYS n 1 547 PRO n 1 548 TRP n 1 549 PRO n 1 550 ASP n 1 551 ALA n 1 552 LEU n 1 553 GLU n 1 554 ALA n 1 555 PHE n 1 556 ASN n 1 557 GLY n 1 558 GLU n 1 559 ARG n 1 560 ILE n 1 561 MET n 1 562 SER n 1 563 GLY n 1 564 LYS n 1 565 ALA n 1 566 ILE n 1 567 ALA n 1 568 GLU n 1 569 TYR n 1 570 PHE n 1 571 GLU n 1 572 PRO n 1 573 LEU n 1 574 ARG n 1 575 VAL n 1 576 TRP n 1 577 LEU n 1 578 GLU n 1 579 ALA n 1 580 GLU n 1 581 ASN n 1 582 ILE n 1 583 LYS n 1 584 ASN n 1 585 ASN n 1 586 VAL n 1 587 HIS n 1 588 ILE n 1 589 GLY n 1 590 TRP n 1 591 THR n 1 592 THR n 1 593 SER n 1 594 ASN n 1 595 LYS n 1 596 CYS n 1 597 VAL n 1 598 SER n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name 'FRUIT FLY' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'DROSOPHILA MELANOGASTER' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 7227 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'PICHIA PASTORIS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code ACE_DROME _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q10714 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4CA7 _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 598 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q10714 _struct_ref_seq.db_align_beg 17 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 614 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 17 _struct_ref_seq.pdbx_auth_seq_align_end 614 # 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 3EF non-polymer . ;N-{(2S)-3-[(S)-[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl]-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tyrosine ; ? 'C38 H38 N3 O9 P' 711.697 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 4CA7 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.2 _exptl_crystal.density_percent_sol 43.8 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '100 MM HEPES 7.5, 1.3 M SODIUM CITRATE' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'DECTRIS PILATUS 2M' _diffrn_detector.pdbx_collection_date 2012-05-03 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.920 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04-1' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04-1 _diffrn_source.pdbx_wavelength 0.920 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CA7 _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 28.96 _reflns.d_resolution_high 1.82 _reflns.number_obs 102293 _reflns.number_all ? _reflns.percent_possible_obs 99.3 _reflns.pdbx_Rmerge_I_obs 0.07 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 15.10 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.6 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.82 _reflns_shell.d_res_low 1.92 _reflns_shell.percent_possible_all 96.7 _reflns_shell.Rmerge_I_obs 0.66 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.50 _reflns_shell.pdbx_redundancy 5.2 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CA7 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 97174 _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 28.88 _refine.ls_d_res_high 1.82 _refine.ls_percent_reflns_obs 99.22 _refine.ls_R_factor_obs 0.17696 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17605 _refine.ls_R_factor_R_free 0.19402 _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 5117 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.969 _refine.correlation_coeff_Fo_to_Fc_free 0.963 _refine.B_iso_mean 28.861 _refine.aniso_B[1][1] -1.78 _refine.aniso_B[2][2] -1.78 _refine.aniso_B[3][3] 5.78 _refine.aniso_B[1][2] -1.78 _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 1.20 _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 2X8Y' _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 0.087 _refine.overall_SU_ML 0.078 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 5.189 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4862 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 152 _refine_hist.number_atoms_solvent 576 _refine_hist.number_atoms_total 5590 _refine_hist.d_res_high 1.82 _refine_hist.d_res_low 28.88 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.008 0.020 ? 5197 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.178 1.976 ? 7061 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.146 5.000 ? 605 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.099 24.677 ? 263 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.843 15.000 ? 863 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 16.949 15.000 ? 25 'X-RAY DIFFRACTION' ? r_chiral_restr 0.082 0.200 ? 755 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.021 ? 3993 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? '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 ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? '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 ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? '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 ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? '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 1.820 _refine_ls_shell.d_res_low 1.868 _refine_ls_shell.number_reflns_R_work 6796 _refine_ls_shell.R_factor_R_work 0.341 _refine_ls_shell.percent_reflns_obs 93.51 _refine_ls_shell.R_factor_R_free 0.346 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 353 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CA7 _struct.title 'Drosophila Angiotensin converting enzyme (AnCE) in complex with a phosphinic tripeptide FI' _struct.pdbx_descriptor 'ANGIOTENSIN-CONVERTING ENZYME (E.C.3.4.15.1)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CA7 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, ZINC METALLOPEPTIDASE, INHIBITOR BINDING' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 5 ? H N N 4 ? I N N 3 ? J N N 3 ? K N N 6 ? L N N 7 ? # _struct_biol.id 1 # 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 ? ILE A 7 ? VAL A 19 ILE A 23 5 ? 5 HELX_P HELX_P2 2 ALA A 9 ? SER A 36 ? ALA A 25 SER A 52 1 ? 28 HELX_P HELX_P3 3 THR A 39 ? THR A 65 ? THR A 55 THR A 81 1 ? 27 HELX_P HELX_P4 4 GLN A 68 ? TYR A 72 ? GLN A 84 TYR A 88 5 ? 5 HELX_P HELX_P5 5 SER A 74 ? LYS A 86 ? SER A 90 LYS A 102 1 ? 13 HELX_P HELX_P6 6 LEU A 87 ? LEU A 92 ? LEU A 103 LEU A 108 5 ? 6 HELX_P HELX_P7 7 PRO A 93 ? VAL A 114 ? PRO A 109 VAL A 130 1 ? 22 HELX_P HELX_P8 8 PRO A 131 ? SER A 140 ? PRO A 147 SER A 156 1 ? 10 HELX_P HELX_P9 9 ASP A 142 ? GLY A 158 ? ASP A 158 GLY A 174 1 ? 17 HELX_P HELX_P10 10 VAL A 161 ? ASN A 179 ? VAL A 177 ASN A 195 1 ? 19 HELX_P HELX_P11 11 SER A 183 ? ASP A 190 ? SER A 199 ASP A 206 1 ? 8 HELX_P HELX_P12 12 GLU A 191 ? GLU A 193 ? GLU A 207 GLU A 209 5 ? 3 HELX_P HELX_P13 13 THR A 196 ? GLY A 228 ? THR A 212 GLY A 244 1 ? 33 HELX_P HELX_P14 14 HIS A 241 ? LEU A 243 ? HIS A 257 LEU A 259 5 ? 3 HELX_P HELX_P15 15 TRP A 251 ? GLU A 253 ? TRP A 267 GLU A 269 5 ? 3 HELX_P HELX_P16 16 ILE A 254 ? SER A 259 ? ILE A 270 SER A 275 1 ? 6 HELX_P HELX_P17 17 VAL A 269 ? GLN A 276 ? VAL A 285 GLN A 292 1 ? 8 HELX_P HELX_P18 18 THR A 279 ? MET A 294 ? THR A 295 MET A 310 1 ? 16 HELX_P HELX_P19 19 PRO A 300 ? SER A 307 ? PRO A 316 SER A 323 1 ? 8 HELX_P HELX_P20 20 THR A 342 ? TYR A 362 ? THR A 358 TYR A 378 1 ? 21 HELX_P HELX_P21 21 PRO A 366 ? ARG A 370 ? PRO A 382 ARG A 386 5 ? 5 HELX_P HELX_P22 22 ASN A 374 ? SER A 390 ? ASN A 390 SER A 406 1 ? 17 HELX_P HELX_P23 23 THR A 391 ? ILE A 398 ? THR A 407 ILE A 414 1 ? 8 HELX_P HELX_P24 24 ASP A 407 ? ILE A 423 ? ASP A 423 ILE A 439 1 ? 17 HELX_P HELX_P25 25 VAL A 424 ? ARG A 441 ? VAL A 440 ARG A 457 1 ? 18 HELX_P HELX_P26 26 ASP A 445 ? ALA A 447 ? ASP A 461 ALA A 463 5 ? 3 HELX_P HELX_P27 27 ASN A 448 ? GLY A 462 ? ASN A 464 GLY A 478 1 ? 15 HELX_P HELX_P28 28 ASP A 475 ? ALA A 478 ? ASP A 491 ALA A 494 5 ? 4 HELX_P HELX_P29 29 LYS A 479 ? ALA A 484 ? LYS A 495 ALA A 500 1 ? 6 HELX_P HELX_P30 30 TYR A 488 ? ALA A 509 ? TYR A 504 ALA A 525 1 ? 22 HELX_P HELX_P31 31 PRO A 520 ? CYS A 524 ? PRO A 536 CYS A 540 5 ? 5 HELX_P HELX_P32 32 SER A 529 ? SER A 541 ? SER A 545 SER A 557 1 ? 13 HELX_P HELX_P33 33 PRO A 547 ? GLY A 557 ? PRO A 563 GLY A 573 1 ? 11 HELX_P HELX_P34 34 GLY A 563 ? ASN A 584 ? GLY A 579 ASN A 600 1 ? 22 # _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 117 SG ? ? ? 1_555 A CYS 125 SG ? ? A CYS 133 A CYS 141 1_555 ? ? ? ? ? ? ? 2.051 ? disulf2 disulf ? ? A CYS 320 SG ? ? ? 1_555 A CYS 338 SG ? ? A CYS 336 A CYS 354 1_555 ? ? ? ? ? ? ? 2.048 ? disulf3 disulf ? ? A CYS 451 SG ? ? ? 1_555 A CYS 596 SG ? ? A CYS 467 A CYS 612 1_555 ? ? ? ? ? ? ? 2.062 ? disulf4 disulf ? ? A CYS 506 SG ? ? ? 1_555 A CYS 524 SG ? ? A CYS 522 A CYS 540 1_555 ? ? ? ? ? ? ? 2.032 ? covale1 covale ? ? A ASN 37 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 53 A NAG 1622 1_555 ? ? ? ? ? ? ? 1.447 ? covale2 covale ? ? A ASN 180 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 196 A NAG 1617 1_555 ? ? ? ? ? ? ? 1.445 ? covale3 covale ? ? A ASN 295 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 311 A NAG 1621 1_555 ? ? ? ? ? ? ? 1.441 ? metalc1 metalc ? ? B ZN . ZN ? ? ? 1_555 A HIS 355 NE2 ? ? A ZN 1616 A HIS 371 1_555 ? ? ? ? ? ? ? 2.108 ? metalc2 metalc ? ? B ZN . ZN ? ? ? 1_555 A HIS 351 NE2 ? ? A ZN 1616 A HIS 367 1_555 ? ? ? ? ? ? ? 2.064 ? metalc3 metalc ? ? B ZN . ZN ? ? ? 1_555 K 3EF . PBY ? ? A ZN 1616 A 3EF 1715 1_555 ? ? ? ? ? ? ? 2.682 ? metalc4 metalc ? ? B ZN . ZN ? ? ? 1_555 K 3EF . OAD ? ? A ZN 1616 A 3EF 1715 1_555 ? ? ? ? ? ? ? 2.235 ? metalc5 metalc ? ? B ZN . ZN ? ? ? 1_555 K 3EF . OAG ? ? A ZN 1616 A 3EF 1715 1_555 ? ? ? ? ? ? ? 2.409 ? metalc6 metalc ? ? B ZN . ZN ? ? ? 1_555 A GLU 379 OE1 ? ? A ZN 1616 A GLU 395 1_555 ? ? ? ? ? ? ? 2.059 ? covale4 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 1617 A NAG 1618 1_555 ? ? ? ? ? ? ? 1.445 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 1618 A BMA 1619 1_555 ? ? ? ? ? ? ? 1.446 ? covale6 covale ? ? E BMA . O6 ? ? ? 1_555 F MAN . C1 ? ? A BMA 1619 A MAN 1620 1_555 ? ? ? ? ? ? ? 1.444 ? covale7 covale ? ? E BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 1619 A MAN 1623 1_555 ? ? ? ? ? ? ? 1.448 ? covale8 covale ? ? G MAN . O6 ? ? ? 1_555 H BMA . C1 ? ? A MAN 1623 A BMA 1624 1_555 ? ? ? ? ? ? ? 1.443 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id ASP _struct_mon_prot_cis.label_seq_id 130 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id ASP _struct_mon_prot_cis.auth_seq_id 146 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 131 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 147 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 7.36 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 2 ? AB ? 2 ? AC ? 2 ? AD ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? anti-parallel AB 1 2 ? parallel AC 1 2 ? anti-parallel AD 1 2 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 LYS A 115 ? VAL A 116 ? LYS A 131 VAL A 132 AA 2 LEU A 127 ? ALA A 128 ? LEU A 143 ALA A 144 AB 1 ILE A 238 ? PRO A 239 ? ILE A 254 PRO A 255 AB 2 ILE A 463 ? GLU A 464 ? ILE A 479 GLU A 480 AC 1 SER A 323 ? ASP A 326 ? SER A 339 ASP A 342 AC 2 VAL A 333 ? LYS A 336 ? VAL A 349 LYS A 352 AD 1 ARG A 469 ? SER A 470 ? ARG A 485 SER A 486 AD 2 CYS A 596 ? VAL A 597 ? CYS A 612 VAL A 613 # 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 AA 1 2 N VAL A 116 ? N VAL A 132 O LEU A 127 ? O LEU A 143 AB 1 2 O ILE A 238 ? O ILE A 254 N GLU A 464 ? N GLU A 480 AC 1 2 N TRP A 325 ? N TRP A 341 O ARG A 334 ? O ARG A 350 AD 1 2 O ARG A 469 ? O ARG A 485 N VAL A 597 ? N VAL A 613 # 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 1616' AC2 Software ? ? ? ? 28 'BINDING SITE FOR RESIDUE 3EF A 1715' AC3 Software ? ? ? ? 6 'Binding site for Mono-Saccharide NAG A1622 bound to ASN A 53' AC4 Software ? ? ? ? 17 'Binding site for Poly-Saccharide residues NAG A1617 through BMA A1624 bound to ASN A 196' AC5 Software ? ? ? ? 2 'Binding site for Mono-Saccharide NAG A1621 bound to ASN A 311' # 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 4 HIS A 351 ? HIS A 367 . ? 1_555 ? 2 AC1 4 HIS A 355 ? HIS A 371 . ? 1_555 ? 3 AC1 4 GLU A 379 ? GLU A 395 . ? 1_555 ? 4 AC1 4 3EF K . ? 3EF A 1715 . ? 1_555 ? 5 AC2 28 GLN A 249 ? GLN A 265 . ? 1_555 ? 6 AC2 28 GLN A 250 ? GLN A 266 . ? 1_555 ? 7 AC2 28 HIS A 321 ? HIS A 337 . ? 1_555 ? 8 AC2 28 ALA A 322 ? ALA A 338 . ? 1_555 ? 9 AC2 28 SER A 323 ? SER A 339 . ? 1_555 ? 10 AC2 28 ALA A 324 ? ALA A 340 . ? 1_555 ? 11 AC2 28 ASP A 344 ? ASP A 360 . ? 1_555 ? 12 AC2 28 PHE A 347 ? PHE A 363 . ? 1_555 ? 13 AC2 28 THR A 348 ? THR A 364 . ? 1_555 ? 14 AC2 28 HIS A 351 ? HIS A 367 . ? 1_555 ? 15 AC2 28 GLU A 352 ? GLU A 368 . ? 1_555 ? 16 AC2 28 HIS A 355 ? HIS A 371 . ? 1_555 ? 17 AC2 28 PHE A 359 ? PHE A 375 . ? 1_555 ? 18 AC2 28 HIS A 378 ? HIS A 394 . ? 1_555 ? 19 AC2 28 GLU A 379 ? GLU A 395 . ? 1_555 ? 20 AC2 28 ASP A 383 ? ASP A 399 . ? 1_555 ? 21 AC2 28 LYS A 479 ? LYS A 495 . ? 1_555 ? 22 AC2 28 TYR A 480 ? TYR A 496 . ? 1_555 ? 23 AC2 28 HIS A 481 ? HIS A 497 . ? 1_555 ? 24 AC2 28 VAL A 486 ? VAL A 502 . ? 1_555 ? 25 AC2 28 TYR A 488 ? TYR A 504 . ? 1_555 ? 26 AC2 28 TYR A 491 ? TYR A 507 . ? 1_555 ? 27 AC2 28 PHE A 495 ? PHE A 511 . ? 1_555 ? 28 AC2 28 ZN B . ? ZN A 1616 . ? 1_555 ? 29 AC2 28 HOH L . ? HOH A 2326 . ? 1_555 ? 30 AC2 28 HOH L . ? HOH A 2327 . ? 1_555 ? 31 AC2 28 HOH L . ? HOH A 2429 . ? 1_555 ? 32 AC2 28 HOH L . ? HOH A 2566 . ? 1_555 ? 33 AC3 6 ASN A 37 ? ASN A 53 . ? 1_555 ? 34 AC3 6 THR A 39 ? THR A 55 . ? 1_555 ? 35 AC3 6 GLU A 41 ? GLU A 57 . ? 1_555 ? 36 AC3 6 ASN A 42 ? ASN A 58 . ? 1_555 ? 37 AC3 6 ASP A 314 ? ASP A 330 . ? 1_555 ? 38 AC3 6 ARG A 316 ? ARG A 332 . ? 1_555 ? 39 AC4 17 GLN A 68 ? GLN A 84 . ? 1_555 ? 40 AC4 17 ARG A 141 ? ARG A 157 . ? 6_555 ? 41 AC4 17 HIS A 143 ? HIS A 159 . ? 6_555 ? 42 AC4 17 ASN A 180 ? ASN A 196 . ? 1_555 ? 43 AC4 17 ARG A 222 ? ARG A 238 . ? 6_555 ? 44 AC4 17 LYS A 225 ? LYS A 241 . ? 6_555 ? 45 AC4 17 HIS A 226 ? HIS A 242 . ? 6_555 ? 46 AC4 17 TYR A 227 ? TYR A 243 . ? 6_555 ? 47 AC4 17 PRO A 262 ? PRO A 278 . ? 6_555 ? 48 AC4 17 HOH L . ? HOH A 2306 . ? 6_555 ? 49 AC4 17 HOH L . ? HOH A 2332 . ? 6_555 ? 50 AC4 17 HOH L . ? HOH A 2568 . ? 1_555 ? 51 AC4 17 HOH L . ? HOH A 2569 . ? 1_555 ? 52 AC4 17 HOH L . ? HOH A 2570 . ? 1_555 ? 53 AC4 17 HOH L . ? HOH A 2572 . ? 1_555 ? 54 AC4 17 HOH L . ? HOH A 2573 . ? 1_555 ? 55 AC4 17 HOH L . ? HOH A 2575 . ? 1_555 ? 56 AC5 2 ASN A 295 ? ASN A 311 . ? 1_555 ? 57 AC5 2 ALA A 530 ? ALA A 546 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CA7 _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 4CA7 _atom_sites.fract_transf_matrix[1][1] 0.005756 _atom_sites.fract_transf_matrix[1][2] 0.003323 _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] 0.006646 _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] 0.009787 _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 P S ZN # 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 . VAL A 1 3 ? 26.456 24.134 44.433 1.00 64.18 ? 19 VAL A N 1 ATOM 2 C CA . VAL A 1 3 ? 26.156 25.548 44.048 1.00 67.84 ? 19 VAL A CA 1 ATOM 3 C C . VAL A 1 3 ? 24.658 25.703 43.733 1.00 66.63 ? 19 VAL A C 1 ATOM 4 O O . VAL A 1 3 ? 24.058 24.816 43.123 1.00 65.71 ? 19 VAL A O 1 ATOM 5 C CB . VAL A 1 3 ? 27.019 26.005 42.840 1.00 69.17 ? 19 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 3 ? 26.990 27.525 42.694 1.00 71.16 ? 19 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 3 ? 28.459 25.525 42.989 1.00 68.77 ? 19 VAL A CG2 1 ATOM 8 N N . LYS A 1 4 ? 24.067 26.826 44.151 1.00 65.44 ? 20 LYS A N 1 ATOM 9 C CA . LYS A 1 4 ? 22.629 27.106 43.946 1.00 62.98 ? 20 LYS A CA 1 ATOM 10 C C . LYS A 1 4 ? 22.268 27.371 42.472 1.00 58.00 ? 20 LYS A C 1 ATOM 11 O O . LYS A 1 4 ? 21.095 27.324 42.079 1.00 56.69 ? 20 LYS A O 1 ATOM 12 C CB . LYS A 1 4 ? 22.182 28.278 44.829 1.00 67.23 ? 20 LYS A CB 1 ATOM 13 C CG . LYS A 1 4 ? 22.478 28.088 46.313 1.00 70.82 ? 20 LYS A CG 1 ATOM 14 C CD . LYS A 1 4 ? 21.876 29.199 47.161 1.00 73.89 ? 20 LYS A CD 1 ATOM 15 C CE . LYS A 1 4 ? 22.069 28.921 48.645 1.00 74.69 ? 20 LYS A CE 1 ATOM 16 N NZ . LYS A 1 4 ? 21.434 29.968 49.491 1.00 76.09 ? 20 LYS A NZ 1 ATOM 17 N N . GLU A 1 5 ? 23.303 27.654 41.681 1.00 53.34 ? 21 GLU A N 1 ATOM 18 C CA . GLU A 1 5 ? 23.240 27.797 40.224 1.00 48.08 ? 21 GLU A CA 1 ATOM 19 C C . GLU A 1 5 ? 22.814 26.488 39.537 1.00 44.21 ? 21 GLU A C 1 ATOM 20 O O . GLU A 1 5 ? 22.322 26.507 38.402 1.00 41.60 ? 21 GLU A O 1 ATOM 21 C CB . GLU A 1 5 ? 24.621 28.244 39.724 1.00 47.40 ? 21 GLU A CB 1 ATOM 22 C CG . GLU A 1 5 ? 24.778 28.436 38.226 1.00 46.36 ? 21 GLU A CG 1 ATOM 23 C CD . GLU A 1 5 ? 26.217 28.740 37.846 1.00 46.67 ? 21 GLU A CD 1 ATOM 24 O OE1 . GLU A 1 5 ? 26.685 29.854 38.162 1.00 46.71 ? 21 GLU A OE1 1 ATOM 25 O OE2 . GLU A 1 5 ? 26.884 27.870 37.239 1.00 44.38 ? 21 GLU A OE2 1 ATOM 26 N N . GLU A 1 6 ? 23.002 25.364 40.235 1.00 41.42 ? 22 GLU A N 1 ATOM 27 C CA . GLU A 1 6 ? 22.610 24.040 39.734 1.00 39.94 ? 22 GLU A CA 1 ATOM 28 C C . GLU A 1 6 ? 21.126 23.918 39.408 1.00 38.73 ? 22 GLU A C 1 ATOM 29 O O . GLU A 1 6 ? 20.751 23.090 38.576 1.00 38.42 ? 22 GLU A O 1 ATOM 30 C CB . GLU A 1 6 ? 23.028 22.921 40.697 1.00 38.81 ? 22 GLU A CB 1 ATOM 31 C CG . GLU A 1 6 ? 24.518 22.652 40.671 1.00 37.90 ? 22 GLU A CG 1 ATOM 32 C CD . GLU A 1 6 ? 24.944 21.496 41.553 1.00 37.26 ? 22 GLU A CD 1 ATOM 33 O OE1 . GLU A 1 6 ? 24.572 20.338 41.252 1.00 35.78 ? 22 GLU A OE1 1 ATOM 34 O OE2 . GLU A 1 6 ? 25.670 21.750 42.540 1.00 37.31 ? 22 GLU A OE2 1 ATOM 35 N N . ILE A 1 7 ? 20.291 24.733 40.056 1.00 38.31 ? 23 ILE A N 1 ATOM 36 C CA . ILE A 1 7 ? 18.856 24.770 39.746 1.00 38.18 ? 23 ILE A CA 1 ATOM 37 C C . ILE A 1 7 ? 18.647 25.309 38.330 1.00 37.06 ? 23 ILE A C 1 ATOM 38 O O . ILE A 1 7 ? 17.987 24.665 37.518 1.00 36.87 ? 23 ILE A O 1 ATOM 39 C CB . ILE A 1 7 ? 18.028 25.613 40.757 1.00 39.57 ? 23 ILE A CB 1 ATOM 40 C CG1 . ILE A 1 7 ? 18.349 25.243 42.219 1.00 40.19 ? 23 ILE A CG1 1 ATOM 41 C CG2 . ILE A 1 7 ? 16.530 25.495 40.461 1.00 39.49 ? 23 ILE A CG2 1 ATOM 42 C CD1 . ILE A 1 7 ? 18.036 23.808 42.611 1.00 40.52 ? 23 ILE A CD1 1 ATOM 43 N N . GLN A 1 8 ? 19.208 26.446 38.025 1.00 39.10 ? 24 GLN A N 1 ATOM 44 C CA . GLN A 1 8 ? 19.100 27.028 36.680 1.00 40.01 ? 24 GLN A CA 1 ATOM 45 C CB . GLN A 1 8 ? 19.689 28.435 36.640 1.00 43.02 ? 24 GLN A CB 1 ATOM 46 C CG . GLN A 1 8 ? 18.999 29.422 37.570 1.00 48.71 ? 24 GLN A CG 1 ATOM 47 C CD . GLN A 1 8 ? 19.876 30.607 37.936 1.00 52.68 ? 24 GLN A CD 1 ATOM 48 O OE1 . GLN A 1 8 ? 19.403 31.566 38.549 1.00 57.73 ? 24 GLN A OE1 1 ATOM 49 N NE2 . GLN A 1 8 ? 21.157 30.549 37.566 1.00 53.29 ? 24 GLN A NE2 1 ATOM 50 N N . ALA A 1 9 ? 20.925 25.584 35.989 1.00 33.51 ? 25 ALA A N 1 ATOM 51 C CA . ALA A 1 9 ? 21.666 24.702 35.078 1.00 33.29 ? 25 ALA A CA 1 ATOM 52 C C . ALA A 1 9 ? 20.836 23.507 34.603 1.00 33.27 ? 25 ALA A C 1 ATOM 53 O O . ALA A 1 9 ? 20.863 23.163 33.420 1.00 33.55 ? 25 ALA A O 1 ATOM 54 C CB . ALA A 1 9 ? 22.956 24.227 35.733 1.00 32.23 ? 25 ALA A CB 1 ATOM 55 N N . LYS A 1 10 ? 20.105 22.884 35.526 1.00 34.16 ? 26 LYS A N 1 ATOM 56 C CA . LYS A 1 10 ? 19.247 21.745 35.214 1.00 36.05 ? 26 LYS A CA 1 ATOM 57 C C . LYS A 1 10 ? 18.149 22.103 34.197 1.00 36.30 ? 26 LYS A C 1 ATOM 58 O O . LYS A 1 10 ? 17.859 21.327 33.282 1.00 35.06 ? 26 LYS A O 1 ATOM 59 C CB . LYS A 1 10 ? 18.631 21.177 36.494 1.00 37.80 ? 26 LYS A CB 1 ATOM 60 C CG . LYS A 1 10 ? 17.903 19.856 36.289 1.00 40.64 ? 26 LYS A CG 1 ATOM 61 C CD . LYS A 1 10 ? 17.258 19.370 37.572 1.00 43.35 ? 26 LYS A CD 1 ATOM 62 C CE . LYS A 1 10 ? 16.866 17.909 37.446 1.00 46.05 ? 26 LYS A CE 1 ATOM 63 N NZ . LYS A 1 10 ? 16.376 17.385 38.750 1.00 48.74 ? 26 LYS A NZ 1 ATOM 64 N N . GLU A 1 11 ? 17.555 23.284 34.360 1.00 36.89 ? 27 GLU A N 1 ATOM 65 C CA . GLU A 1 11 ? 16.539 23.792 33.437 1.00 37.28 ? 27 GLU A CA 1 ATOM 66 C C . GLU A 1 11 ? 17.150 24.124 32.081 1.00 35.29 ? 27 GLU A C 1 ATOM 67 O O . GLU A 1 11 ? 16.539 23.878 31.041 1.00 34.04 ? 27 GLU A O 1 ATOM 68 C CB . GLU A 1 11 ? 15.843 25.026 34.027 1.00 41.29 ? 27 GLU A CB 1 ATOM 69 C CG . GLU A 1 11 ? 14.920 24.707 35.199 1.00 46.11 ? 27 GLU A CG 1 ATOM 70 C CD . GLU A 1 11 ? 14.463 25.940 35.977 1.00 51.09 ? 27 GLU A CD 1 ATOM 71 O OE1 . GLU A 1 11 ? 14.759 27.087 35.561 1.00 52.56 ? 27 GLU A OE1 1 ATOM 72 O OE2 . GLU A 1 11 ? 13.805 25.759 37.026 1.00 53.11 ? 27 GLU A OE2 1 ATOM 73 N N . TYR A 1 12 ? 18.357 24.685 32.101 1.00 33.81 ? 28 TYR A N 1 ATOM 74 C CA . TYR A 1 12 ? 19.112 24.951 30.876 1.00 33.00 ? 28 TYR A CA 1 ATOM 75 C C . TYR A 1 12 ? 19.327 23.671 30.052 1.00 31.96 ? 28 TYR A C 1 ATOM 76 O O . TYR A 1 12 ? 19.095 23.665 28.837 1.00 30.60 ? 28 TYR A O 1 ATOM 77 C CB . TYR A 1 12 ? 20.454 25.625 31.194 1.00 33.14 ? 28 TYR A CB 1 ATOM 78 C CG . TYR A 1 12 ? 21.365 25.777 29.995 1.00 33.58 ? 28 TYR A CG 1 ATOM 79 C CD1 . TYR A 1 12 ? 21.188 26.821 29.086 1.00 34.49 ? 28 TYR A CD1 1 ATOM 80 C CD2 . TYR A 1 12 ? 22.401 24.871 29.766 1.00 33.56 ? 28 TYR A CD2 1 ATOM 81 C CE1 . TYR A 1 12 ? 22.018 26.959 27.981 1.00 34.63 ? 28 TYR A CE1 1 ATOM 82 C CE2 . TYR A 1 12 ? 23.234 24.998 28.664 1.00 34.04 ? 28 TYR A CE2 1 ATOM 83 C CZ . TYR A 1 12 ? 23.041 26.041 27.776 1.00 34.89 ? 28 TYR A CZ 1 ATOM 84 O OH . TYR A 1 12 ? 23.874 26.163 26.684 1.00 35.67 ? 28 TYR A OH 1 ATOM 85 N N . LEU A 1 13 ? 19.762 22.602 30.721 1.00 30.91 ? 29 LEU A N 1 ATOM 86 C CA . LEU A 1 13 ? 20.050 21.325 30.060 1.00 31.12 ? 29 LEU A CA 1 ATOM 87 C C . LEU A 1 13 ? 18.784 20.674 29.510 1.00 32.62 ? 29 LEU A C 1 ATOM 88 O O . LEU A 1 13 ? 18.800 20.092 28.417 1.00 31.27 ? 29 LEU A O 1 ATOM 89 C CB . LEU A 1 13 ? 20.760 20.365 31.016 1.00 30.05 ? 29 LEU A CB 1 ATOM 90 C CG . LEU A 1 13 ? 22.217 20.664 31.386 1.00 29.77 ? 29 LEU A CG 1 ATOM 91 C CD1 . LEU A 1 13 ? 22.675 19.689 32.452 1.00 29.85 ? 29 LEU A CD1 1 ATOM 92 C CD2 . LEU A 1 13 ? 23.140 20.594 30.178 1.00 29.37 ? 29 LEU A CD2 1 ATOM 93 N N . GLU A 1 14 ? 17.698 20.781 30.274 1.00 34.35 ? 30 GLU A N 1 ATOM 94 C CA . GLU A 1 14 ? 16.389 20.286 29.855 1.00 37.26 ? 30 GLU A CA 1 ATOM 95 C C . GLU A 1 14 ? 15.992 20.814 28.478 1.00 36.00 ? 30 GLU A C 1 ATOM 96 O O . GLU A 1 14 ? 15.722 20.024 27.572 1.00 35.52 ? 30 GLU A O 1 ATOM 97 C CB . GLU A 1 14 ? 15.321 20.652 30.889 1.00 42.26 ? 30 GLU A CB 1 ATOM 98 C CG . GLU A 1 14 ? 15.076 19.593 31.953 1.00 48.15 ? 30 GLU A CG 1 ATOM 99 C CD . GLU A 1 14 ? 14.073 18.536 31.512 1.00 53.91 ? 30 GLU A CD 1 ATOM 100 O OE1 . GLU A 1 14 ? 13.081 18.885 30.822 1.00 56.70 ? 30 GLU A OE1 1 ATOM 101 O OE2 . GLU A 1 14 ? 14.275 17.347 31.858 1.00 57.38 ? 30 GLU A OE2 1 ATOM 102 N N . ASN A 1 15 ? 15.974 22.142 28.327 1.00 35.09 ? 31 ASN A N 1 ATOM 103 C CA A ASN A 1 15 ? 15.607 22.776 27.062 0.50 35.15 ? 31 ASN A CA 1 ATOM 104 C CA B ASN A 1 15 ? 15.608 22.780 27.056 0.50 34.90 ? 31 ASN A CA 1 ATOM 105 C C . ASN A 1 15 ? 16.603 22.474 25.942 1.00 34.01 ? 31 ASN A C 1 ATOM 106 O O . ASN A 1 15 ? 16.206 22.162 24.824 1.00 33.91 ? 31 ASN A O 1 ATOM 107 C CB A ASN A 1 15 ? 15.448 24.289 27.243 0.50 35.64 ? 31 ASN A CB 1 ATOM 108 C CB B ASN A 1 15 ? 15.444 24.301 27.214 0.50 34.93 ? 31 ASN A CB 1 ATOM 109 C CG A ASN A 1 15 ? 14.373 24.647 28.250 0.50 36.41 ? 31 ASN A CG 1 ATOM 110 C CG B ASN A 1 15 ? 15.086 24.995 25.904 0.50 35.05 ? 31 ASN A CG 1 ATOM 111 O OD1 A ASN A 1 15 ? 13.541 23.814 28.610 0.50 37.24 ? 31 ASN A OD1 1 ATOM 112 O OD1 B ASN A 1 15 ? 13.919 25.259 25.632 0.50 35.24 ? 31 ASN A OD1 1 ATOM 113 N ND2 A ASN A 1 15 ? 14.384 25.889 28.708 0.50 36.72 ? 31 ASN A ND2 1 ATOM 114 N ND2 B ASN A 1 15 ? 16.096 25.289 25.086 0.50 35.23 ? 31 ASN A ND2 1 ATOM 115 N N . LEU A 1 16 ? 17.893 22.570 26.256 1.00 33.14 ? 32 LEU A N 1 ATOM 116 C CA . LEU A 1 16 ? 18.950 22.332 25.277 1.00 32.50 ? 32 LEU A CA 1 ATOM 117 C C . LEU A 1 16 ? 18.944 20.906 24.708 1.00 32.06 ? 32 LEU A C 1 ATOM 118 O O . LEU A 1 16 ? 19.071 20.728 23.499 1.00 30.39 ? 32 LEU A O 1 ATOM 119 C CB . LEU A 1 16 ? 20.323 22.656 25.867 1.00 32.14 ? 32 LEU A CB 1 ATOM 120 C CG . LEU A 1 16 ? 21.517 22.537 24.918 1.00 32.50 ? 32 LEU A CG 1 ATOM 121 C CD1 . LEU A 1 16 ? 21.337 23.420 23.692 1.00 32.87 ? 32 LEU A CD1 1 ATOM 122 C CD2 . LEU A 1 16 ? 22.788 22.907 25.660 1.00 32.89 ? 32 LEU A CD2 1 ATOM 123 N N . ASN A 1 17 ? 18.813 19.903 25.576 1.00 32.08 ? 33 ASN A N 1 ATOM 124 C CA . ASN A 1 17 ? 18.719 18.512 25.116 1.00 32.60 ? 33 ASN A CA 1 ATOM 125 C C . ASN A 1 17 ? 17.575 18.345 24.114 1.00 33.11 ? 33 ASN A C 1 ATOM 126 O O . ASN A 1 17 ? 17.767 17.816 23.016 1.00 33.39 ? 33 ASN A O 1 ATOM 127 C CB . ASN A 1 17 ? 18.590 17.539 26.301 1.00 31.65 ? 33 ASN A CB 1 ATOM 128 C CG . ASN A 1 17 ? 19.946 17.129 26.876 1.00 31.46 ? 33 ASN A CG 1 ATOM 129 O OD1 . ASN A 1 17 ? 20.805 16.588 26.169 1.00 29.62 ? 33 ASN A OD1 1 ATOM 130 N ND2 . ASN A 1 17 ? 20.138 17.373 28.173 1.00 31.36 ? 33 ASN A ND2 1 ATOM 131 N N . LYS A 1 18 ? 16.397 18.850 24.473 1.00 34.81 ? 34 LYS A N 1 ATOM 132 C CA . LYS A 1 18 ? 15.231 18.799 23.582 1.00 34.88 ? 34 LYS A CA 1 ATOM 133 C C . LYS A 1 18 ? 15.461 19.547 22.270 1.00 33.93 ? 34 LYS A C 1 ATOM 134 O O . LYS A 1 18 ? 15.069 19.080 21.198 1.00 33.49 ? 34 LYS A O 1 ATOM 135 C CB . LYS A 1 18 ? 13.972 19.293 24.303 1.00 37.90 ? 34 LYS A CB 1 ATOM 136 C CG . LYS A 1 18 ? 13.405 18.257 25.273 1.00 40.03 ? 34 LYS A CG 1 ATOM 137 C CD . LYS A 1 18 ? 12.127 18.717 25.956 1.00 43.12 ? 34 LYS A CD 1 ATOM 138 C CE . LYS A 1 18 ? 12.423 19.534 27.204 1.00 44.94 ? 34 LYS A CE 1 ATOM 139 N NZ . LYS A 1 18 ? 11.184 20.039 27.855 1.00 48.31 ? 34 LYS A NZ 1 ATOM 140 N N . GLU A 1 19 ? 16.119 20.697 22.348 1.00 32.60 ? 35 GLU A N 1 ATOM 141 C CA . GLU A 1 19 ? 16.494 21.430 21.148 1.00 31.70 ? 35 GLU A CA 1 ATOM 142 C C . GLU A 1 19 ? 17.507 20.673 20.253 1.00 30.67 ? 35 GLU A C 1 ATOM 143 O O . GLU A 1 19 ? 17.389 20.687 19.024 1.00 29.47 ? 35 GLU A O 1 ATOM 144 C CB . GLU A 1 19 ? 17.024 22.807 21.532 1.00 32.68 ? 35 GLU A CB 1 ATOM 145 C CG . GLU A 1 19 ? 17.721 23.529 20.408 1.00 34.34 ? 35 GLU A CG 1 ATOM 146 C CD . GLU A 1 19 ? 17.492 25.012 20.466 1.00 36.35 ? 35 GLU A CD 1 ATOM 147 O OE1 . GLU A 1 19 ? 17.380 25.538 21.595 1.00 37.41 ? 35 GLU A OE1 1 ATOM 148 O OE2 . GLU A 1 19 ? 17.424 25.641 19.383 1.00 37.41 ? 35 GLU A OE2 1 ATOM 149 N N . LEU A 1 20 ? 18.502 20.032 20.863 1.00 28.89 ? 36 LEU A N 1 ATOM 150 C CA . LEU A 1 20 ? 19.477 19.254 20.099 1.00 28.33 ? 36 LEU A CA 1 ATOM 151 C C . LEU A 1 20 ? 18.837 18.077 19.356 1.00 28.19 ? 36 LEU A C 1 ATOM 152 O O . LEU A 1 20 ? 19.176 17.810 18.206 1.00 27.44 ? 36 LEU A O 1 ATOM 153 C CB . LEU A 1 20 ? 20.628 18.774 20.992 1.00 28.06 ? 36 LEU A CB 1 ATOM 154 C CG . LEU A 1 20 ? 21.582 19.892 21.420 1.00 28.75 ? 36 LEU A CG 1 ATOM 155 C CD1 . LEU A 1 20 ? 22.521 19.441 22.530 1.00 28.21 ? 36 LEU A CD1 1 ATOM 156 C CD2 . LEU A 1 20 ? 22.370 20.429 20.233 1.00 28.47 ? 36 LEU A CD2 1 ATOM 157 N N . ALA A 1 21 ? 17.912 17.389 20.017 1.00 28.16 ? 37 ALA A N 1 ATOM 158 C CA . ALA A 1 21 ? 17.183 16.267 19.413 1.00 28.45 ? 37 ALA A CA 1 ATOM 159 C C . ALA A 1 21 ? 16.455 16.693 18.130 1.00 28.96 ? 37 ALA A C 1 ATOM 160 O O . ALA A 1 21 ? 16.543 16.032 17.092 1.00 28.30 ? 37 ALA A O 1 ATOM 161 C CB . ALA A 1 21 ? 16.207 15.681 20.424 1.00 28.91 ? 37 ALA A CB 1 ATOM 162 N N . LYS A 1 22 ? 15.775 17.834 18.201 1.00 29.11 ? 38 LYS A N 1 ATOM 163 C CA . LYS A 1 22 ? 15.001 18.337 17.081 1.00 29.84 ? 38 LYS A CA 1 ATOM 164 C C . LYS A 1 22 ? 15.877 18.805 15.911 1.00 29.70 ? 38 LYS A C 1 ATOM 165 O O . LYS A 1 22 ? 15.569 18.533 14.746 1.00 29.96 ? 38 LYS A O 1 ATOM 166 C CB . LYS A 1 22 ? 14.090 19.471 17.573 1.00 30.89 ? 38 LYS A CB 1 ATOM 167 C CG . LYS A 1 22 ? 12.946 19.788 16.651 1.00 31.16 ? 38 LYS A CG 1 ATOM 168 C CD . LYS A 1 22 ? 11.932 18.657 16.591 1.00 30.60 ? 38 LYS A CD 1 ATOM 169 C CE . LYS A 1 22 ? 10.571 19.238 16.230 1.00 30.64 ? 38 LYS A CE 1 ATOM 170 N NZ . LYS A 1 22 ? 9.830 18.328 15.324 1.00 30.51 ? 38 LYS A NZ 1 ATOM 171 N N . ARG A 1 23 ? 16.960 19.511 16.223 1.00 29.27 ? 39 ARG A N 1 ATOM 172 C CA . ARG A 1 23 ? 17.917 19.942 15.211 1.00 29.66 ? 39 ARG A CA 1 ATOM 173 C C . ARG A 1 23 ? 18.608 18.735 14.566 1.00 30.01 ? 39 ARG A C 1 ATOM 174 O O . ARG A 1 23 ? 18.830 18.721 13.353 1.00 30.41 ? 39 ARG A O 1 ATOM 175 C CB . ARG A 1 23 ? 18.953 20.902 15.806 1.00 28.90 ? 39 ARG A CB 1 ATOM 176 C CG . ARG A 1 23 ? 18.434 22.319 16.009 1.00 28.94 ? 39 ARG A CG 1 ATOM 177 C CD . ARG A 1 23 ? 19.398 23.156 16.837 1.00 29.17 ? 39 ARG A CD 1 ATOM 178 N NE . ARG A 1 23 ? 18.836 24.474 17.112 1.00 29.46 ? 39 ARG A NE 1 ATOM 179 C CZ . ARG A 1 23 ? 18.987 25.543 16.333 1.00 29.70 ? 39 ARG A CZ 1 ATOM 180 N NH1 . ARG A 1 23 ? 19.704 25.471 15.217 1.00 29.33 ? 39 ARG A NH1 1 ATOM 181 N NH2 . ARG A 1 23 ? 18.419 26.693 16.680 1.00 30.03 ? 39 ARG A NH2 1 ATOM 182 N N . THR A 1 24 ? 18.919 17.724 15.371 1.00 29.78 ? 40 THR A N 1 ATOM 183 C CA . THR A 1 24 ? 19.585 16.514 14.867 1.00 30.69 ? 40 THR A CA 1 ATOM 184 C C . THR A 1 24 ? 18.636 15.670 14.005 1.00 30.95 ? 40 THR A C 1 ATOM 185 O O . THR A 1 24 ? 19.065 15.052 13.028 1.00 31.28 ? 40 THR A O 1 ATOM 186 C CB . THR A 1 24 ? 20.214 15.681 16.008 1.00 30.02 ? 40 THR A CB 1 ATOM 187 O OG1 . THR A 1 24 ? 21.006 16.543 16.837 1.00 29.93 ? 40 THR A OG1 1 ATOM 188 C CG2 . THR A 1 24 ? 21.126 14.578 15.449 1.00 29.97 ? 40 THR A CG2 1 ATOM 189 N N . ASN A 1 25 ? 17.348 15.668 14.354 1.00 31.33 ? 41 ASN A N 1 ATOM 190 C CA . ASN A 1 25 ? 16.331 15.038 13.508 1.00 31.06 ? 41 ASN A CA 1 ATOM 191 C C . ASN A 1 25 ? 16.424 15.531 12.062 1.00 31.66 ? 41 ASN A C 1 ATOM 192 O O . ASN A 1 25 ? 16.418 14.726 11.127 1.00 30.98 ? 41 ASN A O 1 ATOM 193 C CB . ASN A 1 25 ? 14.927 15.266 14.067 1.00 31.68 ? 41 ASN A CB 1 ATOM 194 C CG . ASN A 1 25 ? 13.843 14.739 13.145 1.00 32.71 ? 41 ASN A CG 1 ATOM 195 O OD1 . ASN A 1 25 ? 13.263 15.498 12.373 1.00 33.39 ? 41 ASN A OD1 1 ATOM 196 N ND2 . ASN A 1 25 ? 13.589 13.434 13.197 1.00 31.85 ? 41 ASN A ND2 1 ATOM 197 N N . VAL A 1 26 ? 16.536 16.848 11.897 1.00 31.78 ? 42 VAL A N 1 ATOM 198 C CA . VAL A 1 26 ? 16.617 17.497 10.592 1.00 32.87 ? 42 VAL A CA 1 ATOM 199 C C . VAL A 1 26 ? 17.881 17.088 9.809 1.00 32.27 ? 42 VAL A C 1 ATOM 200 O O . VAL A 1 26 ? 17.799 16.765 8.615 1.00 32.12 ? 42 VAL A O 1 ATOM 201 C CB . VAL A 1 26 ? 16.519 19.040 10.736 1.00 34.16 ? 42 VAL A CB 1 ATOM 202 C CG1 . VAL A 1 26 ? 16.785 19.736 9.407 1.00 34.97 ? 42 VAL A CG1 1 ATOM 203 C CG2 . VAL A 1 26 ? 15.152 19.436 11.289 1.00 34.43 ? 42 VAL A CG2 1 ATOM 204 N N . GLU A 1 27 ? 19.036 17.099 10.474 1.00 30.98 ? 43 GLU A N 1 ATOM 205 C CA . GLU A 1 27 ? 20.285 16.658 9.850 1.00 30.25 ? 43 GLU A CA 1 ATOM 206 C C . GLU A 1 27 ? 20.181 15.191 9.437 1.00 29.12 ? 43 GLU A C 1 ATOM 207 O O . GLU A 1 27 ? 20.575 14.825 8.329 1.00 28.38 ? 43 GLU A O 1 ATOM 208 C CB . GLU A 1 27 ? 21.484 16.852 10.794 1.00 31.26 ? 43 GLU A CB 1 ATOM 209 C CG . GLU A 1 27 ? 22.826 16.493 10.167 1.00 32.28 ? 43 GLU A CG 1 ATOM 210 C CD . GLU A 1 27 ? 23.957 16.354 11.180 1.00 34.68 ? 43 GLU A CD 1 ATOM 211 O OE1 . GLU A 1 27 ? 23.732 15.769 12.270 1.00 35.18 ? 43 GLU A OE1 1 ATOM 212 O OE2 . GLU A 1 27 ? 25.081 16.829 10.879 1.00 34.46 ? 43 GLU A OE2 1 ATOM 213 N N . THR A 1 28 ? 19.633 14.369 10.331 1.00 28.36 ? 44 THR A N 1 ATOM 214 C CA . THR A 1 28 ? 19.512 12.931 10.092 1.00 28.39 ? 44 THR A CA 1 ATOM 215 C C . THR A 1 28 ? 18.637 12.632 8.864 1.00 29.05 ? 44 THR A C 1 ATOM 216 O O . THR A 1 28 ? 18.974 11.753 8.071 1.00 28.92 ? 44 THR A O 1 ATOM 217 C CB . THR A 1 28 ? 19.017 12.179 11.343 1.00 27.83 ? 44 THR A CB 1 ATOM 218 O OG1 . THR A 1 28 ? 19.842 12.535 12.452 1.00 27.07 ? 44 THR A OG1 1 ATOM 219 C CG2 . THR A 1 28 ? 19.104 10.660 11.153 1.00 27.91 ? 44 THR A CG2 1 ATOM 220 N N . GLU A 1 29 ? 17.538 13.372 8.701 1.00 29.74 ? 45 GLU A N 1 ATOM 221 C CA . GLU A 1 29 ? 16.660 13.203 7.534 1.00 30.85 ? 45 GLU A CA 1 ATOM 222 C C . GLU A 1 29 ? 17.376 13.486 6.216 1.00 30.33 ? 45 GLU A C 1 ATOM 223 O O . GLU A 1 29 ? 17.191 12.752 5.235 1.00 30.11 ? 45 GLU A O 1 ATOM 224 C CB . GLU A 1 29 ? 15.393 14.071 7.644 1.00 32.90 ? 45 GLU A CB 1 ATOM 225 C CG . GLU A 1 29 ? 14.325 13.529 8.584 1.00 34.87 ? 45 GLU A CG 1 ATOM 226 C CD . GLU A 1 29 ? 13.625 12.275 8.064 1.00 37.19 ? 45 GLU A CD 1 ATOM 227 O OE1 . GLU A 1 29 ? 13.925 11.807 6.939 1.00 38.36 ? 45 GLU A OE1 1 ATOM 228 O OE2 . GLU A 1 29 ? 12.764 11.743 8.799 1.00 38.00 ? 45 GLU A OE2 1 ATOM 229 N N . ALA A 1 30 ? 18.180 14.552 6.190 1.00 29.49 ? 46 ALA A N 1 ATOM 230 C CA . ALA A 1 30 ? 18.958 14.895 4.996 1.00 29.46 ? 46 ALA A CA 1 ATOM 231 C C . ALA A 1 30 ? 20.051 13.852 4.684 1.00 29.28 ? 46 ALA A C 1 ATOM 232 O O . ALA A 1 30 ? 20.323 13.568 3.508 1.00 28.92 ? 46 ALA A O 1 ATOM 233 C CB . ALA A 1 30 ? 19.561 16.287 5.125 1.00 29.50 ? 46 ALA A CB 1 ATOM 234 N N . ALA A 1 31 ? 20.671 13.303 5.731 1.00 27.98 ? 47 ALA A N 1 ATOM 235 C CA . ALA A 1 31 ? 21.684 12.245 5.583 1.00 28.62 ? 47 ALA A CA 1 ATOM 236 C C . ALA A 1 31 ? 21.042 10.941 5.085 1.00 28.78 ? 47 ALA A C 1 ATOM 237 O O . ALA A 1 31 ? 21.622 10.236 4.263 1.00 29.33 ? 47 ALA A O 1 ATOM 238 C CB . ALA A 1 31 ? 22.433 12.018 6.896 1.00 27.70 ? 47 ALA A CB 1 ATOM 239 N N . TRP A 1 32 ? 19.836 10.647 5.573 1.00 29.27 ? 48 TRP A N 1 ATOM 240 C CA . TRP A 1 32 ? 19.061 9.488 5.124 1.00 29.66 ? 48 TRP A CA 1 ATOM 241 C C . TRP A 1 32 ? 18.689 9.610 3.643 1.00 30.55 ? 48 TRP A C 1 ATOM 242 O O . TRP A 1 32 ? 18.820 8.642 2.899 1.00 30.58 ? 48 TRP A O 1 ATOM 243 C CB . TRP A 1 32 ? 17.810 9.294 5.990 1.00 29.83 ? 48 TRP A CB 1 ATOM 244 C CG . TRP A 1 32 ? 16.787 8.340 5.398 1.00 30.51 ? 48 TRP A CG 1 ATOM 245 C CD1 . TRP A 1 32 ? 15.751 8.659 4.560 1.00 31.04 ? 48 TRP A CD1 1 ATOM 246 C CD2 . TRP A 1 32 ? 16.718 6.922 5.598 1.00 30.36 ? 48 TRP A CD2 1 ATOM 247 N NE1 . TRP A 1 32 ? 15.045 7.526 4.224 1.00 31.44 ? 48 TRP A NE1 1 ATOM 248 C CE2 . TRP A 1 32 ? 15.616 6.446 4.849 1.00 31.17 ? 48 TRP A CE2 1 ATOM 249 C CE3 . TRP A 1 32 ? 17.485 6.004 6.336 1.00 30.13 ? 48 TRP A CE3 1 ATOM 250 C CZ2 . TRP A 1 32 ? 15.257 5.088 4.818 1.00 30.91 ? 48 TRP A CZ2 1 ATOM 251 C CZ3 . TRP A 1 32 ? 17.125 4.654 6.310 1.00 30.28 ? 48 TRP A CZ3 1 ATOM 252 C CH2 . TRP A 1 32 ? 16.019 4.212 5.553 1.00 30.45 ? 48 TRP A CH2 1 ATOM 253 N N . ALA A 1 33 ? 18.253 10.801 3.229 1.00 31.17 ? 49 ALA A N 1 ATOM 254 C CA . ALA A 1 33 ? 17.829 11.052 1.846 1.00 32.26 ? 49 ALA A CA 1 ATOM 255 C C . ALA A 1 33 ? 18.973 10.871 0.847 1.00 32.64 ? 49 ALA A C 1 ATOM 256 O O . ALA A 1 33 ? 18.764 10.372 -0.270 1.00 34.08 ? 49 ALA A O 1 ATOM 257 C CB . ALA A 1 33 ? 17.223 12.445 1.715 1.00 32.60 ? 49 ALA A CB 1 ATOM 258 N N . TYR A 1 34 ? 20.172 11.282 1.256 1.00 31.98 ? 50 TYR A N 1 ATOM 259 C CA . TYR A 1 34 ? 21.366 11.149 0.436 1.00 31.76 ? 50 TYR A CA 1 ATOM 260 C C . TYR A 1 34 ? 21.856 9.703 0.333 1.00 30.89 ? 50 TYR A C 1 ATOM 261 O O . TYR A 1 34 ? 22.209 9.237 -0.753 1.00 30.24 ? 50 TYR A O 1 ATOM 262 C CB . TYR A 1 34 ? 22.485 12.036 0.982 1.00 32.25 ? 50 TYR A CB 1 ATOM 263 C CG . TYR A 1 34 ? 23.777 11.945 0.198 1.00 33.70 ? 50 TYR A CG 1 ATOM 264 C CD1 . TYR A 1 34 ? 23.834 12.372 -1.131 1.00 34.19 ? 50 TYR A CD1 1 ATOM 265 C CD2 . TYR A 1 34 ? 24.947 11.444 0.784 1.00 34.19 ? 50 TYR A CD2 1 ATOM 266 C CE1 . TYR A 1 34 ? 25.010 12.304 -1.859 1.00 35.68 ? 50 TYR A CE1 1 ATOM 267 C CE2 . TYR A 1 34 ? 26.136 11.374 0.061 1.00 35.07 ? 50 TYR A CE2 1 ATOM 268 C CZ . TYR A 1 34 ? 26.158 11.806 -1.261 1.00 36.09 ? 50 TYR A CZ 1 ATOM 269 O OH . TYR A 1 34 ? 27.319 11.751 -1.999 1.00 37.30 ? 50 TYR A OH 1 ATOM 270 N N . GLY A 1 35 ? 21.898 9.013 1.469 1.00 29.61 ? 51 GLY A N 1 ATOM 271 C CA . GLY A 1 35 ? 22.343 7.622 1.519 1.00 29.33 ? 51 GLY A CA 1 ATOM 272 C C . GLY A 1 35 ? 21.390 6.708 0.771 1.00 29.36 ? 51 GLY A C 1 ATOM 273 O O . GLY A 1 35 ? 21.803 5.666 0.277 1.00 29.56 ? 51 GLY A O 1 ATOM 274 N N . SER A 1 36 ? 20.118 7.110 0.698 1.00 30.03 ? 52 SER A N 1 ATOM 275 C CA . SER A 1 36 ? 19.067 6.370 -0.007 1.00 30.97 ? 52 SER A CA 1 ATOM 276 C C . SER A 1 36 ? 19.009 6.711 -1.480 1.00 31.27 ? 52 SER A C 1 ATOM 277 O O . SER A 1 36 ? 18.382 5.996 -2.255 1.00 31.65 ? 52 SER A O 1 ATOM 278 C CB . SER A 1 36 ? 17.695 6.687 0.592 1.00 32.28 ? 52 SER A CB 1 ATOM 279 O OG . SER A 1 36 ? 17.602 6.183 1.907 1.00 33.91 ? 52 SER A OG 1 ATOM 280 N N . ASN A 1 37 ? 19.651 7.813 -1.858 1.00 31.60 ? 53 ASN A N 1 ATOM 281 C CA . ASN A 1 37 ? 19.488 8.385 -3.188 1.00 32.48 ? 53 ASN A CA 1 ATOM 282 C C . ASN A 1 37 ? 20.606 9.391 -3.489 1.00 32.11 ? 53 ASN A C 1 ATOM 283 O O . ASN A 1 37 ? 20.429 10.599 -3.343 1.00 31.73 ? 53 ASN A O 1 ATOM 284 C CB . ASN A 1 37 ? 18.096 9.041 -3.279 1.00 34.30 ? 53 ASN A CB 1 ATOM 285 C CG . ASN A 1 37 ? 17.767 9.550 -4.672 1.00 36.62 ? 53 ASN A CG 1 ATOM 286 O OD1 . ASN A 1 37 ? 18.241 9.003 -5.669 1.00 36.08 ? 53 ASN A OD1 1 ATOM 287 N ND2 . ASN A 1 37 ? 16.938 10.615 -4.738 1.00 38.12 ? 53 ASN A ND2 1 ATOM 288 N N . ILE A 1 38 ? 21.768 8.882 -3.891 1.00 31.95 ? 54 ILE A N 1 ATOM 289 C CA . ILE A 1 38 ? 22.950 9.725 -4.115 1.00 32.33 ? 54 ILE A CA 1 ATOM 290 C C . ILE A 1 38 ? 22.796 10.636 -5.349 1.00 34.27 ? 54 ILE A C 1 ATOM 291 O O . ILE A 1 38 ? 22.822 10.160 -6.485 1.00 34.35 ? 54 ILE A O 1 ATOM 292 C CB . ILE A 1 38 ? 24.244 8.869 -4.206 1.00 32.05 ? 54 ILE A CB 1 ATOM 293 C CG1 . ILE A 1 38 ? 24.455 8.089 -2.897 1.00 31.18 ? 54 ILE A CG1 1 ATOM 294 C CG2 . ILE A 1 38 ? 25.460 9.741 -4.516 1.00 31.71 ? 54 ILE A CG2 1 ATOM 295 C CD1 . ILE A 1 38 ? 25.579 7.076 -2.931 1.00 30.97 ? 54 ILE A CD1 1 ATOM 296 N N . THR A 1 39 ? 22.602 11.937 -5.113 1.00 34.29 ? 55 THR A N 1 ATOM 297 C CA . THR A 1 39 ? 22.556 12.948 -6.184 1.00 35.13 ? 55 THR A CA 1 ATOM 298 C C . THR A 1 39 ? 23.329 14.198 -5.746 1.00 35.64 ? 55 THR A C 1 ATOM 299 O O . THR A 1 39 ? 23.531 14.416 -4.549 1.00 33.47 ? 55 THR A O 1 ATOM 300 C CB . THR A 1 39 ? 21.110 13.353 -6.576 1.00 35.37 ? 55 THR A CB 1 ATOM 301 O OG1 . THR A 1 39 ? 20.495 14.097 -5.516 1.00 34.93 ? 55 THR A OG1 1 ATOM 302 C CG2 . THR A 1 39 ? 20.248 12.134 -6.913 1.00 35.51 ? 55 THR A CG2 1 ATOM 303 N N . ASP A 1 40 ? 23.766 15.015 -6.705 1.00 36.88 ? 56 ASP A N 1 ATOM 304 C CA . ASP A 1 40 ? 24.464 16.269 -6.380 1.00 38.66 ? 56 ASP A CA 1 ATOM 305 C C . ASP A 1 40 ? 23.599 17.175 -5.513 1.00 39.52 ? 56 ASP A C 1 ATOM 306 O O . ASP A 1 40 ? 24.099 17.845 -4.600 1.00 38.70 ? 56 ASP A O 1 ATOM 307 C CB . ASP A 1 40 ? 24.892 17.018 -7.647 1.00 40.91 ? 56 ASP A CB 1 ATOM 308 C CG . ASP A 1 40 ? 26.081 16.376 -8.342 1.00 42.01 ? 56 ASP A CG 1 ATOM 309 O OD1 . ASP A 1 40 ? 26.670 15.425 -7.791 1.00 41.92 ? 56 ASP A OD1 1 ATOM 310 O OD2 . ASP A 1 40 ? 26.429 16.828 -9.454 1.00 44.96 ? 56 ASP A OD2 1 ATOM 311 N N . GLU A 1 41 ? 22.296 17.168 -5.794 1.00 40.65 ? 57 GLU A N 1 ATOM 312 C CA . GLU A 1 41 ? 21.336 17.980 -5.060 1.00 42.76 ? 57 GLU A CA 1 ATOM 313 C C . GLU A 1 41 ? 21.170 17.512 -3.610 1.00 40.56 ? 57 GLU A C 1 ATOM 314 O O . GLU A 1 41 ? 21.160 18.333 -2.696 1.00 39.89 ? 57 GLU A O 1 ATOM 315 C CB . GLU A 1 41 ? 19.984 18.017 -5.782 1.00 46.31 ? 57 GLU A CB 1 ATOM 316 C CG . GLU A 1 41 ? 19.001 19.005 -5.175 1.00 52.52 ? 57 GLU A CG 1 ATOM 317 C CD . GLU A 1 41 ? 17.646 19.041 -5.873 1.00 57.36 ? 57 GLU A CD 1 ATOM 318 O OE1 . GLU A 1 41 ? 17.191 17.997 -6.403 1.00 58.15 ? 57 GLU A OE1 1 ATOM 319 O OE2 . GLU A 1 41 ? 17.026 20.129 -5.878 1.00 60.25 ? 57 GLU A OE2 1 ATOM 320 N N . ASN A 1 42 ? 21.029 16.202 -3.410 1.00 39.44 ? 58 ASN A N 1 ATOM 321 C CA . ASN A 1 42 ? 20.936 15.632 -2.064 1.00 38.08 ? 58 ASN A CA 1 ATOM 322 C C . ASN A 1 42 ? 22.235 15.777 -1.272 1.00 37.10 ? 58 ASN A C 1 ATOM 323 O O . ASN A 1 42 ? 22.201 15.934 -0.049 1.00 37.03 ? 58 ASN A O 1 ATOM 324 C CB . ASN A 1 42 ? 20.506 14.161 -2.110 1.00 38.01 ? 58 ASN A CB 1 ATOM 325 C CG . ASN A 1 42 ? 19.024 13.985 -2.396 1.00 38.72 ? 58 ASN A CG 1 ATOM 326 O OD1 . ASN A 1 42 ? 18.246 14.929 -2.294 1.00 38.63 ? 58 ASN A OD1 1 ATOM 327 N ND2 . ASN A 1 42 ? 18.626 12.765 -2.751 1.00 37.79 ? 58 ASN A ND2 1 ATOM 328 N N . GLU A 1 43 ? 23.371 15.717 -1.968 1.00 36.91 ? 59 GLU A N 1 ATOM 329 C CA . GLU A 1 43 ? 24.678 15.945 -1.340 1.00 37.55 ? 59 GLU A CA 1 ATOM 330 C C . GLU A 1 43 ? 24.740 17.358 -0.764 1.00 38.43 ? 59 GLU A C 1 ATOM 331 O O . GLU A 1 43 ? 25.078 17.553 0.412 1.00 35.81 ? 59 GLU A O 1 ATOM 332 C CB . GLU A 1 43 ? 25.818 15.739 -2.338 1.00 38.51 ? 59 GLU A CB 1 ATOM 333 C CG . GLU A 1 43 ? 27.199 15.964 -1.735 1.00 40.48 ? 59 GLU A CG 1 ATOM 334 C CD . GLU A 1 43 ? 28.328 15.853 -2.745 1.00 42.97 ? 59 GLU A CD 1 ATOM 335 O OE1 . GLU A 1 43 ? 28.061 15.797 -3.963 1.00 45.63 ? 59 GLU A OE1 1 ATOM 336 O OE2 . GLU A 1 43 ? 29.501 15.825 -2.323 1.00 44.40 ? 59 GLU A OE2 1 ATOM 337 N N . LYS A 1 44 ? 24.392 18.329 -1.607 1.00 39.31 ? 60 LYS A N 1 ATOM 338 C CA . LYS A 1 44 ? 24.377 19.739 -1.235 1.00 41.11 ? 60 LYS A CA 1 ATOM 339 C C . LYS A 1 44 ? 23.508 19.979 -0.001 1.00 40.07 ? 60 LYS A C 1 ATOM 340 O O . LYS A 1 44 ? 23.908 20.702 0.915 1.00 40.52 ? 60 LYS A O 1 ATOM 341 C CB . LYS A 1 44 ? 23.883 20.581 -2.412 1.00 42.98 ? 60 LYS A CB 1 ATOM 342 C CG . LYS A 1 44 ? 24.260 22.048 -2.324 1.00 46.60 ? 60 LYS A CG 1 ATOM 343 C CD . LYS A 1 44 ? 24.117 22.728 -3.679 1.00 49.21 ? 60 LYS A CD 1 ATOM 344 C CE . LYS A 1 44 ? 24.588 24.176 -3.623 1.00 51.85 ? 60 LYS A CE 1 ATOM 345 N NZ . LYS A 1 44 ? 23.717 25.033 -2.765 1.00 52.90 ? 60 LYS A NZ 1 ATOM 346 N N . LYS A 1 45 ? 22.342 19.340 0.031 1.00 39.20 ? 61 LYS A N 1 ATOM 347 C CA . LYS A 1 45 ? 21.386 19.522 1.119 1.00 39.20 ? 61 LYS A CA 1 ATOM 348 C C . LYS A 1 45 ? 21.849 18.913 2.437 1.00 37.50 ? 61 LYS A C 1 ATOM 349 O O . LYS A 1 45 ? 21.738 19.553 3.485 1.00 38.12 ? 61 LYS A O 1 ATOM 350 C CB . LYS A 1 45 ? 20.001 19.010 0.714 1.00 40.54 ? 61 LYS A CB 1 ATOM 351 C CG . LYS A 1 45 ? 19.292 19.994 -0.204 1.00 43.78 ? 61 LYS A CG 1 ATOM 352 C CD . LYS A 1 45 ? 18.173 19.373 -1.022 1.00 46.19 ? 61 LYS A CD 1 ATOM 353 C CE . LYS A 1 45 ? 17.616 20.431 -1.963 1.00 48.82 ? 61 LYS A CE 1 ATOM 354 N NZ . LYS A 1 45 ? 16.555 19.897 -2.855 1.00 51.67 ? 61 LYS A NZ 1 ATOM 355 N N . LYS A 1 46 ? 22.370 17.686 2.376 1.00 35.26 ? 62 LYS A N 1 ATOM 356 C CA . LYS A 1 46 ? 22.957 17.025 3.539 1.00 34.06 ? 62 LYS A CA 1 ATOM 357 C C . LYS A 1 46 ? 24.029 17.915 4.180 1.00 32.98 ? 62 LYS A C 1 ATOM 358 O O . LYS A 1 46 ? 23.986 18.184 5.374 1.00 33.26 ? 62 LYS A O 1 ATOM 359 C CB . LYS A 1 46 ? 23.552 15.665 3.145 1.00 33.74 ? 62 LYS A CB 1 ATOM 360 C CG . LYS A 1 46 ? 24.299 14.971 4.270 1.00 34.39 ? 62 LYS A CG 1 ATOM 361 C CD . LYS A 1 46 ? 25.103 13.765 3.809 1.00 34.52 ? 62 LYS A CD 1 ATOM 362 C CE . LYS A 1 46 ? 25.888 13.219 5.000 1.00 34.99 ? 62 LYS A CE 1 ATOM 363 N NZ . LYS A 1 46 ? 26.534 11.907 4.719 1.00 36.26 ? 62 LYS A NZ 1 ATOM 364 N N . ASN A 1 47 ? 24.965 18.384 3.363 1.00 32.75 ? 63 ASN A N 1 ATOM 365 C CA . ASN A 1 47 ? 26.128 19.130 3.841 1.00 32.42 ? 63 ASN A CA 1 ATOM 366 C C . ASN A 1 47 ? 25.823 20.545 4.347 1.00 32.78 ? 63 ASN A C 1 ATOM 367 O O . ASN A 1 47 ? 26.491 21.033 5.260 1.00 32.37 ? 63 ASN A O 1 ATOM 368 C CB . ASN A 1 47 ? 27.232 19.125 2.772 1.00 31.16 ? 63 ASN A CB 1 ATOM 369 C CG . ASN A 1 47 ? 27.900 17.760 2.634 1.00 30.63 ? 63 ASN A CG 1 ATOM 370 O OD1 . ASN A 1 47 ? 27.736 16.890 3.488 1.00 29.53 ? 63 ASN A OD1 1 ATOM 371 N ND2 . ASN A 1 47 ? 28.668 17.575 1.571 1.00 29.31 ? 63 ASN A ND2 1 ATOM 372 N N A GLU A 1 48 ? 24.811 21.186 3.771 0.50 33.42 ? 64 GLU A N 1 ATOM 373 N N B GLU A 1 48 ? 24.817 21.185 3.745 0.50 33.62 ? 64 GLU A N 1 ATOM 374 C CA A GLU A 1 48 ? 24.414 22.523 4.203 0.50 33.84 ? 64 GLU A CA 1 ATOM 375 C CA B GLU A 1 48 ? 24.342 22.505 4.169 0.50 34.27 ? 64 GLU A CA 1 ATOM 376 C C A GLU A 1 48 ? 23.714 22.494 5.565 0.50 33.38 ? 64 GLU A C 1 ATOM 377 C C B GLU A 1 48 ? 23.783 22.436 5.580 0.50 33.56 ? 64 GLU A C 1 ATOM 378 O O A GLU A 1 48 ? 23.929 23.377 6.397 0.50 33.56 ? 64 GLU A O 1 ATOM 379 O O B GLU A 1 48 ? 24.139 23.239 6.446 0.50 33.58 ? 64 GLU A O 1 ATOM 380 C CB A GLU A 1 48 ? 23.566 23.219 3.127 0.50 34.72 ? 64 GLU A CB 1 ATOM 381 C CB B GLU A 1 48 ? 23.248 23.027 3.225 0.50 35.47 ? 64 GLU A CB 1 ATOM 382 C CG A GLU A 1 48 ? 24.391 23.670 1.927 0.50 35.43 ? 64 GLU A CG 1 ATOM 383 C CG B GLU A 1 48 ? 22.528 24.263 3.755 0.50 37.12 ? 64 GLU A CG 1 ATOM 384 C CD A GLU A 1 48 ? 23.589 24.439 0.891 0.50 36.53 ? 64 GLU A CD 1 ATOM 385 C CD B GLU A 1 48 ? 21.117 24.418 3.207 0.50 38.50 ? 64 GLU A CD 1 ATOM 386 O OE1 A GLU A 1 48 ? 22.351 24.265 0.819 0.50 36.59 ? 64 GLU A OE1 1 ATOM 387 O OE1 B GLU A 1 48 ? 20.500 23.394 2.835 0.50 39.70 ? 64 GLU A OE1 1 ATOM 388 O OE2 A GLU A 1 48 ? 24.209 25.223 0.142 0.50 36.97 ? 64 GLU A OE2 1 ATOM 389 O OE2 B GLU A 1 48 ? 20.621 25.563 3.154 0.50 38.29 ? 64 GLU A OE2 1 ATOM 390 N N . ILE A 1 49 ? 22.907 21.463 5.801 1.00 33.02 ? 65 ILE A N 1 ATOM 391 C CA . ILE A 1 49 ? 22.219 21.309 7.076 1.00 32.75 ? 65 ILE A CA 1 ATOM 392 C C . ILE A 1 49 ? 23.199 20.908 8.191 1.00 31.80 ? 65 ILE A C 1 ATOM 393 O O . ILE A 1 49 ? 23.077 21.377 9.325 1.00 30.93 ? 65 ILE A O 1 ATOM 394 C CB . ILE A 1 49 ? 20.995 20.382 6.927 1.00 34.17 ? 65 ILE A CB 1 ATOM 395 C CG1 . ILE A 1 49 ? 19.931 21.110 6.079 1.00 35.64 ? 65 ILE A CG1 1 ATOM 396 C CG2 . ILE A 1 49 ? 20.420 20.008 8.283 1.00 33.36 ? 65 ILE A CG2 1 ATOM 397 C CD1 . ILE A 1 49 ? 19.090 20.244 5.157 1.00 35.92 ? 65 ILE A CD1 1 ATOM 398 N N . SER A 1 50 ? 24.192 20.086 7.849 1.00 30.83 ? 66 SER A N 1 ATOM 399 C CA . SER A 1 50 ? 25.264 19.747 8.789 1.00 29.97 ? 66 SER A CA 1 ATOM 400 C C . SER A 1 50 ? 26.059 20.981 9.206 1.00 29.62 ? 66 SER A C 1 ATOM 401 O O . SER A 1 50 ? 26.358 21.148 10.381 1.00 29.34 ? 66 SER A O 1 ATOM 402 C CB . SER A 1 50 ? 26.213 18.704 8.207 1.00 29.40 ? 66 SER A CB 1 ATOM 403 O OG . SER A 1 50 ? 25.653 17.417 8.313 1.00 30.53 ? 66 SER A OG 1 ATOM 404 N N . ALA A 1 51 ? 26.402 21.827 8.236 1.00 29.51 ? 67 ALA A N 1 ATOM 405 C CA . ALA A 1 51 ? 27.102 23.083 8.499 1.00 29.85 ? 67 ALA A CA 1 ATOM 406 C C . ALA A 1 51 ? 26.285 23.977 9.446 1.00 30.45 ? 67 ALA A C 1 ATOM 407 O O . ALA A 1 51 ? 26.840 24.615 10.352 1.00 31.01 ? 67 ALA A O 1 ATOM 408 C CB . ALA A 1 51 ? 27.393 23.799 7.193 1.00 30.19 ? 67 ALA A CB 1 ATOM 409 N N . GLU A 1 52 ? 24.966 23.991 9.247 1.00 29.87 ? 68 GLU A N 1 ATOM 410 C CA . GLU A 1 52 ? 24.046 24.751 10.095 1.00 29.64 ? 68 GLU A CA 1 ATOM 411 C C . GLU A 1 52 ? 24.084 24.252 11.546 1.00 28.79 ? 68 GLU A C 1 ATOM 412 O O . GLU A 1 52 ? 24.242 25.050 12.475 1.00 27.93 ? 68 GLU A O 1 ATOM 413 C CB . GLU A 1 52 ? 22.632 24.688 9.519 0.50 29.41 ? 68 GLU A CB 1 ATOM 414 C CG . GLU A 1 52 ? 21.601 25.534 10.237 0.50 29.80 ? 68 GLU A CG 1 ATOM 415 C CD . GLU A 1 52 ? 20.318 25.645 9.443 0.50 30.29 ? 68 GLU A CD 1 ATOM 416 O OE1 . GLU A 1 52 ? 20.391 25.609 8.195 0.50 30.04 ? 68 GLU A OE1 1 ATOM 417 O OE2 . GLU A 1 52 ? 19.241 25.759 10.062 0.50 30.58 ? 68 GLU A OE2 1 ATOM 418 N N . LEU A 1 53 ? 23.956 22.939 11.733 1.00 28.38 ? 69 LEU A N 1 ATOM 419 C CA . LEU A 1 53 ? 24.018 22.344 13.078 1.00 28.23 ? 69 LEU A CA 1 ATOM 420 C C . LEU A 1 53 ? 25.389 22.541 13.748 1.00 27.80 ? 69 LEU A C 1 ATOM 421 O O . LEU A 1 53 ? 25.459 22.774 14.960 1.00 27.17 ? 69 LEU A O 1 ATOM 422 C CB . LEU A 1 53 ? 23.631 20.855 13.050 1.00 29.01 ? 69 LEU A CB 1 ATOM 423 C CG . LEU A 1 53 ? 23.672 20.059 14.362 1.00 29.56 ? 69 LEU A CG 1 ATOM 424 C CD1 . LEU A 1 53 ? 22.769 20.653 15.439 1.00 30.38 ? 69 LEU A CD1 1 ATOM 425 C CD2 . LEU A 1 53 ? 23.310 18.605 14.115 1.00 30.18 ? 69 LEU A CD2 1 ATOM 426 N N . ALA A 1 54 ? 26.467 22.447 12.970 1.00 27.28 ? 70 ALA A N 1 ATOM 427 C CA . ALA A 1 54 ? 27.817 22.682 13.499 1.00 28.22 ? 70 ALA A CA 1 ATOM 428 C C . ALA A 1 54 ? 27.938 24.091 14.088 1.00 29.11 ? 70 ALA A C 1 ATOM 429 O O . ALA A 1 54 ? 28.500 24.269 15.175 1.00 28.92 ? 70 ALA A O 1 ATOM 430 C CB . ALA A 1 54 ? 28.869 22.456 12.429 1.00 27.79 ? 70 ALA A CB 1 ATOM 431 N N . LYS A 1 55 ? 27.392 25.079 13.375 1.00 29.95 ? 71 LYS A N 1 ATOM 432 C CA . LYS A 1 55 ? 27.368 26.469 13.844 1.00 31.27 ? 71 LYS A CA 1 ATOM 433 C C . LYS A 1 55 ? 26.640 26.611 15.186 1.00 31.19 ? 71 LYS A C 1 ATOM 434 O O . LYS A 1 55 ? 27.111 27.315 16.083 1.00 31.30 ? 71 LYS A O 1 ATOM 435 C CB . LYS A 1 55 ? 26.732 27.381 12.789 1.00 33.09 ? 71 LYS A CB 1 ATOM 436 C CG . LYS A 1 55 ? 26.972 28.856 13.053 1.00 36.41 ? 71 LYS A CG 1 ATOM 437 C CD . LYS A 1 55 ? 26.478 29.729 11.912 1.00 38.72 ? 71 LYS A CD 1 ATOM 438 C CE . LYS A 1 55 ? 27.213 31.058 11.943 1.00 41.03 ? 71 LYS A CE 1 ATOM 439 N NZ . LYS A 1 55 ? 26.520 32.096 11.131 1.00 44.44 ? 71 LYS A NZ 1 ATOM 440 N N . PHE A 1 56 ? 25.500 25.935 15.324 1.00 30.81 ? 72 PHE A N 1 ATOM 441 C CA . PHE A 1 56 ? 24.751 25.942 16.580 1.00 30.77 ? 72 PHE A CA 1 ATOM 442 C C . PHE A 1 56 ? 25.542 25.291 17.722 1.00 31.21 ? 72 PHE A C 1 ATOM 443 O O . PHE A 1 56 ? 25.538 25.800 18.849 1.00 30.99 ? 72 PHE A O 1 ATOM 444 C CB . PHE A 1 56 ? 23.383 25.261 16.406 1.00 30.18 ? 72 PHE A CB 1 ATOM 445 C CG . PHE A 1 56 ? 22.555 25.240 17.661 1.00 30.27 ? 72 PHE A CG 1 ATOM 446 C CD1 . PHE A 1 56 ? 21.868 26.378 18.079 1.00 30.77 ? 72 PHE A CD1 1 ATOM 447 C CD2 . PHE A 1 56 ? 22.469 24.087 18.435 1.00 29.70 ? 72 PHE A CD2 1 ATOM 448 C CE1 . PHE A 1 56 ? 21.111 26.365 19.243 1.00 30.68 ? 72 PHE A CE1 1 ATOM 449 C CE2 . PHE A 1 56 ? 21.711 24.070 19.597 1.00 29.79 ? 72 PHE A CE2 1 ATOM 450 C CZ . PHE A 1 56 ? 21.033 25.210 20.002 1.00 30.02 ? 72 PHE A CZ 1 ATOM 451 N N . MET A 1 57 ? 26.207 24.171 17.430 1.00 31.52 ? 73 MET A N 1 ATOM 452 C CA . MET A 1 57 ? 27.044 23.477 18.418 1.00 33.24 ? 73 MET A CA 1 ATOM 453 C C . MET A 1 57 ? 28.161 24.381 18.931 1.00 32.85 ? 73 MET A C 1 ATOM 454 O O . MET A 1 57 ? 28.475 24.363 20.126 1.00 31.35 ? 73 MET A O 1 ATOM 455 C CB . MET A 1 57 ? 27.662 22.202 17.838 1.00 34.32 ? 73 MET A CB 1 ATOM 456 C CG . MET A 1 57 ? 26.688 21.122 17.420 1.00 37.40 ? 73 MET A CG 1 ATOM 457 S SD . MET A 1 57 ? 25.491 20.737 18.704 1.00 41.45 ? 73 MET A SD 1 ATOM 458 C CE . MET A 1 57 ? 25.157 19.020 18.259 1.00 43.84 ? 73 MET A CE 1 ATOM 459 N N . LYS A 1 58 ? 28.763 25.158 18.027 1.00 32.94 ? 74 LYS A N 1 ATOM 460 C CA . LYS A 1 58 ? 29.778 26.151 18.413 1.00 34.61 ? 74 LYS A CA 1 ATOM 461 C C . LYS A 1 58 ? 29.241 27.099 19.484 1.00 35.26 ? 74 LYS A C 1 ATOM 462 O O . LYS A 1 58 ? 29.915 27.352 20.486 1.00 36.21 ? 74 LYS A O 1 ATOM 463 C CB . LYS A 1 58 ? 30.257 26.958 17.207 1.00 35.21 ? 74 LYS A CB 1 ATOM 464 C CG . LYS A 1 58 ? 31.449 26.364 16.474 1.00 36.01 ? 74 LYS A CG 1 ATOM 465 C CD . LYS A 1 58 ? 32.163 27.431 15.651 1.00 36.31 ? 74 LYS A CD 1 ATOM 466 C CE . LYS A 1 58 ? 33.140 26.834 14.652 1.00 36.60 ? 74 LYS A CE 1 ATOM 467 N NZ . LYS A 1 58 ? 32.488 25.856 13.727 1.00 38.06 ? 74 LYS A NZ 1 ATOM 468 N N . GLU A 1 59 ? 28.027 27.609 19.270 1.00 35.00 ? 75 GLU A N 1 ATOM 469 C CA . GLU A 1 59 ? 27.354 28.472 20.242 1.00 35.72 ? 75 GLU A CA 1 ATOM 470 C C . GLU A 1 59 ? 27.066 27.746 21.569 1.00 35.63 ? 75 GLU A C 1 ATOM 471 O O . GLU A 1 59 ? 27.226 28.323 22.644 1.00 35.31 ? 75 GLU A O 1 ATOM 472 C CB . GLU A 1 59 ? 26.079 29.076 19.639 0.50 35.90 ? 75 GLU A CB 1 ATOM 473 C CG . GLU A 1 59 ? 26.359 30.141 18.586 0.50 37.15 ? 75 GLU A CG 1 ATOM 474 C CD . GLU A 1 59 ? 25.192 30.383 17.644 0.50 38.11 ? 75 GLU A CD 1 ATOM 475 O OE1 . GLU A 1 59 ? 24.035 30.128 18.044 0.50 39.01 ? 75 GLU A OE1 1 ATOM 476 O OE2 . GLU A 1 59 ? 25.429 30.830 16.499 0.50 37.76 ? 75 GLU A OE2 1 ATOM 477 N N . VAL A 1 60 ? 26.670 26.478 21.496 1.00 35.44 ? 76 VAL A N 1 ATOM 478 C CA . VAL A 1 60 ? 26.426 25.679 22.707 1.00 35.83 ? 76 VAL A CA 1 ATOM 479 C C . VAL A 1 60 ? 27.698 25.521 23.568 1.00 36.67 ? 76 VAL A C 1 ATOM 480 O O . VAL A 1 60 ? 27.677 25.795 24.776 1.00 36.21 ? 76 VAL A O 1 ATOM 481 C CB . VAL A 1 60 ? 25.804 24.299 22.376 1.00 35.76 ? 76 VAL A CB 1 ATOM 482 C CG1 . VAL A 1 60 ? 25.769 23.403 23.611 1.00 36.15 ? 76 VAL A CG1 1 ATOM 483 C CG2 . VAL A 1 60 ? 24.409 24.474 21.799 1.00 34.96 ? 76 VAL A CG2 1 ATOM 484 N N . ALA A 1 61 ? 28.795 25.093 22.945 1.00 36.07 ? 77 ALA A N 1 ATOM 485 C CA . ALA A 1 61 ? 30.058 24.916 23.657 1.00 37.17 ? 77 ALA A CA 1 ATOM 486 C C . ALA A 1 61 ? 30.493 26.225 24.298 1.00 38.39 ? 77 ALA A C 1 ATOM 487 O O . ALA A 1 61 ? 31.000 26.227 25.417 1.00 39.65 ? 77 ALA A O 1 ATOM 488 C CB . ALA A 1 61 ? 31.139 24.383 22.732 1.00 36.01 ? 77 ALA A CB 1 ATOM 489 N N . SER A 1 62 ? 30.268 27.331 23.594 1.00 39.60 ? 78 SER A N 1 ATOM 490 C CA . SER A 1 62 ? 30.545 28.663 24.122 1.00 40.97 ? 78 SER A CA 1 ATOM 491 C C . SER A 1 62 ? 29.712 28.965 25.376 1.00 41.34 ? 78 SER A C 1 ATOM 492 O O . SER A 1 62 ? 30.252 29.421 26.388 1.00 41.07 ? 78 SER A O 1 ATOM 493 C CB . SER A 1 62 ? 30.311 29.725 23.041 1.00 42.17 ? 78 SER A CB 1 ATOM 494 O OG . SER A 1 62 ? 30.417 31.033 23.574 1.00 43.53 ? 78 SER A OG 1 ATOM 495 N N . ASP A 1 63 ? 28.411 28.692 25.315 1.00 40.82 ? 79 ASP A N 1 ATOM 496 C CA . ASP A 1 63 ? 27.506 28.947 26.445 1.00 41.59 ? 79 ASP A CA 1 ATOM 497 C C . ASP A 1 63 ? 27.749 28.102 27.700 1.00 41.17 ? 79 ASP A C 1 ATOM 498 O O . ASP A 1 63 ? 27.323 28.489 28.791 1.00 40.98 ? 79 ASP A O 1 ATOM 499 C CB . ASP A 1 63 ? 26.044 28.813 26.011 1.00 43.28 ? 79 ASP A CB 1 ATOM 500 C CG . ASP A 1 63 ? 25.576 29.985 25.172 1.00 44.99 ? 79 ASP A CG 1 ATOM 501 O OD1 . ASP A 1 63 ? 26.318 30.985 25.063 1.00 46.82 ? 79 ASP A OD1 1 ATOM 502 O OD2 . ASP A 1 63 ? 24.461 29.907 24.619 1.00 46.54 ? 79 ASP A OD2 1 ATOM 503 N N . THR A 1 64 ? 28.417 26.957 27.558 1.00 40.36 ? 80 THR A N 1 ATOM 504 C CA . THR A 1 64 ? 28.750 26.134 28.729 1.00 40.49 ? 80 THR A CA 1 ATOM 505 C C . THR A 1 64 ? 29.705 26.848 29.693 1.00 40.87 ? 80 THR A C 1 ATOM 506 O O . THR A 1 64 ? 29.674 26.594 30.902 1.00 41.43 ? 80 THR A O 1 ATOM 507 C CB . THR A 1 64 ? 29.343 24.752 28.357 1.00 40.50 ? 80 THR A CB 1 ATOM 508 O OG1 . THR A 1 64 ? 30.592 24.913 27.667 1.00 39.33 ? 80 THR A OG1 1 ATOM 509 C CG2 . THR A 1 64 ? 28.360 23.940 27.507 1.00 39.23 ? 80 THR A CG2 1 ATOM 510 N N . THR A 1 65 ? 30.531 27.752 29.160 1.00 40.82 ? 81 THR A N 1 ATOM 511 C CA . THR A 1 65 ? 31.514 28.481 29.976 1.00 41.75 ? 81 THR A CA 1 ATOM 512 C C . THR A 1 65 ? 30.844 29.514 30.890 1.00 41.79 ? 81 THR A C 1 ATOM 513 O O . THR A 1 65 ? 31.471 30.050 31.794 1.00 43.54 ? 81 THR A O 1 ATOM 514 C CB . THR A 1 65 ? 32.615 29.146 29.115 1.00 41.84 ? 81 THR A CB 1 ATOM 515 O OG1 . THR A 1 65 ? 32.044 30.190 28.317 1.00 42.37 ? 81 THR A OG1 1 ATOM 516 C CG2 . THR A 1 65 ? 33.282 28.127 28.201 1.00 41.07 ? 81 THR A CG2 1 ATOM 517 N N . LYS A 1 66 ? 29.563 29.776 30.657 1.00 41.10 ? 82 LYS A N 1 ATOM 518 C CA . LYS A 1 66 ? 28.788 30.667 31.514 1.00 40.69 ? 82 LYS A CA 1 ATOM 519 C C . LYS A 1 66 ? 28.295 29.940 32.767 1.00 38.85 ? 82 LYS A C 1 ATOM 520 O O . LYS A 1 66 ? 27.789 30.573 33.702 1.00 38.90 ? 82 LYS A O 1 ATOM 521 C CB . LYS A 1 66 ? 27.610 31.261 30.731 1.00 43.78 ? 82 LYS A CB 1 ATOM 522 C CG . LYS A 1 66 ? 28.031 32.018 29.472 1.00 46.46 ? 82 LYS A CG 1 ATOM 523 C CD . LYS A 1 66 ? 26.871 32.201 28.500 1.00 50.06 ? 82 LYS A CD 1 ATOM 524 C CE . LYS A 1 66 ? 26.329 33.623 28.506 1.00 52.41 ? 82 LYS A CE 1 ATOM 525 N NZ . LYS A 1 66 ? 25.217 33.780 27.525 1.00 54.85 ? 82 LYS A NZ 1 ATOM 526 N N . PHE A 1 67 ? 28.433 28.614 32.771 1.00 35.05 ? 83 PHE A N 1 ATOM 527 C CA . PHE A 1 67 ? 28.059 27.781 33.912 1.00 33.41 ? 83 PHE A CA 1 ATOM 528 C C . PHE A 1 67 ? 29.301 27.228 34.587 1.00 32.83 ? 83 PHE A C 1 ATOM 529 O O . PHE A 1 67 ? 30.211 26.746 33.909 1.00 32.29 ? 83 PHE A O 1 ATOM 530 C CB . PHE A 1 67 ? 27.153 26.625 33.470 1.00 32.32 ? 83 PHE A CB 1 ATOM 531 C CG . PHE A 1 67 ? 25.775 27.058 33.072 1.00 32.08 ? 83 PHE A CG 1 ATOM 532 C CD1 . PHE A 1 67 ? 24.785 27.246 34.034 1.00 32.37 ? 83 PHE A CD1 1 ATOM 533 C CD2 . PHE A 1 67 ? 25.466 27.299 31.739 1.00 31.98 ? 83 PHE A CD2 1 ATOM 534 C CE1 . PHE A 1 67 ? 23.509 27.658 33.670 1.00 32.89 ? 83 PHE A CE1 1 ATOM 535 C CE2 . PHE A 1 67 ? 24.189 27.707 31.367 1.00 32.12 ? 83 PHE A CE2 1 ATOM 536 C CZ . PHE A 1 67 ? 23.210 27.885 32.331 1.00 32.43 ? 83 PHE A CZ 1 ATOM 537 N N . GLN A 1 68 ? 29.335 27.304 35.917 1.00 32.00 ? 84 GLN A N 1 ATOM 538 C CA . GLN A 1 68 ? 30.446 26.772 36.705 1.00 32.48 ? 84 GLN A CA 1 ATOM 539 C C . GLN A 1 68 ? 30.314 25.262 36.879 1.00 29.95 ? 84 GLN A C 1 ATOM 540 O O . GLN A 1 68 ? 30.381 24.775 38.001 1.00 30.01 ? 84 GLN A O 1 ATOM 541 C CB . GLN A 1 68 ? 30.458 27.409 38.101 1.00 34.90 ? 84 GLN A CB 1 ATOM 542 C CG . GLN A 1 68 ? 30.474 28.925 38.120 1.00 38.47 ? 84 GLN A CG 1 ATOM 543 C CD . GLN A 1 68 ? 31.781 29.483 37.607 1.00 40.62 ? 84 GLN A CD 1 ATOM 544 O OE1 . GLN A 1 68 ? 32.859 29.055 38.026 1.00 42.74 ? 84 GLN A OE1 1 ATOM 545 N NE2 . GLN A 1 68 ? 31.696 30.439 36.690 1.00 42.03 ? 84 GLN A NE2 1 ATOM 546 N N . TRP A 1 69 ? 30.137 24.520 35.786 1.00 28.03 ? 85 TRP A N 1 ATOM 547 C CA . TRP A 1 69 ? 29.685 23.124 35.901 1.00 26.57 ? 85 TRP A CA 1 ATOM 548 C C . TRP A 1 69 ? 30.658 22.190 36.643 1.00 25.75 ? 85 TRP A C 1 ATOM 549 O O . TRP A 1 69 ? 30.214 21.275 37.336 1.00 25.17 ? 85 TRP A O 1 ATOM 550 C CB . TRP A 1 69 ? 29.236 22.543 34.550 1.00 26.33 ? 85 TRP A CB 1 ATOM 551 C CG . TRP A 1 69 ? 30.310 22.422 33.502 1.00 26.18 ? 85 TRP A CG 1 ATOM 552 C CD1 . TRP A 1 69 ? 30.586 23.316 32.506 1.00 26.03 ? 85 TRP A CD1 1 ATOM 553 C CD2 . TRP A 1 69 ? 31.220 21.326 33.319 1.00 25.99 ? 85 TRP A CD2 1 ATOM 554 N NE1 . TRP A 1 69 ? 31.622 22.860 31.734 1.00 25.95 ? 85 TRP A NE1 1 ATOM 555 C CE2 . TRP A 1 69 ? 32.031 21.640 32.208 1.00 25.82 ? 85 TRP A CE2 1 ATOM 556 C CE3 . TRP A 1 69 ? 31.439 20.113 33.997 1.00 25.85 ? 85 TRP A CE3 1 ATOM 557 C CZ2 . TRP A 1 69 ? 33.051 20.787 31.752 1.00 25.60 ? 85 TRP A CZ2 1 ATOM 558 C CZ3 . TRP A 1 69 ? 32.453 19.266 33.545 1.00 25.63 ? 85 TRP A CZ3 1 ATOM 559 C CH2 . TRP A 1 69 ? 33.245 19.608 32.431 1.00 25.60 ? 85 TRP A CH2 1 ATOM 560 N N . ARG A 1 70 ? 31.964 22.440 36.532 1.00 24.73 ? 86 ARG A N 1 ATOM 561 C CA . ARG A 1 70 ? 32.963 21.627 37.250 1.00 24.59 ? 86 ARG A CA 1 ATOM 562 C C . ARG A 1 70 ? 32.850 21.749 38.774 1.00 25.30 ? 86 ARG A C 1 ATOM 563 O O . ARG A 1 70 ? 33.356 20.897 39.496 1.00 25.98 ? 86 ARG A O 1 ATOM 564 C CB . ARG A 1 70 ? 34.392 21.957 36.798 1.00 24.36 ? 86 ARG A CB 1 ATOM 565 C CG . ARG A 1 70 ? 34.683 21.513 35.366 1.00 23.59 ? 86 ARG A CG 1 ATOM 566 C CD . ARG A 1 70 ? 36.132 21.774 34.975 1.00 23.66 ? 86 ARG A CD 1 ATOM 567 N NE . ARG A 1 70 ? 36.377 21.409 33.578 1.00 23.35 ? 86 ARG A NE 1 ATOM 568 C CZ . ARG A 1 70 ? 36.093 22.191 32.537 1.00 23.99 ? 86 ARG A CZ 1 ATOM 569 N NH1 . ARG A 1 70 ? 35.554 23.392 32.728 1.00 24.35 ? 86 ARG A NH1 1 ATOM 570 N NH2 . ARG A 1 70 ? 36.336 21.767 31.302 1.00 23.35 ? 86 ARG A NH2 1 ATOM 571 N N . SER A 1 71 ? 32.172 22.793 39.246 1.00 25.93 ? 87 SER A N 1 ATOM 572 C CA . SER A 1 71 ? 31.964 23.022 40.686 1.00 26.78 ? 87 SER A CA 1 ATOM 573 C C . SER A 1 71 ? 30.717 22.335 41.261 1.00 27.72 ? 87 SER A C 1 ATOM 574 O O . SER A 1 71 ? 30.471 22.409 42.472 1.00 28.15 ? 87 SER A O 1 ATOM 575 C CB . SER A 1 71 ? 31.848 24.522 40.958 1.00 27.09 ? 87 SER A CB 1 ATOM 576 O OG . SER A 1 71 ? 33.051 25.194 40.646 1.00 29.05 ? 87 SER A OG 1 ATOM 577 N N . TYR A 1 72 ? 29.923 21.693 40.405 1.00 27.99 ? 88 TYR A N 1 ATOM 578 C CA . TYR A 1 72 ? 28.600 21.203 40.809 1.00 28.42 ? 88 TYR A CA 1 ATOM 579 C C . TYR A 1 72 ? 28.634 19.955 41.703 1.00 28.75 ? 88 TYR A C 1 ATOM 580 O O . TYR A 1 72 ? 29.581 19.162 41.658 1.00 28.20 ? 88 TYR A O 1 ATOM 581 C CB . TYR A 1 72 ? 27.733 20.933 39.572 1.00 28.64 ? 88 TYR A CB 1 ATOM 582 C CG . TYR A 1 72 ? 27.290 22.157 38.787 1.00 28.89 ? 88 TYR A CG 1 ATOM 583 C CD1 . TYR A 1 72 ? 27.501 23.462 39.268 1.00 29.73 ? 88 TYR A CD1 1 ATOM 584 C CD2 . TYR A 1 72 ? 26.612 22.007 37.579 1.00 29.12 ? 88 TYR A CD2 1 ATOM 585 C CE1 . TYR A 1 72 ? 27.077 24.569 38.540 1.00 30.12 ? 88 TYR A CE1 1 ATOM 586 C CE2 . TYR A 1 72 ? 26.180 23.103 36.852 1.00 29.39 ? 88 TYR A CE2 1 ATOM 587 C CZ . TYR A 1 72 ? 26.408 24.376 37.332 1.00 30.31 ? 88 TYR A CZ 1 ATOM 588 O OH . TYR A 1 72 ? 25.974 25.455 36.596 1.00 31.37 ? 88 TYR A OH 1 ATOM 589 N N . GLN A 1 73 ? 27.589 19.792 42.509 1.00 30.16 ? 89 GLN A N 1 ATOM 590 C CA . GLN A 1 73 ? 27.415 18.604 43.345 1.00 31.53 ? 89 GLN A CA 1 ATOM 591 C C . GLN A 1 73 ? 26.990 17.385 42.524 1.00 31.02 ? 89 GLN A C 1 ATOM 592 O O . GLN A 1 73 ? 27.468 16.279 42.767 1.00 31.18 ? 89 GLN A O 1 ATOM 593 C CB . GLN A 1 73 ? 26.379 18.861 44.447 1.00 32.81 ? 89 GLN A CB 1 ATOM 594 C CG . GLN A 1 73 ? 26.847 19.797 45.555 1.00 35.07 ? 89 GLN A CG 1 ATOM 595 C CD . GLN A 1 73 ? 28.021 19.241 46.344 1.00 36.11 ? 89 GLN A CD 1 ATOM 596 O OE1 . GLN A 1 73 ? 27.988 18.098 46.814 1.00 37.21 ? 89 GLN A OE1 1 ATOM 597 N NE2 . GLN A 1 73 ? 29.073 20.045 46.485 1.00 35.49 ? 89 GLN A NE2 1 ATOM 598 N N . SER A 1 74 ? 26.095 17.598 41.558 1.00 30.52 ? 90 SER A N 1 ATOM 599 C CA . SER A 1 74 ? 25.488 16.510 40.784 1.00 30.50 ? 90 SER A CA 1 ATOM 600 C C . SER A 1 74 ? 26.382 15.943 39.673 1.00 30.55 ? 90 SER A C 1 ATOM 601 O O . SER A 1 74 ? 26.676 16.622 38.673 1.00 29.49 ? 90 SER A O 1 ATOM 602 C CB . SER A 1 74 ? 24.134 16.949 40.209 1.00 30.26 ? 90 SER A CB 1 ATOM 603 O OG . SER A 1 74 ? 23.688 16.038 39.213 1.00 29.69 ? 90 SER A OG 1 ATOM 604 N N . GLU A 1 75 ? 26.798 14.690 39.853 1.00 31.62 ? 91 GLU A N 1 ATOM 605 C CA . GLU A 1 75 ? 27.598 13.980 38.858 1.00 32.34 ? 91 GLU A CA 1 ATOM 606 C C . GLU A 1 75 ? 26.864 13.933 37.529 1.00 30.48 ? 91 GLU A C 1 ATOM 607 O O . GLU A 1 75 ? 27.486 14.019 36.471 1.00 30.34 ? 91 GLU A O 1 ATOM 608 C CB . GLU A 1 75 ? 27.915 12.550 39.317 1.00 35.78 ? 91 GLU A CB 1 ATOM 609 C CG . GLU A 1 75 ? 28.817 12.437 40.542 1.00 40.90 ? 91 GLU A CG 1 ATOM 610 C CD . GLU A 1 75 ? 30.226 12.980 40.318 1.00 44.32 ? 91 GLU A CD 1 ATOM 611 O OE1 . GLU A 1 75 ? 30.780 12.830 39.199 1.00 45.32 ? 91 GLU A OE1 1 ATOM 612 O OE2 . GLU A 1 75 ? 30.784 13.571 41.276 1.00 48.36 ? 91 GLU A OE2 1 ATOM 613 N N . ASP A 1 76 ? 25.538 13.812 37.588 1.00 29.78 ? 92 ASP A N 1 ATOM 614 C CA . ASP A 1 76 ? 24.698 13.760 36.388 1.00 28.80 ? 92 ASP A CA 1 ATOM 615 C C . ASP A 1 76 ? 24.716 15.056 35.576 1.00 28.05 ? 92 ASP A C 1 ATOM 616 O O . ASP A 1 76 ? 24.842 15.016 34.349 1.00 27.03 ? 92 ASP A O 1 ATOM 617 C CB . ASP A 1 76 ? 23.255 13.386 36.748 1.00 30.23 ? 92 ASP A CB 1 ATOM 618 C CG . ASP A 1 76 ? 22.365 13.248 35.521 1.00 31.04 ? 92 ASP A CG 1 ATOM 619 O OD1 . ASP A 1 76 ? 22.801 12.677 34.509 1.00 31.79 ? 92 ASP A OD1 1 ATOM 620 O OD2 . ASP A 1 76 ? 21.221 13.714 35.560 1.00 32.88 ? 92 ASP A OD2 1 ATOM 621 N N . LEU A 1 77 ? 24.570 16.198 36.253 1.00 27.07 ? 93 LEU A N 1 ATOM 622 C CA . LEU A 1 77 ? 24.661 17.500 35.587 1.00 26.38 ? 93 LEU A CA 1 ATOM 623 C C . LEU A 1 77 ? 26.051 17.704 34.987 1.00 25.46 ? 93 LEU A C 1 ATOM 624 O O . LEU A 1 77 ? 26.179 18.096 33.826 1.00 25.01 ? 93 LEU A O 1 ATOM 625 C CB . LEU A 1 77 ? 24.327 18.650 36.553 1.00 27.17 ? 93 LEU A CB 1 ATOM 626 C CG . LEU A 1 77 ? 22.905 18.763 37.113 1.00 27.94 ? 93 LEU A CG 1 ATOM 627 C CD1 . LEU A 1 77 ? 22.776 20.044 37.929 1.00 28.52 ? 93 LEU A CD1 1 ATOM 628 C CD2 . LEU A 1 77 ? 21.863 18.725 36.000 1.00 28.25 ? 93 LEU A CD2 1 ATOM 629 N N . LYS A 1 78 ? 27.088 17.399 35.765 1.00 24.98 ? 94 LYS A N 1 ATOM 630 C CA . LYS A 1 78 ? 28.472 17.495 35.279 1.00 24.99 ? 94 LYS A CA 1 ATOM 631 C C . LYS A 1 78 ? 28.713 16.633 34.031 1.00 24.65 ? 94 LYS A C 1 ATOM 632 O O . LYS A 1 78 ? 29.358 17.081 33.074 1.00 24.27 ? 94 LYS A O 1 ATOM 633 C CB . LYS A 1 78 ? 29.470 17.142 36.387 1.00 25.31 ? 94 LYS A CB 1 ATOM 634 C CG . LYS A 1 78 ? 29.450 18.117 37.565 1.00 25.40 ? 94 LYS A CG 1 ATOM 635 C CD . LYS A 1 78 ? 30.635 17.902 38.499 1.00 26.08 ? 94 LYS A CD 1 ATOM 636 C CE . LYS A 1 78 ? 30.397 16.728 39.437 1.00 26.61 ? 94 LYS A CE 1 ATOM 637 N NZ . LYS A 1 78 ? 31.608 16.450 40.266 1.00 26.32 ? 94 LYS A NZ 1 ATOM 638 N N . ARG A 1 79 ? 28.166 15.416 34.034 1.00 24.43 ? 95 ARG A N 1 ATOM 639 C CA . ARG A 1 79 ? 28.335 14.493 32.901 1.00 24.21 ? 95 ARG A CA 1 ATOM 640 C C . ARG A 1 79 ? 27.705 15.049 31.617 1.00 24.16 ? 95 ARG A C 1 ATOM 641 O O . ARG A 1 79 ? 28.302 14.957 30.539 1.00 23.64 ? 95 ARG A O 1 ATOM 642 C CB . ARG A 1 79 ? 27.788 13.097 33.242 1.00 23.99 ? 95 ARG A CB 1 ATOM 643 C CG . ARG A 1 79 ? 28.105 12.025 32.205 1.00 23.84 ? 95 ARG A CG 1 ATOM 644 C CD . ARG A 1 79 ? 27.670 10.624 32.635 1.00 23.94 ? 95 ARG A CD 1 ATOM 645 N NE . ARG A 1 79 ? 27.909 9.632 31.575 1.00 24.42 ? 95 ARG A NE 1 ATOM 646 C CZ . ARG A 1 79 ? 29.096 9.097 31.273 1.00 24.58 ? 95 ARG A CZ 1 ATOM 647 N NH1 . ARG A 1 79 ? 30.190 9.435 31.954 1.00 23.96 ? 95 ARG A NH1 1 ATOM 648 N NH2 . ARG A 1 79 ? 29.195 8.221 30.274 1.00 23.98 ? 95 ARG A NH2 1 ATOM 649 N N . GLN A 1 80 ? 26.511 15.630 31.742 1.00 24.76 ? 96 GLN A N 1 ATOM 650 C CA . GLN A 1 80 ? 25.822 16.258 30.608 1.00 24.97 ? 96 GLN A CA 1 ATOM 651 C C . GLN A 1 80 ? 26.587 17.476 30.075 1.00 24.72 ? 96 GLN A C 1 ATOM 652 O O . GLN A 1 80 ? 26.781 17.611 28.862 1.00 24.54 ? 96 GLN A O 1 ATOM 653 C CB . GLN A 1 80 ? 24.378 16.632 30.967 1.00 25.38 ? 96 GLN A CB 1 ATOM 654 C CG . GLN A 1 80 ? 23.472 15.439 31.275 1.00 26.01 ? 96 GLN A CG 1 ATOM 655 C CD . GLN A 1 80 ? 22.012 15.824 31.457 1.00 26.82 ? 96 GLN A CD 1 ATOM 656 O OE1 . GLN A 1 80 ? 21.399 16.438 30.578 1.00 26.61 ? 96 GLN A OE1 1 ATOM 657 N NE2 . GLN A 1 80 ? 21.449 15.469 32.608 1.00 27.39 ? 96 GLN A NE2 1 ATOM 658 N N . PHE A 1 81 ? 27.037 18.358 30.970 1.00 25.00 ? 97 PHE A N 1 ATOM 659 C CA . PHE A 1 81 ? 27.801 19.523 30.529 1.00 25.44 ? 97 PHE A CA 1 ATOM 660 C C . PHE A 1 81 ? 29.090 19.105 29.826 1.00 25.96 ? 97 PHE A C 1 ATOM 661 O O . PHE A 1 81 ? 29.447 19.663 28.789 1.00 25.60 ? 97 PHE A O 1 ATOM 662 C CB . PHE A 1 81 ? 28.101 20.476 31.687 1.00 25.63 ? 97 PHE A CB 1 ATOM 663 C CG . PHE A 1 81 ? 27.036 21.507 31.912 1.00 25.93 ? 97 PHE A CG 1 ATOM 664 C CD1 . PHE A 1 81 ? 26.963 22.635 31.102 1.00 26.41 ? 97 PHE A CD1 1 ATOM 665 C CD2 . PHE A 1 81 ? 26.111 21.358 32.944 1.00 26.10 ? 97 PHE A CD2 1 ATOM 666 C CE1 . PHE A 1 81 ? 25.976 23.597 31.309 1.00 26.77 ? 97 PHE A CE1 1 ATOM 667 C CE2 . PHE A 1 81 ? 25.125 22.313 33.154 1.00 26.79 ? 97 PHE A CE2 1 ATOM 668 C CZ . PHE A 1 81 ? 25.059 23.433 32.335 1.00 26.92 ? 97 PHE A CZ 1 ATOM 669 N N . LYS A 1 82 ? 29.775 18.109 30.378 1.00 26.61 ? 98 LYS A N 1 ATOM 670 C CA . LYS A 1 82 ? 30.993 17.613 29.750 1.00 28.86 ? 98 LYS A CA 1 ATOM 671 C C . LYS A 1 82 ? 30.737 17.133 28.318 1.00 28.49 ? 98 LYS A C 1 ATOM 672 O O . LYS A 1 82 ? 31.489 17.489 27.415 1.00 29.04 ? 98 LYS A O 1 ATOM 673 C CB . LYS A 1 82 ? 31.652 16.521 30.583 1.00 29.95 ? 98 LYS A CB 1 ATOM 674 C CG . LYS A 1 82 ? 33.121 16.362 30.254 1.00 33.06 ? 98 LYS A CG 1 ATOM 675 C CD . LYS A 1 82 ? 33.792 15.380 31.191 1.00 35.34 ? 98 LYS A CD 1 ATOM 676 C CE . LYS A 1 82 ? 35.132 14.985 30.610 1.00 37.91 ? 98 LYS A CE 1 ATOM 677 N NZ . LYS A 1 82 ? 35.775 13.950 31.466 1.00 42.03 ? 98 LYS A NZ 1 ATOM 678 N N . ALA A 1 83 ? 29.669 16.360 28.116 1.00 29.32 ? 99 ALA A N 1 ATOM 679 C CA . ALA A 1 83 ? 29.277 15.903 26.770 1.00 30.37 ? 99 ALA A CA 1 ATOM 680 C C . ALA A 1 83 ? 29.042 17.059 25.785 1.00 31.46 ? 99 ALA A C 1 ATOM 681 O O . ALA A 1 83 ? 29.425 16.969 24.613 1.00 31.44 ? 99 ALA A O 1 ATOM 682 C CB . ALA A 1 83 ? 28.055 14.997 26.842 1.00 30.28 ? 99 ALA A CB 1 ATOM 683 N N . LEU A 1 84 ? 28.442 18.150 26.262 1.00 32.70 ? 100 LEU A N 1 ATOM 684 C CA . LEU A 1 84 ? 28.191 19.334 25.419 1.00 34.66 ? 100 LEU A CA 1 ATOM 685 C C . LEU A 1 84 ? 29.428 20.156 25.059 1.00 35.89 ? 100 LEU A C 1 ATOM 686 O O . LEU A 1 84 ? 29.409 20.920 24.095 1.00 37.12 ? 100 LEU A O 1 ATOM 687 C CB . LEU A 1 84 ? 27.152 20.245 26.062 1.00 35.20 ? 100 LEU A CB 1 ATOM 688 C CG . LEU A 1 84 ? 25.758 19.657 26.266 1.00 35.78 ? 100 LEU A CG 1 ATOM 689 C CD1 . LEU A 1 84 ? 24.953 20.600 27.141 1.00 37.09 ? 100 LEU A CD1 1 ATOM 690 C CD2 . LEU A 1 84 ? 25.062 19.415 24.938 1.00 36.24 ? 100 LEU A CD2 1 ATOM 691 N N . THR A 1 85 ? 30.500 20.025 25.832 1.00 36.74 ? 101 THR A N 1 ATOM 692 C CA . THR A 1 85 ? 31.728 20.752 25.512 1.00 38.47 ? 101 THR A CA 1 ATOM 693 C C . THR A 1 85 ? 32.500 20.085 24.374 1.00 38.18 ? 101 THR A C 1 ATOM 694 O O . THR A 1 85 ? 33.410 20.686 23.804 1.00 39.69 ? 101 THR A O 1 ATOM 695 C CB . THR A 1 85 ? 32.666 20.890 26.728 1.00 39.53 ? 101 THR A CB 1 ATOM 696 O OG1 . THR A 1 85 ? 33.091 19.589 27.159 1.00 41.14 ? 101 THR A OG1 1 ATOM 697 C CG2 . THR A 1 85 ? 31.979 21.622 27.867 1.00 37.80 ? 101 THR A CG2 1 ATOM 698 N N . LYS A 1 86 ? 32.132 18.848 24.054 1.00 37.02 ? 102 LYS A N 1 ATOM 699 C CA . LYS A 1 86 ? 32.863 18.045 23.081 1.00 37.58 ? 102 LYS A CA 1 ATOM 700 C C . LYS A 1 86 ? 32.325 18.250 21.668 1.00 35.29 ? 102 LYS A C 1 ATOM 701 O O . LYS A 1 86 ? 31.367 17.605 21.266 1.00 36.93 ? 102 LYS A O 1 ATOM 702 C CB . LYS A 1 86 ? 32.820 16.566 23.475 1.00 39.09 ? 102 LYS A CB 1 ATOM 703 C CG . LYS A 1 86 ? 33.760 16.241 24.624 1.00 42.39 ? 102 LYS A CG 1 ATOM 704 C CD . LYS A 1 86 ? 33.425 14.911 25.276 1.00 45.45 ? 102 LYS A CD 1 ATOM 705 C CE . LYS A 1 86 ? 34.308 14.677 26.496 1.00 46.51 ? 102 LYS A CE 1 ATOM 706 N NZ . LYS A 1 86 ? 34.226 13.277 27.002 1.00 46.82 ? 102 LYS A NZ 1 ATOM 707 N N . LEU A 1 87 ? 32.976 19.139 20.924 1.00 32.93 ? 103 LEU A N 1 ATOM 708 C CA . LEU A 1 87 ? 32.493 19.603 19.617 1.00 29.98 ? 103 LEU A CA 1 ATOM 709 C C . LEU A 1 87 ? 32.810 18.684 18.439 1.00 28.10 ? 103 LEU A C 1 ATOM 710 O O . LEU A 1 87 ? 32.094 18.705 17.438 1.00 27.27 ? 103 LEU A O 1 ATOM 711 C CB . LEU A 1 87 ? 33.073 20.988 19.314 1.00 30.06 ? 103 LEU A CB 1 ATOM 712 C CG . LEU A 1 87 ? 32.452 22.207 19.988 1.00 31.28 ? 103 LEU A CG 1 ATOM 713 C CD1 . LEU A 1 87 ? 33.248 23.457 19.642 1.00 31.60 ? 103 LEU A CD1 1 ATOM 714 C CD2 . LEU A 1 87 ? 30.991 22.364 19.586 1.00 30.92 ? 103 LEU A CD2 1 ATOM 715 N N . GLY A 1 88 ? 33.889 17.906 18.543 1.00 25.84 ? 104 GLY A N 1 ATOM 716 C CA . GLY A 1 88 ? 34.370 17.107 17.413 1.00 24.61 ? 104 GLY A CA 1 ATOM 717 C C . GLY A 1 88 ? 34.669 17.995 16.215 1.00 23.52 ? 104 GLY A C 1 ATOM 718 O O . GLY A 1 88 ? 35.246 19.085 16.357 1.00 22.64 ? 104 GLY A O 1 ATOM 719 N N . TYR A 1 89 ? 34.238 17.553 15.037 1.00 23.01 ? 105 TYR A N 1 ATOM 720 C CA . TYR A 1 89 ? 34.469 18.302 13.800 1.00 23.70 ? 105 TYR A CA 1 ATOM 721 C C . TYR A 1 89 ? 33.890 19.720 13.814 1.00 23.87 ? 105 TYR A C 1 ATOM 722 O O . TYR A 1 89 ? 34.422 20.614 13.154 1.00 24.01 ? 105 TYR A O 1 ATOM 723 C CB . TYR A 1 89 ? 33.914 17.543 12.587 1.00 23.39 ? 105 TYR A CB 1 ATOM 724 C CG . TYR A 1 89 ? 34.615 16.232 12.263 1.00 23.38 ? 105 TYR A CG 1 ATOM 725 C CD1 . TYR A 1 89 ? 35.905 15.952 12.738 1.00 23.18 ? 105 TYR A CD1 1 ATOM 726 C CD2 . TYR A 1 89 ? 34.004 15.297 11.439 1.00 23.32 ? 105 TYR A CD2 1 ATOM 727 C CE1 . TYR A 1 89 ? 36.540 14.759 12.427 1.00 23.32 ? 105 TYR A CE1 1 ATOM 728 C CE2 . TYR A 1 89 ? 34.628 14.101 11.118 1.00 23.16 ? 105 TYR A CE2 1 ATOM 729 C CZ . TYR A 1 89 ? 35.893 13.839 11.599 1.00 22.85 ? 105 TYR A CZ 1 ATOM 730 O OH . TYR A 1 89 ? 36.511 12.653 11.272 1.00 22.46 ? 105 TYR A OH 1 ATOM 731 N N . ALA A 1 90 ? 32.813 19.917 14.569 1.00 23.76 ? 106 ALA A N 1 ATOM 732 C CA . ALA A 1 90 ? 32.157 21.220 14.661 1.00 24.26 ? 106 ALA A CA 1 ATOM 733 C C . ALA A 1 90 ? 33.045 22.311 15.289 1.00 24.77 ? 106 ALA A C 1 ATOM 734 O O . ALA A 1 90 ? 32.690 23.496 15.268 1.00 25.29 ? 106 ALA A O 1 ATOM 735 C CB . ALA A 1 90 ? 30.844 21.085 15.410 1.00 24.04 ? 106 ALA A CB 1 ATOM 736 N N . ALA A 1 91 ? 34.202 21.918 15.831 1.00 24.41 ? 107 ALA A N 1 ATOM 737 C CA . ALA A 1 91 ? 35.188 22.887 16.329 1.00 24.78 ? 107 ALA A CA 1 ATOM 738 C C . ALA A 1 91 ? 35.912 23.645 15.203 1.00 25.85 ? 107 ALA A C 1 ATOM 739 O O . ALA A 1 91 ? 36.500 24.700 15.450 1.00 26.51 ? 107 ALA A O 1 ATOM 740 C CB . ALA A 1 91 ? 36.204 22.203 17.244 1.00 24.27 ? 107 ALA A CB 1 ATOM 741 N N . LEU A 1 92 ? 35.875 23.109 13.982 1.00 25.59 ? 108 LEU A N 1 ATOM 742 C CA . LEU A 1 92 ? 36.593 23.697 12.842 1.00 26.17 ? 108 LEU A CA 1 ATOM 743 C C . LEU A 1 92 ? 35.989 25.038 12.379 1.00 27.11 ? 108 LEU A C 1 ATOM 744 O O . LEU A 1 92 ? 34.775 25.220 12.457 1.00 26.69 ? 108 LEU A O 1 ATOM 745 C CB . LEU A 1 92 ? 36.596 22.722 11.658 1.00 25.77 ? 108 LEU A CB 1 ATOM 746 C CG . LEU A 1 92 ? 37.508 21.491 11.667 1.00 25.62 ? 108 LEU A CG 1 ATOM 747 C CD1 . LEU A 1 92 ? 37.052 20.499 10.607 1.00 25.64 ? 108 LEU A CD1 1 ATOM 748 C CD2 . LEU A 1 92 ? 38.965 21.875 11.451 1.00 25.54 ? 108 LEU A CD2 1 ATOM 749 N N . PRO A 1 93 ? 36.836 25.975 11.892 1.00 27.61 ? 109 PRO A N 1 ATOM 750 C CA . PRO A 1 93 ? 36.328 27.196 11.256 1.00 29.08 ? 109 PRO A CA 1 ATOM 751 C C . PRO A 1 93 ? 35.334 26.829 10.163 1.00 28.98 ? 109 PRO A C 1 ATOM 752 O O . PRO A 1 93 ? 35.463 25.760 9.554 1.00 28.14 ? 109 PRO A O 1 ATOM 753 C CB . PRO A 1 93 ? 37.579 27.819 10.625 1.00 29.51 ? 109 PRO A CB 1 ATOM 754 C CG . PRO A 1 93 ? 38.705 27.332 11.478 1.00 29.79 ? 109 PRO A CG 1 ATOM 755 C CD . PRO A 1 93 ? 38.311 25.950 11.938 1.00 28.27 ? 109 PRO A CD 1 ATOM 756 N N . GLU A 1 94 ? 34.357 27.706 9.941 1.00 29.58 ? 110 GLU A N 1 ATOM 757 C CA . GLU A 1 94 ? 33.248 27.470 9.010 1.00 30.46 ? 110 GLU A CA 1 ATOM 758 C C . GLU A 1 94 ? 33.691 26.885 7.664 1.00 31.08 ? 110 GLU A C 1 ATOM 759 O O . GLU A 1 94 ? 33.142 25.879 7.216 1.00 31.21 ? 110 GLU A O 1 ATOM 760 C CB . GLU A 1 94 ? 32.443 28.761 8.794 0.50 30.37 ? 110 GLU A CB 1 ATOM 761 C CG . GLU A 1 94 ? 31.166 28.571 7.995 0.50 30.50 ? 110 GLU A CG 1 ATOM 762 C CD . GLU A 1 94 ? 30.562 29.881 7.523 0.50 31.03 ? 110 GLU A CD 1 ATOM 763 O OE1 . GLU A 1 94 ? 30.976 30.945 8.015 0.50 30.78 ? 110 GLU A OE1 1 ATOM 764 O OE2 . GLU A 1 94 ? 29.673 29.843 6.647 0.50 31.66 ? 110 GLU A OE2 1 ATOM 765 N N . ASP A 1 95 ? 34.676 27.518 7.028 1.00 32.77 ? 111 ASP A N 1 ATOM 766 C CA . ASP A 1 95 ? 35.181 27.064 5.724 1.00 33.94 ? 111 ASP A CA 1 ATOM 767 C C . ASP A 1 95 ? 35.859 25.689 5.787 1.00 32.79 ? 111 ASP A C 1 ATOM 768 O O . ASP A 1 95 ? 35.684 24.875 4.876 1.00 32.46 ? 111 ASP A O 1 ATOM 769 C CB . ASP A 1 95 ? 36.138 28.093 5.120 1.00 36.42 ? 111 ASP A CB 1 ATOM 770 C CG . ASP A 1 95 ? 35.419 29.341 4.603 1.00 40.16 ? 111 ASP A CG 1 ATOM 771 O OD1 . ASP A 1 95 ? 34.165 29.391 4.603 1.00 40.89 ? 111 ASP A OD1 1 ATOM 772 O OD2 . ASP A 1 95 ? 36.122 30.288 4.192 1.00 43.34 ? 111 ASP A OD2 1 ATOM 773 N N . ASP A 1 96 ? 36.621 25.437 6.857 1.00 31.39 ? 112 ASP A N 1 ATOM 774 C CA . ASP A 1 96 ? 37.272 24.133 7.064 1.00 30.40 ? 112 ASP A CA 1 ATOM 775 C C . ASP A 1 96 ? 36.273 23.003 7.276 1.00 29.02 ? 112 ASP A C 1 ATOM 776 O O . ASP A 1 96 ? 36.511 21.877 6.841 1.00 28.55 ? 112 ASP A O 1 ATOM 777 C CB . ASP A 1 96 ? 38.231 24.167 8.255 1.00 30.94 ? 112 ASP A CB 1 ATOM 778 C CG . ASP A 1 96 ? 39.491 24.955 7.971 1.00 32.62 ? 112 ASP A CG 1 ATOM 779 O OD1 . ASP A 1 96 ? 39.792 25.236 6.793 1.00 33.43 ? 112 ASP A OD1 1 ATOM 780 O OD2 . ASP A 1 96 ? 40.190 25.295 8.942 1.00 34.13 ? 112 ASP A OD2 1 ATOM 781 N N . TYR A 1 97 ? 35.172 23.303 7.958 1.00 28.25 ? 113 TYR A N 1 ATOM 782 C CA . TYR A 1 97 ? 34.129 22.317 8.190 1.00 28.07 ? 113 TYR A CA 1 ATOM 783 C C . TYR A 1 97 ? 33.440 21.953 6.876 1.00 28.43 ? 113 TYR A C 1 ATOM 784 O O . TYR A 1 97 ? 33.216 20.776 6.604 1.00 27.86 ? 113 TYR A O 1 ATOM 785 C CB . TYR A 1 97 ? 33.105 22.819 9.219 1.00 28.48 ? 113 TYR A CB 1 ATOM 786 C CG . TYR A 1 97 ? 32.086 21.769 9.600 1.00 28.48 ? 113 TYR A CG 1 ATOM 787 C CD1 . TYR A 1 97 ? 32.420 20.732 10.469 1.00 28.54 ? 113 TYR A CD1 1 ATOM 788 C CD2 . TYR A 1 97 ? 30.797 21.794 9.077 1.00 28.99 ? 113 TYR A CD2 1 ATOM 789 C CE1 . TYR A 1 97 ? 31.500 19.755 10.812 1.00 28.80 ? 113 TYR A CE1 1 ATOM 790 C CE2 . TYR A 1 97 ? 29.870 20.817 9.417 1.00 29.02 ? 113 TYR A CE2 1 ATOM 791 C CZ . TYR A 1 97 ? 30.230 19.804 10.288 1.00 28.67 ? 113 TYR A CZ 1 ATOM 792 O OH . TYR A 1 97 ? 29.327 18.834 10.631 1.00 28.75 ? 113 TYR A OH 1 ATOM 793 N N . ALA A 1 98 ? 33.120 22.962 6.064 1.00 28.82 ? 114 ALA A N 1 ATOM 794 C CA . ALA A 1 98 ? 32.476 22.733 4.762 1.00 28.96 ? 114 ALA A CA 1 ATOM 795 C C . ALA A 1 98 ? 33.362 21.904 3.819 1.00 28.95 ? 114 ALA A C 1 ATOM 796 O O . ALA A 1 98 ? 32.871 20.997 3.145 1.00 29.60 ? 114 ALA A O 1 ATOM 797 C CB . ALA A 1 98 ? 32.080 24.053 4.113 1.00 29.04 ? 114 ALA A CB 1 ATOM 798 N N . GLU A 1 99 ? 34.656 22.222 3.774 1.00 28.50 ? 115 GLU A N 1 ATOM 799 C CA . GLU A 1 99 ? 35.619 21.443 3.001 1.00 28.80 ? 115 GLU A CA 1 ATOM 800 C C . GLU A 1 99 ? 35.702 19.980 3.474 1.00 28.07 ? 115 GLU A C 1 ATOM 801 O O . GLU A 1 99 ? 35.745 19.060 2.657 1.00 27.69 ? 115 GLU A O 1 ATOM 802 C CB . GLU A 1 99 ? 37.010 22.093 3.016 1.00 29.71 ? 115 GLU A CB 1 ATOM 803 C CG . GLU A 1 99 ? 37.981 21.416 2.054 1.00 30.91 ? 115 GLU A CG 1 ATOM 804 C CD . GLU A 1 99 ? 39.394 21.969 2.094 1.00 31.95 ? 115 GLU A CD 1 ATOM 805 O OE1 . GLU A 1 99 ? 39.675 22.880 2.908 1.00 32.99 ? 115 GLU A OE1 1 ATOM 806 O OE2 . GLU A 1 99 ? 40.236 21.479 1.301 1.00 31.81 ? 115 GLU A OE2 1 ATOM 807 N N . LEU A 1 100 ? 35.717 19.764 4.788 1.00 27.17 ? 116 LEU A N 1 ATOM 808 C CA . LEU A 1 100 ? 35.705 18.400 5.311 1.00 26.73 ? 116 LEU A CA 1 ATOM 809 C C . LEU A 1 100 ? 34.454 17.627 4.876 1.00 26.72 ? 116 LEU A C 1 ATOM 810 O O . LEU A 1 100 ? 34.556 16.485 4.429 1.00 25.94 ? 116 LEU A O 1 ATOM 811 C CB . LEU A 1 100 ? 35.859 18.379 6.837 1.00 26.47 ? 116 LEU A CB 1 ATOM 812 C CG . LEU A 1 100 ? 35.850 16.993 7.507 1.00 26.55 ? 116 LEU A CG 1 ATOM 813 C CD1 . LEU A 1 100 ? 36.921 16.060 6.949 1.00 26.01 ? 116 LEU A CD1 1 ATOM 814 C CD2 . LEU A 1 100 ? 36.019 17.164 9.001 1.00 26.15 ? 116 LEU A CD2 1 ATOM 815 N N . LEU A 1 101 ? 33.282 18.247 4.994 1.00 26.65 ? 117 LEU A N 1 ATOM 816 C CA . LEU A 1 101 ? 32.044 17.588 4.596 1.00 27.31 ? 117 LEU A CA 1 ATOM 817 C C . LEU A 1 101 ? 32.071 17.228 3.110 1.00 27.40 ? 117 LEU A C 1 ATOM 818 O O . LEU A 1 101 ? 31.634 16.144 2.724 1.00 27.09 ? 117 LEU A O 1 ATOM 819 C CB . LEU A 1 101 ? 30.836 18.477 4.891 1.00 28.35 ? 117 LEU A CB 1 ATOM 820 C CG . LEU A 1 101 ? 30.432 18.696 6.354 1.00 28.75 ? 117 LEU A CG 1 ATOM 821 C CD1 . LEU A 1 101 ? 29.221 19.615 6.383 1.00 29.75 ? 117 LEU A CD1 1 ATOM 822 C CD2 . LEU A 1 101 ? 30.132 17.388 7.066 1.00 28.59 ? 117 LEU A CD2 1 ATOM 823 N N . ASP A 1 102 ? 32.594 18.141 2.292 1.00 28.61 ? 118 ASP A N 1 ATOM 824 C CA . ASP A 1 102 ? 32.757 17.891 0.849 1.00 29.39 ? 118 ASP A CA 1 ATOM 825 C C . ASP A 1 102 ? 33.708 16.715 0.590 1.00 28.58 ? 118 ASP A C 1 ATOM 826 O O . ASP A 1 102 ? 33.451 15.880 -0.283 1.00 28.57 ? 118 ASP A O 1 ATOM 827 C CB . ASP A 1 102 ? 33.271 19.142 0.136 1.00 32.01 ? 118 ASP A CB 1 ATOM 828 C CG . ASP A 1 102 ? 32.186 20.200 -0.079 1.00 34.98 ? 118 ASP A CG 1 ATOM 829 O OD1 . ASP A 1 102 ? 30.972 19.881 -0.027 1.00 36.41 ? 118 ASP A OD1 1 ATOM 830 O OD2 . ASP A 1 102 ? 32.559 21.371 -0.310 1.00 37.13 ? 118 ASP A OD2 1 ATOM 831 N N . THR A 1 103 ? 34.792 16.647 1.361 1.00 27.61 ? 119 THR A N 1 ATOM 832 C CA . THR A 1 103 ? 35.759 15.541 1.283 1.00 26.96 ? 119 THR A CA 1 ATOM 833 C C . THR A 1 103 ? 35.117 14.203 1.668 1.00 26.24 ? 119 THR A C 1 ATOM 834 O O . THR A 1 103 ? 35.332 13.192 1.012 1.00 26.18 ? 119 THR A O 1 ATOM 835 C CB . THR A 1 103 ? 36.983 15.808 2.187 1.00 26.11 ? 119 THR A CB 1 ATOM 836 O OG1 . THR A 1 103 ? 37.470 17.125 1.943 1.00 27.01 ? 119 THR A OG1 1 ATOM 837 C CG2 . THR A 1 103 ? 38.105 14.821 1.914 1.00 25.49 ? 119 THR A CG2 1 ATOM 838 N N . LEU A 1 104 ? 34.324 14.205 2.736 1.00 26.21 ? 120 LEU A N 1 ATOM 839 C CA . LEU A 1 104 ? 33.686 12.982 3.219 1.00 25.53 ? 120 LEU A CA 1 ATOM 840 C C . LEU A 1 104 ? 32.682 12.416 2.204 1.00 26.20 ? 120 LEU A C 1 ATOM 841 O O . LEU A 1 104 ? 32.652 11.199 1.957 1.00 24.88 ? 120 LEU A O 1 ATOM 842 C CB . LEU A 1 104 ? 33.032 13.203 4.594 1.00 25.42 ? 120 LEU A CB 1 ATOM 843 C CG . LEU A 1 104 ? 34.018 13.474 5.741 1.00 25.03 ? 120 LEU A CG 1 ATOM 844 C CD1 . LEU A 1 104 ? 33.304 13.866 7.033 1.00 24.74 ? 120 LEU A CD1 1 ATOM 845 C CD2 . LEU A 1 104 ? 34.964 12.297 5.963 1.00 24.31 ? 120 LEU A CD2 1 ATOM 846 N N . SER A 1 105 ? 31.878 13.291 1.601 1.00 26.31 ? 121 SER A N 1 ATOM 847 C CA . SER A 1 105 ? 30.883 12.811 0.655 1.00 27.11 ? 121 SER A CA 1 ATOM 848 C C . SER A 1 105 ? 31.532 12.382 -0.663 1.00 26.63 ? 121 SER A C 1 ATOM 849 O O . SER A 1 105 ? 31.051 11.455 -1.306 1.00 27.05 ? 121 SER A O 1 ATOM 850 C CB . SER A 1 105 ? 29.707 13.786 0.459 1.00 27.80 ? 121 SER A CB 1 ATOM 851 O OG . SER A 1 105 ? 30.142 15.088 0.133 1.00 29.09 ? 121 SER A OG 1 ATOM 852 N N . ALA A 1 106 ? 32.633 13.029 -1.044 1.00 26.03 ? 122 ALA A N 1 ATOM 853 C CA . ALA A 1 106 ? 33.384 12.581 -2.222 1.00 26.06 ? 122 ALA A CA 1 ATOM 854 C C . ALA A 1 106 ? 33.862 11.137 -2.023 1.00 25.64 ? 122 ALA A C 1 ATOM 855 O O . ALA A 1 106 ? 33.724 10.308 -2.913 1.00 25.49 ? 122 ALA A O 1 ATOM 856 C CB . ALA A 1 106 ? 34.554 13.502 -2.520 1.00 26.14 ? 122 ALA A CB 1 ATOM 857 N N . MET A 1 107 ? 34.361 10.822 -0.831 1.00 24.85 ? 123 MET A N 1 ATOM 858 C CA . MET A 1 107 ? 34.849 9.467 -0.561 1.00 24.88 ? 123 MET A CA 1 ATOM 859 C C . MET A 1 107 ? 33.737 8.430 -0.433 1.00 24.66 ? 123 MET A C 1 ATOM 860 O O . MET A 1 107 ? 33.883 7.312 -0.915 1.00 24.28 ? 123 MET A O 1 ATOM 861 C CB . MET A 1 107 ? 35.740 9.436 0.689 1.00 24.73 ? 123 MET A CB 1 ATOM 862 C CG . MET A 1 107 ? 37.017 10.236 0.528 1.00 26.11 ? 123 MET A CG 1 ATOM 863 S SD . MET A 1 107 ? 38.272 9.847 1.758 1.00 27.41 ? 123 MET A SD 1 ATOM 864 C CE . MET A 1 107 ? 37.467 10.445 3.247 1.00 25.86 ? 123 MET A CE 1 ATOM 865 N N . GLU A 1 108 ? 32.642 8.782 0.237 1.00 25.64 ? 124 GLU A N 1 ATOM 866 C CA . GLU A 1 108 ? 31.558 7.823 0.423 1.00 26.94 ? 124 GLU A CA 1 ATOM 867 C C . GLU A 1 108 ? 30.839 7.541 -0.905 1.00 27.32 ? 124 GLU A C 1 ATOM 868 O O . GLU A 1 108 ? 30.536 6.384 -1.200 1.00 27.12 ? 124 GLU A O 1 ATOM 869 C CB . GLU A 1 108 ? 30.579 8.239 1.538 1.00 28.73 ? 124 GLU A CB 1 ATOM 870 C CG . GLU A 1 108 ? 29.424 7.248 1.703 1.00 31.61 ? 124 GLU A CG 1 ATOM 871 C CD . GLU A 1 108 ? 28.895 7.091 3.124 1.00 33.39 ? 124 GLU A CD 1 ATOM 872 O OE1 . GLU A 1 108 ? 29.360 7.799 4.054 1.00 34.32 ? 124 GLU A OE1 1 ATOM 873 O OE2 . GLU A 1 108 ? 28.003 6.233 3.312 1.00 33.84 ? 124 GLU A OE2 1 ATOM 874 N N . SER A 1 109 ? 30.599 8.583 -1.704 1.00 27.14 ? 125 SER A N 1 ATOM 875 C CA . SER A 1 109 ? 29.945 8.410 -3.017 1.00 27.83 ? 125 SER A CA 1 ATOM 876 C C . SER A 1 109 ? 30.819 7.660 -4.029 1.00 27.58 ? 125 SER A C 1 ATOM 877 O O . SER A 1 109 ? 30.299 6.866 -4.823 1.00 28.49 ? 125 SER A O 1 ATOM 878 C CB . SER A 1 109 ? 29.458 9.741 -3.601 1.00 28.06 ? 125 SER A CB 1 ATOM 879 O OG . SER A 1 109 ? 30.548 10.557 -3.979 1.00 28.67 ? 125 SER A OG 1 ATOM 880 N N . ASN A 1 110 ? 32.129 7.917 -4.015 1.00 26.62 ? 126 ASN A N 1 ATOM 881 C CA . ASN A 1 110 ? 33.063 7.117 -4.808 1.00 25.74 ? 126 ASN A CA 1 ATOM 882 C C . ASN A 1 110 ? 32.897 5.633 -4.486 1.00 25.09 ? 126 ASN A C 1 ATOM 883 O O . ASN A 1 110 ? 32.737 4.811 -5.390 1.00 24.45 ? 126 ASN A O 1 ATOM 884 C CB . ASN A 1 110 ? 34.517 7.538 -4.588 1.00 25.43 ? 126 ASN A CB 1 ATOM 885 C CG . ASN A 1 110 ? 35.491 6.707 -5.410 1.00 26.00 ? 126 ASN A CG 1 ATOM 886 O OD1 . ASN A 1 110 ? 35.703 6.978 -6.593 1.00 26.32 ? 126 ASN A OD1 1 ATOM 887 N ND2 . ASN A 1 110 ? 36.082 5.692 -4.796 1.00 24.91 ? 126 ASN A ND2 1 ATOM 888 N N . PHE A 1 111 ? 32.927 5.295 -3.196 1.00 23.88 ? 127 PHE A N 1 ATOM 889 C CA . PHE A 1 111 ? 32.767 3.908 -2.768 1.00 23.83 ? 127 PHE A CA 1 ATOM 890 C C . PHE A 1 111 ? 31.457 3.305 -3.276 1.00 24.55 ? 127 PHE A C 1 ATOM 891 O O . PHE A 1 111 ? 31.461 2.223 -3.868 1.00 24.70 ? 127 PHE A O 1 ATOM 892 C CB . PHE A 1 111 ? 32.844 3.784 -1.227 1.00 23.35 ? 127 PHE A CB 1 ATOM 893 C CG . PHE A 1 111 ? 32.886 2.358 -0.735 1.00 23.00 ? 127 PHE A CG 1 ATOM 894 C CD1 . PHE A 1 111 ? 31.706 1.648 -0.490 1.00 22.77 ? 127 PHE A CD1 1 ATOM 895 C CD2 . PHE A 1 111 ? 34.107 1.716 -0.522 1.00 22.93 ? 127 PHE A CD2 1 ATOM 896 C CE1 . PHE A 1 111 ? 31.740 0.328 -0.065 1.00 22.24 ? 127 PHE A CE1 1 ATOM 897 C CE2 . PHE A 1 111 ? 34.148 0.392 -0.094 1.00 22.29 ? 127 PHE A CE2 1 ATOM 898 C CZ . PHE A 1 111 ? 32.963 -0.300 0.143 1.00 22.35 ? 127 PHE A CZ 1 ATOM 899 N N . ALA A 1 112 ? 30.343 4.004 -3.039 1.00 24.66 ? 128 ALA A N 1 ATOM 900 C CA . ALA A 1 112 ? 29.021 3.495 -3.383 1.00 25.55 ? 128 ALA A CA 1 ATOM 901 C C . ALA A 1 112 ? 28.833 3.347 -4.896 1.00 26.47 ? 128 ALA A C 1 ATOM 902 O O . ALA A 1 112 ? 28.052 2.514 -5.348 1.00 27.24 ? 128 ALA A O 1 ATOM 903 C CB . ALA A 1 112 ? 27.936 4.391 -2.804 1.00 25.85 ? 128 ALA A CB 1 ATOM 904 N N . LYS A 1 113 ? 29.561 4.147 -5.666 1.00 27.51 ? 129 LYS A N 1 ATOM 905 C CA . LYS A 1 113 ? 29.403 4.161 -7.127 1.00 28.89 ? 129 LYS A CA 1 ATOM 906 C C . LYS A 1 113 ? 30.322 3.213 -7.929 1.00 28.86 ? 129 LYS A C 1 ATOM 907 O O . LYS A 1 113 ? 30.200 3.129 -9.154 1.00 29.63 ? 129 LYS A O 1 ATOM 908 C CB . LYS A 1 113 ? 29.534 5.588 -7.650 1.00 30.59 ? 129 LYS A CB 1 ATOM 909 C CG . LYS A 1 113 ? 28.303 6.449 -7.428 1.00 33.01 ? 129 LYS A CG 1 ATOM 910 C CD . LYS A 1 113 ? 28.637 7.888 -7.780 1.00 35.83 ? 129 LYS A CD 1 ATOM 911 C CE . LYS A 1 113 ? 27.393 8.715 -8.025 1.00 38.85 ? 129 LYS A CE 1 ATOM 912 N NZ . LYS A 1 113 ? 27.757 10.160 -7.979 1.00 41.97 ? 129 LYS A NZ 1 ATOM 913 N N . VAL A 1 114 ? 31.232 2.511 -7.254 1.00 28.47 ? 130 VAL A N 1 ATOM 914 C CA . VAL A 1 114 ? 32.165 1.589 -7.927 1.00 27.84 ? 130 VAL A CA 1 ATOM 915 C C . VAL A 1 114 ? 31.436 0.526 -8.758 1.00 28.18 ? 130 VAL A C 1 ATOM 916 O O . VAL A 1 114 ? 30.544 -0.172 -8.258 1.00 28.12 ? 130 VAL A O 1 ATOM 917 C CB . VAL A 1 114 ? 33.118 0.890 -6.917 1.00 27.24 ? 130 VAL A CB 1 ATOM 918 C CG1 . VAL A 1 114 ? 33.878 -0.260 -7.588 1.00 26.34 ? 130 VAL A CG1 1 ATOM 919 C CG2 . VAL A 1 114 ? 34.090 1.895 -6.308 1.00 26.33 ? 130 VAL A CG2 1 ATOM 920 N N . LYS A 1 115 ? 31.817 0.424 -10.031 1.00 28.73 ? 131 LYS A N 1 ATOM 921 C CA . LYS A 1 115 ? 31.332 -0.632 -10.916 1.00 29.65 ? 131 LYS A CA 1 ATOM 922 C C . LYS A 1 115 ? 32.522 -1.202 -11.662 1.00 29.27 ? 131 LYS A C 1 ATOM 923 O O . LYS A 1 115 ? 33.434 -0.461 -12.009 1.00 29.11 ? 131 LYS A O 1 ATOM 924 C CB . LYS A 1 115 ? 30.316 -0.083 -11.924 1.00 30.92 ? 131 LYS A CB 1 ATOM 925 C CG . LYS A 1 115 ? 29.051 0.537 -11.337 1.00 31.71 ? 131 LYS A CG 1 ATOM 926 C CD . LYS A 1 115 ? 28.014 -0.520 -10.995 1.00 33.35 ? 131 LYS A CD 1 ATOM 927 C CE . LYS A 1 115 ? 26.597 0.044 -11.035 1.00 34.61 ? 131 LYS A CE 1 ATOM 928 N NZ . LYS A 1 115 ? 26.319 0.931 -9.872 1.00 35.76 ? 131 LYS A NZ 1 ATOM 929 N N . VAL A 1 116 ? 32.516 -2.515 -11.901 1.00 29.75 ? 132 VAL A N 1 ATOM 930 C CA . VAL A 1 116 ? 33.609 -3.180 -12.633 1.00 30.51 ? 132 VAL A CA 1 ATOM 931 C C . VAL A 1 116 ? 33.075 -3.947 -13.851 1.00 32.16 ? 132 VAL A C 1 ATOM 932 O O . VAL A 1 116 ? 31.868 -4.206 -13.957 1.00 31.95 ? 132 VAL A O 1 ATOM 933 C CB . VAL A 1 116 ? 34.487 -4.097 -11.727 1.00 29.88 ? 132 VAL A CB 1 ATOM 934 C CG1 . VAL A 1 116 ? 34.996 -3.341 -10.507 1.00 29.09 ? 132 VAL A CG1 1 ATOM 935 C CG2 . VAL A 1 116 ? 33.736 -5.348 -11.295 1.00 29.33 ? 132 VAL A CG2 1 ATOM 936 N N . CYS A 1 117 ? 33.975 -4.294 -14.767 1.00 33.20 ? 133 CYS A N 1 ATOM 937 C CA . CYS A 1 117 ? 33.607 -5.104 -15.928 1.00 35.17 ? 133 CYS A CA 1 ATOM 938 C C . CYS A 1 117 ? 33.681 -6.591 -15.610 1.00 34.47 ? 133 CYS A C 1 ATOM 939 O O . CYS A 1 117 ? 34.554 -7.033 -14.854 1.00 32.66 ? 133 CYS A O 1 ATOM 940 C CB . CYS A 1 117 ? 34.479 -4.756 -17.135 1.00 37.98 ? 133 CYS A CB 1 ATOM 941 S SG . CYS A 1 117 ? 34.355 -3.016 -17.615 1.00 41.54 ? 133 CYS A SG 1 ATOM 942 N N . ASP A 1 118 ? 32.750 -7.352 -16.183 1.00 34.50 ? 134 ASP A N 1 ATOM 943 C CA . ASP A 1 118 ? 32.696 -8.803 -16.009 1.00 35.21 ? 134 ASP A CA 1 ATOM 944 C C . ASP A 1 118 ? 34.017 -9.445 -16.466 1.00 35.09 ? 134 ASP A C 1 ATOM 945 O O . ASP A 1 118 ? 34.554 -9.093 -17.520 1.00 35.29 ? 134 ASP A O 1 ATOM 946 C CB . ASP A 1 118 ? 31.505 -9.364 -16.796 1.00 37.09 ? 134 ASP A CB 1 ATOM 947 C CG . ASP A 1 118 ? 31.212 -10.827 -16.489 1.00 38.07 ? 134 ASP A CG 1 ATOM 948 O OD1 . ASP A 1 118 ? 32.064 -11.696 -16.765 1.00 39.60 ? 134 ASP A OD1 1 ATOM 949 O OD2 . ASP A 1 118 ? 30.101 -11.116 -16.004 1.00 38.80 ? 134 ASP A OD2 1 ATOM 950 N N . TYR A 1 119 ? 34.530 -10.372 -15.657 1.00 34.39 ? 135 TYR A N 1 ATOM 951 C CA . TYR A 1 119 ? 35.737 -11.154 -15.970 1.00 34.44 ? 135 TYR A CA 1 ATOM 952 C C . TYR A 1 119 ? 35.660 -11.859 -17.328 1.00 36.75 ? 135 TYR A C 1 ATOM 953 O O . TYR A 1 119 ? 36.666 -11.982 -18.017 1.00 36.82 ? 135 TYR A O 1 ATOM 954 C CB . TYR A 1 119 ? 35.986 -12.195 -14.866 1.00 33.08 ? 135 TYR A CB 1 ATOM 955 C CG . TYR A 1 119 ? 37.241 -13.040 -15.023 1.00 32.17 ? 135 TYR A CG 1 ATOM 956 C CD1 . TYR A 1 119 ? 38.508 -12.449 -15.103 1.00 31.65 ? 135 TYR A CD1 1 ATOM 957 C CD2 . TYR A 1 119 ? 37.161 -14.432 -15.067 1.00 31.67 ? 135 TYR A CD2 1 ATOM 958 C CE1 . TYR A 1 119 ? 39.657 -13.220 -15.233 1.00 31.40 ? 135 TYR A CE1 1 ATOM 959 C CE2 . TYR A 1 119 ? 38.305 -15.215 -15.204 1.00 31.78 ? 135 TYR A CE2 1 ATOM 960 C CZ . TYR A 1 119 ? 39.548 -14.606 -15.286 1.00 31.42 ? 135 TYR A CZ 1 ATOM 961 O OH . TYR A 1 119 ? 40.677 -15.385 -15.412 1.00 31.44 ? 135 TYR A OH 1 ATOM 962 N N . LYS A 1 120 ? 34.466 -12.320 -17.688 1.00 39.41 ? 136 LYS A N 1 ATOM 963 C CA . LYS A 1 120 ? 34.252 -13.083 -18.920 1.00 43.69 ? 136 LYS A CA 1 ATOM 964 C C . LYS A 1 120 ? 33.603 -12.262 -20.042 1.00 45.16 ? 136 LYS A C 1 ATOM 965 O O . LYS A 1 120 ? 33.474 -12.746 -21.169 1.00 46.08 ? 136 LYS A O 1 ATOM 966 C CB . LYS A 1 120 ? 33.411 -14.329 -18.626 1.00 45.06 ? 136 LYS A CB 1 ATOM 967 C CG . LYS A 1 120 ? 34.131 -15.374 -17.788 1.00 48.44 ? 136 LYS A CG 1 ATOM 968 C CD . LYS A 1 120 ? 33.218 -16.546 -17.455 1.00 51.65 ? 136 LYS A CD 1 ATOM 969 C CE . LYS A 1 120 ? 33.974 -17.671 -16.753 1.00 53.39 ? 136 LYS A CE 1 ATOM 970 N NZ . LYS A 1 120 ? 34.210 -17.399 -15.305 1.00 51.57 ? 136 LYS A NZ 1 ATOM 971 N N . ASP A 1 121 ? 33.213 -11.024 -19.747 1.00 45.50 ? 137 ASP A N 1 ATOM 972 C CA . ASP A 1 121 ? 32.503 -10.194 -20.720 1.00 47.69 ? 137 ASP A CA 1 ATOM 973 C C . ASP A 1 121 ? 32.820 -8.713 -20.543 1.00 48.89 ? 137 ASP A C 1 ATOM 974 O O . ASP A 1 121 ? 32.115 -8.007 -19.817 1.00 48.83 ? 137 ASP A O 1 ATOM 975 C CB . ASP A 1 121 ? 30.990 -10.436 -20.602 1.00 48.72 ? 137 ASP A CB 1 ATOM 976 C CG . ASP A 1 121 ? 30.190 -9.789 -21.731 1.00 50.47 ? 137 ASP A CG 1 ATOM 977 O OD1 . ASP A 1 121 ? 30.784 -9.088 -22.580 1.00 51.29 ? 137 ASP A OD1 1 ATOM 978 O OD2 . ASP A 1 121 ? 28.956 -9.991 -21.765 1.00 50.06 ? 137 ASP A OD2 1 ATOM 979 N N . SER A 1 122 ? 33.864 -8.240 -21.224 1.00 50.30 ? 138 SER A N 1 ATOM 980 C CA . SER A 1 122 ? 34.307 -6.844 -21.087 1.00 52.49 ? 138 SER A CA 1 ATOM 981 C C . SER A 1 122 ? 33.291 -5.810 -21.604 1.00 53.82 ? 138 SER A C 1 ATOM 982 O O . SER A 1 122 ? 33.519 -4.603 -21.497 1.00 54.60 ? 138 SER A O 1 ATOM 983 C CB . SER A 1 122 ? 35.692 -6.634 -21.716 1.00 53.18 ? 138 SER A CB 1 ATOM 984 O OG . SER A 1 122 ? 35.693 -6.967 -23.094 1.00 54.55 ? 138 SER A OG 1 ATOM 985 N N . THR A 1 123 ? 32.173 -6.296 -22.147 1.00 55.57 ? 139 THR A N 1 ATOM 986 C CA . THR A 1 123 ? 31.029 -5.459 -22.526 1.00 57.51 ? 139 THR A CA 1 ATOM 987 C C . THR A 1 123 ? 30.216 -5.075 -21.292 1.00 55.63 ? 139 THR A C 1 ATOM 988 O O . THR A 1 123 ? 29.748 -3.937 -21.173 1.00 56.04 ? 139 THR A O 1 ATOM 989 C CB . THR A 1 123 ? 30.087 -6.210 -23.493 1.00 58.47 ? 139 THR A CB 1 ATOM 990 O OG1 . THR A 1 123 ? 30.830 -6.654 -24.629 1.00 61.77 ? 139 THR A OG1 1 ATOM 991 C CG2 . THR A 1 123 ? 28.920 -5.331 -23.951 1.00 60.56 ? 139 THR A CG2 1 ATOM 992 N N . LYS A 1 124 ? 30.045 -6.040 -20.390 1.00 51.96 ? 140 LYS A N 1 ATOM 993 C CA . LYS A 1 124 ? 29.190 -5.890 -19.228 1.00 48.85 ? 140 LYS A CA 1 ATOM 994 C C . LYS A 1 124 ? 29.978 -5.234 -18.090 1.00 46.67 ? 140 LYS A C 1 ATOM 995 O O . LYS A 1 124 ? 30.780 -5.893 -17.420 1.00 44.08 ? 140 LYS A O 1 ATOM 996 C CB . LYS A 1 124 ? 28.651 -7.259 -18.816 1.00 50.04 ? 140 LYS A CB 1 ATOM 997 C CG . LYS A 1 124 ? 27.345 -7.211 -18.042 1.00 53.56 ? 140 LYS A CG 1 ATOM 998 C CD . LYS A 1 124 ? 27.079 -8.531 -17.329 1.00 55.80 ? 140 LYS A CD 1 ATOM 999 C CE . LYS A 1 124 ? 25.640 -8.632 -16.841 1.00 57.84 ? 140 LYS A CE 1 ATOM 1000 N NZ . LYS A 1 124 ? 25.263 -7.548 -15.889 1.00 58.75 ? 140 LYS A NZ 1 ATOM 1001 N N . CYS A 1 125 ? 29.752 -3.937 -17.884 1.00 44.41 ? 141 CYS A N 1 ATOM 1002 C CA . CYS A 1 125 ? 30.533 -3.161 -16.919 1.00 43.13 ? 141 CYS A CA 1 ATOM 1003 C C . CYS A 1 125 ? 29.693 -2.496 -15.825 1.00 41.03 ? 141 CYS A C 1 ATOM 1004 O O . CYS A 1 125 ? 29.974 -1.375 -15.406 1.00 40.32 ? 141 CYS A O 1 ATOM 1005 C CB . CYS A 1 125 ? 31.418 -2.143 -17.646 1.00 44.50 ? 141 CYS A CB 1 ATOM 1006 S SG . CYS A 1 125 ? 32.645 -2.910 -18.743 1.00 47.49 ? 141 CYS A SG 1 ATOM 1007 N N . ASP A 1 126 ? 28.685 -3.216 -15.346 1.00 39.71 ? 142 ASP A N 1 ATOM 1008 C CA . ASP A 1 126 ? 27.762 -2.692 -14.343 1.00 38.75 ? 142 ASP A CA 1 ATOM 1009 C C . ASP A 1 126 ? 27.706 -3.566 -13.084 1.00 36.20 ? 142 ASP A C 1 ATOM 1010 O O . ASP A 1 126 ? 26.680 -3.627 -12.408 1.00 34.77 ? 142 ASP A O 1 ATOM 1011 C CB . ASP A 1 126 ? 26.361 -2.532 -14.949 1.00 41.09 ? 142 ASP A CB 1 ATOM 1012 C CG . ASP A 1 126 ? 25.764 -3.858 -15.425 1.00 44.14 ? 142 ASP A CG 1 ATOM 1013 O OD1 . ASP A 1 126 ? 26.506 -4.868 -15.543 1.00 45.42 ? 142 ASP A OD1 1 ATOM 1014 O OD2 . ASP A 1 126 ? 24.541 -3.889 -15.688 1.00 46.04 ? 142 ASP A OD2 1 ATOM 1015 N N . LEU A 1 127 ? 28.808 -4.251 -12.782 1.00 34.21 ? 143 LEU A N 1 ATOM 1016 C CA . LEU A 1 127 ? 28.875 -5.098 -11.594 1.00 32.50 ? 143 LEU A CA 1 ATOM 1017 C C . LEU A 1 127 ? 29.260 -4.235 -10.389 1.00 31.05 ? 143 LEU A C 1 ATOM 1018 O O . LEU A 1 127 ? 30.320 -3.610 -10.388 1.00 30.36 ? 143 LEU A O 1 ATOM 1019 C CB . LEU A 1 127 ? 29.878 -6.245 -11.797 1.00 32.71 ? 143 LEU A CB 1 ATOM 1020 C CG . LEU A 1 127 ? 29.512 -7.432 -12.713 1.00 33.62 ? 143 LEU A CG 1 ATOM 1021 C CD1 . LEU A 1 127 ? 29.327 -7.024 -14.167 1.00 34.73 ? 143 LEU A CD1 1 ATOM 1022 C CD2 . LEU A 1 127 ? 30.566 -8.528 -12.619 1.00 33.63 ? 143 LEU A CD2 1 ATOM 1023 N N . ALA A 1 128 ? 28.387 -4.190 -9.382 1.00 29.97 ? 144 ALA A N 1 ATOM 1024 C CA . ALA A 1 128 ? 28.676 -3.476 -8.132 1.00 28.46 ? 144 ALA A CA 1 ATOM 1025 C C . ALA A 1 128 ? 29.202 -4.455 -7.074 1.00 27.57 ? 144 ALA A C 1 ATOM 1026 O O . ALA A 1 128 ? 28.980 -5.667 -7.176 1.00 26.80 ? 144 ALA A O 1 ATOM 1027 C CB . ALA A 1 128 ? 27.431 -2.756 -7.631 1.00 27.88 ? 144 ALA A CB 1 ATOM 1028 N N . LEU A 1 129 ? 29.899 -3.936 -6.066 1.00 26.74 ? 145 LEU A N 1 ATOM 1029 C CA . LEU A 1 129 ? 30.353 -4.776 -4.950 1.00 26.72 ? 145 LEU A CA 1 ATOM 1030 C C . LEU A 1 129 ? 29.185 -5.599 -4.408 1.00 27.63 ? 145 LEU A C 1 ATOM 1031 O O . LEU A 1 129 ? 29.281 -6.817 -4.278 1.00 27.73 ? 145 LEU A O 1 ATOM 1032 C CB . LEU A 1 129 ? 30.964 -3.928 -3.822 1.00 25.52 ? 145 LEU A CB 1 ATOM 1033 C CG . LEU A 1 129 ? 31.510 -4.642 -2.572 1.00 25.04 ? 145 LEU A CG 1 ATOM 1034 C CD1 . LEU A 1 129 ? 32.767 -5.452 -2.885 1.00 24.40 ? 145 LEU A CD1 1 ATOM 1035 C CD2 . LEU A 1 129 ? 31.805 -3.631 -1.467 1.00 24.49 ? 145 LEU A CD2 1 ATOM 1036 N N . ASP A 1 130 ? 28.086 -4.911 -4.103 1.00 28.16 ? 146 ASP A N 1 ATOM 1037 C CA . ASP A 1 130 ? 26.911 -5.532 -3.520 1.00 29.00 ? 146 ASP A CA 1 ATOM 1038 C C . ASP A 1 130 ? 25.767 -5.432 -4.529 1.00 29.17 ? 146 ASP A C 1 ATOM 1039 O O . ASP A 1 130 ? 25.238 -4.335 -4.744 1.00 29.02 ? 146 ASP A O 1 ATOM 1040 C CB . ASP A 1 130 ? 26.545 -4.818 -2.207 1.00 29.93 ? 146 ASP A CB 1 ATOM 1041 C CG . ASP A 1 130 ? 25.378 -5.475 -1.470 1.00 31.60 ? 146 ASP A CG 1 ATOM 1042 O OD1 . ASP A 1 130 ? 24.862 -6.517 -1.942 1.00 33.12 ? 146 ASP A OD1 1 ATOM 1043 O OD2 . ASP A 1 130 ? 24.968 -4.936 -0.412 1.00 30.45 ? 146 ASP A OD2 1 ATOM 1044 N N . PRO A 1 131 ? 25.352 -6.576 -5.119 1.00 28.96 ? 147 PRO A N 1 ATOM 1045 C CA . PRO A 1 131 ? 25.774 -7.943 -4.796 1.00 28.57 ? 147 PRO A CA 1 ATOM 1046 C C . PRO A 1 131 ? 26.787 -8.633 -5.728 1.00 28.64 ? 147 PRO A C 1 ATOM 1047 O O . PRO A 1 131 ? 27.330 -9.676 -5.352 1.00 27.87 ? 147 PRO A O 1 ATOM 1048 C CB . PRO A 1 131 ? 24.456 -8.708 -4.871 1.00 29.30 ? 147 PRO A CB 1 ATOM 1049 C CG . PRO A 1 131 ? 23.727 -8.039 -6.003 1.00 29.94 ? 147 PRO A CG 1 ATOM 1050 C CD . PRO A 1 131 ? 24.154 -6.581 -5.986 1.00 29.85 ? 147 PRO A CD 1 ATOM 1051 N N . GLU A 1 132 ? 27.017 -8.094 -6.927 1.00 28.71 ? 148 GLU A N 1 ATOM 1052 C CA . GLU A 1 132 ? 27.733 -8.846 -7.968 1.00 29.18 ? 148 GLU A CA 1 ATOM 1053 C C . GLU A 1 132 ? 29.147 -9.309 -7.593 1.00 28.71 ? 148 GLU A C 1 ATOM 1054 O O . GLU A 1 132 ? 29.460 -10.497 -7.704 1.00 28.48 ? 148 GLU A O 1 ATOM 1055 C CB . GLU A 1 132 ? 27.750 -8.086 -9.306 1.00 29.96 ? 148 GLU A CB 1 ATOM 1056 C CG . GLU A 1 132 ? 26.391 -7.978 -9.992 1.00 31.47 ? 148 GLU A CG 1 ATOM 1057 C CD . GLU A 1 132 ? 25.517 -6.866 -9.432 1.00 31.91 ? 148 GLU A CD 1 ATOM 1058 O OE1 . GLU A 1 132 ? 26.046 -5.877 -8.870 1.00 31.76 ? 148 GLU A OE1 1 ATOM 1059 O OE2 . GLU A 1 132 ? 24.284 -6.984 -9.553 1.00 33.41 ? 148 GLU A OE2 1 ATOM 1060 N N . ILE A 1 133 ? 29.995 -8.384 -7.144 1.00 28.13 ? 149 ILE A N 1 ATOM 1061 C CA . ILE A 1 133 ? 31.394 -8.721 -6.891 1.00 27.44 ? 149 ILE A CA 1 ATOM 1062 C C . ILE A 1 133 ? 31.514 -9.628 -5.664 1.00 27.52 ? 149 ILE A C 1 ATOM 1063 O O . ILE A 1 133 ? 32.243 -10.619 -5.688 1.00 26.47 ? 149 ILE A O 1 ATOM 1064 C CB . ILE A 1 133 ? 32.297 -7.471 -6.777 1.00 26.87 ? 149 ILE A CB 1 ATOM 1065 C CG1 . ILE A 1 133 ? 32.118 -6.559 -7.996 1.00 27.47 ? 149 ILE A CG1 1 ATOM 1066 C CG2 . ILE A 1 133 ? 33.762 -7.880 -6.659 1.00 27.03 ? 149 ILE A CG2 1 ATOM 1067 C CD1 . ILE A 1 133 ? 32.835 -5.226 -7.896 1.00 26.60 ? 149 ILE A CD1 1 ATOM 1068 N N . GLU A 1 134 ? 30.769 -9.308 -4.606 1.00 28.45 ? 150 GLU A N 1 ATOM 1069 C CA . GLU A 1 134 ? 30.783 -10.129 -3.393 1.00 28.65 ? 150 GLU A CA 1 ATOM 1070 C C . GLU A 1 134 ? 30.299 -11.555 -3.643 1.00 29.20 ? 150 GLU A C 1 ATOM 1071 O O . GLU A 1 134 ? 30.755 -12.490 -2.973 1.00 29.11 ? 150 GLU A O 1 ATOM 1072 C CB . GLU A 1 134 ? 29.992 -9.473 -2.265 1.00 29.88 ? 150 GLU A CB 1 ATOM 1073 C CG . GLU A 1 134 ? 30.766 -8.376 -1.546 1.00 30.68 ? 150 GLU A CG 1 ATOM 1074 C CD . GLU A 1 134 ? 30.198 -8.045 -0.179 1.00 31.73 ? 150 GLU A CD 1 ATOM 1075 O OE1 . GLU A 1 134 ? 28.966 -8.151 -0.001 1.00 32.02 ? 150 GLU A OE1 1 ATOM 1076 O OE2 . GLU A 1 134 ? 30.988 -7.683 0.726 1.00 32.59 ? 150 GLU A OE2 1 ATOM 1077 N N . GLU A 1 135 ? 29.396 -11.717 -4.612 1.00 29.45 ? 151 GLU A N 1 ATOM 1078 C CA . GLU A 1 135 ? 28.942 -13.039 -5.041 1.00 30.41 ? 151 GLU A CA 1 ATOM 1079 C C . GLU A 1 135 ? 30.117 -13.890 -5.559 1.00 29.67 ? 151 GLU A C 1 ATOM 1080 O O . GLU A 1 135 ? 30.286 -15.030 -5.129 1.00 30.08 ? 151 GLU A O 1 ATOM 1081 C CB . GLU A 1 135 ? 27.832 -12.922 -6.100 1.00 31.61 ? 151 GLU A CB 1 ATOM 1082 C CG . GLU A 1 135 ? 27.375 -14.234 -6.722 0.50 32.92 ? 151 GLU A CG 1 ATOM 1083 C CD . GLU A 1 135 ? 26.287 -14.936 -5.929 0.50 33.94 ? 151 GLU A CD 1 ATOM 1084 O OE1 . GLU A 1 135 ? 26.242 -14.787 -4.689 0.50 34.89 ? 151 GLU A OE1 1 ATOM 1085 O OE2 . GLU A 1 135 ? 25.474 -15.652 -6.551 0.50 34.84 ? 151 GLU A OE2 1 ATOM 1086 N N . VAL A 1 136 ? 30.925 -13.331 -6.463 1.00 29.06 ? 152 VAL A N 1 ATOM 1087 C CA . VAL A 1 136 ? 32.110 -14.032 -6.988 1.00 28.57 ? 152 VAL A CA 1 ATOM 1088 C C . VAL A 1 136 ? 33.133 -14.344 -5.885 1.00 28.68 ? 152 VAL A C 1 ATOM 1089 O O . VAL A 1 136 ? 33.571 -15.491 -5.738 1.00 28.64 ? 152 VAL A O 1 ATOM 1090 C CB . VAL A 1 136 ? 32.784 -13.250 -8.135 1.00 29.03 ? 152 VAL A CB 1 ATOM 1091 C CG1 . VAL A 1 136 ? 34.001 -14.007 -8.658 1.00 29.09 ? 152 VAL A CG1 1 ATOM 1092 C CG2 . VAL A 1 136 ? 31.793 -13.002 -9.265 1.00 28.88 ? 152 VAL A CG2 1 ATOM 1093 N N . ILE A 1 137 ? 33.493 -13.327 -5.103 1.00 27.67 ? 153 ILE A N 1 ATOM 1094 C CA . ILE A 1 137 ? 34.499 -13.467 -4.050 1.00 27.82 ? 153 ILE A CA 1 ATOM 1095 C C . ILE A 1 137 ? 34.149 -14.571 -3.045 1.00 27.55 ? 153 ILE A C 1 ATOM 1096 O O . ILE A 1 137 ? 35.027 -15.316 -2.596 1.00 26.80 ? 153 ILE A O 1 ATOM 1097 C CB . ILE A 1 137 ? 34.754 -12.116 -3.338 1.00 28.22 ? 153 ILE A CB 1 ATOM 1098 C CG1 . ILE A 1 137 ? 35.311 -11.090 -4.332 1.00 28.14 ? 153 ILE A CG1 1 ATOM 1099 C CG2 . ILE A 1 137 ? 35.737 -12.273 -2.190 1.00 27.61 ? 153 ILE A CG2 1 ATOM 1100 C CD1 . ILE A 1 137 ? 36.731 -11.364 -4.799 1.00 27.88 ? 153 ILE A CD1 1 ATOM 1101 N N . SER A 1 138 ? 32.864 -14.705 -2.727 1.00 27.76 ? 154 SER A N 1 ATOM 1102 C CA . SER A 1 138 ? 32.428 -15.710 -1.754 1.00 29.04 ? 154 SER A CA 1 ATOM 1103 C C . SER A 1 138 ? 32.242 -17.118 -2.347 1.00 29.55 ? 154 SER A C 1 ATOM 1104 O O . SER A 1 138 ? 32.302 -18.101 -1.618 1.00 29.09 ? 154 SER A O 1 ATOM 1105 C CB . SER A 1 138 ? 31.141 -15.255 -1.061 1.00 29.57 ? 154 SER A CB 1 ATOM 1106 O OG . SER A 1 138 ? 30.111 -15.080 -2.014 1.00 32.50 ? 154 SER A OG 1 ATOM 1107 N N . LYS A 1 139 ? 32.026 -17.212 -3.659 1.00 30.50 ? 155 LYS A N 1 ATOM 1108 C CA . LYS A 1 139 ? 31.652 -18.488 -4.288 1.00 31.65 ? 155 LYS A CA 1 ATOM 1109 C C . LYS A 1 139 ? 32.670 -19.086 -5.272 1.00 31.12 ? 155 LYS A C 1 ATOM 1110 O O . LYS A 1 139 ? 32.808 -20.301 -5.342 1.00 30.95 ? 155 LYS A O 1 ATOM 1111 C CB . LYS A 1 139 ? 30.288 -18.373 -4.969 1.00 33.77 ? 155 LYS A CB 1 ATOM 1112 C CG . LYS A 1 139 ? 29.136 -18.195 -3.992 1.00 36.84 ? 155 LYS A CG 1 ATOM 1113 C CD . LYS A 1 139 ? 27.786 -18.148 -4.695 1.00 40.32 ? 155 LYS A CD 1 ATOM 1114 C CE . LYS A 1 139 ? 26.672 -17.966 -3.672 1.00 42.02 ? 155 LYS A CE 1 ATOM 1115 N NZ . LYS A 1 139 ? 25.330 -18.301 -4.222 1.00 45.84 ? 155 LYS A NZ 1 ATOM 1116 N N . SER A 1 140 ? 33.366 -18.245 -6.031 1.00 30.71 ? 156 SER A N 1 ATOM 1117 C CA . SER A 1 140 ? 34.329 -18.734 -7.019 1.00 30.88 ? 156 SER A CA 1 ATOM 1118 C C . SER A 1 140 ? 35.514 -19.417 -6.348 1.00 30.36 ? 156 SER A C 1 ATOM 1119 O O . SER A 1 140 ? 35.978 -18.979 -5.287 1.00 28.76 ? 156 SER A O 1 ATOM 1120 C CB . SER A 1 140 ? 34.818 -17.596 -7.920 1.00 31.46 ? 156 SER A CB 1 ATOM 1121 O OG . SER A 1 140 ? 35.810 -18.045 -8.838 1.00 31.98 ? 156 SER A OG 1 ATOM 1122 N N . ARG A 1 141 ? 35.980 -20.508 -6.949 1.00 30.66 ? 157 ARG A N 1 ATOM 1123 C CA . ARG A 1 141 ? 37.242 -21.132 -6.524 1.00 31.50 ? 157 ARG A CA 1 ATOM 1124 C C . ARG A 1 141 ? 38.242 -21.118 -7.687 1.00 31.14 ? 157 ARG A C 1 ATOM 1125 O O . ARG A 1 141 ? 39.145 -21.952 -7.766 1.00 32.07 ? 157 ARG A O 1 ATOM 1126 C CB . ARG A 1 141 ? 37.036 -22.558 -5.985 1.00 32.47 ? 157 ARG A CB 1 ATOM 1127 C CG . ARG A 1 141 ? 35.875 -22.760 -5.012 1.00 34.22 ? 157 ARG A CG 1 ATOM 1128 C CD . ARG A 1 141 ? 36.066 -22.026 -3.695 1.00 35.20 ? 157 ARG A CD 1 ATOM 1129 N NE . ARG A 1 141 ? 35.118 -22.464 -2.668 1.00 36.24 ? 157 ARG A NE 1 ATOM 1130 C CZ . ARG A 1 141 ? 34.511 -21.658 -1.798 1.00 37.29 ? 157 ARG A CZ 1 ATOM 1131 N NH1 . ARG A 1 141 ? 34.702 -20.330 -1.823 1.00 37.25 ? 157 ARG A NH1 1 ATOM 1132 N NH2 . ARG A 1 141 ? 33.686 -22.182 -0.902 1.00 36.47 ? 157 ARG A NH2 1 ATOM 1133 N N . ASP A 1 142 ? 38.061 -20.162 -8.591 1.00 31.25 ? 158 ASP A N 1 ATOM 1134 C CA . ASP A 1 142 ? 38.989 -19.923 -9.684 1.00 31.59 ? 158 ASP A CA 1 ATOM 1135 C C . ASP A 1 142 ? 39.922 -18.790 -9.242 1.00 30.18 ? 158 ASP A C 1 ATOM 1136 O O . ASP A 1 142 ? 39.542 -17.615 -9.268 1.00 29.09 ? 158 ASP A O 1 ATOM 1137 C CB . ASP A 1 142 ? 38.214 -19.561 -10.958 1.00 33.05 ? 158 ASP A CB 1 ATOM 1138 C CG . ASP A 1 142 ? 39.122 -19.212 -12.140 1.00 35.66 ? 158 ASP A CG 1 ATOM 1139 O OD1 . ASP A 1 142 ? 40.149 -18.525 -11.970 1.00 36.31 ? 158 ASP A OD1 1 ATOM 1140 O OD2 . ASP A 1 142 ? 38.784 -19.600 -13.273 1.00 37.01 ? 158 ASP A OD2 1 ATOM 1141 N N . HIS A 1 143 ? 41.139 -19.151 -8.836 1.00 28.64 ? 159 HIS A N 1 ATOM 1142 C CA . HIS A 1 143 ? 42.053 -18.182 -8.232 1.00 28.15 ? 159 HIS A CA 1 ATOM 1143 C C . HIS A 1 143 ? 42.384 -16.973 -9.122 1.00 27.93 ? 159 HIS A C 1 ATOM 1144 O O . HIS A 1 143 ? 42.587 -15.873 -8.615 1.00 28.07 ? 159 HIS A O 1 ATOM 1145 C CB . HIS A 1 143 ? 43.319 -18.862 -7.703 1.00 28.16 ? 159 HIS A CB 1 ATOM 1146 C CG . HIS A 1 143 ? 44.090 -19.597 -8.746 1.00 28.53 ? 159 HIS A CG 1 ATOM 1147 N ND1 . HIS A 1 143 ? 45.209 -19.067 -9.352 1.00 28.90 ? 159 HIS A ND1 1 ATOM 1148 C CD2 . HIS A 1 143 ? 43.906 -20.823 -9.293 1.00 28.73 ? 159 HIS A CD2 1 ATOM 1149 C CE1 . HIS A 1 143 ? 45.680 -19.934 -10.231 1.00 28.72 ? 159 HIS A CE1 1 ATOM 1150 N NE2 . HIS A 1 143 ? 44.908 -21.007 -10.213 1.00 28.92 ? 159 HIS A NE2 1 ATOM 1151 N N . GLU A 1 144 ? 42.405 -17.158 -10.437 1.00 27.28 ? 160 GLU A N 1 ATOM 1152 C CA . GLU A 1 144 ? 42.677 -16.030 -11.326 1.00 27.07 ? 160 GLU A CA 1 ATOM 1153 C C . GLU A 1 144 ? 41.468 -15.112 -11.460 1.00 25.33 ? 160 GLU A C 1 ATOM 1154 O O . GLU A 1 144 ? 41.627 -13.907 -11.592 1.00 24.79 ? 160 GLU A O 1 ATOM 1155 C CB . GLU A 1 144 ? 43.222 -16.492 -12.681 1.00 29.59 ? 160 GLU A CB 1 ATOM 1156 C CG . GLU A 1 144 ? 44.592 -17.143 -12.535 1.00 32.18 ? 160 GLU A CG 1 ATOM 1157 C CD . GLU A 1 144 ? 45.442 -17.117 -13.787 1.00 35.27 ? 160 GLU A CD 1 ATOM 1158 O OE1 . GLU A 1 144 ? 44.905 -16.963 -14.909 1.00 37.97 ? 160 GLU A OE1 1 ATOM 1159 O OE2 . GLU A 1 144 ? 46.673 -17.263 -13.646 1.00 37.02 ? 160 GLU A OE2 1 ATOM 1160 N N . GLU A 1 145 ? 40.267 -15.681 -11.394 1.00 24.20 ? 161 GLU A N 1 ATOM 1161 C CA . GLU A 1 145 ? 39.052 -14.881 -11.467 1.00 24.46 ? 161 GLU A CA 1 ATOM 1162 C C . GLU A 1 145 ? 38.968 -14.001 -10.228 1.00 23.89 ? 161 GLU A C 1 ATOM 1163 O O . GLU A 1 145 ? 38.664 -12.809 -10.315 1.00 23.86 ? 161 GLU A O 1 ATOM 1164 C CB . GLU A 1 145 ? 37.814 -15.764 -11.584 1.00 25.26 ? 161 GLU A CB 1 ATOM 1165 C CG . GLU A 1 145 ? 36.501 -14.985 -11.579 1.00 26.55 ? 161 GLU A CG 1 ATOM 1166 C CD . GLU A 1 145 ? 35.282 -15.876 -11.725 1.00 28.00 ? 161 GLU A CD 1 ATOM 1167 O OE1 . GLU A 1 145 ? 35.274 -16.998 -11.168 1.00 28.14 ? 161 GLU A OE1 1 ATOM 1168 O OE2 . GLU A 1 145 ? 34.324 -15.448 -12.405 1.00 29.12 ? 161 GLU A OE2 1 ATOM 1169 N N . LEU A 1 146 ? 39.253 -14.617 -9.090 1.00 23.10 ? 162 LEU A N 1 ATOM 1170 C CA . LEU A 1 146 ? 39.278 -13.935 -7.790 1.00 23.08 ? 162 LEU A CA 1 ATOM 1171 C C . LEU A 1 146 ? 40.279 -12.763 -7.764 1.00 23.29 ? 162 LEU A C 1 ATOM 1172 O O . LEU A 1 146 ? 39.953 -11.669 -7.273 1.00 23.65 ? 162 LEU A O 1 ATOM 1173 C CB . LEU A 1 146 ? 39.590 -14.954 -6.690 1.00 22.16 ? 162 LEU A CB 1 ATOM 1174 C CG . LEU A 1 146 ? 38.476 -15.972 -6.362 1.00 22.08 ? 162 LEU A CG 1 ATOM 1175 C CD1 . LEU A 1 146 ? 39.007 -17.150 -5.556 1.00 21.14 ? 162 LEU A CD1 1 ATOM 1176 C CD2 . LEU A 1 146 ? 37.289 -15.323 -5.648 1.00 21.21 ? 162 LEU A CD2 1 ATOM 1177 N N . ALA A 1 147 ? 41.476 -12.988 -8.309 1.00 22.96 ? 163 ALA A N 1 ATOM 1178 C CA . ALA A 1 147 ? 42.529 -11.965 -8.354 1.00 22.71 ? 163 ALA A CA 1 ATOM 1179 C C . ALA A 1 147 ? 42.127 -10.801 -9.255 1.00 23.57 ? 163 ALA A C 1 ATOM 1180 O O . ALA A 1 147 ? 42.431 -9.648 -8.951 1.00 23.40 ? 163 ALA A O 1 ATOM 1181 C CB . ALA A 1 147 ? 43.857 -12.567 -8.802 1.00 22.38 ? 163 ALA A CB 1 ATOM 1182 N N . TYR A 1 148 ? 41.454 -11.111 -10.367 1.00 24.00 ? 164 TYR A N 1 ATOM 1183 C CA . TYR A 1 148 ? 40.913 -10.085 -11.252 1.00 24.67 ? 164 TYR A CA 1 ATOM 1184 C C . TYR A 1 148 ? 39.975 -9.115 -10.504 1.00 23.95 ? 164 TYR A C 1 ATOM 1185 O O . TYR A 1 148 ? 40.165 -7.898 -10.545 1.00 23.72 ? 164 TYR A O 1 ATOM 1186 C CB . TYR A 1 148 ? 40.199 -10.716 -12.463 1.00 25.41 ? 164 TYR A CB 1 ATOM 1187 C CG . TYR A 1 148 ? 39.399 -9.711 -13.269 1.00 26.44 ? 164 TYR A CG 1 ATOM 1188 C CD1 . TYR A 1 148 ? 40.020 -8.891 -14.221 1.00 27.11 ? 164 TYR A CD1 1 ATOM 1189 C CD2 . TYR A 1 148 ? 38.024 -9.564 -13.066 1.00 26.58 ? 164 TYR A CD2 1 ATOM 1190 C CE1 . TYR A 1 148 ? 39.289 -7.955 -14.940 1.00 27.62 ? 164 TYR A CE1 1 ATOM 1191 C CE2 . TYR A 1 148 ? 37.288 -8.634 -13.777 1.00 27.10 ? 164 TYR A CE2 1 ATOM 1192 C CZ . TYR A 1 148 ? 37.922 -7.836 -14.713 1.00 27.86 ? 164 TYR A CZ 1 ATOM 1193 O OH . TYR A 1 148 ? 37.185 -6.910 -15.418 1.00 28.41 ? 164 TYR A OH 1 ATOM 1194 N N . TYR A 1 149 ? 38.978 -9.662 -9.815 1.00 23.77 ? 165 TYR A N 1 ATOM 1195 C CA . TYR A 1 149 ? 37.971 -8.844 -9.139 1.00 23.25 ? 165 TYR A CA 1 ATOM 1196 C C . TYR A 1 149 ? 38.573 -8.085 -7.961 1.00 22.50 ? 165 TYR A C 1 ATOM 1197 O O . TYR A 1 149 ? 38.179 -6.947 -7.671 1.00 21.51 ? 165 TYR A O 1 ATOM 1198 C CB . TYR A 1 149 ? 36.777 -9.700 -8.704 1.00 23.45 ? 165 TYR A CB 1 ATOM 1199 C CG . TYR A 1 149 ? 35.839 -10.033 -9.857 1.00 24.28 ? 165 TYR A CG 1 ATOM 1200 C CD1 . TYR A 1 149 ? 35.069 -9.039 -10.458 1.00 24.89 ? 165 TYR A CD1 1 ATOM 1201 C CD2 . TYR A 1 149 ? 35.730 -11.341 -10.349 1.00 24.89 ? 165 TYR A CD2 1 ATOM 1202 C CE1 . TYR A 1 149 ? 34.222 -9.324 -11.521 1.00 25.63 ? 165 TYR A CE1 1 ATOM 1203 C CE2 . TYR A 1 149 ? 34.879 -11.640 -11.413 1.00 25.25 ? 165 TYR A CE2 1 ATOM 1204 C CZ . TYR A 1 149 ? 34.124 -10.622 -11.987 1.00 25.78 ? 165 TYR A CZ 1 ATOM 1205 O OH . TYR A 1 149 ? 33.273 -10.877 -13.038 1.00 25.96 ? 165 TYR A OH 1 ATOM 1206 N N . TRP A 1 150 ? 39.535 -8.717 -7.301 1.00 22.62 ? 166 TRP A N 1 ATOM 1207 C CA . TRP A 1 150 ? 40.261 -8.070 -6.211 1.00 22.07 ? 166 TRP A CA 1 ATOM 1208 C C . TRP A 1 150 ? 40.950 -6.804 -6.736 1.00 22.89 ? 166 TRP A C 1 ATOM 1209 O O . TRP A 1 150 ? 40.799 -5.726 -6.161 1.00 22.80 ? 166 TRP A O 1 ATOM 1210 C CB . TRP A 1 150 ? 41.290 -9.030 -5.589 1.00 21.78 ? 166 TRP A CB 1 ATOM 1211 C CG . TRP A 1 150 ? 41.929 -8.479 -4.341 1.00 20.65 ? 166 TRP A CG 1 ATOM 1212 C CD1 . TRP A 1 150 ? 41.613 -8.799 -3.052 1.00 20.69 ? 166 TRP A CD1 1 ATOM 1213 C CD2 . TRP A 1 150 ? 42.985 -7.507 -4.268 1.00 20.51 ? 166 TRP A CD2 1 ATOM 1214 N NE1 . TRP A 1 150 ? 42.401 -8.086 -2.180 1.00 20.20 ? 166 TRP A NE1 1 ATOM 1215 C CE2 . TRP A 1 150 ? 43.257 -7.292 -2.900 1.00 20.05 ? 166 TRP A CE2 1 ATOM 1216 C CE3 . TRP A 1 150 ? 43.738 -6.811 -5.225 1.00 20.09 ? 166 TRP A CE3 1 ATOM 1217 C CZ2 . TRP A 1 150 ? 44.244 -6.392 -2.458 1.00 19.99 ? 166 TRP A CZ2 1 ATOM 1218 C CZ3 . TRP A 1 150 ? 44.718 -5.912 -4.798 1.00 20.00 ? 166 TRP A CZ3 1 ATOM 1219 C CH2 . TRP A 1 150 ? 44.958 -5.707 -3.410 1.00 19.87 ? 166 TRP A CH2 1 ATOM 1220 N N . ARG A 1 151 ? 41.677 -6.932 -7.847 1.00 23.72 ? 167 ARG A N 1 ATOM 1221 C CA . ARG A 1 151 ? 42.447 -5.805 -8.372 1.00 25.35 ? 167 ARG A CA 1 ATOM 1222 C C . ARG A 1 151 ? 41.533 -4.694 -8.898 1.00 25.31 ? 167 ARG A C 1 ATOM 1223 O O . ARG A 1 151 ? 41.811 -3.510 -8.698 1.00 24.33 ? 167 ARG A O 1 ATOM 1224 C CB . ARG A 1 151 ? 43.448 -6.254 -9.447 1.00 26.86 ? 167 ARG A CB 1 ATOM 1225 C CG . ARG A 1 151 ? 44.420 -5.169 -9.887 1.00 29.36 ? 167 ARG A CG 1 ATOM 1226 C CD . ARG A 1 151 ? 44.972 -5.417 -11.294 1.00 31.88 ? 167 ARG A CD 1 ATOM 1227 N NE . ARG A 1 151 ? 46.178 -6.250 -11.324 1.00 34.67 ? 167 ARG A NE 1 ATOM 1228 C CZ . ARG A 1 151 ? 47.413 -5.838 -11.000 1.00 37.01 ? 167 ARG A CZ 1 ATOM 1229 N NH1 . ARG A 1 151 ? 47.635 -4.592 -10.587 1.00 38.72 ? 167 ARG A NH1 1 ATOM 1230 N NH2 . ARG A 1 151 ? 48.444 -6.676 -11.077 1.00 36.26 ? 167 ARG A NH2 1 ATOM 1231 N N . GLU A 1 152 ? 40.445 -5.077 -9.560 1.00 26.07 ? 168 GLU A N 1 ATOM 1232 C CA . GLU A 1 152 ? 39.525 -4.089 -10.132 1.00 26.88 ? 168 GLU A CA 1 ATOM 1233 C C . GLU A 1 152 ? 38.881 -3.277 -9.023 1.00 25.66 ? 168 GLU A C 1 ATOM 1234 O O . GLU A 1 152 ? 38.853 -2.045 -9.083 1.00 25.49 ? 168 GLU A O 1 ATOM 1235 C CB . GLU A 1 152 ? 38.463 -4.754 -11.022 1.00 27.92 ? 168 GLU A CB 1 ATOM 1236 C CG . GLU A 1 152 ? 39.018 -5.320 -12.326 1.00 29.94 ? 168 GLU A CG 1 ATOM 1237 C CD . GLU A 1 152 ? 39.738 -4.266 -13.154 1.00 31.32 ? 168 GLU A CD 1 ATOM 1238 O OE1 . GLU A 1 152 ? 39.063 -3.338 -13.637 1.00 32.78 ? 168 GLU A OE1 1 ATOM 1239 O OE2 . GLU A 1 152 ? 40.979 -4.346 -13.300 1.00 31.55 ? 168 GLU A OE2 1 ATOM 1240 N N . PHE A 1 153 ? 38.392 -3.971 -7.999 1.00 24.69 ? 169 PHE A N 1 ATOM 1241 C CA . PHE A 1 153 ? 37.754 -3.300 -6.878 1.00 24.06 ? 169 PHE A CA 1 ATOM 1242 C C . PHE A 1 153 ? 38.708 -2.369 -6.125 1.00 23.69 ? 169 PHE A C 1 ATOM 1243 O O . PHE A 1 153 ? 38.395 -1.183 -5.920 1.00 24.03 ? 169 PHE A O 1 ATOM 1244 C CB . PHE A 1 153 ? 37.072 -4.282 -5.914 1.00 23.43 ? 169 PHE A CB 1 ATOM 1245 C CG . PHE A 1 153 ? 36.318 -3.586 -4.820 1.00 23.14 ? 169 PHE A CG 1 ATOM 1246 C CD1 . PHE A 1 153 ? 35.131 -2.905 -5.101 1.00 23.34 ? 169 PHE A CD1 1 ATOM 1247 C CD2 . PHE A 1 153 ? 36.826 -3.540 -3.528 1.00 23.14 ? 169 PHE A CD2 1 ATOM 1248 C CE1 . PHE A 1 153 ? 34.447 -2.223 -4.112 1.00 23.61 ? 169 PHE A CE1 1 ATOM 1249 C CE2 . PHE A 1 153 ? 36.136 -2.861 -2.532 1.00 23.10 ? 169 PHE A CE2 1 ATOM 1250 C CZ . PHE A 1 153 ? 34.952 -2.203 -2.824 1.00 22.94 ? 169 PHE A CZ 1 ATOM 1251 N N . TYR A 1 154 ? 39.865 -2.889 -5.714 1.00 22.66 ? 170 TYR A N 1 ATOM 1252 C CA . TYR A 1 154 ? 40.824 -2.071 -4.981 1.00 22.12 ? 170 TYR A CA 1 ATOM 1253 C C . TYR A 1 154 ? 41.324 -0.871 -5.781 1.00 22.20 ? 170 TYR A C 1 ATOM 1254 O O . TYR A 1 154 ? 41.488 0.207 -5.228 1.00 22.28 ? 170 TYR A O 1 ATOM 1255 C CB . TYR A 1 154 ? 41.998 -2.903 -4.451 1.00 21.23 ? 170 TYR A CB 1 ATOM 1256 C CG . TYR A 1 154 ? 41.710 -3.629 -3.146 1.00 20.89 ? 170 TYR A CG 1 ATOM 1257 C CD1 . TYR A 1 154 ? 40.914 -4.778 -3.117 1.00 20.73 ? 170 TYR A CD1 1 ATOM 1258 C CD2 . TYR A 1 154 ? 42.255 -3.174 -1.940 1.00 20.54 ? 170 TYR A CD2 1 ATOM 1259 C CE1 . TYR A 1 154 ? 40.660 -5.453 -1.927 1.00 20.39 ? 170 TYR A CE1 1 ATOM 1260 C CE2 . TYR A 1 154 ? 42.014 -3.845 -0.750 1.00 20.29 ? 170 TYR A CE2 1 ATOM 1261 C CZ . TYR A 1 154 ? 41.218 -4.988 -0.751 1.00 20.57 ? 170 TYR A CZ 1 ATOM 1262 O OH . TYR A 1 154 ? 40.970 -5.672 0.430 1.00 20.09 ? 170 TYR A OH 1 ATOM 1263 N N . ASP A 1 155 ? 41.552 -1.021 -7.088 1.00 22.54 ? 171 ASP A N 1 ATOM 1264 C CA . ASP A 1 155 ? 41.980 0.144 -7.862 1.00 22.91 ? 171 ASP A CA 1 ATOM 1265 C C . ASP A 1 155 ? 40.915 1.256 -7.830 1.00 22.95 ? 171 ASP A C 1 ATOM 1266 O O . ASP A 1 155 ? 41.248 2.440 -7.783 1.00 22.87 ? 171 ASP A O 1 ATOM 1267 C CB . ASP A 1 155 ? 42.334 -0.242 -9.323 1.00 23.86 ? 171 ASP A CB 1 ATOM 1268 C CG . ASP A 1 155 ? 43.616 -1.092 -9.427 1.00 24.69 ? 171 ASP A CG 1 ATOM 1269 O OD1 . ASP A 1 155 ? 44.364 -1.253 -8.428 1.00 24.46 ? 171 ASP A OD1 1 ATOM 1270 O OD2 . ASP A 1 155 ? 43.886 -1.612 -10.534 1.00 25.16 ? 171 ASP A OD2 1 ATOM 1271 N N . LYS A 1 156 ? 39.638 0.872 -7.833 1.00 23.44 ? 172 LYS A N 1 ATOM 1272 C CA . LYS A 1 156 ? 38.535 1.842 -7.971 1.00 24.35 ? 172 LYS A CA 1 ATOM 1273 C C . LYS A 1 156 ? 38.020 2.420 -6.647 1.00 23.97 ? 172 LYS A C 1 ATOM 1274 O O . LYS A 1 156 ? 37.675 3.603 -6.567 1.00 24.07 ? 172 LYS A O 1 ATOM 1275 C CB . LYS A 1 156 ? 37.373 1.211 -8.728 1.00 25.71 ? 172 LYS A CB 1 ATOM 1276 C CG . LYS A 1 156 ? 37.596 1.100 -10.230 1.00 27.18 ? 172 LYS A CG 1 ATOM 1277 C CD . LYS A 1 156 ? 36.539 0.196 -10.839 1.00 29.34 ? 172 LYS A CD 1 ATOM 1278 C CE . LYS A 1 156 ? 36.409 0.398 -12.343 1.00 31.21 ? 172 LYS A CE 1 ATOM 1279 N NZ . LYS A 1 156 ? 37.567 -0.190 -13.058 1.00 32.80 ? 172 LYS A NZ 1 ATOM 1280 N N . ALA A 1 157 ? 37.941 1.572 -5.632 1.00 23.18 ? 173 ALA A N 1 ATOM 1281 C CA . ALA A 1 157 ? 37.449 1.981 -4.312 1.00 22.61 ? 173 ALA A CA 1 ATOM 1282 C C . ALA A 1 157 ? 38.569 2.553 -3.445 1.00 22.58 ? 173 ALA A C 1 ATOM 1283 O O . ALA A 1 157 ? 38.318 3.351 -2.522 1.00 22.91 ? 173 ALA A O 1 ATOM 1284 C CB . ALA A 1 157 ? 36.781 0.801 -3.620 1.00 22.32 ? 173 ALA A CB 1 ATOM 1285 N N . GLY A 1 158 ? 39.798 2.119 -3.708 1.00 21.94 ? 174 GLY A N 1 ATOM 1286 C CA . GLY A 1 158 ? 40.943 2.575 -2.943 1.00 21.92 ? 174 GLY A CA 1 ATOM 1287 C C . GLY A 1 158 ? 41.742 3.678 -3.593 1.00 22.51 ? 174 GLY A C 1 ATOM 1288 O O . GLY A 1 158 ? 41.640 4.847 -3.217 1.00 22.40 ? 174 GLY A O 1 ATOM 1289 N N . THR A 1 159 ? 42.556 3.306 -4.576 1.00 23.19 ? 175 THR A N 1 ATOM 1290 C CA . THR A 1 159 ? 43.517 4.239 -5.164 1.00 23.57 ? 175 THR A CA 1 ATOM 1291 C C . THR A 1 159 ? 42.869 5.552 -5.628 1.00 24.53 ? 175 THR A C 1 ATOM 1292 O O . THR A 1 159 ? 43.466 6.629 -5.498 1.00 24.76 ? 175 THR A O 1 ATOM 1293 C CB . THR A 1 159 ? 44.311 3.575 -6.310 1.00 23.34 ? 175 THR A CB 1 ATOM 1294 O OG1 . THR A 1 159 ? 44.902 2.355 -5.834 1.00 22.72 ? 175 THR A OG1 1 ATOM 1295 C CG2 . THR A 1 159 ? 45.424 4.518 -6.820 1.00 23.38 ? 175 THR A CG2 1 ATOM 1296 N N . ALA A 1 160 ? 41.638 5.452 -6.124 1.00 25.49 ? 176 ALA A N 1 ATOM 1297 C CA . ALA A 1 160 ? 40.939 6.584 -6.735 1.00 26.26 ? 176 ALA A CA 1 ATOM 1298 C C . ALA A 1 160 ? 40.714 7.753 -5.782 1.00 25.92 ? 176 ALA A C 1 ATOM 1299 O O . ALA A 1 160 ? 40.506 8.877 -6.227 1.00 25.68 ? 176 ALA A O 1 ATOM 1300 C CB . ALA A 1 160 ? 39.615 6.130 -7.343 1.00 26.09 ? 176 ALA A CB 1 ATOM 1301 N N . VAL A 1 161 ? 40.766 7.508 -4.472 1.00 25.55 ? 177 VAL A N 1 ATOM 1302 C CA . VAL A 1 161 ? 40.503 8.585 -3.521 1.00 26.12 ? 177 VAL A CA 1 ATOM 1303 C C . VAL A 1 161 ? 41.674 9.024 -2.621 1.00 26.36 ? 177 VAL A C 1 ATOM 1304 O O . VAL A 1 161 ? 41.440 9.665 -1.599 1.00 26.41 ? 177 VAL A O 1 ATOM 1305 C CB . VAL A 1 161 ? 39.249 8.310 -2.643 1.00 25.61 ? 177 VAL A CB 1 ATOM 1306 C CG1 . VAL A 1 161 ? 37.995 8.268 -3.500 1.00 25.61 ? 177 VAL A CG1 1 ATOM 1307 C CG2 . VAL A 1 161 ? 39.394 7.022 -1.835 1.00 24.82 ? 177 VAL A CG2 1 ATOM 1308 N N A ARG A 1 162 ? 42.908 8.701 -3.007 0.50 26.79 ? 178 ARG A N 1 ATOM 1309 N N B ARG A 1 162 ? 42.906 8.692 -3.021 0.50 26.37 ? 178 ARG A N 1 ATOM 1310 C CA A ARG A 1 162 ? 44.070 9.054 -2.188 0.50 27.05 ? 178 ARG A CA 1 ATOM 1311 C CA B ARG A 1 162 ? 44.122 9.044 -2.264 0.50 26.27 ? 178 ARG A CA 1 ATOM 1312 C C A ARG A 1 162 ? 44.137 10.538 -1.813 0.50 27.13 ? 178 ARG A C 1 ATOM 1313 C C B ARG A 1 162 ? 44.190 10.517 -1.843 0.50 26.68 ? 178 ARG A C 1 ATOM 1314 O O A ARG A 1 162 ? 44.307 10.870 -0.638 0.50 25.96 ? 178 ARG A O 1 ATOM 1315 O O B ARG A 1 162 ? 44.402 10.819 -0.667 0.50 25.61 ? 178 ARG A O 1 ATOM 1316 C CB A ARG A 1 162 ? 45.388 8.632 -2.838 0.50 27.79 ? 178 ARG A CB 1 ATOM 1317 C CB B ARG A 1 162 ? 45.390 8.657 -3.045 0.50 26.35 ? 178 ARG A CB 1 ATOM 1318 C CG A ARG A 1 162 ? 46.592 9.059 -2.010 0.50 28.19 ? 178 ARG A CG 1 ATOM 1319 C CG B ARG A 1 162 ? 46.694 9.226 -2.480 0.50 25.94 ? 178 ARG A CG 1 ATOM 1320 C CD A ARG A 1 162 ? 47.875 9.084 -2.821 0.50 28.41 ? 178 ARG A CD 1 ATOM 1321 C CD B ARG A 1 162 ? 47.055 8.623 -1.126 0.50 25.10 ? 178 ARG A CD 1 ATOM 1322 N NE A ARG A 1 162 ? 48.317 7.744 -3.181 0.50 28.95 ? 178 ARG A NE 1 ATOM 1323 N NE B ARG A 1 162 ? 48.198 9.284 -0.482 0.50 24.59 ? 178 ARG A NE 1 ATOM 1324 C CZ A ARG A 1 162 ? 49.229 7.051 -2.509 0.50 28.55 ? 178 ARG A CZ 1 ATOM 1325 C CZ B ARG A 1 162 ? 49.363 8.700 -0.209 0.50 24.01 ? 178 ARG A CZ 1 ATOM 1326 N NH1 A ARG A 1 162 ? 49.804 7.571 -1.431 0.50 28.85 ? 178 ARG A NH1 1 ATOM 1327 N NH1 B ARG A 1 162 ? 49.568 7.432 -0.517 0.50 23.74 ? 178 ARG A NH1 1 ATOM 1328 N NH2 A ARG A 1 162 ? 49.563 5.837 -2.917 0.50 28.03 ? 178 ARG A NH2 1 ATOM 1329 N NH2 B ARG A 1 162 ? 50.328 9.387 0.385 0.50 23.90 ? 178 ARG A NH2 1 ATOM 1330 N N . SER A 1 163 ? 44.007 11.426 -2.799 1.00 27.50 ? 179 SER A N 1 ATOM 1331 C CA . SER A 1 163 ? 44.128 12.873 -2.523 1.00 28.77 ? 179 SER A CA 1 ATOM 1332 C C . SER A 1 163 ? 43.043 13.377 -1.557 1.00 27.98 ? 179 SER A C 1 ATOM 1333 O O . SER A 1 163 ? 43.339 14.145 -0.634 1.00 27.09 ? 179 SER A O 1 ATOM 1334 C CB . SER A 1 163 ? 44.215 13.710 -3.808 1.00 30.51 ? 179 SER A CB 1 ATOM 1335 O OG . SER A 1 163 ? 43.063 13.524 -4.595 1.00 33.80 ? 179 SER A OG 1 ATOM 1336 N N . GLN A 1 164 ? 41.811 12.895 -1.736 1.00 27.70 ? 180 GLN A N 1 ATOM 1337 C CA . GLN A 1 164 ? 40.725 13.197 -0.805 1.00 27.38 ? 180 GLN A CA 1 ATOM 1338 C C . GLN A 1 164 ? 41.032 12.634 0.578 1.00 26.25 ? 180 GLN A C 1 ATOM 1339 O O . GLN A 1 164 ? 40.832 13.317 1.590 1.00 25.59 ? 180 GLN A O 1 ATOM 1340 C CB . GLN A 1 164 ? 39.394 12.631 -1.289 1.00 28.33 ? 180 GLN A CB 1 ATOM 1341 C CG . GLN A 1 164 ? 38.818 13.336 -2.504 1.00 30.37 ? 180 GLN A CG 1 ATOM 1342 C CD . GLN A 1 164 ? 39.193 12.656 -3.806 1.00 32.22 ? 180 GLN A CD 1 ATOM 1343 O OE1 . GLN A 1 164 ? 40.140 11.860 -3.868 1.00 31.89 ? 180 GLN A OE1 1 ATOM 1344 N NE2 . GLN A 1 164 ? 38.449 12.971 -4.866 1.00 33.42 ? 180 GLN A NE2 1 ATOM 1345 N N . PHE A 1 165 ? 41.523 11.395 0.627 1.00 25.13 ? 181 PHE A N 1 ATOM 1346 C CA . PHE A 1 165 ? 41.870 10.795 1.924 1.00 24.12 ? 181 PHE A CA 1 ATOM 1347 C C . PHE A 1 165 ? 42.951 11.600 2.650 1.00 24.55 ? 181 PHE A C 1 ATOM 1348 O O . PHE A 1 165 ? 42.866 11.806 3.863 1.00 23.85 ? 181 PHE A O 1 ATOM 1349 C CB . PHE A 1 165 ? 42.278 9.319 1.794 1.00 23.17 ? 181 PHE A CB 1 ATOM 1350 C CG . PHE A 1 165 ? 42.321 8.593 3.121 1.00 22.14 ? 181 PHE A CG 1 ATOM 1351 C CD1 . PHE A 1 165 ? 41.165 8.016 3.648 1.00 21.50 ? 181 PHE A CD1 1 ATOM 1352 C CD2 . PHE A 1 165 ? 43.503 8.500 3.834 1.00 21.69 ? 181 PHE A CD2 1 ATOM 1353 C CE1 . PHE A 1 165 ? 41.191 7.363 4.865 1.00 21.60 ? 181 PHE A CE1 1 ATOM 1354 C CE2 . PHE A 1 165 ? 43.536 7.845 5.065 1.00 21.54 ? 181 PHE A CE2 1 ATOM 1355 C CZ . PHE A 1 165 ? 42.381 7.274 5.571 1.00 20.99 ? 181 PHE A CZ 1 ATOM 1356 N N . GLU A 1 166 ? 43.952 12.062 1.903 1.00 25.77 ? 182 GLU A N 1 ATOM 1357 C CA . GLU A 1 166 ? 45.006 12.919 2.461 1.00 27.14 ? 182 GLU A CA 1 ATOM 1358 C C . GLU A 1 166 ? 44.480 14.200 3.115 1.00 26.21 ? 182 GLU A C 1 ATOM 1359 O O . GLU A 1 166 ? 44.913 14.556 4.222 1.00 25.74 ? 182 GLU A O 1 ATOM 1360 C CB . GLU A 1 166 ? 46.054 13.261 1.404 1.00 28.89 ? 182 GLU A CB 1 ATOM 1361 C CG . GLU A 1 166 ? 47.038 12.136 1.142 1.00 31.96 ? 182 GLU A CG 1 ATOM 1362 C CD . GLU A 1 166 ? 48.120 12.518 0.146 1.00 35.04 ? 182 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 166 ? 48.309 13.723 -0.127 1.00 36.89 ? 182 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 166 ? 48.792 11.604 -0.362 1.00 36.45 ? 182 GLU A OE2 1 ATOM 1365 N N . ARG A 1 167 ? 43.556 14.884 2.439 1.00 26.39 ? 183 ARG A N 1 ATOM 1366 C CA . ARG A 1 167 ? 42.954 16.102 2.991 1.00 26.07 ? 183 ARG A CA 1 ATOM 1367 C C . ARG A 1 167 ? 42.074 15.791 4.200 1.00 25.33 ? 183 ARG A C 1 ATOM 1368 O O . ARG A 1 167 ? 42.045 16.562 5.163 1.00 24.89 ? 183 ARG A O 1 ATOM 1369 C CB . ARG A 1 167 ? 42.164 16.882 1.932 1.00 27.05 ? 183 ARG A CB 1 ATOM 1370 C CG . ARG A 1 167 ? 41.650 18.244 2.401 1.00 27.95 ? 183 ARG A CG 1 ATOM 1371 C CD . ARG A 1 167 ? 42.789 19.242 2.558 1.00 28.86 ? 183 ARG A CD 1 ATOM 1372 N NE . ARG A 1 167 ? 42.309 20.560 2.968 1.00 30.48 ? 183 ARG A NE 1 ATOM 1373 C CZ . ARG A 1 167 ? 42.780 21.262 4.000 1.00 30.68 ? 183 ARG A CZ 1 ATOM 1374 N NH1 . ARG A 1 167 ? 43.769 20.795 4.751 1.00 30.63 ? 183 ARG A NH1 1 ATOM 1375 N NH2 . ARG A 1 167 ? 42.260 22.450 4.275 1.00 31.32 ? 183 ARG A NH2 1 ATOM 1376 N N . TYR A 1 168 ? 41.363 14.663 4.146 1.00 24.33 ? 184 TYR A N 1 ATOM 1377 C CA . TYR A 1 168 ? 40.572 14.201 5.281 1.00 23.84 ? 184 TYR A CA 1 ATOM 1378 C C . TYR A 1 168 ? 41.457 14.040 6.524 1.00 23.34 ? 184 TYR A C 1 ATOM 1379 O O . TYR A 1 168 ? 41.097 14.514 7.605 1.00 23.18 ? 184 TYR A O 1 ATOM 1380 C CB . TYR A 1 168 ? 39.841 12.893 4.930 1.00 23.42 ? 184 TYR A CB 1 ATOM 1381 C CG . TYR A 1 168 ? 39.588 11.923 6.088 1.00 22.80 ? 184 TYR A CG 1 ATOM 1382 C CD1 . TYR A 1 168 ? 38.597 12.179 7.051 1.00 22.59 ? 184 TYR A CD1 1 ATOM 1383 C CD2 . TYR A 1 168 ? 40.320 10.725 6.193 1.00 22.58 ? 184 TYR A CD2 1 ATOM 1384 C CE1 . TYR A 1 168 ? 38.355 11.279 8.088 1.00 21.94 ? 184 TYR A CE1 1 ATOM 1385 C CE2 . TYR A 1 168 ? 40.086 9.820 7.225 1.00 22.10 ? 184 TYR A CE2 1 ATOM 1386 C CZ . TYR A 1 168 ? 39.103 10.097 8.166 1.00 21.77 ? 184 TYR A CZ 1 ATOM 1387 O OH . TYR A 1 168 ? 38.882 9.191 9.179 1.00 21.95 ? 184 TYR A OH 1 ATOM 1388 N N . VAL A 1 169 ? 42.614 13.387 6.370 1.00 22.88 ? 185 VAL A N 1 ATOM 1389 C CA . VAL A 1 169 ? 43.533 13.195 7.511 1.00 22.70 ? 185 VAL A CA 1 ATOM 1390 C C . VAL A 1 169 ? 43.971 14.553 8.089 1.00 22.96 ? 185 VAL A C 1 ATOM 1391 O O . VAL A 1 169 ? 43.963 14.744 9.303 1.00 22.64 ? 185 VAL A O 1 ATOM 1392 C CB . VAL A 1 169 ? 44.747 12.293 7.148 1.00 22.35 ? 185 VAL A CB 1 ATOM 1393 C CG1 . VAL A 1 169 ? 45.803 12.311 8.252 1.00 22.37 ? 185 VAL A CG1 1 ATOM 1394 C CG2 . VAL A 1 169 ? 44.287 10.862 6.881 1.00 21.51 ? 185 VAL A CG2 1 ATOM 1395 N N . GLU A 1 170 ? 44.339 15.490 7.220 1.00 23.50 ? 186 GLU A N 1 ATOM 1396 C CA . GLU A 1 170 ? 44.695 16.857 7.635 1.00 24.84 ? 186 GLU A CA 1 ATOM 1397 C C . GLU A 1 170 ? 43.610 17.558 8.451 1.00 23.99 ? 186 GLU A C 1 ATOM 1398 O O . GLU A 1 170 ? 43.884 18.085 9.535 1.00 24.81 ? 186 GLU A O 1 ATOM 1399 C CB . GLU A 1 170 ? 45.048 17.712 6.418 1.00 26.08 ? 186 GLU A CB 1 ATOM 1400 C CG . GLU A 1 170 ? 46.402 17.377 5.840 1.00 28.74 ? 186 GLU A CG 1 ATOM 1401 C CD . GLU A 1 170 ? 46.736 18.186 4.595 1.00 31.34 ? 186 GLU A CD 1 ATOM 1402 O OE1 . GLU A 1 170 ? 45.866 18.917 4.068 1.00 31.84 ? 186 GLU A OE1 1 ATOM 1403 O OE2 . GLU A 1 170 ? 47.899 18.097 4.161 1.00 33.53 ? 186 GLU A OE2 1 ATOM 1404 N N . LEU A 1 171 ? 42.380 17.540 7.951 1.00 23.49 ? 187 LEU A N 1 ATOM 1405 C CA . LEU A 1 171 ? 41.278 18.230 8.623 1.00 23.41 ? 187 LEU A CA 1 ATOM 1406 C C . LEU A 1 171 ? 40.831 17.509 9.887 1.00 22.97 ? 187 LEU A C 1 ATOM 1407 O O . LEU A 1 171 ? 40.481 18.146 10.890 1.00 23.39 ? 187 LEU A O 1 ATOM 1408 C CB . LEU A 1 171 ? 40.106 18.467 7.662 1.00 24.13 ? 187 LEU A CB 1 ATOM 1409 C CG . LEU A 1 171 ? 40.436 19.515 6.587 1.00 24.57 ? 187 LEU A CG 1 ATOM 1410 C CD1 . LEU A 1 171 ? 39.432 19.467 5.439 1.00 24.49 ? 187 LEU A CD1 1 ATOM 1411 C CD2 . LEU A 1 171 ? 40.517 20.913 7.195 1.00 25.02 ? 187 LEU A CD2 1 ATOM 1412 N N . ASN A 1 172 ? 40.860 16.181 9.848 1.00 21.93 ? 188 ASN A N 1 ATOM 1413 C CA . ASN A 1 172 ? 40.583 15.397 11.044 1.00 21.45 ? 188 ASN A CA 1 ATOM 1414 C C . ASN A 1 172 ? 41.577 15.748 12.167 1.00 21.04 ? 188 ASN A C 1 ATOM 1415 O O . ASN A 1 172 ? 41.176 15.935 13.310 1.00 21.60 ? 188 ASN A O 1 ATOM 1416 C CB . ASN A 1 172 ? 40.577 13.891 10.716 1.00 20.74 ? 188 ASN A CB 1 ATOM 1417 C CG . ASN A 1 172 ? 40.485 13.021 11.956 1.00 20.61 ? 188 ASN A CG 1 ATOM 1418 O OD1 . ASN A 1 172 ? 41.423 12.960 12.735 1.00 20.42 ? 188 ASN A OD1 1 ATOM 1419 N ND2 . ASN A 1 172 ? 39.357 12.345 12.134 1.00 20.34 ? 188 ASN A ND2 1 ATOM 1420 N N . THR A 1 173 ? 42.862 15.845 11.833 1.00 21.11 ? 189 THR A N 1 ATOM 1421 C CA . THR A 1 173 ? 43.909 16.229 12.790 1.00 21.45 ? 189 THR A CA 1 ATOM 1422 C C . THR A 1 173 ? 43.699 17.651 13.337 1.00 22.03 ? 189 THR A C 1 ATOM 1423 O O . THR A 1 173 ? 43.782 17.885 14.559 1.00 21.03 ? 189 THR A O 1 ATOM 1424 C CB . THR A 1 173 ? 45.314 16.116 12.156 1.00 21.36 ? 189 THR A CB 1 ATOM 1425 O OG1 . THR A 1 173 ? 45.491 14.796 11.630 1.00 21.38 ? 189 THR A OG1 1 ATOM 1426 C CG2 . THR A 1 173 ? 46.413 16.402 13.206 1.00 21.29 ? 189 THR A CG2 1 ATOM 1427 N N . LYS A 1 174 ? 43.426 18.586 12.426 1.00 22.02 ? 190 LYS A N 1 ATOM 1428 C CA . LYS A 1 174 ? 43.151 19.967 12.806 1.00 22.56 ? 190 LYS A CA 1 ATOM 1429 C C . LYS A 1 174 ? 41.961 20.068 13.783 1.00 22.15 ? 190 LYS A C 1 ATOM 1430 O O . LYS A 1 174 ? 42.025 20.824 14.766 1.00 21.84 ? 190 LYS A O 1 ATOM 1431 C CB . LYS A 1 174 ? 42.940 20.847 11.563 1.00 23.63 ? 190 LYS A CB 1 ATOM 1432 C CG . LYS A 1 174 ? 42.654 22.307 11.901 1.00 24.77 ? 190 LYS A CG 1 ATOM 1433 C CD . LYS A 1 174 ? 42.644 23.212 10.682 1.00 26.00 ? 190 LYS A CD 1 ATOM 1434 C CE . LYS A 1 174 ? 42.585 24.667 11.133 1.00 27.34 ? 190 LYS A CE 1 ATOM 1435 N NZ . LYS A 1 174 ? 42.613 25.606 9.977 1.00 28.23 ? 190 LYS A NZ 1 ATOM 1436 N N . ALA A 1 175 ? 40.901 19.290 13.526 1.00 21.55 ? 191 ALA A N 1 ATOM 1437 C CA . ALA A 1 175 ? 39.721 19.271 14.393 1.00 21.22 ? 191 ALA A CA 1 ATOM 1438 C C . ALA A 1 175 ? 40.063 18.736 15.768 1.00 21.06 ? 191 ALA A C 1 ATOM 1439 O O . ALA A 1 175 ? 39.647 19.333 16.756 1.00 21.77 ? 191 ALA A O 1 ATOM 1440 C CB . ALA A 1 175 ? 38.583 18.449 13.807 1.00 20.93 ? 191 ALA A CB 1 ATOM 1441 N N . ALA A 1 176 ? 40.782 17.609 15.825 1.00 20.54 ? 192 ALA A N 1 ATOM 1442 C CA . ALA A 1 176 ? 41.195 17.011 17.118 1.00 20.54 ? 192 ALA A CA 1 ATOM 1443 C C . ALA A 1 176 ? 41.970 17.989 17.984 1.00 21.04 ? 192 ALA A C 1 ATOM 1444 O O . ALA A 1 176 ? 41.762 18.058 19.216 1.00 20.98 ? 192 ALA A O 1 ATOM 1445 C CB . ALA A 1 176 ? 42.034 15.760 16.893 1.00 19.77 ? 192 ALA A CB 1 ATOM 1446 N N . LYS A 1 177 ? 42.888 18.714 17.352 1.00 21.40 ? 193 LYS A N 1 ATOM 1447 C CA . LYS A 1 177 ? 43.747 19.656 18.068 1.00 22.72 ? 193 LYS A CA 1 ATOM 1448 C C . LYS A 1 177 ? 42.969 20.881 18.558 1.00 23.08 ? 193 LYS A C 1 ATOM 1449 O O . LYS A 1 177 ? 43.298 21.421 19.599 1.00 23.39 ? 193 LYS A O 1 ATOM 1450 C CB . LYS A 1 177 ? 44.972 20.049 17.231 1.00 23.67 ? 193 LYS A CB 1 ATOM 1451 C CG . LYS A 1 177 ? 45.977 18.909 17.050 1.00 24.31 ? 193 LYS A CG 1 ATOM 1452 C CD . LYS A 1 177 ? 47.253 19.367 16.359 1.00 25.66 ? 193 LYS A CD 1 ATOM 1453 C CE . LYS A 1 177 ? 48.245 18.223 16.160 1.00 25.70 ? 193 LYS A CE 1 ATOM 1454 N NZ . LYS A 1 177 ? 48.712 17.661 17.468 1.00 25.66 ? 193 LYS A NZ 1 ATOM 1455 N N . LEU A 1 178 ? 41.927 21.292 17.831 1.00 23.61 ? 194 LEU A N 1 ATOM 1456 C CA . LEU A 1 178 ? 41.039 22.369 18.300 1.00 24.15 ? 194 LEU A CA 1 ATOM 1457 C C . LEU A 1 178 ? 40.215 21.949 19.518 1.00 24.72 ? 194 LEU A C 1 ATOM 1458 O O . LEU A 1 178 ? 39.734 22.799 20.270 1.00 25.10 ? 194 LEU A O 1 ATOM 1459 C CB . LEU A 1 178 ? 40.114 22.872 17.186 1.00 24.24 ? 194 LEU A CB 1 ATOM 1460 C CG . LEU A 1 178 ? 40.746 23.838 16.176 1.00 24.59 ? 194 LEU A CG 1 ATOM 1461 C CD1 . LEU A 1 178 ? 39.876 23.944 14.936 1.00 25.07 ? 194 LEU A CD1 1 ATOM 1462 C CD2 . LEU A 1 178 ? 40.993 25.219 16.784 1.00 25.25 ? 194 LEU A CD2 1 ATOM 1463 N N . ASN A 1 179 ? 40.057 20.637 19.696 1.00 23.88 ? 195 ASN A N 1 ATOM 1464 C CA . ASN A 1 179 ? 39.426 20.078 20.881 1.00 24.23 ? 195 ASN A CA 1 ATOM 1465 C C . ASN A 1 179 ? 40.458 19.722 21.960 1.00 23.81 ? 195 ASN A C 1 ATOM 1466 O O . ASN A 1 179 ? 40.111 19.150 22.996 1.00 23.63 ? 195 ASN A O 1 ATOM 1467 C CB . ASN A 1 179 ? 38.569 18.862 20.508 1.00 24.20 ? 195 ASN A CB 1 ATOM 1468 C CG . ASN A 1 179 ? 37.335 19.249 19.718 1.00 25.38 ? 195 ASN A CG 1 ATOM 1469 O OD1 . ASN A 1 179 ? 36.395 19.803 20.267 1.00 27.02 ? 195 ASN A OD1 1 ATOM 1470 N ND2 . ASN A 1 179 ? 37.342 18.978 18.416 1.00 24.87 ? 195 ASN A ND2 1 ATOM 1471 N N . ASN A 1 180 ? 41.721 20.068 21.695 1.00 24.03 ? 196 ASN A N 1 ATOM 1472 C CA . ASN A 1 180 ? 42.867 19.778 22.582 1.00 23.70 ? 196 ASN A CA 1 ATOM 1473 C C . ASN A 1 180 ? 43.176 18.294 22.792 1.00 23.35 ? 196 ASN A C 1 ATOM 1474 O O . ASN A 1 180 ? 43.748 17.910 23.819 1.00 23.24 ? 196 ASN A O 1 ATOM 1475 C CB . ASN A 1 180 ? 42.757 20.529 23.916 1.00 24.27 ? 196 ASN A CB 1 ATOM 1476 C CG . ASN A 1 180 ? 42.931 22.028 23.753 1.00 25.10 ? 196 ASN A CG 1 ATOM 1477 O OD1 . ASN A 1 180 ? 43.505 22.487 22.766 1.00 25.41 ? 196 ASN A OD1 1 ATOM 1478 N ND2 . ASN A 1 180 ? 42.441 22.798 24.721 1.00 25.16 ? 196 ASN A ND2 1 ATOM 1479 N N . PHE A 1 181 ? 42.782 17.467 21.821 1.00 22.49 ? 197 PHE A N 1 ATOM 1480 C CA . PHE A 1 181 ? 43.299 16.099 21.716 1.00 22.26 ? 197 PHE A CA 1 ATOM 1481 C C . PHE A 1 181 ? 44.579 16.146 20.884 1.00 22.38 ? 197 PHE A C 1 ATOM 1482 O O . PHE A 1 181 ? 44.718 17.017 20.020 1.00 22.56 ? 197 PHE A O 1 ATOM 1483 C CB . PHE A 1 181 ? 42.267 15.168 21.069 1.00 21.45 ? 197 PHE A CB 1 ATOM 1484 C CG . PHE A 1 181 ? 41.070 14.885 21.940 1.00 21.75 ? 197 PHE A CG 1 ATOM 1485 C CD1 . PHE A 1 181 ? 41.202 14.127 23.112 1.00 21.96 ? 197 PHE A CD1 1 ATOM 1486 C CD2 . PHE A 1 181 ? 39.819 15.382 21.607 1.00 21.60 ? 197 PHE A CD2 1 ATOM 1487 C CE1 . PHE A 1 181 ? 40.103 13.873 23.926 1.00 21.64 ? 197 PHE A CE1 1 ATOM 1488 C CE2 . PHE A 1 181 ? 38.710 15.114 22.401 1.00 22.02 ? 197 PHE A CE2 1 ATOM 1489 C CZ . PHE A 1 181 ? 38.852 14.365 23.564 1.00 22.32 ? 197 PHE A CZ 1 ATOM 1490 N N . THR A 1 182 ? 45.509 15.218 21.122 1.00 22.09 ? 198 THR A N 1 ATOM 1491 C CA . THR A 1 182 ? 46.752 15.195 20.350 1.00 22.17 ? 198 THR A CA 1 ATOM 1492 C C . THR A 1 182 ? 46.446 14.942 18.878 1.00 21.68 ? 198 THR A C 1 ATOM 1493 O O . THR A 1 182 ? 47.048 15.555 17.991 1.00 21.92 ? 198 THR A O 1 ATOM 1494 C CB . THR A 1 182 ? 47.711 14.110 20.851 1.00 22.74 ? 198 THR A CB 1 ATOM 1495 O OG1 . THR A 1 182 ? 47.948 14.308 22.245 1.00 23.14 ? 198 THR A OG1 1 ATOM 1496 C CG2 . THR A 1 182 ? 49.043 14.189 20.113 1.00 23.64 ? 198 THR A CG2 1 ATOM 1497 N N . SER A 1 183 ? 45.490 14.049 18.639 1.00 20.49 ? 199 SER A N 1 ATOM 1498 C CA . SER A 1 183 ? 45.136 13.635 17.291 1.00 19.46 ? 199 SER A CA 1 ATOM 1499 C C . SER A 1 183 ? 43.743 12.988 17.282 1.00 18.69 ? 199 SER A C 1 ATOM 1500 O O . SER A 1 183 ? 43.116 12.810 18.321 1.00 18.02 ? 199 SER A O 1 ATOM 1501 C CB . SER A 1 183 ? 46.197 12.659 16.752 1.00 19.67 ? 199 SER A CB 1 ATOM 1502 O OG . SER A 1 183 ? 45.975 11.325 17.203 1.00 19.30 ? 199 SER A OG 1 ATOM 1503 N N . GLY A 1 184 ? 43.246 12.634 16.105 1.00 17.79 ? 200 GLY A N 1 ATOM 1504 C CA . GLY A 1 184 ? 41.956 11.953 16.041 1.00 17.41 ? 200 GLY A CA 1 ATOM 1505 C C . GLY A 1 184 ? 41.942 10.568 16.672 1.00 16.72 ? 200 GLY A C 1 ATOM 1506 O O . GLY A 1 184 ? 40.878 10.019 16.960 1.00 16.42 ? 200 GLY A O 1 ATOM 1507 N N . ALA A 1 185 ? 43.125 9.987 16.862 1.00 17.14 ? 201 ALA A N 1 ATOM 1508 C CA . ALA A 1 185 ? 43.230 8.692 17.508 1.00 17.23 ? 201 ALA A CA 1 ATOM 1509 C C . ALA A 1 185 ? 42.725 8.903 18.933 1.00 17.61 ? 201 ALA A C 1 ATOM 1510 O O . ALA A 1 185 ? 41.869 8.161 19.400 1.00 17.20 ? 201 ALA A O 1 ATOM 1511 C CB . ALA A 1 185 ? 44.667 8.201 17.521 1.00 17.09 ? 201 ALA A CB 1 ATOM 1512 N N . GLU A 1 186 ? 43.214 9.962 19.575 1.00 18.63 ? 202 GLU A N 1 ATOM 1513 C CA . GLU A 1 186 ? 42.813 10.274 20.964 1.00 19.15 ? 202 GLU A CA 1 ATOM 1514 C C . GLU A 1 186 ? 41.351 10.726 21.062 1.00 19.27 ? 202 GLU A C 1 ATOM 1515 O O . GLU A 1 186 ? 40.646 10.385 22.021 1.00 18.81 ? 202 GLU A O 1 ATOM 1516 C CB . GLU A 1 186 ? 43.744 11.317 21.579 1.00 20.56 ? 202 GLU A CB 1 ATOM 1517 C CG . GLU A 1 186 ? 45.130 10.794 21.943 1.00 21.94 ? 202 GLU A CG 1 ATOM 1518 C CD . GLU A 1 186 ? 46.035 10.548 20.751 1.00 22.95 ? 202 GLU A CD 1 ATOM 1519 O OE1 . GLU A 1 186 ? 45.833 11.169 19.674 1.00 23.67 ? 202 GLU A OE1 1 ATOM 1520 O OE2 . GLU A 1 186 ? 46.957 9.721 20.885 1.00 23.90 ? 202 GLU A OE2 1 ATOM 1521 N N . ALA A 1 187 ? 40.898 11.500 20.079 1.00 19.23 ? 203 ALA A N 1 ATOM 1522 C CA . ALA A 1 187 ? 39.486 11.846 19.943 1.00 19.61 ? 203 ALA A CA 1 ATOM 1523 C C . ALA A 1 187 ? 38.595 10.595 19.909 1.00 19.86 ? 203 ALA A C 1 ATOM 1524 O O . ALA A 1 187 ? 37.614 10.534 20.645 1.00 20.24 ? 203 ALA A O 1 ATOM 1525 C CB . ALA A 1 187 ? 39.260 12.703 18.699 1.00 19.64 ? 203 ALA A CB 1 ATOM 1526 N N . TRP A 1 188 ? 38.927 9.605 19.064 1.00 19.75 ? 204 TRP A N 1 ATOM 1527 C CA . TRP A 1 188 ? 38.163 8.343 19.026 1.00 18.98 ? 204 TRP A CA 1 ATOM 1528 C C . TRP A 1 188 ? 38.198 7.613 20.376 1.00 19.44 ? 204 TRP A C 1 ATOM 1529 O O . TRP A 1 188 ? 37.160 7.168 20.882 1.00 18.86 ? 204 TRP A O 1 ATOM 1530 C CB . TRP A 1 188 ? 38.664 7.408 17.911 1.00 18.99 ? 204 TRP A CB 1 ATOM 1531 C CG . TRP A 1 188 ? 38.176 7.775 16.525 1.00 18.66 ? 204 TRP A CG 1 ATOM 1532 C CD1 . TRP A 1 188 ? 37.213 8.698 16.197 1.00 18.50 ? 204 TRP A CD1 1 ATOM 1533 C CD2 . TRP A 1 188 ? 38.606 7.183 15.285 1.00 18.60 ? 204 TRP A CD2 1 ATOM 1534 N NE1 . TRP A 1 188 ? 37.039 8.727 14.813 1.00 18.55 ? 204 TRP A NE1 1 ATOM 1535 C CE2 . TRP A 1 188 ? 37.874 7.800 14.245 1.00 18.79 ? 204 TRP A CE2 1 ATOM 1536 C CE3 . TRP A 1 188 ? 39.540 6.184 14.960 1.00 18.73 ? 204 TRP A CE3 1 ATOM 1537 C CZ2 . TRP A 1 188 ? 38.064 7.465 12.888 1.00 18.70 ? 204 TRP A CZ2 1 ATOM 1538 C CZ3 . TRP A 1 188 ? 39.725 5.846 13.616 1.00 18.90 ? 204 TRP A CZ3 1 ATOM 1539 C CH2 . TRP A 1 188 ? 38.986 6.487 12.604 1.00 18.86 ? 204 TRP A CH2 1 ATOM 1540 N N . LEU A 1 189 ? 39.396 7.508 20.958 1.00 19.18 ? 205 LEU A N 1 ATOM 1541 C CA . LEU A 1 189 ? 39.566 6.733 22.182 1.00 18.99 ? 205 LEU A CA 1 ATOM 1542 C C . LEU A 1 189 ? 38.827 7.327 23.378 1.00 19.70 ? 205 LEU A C 1 ATOM 1543 O O . LEU A 1 189 ? 38.499 6.609 24.333 1.00 19.72 ? 205 LEU A O 1 ATOM 1544 C CB . LEU A 1 189 ? 41.050 6.529 22.490 1.00 18.68 ? 205 LEU A CB 1 ATOM 1545 C CG . LEU A 1 189 ? 41.725 5.500 21.582 1.00 18.23 ? 205 LEU A CG 1 ATOM 1546 C CD1 . LEU A 1 189 ? 43.236 5.699 21.591 1.00 18.15 ? 205 LEU A CD1 1 ATOM 1547 C CD2 . LEU A 1 189 ? 41.346 4.081 21.977 1.00 18.25 ? 205 LEU A CD2 1 ATOM 1548 N N . ASP A 1 190 ? 38.571 8.630 23.317 1.00 20.36 ? 206 ASP A N 1 ATOM 1549 C CA . ASP A 1 190 ? 37.830 9.348 24.360 1.00 21.42 ? 206 ASP A CA 1 ATOM 1550 C C . ASP A 1 190 ? 36.452 8.728 24.624 1.00 21.46 ? 206 ASP A C 1 ATOM 1551 O O . ASP A 1 190 ? 35.970 8.761 25.756 1.00 21.07 ? 206 ASP A O 1 ATOM 1552 C CB . ASP A 1 190 ? 37.686 10.836 23.991 1.00 22.46 ? 206 ASP A CB 1 ATOM 1553 C CG . ASP A 1 190 ? 37.040 11.669 25.108 1.00 23.94 ? 206 ASP A CG 1 ATOM 1554 O OD1 . ASP A 1 190 ? 37.634 11.756 26.196 1.00 24.30 ? 206 ASP A OD1 1 ATOM 1555 O OD2 . ASP A 1 190 ? 35.943 12.236 24.898 1.00 24.87 ? 206 ASP A OD2 1 ATOM 1556 N N . GLU A 1 191 ? 35.833 8.151 23.592 1.00 21.48 ? 207 GLU A N 1 ATOM 1557 C CA . GLU A 1 191 ? 34.521 7.482 23.727 1.00 22.16 ? 207 GLU A CA 1 ATOM 1558 C C . GLU A 1 191 ? 34.498 6.293 24.715 1.00 21.77 ? 207 GLU A C 1 ATOM 1559 O O . GLU A 1 191 ? 33.421 5.859 25.134 1.00 21.66 ? 207 GLU A O 1 ATOM 1560 C CB . GLU A 1 191 ? 33.991 7.013 22.359 1.00 23.17 ? 207 GLU A CB 1 ATOM 1561 C CG . GLU A 1 191 ? 33.917 8.092 21.275 1.00 24.64 ? 207 GLU A CG 1 ATOM 1562 C CD . GLU A 1 191 ? 32.983 9.242 21.623 1.00 26.73 ? 207 GLU A CD 1 ATOM 1563 O OE1 . GLU A 1 191 ? 31.964 9.032 22.320 1.00 27.38 ? 207 GLU A OE1 1 ATOM 1564 O OE2 . GLU A 1 191 ? 33.270 10.378 21.198 1.00 29.29 ? 207 GLU A OE2 1 ATOM 1565 N N . TYR A 1 192 ? 35.672 5.768 25.074 1.00 21.15 ? 208 TYR A N 1 ATOM 1566 C CA . TYR A 1 192 ? 35.747 4.621 25.986 1.00 21.18 ? 208 TYR A CA 1 ATOM 1567 C C . TYR A 1 192 ? 36.043 5.009 27.424 1.00 21.73 ? 208 TYR A C 1 ATOM 1568 O O . TYR A 1 192 ? 36.105 4.136 28.283 1.00 21.77 ? 208 TYR A O 1 ATOM 1569 C CB . TYR A 1 192 ? 36.752 3.577 25.495 1.00 20.71 ? 208 TYR A CB 1 ATOM 1570 C CG . TYR A 1 192 ? 36.408 3.078 24.107 1.00 20.33 ? 208 TYR A CG 1 ATOM 1571 C CD1 . TYR A 1 192 ? 35.458 2.066 23.924 1.00 20.55 ? 208 TYR A CD1 1 ATOM 1572 C CD2 . TYR A 1 192 ? 36.989 3.650 22.982 1.00 20.72 ? 208 TYR A CD2 1 ATOM 1573 C CE1 . TYR A 1 192 ? 35.123 1.617 22.657 1.00 20.02 ? 208 TYR A CE1 1 ATOM 1574 C CE2 . TYR A 1 192 ? 36.662 3.214 21.706 1.00 20.27 ? 208 TYR A CE2 1 ATOM 1575 C CZ . TYR A 1 192 ? 35.722 2.202 21.552 1.00 20.53 ? 208 TYR A CZ 1 ATOM 1576 O OH . TYR A 1 192 ? 35.393 1.761 20.287 1.00 20.01 ? 208 TYR A OH 1 ATOM 1577 N N . GLU A 1 193 ? 36.246 6.308 27.667 1.00 22.41 ? 209 GLU A N 1 ATOM 1578 C CA . GLU A 1 193 ? 36.393 6.847 29.033 1.00 23.68 ? 209 GLU A CA 1 ATOM 1579 C C . GLU A 1 193 ? 37.363 6.040 29.905 1.00 23.36 ? 209 GLU A C 1 ATOM 1580 O O . GLU A 1 193 ? 37.065 5.745 31.071 1.00 22.89 ? 209 GLU A O 1 ATOM 1581 C CB . GLU A 1 193 ? 35.029 6.887 29.739 1.00 25.50 ? 209 GLU A CB 1 ATOM 1582 C CG . GLU A 1 193 ? 34.009 7.856 29.173 1.00 28.68 ? 209 GLU A CG 1 ATOM 1583 C CD . GLU A 1 193 ? 32.756 7.952 30.043 1.00 30.11 ? 209 GLU A CD 1 ATOM 1584 O OE1 . GLU A 1 193 ? 32.824 8.398 31.212 1.00 30.64 ? 209 GLU A OE1 1 ATOM 1585 O OE2 . GLU A 1 193 ? 31.686 7.565 29.557 1.00 32.53 ? 209 GLU A OE2 1 ATOM 1586 N N . ASP A 1 194 ? 38.509 5.667 29.342 1.00 23.01 ? 210 ASP A N 1 ATOM 1587 C CA . ASP A 1 194 ? 39.459 4.823 30.049 1.00 23.09 ? 210 ASP A CA 1 ATOM 1588 C C . ASP A 1 194 ? 40.860 5.046 29.486 1.00 23.13 ? 210 ASP A C 1 ATOM 1589 O O . ASP A 1 194 ? 41.154 4.681 28.330 1.00 22.45 ? 210 ASP A O 1 ATOM 1590 C CB . ASP A 1 194 ? 39.035 3.346 29.952 1.00 23.13 ? 210 ASP A CB 1 ATOM 1591 C CG . ASP A 1 194 ? 39.859 2.433 30.851 1.00 23.17 ? 210 ASP A CG 1 ATOM 1592 O OD1 . ASP A 1 194 ? 41.047 2.707 31.076 1.00 23.49 ? 210 ASP A OD1 1 ATOM 1593 O OD2 . ASP A 1 194 ? 39.337 1.399 31.306 1.00 24.30 ? 210 ASP A OD2 1 ATOM 1594 N N . ASP A 1 195 ? 41.720 5.677 30.283 1.00 23.37 ? 211 ASP A N 1 ATOM 1595 C CA . ASP A 1 195 ? 43.046 6.037 29.781 1.00 24.09 ? 211 ASP A CA 1 ATOM 1596 C C . ASP A 1 195 ? 44.042 4.862 29.674 1.00 24.07 ? 211 ASP A C 1 ATOM 1597 O O . ASP A 1 195 ? 45.154 5.052 29.205 1.00 25.48 ? 211 ASP A O 1 ATOM 1598 C CB . ASP A 1 195 ? 43.641 7.263 30.504 1.00 24.29 ? 211 ASP A CB 1 ATOM 1599 C CG . ASP A 1 195 ? 43.819 7.052 31.993 0.50 24.02 ? 211 ASP A CG 1 ATOM 1600 O OD1 . ASP A 1 195 ? 43.840 5.901 32.461 0.50 23.97 ? 211 ASP A OD1 1 ATOM 1601 O OD2 . ASP A 1 195 ? 43.950 8.067 32.697 0.50 24.01 ? 211 ASP A OD2 1 ATOM 1602 N N . THR A 1 196 ? 43.637 3.654 30.061 1.00 23.66 ? 212 THR A N 1 ATOM 1603 C CA . THR A 1 196 ? 44.456 2.464 29.786 1.00 23.22 ? 212 THR A CA 1 ATOM 1604 C C . THR A 1 196 ? 43.812 1.549 28.733 1.00 22.96 ? 212 THR A C 1 ATOM 1605 O O . THR A 1 196 ? 44.177 0.372 28.616 1.00 22.33 ? 212 THR A O 1 ATOM 1606 C CB . THR A 1 196 ? 44.730 1.632 31.056 1.00 24.19 ? 212 THR A CB 1 ATOM 1607 O OG1 . THR A 1 196 ? 43.488 1.172 31.610 1.00 25.10 ? 212 THR A OG1 1 ATOM 1608 C CG2 . THR A 1 196 ? 45.495 2.459 32.096 1.00 24.75 ? 212 THR A CG2 1 ATOM 1609 N N . PHE A 1 197 ? 42.875 2.092 27.951 1.00 21.77 ? 213 PHE A N 1 ATOM 1610 C CA . PHE A 1 197 ? 42.054 1.247 27.074 1.00 20.91 ? 213 PHE A CA 1 ATOM 1611 C C . PHE A 1 197 ? 42.872 0.507 26.009 1.00 20.96 ? 213 PHE A C 1 ATOM 1612 O O . PHE A 1 197 ? 42.674 -0.695 25.822 1.00 20.27 ? 213 PHE A O 1 ATOM 1613 C CB . PHE A 1 197 ? 40.902 2.036 26.450 1.00 20.14 ? 213 PHE A CB 1 ATOM 1614 C CG . PHE A 1 197 ? 39.714 1.185 26.079 1.00 20.19 ? 213 PHE A CG 1 ATOM 1615 C CD1 . PHE A 1 197 ? 38.921 0.596 27.052 1.00 19.66 ? 213 PHE A CD1 1 ATOM 1616 C CD2 . PHE A 1 197 ? 39.376 0.996 24.745 1.00 19.10 ? 213 PHE A CD2 1 ATOM 1617 C CE1 . PHE A 1 197 ? 37.818 -0.183 26.711 1.00 20.08 ? 213 PHE A CE1 1 ATOM 1618 C CE2 . PHE A 1 197 ? 38.276 0.220 24.393 1.00 19.43 ? 213 PHE A CE2 1 ATOM 1619 C CZ . PHE A 1 197 ? 37.497 -0.372 25.367 1.00 20.01 ? 213 PHE A CZ 1 ATOM 1620 N N . GLU A 1 198 ? 43.785 1.216 25.329 1.00 21.10 ? 214 GLU A N 1 ATOM 1621 C CA . GLU A 1 198 ? 44.668 0.590 24.335 1.00 21.35 ? 214 GLU A CA 1 ATOM 1622 C C . GLU A 1 198 ? 45.485 -0.564 24.925 1.00 21.42 ? 214 GLU A C 1 ATOM 1623 O O . GLU A 1 198 ? 45.582 -1.626 24.317 1.00 20.90 ? 214 GLU A O 1 ATOM 1624 C CB . GLU A 1 198 ? 45.635 1.609 23.713 1.00 21.79 ? 214 GLU A CB 1 ATOM 1625 C CG . GLU A 1 198 ? 45.001 2.653 22.817 1.00 22.00 ? 214 GLU A CG 1 ATOM 1626 C CD . GLU A 1 198 ? 45.953 3.812 22.550 1.00 22.72 ? 214 GLU A CD 1 ATOM 1627 O OE1 . GLU A 1 198 ? 46.116 4.667 23.451 1.00 22.43 ? 214 GLU A OE1 1 ATOM 1628 O OE2 . GLU A 1 198 ? 46.534 3.880 21.444 1.00 21.64 ? 214 GLU A OE2 1 ATOM 1629 N N . GLN A 1 199 ? 46.081 -0.350 26.100 1.00 21.19 ? 215 GLN A N 1 ATOM 1630 C CA . GLN A 1 199 ? 46.873 -1.401 26.743 1.00 22.12 ? 215 GLN A CA 1 ATOM 1631 C C . GLN A 1 199 ? 46.012 -2.612 27.100 1.00 21.65 ? 215 GLN A C 1 ATOM 1632 O O . GLN A 1 199 ? 46.461 -3.753 26.957 1.00 20.85 ? 215 GLN A O 1 ATOM 1633 C CB . GLN A 1 199 ? 47.614 -0.889 27.989 1.00 23.43 ? 215 GLN A CB 1 ATOM 1634 C CG . GLN A 1 199 ? 48.701 -1.846 28.495 1.00 26.01 ? 215 GLN A CG 1 ATOM 1635 C CD . GLN A 1 199 ? 49.680 -2.293 27.401 1.00 26.74 ? 215 GLN A CD 1 ATOM 1636 O OE1 . GLN A 1 199 ? 50.294 -1.473 26.711 1.00 27.29 ? 215 GLN A OE1 1 ATOM 1637 N NE2 . GLN A 1 199 ? 49.833 -3.606 27.249 1.00 26.99 ? 215 GLN A NE2 1 ATOM 1638 N N . GLN A 1 200 ? 44.782 -2.358 27.556 1.00 21.29 ? 216 GLN A N 1 ATOM 1639 C CA . GLN A 1 200 ? 43.839 -3.427 27.893 1.00 21.17 ? 216 GLN A CA 1 ATOM 1640 C C . GLN A 1 200 ? 43.558 -4.340 26.707 1.00 21.07 ? 216 GLN A C 1 ATOM 1641 O O . GLN A 1 200 ? 43.492 -5.563 26.859 1.00 20.63 ? 216 GLN A O 1 ATOM 1642 C CB . GLN A 1 200 ? 42.525 -2.845 28.397 1.00 21.53 ? 216 GLN A CB 1 ATOM 1643 C CG . GLN A 1 200 ? 42.557 -2.409 29.854 1.00 21.75 ? 216 GLN A CG 1 ATOM 1644 C CD . GLN A 1 200 ? 41.245 -1.766 30.255 1.00 22.08 ? 216 GLN A CD 1 ATOM 1645 O OE1 . GLN A 1 200 ? 40.199 -2.418 30.253 1.00 22.59 ? 216 GLN A OE1 1 ATOM 1646 N NE2 . GLN A 1 200 ? 41.281 -0.474 30.553 1.00 21.69 ? 216 GLN A NE2 1 ATOM 1647 N N . LEU A 1 201 ? 43.391 -3.726 25.534 1.00 20.47 ? 217 LEU A N 1 ATOM 1648 C CA . LEU A 1 201 ? 43.151 -4.449 24.282 1.00 20.94 ? 217 LEU A CA 1 ATOM 1649 C C . LEU A 1 201 ? 44.387 -5.181 23.763 1.00 20.97 ? 217 LEU A C 1 ATOM 1650 O O . LEU A 1 201 ? 44.268 -6.307 23.259 1.00 20.99 ? 217 LEU A O 1 ATOM 1651 C CB . LEU A 1 201 ? 42.592 -3.507 23.211 1.00 20.17 ? 217 LEU A CB 1 ATOM 1652 C CG . LEU A 1 201 ? 41.149 -3.044 23.446 1.00 20.19 ? 217 LEU A CG 1 ATOM 1653 C CD1 . LEU A 1 201 ? 40.793 -1.892 22.517 1.00 20.12 ? 217 LEU A CD1 1 ATOM 1654 C CD2 . LEU A 1 201 ? 40.160 -4.201 23.293 1.00 20.01 ? 217 LEU A CD2 1 ATOM 1655 N N . GLU A 1 202 ? 45.563 -4.557 23.875 1.00 21.24 ? 218 GLU A N 1 ATOM 1656 C CA . GLU A 1 202 ? 46.827 -5.273 23.612 1.00 21.88 ? 218 GLU A CA 1 ATOM 1657 C C . GLU A 1 202 ? 46.947 -6.542 24.469 1.00 21.79 ? 218 GLU A C 1 ATOM 1658 O O . GLU A 1 202 ? 47.345 -7.596 23.972 1.00 21.05 ? 218 GLU A O 1 ATOM 1659 C CB . GLU A 1 202 ? 48.065 -4.371 23.818 1.00 22.90 ? 218 GLU A CB 1 ATOM 1660 C CG . GLU A 1 202 ? 48.161 -3.156 22.878 1.00 24.60 ? 218 GLU A CG 1 ATOM 1661 C CD . GLU A 1 202 ? 48.596 -3.496 21.459 1.00 25.93 ? 218 GLU A CD 1 ATOM 1662 O OE1 . GLU A 1 202 ? 48.835 -4.688 21.167 1.00 26.97 ? 218 GLU A OE1 1 ATOM 1663 O OE2 . GLU A 1 202 ? 48.711 -2.560 20.623 1.00 26.14 ? 218 GLU A OE2 1 ATOM 1664 N N . ASP A 1 203 ? 46.607 -6.447 25.758 1.00 21.76 ? 219 ASP A N 1 ATOM 1665 C CA . ASP A 1 203 ? 46.709 -7.606 26.644 1.00 22.09 ? 219 ASP A CA 1 ATOM 1666 C C . ASP A 1 203 ? 45.724 -8.728 26.263 1.00 21.36 ? 219 ASP A C 1 ATOM 1667 O O . ASP A 1 203 ? 46.094 -9.895 26.218 1.00 21.52 ? 219 ASP A O 1 ATOM 1668 C CB . ASP A 1 203 ? 46.514 -7.209 28.125 1.00 23.27 ? 219 ASP A CB 1 ATOM 1669 C CG . ASP A 1 203 ? 47.634 -6.312 28.663 1.00 24.11 ? 219 ASP A CG 1 ATOM 1670 O OD1 . ASP A 1 203 ? 48.667 -6.130 27.998 1.00 24.62 ? 219 ASP A OD1 1 ATOM 1671 O OD2 . ASP A 1 203 ? 47.476 -5.771 29.776 1.00 25.67 ? 219 ASP A OD2 1 ATOM 1672 N N . ILE A 1 204 ? 44.476 -8.375 25.993 1.00 21.29 ? 220 ILE A N 1 ATOM 1673 C CA . ILE A 1 204 ? 43.469 -9.366 25.599 1.00 21.49 ? 220 ILE A CA 1 ATOM 1674 C C . ILE A 1 204 ? 43.852 -9.970 24.244 1.00 22.05 ? 220 ILE A C 1 ATOM 1675 O O . ILE A 1 204 ? 43.814 -11.191 24.066 1.00 22.46 ? 220 ILE A O 1 ATOM 1676 C CB . ILE A 1 204 ? 42.049 -8.759 25.548 1.00 21.21 ? 220 ILE A CB 1 ATOM 1677 C CG1 . ILE A 1 204 ? 41.555 -8.447 26.972 1.00 21.08 ? 220 ILE A CG1 1 ATOM 1678 C CG2 . ILE A 1 204 ? 41.071 -9.714 24.855 1.00 21.52 ? 220 ILE A CG2 1 ATOM 1679 C CD1 . ILE A 1 204 ? 40.375 -7.492 27.016 1.00 21.05 ? 220 ILE A CD1 1 ATOM 1680 N N . PHE A 1 205 ? 44.233 -9.120 23.298 1.00 22.07 ? 221 PHE A N 1 ATOM 1681 C CA . PHE A 1 205 ? 44.673 -9.628 22.006 1.00 21.97 ? 221 PHE A CA 1 ATOM 1682 C C . PHE A 1 205 ? 45.845 -10.631 22.119 1.00 22.43 ? 221 PHE A C 1 ATOM 1683 O O . PHE A 1 205 ? 45.814 -11.703 21.498 1.00 22.31 ? 221 PHE A O 1 ATOM 1684 C CB . PHE A 1 205 ? 44.974 -8.493 21.023 1.00 22.99 ? 221 PHE A CB 1 ATOM 1685 C CG . PHE A 1 205 ? 45.415 -8.987 19.678 1.00 23.58 ? 221 PHE A CG 1 ATOM 1686 C CD1 . PHE A 1 205 ? 44.498 -9.572 18.804 1.00 24.53 ? 221 PHE A CD1 1 ATOM 1687 C CD2 . PHE A 1 205 ? 46.755 -8.923 19.303 1.00 24.07 ? 221 PHE A CD2 1 ATOM 1688 C CE1 . PHE A 1 205 ? 44.910 -10.078 17.580 1.00 24.51 ? 221 PHE A CE1 1 ATOM 1689 C CE2 . PHE A 1 205 ? 47.171 -9.419 18.075 1.00 24.82 ? 221 PHE A CE2 1 ATOM 1690 C CZ . PHE A 1 205 ? 46.246 -9.995 17.207 1.00 25.08 ? 221 PHE A CZ 1 ATOM 1691 N N . ALA A 1 206 ? 46.855 -10.303 22.923 1.00 22.67 ? 222 ALA A N 1 ATOM 1692 C CA . ALA A 1 206 ? 47.994 -11.207 23.126 1.00 23.20 ? 222 ALA A CA 1 ATOM 1693 C C . ALA A 1 206 ? 47.585 -12.588 23.670 1.00 23.58 ? 222 ALA A C 1 ATOM 1694 O O . ALA A 1 206 ? 48.183 -13.595 23.306 1.00 22.96 ? 222 ALA A O 1 ATOM 1695 C CB . ALA A 1 206 ? 49.058 -10.560 24.007 1.00 23.09 ? 222 ALA A CB 1 ATOM 1696 N N . ASP A 1 207 ? 46.570 -12.631 24.536 1.00 24.87 ? 223 ASP A N 1 ATOM 1697 C CA . ASP A 1 207 ? 46.035 -13.894 25.056 1.00 25.31 ? 223 ASP A CA 1 ATOM 1698 C C . ASP A 1 207 ? 45.366 -14.762 23.992 1.00 25.62 ? 223 ASP A C 1 ATOM 1699 O O . ASP A 1 207 ? 45.435 -15.984 24.076 1.00 24.92 ? 223 ASP A O 1 ATOM 1700 C CB . ASP A 1 207 ? 45.027 -13.648 26.178 1.00 27.09 ? 223 ASP A CB 1 ATOM 1701 C CG . ASP A 1 207 ? 45.675 -13.113 27.441 1.00 27.93 ? 223 ASP A CG 1 ATOM 1702 O OD1 . ASP A 1 207 ? 46.896 -13.307 27.623 1.00 28.89 ? 223 ASP A OD1 1 ATOM 1703 O OD2 . ASP A 1 207 ? 44.957 -12.490 28.250 1.00 29.53 ? 223 ASP A OD2 1 ATOM 1704 N N . ILE A 1 208 ? 44.718 -14.135 23.007 1.00 25.06 ? 224 ILE A N 1 ATOM 1705 C CA . ILE A 1 208 ? 43.956 -14.872 21.986 1.00 25.80 ? 224 ILE A CA 1 ATOM 1706 C C . ILE A 1 208 ? 44.778 -15.136 20.719 1.00 24.89 ? 224 ILE A C 1 ATOM 1707 O O . ILE A 1 208 ? 44.454 -16.029 19.935 1.00 23.85 ? 224 ILE A O 1 ATOM 1708 C CB . ILE A 1 208 ? 42.633 -14.147 21.583 1.00 27.32 ? 224 ILE A CB 1 ATOM 1709 C CG1 . ILE A 1 208 ? 41.896 -13.567 22.794 1.00 29.35 ? 224 ILE A CG1 1 ATOM 1710 C CG2 . ILE A 1 208 ? 41.696 -15.085 20.832 1.00 28.50 ? 224 ILE A CG2 1 ATOM 1711 C CD1 . ILE A 1 208 ? 41.412 -14.589 23.809 1.00 32.18 ? 224 ILE A CD1 1 ATOM 1712 N N . ARG A 1 209 ? 45.850 -14.371 20.532 1.00 23.96 ? 225 ARG A N 1 ATOM 1713 C CA . ARG A 1 209 ? 46.681 -14.478 19.321 1.00 24.20 ? 225 ARG A CA 1 ATOM 1714 C C . ARG A 1 209 ? 47.174 -15.910 19.006 1.00 23.31 ? 225 ARG A C 1 ATOM 1715 O O . ARG A 1 209 ? 47.142 -16.312 17.838 1.00 23.84 ? 225 ARG A O 1 ATOM 1716 C CB . ARG A 1 209 ? 47.855 -13.488 19.398 1.00 25.05 ? 225 ARG A CB 1 ATOM 1717 C CG . ARG A 1 209 ? 48.608 -13.262 18.106 1.00 27.92 ? 225 ARG A CG 1 ATOM 1718 C CD . ARG A 1 209 ? 49.541 -12.071 18.257 1.00 29.15 ? 225 ARG A CD 1 ATOM 1719 N NE . ARG A 1 209 ? 49.976 -11.590 16.947 1.00 30.27 ? 225 ARG A NE 1 ATOM 1720 C CZ . ARG A 1 209 ? 50.634 -10.452 16.727 1.00 31.28 ? 225 ARG A CZ 1 ATOM 1721 N NH1 . ARG A 1 209 ? 50.935 -9.642 17.738 1.00 31.46 ? 225 ARG A NH1 1 ATOM 1722 N NH2 . ARG A 1 209 ? 50.995 -10.125 15.487 1.00 29.96 ? 225 ARG A NH2 1 ATOM 1723 N N . PRO A 1 210 ? 47.623 -16.684 20.024 1.00 23.09 ? 226 PRO A N 1 ATOM 1724 C CA . PRO A 1 210 ? 48.085 -18.050 19.713 1.00 23.00 ? 226 PRO A CA 1 ATOM 1725 C C . PRO A 1 210 ? 47.003 -18.942 19.086 1.00 22.87 ? 226 PRO A C 1 ATOM 1726 O O . PRO A 1 210 ? 47.319 -19.733 18.185 1.00 24.35 ? 226 PRO A O 1 ATOM 1727 C CB . PRO A 1 210 ? 48.527 -18.600 21.082 1.00 23.14 ? 226 PRO A CB 1 ATOM 1728 C CG . PRO A 1 210 ? 48.851 -17.378 21.893 1.00 23.38 ? 226 PRO A CG 1 ATOM 1729 C CD . PRO A 1 210 ? 47.817 -16.373 21.461 1.00 23.09 ? 226 PRO A CD 1 ATOM 1730 N N . LEU A 1 211 ? 45.748 -18.798 19.529 1.00 22.14 ? 227 LEU A N 1 ATOM 1731 C CA . LEU A 1 211 ? 44.633 -19.534 18.911 1.00 21.20 ? 227 LEU A CA 1 ATOM 1732 C C . LEU A 1 211 ? 44.462 -19.109 17.460 1.00 20.70 ? 227 LEU A C 1 ATOM 1733 O O . LEU A 1 211 ? 44.310 -19.961 16.570 1.00 20.05 ? 227 LEU A O 1 ATOM 1734 C CB . LEU A 1 211 ? 43.311 -19.347 19.676 1.00 21.09 ? 227 LEU A CB 1 ATOM 1735 C CG . LEU A 1 211 ? 42.054 -20.044 19.131 1.00 20.93 ? 227 LEU A CG 1 ATOM 1736 C CD1 . LEU A 1 211 ? 42.256 -21.556 18.968 1.00 21.23 ? 227 LEU A CD1 1 ATOM 1737 C CD2 . LEU A 1 211 ? 40.816 -19.756 19.980 1.00 21.21 ? 227 LEU A CD2 1 ATOM 1738 N N . TYR A 1 212 ? 44.510 -17.794 17.221 1.00 19.99 ? 228 TYR A N 1 ATOM 1739 C CA . TYR A 1 212 ? 44.444 -17.285 15.841 1.00 19.43 ? 228 TYR A CA 1 ATOM 1740 C C . TYR A 1 212 ? 45.508 -17.936 14.947 1.00 19.72 ? 228 TYR A C 1 ATOM 1741 O O . TYR A 1 212 ? 45.222 -18.335 13.800 1.00 21.01 ? 228 TYR A O 1 ATOM 1742 C CB . TYR A 1 212 ? 44.557 -15.740 15.758 1.00 18.37 ? 228 TYR A CB 1 ATOM 1743 C CG . TYR A 1 212 ? 44.589 -15.296 14.294 1.00 18.07 ? 228 TYR A CG 1 ATOM 1744 C CD1 . TYR A 1 212 ? 43.447 -15.386 13.516 1.00 18.18 ? 228 TYR A CD1 1 ATOM 1745 C CD2 . TYR A 1 212 ? 45.773 -14.841 13.695 1.00 17.68 ? 228 TYR A CD2 1 ATOM 1746 C CE1 . TYR A 1 212 ? 43.458 -15.027 12.169 1.00 17.74 ? 228 TYR A CE1 1 ATOM 1747 C CE2 . TYR A 1 212 ? 45.801 -14.486 12.343 1.00 17.72 ? 228 TYR A CE2 1 ATOM 1748 C CZ . TYR A 1 212 ? 44.637 -14.575 11.595 1.00 17.39 ? 228 TYR A CZ 1 ATOM 1749 O OH . TYR A 1 212 ? 44.614 -14.217 10.255 1.00 17.03 ? 228 TYR A OH 1 ATOM 1750 N N . GLN A 1 213 ? 46.734 -18.010 15.456 1.00 19.61 ? 229 GLN A N 1 ATOM 1751 C CA . GLN A 1 213 ? 47.849 -18.576 14.707 1.00 20.45 ? 229 GLN A CA 1 ATOM 1752 C C . GLN A 1 213 ? 47.655 -20.067 14.377 1.00 20.36 ? 229 GLN A C 1 ATOM 1753 O O . GLN A 1 213 ? 48.012 -20.504 13.285 1.00 19.50 ? 229 GLN A O 1 ATOM 1754 C CB . GLN A 1 213 ? 49.191 -18.262 15.383 1.00 20.71 ? 229 GLN A CB 1 ATOM 1755 C CG . GLN A 1 213 ? 49.375 -16.761 15.559 0.50 21.77 ? 229 GLN A CG 1 ATOM 1756 C CD . GLN A 1 213 ? 50.756 -16.269 15.218 0.50 23.29 ? 229 GLN A CD 1 ATOM 1757 O OE1 . GLN A 1 213 ? 50.915 -15.189 14.665 0.50 24.45 ? 229 GLN A OE1 1 ATOM 1758 N NE2 . GLN A 1 213 ? 51.764 -17.055 15.543 1.00 25.26 ? 229 GLN A NE2 1 ATOM 1759 N N . GLN A 1 214 ? 47.053 -20.825 15.297 1.00 19.87 ? 230 GLN A N 1 ATOM 1760 C CA . GLN A 1 214 ? 46.648 -22.223 15.020 1.00 20.28 ? 230 GLN A CA 1 ATOM 1761 C C . GLN A 1 214 ? 45.593 -22.332 13.904 1.00 20.68 ? 230 GLN A C 1 ATOM 1762 O O . GLN A 1 214 ? 45.692 -23.200 13.029 1.00 21.19 ? 230 GLN A O 1 ATOM 1763 C CB . GLN A 1 214 ? 46.150 -22.913 16.300 1.00 20.38 ? 230 GLN A CB 1 ATOM 1764 C CG . GLN A 1 214 ? 47.202 -22.999 17.398 1.00 20.14 ? 230 GLN A CG 1 ATOM 1765 C CD . GLN A 1 214 ? 48.333 -23.958 17.053 1.00 20.33 ? 230 GLN A CD 1 ATOM 1766 O OE1 . GLN A 1 214 ? 48.099 -25.108 16.644 1.00 20.78 ? 230 GLN A OE1 1 ATOM 1767 N NE2 . GLN A 1 214 ? 49.562 -23.492 17.205 1.00 19.72 ? 230 GLN A NE2 1 ATOM 1768 N N . ILE A 1 215 ? 44.587 -21.451 13.933 1.00 20.56 ? 231 ILE A N 1 ATOM 1769 C CA . ILE A 1 215 ? 43.535 -21.438 12.904 1.00 20.40 ? 231 ILE A CA 1 ATOM 1770 C C . ILE A 1 215 ? 44.149 -21.069 11.545 1.00 19.78 ? 231 ILE A C 1 ATOM 1771 O O . ILE A 1 215 ? 43.875 -21.708 10.516 1.00 19.55 ? 231 ILE A O 1 ATOM 1772 C CB . ILE A 1 215 ? 42.396 -20.446 13.285 1.00 20.16 ? 231 ILE A CB 1 ATOM 1773 C CG1 . ILE A 1 215 ? 41.657 -20.943 14.541 1.00 20.88 ? 231 ILE A CG1 1 ATOM 1774 C CG2 . ILE A 1 215 ? 41.407 -20.257 12.140 1.00 20.85 ? 231 ILE A CG2 1 ATOM 1775 C CD1 . ILE A 1 215 ? 40.871 -19.873 15.279 1.00 20.85 ? 231 ILE A CD1 1 ATOM 1776 N N . HIS A 1 216 ? 44.973 -20.026 11.558 1.00 19.38 ? 232 HIS A N 1 ATOM 1777 C CA . HIS A 1 216 ? 45.664 -19.558 10.352 1.00 19.35 ? 232 HIS A CA 1 ATOM 1778 C C . HIS A 1 216 ? 46.460 -20.705 9.719 1.00 19.50 ? 232 HIS A C 1 ATOM 1779 O O . HIS A 1 216 ? 46.351 -20.956 8.513 1.00 18.95 ? 232 HIS A O 1 ATOM 1780 C CB . HIS A 1 216 ? 46.570 -18.377 10.711 1.00 19.09 ? 232 HIS A CB 1 ATOM 1781 C CG . HIS A 1 216 ? 47.397 -17.865 9.573 1.00 19.23 ? 232 HIS A CG 1 ATOM 1782 N ND1 . HIS A 1 216 ? 48.547 -18.493 9.149 1.00 19.14 ? 232 HIS A ND1 1 ATOM 1783 C CD2 . HIS A 1 216 ? 47.271 -16.752 8.812 1.00 19.33 ? 232 HIS A CD2 1 ATOM 1784 C CE1 . HIS A 1 216 ? 49.075 -17.805 8.147 1.00 19.80 ? 232 HIS A CE1 1 ATOM 1785 N NE2 . HIS A 1 216 ? 48.320 -16.742 7.926 1.00 19.11 ? 232 HIS A NE2 1 ATOM 1786 N N . GLY A 1 217 ? 47.241 -21.405 10.535 1.00 20.02 ? 233 GLY A N 1 ATOM 1787 C CA . GLY A 1 217 ? 48.085 -22.506 10.034 1.00 20.76 ? 233 GLY A CA 1 ATOM 1788 C C . GLY A 1 217 ? 47.268 -23.620 9.398 1.00 20.76 ? 233 GLY A C 1 ATOM 1789 O O . GLY A 1 217 ? 47.608 -24.109 8.314 1.00 20.82 ? 233 GLY A O 1 ATOM 1790 N N . TYR A 1 218 ? 46.175 -24.005 10.067 1.00 20.90 ? 234 TYR A N 1 ATOM 1791 C CA . TYR A 1 218 ? 45.321 -25.080 9.576 1.00 21.26 ? 234 TYR A CA 1 ATOM 1792 C C . TYR A 1 218 ? 44.621 -24.687 8.262 1.00 21.20 ? 234 TYR A C 1 ATOM 1793 O O . TYR A 1 218 ? 44.622 -25.459 7.289 1.00 21.84 ? 234 TYR A O 1 ATOM 1794 C CB . TYR A 1 218 ? 44.306 -25.516 10.650 1.00 21.86 ? 234 TYR A CB 1 ATOM 1795 C CG . TYR A 1 218 ? 43.560 -26.765 10.250 1.00 22.48 ? 234 TYR A CG 1 ATOM 1796 C CD1 . TYR A 1 218 ? 44.164 -28.017 10.346 1.00 22.60 ? 234 TYR A CD1 1 ATOM 1797 C CD2 . TYR A 1 218 ? 42.261 -26.691 9.743 1.00 23.12 ? 234 TYR A CD2 1 ATOM 1798 C CE1 . TYR A 1 218 ? 43.494 -29.165 9.962 1.00 23.72 ? 234 TYR A CE1 1 ATOM 1799 C CE2 . TYR A 1 218 ? 41.577 -27.838 9.362 1.00 24.27 ? 234 TYR A CE2 1 ATOM 1800 C CZ . TYR A 1 218 ? 42.203 -29.068 9.473 1.00 24.32 ? 234 TYR A CZ 1 ATOM 1801 O OH . TYR A 1 218 ? 41.541 -30.205 9.087 1.00 25.62 ? 234 TYR A OH 1 ATOM 1802 N N . VAL A 1 219 ? 44.073 -23.471 8.213 1.00 20.58 ? 235 VAL A N 1 ATOM 1803 C CA . VAL A 1 219 ? 43.453 -22.952 6.983 1.00 20.54 ? 235 VAL A CA 1 ATOM 1804 C C . VAL A 1 219 ? 44.431 -22.952 5.784 1.00 20.71 ? 235 VAL A C 1 ATOM 1805 O O . VAL A 1 219 ? 44.069 -23.392 4.681 1.00 21.08 ? 235 VAL A O 1 ATOM 1806 C CB . VAL A 1 219 ? 42.789 -21.557 7.196 1.00 20.11 ? 235 VAL A CB 1 ATOM 1807 C CG1 . VAL A 1 219 ? 42.399 -20.923 5.857 1.00 19.86 ? 235 VAL A CG1 1 ATOM 1808 C CG2 . VAL A 1 219 ? 41.542 -21.701 8.060 1.00 19.93 ? 235 VAL A CG2 1 ATOM 1809 N N . ARG A 1 220 ? 45.652 -22.465 6.002 1.00 20.35 ? 236 ARG A N 1 ATOM 1810 C CA . ARG A 1 220 ? 46.686 -22.440 4.946 1.00 20.66 ? 236 ARG A CA 1 ATOM 1811 C C . ARG A 1 220 ? 47.022 -23.856 4.459 1.00 21.10 ? 236 ARG A C 1 ATOM 1812 O O . ARG A 1 220 ? 47.147 -24.101 3.259 1.00 20.51 ? 236 ARG A O 1 ATOM 1813 C CB . ARG A 1 220 ? 47.944 -21.703 5.442 1.00 20.22 ? 236 ARG A CB 1 ATOM 1814 C CG . ARG A 1 220 ? 49.143 -21.741 4.501 1.00 20.05 ? 236 ARG A CG 1 ATOM 1815 C CD . ARG A 1 220 ? 50.276 -20.853 4.983 1.00 19.72 ? 236 ARG A CD 1 ATOM 1816 N NE . ARG A 1 220 ? 50.683 -21.237 6.334 1.00 19.09 ? 236 ARG A NE 1 ATOM 1817 C CZ . ARG A 1 220 ? 51.517 -20.562 7.123 1.00 19.64 ? 236 ARG A CZ 1 ATOM 1818 N NH1 . ARG A 1 220 ? 52.098 -19.434 6.721 1.00 19.33 ? 236 ARG A NH1 1 ATOM 1819 N NH2 . ARG A 1 220 ? 51.782 -21.040 8.337 1.00 18.33 ? 236 ARG A NH2 1 ATOM 1820 N N . PHE A 1 221 ? 47.163 -24.782 5.403 1.00 21.66 ? 237 PHE A N 1 ATOM 1821 C CA . PHE A 1 221 ? 47.363 -26.200 5.103 1.00 22.69 ? 237 PHE A CA 1 ATOM 1822 C C . PHE A 1 221 ? 46.249 -26.730 4.196 1.00 22.97 ? 237 PHE A C 1 ATOM 1823 O O . PHE A 1 221 ? 46.515 -27.321 3.146 1.00 23.00 ? 237 PHE A O 1 ATOM 1824 C CB . PHE A 1 221 ? 47.463 -26.984 6.421 1.00 23.36 ? 237 PHE A CB 1 ATOM 1825 C CG . PHE A 1 221 ? 47.205 -28.468 6.294 1.00 24.47 ? 237 PHE A CG 1 ATOM 1826 C CD1 . PHE A 1 221 ? 48.067 -29.290 5.557 1.00 24.67 ? 237 PHE A CD1 1 ATOM 1827 C CD2 . PHE A 1 221 ? 46.116 -29.048 6.946 1.00 24.37 ? 237 PHE A CD2 1 ATOM 1828 C CE1 . PHE A 1 221 ? 47.828 -30.659 5.464 1.00 25.33 ? 237 PHE A CE1 1 ATOM 1829 C CE2 . PHE A 1 221 ? 45.872 -30.414 6.857 1.00 25.12 ? 237 PHE A CE2 1 ATOM 1830 C CZ . PHE A 1 221 ? 46.736 -31.221 6.122 1.00 25.38 ? 237 PHE A CZ 1 ATOM 1831 N N . ARG A 1 222 ? 45.000 -26.476 4.573 1.00 22.81 ? 238 ARG A N 1 ATOM 1832 C CA . ARG A 1 222 ? 43.866 -26.952 3.783 1.00 23.18 ? 238 ARG A CA 1 ATOM 1833 C C . ARG A 1 222 ? 43.741 -26.257 2.425 1.00 23.10 ? 238 ARG A C 1 ATOM 1834 O O . ARG A 1 222 ? 43.340 -26.880 1.451 1.00 24.13 ? 238 ARG A O 1 ATOM 1835 C CB . ARG A 1 222 ? 42.569 -26.868 4.597 1.00 23.87 ? 238 ARG A CB 1 ATOM 1836 C CG . ARG A 1 222 ? 42.577 -27.793 5.824 1.00 23.96 ? 238 ARG A CG 1 ATOM 1837 C CD . ARG A 1 222 ? 42.553 -29.272 5.422 1.00 25.02 ? 238 ARG A CD 1 ATOM 1838 N NE . ARG A 1 222 ? 41.326 -29.564 4.684 1.00 26.11 ? 238 ARG A NE 1 ATOM 1839 C CZ . ARG A 1 222 ? 40.165 -29.859 5.259 1.00 27.28 ? 238 ARG A CZ 1 ATOM 1840 N NH1 . ARG A 1 222 ? 40.077 -29.944 6.581 1.00 27.38 ? 238 ARG A NH1 1 ATOM 1841 N NH2 . ARG A 1 222 ? 39.090 -30.066 4.512 1.00 28.31 ? 238 ARG A NH2 1 ATOM 1842 N N . LEU A 1 223 ? 44.106 -24.979 2.349 1.00 22.73 ? 239 LEU A N 1 ATOM 1843 C CA . LEU A 1 223 ? 44.108 -24.269 1.059 1.00 22.76 ? 239 LEU A CA 1 ATOM 1844 C C . LEU A 1 223 ? 45.159 -24.797 0.071 1.00 23.08 ? 239 LEU A C 1 ATOM 1845 O O . LEU A 1 223 ? 44.919 -24.797 -1.136 1.00 22.46 ? 239 LEU A O 1 ATOM 1846 C CB . LEU A 1 223 ? 44.263 -22.746 1.244 1.00 22.48 ? 239 LEU A CB 1 ATOM 1847 C CG . LEU A 1 223 ? 43.059 -21.991 1.851 1.00 22.24 ? 239 LEU A CG 1 ATOM 1848 C CD1 . LEU A 1 223 ? 43.453 -20.560 2.200 1.00 22.10 ? 239 LEU A CD1 1 ATOM 1849 C CD2 . LEU A 1 223 ? 41.849 -22.003 0.931 1.00 22.23 ? 239 LEU A CD2 1 ATOM 1850 N N . ARG A 1 224 ? 46.310 -25.230 0.583 1.00 23.18 ? 240 ARG A N 1 ATOM 1851 C CA . ARG A 1 224 ? 47.367 -25.842 -0.253 1.00 24.13 ? 240 ARG A CA 1 ATOM 1852 C C . ARG A 1 224 ? 46.869 -27.120 -0.941 1.00 24.97 ? 240 ARG A C 1 ATOM 1853 O O . ARG A 1 224 ? 47.151 -27.354 -2.121 1.00 25.40 ? 240 ARG A O 1 ATOM 1854 C CB . ARG A 1 224 ? 48.605 -26.145 0.599 1.00 24.40 ? 240 ARG A CB 1 ATOM 1855 C CG . ARG A 1 224 ? 49.366 -24.902 1.046 1.00 24.13 ? 240 ARG A CG 1 ATOM 1856 C CD . ARG A 1 224 ? 50.546 -25.227 1.944 1.00 24.11 ? 240 ARG A CD 1 ATOM 1857 N NE . ARG A 1 224 ? 51.495 -26.150 1.318 1.00 24.08 ? 240 ARG A NE 1 ATOM 1858 C CZ . ARG A 1 224 ? 52.166 -27.101 1.971 1.00 24.48 ? 240 ARG A CZ 1 ATOM 1859 N NH1 . ARG A 1 224 ? 51.992 -27.262 3.274 1.00 23.32 ? 240 ARG A NH1 1 ATOM 1860 N NH2 . ARG A 1 224 ? 53.011 -27.899 1.320 1.00 24.17 ? 240 ARG A NH2 1 ATOM 1861 N N . LYS A 1 225 ? 46.105 -27.924 -0.203 1.00 25.67 ? 241 LYS A N 1 ATOM 1862 C CA . LYS A 1 225 ? 45.520 -29.159 -0.730 1.00 26.68 ? 241 LYS A CA 1 ATOM 1863 C C . LYS A 1 225 ? 44.518 -28.853 -1.833 1.00 26.69 ? 241 LYS A C 1 ATOM 1864 O O . LYS A 1 225 ? 44.430 -29.592 -2.813 1.00 28.36 ? 241 LYS A O 1 ATOM 1865 C CB . LYS A 1 225 ? 44.856 -29.975 0.384 1.00 27.20 ? 241 LYS A CB 1 ATOM 1866 C CG . LYS A 1 225 ? 45.822 -30.415 1.483 1.00 28.82 ? 241 LYS A CG 1 ATOM 1867 C CD . LYS A 1 225 ? 45.157 -31.354 2.483 1.00 30.80 ? 241 LYS A CD 1 ATOM 1868 C CE . LYS A 1 225 ? 44.910 -32.722 1.856 1.00 32.65 ? 241 LYS A CE 1 ATOM 1869 N NZ . LYS A 1 225 ? 44.614 -33.746 2.891 1.00 34.12 ? 241 LYS A NZ 1 ATOM 1870 N N . HIS A 1 226 ? 43.779 -27.749 -1.686 1.00 25.86 ? 242 HIS A N 1 ATOM 1871 C CA . HIS A 1 226 ? 42.786 -27.350 -2.699 1.00 25.04 ? 242 HIS A CA 1 ATOM 1872 C C . HIS A 1 226 ? 43.413 -26.693 -3.938 1.00 24.29 ? 242 HIS A C 1 ATOM 1873 O O . HIS A 1 226 ? 43.131 -27.100 -5.071 1.00 24.42 ? 242 HIS A O 1 ATOM 1874 C CB . HIS A 1 226 ? 41.716 -26.436 -2.079 1.00 24.98 ? 242 HIS A CB 1 ATOM 1875 C CG . HIS A 1 226 ? 40.547 -26.166 -2.976 1.00 25.85 ? 242 HIS A CG 1 ATOM 1876 N ND1 . HIS A 1 226 ? 39.413 -26.951 -2.977 1.00 26.44 ? 242 HIS A ND1 1 ATOM 1877 C CD2 . HIS A 1 226 ? 40.329 -25.191 -3.892 1.00 25.94 ? 242 HIS A CD2 1 ATOM 1878 C CE1 . HIS A 1 226 ? 38.554 -26.478 -3.863 1.00 26.25 ? 242 HIS A CE1 1 ATOM 1879 N NE2 . HIS A 1 226 ? 39.081 -25.406 -4.426 1.00 26.13 ? 242 HIS A NE2 1 ATOM 1880 N N . TYR A 1 227 ? 44.232 -25.660 -3.739 1.00 23.58 ? 243 TYR A N 1 ATOM 1881 C CA . TYR A 1 227 ? 44.768 -24.883 -4.883 1.00 23.02 ? 243 TYR A CA 1 ATOM 1882 C C . TYR A 1 227 ? 46.147 -25.337 -5.385 1.00 23.16 ? 243 TYR A C 1 ATOM 1883 O O . TYR A 1 227 ? 46.524 -25.045 -6.542 1.00 22.74 ? 243 TYR A O 1 ATOM 1884 C CB . TYR A 1 227 ? 44.819 -23.388 -4.553 1.00 23.02 ? 243 TYR A CB 1 ATOM 1885 C CG . TYR A 1 227 ? 43.459 -22.721 -4.413 1.00 23.02 ? 243 TYR A CG 1 ATOM 1886 C CD1 . TYR A 1 227 ? 42.788 -22.251 -5.527 1.00 22.96 ? 243 TYR A CD1 1 ATOM 1887 C CD2 . TYR A 1 227 ? 42.858 -22.545 -3.157 1.00 22.46 ? 243 TYR A CD2 1 ATOM 1888 C CE1 . TYR A 1 227 ? 41.553 -21.632 -5.423 1.00 22.88 ? 243 TYR A CE1 1 ATOM 1889 C CE2 . TYR A 1 227 ? 41.614 -21.918 -3.042 1.00 22.23 ? 243 TYR A CE2 1 ATOM 1890 C CZ . TYR A 1 227 ? 40.973 -21.462 -4.182 1.00 22.68 ? 243 TYR A CZ 1 ATOM 1891 O OH . TYR A 1 227 ? 39.748 -20.840 -4.125 1.00 22.58 ? 243 TYR A OH 1 ATOM 1892 N N . GLY A 1 228 ? 46.886 -26.042 -4.532 1.00 22.70 ? 244 GLY A N 1 ATOM 1893 C CA . GLY A 1 228 ? 48.252 -26.472 -4.840 1.00 23.32 ? 244 GLY A CA 1 ATOM 1894 C C . GLY A 1 228 ? 49.299 -25.455 -4.437 1.00 23.52 ? 244 GLY A C 1 ATOM 1895 O O . GLY A 1 228 ? 48.979 -24.284 -4.199 1.00 23.34 ? 244 GLY A O 1 ATOM 1896 N N . ASP A 1 229 ? 50.553 -25.894 -4.372 1.00 24.36 ? 245 ASP A N 1 ATOM 1897 C CA . ASP A 1 229 ? 51.639 -25.075 -3.798 1.00 25.25 ? 245 ASP A CA 1 ATOM 1898 C C . ASP A 1 229 ? 52.120 -23.920 -4.693 1.00 24.73 ? 245 ASP A C 1 ATOM 1899 O O . ASP A 1 229 ? 52.829 -23.023 -4.234 1.00 24.59 ? 245 ASP A O 1 ATOM 1900 C CB . ASP A 1 229 ? 52.817 -25.962 -3.361 1.00 27.29 ? 245 ASP A CB 1 ATOM 1901 C CG . ASP A 1 229 ? 52.542 -26.696 -2.057 1.00 29.38 ? 245 ASP A CG 1 ATOM 1902 O OD1 . ASP A 1 229 ? 51.551 -27.448 -1.970 1.00 31.51 ? 245 ASP A OD1 1 ATOM 1903 O OD2 . ASP A 1 229 ? 53.314 -26.513 -1.101 1.00 31.94 ? 245 ASP A OD2 1 ATOM 1904 N N . ALA A 1 230 ? 51.729 -23.931 -5.961 1.00 23.62 ? 246 ALA A N 1 ATOM 1905 C CA . ALA A 1 230 ? 52.001 -22.787 -6.833 1.00 23.65 ? 246 ALA A CA 1 ATOM 1906 C C . ALA A 1 230 ? 51.178 -21.543 -6.430 1.00 23.15 ? 246 ALA A C 1 ATOM 1907 O O . ALA A 1 230 ? 51.582 -20.419 -6.710 1.00 24.17 ? 246 ALA A O 1 ATOM 1908 C CB . ALA A 1 230 ? 51.731 -23.154 -8.283 1.00 23.74 ? 246 ALA A CB 1 ATOM 1909 N N . VAL A 1 231 ? 50.046 -21.756 -5.758 1.00 21.71 ? 247 VAL A N 1 ATOM 1910 C CA . VAL A 1 231 ? 49.119 -20.674 -5.359 1.00 20.61 ? 247 VAL A CA 1 ATOM 1911 C C . VAL A 1 231 ? 49.312 -20.309 -3.880 1.00 20.74 ? 247 VAL A C 1 ATOM 1912 O O . VAL A 1 231 ? 49.254 -19.135 -3.500 1.00 20.82 ? 247 VAL A O 1 ATOM 1913 C CB . VAL A 1 231 ? 47.652 -21.100 -5.608 1.00 20.28 ? 247 VAL A CB 1 ATOM 1914 C CG1 . VAL A 1 231 ? 46.663 -20.000 -5.222 1.00 19.55 ? 247 VAL A CG1 1 ATOM 1915 C CG2 . VAL A 1 231 ? 47.454 -21.461 -7.085 1.00 20.41 ? 247 VAL A CG2 1 ATOM 1916 N N . VAL A 1 232 ? 49.547 -21.325 -3.062 1.00 20.17 ? 248 VAL A N 1 ATOM 1917 C CA . VAL A 1 232 ? 49.631 -21.135 -1.599 1.00 20.06 ? 248 VAL A CA 1 ATOM 1918 C C . VAL A 1 232 ? 50.917 -21.775 -1.085 1.00 21.21 ? 248 VAL A C 1 ATOM 1919 O O . VAL A 1 232 ? 51.118 -22.992 -1.239 1.00 22.13 ? 248 VAL A O 1 ATOM 1920 C CB . VAL A 1 232 ? 48.402 -21.742 -0.873 1.00 19.55 ? 248 VAL A CB 1 ATOM 1921 C CG1 . VAL A 1 232 ? 48.495 -21.491 0.639 1.00 18.24 ? 248 VAL A CG1 1 ATOM 1922 C CG2 . VAL A 1 232 ? 47.089 -21.171 -1.388 1.00 18.68 ? 248 VAL A CG2 1 ATOM 1923 N N . SER A 1 233 ? 51.796 -20.969 -0.486 1.00 21.94 ? 249 SER A N 1 ATOM 1924 C CA . SER A 1 233 ? 53.044 -21.494 0.060 1.00 22.91 ? 249 SER A CA 1 ATOM 1925 C C . SER A 1 233 ? 52.806 -21.952 1.493 1.00 22.63 ? 249 SER A C 1 ATOM 1926 O O . SER A 1 233 ? 51.862 -21.495 2.140 1.00 21.46 ? 249 SER A O 1 ATOM 1927 C CB . SER A 1 233 ? 54.165 -20.453 0.004 1.00 23.96 ? 249 SER A CB 1 ATOM 1928 O OG . SER A 1 233 ? 54.081 -19.549 1.086 1.00 25.50 ? 249 SER A OG 1 ATOM 1929 N N . GLU A 1 234 ? 53.648 -22.864 1.969 1.00 22.62 ? 250 GLU A N 1 ATOM 1930 C CA . GLU A 1 234 ? 53.545 -23.367 3.342 1.00 22.89 ? 250 GLU A CA 1 ATOM 1931 C C . GLU A 1 234 ? 53.983 -22.329 4.373 1.00 22.42 ? 250 GLU A C 1 ATOM 1932 O O . GLU A 1 234 ? 53.467 -22.304 5.506 1.00 22.51 ? 250 GLU A O 1 ATOM 1933 C CB . GLU A 1 234 ? 54.386 -24.640 3.505 1.00 24.26 ? 250 GLU A CB 1 ATOM 1934 C CG . GLU A 1 234 ? 54.399 -25.208 4.927 1.00 24.98 ? 250 GLU A CG 1 ATOM 1935 C CD . GLU A 1 234 ? 55.259 -26.449 5.062 1.00 26.65 ? 250 GLU A CD 1 ATOM 1936 O OE1 . GLU A 1 234 ? 56.290 -26.535 4.362 1.00 27.61 ? 250 GLU A OE1 1 ATOM 1937 O OE2 . GLU A 1 234 ? 54.909 -27.346 5.866 1.00 27.03 ? 250 GLU A OE2 1 ATOM 1938 N N . THR A 1 235 ? 54.950 -21.493 4.006 1.00 22.24 ? 251 THR A N 1 ATOM 1939 C CA . THR A 1 235 ? 55.625 -20.656 5.006 1.00 22.26 ? 251 THR A CA 1 ATOM 1940 C C . THR A 1 235 ? 55.269 -19.165 4.908 1.00 21.35 ? 251 THR A C 1 ATOM 1941 O O . THR A 1 235 ? 55.566 -18.406 5.820 1.00 20.60 ? 251 THR A O 1 ATOM 1942 C CB . THR A 1 235 ? 57.162 -20.839 4.954 1.00 22.54 ? 251 THR A CB 1 ATOM 1943 O OG1 . THR A 1 235 ? 57.614 -20.618 3.608 1.00 24.21 ? 251 THR A OG1 1 ATOM 1944 C CG2 . THR A 1 235 ? 57.549 -22.266 5.364 1.00 22.94 ? 251 THR A CG2 1 ATOM 1945 N N . GLY A 1 236 ? 54.662 -18.741 3.798 1.00 20.37 ? 252 GLY A N 1 ATOM 1946 C CA . GLY A 1 236 ? 54.322 -17.319 3.625 1.00 19.48 ? 252 GLY A CA 1 ATOM 1947 C C . GLY A 1 236 ? 52.907 -16.934 4.053 1.00 18.60 ? 252 GLY A C 1 ATOM 1948 O O . GLY A 1 236 ? 52.089 -17.807 4.352 1.00 18.74 ? 252 GLY A O 1 ATOM 1949 N N . PRO A 1 237 ? 52.603 -15.617 4.073 1.00 18.32 ? 253 PRO A N 1 ATOM 1950 C CA . PRO A 1 237 ? 51.234 -15.149 4.329 1.00 18.34 ? 253 PRO A CA 1 ATOM 1951 C C . PRO A 1 237 ? 50.254 -15.741 3.331 1.00 18.97 ? 253 PRO A C 1 ATOM 1952 O O . PRO A 1 237 ? 50.639 -15.995 2.184 1.00 19.48 ? 253 PRO A O 1 ATOM 1953 C CB . PRO A 1 237 ? 51.317 -13.633 4.096 1.00 18.19 ? 253 PRO A CB 1 ATOM 1954 C CG . PRO A 1 237 ? 52.772 -13.287 4.193 1.00 17.99 ? 253 PRO A CG 1 ATOM 1955 C CD . PRO A 1 237 ? 53.548 -14.510 3.827 1.00 18.04 ? 253 PRO A CD 1 ATOM 1956 N N . ILE A 1 238 ? 49.006 -15.934 3.741 1.00 18.72 ? 254 ILE A N 1 ATOM 1957 C CA . ILE A 1 238 ? 47.957 -16.451 2.845 1.00 19.08 ? 254 ILE A CA 1 ATOM 1958 C C . ILE A 1 238 ? 47.546 -15.398 1.801 1.00 18.84 ? 254 ILE A C 1 ATOM 1959 O O . ILE A 1 238 ? 47.293 -14.244 2.150 1.00 18.54 ? 254 ILE A O 1 ATOM 1960 C CB . ILE A 1 238 ? 46.715 -16.936 3.650 1.00 19.44 ? 254 ILE A CB 1 ATOM 1961 C CG1 . ILE A 1 238 ? 47.131 -17.979 4.705 1.00 19.28 ? 254 ILE A CG1 1 ATOM 1962 C CG2 . ILE A 1 238 ? 45.631 -17.479 2.710 1.00 19.57 ? 254 ILE A CG2 1 ATOM 1963 C CD1 . ILE A 1 238 ? 46.026 -18.390 5.669 1.00 19.74 ? 254 ILE A CD1 1 ATOM 1964 N N . PRO A 1 239 ? 47.508 -15.778 0.500 1.00 18.87 ? 255 PRO A N 1 ATOM 1965 C CA . PRO A 1 239 ? 46.922 -14.857 -0.478 1.00 18.82 ? 255 PRO A CA 1 ATOM 1966 C C . PRO A 1 239 ? 45.454 -14.571 -0.143 1.00 18.77 ? 255 PRO A C 1 ATOM 1967 O O . PRO A 1 239 ? 44.620 -15.483 -0.080 1.00 18.47 ? 255 PRO A O 1 ATOM 1968 C CB . PRO A 1 239 ? 47.073 -15.607 -1.815 1.00 18.72 ? 255 PRO A CB 1 ATOM 1969 C CG . PRO A 1 239 ? 48.193 -16.578 -1.585 1.00 18.80 ? 255 PRO A CG 1 ATOM 1970 C CD . PRO A 1 239 ? 48.043 -16.998 -0.137 1.00 18.91 ? 255 PRO A CD 1 ATOM 1971 N N . MET A 1 240 ? 45.155 -13.299 0.087 1.00 19.12 ? 256 MET A N 1 ATOM 1972 C CA . MET A 1 240 ? 43.897 -12.905 0.719 1.00 19.33 ? 256 MET A CA 1 ATOM 1973 C C . MET A 1 240 ? 42.642 -13.145 -0.120 1.00 19.43 ? 256 MET A C 1 ATOM 1974 O O . MET A 1 240 ? 41.544 -13.293 0.420 1.00 19.28 ? 256 MET A O 1 ATOM 1975 C CB . MET A 1 240 ? 43.976 -11.445 1.204 1.00 19.41 ? 256 MET A CB 1 ATOM 1976 C CG . MET A 1 240 ? 43.877 -10.398 0.095 1.00 19.89 ? 256 MET A CG 1 ATOM 1977 S SD . MET A 1 240 ? 44.177 -8.745 0.765 1.00 19.77 ? 256 MET A SD 1 ATOM 1978 C CE . MET A 1 240 ? 42.735 -8.546 1.817 1.00 19.62 ? 256 MET A CE 1 ATOM 1979 N N . HIS A 1 241 ? 42.802 -13.183 -1.443 1.00 19.34 ? 257 HIS A N 1 ATOM 1980 C CA . HIS A 1 241 ? 41.666 -13.362 -2.325 1.00 19.69 ? 257 HIS A CA 1 ATOM 1981 C C . HIS A 1 241 ? 41.066 -14.770 -2.281 1.00 19.72 ? 257 HIS A C 1 ATOM 1982 O O . HIS A 1 241 ? 40.001 -14.996 -2.852 1.00 19.99 ? 257 HIS A O 1 ATOM 1983 C CB . HIS A 1 241 ? 42.047 -12.987 -3.772 1.00 19.22 ? 257 HIS A CB 1 ATOM 1984 C CG . HIS A 1 241 ? 43.092 -13.872 -4.388 1.00 19.68 ? 257 HIS A CG 1 ATOM 1985 N ND1 . HIS A 1 241 ? 44.275 -14.191 -3.758 1.00 19.43 ? 257 HIS A ND1 1 ATOM 1986 C CD2 . HIS A 1 241 ? 43.151 -14.459 -5.610 1.00 19.45 ? 257 HIS A CD2 1 ATOM 1987 C CE1 . HIS A 1 241 ? 45.002 -14.966 -4.543 1.00 19.53 ? 257 HIS A CE1 1 ATOM 1988 N NE2 . HIS A 1 241 ? 44.348 -15.134 -5.681 1.00 19.46 ? 257 HIS A NE2 1 ATOM 1989 N N . LEU A 1 242 ? 41.746 -15.696 -1.603 1.00 19.27 ? 258 LEU A N 1 ATOM 1990 C CA . LEU A 1 242 ? 41.286 -17.086 -1.485 1.00 19.48 ? 258 LEU A CA 1 ATOM 1991 C C . LEU A 1 242 ? 40.442 -17.298 -0.237 1.00 19.46 ? 258 LEU A C 1 ATOM 1992 O O . LEU A 1 242 ? 39.952 -18.401 0.011 1.00 19.69 ? 258 LEU A O 1 ATOM 1993 C CB . LEU A 1 242 ? 42.490 -18.050 -1.454 1.00 19.31 ? 258 LEU A CB 1 ATOM 1994 C CG . LEU A 1 242 ? 43.552 -17.865 -2.532 1.00 19.63 ? 258 LEU A CG 1 ATOM 1995 C CD1 . LEU A 1 242 ? 44.702 -18.837 -2.318 1.00 19.50 ? 258 LEU A CD1 1 ATOM 1996 C CD2 . LEU A 1 242 ? 42.941 -18.079 -3.908 1.00 19.71 ? 258 LEU A CD2 1 ATOM 1997 N N . LEU A 1 243 ? 40.251 -16.232 0.532 1.00 19.48 ? 259 LEU A N 1 ATOM 1998 C CA . LEU A 1 243 ? 39.641 -16.347 1.865 1.00 19.24 ? 259 LEU A CA 1 ATOM 1999 C C . LEU A 1 243 ? 38.134 -16.025 1.909 1.00 19.50 ? 259 LEU A C 1 ATOM 2000 O O . LEU A 1 243 ? 37.536 -15.972 2.969 1.00 19.22 ? 259 LEU A O 1 ATOM 2001 C CB . LEU A 1 243 ? 40.458 -15.539 2.872 1.00 18.89 ? 259 LEU A CB 1 ATOM 2002 C CG . LEU A 1 243 ? 41.851 -16.128 3.174 1.00 19.12 ? 259 LEU A CG 1 ATOM 2003 C CD1 . LEU A 1 243 ? 42.729 -15.109 3.901 1.00 18.22 ? 259 LEU A CD1 1 ATOM 2004 C CD2 . LEU A 1 243 ? 41.753 -17.436 3.973 1.00 18.73 ? 259 LEU A CD2 1 ATOM 2005 N N . GLY A 1 244 ? 37.519 -15.830 0.745 1.00 19.10 ? 260 GLY A N 1 ATOM 2006 C CA . GLY A 1 244 ? 36.056 -15.726 0.653 1.00 19.88 ? 260 GLY A CA 1 ATOM 2007 C C . GLY A 1 244 ? 35.441 -14.393 1.069 1.00 20.01 ? 260 GLY A C 1 ATOM 2008 O O . GLY A 1 244 ? 34.218 -14.276 1.173 1.00 20.73 ? 260 GLY A O 1 ATOM 2009 N N . ASN A 1 245 ? 36.279 -13.389 1.287 1.00 19.49 ? 261 ASN A N 1 ATOM 2010 C CA . ASN A 1 245 ? 35.820 -12.056 1.676 1.00 19.85 ? 261 ASN A CA 1 ATOM 2011 C C . ASN A 1 245 ? 36.788 -11.022 1.107 1.00 20.27 ? 261 ASN A C 1 ATOM 2012 O O . ASN A 1 245 ? 37.999 -11.215 1.191 1.00 20.08 ? 261 ASN A O 1 ATOM 2013 C CB . ASN A 1 245 ? 35.756 -11.960 3.209 1.00 19.44 ? 261 ASN A CB 1 ATOM 2014 C CG . ASN A 1 245 ? 35.381 -10.580 3.682 1.00 18.80 ? 261 ASN A CG 1 ATOM 2015 O OD1 . ASN A 1 245 ? 36.236 -9.699 3.811 1.00 18.47 ? 261 ASN A OD1 1 ATOM 2016 N ND2 . ASN A 1 245 ? 34.095 -10.377 3.940 1.00 19.30 ? 261 ASN A ND2 1 ATOM 2017 N N . MET A 1 246 ? 36.258 -9.954 0.488 1.00 21.25 ? 262 MET A N 1 ATOM 2018 C CA . MET A 1 246 ? 37.080 -8.934 -0.194 1.00 20.73 ? 262 MET A CA 1 ATOM 2019 C C . MET A 1 246 ? 38.224 -8.358 0.668 1.00 20.40 ? 262 MET A C 1 ATOM 2020 O O . MET A 1 246 ? 39.267 -7.943 0.141 1.00 20.27 ? 262 MET A O 1 ATOM 2021 C CB . MET A 1 246 ? 36.194 -7.794 -0.745 1.00 21.18 ? 262 MET A CB 1 ATOM 2022 C CG . MET A 1 246 ? 36.956 -6.725 -1.531 1.00 21.21 ? 262 MET A CG 1 ATOM 2023 S SD . MET A 1 246 ? 37.594 -7.327 -3.128 1.00 22.02 ? 262 MET A SD 1 ATOM 2024 C CE . MET A 1 246 ? 36.082 -7.314 -4.081 1.00 23.17 ? 262 MET A CE 1 ATOM 2025 N N . TRP A 1 247 ? 38.019 -8.335 1.983 1.00 19.76 ? 263 TRP A N 1 ATOM 2026 C CA . TRP A 1 247 ? 38.990 -7.769 2.936 1.00 20.05 ? 263 TRP A CA 1 ATOM 2027 C C . TRP A 1 247 ? 39.631 -8.855 3.814 1.00 19.52 ? 263 TRP A C 1 ATOM 2028 O O . TRP A 1 247 ? 40.430 -8.559 4.706 1.00 19.99 ? 263 TRP A O 1 ATOM 2029 C CB . TRP A 1 247 ? 38.315 -6.651 3.770 1.00 19.57 ? 263 TRP A CB 1 ATOM 2030 C CG . TRP A 1 247 ? 37.561 -5.702 2.837 1.00 19.98 ? 263 TRP A CG 1 ATOM 2031 C CD1 . TRP A 1 247 ? 38.077 -4.628 2.162 1.00 20.01 ? 263 TRP A CD1 1 ATOM 2032 C CD2 . TRP A 1 247 ? 36.190 -5.812 2.428 1.00 19.97 ? 263 TRP A CD2 1 ATOM 2033 N NE1 . TRP A 1 247 ? 37.102 -4.053 1.364 1.00 20.29 ? 263 TRP A NE1 1 ATOM 2034 C CE2 . TRP A 1 247 ? 35.938 -4.762 1.508 1.00 20.43 ? 263 TRP A CE2 1 ATOM 2035 C CE3 . TRP A 1 247 ? 35.151 -6.701 2.743 1.00 20.17 ? 263 TRP A CE3 1 ATOM 2036 C CZ2 . TRP A 1 247 ? 34.682 -4.575 0.905 1.00 20.25 ? 263 TRP A CZ2 1 ATOM 2037 C CZ3 . TRP A 1 247 ? 33.901 -6.510 2.158 1.00 20.72 ? 263 TRP A CZ3 1 ATOM 2038 C CH2 . TRP A 1 247 ? 33.681 -5.449 1.245 1.00 20.48 ? 263 TRP A CH2 1 ATOM 2039 N N . ALA A 1 248 ? 39.271 -10.111 3.535 1.00 19.41 ? 264 ALA A N 1 ATOM 2040 C CA . ALA A 1 248 ? 39.678 -11.272 4.329 1.00 19.63 ? 264 ALA A CA 1 ATOM 2041 C C . ALA A 1 248 ? 39.341 -11.091 5.801 1.00 19.64 ? 264 ALA A C 1 ATOM 2042 O O . ALA A 1 248 ? 40.054 -11.605 6.658 1.00 19.81 ? 264 ALA A O 1 ATOM 2043 C CB . ALA A 1 248 ? 41.171 -11.576 4.148 1.00 19.33 ? 264 ALA A CB 1 ATOM 2044 N N . GLN A 1 249 ? 38.266 -10.362 6.103 1.00 19.85 ? 265 GLN A N 1 ATOM 2045 C CA . GLN A 1 249 ? 37.958 -10.067 7.521 1.00 19.62 ? 265 GLN A CA 1 ATOM 2046 C C . GLN A 1 249 ? 37.295 -11.222 8.272 1.00 20.06 ? 265 GLN A C 1 ATOM 2047 O O . GLN A 1 249 ? 37.403 -11.307 9.507 1.00 19.03 ? 265 GLN A O 1 ATOM 2048 C CB . GLN A 1 249 ? 37.117 -8.790 7.663 1.00 20.27 ? 265 GLN A CB 1 ATOM 2049 C CG . GLN A 1 249 ? 35.681 -8.914 7.175 1.00 21.51 ? 265 GLN A CG 1 ATOM 2050 C CD . GLN A 1 249 ? 35.020 -7.564 6.992 1.00 23.33 ? 265 GLN A CD 1 ATOM 2051 O OE1 . GLN A 1 249 ? 35.635 -6.600 6.519 1.00 23.15 ? 265 GLN A OE1 1 ATOM 2052 N NE2 . GLN A 1 249 ? 33.764 -7.486 7.374 1.00 24.85 ? 265 GLN A NE2 1 ATOM 2053 N N . GLN A 1 250 ? 36.587 -12.078 7.537 1.00 20.27 ? 266 GLN A N 1 ATOM 2054 C CA . GLN A 1 250 ? 35.949 -13.296 8.065 1.00 21.41 ? 266 GLN A CA 1 ATOM 2055 C C . GLN A 1 250 ? 36.082 -14.369 6.993 1.00 20.71 ? 266 GLN A C 1 ATOM 2056 O O . GLN A 1 250 ? 35.968 -14.053 5.797 1.00 20.35 ? 266 GLN A O 1 ATOM 2057 C CB . GLN A 1 250 ? 34.461 -13.060 8.364 1.00 23.05 ? 266 GLN A CB 1 ATOM 2058 C CG . GLN A 1 250 ? 34.219 -12.035 9.460 1.00 25.65 ? 266 GLN A CG 1 ATOM 2059 C CD . GLN A 1 250 ? 32.788 -12.014 9.951 1.00 28.02 ? 266 GLN A CD 1 ATOM 2060 O OE1 . GLN A 1 250 ? 31.843 -11.864 9.169 1.00 29.61 ? 266 GLN A OE1 1 ATOM 2061 N NE2 . GLN A 1 250 ? 32.619 -12.145 11.263 1.00 28.26 ? 266 GLN A NE2 1 ATOM 2062 N N . TRP A 1 251 ? 36.315 -15.617 7.396 1.00 19.88 ? 267 TRP A N 1 ATOM 2063 C CA . TRP A 1 251 ? 36.629 -16.682 6.415 1.00 20.10 ? 267 TRP A CA 1 ATOM 2064 C C . TRP A 1 251 ? 35.552 -17.765 6.254 1.00 20.67 ? 267 TRP A C 1 ATOM 2065 O O . TRP A 1 251 ? 35.791 -18.792 5.606 1.00 20.41 ? 267 TRP A O 1 ATOM 2066 C CB . TRP A 1 251 ? 37.980 -17.345 6.720 1.00 19.16 ? 267 TRP A CB 1 ATOM 2067 C CG . TRP A 1 251 ? 39.158 -16.414 6.865 1.00 18.71 ? 267 TRP A CG 1 ATOM 2068 C CD1 . TRP A 1 251 ? 39.251 -15.104 6.466 1.00 18.27 ? 267 TRP A CD1 1 ATOM 2069 C CD2 . TRP A 1 251 ? 40.422 -16.744 7.446 1.00 18.77 ? 267 TRP A CD2 1 ATOM 2070 N NE1 . TRP A 1 251 ? 40.496 -14.607 6.765 1.00 18.40 ? 267 TRP A NE1 1 ATOM 2071 C CE2 . TRP A 1 251 ? 41.233 -15.589 7.372 1.00 18.58 ? 267 TRP A CE2 1 ATOM 2072 C CE3 . TRP A 1 251 ? 40.952 -17.910 8.019 1.00 18.92 ? 267 TRP A CE3 1 ATOM 2073 C CZ2 . TRP A 1 251 ? 42.546 -15.560 7.866 1.00 18.70 ? 267 TRP A CZ2 1 ATOM 2074 C CZ3 . TRP A 1 251 ? 42.256 -17.882 8.509 1.00 19.17 ? 267 TRP A CZ3 1 ATOM 2075 C CH2 . TRP A 1 251 ? 43.039 -16.713 8.419 1.00 18.83 ? 267 TRP A CH2 1 ATOM 2076 N N . SER A 1 252 ? 34.370 -17.544 6.821 1.00 21.31 ? 268 SER A N 1 ATOM 2077 C CA . SER A 1 252 ? 33.368 -18.612 6.870 1.00 22.51 ? 268 SER A CA 1 ATOM 2078 C C . SER A 1 252 ? 32.865 -19.037 5.491 1.00 23.07 ? 268 SER A C 1 ATOM 2079 O O . SER A 1 252 ? 32.386 -20.158 5.346 1.00 23.29 ? 268 SER A O 1 ATOM 2080 C CB . SER A 1 252 ? 32.195 -18.265 7.799 1.00 22.89 ? 268 SER A CB 1 ATOM 2081 O OG . SER A 1 252 ? 31.628 -17.031 7.432 1.00 23.30 ? 268 SER A OG 1 ATOM 2082 N N . GLU A 1 253 ? 33.001 -18.174 4.482 1.00 23.64 ? 269 GLU A N 1 ATOM 2083 C CA . GLU A 1 253 ? 32.569 -18.534 3.122 1.00 25.01 ? 269 GLU A CA 1 ATOM 2084 C C . GLU A 1 253 ? 33.374 -19.695 2.480 1.00 25.23 ? 269 GLU A C 1 ATOM 2085 O O . GLU A 1 253 ? 32.910 -20.311 1.525 1.00 25.38 ? 269 GLU A O 1 ATOM 2086 C CB . GLU A 1 253 ? 32.540 -17.307 2.200 1.00 26.29 ? 269 GLU A CB 1 ATOM 2087 C CG . GLU A 1 253 ? 31.505 -16.238 2.566 1.00 28.19 ? 269 GLU A CG 1 ATOM 2088 C CD . GLU A 1 253 ? 30.085 -16.559 2.090 1.00 30.18 ? 269 GLU A CD 1 ATOM 2089 O OE1 . GLU A 1 253 ? 29.821 -17.678 1.617 1.00 31.47 ? 269 GLU A OE1 1 ATOM 2090 O OE2 . GLU A 1 253 ? 29.215 -15.676 2.174 1.00 32.16 ? 269 GLU A OE2 1 ATOM 2091 N N . ILE A 1 254 ? 34.571 -19.981 2.991 1.00 24.99 ? 270 ILE A N 1 ATOM 2092 C CA . ILE A 1 254 ? 35.383 -21.089 2.452 1.00 24.81 ? 270 ILE A CA 1 ATOM 2093 C C . ILE A 1 254 ? 35.367 -22.309 3.376 1.00 25.16 ? 270 ILE A C 1 ATOM 2094 O O . ILE A 1 254 ? 36.144 -23.250 3.189 1.00 25.06 ? 270 ILE A O 1 ATOM 2095 C CB . ILE A 1 254 ? 36.838 -20.669 2.100 1.00 24.65 ? 270 ILE A CB 1 ATOM 2096 C CG1 . ILE A 1 254 ? 37.610 -20.239 3.355 1.00 24.25 ? 270 ILE A CG1 1 ATOM 2097 C CG2 . ILE A 1 254 ? 36.845 -19.564 1.052 1.00 24.16 ? 270 ILE A CG2 1 ATOM 2098 C CD1 . ILE A 1 254 ? 39.114 -20.406 3.247 1.00 25.03 ? 270 ILE A CD1 1 ATOM 2099 N N . ALA A 1 255 ? 34.464 -22.297 4.359 1.00 24.77 ? 271 ALA A N 1 ATOM 2100 C CA . ALA A 1 255 ? 34.315 -23.416 5.294 1.00 25.65 ? 271 ALA A CA 1 ATOM 2101 C C . ALA A 1 255 ? 34.165 -24.790 4.630 1.00 26.80 ? 271 ALA A C 1 ATOM 2102 O O . ALA A 1 255 ? 34.653 -25.788 5.158 1.00 27.30 ? 271 ALA A O 1 ATOM 2103 C CB . ALA A 1 255 ? 33.161 -23.165 6.256 1.00 25.37 ? 271 ALA A CB 1 ATOM 2104 N N . ASP A 1 256 ? 33.505 -24.848 3.479 1.00 28.19 ? 272 ASP A N 1 ATOM 2105 C CA . ASP A 1 256 ? 33.291 -26.123 2.794 1.00 30.60 ? 272 ASP A CA 1 ATOM 2106 C C . ASP A 1 256 ? 34.587 -26.752 2.265 1.00 30.86 ? 272 ASP A C 1 ATOM 2107 O O . ASP A 1 256 ? 34.605 -27.940 1.938 1.00 31.63 ? 272 ASP A O 1 ATOM 2108 C CB . ASP A 1 256 ? 32.310 -25.948 1.643 1.00 32.40 ? 272 ASP A CB 1 ATOM 2109 C CG . ASP A 1 256 ? 32.868 -25.073 0.554 1.00 33.68 ? 272 ASP A CG 1 ATOM 2110 O OD1 . ASP A 1 256 ? 33.011 -23.854 0.779 1.00 34.97 ? 272 ASP A OD1 1 ATOM 2111 O OD2 . ASP A 1 256 ? 33.199 -25.607 -0.517 1.00 36.03 ? 272 ASP A OD2 1 ATOM 2112 N N . ILE A 1 257 ? 35.654 -25.963 2.156 1.00 29.67 ? 273 ILE A N 1 ATOM 2113 C CA . ILE A 1 257 ? 36.948 -26.521 1.734 1.00 29.99 ? 273 ILE A CA 1 ATOM 2114 C C . ILE A 1 257 ? 37.987 -26.642 2.859 1.00 29.05 ? 273 ILE A C 1 ATOM 2115 O O . ILE A 1 257 ? 39.016 -27.296 2.686 1.00 29.64 ? 273 ILE A O 1 ATOM 2116 C CB . ILE A 1 257 ? 37.534 -25.837 0.469 1.00 30.98 ? 273 ILE A CB 1 ATOM 2117 C CG1 . ILE A 1 257 ? 37.762 -24.339 0.674 1.00 30.67 ? 273 ILE A CG1 1 ATOM 2118 C CG2 . ILE A 1 257 ? 36.629 -26.098 -0.733 1.00 31.91 ? 273 ILE A CG2 1 ATOM 2119 C CD1 . ILE A 1 257 ? 38.302 -23.626 -0.554 1.00 31.12 ? 273 ILE A CD1 1 ATOM 2120 N N . VAL A 1 258 ? 37.704 -26.050 4.020 1.00 27.48 ? 274 VAL A N 1 ATOM 2121 C CA . VAL A 1 258 ? 38.657 -26.102 5.139 1.00 27.06 ? 274 VAL A CA 1 ATOM 2122 C C . VAL A 1 258 ? 38.095 -26.747 6.418 1.00 27.37 ? 274 VAL A C 1 ATOM 2123 O O . VAL A 1 258 ? 38.753 -26.719 7.463 1.00 27.78 ? 274 VAL A O 1 ATOM 2124 C CB . VAL A 1 258 ? 39.283 -24.712 5.440 1.00 26.36 ? 274 VAL A CB 1 ATOM 2125 C CG1 . VAL A 1 258 ? 39.999 -24.162 4.210 1.00 26.26 ? 274 VAL A CG1 1 ATOM 2126 C CG2 . VAL A 1 258 ? 38.214 -23.733 5.910 1.00 26.86 ? 274 VAL A CG2 1 ATOM 2127 N N . SER A 1 259 ? 36.900 -27.337 6.326 1.00 27.85 ? 275 SER A N 1 ATOM 2128 C CA . SER A 1 259 ? 36.244 -27.994 7.475 1.00 28.76 ? 275 SER A CA 1 ATOM 2129 C C . SER A 1 259 ? 37.050 -29.158 8.041 1.00 28.05 ? 275 SER A C 1 ATOM 2130 O O . SER A 1 259 ? 37.526 -30.006 7.284 1.00 28.57 ? 275 SER A O 1 ATOM 2131 C CB . SER A 1 259 ? 34.860 -28.514 7.090 1.00 29.89 ? 275 SER A CB 1 ATOM 2132 O OG . SER A 1 259 ? 33.917 -27.474 7.190 1.00 34.24 ? 275 SER A OG 1 ATOM 2133 N N . PRO A 1 260 ? 37.194 -29.209 9.377 1.00 27.17 ? 276 PRO A N 1 ATOM 2134 C CA . PRO A 1 260 ? 37.910 -30.298 10.029 1.00 27.10 ? 276 PRO A CA 1 ATOM 2135 C C . PRO A 1 260 ? 37.409 -31.690 9.626 1.00 27.56 ? 276 PRO A C 1 ATOM 2136 O O . PRO A 1 260 ? 38.228 -32.576 9.374 1.00 27.76 ? 276 PRO A O 1 ATOM 2137 C CB . PRO A 1 260 ? 37.649 -30.032 11.513 1.00 27.00 ? 276 PRO A CB 1 ATOM 2138 C CG . PRO A 1 260 ? 37.552 -28.548 11.592 1.00 26.74 ? 276 PRO A CG 1 ATOM 2139 C CD . PRO A 1 260 ? 36.836 -28.143 10.332 1.00 26.92 ? 276 PRO A CD 1 ATOM 2140 N N . PHE A 1 261 ? 36.089 -31.874 9.555 1.00 27.09 ? 277 PHE A N 1 ATOM 2141 C CA . PHE A 1 261 ? 35.500 -33.171 9.199 1.00 27.67 ? 277 PHE A CA 1 ATOM 2142 C C . PHE A 1 261 ? 34.545 -33.052 8.011 1.00 28.58 ? 277 PHE A C 1 ATOM 2143 O O . PHE A 1 261 ? 33.328 -32.913 8.186 1.00 28.30 ? 277 PHE A O 1 ATOM 2144 C CB . PHE A 1 261 ? 34.803 -33.810 10.404 1.00 27.97 ? 277 PHE A CB 1 ATOM 2145 C CG . PHE A 1 261 ? 35.718 -34.053 11.569 1.00 27.99 ? 277 PHE A CG 1 ATOM 2146 C CD1 . PHE A 1 261 ? 36.568 -35.158 11.588 1.00 28.40 ? 277 PHE A CD1 1 ATOM 2147 C CD2 . PHE A 1 261 ? 35.737 -33.175 12.649 1.00 27.95 ? 277 PHE A CD2 1 ATOM 2148 C CE1 . PHE A 1 261 ? 37.420 -35.383 12.662 1.00 28.50 ? 277 PHE A CE1 1 ATOM 2149 C CE2 . PHE A 1 261 ? 36.585 -33.390 13.720 1.00 27.70 ? 277 PHE A CE2 1 ATOM 2150 C CZ . PHE A 1 261 ? 37.429 -34.496 13.731 1.00 28.30 ? 277 PHE A CZ 1 ATOM 2151 N N . PRO A 1 262 ? 35.101 -33.120 6.786 1.00 29.60 ? 278 PRO A N 1 ATOM 2152 C CA . PRO A 1 262 ? 34.350 -32.880 5.547 1.00 30.85 ? 278 PRO A CA 1 ATOM 2153 C C . PRO A 1 262 ? 33.220 -33.878 5.278 1.00 32.18 ? 278 PRO A C 1 ATOM 2154 O O . PRO A 1 262 ? 32.306 -33.562 4.517 1.00 32.53 ? 278 PRO A O 1 ATOM 2155 C CB . PRO A 1 262 ? 35.428 -32.972 4.452 1.00 30.37 ? 278 PRO A CB 1 ATOM 2156 C CG . PRO A 1 262 ? 36.715 -32.736 5.164 1.00 29.85 ? 278 PRO A CG 1 ATOM 2157 C CD . PRO A 1 262 ? 36.526 -33.374 6.512 1.00 29.69 ? 278 PRO A CD 1 ATOM 2158 N N . GLU A 1 263 ? 33.273 -35.057 5.898 1.00 33.31 ? 279 GLU A N 1 ATOM 2159 C CA . GLU A 1 263 ? 32.223 -36.066 5.714 1.00 34.67 ? 279 GLU A CA 1 ATOM 2160 C C . GLU A 1 263 ? 31.096 -35.938 6.748 1.00 35.90 ? 279 GLU A C 1 ATOM 2161 O O . GLU A 1 263 ? 30.107 -36.681 6.700 1.00 36.17 ? 279 GLU A O 1 ATOM 2162 C CB . GLU A 1 263 ? 32.817 -37.479 5.716 1.00 34.95 ? 279 GLU A CB 1 ATOM 2163 C CG . GLU A 1 263 ? 33.770 -37.748 4.555 0.50 34.94 ? 279 GLU A CG 1 ATOM 2164 C CD . GLU A 1 263 ? 34.495 -39.080 4.663 0.50 35.45 ? 279 GLU A CD 1 ATOM 2165 O OE1 . GLU A 1 263 ? 34.148 -39.900 5.542 0.50 35.27 ? 279 GLU A OE1 1 ATOM 2166 O OE2 . GLU A 1 263 ? 35.422 -39.310 3.859 0.50 35.49 ? 279 GLU A OE2 1 ATOM 2167 N N . LYS A 1 264 ? 31.255 -35.000 7.683 1.00 35.21 ? 280 LYS A N 1 ATOM 2168 C CA . LYS A 1 264 ? 30.229 -34.706 8.687 1.00 35.46 ? 280 LYS A CA 1 ATOM 2169 C C . LYS A 1 264 ? 29.541 -33.372 8.368 1.00 35.01 ? 280 LYS A C 1 ATOM 2170 O O . LYS A 1 264 ? 30.066 -32.594 7.567 1.00 33.94 ? 280 LYS A O 1 ATOM 2171 C CB . LYS A 1 264 ? 30.838 -34.711 10.098 1.00 35.25 ? 280 LYS A CB 1 ATOM 2172 C CG . LYS A 1 264 ? 31.308 -36.089 10.561 1.00 36.41 ? 280 LYS A CG 1 ATOM 2173 C CD . LYS A 1 264 ? 30.131 -37.019 10.864 1.00 37.78 ? 280 LYS A CD 1 ATOM 2174 C CE . LYS A 1 264 ? 30.577 -38.436 11.213 1.00 38.43 ? 280 LYS A CE 1 ATOM 2175 N NZ . LYS A 1 264 ? 31.197 -38.526 12.565 1.00 38.26 ? 280 LYS A NZ 1 ATOM 2176 N N . PRO A 1 265 ? 28.353 -33.118 8.967 1.00 35.40 ? 281 PRO A N 1 ATOM 2177 C CA . PRO A 1 265 ? 27.587 -31.921 8.592 1.00 35.27 ? 281 PRO A CA 1 ATOM 2178 C C . PRO A 1 265 ? 28.286 -30.585 8.860 1.00 34.27 ? 281 PRO A C 1 ATOM 2179 O O . PRO A 1 265 ? 28.975 -30.409 9.877 1.00 32.50 ? 281 PRO A O 1 ATOM 2180 C CB . PRO A 1 265 ? 26.299 -32.024 9.434 1.00 36.04 ? 281 PRO A CB 1 ATOM 2181 C CG . PRO A 1 265 ? 26.576 -33.050 10.479 1.00 36.66 ? 281 PRO A CG 1 ATOM 2182 C CD . PRO A 1 265 ? 27.588 -33.989 9.881 1.00 36.00 ? 281 PRO A CD 1 ATOM 2183 N N . LEU A 1 266 ? 28.109 -29.673 7.913 1.00 34.06 ? 282 LEU A N 1 ATOM 2184 C CA . LEU A 1 266 ? 28.513 -28.287 8.062 1.00 33.73 ? 282 LEU A CA 1 ATOM 2185 C C . LEU A 1 266 ? 27.270 -27.423 7.828 1.00 32.70 ? 282 LEU A C 1 ATOM 2186 O O . LEU A 1 266 ? 26.608 -27.536 6.794 1.00 33.35 ? 282 LEU A O 1 ATOM 2187 C CB . LEU A 1 266 ? 29.623 -27.947 7.069 1.00 34.04 ? 282 LEU A CB 1 ATOM 2188 C CG . LEU A 1 266 ? 30.148 -26.511 7.065 1.00 34.76 ? 282 LEU A CG 1 ATOM 2189 C CD1 . LEU A 1 266 ? 30.876 -26.170 8.365 1.00 34.11 ? 282 LEU A CD1 1 ATOM 2190 C CD2 . LEU A 1 266 ? 31.053 -26.314 5.856 1.00 34.97 ? 282 LEU A CD2 1 ATOM 2191 N N . VAL A 1 267 ? 26.945 -26.582 8.804 1.00 31.91 ? 283 VAL A N 1 ATOM 2192 C CA . VAL A 1 267 ? 25.719 -25.790 8.753 1.00 30.70 ? 283 VAL A CA 1 ATOM 2193 C C . VAL A 1 267 ? 25.816 -24.696 7.689 1.00 30.53 ? 283 VAL A C 1 ATOM 2194 O O . VAL A 1 267 ? 26.683 -23.810 7.764 1.00 29.58 ? 283 VAL A O 1 ATOM 2195 C CB . VAL A 1 267 ? 25.375 -25.166 10.125 1.00 30.73 ? 283 VAL A CB 1 ATOM 2196 C CG1 . VAL A 1 267 ? 24.118 -24.312 10.020 1.00 30.11 ? 283 VAL A CG1 1 ATOM 2197 C CG2 . VAL A 1 267 ? 25.208 -26.243 11.194 1.00 30.63 ? 283 VAL A CG2 1 ATOM 2198 N N . ASP A 1 268 ? 24.930 -24.781 6.699 1.00 29.73 ? 284 ASP A N 1 ATOM 2199 C CA . ASP A 1 268 ? 24.779 -23.745 5.679 1.00 29.93 ? 284 ASP A CA 1 ATOM 2200 C C . ASP A 1 268 ? 23.327 -23.721 5.198 1.00 29.53 ? 284 ASP A C 1 ATOM 2201 O O . ASP A 1 268 ? 22.940 -24.512 4.336 1.00 29.43 ? 284 ASP A O 1 ATOM 2202 C CB . ASP A 1 268 ? 25.725 -24.008 4.510 1.00 31.24 ? 284 ASP A CB 1 ATOM 2203 C CG . ASP A 1 268 ? 25.749 -22.872 3.501 1.00 31.87 ? 284 ASP A CG 1 ATOM 2204 O OD1 . ASP A 1 268 ? 24.821 -22.030 3.465 1.00 31.55 ? 284 ASP A OD1 1 ATOM 2205 O OD2 . ASP A 1 268 ? 26.719 -22.828 2.732 1.00 34.37 ? 284 ASP A OD2 1 ATOM 2206 N N . VAL A 1 269 ? 22.534 -22.798 5.746 1.00 28.96 ? 285 VAL A N 1 ATOM 2207 C CA . VAL A 1 269 ? 21.076 -22.844 5.574 1.00 28.56 ? 285 VAL A CA 1 ATOM 2208 C C . VAL A 1 269 ? 20.523 -21.996 4.420 1.00 28.55 ? 285 VAL A C 1 ATOM 2209 O O . VAL A 1 269 ? 19.302 -21.901 4.252 1.00 28.15 ? 285 VAL A O 1 ATOM 2210 C CB . VAL A 1 269 ? 20.329 -22.539 6.899 1.00 28.77 ? 285 VAL A CB 1 ATOM 2211 C CG1 . VAL A 1 269 ? 20.741 -23.529 7.985 1.00 28.68 ? 285 VAL A CG1 1 ATOM 2212 C CG2 . VAL A 1 269 ? 20.558 -21.091 7.354 1.00 28.21 ? 285 VAL A CG2 1 ATOM 2213 N N . SER A 1 270 ? 21.417 -21.418 3.612 1.00 28.20 ? 286 SER A N 1 ATOM 2214 C CA . SER A 1 270 ? 21.018 -20.516 2.525 1.00 28.68 ? 286 SER A CA 1 ATOM 2215 C C . SER A 1 270 ? 20.078 -21.213 1.544 1.00 29.46 ? 286 SER A C 1 ATOM 2216 O O . SER A 1 270 ? 19.022 -20.672 1.202 1.00 29.47 ? 286 SER A O 1 ATOM 2217 C CB . SER A 1 270 ? 22.235 -19.965 1.786 1.00 28.35 ? 286 SER A CB 1 ATOM 2218 O OG . SER A 1 270 ? 23.026 -19.139 2.626 1.00 28.15 ? 286 SER A OG 1 ATOM 2219 N N . ALA A 1 271 ? 20.459 -22.422 1.121 1.00 29.92 ? 287 ALA A N 1 ATOM 2220 C CA . ALA A 1 271 ? 19.635 -23.232 0.216 1.00 30.17 ? 287 ALA A CA 1 ATOM 2221 C C . ALA A 1 271 ? 18.242 -23.517 0.785 1.00 29.95 ? 287 ALA A C 1 ATOM 2222 O O . ALA A 1 271 ? 17.261 -23.402 0.071 1.00 30.35 ? 287 ALA A O 1 ATOM 2223 C CB . ALA A 1 271 ? 20.350 -24.525 -0.162 1.00 30.46 ? 287 ALA A CB 1 ATOM 2224 N N . GLU A 1 272 ? 18.157 -23.857 2.070 1.00 30.29 ? 288 GLU A N 1 ATOM 2225 C CA . GLU A 1 272 ? 16.859 -24.106 2.709 1.00 30.85 ? 288 GLU A CA 1 ATOM 2226 C C . GLU A 1 272 ? 15.993 -22.852 2.845 1.00 31.06 ? 288 GLU A C 1 ATOM 2227 O O . GLU A 1 272 ? 14.765 -22.928 2.699 1.00 30.98 ? 288 GLU A O 1 ATOM 2228 C CB . GLU A 1 272 ? 17.020 -24.801 4.060 1.00 31.54 ? 288 GLU A CB 1 ATOM 2229 C CG . GLU A 1 272 ? 17.235 -26.303 3.946 1.00 33.67 ? 288 GLU A CG 1 ATOM 2230 C CD . GLU A 1 272 ? 16.025 -27.042 3.385 1.00 35.09 ? 288 GLU A CD 1 ATOM 2231 O OE1 . GLU A 1 272 ? 14.882 -26.555 3.541 1.00 35.74 ? 288 GLU A OE1 1 ATOM 2232 O OE2 . GLU A 1 272 ? 16.220 -28.117 2.783 1.00 36.83 ? 288 GLU A OE2 1 ATOM 2233 N N . MET A 1 273 ? 16.632 -21.712 3.117 1.00 30.11 ? 289 MET A N 1 ATOM 2234 C CA . MET A 1 273 ? 15.947 -20.419 3.135 1.00 30.63 ? 289 MET A CA 1 ATOM 2235 C C . MET A 1 273 ? 15.258 -20.159 1.790 1.00 32.36 ? 289 MET A C 1 ATOM 2236 O O . MET A 1 273 ? 14.068 -19.838 1.749 1.00 32.91 ? 289 MET A O 1 ATOM 2237 C CB . MET A 1 273 ? 16.924 -19.280 3.484 1.00 28.73 ? 289 MET A CB 1 ATOM 2238 C CG . MET A 1 273 ? 17.475 -19.320 4.909 1.00 27.30 ? 289 MET A CG 1 ATOM 2239 S SD . MET A 1 273 ? 18.741 -18.065 5.264 1.00 26.22 ? 289 MET A SD 1 ATOM 2240 C CE . MET A 1 273 ? 17.783 -16.558 5.124 1.00 25.48 ? 289 MET A CE 1 ATOM 2241 N N . GLU A 1 274 ? 16.004 -20.325 0.701 1.00 34.51 ? 290 GLU A N 1 ATOM 2242 C CA . GLU A 1 274 ? 15.458 -20.162 -0.647 1.00 37.81 ? 290 GLU A CA 1 ATOM 2243 C C . GLU A 1 274 ? 14.338 -21.159 -0.935 1.00 38.31 ? 290 GLU A C 1 ATOM 2244 O O . GLU A 1 274 ? 13.270 -20.771 -1.417 1.00 38.23 ? 290 GLU A O 1 ATOM 2245 C CB . GLU A 1 274 ? 16.557 -20.292 -1.697 1.00 40.82 ? 290 GLU A CB 1 ATOM 2246 C CG . GLU A 1 274 ? 17.480 -19.087 -1.775 1.00 45.43 ? 290 GLU A CG 1 ATOM 2247 C CD . GLU A 1 274 ? 18.371 -19.127 -2.998 1.00 50.35 ? 290 GLU A CD 1 ATOM 2248 O OE1 . GLU A 1 274 ? 17.841 -19.139 -4.133 1.00 55.17 ? 290 GLU A OE1 1 ATOM 2249 O OE2 . GLU A 1 274 ? 19.606 -19.166 -2.833 1.00 52.70 ? 290 GLU A OE2 1 ATOM 2250 N N . LYS A 1 275 ? 14.580 -22.432 -0.618 1.00 38.51 ? 291 LYS A N 1 ATOM 2251 C CA . LYS A 1 275 ? 13.596 -23.492 -0.844 1.00 40.01 ? 291 LYS A CA 1 ATOM 2252 C C . LYS A 1 275 ? 12.265 -23.190 -0.142 1.00 39.42 ? 291 LYS A C 1 ATOM 2253 O O . LYS A 1 275 ? 11.194 -23.443 -0.694 1.00 39.57 ? 291 LYS A O 1 ATOM 2254 C CB . LYS A 1 275 ? 14.153 -24.856 -0.411 1.00 41.91 ? 291 LYS A CB 1 ATOM 2255 C CG . LYS A 1 275 ? 13.336 -26.047 -0.901 1.00 45.23 ? 291 LYS A CG 1 ATOM 2256 C CD . LYS A 1 275 ? 13.888 -27.375 -0.400 1.00 47.28 ? 291 LYS A CD 1 ATOM 2257 C CE . LYS A 1 275 ? 12.903 -28.506 -0.680 1.00 50.04 ? 291 LYS A CE 1 ATOM 2258 N NZ . LYS A 1 275 ? 13.124 -29.704 0.182 1.00 50.62 ? 291 LYS A NZ 1 ATOM 2259 N N . GLN A 1 276 ? 12.335 -22.621 1.058 1.00 37.53 ? 292 GLN A N 1 ATOM 2260 C CA . GLN A 1 276 ? 11.137 -22.291 1.823 1.00 36.41 ? 292 GLN A CA 1 ATOM 2261 C C . GLN A 1 276 ? 10.517 -20.930 1.472 1.00 34.85 ? 292 GLN A C 1 ATOM 2262 O O . GLN A 1 276 ? 9.525 -20.529 2.071 1.00 33.98 ? 292 GLN A O 1 ATOM 2263 C CB . GLN A 1 276 ? 11.412 -22.405 3.327 1.00 37.12 ? 292 GLN A CB 1 ATOM 2264 C CG . GLN A 1 276 ? 11.547 -23.854 3.781 1.00 39.30 ? 292 GLN A CG 1 ATOM 2265 C CD . GLN A 1 276 ? 12.032 -23.996 5.210 1.00 39.64 ? 292 GLN A CD 1 ATOM 2266 O OE1 . GLN A 1 276 ? 11.513 -23.354 6.128 1.00 40.42 ? 292 GLN A OE1 1 ATOM 2267 N NE2 . GLN A 1 276 ? 13.041 -24.852 5.405 1.00 40.15 ? 292 GLN A NE2 1 ATOM 2268 N N . GLY A 1 277 ? 11.088 -20.239 0.490 1.00 33.44 ? 293 GLY A N 1 ATOM 2269 C CA . GLY A 1 277 ? 10.538 -18.963 0.026 1.00 32.72 ? 293 GLY A CA 1 ATOM 2270 C C . GLY A 1 277 ? 10.702 -17.788 0.979 1.00 32.09 ? 293 GLY A C 1 ATOM 2271 O O . GLY A 1 277 ? 9.837 -16.919 1.039 1.00 32.75 ? 293 GLY A O 1 ATOM 2272 N N . TYR A 1 278 ? 11.804 -17.766 1.728 1.00 30.91 ? 294 TYR A N 1 ATOM 2273 C CA . TYR A 1 278 ? 12.166 -16.626 2.570 1.00 30.23 ? 294 TYR A CA 1 ATOM 2274 C C . TYR A 1 278 ? 12.299 -15.353 1.733 1.00 29.68 ? 294 TYR A C 1 ATOM 2275 O O . TYR A 1 278 ? 12.768 -15.394 0.598 1.00 29.00 ? 294 TYR A O 1 ATOM 2276 C CB . TYR A 1 278 ? 13.503 -16.892 3.270 1.00 30.49 ? 294 TYR A CB 1 ATOM 2277 C CG . TYR A 1 278 ? 13.420 -17.569 4.626 1.00 30.96 ? 294 TYR A CG 1 ATOM 2278 C CD1 . TYR A 1 278 ? 12.717 -18.766 4.802 1.00 31.67 ? 294 TYR A CD1 1 ATOM 2279 C CD2 . TYR A 1 278 ? 14.082 -17.023 5.731 1.00 30.96 ? 294 TYR A CD2 1 ATOM 2280 C CE1 . TYR A 1 278 ? 12.649 -19.385 6.045 1.00 32.12 ? 294 TYR A CE1 1 ATOM 2281 C CE2 . TYR A 1 278 ? 14.029 -17.637 6.973 1.00 31.52 ? 294 TYR A CE2 1 ATOM 2282 C CZ . TYR A 1 278 ? 13.311 -18.815 7.128 1.00 32.42 ? 294 TYR A CZ 1 ATOM 2283 O OH . TYR A 1 278 ? 13.255 -19.422 8.368 1.00 33.29 ? 294 TYR A OH 1 ATOM 2284 N N . THR A 1 279 ? 11.876 -14.233 2.306 1.00 28.91 ? 295 THR A N 1 ATOM 2285 C CA . THR A 1 279 ? 12.049 -12.915 1.705 1.00 28.41 ? 295 THR A CA 1 ATOM 2286 C C . THR A 1 279 ? 12.743 -12.011 2.732 1.00 27.99 ? 295 THR A C 1 ATOM 2287 O O . THR A 1 279 ? 12.790 -12.359 3.912 1.00 27.84 ? 295 THR A O 1 ATOM 2288 C CB . THR A 1 279 ? 10.692 -12.283 1.337 1.00 28.36 ? 295 THR A CB 1 ATOM 2289 O OG1 . THR A 1 279 ? 9.902 -12.154 2.522 1.00 28.39 ? 295 THR A OG1 1 ATOM 2290 C CG2 . THR A 1 279 ? 9.942 -13.138 0.305 1.00 28.85 ? 295 THR A CG2 1 ATOM 2291 N N . PRO A 1 280 ? 13.274 -10.848 2.297 1.00 28.14 ? 296 PRO A N 1 ATOM 2292 C CA . PRO A 1 280 ? 13.785 -9.887 3.282 1.00 27.81 ? 296 PRO A CA 1 ATOM 2293 C C . PRO A 1 280 ? 12.751 -9.520 4.348 1.00 27.78 ? 296 PRO A C 1 ATOM 2294 O O . PRO A 1 280 ? 13.098 -9.469 5.530 1.00 27.31 ? 296 PRO A O 1 ATOM 2295 C CB . PRO A 1 280 ? 14.142 -8.671 2.423 1.00 27.90 ? 296 PRO A CB 1 ATOM 2296 C CG . PRO A 1 280 ? 14.559 -9.280 1.132 1.00 27.87 ? 296 PRO A CG 1 ATOM 2297 C CD . PRO A 1 280 ? 13.599 -10.429 0.921 1.00 28.20 ? 296 PRO A CD 1 ATOM 2298 N N . LEU A 1 281 ? 11.496 -9.297 3.944 1.00 27.91 ? 297 LEU A N 1 ATOM 2299 C CA . LEU A 1 281 ? 10.428 -8.985 4.904 1.00 28.15 ? 297 LEU A CA 1 ATOM 2300 C C . LEU A 1 281 ? 10.296 -10.058 5.989 1.00 27.68 ? 297 LEU A C 1 ATOM 2301 O O . LEU A 1 281 ? 10.236 -9.735 7.177 1.00 27.61 ? 297 LEU A O 1 ATOM 2302 C CB . LEU A 1 281 ? 9.076 -8.739 4.198 1.00 28.96 ? 297 LEU A CB 1 ATOM 2303 C CG . LEU A 1 281 ? 7.891 -8.358 5.098 1.00 29.14 ? 297 LEU A CG 1 ATOM 2304 C CD1 . LEU A 1 281 ? 8.147 -7.044 5.832 1.00 29.09 ? 297 LEU A CD1 1 ATOM 2305 C CD2 . LEU A 1 281 ? 6.580 -8.307 4.315 1.00 29.92 ? 297 LEU A CD2 1 ATOM 2306 N N A LYS A 1 282 ? 10.263 -11.320 5.566 0.50 28.07 ? 298 LYS A N 1 ATOM 2307 N N B LYS A 1 282 ? 10.254 -11.327 5.582 0.50 28.06 ? 298 LYS A N 1 ATOM 2308 C CA A LYS A 1 282 ? 10.206 -12.460 6.478 0.50 27.92 ? 298 LYS A CA 1 ATOM 2309 C CA B LYS A 1 282 ? 10.183 -12.442 6.532 0.50 27.89 ? 298 LYS A CA 1 ATOM 2310 C C A LYS A 1 282 ? 11.392 -12.483 7.445 0.50 27.22 ? 298 LYS A C 1 ATOM 2311 C C B LYS A 1 282 ? 11.400 -12.495 7.461 0.50 27.21 ? 298 LYS A C 1 ATOM 2312 O O A LYS A 1 282 ? 11.227 -12.754 8.634 0.50 27.12 ? 298 LYS A O 1 ATOM 2313 O O B LYS A 1 282 ? 11.264 -12.800 8.645 0.50 27.10 ? 298 LYS A O 1 ATOM 2314 C CB A LYS A 1 282 ? 10.161 -13.767 5.690 0.50 28.17 ? 298 LYS A CB 1 ATOM 2315 C CB B LYS A 1 282 ? 10.012 -13.783 5.812 0.50 28.19 ? 298 LYS A CB 1 ATOM 2316 C CG A LYS A 1 282 ? 10.060 -14.995 6.570 0.50 28.56 ? 298 LYS A CG 1 ATOM 2317 C CG B LYS A 1 282 ? 10.229 -14.984 6.721 0.50 28.49 ? 298 LYS A CG 1 ATOM 2318 C CD A LYS A 1 282 ? 8.843 -14.892 7.467 0.50 29.48 ? 298 LYS A CD 1 ATOM 2319 C CD B LYS A 1 282 ? 10.263 -16.295 5.946 0.50 29.21 ? 298 LYS A CD 1 ATOM 2320 C CE A LYS A 1 282 ? 8.576 -16.185 8.216 0.50 29.87 ? 298 LYS A CE 1 ATOM 2321 C CE B LYS A 1 282 ? 8.920 -17.003 5.963 0.50 29.93 ? 298 LYS A CE 1 ATOM 2322 N NZ A LYS A 1 282 ? 7.203 -16.175 8.791 0.50 30.13 ? 298 LYS A NZ 1 ATOM 2323 N NZ B LYS A 1 282 ? 8.553 -17.421 7.346 0.50 30.29 ? 298 LYS A NZ 1 ATOM 2324 N N . MET A 1 283 ? 12.581 -12.192 6.926 1.00 26.72 ? 299 MET A N 1 ATOM 2325 C CA . MET A 1 283 ? 13.811 -12.166 7.742 1.00 26.29 ? 299 MET A CA 1 ATOM 2326 C C . MET A 1 283 ? 13.735 -11.113 8.857 1.00 25.97 ? 299 MET A C 1 ATOM 2327 O O . MET A 1 283 ? 14.038 -11.414 10.009 1.00 25.71 ? 299 MET A O 1 ATOM 2328 C CB . MET A 1 283 ? 15.048 -11.980 6.863 1.00 25.89 ? 299 MET A CB 1 ATOM 2329 C CG . MET A 1 283 ? 15.310 -13.186 5.960 1.00 26.63 ? 299 MET A CG 1 ATOM 2330 S SD . MET A 1 283 ? 16.379 -12.833 4.553 1.00 26.62 ? 299 MET A SD 1 ATOM 2331 C CE . MET A 1 283 ? 17.969 -12.711 5.372 1.00 26.65 ? 299 MET A CE 1 ATOM 2332 N N . PHE A 1 284 ? 13.285 -9.905 8.521 1.00 25.76 ? 300 PHE A N 1 ATOM 2333 C CA . PHE A 1 284 ? 13.098 -8.856 9.537 1.00 25.80 ? 300 PHE A CA 1 ATOM 2334 C C . PHE A 1 284 ? 11.992 -9.191 10.534 1.00 26.09 ? 300 PHE A C 1 ATOM 2335 O O . PHE A 1 284 ? 12.147 -8.945 11.740 1.00 25.82 ? 300 PHE A O 1 ATOM 2336 C CB . PHE A 1 284 ? 12.862 -7.487 8.889 1.00 26.04 ? 300 PHE A CB 1 ATOM 2337 C CG . PHE A 1 284 ? 14.127 -6.827 8.427 1.00 25.91 ? 300 PHE A CG 1 ATOM 2338 C CD1 . PHE A 1 284 ? 14.659 -7.109 7.171 1.00 25.55 ? 300 PHE A CD1 1 ATOM 2339 C CD2 . PHE A 1 284 ? 14.801 -5.937 9.258 1.00 25.47 ? 300 PHE A CD2 1 ATOM 2340 C CE1 . PHE A 1 284 ? 15.841 -6.513 6.753 1.00 25.75 ? 300 PHE A CE1 1 ATOM 2341 C CE2 . PHE A 1 284 ? 15.981 -5.333 8.845 1.00 25.55 ? 300 PHE A CE2 1 ATOM 2342 C CZ . PHE A 1 284 ? 16.505 -5.626 7.593 1.00 25.61 ? 300 PHE A CZ 1 ATOM 2343 N N . GLN A 1 285 ? 10.897 -9.783 10.043 1.00 26.42 ? 301 GLN A N 1 ATOM 2344 C CA . GLN A 1 285 ? 9.810 -10.229 10.926 1.00 27.11 ? 301 GLN A CA 1 ATOM 2345 C C . GLN A 1 285 ? 10.314 -11.263 11.937 1.00 26.81 ? 301 GLN A C 1 ATOM 2346 O O . GLN A 1 285 ? 9.933 -11.235 13.112 1.00 26.70 ? 301 GLN A O 1 ATOM 2347 C CB . GLN A 1 285 ? 8.610 -10.758 10.113 1.00 27.52 ? 301 GLN A CB 1 ATOM 2348 C CG . GLN A 1 285 ? 7.811 -9.648 9.429 1.00 27.80 ? 301 GLN A CG 1 ATOM 2349 C CD . GLN A 1 285 ? 6.808 -10.148 8.398 1.00 28.38 ? 301 GLN A CD 1 ATOM 2350 O OE1 . GLN A 1 285 ? 6.873 -11.284 7.947 1.00 28.96 ? 301 GLN A OE1 1 ATOM 2351 N NE2 . GLN A 1 285 ? 5.874 -9.283 8.015 1.00 28.62 ? 301 GLN A NE2 1 ATOM 2352 N N . MET A 1 286 ? 11.197 -12.149 11.481 1.00 27.38 ? 302 MET A N 1 ATOM 2353 C CA . MET A 1 286 ? 11.817 -13.166 12.343 1.00 27.95 ? 302 MET A CA 1 ATOM 2354 C C . MET A 1 286 ? 12.753 -12.565 13.394 1.00 26.99 ? 302 MET A C 1 ATOM 2355 O O . MET A 1 286 ? 12.772 -13.008 14.544 1.00 26.75 ? 302 MET A O 1 ATOM 2356 C CB . MET A 1 286 ? 12.566 -14.201 11.499 1.00 29.23 ? 302 MET A CB 1 ATOM 2357 C CG . MET A 1 286 ? 11.636 -15.203 10.829 1.00 31.97 ? 302 MET A CG 1 ATOM 2358 S SD . MET A 1 286 ? 12.490 -16.304 9.688 1.00 36.26 ? 302 MET A SD 1 ATOM 2359 C CE . MET A 1 286 ? 13.579 -17.180 10.818 1.00 34.57 ? 302 MET A CE 1 ATOM 2360 N N . GLY A 1 287 ? 13.537 -11.568 12.990 1.00 26.97 ? 303 GLY A N 1 ATOM 2361 C CA . GLY A 1 287 ? 14.370 -10.808 13.938 1.00 26.48 ? 303 GLY A CA 1 ATOM 2362 C C . GLY A 1 287 ? 13.515 -10.131 15.001 1.00 27.24 ? 303 GLY A C 1 ATOM 2363 O O . GLY A 1 287 ? 13.824 -10.208 16.201 1.00 27.08 ? 303 GLY A O 1 ATOM 2364 N N . ASP A 1 288 ? 12.431 -9.486 14.562 1.00 27.02 ? 304 ASP A N 1 ATOM 2365 C CA . ASP A 1 288 ? 11.478 -8.830 15.470 1.00 28.33 ? 304 ASP A CA 1 ATOM 2366 C C . ASP A 1 288 ? 10.927 -9.846 16.477 1.00 28.58 ? 304 ASP A C 1 ATOM 2367 O O . ASP A 1 288 ? 10.884 -9.582 17.677 1.00 29.07 ? 304 ASP A O 1 ATOM 2368 C CB . ASP A 1 288 ? 10.351 -8.159 14.668 1.00 28.46 ? 304 ASP A CB 1 ATOM 2369 C CG . ASP A 1 288 ? 9.434 -7.279 15.526 1.00 29.64 ? 304 ASP A CG 1 ATOM 2370 O OD1 . ASP A 1 288 ? 9.877 -6.695 16.540 1.00 28.98 ? 304 ASP A OD1 1 ATOM 2371 O OD2 . ASP A 1 288 ? 8.247 -7.155 15.159 1.00 31.06 ? 304 ASP A OD2 1 ATOM 2372 N N . ASP A 1 289 ? 10.549 -11.020 15.979 1.00 29.02 ? 305 ASP A N 1 ATOM 2373 C CA . ASP A 1 289 ? 10.073 -12.122 16.813 1.00 29.56 ? 305 ASP A CA 1 ATOM 2374 C C . ASP A 1 289 ? 11.084 -12.508 17.901 1.00 28.06 ? 305 ASP A C 1 ATOM 2375 O O . ASP A 1 289 ? 10.698 -12.730 19.053 1.00 27.69 ? 305 ASP A O 1 ATOM 2376 C CB . ASP A 1 289 ? 9.722 -13.330 15.925 1.00 30.91 ? 305 ASP A CB 1 ATOM 2377 C CG . ASP A 1 289 ? 9.445 -14.602 16.723 1.00 33.08 ? 305 ASP A CG 1 ATOM 2378 O OD1 . ASP A 1 289 ? 8.853 -14.553 17.828 1.00 33.84 ? 305 ASP A OD1 1 ATOM 2379 O OD2 . ASP A 1 289 ? 9.802 -15.684 16.215 1.00 36.16 ? 305 ASP A OD2 1 ATOM 2380 N N . PHE A 1 290 ? 12.365 -12.600 17.533 1.00 26.99 ? 306 PHE A N 1 ATOM 2381 C CA . PHE A 1 290 ? 13.414 -12.966 18.493 1.00 26.42 ? 306 PHE A CA 1 ATOM 2382 C C . PHE A 1 290 ? 13.466 -11.969 19.655 1.00 26.15 ? 306 PHE A C 1 ATOM 2383 O O . PHE A 1 290 ? 13.426 -12.364 20.823 1.00 25.83 ? 306 PHE A O 1 ATOM 2384 C CB . PHE A 1 290 ? 14.801 -13.092 17.814 1.00 25.86 ? 306 PHE A CB 1 ATOM 2385 C CG . PHE A 1 290 ? 15.732 -14.069 18.500 1.00 25.77 ? 306 PHE A CG 1 ATOM 2386 C CD1 . PHE A 1 290 ? 16.154 -13.862 19.811 1.00 25.63 ? 306 PHE A CD1 1 ATOM 2387 C CD2 . PHE A 1 290 ? 16.189 -15.207 17.827 1.00 25.85 ? 306 PHE A CD2 1 ATOM 2388 C CE1 . PHE A 1 290 ? 17.007 -14.761 20.439 1.00 25.49 ? 306 PHE A CE1 1 ATOM 2389 C CE2 . PHE A 1 290 ? 17.042 -16.112 18.453 1.00 25.77 ? 306 PHE A CE2 1 ATOM 2390 C CZ . PHE A 1 290 ? 17.454 -15.888 19.756 1.00 25.37 ? 306 PHE A CZ 1 ATOM 2391 N N . PHE A 1 291 ? 13.546 -10.679 19.335 1.00 26.55 ? 307 PHE A N 1 ATOM 2392 C CA . PHE A 1 291 ? 13.578 -9.651 20.383 1.00 26.96 ? 307 PHE A CA 1 ATOM 2393 C C . PHE A 1 291 ? 12.322 -9.706 21.268 1.00 27.84 ? 307 PHE A C 1 ATOM 2394 O O . PHE A 1 291 ? 12.435 -9.735 22.498 1.00 28.39 ? 307 PHE A O 1 ATOM 2395 C CB . PHE A 1 291 ? 13.795 -8.250 19.796 1.00 26.77 ? 307 PHE A CB 1 ATOM 2396 C CG . PHE A 1 291 ? 15.227 -7.973 19.381 1.00 26.52 ? 307 PHE A CG 1 ATOM 2397 C CD1 . PHE A 1 291 ? 16.149 -7.450 20.290 1.00 26.55 ? 307 PHE A CD1 1 ATOM 2398 C CD2 . PHE A 1 291 ? 15.655 -8.236 18.082 1.00 26.29 ? 307 PHE A CD2 1 ATOM 2399 C CE1 . PHE A 1 291 ? 17.466 -7.194 19.906 1.00 25.58 ? 307 PHE A CE1 1 ATOM 2400 C CE2 . PHE A 1 291 ? 16.971 -7.985 17.696 1.00 25.65 ? 307 PHE A CE2 1 ATOM 2401 C CZ . PHE A 1 291 ? 17.874 -7.462 18.607 1.00 25.48 ? 307 PHE A CZ 1 ATOM 2402 N N . THR A 1 292 ? 11.139 -9.748 20.656 1.00 28.02 ? 308 THR A N 1 ATOM 2403 C CA . THR A 1 292 ? 9.888 -9.770 21.439 1.00 28.85 ? 308 THR A CA 1 ATOM 2404 C C . THR A 1 292 ? 9.757 -11.046 22.271 1.00 28.93 ? 308 THR A C 1 ATOM 2405 O O . THR A 1 292 ? 9.184 -11.011 23.353 1.00 28.83 ? 308 THR A O 1 ATOM 2406 C CB . THR A 1 292 ? 8.610 -9.513 20.600 1.00 29.23 ? 308 THR A CB 1 ATOM 2407 O OG1 . THR A 1 292 ? 8.434 -10.545 19.619 1.00 30.49 ? 308 THR A OG1 1 ATOM 2408 C CG2 . THR A 1 292 ? 8.685 -8.191 19.898 1.00 28.74 ? 308 THR A CG2 1 ATOM 2409 N N . SER A 1 293 ? 10.323 -12.156 21.788 1.00 29.34 ? 309 SER A N 1 ATOM 2410 C CA . SER A 1 293 ? 10.296 -13.429 22.527 1.00 29.75 ? 309 SER A CA 1 ATOM 2411 C C . SER A 1 293 ? 11.061 -13.345 23.850 1.00 30.21 ? 309 SER A C 1 ATOM 2412 O O . SER A 1 293 ? 10.805 -14.114 24.781 1.00 29.90 ? 309 SER A O 1 ATOM 2413 C CB . SER A 1 293 ? 10.843 -14.580 21.670 1.00 30.15 ? 309 SER A CB 1 ATOM 2414 O OG . SER A 1 293 ? 12.263 -14.618 21.684 1.00 29.52 ? 309 SER A OG 1 ATOM 2415 N N . MET A 1 294 ? 11.995 -12.399 23.924 1.00 29.84 ? 310 MET A N 1 ATOM 2416 C CA . MET A 1 294 ? 12.786 -12.167 25.129 1.00 30.35 ? 310 MET A CA 1 ATOM 2417 C C . MET A 1 294 ? 12.163 -11.067 25.995 1.00 30.78 ? 310 MET A C 1 ATOM 2418 O O . MET A 1 294 ? 12.807 -10.560 26.916 1.00 30.28 ? 310 MET A O 1 ATOM 2419 C CB . MET A 1 294 ? 14.227 -11.774 24.757 1.00 30.06 ? 310 MET A CB 1 ATOM 2420 C CG . MET A 1 294 ? 14.990 -12.834 23.976 1.00 30.22 ? 310 MET A CG 1 ATOM 2421 S SD . MET A 1 294 ? 16.604 -12.259 23.404 1.00 30.81 ? 310 MET A SD 1 ATOM 2422 C CE . MET A 1 294 ? 17.452 -11.997 24.960 1.00 30.23 ? 310 MET A CE 1 ATOM 2423 N N . ASN A 1 295 ? 10.921 -10.694 25.685 1.00 31.63 ? 311 ASN A N 1 ATOM 2424 C CA . ASN A 1 295 ? 10.209 -9.638 26.409 1.00 32.77 ? 311 ASN A CA 1 ATOM 2425 C C . ASN A 1 295 ? 10.834 -8.248 26.155 1.00 32.30 ? 311 ASN A C 1 ATOM 2426 O O . ASN A 1 295 ? 10.743 -7.347 26.992 1.00 31.65 ? 311 ASN A O 1 ATOM 2427 C CB . ASN A 1 295 ? 10.131 -9.990 27.909 1.00 34.33 ? 311 ASN A CB 1 ATOM 2428 C CG . ASN A 1 295 ? 9.106 -9.167 28.666 1.00 36.75 ? 311 ASN A CG 1 ATOM 2429 O OD1 . ASN A 1 295 ? 8.164 -8.620 28.085 1.00 37.19 ? 311 ASN A OD1 1 ATOM 2430 N ND2 . ASN A 1 295 ? 9.288 -9.081 29.988 1.00 38.58 ? 311 ASN A ND2 1 ATOM 2431 N N . LEU A 1 296 ? 11.467 -8.089 24.990 1.00 30.66 ? 312 LEU A N 1 ATOM 2432 C CA . LEU A 1 296 ? 12.024 -6.804 24.569 1.00 29.97 ? 312 LEU A CA 1 ATOM 2433 C C . LEU A 1 296 ? 11.056 -6.101 23.619 1.00 30.17 ? 312 LEU A C 1 ATOM 2434 O O . LEU A 1 296 ? 9.980 -6.630 23.339 1.00 31.53 ? 312 LEU A O 1 ATOM 2435 C CB . LEU A 1 296 ? 13.439 -6.975 23.970 1.00 28.91 ? 312 LEU A CB 1 ATOM 2436 C CG . LEU A 1 296 ? 14.553 -7.373 24.961 1.00 28.31 ? 312 LEU A CG 1 ATOM 2437 C CD1 . LEU A 1 296 ? 15.848 -7.782 24.260 1.00 28.04 ? 312 LEU A CD1 1 ATOM 2438 C CD2 . LEU A 1 296 ? 14.833 -6.266 25.973 1.00 28.34 ? 312 LEU A CD2 1 ATOM 2439 N N . THR A 1 297 ? 11.426 -4.920 23.124 1.00 29.61 ? 313 THR A N 1 ATOM 2440 C CA . THR A 1 297 ? 10.479 -4.025 22.445 1.00 28.99 ? 313 THR A CA 1 ATOM 2441 C C . THR A 1 297 ? 10.248 -4.380 20.978 1.00 30.00 ? 313 THR A C 1 ATOM 2442 O O . THR A 1 297 ? 11.200 -4.553 20.222 1.00 28.56 ? 313 THR A O 1 ATOM 2443 C CB . THR A 1 297 ? 10.942 -2.553 22.562 1.00 28.76 ? 313 THR A CB 1 ATOM 2444 O OG1 . THR A 1 297 ? 11.166 -2.241 23.943 1.00 27.86 ? 313 THR A OG1 1 ATOM 2445 C CG2 . THR A 1 297 ? 9.902 -1.585 21.988 1.00 27.85 ? 313 THR A CG2 1 ATOM 2446 N N . LYS A 1 298 ? 8.971 -4.472 20.600 1.00 30.36 ? 314 LYS A N 1 ATOM 2447 C CA . LYS A 1 298 ? 8.524 -4.713 19.223 1.00 31.28 ? 314 LYS A CA 1 ATOM 2448 C C . LYS A 1 298 ? 8.839 -3.534 18.302 1.00 30.41 ? 314 LYS A C 1 ATOM 2449 O O . LYS A 1 298 ? 8.783 -2.375 18.719 1.00 30.43 ? 314 LYS A O 1 ATOM 2450 C CB . LYS A 1 298 ? 7.009 -5.037 19.240 1.00 34.08 ? 314 LYS A CB 1 ATOM 2451 C CG . LYS A 1 298 ? 6.137 -4.329 18.206 1.00 37.49 ? 314 LYS A CG 1 ATOM 2452 C CD . LYS A 1 298 ? 4.636 -4.542 18.438 1.00 39.94 ? 314 LYS A CD 1 ATOM 2453 C CE . LYS A 1 298 ? 4.061 -3.505 19.403 1.00 42.23 ? 314 LYS A CE 1 ATOM 2454 N NZ . LYS A 1 298 ? 2.599 -3.684 19.649 1.00 44.71 ? 314 LYS A NZ 1 ATOM 2455 N N . LEU A 1 299 ? 9.183 -3.814 17.052 1.00 28.97 ? 315 LEU A N 1 ATOM 2456 C CA . LEU A 1 299 ? 9.433 -2.731 16.103 1.00 28.70 ? 315 LEU A CA 1 ATOM 2457 C C . LEU A 1 299 ? 8.169 -1.870 15.891 1.00 29.34 ? 315 LEU A C 1 ATOM 2458 O O . LEU A 1 299 ? 7.073 -2.408 15.730 1.00 29.14 ? 315 LEU A O 1 ATOM 2459 C CB . LEU A 1 299 ? 9.942 -3.284 14.774 1.00 27.98 ? 315 LEU A CB 1 ATOM 2460 C CG . LEU A 1 299 ? 11.313 -3.975 14.815 1.00 27.41 ? 315 LEU A CG 1 ATOM 2461 C CD1 . LEU A 1 299 ? 11.541 -4.794 13.550 1.00 26.91 ? 315 LEU A CD1 1 ATOM 2462 C CD2 . LEU A 1 299 ? 12.427 -2.960 15.017 1.00 26.80 ? 315 LEU A CD2 1 ATOM 2463 N N . PRO A 1 300 ? 8.318 -0.533 15.912 1.00 29.45 ? 316 PRO A N 1 ATOM 2464 C CA . PRO A 1 300 ? 7.156 0.345 15.705 1.00 30.16 ? 316 PRO A CA 1 ATOM 2465 C C . PRO A 1 300 ? 6.758 0.441 14.231 1.00 31.23 ? 316 PRO A C 1 ATOM 2466 O O . PRO A 1 300 ? 7.536 0.050 13.359 1.00 30.55 ? 316 PRO A O 1 ATOM 2467 C CB . PRO A 1 300 ? 7.649 1.707 16.214 1.00 29.68 ? 316 PRO A CB 1 ATOM 2468 C CG . PRO A 1 300 ? 9.138 1.650 16.088 1.00 29.39 ? 316 PRO A CG 1 ATOM 2469 C CD . PRO A 1 300 ? 9.536 0.219 16.282 1.00 28.61 ? 316 PRO A CD 1 ATOM 2470 N N . GLN A 1 301 ? 5.566 0.975 13.962 1.00 32.04 ? 317 GLN A N 1 ATOM 2471 C CA . GLN A 1 301 ? 5.023 1.057 12.599 1.00 32.92 ? 317 GLN A CA 1 ATOM 2472 C C . GLN A 1 301 ? 5.889 1.933 11.667 1.00 31.87 ? 317 GLN A C 1 ATOM 2473 O O . GLN A 1 301 ? 6.042 1.617 10.487 1.00 30.98 ? 317 GLN A O 1 ATOM 2474 C CB . GLN A 1 301 ? 3.556 1.544 12.648 1.00 35.19 ? 317 GLN A CB 1 ATOM 2475 C CG . GLN A 1 301 ? 2.605 0.967 11.594 1.00 37.66 ? 317 GLN A CG 1 ATOM 2476 C CD . GLN A 1 301 ? 2.808 -0.521 11.312 1.00 39.24 ? 317 GLN A CD 1 ATOM 2477 O OE1 . GLN A 1 301 ? 2.765 -1.367 12.211 1.00 41.01 ? 317 GLN A OE1 1 ATOM 2478 N NE2 . GLN A 1 301 ? 3.040 -0.843 10.048 1.00 39.55 ? 317 GLN A NE2 1 ATOM 2479 N N . ASP A 1 302 ? 6.468 3.012 12.201 1.00 30.93 ? 318 ASP A N 1 ATOM 2480 C CA . ASP A 1 302 ? 7.409 3.843 11.435 1.00 31.19 ? 318 ASP A CA 1 ATOM 2481 C C . ASP A 1 302 ? 8.535 3.002 10.820 1.00 29.99 ? 318 ASP A C 1 ATOM 2482 O O . ASP A 1 302 ? 8.930 3.236 9.668 1.00 29.97 ? 318 ASP A O 1 ATOM 2483 C CB . ASP A 1 302 ? 8.035 4.947 12.300 1.00 32.52 ? 318 ASP A CB 1 ATOM 2484 C CG . ASP A 1 302 ? 7.208 6.230 12.342 1.00 34.78 ? 318 ASP A CG 1 ATOM 2485 O OD1 . ASP A 1 302 ? 6.134 6.307 11.704 1.00 36.10 ? 318 ASP A OD1 1 ATOM 2486 O OD2 . ASP A 1 302 ? 7.654 7.183 13.027 1.00 35.42 ? 318 ASP A OD2 1 ATOM 2487 N N . PHE A 1 303 ? 9.043 2.034 11.577 1.00 28.22 ? 319 PHE A N 1 ATOM 2488 C CA . PHE A 1 303 ? 10.105 1.162 11.065 1.00 28.58 ? 319 PHE A CA 1 ATOM 2489 C C . PHE A 1 303 ? 9.664 0.442 9.788 1.00 28.89 ? 319 PHE A C 1 ATOM 2490 O O . PHE A 1 303 ? 10.371 0.482 8.768 1.00 29.28 ? 319 PHE A O 1 ATOM 2491 C CB . PHE A 1 303 ? 10.585 0.143 12.106 1.00 27.62 ? 319 PHE A CB 1 ATOM 2492 C CG . PHE A 1 303 ? 11.632 -0.807 11.572 1.00 27.75 ? 319 PHE A CG 1 ATOM 2493 C CD1 . PHE A 1 303 ? 11.262 -1.997 10.943 1.00 27.66 ? 319 PHE A CD1 1 ATOM 2494 C CD2 . PHE A 1 303 ? 12.992 -0.493 11.663 1.00 27.21 ? 319 PHE A CD2 1 ATOM 2495 C CE1 . PHE A 1 303 ? 12.221 -2.858 10.429 1.00 27.43 ? 319 PHE A CE1 1 ATOM 2496 C CE2 . PHE A 1 303 ? 13.957 -1.358 11.154 1.00 26.96 ? 319 PHE A CE2 1 ATOM 2497 C CZ . PHE A 1 303 ? 13.569 -2.538 10.533 1.00 27.13 ? 319 PHE A CZ 1 ATOM 2498 N N . TRP A 1 304 ? 8.504 -0.212 9.844 1.00 28.75 ? 320 TRP A N 1 ATOM 2499 C CA . TRP A 1 304 ? 7.986 -0.944 8.687 1.00 29.02 ? 320 TRP A CA 1 ATOM 2500 C C . TRP A 1 304 ? 7.633 -0.013 7.528 1.00 29.60 ? 320 TRP A C 1 ATOM 2501 O O . TRP A 1 304 ? 7.889 -0.340 6.371 1.00 29.45 ? 320 TRP A O 1 ATOM 2502 C CB . TRP A 1 304 ? 6.782 -1.793 9.081 1.00 29.14 ? 320 TRP A CB 1 ATOM 2503 C CG . TRP A 1 304 ? 7.079 -2.830 10.125 1.00 28.77 ? 320 TRP A CG 1 ATOM 2504 C CD1 . TRP A 1 304 ? 6.575 -2.878 11.400 1.00 28.87 ? 320 TRP A CD1 1 ATOM 2505 C CD2 . TRP A 1 304 ? 7.938 -3.977 9.989 1.00 28.64 ? 320 TRP A CD2 1 ATOM 2506 N NE1 . TRP A 1 304 ? 7.072 -3.979 12.065 1.00 28.69 ? 320 TRP A NE1 1 ATOM 2507 C CE2 . TRP A 1 304 ? 7.902 -4.674 11.221 1.00 28.54 ? 320 TRP A CE2 1 ATOM 2508 C CE3 . TRP A 1 304 ? 8.735 -4.483 8.946 1.00 28.77 ? 320 TRP A CE3 1 ATOM 2509 C CZ2 . TRP A 1 304 ? 8.632 -5.850 11.442 1.00 28.27 ? 320 TRP A CZ2 1 ATOM 2510 C CZ3 . TRP A 1 304 ? 9.466 -5.664 9.167 1.00 28.17 ? 320 TRP A CZ3 1 ATOM 2511 C CH2 . TRP A 1 304 ? 9.412 -6.324 10.409 1.00 28.27 ? 320 TRP A CH2 1 ATOM 2512 N N . ASP A 1 305 ? 7.072 1.155 7.848 1.00 29.83 ? 321 ASP A N 1 ATOM 2513 C CA . ASP A 1 305 ? 6.646 2.130 6.846 1.00 30.43 ? 321 ASP A CA 1 ATOM 2514 C C . ASP A 1 305 ? 7.805 2.766 6.091 1.00 29.99 ? 321 ASP A C 1 ATOM 2515 O O . ASP A 1 305 ? 7.689 3.026 4.893 1.00 29.61 ? 321 ASP A O 1 ATOM 2516 C CB . ASP A 1 305 ? 5.842 3.267 7.502 1.00 31.66 ? 321 ASP A CB 1 ATOM 2517 C CG . ASP A 1 305 ? 4.442 2.842 7.938 1.00 32.97 ? 321 ASP A CG 1 ATOM 2518 O OD1 . ASP A 1 305 ? 3.986 1.728 7.609 1.00 33.60 ? 321 ASP A OD1 1 ATOM 2519 O OD2 . ASP A 1 305 ? 3.791 3.643 8.627 1.00 33.95 ? 321 ASP A OD2 1 ATOM 2520 N N . LYS A 1 306 ? 8.901 3.047 6.800 1.00 28.72 ? 322 LYS A N 1 ATOM 2521 C CA . LYS A 1 306 ? 9.953 3.915 6.270 1.00 28.52 ? 322 LYS A CA 1 ATOM 2522 C C . LYS A 1 306 ? 11.291 3.223 5.955 1.00 27.72 ? 322 LYS A C 1 ATOM 2523 O O . LYS A 1 306 ? 12.146 3.814 5.281 1.00 27.85 ? 322 LYS A O 1 ATOM 2524 C CB . LYS A 1 306 ? 10.206 5.084 7.222 1.00 29.50 ? 322 LYS A CB 1 ATOM 2525 C CG . LYS A 1 306 ? 9.042 6.060 7.396 1.00 30.51 ? 322 LYS A CG 1 ATOM 2526 C CD . LYS A 1 306 ? 9.414 7.096 8.450 1.00 31.19 ? 322 LYS A CD 1 ATOM 2527 C CE . LYS A 1 306 ? 8.242 8.008 8.776 1.00 32.32 ? 322 LYS A CE 1 ATOM 2528 N NZ . LYS A 1 306 ? 8.697 9.163 9.603 1.00 33.94 ? 322 LYS A NZ 1 ATOM 2529 N N . SER A 1 307 ? 11.488 1.998 6.438 1.00 26.84 ? 323 SER A N 1 ATOM 2530 C CA . SER A 1 307 ? 12.761 1.299 6.195 1.00 26.20 ? 323 SER A CA 1 ATOM 2531 C C . SER A 1 307 ? 12.905 0.897 4.726 1.00 26.55 ? 323 SER A C 1 ATOM 2532 O O . SER A 1 307 ? 11.914 0.817 3.994 1.00 26.55 ? 323 SER A O 1 ATOM 2533 C CB . SER A 1 307 ? 12.923 0.080 7.101 1.00 25.75 ? 323 SER A CB 1 ATOM 2534 O OG . SER A 1 307 ? 13.110 0.485 8.451 1.00 25.77 ? 323 SER A OG 1 ATOM 2535 N N . ILE A 1 308 ? 14.151 0.689 4.306 1.00 26.13 ? 324 ILE A N 1 ATOM 2536 C CA . ILE A 1 308 ? 14.460 0.141 2.994 1.00 26.83 ? 324 ILE A CA 1 ATOM 2537 C C . ILE A 1 308 ? 15.152 -1.205 3.222 1.00 26.70 ? 324 ILE A C 1 ATOM 2538 O O . ILE A 1 308 ? 16.255 -1.264 3.770 1.00 25.35 ? 324 ILE A O 1 ATOM 2539 C CB . ILE A 1 308 ? 15.346 1.105 2.182 1.00 27.23 ? 324 ILE A CB 1 ATOM 2540 C CG1 . ILE A 1 308 ? 14.570 2.401 1.887 1.00 27.94 ? 324 ILE A CG1 1 ATOM 2541 C CG2 . ILE A 1 308 ? 15.827 0.442 0.898 1.00 27.71 ? 324 ILE A CG2 1 ATOM 2542 C CD1 . ILE A 1 308 ? 15.421 3.530 1.340 1.00 28.00 ? 324 ILE A CD1 1 ATOM 2543 N N . ILE A 1 309 ? 14.485 -2.288 2.838 1.00 27.35 ? 325 ILE A N 1 ATOM 2544 C CA . ILE A 1 309 ? 14.993 -3.622 3.153 1.00 28.12 ? 325 ILE A CA 1 ATOM 2545 C C . ILE A 1 309 ? 15.365 -4.456 1.924 1.00 28.98 ? 325 ILE A C 1 ATOM 2546 O O . ILE A 1 309 ? 15.699 -5.628 2.046 1.00 29.40 ? 325 ILE A O 1 ATOM 2547 C CB . ILE A 1 309 ? 14.061 -4.397 4.123 1.00 28.27 ? 325 ILE A CB 1 ATOM 2548 C CG1 . ILE A 1 309 ? 12.686 -4.665 3.496 1.00 28.42 ? 325 ILE A CG1 1 ATOM 2549 C CG2 . ILE A 1 309 ? 13.932 -3.662 5.450 1.00 27.80 ? 325 ILE A CG2 1 ATOM 2550 C CD1 . ILE A 1 309 ? 11.789 -5.538 4.353 1.00 28.72 ? 325 ILE A CD1 1 ATOM 2551 N N . GLU A 1 310 ? 15.334 -3.831 0.752 1.00 30.94 ? 326 GLU A N 1 ATOM 2552 C CA . GLU A 1 310 ? 15.766 -4.459 -0.494 1.00 32.39 ? 326 GLU A CA 1 ATOM 2553 C C . GLU A 1 310 ? 16.461 -3.419 -1.350 1.00 32.41 ? 326 GLU A C 1 ATOM 2554 O O . GLU A 1 310 ? 16.100 -2.237 -1.297 1.00 31.46 ? 326 GLU A O 1 ATOM 2555 C CB . GLU A 1 310 ? 14.562 -4.976 -1.277 1.00 35.79 ? 326 GLU A CB 1 ATOM 2556 C CG . GLU A 1 310 ? 14.023 -6.310 -0.810 1.00 39.42 ? 326 GLU A CG 1 ATOM 2557 C CD . GLU A 1 310 ? 12.916 -6.841 -1.713 1.00 42.56 ? 326 GLU A CD 1 ATOM 2558 O OE1 . GLU A 1 310 ? 12.245 -6.034 -2.392 1.00 44.23 ? 326 GLU A OE1 1 ATOM 2559 O OE2 . GLU A 1 310 ? 12.717 -8.070 -1.744 1.00 44.81 ? 326 GLU A OE2 1 ATOM 2560 N N . LYS A 1 311 ? 17.442 -3.847 -2.147 1.00 31.51 ? 327 LYS A N 1 ATOM 2561 C CA . LYS A 1 311 ? 18.082 -2.939 -3.102 1.00 32.83 ? 327 LYS A CA 1 ATOM 2562 C C . LYS A 1 311 ? 17.051 -2.458 -4.132 1.00 34.06 ? 327 LYS A C 1 ATOM 2563 O O . LYS A 1 311 ? 16.369 -3.277 -4.743 1.00 33.96 ? 327 LYS A O 1 ATOM 2564 C CB . LYS A 1 311 ? 19.281 -3.595 -3.800 1.00 32.41 ? 327 LYS A CB 1 ATOM 2565 C CG . LYS A 1 311 ? 20.139 -2.622 -4.605 1.00 32.28 ? 327 LYS A CG 1 ATOM 2566 C CD . LYS A 1 311 ? 21.397 -3.282 -5.158 1.00 32.76 ? 327 LYS A CD 1 ATOM 2567 C CE . LYS A 1 311 ? 22.239 -2.296 -5.964 1.00 33.65 ? 327 LYS A CE 1 ATOM 2568 N NZ . LYS A 1 311 ? 23.548 -2.861 -6.420 1.00 33.94 ? 327 LYS A NZ 1 ATOM 2569 N N . PRO A 1 312 ? 16.920 -1.125 -4.303 1.00 35.52 ? 328 PRO A N 1 ATOM 2570 C CA . PRO A 1 312 ? 15.987 -0.544 -5.278 1.00 37.13 ? 328 PRO A CA 1 ATOM 2571 C C . PRO A 1 312 ? 16.300 -1.000 -6.705 1.00 39.27 ? 328 PRO A C 1 ATOM 2572 O O . PRO A 1 312 ? 17.468 -1.217 -7.042 1.00 38.97 ? 328 PRO A O 1 ATOM 2573 C CB . PRO A 1 312 ? 16.227 0.965 -5.143 1.00 37.21 ? 328 PRO A CB 1 ATOM 2574 C CG . PRO A 1 312 ? 16.788 1.145 -3.776 1.00 36.64 ? 328 PRO A CG 1 ATOM 2575 C CD . PRO A 1 312 ? 17.597 -0.088 -3.499 1.00 35.36 ? 328 PRO A CD 1 ATOM 2576 N N . THR A 1 313 ? 15.268 -1.142 -7.532 1.00 41.07 ? 329 THR A N 1 ATOM 2577 C CA . THR A 1 313 ? 15.447 -1.664 -8.887 1.00 43.78 ? 329 THR A CA 1 ATOM 2578 C C . THR A 1 313 ? 15.386 -0.604 -9.992 1.00 45.81 ? 329 THR A C 1 ATOM 2579 O O . THR A 1 313 ? 15.522 -0.935 -11.172 1.00 46.82 ? 329 THR A O 1 ATOM 2580 C CB . THR A 1 313 ? 14.462 -2.810 -9.194 1.00 44.12 ? 329 THR A CB 1 ATOM 2581 O OG1 . THR A 1 313 ? 13.138 -2.410 -8.829 1.00 44.65 ? 329 THR A OG1 1 ATOM 2582 C CG2 . THR A 1 313 ? 14.842 -4.055 -8.408 1.00 43.92 ? 329 THR A CG2 1 ATOM 2583 N N . ASP A 1 314 ? 15.188 0.661 -9.619 1.00 46.63 ? 330 ASP A N 1 ATOM 2584 C CA . ASP A 1 314 ? 15.345 1.774 -10.566 1.00 47.93 ? 330 ASP A CA 1 ATOM 2585 C C . ASP A 1 314 ? 16.844 1.998 -10.835 1.00 48.86 ? 330 ASP A C 1 ATOM 2586 O O . ASP A 1 314 ? 17.687 1.254 -10.325 1.00 50.88 ? 330 ASP A O 1 ATOM 2587 C CB . ASP A 1 314 ? 14.655 3.045 -10.049 1.00 47.48 ? 330 ASP A CB 1 ATOM 2588 C CG . ASP A 1 314 ? 14.993 3.354 -8.591 1.00 48.54 ? 330 ASP A CG 1 ATOM 2589 O OD1 . ASP A 1 314 ? 16.021 2.851 -8.093 1.00 48.09 ? 330 ASP A OD1 1 ATOM 2590 O OD2 . ASP A 1 314 ? 14.235 4.103 -7.936 1.00 48.35 ? 330 ASP A OD2 1 ATOM 2591 N N . GLY A 1 315 ? 17.193 3.007 -11.623 1.00 49.21 ? 331 GLY A N 1 ATOM 2592 C CA . GLY A 1 315 ? 18.603 3.197 -11.994 1.00 48.00 ? 331 GLY A CA 1 ATOM 2593 C C . GLY A 1 315 ? 19.535 3.769 -10.931 1.00 46.05 ? 331 GLY A C 1 ATOM 2594 O O . GLY A 1 315 ? 20.746 3.848 -11.151 1.00 46.56 ? 331 GLY A O 1 ATOM 2595 N N . ARG A 1 316 ? 18.984 4.133 -9.773 1.00 44.07 ? 332 ARG A N 1 ATOM 2596 C CA . ARG A 1 316 ? 19.652 5.052 -8.838 1.00 42.27 ? 332 ARG A CA 1 ATOM 2597 C C . ARG A 1 316 ? 20.928 4.548 -8.165 1.00 41.22 ? 332 ARG A C 1 ATOM 2598 O O . ARG A 1 316 ? 21.112 3.346 -7.954 1.00 41.13 ? 332 ARG A O 1 ATOM 2599 C CB . ARG A 1 316 ? 18.669 5.557 -7.780 1.00 41.58 ? 332 ARG A CB 1 ATOM 2600 C CG . ARG A 1 316 ? 18.568 4.714 -6.519 1.00 41.71 ? 332 ARG A CG 1 ATOM 2601 C CD . ARG A 1 316 ? 17.113 4.625 -6.120 1.00 43.41 ? 332 ARG A CD 1 ATOM 2602 N NE . ARG A 1 316 ? 16.893 4.671 -4.686 1.00 43.94 ? 332 ARG A NE 1 ATOM 2603 C CZ . ARG A 1 316 ? 15.697 4.569 -4.117 1.00 43.12 ? 332 ARG A CZ 1 ATOM 2604 N NH1 . ARG A 1 316 ? 14.611 4.396 -4.856 1.00 42.53 ? 332 ARG A NH1 1 ATOM 2605 N NH2 . ARG A 1 316 ? 15.589 4.627 -2.800 1.00 43.65 ? 332 ARG A NH2 1 ATOM 2606 N N . ASP A 1 317 ? 21.802 5.494 -7.837 1.00 39.73 ? 333 ASP A N 1 ATOM 2607 C CA . ASP A 1 317 ? 22.949 5.227 -6.991 1.00 38.35 ? 333 ASP A CA 1 ATOM 2608 C C . ASP A 1 317 ? 22.535 5.388 -5.535 1.00 36.27 ? 333 ASP A C 1 ATOM 2609 O O . ASP A 1 317 ? 21.754 6.283 -5.202 1.00 35.93 ? 333 ASP A O 1 ATOM 2610 C CB . ASP A 1 317 ? 24.093 6.181 -7.329 1.00 40.01 ? 333 ASP A CB 1 ATOM 2611 C CG . ASP A 1 317 ? 24.707 5.891 -8.687 1.00 42.55 ? 333 ASP A CG 1 ATOM 2612 O OD1 . ASP A 1 317 ? 25.202 4.758 -8.883 1.00 44.15 ? 333 ASP A OD1 1 ATOM 2613 O OD2 . ASP A 1 317 ? 24.700 6.795 -9.551 1.00 43.38 ? 333 ASP A OD2 1 ATOM 2614 N N . LEU A 1 318 ? 23.036 4.497 -4.683 1.00 33.47 ? 334 LEU A N 1 ATOM 2615 C CA . LEU A 1 318 ? 22.801 4.566 -3.235 1.00 31.90 ? 334 LEU A CA 1 ATOM 2616 C C . LEU A 1 318 ? 23.941 3.903 -2.473 1.00 30.42 ? 334 LEU A C 1 ATOM 2617 O O . LEU A 1 318 ? 24.762 3.206 -3.062 1.00 29.75 ? 334 LEU A O 1 ATOM 2618 C CB . LEU A 1 318 ? 21.467 3.900 -2.851 1.00 31.90 ? 334 LEU A CB 1 ATOM 2619 C CG . LEU A 1 318 ? 21.388 2.367 -2.853 1.00 32.37 ? 334 LEU A CG 1 ATOM 2620 C CD1 . LEU A 1 318 ? 20.360 1.859 -1.852 1.00 32.25 ? 334 LEU A CD1 1 ATOM 2621 C CD2 . LEU A 1 318 ? 21.106 1.817 -4.248 1.00 32.69 ? 334 LEU A CD2 1 ATOM 2622 N N . VAL A 1 319 ? 23.975 4.117 -1.157 1.00 29.06 ? 335 VAL A N 1 ATOM 2623 C CA . VAL A 1 319 ? 24.882 3.386 -0.274 1.00 28.39 ? 335 VAL A CA 1 ATOM 2624 C C . VAL A 1 319 ? 24.172 2.101 0.140 1.00 27.81 ? 335 VAL A C 1 ATOM 2625 O O . VAL A 1 319 ? 23.125 2.158 0.787 1.00 27.25 ? 335 VAL A O 1 ATOM 2626 C CB . VAL A 1 319 ? 25.259 4.217 0.983 1.00 27.51 ? 335 VAL A CB 1 ATOM 2627 C CG1 . VAL A 1 319 ? 26.212 3.438 1.884 1.00 26.86 ? 335 VAL A CG1 1 ATOM 2628 C CG2 . VAL A 1 319 ? 25.887 5.543 0.572 1.00 27.40 ? 335 VAL A CG2 1 ATOM 2629 N N . CYS A 1 320 ? 24.718 0.955 -0.266 1.00 27.55 ? 336 CYS A N 1 ATOM 2630 C CA . CYS A 1 320 ? 24.146 -0.334 0.111 1.00 28.29 ? 336 CYS A CA 1 ATOM 2631 C C . CYS A 1 320 ? 24.740 -0.915 1.384 1.00 27.46 ? 336 CYS A C 1 ATOM 2632 O O . CYS A 1 320 ? 24.149 -1.835 1.950 1.00 29.22 ? 336 CYS A O 1 ATOM 2633 C CB . CYS A 1 320 ? 24.238 -1.377 -1.015 1.00 29.76 ? 336 CYS A CB 1 ATOM 2634 S SG . CYS A 1 320 ? 22.739 -1.609 -2.018 1.00 32.62 ? 336 CYS A SG 1 ATOM 2635 N N . HIS A 1 321 ? 25.894 -0.417 1.834 1.00 25.60 ? 337 HIS A N 1 ATOM 2636 C CA . HIS A 1 321 ? 26.444 -0.908 3.102 1.00 23.97 ? 337 HIS A CA 1 ATOM 2637 C C . HIS A 1 321 ? 25.391 -0.704 4.185 1.00 24.12 ? 337 HIS A C 1 ATOM 2638 O O . HIS A 1 321 ? 24.904 0.421 4.368 1.00 24.20 ? 337 HIS A O 1 ATOM 2639 C CB . HIS A 1 321 ? 27.765 -0.224 3.487 1.00 22.97 ? 337 HIS A CB 1 ATOM 2640 C CG . HIS A 1 321 ? 28.469 -0.907 4.619 1.00 22.19 ? 337 HIS A CG 1 ATOM 2641 N ND1 . HIS A 1 321 ? 29.490 -1.811 4.426 1.00 21.72 ? 337 HIS A ND1 1 ATOM 2642 C CD2 . HIS A 1 321 ? 28.267 -0.849 5.958 1.00 22.01 ? 337 HIS A CD2 1 ATOM 2643 C CE1 . HIS A 1 321 ? 29.893 -2.276 5.595 1.00 22.23 ? 337 HIS A CE1 1 ATOM 2644 N NE2 . HIS A 1 321 ? 29.167 -1.710 6.543 1.00 21.78 ? 337 HIS A NE2 1 ATOM 2645 N N . ALA A 1 322 ? 25.050 -1.784 4.896 1.00 23.46 ? 338 ALA A N 1 ATOM 2646 C CA . ALA A 1 322 ? 23.903 -1.797 5.819 1.00 23.63 ? 338 ALA A CA 1 ATOM 2647 C C . ALA A 1 322 ? 24.036 -0.791 6.966 1.00 23.70 ? 338 ALA A C 1 ATOM 2648 O O . ALA A 1 322 ? 25.142 -0.561 7.481 1.00 23.69 ? 338 ALA A O 1 ATOM 2649 C CB . ALA A 1 322 ? 23.689 -3.199 6.369 1.00 23.11 ? 338 ALA A CB 1 ATOM 2650 N N . SER A 1 323 ? 22.913 -0.198 7.376 1.00 23.33 ? 339 SER A N 1 ATOM 2651 C CA . SER A 1 323 ? 22.927 0.763 8.477 1.00 22.94 ? 339 SER A CA 1 ATOM 2652 C C . SER A 1 323 ? 21.584 0.910 9.199 1.00 23.05 ? 339 SER A C 1 ATOM 2653 O O . SER A 1 323 ? 20.520 0.692 8.617 1.00 22.68 ? 339 SER A O 1 ATOM 2654 C CB . SER A 1 323 ? 23.407 2.132 7.987 1.00 23.16 ? 339 SER A CB 1 ATOM 2655 O OG . SER A 1 323 ? 22.486 2.678 7.061 1.00 24.89 ? 339 SER A OG 1 ATOM 2656 N N . ALA A 1 324 ? 21.663 1.278 10.478 1.00 22.28 ? 340 ALA A N 1 ATOM 2657 C CA . ALA A 1 324 ? 20.497 1.530 11.330 1.00 22.68 ? 340 ALA A CA 1 ATOM 2658 C C . ALA A 1 324 ? 20.480 3.009 11.753 1.00 22.90 ? 340 ALA A C 1 ATOM 2659 O O . ALA A 1 324 ? 21.539 3.603 12.016 1.00 22.03 ? 340 ALA A O 1 ATOM 2660 C CB . ALA A 1 324 ? 20.539 0.629 12.555 1.00 22.28 ? 340 ALA A CB 1 ATOM 2661 N N . TRP A 1 325 ? 19.281 3.585 11.822 1.00 23.44 ? 341 TRP A N 1 ATOM 2662 C CA . TRP A 1 325 ? 19.104 5.032 11.902 1.00 24.51 ? 341 TRP A CA 1 ATOM 2663 C C . TRP A 1 325 ? 18.156 5.420 13.034 1.00 25.05 ? 341 TRP A C 1 ATOM 2664 O O . TRP A 1 325 ? 17.049 4.874 13.136 1.00 24.66 ? 341 TRP A O 1 ATOM 2665 C CB . TRP A 1 325 ? 18.549 5.561 10.577 1.00 24.77 ? 341 TRP A CB 1 ATOM 2666 C CG . TRP A 1 325 ? 19.488 5.433 9.429 1.00 25.42 ? 341 TRP A CG 1 ATOM 2667 C CD1 . TRP A 1 325 ? 19.818 4.282 8.758 1.00 25.55 ? 341 TRP A CD1 1 ATOM 2668 C CD2 . TRP A 1 325 ? 20.220 6.489 8.794 1.00 26.02 ? 341 TRP A CD2 1 ATOM 2669 N NE1 . TRP A 1 325 ? 20.711 4.560 7.752 1.00 25.61 ? 341 TRP A NE1 1 ATOM 2670 C CE2 . TRP A 1 325 ? 20.976 5.904 7.749 1.00 25.94 ? 341 TRP A CE2 1 ATOM 2671 C CE3 . TRP A 1 325 ? 20.306 7.875 9.000 1.00 26.41 ? 341 TRP A CE3 1 ATOM 2672 C CZ2 . TRP A 1 325 ? 21.811 6.653 6.917 1.00 26.65 ? 341 TRP A CZ2 1 ATOM 2673 C CZ3 . TRP A 1 325 ? 21.137 8.624 8.168 1.00 27.35 ? 341 TRP A CZ3 1 ATOM 2674 C CH2 . TRP A 1 325 ? 21.879 8.009 7.139 1.00 27.11 ? 341 TRP A CH2 1 ATOM 2675 N N . ASP A 1 326 ? 18.609 6.339 13.889 1.00 25.19 ? 342 ASP A N 1 ATOM 2676 C CA . ASP A 1 326 ? 17.792 6.876 14.977 1.00 25.48 ? 342 ASP A CA 1 ATOM 2677 C C . ASP A 1 326 ? 17.439 8.331 14.656 1.00 25.66 ? 342 ASP A C 1 ATOM 2678 O O . ASP A 1 326 ? 18.328 9.163 14.448 1.00 25.58 ? 342 ASP A O 1 ATOM 2679 C CB . ASP A 1 326 ? 18.547 6.789 16.314 1.00 25.38 ? 342 ASP A CB 1 ATOM 2680 C CG . ASP A 1 326 ? 17.681 7.150 17.513 1.00 26.72 ? 342 ASP A CG 1 ATOM 2681 O OD1 . ASP A 1 326 ? 16.509 7.563 17.317 1.00 27.33 ? 342 ASP A OD1 1 ATOM 2682 O OD2 . ASP A 1 326 ? 18.173 7.024 18.666 1.00 25.80 ? 342 ASP A OD2 1 ATOM 2683 N N . PHE A 1 327 ? 16.147 8.643 14.621 1.00 26.08 ? 343 PHE A N 1 ATOM 2684 C CA . PHE A 1 327 ? 15.709 9.986 14.231 1.00 26.85 ? 343 PHE A CA 1 ATOM 2685 C C . PHE A 1 327 ? 15.407 10.937 15.395 1.00 27.46 ? 343 PHE A C 1 ATOM 2686 O O . PHE A 1 327 ? 15.038 12.101 15.182 1.00 28.43 ? 343 PHE A O 1 ATOM 2687 C CB . PHE A 1 327 ? 14.576 9.903 13.195 1.00 27.26 ? 343 PHE A CB 1 ATOM 2688 C CG . PHE A 1 327 ? 15.055 9.442 11.851 1.00 27.18 ? 343 PHE A CG 1 ATOM 2689 C CD1 . PHE A 1 327 ? 15.203 8.087 11.578 1.00 27.24 ? 343 PHE A CD1 1 ATOM 2690 C CD2 . PHE A 1 327 ? 15.420 10.365 10.877 1.00 27.85 ? 343 PHE A CD2 1 ATOM 2691 C CE1 . PHE A 1 327 ? 15.679 7.663 10.347 1.00 27.13 ? 343 PHE A CE1 1 ATOM 2692 C CE2 . PHE A 1 327 ? 15.893 9.952 9.641 1.00 27.32 ? 343 PHE A CE2 1 ATOM 2693 C CZ . PHE A 1 327 ? 16.028 8.595 9.378 1.00 27.58 ? 343 PHE A CZ 1 ATOM 2694 N N . TYR A 1 328 ? 15.599 10.433 16.611 1.00 27.74 ? 344 TYR A N 1 ATOM 2695 C CA . TYR A 1 328 ? 15.597 11.228 17.853 1.00 28.75 ? 344 TYR A CA 1 ATOM 2696 C C . TYR A 1 328 ? 14.247 11.838 18.234 1.00 29.07 ? 344 TYR A C 1 ATOM 2697 O O . TYR A 1 328 ? 14.192 12.852 18.927 1.00 29.19 ? 344 TYR A O 1 ATOM 2698 C CB . TYR A 1 328 ? 16.692 12.300 17.835 1.00 30.16 ? 344 TYR A CB 1 ATOM 2699 C CG . TYR A 1 328 ? 18.074 11.726 17.660 1.00 31.88 ? 344 TYR A CG 1 ATOM 2700 C CD1 . TYR A 1 328 ? 18.695 11.018 18.691 1.00 33.19 ? 344 TYR A CD1 1 ATOM 2701 C CD2 . TYR A 1 328 ? 18.756 11.879 16.462 1.00 33.54 ? 344 TYR A CD2 1 ATOM 2702 C CE1 . TYR A 1 328 ? 19.960 10.473 18.527 1.00 34.91 ? 344 TYR A CE1 1 ATOM 2703 C CE2 . TYR A 1 328 ? 20.024 11.346 16.287 1.00 35.17 ? 344 TYR A CE2 1 ATOM 2704 C CZ . TYR A 1 328 ? 20.616 10.649 17.318 1.00 35.85 ? 344 TYR A CZ 1 ATOM 2705 O OH . TYR A 1 328 ? 21.872 10.130 17.130 1.00 40.35 ? 344 TYR A OH 1 ATOM 2706 N N . LEU A 1 329 ? 13.170 11.224 17.760 1.00 29.01 ? 345 LEU A N 1 ATOM 2707 C CA . LEU A 1 329 ? 11.827 11.592 18.184 1.00 29.37 ? 345 LEU A CA 1 ATOM 2708 C C . LEU A 1 329 ? 11.331 10.453 19.075 1.00 29.45 ? 345 LEU A C 1 ATOM 2709 O O . LEU A 1 329 ? 12.071 9.993 19.962 1.00 28.92 ? 345 LEU A O 1 ATOM 2710 C CB . LEU A 1 329 ? 10.919 11.854 16.971 1.00 29.03 ? 345 LEU A CB 1 ATOM 2711 C CG . LEU A 1 329 ? 11.408 12.868 15.919 1.00 29.58 ? 345 LEU A CG 1 ATOM 2712 C CD1 . LEU A 1 329 ? 10.452 12.927 14.731 1.00 29.95 ? 345 LEU A CD1 1 ATOM 2713 C CD2 . LEU A 1 329 ? 11.643 14.260 16.492 1.00 29.32 ? 345 LEU A CD2 1 ATOM 2714 N N . THR A 1 330 ? 10.099 10.009 18.862 1.00 29.33 ? 346 THR A N 1 ATOM 2715 C CA . THR A 1 330 ? 9.591 8.808 19.512 1.00 30.20 ? 346 THR A CA 1 ATOM 2716 C C . THR A 1 330 ? 9.285 7.788 18.405 1.00 30.16 ? 346 THR A C 1 ATOM 2717 O O . THR A 1 330 ? 8.512 8.078 17.487 1.00 30.44 ? 346 THR A O 1 ATOM 2718 C CB . THR A 1 330 ? 8.323 9.096 20.363 1.00 31.61 ? 346 THR A CB 1 ATOM 2719 O OG1 . THR A 1 330 ? 8.598 10.148 21.308 1.00 34.11 ? 346 THR A OG1 1 ATOM 2720 C CG2 . THR A 1 330 ? 7.859 7.844 21.120 1.00 31.60 ? 346 THR A CG2 1 ATOM 2721 N N . ASP A 1 331 ? 9.927 6.622 18.470 1.00 29.57 ? 347 ASP A N 1 ATOM 2722 C CA . ASP A 1 331 ? 9.621 5.486 17.584 1.00 29.29 ? 347 ASP A CA 1 ATOM 2723 C C . ASP A 1 331 ? 9.932 5.679 16.097 1.00 28.98 ? 347 ASP A C 1 ATOM 2724 O O . ASP A 1 331 ? 9.538 4.848 15.284 1.00 28.41 ? 347 ASP A O 1 ATOM 2725 C CB . ASP A 1 331 ? 8.147 5.056 17.729 1.00 29.97 ? 347 ASP A CB 1 ATOM 2726 C CG . ASP A 1 331 ? 7.865 4.373 19.044 1.00 30.58 ? 347 ASP A CG 1 ATOM 2727 O OD1 . ASP A 1 331 ? 8.817 4.047 19.793 1.00 30.43 ? 347 ASP A OD1 1 ATOM 2728 O OD2 . ASP A 1 331 ? 6.677 4.146 19.327 1.00 31.65 ? 347 ASP A OD2 1 ATOM 2729 N N . ASP A 1 332 ? 10.618 6.759 15.731 1.00 28.67 ? 348 ASP A N 1 ATOM 2730 C CA . ASP A 1 332 ? 11.036 6.913 14.340 1.00 28.55 ? 348 ASP A CA 1 ATOM 2731 C C . ASP A 1 332 ? 12.456 6.371 14.237 1.00 27.49 ? 348 ASP A C 1 ATOM 2732 O O . ASP A 1 332 ? 13.428 7.074 14.511 1.00 26.65 ? 348 ASP A O 1 ATOM 2733 C CB . ASP A 1 332 ? 10.930 8.363 13.860 1.00 30.28 ? 348 ASP A CB 1 ATOM 2734 C CG . ASP A 1 332 ? 11.143 8.507 12.349 1.00 31.90 ? 348 ASP A CG 1 ATOM 2735 O OD1 . ASP A 1 332 ? 11.585 7.548 11.676 1.00 32.91 ? 348 ASP A OD1 1 ATOM 2736 O OD2 . ASP A 1 332 ? 10.870 9.605 11.830 1.00 33.96 ? 348 ASP A OD2 1 ATOM 2737 N N . VAL A 1 333 ? 12.536 5.093 13.880 1.00 27.11 ? 349 VAL A N 1 ATOM 2738 C CA . VAL A 1 333 ? 13.791 4.354 13.713 1.00 26.21 ? 349 VAL A CA 1 ATOM 2739 C C . VAL A 1 333 ? 13.677 3.545 12.415 1.00 26.72 ? 349 VAL A C 1 ATOM 2740 O O . VAL A 1 333 ? 12.578 3.104 12.069 1.00 27.46 ? 349 VAL A O 1 ATOM 2741 C CB . VAL A 1 333 ? 14.087 3.413 14.915 1.00 25.52 ? 349 VAL A CB 1 ATOM 2742 C CG1 . VAL A 1 333 ? 14.406 4.208 16.174 1.00 25.38 ? 349 VAL A CG1 1 ATOM 2743 C CG2 . VAL A 1 333 ? 12.936 2.444 15.178 1.00 25.82 ? 349 VAL A CG2 1 ATOM 2744 N N . ARG A 1 334 ? 14.793 3.348 11.708 1.00 26.03 ? 350 ARG A N 1 ATOM 2745 C CA . ARG A 1 334 ? 14.775 2.735 10.370 1.00 25.98 ? 350 ARG A CA 1 ATOM 2746 C C . ARG A 1 334 ? 16.056 1.980 10.075 1.00 25.14 ? 350 ARG A C 1 ATOM 2747 O O . ARG A 1 334 ? 17.124 2.317 10.598 1.00 24.42 ? 350 ARG A O 1 ATOM 2748 C CB . ARG A 1 334 ? 14.680 3.803 9.278 1.00 26.97 ? 350 ARG A CB 1 ATOM 2749 C CG . ARG A 1 334 ? 13.449 4.665 9.280 1.00 28.53 ? 350 ARG A CG 1 ATOM 2750 C CD . ARG A 1 334 ? 13.601 5.799 8.285 1.00 28.63 ? 350 ARG A CD 1 ATOM 2751 N NE . ARG A 1 334 ? 12.902 6.955 8.813 1.00 29.19 ? 350 ARG A NE 1 ATOM 2752 C CZ . ARG A 1 334 ? 12.894 8.159 8.262 1.00 29.95 ? 350 ARG A CZ 1 ATOM 2753 N NH1 . ARG A 1 334 ? 13.536 8.391 7.124 1.00 30.63 ? 350 ARG A NH1 1 ATOM 2754 N NH2 . ARG A 1 334 ? 12.231 9.135 8.863 1.00 31.09 ? 350 ARG A NH2 1 ATOM 2755 N N . ILE A 1 335 ? 15.951 1.001 9.177 1.00 24.50 ? 351 ILE A N 1 ATOM 2756 C CA . ILE A 1 335 ? 17.119 0.324 8.620 1.00 23.55 ? 351 ILE A CA 1 ATOM 2757 C C . ILE A 1 335 ? 17.143 0.537 7.107 1.00 24.02 ? 351 ILE A C 1 ATOM 2758 O O . ILE A 1 335 ? 16.091 0.659 6.470 1.00 23.85 ? 351 ILE A O 1 ATOM 2759 C CB . ILE A 1 335 ? 17.139 -1.175 9.020 1.00 23.64 ? 351 ILE A CB 1 ATOM 2760 C CG1 . ILE A 1 335 ? 17.625 -1.311 10.467 1.00 22.97 ? 351 ILE A CG1 1 ATOM 2761 C CG2 . ILE A 1 335 ? 18.023 -2.012 8.098 1.00 23.50 ? 351 ILE A CG2 1 ATOM 2762 C CD1 . ILE A 1 335 ? 17.371 -2.672 11.078 1.00 23.54 ? 351 ILE A CD1 1 ATOM 2763 N N . LYS A 1 336 ? 18.349 0.650 6.555 1.00 23.89 ? 352 LYS A N 1 ATOM 2764 C CA . LYS A 1 336 ? 18.566 0.569 5.110 1.00 24.04 ? 352 LYS A CA 1 ATOM 2765 C C . LYS A 1 336 ? 19.522 -0.599 4.862 1.00 24.23 ? 352 LYS A C 1 ATOM 2766 O O . LYS A 1 336 ? 20.709 -0.532 5.216 1.00 24.05 ? 352 LYS A O 1 ATOM 2767 C CB . LYS A 1 336 ? 19.139 1.882 4.568 1.00 23.98 ? 352 LYS A CB 1 ATOM 2768 C CG . LYS A 1 336 ? 19.407 1.888 3.060 1.00 23.97 ? 352 LYS A CG 1 ATOM 2769 C CD . LYS A 1 336 ? 19.500 3.301 2.490 1.00 24.38 ? 352 LYS A CD 1 ATOM 2770 C CE . LYS A 1 336 ? 20.593 4.149 3.131 1.00 23.97 ? 352 LYS A CE 1 ATOM 2771 N NZ . LYS A 1 336 ? 21.962 3.633 2.839 1.00 24.00 ? 352 LYS A NZ 1 ATOM 2772 N N . GLN A 1 337 ? 19.001 -1.680 4.286 1.00 24.64 ? 353 GLN A N 1 ATOM 2773 C CA . GLN A 1 337 ? 19.808 -2.873 4.018 1.00 24.57 ? 353 GLN A CA 1 ATOM 2774 C C . GLN A 1 337 ? 19.437 -3.436 2.659 1.00 25.26 ? 353 GLN A C 1 ATOM 2775 O O . GLN A 1 337 ? 18.248 -3.600 2.352 1.00 25.80 ? 353 GLN A O 1 ATOM 2776 C CB . GLN A 1 337 ? 19.604 -3.930 5.108 1.00 24.44 ? 353 GLN A CB 1 ATOM 2777 C CG . GLN A 1 337 ? 20.445 -5.199 4.935 1.00 24.42 ? 353 GLN A CG 1 ATOM 2778 C CD . GLN A 1 337 ? 20.345 -6.165 6.110 1.00 24.20 ? 353 GLN A CD 1 ATOM 2779 O OE1 . GLN A 1 337 ? 19.993 -5.780 7.228 1.00 24.69 ? 353 GLN A OE1 1 ATOM 2780 N NE2 . GLN A 1 337 ? 20.666 -7.430 5.862 1.00 24.04 ? 353 GLN A NE2 1 ATOM 2781 N N . CYS A 1 338 ? 20.446 -3.697 1.832 1.00 25.75 ? 354 CYS A N 1 ATOM 2782 C CA . CYS A 1 338 ? 20.213 -4.330 0.533 1.00 26.30 ? 354 CYS A CA 1 ATOM 2783 C C . CYS A 1 338 ? 20.166 -5.846 0.751 1.00 25.87 ? 354 CYS A C 1 ATOM 2784 O O . CYS A 1 338 ? 21.060 -6.583 0.338 1.00 25.72 ? 354 CYS A O 1 ATOM 2785 C CB . CYS A 1 338 ? 21.268 -3.873 -0.490 1.00 27.30 ? 354 CYS A CB 1 ATOM 2786 S SG . CYS A 1 338 ? 21.226 -2.072 -0.718 1.00 28.53 ? 354 CYS A SG 1 ATOM 2787 N N . THR A 1 339 ? 19.099 -6.289 1.417 1.00 25.48 ? 355 THR A N 1 ATOM 2788 C CA . THR A 1 339 ? 18.998 -7.640 1.971 1.00 25.44 ? 355 THR A CA 1 ATOM 2789 C C . THR A 1 339 ? 19.012 -8.732 0.907 1.00 26.08 ? 355 THR A C 1 ATOM 2790 O O . THR A 1 339 ? 18.347 -8.614 -0.127 1.00 26.06 ? 355 THR A O 1 ATOM 2791 C CB . THR A 1 339 ? 17.730 -7.806 2.837 1.00 25.90 ? 355 THR A CB 1 ATOM 2792 O OG1 . THR A 1 339 ? 17.562 -6.661 3.684 1.00 25.27 ? 355 THR A OG1 1 ATOM 2793 C CG2 . THR A 1 339 ? 17.815 -9.065 3.695 1.00 25.63 ? 355 THR A CG2 1 ATOM 2794 N N . ARG A 1 340 ? 19.790 -9.777 1.172 1.00 26.20 ? 356 ARG A N 1 ATOM 2795 C CA . ARG A 1 340 ? 19.806 -10.979 0.339 1.00 27.30 ? 356 ARG A CA 1 ATOM 2796 C C . ARG A 1 340 ? 19.379 -12.170 1.195 1.00 27.08 ? 356 ARG A C 1 ATOM 2797 O O . ARG A 1 340 ? 19.473 -12.114 2.427 1.00 27.25 ? 356 ARG A O 1 ATOM 2798 C CB . ARG A 1 340 ? 21.196 -11.190 -0.285 1.00 27.65 ? 356 ARG A CB 1 ATOM 2799 C CG . ARG A 1 340 ? 21.578 -10.115 -1.300 1.00 28.73 ? 356 ARG A CG 1 ATOM 2800 C CD . ARG A 1 340 ? 23.077 -10.063 -1.586 1.00 28.89 ? 356 ARG A CD 1 ATOM 2801 N NE . ARG A 1 340 ? 23.848 -9.625 -0.421 1.00 29.56 ? 356 ARG A NE 1 ATOM 2802 C CZ . ARG A 1 340 ? 24.590 -10.428 0.335 1.00 29.52 ? 356 ARG A CZ 1 ATOM 2803 N NH1 . ARG A 1 340 ? 24.675 -11.725 0.060 1.00 30.04 ? 356 ARG A NH1 1 ATOM 2804 N NH2 . ARG A 1 340 ? 25.254 -9.936 1.372 1.00 29.97 ? 356 ARG A NH2 1 ATOM 2805 N N . VAL A 1 341 ? 18.894 -13.229 0.550 1.00 26.63 ? 357 VAL A N 1 ATOM 2806 C CA . VAL A 1 341 ? 18.408 -14.427 1.247 1.00 26.50 ? 357 VAL A CA 1 ATOM 2807 C C . VAL A 1 341 ? 19.560 -15.433 1.479 1.00 26.22 ? 357 VAL A C 1 ATOM 2808 O O . VAL A 1 341 ? 19.706 -16.406 0.737 1.00 26.42 ? 357 VAL A O 1 ATOM 2809 C CB . VAL A 1 341 ? 17.202 -15.073 0.496 1.00 26.48 ? 357 VAL A CB 1 ATOM 2810 C CG1 . VAL A 1 341 ? 16.636 -16.268 1.258 1.00 26.56 ? 357 VAL A CG1 1 ATOM 2811 C CG2 . VAL A 1 341 ? 16.101 -14.047 0.263 1.00 26.83 ? 357 VAL A CG2 1 ATOM 2812 N N . THR A 1 342 ? 20.384 -15.179 2.501 1.00 25.85 ? 358 THR A N 1 ATOM 2813 C CA . THR A 1 342 ? 21.499 -16.073 2.865 1.00 25.89 ? 358 THR A CA 1 ATOM 2814 C C . THR A 1 342 ? 21.589 -16.211 4.384 1.00 25.96 ? 358 THR A C 1 ATOM 2815 O O . THR A 1 342 ? 21.026 -15.389 5.120 1.00 25.35 ? 358 THR A O 1 ATOM 2816 C CB . THR A 1 342 ? 22.882 -15.551 2.392 1.00 25.80 ? 358 THR A CB 1 ATOM 2817 O OG1 . THR A 1 342 ? 23.265 -14.417 3.188 1.00 25.97 ? 358 THR A OG1 1 ATOM 2818 C CG2 . THR A 1 342 ? 22.896 -15.185 0.910 1.00 25.76 ? 358 THR A CG2 1 ATOM 2819 N N . GLN A 1 343 ? 22.315 -17.233 4.836 1.00 25.98 ? 359 GLN A N 1 ATOM 2820 C CA . GLN A 1 343 ? 22.597 -17.453 6.259 1.00 26.99 ? 359 GLN A CA 1 ATOM 2821 C C . GLN A 1 343 ? 23.296 -16.220 6.882 1.00 26.92 ? 359 GLN A C 1 ATOM 2822 O O . GLN A 1 343 ? 22.853 -15.697 7.911 1.00 26.31 ? 359 GLN A O 1 ATOM 2823 C CB . GLN A 1 343 ? 23.451 -18.721 6.436 1.00 27.35 ? 359 GLN A CB 1 ATOM 2824 C CG . GLN A 1 343 ? 23.985 -18.944 7.845 1.00 28.56 ? 359 GLN A CG 1 ATOM 2825 C CD . GLN A 1 343 ? 24.558 -20.338 8.063 1.00 29.11 ? 359 GLN A CD 1 ATOM 2826 O OE1 . GLN A 1 343 ? 23.918 -21.341 7.757 1.00 29.64 ? 359 GLN A OE1 1 ATOM 2827 N NE2 . GLN A 1 343 ? 25.762 -20.402 8.618 1.00 29.57 ? 359 GLN A NE2 1 ATOM 2828 N N . ASP A 1 344 ? 24.371 -15.765 6.239 1.00 26.92 ? 360 ASP A N 1 ATOM 2829 C CA . ASP A 1 344 ? 25.124 -14.590 6.675 1.00 28.40 ? 360 ASP A CA 1 ATOM 2830 C C . ASP A 1 344 ? 24.212 -13.353 6.801 1.00 26.84 ? 360 ASP A C 1 ATOM 2831 O O . ASP A 1 344 ? 24.333 -12.571 7.747 1.00 25.86 ? 360 ASP A O 1 ATOM 2832 C CB . ASP A 1 344 ? 26.266 -14.341 5.677 1.00 32.22 ? 360 ASP A CB 1 ATOM 2833 C CG . ASP A 1 344 ? 27.004 -13.042 5.927 1.00 36.68 ? 360 ASP A CG 1 ATOM 2834 O OD1 . ASP A 1 344 ? 27.700 -12.936 6.960 1.00 41.35 ? 360 ASP A OD1 1 ATOM 2835 O OD2 . ASP A 1 344 ? 26.907 -12.131 5.071 1.00 39.90 ? 360 ASP A OD2 1 ATOM 2836 N N . GLN A 1 345 ? 23.295 -13.196 5.850 1.00 25.64 ? 361 GLN A N 1 ATOM 2837 C CA . GLN A 1 345 ? 22.343 -12.081 5.869 1.00 25.12 ? 361 GLN A CA 1 ATOM 2838 C C . GLN A 1 345 ? 21.281 -12.187 6.974 1.00 25.23 ? 361 GLN A C 1 ATOM 2839 O O . GLN A 1 345 ? 20.827 -11.161 7.492 1.00 24.77 ? 361 GLN A O 1 ATOM 2840 C CB . GLN A 1 345 ? 21.706 -11.893 4.497 1.00 24.68 ? 361 GLN A CB 1 ATOM 2841 C CG . GLN A 1 345 ? 22.617 -11.170 3.514 1.00 24.31 ? 361 GLN A CG 1 ATOM 2842 C CD . GLN A 1 345 ? 22.610 -9.666 3.709 1.00 24.40 ? 361 GLN A CD 1 ATOM 2843 O OE1 . GLN A 1 345 ? 21.622 -9.000 3.403 1.00 24.32 ? 361 GLN A OE1 1 ATOM 2844 N NE2 . GLN A 1 345 ? 23.712 -9.122 4.223 1.00 23.72 ? 361 GLN A NE2 1 ATOM 2845 N N . LEU A 1 346 ? 20.907 -13.413 7.341 1.00 25.13 ? 362 LEU A N 1 ATOM 2846 C CA . LEU A 1 346 ? 20.002 -13.630 8.471 1.00 25.40 ? 362 LEU A CA 1 ATOM 2847 C C . LEU A 1 346 ? 20.654 -13.128 9.760 1.00 25.34 ? 362 LEU A C 1 ATOM 2848 O O . LEU A 1 346 ? 19.986 -12.485 10.598 1.00 24.90 ? 362 LEU A O 1 ATOM 2849 C CB . LEU A 1 346 ? 19.607 -15.103 8.601 1.00 26.15 ? 362 LEU A CB 1 ATOM 2850 C CG . LEU A 1 346 ? 18.591 -15.493 9.688 1.00 27.06 ? 362 LEU A CG 1 ATOM 2851 C CD1 . LEU A 1 346 ? 17.249 -14.794 9.503 1.00 27.67 ? 362 LEU A CD1 1 ATOM 2852 C CD2 . LEU A 1 346 ? 18.397 -17.002 9.725 1.00 27.33 ? 362 LEU A CD2 1 ATOM 2853 N N . PHE A 1 347 ? 21.953 -13.414 9.909 1.00 24.70 ? 363 PHE A N 1 ATOM 2854 C CA . PHE A 1 347 ? 22.732 -12.917 11.049 1.00 25.00 ? 363 PHE A CA 1 ATOM 2855 C C . PHE A 1 347 ? 22.871 -11.398 10.986 1.00 24.15 ? 363 PHE A C 1 ATOM 2856 O O . PHE A 1 347 ? 22.752 -10.724 12.006 1.00 24.59 ? 363 PHE A O 1 ATOM 2857 C CB . PHE A 1 347 ? 24.133 -13.558 11.123 1.00 25.14 ? 363 PHE A CB 1 ATOM 2858 C CG . PHE A 1 347 ? 24.136 -15.063 11.151 1.00 25.71 ? 363 PHE A CG 1 ATOM 2859 C CD1 . PHE A 1 347 ? 23.044 -15.785 11.632 1.00 26.57 ? 363 PHE A CD1 1 ATOM 2860 C CD2 . PHE A 1 347 ? 25.268 -15.763 10.733 1.00 25.67 ? 363 PHE A CD2 1 ATOM 2861 C CE1 . PHE A 1 347 ? 23.066 -17.173 11.651 1.00 27.19 ? 363 PHE A CE1 1 ATOM 2862 C CE2 . PHE A 1 347 ? 25.303 -17.146 10.773 1.00 26.19 ? 363 PHE A CE2 1 ATOM 2863 C CZ . PHE A 1 347 ? 24.200 -17.853 11.220 1.00 26.77 ? 363 PHE A CZ 1 ATOM 2864 N N . THR A 1 348 ? 23.127 -10.868 9.789 1.00 23.38 ? 364 THR A N 1 ATOM 2865 C CA . THR A 1 348 ? 23.251 -9.422 9.570 1.00 23.28 ? 364 THR A CA 1 ATOM 2866 C C . THR A 1 348 ? 21.961 -8.682 9.993 1.00 23.73 ? 364 THR A C 1 ATOM 2867 O O . THR A 1 348 ? 22.027 -7.652 10.684 1.00 24.01 ? 364 THR A O 1 ATOM 2868 C CB . THR A 1 348 ? 23.650 -9.095 8.105 1.00 23.76 ? 364 THR A CB 1 ATOM 2869 O OG1 . THR A 1 348 ? 24.913 -9.713 7.796 1.00 24.05 ? 364 THR A OG1 1 ATOM 2870 C CG2 . THR A 1 348 ? 23.781 -7.570 7.869 1.00 23.89 ? 364 THR A CG2 1 ATOM 2871 N N . VAL A 1 349 ? 20.800 -9.225 9.615 1.00 23.10 ? 365 VAL A N 1 ATOM 2872 C CA . VAL A 1 349 ? 19.502 -8.639 9.987 1.00 23.04 ? 365 VAL A CA 1 ATOM 2873 C C . VAL A 1 349 ? 19.411 -8.469 11.505 1.00 22.95 ? 365 VAL A C 1 ATOM 2874 O O . VAL A 1 349 ? 19.003 -7.410 11.974 1.00 22.78 ? 365 VAL A O 1 ATOM 2875 C CB . VAL A 1 349 ? 18.299 -9.451 9.434 1.00 23.09 ? 365 VAL A CB 1 ATOM 2876 C CG1 . VAL A 1 349 ? 16.988 -9.024 10.095 1.00 23.31 ? 365 VAL A CG1 1 ATOM 2877 C CG2 . VAL A 1 349 ? 18.199 -9.267 7.922 1.00 22.77 ? 365 VAL A CG2 1 ATOM 2878 N N . HIS A 1 350 ? 19.819 -9.496 12.254 1.00 22.84 ? 366 HIS A N 1 ATOM 2879 C CA . HIS A 1 350 ? 19.797 -9.436 13.726 1.00 23.40 ? 366 HIS A CA 1 ATOM 2880 C C . HIS A 1 350 ? 20.804 -8.423 14.301 1.00 23.35 ? 366 HIS A C 1 ATOM 2881 O O . HIS A 1 350 ? 20.508 -7.743 15.297 1.00 23.02 ? 366 HIS A O 1 ATOM 2882 C CB . HIS A 1 350 ? 20.040 -10.815 14.328 1.00 23.66 ? 366 HIS A CB 1 ATOM 2883 C CG . HIS A 1 350 ? 18.890 -11.761 14.166 1.00 24.22 ? 366 HIS A CG 1 ATOM 2884 N ND1 . HIS A 1 350 ? 18.610 -12.397 12.974 1.00 24.44 ? 366 HIS A ND1 1 ATOM 2885 C CD2 . HIS A 1 350 ? 17.958 -12.191 15.049 1.00 23.97 ? 366 HIS A CD2 1 ATOM 2886 C CE1 . HIS A 1 350 ? 17.548 -13.171 13.129 1.00 24.73 ? 366 HIS A CE1 1 ATOM 2887 N NE2 . HIS A 1 350 ? 17.131 -13.060 14.380 1.00 24.61 ? 366 HIS A NE2 1 ATOM 2888 N N . HIS A 1 351 ? 21.980 -8.321 13.675 1.00 23.00 ? 367 HIS A N 1 ATOM 2889 C CA . HIS A 1 351 ? 22.951 -7.280 14.039 1.00 23.40 ? 367 HIS A CA 1 ATOM 2890 C C . HIS A 1 351 ? 22.324 -5.883 13.927 1.00 23.03 ? 367 HIS A C 1 ATOM 2891 O O . HIS A 1 351 ? 22.383 -5.098 14.864 1.00 23.22 ? 367 HIS A O 1 ATOM 2892 C CB . HIS A 1 351 ? 24.233 -7.357 13.189 1.00 22.92 ? 367 HIS A CB 1 ATOM 2893 C CG . HIS A 1 351 ? 25.194 -6.243 13.470 1.00 22.68 ? 367 HIS A CG 1 ATOM 2894 N ND1 . HIS A 1 351 ? 26.205 -6.357 14.398 1.00 22.87 ? 367 HIS A ND1 1 ATOM 2895 C CD2 . HIS A 1 351 ? 25.258 -4.975 12.998 1.00 22.63 ? 367 HIS A CD2 1 ATOM 2896 C CE1 . HIS A 1 351 ? 26.875 -5.219 14.459 1.00 22.82 ? 367 HIS A CE1 1 ATOM 2897 N NE2 . HIS A 1 351 ? 26.317 -4.362 13.625 1.00 22.69 ? 367 HIS A NE2 1 ATOM 2898 N N . GLU A 1 352 ? 21.717 -5.585 12.783 1.00 23.18 ? 368 GLU A N 1 ATOM 2899 C CA . GLU A 1 352 ? 21.106 -4.274 12.559 1.00 23.57 ? 368 GLU A CA 1 ATOM 2900 C C . GLU A 1 352 ? 19.947 -3.996 13.501 1.00 23.16 ? 368 GLU A C 1 ATOM 2901 O O . GLU A 1 352 ? 19.785 -2.863 13.958 1.00 23.44 ? 368 GLU A O 1 ATOM 2902 C CB . GLU A 1 352 ? 20.638 -4.124 11.109 1.00 23.91 ? 368 GLU A CB 1 ATOM 2903 C CG . GLU A 1 352 ? 21.717 -4.397 10.069 1.00 24.49 ? 368 GLU A CG 1 ATOM 2904 C CD . GLU A 1 352 ? 22.999 -3.611 10.294 1.00 24.46 ? 368 GLU A CD 1 ATOM 2905 O OE1 . GLU A 1 352 ? 22.935 -2.443 10.750 1.00 24.64 ? 368 GLU A OE1 1 ATOM 2906 O OE2 . GLU A 1 352 ? 24.079 -4.164 9.990 1.00 25.28 ? 368 GLU A OE2 1 ATOM 2907 N N . LEU A 1 353 ? 19.145 -5.026 13.785 1.00 22.98 ? 369 LEU A N 1 ATOM 2908 C CA . LEU A 1 353 ? 18.006 -4.875 14.696 1.00 23.21 ? 369 LEU A CA 1 ATOM 2909 C C . LEU A 1 353 ? 18.463 -4.673 16.144 1.00 22.89 ? 369 LEU A C 1 ATOM 2910 O O . LEU A 1 353 ? 17.709 -4.139 16.961 1.00 22.94 ? 369 LEU A O 1 ATOM 2911 C CB . LEU A 1 353 ? 17.038 -6.063 14.588 1.00 23.52 ? 369 LEU A CB 1 ATOM 2912 C CG . LEU A 1 353 ? 16.182 -6.156 13.315 1.00 23.89 ? 369 LEU A CG 1 ATOM 2913 C CD1 . LEU A 1 353 ? 15.459 -7.499 13.252 1.00 24.22 ? 369 LEU A CD1 1 ATOM 2914 C CD2 . LEU A 1 353 ? 15.193 -5.002 13.204 1.00 23.83 ? 369 LEU A CD2 1 ATOM 2915 N N . GLY A 1 354 ? 19.689 -5.104 16.451 1.00 22.24 ? 370 GLY A N 1 ATOM 2916 C CA . GLY A 1 354 ? 20.327 -4.819 17.748 1.00 21.48 ? 370 GLY A CA 1 ATOM 2917 C C . GLY A 1 354 ? 20.537 -3.325 17.994 1.00 21.55 ? 370 GLY A C 1 ATOM 2918 O O . GLY A 1 354 ? 20.312 -2.830 19.106 1.00 21.35 ? 370 GLY A O 1 ATOM 2919 N N . HIS A 1 355 ? 20.964 -2.608 16.953 1.00 21.66 ? 371 HIS A N 1 ATOM 2920 C CA . HIS A 1 355 ? 21.061 -1.150 16.993 1.00 21.70 ? 371 HIS A CA 1 ATOM 2921 C C . HIS A 1 355 ? 19.679 -0.533 17.249 1.00 22.20 ? 371 HIS A C 1 ATOM 2922 O O . HIS A 1 355 ? 19.526 0.314 18.137 1.00 22.00 ? 371 HIS A O 1 ATOM 2923 C CB . HIS A 1 355 ? 21.617 -0.605 15.678 1.00 21.83 ? 371 HIS A CB 1 ATOM 2924 C CG . HIS A 1 355 ? 23.065 -0.912 15.445 1.00 22.51 ? 371 HIS A CG 1 ATOM 2925 N ND1 . HIS A 1 355 ? 24.049 -0.632 16.371 1.00 22.12 ? 371 HIS A ND1 1 ATOM 2926 C CD2 . HIS A 1 355 ? 23.698 -1.436 14.371 1.00 22.16 ? 371 HIS A CD2 1 ATOM 2927 C CE1 . HIS A 1 355 ? 25.224 -0.984 15.880 1.00 22.23 ? 371 HIS A CE1 1 ATOM 2928 N NE2 . HIS A 1 355 ? 25.038 -1.470 14.667 1.00 23.02 ? 371 HIS A NE2 1 ATOM 2929 N N . ILE A 1 356 ? 18.682 -0.973 16.476 1.00 22.28 ? 372 ILE A N 1 ATOM 2930 C CA . ILE A 1 356 ? 17.306 -0.469 16.594 1.00 22.62 ? 372 ILE A CA 1 ATOM 2931 C C . ILE A 1 356 ? 16.769 -0.670 18.017 1.00 22.56 ? 372 ILE A C 1 ATOM 2932 O O . ILE A 1 356 ? 16.185 0.250 18.601 1.00 22.75 ? 372 ILE A O 1 ATOM 2933 C CB . ILE A 1 356 ? 16.346 -1.113 15.558 1.00 22.98 ? 372 ILE A CB 1 ATOM 2934 C CG1 . ILE A 1 356 ? 16.804 -0.821 14.120 1.00 22.85 ? 372 ILE A CG1 1 ATOM 2935 C CG2 . ILE A 1 356 ? 14.892 -0.672 15.787 1.00 23.23 ? 372 ILE A CG2 1 ATOM 2936 C CD1 . ILE A 1 356 ? 16.679 0.623 13.666 1.00 23.31 ? 372 ILE A CD1 1 ATOM 2937 N N . GLN A 1 357 ? 16.972 -1.860 18.571 1.00 22.48 ? 373 GLN A N 1 ATOM 2938 C CA . GLN A 1 357 ? 16.521 -2.130 19.936 1.00 23.15 ? 373 GLN A CA 1 ATOM 2939 C C . GLN A 1 357 ? 17.142 -1.167 20.954 1.00 23.10 ? 373 GLN A C 1 ATOM 2940 O O . GLN A 1 357 ? 16.450 -0.672 21.862 1.00 23.83 ? 373 GLN A O 1 ATOM 2941 C CB . GLN A 1 357 ? 16.777 -3.592 20.325 1.00 23.21 ? 373 GLN A CB 1 ATOM 2942 C CG . GLN A 1 357 ? 16.225 -4.000 21.697 1.00 23.74 ? 373 GLN A CG 1 ATOM 2943 C CD . GLN A 1 357 ? 14.697 -4.043 21.781 1.00 24.44 ? 373 GLN A CD 1 ATOM 2944 O OE1 . GLN A 1 357 ? 14.121 -3.822 22.854 1.00 24.33 ? 373 GLN A OE1 1 ATOM 2945 N NE2 . GLN A 1 357 ? 14.035 -4.330 20.659 1.00 24.02 ? 373 GLN A NE2 1 ATOM 2946 N N . TYR A 1 358 ? 18.443 -0.910 20.813 1.00 22.45 ? 374 TYR A N 1 ATOM 2947 C CA . TYR A 1 358 ? 19.144 0.024 21.692 1.00 21.96 ? 374 TYR A CA 1 ATOM 2948 C C . TYR A 1 358 ? 18.502 1.422 21.572 1.00 21.93 ? 374 TYR A C 1 ATOM 2949 O O . TYR A 1 358 ? 18.251 2.065 22.589 1.00 21.20 ? 374 TYR A O 1 ATOM 2950 C CB . TYR A 1 358 ? 20.636 0.065 21.332 1.00 21.80 ? 374 TYR A CB 1 ATOM 2951 C CG . TYR A 1 358 ? 21.633 0.210 22.481 1.00 21.40 ? 374 TYR A CG 1 ATOM 2952 C CD1 . TYR A 1 358 ? 21.285 0.816 23.702 1.00 21.72 ? 374 TYR A CD1 1 ATOM 2953 C CD2 . TYR A 1 358 ? 22.942 -0.229 22.321 1.00 21.08 ? 374 TYR A CD2 1 ATOM 2954 C CE1 . TYR A 1 358 ? 22.220 0.951 24.728 1.00 21.51 ? 374 TYR A CE1 1 ATOM 2955 C CE2 . TYR A 1 358 ? 23.884 -0.093 23.329 1.00 20.86 ? 374 TYR A CE2 1 ATOM 2956 C CZ . TYR A 1 358 ? 23.525 0.496 24.528 1.00 21.46 ? 374 TYR A CZ 1 ATOM 2957 O OH . TYR A 1 358 ? 24.484 0.607 25.516 1.00 20.58 ? 374 TYR A OH 1 ATOM 2958 N N . PHE A 1 359 ? 18.199 1.861 20.342 1.00 21.69 ? 375 PHE A N 1 ATOM 2959 C CA . PHE A 1 359 ? 17.516 3.155 20.122 1.00 22.31 ? 375 PHE A CA 1 ATOM 2960 C C . PHE A 1 359 ? 16.214 3.257 20.914 1.00 22.99 ? 375 PHE A C 1 ATOM 2961 O O . PHE A 1 359 ? 15.955 4.272 21.576 1.00 22.93 ? 375 PHE A O 1 ATOM 2962 C CB . PHE A 1 359 ? 17.179 3.401 18.650 1.00 22.31 ? 375 PHE A CB 1 ATOM 2963 C CG . PHE A 1 359 ? 18.363 3.420 17.726 1.00 22.31 ? 375 PHE A CG 1 ATOM 2964 C CD1 . PHE A 1 359 ? 19.642 3.777 18.178 1.00 21.88 ? 375 PHE A CD1 1 ATOM 2965 C CD2 . PHE A 1 359 ? 18.191 3.129 16.376 1.00 22.37 ? 375 PHE A CD2 1 ATOM 2966 C CE1 . PHE A 1 359 ? 20.722 3.804 17.313 1.00 22.23 ? 375 PHE A CE1 1 ATOM 2967 C CE2 . PHE A 1 359 ? 19.271 3.148 15.508 1.00 22.37 ? 375 PHE A CE2 1 ATOM 2968 C CZ . PHE A 1 359 ? 20.534 3.496 15.970 1.00 21.98 ? 375 PHE A CZ 1 ATOM 2969 N N . LEU A 1 360 ? 15.401 2.200 20.826 1.00 23.09 ? 376 LEU A N 1 ATOM 2970 C CA . LEU A 1 360 ? 14.096 2.147 21.475 1.00 23.71 ? 376 LEU A CA 1 ATOM 2971 C C . LEU A 1 360 ? 14.241 2.108 22.992 1.00 24.05 ? 376 LEU A C 1 ATOM 2972 O O . LEU A 1 360 ? 13.473 2.771 23.696 1.00 24.83 ? 376 LEU A O 1 ATOM 2973 C CB . LEU A 1 360 ? 13.286 0.938 20.977 1.00 23.96 ? 376 LEU A CB 1 ATOM 2974 C CG . LEU A 1 360 ? 12.914 0.952 19.488 1.00 23.94 ? 376 LEU A CG 1 ATOM 2975 C CD1 . LEU A 1 360 ? 12.329 -0.387 19.074 1.00 24.46 ? 376 LEU A CD1 1 ATOM 2976 C CD2 . LEU A 1 360 ? 11.939 2.086 19.161 1.00 24.25 ? 376 LEU A CD2 1 ATOM 2977 N N . GLN A 1 361 ? 15.239 1.366 23.482 1.00 23.67 ? 377 GLN A N 1 ATOM 2978 C CA . GLN A 1 361 ? 15.495 1.225 24.926 1.00 23.90 ? 377 GLN A CA 1 ATOM 2979 C C . GLN A 1 361 ? 15.917 2.529 25.638 1.00 23.71 ? 377 GLN A C 1 ATOM 2980 O O . GLN A 1 361 ? 15.572 2.748 26.815 1.00 23.93 ? 377 GLN A O 1 ATOM 2981 C CB . GLN A 1 361 ? 16.548 0.139 25.188 1.00 24.15 ? 377 GLN A CB 1 ATOM 2982 C CG . GLN A 1 361 ? 16.063 -1.302 25.001 1.00 25.41 ? 377 GLN A CG 1 ATOM 2983 C CD . GLN A 1 361 ? 15.057 -1.757 26.057 1.00 26.29 ? 377 GLN A CD 1 ATOM 2984 O OE1 . GLN A 1 361 ? 15.163 -1.408 27.239 1.00 27.09 ? 377 GLN A OE1 1 ATOM 2985 N NE2 . GLN A 1 361 ? 14.080 -2.556 25.633 1.00 26.48 ? 377 GLN A NE2 1 ATOM 2986 N N . TYR A 1 362 ? 16.677 3.378 24.952 1.00 23.11 ? 378 TYR A N 1 ATOM 2987 C CA . TYR A 1 362 ? 17.148 4.631 25.568 1.00 23.18 ? 378 TYR A CA 1 ATOM 2988 C C . TYR A 1 362 ? 16.479 5.932 25.083 1.00 23.81 ? 378 TYR A C 1 ATOM 2989 O O . TYR A 1 362 ? 16.943 7.033 25.409 1.00 23.92 ? 378 TYR A O 1 ATOM 2990 C CB . TYR A 1 362 ? 18.693 4.728 25.548 1.00 21.99 ? 378 TYR A CB 1 ATOM 2991 C CG . TYR A 1 362 ? 19.409 4.786 24.191 1.00 21.37 ? 378 TYR A CG 1 ATOM 2992 C CD1 . TYR A 1 362 ? 18.987 5.634 23.166 1.00 21.26 ? 378 TYR A CD1 1 ATOM 2993 C CD2 . TYR A 1 362 ? 20.577 4.048 23.984 1.00 20.91 ? 378 TYR A CD2 1 ATOM 2994 C CE1 . TYR A 1 362 ? 19.678 5.695 21.953 1.00 21.00 ? 378 TYR A CE1 1 ATOM 2995 C CE2 . TYR A 1 362 ? 21.277 4.105 22.778 1.00 20.74 ? 378 TYR A CE2 1 ATOM 2996 C CZ . TYR A 1 362 ? 20.833 4.924 21.771 1.00 20.91 ? 378 TYR A CZ 1 ATOM 2997 O OH . TYR A 1 362 ? 21.550 4.970 20.583 1.00 20.71 ? 378 TYR A OH 1 ATOM 2998 N N . GLN A 1 363 ? 15.389 5.818 24.324 1.00 24.68 ? 379 GLN A N 1 ATOM 2999 C CA . GLN A 1 363 ? 14.783 7.007 23.717 1.00 25.77 ? 379 GLN A CA 1 ATOM 3000 C C . GLN A 1 363 ? 14.135 7.968 24.730 1.00 25.82 ? 379 GLN A C 1 ATOM 3001 O O . GLN A 1 363 ? 13.879 9.115 24.399 1.00 25.92 ? 379 GLN A O 1 ATOM 3002 C CB . GLN A 1 363 ? 13.827 6.647 22.559 1.00 26.71 ? 379 GLN A CB 1 ATOM 3003 C CG . GLN A 1 363 ? 12.523 5.976 22.958 1.00 28.43 ? 379 GLN A CG 1 ATOM 3004 C CD . GLN A 1 363 ? 11.640 5.625 21.762 1.00 29.92 ? 379 GLN A CD 1 ATOM 3005 O OE1 . GLN A 1 363 ? 11.934 5.976 20.612 1.00 30.84 ? 379 GLN A OE1 1 ATOM 3006 N NE2 . GLN A 1 363 ? 10.546 4.933 22.032 1.00 30.74 ? 379 GLN A NE2 1 ATOM 3007 N N . HIS A 1 364 ? 13.908 7.504 25.958 1.00 26.27 ? 380 HIS A N 1 ATOM 3008 C CA . HIS A 1 364 ? 13.400 8.354 27.045 1.00 27.40 ? 380 HIS A CA 1 ATOM 3009 C C . HIS A 1 364 ? 14.513 9.157 27.738 1.00 27.53 ? 380 HIS A C 1 ATOM 3010 O O . HIS A 1 364 ? 14.215 10.026 28.558 1.00 27.10 ? 380 HIS A O 1 ATOM 3011 C CB . HIS A 1 364 ? 12.710 7.498 28.107 1.00 27.90 ? 380 HIS A CB 1 ATOM 3012 C CG . HIS A 1 364 ? 13.647 6.574 28.818 1.00 28.34 ? 380 HIS A CG 1 ATOM 3013 N ND1 . HIS A 1 364 ? 14.216 5.478 28.204 1.00 27.97 ? 380 HIS A ND1 1 ATOM 3014 C CD2 . HIS A 1 364 ? 14.143 6.602 30.078 1.00 28.74 ? 380 HIS A CD2 1 ATOM 3015 C CE1 . HIS A 1 364 ? 15.008 4.859 29.061 1.00 28.02 ? 380 HIS A CE1 1 ATOM 3016 N NE2 . HIS A 1 364 ? 14.987 5.523 30.203 1.00 29.12 ? 380 HIS A NE2 1 ATOM 3017 N N . GLN A 1 365 ? 15.780 8.840 27.438 1.00 26.34 ? 381 GLN A N 1 ATOM 3018 C CA . GLN A 1 365 ? 16.934 9.557 28.017 1.00 26.30 ? 381 GLN A CA 1 ATOM 3019 C C . GLN A 1 365 ? 17.085 10.976 27.451 1.00 26.31 ? 381 GLN A C 1 ATOM 3020 O O . GLN A 1 365 ? 16.628 11.238 26.344 1.00 26.88 ? 381 GLN A O 1 ATOM 3021 C CB . GLN A 1 365 ? 18.233 8.763 27.787 1.00 25.61 ? 381 GLN A CB 1 ATOM 3022 C CG . GLN A 1 365 ? 18.292 7.421 28.516 1.00 26.04 ? 381 GLN A CG 1 ATOM 3023 C CD . GLN A 1 365 ? 18.620 7.572 29.996 1.00 27.02 ? 381 GLN A CD 1 ATOM 3024 O OE1 . GLN A 1 365 ? 19.025 8.647 30.448 1.00 27.85 ? 381 GLN A OE1 1 ATOM 3025 N NE2 . GLN A 1 365 ? 18.459 6.496 30.755 1.00 26.91 ? 381 GLN A NE2 1 ATOM 3026 N N . PRO A 1 366 ? 17.721 11.902 28.208 1.00 26.66 ? 382 PRO A N 1 ATOM 3027 C CA . PRO A 1 366 ? 18.106 13.180 27.590 1.00 26.57 ? 382 PRO A CA 1 ATOM 3028 C C . PRO A 1 366 ? 18.955 12.936 26.342 1.00 26.25 ? 382 PRO A C 1 ATOM 3029 O O . PRO A 1 366 ? 19.711 11.952 26.285 1.00 25.49 ? 382 PRO A O 1 ATOM 3030 C CB . PRO A 1 366 ? 18.963 13.876 28.659 1.00 27.06 ? 382 PRO A CB 1 ATOM 3031 C CG . PRO A 1 366 ? 18.881 13.049 29.893 1.00 26.91 ? 382 PRO A CG 1 ATOM 3032 C CD . PRO A 1 366 ? 17.999 11.863 29.655 1.00 26.58 ? 382 PRO A CD 1 ATOM 3033 N N . PHE A 1 367 ? 18.832 13.827 25.362 1.00 26.01 ? 383 PHE A N 1 ATOM 3034 C CA . PHE A 1 367 ? 19.517 13.675 24.076 1.00 26.28 ? 383 PHE A CA 1 ATOM 3035 C C . PHE A 1 367 ? 20.973 13.199 24.183 1.00 25.65 ? 383 PHE A C 1 ATOM 3036 O O . PHE A 1 367 ? 21.361 12.238 23.511 1.00 24.93 ? 383 PHE A O 1 ATOM 3037 C CB . PHE A 1 367 ? 19.468 14.975 23.270 1.00 27.18 ? 383 PHE A CB 1 ATOM 3038 C CG . PHE A 1 367 ? 20.282 14.923 22.012 1.00 27.90 ? 383 PHE A CG 1 ATOM 3039 C CD1 . PHE A 1 367 ? 19.757 14.339 20.860 1.00 28.65 ? 383 PHE A CD1 1 ATOM 3040 C CD2 . PHE A 1 367 ? 21.580 15.427 21.982 1.00 27.95 ? 383 PHE A CD2 1 ATOM 3041 C CE1 . PHE A 1 367 ? 20.503 14.274 19.695 1.00 29.16 ? 383 PHE A CE1 1 ATOM 3042 C CE2 . PHE A 1 367 ? 22.335 15.359 20.821 1.00 28.33 ? 383 PHE A CE2 1 ATOM 3043 C CZ . PHE A 1 367 ? 21.794 14.787 19.674 1.00 28.78 ? 383 PHE A CZ 1 ATOM 3044 N N . VAL A 1 368 ? 21.780 13.865 25.011 1.00 24.98 ? 384 VAL A N 1 ATOM 3045 C CA . VAL A 1 368 ? 23.216 13.513 25.092 1.00 24.99 ? 384 VAL A CA 1 ATOM 3046 C C . VAL A 1 368 ? 23.468 12.077 25.561 1.00 24.13 ? 384 VAL A C 1 ATOM 3047 O O . VAL A 1 368 ? 24.529 11.533 25.312 1.00 23.93 ? 384 VAL A O 1 ATOM 3048 C CB . VAL A 1 368 ? 24.067 14.499 25.933 1.00 25.53 ? 384 VAL A CB 1 ATOM 3049 C CG1 . VAL A 1 368 ? 24.154 15.861 25.251 1.00 26.41 ? 384 VAL A CG1 1 ATOM 3050 C CG2 . VAL A 1 368 ? 23.533 14.618 27.354 1.00 26.14 ? 384 VAL A CG2 1 ATOM 3051 N N . TYR A 1 369 ? 22.494 11.480 26.245 1.00 24.34 ? 385 TYR A N 1 ATOM 3052 C CA . TYR A 1 369 ? 22.611 10.103 26.727 1.00 24.23 ? 385 TYR A CA 1 ATOM 3053 C C . TYR A 1 369 ? 22.014 9.078 25.743 1.00 24.09 ? 385 TYR A C 1 ATOM 3054 O O . TYR A 1 369 ? 22.104 7.871 25.977 1.00 24.48 ? 385 TYR A O 1 ATOM 3055 C CB . TYR A 1 369 ? 21.951 9.943 28.098 1.00 24.48 ? 385 TYR A CB 1 ATOM 3056 C CG . TYR A 1 369 ? 22.650 10.646 29.250 1.00 24.53 ? 385 TYR A CG 1 ATOM 3057 C CD1 . TYR A 1 369 ? 24.000 11.008 29.173 1.00 24.38 ? 385 TYR A CD1 1 ATOM 3058 C CD2 . TYR A 1 369 ? 21.958 10.924 30.430 1.00 24.89 ? 385 TYR A CD2 1 ATOM 3059 C CE1 . TYR A 1 369 ? 24.634 11.644 30.233 1.00 24.64 ? 385 TYR A CE1 1 ATOM 3060 C CE2 . TYR A 1 369 ? 22.583 11.553 31.498 1.00 25.22 ? 385 TYR A CE2 1 ATOM 3061 C CZ . TYR A 1 369 ? 23.915 11.910 31.395 1.00 24.95 ? 385 TYR A CZ 1 ATOM 3062 O OH . TYR A 1 369 ? 24.526 12.534 32.453 1.00 25.32 ? 385 TYR A OH 1 ATOM 3063 N N . ARG A 1 370 ? 21.425 9.556 24.649 1.00 23.75 ? 386 ARG A N 1 ATOM 3064 C CA . ARG A 1 370 ? 20.834 8.658 23.651 1.00 23.85 ? 386 ARG A CA 1 ATOM 3065 C C . ARG A 1 370 ? 21.895 8.127 22.676 1.00 23.30 ? 386 ARG A C 1 ATOM 3066 O O . ARG A 1 370 ? 21.906 8.461 21.483 1.00 23.29 ? 386 ARG A O 1 ATOM 3067 C CB . ARG A 1 370 ? 19.656 9.328 22.924 1.00 24.02 ? 386 ARG A CB 1 ATOM 3068 C CG . ARG A 1 370 ? 18.453 9.591 23.819 1.00 25.06 ? 386 ARG A CG 1 ATOM 3069 C CD . ARG A 1 370 ? 17.375 10.426 23.132 1.00 25.25 ? 386 ARG A CD 1 ATOM 3070 N NE . ARG A 1 370 ? 16.655 9.666 22.108 1.00 25.12 ? 386 ARG A NE 1 ATOM 3071 C CZ . ARG A 1 370 ? 15.570 10.098 21.465 1.00 25.87 ? 386 ARG A CZ 1 ATOM 3072 N NH1 . ARG A 1 370 ? 15.060 11.300 21.743 1.00 25.47 ? 386 ARG A NH1 1 ATOM 3073 N NH2 . ARG A 1 370 ? 14.991 9.328 20.540 1.00 24.95 ? 386 ARG A NH2 1 ATOM 3074 N N . THR A 1 371 ? 22.791 7.300 23.211 1.00 22.86 ? 387 THR A N 1 ATOM 3075 C CA . THR A 1 371 ? 23.852 6.643 22.439 1.00 22.57 ? 387 THR A CA 1 ATOM 3076 C C . THR A 1 371 ? 24.349 5.457 23.270 1.00 22.20 ? 387 THR A C 1 ATOM 3077 O O . THR A 1 371 ? 23.912 5.291 24.398 1.00 21.86 ? 387 THR A O 1 ATOM 3078 C CB . THR A 1 371 ? 25.000 7.615 22.064 1.00 22.51 ? 387 THR A CB 1 ATOM 3079 O OG1 . THR A 1 371 ? 25.834 7.000 21.083 1.00 22.48 ? 387 THR A OG1 1 ATOM 3080 C CG2 . THR A 1 371 ? 25.847 7.983 23.277 1.00 22.57 ? 387 THR A CG2 1 ATOM 3081 N N . GLY A 1 372 ? 25.243 4.630 22.726 1.00 21.75 ? 388 GLY A N 1 ATOM 3082 C CA . GLY A 1 372 ? 25.736 3.453 23.464 1.00 21.41 ? 388 GLY A CA 1 ATOM 3083 C C . GLY A 1 372 ? 26.574 3.794 24.688 1.00 21.58 ? 388 GLY A C 1 ATOM 3084 O O . GLY A 1 372 ? 27.189 4.871 24.756 1.00 21.36 ? 388 GLY A O 1 ATOM 3085 N N . ALA A 1 373 ? 26.605 2.884 25.660 1.00 21.47 ? 389 ALA A N 1 ATOM 3086 C CA . ALA A 1 373 ? 27.462 3.061 26.844 1.00 21.49 ? 389 ALA A CA 1 ATOM 3087 C C . ALA A 1 373 ? 28.928 3.276 26.425 1.00 20.91 ? 389 ALA A C 1 ATOM 3088 O O . ALA A 1 373 ? 29.625 4.120 26.979 1.00 21.00 ? 389 ALA A O 1 ATOM 3089 C CB . ALA A 1 373 ? 27.325 1.872 27.784 1.00 21.63 ? 389 ALA A CB 1 ATOM 3090 N N . ASN A 1 374 ? 29.383 2.505 25.441 1.00 20.70 ? 390 ASN A N 1 ATOM 3091 C CA . ASN A 1 374 ? 30.548 2.868 24.617 1.00 20.50 ? 390 ASN A CA 1 ATOM 3092 C C . ASN A 1 374 ? 30.265 2.316 23.215 1.00 20.44 ? 390 ASN A C 1 ATOM 3093 O O . ASN A 1 374 ? 29.298 1.555 23.054 1.00 21.12 ? 390 ASN A O 1 ATOM 3094 C CB . ASN A 1 374 ? 31.913 2.441 25.227 1.00 20.20 ? 390 ASN A CB 1 ATOM 3095 C CG . ASN A 1 374 ? 32.226 0.957 25.077 1.00 20.40 ? 390 ASN A CG 1 ATOM 3096 O OD1 . ASN A 1 374 ? 31.983 0.347 24.033 1.00 21.24 ? 390 ASN A OD1 1 ATOM 3097 N ND2 . ASN A 1 374 ? 32.842 0.385 26.104 1.00 20.17 ? 390 ASN A ND2 1 ATOM 3098 N N . PRO A 1 375 ? 31.042 2.724 22.192 1.00 20.61 ? 391 PRO A N 1 ATOM 3099 C CA . PRO A 1 375 ? 30.642 2.259 20.858 1.00 20.00 ? 391 PRO A CA 1 ATOM 3100 C C . PRO A 1 375 ? 30.606 0.732 20.681 1.00 20.27 ? 391 PRO A C 1 ATOM 3101 O O . PRO A 1 375 ? 29.831 0.238 19.860 1.00 20.89 ? 391 PRO A O 1 ATOM 3102 C CB . PRO A 1 375 ? 31.700 2.889 19.947 1.00 19.69 ? 391 PRO A CB 1 ATOM 3103 C CG . PRO A 1 375 ? 32.066 4.154 20.656 1.00 20.16 ? 391 PRO A CG 1 ATOM 3104 C CD . PRO A 1 375 ? 32.111 3.745 22.107 1.00 19.89 ? 391 PRO A CD 1 ATOM 3105 N N . GLY A 1 376 ? 31.437 -0.001 21.418 1.00 19.55 ? 392 GLY A N 1 ATOM 3106 C CA . GLY A 1 376 ? 31.422 -1.464 21.367 1.00 19.51 ? 392 GLY A CA 1 ATOM 3107 C C . GLY A 1 376 ? 30.110 -2.085 21.845 1.00 20.08 ? 392 GLY A C 1 ATOM 3108 O O . GLY A 1 376 ? 29.681 -3.112 21.318 1.00 19.46 ? 392 GLY A O 1 ATOM 3109 N N . PHE A 1 377 ? 29.486 -1.489 22.870 1.00 20.53 ? 393 PHE A N 1 ATOM 3110 C CA . PHE A 1 377 ? 28.171 -1.942 23.339 1.00 21.18 ? 393 PHE A CA 1 ATOM 3111 C C . PHE A 1 377 ? 27.118 -1.950 22.229 1.00 21.73 ? 393 PHE A C 1 ATOM 3112 O O . PHE A 1 377 ? 26.367 -2.916 22.093 1.00 22.25 ? 393 PHE A O 1 ATOM 3113 C CB . PHE A 1 377 ? 27.680 -1.087 24.507 1.00 21.44 ? 393 PHE A CB 1 ATOM 3114 C CG . PHE A 1 377 ? 28.296 -1.450 25.833 1.00 21.36 ? 393 PHE A CG 1 ATOM 3115 C CD1 . PHE A 1 377 ? 29.678 -1.438 26.009 1.00 21.39 ? 393 PHE A CD1 1 ATOM 3116 C CD2 . PHE A 1 377 ? 27.486 -1.774 26.919 1.00 21.78 ? 393 PHE A CD2 1 ATOM 3117 C CE1 . PHE A 1 377 ? 30.245 -1.761 27.235 1.00 21.35 ? 393 PHE A CE1 1 ATOM 3118 C CE2 . PHE A 1 377 ? 28.044 -2.104 28.144 1.00 21.16 ? 393 PHE A CE2 1 ATOM 3119 C CZ . PHE A 1 377 ? 29.419 -2.091 28.303 1.00 21.40 ? 393 PHE A CZ 1 ATOM 3120 N N . HIS A 1 378 ? 27.074 -0.887 21.429 1.00 21.63 ? 394 HIS A N 1 ATOM 3121 C CA . HIS A 1 378 ? 26.069 -0.778 20.364 1.00 21.96 ? 394 HIS A CA 1 ATOM 3122 C C . HIS A 1 378 ? 26.226 -1.891 19.330 1.00 22.41 ? 394 HIS A C 1 ATOM 3123 O O . HIS A 1 378 ? 25.231 -2.439 18.847 1.00 22.85 ? 394 HIS A O 1 ATOM 3124 C CB . HIS A 1 378 ? 26.128 0.598 19.680 1.00 20.99 ? 394 HIS A CB 1 ATOM 3125 C CG . HIS A 1 378 ? 24.802 1.290 19.596 1.00 20.96 ? 394 HIS A CG 1 ATOM 3126 N ND1 . HIS A 1 378 ? 23.770 0.827 18.808 1.00 20.97 ? 394 HIS A ND1 1 ATOM 3127 C CD2 . HIS A 1 378 ? 24.340 2.412 20.202 1.00 21.00 ? 394 HIS A CD2 1 ATOM 3128 C CE1 . HIS A 1 378 ? 22.731 1.635 18.931 1.00 21.44 ? 394 HIS A CE1 1 ATOM 3129 N NE2 . HIS A 1 378 ? 23.047 2.601 19.777 1.00 20.93 ? 394 HIS A NE2 1 ATOM 3130 N N . GLU A 1 379 ? 27.475 -2.222 18.995 1.00 22.46 ? 395 GLU A N 1 ATOM 3131 C CA . GLU A 1 379 ? 27.753 -3.262 17.989 1.00 22.07 ? 395 GLU A CA 1 ATOM 3132 C C . GLU A 1 379 ? 27.510 -4.666 18.545 1.00 22.04 ? 395 GLU A C 1 ATOM 3133 O O . GLU A 1 379 ? 27.232 -5.592 17.794 1.00 22.84 ? 395 GLU A O 1 ATOM 3134 C CB . GLU A 1 379 ? 29.195 -3.136 17.463 1.00 21.73 ? 395 GLU A CB 1 ATOM 3135 C CG . GLU A 1 379 ? 29.523 -1.760 16.901 1.00 21.79 ? 395 GLU A CG 1 ATOM 3136 C CD . GLU A 1 379 ? 28.605 -1.384 15.747 1.00 21.66 ? 395 GLU A CD 1 ATOM 3137 O OE1 . GLU A 1 379 ? 28.104 -2.300 15.077 1.00 22.53 ? 395 GLU A OE1 1 ATOM 3138 O OE2 . GLU A 1 379 ? 28.360 -0.187 15.517 1.00 21.72 ? 395 GLU A OE2 1 ATOM 3139 N N . ALA A 1 380 ? 27.593 -4.814 19.868 1.00 21.43 ? 396 ALA A N 1 ATOM 3140 C CA . ALA A 1 380 ? 27.473 -6.132 20.500 1.00 21.52 ? 396 ALA A CA 1 ATOM 3141 C C . ALA A 1 380 ? 26.046 -6.700 20.564 1.00 21.76 ? 396 ALA A C 1 ATOM 3142 O O . ALA A 1 380 ? 25.870 -7.917 20.455 1.00 21.81 ? 396 ALA A O 1 ATOM 3143 C CB . ALA A 1 380 ? 28.100 -6.122 21.891 1.00 21.06 ? 396 ALA A CB 1 ATOM 3144 N N . VAL A 1 381 ? 25.046 -5.825 20.734 1.00 22.11 ? 397 VAL A N 1 ATOM 3145 C CA . VAL A 1 381 ? 23.673 -6.248 21.089 1.00 22.55 ? 397 VAL A CA 1 ATOM 3146 C C . VAL A 1 381 ? 23.147 -7.330 20.146 1.00 22.47 ? 397 VAL A C 1 ATOM 3147 O O . VAL A 1 381 ? 22.816 -8.427 20.589 1.00 22.78 ? 397 VAL A O 1 ATOM 3148 C CB . VAL A 1 381 ? 22.675 -5.062 21.133 1.00 22.72 ? 397 VAL A CB 1 ATOM 3149 C CG1 . VAL A 1 381 ? 21.283 -5.545 21.524 1.00 23.16 ? 397 VAL A CG1 1 ATOM 3150 C CG2 . VAL A 1 381 ? 23.151 -3.991 22.110 1.00 23.27 ? 397 VAL A CG2 1 ATOM 3151 N N . GLY A 1 382 ? 23.075 -7.008 18.856 1.00 22.33 ? 398 GLY A N 1 ATOM 3152 C CA . GLY A 1 382 ? 22.533 -7.915 17.848 1.00 23.33 ? 398 GLY A CA 1 ATOM 3153 C C . GLY A 1 382 ? 23.366 -9.168 17.626 1.00 23.73 ? 398 GLY A C 1 ATOM 3154 O O . GLY A 1 382 ? 22.826 -10.224 17.289 1.00 23.97 ? 398 GLY A O 1 ATOM 3155 N N . ASP A 1 383 ? 24.678 -9.052 17.817 1.00 23.85 ? 399 ASP A N 1 ATOM 3156 C CA . ASP A 1 383 ? 25.596 -10.195 17.695 1.00 24.09 ? 399 ASP A CA 1 ATOM 3157 C C . ASP A 1 383 ? 25.366 -11.252 18.767 1.00 24.52 ? 399 ASP A C 1 ATOM 3158 O O . ASP A 1 383 ? 25.563 -12.445 18.521 1.00 24.03 ? 399 ASP A O 1 ATOM 3159 C CB . ASP A 1 383 ? 27.054 -9.727 17.735 1.00 24.08 ? 399 ASP A CB 1 ATOM 3160 C CG . ASP A 1 383 ? 27.528 -9.177 16.398 1.00 24.55 ? 399 ASP A CG 1 ATOM 3161 O OD1 . ASP A 1 383 ? 26.677 -8.712 15.599 1.00 24.89 ? 399 ASP A OD1 1 ATOM 3162 O OD2 . ASP A 1 383 ? 28.756 -9.202 16.152 1.00 24.57 ? 399 ASP A OD2 1 ATOM 3163 N N . VAL A 1 384 ? 24.946 -10.816 19.956 1.00 25.02 ? 400 VAL A N 1 ATOM 3164 C CA . VAL A 1 384 ? 24.612 -11.758 21.023 1.00 25.74 ? 400 VAL A CA 1 ATOM 3165 C C . VAL A 1 384 ? 23.443 -12.653 20.588 1.00 26.46 ? 400 VAL A C 1 ATOM 3166 O O . VAL A 1 384 ? 23.485 -13.872 20.785 1.00 26.72 ? 400 VAL A O 1 ATOM 3167 C CB . VAL A 1 384 ? 24.302 -11.043 22.351 1.00 25.96 ? 400 VAL A CB 1 ATOM 3168 C CG1 . VAL A 1 384 ? 23.894 -12.051 23.419 1.00 25.94 ? 400 VAL A CG1 1 ATOM 3169 C CG2 . VAL A 1 384 ? 25.514 -10.244 22.816 1.00 25.61 ? 400 VAL A CG2 1 ATOM 3170 N N . LEU A 1 385 ? 22.424 -12.056 19.966 1.00 26.68 ? 401 LEU A N 1 ATOM 3171 C CA . LEU A 1 385 ? 21.292 -12.847 19.463 1.00 27.45 ? 401 LEU A CA 1 ATOM 3172 C C . LEU A 1 385 ? 21.719 -13.713 18.277 1.00 27.40 ? 401 LEU A C 1 ATOM 3173 O O . LEU A 1 385 ? 21.342 -14.876 18.201 1.00 27.81 ? 401 LEU A O 1 ATOM 3174 C CB . LEU A 1 385 ? 20.079 -11.985 19.079 1.00 27.55 ? 401 LEU A CB 1 ATOM 3175 C CG . LEU A 1 385 ? 19.435 -10.886 19.949 1.00 28.94 ? 401 LEU A CG 1 ATOM 3176 C CD1 . LEU A 1 385 ? 17.927 -10.905 19.742 1.00 28.20 ? 401 LEU A CD1 1 ATOM 3177 C CD2 . LEU A 1 385 ? 19.765 -10.919 21.436 1.00 27.93 ? 401 LEU A CD2 1 ATOM 3178 N N . SER A 1 386 ? 22.515 -13.146 17.369 1.00 27.90 ? 402 SER A N 1 ATOM 3179 C CA . SER A 1 386 ? 23.035 -13.885 16.202 1.00 27.85 ? 402 SER A CA 1 ATOM 3180 C C . SER A 1 386 ? 23.836 -15.122 16.593 1.00 27.08 ? 402 SER A C 1 ATOM 3181 O O . SER A 1 386 ? 23.837 -16.113 15.850 1.00 26.19 ? 402 SER A O 1 ATOM 3182 C CB . SER A 1 386 ? 23.905 -12.996 15.304 1.00 29.27 ? 402 SER A CB 1 ATOM 3183 O OG . SER A 1 386 ? 23.121 -12.220 14.412 1.00 32.73 ? 402 SER A OG 1 ATOM 3184 N N . LEU A 1 387 ? 24.522 -15.066 17.738 1.00 25.58 ? 403 LEU A N 1 ATOM 3185 C CA . LEU A 1 387 ? 25.215 -16.248 18.251 1.00 25.38 ? 403 LEU A CA 1 ATOM 3186 C C . LEU A 1 387 ? 24.229 -17.391 18.526 1.00 26.03 ? 403 LEU A C 1 ATOM 3187 O O . LEU A 1 387 ? 24.515 -18.536 18.180 1.00 26.22 ? 403 LEU A O 1 ATOM 3188 C CB . LEU A 1 387 ? 26.078 -15.931 19.479 1.00 24.44 ? 403 LEU A CB 1 ATOM 3189 C CG . LEU A 1 387 ? 27.499 -15.410 19.198 1.00 24.10 ? 403 LEU A CG 1 ATOM 3190 C CD1 . LEU A 1 387 ? 28.087 -14.722 20.426 1.00 23.57 ? 403 LEU A CD1 1 ATOM 3191 C CD2 . LEU A 1 387 ? 28.453 -16.506 18.704 1.00 23.95 ? 403 LEU A CD2 1 ATOM 3192 N N . SER A 1 388 ? 23.077 -17.074 19.129 1.00 26.14 ? 404 SER A N 1 ATOM 3193 C CA . SER A 1 388 ? 21.994 -18.049 19.320 1.00 26.55 ? 404 SER A CA 1 ATOM 3194 C C . SER A 1 388 ? 21.385 -18.490 17.989 1.00 26.81 ? 404 SER A C 1 ATOM 3195 O O . SER A 1 388 ? 21.199 -19.683 17.756 1.00 26.95 ? 404 SER A O 1 ATOM 3196 C CB . SER A 1 388 ? 20.883 -17.477 20.210 1.00 27.22 ? 404 SER A CB 1 ATOM 3197 O OG . SER A 1 388 ? 21.169 -17.696 21.583 1.00 27.31 ? 404 SER A OG 1 ATOM 3198 N N . VAL A 1 389 ? 21.062 -17.524 17.130 1.00 26.51 ? 405 VAL A N 1 ATOM 3199 C CA . VAL A 1 389 ? 20.473 -17.818 15.817 1.00 26.68 ? 405 VAL A CA 1 ATOM 3200 C C . VAL A 1 389 ? 21.333 -18.830 15.056 1.00 26.73 ? 405 VAL A C 1 ATOM 3201 O O . VAL A 1 389 ? 20.802 -19.720 14.389 1.00 27.41 ? 405 VAL A O 1 ATOM 3202 C CB . VAL A 1 389 ? 20.253 -16.537 14.971 1.00 26.44 ? 405 VAL A CB 1 ATOM 3203 C CG1 . VAL A 1 389 ? 19.741 -16.883 13.578 1.00 26.17 ? 405 VAL A CG1 1 ATOM 3204 C CG2 . VAL A 1 389 ? 19.271 -15.586 15.658 1.00 26.19 ? 405 VAL A CG2 1 ATOM 3205 N N . SER A 1 390 ? 22.653 -18.712 15.194 1.00 25.50 ? 406 SER A N 1 ATOM 3206 C CA . SER A 1 390 ? 23.593 -19.545 14.445 1.00 24.92 ? 406 SER A CA 1 ATOM 3207 C C . SER A 1 390 ? 23.730 -20.989 14.963 1.00 24.92 ? 406 SER A C 1 ATOM 3208 O O . SER A 1 390 ? 24.280 -21.838 14.268 1.00 24.42 ? 406 SER A O 1 ATOM 3209 C CB . SER A 1 390 ? 24.976 -18.878 14.397 1.00 24.58 ? 406 SER A CB 1 ATOM 3210 O OG . SER A 1 390 ? 25.621 -18.950 15.661 1.00 24.31 ? 406 SER A OG 1 ATOM 3211 N N . THR A 1 391 ? 23.256 -21.262 16.181 1.00 24.83 ? 407 THR A N 1 ATOM 3212 C CA . THR A 1 391 ? 23.377 -22.605 16.764 1.00 25.10 ? 407 THR A CA 1 ATOM 3213 C C . THR A 1 391 ? 22.541 -23.638 16.004 1.00 25.84 ? 407 THR A C 1 ATOM 3214 O O . THR A 1 391 ? 21.444 -23.324 15.523 1.00 25.60 ? 407 THR A O 1 ATOM 3215 C CB . THR A 1 391 ? 22.974 -22.661 18.263 1.00 25.25 ? 407 THR A CB 1 ATOM 3216 O OG1 . THR A 1 391 ? 21.597 -22.285 18.420 1.00 25.38 ? 407 THR A OG1 1 ATOM 3217 C CG2 . THR A 1 391 ? 23.855 -21.747 19.086 1.00 25.22 ? 407 THR A CG2 1 ATOM 3218 N N . PRO A 1 392 ? 23.064 -24.872 15.890 1.00 26.44 ? 408 PRO A N 1 ATOM 3219 C CA . PRO A 1 392 ? 22.243 -25.980 15.411 1.00 26.98 ? 408 PRO A CA 1 ATOM 3220 C C . PRO A 1 392 ? 20.913 -26.056 16.163 1.00 27.42 ? 408 PRO A C 1 ATOM 3221 O O . PRO A 1 392 ? 19.875 -26.260 15.544 1.00 27.32 ? 408 PRO A O 1 ATOM 3222 C CB . PRO A 1 392 ? 23.106 -27.206 15.713 1.00 27.27 ? 408 PRO A CB 1 ATOM 3223 C CG . PRO A 1 392 ? 24.503 -26.697 15.594 1.00 26.90 ? 408 PRO A CG 1 ATOM 3224 C CD . PRO A 1 392 ? 24.470 -25.277 16.091 1.00 26.34 ? 408 PRO A CD 1 ATOM 3225 N N . LYS A 1 393 ? 20.951 -25.858 17.482 1.00 27.66 ? 409 LYS A N 1 ATOM 3226 C CA . LYS A 1 393 ? 19.737 -25.855 18.301 1.00 28.67 ? 409 LYS A CA 1 ATOM 3227 C C . LYS A 1 393 ? 18.636 -24.940 17.752 1.00 28.70 ? 409 LYS A C 1 ATOM 3228 O O . LYS A 1 393 ? 17.487 -25.376 17.588 1.00 28.68 ? 409 LYS A O 1 ATOM 3229 C CB . LYS A 1 393 ? 20.054 -25.479 19.753 1.00 28.79 ? 409 LYS A CB 1 ATOM 3230 C CG . LYS A 1 393 ? 18.822 -25.419 20.653 1.00 30.33 ? 409 LYS A CG 1 ATOM 3231 C CD . LYS A 1 393 ? 19.179 -25.106 22.100 1.00 30.73 ? 409 LYS A CD 1 ATOM 3232 C CE . LYS A 1 393 ? 19.810 -26.316 22.777 1.00 31.47 ? 409 LYS A CE 1 ATOM 3233 N NZ . LYS A 1 393 ? 20.454 -25.928 24.063 1.00 31.50 ? 409 LYS A NZ 1 ATOM 3234 N N . HIS A 1 394 ? 18.981 -23.680 17.468 1.00 27.63 ? 410 HIS A N 1 ATOM 3235 C CA . HIS A 1 394 ? 17.987 -22.726 16.994 1.00 27.59 ? 410 HIS A CA 1 ATOM 3236 C C . HIS A 1 394 ? 17.581 -23.010 15.553 1.00 27.82 ? 410 HIS A C 1 ATOM 3237 O O . HIS A 1 394 ? 16.396 -22.936 15.201 1.00 28.20 ? 410 HIS A O 1 ATOM 3238 C CB . HIS A 1 394 ? 18.468 -21.273 17.136 1.00 27.25 ? 410 HIS A CB 1 ATOM 3239 C CG . HIS A 1 394 ? 17.414 -20.267 16.791 1.00 27.82 ? 410 HIS A CG 1 ATOM 3240 N ND1 . HIS A 1 394 ? 16.438 -19.877 17.682 1.00 28.02 ? 410 HIS A ND1 1 ATOM 3241 C CD2 . HIS A 1 394 ? 17.152 -19.610 15.637 1.00 28.05 ? 410 HIS A CD2 1 ATOM 3242 C CE1 . HIS A 1 394 ? 15.632 -19.009 17.099 1.00 28.48 ? 410 HIS A CE1 1 ATOM 3243 N NE2 . HIS A 1 394 ? 16.042 -18.831 15.856 1.00 28.63 ? 410 HIS A NE2 1 ATOM 3244 N N . LEU A 1 395 ? 18.563 -23.337 14.722 1.00 27.36 ? 411 LEU A N 1 ATOM 3245 C CA . LEU A 1 395 ? 18.305 -23.544 13.300 1.00 27.65 ? 411 LEU A CA 1 ATOM 3246 C C . LEU A 1 395 ? 17.388 -24.742 13.039 1.00 28.51 ? 411 LEU A C 1 ATOM 3247 O O . LEU A 1 395 ? 16.599 -24.721 12.086 1.00 28.49 ? 411 LEU A O 1 ATOM 3248 C CB . LEU A 1 395 ? 19.616 -23.618 12.510 1.00 27.05 ? 411 LEU A CB 1 ATOM 3249 C CG . LEU A 1 395 ? 20.390 -22.281 12.434 1.00 26.65 ? 411 LEU A CG 1 ATOM 3250 C CD1 . LEU A 1 395 ? 21.762 -22.474 11.796 1.00 25.94 ? 411 LEU A CD1 1 ATOM 3251 C CD2 . LEU A 1 395 ? 19.617 -21.190 11.697 1.00 26.28 ? 411 LEU A CD2 1 ATOM 3252 N N . GLU A 1 396 ? 17.475 -25.761 13.894 1.00 29.65 ? 412 GLU A N 1 ATOM 3253 C CA . GLU A 1 396 ? 16.523 -26.883 13.868 1.00 31.68 ? 412 GLU A CA 1 ATOM 3254 C C . GLU A 1 396 ? 15.104 -26.456 14.269 1.00 31.44 ? 412 GLU A C 1 ATOM 3255 O O . GLU A 1 396 ? 14.134 -26.901 13.659 1.00 31.47 ? 412 GLU A O 1 ATOM 3256 C CB . GLU A 1 396 ? 16.980 -28.034 14.768 1.00 34.25 ? 412 GLU A CB 1 ATOM 3257 C CG . GLU A 1 396 ? 18.275 -28.705 14.339 1.00 38.11 ? 412 GLU A CG 1 ATOM 3258 C CD . GLU A 1 396 ? 18.481 -30.055 15.005 1.00 41.83 ? 412 GLU A CD 1 ATOM 3259 O OE1 . GLU A 1 396 ? 18.011 -31.069 14.448 1.00 42.38 ? 412 GLU A OE1 1 ATOM 3260 O OE2 . GLU A 1 396 ? 19.104 -30.098 16.089 1.00 45.50 ? 412 GLU A OE2 1 ATOM 3261 N N . LYS A 1 397 ? 14.989 -25.604 15.292 1.00 31.60 ? 413 LYS A N 1 ATOM 3262 C CA . LYS A 1 397 ? 13.680 -25.079 15.736 1.00 32.06 ? 413 LYS A CA 1 ATOM 3263 C C . LYS A 1 397 ? 12.901 -24.383 14.616 1.00 32.19 ? 413 LYS A C 1 ATOM 3264 O O . LYS A 1 397 ? 11.673 -24.512 14.531 1.00 32.42 ? 413 LYS A O 1 ATOM 3265 C CB . LYS A 1 397 ? 13.833 -24.103 16.900 1.00 32.75 ? 413 LYS A CB 1 ATOM 3266 C CG . LYS A 1 397 ? 14.182 -24.761 18.214 1.00 33.68 ? 413 LYS A CG 1 ATOM 3267 C CD . LYS A 1 397 ? 14.236 -23.746 19.348 1.00 34.42 ? 413 LYS A CD 1 ATOM 3268 C CE . LYS A 1 397 ? 14.933 -24.380 20.545 1.00 35.16 ? 413 LYS A CE 1 ATOM 3269 N NZ . LYS A 1 397 ? 15.219 -23.415 21.639 1.00 35.21 ? 413 LYS A NZ 1 ATOM 3270 N N . ILE A 1 398 ? 13.612 -23.648 13.764 1.00 30.13 ? 414 ILE A N 1 ATOM 3271 C CA . ILE A 1 398 ? 12.956 -22.896 12.703 1.00 29.97 ? 414 ILE A CA 1 ATOM 3272 C C . ILE A 1 398 ? 12.971 -23.637 11.362 1.00 30.67 ? 414 ILE A C 1 ATOM 3273 O O . ILE A 1 398 ? 12.681 -23.042 10.326 1.00 31.44 ? 414 ILE A O 1 ATOM 3274 C CB . ILE A 1 398 ? 13.494 -21.443 12.585 1.00 29.44 ? 414 ILE A CB 1 ATOM 3275 C CG1 . ILE A 1 398 ? 15.008 -21.420 12.332 1.00 28.26 ? 414 ILE A CG1 1 ATOM 3276 C CG2 . ILE A 1 398 ? 13.171 -20.649 13.841 1.00 29.51 ? 414 ILE A CG2 1 ATOM 3277 C CD1 . ILE A 1 398 ? 15.566 -20.025 12.119 1.00 27.84 ? 414 ILE A CD1 1 ATOM 3278 N N . GLY A 1 399 ? 13.305 -24.930 11.389 1.00 30.31 ? 415 GLY A N 1 ATOM 3279 C CA . GLY A 1 399 ? 13.205 -25.783 10.210 1.00 31.09 ? 415 GLY A CA 1 ATOM 3280 C C . GLY A 1 399 ? 14.202 -25.508 9.100 1.00 31.42 ? 415 GLY A C 1 ATOM 3281 O O . GLY A 1 399 ? 14.018 -25.974 7.967 1.00 32.24 ? 415 GLY A O 1 ATOM 3282 N N . LEU A 1 400 ? 15.269 -24.773 9.412 1.00 30.49 ? 416 LEU A N 1 ATOM 3283 C CA . LEU A 1 400 ? 16.295 -24.463 8.415 1.00 30.26 ? 416 LEU A CA 1 ATOM 3284 C C . LEU A 1 400 ? 17.411 -25.514 8.370 1.00 30.42 ? 416 LEU A C 1 ATOM 3285 O O . LEU A 1 400 ? 18.089 -25.662 7.352 1.00 30.63 ? 416 LEU A O 1 ATOM 3286 C CB . LEU A 1 400 ? 16.867 -23.053 8.622 1.00 29.16 ? 416 LEU A CB 1 ATOM 3287 C CG . LEU A 1 400 ? 15.943 -21.864 8.311 1.00 29.49 ? 416 LEU A CG 1 ATOM 3288 C CD1 . LEU A 1 400 ? 16.679 -20.546 8.534 1.00 28.52 ? 416 LEU A CD1 1 ATOM 3289 C CD2 . LEU A 1 400 ? 15.388 -21.933 6.891 1.00 28.85 ? 416 LEU A CD2 1 ATOM 3290 N N . LEU A 1 401 ? 17.588 -26.245 9.468 1.00 30.95 ? 417 LEU A N 1 ATOM 3291 C CA . LEU A 1 401 ? 18.615 -27.280 9.546 1.00 31.41 ? 417 LEU A CA 1 ATOM 3292 C C . LEU A 1 401 ? 17.966 -28.650 9.720 1.00 33.17 ? 417 LEU A C 1 ATOM 3293 O O . LEU A 1 401 ? 17.304 -28.904 10.724 1.00 33.39 ? 417 LEU A O 1 ATOM 3294 C CB . LEU A 1 401 ? 19.583 -26.978 10.690 1.00 30.29 ? 417 LEU A CB 1 ATOM 3295 C CG . LEU A 1 401 ? 20.715 -27.970 10.983 1.00 29.90 ? 417 LEU A CG 1 ATOM 3296 C CD1 . LEU A 1 401 ? 21.666 -28.121 9.803 1.00 29.47 ? 417 LEU A CD1 1 ATOM 3297 C CD2 . LEU A 1 401 ? 21.469 -27.541 12.233 1.00 28.80 ? 417 LEU A CD2 1 ATOM 3298 N N . LYS A 1 402 ? 18.153 -29.519 8.731 1.00 35.24 ? 418 LYS A N 1 ATOM 3299 C CA . LYS A 1 402 ? 17.451 -30.811 8.682 1.00 37.78 ? 418 LYS A CA 1 ATOM 3300 C C . LYS A 1 402 ? 18.398 -32.001 8.820 1.00 38.26 ? 418 LYS A C 1 ATOM 3301 O O . LYS A 1 402 ? 19.528 -31.965 8.322 1.00 37.14 ? 418 LYS A O 1 ATOM 3302 C CB . LYS A 1 402 ? 16.651 -30.926 7.378 1.00 38.92 ? 418 LYS A CB 1 ATOM 3303 C CG . LYS A 1 402 ? 15.613 -29.821 7.195 1.00 40.43 ? 418 LYS A CG 1 ATOM 3304 C CD . LYS A 1 402 ? 14.813 -30.021 5.917 1.00 42.04 ? 418 LYS A CD 1 ATOM 3305 C CE . LYS A 1 402 ? 13.932 -28.821 5.594 1.00 41.40 ? 418 LYS A CE 1 ATOM 3306 N NZ . LYS A 1 402 ? 12.935 -28.498 6.642 1.00 41.72 ? 418 LYS A NZ 1 ATOM 3307 N N . ASP A 1 403 ? 17.922 -33.038 9.512 1.00 39.14 ? 419 ASP A N 1 ATOM 3308 C CA . ASP A 1 403 ? 18.632 -34.321 9.680 1.00 39.88 ? 419 ASP A CA 1 ATOM 3309 C C . ASP A 1 403 ? 20.033 -34.179 10.284 1.00 38.71 ? 419 ASP A C 1 ATOM 3310 O O . ASP A 1 403 ? 20.973 -34.856 9.866 1.00 38.26 ? 419 ASP A O 1 ATOM 3311 C CB . ASP A 1 403 ? 18.687 -35.096 8.349 1.00 42.06 ? 419 ASP A CB 1 ATOM 3312 C CG . ASP A 1 403 ? 17.307 -35.365 7.767 1.00 43.99 ? 419 ASP A CG 1 ATOM 3313 O OD1 . ASP A 1 403 ? 16.428 -35.876 8.494 1.00 45.23 ? 419 ASP A OD1 1 ATOM 3314 O OD2 . ASP A 1 403 ? 17.102 -35.065 6.574 1.00 46.63 ? 419 ASP A OD2 1 ATOM 3315 N N . TYR A 1 404 ? 20.155 -33.302 11.278 1.00 36.93 ? 420 TYR A N 1 ATOM 3316 C CA . TYR A 1 404 ? 21.434 -32.992 11.902 1.00 36.00 ? 420 TYR A CA 1 ATOM 3317 C C . TYR A 1 404 ? 21.713 -33.935 13.075 1.00 36.84 ? 420 TYR A C 1 ATOM 3318 O O . TYR A 1 404 ? 20.878 -34.075 13.968 1.00 37.61 ? 420 TYR A O 1 ATOM 3319 C CB . TYR A 1 404 ? 21.435 -31.527 12.375 1.00 34.41 ? 420 TYR A CB 1 ATOM 3320 C CG . TYR A 1 404 ? 22.786 -30.991 12.801 1.00 33.37 ? 420 TYR A CG 1 ATOM 3321 C CD1 . TYR A 1 404 ? 23.748 -30.613 11.850 1.00 32.84 ? 420 TYR A CD1 1 ATOM 3322 C CD2 . TYR A 1 404 ? 23.098 -30.842 14.150 1.00 32.86 ? 420 TYR A CD2 1 ATOM 3323 C CE1 . TYR A 1 404 ? 24.982 -30.112 12.243 1.00 32.13 ? 420 TYR A CE1 1 ATOM 3324 C CE2 . TYR A 1 404 ? 24.329 -30.350 14.550 1.00 32.26 ? 420 TYR A CE2 1 ATOM 3325 C CZ . TYR A 1 404 ? 25.263 -29.987 13.598 1.00 31.75 ? 420 TYR A CZ 1 ATOM 3326 O OH . TYR A 1 404 ? 26.473 -29.494 14.012 1.00 31.79 ? 420 TYR A OH 1 ATOM 3327 N N . VAL A 1 405 ? 22.879 -34.580 13.061 1.00 37.19 ? 421 VAL A N 1 ATOM 3328 C CA . VAL A 1 405 ? 23.335 -35.406 14.185 1.00 38.65 ? 421 VAL A CA 1 ATOM 3329 C C . VAL A 1 405 ? 24.518 -34.703 14.857 1.00 39.91 ? 421 VAL A C 1 ATOM 3330 O O . VAL A 1 405 ? 25.599 -34.575 14.269 1.00 38.96 ? 421 VAL A O 1 ATOM 3331 C CB . VAL A 1 405 ? 23.739 -36.832 13.739 1.00 39.47 ? 421 VAL A CB 1 ATOM 3332 C CG1 . VAL A 1 405 ? 24.315 -37.619 14.912 1.00 39.24 ? 421 VAL A CG1 1 ATOM 3333 C CG2 . VAL A 1 405 ? 22.549 -37.567 13.133 1.00 39.42 ? 421 VAL A CG2 1 ATOM 3334 N N . ARG A 1 406 ? 24.309 -34.245 16.086 1.00 40.78 ? 422 ARG A N 1 ATOM 3335 C CA . ARG A 1 406 ? 25.308 -33.431 16.769 1.00 42.16 ? 422 ARG A CA 1 ATOM 3336 C C . ARG A 1 406 ? 26.316 -34.296 17.538 1.00 41.36 ? 422 ARG A C 1 ATOM 3337 O O . ARG A 1 406 ? 26.308 -34.324 18.767 1.00 43.06 ? 422 ARG A O 1 ATOM 3338 C CB . ARG A 1 406 ? 24.628 -32.401 17.690 1.00 43.62 ? 422 ARG A CB 1 ATOM 3339 C CG . ARG A 1 406 ? 25.569 -31.345 18.259 1.00 46.14 ? 422 ARG A CG 1 ATOM 3340 C CD . ARG A 1 406 ? 24.944 -30.594 19.428 1.00 48.31 ? 422 ARG A CD 1 ATOM 3341 N NE . ARG A 1 406 ? 25.945 -30.193 20.425 1.00 49.69 ? 422 ARG A NE 1 ATOM 3342 C CZ . ARG A 1 406 ? 26.694 -29.098 20.332 1.00 49.29 ? 422 ARG A CZ 1 ATOM 3343 N NH1 . ARG A 1 406 ? 26.554 -28.296 19.288 1.00 51.18 ? 422 ARG A NH1 1 ATOM 3344 N NH2 . ARG A 1 406 ? 27.578 -28.798 21.275 1.00 48.43 ? 422 ARG A NH2 1 ATOM 3345 N N . ASP A 1 407 ? 27.178 -35.007 16.817 1.00 38.93 ? 423 ASP A N 1 ATOM 3346 C CA . ASP A 1 407 ? 28.240 -35.777 17.474 1.00 37.54 ? 423 ASP A CA 1 ATOM 3347 C C . ASP A 1 407 ? 29.495 -34.913 17.707 1.00 36.36 ? 423 ASP A C 1 ATOM 3348 O O . ASP A 1 407 ? 29.469 -33.703 17.458 1.00 34.79 ? 423 ASP A O 1 ATOM 3349 C CB . ASP A 1 407 ? 28.546 -37.078 16.711 1.00 37.78 ? 423 ASP A CB 1 ATOM 3350 C CG . ASP A 1 407 ? 28.964 -36.840 15.266 1.00 37.57 ? 423 ASP A CG 1 ATOM 3351 O OD1 . ASP A 1 407 ? 29.453 -35.740 14.936 1.00 36.15 ? 423 ASP A OD1 1 ATOM 3352 O OD2 . ASP A 1 407 ? 28.804 -37.767 14.450 1.00 38.21 ? 423 ASP A OD2 1 ATOM 3353 N N . ASP A 1 408 ? 30.576 -35.524 18.193 1.00 35.92 ? 424 ASP A N 1 ATOM 3354 C CA . ASP A 1 408 ? 31.819 -34.796 18.491 1.00 35.73 ? 424 ASP A CA 1 ATOM 3355 C C . ASP A 1 408 ? 32.414 -34.112 17.260 1.00 34.19 ? 424 ASP A C 1 ATOM 3356 O O . ASP A 1 408 ? 32.915 -32.992 17.342 1.00 33.75 ? 424 ASP A O 1 ATOM 3357 C CB . ASP A 1 408 ? 32.866 -35.732 19.095 1.00 37.85 ? 424 ASP A CB 1 ATOM 3358 C CG . ASP A 1 408 ? 32.517 -36.180 20.504 1.00 40.69 ? 424 ASP A CG 1 ATOM 3359 O OD1 . ASP A 1 408 ? 31.570 -35.637 21.108 1.00 42.03 ? 424 ASP A OD1 1 ATOM 3360 O OD2 . ASP A 1 408 ? 33.203 -37.089 21.013 1.00 44.07 ? 424 ASP A OD2 1 ATOM 3361 N N . GLU A 1 409 ? 32.363 -34.799 16.125 1.00 32.90 ? 425 GLU A N 1 ATOM 3362 C CA . GLU A 1 409 ? 32.921 -34.273 14.885 1.00 31.74 ? 425 GLU A CA 1 ATOM 3363 C C . GLU A 1 409 ? 32.101 -33.096 14.329 1.00 30.62 ? 425 GLU A C 1 ATOM 3364 O O . GLU A 1 409 ? 32.673 -32.090 13.909 1.00 29.08 ? 425 GLU A O 1 ATOM 3365 C CB . GLU A 1 409 ? 33.116 -35.398 13.864 1.00 32.92 ? 425 GLU A CB 1 ATOM 3366 C CG . GLU A 1 409 ? 34.207 -36.378 14.291 1.00 34.66 ? 425 GLU A CG 1 ATOM 3367 C CD . GLU A 1 409 ? 34.484 -37.488 13.288 1.00 36.96 ? 425 GLU A CD 1 ATOM 3368 O OE1 . GLU A 1 409 ? 33.711 -37.657 12.320 1.00 37.61 ? 425 GLU A OE1 1 ATOM 3369 O OE2 . GLU A 1 409 ? 35.495 -38.202 13.472 1.00 38.12 ? 425 GLU A OE2 1 ATOM 3370 N N . ALA A 1 410 ? 30.772 -33.209 14.360 1.00 28.99 ? 426 ALA A N 1 ATOM 3371 C CA . ALA A 1 410 ? 29.908 -32.114 13.918 1.00 28.10 ? 426 ALA A CA 1 ATOM 3372 C C . ALA A 1 410 ? 30.092 -30.900 14.826 1.00 27.59 ? 426 ALA A C 1 ATOM 3373 O O . ALA A 1 410 ? 30.065 -29.762 14.351 1.00 26.35 ? 426 ALA A O 1 ATOM 3374 C CB . ALA A 1 410 ? 28.449 -32.544 13.882 1.00 28.27 ? 426 ALA A CB 1 ATOM 3375 N N . ARG A 1 411 ? 30.288 -31.148 16.125 1.00 26.87 ? 427 ARG A N 1 ATOM 3376 C CA . ARG A 1 411 ? 30.562 -30.066 17.063 1.00 27.03 ? 427 ARG A CA 1 ATOM 3377 C C . ARG A 1 411 ? 31.835 -29.285 16.697 1.00 25.96 ? 427 ARG A C 1 ATOM 3378 O O . ARG A 1 411 ? 31.811 -28.053 16.636 1.00 25.46 ? 427 ARG A O 1 ATOM 3379 C CB . ARG A 1 411 ? 30.652 -30.573 18.498 1.00 27.83 ? 427 ARG A CB 1 ATOM 3380 C CG . ARG A 1 411 ? 30.571 -29.436 19.495 1.00 28.65 ? 427 ARG A CG 1 ATOM 3381 C CD . ARG A 1 411 ? 31.255 -29.776 20.801 1.00 29.69 ? 427 ARG A CD 1 ATOM 3382 N NE . ARG A 1 411 ? 31.099 -28.698 21.769 1.00 30.04 ? 427 ARG A NE 1 ATOM 3383 C CZ . ARG A 1 411 ? 31.536 -28.758 23.022 1.00 30.35 ? 427 ARG A CZ 1 ATOM 3384 N NH1 . ARG A 1 411 ? 32.157 -29.850 23.458 1.00 30.55 ? 427 ARG A NH1 1 ATOM 3385 N NH2 . ARG A 1 411 ? 31.350 -27.732 23.839 1.00 30.39 ? 427 ARG A NH2 1 ATOM 3386 N N . ILE A 1 412 ? 32.930 -30.003 16.455 1.00 25.54 ? 428 ILE A N 1 ATOM 3387 C CA . ILE A 1 412 ? 34.179 -29.378 15.992 1.00 25.14 ? 428 ILE A CA 1 ATOM 3388 C C . ILE A 1 412 ? 33.977 -28.563 14.711 1.00 24.43 ? 428 ILE A C 1 ATOM 3389 O O . ILE A 1 412 ? 34.460 -27.433 14.622 1.00 24.21 ? 428 ILE A O 1 ATOM 3390 C CB . ILE A 1 412 ? 35.339 -30.401 15.836 1.00 25.10 ? 428 ILE A CB 1 ATOM 3391 C CG1 . ILE A 1 412 ? 35.712 -31.002 17.200 1.00 25.45 ? 428 ILE A CG1 1 ATOM 3392 C CG2 . ILE A 1 412 ? 36.569 -29.756 15.193 1.00 24.49 ? 428 ILE A CG2 1 ATOM 3393 C CD1 . ILE A 1 412 ? 36.145 -29.985 18.240 1.00 26.01 ? 428 ILE A CD1 1 ATOM 3394 N N . ASN A 1 413 ? 33.266 -29.126 13.738 1.00 24.59 ? 429 ASN A N 1 ATOM 3395 C CA . ASN A 1 413 ? 32.938 -28.397 12.506 1.00 24.72 ? 429 ASN A CA 1 ATOM 3396 C C . ASN A 1 413 ? 32.236 -27.060 12.797 1.00 24.83 ? 429 ASN A C 1 ATOM 3397 O O . ASN A 1 413 ? 32.549 -26.038 12.173 1.00 23.81 ? 429 ASN A O 1 ATOM 3398 C CB . ASN A 1 413 ? 32.054 -29.243 11.590 1.00 25.71 ? 429 ASN A CB 1 ATOM 3399 C CG . ASN A 1 413 ? 32.844 -30.196 10.699 1.00 26.33 ? 429 ASN A CG 1 ATOM 3400 O OD1 . ASN A 1 413 ? 34.077 -30.241 10.727 1.00 26.44 ? 429 ASN A OD1 1 ATOM 3401 N ND2 . ASN A 1 413 ? 32.122 -30.977 9.903 1.00 26.55 ? 429 ASN A ND2 1 ATOM 3402 N N . GLN A 1 414 ? 31.294 -27.073 13.746 1.00 24.66 ? 430 GLN A N 1 ATOM 3403 C CA . GLN A 1 414 ? 30.503 -25.870 14.060 1.00 25.01 ? 430 GLN A CA 1 ATOM 3404 C C . GLN A 1 414 ? 31.324 -24.835 14.838 1.00 24.32 ? 430 GLN A C 1 ATOM 3405 O O . GLN A 1 414 ? 31.247 -23.634 14.556 1.00 23.54 ? 430 GLN A O 1 ATOM 3406 C CB . GLN A 1 414 ? 29.208 -26.240 14.793 1.00 26.44 ? 430 GLN A CB 1 ATOM 3407 C CG . GLN A 1 414 ? 28.378 -25.058 15.298 1.00 27.63 ? 430 GLN A CG 1 ATOM 3408 C CD . GLN A 1 414 ? 27.813 -24.159 14.205 1.00 28.87 ? 430 GLN A CD 1 ATOM 3409 O OE1 . GLN A 1 414 ? 27.627 -24.572 13.052 1.00 29.07 ? 430 GLN A OE1 1 ATOM 3410 N NE2 . GLN A 1 414 ? 27.509 -22.912 14.577 1.00 29.93 ? 430 GLN A NE2 1 ATOM 3411 N N . LEU A 1 415 ? 32.104 -25.308 15.813 1.00 24.37 ? 431 LEU A N 1 ATOM 3412 C CA . LEU A 1 415 ? 33.047 -24.447 16.516 1.00 24.77 ? 431 LEU A CA 1 ATOM 3413 C C . LEU A 1 415 ? 34.044 -23.794 15.561 1.00 24.06 ? 431 LEU A C 1 ATOM 3414 O O . LEU A 1 415 ? 34.303 -22.587 15.662 1.00 23.48 ? 431 LEU A O 1 ATOM 3415 C CB . LEU A 1 415 ? 33.784 -25.216 17.614 1.00 25.01 ? 431 LEU A CB 1 ATOM 3416 C CG . LEU A 1 415 ? 33.025 -25.436 18.928 1.00 26.27 ? 431 LEU A CG 1 ATOM 3417 C CD1 . LEU A 1 415 ? 33.645 -26.572 19.735 1.00 26.94 ? 431 LEU A CD1 1 ATOM 3418 C CD2 . LEU A 1 415 ? 32.934 -24.163 19.771 1.00 26.14 ? 431 LEU A CD2 1 ATOM 3419 N N . PHE A 1 416 ? 34.593 -24.588 14.641 1.00 23.67 ? 432 PHE A N 1 ATOM 3420 C CA . PHE A 1 416 ? 35.564 -24.080 13.677 1.00 23.45 ? 432 PHE A CA 1 ATOM 3421 C C . PHE A 1 416 ? 34.916 -23.026 12.786 1.00 23.19 ? 432 PHE A C 1 ATOM 3422 O O . PHE A 1 416 ? 35.486 -21.962 12.582 1.00 22.64 ? 432 PHE A O 1 ATOM 3423 C CB . PHE A 1 416 ? 36.180 -25.210 12.839 1.00 23.58 ? 432 PHE A CB 1 ATOM 3424 C CG . PHE A 1 416 ? 37.427 -24.805 12.090 1.00 23.60 ? 432 PHE A CG 1 ATOM 3425 C CD1 . PHE A 1 416 ? 38.656 -24.722 12.739 1.00 23.88 ? 432 PHE A CD1 1 ATOM 3426 C CD2 . PHE A 1 416 ? 37.372 -24.506 10.734 1.00 23.74 ? 432 PHE A CD2 1 ATOM 3427 C CE1 . PHE A 1 416 ? 39.806 -24.349 12.046 1.00 24.34 ? 432 PHE A CE1 1 ATOM 3428 C CE2 . PHE A 1 416 ? 38.517 -24.136 10.034 1.00 23.76 ? 432 PHE A CE2 1 ATOM 3429 C CZ . PHE A 1 416 ? 39.736 -24.060 10.688 1.00 24.05 ? 432 PHE A CZ 1 ATOM 3430 N N . LEU A 1 417 ? 33.719 -23.328 12.278 1.00 23.65 ? 433 LEU A N 1 ATOM 3431 C CA . LEU A 1 417 ? 32.945 -22.386 11.471 1.00 23.19 ? 433 LEU A CA 1 ATOM 3432 C C . LEU A 1 417 ? 32.756 -21.068 12.217 1.00 22.65 ? 433 LEU A C 1 ATOM 3433 O O . LEU A 1 417 ? 32.961 -20.003 11.643 1.00 22.30 ? 433 LEU A O 1 ATOM 3434 C CB . LEU A 1 417 ? 31.578 -22.979 11.079 1.00 23.89 ? 433 LEU A CB 1 ATOM 3435 C CG . LEU A 1 417 ? 30.555 -22.091 10.343 1.00 24.22 ? 433 LEU A CG 1 ATOM 3436 C CD1 . LEU A 1 417 ? 31.049 -21.699 8.946 1.00 24.22 ? 433 LEU A CD1 1 ATOM 3437 C CD2 . LEU A 1 417 ? 29.191 -22.780 10.244 1.00 24.58 ? 433 LEU A CD2 1 ATOM 3438 N N . THR A 1 418 ? 32.375 -21.141 13.498 1.00 21.92 ? 434 THR A N 1 ATOM 3439 C CA . THR A 1 418 ? 32.223 -19.927 14.321 1.00 21.44 ? 434 THR A CA 1 ATOM 3440 C C . THR A 1 418 ? 33.558 -19.157 14.478 1.00 20.75 ? 434 THR A C 1 ATOM 3441 O O . THR A 1 418 ? 33.572 -17.924 14.410 1.00 20.69 ? 434 THR A O 1 ATOM 3442 C CB . THR A 1 418 ? 31.577 -20.234 15.702 1.00 21.51 ? 434 THR A CB 1 ATOM 3443 O OG1 . THR A 1 418 ? 30.328 -20.912 15.505 1.00 22.33 ? 434 THR A OG1 1 ATOM 3444 C CG2 . THR A 1 418 ? 31.301 -18.947 16.489 1.00 21.42 ? 434 THR A CG2 1 ATOM 3445 N N . ALA A 1 419 ? 34.663 -19.883 14.662 1.00 20.24 ? 435 ALA A N 1 ATOM 3446 C CA . ALA A 1 419 ? 35.986 -19.264 14.838 1.00 20.06 ? 435 ALA A CA 1 ATOM 3447 C C . ALA A 1 419 ? 36.444 -18.544 13.571 1.00 20.39 ? 435 ALA A C 1 ATOM 3448 O O . ALA A 1 419 ? 37.128 -17.510 13.635 1.00 19.83 ? 435 ALA A O 1 ATOM 3449 C CB . ALA A 1 419 ? 37.020 -20.303 15.268 1.00 19.44 ? 435 ALA A CB 1 ATOM 3450 N N . LEU A 1 420 ? 36.061 -19.090 12.419 1.00 20.87 ? 436 LEU A N 1 ATOM 3451 C CA . LEU A 1 420 ? 36.383 -18.468 11.135 1.00 21.86 ? 436 LEU A CA 1 ATOM 3452 C C . LEU A 1 420 ? 35.781 -17.058 10.997 1.00 23.02 ? 436 LEU A C 1 ATOM 3453 O O . LEU A 1 420 ? 36.251 -16.258 10.184 1.00 23.08 ? 436 LEU A O 1 ATOM 3454 C CB . LEU A 1 420 ? 35.939 -19.360 9.977 1.00 21.60 ? 436 LEU A CB 1 ATOM 3455 C CG . LEU A 1 420 ? 36.733 -20.650 9.710 1.00 22.03 ? 436 LEU A CG 1 ATOM 3456 C CD1 . LEU A 1 420 ? 36.025 -21.498 8.663 1.00 22.00 ? 436 LEU A CD1 1 ATOM 3457 C CD2 . LEU A 1 420 ? 38.177 -20.390 9.288 1.00 21.75 ? 436 LEU A CD2 1 ATOM 3458 N N . ASP A 1 421 ? 34.743 -16.773 11.785 1.00 24.40 ? 437 ASP A N 1 ATOM 3459 C CA . ASP A 1 421 ? 34.198 -15.414 11.919 1.00 26.22 ? 437 ASP A CA 1 ATOM 3460 C C . ASP A 1 421 ? 34.724 -14.697 13.155 1.00 24.79 ? 437 ASP A C 1 ATOM 3461 O O . ASP A 1 421 ? 35.178 -13.560 13.072 1.00 25.69 ? 437 ASP A O 1 ATOM 3462 C CB . ASP A 1 421 ? 32.665 -15.432 11.993 1.00 29.27 ? 437 ASP A CB 1 ATOM 3463 C CG . ASP A 1 421 ? 32.020 -15.949 10.728 1.00 32.32 ? 437 ASP A CG 1 ATOM 3464 O OD1 . ASP A 1 421 ? 32.427 -15.538 9.621 1.00 33.92 ? 437 ASP A OD1 1 ATOM 3465 O OD2 . ASP A 1 421 ? 31.091 -16.778 10.854 1.00 36.33 ? 437 ASP A OD2 1 ATOM 3466 N N . LYS A 1 422 ? 34.662 -15.362 14.300 1.00 23.09 ? 438 LYS A N 1 ATOM 3467 C CA . LYS A 1 422 ? 34.843 -14.679 15.578 1.00 22.44 ? 438 LYS A CA 1 ATOM 3468 C C . LYS A 1 422 ? 36.304 -14.481 16.027 1.00 22.22 ? 438 LYS A C 1 ATOM 3469 O O . LYS A 1 422 ? 36.632 -13.446 16.621 1.00 22.28 ? 438 LYS A O 1 ATOM 3470 C CB . LYS A 1 422 ? 34.006 -15.358 16.676 1.00 22.55 ? 438 LYS A CB 1 ATOM 3471 C CG . LYS A 1 422 ? 32.498 -15.357 16.433 1.00 22.32 ? 438 LYS A CG 1 ATOM 3472 C CD . LYS A 1 422 ? 31.894 -13.953 16.371 1.00 22.22 ? 438 LYS A CD 1 ATOM 3473 C CE . LYS A 1 422 ? 30.375 -14.010 16.227 1.00 22.37 ? 438 LYS A CE 1 ATOM 3474 N NZ . LYS A 1 422 ? 29.804 -12.656 15.956 1.00 22.53 ? 438 LYS A NZ 1 ATOM 3475 N N . ILE A 1 423 ? 37.177 -15.445 15.730 1.00 20.96 ? 439 ILE A N 1 ATOM 3476 C CA . ILE A 1 423 ? 38.605 -15.307 16.047 1.00 20.31 ? 439 ILE A CA 1 ATOM 3477 C C . ILE A 1 423 ? 39.367 -14.614 14.912 1.00 19.75 ? 439 ILE A C 1 ATOM 3478 O O . ILE A 1 423 ? 40.167 -13.701 15.146 1.00 19.46 ? 439 ILE A O 1 ATOM 3479 C CB . ILE A 1 423 ? 39.279 -16.665 16.380 1.00 20.28 ? 439 ILE A CB 1 ATOM 3480 C CG1 . ILE A 1 423 ? 38.553 -17.374 17.552 1.00 20.52 ? 439 ILE A CG1 1 ATOM 3481 C CG2 . ILE A 1 423 ? 40.771 -16.472 16.653 1.00 19.50 ? 439 ILE A CG2 1 ATOM 3482 C CD1 . ILE A 1 423 ? 38.505 -16.588 18.853 1.00 21.22 ? 439 ILE A CD1 1 ATOM 3483 N N . VAL A 1 424 ? 39.124 -15.056 13.683 1.00 19.37 ? 440 VAL A N 1 ATOM 3484 C CA . VAL A 1 424 ? 39.763 -14.456 12.527 1.00 18.56 ? 440 VAL A CA 1 ATOM 3485 C C . VAL A 1 424 ? 39.611 -12.920 12.519 1.00 18.08 ? 440 VAL A C 1 ATOM 3486 O O . VAL A 1 424 ? 40.572 -12.194 12.257 1.00 18.12 ? 440 VAL A O 1 ATOM 3487 C CB . VAL A 1 424 ? 39.205 -15.083 11.233 1.00 18.85 ? 440 VAL A CB 1 ATOM 3488 C CG1 . VAL A 1 424 ? 39.516 -14.215 10.035 1.00 19.59 ? 440 VAL A CG1 1 ATOM 3489 C CG2 . VAL A 1 424 ? 39.730 -16.503 11.050 1.00 19.17 ? 440 VAL A CG2 1 ATOM 3490 N N . PHE A 1 425 ? 38.405 -12.441 12.829 1.00 17.80 ? 441 PHE A N 1 ATOM 3491 C CA . PHE A 1 425 ? 38.079 -11.004 12.829 1.00 17.70 ? 441 PHE A CA 1 ATOM 3492 C C . PHE A 1 425 ? 38.944 -10.135 13.732 1.00 17.22 ? 441 PHE A C 1 ATOM 3493 O O . PHE A 1 425 ? 39.155 -8.961 13.447 1.00 16.81 ? 441 PHE A O 1 ATOM 3494 C CB . PHE A 1 425 ? 36.618 -10.820 13.253 1.00 17.73 ? 441 PHE A CB 1 ATOM 3495 C CG . PHE A 1 425 ? 36.074 -9.422 13.034 1.00 17.97 ? 441 PHE A CG 1 ATOM 3496 C CD1 . PHE A 1 425 ? 35.808 -8.947 11.744 1.00 17.67 ? 441 PHE A CD1 1 ATOM 3497 C CD2 . PHE A 1 425 ? 35.802 -8.592 14.112 1.00 17.67 ? 441 PHE A CD2 1 ATOM 3498 C CE1 . PHE A 1 425 ? 35.290 -7.661 11.549 1.00 17.73 ? 441 PHE A CE1 1 ATOM 3499 C CE2 . PHE A 1 425 ? 35.270 -7.318 13.925 1.00 17.79 ? 441 PHE A CE2 1 ATOM 3500 C CZ . PHE A 1 425 ? 35.019 -6.850 12.645 1.00 18.06 ? 441 PHE A CZ 1 ATOM 3501 N N . LEU A 1 426 ? 39.389 -10.687 14.856 1.00 17.63 ? 442 LEU A N 1 ATOM 3502 C CA . LEU A 1 426 ? 40.068 -9.874 15.860 1.00 17.97 ? 442 LEU A CA 1 ATOM 3503 C C . LEU A 1 426 ? 41.319 -9.113 15.360 1.00 17.72 ? 442 LEU A C 1 ATOM 3504 O O . LEU A 1 426 ? 41.360 -7.882 15.487 1.00 17.64 ? 442 LEU A O 1 ATOM 3505 C CB . LEU A 1 426 ? 40.354 -10.688 17.126 1.00 18.25 ? 442 LEU A CB 1 ATOM 3506 C CG . LEU A 1 426 ? 39.146 -11.404 17.714 1.00 18.97 ? 442 LEU A CG 1 ATOM 3507 C CD1 . LEU A 1 426 ? 39.614 -12.327 18.824 1.00 18.69 ? 442 LEU A CD1 1 ATOM 3508 C CD2 . LEU A 1 426 ? 38.121 -10.396 18.219 1.00 19.20 ? 442 LEU A CD2 1 ATOM 3509 N N . PRO A 1 427 ? 42.317 -9.816 14.765 1.00 17.84 ? 443 PRO A N 1 ATOM 3510 C CA . PRO A 1 427 ? 43.436 -9.016 14.264 1.00 17.59 ? 443 PRO A CA 1 ATOM 3511 C C . PRO A 1 427 ? 43.017 -8.083 13.132 1.00 17.42 ? 443 PRO A C 1 ATOM 3512 O O . PRO A 1 427 ? 43.566 -6.985 13.018 1.00 16.88 ? 443 PRO A O 1 ATOM 3513 C CB . PRO A 1 427 ? 44.460 -10.057 13.764 1.00 17.36 ? 443 PRO A CB 1 ATOM 3514 C CG . PRO A 1 427 ? 43.753 -11.358 13.724 1.00 17.67 ? 443 PRO A CG 1 ATOM 3515 C CD . PRO A 1 427 ? 42.537 -11.269 14.596 1.00 17.63 ? 443 PRO A CD 1 ATOM 3516 N N . PHE A 1 428 ? 42.076 -8.513 12.287 1.00 18.06 ? 444 PHE A N 1 ATOM 3517 C CA . PHE A 1 428 ? 41.575 -7.620 11.236 1.00 17.29 ? 444 PHE A CA 1 ATOM 3518 C C . PHE A 1 428 ? 41.094 -6.267 11.789 1.00 17.28 ? 444 PHE A C 1 ATOM 3519 O O . PHE A 1 428 ? 41.518 -5.196 11.325 1.00 16.45 ? 444 PHE A O 1 ATOM 3520 C CB . PHE A 1 428 ? 40.436 -8.245 10.423 1.00 18.17 ? 444 PHE A CB 1 ATOM 3521 C CG . PHE A 1 428 ? 39.798 -7.262 9.487 1.00 17.60 ? 444 PHE A CG 1 ATOM 3522 C CD1 . PHE A 1 428 ? 40.356 -7.017 8.236 1.00 17.56 ? 444 PHE A CD1 1 ATOM 3523 C CD2 . PHE A 1 428 ? 38.681 -6.521 9.881 1.00 17.54 ? 444 PHE A CD2 1 ATOM 3524 C CE1 . PHE A 1 428 ? 39.800 -6.076 7.385 1.00 17.58 ? 444 PHE A CE1 1 ATOM 3525 C CE2 . PHE A 1 428 ? 38.123 -5.574 9.030 1.00 17.94 ? 444 PHE A CE2 1 ATOM 3526 C CZ . PHE A 1 428 ? 38.680 -5.355 7.775 1.00 17.61 ? 444 PHE A CZ 1 ATOM 3527 N N . ALA A 1 429 ? 40.232 -6.327 12.810 1.00 17.23 ? 445 ALA A N 1 ATOM 3528 C CA . ALA A 1 429 ? 39.574 -5.140 13.350 1.00 17.09 ? 445 ALA A CA 1 ATOM 3529 C C . ALA A 1 429 ? 40.593 -4.253 14.058 1.00 17.80 ? 445 ALA A C 1 ATOM 3530 O O . ALA A 1 429 ? 40.540 -3.030 13.932 1.00 17.18 ? 445 ALA A O 1 ATOM 3531 C CB . ALA A 1 429 ? 38.459 -5.543 14.303 1.00 17.01 ? 445 ALA A CB 1 ATOM 3532 N N . PHE A 1 430 ? 41.501 -4.872 14.827 1.00 18.40 ? 446 PHE A N 1 ATOM 3533 C CA . PHE A 1 430 ? 42.592 -4.136 15.470 1.00 18.96 ? 446 PHE A CA 1 ATOM 3534 C C . PHE A 1 430 ? 43.403 -3.321 14.441 1.00 19.23 ? 446 PHE A C 1 ATOM 3535 O O . PHE A 1 430 ? 43.702 -2.144 14.699 1.00 19.64 ? 446 PHE A O 1 ATOM 3536 C CB . PHE A 1 430 ? 43.506 -5.079 16.291 1.00 19.54 ? 446 PHE A CB 1 ATOM 3537 C CG . PHE A 1 430 ? 44.039 -4.479 17.572 1.00 19.91 ? 446 PHE A CG 1 ATOM 3538 C CD1 . PHE A 1 430 ? 43.823 -3.136 17.891 1.00 20.70 ? 446 PHE A CD1 1 ATOM 3539 C CD2 . PHE A 1 430 ? 44.784 -5.263 18.463 1.00 20.97 ? 446 PHE A CD2 1 ATOM 3540 C CE1 . PHE A 1 430 ? 44.301 -2.593 19.081 1.00 20.58 ? 446 PHE A CE1 1 ATOM 3541 C CE2 . PHE A 1 430 ? 45.287 -4.722 19.641 1.00 20.99 ? 446 PHE A CE2 1 ATOM 3542 C CZ . PHE A 1 430 ? 45.053 -3.383 19.945 1.00 21.05 ? 446 PHE A CZ 1 ATOM 3543 N N . THR A 1 431 ? 43.724 -3.914 13.280 1.00 18.66 ? 447 THR A N 1 ATOM 3544 C CA . THR A 1 431 ? 44.558 -3.229 12.268 1.00 18.58 ? 447 THR A CA 1 ATOM 3545 C C . THR A 1 431 ? 43.891 -2.030 11.574 1.00 18.31 ? 447 THR A C 1 ATOM 3546 O O . THR A 1 431 ? 44.593 -1.096 11.187 1.00 18.05 ? 447 THR A O 1 ATOM 3547 C CB . THR A 1 431 ? 45.145 -4.166 11.179 1.00 18.41 ? 447 THR A CB 1 ATOM 3548 O OG1 . THR A 1 431 ? 44.086 -4.814 10.463 1.00 18.43 ? 447 THR A OG1 1 ATOM 3549 C CG2 . THR A 1 431 ? 46.097 -5.216 11.786 1.00 18.20 ? 447 THR A CG2 1 ATOM 3550 N N . MET A 1 432 ? 42.561 -2.049 11.414 1.00 18.00 ? 448 MET A N 1 ATOM 3551 C CA . MET A 1 432 ? 41.858 -0.931 10.749 1.00 17.63 ? 448 MET A CA 1 ATOM 3552 C C . MET A 1 432 ? 42.092 0.371 11.518 1.00 18.12 ? 448 MET A C 1 ATOM 3553 O O . MET A 1 432 ? 42.330 1.429 10.931 1.00 17.71 ? 448 MET A O 1 ATOM 3554 C CB . MET A 1 432 ? 40.348 -1.185 10.597 1.00 17.49 ? 448 MET A CB 1 ATOM 3555 C CG . MET A 1 432 ? 39.952 -2.396 9.764 1.00 16.88 ? 448 MET A CG 1 ATOM 3556 S SD . MET A 1 432 ? 40.433 -2.203 8.032 1.00 17.58 ? 448 MET A SD 1 ATOM 3557 C CE . MET A 1 432 ? 41.932 -3.187 7.962 1.00 16.43 ? 448 MET A CE 1 ATOM 3558 N N . ASP A 1 433 ? 42.026 0.299 12.843 1.00 17.43 ? 449 ASP A N 1 ATOM 3559 C CA . ASP A 1 433 ? 42.320 1.481 13.635 1.00 18.14 ? 449 ASP A CA 1 ATOM 3560 C C . ASP A 1 433 ? 43.808 1.698 13.970 1.00 17.73 ? 449 ASP A C 1 ATOM 3561 O O . ASP A 1 433 ? 44.230 2.842 14.061 1.00 18.68 ? 449 ASP A O 1 ATOM 3562 C CB . ASP A 1 433 ? 41.427 1.553 14.886 1.00 18.24 ? 449 ASP A CB 1 ATOM 3563 C CG . ASP A 1 433 ? 40.026 2.098 14.574 1.00 19.04 ? 449 ASP A CG 1 ATOM 3564 O OD1 . ASP A 1 433 ? 39.682 2.223 13.372 1.00 19.32 ? 449 ASP A OD1 1 ATOM 3565 O OD2 . ASP A 1 433 ? 39.279 2.449 15.515 1.00 18.91 ? 449 ASP A OD2 1 ATOM 3566 N N . LYS A 1 434 ? 44.604 0.640 14.146 1.00 17.40 ? 450 LYS A N 1 ATOM 3567 C CA . LYS A 1 434 ? 46.056 0.836 14.343 1.00 17.20 ? 450 LYS A CA 1 ATOM 3568 C C . LYS A 1 434 ? 46.603 1.604 13.136 1.00 17.74 ? 450 LYS A C 1 ATOM 3569 O O . LYS A 1 434 ? 47.441 2.505 13.279 1.00 17.91 ? 450 LYS A O 1 ATOM 3570 C CB . LYS A 1 434 ? 46.818 -0.485 14.551 1.00 17.21 ? 450 LYS A CB 1 ATOM 3571 C CG . LYS A 1 434 ? 46.706 -1.089 15.967 1.00 17.28 ? 450 LYS A CG 1 ATOM 3572 C CD . LYS A 1 434 ? 47.470 -2.412 16.072 1.00 17.29 ? 450 LYS A CD 1 ATOM 3573 C CE . LYS A 1 434 ? 47.626 -2.894 17.520 1.00 18.33 ? 450 LYS A CE 1 ATOM 3574 N NZ . LYS A 1 434 ? 48.760 -2.177 18.171 1.00 18.53 ? 450 LYS A NZ 1 ATOM 3575 N N . TYR A 1 435 ? 46.096 1.271 11.950 1.00 17.06 ? 451 TYR A N 1 ATOM 3576 C CA . TYR A 1 435 ? 46.523 1.979 10.744 1.00 17.35 ? 451 TYR A CA 1 ATOM 3577 C C . TYR A 1 435 ? 46.146 3.460 10.761 1.00 17.26 ? 451 TYR A C 1 ATOM 3578 O O . TYR A 1 435 ? 47.013 4.328 10.590 1.00 17.21 ? 451 TYR A O 1 ATOM 3579 C CB . TYR A 1 435 ? 45.944 1.317 9.508 1.00 17.71 ? 451 TYR A CB 1 ATOM 3580 C CG . TYR A 1 435 ? 46.314 2.042 8.229 1.00 18.58 ? 451 TYR A CG 1 ATOM 3581 C CD1 . TYR A 1 435 ? 47.644 2.131 7.811 1.00 19.21 ? 451 TYR A CD1 1 ATOM 3582 C CD2 . TYR A 1 435 ? 45.328 2.642 7.446 1.00 19.12 ? 451 TYR A CD2 1 ATOM 3583 C CE1 . TYR A 1 435 ? 47.980 2.786 6.630 1.00 19.65 ? 451 TYR A CE1 1 ATOM 3584 C CE2 . TYR A 1 435 ? 45.653 3.301 6.271 1.00 19.55 ? 451 TYR A CE2 1 ATOM 3585 C CZ . TYR A 1 435 ? 46.979 3.371 5.874 1.00 19.94 ? 451 TYR A CZ 1 ATOM 3586 O OH . TYR A 1 435 ? 47.293 4.017 4.698 1.00 20.65 ? 451 TYR A OH 1 ATOM 3587 N N . ARG A 1 436 ? 44.859 3.745 10.960 1.00 17.50 ? 452 ARG A N 1 ATOM 3588 C CA . ARG A 1 436 ? 44.383 5.131 10.952 1.00 17.50 ? 452 ARG A CA 1 ATOM 3589 C C . ARG A 1 436 ? 44.965 5.936 12.115 1.00 17.73 ? 452 ARG A C 1 ATOM 3590 O O . ARG A 1 436 ? 45.371 7.086 11.925 1.00 17.43 ? 452 ARG A O 1 ATOM 3591 C CB . ARG A 1 436 ? 42.858 5.209 10.887 1.00 17.32 ? 452 ARG A CB 1 ATOM 3592 C CG . ARG A 1 436 ? 42.319 4.756 9.523 1.00 17.73 ? 452 ARG A CG 1 ATOM 3593 C CD . ARG A 1 436 ? 40.816 4.926 9.401 1.00 17.51 ? 452 ARG A CD 1 ATOM 3594 N NE . ARG A 1 436 ? 40.101 3.972 10.239 1.00 18.26 ? 452 ARG A NE 1 ATOM 3595 C CZ . ARG A 1 436 ? 38.776 3.873 10.322 1.00 18.36 ? 452 ARG A CZ 1 ATOM 3596 N NH1 . ARG A 1 436 ? 37.986 4.676 9.614 1.00 18.19 ? 452 ARG A NH1 1 ATOM 3597 N NH2 . ARG A 1 436 ? 38.244 2.981 11.149 1.00 18.89 ? 452 ARG A NH2 1 ATOM 3598 N N . TRP A 1 437 ? 45.046 5.327 13.302 1.00 18.07 ? 453 TRP A N 1 ATOM 3599 C CA . TRP A 1 437 ? 45.735 5.995 14.409 1.00 18.65 ? 453 TRP A CA 1 ATOM 3600 C C . TRP A 1 437 ? 47.145 6.445 14.043 1.00 18.80 ? 453 TRP A C 1 ATOM 3601 O O . TRP A 1 437 ? 47.540 7.563 14.364 1.00 18.61 ? 453 TRP A O 1 ATOM 3602 C CB . TRP A 1 437 ? 45.861 5.115 15.651 1.00 18.78 ? 453 TRP A CB 1 ATOM 3603 C CG . TRP A 1 437 ? 44.603 4.705 16.323 1.00 19.63 ? 453 TRP A CG 1 ATOM 3604 C CD1 . TRP A 1 437 ? 43.354 5.259 16.200 1.00 19.80 ? 453 TRP A CD1 1 ATOM 3605 C CD2 . TRP A 1 437 ? 44.485 3.652 17.280 1.00 19.46 ? 453 TRP A CD2 1 ATOM 3606 N NE1 . TRP A 1 437 ? 42.463 4.588 17.017 1.00 19.80 ? 453 TRP A NE1 1 ATOM 3607 C CE2 . TRP A 1 437 ? 43.136 3.598 17.684 1.00 19.82 ? 453 TRP A CE2 1 ATOM 3608 C CE3 . TRP A 1 437 ? 45.390 2.721 17.806 1.00 20.08 ? 453 TRP A CE3 1 ATOM 3609 C CZ2 . TRP A 1 437 ? 42.668 2.652 18.608 1.00 19.77 ? 453 TRP A CZ2 1 ATOM 3610 C CZ3 . TRP A 1 437 ? 44.928 1.780 18.717 1.00 19.90 ? 453 TRP A CZ3 1 ATOM 3611 C CH2 . TRP A 1 437 ? 43.576 1.755 19.105 1.00 20.31 ? 453 TRP A CH2 1 ATOM 3612 N N . SER A 1 438 ? 47.910 5.570 13.392 1.00 19.21 ? 454 SER A N 1 ATOM 3613 C CA . SER A 1 438 ? 49.289 5.896 13.041 1.00 19.73 ? 454 SER A CA 1 ATOM 3614 C C . SER A 1 438 ? 49.370 7.064 12.031 1.00 20.47 ? 454 SER A C 1 ATOM 3615 O O . SER A 1 438 ? 50.305 7.872 12.083 1.00 20.61 ? 454 SER A O 1 ATOM 3616 C CB . SER A 1 438 ? 50.045 4.647 12.569 1.00 19.62 ? 454 SER A CB 1 ATOM 3617 O OG . SER A 1 438 ? 49.789 4.350 11.200 1.00 19.66 ? 454 SER A OG 1 ATOM 3618 N N . LEU A 1 439 ? 48.396 7.167 11.129 1.00 20.91 ? 455 LEU A N 1 ATOM 3619 C CA . LEU A 1 439 ? 48.344 8.318 10.206 1.00 21.36 ? 455 LEU A CA 1 ATOM 3620 C C . LEU A 1 439 ? 47.932 9.591 10.944 1.00 21.38 ? 455 LEU A C 1 ATOM 3621 O O . LEU A 1 439 ? 48.567 10.647 10.779 1.00 21.34 ? 455 LEU A O 1 ATOM 3622 C CB . LEU A 1 439 ? 47.391 8.076 9.027 1.00 22.02 ? 455 LEU A CB 1 ATOM 3623 C CG . LEU A 1 439 ? 47.566 6.837 8.147 1.00 22.63 ? 455 LEU A CG 1 ATOM 3624 C CD1 . LEU A 1 439 ? 46.590 6.902 6.983 1.00 23.24 ? 455 LEU A CD1 1 ATOM 3625 C CD2 . LEU A 1 439 ? 48.996 6.681 7.652 1.00 22.56 ? 455 LEU A CD2 1 ATOM 3626 N N . PHE A 1 440 ? 46.885 9.470 11.766 1.00 20.74 ? 456 PHE A N 1 ATOM 3627 C CA . PHE A 1 440 ? 46.361 10.567 12.599 1.00 20.62 ? 456 PHE A CA 1 ATOM 3628 C C . PHE A 1 440 ? 47.450 11.175 13.497 1.00 21.09 ? 456 PHE A C 1 ATOM 3629 O O . PHE A 1 440 ? 47.549 12.401 13.623 1.00 21.21 ? 456 PHE A O 1 ATOM 3630 C CB . PHE A 1 440 ? 45.187 10.076 13.477 1.00 19.27 ? 456 PHE A CB 1 ATOM 3631 C CG . PHE A 1 440 ? 43.889 9.795 12.725 1.00 19.49 ? 456 PHE A CG 1 ATOM 3632 C CD1 . PHE A 1 440 ? 43.681 10.227 11.404 1.00 19.21 ? 456 PHE A CD1 1 ATOM 3633 C CD2 . PHE A 1 440 ? 42.868 9.085 13.346 1.00 19.11 ? 456 PHE A CD2 1 ATOM 3634 C CE1 . PHE A 1 440 ? 42.479 9.963 10.747 1.00 19.48 ? 456 PHE A CE1 1 ATOM 3635 C CE2 . PHE A 1 440 ? 41.660 8.828 12.704 1.00 19.15 ? 456 PHE A CE2 1 ATOM 3636 C CZ . PHE A 1 440 ? 41.468 9.255 11.388 1.00 19.12 ? 456 PHE A CZ 1 ATOM 3637 N N . ARG A 1 441 ? 48.253 10.300 14.113 1.00 21.43 ? 457 ARG A N 1 ATOM 3638 C CA . ARG A 1 441 ? 49.340 10.677 15.016 1.00 21.72 ? 457 ARG A CA 1 ATOM 3639 C C . ARG A 1 441 ? 50.597 11.189 14.291 1.00 21.99 ? 457 ARG A C 1 ATOM 3640 O O . ARG A 1 441 ? 51.556 11.590 14.935 1.00 22.13 ? 457 ARG A O 1 ATOM 3641 C CB . ARG A 1 441 ? 49.705 9.493 15.936 1.00 21.31 ? 457 ARG A CB 1 ATOM 3642 C CG . ARG A 1 441 ? 48.680 9.241 17.039 1.00 21.60 ? 457 ARG A CG 1 ATOM 3643 C CD . ARG A 1 441 ? 48.828 7.876 17.692 1.00 21.58 ? 457 ARG A CD 1 ATOM 3644 N NE . ARG A 1 441 ? 47.941 7.760 18.858 1.00 21.92 ? 457 ARG A NE 1 ATOM 3645 C CZ . ARG A 1 441 ? 47.587 6.618 19.455 1.00 22.19 ? 457 ARG A CZ 1 ATOM 3646 N NH1 . ARG A 1 441 ? 48.013 5.442 19.009 1.00 22.24 ? 457 ARG A NH1 1 ATOM 3647 N NH2 . ARG A 1 441 ? 46.782 6.649 20.510 1.00 22.28 ? 457 ARG A NH2 1 ATOM 3648 N N . GLY A 1 442 ? 50.597 11.175 12.963 1.00 22.02 ? 458 GLY A N 1 ATOM 3649 C CA . GLY A 1 442 ? 51.758 11.631 12.202 1.00 22.67 ? 458 GLY A CA 1 ATOM 3650 C C . GLY A 1 442 ? 52.968 10.712 12.299 1.00 23.39 ? 458 GLY A C 1 ATOM 3651 O O . GLY A 1 442 ? 54.107 11.173 12.221 1.00 23.51 ? 458 GLY A O 1 ATOM 3652 N N . GLU A 1 443 ? 52.723 9.415 12.464 1.00 23.43 ? 459 GLU A N 1 ATOM 3653 C CA . GLU A 1 443 ? 53.792 8.443 12.702 1.00 24.50 ? 459 GLU A CA 1 ATOM 3654 C C . GLU A 1 443 ? 54.319 7.825 11.405 1.00 25.21 ? 459 GLU A C 1 ATOM 3655 O O . GLU A 1 443 ? 55.344 7.150 11.412 1.00 26.00 ? 459 GLU A O 1 ATOM 3656 C CB . GLU A 1 443 ? 53.326 7.346 13.674 1.00 23.85 ? 459 GLU A CB 1 ATOM 3657 C CG . GLU A 1 443 ? 53.138 7.847 15.106 1.00 24.64 ? 459 GLU A CG 1 ATOM 3658 C CD . GLU A 1 443 ? 52.375 6.894 16.011 1.00 25.28 ? 459 GLU A CD 1 ATOM 3659 O OE1 . GLU A 1 443 ? 51.814 5.880 15.524 1.00 25.41 ? 459 GLU A OE1 1 ATOM 3660 O OE2 . GLU A 1 443 ? 52.333 7.162 17.239 1.00 25.01 ? 459 GLU A OE2 1 ATOM 3661 N N . VAL A 1 444 ? 53.622 8.059 10.298 1.00 26.08 ? 460 VAL A N 1 ATOM 3662 C CA . VAL A 1 444 ? 54.027 7.508 9.014 1.00 26.63 ? 460 VAL A CA 1 ATOM 3663 C C . VAL A 1 444 ? 54.149 8.644 7.998 1.00 29.19 ? 460 VAL A C 1 ATOM 3664 O O . VAL A 1 444 ? 53.223 9.441 7.855 1.00 29.94 ? 460 VAL A O 1 ATOM 3665 C CB . VAL A 1 444 ? 53.003 6.470 8.482 1.00 26.41 ? 460 VAL A CB 1 ATOM 3666 C CG1 . VAL A 1 444 ? 53.518 5.803 7.206 1.00 25.01 ? 460 VAL A CG1 1 ATOM 3667 C CG2 . VAL A 1 444 ? 52.655 5.418 9.529 1.00 25.03 ? 460 VAL A CG2 1 ATOM 3668 N N . ASP A 1 445 ? 55.276 8.712 7.292 1.00 31.29 ? 461 ASP A N 1 ATOM 3669 C CA . ASP A 1 445 ? 55.448 9.681 6.200 1.00 34.84 ? 461 ASP A CA 1 ATOM 3670 C C . ASP A 1 445 ? 54.536 9.324 5.039 1.00 33.48 ? 461 ASP A C 1 ATOM 3671 O O . ASP A 1 445 ? 54.333 8.135 4.761 1.00 30.63 ? 461 ASP A O 1 ATOM 3672 C CB . ASP A 1 445 ? 56.896 9.687 5.702 1.00 38.92 ? 461 ASP A CB 1 ATOM 3673 C CG . ASP A 1 445 ? 57.876 10.163 6.761 1.00 43.20 ? 461 ASP A CG 1 ATOM 3674 O OD1 . ASP A 1 445 ? 57.565 11.155 7.465 1.00 44.65 ? 461 ASP A OD1 1 ATOM 3675 O OD2 . ASP A 1 445 ? 58.963 9.549 6.882 1.00 46.31 ? 461 ASP A OD2 1 ATOM 3676 N N . LYS A 1 446 ? 54.011 10.354 4.367 1.00 32.62 ? 462 LYS A N 1 ATOM 3677 C CA . LYS A 1 446 ? 53.057 10.195 3.266 1.00 33.52 ? 462 LYS A CA 1 ATOM 3678 C C . LYS A 1 446 ? 53.588 9.304 2.146 1.00 32.24 ? 462 LYS A C 1 ATOM 3679 O O . LYS A 1 446 ? 52.813 8.624 1.471 1.00 32.39 ? 462 LYS A O 1 ATOM 3680 C CB . LYS A 1 446 ? 52.632 11.562 2.693 1.00 35.94 ? 462 LYS A CB 1 ATOM 3681 C CG . LYS A 1 446 ? 51.356 12.125 3.309 1.00 38.14 ? 462 LYS A CG 1 ATOM 3682 C CD . LYS A 1 446 ? 50.932 13.457 2.698 1.00 41.14 ? 462 LYS A CD 1 ATOM 3683 C CE . LYS A 1 446 ? 51.813 14.598 3.189 1.00 43.81 ? 462 LYS A CE 1 ATOM 3684 N NZ . LYS A 1 446 ? 51.231 15.932 2.870 1.00 47.63 ? 462 LYS A NZ 1 ATOM 3685 N N . ALA A 1 447 ? 54.905 9.316 1.956 1.00 30.83 ? 463 ALA A N 1 ATOM 3686 C CA . ALA A 1 447 ? 55.559 8.448 0.975 1.00 29.49 ? 463 ALA A CA 1 ATOM 3687 C C . ALA A 1 447 ? 55.408 6.963 1.326 1.00 28.17 ? 463 ALA A C 1 ATOM 3688 O O . ALA A 1 447 ? 55.568 6.113 0.463 1.00 27.17 ? 463 ALA A O 1 ATOM 3689 C CB . ALA A 1 447 ? 57.034 8.811 0.839 1.00 30.05 ? 463 ALA A CB 1 ATOM 3690 N N . ASN A 1 448 ? 55.095 6.655 2.587 1.00 25.35 ? 464 ASN A N 1 ATOM 3691 C CA . ASN A 1 448 ? 55.014 5.263 3.046 1.00 24.50 ? 464 ASN A CA 1 ATOM 3692 C C . ASN A 1 448 ? 53.609 4.773 3.433 1.00 23.40 ? 464 ASN A C 1 ATOM 3693 O O . ASN A 1 448 ? 53.475 3.689 3.996 1.00 22.36 ? 464 ASN A O 1 ATOM 3694 C CB . ASN A 1 448 ? 55.959 5.035 4.242 1.00 25.23 ? 464 ASN A CB 1 ATOM 3695 C CG . ASN A 1 448 ? 57.407 5.381 3.924 1.00 27.18 ? 464 ASN A CG 1 ATOM 3696 O OD1 . ASN A 1 448 ? 58.098 5.986 4.738 1.00 28.84 ? 464 ASN A OD1 1 ATOM 3697 N ND2 . ASN A 1 448 ? 57.865 5.011 2.732 1.00 26.54 ? 464 ASN A ND2 1 ATOM 3698 N N . TRP A 1 449 ? 52.575 5.561 3.141 1.00 22.51 ? 465 TRP A N 1 ATOM 3699 C CA . TRP A 1 449 ? 51.217 5.266 3.615 1.00 22.13 ? 465 TRP A CA 1 ATOM 3700 C C . TRP A 1 449 ? 50.623 3.940 3.127 1.00 21.57 ? 465 TRP A C 1 ATOM 3701 O O . TRP A 1 449 ? 49.944 3.262 3.872 1.00 20.52 ? 465 TRP A O 1 ATOM 3702 C CB . TRP A 1 449 ? 50.275 6.414 3.264 1.00 23.21 ? 465 TRP A CB 1 ATOM 3703 C CG . TRP A 1 449 ? 50.306 7.556 4.229 1.00 23.78 ? 465 TRP A CG 1 ATOM 3704 C CD1 . TRP A 1 449 ? 51.285 7.840 5.150 1.00 23.61 ? 465 TRP A CD1 1 ATOM 3705 C CD2 . TRP A 1 449 ? 49.324 8.593 4.351 1.00 23.96 ? 465 TRP A CD2 1 ATOM 3706 N NE1 . TRP A 1 449 ? 50.961 8.988 5.841 1.00 24.32 ? 465 TRP A NE1 1 ATOM 3707 C CE2 . TRP A 1 449 ? 49.765 9.470 5.376 1.00 24.39 ? 465 TRP A CE2 1 ATOM 3708 C CE3 . TRP A 1 449 ? 48.112 8.867 3.697 1.00 24.43 ? 465 TRP A CE3 1 ATOM 3709 C CZ2 . TRP A 1 449 ? 49.029 10.599 5.770 1.00 24.50 ? 465 TRP A CZ2 1 ATOM 3710 C CZ3 . TRP A 1 449 ? 47.381 9.994 4.082 1.00 24.94 ? 465 TRP A CZ3 1 ATOM 3711 C CH2 . TRP A 1 449 ? 47.842 10.841 5.117 1.00 24.54 ? 465 TRP A CH2 1 ATOM 3712 N N . ASN A 1 450 ? 50.865 3.550 1.880 1.00 20.65 ? 466 ASN A N 1 ATOM 3713 C CA . ASN A 1 450 ? 50.262 2.292 1.435 1.00 20.74 ? 466 ASN A CA 1 ATOM 3714 C C . ASN A 1 450 ? 50.937 1.064 1.996 1.00 20.18 ? 466 ASN A C 1 ATOM 3715 O O . ASN A 1 450 ? 50.274 0.100 2.347 1.00 20.16 ? 466 ASN A O 1 ATOM 3716 C CB . ASN A 1 450 ? 50.182 2.151 -0.090 1.00 20.45 ? 466 ASN A CB 1 ATOM 3717 C CG . ASN A 1 450 ? 49.085 1.165 -0.514 1.00 20.92 ? 466 ASN A CG 1 ATOM 3718 O OD1 . ASN A 1 450 ? 47.993 1.158 0.063 1.00 20.31 ? 466 ASN A OD1 1 ATOM 3719 N ND2 . ASN A 1 450 ? 49.375 0.323 -1.522 1.00 20.53 ? 466 ASN A ND2 1 ATOM 3720 N N . CYS A 1 451 ? 52.258 1.068 2.050 1.00 20.57 ? 467 CYS A N 1 ATOM 3721 C CA . CYS A 1 451 ? 52.914 -0.136 2.457 1.00 20.81 ? 467 CYS A CA 1 ATOM 3722 C C . CYS A 1 451 ? 52.797 -0.256 3.973 1.00 19.83 ? 467 CYS A C 1 ATOM 3723 O O . CYS A 1 451 ? 52.870 -1.350 4.473 1.00 19.50 ? 467 CYS A O 1 ATOM 3724 C CB . CYS A 1 451 ? 54.344 -0.250 1.941 1.00 22.99 ? 467 CYS A CB 1 ATOM 3725 S SG . CYS A 1 451 ? 54.408 -0.659 0.154 1.00 27.47 ? 467 CYS A SG 1 ATOM 3726 N N . ALA A 1 452 ? 52.526 0.857 4.666 1.00 19.30 ? 468 ALA A N 1 ATOM 3727 C CA . ALA A 1 452 ? 52.241 0.806 6.122 1.00 18.85 ? 468 ALA A CA 1 ATOM 3728 C C . ALA A 1 452 ? 50.938 0.041 6.453 1.00 18.31 ? 468 ALA A C 1 ATOM 3729 O O . ALA A 1 452 ? 50.832 -0.613 7.506 1.00 18.12 ? 468 ALA A O 1 ATOM 3730 C CB . ALA A 1 452 ? 52.200 2.209 6.708 1.00 18.83 ? 468 ALA A CB 1 ATOM 3731 N N . PHE A 1 453 ? 49.951 0.147 5.564 1.00 18.20 ? 469 PHE A N 1 ATOM 3732 C CA . PHE A 1 453 ? 48.691 -0.601 5.646 1.00 17.86 ? 469 PHE A CA 1 ATOM 3733 C C . PHE A 1 453 ? 48.969 -2.100 5.518 1.00 17.82 ? 469 PHE A C 1 ATOM 3734 O O . PHE A 1 453 ? 48.612 -2.891 6.388 1.00 17.01 ? 469 PHE A O 1 ATOM 3735 C CB . PHE A 1 453 ? 47.706 -0.147 4.519 1.00 17.78 ? 469 PHE A CB 1 ATOM 3736 C CG . PHE A 1 453 ? 46.367 -0.862 4.551 1.00 18.03 ? 469 PHE A CG 1 ATOM 3737 C CD1 . PHE A 1 453 ? 45.429 -0.585 5.550 1.00 17.52 ? 469 PHE A CD1 1 ATOM 3738 C CD2 . PHE A 1 453 ? 46.041 -1.817 3.591 1.00 17.80 ? 469 PHE A CD2 1 ATOM 3739 C CE1 . PHE A 1 453 ? 44.203 -1.246 5.585 1.00 17.91 ? 469 PHE A CE1 1 ATOM 3740 C CE2 . PHE A 1 453 ? 44.810 -2.474 3.617 1.00 17.99 ? 469 PHE A CE2 1 ATOM 3741 C CZ . PHE A 1 453 ? 43.889 -2.198 4.618 1.00 18.06 ? 469 PHE A CZ 1 ATOM 3742 N N . TRP A 1 454 ? 49.585 -2.492 4.407 1.00 17.93 ? 470 TRP A N 1 ATOM 3743 C CA . TRP A 1 454 ? 49.864 -3.908 4.155 1.00 18.34 ? 470 TRP A CA 1 ATOM 3744 C C . TRP A 1 454 ? 50.826 -4.543 5.170 1.00 18.88 ? 470 TRP A C 1 ATOM 3745 O O . TRP A 1 454 ? 50.667 -5.733 5.492 1.00 18.26 ? 470 TRP A O 1 ATOM 3746 C CB . TRP A 1 454 ? 50.288 -4.132 2.689 1.00 18.27 ? 470 TRP A CB 1 ATOM 3747 C CG . TRP A 1 454 ? 49.145 -3.859 1.737 1.00 18.36 ? 470 TRP A CG 1 ATOM 3748 C CD1 . TRP A 1 454 ? 49.119 -2.936 0.700 1.00 18.19 ? 470 TRP A CD1 1 ATOM 3749 C CD2 . TRP A 1 454 ? 47.856 -4.502 1.720 1.00 18.30 ? 470 TRP A CD2 1 ATOM 3750 N NE1 . TRP A 1 454 ? 47.902 -2.969 0.072 1.00 18.13 ? 470 TRP A NE1 1 ATOM 3751 C CE2 . TRP A 1 454 ? 47.118 -3.934 0.645 1.00 18.23 ? 470 TRP A CE2 1 ATOM 3752 C CE3 . TRP A 1 454 ? 47.272 -5.532 2.467 1.00 18.16 ? 470 TRP A CE3 1 ATOM 3753 C CZ2 . TRP A 1 454 ? 45.805 -4.319 0.345 1.00 18.23 ? 470 TRP A CZ2 1 ATOM 3754 C CZ3 . TRP A 1 454 ? 45.958 -5.920 2.172 1.00 18.20 ? 470 TRP A CZ3 1 ATOM 3755 C CH2 . TRP A 1 454 ? 45.246 -5.320 1.096 1.00 18.44 ? 470 TRP A CH2 1 ATOM 3756 N N . LYS A 1 455 ? 51.762 -3.745 5.713 1.00 19.41 ? 471 LYS A N 1 ATOM 3757 C CA . LYS A 1 455 ? 52.658 -4.226 6.774 1.00 20.21 ? 471 LYS A CA 1 ATOM 3758 C C . LYS A 1 455 ? 51.881 -4.658 8.018 1.00 19.29 ? 471 LYS A C 1 ATOM 3759 O O . LYS A 1 455 ? 52.192 -5.695 8.607 1.00 18.67 ? 471 LYS A O 1 ATOM 3760 C CB . LYS A 1 455 ? 53.708 -3.178 7.166 1.00 22.24 ? 471 LYS A CB 1 ATOM 3761 C CG . LYS A 1 455 ? 54.864 -3.034 6.193 1.00 25.45 ? 471 LYS A CG 1 ATOM 3762 C CD . LYS A 1 455 ? 55.712 -1.806 6.529 1.00 28.28 ? 471 LYS A CD 1 ATOM 3763 C CE . LYS A 1 455 ? 56.622 -1.421 5.368 1.00 32.16 ? 471 LYS A CE 1 ATOM 3764 N NZ . LYS A 1 455 ? 57.745 -2.387 5.208 1.00 34.45 ? 471 LYS A NZ 1 ATOM 3765 N N . LEU A 1 456 ? 50.893 -3.857 8.426 1.00 18.87 ? 472 LEU A N 1 ATOM 3766 C CA . LEU A 1 456 ? 50.015 -4.227 9.554 1.00 18.24 ? 472 LEU A CA 1 ATOM 3767 C C . LEU A 1 456 ? 49.173 -5.456 9.213 1.00 17.77 ? 472 LEU A C 1 ATOM 3768 O O . LEU A 1 456 ? 49.075 -6.375 9.981 1.00 16.82 ? 472 LEU A O 1 ATOM 3769 C CB . LEU A 1 456 ? 49.092 -3.066 9.920 1.00 18.77 ? 472 LEU A CB 1 ATOM 3770 C CG . LEU A 1 456 ? 49.759 -1.842 10.531 1.00 19.22 ? 472 LEU A CG 1 ATOM 3771 C CD1 . LEU A 1 456 ? 48.792 -0.670 10.488 1.00 19.25 ? 472 LEU A CD1 1 ATOM 3772 C CD2 . LEU A 1 456 ? 50.177 -2.164 11.962 1.00 19.22 ? 472 LEU A CD2 1 ATOM 3773 N N . ARG A 1 457 ? 48.602 -5.510 8.011 1.00 16.96 ? 473 ARG A N 1 ATOM 3774 C CA . ARG A 1 457 ? 47.794 -6.677 7.645 1.00 17.12 ? 473 ARG A CA 1 ATOM 3775 C C . ARG A 1 457 ? 48.626 -7.980 7.720 1.00 17.23 ? 473 ARG A C 1 ATOM 3776 O O . ARG A 1 457 ? 48.125 -9.042 8.126 1.00 17.43 ? 473 ARG A O 1 ATOM 3777 C CB . ARG A 1 457 ? 47.194 -6.473 6.235 1.00 17.08 ? 473 ARG A CB 1 ATOM 3778 C CG . ARG A 1 457 ? 46.318 -5.214 6.102 1.00 17.83 ? 473 ARG A CG 1 ATOM 3779 C CD . ARG A 1 457 ? 45.100 -5.190 7.042 1.00 17.96 ? 473 ARG A CD 1 ATOM 3780 N NE . ARG A 1 457 ? 44.229 -6.316 6.723 1.00 18.49 ? 473 ARG A NE 1 ATOM 3781 C CZ . ARG A 1 457 ? 43.985 -7.357 7.506 1.00 19.32 ? 473 ARG A CZ 1 ATOM 3782 N NH1 . ARG A 1 457 ? 44.463 -7.405 8.755 1.00 18.36 ? 473 ARG A NH1 1 ATOM 3783 N NH2 . ARG A 1 457 ? 43.220 -8.345 7.044 1.00 19.43 ? 473 ARG A NH2 1 ATOM 3784 N N . ASP A 1 458 ? 49.899 -7.868 7.359 1.00 17.61 ? 474 ASP A N 1 ATOM 3785 C CA . ASP A 1 458 ? 50.857 -8.989 7.348 1.00 18.80 ? 474 ASP A CA 1 ATOM 3786 C C . ASP A 1 458 ? 51.153 -9.358 8.800 1.00 19.52 ? 474 ASP A C 1 ATOM 3787 O O . ASP A 1 458 ? 50.868 -10.476 9.244 1.00 19.09 ? 474 ASP A O 1 ATOM 3788 C CB . ASP A 1 458 ? 52.136 -8.548 6.597 1.00 20.21 ? 474 ASP A CB 1 ATOM 3789 C CG . ASP A 1 458 ? 53.318 -9.545 6.718 1.00 21.33 ? 474 ASP A CG 1 ATOM 3790 O OD1 . ASP A 1 458 ? 53.248 -10.548 7.451 1.00 22.78 ? 474 ASP A OD1 1 ATOM 3791 O OD2 . ASP A 1 458 ? 54.348 -9.304 6.060 1.00 22.18 ? 474 ASP A OD2 1 ATOM 3792 N N . GLU A 1 459 ? 51.685 -8.387 9.531 1.00 20.40 ? 475 GLU A N 1 ATOM 3793 C CA . GLU A 1 459 ? 52.117 -8.592 10.917 1.00 21.36 ? 475 GLU A CA 1 ATOM 3794 C C . GLU A 1 459 ? 51.018 -9.189 11.812 1.00 21.00 ? 475 GLU A C 1 ATOM 3795 O O . GLU A 1 459 ? 51.299 -10.087 12.642 1.00 21.19 ? 475 GLU A O 1 ATOM 3796 C CB . GLU A 1 459 ? 52.636 -7.264 11.482 1.00 24.40 ? 475 GLU A CB 1 ATOM 3797 C CG . GLU A 1 459 ? 52.965 -7.277 12.975 1.00 30.25 ? 475 GLU A CG 1 ATOM 3798 C CD . GLU A 1 459 ? 53.374 -5.905 13.525 1.00 35.14 ? 475 GLU A CD 1 ATOM 3799 O OE1 . GLU A 1 459 ? 53.493 -4.922 12.744 1.00 37.63 ? 475 GLU A OE1 1 ATOM 3800 O OE2 . GLU A 1 459 ? 53.573 -5.804 14.758 1.00 38.44 ? 475 GLU A OE2 1 ATOM 3801 N N . TYR A 1 460 ? 49.790 -8.684 11.697 1.00 19.35 ? 476 TYR A N 1 ATOM 3802 C CA . TYR A 1 460 ? 48.720 -9.144 12.597 1.00 19.59 ? 476 TYR A CA 1 ATOM 3803 C C . TYR A 1 460 ? 47.894 -10.309 12.059 1.00 19.27 ? 476 TYR A C 1 ATOM 3804 O O . TYR A 1 460 ? 47.601 -11.236 12.799 1.00 19.29 ? 476 TYR A O 1 ATOM 3805 C CB . TYR A 1 460 ? 47.818 -7.976 13.067 1.00 19.58 ? 476 TYR A CB 1 ATOM 3806 C CG . TYR A 1 460 ? 48.496 -7.061 14.072 1.00 19.21 ? 476 TYR A CG 1 ATOM 3807 C CD1 . TYR A 1 460 ? 49.332 -6.030 13.652 1.00 19.18 ? 476 TYR A CD1 1 ATOM 3808 C CD2 . TYR A 1 460 ? 48.328 -7.247 15.456 1.00 19.91 ? 476 TYR A CD2 1 ATOM 3809 C CE1 . TYR A 1 460 ? 49.977 -5.198 14.541 1.00 19.68 ? 476 TYR A CE1 1 ATOM 3810 C CE2 . TYR A 1 460 ? 48.978 -6.417 16.359 1.00 20.53 ? 476 TYR A CE2 1 ATOM 3811 C CZ . TYR A 1 460 ? 49.795 -5.397 15.898 1.00 20.43 ? 476 TYR A CZ 1 ATOM 3812 O OH . TYR A 1 460 ? 50.455 -4.561 16.763 1.00 20.38 ? 476 TYR A OH 1 ATOM 3813 N N . SER A 1 461 ? 47.548 -10.284 10.767 1.00 19.09 ? 477 SER A N 1 ATOM 3814 C CA . SER A 1 461 ? 46.633 -11.288 10.199 1.00 19.12 ? 477 SER A CA 1 ATOM 3815 C C . SER A 1 461 ? 47.328 -12.352 9.325 1.00 18.82 ? 477 SER A C 1 ATOM 3816 O O . SER A 1 461 ? 46.741 -13.396 9.055 1.00 18.91 ? 477 SER A O 1 ATOM 3817 C CB . SER A 1 461 ? 45.518 -10.614 9.378 1.00 19.48 ? 477 SER A CB 1 ATOM 3818 O OG . SER A 1 461 ? 44.584 -9.936 10.205 1.00 20.35 ? 477 SER A OG 1 ATOM 3819 N N . GLY A 1 462 ? 48.557 -12.096 8.870 1.00 18.56 ? 478 GLY A N 1 ATOM 3820 C CA . GLY A 1 462 ? 49.279 -13.113 8.092 1.00 18.31 ? 478 GLY A CA 1 ATOM 3821 C C . GLY A 1 462 ? 48.637 -13.319 6.737 1.00 18.15 ? 478 GLY A C 1 ATOM 3822 O O . GLY A 1 462 ? 48.598 -14.431 6.196 1.00 17.97 ? 478 GLY A O 1 ATOM 3823 N N . ILE A 1 463 ? 48.103 -12.229 6.200 1.00 18.15 ? 479 ILE A N 1 ATOM 3824 C CA . ILE A 1 463 ? 47.519 -12.250 4.854 1.00 17.81 ? 479 ILE A CA 1 ATOM 3825 C C . ILE A 1 463 ? 48.228 -11.213 3.990 1.00 17.96 ? 479 ILE A C 1 ATOM 3826 O O . ILE A 1 463 ? 48.906 -10.347 4.513 1.00 17.80 ? 479 ILE A O 1 ATOM 3827 C CB . ILE A 1 463 ? 45.978 -12.035 4.886 1.00 18.10 ? 479 ILE A CB 1 ATOM 3828 C CG1 . ILE A 1 463 ? 45.587 -10.643 5.421 1.00 17.89 ? 479 ILE A CG1 1 ATOM 3829 C CG2 . ILE A 1 463 ? 45.281 -13.131 5.705 1.00 17.70 ? 479 ILE A CG2 1 ATOM 3830 C CD1 . ILE A 1 463 ? 45.631 -9.525 4.403 1.00 17.80 ? 479 ILE A CD1 1 ATOM 3831 N N . GLU A 1 464 ? 48.065 -11.286 2.663 1.00 18.18 ? 480 GLU A N 1 ATOM 3832 C CA . GLU A 1 464 ? 48.704 -10.336 1.777 1.00 18.67 ? 480 GLU A CA 1 ATOM 3833 C C . GLU A 1 464 ? 47.882 -10.215 0.485 1.00 18.85 ? 480 GLU A C 1 ATOM 3834 O O . GLU A 1 464 ? 47.077 -11.092 0.195 1.00 19.06 ? 480 GLU A O 1 ATOM 3835 C CB . GLU A 1 464 ? 50.129 -10.803 1.422 1.00 19.25 ? 480 GLU A CB 1 ATOM 3836 C CG . GLU A 1 464 ? 50.161 -12.082 0.590 1.00 20.22 ? 480 GLU A CG 1 ATOM 3837 C CD . GLU A 1 464 ? 51.568 -12.551 0.261 1.00 21.16 ? 480 GLU A CD 1 ATOM 3838 O OE1 . GLU A 1 464 ? 52.533 -12.146 0.950 1.00 21.41 ? 480 GLU A OE1 1 ATOM 3839 O OE2 . GLU A 1 464 ? 51.704 -13.343 -0.687 1.00 21.74 ? 480 GLU A OE2 1 ATOM 3840 N N . PRO A 1 465 ? 48.078 -9.122 -0.274 1.00 19.13 ? 481 PRO A N 1 ATOM 3841 C CA . PRO A 1 465 ? 47.410 -8.972 -1.581 1.00 19.45 ? 481 PRO A CA 1 ATOM 3842 C C . PRO A 1 465 ? 47.772 -10.092 -2.555 1.00 20.26 ? 481 PRO A C 1 ATOM 3843 O O . PRO A 1 465 ? 48.849 -10.701 -2.422 1.00 20.69 ? 481 PRO A O 1 ATOM 3844 C CB . PRO A 1 465 ? 47.954 -7.632 -2.096 1.00 19.48 ? 481 PRO A CB 1 ATOM 3845 C CG . PRO A 1 465 ? 48.344 -6.891 -0.848 1.00 19.50 ? 481 PRO A CG 1 ATOM 3846 C CD . PRO A 1 465 ? 48.924 -7.953 0.027 1.00 18.95 ? 481 PRO A CD 1 ATOM 3847 N N . PRO A 1 466 ? 46.882 -10.358 -3.540 1.00 20.34 ? 482 PRO A N 1 ATOM 3848 C CA . PRO A 1 466 ? 47.058 -11.375 -4.580 1.00 20.97 ? 482 PRO A CA 1 ATOM 3849 C C . PRO A 1 466 ? 48.112 -10.993 -5.623 1.00 22.19 ? 482 PRO A C 1 ATOM 3850 O O . PRO A 1 466 ? 48.697 -11.872 -6.248 1.00 22.62 ? 482 PRO A O 1 ATOM 3851 C CB . PRO A 1 466 ? 45.678 -11.447 -5.237 1.00 20.60 ? 482 PRO A CB 1 ATOM 3852 C CG . PRO A 1 466 ? 45.081 -10.094 -5.012 1.00 20.27 ? 482 PRO A CG 1 ATOM 3853 C CD . PRO A 1 466 ? 45.532 -9.766 -3.593 1.00 20.06 ? 482 PRO A CD 1 ATOM 3854 N N . VAL A 1 467 ? 48.348 -9.688 -5.776 1.00 22.67 ? 483 VAL A N 1 ATOM 3855 C CA . VAL A 1 467 ? 49.295 -9.124 -6.735 1.00 23.06 ? 483 VAL A CA 1 ATOM 3856 C C . VAL A 1 467 ? 50.209 -8.139 -6.001 1.00 22.96 ? 483 VAL A C 1 ATOM 3857 O O . VAL A 1 467 ? 49.869 -7.667 -4.898 1.00 22.25 ? 483 VAL A O 1 ATOM 3858 C CB . VAL A 1 467 ? 48.554 -8.381 -7.882 1.00 23.57 ? 483 VAL A CB 1 ATOM 3859 C CG1 . VAL A 1 467 ? 47.723 -9.353 -8.715 1.00 24.28 ? 483 VAL A CG1 1 ATOM 3860 C CG2 . VAL A 1 467 ? 47.657 -7.272 -7.331 1.00 23.25 ? 483 VAL A CG2 1 ATOM 3861 N N . VAL A 1 468 ? 51.364 -7.844 -6.594 1.00 22.64 ? 484 VAL A N 1 ATOM 3862 C CA . VAL A 1 468 ? 52.304 -6.879 -6.025 1.00 22.36 ? 484 VAL A CA 1 ATOM 3863 C C . VAL A 1 468 ? 51.704 -5.470 -6.070 1.00 22.28 ? 484 VAL A C 1 ATOM 3864 O O . VAL A 1 468 ? 51.292 -5.008 -7.130 1.00 22.64 ? 484 VAL A O 1 ATOM 3865 C CB . VAL A 1 468 ? 53.673 -6.896 -6.744 1.00 22.80 ? 484 VAL A CB 1 ATOM 3866 C CG1 . VAL A 1 468 ? 54.620 -5.866 -6.130 1.00 22.59 ? 484 VAL A CG1 1 ATOM 3867 C CG2 . VAL A 1 468 ? 54.304 -8.287 -6.691 1.00 22.73 ? 484 VAL A CG2 1 ATOM 3868 N N . ARG A 1 469 ? 51.637 -4.823 -4.903 1.00 21.07 ? 485 ARG A N 1 ATOM 3869 C CA . ARG A 1 469 ? 51.208 -3.426 -4.752 1.00 20.83 ? 485 ARG A CA 1 ATOM 3870 C C . ARG A 1 469 ? 52.439 -2.562 -4.441 1.00 20.40 ? 485 ARG A C 1 ATOM 3871 O O . ARG A 1 469 ? 53.522 -3.082 -4.172 1.00 20.40 ? 485 ARG A O 1 ATOM 3872 C CB . ARG A 1 469 ? 50.160 -3.268 -3.614 1.00 20.12 ? 485 ARG A CB 1 ATOM 3873 C CG . ARG A 1 469 ? 48.946 -4.199 -3.693 1.00 20.05 ? 485 ARG A CG 1 ATOM 3874 C CD . ARG A 1 469 ? 48.148 -4.010 -4.997 1.00 20.88 ? 485 ARG A CD 1 ATOM 3875 N NE . ARG A 1 469 ? 47.126 -2.957 -4.910 1.00 21.35 ? 485 ARG A NE 1 ATOM 3876 C CZ . ARG A 1 469 ? 46.366 -2.578 -5.940 1.00 22.39 ? 485 ARG A CZ 1 ATOM 3877 N NH1 . ARG A 1 469 ? 46.532 -3.150 -7.124 1.00 22.44 ? 485 ARG A NH1 1 ATOM 3878 N NH2 . ARG A 1 469 ? 45.438 -1.635 -5.795 1.00 22.95 ? 485 ARG A NH2 1 ATOM 3879 N N . SER A 1 470 ? 52.269 -1.244 -4.475 1.00 20.60 ? 486 SER A N 1 ATOM 3880 C CA . SER A 1 470 ? 53.361 -0.313 -4.214 1.00 21.03 ? 486 SER A CA 1 ATOM 3881 C C . SER A 1 470 ? 52.737 1.003 -3.810 1.00 21.35 ? 486 SER A C 1 ATOM 3882 O O . SER A 1 470 ? 51.512 1.126 -3.747 1.00 21.25 ? 486 SER A O 1 ATOM 3883 C CB . SER A 1 470 ? 54.170 -0.069 -5.502 1.00 21.93 ? 486 SER A CB 1 ATOM 3884 O OG . SER A 1 470 ? 53.432 0.835 -6.291 1.00 22.61 ? 486 SER A OG 1 ATOM 3885 N N . GLU A 1 471 ? 53.577 2.009 -3.597 1.00 22.78 ? 487 GLU A N 1 ATOM 3886 C CA . GLU A 1 471 ? 53.101 3.324 -3.175 1.00 24.37 ? 487 GLU A CA 1 ATOM 3887 C C . GLU A 1 471 ? 52.355 4.074 -4.280 1.00 25.54 ? 487 GLU A C 1 ATOM 3888 O O . GLU A 1 471 ? 51.833 5.162 -4.043 1.00 26.04 ? 487 GLU A O 1 ATOM 3889 C CB . GLU A 1 471 ? 54.247 4.160 -2.604 1.00 24.76 ? 487 GLU A CB 1 ATOM 3890 C CG . GLU A 1 471 ? 54.821 3.595 -1.309 1.00 25.71 ? 487 GLU A CG 1 ATOM 3891 C CD . GLU A 1 471 ? 53.824 3.548 -0.153 1.00 25.94 ? 487 GLU A CD 1 ATOM 3892 O OE1 . GLU A 1 471 ? 52.751 4.198 -0.230 1.00 26.11 ? 487 GLU A OE1 1 ATOM 3893 O OE2 . GLU A 1 471 ? 54.129 2.868 0.860 1.00 26.01 ? 487 GLU A OE2 1 ATOM 3894 N N . LYS A 1 472 ? 52.292 3.486 -5.475 1.00 26.92 ? 488 LYS A N 1 ATOM 3895 C CA . LYS A 1 472 ? 51.417 3.998 -6.522 1.00 28.32 ? 488 LYS A CA 1 ATOM 3896 C C . LYS A 1 472 ? 49.951 3.602 -6.320 1.00 27.23 ? 488 LYS A C 1 ATOM 3897 O O . LYS A 1 472 ? 49.054 4.169 -6.955 1.00 27.44 ? 488 LYS A O 1 ATOM 3898 C CB . LYS A 1 472 ? 51.900 3.563 -7.915 1.00 30.78 ? 488 LYS A CB 1 ATOM 3899 C CG . LYS A 1 472 ? 53.254 4.156 -8.289 1.00 34.64 ? 488 LYS A CG 1 ATOM 3900 C CD . LYS A 1 472 ? 53.769 3.574 -9.601 1.00 37.94 ? 488 LYS A CD 1 ATOM 3901 C CE . LYS A 1 472 ? 55.238 3.922 -9.804 1.00 41.49 ? 488 LYS A CE 1 ATOM 3902 N NZ . LYS A 1 472 ? 55.844 3.187 -10.957 1.00 44.15 ? 488 LYS A NZ 1 ATOM 3903 N N . ASP A 1 473 ? 49.704 2.619 -5.456 1.00 25.78 ? 489 ASP A N 1 ATOM 3904 C CA . ASP A 1 473 ? 48.333 2.253 -5.110 1.00 24.44 ? 489 ASP A CA 1 ATOM 3905 C C . ASP A 1 473 ? 47.981 2.844 -3.755 1.00 23.40 ? 489 ASP A C 1 ATOM 3906 O O . ASP A 1 473 ? 48.875 3.252 -3.004 1.00 22.86 ? 489 ASP A O 1 ATOM 3907 C CB . ASP A 1 473 ? 48.176 0.734 -5.077 1.00 24.84 ? 489 ASP A CB 1 ATOM 3908 C CG . ASP A 1 473 ? 48.806 0.066 -6.274 1.00 25.54 ? 489 ASP A CG 1 ATOM 3909 O OD1 . ASP A 1 473 ? 48.324 0.283 -7.410 1.00 25.58 ? 489 ASP A OD1 1 ATOM 3910 O OD2 . ASP A 1 473 ? 49.792 -0.664 -6.076 1.00 25.44 ? 489 ASP A OD2 1 ATOM 3911 N N . PHE A 1 474 ? 46.687 2.914 -3.453 1.00 22.12 ? 490 PHE A N 1 ATOM 3912 C CA . PHE A 1 474 ? 46.252 3.310 -2.111 1.00 21.14 ? 490 PHE A CA 1 ATOM 3913 C C . PHE A 1 474 ? 45.033 2.491 -1.703 1.00 20.47 ? 490 PHE A C 1 ATOM 3914 O O . PHE A 1 474 ? 43.905 2.806 -2.073 1.00 19.82 ? 490 PHE A O 1 ATOM 3915 C CB . PHE A 1 474 ? 45.983 4.820 -2.016 1.00 21.36 ? 490 PHE A CB 1 ATOM 3916 C CG . PHE A 1 474 ? 45.844 5.308 -0.596 1.00 21.47 ? 490 PHE A CG 1 ATOM 3917 C CD1 . PHE A 1 474 ? 46.916 5.230 0.282 1.00 21.64 ? 490 PHE A CD1 1 ATOM 3918 C CD2 . PHE A 1 474 ? 44.633 5.818 -0.137 1.00 21.34 ? 490 PHE A CD2 1 ATOM 3919 C CE1 . PHE A 1 474 ? 46.790 5.656 1.596 1.00 21.54 ? 490 PHE A CE1 1 ATOM 3920 C CE2 . PHE A 1 474 ? 44.503 6.254 1.184 1.00 21.73 ? 490 PHE A CE2 1 ATOM 3921 C CZ . PHE A 1 474 ? 45.583 6.161 2.045 1.00 21.28 ? 490 PHE A CZ 1 ATOM 3922 N N . ASP A 1 475 ? 45.274 1.447 -0.910 1.00 20.15 ? 491 ASP A N 1 ATOM 3923 C CA . ASP A 1 475 ? 44.301 0.364 -0.754 1.00 19.64 ? 491 ASP A CA 1 ATOM 3924 C C . ASP A 1 475 ? 43.344 0.467 0.445 1.00 19.44 ? 491 ASP A C 1 ATOM 3925 O O . ASP A 1 475 ? 42.260 -0.138 0.439 1.00 19.33 ? 491 ASP A O 1 ATOM 3926 C CB . ASP A 1 475 ? 45.038 -0.984 -0.773 1.00 19.55 ? 491 ASP A CB 1 ATOM 3927 C CG . ASP A 1 475 ? 45.651 -1.286 -2.134 1.00 20.32 ? 491 ASP A CG 1 ATOM 3928 O OD1 . ASP A 1 475 ? 44.918 -1.153 -3.125 1.00 21.18 ? 491 ASP A OD1 1 ATOM 3929 O OD2 . ASP A 1 475 ? 46.851 -1.630 -2.211 1.00 20.51 ? 491 ASP A OD2 1 ATOM 3930 N N . ALA A 1 476 ? 43.736 1.214 1.473 1.00 18.76 ? 492 ALA A N 1 ATOM 3931 C CA . ALA A 1 476 ? 42.917 1.295 2.680 1.00 18.37 ? 492 ALA A CA 1 ATOM 3932 C C . ALA A 1 476 ? 41.460 1.743 2.432 1.00 18.38 ? 492 ALA A C 1 ATOM 3933 O O . ALA A 1 476 ? 40.541 1.093 2.931 1.00 18.31 ? 492 ALA A O 1 ATOM 3934 C CB . ALA A 1 476 ? 43.599 2.156 3.743 1.00 18.09 ? 492 ALA A CB 1 ATOM 3935 N N . PRO A 1 477 ? 41.224 2.799 1.605 1.00 18.66 ? 493 PRO A N 1 ATOM 3936 C CA . PRO A 1 477 ? 39.821 3.212 1.414 1.00 18.76 ? 493 PRO A CA 1 ATOM 3937 C C . PRO A 1 477 ? 38.919 2.210 0.671 1.00 18.95 ? 493 PRO A C 1 ATOM 3938 O O . PRO A 1 477 ? 37.717 2.461 0.509 1.00 19.23 ? 493 PRO A O 1 ATOM 3939 C CB . PRO A 1 477 ? 39.939 4.536 0.645 1.00 18.80 ? 493 PRO A CB 1 ATOM 3940 C CG . PRO A 1 477 ? 41.327 5.017 0.902 1.00 18.47 ? 493 PRO A CG 1 ATOM 3941 C CD . PRO A 1 477 ? 42.151 3.761 0.977 1.00 18.58 ? 493 PRO A CD 1 ATOM 3942 N N . ALA A 1 478 ? 39.465 1.062 0.280 1.00 19.12 ? 494 ALA A N 1 ATOM 3943 C CA . ALA A 1 478 ? 38.643 0.032 -0.368 1.00 19.63 ? 494 ALA A CA 1 ATOM 3944 C C . ALA A 1 478 ? 37.767 -0.697 0.652 1.00 19.91 ? 494 ALA A C 1 ATOM 3945 O O . ALA A 1 478 ? 36.888 -1.464 0.285 1.00 20.44 ? 494 ALA A O 1 ATOM 3946 C CB . ALA A 1 478 ? 39.495 -0.937 -1.190 1.00 19.91 ? 494 ALA A CB 1 ATOM 3947 N N . LYS A 1 479 ? 38.003 -0.426 1.939 1.00 19.25 ? 495 LYS A N 1 ATOM 3948 C CA . LYS A 1 479 ? 37.121 -0.869 3.019 1.00 19.62 ? 495 LYS A CA 1 ATOM 3949 C C . LYS A 1 479 ? 36.130 0.260 3.358 1.00 19.31 ? 495 LYS A C 1 ATOM 3950 O O . LYS A 1 479 ? 36.545 1.408 3.573 1.00 19.05 ? 495 LYS A O 1 ATOM 3951 C CB . LYS A 1 479 ? 37.957 -1.240 4.256 1.00 19.39 ? 495 LYS A CB 1 ATOM 3952 C CG . LYS A 1 479 ? 37.148 -1.669 5.482 1.00 20.09 ? 495 LYS A CG 1 ATOM 3953 C CD . LYS A 1 479 ? 36.367 -2.960 5.258 1.00 20.63 ? 495 LYS A CD 1 ATOM 3954 C CE . LYS A 1 479 ? 35.390 -3.221 6.408 1.00 21.06 ? 495 LYS A CE 1 ATOM 3955 N NZ . LYS A 1 479 ? 34.260 -4.096 5.983 1.00 21.59 ? 495 LYS A NZ 1 ATOM 3956 N N . TYR A 1 480 ? 34.837 -0.073 3.423 1.00 19.14 ? 496 TYR A N 1 ATOM 3957 C CA . TYR A 1 480 ? 33.770 0.933 3.571 1.00 18.97 ? 496 TYR A CA 1 ATOM 3958 C C . TYR A 1 480 ? 34.037 1.947 4.672 1.00 18.85 ? 496 TYR A C 1 ATOM 3959 O O . TYR A 1 480 ? 33.999 3.151 4.443 1.00 18.84 ? 496 TYR A O 1 ATOM 3960 C CB . TYR A 1 480 ? 32.378 0.285 3.767 1.00 19.36 ? 496 TYR A CB 1 ATOM 3961 C CG . TYR A 1 480 ? 31.289 1.318 4.083 1.00 19.74 ? 496 TYR A CG 1 ATOM 3962 C CD1 . TYR A 1 480 ? 30.737 2.118 3.076 1.00 20.11 ? 496 TYR A CD1 1 ATOM 3963 C CD2 . TYR A 1 480 ? 30.854 1.515 5.397 1.00 19.85 ? 496 TYR A CD2 1 ATOM 3964 C CE1 . TYR A 1 480 ? 29.762 3.071 3.361 1.00 20.57 ? 496 TYR A CE1 1 ATOM 3965 C CE2 . TYR A 1 480 ? 29.879 2.462 5.696 1.00 20.45 ? 496 TYR A CE2 1 ATOM 3966 C CZ . TYR A 1 480 ? 29.344 3.238 4.680 1.00 20.98 ? 496 TYR A CZ 1 ATOM 3967 O OH . TYR A 1 480 ? 28.395 4.174 4.988 1.00 21.99 ? 496 TYR A OH 1 ATOM 3968 N N . HIS A 1 481 ? 34.317 1.446 5.870 1.00 18.48 ? 497 HIS A N 1 ATOM 3969 C CA . HIS A 1 481 ? 34.496 2.290 7.038 1.00 18.40 ? 497 HIS A CA 1 ATOM 3970 C C . HIS A 1 481 ? 35.654 3.270 6.907 1.00 18.62 ? 497 HIS A C 1 ATOM 3971 O O . HIS A 1 481 ? 35.633 4.358 7.489 1.00 19.18 ? 497 HIS A O 1 ATOM 3972 C CB . HIS A 1 481 ? 34.691 1.405 8.265 1.00 18.16 ? 497 HIS A CB 1 ATOM 3973 C CG . HIS A 1 481 ? 33.541 0.481 8.530 1.00 18.38 ? 497 HIS A CG 1 ATOM 3974 N ND1 . HIS A 1 481 ? 33.196 -0.549 7.680 1.00 18.03 ? 497 HIS A ND1 1 ATOM 3975 C CD2 . HIS A 1 481 ? 32.665 0.428 9.563 1.00 18.17 ? 497 HIS A CD2 1 ATOM 3976 C CE1 . HIS A 1 481 ? 32.150 -1.189 8.171 1.00 18.53 ? 497 HIS A CE1 1 ATOM 3977 N NE2 . HIS A 1 481 ? 31.811 -0.619 9.317 1.00 18.34 ? 497 HIS A NE2 1 ATOM 3978 N N . ILE A 1 482 ? 36.674 2.888 6.150 1.00 18.80 ? 498 ILE A N 1 ATOM 3979 C CA . ILE A 1 482 ? 37.785 3.800 5.899 1.00 18.75 ? 498 ILE A CA 1 ATOM 3980 C C . ILE A 1 482 ? 37.358 4.931 4.951 1.00 19.40 ? 498 ILE A C 1 ATOM 3981 O O . ILE A 1 482 ? 37.585 6.099 5.260 1.00 19.27 ? 498 ILE A O 1 ATOM 3982 C CB . ILE A 1 482 ? 39.086 3.048 5.525 1.00 18.24 ? 498 ILE A CB 1 ATOM 3983 C CG1 . ILE A 1 482 ? 39.464 2.126 6.715 1.00 18.28 ? 498 ILE A CG1 1 ATOM 3984 C CG2 . ILE A 1 482 ? 40.213 4.027 5.190 1.00 17.87 ? 498 ILE A CG2 1 ATOM 3985 C CD1 . ILE A 1 482 ? 40.862 1.545 6.687 1.00 18.48 ? 498 ILE A CD1 1 ATOM 3986 N N . SER A 1 483 ? 36.718 4.604 3.823 1.00 20.31 ? 499 SER A N 1 ATOM 3987 C CA . SER A 1 483 ? 36.119 5.651 2.978 1.00 20.73 ? 499 SER A CA 1 ATOM 3988 C C . SER A 1 483 ? 35.063 6.510 3.682 1.00 21.16 ? 499 SER A C 1 ATOM 3989 O O . SER A 1 483 ? 34.969 7.709 3.406 1.00 21.61 ? 499 SER A O 1 ATOM 3990 C CB . SER A 1 483 ? 35.538 5.084 1.674 1.00 21.29 ? 499 SER A CB 1 ATOM 3991 O OG . SER A 1 483 ? 36.557 4.898 0.710 1.00 21.13 ? 499 SER A OG 1 ATOM 3992 N N . ALA A 1 484 ? 34.302 5.916 4.605 1.00 21.34 ? 500 ALA A N 1 ATOM 3993 C CA . ALA A 1 484 ? 33.149 6.592 5.217 1.00 21.84 ? 500 ALA A CA 1 ATOM 3994 C C . ALA A 1 484 ? 33.450 7.214 6.587 1.00 22.13 ? 500 ALA A C 1 ATOM 3995 O O . ALA A 1 484 ? 32.540 7.703 7.259 1.00 21.73 ? 500 ALA A O 1 ATOM 3996 C CB . ALA A 1 484 ? 31.968 5.634 5.325 1.00 22.04 ? 500 ALA A CB 1 ATOM 3997 N N . ASP A 1 485 ? 34.722 7.186 6.985 1.00 21.64 ? 501 ASP A N 1 ATOM 3998 C CA . ASP A 1 485 ? 35.184 7.793 8.239 1.00 21.85 ? 501 ASP A CA 1 ATOM 3999 C C . ASP A 1 485 ? 34.390 7.249 9.435 1.00 21.75 ? 501 ASP A C 1 ATOM 4000 O O . ASP A 1 485 ? 33.799 8.015 10.199 1.00 22.35 ? 501 ASP A O 1 ATOM 4001 C CB . ASP A 1 485 ? 35.136 9.342 8.163 1.00 21.84 ? 501 ASP A CB 1 ATOM 4002 C CG . ASP A 1 485 ? 35.565 10.026 9.479 1.00 22.69 ? 501 ASP A CG 1 ATOM 4003 O OD1 . ASP A 1 485 ? 36.409 9.460 10.207 1.00 21.84 ? 501 ASP A OD1 1 ATOM 4004 O OD2 . ASP A 1 485 ? 35.057 11.138 9.767 1.00 23.29 ? 501 ASP A OD2 1 ATOM 4005 N N . VAL A 1 486 ? 34.366 5.925 9.568 1.00 21.39 ? 502 VAL A N 1 ATOM 4006 C CA . VAL A 1 486 ? 33.716 5.255 10.697 1.00 21.03 ? 502 VAL A CA 1 ATOM 4007 C C . VAL A 1 486 ? 34.768 4.540 11.557 1.00 20.77 ? 502 VAL A C 1 ATOM 4008 O O . VAL A 1 486 ? 35.488 3.672 11.078 1.00 20.92 ? 502 VAL A O 1 ATOM 4009 C CB . VAL A 1 486 ? 32.620 4.264 10.224 1.00 21.18 ? 502 VAL A CB 1 ATOM 4010 C CG1 . VAL A 1 486 ? 31.964 3.556 11.397 1.00 20.86 ? 502 VAL A CG1 1 ATOM 4011 C CG2 . VAL A 1 486 ? 31.555 4.984 9.398 1.00 21.68 ? 502 VAL A CG2 1 ATOM 4012 N N . GLU A 1 487 ? 34.848 4.914 12.832 1.00 20.74 ? 503 GLU A N 1 ATOM 4013 C CA . GLU A 1 487 ? 35.778 4.311 13.786 1.00 20.17 ? 503 GLU A CA 1 ATOM 4014 C C . GLU A 1 487 ? 35.564 2.780 13.831 1.00 19.72 ? 503 GLU A C 1 ATOM 4015 O O . GLU A 1 487 ? 34.414 2.327 13.792 1.00 20.04 ? 503 GLU A O 1 ATOM 4016 C CB . GLU A 1 487 ? 35.545 4.954 15.162 1.00 20.96 ? 503 GLU A CB 1 ATOM 4017 C CG . GLU A 1 487 ? 36.547 4.554 16.222 1.00 20.97 ? 503 GLU A CG 1 ATOM 4018 C CD . GLU A 1 487 ? 36.021 3.466 17.143 1.00 22.01 ? 503 GLU A CD 1 ATOM 4019 O OE1 . GLU A 1 487 ? 35.086 2.721 16.751 1.00 22.37 ? 503 GLU A OE1 1 ATOM 4020 O OE2 . GLU A 1 487 ? 36.553 3.355 18.261 1.00 21.47 ? 503 GLU A OE2 1 ATOM 4021 N N . TYR A 1 488 ? 36.647 1.995 13.878 1.00 18.44 ? 504 TYR A N 1 ATOM 4022 C CA . TYR A 1 488 ? 36.533 0.520 13.766 1.00 18.37 ? 504 TYR A CA 1 ATOM 4023 C C . TYR A 1 488 ? 36.761 -0.249 15.072 1.00 18.23 ? 504 TYR A C 1 ATOM 4024 O O . TYR A 1 488 ? 36.318 -1.403 15.206 1.00 18.06 ? 504 TYR A O 1 ATOM 4025 C CB . TYR A 1 488 ? 37.422 -0.053 12.628 1.00 18.43 ? 504 TYR A CB 1 ATOM 4026 C CG . TYR A 1 488 ? 36.793 -1.258 11.929 1.00 18.60 ? 504 TYR A CG 1 ATOM 4027 C CD1 . TYR A 1 488 ? 35.822 -1.082 10.933 1.00 18.11 ? 504 TYR A CD1 1 ATOM 4028 C CD2 . TYR A 1 488 ? 37.128 -2.566 12.302 1.00 18.22 ? 504 TYR A CD2 1 ATOM 4029 C CE1 . TYR A 1 488 ? 35.221 -2.171 10.313 1.00 18.47 ? 504 TYR A CE1 1 ATOM 4030 C CE2 . TYR A 1 488 ? 36.535 -3.668 11.692 1.00 18.17 ? 504 TYR A CE2 1 ATOM 4031 C CZ . TYR A 1 488 ? 35.589 -3.469 10.689 1.00 18.19 ? 504 TYR A CZ 1 ATOM 4032 O OH . TYR A 1 488 ? 34.978 -4.547 10.083 1.00 18.20 ? 504 TYR A OH 1 ATOM 4033 N N . LEU A 1 489 ? 37.415 0.390 16.042 1.00 18.08 ? 505 LEU A N 1 ATOM 4034 C CA . LEU A 1 489 ? 37.701 -0.264 17.318 1.00 18.30 ? 505 LEU A CA 1 ATOM 4035 C C . LEU A 1 489 ? 36.447 -0.795 18.020 1.00 18.70 ? 505 LEU A C 1 ATOM 4036 O O . LEU A 1 489 ? 36.508 -1.818 18.728 1.00 18.59 ? 505 LEU A O 1 ATOM 4037 C CB . LEU A 1 489 ? 38.471 0.673 18.259 1.00 18.06 ? 505 LEU A CB 1 ATOM 4038 C CG . LEU A 1 489 ? 39.352 -0.046 19.279 1.00 18.25 ? 505 LEU A CG 1 ATOM 4039 C CD1 . LEU A 1 489 ? 40.623 -0.571 18.626 1.00 17.83 ? 505 LEU A CD1 1 ATOM 4040 C CD2 . LEU A 1 489 ? 39.671 0.866 20.472 1.00 17.40 ? 505 LEU A CD2 1 ATOM 4041 N N . ARG A 1 490 ? 35.326 -0.100 17.820 1.00 18.51 ? 506 ARG A N 1 ATOM 4042 C CA . ARG A 1 490 ? 34.012 -0.564 18.259 1.00 18.84 ? 506 ARG A CA 1 ATOM 4043 C C . ARG A 1 490 ? 33.783 -2.059 17.981 1.00 18.90 ? 506 ARG A C 1 ATOM 4044 O O . ARG A 1 490 ? 33.191 -2.750 18.797 1.00 19.00 ? 506 ARG A O 1 ATOM 4045 C CB . ARG A 1 490 ? 32.901 0.275 17.610 1.00 18.63 ? 506 ARG A CB 1 ATOM 4046 C CG . ARG A 1 490 ? 32.887 0.239 16.077 1.00 18.60 ? 506 ARG A CG 1 ATOM 4047 C CD . ARG A 1 490 ? 31.849 1.201 15.501 1.00 18.71 ? 506 ARG A CD 1 ATOM 4048 N NE . ARG A 1 490 ? 32.162 2.610 15.783 1.00 18.76 ? 506 ARG A NE 1 ATOM 4049 C CZ . ARG A 1 490 ? 31.407 3.646 15.415 1.00 19.17 ? 506 ARG A CZ 1 ATOM 4050 N NH1 . ARG A 1 490 ? 30.280 3.451 14.726 1.00 18.87 ? 506 ARG A NH1 1 ATOM 4051 N NH2 . ARG A 1 490 ? 31.773 4.888 15.737 1.00 18.97 ? 506 ARG A NH2 1 ATOM 4052 N N . TYR A 1 491 ? 34.240 -2.549 16.826 1.00 18.50 ? 507 TYR A N 1 ATOM 4053 C CA . TYR A 1 491 ? 33.985 -3.941 16.453 1.00 18.55 ? 507 TYR A CA 1 ATOM 4054 C C . TYR A 1 491 ? 34.894 -4.905 17.215 1.00 18.52 ? 507 TYR A C 1 ATOM 4055 O O . TYR A 1 491 ? 34.474 -6.009 17.576 1.00 18.56 ? 507 TYR A O 1 ATOM 4056 C CB . TYR A 1 491 ? 34.094 -4.140 14.931 1.00 18.76 ? 507 TYR A CB 1 ATOM 4057 C CG . TYR A 1 491 ? 33.094 -3.324 14.149 1.00 19.59 ? 507 TYR A CG 1 ATOM 4058 C CD1 . TYR A 1 491 ? 31.727 -3.643 14.165 1.00 20.16 ? 507 TYR A CD1 1 ATOM 4059 C CD2 . TYR A 1 491 ? 33.505 -2.234 13.375 1.00 19.79 ? 507 TYR A CD2 1 ATOM 4060 C CE1 . TYR A 1 491 ? 30.807 -2.900 13.432 1.00 20.56 ? 507 TYR A CE1 1 ATOM 4061 C CE2 . TYR A 1 491 ? 32.587 -1.485 12.648 1.00 20.47 ? 507 TYR A CE2 1 ATOM 4062 C CZ . TYR A 1 491 ? 31.244 -1.819 12.688 1.00 20.69 ? 507 TYR A CZ 1 ATOM 4063 O OH . TYR A 1 491 ? 30.326 -1.083 11.965 1.00 22.03 ? 507 TYR A OH 1 ATOM 4064 N N . LEU A 1 492 ? 36.133 -4.488 17.471 1.00 18.10 ? 508 LEU A N 1 ATOM 4065 C CA . LEU A 1 492 ? 37.034 -5.295 18.287 1.00 17.23 ? 508 LEU A CA 1 ATOM 4066 C C . LEU A 1 492 ? 36.486 -5.413 19.720 1.00 17.76 ? 508 LEU A C 1 ATOM 4067 O O . LEU A 1 492 ? 36.390 -6.530 20.262 1.00 17.62 ? 508 LEU A O 1 ATOM 4068 C CB . LEU A 1 492 ? 38.474 -4.745 18.266 1.00 16.60 ? 508 LEU A CB 1 ATOM 4069 C CG . LEU A 1 492 ? 39.494 -5.408 19.224 1.00 16.08 ? 508 LEU A CG 1 ATOM 4070 C CD1 . LEU A 1 492 ? 39.649 -6.913 18.976 1.00 16.08 ? 508 LEU A CD1 1 ATOM 4071 C CD2 . LEU A 1 492 ? 40.862 -4.725 19.179 1.00 15.66 ? 508 LEU A CD2 1 ATOM 4072 N N . VAL A 1 493 ? 36.106 -4.279 20.307 1.00 17.54 ? 509 VAL A N 1 ATOM 4073 C CA . VAL A 1 493 ? 35.487 -4.264 21.644 1.00 18.04 ? 509 VAL A CA 1 ATOM 4074 C C . VAL A 1 493 ? 34.217 -5.142 21.653 1.00 18.68 ? 509 VAL A C 1 ATOM 4075 O O . VAL A 1 493 ? 34.054 -5.994 22.527 1.00 18.49 ? 509 VAL A O 1 ATOM 4076 C CB . VAL A 1 493 ? 35.176 -2.823 22.117 1.00 17.87 ? 509 VAL A CB 1 ATOM 4077 C CG1 . VAL A 1 493 ? 34.466 -2.835 23.475 1.00 18.38 ? 509 VAL A CG1 1 ATOM 4078 C CG2 . VAL A 1 493 ? 36.468 -2.003 22.182 1.00 17.75 ? 509 VAL A CG2 1 ATOM 4079 N N . SER A 1 494 ? 33.351 -4.950 20.655 1.00 19.00 ? 510 SER A N 1 ATOM 4080 C CA . SER A 1 494 ? 32.155 -5.791 20.470 1.00 19.93 ? 510 SER A CA 1 ATOM 4081 C C . SER A 1 494 ? 32.459 -7.295 20.465 1.00 20.16 ? 510 SER A C 1 ATOM 4082 O O . SER A 1 494 ? 31.815 -8.059 21.178 1.00 19.86 ? 510 SER A O 1 ATOM 4083 C CB . SER A 1 494 ? 31.435 -5.419 19.171 1.00 20.06 ? 510 SER A CB 1 ATOM 4084 O OG . SER A 1 494 ? 30.406 -6.349 18.874 1.00 20.96 ? 510 SER A OG 1 ATOM 4085 N N . PHE A 1 495 ? 33.425 -7.724 19.650 1.00 20.13 ? 511 PHE A N 1 ATOM 4086 C CA . PHE A 1 495 ? 33.742 -9.162 19.561 1.00 20.57 ? 511 PHE A CA 1 ATOM 4087 C C . PHE A 1 495 ? 34.235 -9.784 20.862 1.00 20.67 ? 511 PHE A C 1 ATOM 4088 O O . PHE A 1 495 ? 34.022 -10.978 21.072 1.00 21.10 ? 511 PHE A O 1 ATOM 4089 C CB . PHE A 1 495 ? 34.695 -9.469 18.417 1.00 20.23 ? 511 PHE A CB 1 ATOM 4090 C CG . PHE A 1 495 ? 33.998 -9.677 17.100 1.00 20.13 ? 511 PHE A CG 1 ATOM 4091 C CD1 . PHE A 1 495 ? 33.036 -8.768 16.649 1.00 20.14 ? 511 PHE A CD1 1 ATOM 4092 C CD2 . PHE A 1 495 ? 34.296 -10.791 16.315 1.00 20.21 ? 511 PHE A CD2 1 ATOM 4093 C CE1 . PHE A 1 495 ? 32.399 -8.959 15.414 1.00 20.10 ? 511 PHE A CE1 1 ATOM 4094 C CE2 . PHE A 1 495 ? 33.666 -10.988 15.091 1.00 19.94 ? 511 PHE A CE2 1 ATOM 4095 C CZ . PHE A 1 495 ? 32.711 -10.079 14.648 1.00 20.36 ? 511 PHE A CZ 1 ATOM 4096 N N . ILE A 1 496 ? 34.853 -8.976 21.729 1.00 20.97 ? 512 ILE A N 1 ATOM 4097 C CA . ILE A 1 496 ? 35.252 -9.408 23.078 1.00 20.98 ? 512 ILE A CA 1 ATOM 4098 C C . ILE A 1 496 ? 34.063 -9.402 24.063 1.00 21.49 ? 512 ILE A C 1 ATOM 4099 O O . ILE A 1 496 ? 33.758 -10.427 24.705 1.00 21.23 ? 512 ILE A O 1 ATOM 4100 C CB . ILE A 1 496 ? 36.404 -8.529 23.638 1.00 21.54 ? 512 ILE A CB 1 ATOM 4101 C CG1 . ILE A 1 496 ? 37.678 -8.692 22.800 1.00 21.28 ? 512 ILE A CG1 1 ATOM 4102 C CG2 . ILE A 1 496 ? 36.704 -8.867 25.103 1.00 21.71 ? 512 ILE A CG2 1 ATOM 4103 C CD1 . ILE A 1 496 ? 38.691 -7.583 23.026 1.00 21.95 ? 512 ILE A CD1 1 ATOM 4104 N N . ILE A 1 497 ? 33.380 -8.265 24.179 1.00 20.98 ? 513 ILE A N 1 ATOM 4105 C CA . ILE A 1 497 ? 32.300 -8.150 25.170 1.00 21.57 ? 513 ILE A CA 1 ATOM 4106 C C . ILE A 1 497 ? 31.035 -8.950 24.820 1.00 21.56 ? 513 ILE A C 1 ATOM 4107 O O . ILE A 1 497 ? 30.309 -9.352 25.715 1.00 22.68 ? 513 ILE A O 1 ATOM 4108 C CB . ILE A 1 497 ? 31.960 -6.680 25.552 1.00 21.36 ? 513 ILE A CB 1 ATOM 4109 C CG1 . ILE A 1 497 ? 31.280 -5.928 24.404 1.00 21.37 ? 513 ILE A CG1 1 ATOM 4110 C CG2 . ILE A 1 497 ? 33.209 -5.962 26.078 1.00 21.62 ? 513 ILE A CG2 1 ATOM 4111 C CD1 . ILE A 1 497 ? 30.826 -4.520 24.748 1.00 21.21 ? 513 ILE A CD1 1 ATOM 4112 N N . GLN A 1 498 ? 30.781 -9.209 23.532 1.00 21.40 ? 514 GLN A N 1 ATOM 4113 C CA . GLN A 1 498 ? 29.576 -9.983 23.173 1.00 21.21 ? 514 GLN A CA 1 ATOM 4114 C C . GLN A 1 498 ? 29.611 -11.409 23.755 1.00 21.48 ? 514 GLN A C 1 ATOM 4115 O O . GLN A 1 498 ? 28.564 -12.016 23.979 1.00 21.78 ? 514 GLN A O 1 ATOM 4116 C CB . GLN A 1 498 ? 29.352 -10.023 21.657 1.00 21.25 ? 514 GLN A CB 1 ATOM 4117 C CG . GLN A 1 498 ? 30.352 -10.878 20.900 1.00 21.31 ? 514 GLN A CG 1 ATOM 4118 C CD . GLN A 1 498 ? 30.155 -10.781 19.402 1.00 21.22 ? 514 GLN A CD 1 ATOM 4119 O OE1 . GLN A 1 498 ? 29.923 -11.785 18.734 1.00 22.36 ? 514 GLN A OE1 1 ATOM 4120 N NE2 . GLN A 1 498 ? 30.214 -9.561 18.871 1.00 20.61 ? 514 GLN A NE2 1 ATOM 4121 N N . PHE A 1 499 ? 30.811 -11.927 24.017 1.00 21.41 ? 515 PHE A N 1 ATOM 4122 C CA . PHE A 1 499 ? 30.936 -13.235 24.645 1.00 21.64 ? 515 PHE A CA 1 ATOM 4123 C C . PHE A 1 499 ? 30.701 -13.164 26.152 1.00 22.32 ? 515 PHE A C 1 ATOM 4124 O O . PHE A 1 499 ? 30.152 -14.110 26.725 1.00 22.64 ? 515 PHE A O 1 ATOM 4125 C CB . PHE A 1 499 ? 32.257 -13.932 24.285 1.00 21.22 ? 515 PHE A CB 1 ATOM 4126 C CG . PHE A 1 499 ? 32.280 -14.465 22.881 1.00 21.56 ? 515 PHE A CG 1 ATOM 4127 C CD1 . PHE A 1 499 ? 32.705 -13.668 21.830 1.00 21.22 ? 515 PHE A CD1 1 ATOM 4128 C CD2 . PHE A 1 499 ? 31.838 -15.761 22.604 1.00 22.17 ? 515 PHE A CD2 1 ATOM 4129 C CE1 . PHE A 1 499 ? 32.700 -14.141 20.523 1.00 21.06 ? 515 PHE A CE1 1 ATOM 4130 C CE2 . PHE A 1 499 ? 31.822 -16.247 21.298 1.00 22.00 ? 515 PHE A CE2 1 ATOM 4131 C CZ . PHE A 1 499 ? 32.267 -15.438 20.258 1.00 21.57 ? 515 PHE A CZ 1 ATOM 4132 N N . GLN A 1 500 ? 31.102 -12.054 26.780 1.00 22.30 ? 516 GLN A N 1 ATOM 4133 C CA . GLN A 1 500 ? 30.714 -11.776 28.176 1.00 23.37 ? 516 GLN A CA 1 ATOM 4134 C C . GLN A 1 500 ? 29.187 -11.687 28.306 1.00 23.74 ? 516 GLN A C 1 ATOM 4135 O O . GLN A 1 500 ? 28.610 -12.260 29.239 1.00 24.91 ? 516 GLN A O 1 ATOM 4136 C CB . GLN A 1 500 ? 31.375 -10.489 28.715 1.00 23.12 ? 516 GLN A CB 1 ATOM 4137 C CG . GLN A 1 500 ? 32.898 -10.486 28.653 1.00 22.72 ? 516 GLN A CG 1 ATOM 4138 C CD . GLN A 1 500 ? 33.523 -9.228 29.228 1.00 22.92 ? 516 GLN A CD 1 ATOM 4139 O OE1 . GLN A 1 500 ? 34.181 -8.465 28.513 1.00 22.32 ? 516 GLN A OE1 1 ATOM 4140 N NE2 . GLN A 1 500 ? 33.332 -9.005 30.545 1.00 22.66 ? 516 GLN A NE2 1 ATOM 4141 N N . PHE A 1 501 ? 28.539 -10.968 27.386 1.00 23.77 ? 517 PHE A N 1 ATOM 4142 C CA . PHE A 1 501 ? 27.068 -10.848 27.374 1.00 24.35 ? 517 PHE A CA 1 ATOM 4143 C C . PHE A 1 501 ? 26.384 -12.194 27.085 1.00 25.07 ? 517 PHE A C 1 ATOM 4144 O O . PHE A 1 501 ? 25.410 -12.561 27.754 1.00 25.18 ? 517 PHE A O 1 ATOM 4145 C CB . PHE A 1 501 ? 26.589 -9.816 26.349 1.00 24.02 ? 517 PHE A CB 1 ATOM 4146 C CG . PHE A 1 501 ? 27.003 -8.394 26.646 1.00 24.15 ? 517 PHE A CG 1 ATOM 4147 C CD1 . PHE A 1 501 ? 27.047 -7.909 27.953 1.00 24.30 ? 517 PHE A CD1 1 ATOM 4148 C CD2 . PHE A 1 501 ? 27.291 -7.519 25.605 1.00 24.03 ? 517 PHE A CD2 1 ATOM 4149 C CE1 . PHE A 1 501 ? 27.412 -6.591 28.207 1.00 23.93 ? 517 PHE A CE1 1 ATOM 4150 C CE2 . PHE A 1 501 ? 27.660 -6.203 25.855 1.00 23.94 ? 517 PHE A CE2 1 ATOM 4151 C CZ . PHE A 1 501 ? 27.723 -5.740 27.160 1.00 23.88 ? 517 PHE A CZ 1 ATOM 4152 N N . TYR A 1 502 ? 26.900 -12.917 26.090 1.00 25.02 ? 518 TYR A N 1 ATOM 4153 C CA . TYR A 1 502 ? 26.323 -14.195 25.670 1.00 25.96 ? 518 TYR A CA 1 ATOM 4154 C C . TYR A 1 502 ? 26.408 -15.249 26.767 1.00 26.82 ? 518 TYR A C 1 ATOM 4155 O O . TYR A 1 502 ? 25.415 -15.914 27.067 1.00 27.18 ? 518 TYR A O 1 ATOM 4156 C CB . TYR A 1 502 ? 26.974 -14.685 24.373 1.00 25.23 ? 518 TYR A CB 1 ATOM 4157 C CG . TYR A 1 502 ? 26.410 -15.966 23.782 1.00 25.78 ? 518 TYR A CG 1 ATOM 4158 C CD1 . TYR A 1 502 ? 25.123 -16.012 23.224 1.00 26.10 ? 518 TYR A CD1 1 ATOM 4159 C CD2 . TYR A 1 502 ? 27.184 -17.124 23.744 1.00 25.97 ? 518 TYR A CD2 1 ATOM 4160 C CE1 . TYR A 1 502 ? 24.621 -17.188 22.671 1.00 26.41 ? 518 TYR A CE1 1 ATOM 4161 C CE2 . TYR A 1 502 ? 26.696 -18.298 23.190 1.00 26.92 ? 518 TYR A CE2 1 ATOM 4162 C CZ . TYR A 1 502 ? 25.417 -18.330 22.656 1.00 26.98 ? 518 TYR A CZ 1 ATOM 4163 O OH . TYR A 1 502 ? 24.963 -19.517 22.105 1.00 27.91 ? 518 TYR A OH 1 ATOM 4164 N N . LYS A 1 503 ? 27.581 -15.381 27.381 1.00 26.88 ? 519 LYS A N 1 ATOM 4165 C CA . LYS A 1 503 ? 27.768 -16.314 28.482 1.00 26.98 ? 519 LYS A CA 1 ATOM 4166 C C . LYS A 1 503 ? 26.797 -16.034 29.634 1.00 27.71 ? 519 LYS A C 1 ATOM 4167 O O . LYS A 1 503 ? 26.127 -16.952 30.128 1.00 27.25 ? 519 LYS A O 1 ATOM 4168 C CB . LYS A 1 503 ? 29.211 -16.272 28.981 1.00 27.32 ? 519 LYS A CB 1 ATOM 4169 C CG . LYS A 1 503 ? 29.494 -17.204 30.143 1.00 28.52 ? 519 LYS A CG 1 ATOM 4170 C CD . LYS A 1 503 ? 30.924 -17.065 30.629 1.00 28.75 ? 519 LYS A CD 1 ATOM 4171 C CE . LYS A 1 503 ? 30.999 -17.408 32.112 1.00 29.45 ? 519 LYS A CE 1 ATOM 4172 N NZ . LYS A 1 503 ? 32.407 -17.470 32.583 1.00 30.21 ? 519 LYS A NZ 1 ATOM 4173 N N . SER A 1 504 ? 26.718 -14.771 30.049 1.00 26.76 ? 520 SER A N 1 ATOM 4174 C CA . SER A 1 504 ? 25.822 -14.383 31.132 1.00 27.29 ? 520 SER A CA 1 ATOM 4175 C C . SER A 1 504 ? 24.342 -14.590 30.809 1.00 27.21 ? 520 SER A C 1 ATOM 4176 O O . SER A 1 504 ? 23.594 -15.079 31.664 1.00 27.65 ? 520 SER A O 1 ATOM 4177 C CB . SER A 1 504 ? 26.085 -12.938 31.568 1.00 27.32 ? 520 SER A CB 1 ATOM 4178 O OG . SER A 1 504 ? 27.316 -12.865 32.263 1.00 27.89 ? 520 SER A OG 1 ATOM 4179 N N . ALA A 1 505 ? 23.930 -14.217 29.595 1.00 26.52 ? 521 ALA A N 1 ATOM 4180 C CA . ALA A 1 505 ? 22.548 -14.397 29.133 1.00 26.95 ? 521 ALA A CA 1 ATOM 4181 C C . ALA A 1 505 ? 22.173 -15.880 29.062 1.00 27.68 ? 521 ALA A C 1 ATOM 4182 O O . ALA A 1 505 ? 21.047 -16.254 29.406 1.00 28.11 ? 521 ALA A O 1 ATOM 4183 C CB . ALA A 1 505 ? 22.337 -13.740 27.776 1.00 26.21 ? 521 ALA A CB 1 ATOM 4184 N N . CYS A 1 506 ? 23.117 -16.707 28.612 1.00 27.69 ? 522 CYS A N 1 ATOM 4185 C CA . CYS A 1 506 ? 22.928 -18.154 28.558 1.00 29.03 ? 522 CYS A CA 1 ATOM 4186 C C . CYS A 1 506 ? 22.774 -18.785 29.946 1.00 29.82 ? 522 CYS A C 1 ATOM 4187 O O . CYS A 1 506 ? 21.939 -19.665 30.131 1.00 30.11 ? 522 CYS A O 1 ATOM 4188 C CB . CYS A 1 506 ? 24.064 -18.826 27.792 1.00 29.27 ? 522 CYS A CB 1 ATOM 4189 S SG . CYS A 1 506 ? 24.020 -18.410 26.038 1.00 29.60 ? 522 CYS A SG 1 ATOM 4190 N N . ILE A 1 507 ? 23.585 -18.345 30.905 1.00 30.16 ? 523 ILE A N 1 ATOM 4191 C CA . ILE A 1 507 ? 23.433 -18.788 32.296 1.00 31.21 ? 523 ILE A CA 1 ATOM 4192 C C . ILE A 1 507 ? 22.045 -18.372 32.820 1.00 32.25 ? 523 ILE A C 1 ATOM 4193 O O . ILE A 1 507 ? 21.296 -19.210 33.325 1.00 33.23 ? 523 ILE A O 1 ATOM 4194 C CB . ILE A 1 507 ? 24.585 -18.279 33.201 1.00 31.21 ? 523 ILE A CB 1 ATOM 4195 C CG1 . ILE A 1 507 ? 25.892 -19.005 32.854 1.00 31.37 ? 523 ILE A CG1 1 ATOM 4196 C CG2 . ILE A 1 507 ? 24.247 -18.467 34.679 1.00 32.05 ? 523 ILE A CG2 1 ATOM 4197 C CD1 . ILE A 1 507 ? 27.145 -18.386 33.446 1.00 30.79 ? 523 ILE A CD1 1 ATOM 4198 N N . LYS A 1 508 ? 21.689 -17.098 32.659 1.00 31.42 ? 524 LYS A N 1 ATOM 4199 C CA . LYS A 1 508 ? 20.371 -16.599 33.082 1.00 31.81 ? 524 LYS A CA 1 ATOM 4200 C C . LYS A 1 508 ? 19.195 -17.353 32.446 1.00 32.18 ? 524 LYS A C 1 ATOM 4201 O O . LYS A 1 508 ? 18.138 -17.489 33.063 1.00 33.00 ? 524 LYS A O 1 ATOM 4202 C CB . LYS A 1 508 ? 20.239 -15.097 32.794 1.00 31.67 ? 524 LYS A CB 1 ATOM 4203 C CG . LYS A 1 508 ? 21.167 -14.213 33.618 1.00 31.63 ? 524 LYS A CG 1 ATOM 4204 C CD . LYS A 1 508 ? 21.213 -12.797 33.069 1.00 31.69 ? 524 LYS A CD 1 ATOM 4205 C CE . LYS A 1 508 ? 22.367 -12.006 33.667 1.00 31.91 ? 524 LYS A CE 1 ATOM 4206 N NZ . LYS A 1 508 ? 22.097 -11.612 35.077 1.00 32.78 ? 524 LYS A NZ 1 ATOM 4207 N N . ALA A 1 509 ? 19.380 -17.829 31.216 1.00 31.69 ? 525 ALA A N 1 ATOM 4208 C CA . ALA A 1 509 ? 18.339 -18.554 30.483 1.00 32.01 ? 525 ALA A CA 1 ATOM 4209 C C . ALA A 1 509 ? 18.285 -20.039 30.844 1.00 32.49 ? 525 ALA A C 1 ATOM 4210 O O . ALA A 1 509 ? 17.422 -20.755 30.351 1.00 33.01 ? 525 ALA A O 1 ATOM 4211 C CB . ALA A 1 509 ? 18.534 -18.392 28.975 1.00 30.89 ? 525 ALA A CB 1 ATOM 4212 N N . GLY A 1 510 ? 19.210 -20.497 31.686 1.00 32.73 ? 526 GLY A N 1 ATOM 4213 C CA . GLY A 1 510 ? 19.335 -21.919 32.013 1.00 33.53 ? 526 GLY A CA 1 ATOM 4214 C C . GLY A 1 510 ? 19.869 -22.738 30.851 1.00 34.06 ? 526 GLY A C 1 ATOM 4215 O O . GLY A 1 510 ? 19.609 -23.939 30.755 1.00 33.98 ? 526 GLY A O 1 ATOM 4216 N N . GLN A 1 511 ? 20.627 -22.085 29.972 1.00 33.26 ? 527 GLN A N 1 ATOM 4217 C CA . GLN A 1 511 ? 21.081 -22.682 28.719 1.00 33.62 ? 527 GLN A CA 1 ATOM 4218 C C . GLN A 1 511 ? 22.574 -23.019 28.717 1.00 33.92 ? 527 GLN A C 1 ATOM 4219 O O . GLN A 1 511 ? 23.088 -23.612 27.762 1.00 34.69 ? 527 GLN A O 1 ATOM 4220 C CB . GLN A 1 511 ? 20.761 -21.748 27.550 1.00 33.34 ? 527 GLN A CB 1 ATOM 4221 C CG . GLN A 1 511 ? 19.317 -21.786 27.083 1.00 33.87 ? 527 GLN A CG 1 ATOM 4222 C CD . GLN A 1 511 ? 19.025 -22.998 26.220 1.00 34.37 ? 527 GLN A CD 1 ATOM 4223 O OE1 . GLN A 1 511 ? 19.765 -23.304 25.281 1.00 34.52 ? 527 GLN A OE1 1 ATOM 4224 N NE2 . GLN A 1 511 ? 17.941 -23.691 26.528 1.00 34.62 ? 527 GLN A NE2 1 ATOM 4225 N N . TYR A 1 512 ? 23.275 -22.630 29.774 1.00 33.56 ? 528 TYR A N 1 ATOM 4226 C CA . TYR A 1 512 ? 24.677 -22.971 29.903 1.00 33.28 ? 528 TYR A CA 1 ATOM 4227 C C . TYR A 1 512 ? 25.015 -23.314 31.334 1.00 34.32 ? 528 TYR A C 1 ATOM 4228 O O . TYR A 1 512 ? 24.715 -22.559 32.251 1.00 34.76 ? 528 TYR A O 1 ATOM 4229 C CB . TYR A 1 512 ? 25.574 -21.826 29.412 1.00 31.82 ? 528 TYR A CB 1 ATOM 4230 C CG . TYR A 1 512 ? 27.054 -22.039 29.672 1.00 31.18 ? 528 TYR A CG 1 ATOM 4231 C CD1 . TYR A 1 512 ? 27.681 -23.237 29.325 1.00 31.20 ? 528 TYR A CD1 1 ATOM 4232 C CD2 . TYR A 1 512 ? 27.835 -21.030 30.241 1.00 31.07 ? 528 TYR A CD2 1 ATOM 4233 C CE1 . TYR A 1 512 ? 29.033 -23.435 29.555 1.00 30.77 ? 528 TYR A CE1 1 ATOM 4234 C CE2 . TYR A 1 512 ? 29.194 -21.217 30.462 1.00 30.58 ? 528 TYR A CE2 1 ATOM 4235 C CZ . TYR A 1 512 ? 29.786 -22.422 30.113 1.00 30.46 ? 528 TYR A CZ 1 ATOM 4236 O OH . TYR A 1 512 ? 31.129 -22.629 30.329 1.00 30.04 ? 528 TYR A OH 1 ATOM 4237 N N . ASP A 1 513 ? 25.641 -24.469 31.502 1.00 36.08 ? 529 ASP A N 1 ATOM 4238 C CA . ASP A 1 513 ? 26.196 -24.895 32.772 1.00 38.38 ? 529 ASP A CA 1 ATOM 4239 C C . ASP A 1 513 ? 27.495 -25.602 32.418 1.00 38.61 ? 529 ASP A C 1 ATOM 4240 O O . ASP A 1 513 ? 27.468 -26.622 31.717 1.00 38.36 ? 529 ASP A O 1 ATOM 4241 C CB . ASP A 1 513 ? 25.218 -25.844 33.485 1.00 40.24 ? 529 ASP A CB 1 ATOM 4242 C CG . ASP A 1 513 ? 25.747 -26.368 34.827 1.00 42.10 ? 529 ASP A CG 1 ATOM 4243 O OD1 . ASP A 1 513 ? 26.963 -26.288 35.100 1.00 41.56 ? 529 ASP A OD1 1 ATOM 4244 O OD2 . ASP A 1 513 ? 24.923 -26.881 35.616 1.00 43.45 ? 529 ASP A OD2 1 ATOM 4245 N N . PRO A 1 514 ? 28.639 -25.064 32.891 1.00 39.86 ? 530 PRO A N 1 ATOM 4246 C CA . PRO A 1 514 ? 29.964 -25.607 32.540 1.00 41.36 ? 530 PRO A CA 1 ATOM 4247 C C . PRO A 1 514 ? 30.207 -27.049 33.006 1.00 43.27 ? 530 PRO A C 1 ATOM 4248 O O . PRO A 1 514 ? 31.104 -27.714 32.488 1.00 42.96 ? 530 PRO A O 1 ATOM 4249 C CB . PRO A 1 514 ? 30.943 -24.646 33.230 1.00 40.43 ? 530 PRO A CB 1 ATOM 4250 C CG . PRO A 1 514 ? 30.141 -23.948 34.275 1.00 41.01 ? 530 PRO A CG 1 ATOM 4251 C CD . PRO A 1 514 ? 28.741 -23.866 33.747 1.00 39.93 ? 530 PRO A CD 1 ATOM 4252 N N . ASP A 1 515 ? 29.411 -27.525 33.963 1.00 45.82 ? 531 ASP A N 1 ATOM 4253 C CA . ASP A 1 515 ? 29.555 -28.891 34.491 1.00 47.92 ? 531 ASP A CA 1 ATOM 4254 C C . ASP A 1 515 ? 28.510 -29.853 33.928 1.00 48.09 ? 531 ASP A C 1 ATOM 4255 O O . ASP A 1 515 ? 28.438 -31.015 34.329 1.00 49.95 ? 531 ASP A O 1 ATOM 4256 C CB . ASP A 1 515 ? 29.505 -28.883 36.024 1.00 49.97 ? 531 ASP A CB 1 ATOM 4257 C CG . ASP A 1 515 ? 30.587 -28.008 36.639 1.00 51.82 ? 531 ASP A CG 1 ATOM 4258 O OD1 . ASP A 1 515 ? 31.765 -28.125 36.233 1.00 52.95 ? 531 ASP A OD1 1 ATOM 4259 O OD2 . ASP A 1 515 ? 30.260 -27.200 37.532 1.00 52.85 ? 531 ASP A OD2 1 ATOM 4260 N N . ASN A 1 516 ? 27.704 -29.366 32.993 1.00 46.46 ? 532 ASN A N 1 ATOM 4261 C CA . ASN A 1 516 ? 26.676 -30.182 32.381 1.00 45.53 ? 532 ASN A CA 1 ATOM 4262 C C . ASN A 1 516 ? 26.943 -30.360 30.893 1.00 45.23 ? 532 ASN A C 1 ATOM 4263 O O . ASN A 1 516 ? 26.770 -29.425 30.101 1.00 43.57 ? 532 ASN A O 1 ATOM 4264 C CB . ASN A 1 516 ? 25.297 -29.567 32.625 1.00 45.36 ? 532 ASN A CB 1 ATOM 4265 C CG . ASN A 1 516 ? 24.163 -30.454 32.146 1.00 45.78 ? 532 ASN A CG 1 ATOM 4266 O OD1 . ASN A 1 516 ? 24.378 -31.451 31.456 1.00 45.92 ? 532 ASN A OD1 1 ATOM 4267 N ND2 . ASN A 1 516 ? 22.941 -30.089 32.514 1.00 45.90 ? 532 ASN A ND2 1 ATOM 4268 N N . VAL A 1 517 ? 27.361 -31.572 30.530 1.00 44.87 ? 533 VAL A N 1 ATOM 4269 C CA . VAL A 1 517 ? 27.645 -31.954 29.139 1.00 44.49 ? 533 VAL A CA 1 ATOM 4270 C C . VAL A 1 517 ? 26.456 -31.666 28.203 1.00 44.37 ? 533 VAL A C 1 ATOM 4271 O O . VAL A 1 517 ? 26.632 -31.454 27.006 1.00 44.40 ? 533 VAL A O 1 ATOM 4272 C CB . VAL A 1 517 ? 28.085 -33.442 29.056 1.00 46.04 ? 533 VAL A CB 1 ATOM 4273 C CG1 . VAL A 1 517 ? 28.180 -33.930 27.613 1.00 46.21 ? 533 VAL A CG1 1 ATOM 4274 C CG2 . VAL A 1 517 ? 29.419 -33.645 29.765 1.00 45.53 ? 533 VAL A CG2 1 ATOM 4275 N N . GLU A 1 518 ? 25.254 -31.632 28.766 1.00 44.80 ? 534 GLU A N 1 ATOM 4276 C CA . GLU A 1 518 ? 24.038 -31.364 28.002 1.00 45.43 ? 534 GLU A CA 1 ATOM 4277 C C . GLU A 1 518 ? 23.798 -29.878 27.717 1.00 42.02 ? 534 GLU A C 1 ATOM 4278 O O . GLU A 1 518 ? 22.945 -29.534 26.901 1.00 41.25 ? 534 GLU A O 1 ATOM 4279 C CB . GLU A 1 518 ? 22.819 -31.954 28.725 1.00 48.89 ? 534 GLU A CB 1 ATOM 4280 C CG . GLU A 1 518 ? 22.870 -33.465 28.898 1.00 53.75 ? 534 GLU A CG 1 ATOM 4281 C CD . GLU A 1 518 ? 22.933 -34.190 27.568 1.00 57.20 ? 534 GLU A CD 1 ATOM 4282 O OE1 . GLU A 1 518 ? 21.909 -34.204 26.848 1.00 60.52 ? 534 GLU A OE1 1 ATOM 4283 O OE2 . GLU A 1 518 ? 24.009 -34.739 27.243 1.00 59.82 ? 534 GLU A OE2 1 ATOM 4284 N N . LEU A 1 519 ? 24.541 -29.000 28.384 1.00 39.74 ? 535 LEU A N 1 ATOM 4285 C CA . LEU A 1 519 ? 24.339 -27.558 28.215 1.00 37.94 ? 535 LEU A CA 1 ATOM 4286 C C . LEU A 1 519 ? 25.635 -26.825 27.835 1.00 36.26 ? 535 LEU A C 1 ATOM 4287 O O . LEU A 1 519 ? 26.117 -25.988 28.602 1.00 36.43 ? 535 LEU A O 1 ATOM 4288 C CB . LEU A 1 519 ? 23.710 -26.951 29.485 1.00 38.48 ? 535 LEU A CB 1 ATOM 4289 C CG . LEU A 1 519 ? 22.351 -27.482 29.979 1.00 39.54 ? 535 LEU A CG 1 ATOM 4290 C CD1 . LEU A 1 519 ? 22.065 -27.030 31.407 1.00 39.61 ? 535 LEU A CD1 1 ATOM 4291 C CD2 . LEU A 1 519 ? 21.210 -27.079 29.054 1.00 39.49 ? 535 LEU A CD2 1 ATOM 4292 N N . PRO A 1 520 ? 26.206 -27.139 26.649 1.00 34.69 ? 536 PRO A N 1 ATOM 4293 C CA . PRO A 1 520 ? 27.442 -26.472 26.207 1.00 33.25 ? 536 PRO A CA 1 ATOM 4294 C C . PRO A 1 520 ? 27.181 -25.040 25.734 1.00 31.18 ? 536 PRO A C 1 ATOM 4295 O O . PRO A 1 520 ? 26.109 -24.751 25.198 1.00 31.56 ? 536 PRO A O 1 ATOM 4296 C CB . PRO A 1 520 ? 27.905 -27.344 25.032 1.00 32.70 ? 536 PRO A CB 1 ATOM 4297 C CG . PRO A 1 520 ? 26.640 -27.892 24.461 1.00 33.64 ? 536 PRO A CG 1 ATOM 4298 C CD . PRO A 1 520 ? 25.689 -28.067 25.622 1.00 34.56 ? 536 PRO A CD 1 ATOM 4299 N N . LEU A 1 521 ? 28.153 -24.151 25.911 1.00 30.02 ? 537 LEU A N 1 ATOM 4300 C CA . LEU A 1 521 ? 27.938 -22.739 25.585 1.00 28.57 ? 537 LEU A CA 1 ATOM 4301 C C . LEU A 1 521 ? 27.695 -22.551 24.085 1.00 28.67 ? 537 LEU A C 1 ATOM 4302 O O . LEU A 1 521 ? 26.892 -21.704 23.672 1.00 27.47 ? 537 LEU A O 1 ATOM 4303 C CB . LEU A 1 521 ? 29.114 -21.884 26.076 1.00 28.37 ? 537 LEU A CB 1 ATOM 4304 C CG . LEU A 1 521 ? 29.020 -20.355 25.971 1.00 27.76 ? 537 LEU A CG 1 ATOM 4305 C CD1 . LEU A 1 521 ? 27.730 -19.791 26.554 1.00 28.05 ? 537 LEU A CD1 1 ATOM 4306 C CD2 . LEU A 1 521 ? 30.231 -19.728 26.643 1.00 27.37 ? 537 LEU A CD2 1 ATOM 4307 N N . ASP A 1 522 ? 28.366 -23.376 23.283 1.00 28.12 ? 538 ASP A N 1 ATOM 4308 C CA . ASP A 1 522 ? 28.265 -23.291 21.821 1.00 28.55 ? 538 ASP A CA 1 ATOM 4309 C C . ASP A 1 522 ? 26.955 -23.850 21.223 1.00 29.31 ? 538 ASP A C 1 ATOM 4310 O O . ASP A 1 522 ? 26.788 -23.864 20.005 1.00 29.75 ? 538 ASP A O 1 ATOM 4311 C CB . ASP A 1 522 ? 29.491 -23.937 21.158 1.00 27.93 ? 538 ASP A CB 1 ATOM 4312 C CG . ASP A 1 522 ? 29.808 -25.319 21.728 1.00 28.33 ? 538 ASP A CG 1 ATOM 4313 O OD1 . ASP A 1 522 ? 30.199 -25.405 22.903 1.00 28.64 ? 538 ASP A OD1 1 ATOM 4314 O OD2 . ASP A 1 522 ? 29.690 -26.317 20.995 1.00 28.81 ? 538 ASP A OD2 1 ATOM 4315 N N . ASN A 1 523 ? 26.031 -24.318 22.059 1.00 30.19 ? 539 ASN A N 1 ATOM 4316 C CA . ASN A 1 523 ? 24.691 -24.649 21.567 1.00 30.06 ? 539 ASN A CA 1 ATOM 4317 C C . ASN A 1 523 ? 23.566 -23.917 22.323 1.00 30.91 ? 539 ASN A C 1 ATOM 4318 O O . ASN A 1 523 ? 22.416 -24.369 22.341 1.00 31.54 ? 539 ASN A O 1 ATOM 4319 C CB . ASN A 1 523 ? 24.465 -26.170 21.545 1.00 30.31 ? 539 ASN A CB 1 ATOM 4320 C CG . ASN A 1 523 ? 23.541 -26.606 20.414 1.00 30.93 ? 539 ASN A CG 1 ATOM 4321 O OD1 . ASN A 1 523 ? 23.511 -25.993 19.342 1.00 30.78 ? 539 ASN A OD1 1 ATOM 4322 N ND2 . ASN A 1 523 ? 22.782 -27.668 20.647 1.00 31.00 ? 539 ASN A ND2 1 ATOM 4323 N N . CYS A 1 524 ? 23.896 -22.778 22.931 1.00 30.67 ? 540 CYS A N 1 ATOM 4324 C CA . CYS A 1 524 ? 22.919 -22.028 23.726 1.00 31.08 ? 540 CYS A CA 1 ATOM 4325 C C . CYS A 1 524 ? 21.939 -21.244 22.847 1.00 31.11 ? 540 CYS A C 1 ATOM 4326 O O . CYS A 1 524 ? 22.355 -20.502 21.950 1.00 30.45 ? 540 CYS A O 1 ATOM 4327 C CB . CYS A 1 524 ? 23.635 -21.099 24.711 1.00 30.72 ? 540 CYS A CB 1 ATOM 4328 S SG . CYS A 1 524 ? 22.644 -19.687 25.261 1.00 32.21 ? 540 CYS A SG 1 ATOM 4329 N N . ASP A 1 525 ? 20.642 -21.418 23.102 1.00 30.30 ? 541 ASP A N 1 ATOM 4330 C CA . ASP A 1 525 ? 19.618 -20.624 22.423 1.00 30.55 ? 541 ASP A CA 1 ATOM 4331 C C . ASP A 1 525 ? 18.851 -19.796 23.448 1.00 30.91 ? 541 ASP A C 1 ATOM 4332 O O . ASP A 1 525 ? 18.079 -20.342 24.248 1.00 30.98 ? 541 ASP A O 1 ATOM 4333 C CB . ASP A 1 525 ? 18.657 -21.516 21.612 1.00 30.79 ? 541 ASP A CB 1 ATOM 4334 C CG . ASP A 1 525 ? 17.733 -20.715 20.682 1.00 31.02 ? 541 ASP A CG 1 ATOM 4335 O OD1 . ASP A 1 525 ? 17.874 -19.471 20.591 1.00 29.70 ? 541 ASP A OD1 1 ATOM 4336 O OD2 . ASP A 1 525 ? 16.854 -21.341 20.033 1.00 30.66 ? 541 ASP A OD2 1 ATOM 4337 N N . ILE A 1 526 ? 19.070 -18.482 23.427 1.00 30.06 ? 542 ILE A N 1 ATOM 4338 C CA . ILE A 1 526 ? 18.356 -17.576 24.333 1.00 29.66 ? 542 ILE A CA 1 ATOM 4339 C C . ILE A 1 526 ? 16.962 -17.155 23.825 1.00 29.93 ? 542 ILE A C 1 ATOM 4340 O O . ILE A 1 526 ? 16.290 -16.350 24.475 1.00 29.33 ? 542 ILE A O 1 ATOM 4341 C CB . ILE A 1 526 ? 19.208 -16.329 24.734 1.00 29.13 ? 542 ILE A CB 1 ATOM 4342 C CG1 . ILE A 1 526 ? 19.520 -15.447 23.517 1.00 28.15 ? 542 ILE A CG1 1 ATOM 4343 C CG2 . ILE A 1 526 ? 20.468 -16.749 25.489 1.00 28.82 ? 542 ILE A CG2 1 ATOM 4344 C CD1 . ILE A 1 526 ? 20.139 -14.100 23.849 1.00 27.64 ? 542 ILE A CD1 1 ATOM 4345 N N . TYR A 1 527 ? 16.528 -17.690 22.677 1.00 29.85 ? 543 TYR A N 1 ATOM 4346 C CA . TYR A 1 527 ? 15.180 -17.401 22.166 1.00 30.27 ? 543 TYR A CA 1 ATOM 4347 C C . TYR A 1 527 ? 14.161 -17.653 23.273 1.00 30.99 ? 543 TYR A C 1 ATOM 4348 O O . TYR A 1 527 ? 14.251 -18.656 23.976 1.00 30.92 ? 543 TYR A O 1 ATOM 4349 C CB . TYR A 1 527 ? 14.824 -18.241 20.920 1.00 29.96 ? 543 TYR A CB 1 ATOM 4350 C CG . TYR A 1 527 ? 13.432 -17.934 20.376 1.00 30.13 ? 543 TYR A CG 1 ATOM 4351 C CD1 . TYR A 1 527 ? 13.233 -16.878 19.487 1.00 30.21 ? 543 TYR A CD1 1 ATOM 4352 C CD2 . TYR A 1 527 ? 12.306 -18.680 20.773 1.00 30.81 ? 543 TYR A CD2 1 ATOM 4353 C CE1 . TYR A 1 527 ? 11.970 -16.569 19.002 1.00 30.13 ? 543 TYR A CE1 1 ATOM 4354 C CE2 . TYR A 1 527 ? 11.033 -18.372 20.298 1.00 30.76 ? 543 TYR A CE2 1 ATOM 4355 C CZ . TYR A 1 527 ? 10.876 -17.316 19.409 1.00 31.44 ? 543 TYR A CZ 1 ATOM 4356 O OH . TYR A 1 527 ? 9.637 -16.983 18.907 1.00 31.89 ? 543 TYR A OH 1 ATOM 4357 N N . GLY A 1 528 ? 13.229 -16.718 23.446 1.00 31.35 ? 544 GLY A N 1 ATOM 4358 C CA . GLY A 1 528 ? 12.133 -16.893 24.393 1.00 32.44 ? 544 GLY A CA 1 ATOM 4359 C C . GLY A 1 528 ? 12.461 -16.654 25.858 1.00 32.71 ? 544 GLY A C 1 ATOM 4360 O O . GLY A 1 528 ? 11.591 -16.816 26.713 1.00 33.23 ? 544 GLY A O 1 ATOM 4361 N N . SER A 1 529 ? 13.698 -16.257 26.160 1.00 31.62 ? 545 SER A N 1 ATOM 4362 C CA . SER A 1 529 ? 14.106 -16.060 27.556 1.00 31.76 ? 545 SER A CA 1 ATOM 4363 C C . SER A 1 529 ? 13.844 -14.638 28.068 1.00 31.52 ? 545 SER A C 1 ATOM 4364 O O . SER A 1 529 ? 14.515 -13.686 27.657 1.00 30.76 ? 545 SER A O 1 ATOM 4365 C CB . SER A 1 529 ? 15.574 -16.455 27.754 1.00 31.36 ? 545 SER A CB 1 ATOM 4366 O OG . SER A 1 529 ? 16.046 -16.091 29.041 1.00 32.05 ? 545 SER A OG 1 ATOM 4367 N N . ALA A 1 530 ? 12.863 -14.508 28.967 1.00 31.84 ? 546 ALA A N 1 ATOM 4368 C CA . ALA A 1 530 ? 12.572 -13.237 29.651 1.00 31.59 ? 546 ALA A CA 1 ATOM 4369 C C . ALA A 1 530 ? 13.674 -12.838 30.647 1.00 31.33 ? 546 ALA A C 1 ATOM 4370 O O . ALA A 1 530 ? 13.913 -11.651 30.866 1.00 30.66 ? 546 ALA A O 1 ATOM 4371 C CB . ALA A 1 530 ? 11.215 -13.291 30.347 1.00 32.45 ? 546 ALA A CB 1 ATOM 4372 N N . ALA A 1 531 ? 14.332 -13.831 31.244 1.00 31.64 ? 547 ALA A N 1 ATOM 4373 C CA . ALA A 1 531 ? 15.495 -13.595 32.109 1.00 31.90 ? 547 ALA A CA 1 ATOM 4374 C C . ALA A 1 531 ? 16.649 -12.896 31.364 1.00 31.77 ? 547 ALA A C 1 ATOM 4375 O O . ALA A 1 531 ? 17.196 -11.897 31.853 1.00 31.94 ? 547 ALA A O 1 ATOM 4376 C CB . ALA A 1 531 ? 15.972 -14.898 32.722 1.00 31.91 ? 547 ALA A CB 1 ATOM 4377 N N . ALA A 1 532 ? 16.999 -13.407 30.181 1.00 31.23 ? 548 ALA A N 1 ATOM 4378 C CA . ALA A 1 532 ? 18.034 -12.786 29.345 1.00 30.60 ? 548 ALA A CA 1 ATOM 4379 C C . ALA A 1 532 ? 17.604 -11.384 28.916 1.00 30.14 ? 548 ALA A C 1 ATOM 4380 O O . ALA A 1 532 ? 18.401 -10.443 28.962 1.00 29.48 ? 548 ALA A O 1 ATOM 4381 C CB . ALA A 1 532 ? 18.347 -13.654 28.126 1.00 30.00 ? 548 ALA A CB 1 ATOM 4382 N N . GLY A 1 533 ? 16.339 -11.258 28.512 1.00 29.93 ? 549 GLY A N 1 ATOM 4383 C CA . GLY A 1 533 ? 15.757 -9.981 28.101 1.00 29.65 ? 549 GLY A CA 1 ATOM 4384 C C . GLY A 1 533 ? 15.803 -8.901 29.175 1.00 29.78 ? 549 GLY A C 1 ATOM 4385 O O . GLY A 1 533 ? 16.065 -7.729 28.871 1.00 29.10 ? 549 GLY A O 1 ATOM 4386 N N . ALA A 1 534 ? 15.555 -9.300 30.425 1.00 29.29 ? 550 ALA A N 1 ATOM 4387 C CA . ALA A 1 534 ? 15.610 -8.384 31.562 1.00 29.43 ? 550 ALA A CA 1 ATOM 4388 C C . ALA A 1 534 ? 16.997 -7.770 31.745 1.00 28.84 ? 550 ALA A C 1 ATOM 4389 O O . ALA A 1 534 ? 17.111 -6.573 32.020 1.00 29.01 ? 550 ALA A O 1 ATOM 4390 C CB . ALA A 1 534 ? 15.169 -9.087 32.840 1.00 29.49 ? 550 ALA A CB 1 ATOM 4391 N N . ALA A 1 535 ? 18.038 -8.591 31.603 1.00 28.47 ? 551 ALA A N 1 ATOM 4392 C CA . ALA A 1 535 ? 19.415 -8.118 31.679 1.00 27.84 ? 551 ALA A CA 1 ATOM 4393 C C . ALA A 1 535 ? 19.695 -7.063 30.597 1.00 27.55 ? 551 ALA A C 1 ATOM 4394 O O . ALA A 1 535 ? 20.269 -6.006 30.892 1.00 26.95 ? 551 ALA A O 1 ATOM 4395 C CB . ALA A 1 535 ? 20.392 -9.283 31.586 1.00 27.99 ? 551 ALA A CB 1 ATOM 4396 N N . PHE A 1 536 ? 19.267 -7.344 29.361 1.00 27.48 ? 552 PHE A N 1 ATOM 4397 C CA . PHE A 1 536 ? 19.339 -6.376 28.263 1.00 27.72 ? 552 PHE A CA 1 ATOM 4398 C C . PHE A 1 536 ? 18.571 -5.088 28.542 1.00 27.50 ? 552 PHE A C 1 ATOM 4399 O O . PHE A 1 536 ? 19.090 -3.999 28.310 1.00 26.55 ? 552 PHE A O 1 ATOM 4400 C CB . PHE A 1 536 ? 18.861 -6.985 26.938 1.00 29.13 ? 552 PHE A CB 1 ATOM 4401 C CG . PHE A 1 536 ? 19.922 -7.766 26.220 1.00 30.00 ? 552 PHE A CG 1 ATOM 4402 C CD1 . PHE A 1 536 ? 20.943 -7.108 25.536 1.00 30.74 ? 552 PHE A CD1 1 ATOM 4403 C CD2 . PHE A 1 536 ? 19.912 -9.159 26.236 1.00 30.38 ? 552 PHE A CD2 1 ATOM 4404 C CE1 . PHE A 1 536 ? 21.934 -7.828 24.874 1.00 30.75 ? 552 PHE A CE1 1 ATOM 4405 C CE2 . PHE A 1 536 ? 20.899 -9.884 25.577 1.00 30.82 ? 552 PHE A CE2 1 ATOM 4406 C CZ . PHE A 1 536 ? 21.912 -9.218 24.898 1.00 30.69 ? 552 PHE A CZ 1 ATOM 4407 N N . HIS A 1 537 ? 17.343 -5.205 29.045 1.00 27.66 ? 553 HIS A N 1 ATOM 4408 C CA . HIS A 1 537 ? 16.584 -4.012 29.405 1.00 28.01 ? 553 HIS A CA 1 ATOM 4409 C C . HIS A 1 537 ? 17.326 -3.165 30.455 1.00 27.82 ? 553 HIS A C 1 ATOM 4410 O O . HIS A 1 537 ? 17.480 -1.962 30.274 1.00 27.41 ? 553 HIS A O 1 ATOM 4411 C CB . HIS A 1 537 ? 15.167 -4.349 29.878 1.00 29.02 ? 553 HIS A CB 1 ATOM 4412 C CG . HIS A 1 537 ? 14.441 -3.174 30.454 1.00 29.78 ? 553 HIS A CG 1 ATOM 4413 N ND1 . HIS A 1 537 ? 14.071 -2.084 29.695 1.00 29.78 ? 553 HIS A ND1 1 ATOM 4414 C CD2 . HIS A 1 537 ? 14.037 -2.906 31.720 1.00 30.61 ? 553 HIS A CD2 1 ATOM 4415 C CE1 . HIS A 1 537 ? 13.455 -1.202 30.464 1.00 31.02 ? 553 HIS A CE1 1 ATOM 4416 N NE2 . HIS A 1 537 ? 13.423 -1.676 31.698 1.00 31.03 ? 553 HIS A NE2 1 ATOM 4417 N N . ASN A 1 538 ? 17.800 -3.799 31.528 1.00 28.66 ? 554 ASN A N 1 ATOM 4418 C CA . ASN A 1 538 ? 18.540 -3.097 32.586 1.00 29.12 ? 554 ASN A CA 1 ATOM 4419 C C . ASN A 1 538 ? 19.742 -2.313 32.052 1.00 28.35 ? 554 ASN A C 1 ATOM 4420 O O . ASN A 1 538 ? 19.994 -1.190 32.482 1.00 27.96 ? 554 ASN A O 1 ATOM 4421 C CB . ASN A 1 538 ? 19.002 -4.070 33.682 1.00 30.40 ? 554 ASN A CB 1 ATOM 4422 C CG . ASN A 1 538 ? 17.845 -4.656 34.473 1.00 32.44 ? 554 ASN A CG 1 ATOM 4423 O OD1 . ASN A 1 538 ? 16.784 -4.046 34.595 1.00 34.26 ? 554 ASN A OD1 1 ATOM 4424 N ND2 . ASN A 1 538 ? 18.047 -5.847 35.020 1.00 33.95 ? 554 ASN A ND2 1 ATOM 4425 N N . MET A 1 539 ? 20.465 -2.905 31.103 1.00 26.59 ? 555 MET A N 1 ATOM 4426 C CA . MET A 1 539 ? 21.664 -2.290 30.557 1.00 25.76 ? 555 MET A CA 1 ATOM 4427 C C . MET A 1 539 ? 21.345 -1.246 29.491 1.00 25.19 ? 555 MET A C 1 ATOM 4428 O O . MET A 1 539 ? 21.817 -0.106 29.573 1.00 24.32 ? 555 MET A O 1 ATOM 4429 C CB . MET A 1 539 ? 22.613 -3.359 29.998 1.00 25.47 ? 555 MET A CB 1 ATOM 4430 C CG . MET A 1 539 ? 23.881 -2.803 29.363 1.00 25.66 ? 555 MET A CG 1 ATOM 4431 S SD . MET A 1 539 ? 25.028 -4.094 28.850 1.00 25.85 ? 555 MET A SD 1 ATOM 4432 C CE . MET A 1 539 ? 24.259 -4.630 27.315 1.00 25.62 ? 555 MET A CE 1 ATOM 4433 N N . LEU A 1 540 ? 20.564 -1.638 28.481 1.00 24.38 ? 556 LEU A N 1 ATOM 4434 C CA . LEU A 1 540 ? 20.343 -0.773 27.327 1.00 24.18 ? 556 LEU A CA 1 ATOM 4435 C C . LEU A 1 540 ? 19.560 0.493 27.666 1.00 24.19 ? 556 LEU A C 1 ATOM 4436 O O . LEU A 1 540 ? 19.783 1.539 27.055 1.00 24.35 ? 556 LEU A O 1 ATOM 4437 C CB . LEU A 1 540 ? 19.660 -1.522 26.177 1.00 23.55 ? 556 LEU A CB 1 ATOM 4438 C CG . LEU A 1 540 ? 20.315 -2.800 25.625 1.00 23.61 ? 556 LEU A CG 1 ATOM 4439 C CD1 . LEU A 1 540 ? 19.488 -3.345 24.467 1.00 23.17 ? 556 LEU A CD1 1 ATOM 4440 C CD2 . LEU A 1 540 ? 21.763 -2.583 25.201 1.00 22.95 ? 556 LEU A CD2 1 ATOM 4441 N N . SER A 1 541 ? 18.645 0.403 28.627 1.00 24.35 ? 557 SER A N 1 ATOM 4442 C CA . SER A 1 541 ? 17.807 1.560 28.971 1.00 24.73 ? 557 SER A CA 1 ATOM 4443 C C . SER A 1 541 ? 18.629 2.713 29.572 1.00 24.41 ? 557 SER A C 1 ATOM 4444 O O . SER A 1 541 ? 18.168 3.858 29.620 1.00 24.24 ? 557 SER A O 1 ATOM 4445 C CB . SER A 1 541 ? 16.672 1.152 29.909 1.00 25.19 ? 557 SER A CB 1 ATOM 4446 O OG . SER A 1 541 ? 17.195 0.674 31.136 1.00 25.75 ? 557 SER A OG 1 ATOM 4447 N N . MET A 1 542 ? 19.847 2.393 30.009 1.00 24.33 ? 558 MET A N 1 ATOM 4448 C CA . MET A 1 542 ? 20.776 3.377 30.581 1.00 24.88 ? 558 MET A CA 1 ATOM 4449 C C . MET A 1 542 ? 21.378 4.321 29.541 1.00 24.20 ? 558 MET A C 1 ATOM 4450 O O . MET A 1 542 ? 21.813 5.428 29.879 1.00 24.31 ? 558 MET A O 1 ATOM 4451 C CB . MET A 1 542 ? 21.909 2.659 31.323 1.00 25.23 ? 558 MET A CB 1 ATOM 4452 C CG . MET A 1 542 ? 21.483 2.003 32.635 1.00 26.23 ? 558 MET A CG 1 ATOM 4453 S SD . MET A 1 542 ? 22.822 1.003 33.317 1.00 28.05 ? 558 MET A SD 1 ATOM 4454 C CE . MET A 1 542 ? 23.993 2.269 33.815 1.00 26.05 ? 558 MET A CE 1 ATOM 4455 N N . GLY A 1 543 ? 21.411 3.890 28.283 1.00 23.48 ? 559 GLY A N 1 ATOM 4456 C CA . GLY A 1 543 ? 22.132 4.622 27.236 1.00 22.80 ? 559 GLY A CA 1 ATOM 4457 C C . GLY A 1 543 ? 23.547 4.967 27.697 1.00 22.96 ? 559 GLY A C 1 ATOM 4458 O O . GLY A 1 543 ? 24.278 4.108 28.209 1.00 21.97 ? 559 GLY A O 1 ATOM 4459 N N . ALA A 1 544 ? 23.920 6.236 27.553 1.00 23.20 ? 560 ALA A N 1 ATOM 4460 C CA . ALA A 1 544 ? 25.242 6.699 27.976 1.00 22.93 ? 560 ALA A CA 1 ATOM 4461 C C . ALA A 1 544 ? 25.169 7.543 29.254 1.00 23.92 ? 560 ALA A C 1 ATOM 4462 O O . ALA A 1 544 ? 26.049 8.379 29.508 1.00 23.23 ? 560 ALA A O 1 ATOM 4463 C CB . ALA A 1 544 ? 25.915 7.477 26.851 1.00 23.73 ? 560 ALA A CB 1 ATOM 4464 N N . SER A 1 545 ? 24.121 7.317 30.055 1.00 23.94 ? 561 SER A N 1 ATOM 4465 C CA . SER A 1 545 ? 23.922 8.050 31.313 1.00 24.47 ? 561 SER A CA 1 ATOM 4466 C C . SER A 1 545 ? 25.008 7.791 32.365 1.00 25.18 ? 561 SER A C 1 ATOM 4467 O O . SER A 1 545 ? 25.204 8.607 33.270 1.00 25.23 ? 561 SER A O 1 ATOM 4468 C CB . SER A 1 545 ? 22.537 7.761 31.900 1.00 24.37 ? 561 SER A CB 1 ATOM 4469 O OG . SER A 1 545 ? 22.366 6.376 32.159 1.00 23.97 ? 561 SER A OG 1 ATOM 4470 N N . LYS A 1 546 ? 25.692 6.654 32.251 1.00 25.50 ? 562 LYS A N 1 ATOM 4471 C CA . LYS A 1 546 ? 26.751 6.260 33.188 1.00 26.38 ? 562 LYS A CA 1 ATOM 4472 C C . LYS A 1 546 ? 27.981 5.745 32.431 1.00 25.19 ? 562 LYS A C 1 ATOM 4473 O O . LYS A 1 546 ? 27.850 5.242 31.296 1.00 25.05 ? 562 LYS A O 1 ATOM 4474 C CB . LYS A 1 546 ? 26.249 5.181 34.154 1.00 27.72 ? 562 LYS A CB 1 ATOM 4475 C CG . LYS A 1 546 ? 25.191 5.625 35.155 1.00 30.77 ? 562 LYS A CG 1 ATOM 4476 C CD . LYS A 1 546 ? 25.850 6.213 36.398 1.00 33.44 ? 562 LYS A CD 1 ATOM 4477 C CE . LYS A 1 546 ? 24.847 6.460 37.509 1.00 36.76 ? 562 LYS A CE 1 ATOM 4478 N NZ . LYS A 1 546 ? 24.042 7.677 37.221 1.00 39.31 ? 562 LYS A NZ 1 ATOM 4479 N N . PRO A 1 547 ? 29.186 5.872 33.040 1.00 24.64 ? 563 PRO A N 1 ATOM 4480 C CA . PRO A 1 547 ? 30.377 5.268 32.421 1.00 23.92 ? 563 PRO A CA 1 ATOM 4481 C C . PRO A 1 547 ? 30.129 3.774 32.146 1.00 23.24 ? 563 PRO A C 1 ATOM 4482 O O . PRO A 1 547 ? 29.423 3.108 32.911 1.00 22.46 ? 563 PRO A O 1 ATOM 4483 C CB . PRO A 1 547 ? 31.470 5.461 33.484 1.00 24.62 ? 563 PRO A CB 1 ATOM 4484 C CG . PRO A 1 547 ? 30.998 6.593 34.331 1.00 24.68 ? 563 PRO A CG 1 ATOM 4485 C CD . PRO A 1 547 ? 29.499 6.496 34.342 1.00 24.68 ? 563 PRO A CD 1 ATOM 4486 N N . TRP A 1 548 ? 30.679 3.262 31.046 1.00 22.31 ? 564 TRP A N 1 ATOM 4487 C CA . TRP A 1 548 ? 30.349 1.908 30.591 1.00 21.95 ? 564 TRP A CA 1 ATOM 4488 C C . TRP A 1 548 ? 30.523 0.760 31.597 1.00 22.32 ? 564 TRP A C 1 ATOM 4489 O O . TRP A 1 548 ? 29.776 -0.205 31.513 1.00 22.83 ? 564 TRP A O 1 ATOM 4490 C CB . TRP A 1 548 ? 31.015 1.578 29.246 1.00 20.44 ? 564 TRP A CB 1 ATOM 4491 C CG . TRP A 1 548 ? 32.503 1.401 29.296 1.00 19.84 ? 564 TRP A CG 1 ATOM 4492 C CD1 . TRP A 1 548 ? 33.451 2.339 28.985 1.00 19.29 ? 564 TRP A CD1 1 ATOM 4493 C CD2 . TRP A 1 548 ? 33.222 0.211 29.669 1.00 19.61 ? 564 TRP A CD2 1 ATOM 4494 N NE1 . TRP A 1 548 ? 34.706 1.817 29.162 1.00 19.02 ? 564 TRP A NE1 1 ATOM 4495 C CE2 . TRP A 1 548 ? 34.599 0.514 29.577 1.00 19.07 ? 564 TRP A CE2 1 ATOM 4496 C CE3 . TRP A 1 548 ? 32.833 -1.075 30.090 1.00 19.56 ? 564 TRP A CE3 1 ATOM 4497 C CZ2 . TRP A 1 548 ? 35.601 -0.426 29.873 1.00 19.20 ? 564 TRP A CZ2 1 ATOM 4498 C CZ3 . TRP A 1 548 ? 33.831 -2.015 30.389 1.00 19.69 ? 564 TRP A CZ3 1 ATOM 4499 C CH2 . TRP A 1 548 ? 35.203 -1.680 30.275 1.00 19.27 ? 564 TRP A CH2 1 ATOM 4500 N N . PRO A 1 549 ? 31.495 0.840 32.544 1.00 23.10 ? 565 PRO A N 1 ATOM 4501 C CA . PRO A 1 549 ? 31.528 -0.281 33.501 1.00 23.33 ? 565 PRO A CA 1 ATOM 4502 C C . PRO A 1 549 ? 30.252 -0.393 34.339 1.00 23.72 ? 565 PRO A C 1 ATOM 4503 O O . PRO A 1 549 ? 29.906 -1.496 34.787 1.00 22.92 ? 565 PRO A O 1 ATOM 4504 C CB . PRO A 1 549 ? 32.746 0.036 34.378 1.00 22.80 ? 565 PRO A CB 1 ATOM 4505 C CG . PRO A 1 549 ? 33.611 0.919 33.525 1.00 22.60 ? 565 PRO A CG 1 ATOM 4506 C CD . PRO A 1 549 ? 32.624 1.767 32.777 1.00 22.62 ? 565 PRO A CD 1 ATOM 4507 N N . ASP A 1 550 ? 29.558 0.732 34.527 1.00 24.71 ? 566 ASP A N 1 ATOM 4508 C CA . ASP A 1 550 ? 28.264 0.744 35.225 1.00 25.64 ? 566 ASP A CA 1 ATOM 4509 C C . ASP A 1 550 ? 27.183 0.043 34.418 1.00 25.74 ? 566 ASP A C 1 ATOM 4510 O O . ASP A 1 550 ? 26.272 -0.570 34.986 1.00 25.98 ? 566 ASP A O 1 ATOM 4511 C CB . ASP A 1 550 ? 27.806 2.170 35.537 1.00 27.28 ? 566 ASP A CB 1 ATOM 4512 C CG . ASP A 1 550 ? 28.646 2.841 36.621 1.00 28.91 ? 566 ASP A CG 1 ATOM 4513 O OD1 . ASP A 1 550 ? 29.239 2.138 37.460 1.00 30.12 ? 566 ASP A OD1 1 ATOM 4514 O OD2 . ASP A 1 550 ? 28.702 4.084 36.633 1.00 29.77 ? 566 ASP A OD2 1 ATOM 4515 N N . ALA A 1 551 ? 27.273 0.158 33.093 1.00 24.26 ? 567 ALA A N 1 ATOM 4516 C CA . ALA A 1 551 ? 26.326 -0.497 32.200 1.00 24.51 ? 567 ALA A CA 1 ATOM 4517 C C . ALA A 1 551 ? 26.554 -2.015 32.157 1.00 24.48 ? 567 ALA A C 1 ATOM 4518 O O . ALA A 1 551 ? 25.588 -2.780 32.139 1.00 24.81 ? 567 ALA A O 1 ATOM 4519 C CB . ALA A 1 551 ? 26.396 0.108 30.802 1.00 23.34 ? 567 ALA A CB 1 ATOM 4520 N N . LEU A 1 552 ? 27.817 -2.442 32.146 1.00 24.35 ? 568 LEU A N 1 ATOM 4521 C CA . LEU A 1 552 ? 28.142 -3.866 32.208 1.00 24.84 ? 568 LEU A CA 1 ATOM 4522 C C . LEU A 1 552 ? 27.660 -4.434 33.541 1.00 25.76 ? 568 LEU A C 1 ATOM 4523 O O . LEU A 1 552 ? 27.094 -5.531 33.601 1.00 25.45 ? 568 LEU A O 1 ATOM 4524 C CB . LEU A 1 552 ? 29.649 -4.095 32.040 1.00 24.99 ? 568 LEU A CB 1 ATOM 4525 C CG . LEU A 1 552 ? 30.175 -5.543 32.085 1.00 25.67 ? 568 LEU A CG 1 ATOM 4526 C CD1 . LEU A 1 552 ? 29.518 -6.434 31.034 1.00 25.60 ? 568 LEU A CD1 1 ATOM 4527 C CD2 . LEU A 1 552 ? 31.694 -5.567 31.937 1.00 24.88 ? 568 LEU A CD2 1 ATOM 4528 N N . GLU A 1 553 ? 27.872 -3.670 34.606 1.00 25.89 ? 569 GLU A N 1 ATOM 4529 C CA . GLU A 1 553 ? 27.431 -4.096 35.934 1.00 27.19 ? 569 GLU A CA 1 ATOM 4530 C C . GLU A 1 553 ? 25.921 -4.339 35.998 1.00 27.38 ? 569 GLU A C 1 ATOM 4531 O O . GLU A 1 553 ? 25.480 -5.326 36.583 1.00 27.86 ? 569 GLU A O 1 ATOM 4532 C CB . GLU A 1 553 ? 27.858 -3.087 36.992 1.00 28.67 ? 569 GLU A CB 1 ATOM 4533 C CG . GLU A 1 553 ? 27.823 -3.665 38.403 1.00 31.12 ? 569 GLU A CG 1 ATOM 4534 C CD . GLU A 1 553 ? 28.383 -2.721 39.447 1.00 33.06 ? 569 GLU A CD 1 ATOM 4535 O OE1 . GLU A 1 553 ? 28.875 -1.638 39.087 1.00 33.62 ? 569 GLU A OE1 1 ATOM 4536 O OE2 . GLU A 1 553 ? 28.334 -3.069 40.643 1.00 35.00 ? 569 GLU A OE2 1 ATOM 4537 N N . ALA A 1 554 ? 25.145 -3.444 35.390 1.00 27.39 ? 570 ALA A N 1 ATOM 4538 C CA . ALA A 1 554 ? 23.691 -3.598 35.283 1.00 28.02 ? 570 ALA A CA 1 ATOM 4539 C C . ALA A 1 554 ? 23.295 -4.907 34.584 1.00 28.05 ? 570 ALA A C 1 ATOM 4540 O O . ALA A 1 554 ? 22.255 -5.486 34.902 1.00 28.36 ? 570 ALA A O 1 ATOM 4541 C CB . ALA A 1 554 ? 23.079 -2.404 34.565 1.00 27.37 ? 570 ALA A CB 1 ATOM 4542 N N . PHE A 1 555 ? 24.128 -5.371 33.652 1.00 27.14 ? 571 PHE A N 1 ATOM 4543 C CA . PHE A 1 555 ? 23.854 -6.610 32.923 1.00 27.64 ? 571 PHE A CA 1 ATOM 4544 C C . PHE A 1 555 ? 24.159 -7.874 33.742 1.00 27.93 ? 571 PHE A C 1 ATOM 4545 O O . PHE A 1 555 ? 23.288 -8.746 33.880 1.00 27.99 ? 571 PHE A O 1 ATOM 4546 C CB . PHE A 1 555 ? 24.598 -6.639 31.577 1.00 26.97 ? 571 PHE A CB 1 ATOM 4547 C CG . PHE A 1 555 ? 24.116 -7.713 30.628 1.00 27.28 ? 571 PHE A CG 1 ATOM 4548 C CD1 . PHE A 1 555 ? 24.629 -9.012 30.690 1.00 27.84 ? 571 PHE A CD1 1 ATOM 4549 C CD2 . PHE A 1 555 ? 23.157 -7.426 29.659 1.00 27.50 ? 571 PHE A CD2 1 ATOM 4550 C CE1 . PHE A 1 555 ? 24.178 -10.002 29.821 1.00 27.52 ? 571 PHE A CE1 1 ATOM 4551 C CE2 . PHE A 1 555 ? 22.714 -8.406 28.776 1.00 27.79 ? 571 PHE A CE2 1 ATOM 4552 C CZ . PHE A 1 555 ? 23.225 -9.696 28.857 1.00 27.63 ? 571 PHE A CZ 1 ATOM 4553 N N . ASN A 1 556 ? 25.375 -7.970 34.282 1.00 27.86 ? 572 ASN A N 1 ATOM 4554 C CA . ASN A 1 556 ? 25.823 -9.205 34.935 1.00 29.20 ? 572 ASN A CA 1 ATOM 4555 C C . ASN A 1 556 ? 26.677 -9.038 36.193 1.00 29.40 ? 572 ASN A C 1 ATOM 4556 O O . ASN A 1 556 ? 27.333 -9.988 36.619 1.00 29.56 ? 572 ASN A O 1 ATOM 4557 C CB . ASN A 1 556 ? 26.559 -10.106 33.927 1.00 28.43 ? 572 ASN A CB 1 ATOM 4558 C CG . ASN A 1 556 ? 27.908 -9.538 33.486 1.00 28.67 ? 572 ASN A CG 1 ATOM 4559 O OD1 . ASN A 1 556 ? 28.386 -8.523 34.007 1.00 28.03 ? 572 ASN A OD1 1 ATOM 4560 N ND2 . ASN A 1 556 ? 28.528 -10.198 32.506 1.00 27.94 ? 572 ASN A ND2 1 ATOM 4561 N N . GLY A 1 557 ? 26.705 -7.832 36.755 1.00 30.08 ? 573 GLY A N 1 ATOM 4562 C CA . GLY A 1 557 ? 27.480 -7.571 37.978 1.00 30.95 ? 573 GLY A CA 1 ATOM 4563 C C . GLY A 1 557 ? 28.987 -7.384 37.804 1.00 31.20 ? 573 GLY A C 1 ATOM 4564 O O . GLY A 1 557 ? 29.699 -7.153 38.777 1.00 31.44 ? 573 GLY A O 1 ATOM 4565 N N . GLU A 1 558 ? 29.481 -7.478 36.571 1.00 31.26 ? 574 GLU A N 1 ATOM 4566 C CA . GLU A 1 558 ? 30.918 -7.292 36.295 1.00 31.09 ? 574 GLU A CA 1 ATOM 4567 C C . GLU A 1 558 ? 31.217 -5.856 35.865 1.00 29.56 ? 574 GLU A C 1 ATOM 4568 O O . GLU A 1 558 ? 30.318 -5.142 35.429 1.00 28.52 ? 574 GLU A O 1 ATOM 4569 C CB . GLU A 1 558 ? 31.398 -8.291 35.237 1.00 32.92 ? 574 GLU A CB 1 ATOM 4570 C CG . GLU A 1 558 ? 31.047 -9.728 35.598 1.00 35.72 ? 574 GLU A CG 1 ATOM 4571 C CD . GLU A 1 558 ? 31.741 -10.775 34.744 1.00 38.15 ? 574 GLU A CD 1 ATOM 4572 O OE1 . GLU A 1 558 ? 32.207 -10.473 33.613 1.00 37.13 ? 574 GLU A OE1 1 ATOM 4573 O OE2 . GLU A 1 558 ? 31.797 -11.931 35.219 1.00 40.49 ? 574 GLU A OE2 1 ATOM 4574 N N . ARG A 1 559 ? 32.477 -5.437 35.996 1.00 29.10 ? 575 ARG A N 1 ATOM 4575 C CA . ARG A 1 559 ? 32.871 -4.061 35.666 1.00 28.31 ? 575 ARG A CA 1 ATOM 4576 C C . ARG A 1 559 ? 34.097 -3.987 34.746 1.00 28.16 ? 575 ARG A C 1 ATOM 4577 O O . ARG A 1 559 ? 34.546 -2.888 34.397 1.00 27.58 ? 575 ARG A O 1 ATOM 4578 C CB . ARG A 1 559 ? 33.134 -3.252 36.950 1.00 28.34 ? 575 ARG A CB 1 ATOM 4579 C CG . ARG A 1 559 ? 31.932 -3.102 37.883 1.00 28.33 ? 575 ARG A CG 1 ATOM 4580 C CD . ARG A 1 559 ? 32.257 -2.221 39.084 1.00 28.41 ? 575 ARG A CD 1 ATOM 4581 N NE . ARG A 1 559 ? 32.799 -0.923 38.673 1.00 27.97 ? 575 ARG A NE 1 ATOM 4582 C CZ . ARG A 1 559 ? 32.062 0.122 38.306 1.00 27.52 ? 575 ARG A CZ 1 ATOM 4583 N NH1 . ARG A 1 559 ? 30.738 0.037 38.301 1.00 27.01 ? 575 ARG A NH1 1 ATOM 4584 N NH2 . ARG A 1 559 ? 32.653 1.252 37.929 1.00 27.77 ? 575 ARG A NH2 1 ATOM 4585 N N . ILE A 1 560 ? 34.615 -5.150 34.345 1.00 27.62 ? 576 ILE A N 1 ATOM 4586 C CA . ILE A 1 560 ? 35.880 -5.250 33.608 1.00 27.42 ? 576 ILE A CA 1 ATOM 4587 C C . ILE A 1 560 ? 35.686 -5.909 32.220 1.00 26.82 ? 576 ILE A C 1 ATOM 4588 O O . ILE A 1 560 ? 35.037 -6.948 32.098 1.00 25.83 ? 576 ILE A O 1 ATOM 4589 C CB . ILE A 1 560 ? 36.951 -6.000 34.452 1.00 28.66 ? 576 ILE A CB 1 ATOM 4590 C CG1 . ILE A 1 560 ? 37.341 -5.164 35.679 1.00 30.13 ? 576 ILE A CG1 1 ATOM 4591 C CG2 . ILE A 1 560 ? 38.219 -6.292 33.655 1.00 29.60 ? 576 ILE A CG2 1 ATOM 4592 C CD1 . ILE A 1 560 ? 38.020 -5.957 36.784 1.00 32.17 ? 576 ILE A CD1 1 ATOM 4593 N N . MET A 1 561 ? 36.227 -5.284 31.178 1.00 26.00 ? 577 MET A N 1 ATOM 4594 C CA . MET A 1 561 ? 36.280 -5.928 29.857 1.00 25.01 ? 577 MET A CA 1 ATOM 4595 C C . MET A 1 561 ? 37.299 -7.070 29.930 1.00 25.13 ? 577 MET A C 1 ATOM 4596 O O . MET A 1 561 ? 38.433 -6.863 30.362 1.00 24.74 ? 577 MET A O 1 ATOM 4597 C CB . MET A 1 561 ? 36.659 -4.906 28.778 1.00 24.81 ? 577 MET A CB 1 ATOM 4598 C CG . MET A 1 561 ? 36.821 -5.476 27.375 1.00 24.71 ? 577 MET A CG 1 ATOM 4599 S SD . MET A 1 561 ? 37.141 -4.143 26.203 1.00 24.10 ? 577 MET A SD 1 ATOM 4600 C CE . MET A 1 561 ? 38.830 -3.688 26.614 1.00 23.46 ? 577 MET A CE 1 ATOM 4601 N N . SER A 1 562 ? 36.898 -8.273 29.521 1.00 25.51 ? 578 SER A N 1 ATOM 4602 C CA . SER A 1 562 ? 37.743 -9.452 29.714 1.00 26.10 ? 578 SER A CA 1 ATOM 4603 C C . SER A 1 562 ? 37.632 -10.473 28.588 1.00 25.23 ? 578 SER A C 1 ATOM 4604 O O . SER A 1 562 ? 36.538 -10.751 28.109 1.00 25.73 ? 578 SER A O 1 ATOM 4605 C CB . SER A 1 562 ? 37.391 -10.119 31.052 1.00 26.97 ? 578 SER A CB 1 ATOM 4606 O OG . SER A 1 562 ? 37.859 -11.458 31.103 1.00 27.46 ? 578 SER A OG 1 ATOM 4607 N N . GLY A 1 563 ? 38.766 -11.053 28.200 1.00 25.17 ? 579 GLY A N 1 ATOM 4608 C CA . GLY A 1 563 ? 38.804 -12.090 27.156 1.00 24.59 ? 579 GLY A CA 1 ATOM 4609 C C . GLY A 1 563 ? 38.525 -13.497 27.681 1.00 24.69 ? 579 GLY A C 1 ATOM 4610 O O . GLY A 1 563 ? 38.629 -14.485 26.948 1.00 23.68 ? 579 GLY A O 1 ATOM 4611 N N . LYS A 1 564 ? 38.169 -13.595 28.958 1.00 24.94 ? 580 LYS A N 1 ATOM 4612 C CA . LYS A 1 564 ? 37.899 -14.896 29.564 1.00 26.28 ? 580 LYS A CA 1 ATOM 4613 C C . LYS A 1 564 ? 36.737 -15.649 28.882 1.00 25.34 ? 580 LYS A C 1 ATOM 4614 O O . LYS A 1 564 ? 36.827 -16.863 28.652 1.00 25.14 ? 580 LYS A O 1 ATOM 4615 C CB . LYS A 1 564 ? 37.640 -14.733 31.070 1.00 28.23 ? 580 LYS A CB 1 ATOM 4616 C CG . LYS A 1 564 ? 37.379 -16.041 31.789 1.00 33.29 ? 580 LYS A CG 1 ATOM 4617 C CD . LYS A 1 564 ? 37.050 -15.823 33.260 1.00 35.70 ? 580 LYS A CD 1 ATOM 4618 C CE . LYS A 1 564 ? 36.516 -17.108 33.871 1.00 39.08 ? 580 LYS A CE 1 ATOM 4619 N NZ . LYS A 1 564 ? 36.164 -16.904 35.304 1.00 42.05 ? 580 LYS A NZ 1 ATOM 4620 N N . ALA A 1 565 ? 35.665 -14.930 28.548 1.00 24.06 ? 581 ALA A N 1 ATOM 4621 C CA . ALA A 1 565 ? 34.457 -15.569 28.035 1.00 23.71 ? 581 ALA A CA 1 ATOM 4622 C C . ALA A 1 565 ? 34.659 -16.107 26.618 1.00 23.54 ? 581 ALA A C 1 ATOM 4623 O O . ALA A 1 565 ? 34.283 -17.242 26.320 1.00 24.01 ? 581 ALA A O 1 ATOM 4624 C CB . ALA A 1 565 ? 33.268 -14.618 28.104 1.00 23.29 ? 581 ALA A CB 1 ATOM 4625 N N . ILE A 1 566 ? 35.281 -15.314 25.754 1.00 22.92 ? 582 ILE A N 1 ATOM 4626 C CA . ILE A 1 566 ? 35.563 -15.786 24.396 1.00 22.59 ? 582 ILE A CA 1 ATOM 4627 C C . ILE A 1 566 ? 36.504 -17.012 24.408 1.00 22.99 ? 582 ILE A C 1 ATOM 4628 O O . ILE A 1 566 ? 36.304 -17.966 23.641 1.00 22.72 ? 582 ILE A O 1 ATOM 4629 C CB . ILE A 1 566 ? 36.037 -14.643 23.459 1.00 22.65 ? 582 ILE A CB 1 ATOM 4630 C CG1 . ILE A 1 566 ? 36.032 -15.121 21.999 1.00 22.11 ? 582 ILE A CG1 1 ATOM 4631 C CG2 . ILE A 1 566 ? 37.390 -14.073 23.899 1.00 22.67 ? 582 ILE A CG2 1 ATOM 4632 C CD1 . ILE A 1 566 ? 36.266 -14.026 20.974 1.00 22.01 ? 582 ILE A CD1 1 ATOM 4633 N N . ALA A 1 567 ? 37.503 -17.011 25.289 1.00 23.30 ? 583 ALA A N 1 ATOM 4634 C CA . ALA A 1 567 ? 38.402 -18.168 25.398 1.00 24.28 ? 583 ALA A CA 1 ATOM 4635 C C . ALA A 1 567 ? 37.660 -19.418 25.911 1.00 25.24 ? 583 ALA A C 1 ATOM 4636 O O . ALA A 1 567 ? 37.925 -20.535 25.464 1.00 24.92 ? 583 ALA A O 1 ATOM 4637 C CB . ALA A 1 567 ? 39.609 -17.845 26.269 1.00 24.66 ? 583 ALA A CB 1 ATOM 4638 N N . GLU A 1 568 ? 36.724 -19.214 26.838 1.00 25.67 ? 584 GLU A N 1 ATOM 4639 C CA . GLU A 1 568 ? 35.895 -20.297 27.375 1.00 26.81 ? 584 GLU A CA 1 ATOM 4640 C C . GLU A 1 568 ? 35.058 -20.923 26.247 1.00 26.15 ? 584 GLU A C 1 ATOM 4641 O O . GLU A 1 568 ? 35.025 -22.138 26.088 1.00 26.34 ? 584 GLU A O 1 ATOM 4642 C CB . GLU A 1 568 ? 35.003 -19.748 28.491 1.00 28.32 ? 584 GLU A CB 1 ATOM 4643 C CG . GLU A 1 568 ? 34.272 -20.771 29.348 1.00 30.46 ? 584 GLU A CG 1 ATOM 4644 C CD . GLU A 1 568 ? 33.541 -20.106 30.503 1.00 32.59 ? 584 GLU A CD 1 ATOM 4645 O OE1 . GLU A 1 568 ? 34.101 -19.162 31.109 1.00 33.43 ? 584 GLU A OE1 1 ATOM 4646 O OE2 . GLU A 1 568 ? 32.396 -20.512 30.796 1.00 33.09 ? 584 GLU A OE2 1 ATOM 4647 N N . TYR A 1 569 ? 34.406 -20.083 25.452 1.00 25.03 ? 585 TYR A N 1 ATOM 4648 C CA . TYR A 1 569 ? 33.619 -20.559 24.320 1.00 24.49 ? 585 TYR A CA 1 ATOM 4649 C C . TYR A 1 569 ? 34.456 -21.486 23.423 1.00 24.45 ? 585 TYR A C 1 ATOM 4650 O O . TYR A 1 569 ? 34.004 -22.572 23.056 1.00 24.18 ? 585 TYR A O 1 ATOM 4651 C CB . TYR A 1 569 ? 33.087 -19.365 23.519 1.00 23.61 ? 585 TYR A CB 1 ATOM 4652 C CG . TYR A 1 569 ? 32.087 -19.707 22.436 1.00 23.41 ? 585 TYR A CG 1 ATOM 4653 C CD1 . TYR A 1 569 ? 32.508 -20.192 21.184 1.00 23.41 ? 585 TYR A CD1 1 ATOM 4654 C CD2 . TYR A 1 569 ? 30.719 -19.506 22.640 1.00 23.42 ? 585 TYR A CD2 1 ATOM 4655 C CE1 . TYR A 1 569 ? 31.584 -20.497 20.187 1.00 23.30 ? 585 TYR A CE1 1 ATOM 4656 C CE2 . TYR A 1 569 ? 29.792 -19.807 21.654 1.00 23.60 ? 585 TYR A CE2 1 ATOM 4657 C CZ . TYR A 1 569 ? 30.228 -20.288 20.426 1.00 23.41 ? 585 TYR A CZ 1 ATOM 4658 O OH . TYR A 1 569 ? 29.300 -20.571 19.451 1.00 24.12 ? 585 TYR A OH 1 ATOM 4659 N N . PHE A 1 570 ? 35.675 -21.062 23.088 1.00 24.37 ? 586 PHE A N 1 ATOM 4660 C CA . PHE A 1 570 ? 36.486 -21.777 22.092 1.00 24.39 ? 586 PHE A CA 1 ATOM 4661 C C . PHE A 1 570 ? 37.440 -22.831 22.648 1.00 25.30 ? 586 PHE A C 1 ATOM 4662 O O . PHE A 1 570 ? 38.162 -23.475 21.893 1.00 25.77 ? 586 PHE A O 1 ATOM 4663 C CB . PHE A 1 570 ? 37.220 -20.783 21.182 1.00 23.06 ? 586 PHE A CB 1 ATOM 4664 C CG . PHE A 1 570 ? 36.301 -20.044 20.260 1.00 23.07 ? 586 PHE A CG 1 ATOM 4665 C CD1 . PHE A 1 570 ? 35.739 -20.691 19.153 1.00 22.35 ? 586 PHE A CD1 1 ATOM 4666 C CD2 . PHE A 1 570 ? 35.955 -18.717 20.510 1.00 22.41 ? 586 PHE A CD2 1 ATOM 4667 C CE1 . PHE A 1 570 ? 34.861 -20.020 18.317 1.00 22.02 ? 586 PHE A CE1 1 ATOM 4668 C CE2 . PHE A 1 570 ? 35.087 -18.044 19.662 1.00 22.75 ? 586 PHE A CE2 1 ATOM 4669 C CZ . PHE A 1 570 ? 34.544 -18.694 18.559 1.00 21.82 ? 586 PHE A CZ 1 ATOM 4670 N N . GLU A 1 571 ? 37.430 -23.024 23.963 1.00 25.97 ? 587 GLU A N 1 ATOM 4671 C CA . GLU A 1 571 ? 38.352 -23.967 24.589 1.00 27.16 ? 587 GLU A CA 1 ATOM 4672 C C . GLU A 1 571 ? 38.321 -25.401 23.993 1.00 26.70 ? 587 GLU A C 1 ATOM 4673 O O . GLU A 1 571 ? 39.380 -25.975 23.772 1.00 26.53 ? 587 GLU A O 1 ATOM 4674 C CB . GLU A 1 571 ? 38.181 -23.963 26.120 1.00 28.26 ? 587 GLU A CB 1 ATOM 4675 C CG . GLU A 1 571 ? 39.042 -24.966 26.867 1.00 31.21 ? 587 GLU A CG 1 ATOM 4676 C CD . GLU A 1 571 ? 40.529 -24.643 26.862 1.00 32.91 ? 587 GLU A CD 1 ATOM 4677 O OE1 . GLU A 1 571 ? 40.934 -23.533 26.436 1.00 33.56 ? 587 GLU A OE1 1 ATOM 4678 O OE2 . GLU A 1 571 ? 41.304 -25.525 27.293 1.00 34.75 ? 587 GLU A OE2 1 ATOM 4679 N N . PRO A 1 572 ? 37.123 -25.970 23.705 1.00 27.04 ? 588 PRO A N 1 ATOM 4680 C CA . PRO A 1 572 ? 37.120 -27.316 23.101 1.00 27.02 ? 588 PRO A CA 1 ATOM 4681 C C . PRO A 1 572 ? 37.761 -27.344 21.712 1.00 26.71 ? 588 PRO A C 1 ATOM 4682 O O . PRO A 1 572 ? 38.392 -28.342 21.339 1.00 26.11 ? 588 PRO A O 1 ATOM 4683 C CB . PRO A 1 572 ? 35.625 -27.660 22.991 1.00 27.91 ? 588 PRO A CB 1 ATOM 4684 C CG . PRO A 1 572 ? 34.933 -26.733 23.933 1.00 28.59 ? 588 PRO A CG 1 ATOM 4685 C CD . PRO A 1 572 ? 35.752 -25.478 23.942 1.00 27.74 ? 588 PRO A CD 1 ATOM 4686 N N . LEU A 1 573 ? 37.602 -26.252 20.964 1.00 26.17 ? 589 LEU A N 1 ATOM 4687 C CA . LEU A 1 573 ? 38.253 -26.117 19.655 1.00 25.65 ? 589 LEU A CA 1 ATOM 4688 C C . LEU A 1 573 ? 39.769 -26.004 19.798 1.00 26.03 ? 589 LEU A C 1 ATOM 4689 O O . LEU A 1 573 ? 40.506 -26.616 19.029 1.00 26.17 ? 589 LEU A O 1 ATOM 4690 C CB . LEU A 1 573 ? 37.709 -24.911 18.883 1.00 25.02 ? 589 LEU A CB 1 ATOM 4691 C CG . LEU A 1 573 ? 38.319 -24.695 17.488 1.00 24.71 ? 589 LEU A CG 1 ATOM 4692 C CD1 . LEU A 1 573 ? 37.935 -25.821 16.536 1.00 24.78 ? 589 LEU A CD1 1 ATOM 4693 C CD2 . LEU A 1 573 ? 37.903 -23.347 16.933 1.00 24.12 ? 589 LEU A CD2 1 ATOM 4694 N N . ARG A 1 574 ? 40.227 -25.224 20.780 1.00 26.43 ? 590 ARG A N 1 ATOM 4695 C CA . ARG A 1 574 ? 41.664 -25.044 21.005 1.00 26.84 ? 590 ARG A CA 1 ATOM 4696 C C . ARG A 1 574 ? 42.361 -26.377 21.289 1.00 26.92 ? 590 ARG A C 1 ATOM 4697 O O . ARG A 1 574 ? 43.403 -26.670 20.701 1.00 26.06 ? 590 ARG A O 1 ATOM 4698 C CB . ARG A 1 574 ? 41.948 -24.059 22.146 1.00 27.08 ? 590 ARG A CB 1 ATOM 4699 C CG . ARG A 1 574 ? 43.438 -23.769 22.317 1.00 27.87 ? 590 ARG A CG 1 ATOM 4700 C CD . ARG A 1 574 ? 43.778 -23.081 23.632 1.00 29.08 ? 590 ARG A CD 1 ATOM 4701 N NE . ARG A 1 574 ? 43.432 -23.894 24.794 1.00 30.81 ? 590 ARG A NE 1 ATOM 4702 C CZ . ARG A 1 574 ? 44.151 -24.919 25.255 1.00 32.32 ? 590 ARG A CZ 1 ATOM 4703 N NH1 . ARG A 1 574 ? 45.279 -25.285 24.662 1.00 32.77 ? 590 ARG A NH1 1 ATOM 4704 N NH2 . ARG A 1 574 ? 43.739 -25.583 26.325 1.00 33.08 ? 590 ARG A NH2 1 ATOM 4705 N N . VAL A 1 575 ? 41.793 -27.161 22.206 1.00 27.50 ? 591 VAL A N 1 ATOM 4706 C CA . VAL A 1 575 ? 42.333 -28.481 22.525 1.00 28.08 ? 591 VAL A CA 1 ATOM 4707 C C . VAL A 1 575 ? 42.419 -29.351 21.258 1.00 27.80 ? 591 VAL A C 1 ATOM 4708 O O . VAL A 1 575 ? 43.486 -29.886 20.942 1.00 28.38 ? 591 VAL A O 1 ATOM 4709 C CB . VAL A 1 575 ? 41.534 -29.176 23.652 1.00 28.97 ? 591 VAL A CB 1 ATOM 4710 C CG1 . VAL A 1 575 ? 42.028 -30.605 23.872 1.00 29.54 ? 591 VAL A CG1 1 ATOM 4711 C CG2 . VAL A 1 575 ? 41.651 -28.372 24.942 1.00 28.97 ? 591 VAL A CG2 1 ATOM 4712 N N . TRP A 1 576 ? 41.314 -29.454 20.523 1.00 27.36 ? 592 TRP A N 1 ATOM 4713 C CA . TRP A 1 576 ? 41.273 -30.277 19.324 1.00 27.12 ? 592 TRP A CA 1 ATOM 4714 C C . TRP A 1 576 ? 42.251 -29.790 18.239 1.00 26.22 ? 592 TRP A C 1 ATOM 4715 O O . TRP A 1 576 ? 42.947 -30.600 17.612 1.00 25.49 ? 592 TRP A O 1 ATOM 4716 C CB . TRP A 1 576 ? 39.855 -30.366 18.741 1.00 28.31 ? 592 TRP A CB 1 ATOM 4717 C CG . TRP A 1 576 ? 39.847 -31.199 17.497 1.00 28.96 ? 592 TRP A CG 1 ATOM 4718 C CD1 . TRP A 1 576 ? 39.702 -32.557 17.425 1.00 29.70 ? 592 TRP A CD1 1 ATOM 4719 C CD2 . TRP A 1 576 ? 40.064 -30.746 16.151 1.00 29.54 ? 592 TRP A CD2 1 ATOM 4720 N NE1 . TRP A 1 576 ? 39.792 -32.973 16.117 1.00 29.75 ? 592 TRP A NE1 1 ATOM 4721 C CE2 . TRP A 1 576 ? 40.023 -31.886 15.315 1.00 29.88 ? 592 TRP A CE2 1 ATOM 4722 C CE3 . TRP A 1 576 ? 40.287 -29.485 15.568 1.00 30.09 ? 592 TRP A CE3 1 ATOM 4723 C CZ2 . TRP A 1 576 ? 40.184 -31.808 13.925 1.00 30.07 ? 592 TRP A CZ2 1 ATOM 4724 C CZ3 . TRP A 1 576 ? 40.459 -29.406 14.178 1.00 30.47 ? 592 TRP A CZ3 1 ATOM 4725 C CH2 . TRP A 1 576 ? 40.406 -30.566 13.377 1.00 30.76 ? 592 TRP A CH2 1 ATOM 4726 N N . LEU A 1 577 ? 42.293 -28.475 18.015 1.00 25.03 ? 593 LEU A N 1 ATOM 4727 C CA . LEU A 1 577 ? 43.089 -27.907 16.918 1.00 24.31 ? 593 LEU A CA 1 ATOM 4728 C C . LEU A 1 577 ? 44.598 -28.000 17.166 1.00 24.45 ? 593 LEU A C 1 ATOM 4729 O O . LEU A 1 577 ? 45.371 -28.262 16.248 1.00 23.23 ? 593 LEU A O 1 ATOM 4730 C CB . LEU A 1 577 ? 42.673 -26.455 16.641 1.00 23.53 ? 593 LEU A CB 1 ATOM 4731 C CG . LEU A 1 577 ? 43.326 -25.716 15.472 1.00 23.60 ? 593 LEU A CG 1 ATOM 4732 C CD1 . LEU A 1 577 ? 43.147 -26.468 14.156 1.00 23.09 ? 593 LEU A CD1 1 ATOM 4733 C CD2 . LEU A 1 577 ? 42.754 -24.307 15.377 1.00 22.94 ? 593 LEU A CD2 1 ATOM 4734 N N . GLU A 1 578 ? 45.017 -27.775 18.408 1.00 24.64 ? 594 GLU A N 1 ATOM 4735 C CA . GLU A 1 578 ? 46.436 -27.862 18.743 1.00 25.07 ? 594 GLU A CA 1 ATOM 4736 C C . GLU A 1 578 ? 46.932 -29.279 18.476 1.00 25.30 ? 594 GLU A C 1 ATOM 4737 O O . GLU A 1 578 ? 48.041 -29.467 17.972 1.00 25.73 ? 594 GLU A O 1 ATOM 4738 C CB . GLU A 1 578 ? 46.678 -27.482 20.210 1.00 25.53 ? 594 GLU A CB 1 ATOM 4739 C CG . GLU A 1 578 ? 46.654 -25.983 20.478 1.00 26.90 ? 594 GLU A CG 1 ATOM 4740 C CD . GLU A 1 578 ? 47.006 -25.635 21.916 1.00 28.99 ? 594 GLU A CD 1 ATOM 4741 O OE1 . GLU A 1 578 ? 47.581 -26.489 22.617 1.00 31.06 ? 594 GLU A OE1 1 ATOM 4742 O OE2 . GLU A 1 578 ? 46.705 -24.508 22.357 1.00 29.85 ? 594 GLU A OE2 1 ATOM 4743 N N . ALA A 1 579 ? 46.094 -30.264 18.795 1.00 25.02 ? 595 ALA A N 1 ATOM 4744 C CA . ALA A 1 579 ? 46.439 -31.670 18.624 1.00 25.61 ? 595 ALA A CA 1 ATOM 4745 C C . ALA A 1 579 ? 46.450 -32.040 17.146 1.00 25.56 ? 595 ALA A C 1 ATOM 4746 O O . ALA A 1 579 ? 47.311 -32.802 16.691 1.00 25.88 ? 595 ALA A O 1 ATOM 4747 C CB . ALA A 1 579 ? 45.473 -32.561 19.402 1.00 25.96 ? 595 ALA A CB 1 ATOM 4748 N N . GLU A 1 580 ? 45.507 -31.484 16.393 1.00 25.14 ? 596 GLU A N 1 ATOM 4749 C CA . GLU A 1 580 ? 45.401 -31.791 14.965 1.00 25.23 ? 596 GLU A CA 1 ATOM 4750 C C . GLU A 1 580 ? 46.564 -31.214 14.152 1.00 24.42 ? 596 GLU A C 1 ATOM 4751 O O . GLU A 1 580 ? 47.034 -31.831 13.187 1.00 25.03 ? 596 GLU A O 1 ATOM 4752 C CB . GLU A 1 580 ? 44.073 -31.287 14.409 1.00 26.21 ? 596 GLU A CB 1 ATOM 4753 C CG . GLU A 1 580 ? 43.799 -31.739 12.982 1.00 28.09 ? 596 GLU A CG 1 ATOM 4754 C CD . GLU A 1 580 ? 43.412 -33.213 12.884 1.00 30.32 ? 596 GLU A CD 1 ATOM 4755 O OE1 . GLU A 1 580 ? 43.341 -33.911 13.923 1.00 31.14 ? 596 GLU A OE1 1 ATOM 4756 O OE2 . GLU A 1 580 ? 43.172 -33.684 11.754 1.00 31.60 ? 596 GLU A OE2 1 ATOM 4757 N N . ASN A 1 581 ? 46.989 -30.012 14.518 1.00 23.04 ? 597 ASN A N 1 ATOM 4758 C CA . ASN A 1 581 ? 48.125 -29.365 13.885 1.00 22.66 ? 597 ASN A CA 1 ATOM 4759 C C . ASN A 1 581 ? 49.436 -30.119 14.164 1.00 23.45 ? 597 ASN A C 1 ATOM 4760 O O . ASN A 1 581 ? 50.298 -30.229 13.293 1.00 23.38 ? 597 ASN A O 1 ATOM 4761 C CB . ASN A 1 581 ? 48.208 -27.893 14.315 1.00 21.22 ? 597 ASN A CB 1 ATOM 4762 C CG . ASN A 1 581 ? 47.251 -26.990 13.536 1.00 21.10 ? 597 ASN A CG 1 ATOM 4763 O OD1 . ASN A 1 581 ? 46.801 -27.333 12.430 1.00 20.50 ? 597 ASN A OD1 1 ATOM 4764 N ND2 . ASN A 1 581 ? 46.976 -25.803 14.083 1.00 20.20 ? 597 ASN A ND2 1 ATOM 4765 N N . ILE A 1 582 ? 49.570 -30.654 15.375 1.00 24.66 ? 598 ILE A N 1 ATOM 4766 C CA . ILE A 1 582 ? 50.716 -31.497 15.708 1.00 26.27 ? 598 ILE A CA 1 ATOM 4767 C C . ILE A 1 582 ? 50.654 -32.812 14.924 1.00 27.16 ? 598 ILE A C 1 ATOM 4768 O O . ILE A 1 582 ? 51.634 -33.209 14.290 1.00 27.90 ? 598 ILE A O 1 ATOM 4769 C CB . ILE A 1 582 ? 50.828 -31.724 17.240 1.00 26.15 ? 598 ILE A CB 1 ATOM 4770 C CG1 . ILE A 1 582 ? 51.316 -30.434 17.906 1.00 26.09 ? 598 ILE A CG1 1 ATOM 4771 C CG2 . ILE A 1 582 ? 51.782 -32.877 17.557 1.00 27.05 ? 598 ILE A CG2 1 ATOM 4772 C CD1 . ILE A 1 582 ? 51.148 -30.409 19.419 1.00 27.39 ? 598 ILE A CD1 1 ATOM 4773 N N . LYS A 1 583 ? 49.487 -33.451 14.920 1.00 28.50 ? 599 LYS A N 1 ATOM 4774 C CA . LYS A 1 583 ? 49.300 -34.715 14.211 1.00 30.01 ? 599 LYS A CA 1 ATOM 4775 C C . LYS A 1 583 ? 49.684 -34.583 12.738 1.00 30.09 ? 599 LYS A C 1 ATOM 4776 O O . LYS A 1 583 ? 50.280 -35.495 12.156 1.00 29.43 ? 599 LYS A O 1 ATOM 4777 C CB . LYS A 1 583 ? 47.845 -35.185 14.323 1.00 31.91 ? 599 LYS A CB 1 ATOM 4778 C CG . LYS A 1 583 ? 47.561 -36.498 13.609 1.00 34.84 ? 599 LYS A CG 1 ATOM 4779 C CD . LYS A 1 583 ? 46.086 -36.652 13.275 1.00 37.70 ? 599 LYS A CD 1 ATOM 4780 C CE . LYS A 1 583 ? 45.821 -38.045 12.720 1.00 40.89 ? 599 LYS A CE 1 ATOM 4781 N NZ . LYS A 1 583 ? 44.367 -38.334 12.556 1.00 43.22 ? 599 LYS A NZ 1 ATOM 4782 N N . ASN A 1 584 ? 49.327 -33.448 12.142 1.00 29.32 ? 600 ASN A N 1 ATOM 4783 C CA . ASN A 1 584 ? 49.550 -33.218 10.710 1.00 29.14 ? 600 ASN A CA 1 ATOM 4784 C C . ASN A 1 584 ? 50.795 -32.382 10.389 1.00 27.81 ? 600 ASN A C 1 ATOM 4785 O O . ASN A 1 584 ? 50.982 -31.960 9.245 1.00 26.84 ? 600 ASN A O 1 ATOM 4786 C CB . ASN A 1 584 ? 48.295 -32.601 10.061 1.00 30.71 ? 600 ASN A CB 1 ATOM 4787 C CG . ASN A 1 584 ? 47.160 -33.606 9.901 1.00 33.09 ? 600 ASN A CG 1 ATOM 4788 O OD1 . ASN A 1 584 ? 47.258 -34.543 9.119 1.00 35.92 ? 600 ASN A OD1 1 ATOM 4789 N ND2 . ASN A 1 584 ? 46.078 -33.410 10.640 1.00 33.56 ? 600 ASN A ND2 1 ATOM 4790 N N . ASN A 1 585 ? 51.640 -32.141 11.391 1.00 27.11 ? 601 ASN A N 1 ATOM 4791 C CA . ASN A 1 585 ? 52.894 -31.404 11.193 1.00 27.00 ? 601 ASN A CA 1 ATOM 4792 C C . ASN A 1 585 ? 52.655 -30.055 10.499 1.00 25.46 ? 601 ASN A C 1 ATOM 4793 O O . ASN A 1 585 ? 53.379 -29.687 9.569 1.00 25.94 ? 601 ASN A O 1 ATOM 4794 C CB . ASN A 1 585 ? 53.893 -32.266 10.390 1.00 27.20 ? 601 ASN A CB 1 ATOM 4795 C CG . ASN A 1 585 ? 55.324 -31.771 10.491 1.00 28.68 ? 601 ASN A CG 1 ATOM 4796 O OD1 . ASN A 1 585 ? 55.675 -31.037 11.410 1.00 29.18 ? 601 ASN A OD1 1 ATOM 4797 N ND2 . ASN A 1 585 ? 56.167 -32.176 9.531 1.00 29.42 ? 601 ASN A ND2 1 ATOM 4798 N N . VAL A 1 586 ? 51.619 -29.340 10.942 1.00 24.17 ? 602 VAL A N 1 ATOM 4799 C CA . VAL A 1 586 ? 51.177 -28.111 10.269 1.00 22.85 ? 602 VAL A CA 1 ATOM 4800 C C . VAL A 1 586 ? 52.107 -26.944 10.629 1.00 22.75 ? 602 VAL A C 1 ATOM 4801 O O . VAL A 1 586 ? 52.342 -26.677 11.805 1.00 21.72 ? 602 VAL A O 1 ATOM 4802 C CB . VAL A 1 586 ? 49.709 -27.761 10.629 1.00 22.39 ? 602 VAL A CB 1 ATOM 4803 C CG1 . VAL A 1 586 ? 49.353 -26.349 10.180 1.00 21.35 ? 602 VAL A CG1 1 ATOM 4804 C CG2 . VAL A 1 586 ? 48.737 -28.777 10.019 1.00 21.89 ? 602 VAL A CG2 1 ATOM 4805 N N . HIS A 1 587 ? 52.642 -26.256 9.622 1.00 21.61 ? 603 HIS A N 1 ATOM 4806 C CA . HIS A 1 587 ? 53.525 -25.111 9.878 1.00 21.91 ? 603 HIS A CA 1 ATOM 4807 C C . HIS A 1 587 ? 52.733 -23.924 10.436 1.00 21.66 ? 603 HIS A C 1 ATOM 4808 O O . HIS A 1 587 ? 51.677 -23.559 9.887 1.00 21.61 ? 603 HIS A O 1 ATOM 4809 C CB . HIS A 1 587 ? 54.283 -24.704 8.610 1.00 21.73 ? 603 HIS A CB 1 ATOM 4810 C CG . HIS A 1 587 ? 55.285 -23.613 8.835 1.00 22.09 ? 603 HIS A CG 1 ATOM 4811 N ND1 . HIS A 1 587 ? 56.525 -23.846 9.388 1.00 21.72 ? 603 HIS A ND1 1 ATOM 4812 C CD2 . HIS A 1 587 ? 55.227 -22.280 8.589 1.00 21.99 ? 603 HIS A CD2 1 ATOM 4813 C CE1 . HIS A 1 587 ? 57.189 -22.707 9.474 1.00 21.89 ? 603 HIS A CE1 1 ATOM 4814 N NE2 . HIS A 1 587 ? 56.419 -21.739 9.008 1.00 22.07 ? 603 HIS A NE2 1 ATOM 4815 N N . ILE A 1 588 ? 53.219 -23.363 11.550 1.00 21.20 ? 604 ILE A N 1 ATOM 4816 C CA . ILE A 1 588 ? 52.596 -22.200 12.206 1.00 20.38 ? 604 ILE A CA 1 ATOM 4817 C C . ILE A 1 588 ? 53.485 -20.970 11.981 1.00 19.73 ? 604 ILE A C 1 ATOM 4818 O O . ILE A 1 588 ? 54.705 -21.067 12.090 1.00 19.37 ? 604 ILE A O 1 ATOM 4819 C CB . ILE A 1 588 ? 52.387 -22.460 13.738 1.00 20.81 ? 604 ILE A CB 1 ATOM 4820 C CG1 . ILE A 1 588 ? 51.653 -23.795 13.977 1.00 21.05 ? 604 ILE A CG1 1 ATOM 4821 C CG2 . ILE A 1 588 ? 51.627 -21.315 14.404 1.00 20.84 ? 604 ILE A CG2 1 ATOM 4822 C CD1 . ILE A 1 588 ? 50.300 -23.928 13.284 1.00 21.66 ? 604 ILE A CD1 1 ATOM 4823 N N . GLY A 1 589 ? 52.880 -19.829 11.646 1.00 19.14 ? 605 GLY A N 1 ATOM 4824 C CA . GLY A 1 589 ? 53.605 -18.552 11.511 1.00 19.08 ? 605 GLY A CA 1 ATOM 4825 C C . GLY A 1 589 ? 53.923 -18.310 10.047 1.00 19.35 ? 605 GLY A C 1 ATOM 4826 O O . GLY A 1 589 ? 53.684 -19.188 9.251 1.00 19.55 ? 605 GLY A O 1 ATOM 4827 N N . TRP A 1 590 ? 54.466 -17.141 9.708 1.00 19.24 ? 606 TRP A N 1 ATOM 4828 C CA . TRP A 1 590 ? 54.674 -16.768 8.295 1.00 20.30 ? 606 TRP A CA 1 ATOM 4829 C C . TRP A 1 590 ? 55.867 -15.843 8.109 1.00 20.71 ? 606 TRP A C 1 ATOM 4830 O O . TRP A 1 590 ? 56.208 -15.065 8.994 1.00 21.30 ? 606 TRP A O 1 ATOM 4831 C CB . TRP A 1 590 ? 53.406 -16.131 7.707 1.00 20.00 ? 606 TRP A CB 1 ATOM 4832 C CG . TRP A 1 590 ? 52.856 -14.974 8.503 1.00 20.49 ? 606 TRP A CG 1 ATOM 4833 C CD1 . TRP A 1 590 ? 53.191 -13.656 8.369 1.00 20.55 ? 606 TRP A CD1 1 ATOM 4834 C CD2 . TRP A 1 590 ? 51.900 -15.037 9.589 1.00 21.08 ? 606 TRP A CD2 1 ATOM 4835 N NE1 . TRP A 1 590 ? 52.494 -12.891 9.280 1.00 21.32 ? 606 TRP A NE1 1 ATOM 4836 C CE2 . TRP A 1 590 ? 51.705 -13.710 10.049 1.00 21.04 ? 606 TRP A CE2 1 ATOM 4837 C CE3 . TRP A 1 590 ? 51.181 -16.080 10.200 1.00 21.03 ? 606 TRP A CE3 1 ATOM 4838 C CZ2 . TRP A 1 590 ? 50.816 -13.395 11.083 1.00 21.03 ? 606 TRP A CZ2 1 ATOM 4839 C CZ3 . TRP A 1 590 ? 50.294 -15.771 11.238 1.00 21.28 ? 606 TRP A CZ3 1 ATOM 4840 C CH2 . TRP A 1 590 ? 50.121 -14.435 11.670 1.00 21.42 ? 606 TRP A CH2 1 ATOM 4841 N N . THR A 1 591 ? 56.495 -15.911 6.941 1.00 20.97 ? 607 THR A N 1 ATOM 4842 C CA . THR A 1 591 ? 57.585 -14.995 6.629 1.00 21.14 ? 607 THR A CA 1 ATOM 4843 C C . THR A 1 591 ? 56.978 -13.627 6.266 1.00 21.29 ? 607 THR A C 1 ATOM 4844 O O . THR A 1 591 ? 55.768 -13.515 6.029 1.00 20.38 ? 607 THR A O 1 ATOM 4845 C CB . THR A 1 591 ? 58.411 -15.523 5.456 1.00 21.84 ? 607 THR A CB 1 ATOM 4846 O OG1 . THR A 1 591 ? 57.505 -16.046 4.493 1.00 21.34 ? 607 THR A OG1 1 ATOM 4847 C CG2 . THR A 1 591 ? 59.343 -16.644 5.910 1.00 22.51 ? 607 THR A CG2 1 ATOM 4848 N N . THR A 1 592 ? 57.814 -12.595 6.230 1.00 21.56 ? 608 THR A N 1 ATOM 4849 C CA . THR A 1 592 ? 57.350 -11.250 5.905 1.00 22.09 ? 608 THR A CA 1 ATOM 4850 C C . THR A 1 592 ? 56.985 -11.194 4.422 1.00 21.65 ? 608 THR A C 1 ATOM 4851 O O . THR A 1 592 ? 57.719 -11.706 3.590 1.00 22.43 ? 608 THR A O 1 ATOM 4852 C CB . THR A 1 592 ? 58.414 -10.197 6.278 1.00 23.19 ? 608 THR A CB 1 ATOM 4853 O OG1 . THR A 1 592 ? 58.614 -10.246 7.700 1.00 24.43 ? 608 THR A OG1 1 ATOM 4854 C CG2 . THR A 1 592 ? 57.960 -8.781 5.893 1.00 23.02 ? 608 THR A CG2 1 ATOM 4855 N N . SER A 1 593 ? 55.830 -10.604 4.118 1.00 20.77 ? 609 SER A N 1 ATOM 4856 C CA . SER A 1 593 ? 55.311 -10.508 2.741 1.00 20.61 ? 609 SER A CA 1 ATOM 4857 C C . SER A 1 593 ? 56.226 -9.752 1.776 1.00 21.29 ? 609 SER A C 1 ATOM 4858 O O . SER A 1 593 ? 56.915 -8.818 2.173 1.00 20.59 ? 609 SER A O 1 ATOM 4859 C CB . SER A 1 593 ? 53.957 -9.792 2.778 1.00 20.41 ? 609 SER A CB 1 ATOM 4860 O OG . SER A 1 593 ? 53.385 -9.718 1.491 1.00 19.68 ? 609 SER A OG 1 ATOM 4861 N N . ASN A 1 594 ? 56.201 -10.150 0.498 1.00 21.91 ? 610 ASN A N 1 ATOM 4862 C CA A ASN A 1 594 ? 56.919 -9.458 -0.573 0.50 22.69 ? 610 ASN A CA 1 ATOM 4863 C CA B ASN A 1 594 ? 56.926 -9.415 -0.542 0.50 22.92 ? 610 ASN A CA 1 ATOM 4864 C C . ASN A 1 594 ? 55.967 -8.688 -1.503 1.00 23.40 ? 610 ASN A C 1 ATOM 4865 O O . ASN A 1 594 ? 56.372 -8.226 -2.595 1.00 23.24 ? 610 ASN A O 1 ATOM 4866 C CB A ASN A 1 594 ? 57.760 -10.462 -1.392 0.50 22.56 ? 610 ASN A CB 1 ATOM 4867 C CB B ASN A 1 594 ? 57.863 -10.352 -1.325 0.50 23.18 ? 610 ASN A CB 1 ATOM 4868 C CG A ASN A 1 594 ? 56.906 -11.416 -2.221 0.50 22.51 ? 610 ASN A CG 1 ATOM 4869 C CG B ASN A 1 594 ? 58.807 -11.132 -0.423 0.50 23.54 ? 610 ASN A CG 1 ATOM 4870 O OD1 A ASN A 1 594 ? 55.695 -11.504 -2.038 0.50 22.47 ? 610 ASN A OD1 1 ATOM 4871 O OD1 B ASN A 1 594 ? 59.524 -10.560 0.408 0.50 23.14 ? 610 ASN A OD1 1 ATOM 4872 N ND2 A ASN A 1 594 ? 57.539 -12.131 -3.145 0.50 22.62 ? 610 ASN A ND2 1 ATOM 4873 N ND2 B ASN A 1 594 ? 58.818 -12.450 -0.591 0.50 23.75 ? 610 ASN A ND2 1 ATOM 4874 N N . LYS A 1 595 ? 54.700 -8.553 -1.101 1.00 23.80 ? 611 LYS A N 1 ATOM 4875 C CA . LYS A 1 595 ? 53.672 -7.991 -2.013 1.00 25.75 ? 611 LYS A CA 1 ATOM 4876 C C . LYS A 1 595 ? 53.424 -6.463 -1.961 1.00 26.66 ? 611 LYS A C 1 ATOM 4877 O O . LYS A 1 595 ? 52.492 -5.973 -2.608 1.00 27.35 ? 611 LYS A O 1 ATOM 4878 C CB . LYS A 1 595 ? 52.342 -8.762 -1.883 1.00 26.15 ? 611 LYS A CB 1 ATOM 4879 C CG . LYS A 1 595 ? 52.389 -10.224 -2.320 1.00 26.73 ? 611 LYS A CG 1 ATOM 4880 C CD . LYS A 1 595 ? 52.494 -10.375 -3.834 1.00 28.59 ? 611 LYS A CD 1 ATOM 4881 C CE . LYS A 1 595 ? 52.378 -11.832 -4.270 1.00 29.62 ? 611 LYS A CE 1 ATOM 4882 N NZ . LYS A 1 595 ? 53.251 -12.742 -3.469 1.00 29.83 ? 611 LYS A NZ 1 ATOM 4883 N N . CYS A 1 596 ? 54.216 -5.717 -1.188 1.00 27.10 ? 612 CYS A N 1 ATOM 4884 C CA . CYS A 1 596 ? 54.153 -4.243 -1.234 1.00 28.39 ? 612 CYS A CA 1 ATOM 4885 C C . CYS A 1 596 ? 55.560 -3.694 -1.368 1.00 29.99 ? 612 CYS A C 1 ATOM 4886 O O . CYS A 1 596 ? 56.352 -3.780 -0.435 1.00 29.78 ? 612 CYS A O 1 ATOM 4887 C CB . CYS A 1 596 ? 53.459 -3.628 -0.004 1.00 26.92 ? 612 CYS A CB 1 ATOM 4888 S SG . CYS A 1 596 ? 52.831 -1.930 -0.230 1.00 25.91 ? 612 CYS A SG 1 ATOM 4889 N N . VAL A 1 597 ? 55.849 -3.139 -2.540 1.00 32.48 ? 613 VAL A N 1 ATOM 4890 C CA . VAL A 1 597 ? 57.177 -2.625 -2.888 1.00 36.25 ? 613 VAL A CA 1 ATOM 4891 C C . VAL A 1 597 ? 57.374 -1.178 -2.423 1.00 39.11 ? 613 VAL A C 1 ATOM 4892 O O . VAL A 1 597 ? 56.563 -0.300 -2.733 1.00 38.29 ? 613 VAL A O 1 ATOM 4893 C CB . VAL A 1 597 ? 57.417 -2.736 -4.417 1.00 35.94 ? 613 VAL A CB 1 ATOM 4894 C CG1 . VAL A 1 597 ? 58.582 -1.861 -4.879 1.00 37.15 ? 613 VAL A CG1 1 ATOM 4895 C CG2 . VAL A 1 597 ? 57.657 -4.188 -4.797 1.00 36.45 ? 613 VAL A CG2 1 ATOM 4896 N N . SER A 1 598 ? 58.453 -0.949 -1.674 1.00 43.72 ? 614 SER A N 1 ATOM 4897 C CA . SER A 1 598 ? 58.888 0.399 -1.292 1.00 47.63 ? 614 SER A CA 1 ATOM 4898 C C . SER A 1 598 ? 59.238 1.243 -2.516 1.00 48.77 ? 614 SER A C 1 ATOM 4899 O O . SER A 1 598 ? 59.241 2.474 -2.447 1.00 53.59 ? 614 SER A O 1 ATOM 4900 C CB . SER A 1 598 ? 60.102 0.327 -0.371 1.00 49.24 ? 614 SER A CB 1 ATOM 4901 O OG . SER A 1 598 ? 59.721 -0.043 0.935 1.00 49.12 ? 614 SER A OG 1 HETATM 4902 ZN ZN . ZN B 2 . ? 26.653 -2.326 13.616 1.00 24.08 ? 1616 ZN A ZN 1 HETATM 4903 C C1 . NAG C 3 . ? 42.540 24.238 24.644 1.00 26.31 ? 1617 NAG A C1 1 HETATM 4904 C C2 . NAG C 3 . ? 41.214 24.887 25.064 1.00 27.22 ? 1617 NAG A C2 1 HETATM 4905 C C3 . NAG C 3 . ? 41.287 26.407 24.974 1.00 27.99 ? 1617 NAG A C3 1 HETATM 4906 C C4 . NAG C 3 . ? 42.539 26.950 25.659 1.00 28.62 ? 1617 NAG A C4 1 HETATM 4907 C C5 . NAG C 3 . ? 43.790 26.196 25.197 1.00 27.70 ? 1617 NAG A C5 1 HETATM 4908 C C6 . NAG C 3 . ? 45.026 26.642 25.962 1.00 27.49 ? 1617 NAG A C6 1 HETATM 4909 C C7 . NAG C 3 . ? 39.157 23.627 24.669 1.00 28.69 ? 1617 NAG A C7 1 HETATM 4910 C C8 . NAG C 3 . ? 38.100 23.227 23.670 1.00 28.58 ? 1617 NAG A C8 1 HETATM 4911 N N2 . NAG C 3 . ? 40.123 24.421 24.225 1.00 27.55 ? 1617 NAG A N2 1 HETATM 4912 O O3 . NAG C 3 . ? 40.139 26.953 25.575 1.00 28.02 ? 1617 NAG A O3 1 HETATM 4913 O O4 . NAG C 3 . ? 42.663 28.312 25.312 1.00 31.60 ? 1617 NAG A O4 1 HETATM 4914 O O5 . NAG C 3 . ? 43.654 24.789 25.339 1.00 26.66 ? 1617 NAG A O5 1 HETATM 4915 O O6 . NAG C 3 . ? 46.138 26.044 25.352 1.00 27.14 ? 1617 NAG A O6 1 HETATM 4916 O O7 . NAG C 3 . ? 39.105 23.221 25.836 1.00 29.05 ? 1617 NAG A O7 1 HETATM 4917 C C1 . NAG D 3 . ? 42.627 29.186 26.462 1.00 34.29 ? 1618 NAG A C1 1 HETATM 4918 C C2 . NAG D 3 . ? 43.080 30.573 26.006 1.00 36.80 ? 1618 NAG A C2 1 HETATM 4919 C C3 . NAG D 3 . ? 43.054 31.552 27.181 1.00 37.64 ? 1618 NAG A C3 1 HETATM 4920 C C4 . NAG D 3 . ? 41.679 31.580 27.853 1.00 39.30 ? 1618 NAG A C4 1 HETATM 4921 C C5 . NAG D 3 . ? 41.178 30.160 28.129 1.00 37.81 ? 1618 NAG A C5 1 HETATM 4922 C C6 . NAG D 3 . ? 39.706 30.200 28.501 1.00 38.85 ? 1618 NAG A C6 1 HETATM 4923 C C7 . NAG D 3 . ? 45.586 30.405 25.759 1.00 39.82 ? 1618 NAG A C7 1 HETATM 4924 C C8 . NAG D 3 . ? 46.703 30.315 24.754 1.00 38.63 ? 1618 NAG A C8 1 HETATM 4925 N N2 . NAG D 3 . ? 44.342 30.493 25.265 1.00 36.99 ? 1618 NAG A N2 1 HETATM 4926 O O3 . NAG D 3 . ? 43.372 32.835 26.700 1.00 37.85 ? 1618 NAG A O3 1 HETATM 4927 O O4 . NAG D 3 . ? 41.761 32.237 29.108 1.00 43.66 ? 1618 NAG A O4 1 HETATM 4928 O O5 . NAG D 3 . ? 41.338 29.274 27.033 1.00 35.35 ? 1618 NAG A O5 1 HETATM 4929 O O6 . NAG D 3 . ? 39.513 29.191 29.458 1.00 41.37 ? 1618 NAG A O6 1 HETATM 4930 O O7 . NAG D 3 . ? 45.864 30.395 26.964 1.00 41.92 ? 1618 NAG A O7 1 HETATM 4931 C C1 . BMA E 4 . ? 41.347 33.622 29.065 1.00 49.03 ? 1619 BMA A C1 1 HETATM 4932 C C2 . BMA E 4 . ? 40.722 34.005 30.406 1.00 50.88 ? 1619 BMA A C2 1 HETATM 4933 C C3 . BMA E 4 . ? 40.373 35.500 30.455 1.00 53.56 ? 1619 BMA A C3 1 HETATM 4934 C C4 . BMA E 4 . ? 41.552 36.366 29.995 1.00 55.83 ? 1619 BMA A C4 1 HETATM 4935 C C5 . BMA E 4 . ? 42.085 35.882 28.645 1.00 57.44 ? 1619 BMA A C5 1 HETATM 4936 C C6 . BMA E 4 . ? 43.272 36.720 28.160 1.00 61.95 ? 1619 BMA A C6 1 HETATM 4937 O O2 . BMA E 4 . ? 41.642 33.675 31.465 1.00 50.08 ? 1619 BMA A O2 1 HETATM 4938 O O3 . BMA E 4 . ? 40.019 35.889 31.792 1.00 54.31 ? 1619 BMA A O3 1 HETATM 4939 O O4 . BMA E 4 . ? 41.145 37.736 29.916 1.00 57.08 ? 1619 BMA A O4 1 HETATM 4940 O O5 . BMA E 4 . ? 42.448 34.498 28.775 1.00 52.95 ? 1619 BMA A O5 1 HETATM 4941 O O6 . BMA E 4 . ? 44.141 35.938 27.327 1.00 67.67 ? 1619 BMA A O6 1 HETATM 4942 C C1 . MAN F 5 . ? 44.666 36.731 26.241 1.00 73.47 ? 1620 MAN A C1 1 HETATM 4943 C C2 . MAN F 5 . ? 44.038 36.319 24.896 1.00 77.54 ? 1620 MAN A C2 1 HETATM 4944 C C3 . MAN F 5 . ? 44.723 35.096 24.260 1.00 78.40 ? 1620 MAN A C3 1 HETATM 4945 C C4 . MAN F 5 . ? 46.246 35.203 24.310 1.00 78.31 ? 1620 MAN A C4 1 HETATM 4946 C C5 . MAN F 5 . ? 46.720 35.557 25.725 1.00 77.78 ? 1620 MAN A C5 1 HETATM 4947 C C6 . MAN F 5 . ? 48.229 35.767 25.765 1.00 79.22 ? 1620 MAN A C6 1 HETATM 4948 O O2 . MAN F 5 . ? 44.055 37.418 24.008 1.00 81.40 ? 1620 MAN A O2 1 HETATM 4949 O O3 . MAN F 5 . ? 44.306 34.900 22.920 1.00 77.27 ? 1620 MAN A O3 1 HETATM 4950 O O4 . MAN F 5 . ? 46.794 33.975 23.885 1.00 78.62 ? 1620 MAN A O4 1 HETATM 4951 O O5 . MAN F 5 . ? 46.089 36.742 26.193 1.00 75.03 ? 1620 MAN A O5 1 HETATM 4952 O O6 . MAN F 5 . ? 48.609 36.120 27.076 1.00 80.70 ? 1620 MAN A O6 1 HETATM 4953 C C1 . MAN G 5 . ? 38.584 35.969 31.969 1.00 55.03 ? 1623 MAN A C1 1 HETATM 4954 C C2 . MAN G 5 . ? 38.243 37.031 33.026 1.00 55.18 ? 1623 MAN A C2 1 HETATM 4955 C C3 . MAN G 5 . ? 38.720 36.571 34.410 1.00 55.39 ? 1623 MAN A C3 1 HETATM 4956 C C4 . MAN G 5 . ? 38.240 35.150 34.717 1.00 54.97 ? 1623 MAN A C4 1 HETATM 4957 C C5 . MAN G 5 . ? 38.504 34.188 33.541 1.00 54.36 ? 1623 MAN A C5 1 HETATM 4958 C C6 . MAN G 5 . ? 37.892 32.803 33.723 1.00 55.35 ? 1623 MAN A C6 1 HETATM 4959 O O2 . MAN G 5 . ? 36.849 37.280 33.028 1.00 55.26 ? 1623 MAN A O2 1 HETATM 4960 O O3 . MAN G 5 . ? 38.306 37.470 35.424 1.00 56.71 ? 1623 MAN A O3 1 HETATM 4961 O O4 . MAN G 5 . ? 38.876 34.693 35.892 1.00 53.53 ? 1623 MAN A O4 1 HETATM 4962 O O5 . MAN G 5 . ? 37.998 34.728 32.330 1.00 53.68 ? 1623 MAN A O5 1 HETATM 4963 O O6 . MAN G 5 . ? 36.900 32.847 34.723 1.00 57.00 ? 1623 MAN A O6 1 HETATM 4964 C C1 . BMA H 4 . ? 36.393 31.533 35.036 1.00 61.09 ? 1624 BMA A C1 1 HETATM 4965 C C2 . BMA H 4 . ? 37.149 30.907 36.220 1.00 62.39 ? 1624 BMA A C2 1 HETATM 4966 C C3 . BMA H 4 . ? 36.415 31.138 37.540 1.00 62.81 ? 1624 BMA A C3 1 HETATM 4967 C C4 . BMA H 4 . ? 35.646 32.454 37.479 1.00 62.88 ? 1624 BMA A C4 1 HETATM 4968 C C5 . BMA H 4 . ? 34.536 32.306 36.430 1.00 64.08 ? 1624 BMA A C5 1 HETATM 4969 C C6 . BMA H 4 . ? 33.981 33.662 36.009 1.00 64.91 ? 1624 BMA A C6 1 HETATM 4970 O O2 . BMA H 4 . ? 38.497 31.384 36.328 1.00 69.68 ? 1624 BMA A O2 1 HETATM 4971 O O3 . BMA H 4 . ? 37.317 31.026 38.650 1.00 60.41 ? 1624 BMA A O3 1 HETATM 4972 O O4 . BMA H 4 . ? 35.087 32.778 38.753 1.00 63.95 ? 1624 BMA A O4 1 HETATM 4973 O O5 . BMA H 4 . ? 34.969 31.533 35.281 1.00 62.01 ? 1624 BMA A O5 1 HETATM 4974 O O6 . BMA H 4 . ? 32.554 33.580 35.968 1.00 66.97 ? 1624 BMA A O6 1 HETATM 4975 C C1 . NAG I 3 . ? 8.425 -8.330 30.864 0.50 40.22 ? 1621 NAG A C1 1 HETATM 4976 C C2 . NAG I 3 . ? 8.361 -9.081 32.189 0.50 41.42 ? 1621 NAG A C2 1 HETATM 4977 C C3 . NAG I 3 . ? 7.597 -8.261 33.218 0.50 43.05 ? 1621 NAG A C3 1 HETATM 4978 C C4 . NAG I 3 . ? 8.244 -6.892 33.325 0.50 42.59 ? 1621 NAG A C4 1 HETATM 4979 C C5 . NAG I 3 . ? 8.268 -6.241 31.949 0.50 42.15 ? 1621 NAG A C5 1 HETATM 4980 C C6 . NAG I 3 . ? 8.941 -4.880 32.008 0.50 42.18 ? 1621 NAG A C6 1 HETATM 4981 C C7 . NAG I 3 . ? 8.330 -11.484 32.419 0.50 41.67 ? 1621 NAG A C7 1 HETATM 4982 C C8 . NAG I 3 . ? 7.614 -12.773 32.151 0.50 42.25 ? 1621 NAG A C8 1 HETATM 4983 N N2 . NAG I 3 . ? 7.744 -10.375 31.986 0.50 41.83 ? 1621 NAG A N2 1 HETATM 4984 O O3 . NAG I 3 . ? 7.615 -8.896 34.477 0.50 44.34 ? 1621 NAG A O3 1 HETATM 4985 O O4 . NAG I 3 . ? 7.521 -6.096 34.236 0.50 43.85 ? 1621 NAG A O4 1 HETATM 4986 O O5 . NAG I 3 . ? 8.990 -7.056 31.059 0.50 40.26 ? 1621 NAG A O5 1 HETATM 4987 O O6 . NAG I 3 . ? 9.017 -4.504 33.363 0.50 44.13 ? 1621 NAG A O6 1 HETATM 4988 O O7 . NAG I 3 . ? 9.405 -11.474 33.012 0.50 41.72 ? 1621 NAG A O7 1 HETATM 4989 C C1 . NAG J 3 . ? 16.498 11.270 -5.951 0.50 38.65 ? 1622 NAG A C1 1 HETATM 4990 C C2 . NAG J 3 . ? 15.005 10.990 -6.121 0.50 39.22 ? 1622 NAG A C2 1 HETATM 4991 C C3 . NAG J 3 . ? 14.303 11.907 -7.121 0.50 40.33 ? 1622 NAG A C3 1 HETATM 4992 C C4 . NAG J 3 . ? 14.864 13.324 -7.150 0.50 40.49 ? 1622 NAG A C4 1 HETATM 4993 C C5 . NAG J 3 . ? 16.382 13.291 -7.097 0.50 39.99 ? 1622 NAG A C5 1 HETATM 4994 C C6 . NAG J 3 . ? 16.980 14.697 -7.199 0.50 39.99 ? 1622 NAG A C6 1 HETATM 4995 C C7 . NAG J 3 . ? 14.061 8.767 -5.886 0.50 38.41 ? 1622 NAG A C7 1 HETATM 4996 C C8 . NAG J 3 . ? 13.953 7.385 -6.457 0.50 38.32 ? 1622 NAG A C8 1 HETATM 4997 N N2 . NAG J 3 . ? 14.818 9.622 -6.561 0.50 38.81 ? 1622 NAG A N2 1 HETATM 4998 O O3 . NAG J 3 . ? 12.940 11.969 -6.772 0.50 40.84 ? 1622 NAG A O3 1 HETATM 4999 O O4 . NAG J 3 . ? 14.443 13.976 -8.327 0.50 41.95 ? 1622 NAG A O4 1 HETATM 5000 O O5 . NAG J 3 . ? 16.734 12.661 -5.885 0.50 38.96 ? 1622 NAG A O5 1 HETATM 5001 O O6 . NAG J 3 . ? 17.974 14.891 -6.215 0.50 38.04 ? 1622 NAG A O6 1 HETATM 5002 O O7 . NAG J 3 . ? 13.473 9.070 -4.850 0.50 38.12 ? 1622 NAG A O7 1 HETATM 5003 O OAB . 3EF K 6 . ? 24.348 1.495 11.567 1.00 25.08 ? 1715 3EF A OAB 1 HETATM 5004 C CAH . 3EF K 6 . ? 25.173 4.682 17.613 1.00 25.92 ? 1715 3EF A CAH 1 HETATM 5005 C CAK . 3EF K 6 . ? 24.236 5.247 16.744 1.00 26.43 ? 1715 3EF A CAK 1 HETATM 5006 C CAL . 3EF K 6 . ? 25.794 3.469 17.290 1.00 26.50 ? 1715 3EF A CAL 1 HETATM 5007 C CAQ . 3EF K 6 . ? 23.914 4.597 15.546 1.00 25.78 ? 1715 3EF A CAQ 1 HETATM 5008 C CAR . 3EF K 6 . ? 25.466 2.813 16.092 1.00 25.34 ? 1715 3EF A CAR 1 HETATM 5009 C CBB . 3EF K 6 . ? 24.191 2.719 14.016 1.00 25.02 ? 1715 3EF A CBB 1 HETATM 5010 O OBJ . 3EF K 6 . ? 25.407 2.186 13.463 1.00 24.73 ? 1715 3EF A OBJ 1 HETATM 5011 C CBM . 3EF K 6 . ? 25.376 1.547 12.253 1.00 24.57 ? 1715 3EF A CBM 1 HETATM 5012 C CBP . 3EF K 6 . ? 24.518 3.374 15.228 1.00 25.78 ? 1715 3EF A CBP 1 HETATM 5013 O OAD . 3EF K 6 . ? 27.902 -1.803 11.838 1.00 22.33 ? 1715 3EF A OAD 1 HETATM 5014 P PBY . 3EF K 6 . ? 26.685 -1.519 11.059 1.00 22.61 ? 1715 3EF A PBY 1 HETATM 5015 O OAG . 3EF K 6 . ? 25.374 -1.902 11.619 1.00 20.88 ? 1715 3EF A OAG 1 HETATM 5016 C CBX . 3EF K 6 . ? 26.629 0.259 10.575 1.00 22.17 ? 1715 3EF A CBX 1 HETATM 5017 N NBI . 3EF K 6 . ? 26.503 0.965 11.845 1.00 22.43 ? 1715 3EF A NBI 1 HETATM 5018 C CBE . 3EF K 6 . ? 27.880 0.815 9.838 1.00 21.62 ? 1715 3EF A CBE 1 HETATM 5019 C CBQ . 3EF K 6 . ? 27.762 2.223 9.651 1.00 22.25 ? 1715 3EF A CBQ 1 HETATM 5020 C CAS . 3EF K 6 . ? 27.117 2.743 8.523 1.00 22.66 ? 1715 3EF A CAS 1 HETATM 5021 C CAM . 3EF K 6 . ? 26.987 4.127 8.343 1.00 23.27 ? 1715 3EF A CAM 1 HETATM 5022 C CAI . 3EF K 6 . ? 27.520 5.021 9.281 1.00 23.41 ? 1715 3EF A CAI 1 HETATM 5023 C CAN . 3EF K 6 . ? 28.176 4.511 10.418 1.00 22.62 ? 1715 3EF A CAN 1 HETATM 5024 C CAT . 3EF K 6 . ? 28.294 3.129 10.588 1.00 21.63 ? 1715 3EF A CAT 1 HETATM 5025 O OAC . 3EF K 6 . ? 29.525 -2.579 9.209 1.00 23.28 ? 1715 3EF A OAC 1 HETATM 5026 C CAJ . 3EF K 6 . ? 26.953 -11.599 11.753 1.00 34.89 ? 1715 3EF A CAJ 1 HETATM 5027 C CAO . 3EF K 6 . ? 26.639 -10.337 12.273 1.00 34.07 ? 1715 3EF A CAO 1 HETATM 5028 C CAP . 3EF K 6 . ? 27.432 -11.712 10.444 1.00 33.16 ? 1715 3EF A CAP 1 HETATM 5029 C CAU . 3EF K 6 . ? 26.816 -9.185 11.496 1.00 32.24 ? 1715 3EF A CAU 1 HETATM 5030 C CAV . 3EF K 6 . ? 27.601 -10.561 9.675 1.00 33.70 ? 1715 3EF A CAV 1 HETATM 5031 C CBA . 3EF K 6 . ? 26.970 -6.981 9.618 1.00 31.05 ? 1715 3EF A CBA 1 HETATM 5032 C CBC . 3EF K 6 . ? 27.021 -4.684 8.419 1.00 25.82 ? 1715 3EF A CBC 1 HETATM 5033 C CBF . 3EF K 6 . ? 26.829 -2.396 9.411 1.00 21.59 ? 1715 3EF A CBF 1 HETATM 5034 N NBG . 3EF K 6 . ? 28.200 -8.248 8.302 1.00 32.84 ? 1715 3EF A NBG 1 HETATM 5035 O OBK . 3EF K 6 . ? 28.108 -6.846 7.749 1.00 31.77 ? 1715 3EF A OBK 1 HETATM 5036 C CBN . 3EF K 6 . ? 29.012 -3.635 9.590 1.00 23.61 ? 1715 3EF A CBN 1 HETATM 5037 C CBS . 3EF K 6 . ? 27.362 -6.175 8.612 1.00 29.27 ? 1715 3EF A CBS 1 HETATM 5038 C CBT . 3EF K 6 . ? 27.301 -9.290 10.192 1.00 32.57 ? 1715 3EF A CBT 1 HETATM 5039 C CBU . 3EF K 6 . ? 27.475 -8.215 9.419 1.00 31.94 ? 1715 3EF A CBU 1 HETATM 5040 C CBV . 3EF K 6 . ? 27.477 -3.788 9.593 1.00 23.82 ? 1715 3EF A CBV 1 HETATM 5041 N N . 3EF K 6 . ? 29.728 -4.710 9.978 1.00 24.14 ? 1715 3EF A N 1 HETATM 5042 C CA . 3EF K 6 . ? 31.219 -4.685 9.956 1.00 26.07 ? 1715 3EF A CA 1 HETATM 5043 C C . 3EF K 6 . ? 31.756 -4.638 8.500 1.00 25.83 ? 1715 3EF A C 1 HETATM 5044 O O . 3EF K 6 . ? 33.001 -4.537 8.345 1.00 23.91 ? 1715 3EF A O 1 HETATM 5045 C CB . 3EF K 6 . ? 31.886 -5.920 10.564 1.00 28.22 ? 1715 3EF A CB 1 HETATM 5046 C CG . 3EF K 6 . ? 31.209 -6.910 11.269 1.00 28.41 ? 1715 3EF A CG 1 HETATM 5047 C CD1 . 3EF K 6 . ? 31.271 -8.232 10.813 1.00 28.43 ? 1715 3EF A CD1 1 HETATM 5048 C CD2 . 3EF K 6 . ? 30.547 -6.600 12.463 1.00 28.50 ? 1715 3EF A CD2 1 HETATM 5049 C CE1 . 3EF K 6 . ? 30.638 -9.253 11.537 1.00 28.59 ? 1715 3EF A CE1 1 HETATM 5050 C CE2 . 3EF K 6 . ? 29.919 -7.618 13.183 1.00 28.88 ? 1715 3EF A CE2 1 HETATM 5051 C CZ . 3EF K 6 . ? 29.973 -8.935 12.727 1.00 28.25 ? 1715 3EF A CZ 1 HETATM 5052 O OH . 3EF K 6 . ? 29.360 -9.905 13.459 1.00 28.98 ? 1715 3EF A OH 1 HETATM 5053 O OXT . 3EF K 6 . ? 30.914 -4.719 7.572 1.00 26.40 ? 1715 3EF A OXT 1 HETATM 5054 O O . HOH L 7 . ? 28.532 30.976 36.400 1.00 43.76 ? 2001 HOH A O 1 HETATM 5055 O O . HOH L 7 . ? 18.060 18.620 33.166 1.00 42.85 ? 2002 HOH A O 1 HETATM 5056 O O . HOH L 7 . ? 18.705 25.699 26.906 1.00 35.65 ? 2003 HOH A O 1 HETATM 5057 O O . HOH L 7 . ? 18.813 17.336 30.714 1.00 30.91 ? 2004 HOH A O 1 HETATM 5058 O O . HOH L 7 . ? 16.359 16.194 30.081 1.00 48.16 ? 2005 HOH A O 1 HETATM 5059 O O . HOH L 7 . ? 26.588 12.402 12.016 1.00 56.26 ? 2006 HOH A O 1 HETATM 5060 O O . HOH L 7 . ? 17.185 16.298 1.794 1.00 40.20 ? 2007 HOH A O 1 HETATM 5061 O O . HOH L 7 . ? 16.319 15.340 25.492 1.00 35.04 ? 2008 HOH A O 1 HETATM 5062 O O . HOH L 7 . ? 13.059 17.102 21.322 1.00 34.94 ? 2009 HOH A O 1 HETATM 5063 O O . HOH L 7 . ? 11.425 17.754 13.122 1.00 34.18 ? 2010 HOH A O 1 HETATM 5064 O O . HOH L 7 . ? 29.427 14.036 6.764 1.00 29.41 ? 2011 HOH A O 1 HETATM 5065 O O . HOH L 7 . ? 19.724 20.890 12.374 1.00 36.35 ? 2012 HOH A O 1 HETATM 5066 O O . HOH L 7 . ? 20.683 23.373 13.540 1.00 32.34 ? 2013 HOH A O 1 HETATM 5067 O O . HOH L 7 . ? 23.781 16.087 16.988 1.00 33.17 ? 2014 HOH A O 1 HETATM 5068 O O . HOH L 7 . ? 11.772 11.944 11.505 1.00 32.80 ? 2015 HOH A O 1 HETATM 5069 O O . HOH L 7 . ? 30.948 29.394 12.580 1.00 42.43 ? 2016 HOH A O 1 HETATM 5070 O O . HOH L 7 . ? 16.270 17.541 6.346 1.00 34.97 ? 2017 HOH A O 1 HETATM 5071 O O . HOH L 7 . ? 22.551 13.112 12.103 1.00 33.34 ? 2018 HOH A O 1 HETATM 5072 O O . HOH L 7 . ? 24.903 15.134 14.581 1.00 46.75 ? 2019 HOH A O 1 HETATM 5073 O O . HOH L 7 . ? 27.227 14.957 11.313 1.00 54.24 ? 2020 HOH A O 1 HETATM 5074 O O . HOH L 7 . ? 26.816 18.846 12.224 1.00 44.19 ? 2021 HOH A O 1 HETATM 5075 O O . HOH L 7 . ? 15.826 15.633 4.207 1.00 40.43 ? 2022 HOH A O 1 HETATM 5076 O O . HOH L 7 . ? 14.676 12.112 4.000 1.00 45.75 ? 2023 HOH A O 1 HETATM 5077 O O . HOH L 7 . ? 19.873 15.294 1.286 1.00 32.76 ? 2024 HOH A O 1 HETATM 5078 O O . HOH L 7 . ? 24.380 9.964 4.015 1.00 29.71 ? 2025 HOH A O 1 HETATM 5079 O O . HOH L 7 . ? 13.170 7.177 1.690 1.00 40.62 ? 2026 HOH A O 1 HETATM 5080 O O . HOH L 7 . ? 11.754 6.279 3.874 1.00 41.49 ? 2027 HOH A O 1 HETATM 5081 O O . HOH L 7 . ? 15.785 11.134 -1.868 1.00 46.01 ? 2028 HOH A O 1 HETATM 5082 O O . HOH L 7 . ? 27.538 12.764 -4.390 1.00 38.91 ? 2029 HOH A O 1 HETATM 5083 O O . HOH L 7 . ? 30.612 15.810 13.801 1.00 54.40 ? 2030 HOH A O 1 HETATM 5084 O O . HOH L 7 . ? 31.518 13.019 13.519 1.00 49.92 ? 2031 HOH A O 1 HETATM 5085 O O . HOH L 7 . ? 30.918 15.041 17.090 1.00 51.35 ? 2032 HOH A O 1 HETATM 5086 O O . HOH L 7 . ? 35.428 14.102 15.977 1.00 34.96 ? 2033 HOH A O 1 HETATM 5087 O O . HOH L 7 . ? 32.346 10.511 12.623 1.00 48.84 ? 2034 HOH A O 1 HETATM 5088 O O . HOH L 7 . ? 20.940 8.253 -7.757 1.00 39.80 ? 2035 HOH A O 1 HETATM 5089 O O . HOH L 7 . ? 25.851 12.743 -6.699 1.00 41.57 ? 2036 HOH A O 1 HETATM 5090 O O . HOH L 7 . ? 23.412 14.290 -9.506 1.00 45.90 ? 2037 HOH A O 1 HETATM 5091 O O . HOH L 7 . ? 30.639 11.063 7.154 1.00 44.87 ? 2038 HOH A O 1 HETATM 5092 O O . HOH L 7 . ? 25.842 7.437 7.118 1.00 37.25 ? 2039 HOH A O 1 HETATM 5093 O O . HOH L 7 . ? 30.920 14.002 -4.408 1.00 50.49 ? 2040 HOH A O 1 HETATM 5094 O O . HOH L 7 . ? 32.138 16.300 -2.800 1.00 40.90 ? 2041 HOH A O 1 HETATM 5095 O O . HOH L 7 . ? 29.043 -1.073 -1.774 1.00 34.77 ? 2042 HOH A O 1 HETATM 5096 O O . HOH L 7 . ? 29.050 12.034 3.428 1.00 38.65 ? 2043 HOH A O 1 HETATM 5097 O O . HOH L 7 . ? 29.519 14.924 4.218 1.00 23.45 ? 2044 HOH A O 1 HETATM 5098 O O . HOH L 7 . ? 24.962 25.883 5.531 1.00 41.31 ? 2045 HOH A O 1 HETATM 5099 O O . HOH L 7 . ? 20.589 -7.425 -4.249 1.00 30.54 ? 2046 HOH A O 1 HETATM 5100 O O . HOH L 7 . ? 28.771 -2.393 0.545 1.00 31.89 ? 2047 HOH A O 1 HETATM 5101 O O . HOH L 7 . ? 20.476 -6.533 -6.776 1.00 33.80 ? 2048 HOH A O 1 HETATM 5102 O O . HOH L 7 . ? 21.312 -10.425 -4.942 1.00 49.31 ? 2049 HOH A O 1 HETATM 5103 O O . HOH L 7 . ? 27.402 15.185 8.325 1.00 46.54 ? 2050 HOH A O 1 HETATM 5104 O O . HOH L 7 . ? 29.270 25.816 9.836 1.00 31.88 ? 2051 HOH A O 1 HETATM 5105 O O . HOH L 7 . ? 22.876 27.380 13.001 1.00 28.51 ? 2052 HOH A O 1 HETATM 5106 O O . HOH L 7 . ? 28.463 29.875 16.084 1.00 44.77 ? 2053 HOH A O 1 HETATM 5107 O O . HOH L 7 . ? 45.256 2.517 -10.163 1.00 39.49 ? 2054 HOH A O 1 HETATM 5108 O O . HOH L 7 . ? 28.203 21.525 21.475 1.00 45.17 ? 2055 HOH A O 1 HETATM 5109 O O . HOH L 7 . ? 32.660 27.520 20.353 1.00 40.86 ? 2056 HOH A O 1 HETATM 5110 O O . HOH L 7 . ? 30.506 26.715 11.988 1.00 34.59 ? 2057 HOH A O 1 HETATM 5111 O O . HOH L 7 . ? 49.114 14.250 6.918 1.00 36.76 ? 2058 HOH A O 1 HETATM 5112 O O . HOH L 7 . ? 46.071 22.267 9.180 1.00 46.27 ? 2059 HOH A O 1 HETATM 5113 O O . HOH L 7 . ? 48.399 17.863 9.224 1.00 38.58 ? 2060 HOH A O 1 HETATM 5114 O O . HOH L 7 . ? 46.864 19.813 12.774 1.00 33.53 ? 2061 HOH A O 1 HETATM 5115 O O . HOH L 7 . ? 50.653 14.887 11.467 1.00 38.49 ? 2062 HOH A O 1 HETATM 5116 O O . HOH L 7 . ? 43.708 25.388 14.316 1.00 31.91 ? 2063 HOH A O 1 HETATM 5117 O O . HOH L 7 . ? 46.467 22.238 13.941 1.00 30.43 ? 2064 HOH A O 1 HETATM 5118 O O . HOH L 7 . ? 41.502 27.071 13.433 1.00 44.99 ? 2065 HOH A O 1 HETATM 5119 O O . HOH L 7 . ? 32.701 26.362 32.945 1.00 30.58 ? 2066 HOH A O 1 HETATM 5120 O O . HOH L 7 . ? 32.680 24.467 29.462 1.00 37.65 ? 2067 HOH A O 1 HETATM 5121 O O . HOH L 7 . ? 35.308 13.627 18.691 1.00 37.50 ? 2068 HOH A O 1 HETATM 5122 O O . HOH L 7 . ? 43.679 12.005 25.404 1.00 30.97 ? 2069 HOH A O 1 HETATM 5123 O O . HOH L 7 . ? 43.210 8.029 25.224 1.00 29.75 ? 2070 HOH A O 1 HETATM 5124 O O . HOH L 7 . ? 51.113 8.122 21.109 1.00 36.98 ? 2071 HOH A O 1 HETATM 5125 O O . HOH L 7 . ? 51.025 11.395 18.907 1.00 30.76 ? 2072 HOH A O 1 HETATM 5126 O O . HOH L 7 . ? 34.371 10.755 16.722 1.00 27.73 ? 2073 HOH A O 1 HETATM 5127 O O . HOH L 7 . ? 33.639 25.752 37.504 1.00 26.24 ? 2074 HOH A O 1 HETATM 5128 O O . HOH L 7 . ? 33.418 27.973 40.554 1.00 41.34 ? 2075 HOH A O 1 HETATM 5129 O O . HOH L 7 . ? 37.154 16.640 26.277 1.00 36.39 ? 2076 HOH A O 1 HETATM 5130 O O . HOH L 7 . ? 34.364 4.510 34.915 1.00 35.90 ? 2077 HOH A O 1 HETATM 5131 O O . HOH L 7 . ? 33.710 24.727 34.936 1.00 21.46 ? 2078 HOH A O 1 HETATM 5132 O O . HOH L 7 . ? 36.708 20.409 28.615 1.00 33.07 ? 2079 HOH A O 1 HETATM 5133 O O . HOH L 7 . ? 48.945 2.775 25.512 1.00 25.57 ? 2080 HOH A O 1 HETATM 5134 O O . HOH L 7 . ? 51.462 3.142 18.747 1.00 42.51 ? 2081 HOH A O 1 HETATM 5135 O O . HOH L 7 . ? 51.887 2.366 22.821 1.00 41.41 ? 2082 HOH A O 1 HETATM 5136 O O . HOH L 7 . ? 51.293 3.163 27.184 1.00 23.84 ? 2083 HOH A O 1 HETATM 5137 O O . HOH L 7 . ? 43.135 -8.927 30.229 1.00 32.28 ? 2084 HOH A O 1 HETATM 5138 O O . HOH L 7 . ? 41.602 -4.973 33.169 1.00 41.24 ? 2085 HOH A O 1 HETATM 5139 O O . HOH L 7 . ? 52.801 -10.199 24.183 1.00 51.30 ? 2086 HOH A O 1 HETATM 5140 O O . HOH L 7 . ? 25.817 13.279 42.139 1.00 36.77 ? 2087 HOH A O 1 HETATM 5141 O O . HOH L 7 . ? 29.636 14.812 43.243 1.00 45.74 ? 2088 HOH A O 1 HETATM 5142 O O . HOH L 7 . ? 50.908 -15.160 19.482 1.00 45.81 ? 2089 HOH A O 1 HETATM 5143 O O . HOH L 7 . ? 51.740 -11.350 21.766 1.00 35.47 ? 2090 HOH A O 1 HETATM 5144 O O . HOH L 7 . ? 45.881 -20.568 23.036 1.00 35.88 ? 2091 HOH A O 1 HETATM 5145 O O . HOH L 7 . ? 42.275 -18.996 23.794 1.00 37.41 ? 2092 HOH A O 1 HETATM 5146 O O . HOH L 7 . ? 23.917 12.822 40.033 1.00 39.31 ? 2093 HOH A O 1 HETATM 5147 O O . HOH L 7 . ? 49.357 -21.918 20.590 1.00 32.76 ? 2094 HOH A O 1 HETATM 5148 O O . HOH L 7 . ? 30.142 13.250 36.314 1.00 34.52 ? 2095 HOH A O 1 HETATM 5149 O O . HOH L 7 . ? 33.058 15.207 38.134 1.00 25.77 ? 2096 HOH A O 1 HETATM 5150 O O . HOH L 7 . ? 51.952 -17.712 19.840 1.00 42.99 ? 2097 HOH A O 1 HETATM 5151 O O . HOH L 7 . ? 50.721 -26.935 20.086 1.00 35.65 ? 2098 HOH A O 1 HETATM 5152 O O . HOH L 7 . ? 51.961 -26.922 16.417 1.00 41.80 ? 2099 HOH A O 1 HETATM 5153 O O . HOH L 7 . ? 26.042 10.513 36.892 1.00 44.66 ? 2100 HOH A O 1 HETATM 5154 O O . HOH L 7 . ? 21.238 9.651 35.148 1.00 44.53 ? 2101 HOH A O 1 HETATM 5155 O O . HOH L 7 . ? 19.513 12.392 33.831 1.00 38.88 ? 2102 HOH A O 1 HETATM 5156 O O . HOH L 7 . ? 23.921 10.173 35.021 1.00 36.73 ? 2103 HOH A O 1 HETATM 5157 O O . HOH L 7 . ? 19.716 15.895 36.593 1.00 46.01 ? 2104 HOH A O 1 HETATM 5158 O O . HOH L 7 . ? 31.678 15.140 33.919 1.00 35.71 ? 2105 HOH A O 1 HETATM 5159 O O . HOH L 7 . ? 30.239 13.307 29.745 1.00 37.49 ? 2106 HOH A O 1 HETATM 5160 O O . HOH L 7 . ? 27.595 10.784 28.400 1.00 34.74 ? 2107 HOH A O 1 HETATM 5161 O O . HOH L 7 . ? 30.454 10.822 34.422 1.00 35.90 ? 2108 HOH A O 1 HETATM 5162 O O . HOH L 7 . ? 28.401 5.920 28.696 1.00 21.48 ? 2109 HOH A O 1 HETATM 5163 O O . HOH L 7 . ? 37.758 13.434 29.769 1.00 49.67 ? 2110 HOH A O 1 HETATM 5164 O O . HOH L 7 . ? 28.388 18.099 21.820 1.00 45.04 ? 2111 HOH A O 1 HETATM 5165 O O . HOH L 7 . ? 34.358 23.331 23.575 1.00 48.98 ? 2112 HOH A O 1 HETATM 5166 O O . HOH L 7 . ? 35.862 20.987 22.329 1.00 54.55 ? 2113 HOH A O 1 HETATM 5167 O O . HOH L 7 . ? 33.349 10.043 26.521 1.00 45.35 ? 2114 HOH A O 1 HETATM 5168 O O . HOH L 7 . ? 35.415 16.960 20.708 1.00 33.19 ? 2115 HOH A O 1 HETATM 5169 O O . HOH L 7 . ? 28.488 -14.653 12.513 1.00 32.13 ? 2116 HOH A O 1 HETATM 5170 O O . HOH L 7 . ? 32.819 14.960 15.029 1.00 28.60 ? 2117 HOH A O 1 HETATM 5171 O O . HOH L 7 . ? 35.221 9.927 12.716 1.00 27.34 ? 2118 HOH A O 1 HETATM 5172 O O . HOH L 7 . ? 36.421 25.899 18.015 1.00 38.63 ? 2119 HOH A O 1 HETATM 5173 O O . HOH L 7 . ? 39.920 28.287 15.093 1.00 40.59 ? 2120 HOH A O 1 HETATM 5174 O O . HOH L 7 . ? 37.698 -36.842 6.736 1.00 49.17 ? 2121 HOH A O 1 HETATM 5175 O O . HOH L 7 . ? 35.895 29.869 8.137 1.00 39.24 ? 2122 HOH A O 1 HETATM 5176 O O . HOH L 7 . ? 30.474 25.107 7.734 1.00 31.44 ? 2123 HOH A O 1 HETATM 5177 O O . HOH L 7 . ? 29.500 26.591 5.503 1.00 39.88 ? 2124 HOH A O 1 HETATM 5178 O O . HOH L 7 . ? 25.841 -33.442 6.025 1.00 42.27 ? 2125 HOH A O 1 HETATM 5179 O O . HOH L 7 . ? 20.268 -27.569 1.648 1.00 43.84 ? 2126 HOH A O 1 HETATM 5180 O O . HOH L 7 . ? 23.893 -22.521 -0.976 1.00 43.69 ? 2127 HOH A O 1 HETATM 5181 O O . HOH L 7 . ? 22.115 -27.475 -0.592 1.00 42.35 ? 2128 HOH A O 1 HETATM 5182 O O . HOH L 7 . ? 35.066 25.539 2.229 1.00 38.83 ? 2129 HOH A O 1 HETATM 5183 O O . HOH L 7 . ? 38.937 25.292 3.928 1.00 40.16 ? 2130 HOH A O 1 HETATM 5184 O O . HOH L 7 . ? 7.754 -9.623 0.882 1.00 44.62 ? 2131 HOH A O 1 HETATM 5185 O O . HOH L 7 . ? 30.191 21.277 2.501 1.00 32.16 ? 2132 HOH A O 1 HETATM 5186 O O . HOH L 7 . ? 39.292 20.038 -0.801 1.00 38.75 ? 2133 HOH A O 1 HETATM 5187 O O . HOH L 7 . ? 5.306 -4.728 7.010 1.00 34.87 ? 2134 HOH A O 1 HETATM 5188 O O . HOH L 7 . ? 5.529 -7.387 22.275 1.00 37.04 ? 2135 HOH A O 1 HETATM 5189 O O . HOH L 7 . ? 12.648 -6.674 31.112 1.00 40.13 ? 2136 HOH A O 1 HETATM 5190 O O . HOH L 7 . ? 30.657 10.078 4.756 1.00 41.62 ? 2137 HOH A O 1 HETATM 5191 O O . HOH L 7 . ? 33.250 9.803 4.057 1.00 23.03 ? 2138 HOH A O 1 HETATM 5192 O O . HOH L 7 . ? 33.566 11.027 -5.594 1.00 40.73 ? 2139 HOH A O 1 HETATM 5193 O O . HOH L 7 . ? 36.085 4.818 -2.096 1.00 27.03 ? 2140 HOH A O 1 HETATM 5194 O O . HOH L 7 . ? 28.478 6.802 6.546 1.00 33.56 ? 2141 HOH A O 1 HETATM 5195 O O . HOH L 7 . ? 25.459 7.318 4.418 1.00 33.93 ? 2142 HOH A O 1 HETATM 5196 O O . HOH L 7 . ? 31.465 9.737 -7.086 1.00 41.05 ? 2143 HOH A O 1 HETATM 5197 O O . HOH L 7 . ? 33.139 5.147 -8.006 1.00 33.53 ? 2144 HOH A O 1 HETATM 5198 O O . HOH L 7 . ? 35.897 9.857 -7.316 1.00 43.75 ? 2145 HOH A O 1 HETATM 5199 O O . HOH L 7 . ? 36.559 4.961 -8.686 1.00 32.52 ? 2146 HOH A O 1 HETATM 5200 O O . HOH L 7 . ? 31.451 -0.678 -3.480 1.00 27.37 ? 2147 HOH A O 1 HETATM 5201 O O . HOH L 7 . ? 25.236 2.979 -6.045 1.00 37.10 ? 2148 HOH A O 1 HETATM 5202 O O . HOH L 7 . ? 27.855 0.820 -7.571 1.00 36.29 ? 2149 HOH A O 1 HETATM 5203 O O . HOH L 7 . ? 24.203 6.891 9.271 1.00 49.51 ? 2150 HOH A O 1 HETATM 5204 O O . HOH L 7 . ? 25.896 5.952 12.785 1.00 45.53 ? 2151 HOH A O 1 HETATM 5205 O O . HOH L 7 . ? 30.212 -1.202 -5.788 1.00 27.06 ? 2152 HOH A O 1 HETATM 5206 O O . HOH L 7 . ? 25.053 -0.217 -6.994 1.00 39.88 ? 2153 HOH A O 1 HETATM 5207 O O . HOH L 7 . ? 10.050 8.167 25.185 1.00 42.86 ? 2154 HOH A O 1 HETATM 5208 O O . HOH L 7 . ? 36.463 -3.163 -14.647 1.00 39.07 ? 2155 HOH A O 1 HETATM 5209 O O . HOH L 7 . ? 40.420 -17.929 -14.920 1.00 36.15 ? 2156 HOH A O 1 HETATM 5210 O O . HOH L 7 . ? 43.293 -14.685 -15.962 1.00 41.21 ? 2157 HOH A O 1 HETATM 5211 O O . HOH L 7 . ? 27.655 -2.058 -3.920 1.00 31.51 ? 2158 HOH A O 1 HETATM 5212 O O . HOH L 7 . ? 22.182 -6.702 -2.194 1.00 27.74 ? 2159 HOH A O 1 HETATM 5213 O O . HOH L 7 . ? 26.692 -8.569 -1.452 1.00 27.95 ? 2160 HOH A O 1 HETATM 5214 O O . HOH L 7 . ? 23.744 -6.910 1.123 1.00 28.20 ? 2161 HOH A O 1 HETATM 5215 O O . HOH L 7 . ? 26.805 -4.264 1.552 1.00 28.66 ? 2162 HOH A O 1 HETATM 5216 O O . HOH L 7 . ? 28.805 4.517 18.258 1.00 27.05 ? 2163 HOH A O 1 HETATM 5217 O O . HOH L 7 . ? 26.594 -10.882 -3.105 1.00 28.42 ? 2164 HOH A O 1 HETATM 5218 O O . HOH L 7 . ? 28.344 -11.970 -9.665 1.00 41.82 ? 2165 HOH A O 1 HETATM 5219 O O . HOH L 7 . ? 22.322 -5.149 -8.434 1.00 42.43 ? 2166 HOH A O 1 HETATM 5220 O O . HOH L 7 . ? 32.273 -12.243 0.077 1.00 39.30 ? 2167 HOH A O 1 HETATM 5221 O O . HOH L 7 . ? 27.369 -7.070 2.024 1.00 38.34 ? 2168 HOH A O 1 HETATM 5222 O O . HOH L 7 . ? 33.365 -9.749 0.373 1.00 23.87 ? 2169 HOH A O 1 HETATM 5223 O O . HOH L 7 . ? 30.669 -9.135 3.141 1.00 39.48 ? 2170 HOH A O 1 HETATM 5224 O O . HOH L 7 . ? 30.294 -5.592 2.769 1.00 37.83 ? 2171 HOH A O 1 HETATM 5225 O O . HOH L 7 . ? 27.713 -19.930 12.139 1.00 36.02 ? 2172 HOH A O 1 HETATM 5226 O O . HOH L 7 . ? 37.734 -16.141 -1.889 1.00 24.75 ? 2173 HOH A O 1 HETATM 5227 O O . HOH L 7 . ? 36.716 -18.531 -2.662 1.00 34.82 ? 2174 HOH A O 1 HETATM 5228 O O . HOH L 7 . ? 31.320 -22.245 -3.978 1.00 41.60 ? 2175 HOH A O 1 HETATM 5229 O O . HOH L 7 . ? 23.791 -18.426 -1.433 1.00 39.44 ? 2176 HOH A O 1 HETATM 5230 O O . HOH L 7 . ? 34.636 -21.567 -9.189 1.00 34.88 ? 2177 HOH A O 1 HETATM 5231 O O . HOH L 7 . ? 42.579 -19.817 -12.081 1.00 32.95 ? 2178 HOH A O 1 HETATM 5232 O O . HOH L 7 . ? 45.908 -16.386 -7.728 1.00 27.64 ? 2179 HOH A O 1 HETATM 5233 O O . HOH L 7 . ? 43.678 -12.711 -12.996 1.00 31.37 ? 2180 HOH A O 1 HETATM 5234 O O . HOH L 7 . ? 43.048 -18.721 -15.752 1.00 36.09 ? 2181 HOH A O 1 HETATM 5235 O O . HOH L 7 . ? 47.234 -19.776 -13.039 1.00 29.00 ? 2182 HOH A O 1 HETATM 5236 O O . HOH L 7 . ? 32.893 -13.387 -13.334 1.00 35.14 ? 2183 HOH A O 1 HETATM 5237 O O . HOH L 7 . ? 44.765 -9.385 -10.688 1.00 42.73 ? 2184 HOH A O 1 HETATM 5238 O O . HOH L 7 . ? 42.110 -6.892 -12.619 1.00 43.11 ? 2185 HOH A O 1 HETATM 5239 O O . HOH L 7 . ? 51.261 1.347 13.869 1.00 38.67 ? 2186 HOH A O 1 HETATM 5240 O O . HOH L 7 . ? 46.462 -2.171 -10.842 1.00 30.68 ? 2187 HOH A O 1 HETATM 5241 O O . HOH L 7 . ? 48.567 -1.474 -9.321 1.00 28.92 ? 2188 HOH A O 1 HETATM 5242 O O . HOH L 7 . ? 49.107 -3.935 -8.401 1.00 26.00 ? 2189 HOH A O 1 HETATM 5243 O O . HOH L 7 . ? 54.281 8.687 20.450 1.00 53.04 ? 2190 HOH A O 1 HETATM 5244 O O . HOH L 7 . ? 41.633 -4.675 2.915 1.00 23.57 ? 2191 HOH A O 1 HETATM 5245 O O . HOH L 7 . ? 42.486 4.046 -9.597 1.00 36.14 ? 2192 HOH A O 1 HETATM 5246 O O . HOH L 7 . ? 45.795 0.982 -7.799 1.00 24.18 ? 2193 HOH A O 1 HETATM 5247 O O . HOH L 7 . ? 53.754 -1.696 10.943 1.00 36.63 ? 2194 HOH A O 1 HETATM 5248 O O . HOH L 7 . ? 55.114 0.951 8.930 1.00 41.34 ? 2195 HOH A O 1 HETATM 5249 O O . HOH L 7 . ? 55.831 -8.348 9.879 1.00 36.61 ? 2196 HOH A O 1 HETATM 5250 O O . HOH L 7 . ? 40.425 0.609 -12.467 1.00 38.69 ? 2197 HOH A O 1 HETATM 5251 O O . HOH L 7 . ? 53.599 -5.752 3.184 1.00 26.49 ? 2198 HOH A O 1 HETATM 5252 O O . HOH L 7 . ? 43.306 10.840 -5.587 1.00 37.09 ? 2199 HOH A O 1 HETATM 5253 O O . HOH L 7 . ? 52.480 6.751 -0.556 1.00 37.81 ? 2200 HOH A O 1 HETATM 5254 O O . HOH L 7 . ? 45.011 16.149 -0.903 1.00 35.19 ? 2201 HOH A O 1 HETATM 5255 O O . HOH L 7 . ? 36.488 15.000 -4.812 1.00 44.02 ? 2202 HOH A O 1 HETATM 5256 O O . HOH L 7 . ? 27.694 8.179 11.179 1.00 53.92 ? 2203 HOH A O 1 HETATM 5257 O O . HOH L 7 . ? 33.356 8.237 15.951 1.00 24.80 ? 2204 HOH A O 1 HETATM 5258 O O . HOH L 7 . ? 31.062 13.493 10.658 1.00 54.05 ? 2205 HOH A O 1 HETATM 5259 O O . HOH L 7 . ? 29.070 11.709 11.052 1.00 54.45 ? 2206 HOH A O 1 HETATM 5260 O O . HOH L 7 . ? 47.728 14.215 4.714 1.00 38.89 ? 2207 HOH A O 1 HETATM 5261 O O . HOH L 7 . ? 30.378 8.489 16.305 1.00 45.47 ? 2208 HOH A O 1 HETATM 5262 O O . HOH L 7 . ? 28.048 6.237 15.717 1.00 45.81 ? 2209 HOH A O 1 HETATM 5263 O O . HOH L 7 . ? 44.916 22.864 6.830 1.00 43.85 ? 2210 HOH A O 1 HETATM 5264 O O . HOH L 7 . ? 38.654 6.678 7.654 1.00 18.37 ? 2211 HOH A O 1 HETATM 5265 O O . HOH L 7 . ? 47.617 15.418 8.725 1.00 34.94 ? 2212 HOH A O 1 HETATM 5266 O O . HOH L 7 . ? 46.133 19.249 10.155 1.00 29.45 ? 2213 HOH A O 1 HETATM 5267 O O . HOH L 7 . ? 39.414 14.480 15.085 1.00 20.21 ? 2214 HOH A O 1 HETATM 5268 O O . HOH L 7 . ? 44.170 13.129 13.506 1.00 20.78 ? 2215 HOH A O 1 HETATM 5269 O O . HOH L 7 . ? 38.865 11.513 15.114 1.00 19.21 ? 2216 HOH A O 1 HETATM 5270 O O . HOH L 7 . ? 48.082 13.694 10.968 1.00 26.32 ? 2217 HOH A O 1 HETATM 5271 O O . HOH L 7 . ? 43.982 22.862 15.289 1.00 24.59 ? 2218 HOH A O 1 HETATM 5272 O O . HOH L 7 . ? 42.080 28.488 11.025 1.00 44.06 ? 2219 HOH A O 1 HETATM 5273 O O . HOH L 7 . ? 46.419 24.019 11.466 1.00 42.25 ? 2220 HOH A O 1 HETATM 5274 O O . HOH L 7 . ? 46.246 21.860 20.440 1.00 34.18 ? 2221 HOH A O 1 HETATM 5275 O O . HOH L 7 . ? 44.513 23.802 17.922 1.00 31.71 ? 2222 HOH A O 1 HETATM 5276 O O . HOH L 7 . ? 44.120 23.410 20.674 1.00 25.84 ? 2223 HOH A O 1 HETATM 5277 O O . HOH L 7 . ? 37.030 24.175 20.203 1.00 41.74 ? 2224 HOH A O 1 HETATM 5278 O O . HOH L 7 . ? 42.405 25.208 20.878 1.00 42.48 ? 2225 HOH A O 1 HETATM 5279 O O . HOH L 7 . ? 37.517 15.907 18.928 1.00 30.10 ? 2226 HOH A O 1 HETATM 5280 O O . HOH L 7 . ? 37.466 16.056 16.239 1.00 26.25 ? 2227 HOH A O 1 HETATM 5281 O O . HOH L 7 . ? 45.534 16.357 24.900 1.00 30.65 ? 2228 HOH A O 1 HETATM 5282 O O . HOH L 7 . ? 45.105 13.805 23.617 1.00 20.67 ? 2229 HOH A O 1 HETATM 5283 O O . HOH L 7 . ? 48.830 14.472 15.218 1.00 31.04 ? 2230 HOH A O 1 HETATM 5284 O O . HOH L 7 . ? 49.748 12.275 22.905 1.00 48.43 ? 2231 HOH A O 1 HETATM 5285 O O . HOH L 7 . ? 48.535 16.913 22.650 1.00 42.82 ? 2232 HOH A O 1 HETATM 5286 O O . HOH L 7 . ? 41.654 10.237 24.498 1.00 27.02 ? 2233 HOH A O 1 HETATM 5287 O O . HOH L 7 . ? 47.566 9.038 23.654 1.00 32.50 ? 2234 HOH A O 1 HETATM 5288 O O . HOH L 7 . ? 49.514 10.488 20.613 1.00 33.62 ? 2235 HOH A O 1 HETATM 5289 O O . HOH L 7 . ? 35.151 10.754 19.166 1.00 32.62 ? 2236 HOH A O 1 HETATM 5290 O O . HOH L 7 . ? 35.353 5.590 19.544 1.00 20.42 ? 2237 HOH A O 1 HETATM 5291 O O . HOH L 7 . ? 36.045 11.794 14.875 1.00 24.86 ? 2238 HOH A O 1 HETATM 5292 O O . HOH L 7 . ? 39.450 6.775 26.852 1.00 25.58 ? 2239 HOH A O 1 HETATM 5293 O O . HOH L 7 . ? 36.647 10.800 28.866 1.00 49.91 ? 2240 HOH A O 1 HETATM 5294 O O . HOH L 7 . ? 40.228 10.950 26.499 1.00 28.13 ? 2241 HOH A O 1 HETATM 5295 O O . HOH L 7 . ? 38.197 14.294 27.525 1.00 30.31 ? 2242 HOH A O 1 HETATM 5296 O O . HOH L 7 . ? 34.017 12.700 22.909 1.00 39.93 ? 2243 HOH A O 1 HETATM 5297 O O . HOH L 7 . ? 35.730 -5.218 39.441 1.00 45.82 ? 2244 HOH A O 1 HETATM 5298 O O . HOH L 7 . ? 31.539 7.590 26.531 1.00 50.81 ? 2245 HOH A O 1 HETATM 5299 O O . HOH L 7 . ? 31.179 10.032 24.863 1.00 40.07 ? 2246 HOH A O 1 HETATM 5300 O O . HOH L 7 . ? 37.226 -23.430 29.771 1.00 46.65 ? 2247 HOH A O 1 HETATM 5301 O O . HOH L 7 . ? 35.825 -26.917 27.637 1.00 43.22 ? 2248 HOH A O 1 HETATM 5302 O O . HOH L 7 . ? 35.124 3.737 32.128 1.00 29.21 ? 2249 HOH A O 1 HETATM 5303 O O . HOH L 7 . ? 31.823 4.975 28.700 1.00 28.24 ? 2250 HOH A O 1 HETATM 5304 O O . HOH L 7 . ? 42.406 5.388 25.877 1.00 22.70 ? 2251 HOH A O 1 HETATM 5305 O O . HOH L 7 . ? 40.357 0.662 33.887 1.00 35.20 ? 2252 HOH A O 1 HETATM 5306 O O . HOH L 7 . ? 36.911 1.442 32.713 1.00 28.61 ? 2253 HOH A O 1 HETATM 5307 O O . HOH L 7 . ? 40.713 7.024 32.681 1.00 38.78 ? 2254 HOH A O 1 HETATM 5308 O O . HOH L 7 . ? 44.667 4.100 25.926 1.00 23.57 ? 2255 HOH A O 1 HETATM 5309 O O . HOH L 7 . ? 46.686 2.429 27.304 1.00 21.51 ? 2256 HOH A O 1 HETATM 5310 O O . HOH L 7 . ? 46.173 6.732 27.216 1.00 34.19 ? 2257 HOH A O 1 HETATM 5311 O O . HOH L 7 . ? 47.932 3.140 29.652 1.00 29.25 ? 2258 HOH A O 1 HETATM 5312 O O . HOH L 7 . ? 45.497 9.100 34.449 1.00 44.47 ? 2259 HOH A O 1 HETATM 5313 O O . HOH L 7 . ? 49.062 -33.411 20.892 1.00 40.32 ? 2260 HOH A O 1 HETATM 5314 O O . HOH L 7 . ? 45.603 7.317 24.017 1.00 34.39 ? 2261 HOH A O 1 HETATM 5315 O O . HOH L 7 . ? 48.917 4.782 23.380 1.00 33.30 ? 2262 HOH A O 1 HETATM 5316 O O . HOH L 7 . ? 48.120 2.158 20.212 1.00 24.49 ? 2263 HOH A O 1 HETATM 5317 O O . HOH L 7 . ? 50.105 3.957 21.237 1.00 36.28 ? 2264 HOH A O 1 HETATM 5318 O O . HOH L 7 . ? 49.452 0.360 24.252 1.00 32.96 ? 2265 HOH A O 1 HETATM 5319 O O . HOH L 7 . ? 51.479 0.641 28.444 1.00 46.03 ? 2266 HOH A O 1 HETATM 5320 O O . HOH L 7 . ? 51.843 -4.296 24.268 1.00 41.07 ? 2267 HOH A O 1 HETATM 5321 O O . HOH L 7 . ? 42.990 -6.365 29.369 1.00 22.99 ? 2268 HOH A O 1 HETATM 5322 O O . HOH L 7 . ? 38.035 -3.124 31.802 1.00 24.99 ? 2269 HOH A O 1 HETATM 5323 O O . HOH L 7 . ? 40.550 -5.163 30.437 1.00 30.69 ? 2270 HOH A O 1 HETATM 5324 O O . HOH L 7 . ? 48.989 -7.367 21.926 1.00 22.63 ? 2271 HOH A O 1 HETATM 5325 O O . HOH L 7 . ? 50.676 -5.052 19.123 1.00 29.75 ? 2272 HOH A O 1 HETATM 5326 O O . HOH L 7 . ? 48.655 -0.152 21.717 1.00 33.75 ? 2273 HOH A O 1 HETATM 5327 O O . HOH L 7 . ? 45.545 -10.153 29.794 1.00 42.21 ? 2274 HOH A O 1 HETATM 5328 O O . HOH L 7 . ? 48.237 -10.657 27.798 1.00 28.85 ? 2275 HOH A O 1 HETATM 5329 O O . HOH L 7 . ? 50.378 -7.631 26.351 1.00 43.40 ? 2276 HOH A O 1 HETATM 5330 O O . HOH L 7 . ? 44.988 -5.479 31.017 1.00 33.37 ? 2277 HOH A O 1 HETATM 5331 O O . HOH L 7 . ? 50.606 -13.676 21.970 1.00 29.22 ? 2278 HOH A O 1 HETATM 5332 O O . HOH L 7 . ? 47.197 -17.288 25.754 1.00 40.91 ? 2279 HOH A O 1 HETATM 5333 O O . HOH L 7 . ? 44.905 -18.183 22.571 1.00 31.35 ? 2280 HOH A O 1 HETATM 5334 O O . HOH L 7 . ? 42.828 -16.725 25.455 1.00 33.75 ? 2281 HOH A O 1 HETATM 5335 O O . HOH L 7 . ? 47.787 -12.685 30.383 1.00 46.13 ? 2282 HOH A O 1 HETATM 5336 O O . HOH L 7 . ? 42.160 -12.498 27.484 1.00 44.17 ? 2283 HOH A O 1 HETATM 5337 O O . HOH L 7 . ? 52.456 -13.730 17.683 1.00 47.28 ? 2284 HOH A O 1 HETATM 5338 O O . HOH L 7 . ? 49.106 -12.701 14.718 1.00 26.04 ? 2285 HOH A O 1 HETATM 5339 O O . HOH L 7 . ? 52.474 -7.134 19.040 1.00 45.05 ? 2286 HOH A O 1 HETATM 5340 O O . HOH L 7 . ? 52.668 -7.866 16.283 1.00 41.65 ? 2287 HOH A O 1 HETATM 5341 O O . HOH L 7 . ? 50.055 -9.511 20.518 1.00 34.37 ? 2288 HOH A O 1 HETATM 5342 O O . HOH L 7 . ? 49.838 -20.693 18.258 1.00 25.79 ? 2289 HOH A O 1 HETATM 5343 O O . HOH L 7 . ? 42.732 -12.081 10.379 1.00 18.49 ? 2290 HOH A O 1 HETATM 5344 O O . HOH L 7 . ? 49.981 -19.776 11.308 1.00 21.14 ? 2291 HOH A O 1 HETATM 5345 O O . HOH L 7 . ? 51.908 -19.065 17.565 1.00 34.02 ? 2292 HOH A O 1 HETATM 5346 O O . HOH L 7 . ? 53.721 -18.144 15.380 1.00 39.84 ? 2293 HOH A O 1 HETATM 5347 O O . HOH L 7 . ? 49.639 -27.232 17.602 1.00 25.97 ? 2294 HOH A O 1 HETATM 5348 O O . HOH L 7 . ? 52.553 -24.320 17.284 1.00 39.80 ? 2295 HOH A O 1 HETATM 5349 O O . HOH L 7 . ? 50.530 -24.324 21.098 1.00 37.90 ? 2296 HOH A O 1 HETATM 5350 O O . HOH L 7 . ? 50.192 -23.958 7.540 1.00 20.28 ? 2297 HOH A O 1 HETATM 5351 O O . HOH L 7 . ? 42.955 -32.507 9.370 1.00 34.50 ? 2298 HOH A O 1 HETATM 5352 O O . HOH L 7 . ? 41.441 -28.815 1.698 1.00 36.41 ? 2299 HOH A O 1 HETATM 5353 O O . HOH L 7 . ? 38.796 -29.643 1.003 1.00 42.30 ? 2300 HOH A O 1 HETATM 5354 O O . HOH L 7 . ? 36.074 -29.246 3.864 1.00 33.07 ? 2301 HOH A O 1 HETATM 5355 O O . HOH L 7 . ? 50.744 -25.916 5.443 1.00 25.72 ? 2302 HOH A O 1 HETATM 5356 O O . HOH L 7 . ? 53.599 -29.543 4.327 1.00 19.49 ? 2303 HOH A O 1 HETATM 5357 O O . HOH L 7 . ? 55.720 -29.145 1.555 1.00 37.55 ? 2304 HOH A O 1 HETATM 5358 O O . HOH L 7 . ? 45.115 -32.173 -3.523 1.00 36.04 ? 2305 HOH A O 1 HETATM 5359 O O . HOH L 7 . ? 39.178 -29.482 -1.786 1.00 32.38 ? 2306 HOH A O 1 HETATM 5360 O O . HOH L 7 . ? 49.170 -24.827 -7.394 1.00 46.95 ? 2307 HOH A O 1 HETATM 5361 O O . HOH L 7 . ? 38.873 -20.013 -1.925 1.00 23.51 ? 2308 HOH A O 1 HETATM 5362 O O . HOH L 7 . ? 53.388 -20.188 -3.717 1.00 38.82 ? 2309 HOH A O 1 HETATM 5363 O O . HOH L 7 . ? 55.054 -22.684 -2.394 1.00 36.69 ? 2310 HOH A O 1 HETATM 5364 O O . HOH L 7 . ? 55.042 -24.312 -0.077 1.00 31.61 ? 2311 HOH A O 1 HETATM 5365 O O . HOH L 7 . ? 54.050 -19.589 -6.332 1.00 39.18 ? 2312 HOH A O 1 HETATM 5366 O O . HOH L 7 . ? 48.197 -17.017 -5.211 1.00 31.14 ? 2313 HOH A O 1 HETATM 5367 O O . HOH L 7 . ? 51.744 -18.014 -2.705 1.00 37.92 ? 2314 HOH A O 1 HETATM 5368 O O . HOH L 7 . ? 50.505 -19.102 2.145 1.00 21.75 ? 2315 HOH A O 1 HETATM 5369 O O . HOH L 7 . ? 51.425 -18.047 0.001 1.00 37.54 ? 2316 HOH A O 1 HETATM 5370 O O . HOH L 7 . ? 52.477 -27.447 7.132 1.00 22.89 ? 2317 HOH A O 1 HETATM 5371 O O . HOH L 7 . ? 57.303 -22.496 1.797 1.00 42.48 ? 2318 HOH A O 1 HETATM 5372 O O . HOH L 7 . ? 57.826 -18.025 2.740 1.00 28.73 ? 2319 HOH A O 1 HETATM 5373 O O . HOH L 7 . ? 52.734 -15.829 0.292 1.00 33.60 ? 2320 HOH A O 1 HETATM 5374 O O . HOH L 7 . ? 40.470 -10.687 -0.449 1.00 21.49 ? 2321 HOH A O 1 HETATM 5375 O O . HOH L 7 . ? 34.360 -15.621 4.219 1.00 24.92 ? 2322 HOH A O 1 HETATM 5376 O O . HOH L 7 . ? 32.670 -8.505 5.134 1.00 38.74 ? 2323 HOH A O 1 HETATM 5377 O O . HOH L 7 . ? 42.383 -6.522 4.762 1.00 23.36 ? 2324 HOH A O 1 HETATM 5378 O O . HOH L 7 . ? 42.347 -10.769 8.053 1.00 24.24 ? 2325 HOH A O 1 HETATM 5379 O O . HOH L 7 . ? 32.072 -5.710 5.221 1.00 25.04 ? 2326 HOH A O 1 HETATM 5380 O O . HOH L 7 . ? 30.245 -12.524 13.138 1.00 23.86 ? 2327 HOH A O 1 HETATM 5381 O O . HOH L 7 . ? 29.561 -20.565 5.647 1.00 41.80 ? 2328 HOH A O 1 HETATM 5382 O O . HOH L 7 . ? 28.616 -19.936 3.101 1.00 45.74 ? 2329 HOH A O 1 HETATM 5383 O O . HOH L 7 . ? 26.677 -15.917 1.790 1.00 36.56 ? 2330 HOH A O 1 HETATM 5384 O O . HOH L 7 . ? 28.181 -18.056 -0.799 1.00 44.46 ? 2331 HOH A O 1 HETATM 5385 O O . HOH L 7 . ? 35.048 -30.562 -0.490 1.00 37.97 ? 2332 HOH A O 1 HETATM 5386 O O . HOH L 7 . ? 34.023 -25.730 9.565 1.00 47.69 ? 2333 HOH A O 1 HETATM 5387 O O . HOH L 7 . ? 40.256 -34.245 10.828 1.00 45.15 ? 2334 HOH A O 1 HETATM 5388 O O . HOH L 7 . ? 35.126 -36.144 7.789 1.00 28.85 ? 2335 HOH A O 1 HETATM 5389 O O . HOH L 7 . ? 29.267 -34.565 4.051 1.00 53.61 ? 2336 HOH A O 1 HETATM 5390 O O . HOH L 7 . ? 28.288 -28.988 12.179 1.00 26.33 ? 2337 HOH A O 1 HETATM 5391 O O . HOH L 7 . ? 26.238 -30.495 6.083 1.00 42.52 ? 2338 HOH A O 1 HETATM 5392 O O . HOH L 7 . ? 23.070 -26.944 6.396 1.00 28.63 ? 2339 HOH A O 1 HETATM 5393 O O . HOH L 7 . ? 26.481 -28.053 4.269 1.00 39.98 ? 2340 HOH A O 1 HETATM 5394 O O . HOH L 7 . ? 23.833 -29.437 7.205 1.00 35.01 ? 2341 HOH A O 1 HETATM 5395 O O . HOH L 7 . ? 28.643 -26.296 11.179 1.00 26.81 ? 2342 HOH A O 1 HETATM 5396 O O . HOH L 7 . ? 20.514 -25.356 3.411 1.00 27.64 ? 2343 HOH A O 1 HETATM 5397 O O . HOH L 7 . ? 20.260 -26.468 5.853 1.00 28.59 ? 2344 HOH A O 1 HETATM 5398 O O . HOH L 7 . ? 23.040 -23.392 1.455 1.00 32.42 ? 2345 HOH A O 1 HETATM 5399 O O . HOH L 7 . ? 23.574 -26.099 1.612 1.00 38.65 ? 2346 HOH A O 1 HETATM 5400 O O . HOH L 7 . ? 23.812 -27.510 3.859 1.00 33.82 ? 2347 HOH A O 1 HETATM 5401 O O . HOH L 7 . ? 25.198 -18.622 0.842 1.00 47.14 ? 2348 HOH A O 1 HETATM 5402 O O . HOH L 7 . ? 12.528 -27.646 2.548 1.00 44.77 ? 2349 HOH A O 1 HETATM 5403 O O . HOH L 7 . ? 18.170 -29.590 4.125 1.00 40.68 ? 2350 HOH A O 1 HETATM 5404 O O . HOH L 7 . ? 20.990 -17.752 -1.222 1.00 46.14 ? 2351 HOH A O 1 HETATM 5405 O O . HOH L 7 . ? 11.675 -21.539 8.460 1.00 39.46 ? 2352 HOH A O 1 HETATM 5406 O O . HOH L 7 . ? 10.433 -18.917 10.338 1.00 35.58 ? 2353 HOH A O 1 HETATM 5407 O O . HOH L 7 . ? 7.316 -11.928 2.604 1.00 35.29 ? 2354 HOH A O 1 HETATM 5408 O O . HOH L 7 . ? 10.548 -8.599 1.113 1.00 31.02 ? 2355 HOH A O 1 HETATM 5409 O O . HOH L 7 . ? 6.689 -13.550 9.348 1.00 37.11 ? 2356 HOH A O 1 HETATM 5410 O O . HOH L 7 . ? 6.002 -6.373 9.113 1.00 34.50 ? 2357 HOH A O 1 HETATM 5411 O O . HOH L 7 . ? 14.989 -14.815 14.450 1.00 33.44 ? 2358 HOH A O 1 HETATM 5412 O O . HOH L 7 . ? 12.213 -5.814 17.926 1.00 30.31 ? 2359 HOH A O 1 HETATM 5413 O O . HOH L 7 . ? 6.599 -4.878 14.737 1.00 30.01 ? 2360 HOH A O 1 HETATM 5414 O O . HOH L 7 . ? 7.747 -13.263 19.501 1.00 31.56 ? 2361 HOH A O 1 HETATM 5415 O O . HOH L 7 . ? 7.720 -8.355 24.074 1.00 37.38 ? 2362 HOH A O 1 HETATM 5416 O O . HOH L 7 . ? 5.017 -8.026 19.653 1.00 46.52 ? 2363 HOH A O 1 HETATM 5417 O O . HOH L 7 . ? 6.433 -10.129 25.784 1.00 47.29 ? 2364 HOH A O 1 HETATM 5418 O O . HOH L 7 . ? 11.992 -9.552 30.727 1.00 35.59 ? 2365 HOH A O 1 HETATM 5419 O O . HOH L 7 . ? 11.960 0.077 24.673 1.00 36.50 ? 2366 HOH A O 1 HETATM 5420 O O . HOH L 7 . ? 7.479 -0.285 19.848 1.00 31.97 ? 2367 HOH A O 1 HETATM 5421 O O . HOH L 7 . ? 1.104 -1.347 19.833 1.00 67.99 ? 2368 HOH A O 1 HETATM 5422 O O . HOH L 7 . ? 4.061 1.651 16.413 1.00 36.44 ? 2369 HOH A O 1 HETATM 5423 O O . HOH L 7 . ? 6.029 4.482 14.764 1.00 41.85 ? 2370 HOH A O 1 HETATM 5424 O O . HOH L 7 . ? 3.361 -2.899 8.253 1.00 34.26 ? 2371 HOH A O 1 HETATM 5425 O O . HOH L 7 . ? 6.643 9.789 11.265 1.00 36.77 ? 2372 HOH A O 1 HETATM 5426 O O . HOH L 7 . ? 6.872 8.021 15.380 1.00 44.97 ? 2373 HOH A O 1 HETATM 5427 O O . HOH L 7 . ? 4.237 -0.681 6.404 1.00 42.21 ? 2374 HOH A O 1 HETATM 5428 O O . HOH L 7 . ? 10.467 2.527 2.157 1.00 43.40 ? 2375 HOH A O 1 HETATM 5429 O O . HOH L 7 . ? 12.227 -1.979 1.048 1.00 27.48 ? 2376 HOH A O 1 HETATM 5430 O O . HOH L 7 . ? 16.273 -5.977 -4.844 1.00 47.06 ? 2377 HOH A O 1 HETATM 5431 O O . HOH L 7 . ? 18.540 -6.486 -2.212 1.00 34.25 ? 2378 HOH A O 1 HETATM 5432 O O . HOH L 7 . ? 12.953 4.543 -1.376 1.00 50.51 ? 2379 HOH A O 1 HETATM 5433 O O . HOH L 7 . ? 26.420 0.761 -2.529 1.00 43.19 ? 2380 HOH A O 1 HETATM 5434 O O . HOH L 7 . ? 27.924 1.133 -0.419 1.00 28.44 ? 2381 HOH A O 1 HETATM 5435 O O . HOH L 7 . ? 22.862 -3.822 3.037 1.00 27.50 ? 2382 HOH A O 1 HETATM 5436 O O . HOH L 7 . ? 22.482 1.445 4.622 1.00 26.62 ? 2383 HOH A O 1 HETATM 5437 O O . HOH L 7 . ? 25.733 2.925 5.505 1.00 30.47 ? 2384 HOH A O 1 HETATM 5438 O O . HOH L 7 . ? 30.983 -2.900 2.339 1.00 18.41 ? 2385 HOH A O 1 HETATM 5439 O O . HOH L 7 . ? 26.383 -4.328 4.119 1.00 22.61 ? 2386 HOH A O 1 HETATM 5440 O O . HOH L 7 . ? 23.610 5.221 11.036 1.00 46.36 ? 2387 HOH A O 1 HETATM 5441 O O . HOH L 7 . ? 21.230 7.480 13.770 1.00 35.80 ? 2388 HOH A O 1 HETATM 5442 O O . HOH L 7 . ? 13.990 7.269 18.744 1.00 27.44 ? 2389 HOH A O 1 HETATM 5443 O O . HOH L 7 . ? 16.768 6.994 20.851 1.00 20.56 ? 2390 HOH A O 1 HETATM 5444 O O . HOH L 7 . ? 20.890 6.914 18.866 1.00 20.60 ? 2391 HOH A O 1 HETATM 5445 O O . HOH L 7 . ? 12.750 8.574 16.833 1.00 26.99 ? 2392 HOH A O 1 HETATM 5446 O O . HOH L 7 . ? 22.270 7.765 16.363 1.00 42.98 ? 2393 HOH A O 1 HETATM 5447 O O . HOH L 7 . ? 23.415 11.834 14.793 1.00 40.57 ? 2394 HOH A O 1 HETATM 5448 O O . HOH L 7 . ? 11.788 9.691 22.622 1.00 32.91 ? 2395 HOH A O 1 HETATM 5449 O O . HOH L 7 . ? 7.770 11.179 17.625 1.00 37.44 ? 2396 HOH A O 1 HETATM 5450 O O . HOH L 7 . ? 8.632 1.859 21.505 1.00 33.25 ? 2397 HOH A O 1 HETATM 5451 O O . HOH L 7 . ? 5.363 1.534 18.918 1.00 43.12 ? 2398 HOH A O 1 HETATM 5452 O O . HOH L 7 . ? 23.799 5.135 4.344 1.00 29.23 ? 2399 HOH A O 1 HETATM 5453 O O . HOH L 7 . ? 16.783 -10.066 -1.904 1.00 39.57 ? 2400 HOH A O 1 HETATM 5454 O O . HOH L 7 . ? 23.853 -13.315 -2.253 1.00 32.75 ? 2401 HOH A O 1 HETATM 5455 O O . HOH L 7 . ? 25.565 -13.322 2.180 1.00 32.70 ? 2402 HOH A O 1 HETATM 5456 O O . HOH L 7 . ? 18.428 -13.048 -2.135 1.00 39.65 ? 2403 HOH A O 1 HETATM 5457 O O . HOH L 7 . ? 25.774 -17.122 4.042 1.00 27.93 ? 2404 HOH A O 1 HETATM 5458 O O . HOH L 7 . ? 26.111 -9.802 5.481 1.00 31.32 ? 2405 HOH A O 1 HETATM 5459 O O . HOH L 7 . ? 24.208 -6.107 3.710 1.00 28.36 ? 2406 HOH A O 1 HETATM 5460 O O . HOH L 7 . ? 23.770 -4.510 17.436 1.00 20.69 ? 2407 HOH A O 1 HETATM 5461 O O . HOH L 7 . ? 14.774 -4.502 18.003 1.00 25.15 ? 2408 HOH A O 1 HETATM 5462 O O . HOH L 7 . ? 23.726 1.357 27.765 1.00 20.49 ? 2409 HOH A O 1 HETATM 5463 O O . HOH L 7 . ? 10.670 2.083 23.473 1.00 39.12 ? 2410 HOH A O 1 HETATM 5464 O O . HOH L 7 . ? 12.664 4.095 26.281 1.00 31.90 ? 2411 HOH A O 1 HETATM 5465 O O . HOH L 7 . ? 13.748 1.453 28.257 1.00 26.99 ? 2412 HOH A O 1 HETATM 5466 O O . HOH L 7 . ? 11.802 -0.276 27.498 1.00 37.63 ? 2413 HOH A O 1 HETATM 5467 O O . HOH L 7 . ? 12.086 -3.514 27.647 1.00 36.02 ? 2414 HOH A O 1 HETATM 5468 O O . HOH L 7 . ? 14.076 11.724 25.528 1.00 42.41 ? 2415 HOH A O 1 HETATM 5469 O O . HOH L 7 . ? 10.113 5.357 25.455 1.00 45.89 ? 2416 HOH A O 1 HETATM 5470 O O . HOH L 7 . ? 16.133 4.598 32.528 1.00 40.56 ? 2417 HOH A O 1 HETATM 5471 O O . HOH L 7 . ? 19.193 9.754 33.067 1.00 34.43 ? 2418 HOH A O 1 HETATM 5472 O O . HOH L 7 . ? 18.880 5.326 33.296 1.00 47.82 ? 2419 HOH A O 1 HETATM 5473 O O . HOH L 7 . ? 22.845 11.472 21.097 1.00 32.27 ? 2420 HOH A O 1 HETATM 5474 O O . HOH L 7 . ? 27.362 11.253 26.034 1.00 42.60 ? 2421 HOH A O 1 HETATM 5475 O O . HOH L 7 . ? 27.499 4.114 20.667 1.00 25.23 ? 2422 HOH A O 1 HETATM 5476 O O . HOH L 7 . ? 28.262 8.176 20.741 1.00 42.42 ? 2423 HOH A O 1 HETATM 5477 O O . HOH L 7 . ? 29.090 5.256 22.611 1.00 23.78 ? 2424 HOH A O 1 HETATM 5478 O O . HOH L 7 . ? 29.079 7.123 25.336 1.00 35.95 ? 2425 HOH A O 1 HETATM 5479 O O . HOH L 7 . ? 34.257 -2.071 26.784 1.00 24.71 ? 2426 HOH A O 1 HETATM 5480 O O . HOH L 7 . ? 28.905 1.796 17.556 1.00 20.64 ? 2427 HOH A O 1 HETATM 5481 O O . HOH L 7 . ? 29.539 -6.574 16.417 1.00 21.20 ? 2428 HOH A O 1 HETATM 5482 O O . HOH L 7 . ? 29.057 1.133 13.433 1.00 21.11 ? 2429 HOH A O 1 HETATM 5483 O O . HOH L 7 . ? 27.085 -12.944 16.134 1.00 27.01 ? 2430 HOH A O 1 HETATM 5484 O O . HOH L 7 . ? 26.373 -15.060 14.456 1.00 34.47 ? 2431 HOH A O 1 HETATM 5485 O O . HOH L 7 . ? 26.747 -20.051 19.707 1.00 27.57 ? 2432 HOH A O 1 HETATM 5486 O O . HOH L 7 . ? 25.973 -22.067 12.163 1.00 26.39 ? 2433 HOH A O 1 HETATM 5487 O O . HOH L 7 . ? 28.342 -19.221 14.702 1.00 31.63 ? 2434 HOH A O 1 HETATM 5488 O O . HOH L 7 . ? 16.358 -27.662 18.483 1.00 35.66 ? 2435 HOH A O 1 HETATM 5489 O O . HOH L 7 . ? 23.410 -25.272 25.515 1.00 29.57 ? 2436 HOH A O 1 HETATM 5490 O O . HOH L 7 . ? 13.945 -17.325 14.629 1.00 35.86 ? 2437 HOH A O 1 HETATM 5491 O O . HOH L 7 . ? 11.953 -28.232 12.241 1.00 33.89 ? 2438 HOH A O 1 HETATM 5492 O O . HOH L 7 . ? 19.219 -33.105 16.068 1.00 39.45 ? 2439 HOH A O 1 HETATM 5493 O O . HOH L 7 . ? 21.205 -29.524 18.675 1.00 42.61 ? 2440 HOH A O 1 HETATM 5494 O O . HOH L 7 . ? 10.480 -25.912 12.158 1.00 35.52 ? 2441 HOH A O 1 HETATM 5495 O O . HOH L 7 . ? 19.491 -29.137 6.373 1.00 30.86 ? 2442 HOH A O 1 HETATM 5496 O O . HOH L 7 . ? 22.439 -31.586 8.525 1.00 35.67 ? 2443 HOH A O 1 HETATM 5497 O O . HOH L 7 . ? 21.693 -30.810 5.729 1.00 47.98 ? 2444 HOH A O 1 HETATM 5498 O O . HOH L 7 . ? 23.709 -33.913 7.694 1.00 47.90 ? 2445 HOH A O 1 HETATM 5499 O O . HOH L 7 . ? 23.866 -35.122 10.078 1.00 37.45 ? 2446 HOH A O 1 HETATM 5500 O O . HOH L 7 . ? 27.270 -35.908 12.523 1.00 38.34 ? 2447 HOH A O 1 HETATM 5501 O O . HOH L 7 . ? 24.748 -33.202 21.161 1.00 52.10 ? 2448 HOH A O 1 HETATM 5502 O O . HOH L 7 . ? 28.437 -30.406 23.090 1.00 43.06 ? 2449 HOH A O 1 HETATM 5503 O O . HOH L 7 . ? 27.020 -26.272 18.400 1.00 32.52 ? 2450 HOH A O 1 HETATM 5504 O O . HOH L 7 . ? 32.036 -38.035 16.131 1.00 36.97 ? 2451 HOH A O 1 HETATM 5505 O O . HOH L 7 . ? 33.757 -32.340 20.048 1.00 41.74 ? 2452 HOH A O 1 HETATM 5506 O O . HOH L 7 . ? 31.830 -32.936 21.979 1.00 44.17 ? 2453 HOH A O 1 HETATM 5507 O O . HOH L 7 . ? 29.714 -26.105 18.057 1.00 46.97 ? 2454 HOH A O 1 HETATM 5508 O O . HOH L 7 . ? 29.853 -22.584 17.703 1.00 43.86 ? 2455 HOH A O 1 HETATM 5509 O O . HOH L 7 . ? 27.237 -22.649 17.362 1.00 43.54 ? 2456 HOH A O 1 HETATM 5510 O O . HOH L 7 . ? 29.154 -18.698 10.087 1.00 35.20 ? 2457 HOH A O 1 HETATM 5511 O O . HOH L 7 . ? 28.660 -15.569 9.701 1.00 43.49 ? 2458 HOH A O 1 HETATM 5512 O O . HOH L 7 . ? 29.675 -17.017 13.495 1.00 40.18 ? 2459 HOH A O 1 HETATM 5513 O O . HOH L 7 . ? 39.562 3.908 17.789 1.00 18.59 ? 2460 HOH A O 1 HETATM 5514 O O . HOH L 7 . ? 48.940 2.325 15.566 1.00 20.15 ? 2461 HOH A O 1 HETATM 5515 O O . HOH L 7 . ? 48.785 0.896 17.889 1.00 25.30 ? 2462 HOH A O 1 HETATM 5516 O O . HOH L 7 . ? 46.554 2.125 2.223 1.00 21.16 ? 2463 HOH A O 1 HETATM 5517 O O . HOH L 7 . ? 51.358 2.050 11.066 1.00 26.02 ? 2464 HOH A O 1 HETATM 5518 O O . HOH L 7 . ? 50.703 13.124 17.044 1.00 42.18 ? 2465 HOH A O 1 HETATM 5519 O O . HOH L 7 . ? 49.728 4.618 17.052 1.00 23.93 ? 2466 HOH A O 1 HETATM 5520 O O . HOH L 7 . ? 51.536 5.985 19.544 1.00 36.90 ? 2467 HOH A O 1 HETATM 5521 O O . HOH L 7 . ? 52.950 3.847 14.575 1.00 32.35 ? 2468 HOH A O 1 HETATM 5522 O O . HOH L 7 . ? 53.118 9.587 18.188 1.00 29.86 ? 2469 HOH A O 1 HETATM 5523 O O . HOH L 7 . ? 57.234 6.647 7.409 1.00 38.47 ? 2470 HOH A O 1 HETATM 5524 O O . HOH L 7 . ? 59.759 9.497 4.079 1.00 57.16 ? 2471 HOH A O 1 HETATM 5525 O O . HOH L 7 . ? 56.651 11.458 2.823 1.00 40.41 ? 2472 HOH A O 1 HETATM 5526 O O . HOH L 7 . ? 54.220 13.194 5.453 1.00 44.81 ? 2473 HOH A O 1 HETATM 5527 O O . HOH L 7 . ? 56.842 2.601 1.253 1.00 29.92 ? 2474 HOH A O 1 HETATM 5528 O O . HOH L 7 . ? 55.754 2.047 6.570 1.00 44.63 ? 2475 HOH A O 1 HETATM 5529 O O . HOH L 7 . ? 52.520 0.114 9.419 1.00 27.43 ? 2476 HOH A O 1 HETATM 5530 O O . HOH L 7 . ? 49.838 -7.766 3.672 1.00 17.79 ? 2477 HOH A O 1 HETATM 5531 O O . HOH L 7 . ? 55.331 -6.167 8.212 1.00 35.66 ? 2478 HOH A O 1 HETATM 5532 O O . HOH L 7 . ? 57.298 -5.607 4.771 1.00 31.13 ? 2479 HOH A O 1 HETATM 5533 O O . HOH L 7 . ? 55.382 -10.899 9.037 1.00 28.39 ? 2480 HOH A O 1 HETATM 5534 O O . HOH L 7 . ? 54.857 -6.746 5.421 1.00 23.47 ? 2481 HOH A O 1 HETATM 5535 O O . HOH L 7 . ? 53.584 -11.545 12.994 1.00 35.45 ? 2482 HOH A O 1 HETATM 5536 O O . HOH L 7 . ? 55.084 -12.772 0.158 1.00 22.06 ? 2483 HOH A O 1 HETATM 5537 O O . HOH L 7 . ? 49.707 -13.378 -2.558 1.00 23.16 ? 2484 HOH A O 1 HETATM 5538 O O . HOH L 7 . ? 49.745 -14.555 -4.897 1.00 37.57 ? 2485 HOH A O 1 HETATM 5539 O O . HOH L 7 . ? 51.907 -9.198 -9.105 1.00 32.37 ? 2486 HOH A O 1 HETATM 5540 O O . HOH L 7 . ? 53.141 -3.023 -8.415 1.00 33.77 ? 2487 HOH A O 1 HETATM 5541 O O . HOH L 7 . ? 51.711 -0.672 -7.951 1.00 25.05 ? 2488 HOH A O 1 HETATM 5542 O O . HOH L 7 . ? 56.478 2.001 -4.150 1.00 32.41 ? 2489 HOH A O 1 HETATM 5543 O O . HOH L 7 . ? 41.094 -1.804 2.349 1.00 18.39 ? 2490 HOH A O 1 HETATM 5544 O O . HOH L 7 . ? 33.606 -2.841 3.233 1.00 20.17 ? 2491 HOH A O 1 HETATM 5545 O O . HOH L 7 . ? 31.453 8.849 9.941 1.00 39.17 ? 2492 HOH A O 1 HETATM 5546 O O . HOH L 7 . ? 29.522 8.123 8.720 1.00 44.04 ? 2493 HOH A O 1 HETATM 5547 O O . HOH L 7 . ? 33.477 7.393 13.632 1.00 20.09 ? 2494 HOH A O 1 HETATM 5548 O O . HOH L 7 . ? 31.003 7.909 12.285 1.00 42.72 ? 2495 HOH A O 1 HETATM 5549 O O . HOH L 7 . ? 32.243 11.338 9.613 1.00 29.40 ? 2496 HOH A O 1 HETATM 5550 O O . HOH L 7 . ? 29.456 6.789 13.943 1.00 46.23 ? 2497 HOH A O 1 HETATM 5551 O O . HOH L 7 . ? 30.640 6.644 18.592 1.00 28.21 ? 2498 HOH A O 1 HETATM 5552 O O . HOH L 7 . ? 33.274 6.161 17.913 1.00 20.37 ? 2499 HOH A O 1 HETATM 5553 O O . HOH L 7 . ? 35.350 -12.359 26.176 1.00 19.99 ? 2500 HOH A O 1 HETATM 5554 O O . HOH L 7 . ? 30.358 -13.595 31.038 1.00 36.11 ? 2501 HOH A O 1 HETATM 5555 O O . HOH L 7 . ? 32.377 -12.101 31.411 1.00 44.42 ? 2502 HOH A O 1 HETATM 5556 O O . HOH L 7 . ? 32.084 -20.906 33.487 1.00 41.94 ? 2503 HOH A O 1 HETATM 5557 O O . HOH L 7 . ? 33.761 -15.043 32.250 1.00 35.69 ? 2504 HOH A O 1 HETATM 5558 O O . HOH L 7 . ? 26.978 -14.130 34.624 1.00 37.18 ? 2505 HOH A O 1 HETATM 5559 O O . HOH L 7 . ? 15.521 -19.373 33.298 1.00 47.88 ? 2506 HOH A O 1 HETATM 5560 O O . HOH L 7 . ? 17.609 -16.379 35.586 1.00 41.54 ? 2507 HOH A O 1 HETATM 5561 O O . HOH L 7 . ? 19.685 -10.237 35.350 1.00 48.24 ? 2508 HOH A O 1 HETATM 5562 O O . HOH L 7 . ? 24.000 -11.092 37.523 1.00 49.06 ? 2509 HOH A O 1 HETATM 5563 O O . HOH L 7 . ? 16.534 -22.759 28.762 1.00 44.24 ? 2510 HOH A O 1 HETATM 5564 O O . HOH L 7 . ? 32.489 -24.568 29.112 1.00 35.11 ? 2511 HOH A O 1 HETATM 5565 O O . HOH L 7 . ? 28.822 -27.339 29.414 1.00 40.09 ? 2512 HOH A O 1 HETATM 5566 O O . HOH L 7 . ? 27.937 -25.371 37.546 1.00 47.88 ? 2513 HOH A O 1 HETATM 5567 O O . HOH L 7 . ? 32.906 -26.795 30.629 1.00 39.99 ? 2514 HOH A O 1 HETATM 5568 O O . HOH L 7 . ? 29.112 -30.805 25.917 1.00 43.49 ? 2515 HOH A O 1 HETATM 5569 O O . HOH L 7 . ? 30.789 -24.938 26.735 1.00 34.10 ? 2516 HOH A O 1 HETATM 5570 O O . HOH L 7 . ? 31.977 -23.956 24.437 1.00 25.78 ? 2517 HOH A O 1 HETATM 5571 O O . HOH L 7 . ? 17.512 -11.681 34.395 1.00 35.35 ? 2518 HOH A O 1 HETATM 5572 O O . HOH L 7 . ? 15.816 -7.522 36.716 1.00 47.73 ? 2519 HOH A O 1 HETATM 5573 O O . HOH L 7 . ? 20.501 -7.673 34.835 1.00 42.96 ? 2520 HOH A O 1 HETATM 5574 O O . HOH L 7 . ? 25.319 4.009 30.820 1.00 21.48 ? 2521 HOH A O 1 HETATM 5575 O O . HOH L 7 . ? 24.984 -0.094 37.298 1.00 34.14 ? 2522 HOH A O 1 HETATM 5576 O O . HOH L 7 . ? 27.096 0.495 39.107 1.00 40.26 ? 2523 HOH A O 1 HETATM 5577 O O . HOH L 7 . ? 32.170 3.834 36.649 1.00 39.00 ? 2524 HOH A O 1 HETATM 5578 O O . HOH L 7 . ? 29.928 2.850 40.009 1.00 42.70 ? 2525 HOH A O 1 HETATM 5579 O O . HOH L 7 . ? 34.710 -9.014 33.960 1.00 33.50 ? 2526 HOH A O 1 HETATM 5580 O O . HOH L 7 . ? 34.289 -6.825 37.622 1.00 37.84 ? 2527 HOH A O 1 HETATM 5581 O O . HOH L 7 . ? 36.675 -1.304 33.507 1.00 30.53 ? 2528 HOH A O 1 HETATM 5582 O O . HOH L 7 . ? 35.817 -0.819 39.387 1.00 46.66 ? 2529 HOH A O 1 HETATM 5583 O O . HOH L 7 . ? 35.925 1.173 37.277 1.00 45.58 ? 2530 HOH A O 1 HETATM 5584 O O . HOH L 7 . ? 34.891 -12.603 30.310 1.00 34.37 ? 2531 HOH A O 1 HETATM 5585 O O . HOH L 7 . ? 41.118 -10.869 29.699 1.00 29.18 ? 2532 HOH A O 1 HETATM 5586 O O . HOH L 7 . ? 38.545 -18.551 29.843 1.00 32.37 ? 2533 HOH A O 1 HETATM 5587 O O . HOH L 7 . ? 40.419 -21.109 24.297 1.00 28.46 ? 2534 HOH A O 1 HETATM 5588 O O . HOH L 7 . ? 39.008 -21.182 28.804 1.00 38.59 ? 2535 HOH A O 1 HETATM 5589 O O . HOH L 7 . ? 35.016 -24.082 27.925 1.00 31.94 ? 2536 HOH A O 1 HETATM 5590 O O . HOH L 7 . ? 37.925 -30.835 22.280 1.00 33.77 ? 2537 HOH A O 1 HETATM 5591 O O . HOH L 7 . ? 46.237 -28.303 24.304 1.00 41.76 ? 2538 HOH A O 1 HETATM 5592 O O . HOH L 7 . ? 45.512 -30.422 22.633 1.00 29.21 ? 2539 HOH A O 1 HETATM 5593 O O . HOH L 7 . ? 42.846 -33.350 17.319 1.00 34.75 ? 2540 HOH A O 1 HETATM 5594 O O . HOH L 7 . ? 49.488 -28.457 22.090 1.00 35.12 ? 2541 HOH A O 1 HETATM 5595 O O . HOH L 7 . ? 46.429 -22.168 20.940 1.00 30.66 ? 2542 HOH A O 1 HETATM 5596 O O . HOH L 7 . ? 48.205 -30.922 21.482 1.00 37.08 ? 2543 HOH A O 1 HETATM 5597 O O . HOH L 7 . ? 48.534 -34.585 18.393 1.00 29.05 ? 2544 HOH A O 1 HETATM 5598 O O . HOH L 7 . ? 43.997 -36.108 10.649 1.00 45.87 ? 2545 HOH A O 1 HETATM 5599 O O . HOH L 7 . ? 52.270 -27.945 14.053 1.00 35.10 ? 2546 HOH A O 1 HETATM 5600 O O . HOH L 7 . ? 54.384 -32.761 14.377 1.00 34.00 ? 2547 HOH A O 1 HETATM 5601 O O . HOH L 7 . ? 52.849 -36.146 10.887 1.00 36.40 ? 2548 HOH A O 1 HETATM 5602 O O . HOH L 7 . ? 50.945 -29.820 7.208 1.00 27.24 ? 2549 HOH A O 1 HETATM 5603 O O . HOH L 7 . ? 54.214 -30.836 7.127 1.00 31.66 ? 2550 HOH A O 1 HETATM 5604 O O . HOH L 7 . ? 55.867 -28.356 9.860 1.00 44.97 ? 2551 HOH A O 1 HETATM 5605 O O . HOH L 7 . ? 57.236 -26.101 10.931 1.00 41.77 ? 2552 HOH A O 1 HETATM 5606 O O . HOH L 7 . ? 57.307 -20.019 11.702 1.00 42.50 ? 2553 HOH A O 1 HETATM 5607 O O . HOH L 7 . ? 55.318 -24.758 12.962 1.00 32.43 ? 2554 HOH A O 1 HETATM 5608 O O . HOH L 7 . ? 54.694 -15.483 12.116 1.00 38.44 ? 2555 HOH A O 1 HETATM 5609 O O . HOH L 7 . ? 57.680 -12.522 9.871 1.00 41.61 ? 2556 HOH A O 1 HETATM 5610 O O . HOH L 7 . ? 55.237 -12.869 11.261 1.00 39.40 ? 2557 HOH A O 1 HETATM 5611 O O . HOH L 7 . ? 57.248 -14.174 2.380 1.00 26.77 ? 2558 HOH A O 1 HETATM 5612 O O . HOH L 7 . ? 60.653 -13.097 7.146 1.00 30.51 ? 2559 HOH A O 1 HETATM 5613 O O . HOH L 7 . ? 55.981 -6.319 1.108 1.00 30.34 ? 2560 HOH A O 1 HETATM 5614 O O . HOH L 7 . ? 51.852 -7.339 1.719 1.00 18.80 ? 2561 HOH A O 1 HETATM 5615 O O . HOH L 7 . ? 57.460 -8.994 -4.873 1.00 21.21 ? 2562 HOH A O 1 HETATM 5616 O O . HOH L 7 . ? 52.711 -15.347 -4.165 1.00 43.15 ? 2563 HOH A O 1 HETATM 5617 O O . HOH L 7 . ? 58.501 -5.619 -0.165 1.00 46.82 ? 2564 HOH A O 1 HETATM 5618 O O . HOH L 7 . ? 61.172 3.504 -0.421 1.00 51.63 ? 2565 HOH A O 1 HETATM 5619 O O . HOH L 7 . ? 28.694 -5.461 5.506 1.00 34.65 ? 2566 HOH A O 1 HETATM 5620 O O . HOH L 7 . ? 28.046 -8.189 4.367 1.00 37.55 ? 2567 HOH A O 1 HETATM 5621 O O . HOH L 7 . ? 38.662 24.682 28.115 1.00 38.07 ? 2568 HOH A O 1 HETATM 5622 O O . HOH L 7 . ? 39.529 26.998 28.049 1.00 35.17 ? 2569 HOH A O 1 HETATM 5623 O O . HOH L 7 . ? 44.211 29.849 22.795 1.00 50.04 ? 2570 HOH A O 1 HETATM 5624 O O . HOH L 7 . ? 39.191 29.765 32.627 1.00 42.22 ? 2571 HOH A O 1 HETATM 5625 O O . HOH L 7 . ? 46.571 32.372 28.736 1.00 44.51 ? 2572 HOH A O 1 HETATM 5626 O O . HOH L 7 . ? 44.737 33.649 30.642 1.00 40.48 ? 2573 HOH A O 1 HETATM 5627 O O . HOH L 7 . ? 36.722 35.474 38.041 1.00 45.10 ? 2574 HOH A O 1 HETATM 5628 O O . HOH L 7 . ? 41.565 33.971 35.709 1.00 41.48 ? 2575 HOH A O 1 HETATM 5629 O O . HOH L 7 . ? 35.633 29.340 41.218 1.00 43.56 ? 2576 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 . VAL A 3 ? 0.7679 0.8486 0.8219 -0.0108 0.0140 -0.0965 19 VAL A N 2 C CA . VAL A 3 ? 0.8102 0.8915 0.8759 -0.0111 0.0096 -0.1003 19 VAL A CA 3 C C . VAL A 3 ? 0.7921 0.8724 0.8671 -0.0120 0.0105 -0.1042 19 VAL A C 4 O O . VAL A 3 ? 0.7816 0.8592 0.8558 -0.0122 0.0123 -0.1019 19 VAL A O 5 C CB . VAL A 3 ? 0.8272 0.9057 0.8951 -0.0108 0.0043 -0.0960 19 VAL A CB 6 C CG1 . VAL A 3 ? 0.8486 0.9280 0.9271 -0.0110 0.0000 -0.0997 19 VAL A CG1 7 C CG2 . VAL A 3 ? 0.8253 0.9042 0.8834 -0.0100 0.0041 -0.0913 19 VAL A CG2 8 N N . LYS A 4 ? 0.7730 0.8557 0.8574 -0.0124 0.0091 -0.1103 20 LYS A N 9 C CA . LYS A 4 ? 0.7387 0.8211 0.8331 -0.0131 0.0097 -0.1149 20 LYS A CA 10 C C . LYS A 4 ? 0.6746 0.7528 0.7764 -0.0129 0.0052 -0.1127 20 LYS A C 11 O O . LYS A 4 ? 0.6559 0.7330 0.7650 -0.0132 0.0056 -0.1154 20 LYS A O 12 C CB . LYS A 4 ? 0.7885 0.8748 0.8909 -0.0134 0.0092 -0.1222 20 LYS A CB 13 C CG . LYS A 4 ? 0.8350 0.9257 0.9301 -0.0134 0.0134 -0.1250 20 LYS A CG 14 C CD . LYS A 4 ? 0.8696 0.9644 0.9733 -0.0137 0.0133 -0.1329 20 LYS A CD 15 C CE . LYS A 4 ? 0.8809 0.9800 0.9766 -0.0137 0.0180 -0.1358 20 LYS A CE 16 N NZ . LYS A 4 ? 0.8946 0.9979 0.9986 -0.0140 0.0181 -0.1439 20 LYS A NZ 17 N N . GLU A 5 ? 0.6170 0.6929 0.7167 -0.0123 0.0011 -0.1079 21 GLU A N 18 C CA . GLU A 5 ? 0.5505 0.6219 0.6543 -0.0120 -0.0031 -0.1043 21 GLU A CA 19 C C . GLU A 5 ? 0.5039 0.5725 0.6032 -0.0119 -0.0008 -0.1005 21 GLU A C 20 O O . GLU A 5 ? 0.4704 0.5356 0.5743 -0.0116 -0.0036 -0.0991 21 GLU A O 21 C CB . GLU A 5 ? 0.5435 0.6135 0.6437 -0.0115 -0.0068 -0.0996 21 GLU A CB 22 C CG . GLU A 5 ? 0.5312 0.5963 0.6338 -0.0111 -0.0112 -0.0951 21 GLU A CG 23 C CD . GLU A 5 ? 0.5370 0.6011 0.6351 -0.0110 -0.0137 -0.0904 21 GLU A CD 24 O OE1 . GLU A 5 ? 0.5355 0.6009 0.6381 -0.0111 -0.0162 -0.0926 21 GLU A OE1 25 O OE2 . GLU A 5 ? 0.5112 0.5733 0.6015 -0.0107 -0.0132 -0.0848 21 GLU A OE2 26 N N . GLU A 6 ? 0.4711 0.5411 0.5613 -0.0121 0.0041 -0.0991 22 GLU A N 27 C CA . GLU A 6 ? 0.4546 0.5223 0.5403 -0.0122 0.0070 -0.0959 22 GLU A CA 28 C C . GLU A 6 ? 0.4367 0.5036 0.5310 -0.0126 0.0080 -0.0998 22 GLU A C 29 O O . GLU A 6 ? 0.4339 0.4981 0.5276 -0.0125 0.0083 -0.0972 22 GLU A O 30 C CB . GLU A 6 ? 0.4435 0.5127 0.5183 -0.0123 0.0125 -0.0941 22 GLU A CB 31 C CG . GLU A 6 ? 0.4353 0.5041 0.5004 -0.0116 0.0114 -0.0887 22 GLU A CG 32 C CD . GLU A 6 ? 0.4306 0.5003 0.4845 -0.0114 0.0165 -0.0865 22 GLU A CD 33 O OE1 . GLU A 6 ? 0.4138 0.4814 0.4641 -0.0116 0.0195 -0.0840 22 GLU A OE1 34 O OE2 . GLU A 6 ? 0.4320 0.5046 0.4809 -0.0111 0.0172 -0.0874 22 GLU A OE2 35 N N . ILE A 7 ? 0.4277 0.4972 0.5304 -0.0131 0.0083 -0.1062 23 ILE A N 36 C CA . ILE A 7 ? 0.4229 0.4922 0.5355 -0.0134 0.0087 -0.1108 23 ILE A CA 37 C C . ILE A 7 ? 0.4076 0.4733 0.5271 -0.0125 0.0026 -0.1093 23 ILE A C 38 O O . ILE A 7 ? 0.4052 0.4686 0.5268 -0.0123 0.0024 -0.1084 23 ILE A O 39 C CB . ILE A 7 ? 0.4365 0.5097 0.5572 -0.0141 0.0101 -0.1185 23 ILE A CB 40 C CG1 . ILE A 7 ? 0.4457 0.5225 0.5588 -0.0148 0.0158 -0.1200 23 ILE A CG1 41 C CG2 . ILE A 7 ? 0.4321 0.5052 0.5630 -0.0145 0.0111 -0.1233 23 ILE A CG2 42 C CD1 . ILE A 7 ? 0.4524 0.5290 0.5581 -0.0156 0.0222 -0.1183 23 ILE A CD1 43 N N . GLN A 8 ? 0.4326 0.4966 0.5562 -0.0137 -0.0012 -0.1095 24 GLN A N 44 C CA . GLN A 8 ? 0.4436 0.5036 0.5729 -0.0126 -0.0072 -0.1075 24 GLN A CA 45 C CB . GLN A 8 ? 0.4803 0.5400 0.6139 -0.0123 -0.0119 -0.1081 24 GLN A CB 46 C CG . GLN A 8 ? 0.5483 0.6114 0.6911 -0.0128 -0.0116 -0.1156 24 GLN A CG 47 C CD . GLN A 8 ? 0.5977 0.6617 0.7420 -0.0128 -0.0145 -0.1161 24 GLN A CD 48 O OE1 . GLN A 8 ? 0.6582 0.7244 0.8107 -0.0130 -0.0153 -0.1219 24 GLN A OE1 49 N NE2 . GLN A 8 ? 0.6086 0.6709 0.7452 -0.0127 -0.0160 -0.1102 24 GLN A NE2 50 N N . ALA A 9 ? 0.3684 0.4264 0.4783 -0.0106 -0.0070 -0.0955 25 ALA A N 51 C CA . ALA A 9 ? 0.3694 0.4243 0.4711 -0.0101 -0.0075 -0.0888 25 ALA A CA 52 C C . ALA A 9 ? 0.3698 0.4234 0.4709 -0.0100 -0.0050 -0.0883 25 ALA A C 53 O O . ALA A 9 ? 0.3746 0.4249 0.4749 -0.0093 -0.0076 -0.0848 25 ALA A O 54 C CB . ALA A 9 ? 0.3589 0.4155 0.4501 -0.0104 -0.0049 -0.0852 25 ALA A CB 55 N N . LYS A 10 ? 0.3800 0.4363 0.4815 -0.0109 0.0000 -0.0920 26 LYS A N 56 C CA . LYS A 10 ? 0.4042 0.4595 0.5060 -0.0110 0.0030 -0.0923 26 LYS A CA 57 C C . LYS A 10 ? 0.4045 0.4579 0.5166 -0.0103 -0.0007 -0.0949 26 LYS A C 58 O O . LYS A 10 ? 0.3899 0.4409 0.5013 -0.0098 -0.0013 -0.0928 26 LYS A O 59 C CB . LYS A 10 ? 0.4254 0.4839 0.5267 -0.0123 0.0094 -0.0962 26 LYS A CB 60 C CG . LYS A 10 ? 0.4621 0.5196 0.5624 -0.0127 0.0135 -0.0959 26 LYS A CG 61 C CD . LYS A 10 ? 0.4955 0.5558 0.5955 -0.0141 0.0202 -0.0999 26 LYS A CD 62 C CE . LYS A 10 ? 0.5314 0.5902 0.6278 -0.0146 0.0249 -0.0980 26 LYS A CE 63 N NZ . LYS A 10 ? 0.5654 0.6266 0.6597 -0.0161 0.0320 -0.1011 26 LYS A NZ 64 N N . GLU A 11 ? 0.4086 0.4629 0.5300 -0.0102 -0.0035 -0.0998 27 GLU A N 65 C CA . GLU A 11 ? 0.4107 0.4632 0.5424 -0.0092 -0.0079 -0.1028 27 GLU A CA 66 C C . GLU A 11 ? 0.3877 0.4359 0.5173 -0.0078 -0.0138 -0.0976 27 GLU A C 67 O O . GLU A 11 ? 0.3714 0.4172 0.5045 -0.0067 -0.0166 -0.0973 27 GLU A O 68 C CB . GLU A 11 ? 0.4573 0.5120 0.5993 -0.0094 -0.0095 -0.1093 27 GLU A CB 69 C CG . GLU A 11 ? 0.5156 0.5744 0.6618 -0.0107 -0.0038 -0.1154 27 GLU A CG 70 C CD . GLU A 11 ? 0.5748 0.6365 0.7298 -0.0110 -0.0048 -0.1217 27 GLU A CD 71 O OE1 . GLU A 11 ? 0.5925 0.6527 0.7516 -0.0101 -0.0103 -0.1216 27 GLU A OE1 72 O OE2 . GLU A 11 ? 0.5982 0.6636 0.7560 -0.0122 0.0000 -0.1268 27 GLU A OE2 73 N N . TYR A 12 ? 0.3709 0.4184 0.4950 -0.0078 -0.0157 -0.0937 28 TYR A N 74 C CA . TYR A 12 ? 0.3633 0.4067 0.4838 -0.0067 -0.0205 -0.0881 28 TYR A CA 75 C C . TYR A 12 ? 0.3531 0.3944 0.4665 -0.0062 -0.0194 -0.0834 28 TYR A C 76 O O . TYR A 12 ? 0.3366 0.3746 0.4513 -0.0050 -0.0233 -0.0815 28 TYR A O 77 C CB . TYR A 12 ? 0.3668 0.4103 0.4821 -0.0071 -0.0214 -0.0849 28 TYR A CB 78 C CG . TYR A 12 ? 0.3753 0.4148 0.4857 -0.0063 -0.0254 -0.0786 28 TYR A CG 79 C CD1 . TYR A 12 ? 0.3862 0.4221 0.5021 -0.0053 -0.0310 -0.0782 28 TYR A CD1 80 C CD2 . TYR A 12 ? 0.3786 0.4176 0.4787 -0.0065 -0.0234 -0.0730 28 TYR A CD2 81 C CE1 . TYR A 12 ? 0.3909 0.4228 0.5018 -0.0047 -0.0342 -0.0724 28 TYR A CE1 82 C CE2 . TYR A 12 ? 0.3874 0.4229 0.4830 -0.0059 -0.0266 -0.0675 28 TYR A CE2 83 C CZ . TYR A 12 ? 0.3976 0.4296 0.4984 -0.0050 -0.0319 -0.0671 28 TYR A CZ 84 O OH . TYR A 12 ? 0.4104 0.4386 0.5062 -0.0045 -0.0347 -0.0614 28 TYR A OH 85 N N . LEU A 13 ? 0.3417 0.3851 0.4477 -0.0071 -0.0141 -0.0818 29 LEU A N 86 C CA . LEU A 13 ? 0.3473 0.3890 0.4461 -0.0068 -0.0126 -0.0774 29 LEU A CA 87 C C . LEU A 13 ? 0.3646 0.4055 0.4691 -0.0063 -0.0123 -0.0802 29 LEU A C 88 O O . LEU A 13 ? 0.3491 0.3875 0.4515 -0.0053 -0.0143 -0.0772 29 LEU A O 89 C CB . LEU A 13 ? 0.3358 0.3798 0.4259 -0.0078 -0.0069 -0.0753 29 LEU A CB 90 C CG . LEU A 13 ? 0.3347 0.3792 0.4169 -0.0081 -0.0071 -0.0713 29 LEU A CG 91 C CD1 . LEU A 13 ? 0.3376 0.3845 0.4121 -0.0088 -0.0014 -0.0704 29 LEU A CD1 92 C CD2 . LEU A 13 ? 0.3324 0.3738 0.4096 -0.0072 -0.0106 -0.0654 29 LEU A CD2 93 N N . GLU A 14 ? 0.3831 0.4266 0.4953 -0.0070 -0.0099 -0.0863 30 GLU A N 94 C CA . GLU A 14 ? 0.4175 0.4609 0.5371 -0.0067 -0.0097 -0.0902 30 GLU A CA 95 C C . GLU A 14 ? 0.4010 0.4411 0.5257 -0.0048 -0.0163 -0.0899 30 GLU A C 96 O O . GLU A 14 ? 0.3958 0.4341 0.5195 -0.0039 -0.0172 -0.0884 30 GLU A O 97 C CB . GLU A 14 ? 0.4768 0.5235 0.6053 -0.0077 -0.0068 -0.0974 30 GLU A CB 98 C CG . GLU A 14 ? 0.5516 0.6009 0.6770 -0.0093 0.0006 -0.0989 30 GLU A CG 99 C CD . GLU A 14 ? 0.6233 0.6722 0.7527 -0.0094 0.0028 -0.1008 30 GLU A CD 100 O OE1 . GLU A 14 ? 0.6556 0.7040 0.7947 -0.0085 -0.0006 -0.1047 30 GLU A OE1 101 O OE2 . GLU A 14 ? 0.6693 0.7183 0.7924 -0.0103 0.0079 -0.0987 30 GLU A OE2 102 N N . ASN A 15 ? 0.3880 0.4272 0.5178 -0.0041 -0.0209 -0.0913 31 ASN A N 103 C CA A ASN A 15 ? 0.3885 0.4241 0.5227 -0.0022 -0.0276 -0.0909 31 ASN A CA 104 C CA B ASN A 15 ? 0.3853 0.4209 0.5196 -0.0021 -0.0276 -0.0909 31 ASN A CA 105 C C . ASN A 15 ? 0.3784 0.4103 0.5035 -0.0012 -0.0303 -0.0838 31 ASN A C 106 O O . ASN A 15 ? 0.3778 0.4071 0.5036 0.0003 -0.0335 -0.0828 31 ASN A O 107 C CB A ASN A 15 ? 0.3925 0.4277 0.5338 -0.0017 -0.0316 -0.0937 31 ASN A CB 108 C CB B ASN A 15 ? 0.3835 0.4186 0.5249 -0.0017 -0.0318 -0.0936 31 ASN A CB 109 C CG A ASN A 15 ? 0.3976 0.4365 0.5490 -0.0025 -0.0294 -0.1013 31 ASN A CG 110 C CG B ASN A 15 ? 0.3852 0.4159 0.5306 0.0004 -0.0389 -0.0928 31 ASN A CG 111 O OD1 A ASN A 15 ? 0.4064 0.4476 0.5609 -0.0032 -0.0256 -0.1049 31 ASN A OD1 112 O OD1 B ASN A 15 ? 0.3845 0.4152 0.5393 0.0015 -0.0414 -0.0977 31 ASN A OD1 113 N ND2 A ASN A 15 ? 0.3997 0.4391 0.5564 -0.0026 -0.0316 -0.1039 31 ASN A ND2 114 N ND2 B ASN A 15 ? 0.3910 0.4181 0.5293 0.0011 -0.0421 -0.0866 31 ASN A ND2 115 N N . LEU A 16 ? 0.3700 0.4019 0.4869 -0.0020 -0.0290 -0.0791 32 LEU A N 116 C CA . LEU A 16 ? 0.3660 0.3948 0.4741 -0.0013 -0.0311 -0.0724 32 LEU A CA 117 C C . LEU A 16 ? 0.3623 0.3907 0.4649 -0.0010 -0.0289 -0.0699 32 LEU A C 118 O O . LEU A 16 ? 0.3432 0.3684 0.4430 0.0003 -0.0323 -0.0668 32 LEU A O 119 C CB . LEU A 16 ? 0.3635 0.3931 0.4645 -0.0025 -0.0295 -0.0686 32 LEU A CB 120 C CG . LEU A 16 ? 0.3719 0.3985 0.4643 -0.0020 -0.0315 -0.0618 32 LEU A CG 121 C CD1 . LEU A 16 ? 0.3772 0.3994 0.4723 -0.0004 -0.0376 -0.0604 32 LEU A CD1 122 C CD2 . LEU A 16 ? 0.3780 0.4062 0.4652 -0.0032 -0.0296 -0.0593 32 LEU A CD2 123 N N . ASN A 17 ? 0.3622 0.3936 0.4630 -0.0022 -0.0232 -0.0713 33 ASN A N 124 C CA . ASN A 17 ? 0.3703 0.4014 0.4669 -0.0020 -0.0208 -0.0696 33 ASN A CA 125 C C . ASN A 17 ? 0.3751 0.4045 0.4784 -0.0005 -0.0241 -0.0723 33 ASN A C 126 O O . ASN A 17 ? 0.3806 0.4077 0.4801 0.0007 -0.0264 -0.0692 33 ASN A O 127 C CB . ASN A 17 ? 0.3578 0.3920 0.4526 -0.0036 -0.0140 -0.0712 33 ASN A CB 128 C CG . ASN A 17 ? 0.3586 0.3935 0.4430 -0.0045 -0.0108 -0.0664 33 ASN A CG 129 O OD1 . ASN A 17 ? 0.3384 0.3716 0.4155 -0.0039 -0.0116 -0.0614 33 ASN A OD1 130 N ND2 . ASN A 17 ? 0.3567 0.3943 0.4405 -0.0058 -0.0073 -0.0682 33 ASN A ND2 131 N N . LYS A 18 ? 0.3927 0.4235 0.5062 -0.0004 -0.0248 -0.0785 34 LYS A N 132 C CA . LYS A 18 ? 0.3914 0.4210 0.5127 0.0011 -0.0284 -0.0820 34 LYS A CA 133 C C . LYS A 18 ? 0.3812 0.4067 0.5013 0.0033 -0.0355 -0.0791 34 LYS A C 134 O O . LYS A 18 ? 0.3762 0.3998 0.4965 0.0050 -0.0384 -0.0786 34 LYS A O 135 C CB . LYS A 18 ? 0.4249 0.4570 0.5579 0.0007 -0.0277 -0.0895 34 LYS A CB 136 C CG . LYS A 18 ? 0.4501 0.4856 0.5851 -0.0010 -0.0208 -0.0929 34 LYS A CG 137 C CD . LYS A 18 ? 0.4843 0.5226 0.6314 -0.0016 -0.0198 -0.1006 34 LYS A CD 138 C CE . LYS A 18 ? 0.5064 0.5470 0.6540 -0.0031 -0.0173 -0.1022 34 LYS A CE 139 N NZ . LYS A 18 ? 0.5441 0.5875 0.7037 -0.0036 -0.0164 -0.1100 34 LYS A NZ 140 N N . GLU A 19 ? 0.3652 0.3892 0.4839 0.0033 -0.0382 -0.0770 35 GLU A N 141 C CA . GLU A 19 ? 0.3561 0.3758 0.4723 0.0052 -0.0443 -0.0733 35 GLU A CA 142 C C . GLU A 19 ? 0.3475 0.3650 0.4528 0.0056 -0.0444 -0.0667 35 GLU A C 143 O O . GLU A 19 ? 0.3339 0.3481 0.4376 0.0075 -0.0488 -0.0647 35 GLU A O 144 C CB . GLU A 19 ? 0.3686 0.3872 0.4859 0.0047 -0.0465 -0.0725 35 GLU A CB 145 C CG . GLU A 19 ? 0.3928 0.4066 0.5053 0.0061 -0.0517 -0.0673 35 GLU A CG 146 C CD . GLU A 19 ? 0.4168 0.4285 0.5357 0.0067 -0.0559 -0.0690 35 GLU A CD 147 O OE1 . GLU A 19 ? 0.4275 0.4422 0.5516 0.0053 -0.0537 -0.0726 35 GLU A OE1 148 O OE2 . GLU A 19 ? 0.4318 0.4389 0.5505 0.0086 -0.0614 -0.0668 35 GLU A OE2 149 N N . LEU A 20 ? 0.3268 0.3461 0.4246 0.0039 -0.0396 -0.0634 36 LEU A N 150 C CA . LEU A 20 ? 0.3235 0.3413 0.4114 0.0042 -0.0392 -0.0575 36 LEU A CA 151 C C . LEU A 20 ? 0.3219 0.3395 0.4097 0.0053 -0.0390 -0.0584 36 LEU A C 152 O O . LEU A 20 ? 0.3149 0.3299 0.3977 0.0067 -0.0418 -0.0549 36 LEU A O 153 C CB . LEU A 20 ? 0.3218 0.3419 0.4024 0.0023 -0.0341 -0.0544 36 LEU A CB 154 C CG . LEU A 20 ? 0.3314 0.3511 0.4099 0.0014 -0.0349 -0.0521 36 LEU A CG 155 C CD1 . LEU A 20 ? 0.3253 0.3480 0.3984 -0.0002 -0.0298 -0.0506 36 LEU A CD1 156 C CD2 . LEU A 20 ? 0.3308 0.3465 0.4042 0.0025 -0.0392 -0.0470 36 LEU A CD2 157 N N . ALA A 21 ? 0.3186 0.3390 0.4122 0.0047 -0.0356 -0.0632 37 ALA A N 158 C CA . ALA A 21 ? 0.3215 0.3422 0.4169 0.0056 -0.0351 -0.0650 37 ALA A CA 159 C C . ALA A 21 ? 0.3276 0.3455 0.4269 0.0082 -0.0417 -0.0663 37 ALA A C 160 O O . ALA A 21 ? 0.3211 0.3374 0.4165 0.0096 -0.0435 -0.0642 37 ALA A O 161 C CB . ALA A 21 ? 0.3238 0.3479 0.4265 0.0043 -0.0304 -0.0707 37 ALA A CB 162 N N . LYS A 22 ? 0.3273 0.3444 0.4341 0.0089 -0.0454 -0.0697 38 LYS A N 163 C CA . LYS A 22 ? 0.3360 0.3504 0.4473 0.0116 -0.0519 -0.0715 38 LYS A CA 164 C C . LYS A 22 ? 0.3385 0.3485 0.4412 0.0132 -0.0565 -0.0653 38 LYS A C 165 O O . LYS A 22 ? 0.3431 0.3508 0.4443 0.0154 -0.0605 -0.0647 38 LYS A O 166 C CB . LYS A 22 ? 0.3457 0.3605 0.4675 0.0119 -0.0544 -0.0768 38 LYS A CB 167 C CG . LYS A 22 ? 0.3472 0.3602 0.4764 0.0147 -0.0604 -0.0807 38 LYS A CG 168 C CD . LYS A 22 ? 0.3372 0.3530 0.4723 0.0150 -0.0585 -0.0856 38 LYS A CD 169 C CE . LYS A 22 ? 0.3339 0.3495 0.4806 0.0172 -0.0636 -0.0920 38 LYS A CE 170 N NZ . LYS A 22 ? 0.3313 0.3471 0.4806 0.0191 -0.0656 -0.0945 38 LYS A NZ 171 N N . ARG A 23 ? 0.3354 0.3442 0.4325 0.0120 -0.0559 -0.0610 39 ARG A N 172 C CA . ARG A 23 ? 0.3446 0.3493 0.4331 0.0130 -0.0593 -0.0548 39 ARG A CA 173 C C . ARG A 23 ? 0.3520 0.3568 0.4314 0.0131 -0.0573 -0.0507 39 ARG A C 174 O O . ARG A 23 ? 0.3598 0.3614 0.4340 0.0150 -0.0610 -0.0475 39 ARG A O 175 C CB . ARG A 23 ? 0.3362 0.3403 0.4216 0.0114 -0.0584 -0.0514 39 ARG A CB 176 C CG . ARG A 23 ? 0.3348 0.3370 0.4276 0.0119 -0.0622 -0.0540 39 ARG A CG 177 C CD . ARG A 23 ? 0.3382 0.3408 0.4293 0.0099 -0.0603 -0.0518 39 ARG A CD 178 N NE . ARG A 23 ? 0.3395 0.3407 0.4388 0.0104 -0.0637 -0.0549 39 ARG A NE 179 C CZ . ARG A 23 ? 0.3444 0.3407 0.4433 0.0117 -0.0688 -0.0524 39 ARG A CZ 180 N NH1 . ARG A 23 ? 0.3439 0.3362 0.4342 0.0126 -0.0709 -0.0465 39 ARG A NH1 181 N NH2 . ARG A 23 ? 0.3462 0.3414 0.4533 0.0121 -0.0718 -0.0557 39 ARG A NH2 182 N N . THR A 24 ? 0.3485 0.3568 0.4261 0.0113 -0.0514 -0.0510 40 THR A N 183 C CA . THR A 24 ? 0.3625 0.3712 0.4321 0.0112 -0.0491 -0.0474 40 THR A CA 184 C C . THR A 24 ? 0.3649 0.3735 0.4374 0.0132 -0.0511 -0.0503 40 THR A C 185 O O . THR A 24 ? 0.3717 0.3789 0.4377 0.0143 -0.0522 -0.0471 40 THR A O 186 C CB . THR A 24 ? 0.3538 0.3660 0.4206 0.0088 -0.0424 -0.0468 40 THR A CB 187 O OG1 . THR A 24 ? 0.3530 0.3657 0.4182 0.0073 -0.0411 -0.0449 40 THR A OG1 188 C CG2 . THR A 24 ? 0.3562 0.3684 0.4140 0.0089 -0.0403 -0.0423 40 THR A CG2 189 N N . ASN A 25 ? 0.3659 0.3761 0.4484 0.0136 -0.0515 -0.0565 41 ASN A N 190 C CA . ASN A 25 ? 0.3611 0.3711 0.4479 0.0157 -0.0543 -0.0600 41 ASN A CA 191 C C . ASN A 25 ? 0.3714 0.3774 0.4539 0.0185 -0.0609 -0.0573 41 ASN A C 192 O O . ASN A 25 ? 0.3643 0.3696 0.4430 0.0200 -0.0622 -0.0564 41 ASN A O 193 C CB . ASN A 25 ? 0.3640 0.3761 0.4633 0.0158 -0.0547 -0.0673 41 ASN A CB 194 C CG . ASN A 25 ? 0.3753 0.3872 0.4800 0.0182 -0.0583 -0.0715 41 ASN A CG 195 O OD1 . ASN A 25 ? 0.3836 0.3932 0.4916 0.0207 -0.0645 -0.0730 41 ASN A OD1 196 N ND2 . ASN A 25 ? 0.3633 0.3776 0.4690 0.0177 -0.0546 -0.0732 41 ASN A ND2 197 N N . VAL A 26 ? 0.3738 0.3768 0.4565 0.0192 -0.0649 -0.0560 42 VAL A N 198 C CA . VAL A 26 ? 0.3907 0.3891 0.4690 0.0219 -0.0713 -0.0531 42 VAL A CA 199 C C . VAL A 26 ? 0.3879 0.3844 0.4538 0.0219 -0.0706 -0.0463 42 VAL A C 200 O O . VAL A 26 ? 0.3882 0.3824 0.4496 0.0242 -0.0742 -0.0449 42 VAL A O 201 C CB . VAL A 26 ? 0.4069 0.4023 0.4884 0.0223 -0.0751 -0.0529 42 VAL A CB 202 C CG1 . VAL A 26 ? 0.4211 0.4110 0.4963 0.0249 -0.0812 -0.0487 42 VAL A CG1 203 C CG2 . VAL A 26 ? 0.4055 0.4026 0.4998 0.0229 -0.0767 -0.0602 42 VAL A CG2 204 N N . GLU A 27 ? 0.3730 0.3704 0.4335 0.0194 -0.0662 -0.0423 43 GLU A N 205 C CA . GLU A 27 ? 0.3678 0.3641 0.4171 0.0190 -0.0648 -0.0361 43 GLU A CA 206 C C . GLU A 27 ? 0.3537 0.3521 0.4005 0.0196 -0.0628 -0.0369 43 GLU A C 207 O O . GLU A 27 ? 0.3473 0.3438 0.3871 0.0211 -0.0648 -0.0339 43 GLU A O 208 C CB . GLU A 27 ? 0.3815 0.3791 0.4268 0.0162 -0.0601 -0.0327 43 GLU A CB 209 C CG . GLU A 27 ? 0.3984 0.3950 0.4328 0.0157 -0.0587 -0.0265 43 GLU A CG 210 C CD . GLU A 27 ? 0.4290 0.4282 0.4603 0.0130 -0.0535 -0.0240 43 GLU A CD 211 O OE1 . GLU A 27 ? 0.4328 0.4356 0.4681 0.0116 -0.0494 -0.0269 43 GLU A OE1 212 O OE2 . GLU A 27 ? 0.4290 0.4264 0.4537 0.0123 -0.0534 -0.0191 43 GLU A OE2 213 N N . THR A 28 ? 0.3407 0.3430 0.3936 0.0183 -0.0587 -0.0411 44 THR A N 214 C CA . THR A 28 ? 0.3407 0.3453 0.3925 0.0185 -0.0562 -0.0422 44 THR A CA 215 C C . THR A 28 ? 0.3490 0.3522 0.4025 0.0215 -0.0611 -0.0447 44 THR A C 216 O O . THR A 28 ? 0.3492 0.3523 0.3971 0.0225 -0.0611 -0.0430 44 THR A O 217 C CB . THR A 28 ? 0.3301 0.3386 0.3885 0.0165 -0.0507 -0.0463 44 THR A CB 218 O OG1 . THR A 28 ? 0.3209 0.3306 0.3771 0.0141 -0.0466 -0.0440 44 THR A OG1 219 C CG2 . THR A 28 ? 0.3312 0.3416 0.3874 0.0164 -0.0473 -0.0465 44 THR A CG2 220 N N . GLU A 29 ? 0.3555 0.3576 0.4167 0.0232 -0.0656 -0.0489 45 GLU A N 221 C CA . GLU A 29 ? 0.3693 0.3700 0.4325 0.0264 -0.0711 -0.0516 45 GLU A CA 222 C C . GLU A 29 ? 0.3676 0.3643 0.4203 0.0284 -0.0752 -0.0463 45 GLU A C 223 O O . GLU A 29 ? 0.3658 0.3624 0.4156 0.0305 -0.0773 -0.0468 45 GLU A O 224 C CB . GLU A 29 ? 0.3921 0.3921 0.4657 0.0279 -0.0754 -0.0570 45 GLU A CB 225 C CG . GLU A 29 ? 0.4118 0.4159 0.4971 0.0267 -0.0723 -0.0639 45 GLU A CG 226 C CD . GLU A 29 ? 0.4392 0.4455 0.5280 0.0280 -0.0722 -0.0679 45 GLU A CD 227 O OE1 . GLU A 29 ? 0.4569 0.4617 0.5389 0.0300 -0.0749 -0.0656 45 GLU A OE1 228 O OE2 . GLU A 29 ? 0.4452 0.4548 0.5435 0.0269 -0.0691 -0.0735 45 GLU A OE2 229 N N . ALA A 30 ? 0.3598 0.3534 0.4070 0.0279 -0.0763 -0.0415 46 ALA A N 230 C CA . ALA A 30 ? 0.3644 0.3540 0.4009 0.0294 -0.0796 -0.0359 46 ALA A CA 231 C C . ALA A 30 ? 0.3647 0.3557 0.3921 0.0284 -0.0756 -0.0319 46 ALA A C 232 O O . ALA A 30 ? 0.3632 0.3522 0.3832 0.0303 -0.0782 -0.0294 46 ALA A O 233 C CB . ALA A 30 ? 0.3672 0.3530 0.4007 0.0287 -0.0811 -0.0318 46 ALA A CB 234 N N . ALA A 31 ? 0.3470 0.3413 0.3747 0.0255 -0.0695 -0.0312 47 ALA A N 235 C CA . ALA A 31 ? 0.3569 0.3531 0.3772 0.0244 -0.0654 -0.0279 47 ALA A CA 236 C C . ALA A 31 ? 0.3576 0.3559 0.3799 0.0258 -0.0653 -0.0315 47 ALA A C 237 O O . ALA A 31 ? 0.3669 0.3652 0.3820 0.0266 -0.0652 -0.0290 47 ALA A O 238 C CB . ALA A 31 ? 0.3442 0.3432 0.3650 0.0212 -0.0592 -0.0267 47 ALA A CB 239 N N . TRP A 32 ? 0.3597 0.3601 0.3921 0.0261 -0.0654 -0.0375 48 TRP A N 240 C CA . TRP A 32 ? 0.3627 0.3652 0.3989 0.0276 -0.0657 -0.0418 48 TRP A CA 241 C C . TRP A 32 ? 0.3761 0.3760 0.4087 0.0311 -0.0721 -0.0420 48 TRP A C 242 O O . TRP A 32 ? 0.3773 0.3781 0.4064 0.0322 -0.0721 -0.0421 48 TRP A O 243 C CB . TRP A 32 ? 0.3599 0.3649 0.4086 0.0270 -0.0645 -0.0485 48 TRP A CB 244 C CG . TRP A 32 ? 0.3660 0.3727 0.4205 0.0289 -0.0662 -0.0538 48 TRP A CG 245 C CD1 . TRP A 32 ? 0.3715 0.3771 0.4306 0.0320 -0.0723 -0.0578 48 TRP A CD1 246 C CD2 . TRP A 32 ? 0.3624 0.3721 0.4189 0.0280 -0.0619 -0.0559 48 TRP A CD2 247 N NE1 . TRP A 32 ? 0.3740 0.3821 0.4382 0.0330 -0.0720 -0.0625 48 TRP A NE1 248 C CE2 . TRP A 32 ? 0.3703 0.3808 0.4331 0.0305 -0.0656 -0.0613 48 TRP A CE2 249 C CE3 . TRP A 32 ? 0.3597 0.3714 0.4134 0.0255 -0.0554 -0.0537 48 TRP A CE3 250 C CZ2 . TRP A 32 ? 0.3648 0.3780 0.4316 0.0303 -0.0627 -0.0647 48 TRP A CZ2 251 C CZ3 . TRP A 32 ? 0.3597 0.3737 0.4170 0.0254 -0.0526 -0.0567 48 TRP A CZ3 252 C CH2 . TRP A 32 ? 0.3593 0.3741 0.4233 0.0277 -0.0561 -0.0622 48 TRP A CH2 253 N N . ALA A 33 ? 0.3847 0.3813 0.4182 0.0328 -0.0774 -0.0420 49 ALA A N 254 C CA . ALA A 33 ? 0.4007 0.3943 0.4306 0.0365 -0.0841 -0.0422 49 ALA A CA 255 C C . ALA A 33 ? 0.4106 0.4021 0.4274 0.0371 -0.0844 -0.0361 49 ALA A C 256 O O . ALA A 33 ? 0.4304 0.4212 0.4432 0.0398 -0.0877 -0.0368 49 ALA A O 257 C CB . ALA A 33 ? 0.4052 0.3952 0.4382 0.0381 -0.0895 -0.0429 49 ALA A CB 258 N N . TYR A 34 ? 0.4047 0.3952 0.4151 0.0347 -0.0809 -0.0306 50 TYR A N 259 C CA . TYR A 34 ? 0.4065 0.3953 0.4049 0.0348 -0.0802 -0.0246 50 TYR A CA 260 C C . TYR A 34 ? 0.3952 0.3876 0.3907 0.0341 -0.0761 -0.0248 50 TYR A C 261 O O . TYR A 34 ? 0.3897 0.3814 0.3778 0.0358 -0.0777 -0.0230 50 TYR A O 262 C CB . TYR A 34 ? 0.4148 0.4019 0.4085 0.0322 -0.0775 -0.0192 50 TYR A CB 263 C CG . TYR A 34 ? 0.4377 0.4231 0.4194 0.0319 -0.0763 -0.0130 50 TYR A CG 264 C CD1 . TYR A 34 ? 0.4480 0.4293 0.4218 0.0345 -0.0809 -0.0104 50 TYR A CD1 265 C CD2 . TYR A 34 ? 0.4442 0.4322 0.4224 0.0291 -0.0705 -0.0100 50 TYR A CD2 266 C CE1 . TYR A 34 ? 0.4709 0.4508 0.4338 0.0341 -0.0794 -0.0049 50 TYR A CE1 267 C CE2 . TYR A 34 ? 0.4593 0.4460 0.4271 0.0287 -0.0692 -0.0047 50 TYR A CE2 268 C CZ . TYR A 34 ? 0.4760 0.4587 0.4363 0.0311 -0.0735 -0.0022 50 TYR A CZ 269 O OH . TYR A 34 ? 0.4952 0.4767 0.4452 0.0307 -0.0720 0.0029 50 TYR A OH 270 N N . GLY A 35 ? 0.3758 0.3720 0.3771 0.0316 -0.0708 -0.0268 51 GLY A N 271 C CA . GLY A 35 ? 0.3717 0.3712 0.3714 0.0308 -0.0666 -0.0271 51 GLY A CA 272 C C . GLY A 35 ? 0.3704 0.3713 0.3737 0.0333 -0.0692 -0.0320 51 GLY A C 273 O O . GLY A 35 ? 0.3736 0.3762 0.3731 0.0336 -0.0676 -0.0316 51 GLY A O 274 N N . SER A 36 ? 0.3764 0.3768 0.3877 0.0350 -0.0733 -0.0368 52 SER A N 275 C CA . SER A 36 ? 0.3862 0.3879 0.4024 0.0377 -0.0766 -0.0423 52 SER A CA 276 C C . SER A 36 ? 0.3934 0.3921 0.4023 0.0412 -0.0829 -0.0411 52 SER A C 277 O O . SER A 36 ? 0.3973 0.3972 0.4079 0.0436 -0.0856 -0.0449 52 SER A O 278 C CB . SER A 36 ? 0.3983 0.4009 0.4270 0.0381 -0.0784 -0.0486 52 SER A CB 279 O OG . SER A 36 ? 0.4156 0.4212 0.4515 0.0350 -0.0724 -0.0505 52 SER A OG 280 N N . ASN A 37 ? 0.4016 0.3964 0.4026 0.0415 -0.0850 -0.0359 53 ASN A N 281 C CA . ASN A 37 ? 0.4163 0.4073 0.4103 0.0450 -0.0915 -0.0345 53 ASN A CA 282 C C . ASN A 37 ? 0.4165 0.4034 0.3997 0.0442 -0.0915 -0.0271 53 ASN A C 283 O O . ASN A 37 ? 0.4127 0.3961 0.3966 0.0444 -0.0941 -0.0256 53 ASN A O 284 C CB . ASN A 37 ? 0.4370 0.4267 0.4395 0.0475 -0.0973 -0.0396 53 ASN A CB 285 C CG . ASN A 37 ? 0.4699 0.4557 0.4658 0.0517 -0.1046 -0.0389 53 ASN A CG 286 O OD1 . ASN A 37 ? 0.4660 0.4514 0.4531 0.0532 -0.1055 -0.0370 53 ASN A OD1 287 N ND2 . ASN A 37 ? 0.4884 0.4711 0.4885 0.0536 -0.1099 -0.0406 53 ASN A ND2 288 N N . ILE A 38 ? 0.4175 0.4048 0.3913 0.0432 -0.0883 -0.0227 54 ILE A N 289 C CA . ILE A 38 ? 0.4268 0.4106 0.3906 0.0419 -0.0872 -0.0157 54 ILE A CA 290 C C . ILE A 38 ? 0.4559 0.4343 0.4119 0.0450 -0.0933 -0.0130 54 ILE A C 291 O O . ILE A 38 ? 0.4594 0.4372 0.4084 0.0475 -0.0958 -0.0128 54 ILE A O 292 C CB . ILE A 38 ? 0.4250 0.4112 0.3815 0.0400 -0.0819 -0.0120 54 ILE A CB 293 C CG1 . ILE A 38 ? 0.4100 0.4008 0.3737 0.0369 -0.0759 -0.0140 54 ILE A CG1 294 C CG2 . ILE A 38 ? 0.4251 0.4079 0.3717 0.0387 -0.0807 -0.0050 54 ILE A CG2 295 C CD1 . ILE A 38 ? 0.4082 0.4019 0.3665 0.0353 -0.0709 -0.0115 54 ILE A CD1 296 N N . THR A 39 ? 0.4570 0.4314 0.4142 0.0450 -0.0958 -0.0113 55 THR A N 297 C CA . THR A 39 ? 0.4724 0.4406 0.4215 0.0477 -0.1013 -0.0078 55 THR A CA 298 C C . THR A 39 ? 0.4811 0.4455 0.4274 0.0453 -0.0997 -0.0023 55 THR A C 299 O O . THR A 39 ? 0.4506 0.4171 0.4038 0.0423 -0.0959 -0.0028 55 THR A O 300 C CB . THR A 39 ? 0.4741 0.4404 0.4292 0.0514 -0.1084 -0.0127 55 THR A CB 301 O OG1 . THR A 39 ? 0.4651 0.4313 0.4307 0.0502 -0.1086 -0.0152 55 THR A OG1 302 C CG2 . THR A 39 ? 0.4729 0.4434 0.4328 0.0536 -0.1100 -0.0190 55 THR A CG2 303 N N . ASP A 40 ? 0.5021 0.4608 0.4383 0.0467 -0.1025 0.0027 56 ASP A N 304 C CA . ASP A 40 ? 0.5269 0.4813 0.4606 0.0447 -0.1014 0.0080 56 ASP A CA 305 C C . ASP A 40 ? 0.5346 0.4878 0.4790 0.0446 -0.1038 0.0050 56 ASP A C 306 O O . ASP A 40 ? 0.5232 0.4761 0.4710 0.0416 -0.1007 0.0068 56 ASP A O 307 C CB . ASP A 40 ? 0.5618 0.5094 0.4830 0.0466 -0.1046 0.0137 56 ASP A CB 308 C CG . ASP A 40 ? 0.5793 0.5277 0.4892 0.0456 -0.1007 0.0181 56 ASP A CG 309 O OD1 . ASP A 40 ? 0.5756 0.5296 0.4875 0.0431 -0.0954 0.0171 56 ASP A OD1 310 O OD2 . ASP A 40 ? 0.6220 0.5653 0.5209 0.0472 -0.1030 0.0226 56 ASP A OD2 311 N N . GLU A 41 ? 0.5473 0.5000 0.4973 0.0479 -0.1094 0.0000 57 GLU A N 312 C CA . GLU A 41 ? 0.5706 0.5224 0.5314 0.0483 -0.1123 -0.0036 57 GLU A CA 313 C C . GLU A 41 ? 0.5370 0.4948 0.5092 0.0451 -0.1074 -0.0080 57 GLU A C 314 O O . GLU A 41 ? 0.5266 0.4839 0.5050 0.0432 -0.1063 -0.0080 57 GLU A O 315 C CB . GLU A 41 ? 0.6150 0.5651 0.5791 0.0528 -0.1197 -0.0083 57 GLU A CB 316 C CG . GLU A 41 ? 0.6909 0.6392 0.6654 0.0536 -0.1234 -0.0118 57 GLU A CG 317 C CD . GLU A 41 ? 0.7513 0.6981 0.7298 0.0583 -0.1310 -0.0169 57 GLU A CD 318 O OE1 . GLU A 41 ? 0.7602 0.7104 0.7387 0.0603 -0.1322 -0.0206 57 GLU A OE1 319 O OE2 . GLU A 41 ? 0.7880 0.7306 0.7704 0.0601 -0.1359 -0.0174 57 GLU A OE2 320 N N . ASN A 42 ? 0.5199 0.4834 0.4950 0.0447 -0.1045 -0.0116 58 ASN A N 321 C CA . ASN A 42 ? 0.4977 0.4667 0.4823 0.0417 -0.0993 -0.0153 58 ASN A CA 322 C C . ASN A 42 ? 0.4859 0.4561 0.4673 0.0377 -0.0930 -0.0107 58 ASN A C 323 O O . ASN A 42 ? 0.4817 0.4545 0.4707 0.0353 -0.0898 -0.0125 58 ASN A O 324 C CB . ASN A 42 ? 0.4940 0.4682 0.4818 0.0422 -0.0976 -0.0199 58 ASN A CB 325 C CG . ASN A 42 ? 0.5001 0.4750 0.4962 0.0454 -0.1027 -0.0265 58 ASN A CG 326 O OD1 . ASN A 42 ? 0.4979 0.4702 0.4994 0.0468 -0.1069 -0.0285 58 ASN A OD1 327 N ND2 . ASN A 42 ? 0.4865 0.4650 0.4842 0.0466 -0.1024 -0.0303 58 ASN A ND2 328 N N . GLU A 43 ? 0.4878 0.4562 0.4581 0.0372 -0.0915 -0.0049 59 GLU A N 329 C CA . GLU A 43 ? 0.4969 0.4659 0.4636 0.0337 -0.0860 -0.0003 59 GLU A CA 330 C C . GLU A 43 ? 0.5081 0.4737 0.4781 0.0325 -0.0870 0.0013 59 GLU A C 331 O O . GLU A 43 ? 0.4723 0.4405 0.4478 0.0296 -0.0832 0.0008 59 GLU A O 332 C CB . GLU A 43 ? 0.5139 0.4810 0.4682 0.0336 -0.0848 0.0053 59 GLU A CB 333 C CG . GLU A 43 ? 0.5397 0.5077 0.4907 0.0300 -0.0793 0.0098 59 GLU A CG 334 C CD . GLU A 43 ? 0.5758 0.5419 0.5149 0.0299 -0.0779 0.0154 59 GLU A CD 335 O OE1 . GLU A 43 ? 0.6128 0.5758 0.5451 0.0326 -0.0816 0.0165 59 GLU A OE1 336 O OE2 . GLU A 43 ? 0.5943 0.5619 0.5308 0.0270 -0.0731 0.0186 59 GLU A OE2 337 N N . LYS A 44 ? 0.5223 0.4821 0.4890 0.0348 -0.0923 0.0033 60 LYS A N 338 C CA . LYS A 44 ? 0.5455 0.5011 0.5151 0.0342 -0.0941 0.0050 60 LYS A CA 339 C C . LYS A 44 ? 0.5270 0.4856 0.5096 0.0333 -0.0940 -0.0005 60 LYS A C 340 O O . LYS A 44 ? 0.5314 0.4901 0.5180 0.0308 -0.0917 0.0002 60 LYS A O 341 C CB . LYS A 44 ? 0.5732 0.5219 0.5378 0.0376 -0.1007 0.0071 60 LYS A CB 342 C CG . LYS A 44 ? 0.6213 0.5642 0.5850 0.0367 -0.1019 0.0112 60 LYS A CG 343 C CD . LYS A 44 ? 0.6598 0.5953 0.6146 0.0399 -0.1074 0.0151 60 LYS A CD 344 C CE . LYS A 44 ? 0.6958 0.6250 0.6493 0.0388 -0.1082 0.0198 60 LYS A CE 345 N NZ . LYS A 44 ? 0.7054 0.6339 0.6705 0.0390 -0.1109 0.0158 60 LYS A NZ 346 N N . LYS A 45 ? 0.5129 0.4741 0.5021 0.0353 -0.0963 -0.0064 61 LYS A N 347 C CA . LYS A 45 ? 0.5078 0.4719 0.5096 0.0348 -0.0963 -0.0123 61 LYS A CA 348 C C . LYS A 45 ? 0.4829 0.4527 0.4892 0.0312 -0.0896 -0.0139 61 LYS A C 349 O O . LYS A 45 ? 0.4880 0.4588 0.5013 0.0294 -0.0882 -0.0155 61 LYS A O 350 C CB . LYS A 45 ? 0.5223 0.4876 0.5302 0.0380 -0.1007 -0.0184 61 LYS A CB 351 C CG . LYS A 45 ? 0.5656 0.5249 0.5726 0.0415 -0.1082 -0.0182 61 LYS A CG 352 C CD . LYS A 45 ? 0.5953 0.5551 0.6044 0.0453 -0.1131 -0.0228 61 LYS A CD 353 C CE . LYS A 45 ? 0.6317 0.5849 0.6384 0.0490 -0.1207 -0.0217 61 LYS A CE 354 N NZ . LYS A 45 ? 0.6673 0.6207 0.6753 0.0531 -0.1263 -0.0261 61 LYS A NZ 355 N N . LYS A 46 ? 0.4547 0.4281 0.4569 0.0303 -0.0857 -0.0133 62 LYS A N 356 C CA . LYS A 46 ? 0.4370 0.4154 0.4417 0.0271 -0.0792 -0.0139 62 LYS A CA 357 C C . LYS A 46 ? 0.4244 0.4018 0.4269 0.0244 -0.0765 -0.0097 62 LYS A C 358 O O . LYS A 46 ? 0.4249 0.4048 0.4339 0.0224 -0.0738 -0.0118 62 LYS A O 359 C CB . LYS A 46 ? 0.4339 0.4153 0.4325 0.0269 -0.0759 -0.0127 62 LYS A CB 360 C CG . LYS A 46 ? 0.4404 0.4263 0.4399 0.0237 -0.0694 -0.0125 62 LYS A CG 361 C CD . LYS A 46 ? 0.4436 0.4317 0.4360 0.0234 -0.0663 -0.0102 62 LYS A CD 362 C CE . LYS A 46 ? 0.4480 0.4401 0.4414 0.0205 -0.0601 -0.0097 62 LYS A CE 363 N NZ . LYS A 46 ? 0.4649 0.4596 0.4531 0.0202 -0.0568 -0.0085 62 LYS A NZ 364 N N . ASN A 47 ? 0.4257 0.3993 0.4190 0.0245 -0.0772 -0.0040 63 ASN A N 365 C CA . ASN A 47 ? 0.4227 0.3955 0.4133 0.0218 -0.0743 0.0002 63 ASN A CA 366 C C . ASN A 47 ? 0.4265 0.3962 0.4228 0.0214 -0.0766 -0.0001 63 ASN A C 367 O O . ASN A 47 ? 0.4201 0.3911 0.4187 0.0188 -0.0735 0.0008 63 ASN A O 368 C CB . ASN A 47 ? 0.4116 0.3814 0.3907 0.0218 -0.0739 0.0064 63 ASN A CB 369 C CG . ASN A 47 ? 0.4052 0.3791 0.3793 0.0211 -0.0698 0.0071 63 ASN A CG 370 O OD1 . ASN A 47 ? 0.3881 0.3669 0.3669 0.0201 -0.0666 0.0038 63 ASN A OD1 371 N ND2 . ASN A 47 ? 0.3925 0.3643 0.3569 0.0216 -0.0698 0.0115 63 ASN A ND2 372 N N A GLU A 48 ? 0.4349 0.4007 0.4340 0.0240 -0.0822 -0.0018 64 GLU A N 373 N N B GLU A 48 ? 0.4375 0.4033 0.4365 0.0241 -0.0823 -0.0017 64 GLU A N 374 C CA A GLU A 48 ? 0.4391 0.4019 0.4445 0.0240 -0.0850 -0.0026 64 GLU A CA 375 C CA B GLU A 48 ? 0.4446 0.4073 0.4501 0.0241 -0.0852 -0.0028 64 GLU A CA 376 C C A GLU A 48 ? 0.4280 0.3954 0.4447 0.0227 -0.0832 -0.0086 64 GLU A C 377 C C B GLU A 48 ? 0.4303 0.3979 0.4467 0.0226 -0.0828 -0.0084 64 GLU A C 378 O O A GLU A 48 ? 0.4288 0.3960 0.4502 0.0210 -0.0822 -0.0088 64 GLU A O 379 O O B GLU A 48 ? 0.4292 0.3970 0.4496 0.0206 -0.0812 -0.0082 64 GLU A O 380 C CB A GLU A 48 ? 0.4525 0.4093 0.4570 0.0274 -0.0918 -0.0024 64 GLU A CB 381 C CB B GLU A 48 ? 0.4610 0.4189 0.4676 0.0278 -0.0921 -0.0042 64 GLU A CB 382 C CG A GLU A 48 ? 0.4673 0.4183 0.4605 0.0282 -0.0934 0.0042 64 GLU A CG 383 C CG B GLU A 48 ? 0.4797 0.4352 0.4952 0.0282 -0.0954 -0.0068 64 GLU A CG 384 C CD A GLU A 48 ? 0.4840 0.4284 0.4755 0.0317 -0.1003 0.0049 64 GLU A CD 385 C CD B GLU A 48 ? 0.4962 0.4496 0.5167 0.0319 -0.1017 -0.0111 64 GLU A CD 386 O OE1 A GLU A 48 ? 0.4824 0.4275 0.4801 0.0343 -0.1043 -0.0002 64 GLU A OE1 387 O OE1 B GLU A 48 ? 0.5105 0.4665 0.5312 0.0336 -0.1024 -0.0142 64 GLU A OE1 388 O OE2 A GLU A 48 ? 0.4940 0.4325 0.4780 0.0320 -0.1018 0.0105 64 GLU A OE2 389 O OE2 B GLU A 48 ? 0.4936 0.4427 0.5183 0.0331 -0.1059 -0.0115 64 GLU A OE2 390 N N . ILE A 49 ? 0.4206 0.3921 0.4417 0.0235 -0.0824 -0.0134 65 ILE A N 391 C CA . ILE A 49 ? 0.4123 0.3884 0.4437 0.0222 -0.0802 -0.0191 65 ILE A CA 392 C C . ILE A 49 ? 0.3991 0.3795 0.4295 0.0189 -0.0737 -0.0180 65 ILE A C 393 O O . ILE A 49 ? 0.3851 0.3677 0.4222 0.0172 -0.0718 -0.0206 65 ILE A O 394 C CB . ILE A 49 ? 0.4276 0.4063 0.4643 0.0241 -0.0815 -0.0247 65 ILE A CB 395 C CG1 . ILE A 49 ? 0.4466 0.4210 0.4866 0.0275 -0.0885 -0.0267 65 ILE A CG1 396 C CG2 . ILE A 49 ? 0.4125 0.3964 0.4586 0.0224 -0.0777 -0.0302 65 ILE A CG2 397 C CD1 . ILE A 49 ? 0.4501 0.4248 0.4898 0.0304 -0.0916 -0.0294 65 ILE A CD1 398 N N . SER A 50 ? 0.3892 0.3707 0.4112 0.0180 -0.0705 -0.0141 66 SER A N 399 C CA . SER A 50 ? 0.3779 0.3630 0.3979 0.0151 -0.0649 -0.0124 66 SER A CA 400 C C . SER A 50 ? 0.3741 0.3572 0.3939 0.0134 -0.0647 -0.0096 66 SER A C 401 O O . SER A 50 ? 0.3682 0.3545 0.3920 0.0114 -0.0614 -0.0111 66 SER A O 402 C CB . SER A 50 ? 0.3732 0.3594 0.3842 0.0148 -0.0621 -0.0087 66 SER A CB 403 O OG . SER A 50 ? 0.3859 0.3755 0.3984 0.0154 -0.0604 -0.0119 66 SER A OG 404 N N . ALA A 51 ? 0.3760 0.3539 0.3913 0.0143 -0.0680 -0.0055 67 ALA A N 405 C CA . ALA A 51 ? 0.3810 0.3562 0.3966 0.0129 -0.0682 -0.0027 67 ALA A CA 406 C C . ALA A 51 ? 0.3851 0.3608 0.4111 0.0126 -0.0697 -0.0073 67 ALA A C 407 O O . ALA A 51 ? 0.3908 0.3677 0.4198 0.0105 -0.0676 -0.0073 67 ALA A O 408 C CB . ALA A 51 ? 0.3896 0.3584 0.3987 0.0142 -0.0719 0.0021 67 ALA A CB 409 N N . GLU A 52 ? 0.3761 0.3509 0.4077 0.0148 -0.0734 -0.0114 68 GLU A N 410 C CA . GLU A 52 ? 0.3695 0.3450 0.4115 0.0149 -0.0750 -0.0165 68 GLU A CA 411 C C . GLU A 52 ? 0.3548 0.3367 0.4020 0.0126 -0.0700 -0.0203 68 GLU A C 412 O O . GLU A 52 ? 0.3420 0.3248 0.3943 0.0111 -0.0690 -0.0218 68 GLU A O 413 C CB . GLU A 52 ? 0.3655 0.3394 0.4124 0.0178 -0.0798 -0.0205 68 GLU A CB 414 C CG . GLU A 52 ? 0.3665 0.3407 0.4246 0.0183 -0.0822 -0.0259 68 GLU A CG 415 C CD . GLU A 52 ? 0.3724 0.3439 0.4346 0.0216 -0.0879 -0.0290 68 GLU A CD 416 O OE1 . GLU A 52 ? 0.3729 0.3401 0.4282 0.0237 -0.0914 -0.0255 68 GLU A OE1 417 O OE2 . GLU A 52 ? 0.3719 0.3458 0.4440 0.0221 -0.0889 -0.0351 68 GLU A OE2 418 N N . LEU A 53 ? 0.3489 0.3348 0.3945 0.0125 -0.0668 -0.0219 69 LEU A N 419 C CA . LEU A 53 ? 0.3439 0.3354 0.3931 0.0104 -0.0617 -0.0251 69 LEU A CA 420 C C . LEU A 53 ? 0.3394 0.3324 0.3842 0.0080 -0.0579 -0.0217 69 LEU A C 421 O O . LEU A 53 ? 0.3289 0.3252 0.3782 0.0063 -0.0552 -0.0243 69 LEU A O 422 C CB . LEU A 53 ? 0.3532 0.3480 0.4010 0.0108 -0.0591 -0.0269 69 LEU A CB 423 C CG . LEU A 53 ? 0.3575 0.3576 0.4077 0.0089 -0.0535 -0.0298 69 LEU A CG 424 C CD1 . LEU A 53 ? 0.3640 0.3661 0.4241 0.0083 -0.0532 -0.0354 69 LEU A CD1 425 C CD2 . LEU A 53 ? 0.3653 0.3675 0.4136 0.0095 -0.0513 -0.0309 69 LEU A CD2 426 N N . ALA A 54 ? 0.3363 0.3273 0.3727 0.0077 -0.0576 -0.0161 70 ALA A N 427 C CA . ALA A 54 ? 0.3490 0.3413 0.3816 0.0055 -0.0544 -0.0129 70 ALA A CA 428 C C . ALA A 54 ? 0.3589 0.3500 0.3970 0.0045 -0.0557 -0.0136 70 ALA A C 429 O O . ALA A 54 ? 0.3548 0.3491 0.3948 0.0027 -0.0527 -0.0147 70 ALA A O 430 C CB . ALA A 54 ? 0.3475 0.3374 0.3708 0.0056 -0.0543 -0.0070 70 ALA A CB 431 N N . LYS A 55 ? 0.3703 0.3564 0.4110 0.0059 -0.0604 -0.0133 71 LYS A N 432 C CA . LYS A 55 ? 0.3857 0.3699 0.4324 0.0052 -0.0623 -0.0143 71 LYS A CA 433 C C . LYS A 55 ? 0.3802 0.3687 0.4360 0.0045 -0.0609 -0.0204 71 LYS A C 434 O O . LYS A 55 ? 0.3799 0.3700 0.4392 0.0029 -0.0595 -0.0214 71 LYS A O 435 C CB . LYS A 55 ? 0.4104 0.3882 0.4584 0.0072 -0.0679 -0.0131 71 LYS A CB 436 C CG . LYS A 55 ? 0.4520 0.4267 0.5047 0.0064 -0.0698 -0.0126 71 LYS A CG 437 C CD . LYS A 55 ? 0.4837 0.4512 0.5361 0.0086 -0.0754 -0.0104 71 LYS A CD 438 C CE . LYS A 55 ? 0.5139 0.4774 0.5675 0.0072 -0.0762 -0.0074 71 LYS A CE 439 N NZ . LYS A 55 ? 0.5587 0.5152 0.6146 0.0094 -0.0819 -0.0065 71 LYS A NZ 440 N N . PHE A 56 ? 0.3735 0.3640 0.4331 0.0058 -0.0612 -0.0247 72 PHE A N 441 C CA . PHE A 56 ? 0.3689 0.3636 0.4366 0.0051 -0.0594 -0.0308 72 PHE A CA 442 C C . PHE A 56 ? 0.3735 0.3735 0.4388 0.0029 -0.0538 -0.0310 72 PHE A C 443 O O . PHE A 56 ? 0.3680 0.3708 0.4384 0.0017 -0.0522 -0.0342 72 PHE A O 444 C CB . PHE A 56 ? 0.3595 0.3552 0.4317 0.0068 -0.0606 -0.0352 72 PHE A CB 445 C CG . PHE A 56 ? 0.3563 0.3564 0.4371 0.0060 -0.0584 -0.0416 72 PHE A CG 446 C CD1 . PHE A 56 ? 0.3601 0.3594 0.4497 0.0063 -0.0610 -0.0455 72 PHE A CD1 447 C CD2 . PHE A 56 ? 0.3479 0.3527 0.4277 0.0050 -0.0535 -0.0436 72 PHE A CD2 448 C CE1 . PHE A 56 ? 0.3549 0.3585 0.4523 0.0055 -0.0587 -0.0515 72 PHE A CE1 449 C CE2 . PHE A 56 ? 0.3453 0.3540 0.4325 0.0042 -0.0510 -0.0494 72 PHE A CE2 450 C CZ . PHE A 56 ? 0.3454 0.3537 0.4414 0.0044 -0.0536 -0.0534 72 PHE A CZ 451 N N . MET A 57 ? 0.3795 0.3808 0.4370 0.0026 -0.0510 -0.0279 73 MET A N 452 C CA . MET A 57 ? 0.4010 0.4069 0.4551 0.0009 -0.0459 -0.0276 73 MET A CA 453 C C . MET A 57 ? 0.3962 0.4024 0.4496 -0.0006 -0.0452 -0.0256 73 MET A C 454 O O . MET A 57 ? 0.3753 0.3855 0.4303 -0.0019 -0.0422 -0.0278 73 MET A O 455 C CB . MET A 57 ? 0.4173 0.4238 0.4629 0.0011 -0.0437 -0.0239 73 MET A CB 456 C CG . MET A 57 ? 0.4560 0.4629 0.5020 0.0025 -0.0436 -0.0259 73 MET A CG 457 S SD . MET A 57 ? 0.5033 0.5142 0.5572 0.0021 -0.0409 -0.0327 73 MET A SD 458 C CE . MET A 57 ? 0.5346 0.5467 0.5845 0.0028 -0.0385 -0.0325 73 MET A CE 459 N N . LYS A 58 ? 0.3995 0.4015 0.4505 -0.0005 -0.0480 -0.0216 74 LYS A N 460 C CA . LYS A 58 ? 0.4205 0.4223 0.4721 -0.0020 -0.0477 -0.0199 74 LYS A CA 461 C C . LYS A 58 ? 0.4253 0.4287 0.4857 -0.0026 -0.0483 -0.0248 74 LYS A C 462 O O . LYS A 58 ? 0.4357 0.4425 0.4973 -0.0041 -0.0460 -0.0259 74 LYS A O 463 C CB . LYS A 58 ? 0.4309 0.4270 0.4798 -0.0017 -0.0509 -0.0151 74 LYS A CB 464 C CG . LYS A 58 ? 0.4443 0.4397 0.4841 -0.0023 -0.0491 -0.0097 74 LYS A CG 465 C CD . LYS A 58 ? 0.4503 0.4408 0.4885 -0.0028 -0.0512 -0.0053 74 LYS A CD 466 C CE . LYS A 58 ? 0.4574 0.4465 0.4865 -0.0030 -0.0499 0.0001 74 LYS A CE 467 N NZ . LYS A 58 ? 0.4780 0.4657 0.5023 -0.0010 -0.0510 0.0009 74 LYS A NZ 468 N N . GLU A 59 ? 0.4206 0.4217 0.4874 -0.0013 -0.0516 -0.0279 75 GLU A N 469 C CA . GLU A 59 ? 0.4261 0.4288 0.5021 -0.0016 -0.0524 -0.0332 75 GLU A CA 470 C C . GLU A 59 ? 0.4222 0.4311 0.5001 -0.0024 -0.0482 -0.0378 75 GLU A C 471 O O . GLU A 59 ? 0.4158 0.4276 0.4980 -0.0035 -0.0469 -0.0408 75 GLU A O 472 C CB . GLU A 59 ? 0.4274 0.4265 0.5099 0.0001 -0.0570 -0.0357 75 GLU A CB 473 C CG . GLU A 59 ? 0.4456 0.4382 0.5276 0.0008 -0.0613 -0.0318 75 GLU A CG 474 C CD . GLU A 59 ? 0.4582 0.4465 0.5433 0.0032 -0.0662 -0.0328 75 GLU A CD 475 O OE1 . GLU A 59 ? 0.4668 0.4573 0.5581 0.0042 -0.0667 -0.0380 75 GLU A OE1 476 O OE2 . GLU A 59 ? 0.4568 0.4394 0.5382 0.0043 -0.0695 -0.0283 75 GLU A OE2 477 N N . VAL A 60 ? 0.4204 0.4311 0.4948 -0.0019 -0.0459 -0.0381 76 VAL A N 478 C CA . VAL A 60 ? 0.4235 0.4395 0.4984 -0.0027 -0.0415 -0.0418 76 VAL A CA 479 C C . VAL A 60 ? 0.4346 0.4539 0.5045 -0.0042 -0.0380 -0.0401 76 VAL A C 480 O O . VAL A 60 ? 0.4265 0.4494 0.4997 -0.0051 -0.0360 -0.0437 76 VAL A O 481 C CB . VAL A 60 ? 0.4233 0.4401 0.4952 -0.0019 -0.0397 -0.0420 76 VAL A CB 482 C CG1 . VAL A 60 ? 0.4270 0.4486 0.4977 -0.0029 -0.0345 -0.0446 76 VAL A CG1 483 C CG2 . VAL A 60 ? 0.4117 0.4263 0.4902 -0.0003 -0.0429 -0.0453 76 VAL A CG2 484 N N . ALA A 61 ? 0.4299 0.4481 0.4922 -0.0044 -0.0374 -0.0348 77 ALA A N 485 C CA . ALA A 61 ? 0.4444 0.4657 0.5021 -0.0057 -0.0345 -0.0331 77 ALA A CA 486 C C . ALA A 61 ? 0.4579 0.4799 0.5207 -0.0067 -0.0357 -0.0348 77 ALA A C 487 O O . ALA A 61 ? 0.4727 0.4986 0.5352 -0.0075 -0.0332 -0.0367 77 ALA A O 488 C CB . ALA A 61 ? 0.4329 0.4525 0.4827 -0.0057 -0.0342 -0.0273 77 ALA A CB 489 N N . SER A 62 ? 0.4731 0.4910 0.5404 -0.0064 -0.0396 -0.0342 78 SER A N 490 C CA . SER A 62 ? 0.4885 0.5064 0.5619 -0.0073 -0.0411 -0.0361 78 SER A CA 491 C C . SER A 62 ? 0.4895 0.5111 0.5698 -0.0074 -0.0402 -0.0425 78 SER A C 492 O O . SER A 62 ? 0.4844 0.5093 0.5666 -0.0084 -0.0388 -0.0447 78 SER A O 493 C CB . SER A 62 ? 0.5044 0.5164 0.5813 -0.0067 -0.0456 -0.0341 78 SER A CB 494 O OG . SER A 62 ? 0.5194 0.5311 0.6034 -0.0075 -0.0472 -0.0365 78 SER A OG 495 N N . ASP A 63 ? 0.4818 0.5030 0.5659 -0.0064 -0.0408 -0.0457 79 ASP A N 496 C CA . ASP A 63 ? 0.4882 0.5128 0.5792 -0.0066 -0.0397 -0.0521 79 ASP A CA 497 C C . ASP A 63 ? 0.4822 0.5124 0.5696 -0.0073 -0.0349 -0.0543 79 ASP A C 498 O O . ASP A 63 ? 0.4771 0.5105 0.5694 -0.0078 -0.0336 -0.0593 79 ASP A O 499 C CB . ASP A 63 ? 0.5084 0.5313 0.6046 -0.0053 -0.0415 -0.0551 79 ASP A CB 500 C CG . ASP A 63 ? 0.5295 0.5476 0.6321 -0.0044 -0.0467 -0.0551 79 ASP A CG 501 O OD1 . ASP A 63 ? 0.5530 0.5692 0.6567 -0.0050 -0.0486 -0.0533 79 ASP A OD1 502 O OD2 . ASP A 63 ? 0.5485 0.5646 0.6550 -0.0030 -0.0490 -0.0570 79 ASP A OD2 503 N N . THR A 64 ? 0.4745 0.5055 0.5533 -0.0074 -0.0322 -0.0506 80 THR A N 504 C CA . THR A 64 ? 0.4760 0.5118 0.5504 -0.0079 -0.0276 -0.0520 80 THR A CA 505 C C . THR A 64 ? 0.4797 0.5185 0.5544 -0.0088 -0.0271 -0.0531 80 THR A C 506 O O . THR A 64 ? 0.4857 0.5286 0.5596 -0.0092 -0.0241 -0.0564 80 THR A O 507 C CB . THR A 64 ? 0.4793 0.5151 0.5444 -0.0077 -0.0251 -0.0476 80 THR A CB 508 O OG1 . THR A 64 ? 0.4665 0.5007 0.5269 -0.0079 -0.0264 -0.0426 80 THR A OG1 509 C CG2 . THR A 64 ? 0.4641 0.4975 0.5290 -0.0068 -0.0253 -0.0471 80 THR A CG2 510 N N . THR A 65 ? 0.4794 0.5161 0.5552 -0.0092 -0.0298 -0.0507 81 THR A N 511 C CA . THR A 65 ? 0.4899 0.5295 0.5667 -0.0101 -0.0296 -0.0517 81 THR A CA 512 C C . THR A 65 ? 0.4869 0.5284 0.5723 -0.0103 -0.0305 -0.0578 81 THR A C 513 O O . THR A 65 ? 0.5076 0.5524 0.5943 -0.0109 -0.0300 -0.0600 81 THR A O 514 C CB . THR A 65 ? 0.4922 0.5289 0.5683 -0.0106 -0.0320 -0.0473 81 THR A CB 515 O OG1 . THR A 65 ? 0.4983 0.5305 0.5810 -0.0105 -0.0358 -0.0474 81 THR A OG1 516 C CG2 . THR A 65 ? 0.4859 0.5208 0.5535 -0.0104 -0.0310 -0.0416 81 THR A CG2 517 N N . LYS A 66 ? 0.4767 0.5165 0.5682 -0.0098 -0.0319 -0.0607 82 LYS A N 518 C CA . LYS A 66 ? 0.4680 0.5099 0.5681 -0.0100 -0.0326 -0.0669 82 LYS A CA 519 C C . LYS A 66 ? 0.4436 0.4904 0.5420 -0.0101 -0.0284 -0.0711 82 LYS A C 520 O O . LYS A 66 ? 0.4413 0.4909 0.5456 -0.0103 -0.0280 -0.0766 82 LYS A O 521 C CB . LYS A 66 ? 0.5058 0.5438 0.6136 -0.0092 -0.0360 -0.0685 82 LYS A CB 522 C CG . LYS A 66 ? 0.5412 0.5736 0.6502 -0.0090 -0.0402 -0.0641 82 LYS A CG 523 C CD . LYS A 66 ? 0.5868 0.6148 0.7005 -0.0078 -0.0434 -0.0644 82 LYS A CD 524 C CE . LYS A 66 ? 0.6137 0.6397 0.7377 -0.0076 -0.0473 -0.0679 82 LYS A CE 525 N NZ . LYS A 66 ? 0.6447 0.6662 0.7729 -0.0061 -0.0509 -0.0681 82 LYS A NZ 526 N N . PHE A 67 ? 0.3980 0.4455 0.4882 -0.0098 -0.0251 -0.0685 83 PHE A N 527 C CA . PHE A 67 ? 0.3769 0.4285 0.4638 -0.0099 -0.0207 -0.0715 83 PHE A CA 528 C C . PHE A 67 ? 0.3715 0.4259 0.4498 -0.0101 -0.0182 -0.0692 83 PHE A C 529 O O . PHE A 67 ? 0.3672 0.4199 0.4395 -0.0100 -0.0186 -0.0640 83 PHE A O 530 C CB . PHE A 67 ? 0.3644 0.4146 0.4490 -0.0095 -0.0186 -0.0707 83 PHE A CB 531 C CG . PHE A 67 ? 0.3589 0.4074 0.4524 -0.0092 -0.0205 -0.0744 83 PHE A CG 532 C CD1 . PHE A 67 ? 0.3598 0.4112 0.4589 -0.0095 -0.0184 -0.0805 83 PHE A CD1 533 C CD2 . PHE A 67 ? 0.3582 0.4022 0.4546 -0.0085 -0.0243 -0.0719 83 PHE A CD2 534 C CE1 . PHE A 67 ? 0.3638 0.4139 0.4718 -0.0092 -0.0203 -0.0843 83 PHE A CE1 535 C CE2 . PHE A 67 ? 0.3577 0.4002 0.4625 -0.0080 -0.0264 -0.0755 83 PHE A CE2 536 C CZ . PHE A 67 ? 0.3585 0.4041 0.4695 -0.0083 -0.0244 -0.0818 83 PHE A CZ 537 N N . GLN A 68 ? 0.3597 0.4184 0.4374 -0.0103 -0.0157 -0.0732 84 GLN A N 538 C CA . GLN A 68 ? 0.3676 0.4294 0.4371 -0.0102 -0.0134 -0.0716 84 GLN A CA 539 C C . GLN A 68 ? 0.3384 0.4003 0.3993 -0.0098 -0.0094 -0.0693 84 GLN A C 540 O O . GLN A 68 ? 0.3397 0.4047 0.3958 -0.0096 -0.0061 -0.0711 84 GLN A O 541 C CB . GLN A 68 ? 0.3959 0.4623 0.4676 -0.0103 -0.0124 -0.0771 84 GLN A CB 542 C CG . GLN A 68 ? 0.4379 0.5046 0.5191 -0.0108 -0.0160 -0.0806 84 GLN A CG 543 C CD . GLN A 68 ? 0.4656 0.5314 0.5463 -0.0109 -0.0189 -0.0772 84 GLN A CD 544 O OE1 . GLN A 68 ? 0.4939 0.5620 0.5679 -0.0107 -0.0178 -0.0753 84 GLN A OE1 545 N NE2 . GLN A 68 ? 0.4822 0.5446 0.5701 -0.0113 -0.0226 -0.0764 84 GLN A NE2 546 N N . TRP A 69 ? 0.3160 0.3744 0.3746 -0.0095 -0.0097 -0.0652 85 TRP A N 547 C CA . TRP A 69 ? 0.2996 0.3577 0.3521 -0.0092 -0.0058 -0.0638 85 TRP A CA 548 C C . TRP A 69 ? 0.2919 0.3520 0.3343 -0.0088 -0.0028 -0.0613 85 TRP A C 549 O O . TRP A 69 ? 0.2858 0.3468 0.3238 -0.0087 0.0011 -0.0621 85 TRP A O 550 C CB . TRP A 69 ? 0.2977 0.3517 0.3507 -0.0090 -0.0069 -0.0604 85 TRP A CB 551 C CG . TRP A 69 ? 0.2980 0.3497 0.3469 -0.0087 -0.0093 -0.0549 85 TRP A CG 552 C CD1 . TRP A 69 ? 0.2956 0.3447 0.3487 -0.0088 -0.0135 -0.0532 85 TRP A CD1 553 C CD2 . TRP A 69 ? 0.2986 0.3502 0.3386 -0.0083 -0.0076 -0.0503 85 TRP A CD2 554 N NE1 . TRP A 69 ? 0.2970 0.3447 0.3442 -0.0086 -0.0141 -0.0480 85 TRP A NE1 555 C CE2 . TRP A 69 ? 0.2974 0.3467 0.3368 -0.0082 -0.0107 -0.0462 85 TRP A CE2 556 C CE3 . TRP A 69 ? 0.2989 0.3519 0.3313 -0.0079 -0.0036 -0.0492 85 TRP A CE3 557 C CZ2 . TRP A 69 ? 0.2972 0.3460 0.3292 -0.0078 -0.0100 -0.0415 85 TRP A CZ2 558 C CZ3 . TRP A 69 ? 0.2988 0.3511 0.3238 -0.0074 -0.0032 -0.0443 85 TRP A CZ3 559 C CH2 . TRP A 69 ? 0.2991 0.3495 0.3241 -0.0073 -0.0064 -0.0407 85 TRP A CH2 560 N N . ARG A 70 ? 0.2799 0.3407 0.3189 -0.0085 -0.0046 -0.0586 86 ARG A N 561 C CA . ARG A 70 ? 0.2805 0.3434 0.3103 -0.0078 -0.0023 -0.0565 86 ARG A CA 562 C C . ARG A 70 ? 0.2889 0.3557 0.3168 -0.0076 0.0000 -0.0607 86 ARG A C 563 O O . ARG A 70 ? 0.2997 0.3679 0.3193 -0.0068 0.0026 -0.0595 86 ARG A O 564 C CB . ARG A 70 ? 0.2782 0.3414 0.3060 -0.0076 -0.0050 -0.0532 86 ARG A CB 565 C CG . ARG A 70 ? 0.2700 0.3297 0.2967 -0.0076 -0.0065 -0.0482 86 ARG A CG 566 C CD . ARG A 70 ? 0.2714 0.3317 0.2959 -0.0076 -0.0086 -0.0450 86 ARG A CD 567 N NE . ARG A 70 ? 0.2690 0.3258 0.2924 -0.0077 -0.0099 -0.0404 86 ARG A NE 568 C CZ . ARG A 70 ? 0.2762 0.3300 0.3053 -0.0083 -0.0127 -0.0396 86 ARG A CZ 569 N NH1 . ARG A 70 ? 0.2782 0.3320 0.3150 -0.0089 -0.0146 -0.0432 86 ARG A NH1 570 N NH2 . ARG A 70 ? 0.2697 0.3205 0.2967 -0.0083 -0.0136 -0.0353 86 ARG A NH2 571 N N . SER A 71 ? 0.2938 0.3622 0.3292 -0.0082 -0.0007 -0.0658 87 SER A N 572 C CA . SER A 71 ? 0.3036 0.3758 0.3379 -0.0080 0.0014 -0.0705 87 SER A CA 573 C C . SER A 71 ? 0.3159 0.3880 0.3492 -0.0083 0.0057 -0.0729 87 SER A C 574 O O . SER A 71 ? 0.3210 0.3961 0.3524 -0.0082 0.0083 -0.0767 87 SER A O 575 C CB . SER A 71 ? 0.3039 0.3781 0.3472 -0.0085 -0.0014 -0.0753 87 SER A CB 576 O OG . SER A 71 ? 0.3282 0.4030 0.3724 -0.0084 -0.0049 -0.0736 87 SER A OG 577 N N . TYR A 72 ? 0.3199 0.3887 0.3548 -0.0087 0.0067 -0.0711 88 TYR A N 578 C CA . TYR A 72 ? 0.3248 0.3934 0.3614 -0.0092 0.0105 -0.0741 88 TYR A CA 579 C C . TYR A 72 ? 0.3322 0.4013 0.3589 -0.0089 0.0157 -0.0728 88 TYR A C 580 O O . TYR A 72 ? 0.3283 0.3966 0.3464 -0.0080 0.0162 -0.0683 88 TYR A O 581 C CB . TYR A 72 ? 0.3269 0.3919 0.3691 -0.0097 0.0095 -0.0728 88 TYR A CB 582 C CG . TYR A 72 ? 0.3268 0.3909 0.3796 -0.0100 0.0049 -0.0751 88 TYR A CG 583 C CD1 . TYR A 72 ? 0.3349 0.4013 0.3931 -0.0102 0.0024 -0.0787 88 TYR A CD1 584 C CD2 . TYR A 72 ? 0.3293 0.3900 0.3869 -0.0101 0.0031 -0.0737 88 TYR A CD2 585 C CE1 . TYR A 72 ? 0.3371 0.4021 0.4051 -0.0104 -0.0017 -0.0806 88 TYR A CE1 586 C CE2 . TYR A 72 ? 0.3301 0.3894 0.3969 -0.0102 -0.0011 -0.0756 88 TYR A CE2 587 C CZ . TYR A 72 ? 0.3393 0.4007 0.4114 -0.0104 -0.0035 -0.0789 88 TYR A CZ 588 O OH . TYR A 72 ? 0.3504 0.4099 0.4316 -0.0104 -0.0078 -0.0805 88 TYR A OH 589 N N . GLN A 73 ? 0.3492 0.4194 0.3772 -0.0095 0.0196 -0.0768 89 GLN A N 590 C CA . GLN A 73 ? 0.3695 0.4395 0.3887 -0.0094 0.0251 -0.0757 89 GLN A CA 591 C C . GLN A 73 ? 0.3649 0.4312 0.3823 -0.0096 0.0272 -0.0719 89 GLN A C 592 O O . GLN A 73 ? 0.3705 0.4354 0.3787 -0.0090 0.0300 -0.0681 89 GLN A O 593 C CB . GLN A 73 ? 0.3840 0.4565 0.4058 -0.0102 0.0290 -0.0815 89 GLN A CB 594 C CG . GLN A 73 ? 0.4117 0.4882 0.4325 -0.0097 0.0282 -0.0853 89 GLN A CG 595 C CD . GLN A 73 ? 0.4285 0.5060 0.4372 -0.0083 0.0293 -0.0822 89 GLN A CD 596 O OE1 . GLN A 73 ? 0.4460 0.5220 0.4457 -0.0080 0.0336 -0.0797 89 GLN A OE1 597 N NE2 . GLN A 73 ? 0.4201 0.4999 0.4284 -0.0074 0.0253 -0.0825 89 GLN A NE2 598 N N . SER A 74 ? 0.3563 0.4208 0.3826 -0.0104 0.0257 -0.0731 90 SER A N 599 C CA . SER A 74 ? 0.3570 0.4183 0.3833 -0.0107 0.0277 -0.0707 90 SER A CA 600 C C . SER A 74 ? 0.3599 0.4185 0.3822 -0.0098 0.0249 -0.0648 90 SER A C 601 O O . SER A 74 ? 0.3451 0.4029 0.3721 -0.0096 0.0201 -0.0638 90 SER A O 602 C CB . SER A 74 ? 0.3503 0.4111 0.3881 -0.0116 0.0270 -0.0748 90 SER A CB 603 O OG . SER A 74 ? 0.3439 0.4015 0.3827 -0.0117 0.0274 -0.0723 90 SER A OG 604 N N . GLU A 75 ? 0.3769 0.4340 0.3904 -0.0094 0.0282 -0.0609 91 GLU A N 605 C CA . GLU A 75 ? 0.3883 0.4429 0.3975 -0.0086 0.0263 -0.0554 91 GLU A CA 606 C C . GLU A 75 ? 0.3631 0.4153 0.3797 -0.0089 0.0241 -0.0553 91 GLU A C 607 O O . GLU A 75 ? 0.3617 0.4126 0.3784 -0.0084 0.0204 -0.0521 91 GLU A O 608 C CB . GLU A 75 ? 0.4356 0.4886 0.4351 -0.0081 0.0307 -0.0519 91 GLU A CB 609 C CG . GLU A 75 ? 0.5028 0.5577 0.4932 -0.0072 0.0324 -0.0510 91 GLU A CG 610 C CD . GLU A 75 ? 0.5468 0.6031 0.5340 -0.0060 0.0279 -0.0486 91 GLU A CD 611 O OE1 . GLU A 75 ? 0.5597 0.6144 0.5476 -0.0057 0.0249 -0.0452 91 GLU A OE1 612 O OE2 . GLU A 75 ? 0.5980 0.6571 0.5823 -0.0055 0.0275 -0.0503 91 GLU A OE2 613 N N . ASP A 76 ? 0.3522 0.4041 0.3751 -0.0099 0.0265 -0.0590 92 ASP A N 614 C CA . ASP A 76 ? 0.3379 0.3877 0.3684 -0.0101 0.0244 -0.0596 92 ASP A CA 615 C C . ASP A 76 ? 0.3259 0.3759 0.3638 -0.0098 0.0186 -0.0609 92 ASP A C 616 O O . ASP A 76 ? 0.3131 0.3610 0.3528 -0.0093 0.0151 -0.0585 92 ASP A O 617 C CB . ASP A 76 ? 0.3540 0.4040 0.3905 -0.0112 0.0284 -0.0640 92 ASP A CB 618 C CG . ASP A 76 ? 0.3623 0.4103 0.4067 -0.0112 0.0262 -0.0650 92 ASP A CG 619 O OD1 . ASP A 76 ? 0.3733 0.4191 0.4152 -0.0104 0.0242 -0.0610 92 ASP A OD1 620 O OD2 . ASP A 76 ? 0.3823 0.4312 0.4357 -0.0119 0.0264 -0.0699 92 ASP A OD2 621 N N . LEU A 77 ? 0.3112 0.3637 0.3535 -0.0102 0.0175 -0.0648 93 LEU A N 622 C CA . LEU A 77 ? 0.3003 0.3527 0.3493 -0.0099 0.0120 -0.0660 93 LEU A CA 623 C C . LEU A 77 ? 0.2907 0.3422 0.3344 -0.0092 0.0085 -0.0610 93 LEU A C 624 O O . LEU A 77 ? 0.2847 0.3341 0.3314 -0.0087 0.0044 -0.0591 93 LEU A O 625 C CB . LEU A 77 ? 0.3075 0.3630 0.3618 -0.0105 0.0118 -0.0712 93 LEU A CB 626 C CG . LEU A 77 ? 0.3143 0.3711 0.3760 -0.0113 0.0145 -0.0771 93 LEU A CG 627 C CD1 . LEU A 77 ? 0.3189 0.3786 0.3859 -0.0116 0.0133 -0.0820 93 LEU A CD1 628 C CD2 . LEU A 77 ? 0.3162 0.3707 0.3862 -0.0112 0.0123 -0.0784 93 LEU A CD2 629 N N . LYS A 78 ? 0.2868 0.3399 0.3223 -0.0089 0.0103 -0.0589 94 LYS A N 630 C CA . LYS A 78 ? 0.2887 0.3414 0.3191 -0.0083 0.0076 -0.0543 94 LYS A CA 631 C C . LYS A 78 ? 0.2864 0.3360 0.3139 -0.0077 0.0066 -0.0497 94 LYS A C 632 O O . LYS A 78 ? 0.2819 0.3302 0.3100 -0.0074 0.0029 -0.0470 94 LYS A O 633 C CB . LYS A 78 ? 0.2949 0.3500 0.3168 -0.0079 0.0099 -0.0532 94 LYS A CB 634 C CG . LYS A 78 ? 0.2941 0.3525 0.3183 -0.0082 0.0101 -0.0576 94 LYS A CG 635 C CD . LYS A 78 ? 0.3047 0.3655 0.3205 -0.0074 0.0112 -0.0561 94 LYS A CD 636 C CE . LYS A 78 ? 0.3139 0.3749 0.3221 -0.0071 0.0164 -0.0558 94 LYS A CE 637 N NZ . LYS A 78 ? 0.3126 0.3755 0.3119 -0.0060 0.0169 -0.0539 94 LYS A NZ 638 N N . ARG A 79 ? 0.2850 0.3334 0.3097 -0.0077 0.0101 -0.0490 95 ARG A N 639 C CA . ARG A 79 ? 0.2839 0.3296 0.3060 -0.0072 0.0096 -0.0450 95 ARG A CA 640 C C . ARG A 79 ? 0.2816 0.3252 0.3109 -0.0071 0.0056 -0.0455 95 ARG A C 641 O O . ARG A 79 ? 0.2763 0.3181 0.3037 -0.0065 0.0028 -0.0419 95 ARG A O 642 C CB . ARG A 79 ? 0.2826 0.3275 0.3012 -0.0073 0.0144 -0.0446 95 ARG A CB 643 C CG . ARG A 79 ? 0.2828 0.3252 0.2977 -0.0066 0.0142 -0.0404 95 ARG A CG 644 C CD . ARG A 79 ? 0.2856 0.3270 0.2968 -0.0068 0.0192 -0.0399 95 ARG A CD 645 N NE . ARG A 79 ? 0.2933 0.3324 0.3021 -0.0061 0.0187 -0.0363 95 ARG A NE 646 C CZ . ARG A 79 ? 0.2978 0.3364 0.2995 -0.0053 0.0181 -0.0319 95 ARG A CZ 647 N NH1 . ARG A 79 ? 0.2913 0.3316 0.2876 -0.0049 0.0178 -0.0303 95 ARG A NH1 648 N NH2 . ARG A 79 ? 0.2913 0.3280 0.2917 -0.0047 0.0177 -0.0293 95 ARG A NH2 649 N N . GLN A 80 ? 0.2864 0.3302 0.3238 -0.0076 0.0052 -0.0502 96 GLN A N 650 C CA . GLN A 80 ? 0.2874 0.3292 0.3321 -0.0072 0.0010 -0.0513 96 GLN A CA 651 C C . GLN A 80 ? 0.2840 0.3252 0.3300 -0.0070 -0.0037 -0.0497 96 GLN A C 652 O O . GLN A 80 ? 0.2825 0.3211 0.3287 -0.0063 -0.0071 -0.0470 96 GLN A O 653 C CB . GLN A 80 ? 0.2894 0.3319 0.3431 -0.0077 0.0017 -0.0570 96 GLN A CB 654 C CG . GLN A 80 ? 0.2972 0.3398 0.3511 -0.0081 0.0063 -0.0587 96 GLN A CG 655 C CD . GLN A 80 ? 0.3038 0.3472 0.3677 -0.0086 0.0067 -0.0647 96 GLN A CD 656 O OE1 . GLN A 80 ? 0.2993 0.3414 0.3703 -0.0080 0.0025 -0.0663 96 GLN A OE1 657 N NE2 . GLN A 80 ? 0.3101 0.3556 0.3747 -0.0096 0.0117 -0.0679 96 GLN A NE2 658 N N . PHE A 81 ? 0.2865 0.3300 0.3332 -0.0074 -0.0038 -0.0514 97 PHE A N 659 C CA . PHE A 81 ? 0.2918 0.3345 0.3400 -0.0074 -0.0080 -0.0500 97 PHE A CA 660 C C . PHE A 81 ? 0.3012 0.3428 0.3422 -0.0070 -0.0089 -0.0443 97 PHE A C 661 O O . PHE A 81 ? 0.2971 0.3363 0.3392 -0.0067 -0.0125 -0.0419 97 PHE A O 662 C CB . PHE A 81 ? 0.2925 0.3382 0.3429 -0.0080 -0.0077 -0.0532 97 PHE A CB 663 C CG . PHE A 81 ? 0.2929 0.3390 0.3529 -0.0082 -0.0094 -0.0583 97 PHE A CG 664 C CD1 . PHE A 81 ? 0.2978 0.3416 0.3638 -0.0080 -0.0141 -0.0584 97 PHE A CD1 665 C CD2 . PHE A 81 ? 0.2933 0.3419 0.3564 -0.0087 -0.0061 -0.0632 97 PHE A CD2 666 C CE1 . PHE A 81 ? 0.2992 0.3432 0.3745 -0.0081 -0.0159 -0.0634 97 PHE A CE1 667 C CE2 . PHE A 81 ? 0.2987 0.3478 0.3712 -0.0089 -0.0077 -0.0684 97 PHE A CE2 668 C CZ . PHE A 81 ? 0.2991 0.3459 0.3778 -0.0086 -0.0127 -0.0685 97 PHE A CZ 669 N N . LYS A 82 ? 0.3115 0.3546 0.3450 -0.0069 -0.0056 -0.0422 98 LYS A N 670 C CA . LYS A 82 ? 0.3425 0.3848 0.3692 -0.0065 -0.0061 -0.0371 98 LYS A CA 671 C C . LYS A 82 ? 0.3390 0.3779 0.3655 -0.0059 -0.0079 -0.0343 98 LYS A C 672 O O . LYS A 82 ? 0.3469 0.3844 0.3720 -0.0058 -0.0106 -0.0311 98 LYS A O 673 C CB . LYS A 82 ? 0.3582 0.4024 0.3771 -0.0063 -0.0023 -0.0356 98 LYS A CB 674 C CG . LYS A 82 ? 0.3995 0.4441 0.4125 -0.0059 -0.0032 -0.0313 98 LYS A CG 675 C CD . LYS A 82 ? 0.4302 0.4768 0.4358 -0.0054 0.0000 -0.0302 98 LYS A CD 676 C CE . LYS A 82 ? 0.4646 0.5111 0.4646 -0.0049 -0.0008 -0.0258 98 LYS A CE 677 N NZ . LYS A 82 ? 0.5187 0.5668 0.5114 -0.0042 0.0021 -0.0245 98 LYS A NZ 678 N N . ALA A 83 ? 0.3492 0.3872 0.3774 -0.0057 -0.0064 -0.0358 99 ALA A N 679 C CA . ALA A 83 ? 0.3634 0.3985 0.3921 -0.0050 -0.0084 -0.0339 99 ALA A CA 680 C C . ALA A 83 ? 0.3763 0.4090 0.4100 -0.0047 -0.0132 -0.0339 99 ALA A C 681 O O . ALA A 83 ? 0.3777 0.4079 0.4090 -0.0041 -0.0156 -0.0305 99 ALA A O 682 C CB . ALA A 83 ? 0.3614 0.3961 0.3926 -0.0048 -0.0060 -0.0365 99 ALA A CB 683 N N . LEU A 84 ? 0.3895 0.4227 0.4300 -0.0051 -0.0147 -0.0377 100 LEU A N 684 C CA . LEU A 84 ? 0.4135 0.4441 0.4592 -0.0047 -0.0194 -0.0378 100 LEU A CA 685 C C . LEU A 84 ? 0.4303 0.4599 0.4733 -0.0050 -0.0216 -0.0343 100 LEU A C 686 O O . LEU A 84 ? 0.4463 0.4727 0.4913 -0.0047 -0.0254 -0.0328 100 LEU A O 687 C CB . LEU A 84 ? 0.4172 0.4486 0.4715 -0.0050 -0.0203 -0.0432 100 LEU A CB 688 C CG . LEU A 84 ? 0.4227 0.4546 0.4819 -0.0047 -0.0187 -0.0474 100 LEU A CG 689 C CD1 . LEU A 84 ? 0.4361 0.4697 0.5033 -0.0052 -0.0189 -0.0528 100 LEU A CD1 690 C CD2 . LEU A 84 ? 0.4290 0.4577 0.4901 -0.0035 -0.0218 -0.0466 100 LEU A CD2 691 N N . THR A 85 ? 0.4417 0.4739 0.4803 -0.0057 -0.0194 -0.0330 101 THR A N 692 C CA . THR A 85 ? 0.4645 0.4962 0.5009 -0.0062 -0.0212 -0.0298 101 THR A CA 693 C C . THR A 85 ? 0.4636 0.4933 0.4936 -0.0058 -0.0216 -0.0247 101 THR A C 694 O O . THR A 85 ? 0.4836 0.5120 0.5122 -0.0061 -0.0233 -0.0217 101 THR A O 695 C CB . THR A 85 ? 0.4774 0.5129 0.5117 -0.0069 -0.0189 -0.0306 101 THR A CB 696 O OG1 . THR A 85 ? 0.4993 0.5368 0.5268 -0.0067 -0.0155 -0.0291 101 THR A OG1 697 C CG2 . THR A 85 ? 0.4527 0.4903 0.4930 -0.0074 -0.0186 -0.0358 101 THR A CG2 698 N N . LYS A 86 ? 0.4502 0.4797 0.4766 -0.0051 -0.0198 -0.0239 102 LYS A N 699 C CA . LYS A 86 ? 0.4598 0.4880 0.4798 -0.0046 -0.0197 -0.0194 102 LYS A CA 700 C C . LYS A 86 ? 0.4318 0.4560 0.4529 -0.0038 -0.0230 -0.0179 102 LYS A C 701 O O . LYS A 86 ? 0.4525 0.4757 0.4747 -0.0029 -0.0231 -0.0192 102 LYS A O 702 C CB . LYS A 86 ? 0.4799 0.5099 0.4954 -0.0042 -0.0160 -0.0192 102 LYS A CB 703 C CG . LYS A 86 ? 0.5218 0.5552 0.5334 -0.0047 -0.0131 -0.0190 102 LYS A CG 704 C CD . LYS A 86 ? 0.5612 0.5960 0.5696 -0.0043 -0.0093 -0.0197 102 LYS A CD 705 C CE . LYS A 86 ? 0.5749 0.6128 0.5793 -0.0045 -0.0068 -0.0197 102 LYS A CE 706 N NZ . LYS A 86 ? 0.5802 0.6188 0.5798 -0.0040 -0.0031 -0.0192 102 LYS A NZ 707 N N . LEU A 87 ? 0.4027 0.4247 0.4234 -0.0040 -0.0256 -0.0152 103 LEU A N 708 C CA . LEU A 87 ? 0.3666 0.3843 0.3882 -0.0032 -0.0292 -0.0137 103 LEU A CA 709 C C . LEU A 87 ? 0.3454 0.3615 0.3607 -0.0023 -0.0293 -0.0100 103 LEU A C 710 O O . LEU A 87 ? 0.3358 0.3488 0.3516 -0.0012 -0.0319 -0.0097 103 LEU A O 711 C CB . LEU A 87 ? 0.3677 0.3831 0.3912 -0.0039 -0.0318 -0.0120 103 LEU A CB 712 C CG . LEU A 87 ? 0.3806 0.3958 0.4119 -0.0043 -0.0336 -0.0156 103 LEU A CG 713 C CD1 . LEU A 87 ? 0.3851 0.3979 0.4175 -0.0052 -0.0356 -0.0133 103 LEU A CD1 714 C CD2 . LEU A 87 ? 0.3751 0.3879 0.4115 -0.0030 -0.0362 -0.0185 103 LEU A CD2 715 N N . GLY A 88 ? 0.3180 0.3362 0.3275 -0.0028 -0.0266 -0.0074 104 GLY A N 716 C CA . GLY A 88 ? 0.3050 0.3219 0.3082 -0.0021 -0.0266 -0.0038 104 GLY A CA 717 C C . GLY A 88 ? 0.2929 0.3058 0.2948 -0.0020 -0.0297 -0.0007 104 GLY A C 718 O O . GLY A 88 ? 0.2815 0.2937 0.2851 -0.0030 -0.0306 0.0002 104 GLY A O 719 N N . TYR A 89 ? 0.2882 0.2986 0.2874 -0.0007 -0.0314 0.0006 105 TYR A N 720 C CA . TYR A 89 ? 0.2992 0.3053 0.2959 -0.0003 -0.0344 0.0039 105 TYR A CA 721 C C . TYR A 89 ? 0.3005 0.3034 0.3027 -0.0004 -0.0377 0.0028 105 TYR A C 722 O O . TYR A 89 ? 0.3040 0.3036 0.3045 -0.0008 -0.0394 0.0059 105 TYR A O 723 C CB . TYR A 89 ? 0.2973 0.3012 0.2902 0.0014 -0.0360 0.0049 105 TYR A CB 724 C CG . TYR A 89 ? 0.2984 0.3046 0.2852 0.0016 -0.0333 0.0068 105 TYR A CG 725 C CD1 . TYR A 89 ? 0.2960 0.3051 0.2796 0.0002 -0.0301 0.0088 105 TYR A CD1 726 C CD2 . TYR A 89 ? 0.2987 0.3042 0.2831 0.0032 -0.0341 0.0064 105 TYR A CD2 727 C CE1 . TYR A 89 ? 0.2989 0.3099 0.2773 0.0004 -0.0277 0.0104 105 TYR A CE1 728 C CE2 . TYR A 89 ? 0.2978 0.3053 0.2770 0.0034 -0.0317 0.0080 105 TYR A CE2 729 C CZ . TYR A 89 ? 0.2939 0.3040 0.2700 0.0020 -0.0285 0.0100 105 TYR A CZ 730 O OH . TYR A 89 ? 0.2899 0.3020 0.2612 0.0024 -0.0263 0.0114 105 TYR A OH 731 N N . ALA A 90 ? 0.2967 0.3005 0.3055 0.0000 -0.0384 -0.0015 106 ALA A N 732 C CA . ALA A 90 ? 0.3019 0.3030 0.3169 0.0000 -0.0417 -0.0032 106 ALA A CA 733 C C . ALA A 90 ? 0.3075 0.3088 0.3245 -0.0017 -0.0411 -0.0023 106 ALA A C 734 O O . ALA A 90 ? 0.3135 0.3121 0.3353 -0.0017 -0.0438 -0.0031 106 ALA A O 735 C CB . ALA A 90 ? 0.2962 0.2989 0.3181 0.0007 -0.0421 -0.0086 106 ALA A CB 736 N N . ALA A 91 ? 0.3030 0.3076 0.3167 -0.0030 -0.0377 -0.0009 107 ALA A N 737 C CA . ALA A 91 ? 0.3070 0.3122 0.3223 -0.0047 -0.0371 0.0000 107 ALA A CA 738 C C . ALA A 91 ? 0.3230 0.3238 0.3353 -0.0052 -0.0387 0.0047 107 ALA A C 739 O O . ALA A 91 ? 0.3308 0.3306 0.3459 -0.0065 -0.0391 0.0054 107 ALA A O 740 C CB . ALA A 91 ? 0.2996 0.3099 0.3125 -0.0059 -0.0332 0.0000 107 ALA A CB 741 N N . LEU A 92 ? 0.3226 0.3207 0.3290 -0.0041 -0.0396 0.0078 108 LEU A N 742 C CA . LEU A 92 ? 0.3329 0.3266 0.3348 -0.0045 -0.0406 0.0127 108 LEU A CA 743 C C . LEU A 92 ? 0.3453 0.3334 0.3510 -0.0041 -0.0445 0.0131 108 LEU A C 744 O O . LEU A 92 ? 0.3391 0.3258 0.3491 -0.0027 -0.0472 0.0101 108 LEU A O 745 C CB . LEU A 92 ? 0.3308 0.3230 0.3251 -0.0032 -0.0407 0.0155 108 LEU A CB 746 C CG . LEU A 92 ? 0.3295 0.3258 0.3182 -0.0036 -0.0370 0.0169 108 LEU A CG 747 C CD1 . LEU A 92 ? 0.3320 0.3271 0.3152 -0.0018 -0.0378 0.0180 108 LEU A CD1 748 C CD2 . LEU A 92 ? 0.3294 0.3259 0.3151 -0.0055 -0.0349 0.0205 108 LEU A CD2 749 N N . PRO A 93 ? 0.3533 0.3380 0.3578 -0.0054 -0.0447 0.0168 109 PRO A N 750 C CA . PRO A 93 ? 0.3732 0.3516 0.3800 -0.0049 -0.0484 0.0181 109 PRO A CA 751 C C . PRO A 93 ? 0.3746 0.3490 0.3774 -0.0023 -0.0516 0.0190 109 PRO A C 752 O O . PRO A 93 ? 0.3657 0.3413 0.3621 -0.0015 -0.0505 0.0204 109 PRO A O 753 C CB . PRO A 93 ? 0.3809 0.3563 0.3837 -0.0066 -0.0470 0.0231 109 PRO A CB 754 C CG . PRO A 93 ? 0.3824 0.3639 0.3855 -0.0086 -0.0428 0.0225 109 PRO A CG 755 C CD . PRO A 93 ? 0.3619 0.3486 0.3633 -0.0075 -0.0413 0.0197 109 PRO A CD 756 N N . GLU A 94 ? 0.3823 0.3523 0.3894 -0.0010 -0.0557 0.0178 110 GLU A N 757 C CA . GLU A 94 ? 0.3953 0.3616 0.4002 0.0017 -0.0596 0.0177 110 GLU A CA 758 C C . GLU A 94 ? 0.4076 0.3711 0.4023 0.0026 -0.0596 0.0225 110 GLU A C 759 O O . GLU A 94 ? 0.4098 0.3746 0.4012 0.0044 -0.0602 0.0215 110 GLU A O 760 C CB . GLU A 94 ? 0.3943 0.3550 0.4044 0.0028 -0.0642 0.0172 110 GLU A CB 761 C CG . GLU A 94 ? 0.3973 0.3546 0.4067 0.0060 -0.0688 0.0159 110 GLU A CG 762 C CD . GLU A 94 ? 0.4053 0.3558 0.4179 0.0073 -0.0736 0.0167 110 GLU A CD 763 O OE1 . GLU A 94 ? 0.4012 0.3500 0.4183 0.0057 -0.0734 0.0173 110 GLU A OE1 764 O OE2 . GLU A 94 ? 0.4152 0.3618 0.4257 0.0101 -0.0779 0.0168 110 GLU A OE2 765 N N . ASP A 95 ? 0.4317 0.3914 0.4217 0.0013 -0.0587 0.0275 111 ASP A N 766 C CA . ASP A 95 ? 0.4510 0.4078 0.4308 0.0020 -0.0584 0.0324 111 ASP A CA 767 C C . ASP A 95 ? 0.4361 0.3986 0.4111 0.0014 -0.0544 0.0324 111 ASP A C 768 O O . ASP A 95 ? 0.4343 0.3963 0.4027 0.0030 -0.0549 0.0337 111 ASP A O 769 C CB . ASP A 95 ? 0.4853 0.4368 0.4616 0.0004 -0.0577 0.0377 111 ASP A CB 770 C CG . ASP A 95 ? 0.5345 0.4785 0.5126 0.0017 -0.0623 0.0390 111 ASP A CG 771 O OD1 . ASP A 95 ? 0.5430 0.4857 0.5246 0.0042 -0.0664 0.0359 111 ASP A OD1 772 O OD2 . ASP A 95 ? 0.5771 0.5162 0.5533 0.0003 -0.0618 0.0433 111 ASP A OD2 773 N N . ASP A 96 ? 0.4153 0.3834 0.3938 -0.0007 -0.0505 0.0308 112 ASP A N 774 C CA . ASP A 96 ? 0.4021 0.3759 0.3770 -0.0013 -0.0467 0.0304 112 ASP A CA 775 C C . ASP A 96 ? 0.3832 0.3601 0.3590 0.0006 -0.0475 0.0266 112 ASP A C 776 O O . ASP A 96 ? 0.3783 0.3575 0.3488 0.0012 -0.0459 0.0272 112 ASP A O 777 C CB . ASP A 96 ? 0.4059 0.3848 0.3849 -0.0038 -0.0430 0.0292 112 ASP A CB 778 C CG . ASP A 96 ? 0.4283 0.4053 0.4054 -0.0060 -0.0410 0.0331 112 ASP A CG 779 O OD1 . ASP A 96 ? 0.4423 0.4145 0.4133 -0.0058 -0.0416 0.0374 112 ASP A OD1 780 O OD2 . ASP A 96 ? 0.4448 0.4251 0.4266 -0.0080 -0.0388 0.0318 112 ASP A OD2 781 N N . TYR A 97 ? 0.3710 0.3482 0.3540 0.0015 -0.0498 0.0224 113 TYR A N 782 C CA . TYR A 97 ? 0.3671 0.3471 0.3521 0.0032 -0.0505 0.0184 113 TYR A CA 783 C C . TYR A 97 ? 0.3746 0.3510 0.3546 0.0058 -0.0538 0.0195 113 TYR A C 784 O O . TYR A 97 ? 0.3675 0.3463 0.3446 0.0068 -0.0529 0.0185 113 TYR A O 785 C CB . TYR A 97 ? 0.3688 0.3499 0.3631 0.0034 -0.0521 0.0134 113 TYR A CB 786 C CG . TYR A 97 ? 0.3668 0.3512 0.3640 0.0048 -0.0519 0.0090 113 TYR A CG 787 C CD1 . TYR A 97 ? 0.3657 0.3557 0.3631 0.0038 -0.0479 0.0071 113 TYR A CD1 788 C CD2 . TYR A 97 ? 0.3732 0.3552 0.3730 0.0071 -0.0559 0.0065 113 TYR A CD2 789 C CE1 . TYR A 97 ? 0.3671 0.3598 0.3671 0.0049 -0.0474 0.0033 113 TYR A CE1 790 C CE2 . TYR A 97 ? 0.3714 0.3566 0.3744 0.0082 -0.0555 0.0023 113 TYR A CE2 791 C CZ . TYR A 97 ? 0.3651 0.3556 0.3683 0.0069 -0.0510 0.0007 113 TYR A CZ 792 O OH . TYR A 97 ? 0.3642 0.3575 0.3706 0.0078 -0.0503 -0.0032 113 TYR A OH 793 N N . ALA A 98 ? 0.3820 0.3523 0.3607 0.0068 -0.0575 0.0217 114 ALA A N 794 C CA . ALA A 98 ? 0.3868 0.3531 0.3602 0.0095 -0.0612 0.0230 114 ALA A CA 795 C C . ALA A 98 ? 0.3898 0.3564 0.3534 0.0095 -0.0590 0.0269 114 ALA A C 796 O O . ALA A 98 ? 0.3991 0.3663 0.3591 0.0115 -0.0602 0.0260 114 ALA A O 797 C CB . ALA A 98 ? 0.3902 0.3495 0.3636 0.0106 -0.0655 0.0252 114 ALA A CB 798 N N . GLU A 99 ? 0.3855 0.3519 0.3452 0.0072 -0.0558 0.0309 115 GLU A N 799 C CA . GLU A 99 ? 0.3918 0.3592 0.3429 0.0068 -0.0530 0.0343 115 GLU A CA 800 C C . GLU A 99 ? 0.3804 0.3542 0.3318 0.0068 -0.0501 0.0314 115 GLU A C 801 O O . GLU A 99 ? 0.3774 0.3519 0.3228 0.0081 -0.0499 0.0322 115 GLU A O 802 C CB . GLU A 99 ? 0.4045 0.3711 0.3531 0.0041 -0.0497 0.0385 115 GLU A CB 803 C CG . GLU A 99 ? 0.4227 0.3897 0.3620 0.0037 -0.0471 0.0422 115 GLU A CG 804 C CD . GLU A 99 ? 0.4366 0.4034 0.3740 0.0008 -0.0434 0.0459 115 GLU A CD 805 O OE1 . GLU A 99 ? 0.4478 0.4144 0.3912 -0.0009 -0.0428 0.0456 115 GLU A OE1 806 O OE2 . GLU A 99 ? 0.4371 0.4042 0.3672 0.0004 -0.0410 0.0490 115 GLU A OE2 807 N N . LEU A 100 ? 0.3652 0.3437 0.3234 0.0055 -0.0478 0.0281 116 LEU A N 808 C CA . LEU A 100 ? 0.3575 0.3416 0.3163 0.0056 -0.0452 0.0254 116 LEU A CA 809 C C . LEU A 100 ? 0.3572 0.3412 0.3167 0.0082 -0.0479 0.0223 116 LEU A C 810 O O . LEU A 100 ? 0.3480 0.3341 0.3035 0.0091 -0.0467 0.0221 116 LEU A O 811 C CB . LEU A 100 ? 0.3504 0.3389 0.3161 0.0039 -0.0426 0.0224 116 LEU A CB 812 C CG . LEU A 100 ? 0.3494 0.3433 0.3158 0.0039 -0.0396 0.0197 116 LEU A CG 813 C CD1 . LEU A 100 ? 0.3442 0.3401 0.3037 0.0036 -0.0367 0.0225 116 LEU A CD1 814 C CD2 . LEU A 100 ? 0.3411 0.3386 0.3136 0.0023 -0.0373 0.0172 116 LEU A CD2 815 N N . LEU A 101 ? 0.3554 0.3369 0.3202 0.0095 -0.0516 0.0196 117 LEU A N 816 C CA . LEU A 101 ? 0.3631 0.3447 0.3297 0.0120 -0.0544 0.0162 117 LEU A CA 817 C C . LEU A 101 ? 0.3679 0.3466 0.3263 0.0141 -0.0566 0.0188 117 LEU A C 818 O O . LEU A 101 ? 0.3638 0.3444 0.3209 0.0156 -0.0567 0.0167 117 LEU A O 819 C CB . LEU A 101 ? 0.3747 0.3538 0.3485 0.0132 -0.0583 0.0130 117 LEU A CB 820 C CG . LEU A 101 ? 0.3757 0.3580 0.3587 0.0118 -0.0567 0.0089 117 LEU A CG 821 C CD1 . LEU A 101 ? 0.3871 0.3664 0.3767 0.0132 -0.0612 0.0060 117 LEU A CD1 822 C CD2 . LEU A 101 ? 0.3709 0.3586 0.3567 0.0115 -0.0536 0.0053 117 LEU A CD2 823 N N . ASP A 102 ? 0.3868 0.3607 0.3395 0.0141 -0.0581 0.0232 118 ASP A N 824 C CA . ASP A 102 ? 0.4007 0.3715 0.3443 0.0159 -0.0599 0.0263 118 ASP A CA 825 C C . ASP A 102 ? 0.3910 0.3657 0.3289 0.0150 -0.0558 0.0277 118 ASP A C 826 O O . ASP A 102 ? 0.3924 0.3673 0.3256 0.0170 -0.0569 0.0273 118 ASP A O 827 C CB . ASP A 102 ? 0.4377 0.4024 0.3761 0.0155 -0.0614 0.0313 118 ASP A CB 828 C CG . ASP A 102 ? 0.4759 0.4354 0.4177 0.0175 -0.0668 0.0304 118 ASP A CG 829 O OD1 . ASP A 102 ? 0.4922 0.4523 0.4387 0.0197 -0.0701 0.0260 118 ASP A OD1 830 O OD2 . ASP A 102 ? 0.5053 0.4598 0.4454 0.0167 -0.0677 0.0340 118 ASP A OD2 831 N N . THR A 103 ? 0.3776 0.3554 0.3162 0.0123 -0.0513 0.0290 119 THR A N 832 C CA . THR A 103 ? 0.3693 0.3513 0.3037 0.0114 -0.0472 0.0300 119 THR A CA 833 C C . THR A 103 ? 0.3576 0.3440 0.2953 0.0125 -0.0465 0.0256 119 THR A C 834 O O . THR A 103 ? 0.3578 0.3459 0.2909 0.0134 -0.0456 0.0258 119 THR A O 835 C CB . THR A 103 ? 0.3571 0.3417 0.2930 0.0083 -0.0429 0.0316 119 THR A CB 836 O OG1 . THR A 103 ? 0.3704 0.3509 0.3049 0.0071 -0.0435 0.0352 119 THR A OG1 837 C CG2 . THR A 103 ? 0.3499 0.3380 0.2805 0.0075 -0.0390 0.0333 119 THR A CG2 838 N N . LEU A 104 ? 0.3539 0.3421 0.2997 0.0123 -0.0468 0.0217 120 LEU A N 839 C CA . LEU A 104 ? 0.3427 0.3348 0.2925 0.0131 -0.0457 0.0175 120 LEU A CA 840 C C . LEU A 104 ? 0.3521 0.3428 0.3005 0.0160 -0.0492 0.0155 120 LEU A C 841 O O . LEU A 104 ? 0.3349 0.3284 0.2820 0.0167 -0.0478 0.0140 120 LEU A O 842 C CB . LEU A 104 ? 0.3376 0.3317 0.2964 0.0122 -0.0450 0.0138 120 LEU A CB 843 C CG . LEU A 104 ? 0.3313 0.3279 0.2917 0.0095 -0.0411 0.0149 120 LEU A CG 844 C CD1 . LEU A 104 ? 0.3244 0.3224 0.2932 0.0088 -0.0409 0.0113 120 LEU A CD1 845 C CD2 . LEU A 104 ? 0.3219 0.3225 0.2790 0.0087 -0.0370 0.0158 120 LEU A CD2 846 N N . SER A 105 ? 0.3548 0.3412 0.3035 0.0176 -0.0538 0.0153 121 SER A N 847 C CA . SER A 105 ? 0.3656 0.3508 0.3134 0.0206 -0.0576 0.0130 121 SER A CA 848 C C . SER A 105 ? 0.3633 0.3472 0.3011 0.0217 -0.0579 0.0163 121 SER A C 849 O O . SER A 105 ? 0.3687 0.3538 0.3051 0.0237 -0.0592 0.0141 121 SER A O 850 C CB . SER A 105 ? 0.3743 0.3556 0.3263 0.0224 -0.0629 0.0111 121 SER A CB 851 O OG . SER A 105 ? 0.3933 0.3700 0.3418 0.0220 -0.0645 0.0152 121 SER A OG 852 N N . ALA A 106 ? 0.3586 0.3404 0.2898 0.0204 -0.0565 0.0213 122 ALA A N 853 C CA . ALA A 106 ? 0.3624 0.3435 0.2839 0.0211 -0.0559 0.0245 122 ALA A CA 854 C C . ALA A 106 ? 0.3555 0.3419 0.2767 0.0206 -0.0521 0.0229 122 ALA A C 855 O O . ALA A 106 ? 0.3548 0.3419 0.2717 0.0224 -0.0530 0.0222 122 ALA A O 856 C CB . ALA A 106 ? 0.3665 0.3447 0.2818 0.0192 -0.0542 0.0301 122 ALA A CB 857 N N . MET A 107 ? 0.3425 0.3327 0.2687 0.0183 -0.0481 0.0221 123 MET A N 858 C CA . MET A 107 ? 0.3413 0.3363 0.2675 0.0178 -0.0445 0.0207 123 MET A CA 859 C C . MET A 107 ? 0.3361 0.3333 0.2675 0.0195 -0.0456 0.0158 123 MET A C 860 O O . MET A 107 ? 0.3313 0.3308 0.2602 0.0205 -0.0446 0.0148 123 MET A O 861 C CB . MET A 107 ? 0.3372 0.3354 0.2668 0.0150 -0.0400 0.0215 123 MET A CB 862 C CG . MET A 107 ? 0.3567 0.3538 0.2814 0.0131 -0.0381 0.0261 123 MET A CG 863 S SD . MET A 107 ? 0.3708 0.3726 0.2979 0.0103 -0.0328 0.0267 123 MET A SD 864 C CE . MET A 107 ? 0.3480 0.3502 0.2844 0.0095 -0.0333 0.0237 123 MET A CE 865 N N . GLU A 108 ? 0.3461 0.3428 0.2850 0.0199 -0.0476 0.0124 124 GLU A N 866 C CA . GLU A 108 ? 0.3599 0.3587 0.3047 0.0214 -0.0484 0.0074 124 GLU A CA 867 C C . GLU A 108 ? 0.3664 0.3634 0.3080 0.0244 -0.0526 0.0060 124 GLU A C 868 O O . GLU A 108 ? 0.3628 0.3622 0.3052 0.0255 -0.0522 0.0033 124 GLU A O 869 C CB . GLU A 108 ? 0.3794 0.3785 0.3337 0.0208 -0.0489 0.0039 124 GLU A CB 870 C CG . GLU A 108 ? 0.4130 0.4141 0.3738 0.0221 -0.0494 -0.0014 124 GLU A CG 871 C CD . GLU A 108 ? 0.4318 0.4352 0.4014 0.0206 -0.0468 -0.0046 124 GLU A CD 872 O OE1 . GLU A 108 ? 0.4432 0.4466 0.4141 0.0186 -0.0448 -0.0030 124 GLU A OE1 873 O OE2 . GLU A 108 ? 0.4350 0.4402 0.4103 0.0213 -0.0465 -0.0089 124 GLU A OE2 874 N N . SER A 109 ? 0.3669 0.3596 0.3047 0.0258 -0.0568 0.0079 125 SER A N 875 C CA . SER A 109 ? 0.3777 0.3683 0.3113 0.0289 -0.0613 0.0068 125 SER A CA 876 C C . SER A 109 ? 0.3772 0.3687 0.3018 0.0295 -0.0599 0.0092 125 SER A C 877 O O . SER A 109 ? 0.3889 0.3814 0.3122 0.0319 -0.0621 0.0066 125 SER A O 878 C CB . SER A 109 ? 0.3831 0.3683 0.3145 0.0305 -0.0662 0.0085 125 SER A CB 879 O OG . SER A 109 ? 0.3945 0.3768 0.3179 0.0292 -0.0651 0.0142 125 SER A OG 880 N N . ASN A 110 ? 0.3671 0.3586 0.2858 0.0274 -0.0565 0.0139 126 ASN A N 881 C CA . ASN A 110 ? 0.3578 0.3510 0.2688 0.0275 -0.0542 0.0159 126 ASN A CA 882 C C . ASN A 110 ? 0.3465 0.3446 0.2619 0.0278 -0.0520 0.0119 126 ASN A C 883 O O . ASN A 110 ? 0.3392 0.3383 0.2513 0.0298 -0.0532 0.0104 126 ASN A O 884 C CB . ASN A 110 ? 0.3555 0.3489 0.2618 0.0248 -0.0501 0.0208 126 ASN A CB 885 C CG . ASN A 110 ? 0.3645 0.3600 0.2632 0.0249 -0.0476 0.0225 126 ASN A CG 886 O OD1 . ASN A 110 ? 0.3722 0.3651 0.2626 0.0262 -0.0493 0.0249 126 ASN A OD1 887 N ND2 . ASN A 110 ? 0.3482 0.3483 0.2497 0.0235 -0.0436 0.0213 126 ASN A ND2 888 N N . PHE A 111 ? 0.3279 0.3288 0.2506 0.0258 -0.0487 0.0103 127 PHE A N 889 C CA . PHE A 111 ? 0.3243 0.3293 0.2517 0.0258 -0.0463 0.0068 127 PHE A CA 890 C C . PHE A 111 ? 0.3321 0.3372 0.2634 0.0285 -0.0498 0.0019 127 PHE A C 891 O O . PHE A 111 ? 0.3337 0.3409 0.2637 0.0298 -0.0495 0.0000 127 PHE A O 892 C CB . PHE A 111 ? 0.3151 0.3222 0.2498 0.0235 -0.0426 0.0058 127 PHE A CB 893 C CG . PHE A 111 ? 0.3081 0.3190 0.2465 0.0232 -0.0393 0.0032 127 PHE A CG 894 C CD1 . PHE A 111 ? 0.3026 0.3145 0.2481 0.0243 -0.0403 -0.0016 127 PHE A CD1 895 C CD2 . PHE A 111 ? 0.3076 0.3210 0.2426 0.0218 -0.0353 0.0055 127 PHE A CD2 896 C CE1 . PHE A 111 ? 0.2936 0.3085 0.2426 0.0240 -0.0371 -0.0038 127 PHE A CE1 897 C CE2 . PHE A 111 ? 0.2974 0.3138 0.2357 0.0217 -0.0324 0.0032 127 PHE A CE2 898 C CZ . PHE A 111 ? 0.2956 0.3126 0.2408 0.0228 -0.0332 -0.0013 127 PHE A CZ 899 N N . ALA A 112 ? 0.3323 0.3353 0.2691 0.0294 -0.0532 -0.0004 128 ALA A N 900 C CA . ALA A 112 ? 0.3416 0.3451 0.2839 0.0318 -0.0566 -0.0057 128 ALA A CA 901 C C . ALA A 112 ? 0.3560 0.3581 0.2915 0.0348 -0.0607 -0.0059 128 ALA A C 902 O O . ALA A 112 ? 0.3642 0.3678 0.3029 0.0369 -0.0627 -0.0103 128 ALA A O 903 C CB . ALA A 112 ? 0.3436 0.3451 0.2932 0.0320 -0.0594 -0.0080 128 ALA A CB 904 N N . LYS A 113 ? 0.3733 0.3724 0.2994 0.0351 -0.0619 -0.0012 129 LYS A N 905 C CA . LYS A 113 ? 0.3940 0.3911 0.3122 0.0381 -0.0661 -0.0008 129 LYS A CA 906 C C . LYS A 113 ? 0.3955 0.3949 0.3062 0.0384 -0.0638 0.0004 129 LYS A C 907 O O . LYS A 113 ? 0.4079 0.4060 0.3116 0.0409 -0.0670 0.0004 129 LYS A O 908 C CB . LYS A 113 ? 0.4196 0.4114 0.3312 0.0386 -0.0692 0.0033 129 LYS A CB 909 C CG . LYS A 113 ? 0.4491 0.4381 0.3668 0.0401 -0.0739 0.0009 129 LYS A CG 910 C CD . LYS A 113 ? 0.4888 0.4723 0.4001 0.0400 -0.0760 0.0059 129 LYS A CD 911 C CE . LYS A 113 ? 0.5272 0.5070 0.4418 0.0427 -0.0822 0.0036 129 LYS A CE 912 N NZ . LYS A 113 ? 0.5696 0.5443 0.4805 0.0418 -0.0832 0.0085 129 LYS A NZ 913 N N . VAL A 114 ? 0.3890 0.3917 0.3009 0.0359 -0.0584 0.0014 130 VAL A N 914 C CA . VAL A 114 ? 0.3823 0.3876 0.2879 0.0360 -0.0558 0.0025 130 VAL A CA 915 C C . VAL A 114 ? 0.3857 0.3929 0.2921 0.0389 -0.0584 -0.0022 130 VAL A C 916 O O . VAL A 114 ? 0.3812 0.3904 0.2966 0.0394 -0.0588 -0.0070 130 VAL A O 917 C CB . VAL A 114 ? 0.3724 0.3812 0.2811 0.0331 -0.0499 0.0034 130 VAL A CB 918 C CG1 . VAL A 114 ? 0.3614 0.3734 0.2657 0.0336 -0.0476 0.0031 130 VAL A CG1 919 C CG2 . VAL A 114 ? 0.3623 0.3697 0.2685 0.0303 -0.0472 0.0084 130 VAL A CG2 920 N N . LYS A 115 ? 0.3959 0.4025 0.2931 0.0407 -0.0601 -0.0009 131 LYS A N 921 C CA . LYS A 115 ? 0.4070 0.4158 0.3036 0.0435 -0.0622 -0.0052 131 LYS A CA 922 C C . LYS A 115 ? 0.4044 0.4151 0.2924 0.0432 -0.0594 -0.0028 131 LYS A C 923 O O . LYS A 115 ? 0.4059 0.4145 0.2855 0.0422 -0.0581 0.0022 131 LYS A O 924 C CB . LYS A 115 ? 0.4252 0.4309 0.3187 0.0470 -0.0687 -0.0070 131 LYS A CB 925 C CG . LYS A 115 ? 0.4329 0.4367 0.3349 0.0477 -0.0723 -0.0098 131 LYS A CG 926 C CD . LYS A 115 ? 0.4490 0.4562 0.3618 0.0488 -0.0731 -0.0167 131 LYS A CD 927 C CE . LYS A 115 ? 0.4636 0.4688 0.3826 0.0511 -0.0787 -0.0205 131 LYS A CE 928 N NZ . LYS A 115 ? 0.4766 0.4800 0.4020 0.0489 -0.0777 -0.0194 131 LYS A NZ 929 N N . VAL A 116 ? 0.4084 0.4230 0.2989 0.0441 -0.0582 -0.0065 132 VAL A N 930 C CA . VAL A 116 ? 0.4196 0.4366 0.3027 0.0440 -0.0555 -0.0050 132 VAL A CA 931 C C . VAL A 116 ? 0.4411 0.4595 0.3212 0.0475 -0.0590 -0.0092 132 VAL A C 932 O O . VAL A 116 ? 0.4365 0.4550 0.3225 0.0497 -0.0629 -0.0139 132 VAL A O 933 C CB . VAL A 116 ? 0.4088 0.4296 0.2967 0.0414 -0.0497 -0.0049 132 VAL A CB 934 C CG1 . VAL A 116 ? 0.3983 0.4179 0.2891 0.0382 -0.0466 -0.0012 132 VAL A CG1 935 C CG2 . VAL A 116 ? 0.3974 0.4214 0.2953 0.0421 -0.0495 -0.0106 132 VAL A CG2 936 N N . CYS A 117 ? 0.4567 0.4765 0.3280 0.0480 -0.0576 -0.0075 133 CYS A N 937 C CA . CYS A 117 ? 0.4822 0.5038 0.3501 0.0512 -0.0605 -0.0116 133 CYS A CA 938 C C . CYS A 117 ? 0.4691 0.4957 0.3447 0.0509 -0.0578 -0.0161 133 CYS A C 939 O O . CYS A 117 ? 0.4445 0.4732 0.3230 0.0483 -0.0528 -0.0144 133 CYS A O 940 C CB . CYS A 117 ? 0.5227 0.5432 0.3769 0.0520 -0.0604 -0.0079 133 CYS A CB 941 S SG . CYS A 117 ? 0.5732 0.5871 0.4177 0.0526 -0.0637 -0.0024 133 CYS A SG 942 N N . ASP A 118 ? 0.4677 0.4960 0.3469 0.0538 -0.0613 -0.0219 134 ASP A N 943 C CA . ASP A 118 ? 0.4727 0.5054 0.3595 0.0540 -0.0593 -0.0267 134 ASP A CA 944 C C . ASP A 118 ? 0.4724 0.5080 0.3528 0.0532 -0.0553 -0.0249 134 ASP A C 945 O O . ASP A 118 ? 0.4787 0.5138 0.3482 0.0544 -0.0563 -0.0227 134 ASP A O 946 C CB . ASP A 118 ? 0.4951 0.5289 0.3851 0.0577 -0.0645 -0.0332 134 ASP A CB 947 C CG . ASP A 118 ? 0.5027 0.5406 0.4029 0.0578 -0.0628 -0.0389 134 ASP A CG 948 O OD1 . ASP A 118 ? 0.5218 0.5628 0.4200 0.0574 -0.0597 -0.0391 134 ASP A OD1 949 O OD2 . ASP A 118 ? 0.5084 0.5466 0.4191 0.0583 -0.0646 -0.0433 134 ASP A OD2 950 N N . TYR A 119 ? 0.4602 0.4988 0.3476 0.0512 -0.0508 -0.0257 135 TYR A N 951 C CA . TYR A 119 ? 0.4610 0.5028 0.3446 0.0504 -0.0469 -0.0249 135 TYR A CA 952 C C . TYR A 119 ? 0.4911 0.5354 0.3698 0.0535 -0.0493 -0.0287 135 TYR A C 953 O O . TYR A 119 ? 0.4942 0.5400 0.3647 0.0534 -0.0473 -0.0268 135 TYR A O 954 C CB . TYR A 119 ? 0.4394 0.4838 0.3333 0.0485 -0.0427 -0.0265 135 TYR A CB 955 C CG . TYR A 119 ? 0.4276 0.4754 0.3193 0.0476 -0.0385 -0.0258 135 TYR A CG 956 C CD1 . TYR A 119 ? 0.4236 0.4713 0.3073 0.0458 -0.0356 -0.0206 135 TYR A CD1 957 C CD2 . TYR A 119 ? 0.4180 0.4692 0.3161 0.0485 -0.0375 -0.0305 135 TYR A CD2 958 C CE1 . TYR A 119 ? 0.4198 0.4710 0.3021 0.0450 -0.0318 -0.0203 135 TYR A CE1 959 C CE2 . TYR A 119 ? 0.4188 0.4732 0.3154 0.0478 -0.0338 -0.0301 135 TYR A CE2 960 C CZ . TYR A 119 ? 0.4168 0.4713 0.3055 0.0461 -0.0310 -0.0251 135 TYR A CZ 961 O OH . TYR A 119 ? 0.4162 0.4741 0.3040 0.0455 -0.0274 -0.0250 135 TYR A OH 962 N N . LYS A 120 ? 0.5229 0.5677 0.4067 0.0561 -0.0535 -0.0343 136 LYS A N 963 C CA . LYS A 120 ? 0.5773 0.6247 0.4578 0.0593 -0.0562 -0.0389 136 LYS A CA 964 C C . LYS A 120 ? 0.5997 0.6447 0.4714 0.0624 -0.0619 -0.0392 136 LYS A C 965 O O . LYS A 120 ? 0.6123 0.6592 0.4791 0.0653 -0.0645 -0.0426 136 LYS A O 966 C CB . LYS A 120 ? 0.5896 0.6399 0.4825 0.0603 -0.0568 -0.0457 136 LYS A CB 967 C CG . LYS A 120 ? 0.6291 0.6821 0.5292 0.0579 -0.0514 -0.0460 136 LYS A CG 968 C CD . LYS A 120 ? 0.6647 0.7198 0.5776 0.0588 -0.0520 -0.0525 136 LYS A CD 969 C CE . LYS A 120 ? 0.6839 0.7414 0.6031 0.0568 -0.0467 -0.0529 136 LYS A CE 970 N NZ . LYS A 120 ? 0.6597 0.7152 0.5842 0.0536 -0.0429 -0.0490 136 LYS A NZ 971 N N . ASP A 121 ? 0.6062 0.6468 0.4755 0.0620 -0.0639 -0.0356 137 ASP A N 972 C CA . ASP A 121 ? 0.6376 0.6752 0.4991 0.0651 -0.0698 -0.0358 137 ASP A CA 973 C C . ASP A 121 ? 0.6570 0.6896 0.5109 0.0637 -0.0699 -0.0290 137 ASP A C 974 O O . ASP A 121 ? 0.6553 0.6850 0.5147 0.0631 -0.0716 -0.0283 137 ASP A O 975 C CB . ASP A 121 ? 0.6473 0.6850 0.5186 0.0675 -0.0748 -0.0419 137 ASP A CB 976 C CG . ASP A 121 ? 0.6729 0.7080 0.5366 0.0715 -0.0816 -0.0433 137 ASP A CG 977 O OD1 . ASP A 121 ? 0.6885 0.7213 0.5387 0.0724 -0.0824 -0.0391 137 ASP A OD1 978 O OD2 . ASP A 121 ? 0.6650 0.7005 0.5364 0.0738 -0.0862 -0.0489 137 ASP A OD2 979 N N . SER A 122 ? 0.6794 0.7109 0.5209 0.0632 -0.0680 -0.0241 138 SER A N 980 C CA . SER A 122 ? 0.7112 0.7379 0.5452 0.0615 -0.0674 -0.0173 138 SER A CA 981 C C . SER A 122 ? 0.7311 0.7529 0.5607 0.0643 -0.0736 -0.0169 138 SER A C 982 O O . SER A 122 ? 0.7444 0.7615 0.5683 0.0632 -0.0737 -0.0114 138 SER A O 983 C CB . SER A 122 ? 0.7238 0.7506 0.5460 0.0602 -0.0634 -0.0124 138 SER A CB 984 O OG . SER A 122 ? 0.7442 0.7718 0.5566 0.0633 -0.0658 -0.0142 138 SER A OG 985 N N . THR A 123 ? 0.7519 0.7747 0.5846 0.0679 -0.0789 -0.0228 139 THR A N 986 C CA . THR A 123 ? 0.7783 0.7970 0.6095 0.0710 -0.0856 -0.0238 139 THR A CA 987 C C . THR A 123 ? 0.7509 0.7682 0.5945 0.0695 -0.0862 -0.0248 139 THR A C 988 O O . THR A 123 ? 0.7582 0.7709 0.6000 0.0699 -0.0893 -0.0222 139 THR A O 989 C CB . THR A 123 ? 0.7896 0.8106 0.6212 0.0755 -0.0912 -0.0307 139 THR A CB 990 O OG1 . THR A 123 ? 0.8347 0.8574 0.6549 0.0770 -0.0904 -0.0302 139 THR A OG1 991 C CG2 . THR A 123 ? 0.8183 0.8350 0.6477 0.0790 -0.0985 -0.0318 139 THR A CG2 992 N N . LYS A 124 ? 0.6987 0.7202 0.5550 0.0678 -0.0833 -0.0288 140 LYS A N 993 C CA . LYS A 124 ? 0.6552 0.6762 0.5244 0.0665 -0.0837 -0.0309 140 LYS A CA 994 C C . LYS A 124 ? 0.6278 0.6471 0.4984 0.0622 -0.0786 -0.0252 140 LYS A C 995 O O . LYS A 124 ? 0.5928 0.6150 0.4669 0.0594 -0.0731 -0.0243 140 LYS A O 996 C CB . LYS A 124 ? 0.6646 0.6905 0.5462 0.0666 -0.0827 -0.0377 140 LYS A CB 997 C CG . LYS A 124 ? 0.7050 0.7305 0.5995 0.0669 -0.0853 -0.0422 140 LYS A CG 998 C CD . LYS A 124 ? 0.7276 0.7576 0.6349 0.0657 -0.0821 -0.0473 140 LYS A CD 999 C CE . LYS A 124 ? 0.7491 0.7793 0.6691 0.0667 -0.0853 -0.0532 140 LYS A CE 1000 N NZ . LYS A 124 ? 0.7605 0.7873 0.6843 0.0649 -0.0852 -0.0504 140 LYS A NZ 1001 N N . CYS A 125 ? 0.6016 0.6162 0.4694 0.0619 -0.0806 -0.0214 141 CYS A N 1002 C CA . CYS A 125 ? 0.5860 0.5987 0.4539 0.0581 -0.0763 -0.0157 141 CYS A CA 1003 C C . CYS A 125 ? 0.5568 0.5675 0.4345 0.0570 -0.0774 -0.0164 141 CYS A C 1004 O O . CYS A 125 ? 0.5499 0.5570 0.4250 0.0554 -0.0769 -0.0117 141 CYS A O 1005 C CB . CYS A 125 ? 0.6093 0.6180 0.4634 0.0579 -0.0760 -0.0092 141 CYS A CB 1006 S SG . CYS A 125 ? 0.6499 0.6615 0.4927 0.0582 -0.0729 -0.0077 141 CYS A SG 1007 N N . ASP A 126 ? 0.5354 0.5486 0.4246 0.0578 -0.0787 -0.0224 142 ASP A N 1008 C CA . ASP A 126 ? 0.5204 0.5322 0.4197 0.0570 -0.0799 -0.0241 142 ASP A CA 1009 C C . ASP A 126 ? 0.4829 0.4982 0.3941 0.0542 -0.0752 -0.0268 142 ASP A C 1010 O O . ASP A 126 ? 0.4612 0.4769 0.3829 0.0543 -0.0764 -0.0308 142 ASP A O 1011 C CB . ASP A 126 ? 0.5493 0.5600 0.4519 0.0608 -0.0868 -0.0293 142 ASP A CB 1012 C CG . ASP A 126 ? 0.5847 0.5996 0.4927 0.0630 -0.0882 -0.0361 142 ASP A CG 1013 O OD1 . ASP A 126 ? 0.6001 0.6184 0.5069 0.0621 -0.0843 -0.0364 142 ASP A OD1 1014 O OD2 . ASP A 126 ? 0.6067 0.6217 0.5207 0.0657 -0.0932 -0.0414 142 ASP A OD2 1015 N N . LEU A 127 ? 0.4574 0.4752 0.3669 0.0519 -0.0697 -0.0246 143 LEU A N 1016 C CA . LEU A 127 ? 0.4315 0.4523 0.3509 0.0494 -0.0650 -0.0264 143 LEU A CA 1017 C C . LEU A 127 ? 0.4131 0.4319 0.3345 0.0462 -0.0619 -0.0222 143 LEU A C 1018 O O . LEU A 127 ? 0.4073 0.4249 0.3212 0.0446 -0.0597 -0.0168 143 LEU A O 1019 C CB . LEU A 127 ? 0.4339 0.4581 0.3508 0.0486 -0.0608 -0.0261 143 LEU A CB 1020 C CG . LEU A 127 ? 0.4440 0.4712 0.3619 0.0513 -0.0626 -0.0314 143 LEU A CG 1021 C CD1 . LEU A 127 ? 0.4617 0.4876 0.3701 0.0546 -0.0678 -0.0317 143 LEU A CD1 1022 C CD2 . LEU A 127 ? 0.4433 0.4739 0.3605 0.0499 -0.0577 -0.0308 143 LEU A CD2 1023 N N . ALA A 128 ? 0.3959 0.4148 0.3277 0.0453 -0.0617 -0.0250 144 ALA A N 1024 C CA . ALA A 128 ? 0.3763 0.3938 0.3112 0.0423 -0.0586 -0.0218 144 ALA A CA 1025 C C . ALA A 128 ? 0.3621 0.3826 0.3025 0.0397 -0.0528 -0.0221 144 ALA A C 1026 O O . ALA A 128 ? 0.3501 0.3732 0.2948 0.0403 -0.0516 -0.0258 144 ALA A O 1027 C CB . ALA A 128 ? 0.3670 0.3827 0.3095 0.0428 -0.0617 -0.0245 144 ALA A CB 1028 N N . LEU A 129 ? 0.3520 0.3718 0.2922 0.0369 -0.0492 -0.0181 145 LEU A N 1029 C CA . LEU A 129 ? 0.3493 0.3713 0.2946 0.0346 -0.0439 -0.0182 145 LEU A CA 1030 C C . LEU A 129 ? 0.3568 0.3800 0.3129 0.0349 -0.0437 -0.0237 145 LEU A C 1031 O O . LEU A 129 ? 0.3561 0.3817 0.3157 0.0348 -0.0411 -0.0259 145 LEU A O 1032 C CB . LEU A 129 ? 0.3346 0.3554 0.2796 0.0319 -0.0410 -0.0141 145 LEU A CB 1033 C CG . LEU A 129 ? 0.3264 0.3492 0.2757 0.0295 -0.0357 -0.0135 145 LEU A CG 1034 C CD1 . LEU A 129 ? 0.3194 0.3443 0.2633 0.0291 -0.0327 -0.0112 145 LEU A CD1 1035 C CD2 . LEU A 129 ? 0.3196 0.3410 0.2696 0.0272 -0.0340 -0.0104 145 LEU A CD2 1036 N N . ASP A 130 ? 0.3621 0.3838 0.3238 0.0353 -0.0464 -0.0261 146 ASP A N 1037 C CA . ASP A 130 ? 0.3689 0.3915 0.3415 0.0354 -0.0460 -0.0314 146 ASP A CA 1038 C C . ASP A 130 ? 0.3702 0.3926 0.3453 0.0384 -0.0517 -0.0360 146 ASP A C 1039 O O . ASP A 130 ? 0.3694 0.3895 0.3437 0.0394 -0.0556 -0.0359 146 ASP A O 1040 C CB . ASP A 130 ? 0.3792 0.4007 0.3574 0.0332 -0.0441 -0.0308 146 ASP A CB 1041 C CG . ASP A 130 ? 0.3960 0.4186 0.3858 0.0328 -0.0428 -0.0362 146 ASP A CG 1042 O OD1 . ASP A 130 ? 0.4134 0.4375 0.4075 0.0341 -0.0432 -0.0403 146 ASP A OD1 1043 O OD2 . ASP A 130 ? 0.3801 0.4019 0.3750 0.0311 -0.0413 -0.0363 146 ASP A OD2 1044 N N . PRO A 131 ? 0.3657 0.3902 0.3442 0.0400 -0.0523 -0.0404 147 PRO A N 1045 C CA . PRO A 131 ? 0.3589 0.3859 0.3404 0.0390 -0.0478 -0.0415 147 PRO A CA 1046 C C . PRO A 131 ? 0.3620 0.3904 0.3356 0.0400 -0.0473 -0.0398 147 PRO A C 1047 O O . PRO A 131 ? 0.3511 0.3813 0.3264 0.0389 -0.0432 -0.0398 147 PRO A O 1048 C CB . PRO A 131 ? 0.3642 0.3925 0.3565 0.0403 -0.0493 -0.0485 147 PRO A CB 1049 C CG . PRO A 131 ? 0.3732 0.4007 0.3634 0.0434 -0.0559 -0.0509 147 PRO A CG 1050 C CD . PRO A 131 ? 0.3756 0.4002 0.3581 0.0430 -0.0578 -0.0458 147 PRO A CD 1051 N N . GLU A 132 ? 0.3660 0.3937 0.3311 0.0422 -0.0514 -0.0386 148 GLU A N 1052 C CA . GLU A 132 ? 0.3735 0.4031 0.3321 0.0437 -0.0516 -0.0385 148 GLU A CA 1053 C C . GLU A 132 ? 0.3687 0.3995 0.3225 0.0416 -0.0465 -0.0342 148 GLU A C 1054 O O . GLU A 132 ? 0.3643 0.3975 0.3202 0.0417 -0.0442 -0.0361 148 GLU A O 1055 C CB . GLU A 132 ? 0.3869 0.4151 0.3361 0.0463 -0.0568 -0.0375 148 GLU A CB 1056 C CG . GLU A 132 ? 0.4048 0.4327 0.3583 0.0494 -0.0626 -0.0430 148 GLU A CG 1057 C CD . GLU A 132 ? 0.4098 0.4349 0.3675 0.0491 -0.0651 -0.0431 148 GLU A CD 1058 O OE1 . GLU A 132 ? 0.4099 0.4328 0.3639 0.0473 -0.0637 -0.0381 148 GLU A OE1 1059 O OE2 . GLU A 132 ? 0.4261 0.4516 0.3917 0.0509 -0.0685 -0.0486 148 GLU A OE2 1060 N N . ILE A 133 ? 0.3639 0.3930 0.3119 0.0397 -0.0448 -0.0287 149 ILE A N 1061 C CA . ILE A 133 ? 0.3563 0.3867 0.2993 0.0380 -0.0404 -0.0246 149 ILE A CA 1062 C C . ILE A 133 ? 0.3544 0.3861 0.3050 0.0360 -0.0357 -0.0254 149 ILE A C 1063 O O . ILE A 133 ? 0.3407 0.3744 0.2907 0.0357 -0.0328 -0.0253 149 ILE A O 1064 C CB . ILE A 133 ? 0.3525 0.3809 0.2875 0.0365 -0.0400 -0.0187 149 ILE A CB 1065 C CG1 . ILE A 133 ? 0.3633 0.3897 0.2905 0.0386 -0.0446 -0.0177 149 ILE A CG1 1066 C CG2 . ILE A 133 ? 0.3555 0.3857 0.2855 0.0350 -0.0358 -0.0151 149 ILE A CG2 1067 C CD1 . ILE A 133 ? 0.3555 0.3794 0.2758 0.0372 -0.0445 -0.0121 149 ILE A CD1 1068 N N . GLU A 134 ? 0.3643 0.3947 0.3219 0.0347 -0.0349 -0.0263 150 GLU A N 1069 C CA . GLU A 134 ? 0.3643 0.3954 0.3288 0.0328 -0.0304 -0.0270 150 GLU A CA 1070 C C . GLU A 134 ? 0.3686 0.4015 0.3394 0.0339 -0.0296 -0.0317 150 GLU A C 1071 O O . GLU A 134 ? 0.3661 0.3999 0.3397 0.0327 -0.0255 -0.0313 150 GLU A O 1072 C CB . GLU A 134 ? 0.3783 0.4077 0.3491 0.0313 -0.0298 -0.0274 150 GLU A CB 1073 C CG . GLU A 134 ? 0.3905 0.4186 0.3565 0.0294 -0.0284 -0.0223 150 GLU A CG 1074 C CD . GLU A 134 ? 0.4020 0.4290 0.3745 0.0275 -0.0263 -0.0227 150 GLU A CD 1075 O OE1 . GLU A 134 ? 0.4033 0.4298 0.3833 0.0280 -0.0275 -0.0269 150 GLU A OE1 1076 O OE2 . GLU A 134 ? 0.4137 0.4404 0.3839 0.0256 -0.0234 -0.0190 150 GLU A OE2 1077 N N . GLU A 135 ? 0.3708 0.4042 0.3438 0.0362 -0.0336 -0.0361 151 GLU A N 1078 C CA . GLU A 135 ? 0.3803 0.4157 0.3591 0.0375 -0.0334 -0.0410 151 GLU A CA 1079 C C . GLU A 135 ? 0.3721 0.4094 0.3455 0.0378 -0.0314 -0.0394 151 GLU A C 1080 O O . GLU A 135 ? 0.3754 0.4137 0.3537 0.0372 -0.0280 -0.0408 151 GLU A O 1081 C CB . GLU A 135 ? 0.3947 0.4304 0.3758 0.0402 -0.0388 -0.0460 151 GLU A CB 1082 C CG . GLU A 135 ? 0.4086 0.4466 0.3953 0.0419 -0.0393 -0.0515 151 GLU A CG 1083 C CD . GLU A 135 ? 0.4173 0.4553 0.4167 0.0411 -0.0374 -0.0562 151 GLU A CD 1084 O OE1 . GLU A 135 ? 0.4286 0.4651 0.4319 0.0386 -0.0338 -0.0543 151 GLU A OE1 1085 O OE2 . GLU A 135 ? 0.4261 0.4657 0.4317 0.0429 -0.0396 -0.0620 151 GLU A OE2 1086 N N . VAL A 136 ? 0.3676 0.4052 0.3311 0.0388 -0.0333 -0.0365 152 VAL A N 1087 C CA . VAL A 136 ? 0.3626 0.4024 0.3205 0.0390 -0.0313 -0.0349 152 VAL A CA 1088 C C . VAL A 136 ? 0.3639 0.4037 0.3219 0.0366 -0.0262 -0.0311 152 VAL A C 1089 O O . VAL A 136 ? 0.3620 0.4034 0.3227 0.0365 -0.0234 -0.0321 152 VAL A O 1090 C CB . VAL A 136 ? 0.3720 0.4120 0.3189 0.0402 -0.0340 -0.0322 152 VAL A CB 1091 C CG1 . VAL A 136 ? 0.3737 0.4162 0.3154 0.0404 -0.0317 -0.0310 152 VAL A CG1 1092 C CG2 . VAL A 136 ? 0.3705 0.4102 0.3164 0.0431 -0.0394 -0.0360 152 VAL A CG2 1093 N N . ILE A 137 ? 0.3526 0.3907 0.3080 0.0347 -0.0251 -0.0268 153 ILE A N 1094 C CA . ILE A 137 ? 0.3547 0.3928 0.3093 0.0326 -0.0207 -0.0230 153 ILE A CA 1095 C C . ILE A 137 ? 0.3485 0.3866 0.3116 0.0318 -0.0174 -0.0251 153 ILE A C 1096 O O . ILE A 137 ? 0.3387 0.3777 0.3015 0.0311 -0.0140 -0.0235 153 ILE A O 1097 C CB . ILE A 137 ? 0.3615 0.3977 0.3129 0.0309 -0.0206 -0.0188 153 ILE A CB 1098 C CG1 . ILE A 137 ? 0.3635 0.3996 0.3059 0.0315 -0.0232 -0.0161 153 ILE A CG1 1099 C CG2 . ILE A 137 ? 0.3538 0.3903 0.3050 0.0288 -0.0163 -0.0154 153 ILE A CG2 1100 C CD1 . ILE A 137 ? 0.3618 0.3999 0.2974 0.0312 -0.0212 -0.0133 153 ILE A CD1 1101 N N . SER A 138 ? 0.3489 0.3859 0.3197 0.0319 -0.0182 -0.0287 154 SER A N 1102 C CA . SER A 138 ? 0.3626 0.3989 0.3416 0.0310 -0.0148 -0.0306 154 SER A CA 1103 C C . SER A 138 ? 0.3671 0.4050 0.3506 0.0324 -0.0143 -0.0347 154 SER A C 1104 O O . SER A 138 ? 0.3597 0.3971 0.3481 0.0316 -0.0108 -0.0352 154 SER A O 1105 C CB . SER A 138 ? 0.3677 0.4022 0.3536 0.0302 -0.0152 -0.0329 154 SER A CB 1106 O OG . SER A 138 ? 0.4037 0.4386 0.3923 0.0320 -0.0194 -0.0372 154 SER A OG 1107 N N . LYS A 139 ? 0.3792 0.4188 0.3608 0.0345 -0.0179 -0.0376 155 LYS A N 1108 C CA . LYS A 139 ? 0.3914 0.4326 0.3784 0.0360 -0.0182 -0.0424 155 LYS A CA 1109 C C . LYS A 139 ? 0.3857 0.4295 0.3670 0.0374 -0.0185 -0.0421 155 LYS A C 1110 O O . LYS A 139 ? 0.3818 0.4266 0.3674 0.0379 -0.0166 -0.0445 155 LYS A O 1111 C CB . LYS A 139 ? 0.4165 0.4579 0.4087 0.0377 -0.0221 -0.0478 155 LYS A CB 1112 C CG . LYS A 139 ? 0.4531 0.4925 0.4541 0.0363 -0.0212 -0.0497 155 LYS A CG 1113 C CD . LYS A 139 ? 0.4949 0.5349 0.5021 0.0381 -0.0253 -0.0557 155 LYS A CD 1114 C CE . LYS A 139 ? 0.5139 0.5522 0.5303 0.0366 -0.0238 -0.0577 155 LYS A CE 1115 N NZ . LYS A 139 ? 0.5591 0.5983 0.5844 0.0382 -0.0268 -0.0645 155 LYS A NZ 1116 N N . SER A 140 ? 0.3834 0.4280 0.3552 0.0380 -0.0206 -0.0394 156 SER A N 1117 C CA . SER A 140 ? 0.3866 0.4338 0.3526 0.0393 -0.0208 -0.0393 156 SER A CA 1118 C C . SER A 140 ? 0.3800 0.4278 0.3454 0.0380 -0.0165 -0.0363 156 SER A C 1119 O O . SER A 140 ? 0.3606 0.4069 0.3252 0.0361 -0.0139 -0.0323 156 SER A O 1120 C CB . SER A 140 ? 0.3974 0.4449 0.3530 0.0400 -0.0236 -0.0365 156 SER A CB 1121 O OG . SER A 140 ? 0.4050 0.4552 0.3546 0.0410 -0.0234 -0.0362 156 SER A OG 1122 N N . ARG A 141 ? 0.3829 0.4330 0.3490 0.0392 -0.0157 -0.0386 157 ARG A N 1123 C CA . ARG A 141 ? 0.3937 0.4449 0.3583 0.0384 -0.0122 -0.0360 157 ARG A CA 1124 C C . ARG A 141 ? 0.3907 0.4450 0.3475 0.0396 -0.0131 -0.0355 157 ARG A C 1125 O O . ARG A 141 ? 0.4018 0.4580 0.3585 0.0398 -0.0110 -0.0355 157 ARG A O 1126 C CB . ARG A 141 ? 0.4030 0.4540 0.3764 0.0385 -0.0095 -0.0387 157 ARG A CB 1127 C CG . ARG A 141 ? 0.4233 0.4713 0.4053 0.0375 -0.0085 -0.0403 157 ARG A CG 1128 C CD . ARG A 141 ? 0.4370 0.4824 0.4178 0.0353 -0.0062 -0.0356 157 ARG A CD 1129 N NE . ARG A 141 ? 0.4483 0.4909 0.4375 0.0343 -0.0041 -0.0370 157 ARG A NE 1130 C CZ . ARG A 141 ? 0.4620 0.5023 0.4525 0.0328 -0.0037 -0.0355 157 ARG A CZ 1131 N NH1 . ARG A 141 ? 0.4635 0.5038 0.4477 0.0322 -0.0055 -0.0326 157 ARG A NH1 1132 N NH2 . ARG A 141 ? 0.4497 0.4877 0.4479 0.0318 -0.0013 -0.0370 157 ARG A NH2 1133 N N . ASP A 142 ? 0.3941 0.4487 0.3444 0.0404 -0.0163 -0.0352 158 ASP A N 1134 C CA . ASP A 142 ? 0.4005 0.4576 0.3421 0.0413 -0.0171 -0.0341 158 ASP A CA 1135 C C . ASP A 142 ? 0.3852 0.4414 0.3199 0.0394 -0.0156 -0.0283 158 ASP A C 1136 O O . ASP A 142 ? 0.3734 0.4275 0.3042 0.0389 -0.0175 -0.0262 158 ASP A O 1137 C CB . ASP A 142 ? 0.4200 0.4776 0.3579 0.0435 -0.0215 -0.0372 158 ASP A CB 1138 C CG . ASP A 142 ? 0.4557 0.5156 0.3834 0.0444 -0.0222 -0.0359 158 ASP A CG 1139 O OD1 . ASP A 142 ? 0.4661 0.5258 0.3875 0.0428 -0.0203 -0.0312 158 ASP A OD1 1140 O OD2 . ASP A 142 ? 0.4729 0.5345 0.3987 0.0466 -0.0248 -0.0397 158 ASP A OD2 1141 N N . HIS A 143 ? 0.3656 0.4233 0.2990 0.0383 -0.0123 -0.0259 159 HIS A N 1142 C CA . HIS A 143 ? 0.3612 0.4182 0.2899 0.0363 -0.0105 -0.0206 159 HIS A CA 1143 C C . HIS A 143 ? 0.3616 0.4186 0.2809 0.0363 -0.0122 -0.0181 159 HIS A C 1144 O O . HIS A 143 ? 0.3649 0.4201 0.2814 0.0347 -0.0120 -0.0143 159 HIS A O 1145 C CB . HIS A 143 ? 0.3604 0.4194 0.2899 0.0355 -0.0069 -0.0190 159 HIS A CB 1146 C CG . HIS A 143 ? 0.3648 0.4275 0.2916 0.0368 -0.0065 -0.0210 159 HIS A CG 1147 N ND1 . HIS A 143 ? 0.3712 0.4360 0.2907 0.0363 -0.0055 -0.0186 159 HIS A ND1 1148 C CD2 . HIS A 143 ? 0.3654 0.4300 0.2960 0.0385 -0.0066 -0.0253 159 HIS A CD2 1149 C CE1 . HIS A 143 ? 0.3682 0.4362 0.2868 0.0377 -0.0052 -0.0214 159 HIS A CE1 1150 N NE2 . HIS A 143 ? 0.3685 0.4365 0.2939 0.0391 -0.0059 -0.0256 159 HIS A NE2 1151 N N . GLU A 144 ? 0.3543 0.4131 0.2689 0.0380 -0.0140 -0.0203 160 GLU A N 1152 C CA . GLU A 144 ? 0.3549 0.4133 0.2602 0.0380 -0.0156 -0.0177 160 GLU A CA 1153 C C . GLU A 144 ? 0.3343 0.3893 0.2387 0.0386 -0.0193 -0.0178 160 GLU A C 1154 O O . GLU A 144 ? 0.3302 0.3832 0.2286 0.0378 -0.0201 -0.0142 160 GLU A O 1155 C CB . GLU A 144 ? 0.3879 0.4493 0.2871 0.0396 -0.0159 -0.0196 160 GLU A CB 1156 C CG . GLU A 144 ? 0.4195 0.4842 0.3187 0.0387 -0.0120 -0.0187 160 GLU A CG 1157 C CD . GLU A 144 ? 0.4605 0.5280 0.3514 0.0394 -0.0114 -0.0187 160 GLU A CD 1158 O OE1 . GLU A 144 ? 0.4965 0.5639 0.3822 0.0412 -0.0142 -0.0206 160 GLU A OE1 1159 O OE2 . GLU A 144 ? 0.4823 0.5522 0.3720 0.0381 -0.0081 -0.0169 160 GLU A OE2 1160 N N . GLU A 145 ? 0.3180 0.3724 0.2290 0.0401 -0.0215 -0.0220 161 GLU A N 1161 C CA . GLU A 145 ? 0.3221 0.3735 0.2336 0.0408 -0.0252 -0.0228 161 GLU A CA 1162 C C . GLU A 145 ? 0.3150 0.3636 0.2291 0.0385 -0.0240 -0.0192 161 GLU A C 1163 O O . GLU A 145 ? 0.3168 0.3629 0.2269 0.0382 -0.0261 -0.0168 161 GLU A O 1164 C CB . GLU A 145 ? 0.3295 0.3812 0.2490 0.0427 -0.0275 -0.0286 161 GLU A CB 1165 C CG . GLU A 145 ? 0.3460 0.3949 0.2675 0.0435 -0.0314 -0.0299 161 GLU A CG 1166 C CD . GLU A 145 ? 0.3614 0.4110 0.2915 0.0453 -0.0336 -0.0361 161 GLU A CD 1167 O OE1 . GLU A 145 ? 0.3601 0.4111 0.2979 0.0448 -0.0310 -0.0385 161 GLU A OE1 1168 O OE2 . GLU A 145 ? 0.3761 0.4247 0.3054 0.0472 -0.0380 -0.0386 161 GLU A OE2 1169 N N . LEU A 146 ? 0.3027 0.3518 0.2232 0.0370 -0.0207 -0.0189 162 LEU A N 1170 C CA . LEU A 146 ? 0.3022 0.3491 0.2254 0.0348 -0.0191 -0.0157 162 LEU A CA 1171 C C . LEU A 146 ? 0.3076 0.3539 0.2233 0.0332 -0.0181 -0.0105 162 LEU A C 1172 O O . LEU A 146 ? 0.3132 0.3569 0.2283 0.0322 -0.0191 -0.0082 162 LEU A O 1173 C CB . LEU A 146 ? 0.2880 0.3357 0.2180 0.0338 -0.0155 -0.0162 162 LEU A CB 1174 C CG . LEU A 146 ? 0.2841 0.3314 0.2231 0.0347 -0.0158 -0.0208 162 LEU A CG 1175 C CD1 . LEU A 146 ? 0.2702 0.3185 0.2144 0.0341 -0.0121 -0.0211 162 LEU A CD1 1176 C CD2 . LEU A 146 ? 0.2725 0.3170 0.2163 0.0341 -0.0172 -0.0214 162 LEU A CD2 1177 N N . ALA A 147 ? 0.3044 0.3531 0.2148 0.0331 -0.0162 -0.0090 163 ALA A N 1178 C CA . ALA A 147 ? 0.3035 0.3519 0.2072 0.0314 -0.0149 -0.0044 163 ALA A CA 1179 C C . ALA A 147 ? 0.3176 0.3637 0.2143 0.0320 -0.0180 -0.0029 163 ALA A C 1180 O O . ALA A 147 ? 0.3171 0.3612 0.2108 0.0305 -0.0177 0.0008 163 ALA A O 1181 C CB . ALA A 147 ? 0.2993 0.3513 0.1996 0.0312 -0.0121 -0.0037 163 ALA A CB 1182 N N . TYR A 148 ? 0.3238 0.3700 0.2181 0.0344 -0.0209 -0.0059 164 TYR A N 1183 C CA . TYR A 148 ? 0.3352 0.3787 0.2230 0.0354 -0.0245 -0.0048 164 TYR A CA 1184 C C . TYR A 148 ? 0.3263 0.3661 0.2175 0.0348 -0.0266 -0.0038 164 TYR A C 1185 O O . TYR A 148 ? 0.3259 0.3630 0.2122 0.0339 -0.0273 -0.0001 164 TYR A O 1186 C CB . TYR A 148 ? 0.3451 0.3895 0.2309 0.0384 -0.0278 -0.0090 164 TYR A CB 1187 C CG . TYR A 148 ? 0.3611 0.4022 0.2412 0.0400 -0.0322 -0.0085 164 TYR A CG 1188 C CD1 . TYR A 148 ? 0.3736 0.4134 0.2428 0.0402 -0.0326 -0.0051 164 TYR A CD1 1189 C CD2 . TYR A 148 ? 0.3618 0.4009 0.2472 0.0414 -0.0359 -0.0114 164 TYR A CD2 1190 C CE1 . TYR A 148 ? 0.3832 0.4194 0.2467 0.0418 -0.0368 -0.0042 164 TYR A CE1 1191 C CE2 . TYR A 148 ? 0.3710 0.4070 0.2514 0.0431 -0.0403 -0.0110 164 TYR A CE2 1192 C CZ . TYR A 148 ? 0.3850 0.4193 0.2542 0.0434 -0.0409 -0.0073 164 TYR A CZ 1193 O OH . TYR A 148 ? 0.3950 0.4256 0.2587 0.0452 -0.0454 -0.0066 164 TYR A OH 1194 N N . TYR A 149 ? 0.3212 0.3608 0.2211 0.0353 -0.0275 -0.0073 165 TYR A N 1195 C CA . TYR A 149 ? 0.3142 0.3507 0.2183 0.0349 -0.0297 -0.0072 165 TYR A CA 1196 C C . TYR A 149 ? 0.3046 0.3400 0.2099 0.0322 -0.0269 -0.0032 165 TYR A C 1197 O O . TYR A 149 ? 0.2933 0.3258 0.1980 0.0315 -0.0286 -0.0013 165 TYR A O 1198 C CB . TYR A 149 ? 0.3135 0.3504 0.2271 0.0360 -0.0308 -0.0122 165 TYR A CB 1199 C CG . TYR A 149 ? 0.3241 0.3612 0.2370 0.0390 -0.0351 -0.0165 165 TYR A CG 1200 C CD1 . TYR A 149 ? 0.3339 0.3683 0.2434 0.0404 -0.0395 -0.0164 165 TYR A CD1 1201 C CD2 . TYR A 149 ? 0.3299 0.3699 0.2457 0.0405 -0.0348 -0.0207 165 TYR A CD2 1202 C CE1 . TYR A 149 ? 0.3435 0.3781 0.2521 0.0434 -0.0437 -0.0204 165 TYR A CE1 1203 C CE2 . TYR A 149 ? 0.3345 0.3749 0.2498 0.0434 -0.0389 -0.0249 165 TYR A CE2 1204 C CZ . TYR A 149 ? 0.3433 0.3811 0.2549 0.0448 -0.0434 -0.0248 165 TYR A CZ 1205 O OH . TYR A 149 ? 0.3458 0.3839 0.2566 0.0479 -0.0479 -0.0291 165 TYR A OH 1206 N N . TRP A 150 ? 0.3048 0.3426 0.2119 0.0307 -0.0229 -0.0021 166 TRP A N 1207 C CA . TRP A 150 ? 0.2978 0.3351 0.2056 0.0282 -0.0202 0.0014 166 TRP A CA 1208 C C . TRP A 150 ? 0.3113 0.3470 0.2113 0.0273 -0.0206 0.0056 166 TRP A C 1209 O O . TRP A 150 ? 0.3108 0.3441 0.2112 0.0260 -0.0212 0.0079 166 TRP A O 1210 C CB . TRP A 150 ? 0.2923 0.3326 0.2023 0.0272 -0.0162 0.0017 166 TRP A CB 1211 C CG . TRP A 150 ? 0.2776 0.3176 0.1894 0.0249 -0.0137 0.0048 166 TRP A CG 1212 C CD1 . TRP A 150 ? 0.2760 0.3157 0.1943 0.0241 -0.0122 0.0041 166 TRP A CD1 1213 C CD2 . TRP A 150 ? 0.2773 0.3173 0.1844 0.0232 -0.0123 0.0088 166 TRP A CD2 1214 N NE1 . TRP A 150 ? 0.2700 0.3096 0.1877 0.0222 -0.0103 0.0073 166 TRP A NE1 1215 C CE2 . TRP A 150 ? 0.2702 0.3101 0.1814 0.0216 -0.0103 0.0101 166 TRP A CE2 1216 C CE3 . TRP A 150 ? 0.2745 0.3145 0.1742 0.0229 -0.0124 0.0113 166 TRP A CE3 1217 C CZ2 . TRP A 150 ? 0.2701 0.3102 0.1790 0.0197 -0.0088 0.0136 166 TRP A CZ2 1218 C CZ3 . TRP A 150 ? 0.2741 0.3140 0.1715 0.0208 -0.0105 0.0150 166 TRP A CZ3 1219 C CH2 . TRP A 150 ? 0.2708 0.3109 0.1732 0.0193 -0.0088 0.0159 166 TRP A CH2 1220 N N . ARG A 151 ? 0.3237 0.3607 0.2167 0.0279 -0.0203 0.0065 167 ARG A N 1221 C CA . ARG A 151 ? 0.3473 0.3829 0.2326 0.0269 -0.0200 0.0107 167 ARG A CA 1222 C C . ARG A 151 ? 0.3494 0.3807 0.2313 0.0278 -0.0240 0.0116 167 ARG A C 1223 O O . ARG A 151 ? 0.3387 0.3675 0.2180 0.0263 -0.0239 0.0152 167 ARG A O 1224 C CB . ARG A 151 ? 0.3679 0.4059 0.2464 0.0273 -0.0183 0.0113 167 ARG A CB 1225 C CG . ARG A 151 ? 0.4025 0.4393 0.2736 0.0256 -0.0169 0.0159 167 ARG A CG 1226 C CD . ARG A 151 ? 0.4369 0.4749 0.2995 0.0267 -0.0165 0.0161 167 ARG A CD 1227 N NE . ARG A 151 ? 0.4707 0.5131 0.3334 0.0259 -0.0126 0.0158 167 ARG A NE 1228 C CZ . ARG A 151 ? 0.5002 0.5440 0.3618 0.0235 -0.0090 0.0188 167 ARG A CZ 1229 N NH1 . ARG A 151 ? 0.5233 0.5642 0.3836 0.0216 -0.0086 0.0225 167 ARG A NH1 1230 N NH2 . ARG A 151 ? 0.4891 0.5371 0.3512 0.0230 -0.0058 0.0179 167 ARG A NH2 1231 N N . GLU A 152 ? 0.3592 0.3898 0.2416 0.0303 -0.0275 0.0082 168 GLU A N 1232 C CA . GLU A 152 ? 0.3718 0.3985 0.2510 0.0317 -0.0319 0.0087 168 GLU A CA 1233 C C . GLU A 152 ? 0.3551 0.3793 0.2404 0.0305 -0.0327 0.0093 168 GLU A C 1234 O O . GLU A 152 ? 0.3553 0.3760 0.2372 0.0298 -0.0341 0.0124 168 GLU A O 1235 C CB . GLU A 152 ? 0.3849 0.4117 0.2642 0.0349 -0.0358 0.0042 168 GLU A CB 1236 C CG . GLU A 152 ? 0.4124 0.4411 0.2839 0.0364 -0.0357 0.0038 168 GLU A CG 1237 C CD . GLU A 152 ? 0.4344 0.4605 0.2950 0.0360 -0.0357 0.0085 168 GLU A CD 1238 O OE1 . GLU A 152 ? 0.4555 0.4776 0.3121 0.0372 -0.0394 0.0097 168 GLU A OE1 1239 O OE2 . GLU A 152 ? 0.4381 0.4661 0.2945 0.0343 -0.0318 0.0112 168 GLU A OE2 1240 N N . PHE A 153 ? 0.3394 0.3651 0.2336 0.0300 -0.0317 0.0063 169 PHE A N 1241 C CA . PHE A 153 ? 0.3299 0.3538 0.2304 0.0289 -0.0322 0.0064 169 PHE A CA 1242 C C . PHE A 153 ? 0.3260 0.3491 0.2251 0.0262 -0.0295 0.0108 169 PHE A C 1243 O O . PHE A 153 ? 0.3315 0.3514 0.2301 0.0256 -0.0313 0.0127 169 PHE A O 1244 C CB . PHE A 153 ? 0.3181 0.3438 0.2281 0.0288 -0.0311 0.0025 169 PHE A CB 1245 C CG . PHE A 153 ? 0.3129 0.3367 0.2293 0.0278 -0.0317 0.0021 169 PHE A CG 1246 C CD1 . PHE A 153 ? 0.3158 0.3370 0.2340 0.0291 -0.0359 0.0004 169 PHE A CD1 1247 C CD2 . PHE A 153 ? 0.3114 0.3361 0.2316 0.0255 -0.0282 0.0036 169 PHE A CD2 1248 C CE1 . PHE A 153 ? 0.3177 0.3372 0.2418 0.0281 -0.0364 0.0000 169 PHE A CE1 1249 C CE2 . PHE A 153 ? 0.3096 0.3326 0.2353 0.0245 -0.0287 0.0032 169 PHE A CE2 1250 C CZ . PHE A 153 ? 0.3077 0.3282 0.2354 0.0258 -0.0326 0.0013 169 PHE A CZ 1251 N N . TYR A 154 ? 0.3120 0.3380 0.2107 0.0246 -0.0255 0.0123 170 TYR A N 1252 C CA . TYR A 154 ? 0.3055 0.3313 0.2035 0.0221 -0.0229 0.0160 170 TYR A CA 1253 C C . TYR A 154 ? 0.3099 0.3330 0.2004 0.0216 -0.0238 0.0199 170 TYR A C 1254 O O . TYR A 154 ? 0.3115 0.3325 0.2025 0.0200 -0.0237 0.0223 170 TYR A O 1255 C CB . TYR A 154 ? 0.2927 0.3222 0.1917 0.0208 -0.0187 0.0165 170 TYR A CB 1256 C CG . TYR A 154 ? 0.2853 0.3164 0.1921 0.0203 -0.0170 0.0143 170 TYR A CG 1257 C CD1 . TYR A 154 ? 0.2813 0.3135 0.1926 0.0219 -0.0175 0.0105 170 TYR A CD1 1258 C CD2 . TYR A 154 ? 0.2796 0.3111 0.1893 0.0183 -0.0148 0.0161 170 TYR A CD2 1259 C CE1 . TYR A 154 ? 0.2745 0.3076 0.1925 0.0213 -0.0157 0.0089 170 TYR A CE1 1260 C CE2 . TYR A 154 ? 0.2741 0.3067 0.1900 0.0180 -0.0132 0.0144 170 TYR A CE2 1261 C CZ . TYR A 154 ? 0.2761 0.3093 0.1959 0.0194 -0.0135 0.0109 170 TYR A CZ 1262 O OH . TYR A 154 ? 0.2679 0.3018 0.1935 0.0190 -0.0116 0.0095 170 TYR A OH 1263 N N . ASP A 155 ? 0.3167 0.3396 0.1999 0.0229 -0.0247 0.0204 171 ASP A N 1264 C CA . ASP A 155 ? 0.3250 0.3447 0.2006 0.0224 -0.0254 0.0244 171 ASP A CA 1265 C C . ASP A 155 ? 0.3268 0.3418 0.2031 0.0231 -0.0294 0.0249 171 ASP A C 1266 O O . ASP A 155 ? 0.3277 0.3397 0.2013 0.0217 -0.0294 0.0284 171 ASP A O 1267 C CB . ASP A 155 ? 0.3399 0.3599 0.2068 0.0239 -0.0257 0.0247 171 ASP A CB 1268 C CG . ASP A 155 ? 0.3493 0.3738 0.2147 0.0228 -0.0214 0.0250 171 ASP A CG 1269 O OD1 . ASP A 155 ? 0.3440 0.3710 0.2142 0.0208 -0.0181 0.0256 171 ASP A OD1 1270 O OD2 . ASP A 155 ? 0.3569 0.3826 0.2163 0.0242 -0.0213 0.0245 171 ASP A OD2 1271 N N . LYS A 156 ? 0.3319 0.3463 0.2122 0.0252 -0.0328 0.0211 172 LYS A N 1272 C CA . LYS A 156 ? 0.3447 0.3548 0.2256 0.0264 -0.0372 0.0210 172 LYS A CA 1273 C C . LYS A 156 ? 0.3374 0.3467 0.2266 0.0250 -0.0373 0.0203 172 LYS A C 1274 O O . LYS A 156 ? 0.3400 0.3455 0.2289 0.0247 -0.0394 0.0222 172 LYS A O 1275 C CB . LYS A 156 ? 0.3619 0.3718 0.2432 0.0296 -0.0413 0.0169 172 LYS A CB 1276 C CG . LYS A 156 ? 0.3840 0.3930 0.2555 0.0317 -0.0429 0.0178 172 LYS A CG 1277 C CD . LYS A 156 ? 0.4104 0.4206 0.2837 0.0348 -0.0464 0.0128 172 LYS A CD 1278 C CE . LYS A 156 ? 0.4382 0.4461 0.3015 0.0374 -0.0497 0.0135 172 LYS A CE 1279 N NZ . LYS A 156 ? 0.4599 0.4703 0.3159 0.0370 -0.0464 0.0152 172 LYS A NZ 1280 N N . ALA A 157 ? 0.3238 0.3364 0.2204 0.0242 -0.0350 0.0177 173 ALA A N 1281 C CA . ALA A 157 ? 0.3140 0.3263 0.2185 0.0229 -0.0346 0.0166 173 ALA A CA 1282 C C . ALA A 157 ? 0.3134 0.3264 0.2181 0.0200 -0.0311 0.0200 173 ALA A C 1283 O O . ALA A 157 ? 0.3166 0.3283 0.2256 0.0188 -0.0312 0.0203 173 ALA A O 1284 C CB . ALA A 157 ? 0.3069 0.3220 0.2189 0.0234 -0.0338 0.0122 173 ALA A CB 1285 N N . GLY A 158 ? 0.3059 0.3212 0.2062 0.0191 -0.0279 0.0220 174 GLY A N 1286 C CA . GLY A 158 ? 0.3052 0.3218 0.2059 0.0165 -0.0245 0.0248 174 GLY A CA 1287 C C . GLY A 158 ? 0.3156 0.3298 0.2099 0.0154 -0.0242 0.0291 174 GLY A C 1288 O O . GLY A 158 ? 0.3147 0.3261 0.2101 0.0143 -0.0251 0.0309 174 GLY A O 1289 N N . THR A 159 ? 0.3260 0.3412 0.2138 0.0156 -0.0228 0.0306 175 THR A N 1290 C CA . THR A 159 ? 0.3335 0.3468 0.2151 0.0141 -0.0215 0.0348 175 THR A CA 1291 C C . THR A 159 ? 0.3485 0.3562 0.2272 0.0145 -0.0248 0.0370 175 THR A C 1292 O O . THR A 159 ? 0.3525 0.3581 0.2300 0.0126 -0.0237 0.0403 175 THR A O 1293 C CB . THR A 159 ? 0.3323 0.3475 0.2068 0.0146 -0.0197 0.0357 175 THR A CB 1294 O OG1 . THR A 159 ? 0.3218 0.3420 0.1995 0.0144 -0.0168 0.0336 175 THR A OG1 1295 C CG2 . THR A 159 ? 0.3353 0.3489 0.2039 0.0126 -0.0174 0.0402 175 THR A CG2 1296 N N . ALA A 160 ? 0.3614 0.3669 0.2399 0.0170 -0.0289 0.0349 176 ALA A N 1297 C CA . ALA A 160 ? 0.3743 0.3742 0.2493 0.0180 -0.0327 0.0367 176 ALA A CA 1298 C C . ALA A 160 ? 0.3690 0.3664 0.2493 0.0164 -0.0333 0.0378 176 ALA A C 1299 O O . ALA A 160 ? 0.3686 0.3612 0.2456 0.0165 -0.0355 0.0405 176 ALA A O 1300 C CB . ALA A 160 ? 0.3725 0.3713 0.2475 0.0213 -0.0372 0.0334 176 ALA A CB 1301 N N . VAL A 161 ? 0.3606 0.3611 0.2488 0.0150 -0.0315 0.0358 177 VAL A N 1302 C CA . VAL A 161 ? 0.3666 0.3652 0.2604 0.0136 -0.0322 0.0363 177 VAL A CA 1303 C C . VAL A 161 ? 0.3683 0.3688 0.2645 0.0106 -0.0282 0.0383 177 VAL A C 1304 O O . VAL A 161 ? 0.3670 0.3671 0.2692 0.0094 -0.0285 0.0377 177 VAL A O 1305 C CB . VAL A 161 ? 0.3572 0.3565 0.2592 0.0147 -0.0344 0.0320 177 VAL A CB 1306 C CG1 . VAL A 161 ? 0.3586 0.3550 0.2592 0.0176 -0.0390 0.0301 177 VAL A CG1 1307 C CG2 . VAL A 161 ? 0.3439 0.3484 0.2505 0.0144 -0.0315 0.0290 177 VAL A CG2 1308 N N A ARG A 162 ? 0.3745 0.3771 0.2663 0.0093 -0.0248 0.0405 178 ARG A N 1309 N N B ARG A 162 ? 0.3691 0.3718 0.2609 0.0093 -0.0248 0.0405 178 ARG A N 1310 C CA A ARG A 162 ? 0.3760 0.3810 0.2705 0.0066 -0.0212 0.0420 178 ARG A CA 1311 C CA B ARG A 162 ? 0.3664 0.3714 0.2604 0.0066 -0.0211 0.0422 178 ARG A CA 1312 C C A ARG A 162 ? 0.3776 0.3790 0.2740 0.0049 -0.0219 0.0443 178 ARG A C 1313 C C B ARG A 162 ? 0.3720 0.3734 0.2681 0.0049 -0.0217 0.0444 178 ARG A C 1314 O O A ARG A 162 ? 0.3601 0.3631 0.2629 0.0034 -0.0209 0.0433 178 ARG A O 1315 O O B ARG A 162 ? 0.3557 0.3590 0.2582 0.0034 -0.0206 0.0434 178 ARG A O 1316 C CB A ARG A 162 ? 0.3864 0.3938 0.2756 0.0055 -0.0176 0.0442 178 ARG A CB 1317 C CB B ARG A 162 ? 0.3688 0.3756 0.2567 0.0056 -0.0178 0.0445 178 ARG A CB 1318 C CG A ARG A 162 ? 0.3895 0.3993 0.2820 0.0027 -0.0141 0.0454 178 ARG A CG 1319 C CG B ARG A 162 ? 0.3623 0.3710 0.2521 0.0027 -0.0141 0.0466 178 ARG A CG 1320 C CD A ARG A 162 ? 0.3938 0.4046 0.2807 0.0013 -0.0108 0.0483 178 ARG A CD 1321 C CD B ARG A 162 ? 0.3477 0.3613 0.2445 0.0019 -0.0122 0.0440 178 ARG A CD 1322 N NE A ARG A 162 ? 0.4000 0.4150 0.2848 0.0023 -0.0090 0.0467 178 ARG A NE 1323 N NE B ARG A 162 ? 0.3398 0.3550 0.2393 -0.0006 -0.0094 0.0455 178 ARG A NE 1324 C CZ A ARG A 162 ? 0.3921 0.4122 0.2803 0.0013 -0.0060 0.0455 178 ARG A CZ 1325 C CZ B ARG A 162 ? 0.3307 0.3504 0.2310 -0.0017 -0.0060 0.0453 178 ARG A CZ 1326 N NH1 A ARG A 162 ? 0.3936 0.4152 0.2873 -0.0005 -0.0045 0.0455 178 ARG A NH1 1327 N NH1 B ARG A 162 ? 0.3268 0.3499 0.2252 -0.0004 -0.0049 0.0438 178 ARG A NH1 1328 N NH2 A ARG A 162 ? 0.3850 0.4086 0.2712 0.0024 -0.0046 0.0440 178 ARG A NH2 1329 N NH2 B ARG A 162 ? 0.3278 0.3489 0.2312 -0.0040 -0.0039 0.0463 178 ARG A NH2 1330 N N . SER A 163 ? 0.3859 0.3822 0.2768 0.0052 -0.0236 0.0473 179 SER A N 1331 C CA . SER A 163 ? 0.4026 0.3950 0.2953 0.0035 -0.0242 0.0498 179 SER A CA 1332 C C . SER A 163 ? 0.3905 0.3817 0.2907 0.0041 -0.0272 0.0472 179 SER A C 1333 O O . SER A 163 ? 0.3775 0.3688 0.2830 0.0022 -0.0263 0.0473 179 SER A O 1334 C CB . SER A 163 ? 0.4293 0.4159 0.3140 0.0038 -0.0253 0.0539 179 SER A CB 1335 O OG . SER A 163 ? 0.4732 0.4566 0.3543 0.0068 -0.0295 0.0531 179 SER A OG 1336 N N . GLN A 164 ? 0.3869 0.3774 0.2880 0.0066 -0.0305 0.0444 180 GLN A N 1337 C CA . GLN A 164 ? 0.3804 0.3705 0.2891 0.0072 -0.0331 0.0412 180 GLN A CA 1338 C C . GLN A 164 ? 0.3622 0.3575 0.2776 0.0059 -0.0303 0.0385 180 GLN A C 1339 O O . GLN A 164 ? 0.3517 0.3470 0.2733 0.0048 -0.0305 0.0374 180 GLN A O 1340 C CB . GLN A 164 ? 0.3928 0.3818 0.3015 0.0102 -0.0369 0.0383 180 GLN A CB 1341 C CG . GLN A 164 ? 0.4226 0.4057 0.3254 0.0121 -0.0408 0.0404 180 GLN A CG 1342 C CD . GLN A 164 ? 0.4490 0.4320 0.3429 0.0134 -0.0405 0.0421 180 GLN A CD 1343 O OE1 . GLN A 164 ? 0.4444 0.4312 0.3358 0.0124 -0.0368 0.0427 180 GLN A OE1 1344 N NE2 . GLN A 164 ? 0.4674 0.4459 0.3562 0.0159 -0.0446 0.0428 180 GLN A NE2 1345 N N . PHE A 165 ? 0.3470 0.3467 0.2612 0.0060 -0.0277 0.0374 181 PHE A N 1346 C CA . PHE A 165 ? 0.3306 0.3351 0.2505 0.0049 -0.0250 0.0351 181 PHE A CA 1347 C C . PHE A 165 ? 0.3351 0.3406 0.2570 0.0023 -0.0225 0.0369 181 PHE A C 1348 O O . PHE A 165 ? 0.3236 0.3309 0.2514 0.0014 -0.0219 0.0350 181 PHE A O 1349 C CB . PHE A 165 ? 0.3180 0.3266 0.2358 0.0056 -0.0227 0.0339 181 PHE A CB 1350 C CG . PHE A 165 ? 0.3017 0.3144 0.2252 0.0051 -0.0206 0.0311 181 PHE A CG 1351 C CD1 . PHE A 165 ? 0.2919 0.3050 0.2198 0.0064 -0.0219 0.0277 181 PHE A CD1 1352 C CD2 . PHE A 165 ? 0.2945 0.3105 0.2189 0.0034 -0.0174 0.0320 181 PHE A CD2 1353 C CE1 . PHE A 165 ? 0.2906 0.3070 0.2230 0.0060 -0.0198 0.0255 181 PHE A CE1 1354 C CE2 . PHE A 165 ? 0.2900 0.3094 0.2189 0.0032 -0.0157 0.0297 181 PHE A CE2 1355 C CZ . PHE A 165 ? 0.2818 0.3012 0.2143 0.0045 -0.0168 0.0266 181 PHE A CZ 1356 N N . GLU A 166 ? 0.3525 0.3569 0.2696 0.0011 -0.0211 0.0404 182 GLU A N 1357 C CA . GLU A 166 ? 0.3689 0.3740 0.2881 -0.0013 -0.0188 0.0422 182 GLU A CA 1358 C C . GLU A 166 ? 0.3564 0.3585 0.2807 -0.0021 -0.0208 0.0419 182 GLU A C 1359 O O . GLU A 166 ? 0.3478 0.3523 0.2776 -0.0036 -0.0194 0.0408 182 GLU A O 1360 C CB . GLU A 166 ? 0.3936 0.3972 0.3067 -0.0025 -0.0169 0.0460 182 GLU A CB 1361 C CG . GLU A 166 ? 0.4319 0.4401 0.3420 -0.0027 -0.0137 0.0460 182 GLU A CG 1362 C CD . GLU A 166 ? 0.4732 0.4802 0.3777 -0.0041 -0.0113 0.0496 182 GLU A CD 1363 O OE1 . GLU A 166 ? 0.4982 0.5013 0.4020 -0.0055 -0.0115 0.0523 182 GLU A OE1 1364 O OE2 . GLU A 166 ? 0.4913 0.5014 0.3922 -0.0039 -0.0090 0.0498 182 GLU A OE2 1365 N N . ARG A 167 ? 0.3609 0.3579 0.2838 -0.0009 -0.0242 0.0428 183 ARG A N 1366 C CA . ARG A 167 ? 0.3562 0.3500 0.2842 -0.0014 -0.0265 0.0423 183 ARG A CA 1367 C C . ARG A 167 ? 0.3436 0.3400 0.2786 -0.0007 -0.0275 0.0379 183 ARG A C 1368 O O . ARG A 167 ? 0.3360 0.3327 0.2769 -0.0019 -0.0276 0.0368 183 ARG A O 1369 C CB . ARG A 167 ? 0.3720 0.3593 0.2963 0.0000 -0.0302 0.0443 183 ARG A CB 1370 C CG . ARG A 167 ? 0.3829 0.3665 0.3124 -0.0006 -0.0325 0.0443 183 ARG A CG 1371 C CD . ARG A 167 ? 0.3945 0.3771 0.3247 -0.0034 -0.0302 0.0473 183 ARG A CD 1372 N NE . ARG A 167 ? 0.4146 0.3933 0.3500 -0.0039 -0.0325 0.0472 183 ARG A NE 1373 C CZ . ARG A 167 ? 0.4144 0.3947 0.3564 -0.0059 -0.0312 0.0462 183 ARG A CZ 1374 N NH1 . ARG A 167 ? 0.4113 0.3971 0.3553 -0.0076 -0.0276 0.0452 183 ARG A NH1 1375 N NH2 . ARG A 167 ? 0.4223 0.3987 0.3688 -0.0062 -0.0336 0.0461 183 ARG A NH2 1376 N N . TYR A 168 ? 0.3305 0.3288 0.2651 0.0010 -0.0281 0.0355 184 TYR A N 1377 C CA . TYR A 168 ? 0.3212 0.3223 0.2621 0.0015 -0.0283 0.0313 184 TYR A CA 1378 C C . TYR A 168 ? 0.3123 0.3178 0.2567 -0.0002 -0.0250 0.0304 184 TYR A C 1379 O O . TYR A 168 ? 0.3080 0.3143 0.2581 -0.0008 -0.0253 0.0282 184 TYR A O 1380 C CB . TYR A 168 ? 0.3160 0.3185 0.2554 0.0036 -0.0288 0.0291 184 TYR A CB 1381 C CG . TYR A 168 ? 0.3052 0.3120 0.2492 0.0036 -0.0269 0.0256 184 TYR A CG 1382 C CD1 . TYR A 168 ? 0.3003 0.3072 0.2508 0.0038 -0.0280 0.0223 184 TYR A CD1 1383 C CD2 . TYR A 168 ? 0.3019 0.3125 0.2435 0.0036 -0.0239 0.0257 184 TYR A CD2 1384 C CE1 . TYR A 168 ? 0.2897 0.3001 0.2436 0.0038 -0.0259 0.0194 184 TYR A CE1 1385 C CE2 . TYR A 168 ? 0.2935 0.3074 0.2386 0.0037 -0.0220 0.0229 184 TYR A CE2 1386 C CZ . TYR A 168 ? 0.2874 0.3011 0.2384 0.0038 -0.0229 0.0199 184 TYR A CZ 1387 O OH . TYR A 168 ? 0.2878 0.3045 0.2417 0.0039 -0.0208 0.0174 184 TYR A OH 1388 N N . VAL A 169 ? 0.3067 0.3152 0.2475 -0.0009 -0.0220 0.0320 185 VAL A N 1389 C CA . VAL A 169 ? 0.3019 0.3148 0.2457 -0.0024 -0.0191 0.0312 185 VAL A CA 1390 C C . VAL A 169 ? 0.3042 0.3162 0.2518 -0.0042 -0.0193 0.0318 185 VAL A C 1391 O O . VAL A 169 ? 0.2977 0.3120 0.2503 -0.0049 -0.0187 0.0296 185 VAL A O 1392 C CB . VAL A 169 ? 0.2978 0.3139 0.2372 -0.0027 -0.0162 0.0327 185 VAL A CB 1393 C CG1 . VAL A 169 ? 0.2957 0.3160 0.2382 -0.0042 -0.0136 0.0321 185 VAL A CG1 1394 C CG2 . VAL A 169 ? 0.2874 0.3051 0.2246 -0.0009 -0.0159 0.0312 185 VAL A CG2 1395 N N . GLU A 170 ? 0.3130 0.3213 0.2582 -0.0051 -0.0199 0.0349 186 GLU A N 1396 C CA . GLU A 170 ? 0.3292 0.3359 0.2784 -0.0069 -0.0202 0.0357 186 GLU A CA 1397 C C . GLU A 170 ? 0.3169 0.3222 0.2722 -0.0065 -0.0228 0.0329 186 GLU A C 1398 O O . GLU A 170 ? 0.3249 0.3322 0.2854 -0.0077 -0.0221 0.0312 186 GLU A O 1399 C CB . GLU A 170 ? 0.3479 0.3498 0.2930 -0.0076 -0.0208 0.0397 186 GLU A CB 1400 C CG . GLU A 170 ? 0.3825 0.3862 0.3232 -0.0089 -0.0175 0.0423 186 GLU A CG 1401 C CD . GLU A 170 ? 0.4186 0.4173 0.3545 -0.0097 -0.0177 0.0465 186 GLU A CD 1402 O OE1 . GLU A 170 ? 0.4271 0.4204 0.3621 -0.0089 -0.0206 0.0476 186 GLU A OE1 1403 O OE2 . GLU A 170 ? 0.4469 0.4469 0.3800 -0.0112 -0.0147 0.0487 186 GLU A OE2 1404 N N . LEU A 171 ? 0.3118 0.3138 0.2666 -0.0048 -0.0257 0.0322 187 LEU A N 1405 C CA . LEU A 171 ? 0.3094 0.3098 0.2702 -0.0043 -0.0283 0.0294 187 LEU A CA 1406 C C . LEU A 171 ? 0.3009 0.3057 0.2661 -0.0039 -0.0272 0.0253 187 LEU A C 1407 O O . LEU A 171 ? 0.3040 0.3096 0.2751 -0.0045 -0.0277 0.0228 187 LEU A O 1408 C CB . LEU A 171 ? 0.3206 0.3161 0.2799 -0.0024 -0.0320 0.0297 187 LEU A CB 1409 C CG . LEU A 171 ? 0.3292 0.3192 0.2849 -0.0028 -0.0335 0.0338 187 LEU A CG 1410 C CD1 . LEU A 171 ? 0.3310 0.3165 0.2828 -0.0005 -0.0370 0.0345 187 LEU A CD1 1411 C CD2 . LEU A 171 ? 0.3337 0.3217 0.2951 -0.0043 -0.0343 0.0337 187 LEU A CD2 1412 N N . ASN A 172 ? 0.2878 0.2955 0.2500 -0.0030 -0.0256 0.0246 188 ASN A N 1413 C CA . ASN A 172 ? 0.2792 0.2910 0.2446 -0.0027 -0.0239 0.0212 188 ASN A CA 1414 C C . ASN A 172 ? 0.2720 0.2872 0.2399 -0.0044 -0.0217 0.0208 188 ASN A C 1415 O O . ASN A 172 ? 0.2771 0.2940 0.2496 -0.0046 -0.0215 0.0179 188 ASN A O 1416 C CB . ASN A 172 ? 0.2709 0.2847 0.2323 -0.0015 -0.0224 0.0211 188 ASN A CB 1417 C CG . ASN A 172 ? 0.2671 0.2849 0.2309 -0.0014 -0.0201 0.0183 188 ASN A CG 1418 O OD1 . ASN A 172 ? 0.2637 0.2845 0.2276 -0.0024 -0.0180 0.0185 188 ASN A OD1 1419 N ND2 . ASN A 172 ? 0.2631 0.2807 0.2287 -0.0001 -0.0206 0.0157 188 ASN A ND2 1420 N N . THR A 173 ? 0.2736 0.2898 0.2386 -0.0055 -0.0201 0.0235 189 THR A N 1421 C CA . THR A 173 ? 0.2760 0.2955 0.2435 -0.0071 -0.0182 0.0230 189 THR A CA 1422 C C . THR A 173 ? 0.2820 0.2999 0.2551 -0.0082 -0.0198 0.0220 189 THR A C 1423 O O . THR A 173 ? 0.2669 0.2877 0.2443 -0.0087 -0.0192 0.0193 189 THR A O 1424 C CB . THR A 173 ? 0.2756 0.2964 0.2395 -0.0081 -0.0162 0.0261 189 THR A CB 1425 O OG1 . THR A 173 ? 0.2770 0.2992 0.2359 -0.0070 -0.0149 0.0268 189 THR A OG1 1426 C CG2 . THR A 173 ? 0.2723 0.2971 0.2392 -0.0095 -0.0144 0.0251 189 THR A CG2 1427 N N . LYS A 174 ? 0.2834 0.2967 0.2565 -0.0085 -0.0218 0.0240 190 LYS A N 1428 C CA . LYS A 174 ? 0.2891 0.3001 0.2677 -0.0095 -0.0236 0.0232 190 LYS A CA 1429 C C . LYS A 174 ? 0.2820 0.2937 0.2658 -0.0086 -0.0251 0.0191 190 LYS A C 1430 O O . LYS A 174 ? 0.2758 0.2889 0.2650 -0.0095 -0.0252 0.0168 190 LYS A O 1431 C CB . LYS A 174 ? 0.3053 0.3104 0.2821 -0.0096 -0.0257 0.0264 190 LYS A CB 1432 C CG . LYS A 174 ? 0.3187 0.3208 0.3014 -0.0105 -0.0277 0.0257 190 LYS A CG 1433 C CD . LYS A 174 ? 0.3371 0.3330 0.3174 -0.0108 -0.0295 0.0295 190 LYS A CD 1434 C CE . LYS A 174 ? 0.3528 0.3461 0.3397 -0.0121 -0.0309 0.0289 190 LYS A CE 1435 N NZ . LYS A 174 ? 0.3671 0.3538 0.3516 -0.0124 -0.0325 0.0329 190 LYS A NZ 1436 N N . ALA A 175 ? 0.2751 0.2860 0.2575 -0.0069 -0.0260 0.0178 191 ALA A N 1437 C CA . ALA A 175 ? 0.2690 0.2807 0.2563 -0.0061 -0.0271 0.0138 191 ALA A CA 1438 C C . ALA A 175 ? 0.2648 0.2816 0.2538 -0.0065 -0.0245 0.0111 191 ALA A C 1439 O O . ALA A 175 ? 0.2716 0.2895 0.2658 -0.0069 -0.0249 0.0081 191 ALA A O 1440 C CB . ALA A 175 ? 0.2664 0.2766 0.2521 -0.0042 -0.0283 0.0129 191 ALA A CB 1441 N N . ALA A 176 ? 0.2587 0.2785 0.2432 -0.0063 -0.0219 0.0121 192 ALA A N 1442 C CA . ALA A 176 ? 0.2570 0.2814 0.2420 -0.0064 -0.0195 0.0100 192 ALA A CA 1443 C C . ALA A 176 ? 0.2615 0.2878 0.2501 -0.0078 -0.0192 0.0090 192 ALA A C 1444 O O . ALA A 176 ? 0.2589 0.2879 0.2504 -0.0078 -0.0186 0.0059 192 ALA A O 1445 C CB . ALA A 176 ? 0.2482 0.2750 0.2277 -0.0060 -0.0171 0.0118 192 ALA A CB 1446 N N . LYS A 177 ? 0.2665 0.2917 0.2547 -0.0090 -0.0196 0.0116 193 LYS A N 1447 C CA . LYS A 177 ? 0.2813 0.3085 0.2734 -0.0104 -0.0193 0.0108 193 LYS A CA 1448 C C . LYS A 177 ? 0.2844 0.3098 0.2828 -0.0109 -0.0215 0.0083 193 LYS A C 1449 O O . LYS A 177 ? 0.2860 0.3141 0.2884 -0.0116 -0.0212 0.0058 193 LYS A O 1450 C CB . LYS A 177 ? 0.2942 0.3206 0.2844 -0.0117 -0.0187 0.0142 193 LYS A CB 1451 C CG . LYS A 177 ? 0.3029 0.3325 0.2881 -0.0114 -0.0163 0.0159 193 LYS A CG 1452 C CD . LYS A 177 ? 0.3202 0.3498 0.3046 -0.0130 -0.0153 0.0187 193 LYS A CD 1453 C CE . LYS A 177 ? 0.3212 0.3541 0.3010 -0.0126 -0.0130 0.0200 193 LYS A CE 1454 N NZ . LYS A 177 ? 0.3186 0.3567 0.2996 -0.0121 -0.0119 0.0172 193 LYS A NZ 1455 N N . LEU A 178 ? 0.2921 0.3131 0.2917 -0.0103 -0.0237 0.0087 194 LEU A N 1456 C CA . LEU A 178 ? 0.2974 0.3167 0.3035 -0.0105 -0.0259 0.0059 194 LEU A CA 1457 C C . LEU A 178 ? 0.3027 0.3250 0.3114 -0.0097 -0.0253 0.0015 194 LEU A C 1458 O O . LEU A 178 ? 0.3054 0.3281 0.3200 -0.0101 -0.0264 -0.0015 194 LEU A O 1459 C CB . LEU A 178 ? 0.3002 0.3139 0.3066 -0.0098 -0.0288 0.0074 194 LEU A CB 1460 C CG . LEU A 178 ? 0.3063 0.3157 0.3121 -0.0108 -0.0300 0.0112 194 LEU A CG 1461 C CD1 . LEU A 178 ? 0.3149 0.3189 0.3184 -0.0096 -0.0326 0.0133 194 LEU A CD1 1462 C CD2 . LEU A 178 ? 0.3126 0.3215 0.3252 -0.0122 -0.0310 0.0097 194 LEU A CD2 1463 N N . ASN A 179 ? 0.2928 0.3173 0.2973 -0.0087 -0.0234 0.0013 195 ASN A N 1464 C CA . ASN A 179 ? 0.2956 0.3233 0.3015 -0.0081 -0.0220 -0.0023 195 ASN A CA 1465 C C . ASN A 179 ? 0.2894 0.3217 0.2936 -0.0085 -0.0196 -0.0031 195 ASN A C 1466 O O . ASN A 179 ? 0.2863 0.3213 0.2902 -0.0080 -0.0180 -0.0057 195 ASN A O 1467 C CB . ASN A 179 ? 0.2966 0.3235 0.2993 -0.0068 -0.0212 -0.0023 195 ASN A CB 1468 C CG . ASN A 179 ? 0.3118 0.3348 0.3175 -0.0061 -0.0239 -0.0030 195 ASN A CG 1469 O OD1 . ASN A 179 ? 0.3309 0.3536 0.3420 -0.0060 -0.0249 -0.0063 195 ASN A OD1 1470 N ND2 . ASN A 179 ? 0.3076 0.3275 0.3098 -0.0055 -0.0251 0.0000 195 ASN A ND2 1471 N N . ASN A 180 ? 0.2922 0.3253 0.2952 -0.0094 -0.0194 -0.0009 196 ASN A N 1472 C CA . ASN A 180 ? 0.2871 0.3247 0.2886 -0.0097 -0.0176 -0.0014 196 ASN A CA 1473 C C . ASN A 180 ? 0.2839 0.3238 0.2794 -0.0085 -0.0153 -0.0005 196 ASN A C 1474 O O . ASN A 180 ? 0.2817 0.3254 0.2760 -0.0082 -0.0139 -0.0020 196 ASN A O 1475 C CB . ASN A 180 ? 0.2918 0.3321 0.2981 -0.0100 -0.0178 -0.0054 196 ASN A CB 1476 C CG . ASN A 180 ? 0.3008 0.3396 0.3133 -0.0114 -0.0199 -0.0060 196 ASN A CG 1477 O OD1 . ASN A 180 ? 0.3055 0.3418 0.3179 -0.0122 -0.0207 -0.0030 196 ASN A OD1 1478 N ND2 . ASN A 180 ? 0.2993 0.3394 0.3170 -0.0116 -0.0207 -0.0099 196 ASN A ND2 1479 N N . PHE A 181 ? 0.2750 0.3125 0.2668 -0.0078 -0.0150 0.0017 197 PHE A N 1480 C CA . PHE A 181 ? 0.2735 0.3127 0.2596 -0.0069 -0.0130 0.0033 197 PHE A CA 1481 C C . PHE A 181 ? 0.2756 0.3152 0.2594 -0.0075 -0.0129 0.0065 197 PHE A C 1482 O O . PHE A 181 ? 0.2781 0.3152 0.2636 -0.0085 -0.0143 0.0081 197 PHE A O 1483 C CB . PHE A 181 ? 0.2647 0.3015 0.2485 -0.0058 -0.0128 0.0039 197 PHE A CB 1484 C CG . PHE A 181 ? 0.2679 0.3048 0.2537 -0.0052 -0.0122 0.0007 197 PHE A CG 1485 C CD1 . PHE A 181 ? 0.2703 0.3101 0.2540 -0.0046 -0.0099 -0.0007 197 PHE A CD1 1486 C CD2 . PHE A 181 ? 0.2655 0.2997 0.2552 -0.0052 -0.0138 -0.0008 197 PHE A CD2 1487 C CE1 . PHE A 181 ? 0.2657 0.3055 0.2510 -0.0042 -0.0089 -0.0036 197 PHE A CE1 1488 C CE2 . PHE A 181 ? 0.2700 0.3044 0.2619 -0.0047 -0.0130 -0.0040 197 PHE A CE2 1489 C CZ . PHE A 181 ? 0.2737 0.3110 0.2635 -0.0044 -0.0103 -0.0054 197 PHE A CZ 1490 N N . THR A 182 ? 0.2722 0.3147 0.2522 -0.0070 -0.0111 0.0074 198 THR A N 1491 C CA . THR A 182 ? 0.2737 0.3170 0.2517 -0.0076 -0.0107 0.0101 198 THR A CA 1492 C C . THR A 182 ? 0.2694 0.3092 0.2448 -0.0076 -0.0111 0.0130 198 THR A C 1493 O O . THR A 182 ? 0.2729 0.3113 0.2485 -0.0087 -0.0115 0.0152 198 THR A O 1494 C CB . THR A 182 ? 0.2808 0.3278 0.2552 -0.0067 -0.0088 0.0103 198 THR A CB 1495 O OG1 . THR A 182 ? 0.2843 0.3345 0.2605 -0.0064 -0.0087 0.0075 198 THR A OG1 1496 C CG2 . THR A 182 ? 0.2921 0.3404 0.2656 -0.0075 -0.0083 0.0125 198 THR A CG2 1497 N N . SER A 183 ? 0.2557 0.2940 0.2288 -0.0064 -0.0109 0.0129 199 SER A N 1498 C CA . SER A 183 ? 0.2446 0.2799 0.2147 -0.0059 -0.0114 0.0152 199 SER A CA 1499 C C . SER A 183 ? 0.2356 0.2690 0.2055 -0.0047 -0.0118 0.0137 199 SER A C 1500 O O . SER A 183 ? 0.2260 0.2605 0.1980 -0.0043 -0.0113 0.0111 199 SER A O 1501 C CB . SER A 183 ? 0.2482 0.2854 0.2137 -0.0056 -0.0097 0.0173 199 SER A CB 1502 O OG . SER A 183 ? 0.2438 0.2826 0.2067 -0.0042 -0.0082 0.0165 199 SER A OG 1503 N N . GLY A 184 ? 0.2258 0.2565 0.1935 -0.0041 -0.0127 0.0152 200 GLY A N 1504 C CA . GLY A 184 ? 0.2213 0.2505 0.1894 -0.0028 -0.0130 0.0135 200 GLY A CA 1505 C C . GLY A 184 ? 0.2125 0.2440 0.1786 -0.0019 -0.0107 0.0125 200 GLY A C 1506 O O . GLY A 184 ? 0.2085 0.2393 0.1759 -0.0011 -0.0104 0.0105 200 GLY A O 1507 N N . ALA A 185 ? 0.2180 0.2522 0.1810 -0.0019 -0.0089 0.0139 201 ALA A N 1508 C CA . ALA A 185 ? 0.2192 0.2553 0.1799 -0.0009 -0.0067 0.0133 201 ALA A CA 1509 C C . ALA A 185 ? 0.2227 0.2599 0.1861 -0.0009 -0.0060 0.0107 201 ALA A C 1510 O O . ALA A 185 ? 0.2177 0.2544 0.1813 -0.0002 -0.0048 0.0091 201 ALA A O 1511 C CB . ALA A 185 ? 0.2176 0.2564 0.1750 -0.0008 -0.0053 0.0151 201 ALA A CB 1512 N N . GLU A 186 ? 0.2346 0.2731 0.2002 -0.0019 -0.0066 0.0100 202 GLU A N 1513 C CA . GLU A 186 ? 0.2398 0.2796 0.2078 -0.0020 -0.0060 0.0073 202 GLU A CA 1514 C C . GLU A 186 ? 0.2408 0.2784 0.2128 -0.0021 -0.0069 0.0050 202 GLU A C 1515 O O . GLU A 186 ? 0.2345 0.2725 0.2074 -0.0018 -0.0055 0.0027 202 GLU A O 1516 C CB . GLU A 186 ? 0.2563 0.2984 0.2262 -0.0029 -0.0067 0.0069 202 GLU A CB 1517 C CG . GLU A 186 ? 0.2738 0.3191 0.2404 -0.0025 -0.0055 0.0081 202 GLU A CG 1518 C CD . GLU A 186 ? 0.2875 0.3326 0.2518 -0.0027 -0.0056 0.0110 202 GLU A CD 1519 O OE1 . GLU A 186 ? 0.2969 0.3397 0.2625 -0.0036 -0.0069 0.0123 202 GLU A OE1 1520 O OE2 . GLU A 186 ? 0.2997 0.3471 0.2609 -0.0020 -0.0044 0.0119 202 GLU A OE2 1521 N N . ALA A 187 ? 0.2404 0.2754 0.2148 -0.0026 -0.0092 0.0055 203 ALA A N 1522 C CA . ALA A 187 ? 0.2447 0.2772 0.2230 -0.0025 -0.0105 0.0033 203 ALA A CA 1523 C C . ALA A 187 ? 0.2483 0.2803 0.2257 -0.0014 -0.0089 0.0023 203 ALA A C 1524 O O . ALA A 187 ? 0.2521 0.2841 0.2325 -0.0014 -0.0081 -0.0005 203 ALA A O 1525 C CB . ALA A 187 ? 0.2456 0.2751 0.2253 -0.0027 -0.0134 0.0046 203 ALA A CB 1526 N N . TRP A 188 ? 0.2484 0.2799 0.2218 -0.0007 -0.0084 0.0044 204 TRP A N 1527 C CA . TRP A 188 ? 0.2391 0.2701 0.2118 0.0001 -0.0067 0.0035 204 TRP A CA 1528 C C . TRP A 188 ? 0.2446 0.2775 0.2164 0.0003 -0.0036 0.0022 204 TRP A C 1529 O O . TRP A 188 ? 0.2368 0.2690 0.2108 0.0004 -0.0022 0.0000 204 TRP A O 1530 C CB . TRP A 188 ? 0.2408 0.2713 0.2094 0.0010 -0.0066 0.0059 204 TRP A CB 1531 C CG . TRP A 188 ? 0.2372 0.2652 0.2065 0.0013 -0.0094 0.0065 204 TRP A CG 1532 C CD1 . TRP A 188 ? 0.2345 0.2604 0.2078 0.0012 -0.0119 0.0050 204 TRP A CD1 1533 C CD2 . TRP A 188 ? 0.2379 0.2653 0.2034 0.0020 -0.0100 0.0087 204 TRP A CD2 1534 N NE1 . TRP A 188 ? 0.2364 0.2600 0.2081 0.0019 -0.0142 0.0063 204 TRP A NE1 1535 C CE2 . TRP A 188 ? 0.2408 0.2654 0.2077 0.0024 -0.0129 0.0086 204 TRP A CE2 1536 C CE3 . TRP A 188 ? 0.2405 0.2693 0.2016 0.0025 -0.0083 0.0107 204 TRP A CE3 1537 C CZ2 . TRP A 188 ? 0.2412 0.2645 0.2046 0.0032 -0.0142 0.0104 204 TRP A CZ2 1538 C CZ3 . TRP A 188 ? 0.2440 0.2718 0.2022 0.0032 -0.0094 0.0123 204 TRP A CZ3 1539 C CH2 . TRP A 188 ? 0.2441 0.2692 0.2032 0.0035 -0.0123 0.0122 204 TRP A CH2 1540 N N . LEU A 189 ? 0.2417 0.2768 0.2101 0.0002 -0.0025 0.0037 205 LEU A N 1541 C CA . LEU A 189 ? 0.2396 0.2762 0.2057 0.0006 0.0002 0.0031 205 LEU A CA 1542 C C . LEU A 189 ? 0.2474 0.2845 0.2166 0.0001 0.0009 0.0001 205 LEU A C 1543 O O . LEU A 189 ? 0.2480 0.2854 0.2157 0.0005 0.0036 -0.0008 205 LEU A O 1544 C CB . LEU A 189 ? 0.2362 0.2752 0.1982 0.0009 0.0007 0.0052 205 LEU A CB 1545 C CG . LEU A 189 ? 0.2318 0.2707 0.1901 0.0018 0.0011 0.0077 205 LEU A CG 1546 C CD1 . LEU A 189 ? 0.2308 0.2722 0.1866 0.0018 0.0007 0.0095 205 LEU A CD1 1547 C CD2 . LEU A 189 ? 0.2331 0.2713 0.1891 0.0028 0.0037 0.0077 205 LEU A CD2 1548 N N . ASP A 190 ? 0.2544 0.2914 0.2277 -0.0007 -0.0012 -0.0011 206 ASP A N 1549 C CA . ASP A 190 ? 0.2664 0.3040 0.2434 -0.0013 -0.0008 -0.0043 206 ASP A CA 1550 C C . ASP A 190 ? 0.2666 0.3028 0.2459 -0.0011 0.0009 -0.0067 206 ASP A C 1551 O O . ASP A 190 ? 0.2610 0.2980 0.2412 -0.0014 0.0028 -0.0090 206 ASP A O 1552 C CB . ASP A 190 ? 0.2781 0.3151 0.2599 -0.0021 -0.0039 -0.0053 206 ASP A CB 1553 C CG . ASP A 190 ? 0.2952 0.3333 0.2811 -0.0027 -0.0037 -0.0089 206 ASP A CG 1554 O OD1 . ASP A 190 ? 0.2995 0.3400 0.2836 -0.0028 -0.0024 -0.0096 206 ASP A OD1 1555 O OD2 . ASP A 190 ? 0.3057 0.3423 0.2969 -0.0031 -0.0049 -0.0112 206 ASP A OD2 1556 N N . GLU A 191 ? 0.2672 0.3013 0.2475 -0.0007 0.0004 -0.0063 207 GLU A N 1557 C CA . GLU A 191 ? 0.2753 0.3081 0.2585 -0.0006 0.0022 -0.0087 207 GLU A CA 1558 C C . GLU A 191 ? 0.2713 0.3046 0.2511 -0.0003 0.0063 -0.0087 207 GLU A C 1559 O O . GLU A 191 ? 0.2692 0.3016 0.2518 -0.0006 0.0085 -0.0111 207 GLU A O 1560 C CB . GLU A 191 ? 0.2884 0.3191 0.2730 0.0000 0.0006 -0.0082 207 GLU A CB 1561 C CG . GLU A 191 ? 0.3064 0.3359 0.2937 0.0000 -0.0034 -0.0078 207 GLU A CG 1562 C CD . GLU A 191 ? 0.3309 0.3600 0.3244 -0.0006 -0.0051 -0.0111 207 GLU A CD 1563 O OE1 . GLU A 191 ? 0.3379 0.3672 0.3351 -0.0009 -0.0033 -0.0143 207 GLU A OE1 1564 O OE2 . GLU A 191 ? 0.3632 0.3917 0.3580 -0.0009 -0.0081 -0.0105 207 GLU A OE2 1565 N N . TYR A 192 ? 0.2650 0.2994 0.2390 0.0001 0.0074 -0.0061 208 TYR A N 1566 C CA . TYR A 192 ? 0.2668 0.3011 0.2366 0.0006 0.0112 -0.0056 208 TYR A CA 1567 C C . TYR A 192 ? 0.2739 0.3099 0.2416 0.0004 0.0127 -0.0065 208 TYR A C 1568 O O . TYR A 192 ? 0.2758 0.3115 0.2396 0.0009 0.0158 -0.0060 208 TYR A O 1569 C CB . TYR A 192 ? 0.2626 0.2967 0.2272 0.0016 0.0116 -0.0022 208 TYR A CB 1570 C CG . TYR A 192 ? 0.2578 0.2904 0.2242 0.0019 0.0104 -0.0015 208 TYR A CG 1571 C CD1 . TYR A 192 ? 0.2607 0.2914 0.2288 0.0021 0.0124 -0.0025 208 TYR A CD1 1572 C CD2 . TYR A 192 ? 0.2625 0.2954 0.2291 0.0020 0.0072 -0.0001 208 TYR A CD2 1573 C CE1 . TYR A 192 ? 0.2537 0.2831 0.2236 0.0025 0.0111 -0.0023 208 TYR A CE1 1574 C CE2 . TYR A 192 ? 0.2569 0.2884 0.2247 0.0024 0.0059 0.0003 208 TYR A CE2 1575 C CZ . TYR A 192 ? 0.2602 0.2901 0.2296 0.0027 0.0077 -0.0008 208 TYR A CZ 1576 O OH . TYR A 192 ? 0.2535 0.2823 0.2242 0.0033 0.0063 -0.0007 208 TYR A OH 1577 N N . GLU A 193 ? 0.2812 0.3188 0.2514 -0.0001 0.0105 -0.0079 209 GLU A N 1578 C CA . GLU A 193 ? 0.2970 0.3365 0.2661 -0.0003 0.0116 -0.0096 209 GLU A CA 1579 C C . GLU A 193 ? 0.2951 0.3356 0.2569 0.0007 0.0136 -0.0076 209 GLU A C 1580 O O . GLU A 193 ? 0.2898 0.3305 0.2491 0.0009 0.0164 -0.0088 209 GLU A O 1581 C CB . GLU A 193 ? 0.3191 0.3579 0.2917 -0.0010 0.0140 -0.0131 209 GLU A CB 1582 C CG . GLU A 193 ? 0.3570 0.3953 0.3373 -0.0020 0.0119 -0.0159 209 GLU A CG 1583 C CD . GLU A 193 ? 0.3739 0.4121 0.3579 -0.0027 0.0145 -0.0198 209 GLU A CD 1584 O OE1 . GLU A 193 ? 0.3803 0.4204 0.3633 -0.0030 0.0158 -0.0215 209 GLU A OE1 1585 O OE2 . GLU A 193 ? 0.4037 0.4403 0.3919 -0.0031 0.0153 -0.0212 209 GLU A OE2 1586 N N . ASP A 194 ? 0.2916 0.3327 0.2500 0.0015 0.0123 -0.0047 210 ASP A N 1587 C CA . ASP A 194 ? 0.2946 0.3363 0.2463 0.0028 0.0138 -0.0027 210 ASP A CA 1588 C C . ASP A 194 ? 0.2951 0.3387 0.2451 0.0034 0.0112 -0.0005 210 ASP A C 1589 O O . ASP A 194 ? 0.2865 0.3294 0.2370 0.0034 0.0102 0.0013 210 ASP A O 1590 C CB . ASP A 194 ? 0.2970 0.3361 0.2457 0.0035 0.0168 -0.0011 210 ASP A CB 1591 C CG . ASP A 194 ? 0.2999 0.3391 0.2414 0.0050 0.0187 0.0008 210 ASP A CG 1592 O OD1 . ASP A 194 ? 0.3041 0.3456 0.2428 0.0059 0.0169 0.0018 210 ASP A OD1 1593 O OD2 . ASP A 194 ? 0.3159 0.3527 0.2546 0.0054 0.0219 0.0013 210 ASP A OD2 1594 N N . ASP A 195 ? 0.2977 0.3440 0.2461 0.0037 0.0102 -0.0011 211 ASP A N 1595 C CA . ASP A 195 ? 0.3062 0.3548 0.2542 0.0040 0.0077 0.0003 211 ASP A CA 1596 C C . ASP A 195 ? 0.3077 0.3565 0.2503 0.0056 0.0084 0.0031 211 ASP A C 1597 O O . ASP A 195 ? 0.3250 0.3757 0.2675 0.0058 0.0066 0.0042 211 ASP A O 1598 C CB . ASP A 195 ? 0.3071 0.3588 0.2569 0.0037 0.0059 -0.0016 211 ASP A CB 1599 C CG . ASP A 195 ? 0.3046 0.3577 0.2500 0.0049 0.0072 -0.0029 211 ASP A CG 1600 O OD1 . ASP A 195 ? 0.3063 0.3582 0.2462 0.0062 0.0094 -0.0015 211 ASP A OD1 1601 O OD2 . ASP A 195 ? 0.3031 0.3584 0.2505 0.0045 0.0061 -0.0054 211 ASP A OD2 1602 N N . THR A 196 ? 0.3045 0.3511 0.2431 0.0066 0.0110 0.0041 212 THR A N 1603 C CA . THR A 196 ? 0.3005 0.3468 0.2348 0.0081 0.0115 0.0067 212 THR A CA 1604 C C . THR A 196 ? 0.2978 0.3412 0.2331 0.0079 0.0127 0.0081 212 THR A C 1605 O O . THR A 196 ? 0.2914 0.3336 0.2231 0.0091 0.0139 0.0101 212 THR A O 1606 C CB . THR A 196 ? 0.3151 0.3609 0.2430 0.0099 0.0135 0.0073 212 THR A CB 1607 O OG1 . THR A 196 ? 0.3279 0.3708 0.2550 0.0095 0.0165 0.0066 212 THR A OG1 1608 C CG2 . THR A 196 ? 0.3216 0.3707 0.2480 0.0105 0.0119 0.0058 212 THR A CG2 1609 N N . PHE A 197 ? 0.2815 0.3237 0.2218 0.0064 0.0122 0.0069 213 PHE A N 1610 C CA . PHE A 197 ? 0.2711 0.3106 0.2128 0.0063 0.0134 0.0075 213 PHE A CA 1611 C C . PHE A 197 ? 0.2722 0.3118 0.2124 0.0070 0.0126 0.0099 213 PHE A C 1612 O O . PHE A 197 ? 0.2647 0.3024 0.2030 0.0078 0.0143 0.0109 213 PHE A O 1613 C CB . PHE A 197 ? 0.2597 0.2982 0.2072 0.0048 0.0125 0.0055 213 PHE A CB 1614 C CG . PHE A 197 ? 0.2606 0.2963 0.2099 0.0046 0.0144 0.0049 213 PHE A CG 1615 C CD1 . PHE A 197 ? 0.2548 0.2889 0.2032 0.0047 0.0176 0.0038 213 PHE A CD1 1616 C CD2 . PHE A 197 ? 0.2464 0.2810 0.1984 0.0045 0.0131 0.0052 213 PHE A CD2 1617 C CE1 . PHE A 197 ? 0.2601 0.2917 0.2111 0.0044 0.0196 0.0029 213 PHE A CE1 1618 C CE2 . PHE A 197 ? 0.2504 0.2827 0.2049 0.0044 0.0147 0.0041 213 PHE A CE2 1619 C CZ . PHE A 197 ? 0.2583 0.2891 0.2126 0.0043 0.0180 0.0030 213 PHE A CZ 1620 N N . GLU A 198 ? 0.2729 0.3147 0.2140 0.0067 0.0101 0.0106 214 GLU A N 1621 C CA . GLU A 198 ? 0.2763 0.3188 0.2160 0.0074 0.0094 0.0126 214 GLU A CA 1622 C C . GLU A 198 ? 0.2787 0.3215 0.2137 0.0091 0.0107 0.0141 214 GLU A C 1623 O O . GLU A 198 ? 0.2728 0.3145 0.2065 0.0100 0.0116 0.0154 214 GLU A O 1624 C CB . GLU A 198 ? 0.2805 0.3255 0.2217 0.0067 0.0069 0.0130 214 GLU A CB 1625 C CG . GLU A 198 ? 0.2822 0.3263 0.2275 0.0051 0.0052 0.0123 214 GLU A CG 1626 C CD . GLU A 198 ? 0.2900 0.3364 0.2368 0.0042 0.0033 0.0126 214 GLU A CD 1627 O OE1 . GLU A 198 ? 0.2855 0.3333 0.2335 0.0038 0.0027 0.0113 214 GLU A OE1 1628 O OE2 . GLU A 198 ? 0.2762 0.3229 0.2230 0.0039 0.0024 0.0141 214 GLU A OE2 1629 N N . GLN A 199 ? 0.2760 0.3204 0.2084 0.0099 0.0108 0.0138 215 GLN A N 1630 C CA . GLN A 199 ? 0.2894 0.3339 0.2170 0.0118 0.0118 0.0152 215 GLN A CA 1631 C C . GLN A 199 ? 0.2855 0.3264 0.2108 0.0126 0.0146 0.0159 215 GLN A C 1632 O O . GLN A 199 ? 0.2765 0.3164 0.1991 0.0140 0.0154 0.0175 215 GLN A O 1633 C CB . GLN A 199 ? 0.3060 0.3529 0.2310 0.0127 0.0110 0.0145 215 GLN A CB 1634 C CG . GLN A 199 ? 0.3401 0.3877 0.2603 0.0150 0.0110 0.0161 215 GLN A CG 1635 C CD . GLN A 199 ? 0.3485 0.3977 0.2697 0.0155 0.0098 0.0174 215 GLN A CD 1636 O OE1 . GLN A 199 ? 0.3535 0.4053 0.2778 0.0144 0.0080 0.0169 215 GLN A OE1 1637 N NE2 . GLN A 199 ? 0.3531 0.4004 0.2716 0.0170 0.0111 0.0190 215 GLN A NE2 1638 N N . GLN A 200 ? 0.2810 0.3199 0.2077 0.0116 0.0161 0.0144 216 GLN A N 1639 C CA . GLN A 200 ? 0.2812 0.3165 0.2066 0.0119 0.0193 0.0148 216 GLN A CA 1640 C C . GLN A 200 ? 0.2798 0.3134 0.2073 0.0119 0.0197 0.0156 216 GLN A C 1641 O O . GLN A 200 ? 0.2759 0.3070 0.2009 0.0130 0.0218 0.0169 216 GLN A O 1642 C CB . GLN A 200 ? 0.2853 0.3193 0.2135 0.0104 0.0207 0.0125 216 GLN A CB 1643 C CG . GLN A 200 ? 0.2889 0.3234 0.2137 0.0107 0.0217 0.0117 216 GLN A CG 1644 C CD . GLN A 200 ? 0.2922 0.3259 0.2206 0.0091 0.0231 0.0091 216 GLN A CD 1645 O OE1 . GLN A 200 ? 0.2992 0.3300 0.2289 0.0086 0.0259 0.0087 216 GLN A OE1 1646 N NE2 . GLN A 200 ? 0.2857 0.3219 0.2163 0.0083 0.0213 0.0072 216 GLN A NE2 1647 N N . LEU A 201 ? 0.2704 0.3051 0.2021 0.0108 0.0177 0.0149 217 LEU A N 1648 C CA . LEU A 201 ? 0.2761 0.3096 0.2098 0.0109 0.0177 0.0153 217 LEU A CA 1649 C C . LEU A 201 ? 0.2769 0.3117 0.2080 0.0122 0.0169 0.0173 217 LEU A C 1650 O O . LEU A 201 ? 0.2778 0.3110 0.2087 0.0130 0.0180 0.0180 217 LEU A O 1651 C CB . LEU A 201 ? 0.2646 0.2987 0.2029 0.0094 0.0156 0.0139 217 LEU A CB 1652 C CG . LEU A 201 ? 0.2641 0.2965 0.2064 0.0082 0.0164 0.0116 217 LEU A CG 1653 C CD1 . LEU A 201 ? 0.2616 0.2949 0.2079 0.0071 0.0136 0.0104 217 LEU A CD1 1654 C CD2 . LEU A 201 ? 0.2623 0.2918 0.2060 0.0084 0.0189 0.0110 217 LEU A CD2 1655 N N . GLU A 202 ? 0.2798 0.3176 0.2094 0.0126 0.0150 0.0179 218 GLU A N 1656 C CA . GLU A 202 ? 0.2883 0.3276 0.2153 0.0140 0.0144 0.0195 218 GLU A CA 1657 C C . GLU A 202 ? 0.2891 0.3263 0.2123 0.0158 0.0165 0.0207 218 GLU A C 1658 O O . GLU A 202 ? 0.2803 0.3168 0.2026 0.0170 0.0169 0.0218 218 GLU A O 1659 C CB . GLU A 202 ? 0.3002 0.3433 0.2265 0.0141 0.0123 0.0196 218 GLU A CB 1660 C CG . GLU A 202 ? 0.3198 0.3649 0.2497 0.0124 0.0103 0.0189 218 GLU A CG 1661 C CD . GLU A 202 ? 0.3361 0.3820 0.2671 0.0123 0.0097 0.0197 218 GLU A CD 1662 O OE1 . GLU A 202 ? 0.3500 0.3952 0.2795 0.0136 0.0106 0.0205 218 GLU A OE1 1663 O OE2 . GLU A 202 ? 0.3376 0.3847 0.2708 0.0109 0.0082 0.0195 218 GLU A OE2 1664 N N . ASP A 203 ? 0.2900 0.3260 0.2107 0.0161 0.0178 0.0205 219 ASP A N 1665 C CA . ASP A 203 ? 0.2966 0.3299 0.2128 0.0179 0.0198 0.0220 219 ASP A CA 1666 C C . ASP A 203 ? 0.2882 0.3176 0.2057 0.0178 0.0225 0.0223 219 ASP A C 1667 O O . ASP A 203 ? 0.2915 0.3191 0.2069 0.0193 0.0234 0.0239 219 ASP A O 1668 C CB . ASP A 203 ? 0.3129 0.3456 0.2255 0.0182 0.0208 0.0217 219 ASP A CB 1669 C CG . ASP A 203 ? 0.3229 0.3594 0.2337 0.0189 0.0182 0.0213 219 ASP A CG 1670 O OD1 . ASP A 203 ? 0.3279 0.3674 0.2400 0.0193 0.0160 0.0216 219 ASP A OD1 1671 O OD2 . ASP A 203 ? 0.3434 0.3801 0.2519 0.0190 0.0185 0.0206 219 ASP A OD2 1672 N N . ILE A 204 ? 0.2865 0.3145 0.2077 0.0160 0.0235 0.0207 220 ILE A N 1673 C CA . ILE A 204 ? 0.2895 0.3140 0.2129 0.0157 0.0260 0.0205 220 ILE A CA 1674 C C . ILE A 204 ? 0.2955 0.3209 0.2213 0.0162 0.0247 0.0208 220 ILE A C 1675 O O . ILE A 204 ? 0.3016 0.3246 0.2270 0.0171 0.0263 0.0217 220 ILE A O 1676 C CB . ILE A 204 ? 0.2847 0.3082 0.2126 0.0138 0.0270 0.0182 220 ILE A CB 1677 C CG1 . ILE A 204 ? 0.2844 0.3065 0.2098 0.0134 0.0292 0.0179 220 ILE A CG1 1678 C CG2 . ILE A 204 ? 0.2883 0.3090 0.2200 0.0134 0.0290 0.0174 220 ILE A CG2 1679 C CD1 . ILE A 204 ? 0.2825 0.3048 0.2124 0.0115 0.0295 0.0152 220 ILE A CD1 1680 N N . PHE A 205 ? 0.2939 0.3224 0.2220 0.0155 0.0220 0.0201 221 PHE A N 1681 C CA . PHE A 205 ? 0.2918 0.3213 0.2214 0.0159 0.0207 0.0203 221 PHE A CA 1682 C C . PHE A 205 ? 0.2987 0.3285 0.2250 0.0179 0.0208 0.0221 221 PHE A C 1683 O O . PHE A 205 ? 0.2972 0.3258 0.2244 0.0187 0.0216 0.0223 221 PHE A O 1684 C CB . PHE A 205 ? 0.3030 0.3356 0.2347 0.0149 0.0179 0.0195 221 PHE A CB 1685 C CG . PHE A 205 ? 0.3097 0.3435 0.2425 0.0153 0.0169 0.0196 221 PHE A CG 1686 C CD1 . PHE A 205 ? 0.3213 0.3534 0.2571 0.0151 0.0174 0.0185 221 PHE A CD1 1687 C CD2 . PHE A 205 ? 0.3156 0.3523 0.2465 0.0160 0.0154 0.0207 221 PHE A CD2 1688 C CE1 . PHE A 205 ? 0.3206 0.3538 0.2569 0.0157 0.0164 0.0184 221 PHE A CE1 1689 C CE2 . PHE A 205 ? 0.3245 0.3624 0.2562 0.0165 0.0147 0.0207 221 PHE A CE2 1690 C CZ . PHE A 205 ? 0.3275 0.3636 0.2616 0.0163 0.0152 0.0196 221 PHE A CZ 1691 N N . ALA A 206 ? 0.3023 0.3339 0.2251 0.0188 0.0200 0.0232 222 ALA A N 1692 C CA . ALA A 206 ? 0.3097 0.3418 0.2296 0.0209 0.0198 0.0247 222 ALA A CA 1693 C C . ALA A 206 ? 0.3166 0.3444 0.2346 0.0222 0.0224 0.0259 222 ALA A C 1694 O O . ALA A 206 ? 0.3092 0.3365 0.2267 0.0238 0.0224 0.0268 222 ALA A O 1695 C CB . ALA A 206 ? 0.3086 0.3433 0.2252 0.0218 0.0182 0.0253 222 ALA A CB 1696 N N . ASP A 207 ? 0.3344 0.3589 0.2516 0.0216 0.0247 0.0258 223 ASP A N 1697 C CA . ASP A 207 ? 0.3421 0.3619 0.2577 0.0225 0.0277 0.0270 223 ASP A CA 1698 C C . ASP A 207 ? 0.3450 0.3630 0.2651 0.0221 0.0288 0.0262 223 ASP A C 1699 O O . ASP A 207 ? 0.3374 0.3525 0.2568 0.0233 0.0304 0.0273 223 ASP A O 1700 C CB . ASP A 207 ? 0.3661 0.3829 0.2802 0.0216 0.0303 0.0269 223 ASP A CB 1701 C CG . ASP A 207 ? 0.3783 0.3959 0.2868 0.0226 0.0297 0.0279 223 ASP A CG 1702 O OD1 . ASP A 207 ? 0.3911 0.4103 0.2963 0.0245 0.0278 0.0292 223 ASP A OD1 1703 O OD2 . ASP A 207 ? 0.3992 0.4160 0.3068 0.0215 0.0311 0.0272 223 ASP A OD2 1704 N N . ILE A 208 ? 0.3358 0.3556 0.2606 0.0204 0.0278 0.0241 224 ILE A N 1705 C CA . ILE A 208 ? 0.3440 0.3624 0.2735 0.0199 0.0287 0.0227 224 ILE A CA 1706 C C . ILE A 208 ? 0.3312 0.3524 0.2621 0.0207 0.0264 0.0224 224 ILE A C 1707 O O . ILE A 208 ? 0.3174 0.3376 0.2512 0.0210 0.0270 0.0216 224 ILE A O 1708 C CB . ILE A 208 ? 0.3618 0.3800 0.2959 0.0179 0.0289 0.0202 224 ILE A CB 1709 C CG1 . ILE A 208 ? 0.3885 0.4050 0.3215 0.0168 0.0308 0.0201 224 ILE A CG1 1710 C CG2 . ILE A 208 ? 0.3759 0.3919 0.3148 0.0176 0.0304 0.0187 224 ILE A CG2 1711 C CD1 . ILE A 208 ? 0.4264 0.4384 0.3576 0.0172 0.0346 0.0212 224 ILE A CD1 1712 N N . ARG A 209 ? 0.3188 0.3438 0.2477 0.0210 0.0239 0.0230 225 ARG A N 1713 C CA . ARG A 209 ? 0.3204 0.3486 0.2504 0.0215 0.0219 0.0226 225 ARG A CA 1714 C C . ARG A 209 ? 0.3095 0.3365 0.2395 0.0233 0.0227 0.0232 225 ARG A C 1715 O O . ARG A 209 ? 0.3150 0.3431 0.2477 0.0234 0.0221 0.0220 225 ARG A O 1716 C CB . ARG A 209 ? 0.3306 0.3628 0.2583 0.0215 0.0196 0.0233 225 ARG A CB 1717 C CG . ARG A 209 ? 0.3653 0.4011 0.2943 0.0214 0.0177 0.0227 225 ARG A CG 1718 C CD . ARG A 209 ? 0.3801 0.4195 0.3077 0.0209 0.0159 0.0231 225 ARG A CD 1719 N NE . ARG A 209 ? 0.3928 0.4352 0.3218 0.0201 0.0144 0.0224 225 ARG A NE 1720 C CZ . ARG A 209 ? 0.4047 0.4502 0.3335 0.0191 0.0129 0.0225 225 ARG A CZ 1721 N NH1 . ARG A 209 ? 0.4071 0.4533 0.3348 0.0187 0.0125 0.0229 225 ARG A NH1 1722 N NH2 . ARG A 209 ? 0.3870 0.4347 0.3167 0.0184 0.0120 0.0221 225 ARG A NH2 1723 N N . PRO A 210 ? 0.3084 0.3332 0.2354 0.0249 0.0240 0.0250 226 PRO A N 1724 C CA . PRO A 210 ? 0.3077 0.3311 0.2351 0.0267 0.0246 0.0255 226 PRO A CA 1725 C C . PRO A 210 ? 0.3056 0.3261 0.2372 0.0262 0.0264 0.0241 226 PRO A C 1726 O O . PRO A 210 ? 0.3233 0.3446 0.2572 0.0271 0.0260 0.0233 226 PRO A O 1727 C CB . PRO A 210 ? 0.3118 0.3324 0.2349 0.0284 0.0257 0.0278 226 PRO A CB 1728 C CG . PRO A 210 ? 0.3153 0.3379 0.2351 0.0278 0.0246 0.0283 226 PRO A CG 1729 C CD . PRO A 210 ? 0.3104 0.3338 0.2331 0.0254 0.0246 0.0266 226 PRO A CD 1730 N N . LEU A 211 ? 0.2969 0.3144 0.2300 0.0249 0.0284 0.0236 227 LEU A N 1731 C CA . LEU A 211 ? 0.2841 0.2992 0.2221 0.0242 0.0301 0.0217 227 LEU A CA 1732 C C . LEU A 211 ? 0.2754 0.2939 0.2170 0.0235 0.0279 0.0193 227 LEU A C 1733 O O . LEU A 211 ? 0.2661 0.2845 0.2111 0.0240 0.0279 0.0178 227 LEU A O 1734 C CB . LEU A 211 ? 0.2834 0.2950 0.2228 0.0227 0.0327 0.0212 227 LEU A CB 1735 C CG . LEU A 211 ? 0.2802 0.2893 0.2255 0.0218 0.0346 0.0189 227 LEU A CG 1736 C CD1 . LEU A 211 ? 0.2845 0.2908 0.2312 0.0232 0.0362 0.0194 227 LEU A CD1 1737 C CD2 . LEU A 211 ? 0.2842 0.2904 0.2310 0.0202 0.0373 0.0183 227 LEU A CD2 1738 N N . TYR A 212 ? 0.2657 0.2872 0.2065 0.0223 0.0258 0.0188 228 TYR A N 1739 C CA . TYR A 212 ? 0.2568 0.2815 0.1999 0.0218 0.0235 0.0169 228 TYR A CA 1740 C C . TYR A 212 ? 0.2597 0.2869 0.2024 0.0232 0.0223 0.0169 228 TYR A C 1741 O O . TYR A 212 ? 0.2749 0.3029 0.2203 0.0233 0.0217 0.0150 228 TYR A O 1742 C CB . TYR A 212 ? 0.2429 0.2703 0.1845 0.0205 0.0214 0.0169 228 TYR A CB 1743 C CG . TYR A 212 ? 0.2377 0.2679 0.1807 0.0201 0.0191 0.0154 228 TYR A CG 1744 C CD1 . TYR A 212 ? 0.2383 0.2675 0.1850 0.0196 0.0188 0.0130 228 TYR A CD1 1745 C CD2 . TYR A 212 ? 0.2325 0.2662 0.1730 0.0204 0.0173 0.0163 228 TYR A CD2 1746 C CE1 . TYR A 212 ? 0.2317 0.2632 0.1791 0.0196 0.0166 0.0117 228 TYR A CE1 1747 C CE2 . TYR A 212 ? 0.2321 0.2680 0.1732 0.0202 0.0155 0.0151 228 TYR A CE2 1748 C CZ . TYR A 212 ? 0.2273 0.2620 0.1715 0.0198 0.0151 0.0129 228 TYR A CZ 1749 O OH . TYR A 212 ? 0.2221 0.2587 0.1662 0.0198 0.0131 0.0117 228 TYR A OH 1750 N N . GLN A 213 ? 0.2591 0.2875 0.1983 0.0243 0.0220 0.0189 229 GLN A N 1751 C CA . GLN A 213 ? 0.2689 0.3001 0.2078 0.0256 0.0209 0.0188 229 GLN A CA 1752 C C . GLN A 213 ? 0.2677 0.2966 0.2092 0.0269 0.0223 0.0180 229 GLN A C 1753 O O . GLN A 213 ? 0.2554 0.2866 0.1986 0.0275 0.0214 0.0165 229 GLN A O 1754 C CB . GLN A 213 ? 0.2727 0.3060 0.2079 0.0265 0.0201 0.0207 229 GLN A CB 1755 C CG . GLN A 213 ? 0.2859 0.3217 0.2194 0.0250 0.0187 0.0211 229 GLN A CG 1756 C CD . GLN A 213 ? 0.3042 0.3445 0.2361 0.0254 0.0170 0.0215 229 GLN A CD 1757 O OE1 . GLN A 213 ? 0.3181 0.3610 0.2499 0.0240 0.0157 0.0212 229 GLN A OE1 1758 N NE2 . GLN A 213 ? 0.3293 0.3702 0.2602 0.0272 0.0170 0.0223 229 GLN A NE2 1759 N N . GLN A 214 ? 0.2628 0.2873 0.2049 0.0273 0.0246 0.0188 230 GLN A N 1760 C CA . GLN A 214 ? 0.2678 0.2895 0.2133 0.0283 0.0262 0.0178 230 GLN A CA 1761 C C . GLN A 214 ? 0.2711 0.2931 0.2215 0.0273 0.0260 0.0147 230 GLN A C 1762 O O . GLN A 214 ? 0.2764 0.2990 0.2297 0.0283 0.0258 0.0130 230 GLN A O 1763 C CB . GLN A 214 ? 0.2710 0.2873 0.2158 0.0286 0.0290 0.0196 230 GLN A CB 1764 C CG . GLN A 214 ? 0.2700 0.2855 0.2097 0.0301 0.0290 0.0226 230 GLN A CG 1765 C CD . GLN A 214 ? 0.2720 0.2885 0.2116 0.0323 0.0281 0.0230 230 GLN A CD 1766 O OE1 . GLN A 214 ? 0.2774 0.2917 0.2204 0.0331 0.0292 0.0221 230 GLN A OE1 1767 N NE2 . GLN A 214 ? 0.2642 0.2841 0.2006 0.0333 0.0261 0.0240 230 GLN A NE2 1768 N N . ILE A 215 ? 0.2693 0.2910 0.2208 0.0256 0.0260 0.0138 231 ILE A N 1769 C CA . ILE A 215 ? 0.2656 0.2877 0.2217 0.0249 0.0254 0.0106 231 ILE A CA 1770 C C . ILE A 215 ? 0.2564 0.2829 0.2119 0.0253 0.0226 0.0093 231 ILE A C 1771 O O . ILE A 215 ? 0.2522 0.2795 0.2108 0.0258 0.0220 0.0068 231 ILE A O 1772 C CB . ILE A 215 ? 0.2625 0.2835 0.2197 0.0231 0.0255 0.0099 231 ILE A CB 1773 C CG1 . ILE A 215 ? 0.2728 0.2892 0.2311 0.0226 0.0288 0.0107 231 ILE A CG1 1774 C CG2 . ILE A 215 ? 0.2695 0.2915 0.2311 0.0225 0.0241 0.0065 231 ILE A CG2 1775 C CD1 . ILE A 215 ? 0.2729 0.2885 0.2308 0.0209 0.0293 0.0108 231 ILE A CD1 1776 N N . HIS A 216 ? 0.2518 0.2812 0.2031 0.0249 0.0210 0.0108 232 HIS A N 1777 C CA . HIS A 216 ? 0.2506 0.2841 0.2005 0.0251 0.0187 0.0101 232 HIS A CA 1778 C C . HIS A 216 ? 0.2517 0.2867 0.2024 0.0267 0.0188 0.0094 232 HIS A C 1779 O O . HIS A 216 ? 0.2436 0.2805 0.1958 0.0271 0.0178 0.0071 232 HIS A O 1780 C CB . HIS A 216 ? 0.2479 0.2838 0.1935 0.0244 0.0176 0.0123 232 HIS A CB 1781 C CG . HIS A 216 ? 0.2489 0.2889 0.1926 0.0244 0.0157 0.0119 232 HIS A CG 1782 N ND1 . HIS A 216 ? 0.2472 0.2898 0.1901 0.0256 0.0157 0.0121 232 HIS A ND1 1783 C CD2 . HIS A 216 ? 0.2501 0.2919 0.1923 0.0233 0.0140 0.0117 232 HIS A CD2 1784 C CE1 . HIS A 216 ? 0.2551 0.3009 0.1960 0.0251 0.0143 0.0117 232 HIS A CE1 1785 N NE2 . HIS A 216 ? 0.2468 0.2921 0.1871 0.0237 0.0133 0.0117 232 HIS A NE2 1786 N N . GLY A 217 ? 0.2590 0.2929 0.2087 0.0278 0.0200 0.0111 233 GLY A N 1787 C CA . GLY A 217 ? 0.2676 0.3028 0.2183 0.0295 0.0201 0.0104 233 GLY A CA 1788 C C . GLY A 217 ? 0.2665 0.3000 0.2221 0.0301 0.0209 0.0078 233 GLY A C 1789 O O . GLY A 217 ? 0.2659 0.3020 0.2230 0.0310 0.0201 0.0057 233 GLY A O 1790 N N . TYR A 218 ? 0.2689 0.2981 0.2271 0.0297 0.0227 0.0076 234 TYR A N 1791 C CA . TYR A 218 ? 0.2723 0.2994 0.2359 0.0301 0.0237 0.0049 234 TYR A CA 1792 C C . TYR A 218 ? 0.2699 0.2997 0.2358 0.0296 0.0218 0.0016 234 TYR A C 1793 O O . TYR A 218 ? 0.2765 0.3077 0.2454 0.0305 0.0213 -0.0010 234 TYR A O 1794 C CB . TYR A 218 ? 0.2808 0.3027 0.2470 0.0294 0.0263 0.0056 234 TYR A CB 1795 C CG . TYR A 218 ? 0.2874 0.3069 0.2598 0.0299 0.0278 0.0030 234 TYR A CG 1796 C CD1 . TYR A 218 ? 0.2889 0.3069 0.2627 0.0315 0.0289 0.0033 234 TYR A CD1 1797 C CD2 . TYR A 218 ? 0.2940 0.3130 0.2712 0.0289 0.0278 -0.0001 234 TYR A CD2 1798 C CE1 . TYR A 218 ? 0.3017 0.3175 0.2818 0.0320 0.0302 0.0007 234 TYR A CE1 1799 C CE2 . TYR A 218 ? 0.3072 0.3241 0.2907 0.0293 0.0291 -0.0029 234 TYR A CE2 1800 C CZ . TYR A 218 ? 0.3078 0.3232 0.2928 0.0308 0.0304 -0.0024 234 TYR A CZ 1801 O OH . TYR A 218 ? 0.3227 0.3360 0.3145 0.0312 0.0317 -0.0053 234 TYR A OH 1802 N N . VAL A 219 ? 0.2624 0.2928 0.2266 0.0282 0.0206 0.0017 235 VAL A N 1803 C CA . VAL A 219 ? 0.2606 0.2934 0.2260 0.0278 0.0184 -0.0010 235 VAL A CA 1804 C C . VAL A 219 ? 0.2622 0.2993 0.2251 0.0288 0.0166 -0.0018 235 VAL A C 1805 O O . VAL A 219 ? 0.2657 0.3042 0.2309 0.0295 0.0155 -0.0049 235 VAL A O 1806 C CB . VAL A 219 ? 0.2559 0.2885 0.2195 0.0263 0.0173 -0.0004 235 VAL A CB 1807 C CG1 . VAL A 219 ? 0.2520 0.2872 0.2153 0.0263 0.0145 -0.0028 235 VAL A CG1 1808 C CG2 . VAL A 219 ? 0.2535 0.2823 0.2212 0.0253 0.0191 -0.0011 235 VAL A CG2 1809 N N . ARG A 220 ? 0.2585 0.2977 0.2167 0.0288 0.0163 0.0007 236 ARG A N 1810 C CA . ARG A 220 ? 0.2618 0.3053 0.2176 0.0296 0.0151 0.0001 236 ARG A CA 1811 C C . ARG A 220 ? 0.2662 0.3102 0.2252 0.0313 0.0158 -0.0019 236 ARG A C 1812 O O . ARG A 220 ? 0.2577 0.3045 0.2169 0.0319 0.0147 -0.0044 236 ARG A O 1813 C CB . ARG A 220 ? 0.2571 0.3026 0.2084 0.0292 0.0151 0.0031 236 ARG A CB 1814 C CG . ARG A 220 ? 0.2542 0.3041 0.2032 0.0298 0.0144 0.0027 236 ARG A CG 1815 C CD . ARG A 220 ? 0.2507 0.3027 0.1959 0.0291 0.0143 0.0054 236 ARG A CD 1816 N NE . ARG A 220 ? 0.2431 0.2932 0.1888 0.0296 0.0155 0.0074 236 ARG A NE 1817 C CZ . ARG A 220 ? 0.2506 0.3016 0.1937 0.0292 0.0155 0.0097 236 ARG A CZ 1818 N NH1 . ARG A 220 ? 0.2466 0.3007 0.1870 0.0280 0.0146 0.0105 236 ARG A NH1 1819 N NH2 . ARG A 220 ? 0.2347 0.2836 0.1782 0.0300 0.0164 0.0113 236 ARG A NH2 1820 N N . PHE A 221 ? 0.2734 0.3147 0.2347 0.0320 0.0176 -0.0010 237 PHE A N 1821 C CA . PHE A 221 ? 0.2852 0.3261 0.2506 0.0336 0.0185 -0.0029 237 PHE A CA 1822 C C . PHE A 221 ? 0.2874 0.3279 0.2574 0.0338 0.0180 -0.0068 237 PHE A C 1823 O O . PHE A 221 ? 0.2863 0.3295 0.2578 0.0349 0.0172 -0.0096 237 PHE A O 1824 C CB . PHE A 221 ? 0.2946 0.3314 0.2615 0.0341 0.0206 -0.0007 237 PHE A CB 1825 C CG . PHE A 221 ? 0.3077 0.3422 0.2799 0.0354 0.0219 -0.0028 237 PHE A CG 1826 C CD1 . PHE A 221 ? 0.3088 0.3460 0.2825 0.0370 0.0213 -0.0044 237 PHE A CD1 1827 C CD2 . PHE A 221 ? 0.3067 0.3363 0.2830 0.0350 0.0238 -0.0030 237 PHE A CD2 1828 C CE1 . PHE A 221 ? 0.3161 0.3510 0.2952 0.0383 0.0225 -0.0064 237 PHE A CE1 1829 C CE2 . PHE A 221 ? 0.3151 0.3423 0.2968 0.0361 0.0251 -0.0048 237 PHE A CE2 1830 C CZ . PHE A 221 ? 0.3171 0.3469 0.3003 0.0378 0.0244 -0.0065 237 PHE A CZ 1831 N N . ARG A 222 ? 0.2855 0.3230 0.2579 0.0327 0.0184 -0.0073 238 ARG A N 1832 C CA . ARG A 222 ? 0.2886 0.3257 0.2661 0.0329 0.0178 -0.0114 238 ARG A CA 1833 C C . ARG A 222 ? 0.2871 0.3281 0.2624 0.0331 0.0150 -0.0137 238 ARG A C 1834 O O . ARG A 222 ? 0.2986 0.3409 0.2771 0.0340 0.0141 -0.0175 238 ARG A O 1835 C CB . ARG A 222 ? 0.2976 0.3305 0.2788 0.0317 0.0192 -0.0115 238 ARG A CB 1836 C CG . ARG A 222 ? 0.2993 0.3278 0.2831 0.0318 0.0223 -0.0097 238 ARG A CG 1837 C CD . ARG A 222 ? 0.3112 0.3388 0.3006 0.0331 0.0233 -0.0122 238 ARG A CD 1838 N NE . ARG A 222 ? 0.3229 0.3504 0.3184 0.0329 0.0228 -0.0167 238 ARG A NE 1839 C CZ . ARG A 222 ? 0.3373 0.3610 0.3381 0.0319 0.0247 -0.0177 238 ARG A CZ 1840 N NH1 . ARG A 222 ? 0.3402 0.3596 0.3403 0.0311 0.0275 -0.0144 238 ARG A NH1 1841 N NH2 . ARG A 222 ? 0.3482 0.3724 0.3548 0.0319 0.0238 -0.0222 238 ARG A NH2 1842 N N . LEU A 223 ? 0.2837 0.3264 0.2533 0.0322 0.0137 -0.0115 239 LEU A N 1843 C CA . LEU A 223 ? 0.2841 0.3302 0.2504 0.0323 0.0111 -0.0131 239 LEU A CA 1844 C C . LEU A 223 ? 0.2875 0.3374 0.2519 0.0336 0.0107 -0.0143 239 LEU A C 1845 O O . LEU A 223 ? 0.2791 0.3313 0.2428 0.0344 0.0089 -0.0172 239 LEU A O 1846 C CB . LEU A 223 ? 0.2822 0.3287 0.2430 0.0310 0.0100 -0.0102 239 LEU A CB 1847 C CG . LEU A 223 ? 0.2797 0.3233 0.2421 0.0297 0.0096 -0.0100 239 LEU A CG 1848 C CD1 . LEU A 223 ? 0.2795 0.3234 0.2365 0.0284 0.0089 -0.0067 239 LEU A CD1 1849 C CD2 . LEU A 223 ? 0.2785 0.3220 0.2439 0.0302 0.0076 -0.0138 239 LEU A CD2 1850 N N . ARG A 224 ? 0.2887 0.3394 0.2522 0.0340 0.0122 -0.0124 240 ARG A N 1851 C CA . ARG A 224 ? 0.2999 0.3543 0.2625 0.0352 0.0122 -0.0137 240 ARG A CA 1852 C C . ARG A 224 ? 0.3086 0.3633 0.2767 0.0368 0.0121 -0.0180 240 ARG A C 1853 O O . ARG A 224 ? 0.3133 0.3713 0.2804 0.0377 0.0110 -0.0207 240 ARG A O 1854 C CB . ARG A 224 ? 0.3034 0.3582 0.2652 0.0355 0.0138 -0.0110 240 ARG A CB 1855 C CG . ARG A 224 ? 0.3014 0.3574 0.2577 0.0342 0.0136 -0.0074 240 ARG A CG 1856 C CD . ARG A 224 ? 0.3011 0.3575 0.2571 0.0347 0.0149 -0.0051 240 ARG A CD 1857 N NE . ARG A 224 ? 0.2993 0.3587 0.2567 0.0362 0.0152 -0.0070 240 ARG A NE 1858 C CZ . ARG A 224 ? 0.3037 0.3624 0.2638 0.0374 0.0162 -0.0066 240 ARG A CZ 1859 N NH1 . ARG A 224 ? 0.2901 0.3449 0.2511 0.0375 0.0171 -0.0041 240 ARG A NH1 1860 N NH2 . ARG A 224 ? 0.2982 0.3601 0.2600 0.0388 0.0164 -0.0086 240 ARG A NH2 1861 N N . LYS A 225 ? 0.3169 0.3677 0.2907 0.0369 0.0133 -0.0187 241 LYS A N 1862 C CA . LYS A 225 ? 0.3276 0.3780 0.3078 0.0382 0.0135 -0.0229 241 LYS A CA 1863 C C . LYS A 225 ? 0.3271 0.3789 0.3080 0.0384 0.0112 -0.0266 241 LYS A C 1864 O O . LYS A 225 ? 0.3465 0.4005 0.3302 0.0397 0.0103 -0.0306 241 LYS A O 1865 C CB . LYS A 225 ? 0.3340 0.3793 0.3201 0.0380 0.0156 -0.0224 241 LYS A CB 1866 C CG . LYS A 225 ? 0.3554 0.3988 0.3407 0.0382 0.0177 -0.0188 241 LYS A CG 1867 C CD . LYS A 225 ? 0.3804 0.4185 0.3713 0.0382 0.0200 -0.0184 241 LYS A CD 1868 C CE . LYS A 225 ? 0.4016 0.4395 0.3993 0.0396 0.0204 -0.0225 241 LYS A CE 1869 N NZ . LYS A 225 ? 0.4205 0.4529 0.4230 0.0397 0.0231 -0.0213 241 LYS A NZ 1870 N N . HIS A 226 ? 0.3177 0.3684 0.2962 0.0371 0.0101 -0.0255 242 HIS A N 1871 C CA . HIS A 226 ? 0.3069 0.3587 0.2857 0.0375 0.0075 -0.0289 242 HIS A CA 1872 C C . HIS A 226 ? 0.2983 0.3543 0.2704 0.0381 0.0054 -0.0293 242 HIS A C 1873 O O . HIS A 226 ? 0.2988 0.3572 0.2717 0.0395 0.0037 -0.0332 242 HIS A O 1874 C CB . HIS A 226 ? 0.3069 0.3558 0.2862 0.0361 0.0070 -0.0277 242 HIS A CB 1875 C CG . HIS A 226 ? 0.3171 0.3666 0.2983 0.0366 0.0043 -0.0316 242 HIS A CG 1876 N ND1 . HIS A 226 ? 0.3224 0.3703 0.3116 0.0371 0.0043 -0.0356 242 HIS A ND1 1877 C CD2 . HIS A 226 ? 0.3193 0.3707 0.2956 0.0369 0.0013 -0.0322 242 HIS A CD2 1878 C CE1 . HIS A 226 ? 0.3196 0.3686 0.3088 0.0377 0.0013 -0.0388 242 HIS A CE1 1879 N NE2 . HIS A 226 ? 0.3202 0.3712 0.3013 0.0377 -0.0006 -0.0366 242 HIS A NE2 1880 N N . TYR A 227 ? 0.2911 0.3480 0.2565 0.0371 0.0054 -0.0253 243 TYR A N 1881 C CA . TYR A 227 ? 0.2853 0.3456 0.2436 0.0374 0.0037 -0.0252 243 TYR A CA 1882 C C . TYR A 227 ? 0.2867 0.3507 0.2423 0.0380 0.0048 -0.0251 243 TYR A C 1883 O O . TYR A 227 ? 0.2820 0.3492 0.2328 0.0386 0.0036 -0.0263 243 TYR A O 1884 C CB . TYR A 227 ? 0.2875 0.3468 0.2401 0.0358 0.0030 -0.0213 243 TYR A CB 1885 C CG . TYR A 227 ? 0.2880 0.3446 0.2421 0.0353 0.0012 -0.0220 243 TYR A CG 1886 C CD1 . TYR A 227 ? 0.2878 0.3452 0.2393 0.0362 -0.0016 -0.0243 243 TYR A CD1 1887 C CD2 . TYR A 227 ? 0.2808 0.3339 0.2386 0.0341 0.0023 -0.0204 243 TYR A CD2 1888 C CE1 . TYR A 227 ? 0.2870 0.3420 0.2402 0.0359 -0.0036 -0.0252 243 TYR A CE1 1889 C CE2 . TYR A 227 ? 0.2781 0.3289 0.2377 0.0337 0.0006 -0.0213 243 TYR A CE2 1890 C CZ . TYR A 227 ? 0.2840 0.3359 0.2416 0.0346 -0.0024 -0.0238 243 TYR A CZ 1891 O OH . TYR A 227 ? 0.2828 0.3326 0.2424 0.0344 -0.0044 -0.0250 243 TYR A OH 1892 N N . GLY A 228 ? 0.2801 0.3437 0.2387 0.0380 0.0070 -0.0238 244 GLY A N 1893 C CA . GLY A 228 ? 0.2874 0.3544 0.2442 0.0386 0.0082 -0.0235 244 GLY A CA 1894 C C . GLY A 228 ? 0.2913 0.3596 0.2426 0.0372 0.0091 -0.0194 244 GLY A C 1895 O O . GLY A 228 ? 0.2907 0.3576 0.2383 0.0359 0.0083 -0.0168 244 GLY A O 1896 N N . ASP A 229 ? 0.3011 0.3720 0.2523 0.0376 0.0105 -0.0189 245 ASP A N 1897 C CA . ASP A 229 ? 0.3132 0.3853 0.2606 0.0364 0.0115 -0.0151 245 ASP A CA 1898 C C . ASP A 229 ? 0.3080 0.3829 0.2486 0.0353 0.0111 -0.0141 245 ASP A C 1899 O O . ASP A 229 ? 0.3070 0.3825 0.2445 0.0340 0.0118 -0.0109 245 ASP A O 1900 C CB . ASP A 229 ? 0.3375 0.4114 0.2878 0.0373 0.0131 -0.0152 245 ASP A CB 1901 C CG . ASP A 229 ? 0.3636 0.4336 0.3189 0.0378 0.0139 -0.0141 245 ASP A CG 1902 O OD1 . ASP A 229 ? 0.3901 0.4573 0.3496 0.0385 0.0137 -0.0160 245 ASP A OD1 1903 O OD2 . ASP A 229 ? 0.3963 0.4660 0.3512 0.0375 0.0147 -0.0114 245 ASP A OD2 1904 N N . ALA A 230 ? 0.2942 0.3708 0.2324 0.0360 0.0099 -0.0167 246 ALA A N 1905 C CA . ALA A 230 ? 0.2964 0.3747 0.2274 0.0350 0.0094 -0.0154 246 ALA A CA 1906 C C . ALA A 230 ? 0.2922 0.3670 0.2203 0.0336 0.0081 -0.0126 246 ALA A C 1907 O O . ALA A 230 ? 0.3067 0.3821 0.2294 0.0323 0.0081 -0.0100 246 ALA A O 1908 C CB . ALA A 230 ? 0.2975 0.3782 0.2261 0.0363 0.0083 -0.0189 246 ALA A CB 1909 N N . VAL A 231 ? 0.2738 0.3450 0.2061 0.0338 0.0071 -0.0130 247 VAL A N 1910 C CA . VAL A 231 ? 0.2614 0.3293 0.1922 0.0327 0.0056 -0.0110 247 VAL A CA 1911 C C . VAL A 231 ? 0.2632 0.3288 0.1961 0.0314 0.0069 -0.0078 247 VAL A C 1912 O O . VAL A 231 ? 0.2656 0.3298 0.1955 0.0299 0.0065 -0.0050 247 VAL A O 1913 C CB . VAL A 231 ? 0.2569 0.3224 0.1912 0.0338 0.0037 -0.0141 247 VAL A CB 1914 C CG1 . VAL A 231 ? 0.2491 0.3113 0.1823 0.0327 0.0020 -0.0125 247 VAL A CG1 1915 C CG2 . VAL A 231 ? 0.2585 0.3264 0.1904 0.0353 0.0021 -0.0176 247 VAL A CG2 1916 N N . VAL A 232 ? 0.2544 0.3195 0.1923 0.0320 0.0083 -0.0083 248 VAL A N 1917 C CA . VAL A 232 ? 0.2532 0.3158 0.1931 0.0311 0.0094 -0.0056 248 VAL A CA 1918 C C . VAL A 232 ? 0.2667 0.3314 0.2078 0.0316 0.0112 -0.0048 248 VAL A C 1919 O O . VAL A 232 ? 0.2769 0.3423 0.2215 0.0330 0.0118 -0.0070 248 VAL A O 1920 C CB . VAL A 232 ? 0.2462 0.3050 0.1914 0.0315 0.0093 -0.0068 248 VAL A CB 1921 C CG1 . VAL A 232 ? 0.2302 0.2863 0.1765 0.0306 0.0106 -0.0038 248 VAL A CG1 1922 C CG2 . VAL A 232 ? 0.2358 0.2928 0.1809 0.0312 0.0074 -0.0082 248 VAL A CG2 1923 N N . SER A 233 ? 0.2764 0.3420 0.2149 0.0304 0.0118 -0.0018 249 SER A N 1924 C CA . SER A 233 ? 0.2876 0.3552 0.2274 0.0310 0.0132 -0.0011 249 SER A CA 1925 C C . SER A 233 ? 0.2842 0.3485 0.2272 0.0314 0.0138 0.0002 249 SER A C 1926 O O . SER A 233 ? 0.2704 0.3313 0.2136 0.0306 0.0135 0.0013 249 SER A O 1927 C CB . SER A 233 ? 0.3012 0.3718 0.2372 0.0297 0.0136 0.0009 249 SER A CB 1928 O OG . SER A 233 ? 0.3217 0.3903 0.2568 0.0284 0.0135 0.0038 249 SER A OG 1929 N N . GLU A 234 ? 0.2829 0.3480 0.2283 0.0326 0.0147 0.0001 250 GLU A N 1930 C CA . GLU A 234 ? 0.2868 0.3484 0.2344 0.0332 0.0154 0.0017 250 GLU A CA 1931 C C . GLU A 234 ? 0.2818 0.3431 0.2268 0.0321 0.0154 0.0048 250 GLU A C 1932 O O . GLU A 234 ? 0.2841 0.3417 0.2295 0.0320 0.0157 0.0065 250 GLU A O 1933 C CB . GLU A 234 ? 0.3027 0.3653 0.2534 0.0352 0.0161 0.0006 250 GLU A CB 1934 C CG . GLU A 234 ? 0.3126 0.3713 0.2649 0.0361 0.0168 0.0026 250 GLU A CG 1935 C CD . GLU A 234 ? 0.3326 0.3920 0.2879 0.0383 0.0172 0.0017 250 GLU A CD 1936 O OE1 . GLU A 234 ? 0.3432 0.4072 0.2986 0.0388 0.0169 0.0003 250 GLU A OE1 1937 O OE2 . GLU A 234 ? 0.3379 0.3932 0.2956 0.0394 0.0178 0.0023 250 GLU A OE2 1938 N N . THR A 235 ? 0.2792 0.3442 0.2215 0.0313 0.0152 0.0055 251 THR A N 1939 C CA . THR A 235 ? 0.2798 0.3453 0.2205 0.0305 0.0151 0.0080 251 THR A CA 1940 C C . THR A 235 ? 0.2694 0.3349 0.2069 0.0283 0.0146 0.0095 251 THR A C 1941 O O . THR A 235 ? 0.2603 0.3255 0.1968 0.0276 0.0144 0.0114 251 THR A O 1942 C CB . THR A 235 ? 0.2819 0.3517 0.2229 0.0312 0.0155 0.0078 251 THR A CB 1943 O OG1 . THR A 235 ? 0.3020 0.3757 0.2419 0.0306 0.0157 0.0062 251 THR A OG1 1944 C CG2 . THR A 235 ? 0.2860 0.3552 0.2303 0.0335 0.0158 0.0068 251 THR A CG2 1945 N N . GLY A 236 ? 0.2574 0.3232 0.1934 0.0275 0.0141 0.0085 252 GLY A N 1946 C CA . GLY A 236 ? 0.2472 0.3127 0.1801 0.0256 0.0134 0.0100 252 GLY A CA 1947 C C . GLY A 236 ? 0.2373 0.2986 0.1706 0.0250 0.0126 0.0104 252 GLY A C 1948 O O . GLY A 236 ? 0.2391 0.2977 0.1750 0.0260 0.0127 0.0092 252 GLY A O 1949 N N . PRO A 237 ? 0.2348 0.2955 0.1658 0.0233 0.0118 0.0118 253 PRO A N 1950 C CA . PRO A 237 ? 0.2360 0.2931 0.1675 0.0227 0.0109 0.0118 253 PRO A CA 1951 C C . PRO A 237 ? 0.2440 0.3000 0.1764 0.0236 0.0101 0.0094 253 PRO A C 1952 O O . PRO A 237 ? 0.2503 0.3087 0.1812 0.0241 0.0099 0.0082 253 PRO A O 1953 C CB . PRO A 237 ? 0.2351 0.2925 0.1636 0.0210 0.0100 0.0135 253 PRO A CB 1954 C CG . PRO A 237 ? 0.2319 0.2927 0.1590 0.0204 0.0108 0.0148 253 PRO A CG 1955 C CD . PRO A 237 ? 0.2313 0.2945 0.1595 0.0219 0.0118 0.0133 253 PRO A CD 1956 N N . ILE A 238 ? 0.2412 0.2939 0.1761 0.0237 0.0097 0.0085 254 ILE A N 1957 C CA . ILE A 238 ? 0.2456 0.2973 0.1821 0.0245 0.0087 0.0059 254 ILE A CA 1958 C C . ILE A 238 ? 0.2435 0.2955 0.1767 0.0239 0.0067 0.0057 254 ILE A C 1959 O O . ILE A 238 ? 0.2406 0.2914 0.1723 0.0226 0.0059 0.0074 254 ILE A O 1960 C CB . ILE A 238 ? 0.2498 0.2979 0.1907 0.0247 0.0090 0.0047 254 ILE A CB 1961 C CG1 . ILE A 238 ? 0.2473 0.2944 0.1907 0.0254 0.0111 0.0053 254 ILE A CG1 1962 C CG2 . ILE A 238 ? 0.2509 0.2982 0.1943 0.0256 0.0079 0.0015 254 ILE A CG2 1963 C CD1 . ILE A 238 ? 0.2531 0.2965 0.2004 0.0253 0.0122 0.0048 254 ILE A CD1 1964 N N . PRO A 239 ? 0.2438 0.2974 0.1756 0.0248 0.0058 0.0038 255 PRO A N 1965 C CA . PRO A 239 ? 0.2444 0.2975 0.1729 0.0246 0.0036 0.0036 255 PRO A CA 1966 C C . PRO A 239 ? 0.2439 0.2937 0.1754 0.0245 0.0021 0.0024 255 PRO A C 1967 O O . PRO A 239 ? 0.2390 0.2877 0.1749 0.0255 0.0020 -0.0002 255 PRO A O 1968 C CB . PRO A 239 ? 0.2430 0.2983 0.1700 0.0260 0.0031 0.0011 255 PRO A CB 1969 C CG . PRO A 239 ? 0.2426 0.3005 0.1710 0.0265 0.0053 0.0009 255 PRO A CG 1970 C CD . PRO A 239 ? 0.2432 0.2991 0.1760 0.0263 0.0066 0.0017 255 PRO A CD 1971 N N . MET A 240 ? 0.2494 0.2977 0.1790 0.0233 0.0009 0.0042 256 MET A N 1972 C CA . MET A 240 ? 0.2521 0.2973 0.1851 0.0230 0.0000 0.0035 256 MET A CA 1973 C C . MET A 240 ? 0.2530 0.2971 0.1879 0.0242 -0.0023 0.0002 256 MET A C 1974 O O . MET A 240 ? 0.2502 0.2923 0.1899 0.0242 -0.0027 -0.0014 256 MET A O 1975 C CB . MET A 240 ? 0.2541 0.2982 0.1848 0.0214 -0.0007 0.0062 256 MET A CB 1976 C CG . MET A 240 ? 0.2619 0.3057 0.1879 0.0213 -0.0031 0.0070 256 MET A CG 1977 S SD . MET A 240 ? 0.2616 0.3040 0.1855 0.0193 -0.0034 0.0104 256 MET A SD 1978 C CE . MET A 240 ? 0.2587 0.2981 0.1884 0.0191 -0.0042 0.0088 256 MET A CE 1979 N N . HIS A 241 ? 0.2526 0.2982 0.1838 0.0253 -0.0039 -0.0007 257 HIS A N 1980 C CA . HIS A 241 ? 0.2569 0.3017 0.1893 0.0267 -0.0066 -0.0039 257 HIS A CA 1981 C C . HIS A 241 ? 0.2552 0.3003 0.1937 0.0279 -0.0059 -0.0077 257 HIS A C 1982 O O . HIS A 241 ? 0.2579 0.3024 0.1991 0.0291 -0.0081 -0.0110 257 HIS A O 1983 C CB . HIS A 241 ? 0.2527 0.2988 0.1785 0.0276 -0.0085 -0.0038 257 HIS A CB 1984 C CG . HIS A 241 ? 0.2583 0.3076 0.1818 0.0283 -0.0068 -0.0042 257 HIS A CG 1985 N ND1 . HIS A 241 ? 0.2546 0.3056 0.1781 0.0274 -0.0039 -0.0022 257 HIS A ND1 1986 C CD2 . HIS A 241 ? 0.2556 0.3067 0.1767 0.0299 -0.0079 -0.0066 257 HIS A CD2 1987 C CE1 . HIS A 241 ? 0.2555 0.3093 0.1772 0.0283 -0.0031 -0.0034 257 HIS A CE1 1988 N NE2 . HIS A 241 ? 0.2551 0.3091 0.1751 0.0298 -0.0054 -0.0060 257 HIS A NE2 1989 N N . LEU A 242 ? 0.2484 0.2944 0.1893 0.0277 -0.0031 -0.0073 258 LEU A N 1990 C CA . LEU A 242 ? 0.2490 0.2950 0.1959 0.0288 -0.0020 -0.0105 258 LEU A CA 1991 C C . LEU A 242 ? 0.2477 0.2909 0.2007 0.0279 -0.0006 -0.0109 258 LEU A C 1992 O O . LEU A 242 ? 0.2490 0.2915 0.2076 0.0285 0.0006 -0.0134 258 LEU A O 1993 C CB . LEU A 242 ? 0.2463 0.2945 0.1926 0.0292 0.0003 -0.0099 258 LEU A CB 1994 C CG . LEU A 242 ? 0.2514 0.3027 0.1917 0.0297 -0.0002 -0.0092 258 LEU A CG 1995 C CD1 . LEU A 242 ? 0.2488 0.3022 0.1897 0.0300 0.0022 -0.0088 258 LEU A CD1 1996 C CD2 . LEU A 242 ? 0.2524 0.3048 0.1917 0.0313 -0.0027 -0.0126 258 LEU A CD2 1997 N N . LEU A 243 ? 0.2488 0.2904 0.2008 0.0265 -0.0006 -0.0085 259 LEU A N 1998 C CA . LEU A 243 ? 0.2450 0.2841 0.2017 0.0255 0.0012 -0.0083 259 LEU A CA 1999 C C . LEU A 243 ? 0.2473 0.2844 0.2089 0.0254 -0.0002 -0.0111 259 LEU A C 2000 O O . LEU A 243 ? 0.2433 0.2783 0.2086 0.0244 0.0013 -0.0110 259 LEU A O 2001 C CB . LEU A 243 ? 0.2418 0.2806 0.1951 0.0240 0.0026 -0.0042 259 LEU A CB 2002 C CG . LEU A 243 ? 0.2451 0.2855 0.1958 0.0242 0.0047 -0.0020 259 LEU A CG 2003 C CD1 . LEU A 243 ? 0.2349 0.2757 0.1816 0.0229 0.0052 0.0015 259 LEU A CD1 2004 C CD2 . LEU A 243 ? 0.2391 0.2781 0.1943 0.0246 0.0074 -0.0028 259 LEU A CD2 2005 N N . GLY A 244 ? 0.2421 0.2799 0.2035 0.0265 -0.0033 -0.0137 260 GLY A N 2006 C CA . GLY A 244 ? 0.2506 0.2870 0.2177 0.0269 -0.0050 -0.0173 260 GLY A CA 2007 C C . GLY A 244 ? 0.2529 0.2876 0.2195 0.0259 -0.0066 -0.0163 260 GLY A C 2008 O O . GLY A 244 ? 0.2606 0.2941 0.2328 0.0260 -0.0078 -0.0193 260 GLY A O 2009 N N . ASN A 245 ? 0.2483 0.2831 0.2091 0.0249 -0.0067 -0.0123 261 ASN A N 2010 C CA . ASN A 245 ? 0.2536 0.2869 0.2137 0.0240 -0.0083 -0.0111 261 ASN A CA 2011 C C . ASN A 245 ? 0.2612 0.2952 0.2136 0.0238 -0.0098 -0.0077 261 ASN A C 2012 O O . ASN A 245 ? 0.2597 0.2951 0.2081 0.0233 -0.0079 -0.0050 261 ASN A O 2013 C CB . ASN A 245 ? 0.2478 0.2797 0.2110 0.0223 -0.0052 -0.0097 261 ASN A CB 2014 C CG . ASN A 245 ? 0.2402 0.2709 0.2029 0.0212 -0.0066 -0.0085 261 ASN A CG 2015 O OD1 . ASN A 245 ? 0.2376 0.2686 0.1953 0.0204 -0.0068 -0.0052 261 ASN A OD1 2016 N ND2 . ASN A 245 ? 0.2452 0.2745 0.2136 0.0211 -0.0075 -0.0114 261 ASN A ND2 2017 N N . MET A 246 ? 0.2746 0.3076 0.2251 0.0242 -0.0131 -0.0078 262 MET A N 2018 C CA . MET A 246 ? 0.2705 0.3036 0.2135 0.0240 -0.0147 -0.0045 262 MET A CA 2019 C C . MET A 246 ? 0.2672 0.3007 0.2072 0.0221 -0.0122 -0.0004 262 MET A C 2020 O O . MET A 246 ? 0.2671 0.3016 0.2012 0.0219 -0.0121 0.0022 262 MET A O 2021 C CB . MET A 246 ? 0.2771 0.3081 0.2193 0.0246 -0.0186 -0.0051 262 MET A CB 2022 C CG . MET A 246 ? 0.2803 0.3108 0.2145 0.0245 -0.0203 -0.0016 262 MET A CG 2023 S SD . MET A 246 ? 0.2922 0.3245 0.2197 0.0263 -0.0213 -0.0018 262 MET A SD 2024 C CE . MET A 246 ? 0.3067 0.3375 0.2361 0.0288 -0.0261 -0.0060 262 MET A CE 2025 N N . TRP A 247 ? 0.2579 0.2907 0.2021 0.0209 -0.0102 -0.0002 263 TRP A N 2026 C CA . TRP A 247 ? 0.2621 0.2952 0.2042 0.0192 -0.0080 0.0031 263 TRP A CA 2027 C C . TRP A 247 ? 0.2545 0.2889 0.1983 0.0189 -0.0045 0.0035 263 TRP A C 2028 O O . TRP A 247 ? 0.2606 0.2955 0.2032 0.0178 -0.0027 0.0058 263 TRP A O 2029 C CB . TRP A 247 ? 0.2558 0.2870 0.2005 0.0181 -0.0088 0.0034 263 TRP A CB 2030 C CG . TRP A 247 ? 0.2620 0.2915 0.2056 0.0188 -0.0127 0.0027 263 TRP A CG 2031 C CD1 . TRP A 247 ? 0.2643 0.2932 0.2026 0.0185 -0.0145 0.0052 263 TRP A CD1 2032 C CD2 . TRP A 247 ? 0.2608 0.2891 0.2086 0.0200 -0.0151 -0.0008 263 TRP A CD2 2033 N NE1 . TRP A 247 ? 0.2684 0.2955 0.2069 0.0197 -0.0181 0.0037 263 TRP A NE1 2034 C CE2 . TRP A 247 ? 0.2683 0.2951 0.2127 0.0206 -0.0187 -0.0001 263 TRP A CE2 2035 C CE3 . TRP A 247 ? 0.2613 0.2894 0.2155 0.0205 -0.0146 -0.0046 263 TRP A CE3 2036 C CZ2 . TRP A 247 ? 0.2656 0.2909 0.2128 0.0221 -0.0222 -0.0032 263 TRP A CZ2 2037 C CZ3 . TRP A 247 ? 0.2674 0.2944 0.2252 0.0218 -0.0177 -0.0079 263 TRP A CZ3 2038 C CH2 . TRP A 247 ? 0.2660 0.2917 0.2202 0.0226 -0.0217 -0.0073 263 TRP A CH2 2039 N N . ALA A 248 ? 0.2520 0.2868 0.1986 0.0201 -0.0038 0.0010 264 ALA A N 2040 C CA . ALA A 248 ? 0.2539 0.2891 0.2027 0.0201 -0.0006 0.0009 264 ALA A CA 2041 C C . ALA A 248 ? 0.2535 0.2872 0.2053 0.0189 0.0013 0.0016 264 ALA A C 2042 O O . ALA A 248 ? 0.2558 0.2897 0.2071 0.0186 0.0038 0.0031 264 ALA A O 2043 C CB . ALA A 248 ? 0.2508 0.2884 0.1952 0.0202 0.0006 0.0033 264 ALA A CB 2044 N N . GLN A 249 ? 0.2558 0.2878 0.2106 0.0183 0.0001 0.0003 265 GLN A N 2045 C CA . GLN A 249 ? 0.2525 0.2831 0.2097 0.0171 0.0021 0.0009 265 GLN A CA 2046 C C . GLN A 249 ? 0.2569 0.2862 0.2190 0.0171 0.0049 -0.0009 265 GLN A C 2047 O O . GLN A 249 ? 0.2441 0.2724 0.2066 0.0163 0.0074 0.0002 265 GLN A O 2048 C CB . GLN A 249 ? 0.2606 0.2900 0.2194 0.0163 0.0000 0.0002 265 GLN A CB 2049 C CG . GLN A 249 ? 0.2750 0.3033 0.2390 0.0169 -0.0015 -0.0035 265 GLN A CG 2050 C CD . GLN A 249 ? 0.2981 0.3255 0.2628 0.0165 -0.0045 -0.0040 265 GLN A CD 2051 O OE1 . GLN A 249 ? 0.2971 0.3248 0.2573 0.0164 -0.0065 -0.0017 265 GLN A OE1 2052 N NE2 . GLN A 249 ? 0.3158 0.3419 0.2864 0.0163 -0.0047 -0.0070 265 GLN A NE2 2053 N N . GLN A 250 ? 0.2584 0.2874 0.2241 0.0181 0.0044 -0.0039 266 GLN A N 2054 C CA . GLN A 250 ? 0.2717 0.2993 0.2425 0.0182 0.0072 -0.0059 266 GLN A CA 2055 C C . GLN A 250 ? 0.2622 0.2908 0.2339 0.0197 0.0066 -0.0077 266 GLN A C 2056 O O . GLN A 250 ? 0.2575 0.2874 0.2280 0.0206 0.0035 -0.0090 266 GLN A O 2057 C CB . GLN A 250 ? 0.2909 0.3168 0.2680 0.0176 0.0071 -0.0091 266 GLN A CB 2058 C CG . GLN A 250 ? 0.3241 0.3491 0.3011 0.0162 0.0078 -0.0078 266 GLN A CG 2059 C CD . GLN A 250 ? 0.3524 0.3758 0.3364 0.0154 0.0087 -0.0112 266 GLN A CD 2060 O OE1 . GLN A 250 ? 0.3710 0.3946 0.3592 0.0160 0.0063 -0.0145 266 GLN A OE1 2061 N NE2 . GLN A 250 ? 0.3555 0.3775 0.3407 0.0142 0.0122 -0.0104 266 GLN A NE2 2062 N N . TRP A 251 ? 0.2512 0.2791 0.2248 0.0200 0.0094 -0.0078 267 TRP A N 2063 C CA . TRP A 251 ? 0.2534 0.2826 0.2275 0.0215 0.0090 -0.0093 267 TRP A CA 2064 C C . TRP A 251 ? 0.2587 0.2865 0.2401 0.0219 0.0100 -0.0133 267 TRP A C 2065 O O . TRP A 251 ? 0.2546 0.2832 0.2374 0.0231 0.0102 -0.0147 267 TRP A O 2066 C CB . TRP A 251 ? 0.2426 0.2725 0.2129 0.0219 0.0109 -0.0065 267 TRP A CB 2067 C CG . TRP A 251 ? 0.2384 0.2700 0.2021 0.0215 0.0101 -0.0029 267 TRP A CG 2068 C CD1 . TRP A 251 ? 0.2336 0.2663 0.1940 0.0210 0.0077 -0.0019 267 TRP A CD1 2069 C CD2 . TRP A 251 ? 0.2402 0.2724 0.2003 0.0217 0.0118 0.0000 267 TRP A CD2 2070 N NE1 . TRP A 251 ? 0.2366 0.2707 0.1918 0.0206 0.0080 0.0012 267 TRP A NE1 2071 C CE2 . TRP A 251 ? 0.2388 0.2729 0.1940 0.0211 0.0104 0.0024 267 TRP A CE2 2072 C CE3 . TRP A 251 ? 0.2422 0.2736 0.2031 0.0223 0.0143 0.0008 267 TRP A CE3 2073 C CZ2 . TRP A 251 ? 0.2413 0.2766 0.1925 0.0211 0.0113 0.0052 267 TRP A CZ2 2074 C CZ3 . TRP A 251 ? 0.2463 0.2789 0.2030 0.0226 0.0150 0.0037 267 TRP A CZ3 2075 C CH2 . TRP A 251 ? 0.2428 0.2776 0.1949 0.0219 0.0135 0.0057 267 TRP A CH2 2076 N N . SER A 252 ? 0.2656 0.2917 0.2523 0.0210 0.0108 -0.0152 268 SER A N 2077 C CA . SER A 252 ? 0.2788 0.3033 0.2732 0.0211 0.0126 -0.0188 268 SER A CA 2078 C C . SER A 252 ? 0.2841 0.3104 0.2818 0.0226 0.0097 -0.0230 268 SER A C 2079 O O . SER A 252 ? 0.2852 0.3108 0.2888 0.0230 0.0111 -0.0259 268 SER A O 2080 C CB . SER A 252 ? 0.2825 0.3048 0.2821 0.0196 0.0143 -0.0203 268 SER A CB 2081 O OG . SER A 252 ? 0.2874 0.3108 0.2869 0.0194 0.0111 -0.0215 268 SER A OG 2082 N N . GLU A 253 ? 0.2919 0.3203 0.2858 0.0235 0.0057 -0.0233 269 GLU A N 2083 C CA . GLU A 253 ? 0.3080 0.3382 0.3040 0.0252 0.0025 -0.0272 269 GLU A CA 2084 C C . GLU A 253 ? 0.3106 0.3423 0.3056 0.0265 0.0032 -0.0276 269 GLU A C 2085 O O . GLU A 253 ? 0.3109 0.3438 0.3093 0.0279 0.0014 -0.0316 269 GLU A O 2086 C CB . GLU A 253 ? 0.3253 0.3570 0.3165 0.0260 -0.0018 -0.0271 269 GLU A CB 2087 C CG . GLU A 253 ? 0.3488 0.3793 0.3428 0.0252 -0.0034 -0.0282 269 GLU A CG 2088 C CD . GLU A 253 ? 0.3713 0.4018 0.3735 0.0260 -0.0052 -0.0338 269 GLU A CD 2089 O OE1 . GLU A 253 ? 0.3860 0.4171 0.3926 0.0270 -0.0048 -0.0371 269 GLU A OE1 2090 O OE2 . GLU A 253 ? 0.3957 0.4256 0.4003 0.0258 -0.0072 -0.0353 269 GLU A OE2 2091 N N . ILE A 254 ? 0.3091 0.3408 0.2995 0.0261 0.0055 -0.0238 270 ILE A N 2092 C CA . ILE A 254 ? 0.3065 0.3396 0.2963 0.0274 0.0062 -0.0241 270 ILE A CA 2093 C C . ILE A 254 ? 0.3101 0.3408 0.3048 0.0269 0.0103 -0.0240 270 ILE A C 2094 O O . ILE A 254 ? 0.3089 0.3401 0.3030 0.0278 0.0114 -0.0236 270 ILE A O 2095 C CB . ILE A 254 ? 0.3066 0.3418 0.2879 0.0277 0.0055 -0.0205 270 ILE A CB 2096 C CG1 . ILE A 254 ? 0.3032 0.3371 0.2809 0.0264 0.0080 -0.0159 270 ILE A CG1 2097 C CG2 . ILE A 254 ? 0.3013 0.3386 0.2777 0.0283 0.0017 -0.0207 270 ILE A CG2 2098 C CD1 . ILE A 254 ? 0.3143 0.3501 0.2864 0.0268 0.0085 -0.0129 270 ILE A CD1 2099 N N . ALA A 255 ? 0.3047 0.3324 0.3040 0.0256 0.0125 -0.0244 271 ALA A N 2100 C CA . ALA A 255 ? 0.3152 0.3399 0.3192 0.0250 0.0166 -0.0242 271 ALA A CA 2101 C C . ALA A 255 ? 0.3279 0.3528 0.3375 0.0262 0.0172 -0.0276 271 ALA A C 2102 O O . ALA A 255 ? 0.3344 0.3575 0.3451 0.0263 0.0201 -0.0262 271 ALA A O 2103 C CB . ALA A 255 ? 0.3110 0.3329 0.3200 0.0233 0.0188 -0.0250 271 ALA A CB 2104 N N . ASP A 256 ? 0.3435 0.3706 0.3567 0.0272 0.0142 -0.0321 272 ASP A N 2105 C CA . ASP A 256 ? 0.3719 0.3996 0.3912 0.0284 0.0145 -0.0360 272 ASP A CA 2106 C C . ASP A 256 ? 0.3760 0.4055 0.3908 0.0298 0.0142 -0.0346 272 ASP A C 2107 O O . ASP A 256 ? 0.3842 0.4136 0.4039 0.0307 0.0152 -0.0371 272 ASP A O 2108 C CB . ASP A 256 ? 0.3925 0.4225 0.4161 0.0295 0.0108 -0.0415 272 ASP A CB 2109 C CG . ASP A 256 ? 0.4100 0.4435 0.4261 0.0308 0.0065 -0.0410 272 ASP A CG 2110 O OD1 . ASP A 256 ? 0.4282 0.4618 0.4387 0.0301 0.0052 -0.0382 272 ASP A OD1 2111 O OD2 . ASP A 256 ? 0.4391 0.4751 0.4547 0.0325 0.0046 -0.0435 272 ASP A OD2 2112 N N . ILE A 257 ? 0.3632 0.3946 0.3695 0.0300 0.0129 -0.0309 273 ILE A N 2113 C CA . ILE A 257 ? 0.3679 0.4012 0.3701 0.0312 0.0129 -0.0295 273 ILE A CA 2114 C C . ILE A 257 ? 0.3579 0.3894 0.3562 0.0306 0.0158 -0.0245 273 ILE A C 2115 O O . ILE A 257 ? 0.3657 0.3983 0.3621 0.0316 0.0163 -0.0235 273 ILE A O 2116 C CB . ILE A 257 ? 0.3811 0.4186 0.3771 0.0324 0.0093 -0.0300 273 ILE A CB 2117 C CG1 . ILE A 257 ? 0.3793 0.4173 0.3686 0.0314 0.0078 -0.0266 273 ILE A CG1 2118 C CG2 . ILE A 257 ? 0.3909 0.4302 0.3911 0.0336 0.0065 -0.0354 273 ILE A CG2 2119 C CD1 . ILE A 257 ? 0.3859 0.4274 0.3688 0.0323 0.0046 -0.0267 273 ILE A CD1 2120 N N . VAL A 258 ? 0.3393 0.3680 0.3366 0.0291 0.0175 -0.0216 274 VAL A N 2121 C CA . VAL A 258 ? 0.3359 0.3629 0.3291 0.0286 0.0199 -0.0170 274 VAL A CA 2122 C C . VAL A 258 ? 0.3401 0.3622 0.3373 0.0277 0.0237 -0.0159 274 VAL A C 2123 O O . VAL A 258 ? 0.3473 0.3674 0.3407 0.0274 0.0256 -0.0119 274 VAL A O 2124 C CB . VAL A 258 ? 0.3291 0.3575 0.3148 0.0279 0.0185 -0.0135 274 VAL A CB 2125 C CG1 . VAL A 258 ? 0.3279 0.3606 0.3091 0.0288 0.0154 -0.0140 274 VAL A CG1 2126 C CG2 . VAL A 258 ? 0.3355 0.3625 0.3224 0.0264 0.0183 -0.0137 274 VAL A CG2 2127 N N . SER A 259 ? 0.3444 0.3647 0.3491 0.0273 0.0248 -0.0194 275 SER A N 2128 C CA . SER A 259 ? 0.3560 0.3714 0.3651 0.0262 0.0288 -0.0187 275 SER A CA 2129 C C . SER A 259 ? 0.3481 0.3608 0.3569 0.0270 0.0315 -0.0163 275 SER A C 2130 O O . SER A 259 ? 0.3536 0.3676 0.3642 0.0285 0.0307 -0.0180 275 SER A O 2131 C CB . SER A 259 ? 0.3676 0.3820 0.3860 0.0257 0.0294 -0.0236 275 SER A CB 2132 O OG . SER A 259 ? 0.4222 0.4371 0.4416 0.0245 0.0284 -0.0249 275 SER A OG 2133 N N . PRO A 260 ? 0.3391 0.3478 0.3453 0.0262 0.0346 -0.0125 276 PRO A N 2134 C CA . PRO A 260 ? 0.3395 0.3449 0.3450 0.0271 0.0371 -0.0098 276 PRO A CA 2135 C C . PRO A 260 ? 0.3434 0.3466 0.3569 0.0276 0.0389 -0.0130 276 PRO A C 2136 O O . PRO A 260 ? 0.3460 0.3491 0.3596 0.0292 0.0388 -0.0125 276 PRO A O 2137 C CB . PRO A 260 ? 0.3407 0.3416 0.3433 0.0258 0.0404 -0.0062 276 PRO A CB 2138 C CG . PRO A 260 ? 0.3379 0.3417 0.3362 0.0248 0.0383 -0.0055 276 PRO A CG 2139 C CD . PRO A 260 ? 0.3375 0.3450 0.3402 0.0246 0.0354 -0.0101 276 PRO A CD 2140 N N . PHE A 261 ? 0.3356 0.3372 0.3564 0.0264 0.0403 -0.0163 277 PHE A N 2141 C CA . PHE A 261 ? 0.3408 0.3402 0.3704 0.0266 0.0422 -0.0197 277 PHE A CA 2142 C C . PHE A 261 ? 0.3488 0.3517 0.3853 0.0266 0.0397 -0.0257 277 PHE A C 2143 O O . PHE A 261 ? 0.3438 0.3454 0.3862 0.0251 0.0411 -0.0283 277 PHE A O 2144 C CB . PHE A 261 ? 0.3455 0.3384 0.3785 0.0252 0.0472 -0.0181 277 PHE A CB 2145 C CG . PHE A 261 ? 0.3494 0.3384 0.3755 0.0256 0.0496 -0.0122 277 PHE A CG 2146 C CD1 . PHE A 261 ? 0.3555 0.3423 0.3814 0.0272 0.0503 -0.0107 277 PHE A CD1 2147 C CD2 . PHE A 261 ? 0.3515 0.3389 0.3713 0.0245 0.0508 -0.0085 277 PHE A CD2 2148 C CE1 . PHE A 261 ? 0.3601 0.3431 0.3794 0.0279 0.0521 -0.0054 277 PHE A CE1 2149 C CE2 . PHE A 261 ? 0.3518 0.3356 0.3648 0.0251 0.0526 -0.0032 277 PHE A CE2 2150 C CZ . PHE A 261 ? 0.3604 0.3419 0.3730 0.0269 0.0532 -0.0016 277 PHE A CZ 2151 N N . PRO A 262 ? 0.3603 0.3679 0.3962 0.0283 0.0361 -0.0282 278 PRO A N 2152 C CA . PRO A 262 ? 0.3733 0.3848 0.4139 0.0287 0.0329 -0.0337 278 PRO A CA 2153 C C . PRO A 262 ? 0.3870 0.3968 0.4388 0.0283 0.0345 -0.0388 278 PRO A C 2154 O O . PRO A 262 ? 0.3889 0.4013 0.4455 0.0283 0.0323 -0.0435 278 PRO A O 2155 C CB . PRO A 262 ? 0.3671 0.3831 0.4036 0.0307 0.0295 -0.0344 278 PRO A CB 2156 C CG . PRO A 262 ? 0.3636 0.3789 0.3917 0.0310 0.0302 -0.0287 278 PRO A CG 2157 C CD . PRO A 262 ? 0.3628 0.3722 0.3928 0.0300 0.0347 -0.0257 278 PRO A CD 2158 N N . GLU A 263 ? 0.4013 0.4067 0.4574 0.0281 0.0383 -0.0379 279 GLU A N 2159 C CA . GLU A 263 ? 0.4155 0.4187 0.4829 0.0276 0.0404 -0.0426 279 GLU A CA 2160 C C . GLU A 263 ? 0.4310 0.4300 0.5030 0.0252 0.0444 -0.0423 279 GLU A C 2161 O O . GLU A 263 ? 0.4317 0.4287 0.5138 0.0244 0.0466 -0.0462 279 GLU A O 2162 C CB . GLU A 263 ? 0.4187 0.4194 0.4896 0.0287 0.0424 -0.0424 279 GLU A CB 2163 C CG . GLU A 263 ? 0.4178 0.4232 0.4864 0.0311 0.0386 -0.0441 279 GLU A CG 2164 C CD . GLU A 263 ? 0.4243 0.4270 0.4955 0.0323 0.0406 -0.0433 279 GLU A CD 2165 O OE1 . GLU A 263 ? 0.4225 0.4193 0.4983 0.0314 0.0448 -0.0419 279 GLU A OE1 2166 O OE2 . GLU A 263 ? 0.4245 0.4308 0.4930 0.0343 0.0379 -0.0442 279 GLU A OE2 2167 N N . LYS A 264 ? 0.4251 0.4227 0.4899 0.0241 0.0454 -0.0377 280 LYS A N 2168 C CA . LYS A 264 ? 0.4285 0.4225 0.4964 0.0217 0.0491 -0.0372 280 LYS A CA 2169 C C . LYS A 264 ? 0.4216 0.4194 0.4889 0.0210 0.0461 -0.0394 280 LYS A C 2170 O O . LYS A 264 ? 0.4084 0.4109 0.4703 0.0223 0.0415 -0.0397 280 LYS A O 2171 C CB . LYS A 264 ? 0.4298 0.4188 0.4906 0.0209 0.0529 -0.0306 280 LYS A CB 2172 C CG . LYS A 264 ? 0.4456 0.4296 0.5081 0.0214 0.0565 -0.0284 280 LYS A CG 2173 C CD . LYS A 264 ? 0.4608 0.4405 0.5342 0.0198 0.0610 -0.0314 280 LYS A CD 2174 C CE . LYS A 264 ? 0.4700 0.4444 0.5457 0.0204 0.0644 -0.0295 280 LYS A CE 2175 N NZ . LYS A 264 ? 0.4724 0.4412 0.5400 0.0201 0.0679 -0.0227 280 LYS A NZ 2176 N N . PRO A 265 ? 0.4254 0.4213 0.4984 0.0189 0.0488 -0.0412 281 PRO A N 2177 C CA . PRO A 265 ? 0.4223 0.4217 0.4961 0.0184 0.0457 -0.0440 281 PRO A CA 2178 C C . PRO A 265 ? 0.4125 0.4139 0.4755 0.0186 0.0432 -0.0398 281 PRO A C 2179 O O . PRO A 265 ? 0.3934 0.3921 0.4493 0.0181 0.0456 -0.0344 281 PRO A O 2180 C CB . PRO A 265 ? 0.4305 0.4266 0.5123 0.0160 0.0501 -0.0460 281 PRO A CB 2181 C CG . PRO A 265 ? 0.4403 0.4305 0.5221 0.0150 0.0559 -0.0423 281 PRO A CG 2182 C CD . PRO A 265 ? 0.4325 0.4229 0.5125 0.0171 0.0546 -0.0413 281 PRO A CD 2183 N N . LEU A 266 ? 0.4087 0.4147 0.4707 0.0195 0.0382 -0.0425 282 LEU A N 2184 C CA . LEU A 266 ? 0.4066 0.4147 0.4602 0.0195 0.0356 -0.0396 282 LEU A CA 2185 C C . LEU A 266 ? 0.3912 0.4010 0.4501 0.0187 0.0337 -0.0437 282 LEU A C 2186 O O . LEU A 266 ? 0.3966 0.4090 0.4616 0.0197 0.0307 -0.0489 282 LEU A O 2187 C CB . LEU A 266 ? 0.4117 0.4236 0.4580 0.0216 0.0311 -0.0383 282 LEU A CB 2188 C CG . LEU A 266 ? 0.4229 0.4371 0.4605 0.0216 0.0280 -0.0353 282 LEU A CG 2189 C CD1 . LEU A 266 ? 0.4178 0.4294 0.4485 0.0205 0.0309 -0.0295 282 LEU A CD1 2190 C CD2 . LEU A 266 ? 0.4261 0.4443 0.4583 0.0236 0.0237 -0.0354 282 LEU A CD2 2191 N N . VAL A 267 ? 0.3823 0.3907 0.4392 0.0170 0.0354 -0.0416 283 VAL A N 2192 C CA . VAL A 267 ? 0.3647 0.3743 0.4274 0.0161 0.0342 -0.0455 283 VAL A CA 2193 C C . VAL A 267 ? 0.3623 0.3761 0.4213 0.0177 0.0280 -0.0469 283 VAL A C 2194 O O . VAL A 267 ? 0.3530 0.3679 0.4028 0.0181 0.0260 -0.0428 283 VAL A O 2195 C CB . VAL A 267 ? 0.3664 0.3734 0.4277 0.0139 0.0379 -0.0428 283 VAL A CB 2196 C CG1 . VAL A 267 ? 0.3559 0.3644 0.4235 0.0131 0.0364 -0.0472 283 VAL A CG1 2197 C CG2 . VAL A 267 ? 0.3657 0.3679 0.4301 0.0123 0.0444 -0.0413 283 VAL A CG2 2198 N N . ASP A 268 ? 0.3490 0.3652 0.4153 0.0186 0.0249 -0.0527 284 ASP A N 2199 C CA . ASP A 268 ? 0.3511 0.3709 0.4150 0.0202 0.0190 -0.0547 284 ASP A CA 2200 C C . ASP A 268 ? 0.3421 0.3631 0.4166 0.0203 0.0172 -0.0615 284 ASP A C 2201 O O . ASP A 268 ? 0.3383 0.3607 0.4190 0.0216 0.0158 -0.0661 284 ASP A O 2202 C CB . ASP A 268 ? 0.3688 0.3911 0.4270 0.0225 0.0153 -0.0542 284 ASP A CB 2203 C CG . ASP A 268 ? 0.3774 0.4027 0.4307 0.0241 0.0094 -0.0550 284 ASP A CG 2204 O OD1 . ASP A 268 ? 0.3721 0.3980 0.4287 0.0239 0.0073 -0.0575 284 ASP A OD1 2205 O OD2 . ASP A 268 ? 0.4108 0.4379 0.4569 0.0256 0.0069 -0.0531 284 ASP A OD2 2206 N N . VAL A 269 ? 0.3341 0.3549 0.4112 0.0191 0.0172 -0.0624 285 VAL A N 2207 C CA . VAL A 269 ? 0.3250 0.3465 0.4137 0.0187 0.0167 -0.0689 285 VAL A CA 2208 C C . VAL A 269 ? 0.3233 0.3482 0.4130 0.0209 0.0099 -0.0730 285 VAL A C 2209 O O . VAL A 269 ? 0.3148 0.3406 0.4141 0.0208 0.0088 -0.0787 285 VAL A O 2210 C CB . VAL A 269 ? 0.3268 0.3460 0.4202 0.0160 0.0214 -0.0687 285 VAL A CB 2211 C CG1 . VAL A 269 ? 0.3270 0.3424 0.4201 0.0141 0.0282 -0.0652 285 VAL A CG1 2212 C CG2 . VAL A 269 ? 0.3220 0.3415 0.4082 0.0156 0.0196 -0.0653 285 VAL A CG2 2213 N N . SER A 270 ? 0.3217 0.3482 0.4016 0.0228 0.0055 -0.0702 286 SER A N 2214 C CA . SER A 270 ? 0.3272 0.3564 0.4059 0.0250 -0.0010 -0.0731 286 SER A CA 2215 C C . SER A 270 ? 0.3333 0.3646 0.4215 0.0267 -0.0037 -0.0804 286 SER A C 2216 O O . SER A 270 ? 0.3309 0.3635 0.4252 0.0275 -0.0071 -0.0851 286 SER A O 2217 C CB . SER A 270 ? 0.3269 0.3571 0.3932 0.0266 -0.0045 -0.0686 286 SER A CB 2218 O OG . SER A 270 ? 0.3275 0.3563 0.3856 0.0252 -0.0028 -0.0625 286 SER A OG 2219 N N . ALA A 271 ? 0.3384 0.3700 0.4282 0.0273 -0.0024 -0.0815 287 ALA A N 2220 C CA . ALA A 271 ? 0.3378 0.3715 0.4370 0.0290 -0.0046 -0.0886 287 ALA A CA 2221 C C . ALA A 271 ? 0.3305 0.3637 0.4436 0.0274 -0.0022 -0.0942 287 ALA A C 2222 O O . ALA A 271 ? 0.3323 0.3678 0.4527 0.0289 -0.0062 -0.1004 287 ALA A O 2223 C CB . ALA A 271 ? 0.3414 0.3753 0.4404 0.0296 -0.0027 -0.0885 287 ALA A CB 2224 N N . GLU A 272 ? 0.3348 0.3650 0.4511 0.0245 0.0041 -0.0919 288 GLU A N 2225 C CA . GLU A 272 ? 0.3378 0.3672 0.4671 0.0226 0.0072 -0.0968 288 GLU A CA 2226 C C . GLU A 272 ? 0.3392 0.3698 0.4709 0.0226 0.0043 -0.0989 288 GLU A C 2227 O O . GLU A 272 ? 0.3338 0.3658 0.4772 0.0225 0.0035 -0.1056 288 GLU A O 2228 C CB . GLU A 272 ? 0.3471 0.3727 0.4784 0.0195 0.0152 -0.0934 288 GLU A CB 2229 C CG . GLU A 272 ? 0.3728 0.3972 0.5090 0.0193 0.0186 -0.0946 288 GLU A CG 2230 C CD . GLU A 272 ? 0.3853 0.4114 0.5362 0.0196 0.0181 -0.1030 288 GLU A CD 2231 O OE1 . GLU A 272 ? 0.3905 0.4176 0.5498 0.0189 0.0175 -0.1076 288 GLU A OE1 2232 O OE2 . GLU A 272 ? 0.4061 0.4327 0.5605 0.0206 0.0182 -0.1053 288 GLU A OE2 2233 N N . MET A 273 ? 0.3309 0.3610 0.4521 0.0226 0.0027 -0.0936 289 MET A N 2234 C CA . MET A 273 ? 0.3369 0.3680 0.4589 0.0229 -0.0008 -0.0952 289 MET A CA 2235 C C . MET A 273 ? 0.3564 0.3907 0.4823 0.0260 -0.0080 -0.1012 289 MET A C 2236 O O . MET A 273 ? 0.3597 0.3952 0.4953 0.0262 -0.0098 -0.1069 289 MET A O 2237 C CB . MET A 273 ? 0.3175 0.3475 0.4265 0.0227 -0.0019 -0.0881 289 MET A CB 2238 C CG . MET A 273 ? 0.3015 0.3286 0.4069 0.0198 0.0046 -0.0826 289 MET A CG 2239 S SD . MET A 273 ? 0.2931 0.3194 0.3834 0.0197 0.0032 -0.0746 289 MET A SD 2240 C CE . MET A 273 ? 0.2824 0.3099 0.3756 0.0203 -0.0015 -0.0775 289 MET A CE 2241 N N . GLU A 274 ? 0.3856 0.4213 0.5041 0.0286 -0.0121 -0.1001 290 GLU A N 2242 C CA . GLU A 274 ? 0.4258 0.4643 0.5464 0.0319 -0.0191 -0.1056 290 GLU A CA 2243 C C . GLU A 274 ? 0.4266 0.4669 0.5619 0.0322 -0.0187 -0.1137 290 GLU A C 2244 O O . GLU A 274 ? 0.4225 0.4647 0.5653 0.0337 -0.0230 -0.1198 290 GLU A O 2245 C CB . GLU A 274 ? 0.4672 0.5068 0.5767 0.0343 -0.0225 -0.1026 290 GLU A CB 2246 C CG . GLU A 274 ? 0.5305 0.5692 0.6262 0.0348 -0.0250 -0.0960 290 GLU A CG 2247 C CD . GLU A 274 ? 0.5957 0.6358 0.6812 0.0375 -0.0291 -0.0943 290 GLU A CD 2248 O OE1 . GLU A 274 ? 0.6555 0.6978 0.7428 0.0404 -0.0346 -0.0992 290 GLU A OE1 2249 O OE2 . GLU A 274 ? 0.6291 0.6682 0.7049 0.0368 -0.0269 -0.0882 290 GLU A OE2 2250 N N . LYS A 275 ? 0.4281 0.4675 0.5676 0.0308 -0.0136 -0.1140 291 LYS A N 2251 C CA . LYS A 275 ? 0.4417 0.4825 0.5956 0.0308 -0.0125 -0.1215 291 LYS A CA 2252 C C . LYS A 275 ? 0.4301 0.4708 0.5965 0.0290 -0.0107 -0.1264 291 LYS A C 2253 O O . LYS A 275 ? 0.4274 0.4706 0.6053 0.0302 -0.0134 -0.1342 291 LYS A O 2254 C CB . LYS A 275 ? 0.4658 0.5047 0.6217 0.0290 -0.0063 -0.1198 291 LYS A CB 2255 C CG . LYS A 275 ? 0.5028 0.5433 0.6724 0.0295 -0.0058 -0.1276 291 LYS A CG 2256 C CD . LYS A 275 ? 0.5289 0.5669 0.7006 0.0277 0.0005 -0.1255 291 LYS A CD 2257 C CE . LYS A 275 ? 0.5581 0.5972 0.7457 0.0275 0.0018 -0.1336 291 LYS A CE 2258 N NZ . LYS A 275 ? 0.5651 0.6007 0.7576 0.0247 0.0096 -0.1317 291 LYS A NZ 2259 N N . GLN A 276 ? 0.4078 0.4460 0.5721 0.0262 -0.0062 -0.1220 292 GLN A N 2260 C CA . GLN A 276 ? 0.3899 0.4280 0.5655 0.0243 -0.0039 -0.1261 292 GLN A CA 2261 C C . GLN A 276 ? 0.3696 0.4096 0.5449 0.0260 -0.0100 -0.1284 292 GLN A C 2262 O O . GLN A 276 ? 0.3553 0.3956 0.5398 0.0245 -0.0087 -0.1320 292 GLN A O 2263 C CB . GLN A 276 ? 0.4005 0.4350 0.5748 0.0204 0.0041 -0.1210 292 GLN A CB 2264 C CG . GLN A 276 ? 0.4270 0.4594 0.6067 0.0184 0.0108 -0.1210 292 GLN A CG 2265 C CD . GLN A 276 ? 0.4341 0.4624 0.6096 0.0150 0.0185 -0.1147 292 GLN A CD 2266 O OE1 . GLN A 276 ? 0.4434 0.4708 0.6213 0.0130 0.0213 -0.1144 292 GLN A OE1 2267 N NE2 . GLN A 276 ? 0.4435 0.4693 0.6127 0.0146 0.0219 -0.1098 292 GLN A NE2 2268 N N . GLY A 277 ? 0.3547 0.3960 0.5198 0.0291 -0.0167 -0.1264 293 GLY A N 2269 C CA . GLY A 277 ? 0.3454 0.3881 0.5096 0.0312 -0.0233 -0.1284 293 GLY A CA 2270 C C . GLY A 277 ? 0.3398 0.3806 0.4987 0.0294 -0.0217 -0.1236 293 GLY A C 2271 O O . GLY A 277 ? 0.3461 0.3878 0.5102 0.0299 -0.0247 -0.1270 293 GLY A O 2272 N N . TYR A 278 ? 0.3292 0.3673 0.4780 0.0274 -0.0172 -0.1159 294 TYR A N 2273 C CA . TYR A 278 ? 0.3233 0.3597 0.4652 0.0259 -0.0161 -0.1106 294 TYR A CA 2274 C C . TYR A 278 ? 0.3186 0.3558 0.4530 0.0287 -0.0237 -0.1096 294 TYR A C 2275 O O . TYR A 278 ? 0.3119 0.3500 0.4399 0.0315 -0.0286 -0.1091 294 TYR A O 2276 C CB . TYR A 278 ? 0.3311 0.3650 0.4621 0.0240 -0.0111 -0.1025 294 TYR A CB 2277 C CG . TYR A 278 ? 0.3363 0.3681 0.4720 0.0204 -0.0028 -0.1012 294 TYR A CG 2278 C CD1 . TYR A 278 ? 0.3414 0.3732 0.4884 0.0192 0.0012 -0.1060 294 TYR A CD1 2279 C CD2 . TYR A 278 ? 0.3395 0.3690 0.4678 0.0183 0.0010 -0.0950 294 TYR A CD2 2280 C CE1 . TYR A 278 ? 0.3468 0.3761 0.4974 0.0160 0.0090 -0.1043 294 TYR A CE1 2281 C CE2 . TYR A 278 ? 0.3463 0.3735 0.4776 0.0152 0.0086 -0.0935 294 TYR A CE2 2282 C CZ . TYR A 278 ? 0.3541 0.3811 0.4964 0.0140 0.0126 -0.0980 294 TYR A CZ 2283 O OH . TYR A 278 ? 0.3652 0.3895 0.5101 0.0109 0.0204 -0.0962 294 TYR A OH 2284 N N . THR A 279 ? 0.3088 0.3454 0.4441 0.0280 -0.0245 -0.1092 295 THR A N 2285 C CA . THR A 279 ? 0.3050 0.3415 0.4327 0.0303 -0.0311 -0.1073 295 THR A CA 2286 C C . THR A 279 ? 0.3029 0.3373 0.4230 0.0281 -0.0281 -0.1007 295 THR A C 2287 O O . THR A 279 ? 0.3006 0.3339 0.4233 0.0250 -0.0215 -0.0993 295 THR A O 2288 C CB . THR A 279 ? 0.3004 0.3386 0.4383 0.0320 -0.0361 -0.1144 295 THR A CB 2289 O OG1 . THR A 279 ? 0.2975 0.3357 0.4454 0.0292 -0.0314 -0.1169 295 THR A OG1 2290 C CG2 . THR A 279 ? 0.3030 0.3438 0.4493 0.0345 -0.0396 -0.1216 295 THR A CG2 2291 N N . PRO A 280 ? 0.3084 0.3419 0.4187 0.0296 -0.0328 -0.0969 296 PRO A N 2292 C CA . PRO A 280 ? 0.3066 0.3383 0.4114 0.0276 -0.0305 -0.0916 296 PRO A CA 2293 C C . PRO A 280 ? 0.3027 0.3346 0.4180 0.0255 -0.0276 -0.0953 296 PRO A C 2294 O O . PRO A 280 ? 0.2976 0.3284 0.4116 0.0226 -0.0219 -0.0921 296 PRO A O 2295 C CB . PRO A 280 ? 0.3110 0.3419 0.4071 0.0301 -0.0373 -0.0891 296 PRO A CB 2296 C CG . PRO A 280 ? 0.3120 0.3438 0.4030 0.0328 -0.0409 -0.0892 296 PRO A CG 2297 C CD . PRO A 280 ? 0.3116 0.3454 0.4144 0.0332 -0.0400 -0.0963 296 PRO A CD 2298 N N . LEU A 281 ? 0.3003 0.3338 0.4261 0.0269 -0.0313 -0.1022 297 LEU A N 2299 C CA . LEU A 281 ? 0.2994 0.3336 0.4365 0.0250 -0.0286 -0.1066 297 LEU A CA 2300 C C . LEU A 281 ? 0.2915 0.3255 0.4346 0.0216 -0.0201 -0.1072 297 LEU A C 2301 O O . LEU A 281 ? 0.2904 0.3236 0.4348 0.0189 -0.0152 -0.1057 297 LEU A O 2302 C CB . LEU A 281 ? 0.3052 0.3415 0.4537 0.0273 -0.0341 -0.1147 297 LEU A CB 2303 C CG . LEU A 281 ? 0.3028 0.3402 0.4641 0.0256 -0.0318 -0.1201 297 LEU A CG 2304 C CD1 . LEU A 281 ? 0.3042 0.3402 0.4607 0.0246 -0.0320 -0.1163 297 LEU A CD1 2305 C CD2 . LEU A 281 ? 0.3077 0.3476 0.4812 0.0281 -0.0374 -0.1287 297 LEU A CD2 2306 N N A LYS A 282 ? 0.2951 0.3298 0.4416 0.0218 -0.0184 -0.1093 298 LYS A N 2307 N N B LYS A 282 ? 0.2949 0.3296 0.4416 0.0218 -0.0183 -0.1094 298 LYS A N 2308 C CA A LYS A 282 ? 0.2917 0.3257 0.4433 0.0188 -0.0104 -0.1095 298 LYS A CA 2309 C CA B LYS A 282 ? 0.2912 0.3252 0.4431 0.0187 -0.0102 -0.1096 298 LYS A CA 2310 C C A LYS A 282 ? 0.2873 0.3187 0.4281 0.0165 -0.0050 -0.1016 298 LYS A C 2311 C C B LYS A 282 ? 0.2871 0.3185 0.4279 0.0164 -0.0049 -0.1016 298 LYS A C 2312 O O A LYS A 282 ? 0.2854 0.3157 0.4294 0.0135 0.0015 -0.1009 298 LYS A O 2313 O O B LYS A 282 ? 0.2853 0.3155 0.4290 0.0135 0.0017 -0.1007 298 LYS A O 2314 C CB A LYS A 282 ? 0.2933 0.3281 0.4487 0.0199 -0.0103 -0.1124 298 LYS A CB 2315 C CB B LYS A 282 ? 0.2930 0.3279 0.4501 0.0195 -0.0097 -0.1131 298 LYS A CB 2316 C CG A LYS A 282 ? 0.2967 0.3303 0.4579 0.0168 -0.0021 -0.1128 298 LYS A CG 2317 C CG B LYS A 282 ? 0.2965 0.3297 0.4560 0.0165 -0.0013 -0.1116 298 LYS A CG 2318 C CD A LYS A 282 ? 0.3040 0.3381 0.4778 0.0145 0.0017 -0.1179 298 LYS A CD 2319 C CD B LYS A 282 ? 0.3043 0.3381 0.4674 0.0175 -0.0012 -0.1142 298 LYS A CD 2320 C CE A LYS A 282 ? 0.3069 0.3398 0.4881 0.0116 0.0097 -0.1192 298 LYS A CE 2321 C CE B LYS A 282 ? 0.3074 0.3428 0.4869 0.0168 0.0005 -0.1225 298 LYS A CE 2322 N NZ A LYS A 282 ? 0.3049 0.3390 0.5008 0.0097 0.0127 -0.1260 298 LYS A NZ 2323 N NZ B LYS A 282 ? 0.3106 0.3442 0.4961 0.0128 0.0091 -0.1221 298 LYS A NZ 2324 N N . MET A 283 ? 0.2855 0.3161 0.4136 0.0179 -0.0078 -0.0958 299 MET A N 2325 C CA . MET A 283 ? 0.2843 0.3128 0.4015 0.0162 -0.0036 -0.0882 299 MET A CA 2326 C C . MET A 283 ? 0.2810 0.3086 0.3970 0.0143 -0.0015 -0.0862 299 MET A C 2327 O O . MET A 283 ? 0.2787 0.3048 0.3931 0.0117 0.0046 -0.0834 299 MET A O 2328 C CB . MET A 283 ? 0.2835 0.3117 0.3882 0.0182 -0.0075 -0.0831 299 MET A CB 2329 C CG . MET A 283 ? 0.2927 0.3215 0.3976 0.0197 -0.0081 -0.0843 299 MET A CG 2330 S SD . MET A 283 ? 0.2963 0.3257 0.3891 0.0229 -0.0146 -0.0807 299 MET A SD 2331 C CE . MET A 283 ? 0.3016 0.3290 0.3816 0.0211 -0.0104 -0.0719 299 MET A CE 2332 N N . PHE A 284 ? 0.2777 0.3062 0.3947 0.0156 -0.0068 -0.0880 300 PHE A N 2333 C CA . PHE A 284 ? 0.2783 0.3064 0.3955 0.0139 -0.0052 -0.0870 300 PHE A CA 2334 C C . PHE A 284 ? 0.2779 0.3065 0.4068 0.0115 0.0000 -0.0918 300 PHE A C 2335 O O . PHE A 284 ? 0.2753 0.3029 0.4026 0.0090 0.0050 -0.0895 300 PHE A O 2336 C CB . PHE A 284 ? 0.2815 0.3102 0.3975 0.0161 -0.0124 -0.0879 300 PHE A CB 2337 C CG . PHE A 284 ? 0.2847 0.3122 0.3873 0.0173 -0.0157 -0.0813 300 PHE A CG 2338 C CD1 . PHE A 284 ? 0.2821 0.3096 0.3788 0.0198 -0.0200 -0.0800 300 PHE A CD1 2339 C CD2 . PHE A 284 ? 0.2817 0.3080 0.3778 0.0159 -0.0141 -0.0766 300 PHE A CD2 2340 C CE1 . PHE A 284 ? 0.2891 0.3155 0.3737 0.0208 -0.0226 -0.0740 300 PHE A CE1 2341 C CE2 . PHE A 284 ? 0.2870 0.3123 0.3714 0.0169 -0.0168 -0.0707 300 PHE A CE2 2342 C CZ . PHE A 284 ? 0.2897 0.3149 0.3683 0.0192 -0.0209 -0.0693 300 PHE A CZ 2343 N N . GLN A 285 ? 0.2777 0.3079 0.4181 0.0121 -0.0007 -0.0986 301 GLN A N 2344 C CA . GLN A 285 ? 0.2822 0.3130 0.4348 0.0096 0.0047 -0.1036 301 GLN A CA 2345 C C . GLN A 285 ? 0.2800 0.3086 0.4299 0.0068 0.0131 -0.1001 301 GLN A C 2346 O O . GLN A 285 ? 0.2777 0.3057 0.4311 0.0040 0.0189 -0.1005 301 GLN A O 2347 C CB . GLN A 285 ? 0.2822 0.3152 0.4479 0.0109 0.0021 -0.1118 301 GLN A CB 2348 C CG . GLN A 285 ? 0.2834 0.3184 0.4544 0.0134 -0.0052 -0.1165 301 GLN A CG 2349 C CD . GLN A 285 ? 0.2862 0.3236 0.4683 0.0155 -0.0094 -0.1241 301 GLN A CD 2350 O OE1 . GLN A 285 ? 0.2928 0.3304 0.4769 0.0158 -0.0080 -0.1253 301 GLN A OE1 2351 N NE2 . GLN A 285 ? 0.2862 0.3254 0.4756 0.0173 -0.0148 -0.1294 301 GLN A NE2 2352 N N . MET A 286 ? 0.2898 0.3172 0.4330 0.0075 0.0136 -0.0964 302 MET A N 2353 C CA . MET A 286 ? 0.2991 0.3241 0.4385 0.0052 0.0209 -0.0923 302 MET A CA 2354 C C . MET A 286 ? 0.2912 0.3144 0.4198 0.0038 0.0238 -0.0856 302 MET A C 2355 O O . MET A 286 ? 0.2888 0.3101 0.4173 0.0012 0.0306 -0.0839 302 MET A O 2356 C CB . MET A 286 ? 0.3170 0.3414 0.4520 0.0067 0.0199 -0.0902 302 MET A CB 2357 C CG . MET A 286 ? 0.3474 0.3730 0.4943 0.0072 0.0198 -0.0968 302 MET A CG 2358 S SD . MET A 286 ? 0.4033 0.4288 0.5453 0.0094 0.0175 -0.0951 302 MET A SD 2359 C CE . MET A 286 ? 0.3860 0.4076 0.5196 0.0070 0.0254 -0.0879 302 MET A CE 2360 N N . GLY A 287 ? 0.2939 0.3175 0.4133 0.0054 0.0187 -0.0819 303 GLY A N 2361 C CA . GLY A 287 ? 0.2912 0.3136 0.4012 0.0043 0.0206 -0.0764 303 GLY A CA 2362 C C . GLY A 287 ? 0.2986 0.3214 0.4147 0.0022 0.0237 -0.0791 303 GLY A C 2363 O O . GLY A 287 ? 0.2984 0.3197 0.4108 0.0001 0.0293 -0.0761 303 GLY A O 2364 N N . ASP A 288 ? 0.2921 0.3169 0.4174 0.0030 0.0199 -0.0850 304 ASP A N 2365 C CA . ASP A 288 ? 0.3058 0.3315 0.4387 0.0012 0.0224 -0.0887 304 ASP A CA 2366 C C . ASP A 288 ? 0.3074 0.3320 0.4464 -0.0016 0.0308 -0.0905 304 ASP A C 2367 O O . ASP A 288 ? 0.3143 0.3381 0.4520 -0.0038 0.0358 -0.0892 304 ASP A O 2368 C CB . ASP A 288 ? 0.3033 0.3315 0.4465 0.0029 0.0166 -0.0955 304 ASP A CB 2369 C CG . ASP A 288 ? 0.3153 0.3447 0.4660 0.0013 0.0182 -0.0994 304 ASP A CG 2370 O OD1 . ASP A 288 ? 0.3091 0.3377 0.4541 -0.0002 0.0212 -0.0960 304 ASP A OD1 2371 O OD2 . ASP A 288 ? 0.3287 0.3601 0.4913 0.0018 0.0161 -0.1063 304 ASP A OD2 2372 N N . ASP A 289 ? 0.3110 0.3354 0.4561 -0.0015 0.0323 -0.0931 305 ASP A N 2373 C CA . ASP A 289 ? 0.3165 0.3393 0.4672 -0.0042 0.0403 -0.0945 305 ASP A CA 2374 C C . ASP A 289 ? 0.3022 0.3219 0.4420 -0.0059 0.0463 -0.0875 305 ASP A C 2375 O O . ASP A 289 ? 0.2973 0.3155 0.4392 -0.0086 0.0530 -0.0877 305 ASP A O 2376 C CB . ASP A 289 ? 0.3313 0.3542 0.4890 -0.0034 0.0401 -0.0978 305 ASP A CB 2377 C CG . ASP A 289 ? 0.3581 0.3785 0.5201 -0.0061 0.0486 -0.0979 305 ASP A CG 2378 O OD1 . ASP A 289 ? 0.3667 0.3863 0.5328 -0.0088 0.0546 -0.0992 305 ASP A OD1 2379 O OD2 . ASP A 289 ? 0.3977 0.4168 0.5591 -0.0055 0.0493 -0.0969 305 ASP A OD2 2380 N N . PHE A 290 ? 0.2929 0.3114 0.4210 -0.0044 0.0438 -0.0815 306 PHE A N 2381 C CA . PHE A 290 ? 0.2903 0.3058 0.4074 -0.0056 0.0487 -0.0747 306 PHE A CA 2382 C C . PHE A 290 ? 0.2882 0.3038 0.4014 -0.0070 0.0509 -0.0731 306 PHE A C 2383 O O . PHE A 290 ? 0.2854 0.2989 0.3970 -0.0092 0.0576 -0.0714 306 PHE A O 2384 C CB . PHE A 290 ? 0.2872 0.3022 0.3930 -0.0034 0.0448 -0.0690 306 PHE A CB 2385 C CG . PHE A 290 ? 0.2898 0.3015 0.3875 -0.0042 0.0500 -0.0635 306 PHE A CG 2386 C CD1 . PHE A 290 ? 0.2910 0.3008 0.3820 -0.0059 0.0547 -0.0595 306 PHE A CD1 2387 C CD2 . PHE A 290 ? 0.2915 0.3020 0.3883 -0.0032 0.0500 -0.0622 306 PHE A CD2 2388 C CE1 . PHE A 290 ? 0.2928 0.2994 0.3762 -0.0063 0.0591 -0.0544 306 PHE A CE1 2389 C CE2 . PHE A 290 ? 0.2940 0.3013 0.3837 -0.0038 0.0545 -0.0571 306 PHE A CE2 2390 C CZ . PHE A 290 ? 0.2919 0.2972 0.3747 -0.0053 0.0590 -0.0531 306 PHE A CZ 2391 N N . PHE A 291 ? 0.2931 0.3109 0.4046 -0.0058 0.0453 -0.0735 307 PHE A N 2392 C CA . PHE A 291 ? 0.2992 0.3174 0.4076 -0.0070 0.0468 -0.0724 307 PHE A CA 2393 C C . PHE A 291 ? 0.3069 0.3255 0.4253 -0.0095 0.0523 -0.0775 307 PHE A C 2394 O O . PHE A 291 ? 0.3155 0.3326 0.4303 -0.0115 0.0580 -0.0755 307 PHE A O 2395 C CB . PHE A 291 ? 0.2968 0.3172 0.4030 -0.0052 0.0395 -0.0726 307 PHE A CB 2396 C CG . PHE A 291 ? 0.2980 0.3178 0.3919 -0.0035 0.0358 -0.0663 307 PHE A CG 2397 C CD1 . PHE A 291 ? 0.3018 0.3208 0.3861 -0.0042 0.0375 -0.0614 307 PHE A CD1 2398 C CD2 . PHE A 291 ? 0.2955 0.3156 0.3875 -0.0013 0.0307 -0.0655 307 PHE A CD2 2399 C CE1 . PHE A 291 ? 0.2931 0.3117 0.3669 -0.0027 0.0342 -0.0560 307 PHE A CE1 2400 C CE2 . PHE A 291 ? 0.2912 0.3109 0.3723 0.0000 0.0277 -0.0599 307 PHE A CE2 2401 C CZ . PHE A 291 ? 0.2923 0.3113 0.3646 -0.0006 0.0294 -0.0552 307 PHE A CZ 2402 N N . THR A 292 ? 0.3044 0.3249 0.4353 -0.0094 0.0506 -0.0842 308 THR A N 2403 C CA . THR A 292 ? 0.3110 0.3322 0.4528 -0.0118 0.0558 -0.0897 308 THR A CA 2404 C C . THR A 292 ? 0.3127 0.3310 0.4552 -0.0143 0.0644 -0.0886 308 THR A C 2405 O O . THR A 292 ? 0.3106 0.3285 0.4561 -0.0167 0.0705 -0.0901 308 THR A O 2406 C CB . THR A 292 ? 0.3101 0.3343 0.4662 -0.0110 0.0519 -0.0977 308 THR A CB 2407 O OG1 . THR A 292 ? 0.3245 0.3485 0.4853 -0.0099 0.0505 -0.0996 308 THR A OG1 2408 C CG2 . THR A 292 ? 0.3033 0.3299 0.4585 -0.0086 0.0436 -0.0987 308 THR A CG2 2409 N N . SER A 293 ? 0.3198 0.3359 0.4589 -0.0136 0.0651 -0.0857 309 SER A N 2410 C CA . SER A 293 ? 0.3262 0.3388 0.4651 -0.0157 0.0732 -0.0840 309 SER A CA 2411 C C . SER A 293 ? 0.3368 0.3467 0.4643 -0.0172 0.0784 -0.0780 309 SER A C 2412 O O . SER A 293 ? 0.3337 0.3407 0.4615 -0.0195 0.0861 -0.0771 309 SER A O 2413 C CB . SER A 293 ? 0.3323 0.3433 0.4696 -0.0144 0.0721 -0.0819 309 SER A CB 2414 O OG . SER A 293 ? 0.3296 0.3388 0.4530 -0.0130 0.0704 -0.0747 309 SER A OG 2415 N N . MET A 294 ? 0.3352 0.3460 0.4525 -0.0157 0.0742 -0.0739 310 MET A N 2416 C CA . MET A 294 ? 0.3461 0.3549 0.4520 -0.0166 0.0780 -0.0684 310 MET A CA 2417 C C . MET A 294 ? 0.3501 0.3609 0.4586 -0.0180 0.0794 -0.0713 310 MET A C 2418 O O . MET A 294 ? 0.3470 0.3571 0.4462 -0.0184 0.0810 -0.0675 310 MET A O 2419 C CB . MET A 294 ? 0.3466 0.3553 0.4401 -0.0143 0.0727 -0.0625 310 MET A CB 2420 C CG . MET A 294 ? 0.3505 0.3573 0.4401 -0.0128 0.0715 -0.0592 310 MET A CG 2421 S SD . MET A 294 ? 0.3621 0.3696 0.4388 -0.0100 0.0648 -0.0531 310 MET A SD 2422 C CE . MET A 294 ? 0.3594 0.3648 0.4241 -0.0111 0.0694 -0.0476 310 MET A CE 2423 N N . ASN A 295 ? 0.3557 0.3691 0.4770 -0.0187 0.0786 -0.0782 311 ASN A N 2424 C CA . ASN A 295 ? 0.3679 0.3837 0.4935 -0.0200 0.0796 -0.0820 311 ASN A CA 2425 C C . ASN A 295 ? 0.3630 0.3812 0.4830 -0.0181 0.0726 -0.0805 311 ASN A C 2426 O O . ASN A 295 ? 0.3549 0.3743 0.4732 -0.0189 0.0737 -0.0810 311 ASN A O 2427 C CB . ASN A 295 ? 0.3898 0.4032 0.5113 -0.0227 0.0884 -0.0801 311 ASN A CB 2428 C CG . ASN A 295 ? 0.4171 0.4329 0.5461 -0.0246 0.0911 -0.0854 311 ASN A CG 2429 O OD1 . ASN A 295 ? 0.4177 0.4368 0.5584 -0.0243 0.0878 -0.0917 311 ASN A OD1 2430 N ND2 . ASN A 295 ? 0.4430 0.4574 0.5652 -0.0263 0.0971 -0.0830 311 ASN A ND2 2431 N N . LEU A 296 ? 0.3429 0.3617 0.4600 -0.0155 0.0655 -0.0787 312 LEU A N 2432 C CA . LEU A 296 ? 0.3351 0.3559 0.4477 -0.0136 0.0585 -0.0775 312 LEU A CA 2433 C C . LEU A 296 ? 0.3329 0.3566 0.4568 -0.0124 0.0528 -0.0837 312 LEU A C 2434 O O . LEU A 296 ? 0.3461 0.3706 0.4811 -0.0131 0.0543 -0.0891 312 LEU A O 2435 C CB . LEU A 296 ? 0.3260 0.3455 0.4270 -0.0115 0.0547 -0.0710 312 LEU A CB 2436 C CG . LEU A 296 ? 0.3233 0.3403 0.4120 -0.0122 0.0591 -0.0645 312 LEU A CG 2437 C CD1 . LEU A 296 ? 0.3234 0.3391 0.4026 -0.0103 0.0557 -0.0590 312 LEU A CD1 2438 C CD2 . LEU A 296 ? 0.3249 0.3429 0.4087 -0.0129 0.0596 -0.0634 312 LEU A CD2 2439 N N . THR A 297 ? 0.3262 0.3515 0.4473 -0.0106 0.0461 -0.0830 313 THR A N 2440 C CA . THR A 297 ? 0.3140 0.3419 0.4452 -0.0095 0.0407 -0.0889 313 THR A CA 2441 C C . THR A 297 ? 0.3252 0.3535 0.4608 -0.0072 0.0349 -0.0909 313 THR A C 2442 O O . THR A 297 ? 0.3102 0.3373 0.4377 -0.0054 0.0313 -0.0865 313 THR A O 2443 C CB . THR A 297 ? 0.3123 0.3412 0.4389 -0.0085 0.0359 -0.0874 313 THR A CB 2444 O OG1 . THR A 297 ? 0.3024 0.3311 0.4248 -0.0105 0.0412 -0.0858 313 THR A OG1 2445 C CG2 . THR A 297 ? 0.2965 0.3277 0.4338 -0.0074 0.0306 -0.0936 313 THR A CG2 2446 N N . LYS A 298 ? 0.3249 0.3549 0.4736 -0.0072 0.0342 -0.0979 314 LYS A N 2447 C CA . LYS A 298 ? 0.3342 0.3651 0.4889 -0.0048 0.0284 -0.1013 314 LYS A CA 2448 C C . LYS A 298 ? 0.3241 0.3557 0.4756 -0.0020 0.0196 -0.1005 314 LYS A C 2449 O O . LYS A 298 ? 0.3241 0.3565 0.4753 -0.0020 0.0178 -0.1008 314 LYS A O 2450 C CB . LYS A 298 ? 0.3638 0.3967 0.5342 -0.0058 0.0303 -0.1096 314 LYS A CB 2451 C CG . LYS A 298 ? 0.4031 0.4383 0.5830 -0.0033 0.0227 -0.1156 314 LYS A CG 2452 C CD . LYS A 298 ? 0.4279 0.4655 0.6240 -0.0046 0.0252 -0.1241 314 LYS A CD 2453 C CE . LYS A 298 ? 0.4548 0.4940 0.6556 -0.0061 0.0270 -0.1271 314 LYS A CE 2454 N NZ . LYS A 298 ? 0.4799 0.5218 0.6971 -0.0074 0.0296 -0.1357 314 LYS A NZ 2455 N N . LEU A 299 ? 0.3068 0.3380 0.4557 0.0004 0.0143 -0.0994 315 LEU A N 2456 C CA . LEU A 299 ? 0.3044 0.3359 0.4501 0.0032 0.0060 -0.0986 315 LEU A CA 2457 C C . LEU A 299 ? 0.3079 0.3414 0.4655 0.0041 0.0020 -0.1057 315 LEU A C 2458 O O . LEU A 299 ? 0.3010 0.3360 0.4701 0.0040 0.0030 -0.1120 315 LEU A O 2459 C CB . LEU A 299 ? 0.2970 0.3277 0.4381 0.0058 0.0014 -0.0967 315 LEU A CB 2460 C CG . LEU A 299 ? 0.2947 0.3235 0.4233 0.0054 0.0039 -0.0895 315 LEU A CG 2461 C CD1 . LEU A 299 ? 0.2889 0.3175 0.4160 0.0076 0.0006 -0.0894 315 LEU A CD1 2462 C CD2 . LEU A 299 ? 0.2910 0.3188 0.4085 0.0057 0.0018 -0.0835 315 LEU A CD2 2463 N N . PRO A 300 ? 0.3101 0.3436 0.4653 0.0051 -0.0022 -0.1047 316 PRO A N 2464 C CA . PRO A 300 ? 0.3148 0.3501 0.4811 0.0062 -0.0065 -0.1113 316 PRO A CA 2465 C C . PRO A 300 ? 0.3273 0.3627 0.4966 0.0097 -0.0145 -0.1140 316 PRO A C 2466 O O . PRO A 300 ? 0.3219 0.3558 0.4828 0.0114 -0.0172 -0.1099 316 PRO A O 2467 C CB . PRO A 300 ? 0.3107 0.3454 0.4716 0.0061 -0.0084 -0.1083 316 PRO A CB 2468 C CG . PRO A 300 ? 0.3127 0.3451 0.4589 0.0063 -0.0085 -0.1001 316 PRO A CG 2469 C CD . PRO A 300 ? 0.3040 0.3360 0.4470 0.0049 -0.0027 -0.0979 316 PRO A CD 2470 N N . GLN A 301 ? 0.3331 0.3702 0.5141 0.0110 -0.0182 -0.1209 317 GLN A N 2471 C CA . GLN A 301 ? 0.3426 0.3802 0.5278 0.0145 -0.0260 -0.1244 317 GLN A CA 2472 C C . GLN A 301 ? 0.3339 0.3690 0.5079 0.0174 -0.0333 -0.1191 317 GLN A C 2473 O O . GLN A 301 ? 0.3240 0.3584 0.4947 0.0201 -0.0382 -0.1185 317 GLN A O 2474 C CB . GLN A 301 ? 0.3655 0.4055 0.5660 0.0152 -0.0284 -0.1332 317 GLN A CB 2475 C CG . GLN A 301 ? 0.3930 0.4346 0.6032 0.0177 -0.0328 -0.1397 317 GLN A CG 2476 C CD . GLN A 301 ? 0.4132 0.4551 0.6227 0.0169 -0.0289 -0.1393 317 GLN A CD 2477 O OE1 . GLN A 301 ? 0.4345 0.4770 0.6467 0.0137 -0.0208 -0.1395 317 GLN A OE1 2478 N NE2 . GLN A 301 ? 0.4186 0.4599 0.6241 0.0200 -0.0346 -0.1386 317 GLN A NE2 2479 N N . ASP A 302 ? 0.3244 0.3581 0.4923 0.0168 -0.0337 -0.1151 318 ASP A N 2480 C CA . ASP A 302 ? 0.3325 0.3635 0.4891 0.0190 -0.0396 -0.1092 318 ASP A CA 2481 C C . ASP A 302 ? 0.3217 0.3511 0.4666 0.0194 -0.0388 -0.1032 318 ASP A C 2482 O O . ASP A 302 ? 0.3240 0.3519 0.4626 0.0222 -0.0447 -0.1008 318 ASP A O 2483 C CB . ASP A 302 ? 0.3514 0.3813 0.5028 0.0175 -0.0384 -0.1053 318 ASP A CB 2484 C CG . ASP A 302 ? 0.3774 0.4075 0.5365 0.0188 -0.0432 -0.1094 318 ASP A CG 2485 O OD1 . ASP A 302 ? 0.3907 0.4217 0.5592 0.0209 -0.0477 -0.1155 318 ASP A OD1 2486 O OD2 . ASP A 302 ? 0.3868 0.4161 0.5427 0.0177 -0.0425 -0.1068 318 ASP A OD2 2487 N N . PHE A 303 ? 0.3000 0.3300 0.4421 0.0167 -0.0316 -0.1009 319 PHE A N 2488 C CA . PHE A 303 ? 0.3084 0.3372 0.4402 0.0169 -0.0304 -0.0956 319 PHE A CA 2489 C C . PHE A 303 ? 0.3112 0.3404 0.4458 0.0196 -0.0346 -0.0987 319 PHE A C 2490 O O . PHE A 303 ? 0.3196 0.3474 0.4455 0.0218 -0.0389 -0.0950 319 PHE A O 2491 C CB . PHE A 303 ? 0.2968 0.3260 0.4266 0.0138 -0.0219 -0.0933 319 PHE A CB 2492 C CG . PHE A 303 ? 0.3020 0.3301 0.4222 0.0142 -0.0208 -0.0883 319 PHE A CG 2493 C CD1 . PHE A 303 ? 0.2993 0.3281 0.4235 0.0149 -0.0203 -0.0912 319 PHE A CD1 2494 C CD2 . PHE A 303 ? 0.2998 0.3262 0.4075 0.0139 -0.0205 -0.0811 319 PHE A CD2 2495 C CE1 . PHE A 303 ? 0.2995 0.3274 0.4152 0.0154 -0.0195 -0.0869 319 PHE A CE1 2496 C CE2 . PHE A 303 ? 0.2997 0.3253 0.3991 0.0143 -0.0196 -0.0769 319 PHE A CE2 2497 C CZ . PHE A 303 ? 0.3003 0.3267 0.4037 0.0151 -0.0191 -0.0797 319 PHE A CZ 2498 N N . TRP A 304 ? 0.3047 0.3361 0.4515 0.0194 -0.0333 -0.1056 320 TRP A N 2499 C CA . TRP A 304 ? 0.3064 0.3387 0.4573 0.0219 -0.0371 -0.1095 320 TRP A CA 2500 C C . TRP A 304 ? 0.3141 0.3457 0.4647 0.0257 -0.0463 -0.1111 320 TRP A C 2501 O O . TRP A 304 ? 0.3140 0.3450 0.4598 0.0284 -0.0508 -0.1103 320 TRP A O 2502 C CB . TRP A 304 ? 0.3024 0.3372 0.4676 0.0206 -0.0335 -0.1170 320 TRP A CB 2503 C CG . TRP A 304 ? 0.2976 0.3326 0.4630 0.0171 -0.0244 -0.1154 320 TRP A CG 2504 C CD1 . TRP A 304 ? 0.2962 0.3321 0.4685 0.0139 -0.0179 -0.1176 320 TRP A CD1 2505 C CD2 . TRP A 304 ? 0.2985 0.3326 0.4568 0.0163 -0.0208 -0.1113 320 TRP A CD2 2506 N NE1 . TRP A 304 ? 0.2951 0.3303 0.4644 0.0113 -0.0105 -0.1148 320 TRP A NE1 2507 C CE2 . TRP A 304 ? 0.2964 0.3305 0.4576 0.0128 -0.0122 -0.1110 320 TRP A CE2 2508 C CE3 . TRP A 304 ? 0.3033 0.3365 0.4531 0.0184 -0.0239 -0.1078 320 TRP A CE3 2509 C CZ2 . TRP A 304 ? 0.2951 0.3281 0.4510 0.0114 -0.0070 -0.1073 320 TRP A CZ2 2510 C CZ3 . TRP A 304 ? 0.2975 0.3300 0.4426 0.0169 -0.0185 -0.1045 320 TRP A CZ3 2511 C CH2 . TRP A 304 ? 0.2979 0.3301 0.4461 0.0135 -0.0103 -0.1041 320 TRP A CH2 2512 N N . ASP A 305 ? 0.3155 0.3470 0.4707 0.0261 -0.0491 -0.1133 321 ASP A N 2513 C CA . ASP A 305 ? 0.3233 0.3537 0.4789 0.0298 -0.0579 -0.1150 321 ASP A CA 2514 C C . ASP A 305 ? 0.3237 0.3509 0.4646 0.0316 -0.0622 -0.1076 321 ASP A C 2515 O O . ASP A 305 ? 0.3202 0.3463 0.4583 0.0351 -0.0691 -0.1080 321 ASP A O 2516 C CB . ASP A 305 ? 0.3359 0.3668 0.5000 0.0295 -0.0594 -0.1187 321 ASP A CB 2517 C CG . ASP A 305 ? 0.3459 0.3802 0.5264 0.0288 -0.0575 -0.1276 321 ASP A CG 2518 O OD1 . ASP A 305 ? 0.3514 0.3876 0.5376 0.0289 -0.0560 -0.1315 321 ASP A OD1 2519 O OD2 . ASP A 305 ? 0.3555 0.3906 0.5437 0.0280 -0.0574 -0.1310 321 ASP A OD2 2520 N N . LYS A 306 ? 0.3112 0.3369 0.4430 0.0292 -0.0580 -0.1010 322 LYS A N 2521 C CA . LYS A 306 ? 0.3139 0.3365 0.4332 0.0304 -0.0617 -0.0942 322 LYS A CA 2522 C C . LYS A 306 ? 0.3083 0.3299 0.4151 0.0298 -0.0590 -0.0876 322 LYS A C 2523 O O . LYS A 306 ? 0.3142 0.3333 0.4105 0.0312 -0.0624 -0.0822 322 LYS A O 2524 C CB . LYS A 306 ? 0.3269 0.3485 0.4455 0.0287 -0.0604 -0.0918 322 LYS A CB 2525 C CG . LYS A 306 ? 0.3361 0.3579 0.4652 0.0298 -0.0643 -0.0975 322 LYS A CG 2526 C CD . LYS A 306 ? 0.3453 0.3664 0.4733 0.0276 -0.0620 -0.0949 322 LYS A CD 2527 C CE . LYS A 306 ? 0.3555 0.3774 0.4951 0.0283 -0.0651 -0.1009 322 LYS A CE 2528 N NZ . LYS A 306 ? 0.3772 0.3978 0.5145 0.0268 -0.0641 -0.0980 322 LYS A NZ 2529 N N . SER A 307 ? 0.2961 0.3195 0.4040 0.0277 -0.0529 -0.0878 323 SER A N 2530 C CA . SER A 307 ? 0.2920 0.3147 0.3888 0.0271 -0.0502 -0.0818 323 SER A CA 2531 C C . SER A 307 ? 0.2983 0.3203 0.3902 0.0303 -0.0554 -0.0816 323 SER A C 2532 O O . SER A 307 ? 0.2957 0.3185 0.3943 0.0327 -0.0600 -0.0871 323 SER A O 2533 C CB . SER A 307 ? 0.2849 0.3092 0.3843 0.0242 -0.0425 -0.0821 323 SER A CB 2534 O OG . SER A 307 ? 0.2848 0.3092 0.3850 0.0213 -0.0375 -0.0805 323 SER A OG 2535 N N . ILE A 308 ? 0.2973 0.3181 0.3774 0.0303 -0.0547 -0.0755 324 ILE A N 2536 C CA . ILE A 308 ? 0.3082 0.3287 0.3824 0.0329 -0.0583 -0.0748 324 ILE A CA 2537 C C . ILE A 308 ? 0.3069 0.3288 0.3785 0.0312 -0.0526 -0.0731 324 ILE A C 2538 O O . ILE A 308 ? 0.2925 0.3138 0.3566 0.0292 -0.0485 -0.0676 324 ILE A O 2539 C CB . ILE A 308 ? 0.3182 0.3358 0.3804 0.0346 -0.0628 -0.0690 324 ILE A CB 2540 C CG1 . ILE A 308 ? 0.3268 0.3426 0.3922 0.0366 -0.0689 -0.0710 324 ILE A CG1 2541 C CG2 . ILE A 308 ? 0.3268 0.3443 0.3815 0.0369 -0.0655 -0.0677 324 ILE A CG2 2542 C CD1 . ILE A 308 ? 0.3323 0.3446 0.3866 0.0376 -0.0725 -0.0649 324 ILE A CD1 2543 N N . ILE A 309 ? 0.3123 0.3361 0.3905 0.0321 -0.0524 -0.0780 325 ILE A N 2544 C CA . ILE A 309 ? 0.3219 0.3470 0.3995 0.0304 -0.0467 -0.0771 325 ILE A CA 2545 C C . ILE A 309 ? 0.3342 0.3599 0.4070 0.0327 -0.0492 -0.0771 325 ILE A C 2546 O O . ILE A 309 ? 0.3390 0.3658 0.4123 0.0317 -0.0451 -0.0771 325 ILE A O 2547 C CB . ILE A 309 ? 0.3190 0.3459 0.4090 0.0283 -0.0416 -0.0823 325 ILE A CB 2548 C CG1 . ILE A 309 ? 0.3166 0.3452 0.4180 0.0303 -0.0454 -0.0902 325 ILE A CG1 2549 C CG2 . ILE A 309 ? 0.3124 0.3387 0.4052 0.0256 -0.0380 -0.0813 325 ILE A CG2 2550 C CD1 . ILE A 309 ? 0.3156 0.3460 0.4295 0.0281 -0.0401 -0.0955 325 ILE A CD1 2551 N N . GLU A 310 ? 0.3610 0.3858 0.4288 0.0358 -0.0559 -0.0770 326 GLU A N 2552 C CA . GLU A 310 ? 0.3812 0.4064 0.4428 0.0382 -0.0588 -0.0766 326 GLU A CA 2553 C C . GLU A 310 ? 0.3863 0.4090 0.4360 0.0402 -0.0637 -0.0717 326 GLU A C 2554 O O . GLU A 310 ? 0.3748 0.3958 0.4247 0.0409 -0.0671 -0.0714 326 GLU A O 2555 C CB . GLU A 310 ? 0.4207 0.4477 0.4912 0.0409 -0.0630 -0.0841 326 GLU A CB 2556 C CG . GLU A 310 ? 0.4624 0.4920 0.5433 0.0394 -0.0583 -0.0890 326 GLU A CG 2557 C CD . GLU A 310 ? 0.4986 0.5302 0.5880 0.0423 -0.0629 -0.0966 326 GLU A CD 2558 O OE1 . GLU A 310 ? 0.5195 0.5507 0.6100 0.0451 -0.0695 -0.0993 326 GLU A OE1 2559 O OE2 . GLU A 310 ? 0.5246 0.5581 0.6198 0.0418 -0.0600 -0.0999 326 GLU A OE2 2560 N N . LYS A 311 ? 0.3782 0.4008 0.4180 0.0411 -0.0639 -0.0681 327 LYS A N 2561 C CA . LYS A 311 ? 0.3996 0.4198 0.4279 0.0431 -0.0686 -0.0637 327 LYS A CA 2562 C C . LYS A 311 ? 0.4146 0.4342 0.4452 0.0469 -0.0761 -0.0681 327 LYS A C 2563 O O . LYS A 311 ? 0.4109 0.4325 0.4466 0.0489 -0.0782 -0.0735 327 LYS A O 2564 C CB . LYS A 311 ? 0.3976 0.4181 0.4154 0.0434 -0.0671 -0.0596 327 LYS A CB 2565 C CG . LYS A 311 ? 0.4012 0.4190 0.4062 0.0447 -0.0704 -0.0539 327 LYS A CG 2566 C CD . LYS A 311 ? 0.4104 0.4289 0.4055 0.0445 -0.0680 -0.0498 327 LYS A CD 2567 C CE . LYS A 311 ? 0.4267 0.4424 0.4093 0.0455 -0.0708 -0.0442 327 LYS A CE 2568 N NZ . LYS A 311 ? 0.4334 0.4498 0.4064 0.0449 -0.0679 -0.0400 327 LYS A NZ 2569 N N . PRO A 312 ? 0.4353 0.4519 0.4624 0.0480 -0.0803 -0.0660 328 PRO A N 2570 C CA . PRO A 312 ? 0.4556 0.4710 0.4839 0.0519 -0.0880 -0.0696 328 PRO A CA 2571 C C . PRO A 312 ? 0.4857 0.5010 0.5052 0.0551 -0.0919 -0.0693 328 PRO A C 2572 O O . PRO A 312 ? 0.4855 0.5003 0.4945 0.0544 -0.0896 -0.0641 328 PRO A O 2573 C CB . PRO A 312 ? 0.4598 0.4713 0.4827 0.0519 -0.0905 -0.0650 328 PRO A CB 2574 C CG . PRO A 312 ? 0.4518 0.4635 0.4766 0.0477 -0.0840 -0.0618 328 PRO A CG 2575 C CD . PRO A 312 ? 0.4354 0.4497 0.4583 0.0456 -0.0780 -0.0604 328 PRO A CD 2576 N N . THR A 313 ? 0.5067 0.5228 0.5308 0.0587 -0.0978 -0.0752 329 THR A N 2577 C CA . THR A 313 ? 0.5434 0.5600 0.5600 0.0620 -0.1017 -0.0759 329 THR A CA 2578 C C . THR A 313 ? 0.5736 0.5864 0.5805 0.0657 -0.1091 -0.0737 329 THR A C 2579 O O . THR A 313 ? 0.5888 0.6016 0.5884 0.0688 -0.1128 -0.0742 329 THR A O 2580 C CB . THR A 313 ? 0.5429 0.5633 0.5701 0.0637 -0.1031 -0.0843 329 THR A CB 2581 O OG1 . THR A 313 ? 0.5453 0.5663 0.5849 0.0646 -0.1062 -0.0902 329 THR A OG1 2582 C CG2 . THR A 313 ? 0.5374 0.5611 0.5703 0.0603 -0.0956 -0.0850 329 THR A CG2 2583 N N . ASP A 314 ? 0.5851 0.5945 0.5918 0.0656 -0.1111 -0.0713 330 ASP A N 2584 C CA . ASP A 314 ? 0.6068 0.6116 0.6025 0.0686 -0.1172 -0.0675 330 ASP A CA 2585 C C . ASP A 314 ? 0.6243 0.6267 0.6054 0.0669 -0.1138 -0.0591 330 ASP A C 2586 O O . ASP A 314 ? 0.6493 0.6541 0.6295 0.0638 -0.1074 -0.0569 330 ASP A O 2587 C CB . ASP A 314 ? 0.6004 0.6021 0.6012 0.0688 -0.1203 -0.0678 330 ASP A CB 2588 C CG . ASP A 314 ? 0.6118 0.6139 0.6183 0.0642 -0.1139 -0.0654 330 ASP A CG 2589 O OD1 . ASP A 314 ? 0.6071 0.6104 0.6097 0.0609 -0.1075 -0.0614 330 ASP A OD1 2590 O OD2 . ASP A 314 ? 0.6069 0.6083 0.6219 0.0639 -0.1154 -0.0677 330 ASP A OD2 2591 N N . GLY A 315 ? 0.6341 0.6318 0.6039 0.0690 -0.1180 -0.0544 331 GLY A N 2592 C CA . GLY A 315 ? 0.6241 0.6197 0.5799 0.0676 -0.1149 -0.0467 331 GLY A CA 2593 C C . GLY A 315 ? 0.6002 0.5946 0.5549 0.0632 -0.1089 -0.0409 331 GLY A C 2594 O O . GLY A 315 ? 0.6104 0.6036 0.5548 0.0616 -0.1057 -0.0349 331 GLY A O 2595 N N . ARG A 316 ? 0.5712 0.5662 0.5368 0.0611 -0.1074 -0.0429 332 ARG A N 2596 C CA . ARG A 316 ? 0.5496 0.5423 0.5141 0.0578 -0.1037 -0.0377 332 ARG A CA 2597 C C . ARG A 316 ? 0.5367 0.5314 0.4979 0.0539 -0.0962 -0.0334 332 ARG A C 2598 O O . ARG A 316 ? 0.5332 0.5320 0.4973 0.0528 -0.0924 -0.0357 332 ARG A O 2599 C CB . ARG A 316 ? 0.5364 0.5295 0.5137 0.0568 -0.1042 -0.0416 332 ARG A CB 2600 C CG . ARG A 316 ? 0.5330 0.5307 0.5209 0.0535 -0.0980 -0.0447 332 ARG A CG 2601 C CD . ARG A 316 ? 0.5495 0.5490 0.5509 0.0546 -0.1006 -0.0522 332 ARG A CD 2602 N NE . ARG A 316 ? 0.5522 0.5535 0.5635 0.0513 -0.0958 -0.0537 332 ARG A NE 2603 C CZ . ARG A 316 ? 0.5369 0.5403 0.5610 0.0514 -0.0966 -0.0601 332 ARG A CZ 2604 N NH1 . ARG A 316 ? 0.5275 0.5314 0.5568 0.0548 -0.1021 -0.0659 332 ARG A NH1 2605 N NH2 . ARG A 316 ? 0.5406 0.5455 0.5724 0.0482 -0.0917 -0.0610 332 ARG A NH2 2606 N N . ASP A 317 ? 0.5207 0.5125 0.4760 0.0518 -0.0942 -0.0273 333 ASP A N 2607 C CA . ASP A 317 ? 0.5033 0.4968 0.4569 0.0479 -0.0873 -0.0234 333 ASP A CA 2608 C C . ASP A 317 ? 0.4727 0.4679 0.4374 0.0452 -0.0842 -0.0257 333 ASP A C 2609 O O . ASP A 317 ? 0.4673 0.4605 0.4374 0.0458 -0.0872 -0.0273 333 ASP A O 2610 C CB . ASP A 317 ? 0.5292 0.5190 0.4717 0.0469 -0.0866 -0.0161 333 ASP A CB 2611 C CG . ASP A 317 ? 0.5658 0.5543 0.4963 0.0489 -0.0882 -0.0134 333 ASP A CG 2612 O OD1 . ASP A 317 ? 0.5855 0.5776 0.5142 0.0485 -0.0851 -0.0142 333 ASP A OD1 2613 O OD2 . ASP A 317 ? 0.5805 0.5645 0.5032 0.0510 -0.0924 -0.0105 333 ASP A OD2 2614 N N . LEU A 318 ? 0.4349 0.4337 0.4029 0.0425 -0.0782 -0.0259 334 LEU A N 2615 C CA . LEU A 318 ? 0.4114 0.4119 0.3886 0.0396 -0.0743 -0.0275 334 LEU A CA 2616 C C . LEU A 318 ? 0.3926 0.3955 0.3676 0.0365 -0.0677 -0.0244 334 LEU A C 2617 O O . LEU A 318 ? 0.3860 0.3899 0.3542 0.0366 -0.0660 -0.0222 334 LEU A O 2618 C CB . LEU A 318 ? 0.4066 0.4097 0.3958 0.0404 -0.0751 -0.0347 334 LEU A CB 2619 C CG . LEU A 318 ? 0.4100 0.4170 0.4026 0.0403 -0.0720 -0.0380 334 LEU A CG 2620 C CD1 . LEU A 318 ? 0.4034 0.4129 0.4090 0.0391 -0.0699 -0.0437 334 LEU A CD1 2621 C CD2 . LEU A 318 ? 0.4154 0.4225 0.4041 0.0437 -0.0764 -0.0401 334 LEU A CD2 2622 N N . VAL A 319 ? 0.3730 0.3770 0.3539 0.0338 -0.0639 -0.0245 335 VAL A N 2623 C CA . VAL A 319 ? 0.3639 0.3705 0.3443 0.0310 -0.0577 -0.0225 335 VAL A CA 2624 C C . VAL A 319 ? 0.3528 0.3625 0.3412 0.0309 -0.0553 -0.0276 335 VAL A C 2625 O O . VAL A 319 ? 0.3423 0.3527 0.3400 0.0307 -0.0555 -0.0319 335 VAL A O 2626 C CB . VAL A 319 ? 0.3521 0.3583 0.3347 0.0283 -0.0548 -0.0203 335 VAL A CB 2627 C CG1 . VAL A 319 ? 0.3433 0.3521 0.3249 0.0257 -0.0486 -0.0183 335 VAL A CG1 2628 C CG2 . VAL A 319 ? 0.3541 0.3568 0.3298 0.0283 -0.0572 -0.0156 335 VAL A CG2 2629 N N . CYS A 320 ? 0.3499 0.3616 0.3351 0.0311 -0.0531 -0.0273 336 CYS A N 2630 C CA . CYS A 320 ? 0.3560 0.3704 0.3485 0.0309 -0.0505 -0.0317 336 CYS A CA 2631 C C . CYS A 320 ? 0.3442 0.3603 0.3387 0.0280 -0.0442 -0.0303 336 CYS A C 2632 O O . CYS A 320 ? 0.3636 0.3814 0.3653 0.0274 -0.0415 -0.0339 336 CYS A O 2633 C CB . CYS A 320 ? 0.3751 0.3908 0.3646 0.0329 -0.0517 -0.0332 336 CYS A CB 2634 S SG . CYS A 320 ? 0.4093 0.4252 0.4049 0.0364 -0.0577 -0.0399 336 CYS A SG 2635 N N . HIS A 321 ? 0.3229 0.3385 0.3112 0.0262 -0.0417 -0.0252 337 HIS A N 2636 C CA . HIS A 321 ? 0.3013 0.3183 0.2912 0.0237 -0.0361 -0.0239 337 HIS A CA 2637 C C . HIS A 321 ? 0.3000 0.3171 0.2992 0.0226 -0.0349 -0.0275 337 HIS A C 2638 O O . HIS A 321 ? 0.3007 0.3164 0.3021 0.0226 -0.0374 -0.0280 337 HIS A O 2639 C CB . HIS A 321 ? 0.2912 0.3076 0.2739 0.0221 -0.0342 -0.0183 337 HIS A CB 2640 C CG . HIS A 321 ? 0.2806 0.2987 0.2636 0.0200 -0.0288 -0.0168 337 HIS A CG 2641 N ND1 . HIS A 321 ? 0.2759 0.2953 0.2540 0.0198 -0.0262 -0.0145 337 HIS A ND1 2642 C CD2 . HIS A 321 ? 0.2767 0.2952 0.2643 0.0181 -0.0255 -0.0175 337 HIS A CD2 2643 C CE1 . HIS A 321 ? 0.2815 0.3020 0.2610 0.0181 -0.0218 -0.0137 337 HIS A CE1 2644 N NE2 . HIS A 321 ? 0.2742 0.2941 0.2592 0.0170 -0.0212 -0.0154 337 HIS A NE2 2645 N N . ALA A 322 ? 0.2893 0.3080 0.2940 0.0216 -0.0309 -0.0300 338 ALA A N 2646 C CA . ALA A 322 ? 0.2881 0.3072 0.3025 0.0207 -0.0294 -0.0343 338 ALA A CA 2647 C C . ALA A 322 ? 0.2889 0.3075 0.3041 0.0188 -0.0278 -0.0327 338 ALA A C 2648 O O . ALA A 322 ? 0.2907 0.3092 0.2999 0.0174 -0.0254 -0.0283 338 ALA A O 2649 C CB . ALA A 322 ? 0.2795 0.3001 0.2985 0.0198 -0.0247 -0.0365 338 ALA A CB 2650 N N . SER A 323 ? 0.2817 0.3000 0.3045 0.0187 -0.0291 -0.0365 339 SER A N 2651 C CA . SER A 323 ? 0.2764 0.2943 0.3007 0.0169 -0.0276 -0.0357 339 SER A CA 2652 C C . SER A 323 ? 0.2741 0.2927 0.3089 0.0163 -0.0269 -0.0411 339 SER A C 2653 O O . SER A 323 ? 0.2672 0.2860 0.3085 0.0177 -0.0295 -0.0456 339 SER A O 2654 C CB . SER A 323 ? 0.2814 0.2976 0.3007 0.0176 -0.0318 -0.0326 339 SER A CB 2655 O OG . SER A 323 ? 0.3027 0.3177 0.3252 0.0197 -0.0372 -0.0355 339 SER A OG 2656 N N . ALA A 324 ? 0.2637 0.2827 0.3002 0.0142 -0.0233 -0.0406 340 ALA A N 2657 C CA . ALA A 324 ? 0.2653 0.2851 0.3113 0.0133 -0.0220 -0.0454 340 ALA A CA 2658 C C . ALA A 324 ? 0.2681 0.2871 0.3145 0.0129 -0.0242 -0.0448 340 ALA A C 2659 O O . ALA A 324 ? 0.2597 0.2782 0.2992 0.0121 -0.0239 -0.0403 340 ALA A O 2660 C CB . ALA A 324 ? 0.2593 0.2801 0.3070 0.0111 -0.0153 -0.0457 340 ALA A CB 2661 N N . TRP A 325 ? 0.2721 0.2912 0.3270 0.0133 -0.0265 -0.0497 341 TRP A N 2662 C CA . TRP A 325 ? 0.2855 0.3037 0.3419 0.0136 -0.0301 -0.0498 341 TRP A CA 2663 C C . TRP A 325 ? 0.2889 0.3084 0.3543 0.0122 -0.0278 -0.0543 341 TRP A C 2664 O O . TRP A 325 ? 0.2808 0.3015 0.3546 0.0122 -0.0268 -0.0595 341 TRP A O 2665 C CB . TRP A 325 ? 0.2889 0.3054 0.3465 0.0164 -0.0369 -0.0513 341 TRP A CB 2666 C CG . TRP A 325 ? 0.3009 0.3158 0.3490 0.0179 -0.0396 -0.0467 341 TRP A CG 2667 C CD1 . TRP A 325 ? 0.3036 0.3191 0.3480 0.0186 -0.0387 -0.0459 341 TRP A CD1 2668 C CD2 . TRP A 325 ? 0.3117 0.3242 0.3527 0.0188 -0.0435 -0.0425 341 TRP A CD2 2669 N NE1 . TRP A 325 ? 0.3079 0.3217 0.3432 0.0200 -0.0418 -0.0414 341 TRP A NE1 2670 C CE2 . TRP A 325 ? 0.3136 0.3254 0.3466 0.0200 -0.0446 -0.0391 341 TRP A CE2 2671 C CE3 . TRP A 325 ? 0.3172 0.3279 0.3581 0.0187 -0.0461 -0.0412 341 TRP A CE3 2672 C CZ2 . TRP A 325 ? 0.3262 0.3354 0.3508 0.0210 -0.0479 -0.0344 341 TRP A CZ2 2673 C CZ3 . TRP A 325 ? 0.3328 0.3408 0.3657 0.0196 -0.0495 -0.0364 341 TRP A CZ3 2674 C CH2 . TRP A 325 ? 0.3327 0.3399 0.3573 0.0207 -0.0502 -0.0330 341 TRP A CH2 2675 N N . ASP A 326 ? 0.2913 0.3107 0.3550 0.0108 -0.0267 -0.0525 342 ASP A N 2676 C CA . ASP A 326 ? 0.2919 0.3127 0.3636 0.0094 -0.0248 -0.0567 342 ASP A CA 2677 C C . ASP A 326 ? 0.2936 0.3130 0.3683 0.0106 -0.0302 -0.0578 342 ASP A C 2678 O O . ASP A 326 ? 0.2952 0.3131 0.3635 0.0108 -0.0325 -0.0535 342 ASP A O 2679 C CB . ASP A 326 ? 0.2916 0.3134 0.3593 0.0070 -0.0191 -0.0542 342 ASP A CB 2680 C CG . ASP A 326 ? 0.3053 0.3289 0.3809 0.0054 -0.0161 -0.0587 342 ASP A CG 2681 O OD1 . ASP A 326 ? 0.3098 0.3338 0.3945 0.0061 -0.0186 -0.0639 342 ASP A OD1 2682 O OD2 . ASP A 326 ? 0.2943 0.3189 0.3670 0.0035 -0.0113 -0.0573 342 ASP A OD2 2683 N N . PHE A 327 ? 0.2954 0.3154 0.3801 0.0113 -0.0323 -0.0636 343 PHE A N 2684 C CA . PHE A 327 ? 0.3044 0.3230 0.3927 0.0128 -0.0381 -0.0650 343 PHE A CA 2685 C C . PHE A 327 ? 0.3099 0.3296 0.4036 0.0112 -0.0365 -0.0674 343 PHE A C 2686 O O . PHE A 327 ? 0.3215 0.3398 0.4188 0.0123 -0.0411 -0.0688 343 PHE A O 2687 C CB . PHE A 327 ? 0.3075 0.3256 0.4026 0.0153 -0.0431 -0.0695 343 PHE A CB 2688 C CG . PHE A 327 ? 0.3095 0.3256 0.3974 0.0175 -0.0467 -0.0663 343 PHE A CG 2689 C CD1 . PHE A 327 ? 0.3106 0.3279 0.3963 0.0173 -0.0437 -0.0660 343 PHE A CD1 2690 C CD2 . PHE A 327 ? 0.3208 0.3338 0.4036 0.0196 -0.0526 -0.0632 343 PHE A CD2 2691 C CE1 . PHE A 327 ? 0.3120 0.3278 0.3909 0.0193 -0.0469 -0.0631 343 PHE A CE1 2692 C CE2 . PHE A 327 ? 0.3171 0.3283 0.3925 0.0215 -0.0556 -0.0601 343 PHE A CE2 2693 C CZ . PHE A 327 ? 0.3204 0.3332 0.3939 0.0214 -0.0528 -0.0602 343 PHE A CZ 2694 N N . TYR A 328 ? 0.3127 0.3346 0.4064 0.0087 -0.0301 -0.0677 344 TYR A N 2695 C CA . TYR A 328 ? 0.3242 0.3474 0.4206 0.0069 -0.0276 -0.0690 344 TYR A CA 2696 C C . TYR A 328 ? 0.3238 0.3484 0.4322 0.0070 -0.0288 -0.0758 344 TYR A C 2697 O O . TYR A 328 ? 0.3242 0.3493 0.4354 0.0063 -0.0291 -0.0770 344 TYR A O 2698 C CB . TYR A 328 ? 0.3450 0.3665 0.4344 0.0070 -0.0300 -0.0641 344 TYR A CB 2699 C CG . TYR A 328 ? 0.3708 0.3916 0.4490 0.0065 -0.0281 -0.0578 344 TYR A CG 2700 C CD1 . TYR A 328 ? 0.3881 0.4107 0.4621 0.0045 -0.0220 -0.0561 344 TYR A CD1 2701 C CD2 . TYR A 328 ? 0.3948 0.4130 0.4665 0.0081 -0.0322 -0.0535 344 TYR A CD2 2702 C CE1 . TYR A 328 ? 0.4134 0.4355 0.4776 0.0042 -0.0204 -0.0505 344 TYR A CE1 2703 C CE2 . TYR A 328 ? 0.4188 0.4366 0.4807 0.0076 -0.0304 -0.0480 344 TYR A CE2 2704 C CZ . TYR A 328 ? 0.4279 0.4477 0.4865 0.0058 -0.0246 -0.0467 344 TYR A CZ 2705 O OH . TYR A 328 ? 0.4880 0.5075 0.5373 0.0055 -0.0230 -0.0414 344 TYR A OH 2706 N N . LEU A 329 ? 0.3203 0.3457 0.4361 0.0080 -0.0296 -0.0804 345 LEU A N 2707 C CA . LEU A 329 ? 0.3202 0.3474 0.4483 0.0079 -0.0298 -0.0876 345 LEU A CA 2708 C C . LEU A 329 ? 0.3190 0.3489 0.4511 0.0057 -0.0226 -0.0906 345 LEU A C 2709 O O . LEU A 329 ? 0.3141 0.3446 0.4399 0.0036 -0.0169 -0.0875 345 LEU A O 2710 C CB . LEU A 329 ? 0.3140 0.3401 0.4487 0.0108 -0.0365 -0.0911 345 LEU A CB 2711 C CG . LEU A 329 ? 0.3238 0.3465 0.4535 0.0133 -0.0439 -0.0875 345 LEU A CG 2712 C CD1 . LEU A 329 ? 0.3269 0.3484 0.4625 0.0164 -0.0503 -0.0912 345 LEU A CD1 2713 C CD2 . LEU A 329 ? 0.3205 0.3423 0.4509 0.0128 -0.0456 -0.0869 345 LEU A CD2 2714 N N . THR A 330 ? 0.3134 0.3448 0.4559 0.0061 -0.0226 -0.0967 346 THR A N 2715 C CA . THR A 330 ? 0.3225 0.3559 0.4689 0.0041 -0.0159 -0.0995 346 THR A CA 2716 C C . THR A 330 ? 0.3219 0.3546 0.4695 0.0057 -0.0178 -0.1003 346 THR A C 2717 O O . THR A 330 ? 0.3232 0.3558 0.4775 0.0080 -0.0234 -0.1040 346 THR A O 2718 C CB . THR A 330 ? 0.3352 0.3714 0.4943 0.0028 -0.0132 -0.1070 346 THR A CB 2719 O OG1 . THR A 330 ? 0.3670 0.4038 0.5251 0.0017 -0.0123 -0.1066 346 THR A OG1 2720 C CG2 . THR A 330 ? 0.3333 0.3712 0.4958 0.0004 -0.0053 -0.1094 346 THR A CG2 2721 N N . ASP A 331 ? 0.3167 0.3490 0.4576 0.0047 -0.0134 -0.0966 347 ASP A N 2722 C CA . ASP A 331 ? 0.3127 0.3448 0.4554 0.0058 -0.0139 -0.0978 347 ASP A CA 2723 C C . ASP A 331 ? 0.3107 0.3410 0.4492 0.0089 -0.0213 -0.0957 347 ASP A C 2724 O O . ASP A 331 ? 0.3025 0.3330 0.4438 0.0102 -0.0226 -0.0976 347 ASP A O 2725 C CB . ASP A 331 ? 0.3157 0.3502 0.4725 0.0053 -0.0122 -0.1058 347 ASP A CB 2726 C CG . ASP A 331 ? 0.3220 0.3579 0.4818 0.0020 -0.0035 -0.1074 347 ASP A CG 2727 O OD1 . ASP A 331 ? 0.3235 0.3586 0.4740 0.0003 0.0012 -0.1022 347 ASP A OD1 2728 O OD2 . ASP A 331 ? 0.3310 0.3690 0.5026 0.0012 -0.0014 -0.1141 347 ASP A OD2 2729 N N . ASP A 332 ? 0.3095 0.3379 0.4416 0.0102 -0.0261 -0.0918 348 ASP A N 2730 C CA . ASP A 332 ? 0.3107 0.3370 0.4371 0.0131 -0.0326 -0.0890 348 ASP A CA 2731 C C . ASP A 332 ? 0.3020 0.3269 0.4155 0.0125 -0.0302 -0.0817 348 ASP A C 2732 O O . ASP A 332 ? 0.2943 0.3180 0.4001 0.0119 -0.0304 -0.0768 348 ASP A O 2733 C CB . ASP A 332 ? 0.3329 0.3575 0.4598 0.0151 -0.0394 -0.0889 348 ASP A CB 2734 C CG . ASP A 332 ? 0.3559 0.3780 0.4778 0.0183 -0.0463 -0.0868 348 ASP A CG 2735 O OD1 . ASP A 332 ? 0.3707 0.3925 0.4872 0.0190 -0.0459 -0.0845 348 ASP A OD1 2736 O OD2 . ASP A 332 ? 0.3821 0.4025 0.5054 0.0203 -0.0524 -0.0874 348 ASP A OD2 2737 N N . VAL A 333 ? 0.2974 0.3227 0.4096 0.0124 -0.0279 -0.0815 349 VAL A N 2738 C CA . VAL A 333 ? 0.2901 0.3144 0.3913 0.0120 -0.0255 -0.0753 349 VAL A CA 2739 C C . VAL A 333 ? 0.2970 0.3209 0.3974 0.0142 -0.0287 -0.0759 349 VAL A C 2740 O O . VAL A 333 ? 0.3029 0.3280 0.4124 0.0151 -0.0298 -0.0816 349 VAL A O 2741 C CB . VAL A 333 ? 0.2813 0.3068 0.3815 0.0091 -0.0174 -0.0744 349 VAL A CB 2742 C CG1 . VAL A 333 ? 0.2798 0.3056 0.3786 0.0071 -0.0143 -0.0730 349 VAL A CG1 2743 C CG2 . VAL A 333 ? 0.2812 0.3083 0.3916 0.0083 -0.0139 -0.0802 349 VAL A CG2 2744 N N . ARG A 334 ? 0.2922 0.3146 0.3820 0.0152 -0.0302 -0.0703 350 ARG A N 2745 C CA . ARG A 334 ? 0.2924 0.3143 0.3802 0.0176 -0.0340 -0.0706 350 ARG A CA 2746 C C . ARG A 334 ? 0.2855 0.3067 0.3627 0.0173 -0.0319 -0.0648 350 ARG A C 2747 O O . ARG A 334 ? 0.2792 0.2998 0.3487 0.0160 -0.0297 -0.0597 350 ARG A O 2748 C CB . ARG A 334 ? 0.3063 0.3263 0.3919 0.0204 -0.0417 -0.0701 350 ARG A CB 2749 C CG . ARG A 334 ? 0.3227 0.3430 0.4182 0.0215 -0.0456 -0.0756 350 ARG A CG 2750 C CD . ARG A 334 ? 0.3264 0.3441 0.4173 0.0242 -0.0529 -0.0736 350 ARG A CD 2751 N NE . ARG A 334 ? 0.3312 0.3486 0.4290 0.0241 -0.0549 -0.0765 350 ARG A NE 2752 C CZ . ARG A 334 ? 0.3423 0.3572 0.4382 0.0260 -0.0608 -0.0753 350 ARG A CZ 2753 N NH1 . ARG A 334 ? 0.3549 0.3670 0.4416 0.0282 -0.0652 -0.0710 350 ARG A NH1 2754 N NH2 . ARG A 334 ? 0.3544 0.3693 0.4576 0.0257 -0.0621 -0.0783 350 ARG A NH2 2755 N N . ILE A 335 ? 0.2773 0.2990 0.3544 0.0188 -0.0329 -0.0660 351 ILE A N 2756 C CA . ILE A 335 ? 0.2688 0.2899 0.3360 0.0191 -0.0321 -0.0610 351 ILE A CA 2757 C C . ILE A 335 ? 0.2764 0.2964 0.3397 0.0222 -0.0386 -0.0608 351 ILE A C 2758 O O . ILE A 335 ? 0.2718 0.2922 0.3419 0.0242 -0.0428 -0.0657 351 ILE A O 2759 C CB . ILE A 335 ? 0.2688 0.2911 0.3382 0.0178 -0.0265 -0.0620 351 ILE A CB 2760 C CG1 . ILE A 335 ? 0.2608 0.2832 0.3288 0.0148 -0.0200 -0.0596 351 ILE A CG1 2761 C CG2 . ILE A 335 ? 0.2696 0.2917 0.3313 0.0190 -0.0271 -0.0589 351 ILE A CG2 2762 C CD1 . ILE A 335 ? 0.2662 0.2895 0.3384 0.0133 -0.0141 -0.0613 351 ILE A CD1 2763 N N . LYS A 336 ? 0.2787 0.2975 0.3312 0.0227 -0.0396 -0.0552 352 LYS A N 2764 C CA . LYS A 336 ? 0.2828 0.3007 0.3298 0.0255 -0.0446 -0.0543 352 LYS A CA 2765 C C . LYS A 336 ? 0.2870 0.3058 0.3278 0.0251 -0.0413 -0.0513 352 LYS A C 2766 O O . LYS A 336 ? 0.2875 0.3058 0.3204 0.0237 -0.0385 -0.0461 352 LYS A O 2767 C CB . LYS A 336 ? 0.2854 0.3008 0.3247 0.0266 -0.0490 -0.0501 352 LYS A CB 2768 C CG . LYS A 336 ? 0.2880 0.3021 0.3204 0.0295 -0.0541 -0.0487 352 LYS A CG 2769 C CD . LYS A 336 ? 0.2958 0.3068 0.3235 0.0309 -0.0594 -0.0462 352 LYS A CD 2770 C CE . LYS A 336 ? 0.2932 0.3028 0.3146 0.0288 -0.0570 -0.0404 352 LYS A CE 2771 N NZ . LYS A 336 ? 0.2968 0.3066 0.3083 0.0280 -0.0543 -0.0352 352 LYS A NZ 2772 N N . GLN A 337 ? 0.2904 0.3106 0.3352 0.0263 -0.0415 -0.0551 353 GLN A N 2773 C CA . GLN A 337 ? 0.2908 0.3119 0.3308 0.0260 -0.0385 -0.0530 353 GLN A CA 2774 C C . GLN A 337 ? 0.2994 0.3210 0.3394 0.0289 -0.0427 -0.0559 353 GLN A C 2775 O O . GLN A 337 ? 0.3031 0.3255 0.3517 0.0303 -0.0453 -0.0617 353 GLN A O 2776 C CB . GLN A 337 ? 0.2867 0.3090 0.3329 0.0237 -0.0321 -0.0548 353 GLN A CB 2777 C CG . GLN A 337 ? 0.2876 0.3106 0.3294 0.0234 -0.0287 -0.0526 353 GLN A CG 2778 C CD . GLN A 337 ? 0.2829 0.3065 0.3298 0.0210 -0.0221 -0.0534 353 GLN A CD 2779 O OE1 . GLN A 337 ? 0.2880 0.3112 0.3387 0.0191 -0.0191 -0.0538 353 GLN A OE1 2780 N NE2 . GLN A 337 ? 0.2809 0.3050 0.3274 0.0211 -0.0196 -0.0536 353 GLN A NE2 2781 N N . CYS A 338 ? 0.3088 0.3301 0.3393 0.0299 -0.0437 -0.0522 354 CYS A N 2782 C CA . CYS A 338 ? 0.3158 0.3379 0.3453 0.0327 -0.0474 -0.0548 354 CYS A CA 2783 C C . CYS A 338 ? 0.3081 0.3323 0.3424 0.0319 -0.0431 -0.0573 354 CYS A C 2784 O O . CYS A 338 ? 0.3081 0.3328 0.3363 0.0320 -0.0416 -0.0548 354 CYS A O 2785 C CB . CYS A 338 ? 0.3331 0.3540 0.3502 0.0341 -0.0503 -0.0498 354 CYS A CB 2786 S SG . CYS A 338 ? 0.3512 0.3690 0.3636 0.0350 -0.0552 -0.0469 354 CYS A SG 2787 N N . THR A 339 ? 0.2991 0.3243 0.3446 0.0310 -0.0411 -0.0623 355 THR A N 2788 C CA . THR A 339 ? 0.2962 0.3227 0.3475 0.0295 -0.0358 -0.0644 355 THR A CA 2789 C C . THR A 339 ? 0.3038 0.3317 0.3551 0.0315 -0.0374 -0.0669 355 THR A C 2790 O O . THR A 339 ? 0.3027 0.3314 0.3561 0.0341 -0.0427 -0.0708 355 THR A O 2791 C CB . THR A 339 ? 0.2976 0.3247 0.3616 0.0281 -0.0335 -0.0698 355 THR A CB 2792 O OG1 . THR A 339 ? 0.2898 0.3158 0.3543 0.0267 -0.0332 -0.0683 355 THR A OG1 2793 C CG2 . THR A 339 ? 0.2925 0.3200 0.3610 0.0258 -0.0268 -0.0702 355 THR A CG2 2794 N N . ARG A 340 ? 0.3060 0.3344 0.3550 0.0303 -0.0328 -0.0648 356 ARG A N 2795 C CA . ARG A 340 ? 0.3190 0.3489 0.3694 0.0317 -0.0332 -0.0675 356 ARG A CA 2796 C C . ARG A 340 ? 0.3130 0.3433 0.3726 0.0297 -0.0275 -0.0703 356 ARG A C 2797 O O . ARG A 340 ? 0.3149 0.3440 0.3762 0.0271 -0.0226 -0.0682 356 ARG A O 2798 C CB . ARG A 340 ? 0.3272 0.3572 0.3661 0.0324 -0.0332 -0.0624 356 ARG A CB 2799 C CG . ARG A 340 ? 0.3442 0.3735 0.3738 0.0346 -0.0389 -0.0600 356 ARG A CG 2800 C CD . ARG A 340 ? 0.3503 0.3793 0.3681 0.0343 -0.0377 -0.0538 356 ARG A CD 2801 N NE . ARG A 340 ? 0.3602 0.3880 0.3748 0.0316 -0.0334 -0.0488 356 ARG A NE 2802 C CZ . ARG A 340 ? 0.3598 0.3879 0.3739 0.0298 -0.0282 -0.0464 356 ARG A CZ 2803 N NH1 . ARG A 340 ? 0.3651 0.3945 0.3818 0.0302 -0.0263 -0.0485 356 ARG A NH1 2804 N NH2 . ARG A 340 ? 0.3669 0.3939 0.3778 0.0276 -0.0249 -0.0420 356 ARG A NH2 2805 N N . VAL A 341 ? 0.3047 0.3365 0.3703 0.0310 -0.0280 -0.0751 357 VAL A N 2806 C CA . VAL A 341 ? 0.2999 0.3319 0.3751 0.0292 -0.0228 -0.0782 357 VAL A CA 2807 C C . VAL A 341 ? 0.2982 0.3297 0.3681 0.0282 -0.0183 -0.0741 357 VAL A C 2808 O O . VAL A 341 ? 0.3001 0.3327 0.3710 0.0296 -0.0188 -0.0762 357 VAL A O 2809 C CB . VAL A 341 ? 0.2952 0.3292 0.3815 0.0310 -0.0255 -0.0862 357 VAL A CB 2810 C CG1 . VAL A 341 ? 0.2927 0.3265 0.3898 0.0289 -0.0197 -0.0895 357 VAL A CG1 2811 C CG2 . VAL A 341 ? 0.2978 0.3323 0.3893 0.0322 -0.0303 -0.0903 357 VAL A CG2 2812 N N . THR A 342 ? 0.2960 0.3257 0.3602 0.0261 -0.0141 -0.0684 358 THR A N 2813 C CA . THR A 342 ? 0.2985 0.3274 0.3575 0.0251 -0.0098 -0.0642 358 THR A CA 2814 C C . THR A 342 ? 0.2996 0.3264 0.3603 0.0222 -0.0036 -0.0615 358 THR A C 2815 O O . THR A 342 ? 0.2913 0.3173 0.3544 0.0209 -0.0030 -0.0617 358 THR A O 2816 C CB . THR A 342 ? 0.3016 0.3307 0.3479 0.0260 -0.0117 -0.0584 358 THR A CB 2817 O OG1 . THR A 342 ? 0.3059 0.3338 0.3470 0.0246 -0.0111 -0.0541 358 THR A OG1 2818 C CG2 . THR A 342 ? 0.3018 0.3327 0.3442 0.0289 -0.0180 -0.0601 358 THR A CG2 2819 N N . GLN A 343 ? 0.3007 0.3264 0.3596 0.0213 0.0007 -0.0589 359 GLN A N 2820 C CA . GLN A 343 ? 0.3145 0.3378 0.3729 0.0188 0.0066 -0.0555 359 GLN A CA 2821 C C . GLN A 343 ? 0.3167 0.3395 0.3666 0.0180 0.0062 -0.0504 359 GLN A C 2822 O O . GLN A 343 ? 0.3086 0.3302 0.3606 0.0163 0.0087 -0.0500 359 GLN A O 2823 C CB . GLN A 343 ? 0.3203 0.3425 0.3764 0.0186 0.0104 -0.0530 359 GLN A CB 2824 C CG . GLN A 343 ? 0.3375 0.3570 0.3905 0.0165 0.0160 -0.0485 359 GLN A CG 2825 C CD . GLN A 343 ? 0.3450 0.3628 0.3981 0.0164 0.0199 -0.0470 359 GLN A CD 2826 O OE1 . GLN A 343 ? 0.3492 0.3667 0.4102 0.0165 0.0212 -0.0510 359 GLN A OE1 2827 N NE2 . GLN A 343 ? 0.3540 0.3707 0.3987 0.0161 0.0218 -0.0415 359 GLN A NE2 2828 N N . ASP A 344 ? 0.3194 0.3432 0.3600 0.0193 0.0032 -0.0467 360 ASP A N 2829 C CA . ASP A 344 ? 0.3410 0.3645 0.3735 0.0187 0.0024 -0.0421 360 ASP A CA 2830 C C . ASP A 344 ? 0.3201 0.3437 0.3558 0.0185 -0.0002 -0.0442 360 ASP A C 2831 O O . ASP A 344 ? 0.3086 0.3314 0.3424 0.0170 0.0013 -0.0418 360 ASP A O 2832 C CB . ASP A 344 ? 0.3920 0.4168 0.4154 0.0204 -0.0009 -0.0390 360 ASP A CB 2833 C CG . ASP A 344 ? 0.4511 0.4758 0.4668 0.0199 -0.0024 -0.0346 360 ASP A CG 2834 O OD1 . ASP A 344 ? 0.5117 0.5355 0.5238 0.0185 0.0008 -0.0309 360 ASP A OD1 2835 O OD2 . ASP A 344 ? 0.4924 0.5179 0.5055 0.0211 -0.0070 -0.0350 360 ASP A OD2 2836 N N . GLN A 345 ? 0.3028 0.3276 0.3436 0.0200 -0.0043 -0.0488 361 GLN A N 2837 C CA . GLN A 345 ? 0.2948 0.3198 0.3397 0.0201 -0.0073 -0.0515 361 GLN A CA 2838 C C . GLN A 345 ? 0.2934 0.3175 0.3475 0.0181 -0.0036 -0.0546 361 GLN A C 2839 O O . GLN A 345 ? 0.2871 0.3110 0.3427 0.0174 -0.0043 -0.0549 361 GLN A O 2840 C CB . GLN A 345 ? 0.2880 0.3143 0.3352 0.0227 -0.0133 -0.0556 361 GLN A CB 2841 C CG . GLN A 345 ? 0.2867 0.3133 0.3236 0.0244 -0.0177 -0.0520 361 GLN A CG 2842 C CD . GLN A 345 ? 0.2892 0.3150 0.3226 0.0242 -0.0205 -0.0499 361 GLN A CD 2843 O OE1 . GLN A 345 ? 0.2866 0.3124 0.3249 0.0252 -0.0241 -0.0535 361 GLN A OE1 2844 N NE2 . GLN A 345 ? 0.2835 0.3085 0.3090 0.0231 -0.0188 -0.0443 361 GLN A NE2 2845 N N . LEU A 346 ? 0.2902 0.3139 0.3505 0.0172 0.0006 -0.0568 362 LEU A N 2846 C CA . LEU A 346 ? 0.2912 0.3139 0.3597 0.0150 0.0052 -0.0593 362 LEU A CA 2847 C C . LEU A 346 ? 0.2930 0.3142 0.3557 0.0130 0.0091 -0.0543 362 LEU A C 2848 O O . LEU A 346 ? 0.2862 0.3071 0.3528 0.0116 0.0107 -0.0557 362 LEU A O 2849 C CB . LEU A 346 ? 0.2986 0.3206 0.3741 0.0144 0.0094 -0.0620 362 LEU A CB 2850 C CG . LEU A 346 ? 0.3074 0.3283 0.3924 0.0120 0.0148 -0.0650 362 LEU A CG 2851 C CD1 . LEU A 346 ? 0.3114 0.3338 0.4058 0.0121 0.0122 -0.0709 362 LEU A CD1 2852 C CD2 . LEU A 346 ? 0.3092 0.3290 0.3998 0.0114 0.0190 -0.0668 362 LEU A CD2 2853 N N . PHE A 347 ? 0.2882 0.3086 0.3417 0.0131 0.0105 -0.0490 363 PHE A N 2854 C CA . PHE A 347 ? 0.2946 0.3138 0.3413 0.0116 0.0134 -0.0440 363 PHE A CA 2855 C C . PHE A 347 ? 0.2848 0.3049 0.3277 0.0118 0.0095 -0.0427 363 PHE A C 2856 O O . PHE A 347 ? 0.2907 0.3102 0.3333 0.0103 0.0115 -0.0417 363 PHE A O 2857 C CB . PHE A 347 ? 0.2995 0.3180 0.3376 0.0119 0.0151 -0.0389 363 PHE A CB 2858 C CG . PHE A 347 ? 0.3061 0.3234 0.3473 0.0118 0.0188 -0.0396 363 PHE A CG 2859 C CD1 . PHE A 347 ? 0.3143 0.3304 0.3647 0.0106 0.0224 -0.0434 363 PHE A CD1 2860 C CD2 . PHE A 347 ? 0.3076 0.3249 0.3427 0.0128 0.0187 -0.0364 363 PHE A CD2 2861 C CE1 . PHE A 347 ? 0.3216 0.3363 0.3750 0.0104 0.0259 -0.0439 363 PHE A CE1 2862 C CE2 . PHE A 347 ? 0.3137 0.3297 0.3517 0.0128 0.0220 -0.0370 363 PHE A CE2 2863 C CZ . PHE A 347 ? 0.3184 0.3329 0.3656 0.0116 0.0255 -0.0407 363 PHE A CZ 2864 N N . THR A 348 ? 0.2757 0.2970 0.3154 0.0138 0.0041 -0.0428 364 THR A N 2865 C CA . THR A 348 ? 0.2754 0.2972 0.3116 0.0142 0.0000 -0.0415 364 THR A CA 2866 C C . THR A 348 ? 0.2784 0.3003 0.3228 0.0136 -0.0007 -0.0458 364 THR A C 2867 O O . THR A 348 ? 0.2826 0.3042 0.3253 0.0126 -0.0007 -0.0443 364 THR A O 2868 C CB . THR A 348 ? 0.2827 0.3055 0.3143 0.0166 -0.0056 -0.0411 364 THR A CB 2869 O OG1 . THR A 348 ? 0.2890 0.3119 0.3129 0.0170 -0.0046 -0.0370 364 THR A OG1 2870 C CG2 . THR A 348 ? 0.2858 0.3084 0.3135 0.0170 -0.0098 -0.0395 364 THR A CG2 2871 N N . VAL A 349 ? 0.2671 0.2896 0.3207 0.0140 -0.0011 -0.0513 365 VAL A N 2872 C CA . VAL A 349 ? 0.2632 0.2861 0.3259 0.0134 -0.0016 -0.0561 365 VAL A CA 2873 C C . VAL A 349 ? 0.2620 0.2840 0.3259 0.0108 0.0037 -0.0550 365 VAL A C 2874 O O . VAL A 349 ? 0.2591 0.2813 0.3248 0.0103 0.0027 -0.0558 365 VAL A O 2875 C CB . VAL A 349 ? 0.2600 0.2837 0.3333 0.0141 -0.0021 -0.0625 365 VAL A CB 2876 C CG1 . VAL A 349 ? 0.2592 0.2835 0.3430 0.0129 -0.0010 -0.0675 365 VAL A CG1 2877 C CG2 . VAL A 349 ? 0.2559 0.2807 0.3283 0.0171 -0.0088 -0.0644 365 VAL A CG2 2878 N N . HIS A 350 ? 0.2615 0.2823 0.3240 0.0094 0.0093 -0.0529 366 HIS A N 2879 C CA . HIS A 350 ? 0.2689 0.2887 0.3313 0.0070 0.0149 -0.0515 366 HIS A CA 2880 C C . HIS A 350 ? 0.2714 0.2910 0.3248 0.0067 0.0143 -0.0466 366 HIS A C 2881 O O . HIS A 350 ? 0.2668 0.2863 0.3213 0.0052 0.0163 -0.0468 366 HIS A O 2882 C CB . HIS A 350 ? 0.2728 0.2909 0.3351 0.0059 0.0208 -0.0502 366 HIS A CB 2883 C CG . HIS A 350 ? 0.2764 0.2944 0.3493 0.0054 0.0231 -0.0555 366 HIS A CG 2884 N ND1 . HIS A 350 ? 0.2775 0.2965 0.3544 0.0071 0.0200 -0.0584 366 HIS A ND1 2885 C CD2 . HIS A 350 ? 0.2709 0.2881 0.3515 0.0034 0.0282 -0.0585 366 HIS A CD2 2886 C CE1 . HIS A 350 ? 0.2779 0.2966 0.3650 0.0061 0.0231 -0.0632 366 HIS A CE1 2887 N NE2 . HIS A 350 ? 0.2759 0.2935 0.3654 0.0038 0.0282 -0.0633 366 HIS A NE2 2888 N N . HIS A 351 ? 0.2698 0.2895 0.3145 0.0080 0.0116 -0.0423 367 HIS A N 2889 C CA . HIS A 351 ? 0.2775 0.2973 0.3142 0.0078 0.0103 -0.0380 367 HIS A CA 2890 C C . HIS A 351 ? 0.2716 0.2921 0.3114 0.0080 0.0064 -0.0402 367 HIS A C 2891 O O . HIS A 351 ? 0.2743 0.2948 0.3132 0.0067 0.0077 -0.0393 367 HIS A O 2892 C CB . HIS A 351 ? 0.2742 0.2943 0.3023 0.0092 0.0076 -0.0338 367 HIS A CB 2893 C CG . HIS A 351 ? 0.2735 0.2938 0.2943 0.0090 0.0060 -0.0298 367 HIS A CG 2894 N ND1 . HIS A 351 ? 0.2780 0.2980 0.2927 0.0081 0.0092 -0.0258 367 HIS A ND1 2895 C CD2 . HIS A 351 ? 0.2733 0.2940 0.2925 0.0096 0.0016 -0.0294 367 HIS A CD2 2896 C CE1 . HIS A 351 ? 0.2789 0.2994 0.2887 0.0081 0.0068 -0.0232 367 HIS A CE1 2897 N NE2 . HIS A 351 ? 0.2762 0.2970 0.2888 0.0089 0.0023 -0.0253 367 HIS A NE2 2898 N N . GLU A 352 ? 0.2719 0.2931 0.3155 0.0096 0.0016 -0.0432 368 GLU A N 2899 C CA . GLU A 352 ? 0.2758 0.2973 0.3224 0.0101 -0.0026 -0.0453 368 GLU A CA 2900 C C . GLU A 352 ? 0.2675 0.2894 0.3229 0.0086 -0.0002 -0.0496 368 GLU A C 2901 O O . GLU A 352 ? 0.2708 0.2929 0.3268 0.0082 -0.0015 -0.0498 368 GLU A O 2902 C CB . GLU A 352 ? 0.2792 0.3011 0.3279 0.0125 -0.0084 -0.0478 368 GLU A CB 2903 C CG . GLU A 352 ? 0.2896 0.3112 0.3297 0.0140 -0.0109 -0.0440 368 GLU A CG 2904 C CD . GLU A 352 ? 0.2925 0.3136 0.3232 0.0136 -0.0113 -0.0383 368 GLU A CD 2905 O OE1 . GLU A 352 ? 0.2949 0.3157 0.3255 0.0130 -0.0125 -0.0377 368 GLU A OE1 2906 O OE2 . GLU A 352 ? 0.3052 0.3264 0.3289 0.0139 -0.0103 -0.0346 368 GLU A OE2 2907 N N . LEU A 353 ? 0.2628 0.2848 0.3252 0.0079 0.0034 -0.0531 369 LEU A N 2908 C CA . LEU A 353 ? 0.2626 0.2851 0.3340 0.0062 0.0064 -0.0575 369 LEU A CA 2909 C C . LEU A 353 ? 0.2601 0.2820 0.3276 0.0041 0.0116 -0.0547 369 LEU A C 2910 O O . LEU A 353 ? 0.2587 0.2811 0.3317 0.0027 0.0134 -0.0575 369 LEU A O 2911 C CB . LEU A 353 ? 0.2635 0.2862 0.3438 0.0058 0.0093 -0.0621 369 LEU A CB 2912 C CG . LEU A 353 ? 0.2654 0.2892 0.3528 0.0079 0.0043 -0.0670 369 LEU A CG 2913 C CD1 . LEU A 353 ? 0.2670 0.2909 0.3623 0.0074 0.0078 -0.0709 369 LEU A CD1 2914 C CD2 . LEU A 353 ? 0.2620 0.2869 0.3564 0.0085 0.0003 -0.0714 369 LEU A CD2 2915 N N . GLY A 354 ? 0.2552 0.2762 0.3134 0.0038 0.0138 -0.0493 370 GLY A N 2916 C CA . GLY A 354 ? 0.2476 0.2681 0.3003 0.0022 0.0177 -0.0460 370 GLY A CA 2917 C C . GLY A 354 ? 0.2490 0.2702 0.2996 0.0022 0.0146 -0.0453 370 GLY A C 2918 O O . GLY A 354 ? 0.2459 0.2675 0.2975 0.0008 0.0174 -0.0459 370 GLY A O 2919 N N . HIS A 355 ? 0.2512 0.2728 0.2989 0.0039 0.0088 -0.0440 371 HIS A N 2920 C CA . HIS A 355 ? 0.2517 0.2738 0.2987 0.0041 0.0051 -0.0437 371 HIS A CA 2921 C C . HIS A 355 ? 0.2545 0.2774 0.3115 0.0037 0.0044 -0.0493 371 HIS A C 2922 O O . HIS A 355 ? 0.2513 0.2747 0.3096 0.0026 0.0054 -0.0500 371 HIS A O 2923 C CB . HIS A 355 ? 0.2549 0.2766 0.2977 0.0061 -0.0007 -0.0416 371 HIS A CB 2924 C CG . HIS A 355 ? 0.2670 0.2883 0.2999 0.0064 -0.0005 -0.0360 371 HIS A CG 2925 N ND1 . HIS A 355 ? 0.2640 0.2855 0.2908 0.0053 0.0019 -0.0323 371 HIS A ND1 2926 C CD2 . HIS A 355 ? 0.2642 0.2852 0.2925 0.0078 -0.0026 -0.0338 371 HIS A CD2 2927 C CE1 . HIS A 355 ? 0.2680 0.2893 0.2873 0.0060 0.0013 -0.0281 371 HIS A CE1 2928 N NE2 . HIS A 355 ? 0.2778 0.2989 0.2978 0.0075 -0.0012 -0.0289 371 HIS A NE2 2929 N N . ILE A 356 ? 0.2530 0.2760 0.3174 0.0046 0.0027 -0.0536 372 ILE A N 2930 C CA . ILE A 356 ? 0.2534 0.2774 0.3284 0.0044 0.0016 -0.0596 372 ILE A CA 2931 C C . ILE A 356 ? 0.2510 0.2756 0.3304 0.0020 0.0079 -0.0618 372 ILE A C 2932 O O . ILE A 356 ? 0.2516 0.2771 0.3357 0.0013 0.0076 -0.0645 372 ILE A O 2933 C CB . ILE A 356 ? 0.2552 0.2796 0.3379 0.0059 -0.0007 -0.0642 372 ILE A CB 2934 C CG1 . ILE A 356 ? 0.2554 0.2792 0.3335 0.0085 -0.0073 -0.0623 372 ILE A CG1 2935 C CG2 . ILE A 356 ? 0.2540 0.2797 0.3487 0.0056 -0.0013 -0.0709 372 ILE A CG2 2936 C CD1 . ILE A 356 ? 0.2613 0.2848 0.3394 0.0098 -0.0132 -0.0626 372 ILE A CD1 2937 N N . GLN A 357 ? 0.2508 0.2748 0.3284 0.0008 0.0135 -0.0605 373 GLN A N 2938 C CA . GLN A 357 ? 0.2583 0.2824 0.3387 -0.0015 0.0200 -0.0620 373 GLN A CA 2939 C C . GLN A 357 ? 0.2595 0.2839 0.3342 -0.0024 0.0210 -0.0594 373 GLN A C 2940 O O . GLN A 357 ? 0.2668 0.2921 0.3464 -0.0038 0.0235 -0.0625 373 GLN A O 2941 C CB . GLN A 357 ? 0.2604 0.2831 0.3384 -0.0025 0.0258 -0.0601 373 GLN A CB 2942 C CG . GLN A 357 ? 0.2663 0.2886 0.3471 -0.0049 0.0330 -0.0617 373 GLN A CG 2943 C CD . GLN A 357 ? 0.2705 0.2940 0.3642 -0.0059 0.0345 -0.0686 373 GLN A CD 2944 O OE1 . GLN A 357 ? 0.2678 0.2917 0.3649 -0.0078 0.0389 -0.0708 373 GLN A OE1 2945 N NE2 . GLN A 357 ? 0.2624 0.2866 0.3634 -0.0046 0.0309 -0.0723 373 GLN A NE2 2946 N N . TYR A 358 ? 0.2548 0.2786 0.3195 -0.0017 0.0191 -0.0539 374 TYR A N 2947 C CA . TYR A 358 ? 0.2503 0.2745 0.3094 -0.0023 0.0195 -0.0514 374 TYR A CA 2948 C C . TYR A 358 ? 0.2475 0.2730 0.3126 -0.0020 0.0153 -0.0548 374 TYR A C 2949 O O . TYR A 358 ? 0.2374 0.2638 0.3041 -0.0033 0.0174 -0.0563 374 TYR A O 2950 C CB . TYR A 358 ? 0.2520 0.2756 0.3006 -0.0013 0.0174 -0.0454 374 TYR A CB 2951 C CG . TYR A 358 ? 0.2496 0.2732 0.2902 -0.0023 0.0206 -0.0416 374 TYR A CG 2952 C CD1 . TYR A 358 ? 0.2528 0.2773 0.2950 -0.0037 0.0234 -0.0434 374 TYR A CD1 2953 C CD2 . TYR A 358 ? 0.2487 0.2717 0.2803 -0.0016 0.0205 -0.0364 374 TYR A CD2 2954 C CE1 . TYR A 358 ? 0.2526 0.2773 0.2872 -0.0042 0.0259 -0.0401 374 TYR A CE1 2955 C CE2 . TYR A 358 ? 0.2484 0.2715 0.2727 -0.0022 0.0229 -0.0332 374 TYR A CE2 2956 C CZ . TYR A 358 ? 0.2552 0.2792 0.2809 -0.0034 0.0255 -0.0350 374 TYR A CZ 2957 O OH . TYR A 358 ? 0.2465 0.2708 0.2646 -0.0037 0.0275 -0.0319 374 TYR A OH 2958 N N . PHE A 359 ? 0.2435 0.2689 0.3118 -0.0003 0.0095 -0.0562 375 PHE A N 2959 C CA . PHE A 359 ? 0.2489 0.2750 0.3234 0.0002 0.0050 -0.0596 375 PHE A CA 2960 C C . PHE A 359 ? 0.2537 0.2812 0.3383 -0.0010 0.0080 -0.0656 375 PHE A C 2961 O O . PHE A 359 ? 0.2517 0.2803 0.3391 -0.0017 0.0077 -0.0674 375 PHE A O 2962 C CB . PHE A 359 ? 0.2483 0.2738 0.3256 0.0025 -0.0013 -0.0608 375 PHE A CB 2963 C CG . PHE A 359 ? 0.2518 0.2759 0.3198 0.0039 -0.0047 -0.0554 375 PHE A CG 2964 C CD1 . PHE A 359 ? 0.2494 0.2732 0.3084 0.0033 -0.0038 -0.0502 375 PHE A CD1 2965 C CD2 . PHE A 359 ? 0.2526 0.2760 0.3211 0.0059 -0.0090 -0.0558 375 PHE A CD2 2966 C CE1 . PHE A 359 ? 0.2569 0.2796 0.3079 0.0045 -0.0067 -0.0455 375 PHE A CE1 2967 C CE2 . PHE A 359 ? 0.2559 0.2781 0.3157 0.0072 -0.0119 -0.0509 375 PHE A CE2 2968 C CZ . PHE A 359 ? 0.2540 0.2758 0.3052 0.0064 -0.0106 -0.0458 375 PHE A CZ 2969 N N . LEU A 360 ? 0.2530 0.2807 0.3435 -0.0015 0.0110 -0.0687 376 LEU A N 2970 C CA . LEU A 360 ? 0.2569 0.2860 0.3580 -0.0029 0.0142 -0.0748 376 LEU A CA 2971 C C . LEU A 360 ? 0.2618 0.2914 0.3604 -0.0052 0.0208 -0.0742 376 LEU A C 2972 O O . LEU A 360 ? 0.2690 0.3001 0.3741 -0.0063 0.0220 -0.0784 376 LEU A O 2973 C CB . LEU A 360 ? 0.2578 0.2869 0.3656 -0.0029 0.0161 -0.0781 376 LEU A CB 2974 C CG . LEU A 360 ? 0.2562 0.2852 0.3679 -0.0004 0.0096 -0.0801 376 LEU A CG 2975 C CD1 . LEU A 360 ? 0.2611 0.2900 0.3781 -0.0005 0.0121 -0.0827 376 LEU A CD1 2976 C CD2 . LEU A 360 ? 0.2567 0.2870 0.3775 0.0006 0.0047 -0.0853 376 LEU A CD2 2977 N N . GLN A 361 ? 0.2605 0.2889 0.3497 -0.0059 0.0246 -0.0691 377 GLN A N 2978 C CA . GLN A 361 ? 0.2648 0.2932 0.3498 -0.0079 0.0308 -0.0678 377 GLN A CA 2979 C C . GLN A 361 ? 0.2631 0.2927 0.3450 -0.0081 0.0294 -0.0672 377 GLN A C 2980 O O . GLN A 361 ? 0.2651 0.2957 0.3482 -0.0097 0.0338 -0.0691 377 GLN A O 2981 C CB . GLN A 361 ? 0.2720 0.2984 0.3469 -0.0081 0.0344 -0.0622 377 GLN A CB 2982 C CG . GLN A 361 ? 0.2875 0.3125 0.3654 -0.0086 0.0385 -0.0630 377 GLN A CG 2983 C CD . GLN A 361 ? 0.2965 0.3217 0.3804 -0.0109 0.0453 -0.0668 377 GLN A CD 2984 O OE1 . GLN A 361 ? 0.3077 0.3331 0.3884 -0.0122 0.0491 -0.0663 377 GLN A OE1 2985 N NE2 . GLN A 361 ? 0.2961 0.3210 0.3888 -0.0114 0.0471 -0.0707 377 GLN A NE2 2986 N N . TYR A 362 ? 0.2569 0.2864 0.3348 -0.0065 0.0235 -0.0645 378 TYR A N 2987 C CA . TYR A 362 ? 0.2583 0.2889 0.3335 -0.0067 0.0218 -0.0638 378 TYR A CA 2988 C C . TYR A 362 ? 0.2633 0.2949 0.3463 -0.0059 0.0164 -0.0677 378 TYR A C 2989 O O . TYR A 362 ? 0.2652 0.2974 0.3462 -0.0058 0.0141 -0.0668 378 TYR A O 2990 C CB . TYR A 362 ? 0.2473 0.2770 0.3110 -0.0061 0.0205 -0.0574 378 TYR A CB 2991 C CG . TYR A 362 ? 0.2411 0.2696 0.3011 -0.0042 0.0150 -0.0540 378 TYR A CG 2992 C CD1 . TYR A 362 ? 0.2381 0.2664 0.3032 -0.0029 0.0091 -0.0559 378 TYR A CD1 2993 C CD2 . TYR A 362 ? 0.2386 0.2661 0.2895 -0.0037 0.0158 -0.0487 378 TYR A CD2 2994 C CE1 . TYR A 362 ? 0.2367 0.2637 0.2974 -0.0012 0.0044 -0.0524 378 TYR A CE1 2995 C CE2 . TYR A 362 ? 0.2381 0.2646 0.2852 -0.0022 0.0112 -0.0456 378 TYR A CE2 2996 C CZ . TYR A 362 ? 0.2388 0.2650 0.2905 -0.0010 0.0057 -0.0473 378 TYR A CZ 2997 O OH . TYR A 362 ? 0.2382 0.2632 0.2853 0.0004 0.0014 -0.0440 378 TYR A OH 2998 N N . GLN A 363 ? 0.2712 0.3029 0.3634 -0.0052 0.0142 -0.0720 379 GLN A N 2999 C CA . GLN A 363 ? 0.2825 0.3148 0.3818 -0.0040 0.0083 -0.0754 379 GLN A CA 3000 C C . GLN A 363 ? 0.2804 0.3146 0.3859 -0.0052 0.0096 -0.0798 379 GLN A C 3001 O O . GLN A 363 ? 0.2801 0.3146 0.3899 -0.0042 0.0046 -0.0817 379 GLN A O 3002 C CB . GLN A 363 ? 0.2919 0.3238 0.3990 -0.0025 0.0048 -0.0790 379 GLN A CB 3003 C CG . GLN A 363 ? 0.3098 0.3432 0.4271 -0.0037 0.0089 -0.0850 379 GLN A CG 3004 C CD . GLN A 363 ? 0.3261 0.3594 0.4513 -0.0020 0.0049 -0.0887 379 GLN A CD 3005 O OE1 . GLN A 363 ? 0.3390 0.3709 0.4619 0.0002 -0.0012 -0.0870 379 GLN A OE1 3006 N NE2 . GLN A 363 ? 0.3329 0.3675 0.4673 -0.0031 0.0086 -0.0940 379 GLN A NE2 3007 N N . HIS A 364 ? 0.2856 0.3211 0.3912 -0.0072 0.0162 -0.0812 380 HIS A N 3008 C CA . HIS A 364 ? 0.2977 0.3353 0.4080 -0.0085 0.0183 -0.0851 380 HIS A CA 3009 C C . HIS A 364 ? 0.3020 0.3399 0.4040 -0.0087 0.0179 -0.0814 380 HIS A C 3010 O O . HIS A 364 ? 0.2948 0.3345 0.4002 -0.0095 0.0187 -0.0845 380 HIS A O 3011 C CB . HIS A 364 ? 0.3026 0.3414 0.4157 -0.0107 0.0261 -0.0881 380 HIS A CB 3012 C CG . HIS A 364 ? 0.3123 0.3498 0.4144 -0.0117 0.0314 -0.0829 380 HIS A CG 3013 N ND1 . HIS A 364 ? 0.3103 0.3457 0.4066 -0.0111 0.0320 -0.0787 380 HIS A ND1 3014 C CD2 . HIS A 364 ? 0.3193 0.3575 0.4150 -0.0131 0.0362 -0.0813 380 HIS A CD2 3015 C CE1 . HIS A 364 ? 0.3143 0.3489 0.4013 -0.0121 0.0368 -0.0746 380 HIS A CE1 3016 N NE2 . HIS A 364 ? 0.3280 0.3642 0.4141 -0.0132 0.0393 -0.0761 380 HIS A NE2 3017 N N . GLN A 365 ? 0.2910 0.3272 0.3825 -0.0081 0.0170 -0.0752 381 GLN A N 3018 C CA . GLN A 365 ? 0.2930 0.3296 0.3766 -0.0081 0.0164 -0.0715 381 GLN A CA 3019 C C . GLN A 365 ? 0.2921 0.3286 0.3786 -0.0070 0.0098 -0.0720 381 GLN A C 3020 O O . GLN A 365 ? 0.2981 0.3335 0.3896 -0.0056 0.0050 -0.0731 381 GLN A O 3021 C CB . GLN A 365 ? 0.2885 0.3235 0.3609 -0.0077 0.0171 -0.0650 381 GLN A CB 3022 C CG . GLN A 365 ? 0.2956 0.3302 0.3634 -0.0088 0.0238 -0.0636 381 GLN A CG 3023 C CD . GLN A 365 ? 0.3091 0.3451 0.3724 -0.0101 0.0284 -0.0635 381 GLN A CD 3024 O OE1 . GLN A 365 ? 0.3195 0.3568 0.3817 -0.0101 0.0265 -0.0638 381 GLN A OE1 3025 N NE2 . GLN A 365 ? 0.3089 0.3443 0.3691 -0.0112 0.0346 -0.0631 381 GLN A NE2 3026 N N . PRO A 366 ? 0.2972 0.3349 0.3808 -0.0074 0.0095 -0.0712 382 PRO A N 3027 C CA . PRO A 366 ? 0.2959 0.3328 0.3807 -0.0063 0.0033 -0.0704 382 PRO A CA 3028 C C . PRO A 366 ? 0.2947 0.3291 0.3735 -0.0048 -0.0005 -0.0651 382 PRO A C 3029 O O . PRO A 366 ? 0.2879 0.3216 0.3589 -0.0049 0.0019 -0.0610 382 PRO A O 3030 C CB . PRO A 366 ? 0.3031 0.3416 0.3831 -0.0071 0.0047 -0.0692 382 PRO A CB 3031 C CG . PRO A 366 ? 0.3017 0.3420 0.3786 -0.0086 0.0115 -0.0700 382 PRO A CG 3032 C CD . PRO A 366 ? 0.2968 0.3364 0.3767 -0.0089 0.0147 -0.0717 382 PRO A CD 3033 N N . PHE A 367 ? 0.2911 0.3239 0.3733 -0.0035 -0.0065 -0.0652 383 PHE A N 3034 C CA . PHE A 367 ? 0.2970 0.3272 0.3741 -0.0021 -0.0104 -0.0606 383 PHE A CA 3035 C C . PHE A 367 ? 0.2928 0.3227 0.3590 -0.0024 -0.0087 -0.0546 383 PHE A C 3036 O O . PHE A 367 ? 0.2857 0.3145 0.3470 -0.0018 -0.0082 -0.0516 383 PHE A O 3037 C CB . PHE A 367 ? 0.3080 0.3363 0.3884 -0.0008 -0.0168 -0.0606 383 PHE A CB 3038 C CG . PHE A 367 ? 0.3201 0.3456 0.3941 0.0005 -0.0206 -0.0555 383 PHE A CG 3039 C CD1 . PHE A 367 ? 0.3299 0.3537 0.4050 0.0020 -0.0231 -0.0556 383 PHE A CD1 3040 C CD2 . PHE A 367 ? 0.3233 0.3481 0.3902 0.0002 -0.0215 -0.0507 383 PHE A CD2 3041 C CE1 . PHE A 367 ? 0.3392 0.3605 0.4079 0.0032 -0.0264 -0.0509 383 PHE A CE1 3042 C CE2 . PHE A 367 ? 0.3310 0.3533 0.3919 0.0013 -0.0245 -0.0460 383 PHE A CE2 3043 C CZ . PHE A 367 ? 0.3372 0.3576 0.3987 0.0028 -0.0269 -0.0460 383 PHE A CZ 3044 N N . VAL A 368 ? 0.2850 0.3160 0.3478 -0.0032 -0.0078 -0.0533 384 VAL A N 3045 C CA . VAL A 368 ? 0.2884 0.3194 0.3415 -0.0034 -0.0066 -0.0479 384 VAL A CA 3046 C C . VAL A 368 ? 0.2791 0.3109 0.3267 -0.0039 -0.0015 -0.0463 384 VAL A C 3047 O O . VAL A 368 ? 0.2793 0.3105 0.3193 -0.0036 -0.0010 -0.0418 384 VAL A O 3048 C CB . VAL A 368 ? 0.2955 0.3279 0.3464 -0.0041 -0.0068 -0.0471 384 VAL A CB 3049 C CG1 . VAL A 368 ? 0.3060 0.3369 0.3605 -0.0035 -0.0122 -0.0470 384 VAL A CG1 3050 C CG2 . VAL A 368 ? 0.3014 0.3365 0.3553 -0.0053 -0.0029 -0.0513 384 VAL A CG2 3051 N N . TYR A 369 ? 0.2801 0.3128 0.3317 -0.0046 0.0023 -0.0500 385 TYR A N 3052 C CA . TYR A 369 ? 0.2802 0.3131 0.3272 -0.0051 0.0075 -0.0487 385 TYR A CA 3053 C C . TYR A 369 ? 0.2783 0.3096 0.3274 -0.0045 0.0073 -0.0488 385 TYR A C 3054 O O . TYR A 369 ? 0.2845 0.3155 0.3301 -0.0048 0.0113 -0.0475 385 TYR A O 3055 C CB . TYR A 369 ? 0.2820 0.3167 0.3314 -0.0065 0.0126 -0.0523 385 TYR A CB 3056 C CG . TYR A 369 ? 0.2832 0.3198 0.3288 -0.0072 0.0138 -0.0519 385 TYR A CG 3057 C CD1 . TYR A 369 ? 0.2837 0.3203 0.3222 -0.0067 0.0117 -0.0477 385 TYR A CD1 3058 C CD2 . TYR A 369 ? 0.2860 0.3245 0.3350 -0.0083 0.0173 -0.0561 385 TYR A CD2 3059 C CE1 . TYR A 369 ? 0.2874 0.3259 0.3228 -0.0071 0.0127 -0.0478 385 TYR A CE1 3060 C CE2 . TYR A 369 ? 0.2908 0.3311 0.3361 -0.0088 0.0184 -0.0561 385 TYR A CE2 3061 C CZ . TYR A 369 ? 0.2896 0.3300 0.3282 -0.0081 0.0159 -0.0520 385 TYR A CZ 3062 O OH . TYR A 369 ? 0.2947 0.3372 0.3301 -0.0084 0.0168 -0.0524 385 TYR A OH 3063 N N . ARG A 370 ? 0.2724 0.3027 0.3270 -0.0034 0.0027 -0.0504 386 ARG A N 3064 C CA . ARG A 370 ? 0.2733 0.3023 0.3303 -0.0025 0.0019 -0.0510 386 ARG A CA 3065 C C . ARG A 370 ? 0.2695 0.2970 0.3187 -0.0014 0.0000 -0.0458 386 ARG A C 3066 O O . ARG A 370 ? 0.2696 0.2957 0.3194 -0.0001 -0.0047 -0.0449 386 ARG A O 3067 C CB . ARG A 370 ? 0.2724 0.3011 0.3389 -0.0016 -0.0022 -0.0555 386 ARG A CB 3068 C CG . ARG A 370 ? 0.2821 0.3125 0.3575 -0.0027 0.0002 -0.0614 386 ARG A CG 3069 C CD . ARG A 370 ? 0.2813 0.3115 0.3664 -0.0016 -0.0046 -0.0659 386 ARG A CD 3070 N NE . ARG A 370 ? 0.2787 0.3080 0.3677 -0.0004 -0.0062 -0.0676 386 ARG A NE 3071 C CZ . ARG A 370 ? 0.2852 0.3144 0.3832 0.0007 -0.0101 -0.0721 386 ARG A CZ 3072 N NH1 . ARG A 370 ? 0.2780 0.3077 0.3821 0.0008 -0.0128 -0.0754 386 ARG A NH1 3073 N NH2 . ARG A 370 ? 0.2728 0.3013 0.3737 0.0018 -0.0116 -0.0736 386 ARG A NH2 3074 N N . THR A 371 ? 0.2663 0.2941 0.3082 -0.0020 0.0038 -0.0424 387 THR A N 3075 C CA . THR A 371 ? 0.2654 0.2921 0.2998 -0.0011 0.0029 -0.0375 387 THR A CA 3076 C C . THR A 371 ? 0.2624 0.2894 0.2914 -0.0018 0.0083 -0.0356 387 THR A C 3077 O O . THR A 371 ? 0.2573 0.2852 0.2878 -0.0030 0.0123 -0.0376 387 THR A O 3078 C CB . THR A 371 ? 0.2665 0.2929 0.2958 -0.0006 -0.0007 -0.0339 387 THR A CB 3079 O OG1 . THR A 371 ? 0.2684 0.2938 0.2919 0.0002 -0.0020 -0.0299 387 THR A OG1 3080 C CG2 . THR A 371 ? 0.2682 0.2962 0.2932 -0.0017 0.0017 -0.0324 387 THR A CG2 3081 N N . GLY A 372 ? 0.2591 0.2853 0.2817 -0.0011 0.0085 -0.0316 388 GLY A N 3082 C CA . GLY A 372 ? 0.2566 0.2827 0.2740 -0.0016 0.0134 -0.0295 388 GLY A CA 3083 C C . GLY A 372 ? 0.2603 0.2875 0.2721 -0.0023 0.0156 -0.0277 388 GLY A C 3084 O O . GLY A 372 ? 0.2577 0.2859 0.2681 -0.0022 0.0129 -0.0267 388 GLY A O 3085 N N . ALA A 373 ? 0.2599 0.2868 0.2687 -0.0028 0.0206 -0.0272 389 ALA A N 3086 C CA . ALA A 373 ? 0.2620 0.2899 0.2645 -0.0032 0.0228 -0.0252 389 ALA A CA 3087 C C . ALA A 373 ? 0.2566 0.2851 0.2525 -0.0022 0.0199 -0.0210 389 ALA A C 3088 O O . ALA A 373 ? 0.2582 0.2881 0.2514 -0.0023 0.0188 -0.0202 389 ALA A O 3089 C CB . ALA A 373 ? 0.2653 0.2921 0.2645 -0.0036 0.0284 -0.0246 389 ALA A CB 3090 N N . ASN A 374 ? 0.2551 0.2825 0.2487 -0.0013 0.0188 -0.0185 390 ASN A N 3091 C CA . ASN A 374 ? 0.2538 0.2817 0.2434 -0.0004 0.0152 -0.0152 390 ASN A CA 3092 C C . ASN A 374 ? 0.2528 0.2794 0.2443 0.0002 0.0132 -0.0149 390 ASN A C 3093 O O . ASN A 374 ? 0.2604 0.2859 0.2558 0.0001 0.0150 -0.0170 390 ASN A O 3094 C CB . ASN A 374 ? 0.2524 0.2810 0.2341 0.0000 0.0167 -0.0116 390 ASN A CB 3095 C CG . ASN A 374 ? 0.2566 0.2839 0.2344 0.0007 0.0192 -0.0094 390 ASN A CG 3096 O OD1 . ASN A 374 ? 0.2671 0.2933 0.2465 0.0012 0.0183 -0.0092 390 ASN A OD1 3097 N ND2 . ASN A 374 ? 0.2555 0.2828 0.2278 0.0009 0.0222 -0.0077 390 ASN A ND2 3098 N N . PRO A 375 ? 0.2556 0.2824 0.2449 0.0009 0.0096 -0.0127 391 PRO A N 3099 C CA . PRO A 375 ? 0.2476 0.2732 0.2390 0.0018 0.0075 -0.0129 391 PRO A CA 3100 C C . PRO A 375 ? 0.2518 0.2766 0.2417 0.0023 0.0103 -0.0122 391 PRO A C 3101 O O . PRO A 375 ? 0.2586 0.2825 0.2523 0.0028 0.0095 -0.0140 391 PRO A O 3102 C CB . PRO A 375 ? 0.2448 0.2708 0.2324 0.0023 0.0039 -0.0099 391 PRO A CB 3103 C CG . PRO A 375 ? 0.2504 0.2774 0.2379 0.0016 0.0029 -0.0099 391 PRO A CG 3104 C CD . PRO A 375 ? 0.2471 0.2751 0.2333 0.0009 0.0069 -0.0105 391 PRO A CD 3105 N N . GLY A 376 ? 0.2443 0.2693 0.2288 0.0023 0.0133 -0.0098 392 GLY A N 3106 C CA . GLY A 376 ? 0.2448 0.2686 0.2279 0.0028 0.0162 -0.0090 392 GLY A CA 3107 C C . GLY A 376 ? 0.2506 0.2732 0.2391 0.0021 0.0195 -0.0122 392 GLY A C 3108 O O . GLY A 376 ? 0.2425 0.2639 0.2330 0.0025 0.0206 -0.0129 392 GLY A O 3109 N N . PHE A 377 ? 0.2554 0.2782 0.2463 0.0010 0.0212 -0.0144 393 PHE A N 3110 C CA . PHE A 377 ? 0.2620 0.2838 0.2588 0.0001 0.0244 -0.0179 393 PHE A CA 3111 C C . PHE A 377 ? 0.2665 0.2880 0.2708 0.0004 0.0220 -0.0212 393 PHE A C 3112 O O . PHE A 377 ? 0.2721 0.2926 0.2804 0.0002 0.0244 -0.0230 393 PHE A O 3113 C CB . PHE A 377 ? 0.2644 0.2871 0.2631 -0.0010 0.0261 -0.0200 393 PHE A CB 3114 C CG . PHE A 377 ? 0.2655 0.2879 0.2579 -0.0013 0.0300 -0.0178 393 PHE A CG 3115 C CD1 . PHE A 377 ? 0.2683 0.2912 0.2529 -0.0005 0.0291 -0.0139 393 PHE A CD1 3116 C CD2 . PHE A 377 ? 0.2706 0.2921 0.2646 -0.0025 0.0347 -0.0199 393 PHE A CD2 3117 C CE1 . PHE A 377 ? 0.2700 0.2927 0.2485 -0.0005 0.0323 -0.0120 393 PHE A CE1 3118 C CE2 . PHE A 377 ? 0.2651 0.2862 0.2526 -0.0026 0.0383 -0.0177 393 PHE A CE2 3119 C CZ . PHE A 377 ? 0.2706 0.2922 0.2502 -0.0015 0.0368 -0.0139 393 PHE A CZ 3120 N N . HIS A 378 ? 0.2642 0.2867 0.2706 0.0009 0.0173 -0.0220 394 HIS A N 3121 C CA . HIS A 378 ? 0.2662 0.2885 0.2795 0.0014 0.0143 -0.0253 394 HIS A CA 3122 C C . HIS A 378 ? 0.2725 0.2939 0.2848 0.0025 0.0138 -0.0244 394 HIS A C 3123 O O . HIS A 378 ? 0.2762 0.2972 0.2947 0.0027 0.0139 -0.0276 394 HIS A O 3124 C CB . HIS A 378 ? 0.2535 0.2763 0.2677 0.0020 0.0090 -0.0255 394 HIS A CB 3125 C CG . HIS A 378 ? 0.2501 0.2732 0.2729 0.0018 0.0073 -0.0303 394 HIS A CG 3126 N ND1 . HIS A 378 ? 0.2483 0.2709 0.2775 0.0024 0.0061 -0.0337 394 HIS A ND1 3127 C CD2 . HIS A 378 ? 0.2493 0.2730 0.2757 0.0011 0.0065 -0.0325 394 HIS A CD2 3128 C CE1 . HIS A 378 ? 0.2518 0.2748 0.2881 0.0022 0.0046 -0.0377 394 HIS A CE1 3129 N NE2 . HIS A 378 ? 0.2456 0.2692 0.2805 0.0013 0.0048 -0.0371 394 HIS A NE2 3130 N N . GLU A 379 ? 0.2755 0.2970 0.2807 0.0033 0.0132 -0.0202 395 GLU A N 3131 C CA . GLU A 379 ? 0.2712 0.2922 0.2750 0.0044 0.0126 -0.0193 395 GLU A CA 3132 C C . GLU A 379 ? 0.2709 0.2908 0.2756 0.0040 0.0175 -0.0196 395 GLU A C 3133 O O . GLU A 379 ? 0.2805 0.2998 0.2873 0.0047 0.0175 -0.0206 395 GLU A O 3134 C CB . GLU A 379 ? 0.2693 0.2909 0.2653 0.0053 0.0106 -0.0149 395 GLU A CB 3135 C CG . GLU A 379 ? 0.2702 0.2926 0.2650 0.0055 0.0062 -0.0142 395 GLU A CG 3136 C CD . GLU A 379 ? 0.2671 0.2890 0.2668 0.0064 0.0023 -0.0170 395 GLU A CD 3137 O OE1 . GLU A 379 ? 0.2775 0.2990 0.2796 0.0072 0.0023 -0.0186 395 GLU A OE1 3138 O OE2 . GLU A 379 ? 0.2674 0.2893 0.2685 0.0064 -0.0008 -0.0176 395 GLU A OE2 3139 N N . ALA A 380 ? 0.2639 0.2833 0.2669 0.0029 0.0216 -0.0188 396 ALA A N 3140 C CA . ALA A 380 ? 0.2658 0.2835 0.2684 0.0025 0.0266 -0.0184 396 ALA A CA 3141 C C . ALA A 380 ? 0.2662 0.2829 0.2773 0.0016 0.0291 -0.0227 396 ALA A C 3142 O O . ALA A 380 ? 0.2670 0.2822 0.2794 0.0017 0.0318 -0.0228 396 ALA A O 3143 C CB . ALA A 380 ? 0.2621 0.2792 0.2589 0.0018 0.0301 -0.0157 396 ALA A CB 3144 N N . VAL A 381 ? 0.2685 0.2860 0.2856 0.0008 0.0282 -0.0264 397 VAL A N 3145 C CA . VAL A 381 ? 0.2714 0.2882 0.2970 -0.0003 0.0315 -0.0308 397 VAL A CA 3146 C C . VAL A 381 ? 0.2689 0.2850 0.2997 0.0003 0.0314 -0.0329 397 VAL A C 3147 O O . VAL A 381 ? 0.2728 0.2872 0.3054 -0.0004 0.0361 -0.0333 397 VAL A O 3148 C CB . VAL A 381 ? 0.2707 0.2891 0.3032 -0.0008 0.0293 -0.0350 397 VAL A CB 3149 C CG1 . VAL A 381 ? 0.2734 0.2914 0.3151 -0.0021 0.0330 -0.0398 397 VAL A CG1 3150 C CG2 . VAL A 381 ? 0.2789 0.2981 0.3071 -0.0015 0.0295 -0.0334 397 VAL A CG2 3151 N N . GLY A 382 ? 0.2661 0.2834 0.2989 0.0017 0.0262 -0.0341 398 GLY A N 3152 C CA . GLY A 382 ? 0.2770 0.2941 0.3151 0.0026 0.0253 -0.0367 398 GLY A CA 3153 C C . GLY A 382 ? 0.2841 0.2999 0.3174 0.0032 0.0273 -0.0336 398 GLY A C 3154 O O . GLY A 382 ? 0.2858 0.3008 0.3241 0.0032 0.0291 -0.0358 398 GLY A O 3155 N N . ASP A 383 ? 0.2888 0.3045 0.3129 0.0037 0.0269 -0.0287 399 ASP A N 3156 C CA . ASP A 383 ? 0.2938 0.3084 0.3129 0.0044 0.0287 -0.0254 399 ASP A CA 3157 C C . ASP A 383 ? 0.2999 0.3120 0.3197 0.0031 0.0349 -0.0249 399 ASP A C 3158 O O . ASP A 383 ? 0.2941 0.3048 0.3141 0.0036 0.0368 -0.0242 399 ASP A O 3159 C CB . ASP A 383 ? 0.2966 0.3119 0.3062 0.0051 0.0268 -0.0205 399 ASP A CB 3160 C CG . ASP A 383 ? 0.3026 0.3197 0.3103 0.0066 0.0213 -0.0202 399 ASP A CG 3161 O OD1 . ASP A 383 ? 0.3048 0.3228 0.3179 0.0071 0.0181 -0.0236 399 ASP A OD1 3162 O OD2 . ASP A 383 ? 0.3051 0.3227 0.3058 0.0075 0.0201 -0.0165 399 ASP A OD2 3163 N N . VAL A 384 ? 0.3063 0.3177 0.3265 0.0016 0.0381 -0.0252 400 VAL A N 3164 C CA . VAL A 384 ? 0.3160 0.3247 0.3369 0.0003 0.0444 -0.0248 400 VAL A CA 3165 C C . VAL A 384 ? 0.3223 0.3301 0.3528 -0.0002 0.0464 -0.0291 400 VAL A C 3166 O O . VAL A 384 ? 0.3263 0.3316 0.3571 -0.0004 0.0502 -0.0281 400 VAL A O 3167 C CB . VAL A 384 ? 0.3194 0.3278 0.3391 -0.0011 0.0474 -0.0248 400 VAL A CB 3168 C CG1 . VAL A 384 ? 0.3201 0.3253 0.3401 -0.0025 0.0542 -0.0244 400 VAL A CG1 3169 C CG2 . VAL A 384 ? 0.3177 0.3271 0.3280 -0.0005 0.0455 -0.0207 400 VAL A CG2 3170 N N . LEU A 385 ? 0.3218 0.3315 0.3604 -0.0003 0.0437 -0.0339 401 LEU A N 3171 C CA . LEU A 385 ? 0.3283 0.3376 0.3770 -0.0007 0.0451 -0.0386 401 LEU A CA 3172 C C . LEU A 385 ? 0.3276 0.3370 0.3763 0.0009 0.0425 -0.0383 401 LEU A C 3173 O O . LEU A 385 ? 0.3319 0.3396 0.3851 0.0005 0.0457 -0.0397 401 LEU A O 3174 C CB . LEU A 385 ? 0.3257 0.3373 0.3835 -0.0011 0.0424 -0.0442 401 LEU A CB 3175 C CG . LEU A 385 ? 0.3422 0.3547 0.4025 -0.0025 0.0433 -0.0462 401 LEU A CG 3176 C CD1 . LEU A 385 ? 0.3283 0.3418 0.4011 -0.0033 0.0439 -0.0528 401 LEU A CD1 3177 C CD2 . LEU A 385 ? 0.3319 0.3426 0.3867 -0.0041 0.0489 -0.0431 401 LEU A CD2 3178 N N . SER A 386 ? 0.3350 0.3462 0.3786 0.0027 0.0370 -0.0366 402 SER A N 3179 C CA . SER A 386 ? 0.3345 0.3463 0.3771 0.0044 0.0343 -0.0362 402 SER A CA 3180 C C . SER A 386 ? 0.3272 0.3365 0.3653 0.0044 0.0382 -0.0326 402 SER A C 3181 O O . SER A 386 ? 0.3150 0.3240 0.3559 0.0053 0.0380 -0.0337 402 SER A O 3182 C CB . SER A 386 ? 0.3540 0.3679 0.3902 0.0062 0.0284 -0.0341 402 SER A CB 3183 O OG . SER A 386 ? 0.3953 0.4112 0.4367 0.0070 0.0237 -0.0380 402 SER A OG 3184 N N . LEU A 387 ? 0.3110 0.3186 0.3422 0.0037 0.0415 -0.0284 403 LEU A N 3185 C CA . LEU A 387 ? 0.3107 0.3155 0.3378 0.0037 0.0454 -0.0249 403 LEU A CA 3186 C C . LEU A 387 ? 0.3172 0.3194 0.3522 0.0025 0.0503 -0.0277 403 LEU A C 3187 O O . LEU A 387 ? 0.3199 0.3205 0.3556 0.0031 0.0516 -0.0271 403 LEU A O 3188 C CB . LEU A 387 ? 0.3023 0.3057 0.3205 0.0033 0.0478 -0.0201 403 LEU A CB 3189 C CG . LEU A 387 ? 0.3004 0.3055 0.3095 0.0048 0.0441 -0.0161 403 LEU A CG 3190 C CD1 . LEU A 387 ? 0.2963 0.3009 0.2983 0.0042 0.0456 -0.0127 403 LEU A CD1 3191 C CD2 . LEU A 387 ? 0.3000 0.3042 0.3056 0.0063 0.0440 -0.0135 403 LEU A CD2 3192 N N . SER A 388 ? 0.3166 0.3185 0.3581 0.0007 0.0530 -0.0310 404 SER A N 3193 C CA . SER A 388 ? 0.3194 0.3191 0.3700 -0.0006 0.0576 -0.0344 404 SER A CA 3194 C C . SER A 388 ? 0.3192 0.3207 0.3784 0.0003 0.0544 -0.0392 404 SER A C 3195 O O . SER A 388 ? 0.3202 0.3198 0.3837 0.0002 0.0569 -0.0402 404 SER A O 3196 C CB . SER A 388 ? 0.3262 0.3257 0.3821 -0.0028 0.0610 -0.0374 404 SER A CB 3197 O OG . SER A 388 ? 0.3304 0.3267 0.3804 -0.0041 0.0666 -0.0336 404 SER A OG 3198 N N . VAL A 389 ? 0.3135 0.3185 0.3753 0.0012 0.0489 -0.0422 405 VAL A N 3199 C CA . VAL A 389 ? 0.3123 0.3195 0.3818 0.0025 0.0450 -0.0470 405 VAL A CA 3200 C C . VAL A 389 ? 0.3142 0.3209 0.3804 0.0041 0.0440 -0.0450 405 VAL A C 3201 O O . VAL A 389 ? 0.3203 0.3270 0.3939 0.0045 0.0441 -0.0487 405 VAL A O 3202 C CB . VAL A 389 ? 0.3080 0.3187 0.3779 0.0038 0.0384 -0.0493 405 VAL A CB 3203 C CG1 . VAL A 389 ? 0.3016 0.3144 0.3782 0.0056 0.0341 -0.0540 405 VAL A CG1 3204 C CG2 . VAL A 389 ? 0.3028 0.3142 0.3778 0.0023 0.0393 -0.0522 405 VAL A CG2 3205 N N . SER A 390 ? 0.3023 0.3085 0.3579 0.0051 0.0431 -0.0396 406 SER A N 3206 C CA . SER A 390 ? 0.2963 0.3025 0.3481 0.0067 0.0416 -0.0375 406 SER A CA 3207 C C . SER A 390 ? 0.2970 0.2996 0.3502 0.0061 0.0469 -0.0362 406 SER A C 3208 O O . SER A 390 ? 0.2908 0.2934 0.3434 0.0075 0.0459 -0.0358 406 SER A O 3209 C CB . SER A 390 ? 0.2954 0.3027 0.3358 0.0079 0.0387 -0.0324 406 SER A CB 3210 O OG . SER A 390 ? 0.2949 0.2997 0.3289 0.0070 0.0427 -0.0278 406 SER A OG 3211 N N . THR A 391 ? 0.2963 0.2958 0.3511 0.0041 0.0526 -0.0354 407 THR A N 3212 C CA . THR A 391 ? 0.3008 0.2961 0.3565 0.0034 0.0581 -0.0336 407 THR A CA 3213 C C . THR A 391 ? 0.3067 0.3017 0.3732 0.0034 0.0588 -0.0386 407 THR A C 3214 O O . THR A 391 ? 0.3000 0.2971 0.3754 0.0029 0.0575 -0.0440 407 THR A O 3215 C CB . THR A 391 ? 0.3043 0.2958 0.3590 0.0012 0.0644 -0.0317 407 THR A CB 3216 O OG1 . THR A 391 ? 0.3025 0.2948 0.3667 -0.0005 0.0660 -0.0367 407 THR A OG1 3217 C CG2 . THR A 391 ? 0.3075 0.2991 0.3514 0.0014 0.0638 -0.0268 407 THR A CG2 3218 N N . PRO A 392 ? 0.3153 0.3077 0.3813 0.0040 0.0609 -0.0369 408 PRO A N 3219 C CA . PRO A 392 ? 0.3189 0.3102 0.3958 0.0036 0.0629 -0.0414 408 PRO A CA 3220 C C . PRO A 392 ? 0.3221 0.3115 0.4079 0.0010 0.0680 -0.0447 408 PRO A C 3221 O O . PRO A 392 ? 0.3166 0.3077 0.4134 0.0006 0.0674 -0.0507 408 PRO A O 3222 C CB . PRO A 392 ? 0.3253 0.3126 0.3983 0.0041 0.0661 -0.0373 408 PRO A CB 3223 C CG . PRO A 392 ? 0.3240 0.3128 0.3852 0.0060 0.0624 -0.0324 408 PRO A CG 3224 C CD . PRO A 392 ? 0.3179 0.3087 0.3740 0.0054 0.0608 -0.0312 408 PRO A CD 3225 N N . LYS A 393 ? 0.3279 0.3141 0.4089 -0.0006 0.0728 -0.0410 409 LYS A N 3226 C CA . LYS A 393 ? 0.3388 0.3231 0.4273 -0.0033 0.0781 -0.0438 409 LYS A CA 3227 C C . LYS A 393 ? 0.3347 0.3235 0.4319 -0.0037 0.0749 -0.0501 409 LYS A C 3228 O O . LYS A 393 ? 0.3305 0.3193 0.4396 -0.0051 0.0772 -0.0555 409 LYS A O 3229 C CB . LYS A 393 ? 0.3443 0.3254 0.4242 -0.0047 0.0827 -0.0387 409 LYS A CB 3230 C CG . LYS A 393 ? 0.3620 0.3413 0.4490 -0.0076 0.0886 -0.0415 409 LYS A CG 3231 C CD . LYS A 393 ? 0.3714 0.3472 0.4489 -0.0089 0.0932 -0.0363 409 LYS A CD 3232 C CE . LYS A 393 ? 0.3846 0.3543 0.4566 -0.0090 0.0982 -0.0311 409 LYS A CE 3233 N NZ . LYS A 393 ? 0.3898 0.3568 0.4499 -0.0093 0.1011 -0.0253 409 LYS A NZ 3234 N N . HIS A 394 ? 0.3218 0.3142 0.4135 -0.0026 0.0696 -0.0495 410 HIS A N 3235 C CA . HIS A 394 ? 0.3175 0.3139 0.4166 -0.0027 0.0662 -0.0550 410 HIS A CA 3236 C C . HIS A 394 ? 0.3168 0.3164 0.4238 -0.0010 0.0612 -0.0603 410 HIS A C 3237 O O . HIS A 394 ? 0.3172 0.3186 0.4354 -0.0016 0.0608 -0.0666 410 HIS A O 3238 C CB . HIS A 394 ? 0.3152 0.3141 0.4061 -0.0020 0.0621 -0.0527 410 HIS A CB 3239 C CG . HIS A 394 ? 0.3187 0.3211 0.4172 -0.0023 0.0590 -0.0582 410 HIS A CG 3240 N ND1 . HIS A 394 ? 0.3195 0.3214 0.4236 -0.0045 0.0629 -0.0607 410 HIS A ND1 3241 C CD2 . HIS A 394 ? 0.3193 0.3255 0.4209 -0.0004 0.0523 -0.0618 410 HIS A CD2 3242 C CE1 . HIS A 394 ? 0.3219 0.3274 0.4327 -0.0040 0.0586 -0.0657 410 HIS A CE1 3243 N NE2 . HIS A 394 ? 0.3235 0.3315 0.4327 -0.0015 0.0520 -0.0664 410 HIS A NE2 3244 N N . LEU A 395 ? 0.3126 0.3130 0.4138 0.0011 0.0574 -0.0581 411 LEU A N 3245 C CA . LEU A 395 ? 0.3133 0.3170 0.4202 0.0031 0.0521 -0.0628 411 LEU A CA 3246 C C . LEU A 395 ? 0.3203 0.3230 0.4397 0.0023 0.0552 -0.0680 411 LEU A C 3247 O O . LEU A 395 ? 0.3161 0.3219 0.4443 0.0033 0.0515 -0.0741 411 LEU A O 3248 C CB . LEU A 395 ? 0.3084 0.3132 0.4058 0.0056 0.0478 -0.0590 411 LEU A CB 3249 C CG . LEU A 395 ? 0.3062 0.3131 0.3932 0.0067 0.0433 -0.0554 411 LEU A CG 3250 C CD1 . LEU A 395 ? 0.3001 0.3077 0.3776 0.0088 0.0402 -0.0513 411 LEU A CD1 3251 C CD2 . LEU A 395 ? 0.2990 0.3096 0.3900 0.0075 0.0379 -0.0599 411 LEU A CD2 3252 N N . GLU A 396 ? 0.3360 0.3342 0.4562 0.0006 0.0618 -0.0656 412 GLU A N 3253 C CA . GLU A 396 ? 0.3581 0.3546 0.4908 -0.0007 0.0660 -0.0703 412 GLU A CA 3254 C C . GLU A 396 ? 0.3512 0.3486 0.4947 -0.0028 0.0684 -0.0758 412 GLU A C 3255 O O . GLU A 396 ? 0.3468 0.3459 0.5028 -0.0029 0.0679 -0.0824 412 GLU A O 3256 C CB . GLU A 396 ? 0.3933 0.3841 0.5236 -0.0021 0.0729 -0.0658 412 GLU A CB 3257 C CG . GLU A 396 ? 0.4453 0.4350 0.5674 0.0000 0.0711 -0.0614 412 GLU A CG 3258 C CD . GLU A 396 ? 0.4940 0.4780 0.6172 -0.0012 0.0776 -0.0586 412 GLU A CD 3259 O OE1 . GLU A 396 ? 0.4979 0.4813 0.6309 -0.0012 0.0786 -0.0627 412 GLU A OE1 3260 O OE2 . GLU A 396 ? 0.5448 0.5247 0.6592 -0.0020 0.0815 -0.0525 412 GLU A OE2 3261 N N . LYS A 397 ? 0.3549 0.3514 0.4941 -0.0044 0.0708 -0.0733 413 LYS A N 3262 C CA . LYS A 397 ? 0.3570 0.3548 0.5060 -0.0064 0.0730 -0.0784 413 LYS A CA 3263 C C . LYS A 397 ? 0.3542 0.3573 0.5114 -0.0048 0.0663 -0.0853 413 LYS A C 3264 O O . LYS A 397 ? 0.3523 0.3567 0.5225 -0.0060 0.0677 -0.0918 413 LYS A O 3265 C CB . LYS A 397 ? 0.3686 0.3654 0.5101 -0.0079 0.0755 -0.0745 413 LYS A CB 3266 C CG . LYS A 397 ? 0.3841 0.3754 0.5202 -0.0101 0.0834 -0.0692 413 LYS A CG 3267 C CD . LYS A 397 ? 0.3959 0.3867 0.5252 -0.0114 0.0856 -0.0662 413 LYS A CD 3268 C CE . LYS A 397 ? 0.4102 0.3954 0.5302 -0.0127 0.0921 -0.0595 413 LYS A CE 3269 N NZ . LYS A 397 ? 0.4139 0.3987 0.5250 -0.0135 0.0937 -0.0558 413 LYS A NZ 3270 N N . ILE A 398 ? 0.3297 0.3357 0.4792 -0.0021 0.0591 -0.0838 414 ILE A N 3271 C CA . ILE A 398 ? 0.3242 0.3349 0.4796 -0.0002 0.0522 -0.0896 414 ILE A CA 3272 C C . ILE A 398 ? 0.3308 0.3436 0.4908 0.0021 0.0478 -0.0933 414 ILE A C 3273 O O . ILE A 398 ? 0.3386 0.3551 0.5006 0.0044 0.0410 -0.0971 414 ILE A O 3274 C CB . ILE A 398 ? 0.3200 0.3328 0.4656 0.0012 0.0467 -0.0866 414 ILE A CB 3275 C CG1 . ILE A 398 ? 0.3101 0.3220 0.4416 0.0029 0.0444 -0.0797 414 ILE A CG1 3276 C CG2 . ILE A 398 ? 0.3216 0.3333 0.4660 -0.0011 0.0506 -0.0850 414 ILE A CG2 3277 C CD1 . ILE A 398 ? 0.3071 0.3211 0.4295 0.0043 0.0390 -0.0769 414 ILE A CD1 3278 N N . GLY A 399 ? 0.3267 0.3368 0.4881 0.0016 0.0516 -0.0922 415 GLY A N 3279 C CA . GLY A 399 ? 0.3340 0.3459 0.5014 0.0035 0.0484 -0.0964 415 GLY A CA 3280 C C . GLY A 399 ? 0.3404 0.3547 0.4984 0.0068 0.0415 -0.0943 415 GLY A C 3281 O O . GLY A 399 ? 0.3484 0.3652 0.5112 0.0089 0.0375 -0.0988 415 GLY A O 3282 N N . LEU A 400 ? 0.3335 0.3471 0.4780 0.0073 0.0403 -0.0876 416 LEU A N 3283 C CA . LEU A 400 ? 0.3330 0.3487 0.4677 0.0102 0.0342 -0.0851 416 LEU A CA 3284 C C . LEU A 400 ? 0.3378 0.3513 0.4666 0.0107 0.0364 -0.0808 416 LEU A C 3285 O O . LEU A 400 ? 0.3413 0.3569 0.4656 0.0131 0.0320 -0.0805 416 LEU A O 3286 C CB . LEU A 400 ? 0.3224 0.3390 0.4464 0.0107 0.0310 -0.0807 416 LEU A CB 3287 C CG . LEU A 400 ? 0.3242 0.3436 0.4525 0.0112 0.0266 -0.0849 416 LEU A CG 3288 C CD1 . LEU A 400 ? 0.3155 0.3354 0.4324 0.0117 0.0238 -0.0798 416 LEU A CD1 3289 C CD2 . LEU A 400 ? 0.3129 0.3359 0.4471 0.0139 0.0204 -0.0910 416 LEU A CD2 3290 N N . LEU A 401 ? 0.3458 0.3552 0.4747 0.0085 0.0432 -0.0775 417 LEU A N 3291 C CA . LEU A 401 ? 0.3543 0.3610 0.4780 0.0089 0.0456 -0.0733 417 LEU A CA 3292 C C . LEU A 401 ? 0.3737 0.3779 0.5085 0.0076 0.0506 -0.0767 417 LEU A C 3293 O O . LEU A 401 ? 0.3759 0.3769 0.5159 0.0050 0.0565 -0.0768 417 LEU A O 3294 C CB . LEU A 401 ? 0.3450 0.3485 0.4573 0.0078 0.0490 -0.0656 417 LEU A CB 3295 C CG . LEU A 401 ? 0.3432 0.3436 0.4493 0.0082 0.0518 -0.0605 417 LEU A CG 3296 C CD1 . LEU A 401 ? 0.3385 0.3417 0.4393 0.0110 0.0465 -0.0600 417 LEU A CD1 3297 C CD2 . LEU A 401 ? 0.3337 0.3309 0.4294 0.0071 0.0551 -0.0536 417 LEU A CD2 3298 N N . LYS A 402 ? 0.3983 0.4038 0.5368 0.0093 0.0484 -0.0795 418 LYS A N 3299 C CA . LYS A 402 ? 0.4271 0.4307 0.5777 0.0083 0.0523 -0.0839 418 LYS A CA 3300 C C . LYS A 402 ? 0.4355 0.4356 0.5826 0.0086 0.0553 -0.0800 418 LYS A C 3301 O O . LYS A 402 ? 0.4239 0.4252 0.5618 0.0107 0.0519 -0.0766 418 LYS A O 3302 C CB . LYS A 402 ? 0.4366 0.4449 0.5973 0.0101 0.0472 -0.0920 418 LYS A CB 3303 C CG . LYS A 402 ? 0.4530 0.4646 0.6185 0.0100 0.0439 -0.0966 418 LYS A CG 3304 C CD . LYS A 402 ? 0.4685 0.4845 0.6441 0.0120 0.0387 -0.1049 418 LYS A CD 3305 C CE . LYS A 402 ? 0.4583 0.4779 0.6369 0.0126 0.0341 -0.1091 418 LYS A CE 3306 N NZ . LYS A 402 ? 0.4602 0.4782 0.6464 0.0097 0.0388 -0.1106 418 LYS A NZ 3307 N N . ASP A 403 ? 0.4455 0.4413 0.6004 0.0065 0.0617 -0.0806 419 ASP A N 3308 C CA . ASP A 403 ? 0.4564 0.4482 0.6106 0.0066 0.0652 -0.0776 419 ASP A CA 3309 C C . ASP A 403 ? 0.4472 0.4364 0.5868 0.0073 0.0658 -0.0692 419 ASP A C 3310 O O . ASP A 403 ? 0.4431 0.4318 0.5787 0.0090 0.0646 -0.0671 419 ASP A O 3311 C CB . ASP A 403 ? 0.4809 0.4758 0.6413 0.0089 0.0612 -0.0828 419 ASP A CB 3312 C CG . ASP A 403 ? 0.4993 0.4967 0.6751 0.0083 0.0606 -0.0915 419 ASP A CG 3313 O OD1 . ASP A 403 ? 0.5130 0.5070 0.6983 0.0057 0.0665 -0.0934 419 ASP A OD1 3314 O OD2 . ASP A 403 ? 0.5301 0.5328 0.7086 0.0106 0.0544 -0.0966 419 ASP A OD2 3315 N N . TYR A 404 ? 0.4278 0.4154 0.5598 0.0060 0.0677 -0.0647 420 TYR A N 3316 C CA . TYR A 404 ? 0.4213 0.4070 0.5394 0.0067 0.0678 -0.0571 420 TYR A CA 3317 C C . TYR A 404 ? 0.4347 0.4136 0.5511 0.0052 0.0748 -0.0523 420 TYR A C 3318 O O . TYR A 404 ? 0.4441 0.4195 0.5652 0.0027 0.0803 -0.0526 420 TYR A O 3319 C CB . TYR A 404 ? 0.4030 0.3907 0.5138 0.0062 0.0660 -0.0549 420 TYR A CB 3320 C CG . TYR A 404 ? 0.3946 0.3819 0.4912 0.0073 0.0646 -0.0479 420 TYR A CG 3321 C CD1 . TYR A 404 ? 0.3888 0.3800 0.4787 0.0098 0.0587 -0.0470 420 TYR A CD1 3322 C CD2 . TYR A 404 ? 0.3918 0.3749 0.4815 0.0059 0.0692 -0.0424 420 TYR A CD2 3323 C CE1 . TYR A 404 ? 0.3840 0.3750 0.4616 0.0107 0.0575 -0.0410 420 TYR A CE1 3324 C CE2 . TYR A 404 ? 0.3885 0.3714 0.4657 0.0070 0.0677 -0.0364 420 TYR A CE2 3325 C CZ . TYR A 404 ? 0.3825 0.3695 0.4542 0.0094 0.0619 -0.0358 420 TYR A CZ 3326 O OH . TYR A 404 ? 0.3869 0.3738 0.4470 0.0103 0.0606 -0.0302 420 TYR A OH 3327 N N . VAL A 405 ? 0.4422 0.4191 0.5517 0.0068 0.0746 -0.0479 421 VAL A N 3328 C CA . VAL A 405 ? 0.4642 0.4342 0.5697 0.0058 0.0804 -0.0424 421 VAL A CA 3329 C C . VAL A 405 ? 0.4853 0.4547 0.5762 0.0068 0.0793 -0.0354 421 VAL A C 3330 O O . VAL A 405 ? 0.4746 0.4467 0.5588 0.0091 0.0748 -0.0335 421 VAL A O 3331 C CB . VAL A 405 ? 0.4740 0.4414 0.5840 0.0070 0.0815 -0.0428 421 VAL A CB 3332 C CG1 . VAL A 405 ? 0.4755 0.4355 0.5798 0.0064 0.0871 -0.0364 421 VAL A CG1 3333 C CG2 . VAL A 405 ? 0.4683 0.4361 0.5934 0.0059 0.0830 -0.0499 421 VAL A CG2 3334 N N . ARG A 406 ? 0.4989 0.4651 0.5852 0.0050 0.0833 -0.0319 422 ARG A N 3335 C CA . ARG A 406 ? 0.5208 0.4870 0.5939 0.0058 0.0820 -0.0260 422 ARG A CA 3336 C C . ARG A 406 ? 0.5151 0.4756 0.5806 0.0067 0.0849 -0.0198 422 ARG A C 3337 O O . ARG A 406 ? 0.5399 0.4956 0.6004 0.0055 0.0895 -0.0156 422 ARG A O 3338 C CB . ARG A 406 ? 0.5400 0.5060 0.6111 0.0038 0.0842 -0.0255 422 ARG A CB 3339 C CG . ARG A 406 ? 0.5757 0.5431 0.6341 0.0046 0.0819 -0.0205 422 ARG A CG 3340 C CD . ARG A 406 ? 0.6045 0.5702 0.6607 0.0024 0.0856 -0.0193 422 ARG A CD 3341 N NE . ARG A 406 ? 0.6269 0.5906 0.6704 0.0031 0.0862 -0.0130 422 ARG A NE 3342 C CZ . ARG A 406 ? 0.6231 0.5907 0.6587 0.0043 0.0816 -0.0112 422 ARG A CZ 3343 N NH1 . ARG A 406 ? 0.6441 0.6176 0.6828 0.0050 0.0763 -0.0149 422 ARG A NH1 3344 N NH2 . ARG A 406 ? 0.6165 0.5823 0.6413 0.0050 0.0823 -0.0058 422 ARG A NH2 3345 N N . ASP A 407 ? 0.4843 0.4455 0.5491 0.0089 0.0823 -0.0193 423 ASP A N 3346 C CA . ASP A 407 ? 0.4709 0.4271 0.5282 0.0102 0.0842 -0.0135 423 ASP A CA 3347 C C . ASP A 407 ? 0.4593 0.4180 0.5040 0.0120 0.0803 -0.0089 423 ASP A C 3348 O O . ASP A 407 ? 0.4387 0.4024 0.4806 0.0119 0.0769 -0.0100 423 ASP A O 3349 C CB . ASP A 407 ? 0.4723 0.4273 0.5356 0.0117 0.0838 -0.0152 423 ASP A CB 3350 C CG . ASP A 407 ? 0.4667 0.4286 0.5321 0.0136 0.0774 -0.0191 423 ASP A CG 3351 O OD1 . ASP A 407 ? 0.4491 0.4160 0.5081 0.0145 0.0730 -0.0186 423 ASP A OD1 3352 O OD2 . ASP A 407 ? 0.4721 0.4342 0.5454 0.0143 0.0770 -0.0227 423 ASP A OD2 3353 N N . ASP A 408 ? 0.4572 0.4124 0.4948 0.0137 0.0809 -0.0040 424 ASP A N 3354 C CA . ASP A 408 ? 0.4580 0.4154 0.4841 0.0155 0.0776 0.0002 424 ASP A CA 3355 C C . ASP A 408 ? 0.4362 0.4010 0.4617 0.0170 0.0712 -0.0023 424 ASP A C 3356 O O . ASP A 408 ? 0.4316 0.4001 0.4503 0.0174 0.0682 -0.0008 424 ASP A O 3357 C CB . ASP A 408 ? 0.4885 0.4409 0.5086 0.0173 0.0790 0.0053 424 ASP A CB 3358 C CG . ASP A 408 ? 0.5282 0.4728 0.5449 0.0161 0.0850 0.0094 424 ASP A CG 3359 O OD1 . ASP A 408 ? 0.5451 0.4888 0.5630 0.0138 0.0880 0.0088 424 ASP A OD1 3360 O OD2 . ASP A 408 ? 0.5740 0.5135 0.5869 0.0176 0.0866 0.0134 424 ASP A OD2 3361 N N . GLU A 409 ? 0.4168 0.3837 0.4494 0.0179 0.0693 -0.0061 425 GLU A N 3362 C CA . GLU A 409 ? 0.4001 0.3737 0.4321 0.0195 0.0635 -0.0087 425 GLU A CA 3363 C C . GLU A 409 ? 0.3833 0.3619 0.4180 0.0183 0.0610 -0.0125 425 GLU A C 3364 O O . GLU A 409 ? 0.3641 0.3474 0.3932 0.0190 0.0568 -0.0120 425 GLU A O 3365 C CB . GLU A 409 ? 0.4127 0.3870 0.4512 0.0209 0.0624 -0.0117 425 GLU A CB 3366 C CG . GLU A 409 ? 0.4373 0.4078 0.4717 0.0227 0.0635 -0.0077 425 GLU A CG 3367 C CD . GLU A 409 ? 0.4640 0.4353 0.5048 0.0242 0.0623 -0.0107 425 GLU A CD 3368 O OE1 . GLU A 409 ? 0.4684 0.4426 0.5177 0.0238 0.0611 -0.0163 425 GLU A OE1 3369 O OE2 . GLU A 409 ? 0.4805 0.4497 0.5179 0.0260 0.0623 -0.0078 425 GLU A OE2 3370 N N . ALA A 410 ? 0.3603 0.3377 0.4034 0.0164 0.0634 -0.0162 426 ALA A N 3371 C CA . ALA A 410 ? 0.3467 0.3282 0.3928 0.0153 0.0611 -0.0200 426 ALA A CA 3372 C C . ALA A 410 ? 0.3428 0.3246 0.3808 0.0144 0.0612 -0.0164 426 ALA A C 3373 O O . ALA A 410 ? 0.3263 0.3126 0.3622 0.0146 0.0573 -0.0177 426 ALA A O 3374 C CB . ALA A 410 ? 0.3456 0.3255 0.4030 0.0134 0.0642 -0.0247 426 ALA A CB 3375 N N . ARG A 411 ? 0.3369 0.3137 0.3703 0.0137 0.0655 -0.0120 427 ARG A N 3376 C CA . ARG A 411 ? 0.3416 0.3185 0.3667 0.0131 0.0656 -0.0084 427 ARG A CA 3377 C C . ARG A 411 ? 0.3296 0.3107 0.3461 0.0149 0.0607 -0.0060 427 ARG A C 3378 O O . ARG A 411 ? 0.3231 0.3076 0.3365 0.0145 0.0581 -0.0063 427 ARG A O 3379 C CB . ARG A 411 ? 0.3553 0.3259 0.3760 0.0123 0.0710 -0.0039 427 ARG A CB 3380 C CG . ARG A 411 ? 0.3678 0.3386 0.3821 0.0112 0.0718 -0.0016 427 ARG A CG 3381 C CD . ARG A 411 ? 0.3856 0.3513 0.3911 0.0116 0.0751 0.0040 427 ARG A CD 3382 N NE . ARG A 411 ? 0.3918 0.3578 0.3916 0.0105 0.0760 0.0057 427 ARG A NE 3383 C CZ . ARG A 411 ? 0.3998 0.3618 0.3914 0.0106 0.0789 0.0104 427 ARG A CZ 3384 N NH1 . ARG A 411 ? 0.4052 0.3622 0.3932 0.0119 0.0811 0.0140 427 ARG A NH1 3385 N NH2 . ARG A 411 ? 0.4016 0.3645 0.3886 0.0096 0.0795 0.0113 427 ARG A NH2 3386 N N . ILE A 412 ? 0.3256 0.3062 0.3385 0.0168 0.0596 -0.0037 428 ILE A N 3387 C CA . ILE A 412 ? 0.3215 0.3063 0.3273 0.0186 0.0551 -0.0018 428 ILE A CA 3388 C C . ILE A 412 ? 0.3097 0.3004 0.3181 0.0188 0.0505 -0.0057 428 ILE A C 3389 O O . ILE A 412 ? 0.3075 0.3017 0.3105 0.0190 0.0475 -0.0046 428 ILE A O 3390 C CB . ILE A 412 ? 0.3223 0.3059 0.3254 0.0207 0.0547 0.0005 428 ILE A CB 3391 C CG1 . ILE A 412 ? 0.3304 0.3080 0.3286 0.0209 0.0587 0.0052 428 ILE A CG1 3392 C CG2 . ILE A 412 ? 0.3148 0.3034 0.3120 0.0224 0.0501 0.0015 428 ILE A CG2 3393 C CD1 . ILE A 412 ? 0.3403 0.3179 0.3298 0.0206 0.0586 0.0089 428 ILE A CD1 3394 N N . ASN A 413 ? 0.3085 0.3003 0.3252 0.0188 0.0498 -0.0103 429 ASN A N 3395 C CA . ASN A 413 ? 0.3076 0.3046 0.3268 0.0191 0.0454 -0.0142 429 ASN A CA 3396 C C . ASN A 413 ? 0.3087 0.3073 0.3272 0.0177 0.0445 -0.0149 429 ASN A C 3397 O O . ASN A 413 ? 0.2956 0.2982 0.3106 0.0182 0.0404 -0.0152 429 ASN A O 3398 C CB . ASN A 413 ? 0.3168 0.3142 0.3459 0.0192 0.0454 -0.0195 429 ASN A CB 3399 C CG . ASN A 413 ? 0.3240 0.3226 0.3537 0.0212 0.0438 -0.0203 429 ASN A CG 3400 O OD1 . ASN A 413 ? 0.3274 0.3268 0.3503 0.0225 0.0427 -0.0170 429 ASN A OD1 3401 N ND2 . ASN A 413 ? 0.3237 0.3228 0.3621 0.0215 0.0437 -0.0251 429 ASN A ND2 3402 N N . GLN A 414 ? 0.3065 0.3018 0.3283 0.0158 0.0483 -0.0152 430 GLN A N 3403 C CA . GLN A 414 ? 0.3104 0.3069 0.3328 0.0144 0.0478 -0.0164 430 GLN A CA 3404 C C . GLN A 414 ? 0.3046 0.3017 0.3175 0.0143 0.0470 -0.0120 430 GLN A C 3405 O O . GLN A 414 ? 0.2943 0.2946 0.3053 0.0141 0.0438 -0.0127 430 GLN A O 3406 C CB . GLN A 414 ? 0.3272 0.3203 0.3568 0.0123 0.0524 -0.0186 430 GLN A CB 3407 C CG . GLN A 414 ? 0.3417 0.3358 0.3722 0.0107 0.0525 -0.0198 430 GLN A CG 3408 C CD . GLN A 414 ? 0.3546 0.3533 0.3890 0.0111 0.0476 -0.0241 430 GLN A CD 3409 O OE1 . GLN A 414 ? 0.3548 0.3556 0.3939 0.0122 0.0449 -0.0275 430 GLN A OE1 3410 N NE2 . GLN A 414 ? 0.3682 0.3684 0.4005 0.0102 0.0463 -0.0240 430 GLN A NE2 3411 N N . LEU A 415 ? 0.3082 0.3022 0.3154 0.0146 0.0497 -0.0076 431 LEU A N 3412 C CA . LEU A 415 ? 0.3161 0.3108 0.3142 0.0149 0.0487 -0.0034 431 LEU A CA 3413 C C . LEU A 415 ? 0.3069 0.3064 0.3008 0.0163 0.0437 -0.0030 431 LEU A C 3414 O O . LEU A 415 ? 0.3001 0.3021 0.2899 0.0160 0.0414 -0.0021 431 LEU A O 3415 C CB . LEU A 415 ? 0.3223 0.3128 0.3150 0.0154 0.0521 0.0009 431 LEU A CB 3416 C CG . LEU A 415 ? 0.3398 0.3255 0.3328 0.0138 0.0573 0.0022 431 LEU A CG 3417 C CD1 . LEU A 415 ? 0.3512 0.3319 0.3403 0.0147 0.0606 0.0060 431 LEU A CD1 3418 C CD2 . LEU A 415 ? 0.3394 0.3262 0.3276 0.0128 0.0571 0.0034 431 LEU A CD2 3419 N N . PHE A 416 ? 0.3012 0.3018 0.2963 0.0178 0.0422 -0.0038 432 PHE A N 3420 C CA . PHE A 416 ? 0.2983 0.3033 0.2894 0.0192 0.0378 -0.0035 432 PHE A CA 3421 C C . PHE A 416 ? 0.2930 0.3015 0.2864 0.0187 0.0344 -0.0066 432 PHE A C 3422 O O . PHE A 416 ? 0.2868 0.2981 0.2753 0.0188 0.0316 -0.0053 432 PHE A O 3423 C CB . PHE A 416 ? 0.2991 0.3047 0.2918 0.0209 0.0372 -0.0042 432 PHE A CB 3424 C CG . PHE A 416 ? 0.2999 0.3095 0.2872 0.0223 0.0336 -0.0030 432 PHE A CG 3425 C CD1 . PHE A 416 ? 0.3057 0.3152 0.2863 0.0230 0.0338 0.0009 432 PHE A CD1 3426 C CD2 . PHE A 416 ? 0.2998 0.3132 0.2886 0.0229 0.0302 -0.0059 432 PHE A CD2 3427 C CE1 . PHE A 416 ? 0.3116 0.3251 0.2879 0.0242 0.0308 0.0018 432 PHE A CE1 3428 C CE2 . PHE A 416 ? 0.3005 0.3176 0.2844 0.0240 0.0274 -0.0048 432 PHE A CE2 3429 C CZ . PHE A 416 ? 0.3062 0.3233 0.2841 0.0245 0.0278 -0.0009 432 PHE A CZ 3430 N N . LEU A 417 ? 0.2964 0.3046 0.2974 0.0181 0.0347 -0.0108 433 LEU A N 3431 C CA . LEU A 417 ? 0.2887 0.2997 0.2926 0.0178 0.0314 -0.0141 433 LEU A CA 3432 C C . LEU A 417 ? 0.2829 0.2941 0.2836 0.0166 0.0310 -0.0126 433 LEU A C 3433 O O . LEU A 417 ? 0.2784 0.2924 0.2762 0.0168 0.0274 -0.0127 433 LEU A O 3434 C CB . LEU A 417 ? 0.2947 0.3048 0.3082 0.0173 0.0323 -0.0191 433 LEU A CB 3435 C CG . LEU A 417 ? 0.2966 0.3091 0.3144 0.0171 0.0291 -0.0232 433 LEU A CG 3436 C CD1 . LEU A 417 ? 0.2963 0.3126 0.3113 0.0188 0.0240 -0.0243 433 LEU A CD1 3437 C CD2 . LEU A 417 ? 0.2982 0.3093 0.3263 0.0164 0.0309 -0.0280 433 LEU A CD2 3438 N N . THR A 418 ? 0.2746 0.2826 0.2755 0.0152 0.0349 -0.0112 434 THR A N 3439 C CA . THR A 418 ? 0.2694 0.2777 0.2674 0.0140 0.0349 -0.0098 434 THR A CA 3440 C C . THR A 418 ? 0.2630 0.2732 0.2522 0.0147 0.0328 -0.0058 434 THR A C 3441 O O . THR A 418 ? 0.2623 0.2745 0.2494 0.0143 0.0303 -0.0057 434 THR A O 3442 C CB . THR A 418 ? 0.2711 0.2755 0.2706 0.0125 0.0399 -0.0091 434 THR A CB 3443 O OG1 . THR A 418 ? 0.2790 0.2820 0.2874 0.0117 0.0420 -0.0130 434 THR A OG1 3444 C CG2 . THR A 418 ? 0.2705 0.2756 0.2677 0.0112 0.0397 -0.0084 434 THR A CG2 3445 N N . ALA A 419 ? 0.2582 0.2678 0.2430 0.0158 0.0336 -0.0029 435 ALA A N 3446 C CA . ALA A 419 ? 0.2577 0.2692 0.2349 0.0165 0.0318 0.0005 435 ALA A CA 3447 C C . ALA A 419 ? 0.2611 0.2766 0.2369 0.0172 0.0274 -0.0003 435 ALA A C 3448 O O . ALA A 419 ? 0.2548 0.2724 0.2260 0.0171 0.0254 0.0015 435 ALA A O 3449 C CB . ALA A 419 ? 0.2516 0.2616 0.2252 0.0177 0.0336 0.0034 435 ALA A CB 3450 N N . LEU A 420 ? 0.2654 0.2819 0.2454 0.0179 0.0260 -0.0032 436 LEU A N 3451 C CA . LEU A 420 ? 0.2773 0.2972 0.2558 0.0187 0.0220 -0.0042 436 LEU A CA 3452 C C . LEU A 420 ? 0.2916 0.3126 0.2701 0.0177 0.0196 -0.0051 436 LEU A C 3453 O O . LEU A 420 ? 0.2927 0.3162 0.2680 0.0181 0.0164 -0.0047 436 LEU A O 3454 C CB . LEU A 420 ? 0.2722 0.2928 0.2554 0.0197 0.0210 -0.0077 436 LEU A CB 3455 C CG . LEU A 420 ? 0.2779 0.2983 0.2607 0.0210 0.0222 -0.0071 436 LEU A CG 3456 C CD1 . LEU A 420 ? 0.2754 0.2963 0.2643 0.0218 0.0214 -0.0113 436 LEU A CD1 3457 C CD2 . LEU A 420 ? 0.2755 0.2987 0.2519 0.0220 0.0205 -0.0045 436 LEU A CD2 3458 N N . ASP A 421 ? 0.3085 0.3276 0.2907 0.0165 0.0213 -0.0064 437 ASP A N 3459 C CA . ASP A 421 ? 0.3313 0.3511 0.3137 0.0155 0.0194 -0.0070 437 ASP A CA 3460 C C . ASP A 421 ? 0.3149 0.3342 0.2929 0.0145 0.0208 -0.0038 437 ASP A C 3461 O O . ASP A 421 ? 0.3268 0.3477 0.3013 0.0143 0.0185 -0.0025 437 ASP A O 3462 C CB . ASP A 421 ? 0.3679 0.3864 0.3578 0.0147 0.0200 -0.0109 437 ASP A CB 3463 C CG . ASP A 421 ? 0.4046 0.4240 0.3994 0.0158 0.0179 -0.0147 437 ASP A CG 3464 O OD1 . ASP A 421 ? 0.4249 0.4466 0.4170 0.0169 0.0142 -0.0148 437 ASP A OD1 3465 O OD2 . ASP A 421 ? 0.4536 0.4715 0.4550 0.0155 0.0200 -0.0176 437 ASP A OD2 3466 N N . LYS A 422 ? 0.2941 0.3109 0.2721 0.0140 0.0247 -0.0027 438 LYS A N 3467 C CA . LYS A 422 ? 0.2872 0.3032 0.2621 0.0130 0.0263 -0.0006 438 LYS A CA 3468 C C . LYS A 422 ? 0.2865 0.3036 0.2541 0.0137 0.0260 0.0032 438 LYS A C 3469 O O . LYS A 422 ? 0.2879 0.3059 0.2524 0.0131 0.0252 0.0046 438 LYS A O 3470 C CB . LYS A 422 ? 0.2887 0.3014 0.2666 0.0121 0.0307 -0.0012 438 LYS A CB 3471 C CG . LYS A 422 ? 0.2834 0.2953 0.2692 0.0111 0.0313 -0.0054 438 LYS A CG 3472 C CD . LYS A 422 ? 0.2810 0.2946 0.2684 0.0103 0.0289 -0.0071 438 LYS A CD 3473 C CE . LYS A 422 ? 0.2804 0.2932 0.2763 0.0094 0.0297 -0.0116 438 LYS A CE 3474 N NZ . LYS A 422 ? 0.2812 0.2958 0.2791 0.0089 0.0264 -0.0135 438 LYS A NZ 3475 N N . ILE A 423 ? 0.2712 0.2883 0.2366 0.0150 0.0264 0.0047 439 ILE A N 3476 C CA . ILE A 423 ? 0.2646 0.2831 0.2238 0.0158 0.0257 0.0080 439 ILE A CA 3477 C C . ILE A 423 ? 0.2570 0.2791 0.2143 0.0162 0.0221 0.0081 439 ILE A C 3478 O O . ILE A 423 ? 0.2540 0.2779 0.2074 0.0160 0.0207 0.0099 439 ILE A O 3479 C CB . ILE A 423 ? 0.2654 0.2822 0.2229 0.0171 0.0279 0.0097 439 ILE A CB 3480 C CG1 . ILE A 423 ? 0.2694 0.2820 0.2281 0.0166 0.0319 0.0100 439 ILE A CG1 3481 C CG2 . ILE A 423 ? 0.2568 0.2755 0.2085 0.0181 0.0268 0.0126 439 ILE A CG2 3482 C CD1 . ILE A 423 ? 0.2796 0.2914 0.2350 0.0157 0.0332 0.0115 439 ILE A CD1 3483 N N . VAL A 424 ? 0.2510 0.2739 0.2109 0.0168 0.0206 0.0062 440 VAL A N 3484 C CA . VAL A 424 ? 0.2404 0.2664 0.1982 0.0173 0.0175 0.0063 440 VAL A CA 3485 C C . VAL A 424 ? 0.2343 0.2614 0.1908 0.0162 0.0153 0.0065 440 VAL A C 3486 O O . VAL A 424 ? 0.2355 0.2648 0.1882 0.0162 0.0137 0.0083 440 VAL A O 3487 C CB . VAL A 424 ? 0.2428 0.2692 0.2040 0.0180 0.0162 0.0035 440 VAL A CB 3488 C CG1 . VAL A 424 ? 0.2520 0.2810 0.2110 0.0182 0.0128 0.0032 440 VAL A CG1 3489 C CG2 . VAL A 424 ? 0.2469 0.2729 0.2085 0.0193 0.0178 0.0036 440 VAL A CG2 3490 N N . PHE A 425 ? 0.2301 0.2557 0.1903 0.0152 0.0154 0.0046 441 PHE A N 3491 C CA . PHE A 425 ? 0.2287 0.2550 0.1887 0.0143 0.0133 0.0044 441 PHE A CA 3492 C C . PHE A 425 ? 0.2236 0.2508 0.1796 0.0136 0.0134 0.0071 441 PHE A C 3493 O O . PHE A 425 ? 0.2185 0.2469 0.1731 0.0130 0.0112 0.0076 441 PHE A O 3494 C CB . PHE A 425 ? 0.2279 0.2523 0.1933 0.0134 0.0140 0.0017 441 PHE A CB 3495 C CG . PHE A 425 ? 0.2304 0.2553 0.1968 0.0127 0.0113 0.0008 441 PHE A CG 3496 C CD1 . PHE A 425 ? 0.2262 0.2519 0.1932 0.0132 0.0079 -0.0004 441 PHE A CD1 3497 C CD2 . PHE A 425 ? 0.2267 0.2510 0.1935 0.0115 0.0122 0.0010 441 PHE A CD2 3498 C CE1 . PHE A 425 ? 0.2266 0.2522 0.1946 0.0127 0.0053 -0.0012 441 PHE A CE1 3499 C CE2 . PHE A 425 ? 0.2276 0.2522 0.1959 0.0109 0.0097 0.0000 441 PHE A CE2 3500 C CZ . PHE A 425 ? 0.2307 0.2558 0.1997 0.0115 0.0062 -0.0010 441 PHE A CZ 3501 N N . LEU A 426 ? 0.2298 0.2561 0.1840 0.0137 0.0161 0.0086 442 LEU A N 3502 C CA . LEU A 426 ? 0.2348 0.2620 0.1857 0.0131 0.0163 0.0105 442 LEU A CA 3503 C C . LEU A 426 ? 0.2320 0.2620 0.1792 0.0133 0.0140 0.0123 442 LEU A C 3504 O O . LEU A 426 ? 0.2308 0.2617 0.1776 0.0123 0.0125 0.0125 442 LEU A O 3505 C CB . LEU A 426 ? 0.2396 0.2651 0.1885 0.0136 0.0193 0.0119 442 LEU A CB 3506 C CG . LEU A 426 ? 0.2486 0.2710 0.2009 0.0132 0.0222 0.0103 442 LEU A CG 3507 C CD1 . LEU A 426 ? 0.2467 0.2673 0.1960 0.0139 0.0252 0.0123 442 LEU A CD1 3508 C CD2 . LEU A 426 ? 0.2507 0.2727 0.2058 0.0118 0.0222 0.0086 442 LEU A CD2 3509 N N . PRO A 427 ? 0.2338 0.2652 0.1788 0.0143 0.0138 0.0135 443 PRO A N 3510 C CA . PRO A 427 ? 0.2306 0.2647 0.1727 0.0142 0.0119 0.0149 443 PRO A CA 3511 C C . PRO A 427 ? 0.2280 0.2627 0.1711 0.0135 0.0094 0.0141 443 PRO A C 3512 O O . PRO A 427 ? 0.2212 0.2573 0.1627 0.0127 0.0080 0.0152 443 PRO A O 3513 C CB . PRO A 427 ? 0.2278 0.2634 0.1681 0.0155 0.0124 0.0158 443 PRO A CB 3514 C CG . PRO A 427 ? 0.2318 0.2652 0.1744 0.0163 0.0141 0.0146 443 PRO A CG 3515 C CD . PRO A 427 ? 0.2313 0.2619 0.1764 0.0156 0.0154 0.0135 443 PRO A CD 3516 N N . PHE A 428 ? 0.2357 0.2691 0.1812 0.0138 0.0089 0.0122 444 PHE A N 3517 C CA . PHE A 428 ? 0.2258 0.2593 0.1719 0.0134 0.0062 0.0114 444 PHE A CA 3518 C C . PHE A 428 ? 0.2255 0.2583 0.1727 0.0122 0.0051 0.0113 444 PHE A C 3519 O O . PHE A 428 ? 0.2154 0.2489 0.1607 0.0116 0.0032 0.0125 444 PHE A O 3520 C CB . PHE A 428 ? 0.2362 0.2683 0.1855 0.0141 0.0055 0.0087 444 PHE A CB 3521 C CG . PHE A 428 ? 0.2291 0.2608 0.1789 0.0140 0.0025 0.0078 444 PHE A CG 3522 C CD1 . PHE A 428 ? 0.2293 0.2621 0.1758 0.0145 0.0006 0.0086 444 PHE A CD1 3523 C CD2 . PHE A 428 ? 0.2277 0.2577 0.1809 0.0133 0.0016 0.0062 444 PHE A CD2 3524 C CE1 . PHE A 428 ? 0.2299 0.2619 0.1760 0.0144 -0.0022 0.0081 444 PHE A CE1 3525 C CE2 . PHE A 428 ? 0.2328 0.2622 0.1864 0.0133 -0.0014 0.0055 444 PHE A CE2 3526 C CZ . PHE A 428 ? 0.2297 0.2599 0.1794 0.0140 -0.0034 0.0066 444 PHE A CZ 3527 N N . ALA A 429 ? 0.2243 0.2555 0.1745 0.0117 0.0065 0.0101 445 ALA A N 3528 C CA . ALA A 429 ? 0.2222 0.2526 0.1743 0.0106 0.0055 0.0093 445 ALA A CA 3529 C C . ALA A 429 ? 0.2316 0.2635 0.1809 0.0099 0.0055 0.0114 445 ALA A C 3530 O O . ALA A 429 ? 0.2237 0.2557 0.1734 0.0091 0.0036 0.0116 445 ALA A O 3531 C CB . ALA A 429 ? 0.2205 0.2492 0.1765 0.0103 0.0075 0.0073 445 ALA A CB 3532 N N . PHE A 430 ? 0.2398 0.2727 0.1866 0.0103 0.0075 0.0128 446 PHE A N 3533 C CA . PHE A 430 ? 0.2470 0.2818 0.1914 0.0098 0.0073 0.0146 446 PHE A CA 3534 C C . PHE A 430 ? 0.2504 0.2868 0.1931 0.0093 0.0052 0.0159 446 PHE A C 3535 O O . PHE A 430 ? 0.2554 0.2926 0.1982 0.0083 0.0041 0.0164 446 PHE A O 3536 C CB . PHE A 430 ? 0.2549 0.2907 0.1966 0.0107 0.0094 0.0158 446 PHE A CB 3537 C CG . PHE A 430 ? 0.2597 0.2964 0.2001 0.0103 0.0099 0.0165 446 PHE A CG 3538 C CD1 . PHE A 430 ? 0.2692 0.3063 0.2109 0.0091 0.0086 0.0159 446 PHE A CD1 3539 C CD2 . PHE A 430 ? 0.2739 0.3112 0.2116 0.0114 0.0115 0.0175 446 PHE A CD2 3540 C CE1 . PHE A 430 ? 0.2675 0.3059 0.2082 0.0088 0.0089 0.0161 446 PHE A CE1 3541 C CE2 . PHE A 430 ? 0.2743 0.3126 0.2104 0.0113 0.0117 0.0179 446 PHE A CE2 3542 C CZ . PHE A 430 ? 0.2743 0.3134 0.2121 0.0100 0.0104 0.0171 446 PHE A CZ 3543 N N . THR A 431 ? 0.2435 0.2804 0.1849 0.0100 0.0047 0.0163 447 THR A N 3544 C CA . THR A 431 ? 0.2427 0.2811 0.1819 0.0096 0.0032 0.0177 447 THR A CA 3545 C C . THR A 431 ? 0.2396 0.2764 0.1797 0.0088 0.0009 0.0175 447 THR A C 3546 O O . THR A 431 ? 0.2365 0.2741 0.1750 0.0079 0.0000 0.0190 447 THR A O 3547 C CB . THR A 431 ? 0.2409 0.2804 0.1779 0.0106 0.0035 0.0182 447 THR A CB 3548 O OG1 . THR A 431 ? 0.2413 0.2790 0.1797 0.0114 0.0029 0.0165 447 THR A OG1 3549 C CG2 . THR A 431 ? 0.2381 0.2793 0.1739 0.0115 0.0054 0.0188 447 THR A CG2 3550 N N . MET A 432 ? 0.2355 0.2701 0.1782 0.0090 0.0000 0.0156 448 MET A N 3551 C CA . MET A 432 ? 0.2311 0.2639 0.1748 0.0085 -0.0025 0.0152 448 MET A CA 3552 C C . MET A 432 ? 0.2369 0.2698 0.1816 0.0072 -0.0030 0.0159 448 MET A C 3553 O O . MET A 432 ? 0.2323 0.2646 0.1760 0.0065 -0.0048 0.0171 448 MET A O 3554 C CB . MET A 432 ? 0.2287 0.2595 0.1761 0.0092 -0.0035 0.0126 448 MET A CB 3555 C CG . MET A 432 ? 0.2210 0.2516 0.1684 0.0105 -0.0034 0.0113 448 MET A CG 3556 S SD . MET A 432 ? 0.2314 0.2621 0.1744 0.0112 -0.0057 0.0126 448 MET A SD 3557 C CE . MET A 432 ? 0.2171 0.2506 0.1563 0.0115 -0.0032 0.0145 448 MET A CE 3558 N N . ASP A 433 ? 0.2274 0.2609 0.1739 0.0068 -0.0015 0.0152 449 ASP A N 3559 C CA . ASP A 433 ? 0.2359 0.2699 0.1834 0.0056 -0.0019 0.0155 449 ASP A CA 3560 C C . ASP A 433 ? 0.2306 0.2672 0.1757 0.0051 -0.0010 0.0175 449 ASP A C 3561 O O . ASP A 433 ? 0.2424 0.2793 0.1880 0.0041 -0.0020 0.0182 449 ASP A O 3562 C CB . ASP A 433 ? 0.2362 0.2696 0.1870 0.0054 -0.0010 0.0135 449 ASP A CB 3563 C CG . ASP A 433 ? 0.2459 0.2768 0.2004 0.0053 -0.0027 0.0114 449 ASP A CG 3564 O OD1 . ASP A 433 ? 0.2499 0.2796 0.2042 0.0057 -0.0047 0.0115 449 ASP A OD1 3565 O OD2 . ASP A 433 ? 0.2433 0.2738 0.2011 0.0048 -0.0023 0.0095 449 ASP A OD2 3566 N N . LYS A 434 ? 0.2266 0.2649 0.1694 0.0059 0.0006 0.0182 450 LYS A N 3567 C CA . LYS A 434 ? 0.2238 0.2649 0.1647 0.0056 0.0012 0.0197 450 LYS A CA 3568 C C . LYS A 434 ? 0.2310 0.2722 0.1707 0.0048 0.0000 0.0212 450 LYS A C 3569 O O . LYS A 434 ? 0.2326 0.2752 0.1725 0.0037 -0.0003 0.0221 450 LYS A O 3570 C CB . LYS A 434 ? 0.2240 0.2668 0.1628 0.0068 0.0029 0.0201 450 LYS A CB 3571 C CG . LYS A 434 ? 0.2248 0.2678 0.1638 0.0076 0.0044 0.0194 450 LYS A CG 3572 C CD . LYS A 434 ? 0.2252 0.2696 0.1620 0.0090 0.0059 0.0200 450 LYS A CD 3573 C CE . LYS A 434 ? 0.2386 0.2831 0.1745 0.0098 0.0073 0.0198 450 LYS A CE 3574 N NZ . LYS A 434 ? 0.2405 0.2878 0.1758 0.0096 0.0067 0.0202 450 LYS A NZ 3575 N N . TYR A 435 ? 0.2233 0.2630 0.1619 0.0053 -0.0008 0.0214 451 TYR A N 3576 C CA . TYR A 435 ? 0.2278 0.2670 0.1644 0.0046 -0.0019 0.0230 451 TYR A CA 3577 C C . TYR A 435 ? 0.2267 0.2640 0.1650 0.0033 -0.0036 0.0234 451 TYR A C 3578 O O . TYR A 435 ? 0.2261 0.2640 0.1638 0.0021 -0.0037 0.0249 451 TYR A O 3579 C CB . TYR A 435 ? 0.2335 0.2713 0.1681 0.0056 -0.0026 0.0228 451 TYR A CB 3580 C CG . TYR A 435 ? 0.2458 0.2826 0.1775 0.0050 -0.0037 0.0247 451 TYR A CG 3581 C CD1 . TYR A 435 ? 0.2538 0.2929 0.1830 0.0043 -0.0025 0.0265 451 TYR A CD1 3582 C CD2 . TYR A 435 ? 0.2538 0.2874 0.1851 0.0053 -0.0061 0.0246 451 TYR A CD2 3583 C CE1 . TYR A 435 ? 0.2609 0.2987 0.1869 0.0037 -0.0031 0.0283 451 TYR A CE1 3584 C CE2 . TYR A 435 ? 0.2609 0.2931 0.1886 0.0049 -0.0070 0.0266 451 TYR A CE2 3585 C CZ . TYR A 435 ? 0.2660 0.3003 0.1910 0.0040 -0.0053 0.0285 451 TYR A CZ 3586 O OH . TYR A 435 ? 0.2770 0.3096 0.1980 0.0035 -0.0059 0.0307 451 TYR A OH 3587 N N . ARG A 436 ? 0.2297 0.2645 0.1704 0.0036 -0.0050 0.0218 452 ARG A N 3588 C CA . ARG A 436 ? 0.2297 0.2624 0.1724 0.0026 -0.0070 0.0219 452 ARG A CA 3589 C C . ARG A 436 ? 0.2314 0.2656 0.1765 0.0013 -0.0064 0.0218 452 ARG A C 3590 O O . ARG A 436 ? 0.2276 0.2612 0.1734 0.0001 -0.0073 0.0230 452 ARG A O 3591 C CB . ARG A 436 ? 0.2276 0.2575 0.1729 0.0033 -0.0088 0.0199 452 ARG A CB 3592 C CG . ARG A 436 ? 0.2341 0.2622 0.1770 0.0045 -0.0102 0.0201 452 ARG A CG 3593 C CD . ARG A 436 ? 0.2312 0.2567 0.1772 0.0053 -0.0124 0.0179 452 ARG A CD 3594 N NE . ARG A 436 ? 0.2394 0.2658 0.1886 0.0059 -0.0109 0.0152 452 ARG A NE 3595 C CZ . ARG A 436 ? 0.2399 0.2647 0.1928 0.0065 -0.0121 0.0126 452 ARG A CZ 3596 N NH1 . ARG A 436 ? 0.2382 0.2605 0.1923 0.0069 -0.0151 0.0120 452 ARG A NH1 3597 N NH2 . ARG A 436 ? 0.2454 0.2711 0.2010 0.0068 -0.0101 0.0105 452 ARG A NH2 3598 N N . TRP A 437 ? 0.2346 0.2708 0.1809 0.0017 -0.0048 0.0204 453 TRP A N 3599 C CA . TRP A 437 ? 0.2407 0.2790 0.1888 0.0008 -0.0043 0.0201 453 TRP A CA 3600 C C . TRP A 437 ? 0.2423 0.2826 0.1891 -0.0001 -0.0038 0.0220 453 TRP A C 3601 O O . TRP A 437 ? 0.2392 0.2798 0.1881 -0.0014 -0.0044 0.0221 453 TRP A O 3602 C CB . TRP A 437 ? 0.2416 0.2820 0.1897 0.0016 -0.0025 0.0188 453 TRP A CB 3603 C CG . TRP A 437 ? 0.2523 0.2911 0.2021 0.0022 -0.0022 0.0168 453 TRP A CG 3604 C CD1 . TRP A 437 ? 0.2544 0.2908 0.2071 0.0020 -0.0035 0.0153 453 TRP A CD1 3605 C CD2 . TRP A 437 ? 0.2502 0.2899 0.1992 0.0032 -0.0002 0.0159 453 TRP A CD2 3606 N NE1 . TRP A 437 ? 0.2541 0.2900 0.2081 0.0026 -0.0022 0.0134 453 TRP A NE1 3607 C CE2 . TRP A 437 ? 0.2547 0.2923 0.2061 0.0033 -0.0001 0.0139 453 TRP A CE2 3608 C CE3 . TRP A 437 ? 0.2583 0.3000 0.2045 0.0041 0.0014 0.0166 453 TRP A CE3 3609 C CZ2 . TRP A 437 ? 0.2542 0.2917 0.2053 0.0040 0.0019 0.0127 453 TRP A CZ2 3610 C CZ3 . TRP A 437 ? 0.2563 0.2977 0.2019 0.0050 0.0031 0.0156 453 TRP A CZ3 3611 C CH2 . TRP A 437 ? 0.2615 0.3006 0.2094 0.0049 0.0036 0.0138 453 TRP A CH2 3612 N N . SER A 438 ? 0.2481 0.2898 0.1918 0.0004 -0.0027 0.0232 454 SER A N 3613 C CA . SER A 438 ? 0.2543 0.2983 0.1971 -0.0005 -0.0019 0.0247 454 SER A CA 3614 C C . SER A 438 ? 0.2644 0.3062 0.2070 -0.0019 -0.0029 0.0265 454 SER A C 3615 O O . SER A 438 ? 0.2653 0.3084 0.2092 -0.0033 -0.0025 0.0273 454 SER A O 3616 C CB . SER A 438 ? 0.2531 0.2993 0.1929 0.0005 -0.0004 0.0254 454 SER A CB 3617 O OG . SER A 438 ? 0.2552 0.2996 0.1922 0.0007 -0.0006 0.0265 454 SER A OG 3618 N N . LEU A 439 ? 0.2716 0.3100 0.2128 -0.0015 -0.0043 0.0270 455 LEU A N 3619 C CA . LEU A 439 ? 0.2785 0.3140 0.2191 -0.0027 -0.0056 0.0288 455 LEU A CA 3620 C C . LEU A 439 ? 0.2778 0.3119 0.2227 -0.0038 -0.0069 0.0280 455 LEU A C 3621 O O . LEU A 439 ? 0.2771 0.3106 0.2230 -0.0053 -0.0070 0.0294 455 LEU A O 3622 C CB . LEU A 439 ? 0.2890 0.3211 0.2266 -0.0016 -0.0071 0.0294 455 LEU A CB 3623 C CG . LEU A 439 ? 0.2977 0.3308 0.2313 -0.0004 -0.0062 0.0298 455 LEU A CG 3624 C CD1 . LEU A 439 ? 0.3075 0.3369 0.2384 0.0005 -0.0083 0.0303 455 LEU A CD1 3625 C CD2 . LEU A 439 ? 0.2968 0.3324 0.2278 -0.0012 -0.0041 0.0316 455 LEU A CD2 3626 N N . PHE A 440 ? 0.2690 0.3024 0.2165 -0.0030 -0.0079 0.0258 456 PHE A N 3627 C CA . PHE A 440 ? 0.2663 0.2986 0.2183 -0.0038 -0.0092 0.0244 456 PHE A CA 3628 C C . PHE A 440 ? 0.2705 0.3058 0.2250 -0.0051 -0.0081 0.0241 456 PHE A C 3629 O O . PHE A 440 ? 0.2714 0.3056 0.2288 -0.0064 -0.0091 0.0242 456 PHE A O 3630 C CB . PHE A 440 ? 0.2485 0.2807 0.2028 -0.0026 -0.0096 0.0216 456 PHE A CB 3631 C CG . PHE A 440 ? 0.2525 0.2816 0.2063 -0.0015 -0.0112 0.0210 456 PHE A CG 3632 C CD1 . PHE A 440 ? 0.2508 0.2767 0.2024 -0.0014 -0.0129 0.0229 456 PHE A CD1 3633 C CD2 . PHE A 440 ? 0.2470 0.2761 0.2026 -0.0005 -0.0110 0.0185 456 PHE A CD2 3634 C CE1 . PHE A 440 ? 0.2551 0.2783 0.2065 -0.0001 -0.0148 0.0220 456 PHE A CE1 3635 C CE2 . PHE A 440 ? 0.2482 0.2748 0.2043 0.0005 -0.0126 0.0175 456 PHE A CE2 3636 C CZ . PHE A 440 ? 0.2496 0.2732 0.2036 0.0008 -0.0147 0.0192 456 PHE A CZ 3637 N N . ARG A 441 ? 0.2738 0.3129 0.2273 -0.0046 -0.0063 0.0235 457 ARG A N 3638 C CA . ARG A 441 ? 0.2757 0.3182 0.2314 -0.0054 -0.0054 0.0228 457 ARG A CA 3639 C C . ARG A 441 ? 0.2788 0.3224 0.2342 -0.0068 -0.0046 0.0248 457 ARG A C 3640 O O . ARG A 441 ? 0.2788 0.3253 0.2367 -0.0077 -0.0040 0.0241 457 ARG A O 3641 C CB . ARG A 441 ? 0.2698 0.3157 0.2242 -0.0040 -0.0040 0.0215 457 ARG A CB 3642 C CG . ARG A 441 ? 0.2731 0.3186 0.2288 -0.0031 -0.0044 0.0192 457 ARG A CG 3643 C CD . ARG A 441 ? 0.2731 0.3206 0.2262 -0.0014 -0.0029 0.0185 457 ARG A CD 3644 N NE . ARG A 441 ? 0.2771 0.3242 0.2313 -0.0008 -0.0028 0.0164 457 ARG A NE 3645 C CZ . ARG A 441 ? 0.2812 0.3286 0.2333 0.0005 -0.0015 0.0157 457 ARG A CZ 3646 N NH1 . ARG A 441 ? 0.2827 0.3306 0.2316 0.0016 -0.0004 0.0170 457 ARG A NH1 3647 N NH2 . ARG A 441 ? 0.2821 0.3291 0.2353 0.0009 -0.0012 0.0138 457 ARG A NH2 3648 N N . GLY A 442 ? 0.2810 0.3222 0.2334 -0.0071 -0.0045 0.0272 458 GLY A N 3649 C CA . GLY A 442 ? 0.2892 0.3311 0.2410 -0.0087 -0.0033 0.0292 458 GLY A CA 3650 C C . GLY A 442 ? 0.2972 0.3436 0.2477 -0.0083 -0.0012 0.0290 458 GLY A C 3651 O O . GLY A 442 ? 0.2974 0.3460 0.2496 -0.0097 0.0000 0.0295 458 GLY A O 3652 N N . GLU A 443 ? 0.2980 0.3458 0.2461 -0.0065 -0.0008 0.0282 459 GLU A N 3653 C CA . GLU A 443 ? 0.3105 0.3625 0.2578 -0.0058 0.0007 0.0277 459 GLU A CA 3654 C C . GLU A 443 ? 0.3207 0.3728 0.2642 -0.0058 0.0021 0.0295 459 GLU A C 3655 O O . GLU A 443 ? 0.3295 0.3852 0.2728 -0.0055 0.0035 0.0292 459 GLU A O 3656 C CB . GLU A 443 ? 0.3020 0.3553 0.2487 -0.0037 0.0005 0.0259 459 GLU A CB 3657 C CG . GLU A 443 ? 0.3106 0.3649 0.2606 -0.0037 -0.0002 0.0239 459 GLU A CG 3658 C CD . GLU A 443 ? 0.3192 0.3733 0.2680 -0.0018 -0.0003 0.0224 459 GLU A CD 3659 O OE1 . GLU A 443 ? 0.3222 0.3749 0.2682 -0.0006 0.0000 0.0229 459 GLU A OE1 3660 O OE2 . GLU A 443 ? 0.3147 0.3701 0.2654 -0.0015 -0.0007 0.0207 459 GLU A OE2 3661 N N . VAL A 444 ? 0.3339 0.3823 0.2747 -0.0060 0.0015 0.0312 460 VAL A N 3662 C CA . VAL A 444 ? 0.3423 0.3906 0.2789 -0.0059 0.0027 0.0329 460 VAL A CA 3663 C C . VAL A 444 ? 0.3761 0.4214 0.3114 -0.0077 0.0028 0.0353 460 VAL A C 3664 O O . VAL A 444 ? 0.3869 0.4282 0.3223 -0.0080 0.0010 0.0359 460 VAL A O 3665 C CB . VAL A 444 ? 0.3413 0.3877 0.2745 -0.0039 0.0019 0.0326 460 VAL A CB 3666 C CG1 . VAL A 444 ? 0.3247 0.3717 0.2536 -0.0037 0.0032 0.0339 460 VAL A CG1 3667 C CG2 . VAL A 444 ? 0.3227 0.3709 0.2572 -0.0022 0.0018 0.0304 460 VAL A CG2 3668 N N . ASP A 445 ? 0.4025 0.4496 0.3367 -0.0089 0.0050 0.0366 461 ASP A N 3669 C CA . ASP A 445 ? 0.4493 0.4931 0.3811 -0.0107 0.0056 0.0393 461 ASP A CA 3670 C C . ASP A 445 ? 0.4353 0.4753 0.3612 -0.0095 0.0045 0.0408 461 ASP A C 3671 O O . ASP A 445 ? 0.3996 0.4411 0.3230 -0.0077 0.0046 0.0399 461 ASP A O 3672 C CB . ASP A 445 ? 0.5000 0.5470 0.4318 -0.0123 0.0086 0.0401 461 ASP A CB 3673 C CG . ASP A 445 ? 0.5508 0.6016 0.4889 -0.0136 0.0096 0.0386 461 ASP A CG 3674 O OD1 . ASP A 445 ? 0.5684 0.6176 0.5102 -0.0145 0.0083 0.0382 461 ASP A OD1 3675 O OD2 . ASP A 445 ? 0.5881 0.6436 0.5275 -0.0137 0.0115 0.0374 461 ASP A OD2 3676 N N . LYS A 446 ? 0.4267 0.4618 0.3507 -0.0103 0.0034 0.0430 462 LYS A N 3677 C CA . LYS A 446 ? 0.4414 0.4724 0.3598 -0.0090 0.0018 0.0444 462 LYS A CA 3678 C C . LYS A 446 ? 0.4266 0.4590 0.3394 -0.0084 0.0036 0.0453 462 LYS A C 3679 O O . LYS A 446 ? 0.4302 0.4612 0.3390 -0.0065 0.0022 0.0450 462 LYS A O 3680 C CB . LYS A 446 ? 0.4744 0.4998 0.3914 -0.0101 0.0005 0.0470 462 LYS A CB 3681 C CG . LYS A 446 ? 0.5023 0.5245 0.4223 -0.0092 -0.0028 0.0459 462 LYS A CG 3682 C CD . LYS A 446 ? 0.5428 0.5590 0.4613 -0.0101 -0.0043 0.0486 462 LYS A CD 3683 C CE . LYS A 446 ? 0.5751 0.5914 0.4979 -0.0127 -0.0027 0.0496 462 LYS A CE 3684 N NZ . LYS A 446 ? 0.6253 0.6357 0.5484 -0.0134 -0.0047 0.0517 462 LYS A NZ 3685 N N . ALA A 447 ? 0.4076 0.4431 0.3206 -0.0100 0.0067 0.0460 463 ALA A N 3686 C CA . ALA A 447 ? 0.3914 0.4291 0.2998 -0.0097 0.0090 0.0464 463 ALA A CA 3687 C C . ALA A 447 ? 0.3733 0.4147 0.2822 -0.0075 0.0087 0.0437 463 ALA A C 3688 O O . ALA A 447 ? 0.3615 0.4041 0.2664 -0.0065 0.0096 0.0436 463 ALA A O 3689 C CB . ALA A 447 ? 0.3970 0.4376 0.3069 -0.0121 0.0125 0.0473 463 ALA A CB 3690 N N . ASN A 448 ? 0.3353 0.3785 0.2493 -0.0067 0.0075 0.0414 464 ASN A N 3691 C CA . ASN A 448 ? 0.3230 0.3695 0.2380 -0.0047 0.0074 0.0389 464 ASN A CA 3692 C C . ASN A 448 ? 0.3098 0.3541 0.2251 -0.0027 0.0047 0.0374 464 ASN A C 3693 O O . ASN A 448 ? 0.2954 0.3419 0.2122 -0.0012 0.0047 0.0354 464 ASN A O 3694 C CB . ASN A 448 ? 0.3291 0.3801 0.2493 -0.0051 0.0087 0.0372 464 ASN A CB 3695 C CG . ASN A 448 ? 0.3525 0.4066 0.2735 -0.0070 0.0115 0.0380 464 ASN A CG 3696 O OD1 . ASN A 448 ? 0.3713 0.4274 0.2969 -0.0083 0.0121 0.0375 464 ASN A OD1 3697 N ND2 . ASN A 448 ? 0.3457 0.4003 0.2625 -0.0072 0.0132 0.0390 464 ASN A ND2 3698 N N . TRP A 449 ? 0.3004 0.3401 0.2145 -0.0027 0.0025 0.0384 465 TRP A N 3699 C CA . TRP A 449 ? 0.2958 0.3334 0.2114 -0.0010 0.0000 0.0367 465 TRP A CA 3700 C C . TRP A 449 ? 0.2892 0.3274 0.2027 0.0010 -0.0004 0.0351 465 TRP A C 3701 O O . TRP A 449 ? 0.2749 0.3135 0.1911 0.0023 -0.0012 0.0330 465 TRP A O 3702 C CB . TRP A 449 ? 0.3114 0.3441 0.2263 -0.0014 -0.0024 0.0379 465 TRP A CB 3703 C CG . TRP A 449 ? 0.3174 0.3493 0.2368 -0.0029 -0.0028 0.0381 465 TRP A CG 3704 C CD1 . TRP A 449 ? 0.3129 0.3480 0.2361 -0.0043 -0.0011 0.0377 465 TRP A CD1 3705 C CD2 . TRP A 449 ? 0.3205 0.3483 0.2414 -0.0030 -0.0054 0.0383 465 TRP A CD2 3706 N NE1 . TRP A 449 ? 0.3213 0.3545 0.2482 -0.0054 -0.0023 0.0377 465 TRP A NE1 3707 C CE2 . TRP A 449 ? 0.3241 0.3528 0.2498 -0.0047 -0.0049 0.0381 465 TRP A CE2 3708 C CE3 . TRP A 449 ? 0.3285 0.3520 0.2475 -0.0018 -0.0082 0.0385 465 TRP A CE3 3709 C CZ2 . TRP A 449 ? 0.3255 0.3510 0.2543 -0.0052 -0.0070 0.0381 465 TRP A CZ2 3710 C CZ3 . TRP A 449 ? 0.3351 0.3553 0.2571 -0.0023 -0.0104 0.0386 465 TRP A CZ3 3711 C CH2 . TRP A 449 ? 0.3280 0.3492 0.2549 -0.0040 -0.0097 0.0383 465 TRP A CH2 3712 N N . ASN A 450 ? 0.2793 0.3174 0.1879 0.0015 0.0000 0.0360 466 ASN A N 3713 C CA . ASN A 450 ? 0.2808 0.3194 0.1878 0.0037 -0.0005 0.0341 466 ASN A CA 3714 C C . ASN A 450 ? 0.2715 0.3144 0.1807 0.0043 0.0014 0.0324 466 ASN A C 3715 O O . ASN A 450 ? 0.2705 0.3138 0.1815 0.0059 0.0007 0.0303 466 ASN A O 3716 C CB . ASN A 450 ? 0.2796 0.3169 0.1805 0.0044 -0.0009 0.0351 466 ASN A CB 3717 C CG . ASN A 450 ? 0.2860 0.3225 0.1862 0.0068 -0.0028 0.0328 466 ASN A CG 3718 O OD1 . ASN A 450 ? 0.2778 0.3125 0.1813 0.0076 -0.0049 0.0313 466 ASN A OD1 3719 N ND2 . ASN A 450 ? 0.2818 0.3198 0.1781 0.0079 -0.0021 0.0323 466 ASN A ND2 3720 N N . CYS A 451 ? 0.2753 0.3214 0.1846 0.0032 0.0038 0.0332 467 CYS A N 3721 C CA . CYS A 451 ? 0.2765 0.3265 0.1875 0.0041 0.0054 0.0316 467 CYS A CA 3722 C C . CYS A 451 ? 0.2621 0.3130 0.1781 0.0042 0.0052 0.0304 467 CYS A C 3723 O O . CYS A 451 ? 0.2568 0.3096 0.1744 0.0055 0.0057 0.0288 467 CYS A O 3724 C CB . CYS A 451 ? 0.3034 0.3569 0.2131 0.0031 0.0080 0.0323 467 CYS A CB 3725 S SG . CYS A 451 ? 0.3624 0.4156 0.2657 0.0037 0.0086 0.0329 467 CYS A SG 3726 N N . ALA A 452 ? 0.2553 0.3045 0.1734 0.0030 0.0042 0.0311 468 ALA A N 3727 C CA . ALA A 452 ? 0.2481 0.2977 0.1703 0.0033 0.0038 0.0298 468 ALA A CA 3728 C C . ALA A 452 ? 0.2417 0.2892 0.1647 0.0049 0.0026 0.0282 468 ALA A C 3729 O O . ALA A 452 ? 0.2381 0.2866 0.1635 0.0057 0.0030 0.0269 468 ALA A O 3730 C CB . ALA A 452 ? 0.2476 0.2958 0.1719 0.0016 0.0031 0.0307 468 ALA A CB 3731 N N . PHE A 453 ? 0.2418 0.2864 0.1630 0.0054 0.0010 0.0282 469 PHE A N 3732 C CA . PHE A 453 ? 0.2378 0.2806 0.1601 0.0070 -0.0001 0.0263 469 PHE A CA 3733 C C . PHE A 453 ? 0.2366 0.2816 0.1586 0.0085 0.0012 0.0250 469 PHE A C 3734 O O . PHE A 453 ? 0.2254 0.2706 0.1500 0.0093 0.0017 0.0236 469 PHE A O 3735 C CB . PHE A 453 ? 0.2387 0.2782 0.1587 0.0074 -0.0023 0.0264 469 PHE A CB 3736 C CG . PHE A 453 ? 0.2417 0.2795 0.1636 0.0090 -0.0036 0.0241 469 PHE A CG 3737 C CD1 . PHE A 453 ? 0.2344 0.2707 0.1604 0.0089 -0.0044 0.0228 469 PHE A CD1 3738 C CD2 . PHE A 453 ? 0.2394 0.2773 0.1594 0.0105 -0.0040 0.0229 469 PHE A CD2 3739 C CE1 . PHE A 453 ? 0.2391 0.2739 0.1675 0.0101 -0.0054 0.0204 469 PHE A CE1 3740 C CE2 . PHE A 453 ? 0.2415 0.2780 0.1641 0.0118 -0.0052 0.0204 469 PHE A CE2 3741 C CZ . PHE A 453 ? 0.2414 0.2763 0.1683 0.0116 -0.0058 0.0191 469 PHE A CZ 3742 N N . TRP A 454 ? 0.2387 0.2850 0.1575 0.0088 0.0018 0.0255 470 TRP A N 3743 C CA . TRP A 454 ? 0.2433 0.2916 0.1619 0.0103 0.0029 0.0241 470 TRP A CA 3744 C C . TRP A 454 ? 0.2484 0.2997 0.1693 0.0104 0.0048 0.0239 470 TRP A C 3745 O O . TRP A 454 ? 0.2398 0.2917 0.1621 0.0118 0.0054 0.0225 470 TRP A O 3746 C CB . TRP A 454 ? 0.2434 0.2927 0.1579 0.0106 0.0031 0.0245 470 TRP A CB 3747 C CG . TRP A 454 ? 0.2463 0.2925 0.1586 0.0113 0.0009 0.0240 470 TRP A CG 3748 C CD1 . TRP A 454 ? 0.2460 0.2907 0.1541 0.0107 0.0000 0.0256 470 TRP A CD1 3749 C CD2 . TRP A 454 ? 0.2455 0.2899 0.1597 0.0128 -0.0006 0.0218 470 TRP A CD2 3750 N NE1 . TRP A 454 ? 0.2466 0.2885 0.1537 0.0119 -0.0025 0.0245 470 TRP A NE1 3751 C CE2 . TRP A 454 ? 0.2465 0.2885 0.1576 0.0132 -0.0028 0.0219 470 TRP A CE2 3752 C CE3 . TRP A 454 ? 0.2424 0.2869 0.1607 0.0138 -0.0002 0.0197 470 TRP A CE3 3753 C CZ2 . TRP A 454 ? 0.2467 0.2866 0.1593 0.0147 -0.0050 0.0197 470 TRP A CZ2 3754 C CZ3 . TRP A 454 ? 0.2430 0.2854 0.1630 0.0150 -0.0019 0.0175 470 TRP A CZ3 3755 C CH2 . TRP A 454 ? 0.2476 0.2879 0.1649 0.0155 -0.0044 0.0173 470 TRP A CH2 3756 N N . LYS A 455 ? 0.2544 0.3073 0.1757 0.0090 0.0055 0.0252 471 LYS A N 3757 C CA . LYS A 455 ? 0.2629 0.3185 0.1864 0.0093 0.0068 0.0249 471 LYS A CA 3758 C C . LYS A 455 ? 0.2510 0.3049 0.1769 0.0102 0.0065 0.0239 471 LYS A C 3759 O O . LYS A 455 ? 0.2424 0.2975 0.1693 0.0115 0.0074 0.0232 471 LYS A O 3760 C CB . LYS A 455 ? 0.2877 0.3452 0.2118 0.0077 0.0073 0.0261 471 LYS A CB 3761 C CG . LYS A 455 ? 0.3280 0.3882 0.2505 0.0069 0.0086 0.0268 471 LYS A CG 3762 C CD . LYS A 455 ? 0.3630 0.4246 0.2868 0.0049 0.0091 0.0279 471 LYS A CD 3763 C CE . LYS A 455 ? 0.4123 0.4755 0.3340 0.0036 0.0106 0.0290 471 LYS A CE 3764 N NZ . LYS A 455 ? 0.4396 0.5071 0.3620 0.0043 0.0123 0.0279 471 LYS A NZ 3765 N N . LEU A 456 ? 0.2462 0.2974 0.1731 0.0095 0.0053 0.0239 472 LEU A N 3766 C CA . LEU A 456 ? 0.2381 0.2876 0.1672 0.0102 0.0052 0.0229 472 LEU A CA 3767 C C . LEU A 456 ? 0.2325 0.2805 0.1619 0.0117 0.0055 0.0215 472 LEU A C 3768 O O . LEU A 456 ? 0.2201 0.2679 0.1507 0.0127 0.0065 0.0209 472 LEU A O 3769 C CB . LEU A 456 ? 0.2453 0.2923 0.1756 0.0091 0.0039 0.0229 472 LEU A CB 3770 C CG . LEU A 456 ? 0.2504 0.2985 0.1814 0.0076 0.0037 0.0239 472 LEU A CG 3771 C CD1 . LEU A 456 ? 0.2513 0.2966 0.1835 0.0066 0.0020 0.0238 472 LEU A CD1 3772 C CD2 . LEU A 456 ? 0.2495 0.2990 0.1818 0.0081 0.0046 0.0234 472 LEU A CD2 3773 N N . ARG A 457 ? 0.2230 0.2699 0.1514 0.0119 0.0045 0.0210 473 ARG A N 3774 C CA . ARG A 457 ? 0.2251 0.2708 0.1545 0.0133 0.0046 0.0193 473 ARG A CA 3775 C C . ARG A 457 ? 0.2257 0.2735 0.1550 0.0145 0.0063 0.0190 473 ARG A C 3776 O O . ARG A 457 ? 0.2280 0.2747 0.1592 0.0156 0.0071 0.0178 473 ARG A O 3777 C CB . ARG A 457 ? 0.2254 0.2701 0.1532 0.0135 0.0030 0.0187 473 ARG A CB 3778 C CG . ARG A 457 ? 0.2357 0.2779 0.1636 0.0126 0.0010 0.0190 473 ARG A CG 3779 C CD . ARG A 457 ? 0.2369 0.2768 0.1687 0.0126 0.0007 0.0175 473 ARG A CD 3780 N NE . ARG A 457 ? 0.2432 0.2823 0.1770 0.0140 0.0007 0.0152 473 ARG A NE 3781 C CZ . ARG A 457 ? 0.2529 0.2917 0.1893 0.0146 0.0024 0.0141 473 ARG A CZ 3782 N NH1 . ARG A 457 ? 0.2405 0.2797 0.1774 0.0141 0.0041 0.0151 473 ARG A NH1 3783 N NH2 . ARG A 457 ? 0.2538 0.2918 0.1923 0.0157 0.0024 0.0119 473 ARG A NH2 3784 N N . ASP A 458 ? 0.2303 0.2810 0.1578 0.0143 0.0068 0.0200 474 ASP A N 3785 C CA . ASP A 458 ? 0.2445 0.2977 0.1720 0.0155 0.0082 0.0197 474 ASP A CA 3786 C C . ASP A 458 ? 0.2532 0.3062 0.1822 0.0160 0.0091 0.0200 474 ASP A C 3787 O O . ASP A 458 ? 0.2476 0.2996 0.1779 0.0173 0.0099 0.0193 474 ASP A O 3788 C CB . ASP A 458 ? 0.2620 0.3184 0.1873 0.0148 0.0086 0.0206 474 ASP A CB 3789 C CG . ASP A 458 ? 0.2749 0.3345 0.2009 0.0159 0.0099 0.0202 474 ASP A CG 3790 O OD1 . ASP A 458 ? 0.2929 0.3519 0.2205 0.0172 0.0104 0.0195 474 ASP A OD1 3791 O OD2 . ASP A 458 ? 0.2851 0.3476 0.2099 0.0153 0.0105 0.0205 474 ASP A OD2 3792 N N . GLU A 459 ? 0.2640 0.3180 0.1928 0.0149 0.0089 0.0212 475 GLU A N 3793 C CA . GLU A 459 ? 0.2759 0.3302 0.2054 0.0155 0.0095 0.0215 475 GLU A CA 3794 C C . GLU A 459 ? 0.2720 0.3230 0.2026 0.0162 0.0100 0.0210 475 GLU A C 3795 O O . GLU A 459 ? 0.2745 0.3252 0.2052 0.0175 0.0109 0.0211 475 GLU A O 3796 C CB . GLU A 459 ? 0.3140 0.3695 0.2435 0.0140 0.0089 0.0224 475 GLU A CB 3797 C CG . GLU A 459 ? 0.3878 0.4436 0.3177 0.0146 0.0091 0.0226 475 GLU A CG 3798 C CD . GLU A 459 ? 0.4491 0.5062 0.3796 0.0131 0.0083 0.0231 475 GLU A CD 3799 O OE1 . GLU A 459 ? 0.4804 0.5382 0.4111 0.0115 0.0078 0.0235 475 GLU A OE1 3800 O OE2 . GLU A 459 ? 0.4908 0.5481 0.4214 0.0136 0.0083 0.0230 475 GLU A OE2 3801 N N . TYR A 460 ? 0.2517 0.3001 0.1832 0.0154 0.0094 0.0205 476 TYR A N 3802 C CA . TYR A 460 ? 0.2554 0.3007 0.1883 0.0158 0.0102 0.0199 476 TYR A CA 3803 C C . TYR A 460 ? 0.2515 0.2949 0.1859 0.0168 0.0108 0.0185 476 TYR A C 3804 O O . TYR A 460 ? 0.2520 0.2936 0.1872 0.0177 0.0123 0.0183 476 TYR A O 3805 C CB . TYR A 460 ? 0.2554 0.2991 0.1893 0.0144 0.0094 0.0196 476 TYR A CB 3806 C CG . TYR A 460 ? 0.2505 0.2956 0.1836 0.0137 0.0092 0.0206 476 TYR A CG 3807 C CD1 . TYR A 460 ? 0.2496 0.2970 0.1820 0.0127 0.0081 0.0214 476 TYR A CD1 3808 C CD2 . TYR A 460 ? 0.2599 0.3038 0.1928 0.0141 0.0102 0.0207 476 TYR A CD2 3809 C CE1 . TYR A 460 ? 0.2554 0.3043 0.1877 0.0121 0.0078 0.0219 476 TYR A CE1 3810 C CE2 . TYR A 460 ? 0.2674 0.3129 0.1996 0.0137 0.0098 0.0212 476 TYR A CE2 3811 C CZ . TYR A 460 ? 0.2653 0.3134 0.1975 0.0126 0.0085 0.0217 476 TYR A CZ 3812 O OH . TYR A 460 ? 0.2641 0.3140 0.1962 0.0122 0.0080 0.0219 476 TYR A OH 3813 N N . SER A 461 ? 0.2489 0.2926 0.1836 0.0167 0.0098 0.0176 477 SER A N 3814 C CA . SER A 461 ? 0.2492 0.2911 0.1860 0.0176 0.0102 0.0158 477 SER A CA 3815 C C . SER A 461 ? 0.2450 0.2886 0.1813 0.0188 0.0105 0.0153 477 SER A C 3816 O O . SER A 461 ? 0.2458 0.2882 0.1843 0.0198 0.0111 0.0137 477 SER A O 3817 C CB . SER A 461 ? 0.2538 0.2944 0.1917 0.0169 0.0085 0.0144 477 SER A CB 3818 O OG . SER A 461 ? 0.2650 0.3035 0.2047 0.0160 0.0084 0.0141 477 SER A OG 3819 N N . GLY A 462 ? 0.2414 0.2882 0.1754 0.0188 0.0102 0.0163 478 GLY A N 3820 C CA . GLY A 462 ? 0.2377 0.2864 0.1714 0.0201 0.0107 0.0156 478 GLY A CA 3821 C C . GLY A 462 ? 0.2356 0.2843 0.1695 0.0203 0.0097 0.0138 478 GLY A C 3822 O O . GLY A 462 ? 0.2328 0.2818 0.1680 0.0216 0.0102 0.0122 478 GLY A O 3823 N N . ILE A 463 ? 0.2362 0.2843 0.1688 0.0193 0.0082 0.0139 479 ILE A N 3824 C CA . ILE A 463 ? 0.2322 0.2804 0.1641 0.0196 0.0068 0.0124 479 ILE A CA 3825 C C . ILE A 463 ? 0.2348 0.2848 0.1626 0.0187 0.0060 0.0138 479 ILE A C 3826 O O . ILE A 463 ? 0.2329 0.2837 0.1595 0.0175 0.0063 0.0157 479 ILE A O 3827 C CB . ILE A 463 ? 0.2360 0.2811 0.1703 0.0196 0.0056 0.0108 479 ILE A CB 3828 C CG1 . ILE A 463 ? 0.2340 0.2777 0.1678 0.0181 0.0046 0.0122 479 ILE A CG1 3829 C CG2 . ILE A 463 ? 0.2302 0.2734 0.1688 0.0203 0.0070 0.0094 479 ILE A CG2 3830 C CD1 . ILE A 463 ? 0.2340 0.2779 0.1644 0.0175 0.0026 0.0130 479 ILE A CD1 3831 N N . GLU A 464 ? 0.2381 0.2887 0.1638 0.0193 0.0049 0.0128 480 GLU A N 3832 C CA . GLU A 464 ? 0.2453 0.2973 0.1667 0.0184 0.0044 0.0143 480 GLU A CA 3833 C C . GLU A 464 ? 0.2488 0.2996 0.1678 0.0191 0.0024 0.0130 480 GLU A C 3834 O O . GLU A 464 ? 0.2509 0.3010 0.1721 0.0205 0.0017 0.0105 480 GLU A O 3835 C CB . GLU A 464 ? 0.2520 0.3076 0.1717 0.0185 0.0061 0.0147 480 GLU A CB 3836 C CG . GLU A 464 ? 0.2636 0.3208 0.1837 0.0202 0.0064 0.0123 480 GLU A CG 3837 C CD . GLU A 464 ? 0.2746 0.3355 0.1936 0.0203 0.0082 0.0125 480 GLU A CD 3838 O OE1 . GLU A 464 ? 0.2772 0.3397 0.1964 0.0193 0.0094 0.0141 480 GLU A OE1 3839 O OE2 . GLU A 464 ? 0.2816 0.3443 0.1999 0.0214 0.0084 0.0106 480 GLU A OE2 3840 N N . PRO A 465 ? 0.2538 0.3043 0.1685 0.0183 0.0014 0.0146 481 PRO A N 3841 C CA . PRO A 465 ? 0.2594 0.3088 0.1707 0.0192 -0.0005 0.0136 481 PRO A CA 3842 C C . PRO A 465 ? 0.2693 0.3213 0.1792 0.0207 0.0000 0.0116 481 PRO A C 3843 O O . PRO A 465 ? 0.2737 0.3285 0.1839 0.0205 0.0021 0.0117 481 PRO A O 3844 C CB . PRO A 465 ? 0.2616 0.3105 0.1678 0.0178 -0.0008 0.0165 481 PRO A CB 3845 C CG . PRO A 465 ? 0.2612 0.3097 0.1699 0.0161 0.0001 0.0185 481 PRO A CG 3846 C CD . PRO A 465 ? 0.2522 0.3030 0.1647 0.0164 0.0021 0.0175 481 PRO A CD 3847 N N . PRO A 466 ? 0.2710 0.3220 0.1796 0.0221 -0.0021 0.0094 482 PRO A N 3848 C CA . PRO A 466 ? 0.2788 0.3320 0.1859 0.0237 -0.0020 0.0070 482 PRO A CA 3849 C C . PRO A 466 ? 0.2958 0.3511 0.1963 0.0233 -0.0011 0.0086 482 PRO A C 3850 O O . PRO A 466 ? 0.3004 0.3587 0.2001 0.0242 0.0000 0.0069 482 PRO A O 3851 C CB . PRO A 466 ? 0.2746 0.3257 0.1820 0.0253 -0.0051 0.0045 482 PRO A CB 3852 C CG . PRO A 466 ? 0.2721 0.3200 0.1779 0.0244 -0.0070 0.0066 482 PRO A CG 3853 C CD . PRO A 466 ? 0.2683 0.3159 0.1777 0.0226 -0.0050 0.0087 482 PRO A CD 3854 N N . VAL A 467 ? 0.3038 0.3575 0.1999 0.0219 -0.0014 0.0117 483 VAL A N 3855 C CA . VAL A 467 ? 0.3105 0.3655 0.2000 0.0211 -0.0002 0.0137 483 VAL A CA 3856 C C . VAL A 467 ? 0.3093 0.3643 0.1988 0.0187 0.0016 0.0171 483 VAL A C 3857 O O . VAL A 467 ? 0.2995 0.3528 0.1929 0.0179 0.0012 0.0180 483 VAL A O 3858 C CB . VAL A 467 ? 0.3200 0.3723 0.2033 0.0219 -0.0029 0.0142 483 VAL A CB 3859 C CG1 . VAL A 467 ? 0.3289 0.3816 0.2119 0.0245 -0.0050 0.0105 483 VAL A CG1 3860 C CG2 . VAL A 467 ? 0.3170 0.3650 0.2012 0.0213 -0.0052 0.0159 483 VAL A CG2 3861 N N . VAL A 468 ? 0.3058 0.3630 0.1912 0.0177 0.0039 0.0187 484 VAL A N 3862 C CA . VAL A 468 ? 0.3022 0.3597 0.1876 0.0153 0.0059 0.0217 484 VAL A CA 3863 C C . VAL A 468 ? 0.3035 0.3567 0.1861 0.0142 0.0041 0.0244 484 VAL A C 3864 O O . VAL A 468 ? 0.3108 0.3618 0.1875 0.0147 0.0028 0.0252 484 VAL A O 3865 C CB . VAL A 468 ? 0.3078 0.3687 0.1898 0.0143 0.0090 0.0225 484 VAL A CB 3866 C CG1 . VAL A 468 ? 0.3047 0.3659 0.1876 0.0117 0.0110 0.0253 484 VAL A CG1 3867 C CG2 . VAL A 468 ? 0.3043 0.3696 0.1895 0.0154 0.0106 0.0197 484 VAL A CG2 3868 N N . ARG A 469 ? 0.2873 0.3392 0.1741 0.0130 0.0040 0.0256 485 ARG A N 3869 C CA . ARG A 469 ? 0.2860 0.3341 0.1713 0.0117 0.0026 0.0282 485 ARG A CA 3870 C C . ARG A 469 ? 0.2802 0.3295 0.1654 0.0092 0.0052 0.0308 485 ARG A C 3871 O O . ARG A 469 ? 0.2782 0.3314 0.1654 0.0086 0.0078 0.0303 485 ARG A O 3872 C CB . ARG A 469 ? 0.2759 0.3217 0.1667 0.0120 0.0005 0.0273 485 ARG A CB 3873 C CG . ARG A 469 ? 0.2746 0.3196 0.1674 0.0143 -0.0017 0.0242 485 ARG A CG 3874 C CD . ARG A 469 ? 0.2877 0.3302 0.1752 0.0157 -0.0042 0.0239 485 ARG A CD 3875 N NE . ARG A 469 ? 0.2951 0.3334 0.1824 0.0157 -0.0071 0.0248 485 ARG A NE 3876 C CZ . ARG A 469 ? 0.3108 0.3463 0.1935 0.0170 -0.0099 0.0249 485 ARG A CZ 3877 N NH1 . ARG A 469 ? 0.3128 0.3493 0.1903 0.0184 -0.0100 0.0241 485 ARG A NH1 3878 N NH2 . ARG A 469 ? 0.3190 0.3506 0.2022 0.0172 -0.0127 0.0255 485 ARG A NH2 3879 N N . SER A 470 ? 0.2844 0.3303 0.1677 0.0078 0.0045 0.0334 486 SER A N 3880 C CA . SER A 470 ? 0.2896 0.3362 0.1732 0.0053 0.0069 0.0359 486 SER A CA 3881 C C . SER A 470 ? 0.2948 0.3371 0.1790 0.0043 0.0050 0.0379 486 SER A C 3882 O O . SER A 470 ? 0.2945 0.3336 0.1790 0.0056 0.0020 0.0372 486 SER A O 3883 C CB . SER A 470 ? 0.3030 0.3500 0.1801 0.0045 0.0091 0.0377 486 SER A CB 3884 O OG . SER A 470 ? 0.3151 0.3572 0.1867 0.0046 0.0071 0.0399 486 SER A OG 3885 N N . GLU A 471 ? 0.3129 0.3551 0.1976 0.0019 0.0069 0.0402 487 GLU A N 3886 C CA . GLU A 471 ? 0.3340 0.3721 0.2198 0.0007 0.0053 0.0421 487 GLU A CA 3887 C C . GLU A 471 ? 0.3527 0.3856 0.2321 0.0012 0.0033 0.0443 487 GLU A C 3888 O O . GLU A 471 ? 0.3601 0.3890 0.2401 0.0005 0.0016 0.0459 487 GLU A O 3889 C CB . GLU A 471 ? 0.3374 0.3770 0.2263 -0.0019 0.0079 0.0437 487 GLU A CB 3890 C CG . GLU A 471 ? 0.3457 0.3898 0.2414 -0.0021 0.0090 0.0414 487 GLU A CG 3891 C CD . GLU A 471 ? 0.3474 0.3904 0.2478 -0.0010 0.0064 0.0397 487 GLU A CD 3892 O OE1 . GLU A 471 ? 0.3511 0.3898 0.2508 -0.0006 0.0038 0.0404 487 GLU A OE1 3893 O OE2 . GLU A 471 ? 0.3456 0.3919 0.2505 -0.0006 0.0070 0.0377 487 GLU A OE2 3894 N N . LYS A 472 ? 0.3723 0.4051 0.2455 0.0025 0.0034 0.0443 488 LYS A N 3895 C CA . LYS A 472 ? 0.3938 0.4217 0.2605 0.0037 0.0008 0.0458 488 LYS A CA 3896 C C . LYS A 472 ? 0.3800 0.4060 0.2486 0.0063 -0.0033 0.0434 488 LYS A C 3897 O O . LYS A 472 ? 0.3854 0.4070 0.2501 0.0074 -0.0063 0.0444 488 LYS A O 3898 C CB . LYS A 472 ? 0.4273 0.4559 0.2861 0.0043 0.0023 0.0466 488 LYS A CB 3899 C CG . LYS A 472 ? 0.4769 0.5063 0.3329 0.0017 0.0065 0.0495 488 LYS A CG 3900 C CD . LYS A 472 ? 0.5207 0.5515 0.3691 0.0023 0.0085 0.0497 488 LYS A CD 3901 C CE . LYS A 472 ? 0.5652 0.5983 0.4128 -0.0005 0.0134 0.0516 488 LYS A CE 3902 N NZ . LYS A 472 ? 0.6001 0.6359 0.4415 0.0000 0.0159 0.0512 488 LYS A NZ 3903 N N . ASP A 473 ? 0.3585 0.3878 0.2331 0.0071 -0.0034 0.0401 489 ASP A N 3904 C CA . ASP A 473 ? 0.3409 0.3687 0.2187 0.0092 -0.0069 0.0376 489 ASP A CA 3905 C C . ASP A 473 ? 0.3258 0.3528 0.2104 0.0081 -0.0076 0.0373 489 ASP A C 3906 O O . ASP A 473 ? 0.3175 0.3462 0.2049 0.0061 -0.0052 0.0384 489 ASP A O 3907 C CB . ASP A 473 ? 0.3441 0.3756 0.2240 0.0109 -0.0066 0.0341 489 ASP A CB 3908 C CG . ASP A 473 ? 0.3543 0.3878 0.2282 0.0116 -0.0051 0.0341 489 ASP A CG 3909 O OD1 . ASP A 473 ? 0.3577 0.3886 0.2254 0.0129 -0.0070 0.0347 489 ASP A OD1 3910 O OD2 . ASP A 473 ? 0.3512 0.3889 0.2265 0.0110 -0.0021 0.0334 489 ASP A OD2 3911 N N . PHE A 474 ? 0.3094 0.3341 0.1968 0.0095 -0.0108 0.0355 490 PHE A N 3912 C CA . PHE A 474 ? 0.2948 0.3192 0.1891 0.0087 -0.0113 0.0345 490 PHE A CA 3913 C C . PHE A 474 ? 0.2849 0.3094 0.1834 0.0106 -0.0133 0.0310 490 PHE A C 3914 O O . PHE A 474 ? 0.2777 0.2992 0.1761 0.0119 -0.0166 0.0301 490 PHE A O 3915 C CB . PHE A 474 ? 0.2989 0.3192 0.1931 0.0076 -0.0129 0.0369 490 PHE A CB 3916 C CG . PHE A 474 ? 0.2980 0.3187 0.1990 0.0063 -0.0127 0.0361 490 PHE A CG 3917 C CD1 . PHE A 474 ? 0.2980 0.3221 0.2020 0.0046 -0.0097 0.0364 490 PHE A CD1 3918 C CD2 . PHE A 474 ? 0.2960 0.3139 0.2007 0.0070 -0.0157 0.0347 490 PHE A CD2 3919 C CE1 . PHE A 474 ? 0.2945 0.3192 0.2044 0.0036 -0.0096 0.0354 490 PHE A CE1 3920 C CE2 . PHE A 474 ? 0.2986 0.3172 0.2096 0.0059 -0.0153 0.0337 490 PHE A CE2 3921 C CZ . PHE A 474 ? 0.2910 0.3130 0.2042 0.0042 -0.0123 0.0341 490 PHE A CZ 3922 N N . ASP A 475 ? 0.2783 0.3064 0.1809 0.0107 -0.0114 0.0289 491 ASP A N 3923 C CA . ASP A 475 ? 0.2706 0.2993 0.1764 0.0125 -0.0125 0.0255 491 ASP A CA 3924 C C . ASP A 475 ? 0.2662 0.2940 0.1785 0.0125 -0.0134 0.0235 491 ASP A C 3925 O O . ASP A 475 ? 0.2639 0.2912 0.1792 0.0139 -0.0149 0.0207 491 ASP A O 3926 C CB . ASP A 475 ? 0.2681 0.3007 0.1739 0.0130 -0.0099 0.0243 491 ASP A CB 3927 C CG . ASP A 475 ? 0.2796 0.3131 0.1791 0.0137 -0.0095 0.0252 491 ASP A CG 3928 O OD1 . ASP A 475 ? 0.2924 0.3237 0.1886 0.0151 -0.0121 0.0248 491 ASP A OD1 3929 O OD2 . ASP A 475 ? 0.2816 0.3180 0.1794 0.0128 -0.0068 0.0263 491 ASP A OD2 3930 N N . ALA A 476 ? 0.2566 0.2845 0.1716 0.0108 -0.0123 0.0247 492 ALA A N 3931 C CA . ALA A 476 ? 0.2498 0.2772 0.1708 0.0106 -0.0127 0.0228 492 ALA A CA 3932 C C . ALA A 476 ? 0.2503 0.2745 0.1734 0.0116 -0.0160 0.0210 492 ALA A C 3933 O O . ALA A 476 ? 0.2479 0.2723 0.1755 0.0125 -0.0163 0.0181 492 ALA A O 3934 C CB . ALA A 476 ? 0.2454 0.2734 0.1684 0.0086 -0.0113 0.0243 492 ALA A CB 3935 N N . PRO A 477 ? 0.2559 0.2771 0.1759 0.0118 -0.0186 0.0226 493 PRO A N 3936 C CA . PRO A 477 ? 0.2573 0.2755 0.1799 0.0130 -0.0221 0.0206 493 PRO A CA 3937 C C . PRO A 477 ? 0.2596 0.2779 0.1823 0.0153 -0.0238 0.0176 493 PRO A C 3938 O O . PRO A 477 ? 0.2628 0.2791 0.1884 0.0165 -0.0268 0.0154 493 PRO A O 3939 C CB . PRO A 477 ? 0.2603 0.2751 0.1787 0.0127 -0.0243 0.0235 493 PRO A CB 3940 C CG . PRO A 477 ? 0.2565 0.2725 0.1724 0.0107 -0.0215 0.0267 493 PRO A CG 3941 C CD . PRO A 477 ? 0.2570 0.2769 0.1719 0.0106 -0.0184 0.0263 493 PRO A CD 3942 N N . ALA A 478 ? 0.2616 0.2826 0.1823 0.0159 -0.0219 0.0172 494 ALA A N 3943 C CA . ALA A 478 ? 0.2676 0.2890 0.1891 0.0179 -0.0233 0.0140 494 ALA A CA 3944 C C . ALA A 478 ? 0.2683 0.2907 0.1975 0.0181 -0.0225 0.0105 494 ALA A C 3945 O O . ALA A 478 ? 0.2740 0.2965 0.2058 0.0197 -0.0238 0.0072 494 ALA A O 3946 C CB . ALA A 478 ? 0.2719 0.2957 0.1888 0.0186 -0.0217 0.0145 494 ALA A CB 3947 N N . LYS A 479 ? 0.2586 0.2815 0.1913 0.0164 -0.0203 0.0111 495 LYS A N 3948 C CA . LYS A 479 ? 0.2608 0.2841 0.2006 0.0162 -0.0194 0.0081 495 LYS A CA 3949 C C . LYS A 479 ? 0.2564 0.2772 0.1998 0.0160 -0.0220 0.0071 495 LYS A C 3950 O O . LYS A 479 ? 0.2541 0.2737 0.1958 0.0149 -0.0225 0.0095 495 LYS A O 3951 C CB . LYS A 479 ? 0.2567 0.2820 0.1977 0.0147 -0.0156 0.0093 495 LYS A CB 3952 C CG . LYS A 479 ? 0.2634 0.2888 0.2108 0.0143 -0.0140 0.0067 495 LYS A CG 3953 C CD . LYS A 479 ? 0.2691 0.2948 0.2198 0.0155 -0.0135 0.0035 495 LYS A CD 3954 C CE . LYS A 479 ? 0.2725 0.2978 0.2298 0.0150 -0.0121 0.0008 495 LYS A CE 3955 N NZ . LYS A 479 ? 0.2778 0.3027 0.2397 0.0162 -0.0128 -0.0029 495 LYS A NZ 3956 N N . TYR A 480 ? 0.2528 0.2729 0.2015 0.0170 -0.0234 0.0034 496 TYR A N 3957 C CA . TYR A 480 ? 0.2501 0.2679 0.2028 0.0172 -0.0264 0.0018 496 TYR A CA 3958 C C . TYR A 480 ? 0.2481 0.2654 0.2025 0.0153 -0.0253 0.0033 496 TYR A C 3959 O O . TYR A 480 ? 0.2490 0.2643 0.2023 0.0152 -0.0277 0.0047 496 TYR A O 3960 C CB . TYR A 480 ? 0.2526 0.2705 0.2125 0.0183 -0.0272 -0.0030 496 TYR A CB 3961 C CG . TYR A 480 ? 0.2563 0.2723 0.2213 0.0183 -0.0299 -0.0050 496 TYR A CG 3962 C CD1 . TYR A 480 ? 0.2622 0.2758 0.2258 0.0199 -0.0346 -0.0053 496 TYR A CD1 3963 C CD2 . TYR A 480 ? 0.2555 0.2720 0.2265 0.0169 -0.0278 -0.0065 496 TYR A CD2 3964 C CE1 . TYR A 480 ? 0.2670 0.2788 0.2355 0.0201 -0.0373 -0.0073 496 TYR A CE1 3965 C CE2 . TYR A 480 ? 0.2619 0.2768 0.2379 0.0169 -0.0302 -0.0087 496 TYR A CE2 3966 C CZ . TYR A 480 ? 0.2698 0.2824 0.2448 0.0186 -0.0350 -0.0090 496 TYR A CZ 3967 O OH . TYR A 480 ? 0.2813 0.2924 0.2617 0.0187 -0.0376 -0.0113 496 TYR A OH 3968 N N . HIS A 481 ? 0.2419 0.2611 0.1990 0.0140 -0.0217 0.0029 497 HIS A N 3969 C CA . HIS A 481 ? 0.2402 0.2594 0.1995 0.0124 -0.0204 0.0037 497 HIS A CA 3970 C C . HIS A 481 ? 0.2446 0.2635 0.1991 0.0113 -0.0206 0.0076 497 HIS A C 3971 O O . HIS A 481 ? 0.2515 0.2695 0.2077 0.0103 -0.0212 0.0081 497 HIS A O 3972 C CB . HIS A 481 ? 0.2356 0.2569 0.1974 0.0114 -0.0164 0.0029 497 HIS A CB 3973 C CG . HIS A 481 ? 0.2366 0.2579 0.2038 0.0121 -0.0156 -0.0008 497 HIS A CG 3974 N ND1 . HIS A 481 ? 0.2320 0.2535 0.1993 0.0135 -0.0161 -0.0024 497 HIS A ND1 3975 C CD2 . HIS A 481 ? 0.2319 0.2532 0.2050 0.0115 -0.0142 -0.0036 497 HIS A CD2 3976 C CE1 . HIS A 481 ? 0.2363 0.2579 0.2097 0.0137 -0.0150 -0.0059 497 HIS A CE1 3977 N NE2 . HIS A 481 ? 0.2329 0.2543 0.2097 0.0124 -0.0136 -0.0066 497 HIS A NE2 3978 N N . ILE A 482 ? 0.2486 0.2683 0.1974 0.0115 -0.0199 0.0101 498 ILE A N 3979 C CA . ILE A 482 ? 0.2495 0.2689 0.1938 0.0104 -0.0199 0.0138 498 ILE A CA 3980 C C . ILE A 482 ? 0.2595 0.2755 0.2020 0.0110 -0.0236 0.0148 498 ILE A C 3981 O O . ILE A 482 ? 0.2581 0.2728 0.2011 0.0099 -0.0243 0.0163 498 ILE A O 3982 C CB . ILE A 482 ? 0.2439 0.2656 0.1832 0.0102 -0.0175 0.0160 498 ILE A CB 3983 C CG1 . ILE A 482 ? 0.2428 0.2672 0.1846 0.0097 -0.0141 0.0151 498 ILE A CG1 3984 C CG2 . ILE A 482 ? 0.2408 0.2621 0.1759 0.0090 -0.0173 0.0196 498 ILE A CG2 3985 C CD1 . ILE A 482 ? 0.2456 0.2727 0.1836 0.0092 -0.0115 0.0172 498 ILE A CD1 3986 N N . SER A 483 ? 0.2722 0.2868 0.2128 0.0128 -0.0262 0.0138 499 SER A N 3987 C CA . SER A 483 ? 0.2791 0.2901 0.2183 0.0138 -0.0302 0.0144 499 SER A CA 3988 C C . SER A 483 ? 0.2831 0.2923 0.2286 0.0136 -0.0322 0.0122 499 SER A C 3989 O O . SER A 483 ? 0.2900 0.2962 0.2347 0.0135 -0.0347 0.0138 499 SER A O 3990 C CB . SER A 483 ? 0.2876 0.2975 0.2236 0.0161 -0.0328 0.0133 499 SER A CB 3991 O OG . SER A 483 ? 0.2880 0.2981 0.2165 0.0162 -0.0321 0.0163 499 SER A OG 3992 N N . ALA A 484 ? 0.2826 0.2935 0.2345 0.0136 -0.0311 0.0087 500 ALA A N 3993 C CA . ALA A 484 ? 0.2871 0.2967 0.2457 0.0137 -0.0330 0.0058 500 ALA A CA 3994 C C . ALA A 484 ? 0.2893 0.2999 0.2515 0.0116 -0.0308 0.0059 500 ALA A C 3995 O O . ALA A 484 ? 0.2824 0.2925 0.2507 0.0115 -0.0317 0.0032 500 ALA A O 3996 C CB . ALA A 484 ? 0.2875 0.2981 0.2515 0.0149 -0.0333 0.0013 500 ALA A CB 3997 N N . ASP A 485 ? 0.2838 0.2960 0.2425 0.0101 -0.0279 0.0089 501 ASP A N 3998 C CA . ASP A 485 ? 0.2851 0.2985 0.2464 0.0083 -0.0258 0.0092 501 ASP A CA 3999 C C . ASP A 485 ? 0.2813 0.2965 0.2486 0.0080 -0.0239 0.0056 501 ASP A C 4000 O O . ASP A 485 ? 0.2874 0.3021 0.2595 0.0074 -0.0245 0.0038 501 ASP A O 4001 C CB . ASP A 485 ? 0.2855 0.2963 0.2478 0.0077 -0.0284 0.0104 501 ASP A CB 4002 C CG . ASP A 485 ? 0.2947 0.3069 0.2602 0.0059 -0.0265 0.0103 501 ASP A CG 4003 O OD1 . ASP A 485 ? 0.2834 0.2985 0.2477 0.0049 -0.0232 0.0110 501 ASP A OD1 4004 O OD2 . ASP A 485 ? 0.3017 0.3120 0.2710 0.0055 -0.0286 0.0094 501 ASP A OD2 4005 N N . VAL A 486 ? 0.2761 0.2932 0.2431 0.0085 -0.0216 0.0045 502 VAL A N 4006 C CA . VAL A 486 ? 0.2694 0.2881 0.2412 0.0081 -0.0190 0.0015 502 VAL A CA 4007 C C . VAL A 486 ? 0.2663 0.2874 0.2354 0.0072 -0.0151 0.0031 502 VAL A C 4008 O O . VAL A 486 ? 0.2691 0.2912 0.2342 0.0076 -0.0139 0.0048 502 VAL A O 4009 C CB . VAL A 486 ? 0.2704 0.2888 0.2453 0.0095 -0.0195 -0.0015 502 VAL A CB 4010 C CG1 . VAL A 486 ? 0.2643 0.2840 0.2441 0.0089 -0.0163 -0.0045 502 VAL A CG1 4011 C CG2 . VAL A 486 ? 0.2766 0.2926 0.2544 0.0107 -0.0238 -0.0035 502 VAL A CG2 4012 N N . GLU A 487 ? 0.2648 0.2870 0.2362 0.0060 -0.0132 0.0025 503 GLU A N 4013 C CA . GLU A 487 ? 0.2576 0.2820 0.2265 0.0053 -0.0098 0.0038 503 GLU A CA 4014 C C . GLU A 487 ? 0.2519 0.2769 0.2204 0.0061 -0.0073 0.0029 503 GLU A C 4015 O O . GLU A 487 ? 0.2549 0.2790 0.2274 0.0066 -0.0073 0.0001 503 GLU A O 4016 C CB . GLU A 487 ? 0.2663 0.2914 0.2384 0.0042 -0.0086 0.0023 503 GLU A CB 4017 C CG . GLU A 487 ? 0.2667 0.2940 0.2359 0.0036 -0.0056 0.0036 503 GLU A CG 4018 C CD . GLU A 487 ? 0.2794 0.3071 0.2498 0.0038 -0.0023 0.0019 503 GLU A CD 4019 O OE1 . GLU A 487 ? 0.2835 0.3101 0.2562 0.0044 -0.0020 0.0001 503 GLU A OE1 4020 O OE2 . GLU A 487 ? 0.2726 0.3017 0.2414 0.0034 -0.0001 0.0023 503 GLU A OE2 4021 N N . TYR A 488 ? 0.2367 0.2631 0.2008 0.0062 -0.0054 0.0051 504 TYR A N 4022 C CA . TYR A 488 ? 0.2359 0.2626 0.1995 0.0071 -0.0032 0.0046 504 TYR A CA 4023 C C . TYR A 488 ? 0.2339 0.2615 0.1972 0.0068 0.0003 0.0045 504 TYR A C 4024 O O . TYR A 488 ? 0.2315 0.2587 0.1960 0.0073 0.0023 0.0034 504 TYR A O 4025 C CB . TYR A 488 ? 0.2378 0.2652 0.1969 0.0079 -0.0039 0.0067 504 TYR A CB 4026 C CG . TYR A 488 ? 0.2398 0.2667 0.2001 0.0091 -0.0036 0.0051 504 TYR A CG 4027 C CD1 . TYR A 488 ? 0.2333 0.2588 0.1959 0.0099 -0.0063 0.0032 504 TYR A CD1 4028 C CD2 . TYR A 488 ? 0.2351 0.2627 0.1945 0.0096 -0.0007 0.0053 504 TYR A CD2 4029 C CE1 . TYR A 488 ? 0.2374 0.2625 0.2016 0.0111 -0.0061 0.0012 504 TYR A CE1 4030 C CE2 . TYR A 488 ? 0.2340 0.2611 0.1952 0.0106 -0.0004 0.0035 504 TYR A CE2 4031 C CZ . TYR A 488 ? 0.2337 0.2597 0.1974 0.0113 -0.0031 0.0013 504 TYR A CZ 4032 O OH . TYR A 488 ? 0.2332 0.2589 0.1992 0.0124 -0.0029 -0.0007 504 TYR A OH 4033 N N . LEU A 489 ? 0.2320 0.2607 0.1940 0.0060 0.0011 0.0056 505 LEU A N 4034 C CA . LEU A 489 ? 0.2350 0.2644 0.1958 0.0058 0.0043 0.0058 505 LEU A CA 4035 C C . LEU A 489 ? 0.2393 0.2673 0.2039 0.0057 0.0064 0.0031 505 LEU A C 4036 O O . LEU A 489 ? 0.2384 0.2661 0.2017 0.0060 0.0095 0.0033 505 LEU A O 4037 C CB . LEU A 489 ? 0.2320 0.2629 0.1913 0.0051 0.0043 0.0067 505 LEU A CB 4038 C CG . LEU A 489 ? 0.2353 0.2674 0.1908 0.0055 0.0069 0.0081 505 LEU A CG 4039 C CD1 . LEU A 489 ? 0.2307 0.2642 0.1823 0.0062 0.0065 0.0106 505 LEU A CD1 4040 C CD2 . LEU A 489 ? 0.2242 0.2576 0.1794 0.0048 0.0071 0.0078 505 LEU A CD2 4041 N N . ARG A 490 ? 0.2356 0.2627 0.2050 0.0052 0.0049 0.0006 506 ARG A N 4042 C CA . ARG A 490 ? 0.2386 0.2644 0.2128 0.0050 0.0067 -0.0024 506 ARG A CA 4043 C C . ARG A 490 ? 0.2396 0.2646 0.2139 0.0057 0.0089 -0.0026 506 ARG A C 4044 O O . ARG A 490 ? 0.2405 0.2646 0.2166 0.0054 0.0122 -0.0039 506 ARG A O 4045 C CB . ARG A 490 ? 0.2343 0.2593 0.2140 0.0049 0.0038 -0.0052 506 ARG A CB 4046 C CG . ARG A 490 ? 0.2343 0.2588 0.2137 0.0059 0.0005 -0.0048 506 ARG A CG 4047 C CD . ARG A 490 ? 0.2343 0.2578 0.2186 0.0060 -0.0028 -0.0073 506 ARG A CD 4048 N NE . ARG A 490 ? 0.2350 0.2587 0.2191 0.0053 -0.0047 -0.0065 506 ARG A NE 4049 C CZ . ARG A 490 ? 0.2392 0.2618 0.2271 0.0054 -0.0078 -0.0083 506 ARG A CZ 4050 N NH1 . ARG A 490 ? 0.2342 0.2558 0.2266 0.0063 -0.0096 -0.0112 506 ARG A NH1 4051 N NH2 . ARG A 490 ? 0.2368 0.2594 0.2246 0.0047 -0.0093 -0.0075 506 ARG A NH2 4052 N N . TYR A 491 ? 0.2351 0.2602 0.2074 0.0067 0.0074 -0.0014 507 TYR A N 4053 C CA . TYR A 491 ? 0.2357 0.2600 0.2088 0.0075 0.0091 -0.0020 507 TYR A CA 4054 C C . TYR A 491 ? 0.2368 0.2612 0.2056 0.0077 0.0123 0.0003 507 TYR A C 4055 O O . TYR A 491 ? 0.2372 0.2603 0.2073 0.0078 0.0152 -0.0003 507 TYR A O 4056 C CB . TYR A 491 ? 0.2385 0.2630 0.2111 0.0085 0.0062 -0.0019 507 TYR A CB 4057 C CG . TYR A 491 ? 0.2478 0.2717 0.2246 0.0087 0.0029 -0.0044 507 TYR A CG 4058 C CD1 . TYR A 491 ? 0.2533 0.2762 0.2365 0.0087 0.0033 -0.0082 507 TYR A CD1 4059 C CD2 . TYR A 491 ? 0.2510 0.2753 0.2256 0.0089 -0.0006 -0.0032 507 TYR A CD2 4060 C CE1 . TYR A 491 ? 0.2571 0.2796 0.2443 0.0091 -0.0001 -0.0107 507 TYR A CE1 4061 C CE2 . TYR A 491 ? 0.2588 0.2822 0.2368 0.0093 -0.0039 -0.0053 507 TYR A CE2 4062 C CZ . TYR A 491 ? 0.2597 0.2823 0.2441 0.0095 -0.0038 -0.0091 507 TYR A CZ 4063 O OH . TYR A 491 ? 0.2757 0.2974 0.2637 0.0101 -0.0075 -0.0115 507 TYR A OH 4064 N N . LEU A 492 ? 0.2326 0.2584 0.1964 0.0078 0.0118 0.0031 508 LEU A N 4065 C CA . LEU A 492 ? 0.2230 0.2489 0.1826 0.0082 0.0144 0.0053 508 LEU A CA 4066 C C . LEU A 492 ? 0.2300 0.2547 0.1902 0.0075 0.0176 0.0045 508 LEU A C 4067 O O . LEU A 492 ? 0.2290 0.2522 0.1883 0.0079 0.0206 0.0049 508 LEU A O 4068 C CB . LEU A 492 ? 0.2159 0.2440 0.1707 0.0085 0.0129 0.0080 508 LEU A CB 4069 C CG . LEU A 492 ? 0.2106 0.2392 0.1609 0.0091 0.0151 0.0101 508 LEU A CG 4070 C CD1 . LEU A 492 ? 0.2114 0.2388 0.1608 0.0102 0.0169 0.0108 508 LEU A CD1 4071 C CD2 . LEU A 492 ? 0.2057 0.2368 0.1525 0.0093 0.0133 0.0122 508 LEU A CD2 4072 N N . VAL A 493 ? 0.2265 0.2517 0.1882 0.0066 0.0169 0.0034 509 VAL A N 4073 C CA . VAL A 493 ? 0.2329 0.2572 0.1953 0.0058 0.0199 0.0022 509 VAL A CA 4074 C C . VAL A 493 ? 0.2402 0.2623 0.2072 0.0055 0.0225 0.0000 509 VAL A C 4075 O O . VAL A 493 ? 0.2387 0.2592 0.2044 0.0054 0.0262 0.0003 509 VAL A O 4076 C CB . VAL A 493 ? 0.2296 0.2551 0.1940 0.0048 0.0183 0.0007 509 VAL A CB 4077 C CG1 . VAL A 493 ? 0.2361 0.2608 0.2013 0.0040 0.0217 -0.0007 509 VAL A CG1 4078 C CG2 . VAL A 493 ? 0.2287 0.2564 0.1890 0.0050 0.0161 0.0029 509 VAL A CG2 4079 N N . SER A 494 ? 0.2425 0.2645 0.2148 0.0053 0.0205 -0.0024 510 SER A N 4080 C CA . SER A 494 ? 0.2530 0.2732 0.2307 0.0051 0.0225 -0.0051 510 SER A CA 4081 C C . SER A 494 ? 0.2571 0.2758 0.2330 0.0058 0.0254 -0.0036 510 SER A C 4082 O O . SER A 494 ? 0.2534 0.2701 0.2310 0.0052 0.0292 -0.0045 510 SER A O 4083 C CB . SER A 494 ? 0.2528 0.2735 0.2357 0.0054 0.0190 -0.0076 510 SER A CB 4084 O OG . SER A 494 ? 0.2629 0.2822 0.2512 0.0053 0.0208 -0.0103 510 SER A OG 4085 N N . PHE A 495 ? 0.2576 0.2770 0.2301 0.0070 0.0236 -0.0015 511 PHE A N 4086 C CA . PHE A 495 ? 0.2642 0.2821 0.2353 0.0078 0.0259 -0.0003 511 PHE A CA 4087 C C . PHE A 495 ? 0.2675 0.2838 0.2340 0.0078 0.0297 0.0020 511 PHE A C 4088 O O . PHE A 495 ? 0.2735 0.2875 0.2406 0.0081 0.0327 0.0023 511 PHE A O 4089 C CB . PHE A 495 ? 0.2602 0.2795 0.2287 0.0091 0.0233 0.0012 511 PHE A CB 4090 C CG . PHE A 495 ? 0.2573 0.2769 0.2305 0.0095 0.0211 -0.0012 511 PHE A CG 4091 C CD1 . PHE A 495 ? 0.2558 0.2758 0.2335 0.0089 0.0188 -0.0040 511 PHE A CD1 4092 C CD2 . PHE A 495 ? 0.2583 0.2777 0.2315 0.0106 0.0213 -0.0011 511 PHE A CD2 4093 C CE1 . PHE A 495 ? 0.2538 0.2741 0.2355 0.0096 0.0165 -0.0065 511 PHE A CE1 4094 C CE2 . PHE A 495 ? 0.2534 0.2732 0.2307 0.0111 0.0191 -0.0037 511 PHE A CE2 4095 C CZ . PHE A 495 ? 0.2573 0.2775 0.2387 0.0107 0.0166 -0.0064 511 PHE A CZ 4096 N N . ILE A 496 ? 0.2724 0.2897 0.2347 0.0076 0.0294 0.0036 512 ILE A N 4097 C CA . ILE A 496 ? 0.2746 0.2904 0.2320 0.0078 0.0327 0.0056 512 ILE A CA 4098 C C . ILE A 496 ? 0.2808 0.2946 0.2410 0.0064 0.0363 0.0037 512 ILE A C 4099 O O . ILE A 496 ? 0.2788 0.2896 0.2382 0.0064 0.0403 0.0043 512 ILE A O 4100 C CB . ILE A 496 ? 0.2828 0.3008 0.2347 0.0082 0.0308 0.0077 512 ILE A CB 4101 C CG1 . ILE A 496 ? 0.2799 0.2997 0.2287 0.0095 0.0281 0.0098 512 ILE A CG1 4102 C CG2 . ILE A 496 ? 0.2872 0.3037 0.2339 0.0085 0.0340 0.0094 512 ILE A CG2 4103 C CD1 . ILE A 496 ? 0.2885 0.3113 0.2340 0.0096 0.0255 0.0110 512 ILE A CD1 4104 N N . ILE A 497 ? 0.2727 0.2879 0.2364 0.0053 0.0352 0.0012 513 ILE A N 4105 C CA . ILE A 497 ? 0.2798 0.2936 0.2461 0.0039 0.0387 -0.0008 513 ILE A CA 4106 C C . ILE A 497 ? 0.2781 0.2898 0.2513 0.0031 0.0412 -0.0035 513 ILE A C 4107 O O . ILE A 497 ? 0.2925 0.3022 0.2668 0.0021 0.0455 -0.0044 513 ILE A O 4108 C CB . ILE A 497 ? 0.2758 0.2918 0.2439 0.0030 0.0369 -0.0028 513 ILE A CB 4109 C CG1 . ILE A 497 ? 0.2731 0.2907 0.2480 0.0026 0.0333 -0.0058 513 ILE A CG1 4110 C CG2 . ILE A 497 ? 0.2806 0.2985 0.2421 0.0037 0.0350 -0.0003 513 ILE A CG2 4111 C CD1 . ILE A 497 ? 0.2696 0.2889 0.2473 0.0016 0.0315 -0.0081 513 ILE A CD1 4112 N N . GLN A 498 ? 0.2743 0.2866 0.2520 0.0035 0.0388 -0.0049 514 GLN A N 4113 C CA . GLN A 498 ? 0.2701 0.2807 0.2550 0.0028 0.0410 -0.0080 514 GLN A CA 4114 C C . GLN A 498 ? 0.2752 0.2825 0.2584 0.0029 0.0458 -0.0063 514 GLN A C 4115 O O . GLN A 498 ? 0.2778 0.2831 0.2663 0.0018 0.0493 -0.0086 514 GLN A O 4116 C CB . GLN A 498 ? 0.2686 0.2805 0.2582 0.0036 0.0371 -0.0099 514 GLN A CB 4117 C CG . GLN A 498 ? 0.2706 0.2825 0.2565 0.0051 0.0359 -0.0073 514 GLN A CG 4118 C CD . GLN A 498 ? 0.2677 0.2811 0.2574 0.0059 0.0318 -0.0093 514 GLN A CD 4119 O OE1 . GLN A 498 ? 0.2813 0.2940 0.2740 0.0065 0.0323 -0.0103 514 GLN A OE1 4120 N NE2 . GLN A 498 ? 0.2591 0.2748 0.2489 0.0061 0.0277 -0.0100 514 GLN A NE2 4121 N N . PHE A 499 ? 0.2770 0.2835 0.2528 0.0041 0.0460 -0.0023 515 PHE A N 4122 C CA . PHE A 499 ? 0.2820 0.2848 0.2552 0.0043 0.0504 -0.0002 515 PHE A CA 4123 C C . PHE A 499 ? 0.2926 0.2933 0.2620 0.0034 0.0547 0.0008 515 PHE A C 4124 O O . PHE A 499 ? 0.2976 0.2946 0.2678 0.0028 0.0595 0.0010 515 PHE A O 4125 C CB . PHE A 499 ? 0.2787 0.2813 0.2461 0.0062 0.0489 0.0033 515 PHE A CB 4126 C CG . PHE A 499 ? 0.2812 0.2848 0.2529 0.0070 0.0464 0.0020 515 PHE A CG 4127 C CD1 . PHE A 499 ? 0.2756 0.2827 0.2478 0.0076 0.0414 0.0013 515 PHE A CD1 4128 C CD2 . PHE A 499 ? 0.2887 0.2895 0.2641 0.0071 0.0490 0.0014 515 PHE A CD2 4129 C CE1 . PHE A 499 ? 0.2721 0.2802 0.2478 0.0084 0.0391 0.0000 515 PHE A CE1 4130 C CE2 . PHE A 499 ? 0.2848 0.2867 0.2643 0.0079 0.0466 -0.0001 515 PHE A CE2 4131 C CZ . PHE A 499 ? 0.2782 0.2838 0.2575 0.0086 0.0416 -0.0008 515 PHE A CZ 4132 N N . GLN A 500 ? 0.2930 0.2957 0.2583 0.0034 0.0532 0.0013 516 GLN A N 4133 C CA . GLN A 500 ? 0.3080 0.3094 0.2705 0.0023 0.0570 0.0014 516 GLN A CA 4134 C C . GLN A 500 ? 0.3102 0.3109 0.2807 0.0003 0.0600 -0.0026 516 GLN A C 4135 O O . GLN A 500 ? 0.3263 0.3239 0.2961 -0.0006 0.0653 -0.0024 516 GLN A O 4136 C CB . GLN A 500 ? 0.3053 0.3097 0.2631 0.0027 0.0542 0.0020 516 GLN A CB 4137 C CG . GLN A 500 ? 0.3024 0.3080 0.2528 0.0046 0.0512 0.0056 516 GLN A CG 4138 C CD . GLN A 500 ? 0.3052 0.3138 0.2518 0.0048 0.0487 0.0058 516 GLN A CD 4139 O OE1 . GLN A 500 ? 0.2965 0.3081 0.2435 0.0053 0.0442 0.0058 516 GLN A OE1 4140 N NE2 . GLN A 500 ? 0.3036 0.3112 0.2462 0.0044 0.0516 0.0060 516 GLN A NE2 4141 N N . PHE A 501 ? 0.3072 0.3106 0.2852 -0.0002 0.0568 -0.0062 517 PHE A N 4142 C CA . PHE A 501 ? 0.3117 0.3149 0.2986 -0.0020 0.0591 -0.0107 517 PHE A CA 4143 C C . PHE A 501 ? 0.3202 0.3203 0.3120 -0.0025 0.0628 -0.0116 517 PHE A C 4144 O O . PHE A 501 ? 0.3209 0.3190 0.3165 -0.0041 0.0677 -0.0135 517 PHE A O 4145 C CB . PHE A 501 ? 0.3040 0.3107 0.2977 -0.0020 0.0541 -0.0143 517 PHE A CB 4146 C CG . PHE A 501 ? 0.3056 0.3151 0.2965 -0.0019 0.0509 -0.0143 517 PHE A CG 4147 C CD1 . PHE A 501 ? 0.3090 0.3184 0.2959 -0.0027 0.0535 -0.0137 517 PHE A CD1 4148 C CD2 . PHE A 501 ? 0.3027 0.3149 0.2954 -0.0011 0.0452 -0.0150 517 PHE A CD2 4149 C CE1 . PHE A 501 ? 0.3040 0.3161 0.2890 -0.0026 0.0504 -0.0141 517 PHE A CE1 4150 C CE2 . PHE A 501 ? 0.3014 0.3160 0.2922 -0.0011 0.0422 -0.0150 517 PHE A CE2 4151 C CZ . PHE A 501 ? 0.3017 0.3164 0.2890 -0.0018 0.0448 -0.0147 517 PHE A CZ 4152 N N . TYR A 502 ? 0.3196 0.3194 0.3115 -0.0012 0.0606 -0.0104 518 TYR A N 4153 C CA . TYR A 502 ? 0.3306 0.3278 0.3279 -0.0015 0.0634 -0.0115 518 TYR A CA 4154 C C . TYR A 502 ? 0.3444 0.3371 0.3373 -0.0020 0.0695 -0.0086 518 TYR A C 4155 O O . TYR A 502 ? 0.3481 0.3382 0.3464 -0.0035 0.0742 -0.0106 518 TYR A O 4156 C CB . TYR A 502 ? 0.3209 0.3191 0.3185 0.0001 0.0594 -0.0108 518 TYR A CB 4157 C CG . TYR A 502 ? 0.3264 0.3225 0.3303 0.0000 0.0616 -0.0124 518 TYR A CG 4158 C CD1 . TYR A 502 ? 0.3269 0.3236 0.3412 -0.0010 0.0619 -0.0175 518 TYR A CD1 4159 C CD2 . TYR A 502 ? 0.3311 0.3245 0.3309 0.0011 0.0630 -0.0091 518 TYR A CD2 4160 C CE1 . TYR A 502 ? 0.3293 0.3242 0.3498 -0.0011 0.0638 -0.0193 518 TYR A CE1 4161 C CE2 . TYR A 502 ? 0.3418 0.3331 0.3476 0.0010 0.0649 -0.0107 518 TYR A CE2 4162 C CZ . TYR A 502 ? 0.3389 0.3310 0.3552 -0.0001 0.0654 -0.0159 518 TYR A CZ 4163 O OH . TYR A 502 ? 0.3492 0.3394 0.3719 -0.0001 0.0672 -0.0177 518 TYR A OH 4164 N N . LYS A 503 ? 0.3490 0.3405 0.3319 -0.0007 0.0695 -0.0039 519 LYS A N 4165 C CA . LYS A 503 ? 0.3536 0.3404 0.3308 -0.0008 0.0748 -0.0006 519 LYS A CA 4166 C C . LYS A 503 ? 0.3632 0.3484 0.3413 -0.0029 0.0800 -0.0021 519 LYS A C 4167 O O . LYS A 503 ? 0.3579 0.3391 0.3380 -0.0041 0.0856 -0.0021 519 LYS A O 4168 C CB . LYS A 503 ? 0.3617 0.3482 0.3278 0.0011 0.0730 0.0041 519 LYS A CB 4169 C CG . LYS A 503 ? 0.3810 0.3624 0.3399 0.0014 0.0781 0.0080 519 LYS A CG 4170 C CD . LYS A 503 ? 0.3874 0.3690 0.3357 0.0036 0.0756 0.0123 519 LYS A CD 4171 C CE . LYS A 503 ? 0.4004 0.3778 0.3405 0.0037 0.0803 0.0153 519 LYS A CE 4172 N NZ . LYS A 503 ? 0.4135 0.3907 0.3435 0.0062 0.0779 0.0196 519 LYS A NZ 4173 N N . SER A 504 ? 0.3505 0.3389 0.3274 -0.0033 0.0782 -0.0035 520 SER A N 4174 C CA . SER A 504 ? 0.3571 0.3446 0.3349 -0.0053 0.0828 -0.0054 520 SER A CA 4175 C C . SER A 504 ? 0.3523 0.3397 0.3416 -0.0074 0.0858 -0.0103 520 SER A C 4176 O O . SER A 504 ? 0.3587 0.3429 0.3489 -0.0091 0.0920 -0.0108 520 SER A O 4177 C CB . SER A 504 ? 0.3572 0.3487 0.3320 -0.0052 0.0798 -0.0062 520 SER A CB 4178 O OG . SER A 504 ? 0.3683 0.3591 0.3320 -0.0035 0.0788 -0.0018 520 SER A OG 4179 N N . ALA A 505 ? 0.3397 0.3303 0.3375 -0.0073 0.0815 -0.0139 521 ALA A N 4180 C CA . ALA A 505 ? 0.3411 0.3320 0.3508 -0.0091 0.0833 -0.0192 521 ALA A CA 4181 C C . ALA A 505 ? 0.3507 0.3374 0.3636 -0.0097 0.0881 -0.0187 521 ALA A C 4182 O O . ALA A 505 ? 0.3543 0.3394 0.3743 -0.0118 0.0931 -0.0217 521 ALA A O 4183 C CB . ALA A 505 ? 0.3279 0.3230 0.3448 -0.0083 0.0769 -0.0227 521 ALA A CB 4184 N N . CYS A 506 ? 0.3530 0.3378 0.3611 -0.0080 0.0867 -0.0150 522 CYS A N 4185 C CA . CYS A 506 ? 0.3707 0.3511 0.3810 -0.0083 0.0909 -0.0139 522 CYS A CA 4186 C C . CYS A 506 ? 0.3842 0.3595 0.3892 -0.0096 0.0983 -0.0110 522 CYS A C 4187 O O . CYS A 506 ? 0.3870 0.3590 0.3978 -0.0113 0.1036 -0.0124 522 CYS A O 4188 C CB . CYS A 506 ? 0.3754 0.3553 0.3813 -0.0060 0.0874 -0.0105 522 CYS A CB 4189 S SG . CYS A 506 ? 0.3754 0.3603 0.3889 -0.0047 0.0801 -0.0144 522 CYS A SG 4190 N N . ILE A 507 ? 0.3924 0.3670 0.3864 -0.0088 0.0985 -0.0070 523 ILE A N 4191 C CA . ILE A 507 ? 0.4093 0.3793 0.3970 -0.0099 0.1052 -0.0043 523 ILE A CA 4192 C C . ILE A 507 ? 0.4199 0.3904 0.4150 -0.0128 0.1099 -0.0088 523 ILE A C 4193 O O . ILE A 507 ? 0.4327 0.3990 0.4307 -0.0146 0.1165 -0.0091 523 ILE A O 4194 C CB . ILE A 507 ? 0.4139 0.3837 0.3882 -0.0082 0.1038 0.0003 523 ILE A CB 4195 C CG1 . ILE A 507 ? 0.4189 0.3869 0.3861 -0.0055 0.1008 0.0050 523 ILE A CG1 4196 C CG2 . ILE A 507 ? 0.4280 0.3937 0.3960 -0.0094 0.1105 0.0022 523 ILE A CG2 4197 C CD1 . ILE A 507 ? 0.4150 0.3843 0.3706 -0.0034 0.0975 0.0088 523 ILE A CD1 4198 N N . LYS A 508 ? 0.4064 0.3820 0.4052 -0.0132 0.1065 -0.0125 524 LYS A N 4199 C CA . LYS A 508 ? 0.4083 0.3852 0.4150 -0.0158 0.1102 -0.0175 524 LYS A CA 4200 C C . LYS A 508 ? 0.4089 0.3849 0.4286 -0.0176 0.1132 -0.0218 524 LYS A C 4201 O O . LYS A 508 ? 0.4180 0.3927 0.4431 -0.0200 0.1191 -0.0247 524 LYS A O 4202 C CB . LYS A 508 ? 0.4036 0.3864 0.4133 -0.0155 0.1049 -0.0210 524 LYS A CB 4203 C CG . LYS A 508 ? 0.4064 0.3905 0.4049 -0.0144 0.1029 -0.0178 524 LYS A CG 4204 C CD . LYS A 508 ? 0.4042 0.3939 0.4060 -0.0137 0.0965 -0.0209 524 LYS A CD 4205 C CE . LYS A 508 ? 0.4101 0.4013 0.4009 -0.0121 0.0934 -0.0174 524 LYS A CE 4206 N NZ . LYS A 508 ? 0.4230 0.4134 0.4088 -0.0133 0.0981 -0.0174 524 LYS A NZ 4207 N N . ALA A 509 ? 0.4008 0.3776 0.4256 -0.0163 0.1091 -0.0227 525 ALA A N 4208 C CA . ALA A 509 ? 0.4007 0.3771 0.4382 -0.0177 0.1110 -0.0271 525 ALA A CA 4209 C C . ALA A 509 ? 0.4091 0.3794 0.4460 -0.0185 0.1173 -0.0244 525 ALA A C 4210 O O . ALA A 509 ? 0.4124 0.3818 0.4599 -0.0198 0.1198 -0.0280 525 ALA A O 4211 C CB . ALA A 509 ? 0.3834 0.3635 0.4266 -0.0159 0.1037 -0.0295 525 ALA A CB 4212 N N . GLY A 510 ? 0.4176 0.3837 0.4423 -0.0176 0.1197 -0.0182 526 GLY A N 4213 C CA . GLY A 510 ? 0.4306 0.3902 0.4531 -0.0180 0.1252 -0.0148 526 GLY A CA 4214 C C . GLY A 510 ? 0.4364 0.3958 0.4618 -0.0162 0.1213 -0.0141 526 GLY A C 4215 O O . GLY A 510 ? 0.4356 0.3905 0.4648 -0.0168 0.1253 -0.0136 526 GLY A O 4216 N N . GLN A 511 ? 0.4253 0.3893 0.4489 -0.0139 0.1136 -0.0142 527 GLN A N 4217 C CA . GLN A 511 ? 0.4284 0.3934 0.4556 -0.0121 0.1091 -0.0146 527 GLN A CA 4218 C C . GLN A 511 ? 0.4365 0.3998 0.4522 -0.0094 0.1062 -0.0087 527 GLN A C 4219 O O . GLN A 511 ? 0.4455 0.4093 0.4630 -0.0078 0.1028 -0.0084 527 GLN A O 4220 C CB . GLN A 511 ? 0.4201 0.3915 0.4548 -0.0115 0.1025 -0.0196 527 GLN A CB 4221 C CG . GLN A 511 ? 0.4217 0.3947 0.4705 -0.0135 0.1042 -0.0263 527 GLN A CG 4222 C CD . GLN A 511 ? 0.4258 0.3971 0.4828 -0.0134 0.1048 -0.0282 527 GLN A CD 4223 O OE1 . GLN A 511 ? 0.4278 0.4003 0.4834 -0.0112 0.1001 -0.0272 527 GLN A OE1 4224 N NE2 . GLN A 511 ? 0.4268 0.3955 0.4927 -0.0157 0.1109 -0.0312 527 GLN A NE2 4225 N N . TYR A 512 ? 0.4362 0.3980 0.4406 -0.0088 0.1072 -0.0043 528 TYR A N 4226 C CA . TYR A 512 ? 0.4368 0.3970 0.4305 -0.0062 0.1048 0.0012 528 TYR A CA 4227 C C . TYR A 512 ? 0.4552 0.4101 0.4384 -0.0063 0.1099 0.0061 528 TYR A C 4228 O O . TYR A 512 ? 0.4619 0.4172 0.4414 -0.0074 0.1120 0.0060 528 TYR A O 4229 C CB . TYR A 512 ? 0.4180 0.3838 0.4071 -0.0043 0.0975 0.0014 528 TYR A CB 4230 C CG . TYR A 512 ? 0.4141 0.3787 0.3918 -0.0017 0.0950 0.0069 528 TYR A CG 4231 C CD1 . TYR A 512 ? 0.4159 0.3772 0.3923 -0.0003 0.0952 0.0096 528 TYR A CD1 4232 C CD2 . TYR A 512 ? 0.4147 0.3819 0.3839 -0.0007 0.0922 0.0090 528 TYR A CD2 4233 C CE1 . TYR A 512 ? 0.4140 0.3744 0.3805 0.0022 0.0928 0.0143 528 TYR A CE1 4234 C CE2 . TYR A 512 ? 0.4120 0.3784 0.3714 0.0017 0.0896 0.0136 528 TYR A CE2 4235 C CZ . TYR A 512 ? 0.4120 0.3751 0.3703 0.0032 0.0899 0.0162 528 TYR A CZ 4236 O OH . TYR A 512 ? 0.4099 0.3724 0.3591 0.0058 0.0873 0.0204 528 TYR A OH 4237 N N . ASP A 513 ? 0.4808 0.4306 0.4594 -0.0051 0.1118 0.0103 529 ASP A N 4238 C CA . ASP A 513 ? 0.5156 0.4598 0.4826 -0.0044 0.1157 0.0158 529 ASP A CA 4239 C C . ASP A 513 ? 0.5211 0.4637 0.4820 -0.0013 0.1122 0.0200 529 ASP A C 4240 O O . ASP A 513 ? 0.5168 0.4572 0.4831 -0.0010 0.1126 0.0198 529 ASP A O 4241 C CB . ASP A 513 ? 0.5404 0.4781 0.5102 -0.0067 0.1240 0.0162 529 ASP A CB 4242 C CG . ASP A 513 ? 0.5704 0.5015 0.5276 -0.0059 0.1285 0.0223 529 ASP A CG 4243 O OD1 . ASP A 513 ? 0.5671 0.4979 0.5138 -0.0031 0.1249 0.0265 529 ASP A OD1 4244 O OD2 . ASP A 513 ? 0.5890 0.5150 0.5468 -0.0081 0.1357 0.0228 529 ASP A OD2 4245 N N . PRO A 514 ? 0.5402 0.4841 0.4902 0.0008 0.1086 0.0235 530 PRO A N 4246 C CA . PRO A 514 ? 0.5613 0.5045 0.5055 0.0039 0.1046 0.0272 530 PRO A CA 4247 C C . PRO A 514 ? 0.5893 0.5247 0.5298 0.0048 0.1088 0.0314 530 PRO A C 4248 O O . PRO A 514 ? 0.5861 0.5208 0.5251 0.0071 0.1059 0.0335 530 PRO A O 4249 C CB . PRO A 514 ? 0.5523 0.4982 0.4857 0.0057 0.1012 0.0297 530 PRO A CB 4250 C CG . PRO A 514 ? 0.5605 0.5059 0.4918 0.0037 0.1052 0.0288 530 PRO A CG 4251 C CD . PRO A 514 ? 0.5423 0.4889 0.4857 0.0007 0.1079 0.0237 530 PRO A CD 4252 N N . ASP A 515 ? 0.6240 0.5536 0.5632 0.0030 0.1158 0.0327 531 ASP A N 4253 C CA . ASP A 515 ? 0.6546 0.5760 0.5900 0.0036 0.1204 0.0370 531 ASP A CA 4254 C C . ASP A 515 ? 0.6539 0.5721 0.6010 0.0013 0.1249 0.0344 531 ASP A C 4255 O O . ASP A 515 ? 0.6803 0.5912 0.6260 0.0013 0.1296 0.0375 531 ASP A O 4256 C CB . ASP A 515 ? 0.6861 0.6020 0.6103 0.0034 0.1255 0.0412 531 ASP A CB 4257 C CG . ASP A 515 ? 0.7125 0.6313 0.6249 0.0059 0.1210 0.0438 531 ASP A CG 4258 O OD1 . ASP A 515 ? 0.7275 0.6479 0.6361 0.0089 0.1156 0.0458 531 ASP A OD1 4259 O OD2 . ASP A 515 ? 0.7269 0.6466 0.6343 0.0050 0.1230 0.0436 531 ASP A OD2 4260 N N . ASN A 516 ? 0.6276 0.5512 0.5862 -0.0004 0.1233 0.0285 532 ASN A N 4261 C CA . ASN A 516 ? 0.6124 0.5340 0.5834 -0.0026 0.1270 0.0251 532 ASN A CA 4262 C C . ASN A 516 ? 0.6042 0.5305 0.5837 -0.0014 0.1213 0.0217 532 ASN A C 4263 O O . ASN A 516 ? 0.5792 0.5125 0.5638 -0.0016 0.1166 0.0175 532 ASN A O 4264 C CB . ASN A 516 ? 0.6072 0.5306 0.5857 -0.0060 0.1310 0.0205 532 ASN A CB 4265 C CG . ASN A 516 ? 0.6090 0.5299 0.6005 -0.0085 0.1356 0.0168 532 ASN A CG 4266 O OD1 . ASN A 516 ? 0.6099 0.5287 0.6061 -0.0076 0.1351 0.0170 532 ASN A OD1 4267 N ND2 . ASN A 516 ? 0.6081 0.5295 0.6061 -0.0116 0.1402 0.0132 532 ASN A ND2 4268 N N . VAL A 517 ? 0.6006 0.5227 0.5814 -0.0002 0.1218 0.0237 533 VAL A N 4269 C CA . VAL A 517 ? 0.5919 0.5177 0.5805 0.0010 0.1170 0.0207 533 VAL A CA 4270 C C . VAL A 517 ? 0.5844 0.5146 0.5868 -0.0012 0.1167 0.0137 533 VAL A C 4271 O O . VAL A 517 ? 0.5811 0.5167 0.5890 -0.0002 0.1114 0.0103 533 VAL A O 4272 C CB . VAL A 517 ? 0.6136 0.5330 0.6024 0.0023 0.1191 0.0237 533 VAL A CB 4273 C CG1 . VAL A 517 ? 0.6113 0.5343 0.6099 0.0032 0.1151 0.0198 533 VAL A CG1 4274 C CG2 . VAL A 517 ? 0.6128 0.5289 0.5882 0.0052 0.1176 0.0301 533 VAL A CG2 4275 N N . GLU A 518 ? 0.5888 0.5169 0.5964 -0.0041 0.1225 0.0116 534 GLU A N 4276 C CA . GLU A 518 ? 0.5909 0.5231 0.6120 -0.0063 0.1226 0.0048 534 GLU A CA 4277 C C . GLU A 518 ? 0.5451 0.4845 0.5669 -0.0066 0.1181 0.0013 534 GLU A C 4278 O O . GLU A 518 ? 0.5302 0.4741 0.5627 -0.0077 0.1164 -0.0045 534 GLU A O 4279 C CB . GLU A 518 ? 0.6343 0.5613 0.6617 -0.0095 0.1309 0.0035 534 GLU A CB 4280 C CG . GLU A 518 ? 0.6979 0.6172 0.7269 -0.0097 0.1358 0.0062 534 GLU A CG 4281 C CD . GLU A 518 ? 0.7377 0.6591 0.7765 -0.0086 0.1323 0.0028 534 GLU A CD 4282 O OE1 . GLU A 518 ? 0.7744 0.6988 0.8261 -0.0103 0.1326 -0.0034 534 GLU A OE1 4283 O OE2 . GLU A 518 ? 0.7729 0.6931 0.8066 -0.0059 0.1291 0.0061 534 GLU A OE2 4284 N N . LEU A 519 ? 0.5194 0.4602 0.5301 -0.0055 0.1161 0.0047 535 LEU A N 4285 C CA . LEU A 519 ? 0.4944 0.4417 0.5053 -0.0058 0.1121 0.0018 535 LEU A CA 4286 C C . LEU A 519 ? 0.4746 0.4260 0.4770 -0.0030 0.1051 0.0042 535 LEU A C 4287 O O . LEU A 519 ? 0.4794 0.4318 0.4730 -0.0026 0.1042 0.0067 535 LEU A O 4288 C CB . LEU A 519 ? 0.5030 0.4487 0.5104 -0.0079 0.1170 0.0023 535 LEU A CB 4289 C CG . LEU A 519 ? 0.5148 0.4568 0.5305 -0.0111 0.1245 -0.0002 535 LEU A CG 4290 C CD1 . LEU A 519 ? 0.5190 0.4583 0.5275 -0.0127 0.1298 0.0019 535 LEU A CD1 4291 C CD2 . LEU A 519 ? 0.5079 0.4548 0.5377 -0.0127 0.1230 -0.0076 535 LEU A CD2 4292 N N . PRO A 520 ? 0.4528 0.4069 0.4581 -0.0012 0.1001 0.0032 536 PRO A N 4293 C CA . PRO A 520 ? 0.4357 0.3939 0.4337 0.0012 0.0937 0.0052 536 PRO A CA 4294 C C . PRO A 520 ? 0.4066 0.3713 0.4067 0.0008 0.0891 0.0018 536 PRO A C 4295 O O . PRO A 520 ? 0.4075 0.3745 0.4170 -0.0006 0.0891 -0.0031 536 PRO A O 4296 C CB . PRO A 520 ? 0.4270 0.3859 0.4293 0.0028 0.0907 0.0044 536 PRO A CB 4297 C CG . PRO A 520 ? 0.4350 0.3934 0.4497 0.0010 0.0932 -0.0005 536 PRO A CG 4298 C CD . PRO A 520 ? 0.4477 0.4015 0.4636 -0.0014 0.1002 -0.0002 536 PRO A CD 4299 N N . LEU A 521 ? 0.3937 0.3613 0.3853 0.0023 0.0852 0.0043 537 LEU A N 4300 C CA . LEU A 521 ? 0.3732 0.3463 0.3660 0.0018 0.0812 0.0015 537 LEU A CA 4301 C C . LEU A 521 ? 0.3703 0.3478 0.3710 0.0023 0.0763 -0.0026 537 LEU A C 4302 O O . LEU A 521 ? 0.3520 0.3329 0.3586 0.0013 0.0745 -0.0066 537 LEU A O 4303 C CB . LEU A 521 ? 0.3735 0.3485 0.3557 0.0033 0.0780 0.0052 537 LEU A CB 4304 C CG . LEU A 521 ? 0.3641 0.3443 0.3461 0.0029 0.0742 0.0031 537 LEU A CG 4305 C CD1 . LEU A 521 ? 0.3662 0.3463 0.3533 0.0005 0.0775 0.0000 537 LEU A CD1 4306 C CD2 . LEU A 521 ? 0.3624 0.3435 0.3338 0.0044 0.0721 0.0071 537 LEU A CD2 4307 N N . ASP A 522 ? 0.3634 0.3407 0.3642 0.0040 0.0744 -0.0017 538 ASP A N 4308 C CA . ASP A 522 ? 0.3654 0.3467 0.3725 0.0048 0.0697 -0.0053 538 ASP A CA 4309 C C . ASP A 522 ? 0.3712 0.3521 0.3901 0.0035 0.0715 -0.0105 538 ASP A C 4310 O O . ASP A 522 ? 0.3739 0.3580 0.3983 0.0043 0.0677 -0.0139 538 ASP A O 4311 C CB . ASP A 522 ? 0.3588 0.3405 0.3617 0.0071 0.0668 -0.0028 538 ASP A CB 4312 C CG . ASP A 522 ? 0.3663 0.3425 0.3675 0.0076 0.0711 0.0001 538 ASP A CG 4313 O OD1 . ASP A 522 ? 0.3738 0.3466 0.3679 0.0075 0.0740 0.0041 538 ASP A OD1 4314 O OD2 . ASP A 522 ? 0.3709 0.3462 0.3776 0.0081 0.0713 -0.0014 538 ASP A OD2 4315 N N . ASN A 523 ? 0.3823 0.3595 0.4052 0.0015 0.0772 -0.0113 539 ASN A N 4316 C CA . ASN A 523 ? 0.3765 0.3540 0.4115 0.0000 0.0789 -0.0169 539 ASN A CA 4317 C C . ASN A 523 ? 0.3859 0.3635 0.4249 -0.0023 0.0820 -0.0194 539 ASN A C 4318 O O . ASN A 523 ? 0.3911 0.3675 0.4397 -0.0041 0.0856 -0.0233 539 ASN A O 4319 C CB . ASN A 523 ? 0.3796 0.3525 0.4195 -0.0003 0.0832 -0.0169 539 ASN A CB 4320 C CG . ASN A 523 ? 0.3826 0.3575 0.4349 -0.0006 0.0819 -0.0230 539 ASN A CG 4321 O OD1 . ASN A 523 ? 0.3782 0.3581 0.4332 0.0005 0.0763 -0.0262 539 ASN A OD1 4322 N ND2 . ASN A 523 ? 0.3822 0.3534 0.4421 -0.0021 0.0871 -0.0247 539 ASN A ND2 4323 N N . CYS A 524 ? 0.3845 0.3638 0.4167 -0.0024 0.0806 -0.0176 540 CYS A N 4324 C CA . CYS A 524 ? 0.3886 0.3683 0.4238 -0.0045 0.0835 -0.0198 540 CYS A CA 4325 C C . CYS A 524 ? 0.3843 0.3685 0.4292 -0.0050 0.0799 -0.0260 540 CYS A C 4326 O O . CYS A 524 ? 0.3749 0.3632 0.4186 -0.0034 0.0737 -0.0268 540 CYS A O 4327 C CB . CYS A 524 ? 0.3875 0.3675 0.4120 -0.0043 0.0833 -0.0159 540 CYS A CB 4328 S SG . CYS A 524 ? 0.4043 0.3873 0.4323 -0.0062 0.0835 -0.0196 540 CYS A SG 4329 N N . ASP A 525 ? 0.3711 0.3546 0.4255 -0.0071 0.0839 -0.0303 541 ASP A N 4330 C CA . ASP A 525 ? 0.3696 0.3574 0.4337 -0.0076 0.0807 -0.0364 541 ASP A CA 4331 C C . ASP A 525 ? 0.3736 0.3616 0.4391 -0.0097 0.0840 -0.0380 541 ASP A C 4332 O O . ASP A 525 ? 0.3740 0.3591 0.4437 -0.0119 0.0905 -0.0391 541 ASP A O 4333 C CB . ASP A 525 ? 0.3685 0.3562 0.4450 -0.0081 0.0816 -0.0417 541 ASP A CB 4334 C CG . ASP A 525 ? 0.3666 0.3591 0.4527 -0.0078 0.0768 -0.0481 541 ASP A CG 4335 O OD1 . ASP A 525 ? 0.3499 0.3455 0.4327 -0.0071 0.0725 -0.0483 541 ASP A OD1 4336 O OD2 . ASP A 525 ? 0.3583 0.3513 0.4554 -0.0082 0.0772 -0.0532 541 ASP A OD2 4337 N N . ILE A 526 ? 0.3629 0.3543 0.4248 -0.0090 0.0796 -0.0381 542 ILE A N 4338 C CA . ILE A 526 ? 0.3570 0.3494 0.4206 -0.0108 0.0820 -0.0400 542 ILE A CA 4339 C C . ILE A 526 ? 0.3550 0.3503 0.4318 -0.0119 0.0811 -0.0473 542 ILE A C 4340 O O . ILE A 526 ? 0.3460 0.3427 0.4256 -0.0133 0.0826 -0.0497 542 ILE A O 4341 C CB . ILE A 526 ? 0.3528 0.3472 0.4066 -0.0099 0.0785 -0.0368 542 ILE A CB 4342 C CG1 . ILE A 526 ? 0.3387 0.3374 0.3933 -0.0079 0.0704 -0.0383 542 ILE A CG1 4343 C CG2 . ILE A 526 ? 0.3540 0.3454 0.3953 -0.0091 0.0804 -0.0301 542 ILE A CG2 4344 C CD1 . ILE A 526 ? 0.3338 0.3348 0.3814 -0.0073 0.0669 -0.0363 542 ILE A CD1 4345 N N . TYR A 527 ? 0.3508 0.3474 0.4360 -0.0111 0.0784 -0.0510 543 TYR A N 4346 C CA . TYR A 527 ? 0.3507 0.3500 0.4492 -0.0119 0.0774 -0.0582 543 TYR A CA 4347 C C . TYR A 527 ? 0.3584 0.3558 0.4630 -0.0149 0.0849 -0.0607 543 TYR A C 4348 O O . TYR A 527 ? 0.3596 0.3528 0.4623 -0.0163 0.0913 -0.0581 543 TYR A O 4349 C CB . TYR A 527 ? 0.3437 0.3438 0.4506 -0.0107 0.0748 -0.0619 543 TYR A CB 4350 C CG . TYR A 527 ? 0.3401 0.3433 0.4611 -0.0113 0.0733 -0.0698 543 TYR A CG 4351 C CD1 . TYR A 527 ? 0.3390 0.3463 0.4623 -0.0094 0.0659 -0.0729 543 TYR A CD1 4352 C CD2 . TYR A 527 ? 0.3455 0.3473 0.4776 -0.0136 0.0792 -0.0742 543 TYR A CD2 4353 C CE1 . TYR A 527 ? 0.3328 0.3429 0.4689 -0.0097 0.0641 -0.0802 543 TYR A CE1 4354 C CE2 . TYR A 527 ? 0.3393 0.3444 0.4849 -0.0141 0.0777 -0.0818 543 TYR A CE2 4355 C CZ . TYR A 527 ? 0.3460 0.3552 0.4934 -0.0119 0.0699 -0.0848 543 TYR A CZ 4356 O OH . TYR A 527 ? 0.3462 0.3586 0.5068 -0.0120 0.0677 -0.0924 543 TYR A OH 4357 N N . GLY A 528 ? 0.3597 0.3600 0.4713 -0.0158 0.0843 -0.0654 544 GLY A N 4358 C CA . GLY A 528 ? 0.3714 0.3706 0.4905 -0.0188 0.0913 -0.0688 544 GLY A CA 4359 C C . GLY A 528 ? 0.3785 0.3752 0.4888 -0.0205 0.0970 -0.0646 544 GLY A C 4360 O O . GLY A 528 ? 0.3838 0.3793 0.4993 -0.0231 0.1035 -0.0671 544 GLY A O 4361 N N . SER A 529 ? 0.3695 0.3654 0.4664 -0.0190 0.0948 -0.0585 545 SER A N 4362 C CA . SER A 529 ? 0.3753 0.3687 0.4625 -0.0202 0.0998 -0.0543 545 SER A CA 4363 C C . SER A 529 ? 0.3713 0.3682 0.4580 -0.0206 0.0980 -0.0563 545 SER A C 4364 O O . SER A 529 ? 0.3624 0.3620 0.4441 -0.0187 0.0917 -0.0550 545 SER A O 4365 C CB . SER A 529 ? 0.3758 0.3665 0.4490 -0.0185 0.0989 -0.0468 545 SER A CB 4366 O OG . SER A 529 ? 0.3885 0.3775 0.4517 -0.0192 0.1025 -0.0429 545 SER A OG 4367 N N . ALA A 530 ? 0.3737 0.3703 0.4658 -0.0232 0.1039 -0.0595 546 ALA A N 4368 C CA . ALA A 530 ? 0.3697 0.3693 0.4612 -0.0238 0.1034 -0.0615 546 ALA A CA 4369 C C . ALA A 530 ? 0.3718 0.3698 0.4485 -0.0233 0.1043 -0.0554 546 ALA A C 4370 O O . ALA A 530 ? 0.3634 0.3644 0.4371 -0.0226 0.1008 -0.0557 546 ALA A O 4371 C CB . ALA A 530 ? 0.3771 0.3769 0.4787 -0.0268 0.1100 -0.0669 546 ALA A CB 4372 N N . ALA A 531 ? 0.3802 0.3736 0.4481 -0.0234 0.1089 -0.0500 547 ALA A N 4373 C CA . ALA A 531 ? 0.3889 0.3807 0.4422 -0.0224 0.1092 -0.0438 547 ALA A CA 4374 C C . ALA A 531 ? 0.3886 0.3829 0.4354 -0.0196 0.1009 -0.0411 547 ALA A C 4375 O O . ALA A 531 ? 0.3923 0.3886 0.4326 -0.0189 0.0985 -0.0397 547 ALA A O 4376 C CB . ALA A 531 ? 0.3935 0.3795 0.4393 -0.0228 0.1150 -0.0387 547 ALA A CB 4377 N N . ALA A 532 ? 0.3810 0.3754 0.4302 -0.0180 0.0967 -0.0406 548 ALA A N 4378 C CA . ALA A 532 ? 0.3738 0.3707 0.4179 -0.0155 0.0890 -0.0383 548 ALA A CA 4379 C C . ALA A 532 ? 0.3647 0.3663 0.4142 -0.0152 0.0837 -0.0425 548 ALA A C 4380 O O . ALA A 532 ? 0.3578 0.3613 0.4008 -0.0140 0.0795 -0.0404 548 ALA A O 4381 C CB . ALA A 532 ? 0.3657 0.3619 0.4123 -0.0140 0.0860 -0.0377 548 ALA A CB 4382 N N . GLY A 533 ? 0.3573 0.3605 0.4191 -0.0164 0.0841 -0.0485 549 GLY A N 4383 C CA . GLY A 533 ? 0.3501 0.3576 0.4186 -0.0162 0.0793 -0.0532 549 GLY A CA 4384 C C . GLY A 533 ? 0.3527 0.3616 0.4172 -0.0170 0.0804 -0.0531 549 GLY A C 4385 O O . GLY A 533 ? 0.3433 0.3550 0.4070 -0.0159 0.0749 -0.0538 549 GLY A O 4386 N N . ALA A 534 ? 0.3481 0.3548 0.4097 -0.0189 0.0876 -0.0523 550 ALA A N 4387 C CA . ALA A 534 ? 0.3511 0.3589 0.4081 -0.0197 0.0894 -0.0523 550 ALA A CA 4388 C C . ALA A 534 ? 0.3474 0.3557 0.3924 -0.0178 0.0853 -0.0472 550 ALA A C 4389 O O . ALA A 534 ? 0.3489 0.3600 0.3930 -0.0175 0.0824 -0.0484 550 ALA A O 4390 C CB . ALA A 534 ? 0.3535 0.3583 0.4084 -0.0219 0.0982 -0.0517 550 ALA A CB 4391 N N . ALA A 535 ? 0.3465 0.3521 0.3829 -0.0165 0.0852 -0.0417 551 ALA A N 4392 C CA . ALA A 535 ? 0.3420 0.3482 0.3676 -0.0146 0.0811 -0.0369 551 ALA A CA 4393 C C . ALA A 535 ? 0.3361 0.3458 0.3647 -0.0131 0.0732 -0.0383 551 ALA A C 4394 O O . ALA A 535 ? 0.3292 0.3410 0.3535 -0.0124 0.0701 -0.0375 551 ALA A O 4395 C CB . ALA A 535 ? 0.3478 0.3504 0.3652 -0.0134 0.0823 -0.0314 551 ALA A CB 4396 N N . PHE A 536 ? 0.3324 0.3427 0.3687 -0.0125 0.0701 -0.0406 552 PHE A N 4397 C CA . PHE A 536 ? 0.3332 0.3465 0.3732 -0.0112 0.0628 -0.0424 552 PHE A CA 4398 C C . PHE A 536 ? 0.3275 0.3436 0.3736 -0.0119 0.0612 -0.0469 552 PHE A C 4399 O O . PHE A 536 ? 0.3155 0.3336 0.3593 -0.0109 0.0563 -0.0463 552 PHE A O 4400 C CB . PHE A 536 ? 0.3487 0.3619 0.3961 -0.0104 0.0602 -0.0446 552 PHE A CB 4401 C CG . PHE A 536 ? 0.3623 0.3741 0.4034 -0.0088 0.0582 -0.0401 552 PHE A CG 4402 C CD1 . PHE A 536 ? 0.3730 0.3862 0.4085 -0.0070 0.0523 -0.0373 552 PHE A CD1 4403 C CD2 . PHE A 536 ? 0.3682 0.3771 0.4089 -0.0091 0.0623 -0.0387 552 PHE A CD2 4404 C CE1 . PHE A 536 ? 0.3755 0.3876 0.4052 -0.0055 0.0506 -0.0334 552 PHE A CE1 4405 C CE2 . PHE A 536 ? 0.3760 0.3837 0.4111 -0.0075 0.0604 -0.0348 552 PHE A CE2 4406 C CZ . PHE A 536 ? 0.3757 0.3851 0.4053 -0.0057 0.0546 -0.0323 552 PHE A CZ 4407 N N . HIS A 537 ? 0.3267 0.3430 0.3810 -0.0138 0.0655 -0.0515 553 HIS A N 4408 C CA . HIS A 537 ? 0.3283 0.3473 0.3887 -0.0146 0.0645 -0.0560 553 HIS A CA 4409 C C . HIS A 537 ? 0.3283 0.3482 0.3803 -0.0146 0.0649 -0.0536 553 HIS A C 4410 O O . HIS A 537 ? 0.3221 0.3444 0.3750 -0.0139 0.0601 -0.0548 553 HIS A O 4411 C CB . HIS A 537 ? 0.3376 0.3568 0.4080 -0.0167 0.0698 -0.0615 553 HIS A CB 4412 C CG . HIS A 537 ? 0.3445 0.3665 0.4205 -0.0177 0.0696 -0.0661 553 HIS A CG 4413 N ND1 . HIS A 537 ? 0.3412 0.3660 0.4241 -0.0166 0.0633 -0.0696 553 HIS A ND1 4414 C CD2 . HIS A 537 ? 0.3549 0.3774 0.4305 -0.0195 0.0749 -0.0677 553 HIS A CD2 4415 C CE1 . HIS A 537 ? 0.3548 0.3817 0.4418 -0.0177 0.0646 -0.0734 553 HIS A CE1 4416 N NE2 . HIS A 537 ? 0.3568 0.3825 0.4395 -0.0195 0.0717 -0.0724 553 HIS A NE2 4417 N N . ASN A 538 ? 0.3425 0.3602 0.3861 -0.0154 0.0703 -0.0502 554 ASN A N 4418 C CA . ASN A 538 ? 0.3510 0.3695 0.3860 -0.0153 0.0709 -0.0479 554 ASN A CA 4419 C C . ASN A 538 ? 0.3426 0.3626 0.3717 -0.0133 0.0643 -0.0447 554 ASN A C 4420 O O . ASN A 538 ? 0.3375 0.3597 0.3651 -0.0131 0.0621 -0.0455 554 ASN A O 4421 C CB . ASN A 538 ? 0.3713 0.3866 0.3968 -0.0158 0.0773 -0.0440 554 ASN A CB 4422 C CG . ASN A 538 ? 0.3961 0.4100 0.4265 -0.0181 0.0847 -0.0470 554 ASN A CG 4423 O OD1 . ASN A 538 ? 0.4153 0.4315 0.4547 -0.0195 0.0855 -0.0524 554 ASN A OD1 4424 N ND2 . ASN A 538 ? 0.4184 0.4285 0.4428 -0.0186 0.0902 -0.0437 554 ASN A ND2 4425 N N . MET A 539 ? 0.3218 0.3405 0.3479 -0.0118 0.0613 -0.0413 555 MET A N 4426 C CA . MET A 539 ? 0.3128 0.3326 0.3330 -0.0101 0.0556 -0.0380 555 MET A CA 4427 C C . MET A 539 ? 0.3025 0.3246 0.3298 -0.0094 0.0494 -0.0408 555 MET A C 4428 O O . MET A 539 ? 0.2914 0.3154 0.3170 -0.0089 0.0457 -0.0406 555 MET A O 4429 C CB . MET A 539 ? 0.3121 0.3297 0.3259 -0.0088 0.0552 -0.0332 555 MET A CB 4430 C CG . MET A 539 ? 0.3159 0.3348 0.3241 -0.0071 0.0496 -0.0298 555 MET A CG 4431 S SD . MET A 539 ? 0.3217 0.3382 0.3223 -0.0056 0.0497 -0.0244 555 MET A SD 4432 C CE . MET A 539 ? 0.3159 0.3321 0.3252 -0.0053 0.0473 -0.0269 555 MET A CE 4433 N N . LEU A 540 ? 0.2898 0.3115 0.3248 -0.0093 0.0479 -0.0434 556 LEU A N 4434 C CA . LEU A 540 ? 0.2849 0.3082 0.3255 -0.0082 0.0415 -0.0454 556 LEU A CA 4435 C C . LEU A 540 ? 0.2820 0.3075 0.3293 -0.0089 0.0400 -0.0499 556 LEU A C 4436 O O . LEU A 540 ? 0.2833 0.3100 0.3317 -0.0079 0.0345 -0.0502 556 LEU A O 4437 C CB . LEU A 540 ? 0.2750 0.2975 0.3223 -0.0077 0.0402 -0.0475 556 LEU A CB 4438 C CG . LEU A 540 ? 0.2780 0.2985 0.3204 -0.0069 0.0412 -0.0438 556 LEU A CG 4439 C CD1 . LEU A 540 ? 0.2698 0.2902 0.3203 -0.0063 0.0393 -0.0470 556 LEU A CD1 4440 C CD2 . LEU A 540 ? 0.2727 0.2932 0.3058 -0.0054 0.0375 -0.0386 556 LEU A CD2 4441 N N . SER A 541 ? 0.2824 0.3083 0.3342 -0.0106 0.0449 -0.0534 557 SER A N 4442 C CA . SER A 541 ? 0.2841 0.3123 0.3432 -0.0112 0.0437 -0.0583 557 SER A CA 4443 C C . SER A 541 ? 0.2814 0.3110 0.3349 -0.0109 0.0415 -0.0566 557 SER A C 4444 O O . SER A 541 ? 0.2768 0.3083 0.3359 -0.0110 0.0388 -0.0600 557 SER A O 4445 C CB . SER A 541 ? 0.2878 0.3162 0.3528 -0.0133 0.0501 -0.0626 557 SER A CB 4446 O OG . SER A 541 ? 0.2981 0.3255 0.3547 -0.0142 0.0557 -0.0597 557 SER A OG 4447 N N . MET A 542 ? 0.2842 0.3129 0.3271 -0.0105 0.0426 -0.0515 558 MET A N 4448 C CA . MET A 542 ? 0.2928 0.3229 0.3297 -0.0101 0.0406 -0.0495 558 MET A CA 4449 C C . MET A 542 ? 0.2838 0.3145 0.3210 -0.0087 0.0336 -0.0482 558 MET A C 4450 O O . MET A 542 ? 0.2851 0.3174 0.3212 -0.0086 0.0311 -0.0483 558 MET A O 4451 C CB . MET A 542 ? 0.3013 0.3302 0.3269 -0.0099 0.0437 -0.0445 558 MET A CB 4452 C CG . MET A 542 ? 0.3151 0.3433 0.3382 -0.0112 0.0507 -0.0453 558 MET A CG 4453 S SD . MET A 542 ? 0.3433 0.3694 0.3529 -0.0104 0.0537 -0.0390 558 MET A SD 4454 C CE . MET A 542 ? 0.3192 0.3479 0.3227 -0.0095 0.0497 -0.0374 558 MET A CE 4455 N N . GLY A 543 ? 0.2746 0.3041 0.3132 -0.0077 0.0305 -0.0470 559 GLY A N 4456 C CA . GLY A 543 ? 0.2665 0.2960 0.3036 -0.0063 0.0243 -0.0448 559 GLY A CA 4457 C C . GLY A 543 ? 0.2715 0.3015 0.2994 -0.0059 0.0237 -0.0404 559 GLY A C 4458 O O . GLY A 543 ? 0.2616 0.2909 0.2823 -0.0059 0.0269 -0.0372 559 GLY A O 4459 N N . ALA A 544 ? 0.2739 0.3050 0.3025 -0.0056 0.0196 -0.0405 560 ALA A N 4460 C CA . ALA A 544 ? 0.2727 0.3046 0.2939 -0.0053 0.0186 -0.0370 560 ALA A CA 4461 C C . ALA A 544 ? 0.2844 0.3182 0.3061 -0.0062 0.0202 -0.0393 560 ALA A C 4462 O O . ALA A 544 ? 0.2763 0.3114 0.2949 -0.0060 0.0181 -0.0379 560 ALA A O 4463 C CB . ALA A 544 ? 0.2831 0.3146 0.3038 -0.0043 0.0130 -0.0348 560 ALA A CB 4464 N N . SER A 545 ? 0.2831 0.3174 0.3089 -0.0072 0.0241 -0.0431 561 SER A N 4465 C CA . SER A 545 ? 0.2889 0.3253 0.3155 -0.0081 0.0262 -0.0459 561 SER A CA 4466 C C . SER A 545 ? 0.3008 0.3379 0.3178 -0.0080 0.0288 -0.0429 561 SER A C 4467 O O . SER A 545 ? 0.3010 0.3401 0.3173 -0.0083 0.0290 -0.0445 561 SER A O 4468 C CB . SER A 545 ? 0.2854 0.3221 0.3185 -0.0094 0.0303 -0.0506 561 SER A CB 4469 O OG . SER A 545 ? 0.2820 0.3171 0.3116 -0.0097 0.0353 -0.0492 561 SER A OG 4470 N N . LYS A 546 ? 0.3078 0.3433 0.3177 -0.0074 0.0306 -0.0388 562 LYS A N 4471 C CA . LYS A 546 ? 0.3220 0.3578 0.3224 -0.0070 0.0329 -0.0356 562 LYS A CA 4472 C C . LYS A 546 ? 0.3093 0.3441 0.3035 -0.0057 0.0305 -0.0306 562 LYS A C 4473 O O . LYS A 546 ? 0.3073 0.3406 0.3036 -0.0053 0.0290 -0.0294 562 LYS A O 4474 C CB . LYS A 546 ? 0.3405 0.3751 0.3375 -0.0076 0.0392 -0.0358 562 LYS A CB 4475 C CG . LYS A 546 ? 0.3773 0.4131 0.3786 -0.0089 0.0425 -0.0405 562 LYS A CG 4476 C CD . LYS A 546 ? 0.4125 0.4502 0.4077 -0.0087 0.0434 -0.0405 562 LYS A CD 4477 C CE . LYS A 546 ? 0.4533 0.4922 0.4512 -0.0101 0.0478 -0.0449 562 LYS A CE 4478 N NZ . LYS A 546 ? 0.4814 0.5225 0.4895 -0.0108 0.0449 -0.0498 562 LYS A NZ 4479 N N . PRO A 547 ? 0.3044 0.3404 0.2913 -0.0049 0.0301 -0.0280 563 PRO A N 4480 C CA . PRO A 547 ? 0.2975 0.3327 0.2784 -0.0037 0.0285 -0.0234 563 PRO A CA 4481 C C . PRO A 547 ? 0.2907 0.3232 0.2692 -0.0035 0.0317 -0.0214 563 PRO A C 4482 O O . PRO A 547 ? 0.2814 0.3126 0.2592 -0.0041 0.0362 -0.0225 563 PRO A O 4483 C CB . PRO A 547 ? 0.3083 0.3451 0.2818 -0.0030 0.0289 -0.0219 563 PRO A CB 4484 C CG . PRO A 547 ? 0.3072 0.3463 0.2841 -0.0038 0.0289 -0.0258 563 PRO A CG 4485 C CD . PRO A 547 ? 0.3053 0.3434 0.2889 -0.0050 0.0314 -0.0293 563 PRO A CD 4486 N N . TRP A 548 ? 0.2795 0.3109 0.2569 -0.0027 0.0295 -0.0186 564 TRP A N 4487 C CA . TRP A 548 ? 0.2760 0.3049 0.2528 -0.0024 0.0320 -0.0172 564 TRP A CA 4488 C C . TRP A 548 ? 0.2835 0.3107 0.2538 -0.0022 0.0369 -0.0153 564 TRP A C 4489 O O . TRP A 548 ? 0.2901 0.3150 0.2622 -0.0026 0.0402 -0.0157 564 TRP A O 4490 C CB . TRP A 548 ? 0.2572 0.2856 0.2335 -0.0015 0.0287 -0.0146 564 TRP A CB 4491 C CG . TRP A 548 ? 0.2518 0.2810 0.2208 -0.0003 0.0274 -0.0107 564 TRP A CG 4492 C CD1 . TRP A 548 ? 0.2446 0.2758 0.2125 0.0000 0.0236 -0.0097 564 TRP A CD1 4493 C CD2 . TRP A 548 ? 0.2516 0.2794 0.2138 0.0006 0.0298 -0.0076 564 TRP A CD2 4494 N NE1 . TRP A 548 ? 0.2433 0.2749 0.2044 0.0011 0.0236 -0.0063 564 TRP A NE1 4495 C CE2 . TRP A 548 ? 0.2458 0.2754 0.2032 0.0016 0.0272 -0.0050 564 TRP A CE2 4496 C CE3 . TRP A 548 ? 0.2526 0.2779 0.2125 0.0007 0.0341 -0.0067 564 TRP A CE3 4497 C CZ2 . TRP A 548 ? 0.2500 0.2789 0.2006 0.0029 0.0283 -0.0017 564 TRP A CZ2 4498 C CZ3 . TRP A 548 ? 0.2570 0.2813 0.2097 0.0020 0.0353 -0.0031 564 TRP A CZ3 4499 C CH2 . TRP A 548 ? 0.2526 0.2788 0.2008 0.0032 0.0322 -0.0008 564 TRP A CH2 4500 N N . PRO A 549 ? 0.2955 0.3235 0.2584 -0.0014 0.0374 -0.0133 565 PRO A N 4501 C CA . PRO A 549 ? 0.3013 0.3270 0.2579 -0.0010 0.0422 -0.0115 565 PRO A CA 4502 C C . PRO A 549 ? 0.3057 0.3304 0.2651 -0.0025 0.0469 -0.0146 565 PRO A C 4503 O O . PRO A 549 ? 0.2974 0.3192 0.2540 -0.0026 0.0514 -0.0134 565 PRO A O 4504 C CB . PRO A 549 ? 0.2967 0.3240 0.2454 0.0001 0.0413 -0.0095 565 PRO A CB 4505 C CG . PRO A 549 ? 0.2928 0.3227 0.2432 0.0006 0.0359 -0.0090 565 PRO A CG 4506 C CD . PRO A 549 ? 0.2897 0.3204 0.2492 -0.0006 0.0340 -0.0124 565 PRO A CD 4507 N N . ASP A 550 ? 0.3156 0.3425 0.2808 -0.0036 0.0459 -0.0185 566 ASP A N 4508 C CA . ASP A 550 ? 0.3261 0.3524 0.2954 -0.0052 0.0502 -0.0221 566 ASP A CA 4509 C C . ASP A 550 ? 0.3257 0.3501 0.3022 -0.0061 0.0518 -0.0237 566 ASP A C 4510 O O . ASP A 550 ? 0.3287 0.3514 0.3068 -0.0073 0.0569 -0.0252 566 ASP A O 4511 C CB . ASP A 550 ? 0.3441 0.3735 0.3188 -0.0060 0.0482 -0.0263 566 ASP A CB 4512 C CG . ASP A 550 ? 0.3662 0.3977 0.3343 -0.0053 0.0478 -0.0258 566 ASP A CG 4513 O OD1 . ASP A 550 ? 0.3848 0.4151 0.3442 -0.0045 0.0505 -0.0231 566 ASP A OD1 4514 O OD2 . ASP A 550 ? 0.3749 0.4093 0.3467 -0.0055 0.0445 -0.0282 566 ASP A OD2 4515 N N . ALA A 551 ? 0.3052 0.3299 0.2864 -0.0057 0.0476 -0.0234 567 ALA A N 4516 C CA . ALA A 551 ? 0.3066 0.3297 0.2947 -0.0063 0.0484 -0.0251 567 ALA A CA 4517 C C . ALA A 551 ? 0.3088 0.3287 0.2926 -0.0058 0.0518 -0.0219 567 ALA A C 4518 O O . ALA A 551 ? 0.3121 0.3302 0.3003 -0.0068 0.0555 -0.0236 567 ALA A O 4519 C CB . ALA A 551 ? 0.2897 0.3140 0.2831 -0.0056 0.0426 -0.0257 567 ALA A CB 4520 N N . LEU A 552 ? 0.3099 0.3293 0.2857 -0.0044 0.0507 -0.0175 568 LEU A N 4521 C CA . LEU A 552 ? 0.3188 0.3350 0.2897 -0.0038 0.0538 -0.0142 568 LEU A CA 4522 C C . LEU A 552 ? 0.3325 0.3464 0.2998 -0.0046 0.0600 -0.0142 568 LEU A C 4523 O O . LEU A 552 ? 0.3292 0.3400 0.2976 -0.0052 0.0642 -0.0139 568 LEU A O 4524 C CB . LEU A 552 ? 0.3234 0.3398 0.2863 -0.0019 0.0511 -0.0098 568 LEU A CB 4525 C CG . LEU A 552 ? 0.3349 0.3480 0.2923 -0.0009 0.0537 -0.0061 568 LEU A CG 4526 C CD1 . LEU A 552 ? 0.3326 0.3438 0.2961 -0.0013 0.0544 -0.0068 568 LEU A CD1 4527 C CD2 . LEU A 552 ? 0.3270 0.3410 0.2772 0.0009 0.0504 -0.0023 568 LEU A CD2 4528 N N . GLU A 553 ? 0.3349 0.3503 0.2982 -0.0047 0.0606 -0.0147 569 GLU A N 4529 C CA . GLU A 553 ? 0.3536 0.3670 0.3125 -0.0055 0.0665 -0.0148 569 GLU A CA 4530 C C . GLU A 553 ? 0.3536 0.3659 0.3207 -0.0077 0.0709 -0.0187 569 GLU A C 4531 O O . GLU A 553 ? 0.3615 0.3705 0.3265 -0.0084 0.0765 -0.0177 569 GLU A O 4532 C CB . GLU A 553 ? 0.3731 0.3890 0.3271 -0.0052 0.0659 -0.0154 569 GLU A CB 4533 C CG . GLU A 553 ? 0.4077 0.4211 0.3534 -0.0053 0.0715 -0.0139 569 GLU A CG 4534 C CD . GLU A 553 ? 0.4335 0.4495 0.3732 -0.0046 0.0705 -0.0144 569 GLU A CD 4535 O OE1 . GLU A 553 ? 0.4385 0.4582 0.3806 -0.0041 0.0654 -0.0158 569 GLU A OE1 4536 O OE2 . GLU A 553 ? 0.4610 0.4752 0.3935 -0.0045 0.0748 -0.0135 569 GLU A OE2 4537 N N . ALA A 554 ? 0.3497 0.3647 0.3263 -0.0086 0.0683 -0.0230 570 ALA A N 4538 C CA . ALA A 554 ? 0.3546 0.3692 0.3407 -0.0106 0.0716 -0.0274 570 ALA A CA 4539 C C . ALA A 554 ? 0.3549 0.3664 0.3442 -0.0108 0.0739 -0.0265 570 ALA A C 4540 O O . ALA A 554 ? 0.3579 0.3676 0.3519 -0.0125 0.0790 -0.0288 570 ALA A O 4541 C CB . ALA A 554 ? 0.3421 0.3601 0.3378 -0.0110 0.0671 -0.0319 570 ALA A CB 4542 N N . PHE A 555 ? 0.3444 0.3552 0.3314 -0.0093 0.0703 -0.0233 571 PHE A N 4543 C CA . PHE A 555 ? 0.3507 0.3588 0.3407 -0.0093 0.0719 -0.0225 571 PHE A CA 4544 C C . PHE A 555 ? 0.3582 0.3620 0.3408 -0.0092 0.0775 -0.0187 571 PHE A C 4545 O O . PHE A 555 ? 0.3585 0.3595 0.3452 -0.0106 0.0825 -0.0199 571 PHE A O 4546 C CB . PHE A 555 ? 0.3417 0.3508 0.3323 -0.0076 0.0660 -0.0208 571 PHE A CB 4547 C CG . PHE A 555 ? 0.3443 0.3514 0.3405 -0.0077 0.0668 -0.0214 571 PHE A CG 4548 C CD1 . PHE A 555 ? 0.3543 0.3580 0.3455 -0.0070 0.0695 -0.0178 571 PHE A CD1 4549 C CD2 . PHE A 555 ? 0.3431 0.3518 0.3497 -0.0082 0.0645 -0.0258 571 PHE A CD2 4550 C CE1 . PHE A 555 ? 0.3488 0.3509 0.3458 -0.0071 0.0702 -0.0186 571 PHE A CE1 4551 C CE2 . PHE A 555 ? 0.3455 0.3528 0.3575 -0.0081 0.0649 -0.0268 571 PHE A CE2 4552 C CZ . PHE A 555 ? 0.3461 0.3501 0.3534 -0.0077 0.0679 -0.0232 571 PHE A CZ 4553 N N . ASN A 556 ? 0.3612 0.3642 0.3331 -0.0077 0.0767 -0.0142 572 ASN A N 4554 C CA . ASN A 556 ? 0.3822 0.3807 0.3463 -0.0071 0.0811 -0.0100 572 ASN A CA 4555 C C . ASN A 556 ? 0.3889 0.3867 0.3414 -0.0061 0.0824 -0.0067 572 ASN A C 4556 O O . ASN A 556 ? 0.3947 0.3889 0.3393 -0.0049 0.0845 -0.0025 572 ASN A O 4557 C CB . ASN A 556 ? 0.3733 0.3703 0.3365 -0.0056 0.0786 -0.0070 572 ASN A CB 4558 C CG . ASN A 556 ? 0.3773 0.3770 0.3351 -0.0034 0.0725 -0.0045 572 ASN A CG 4559 O OD1 . ASN A 556 ? 0.3695 0.3719 0.3235 -0.0030 0.0703 -0.0046 572 ASN A OD1 4560 N ND2 . ASN A 556 ? 0.3681 0.3672 0.3260 -0.0022 0.0699 -0.0025 572 ASN A ND2 4561 N N . GLY A 557 ? 0.3967 0.3978 0.3482 -0.0063 0.0808 -0.0087 573 GLY A N 4562 C CA . GLY A 557 ? 0.4114 0.4123 0.3522 -0.0052 0.0817 -0.0063 573 GLY A CA 4563 C C . GLY A 557 ? 0.4166 0.4189 0.3500 -0.0026 0.0766 -0.0028 573 GLY A C 4564 O O . GLY A 557 ? 0.4224 0.4249 0.3471 -0.0014 0.0767 -0.0009 573 GLY A O 4565 N N . GLU A 558 ? 0.4156 0.4191 0.3527 -0.0018 0.0721 -0.0020 574 GLU A N 4566 C CA . GLU A 558 ? 0.4149 0.4200 0.3461 0.0003 0.0672 0.0009 574 GLU A CA 4567 C C . GLU A 558 ? 0.3927 0.4028 0.3276 0.0003 0.0619 -0.0014 574 GLU A C 4568 O O . GLU A 558 ? 0.3762 0.3882 0.3193 -0.0011 0.0612 -0.0052 574 GLU A O 4569 C CB . GLU A 558 ? 0.4383 0.4417 0.3705 0.0013 0.0657 0.0034 574 GLU A CB 4570 C CG . GLU A 558 ? 0.4765 0.4746 0.4060 0.0013 0.0710 0.0057 574 GLU A CG 4571 C CD . GLU A 558 ? 0.5082 0.5044 0.4369 0.0027 0.0696 0.0086 574 GLU A CD 4572 O OE1 . GLU A 558 ? 0.4931 0.4921 0.4256 0.0033 0.0648 0.0082 574 GLU A OE1 4573 O OE2 . GLU A 558 ? 0.5407 0.5324 0.4650 0.0032 0.0734 0.0115 574 GLU A OE2 4574 N N . ARG A 559 ? 0.3881 0.4003 0.3172 0.0020 0.0582 0.0006 575 ARG A N 4575 C CA . ARG A 559 ? 0.3756 0.3922 0.3076 0.0020 0.0533 -0.0013 575 ARG A CA 4576 C C . ARG A 559 ? 0.3735 0.3919 0.3044 0.0035 0.0484 0.0008 575 ARG A C 4577 O O . ARG A 559 ? 0.3642 0.3860 0.2974 0.0036 0.0443 -0.0003 575 ARG A O 4578 C CB . ARG A 559 ? 0.3770 0.3955 0.3040 0.0023 0.0537 -0.0023 575 ARG A CB 4579 C CG . ARG A 559 ? 0.3768 0.3943 0.3052 0.0007 0.0584 -0.0051 575 ARG A CG 4580 C CD . ARG A 559 ? 0.3786 0.3985 0.3020 0.0011 0.0583 -0.0064 575 ARG A CD 4581 N NE . ARG A 559 ? 0.3704 0.3947 0.2975 0.0013 0.0529 -0.0082 575 ARG A NE 4582 C CZ . ARG A 559 ? 0.3611 0.3879 0.2966 -0.0001 0.0513 -0.0121 575 ARG A CZ 4583 N NH1 . ARG A 559 ? 0.3530 0.3787 0.2945 -0.0019 0.0546 -0.0150 575 ARG A NH1 4584 N NH2 . ARG A 559 ? 0.3622 0.3925 0.3004 0.0001 0.0464 -0.0133 575 ARG A NH2 4585 N N . ILE A 560 ? 0.3685 0.3844 0.2963 0.0047 0.0489 0.0040 576 ILE A N 4586 C CA . ILE A 560 ? 0.3662 0.3836 0.2918 0.0063 0.0449 0.0064 576 ILE A CA 4587 C C . ILE A 560 ? 0.3573 0.3737 0.2880 0.0061 0.0439 0.0068 576 ILE A C 4588 O O . ILE A 560 ? 0.3454 0.3585 0.2773 0.0058 0.0472 0.0072 576 ILE A O 4589 C CB . ILE A 560 ? 0.3856 0.4015 0.3017 0.0084 0.0458 0.0099 576 ILE A CB 4590 C CG1 . ILE A 560 ? 0.4053 0.4232 0.3163 0.0090 0.0454 0.0093 576 ILE A CG1 4591 C CG2 . ILE A 560 ? 0.3976 0.4149 0.3121 0.0101 0.0421 0.0123 576 ILE A CG2 4592 C CD1 . ILE A 560 ? 0.4351 0.4507 0.3363 0.0110 0.0473 0.0122 576 ILE A CD1 4593 N N . MET A 561 ? 0.3449 0.3641 0.2787 0.0063 0.0396 0.0066 577 MET A N 4594 C CA . MET A 561 ? 0.3314 0.3500 0.2686 0.0065 0.0382 0.0073 577 MET A CA 4595 C C . MET A 561 ? 0.3355 0.3525 0.2667 0.0084 0.0388 0.0108 577 MET A C 4596 O O . MET A 561 ? 0.3318 0.3504 0.2577 0.0097 0.0371 0.0126 577 MET A O 4597 C CB . MET A 561 ? 0.3266 0.3484 0.2675 0.0063 0.0335 0.0063 577 MET A CB 4598 C CG . MET A 561 ? 0.3245 0.3460 0.2681 0.0067 0.0318 0.0071 577 MET A CG 4599 S SD . MET A 561 ? 0.3143 0.3392 0.2619 0.0062 0.0267 0.0060 577 MET A SD 4600 C CE . MET A 561 ? 0.3073 0.3349 0.2488 0.0073 0.0245 0.0085 577 MET A CE 4601 N N . SER A 562 ? 0.3409 0.3549 0.2733 0.0085 0.0411 0.0116 578 SER A N 4602 C CA . SER A 562 ? 0.3509 0.3627 0.2778 0.0103 0.0421 0.0148 578 SER A CA 4603 C C . SER A 562 ? 0.3392 0.3496 0.2696 0.0106 0.0422 0.0152 578 SER A C 4604 O O . SER A 562 ? 0.3441 0.3530 0.2802 0.0093 0.0438 0.0132 578 SER A O 4605 C CB . SER A 562 ? 0.3649 0.3730 0.2867 0.0105 0.0466 0.0161 578 SER A CB 4606 O OG . SER A 562 ? 0.3734 0.3783 0.2915 0.0120 0.0483 0.0190 578 SER A OG 4607 N N . GLY A 563 ? 0.3395 0.3503 0.2666 0.0123 0.0404 0.0176 579 GLY A N 4608 C CA . GLY A 563 ? 0.3316 0.3412 0.2615 0.0129 0.0404 0.0180 579 GLY A CA 4609 C C . GLY A 563 ? 0.3351 0.3399 0.2630 0.0135 0.0444 0.0197 579 GLY A C 4610 O O . GLY A 563 ? 0.3221 0.3255 0.2519 0.0142 0.0446 0.0202 579 GLY A O 4611 N N . LYS A 564 ? 0.3405 0.3426 0.2645 0.0133 0.0477 0.0206 580 LYS A N 4612 C CA . LYS A 564 ? 0.3600 0.3569 0.2814 0.0138 0.0519 0.0225 580 LYS A CA 4613 C C . LYS A 564 ? 0.3464 0.3409 0.2752 0.0124 0.0546 0.0206 580 LYS A C 4614 O O . LYS A 564 ? 0.3450 0.3363 0.2739 0.0132 0.0563 0.0221 580 LYS A O 4615 C CB . LYS A 564 ? 0.3875 0.3820 0.3031 0.0136 0.0551 0.0236 580 LYS A CB 4616 C CG . LYS A 564 ? 0.4547 0.4433 0.3667 0.0142 0.0598 0.0261 580 LYS A CG 4617 C CD . LYS A 564 ? 0.4881 0.4743 0.3938 0.0139 0.0633 0.0271 580 LYS A CD 4618 C CE . LYS A 564 ? 0.5339 0.5136 0.4373 0.0138 0.0687 0.0293 580 LYS A CE 4619 N NZ . LYS A 564 ? 0.5746 0.5517 0.4713 0.0135 0.0724 0.0303 580 LYS A NZ 4620 N N . ALA A 565 ? 0.3276 0.3237 0.2628 0.0104 0.0548 0.0172 581 ALA A N 4621 C CA . ALA A 565 ? 0.3214 0.3153 0.2640 0.0089 0.0575 0.0148 581 ALA A CA 4622 C C . ALA A 565 ? 0.3173 0.3124 0.2646 0.0096 0.0548 0.0140 581 ALA A C 4623 O O . ALA A 565 ? 0.3232 0.3153 0.2736 0.0096 0.0572 0.0139 581 ALA A O 4624 C CB . ALA A 565 ? 0.3136 0.3091 0.2619 0.0068 0.0581 0.0111 581 ALA A CB 4625 N N . ILE A 566 ? 0.3078 0.3072 0.2557 0.0102 0.0501 0.0133 582 ILE A N 4626 C CA . ILE A 566 ? 0.3020 0.3027 0.2534 0.0110 0.0474 0.0126 582 ILE A CA 4627 C C . ILE A 566 ? 0.3091 0.3077 0.2565 0.0128 0.0482 0.0156 582 ILE A C 4628 O O . ILE A 566 ? 0.3048 0.3022 0.2562 0.0131 0.0487 0.0148 582 ILE A O 4629 C CB . ILE A 566 ? 0.3008 0.3064 0.2531 0.0111 0.0424 0.0115 582 ILE A CB 4630 C CG1 . ILE A 566 ? 0.2922 0.2989 0.2489 0.0116 0.0402 0.0100 582 ILE A CG1 4631 C CG2 . ILE A 566 ? 0.3028 0.3105 0.2481 0.0123 0.0402 0.0142 582 ILE A CG2 4632 C CD1 . ILE A 566 ? 0.2891 0.2999 0.2471 0.0116 0.0357 0.0087 582 ILE A CD1 4633 N N . ALA A 567 ? 0.3157 0.3137 0.2557 0.0141 0.0482 0.0188 583 ALA A N 4634 C CA . ALA A 567 ? 0.3301 0.3259 0.2663 0.0160 0.0488 0.0216 583 ALA A CA 4635 C C . ALA A 567 ? 0.3438 0.3340 0.2812 0.0157 0.0536 0.0224 583 ALA A C 4636 O O . ALA A 567 ? 0.3401 0.3281 0.2787 0.0168 0.0542 0.0232 583 ALA A O 4637 C CB . ALA A 567 ? 0.3374 0.3339 0.2655 0.0177 0.0474 0.0246 583 ALA A CB 4638 N N . GLU A 568 ? 0.3500 0.3377 0.2873 0.0142 0.0572 0.0219 584 GLU A N 4639 C CA . GLU A 568 ? 0.3658 0.3479 0.3047 0.0135 0.0624 0.0224 584 GLU A CA 4640 C C . GLU A 568 ? 0.3545 0.3364 0.3027 0.0125 0.0629 0.0193 584 GLU A C 4641 O O . GLU A 568 ? 0.3575 0.3358 0.3073 0.0131 0.0651 0.0202 584 GLU A O 4642 C CB . GLU A 568 ? 0.3860 0.3664 0.3236 0.0117 0.0660 0.0219 584 GLU A CB 4643 C CG . GLU A 568 ? 0.4153 0.3895 0.3524 0.0109 0.0721 0.0232 584 GLU A CG 4644 C CD . GLU A 568 ? 0.4435 0.4166 0.3781 0.0093 0.0754 0.0228 584 GLU A CD 4645 O OE1 . GLU A 568 ? 0.4552 0.4309 0.3839 0.0099 0.0734 0.0237 584 GLU A OE1 4646 O OE2 . GLU A 568 ? 0.4493 0.4194 0.3884 0.0074 0.0802 0.0213 584 GLU A OE2 4647 N N . TYR A 569 ? 0.3370 0.3227 0.2913 0.0112 0.0607 0.0156 585 TYR A N 4648 C CA . TYR A 569 ? 0.3270 0.3132 0.2902 0.0105 0.0605 0.0122 585 TYR A CA 4649 C C . TYR A 569 ? 0.3264 0.3127 0.2897 0.0124 0.0584 0.0132 585 TYR A C 4650 O O . TYR A 569 ? 0.3222 0.3059 0.2904 0.0123 0.0606 0.0122 585 TYR A O 4651 C CB . TYR A 569 ? 0.3126 0.3036 0.2807 0.0095 0.0569 0.0085 585 TYR A CB 4652 C CG . TYR A 569 ? 0.3068 0.2984 0.2843 0.0088 0.0566 0.0044 585 TYR A CG 4653 C CD1 . TYR A 569 ? 0.3053 0.2987 0.2853 0.0101 0.0535 0.0035 585 TYR A CD1 4654 C CD2 . TYR A 569 ? 0.3048 0.2957 0.2891 0.0068 0.0591 0.0010 585 TYR A CD2 4655 C CE1 . TYR A 569 ? 0.3008 0.2950 0.2893 0.0096 0.0529 -0.0006 585 TYR A CE1 4656 C CE2 . TYR A 569 ? 0.3038 0.2955 0.2971 0.0063 0.0584 -0.0031 585 TYR A CE2 4657 C CZ . TYR A 569 ? 0.3002 0.2937 0.2955 0.0077 0.0552 -0.0040 585 TYR A CZ 4658 O OH . TYR A 569 ? 0.3059 0.3004 0.3101 0.0073 0.0543 -0.0084 585 TYR A OH 4659 N N . PHE A 570 ? 0.3260 0.3155 0.2844 0.0140 0.0545 0.0149 586 PHE A N 4660 C CA . PHE A 570 ? 0.3256 0.3164 0.2847 0.0157 0.0520 0.0152 586 PHE A CA 4661 C C . PHE A 570 ? 0.3400 0.3274 0.2938 0.0176 0.0534 0.0189 586 PHE A C 4662 O O . PHE A 570 ? 0.3454 0.3338 0.2998 0.0191 0.0515 0.0191 586 PHE A O 4663 C CB . PHE A 570 ? 0.3072 0.3035 0.2651 0.0163 0.0469 0.0144 586 PHE A CB 4664 C CG . PHE A 570 ? 0.3044 0.3035 0.2685 0.0150 0.0450 0.0106 586 PHE A CG 4665 C CD1 . PHE A 570 ? 0.2929 0.2924 0.2636 0.0150 0.0445 0.0076 586 PHE A CD1 4666 C CD2 . PHE A 570 ? 0.2955 0.2969 0.2591 0.0138 0.0437 0.0097 586 PHE A CD2 4667 C CE1 . PHE A 570 ? 0.2862 0.2881 0.2624 0.0141 0.0425 0.0040 586 PHE A CE1 4668 C CE2 . PHE A 570 ? 0.2972 0.3008 0.2664 0.0128 0.0417 0.0061 586 PHE A CE2 4669 C CZ . PHE A 570 ? 0.2832 0.2871 0.2585 0.0130 0.0410 0.0033 586 PHE A CZ 4670 N N . GLU A 571 ? 0.3514 0.3349 0.3002 0.0175 0.0566 0.0217 587 GLU A N 4671 C CA . GLU A 571 ? 0.3696 0.3495 0.3126 0.0196 0.0577 0.0254 587 GLU A CA 4672 C C . GLU A 571 ? 0.3634 0.3402 0.3107 0.0204 0.0591 0.0253 587 GLU A C 4673 O O . GLU A 571 ? 0.3621 0.3390 0.3067 0.0225 0.0573 0.0271 587 GLU A O 4674 C CB . GLU A 571 ? 0.3871 0.3627 0.3237 0.0194 0.0613 0.0283 587 GLU A CB 4675 C CG . GLU A 571 ? 0.4282 0.3993 0.3583 0.0216 0.0626 0.0325 587 GLU A CG 4676 C CD . GLU A 571 ? 0.4507 0.4250 0.3748 0.0241 0.0582 0.0344 587 GLU A CD 4677 O OE1 . GLU A 571 ? 0.4570 0.4370 0.3811 0.0239 0.0545 0.0329 587 GLU A OE1 4678 O OE2 . GLU A 571 ? 0.4765 0.4475 0.3962 0.0263 0.0585 0.0375 587 GLU A OE2 4679 N N . PRO A 572 ? 0.3660 0.3404 0.3207 0.0188 0.0622 0.0229 588 PRO A N 4680 C CA . PRO A 572 ? 0.3652 0.3369 0.3245 0.0196 0.0633 0.0224 588 PRO A CA 4681 C C . PRO A 572 ? 0.3585 0.3351 0.3211 0.0208 0.0588 0.0203 588 PRO A C 4682 O O . PRO A 572 ? 0.3512 0.3265 0.3142 0.0225 0.0584 0.0211 588 PRO A O 4683 C CB . PRO A 572 ? 0.3745 0.3438 0.3421 0.0173 0.0671 0.0193 588 PRO A CB 4684 C CG . PRO A 572 ? 0.3840 0.3529 0.3492 0.0154 0.0692 0.0195 588 PRO A CG 4685 C CD . PRO A 572 ? 0.3736 0.3474 0.3329 0.0162 0.0649 0.0202 588 PRO A CD 4686 N N . LEU A 573 ? 0.3492 0.3312 0.3136 0.0200 0.0555 0.0176 589 LEU A N 4687 C CA . LEU A 573 ? 0.3404 0.3274 0.3067 0.0212 0.0512 0.0157 589 LEU A CA 4688 C C . LEU A 573 ? 0.3469 0.3358 0.3062 0.0232 0.0486 0.0187 589 LEU A C 4689 O O . LEU A 573 ? 0.3478 0.3382 0.3081 0.0248 0.0467 0.0184 589 LEU A O 4690 C CB . LEU A 573 ? 0.3299 0.3217 0.2990 0.0198 0.0484 0.0125 589 LEU A CB 4691 C CG . LEU A 573 ? 0.3238 0.3207 0.2943 0.0209 0.0441 0.0106 589 LEU A CG 4692 C CD1 . LEU A 573 ? 0.3227 0.3189 0.2999 0.0214 0.0445 0.0078 589 LEU A CD1 4693 C CD2 . LEU A 573 ? 0.3147 0.3157 0.2861 0.0197 0.0412 0.0084 589 LEU A CD2 4694 N N . ARG A 574 ? 0.3541 0.3431 0.3067 0.0233 0.0484 0.0213 590 ARG A N 4695 C CA . ARG A 574 ? 0.3607 0.3517 0.3070 0.0253 0.0458 0.0240 590 ARG A CA 4696 C C . ARG A 574 ? 0.3636 0.3509 0.3083 0.0274 0.0469 0.0263 590 ARG A C 4697 O O . ARG A 574 ? 0.3520 0.3419 0.2960 0.0291 0.0443 0.0265 590 ARG A O 4698 C CB . ARG A 574 ? 0.3659 0.3572 0.3056 0.0250 0.0457 0.0262 590 ARG A CB 4699 C CG . ARG A 574 ? 0.3769 0.3710 0.3109 0.0270 0.0426 0.0283 590 ARG A CG 4700 C CD . ARG A 574 ? 0.3948 0.3882 0.3219 0.0273 0.0429 0.0307 590 ARG A CD 4701 N NE . ARG A 574 ? 0.4199 0.4071 0.3436 0.0279 0.0466 0.0332 590 ARG A NE 4702 C CZ . ARG A 574 ? 0.4413 0.4250 0.3614 0.0301 0.0471 0.0359 590 ARG A CZ 4703 N NH1 . ARG A 574 ? 0.4462 0.4325 0.3663 0.0321 0.0442 0.0362 590 ARG A NH1 4704 N NH2 . ARG A 574 ? 0.4542 0.4318 0.3708 0.0304 0.0507 0.0384 590 ARG A NH2 4705 N N . VAL A 575 ? 0.3731 0.3544 0.3171 0.0272 0.0509 0.0281 591 VAL A N 4706 C CA . VAL A 575 ? 0.3825 0.3592 0.3251 0.0292 0.0523 0.0304 591 VAL A CA 4707 C C . VAL A 575 ? 0.3762 0.3542 0.3256 0.0299 0.0512 0.0279 591 VAL A C 4708 O O . VAL A 575 ? 0.3837 0.3627 0.3318 0.0320 0.0492 0.0288 591 VAL A O 4709 C CB . VAL A 575 ? 0.3967 0.3660 0.3379 0.0286 0.0573 0.0327 591 VAL A CB 4710 C CG1 . VAL A 575 ? 0.4058 0.3699 0.3464 0.0306 0.0588 0.0351 591 VAL A CG1 4711 C CG2 . VAL A 575 ? 0.3997 0.3679 0.3330 0.0284 0.0581 0.0354 591 VAL A CG2 4712 N N . TRP A 576 ? 0.3682 0.3465 0.3249 0.0281 0.0524 0.0245 592 TRP A N 4713 C CA . TRP A 576 ? 0.3625 0.3420 0.3260 0.0286 0.0515 0.0216 592 TRP A CA 4714 C C . TRP A 576 ? 0.3489 0.3351 0.3120 0.0297 0.0469 0.0200 592 TRP A C 4715 O O . TRP A 576 ? 0.3388 0.3258 0.3037 0.0314 0.0456 0.0195 592 TRP A O 4716 C CB . TRP A 576 ? 0.3748 0.3540 0.3465 0.0265 0.0533 0.0177 592 TRP A CB 4717 C CG . TRP A 576 ? 0.3803 0.3612 0.3588 0.0272 0.0521 0.0144 592 TRP A CG 4718 C CD1 . TRP A 576 ? 0.3896 0.3663 0.3725 0.0279 0.0544 0.0142 592 TRP A CD1 4719 C CD2 . TRP A 576 ? 0.3847 0.3717 0.3659 0.0275 0.0482 0.0110 592 TRP A CD2 4720 N NE1 . TRP A 576 ? 0.3871 0.3674 0.3758 0.0286 0.0521 0.0105 592 TRP A NE1 4721 C CE2 . TRP A 576 ? 0.3871 0.3737 0.3744 0.0284 0.0483 0.0086 592 TRP A CE2 4722 C CE3 . TRP A 576 ? 0.3905 0.3832 0.3694 0.0270 0.0447 0.0099 592 TRP A CE3 4723 C CZ2 . TRP A 576 ? 0.3866 0.3784 0.3774 0.0290 0.0451 0.0049 592 TRP A CZ2 4724 C CZ3 . TRP A 576 ? 0.3927 0.3902 0.3747 0.0276 0.0416 0.0065 592 TRP A CZ3 4725 C CH2 . TRP A 576 ? 0.3945 0.3917 0.3823 0.0286 0.0418 0.0040 592 TRP A CH2 4726 N N . LEU A 577 ? 0.3330 0.3238 0.2939 0.0288 0.0445 0.0192 593 LEU A N 4727 C CA . LEU A 577 ? 0.3219 0.3189 0.2826 0.0294 0.0405 0.0176 593 LEU A CA 4728 C C . LEU A 577 ? 0.3249 0.3235 0.2803 0.0315 0.0386 0.0201 593 LEU A C 4729 O O . LEU A 577 ? 0.3079 0.3100 0.2646 0.0327 0.0364 0.0189 593 LEU A O 4730 C CB . LEU A 577 ? 0.3110 0.3120 0.2710 0.0277 0.0387 0.0162 593 LEU A CB 4731 C CG . LEU A 577 ? 0.3099 0.3170 0.2696 0.0279 0.0349 0.0146 593 LEU A CG 4732 C CD1 . LEU A 577 ? 0.3011 0.3098 0.2662 0.0285 0.0340 0.0113 593 LEU A CD1 4733 C CD2 . LEU A 577 ? 0.3010 0.3106 0.2600 0.0261 0.0336 0.0136 593 LEU A CD2 4734 N N . GLU A 578 ? 0.3300 0.3263 0.2796 0.0321 0.0394 0.0235 594 GLU A N 4735 C CA . GLU A 578 ? 0.3367 0.3344 0.2814 0.0343 0.0374 0.0258 594 GLU A CA 4736 C C . GLU A 578 ? 0.3396 0.3349 0.2865 0.0364 0.0378 0.0260 594 GLU A C 4737 O O . GLU A 578 ? 0.3441 0.3428 0.2907 0.0380 0.0354 0.0257 594 GLU A O 4738 C CB . GLU A 578 ? 0.3457 0.3406 0.2837 0.0347 0.0383 0.0292 594 GLU A CB 4739 C CG . GLU A 578 ? 0.3628 0.3613 0.2976 0.0333 0.0369 0.0291 594 GLU A CG 4740 C CD . GLU A 578 ? 0.3924 0.3887 0.3204 0.0340 0.0374 0.0322 594 GLU A CD 4741 O OE1 . GLU A 578 ? 0.4209 0.4136 0.3456 0.0362 0.0381 0.0347 594 GLU A OE1 4742 O OE2 . GLU A 578 ? 0.4034 0.4013 0.3292 0.0326 0.0372 0.0321 594 GLU A OE2 4743 N N . ALA A 579 ? 0.3370 0.3267 0.2869 0.0361 0.0410 0.0263 595 ALA A N 4744 C CA . ALA A 579 ? 0.3446 0.3310 0.2972 0.0380 0.0418 0.0265 595 ALA A CA 4745 C C . ALA A 579 ? 0.3404 0.3309 0.2996 0.0380 0.0403 0.0226 595 ALA A C 4746 O O . ALA A 579 ? 0.3438 0.3352 0.3043 0.0400 0.0389 0.0222 595 ALA A O 4747 C CB . ALA A 579 ? 0.3511 0.3300 0.3051 0.0375 0.0461 0.0280 595 ALA A CB 4748 N N . GLU A 580 ? 0.3329 0.3259 0.2962 0.0360 0.0403 0.0195 596 GLU A N 4749 C CA . GLU A 580 ? 0.3309 0.3276 0.3000 0.0360 0.0387 0.0155 596 GLU A CA 4750 C C . GLU A 580 ? 0.3191 0.3224 0.2860 0.0369 0.0351 0.0146 596 GLU A C 4751 O O . GLU A 580 ? 0.3249 0.3308 0.2951 0.0381 0.0338 0.0124 596 GLU A O 4752 C CB . GLU A 580 ? 0.3415 0.3391 0.3151 0.0337 0.0393 0.0124 596 GLU A CB 4753 C CG . GLU A 580 ? 0.3621 0.3629 0.3421 0.0339 0.0380 0.0080 596 GLU A CG 4754 C CD . GLU A 580 ? 0.3897 0.3863 0.3758 0.0346 0.0402 0.0067 596 GLU A CD 4755 O OE1 . GLU A 580 ? 0.4023 0.3931 0.3876 0.0350 0.0430 0.0095 596 GLU A OE1 4756 O OE2 . GLU A 580 ? 0.4032 0.4023 0.3949 0.0349 0.0392 0.0028 596 GLU A OE2 4757 N N . ASN A 581 ? 0.3026 0.3087 0.2642 0.0364 0.0336 0.0162 597 ASN A N 4758 C CA . ASN A 581 ? 0.2966 0.3086 0.2557 0.0370 0.0306 0.0158 597 ASN A CA 4759 C C . ASN A 581 ? 0.3071 0.3192 0.2646 0.0395 0.0298 0.0173 597 ASN A C 4760 O O . ASN A 581 ? 0.3044 0.3210 0.2629 0.0405 0.0279 0.0156 597 ASN A O 4761 C CB . ASN A 581 ? 0.2791 0.2936 0.2335 0.0357 0.0295 0.0171 597 ASN A CB 4762 C CG . ASN A 581 ? 0.2762 0.2930 0.2326 0.0335 0.0289 0.0147 597 ASN A CG 4763 O OD1 . ASN A 581 ? 0.2666 0.2849 0.2274 0.0333 0.0285 0.0117 597 ASN A OD1 4764 N ND2 . ASN A 581 ? 0.2656 0.2829 0.2188 0.0321 0.0286 0.0159 597 ASN A ND2 4765 N N . ILE A 582 ? 0.3249 0.3320 0.2797 0.0407 0.0313 0.0204 598 ILE A N 4766 C CA . ILE A 582 ? 0.3461 0.3523 0.2996 0.0434 0.0305 0.0218 598 ILE A CA 4767 C C . ILE A 582 ? 0.3558 0.3608 0.3153 0.0445 0.0311 0.0196 598 ILE A C 4768 O O . ILE A 582 ? 0.3635 0.3719 0.3245 0.0461 0.0293 0.0183 598 ILE A O 4769 C CB . ILE A 582 ? 0.3482 0.3487 0.2966 0.0445 0.0318 0.0259 598 ILE A CB 4770 C CG1 . ILE A 582 ? 0.3485 0.3519 0.2910 0.0440 0.0303 0.0276 598 ILE A CG1 4771 C CG2 . ILE A 582 ? 0.3605 0.3586 0.3087 0.0475 0.0313 0.0273 598 ILE A CG2 4772 C CD1 . ILE A 582 ? 0.3685 0.3666 0.3053 0.0446 0.0318 0.0313 598 ILE A CD1 4773 N N . LYS A 583 ? 0.3729 0.3734 0.3364 0.0435 0.0336 0.0189 599 LYS A N 4774 C CA . LYS A 583 ? 0.3904 0.3894 0.3603 0.0445 0.0344 0.0165 599 LYS A CA 4775 C C . LYS A 583 ? 0.3880 0.3937 0.3615 0.0445 0.0321 0.0125 599 LYS A C 4776 O O . LYS A 583 ? 0.3782 0.3849 0.3551 0.0462 0.0314 0.0108 599 LYS A O 4777 C CB . LYS A 583 ? 0.4147 0.4086 0.3890 0.0428 0.0375 0.0157 599 LYS A CB 4778 C CG . LYS A 583 ? 0.4499 0.4421 0.4317 0.0436 0.0385 0.0129 599 LYS A CG 4779 C CD . LYS A 583 ? 0.4848 0.4749 0.4724 0.0415 0.0407 0.0103 599 LYS A CD 4780 C CE . LYS A 583 ? 0.5235 0.5111 0.5188 0.0424 0.0419 0.0078 599 LYS A CE 4781 N NZ . LYS A 583 ? 0.5518 0.5365 0.5535 0.0404 0.0445 0.0053 599 LYS A NZ 4782 N N . ASN A 584 ? 0.3771 0.3872 0.3496 0.0427 0.0310 0.0109 600 ASN A N 4783 C CA . ASN A 584 ? 0.3719 0.3881 0.3470 0.0425 0.0290 0.0071 600 ASN A CA 4784 C C . ASN A 584 ? 0.3546 0.3767 0.3254 0.0429 0.0265 0.0076 600 ASN A C 4785 O O . ASN A 584 ? 0.3402 0.3676 0.3118 0.0425 0.0250 0.0049 600 ASN A O 4786 C CB . ASN A 584 ? 0.3907 0.4079 0.3680 0.0403 0.0292 0.0047 600 ASN A CB 4787 C CG . ASN A 584 ? 0.4200 0.4331 0.4039 0.0400 0.0312 0.0025 600 ASN A CG 4788 O OD1 . ASN A 584 ? 0.4540 0.4679 0.4427 0.0411 0.0310 -0.0002 600 ASN A OD1 4789 N ND2 . ASN A 584 ? 0.4272 0.4360 0.4116 0.0385 0.0333 0.0035 600 ASN A ND2 4790 N N . ASN A 585 ? 0.3474 0.3687 0.3137 0.0439 0.0261 0.0108 601 ASN A N 4791 C CA . ASN A 585 ? 0.3453 0.3721 0.3082 0.0444 0.0240 0.0111 601 ASN A CA 4792 C C . ASN A 585 ? 0.3249 0.3563 0.2859 0.0422 0.0229 0.0100 601 ASN A C 4793 O O . ASN A 585 ? 0.3292 0.3661 0.2902 0.0422 0.0215 0.0082 601 ASN A O 4794 C CB . ASN A 585 ? 0.3457 0.3758 0.3119 0.0464 0.0229 0.0089 601 ASN A CB 4795 C CG . ASN A 585 ? 0.3639 0.3986 0.3271 0.0474 0.0211 0.0096 601 ASN A CG 4796 O OD1 . ASN A 585 ? 0.3717 0.4060 0.3307 0.0472 0.0206 0.0123 601 ASN A OD1 4797 N ND2 . ASN A 585 ? 0.3708 0.4101 0.3368 0.0484 0.0201 0.0069 601 ASN A ND2 4798 N N . VAL A 586 ? 0.3099 0.3389 0.2696 0.0404 0.0238 0.0110 602 VAL A N 4799 C CA . VAL A 586 ? 0.2924 0.3248 0.2508 0.0383 0.0228 0.0099 602 VAL A CA 4800 C C . VAL A 586 ? 0.2916 0.3274 0.2452 0.0379 0.0214 0.0117 602 VAL A C 4801 O O . VAL A 586 ? 0.2802 0.3139 0.2308 0.0381 0.0217 0.0144 602 VAL A O 4802 C CB . VAL A 586 ? 0.2875 0.3162 0.2468 0.0366 0.0241 0.0100 602 VAL A CB 4803 C CG1 . VAL A 586 ? 0.2742 0.3058 0.2312 0.0346 0.0228 0.0095 602 VAL A CG1 4804 C CG2 . VAL A 586 ? 0.2802 0.3065 0.2450 0.0367 0.0253 0.0072 602 VAL A CG2 4805 N N . HIS A 587 ? 0.2757 0.3167 0.2286 0.0372 0.0200 0.0103 603 HIS A N 4806 C CA . HIS A 587 ? 0.2796 0.3241 0.2287 0.0366 0.0188 0.0118 603 HIS A CA 4807 C C . HIS A 587 ? 0.2778 0.3208 0.2244 0.0346 0.0189 0.0132 603 HIS A C 4808 O O . HIS A 587 ? 0.2771 0.3193 0.2247 0.0332 0.0190 0.0120 603 HIS A O 4809 C CB . HIS A 587 ? 0.2754 0.3256 0.2244 0.0362 0.0177 0.0099 603 HIS A CB 4810 C CG . HIS A 587 ? 0.2798 0.3336 0.2258 0.0355 0.0168 0.0112 603 HIS A CG 4811 N ND1 . HIS A 587 ? 0.2745 0.3302 0.2202 0.0369 0.0164 0.0120 603 HIS A ND1 4812 C CD2 . HIS A 587 ? 0.2787 0.3346 0.2222 0.0336 0.0162 0.0117 603 HIS A CD2 4813 C CE1 . HIS A 587 ? 0.2764 0.3353 0.2198 0.0358 0.0157 0.0128 603 HIS A CE1 4814 N NE2 . HIS A 587 ? 0.2792 0.3381 0.2212 0.0337 0.0156 0.0128 603 HIS A NE2 4815 N N . ILE A 588 ? 0.2731 0.3156 0.2166 0.0346 0.0187 0.0156 604 ILE A N 4816 C CA . ILE A 588 ? 0.2640 0.3053 0.2051 0.0329 0.0187 0.0170 604 ILE A CA 4817 C C . ILE A 588 ? 0.2549 0.3008 0.1937 0.0319 0.0172 0.0174 604 ILE A C 4818 O O . ILE A 588 ? 0.2496 0.2983 0.1878 0.0330 0.0165 0.0176 604 ILE A O 4819 C CB . ILE A 588 ? 0.2715 0.3084 0.2107 0.0336 0.0197 0.0193 604 ILE A CB 4820 C CG1 . ILE A 588 ? 0.2753 0.3074 0.2169 0.0347 0.0216 0.0192 604 ILE A CG1 4821 C CG2 . ILE A 588 ? 0.2729 0.3085 0.2101 0.0318 0.0199 0.0203 604 ILE A CG2 4822 C CD1 . ILE A 588 ? 0.2825 0.3128 0.2276 0.0333 0.0226 0.0173 604 ILE A CD1 4823 N N . GLY A 589 ? 0.2474 0.2940 0.1855 0.0299 0.0167 0.0172 605 GLY A N 4824 C CA . GLY A 589 ? 0.2462 0.2965 0.1822 0.0287 0.0155 0.0177 605 GLY A CA 4825 C C . GLY A 589 ? 0.2482 0.3021 0.1848 0.0281 0.0149 0.0162 605 GLY A C 4826 O O . GLY A 589 ? 0.2502 0.3040 0.1886 0.0288 0.0153 0.0146 605 GLY A O 4827 N N . TRP A 590 ? 0.2463 0.3032 0.1812 0.0266 0.0142 0.0166 606 TRP A N 4828 C CA . TRP A 590 ? 0.2589 0.3188 0.1935 0.0258 0.0138 0.0154 606 TRP A CA 4829 C C . TRP A 590 ? 0.2631 0.3271 0.1964 0.0248 0.0135 0.0161 606 TRP A C 4830 O O . TRP A 590 ? 0.2708 0.3350 0.2034 0.0242 0.0132 0.0174 606 TRP A O 4831 C CB . TRP A 590 ? 0.2560 0.3138 0.1900 0.0244 0.0133 0.0151 606 TRP A CB 4832 C CG . TRP A 590 ? 0.2632 0.3191 0.1961 0.0230 0.0128 0.0165 606 TRP A CG 4833 C CD1 . TRP A 590 ? 0.2639 0.3215 0.1952 0.0214 0.0121 0.0175 606 TRP A CD1 4834 C CD2 . TRP A 590 ? 0.2717 0.3238 0.2054 0.0230 0.0132 0.0170 606 TRP A CD2 4835 N NE1 . TRP A 590 ? 0.2746 0.3297 0.2058 0.0205 0.0118 0.0185 606 TRP A NE1 4836 C CE2 . TRP A 590 ? 0.2716 0.3235 0.2041 0.0214 0.0125 0.0182 606 TRP A CE2 4837 C CE3 . TRP A 590 ? 0.2715 0.3203 0.2070 0.0241 0.0142 0.0166 606 TRP A CE3 4838 C CZ2 . TRP A 590 ? 0.2723 0.3212 0.2053 0.0209 0.0127 0.0187 606 TRP A CZ2 4839 C CZ3 . TRP A 590 ? 0.2757 0.3213 0.2115 0.0235 0.0146 0.0173 606 TRP A CZ3 4840 C CH2 . TRP A 590 ? 0.2779 0.3237 0.2123 0.0220 0.0139 0.0182 606 TRP A CH2 4841 N N . THR A 591 ? 0.2654 0.3326 0.1985 0.0246 0.0138 0.0150 607 THR A N 4842 C CA . THR A 591 ? 0.2666 0.3377 0.1988 0.0234 0.0139 0.0154 607 THR A CA 4843 C C . THR A 591 ? 0.2696 0.3396 0.1995 0.0212 0.0134 0.0166 607 THR A C 4844 O O . THR A 591 ? 0.2594 0.3262 0.1885 0.0209 0.0129 0.0165 607 THR A O 4845 C CB . THR A 591 ? 0.2741 0.3490 0.2066 0.0238 0.0147 0.0138 607 THR A CB 4846 O OG1 . THR A 591 ? 0.2686 0.3419 0.2004 0.0242 0.0146 0.0126 607 THR A OG1 4847 C CG2 . THR A 591 ? 0.2811 0.3579 0.2162 0.0258 0.0150 0.0128 607 THR A CG2 4848 N N . THR A 592 ? 0.2725 0.3450 0.2017 0.0197 0.0136 0.0174 608 THR A N 4849 C CA . THR A 592 ? 0.2802 0.3515 0.2074 0.0176 0.0132 0.0187 608 THR A CA 4850 C C . THR A 592 ? 0.2755 0.3468 0.2003 0.0172 0.0134 0.0182 608 THR A C 4851 O O . THR A 592 ? 0.2844 0.3586 0.2089 0.0175 0.0143 0.0172 608 THR A O 4852 C CB . THR A 592 ? 0.2931 0.3672 0.2208 0.0161 0.0135 0.0196 608 THR A CB 4853 O OG1 . THR A 592 ? 0.3083 0.3821 0.2378 0.0169 0.0130 0.0199 608 THR A OG1 4854 C CG2 . THR A 592 ? 0.2921 0.3646 0.2179 0.0139 0.0131 0.0211 608 THR A CG2 4855 N N . SER A 593 ? 0.2659 0.3340 0.1891 0.0165 0.0123 0.0188 609 SER A N 4856 C CA . SER A 593 ? 0.2651 0.3326 0.1854 0.0163 0.0120 0.0183 609 SER A CA 4857 C C . SER A 593 ? 0.2738 0.3437 0.1911 0.0148 0.0130 0.0192 609 SER A C 4858 O O . SER A 593 ? 0.2645 0.3355 0.1821 0.0133 0.0135 0.0206 609 SER A O 4859 C CB . SER A 593 ? 0.2643 0.3276 0.1835 0.0158 0.0103 0.0189 609 SER A CB 4860 O OG . SER A 593 ? 0.2563 0.3188 0.1726 0.0159 0.0095 0.0184 609 SER A OG 4861 N N . ASN A 594 ? 0.2823 0.3531 0.1970 0.0153 0.0133 0.0183 610 ASN A N 4862 C CA A ASN A 594 ? 0.2927 0.3654 0.2038 0.0139 0.0145 0.0192 610 ASN A CA 4863 C CA B ASN A 594 ? 0.2957 0.3682 0.2068 0.0139 0.0145 0.0192 610 ASN A CA 4864 C C . ASN A 594 ? 0.3044 0.3737 0.2108 0.0134 0.0132 0.0202 610 ASN A C 4865 O O . ASN A 594 ? 0.3035 0.3736 0.2058 0.0126 0.0141 0.0210 610 ASN A O 4866 C CB A ASN A 594 ? 0.2899 0.3663 0.2007 0.0149 0.0161 0.0172 610 ASN A CB 4867 C CB B ASN A 594 ? 0.2977 0.3744 0.2086 0.0147 0.0162 0.0175 610 ASN A CB 4868 C CG A ASN A 594 ? 0.2900 0.3655 0.1995 0.0167 0.0151 0.0152 610 ASN A CG 4869 C CG B ASN A 594 ? 0.2996 0.3793 0.2152 0.0155 0.0172 0.0163 610 ASN A CG 4870 O OD1 A ASN A 594 ? 0.2906 0.3627 0.2003 0.0175 0.0132 0.0149 610 ASN A OD1 4871 O OD1 B ASN A 594 ? 0.2935 0.3745 0.2112 0.0144 0.0177 0.0173 610 ASN A OD1 4872 N ND2 A ASN A 594 ? 0.2907 0.3695 0.1991 0.0174 0.0164 0.0135 610 ASN A ND2 4873 N ND2 B ASN A 594 ? 0.3013 0.3824 0.2187 0.0174 0.0173 0.0141 610 ASN A ND2 4874 N N . LYS A 595 ? 0.3105 0.3761 0.2176 0.0140 0.0110 0.0202 611 LYS A N 4875 C CA . LYS A 595 ? 0.3375 0.3999 0.2407 0.0141 0.0092 0.0206 611 LYS A CA 4876 C C . LYS A 595 ? 0.3507 0.4103 0.2517 0.0123 0.0084 0.0233 611 LYS A C 4877 O O . LYS A 595 ? 0.3616 0.4180 0.2595 0.0127 0.0065 0.0237 611 LYS A O 4878 C CB . LYS A 595 ? 0.3427 0.4029 0.2480 0.0159 0.0072 0.0185 611 LYS A CB 4879 C CG . LYS A 595 ? 0.3489 0.4112 0.2555 0.0178 0.0077 0.0157 611 LYS A CG 4880 C CD . LYS A 595 ? 0.3737 0.4371 0.2754 0.0184 0.0076 0.0149 611 LYS A CD 4881 C CE . LYS A 595 ? 0.3854 0.4507 0.2889 0.0205 0.0077 0.0116 611 LYS A CE 4882 N NZ . LYS A 595 ? 0.3858 0.4538 0.2938 0.0208 0.0096 0.0108 611 LYS A NZ 4883 N N . CYS A 596 ? 0.3554 0.4160 0.2582 0.0106 0.0096 0.0249 612 CYS A N 4884 C CA . CYS A 596 ? 0.3732 0.4312 0.2741 0.0088 0.0091 0.0274 612 CYS A CA 4885 C C . CYS A 596 ? 0.3927 0.4535 0.2931 0.0069 0.0117 0.0289 612 CYS A C 4886 O O . CYS A 596 ? 0.3879 0.4513 0.2923 0.0063 0.0129 0.0285 612 CYS A O 4887 C CB . CYS A 596 ? 0.3541 0.4098 0.2587 0.0083 0.0076 0.0278 612 CYS A CB 4888 S SG . CYS A 596 ? 0.3437 0.3948 0.2460 0.0068 0.0060 0.0304 612 CYS A SG 4889 N N . VAL A 597 ? 0.4262 0.4864 0.3215 0.0060 0.0126 0.0304 613 VAL A N 4890 C CA . VAL A 597 ? 0.4734 0.5362 0.3678 0.0040 0.0155 0.0317 613 VAL A CA 4891 C C . VAL A 597 ? 0.5100 0.5707 0.4053 0.0017 0.0157 0.0342 613 VAL A C 4892 O O . VAL A 597 ? 0.5020 0.5583 0.3944 0.0013 0.0140 0.0360 613 VAL A O 4893 C CB . VAL A 597 ? 0.4715 0.5344 0.3593 0.0041 0.0168 0.0323 613 VAL A CB 4894 C CG1 . VAL A 597 ? 0.4871 0.5512 0.3731 0.0015 0.0199 0.0343 613 VAL A CG1 4895 C CG2 . VAL A 597 ? 0.4767 0.5432 0.3649 0.0059 0.0175 0.0294 613 VAL A CG2 4896 N N . SER A 598 ? 0.5659 0.6297 0.4655 0.0003 0.0176 0.0341 614 SER A N 4897 C CA . SER A 598 ? 0.6152 0.6779 0.5164 -0.0020 0.0183 0.0361 614 SER A CA 4898 C C . SER A 598 ? 0.6320 0.6929 0.5279 -0.0038 0.0201 0.0386 614 SER A C 4899 O O . SER A 598 ? 0.6941 0.7522 0.5899 -0.0057 0.0202 0.0408 614 SER A O 4900 C CB . SER A 598 ? 0.6321 0.6995 0.5392 -0.0030 0.0201 0.0348 614 SER A CB 4901 O OG . SER A 598 ? 0.6290 0.6968 0.5406 -0.0017 0.0182 0.0333 614 SER A OG 4902 ZN ZN . ZN B . ? 0.2946 0.3157 0.3044 0.0088 -0.0020 -0.0236 1616 ZN A ZN 4903 C C1 . NAG C . ? 0.3122 0.3508 0.3365 -0.0128 -0.0227 -0.0109 1617 NAG A C1 4904 C C2 . NAG C . ? 0.3224 0.3595 0.3521 -0.0125 -0.0243 -0.0144 1617 NAG A C2 4905 C C3 . NAG C . ? 0.3305 0.3656 0.3674 -0.0137 -0.0265 -0.0154 1617 NAG A C3 4906 C C4 . NAG C . ? 0.3365 0.3752 0.3757 -0.0148 -0.0260 -0.0165 1617 NAG A C4 4907 C C5 . NAG C . ? 0.3263 0.3665 0.3598 -0.0150 -0.0242 -0.0130 1617 NAG A C5 4908 C C6 . NAG C . ? 0.3212 0.3657 0.3574 -0.0159 -0.0237 -0.0147 1617 NAG A C6 4909 C C7 . NAG C . ? 0.3430 0.3773 0.3698 -0.0106 -0.0240 -0.0151 1617 NAG A C7 4910 C C8 . NAG C . ? 0.3432 0.3735 0.3690 -0.0097 -0.0251 -0.0138 1617 NAG A C8 4911 N N2 . NAG C . ? 0.3285 0.3618 0.3565 -0.0116 -0.0250 -0.0131 1617 NAG A N2 4912 O O3 . NAG C . ? 0.3292 0.3640 0.3715 -0.0134 -0.0278 -0.0194 1617 NAG A O3 4913 O O4 . NAG C . ? 0.3729 0.4089 0.4186 -0.0161 -0.0280 -0.0166 1617 NAG A O4 4914 O O5 . NAG C . ? 0.3147 0.3567 0.3414 -0.0137 -0.0224 -0.0122 1617 NAG A O5 4915 O O6 . NAG C . ? 0.3181 0.3633 0.3498 -0.0162 -0.0223 -0.0112 1617 NAG A O6 4916 O O7 . NAG C . ? 0.3464 0.3844 0.3726 -0.0102 -0.0222 -0.0181 1617 NAG A O7 4917 C C1 . NAG D . ? 0.4037 0.4427 0.4561 -0.0165 -0.0287 -0.0214 1618 NAG A C1 4918 C C2 . NAG D . ? 0.4344 0.4704 0.4934 -0.0181 -0.0304 -0.0208 1618 NAG A C2 4919 C C3 . NAG D . ? 0.4414 0.4806 0.5082 -0.0185 -0.0314 -0.0261 1618 NAG A C3 4920 C C4 . NAG D . ? 0.4614 0.5010 0.5307 -0.0174 -0.0322 -0.0302 1618 NAG A C4 4921 C C5 . NAG D . ? 0.4444 0.4860 0.5062 -0.0159 -0.0302 -0.0301 1618 NAG A C5 4922 C C6 . NAG D . ? 0.4568 0.4977 0.5214 -0.0149 -0.0310 -0.0334 1618 NAG A C6 4923 C C7 . NAG D . ? 0.4722 0.5121 0.5286 -0.0199 -0.0280 -0.0173 1618 NAG A C7 4924 C C8 . NAG D . ? 0.4585 0.4968 0.5124 -0.0211 -0.0268 -0.0128 1618 NAG A C8 4925 N N2 . NAG D . ? 0.4378 0.4734 0.4943 -0.0192 -0.0294 -0.0167 1618 NAG A N2 4926 O O3 . NAG D . ? 0.4428 0.4787 0.5163 -0.0200 -0.0330 -0.0254 1618 NAG A O3 4927 O O4 . NAG D . ? 0.5133 0.5571 0.5883 -0.0175 -0.0325 -0.0356 1618 NAG A O4 4928 O O5 . NAG D . ? 0.4163 0.4552 0.4714 -0.0156 -0.0294 -0.0250 1618 NAG A O5 4929 O O6 . NAG D . ? 0.4888 0.5340 0.5488 -0.0139 -0.0286 -0.0356 1618 NAG A O6 4930 O O7 . NAG D . ? 0.4963 0.5414 0.5547 -0.0195 -0.0276 -0.0215 1618 NAG A O7 4931 C C1 . BMA E . ? 0.5793 0.6204 0.6632 -0.0183 -0.0349 -0.0378 1619 BMA A C1 4932 C C2 . BMA E . ? 0.5996 0.6449 0.6885 -0.0178 -0.0352 -0.0443 1619 BMA A C2 4933 C C3 . BMA E . ? 0.6309 0.6739 0.7302 -0.0186 -0.0378 -0.0472 1619 BMA A C3 4934 C C4 . BMA E . ? 0.6588 0.7003 0.7620 -0.0203 -0.0386 -0.0451 1619 BMA A C4 4935 C C5 . BMA E . ? 0.6827 0.7198 0.7799 -0.0208 -0.0379 -0.0382 1619 BMA A C5 4936 C C6 . BMA E . ? 0.7391 0.7745 0.8402 -0.0227 -0.0381 -0.0360 1619 BMA A C6 4937 O O2 . BMA E . ? 0.5881 0.6396 0.6751 -0.0177 -0.0336 -0.0468 1619 BMA A O2 4938 O O3 . BMA E . ? 0.6372 0.6850 0.7412 -0.0182 -0.0379 -0.0536 1619 BMA A O3 4939 O O4 . BMA E . ? 0.6726 0.7109 0.7853 -0.0211 -0.0411 -0.0472 1619 BMA A O4 4940 O O5 . BMA E . ? 0.6277 0.6682 0.7159 -0.0199 -0.0355 -0.0365 1619 BMA A O5 4941 O O6 . BMA E . ? 0.8142 0.8488 0.9080 -0.0231 -0.0363 -0.0307 1619 BMA A O6 4942 C C1 . MAN F . ? 0.8886 0.9177 0.9850 -0.0248 -0.0368 -0.0265 1620 MAN A C1 4943 C C2 . MAN F . ? 0.9444 0.9670 1.0347 -0.0242 -0.0373 -0.0210 1620 MAN A C2 4944 C C3 . MAN F . ? 0.9581 0.9816 1.0390 -0.0240 -0.0349 -0.0167 1620 MAN A C3 4945 C C4 . MAN F . ? 0.9557 0.9822 1.0374 -0.0257 -0.0329 -0.0157 1620 MAN A C4 4946 C C5 . MAN F . ? 0.9449 0.9779 1.0325 -0.0259 -0.0329 -0.0216 1620 MAN A C5 4947 C C6 . MAN F . ? 0.9613 0.9973 1.0511 -0.0276 -0.0312 -0.0211 1620 MAN A C6 4948 O O2 . MAN F . ? 0.9939 1.0100 1.0886 -0.0254 -0.0388 -0.0182 1620 MAN A O2 4949 O O3 . MAN F . ? 0.9475 0.9648 1.0235 -0.0237 -0.0354 -0.0115 1620 MAN A O3 4950 O O4 . MAN F . ? 0.9619 0.9902 1.0351 -0.0252 -0.0308 -0.0126 1620 MAN A O4 4951 O O5 . MAN F . ? 0.9075 0.9391 1.0039 -0.0262 -0.0351 -0.0252 1620 MAN A O5 4952 O O6 . MAN F . ? 0.9762 1.0182 1.0717 -0.0275 -0.0316 -0.0269 1620 MAN A O6 4953 C C1 . MAN G . ? 0.6459 0.6924 0.7526 -0.0173 -0.0387 -0.0565 1623 MAN A C1 4954 C C2 . MAN G . ? 0.6437 0.6932 0.7595 -0.0175 -0.0400 -0.0632 1623 MAN A C2 4955 C C3 . MAN G . ? 0.6449 0.7017 0.7578 -0.0170 -0.0379 -0.0673 1623 MAN A C3 4956 C C4 . MAN G . ? 0.6420 0.7007 0.7456 -0.0158 -0.0352 -0.0666 1623 MAN A C4 4957 C C5 . MAN G . ? 0.6381 0.6931 0.7341 -0.0157 -0.0343 -0.0598 1623 MAN A C5 4958 C C6 . MAN G . ? 0.6530 0.7091 0.7408 -0.0145 -0.0318 -0.0589 1623 MAN A C6 4959 O O2 . MAN G . ? 0.6440 0.6915 0.7640 -0.0168 -0.0411 -0.0658 1623 MAN A O2 4960 O O3 . MAN G . ? 0.6581 0.7179 0.7787 -0.0170 -0.0389 -0.0739 1623 MAN A O3 4961 O O4 . MAN G . ? 0.6230 0.6879 0.7227 -0.0152 -0.0333 -0.0694 1623 MAN A O4 4962 O O5 . MAN G . ? 0.6303 0.6791 0.7299 -0.0161 -0.0365 -0.0568 1623 MAN A O5 4963 O O6 . MAN G . ? 0.6721 0.7310 0.7624 -0.0139 -0.0310 -0.0643 1623 MAN A O6 4964 C C1 . BMA H . ? 0.7261 0.7863 0.8087 -0.0129 -0.0281 -0.0637 1624 BMA A C1 4965 C C2 . BMA H . ? 0.7427 0.8085 0.8192 -0.0123 -0.0257 -0.0654 1624 BMA A C2 4966 C C3 . BMA H . ? 0.7459 0.8156 0.8247 -0.0119 -0.0245 -0.0717 1624 BMA A C3 4967 C C4 . BMA H . ? 0.7436 0.8120 0.8333 -0.0125 -0.0270 -0.0757 1624 BMA A C4 4968 C C5 . BMA H . ? 0.7598 0.8231 0.8518 -0.0126 -0.0278 -0.0736 1624 BMA A C5 4969 C C6 . BMA H . ? 0.7676 0.8281 0.8704 -0.0131 -0.0312 -0.0759 1624 BMA A C6 4970 O O2 . BMA H . ? 0.8342 0.9019 0.9113 -0.0128 -0.0268 -0.0647 1624 BMA A O2 4971 O O3 . BMA H . ? 0.7150 0.7898 0.7902 -0.0113 -0.0235 -0.0739 1624 BMA A O3 4972 O O4 . BMA H . ? 0.7549 0.8275 0.8474 -0.0122 -0.0260 -0.0820 1624 BMA A O4 4973 O O5 . BMA H . ? 0.7368 0.7965 0.8228 -0.0125 -0.0277 -0.0671 1624 BMA A O5 4974 O O6 . BMA H . ? 0.7930 0.8522 0.8993 -0.0127 -0.0310 -0.0785 1624 BMA A O6 4975 C C1 . NAG I . ? 0.4612 0.4778 0.5889 -0.0282 0.1005 -0.0875 1621 NAG A C1 4976 C C2 . NAG I . ? 0.4793 0.4925 0.6019 -0.0309 0.1103 -0.0851 1621 NAG A C2 4977 C C3 . NAG I . ? 0.4980 0.5134 0.6243 -0.0329 0.1142 -0.0893 1621 NAG A C3 4978 C C4 . NAG I . ? 0.4932 0.5115 0.6133 -0.0311 0.1081 -0.0881 1621 NAG A C4 4979 C C5 . NAG I . ? 0.4847 0.5059 0.6108 -0.0286 0.0986 -0.0904 1621 NAG A C5 4980 C C6 . NAG I . ? 0.4863 0.5098 0.6064 -0.0269 0.0926 -0.0890 1621 NAG A C6 4981 C C7 . NAG I . ? 0.4854 0.4912 0.6066 -0.0330 0.1205 -0.0811 1621 NAG A C7 4982 C C8 . NAG I . ? 0.4906 0.4939 0.6206 -0.0346 0.1257 -0.0832 1621 NAG A C8 4983 N N2 . NAG I . ? 0.4830 0.4936 0.6126 -0.0324 0.1154 -0.0865 1621 NAG A N2 4984 O O3 . NAG I . ? 0.5176 0.5297 0.6375 -0.0352 0.1232 -0.0865 1621 NAG A O3 4985 O O4 . NAG I . ? 0.5070 0.5278 0.6312 -0.0329 0.1114 -0.0924 1621 NAG A O4 4986 O O5 . NAG I . ? 0.4629 0.4818 0.5847 -0.0269 0.0957 -0.0863 1621 NAG A O5 4987 O O6 . NAG I . ? 0.5129 0.5365 0.6273 -0.0285 0.0978 -0.0882 1621 NAG A O6 4988 O O7 . NAG I . ? 0.4914 0.4949 0.5988 -0.0321 0.1209 -0.0747 1621 NAG A O7 4989 C C1 . NAG J . ? 0.4985 0.4768 0.4931 0.0578 -0.1174 -0.0401 1622 NAG A C1 4990 C C2 . NAG J . ? 0.5015 0.4817 0.5069 0.0608 -0.1224 -0.0482 1622 NAG A C2 4991 C C3 . NAG J . ? 0.5180 0.4934 0.5207 0.0654 -0.1310 -0.0488 1622 NAG A C3 4992 C C4 . NAG J . ? 0.5245 0.4937 0.5202 0.0651 -0.1326 -0.0424 1622 NAG A C4 4993 C C5 . NAG J . ? 0.5222 0.4904 0.5067 0.0620 -0.1269 -0.0347 1622 NAG A C5 4994 C C6 . NAG J . ? 0.5267 0.4885 0.5041 0.0616 -0.1283 -0.0282 1622 NAG A C6 4995 C C7 . NAG J . ? 0.4837 0.4731 0.5023 0.0607 -0.1190 -0.0585 1622 NAG A C7 4996 C C8 . NAG J . ? 0.4814 0.4745 0.5001 0.0618 -0.1183 -0.0619 1622 NAG A C8 4997 N N2 . NAG J . ? 0.4946 0.4789 0.5010 0.0618 -0.1214 -0.0520 1622 NAG A N2 4998 O O3 . NAG J . ? 0.5194 0.4967 0.5356 0.0670 -0.1345 -0.0563 1622 NAG A O3 4999 O O4 . NAG J . ? 0.5467 0.5109 0.5361 0.0696 -0.1404 -0.0415 1622 NAG A O4 5000 O O5 . NAG J . ? 0.5053 0.4784 0.4965 0.0578 -0.1197 -0.0359 1622 NAG A O5 5001 O O6 . NAG J . ? 0.5017 0.4645 0.4789 0.0571 -0.1216 -0.0242 1622 NAG A O6 5002 O O7 . NAG J . ? 0.4761 0.4669 0.5054 0.0590 -0.1173 -0.0617 1622 NAG A O7 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 17 ? ? ? A . n A 1 2 LEU 2 18 ? ? ? A . n A 1 3 VAL 3 19 19 VAL VAL A . n A 1 4 LYS 4 20 20 LYS LYS A . n A 1 5 GLU 5 21 21 GLU GLU A . n A 1 6 GLU 6 22 22 GLU GLU A . n A 1 7 ILE 7 23 23 ILE ILE A . n A 1 8 GLN 8 24 24 GLN GLN A . n A 1 9 ALA 9 25 25 ALA ALA A . n A 1 10 LYS 10 26 26 LYS LYS A . n A 1 11 GLU 11 27 27 GLU GLU A . n A 1 12 TYR 12 28 28 TYR TYR A . n A 1 13 LEU 13 29 29 LEU LEU A . n A 1 14 GLU 14 30 30 GLU GLU A . n A 1 15 ASN 15 31 31 ASN ASN A . n A 1 16 LEU 16 32 32 LEU LEU A . n A 1 17 ASN 17 33 33 ASN ASN A . n A 1 18 LYS 18 34 34 LYS LYS A . n A 1 19 GLU 19 35 35 GLU GLU A . n A 1 20 LEU 20 36 36 LEU LEU A . n A 1 21 ALA 21 37 37 ALA ALA A . n A 1 22 LYS 22 38 38 LYS LYS A . n A 1 23 ARG 23 39 39 ARG ARG A . n A 1 24 THR 24 40 40 THR THR A . n A 1 25 ASN 25 41 41 ASN ASN A . n A 1 26 VAL 26 42 42 VAL VAL A . n A 1 27 GLU 27 43 43 GLU GLU A . n A 1 28 THR 28 44 44 THR THR A . n A 1 29 GLU 29 45 45 GLU GLU A . n A 1 30 ALA 30 46 46 ALA ALA A . n A 1 31 ALA 31 47 47 ALA ALA A . n A 1 32 TRP 32 48 48 TRP TRP A . n A 1 33 ALA 33 49 49 ALA ALA A . n A 1 34 TYR 34 50 50 TYR TYR A . n A 1 35 GLY 35 51 51 GLY GLY A . n A 1 36 SER 36 52 52 SER SER A . n A 1 37 ASN 37 53 53 ASN ASN A . n A 1 38 ILE 38 54 54 ILE ILE A . n A 1 39 THR 39 55 55 THR THR A . n A 1 40 ASP 40 56 56 ASP ASP A . n A 1 41 GLU 41 57 57 GLU GLU A . n A 1 42 ASN 42 58 58 ASN ASN A . n A 1 43 GLU 43 59 59 GLU GLU A . n A 1 44 LYS 44 60 60 LYS LYS A . n A 1 45 LYS 45 61 61 LYS LYS A . n A 1 46 LYS 46 62 62 LYS LYS A . n A 1 47 ASN 47 63 63 ASN ASN A . n A 1 48 GLU 48 64 64 GLU GLU A . n A 1 49 ILE 49 65 65 ILE ILE A . n A 1 50 SER 50 66 66 SER SER A . n A 1 51 ALA 51 67 67 ALA ALA A . n A 1 52 GLU 52 68 68 GLU GLU A . n A 1 53 LEU 53 69 69 LEU LEU A . n A 1 54 ALA 54 70 70 ALA ALA A . n A 1 55 LYS 55 71 71 LYS LYS A . n A 1 56 PHE 56 72 72 PHE PHE A . n A 1 57 MET 57 73 73 MET MET A . n A 1 58 LYS 58 74 74 LYS LYS A . n A 1 59 GLU 59 75 75 GLU GLU A . n A 1 60 VAL 60 76 76 VAL VAL A . n A 1 61 ALA 61 77 77 ALA ALA A . n A 1 62 SER 62 78 78 SER SER A . n A 1 63 ASP 63 79 79 ASP ASP A . n A 1 64 THR 64 80 80 THR THR A . n A 1 65 THR 65 81 81 THR THR A . n A 1 66 LYS 66 82 82 LYS LYS A . n A 1 67 PHE 67 83 83 PHE PHE A . n A 1 68 GLN 68 84 84 GLN GLN A . n A 1 69 TRP 69 85 85 TRP TRP A . n A 1 70 ARG 70 86 86 ARG ARG A . n A 1 71 SER 71 87 87 SER SER A . n A 1 72 TYR 72 88 88 TYR TYR A . n A 1 73 GLN 73 89 89 GLN GLN A . n A 1 74 SER 74 90 90 SER SER A . n A 1 75 GLU 75 91 91 GLU GLU A . n A 1 76 ASP 76 92 92 ASP ASP A . n A 1 77 LEU 77 93 93 LEU LEU A . n A 1 78 LYS 78 94 94 LYS LYS A . n A 1 79 ARG 79 95 95 ARG ARG A . n A 1 80 GLN 80 96 96 GLN GLN A . n A 1 81 PHE 81 97 97 PHE PHE A . n A 1 82 LYS 82 98 98 LYS LYS A . n A 1 83 ALA 83 99 99 ALA ALA A . n A 1 84 LEU 84 100 100 LEU LEU A . n A 1 85 THR 85 101 101 THR THR A . n A 1 86 LYS 86 102 102 LYS LYS A . n A 1 87 LEU 87 103 103 LEU LEU A . n A 1 88 GLY 88 104 104 GLY GLY A . n A 1 89 TYR 89 105 105 TYR TYR A . n A 1 90 ALA 90 106 106 ALA ALA A . n A 1 91 ALA 91 107 107 ALA ALA A . n A 1 92 LEU 92 108 108 LEU LEU A . n A 1 93 PRO 93 109 109 PRO PRO A . n A 1 94 GLU 94 110 110 GLU GLU A . n A 1 95 ASP 95 111 111 ASP ASP A . n A 1 96 ASP 96 112 112 ASP ASP A . n A 1 97 TYR 97 113 113 TYR TYR A . n A 1 98 ALA 98 114 114 ALA ALA A . n A 1 99 GLU 99 115 115 GLU GLU A . n A 1 100 LEU 100 116 116 LEU LEU A . n A 1 101 LEU 101 117 117 LEU LEU A . n A 1 102 ASP 102 118 118 ASP ASP A . n A 1 103 THR 103 119 119 THR THR A . n A 1 104 LEU 104 120 120 LEU LEU A . n A 1 105 SER 105 121 121 SER SER A . n A 1 106 ALA 106 122 122 ALA ALA A . n A 1 107 MET 107 123 123 MET MET A . n A 1 108 GLU 108 124 124 GLU GLU A . n A 1 109 SER 109 125 125 SER SER A . n A 1 110 ASN 110 126 126 ASN ASN A . n A 1 111 PHE 111 127 127 PHE PHE A . n A 1 112 ALA 112 128 128 ALA ALA A . n A 1 113 LYS 113 129 129 LYS LYS A . n A 1 114 VAL 114 130 130 VAL VAL A . n A 1 115 LYS 115 131 131 LYS LYS A . n A 1 116 VAL 116 132 132 VAL VAL A . n A 1 117 CYS 117 133 133 CYS CYS A . n A 1 118 ASP 118 134 134 ASP ASP A . n A 1 119 TYR 119 135 135 TYR TYR A . n A 1 120 LYS 120 136 136 LYS LYS A . n A 1 121 ASP 121 137 137 ASP ASP A . n A 1 122 SER 122 138 138 SER SER A . n A 1 123 THR 123 139 139 THR THR A . n A 1 124 LYS 124 140 140 LYS LYS A . n A 1 125 CYS 125 141 141 CYS CYS A . n A 1 126 ASP 126 142 142 ASP ASP A . n A 1 127 LEU 127 143 143 LEU LEU A . n A 1 128 ALA 128 144 144 ALA ALA A . n A 1 129 LEU 129 145 145 LEU LEU A . n A 1 130 ASP 130 146 146 ASP ASP A . n A 1 131 PRO 131 147 147 PRO PRO A . n A 1 132 GLU 132 148 148 GLU GLU A . n A 1 133 ILE 133 149 149 ILE ILE A . n A 1 134 GLU 134 150 150 GLU GLU A . n A 1 135 GLU 135 151 151 GLU GLU A . n A 1 136 VAL 136 152 152 VAL VAL A . n A 1 137 ILE 137 153 153 ILE ILE A . n A 1 138 SER 138 154 154 SER SER A . n A 1 139 LYS 139 155 155 LYS LYS A . n A 1 140 SER 140 156 156 SER SER A . n A 1 141 ARG 141 157 157 ARG ARG A . n A 1 142 ASP 142 158 158 ASP ASP A . n A 1 143 HIS 143 159 159 HIS HIS A . n A 1 144 GLU 144 160 160 GLU GLU A . n A 1 145 GLU 145 161 161 GLU GLU A . n A 1 146 LEU 146 162 162 LEU LEU A . n A 1 147 ALA 147 163 163 ALA ALA A . n A 1 148 TYR 148 164 164 TYR TYR A . n A 1 149 TYR 149 165 165 TYR TYR A . n A 1 150 TRP 150 166 166 TRP TRP A . n A 1 151 ARG 151 167 167 ARG ARG A . n A 1 152 GLU 152 168 168 GLU GLU A . n A 1 153 PHE 153 169 169 PHE PHE A . n A 1 154 TYR 154 170 170 TYR TYR A . n A 1 155 ASP 155 171 171 ASP ASP A . n A 1 156 LYS 156 172 172 LYS LYS A . n A 1 157 ALA 157 173 173 ALA ALA A . n A 1 158 GLY 158 174 174 GLY GLY A . n A 1 159 THR 159 175 175 THR THR A . n A 1 160 ALA 160 176 176 ALA ALA A . n A 1 161 VAL 161 177 177 VAL VAL A . n A 1 162 ARG 162 178 178 ARG ARG A . n A 1 163 SER 163 179 179 SER SER A . n A 1 164 GLN 164 180 180 GLN GLN A . n A 1 165 PHE 165 181 181 PHE PHE A . n A 1 166 GLU 166 182 182 GLU GLU A . n A 1 167 ARG 167 183 183 ARG ARG A . n A 1 168 TYR 168 184 184 TYR TYR A . n A 1 169 VAL 169 185 185 VAL VAL A . n A 1 170 GLU 170 186 186 GLU GLU A . n A 1 171 LEU 171 187 187 LEU LEU A . n A 1 172 ASN 172 188 188 ASN ASN A . n A 1 173 THR 173 189 189 THR THR A . n A 1 174 LYS 174 190 190 LYS LYS A . n A 1 175 ALA 175 191 191 ALA ALA A . n A 1 176 ALA 176 192 192 ALA ALA A . n A 1 177 LYS 177 193 193 LYS LYS A . n A 1 178 LEU 178 194 194 LEU LEU A . n A 1 179 ASN 179 195 195 ASN ASN A . n A 1 180 ASN 180 196 196 ASN ASN A . n A 1 181 PHE 181 197 197 PHE PHE A . n A 1 182 THR 182 198 198 THR THR A . n A 1 183 SER 183 199 199 SER SER A . n A 1 184 GLY 184 200 200 GLY GLY A . n A 1 185 ALA 185 201 201 ALA ALA A . n A 1 186 GLU 186 202 202 GLU GLU A . n A 1 187 ALA 187 203 203 ALA ALA A . n A 1 188 TRP 188 204 204 TRP TRP A . n A 1 189 LEU 189 205 205 LEU LEU A . n A 1 190 ASP 190 206 206 ASP ASP A . n A 1 191 GLU 191 207 207 GLU GLU A . n A 1 192 TYR 192 208 208 TYR TYR A . n A 1 193 GLU 193 209 209 GLU GLU A . n A 1 194 ASP 194 210 210 ASP ASP A . n A 1 195 ASP 195 211 211 ASP ASP A . n A 1 196 THR 196 212 212 THR THR A . n A 1 197 PHE 197 213 213 PHE PHE A . n A 1 198 GLU 198 214 214 GLU GLU A . n A 1 199 GLN 199 215 215 GLN GLN A . n A 1 200 GLN 200 216 216 GLN GLN A . n A 1 201 LEU 201 217 217 LEU LEU A . n A 1 202 GLU 202 218 218 GLU GLU A . n A 1 203 ASP 203 219 219 ASP ASP A . n A 1 204 ILE 204 220 220 ILE ILE A . n A 1 205 PHE 205 221 221 PHE PHE A . n A 1 206 ALA 206 222 222 ALA ALA A . n A 1 207 ASP 207 223 223 ASP ASP A . n A 1 208 ILE 208 224 224 ILE ILE A . n A 1 209 ARG 209 225 225 ARG ARG A . n A 1 210 PRO 210 226 226 PRO PRO A . n A 1 211 LEU 211 227 227 LEU LEU A . n A 1 212 TYR 212 228 228 TYR TYR A . n A 1 213 GLN 213 229 229 GLN GLN A . n A 1 214 GLN 214 230 230 GLN GLN A . n A 1 215 ILE 215 231 231 ILE ILE A . n A 1 216 HIS 216 232 232 HIS HIS A . n A 1 217 GLY 217 233 233 GLY GLY A . n A 1 218 TYR 218 234 234 TYR TYR A . n A 1 219 VAL 219 235 235 VAL VAL A . n A 1 220 ARG 220 236 236 ARG ARG A . n A 1 221 PHE 221 237 237 PHE PHE A . n A 1 222 ARG 222 238 238 ARG ARG A . n A 1 223 LEU 223 239 239 LEU LEU A . n A 1 224 ARG 224 240 240 ARG ARG A . n A 1 225 LYS 225 241 241 LYS LYS A . n A 1 226 HIS 226 242 242 HIS HIS A . n A 1 227 TYR 227 243 243 TYR TYR A . n A 1 228 GLY 228 244 244 GLY GLY A . n A 1 229 ASP 229 245 245 ASP ASP A . n A 1 230 ALA 230 246 246 ALA ALA A . n A 1 231 VAL 231 247 247 VAL VAL A . n A 1 232 VAL 232 248 248 VAL VAL A . n A 1 233 SER 233 249 249 SER SER A . n A 1 234 GLU 234 250 250 GLU GLU A . n A 1 235 THR 235 251 251 THR THR A . n A 1 236 GLY 236 252 252 GLY GLY A . n A 1 237 PRO 237 253 253 PRO PRO A . n A 1 238 ILE 238 254 254 ILE ILE A . n A 1 239 PRO 239 255 255 PRO PRO A . n A 1 240 MET 240 256 256 MET MET A . n A 1 241 HIS 241 257 257 HIS HIS A . n A 1 242 LEU 242 258 258 LEU LEU A . n A 1 243 LEU 243 259 259 LEU LEU A . n A 1 244 GLY 244 260 260 GLY GLY A . n A 1 245 ASN 245 261 261 ASN ASN A . n A 1 246 MET 246 262 262 MET MET A . n A 1 247 TRP 247 263 263 TRP TRP A . n A 1 248 ALA 248 264 264 ALA ALA A . n A 1 249 GLN 249 265 265 GLN GLN A . n A 1 250 GLN 250 266 266 GLN GLN A . n A 1 251 TRP 251 267 267 TRP TRP A . n A 1 252 SER 252 268 268 SER SER A . n A 1 253 GLU 253 269 269 GLU GLU A . n A 1 254 ILE 254 270 270 ILE ILE A . n A 1 255 ALA 255 271 271 ALA ALA A . n A 1 256 ASP 256 272 272 ASP ASP A . n A 1 257 ILE 257 273 273 ILE ILE A . n A 1 258 VAL 258 274 274 VAL VAL A . n A 1 259 SER 259 275 275 SER SER A . n A 1 260 PRO 260 276 276 PRO PRO A . n A 1 261 PHE 261 277 277 PHE PHE A . n A 1 262 PRO 262 278 278 PRO PRO A . n A 1 263 GLU 263 279 279 GLU GLU A . n A 1 264 LYS 264 280 280 LYS LYS A . n A 1 265 PRO 265 281 281 PRO PRO A . n A 1 266 LEU 266 282 282 LEU LEU A . n A 1 267 VAL 267 283 283 VAL VAL A . n A 1 268 ASP 268 284 284 ASP ASP A . n A 1 269 VAL 269 285 285 VAL VAL A . n A 1 270 SER 270 286 286 SER SER A . n A 1 271 ALA 271 287 287 ALA ALA A . n A 1 272 GLU 272 288 288 GLU GLU A . n A 1 273 MET 273 289 289 MET MET A . n A 1 274 GLU 274 290 290 GLU GLU A . n A 1 275 LYS 275 291 291 LYS LYS A . n A 1 276 GLN 276 292 292 GLN GLN A . n A 1 277 GLY 277 293 293 GLY GLY A . n A 1 278 TYR 278 294 294 TYR TYR A . n A 1 279 THR 279 295 295 THR THR A . n A 1 280 PRO 280 296 296 PRO PRO A . n A 1 281 LEU 281 297 297 LEU LEU A . n A 1 282 LYS 282 298 298 LYS LYS A . n A 1 283 MET 283 299 299 MET MET A . n A 1 284 PHE 284 300 300 PHE PHE A . n A 1 285 GLN 285 301 301 GLN GLN A . n A 1 286 MET 286 302 302 MET MET A . n A 1 287 GLY 287 303 303 GLY GLY A . n A 1 288 ASP 288 304 304 ASP ASP A . n A 1 289 ASP 289 305 305 ASP ASP A . n A 1 290 PHE 290 306 306 PHE PHE A . n A 1 291 PHE 291 307 307 PHE PHE A . n A 1 292 THR 292 308 308 THR THR A . n A 1 293 SER 293 309 309 SER SER A . n A 1 294 MET 294 310 310 MET MET A . n A 1 295 ASN 295 311 311 ASN ASN A . n A 1 296 LEU 296 312 312 LEU LEU A . n A 1 297 THR 297 313 313 THR THR A . n A 1 298 LYS 298 314 314 LYS LYS A . n A 1 299 LEU 299 315 315 LEU LEU A . n A 1 300 PRO 300 316 316 PRO PRO A . n A 1 301 GLN 301 317 317 GLN GLN A . n A 1 302 ASP 302 318 318 ASP ASP A . n A 1 303 PHE 303 319 319 PHE PHE A . n A 1 304 TRP 304 320 320 TRP TRP A . n A 1 305 ASP 305 321 321 ASP ASP A . n A 1 306 LYS 306 322 322 LYS LYS A . n A 1 307 SER 307 323 323 SER SER A . n A 1 308 ILE 308 324 324 ILE ILE A . n A 1 309 ILE 309 325 325 ILE ILE A . n A 1 310 GLU 310 326 326 GLU GLU A . n A 1 311 LYS 311 327 327 LYS LYS A . n A 1 312 PRO 312 328 328 PRO PRO A . n A 1 313 THR 313 329 329 THR THR A . n A 1 314 ASP 314 330 330 ASP ASP A . n A 1 315 GLY 315 331 331 GLY GLY A . n A 1 316 ARG 316 332 332 ARG ARG A . n A 1 317 ASP 317 333 333 ASP ASP A . n A 1 318 LEU 318 334 334 LEU LEU A . n A 1 319 VAL 319 335 335 VAL VAL A . n A 1 320 CYS 320 336 336 CYS CYS A . n A 1 321 HIS 321 337 337 HIS HIS A . n A 1 322 ALA 322 338 338 ALA ALA A . n A 1 323 SER 323 339 339 SER SER A . n A 1 324 ALA 324 340 340 ALA ALA A . n A 1 325 TRP 325 341 341 TRP TRP A . n A 1 326 ASP 326 342 342 ASP ASP A . n A 1 327 PHE 327 343 343 PHE PHE A . n A 1 328 TYR 328 344 344 TYR TYR A . n A 1 329 LEU 329 345 345 LEU LEU A . n A 1 330 THR 330 346 346 THR THR A . n A 1 331 ASP 331 347 347 ASP ASP A . n A 1 332 ASP 332 348 348 ASP ASP A . n A 1 333 VAL 333 349 349 VAL VAL A . n A 1 334 ARG 334 350 350 ARG ARG A . n A 1 335 ILE 335 351 351 ILE ILE A . n A 1 336 LYS 336 352 352 LYS LYS A . n A 1 337 GLN 337 353 353 GLN GLN A . n A 1 338 CYS 338 354 354 CYS CYS A . n A 1 339 THR 339 355 355 THR THR A . n A 1 340 ARG 340 356 356 ARG ARG A . n A 1 341 VAL 341 357 357 VAL VAL A . n A 1 342 THR 342 358 358 THR THR A . n A 1 343 GLN 343 359 359 GLN GLN A . n A 1 344 ASP 344 360 360 ASP ASP A . n A 1 345 GLN 345 361 361 GLN GLN A . n A 1 346 LEU 346 362 362 LEU LEU A . n A 1 347 PHE 347 363 363 PHE PHE A . n A 1 348 THR 348 364 364 THR THR A . n A 1 349 VAL 349 365 365 VAL VAL A . n A 1 350 HIS 350 366 366 HIS HIS A . n A 1 351 HIS 351 367 367 HIS HIS A . n A 1 352 GLU 352 368 368 GLU GLU A . n A 1 353 LEU 353 369 369 LEU LEU A . n A 1 354 GLY 354 370 370 GLY GLY A . n A 1 355 HIS 355 371 371 HIS HIS A . n A 1 356 ILE 356 372 372 ILE ILE A . n A 1 357 GLN 357 373 373 GLN GLN A . n A 1 358 TYR 358 374 374 TYR TYR A . n A 1 359 PHE 359 375 375 PHE PHE A . n A 1 360 LEU 360 376 376 LEU LEU A . n A 1 361 GLN 361 377 377 GLN GLN A . n A 1 362 TYR 362 378 378 TYR TYR A . n A 1 363 GLN 363 379 379 GLN GLN A . n A 1 364 HIS 364 380 380 HIS HIS A . n A 1 365 GLN 365 381 381 GLN GLN A . n A 1 366 PRO 366 382 382 PRO PRO A . n A 1 367 PHE 367 383 383 PHE PHE A . n A 1 368 VAL 368 384 384 VAL VAL A . n A 1 369 TYR 369 385 385 TYR TYR A . n A 1 370 ARG 370 386 386 ARG ARG A . n A 1 371 THR 371 387 387 THR THR A . n A 1 372 GLY 372 388 388 GLY GLY A . n A 1 373 ALA 373 389 389 ALA ALA A . n A 1 374 ASN 374 390 390 ASN ASN A . n A 1 375 PRO 375 391 391 PRO PRO A . n A 1 376 GLY 376 392 392 GLY GLY A . n A 1 377 PHE 377 393 393 PHE PHE A . n A 1 378 HIS 378 394 394 HIS HIS A . n A 1 379 GLU 379 395 395 GLU GLU A . n A 1 380 ALA 380 396 396 ALA ALA A . n A 1 381 VAL 381 397 397 VAL VAL A . n A 1 382 GLY 382 398 398 GLY GLY A . n A 1 383 ASP 383 399 399 ASP ASP A . n A 1 384 VAL 384 400 400 VAL VAL A . n A 1 385 LEU 385 401 401 LEU LEU A . n A 1 386 SER 386 402 402 SER SER A . n A 1 387 LEU 387 403 403 LEU LEU A . n A 1 388 SER 388 404 404 SER SER A . n A 1 389 VAL 389 405 405 VAL VAL A . n A 1 390 SER 390 406 406 SER SER A . n A 1 391 THR 391 407 407 THR THR A . n A 1 392 PRO 392 408 408 PRO PRO A . n A 1 393 LYS 393 409 409 LYS LYS A . n A 1 394 HIS 394 410 410 HIS HIS A . n A 1 395 LEU 395 411 411 LEU LEU A . n A 1 396 GLU 396 412 412 GLU GLU A . n A 1 397 LYS 397 413 413 LYS LYS A . n A 1 398 ILE 398 414 414 ILE ILE A . n A 1 399 GLY 399 415 415 GLY GLY A . n A 1 400 LEU 400 416 416 LEU LEU A . n A 1 401 LEU 401 417 417 LEU LEU A . n A 1 402 LYS 402 418 418 LYS LYS A . n A 1 403 ASP 403 419 419 ASP ASP A . n A 1 404 TYR 404 420 420 TYR TYR A . n A 1 405 VAL 405 421 421 VAL VAL A . n A 1 406 ARG 406 422 422 ARG ARG A . n A 1 407 ASP 407 423 423 ASP ASP A . n A 1 408 ASP 408 424 424 ASP ASP A . n A 1 409 GLU 409 425 425 GLU GLU A . n A 1 410 ALA 410 426 426 ALA ALA A . n A 1 411 ARG 411 427 427 ARG ARG A . n A 1 412 ILE 412 428 428 ILE ILE A . n A 1 413 ASN 413 429 429 ASN ASN A . n A 1 414 GLN 414 430 430 GLN GLN A . n A 1 415 LEU 415 431 431 LEU LEU A . n A 1 416 PHE 416 432 432 PHE PHE A . n A 1 417 LEU 417 433 433 LEU LEU A . n A 1 418 THR 418 434 434 THR THR A . n A 1 419 ALA 419 435 435 ALA ALA A . n A 1 420 LEU 420 436 436 LEU LEU A . n A 1 421 ASP 421 437 437 ASP ASP A . n A 1 422 LYS 422 438 438 LYS LYS A . n A 1 423 ILE 423 439 439 ILE ILE A . n A 1 424 VAL 424 440 440 VAL VAL A . n A 1 425 PHE 425 441 441 PHE PHE A . n A 1 426 LEU 426 442 442 LEU LEU A . n A 1 427 PRO 427 443 443 PRO PRO A . n A 1 428 PHE 428 444 444 PHE PHE A . n A 1 429 ALA 429 445 445 ALA ALA A . n A 1 430 PHE 430 446 446 PHE PHE A . n A 1 431 THR 431 447 447 THR THR A . n A 1 432 MET 432 448 448 MET MET A . n A 1 433 ASP 433 449 449 ASP ASP A . n A 1 434 LYS 434 450 450 LYS LYS A . n A 1 435 TYR 435 451 451 TYR TYR A . n A 1 436 ARG 436 452 452 ARG ARG A . n A 1 437 TRP 437 453 453 TRP TRP A . n A 1 438 SER 438 454 454 SER SER A . n A 1 439 LEU 439 455 455 LEU LEU A . n A 1 440 PHE 440 456 456 PHE PHE A . n A 1 441 ARG 441 457 457 ARG ARG A . n A 1 442 GLY 442 458 458 GLY GLY A . n A 1 443 GLU 443 459 459 GLU GLU A . n A 1 444 VAL 444 460 460 VAL VAL A . n A 1 445 ASP 445 461 461 ASP ASP A . n A 1 446 LYS 446 462 462 LYS LYS A . n A 1 447 ALA 447 463 463 ALA ALA A . n A 1 448 ASN 448 464 464 ASN ASN A . n A 1 449 TRP 449 465 465 TRP TRP A . n A 1 450 ASN 450 466 466 ASN ASN A . n A 1 451 CYS 451 467 467 CYS CYS A . n A 1 452 ALA 452 468 468 ALA ALA A . n A 1 453 PHE 453 469 469 PHE PHE A . n A 1 454 TRP 454 470 470 TRP TRP A . n A 1 455 LYS 455 471 471 LYS LYS A . n A 1 456 LEU 456 472 472 LEU LEU A . n A 1 457 ARG 457 473 473 ARG ARG A . n A 1 458 ASP 458 474 474 ASP ASP A . n A 1 459 GLU 459 475 475 GLU GLU A . n A 1 460 TYR 460 476 476 TYR TYR A . n A 1 461 SER 461 477 477 SER SER A . n A 1 462 GLY 462 478 478 GLY GLY A . n A 1 463 ILE 463 479 479 ILE ILE A . n A 1 464 GLU 464 480 480 GLU GLU A . n A 1 465 PRO 465 481 481 PRO PRO A . n A 1 466 PRO 466 482 482 PRO PRO A . n A 1 467 VAL 467 483 483 VAL VAL A . n A 1 468 VAL 468 484 484 VAL VAL A . n A 1 469 ARG 469 485 485 ARG ARG A . n A 1 470 SER 470 486 486 SER SER A . n A 1 471 GLU 471 487 487 GLU GLU A . n A 1 472 LYS 472 488 488 LYS LYS A . n A 1 473 ASP 473 489 489 ASP ASP A . n A 1 474 PHE 474 490 490 PHE PHE A . n A 1 475 ASP 475 491 491 ASP ASP A . n A 1 476 ALA 476 492 492 ALA ALA A . n A 1 477 PRO 477 493 493 PRO PRO A . n A 1 478 ALA 478 494 494 ALA ALA A . n A 1 479 LYS 479 495 495 LYS LYS A . n A 1 480 TYR 480 496 496 TYR TYR A . n A 1 481 HIS 481 497 497 HIS HIS A . n A 1 482 ILE 482 498 498 ILE ILE A . n A 1 483 SER 483 499 499 SER SER A . n A 1 484 ALA 484 500 500 ALA ALA A . n A 1 485 ASP 485 501 501 ASP ASP A . n A 1 486 VAL 486 502 502 VAL VAL A . n A 1 487 GLU 487 503 503 GLU GLU A . n A 1 488 TYR 488 504 504 TYR TYR A . n A 1 489 LEU 489 505 505 LEU LEU A . n A 1 490 ARG 490 506 506 ARG ARG A . n A 1 491 TYR 491 507 507 TYR TYR A . n A 1 492 LEU 492 508 508 LEU LEU A . n A 1 493 VAL 493 509 509 VAL VAL A . n A 1 494 SER 494 510 510 SER SER A . n A 1 495 PHE 495 511 511 PHE PHE A . n A 1 496 ILE 496 512 512 ILE ILE A . n A 1 497 ILE 497 513 513 ILE ILE A . n A 1 498 GLN 498 514 514 GLN GLN A . n A 1 499 PHE 499 515 515 PHE PHE A . n A 1 500 GLN 500 516 516 GLN GLN A . n A 1 501 PHE 501 517 517 PHE PHE A . n A 1 502 TYR 502 518 518 TYR TYR A . n A 1 503 LYS 503 519 519 LYS LYS A . n A 1 504 SER 504 520 520 SER SER A . n A 1 505 ALA 505 521 521 ALA ALA A . n A 1 506 CYS 506 522 522 CYS CYS A . n A 1 507 ILE 507 523 523 ILE ILE A . n A 1 508 LYS 508 524 524 LYS LYS A . n A 1 509 ALA 509 525 525 ALA ALA A . n A 1 510 GLY 510 526 526 GLY GLY A . n A 1 511 GLN 511 527 527 GLN GLN A . n A 1 512 TYR 512 528 528 TYR TYR A . n A 1 513 ASP 513 529 529 ASP ASP A . n A 1 514 PRO 514 530 530 PRO PRO A . n A 1 515 ASP 515 531 531 ASP ASP A . n A 1 516 ASN 516 532 532 ASN ASN A . n A 1 517 VAL 517 533 533 VAL VAL A . n A 1 518 GLU 518 534 534 GLU GLU A . n A 1 519 LEU 519 535 535 LEU LEU A . n A 1 520 PRO 520 536 536 PRO PRO A . n A 1 521 LEU 521 537 537 LEU LEU A . n A 1 522 ASP 522 538 538 ASP ASP A . n A 1 523 ASN 523 539 539 ASN ASN A . n A 1 524 CYS 524 540 540 CYS CYS A . n A 1 525 ASP 525 541 541 ASP ASP A . n A 1 526 ILE 526 542 542 ILE ILE A . n A 1 527 TYR 527 543 543 TYR TYR A . n A 1 528 GLY 528 544 544 GLY GLY A . n A 1 529 SER 529 545 545 SER SER A . n A 1 530 ALA 530 546 546 ALA ALA A . n A 1 531 ALA 531 547 547 ALA ALA A . n A 1 532 ALA 532 548 548 ALA ALA A . n A 1 533 GLY 533 549 549 GLY GLY A . n A 1 534 ALA 534 550 550 ALA ALA A . n A 1 535 ALA 535 551 551 ALA ALA A . n A 1 536 PHE 536 552 552 PHE PHE A . n A 1 537 HIS 537 553 553 HIS HIS A . n A 1 538 ASN 538 554 554 ASN ASN A . n A 1 539 MET 539 555 555 MET MET A . n A 1 540 LEU 540 556 556 LEU LEU A . n A 1 541 SER 541 557 557 SER SER A . n A 1 542 MET 542 558 558 MET MET A . n A 1 543 GLY 543 559 559 GLY GLY A . n A 1 544 ALA 544 560 560 ALA ALA A . n A 1 545 SER 545 561 561 SER SER A . n A 1 546 LYS 546 562 562 LYS LYS A . n A 1 547 PRO 547 563 563 PRO PRO A . n A 1 548 TRP 548 564 564 TRP TRP A . n A 1 549 PRO 549 565 565 PRO PRO A . n A 1 550 ASP 550 566 566 ASP ASP A . n A 1 551 ALA 551 567 567 ALA ALA A . n A 1 552 LEU 552 568 568 LEU LEU A . n A 1 553 GLU 553 569 569 GLU GLU A . n A 1 554 ALA 554 570 570 ALA ALA A . n A 1 555 PHE 555 571 571 PHE PHE A . n A 1 556 ASN 556 572 572 ASN ASN A . n A 1 557 GLY 557 573 573 GLY GLY A . n A 1 558 GLU 558 574 574 GLU GLU A . n A 1 559 ARG 559 575 575 ARG ARG A . n A 1 560 ILE 560 576 576 ILE ILE A . n A 1 561 MET 561 577 577 MET MET A . n A 1 562 SER 562 578 578 SER SER A . n A 1 563 GLY 563 579 579 GLY GLY A . n A 1 564 LYS 564 580 580 LYS LYS A . n A 1 565 ALA 565 581 581 ALA ALA A . n A 1 566 ILE 566 582 582 ILE ILE A . n A 1 567 ALA 567 583 583 ALA ALA A . n A 1 568 GLU 568 584 584 GLU GLU A . n A 1 569 TYR 569 585 585 TYR TYR A . n A 1 570 PHE 570 586 586 PHE PHE A . n A 1 571 GLU 571 587 587 GLU GLU A . n A 1 572 PRO 572 588 588 PRO PRO A . n A 1 573 LEU 573 589 589 LEU LEU A . n A 1 574 ARG 574 590 590 ARG ARG A . n A 1 575 VAL 575 591 591 VAL VAL A . n A 1 576 TRP 576 592 592 TRP TRP A . n A 1 577 LEU 577 593 593 LEU LEU A . n A 1 578 GLU 578 594 594 GLU GLU A . n A 1 579 ALA 579 595 595 ALA ALA A . n A 1 580 GLU 580 596 596 GLU GLU A . n A 1 581 ASN 581 597 597 ASN ASN A . n A 1 582 ILE 582 598 598 ILE ILE A . n A 1 583 LYS 583 599 599 LYS LYS A . n A 1 584 ASN 584 600 600 ASN ASN A . n A 1 585 ASN 585 601 601 ASN ASN A . n A 1 586 VAL 586 602 602 VAL VAL A . n A 1 587 HIS 587 603 603 HIS HIS A . n A 1 588 ILE 588 604 604 ILE ILE A . n A 1 589 GLY 589 605 605 GLY GLY A . n A 1 590 TRP 590 606 606 TRP TRP A . n A 1 591 THR 591 607 607 THR THR A . n A 1 592 THR 592 608 608 THR THR A . n A 1 593 SER 593 609 609 SER SER A . n A 1 594 ASN 594 610 610 ASN ASN A . n A 1 595 LYS 595 611 611 LYS LYS A . n A 1 596 CYS 596 612 612 CYS CYS A . n A 1 597 VAL 597 613 613 VAL VAL A . n A 1 598 SER 598 614 614 SER SER 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 ZN 1 1616 1616 ZN ZN A . C 3 NAG 1 1617 1617 NAG NAG A . D 3 NAG 2 1618 1618 NAG NAG A . E 4 BMA 3 1619 1619 BMA BMA A . F 5 MAN 4 1620 1620 MAN MAN A . G 5 MAN 5 1623 1623 MAN MAN A . H 4 BMA 6 1624 1624 BMA BMA A . I 3 NAG 1 1621 1621 NAG NAG A . J 3 NAG 1 1622 1622 NAG NAG A . K 6 3EF 1 1715 1715 3EF 3EF A . L 7 HOH 1 2001 2001 HOH HOH A . L 7 HOH 2 2002 2002 HOH HOH A . L 7 HOH 3 2003 2003 HOH HOH A . L 7 HOH 4 2004 2004 HOH HOH A . L 7 HOH 5 2005 2005 HOH HOH A . L 7 HOH 6 2006 2006 HOH HOH A . L 7 HOH 7 2007 2007 HOH HOH A . L 7 HOH 8 2008 2008 HOH HOH A . L 7 HOH 9 2009 2009 HOH HOH A . L 7 HOH 10 2010 2010 HOH HOH A . L 7 HOH 11 2011 2011 HOH HOH A . L 7 HOH 12 2012 2012 HOH HOH A . L 7 HOH 13 2013 2013 HOH HOH A . L 7 HOH 14 2014 2014 HOH HOH A . L 7 HOH 15 2015 2015 HOH HOH A . L 7 HOH 16 2016 2016 HOH HOH A . L 7 HOH 17 2017 2017 HOH HOH A . L 7 HOH 18 2018 2018 HOH HOH A . L 7 HOH 19 2019 2019 HOH HOH A . L 7 HOH 20 2020 2020 HOH HOH A . L 7 HOH 21 2021 2021 HOH HOH A . L 7 HOH 22 2022 2022 HOH HOH A . L 7 HOH 23 2023 2023 HOH HOH A . L 7 HOH 24 2024 2024 HOH HOH A . L 7 HOH 25 2025 2025 HOH HOH A . L 7 HOH 26 2026 2026 HOH HOH A . L 7 HOH 27 2027 2027 HOH HOH A . L 7 HOH 28 2028 2028 HOH HOH A . L 7 HOH 29 2029 2029 HOH HOH A . L 7 HOH 30 2030 2030 HOH HOH A . L 7 HOH 31 2031 2031 HOH HOH A . L 7 HOH 32 2032 2032 HOH HOH A . L 7 HOH 33 2033 2033 HOH HOH A . L 7 HOH 34 2034 2034 HOH HOH A . L 7 HOH 35 2035 2035 HOH HOH A . L 7 HOH 36 2036 2036 HOH HOH A . L 7 HOH 37 2037 2037 HOH HOH A . L 7 HOH 38 2038 2038 HOH HOH A . L 7 HOH 39 2039 2039 HOH HOH A . L 7 HOH 40 2040 2040 HOH HOH A . L 7 HOH 41 2041 2041 HOH HOH A . L 7 HOH 42 2042 2042 HOH HOH A . L 7 HOH 43 2043 2043 HOH HOH A . L 7 HOH 44 2044 2044 HOH HOH A . L 7 HOH 45 2045 2045 HOH HOH A . L 7 HOH 46 2046 2046 HOH HOH A . L 7 HOH 47 2047 2047 HOH HOH A . L 7 HOH 48 2048 2048 HOH HOH A . L 7 HOH 49 2049 2049 HOH HOH A . L 7 HOH 50 2050 2050 HOH HOH A . L 7 HOH 51 2051 2051 HOH HOH A . L 7 HOH 52 2052 2052 HOH HOH A . L 7 HOH 53 2053 2053 HOH HOH A . L 7 HOH 54 2054 2054 HOH HOH A . L 7 HOH 55 2055 2055 HOH HOH A . L 7 HOH 56 2056 2056 HOH HOH A . L 7 HOH 57 2057 2057 HOH HOH A . L 7 HOH 58 2058 2058 HOH HOH A . L 7 HOH 59 2059 2059 HOH HOH A . L 7 HOH 60 2060 2060 HOH HOH A . L 7 HOH 61 2061 2061 HOH HOH A . L 7 HOH 62 2062 2062 HOH HOH A . L 7 HOH 63 2063 2063 HOH HOH A . L 7 HOH 64 2064 2064 HOH HOH A . L 7 HOH 65 2065 2065 HOH HOH A . L 7 HOH 66 2066 2066 HOH HOH A . L 7 HOH 67 2067 2067 HOH HOH A . L 7 HOH 68 2068 2068 HOH HOH A . L 7 HOH 69 2069 2069 HOH HOH A . L 7 HOH 70 2070 2070 HOH HOH A . L 7 HOH 71 2071 2071 HOH HOH A . L 7 HOH 72 2072 2072 HOH HOH A . L 7 HOH 73 2073 2073 HOH HOH A . L 7 HOH 74 2074 2074 HOH HOH A . L 7 HOH 75 2075 2075 HOH HOH A . L 7 HOH 76 2076 2076 HOH HOH A . L 7 HOH 77 2077 2077 HOH HOH A . L 7 HOH 78 2078 2078 HOH HOH A . L 7 HOH 79 2079 2079 HOH HOH A . L 7 HOH 80 2080 2080 HOH HOH A . L 7 HOH 81 2081 2081 HOH HOH A . L 7 HOH 82 2082 2082 HOH HOH A . L 7 HOH 83 2083 2083 HOH HOH A . L 7 HOH 84 2084 2084 HOH HOH A . L 7 HOH 85 2085 2085 HOH HOH A . L 7 HOH 86 2086 2086 HOH HOH A . L 7 HOH 87 2087 2087 HOH HOH A . L 7 HOH 88 2088 2088 HOH HOH A . L 7 HOH 89 2089 2089 HOH HOH A . L 7 HOH 90 2090 2090 HOH HOH A . L 7 HOH 91 2091 2091 HOH HOH A . L 7 HOH 92 2092 2092 HOH HOH A . L 7 HOH 93 2093 2093 HOH HOH A . L 7 HOH 94 2094 2094 HOH HOH A . L 7 HOH 95 2095 2095 HOH HOH A . L 7 HOH 96 2096 2096 HOH HOH A . L 7 HOH 97 2097 2097 HOH HOH A . L 7 HOH 98 2098 2098 HOH HOH A . L 7 HOH 99 2099 2099 HOH HOH A . L 7 HOH 100 2100 2100 HOH HOH A . L 7 HOH 101 2101 2101 HOH HOH A . L 7 HOH 102 2102 2102 HOH HOH A . L 7 HOH 103 2103 2103 HOH HOH A . L 7 HOH 104 2104 2104 HOH HOH A . L 7 HOH 105 2105 2105 HOH HOH A . L 7 HOH 106 2106 2106 HOH HOH A . L 7 HOH 107 2107 2107 HOH HOH A . L 7 HOH 108 2108 2108 HOH HOH A . L 7 HOH 109 2109 2109 HOH HOH A . L 7 HOH 110 2110 2110 HOH HOH A . L 7 HOH 111 2111 2111 HOH HOH A . L 7 HOH 112 2112 2112 HOH HOH A . L 7 HOH 113 2113 2113 HOH HOH A . L 7 HOH 114 2114 2114 HOH HOH A . L 7 HOH 115 2115 2115 HOH HOH A . L 7 HOH 116 2116 2116 HOH HOH A . L 7 HOH 117 2117 2117 HOH HOH A . L 7 HOH 118 2118 2118 HOH HOH A . L 7 HOH 119 2119 2119 HOH HOH A . L 7 HOH 120 2120 2120 HOH HOH A . L 7 HOH 121 2121 2121 HOH HOH A . L 7 HOH 122 2122 2122 HOH HOH A . L 7 HOH 123 2123 2123 HOH HOH A . L 7 HOH 124 2124 2124 HOH HOH A . L 7 HOH 125 2125 2125 HOH HOH A . L 7 HOH 126 2126 2126 HOH HOH A . L 7 HOH 127 2127 2127 HOH HOH A . L 7 HOH 128 2128 2128 HOH HOH A . L 7 HOH 129 2129 2129 HOH HOH A . L 7 HOH 130 2130 2130 HOH HOH A . L 7 HOH 131 2131 2131 HOH HOH A . L 7 HOH 132 2132 2132 HOH HOH A . L 7 HOH 133 2133 2133 HOH HOH A . L 7 HOH 134 2134 2134 HOH HOH A . L 7 HOH 135 2135 2135 HOH HOH A . L 7 HOH 136 2136 2136 HOH HOH A . L 7 HOH 137 2137 2137 HOH HOH A . L 7 HOH 138 2138 2138 HOH HOH A . L 7 HOH 139 2139 2139 HOH HOH A . L 7 HOH 140 2140 2140 HOH HOH A . L 7 HOH 141 2141 2141 HOH HOH A . L 7 HOH 142 2142 2142 HOH HOH A . L 7 HOH 143 2143 2143 HOH HOH A . L 7 HOH 144 2144 2144 HOH HOH A . L 7 HOH 145 2145 2145 HOH HOH A . L 7 HOH 146 2146 2146 HOH HOH A . L 7 HOH 147 2147 2147 HOH HOH A . L 7 HOH 148 2148 2148 HOH HOH A . L 7 HOH 149 2149 2149 HOH HOH A . L 7 HOH 150 2150 2150 HOH HOH A . L 7 HOH 151 2151 2151 HOH HOH A . L 7 HOH 152 2152 2152 HOH HOH A . L 7 HOH 153 2153 2153 HOH HOH A . L 7 HOH 154 2154 2154 HOH HOH A . L 7 HOH 155 2155 2155 HOH HOH A . L 7 HOH 156 2156 2156 HOH HOH A . L 7 HOH 157 2157 2157 HOH HOH A . L 7 HOH 158 2158 2158 HOH HOH A . L 7 HOH 159 2159 2159 HOH HOH A . L 7 HOH 160 2160 2160 HOH HOH A . L 7 HOH 161 2161 2161 HOH HOH A . L 7 HOH 162 2162 2162 HOH HOH A . L 7 HOH 163 2163 2163 HOH HOH A . L 7 HOH 164 2164 2164 HOH HOH A . L 7 HOH 165 2165 2165 HOH HOH A . L 7 HOH 166 2166 2166 HOH HOH A . L 7 HOH 167 2167 2167 HOH HOH A . L 7 HOH 168 2168 2168 HOH HOH A . L 7 HOH 169 2169 2169 HOH HOH A . L 7 HOH 170 2170 2170 HOH HOH A . L 7 HOH 171 2171 2171 HOH HOH A . L 7 HOH 172 2172 2172 HOH HOH A . L 7 HOH 173 2173 2173 HOH HOH A . L 7 HOH 174 2174 2174 HOH HOH A . L 7 HOH 175 2175 2175 HOH HOH A . L 7 HOH 176 2176 2176 HOH HOH A . L 7 HOH 177 2177 2177 HOH HOH A . L 7 HOH 178 2178 2178 HOH HOH A . L 7 HOH 179 2179 2179 HOH HOH A . L 7 HOH 180 2180 2180 HOH HOH A . L 7 HOH 181 2181 2181 HOH HOH A . L 7 HOH 182 2182 2182 HOH HOH A . L 7 HOH 183 2183 2183 HOH HOH A . L 7 HOH 184 2184 2184 HOH HOH A . L 7 HOH 185 2185 2185 HOH HOH A . L 7 HOH 186 2186 2186 HOH HOH A . L 7 HOH 187 2187 2187 HOH HOH A . L 7 HOH 188 2188 2188 HOH HOH A . L 7 HOH 189 2189 2189 HOH HOH A . L 7 HOH 190 2190 2190 HOH HOH A . L 7 HOH 191 2191 2191 HOH HOH A . L 7 HOH 192 2192 2192 HOH HOH A . L 7 HOH 193 2193 2193 HOH HOH A . L 7 HOH 194 2194 2194 HOH HOH A . L 7 HOH 195 2195 2195 HOH HOH A . L 7 HOH 196 2196 2196 HOH HOH A . L 7 HOH 197 2197 2197 HOH HOH A . L 7 HOH 198 2198 2198 HOH HOH A . L 7 HOH 199 2199 2199 HOH HOH A . L 7 HOH 200 2200 2200 HOH HOH A . L 7 HOH 201 2201 2201 HOH HOH A . L 7 HOH 202 2202 2202 HOH HOH A . L 7 HOH 203 2203 2203 HOH HOH A . L 7 HOH 204 2204 2204 HOH HOH A . L 7 HOH 205 2205 2205 HOH HOH A . L 7 HOH 206 2206 2206 HOH HOH A . L 7 HOH 207 2207 2207 HOH HOH A . L 7 HOH 208 2208 2208 HOH HOH A . L 7 HOH 209 2209 2209 HOH HOH A . L 7 HOH 210 2210 2210 HOH HOH A . L 7 HOH 211 2211 2211 HOH HOH A . L 7 HOH 212 2212 2212 HOH HOH A . L 7 HOH 213 2213 2213 HOH HOH A . L 7 HOH 214 2214 2214 HOH HOH A . L 7 HOH 215 2215 2215 HOH HOH A . L 7 HOH 216 2216 2216 HOH HOH A . L 7 HOH 217 2217 2217 HOH HOH A . L 7 HOH 218 2218 2218 HOH HOH A . L 7 HOH 219 2219 2219 HOH HOH A . L 7 HOH 220 2220 2220 HOH HOH A . L 7 HOH 221 2221 2221 HOH HOH A . L 7 HOH 222 2222 2222 HOH HOH A . L 7 HOH 223 2223 2223 HOH HOH A . L 7 HOH 224 2224 2224 HOH HOH A . L 7 HOH 225 2225 2225 HOH HOH A . L 7 HOH 226 2226 2226 HOH HOH A . L 7 HOH 227 2227 2227 HOH HOH A . L 7 HOH 228 2228 2228 HOH HOH A . L 7 HOH 229 2229 2229 HOH HOH A . L 7 HOH 230 2230 2230 HOH HOH A . L 7 HOH 231 2231 2231 HOH HOH A . L 7 HOH 232 2232 2232 HOH HOH A . L 7 HOH 233 2233 2233 HOH HOH A . L 7 HOH 234 2234 2234 HOH HOH A . L 7 HOH 235 2235 2235 HOH HOH A . L 7 HOH 236 2236 2236 HOH HOH A . L 7 HOH 237 2237 2237 HOH HOH A . L 7 HOH 238 2238 2238 HOH HOH A . L 7 HOH 239 2239 2239 HOH HOH A . L 7 HOH 240 2240 2240 HOH HOH A . L 7 HOH 241 2241 2241 HOH HOH A . L 7 HOH 242 2242 2242 HOH HOH A . L 7 HOH 243 2243 2243 HOH HOH A . L 7 HOH 244 2244 2244 HOH HOH A . L 7 HOH 245 2245 2245 HOH HOH A . L 7 HOH 246 2246 2246 HOH HOH A . L 7 HOH 247 2247 2247 HOH HOH A . L 7 HOH 248 2248 2248 HOH HOH A . L 7 HOH 249 2249 2249 HOH HOH A . L 7 HOH 250 2250 2250 HOH HOH A . L 7 HOH 251 2251 2251 HOH HOH A . L 7 HOH 252 2252 2252 HOH HOH A . L 7 HOH 253 2253 2253 HOH HOH A . L 7 HOH 254 2254 2254 HOH HOH A . L 7 HOH 255 2255 2255 HOH HOH A . L 7 HOH 256 2256 2256 HOH HOH A . L 7 HOH 257 2257 2257 HOH HOH A . L 7 HOH 258 2258 2258 HOH HOH A . L 7 HOH 259 2259 2259 HOH HOH A . L 7 HOH 260 2260 2260 HOH HOH A . L 7 HOH 261 2261 2261 HOH HOH A . L 7 HOH 262 2262 2262 HOH HOH A . L 7 HOH 263 2263 2263 HOH HOH A . L 7 HOH 264 2264 2264 HOH HOH A . L 7 HOH 265 2265 2265 HOH HOH A . L 7 HOH 266 2266 2266 HOH HOH A . L 7 HOH 267 2267 2267 HOH HOH A . L 7 HOH 268 2268 2268 HOH HOH A . L 7 HOH 269 2269 2269 HOH HOH A . L 7 HOH 270 2270 2270 HOH HOH A . L 7 HOH 271 2271 2271 HOH HOH A . L 7 HOH 272 2272 2272 HOH HOH A . L 7 HOH 273 2273 2273 HOH HOH A . L 7 HOH 274 2274 2274 HOH HOH A . L 7 HOH 275 2275 2275 HOH HOH A . L 7 HOH 276 2276 2276 HOH HOH A . L 7 HOH 277 2277 2277 HOH HOH A . L 7 HOH 278 2278 2278 HOH HOH A . L 7 HOH 279 2279 2279 HOH HOH A . L 7 HOH 280 2280 2280 HOH HOH A . L 7 HOH 281 2281 2281 HOH HOH A . L 7 HOH 282 2282 2282 HOH HOH A . L 7 HOH 283 2283 2283 HOH HOH A . L 7 HOH 284 2284 2284 HOH HOH A . L 7 HOH 285 2285 2285 HOH HOH A . L 7 HOH 286 2286 2286 HOH HOH A . L 7 HOH 287 2287 2287 HOH HOH A . L 7 HOH 288 2288 2288 HOH HOH A . L 7 HOH 289 2289 2289 HOH HOH A . L 7 HOH 290 2290 2290 HOH HOH A . L 7 HOH 291 2291 2291 HOH HOH A . L 7 HOH 292 2292 2292 HOH HOH A . L 7 HOH 293 2293 2293 HOH HOH A . L 7 HOH 294 2294 2294 HOH HOH A . L 7 HOH 295 2295 2295 HOH HOH A . L 7 HOH 296 2296 2296 HOH HOH A . L 7 HOH 297 2297 2297 HOH HOH A . L 7 HOH 298 2298 2298 HOH HOH A . L 7 HOH 299 2299 2299 HOH HOH A . L 7 HOH 300 2300 2300 HOH HOH A . L 7 HOH 301 2301 2301 HOH HOH A . L 7 HOH 302 2302 2302 HOH HOH A . L 7 HOH 303 2303 2303 HOH HOH A . L 7 HOH 304 2304 2304 HOH HOH A . L 7 HOH 305 2305 2305 HOH HOH A . L 7 HOH 306 2306 2306 HOH HOH A . L 7 HOH 307 2307 2307 HOH HOH A . L 7 HOH 308 2308 2308 HOH HOH A . L 7 HOH 309 2309 2309 HOH HOH A . L 7 HOH 310 2310 2310 HOH HOH A . L 7 HOH 311 2311 2311 HOH HOH A . L 7 HOH 312 2312 2312 HOH HOH A . L 7 HOH 313 2313 2313 HOH HOH A . L 7 HOH 314 2314 2314 HOH HOH A . L 7 HOH 315 2315 2315 HOH HOH A . L 7 HOH 316 2316 2316 HOH HOH A . L 7 HOH 317 2317 2317 HOH HOH A . L 7 HOH 318 2318 2318 HOH HOH A . L 7 HOH 319 2319 2319 HOH HOH A . L 7 HOH 320 2320 2320 HOH HOH A . L 7 HOH 321 2321 2321 HOH HOH A . L 7 HOH 322 2322 2322 HOH HOH A . L 7 HOH 323 2323 2323 HOH HOH A . L 7 HOH 324 2324 2324 HOH HOH A . L 7 HOH 325 2325 2325 HOH HOH A . L 7 HOH 326 2326 2326 HOH HOH A . L 7 HOH 327 2327 2327 HOH HOH A . L 7 HOH 328 2328 2328 HOH HOH A . L 7 HOH 329 2329 2329 HOH HOH A . L 7 HOH 330 2330 2330 HOH HOH A . L 7 HOH 331 2331 2331 HOH HOH A . L 7 HOH 332 2332 2332 HOH HOH A . L 7 HOH 333 2333 2333 HOH HOH A . L 7 HOH 334 2334 2334 HOH HOH A . L 7 HOH 335 2335 2335 HOH HOH A . L 7 HOH 336 2336 2336 HOH HOH A . L 7 HOH 337 2337 2337 HOH HOH A . L 7 HOH 338 2338 2338 HOH HOH A . L 7 HOH 339 2339 2339 HOH HOH A . L 7 HOH 340 2340 2340 HOH HOH A . L 7 HOH 341 2341 2341 HOH HOH A . L 7 HOH 342 2342 2342 HOH HOH A . L 7 HOH 343 2343 2343 HOH HOH A . L 7 HOH 344 2344 2344 HOH HOH A . L 7 HOH 345 2345 2345 HOH HOH A . L 7 HOH 346 2346 2346 HOH HOH A . L 7 HOH 347 2347 2347 HOH HOH A . L 7 HOH 348 2348 2348 HOH HOH A . L 7 HOH 349 2349 2349 HOH HOH A . L 7 HOH 350 2350 2350 HOH HOH A . L 7 HOH 351 2351 2351 HOH HOH A . L 7 HOH 352 2352 2352 HOH HOH A . L 7 HOH 353 2353 2353 HOH HOH A . L 7 HOH 354 2354 2354 HOH HOH A . L 7 HOH 355 2355 2355 HOH HOH A . L 7 HOH 356 2356 2356 HOH HOH A . L 7 HOH 357 2357 2357 HOH HOH A . L 7 HOH 358 2358 2358 HOH HOH A . L 7 HOH 359 2359 2359 HOH HOH A . L 7 HOH 360 2360 2360 HOH HOH A . L 7 HOH 361 2361 2361 HOH HOH A . L 7 HOH 362 2362 2362 HOH HOH A . L 7 HOH 363 2363 2363 HOH HOH A . L 7 HOH 364 2364 2364 HOH HOH A . L 7 HOH 365 2365 2365 HOH HOH A . L 7 HOH 366 2366 2366 HOH HOH A . L 7 HOH 367 2367 2367 HOH HOH A . L 7 HOH 368 2368 2368 HOH HOH A . L 7 HOH 369 2369 2369 HOH HOH A . L 7 HOH 370 2370 2370 HOH HOH A . L 7 HOH 371 2371 2371 HOH HOH A . L 7 HOH 372 2372 2372 HOH HOH A . L 7 HOH 373 2373 2373 HOH HOH A . L 7 HOH 374 2374 2374 HOH HOH A . L 7 HOH 375 2375 2375 HOH HOH A . L 7 HOH 376 2376 2376 HOH HOH A . L 7 HOH 377 2377 2377 HOH HOH A . L 7 HOH 378 2378 2378 HOH HOH A . L 7 HOH 379 2379 2379 HOH HOH A . L 7 HOH 380 2380 2380 HOH HOH A . L 7 HOH 381 2381 2381 HOH HOH A . L 7 HOH 382 2382 2382 HOH HOH A . L 7 HOH 383 2383 2383 HOH HOH A . L 7 HOH 384 2384 2384 HOH HOH A . L 7 HOH 385 2385 2385 HOH HOH A . L 7 HOH 386 2386 2386 HOH HOH A . L 7 HOH 387 2387 2387 HOH HOH A . L 7 HOH 388 2388 2388 HOH HOH A . L 7 HOH 389 2389 2389 HOH HOH A . L 7 HOH 390 2390 2390 HOH HOH A . L 7 HOH 391 2391 2391 HOH HOH A . L 7 HOH 392 2392 2392 HOH HOH A . L 7 HOH 393 2393 2393 HOH HOH A . L 7 HOH 394 2394 2394 HOH HOH A . L 7 HOH 395 2395 2395 HOH HOH A . L 7 HOH 396 2396 2396 HOH HOH A . L 7 HOH 397 2397 2397 HOH HOH A . L 7 HOH 398 2398 2398 HOH HOH A . L 7 HOH 399 2399 2399 HOH HOH A . L 7 HOH 400 2400 2400 HOH HOH A . L 7 HOH 401 2401 2401 HOH HOH A . L 7 HOH 402 2402 2402 HOH HOH A . L 7 HOH 403 2403 2403 HOH HOH A . L 7 HOH 404 2404 2404 HOH HOH A . L 7 HOH 405 2405 2405 HOH HOH A . L 7 HOH 406 2406 2406 HOH HOH A . L 7 HOH 407 2407 2407 HOH HOH A . L 7 HOH 408 2408 2408 HOH HOH A . L 7 HOH 409 2409 2409 HOH HOH A . L 7 HOH 410 2410 2410 HOH HOH A . L 7 HOH 411 2411 2411 HOH HOH A . L 7 HOH 412 2412 2412 HOH HOH A . L 7 HOH 413 2413 2413 HOH HOH A . L 7 HOH 414 2414 2414 HOH HOH A . L 7 HOH 415 2415 2415 HOH HOH A . L 7 HOH 416 2416 2416 HOH HOH A . L 7 HOH 417 2417 2417 HOH HOH A . L 7 HOH 418 2418 2418 HOH HOH A . L 7 HOH 419 2419 2419 HOH HOH A . L 7 HOH 420 2420 2420 HOH HOH A . L 7 HOH 421 2421 2421 HOH HOH A . L 7 HOH 422 2422 2422 HOH HOH A . L 7 HOH 423 2423 2423 HOH HOH A . L 7 HOH 424 2424 2424 HOH HOH A . L 7 HOH 425 2425 2425 HOH HOH A . L 7 HOH 426 2426 2426 HOH HOH A . L 7 HOH 427 2427 2427 HOH HOH A . L 7 HOH 428 2428 2428 HOH HOH A . L 7 HOH 429 2429 2429 HOH HOH A . L 7 HOH 430 2430 2430 HOH HOH A . L 7 HOH 431 2431 2431 HOH HOH A . L 7 HOH 432 2432 2432 HOH HOH A . L 7 HOH 433 2433 2433 HOH HOH A . L 7 HOH 434 2434 2434 HOH HOH A . L 7 HOH 435 2435 2435 HOH HOH A . L 7 HOH 436 2436 2436 HOH HOH A . L 7 HOH 437 2437 2437 HOH HOH A . L 7 HOH 438 2438 2438 HOH HOH A . L 7 HOH 439 2439 2439 HOH HOH A . L 7 HOH 440 2440 2440 HOH HOH A . L 7 HOH 441 2441 2441 HOH HOH A . L 7 HOH 442 2442 2442 HOH HOH A . L 7 HOH 443 2443 2443 HOH HOH A . L 7 HOH 444 2444 2444 HOH HOH A . L 7 HOH 445 2445 2445 HOH HOH A . L 7 HOH 446 2446 2446 HOH HOH A . L 7 HOH 447 2447 2447 HOH HOH A . L 7 HOH 448 2448 2448 HOH HOH A . L 7 HOH 449 2449 2449 HOH HOH A . L 7 HOH 450 2450 2450 HOH HOH A . L 7 HOH 451 2451 2451 HOH HOH A . L 7 HOH 452 2452 2452 HOH HOH A . L 7 HOH 453 2453 2453 HOH HOH A . L 7 HOH 454 2454 2454 HOH HOH A . L 7 HOH 455 2455 2455 HOH HOH A . L 7 HOH 456 2456 2456 HOH HOH A . L 7 HOH 457 2457 2457 HOH HOH A . L 7 HOH 458 2458 2458 HOH HOH A . L 7 HOH 459 2459 2459 HOH HOH A . L 7 HOH 460 2460 2460 HOH HOH A . L 7 HOH 461 2461 2461 HOH HOH A . L 7 HOH 462 2462 2462 HOH HOH A . L 7 HOH 463 2463 2463 HOH HOH A . L 7 HOH 464 2464 2464 HOH HOH A . L 7 HOH 465 2465 2465 HOH HOH A . L 7 HOH 466 2466 2466 HOH HOH A . L 7 HOH 467 2467 2467 HOH HOH A . L 7 HOH 468 2468 2468 HOH HOH A . L 7 HOH 469 2469 2469 HOH HOH A . L 7 HOH 470 2470 2470 HOH HOH A . L 7 HOH 471 2471 2471 HOH HOH A . L 7 HOH 472 2472 2472 HOH HOH A . L 7 HOH 473 2473 2473 HOH HOH A . L 7 HOH 474 2474 2474 HOH HOH A . L 7 HOH 475 2475 2475 HOH HOH A . L 7 HOH 476 2476 2476 HOH HOH A . L 7 HOH 477 2477 2477 HOH HOH A . L 7 HOH 478 2478 2478 HOH HOH A . L 7 HOH 479 2479 2479 HOH HOH A . L 7 HOH 480 2480 2480 HOH HOH A . L 7 HOH 481 2481 2481 HOH HOH A . L 7 HOH 482 2482 2482 HOH HOH A . L 7 HOH 483 2483 2483 HOH HOH A . L 7 HOH 484 2484 2484 HOH HOH A . L 7 HOH 485 2485 2485 HOH HOH A . L 7 HOH 486 2486 2486 HOH HOH A . L 7 HOH 487 2487 2487 HOH HOH A . L 7 HOH 488 2488 2488 HOH HOH A . L 7 HOH 489 2489 2489 HOH HOH A . L 7 HOH 490 2490 2490 HOH HOH A . L 7 HOH 491 2491 2491 HOH HOH A . L 7 HOH 492 2492 2492 HOH HOH A . L 7 HOH 493 2493 2493 HOH HOH A . L 7 HOH 494 2494 2494 HOH HOH A . L 7 HOH 495 2495 2495 HOH HOH A . L 7 HOH 496 2496 2496 HOH HOH A . L 7 HOH 497 2497 2497 HOH HOH A . L 7 HOH 498 2498 2498 HOH HOH A . L 7 HOH 499 2499 2499 HOH HOH A . L 7 HOH 500 2500 2500 HOH HOH A . L 7 HOH 501 2501 2501 HOH HOH A . L 7 HOH 502 2502 2502 HOH HOH A . L 7 HOH 503 2503 2503 HOH HOH A . L 7 HOH 504 2504 2504 HOH HOH A . L 7 HOH 505 2505 2505 HOH HOH A . L 7 HOH 506 2506 2506 HOH HOH A . L 7 HOH 507 2507 2507 HOH HOH A . L 7 HOH 508 2508 2508 HOH HOH A . L 7 HOH 509 2509 2509 HOH HOH A . L 7 HOH 510 2510 2510 HOH HOH A . L 7 HOH 511 2511 2511 HOH HOH A . L 7 HOH 512 2512 2512 HOH HOH A . L 7 HOH 513 2513 2513 HOH HOH A . L 7 HOH 514 2514 2514 HOH HOH A . L 7 HOH 515 2515 2515 HOH HOH A . L 7 HOH 516 2516 2516 HOH HOH A . L 7 HOH 517 2517 2517 HOH HOH A . L 7 HOH 518 2518 2518 HOH HOH A . L 7 HOH 519 2519 2519 HOH HOH A . L 7 HOH 520 2520 2520 HOH HOH A . L 7 HOH 521 2521 2521 HOH HOH A . L 7 HOH 522 2522 2522 HOH HOH A . L 7 HOH 523 2523 2523 HOH HOH A . L 7 HOH 524 2524 2524 HOH HOH A . L 7 HOH 525 2525 2525 HOH HOH A . L 7 HOH 526 2526 2526 HOH HOH A . L 7 HOH 527 2527 2527 HOH HOH A . L 7 HOH 528 2528 2528 HOH HOH A . L 7 HOH 529 2529 2529 HOH HOH A . L 7 HOH 530 2530 2530 HOH HOH A . L 7 HOH 531 2531 2531 HOH HOH A . L 7 HOH 532 2532 2532 HOH HOH A . L 7 HOH 533 2533 2533 HOH HOH A . L 7 HOH 534 2534 2534 HOH HOH A . L 7 HOH 535 2535 2535 HOH HOH A . L 7 HOH 536 2536 2536 HOH HOH A . L 7 HOH 537 2537 2537 HOH HOH A . L 7 HOH 538 2538 2538 HOH HOH A . L 7 HOH 539 2539 2539 HOH HOH A . L 7 HOH 540 2540 2540 HOH HOH A . L 7 HOH 541 2541 2541 HOH HOH A . L 7 HOH 542 2542 2542 HOH HOH A . L 7 HOH 543 2543 2543 HOH HOH A . L 7 HOH 544 2544 2544 HOH HOH A . L 7 HOH 545 2545 2545 HOH HOH A . L 7 HOH 546 2546 2546 HOH HOH A . L 7 HOH 547 2547 2547 HOH HOH A . L 7 HOH 548 2548 2548 HOH HOH A . L 7 HOH 549 2549 2549 HOH HOH A . L 7 HOH 550 2550 2550 HOH HOH A . L 7 HOH 551 2551 2551 HOH HOH A . L 7 HOH 552 2552 2552 HOH HOH A . L 7 HOH 553 2553 2553 HOH HOH A . L 7 HOH 554 2554 2554 HOH HOH A . L 7 HOH 555 2555 2555 HOH HOH A . L 7 HOH 556 2556 2556 HOH HOH A . L 7 HOH 557 2557 2557 HOH HOH A . L 7 HOH 558 2558 2558 HOH HOH A . L 7 HOH 559 2559 2559 HOH HOH A . L 7 HOH 560 2560 2560 HOH HOH A . L 7 HOH 561 2561 2561 HOH HOH A . L 7 HOH 562 2562 2562 HOH HOH A . L 7 HOH 563 2563 2563 HOH HOH A . L 7 HOH 564 2564 2564 HOH HOH A . L 7 HOH 565 2565 2565 HOH HOH A . L 7 HOH 566 2566 2566 HOH HOH A . L 7 HOH 567 2567 2567 HOH HOH A . L 7 HOH 568 2568 2568 HOH HOH A . L 7 HOH 569 2569 2569 HOH HOH A . L 7 HOH 570 2570 2570 HOH HOH A . L 7 HOH 571 2571 2571 HOH HOH A . L 7 HOH 572 2572 2572 HOH HOH A . L 7 HOH 573 2573 2573 HOH HOH A . L 7 HOH 574 2574 2574 HOH HOH A . L 7 HOH 575 2575 2575 HOH HOH A . L 7 HOH 576 2576 2576 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 37 A ASN 53 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 180 A ASN 196 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 295 A ASN 311 ? 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 # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 NE2 ? A HIS 355 ? A HIS 371 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 NE2 ? A HIS 351 ? A HIS 367 ? 1_555 105.9 ? 2 NE2 ? A HIS 355 ? A HIS 371 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 PBY ? K 3EF . ? A 3EF 1715 ? 1_555 111.2 ? 3 NE2 ? A HIS 351 ? A HIS 367 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 PBY ? K 3EF . ? A 3EF 1715 ? 1_555 107.6 ? 4 NE2 ? A HIS 355 ? A HIS 371 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OAD ? K 3EF . ? A 3EF 1715 ? 1_555 136.9 ? 5 NE2 ? A HIS 351 ? A HIS 367 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OAD ? K 3EF . ? A 3EF 1715 ? 1_555 109.0 ? 6 PBY ? K 3EF . ? A 3EF 1715 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OAD ? K 3EF . ? A 3EF 1715 ? 1_555 33.3 ? 7 NE2 ? A HIS 355 ? A HIS 371 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OAG ? K 3EF . ? A 3EF 1715 ? 1_555 86.3 ? 8 NE2 ? A HIS 351 ? A HIS 367 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OAG ? K 3EF . ? A 3EF 1715 ? 1_555 95.2 ? 9 PBY ? K 3EF . ? A 3EF 1715 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OAG ? K 3EF . ? A 3EF 1715 ? 1_555 33.2 ? 10 OAD ? K 3EF . ? A 3EF 1715 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OAG ? K 3EF . ? A 3EF 1715 ? 1_555 66.2 ? 11 NE2 ? A HIS 355 ? A HIS 371 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OE1 ? A GLU 379 ? A GLU 395 ? 1_555 100.4 ? 12 NE2 ? A HIS 351 ? A HIS 367 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OE1 ? A GLU 379 ? A GLU 395 ? 1_555 97.1 ? 13 PBY ? K 3EF . ? A 3EF 1715 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OE1 ? A GLU 379 ? A GLU 395 ? 1_555 131.6 ? 14 OAD ? K 3EF . ? A 3EF 1715 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OE1 ? A GLU 379 ? A GLU 395 ? 1_555 99.7 ? 15 OAG ? K 3EF . ? A 3EF 1715 ? 1_555 ZN ? B ZN . ? A ZN 1616 ? 1_555 OE1 ? A GLU 379 ? A GLU 395 ? 1_555 163.7 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-12-11 2 'Structure model' 1 1 2014-02-12 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 31.4833 _pdbx_refine_tls.origin_y -3.0573 _pdbx_refine_tls.origin_z 12.9183 _pdbx_refine_tls.T[1][1] 0.0741 _pdbx_refine_tls.T[2][2] 0.0969 _pdbx_refine_tls.T[3][3] 0.0577 _pdbx_refine_tls.T[1][2] 0.0096 _pdbx_refine_tls.T[1][3] -0.0009 _pdbx_refine_tls.T[2][3] -0.0089 _pdbx_refine_tls.L[1][1] 0.3361 _pdbx_refine_tls.L[2][2] 0.3696 _pdbx_refine_tls.L[3][3] 0.1478 _pdbx_refine_tls.L[1][2] -0.0709 _pdbx_refine_tls.L[1][3] -0.0051 _pdbx_refine_tls.L[2][3] 0.1980 _pdbx_refine_tls.S[1][1] -0.0187 _pdbx_refine_tls.S[1][2] 0.0188 _pdbx_refine_tls.S[1][3] -0.0060 _pdbx_refine_tls.S[2][1] -0.0198 _pdbx_refine_tls.S[2][2] -0.0716 _pdbx_refine_tls.S[2][3] 0.1384 _pdbx_refine_tls.S[3][1] -0.0010 _pdbx_refine_tls.S[3][2] 0.0171 _pdbx_refine_tls.S[3][3] 0.0903 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 1 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 1624 _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.7.0029 ? 1 XDS 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4CA7 _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ;5,6-DIHYDRO-BENZO[H]CINNOLIN-3-YLAMINE (DRG): ENANTIOMER OF COMPOUND 3ES SEEN IN PDB FILES 2XY9 AND 2XYD ; _pdbx_entry_details.sequence_details ? # 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 ASN A 53 ? ? -164.22 81.06 2 1 LEU A 345 ? ? -107.98 -134.38 3 1 PRO A 493 ? ? -67.02 0.75 4 1 ASN A 572 ? ? -141.99 14.14 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2203 ? 6.19 . 2 1 O ? A HOH 2206 ? 6.06 . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A GLN 24 ? C ? A GLN 8 C 2 1 Y 1 A GLN 24 ? O ? A GLN 8 O # 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 ALA 17 ? A ALA 1 2 1 Y 1 A LEU 18 ? A LEU 2 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'ZINC ION' ZN 3 N-ACETYL-D-GLUCOSAMINE NAG 4 BETA-D-MANNOSE BMA 5 ALPHA-D-MANNOSE MAN 6 ;N-{(2S)-3-[(S)-[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl]-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tyrosine ; 3EF 7 water HOH #