data_4CCC # _entry.id 4CCC # _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 4CCC PDBE EBI-58780 WWPDB D_1290058780 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4CCD unspecified 'STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME-INTERMEDIATE COMPLEX' PDB 4CCE unspecified 'STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH GALACTOSE: ENZYME-PRODUCT COMPLEX' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4CCC _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2013-10-21 _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 'Hill, C.H.' 1 'Graham, S.C.' 2 'Read, R.J.' 3 'Deane, J.E.' 4 # _citation.id primary _citation.title 'Structural Snapshots Illustrate the Catalytic Cycle of Beta-Galactocerebrosidase, the Defective Enzyme in Krabbe Disease' _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 110 _citation.page_first 20479 _citation.page_last ? _citation.year 2013 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24297913 _citation.pdbx_database_id_DOI 10.1073/PNAS.1311990110 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Hill, C.H.' 1 primary 'Graham, S.C.' 2 primary 'Read, R.J.' 3 primary 'Deane, J.E.' 4 # _cell.entry_id 4CCC _cell.length_a 250.012 _cell.length_b 250.012 _cell.length_c 77.790 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 18 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4CCC _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # 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 GALACTOCEREBROSIDASE 74596.750 1 3.2.1.46 ? 'RESIDUES 41-684' 'FRAGMENT CORRESPONDS TO RESIDUES 25-668 BASED ON NUMBERING STARTING AT SECOND UNIPROT INITIATION SITE.' 2 non-polymer man '1-O-[P-NITROPHENYL]-BETA-D-GALACTOPYRANOSE' 301.249 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 5 water nat water 18.015 272 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;GALCERASE, GALACTOCEREBROSIDE BETA-GALACTOSIDASE, GALACTOSYLCERAMIDASE, GALACTOSYLCERAMIDE BETA-GALACTOSIDASE, BETA-GALACTOCEREBROSIDASE, GALC ; # _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 ;HHHHHHIEGRGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSEILDYLFKPNFGASLHILKVEIGGDGQTTD GTEPSHMHYELDENYFRGYEWWLMKEAKKRNPDIILMGLPWSFPGWLGKGFSWPYVNLQLTAYYVVRWILGAKHYHDLDI DYIGIWNERPFDANYIKELRKMLDYQGLQRVRIIASDNLWEPISSSLLLDQELWKVVDVIGAHYPGTYTVWNAKMSGKKL WSSEDFSTINSNVGAGCWSRILNQNYINGNMTSTIAWNLVASYYEELPYGRSGLMTAQEPWSGHYVVASPIWVSAHTTQF TQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHQHSMCIRPYLPYYNVSHQLATFTLKGSLREIQELQVWYTKL GTPQQRLHFKQLDTLWLLDGSGSFTLELEEDEIFTLTTLTTGRKGSYPPPPSSKPFPTNYKDDFNVEYPLFSEAPNFADQ TGVFEYYMNNEDREHRFTLRQVLNQRPITWAADASSTISVIGDHHWTNMTVQCDVYIETPRSGGVFIAGRVNKGGILIRS ATGVFFWIFANGSYRVTADLGGWITYASGHADVTAKRWYTLTLGIKGYFAFGMLNGTILWKNVRVKYPGHGWAAIGTHTF EFAQFDNFRVEAAR ; _entity_poly.pdbx_seq_one_letter_code_can ;HHHHHHIEGRGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSEILDYLFKPNFGASLHILKVEIGGDGQTTD GTEPSHMHYELDENYFRGYEWWLMKEAKKRNPDIILMGLPWSFPGWLGKGFSWPYVNLQLTAYYVVRWILGAKHYHDLDI DYIGIWNERPFDANYIKELRKMLDYQGLQRVRIIASDNLWEPISSSLLLDQELWKVVDVIGAHYPGTYTVWNAKMSGKKL WSSEDFSTINSNVGAGCWSRILNQNYINGNMTSTIAWNLVASYYEELPYGRSGLMTAQEPWSGHYVVASPIWVSAHTTQF TQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHQHSMCIRPYLPYYNVSHQLATFTLKGSLREIQELQVWYTKL GTPQQRLHFKQLDTLWLLDGSGSFTLELEEDEIFTLTTLTTGRKGSYPPPPSSKPFPTNYKDDFNVEYPLFSEAPNFADQ TGVFEYYMNNEDREHRFTLRQVLNQRPITWAADASSTISVIGDHHWTNMTVQCDVYIETPRSGGVFIAGRVNKGGILIRS ATGVFFWIFANGSYRVTADLGGWITYASGHADVTAKRWYTLTLGIKGYFAFGMLNGTILWKNVRVKYPGHGWAAIGTHTF EFAQFDNFRVEAAR ; _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 HIS n 1 2 HIS n 1 3 HIS n 1 4 HIS n 1 5 HIS n 1 6 HIS n 1 7 ILE n 1 8 GLU n 1 9 GLY n 1 10 ARG n 1 11 GLY n 1 12 ALA n 1 13 TYR n 1 14 VAL n 1 15 LEU n 1 16 ASP n 1 17 ASP n 1 18 SER n 1 19 ASP n 1 20 GLY n 1 21 LEU n 1 22 GLY n 1 23 ARG n 1 24 GLU n 1 25 PHE n 1 26 ASP n 1 27 GLY n 1 28 ILE n 1 29 GLY n 1 30 ALA n 1 31 VAL n 1 32 SER n 1 33 GLY n 1 34 GLY n 1 35 GLY n 1 36 ALA n 1 37 THR n 1 38 SER n 1 39 ARG n 1 40 LEU n 1 41 LEU n 1 42 VAL n 1 43 ASN n 1 44 TYR n 1 45 PRO n 1 46 GLU n 1 47 PRO n 1 48 TYR n 1 49 ARG n 1 50 SER n 1 51 GLU n 1 52 ILE n 1 53 LEU n 1 54 ASP n 1 55 TYR n 1 56 LEU n 1 57 PHE n 1 58 LYS n 1 59 PRO n 1 60 ASN n 1 61 PHE n 1 62 GLY n 1 63 ALA n 1 64 SER n 1 65 LEU n 1 66 HIS n 1 67 ILE n 1 68 LEU n 1 69 LYS n 1 70 VAL n 1 71 GLU n 1 72 ILE n 1 73 GLY n 1 74 GLY n 1 75 ASP n 1 76 GLY n 1 77 GLN n 1 78 THR n 1 79 THR n 1 80 ASP n 1 81 GLY n 1 82 THR n 1 83 GLU n 1 84 PRO n 1 85 SER n 1 86 HIS n 1 87 MET n 1 88 HIS n 1 89 TYR n 1 90 GLU n 1 91 LEU n 1 92 ASP n 1 93 GLU n 1 94 ASN n 1 95 TYR n 1 96 PHE n 1 97 ARG n 1 98 GLY n 1 99 TYR n 1 100 GLU n 1 101 TRP n 1 102 TRP n 1 103 LEU n 1 104 MET n 1 105 LYS n 1 106 GLU n 1 107 ALA n 1 108 LYS n 1 109 LYS n 1 110 ARG n 1 111 ASN n 1 112 PRO n 1 113 ASP n 1 114 ILE n 1 115 ILE n 1 116 LEU n 1 117 MET n 1 118 GLY n 1 119 LEU n 1 120 PRO n 1 121 TRP n 1 122 SER n 1 123 PHE n 1 124 PRO n 1 125 GLY n 1 126 TRP n 1 127 LEU n 1 128 GLY n 1 129 LYS n 1 130 GLY n 1 131 PHE n 1 132 SER n 1 133 TRP n 1 134 PRO n 1 135 TYR n 1 136 VAL n 1 137 ASN n 1 138 LEU n 1 139 GLN n 1 140 LEU n 1 141 THR n 1 142 ALA n 1 143 TYR n 1 144 TYR n 1 145 VAL n 1 146 VAL n 1 147 ARG n 1 148 TRP n 1 149 ILE n 1 150 LEU n 1 151 GLY n 1 152 ALA n 1 153 LYS n 1 154 HIS n 1 155 TYR n 1 156 HIS n 1 157 ASP n 1 158 LEU n 1 159 ASP n 1 160 ILE n 1 161 ASP n 1 162 TYR n 1 163 ILE n 1 164 GLY n 1 165 ILE n 1 166 TRP n 1 167 ASN n 1 168 GLU n 1 169 ARG n 1 170 PRO n 1 171 PHE n 1 172 ASP n 1 173 ALA n 1 174 ASN n 1 175 TYR n 1 176 ILE n 1 177 LYS n 1 178 GLU n 1 179 LEU n 1 180 ARG n 1 181 LYS n 1 182 MET n 1 183 LEU n 1 184 ASP n 1 185 TYR n 1 186 GLN n 1 187 GLY n 1 188 LEU n 1 189 GLN n 1 190 ARG n 1 191 VAL n 1 192 ARG n 1 193 ILE n 1 194 ILE n 1 195 ALA n 1 196 SER n 1 197 ASP n 1 198 ASN n 1 199 LEU n 1 200 TRP n 1 201 GLU n 1 202 PRO n 1 203 ILE n 1 204 SER n 1 205 SER n 1 206 SER n 1 207 LEU n 1 208 LEU n 1 209 LEU n 1 210 ASP n 1 211 GLN n 1 212 GLU n 1 213 LEU n 1 214 TRP n 1 215 LYS n 1 216 VAL n 1 217 VAL n 1 218 ASP n 1 219 VAL n 1 220 ILE n 1 221 GLY n 1 222 ALA n 1 223 HIS n 1 224 TYR n 1 225 PRO n 1 226 GLY n 1 227 THR n 1 228 TYR n 1 229 THR n 1 230 VAL n 1 231 TRP n 1 232 ASN n 1 233 ALA n 1 234 LYS n 1 235 MET n 1 236 SER n 1 237 GLY n 1 238 LYS n 1 239 LYS n 1 240 LEU n 1 241 TRP n 1 242 SER n 1 243 SER n 1 244 GLU n 1 245 ASP n 1 246 PHE n 1 247 SER n 1 248 THR n 1 249 ILE n 1 250 ASN n 1 251 SER n 1 252 ASN n 1 253 VAL n 1 254 GLY n 1 255 ALA n 1 256 GLY n 1 257 CYS n 1 258 TRP n 1 259 SER n 1 260 ARG n 1 261 ILE n 1 262 LEU n 1 263 ASN n 1 264 GLN n 1 265 ASN n 1 266 TYR n 1 267 ILE n 1 268 ASN n 1 269 GLY n 1 270 ASN n 1 271 MET n 1 272 THR n 1 273 SER n 1 274 THR n 1 275 ILE n 1 276 ALA n 1 277 TRP n 1 278 ASN n 1 279 LEU n 1 280 VAL n 1 281 ALA n 1 282 SER n 1 283 TYR n 1 284 TYR n 1 285 GLU n 1 286 GLU n 1 287 LEU n 1 288 PRO n 1 289 TYR n 1 290 GLY n 1 291 ARG n 1 292 SER n 1 293 GLY n 1 294 LEU n 1 295 MET n 1 296 THR n 1 297 ALA n 1 298 GLN n 1 299 GLU n 1 300 PRO n 1 301 TRP n 1 302 SER n 1 303 GLY n 1 304 HIS n 1 305 TYR n 1 306 VAL n 1 307 VAL n 1 308 ALA n 1 309 SER n 1 310 PRO n 1 311 ILE n 1 312 TRP n 1 313 VAL n 1 314 SER n 1 315 ALA n 1 316 HIS n 1 317 THR n 1 318 THR n 1 319 GLN n 1 320 PHE n 1 321 THR n 1 322 GLN n 1 323 PRO n 1 324 GLY n 1 325 TRP n 1 326 TYR n 1 327 TYR n 1 328 LEU n 1 329 LYS n 1 330 THR n 1 331 VAL n 1 332 GLY n 1 333 HIS n 1 334 LEU n 1 335 GLU n 1 336 LYS n 1 337 GLY n 1 338 GLY n 1 339 SER n 1 340 TYR n 1 341 VAL n 1 342 ALA n 1 343 LEU n 1 344 THR n 1 345 ASP n 1 346 GLY n 1 347 LEU n 1 348 GLY n 1 349 ASN n 1 350 LEU n 1 351 THR n 1 352 ILE n 1 353 ILE n 1 354 ILE n 1 355 GLU n 1 356 THR n 1 357 MET n 1 358 SER n 1 359 HIS n 1 360 GLN n 1 361 HIS n 1 362 SER n 1 363 MET n 1 364 CYS n 1 365 ILE n 1 366 ARG n 1 367 PRO n 1 368 TYR n 1 369 LEU n 1 370 PRO n 1 371 TYR n 1 372 TYR n 1 373 ASN n 1 374 VAL n 1 375 SER n 1 376 HIS n 1 377 GLN n 1 378 LEU n 1 379 ALA n 1 380 THR n 1 381 PHE n 1 382 THR n 1 383 LEU n 1 384 LYS n 1 385 GLY n 1 386 SER n 1 387 LEU n 1 388 ARG n 1 389 GLU n 1 390 ILE n 1 391 GLN n 1 392 GLU n 1 393 LEU n 1 394 GLN n 1 395 VAL n 1 396 TRP n 1 397 TYR n 1 398 THR n 1 399 LYS n 1 400 LEU n 1 401 GLY n 1 402 THR n 1 403 PRO n 1 404 GLN n 1 405 GLN n 1 406 ARG n 1 407 LEU n 1 408 HIS n 1 409 PHE n 1 410 LYS n 1 411 GLN n 1 412 LEU n 1 413 ASP n 1 414 THR n 1 415 LEU n 1 416 TRP n 1 417 LEU n 1 418 LEU n 1 419 ASP n 1 420 GLY n 1 421 SER n 1 422 GLY n 1 423 SER n 1 424 PHE n 1 425 THR n 1 426 LEU n 1 427 GLU n 1 428 LEU n 1 429 GLU n 1 430 GLU n 1 431 ASP n 1 432 GLU n 1 433 ILE n 1 434 PHE n 1 435 THR n 1 436 LEU n 1 437 THR n 1 438 THR n 1 439 LEU n 1 440 THR n 1 441 THR n 1 442 GLY n 1 443 ARG n 1 444 LYS n 1 445 GLY n 1 446 SER n 1 447 TYR n 1 448 PRO n 1 449 PRO n 1 450 PRO n 1 451 PRO n 1 452 SER n 1 453 SER n 1 454 LYS n 1 455 PRO n 1 456 PHE n 1 457 PRO n 1 458 THR n 1 459 ASN n 1 460 TYR n 1 461 LYS n 1 462 ASP n 1 463 ASP n 1 464 PHE n 1 465 ASN n 1 466 VAL n 1 467 GLU n 1 468 TYR n 1 469 PRO n 1 470 LEU n 1 471 PHE n 1 472 SER n 1 473 GLU n 1 474 ALA n 1 475 PRO n 1 476 ASN n 1 477 PHE n 1 478 ALA n 1 479 ASP n 1 480 GLN n 1 481 THR n 1 482 GLY n 1 483 VAL n 1 484 PHE n 1 485 GLU n 1 486 TYR n 1 487 TYR n 1 488 MET n 1 489 ASN n 1 490 ASN n 1 491 GLU n 1 492 ASP n 1 493 ARG n 1 494 GLU n 1 495 HIS n 1 496 ARG n 1 497 PHE n 1 498 THR n 1 499 LEU n 1 500 ARG n 1 501 GLN n 1 502 VAL n 1 503 LEU n 1 504 ASN n 1 505 GLN n 1 506 ARG n 1 507 PRO n 1 508 ILE n 1 509 THR n 1 510 TRP n 1 511 ALA n 1 512 ALA n 1 513 ASP n 1 514 ALA n 1 515 SER n 1 516 SER n 1 517 THR n 1 518 ILE n 1 519 SER n 1 520 VAL n 1 521 ILE n 1 522 GLY n 1 523 ASP n 1 524 HIS n 1 525 HIS n 1 526 TRP n 1 527 THR n 1 528 ASN n 1 529 MET n 1 530 THR n 1 531 VAL n 1 532 GLN n 1 533 CYS n 1 534 ASP n 1 535 VAL n 1 536 TYR n 1 537 ILE n 1 538 GLU n 1 539 THR n 1 540 PRO n 1 541 ARG n 1 542 SER n 1 543 GLY n 1 544 GLY n 1 545 VAL n 1 546 PHE n 1 547 ILE n 1 548 ALA n 1 549 GLY n 1 550 ARG n 1 551 VAL n 1 552 ASN n 1 553 LYS n 1 554 GLY n 1 555 GLY n 1 556 ILE n 1 557 LEU n 1 558 ILE n 1 559 ARG n 1 560 SER n 1 561 ALA n 1 562 THR n 1 563 GLY n 1 564 VAL n 1 565 PHE n 1 566 PHE n 1 567 TRP n 1 568 ILE n 1 569 PHE n 1 570 ALA n 1 571 ASN n 1 572 GLY n 1 573 SER n 1 574 TYR n 1 575 ARG n 1 576 VAL n 1 577 THR n 1 578 ALA n 1 579 ASP n 1 580 LEU n 1 581 GLY n 1 582 GLY n 1 583 TRP n 1 584 ILE n 1 585 THR n 1 586 TYR n 1 587 ALA n 1 588 SER n 1 589 GLY n 1 590 HIS n 1 591 ALA n 1 592 ASP n 1 593 VAL n 1 594 THR n 1 595 ALA n 1 596 LYS n 1 597 ARG n 1 598 TRP n 1 599 TYR n 1 600 THR n 1 601 LEU n 1 602 THR n 1 603 LEU n 1 604 GLY n 1 605 ILE n 1 606 LYS n 1 607 GLY n 1 608 TYR n 1 609 PHE n 1 610 ALA n 1 611 PHE n 1 612 GLY n 1 613 MET n 1 614 LEU n 1 615 ASN n 1 616 GLY n 1 617 THR n 1 618 ILE n 1 619 LEU n 1 620 TRP n 1 621 LYS n 1 622 ASN n 1 623 VAL n 1 624 ARG n 1 625 VAL n 1 626 LYS n 1 627 TYR n 1 628 PRO n 1 629 GLY n 1 630 HIS n 1 631 GLY n 1 632 TRP n 1 633 ALA n 1 634 ALA n 1 635 ILE n 1 636 GLY n 1 637 THR n 1 638 HIS n 1 639 THR n 1 640 PHE n 1 641 GLU n 1 642 PHE n 1 643 ALA n 1 644 GLN n 1 645 PHE n 1 646 ASP n 1 647 ASN n 1 648 PHE n 1 649 ARG n 1 650 VAL n 1 651 GLU n 1 652 ALA n 1 653 ALA n 1 654 ARG 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 'HOUSE MOUSE' _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 'MUS MUSCULUS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 10090 _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 'HOMO SAPIENS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _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 HEK293T _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 PLASMID _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PSECTAG2B _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code GALC_MOUSE _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P54818 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4CCC _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 11 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 654 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P54818 _struct_ref_seq.db_align_beg 41 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 684 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 25 _struct_ref_seq.pdbx_auth_seq_align_end 668 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4CCC HIS A 1 ? UNP P54818 ? ? 'expression tag' 15 1 1 4CCC HIS A 2 ? UNP P54818 ? ? 'expression tag' 16 2 1 4CCC HIS A 3 ? UNP P54818 ? ? 'expression tag' 17 3 1 4CCC HIS A 4 ? UNP P54818 ? ? 'expression tag' 18 4 1 4CCC HIS A 5 ? UNP P54818 ? ? 'expression tag' 19 5 1 4CCC HIS A 6 ? UNP P54818 ? ? 'expression tag' 20 6 1 4CCC ILE A 7 ? UNP P54818 ? ? 'expression tag' 21 7 1 4CCC GLU A 8 ? UNP P54818 ? ? 'expression tag' 22 8 1 4CCC GLY A 9 ? UNP P54818 ? ? 'expression tag' 23 9 1 4CCC ARG A 10 ? UNP P54818 ? ? 'expression tag' 24 10 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight 147 D-saccharide . '1-O-[P-NITROPHENYL]-BETA-D-GALACTOPYRANOSE' ? 'C12 H15 N O8' 301.249 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 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 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 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4CCC _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.23 _exptl_crystal.density_percent_sol 61.9 _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 6.8 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '34% PEG 8000, 200 MM SODIUM ACETATE, 100 MM SODIUM CACODYLATE PH 6.8' # _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 2012-08-03 _diffrn_detector.details 'SI (111) DOUBLE CRYSTAL MONOCHROMATOR. KIRKPATRICK BAEZ BIMORPH MIRROR PAIR FOR HORIZONTAL AND VERTICAL FOCUSSING' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'DOUBLE CRYSTAL' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.92 _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 0.92 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CCC _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 56.38 _reflns.d_resolution_high 2.09 _reflns.number_obs 54656 _reflns.number_all ? _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs 0.15 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 13.50 _reflns.B_iso_Wilson_estimate 31.32 _reflns.pdbx_redundancy 19.0 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.09 _reflns_shell.d_res_low 2.15 _reflns_shell.percent_possible_all 99.4 _reflns_shell.Rmerge_I_obs 1.29 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.50 _reflns_shell.pdbx_redundancy 14.8 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CCC _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 54646 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.36 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 56.382 _refine.ls_d_res_high 2.090 _refine.ls_percent_reflns_obs 99.87 _refine.ls_R_factor_obs 0.1891 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1872 _refine.ls_R_factor_R_free 0.2240 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 2773 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details 'RESIDUES 416-419 ARE DISORDERED.' _refine.pdbx_starting_model 'PDB ENTRY 3ZR5' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.23 _refine.pdbx_overall_phase_error 21.84 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5110 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 120 _refine_hist.number_atoms_solvent 272 _refine_hist.number_atoms_total 5502 _refine_hist.d_res_high 2.090 _refine_hist.d_res_low 56.382 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.008 ? ? 5411 'X-RAY DIFFRACTION' ? f_angle_d 1.125 ? ? 7390 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 16.444 ? ? 1894 'X-RAY DIFFRACTION' ? f_chiral_restr 0.076 ? ? 792 'X-RAY DIFFRACTION' ? f_plane_restr 0.004 ? ? 926 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all 'X-RAY DIFFRACTION' . 2.0899 2.1259 2561 0.2878 99.00 0.2680 . . 138 . . 'X-RAY DIFFRACTION' . 2.1259 2.1646 2609 0.2703 100.00 0.3250 . . 120 . . 'X-RAY DIFFRACTION' . 2.1646 2.2062 2590 0.2605 100.00 0.2790 . . 114 . . 'X-RAY DIFFRACTION' . 2.2062 2.2513 2589 0.2672 100.00 0.2787 . . 141 . . 'X-RAY DIFFRACTION' . 2.2513 2.3002 2566 0.2541 100.00 0.2955 . . 148 . . 'X-RAY DIFFRACTION' . 2.3002 2.3537 2575 0.2510 100.00 0.2747 . . 140 . . 'X-RAY DIFFRACTION' . 2.3537 2.4126 2579 0.2411 100.00 0.2654 . . 151 . . 'X-RAY DIFFRACTION' . 2.4126 2.4778 2559 0.2203 100.00 0.2950 . . 157 . . 'X-RAY DIFFRACTION' . 2.4778 2.5507 2574 0.2140 100.00 0.2825 . . 152 . . 'X-RAY DIFFRACTION' . 2.5507 2.6330 2591 0.2116 100.00 0.2084 . . 126 . . 'X-RAY DIFFRACTION' . 2.6330 2.7272 2553 0.2026 100.00 0.2342 . . 157 . . 'X-RAY DIFFRACTION' . 2.7272 2.8363 2592 0.2035 100.00 0.2330 . . 144 . . 'X-RAY DIFFRACTION' . 2.8363 2.9654 2608 0.1994 100.00 0.2357 . . 125 . . 'X-RAY DIFFRACTION' . 2.9654 3.1218 2618 0.2023 100.00 0.2297 . . 129 . . 'X-RAY DIFFRACTION' . 3.1218 3.3173 2576 0.1984 100.00 0.2507 . . 139 . . 'X-RAY DIFFRACTION' . 3.3173 3.5734 2622 0.1801 100.00 0.2205 . . 129 . . 'X-RAY DIFFRACTION' . 3.5734 3.9329 2597 0.1601 100.00 0.2087 . . 149 . . 'X-RAY DIFFRACTION' . 3.9329 4.5018 2612 0.1404 100.00 0.1855 . . 135 . . 'X-RAY DIFFRACTION' . 4.5018 5.6710 2637 0.1330 100.00 0.1435 . . 136 . . 'X-RAY DIFFRACTION' . 5.6710 56.4023 2665 0.1592 99.00 0.2043 . . 143 . . # _struct.entry_id 4CCC _struct.title 'STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH 4NBDG: ENZYME-SUBSTRATE COMPLEX' _struct.pdbx_descriptor 'GALACTOCEREBROSIDASE (E.C.3.2.1.46)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CCC _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text ;HYDROLASE, KRABBE DISEASE, GLYCOSYL HYDROLASE, 4-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE, LYSOSOMAL STORAGE DISEASE, ENZYME- SUBSTRATE COMPLEX ; # 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 3 ? F N N 3 ? G N N 3 ? H N N 3 ? I N N 3 ? J N N 4 ? K N N 5 ? # _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 PRO A 47 ? LYS A 58 ? PRO A 61 LYS A 72 1 ? 12 HELX_P HELX_P2 2 TYR A 99 ? ASN A 111 ? TYR A 113 ASN A 125 1 ? 13 HELX_P HELX_P3 3 PRO A 124 ? LYS A 129 ? PRO A 138 LYS A 143 5 ? 6 HELX_P HELX_P4 4 ASN A 137 ? ASP A 157 ? ASN A 151 ASP A 171 1 ? 21 HELX_P HELX_P5 5 ASP A 172 ? GLN A 186 ? ASP A 186 GLN A 200 1 ? 15 HELX_P HELX_P6 6 PRO A 202 ? ASP A 210 ? PRO A 216 ASP A 224 1 ? 9 HELX_P HELX_P7 7 ASP A 210 ? VAL A 217 ? ASP A 224 VAL A 231 1 ? 8 HELX_P HELX_P8 8 VAL A 230 ? GLY A 237 ? VAL A 244 GLY A 251 1 ? 8 HELX_P HELX_P9 9 SER A 251 ? ASN A 270 ? SER A 265 ASN A 284 1 ? 20 HELX_P HELX_P10 10 ALA A 308 ? GLN A 319 ? ALA A 322 GLN A 333 1 ? 12 HELX_P HELX_P11 11 SER A 358 ? SER A 362 ? SER A 372 SER A 376 5 ? 5 HELX_P HELX_P12 12 GLY A 385 ? ARG A 388 ? GLY A 399 ARG A 402 5 ? 4 HELX_P HELX_P13 13 GLY A 554 ? SER A 560 ? GLY A 568 SER A 574 5 ? 7 # _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 257 SG ? ? ? 1_555 A CYS 364 SG ? ? A CYS 271 A CYS 378 1_555 ? ? ? ? ? ? ? 2.040 ? covale1 covale ? ? A ASN 270 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 284 A NAG 1284 1_555 ? ? ? ? ? ? ? 1.444 ? covale2 covale ? ? A ASN 349 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 363 A NAG 1363 1_555 ? ? ? ? ? ? ? 1.435 ? covale3 covale ? ? A ASN 373 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 387 A NAG 1387 1_555 ? ? ? ? ? ? ? 1.453 ? covale4 covale ? ? A ASN 528 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 542 A NAG 1542 1_555 ? ? ? ? ? ? ? 1.437 ? covale5 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 1284 A NAG 1285 1_555 ? ? ? ? ? ? ? 1.454 ? covale6 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 1363 A NAG 1364 1_555 ? ? ? ? ? ? ? 1.444 ? covale7 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 1542 A NAG 1543 1_555 ? ? ? ? ? ? ? 1.440 ? metalc1 metalc ? ? J CA . CA ? ? ? 1_555 A ASN 465 OD1 ? ? A CA 1669 A ASN 479 1_555 ? ? ? ? ? ? ? 2.381 ? metalc2 metalc ? ? J CA . CA ? ? ? 1_555 A ASP 463 O ? ? A CA 1669 A ASP 477 1_555 ? ? ? ? ? ? ? 2.430 ? metalc3 metalc ? ? J CA . CA ? ? ? 1_555 A ASP 646 OD1 ? ? A CA 1669 A ASP 660 1_555 ? ? ? ? ? ? ? 2.498 ? metalc4 metalc ? ? J CA . CA ? ? ? 1_555 K HOH . O ? ? A CA 1669 A HOH 2209 1_555 ? ? ? ? ? ? ? 2.435 ? metalc5 metalc ? ? J CA . CA ? ? ? 1_555 A PHE 497 O ? ? A CA 1669 A PHE 511 1_555 ? ? ? ? ? ? ? 2.317 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 GLY 34 A . ? GLY 48 A GLY 35 A ? GLY 49 A 1 4.15 2 GLU 46 A . ? GLU 60 A PRO 47 A ? PRO 61 A 1 3.62 3 ALA 195 A . ? ALA 209 A SER 196 A ? SER 210 A 1 -1.58 4 GLU 201 A . ? GLU 215 A PRO 202 A ? PRO 216 A 1 6.67 5 TRP 277 A . ? TRP 291 A ASN 278 A ? ASN 292 A 1 2.50 6 ARG 366 A . ? ARG 380 A PRO 367 A ? PRO 381 A 1 -3.90 7 TYR 627 A . ? TYR 641 A PRO 628 A ? PRO 642 A 1 -3.46 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 3 ? AB ? 7 ? AC ? 4 ? AD ? 9 ? AE ? 2 ? AF ? 2 ? AG ? 7 ? AH ? 4 ? AI ? 7 ? # 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 ? parallel AA 2 3 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AB 4 5 ? anti-parallel AB 5 6 ? anti-parallel AB 6 7 ? anti-parallel AC 1 2 ? anti-parallel AC 2 3 ? anti-parallel AC 3 4 ? parallel AD 1 2 ? parallel AD 2 3 ? parallel AD 3 4 ? parallel AD 4 5 ? parallel AD 5 6 ? parallel AD 6 7 ? parallel AD 7 8 ? parallel AD 8 9 ? parallel AE 1 2 ? parallel AF 1 2 ? parallel AG 1 2 ? anti-parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AG 5 6 ? anti-parallel AG 6 7 ? anti-parallel AH 1 2 ? anti-parallel AH 2 3 ? anti-parallel AH 3 4 ? parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AI 3 4 ? anti-parallel AI 4 5 ? anti-parallel AI 5 6 ? anti-parallel AI 6 7 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 ALA A 12 ? LEU A 15 ? ALA A 26 LEU A 29 AA 2 GLN A 377 ? LEU A 383 ? GLN A 391 LEU A 397 AA 3 SER A 423 ? LEU A 428 ? SER A 437 LEU A 442 AB 1 LEU A 21 ? GLU A 24 ? LEU A 35 GLU A 38 AB 2 TYR A 326 ? LEU A 328 ? TYR A 340 LEU A 342 AB 3 SER A 339 ? THR A 344 ? SER A 353 THR A 358 AB 4 LEU A 350 ? GLU A 355 ? LEU A 364 GLU A 369 AB 5 GLU A 432 ? THR A 437 ? GLU A 446 THR A 451 AB 6 GLU A 392 ? LYS A 399 ? GLU A 406 LYS A 413 AB 7 LEU A 407 ? TRP A 416 ? LEU A 421 TRP A 430 AC 1 LEU A 21 ? GLU A 24 ? LEU A 35 GLU A 38 AC 2 TYR A 326 ? LEU A 328 ? TYR A 340 LEU A 342 AC 3 SER A 339 ? THR A 344 ? SER A 353 THR A 358 AC 4 GLY A 332 ? HIS A 333 ? GLY A 346 HIS A 347 AD 1 GLY A 27 ? SER A 32 ? GLY A 41 SER A 46 AD 2 SER A 273 ? TRP A 277 ? SER A 287 TRP A 291 AD 3 LYS A 239 ? PHE A 246 ? LYS A 253 PHE A 260 AD 4 VAL A 219 ? HIS A 223 ? VAL A 233 HIS A 237 AD 5 ARG A 192 ? ASN A 198 ? ARG A 206 ASN A 212 AD 6 TYR A 162 ? ILE A 163 ? TYR A 176 ILE A 177 AD 7 ILE A 115 ? PRO A 120 ? ILE A 129 PRO A 134 AD 8 ILE A 67 ? ILE A 72 ? ILE A 81 ILE A 86 AD 9 GLY A 27 ? SER A 32 ? GLY A 41 SER A 46 AE 1 VAL A 280 ? ALA A 281 ? VAL A 294 ALA A 295 AE 2 MET A 295 ? THR A 296 ? MET A 309 THR A 310 AF 1 ASN A 459 ? ASP A 462 ? ASN A 473 ASP A 476 AF 2 ALA A 643 ? ALA A 653 ? ALA A 657 ALA A 667 AG 1 PHE A 484 ? MET A 488 ? PHE A 498 MET A 502 AG 2 PHE A 497 ? GLN A 501 ? PHE A 511 GLN A 515 AG 3 ALA A 643 ? ALA A 653 ? ALA A 657 ALA A 667 AG 4 ASN A 528 ? ILE A 537 ? ASN A 542 ILE A 551 AG 5 TRP A 598 ? LYS A 606 ? TRP A 612 LYS A 620 AG 6 PHE A 609 ? LEU A 614 ? PHE A 623 LEU A 628 AG 7 THR A 617 ? ARG A 624 ? THR A 631 ARG A 638 AH 1 PHE A 484 ? MET A 488 ? PHE A 498 MET A 502 AH 2 PHE A 497 ? GLN A 501 ? PHE A 511 GLN A 515 AH 3 ALA A 643 ? ALA A 653 ? ALA A 657 ALA A 667 AH 4 ASN A 459 ? ASP A 462 ? ASN A 473 ASP A 476 AI 1 ALA A 478 ? THR A 481 ? ALA A 492 THR A 495 AI 2 THR A 517 ? ILE A 521 ? THR A 531 ILE A 535 AI 3 TRP A 632 ? THR A 637 ? TRP A 646 THR A 651 AI 4 GLY A 544 ? VAL A 551 ? GLY A 558 VAL A 565 AI 5 THR A 562 ? PHE A 569 ? THR A 576 PHE A 583 AI 6 SER A 573 ? ASP A 579 ? SER A 587 ASP A 593 AI 7 THR A 585 ? HIS A 590 ? THR A 599 HIS A 604 # 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 TYR A 13 ? N TYR A 27 O THR A 380 ? O THR A 394 AA 2 3 N PHE A 381 ? N PHE A 395 O PHE A 424 ? O PHE A 438 AB 1 2 N GLY A 22 ? N GLY A 36 O TYR A 327 ? O TYR A 341 AB 2 3 N LEU A 328 ? N LEU A 342 O ALA A 342 ? O ALA A 356 AB 3 4 N LEU A 343 ? N LEU A 357 O THR A 351 ? O THR A 365 AB 4 5 N ILE A 354 ? N ILE A 368 O PHE A 434 ? O PHE A 448 AB 5 6 N THR A 437 ? N THR A 451 O GLN A 394 ? O GLN A 408 AB 6 7 N LYS A 399 ? N LYS A 413 O LEU A 407 ? O LEU A 421 AC 1 2 N GLY A 22 ? N GLY A 36 O TYR A 327 ? O TYR A 341 AC 2 3 N LEU A 328 ? N LEU A 342 O ALA A 342 ? O ALA A 356 AC 3 4 N TYR A 340 ? N TYR A 354 O GLY A 332 ? O GLY A 346 AD 1 2 N GLY A 29 ? N GLY A 43 O THR A 274 ? O THR A 288 AD 2 3 N ILE A 275 ? N ILE A 289 O SER A 242 ? O SER A 256 AD 3 4 N TRP A 241 ? N TRP A 255 O ILE A 220 ? O ILE A 234 AD 4 5 N GLY A 221 ? N GLY A 235 O ALA A 195 ? O ALA A 209 AD 5 6 N ILE A 194 ? N ILE A 208 O ILE A 163 ? O ILE A 177 AD 6 7 N TYR A 162 ? N TYR A 176 O LEU A 116 ? O LEU A 130 AD 7 8 N MET A 117 ? N MET A 131 O LEU A 68 ? O LEU A 82 AD 8 9 N LYS A 69 ? N LYS A 83 O ALA A 30 ? O ALA A 44 AE 1 2 N ALA A 281 ? N ALA A 295 O MET A 295 ? O MET A 309 AF 1 2 N ASP A 462 ? N ASP A 476 O PHE A 648 ? O PHE A 662 AG 1 2 N TYR A 487 ? N TYR A 501 O THR A 498 ? O THR A 512 AG 2 3 N GLN A 501 ? N GLN A 515 O ALA A 643 ? O ALA A 657 AG 3 4 N ALA A 653 ? N ALA A 667 O ASN A 528 ? O ASN A 542 AG 4 5 N VAL A 535 ? N VAL A 549 O TYR A 599 ? O TYR A 613 AG 5 6 N LYS A 606 ? N LYS A 620 O PHE A 609 ? O PHE A 623 AG 6 7 N LEU A 614 ? N LEU A 628 O THR A 617 ? O THR A 631 AH 1 2 N TYR A 487 ? N TYR A 501 O THR A 498 ? O THR A 512 AH 2 3 N GLN A 501 ? N GLN A 515 O ALA A 643 ? O ALA A 657 AH 3 4 N VAL A 650 ? N VAL A 664 O TYR A 460 ? O TYR A 474 AI 1 2 N GLN A 480 ? N GLN A 494 O ILE A 518 ? O ILE A 532 AI 2 3 N ILE A 521 ? N ILE A 535 O ALA A 633 ? O ALA A 647 AI 3 4 N GLY A 636 ? N GLY A 650 O PHE A 546 ? O PHE A 560 AI 4 5 N GLY A 549 ? N GLY A 563 O VAL A 564 ? O VAL A 578 AI 5 6 N PHE A 569 ? N PHE A 583 O SER A 573 ? O SER A 587 AI 6 7 O VAL A 576 ? O VAL A 590 N TYR A 586 ? N TYR A 600 # 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 ? ? ? ? 14 'BINDING SITE FOR RESIDUE 147 A 1001' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 1669' AC3 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG A1284 through NAG A1285 bound to ASN A 284' AC4 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG A1363 through NAG A1364 bound to ASN A 363' AC5 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A1387 bound to ASN A 387' AC6 Software ? ? ? ? 5 'Binding site for Poly-Saccharide residues NAG A1542 through NAG A1543 bound to ASN A 542' # 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 14 GLY A 34 ? GLY A 48 . ? 1_555 ? 2 AC1 14 THR A 78 ? THR A 92 . ? 1_555 ? 3 AC1 14 THR A 79 ? THR A 93 . ? 1_555 ? 4 AC1 14 TRP A 121 ? TRP A 135 . ? 1_555 ? 5 AC1 14 ASN A 167 ? ASN A 181 . ? 1_555 ? 6 AC1 14 GLU A 168 ? GLU A 182 . ? 1_555 ? 7 AC1 14 GLU A 244 ? GLU A 258 . ? 1_555 ? 8 AC1 14 SER A 247 ? SER A 261 . ? 1_555 ? 9 AC1 14 TYR A 289 ? TYR A 303 . ? 1_555 ? 10 AC1 14 ARG A 366 ? ARG A 380 . ? 1_555 ? 11 AC1 14 ARG A 575 ? ARG A 589 . ? 17_555 ? 12 AC1 14 THR A 585 ? THR A 599 . ? 17_555 ? 13 AC1 14 HOH K . ? HOH A 2270 . ? 1_555 ? 14 AC1 14 HOH K . ? HOH A 2271 . ? 1_555 ? 15 AC2 5 ASP A 463 ? ASP A 477 . ? 1_555 ? 16 AC2 5 ASN A 465 ? ASN A 479 . ? 1_555 ? 17 AC2 5 PHE A 497 ? PHE A 511 . ? 1_555 ? 18 AC2 5 ASP A 646 ? ASP A 660 . ? 1_555 ? 19 AC2 5 HOH K . ? HOH A 2209 . ? 1_555 ? 20 AC3 3 ILE A 267 ? ILE A 281 . ? 1_555 ? 21 AC3 3 ASN A 270 ? ASN A 284 . ? 1_555 ? 22 AC3 3 HOH K . ? HOH A 2272 . ? 1_555 ? 23 AC4 3 ASP A 345 ? ASP A 359 . ? 1_555 ? 24 AC4 3 LEU A 347 ? LEU A 361 . ? 1_555 ? 25 AC4 3 ASN A 349 ? ASN A 363 . ? 1_555 ? 26 AC5 3 LYS A 336 ? LYS A 350 . ? 1_555 ? 27 AC5 3 TYR A 371 ? TYR A 385 . ? 1_555 ? 28 AC5 3 ASN A 373 ? ASN A 387 . ? 1_555 ? 29 AC6 5 ASN A 528 ? ASN A 542 . ? 1_555 ? 30 AC6 5 LYS A 606 ? LYS A 620 . ? 1_555 ? 31 AC6 5 GLY A 607 ? GLY A 621 . ? 1_555 ? 32 AC6 5 ALA A 653 ? ALA A 667 . ? 1_555 ? 33 AC6 5 ARG A 654 ? ARG A 668 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CCC _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 4CCC _atom_sites.fract_transf_matrix[1][1] 0.004000 _atom_sites.fract_transf_matrix[1][2] 0.002309 _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] 0.004619 _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] 0.012855 _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 CA N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . GLY A 1 11 ? 91.821 108.423 -12.021 1.00 70.77 ? 25 GLY A N 1 ATOM 2 C CA . GLY A 1 11 ? 92.691 109.542 -12.347 1.00 75.01 ? 25 GLY A CA 1 ATOM 3 C C . GLY A 1 11 ? 92.300 110.798 -11.593 1.00 79.33 ? 25 GLY A C 1 ATOM 4 O O . GLY A 1 11 ? 92.906 111.132 -10.571 1.00 81.11 ? 25 GLY A O 1 ATOM 5 N N . ALA A 1 12 ? 91.287 111.499 -12.099 1.00 80.14 ? 26 ALA A N 1 ATOM 6 C CA . ALA A 1 12 ? 90.759 112.691 -11.433 1.00 78.69 ? 26 ALA A CA 1 ATOM 7 C C . ALA A 1 12 ? 89.507 112.345 -10.631 1.00 79.19 ? 26 ALA A C 1 ATOM 8 O O . ALA A 1 12 ? 88.645 111.604 -11.111 1.00 81.37 ? 26 ALA A O 1 ATOM 9 C CB . ALA A 1 12 ? 90.447 113.778 -12.451 1.00 78.49 ? 26 ALA A CB 1 ATOM 10 N N . TYR A 1 13 ? 89.413 112.881 -9.413 1.00 77.66 ? 27 TYR A N 1 ATOM 11 C CA . TYR A 1 13 ? 88.245 112.682 -8.551 1.00 74.66 ? 27 TYR A CA 1 ATOM 12 C C . TYR A 1 13 ? 87.667 114.031 -8.099 1.00 76.73 ? 27 TYR A C 1 ATOM 13 O O . TYR A 1 13 ? 88.298 114.752 -7.322 1.00 79.26 ? 27 TYR A O 1 ATOM 14 C CB . TYR A 1 13 ? 88.610 111.846 -7.315 1.00 69.82 ? 27 TYR A CB 1 ATOM 15 C CG . TYR A 1 13 ? 89.355 110.549 -7.588 1.00 68.67 ? 27 TYR A CG 1 ATOM 16 C CD1 . TYR A 1 13 ? 88.671 109.378 -7.918 1.00 66.66 ? 27 TYR A CD1 1 ATOM 17 C CD2 . TYR A 1 13 ? 90.742 110.488 -7.481 1.00 69.28 ? 27 TYR A CD2 1 ATOM 18 C CE1 . TYR A 1 13 ? 89.358 108.187 -8.152 1.00 66.73 ? 27 TYR A CE1 1 ATOM 19 C CE2 . TYR A 1 13 ? 91.438 109.312 -7.719 1.00 69.42 ? 27 TYR A CE2 1 ATOM 20 C CZ . TYR A 1 13 ? 90.747 108.163 -8.052 1.00 69.63 ? 27 TYR A CZ 1 ATOM 21 O OH . TYR A 1 13 ? 91.454 106.995 -8.276 1.00 70.46 ? 27 TYR A OH 1 ATOM 22 N N . VAL A 1 14 ? 86.471 114.370 -8.574 1.00 75.60 ? 28 VAL A N 1 ATOM 23 C CA . VAL A 1 14 ? 85.853 115.654 -8.234 1.00 76.10 ? 28 VAL A CA 1 ATOM 24 C C . VAL A 1 14 ? 85.172 115.604 -6.869 1.00 77.31 ? 28 VAL A C 1 ATOM 25 O O . VAL A 1 14 ? 84.426 114.673 -6.582 1.00 74.09 ? 28 VAL A O 1 ATOM 26 C CB . VAL A 1 14 ? 84.812 116.078 -9.289 1.00 77.08 ? 28 VAL A CB 1 ATOM 27 C CG1 . VAL A 1 14 ? 84.098 117.362 -8.862 1.00 76.75 ? 28 VAL A CG1 1 ATOM 28 C CG2 . VAL A 1 14 ? 85.478 116.253 -10.654 1.00 80.22 ? 28 VAL A CG2 1 ATOM 29 N N . LEU A 1 15 ? 85.440 116.599 -6.027 1.00 78.90 ? 29 LEU A N 1 ATOM 30 C CA . LEU A 1 15 ? 84.687 116.760 -4.786 1.00 77.80 ? 29 LEU A CA 1 ATOM 31 C C . LEU A 1 15 ? 83.878 118.052 -4.878 1.00 80.88 ? 29 LEU A C 1 ATOM 32 O O . LEU A 1 15 ? 84.448 119.150 -4.949 1.00 80.22 ? 29 LEU A O 1 ATOM 33 C CB . LEU A 1 15 ? 85.620 116.771 -3.575 1.00 74.74 ? 29 LEU A CB 1 ATOM 34 C CG . LEU A 1 15 ? 86.587 115.586 -3.518 1.00 72.99 ? 29 LEU A CG 1 ATOM 35 C CD1 . LEU A 1 15 ? 87.694 115.850 -2.519 1.00 72.09 ? 29 LEU A CD1 1 ATOM 36 C CD2 . LEU A 1 15 ? 85.868 114.276 -3.198 1.00 71.10 ? 29 LEU A CD2 1 ATOM 37 N N . ASP A 1 16 ? 82.554 117.913 -4.903 1.00 82.43 ? 30 ASP A N 1 ATOM 38 C CA . ASP A 1 16 ? 81.671 119.044 -5.163 1.00 86.71 ? 30 ASP A CA 1 ATOM 39 C C . ASP A 1 16 ? 80.369 118.981 -4.358 1.00 88.19 ? 30 ASP A C 1 ATOM 40 O O . ASP A 1 16 ? 79.811 117.902 -4.123 1.00 84.90 ? 30 ASP A O 1 ATOM 41 C CB . ASP A 1 16 ? 81.374 119.133 -6.665 1.00 92.31 ? 30 ASP A CB 1 ATOM 42 C CG . ASP A 1 16 ? 80.440 120.278 -7.014 1.00 97.84 ? 30 ASP A CG 1 ATOM 43 O OD1 . ASP A 1 16 ? 80.332 121.233 -6.214 1.00 99.91 ? 30 ASP A OD1 1 ATOM 44 O OD2 . ASP A 1 16 ? 79.816 120.227 -8.096 1.00 99.39 ? 30 ASP A OD2 1 ATOM 45 N N . ASP A 1 17 ? 79.891 120.154 -3.948 1.00 90.76 ? 31 ASP A N 1 ATOM 46 C CA . ASP A 1 17 ? 78.641 120.282 -3.200 1.00 89.82 ? 31 ASP A CA 1 ATOM 47 C C . ASP A 1 17 ? 77.573 121.024 -4.015 1.00 88.46 ? 31 ASP A C 1 ATOM 48 O O . ASP A 1 17 ? 76.499 121.354 -3.498 1.00 86.70 ? 31 ASP A O 1 ATOM 49 C CB . ASP A 1 17 ? 78.890 121.015 -1.869 1.00 91.26 ? 31 ASP A CB 1 ATOM 50 C CG . ASP A 1 17 ? 79.641 122.339 -2.053 1.00 94.04 ? 31 ASP A CG 1 ATOM 51 O OD1 . ASP A 1 17 ? 79.880 122.731 -3.217 1.00 94.71 ? 31 ASP A OD1 1 ATOM 52 O OD2 . ASP A 1 17 ? 79.984 122.995 -1.040 1.00 93.74 ? 31 ASP A OD2 1 ATOM 53 N N . SER A 1 18 ? 77.874 121.280 -5.287 1.00 88.71 ? 32 SER A N 1 ATOM 54 C CA . SER A 1 18 ? 77.023 122.121 -6.126 1.00 89.43 ? 32 SER A CA 1 ATOM 55 C C . SER A 1 18 ? 75.698 121.462 -6.482 1.00 90.62 ? 32 SER A C 1 ATOM 56 O O . SER A 1 18 ? 74.658 122.126 -6.512 1.00 88.74 ? 32 SER A O 1 ATOM 57 C CB . SER A 1 18 ? 77.757 122.539 -7.400 1.00 89.62 ? 32 SER A CB 1 ATOM 58 O OG . SER A 1 18 ? 77.093 123.622 -8.020 1.00 89.62 ? 32 SER A OG 1 ATOM 59 N N . ASP A 1 19 ? 75.733 120.160 -6.755 1.00 93.89 ? 33 ASP A N 1 ATOM 60 C CA . ASP A 1 19 ? 74.511 119.423 -7.055 1.00 96.07 ? 33 ASP A CA 1 ATOM 61 C C . ASP A 1 19 ? 73.893 118.862 -5.776 1.00 94.46 ? 33 ASP A C 1 ATOM 62 O O . ASP A 1 19 ? 73.137 117.885 -5.805 1.00 95.15 ? 33 ASP A O 1 ATOM 63 C CB . ASP A 1 19 ? 74.777 118.305 -8.069 1.00 99.76 ? 33 ASP A CB 1 ATOM 64 C CG . ASP A 1 19 ? 73.500 117.793 -8.727 1.00 102.69 ? 33 ASP A CG 1 ATOM 65 O OD1 . ASP A 1 19 ? 72.540 118.583 -8.878 1.00 103.86 ? 33 ASP A OD1 1 ATOM 66 O OD2 . ASP A 1 19 ? 73.456 116.598 -9.089 1.00 103.04 ? 33 ASP A OD2 1 ATOM 67 N N . GLY A 1 20 ? 74.214 119.487 -4.649 1.00 90.55 ? 34 GLY A N 1 ATOM 68 C CA . GLY A 1 20 ? 73.619 119.095 -3.386 1.00 86.05 ? 34 GLY A CA 1 ATOM 69 C C . GLY A 1 20 ? 74.509 118.212 -2.534 1.00 81.91 ? 34 GLY A C 1 ATOM 70 O O . GLY A 1 20 ? 75.712 118.077 -2.781 1.00 81.22 ? 34 GLY A O 1 ATOM 71 N N . LEU A 1 21 ? 73.909 117.600 -1.521 1.00 79.28 ? 35 LEU A N 1 ATOM 72 C CA . LEU A 1 21 ? 74.676 116.852 -0.543 1.00 75.72 ? 35 LEU A CA 1 ATOM 73 C C . LEU A 1 21 ? 74.195 115.420 -0.415 1.00 73.91 ? 35 LEU A C 1 ATOM 74 O O . LEU A 1 21 ? 73.074 115.091 -0.810 1.00 73.68 ? 35 LEU A O 1 ATOM 75 C CB . LEU A 1 21 ? 74.615 117.556 0.812 1.00 74.18 ? 35 LEU A CB 1 ATOM 76 C CG . LEU A 1 21 ? 75.387 118.876 0.840 1.00 73.70 ? 35 LEU A CG 1 ATOM 77 C CD1 . LEU A 1 21 ? 75.020 119.675 2.076 1.00 72.88 ? 35 LEU A CD1 1 ATOM 78 C CD2 . LEU A 1 21 ? 76.893 118.637 0.772 1.00 71.28 ? 35 LEU A CD2 1 ATOM 79 N N . GLY A 1 22 ? 75.058 114.568 0.130 1.00 72.76 ? 36 GLY A N 1 ATOM 80 C CA . GLY A 1 22 ? 74.707 113.183 0.381 1.00 70.30 ? 36 GLY A CA 1 ATOM 81 C C . GLY A 1 22 ? 73.919 113.063 1.673 1.00 67.45 ? 36 GLY A C 1 ATOM 82 O O . GLY A 1 22 ? 73.183 113.980 2.053 1.00 66.88 ? 36 GLY A O 1 ATOM 83 N N . ARG A 1 23 ? 74.064 111.931 2.353 1.00 63.94 ? 37 ARG A N 1 ATOM 84 C CA . ARG A 1 23 ? 73.326 111.714 3.594 1.00 63.84 ? 37 ARG A CA 1 ATOM 85 C C . ARG A 1 23 ? 73.978 112.366 4.807 1.00 56.28 ? 37 ARG A C 1 ATOM 86 O O . ARG A 1 23 ? 75.195 112.565 4.841 1.00 56.61 ? 37 ARG A O 1 ATOM 87 C CB . ARG A 1 23 ? 73.128 110.221 3.852 1.00 55.36 ? 37 ARG A CB 1 ATOM 88 C CG . ARG A 1 23 ? 72.038 109.628 3.004 1.00 55.18 ? 37 ARG A CG 1 ATOM 89 C CD . ARG A 1 23 ? 71.596 108.279 3.508 1.00 54.27 ? 37 ARG A CD 1 ATOM 90 N NE . ARG A 1 23 ? 70.463 107.798 2.731 1.00 65.22 ? 37 ARG A NE 1 ATOM 91 C CZ . ARG A 1 23 ? 69.699 106.771 3.076 1.00 66.66 ? 37 ARG A CZ 1 ATOM 92 N NH1 . ARG A 1 23 ? 69.938 106.105 4.204 1.00 71.08 ? 37 ARG A NH1 1 ATOM 93 N NH2 . ARG A 1 23 ? 68.686 106.416 2.302 1.00 65.47 ? 37 ARG A NH2 1 ATOM 94 N N . GLU A 1 24 ? 73.156 112.696 5.799 1.00 56.55 ? 38 GLU A N 1 ATOM 95 C CA . GLU A 1 24 ? 73.649 113.205 7.077 1.00 59.08 ? 38 GLU A CA 1 ATOM 96 C C . GLU A 1 24 ? 74.449 112.132 7.818 1.00 55.32 ? 38 GLU A C 1 ATOM 97 O O . GLU A 1 24 ? 74.003 110.990 7.926 1.00 54.61 ? 38 GLU A O 1 ATOM 98 C CB . GLU A 1 24 ? 72.471 113.663 7.939 1.00 62.97 ? 38 GLU A CB 1 ATOM 99 C CG . GLU A 1 24 ? 72.871 114.146 9.325 1.00 68.22 ? 38 GLU A CG 1 ATOM 100 C CD . GLU A 1 24 ? 71.696 114.657 10.132 1.00 71.23 ? 38 GLU A CD 1 ATOM 101 O OE1 . GLU A 1 24 ? 70.546 114.259 9.839 1.00 73.60 ? 38 GLU A OE1 1 ATOM 102 O OE2 . GLU A 1 24 ? 71.927 115.459 11.062 1.00 71.11 ? 38 GLU A OE2 1 ATOM 103 N N . PHE A 1 25 ? 75.628 112.504 8.314 1.00 55.64 ? 39 PHE A N 1 ATOM 104 C CA . PHE A 1 25 ? 76.484 111.620 9.095 1.00 55.18 ? 39 PHE A CA 1 ATOM 105 C C . PHE A 1 25 ? 75.984 111.620 10.541 1.00 59.93 ? 39 PHE A C 1 ATOM 106 O O . PHE A 1 25 ? 75.715 112.685 11.107 1.00 59.21 ? 39 PHE A O 1 ATOM 107 C CB . PHE A 1 25 ? 77.919 112.118 9.026 1.00 55.80 ? 39 PHE A CB 1 ATOM 108 C CG . PHE A 1 25 ? 78.882 111.403 9.943 1.00 65.71 ? 39 PHE A CG 1 ATOM 109 C CD1 . PHE A 1 25 ? 79.333 110.126 9.642 1.00 64.28 ? 39 PHE A CD1 1 ATOM 110 C CD2 . PHE A 1 25 ? 79.385 112.038 11.075 1.00 65.86 ? 39 PHE A CD2 1 ATOM 111 C CE1 . PHE A 1 25 ? 80.240 109.476 10.465 1.00 54.85 ? 39 PHE A CE1 1 ATOM 112 C CE2 . PHE A 1 25 ? 80.288 111.389 11.913 1.00 65.10 ? 39 PHE A CE2 1 ATOM 113 C CZ . PHE A 1 25 ? 80.718 110.105 11.603 1.00 63.15 ? 39 PHE A CZ 1 ATOM 114 N N . ASP A 1 26 ? 75.843 110.428 11.121 1.00 57.62 ? 40 ASP A N 1 ATOM 115 C CA . ASP A 1 26 ? 75.262 110.284 12.450 1.00 53.42 ? 40 ASP A CA 1 ATOM 116 C C . ASP A 1 26 ? 76.266 109.956 13.558 1.00 55.19 ? 40 ASP A C 1 ATOM 117 O O . ASP A 1 26 ? 75.931 110.052 14.745 1.00 57.70 ? 40 ASP A O 1 ATOM 118 C CB . ASP A 1 26 ? 74.151 109.227 12.428 1.00 52.62 ? 40 ASP A CB 1 ATOM 119 C CG . ASP A 1 26 ? 72.993 109.617 11.534 1.00 61.81 ? 40 ASP A CG 1 ATOM 120 O OD1 . ASP A 1 26 ? 72.523 110.765 11.630 1.00 62.62 ? 40 ASP A OD1 1 ATOM 121 O OD2 . ASP A 1 26 ? 72.544 108.771 10.732 1.00 62.51 ? 40 ASP A OD2 1 ATOM 122 N N . GLY A 1 27 ? 77.477 109.547 13.190 1.00 45.74 ? 41 GLY A N 1 ATOM 123 C CA . GLY A 1 27 ? 78.525 109.307 14.174 1.00 45.89 ? 41 GLY A CA 1 ATOM 124 C C . GLY A 1 27 ? 79.153 107.919 14.153 1.00 45.42 ? 41 GLY A C 1 ATOM 125 O O . GLY A 1 27 ? 78.548 106.946 13.680 1.00 46.24 ? 41 GLY A O 1 ATOM 126 N N . ILE A 1 28 ? 80.384 107.836 14.650 1.00 46.00 ? 42 ILE A N 1 ATOM 127 C CA . ILE A 1 28 ? 81.034 106.557 14.901 1.00 45.58 ? 42 ILE A CA 1 ATOM 128 C C . ILE A 1 28 ? 80.987 106.263 16.402 1.00 52.26 ? 42 ILE A C 1 ATOM 129 O O . ILE A 1 28 ? 81.179 107.171 17.230 1.00 54.15 ? 42 ILE A O 1 ATOM 130 C CB . ILE A 1 28 ? 82.512 106.574 14.477 1.00 47.33 ? 42 ILE A CB 1 ATOM 131 C CG1 . ILE A 1 28 ? 82.665 106.965 12.995 1.00 48.33 ? 42 ILE A CG1 1 ATOM 132 C CG2 . ILE A 1 28 ? 83.174 105.223 14.762 1.00 46.31 ? 42 ILE A CG2 1 ATOM 133 C CD1 . ILE A 1 28 ? 81.696 106.242 12.052 1.00 48.96 ? 42 ILE A CD1 1 ATOM 134 N N . GLY A 1 29 ? 80.769 105.000 16.760 1.00 48.02 ? 43 GLY A N 1 ATOM 135 C CA . GLY A 1 29 ? 80.771 104.611 18.158 1.00 51.00 ? 43 GLY A CA 1 ATOM 136 C C . GLY A 1 29 ? 81.231 103.187 18.414 1.00 50.80 ? 43 GLY A C 1 ATOM 137 O O . GLY A 1 29 ? 81.809 102.536 17.532 1.00 48.83 ? 43 GLY A O 1 ATOM 138 N N . ALA A 1 30 ? 80.978 102.707 19.631 1.00 47.48 ? 44 ALA A N 1 ATOM 139 C CA . ALA A 1 30 ? 81.368 101.356 20.027 1.00 42.70 ? 44 ALA A CA 1 ATOM 140 C C . ALA A 1 30 ? 80.420 100.795 21.090 1.00 42.02 ? 44 ALA A C 1 ATOM 141 O O . ALA A 1 30 ? 79.677 101.542 21.740 1.00 40.12 ? 44 ALA A O 1 ATOM 142 C CB . ALA A 1 30 ? 82.810 101.335 20.529 1.00 42.90 ? 44 ALA A CB 1 ATOM 143 N N . VAL A 1 31 ? 80.454 99.478 21.270 1.00 39.73 ? 45 VAL A N 1 ATOM 144 C CA . VAL A 1 31 ? 79.550 98.825 22.205 1.00 45.74 ? 45 VAL A CA 1 ATOM 145 C C . VAL A 1 31 ? 80.248 98.377 23.487 1.00 45.74 ? 45 VAL A C 1 ATOM 146 O O . VAL A 1 31 ? 81.273 97.684 23.460 1.00 39.09 ? 45 VAL A O 1 ATOM 147 C CB . VAL A 1 31 ? 78.910 97.591 21.581 1.00 44.65 ? 45 VAL A CB 1 ATOM 148 C CG1 . VAL A 1 31 ? 78.061 96.850 22.615 1.00 36.64 ? 45 VAL A CG1 1 ATOM 149 C CG2 . VAL A 1 31 ? 78.087 97.968 20.332 1.00 37.62 ? 45 VAL A CG2 1 ATOM 150 N N . SER A 1 32 ? 79.687 98.765 24.619 1.00 38.30 ? 46 SER A N 1 ATOM 151 C CA . SER A 1 32 ? 80.118 98.166 25.861 1.00 39.81 ? 46 SER A CA 1 ATOM 152 C C . SER A 1 32 ? 79.012 97.245 26.318 1.00 38.93 ? 46 SER A C 1 ATOM 153 O O . SER A 1 32 ? 77.933 97.704 26.708 1.00 36.59 ? 46 SER A O 1 ATOM 154 C CB . SER A 1 32 ? 80.371 99.219 26.917 1.00 40.65 ? 46 SER A CB 1 ATOM 155 O OG . SER A 1 32 ? 80.400 98.606 28.199 1.00 42.02 ? 46 SER A OG 1 ATOM 156 N N . GLY A 1 33 ? 79.271 95.945 26.261 1.00 37.68 ? 47 GLY A N 1 ATOM 157 C CA . GLY A 1 33 ? 78.251 94.982 26.606 1.00 35.75 ? 47 GLY A CA 1 ATOM 158 C C . GLY A 1 33 ? 78.198 93.880 25.572 1.00 37.41 ? 47 GLY A C 1 ATOM 159 O O . GLY A 1 33 ? 78.951 93.885 24.582 1.00 38.60 ? 47 GLY A O 1 ATOM 160 N N . GLY A 1 34 ? 77.300 92.932 25.802 1.00 38.09 ? 48 GLY A N 1 ATOM 161 C CA . GLY A 1 34 ? 77.221 91.743 24.976 1.00 37.48 ? 48 GLY A CA 1 ATOM 162 C C . GLY A 1 34 ? 78.546 91.000 24.846 1.00 41.86 ? 48 GLY A C 1 ATOM 163 O O . GLY A 1 34 ? 78.985 90.769 23.719 1.00 36.00 ? 48 GLY A O 1 ATOM 164 N N . GLY A 1 35 ? 79.170 90.579 25.954 1.00 43.68 ? 49 GLY A N 1 ATOM 165 C CA . GLY A 1 35 ? 78.641 90.697 27.307 1.00 44.21 ? 49 GLY A CA 1 ATOM 166 C C . GLY A 1 35 ? 79.775 90.823 28.317 1.00 42.13 ? 49 GLY A C 1 ATOM 167 O O . GLY A 1 35 ? 80.762 90.090 28.233 1.00 41.48 ? 49 GLY A O 1 ATOM 168 N N . ALA A 1 36 ? 79.644 91.760 29.254 1.00 39.20 ? 50 ALA A N 1 ATOM 169 C CA . ALA A 1 36 ? 80.661 91.988 30.287 1.00 40.36 ? 50 ALA A CA 1 ATOM 170 C C . ALA A 1 36 ? 82.017 92.336 29.692 1.00 41.73 ? 50 ALA A C 1 ATOM 171 O O . ALA A 1 36 ? 83.055 91.934 30.220 1.00 40.87 ? 50 ALA A O 1 ATOM 172 C CB . ALA A 1 36 ? 80.775 90.757 31.207 1.00 39.16 ? 50 ALA A CB 1 ATOM 173 N N . THR A 1 37 ? 82.008 93.082 28.590 1.00 42.05 ? 51 THR A N 1 ATOM 174 C CA . THR A 1 37 ? 83.243 93.378 27.883 1.00 38.99 ? 51 THR A CA 1 ATOM 175 C C . THR A 1 37 ? 84.097 94.401 28.631 1.00 43.82 ? 51 THR A C 1 ATOM 176 O O . THR A 1 37 ? 85.304 94.465 28.427 1.00 40.97 ? 51 THR A O 1 ATOM 177 C CB . THR A 1 37 ? 82.999 93.851 26.423 1.00 38.92 ? 51 THR A CB 1 ATOM 178 O OG1 . THR A 1 37 ? 82.242 95.069 26.422 1.00 41.24 ? 51 THR A OG1 1 ATOM 179 C CG2 . THR A 1 37 ? 82.253 92.790 25.623 1.00 38.03 ? 51 THR A CG2 1 ATOM 180 N N . SER A 1 38 ? 83.467 95.192 29.496 1.00 39.80 ? 52 SER A N 1 ATOM 181 C CA . SER A 1 38 ? 84.163 96.212 30.279 1.00 42.35 ? 52 SER A CA 1 ATOM 182 C C . SER A 1 38 ? 84.392 95.777 31.722 1.00 44.81 ? 52 SER A C 1 ATOM 183 O O . SER A 1 38 ? 84.657 96.619 32.600 1.00 42.52 ? 52 SER A O 1 ATOM 184 C CB . SER A 1 38 ? 83.367 97.523 30.271 1.00 42.49 ? 52 SER A CB 1 ATOM 185 O OG . SER A 1 38 ? 83.155 97.987 28.950 1.00 45.26 ? 52 SER A OG 1 ATOM 186 N N . ARG A 1 39 ? 84.302 94.468 31.960 1.00 42.33 ? 53 ARG A N 1 ATOM 187 C CA . ARG A 1 39 ? 84.323 93.912 33.315 1.00 44.91 ? 53 ARG A CA 1 ATOM 188 C C . ARG A 1 39 ? 85.572 94.272 34.145 1.00 45.45 ? 53 ARG A C 1 ATOM 189 O O . ARG A 1 39 ? 85.465 94.532 35.348 1.00 43.63 ? 53 ARG A O 1 ATOM 190 C CB . ARG A 1 39 ? 84.161 92.394 33.249 1.00 39.79 ? 53 ARG A CB 1 ATOM 191 C CG . ARG A 1 39 ? 84.161 91.709 34.597 1.00 46.79 ? 53 ARG A CG 1 ATOM 192 C CD . ARG A 1 39 ? 82.910 92.064 35.414 1.00 47.23 ? 53 ARG A CD 1 ATOM 193 N NE . ARG A 1 39 ? 82.966 91.568 36.790 1.00 45.98 ? 53 ARG A NE 1 ATOM 194 C CZ . ARG A 1 39 ? 83.457 92.256 37.822 1.00 44.47 ? 53 ARG A CZ 1 ATOM 195 N NH1 . ARG A 1 39 ? 83.937 93.479 37.646 1.00 46.83 ? 53 ARG A NH1 1 ATOM 196 N NH2 . ARG A 1 39 ? 83.469 91.724 39.040 1.00 41.03 ? 53 ARG A NH2 1 ATOM 197 N N . LEU A 1 40 ? 86.742 94.287 33.505 1.00 45.64 ? 54 LEU A N 1 ATOM 198 C CA . LEU A 1 40 ? 88.008 94.443 34.228 1.00 46.00 ? 54 LEU A CA 1 ATOM 199 C C . LEU A 1 40 ? 88.508 95.886 34.212 1.00 44.52 ? 54 LEU A C 1 ATOM 200 O O . LEU A 1 40 ? 89.567 96.197 34.753 1.00 53.01 ? 54 LEU A O 1 ATOM 201 C CB . LEU A 1 40 ? 89.072 93.500 33.654 1.00 46.51 ? 54 LEU A CB 1 ATOM 202 C CG . LEU A 1 40 ? 88.780 91.996 33.687 1.00 43.57 ? 54 LEU A CG 1 ATOM 203 C CD1 . LEU A 1 40 ? 89.789 91.232 32.841 1.00 44.16 ? 54 LEU A CD1 1 ATOM 204 C CD2 . LEU A 1 40 ? 88.817 91.486 35.116 1.00 43.66 ? 54 LEU A CD2 1 ATOM 205 N N . LEU A 1 41 ? 87.737 96.773 33.598 1.00 49.44 ? 55 LEU A N 1 ATOM 206 C CA . LEU A 1 41 ? 88.138 98.172 33.519 1.00 48.72 ? 55 LEU A CA 1 ATOM 207 C C . LEU A 1 41 ? 87.906 98.872 34.838 1.00 47.01 ? 55 LEU A C 1 ATOM 208 O O . LEU A 1 41 ? 88.678 99.747 35.218 1.00 50.74 ? 55 LEU A O 1 ATOM 209 C CB . LEU A 1 41 ? 87.360 98.898 32.424 1.00 48.01 ? 55 LEU A CB 1 ATOM 210 C CG . LEU A 1 41 ? 87.689 100.384 32.285 1.00 50.48 ? 55 LEU A CG 1 ATOM 211 C CD1 . LEU A 1 41 ? 89.176 100.572 31.948 1.00 51.15 ? 55 LEU A CD1 1 ATOM 212 C CD2 . LEU A 1 41 ? 86.813 101.065 31.243 1.00 46.79 ? 55 LEU A CD2 1 ATOM 213 N N . VAL A 1 42 ? 86.846 98.477 35.536 1.00 45.67 ? 56 VAL A N 1 ATOM 214 C CA . VAL A 1 42 ? 86.343 99.238 36.685 1.00 46.76 ? 56 VAL A CA 1 ATOM 215 C C . VAL A 1 42 ? 87.280 99.318 37.882 1.00 50.60 ? 56 VAL A C 1 ATOM 216 O O . VAL A 1 42 ? 87.249 100.308 38.631 1.00 45.87 ? 56 VAL A O 1 ATOM 217 C CB . VAL A 1 42 ? 84.947 98.733 37.173 1.00 43.12 ? 56 VAL A CB 1 ATOM 218 C CG1 . VAL A 1 42 ? 83.938 98.850 36.064 1.00 43.84 ? 56 VAL A CG1 1 ATOM 219 C CG2 . VAL A 1 42 ? 85.015 97.297 37.709 1.00 42.71 ? 56 VAL A CG2 1 ATOM 220 N N . ASN A 1 43 ? 88.102 98.287 38.067 1.00 51.09 ? 57 ASN A N 1 ATOM 221 C CA . ASN A 1 43 ? 89.049 98.275 39.181 1.00 51.71 ? 57 ASN A CA 1 ATOM 222 C C . ASN A 1 43 ? 90.487 98.641 38.781 1.00 54.33 ? 57 ASN A C 1 ATOM 223 O O . ASN A 1 43 ? 91.428 98.358 39.524 1.00 54.07 ? 57 ASN A O 1 ATOM 224 C CB . ASN A 1 43 ? 89.023 96.934 39.920 1.00 50.02 ? 57 ASN A CB 1 ATOM 225 C CG . ASN A 1 43 ? 89.250 95.748 38.992 1.00 50.77 ? 57 ASN A CG 1 ATOM 226 O OD1 . ASN A 1 43 ? 88.868 95.777 37.818 1.00 51.59 ? 57 ASN A OD1 1 ATOM 227 N ND2 . ASN A 1 43 ? 89.873 94.695 39.519 1.00 51.88 ? 57 ASN A ND2 1 ATOM 228 N N . TYR A 1 44 ? 90.665 99.263 37.616 1.00 52.68 ? 58 TYR A N 1 ATOM 229 C CA . TYR A 1 44 ? 91.963 99.871 37.316 1.00 53.26 ? 58 TYR A CA 1 ATOM 230 C C . TYR A 1 44 ? 92.249 100.954 38.345 1.00 55.90 ? 58 TYR A C 1 ATOM 231 O O . TYR A 1 44 ? 91.349 101.700 38.736 1.00 55.08 ? 58 TYR A O 1 ATOM 232 C CB . TYR A 1 44 ? 92.005 100.467 35.909 1.00 49.40 ? 58 TYR A CB 1 ATOM 233 C CG . TYR A 1 44 ? 92.591 99.533 34.881 1.00 53.35 ? 58 TYR A CG 1 ATOM 234 C CD1 . TYR A 1 44 ? 91.887 98.417 34.462 1.00 48.29 ? 58 TYR A CD1 1 ATOM 235 C CD2 . TYR A 1 44 ? 93.842 99.772 34.315 1.00 54.43 ? 58 TYR A CD2 1 ATOM 236 C CE1 . TYR A 1 44 ? 92.408 97.548 33.516 1.00 54.43 ? 58 TYR A CE1 1 ATOM 237 C CE2 . TYR A 1 44 ? 94.377 98.903 33.361 1.00 53.50 ? 58 TYR A CE2 1 ATOM 238 C CZ . TYR A 1 44 ? 93.646 97.794 32.967 1.00 54.16 ? 58 TYR A CZ 1 ATOM 239 O OH . TYR A 1 44 ? 94.143 96.908 32.034 1.00 49.46 ? 58 TYR A OH 1 ATOM 240 N N . PRO A 1 45 ? 93.500 101.018 38.819 1.00 59.70 ? 59 PRO A N 1 ATOM 241 C CA . PRO A 1 45 ? 93.924 102.130 39.675 1.00 60.39 ? 59 PRO A CA 1 ATOM 242 C C . PRO A 1 45 ? 94.009 103.415 38.867 1.00 61.24 ? 59 PRO A C 1 ATOM 243 O O . PRO A 1 45 ? 94.233 103.358 37.648 1.00 61.39 ? 59 PRO A O 1 ATOM 244 C CB . PRO A 1 45 ? 95.334 101.715 40.116 1.00 61.88 ? 59 PRO A CB 1 ATOM 245 C CG . PRO A 1 45 ? 95.373 100.231 39.953 1.00 63.47 ? 59 PRO A CG 1 ATOM 246 C CD . PRO A 1 45 ? 94.513 99.951 38.751 1.00 61.99 ? 59 PRO A CD 1 ATOM 247 N N . GLU A 1 46 ? 93.817 104.556 39.523 1.00 63.84 ? 60 GLU A N 1 ATOM 248 C CA . GLU A 1 46 ? 94.145 105.828 38.889 1.00 69.15 ? 60 GLU A CA 1 ATOM 249 C C . GLU A 1 46 ? 95.667 105.936 38.842 1.00 68.24 ? 60 GLU A C 1 ATOM 250 O O . GLU A 1 46 ? 96.352 105.330 39.663 1.00 69.24 ? 60 GLU A O 1 ATOM 251 C CB . GLU A 1 46 ? 93.518 107.012 39.645 1.00 71.67 ? 60 GLU A CB 1 ATOM 252 C CG . GLU A 1 46 ? 91.980 106.988 39.718 1.00 72.41 ? 60 GLU A CG 1 ATOM 253 C CD . GLU A 1 46 ? 91.277 107.196 38.371 1.00 74.75 ? 60 GLU A CD 1 ATOM 254 O OE1 . GLU A 1 46 ? 91.939 107.179 37.306 1.00 73.97 ? 60 GLU A OE1 1 ATOM 255 O OE2 . GLU A 1 46 ? 90.039 107.377 38.380 1.00 76.62 ? 60 GLU A OE2 1 ATOM 256 N N . PRO A 1 47 ? 96.209 106.700 37.884 1.00 67.49 ? 61 PRO A N 1 ATOM 257 C CA . PRO A 1 47 ? 95.515 107.525 36.891 1.00 65.26 ? 61 PRO A CA 1 ATOM 258 C C . PRO A 1 47 ? 95.078 106.706 35.686 1.00 61.34 ? 61 PRO A C 1 ATOM 259 O O . PRO A 1 47 ? 94.407 107.246 34.810 1.00 61.88 ? 61 PRO A O 1 ATOM 260 C CB . PRO A 1 47 ? 96.623 108.487 36.442 1.00 57.30 ? 61 PRO A CB 1 ATOM 261 C CG . PRO A 1 47 ? 97.834 107.627 36.480 1.00 57.90 ? 61 PRO A CG 1 ATOM 262 C CD . PRO A 1 47 ? 97.675 106.802 37.736 1.00 57.56 ? 61 PRO A CD 1 ATOM 263 N N . TYR A 1 48 ? 95.470 105.437 35.640 1.00 58.55 ? 62 TYR A N 1 ATOM 264 C CA . TYR A 1 48 ? 95.370 104.641 34.415 1.00 59.19 ? 62 TYR A CA 1 ATOM 265 C C . TYR A 1 48 ? 93.931 104.502 33.921 1.00 57.76 ? 62 TYR A C 1 ATOM 266 O O . TYR A 1 48 ? 93.670 104.565 32.715 1.00 58.30 ? 62 TYR A O 1 ATOM 267 C CB . TYR A 1 48 ? 95.984 103.256 34.640 1.00 65.56 ? 62 TYR A CB 1 ATOM 268 C CG . TYR A 1 48 ? 97.388 103.269 35.218 1.00 73.53 ? 62 TYR A CG 1 ATOM 269 C CD1 . TYR A 1 48 ? 98.274 104.313 34.945 1.00 79.98 ? 62 TYR A CD1 1 ATOM 270 C CD2 . TYR A 1 48 ? 97.835 102.229 36.024 1.00 75.36 ? 62 TYR A CD2 1 ATOM 271 C CE1 . TYR A 1 48 ? 99.557 104.323 35.473 1.00 82.70 ? 62 TYR A CE1 1 ATOM 272 C CE2 . TYR A 1 48 ? 99.117 102.227 36.549 1.00 79.57 ? 62 TYR A CE2 1 ATOM 273 C CZ . TYR A 1 48 ? 99.974 103.278 36.272 1.00 82.71 ? 62 TYR A CZ 1 ATOM 274 O OH . TYR A 1 48 ? 101.251 103.283 36.791 1.00 85.09 ? 62 TYR A OH 1 ATOM 275 N N . ARG A 1 49 ? 93.004 104.310 34.859 1.00 53.56 ? 63 ARG A N 1 ATOM 276 C CA . ARG A 1 49 ? 91.594 104.168 34.514 1.00 50.94 ? 63 ARG A CA 1 ATOM 277 C C . ARG A 1 49 ? 91.107 105.398 33.761 1.00 52.55 ? 63 ARG A C 1 ATOM 278 O O . ARG A 1 49 ? 90.488 105.279 32.706 1.00 50.69 ? 63 ARG A O 1 ATOM 279 C CB . ARG A 1 49 ? 90.738 103.921 35.764 1.00 49.85 ? 63 ARG A CB 1 ATOM 280 C CG . ARG A 1 49 ? 89.518 103.027 35.472 1.00 54.71 ? 63 ARG A CG 1 ATOM 281 C CD . ARG A 1 49 ? 88.658 102.814 36.710 1.00 56.52 ? 63 ARG A CD 1 ATOM 282 N NE . ARG A 1 49 ? 88.131 104.075 37.225 1.00 57.09 ? 63 ARG A NE 1 ATOM 283 C CZ . ARG A 1 49 ? 87.307 104.170 38.261 1.00 56.11 ? 63 ARG A CZ 1 ATOM 284 N NH1 . ARG A 1 49 ? 86.910 103.072 38.892 1.00 54.69 ? 63 ARG A NH1 1 ATOM 285 N NH2 . ARG A 1 49 ? 86.877 105.360 38.659 1.00 55.86 ? 63 ARG A NH2 1 ATOM 286 N N . SER A 1 50 ? 91.431 106.575 34.288 1.00 57.07 ? 64 SER A N 1 ATOM 287 C CA . SER A 1 50 ? 91.033 107.838 33.675 1.00 59.92 ? 64 SER A CA 1 ATOM 288 C C . SER A 1 50 ? 91.721 108.088 32.320 1.00 60.44 ? 64 SER A C 1 ATOM 289 O O . SER A 1 50 ? 91.121 108.662 31.396 1.00 55.49 ? 64 SER A O 1 ATOM 290 C CB . SER A 1 50 ? 91.297 108.991 34.651 1.00 61.09 ? 64 SER A CB 1 ATOM 291 O OG . SER A 1 50 ? 90.804 110.213 34.134 1.00 61.36 ? 64 SER A OG 1 ATOM 292 N N . GLU A 1 51 ? 92.974 107.650 32.199 1.00 62.63 ? 65 GLU A N 1 ATOM 293 C CA . GLU A 1 51 ? 93.695 107.717 30.922 1.00 60.14 ? 65 GLU A CA 1 ATOM 294 C C . GLU A 1 51 ? 92.988 106.882 29.848 1.00 57.78 ? 65 GLU A C 1 ATOM 295 O O . GLU A 1 51 ? 92.775 107.341 28.718 1.00 57.06 ? 65 GLU A O 1 ATOM 296 C CB . GLU A 1 51 ? 95.127 107.206 31.104 1.00 62.04 ? 65 GLU A CB 1 ATOM 297 C CG . GLU A 1 51 ? 96.029 108.120 31.940 1.00 66.32 ? 65 GLU A CG 1 ATOM 298 C CD . GLU A 1 51 ? 97.374 107.483 32.265 1.00 70.62 ? 65 GLU A CD 1 ATOM 299 O OE1 . GLU A 1 51 ? 97.684 106.408 31.703 1.00 70.40 ? 65 GLU A OE1 1 ATOM 300 O OE2 . GLU A 1 51 ? 98.120 108.059 33.090 1.00 75.16 ? 65 GLU A OE2 1 ATOM 301 N N . ILE A 1 52 ? 92.641 105.646 30.199 1.00 56.42 ? 66 ILE A N 1 ATOM 302 C CA . ILE A 1 52 ? 91.956 104.756 29.260 1.00 55.99 ? 66 ILE A CA 1 ATOM 303 C C . ILE A 1 52 ? 90.668 105.408 28.762 1.00 53.22 ? 66 ILE A C 1 ATOM 304 O O . ILE A 1 52 ? 90.413 105.461 27.562 1.00 49.64 ? 66 ILE A O 1 ATOM 305 C CB . ILE A 1 52 ? 91.634 103.385 29.897 1.00 52.93 ? 66 ILE A CB 1 ATOM 306 C CG1 . ILE A 1 52 ? 92.919 102.581 30.125 1.00 51.32 ? 66 ILE A CG1 1 ATOM 307 C CG2 . ILE A 1 52 ? 90.675 102.588 29.011 1.00 48.49 ? 66 ILE A CG2 1 ATOM 308 C CD1 . ILE A 1 52 ? 92.750 101.435 31.129 1.00 49.86 ? 66 ILE A CD1 1 ATOM 309 N N . LEU A 1 53 ? 89.869 105.914 29.694 1.00 54.49 ? 67 LEU A N 1 ATOM 310 C CA . LEU A 1 53 ? 88.632 106.607 29.349 1.00 55.26 ? 67 LEU A CA 1 ATOM 311 C C . LEU A 1 53 ? 88.844 107.815 28.424 1.00 54.48 ? 67 LEU A C 1 ATOM 312 O O . LEU A 1 53 ? 88.031 108.066 27.529 1.00 49.21 ? 67 LEU A O 1 ATOM 313 C CB . LEU A 1 53 ? 87.915 107.027 30.631 1.00 56.16 ? 67 LEU A CB 1 ATOM 314 C CG . LEU A 1 53 ? 87.330 105.837 31.388 1.00 47.61 ? 67 LEU A CG 1 ATOM 315 C CD1 . LEU A 1 53 ? 86.910 106.214 32.814 1.00 47.62 ? 67 LEU A CD1 1 ATOM 316 C CD2 . LEU A 1 53 ? 86.161 105.290 30.590 1.00 46.36 ? 67 LEU A CD2 1 ATOM 317 N N . ASP A 1 54 ? 89.924 108.562 28.653 1.00 57.52 ? 68 ASP A N 1 ATOM 318 C CA . ASP A 1 54 ? 90.277 109.681 27.785 1.00 59.60 ? 68 ASP A CA 1 ATOM 319 C C . ASP A 1 54 ? 90.614 109.216 26.377 1.00 55.57 ? 68 ASP A C 1 ATOM 320 O O . ASP A 1 54 ? 90.179 109.828 25.402 1.00 53.54 ? 68 ASP A O 1 ATOM 321 C CB . ASP A 1 54 ? 91.458 110.454 28.355 1.00 64.83 ? 68 ASP A CB 1 ATOM 322 C CG . ASP A 1 54 ? 91.077 111.312 29.536 1.00 70.74 ? 68 ASP A CG 1 ATOM 323 O OD1 . ASP A 1 54 ? 89.859 111.512 29.758 1.00 68.31 ? 68 ASP A OD1 1 ATOM 324 O OD2 . ASP A 1 54 ? 92.004 111.797 30.230 1.00 72.72 ? 68 ASP A OD2 1 ATOM 325 N N . TYR A 1 55 ? 91.387 108.137 26.268 1.00 51.86 ? 69 TYR A N 1 ATOM 326 C CA . TYR A 1 55 ? 91.751 107.607 24.951 1.00 58.66 ? 69 TYR A CA 1 ATOM 327 C C . TYR A 1 55 ? 90.490 107.285 24.162 1.00 54.09 ? 69 TYR A C 1 ATOM 328 O O . TYR A 1 55 ? 90.462 107.409 22.940 1.00 51.68 ? 69 TYR A O 1 ATOM 329 C CB . TYR A 1 55 ? 92.631 106.355 25.072 1.00 58.91 ? 69 TYR A CB 1 ATOM 330 C CG . TYR A 1 55 ? 94.119 106.632 25.218 1.00 57.24 ? 69 TYR A CG 1 ATOM 331 C CD1 . TYR A 1 55 ? 94.852 107.170 24.173 1.00 57.59 ? 69 TYR A CD1 1 ATOM 332 C CD2 . TYR A 1 55 ? 94.789 106.325 26.398 1.00 59.33 ? 69 TYR A CD2 1 ATOM 333 C CE1 . TYR A 1 55 ? 96.213 107.418 24.303 1.00 62.35 ? 69 TYR A CE1 1 ATOM 334 C CE2 . TYR A 1 55 ? 96.138 106.559 26.541 1.00 60.48 ? 69 TYR A CE2 1 ATOM 335 C CZ . TYR A 1 55 ? 96.849 107.103 25.485 1.00 62.37 ? 69 TYR A CZ 1 ATOM 336 O OH . TYR A 1 55 ? 98.196 107.342 25.635 1.00 66.39 ? 69 TYR A OH 1 ATOM 337 N N . LEU A 1 56 ? 89.439 106.906 24.885 1.00 52.33 ? 70 LEU A N 1 ATOM 338 C CA . LEU A 1 56 ? 88.175 106.506 24.276 1.00 52.55 ? 70 LEU A CA 1 ATOM 339 C C . LEU A 1 56 ? 87.236 107.686 23.998 1.00 51.66 ? 70 LEU A C 1 ATOM 340 O O . LEU A 1 56 ? 86.661 107.777 22.919 1.00 50.14 ? 70 LEU A O 1 ATOM 341 C CB . LEU A 1 56 ? 87.475 105.480 25.173 1.00 49.66 ? 70 LEU A CB 1 ATOM 342 C CG . LEU A 1 56 ? 88.222 104.160 25.352 1.00 48.20 ? 70 LEU A CG 1 ATOM 343 C CD1 . LEU A 1 56 ? 87.646 103.340 26.509 1.00 47.91 ? 70 LEU A CD1 1 ATOM 344 C CD2 . LEU A 1 56 ? 88.189 103.351 24.062 1.00 46.82 ? 70 LEU A CD2 1 ATOM 345 N N . PHE A 1 57 ? 87.109 108.600 24.958 1.00 50.39 ? 71 PHE A N 1 ATOM 346 C CA . PHE A 1 57 ? 85.992 109.545 24.946 1.00 52.14 ? 71 PHE A CA 1 ATOM 347 C C . PHE A 1 57 ? 86.357 111.030 24.906 1.00 55.32 ? 71 PHE A C 1 ATOM 348 O O . PHE A 1 57 ? 85.543 111.856 24.481 1.00 57.21 ? 71 PHE A O 1 ATOM 349 C CB . PHE A 1 57 ? 85.087 109.281 26.151 1.00 52.84 ? 71 PHE A CB 1 ATOM 350 C CG . PHE A 1 57 ? 84.484 107.902 26.158 1.00 53.67 ? 71 PHE A CG 1 ATOM 351 C CD1 . PHE A 1 57 ? 83.739 107.449 25.068 1.00 49.66 ? 71 PHE A CD1 1 ATOM 352 C CD2 . PHE A 1 57 ? 84.651 107.063 27.251 1.00 54.03 ? 71 PHE A CD2 1 ATOM 353 C CE1 . PHE A 1 57 ? 83.182 106.180 25.068 1.00 44.55 ? 71 PHE A CE1 1 ATOM 354 C CE2 . PHE A 1 57 ? 84.096 105.791 27.262 1.00 55.18 ? 71 PHE A CE2 1 ATOM 355 C CZ . PHE A 1 57 ? 83.361 105.344 26.172 1.00 44.17 ? 71 PHE A CZ 1 ATOM 356 N N . LYS A 1 58 ? 87.548 111.374 25.387 1.00 54.31 ? 72 LYS A N 1 ATOM 357 C CA . LYS A 1 58 ? 88.013 112.750 25.355 1.00 58.93 ? 72 LYS A CA 1 ATOM 358 C C . LYS A 1 58 ? 88.162 113.258 23.916 1.00 57.88 ? 72 LYS A C 1 ATOM 359 O O . LYS A 1 58 ? 88.893 112.667 23.122 1.00 53.95 ? 72 LYS A O 1 ATOM 360 C CB . LYS A 1 58 ? 89.355 112.839 26.064 1.00 62.93 ? 72 LYS A CB 1 ATOM 361 C CG . LYS A 1 58 ? 89.875 114.235 26.267 1.00 65.36 ? 72 LYS A CG 1 ATOM 362 C CD . LYS A 1 58 ? 91.137 114.155 27.100 1.00 69.37 ? 72 LYS A CD 1 ATOM 363 C CE . LYS A 1 58 ? 91.752 115.503 27.319 1.00 72.96 ? 72 LYS A CE 1 ATOM 364 N NZ . LYS A 1 58 ? 92.992 115.345 28.131 1.00 79.17 ? 72 LYS A NZ 1 ATOM 365 N N . PRO A 1 59 ? 87.449 114.351 23.580 1.00 59.73 ? 73 PRO A N 1 ATOM 366 C CA . PRO A 1 59 ? 87.438 115.000 22.258 1.00 60.83 ? 73 PRO A CA 1 ATOM 367 C C . PRO A 1 59 ? 88.815 115.522 21.874 1.00 60.47 ? 73 PRO A C 1 ATOM 368 O O . PRO A 1 59 ? 89.554 115.973 22.754 1.00 58.77 ? 73 PRO A O 1 ATOM 369 C CB . PRO A 1 59 ? 86.499 116.193 22.465 1.00 60.54 ? 73 PRO A CB 1 ATOM 370 C CG . PRO A 1 59 ? 85.630 115.799 23.626 1.00 58.15 ? 73 PRO A CG 1 ATOM 371 C CD . PRO A 1 59 ? 86.540 115.021 24.529 1.00 59.48 ? 73 PRO A CD 1 ATOM 372 N N . ASN A 1 60 ? 89.143 115.470 20.587 1.00 60.16 ? 74 ASN A N 1 ATOM 373 C CA . ASN A 1 60 ? 90.437 115.936 20.095 1.00 63.75 ? 74 ASN A CA 1 ATOM 374 C C . ASN A 1 60 ? 91.598 115.313 20.858 1.00 62.57 ? 74 ASN A C 1 ATOM 375 O O . ASN A 1 60 ? 92.499 116.015 21.315 1.00 58.86 ? 74 ASN A O 1 ATOM 376 C CB . ASN A 1 60 ? 90.516 117.470 20.147 1.00 66.28 ? 74 ASN A CB 1 ATOM 377 C CG . ASN A 1 60 ? 89.390 118.140 19.371 1.00 68.59 ? 74 ASN A CG 1 ATOM 378 O OD1 . ASN A 1 60 ? 89.049 117.726 18.256 1.00 68.40 ? 74 ASN A OD1 1 ATOM 379 N ND2 . ASN A 1 60 ? 88.800 119.172 19.964 1.00 58.30 ? 74 ASN A ND2 1 ATOM 380 N N . PHE A 1 61 ? 91.570 113.990 20.992 1.00 61.89 ? 75 PHE A N 1 ATOM 381 C CA . PHE A 1 61 ? 92.565 113.294 21.799 1.00 60.77 ? 75 PHE A CA 1 ATOM 382 C C . PHE A 1 61 ? 92.837 111.889 21.268 1.00 61.49 ? 75 PHE A C 1 ATOM 383 O O . PHE A 1 61 ? 93.894 111.611 20.698 1.00 59.30 ? 75 PHE A O 1 ATOM 384 C CB . PHE A 1 61 ? 92.087 113.208 23.245 1.00 60.95 ? 75 PHE A CB 1 ATOM 385 C CG . PHE A 1 61 ? 93.186 112.951 24.223 1.00 63.13 ? 75 PHE A CG 1 ATOM 386 C CD1 . PHE A 1 61 ? 93.899 114.011 24.782 1.00 61.99 ? 75 PHE A CD1 1 ATOM 387 C CD2 . PHE A 1 61 ? 93.520 111.653 24.578 1.00 62.59 ? 75 PHE A CD2 1 ATOM 388 C CE1 . PHE A 1 61 ? 94.926 113.782 25.685 1.00 58.82 ? 75 PHE A CE1 1 ATOM 389 C CE2 . PHE A 1 61 ? 94.538 111.411 25.472 1.00 61.15 ? 75 PHE A CE2 1 ATOM 390 C CZ . PHE A 1 61 ? 95.250 112.477 26.029 1.00 60.56 ? 75 PHE A CZ 1 ATOM 391 N N . GLY A 1 62 ? 91.872 110.997 21.456 1.00 61.10 ? 76 GLY A N 1 ATOM 392 C CA . GLY A 1 62 ? 92.048 109.625 21.035 1.00 58.60 ? 76 GLY A CA 1 ATOM 393 C C . GLY A 1 62 ? 90.980 109.206 20.057 1.00 59.02 ? 76 GLY A C 1 ATOM 394 O O . GLY A 1 62 ? 90.752 109.862 19.038 1.00 58.56 ? 76 GLY A O 1 ATOM 395 N N . ALA A 1 63 ? 90.310 108.107 20.377 1.00 56.07 ? 77 ALA A N 1 ATOM 396 C CA . ALA A 1 63 ? 89.234 107.609 19.539 1.00 52.65 ? 77 ALA A CA 1 ATOM 397 C C . ALA A 1 63 ? 88.063 108.592 19.480 1.00 52.29 ? 77 ALA A C 1 ATOM 398 O O . ALA A 1 63 ? 87.231 108.494 18.573 1.00 51.24 ? 77 ALA A O 1 ATOM 399 C CB . ALA A 1 63 ? 88.772 106.248 20.023 1.00 49.83 ? 77 ALA A CB 1 ATOM 400 N N . SER A 1 64 ? 88.006 109.513 20.449 1.00 52.13 ? 78 SER A N 1 ATOM 401 C CA . SER A 1 64 ? 87.033 110.617 20.464 1.00 54.90 ? 78 SER A CA 1 ATOM 402 C C . SER A 1 64 ? 85.649 110.192 19.963 1.00 53.81 ? 78 SER A C 1 ATOM 403 O O . SER A 1 64 ? 85.107 110.806 19.042 1.00 52.57 ? 78 SER A O 1 ATOM 404 C CB . SER A 1 64 ? 87.534 111.786 19.605 1.00 57.08 ? 78 SER A CB 1 ATOM 405 O OG . SER A 1 64 ? 88.935 112.009 19.754 1.00 55.92 ? 78 SER A OG 1 ATOM 406 N N . LEU A 1 65 ? 85.092 109.146 20.565 1.00 49.32 ? 79 LEU A N 1 ATOM 407 C CA . LEU A 1 65 ? 83.891 108.504 20.027 1.00 51.25 ? 79 LEU A CA 1 ATOM 408 C C . LEU A 1 65 ? 82.653 109.396 20.117 1.00 47.00 ? 79 LEU A C 1 ATOM 409 O O . LEU A 1 65 ? 82.479 110.150 21.075 1.00 47.17 ? 79 LEU A O 1 ATOM 410 C CB . LEU A 1 65 ? 83.662 107.148 20.706 1.00 49.57 ? 79 LEU A CB 1 ATOM 411 C CG . LEU A 1 65 ? 84.669 106.063 20.317 1.00 48.44 ? 79 LEU A CG 1 ATOM 412 C CD1 . LEU A 1 65 ? 84.476 104.827 21.177 1.00 46.40 ? 79 LEU A CD1 1 ATOM 413 C CD2 . LEU A 1 65 ? 84.529 105.703 18.846 1.00 51.10 ? 79 LEU A CD2 1 ATOM 414 N N . HIS A 1 66 ? 81.808 109.313 19.100 1.00 46.61 ? 80 HIS A N 1 ATOM 415 C CA . HIS A 1 66 ? 80.594 110.117 19.021 1.00 52.94 ? 80 HIS A CA 1 ATOM 416 C C . HIS A 1 66 ? 79.420 109.396 19.696 1.00 50.29 ? 80 HIS A C 1 ATOM 417 O O . HIS A 1 66 ? 78.434 110.020 20.095 1.00 51.40 ? 80 HIS A O 1 ATOM 418 C CB . HIS A 1 66 ? 80.251 110.360 17.546 1.00 55.36 ? 80 HIS A CB 1 ATOM 419 C CG . HIS A 1 66 ? 81.391 110.914 16.737 1.00 55.20 ? 80 HIS A CG 1 ATOM 420 N ND1 . HIS A 1 66 ? 81.636 110.523 15.439 1.00 56.55 ? 80 HIS A ND1 1 ATOM 421 C CD2 . HIS A 1 66 ? 82.344 111.827 17.042 1.00 56.10 ? 80 HIS A CD2 1 ATOM 422 C CE1 . HIS A 1 66 ? 82.692 111.174 14.976 1.00 56.09 ? 80 HIS A CE1 1 ATOM 423 N NE2 . HIS A 1 66 ? 83.140 111.974 15.928 1.00 54.49 ? 80 HIS A NE2 1 ATOM 424 N N . ILE A 1 67 ? 79.532 108.075 19.796 1.00 45.99 ? 81 ILE A N 1 ATOM 425 C CA . ILE A 1 67 ? 78.423 107.226 20.233 1.00 47.36 ? 81 ILE A CA 1 ATOM 426 C C . ILE A 1 67 ? 78.906 106.164 21.215 1.00 47.88 ? 81 ILE A C 1 ATOM 427 O O . ILE A 1 67 ? 79.962 105.557 21.007 1.00 42.65 ? 81 ILE A O 1 ATOM 428 C CB . ILE A 1 67 ? 77.776 106.486 19.025 1.00 46.73 ? 81 ILE A CB 1 ATOM 429 C CG1 . ILE A 1 67 ? 77.241 107.482 17.994 1.00 46.74 ? 81 ILE A CG1 1 ATOM 430 C CG2 . ILE A 1 67 ? 76.666 105.576 19.484 1.00 40.86 ? 81 ILE A CG2 1 ATOM 431 C CD1 . ILE A 1 67 ? 76.628 106.829 16.752 1.00 48.63 ? 81 ILE A CD1 1 ATOM 432 N N . LEU A 1 68 ? 78.134 105.932 22.279 1.00 45.53 ? 82 LEU A N 1 ATOM 433 C CA . LEU A 1 68 ? 78.395 104.813 23.172 1.00 44.15 ? 82 LEU A CA 1 ATOM 434 C C . LEU A 1 68 ? 77.124 103.983 23.309 1.00 43.24 ? 82 LEU A C 1 ATOM 435 O O . LEU A 1 68 ? 76.098 104.477 23.766 1.00 39.00 ? 82 LEU A O 1 ATOM 436 C CB . LEU A 1 68 ? 78.889 105.295 24.539 1.00 44.18 ? 82 LEU A CB 1 ATOM 437 C CG . LEU A 1 68 ? 78.954 104.241 25.656 1.00 41.18 ? 82 LEU A CG 1 ATOM 438 C CD1 . LEU A 1 68 ? 79.955 103.147 25.305 1.00 40.58 ? 82 LEU A CD1 1 ATOM 439 C CD2 . LEU A 1 68 ? 79.308 104.893 26.984 1.00 41.08 ? 82 LEU A CD2 1 ATOM 440 N N . LYS A 1 69 ? 77.189 102.735 22.869 1.00 44.37 ? 83 LYS A N 1 ATOM 441 C CA . LYS A 1 69 ? 76.063 101.826 22.991 1.00 45.15 ? 83 LYS A CA 1 ATOM 442 C C . LYS A 1 69 ? 76.344 100.842 24.118 1.00 41.39 ? 83 LYS A C 1 ATOM 443 O O . LYS A 1 69 ? 77.446 100.290 24.209 1.00 37.56 ? 83 LYS A O 1 ATOM 444 C CB . LYS A 1 69 ? 75.858 101.069 21.678 1.00 45.22 ? 83 LYS A CB 1 ATOM 445 C CG . LYS A 1 69 ? 74.688 100.092 21.690 1.00 36.12 ? 83 LYS A CG 1 ATOM 446 C CD . LYS A 1 69 ? 74.402 99.585 20.241 1.00 36.00 ? 83 LYS A CD 1 ATOM 447 C CE . LYS A 1 69 ? 74.182 98.083 20.207 1.00 40.57 ? 83 LYS A CE 1 ATOM 448 N NZ . LYS A 1 69 ? 73.601 97.588 18.912 1.00 42.61 ? 83 LYS A NZ 1 ATOM 449 N N . VAL A 1 70 ? 75.364 100.622 24.985 1.00 36.26 ? 84 VAL A N 1 ATOM 450 C CA . VAL A 1 70 ? 75.573 99.670 26.062 1.00 35.86 ? 84 VAL A CA 1 ATOM 451 C C . VAL A 1 70 ? 74.475 98.633 26.172 1.00 35.12 ? 84 VAL A C 1 ATOM 452 O O . VAL A 1 70 ? 73.321 98.880 25.788 1.00 36.77 ? 84 VAL A O 1 ATOM 453 C CB . VAL A 1 70 ? 75.712 100.373 27.428 1.00 46.48 ? 84 VAL A CB 1 ATOM 454 C CG1 . VAL A 1 70 ? 76.831 101.423 27.378 1.00 37.56 ? 84 VAL A CG1 1 ATOM 455 C CG2 . VAL A 1 70 ? 74.397 101.013 27.814 1.00 35.76 ? 84 VAL A CG2 1 ATOM 456 N N . GLU A 1 71 ? 74.841 97.476 26.717 1.00 36.28 ? 85 GLU A N 1 ATOM 457 C CA . GLU A 1 71 ? 73.871 96.430 27.005 1.00 35.75 ? 85 GLU A CA 1 ATOM 458 C C . GLU A 1 71 ? 73.002 96.809 28.207 1.00 36.72 ? 85 GLU A C 1 ATOM 459 O O . GLU A 1 71 ? 73.500 97.345 29.208 1.00 38.87 ? 85 GLU A O 1 ATOM 460 C CB . GLU A 1 71 ? 74.576 95.100 27.280 1.00 33.24 ? 85 GLU A CB 1 ATOM 461 C CG . GLU A 1 71 ? 73.694 94.069 27.985 1.00 32.27 ? 85 GLU A CG 1 ATOM 462 C CD . GLU A 1 71 ? 74.383 92.729 28.160 1.00 35.93 ? 85 GLU A CD 1 ATOM 463 O OE1 . GLU A 1 71 ? 75.604 92.649 27.875 1.00 38.47 ? 85 GLU A OE1 1 ATOM 464 O OE2 . GLU A 1 71 ? 73.711 91.756 28.588 1.00 33.67 ? 85 GLU A OE2 1 ATOM 465 N N . ILE A 1 72 ? 71.704 96.553 28.095 1.00 33.23 ? 86 ILE A N 1 ATOM 466 C CA . ILE A 1 72 ? 70.829 96.624 29.249 1.00 37.32 ? 86 ILE A CA 1 ATOM 467 C C . ILE A 1 72 ? 70.812 95.214 29.819 1.00 35.11 ? 86 ILE A C 1 ATOM 468 O O . ILE A 1 72 ? 70.117 94.328 29.301 1.00 32.20 ? 86 ILE A O 1 ATOM 469 C CB . ILE A 1 72 ? 69.417 97.059 28.861 1.00 38.80 ? 86 ILE A CB 1 ATOM 470 C CG1 . ILE A 1 72 ? 69.459 98.461 28.241 1.00 36.09 ? 86 ILE A CG1 1 ATOM 471 C CG2 . ILE A 1 72 ? 68.488 97.044 30.072 1.00 33.67 ? 86 ILE A CG2 1 ATOM 472 C CD1 . ILE A 1 72 ? 68.177 98.832 27.568 1.00 31.77 ? 86 ILE A CD1 1 ATOM 473 N N . GLY A 1 73 ? 71.620 95.015 30.858 1.00 35.62 ? 87 GLY A N 1 ATOM 474 C CA . GLY A 1 73 ? 71.837 93.710 31.458 1.00 36.13 ? 87 GLY A CA 1 ATOM 475 C C . GLY A 1 73 ? 70.546 93.027 31.839 1.00 33.49 ? 87 GLY A C 1 ATOM 476 O O . GLY A 1 73 ? 69.649 93.656 32.402 1.00 33.91 ? 87 GLY A O 1 ATOM 477 N N . GLY A 1 74 ? 70.438 91.745 31.507 1.00 32.37 ? 88 GLY A N 1 ATOM 478 C CA . GLY A 1 74 ? 69.241 90.988 31.823 1.00 30.36 ? 88 GLY A CA 1 ATOM 479 C C . GLY A 1 74 ? 69.569 89.752 32.645 1.00 33.71 ? 88 GLY A C 1 ATOM 480 O O . GLY A 1 74 ? 68.803 88.787 32.642 1.00 42.27 ? 88 GLY A O 1 ATOM 481 N N . ASP A 1 75 ? 70.720 89.779 33.316 1.00 33.44 ? 89 ASP A N 1 ATOM 482 C CA . ASP A 1 75 ? 71.175 88.680 34.187 1.00 34.15 ? 89 ASP A CA 1 ATOM 483 C C . ASP A 1 75 ? 71.594 87.415 33.441 1.00 34.18 ? 89 ASP A C 1 ATOM 484 O O . ASP A 1 75 ? 72.002 86.440 34.070 1.00 30.43 ? 89 ASP A O 1 ATOM 485 C CB . ASP A 1 75 ? 70.129 88.304 35.260 1.00 34.41 ? 89 ASP A CB 1 ATOM 486 C CG . ASP A 1 75 ? 69.883 89.413 36.280 1.00 34.18 ? 89 ASP A CG 1 ATOM 487 O OD1 . ASP A 1 75 ? 70.751 90.315 36.430 1.00 32.26 ? 89 ASP A OD1 1 ATOM 488 O OD2 . ASP A 1 75 ? 68.809 89.374 36.939 1.00 32.57 ? 89 ASP A OD2 1 ATOM 489 N N . GLY A 1 76 ? 71.501 87.415 32.115 1.00 35.45 ? 90 GLY A N 1 ATOM 490 C CA . GLY A 1 76 ? 71.924 86.247 31.356 1.00 33.04 ? 90 GLY A CA 1 ATOM 491 C C . GLY A 1 76 ? 73.323 86.394 30.768 1.00 32.81 ? 90 GLY A C 1 ATOM 492 O O . GLY A 1 76 ? 73.838 87.503 30.668 1.00 30.58 ? 90 GLY A O 1 ATOM 493 N N . GLN A 1 77 ? 73.941 85.268 30.403 1.00 30.22 ? 91 GLN A N 1 ATOM 494 C CA . GLN A 1 77 ? 75.256 85.273 29.765 1.00 35.90 ? 91 GLN A CA 1 ATOM 495 C C . GLN A 1 77 ? 75.096 85.892 28.370 1.00 36.61 ? 91 GLN A C 1 ATOM 496 O O . GLN A 1 77 ? 74.200 85.489 27.621 1.00 32.58 ? 91 GLN A O 1 ATOM 497 C CB . GLN A 1 77 ? 75.791 83.844 29.624 1.00 31.34 ? 91 GLN A CB 1 ATOM 498 C CG . GLN A 1 77 ? 76.801 83.702 28.468 1.00 35.76 ? 91 GLN A CG 1 ATOM 499 C CD . GLN A 1 77 ? 78.151 84.276 28.846 1.00 37.10 ? 91 GLN A CD 1 ATOM 500 O OE1 . GLN A 1 77 ? 78.807 84.969 28.060 1.00 34.54 ? 91 GLN A OE1 1 ATOM 501 N NE2 . GLN A 1 77 ? 78.570 83.991 30.075 1.00 36.45 ? 91 GLN A NE2 1 ATOM 502 N N . THR A 1 78 ? 75.935 86.879 28.036 1.00 34.69 ? 92 THR A N 1 ATOM 503 C CA . THR A 1 78 ? 75.773 87.616 26.774 1.00 38.14 ? 92 THR A CA 1 ATOM 504 C C . THR A 1 78 ? 77.016 87.790 25.880 1.00 37.53 ? 92 THR A C 1 ATOM 505 O O . THR A 1 78 ? 77.006 88.639 24.985 1.00 34.22 ? 92 THR A O 1 ATOM 506 C CB . THR A 1 78 ? 75.054 88.961 27.001 1.00 35.08 ? 92 THR A CB 1 ATOM 507 O OG1 . THR A 1 78 ? 75.773 89.734 27.969 1.00 34.64 ? 92 THR A OG1 1 ATOM 508 C CG2 . THR A 1 78 ? 73.645 88.689 27.527 1.00 31.85 ? 92 THR A CG2 1 ATOM 509 N N . THR A 1 79 ? 78.050 86.984 26.161 1.00 36.38 ? 93 THR A N 1 ATOM 510 C CA . THR A 1 79 ? 79.193 86.619 25.275 1.00 34.26 ? 93 THR A CA 1 ATOM 511 C C . THR A 1 79 ? 80.489 86.381 26.067 1.00 36.40 ? 93 THR A C 1 ATOM 512 O O . THR A 1 79 ? 81.166 85.364 25.870 1.00 40.93 ? 93 THR A O 1 ATOM 513 C CB . THR A 1 79 ? 79.426 87.551 24.048 1.00 34.64 ? 93 THR A CB 1 ATOM 514 O OG1 . THR A 1 79 ? 78.359 87.373 23.098 1.00 33.84 ? 93 THR A OG1 1 ATOM 515 C CG2 . THR A 1 79 ? 80.745 87.205 23.350 1.00 35.63 ? 93 THR A CG2 1 ATOM 516 N N . ASP A 1 80 ? 80.820 87.306 26.964 1.00 36.10 ? 94 ASP A N 1 ATOM 517 C CA . ASP A 1 80 ? 82.000 87.168 27.824 1.00 36.55 ? 94 ASP A CA 1 ATOM 518 C C . ASP A 1 80 ? 81.643 87.258 29.320 1.00 37.85 ? 94 ASP A C 1 ATOM 519 O O . ASP A 1 80 ? 82.500 87.547 30.163 1.00 40.59 ? 94 ASP A O 1 ATOM 520 C CB . ASP A 1 80 ? 83.048 88.221 27.445 1.00 38.64 ? 94 ASP A CB 1 ATOM 521 C CG . ASP A 1 80 ? 83.502 88.084 26.006 1.00 42.75 ? 94 ASP A CG 1 ATOM 522 O OD1 . ASP A 1 80 ? 84.124 87.044 25.700 1.00 40.95 ? 94 ASP A OD1 1 ATOM 523 O OD2 . ASP A 1 80 ? 83.230 88.992 25.181 1.00 40.30 ? 94 ASP A OD2 1 ATOM 524 N N . GLY A 1 81 ? 80.383 86.966 29.643 1.00 35.31 ? 95 GLY A N 1 ATOM 525 C CA . GLY A 1 81 ? 79.897 86.994 31.019 1.00 35.01 ? 95 GLY A CA 1 ATOM 526 C C . GLY A 1 81 ? 78.419 87.355 31.096 1.00 42.15 ? 95 GLY A C 1 ATOM 527 O O . GLY A 1 81 ? 77.756 87.511 30.062 1.00 34.77 ? 95 GLY A O 1 ATOM 528 N N . THR A 1 82 ? 77.882 87.464 32.308 1.00 40.35 ? 96 THR A N 1 ATOM 529 C CA . THR A 1 82 ? 76.521 87.970 32.487 1.00 35.23 ? 96 THR A CA 1 ATOM 530 C C . THR A 1 82 ? 76.639 89.453 32.844 1.00 35.39 ? 96 THR A C 1 ATOM 531 O O . THR A 1 82 ? 77.701 89.890 33.267 1.00 34.82 ? 96 THR A O 1 ATOM 532 C CB . THR A 1 82 ? 75.791 87.233 33.616 1.00 35.20 ? 96 THR A CB 1 ATOM 533 O OG1 . THR A 1 82 ? 76.336 87.638 34.880 1.00 36.17 ? 96 THR A OG1 1 ATOM 534 C CG2 . THR A 1 82 ? 75.930 85.727 33.452 1.00 34.12 ? 96 THR A CG2 1 ATOM 535 N N . GLU A 1 83 ? 75.582 90.237 32.660 1.00 34.97 ? 97 GLU A N 1 ATOM 536 C CA . GLU A 1 83 ? 75.584 91.603 33.198 1.00 39.86 ? 97 GLU A CA 1 ATOM 537 C C . GLU A 1 83 ? 74.311 91.812 34.013 1.00 39.09 ? 97 GLU A C 1 ATOM 538 O O . GLU A 1 83 ? 73.238 91.467 33.549 1.00 33.17 ? 97 GLU A O 1 ATOM 539 C CB . GLU A 1 83 ? 75.727 92.657 32.089 1.00 40.37 ? 97 GLU A CB 1 ATOM 540 C CG . GLU A 1 83 ? 77.159 92.765 31.540 1.00 43.31 ? 97 GLU A CG 1 ATOM 541 C CD . GLU A 1 83 ? 77.406 94.026 30.731 1.00 44.08 ? 97 GLU A CD 1 ATOM 542 O OE1 . GLU A 1 83 ? 76.856 95.083 31.104 1.00 44.23 ? 97 GLU A OE1 1 ATOM 543 O OE2 . GLU A 1 83 ? 78.154 93.966 29.724 1.00 42.71 ? 97 GLU A OE2 1 ATOM 544 N N . PRO A 1 84 ? 74.434 92.364 35.237 1.00 36.36 ? 98 PRO A N 1 ATOM 545 C CA . PRO A 1 84 ? 73.300 92.493 36.169 1.00 35.18 ? 98 PRO A CA 1 ATOM 546 C C . PRO A 1 84 ? 72.165 93.388 35.681 1.00 31.89 ? 98 PRO A C 1 ATOM 547 O O . PRO A 1 84 ? 72.377 94.470 35.112 1.00 33.37 ? 98 PRO A O 1 ATOM 548 C CB . PRO A 1 84 ? 73.930 93.088 37.441 1.00 32.92 ? 98 PRO A CB 1 ATOM 549 C CG . PRO A 1 84 ? 75.224 93.684 36.981 1.00 35.61 ? 98 PRO A CG 1 ATOM 550 C CD . PRO A 1 84 ? 75.693 92.816 35.842 1.00 38.96 ? 98 PRO A CD 1 ATOM 551 N N . SER A 1 85 ? 70.946 92.925 35.922 1.00 31.31 ? 99 SER A N 1 ATOM 552 C CA . SER A 1 85 ? 69.744 93.660 35.532 1.00 31.82 ? 99 SER A CA 1 ATOM 553 C C . SER A 1 85 ? 69.334 94.657 36.613 1.00 36.43 ? 99 SER A C 1 ATOM 554 O O . SER A 1 85 ? 69.728 94.528 37.783 1.00 37.04 ? 99 SER A O 1 ATOM 555 C CB . SER A 1 85 ? 68.611 92.671 35.297 1.00 28.97 ? 99 SER A CB 1 ATOM 556 O OG . SER A 1 85 ? 67.388 93.342 35.069 1.00 29.16 ? 99 SER A OG 1 ATOM 557 N N . HIS A 1 86 ? 68.546 95.655 36.229 1.00 36.92 ? 100 HIS A N 1 ATOM 558 C CA . HIS A 1 86 ? 67.992 96.577 37.222 1.00 37.11 ? 100 HIS A CA 1 ATOM 559 C C . HIS A 1 86 ? 66.810 95.960 37.962 1.00 37.72 ? 100 HIS A C 1 ATOM 560 O O . HIS A 1 86 ? 66.416 96.465 39.010 1.00 35.36 ? 100 HIS A O 1 ATOM 561 C CB . HIS A 1 86 ? 67.575 97.905 36.586 1.00 34.61 ? 100 HIS A CB 1 ATOM 562 C CG . HIS A 1 86 ? 66.589 97.751 35.470 1.00 34.63 ? 100 HIS A CG 1 ATOM 563 N ND1 . HIS A 1 86 ? 66.917 97.161 34.267 1.00 35.44 ? 100 HIS A ND1 1 ATOM 564 C CD2 . HIS A 1 86 ? 65.294 98.124 35.366 1.00 30.37 ? 100 HIS A CD2 1 ATOM 565 C CE1 . HIS A 1 86 ? 65.855 97.158 33.477 1.00 36.67 ? 100 HIS A CE1 1 ATOM 566 N NE2 . HIS A 1 86 ? 64.859 97.747 34.116 1.00 34.73 ? 100 HIS A NE2 1 ATOM 567 N N . MET A 1 87 ? 66.228 94.887 37.420 1.00 35.76 ? 101 MET A N 1 ATOM 568 C CA . MET A 1 87 ? 65.132 94.191 38.108 1.00 34.29 ? 101 MET A CA 1 ATOM 569 C C . MET A 1 87 ? 65.338 92.673 38.147 1.00 34.70 ? 101 MET A C 1 ATOM 570 O O . MET A 1 87 ? 64.849 91.949 37.265 1.00 29.79 ? 101 MET A O 1 ATOM 571 C CB . MET A 1 87 ? 63.779 94.485 37.447 1.00 31.58 ? 101 MET A CB 1 ATOM 572 C CG . MET A 1 87 ? 63.448 95.954 37.232 1.00 33.22 ? 101 MET A CG 1 ATOM 573 S SD . MET A 1 87 ? 61.846 96.148 36.420 1.00 38.56 ? 101 MET A SD 1 ATOM 574 C CE . MET A 1 87 ? 60.751 95.834 37.798 1.00 36.34 ? 101 MET A CE 1 ATOM 575 N N . HIS A 1 88 ? 66.050 92.188 39.163 1.00 34.17 ? 102 HIS A N 1 ATOM 576 C CA . HIS A 1 88 ? 66.319 90.751 39.288 1.00 32.66 ? 102 HIS A CA 1 ATOM 577 C C . HIS A 1 88 ? 65.026 89.951 39.462 1.00 30.81 ? 102 HIS A C 1 ATOM 578 O O . HIS A 1 88 ? 64.887 88.847 38.935 1.00 36.61 ? 102 HIS A O 1 ATOM 579 C CB . HIS A 1 88 ? 67.230 90.466 40.490 1.00 30.89 ? 102 HIS A CB 1 ATOM 580 C CG . HIS A 1 88 ? 68.643 90.935 40.333 1.00 31.64 ? 102 HIS A CG 1 ATOM 581 N ND1 . HIS A 1 88 ? 69.337 90.868 39.141 1.00 30.64 ? 102 HIS A ND1 1 ATOM 582 C CD2 . HIS A 1 88 ? 69.512 91.442 41.244 1.00 32.21 ? 102 HIS A CD2 1 ATOM 583 C CE1 . HIS A 1 88 ? 70.563 91.339 39.320 1.00 33.67 ? 102 HIS A CE1 1 ATOM 584 N NE2 . HIS A 1 88 ? 70.692 91.694 40.591 1.00 35.31 ? 102 HIS A NE2 1 ATOM 585 N N . TYR A 1 89 ? 64.095 90.506 40.231 1.00 27.91 ? 103 TYR A N 1 ATOM 586 C CA . TYR A 1 89 ? 62.829 89.847 40.535 1.00 31.83 ? 103 TYR A CA 1 ATOM 587 C C . TYR A 1 89 ? 61.723 90.845 40.273 1.00 32.57 ? 103 TYR A C 1 ATOM 588 O O . TYR A 1 89 ? 61.984 92.034 40.122 1.00 32.70 ? 103 TYR A O 1 ATOM 589 C CB . TYR A 1 89 ? 62.764 89.410 42.014 1.00 31.22 ? 103 TYR A CB 1 ATOM 590 C CG . TYR A 1 89 ? 64.107 89.093 42.619 1.00 33.54 ? 103 TYR A CG 1 ATOM 591 C CD1 . TYR A 1 89 ? 64.773 87.912 42.304 1.00 35.19 ? 103 TYR A CD1 1 ATOM 592 C CD2 . TYR A 1 89 ? 64.713 89.972 43.506 1.00 34.41 ? 103 TYR A CD2 1 ATOM 593 C CE1 . TYR A 1 89 ? 66.019 87.623 42.850 1.00 31.34 ? 103 TYR A CE1 1 ATOM 594 C CE2 . TYR A 1 89 ? 65.964 89.696 44.054 1.00 35.52 ? 103 TYR A CE2 1 ATOM 595 C CZ . TYR A 1 89 ? 66.600 88.511 43.719 1.00 35.06 ? 103 TYR A CZ 1 ATOM 596 O OH . TYR A 1 89 ? 67.836 88.214 44.238 1.00 34.96 ? 103 TYR A OH 1 ATOM 597 N N . GLU A 1 90 ? 60.489 90.363 40.202 1.00 29.72 ? 104 GLU A N 1 ATOM 598 C CA . GLU A 1 90 ? 59.331 91.256 40.244 1.00 38.90 ? 104 GLU A CA 1 ATOM 599 C C . GLU A 1 90 ? 59.409 92.105 41.537 1.00 41.06 ? 104 GLU A C 1 ATOM 600 O O . GLU A 1 90 ? 59.808 91.585 42.579 1.00 39.64 ? 104 GLU A O 1 ATOM 601 C CB . GLU A 1 90 ? 58.049 90.415 40.252 1.00 40.04 ? 104 GLU A CB 1 ATOM 602 C CG . GLU A 1 90 ? 56.831 91.072 39.597 1.00 48.79 ? 104 GLU A CG 1 ATOM 603 C CD . GLU A 1 90 ? 55.612 90.139 39.586 1.00 58.76 ? 104 GLU A CD 1 ATOM 604 O OE1 . GLU A 1 90 ? 55.728 88.997 40.090 1.00 59.41 ? 104 GLU A OE1 1 ATOM 605 O OE2 . GLU A 1 90 ? 54.545 90.544 39.066 1.00 63.27 ? 104 GLU A OE2 1 ATOM 606 N N . LEU A 1 91 ? 59.036 93.389 41.449 1.00 39.32 ? 105 LEU A N 1 ATOM 607 C CA . LEU A 1 91 ? 59.077 94.346 42.563 1.00 36.15 ? 105 LEU A CA 1 ATOM 608 C C . LEU A 1 91 ? 60.476 94.770 42.976 1.00 39.17 ? 105 LEU A C 1 ATOM 609 O O . LEU A 1 91 ? 60.654 95.513 43.956 1.00 42.27 ? 105 LEU A O 1 ATOM 610 C CB . LEU A 1 91 ? 58.336 93.822 43.810 1.00 39.59 ? 105 LEU A CB 1 ATOM 611 C CG . LEU A 1 91 ? 56.892 93.390 43.599 1.00 38.92 ? 105 LEU A CG 1 ATOM 612 C CD1 . LEU A 1 91 ? 56.228 93.181 44.963 1.00 40.26 ? 105 LEU A CD1 1 ATOM 613 C CD2 . LEU A 1 91 ? 56.151 94.416 42.740 1.00 38.37 ? 105 LEU A CD2 1 ATOM 614 N N . ASP A 1 92 ? 61.482 94.299 42.261 1.00 34.12 ? 106 ASP A N 1 ATOM 615 C CA . ASP A 1 92 ? 62.821 94.734 42.586 1.00 36.76 ? 106 ASP A CA 1 ATOM 616 C C . ASP A 1 92 ? 63.259 95.826 41.618 1.00 36.40 ? 106 ASP A C 1 ATOM 617 O O . ASP A 1 92 ? 63.105 95.671 40.400 1.00 35.55 ? 106 ASP A O 1 ATOM 618 C CB . ASP A 1 92 ? 63.776 93.558 42.528 1.00 40.60 ? 106 ASP A CB 1 ATOM 619 C CG . ASP A 1 92 ? 65.211 93.996 42.606 1.00 45.84 ? 106 ASP A CG 1 ATOM 620 O OD1 . ASP A 1 92 ? 65.580 94.572 43.655 1.00 48.57 ? 106 ASP A OD1 1 ATOM 621 O OD2 . ASP A 1 92 ? 65.960 93.778 41.625 1.00 46.88 ? 106 ASP A OD2 1 ATOM 622 N N . GLU A 1 93 ? 63.762 96.944 42.139 1.00 33.54 ? 107 GLU A N 1 ATOM 623 C CA . GLU A 1 93 ? 64.376 97.958 41.272 1.00 31.70 ? 107 GLU A CA 1 ATOM 624 C C . GLU A 1 93 ? 65.668 98.438 41.901 1.00 37.22 ? 107 GLU A C 1 ATOM 625 O O . GLU A 1 93 ? 65.695 98.801 43.085 1.00 39.16 ? 107 GLU A O 1 ATOM 626 C CB . GLU A 1 93 ? 63.433 99.156 41.011 1.00 36.02 ? 107 GLU A CB 1 ATOM 627 C CG . GLU A 1 93 ? 62.259 98.876 40.038 1.00 48.72 ? 107 GLU A CG 1 ATOM 628 C CD . GLU A 1 93 ? 61.481 100.143 39.605 1.00 50.00 ? 107 GLU A CD 1 ATOM 629 O OE1 . GLU A 1 93 ? 62.122 101.180 39.287 1.00 47.79 ? 107 GLU A OE1 1 ATOM 630 O OE2 . GLU A 1 93 ? 60.222 100.085 39.551 1.00 51.60 ? 107 GLU A OE2 1 ATOM 631 N N . ASN A 1 94 ? 66.745 98.442 41.121 1.00 34.78 ? 108 ASN A N 1 ATOM 632 C CA . ASN A 1 94 ? 68.017 98.969 41.605 1.00 35.50 ? 108 ASN A CA 1 ATOM 633 C C . ASN A 1 94 ? 68.816 99.499 40.427 1.00 37.14 ? 108 ASN A C 1 ATOM 634 O O . ASN A 1 94 ? 69.087 98.749 39.485 1.00 32.48 ? 108 ASN A O 1 ATOM 635 C CB . ASN A 1 94 ? 68.798 97.867 42.322 1.00 37.61 ? 108 ASN A CB 1 ATOM 636 C CG . ASN A 1 94 ? 70.064 98.375 43.000 1.00 41.08 ? 108 ASN A CG 1 ATOM 637 O OD1 . ASN A 1 94 ? 70.827 99.158 42.435 1.00 41.54 ? 108 ASN A OD1 1 ATOM 638 N ND2 . ASN A 1 94 ? 70.299 97.905 44.221 1.00 47.82 ? 108 ASN A ND2 1 ATOM 639 N N . TYR A 1 95 ? 69.213 100.770 40.487 1.00 33.78 ? 109 TYR A N 1 ATOM 640 C CA . TYR A 1 95 ? 69.833 101.411 39.322 1.00 35.22 ? 109 TYR A CA 1 ATOM 641 C C . TYR A 1 95 ? 71.296 101.710 39.586 1.00 35.38 ? 109 TYR A C 1 ATOM 642 O O . TYR A 1 95 ? 71.892 102.643 39.012 1.00 38.72 ? 109 TYR A O 1 ATOM 643 C CB . TYR A 1 95 ? 69.028 102.651 38.902 1.00 34.42 ? 109 TYR A CB 1 ATOM 644 C CG . TYR A 1 95 ? 67.622 102.297 38.492 1.00 33.34 ? 109 TYR A CG 1 ATOM 645 C CD1 . TYR A 1 95 ? 67.339 101.919 37.189 1.00 37.97 ? 109 TYR A CD1 1 ATOM 646 C CD2 . TYR A 1 95 ? 66.576 102.307 39.413 1.00 32.92 ? 109 TYR A CD2 1 ATOM 647 C CE1 . TYR A 1 95 ? 66.044 101.564 36.801 1.00 35.51 ? 109 TYR A CE1 1 ATOM 648 C CE2 . TYR A 1 95 ? 65.284 101.955 39.036 1.00 35.28 ? 109 TYR A CE2 1 ATOM 649 C CZ . TYR A 1 95 ? 65.028 101.587 37.716 1.00 34.79 ? 109 TYR A CZ 1 ATOM 650 O OH . TYR A 1 95 ? 63.751 101.220 37.316 1.00 38.69 ? 109 TYR A OH 1 ATOM 651 N N . PHE A 1 96 ? 71.886 100.875 40.431 1.00 35.47 ? 110 PHE A N 1 ATOM 652 C CA . PHE A 1 96 ? 73.287 101.052 40.797 1.00 40.98 ? 110 PHE A CA 1 ATOM 653 C C . PHE A 1 96 ? 74.137 99.786 40.605 1.00 42.56 ? 110 PHE A C 1 ATOM 654 O O . PHE A 1 96 ? 75.315 99.762 40.968 1.00 43.53 ? 110 PHE A O 1 ATOM 655 C CB . PHE A 1 96 ? 73.391 101.628 42.215 1.00 40.80 ? 110 PHE A CB 1 ATOM 656 C CG . PHE A 1 96 ? 72.838 103.032 42.325 1.00 40.23 ? 110 PHE A CG 1 ATOM 657 C CD1 . PHE A 1 96 ? 73.646 104.138 42.063 1.00 42.64 ? 110 PHE A CD1 1 ATOM 658 C CD2 . PHE A 1 96 ? 71.503 103.241 42.655 1.00 40.89 ? 110 PHE A CD2 1 ATOM 659 C CE1 . PHE A 1 96 ? 73.130 105.431 42.146 1.00 42.95 ? 110 PHE A CE1 1 ATOM 660 C CE2 . PHE A 1 96 ? 70.979 104.525 42.736 1.00 42.66 ? 110 PHE A CE2 1 ATOM 661 C CZ . PHE A 1 96 ? 71.783 105.616 42.479 1.00 41.58 ? 110 PHE A CZ 1 ATOM 662 N N . ARG A 1 97 ? 73.559 98.749 39.991 1.00 35.77 ? 111 ARG A N 1 ATOM 663 C CA . ARG A 1 97 ? 74.321 97.536 39.725 1.00 37.13 ? 111 ARG A CA 1 ATOM 664 C C . ARG A 1 97 ? 75.155 97.657 38.452 1.00 38.05 ? 111 ARG A C 1 ATOM 665 O O . ARG A 1 97 ? 74.843 98.468 37.581 1.00 42.49 ? 111 ARG A O 1 ATOM 666 C CB . ARG A 1 97 ? 73.389 96.337 39.611 1.00 39.17 ? 111 ARG A CB 1 ATOM 667 C CG . ARG A 1 97 ? 72.484 96.128 40.826 1.00 38.16 ? 111 ARG A CG 1 ATOM 668 C CD . ARG A 1 97 ? 71.525 95.003 40.553 1.00 38.47 ? 111 ARG A CD 1 ATOM 669 N NE . ARG A 1 97 ? 70.697 94.699 41.721 1.00 38.46 ? 111 ARG A NE 1 ATOM 670 C CZ . ARG A 1 97 ? 69.379 94.565 41.673 1.00 39.86 ? 111 ARG A CZ 1 ATOM 671 N NH1 . ARG A 1 97 ? 68.738 94.691 40.513 1.00 30.64 ? 111 ARG A NH1 1 ATOM 672 N NH2 . ARG A 1 97 ? 68.707 94.284 42.777 1.00 39.17 ? 111 ARG A NH2 1 ATOM 673 N N . GLY A 1 98 ? 76.218 96.855 38.354 1.00 39.24 ? 112 GLY A N 1 ATOM 674 C CA . GLY A 1 98 ? 77.012 96.764 37.134 1.00 36.40 ? 112 GLY A CA 1 ATOM 675 C C . GLY A 1 98 ? 77.917 97.944 36.892 1.00 38.48 ? 112 GLY A C 1 ATOM 676 O O . GLY A 1 98 ? 78.276 98.668 37.814 1.00 42.62 ? 112 GLY A O 1 ATOM 677 N N . TYR A 1 99 ? 78.297 98.163 35.641 1.00 39.46 ? 113 TYR A N 1 ATOM 678 C CA . TYR A 1 99 ? 79.256 99.212 35.386 1.00 43.08 ? 113 TYR A CA 1 ATOM 679 C C . TYR A 1 99 ? 78.878 100.104 34.212 1.00 45.01 ? 113 TYR A C 1 ATOM 680 O O . TYR A 1 99 ? 79.588 101.066 33.908 1.00 39.86 ? 113 TYR A O 1 ATOM 681 C CB . TYR A 1 99 ? 80.646 98.603 35.215 1.00 44.29 ? 113 TYR A CB 1 ATOM 682 C CG . TYR A 1 99 ? 80.616 97.192 34.672 1.00 44.28 ? 113 TYR A CG 1 ATOM 683 C CD1 . TYR A 1 99 ? 80.623 96.957 33.295 1.00 42.75 ? 113 TYR A CD1 1 ATOM 684 C CD2 . TYR A 1 99 ? 80.579 96.096 35.534 1.00 44.17 ? 113 TYR A CD2 1 ATOM 685 C CE1 . TYR A 1 99 ? 80.584 95.665 32.789 1.00 46.31 ? 113 TYR A CE1 1 ATOM 686 C CE2 . TYR A 1 99 ? 80.545 94.807 35.042 1.00 49.83 ? 113 TYR A CE2 1 ATOM 687 C CZ . TYR A 1 99 ? 80.548 94.597 33.663 1.00 50.08 ? 113 TYR A CZ 1 ATOM 688 O OH . TYR A 1 99 ? 80.515 93.314 33.161 1.00 50.23 ? 113 TYR A OH 1 ATOM 689 N N . GLU A 1 100 ? 77.749 99.816 33.573 1.00 43.82 ? 114 GLU A N 1 ATOM 690 C CA . GLU A 1 100 ? 77.344 100.616 32.420 1.00 42.45 ? 114 GLU A CA 1 ATOM 691 C C . GLU A 1 100 ? 76.869 102.014 32.844 1.00 42.72 ? 114 GLU A C 1 ATOM 692 O O . GLU A 1 100 ? 77.030 102.962 32.093 1.00 43.46 ? 114 GLU A O 1 ATOM 693 C CB . GLU A 1 100 ? 76.276 99.892 31.575 1.00 38.95 ? 114 GLU A CB 1 ATOM 694 C CG . GLU A 1 100 ? 76.608 98.430 31.183 1.00 46.01 ? 114 GLU A CG 1 ATOM 695 C CD . GLU A 1 100 ? 77.901 98.263 30.354 1.00 47.63 ? 114 GLU A CD 1 ATOM 696 O OE1 . GLU A 1 100 ? 78.471 99.263 29.866 1.00 48.84 ? 114 GLU A OE1 1 ATOM 697 O OE2 . GLU A 1 100 ? 78.355 97.107 30.184 1.00 45.14 ? 114 GLU A OE2 1 ATOM 698 N N . TRP A 1 101 ? 76.289 102.150 34.041 1.00 41.06 ? 115 TRP A N 1 ATOM 699 C CA . TRP A 1 101 ? 75.902 103.479 34.526 1.00 42.02 ? 115 TRP A CA 1 ATOM 700 C C . TRP A 1 101 ? 77.154 104.357 34.657 1.00 45.12 ? 115 TRP A C 1 ATOM 701 O O . TRP A 1 101 ? 77.228 105.471 34.118 1.00 45.61 ? 115 TRP A O 1 ATOM 702 C CB . TRP A 1 101 ? 75.237 103.390 35.906 1.00 42.03 ? 115 TRP A CB 1 ATOM 703 C CG . TRP A 1 101 ? 74.066 102.456 36.001 1.00 41.40 ? 115 TRP A CG 1 ATOM 704 C CD1 . TRP A 1 101 ? 73.978 101.323 36.770 1.00 41.88 ? 115 TRP A CD1 1 ATOM 705 C CD2 . TRP A 1 101 ? 72.797 102.588 35.342 1.00 41.49 ? 115 TRP A CD2 1 ATOM 706 N NE1 . TRP A 1 101 ? 72.736 100.742 36.619 1.00 37.12 ? 115 TRP A NE1 1 ATOM 707 C CE2 . TRP A 1 101 ? 71.995 101.497 35.749 1.00 38.17 ? 115 TRP A CE2 1 ATOM 708 C CE3 . TRP A 1 101 ? 72.264 103.523 34.449 1.00 43.33 ? 115 TRP A CE3 1 ATOM 709 C CZ2 . TRP A 1 101 ? 70.689 101.319 35.293 1.00 35.88 ? 115 TRP A CZ2 1 ATOM 710 C CZ3 . TRP A 1 101 ? 70.963 103.338 33.991 1.00 39.84 ? 115 TRP A CZ3 1 ATOM 711 C CH2 . TRP A 1 101 ? 70.194 102.250 34.417 1.00 37.97 ? 115 TRP A CH2 1 ATOM 712 N N . TRP A 1 102 ? 78.129 103.843 35.396 1.00 40.29 ? 116 TRP A N 1 ATOM 713 C CA . TRP A 1 102 ? 79.410 104.507 35.593 1.00 45.04 ? 116 TRP A CA 1 ATOM 714 C C . TRP A 1 102 ? 80.056 104.852 34.249 1.00 48.53 ? 116 TRP A C 1 ATOM 715 O O . TRP A 1 102 ? 80.503 105.979 34.034 1.00 45.99 ? 116 TRP A O 1 ATOM 716 C CB . TRP A 1 102 ? 80.313 103.592 36.424 1.00 44.95 ? 116 TRP A CB 1 ATOM 717 C CG . TRP A 1 102 ? 81.704 104.057 36.551 1.00 47.99 ? 116 TRP A CG 1 ATOM 718 C CD1 . TRP A 1 102 ? 82.195 104.989 37.430 1.00 48.17 ? 116 TRP A CD1 1 ATOM 719 C CD2 . TRP A 1 102 ? 82.817 103.598 35.783 1.00 50.50 ? 116 TRP A CD2 1 ATOM 720 N NE1 . TRP A 1 102 ? 83.548 105.149 37.229 1.00 49.14 ? 116 TRP A NE1 1 ATOM 721 C CE2 . TRP A 1 102 ? 83.955 104.301 36.231 1.00 49.09 ? 116 TRP A CE2 1 ATOM 722 C CE3 . TRP A 1 102 ? 82.956 102.662 34.749 1.00 48.90 ? 116 TRP A CE3 1 ATOM 723 C CZ2 . TRP A 1 102 ? 85.225 104.096 35.681 1.00 51.45 ? 116 TRP A CZ2 1 ATOM 724 C CZ3 . TRP A 1 102 ? 84.215 102.458 34.206 1.00 51.75 ? 116 TRP A CZ3 1 ATOM 725 C CH2 . TRP A 1 102 ? 85.335 103.176 34.669 1.00 50.15 ? 116 TRP A CH2 1 ATOM 726 N N . LEU A 1 103 ? 80.071 103.893 33.332 1.00 47.40 ? 117 LEU A N 1 ATOM 727 C CA . LEU A 1 103 ? 80.742 104.120 32.057 1.00 50.35 ? 117 LEU A CA 1 ATOM 728 C C . LEU A 1 103 ? 80.092 105.248 31.258 1.00 47.98 ? 117 LEU A C 1 ATOM 729 O O . LEU A 1 103 ? 80.787 106.126 30.743 1.00 51.48 ? 117 LEU A O 1 ATOM 730 C CB . LEU A 1 103 ? 80.791 102.834 31.236 1.00 47.35 ? 117 LEU A CB 1 ATOM 731 C CG . LEU A 1 103 ? 81.583 102.873 29.925 1.00 47.46 ? 117 LEU A CG 1 ATOM 732 C CD1 . LEU A 1 103 ? 83.059 103.110 30.176 1.00 48.29 ? 117 LEU A CD1 1 ATOM 733 C CD2 . LEU A 1 103 ? 81.367 101.562 29.200 1.00 43.83 ? 117 LEU A CD2 1 ATOM 734 N N . MET A 1 104 ? 78.770 105.230 31.160 1.00 45.39 ? 118 MET A N 1 ATOM 735 C CA . MET A 1 104 ? 78.062 106.295 30.467 1.00 42.40 ? 118 MET A CA 1 ATOM 736 C C . MET A 1 104 ? 78.382 107.652 31.080 1.00 45.54 ? 118 MET A C 1 ATOM 737 O O . MET A 1 104 ? 78.671 108.617 30.353 1.00 46.11 ? 118 MET A O 1 ATOM 738 C CB . MET A 1 104 ? 76.558 106.016 30.476 1.00 40.03 ? 118 MET A CB 1 ATOM 739 C CG . MET A 1 104 ? 76.206 104.819 29.625 1.00 39.05 ? 118 MET A CG 1 ATOM 740 S SD . MET A 1 104 ? 74.448 104.648 29.344 1.00 41.35 ? 118 MET A SD 1 ATOM 741 C CE . MET A 1 104 ? 73.951 103.781 30.836 1.00 45.58 ? 118 MET A CE 1 ATOM 742 N N . LYS A 1 105 ? 78.372 107.723 32.412 1.00 45.35 ? 119 LYS A N 1 ATOM 743 C CA . LYS A 1 105 ? 78.729 108.974 33.086 1.00 46.63 ? 119 LYS A CA 1 ATOM 744 C C . LYS A 1 105 ? 80.170 109.423 32.827 1.00 47.24 ? 119 LYS A C 1 ATOM 745 O O . LYS A 1 105 ? 80.428 110.617 32.692 1.00 45.67 ? 119 LYS A O 1 ATOM 746 C CB . LYS A 1 105 ? 78.467 108.892 34.586 1.00 46.34 ? 119 LYS A CB 1 ATOM 747 C CG . LYS A 1 105 ? 77.065 109.313 35.000 1.00 48.85 ? 119 LYS A CG 1 ATOM 748 C CD . LYS A 1 105 ? 76.849 109.053 36.493 1.00 49.88 ? 119 LYS A CD 1 ATOM 749 C CE . LYS A 1 105 ? 77.182 107.613 36.828 1.00 48.87 ? 119 LYS A CE 1 ATOM 750 N NZ . LYS A 1 105 ? 76.932 107.275 38.240 1.00 50.00 ? 119 LYS A NZ 1 ATOM 751 N N . GLU A 1 106 ? 81.108 108.482 32.767 1.00 44.74 ? 120 GLU A N 1 ATOM 752 C CA . GLU A 1 106 ? 82.489 108.847 32.456 1.00 47.50 ? 120 GLU A CA 1 ATOM 753 C C . GLU A 1 106 ? 82.603 109.344 31.022 1.00 52.39 ? 120 GLU A C 1 ATOM 754 O O . GLU A 1 106 ? 83.375 110.274 30.740 1.00 51.25 ? 120 GLU A O 1 ATOM 755 C CB . GLU A 1 106 ? 83.435 107.668 32.680 1.00 46.48 ? 120 GLU A CB 1 ATOM 756 C CG . GLU A 1 106 ? 83.583 107.255 34.136 1.00 49.57 ? 120 GLU A CG 1 ATOM 757 C CD . GLU A 1 106 ? 84.180 108.349 34.999 1.00 54.15 ? 120 GLU A CD 1 ATOM 758 O OE1 . GLU A 1 106 ? 84.999 109.140 34.485 1.00 56.12 ? 120 GLU A OE1 1 ATOM 759 O OE2 . GLU A 1 106 ? 83.836 108.422 36.198 1.00 55.91 ? 120 GLU A OE2 1 ATOM 760 N N . ALA A 1 107 ? 81.839 108.723 30.118 1.00 51.86 ? 121 ALA A N 1 ATOM 761 C CA . ALA A 1 107 ? 81.831 109.128 28.716 1.00 50.38 ? 121 ALA A CA 1 ATOM 762 C C . ALA A 1 107 ? 81.276 110.536 28.614 1.00 51.99 ? 121 ALA A C 1 ATOM 763 O O . ALA A 1 107 ? 81.890 111.408 27.983 1.00 51.73 ? 121 ALA A O 1 ATOM 764 C CB . ALA A 1 107 ? 80.999 108.157 27.873 1.00 44.18 ? 121 ALA A CB 1 ATOM 765 N N . LYS A 1 108 ? 80.127 110.762 29.254 1.00 50.30 ? 122 LYS A N 1 ATOM 766 C CA . LYS A 1 108 ? 79.471 112.066 29.210 1.00 56.50 ? 122 LYS A CA 1 ATOM 767 C C . LYS A 1 108 ? 80.310 113.179 29.866 1.00 61.90 ? 122 LYS A C 1 ATOM 768 O O . LYS A 1 108 ? 80.249 114.343 29.449 1.00 64.09 ? 122 LYS A O 1 ATOM 769 C CB . LYS A 1 108 ? 78.088 111.988 29.852 1.00 59.77 ? 122 LYS A CB 1 ATOM 770 C CG . LYS A 1 108 ? 77.185 113.164 29.502 1.00 63.90 ? 122 LYS A CG 1 ATOM 771 C CD . LYS A 1 108 ? 75.930 113.160 30.365 1.00 66.91 ? 122 LYS A CD 1 ATOM 772 C CE . LYS A 1 108 ? 75.180 114.484 30.257 1.00 69.70 ? 122 LYS A CE 1 ATOM 773 N NZ . LYS A 1 108 ? 74.061 114.578 31.243 1.00 68.03 ? 122 LYS A NZ 1 ATOM 774 N N . LYS A 1 109 ? 81.098 112.830 30.880 1.00 60.34 ? 123 LYS A N 1 ATOM 775 C CA . LYS A 1 109 ? 81.975 113.821 31.513 1.00 62.59 ? 123 LYS A CA 1 ATOM 776 C C . LYS A 1 109 ? 83.038 114.347 30.556 1.00 62.81 ? 123 LYS A C 1 ATOM 777 O O . LYS A 1 109 ? 83.449 115.501 30.656 1.00 61.67 ? 123 LYS A O 1 ATOM 778 C CB . LYS A 1 109 ? 82.664 113.245 32.749 1.00 64.11 ? 123 LYS A CB 1 ATOM 779 C CG . LYS A 1 109 ? 81.908 113.454 34.036 1.00 69.97 ? 123 LYS A CG 1 ATOM 780 C CD . LYS A 1 109 ? 82.794 113.150 35.234 1.00 76.79 ? 123 LYS A CD 1 ATOM 781 C CE . LYS A 1 109 ? 83.399 111.761 35.138 1.00 80.30 ? 123 LYS A CE 1 ATOM 782 N NZ . LYS A 1 109 ? 84.178 111.395 36.362 1.00 84.14 ? 123 LYS A NZ 1 ATOM 783 N N . ARG A 1 110 ? 83.488 113.496 29.639 1.00 58.58 ? 124 ARG A N 1 ATOM 784 C CA . ARG A 1 110 ? 84.556 113.871 28.725 1.00 57.95 ? 124 ARG A CA 1 ATOM 785 C C . ARG A 1 110 ? 83.964 114.484 27.481 1.00 59.18 ? 124 ARG A C 1 ATOM 786 O O . ARG A 1 110 ? 84.543 115.387 26.870 1.00 58.53 ? 124 ARG A O 1 ATOM 787 C CB . ARG A 1 110 ? 85.394 112.645 28.377 1.00 57.23 ? 124 ARG A CB 1 ATOM 788 C CG . ARG A 1 110 ? 86.298 112.232 29.525 1.00 55.53 ? 124 ARG A CG 1 ATOM 789 C CD . ARG A 1 110 ? 86.748 110.798 29.394 1.00 52.81 ? 124 ARG A CD 1 ATOM 790 N NE . ARG A 1 110 ? 87.661 110.465 30.476 1.00 50.52 ? 124 ARG A NE 1 ATOM 791 C CZ . ARG A 1 110 ? 87.276 110.149 31.705 1.00 52.61 ? 124 ARG A CZ 1 ATOM 792 N NH1 . ARG A 1 110 ? 85.974 110.102 32.012 1.00 52.40 ? 124 ARG A NH1 1 ATOM 793 N NH2 . ARG A 1 110 ? 88.188 109.866 32.631 1.00 52.35 ? 124 ARG A NH2 1 ATOM 794 N N . ASN A 1 111 ? 82.791 113.992 27.110 1.00 60.07 ? 125 ASN A N 1 ATOM 795 C CA . ASN A 1 111 ? 82.084 114.537 25.962 1.00 59.40 ? 125 ASN A CA 1 ATOM 796 C C . ASN A 1 111 ? 80.581 114.632 26.214 1.00 60.37 ? 125 ASN A C 1 ATOM 797 O O . ASN A 1 111 ? 79.849 113.645 26.086 1.00 61.17 ? 125 ASN A O 1 ATOM 798 C CB . ASN A 1 111 ? 82.397 113.732 24.705 1.00 57.19 ? 125 ASN A CB 1 ATOM 799 C CG . ASN A 1 111 ? 81.589 114.184 23.508 1.00 59.17 ? 125 ASN A CG 1 ATOM 800 O OD1 . ASN A 1 111 ? 81.000 115.267 23.510 1.00 61.70 ? 125 ASN A OD1 1 ATOM 801 N ND2 . ASN A 1 111 ? 81.555 113.354 22.472 1.00 60.36 ? 125 ASN A ND2 1 ATOM 802 N N . PRO A 1 112 ? 80.117 115.842 26.552 1.00 61.14 ? 126 PRO A N 1 ATOM 803 C CA . PRO A 1 112 ? 78.723 116.133 26.901 1.00 60.74 ? 126 PRO A CA 1 ATOM 804 C C . PRO A 1 112 ? 77.776 115.838 25.753 1.00 59.17 ? 126 PRO A C 1 ATOM 805 O O . PRO A 1 112 ? 76.609 115.533 25.999 1.00 60.69 ? 126 PRO A O 1 ATOM 806 C CB . PRO A 1 112 ? 78.746 117.640 27.184 1.00 60.67 ? 126 PRO A CB 1 ATOM 807 C CG . PRO A 1 112 ? 80.168 117.942 27.510 1.00 62.50 ? 126 PRO A CG 1 ATOM 808 C CD . PRO A 1 112 ? 80.957 117.050 26.611 1.00 61.86 ? 126 PRO A CD 1 ATOM 809 N N . ASP A 1 113 ? 78.273 115.923 24.521 1.00 59.38 ? 127 ASP A N 1 ATOM 810 C CA . ASP A 1 113 ? 77.442 115.688 23.341 1.00 59.65 ? 127 ASP A CA 1 ATOM 811 C C . ASP A 1 113 ? 77.456 114.236 22.858 1.00 53.27 ? 127 ASP A C 1 ATOM 812 O O . ASP A 1 113 ? 76.905 113.927 21.787 1.00 46.62 ? 127 ASP A O 1 ATOM 813 C CB . ASP A 1 113 ? 77.867 116.602 22.189 1.00 64.46 ? 127 ASP A CB 1 ATOM 814 C CG . ASP A 1 113 ? 77.587 118.070 22.467 1.00 71.08 ? 127 ASP A CG 1 ATOM 815 O OD1 . ASP A 1 113 ? 76.431 118.508 22.280 1.00 71.80 ? 127 ASP A OD1 1 ATOM 816 O OD2 . ASP A 1 113 ? 78.530 118.791 22.847 1.00 76.29 ? 127 ASP A OD2 1 ATOM 817 N N . ILE A 1 114 ? 78.075 113.340 23.623 1.00 50.83 ? 128 ILE A N 1 ATOM 818 C CA . ILE A 1 114 ? 78.084 111.931 23.214 1.00 50.37 ? 128 ILE A CA 1 ATOM 819 C C . ILE A 1 114 ? 76.667 111.389 23.061 1.00 48.00 ? 128 ILE A C 1 ATOM 820 O O . ILE A 1 114 ? 75.764 111.805 23.780 1.00 45.98 ? 128 ILE A O 1 ATOM 821 C CB . ILE A 1 114 ? 78.898 111.029 24.174 1.00 49.69 ? 128 ILE A CB 1 ATOM 822 C CG1 . ILE A 1 114 ? 79.108 109.648 23.530 1.00 49.59 ? 128 ILE A CG1 1 ATOM 823 C CG2 . ILE A 1 114 ? 78.224 110.928 25.540 1.00 44.90 ? 128 ILE A CG2 1 ATOM 824 C CD1 . ILE A 1 114 ? 80.247 108.844 24.120 1.00 49.34 ? 128 ILE A CD1 1 ATOM 825 N N . ILE A 1 115 ? 76.467 110.498 22.091 1.00 47.18 ? 129 ILE A N 1 ATOM 826 C CA . ILE A 1 115 ? 75.160 109.898 21.859 1.00 46.46 ? 129 ILE A CA 1 ATOM 827 C C . ILE A 1 115 ? 75.051 108.564 22.615 1.00 45.40 ? 129 ILE A C 1 ATOM 828 O O . ILE A 1 115 ? 75.895 107.678 22.425 1.00 47.00 ? 129 ILE A O 1 ATOM 829 C CB . ILE A 1 115 ? 74.922 109.670 20.335 1.00 42.18 ? 129 ILE A CB 1 ATOM 830 C CG1 . ILE A 1 115 ? 75.006 111.002 19.577 1.00 43.31 ? 129 ILE A CG1 1 ATOM 831 C CG2 . ILE A 1 115 ? 73.587 109.023 20.109 1.00 41.00 ? 129 ILE A CG2 1 ATOM 832 C CD1 . ILE A 1 115 ? 75.073 110.842 18.026 1.00 46.04 ? 129 ILE A CD1 1 ATOM 833 N N . LEU A 1 116 ? 74.023 108.413 23.457 1.00 40.20 ? 130 LEU A N 1 ATOM 834 C CA . LEU A 1 116 ? 73.862 107.202 24.253 1.00 42.74 ? 130 LEU A CA 1 ATOM 835 C C . LEU A 1 116 ? 72.780 106.224 23.734 1.00 41.88 ? 130 LEU A C 1 ATOM 836 O O . LEU A 1 116 ? 71.635 106.619 23.438 1.00 42.03 ? 130 LEU A O 1 ATOM 837 C CB . LEU A 1 116 ? 73.574 107.563 25.726 1.00 44.26 ? 130 LEU A CB 1 ATOM 838 C CG . LEU A 1 116 ? 74.604 108.406 26.479 1.00 43.23 ? 130 LEU A CG 1 ATOM 839 C CD1 . LEU A 1 116 ? 74.156 108.681 27.928 1.00 40.56 ? 130 LEU A CD1 1 ATOM 840 C CD2 . LEU A 1 116 ? 75.970 107.737 26.462 1.00 40.99 ? 130 LEU A CD2 1 ATOM 841 N N . MET A 1 117 ? 73.137 104.939 23.651 1.00 37.77 ? 131 MET A N 1 ATOM 842 C CA . MET A 1 117 ? 72.210 103.909 23.197 1.00 36.38 ? 131 MET A CA 1 ATOM 843 C C . MET A 1 117 ? 72.158 102.735 24.166 1.00 35.52 ? 131 MET A C 1 ATOM 844 O O . MET A 1 117 ? 73.198 102.333 24.715 1.00 40.34 ? 131 MET A O 1 ATOM 845 C CB . MET A 1 117 ? 72.652 103.352 21.843 1.00 36.58 ? 131 MET A CB 1 ATOM 846 C CG . MET A 1 117 ? 73.051 104.395 20.846 1.00 38.76 ? 131 MET A CG 1 ATOM 847 S SD . MET A 1 117 ? 73.578 103.626 19.285 1.00 43.25 ? 131 MET A SD 1 ATOM 848 C CE . MET A 1 117 ? 72.135 102.616 18.869 1.00 39.55 ? 131 MET A CE 1 ATOM 849 N N . GLY A 1 118 ? 70.969 102.167 24.329 1.00 34.47 ? 132 GLY A N 1 ATOM 850 C CA . GLY A 1 118 ? 70.764 100.965 25.145 1.00 36.01 ? 132 GLY A CA 1 ATOM 851 C C . GLY A 1 118 ? 70.103 99.837 24.359 1.00 36.01 ? 132 GLY A C 1 ATOM 852 O O . GLY A 1 118 ? 69.242 100.096 23.506 1.00 34.78 ? 132 GLY A O 1 ATOM 853 N N . LEU A 1 119 ? 70.509 98.590 24.616 1.00 33.62 ? 133 LEU A N 1 ATOM 854 C CA . LEU A 1 119 ? 69.891 97.431 23.951 1.00 31.45 ? 133 LEU A CA 1 ATOM 855 C C . LEU A 1 119 ? 69.930 96.175 24.820 1.00 30.76 ? 133 LEU A C 1 ATOM 856 O O . LEU A 1 119 ? 70.973 95.829 25.384 1.00 37.79 ? 133 LEU A O 1 ATOM 857 C CB . LEU A 1 119 ? 70.588 97.160 22.611 1.00 31.98 ? 133 LEU A CB 1 ATOM 858 C CG . LEU A 1 119 ? 70.269 95.907 21.791 1.00 39.29 ? 133 LEU A CG 1 ATOM 859 C CD1 . LEU A 1 119 ? 68.836 95.892 21.218 1.00 31.92 ? 133 LEU A CD1 1 ATOM 860 C CD2 . LEU A 1 119 ? 71.274 95.787 20.661 1.00 42.55 ? 133 LEU A CD2 1 ATOM 861 N N . PRO A 1 120 ? 68.797 95.474 24.928 1.00 30.98 ? 134 PRO A N 1 ATOM 862 C CA . PRO A 1 120 ? 68.839 94.217 25.688 1.00 31.81 ? 134 PRO A CA 1 ATOM 863 C C . PRO A 1 120 ? 69.333 93.026 24.866 1.00 34.67 ? 134 PRO A C 1 ATOM 864 O O . PRO A 1 120 ? 69.020 92.900 23.670 1.00 33.70 ? 134 PRO A O 1 ATOM 865 C CB . PRO A 1 120 ? 67.369 93.978 26.073 1.00 32.44 ? 134 PRO A CB 1 ATOM 866 C CG . PRO A 1 120 ? 66.631 95.213 25.671 1.00 28.32 ? 134 PRO A CG 1 ATOM 867 C CD . PRO A 1 120 ? 67.425 95.860 24.575 1.00 29.18 ? 134 PRO A CD 1 ATOM 868 N N . TRP A 1 121 ? 70.098 92.160 25.524 1.00 33.93 ? 135 TRP A N 1 ATOM 869 C CA . TRP A 1 121 ? 70.540 90.878 24.985 1.00 29.15 ? 135 TRP A CA 1 ATOM 870 C C . TRP A 1 121 ? 69.719 89.773 25.656 1.00 31.91 ? 135 TRP A C 1 ATOM 871 O O . TRP A 1 121 ? 69.188 88.885 24.990 1.00 34.11 ? 135 TRP A O 1 ATOM 872 C CB . TRP A 1 121 ? 72.028 90.663 25.327 1.00 30.40 ? 135 TRP A CB 1 ATOM 873 C CG . TRP A 1 121 ? 73.071 91.048 24.282 1.00 30.90 ? 135 TRP A CG 1 ATOM 874 C CD1 . TRP A 1 121 ? 73.891 90.194 23.598 1.00 31.25 ? 135 TRP A CD1 1 ATOM 875 C CD2 . TRP A 1 121 ? 73.445 92.380 23.862 1.00 35.14 ? 135 TRP A CD2 1 ATOM 876 N NE1 . TRP A 1 121 ? 74.727 90.909 22.757 1.00 37.17 ? 135 TRP A NE1 1 ATOM 877 C CE2 . TRP A 1 121 ? 74.467 92.246 22.898 1.00 32.34 ? 135 TRP A CE2 1 ATOM 878 C CE3 . TRP A 1 121 ? 73.003 93.670 24.205 1.00 31.71 ? 135 TRP A CE3 1 ATOM 879 C CZ2 . TRP A 1 121 ? 75.062 93.355 22.275 1.00 40.71 ? 135 TRP A CZ2 1 ATOM 880 C CZ3 . TRP A 1 121 ? 73.572 94.761 23.576 1.00 32.61 ? 135 TRP A CZ3 1 ATOM 881 C CH2 . TRP A 1 121 ? 74.599 94.600 22.628 1.00 33.38 ? 135 TRP A CH2 1 ATOM 882 N N . SER A 1 122 ? 69.611 89.822 26.986 1.00 29.44 ? 136 SER A N 1 ATOM 883 C CA . SER A 1 122 ? 68.839 88.834 27.737 1.00 27.43 ? 136 SER A CA 1 ATOM 884 C C . SER A 1 122 ? 67.844 89.554 28.633 1.00 29.98 ? 136 SER A C 1 ATOM 885 O O . SER A 1 122 ? 67.879 90.774 28.716 1.00 33.13 ? 136 SER A O 1 ATOM 886 C CB . SER A 1 122 ? 69.768 87.964 28.586 1.00 28.80 ? 136 SER A CB 1 ATOM 887 O OG . SER A 1 122 ? 70.334 88.700 29.664 1.00 34.78 ? 136 SER A OG 1 ATOM 888 N N . PHE A 1 123 ? 66.948 88.814 29.290 1.00 27.10 ? 137 PHE A N 1 ATOM 889 C CA . PHE A 1 123 ? 65.969 89.413 30.202 1.00 26.80 ? 137 PHE A CA 1 ATOM 890 C C . PHE A 1 123 ? 65.869 88.512 31.422 1.00 32.34 ? 137 PHE A C 1 ATOM 891 O O . PHE A 1 123 ? 66.123 87.303 31.317 1.00 27.73 ? 137 PHE A O 1 ATOM 892 C CB . PHE A 1 123 ? 64.577 89.487 29.547 1.00 25.73 ? 137 PHE A CB 1 ATOM 893 C CG . PHE A 1 123 ? 64.515 90.343 28.303 1.00 32.57 ? 137 PHE A CG 1 ATOM 894 C CD1 . PHE A 1 123 ? 64.259 91.701 28.388 1.00 30.73 ? 137 PHE A CD1 1 ATOM 895 C CD2 . PHE A 1 123 ? 64.689 89.780 27.046 1.00 34.01 ? 137 PHE A CD2 1 ATOM 896 C CE1 . PHE A 1 123 ? 64.171 92.500 27.227 1.00 27.99 ? 137 PHE A CE1 1 ATOM 897 C CE2 . PHE A 1 123 ? 64.621 90.565 25.880 1.00 33.14 ? 137 PHE A CE2 1 ATOM 898 C CZ . PHE A 1 123 ? 64.360 91.925 25.972 1.00 32.90 ? 137 PHE A CZ 1 ATOM 899 N N . PRO A 1 124 ? 65.471 89.079 32.579 1.00 32.29 ? 138 PRO A N 1 ATOM 900 C CA . PRO A 1 124 ? 65.223 88.225 33.754 1.00 29.33 ? 138 PRO A CA 1 ATOM 901 C C . PRO A 1 124 ? 64.060 87.278 33.495 1.00 30.37 ? 138 PRO A C 1 ATOM 902 O O . PRO A 1 124 ? 63.096 87.642 32.798 1.00 29.41 ? 138 PRO A O 1 ATOM 903 C CB . PRO A 1 124 ? 64.866 89.233 34.859 1.00 29.23 ? 138 PRO A CB 1 ATOM 904 C CG . PRO A 1 124 ? 65.503 90.514 34.404 1.00 32.41 ? 138 PRO A CG 1 ATOM 905 C CD . PRO A 1 124 ? 65.332 90.509 32.899 1.00 29.36 ? 138 PRO A CD 1 ATOM 906 N N . GLY A 1 125 ? 64.145 86.069 34.049 1.00 28.87 ? 139 GLY A N 1 ATOM 907 C CA . GLY A 1 125 ? 63.158 85.048 33.771 1.00 31.53 ? 139 GLY A CA 1 ATOM 908 C C . GLY A 1 125 ? 61.734 85.421 34.137 1.00 30.62 ? 139 GLY A C 1 ATOM 909 O O . GLY A 1 125 ? 60.788 84.980 33.477 1.00 29.23 ? 139 GLY A O 1 ATOM 910 N N . TRP A 1 126 ? 61.565 86.245 35.166 1.00 28.35 ? 140 TRP A N 1 ATOM 911 C CA . TRP A 1 126 ? 60.216 86.515 35.663 1.00 30.27 ? 140 TRP A CA 1 ATOM 912 C C . TRP A 1 126 ? 59.367 87.276 34.628 1.00 33.65 ? 140 TRP A C 1 ATOM 913 O O . TRP A 1 126 ? 58.136 87.200 34.655 1.00 32.14 ? 140 TRP A O 1 ATOM 914 C CB . TRP A 1 126 ? 60.266 87.253 37.002 1.00 30.80 ? 140 TRP A CB 1 ATOM 915 C CG . TRP A 1 126 ? 60.856 88.645 36.933 1.00 34.03 ? 140 TRP A CG 1 ATOM 916 C CD1 . TRP A 1 126 ? 62.167 88.994 37.097 1.00 34.84 ? 140 TRP A CD1 1 ATOM 917 C CD2 . TRP A 1 126 ? 60.138 89.877 36.731 1.00 34.23 ? 140 TRP A CD2 1 ATOM 918 N NE1 . TRP A 1 126 ? 62.316 90.363 36.992 1.00 35.19 ? 140 TRP A NE1 1 ATOM 919 C CE2 . TRP A 1 126 ? 61.085 90.927 36.768 1.00 37.14 ? 140 TRP A CE2 1 ATOM 920 C CE3 . TRP A 1 126 ? 58.790 90.186 36.532 1.00 32.17 ? 140 TRP A CE3 1 ATOM 921 C CZ2 . TRP A 1 126 ? 60.723 92.276 36.587 1.00 38.49 ? 140 TRP A CZ2 1 ATOM 922 C CZ3 . TRP A 1 126 ? 58.434 91.521 36.351 1.00 37.88 ? 140 TRP A CZ3 1 ATOM 923 C CH2 . TRP A 1 126 ? 59.397 92.551 36.391 1.00 37.65 ? 140 TRP A CH2 1 ATOM 924 N N . LEU A 1 127 ? 60.023 87.968 33.700 1.00 31.88 ? 141 LEU A N 1 ATOM 925 C CA . LEU A 1 127 ? 59.311 88.668 32.630 1.00 36.90 ? 141 LEU A CA 1 ATOM 926 C C . LEU A 1 127 ? 58.590 87.704 31.693 1.00 33.33 ? 141 LEU A C 1 ATOM 927 O O . LEU A 1 127 ? 57.696 88.109 30.935 1.00 36.90 ? 141 LEU A O 1 ATOM 928 C CB . LEU A 1 127 ? 60.273 89.505 31.770 1.00 35.63 ? 141 LEU A CB 1 ATOM 929 C CG . LEU A 1 127 ? 61.005 90.721 32.334 1.00 39.62 ? 141 LEU A CG 1 ATOM 930 C CD1 . LEU A 1 127 ? 61.832 91.412 31.220 1.00 38.79 ? 141 LEU A CD1 1 ATOM 931 C CD2 . LEU A 1 127 ? 60.034 91.707 32.949 1.00 37.75 ? 141 LEU A CD2 1 ATOM 932 N N . GLY A 1 128 ? 59.012 86.446 31.699 1.00 29.87 ? 142 GLY A N 1 ATOM 933 C CA . GLY A 1 128 ? 58.510 85.482 30.730 1.00 32.74 ? 142 GLY A CA 1 ATOM 934 C C . GLY A 1 128 ? 57.263 84.777 31.235 1.00 35.15 ? 142 GLY A C 1 ATOM 935 O O . GLY A 1 128 ? 56.620 84.055 30.477 1.00 36.94 ? 142 GLY A O 1 ATOM 936 N N . LYS A 1 129 ? 56.943 84.996 32.514 1.00 35.79 ? 143 LYS A N 1 ATOM 937 C CA . LYS A 1 129 ? 55.725 84.488 33.152 1.00 43.71 ? 143 LYS A CA 1 ATOM 938 C C . LYS A 1 129 ? 55.496 82.999 32.893 1.00 48.09 ? 143 LYS A C 1 ATOM 939 O O . LYS A 1 129 ? 54.373 82.580 32.616 1.00 50.26 ? 143 LYS A O 1 ATOM 940 C CB . LYS A 1 129 ? 54.490 85.310 32.727 1.00 45.95 ? 143 LYS A CB 1 ATOM 941 C CG . LYS A 1 129 ? 54.407 86.719 33.341 1.00 51.24 ? 143 LYS A CG 1 ATOM 942 C CD . LYS A 1 129 ? 54.418 86.660 34.877 1.00 58.08 ? 143 LYS A CD 1 ATOM 943 C CE . LYS A 1 129 ? 54.414 88.062 35.517 1.00 63.02 ? 143 LYS A CE 1 ATOM 944 N NZ . LYS A 1 129 ? 54.644 88.063 37.001 1.00 63.24 ? 143 LYS A NZ 1 ATOM 945 N N . GLY A 1 130 ? 56.557 82.203 32.980 1.00 48.59 ? 144 GLY A N 1 ATOM 946 C CA . GLY A 1 130 ? 56.423 80.783 32.725 1.00 51.64 ? 144 GLY A CA 1 ATOM 947 C C . GLY A 1 130 ? 57.117 80.299 31.461 1.00 56.86 ? 144 GLY A C 1 ATOM 948 O O . GLY A 1 130 ? 57.355 79.097 31.313 1.00 59.96 ? 144 GLY A O 1 ATOM 949 N N . PHE A 1 131 ? 57.437 81.212 30.543 1.00 56.01 ? 145 PHE A N 1 ATOM 950 C CA . PHE A 1 131 ? 58.167 80.840 29.323 1.00 55.14 ? 145 PHE A CA 1 ATOM 951 C C . PHE A 1 131 ? 59.472 81.612 29.174 1.00 52.75 ? 145 PHE A C 1 ATOM 952 O O . PHE A 1 131 ? 59.646 82.679 29.766 1.00 51.77 ? 145 PHE A O 1 ATOM 953 C CB . PHE A 1 131 ? 57.301 81.068 28.089 1.00 59.49 ? 145 PHE A CB 1 ATOM 954 C CG . PHE A 1 131 ? 55.916 80.515 28.219 1.00 63.83 ? 145 PHE A CG 1 ATOM 955 C CD1 . PHE A 1 131 ? 55.659 79.182 27.929 1.00 66.28 ? 145 PHE A CD1 1 ATOM 956 C CD2 . PHE A 1 131 ? 54.865 81.326 28.628 1.00 65.31 ? 145 PHE A CD2 1 ATOM 957 C CE1 . PHE A 1 131 ? 54.375 78.665 28.051 1.00 67.15 ? 145 PHE A CE1 1 ATOM 958 C CE2 . PHE A 1 131 ? 53.579 80.820 28.749 1.00 67.02 ? 145 PHE A CE2 1 ATOM 959 C CZ . PHE A 1 131 ? 53.334 79.486 28.460 1.00 67.53 ? 145 PHE A CZ 1 ATOM 960 N N . SER A 1 132 ? 60.399 81.070 28.391 1.00 51.46 ? 146 SER A N 1 ATOM 961 C CA . SER A 1 132 ? 61.633 81.788 28.091 1.00 49.71 ? 146 SER A CA 1 ATOM 962 C C . SER A 1 132 ? 61.379 82.678 26.873 1.00 45.44 ? 146 SER A C 1 ATOM 963 O O . SER A 1 132 ? 62.020 82.508 25.833 1.00 47.70 ? 146 SER A O 1 ATOM 964 C CB . SER A 1 132 ? 62.787 80.800 27.827 1.00 51.21 ? 146 SER A CB 1 ATOM 965 O OG . SER A 1 132 ? 64.037 81.455 27.587 1.00 52.66 ? 146 SER A OG 1 ATOM 966 N N . TRP A 1 133 ? 60.456 83.635 27.005 1.00 39.67 ? 147 TRP A N 1 ATOM 967 C CA . TRP A 1 133 ? 60.040 84.461 25.869 1.00 38.45 ? 147 TRP A CA 1 ATOM 968 C C . TRP A 1 133 ? 59.571 85.839 26.317 1.00 37.23 ? 147 TRP A C 1 ATOM 969 O O . TRP A 1 133 ? 58.659 85.944 27.144 1.00 40.30 ? 147 TRP A O 1 ATOM 970 C CB . TRP A 1 133 ? 58.899 83.764 25.135 1.00 36.61 ? 147 TRP A CB 1 ATOM 971 C CG . TRP A 1 133 ? 58.593 84.292 23.777 1.00 35.95 ? 147 TRP A CG 1 ATOM 972 C CD1 . TRP A 1 133 ? 57.405 84.816 23.351 1.00 37.92 ? 147 TRP A CD1 1 ATOM 973 C CD2 . TRP A 1 133 ? 59.463 84.290 22.633 1.00 33.79 ? 147 TRP A CD2 1 ATOM 974 N NE1 . TRP A 1 133 ? 57.490 85.155 22.020 1.00 38.97 ? 147 TRP A NE1 1 ATOM 975 C CE2 . TRP A 1 133 ? 58.741 84.841 21.556 1.00 35.42 ? 147 TRP A CE2 1 ATOM 976 C CE3 . TRP A 1 133 ? 60.778 83.868 22.416 1.00 33.74 ? 147 TRP A CE3 1 ATOM 977 C CZ2 . TRP A 1 133 ? 59.298 84.994 20.277 1.00 33.23 ? 147 TRP A CZ2 1 ATOM 978 C CZ3 . TRP A 1 133 ? 61.328 84.018 21.142 1.00 32.58 ? 147 TRP A CZ3 1 ATOM 979 C CH2 . TRP A 1 133 ? 60.589 84.580 20.098 1.00 35.50 ? 147 TRP A CH2 1 ATOM 980 N N . PRO A 1 134 ? 60.168 86.900 25.744 1.00 34.74 ? 148 PRO A N 1 ATOM 981 C CA . PRO A 1 134 ? 59.947 88.295 26.183 1.00 33.68 ? 148 PRO A CA 1 ATOM 982 C C . PRO A 1 134 ? 58.675 88.922 25.600 1.00 32.71 ? 148 PRO A C 1 ATOM 983 O O . PRO A 1 134 ? 58.293 90.047 25.974 1.00 32.19 ? 148 PRO A O 1 ATOM 984 C CB . PRO A 1 134 ? 61.175 89.022 25.648 1.00 32.04 ? 148 PRO A CB 1 ATOM 985 C CG . PRO A 1 134 ? 61.509 88.256 24.354 1.00 31.92 ? 148 PRO A CG 1 ATOM 986 C CD . PRO A 1 134 ? 61.189 86.799 24.683 1.00 33.82 ? 148 PRO A CD 1 ATOM 987 N N . TYR A 1 135 ? 58.021 88.206 24.691 1.00 28.18 ? 149 TYR A N 1 ATOM 988 C CA . TYR A 1 135 ? 56.839 88.762 24.044 1.00 33.66 ? 149 TYR A CA 1 ATOM 989 C C . TYR A 1 135 ? 55.551 88.109 24.557 1.00 37.53 ? 149 TYR A C 1 ATOM 990 O O . TYR A 1 135 ? 54.507 88.170 23.911 1.00 40.36 ? 149 TYR A O 1 ATOM 991 C CB . TYR A 1 135 ? 56.962 88.656 22.521 1.00 33.06 ? 149 TYR A CB 1 ATOM 992 C CG . TYR A 1 135 ? 58.222 89.312 21.951 1.00 31.07 ? 149 TYR A CG 1 ATOM 993 C CD1 . TYR A 1 135 ? 58.600 90.586 22.321 1.00 26.14 ? 149 TYR A CD1 1 ATOM 994 C CD2 . TYR A 1 135 ? 59.012 88.646 21.013 1.00 33.08 ? 149 TYR A CD2 1 ATOM 995 C CE1 . TYR A 1 135 ? 59.758 91.190 21.781 1.00 29.78 ? 149 TYR A CE1 1 ATOM 996 C CE2 . TYR A 1 135 ? 60.153 89.231 20.474 1.00 31.80 ? 149 TYR A CE2 1 ATOM 997 C CZ . TYR A 1 135 ? 60.524 90.495 20.867 1.00 29.74 ? 149 TYR A CZ 1 ATOM 998 O OH . TYR A 1 135 ? 61.656 91.070 20.322 1.00 34.31 ? 149 TYR A OH 1 ATOM 999 N N . VAL A 1 136 ? 55.622 87.489 25.730 1.00 39.36 ? 150 VAL A N 1 ATOM 1000 C CA . VAL A 1 136 ? 54.423 86.874 26.315 1.00 40.53 ? 150 VAL A CA 1 ATOM 1001 C C . VAL A 1 136 ? 53.479 87.972 26.809 1.00 36.53 ? 150 VAL A C 1 ATOM 1002 O O . VAL A 1 136 ? 52.273 87.933 26.581 1.00 35.88 ? 150 VAL A O 1 ATOM 1003 C CB . VAL A 1 136 ? 54.784 85.893 27.458 1.00 41.00 ? 150 VAL A CB 1 ATOM 1004 C CG1 . VAL A 1 136 ? 53.524 85.395 28.175 1.00 44.65 ? 150 VAL A CG1 1 ATOM 1005 C CG2 . VAL A 1 136 ? 55.558 84.714 26.897 1.00 37.48 ? 150 VAL A CG2 1 ATOM 1006 N N . ASN A 1 137 ? 54.043 88.964 27.480 1.00 34.72 ? 151 ASN A N 1 ATOM 1007 C CA . ASN A 1 137 ? 53.275 90.120 27.921 1.00 33.63 ? 151 ASN A CA 1 ATOM 1008 C C . ASN A 1 137 ? 54.036 91.345 27.430 1.00 30.52 ? 151 ASN A C 1 ATOM 1009 O O . ASN A 1 137 ? 55.030 91.741 28.039 1.00 27.76 ? 151 ASN A O 1 ATOM 1010 C CB . ASN A 1 137 ? 53.138 90.115 29.467 1.00 40.88 ? 151 ASN A CB 1 ATOM 1011 C CG . ASN A 1 137 ? 52.288 91.281 30.007 1.00 39.02 ? 151 ASN A CG 1 ATOM 1012 O OD1 . ASN A 1 137 ? 52.250 92.378 29.427 1.00 37.74 ? 151 ASN A OD1 1 ATOM 1013 N ND2 . ASN A 1 137 ? 51.625 91.050 31.140 1.00 37.41 ? 151 ASN A ND2 1 ATOM 1014 N N . LEU A 1 138 ? 53.574 91.918 26.319 1.00 32.43 ? 152 LEU A N 1 ATOM 1015 C CA . LEU A 1 138 ? 54.246 93.032 25.662 1.00 34.68 ? 152 LEU A CA 1 ATOM 1016 C C . LEU A 1 138 ? 54.388 94.238 26.581 1.00 31.35 ? 152 LEU A C 1 ATOM 1017 O O . LEU A 1 138 ? 55.448 94.860 26.629 1.00 29.61 ? 152 LEU A O 1 ATOM 1018 C CB . LEU A 1 138 ? 53.496 93.452 24.393 1.00 30.65 ? 152 LEU A CB 1 ATOM 1019 C CG . LEU A 1 138 ? 53.397 92.371 23.316 1.00 36.06 ? 152 LEU A CG 1 ATOM 1020 C CD1 . LEU A 1 138 ? 52.687 92.906 22.078 1.00 36.33 ? 152 LEU A CD1 1 ATOM 1021 C CD2 . LEU A 1 138 ? 54.774 91.830 22.961 1.00 37.04 ? 152 LEU A CD2 1 ATOM 1022 N N . GLN A 1 139 ? 53.323 94.579 27.299 1.00 31.94 ? 153 GLN A N 1 ATOM 1023 C CA . GLN A 1 139 ? 53.386 95.745 28.184 1.00 33.97 ? 153 GLN A CA 1 ATOM 1024 C C . GLN A 1 139 ? 54.403 95.543 29.307 1.00 31.57 ? 153 GLN A C 1 ATOM 1025 O O . GLN A 1 139 ? 55.141 96.478 29.675 1.00 31.97 ? 153 GLN A O 1 ATOM 1026 C CB . GLN A 1 139 ? 52.005 96.100 28.760 1.00 39.85 ? 153 GLN A CB 1 ATOM 1027 C CG . GLN A 1 139 ? 52.061 97.397 29.567 1.00 49.40 ? 153 GLN A CG 1 ATOM 1028 C CD . GLN A 1 139 ? 50.770 97.744 30.297 1.00 53.75 ? 153 GLN A CD 1 ATOM 1029 O OE1 . GLN A 1 139 ? 49.823 96.953 30.333 1.00 54.26 ? 153 GLN A OE1 1 ATOM 1030 N NE2 . GLN A 1 139 ? 50.730 98.942 30.884 1.00 53.21 ? 153 GLN A NE2 1 ATOM 1031 N N . LEU A 1 140 ? 54.462 94.329 29.850 1.00 29.49 ? 154 LEU A N 1 ATOM 1032 C CA . LEU A 1 140 ? 55.422 94.049 30.937 1.00 30.10 ? 154 LEU A CA 1 ATOM 1033 C C . LEU A 1 140 ? 56.865 94.204 30.480 1.00 26.78 ? 154 LEU A C 1 ATOM 1034 O O . LEU A 1 140 ? 57.697 94.808 31.176 1.00 28.95 ? 154 LEU A O 1 ATOM 1035 C CB . LEU A 1 140 ? 55.199 92.635 31.502 1.00 30.93 ? 154 LEU A CB 1 ATOM 1036 C CG . LEU A 1 140 ? 56.157 92.216 32.634 1.00 32.71 ? 154 LEU A CG 1 ATOM 1037 C CD1 . LEU A 1 140 ? 56.099 93.168 33.815 1.00 36.20 ? 154 LEU A CD1 1 ATOM 1038 C CD2 . LEU A 1 140 ? 55.842 90.799 33.098 1.00 31.22 ? 154 LEU A CD2 1 ATOM 1039 N N . THR A 1 141 ? 57.185 93.649 29.314 1.00 25.15 ? 155 THR A N 1 ATOM 1040 C CA . THR A 1 141 ? 58.547 93.781 28.809 1.00 31.64 ? 155 THR A CA 1 ATOM 1041 C C . THR A 1 141 ? 58.860 95.242 28.462 1.00 32.25 ? 155 THR A C 1 ATOM 1042 O O . THR A 1 141 ? 59.962 95.725 28.711 1.00 33.83 ? 155 THR A O 1 ATOM 1043 C CB . THR A 1 141 ? 58.769 92.885 27.567 1.00 33.45 ? 155 THR A CB 1 ATOM 1044 O OG1 . THR A 1 141 ? 58.620 91.498 27.940 1.00 30.87 ? 155 THR A OG1 1 ATOM 1045 C CG2 . THR A 1 141 ? 60.154 93.140 26.978 1.00 27.65 ? 155 THR A CG2 1 ATOM 1046 N N . ALA A 1 142 ? 57.899 95.953 27.885 1.00 31.74 ? 156 ALA A N 1 ATOM 1047 C CA . ALA A 1 142 ? 58.144 97.365 27.581 1.00 33.73 ? 156 ALA A CA 1 ATOM 1048 C C . ALA A 1 142 ? 58.296 98.177 28.870 1.00 33.78 ? 156 ALA A C 1 ATOM 1049 O O . ALA A 1 142 ? 59.110 99.099 28.936 1.00 34.78 ? 156 ALA A O 1 ATOM 1050 C CB . ALA A 1 142 ? 57.031 97.939 26.675 1.00 29.94 ? 156 ALA A CB 1 ATOM 1051 N N . TYR A 1 143 ? 57.523 97.819 29.892 1.00 32.79 ? 157 TYR A N 1 ATOM 1052 C CA . TYR A 1 143 ? 57.597 98.484 31.199 1.00 31.90 ? 157 TYR A CA 1 ATOM 1053 C C . TYR A 1 143 ? 58.985 98.327 31.799 1.00 30.57 ? 157 TYR A C 1 ATOM 1054 O O . TYR A 1 143 ? 59.570 99.282 32.334 1.00 27.51 ? 157 TYR A O 1 ATOM 1055 C CB . TYR A 1 143 ? 56.552 97.859 32.132 1.00 35.47 ? 157 TYR A CB 1 ATOM 1056 C CG . TYR A 1 143 ? 56.612 98.268 33.594 1.00 45.14 ? 157 TYR A CG 1 ATOM 1057 C CD1 . TYR A 1 143 ? 55.879 99.358 34.060 1.00 51.00 ? 157 TYR A CD1 1 ATOM 1058 C CD2 . TYR A 1 143 ? 57.365 97.538 34.520 1.00 48.26 ? 157 TYR A CD2 1 ATOM 1059 C CE1 . TYR A 1 143 ? 55.906 99.732 35.400 1.00 54.02 ? 157 TYR A CE1 1 ATOM 1060 C CE2 . TYR A 1 143 ? 57.400 97.905 35.874 1.00 53.20 ? 157 TYR A CE2 1 ATOM 1061 C CZ . TYR A 1 143 ? 56.665 99.002 36.301 1.00 56.31 ? 157 TYR A CZ 1 ATOM 1062 O OH . TYR A 1 143 ? 56.683 99.378 37.628 1.00 63.08 ? 157 TYR A OH 1 ATOM 1063 N N . TYR A 1 144 ? 59.510 97.108 31.728 1.00 29.64 ? 158 TYR A N 1 ATOM 1064 C CA . TYR A 1 144 ? 60.871 96.831 32.189 1.00 31.35 ? 158 TYR A CA 1 ATOM 1065 C C . TYR A 1 144 ? 61.923 97.681 31.452 1.00 30.30 ? 158 TYR A C 1 ATOM 1066 O O . TYR A 1 144 ? 62.798 98.294 32.078 1.00 29.83 ? 158 TYR A O 1 ATOM 1067 C CB . TYR A 1 144 ? 61.160 95.340 31.998 1.00 25.51 ? 158 TYR A CB 1 ATOM 1068 C CG . TYR A 1 144 ? 62.616 94.932 32.139 1.00 33.87 ? 158 TYR A CG 1 ATOM 1069 C CD1 . TYR A 1 144 ? 63.141 94.546 33.368 1.00 30.50 ? 158 TYR A CD1 1 ATOM 1070 C CD2 . TYR A 1 144 ? 63.445 94.874 31.030 1.00 28.64 ? 158 TYR A CD2 1 ATOM 1071 C CE1 . TYR A 1 144 ? 64.463 94.131 33.472 1.00 31.46 ? 158 TYR A CE1 1 ATOM 1072 C CE2 . TYR A 1 144 ? 64.748 94.475 31.126 1.00 32.19 ? 158 TYR A CE2 1 ATOM 1073 C CZ . TYR A 1 144 ? 65.260 94.097 32.343 1.00 33.69 ? 158 TYR A CZ 1 ATOM 1074 O OH . TYR A 1 144 ? 66.590 93.708 32.411 1.00 34.72 ? 158 TYR A OH 1 ATOM 1075 N N . VAL A 1 145 ? 61.861 97.687 30.122 1.00 30.00 ? 159 VAL A N 1 ATOM 1076 C CA . VAL A 1 145 ? 62.820 98.465 29.353 1.00 27.80 ? 159 VAL A CA 1 ATOM 1077 C C . VAL A 1 145 ? 62.697 99.948 29.664 1.00 28.54 ? 159 VAL A C 1 ATOM 1078 O O . VAL A 1 145 ? 63.697 100.634 29.841 1.00 33.37 ? 159 VAL A O 1 ATOM 1079 C CB . VAL A 1 145 ? 62.679 98.255 27.820 1.00 33.05 ? 159 VAL A CB 1 ATOM 1080 C CG1 . VAL A 1 145 ? 63.744 99.051 27.104 1.00 28.56 ? 159 VAL A CG1 1 ATOM 1081 C CG2 . VAL A 1 145 ? 62.832 96.782 27.471 1.00 26.93 ? 159 VAL A CG2 1 ATOM 1082 N N . VAL A 1 146 ? 61.473 100.458 29.706 1.00 36.35 ? 160 VAL A N 1 ATOM 1083 C CA . VAL A 1 146 ? 61.317 101.883 29.905 1.00 35.15 ? 160 VAL A CA 1 ATOM 1084 C C . VAL A 1 146 ? 61.778 102.301 31.306 1.00 32.95 ? 160 VAL A C 1 ATOM 1085 O O . VAL A 1 146 ? 62.394 103.359 31.443 1.00 33.86 ? 160 VAL A O 1 ATOM 1086 C CB . VAL A 1 146 ? 59.905 102.357 29.591 1.00 35.57 ? 160 VAL A CB 1 ATOM 1087 C CG1 . VAL A 1 146 ? 59.750 103.818 30.008 1.00 34.28 ? 160 VAL A CG1 1 ATOM 1088 C CG2 . VAL A 1 146 ? 59.653 102.211 28.109 1.00 35.42 ? 160 VAL A CG2 1 ATOM 1089 N N . ARG A 1 147 ? 61.525 101.465 32.320 1.00 32.89 ? 161 ARG A N 1 ATOM 1090 C CA . ARG A 1 147 ? 62.092 101.689 33.680 1.00 36.82 ? 161 ARG A CA 1 ATOM 1091 C C . ARG A 1 147 ? 63.561 102.012 33.612 1.00 33.07 ? 161 ARG A C 1 ATOM 1092 O O . ARG A 1 147 ? 64.048 102.883 34.337 1.00 37.84 ? 161 ARG A O 1 ATOM 1093 C CB . ARG A 1 147 ? 61.989 100.437 34.581 1.00 41.49 ? 161 ARG A CB 1 ATOM 1094 C CG . ARG A 1 147 ? 60.674 100.173 35.276 1.00 49.88 ? 161 ARG A CG 1 ATOM 1095 C CD . ARG A 1 147 ? 60.089 101.420 35.852 1.00 56.54 ? 161 ARG A CD 1 ATOM 1096 N NE . ARG A 1 147 ? 59.043 101.907 34.964 1.00 61.48 ? 161 ARG A NE 1 ATOM 1097 C CZ . ARG A 1 147 ? 58.424 103.073 35.100 1.00 66.43 ? 161 ARG A CZ 1 ATOM 1098 N NH1 . ARG A 1 147 ? 58.747 103.894 36.101 1.00 69.01 ? 161 ARG A NH1 1 ATOM 1099 N NH2 . ARG A 1 147 ? 57.483 103.414 34.229 1.00 67.12 ? 161 ARG A NH2 1 ATOM 1100 N N . TRP A 1 148 ? 64.288 101.271 32.779 1.00 30.26 ? 162 TRP A N 1 ATOM 1101 C CA . TRP A 1 148 ? 65.732 101.459 32.671 1.00 31.12 ? 162 TRP A CA 1 ATOM 1102 C C . TRP A 1 148 ? 66.053 102.855 32.145 1.00 38.98 ? 162 TRP A C 1 ATOM 1103 O O . TRP A 1 148 ? 67.013 103.490 32.592 1.00 39.07 ? 162 TRP A O 1 ATOM 1104 C CB . TRP A 1 148 ? 66.350 100.407 31.734 1.00 30.81 ? 162 TRP A CB 1 ATOM 1105 C CG . TRP A 1 148 ? 67.896 100.424 31.691 1.00 32.74 ? 162 TRP A CG 1 ATOM 1106 C CD1 . TRP A 1 148 ? 68.742 99.840 32.592 1.00 34.77 ? 162 TRP A CD1 1 ATOM 1107 C CD2 . TRP A 1 148 ? 68.746 101.037 30.693 1.00 34.32 ? 162 TRP A CD2 1 ATOM 1108 N NE1 . TRP A 1 148 ? 70.055 100.055 32.224 1.00 33.42 ? 162 TRP A NE1 1 ATOM 1109 C CE2 . TRP A 1 148 ? 70.085 100.786 31.066 1.00 34.35 ? 162 TRP A CE2 1 ATOM 1110 C CE3 . TRP A 1 148 ? 68.505 101.778 29.531 1.00 32.96 ? 162 TRP A CE3 1 ATOM 1111 C CZ2 . TRP A 1 148 ? 71.185 101.253 30.309 1.00 33.97 ? 162 TRP A CZ2 1 ATOM 1112 C CZ3 . TRP A 1 148 ? 69.599 102.249 28.788 1.00 33.52 ? 162 TRP A CZ3 1 ATOM 1113 C CH2 . TRP A 1 148 ? 70.913 101.978 29.174 1.00 34.15 ? 162 TRP A CH2 1 ATOM 1114 N N . ILE A 1 149 ? 65.261 103.328 31.185 1.00 38.46 ? 163 ILE A N 1 ATOM 1115 C CA . ILE A 1 149 ? 65.564 104.606 30.559 1.00 36.00 ? 163 ILE A CA 1 ATOM 1116 C C . ILE A 1 149 ? 65.258 105.727 31.555 1.00 40.38 ? 163 ILE A C 1 ATOM 1117 O O . ILE A 1 149 ? 66.041 106.676 31.685 1.00 34.47 ? 163 ILE A O 1 ATOM 1118 C CB . ILE A 1 149 ? 64.820 104.812 29.204 1.00 38.80 ? 163 ILE A CB 1 ATOM 1119 C CG1 . ILE A 1 149 ? 65.286 103.787 28.167 1.00 37.61 ? 163 ILE A CG1 1 ATOM 1120 C CG2 . ILE A 1 149 ? 65.107 106.214 28.633 1.00 39.27 ? 163 ILE A CG2 1 ATOM 1121 C CD1 . ILE A 1 149 ? 64.303 103.589 27.001 1.00 37.82 ? 163 ILE A CD1 1 ATOM 1122 N N . LEU A 1 150 ? 64.130 105.603 32.259 1.00 36.69 ? 164 LEU A N 1 ATOM 1123 C CA . LEU A 1 150 ? 63.794 106.543 33.323 1.00 38.42 ? 164 LEU A CA 1 ATOM 1124 C C . LEU A 1 150 ? 64.884 106.588 34.398 1.00 37.45 ? 164 LEU A C 1 ATOM 1125 O O . LEU A 1 150 ? 65.266 107.666 34.860 1.00 36.63 ? 164 LEU A O 1 ATOM 1126 C CB . LEU A 1 150 ? 62.445 106.168 33.950 1.00 36.38 ? 164 LEU A CB 1 ATOM 1127 C CG . LEU A 1 150 ? 61.251 106.309 32.994 1.00 34.25 ? 164 LEU A CG 1 ATOM 1128 C CD1 . LEU A 1 150 ? 59.959 105.829 33.619 1.00 34.08 ? 164 LEU A CD1 1 ATOM 1129 C CD2 . LEU A 1 150 ? 61.114 107.759 32.565 1.00 32.96 ? 164 LEU A CD2 1 ATOM 1130 N N . GLY A 1 151 ? 65.377 105.415 34.795 1.00 38.60 ? 165 GLY A N 1 ATOM 1131 C CA . GLY A 1 151 ? 66.385 105.319 35.841 1.00 36.66 ? 165 GLY A CA 1 ATOM 1132 C C . GLY A 1 151 ? 67.662 106.040 35.439 1.00 36.48 ? 165 GLY A C 1 ATOM 1133 O O . GLY A 1 151 ? 68.265 106.739 36.254 1.00 36.12 ? 165 GLY A O 1 ATOM 1134 N N . ALA A 1 152 ? 68.067 105.879 34.180 1.00 36.03 ? 166 ALA A N 1 ATOM 1135 C CA . ALA A 1 152 ? 69.234 106.595 33.656 1.00 36.26 ? 166 ALA A CA 1 ATOM 1136 C C . ALA A 1 152 ? 69.110 108.089 33.907 1.00 37.22 ? 166 ALA A C 1 ATOM 1137 O O . ALA A 1 152 ? 70.058 108.739 34.365 1.00 38.23 ? 166 ALA A O 1 ATOM 1138 C CB . ALA A 1 152 ? 69.435 106.314 32.158 1.00 36.06 ? 166 ALA A CB 1 ATOM 1139 N N . LYS A 1 153 ? 67.943 108.642 33.598 1.00 40.07 ? 167 LYS A N 1 ATOM 1140 C CA . LYS A 1 153 ? 67.708 110.059 33.855 1.00 37.87 ? 167 LYS A CA 1 ATOM 1141 C C . LYS A 1 153 ? 67.676 110.357 35.352 1.00 40.19 ? 167 LYS A C 1 ATOM 1142 O O . LYS A 1 153 ? 68.415 111.216 35.832 1.00 42.59 ? 167 LYS A O 1 ATOM 1143 C CB . LYS A 1 153 ? 66.404 110.520 33.209 1.00 37.50 ? 167 LYS A CB 1 ATOM 1144 C CG . LYS A 1 153 ? 66.193 112.021 33.269 1.00 54.15 ? 167 LYS A CG 1 ATOM 1145 C CD . LYS A 1 153 ? 67.451 112.762 32.814 1.00 60.61 ? 167 LYS A CD 1 ATOM 1146 C CE . LYS A 1 153 ? 67.222 114.261 32.651 1.00 62.89 ? 167 LYS A CE 1 ATOM 1147 N NZ . LYS A 1 153 ? 66.485 114.566 31.392 1.00 63.10 ? 167 LYS A NZ 1 ATOM 1148 N N . HIS A 1 154 ? 66.830 109.637 36.091 1.00 43.86 ? 168 HIS A N 1 ATOM 1149 C CA . HIS A 1 154 ? 66.584 109.990 37.492 1.00 44.02 ? 168 HIS A CA 1 ATOM 1150 C C . HIS A 1 154 ? 67.755 109.750 38.435 1.00 44.59 ? 168 HIS A C 1 ATOM 1151 O O . HIS A 1 154 ? 67.992 110.555 39.341 1.00 46.28 ? 168 HIS A O 1 ATOM 1152 C CB . HIS A 1 154 ? 65.293 109.345 37.991 1.00 43.41 ? 168 HIS A CB 1 ATOM 1153 C CG . HIS A 1 154 ? 64.104 109.718 37.166 1.00 44.45 ? 168 HIS A CG 1 ATOM 1154 N ND1 . HIS A 1 154 ? 63.013 108.892 37.008 1.00 43.46 ? 168 HIS A ND1 1 ATOM 1155 C CD2 . HIS A 1 154 ? 63.852 110.824 36.422 1.00 46.37 ? 168 HIS A CD2 1 ATOM 1156 C CE1 . HIS A 1 154 ? 62.127 109.482 36.223 1.00 45.61 ? 168 HIS A CE1 1 ATOM 1157 N NE2 . HIS A 1 154 ? 62.614 110.655 35.850 1.00 46.22 ? 168 HIS A NE2 1 ATOM 1158 N N . TYR A 1 155 ? 68.510 108.679 38.222 1.00 43.24 ? 169 TYR A N 1 ATOM 1159 C CA . TYR A 1 155 ? 69.618 108.390 39.129 1.00 43.02 ? 169 TYR A CA 1 ATOM 1160 C C . TYR A 1 155 ? 70.978 108.850 38.624 1.00 47.27 ? 169 TYR A C 1 ATOM 1161 O O . TYR A 1 155 ? 71.912 108.972 39.409 1.00 46.58 ? 169 TYR A O 1 ATOM 1162 C CB . TYR A 1 155 ? 69.632 106.905 39.514 1.00 40.70 ? 169 TYR A CB 1 ATOM 1163 C CG . TYR A 1 155 ? 68.383 106.507 40.260 1.00 44.93 ? 169 TYR A CG 1 ATOM 1164 C CD1 . TYR A 1 155 ? 68.228 106.797 41.624 1.00 42.54 ? 169 TYR A CD1 1 ATOM 1165 C CD2 . TYR A 1 155 ? 67.337 105.873 39.602 1.00 42.56 ? 169 TYR A CD2 1 ATOM 1166 C CE1 . TYR A 1 155 ? 67.061 106.439 42.301 1.00 40.18 ? 169 TYR A CE1 1 ATOM 1167 C CE2 . TYR A 1 155 ? 66.182 105.515 40.272 1.00 42.45 ? 169 TYR A CE2 1 ATOM 1168 C CZ . TYR A 1 155 ? 66.048 105.804 41.617 1.00 43.96 ? 169 TYR A CZ 1 ATOM 1169 O OH . TYR A 1 155 ? 64.880 105.440 42.265 1.00 45.90 ? 169 TYR A OH 1 ATOM 1170 N N . HIS A 1 156 ? 71.094 109.128 37.324 1.00 45.04 ? 170 HIS A N 1 ATOM 1171 C CA . HIS A 1 156 ? 72.409 109.415 36.752 1.00 45.24 ? 170 HIS A CA 1 ATOM 1172 C C . HIS A 1 156 ? 72.486 110.665 35.867 1.00 41.13 ? 170 HIS A C 1 ATOM 1173 O O . HIS A 1 156 ? 73.563 111.013 35.386 1.00 41.95 ? 170 HIS A O 1 ATOM 1174 C CB . HIS A 1 156 ? 72.909 108.176 36.006 1.00 42.72 ? 170 HIS A CB 1 ATOM 1175 C CG . HIS A 1 156 ? 72.982 106.964 36.876 1.00 40.92 ? 170 HIS A CG 1 ATOM 1176 N ND1 . HIS A 1 156 ? 73.855 106.873 37.937 1.00 42.32 ? 170 HIS A ND1 1 ATOM 1177 C CD2 . HIS A 1 156 ? 72.260 105.818 36.884 1.00 41.54 ? 170 HIS A CD2 1 ATOM 1178 C CE1 . HIS A 1 156 ? 73.687 105.713 38.550 1.00 38.97 ? 170 HIS A CE1 1 ATOM 1179 N NE2 . HIS A 1 156 ? 72.724 105.055 37.927 1.00 45.89 ? 170 HIS A NE2 1 ATOM 1180 N N . ASP A 1 157 ? 71.349 111.336 35.688 1.00 43.28 ? 171 ASP A N 1 ATOM 1181 C CA . ASP A 1 157 ? 71.248 112.498 34.800 1.00 47.35 ? 171 ASP A CA 1 ATOM 1182 C C . ASP A 1 157 ? 71.668 112.101 33.382 1.00 46.54 ? 171 ASP A C 1 ATOM 1183 O O . ASP A 1 157 ? 72.385 112.844 32.698 1.00 47.42 ? 171 ASP A O 1 ATOM 1184 C CB . ASP A 1 157 ? 72.078 113.687 35.324 1.00 53.15 ? 171 ASP A CB 1 ATOM 1185 C CG . ASP A 1 157 ? 71.748 114.996 34.607 1.00 62.06 ? 171 ASP A CG 1 ATOM 1186 O OD1 . ASP A 1 157 ? 70.542 115.291 34.439 1.00 64.95 ? 171 ASP A OD1 1 ATOM 1187 O OD2 . ASP A 1 157 ? 72.682 115.723 34.198 1.00 66.51 ? 171 ASP A OD2 1 ATOM 1188 N N . LEU A 1 158 ? 71.220 110.923 32.951 1.00 46.87 ? 172 LEU A N 1 ATOM 1189 C CA . LEU A 1 158 ? 71.568 110.402 31.625 1.00 47.59 ? 172 LEU A CA 1 ATOM 1190 C C . LEU A 1 158 ? 70.358 110.368 30.724 1.00 50.04 ? 172 LEU A C 1 ATOM 1191 O O . LEU A 1 158 ? 69.295 109.840 31.094 1.00 38.33 ? 172 LEU A O 1 ATOM 1192 C CB . LEU A 1 158 ? 72.176 108.997 31.717 1.00 43.74 ? 172 LEU A CB 1 ATOM 1193 C CG . LEU A 1 158 ? 73.526 108.937 32.435 1.00 47.36 ? 172 LEU A CG 1 ATOM 1194 C CD1 . LEU A 1 158 ? 73.977 107.482 32.549 1.00 47.89 ? 172 LEU A CD1 1 ATOM 1195 C CD2 . LEU A 1 158 ? 74.566 109.792 31.687 1.00 45.44 ? 172 LEU A CD2 1 ATOM 1196 N N . ASP A 1 159 ? 70.540 110.948 29.545 1.00 51.83 ? 173 ASP A N 1 ATOM 1197 C CA . ASP A 1 159 ? 69.536 110.982 28.507 1.00 53.12 ? 173 ASP A CA 1 ATOM 1198 C C . ASP A 1 159 ? 69.912 109.942 27.477 1.00 50.95 ? 173 ASP A C 1 ATOM 1199 O O . ASP A 1 159 ? 70.870 110.126 26.722 1.00 53.42 ? 173 ASP A O 1 ATOM 1200 C CB . ASP A 1 159 ? 69.525 112.354 27.838 1.00 58.32 ? 173 ASP A CB 1 ATOM 1201 C CG . ASP A 1 159 ? 69.006 113.433 28.748 1.00 64.76 ? 173 ASP A CG 1 ATOM 1202 O OD1 . ASP A 1 159 ? 68.081 113.135 29.531 1.00 67.92 ? 173 ASP A OD1 1 ATOM 1203 O OD2 . ASP A 1 159 ? 69.518 114.570 28.686 1.00 68.69 ? 173 ASP A OD2 1 ATOM 1204 N N . ILE A 1 160 ? 69.178 108.839 27.468 1.00 42.27 ? 174 ILE A N 1 ATOM 1205 C CA . ILE A 1 160 ? 69.416 107.791 26.500 1.00 36.85 ? 174 ILE A CA 1 ATOM 1206 C C . ILE A 1 160 ? 68.824 108.276 25.176 1.00 36.90 ? 174 ILE A C 1 ATOM 1207 O O . ILE A 1 160 ? 67.645 108.630 25.111 1.00 40.22 ? 174 ILE A O 1 ATOM 1208 C CB . ILE A 1 160 ? 68.742 106.464 26.924 1.00 37.16 ? 174 ILE A CB 1 ATOM 1209 C CG1 . ILE A 1 160 ? 69.246 106.004 28.316 1.00 35.58 ? 174 ILE A CG1 1 ATOM 1210 C CG2 . ILE A 1 160 ? 68.936 105.401 25.851 1.00 35.27 ? 174 ILE A CG2 1 ATOM 1211 C CD1 . ILE A 1 160 ? 70.789 105.960 28.464 1.00 37.54 ? 174 ILE A CD1 1 ATOM 1212 N N . ASP A 1 161 ? 69.628 108.298 24.124 1.00 37.49 ? 175 ASP A N 1 ATOM 1213 C CA . ASP A 1 161 ? 69.130 108.756 22.826 1.00 45.24 ? 175 ASP A CA 1 ATOM 1214 C C . ASP A 1 161 ? 68.418 107.674 22.019 1.00 40.85 ? 175 ASP A C 1 ATOM 1215 O O . ASP A 1 161 ? 67.402 107.930 21.360 1.00 42.31 ? 175 ASP A O 1 ATOM 1216 C CB . ASP A 1 161 ? 70.280 109.361 22.023 1.00 44.36 ? 175 ASP A CB 1 ATOM 1217 C CG . ASP A 1 161 ? 70.988 110.452 22.790 1.00 50.26 ? 175 ASP A CG 1 ATOM 1218 O OD1 . ASP A 1 161 ? 70.398 111.546 22.917 1.00 53.70 ? 175 ASP A OD1 1 ATOM 1219 O OD2 . ASP A 1 161 ? 72.112 110.212 23.292 1.00 50.33 ? 175 ASP A OD2 1 ATOM 1220 N N . TYR A 1 162 ? 68.944 106.459 22.060 1.00 39.65 ? 176 TYR A N 1 ATOM 1221 C CA . TYR A 1 162 ? 68.363 105.388 21.253 1.00 41.69 ? 176 TYR A CA 1 ATOM 1222 C C . TYR A 1 162 ? 68.080 104.145 22.063 1.00 37.97 ? 176 TYR A C 1 ATOM 1223 O O . TYR A 1 162 ? 68.870 103.784 22.944 1.00 41.42 ? 176 TYR A O 1 ATOM 1224 C CB . TYR A 1 162 ? 69.272 105.054 20.068 1.00 41.03 ? 176 TYR A CB 1 ATOM 1225 C CG . TYR A 1 162 ? 69.348 106.168 19.059 1.00 40.60 ? 176 TYR A CG 1 ATOM 1226 C CD1 . TYR A 1 162 ? 70.228 107.234 19.230 1.00 44.12 ? 176 TYR A CD1 1 ATOM 1227 C CD2 . TYR A 1 162 ? 68.543 106.163 17.934 1.00 43.18 ? 176 TYR A CD2 1 ATOM 1228 C CE1 . TYR A 1 162 ? 70.313 108.273 18.277 1.00 45.49 ? 176 TYR A CE1 1 ATOM 1229 C CE2 . TYR A 1 162 ? 68.624 107.190 16.976 1.00 45.80 ? 176 TYR A CE2 1 ATOM 1230 C CZ . TYR A 1 162 ? 69.503 108.233 17.161 1.00 46.35 ? 176 TYR A CZ 1 ATOM 1231 O OH . TYR A 1 162 ? 69.556 109.235 16.226 1.00 51.48 ? 176 TYR A OH 1 ATOM 1232 N N . ILE A 1 163 ? 66.945 103.519 21.774 1.00 34.18 ? 177 ILE A N 1 ATOM 1233 C CA . ILE A 1 163 ? 66.561 102.260 22.421 1.00 38.09 ? 177 ILE A CA 1 ATOM 1234 C C . ILE A 1 163 ? 66.304 101.191 21.347 1.00 31.84 ? 177 ILE A C 1 ATOM 1235 O O . ILE A 1 163 ? 65.631 101.461 20.343 1.00 32.53 ? 177 ILE A O 1 ATOM 1236 C CB . ILE A 1 163 ? 65.319 102.421 23.326 1.00 34.40 ? 177 ILE A CB 1 ATOM 1237 C CG1 . ILE A 1 163 ? 65.052 101.134 24.098 1.00 35.18 ? 177 ILE A CG1 1 ATOM 1238 C CG2 . ILE A 1 163 ? 64.072 102.782 22.518 1.00 31.33 ? 177 ILE A CG2 1 ATOM 1239 C CD1 . ILE A 1 163 ? 66.234 100.728 25.004 1.00 34.42 ? 177 ILE A CD1 1 ATOM 1240 N N . GLY A 1 164 ? 66.861 99.995 21.536 1.00 31.46 ? 178 GLY A N 1 ATOM 1241 C CA . GLY A 1 164 ? 66.660 98.904 20.578 1.00 30.99 ? 178 GLY A CA 1 ATOM 1242 C C . GLY A 1 164 ? 65.654 97.869 21.064 1.00 34.19 ? 178 GLY A C 1 ATOM 1243 O O . GLY A 1 164 ? 64.942 98.089 22.065 1.00 33.07 ? 178 GLY A O 1 ATOM 1244 N N . ILE A 1 165 ? 65.596 96.736 20.368 1.00 36.35 ? 179 ILE A N 1 ATOM 1245 C CA . ILE A 1 165 ? 64.524 95.758 20.564 1.00 28.30 ? 179 ILE A CA 1 ATOM 1246 C C . ILE A 1 165 ? 65.029 94.504 21.300 1.00 33.86 ? 179 ILE A C 1 ATOM 1247 O O . ILE A 1 165 ? 64.854 94.384 22.533 1.00 34.06 ? 179 ILE A O 1 ATOM 1248 C CB . ILE A 1 165 ? 63.841 95.409 19.219 1.00 28.11 ? 179 ILE A CB 1 ATOM 1249 C CG1 . ILE A 1 165 ? 63.328 96.686 18.529 1.00 29.73 ? 179 ILE A CG1 1 ATOM 1250 C CG2 . ILE A 1 165 ? 62.727 94.355 19.406 1.00 28.08 ? 179 ILE A CG2 1 ATOM 1251 C CD1 . ILE A 1 165 ? 62.453 97.605 19.436 1.00 30.20 ? 179 ILE A CD1 1 ATOM 1252 N N . TRP A 1 166 ? 65.641 93.568 20.565 1.00 30.47 ? 180 TRP A N 1 ATOM 1253 C CA . TRP A 1 166 ? 66.191 92.348 21.189 1.00 32.67 ? 180 TRP A CA 1 ATOM 1254 C C . TRP A 1 166 ? 67.358 91.880 20.362 1.00 33.35 ? 180 TRP A C 1 ATOM 1255 O O . TRP A 1 166 ? 67.178 91.371 19.250 1.00 32.56 ? 180 TRP A O 1 ATOM 1256 C CB . TRP A 1 166 ? 65.135 91.240 21.318 1.00 28.28 ? 180 TRP A CB 1 ATOM 1257 C CG . TRP A 1 166 ? 65.569 89.996 22.149 1.00 26.18 ? 180 TRP A CG 1 ATOM 1258 C CD1 . TRP A 1 166 ? 66.657 89.887 22.968 1.00 28.19 ? 180 TRP A CD1 1 ATOM 1259 C CD2 . TRP A 1 166 ? 64.894 88.720 22.212 1.00 28.53 ? 180 TRP A CD2 1 ATOM 1260 N NE1 . TRP A 1 166 ? 66.704 88.625 23.534 1.00 27.13 ? 180 TRP A NE1 1 ATOM 1261 C CE2 . TRP A 1 166 ? 65.634 87.894 23.088 1.00 27.28 ? 180 TRP A CE2 1 ATOM 1262 C CE3 . TRP A 1 166 ? 63.746 88.195 21.593 1.00 27.03 ? 180 TRP A CE3 1 ATOM 1263 C CZ2 . TRP A 1 166 ? 65.259 86.564 23.369 1.00 26.65 ? 180 TRP A CZ2 1 ATOM 1264 C CZ3 . TRP A 1 166 ? 63.372 86.868 21.877 1.00 25.07 ? 180 TRP A CZ3 1 ATOM 1265 C CH2 . TRP A 1 166 ? 64.130 86.076 22.758 1.00 27.06 ? 180 TRP A CH2 1 ATOM 1266 N N . ASN A 1 167 ? 68.558 92.078 20.903 1.00 32.48 ? 181 ASN A N 1 ATOM 1267 C CA . ASN A 1 167 ? 69.789 91.877 20.151 1.00 29.81 ? 181 ASN A CA 1 ATOM 1268 C C . ASN A 1 167 ? 69.905 90.548 19.425 1.00 35.12 ? 181 ASN A C 1 ATOM 1269 O O . ASN A 1 167 ? 69.849 89.500 20.057 1.00 34.51 ? 181 ASN A O 1 ATOM 1270 C CB . ASN A 1 167 ? 71.007 91.996 21.050 1.00 30.40 ? 181 ASN A CB 1 ATOM 1271 C CG . ASN A 1 167 ? 72.298 91.912 20.255 1.00 39.25 ? 181 ASN A CG 1 ATOM 1272 O OD1 . ASN A 1 167 ? 72.593 92.804 19.451 1.00 39.16 ? 181 ASN A OD1 1 ATOM 1273 N ND2 . ASN A 1 167 ? 73.046 90.826 20.434 1.00 31.42 ? 181 ASN A ND2 1 ATOM 1274 N N . GLU A 1 168 ? 70.091 90.601 18.108 1.00 37.64 ? 182 GLU A N 1 ATOM 1275 C CA . GLU A 1 168 ? 70.296 89.399 17.288 1.00 35.53 ? 182 GLU A CA 1 ATOM 1276 C C . GLU A 1 168 ? 69.182 88.367 17.429 1.00 34.37 ? 182 GLU A C 1 ATOM 1277 O O . GLU A 1 168 ? 69.405 87.187 17.171 1.00 37.38 ? 182 GLU A O 1 ATOM 1278 C CB . GLU A 1 168 ? 71.644 88.740 17.623 1.00 36.21 ? 182 GLU A CB 1 ATOM 1279 C CG . GLU A 1 168 ? 72.894 89.526 17.183 1.00 40.90 ? 182 GLU A CG 1 ATOM 1280 C CD . GLU A 1 168 ? 73.275 89.238 15.739 1.00 51.28 ? 182 GLU A CD 1 ATOM 1281 O OE1 . GLU A 1 168 ? 72.811 88.201 15.214 1.00 52.16 ? 182 GLU A OE1 1 ATOM 1282 O OE2 . GLU A 1 168 ? 74.042 90.034 15.135 1.00 54.56 ? 182 GLU A OE2 1 ATOM 1283 N N . ARG A 1 169 ? 67.981 88.801 17.814 1.00 30.62 ? 183 ARG A N 1 ATOM 1284 C CA . ARG A 1 169 ? 66.862 87.882 18.060 1.00 30.65 ? 183 ARG A CA 1 ATOM 1285 C C . ARG A 1 169 ? 65.609 88.448 17.418 1.00 31.92 ? 183 ARG A C 1 ATOM 1286 O O . ARG A 1 169 ? 65.622 89.600 16.983 1.00 32.74 ? 183 ARG A O 1 ATOM 1287 C CB . ARG A 1 169 ? 66.651 87.698 19.570 1.00 29.21 ? 183 ARG A CB 1 ATOM 1288 C CG . ARG A 1 169 ? 67.765 86.965 20.276 1.00 29.14 ? 183 ARG A CG 1 ATOM 1289 C CD . ARG A 1 169 ? 67.788 85.476 19.935 1.00 31.45 ? 183 ARG A CD 1 ATOM 1290 N NE . ARG A 1 169 ? 68.944 84.853 20.581 1.00 33.32 ? 183 ARG A NE 1 ATOM 1291 C CZ . ARG A 1 169 ? 70.189 84.882 20.106 1.00 33.63 ? 183 ARG A CZ 1 ATOM 1292 N NH1 . ARG A 1 169 ? 70.466 85.489 18.963 1.00 38.46 ? 183 ARG A NH1 1 ATOM 1293 N NH2 . ARG A 1 169 ? 71.168 84.287 20.777 1.00 33.01 ? 183 ARG A NH2 1 ATOM 1294 N N . PRO A 1 170 ? 64.522 87.658 17.345 1.00 33.30 ? 184 PRO A N 1 ATOM 1295 C CA . PRO A 1 170 ? 63.383 88.185 16.583 1.00 38.72 ? 184 PRO A CA 1 ATOM 1296 C C . PRO A 1 170 ? 62.706 89.393 17.220 1.00 39.35 ? 184 PRO A C 1 ATOM 1297 O O . PRO A 1 170 ? 62.749 89.550 18.446 1.00 37.90 ? 184 PRO A O 1 ATOM 1298 C CB . PRO A 1 170 ? 62.400 87.002 16.549 1.00 39.91 ? 184 PRO A CB 1 ATOM 1299 C CG . PRO A 1 170 ? 63.269 85.781 16.751 1.00 36.71 ? 184 PRO A CG 1 ATOM 1300 C CD . PRO A 1 170 ? 64.320 86.247 17.729 1.00 35.26 ? 184 PRO A CD 1 ATOM 1301 N N . PHE A 1 171 ? 62.107 90.247 16.386 1.00 38.11 ? 185 PHE A N 1 ATOM 1302 C CA . PHE A 1 171 ? 61.282 91.336 16.892 1.00 37.20 ? 185 PHE A CA 1 ATOM 1303 C C . PHE A 1 171 ? 59.802 90.977 16.802 1.00 40.72 ? 185 PHE A C 1 ATOM 1304 O O . PHE A 1 171 ? 59.405 90.055 16.073 1.00 40.21 ? 185 PHE A O 1 ATOM 1305 C CB . PHE A 1 171 ? 61.558 92.660 16.156 1.00 37.96 ? 185 PHE A CB 1 ATOM 1306 C CG . PHE A 1 171 ? 61.129 92.666 14.693 1.00 34.53 ? 185 PHE A CG 1 ATOM 1307 C CD1 . PHE A 1 171 ? 59.808 92.945 14.326 1.00 33.42 ? 185 PHE A CD1 1 ATOM 1308 C CD2 . PHE A 1 171 ? 62.061 92.436 13.693 1.00 34.55 ? 185 PHE A CD2 1 ATOM 1309 C CE1 . PHE A 1 171 ? 59.426 92.967 12.988 1.00 38.02 ? 185 PHE A CE1 1 ATOM 1310 C CE2 . PHE A 1 171 ? 61.695 92.459 12.357 1.00 37.62 ? 185 PHE A CE2 1 ATOM 1311 C CZ . PHE A 1 171 ? 60.370 92.717 11.999 1.00 36.67 ? 185 PHE A CZ 1 ATOM 1312 N N . ASP A 1 172 ? 58.982 91.715 17.540 1.00 39.50 ? 186 ASP A N 1 ATOM 1313 C CA . ASP A 1 172 ? 57.546 91.550 17.451 1.00 36.14 ? 186 ASP A CA 1 ATOM 1314 C C . ASP A 1 172 ? 57.024 92.936 17.130 1.00 35.42 ? 186 ASP A C 1 ATOM 1315 O O . ASP A 1 172 ? 57.296 93.898 17.866 1.00 29.93 ? 186 ASP A O 1 ATOM 1316 C CB . ASP A 1 172 ? 57.004 91.052 18.788 1.00 39.08 ? 186 ASP A CB 1 ATOM 1317 C CG . ASP A 1 172 ? 55.504 90.842 18.778 1.00 43.78 ? 186 ASP A CG 1 ATOM 1318 O OD1 . ASP A 1 172 ? 54.761 91.825 18.579 1.00 47.58 ? 186 ASP A OD1 1 ATOM 1319 O OD2 . ASP A 1 172 ? 55.060 89.705 19.024 1.00 46.10 ? 186 ASP A OD2 1 ATOM 1320 N N . ALA A 1 173 ? 56.304 93.067 16.021 1.00 34.04 ? 187 ALA A N 1 ATOM 1321 C CA . ALA A 1 173 ? 55.932 94.402 15.556 1.00 33.71 ? 187 ALA A CA 1 ATOM 1322 C C . ALA A 1 173 ? 55.000 95.045 16.584 1.00 31.09 ? 187 ALA A C 1 ATOM 1323 O O . ALA A 1 173 ? 55.041 96.249 16.801 1.00 33.41 ? 187 ALA A O 1 ATOM 1324 C CB . ALA A 1 173 ? 55.274 94.340 14.181 1.00 31.83 ? 187 ALA A CB 1 ATOM 1325 N N . ASN A 1 174 ? 54.161 94.237 17.218 1.00 30.12 ? 188 ASN A N 1 ATOM 1326 C CA . ASN A 1 174 ? 53.304 94.759 18.266 1.00 33.72 ? 188 ASN A CA 1 ATOM 1327 C C . ASN A 1 174 ? 54.096 95.248 19.490 1.00 35.29 ? 188 ASN A C 1 ATOM 1328 O O . ASN A 1 174 ? 53.706 96.238 20.118 1.00 37.10 ? 188 ASN A O 1 ATOM 1329 C CB . ASN A 1 174 ? 52.234 93.746 18.641 1.00 33.28 ? 188 ASN A CB 1 ATOM 1330 C CG . ASN A 1 174 ? 51.163 93.626 17.571 1.00 41.55 ? 188 ASN A CG 1 ATOM 1331 O OD1 . ASN A 1 174 ? 50.744 94.629 16.980 1.00 44.27 ? 188 ASN A OD1 1 ATOM 1332 N ND2 . ASN A 1 174 ? 50.731 92.404 17.302 1.00 41.29 ? 188 ASN A ND2 1 ATOM 1333 N N . TYR A 1 175 ? 55.216 94.583 19.802 1.00 28.22 ? 189 TYR A N 1 ATOM 1334 C CA . TYR A 1 175 ? 56.085 95.046 20.880 1.00 32.02 ? 189 TYR A CA 1 ATOM 1335 C C . TYR A 1 175 ? 56.685 96.400 20.571 1.00 32.84 ? 189 TYR A C 1 ATOM 1336 O O . TYR A 1 175 ? 56.733 97.276 21.442 1.00 31.69 ? 189 TYR A O 1 ATOM 1337 C CB . TYR A 1 175 ? 57.214 94.050 21.197 1.00 28.80 ? 189 TYR A CB 1 ATOM 1338 C CG . TYR A 1 175 ? 58.226 94.632 22.168 1.00 29.13 ? 189 TYR A CG 1 ATOM 1339 C CD1 . TYR A 1 175 ? 57.922 94.756 23.522 1.00 28.24 ? 189 TYR A CD1 1 ATOM 1340 C CD2 . TYR A 1 175 ? 59.460 95.074 21.735 1.00 25.82 ? 189 TYR A CD2 1 ATOM 1341 C CE1 . TYR A 1 175 ? 58.823 95.282 24.415 1.00 29.32 ? 189 TYR A CE1 1 ATOM 1342 C CE2 . TYR A 1 175 ? 60.378 95.618 22.623 1.00 31.61 ? 189 TYR A CE2 1 ATOM 1343 C CZ . TYR A 1 175 ? 60.047 95.727 23.966 1.00 33.08 ? 189 TYR A CZ 1 ATOM 1344 O OH . TYR A 1 175 ? 60.951 96.253 24.872 1.00 32.05 ? 189 TYR A OH 1 ATOM 1345 N N . ILE A 1 176 ? 57.167 96.575 19.344 1.00 32.75 ? 190 ILE A N 1 ATOM 1346 C CA . ILE A 1 176 ? 57.815 97.829 18.993 1.00 31.82 ? 190 ILE A CA 1 ATOM 1347 C C . ILE A 1 176 ? 56.810 98.978 19.115 1.00 34.96 ? 190 ILE A C 1 ATOM 1348 O O . ILE A 1 176 ? 57.161 100.077 19.574 1.00 34.32 ? 190 ILE A O 1 ATOM 1349 C CB . ILE A 1 176 ? 58.403 97.800 17.554 1.00 34.01 ? 190 ILE A CB 1 ATOM 1350 C CG1 . ILE A 1 176 ? 59.437 96.677 17.419 1.00 33.60 ? 190 ILE A CG1 1 ATOM 1351 C CG2 . ILE A 1 176 ? 59.025 99.135 17.215 1.00 31.04 ? 190 ILE A CG2 1 ATOM 1352 C CD1 . ILE A 1 176 ? 60.121 96.616 16.039 1.00 32.62 ? 190 ILE A CD1 1 ATOM 1353 N N . LYS A 1 177 ? 55.575 98.736 18.678 1.00 32.49 ? 191 LYS A N 1 ATOM 1354 C CA . LYS A 1 177 ? 54.512 99.733 18.808 1.00 37.95 ? 191 LYS A CA 1 ATOM 1355 C C . LYS A 1 177 ? 54.194 100.055 20.288 1.00 37.16 ? 191 LYS A C 1 ATOM 1356 O O . LYS A 1 177 ? 54.067 101.224 20.643 1.00 34.55 ? 191 LYS A O 1 ATOM 1357 C CB . LYS A 1 177 ? 53.243 99.275 18.061 1.00 39.29 ? 191 LYS A CB 1 ATOM 1358 C CG . LYS A 1 177 ? 53.332 99.398 16.502 1.00 34.42 ? 191 LYS A CG 1 ATOM 1359 C CD . LYS A 1 177 ? 52.254 98.553 15.788 1.00 32.64 ? 191 LYS A CD 1 ATOM 1360 C CE . LYS A 1 177 ? 52.510 98.498 14.258 1.00 40.17 ? 191 LYS A CE 1 ATOM 1361 N NZ . LYS A 1 177 ? 51.402 97.785 13.520 1.00 40.08 ? 191 LYS A NZ 1 ATOM 1362 N N A GLU A 1 178 ? 54.061 99.020 21.119 0.46 35.74 ? 192 GLU A N 1 ATOM 1363 N N B GLU A 1 178 ? 54.063 99.024 21.126 0.54 35.84 ? 192 GLU A N 1 ATOM 1364 C CA A GLU A 1 178 ? 53.815 99.202 22.552 0.46 33.79 ? 192 GLU A CA 1 ATOM 1365 C CA B GLU A 1 178 ? 53.805 99.207 22.562 0.54 33.72 ? 192 GLU A CA 1 ATOM 1366 C C A GLU A 1 178 ? 54.962 99.944 23.215 0.46 32.60 ? 192 GLU A C 1 ATOM 1367 C C B GLU A 1 178 ? 54.967 99.912 23.252 0.54 32.50 ? 192 GLU A C 1 ATOM 1368 O O A GLU A 1 178 ? 54.739 100.802 24.062 0.46 33.71 ? 192 GLU A O 1 ATOM 1369 O O B GLU A 1 178 ? 54.759 100.722 24.149 0.54 33.74 ? 192 GLU A O 1 ATOM 1370 C CB A GLU A 1 178 ? 53.606 97.855 23.253 0.46 34.47 ? 192 GLU A CB 1 ATOM 1371 C CB B GLU A 1 178 ? 53.514 97.857 23.236 0.54 34.32 ? 192 GLU A CB 1 ATOM 1372 C CG A GLU A 1 178 ? 52.269 97.183 22.981 0.46 37.02 ? 192 GLU A CG 1 ATOM 1373 C CG B GLU A 1 178 ? 53.415 97.886 24.772 0.54 37.40 ? 192 GLU A CG 1 ATOM 1374 C CD A GLU A 1 178 ? 51.075 98.032 23.389 0.46 43.22 ? 192 GLU A CD 1 ATOM 1375 C CD B GLU A 1 178 ? 52.162 98.587 25.295 0.54 44.39 ? 192 GLU A CD 1 ATOM 1376 O OE1 A GLU A 1 178 ? 51.002 98.440 24.571 0.46 45.23 ? 192 GLU A OE1 1 ATOM 1377 O OE1 B GLU A 1 178 ? 51.070 98.407 24.706 0.54 45.32 ? 192 GLU A OE1 1 ATOM 1378 O OE2 A GLU A 1 178 ? 50.205 98.293 22.527 0.46 43.05 ? 192 GLU A OE2 1 ATOM 1379 O OE2 B GLU A 1 178 ? 52.268 99.318 26.306 0.54 47.04 ? 192 GLU A OE2 1 ATOM 1380 N N . LEU A 1 179 ? 56.193 99.612 22.830 1.00 30.28 ? 193 LEU A N 1 ATOM 1381 C CA . LEU A 1 179 ? 57.370 100.287 23.370 1.00 34.59 ? 193 LEU A CA 1 ATOM 1382 C C . LEU A 1 179 ? 57.325 101.786 23.049 1.00 38.57 ? 193 LEU A C 1 ATOM 1383 O O . LEU A 1 179 ? 57.675 102.612 23.899 1.00 34.76 ? 193 LEU A O 1 ATOM 1384 C CB . LEU A 1 179 ? 58.660 99.664 22.821 1.00 35.53 ? 193 LEU A CB 1 ATOM 1385 C CG . LEU A 1 179 ? 59.949 100.358 23.278 1.00 35.67 ? 193 LEU A CG 1 ATOM 1386 C CD1 . LEU A 1 179 ? 60.145 100.209 24.808 1.00 36.04 ? 193 LEU A CD1 1 ATOM 1387 C CD2 . LEU A 1 179 ? 61.158 99.837 22.524 1.00 30.46 ? 193 LEU A CD2 1 ATOM 1388 N N . ARG A 1 180 ? 56.864 102.140 21.843 1.00 36.62 ? 194 ARG A N 1 ATOM 1389 C CA . ARG A 1 180 ? 56.720 103.564 21.469 1.00 37.69 ? 194 ARG A CA 1 ATOM 1390 C C . ARG A 1 180 ? 55.648 104.262 22.330 1.00 34.66 ? 194 ARG A C 1 ATOM 1391 O O . ARG A 1 180 ? 55.889 105.345 22.867 1.00 36.04 ? 194 ARG A O 1 ATOM 1392 C CB . ARG A 1 180 ? 56.368 103.715 19.977 1.00 38.30 ? 194 ARG A CB 1 ATOM 1393 C CG . ARG A 1 180 ? 56.193 105.177 19.500 1.00 34.61 ? 194 ARG A CG 1 ATOM 1394 C CD . ARG A 1 180 ? 57.511 105.889 19.395 1.00 34.80 ? 194 ARG A CD 1 ATOM 1395 N NE . ARG A 1 180 ? 57.840 106.631 20.598 1.00 35.12 ? 194 ARG A NE 1 ATOM 1396 C CZ . ARG A 1 180 ? 59.044 107.131 20.862 1.00 37.99 ? 194 ARG A CZ 1 ATOM 1397 N NH1 . ARG A 1 180 ? 60.032 106.973 19.989 1.00 38.59 ? 194 ARG A NH1 1 ATOM 1398 N NH2 . ARG A 1 180 ? 59.269 107.790 22.000 1.00 35.31 ? 194 ARG A NH2 1 ATOM 1399 N N . LYS A 1 181 ? 54.482 103.624 22.442 1.00 33.46 ? 195 LYS A N 1 ATOM 1400 C CA . LYS A 1 181 ? 53.355 104.111 23.225 1.00 37.01 ? 195 LYS A CA 1 ATOM 1401 C C . LYS A 1 181 ? 53.758 104.322 24.695 1.00 39.57 ? 195 LYS A C 1 ATOM 1402 O O . LYS A 1 181 ? 53.492 105.379 25.280 1.00 38.63 ? 195 LYS A O 1 ATOM 1403 C CB . LYS A 1 181 ? 52.207 103.097 23.110 1.00 41.05 ? 195 LYS A CB 1 ATOM 1404 C CG . LYS A 1 181 ? 50.989 103.366 23.984 1.00 47.76 ? 195 LYS A CG 1 ATOM 1405 C CD . LYS A 1 181 ? 49.842 102.411 23.637 1.00 55.33 ? 195 LYS A CD 1 ATOM 1406 C CE . LYS A 1 181 ? 49.386 101.590 24.849 1.00 58.24 ? 195 LYS A CE 1 ATOM 1407 N NZ . LYS A 1 181 ? 48.292 100.619 24.527 1.00 60.55 ? 195 LYS A NZ 1 ATOM 1408 N N . MET A 1 182 ? 54.417 103.316 25.272 1.00 40.15 ? 196 MET A N 1 ATOM 1409 C CA . MET A 1 182 ? 54.942 103.375 26.644 1.00 37.30 ? 196 MET A CA 1 ATOM 1410 C C . MET A 1 182 ? 56.005 104.459 26.814 1.00 37.51 ? 196 MET A C 1 ATOM 1411 O O . MET A 1 182 ? 56.009 105.174 27.827 1.00 35.03 ? 196 MET A O 1 ATOM 1412 C CB . MET A 1 182 ? 55.506 102.001 27.038 1.00 36.33 ? 196 MET A CB 1 ATOM 1413 C CG . MET A 1 182 ? 56.203 101.950 28.401 1.00 41.21 ? 196 MET A CG 1 ATOM 1414 S SD . MET A 1 182 ? 55.096 101.548 29.767 1.00 58.58 ? 196 MET A SD 1 ATOM 1415 C CE . MET A 1 182 ? 54.598 99.879 29.358 1.00 36.37 ? 196 MET A CE 1 ATOM 1416 N N . LEU A 1 183 ? 56.907 104.596 25.839 1.00 37.15 ? 197 LEU A N 1 ATOM 1417 C CA . LEU A 1 183 ? 57.904 105.669 25.900 1.00 37.07 ? 197 LEU A CA 1 ATOM 1418 C C . LEU A 1 183 ? 57.196 107.009 25.948 1.00 37.24 ? 197 LEU A C 1 ATOM 1419 O O . LEU A 1 183 ? 57.493 107.844 26.819 1.00 37.80 ? 197 LEU A O 1 ATOM 1420 C CB . LEU A 1 183 ? 58.847 105.651 24.691 1.00 38.25 ? 197 LEU A CB 1 ATOM 1421 C CG . LEU A 1 183 ? 59.981 104.634 24.624 1.00 35.94 ? 197 LEU A CG 1 ATOM 1422 C CD1 . LEU A 1 183 ? 60.614 104.639 23.224 1.00 31.58 ? 197 LEU A CD1 1 ATOM 1423 C CD2 . LEU A 1 183 ? 61.033 104.901 25.681 1.00 31.24 ? 197 LEU A CD2 1 ATOM 1424 N N . ASP A 1 184 ? 56.245 107.208 25.032 1.00 38.64 ? 198 ASP A N 1 ATOM 1425 C CA . ASP A 1 184 ? 55.520 108.480 24.969 1.00 42.84 ? 198 ASP A CA 1 ATOM 1426 C C . ASP A 1 184 ? 54.755 108.726 26.283 1.00 43.68 ? 198 ASP A C 1 ATOM 1427 O O . ASP A 1 184 ? 54.767 109.832 26.807 1.00 42.95 ? 198 ASP A O 1 ATOM 1428 C CB . ASP A 1 184 ? 54.554 108.521 23.777 1.00 43.72 ? 198 ASP A CB 1 ATOM 1429 C CG . ASP A 1 184 ? 55.266 108.396 22.417 1.00 44.34 ? 198 ASP A CG 1 ATOM 1430 O OD1 . ASP A 1 184 ? 56.472 108.725 22.326 1.00 39.36 ? 198 ASP A OD1 1 ATOM 1431 O OD2 . ASP A 1 184 ? 54.603 107.961 21.438 1.00 44.30 ? 198 ASP A OD2 1 ATOM 1432 N N . TYR A 1 185 ? 54.106 107.685 26.807 1.00 42.14 ? 199 TYR A N 1 ATOM 1433 C CA . TYR A 1 185 ? 53.312 107.798 28.037 1.00 44.06 ? 199 TYR A CA 1 ATOM 1434 C C . TYR A 1 185 ? 54.153 108.260 29.233 1.00 40.46 ? 199 TYR A C 1 ATOM 1435 O O . TYR A 1 185 ? 53.673 108.999 30.097 1.00 35.87 ? 199 TYR A O 1 ATOM 1436 C CB . TYR A 1 185 ? 52.626 106.465 28.356 1.00 46.43 ? 199 TYR A CB 1 ATOM 1437 C CG . TYR A 1 185 ? 51.662 106.503 29.530 1.00 53.51 ? 199 TYR A CG 1 ATOM 1438 C CD1 . TYR A 1 185 ? 50.557 107.349 29.526 1.00 55.55 ? 199 TYR A CD1 1 ATOM 1439 C CD2 . TYR A 1 185 ? 51.837 105.663 30.627 1.00 56.39 ? 199 TYR A CD2 1 ATOM 1440 C CE1 . TYR A 1 185 ? 49.665 107.376 30.598 1.00 56.82 ? 199 TYR A CE1 1 ATOM 1441 C CE2 . TYR A 1 185 ? 50.949 105.678 31.704 1.00 55.74 ? 199 TYR A CE2 1 ATOM 1442 C CZ . TYR A 1 185 ? 49.869 106.535 31.681 1.00 56.46 ? 199 TYR A CZ 1 ATOM 1443 O OH . TYR A 1 185 ? 48.987 106.547 32.739 1.00 55.97 ? 199 TYR A OH 1 ATOM 1444 N N . GLN A 1 186 ? 55.409 107.828 29.269 1.00 40.94 ? 200 GLN A N 1 ATOM 1445 C CA . GLN A 1 186 ? 56.315 108.179 30.359 1.00 41.59 ? 200 GLN A CA 1 ATOM 1446 C C . GLN A 1 186 ? 57.121 109.435 30.066 1.00 45.36 ? 200 GLN A C 1 ATOM 1447 O O . GLN A 1 186 ? 58.105 109.714 30.751 1.00 46.70 ? 200 GLN A O 1 ATOM 1448 C CB . GLN A 1 186 ? 57.253 107.006 30.671 1.00 39.12 ? 200 GLN A CB 1 ATOM 1449 C CG . GLN A 1 186 ? 56.509 105.746 31.147 1.00 39.54 ? 200 GLN A CG 1 ATOM 1450 C CD . GLN A 1 186 ? 55.886 105.948 32.518 1.00 41.87 ? 200 GLN A CD 1 ATOM 1451 O OE1 . GLN A 1 186 ? 56.394 106.739 33.323 1.00 46.56 ? 200 GLN A OE1 1 ATOM 1452 N NE2 . GLN A 1 186 ? 54.784 105.251 32.787 1.00 35.36 ? 200 GLN A NE2 1 ATOM 1453 N N . GLY A 1 187 ? 56.716 110.187 29.044 1.00 47.22 ? 201 GLY A N 1 ATOM 1454 C CA . GLY A 1 187 ? 57.337 111.465 28.749 1.00 46.28 ? 201 GLY A CA 1 ATOM 1455 C C . GLY A 1 187 ? 58.659 111.351 28.023 1.00 47.05 ? 201 GLY A C 1 ATOM 1456 O O . GLY A 1 187 ? 59.489 112.274 28.067 1.00 44.38 ? 201 GLY A O 1 ATOM 1457 N N . LEU A 1 188 ? 58.853 110.232 27.328 1.00 41.97 ? 202 LEU A N 1 ATOM 1458 C CA . LEU A 1 188 ? 60.107 110.009 26.615 1.00 44.06 ? 202 LEU A CA 1 ATOM 1459 C C . LEU A 1 188 ? 59.912 110.075 25.089 1.00 45.77 ? 202 LEU A C 1 ATOM 1460 O O . LEU A 1 188 ? 60.450 109.249 24.330 1.00 43.10 ? 202 LEU A O 1 ATOM 1461 C CB . LEU A 1 188 ? 60.727 108.677 27.052 1.00 42.82 ? 202 LEU A CB 1 ATOM 1462 C CG . LEU A 1 188 ? 60.991 108.571 28.550 1.00 39.71 ? 202 LEU A CG 1 ATOM 1463 C CD1 . LEU A 1 188 ? 61.402 107.149 28.912 1.00 39.09 ? 202 LEU A CD1 1 ATOM 1464 C CD2 . LEU A 1 188 ? 62.052 109.570 28.972 1.00 39.77 ? 202 LEU A CD2 1 ATOM 1465 N N . GLN A 1 189 ? 59.150 111.071 24.640 1.00 48.45 ? 203 GLN A N 1 ATOM 1466 C CA . GLN A 1 189 ? 58.963 111.289 23.208 1.00 47.45 ? 203 GLN A CA 1 ATOM 1467 C C . GLN A 1 189 ? 60.283 111.499 22.500 1.00 44.26 ? 203 GLN A C 1 ATOM 1468 O O . GLN A 1 189 ? 60.411 111.159 21.337 1.00 47.43 ? 203 GLN A O 1 ATOM 1469 C CB . GLN A 1 189 ? 58.024 112.469 22.940 1.00 49.14 ? 203 GLN A CB 1 ATOM 1470 C CG . GLN A 1 189 ? 56.593 112.241 23.441 1.00 51.90 ? 203 GLN A CG 1 ATOM 1471 C CD . GLN A 1 189 ? 56.456 112.480 24.937 1.00 54.70 ? 203 GLN A CD 1 ATOM 1472 O OE1 . GLN A 1 189 ? 57.450 112.659 25.650 1.00 55.98 ? 203 GLN A OE1 1 ATOM 1473 N NE2 . GLN A 1 189 ? 55.220 112.497 25.417 1.00 58.20 ? 203 GLN A NE2 1 ATOM 1474 N N . ARG A 1 190 ? 61.278 112.030 23.197 1.00 44.93 ? 204 ARG A N 1 ATOM 1475 C CA . ARG A 1 190 ? 62.551 112.331 22.535 1.00 50.98 ? 204 ARG A CA 1 ATOM 1476 C C . ARG A 1 190 ? 63.393 111.083 22.249 1.00 47.84 ? 204 ARG A C 1 ATOM 1477 O O . ARG A 1 190 ? 64.318 111.127 21.433 1.00 53.40 ? 204 ARG A O 1 ATOM 1478 C CB . ARG A 1 190 ? 63.377 113.336 23.340 1.00 58.34 ? 204 ARG A CB 1 ATOM 1479 C CG . ARG A 1 190 ? 64.063 112.726 24.550 1.00 67.14 ? 204 ARG A CG 1 ATOM 1480 C CD . ARG A 1 190 ? 65.109 113.662 25.143 1.00 76.27 ? 204 ARG A CD 1 ATOM 1481 N NE . ARG A 1 190 ? 66.062 114.124 24.133 1.00 83.01 ? 204 ARG A NE 1 ATOM 1482 C CZ . ARG A 1 190 ? 67.178 113.479 23.804 1.00 86.18 ? 204 ARG A CZ 1 ATOM 1483 N NH1 . ARG A 1 190 ? 67.490 112.338 24.408 1.00 87.10 ? 204 ARG A NH1 1 ATOM 1484 N NH2 . ARG A 1 190 ? 67.983 113.971 22.870 1.00 87.42 ? 204 ARG A NH2 1 ATOM 1485 N N . VAL A 1 191 ? 63.090 109.978 22.924 1.00 40.92 ? 205 VAL A N 1 ATOM 1486 C CA . VAL A 1 191 ? 63.867 108.760 22.738 1.00 40.85 ? 205 VAL A CA 1 ATOM 1487 C C . VAL A 1 191 ? 63.515 108.120 21.393 1.00 40.17 ? 205 VAL A C 1 ATOM 1488 O O . VAL A 1 191 ? 62.334 107.907 21.104 1.00 41.14 ? 205 VAL A O 1 ATOM 1489 C CB . VAL A 1 191 ? 63.588 107.726 23.839 1.00 39.64 ? 205 VAL A CB 1 ATOM 1490 C CG1 . VAL A 1 191 ? 64.342 106.436 23.532 1.00 33.55 ? 205 VAL A CG1 1 ATOM 1491 C CG2 . VAL A 1 191 ? 63.995 108.272 25.212 1.00 37.24 ? 205 VAL A CG2 1 ATOM 1492 N N . ARG A 1 192 ? 64.531 107.819 20.583 1.00 38.17 ? 206 ARG A N 1 ATOM 1493 C CA . ARG A 1 192 ? 64.297 107.147 19.300 1.00 41.58 ? 206 ARG A CA 1 ATOM 1494 C C . ARG A 1 192 ? 64.440 105.636 19.384 1.00 40.98 ? 206 ARG A C 1 ATOM 1495 O O . ARG A 1 192 ? 65.173 105.116 20.230 1.00 42.82 ? 206 ARG A O 1 ATOM 1496 C CB . ARG A 1 192 ? 65.262 107.668 18.240 1.00 40.02 ? 206 ARG A CB 1 ATOM 1497 C CG . ARG A 1 192 ? 65.096 109.119 17.959 1.00 45.87 ? 206 ARG A CG 1 ATOM 1498 C CD . ARG A 1 192 ? 66.028 109.538 16.847 1.00 59.46 ? 206 ARG A CD 1 ATOM 1499 N NE . ARG A 1 192 ? 66.952 110.565 17.310 1.00 69.86 ? 206 ARG A NE 1 ATOM 1500 C CZ . ARG A 1 192 ? 66.755 111.869 17.144 1.00 74.96 ? 206 ARG A CZ 1 ATOM 1501 N NH1 . ARG A 1 192 ? 65.663 112.302 16.516 1.00 76.10 ? 206 ARG A NH1 1 ATOM 1502 N NH2 . ARG A 1 192 ? 67.650 112.736 17.602 1.00 73.77 ? 206 ARG A NH2 1 ATOM 1503 N N . ILE A 1 193 ? 63.752 104.940 18.484 1.00 39.25 ? 207 ILE A N 1 ATOM 1504 C CA . ILE A 1 193 ? 63.819 103.487 18.423 1.00 37.54 ? 207 ILE A CA 1 ATOM 1505 C C . ILE A 1 193 ? 64.661 103.016 17.229 1.00 39.87 ? 207 ILE A C 1 ATOM 1506 O O . ILE A 1 193 ? 64.463 103.480 16.090 1.00 39.04 ? 207 ILE A O 1 ATOM 1507 C CB . ILE A 1 193 ? 62.401 102.887 18.313 1.00 35.64 ? 207 ILE A CB 1 ATOM 1508 C CG1 . ILE A 1 193 ? 61.575 103.197 19.572 1.00 35.86 ? 207 ILE A CG1 1 ATOM 1509 C CG2 . ILE A 1 193 ? 62.457 101.379 18.079 1.00 34.08 ? 207 ILE A CG2 1 ATOM 1510 C CD1 . ILE A 1 193 ? 60.193 102.557 19.555 1.00 32.82 ? 207 ILE A CD1 1 ATOM 1511 N N . ILE A 1 194 ? 65.591 102.096 17.488 1.00 39.54 ? 208 ILE A N 1 ATOM 1512 C CA . ILE A 1 194 ? 66.353 101.440 16.422 1.00 40.50 ? 208 ILE A CA 1 ATOM 1513 C C . ILE A 1 194 ? 65.995 99.946 16.316 1.00 41.64 ? 208 ILE A C 1 ATOM 1514 O O . ILE A 1 194 ? 65.823 99.260 17.331 1.00 35.33 ? 208 ILE A O 1 ATOM 1515 C CB . ILE A 1 194 ? 67.879 101.638 16.622 1.00 39.85 ? 208 ILE A CB 1 ATOM 1516 C CG1 . ILE A 1 194 ? 68.685 100.956 15.516 1.00 34.62 ? 208 ILE A CG1 1 ATOM 1517 C CG2 . ILE A 1 194 ? 68.316 101.112 18.012 1.00 36.45 ? 208 ILE A CG2 1 ATOM 1518 C CD1 . ILE A 1 194 ? 70.173 101.235 15.638 1.00 42.68 ? 208 ILE A CD1 1 ATOM 1519 N N . ALA A 1 195 ? 65.876 99.440 15.086 1.00 40.30 ? 209 ALA A N 1 ATOM 1520 C CA . ALA A 1 195 ? 65.461 98.057 14.883 1.00 31.56 ? 209 ALA A CA 1 ATOM 1521 C C . ALA A 1 195 ? 66.188 97.411 13.692 1.00 32.07 ? 209 ALA A C 1 ATOM 1522 O O . ALA A 1 195 ? 66.535 98.094 12.737 1.00 33.57 ? 209 ALA A O 1 ATOM 1523 C CB . ALA A 1 195 ? 63.942 97.990 14.707 1.00 35.30 ? 209 ALA A CB 1 ATOM 1524 N N . SER A 1 196 ? 66.424 96.103 13.737 1.00 36.05 ? 210 SER A N 1 ATOM 1525 C CA . SER A 1 196 ? 66.061 95.251 14.869 1.00 34.45 ? 210 SER A CA 1 ATOM 1526 C C . SER A 1 196 ? 67.322 94.622 15.407 1.00 30.83 ? 210 SER A C 1 ATOM 1527 O O . SER A 1 196 ? 67.267 93.598 16.087 1.00 33.82 ? 210 SER A O 1 ATOM 1528 C CB . SER A 1 196 ? 65.096 94.153 14.428 1.00 35.56 ? 210 SER A CB 1 ATOM 1529 O OG . SER A 1 196 ? 65.736 93.232 13.557 1.00 38.48 ? 210 SER A OG 1 ATOM 1530 N N . ASP A 1 197 ? 68.455 95.246 15.096 1.00 31.85 ? 211 ASP A N 1 ATOM 1531 C CA . ASP A 1 197 ? 69.757 94.786 15.564 1.00 35.81 ? 211 ASP A CA 1 ATOM 1532 C C . ASP A 1 197 ? 69.971 93.313 15.209 1.00 38.74 ? 211 ASP A C 1 ATOM 1533 O O . ASP A 1 197 ? 70.399 92.494 16.037 1.00 33.80 ? 211 ASP A O 1 ATOM 1534 C CB . ASP A 1 197 ? 69.922 95.085 17.069 1.00 35.30 ? 211 ASP A CB 1 ATOM 1535 C CG . ASP A 1 197 ? 70.371 96.516 17.315 1.00 40.11 ? 211 ASP A CG 1 ATOM 1536 O OD1 . ASP A 1 197 ? 71.518 96.844 16.946 1.00 39.50 ? 211 ASP A OD1 1 ATOM 1537 O OD2 . ASP A 1 197 ? 69.587 97.322 17.863 1.00 43.04 ? 211 ASP A OD2 1 ATOM 1538 N N . ASN A 1 198 ? 69.679 93.006 13.946 1.00 41.91 ? 212 ASN A N 1 ATOM 1539 C CA . ASN A 1 198 ? 69.833 91.670 13.390 1.00 41.04 ? 212 ASN A CA 1 ATOM 1540 C C . ASN A 1 198 ? 70.187 91.817 11.890 1.00 42.89 ? 212 ASN A C 1 ATOM 1541 O O . ASN A 1 198 ? 71.114 92.562 11.547 1.00 46.62 ? 212 ASN A O 1 ATOM 1542 C CB . ASN A 1 198 ? 68.541 90.855 13.624 1.00 39.94 ? 212 ASN A CB 1 ATOM 1543 C CG . ASN A 1 198 ? 68.795 89.364 13.775 1.00 43.21 ? 212 ASN A CG 1 ATOM 1544 O OD1 . ASN A 1 198 ? 69.856 88.864 13.404 1.00 49.91 ? 212 ASN A OD1 1 ATOM 1545 N ND2 . ASN A 1 198 ? 67.814 88.644 14.312 1.00 44.57 ? 212 ASN A ND2 1 ATOM 1546 N N . LEU A 1 199 ? 69.470 91.136 10.995 1.00 42.29 ? 213 LEU A N 1 ATOM 1547 C CA . LEU A 1 199 ? 69.731 91.286 9.550 1.00 43.83 ? 213 LEU A CA 1 ATOM 1548 C C . LEU A 1 199 ? 68.836 92.366 8.940 1.00 42.35 ? 213 LEU A C 1 ATOM 1549 O O . LEU A 1 199 ? 67.957 92.891 9.624 1.00 41.13 ? 213 LEU A O 1 ATOM 1550 C CB . LEU A 1 199 ? 69.514 89.957 8.804 1.00 44.99 ? 213 LEU A CB 1 ATOM 1551 C CG . LEU A 1 199 ? 70.318 88.722 9.230 1.00 44.37 ? 213 LEU A CG 1 ATOM 1552 C CD1 . LEU A 1 199 ? 69.927 87.489 8.422 1.00 44.52 ? 213 LEU A CD1 1 ATOM 1553 C CD2 . LEU A 1 199 ? 71.814 88.970 9.118 1.00 43.73 ? 213 LEU A CD2 1 ATOM 1554 N N . TRP A 1 200 ? 69.027 92.688 7.656 1.00 38.46 ? 214 TRP A N 1 ATOM 1555 C CA . TRP A 1 200 ? 68.195 93.720 7.036 1.00 36.97 ? 214 TRP A CA 1 ATOM 1556 C C . TRP A 1 200 ? 66.726 93.318 7.003 1.00 39.39 ? 214 TRP A C 1 ATOM 1557 O O . TRP A 1 200 ? 65.843 94.180 7.063 1.00 43.52 ? 214 TRP A O 1 ATOM 1558 C CB . TRP A 1 200 ? 68.680 94.054 5.626 1.00 39.95 ? 214 TRP A CB 1 ATOM 1559 C CG . TRP A 1 200 ? 70.052 94.651 5.601 1.00 38.72 ? 214 TRP A CG 1 ATOM 1560 C CD1 . TRP A 1 200 ? 71.196 94.061 5.142 1.00 38.13 ? 214 TRP A CD1 1 ATOM 1561 C CD2 . TRP A 1 200 ? 70.431 95.968 6.038 1.00 40.63 ? 214 TRP A CD2 1 ATOM 1562 N NE1 . TRP A 1 200 ? 72.257 94.924 5.267 1.00 39.79 ? 214 TRP A NE1 1 ATOM 1563 C CE2 . TRP A 1 200 ? 71.819 96.102 5.811 1.00 38.20 ? 214 TRP A CE2 1 ATOM 1564 C CE3 . TRP A 1 200 ? 69.731 97.042 6.597 1.00 40.10 ? 214 TRP A CE3 1 ATOM 1565 C CZ2 . TRP A 1 200 ? 72.526 97.273 6.122 1.00 38.98 ? 214 TRP A CZ2 1 ATOM 1566 C CZ3 . TRP A 1 200 ? 70.435 98.206 6.907 1.00 42.38 ? 214 TRP A CZ3 1 ATOM 1567 C CH2 . TRP A 1 200 ? 71.817 98.307 6.676 1.00 42.52 ? 214 TRP A CH2 1 ATOM 1568 N N . GLU A 1 201 ? 66.471 92.008 6.926 1.00 37.03 ? 215 GLU A N 1 ATOM 1569 C CA . GLU A 1 201 ? 65.126 91.457 6.932 1.00 39.66 ? 215 GLU A CA 1 ATOM 1570 C C . GLU A 1 201 ? 64.920 90.572 8.168 1.00 38.38 ? 215 GLU A C 1 ATOM 1571 O O . GLU A 1 201 ? 65.868 89.959 8.639 1.00 38.46 ? 215 GLU A O 1 ATOM 1572 C CB . GLU A 1 201 ? 64.896 90.639 5.648 1.00 41.03 ? 215 GLU A CB 1 ATOM 1573 C CG . GLU A 1 201 ? 65.063 91.457 4.353 1.00 42.81 ? 215 GLU A CG 1 ATOM 1574 C CD . GLU A 1 201 ? 63.934 92.452 4.131 1.00 46.13 ? 215 GLU A CD 1 ATOM 1575 O OE1 . GLU A 1 201 ? 63.051 92.572 5.010 1.00 50.33 ? 215 GLU A OE1 1 ATOM 1576 O OE2 . GLU A 1 201 ? 63.910 93.105 3.068 1.00 46.26 ? 215 GLU A OE2 1 ATOM 1577 N N . PRO A 1 202 ? 63.677 90.470 8.666 1.00 35.29 ? 216 PRO A N 1 ATOM 1578 C CA . PRO A 1 202 ? 62.487 91.035 8.024 1.00 36.71 ? 216 PRO A CA 1 ATOM 1579 C C . PRO A 1 202 ? 62.124 92.483 8.391 1.00 36.69 ? 216 PRO A C 1 ATOM 1580 O O . PRO A 1 202 ? 61.053 92.902 7.952 1.00 41.15 ? 216 PRO A O 1 ATOM 1581 C CB . PRO A 1 202 ? 61.367 90.074 8.470 1.00 33.91 ? 216 PRO A CB 1 ATOM 1582 C CG . PRO A 1 202 ? 61.815 89.635 9.856 1.00 37.80 ? 216 PRO A CG 1 ATOM 1583 C CD . PRO A 1 202 ? 63.329 89.593 9.804 1.00 34.37 ? 216 PRO A CD 1 ATOM 1584 N N . ILE A 1 203 ? 62.949 93.230 9.122 1.00 36.47 ? 217 ILE A N 1 ATOM 1585 C CA . ILE A 1 203 ? 62.541 94.595 9.500 1.00 34.49 ? 217 ILE A CA 1 ATOM 1586 C C . ILE A 1 203 ? 62.269 95.506 8.290 1.00 38.12 ? 217 ILE A C 1 ATOM 1587 O O . ILE A 1 203 ? 61.255 96.211 8.260 1.00 41.67 ? 217 ILE A O 1 ATOM 1588 C CB . ILE A 1 203 ? 63.524 95.285 10.493 1.00 37.69 ? 217 ILE A CB 1 ATOM 1589 C CG1 . ILE A 1 203 ? 62.874 96.530 11.113 1.00 33.16 ? 217 ILE A CG1 1 ATOM 1590 C CG2 . ILE A 1 203 ? 64.854 95.678 9.813 1.00 37.45 ? 217 ILE A CG2 1 ATOM 1591 C CD1 . ILE A 1 203 ? 61.619 96.238 11.933 1.00 30.34 ? 217 ILE A CD1 1 ATOM 1592 N N . SER A 1 204 ? 63.143 95.448 7.288 1.00 37.93 ? 218 SER A N 1 ATOM 1593 C CA . SER A 1 204 ? 63.056 96.341 6.131 1.00 39.07 ? 218 SER A CA 1 ATOM 1594 C C . SER A 1 204 ? 61.749 96.201 5.347 1.00 38.96 ? 218 SER A C 1 ATOM 1595 O O . SER A 1 204 ? 61.088 97.195 5.071 1.00 40.65 ? 218 SER A O 1 ATOM 1596 C CB . SER A 1 204 ? 64.254 96.143 5.207 1.00 38.78 ? 218 SER A CB 1 ATOM 1597 O OG . SER A 1 204 ? 65.446 96.603 5.830 1.00 39.48 ? 218 SER A OG 1 ATOM 1598 N N . SER A 1 205 ? 61.358 94.981 4.997 1.00 39.69 ? 219 SER A N 1 ATOM 1599 C CA . SER A 1 205 ? 60.101 94.812 4.280 1.00 42.38 ? 219 SER A CA 1 ATOM 1600 C C . SER A 1 205 ? 58.885 95.045 5.183 1.00 44.30 ? 219 SER A C 1 ATOM 1601 O O . SER A 1 205 ? 57.842 95.491 4.712 1.00 43.76 ? 219 SER A O 1 ATOM 1602 C CB . SER A 1 205 ? 60.028 93.444 3.596 1.00 45.32 ? 219 SER A CB 1 ATOM 1603 O OG . SER A 1 205 ? 60.198 92.392 4.524 1.00 49.56 ? 219 SER A OG 1 ATOM 1604 N N . SER A 1 206 ? 59.020 94.754 6.474 1.00 45.41 ? 220 SER A N 1 ATOM 1605 C CA . SER A 1 206 ? 57.947 95.037 7.422 1.00 42.62 ? 220 SER A CA 1 ATOM 1606 C C . SER A 1 206 ? 57.598 96.526 7.452 1.00 35.98 ? 220 SER A C 1 ATOM 1607 O O . SER A 1 206 ? 56.424 96.906 7.516 1.00 35.47 ? 220 SER A O 1 ATOM 1608 C CB . SER A 1 206 ? 58.343 94.570 8.825 1.00 43.41 ? 220 SER A CB 1 ATOM 1609 O OG . SER A 1 206 ? 58.412 93.157 8.864 1.00 37.52 ? 220 SER A OG 1 ATOM 1610 N N . LEU A 1 207 ? 58.625 97.356 7.412 1.00 33.35 ? 221 LEU A N 1 ATOM 1611 C CA . LEU A 1 207 ? 58.434 98.798 7.392 1.00 41.42 ? 221 LEU A CA 1 ATOM 1612 C C . LEU A 1 207 ? 57.769 99.310 6.094 1.00 44.76 ? 221 LEU A C 1 ATOM 1613 O O . LEU A 1 207 ? 57.280 100.429 6.069 1.00 46.40 ? 221 LEU A O 1 ATOM 1614 C CB . LEU A 1 207 ? 59.763 99.512 7.601 1.00 42.76 ? 221 LEU A CB 1 ATOM 1615 C CG . LEU A 1 207 ? 60.433 99.413 8.966 1.00 47.81 ? 221 LEU A CG 1 ATOM 1616 C CD1 . LEU A 1 207 ? 61.658 100.288 8.992 1.00 49.30 ? 221 LEU A CD1 1 ATOM 1617 C CD2 . LEU A 1 207 ? 59.470 99.819 10.058 1.00 47.78 ? 221 LEU A CD2 1 ATOM 1618 N N . LEU A 1 208 ? 57.751 98.516 5.023 1.00 43.69 ? 222 LEU A N 1 ATOM 1619 C CA . LEU A 1 208 ? 57.193 99.006 3.754 1.00 44.87 ? 222 LEU A CA 1 ATOM 1620 C C . LEU A 1 208 ? 55.736 98.591 3.647 1.00 44.78 ? 222 LEU A C 1 ATOM 1621 O O . LEU A 1 208 ? 54.952 99.213 2.942 1.00 47.88 ? 222 LEU A O 1 ATOM 1622 C CB . LEU A 1 208 ? 57.967 98.448 2.558 1.00 46.10 ? 222 LEU A CB 1 ATOM 1623 C CG . LEU A 1 208 ? 59.383 98.957 2.296 1.00 48.01 ? 222 LEU A CG 1 ATOM 1624 C CD1 . LEU A 1 208 ? 59.978 98.211 1.102 1.00 49.40 ? 222 LEU A CD1 1 ATOM 1625 C CD2 . LEU A 1 208 ? 59.382 100.438 2.020 1.00 46.76 ? 222 LEU A CD2 1 ATOM 1626 N N . LEU A 1 209 ? 55.382 97.544 4.388 1.00 43.65 ? 223 LEU A N 1 ATOM 1627 C CA . LEU A 1 209 ? 54.073 96.935 4.309 1.00 45.86 ? 223 LEU A CA 1 ATOM 1628 C C . LEU A 1 209 ? 53.159 97.419 5.432 1.00 47.63 ? 223 LEU A C 1 ATOM 1629 O O . LEU A 1 209 ? 51.945 97.185 5.390 1.00 44.08 ? 223 LEU A O 1 ATOM 1630 C CB . LEU A 1 209 ? 54.216 95.409 4.398 1.00 50.17 ? 223 LEU A CB 1 ATOM 1631 C CG . LEU A 1 209 ? 54.812 94.645 3.211 1.00 55.60 ? 223 LEU A CG 1 ATOM 1632 C CD1 . LEU A 1 209 ? 55.225 93.249 3.644 1.00 56.86 ? 223 LEU A CD1 1 ATOM 1633 C CD2 . LEU A 1 209 ? 53.802 94.555 2.080 1.00 52.64 ? 223 LEU A CD2 1 ATOM 1634 N N . ASP A 1 210 ? 53.749 98.069 6.440 1.00 46.30 ? 224 ASP A N 1 ATOM 1635 C CA . ASP A 1 210 ? 53.018 98.460 7.644 1.00 45.31 ? 224 ASP A CA 1 ATOM 1636 C C . ASP A 1 210 ? 53.357 99.908 7.957 1.00 45.51 ? 224 ASP A C 1 ATOM 1637 O O . ASP A 1 210 ? 54.450 100.221 8.452 1.00 44.40 ? 224 ASP A O 1 ATOM 1638 C CB . ASP A 1 210 ? 53.409 97.546 8.814 1.00 48.81 ? 224 ASP A CB 1 ATOM 1639 C CG . ASP A 1 210 ? 52.661 97.872 10.118 1.00 49.29 ? 224 ASP A CG 1 ATOM 1640 O OD1 . ASP A 1 210 ? 52.041 98.956 10.216 1.00 46.80 ? 224 ASP A OD1 1 ATOM 1641 O OD2 . ASP A 1 210 ? 52.709 97.030 11.055 1.00 48.50 ? 224 ASP A OD2 1 ATOM 1642 N N . GLN A 1 211 ? 52.422 100.800 7.658 1.00 45.12 ? 225 GLN A N 1 ATOM 1643 C CA . GLN A 1 211 ? 52.647 102.222 7.869 1.00 45.83 ? 225 GLN A CA 1 ATOM 1644 C C . GLN A 1 211 ? 52.779 102.572 9.366 1.00 42.37 ? 225 GLN A C 1 ATOM 1645 O O . GLN A 1 211 ? 53.566 103.440 9.747 1.00 35.83 ? 225 GLN A O 1 ATOM 1646 C CB . GLN A 1 211 ? 51.502 103.009 7.239 1.00 46.97 ? 225 GLN A CB 1 ATOM 1647 C CG . GLN A 1 211 ? 51.678 104.504 7.332 1.00 52.95 ? 225 GLN A CG 1 ATOM 1648 C CD . GLN A 1 211 ? 50.500 105.249 6.763 1.00 59.27 ? 225 GLN A CD 1 ATOM 1649 O OE1 . GLN A 1 211 ? 49.568 104.642 6.223 1.00 62.64 ? 225 GLN A OE1 1 ATOM 1650 N NE2 . GLN A 1 211 ? 50.524 106.570 6.886 1.00 62.53 ? 225 GLN A NE2 1 ATOM 1651 N N . GLU A 1 212 ? 52.003 101.902 10.210 1.00 41.42 ? 226 GLU A N 1 ATOM 1652 C CA . GLU A 1 212 ? 52.050 102.209 11.636 1.00 46.77 ? 226 GLU A CA 1 ATOM 1653 C C . GLU A 1 212 ? 53.417 101.853 12.213 1.00 44.12 ? 226 GLU A C 1 ATOM 1654 O O . GLU A 1 212 ? 53.932 102.563 13.075 1.00 44.40 ? 226 GLU A O 1 ATOM 1655 C CB . GLU A 1 212 ? 50.916 101.504 12.399 1.00 52.68 ? 226 GLU A CB 1 ATOM 1656 C CG . GLU A 1 212 ? 49.515 102.061 12.099 1.00 59.86 ? 226 GLU A CG 1 ATOM 1657 C CD . GLU A 1 212 ? 49.454 103.599 12.130 1.00 69.08 ? 226 GLU A CD 1 ATOM 1658 O OE1 . GLU A 1 212 ? 49.953 104.220 13.102 1.00 72.74 ? 226 GLU A OE1 1 ATOM 1659 O OE2 . GLU A 1 212 ? 48.907 104.192 11.173 1.00 72.22 ? 226 GLU A OE2 1 ATOM 1660 N N . LEU A 1 213 ? 54.012 100.773 11.709 1.00 37.24 ? 227 LEU A N 1 ATOM 1661 C CA . LEU A 1 213 ? 55.342 100.361 12.143 1.00 35.38 ? 227 LEU A CA 1 ATOM 1662 C C . LEU A 1 213 ? 56.389 101.328 11.627 1.00 38.87 ? 227 LEU A C 1 ATOM 1663 O O . LEU A 1 213 ? 57.335 101.709 12.343 1.00 39.32 ? 227 LEU A O 1 ATOM 1664 C CB . LEU A 1 213 ? 55.635 98.945 11.634 1.00 32.64 ? 227 LEU A CB 1 ATOM 1665 C CG . LEU A 1 213 ? 56.941 98.327 12.148 1.00 38.67 ? 227 LEU A CG 1 ATOM 1666 C CD1 . LEU A 1 213 ? 56.933 98.280 13.685 1.00 32.51 ? 227 LEU A CD1 1 ATOM 1667 C CD2 . LEU A 1 213 ? 57.124 96.922 11.559 1.00 43.80 ? 227 LEU A CD2 1 ATOM 1668 N N . TRP A 1 214 ? 56.213 101.738 10.371 1.00 39.53 ? 228 TRP A N 1 ATOM 1669 C CA . TRP A 1 214 ? 57.107 102.709 9.755 1.00 39.32 ? 228 TRP A CA 1 ATOM 1670 C C . TRP A 1 214 ? 57.190 103.977 10.592 1.00 35.64 ? 228 TRP A C 1 ATOM 1671 O O . TRP A 1 214 ? 58.264 104.581 10.728 1.00 36.09 ? 228 TRP A O 1 ATOM 1672 C CB . TRP A 1 214 ? 56.628 103.042 8.330 1.00 44.14 ? 228 TRP A CB 1 ATOM 1673 C CG . TRP A 1 214 ? 57.601 103.872 7.546 1.00 45.82 ? 228 TRP A CG 1 ATOM 1674 C CD1 . TRP A 1 214 ? 58.547 103.416 6.671 1.00 47.53 ? 228 TRP A CD1 1 ATOM 1675 C CD2 . TRP A 1 214 ? 57.732 105.307 7.560 1.00 47.42 ? 228 TRP A CD2 1 ATOM 1676 N NE1 . TRP A 1 214 ? 59.262 104.476 6.147 1.00 45.24 ? 228 TRP A NE1 1 ATOM 1677 C CE2 . TRP A 1 214 ? 58.781 105.643 6.674 1.00 45.06 ? 228 TRP A CE2 1 ATOM 1678 C CE3 . TRP A 1 214 ? 57.067 106.333 8.239 1.00 48.12 ? 228 TRP A CE3 1 ATOM 1679 C CZ2 . TRP A 1 214 ? 59.181 106.973 6.443 1.00 49.38 ? 228 TRP A CZ2 1 ATOM 1680 C CZ3 . TRP A 1 214 ? 57.466 107.644 8.020 1.00 53.23 ? 228 TRP A CZ3 1 ATOM 1681 C CH2 . TRP A 1 214 ? 58.513 107.955 7.122 1.00 52.98 ? 228 TRP A CH2 1 ATOM 1682 N N . LYS A 1 215 ? 56.074 104.393 11.180 1.00 38.82 ? 229 LYS A N 1 ATOM 1683 C CA . LYS A 1 215 ? 56.111 105.631 11.974 1.00 44.92 ? 229 LYS A CA 1 ATOM 1684 C C . LYS A 1 215 ? 56.960 105.519 13.252 1.00 42.00 ? 229 LYS A C 1 ATOM 1685 O O . LYS A 1 215 ? 57.653 106.467 13.621 1.00 42.08 ? 229 LYS A O 1 ATOM 1686 C CB . LYS A 1 215 ? 54.697 106.113 12.304 1.00 49.60 ? 229 LYS A CB 1 ATOM 1687 C CG . LYS A 1 215 ? 53.876 106.437 11.059 1.00 55.05 ? 229 LYS A CG 1 ATOM 1688 C CD . LYS A 1 215 ? 52.445 106.860 11.397 1.00 59.12 ? 229 LYS A CD 1 ATOM 1689 C CE . LYS A 1 215 ? 51.627 107.055 10.115 1.00 63.63 ? 229 LYS A CE 1 ATOM 1690 N NZ . LYS A 1 215 ? 50.209 107.462 10.359 1.00 65.83 ? 229 LYS A NZ 1 ATOM 1691 N N . VAL A 1 216 ? 56.952 104.353 13.890 1.00 36.22 ? 230 VAL A N 1 ATOM 1692 C CA . VAL A 1 216 ? 57.602 104.207 15.203 1.00 33.27 ? 230 VAL A CA 1 ATOM 1693 C C . VAL A 1 216 ? 59.089 103.840 15.150 1.00 39.08 ? 230 VAL A C 1 ATOM 1694 O O . VAL A 1 216 ? 59.770 103.903 16.161 1.00 42.25 ? 230 VAL A O 1 ATOM 1695 C CB . VAL A 1 216 ? 56.827 103.223 16.080 1.00 34.72 ? 230 VAL A CB 1 ATOM 1696 C CG1 . VAL A 1 216 ? 55.383 103.688 16.203 1.00 36.46 ? 230 VAL A CG1 1 ATOM 1697 C CG2 . VAL A 1 216 ? 56.842 101.838 15.462 1.00 32.24 ? 230 VAL A CG2 1 ATOM 1698 N N . VAL A 1 217 ? 59.607 103.502 13.971 1.00 40.14 ? 231 VAL A N 1 ATOM 1699 C CA . VAL A 1 217 ? 61.010 103.093 13.851 1.00 38.80 ? 231 VAL A CA 1 ATOM 1700 C C . VAL A 1 217 ? 61.850 104.201 13.233 1.00 44.84 ? 231 VAL A C 1 ATOM 1701 O O . VAL A 1 217 ? 61.649 104.565 12.076 1.00 44.61 ? 231 VAL A O 1 ATOM 1702 C CB . VAL A 1 217 ? 61.143 101.804 12.995 1.00 36.39 ? 231 VAL A CB 1 ATOM 1703 C CG1 . VAL A 1 217 ? 62.625 101.438 12.763 1.00 36.40 ? 231 VAL A CG1 1 ATOM 1704 C CG2 . VAL A 1 217 ? 60.386 100.665 13.646 1.00 34.90 ? 231 VAL A CG2 1 ATOM 1705 N N . ASP A 1 218 ? 62.803 104.735 13.984 1.00 46.29 ? 232 ASP A N 1 ATOM 1706 C CA . ASP A 1 218 ? 63.557 105.860 13.467 1.00 46.54 ? 232 ASP A CA 1 ATOM 1707 C C . ASP A 1 218 ? 64.794 105.427 12.684 1.00 45.79 ? 232 ASP A C 1 ATOM 1708 O O . ASP A 1 218 ? 65.221 106.117 11.757 1.00 47.84 ? 232 ASP A O 1 ATOM 1709 C CB . ASP A 1 218 ? 63.921 106.823 14.601 1.00 46.83 ? 232 ASP A CB 1 ATOM 1710 C CG . ASP A 1 218 ? 62.716 107.182 15.459 1.00 50.37 ? 232 ASP A CG 1 ATOM 1711 O OD1 . ASP A 1 218 ? 61.905 108.025 15.017 1.00 54.56 ? 232 ASP A OD1 1 ATOM 1712 O OD2 . ASP A 1 218 ? 62.568 106.616 16.570 1.00 49.05 ? 232 ASP A OD2 1 ATOM 1713 N N . VAL A 1 219 ? 65.372 104.288 13.054 1.00 42.13 ? 233 VAL A N 1 ATOM 1714 C CA . VAL A 1 219 ? 66.642 103.857 12.469 1.00 41.34 ? 233 VAL A CA 1 ATOM 1715 C C . VAL A 1 219 ? 66.647 102.356 12.208 1.00 42.37 ? 233 VAL A C 1 ATOM 1716 O O . VAL A 1 219 ? 66.228 101.569 13.072 1.00 36.12 ? 233 VAL A O 1 ATOM 1717 C CB . VAL A 1 219 ? 67.844 104.221 13.372 1.00 41.34 ? 233 VAL A CB 1 ATOM 1718 C CG1 . VAL A 1 219 ? 69.155 103.740 12.739 1.00 39.29 ? 233 VAL A CG1 1 ATOM 1719 C CG2 . VAL A 1 219 ? 67.912 105.731 13.609 1.00 41.57 ? 233 VAL A CG2 1 ATOM 1720 N N . ILE A 1 220 ? 67.090 101.954 11.012 1.00 42.41 ? 234 ILE A N 1 ATOM 1721 C CA . ILE A 1 220 ? 67.273 100.528 10.751 1.00 43.38 ? 234 ILE A CA 1 ATOM 1722 C C . ILE A 1 220 ? 68.715 100.175 11.082 1.00 39.93 ? 234 ILE A C 1 ATOM 1723 O O . ILE A 1 220 ? 69.638 100.620 10.406 1.00 41.10 ? 234 ILE A O 1 ATOM 1724 C CB . ILE A 1 220 ? 66.942 100.122 9.286 1.00 41.01 ? 234 ILE A CB 1 ATOM 1725 C CG1 . ILE A 1 220 ? 65.499 100.499 8.939 1.00 41.93 ? 234 ILE A CG1 1 ATOM 1726 C CG2 . ILE A 1 220 ? 67.118 98.608 9.094 1.00 35.06 ? 234 ILE A CG2 1 ATOM 1727 C CD1 . ILE A 1 220 ? 65.118 100.242 7.456 1.00 45.85 ? 234 ILE A CD1 1 ATOM 1728 N N . GLY A 1 221 ? 68.911 99.398 12.143 1.00 36.66 ? 235 GLY A N 1 ATOM 1729 C CA . GLY A 1 221 ? 70.252 99.025 12.568 1.00 36.38 ? 235 GLY A CA 1 ATOM 1730 C C . GLY A 1 221 ? 70.496 97.570 12.212 1.00 40.02 ? 235 GLY A C 1 ATOM 1731 O O . GLY A 1 221 ? 69.766 96.675 12.677 1.00 41.95 ? 235 GLY A O 1 ATOM 1732 N N . ALA A 1 222 ? 71.507 97.326 11.381 1.00 40.24 ? 236 ALA A N 1 ATOM 1733 C CA . ALA A 1 222 ? 71.808 95.970 10.946 1.00 42.57 ? 236 ALA A CA 1 ATOM 1734 C C . ALA A 1 222 ? 73.193 95.549 11.425 1.00 40.02 ? 236 ALA A C 1 ATOM 1735 O O . ALA A 1 222 ? 74.077 96.394 11.625 1.00 37.04 ? 236 ALA A O 1 ATOM 1736 C CB . ALA A 1 222 ? 71.700 95.864 9.408 1.00 44.31 ? 236 ALA A CB 1 ATOM 1737 N N . HIS A 1 223 ? 73.394 94.244 11.584 1.00 40.92 ? 237 HIS A N 1 ATOM 1738 C CA . HIS A 1 223 ? 74.666 93.725 12.103 1.00 44.44 ? 237 HIS A CA 1 ATOM 1739 C C . HIS A 1 223 ? 75.579 93.077 11.054 1.00 44.65 ? 237 HIS A C 1 ATOM 1740 O O . HIS A 1 223 ? 75.114 92.290 10.234 1.00 44.64 ? 237 HIS A O 1 ATOM 1741 C CB . HIS A 1 223 ? 74.373 92.727 13.212 1.00 42.34 ? 237 HIS A CB 1 ATOM 1742 C CG . HIS A 1 223 ? 73.888 93.370 14.472 1.00 43.70 ? 237 HIS A CG 1 ATOM 1743 N ND1 . HIS A 1 223 ? 73.747 92.678 15.654 1.00 43.21 ? 237 HIS A ND1 1 ATOM 1744 C CD2 . HIS A 1 223 ? 73.543 94.652 14.742 1.00 43.92 ? 237 HIS A CD2 1 ATOM 1745 C CE1 . HIS A 1 223 ? 73.327 93.503 16.598 1.00 43.65 ? 237 HIS A CE1 1 ATOM 1746 N NE2 . HIS A 1 223 ? 73.190 94.706 16.071 1.00 43.87 ? 237 HIS A NE2 1 ATOM 1747 N N . TYR A 1 224 ? 76.870 93.414 11.096 1.00 45.72 ? 238 TYR A N 1 ATOM 1748 C CA . TYR A 1 224 ? 77.882 92.810 10.215 1.00 44.41 ? 238 TYR A CA 1 ATOM 1749 C C . TYR A 1 224 ? 77.421 92.708 8.764 1.00 44.60 ? 238 TYR A C 1 ATOM 1750 O O . TYR A 1 224 ? 77.407 91.616 8.188 1.00 41.90 ? 238 TYR A O 1 ATOM 1751 C CB . TYR A 1 224 ? 78.279 91.431 10.762 1.00 45.56 ? 238 TYR A CB 1 ATOM 1752 C CG . TYR A 1 224 ? 78.746 91.541 12.195 1.00 46.36 ? 238 TYR A CG 1 ATOM 1753 C CD1 . TYR A 1 224 ? 80.065 91.855 12.481 1.00 46.21 ? 238 TYR A CD1 1 ATOM 1754 C CD2 . TYR A 1 224 ? 77.863 91.389 13.248 1.00 39.63 ? 238 TYR A CD2 1 ATOM 1755 C CE1 . TYR A 1 224 ? 80.502 91.984 13.778 1.00 46.58 ? 238 TYR A CE1 1 ATOM 1756 C CE2 . TYR A 1 224 ? 78.291 91.523 14.573 1.00 43.08 ? 238 TYR A CE2 1 ATOM 1757 C CZ . TYR A 1 224 ? 79.617 91.823 14.820 1.00 44.55 ? 238 TYR A CZ 1 ATOM 1758 O OH . TYR A 1 224 ? 80.088 91.970 16.106 1.00 46.18 ? 238 TYR A OH 1 ATOM 1759 N N . PRO A 1 225 ? 77.041 93.849 8.169 1.00 46.57 ? 239 PRO A N 1 ATOM 1760 C CA . PRO A 1 225 ? 76.374 93.827 6.862 1.00 50.47 ? 239 PRO A CA 1 ATOM 1761 C C . PRO A 1 225 ? 77.365 93.771 5.704 1.00 49.91 ? 239 PRO A C 1 ATOM 1762 O O . PRO A 1 225 ? 76.943 93.852 4.541 1.00 48.15 ? 239 PRO A O 1 ATOM 1763 C CB . PRO A 1 225 ? 75.671 95.185 6.829 1.00 50.50 ? 239 PRO A CB 1 ATOM 1764 C CG . PRO A 1 225 ? 76.671 96.091 7.522 1.00 49.52 ? 239 PRO A CG 1 ATOM 1765 C CD . PRO A 1 225 ? 77.283 95.232 8.630 1.00 49.26 ? 239 PRO A CD 1 ATOM 1766 N N . GLY A 1 226 ? 78.654 93.653 6.009 1.00 47.95 ? 240 GLY A N 1 ATOM 1767 C CA . GLY A 1 226 ? 79.656 93.535 4.961 1.00 47.80 ? 240 GLY A CA 1 ATOM 1768 C C . GLY A 1 226 ? 79.636 94.691 3.979 1.00 50.67 ? 240 GLY A C 1 ATOM 1769 O O . GLY A 1 226 ? 79.753 94.489 2.768 1.00 54.19 ? 240 GLY A O 1 ATOM 1770 N N . THR A 1 227 ? 79.469 95.898 4.515 1.00 49.70 ? 241 THR A N 1 ATOM 1771 C CA . THR A 1 227 ? 79.510 97.164 3.761 1.00 47.29 ? 241 THR A CA 1 ATOM 1772 C C . THR A 1 227 ? 78.290 97.418 2.859 1.00 49.32 ? 241 THR A C 1 ATOM 1773 O O . THR A 1 227 ? 78.165 98.494 2.267 1.00 51.13 ? 241 THR A O 1 ATOM 1774 C CB . THR A 1 227 ? 80.858 97.380 2.991 1.00 54.09 ? 241 THR A CB 1 ATOM 1775 O OG1 . THR A 1 227 ? 80.933 96.542 1.826 1.00 52.75 ? 241 THR A OG1 1 ATOM 1776 C CG2 . THR A 1 227 ? 82.043 97.105 3.904 1.00 50.52 ? 241 THR A CG2 1 ATOM 1777 N N . TYR A 1 228 ? 77.373 96.453 2.810 1.00 47.89 ? 242 TYR A N 1 ATOM 1778 C CA . TYR A 1 228 ? 76.209 96.551 1.934 1.00 51.42 ? 242 TYR A CA 1 ATOM 1779 C C . TYR A 1 228 ? 74.876 96.607 2.678 1.00 50.60 ? 242 TYR A C 1 ATOM 1780 O O . TYR A 1 228 ? 74.761 96.101 3.800 1.00 54.47 ? 242 TYR A O 1 ATOM 1781 C CB . TYR A 1 228 ? 76.192 95.380 0.943 1.00 53.72 ? 242 TYR A CB 1 ATOM 1782 C CG . TYR A 1 228 ? 77.330 95.425 -0.043 1.00 58.94 ? 242 TYR A CG 1 ATOM 1783 C CD1 . TYR A 1 228 ? 77.358 96.372 -1.062 1.00 64.77 ? 242 TYR A CD1 1 ATOM 1784 C CD2 . TYR A 1 228 ? 78.383 94.525 0.044 1.00 61.49 ? 242 TYR A CD2 1 ATOM 1785 C CE1 . TYR A 1 228 ? 78.412 96.417 -1.978 1.00 66.22 ? 242 TYR A CE1 1 ATOM 1786 C CE2 . TYR A 1 228 ? 79.433 94.565 -0.851 1.00 63.86 ? 242 TYR A CE2 1 ATOM 1787 C CZ . TYR A 1 228 ? 79.442 95.509 -1.861 1.00 66.64 ? 242 TYR A CZ 1 ATOM 1788 O OH . TYR A 1 228 ? 80.489 95.538 -2.748 1.00 70.39 ? 242 TYR A OH 1 ATOM 1789 N N . THR A 1 229 ? 73.879 97.230 2.046 1.00 44.99 ? 243 THR A N 1 ATOM 1790 C CA . THR A 1 229 ? 72.492 97.174 2.520 1.00 40.89 ? 243 THR A CA 1 ATOM 1791 C C . THR A 1 229 ? 71.657 96.415 1.458 1.00 48.60 ? 243 THR A C 1 ATOM 1792 O O . THR A 1 229 ? 72.234 95.731 0.623 1.00 50.10 ? 243 THR A O 1 ATOM 1793 C CB . THR A 1 229 ? 71.951 98.591 2.837 1.00 43.97 ? 243 THR A CB 1 ATOM 1794 O OG1 . THR A 1 229 ? 70.672 98.499 3.473 1.00 45.09 ? 243 THR A OG1 1 ATOM 1795 C CG2 . THR A 1 229 ? 71.844 99.453 1.570 1.00 42.13 ? 243 THR A CG2 1 ATOM 1796 N N . VAL A 1 230 ? 70.330 96.490 1.511 1.00 46.06 ? 244 VAL A N 1 ATOM 1797 C CA . VAL A 1 230 ? 69.467 95.783 0.552 1.00 47.18 ? 244 VAL A CA 1 ATOM 1798 C C . VAL A 1 230 ? 68.404 96.771 0.083 1.00 50.88 ? 244 VAL A C 1 ATOM 1799 O O . VAL A 1 230 ? 68.206 97.821 0.707 1.00 49.42 ? 244 VAL A O 1 ATOM 1800 C CB . VAL A 1 230 ? 68.725 94.555 1.166 1.00 51.02 ? 244 VAL A CB 1 ATOM 1801 C CG1 . VAL A 1 230 ? 69.690 93.505 1.727 1.00 52.88 ? 244 VAL A CG1 1 ATOM 1802 C CG2 . VAL A 1 230 ? 67.758 95.006 2.252 1.00 45.85 ? 244 VAL A CG2 1 ATOM 1803 N N . TRP A 1 231 ? 67.694 96.429 -0.987 1.00 52.15 ? 245 TRP A N 1 ATOM 1804 C CA . TRP A 1 231 ? 66.837 97.404 -1.646 1.00 50.68 ? 245 TRP A CA 1 ATOM 1805 C C . TRP A 1 231 ? 65.686 97.932 -0.779 1.00 43.37 ? 245 TRP A C 1 ATOM 1806 O O . TRP A 1 231 ? 65.447 99.140 -0.730 1.00 45.61 ? 245 TRP A O 1 ATOM 1807 C CB . TRP A 1 231 ? 66.301 96.846 -2.959 1.00 53.42 ? 245 TRP A CB 1 ATOM 1808 C CG . TRP A 1 231 ? 65.794 97.928 -3.822 1.00 53.56 ? 245 TRP A CG 1 ATOM 1809 C CD1 . TRP A 1 231 ? 66.533 98.875 -4.489 1.00 57.44 ? 245 TRP A CD1 1 ATOM 1810 C CD2 . TRP A 1 231 ? 64.430 98.212 -4.099 1.00 50.82 ? 245 TRP A CD2 1 ATOM 1811 N NE1 . TRP A 1 231 ? 65.694 99.720 -5.186 1.00 58.73 ? 245 TRP A NE1 1 ATOM 1812 C CE2 . TRP A 1 231 ? 64.398 99.337 -4.954 1.00 53.72 ? 245 TRP A CE2 1 ATOM 1813 C CE3 . TRP A 1 231 ? 63.230 97.628 -3.710 1.00 51.31 ? 245 TRP A CE3 1 ATOM 1814 C CZ2 . TRP A 1 231 ? 63.210 99.879 -5.420 1.00 54.60 ? 245 TRP A CZ2 1 ATOM 1815 C CZ3 . TRP A 1 231 ? 62.050 98.167 -4.179 1.00 56.77 ? 245 TRP A CZ3 1 ATOM 1816 C CH2 . TRP A 1 231 ? 62.046 99.279 -5.024 1.00 55.24 ? 245 TRP A CH2 1 ATOM 1817 N N . ASN A 1 232 ? 64.991 97.031 -0.098 1.00 38.21 ? 246 ASN A N 1 ATOM 1818 C CA . ASN A 1 232 ? 63.885 97.401 0.791 1.00 37.83 ? 246 ASN A CA 1 ATOM 1819 C C . ASN A 1 232 ? 64.298 98.459 1.835 1.00 44.25 ? 246 ASN A C 1 ATOM 1820 O O . ASN A 1 232 ? 63.473 99.269 2.260 1.00 45.01 ? 246 ASN A O 1 ATOM 1821 C CB . ASN A 1 232 ? 63.311 96.157 1.485 1.00 35.94 ? 246 ASN A CB 1 ATOM 1822 C CG . ASN A 1 232 ? 62.437 95.327 0.569 1.00 43.48 ? 246 ASN A CG 1 ATOM 1823 O OD1 . ASN A 1 232 ? 62.079 95.764 -0.526 1.00 43.38 ? 246 ASN A OD1 1 ATOM 1824 N ND2 . ASN A 1 232 ? 62.065 94.126 1.023 1.00 38.79 ? 246 ASN A ND2 1 ATOM 1825 N N . ALA A 1 233 ? 65.577 98.460 2.216 1.00 43.12 ? 247 ALA A N 1 ATOM 1826 C CA . ALA A 1 233 ? 66.083 99.383 3.239 1.00 46.98 ? 247 ALA A CA 1 ATOM 1827 C C . ALA A 1 233 ? 66.243 100.788 2.674 1.00 47.33 ? 247 ALA A C 1 ATOM 1828 O O . ALA A 1 233 ? 65.836 101.766 3.302 1.00 43.19 ? 247 ALA A O 1 ATOM 1829 C CB . ALA A 1 233 ? 67.418 98.889 3.826 1.00 43.16 ? 247 ALA A CB 1 ATOM 1830 N N . LYS A 1 234 ? 66.849 100.883 1.493 1.00 48.17 ? 248 LYS A N 1 ATOM 1831 C CA . LYS A 1 234 ? 66.940 102.156 0.784 1.00 50.05 ? 248 LYS A CA 1 ATOM 1832 C C . LYS A 1 234 ? 65.545 102.747 0.552 1.00 46.39 ? 248 LYS A C 1 ATOM 1833 O O . LYS A 1 234 ? 65.312 103.936 0.775 1.00 45.55 ? 248 LYS A O 1 ATOM 1834 C CB . LYS A 1 234 ? 67.649 101.975 -0.561 1.00 55.52 ? 248 LYS A CB 1 ATOM 1835 C CG . LYS A 1 234 ? 68.970 101.212 -0.518 1.00 61.59 ? 248 LYS A CG 1 ATOM 1836 C CD . LYS A 1 234 ? 69.603 101.204 -1.920 1.00 69.55 ? 248 LYS A CD 1 ATOM 1837 C CE . LYS A 1 234 ? 70.810 100.268 -2.023 1.00 74.12 ? 248 LYS A CE 1 ATOM 1838 N NZ . LYS A 1 234 ? 72.125 100.952 -1.766 1.00 75.90 ? 248 LYS A NZ 1 ATOM 1839 N N . MET A 1 235 ? 64.618 101.905 0.113 1.00 47.79 ? 249 MET A N 1 ATOM 1840 C CA . MET A 1 235 ? 63.244 102.336 -0.135 1.00 52.89 ? 249 MET A CA 1 ATOM 1841 C C . MET A 1 235 ? 62.519 102.906 1.086 1.00 57.97 ? 249 MET A C 1 ATOM 1842 O O . MET A 1 235 ? 61.589 103.708 0.925 1.00 59.56 ? 249 MET A O 1 ATOM 1843 C CB . MET A 1 235 ? 62.417 101.181 -0.708 1.00 48.98 ? 249 MET A CB 1 ATOM 1844 C CG . MET A 1 235 ? 62.759 100.895 -2.137 1.00 55.27 ? 249 MET A CG 1 ATOM 1845 S SD . MET A 1 235 ? 62.337 102.295 -3.197 1.00 78.68 ? 249 MET A SD 1 ATOM 1846 C CE . MET A 1 235 ? 60.544 102.147 -3.183 1.00 44.49 ? 249 MET A CE 1 ATOM 1847 N N . SER A 1 236 ? 62.924 102.482 2.287 1.00 55.10 ? 250 SER A N 1 ATOM 1848 C CA . SER A 1 236 ? 62.255 102.919 3.516 1.00 51.50 ? 250 SER A CA 1 ATOM 1849 C C . SER A 1 236 ? 62.514 104.407 3.731 1.00 50.13 ? 250 SER A C 1 ATOM 1850 O O . SER A 1 236 ? 61.665 105.136 4.251 1.00 52.64 ? 250 SER A O 1 ATOM 1851 C CB . SER A 1 236 ? 62.768 102.142 4.733 1.00 43.86 ? 250 SER A CB 1 ATOM 1852 O OG . SER A 1 236 ? 64.086 102.560 5.060 1.00 48.01 ? 250 SER A OG 1 ATOM 1853 N N . GLY A 1 237 ? 63.691 104.853 3.323 1.00 47.09 ? 251 GLY A N 1 ATOM 1854 C CA . GLY A 1 237 ? 64.078 106.229 3.553 1.00 50.94 ? 251 GLY A CA 1 ATOM 1855 C C . GLY A 1 237 ? 64.444 106.438 5.011 1.00 54.21 ? 251 GLY A C 1 ATOM 1856 O O . GLY A 1 237 ? 64.560 107.576 5.467 1.00 58.20 ? 251 GLY A O 1 ATOM 1857 N N . LYS A 1 238 ? 64.621 105.339 5.747 1.00 50.05 ? 252 LYS A N 1 ATOM 1858 C CA . LYS A 1 238 ? 65.131 105.422 7.109 1.00 45.31 ? 252 LYS A CA 1 ATOM 1859 C C . LYS A 1 238 ? 66.653 105.557 7.130 1.00 44.08 ? 252 LYS A C 1 ATOM 1860 O O . LYS A 1 238 ? 67.344 105.151 6.186 1.00 47.13 ? 252 LYS A O 1 ATOM 1861 C CB . LYS A 1 238 ? 64.713 104.192 7.918 1.00 44.59 ? 252 LYS A CB 1 ATOM 1862 C CG . LYS A 1 238 ? 63.207 104.046 8.105 1.00 46.14 ? 252 LYS A CG 1 ATOM 1863 C CD . LYS A 1 238 ? 62.615 105.199 8.947 1.00 46.70 ? 252 LYS A CD 1 ATOM 1864 C CE . LYS A 1 238 ? 61.107 104.972 9.112 1.00 45.97 ? 252 LYS A CE 1 ATOM 1865 N NZ . LYS A 1 238 ? 60.443 106.025 9.928 1.00 43.70 ? 252 LYS A NZ 1 ATOM 1866 N N . LYS A 1 239 ? 67.168 106.161 8.194 1.00 41.90 ? 253 LYS A N 1 ATOM 1867 C CA . LYS A 1 239 ? 68.602 106.153 8.471 1.00 42.22 ? 253 LYS A CA 1 ATOM 1868 C C . LYS A 1 239 ? 69.077 104.703 8.592 1.00 41.30 ? 253 LYS A C 1 ATOM 1869 O O . LYS A 1 239 ? 68.412 103.878 9.227 1.00 41.03 ? 253 LYS A O 1 ATOM 1870 C CB . LYS A 1 239 ? 68.887 106.895 9.792 1.00 41.97 ? 253 LYS A CB 1 ATOM 1871 C CG . LYS A 1 239 ? 68.815 108.439 9.709 1.00 45.71 ? 253 LYS A CG 1 ATOM 1872 C CD . LYS A 1 239 ? 69.142 109.080 11.077 1.00 49.29 ? 253 LYS A CD 1 ATOM 1873 C CE . LYS A 1 239 ? 68.979 110.595 11.068 1.00 53.91 ? 253 LYS A CE 1 ATOM 1874 N NZ . LYS A 1 239 ? 69.749 111.209 9.945 1.00 62.11 ? 253 LYS A NZ 1 ATOM 1875 N N . LEU A 1 240 ? 70.220 104.388 7.986 1.00 40.62 ? 254 LEU A N 1 ATOM 1876 C CA . LEU A 1 240 ? 70.734 103.022 8.005 1.00 42.25 ? 254 LEU A CA 1 ATOM 1877 C C . LEU A 1 240 ? 72.052 103.024 8.760 1.00 45.37 ? 254 LEU A C 1 ATOM 1878 O O . LEU A 1 240 ? 72.978 103.748 8.393 1.00 46.13 ? 254 LEU A O 1 ATOM 1879 C CB . LEU A 1 240 ? 70.942 102.490 6.579 1.00 42.11 ? 254 LEU A CB 1 ATOM 1880 C CG . LEU A 1 240 ? 69.761 102.623 5.615 1.00 40.90 ? 254 LEU A CG 1 ATOM 1881 C CD1 . LEU A 1 240 ? 70.112 102.053 4.249 1.00 42.55 ? 254 LEU A CD1 1 ATOM 1882 C CD2 . LEU A 1 240 ? 68.541 101.929 6.160 1.00 39.79 ? 254 LEU A CD2 1 ATOM 1883 N N . TRP A 1 241 ? 72.128 102.220 9.821 1.00 43.55 ? 255 TRP A N 1 ATOM 1884 C CA . TRP A 1 241 ? 73.341 102.121 10.616 1.00 45.26 ? 255 TRP A CA 1 ATOM 1885 C C . TRP A 1 241 ? 73.874 100.700 10.621 1.00 43.47 ? 255 TRP A C 1 ATOM 1886 O O . TRP A 1 241 ? 73.103 99.743 10.683 1.00 44.60 ? 255 TRP A O 1 ATOM 1887 C CB . TRP A 1 241 ? 73.064 102.508 12.071 1.00 41.68 ? 255 TRP A CB 1 ATOM 1888 C CG . TRP A 1 241 ? 72.732 103.960 12.299 1.00 45.24 ? 255 TRP A CG 1 ATOM 1889 C CD1 . TRP A 1 241 ? 72.502 104.913 11.350 1.00 40.56 ? 255 TRP A CD1 1 ATOM 1890 C CD2 . TRP A 1 241 ? 72.571 104.614 13.574 1.00 45.93 ? 255 TRP A CD2 1 ATOM 1891 N NE1 . TRP A 1 241 ? 72.221 106.122 11.948 1.00 43.31 ? 255 TRP A NE1 1 ATOM 1892 C CE2 . TRP A 1 241 ? 72.258 105.967 13.313 1.00 46.14 ? 255 TRP A CE2 1 ATOM 1893 C CE3 . TRP A 1 241 ? 72.679 104.188 14.908 1.00 42.91 ? 255 TRP A CE3 1 ATOM 1894 C CZ2 . TRP A 1 241 ? 72.039 106.900 14.340 1.00 45.57 ? 255 TRP A CZ2 1 ATOM 1895 C CZ3 . TRP A 1 241 ? 72.475 105.122 15.938 1.00 41.86 ? 255 TRP A CZ3 1 ATOM 1896 C CH2 . TRP A 1 241 ? 72.153 106.457 15.645 1.00 47.92 ? 255 TRP A CH2 1 ATOM 1897 N N . SER A 1 242 ? 75.193 100.561 10.566 1.00 42.11 ? 256 SER A N 1 ATOM 1898 C CA . SER A 1 242 ? 75.802 99.306 10.966 1.00 42.83 ? 256 SER A CA 1 ATOM 1899 C C . SER A 1 242 ? 75.864 99.340 12.500 1.00 42.06 ? 256 SER A C 1 ATOM 1900 O O . SER A 1 242 ? 76.861 99.798 13.074 1.00 41.00 ? 256 SER A O 1 ATOM 1901 C CB . SER A 1 242 ? 77.202 99.174 10.364 1.00 43.08 ? 256 SER A CB 1 ATOM 1902 O OG . SER A 1 242 ? 77.689 97.854 10.540 1.00 46.11 ? 256 SER A OG 1 ATOM 1903 N N . SER A 1 243 ? 74.797 98.881 13.160 1.00 43.42 ? 257 SER A N 1 ATOM 1904 C CA . SER A 1 243 ? 74.689 99.038 14.617 1.00 42.57 ? 257 SER A CA 1 ATOM 1905 C C . SER A 1 243 ? 75.533 98.047 15.415 1.00 43.78 ? 257 SER A C 1 ATOM 1906 O O . SER A 1 243 ? 75.630 98.144 16.640 1.00 44.63 ? 257 SER A O 1 ATOM 1907 C CB . SER A 1 243 ? 73.227 99.010 15.081 1.00 42.39 ? 257 SER A CB 1 ATOM 1908 O OG . SER A 1 243 ? 72.586 97.777 14.790 1.00 40.80 ? 257 SER A OG 1 ATOM 1909 N N . GLU A 1 244 ? 76.128 97.084 14.726 1.00 43.85 ? 258 GLU A N 1 ATOM 1910 C CA . GLU A 1 244 ? 77.181 96.276 15.331 1.00 44.99 ? 258 GLU A CA 1 ATOM 1911 C C . GLU A 1 244 ? 78.077 95.705 14.242 1.00 47.49 ? 258 GLU A C 1 ATOM 1912 O O . GLU A 1 244 ? 77.610 94.995 13.345 1.00 46.31 ? 258 GLU A O 1 ATOM 1913 C CB . GLU A 1 244 ? 76.631 95.140 16.198 1.00 44.66 ? 258 GLU A CB 1 ATOM 1914 C CG . GLU A 1 244 ? 77.707 94.599 17.146 1.00 47.16 ? 258 GLU A CG 1 ATOM 1915 C CD . GLU A 1 244 ? 77.297 93.347 17.886 1.00 45.73 ? 258 GLU A CD 1 ATOM 1916 O OE1 . GLU A 1 244 ? 76.262 93.371 18.578 1.00 45.67 ? 258 GLU A OE1 1 ATOM 1917 O OE2 . GLU A 1 244 ? 78.021 92.335 17.784 1.00 45.83 ? 258 GLU A OE2 1 ATOM 1918 N N . ASP A 1 245 ? 79.368 96.010 14.333 1.00 47.65 ? 259 ASP A N 1 ATOM 1919 C CA . ASP A 1 245 ? 80.334 95.563 13.340 1.00 47.72 ? 259 ASP A CA 1 ATOM 1920 C C . ASP A 1 245 ? 81.663 95.313 14.040 1.00 51.95 ? 259 ASP A C 1 ATOM 1921 O O . ASP A 1 245 ? 81.722 95.323 15.287 1.00 48.60 ? 259 ASP A O 1 ATOM 1922 C CB . ASP A 1 245 ? 80.509 96.657 12.282 1.00 51.50 ? 259 ASP A CB 1 ATOM 1923 C CG . ASP A 1 245 ? 80.595 96.102 10.865 1.00 50.82 ? 259 ASP A CG 1 ATOM 1924 O OD1 . ASP A 1 245 ? 81.218 95.031 10.687 1.00 48.49 ? 259 ASP A OD1 1 ATOM 1925 O OD2 . ASP A 1 245 ? 80.048 96.741 9.934 1.00 50.60 ? 259 ASP A OD2 1 ATOM 1926 N N . PHE A 1 246 ? 82.718 95.112 13.240 1.00 50.43 ? 260 PHE A N 1 ATOM 1927 C CA . PHE A 1 246 ? 84.090 94.905 13.734 1.00 51.15 ? 260 PHE A CA 1 ATOM 1928 C C . PHE A 1 246 ? 84.311 93.514 14.352 1.00 50.68 ? 260 PHE A C 1 ATOM 1929 O O . PHE A 1 246 ? 84.502 92.544 13.608 1.00 48.39 ? 260 PHE A O 1 ATOM 1930 C CB . PHE A 1 246 ? 84.499 96.024 14.697 1.00 51.47 ? 260 PHE A CB 1 ATOM 1931 C CG . PHE A 1 246 ? 85.951 96.010 15.080 1.00 53.85 ? 260 PHE A CG 1 ATOM 1932 C CD1 . PHE A 1 246 ? 86.940 96.265 14.127 1.00 53.21 ? 260 PHE A CD1 1 ATOM 1933 C CD2 . PHE A 1 246 ? 86.329 95.788 16.397 1.00 53.02 ? 260 PHE A CD2 1 ATOM 1934 C CE1 . PHE A 1 246 ? 88.290 96.276 14.478 1.00 52.09 ? 260 PHE A CE1 1 ATOM 1935 C CE2 . PHE A 1 246 ? 87.684 95.795 16.763 1.00 53.43 ? 260 PHE A CE2 1 ATOM 1936 C CZ . PHE A 1 246 ? 88.667 96.041 15.790 1.00 52.22 ? 260 PHE A CZ 1 ATOM 1937 N N . SER A 1 247 ? 84.280 93.414 15.691 1.00 43.84 ? 261 SER A N 1 ATOM 1938 C CA . SER A 1 247 ? 84.476 92.122 16.373 1.00 42.60 ? 261 SER A CA 1 ATOM 1939 C C . SER A 1 247 ? 85.760 91.396 15.914 1.00 44.73 ? 261 SER A C 1 ATOM 1940 O O . SER A 1 247 ? 85.811 90.161 15.860 1.00 43.61 ? 261 SER A O 1 ATOM 1941 C CB . SER A 1 247 ? 83.245 91.221 16.186 1.00 46.05 ? 261 SER A CB 1 ATOM 1942 O OG . SER A 1 247 ? 83.398 89.984 16.862 1.00 49.97 ? 261 SER A OG 1 ATOM 1943 N N . THR A 1 248 ? 86.797 92.170 15.596 1.00 43.02 ? 262 THR A N 1 ATOM 1944 C CA . THR A 1 248 ? 88.050 91.588 15.130 1.00 49.59 ? 262 THR A CA 1 ATOM 1945 C C . THR A 1 248 ? 89.214 91.911 16.077 1.00 52.90 ? 262 THR A C 1 ATOM 1946 O O . THR A 1 248 ? 89.275 93.005 16.649 1.00 51.67 ? 262 THR A O 1 ATOM 1947 C CB . THR A 1 248 ? 88.350 92.049 13.688 1.00 52.59 ? 262 THR A CB 1 ATOM 1948 O OG1 . THR A 1 248 ? 87.180 91.838 12.880 1.00 52.31 ? 262 THR A OG1 1 ATOM 1949 C CG2 . THR A 1 248 ? 89.514 91.261 13.092 1.00 53.54 ? 262 THR A CG2 1 ATOM 1950 N N . ILE A 1 249 ? 90.116 90.945 16.263 1.00 54.89 ? 263 ILE A N 1 ATOM 1951 C CA . ILE A 1 249 ? 91.311 91.146 17.092 1.00 56.05 ? 263 ILE A CA 1 ATOM 1952 C C . ILE A 1 249 ? 92.014 92.463 16.756 1.00 57.25 ? 263 ILE A C 1 ATOM 1953 O O . ILE A 1 249 ? 92.230 92.785 15.581 1.00 47.61 ? 263 ILE A O 1 ATOM 1954 C CB . ILE A 1 249 ? 92.282 89.937 16.998 1.00 59.82 ? 263 ILE A CB 1 ATOM 1955 C CG1 . ILE A 1 249 ? 91.512 88.651 17.355 1.00 61.83 ? 263 ILE A CG1 1 ATOM 1956 C CG2 . ILE A 1 249 ? 93.508 90.147 17.901 1.00 58.15 ? 263 ILE A CG2 1 ATOM 1957 C CD1 . ILE A 1 249 ? 92.354 87.390 17.492 1.00 63.74 ? 263 ILE A CD1 1 ATOM 1958 N N . ASN A 1 250 ? 92.344 93.238 17.787 1.00 47.22 ? 264 ASN A N 1 ATOM 1959 C CA . ASN A 1 250 ? 92.818 94.599 17.553 1.00 50.46 ? 264 ASN A CA 1 ATOM 1960 C C . ASN A 1 250 ? 94.311 94.723 17.214 1.00 52.72 ? 264 ASN A C 1 ATOM 1961 O O . ASN A 1 250 ? 94.978 95.674 17.631 1.00 50.29 ? 264 ASN A O 1 ATOM 1962 C CB . ASN A 1 250 ? 92.406 95.550 18.688 1.00 48.23 ? 264 ASN A CB 1 ATOM 1963 C CG . ASN A 1 250 ? 92.980 95.158 20.045 1.00 51.90 ? 264 ASN A CG 1 ATOM 1964 O OD1 . ASN A 1 250 ? 93.936 94.384 20.141 1.00 54.61 ? 264 ASN A OD1 1 ATOM 1965 N ND2 . ASN A 1 250 ? 92.399 95.716 21.111 1.00 49.62 ? 264 ASN A ND2 1 ATOM 1966 N N . SER A 1 251 ? 94.819 93.755 16.457 1.00 54.71 ? 265 SER A N 1 ATOM 1967 C CA . SER A 1 251 ? 96.119 93.897 15.796 1.00 56.97 ? 265 SER A CA 1 ATOM 1968 C C . SER A 1 251 ? 95.984 94.867 14.630 1.00 59.12 ? 265 SER A C 1 ATOM 1969 O O . SER A 1 251 ? 94.922 95.464 14.413 1.00 57.96 ? 265 SER A O 1 ATOM 1970 C CB . SER A 1 251 ? 96.582 92.550 15.248 1.00 56.26 ? 265 SER A CB 1 ATOM 1971 O OG . SER A 1 251 ? 95.683 92.078 14.259 1.00 61.28 ? 265 SER A OG 1 ATOM 1972 N N . ASN A 1 252 ? 97.058 95.019 13.863 1.00 62.26 ? 266 ASN A N 1 ATOM 1973 C CA . ASN A 1 252 ? 96.986 95.818 12.648 1.00 63.98 ? 266 ASN A CA 1 ATOM 1974 C C . ASN A 1 252 ? 95.940 95.265 11.669 1.00 59.41 ? 266 ASN A C 1 ATOM 1975 O O . ASN A 1 252 ? 95.301 96.027 10.944 1.00 58.81 ? 266 ASN A O 1 ATOM 1976 C CB . ASN A 1 252 ? 98.355 95.878 11.975 1.00 70.94 ? 266 ASN A CB 1 ATOM 1977 C CG . ASN A 1 252 ? 98.830 94.515 11.530 1.00 76.86 ? 266 ASN A CG 1 ATOM 1978 O OD1 . ASN A 1 252 ? 99.257 93.702 12.349 1.00 80.13 ? 266 ASN A OD1 1 ATOM 1979 N ND2 . ASN A 1 252 ? 98.742 94.247 10.227 1.00 78.64 ? 266 ASN A ND2 1 ATOM 1980 N N . VAL A 1 253 ? 95.771 93.943 11.647 1.00 59.03 ? 267 VAL A N 1 ATOM 1981 C CA . VAL A 1 253 ? 94.758 93.312 10.795 1.00 61.56 ? 267 VAL A CA 1 ATOM 1982 C C . VAL A 1 253 ? 93.372 93.876 11.106 1.00 62.18 ? 267 VAL A C 1 ATOM 1983 O O . VAL A 1 253 ? 92.633 94.283 10.202 1.00 63.76 ? 267 VAL A O 1 ATOM 1984 C CB . VAL A 1 253 ? 94.751 91.770 10.966 1.00 74.48 ? 267 VAL A CB 1 ATOM 1985 C CG1 . VAL A 1 253 ? 93.469 91.156 10.424 1.00 73.73 ? 267 VAL A CG1 1 ATOM 1986 C CG2 . VAL A 1 253 ? 95.951 91.149 10.281 1.00 73.56 ? 267 VAL A CG2 1 ATOM 1987 N N . GLY A 1 254 ? 93.032 93.904 12.393 1.00 60.65 ? 268 GLY A N 1 ATOM 1988 C CA . GLY A 1 254 ? 91.765 94.457 12.845 1.00 55.99 ? 268 GLY A CA 1 ATOM 1989 C C . GLY A 1 254 ? 91.633 95.944 12.560 1.00 52.96 ? 268 GLY A C 1 ATOM 1990 O O . GLY A 1 254 ? 90.564 96.432 12.191 1.00 52.38 ? 268 GLY A O 1 ATOM 1991 N N . ALA A 1 255 ? 92.727 96.675 12.715 1.00 52.55 ? 269 ALA A N 1 ATOM 1992 C CA . ALA A 1 255 ? 92.698 98.095 12.425 1.00 52.94 ? 269 ALA A CA 1 ATOM 1993 C C . ALA A 1 255 ? 92.385 98.345 10.939 1.00 54.66 ? 269 ALA A C 1 ATOM 1994 O O . ALA A 1 255 ? 91.734 99.337 10.595 1.00 55.67 ? 269 ALA A O 1 ATOM 1995 C CB . ALA A 1 255 ? 93.997 98.724 12.808 1.00 53.20 ? 269 ALA A CB 1 ATOM 1996 N N . GLY A 1 256 ? 92.831 97.445 10.064 1.00 51.70 ? 270 GLY A N 1 ATOM 1997 C CA . GLY A 1 256 ? 92.598 97.619 8.636 1.00 53.04 ? 270 GLY A CA 1 ATOM 1998 C C . GLY A 1 256 ? 91.134 97.394 8.308 1.00 53.07 ? 270 GLY A C 1 ATOM 1999 O O . GLY A 1 256 ? 90.533 98.114 7.496 1.00 54.74 ? 270 GLY A O 1 ATOM 2000 N N . CYS A 1 257 ? 90.561 96.379 8.949 1.00 51.92 ? 271 CYS A N 1 ATOM 2001 C CA . CYS A 1 257 ? 89.154 96.052 8.779 1.00 48.78 ? 271 CYS A CA 1 ATOM 2002 C C . CYS A 1 257 ? 88.295 97.256 9.166 1.00 51.70 ? 271 CYS A C 1 ATOM 2003 O O . CYS A 1 257 ? 87.385 97.642 8.422 1.00 53.32 ? 271 CYS A O 1 ATOM 2004 C CB . CYS A 1 257 ? 88.817 94.803 9.604 1.00 50.73 ? 271 CYS A CB 1 ATOM 2005 S SG . CYS A 1 257 ? 87.082 94.629 10.213 1.00 61.42 ? 271 CYS A SG 1 ATOM 2006 N N . TRP A 1 258 ? 88.615 97.853 10.317 1.00 50.14 ? 272 TRP A N 1 ATOM 2007 C CA . TRP A 1 258 ? 87.878 98.996 10.860 1.00 48.09 ? 272 TRP A CA 1 ATOM 2008 C C . TRP A 1 258 ? 88.011 100.164 9.882 1.00 49.10 ? 272 TRP A C 1 ATOM 2009 O O . TRP A 1 258 ? 87.017 100.761 9.461 1.00 50.89 ? 272 TRP A O 1 ATOM 2010 C CB . TRP A 1 258 ? 88.444 99.337 12.244 1.00 49.92 ? 272 TRP A CB 1 ATOM 2011 C CG . TRP A 1 258 ? 87.734 100.399 13.060 1.00 51.53 ? 272 TRP A CG 1 ATOM 2012 C CD1 . TRP A 1 258 ? 88.330 101.424 13.742 1.00 49.43 ? 272 TRP A CD1 1 ATOM 2013 C CD2 . TRP A 1 258 ? 86.317 100.525 13.312 1.00 50.92 ? 272 TRP A CD2 1 ATOM 2014 N NE1 . TRP A 1 258 ? 87.380 102.178 14.396 1.00 50.37 ? 272 TRP A NE1 1 ATOM 2015 C CE2 . TRP A 1 258 ? 86.140 101.652 14.146 1.00 52.63 ? 272 TRP A CE2 1 ATOM 2016 C CE3 . TRP A 1 258 ? 85.187 99.798 12.915 1.00 51.42 ? 272 TRP A CE3 1 ATOM 2017 C CZ2 . TRP A 1 258 ? 84.876 102.069 14.590 1.00 50.81 ? 272 TRP A CZ2 1 ATOM 2018 C CZ3 . TRP A 1 258 ? 83.933 100.220 13.349 1.00 50.79 ? 272 TRP A CZ3 1 ATOM 2019 C CH2 . TRP A 1 258 ? 83.793 101.343 14.184 1.00 49.46 ? 272 TRP A CH2 1 ATOM 2020 N N . SER A 1 259 ? 89.245 100.466 9.498 1.00 50.35 ? 273 SER A N 1 ATOM 2021 C CA . SER A 1 259 ? 89.492 101.508 8.506 1.00 55.82 ? 273 SER A CA 1 ATOM 2022 C C . SER A 1 259 ? 88.624 101.364 7.251 1.00 51.29 ? 273 SER A C 1 ATOM 2023 O O . SER A 1 259 ? 87.898 102.290 6.868 1.00 53.52 ? 273 SER A O 1 ATOM 2024 C CB . SER A 1 259 ? 90.974 101.549 8.127 1.00 52.79 ? 273 SER A CB 1 ATOM 2025 O OG . SER A 1 259 ? 91.180 102.560 7.168 1.00 56.12 ? 273 SER A OG 1 ATOM 2026 N N . ARG A 1 260 ? 88.688 100.197 6.626 1.00 51.11 ? 274 ARG A N 1 ATOM 2027 C CA . ARG A 1 260 ? 87.951 99.963 5.398 1.00 58.56 ? 274 ARG A CA 1 ATOM 2028 C C . ARG A 1 260 ? 86.429 100.122 5.579 1.00 57.14 ? 274 ARG A C 1 ATOM 2029 O O . ARG A 1 260 ? 85.783 100.832 4.798 1.00 56.85 ? 274 ARG A O 1 ATOM 2030 C CB . ARG A 1 260 ? 88.309 98.584 4.827 1.00 59.26 ? 274 ARG A CB 1 ATOM 2031 C CG . ARG A 1 260 ? 87.723 98.293 3.454 1.00 61.20 ? 274 ARG A CG 1 ATOM 2032 C CD . ARG A 1 260 ? 88.229 96.959 2.910 1.00 60.33 ? 274 ARG A CD 1 ATOM 2033 N NE . ARG A 1 260 ? 88.239 95.943 3.955 1.00 58.94 ? 274 ARG A NE 1 ATOM 2034 C CZ . ARG A 1 260 ? 87.161 95.274 4.348 1.00 56.31 ? 274 ARG A CZ 1 ATOM 2035 N NH1 . ARG A 1 260 ? 85.991 95.513 3.773 1.00 56.17 ? 274 ARG A NH1 1 ATOM 2036 N NH2 . ARG A 1 260 ? 87.244 94.365 5.313 1.00 53.71 ? 274 ARG A NH2 1 ATOM 2037 N N . ILE A 1 261 ? 85.855 99.489 6.607 1.00 54.61 ? 275 ILE A N 1 ATOM 2038 C CA . ILE A 1 261 ? 84.400 99.536 6.763 1.00 50.41 ? 275 ILE A CA 1 ATOM 2039 C C . ILE A 1 261 ? 83.884 100.922 7.166 1.00 50.11 ? 275 ILE A C 1 ATOM 2040 O O . ILE A 1 261 ? 82.767 101.283 6.798 1.00 49.89 ? 275 ILE A O 1 ATOM 2041 C CB . ILE A 1 261 ? 83.856 98.447 7.701 1.00 51.04 ? 275 ILE A CB 1 ATOM 2042 C CG1 . ILE A 1 261 ? 84.343 98.649 9.137 1.00 50.66 ? 275 ILE A CG1 1 ATOM 2043 C CG2 . ILE A 1 261 ? 84.230 97.075 7.173 1.00 46.19 ? 275 ILE A CG2 1 ATOM 2044 C CD1 . ILE A 1 261 ? 83.861 97.554 10.097 1.00 50.50 ? 275 ILE A CD1 1 ATOM 2045 N N . LEU A 1 262 ? 84.694 101.701 7.885 1.00 48.26 ? 276 LEU A N 1 ATOM 2046 C CA . LEU A 1 262 ? 84.299 103.067 8.241 1.00 61.10 ? 276 LEU A CA 1 ATOM 2047 C C . LEU A 1 262 ? 83.975 103.915 6.999 1.00 60.09 ? 276 LEU A C 1 ATOM 2048 O O . LEU A 1 262 ? 82.958 104.613 6.963 1.00 62.53 ? 276 LEU A O 1 ATOM 2049 C CB . LEU A 1 262 ? 85.367 103.752 9.102 1.00 49.23 ? 276 LEU A CB 1 ATOM 2050 C CG . LEU A 1 262 ? 85.505 103.317 10.568 1.00 56.59 ? 276 LEU A CG 1 ATOM 2051 C CD1 . LEU A 1 262 ? 86.774 103.893 11.180 1.00 49.46 ? 276 LEU A CD1 1 ATOM 2052 C CD2 . LEU A 1 262 ? 84.284 103.710 11.414 1.00 47.47 ? 276 LEU A CD2 1 ATOM 2053 N N . ASN A 1 263 ? 84.841 103.853 5.990 1.00 54.36 ? 277 ASN A N 1 ATOM 2054 C CA . ASN A 1 263 ? 84.552 104.458 4.688 1.00 56.47 ? 277 ASN A CA 1 ATOM 2055 C C . ASN A 1 263 ? 83.432 103.755 3.927 1.00 55.29 ? 277 ASN A C 1 ATOM 2056 O O . ASN A 1 263 ? 82.422 104.373 3.573 1.00 59.03 ? 277 ASN A O 1 ATOM 2057 C CB . ASN A 1 263 ? 85.810 104.465 3.807 1.00 52.50 ? 277 ASN A CB 1 ATOM 2058 C CG . ASN A 1 263 ? 86.628 105.718 3.965 1.00 59.00 ? 277 ASN A CG 1 ATOM 2059 O OD1 . ASN A 1 263 ? 86.950 106.398 2.981 1.00 65.97 ? 277 ASN A OD1 1 ATOM 2060 N ND2 . ASN A 1 263 ? 86.981 106.035 5.195 1.00 53.47 ? 277 ASN A ND2 1 ATOM 2061 N N . GLN A 1 264 ? 83.612 102.462 3.666 1.00 51.57 ? 278 GLN A N 1 ATOM 2062 C CA . GLN A 1 264 ? 82.752 101.771 2.705 1.00 52.14 ? 278 GLN A CA 1 ATOM 2063 C C . GLN A 1 264 ? 81.336 101.424 3.188 1.00 53.83 ? 278 GLN A C 1 ATOM 2064 O O . GLN A 1 264 ? 80.479 101.097 2.365 1.00 47.90 ? 278 GLN A O 1 ATOM 2065 C CB . GLN A 1 264 ? 83.442 100.517 2.164 1.00 52.89 ? 278 GLN A CB 1 ATOM 2066 C CG . GLN A 1 264 ? 84.818 100.768 1.568 1.00 57.77 ? 278 GLN A CG 1 ATOM 2067 C CD . GLN A 1 264 ? 85.257 99.619 0.702 1.00 56.58 ? 278 GLN A CD 1 ATOM 2068 O OE1 . GLN A 1 264 ? 84.430 98.932 0.117 1.00 58.81 ? 278 GLN A OE1 1 ATOM 2069 N NE2 . GLN A 1 264 ? 86.558 99.392 0.626 1.00 56.93 ? 278 GLN A NE2 1 ATOM 2070 N N . ASN A 1 265 ? 81.087 101.478 4.497 1.00 50.11 ? 279 ASN A N 1 ATOM 2071 C CA . ASN A 1 265 ? 79.721 101.273 4.981 1.00 48.28 ? 279 ASN A CA 1 ATOM 2072 C C . ASN A 1 265 ? 78.809 102.354 4.408 1.00 46.74 ? 279 ASN A C 1 ATOM 2073 O O . ASN A 1 265 ? 77.665 102.085 4.042 1.00 49.31 ? 279 ASN A O 1 ATOM 2074 C CB . ASN A 1 265 ? 79.657 101.260 6.516 1.00 47.35 ? 279 ASN A CB 1 ATOM 2075 C CG . ASN A 1 265 ? 80.011 99.907 7.105 1.00 50.05 ? 279 ASN A CG 1 ATOM 2076 O OD1 . ASN A 1 265 ? 79.998 98.895 6.405 1.00 47.30 ? 279 ASN A OD1 1 ATOM 2077 N ND2 . ASN A 1 265 ? 80.303 99.878 8.412 1.00 51.94 ? 279 ASN A ND2 1 ATOM 2078 N N . TYR A 1 266 ? 79.321 103.577 4.315 1.00 48.03 ? 280 TYR A N 1 ATOM 2079 C CA . TYR A 1 266 ? 78.554 104.625 3.655 1.00 52.69 ? 280 TYR A CA 1 ATOM 2080 C C . TYR A 1 266 ? 78.583 104.490 2.125 1.00 53.02 ? 280 TYR A C 1 ATOM 2081 O O . TYR A 1 266 ? 77.532 104.478 1.480 1.00 53.04 ? 280 TYR A O 1 ATOM 2082 C CB . TYR A 1 266 ? 78.990 106.041 4.062 1.00 52.48 ? 280 TYR A CB 1 ATOM 2083 C CG . TYR A 1 266 ? 78.114 107.056 3.366 1.00 53.37 ? 280 TYR A CG 1 ATOM 2084 C CD1 . TYR A 1 266 ? 76.759 107.141 3.676 1.00 51.86 ? 280 TYR A CD1 1 ATOM 2085 C CD2 . TYR A 1 266 ? 78.616 107.880 2.352 1.00 57.73 ? 280 TYR A CD2 1 ATOM 2086 C CE1 . TYR A 1 266 ? 75.921 108.034 3.032 1.00 54.89 ? 280 TYR A CE1 1 ATOM 2087 C CE2 . TYR A 1 266 ? 77.781 108.784 1.687 1.00 57.02 ? 280 TYR A CE2 1 ATOM 2088 C CZ . TYR A 1 266 ? 76.435 108.855 2.033 1.00 56.14 ? 280 TYR A CZ 1 ATOM 2089 O OH . TYR A 1 266 ? 75.581 109.742 1.412 1.00 55.08 ? 280 TYR A OH 1 ATOM 2090 N N . ILE A 1 267 ? 79.780 104.382 1.556 1.00 55.46 ? 281 ILE A N 1 ATOM 2091 C CA . ILE A 1 267 ? 79.922 104.259 0.100 1.00 58.65 ? 281 ILE A CA 1 ATOM 2092 C C . ILE A 1 267 ? 79.071 103.133 -0.488 1.00 59.88 ? 281 ILE A C 1 ATOM 2093 O O . ILE A 1 267 ? 78.199 103.381 -1.321 1.00 62.83 ? 281 ILE A O 1 ATOM 2094 C CB . ILE A 1 267 ? 81.394 104.053 -0.317 1.00 59.18 ? 281 ILE A CB 1 ATOM 2095 C CG1 . ILE A 1 267 ? 82.252 105.235 0.149 1.00 57.65 ? 281 ILE A CG1 1 ATOM 2096 C CG2 . ILE A 1 267 ? 81.510 103.862 -1.849 1.00 58.44 ? 281 ILE A CG2 1 ATOM 2097 C CD1 . ILE A 1 267 ? 83.739 104.976 0.112 1.00 57.85 ? 281 ILE A CD1 1 ATOM 2098 N N . ASN A 1 268 ? 79.312 101.902 -0.050 1.00 55.94 ? 282 ASN A N 1 ATOM 2099 C CA . ASN A 1 268 ? 78.625 100.754 -0.629 1.00 54.95 ? 282 ASN A CA 1 ATOM 2100 C C . ASN A 1 268 ? 77.219 100.515 -0.098 1.00 53.53 ? 282 ASN A C 1 ATOM 2101 O O . ASN A 1 268 ? 76.400 99.936 -0.797 1.00 50.82 ? 282 ASN A O 1 ATOM 2102 C CB . ASN A 1 268 ? 79.455 99.485 -0.435 1.00 59.83 ? 282 ASN A CB 1 ATOM 2103 C CG . ASN A 1 268 ? 80.848 99.618 -0.985 1.00 63.62 ? 282 ASN A CG 1 ATOM 2104 O OD1 . ASN A 1 268 ? 81.194 100.641 -1.565 1.00 65.46 ? 282 ASN A OD1 1 ATOM 2105 N ND2 . ASN A 1 268 ? 81.666 98.590 -0.793 1.00 65.47 ? 282 ASN A ND2 1 ATOM 2106 N N . GLY A 1 269 ? 76.943 100.933 1.140 1.00 54.60 ? 283 GLY A N 1 ATOM 2107 C CA . GLY A 1 269 ? 75.677 100.579 1.763 1.00 50.68 ? 283 GLY A CA 1 ATOM 2108 C C . GLY A 1 269 ? 74.828 101.710 2.322 1.00 49.69 ? 283 GLY A C 1 ATOM 2109 O O . GLY A 1 269 ? 73.849 101.444 3.021 1.00 50.09 ? 283 GLY A O 1 ATOM 2110 N N . ASN A 1 270 ? 75.200 102.959 2.036 1.00 52.86 ? 284 ASN A N 1 ATOM 2111 C CA . ASN A 1 270 ? 74.439 104.119 2.499 1.00 61.06 ? 284 ASN A CA 1 ATOM 2112 C C . ASN A 1 270 ? 74.310 104.179 4.021 1.00 57.48 ? 284 ASN A C 1 ATOM 2113 O O . ASN A 1 270 ? 73.436 104.878 4.527 1.00 44.30 ? 284 ASN A O 1 ATOM 2114 C CB . ASN A 1 270 ? 73.026 104.148 1.889 1.00 73.49 ? 284 ASN A CB 1 ATOM 2115 C CG . ASN A 1 270 ? 73.027 103.965 0.378 1.00 89.75 ? 284 ASN A CG 1 ATOM 2116 O OD1 . ASN A 1 270 ? 73.009 102.837 -0.125 1.00 89.51 ? 284 ASN A OD1 1 ATOM 2117 N ND2 . ASN A 1 270 ? 73.026 105.077 -0.353 1.00 104.43 ? 284 ASN A ND2 1 ATOM 2118 N N . MET A 1 271 ? 75.162 103.449 4.742 1.00 52.71 ? 285 MET A N 1 ATOM 2119 C CA . MET A 1 271 ? 75.108 103.445 6.209 1.00 49.64 ? 285 MET A CA 1 ATOM 2120 C C . MET A 1 271 ? 75.872 104.616 6.782 1.00 49.19 ? 285 MET A C 1 ATOM 2121 O O . MET A 1 271 ? 77.062 104.792 6.518 1.00 51.97 ? 285 MET A O 1 ATOM 2122 C CB . MET A 1 271 ? 75.633 102.138 6.791 1.00 44.24 ? 285 MET A CB 1 ATOM 2123 C CG . MET A 1 271 ? 74.736 100.984 6.517 1.00 43.70 ? 285 MET A CG 1 ATOM 2124 S SD . MET A 1 271 ? 75.513 99.431 6.947 1.00 48.55 ? 285 MET A SD 1 ATOM 2125 C CE . MET A 1 271 ? 76.172 98.942 5.340 1.00 49.32 ? 285 MET A CE 1 ATOM 2126 N N . THR A 1 272 ? 75.179 105.407 7.593 1.00 49.18 ? 286 THR A N 1 ATOM 2127 C CA . THR A 1 272 ? 75.711 106.679 8.069 1.00 49.31 ? 286 THR A CA 1 ATOM 2128 C C . THR A 1 272 ? 76.203 106.619 9.513 1.00 52.27 ? 286 THR A C 1 ATOM 2129 O O . THR A 1 272 ? 76.636 107.626 10.088 1.00 54.30 ? 286 THR A O 1 ATOM 2130 C CB . THR A 1 272 ? 74.677 107.784 7.872 1.00 49.87 ? 286 THR A CB 1 ATOM 2131 O OG1 . THR A 1 272 ? 73.403 107.339 8.354 1.00 45.97 ? 286 THR A OG1 1 ATOM 2132 C CG2 . THR A 1 272 ? 74.552 108.107 6.362 1.00 48.23 ? 286 THR A CG2 1 ATOM 2133 N N . SER A 1 273 ? 76.148 105.426 10.094 1.00 49.94 ? 287 SER A N 1 ATOM 2134 C CA . SER A 1 273 ? 76.854 105.182 11.344 1.00 48.86 ? 287 SER A CA 1 ATOM 2135 C C . SER A 1 273 ? 77.390 103.752 11.377 1.00 44.85 ? 287 SER A C 1 ATOM 2136 O O . SER A 1 273 ? 76.778 102.836 10.829 1.00 46.26 ? 287 SER A O 1 ATOM 2137 C CB . SER A 1 273 ? 75.941 105.454 12.542 1.00 50.71 ? 287 SER A CB 1 ATOM 2138 O OG . SER A 1 273 ? 76.576 105.109 13.756 1.00 55.23 ? 287 SER A OG 1 ATOM 2139 N N . THR A 1 274 ? 78.554 103.574 11.991 1.00 44.98 ? 288 THR A N 1 ATOM 2140 C CA . THR A 1 274 ? 79.085 102.242 12.249 1.00 43.69 ? 288 THR A CA 1 ATOM 2141 C C . THR A 1 274 ? 79.475 102.161 13.733 1.00 46.32 ? 288 THR A C 1 ATOM 2142 O O . THR A 1 274 ? 80.136 103.064 14.269 1.00 44.87 ? 288 THR A O 1 ATOM 2143 C CB . THR A 1 274 ? 80.290 101.930 11.347 1.00 47.75 ? 288 THR A CB 1 ATOM 2144 O OG1 . THR A 1 274 ? 79.901 102.033 9.967 1.00 45.51 ? 288 THR A OG1 1 ATOM 2145 C CG2 . THR A 1 274 ? 80.800 100.513 11.618 1.00 47.51 ? 288 THR A CG2 1 ATOM 2146 N N . ILE A 1 275 ? 79.046 101.095 14.406 1.00 46.92 ? 289 ILE A N 1 ATOM 2147 C CA . ILE A 1 275 ? 79.335 100.933 15.835 1.00 43.83 ? 289 ILE A CA 1 ATOM 2148 C C . ILE A 1 275 ? 80.104 99.629 16.068 1.00 43.96 ? 289 ILE A C 1 ATOM 2149 O O . ILE A 1 275 ? 79.607 98.535 15.759 1.00 41.58 ? 289 ILE A O 1 ATOM 2150 C CB . ILE A 1 275 ? 78.040 100.959 16.654 1.00 42.70 ? 289 ILE A CB 1 ATOM 2151 C CG1 . ILE A 1 275 ? 77.278 102.258 16.357 1.00 40.24 ? 289 ILE A CG1 1 ATOM 2152 C CG2 . ILE A 1 275 ? 78.328 100.823 18.167 1.00 39.67 ? 289 ILE A CG2 1 ATOM 2153 C CD1 . ILE A 1 275 ? 75.877 102.289 16.910 1.00 43.62 ? 289 ILE A CD1 1 ATOM 2154 N N . ALA A 1 276 ? 81.327 99.753 16.581 1.00 41.64 ? 290 ALA A N 1 ATOM 2155 C CA . ALA A 1 276 ? 82.191 98.591 16.832 1.00 43.64 ? 290 ALA A CA 1 ATOM 2156 C C . ALA A 1 276 ? 81.817 97.780 18.084 1.00 41.81 ? 290 ALA A C 1 ATOM 2157 O O . ALA A 1 276 ? 81.671 98.340 19.176 1.00 40.54 ? 290 ALA A O 1 ATOM 2158 C CB . ALA A 1 276 ? 83.652 99.035 16.942 1.00 43.78 ? 290 ALA A CB 1 ATOM 2159 N N . TRP A 1 277 ? 81.671 96.465 17.939 1.00 42.79 ? 291 TRP A N 1 ATOM 2160 C CA . TRP A 1 277 ? 81.772 95.595 19.107 1.00 43.73 ? 291 TRP A CA 1 ATOM 2161 C C . TRP A 1 277 ? 83.220 95.128 19.150 1.00 46.13 ? 291 TRP A C 1 ATOM 2162 O O . TRP A 1 277 ? 83.657 94.464 18.208 1.00 44.38 ? 291 TRP A O 1 ATOM 2163 C CB . TRP A 1 277 ? 80.884 94.374 18.973 1.00 40.40 ? 291 TRP A CB 1 ATOM 2164 C CG . TRP A 1 277 ? 80.831 93.572 20.253 1.00 40.18 ? 291 TRP A CG 1 ATOM 2165 C CD1 . TRP A 1 277 ? 80.003 93.785 21.313 1.00 38.19 ? 291 TRP A CD1 1 ATOM 2166 C CD2 . TRP A 1 277 ? 81.649 92.442 20.605 1.00 41.97 ? 291 TRP A CD2 1 ATOM 2167 N NE1 . TRP A 1 277 ? 80.243 92.855 22.301 1.00 39.21 ? 291 TRP A NE1 1 ATOM 2168 C CE2 . TRP A 1 277 ? 81.253 92.025 21.891 1.00 38.39 ? 291 TRP A CE2 1 ATOM 2169 C CE3 . TRP A 1 277 ? 82.676 91.746 19.950 1.00 46.16 ? 291 TRP A CE3 1 ATOM 2170 C CZ2 . TRP A 1 277 ? 81.853 90.933 22.545 1.00 38.37 ? 291 TRP A CZ2 1 ATOM 2171 C CZ3 . TRP A 1 277 ? 83.277 90.674 20.602 1.00 46.90 ? 291 TRP A CZ3 1 ATOM 2172 C CH2 . TRP A 1 277 ? 82.859 90.276 21.887 1.00 44.62 ? 291 TRP A CH2 1 ATOM 2173 N N . ASN A 1 278 ? 83.965 95.433 20.216 1.00 45.65 ? 292 ASN A N 1 ATOM 2174 C CA . ASN A 1 278 ? 83.480 96.152 21.397 1.00 43.87 ? 292 ASN A CA 1 ATOM 2175 C C . ASN A 1 278 ? 84.386 97.333 21.731 1.00 44.92 ? 292 ASN A C 1 ATOM 2176 O O . ASN A 1 278 ? 85.435 97.521 21.101 1.00 46.62 ? 292 ASN A O 1 ATOM 2177 C CB . ASN A 1 278 ? 83.410 95.215 22.604 1.00 42.90 ? 292 ASN A CB 1 ATOM 2178 C CG . ASN A 1 278 ? 84.759 94.557 22.934 1.00 43.71 ? 292 ASN A CG 1 ATOM 2179 O OD1 . ASN A 1 278 ? 85.689 95.215 23.428 1.00 43.62 ? 292 ASN A OD1 1 ATOM 2180 N ND2 . ASN A 1 278 ? 84.856 93.249 22.693 1.00 40.30 ? 292 ASN A ND2 1 ATOM 2181 N N . LEU A 1 279 ? 83.998 98.104 22.744 1.00 45.90 ? 293 LEU A N 1 ATOM 2182 C CA . LEU A 1 279 ? 84.667 99.362 23.102 1.00 47.04 ? 293 LEU A CA 1 ATOM 2183 C C . LEU A 1 279 ? 86.111 99.203 23.577 1.00 48.97 ? 293 LEU A C 1 ATOM 2184 O O . LEU A 1 279 ? 87.018 99.885 23.087 1.00 47.03 ? 293 LEU A O 1 ATOM 2185 C CB . LEU A 1 279 ? 83.861 100.082 24.178 1.00 45.35 ? 293 LEU A CB 1 ATOM 2186 C CG . LEU A 1 279 ? 84.478 101.306 24.850 1.00 46.35 ? 293 LEU A CG 1 ATOM 2187 C CD1 . LEU A 1 279 ? 84.387 102.514 23.943 1.00 43.55 ? 293 LEU A CD1 1 ATOM 2188 C CD2 . LEU A 1 279 ? 83.780 101.575 26.194 1.00 42.54 ? 293 LEU A CD2 1 ATOM 2189 N N . VAL A 1 280 ? 86.317 98.304 24.533 1.00 47.63 ? 294 VAL A N 1 ATOM 2190 C CA . VAL A 1 280 ? 87.651 98.045 25.062 1.00 45.86 ? 294 VAL A CA 1 ATOM 2191 C C . VAL A 1 280 ? 87.692 96.597 25.505 1.00 48.96 ? 294 VAL A C 1 ATOM 2192 O O . VAL A 1 280 ? 86.748 96.104 26.122 1.00 55.15 ? 294 VAL A O 1 ATOM 2193 C CB . VAL A 1 280 ? 87.984 99.006 26.245 1.00 48.22 ? 294 VAL A CB 1 ATOM 2194 C CG1 . VAL A 1 280 ? 86.890 98.971 27.300 1.00 43.82 ? 294 VAL A CG1 1 ATOM 2195 C CG2 . VAL A 1 280 ? 89.372 98.700 26.856 1.00 47.97 ? 294 VAL A CG2 1 ATOM 2196 N N . ALA A 1 281 ? 88.752 95.884 25.159 1.00 45.19 ? 295 ALA A N 1 ATOM 2197 C CA . ALA A 1 281 ? 88.855 94.505 25.625 1.00 43.85 ? 295 ALA A CA 1 ATOM 2198 C C . ALA A 1 281 ? 89.276 94.499 27.097 1.00 53.44 ? 295 ALA A C 1 ATOM 2199 O O . ALA A 1 281 ? 90.470 94.445 27.427 1.00 45.21 ? 295 ALA A O 1 ATOM 2200 C CB . ALA A 1 281 ? 89.828 93.705 24.766 1.00 44.45 ? 295 ALA A CB 1 ATOM 2201 N N . SER A 1 282 ? 88.287 94.592 27.979 1.00 54.17 ? 296 SER A N 1 ATOM 2202 C CA . SER A 1 282 ? 88.539 94.482 29.410 1.00 52.75 ? 296 SER A CA 1 ATOM 2203 C C . SER A 1 282 ? 87.888 93.223 29.945 1.00 46.93 ? 296 SER A C 1 ATOM 2204 O O . SER A 1 282 ? 87.119 93.265 30.904 1.00 47.49 ? 296 SER A O 1 ATOM 2205 C CB . SER A 1 282 ? 88.041 95.720 30.167 1.00 52.14 ? 296 SER A CB 1 ATOM 2206 O OG . SER A 1 282 ? 88.863 96.840 29.883 1.00 51.71 ? 296 SER A OG 1 ATOM 2207 N N . TYR A 1 283 ? 88.215 92.098 29.325 1.00 42.74 ? 297 TYR A N 1 ATOM 2208 C CA . TYR A 1 283 ? 87.715 90.804 29.775 1.00 44.58 ? 297 TYR A CA 1 ATOM 2209 C C . TYR A 1 283 ? 88.819 89.810 29.497 1.00 42.75 ? 297 TYR A C 1 ATOM 2210 O O . TYR A 1 283 ? 89.569 90.003 28.552 1.00 48.51 ? 297 TYR A O 1 ATOM 2211 C CB . TYR A 1 283 ? 86.419 90.415 29.024 1.00 40.82 ? 297 TYR A CB 1 ATOM 2212 C CG . TYR A 1 283 ? 86.526 90.482 27.505 1.00 43.04 ? 297 TYR A CG 1 ATOM 2213 C CD1 . TYR A 1 283 ? 86.462 91.701 26.826 1.00 41.10 ? 297 TYR A CD1 1 ATOM 2214 C CD2 . TYR A 1 283 ? 86.670 89.327 26.748 1.00 44.27 ? 297 TYR A CD2 1 ATOM 2215 C CE1 . TYR A 1 283 ? 86.546 91.768 25.437 1.00 41.18 ? 297 TYR A CE1 1 ATOM 2216 C CE2 . TYR A 1 283 ? 86.753 89.388 25.345 1.00 46.60 ? 297 TYR A CE2 1 ATOM 2217 C CZ . TYR A 1 283 ? 86.694 90.609 24.702 1.00 46.19 ? 297 TYR A CZ 1 ATOM 2218 O OH . TYR A 1 283 ? 86.772 90.651 23.312 1.00 48.24 ? 297 TYR A OH 1 ATOM 2219 N N . TYR A 1 284 ? 88.919 88.760 30.306 1.00 42.69 ? 298 TYR A N 1 ATOM 2220 C CA . TYR A 1 284 ? 89.962 87.733 30.156 1.00 43.43 ? 298 TYR A CA 1 ATOM 2221 C C . TYR A 1 284 ? 90.109 87.278 28.696 1.00 43.42 ? 298 TYR A C 1 ATOM 2222 O O . TYR A 1 284 ? 89.127 86.881 28.080 1.00 43.98 ? 298 TYR A O 1 ATOM 2223 C CB . TYR A 1 284 ? 89.628 86.527 31.050 1.00 43.04 ? 298 TYR A CB 1 ATOM 2224 C CG . TYR A 1 284 ? 89.663 86.816 32.546 1.00 43.24 ? 298 TYR A CG 1 ATOM 2225 C CD1 . TYR A 1 284 ? 90.755 87.470 33.128 1.00 46.00 ? 298 TYR A CD1 1 ATOM 2226 C CD2 . TYR A 1 284 ? 88.610 86.427 33.379 1.00 45.02 ? 298 TYR A CD2 1 ATOM 2227 C CE1 . TYR A 1 284 ? 90.792 87.738 34.495 1.00 44.60 ? 298 TYR A CE1 1 ATOM 2228 C CE2 . TYR A 1 284 ? 88.632 86.698 34.761 1.00 42.58 ? 298 TYR A CE2 1 ATOM 2229 C CZ . TYR A 1 284 ? 89.732 87.352 35.307 1.00 43.72 ? 298 TYR A CZ 1 ATOM 2230 O OH . TYR A 1 284 ? 89.777 87.620 36.672 1.00 44.73 ? 298 TYR A OH 1 ATOM 2231 N N . GLU A 1 285 ? 91.316 87.317 28.139 1.00 47.03 ? 299 GLU A N 1 ATOM 2232 C CA . GLU A 1 285 ? 91.448 87.114 26.680 1.00 51.53 ? 299 GLU A CA 1 ATOM 2233 C C . GLU A 1 285 ? 91.127 85.693 26.213 1.00 49.85 ? 299 GLU A C 1 ATOM 2234 O O . GLU A 1 285 ? 90.866 85.467 25.034 1.00 45.31 ? 299 GLU A O 1 ATOM 2235 C CB . GLU A 1 285 ? 92.810 87.587 26.145 1.00 55.95 ? 299 GLU A CB 1 ATOM 2236 C CG . GLU A 1 285 ? 93.984 86.685 26.504 1.00 62.29 ? 299 GLU A CG 1 ATOM 2237 C CD . GLU A 1 285 ? 95.318 87.137 25.884 1.00 66.67 ? 299 GLU A CD 1 ATOM 2238 O OE1 . GLU A 1 285 ? 95.324 87.906 24.884 1.00 64.89 ? 299 GLU A OE1 1 ATOM 2239 O OE2 . GLU A 1 285 ? 96.368 86.700 26.409 1.00 69.05 ? 299 GLU A OE2 1 ATOM 2240 N N . GLU A 1 286 ? 91.115 84.746 27.146 1.00 51.92 ? 300 GLU A N 1 ATOM 2241 C CA . GLU A 1 286 ? 90.783 83.359 26.829 1.00 50.31 ? 300 GLU A CA 1 ATOM 2242 C C . GLU A 1 286 ? 89.266 83.134 26.807 1.00 47.68 ? 300 GLU A C 1 ATOM 2243 O O . GLU A 1 286 ? 88.793 82.023 26.489 1.00 47.07 ? 300 GLU A O 1 ATOM 2244 C CB . GLU A 1 286 ? 91.468 82.408 27.823 1.00 53.27 ? 300 GLU A CB 1 ATOM 2245 C CG . GLU A 1 286 ? 93.008 82.454 27.790 1.00 60.19 ? 300 GLU A CG 1 ATOM 2246 C CD . GLU A 1 286 ? 93.630 83.503 28.736 1.00 65.03 ? 300 GLU A CD 1 ATOM 2247 O OE1 . GLU A 1 286 ? 92.892 84.345 29.301 1.00 62.46 ? 300 GLU A OE1 1 ATOM 2248 O OE2 . GLU A 1 286 ? 94.874 83.479 28.919 1.00 67.58 ? 300 GLU A OE2 1 ATOM 2249 N N . LEU A 1 287 ? 88.510 84.186 27.145 1.00 44.62 ? 301 LEU A N 1 ATOM 2250 C CA . LEU A 1 287 ? 87.051 84.213 26.913 1.00 48.84 ? 301 LEU A CA 1 ATOM 2251 C C . LEU A 1 287 ? 86.787 84.419 25.408 1.00 40.15 ? 301 LEU A C 1 ATOM 2252 O O . LEU A 1 287 ? 87.675 84.893 24.699 1.00 40.97 ? 301 LEU A O 1 ATOM 2253 C CB . LEU A 1 287 ? 86.401 85.327 27.745 1.00 46.32 ? 301 LEU A CB 1 ATOM 2254 C CG . LEU A 1 287 ? 86.266 85.068 29.250 1.00 45.38 ? 301 LEU A CG 1 ATOM 2255 C CD1 . LEU A 1 287 ? 85.752 86.305 29.982 1.00 39.59 ? 301 LEU A CD1 1 ATOM 2256 C CD2 . LEU A 1 287 ? 85.348 83.876 29.512 1.00 38.96 ? 301 LEU A CD2 1 ATOM 2257 N N . PRO A 1 288 ? 85.581 84.053 24.916 1.00 39.10 ? 302 PRO A N 1 ATOM 2258 C CA . PRO A 1 288 ? 85.292 84.147 23.471 1.00 38.91 ? 302 PRO A CA 1 ATOM 2259 C C . PRO A 1 288 ? 85.611 85.509 22.860 1.00 43.43 ? 302 PRO A C 1 ATOM 2260 O O . PRO A 1 288 ? 85.305 86.547 23.449 1.00 41.80 ? 302 PRO A O 1 ATOM 2261 C CB . PRO A 1 288 ? 83.782 83.906 23.392 1.00 37.63 ? 302 PRO A CB 1 ATOM 2262 C CG . PRO A 1 288 ? 83.476 83.006 24.600 1.00 42.98 ? 302 PRO A CG 1 ATOM 2263 C CD . PRO A 1 288 ? 84.469 83.442 25.675 1.00 38.10 ? 302 PRO A CD 1 ATOM 2264 N N . TYR A 1 289 ? 86.231 85.495 21.685 1.00 42.39 ? 303 TYR A N 1 ATOM 2265 C CA . TYR A 1 289 ? 86.569 86.718 20.958 1.00 42.52 ? 303 TYR A CA 1 ATOM 2266 C C . TYR A 1 289 ? 87.523 87.629 21.742 1.00 45.54 ? 303 TYR A C 1 ATOM 2267 O O . TYR A 1 289 ? 87.400 88.858 21.702 1.00 48.11 ? 303 TYR A O 1 ATOM 2268 C CB . TYR A 1 289 ? 85.300 87.484 20.540 1.00 41.68 ? 303 TYR A CB 1 ATOM 2269 C CG . TYR A 1 289 ? 84.340 86.698 19.668 1.00 45.52 ? 303 TYR A CG 1 ATOM 2270 C CD1 . TYR A 1 289 ? 84.507 86.656 18.287 1.00 46.61 ? 303 TYR A CD1 1 ATOM 2271 C CD2 . TYR A 1 289 ? 83.259 86.012 20.221 1.00 44.90 ? 303 TYR A CD2 1 ATOM 2272 C CE1 . TYR A 1 289 ? 83.632 85.955 17.482 1.00 47.70 ? 303 TYR A CE1 1 ATOM 2273 C CE2 . TYR A 1 289 ? 82.373 85.303 19.419 1.00 45.62 ? 303 TYR A CE2 1 ATOM 2274 C CZ . TYR A 1 289 ? 82.573 85.278 18.047 1.00 47.51 ? 303 TYR A CZ 1 ATOM 2275 O OH . TYR A 1 289 ? 81.714 84.580 17.223 1.00 46.63 ? 303 TYR A OH 1 ATOM 2276 N N . GLY A 1 290 ? 88.493 87.031 22.427 1.00 47.84 ? 304 GLY A N 1 ATOM 2277 C CA . GLY A 1 290 ? 89.488 87.800 23.168 1.00 49.92 ? 304 GLY A CA 1 ATOM 2278 C C . GLY A 1 290 ? 90.156 88.901 22.354 1.00 48.97 ? 304 GLY A C 1 ATOM 2279 O O . GLY A 1 290 ? 90.410 88.741 21.149 1.00 46.06 ? 304 GLY A O 1 ATOM 2280 N N . ARG A 1 291 ? 90.419 90.027 23.014 1.00 46.59 ? 305 ARG A N 1 ATOM 2281 C CA . ARG A 1 291 ? 91.112 91.167 22.408 1.00 47.60 ? 305 ARG A CA 1 ATOM 2282 C C . ARG A 1 291 ? 90.449 91.751 21.155 1.00 50.84 ? 305 ARG A C 1 ATOM 2283 O O . ARG A 1 291 ? 91.153 92.233 20.254 1.00 51.22 ? 305 ARG A O 1 ATOM 2284 C CB . ARG A 1 291 ? 92.573 90.809 22.087 1.00 52.99 ? 305 ARG A CB 1 ATOM 2285 C CG . ARG A 1 291 ? 93.559 90.945 23.258 1.00 58.17 ? 305 ARG A CG 1 ATOM 2286 C CD . ARG A 1 291 ? 94.977 90.716 22.780 1.00 61.76 ? 305 ARG A CD 1 ATOM 2287 N NE . ARG A 1 291 ? 95.236 91.487 21.565 1.00 64.74 ? 305 ARG A NE 1 ATOM 2288 C CZ . ARG A 1 291 ? 96.073 91.113 20.603 1.00 67.44 ? 305 ARG A CZ 1 ATOM 2289 N NH1 . ARG A 1 291 ? 96.728 89.966 20.709 1.00 69.35 ? 305 ARG A NH1 1 ATOM 2290 N NH2 . ARG A 1 291 ? 96.249 91.882 19.531 1.00 67.21 ? 305 ARG A NH2 1 ATOM 2291 N N . SER A 1 292 ? 89.119 91.725 21.086 1.00 49.30 ? 306 SER A N 1 ATOM 2292 C CA . SER A 1 292 ? 88.422 92.361 19.969 1.00 45.04 ? 306 SER A CA 1 ATOM 2293 C C . SER A 1 292 ? 87.738 93.669 20.394 1.00 44.17 ? 306 SER A C 1 ATOM 2294 O O . SER A 1 292 ? 86.575 93.940 20.040 1.00 42.89 ? 306 SER A O 1 ATOM 2295 C CB . SER A 1 292 ? 87.412 91.406 19.346 1.00 47.66 ? 306 SER A CB 1 ATOM 2296 O OG . SER A 1 292 ? 87.950 90.099 19.253 1.00 51.62 ? 306 SER A OG 1 ATOM 2297 N N . GLY A 1 293 ? 88.464 94.470 21.164 1.00 45.49 ? 307 GLY A N 1 ATOM 2298 C CA . GLY A 1 293 ? 88.038 95.820 21.493 1.00 45.54 ? 307 GLY A CA 1 ATOM 2299 C C . GLY A 1 293 ? 88.867 96.834 20.727 1.00 48.32 ? 307 GLY A C 1 ATOM 2300 O O . GLY A 1 293 ? 89.887 96.485 20.142 1.00 46.29 ? 307 GLY A O 1 ATOM 2301 N N . LEU A 1 294 ? 88.436 98.090 20.719 1.00 48.96 ? 308 LEU A N 1 ATOM 2302 C CA . LEU A 1 294 ? 89.176 99.115 20.013 1.00 50.60 ? 308 LEU A CA 1 ATOM 2303 C C . LEU A 1 294 ? 90.576 99.250 20.617 1.00 58.06 ? 308 LEU A C 1 ATOM 2304 O O . LEU A 1 294 ? 91.559 99.467 19.901 1.00 60.97 ? 308 LEU A O 1 ATOM 2305 C CB . LEU A 1 294 ? 88.420 100.443 20.054 1.00 51.74 ? 308 LEU A CB 1 ATOM 2306 C CG . LEU A 1 294 ? 87.125 100.528 19.240 1.00 50.35 ? 308 LEU A CG 1 ATOM 2307 C CD1 . LEU A 1 294 ? 86.602 101.960 19.161 1.00 50.55 ? 308 LEU A CD1 1 ATOM 2308 C CD2 . LEU A 1 294 ? 87.329 99.955 17.846 1.00 51.52 ? 308 LEU A CD2 1 ATOM 2309 N N . MET A 1 295 ? 90.660 99.115 21.936 1.00 56.81 ? 309 MET A N 1 ATOM 2310 C CA . MET A 1 295 ? 91.953 99.014 22.600 1.00 54.80 ? 309 MET A CA 1 ATOM 2311 C C . MET A 1 295 ? 91.873 97.895 23.624 1.00 53.30 ? 309 MET A C 1 ATOM 2312 O O . MET A 1 295 ? 90.867 97.173 23.674 1.00 50.81 ? 309 MET A O 1 ATOM 2313 C CB . MET A 1 295 ? 92.327 100.331 23.268 1.00 53.37 ? 309 MET A CB 1 ATOM 2314 C CG . MET A 1 295 ? 91.314 100.858 24.267 1.00 48.22 ? 309 MET A CG 1 ATOM 2315 S SD . MET A 1 295 ? 91.942 102.403 24.954 1.00 53.56 ? 309 MET A SD 1 ATOM 2316 C CE . MET A 1 295 ? 93.289 101.775 25.967 1.00 63.05 ? 309 MET A CE 1 ATOM 2317 N N . THR A 1 296 ? 92.912 97.758 24.446 1.00 49.48 ? 310 THR A N 1 ATOM 2318 C CA . THR A 1 296 ? 92.987 96.639 25.383 1.00 50.16 ? 310 THR A CA 1 ATOM 2319 C C . THR A 1 296 ? 93.237 97.154 26.789 1.00 54.01 ? 310 THR A C 1 ATOM 2320 O O . THR A 1 296 ? 94.120 97.978 26.998 1.00 55.21 ? 310 THR A O 1 ATOM 2321 C CB . THR A 1 296 ? 94.140 95.672 25.013 1.00 53.90 ? 310 THR A CB 1 ATOM 2322 O OG1 . THR A 1 296 ? 93.833 94.994 23.790 1.00 52.19 ? 310 THR A OG1 1 ATOM 2323 C CG2 . THR A 1 296 ? 94.372 94.639 26.108 1.00 53.07 ? 310 THR A CG2 1 ATOM 2324 N N . ALA A 1 297 ? 92.454 96.680 27.752 1.00 52.86 ? 311 ALA A N 1 ATOM 2325 C CA . ALA A 1 297 ? 92.707 96.997 29.151 1.00 53.18 ? 311 ALA A CA 1 ATOM 2326 C C . ALA A 1 297 ? 92.291 95.817 30.011 1.00 50.25 ? 311 ALA A C 1 ATOM 2327 O O . ALA A 1 297 ? 91.329 95.901 30.768 1.00 46.56 ? 311 ALA A O 1 ATOM 2328 C CB . ALA A 1 297 ? 91.959 98.260 29.557 1.00 47.82 ? 311 ALA A CB 1 ATOM 2329 N N . GLN A 1 298 ? 93.028 94.715 29.900 1.00 49.88 ? 312 GLN A N 1 ATOM 2330 C CA . GLN A 1 298 ? 92.644 93.485 30.589 1.00 47.00 ? 312 GLN A CA 1 ATOM 2331 C C . GLN A 1 298 ? 93.517 93.110 31.793 1.00 58.45 ? 312 GLN A C 1 ATOM 2332 O O . GLN A 1 298 ? 93.610 91.927 32.143 1.00 47.63 ? 312 GLN A O 1 ATOM 2333 C CB . GLN A 1 298 ? 92.650 92.330 29.597 1.00 46.66 ? 312 GLN A CB 1 ATOM 2334 C CG . GLN A 1 298 ? 93.935 92.219 28.824 1.00 54.91 ? 312 GLN A CG 1 ATOM 2335 C CD . GLN A 1 298 ? 93.868 91.175 27.732 1.00 58.52 ? 312 GLN A CD 1 ATOM 2336 O OE1 . GLN A 1 298 ? 92.804 90.933 27.148 1.00 60.32 ? 312 GLN A OE1 1 ATOM 2337 N NE2 . GLN A 1 298 ? 95.008 90.550 27.438 1.00 56.30 ? 312 GLN A NE2 1 ATOM 2338 N N . GLU A 1 299 ? 94.151 94.101 32.424 1.00 59.10 ? 313 GLU A N 1 ATOM 2339 C CA . GLU A 1 299 ? 94.990 93.846 33.602 1.00 60.66 ? 313 GLU A CA 1 ATOM 2340 C C . GLU A 1 299 ? 94.889 94.941 34.658 1.00 56.57 ? 313 GLU A C 1 ATOM 2341 O O . GLU A 1 299 ? 95.816 95.736 34.810 1.00 54.13 ? 313 GLU A O 1 ATOM 2342 C CB . GLU A 1 299 ? 96.462 93.718 33.194 1.00 64.71 ? 313 GLU A CB 1 ATOM 2343 C CG . GLU A 1 299 ? 96.845 92.453 32.442 1.00 66.49 ? 313 GLU A CG 1 ATOM 2344 C CD . GLU A 1 299 ? 98.331 92.424 32.112 1.00 69.58 ? 313 GLU A CD 1 ATOM 2345 O OE1 . GLU A 1 299 ? 99.111 93.068 32.848 1.00 67.63 ? 313 GLU A OE1 1 ATOM 2346 O OE2 . GLU A 1 299 ? 98.717 91.768 31.118 1.00 71.85 ? 313 GLU A OE2 1 ATOM 2347 N N . PRO A 1 300 ? 93.778 94.979 35.404 1.00 55.37 ? 314 PRO A N 1 ATOM 2348 C CA . PRO A 1 300 ? 93.618 96.025 36.422 1.00 56.99 ? 314 PRO A CA 1 ATOM 2349 C C . PRO A 1 300 ? 94.605 95.896 37.585 1.00 57.66 ? 314 PRO A C 1 ATOM 2350 O O . PRO A 1 300 ? 94.885 96.892 38.239 1.00 57.75 ? 314 PRO A O 1 ATOM 2351 C CB . PRO A 1 300 ? 92.177 95.805 36.932 1.00 53.77 ? 314 PRO A CB 1 ATOM 2352 C CG . PRO A 1 300 ? 91.894 94.359 36.662 1.00 54.58 ? 314 PRO A CG 1 ATOM 2353 C CD . PRO A 1 300 ? 92.607 94.077 35.347 1.00 56.82 ? 314 PRO A CD 1 ATOM 2354 N N . TRP A 1 301 ? 95.090 94.681 37.833 1.00 56.47 ? 315 TRP A N 1 ATOM 2355 C CA . TRP A 1 301 ? 96.022 94.391 38.915 1.00 55.22 ? 315 TRP A CA 1 ATOM 2356 C C . TRP A 1 301 ? 97.441 94.896 38.622 1.00 58.26 ? 315 TRP A C 1 ATOM 2357 O O . TRP A 1 301 ? 98.274 94.933 39.517 1.00 55.72 ? 315 TRP A O 1 ATOM 2358 C CB . TRP A 1 301 ? 96.075 92.880 39.148 1.00 53.46 ? 315 TRP A CB 1 ATOM 2359 C CG . TRP A 1 301 ? 96.342 92.134 37.872 1.00 56.44 ? 315 TRP A CG 1 ATOM 2360 C CD1 . TRP A 1 301 ? 97.553 91.940 37.267 1.00 52.02 ? 315 TRP A CD1 1 ATOM 2361 C CD2 . TRP A 1 301 ? 95.368 91.494 37.033 1.00 57.15 ? 315 TRP A CD2 1 ATOM 2362 N NE1 . TRP A 1 301 ? 97.390 91.222 36.099 1.00 51.52 ? 315 TRP A NE1 1 ATOM 2363 C CE2 . TRP A 1 301 ? 96.060 90.934 35.936 1.00 58.06 ? 315 TRP A CE2 1 ATOM 2364 C CE3 . TRP A 1 301 ? 93.981 91.335 37.107 1.00 55.96 ? 315 TRP A CE3 1 ATOM 2365 C CZ2 . TRP A 1 301 ? 95.407 90.227 34.919 1.00 56.87 ? 315 TRP A CZ2 1 ATOM 2366 C CZ3 . TRP A 1 301 ? 93.333 90.641 36.089 1.00 56.20 ? 315 TRP A CZ3 1 ATOM 2367 C CH2 . TRP A 1 301 ? 94.047 90.093 35.017 1.00 56.16 ? 315 TRP A CH2 1 ATOM 2368 N N . SER A 1 302 ? 97.725 95.249 37.371 1.00 58.55 ? 316 SER A N 1 ATOM 2369 C CA . SER A 1 302 ? 99.049 95.766 37.015 1.00 59.73 ? 316 SER A CA 1 ATOM 2370 C C . SER A 1 302 ? 98.953 97.189 36.469 1.00 62.68 ? 316 SER A C 1 ATOM 2371 O O . SER A 1 302 ? 99.914 97.968 36.550 1.00 66.01 ? 316 SER A O 1 ATOM 2372 C CB . SER A 1 302 ? 99.713 94.877 35.965 1.00 57.77 ? 316 SER A CB 1 ATOM 2373 O OG . SER A 1 302 ? 99.095 95.039 34.693 1.00 55.67 ? 316 SER A OG 1 ATOM 2374 N N . GLY A 1 303 ? 97.796 97.520 35.897 1.00 57.75 ? 317 GLY A N 1 ATOM 2375 C CA . GLY A 1 303 ? 97.584 98.833 35.309 1.00 56.42 ? 317 GLY A CA 1 ATOM 2376 C C . GLY A 1 303 ? 97.971 98.893 33.843 1.00 56.51 ? 317 GLY A C 1 ATOM 2377 O O . GLY A 1 303 ? 97.785 99.923 33.177 1.00 53.91 ? 317 GLY A O 1 ATOM 2378 N N . HIS A 1 304 ? 98.510 97.786 33.335 1.00 55.60 ? 318 HIS A N 1 ATOM 2379 C CA . HIS A 1 304 ? 98.945 97.723 31.948 1.00 55.97 ? 318 HIS A CA 1 ATOM 2380 C C . HIS A 1 304 ? 97.729 97.791 31.029 1.00 56.03 ? 318 HIS A C 1 ATOM 2381 O O . HIS A 1 304 ? 96.750 97.060 31.233 1.00 55.80 ? 318 HIS A O 1 ATOM 2382 C CB . HIS A 1 304 ? 99.727 96.427 31.699 1.00 57.61 ? 318 HIS A CB 1 ATOM 2383 C CG . HIS A 1 304 ? 100.199 96.266 30.289 1.00 62.75 ? 318 HIS A CG 1 ATOM 2384 N ND1 . HIS A 1 304 ? 99.947 95.131 29.546 1.00 65.94 ? 318 HIS A ND1 1 ATOM 2385 C CD2 . HIS A 1 304 ? 100.894 97.098 29.477 1.00 64.29 ? 318 HIS A CD2 1 ATOM 2386 C CE1 . HIS A 1 304 ? 100.465 95.270 28.338 1.00 63.33 ? 318 HIS A CE1 1 ATOM 2387 N NE2 . HIS A 1 304 ? 101.044 96.456 28.270 1.00 65.50 ? 318 HIS A NE2 1 ATOM 2388 N N . TYR A 1 305 ? 97.777 98.683 30.045 1.00 57.26 ? 319 TYR A N 1 ATOM 2389 C CA . TYR A 1 305 ? 96.783 98.703 28.969 1.00 57.33 ? 319 TYR A CA 1 ATOM 2390 C C . TYR A 1 305 ? 97.502 98.964 27.648 1.00 62.06 ? 319 TYR A C 1 ATOM 2391 O O . TYR A 1 305 ? 98.629 99.470 27.641 1.00 65.54 ? 319 TYR A O 1 ATOM 2392 C CB . TYR A 1 305 ? 95.706 99.771 29.226 1.00 55.99 ? 319 TYR A CB 1 ATOM 2393 C CG . TYR A 1 305 ? 96.217 101.204 29.317 1.00 60.00 ? 319 TYR A CG 1 ATOM 2394 C CD1 . TYR A 1 305 ? 96.384 101.982 28.169 1.00 59.77 ? 319 TYR A CD1 1 ATOM 2395 C CD2 . TYR A 1 305 ? 96.504 101.786 30.550 1.00 58.92 ? 319 TYR A CD2 1 ATOM 2396 C CE1 . TYR A 1 305 ? 96.834 103.288 28.247 1.00 60.40 ? 319 TYR A CE1 1 ATOM 2397 C CE2 . TYR A 1 305 ? 96.948 103.092 30.638 1.00 60.61 ? 319 TYR A CE2 1 ATOM 2398 C CZ . TYR A 1 305 ? 97.117 103.837 29.486 1.00 62.59 ? 319 TYR A CZ 1 ATOM 2399 O OH . TYR A 1 305 ? 97.571 105.140 29.564 1.00 55.61 ? 319 TYR A OH 1 ATOM 2400 N N . VAL A 1 306 ? 96.864 98.617 26.532 1.00 60.32 ? 320 VAL A N 1 ATOM 2401 C CA . VAL A 1 306 ? 97.461 98.847 25.212 1.00 59.86 ? 320 VAL A CA 1 ATOM 2402 C C . VAL A 1 306 ? 96.568 99.759 24.365 1.00 56.27 ? 320 VAL A C 1 ATOM 2403 O O . VAL A 1 306 ? 95.398 99.444 24.134 1.00 53.85 ? 320 VAL A O 1 ATOM 2404 C CB . VAL A 1 306 ? 97.718 97.509 24.472 1.00 57.67 ? 320 VAL A CB 1 ATOM 2405 C CG1 . VAL A 1 306 ? 98.334 97.743 23.086 1.00 56.58 ? 320 VAL A CG1 1 ATOM 2406 C CG2 . VAL A 1 306 ? 98.601 96.597 25.314 1.00 56.36 ? 320 VAL A CG2 1 ATOM 2407 N N . VAL A 1 307 ? 97.109 100.894 23.927 1.00 56.31 ? 321 VAL A N 1 ATOM 2408 C CA . VAL A 1 307 ? 96.399 101.789 23.019 1.00 55.61 ? 321 VAL A CA 1 ATOM 2409 C C . VAL A 1 307 ? 96.543 101.232 21.605 1.00 57.88 ? 321 VAL A C 1 ATOM 2410 O O . VAL A 1 307 ? 97.436 101.628 20.862 1.00 54.03 ? 321 VAL A O 1 ATOM 2411 C CB . VAL A 1 307 ? 96.979 103.221 23.056 1.00 58.64 ? 321 VAL A CB 1 ATOM 2412 C CG1 . VAL A 1 307 ? 96.043 104.198 22.351 1.00 59.41 ? 321 VAL A CG1 1 ATOM 2413 C CG2 . VAL A 1 307 ? 97.210 103.665 24.487 1.00 58.11 ? 321 VAL A CG2 1 ATOM 2414 N N . ALA A 1 308 ? 95.657 100.312 21.238 1.00 59.67 ? 322 ALA A N 1 ATOM 2415 C CA . ALA A 1 308 ? 95.785 99.554 19.992 1.00 56.72 ? 322 ALA A CA 1 ATOM 2416 C C . ALA A 1 308 ? 95.535 100.392 18.733 1.00 60.37 ? 322 ALA A C 1 ATOM 2417 O O . ALA A 1 308 ? 94.904 101.453 18.804 1.00 58.66 ? 322 ALA A O 1 ATOM 2418 C CB . ALA A 1 308 ? 94.851 98.349 20.028 1.00 55.04 ? 322 ALA A CB 1 ATOM 2419 N N . SER A 1 309 ? 96.016 99.892 17.589 1.00 61.43 ? 323 SER A N 1 ATOM 2420 C CA . SER A 1 309 ? 95.853 100.547 16.285 1.00 64.36 ? 323 SER A CA 1 ATOM 2421 C C . SER A 1 309 ? 94.453 101.112 15.988 1.00 60.75 ? 323 SER A C 1 ATOM 2422 O O . SER A 1 309 ? 94.354 102.246 15.494 1.00 59.35 ? 323 SER A O 1 ATOM 2423 C CB . SER A 1 309 ? 96.282 99.619 15.130 1.00 67.68 ? 323 SER A CB 1 ATOM 2424 O OG . SER A 1 309 ? 97.533 98.991 15.354 1.00 72.24 ? 323 SER A OG 1 ATOM 2425 N N . PRO A 1 310 ? 93.373 100.331 16.267 1.00 57.14 ? 324 PRO A N 1 ATOM 2426 C CA . PRO A 1 310 ? 92.031 100.848 15.947 1.00 52.94 ? 324 PRO A CA 1 ATOM 2427 C C . PRO A 1 310 ? 91.689 102.198 16.596 1.00 53.17 ? 324 PRO A C 1 ATOM 2428 O O . PRO A 1 310 ? 90.906 102.938 15.994 1.00 53.62 ? 324 PRO A O 1 ATOM 2429 C CB . PRO A 1 310 ? 91.101 99.747 16.467 1.00 52.73 ? 324 PRO A CB 1 ATOM 2430 C CG . PRO A 1 310 ? 91.902 98.503 16.332 1.00 53.65 ? 324 PRO A CG 1 ATOM 2431 C CD . PRO A 1 310 ? 93.310 98.918 16.699 1.00 53.76 ? 324 PRO A CD 1 ATOM 2432 N N . ILE A 1 311 ? 92.267 102.518 17.759 1.00 50.84 ? 325 ILE A N 1 ATOM 2433 C CA . ILE A 1 311 ? 92.089 103.841 18.348 1.00 51.20 ? 325 ILE A CA 1 ATOM 2434 C C . ILE A 1 311 ? 92.407 104.938 17.325 1.00 57.51 ? 325 ILE A C 1 ATOM 2435 O O . ILE A 1 311 ? 91.630 105.885 17.152 1.00 56.69 ? 325 ILE A O 1 ATOM 2436 C CB . ILE A 1 311 ? 92.987 104.054 19.590 1.00 54.17 ? 325 ILE A CB 1 ATOM 2437 C CG1 . ILE A 1 311 ? 92.632 103.066 20.711 1.00 53.95 ? 325 ILE A CG1 1 ATOM 2438 C CG2 . ILE A 1 311 ? 92.865 105.492 20.112 1.00 52.28 ? 325 ILE A CG2 1 ATOM 2439 C CD1 . ILE A 1 311 ? 91.215 103.218 21.239 1.00 49.56 ? 325 ILE A CD1 1 ATOM 2440 N N . TRP A 1 312 ? 93.533 104.794 16.628 1.00 53.30 ? 326 TRP A N 1 ATOM 2441 C CA . TRP A 1 312 ? 93.988 105.844 15.720 1.00 58.38 ? 326 TRP A CA 1 ATOM 2442 C C . TRP A 1 312 ? 93.205 105.843 14.419 1.00 57.53 ? 326 TRP A C 1 ATOM 2443 O O . TRP A 1 312 ? 93.010 106.888 13.794 1.00 57.01 ? 326 TRP A O 1 ATOM 2444 C CB . TRP A 1 312 ? 95.512 105.768 15.508 1.00 55.75 ? 326 TRP A CB 1 ATOM 2445 C CG . TRP A 1 312 ? 96.217 105.824 16.839 1.00 55.98 ? 326 TRP A CG 1 ATOM 2446 C CD1 . TRP A 1 312 ? 97.006 104.858 17.404 1.00 55.99 ? 326 TRP A CD1 1 ATOM 2447 C CD2 . TRP A 1 312 ? 96.135 106.885 17.797 1.00 56.23 ? 326 TRP A CD2 1 ATOM 2448 N NE1 . TRP A 1 312 ? 97.429 105.266 18.648 1.00 56.25 ? 326 TRP A NE1 1 ATOM 2449 C CE2 . TRP A 1 312 ? 96.898 106.501 18.916 1.00 56.38 ? 326 TRP A CE2 1 ATOM 2450 C CE3 . TRP A 1 312 ? 95.488 108.125 17.815 1.00 56.38 ? 326 TRP A CE3 1 ATOM 2451 C CZ2 . TRP A 1 312 ? 97.028 107.312 20.039 1.00 59.49 ? 326 TRP A CZ2 1 ATOM 2452 C CZ3 . TRP A 1 312 ? 95.612 108.921 18.925 1.00 56.67 ? 326 TRP A CZ3 1 ATOM 2453 C CH2 . TRP A 1 312 ? 96.378 108.518 20.023 1.00 61.78 ? 326 TRP A CH2 1 ATOM 2454 N N . VAL A 1 313 ? 92.730 104.672 14.017 1.00 56.04 ? 327 VAL A N 1 ATOM 2455 C CA . VAL A 1 313 ? 91.904 104.611 12.832 1.00 55.53 ? 327 VAL A CA 1 ATOM 2456 C C . VAL A 1 313 ? 90.598 105.367 13.089 1.00 58.09 ? 327 VAL A C 1 ATOM 2457 O O . VAL A 1 313 ? 90.152 106.151 12.247 1.00 56.33 ? 327 VAL A O 1 ATOM 2458 C CB . VAL A 1 313 ? 91.630 103.171 12.439 1.00 55.04 ? 327 VAL A CB 1 ATOM 2459 C CG1 . VAL A 1 313 ? 90.635 103.128 11.324 1.00 52.68 ? 327 VAL A CG1 1 ATOM 2460 C CG2 . VAL A 1 313 ? 92.929 102.494 12.033 1.00 53.18 ? 327 VAL A CG2 1 ATOM 2461 N N . SER A 1 314 ? 90.003 105.137 14.261 1.00 51.43 ? 328 SER A N 1 ATOM 2462 C CA . SER A 1 314 ? 88.840 105.898 14.683 1.00 52.83 ? 328 SER A CA 1 ATOM 2463 C C . SER A 1 314 ? 89.099 107.408 14.578 1.00 55.19 ? 328 SER A C 1 ATOM 2464 O O . SER A 1 314 ? 88.332 108.141 13.939 1.00 57.38 ? 328 SER A O 1 ATOM 2465 C CB . SER A 1 314 ? 88.473 105.521 16.119 1.00 49.89 ? 328 SER A CB 1 ATOM 2466 O OG . SER A 1 314 ? 88.353 104.115 16.239 1.00 49.02 ? 328 SER A OG 1 ATOM 2467 N N . ALA A 1 315 ? 90.193 107.853 15.193 1.00 54.43 ? 329 ALA A N 1 ATOM 2468 C CA . ALA A 1 315 ? 90.585 109.258 15.189 1.00 57.45 ? 329 ALA A CA 1 ATOM 2469 C C . ALA A 1 315 ? 90.546 109.898 13.794 1.00 58.37 ? 329 ALA A C 1 ATOM 2470 O O . ALA A 1 315 ? 90.080 111.029 13.641 1.00 58.38 ? 329 ALA A O 1 ATOM 2471 C CB . ALA A 1 315 ? 91.968 109.408 15.802 1.00 57.88 ? 329 ALA A CB 1 ATOM 2472 N N . HIS A 1 316 ? 91.019 109.173 12.783 1.00 58.90 ? 330 HIS A N 1 ATOM 2473 C CA . HIS A 1 316 ? 91.040 109.682 11.410 1.00 63.10 ? 330 HIS A CA 1 ATOM 2474 C C . HIS A 1 316 ? 89.668 110.133 10.926 1.00 63.09 ? 330 HIS A C 1 ATOM 2475 O O . HIS A 1 316 ? 89.568 110.901 9.963 1.00 62.10 ? 330 HIS A O 1 ATOM 2476 C CB . HIS A 1 316 ? 91.571 108.624 10.443 1.00 65.50 ? 330 HIS A CB 1 ATOM 2477 C CG . HIS A 1 316 ? 93.057 108.627 10.298 1.00 72.03 ? 330 HIS A CG 1 ATOM 2478 N ND1 . HIS A 1 316 ? 93.727 109.552 9.525 1.00 76.27 ? 330 HIS A ND1 1 ATOM 2479 C CD2 . HIS A 1 316 ? 94.004 107.809 10.813 1.00 74.60 ? 330 HIS A CD2 1 ATOM 2480 C CE1 . HIS A 1 316 ? 95.024 109.310 9.577 1.00 77.36 ? 330 HIS A CE1 1 ATOM 2481 N NE2 . HIS A 1 316 ? 95.219 108.259 10.352 1.00 77.72 ? 330 HIS A NE2 1 ATOM 2482 N N . THR A 1 317 ? 88.611 109.628 11.565 1.00 60.01 ? 331 THR A N 1 ATOM 2483 C CA . THR A 1 317 ? 87.263 110.070 11.241 1.00 55.93 ? 331 THR A CA 1 ATOM 2484 C C . THR A 1 317 ? 86.678 110.889 12.385 1.00 58.53 ? 331 THR A C 1 ATOM 2485 O O . THR A 1 317 ? 86.172 111.990 12.160 1.00 62.58 ? 331 THR A O 1 ATOM 2486 C CB . THR A 1 317 ? 86.342 108.896 10.900 1.00 56.20 ? 331 THR A CB 1 ATOM 2487 O OG1 . THR A 1 317 ? 86.864 108.187 9.765 1.00 56.08 ? 331 THR A OG1 1 ATOM 2488 C CG2 . THR A 1 317 ? 84.954 109.410 10.572 1.00 53.75 ? 331 THR A CG2 1 ATOM 2489 N N . THR A 1 318 ? 86.782 110.374 13.610 1.00 54.94 ? 332 THR A N 1 ATOM 2490 C CA . THR A 1 318 ? 86.124 111.001 14.756 1.00 55.85 ? 332 THR A CA 1 ATOM 2491 C C . THR A 1 318 ? 86.617 112.409 15.133 1.00 57.77 ? 332 THR A C 1 ATOM 2492 O O . THR A 1 318 ? 85.804 113.264 15.488 1.00 57.46 ? 332 THR A O 1 ATOM 2493 C CB . THR A 1 318 ? 86.100 110.077 16.008 1.00 54.60 ? 332 THR A CB 1 ATOM 2494 O OG1 . THR A 1 318 ? 87.434 109.750 16.409 1.00 51.52 ? 332 THR A OG1 1 ATOM 2495 C CG2 . THR A 1 318 ? 85.334 108.787 15.713 1.00 51.50 ? 332 THR A CG2 1 ATOM 2496 N N . GLN A 1 319 ? 87.924 112.657 15.065 1.00 60.53 ? 333 GLN A N 1 ATOM 2497 C CA . GLN A 1 319 ? 88.453 113.985 15.402 1.00 61.09 ? 333 GLN A CA 1 ATOM 2498 C C . GLN A 1 319 ? 88.019 115.065 14.400 1.00 61.50 ? 333 GLN A C 1 ATOM 2499 O O . GLN A 1 319 ? 87.954 116.250 14.732 1.00 63.09 ? 333 GLN A O 1 ATOM 2500 C CB . GLN A 1 319 ? 89.986 113.953 15.509 1.00 60.18 ? 333 GLN A CB 1 ATOM 2501 C CG . GLN A 1 319 ? 90.510 112.935 16.528 1.00 61.33 ? 333 GLN A CG 1 ATOM 2502 C CD . GLN A 1 319 ? 91.721 113.426 17.311 1.00 65.19 ? 333 GLN A CD 1 ATOM 2503 O OE1 . GLN A 1 319 ? 92.087 114.604 17.245 1.00 70.61 ? 333 GLN A OE1 1 ATOM 2504 N NE2 . GLN A 1 319 ? 92.350 112.521 18.056 1.00 62.23 ? 333 GLN A NE2 1 ATOM 2505 N N . PHE A 1 320 ? 87.685 114.640 13.186 1.00 60.44 ? 334 PHE A N 1 ATOM 2506 C CA . PHE A 1 320 ? 87.512 115.564 12.070 1.00 61.61 ? 334 PHE A CA 1 ATOM 2507 C C . PHE A 1 320 ? 86.108 115.520 11.473 1.00 62.72 ? 334 PHE A C 1 ATOM 2508 O O . PHE A 1 320 ? 85.847 116.122 10.421 1.00 60.78 ? 334 PHE A O 1 ATOM 2509 C CB . PHE A 1 320 ? 88.570 115.267 11.011 1.00 57.87 ? 334 PHE A CB 1 ATOM 2510 C CG . PHE A 1 320 ? 89.959 115.150 11.579 1.00 64.59 ? 334 PHE A CG 1 ATOM 2511 C CD1 . PHE A 1 320 ? 90.603 116.269 12.106 1.00 66.29 ? 334 PHE A CD1 1 ATOM 2512 C CD2 . PHE A 1 320 ? 90.619 113.926 11.602 1.00 62.59 ? 334 PHE A CD2 1 ATOM 2513 C CE1 . PHE A 1 320 ? 91.890 116.172 12.647 1.00 67.70 ? 334 PHE A CE1 1 ATOM 2514 C CE2 . PHE A 1 320 ? 91.908 113.822 12.135 1.00 65.23 ? 334 PHE A CE2 1 ATOM 2515 C CZ . PHE A 1 320 ? 92.543 114.949 12.662 1.00 59.95 ? 334 PHE A CZ 1 ATOM 2516 N N . THR A 1 321 ? 85.218 114.790 12.147 1.00 59.98 ? 335 THR A N 1 ATOM 2517 C CA . THR A 1 321 ? 83.798 114.763 11.817 1.00 59.99 ? 335 THR A CA 1 ATOM 2518 C C . THR A 1 321 ? 82.971 114.839 13.102 1.00 59.58 ? 335 THR A C 1 ATOM 2519 O O . THR A 1 321 ? 83.469 114.517 14.182 1.00 58.70 ? 335 THR A O 1 ATOM 2520 C CB . THR A 1 321 ? 83.412 113.476 11.066 1.00 60.38 ? 335 THR A CB 1 ATOM 2521 O OG1 . THR A 1 321 ? 83.701 112.336 11.889 1.00 60.68 ? 335 THR A OG1 1 ATOM 2522 C CG2 . THR A 1 321 ? 84.172 113.367 9.764 1.00 56.31 ? 335 THR A CG2 1 ATOM 2523 N N . GLN A 1 322 ? 81.717 115.273 12.981 1.00 61.03 ? 336 GLN A N 1 ATOM 2524 C CA . GLN A 1 322 ? 80.770 115.277 14.103 1.00 61.00 ? 336 GLN A CA 1 ATOM 2525 C C . GLN A 1 322 ? 79.377 114.937 13.598 1.00 62.00 ? 336 GLN A C 1 ATOM 2526 O O . GLN A 1 322 ? 79.036 115.266 12.456 1.00 64.72 ? 336 GLN A O 1 ATOM 2527 C CB . GLN A 1 322 ? 80.730 116.638 14.798 1.00 64.08 ? 336 GLN A CB 1 ATOM 2528 C CG . GLN A 1 322 ? 81.954 116.956 15.643 1.00 65.00 ? 336 GLN A CG 1 ATOM 2529 C CD . GLN A 1 322 ? 82.045 116.086 16.870 1.00 65.76 ? 336 GLN A CD 1 ATOM 2530 O OE1 . GLN A 1 322 ? 81.027 115.699 17.452 1.00 63.25 ? 336 GLN A OE1 1 ATOM 2531 N NE2 . GLN A 1 322 ? 83.271 115.772 17.279 1.00 66.55 ? 336 GLN A NE2 1 ATOM 2532 N N . PRO A 1 323 ? 78.572 114.258 14.440 1.00 58.46 ? 337 PRO A N 1 ATOM 2533 C CA . PRO A 1 323 ? 77.177 113.989 14.083 1.00 55.41 ? 337 PRO A CA 1 ATOM 2534 C C . PRO A 1 323 ? 76.475 115.282 13.677 1.00 55.56 ? 337 PRO A C 1 ATOM 2535 O O . PRO A 1 323 ? 76.592 116.280 14.391 1.00 61.42 ? 337 PRO A O 1 ATOM 2536 C CB . PRO A 1 323 ? 76.580 113.458 15.401 1.00 52.50 ? 337 PRO A CB 1 ATOM 2537 C CG . PRO A 1 323 ? 77.725 112.784 16.077 1.00 51.83 ? 337 PRO A CG 1 ATOM 2538 C CD . PRO A 1 323 ? 78.934 113.658 15.742 1.00 56.35 ? 337 PRO A CD 1 ATOM 2539 N N . GLY A 1 324 ? 75.765 115.265 12.553 1.00 58.16 ? 338 GLY A N 1 ATOM 2540 C CA . GLY A 1 324 ? 75.094 116.455 12.067 1.00 56.83 ? 338 GLY A CA 1 ATOM 2541 C C . GLY A 1 324 ? 75.779 117.053 10.847 1.00 59.61 ? 338 GLY A C 1 ATOM 2542 O O . GLY A 1 324 ? 75.191 117.888 10.158 1.00 60.27 ? 338 GLY A O 1 ATOM 2543 N N . TRP A 1 325 ? 77.023 116.642 10.591 1.00 59.76 ? 339 TRP A N 1 ATOM 2544 C CA . TRP A 1 325 ? 77.714 116.963 9.343 1.00 62.71 ? 339 TRP A CA 1 ATOM 2545 C C . TRP A 1 325 ? 77.008 116.255 8.203 1.00 62.20 ? 339 TRP A C 1 ATOM 2546 O O . TRP A 1 325 ? 76.065 115.494 8.437 1.00 59.44 ? 339 TRP A O 1 ATOM 2547 C CB . TRP A 1 325 ? 79.164 116.483 9.389 1.00 66.66 ? 339 TRP A CB 1 ATOM 2548 C CG . TRP A 1 325 ? 80.089 117.405 10.131 1.00 70.94 ? 339 TRP A CG 1 ATOM 2549 C CD1 . TRP A 1 325 ? 79.799 118.133 11.251 1.00 72.25 ? 339 TRP A CD1 1 ATOM 2550 C CD2 . TRP A 1 325 ? 81.456 117.705 9.801 1.00 74.20 ? 339 TRP A CD2 1 ATOM 2551 N NE1 . TRP A 1 325 ? 80.900 118.862 11.637 1.00 75.10 ? 339 TRP A NE1 1 ATOM 2552 C CE2 . TRP A 1 325 ? 81.929 118.617 10.765 1.00 74.97 ? 339 TRP A CE2 1 ATOM 2553 C CE3 . TRP A 1 325 ? 82.323 117.294 8.781 1.00 77.87 ? 339 TRP A CE3 1 ATOM 2554 C CZ2 . TRP A 1 325 ? 83.233 119.126 10.739 1.00 78.06 ? 339 TRP A CZ2 1 ATOM 2555 C CZ3 . TRP A 1 325 ? 83.618 117.803 8.754 1.00 77.72 ? 339 TRP A CZ3 1 ATOM 2556 C CH2 . TRP A 1 325 ? 84.058 118.707 9.726 1.00 77.66 ? 339 TRP A CH2 1 ATOM 2557 N N . TYR A 1 326 ? 77.455 116.492 6.972 1.00 60.27 ? 340 TYR A N 1 ATOM 2558 C CA . TYR A 1 326 ? 76.901 115.757 5.826 1.00 61.52 ? 340 TYR A CA 1 ATOM 2559 C C . TYR A 1 326 ? 77.969 115.097 4.949 1.00 61.01 ? 340 TYR A C 1 ATOM 2560 O O . TYR A 1 326 ? 79.061 115.637 4.763 1.00 61.47 ? 340 TYR A O 1 ATOM 2561 C CB . TYR A 1 326 ? 76.011 116.657 4.958 1.00 62.27 ? 340 TYR A CB 1 ATOM 2562 C CG . TYR A 1 326 ? 74.645 116.927 5.539 1.00 62.65 ? 340 TYR A CG 1 ATOM 2563 C CD1 . TYR A 1 326 ? 74.482 117.815 6.594 1.00 64.67 ? 340 TYR A CD1 1 ATOM 2564 C CD2 . TYR A 1 326 ? 73.513 116.310 5.018 1.00 63.02 ? 340 TYR A CD2 1 ATOM 2565 C CE1 . TYR A 1 326 ? 73.229 118.068 7.129 1.00 65.78 ? 340 TYR A CE1 1 ATOM 2566 C CE2 . TYR A 1 326 ? 72.256 116.558 5.547 1.00 65.84 ? 340 TYR A CE2 1 ATOM 2567 C CZ . TYR A 1 326 ? 72.123 117.440 6.600 1.00 68.53 ? 340 TYR A CZ 1 ATOM 2568 O OH . TYR A 1 326 ? 70.878 117.694 7.134 1.00 73.08 ? 340 TYR A OH 1 ATOM 2569 N N . TYR A 1 327 ? 77.652 113.917 4.428 1.00 62.92 ? 341 TYR A N 1 ATOM 2570 C CA . TYR A 1 327 ? 78.481 113.311 3.395 1.00 66.18 ? 341 TYR A CA 1 ATOM 2571 C C . TYR A 1 327 ? 78.260 114.094 2.097 1.00 65.70 ? 341 TYR A C 1 ATOM 2572 O O . TYR A 1 327 ? 77.163 114.599 1.844 1.00 59.07 ? 341 TYR A O 1 ATOM 2573 C CB . TYR A 1 327 ? 78.123 111.832 3.198 1.00 64.58 ? 341 TYR A CB 1 ATOM 2574 C CG . TYR A 1 327 ? 78.771 110.893 4.201 1.00 62.60 ? 341 TYR A CG 1 ATOM 2575 C CD1 . TYR A 1 327 ? 80.105 110.523 4.070 1.00 62.34 ? 341 TYR A CD1 1 ATOM 2576 C CD2 . TYR A 1 327 ? 78.046 110.366 5.270 1.00 61.02 ? 341 TYR A CD2 1 ATOM 2577 C CE1 . TYR A 1 327 ? 80.706 109.663 4.980 1.00 59.69 ? 341 TYR A CE1 1 ATOM 2578 C CE2 . TYR A 1 327 ? 78.642 109.497 6.192 1.00 60.56 ? 341 TYR A CE2 1 ATOM 2579 C CZ . TYR A 1 327 ? 79.976 109.155 6.033 1.00 61.44 ? 341 TYR A CZ 1 ATOM 2580 O OH . TYR A 1 327 ? 80.599 108.305 6.921 1.00 59.14 ? 341 TYR A OH 1 ATOM 2581 N N . LEU A 1 328 ? 79.303 114.229 1.291 1.00 59.52 ? 342 LEU A N 1 ATOM 2582 C CA . LEU A 1 328 ? 79.130 114.805 -0.038 1.00 60.26 ? 342 LEU A CA 1 ATOM 2583 C C . LEU A 1 328 ? 78.534 113.737 -0.955 1.00 67.25 ? 342 LEU A C 1 ATOM 2584 O O . LEU A 1 328 ? 78.547 112.547 -0.624 1.00 59.26 ? 342 LEU A O 1 ATOM 2585 C CB . LEU A 1 328 ? 80.470 115.278 -0.595 1.00 60.98 ? 342 LEU A CB 1 ATOM 2586 C CG . LEU A 1 328 ? 81.168 116.399 0.166 1.00 69.14 ? 342 LEU A CG 1 ATOM 2587 C CD1 . LEU A 1 328 ? 82.482 116.737 -0.500 1.00 72.61 ? 342 LEU A CD1 1 ATOM 2588 C CD2 . LEU A 1 328 ? 80.286 117.618 0.204 1.00 68.71 ? 342 LEU A CD2 1 ATOM 2589 N N . LYS A 1 329 ? 78.015 114.151 -2.106 1.00 68.31 ? 343 LYS A N 1 ATOM 2590 C CA . LYS A 1 329 ? 77.600 113.181 -3.112 1.00 70.00 ? 343 LYS A CA 1 ATOM 2591 C C . LYS A 1 329 ? 78.835 112.538 -3.728 1.00 69.57 ? 343 LYS A C 1 ATOM 2592 O O . LYS A 1 329 ? 78.776 111.427 -4.257 1.00 71.11 ? 343 LYS A O 1 ATOM 2593 C CB . LYS A 1 329 ? 76.731 113.837 -4.189 1.00 71.75 ? 343 LYS A CB 1 ATOM 2594 C CG . LYS A 1 329 ? 75.377 114.294 -3.665 1.00 74.18 ? 343 LYS A CG 1 ATOM 2595 C CD . LYS A 1 329 ? 74.447 114.736 -4.783 1.00 75.10 ? 343 LYS A CD 1 ATOM 2596 C CE . LYS A 1 329 ? 73.114 115.184 -4.194 1.00 77.63 ? 343 LYS A CE 1 ATOM 2597 N NZ . LYS A 1 329 ? 72.066 115.409 -5.233 1.00 79.45 ? 343 LYS A NZ 1 ATOM 2598 N N . THR A 1 330 ? 79.961 113.232 -3.626 1.00 66.66 ? 344 THR A N 1 ATOM 2599 C CA . THR A 1 330 ? 81.184 112.787 -4.283 1.00 66.15 ? 344 THR A CA 1 ATOM 2600 C C . THR A 1 330 ? 82.076 111.914 -3.398 1.00 63.88 ? 344 THR A C 1 ATOM 2601 O O . THR A 1 330 ? 83.042 112.391 -2.794 1.00 64.14 ? 344 THR A O 1 ATOM 2602 C CB . THR A 1 330 ? 81.988 113.983 -4.864 1.00 69.58 ? 344 THR A CB 1 ATOM 2603 O OG1 . THR A 1 330 ? 82.154 115.004 -3.863 1.00 70.82 ? 344 THR A OG1 1 ATOM 2604 C CG2 . THR A 1 330 ? 81.258 114.566 -6.068 1.00 66.17 ? 344 THR A CG2 1 ATOM 2605 N N . VAL A 1 331 ? 81.736 110.632 -3.322 1.00 60.23 ? 345 VAL A N 1 ATOM 2606 C CA . VAL A 1 331 ? 82.588 109.643 -2.679 1.00 64.25 ? 345 VAL A CA 1 ATOM 2607 C C . VAL A 1 331 ? 82.582 108.388 -3.545 1.00 64.05 ? 345 VAL A C 1 ATOM 2608 O O . VAL A 1 331 ? 81.664 108.191 -4.348 1.00 59.70 ? 345 VAL A O 1 ATOM 2609 C CB . VAL A 1 331 ? 82.089 109.277 -1.248 1.00 62.67 ? 345 VAL A CB 1 ATOM 2610 C CG1 . VAL A 1 331 ? 81.898 110.527 -0.389 1.00 62.08 ? 345 VAL A CG1 1 ATOM 2611 C CG2 . VAL A 1 331 ? 80.807 108.488 -1.322 1.00 58.29 ? 345 VAL A CG2 1 ATOM 2612 N N . GLY A 1 332 ? 83.593 107.537 -3.390 1.00 62.35 ? 346 GLY A N 1 ATOM 2613 C CA . GLY A 1 332 ? 83.620 106.276 -4.114 1.00 61.17 ? 346 GLY A CA 1 ATOM 2614 C C . GLY A 1 332 ? 84.922 105.514 -3.955 1.00 62.81 ? 346 GLY A C 1 ATOM 2615 O O . GLY A 1 332 ? 85.718 105.800 -3.051 1.00 63.06 ? 346 GLY A O 1 ATOM 2616 N N . HIS A 1 333 ? 85.143 104.541 -4.836 1.00 62.91 ? 347 HIS A N 1 ATOM 2617 C CA . HIS A 1 333 ? 86.350 103.721 -4.797 1.00 63.53 ? 347 HIS A CA 1 ATOM 2618 C C . HIS A 1 333 ? 87.472 104.299 -5.668 1.00 66.93 ? 347 HIS A C 1 ATOM 2619 O O . HIS A 1 333 ? 87.211 104.949 -6.689 1.00 67.81 ? 347 HIS A O 1 ATOM 2620 C CB . HIS A 1 333 ? 86.022 102.293 -5.239 1.00 64.92 ? 347 HIS A CB 1 ATOM 2621 C CG . HIS A 1 333 ? 85.176 101.537 -4.263 1.00 70.00 ? 347 HIS A CG 1 ATOM 2622 N ND1 . HIS A 1 333 ? 85.611 100.387 -3.639 1.00 72.66 ? 347 HIS A ND1 1 ATOM 2623 C CD2 . HIS A 1 333 ? 83.919 101.758 -3.809 1.00 71.27 ? 347 HIS A CD2 1 ATOM 2624 C CE1 . HIS A 1 333 ? 84.663 99.937 -2.836 1.00 70.66 ? 347 HIS A CE1 1 ATOM 2625 N NE2 . HIS A 1 333 ? 83.626 100.751 -2.921 1.00 70.76 ? 347 HIS A NE2 1 ATOM 2626 N N . LEU A 1 334 ? 88.722 104.064 -5.268 1.00 67.07 ? 348 LEU A N 1 ATOM 2627 C CA . LEU A 1 334 ? 89.869 104.494 -6.077 1.00 66.02 ? 348 LEU A CA 1 ATOM 2628 C C . LEU A 1 334 ? 90.120 103.488 -7.196 1.00 65.63 ? 348 LEU A C 1 ATOM 2629 O O . LEU A 1 334 ? 89.772 102.312 -7.062 1.00 67.12 ? 348 LEU A O 1 ATOM 2630 C CB . LEU A 1 334 ? 91.116 104.681 -5.203 1.00 63.69 ? 348 LEU A CB 1 ATOM 2631 C CG . LEU A 1 334 ? 90.900 105.741 -4.123 1.00 62.87 ? 348 LEU A CG 1 ATOM 2632 C CD1 . LEU A 1 334 ? 92.039 105.790 -3.116 1.00 62.84 ? 348 LEU A CD1 1 ATOM 2633 C CD2 . LEU A 1 334 ? 90.697 107.099 -4.771 1.00 64.15 ? 348 LEU A CD2 1 ATOM 2634 N N . GLU A 1 335 ? 90.707 103.955 -8.297 1.00 65.32 ? 349 GLU A N 1 ATOM 2635 C CA . GLU A 1 335 ? 90.922 103.123 -9.487 1.00 64.60 ? 349 GLU A CA 1 ATOM 2636 C C . GLU A 1 335 ? 91.682 101.822 -9.197 1.00 64.26 ? 349 GLU A C 1 ATOM 2637 O O . GLU A 1 335 ? 91.270 100.744 -9.642 1.00 63.92 ? 349 GLU A O 1 ATOM 2638 C CB . GLU A 1 335 ? 91.637 103.928 -10.591 1.00 64.34 ? 349 GLU A CB 1 ATOM 2639 N N . LYS A 1 336 ? 92.775 101.929 -8.443 1.00 67.34 ? 350 LYS A N 1 ATOM 2640 C CA . LYS A 1 336 ? 93.637 100.782 -8.138 1.00 68.96 ? 350 LYS A CA 1 ATOM 2641 C C . LYS A 1 336 ? 93.381 100.197 -6.739 1.00 67.50 ? 350 LYS A C 1 ATOM 2642 O O . LYS A 1 336 ? 94.227 99.480 -6.184 1.00 64.85 ? 350 LYS A O 1 ATOM 2643 C CB . LYS A 1 336 ? 95.119 101.169 -8.292 1.00 71.92 ? 350 LYS A CB 1 ATOM 2644 C CG . LYS A 1 336 ? 95.468 101.836 -9.623 1.00 74.92 ? 350 LYS A CG 1 ATOM 2645 C CD . LYS A 1 336 ? 95.282 100.896 -10.814 1.00 79.59 ? 350 LYS A CD 1 ATOM 2646 C CE . LYS A 1 336 ? 96.368 99.817 -10.873 1.00 83.16 ? 350 LYS A CE 1 ATOM 2647 N NZ . LYS A 1 336 ? 96.169 98.841 -11.993 1.00 85.07 ? 350 LYS A NZ 1 ATOM 2648 N N . GLY A 1 337 ? 92.214 100.501 -6.173 1.00 66.49 ? 351 GLY A N 1 ATOM 2649 C CA . GLY A 1 337 ? 91.832 99.947 -4.881 1.00 66.46 ? 351 GLY A CA 1 ATOM 2650 C C . GLY A 1 337 ? 91.785 100.958 -3.748 1.00 63.61 ? 351 GLY A C 1 ATOM 2651 O O . GLY A 1 337 ? 92.498 101.965 -3.762 1.00 63.09 ? 351 GLY A O 1 ATOM 2652 N N . GLY A 1 338 ? 90.953 100.678 -2.749 1.00 65.86 ? 352 GLY A N 1 ATOM 2653 C CA . GLY A 1 338 ? 90.784 101.595 -1.637 1.00 64.97 ? 352 GLY A CA 1 ATOM 2654 C C . GLY A 1 338 ? 89.627 102.532 -1.911 1.00 64.46 ? 352 GLY A C 1 ATOM 2655 O O . GLY A 1 338 ? 88.936 102.386 -2.924 1.00 65.62 ? 352 GLY A O 1 ATOM 2656 N N . SER A 1 339 ? 89.412 103.498 -1.023 1.00 62.00 ? 353 SER A N 1 ATOM 2657 C CA . SER A 1 339 ? 88.223 104.340 -1.105 1.00 62.70 ? 353 SER A CA 1 ATOM 2658 C C . SER A 1 339 ? 88.462 105.723 -0.528 1.00 63.26 ? 353 SER A C 1 ATOM 2659 O O . SER A 1 339 ? 89.453 105.962 0.168 1.00 59.48 ? 353 SER A O 1 ATOM 2660 C CB . SER A 1 339 ? 87.035 103.669 -0.386 1.00 64.44 ? 353 SER A CB 1 ATOM 2661 O OG . SER A 1 339 ? 87.364 103.307 0.945 1.00 57.65 ? 353 SER A OG 1 ATOM 2662 N N . TYR A 1 340 ? 87.539 106.631 -0.820 1.00 59.39 ? 354 TYR A N 1 ATOM 2663 C CA . TYR A 1 340 ? 87.616 107.993 -0.306 1.00 64.33 ? 354 TYR A CA 1 ATOM 2664 C C . TYR A 1 340 ? 86.216 108.475 0.059 1.00 66.84 ? 354 TYR A C 1 ATOM 2665 O O . TYR A 1 340 ? 85.265 108.300 -0.714 1.00 68.33 ? 354 TYR A O 1 ATOM 2666 C CB . TYR A 1 340 ? 88.267 108.926 -1.342 1.00 66.67 ? 354 TYR A CB 1 ATOM 2667 C CG . TYR A 1 340 ? 87.460 109.155 -2.604 1.00 67.64 ? 354 TYR A CG 1 ATOM 2668 C CD1 . TYR A 1 340 ? 87.552 108.281 -3.681 1.00 69.19 ? 354 TYR A CD1 1 ATOM 2669 C CD2 . TYR A 1 340 ? 86.622 110.261 -2.729 1.00 69.14 ? 354 TYR A CD2 1 ATOM 2670 C CE1 . TYR A 1 340 ? 86.818 108.492 -4.847 1.00 70.21 ? 354 TYR A CE1 1 ATOM 2671 C CE2 . TYR A 1 340 ? 85.882 110.481 -3.890 1.00 70.02 ? 354 TYR A CE2 1 ATOM 2672 C CZ . TYR A 1 340 ? 85.985 109.593 -4.945 1.00 69.30 ? 354 TYR A CZ 1 ATOM 2673 O OH . TYR A 1 340 ? 85.257 109.800 -6.102 1.00 68.42 ? 354 TYR A OH 1 ATOM 2674 N N . VAL A 1 341 ? 86.073 109.032 1.259 1.00 66.47 ? 355 VAL A N 1 ATOM 2675 C CA . VAL A 1 341 ? 84.854 109.746 1.605 1.00 58.82 ? 355 VAL A CA 1 ATOM 2676 C C . VAL A 1 341 ? 85.202 111.196 1.906 1.00 67.27 ? 355 VAL A C 1 ATOM 2677 O O . VAL A 1 341 ? 86.347 111.523 2.238 1.00 59.78 ? 355 VAL A O 1 ATOM 2678 C CB . VAL A 1 341 ? 84.082 109.110 2.798 1.00 63.00 ? 355 VAL A CB 1 ATOM 2679 C CG1 . VAL A 1 341 ? 83.838 107.629 2.550 1.00 61.95 ? 355 VAL A CG1 1 ATOM 2680 C CG2 . VAL A 1 341 ? 84.817 109.340 4.125 1.00 57.84 ? 355 VAL A CG2 1 ATOM 2681 N N . ALA A 1 342 ? 84.205 112.063 1.778 1.00 67.33 ? 356 ALA A N 1 ATOM 2682 C CA . ALA A 1 342 ? 84.389 113.480 2.048 1.00 65.15 ? 356 ALA A CA 1 ATOM 2683 C C . ALA A 1 342 ? 83.143 114.018 2.745 1.00 63.84 ? 356 ALA A C 1 ATOM 2684 O O . ALA A 1 342 ? 82.017 113.635 2.410 1.00 59.47 ? 356 ALA A O 1 ATOM 2685 C CB . ALA A 1 342 ? 84.649 114.232 0.762 1.00 60.97 ? 356 ALA A CB 1 ATOM 2686 N N . LEU A 1 343 ? 83.351 114.893 3.725 1.00 63.87 ? 357 LEU A N 1 ATOM 2687 C CA . LEU A 1 343 ? 82.244 115.474 4.478 1.00 63.98 ? 357 LEU A CA 1 ATOM 2688 C C . LEU A 1 343 ? 82.480 116.955 4.727 1.00 64.30 ? 357 LEU A C 1 ATOM 2689 O O . LEU A 1 343 ? 83.623 117.429 4.739 1.00 61.07 ? 357 LEU A O 1 ATOM 2690 C CB . LEU A 1 343 ? 82.049 114.763 5.823 1.00 59.01 ? 357 LEU A CB 1 ATOM 2691 C CG . LEU A 1 343 ? 81.863 113.244 5.846 1.00 58.21 ? 357 LEU A CG 1 ATOM 2692 C CD1 . LEU A 1 343 ? 83.209 112.542 5.928 1.00 58.23 ? 357 LEU A CD1 1 ATOM 2693 C CD2 . LEU A 1 343 ? 80.956 112.816 7.006 1.00 57.45 ? 357 LEU A CD2 1 ATOM 2694 N N . THR A 1 344 ? 81.388 117.686 4.924 1.00 64.13 ? 358 THR A N 1 ATOM 2695 C CA . THR A 1 344 ? 81.467 119.100 5.261 1.00 64.68 ? 358 THR A CA 1 ATOM 2696 C C . THR A 1 344 ? 80.566 119.298 6.461 1.00 64.11 ? 358 THR A C 1 ATOM 2697 O O . THR A 1 344 ? 80.067 118.328 7.002 1.00 66.01 ? 358 THR A O 1 ATOM 2698 C CB . THR A 1 344 ? 80.984 119.989 4.105 1.00 64.26 ? 358 THR A CB 1 ATOM 2699 O OG1 . THR A 1 344 ? 79.594 119.729 3.850 1.00 64.74 ? 358 THR A OG1 1 ATOM 2700 C CG2 . THR A 1 344 ? 81.798 119.709 2.842 1.00 63.07 ? 358 THR A CG2 1 ATOM 2701 N N . ASP A 1 345 ? 80.339 120.547 6.854 1.00 66.29 ? 359 ASP A N 1 ATOM 2702 C CA . ASP A 1 345 ? 79.498 120.850 8.006 1.00 70.37 ? 359 ASP A CA 1 ATOM 2703 C C . ASP A 1 345 ? 78.535 122.008 7.746 1.00 74.07 ? 359 ASP A C 1 ATOM 2704 O O . ASP A 1 345 ? 77.802 122.425 8.646 1.00 74.46 ? 359 ASP A O 1 ATOM 2705 C CB . ASP A 1 345 ? 80.365 121.178 9.221 1.00 71.18 ? 359 ASP A CB 1 ATOM 2706 C CG . ASP A 1 345 ? 81.261 122.385 8.992 1.00 76.76 ? 359 ASP A CG 1 ATOM 2707 O OD1 . ASP A 1 345 ? 81.415 122.823 7.823 1.00 78.96 ? 359 ASP A OD1 1 ATOM 2708 O OD2 . ASP A 1 345 ? 81.825 122.892 9.988 1.00 76.91 ? 359 ASP A OD2 1 ATOM 2709 N N . GLY A 1 346 ? 78.548 122.527 6.520 1.00 78.52 ? 360 GLY A N 1 ATOM 2710 C CA . GLY A 1 346 ? 77.774 123.709 6.187 1.00 81.04 ? 360 GLY A CA 1 ATOM 2711 C C . GLY A 1 346 ? 78.412 124.989 6.709 1.00 81.35 ? 360 GLY A C 1 ATOM 2712 O O . GLY A 1 346 ? 77.839 126.068 6.566 1.00 82.18 ? 360 GLY A O 1 ATOM 2713 N N . LEU A 1 347 ? 79.591 124.870 7.321 1.00 80.24 ? 361 LEU A N 1 ATOM 2714 C CA . LEU A 1 347 ? 80.299 126.025 7.880 1.00 81.48 ? 361 LEU A CA 1 ATOM 2715 C C . LEU A 1 347 ? 81.629 126.236 7.171 1.00 81.98 ? 361 LEU A C 1 ATOM 2716 O O . LEU A 1 347 ? 82.549 126.854 7.717 1.00 84.81 ? 361 LEU A O 1 ATOM 2717 C CB . LEU A 1 347 ? 80.515 125.874 9.393 1.00 81.27 ? 361 LEU A CB 1 ATOM 2718 C CG . LEU A 1 347 ? 79.255 125.842 10.271 1.00 79.39 ? 361 LEU A CG 1 ATOM 2719 C CD1 . LEU A 1 347 ? 79.595 125.765 11.761 1.00 75.35 ? 361 LEU A CD1 1 ATOM 2720 C CD2 . LEU A 1 347 ? 78.376 127.051 9.979 1.00 81.48 ? 361 LEU A CD2 1 ATOM 2721 N N . GLY A 1 348 ? 81.730 125.720 5.951 1.00 78.99 ? 362 GLY A N 1 ATOM 2722 C CA . GLY A 1 348 ? 82.922 125.930 5.152 1.00 79.82 ? 362 GLY A CA 1 ATOM 2723 C C . GLY A 1 348 ? 84.059 124.964 5.428 1.00 80.93 ? 362 GLY A C 1 ATOM 2724 O O . GLY A 1 348 ? 85.073 124.966 4.725 1.00 80.83 ? 362 GLY A O 1 ATOM 2725 N N . ASN A 1 349 ? 83.907 124.131 6.451 1.00 81.73 ? 363 ASN A N 1 ATOM 2726 C CA . ASN A 1 349 ? 84.912 123.109 6.699 1.00 82.34 ? 363 ASN A CA 1 ATOM 2727 C C . ASN A 1 349 ? 84.719 121.887 5.812 1.00 72.22 ? 363 ASN A C 1 ATOM 2728 O O . ASN A 1 349 ? 83.606 121.600 5.356 1.00 68.44 ? 363 ASN A O 1 ATOM 2729 C CB . ASN A 1 349 ? 84.933 122.705 8.170 1.00 93.97 ? 363 ASN A CB 1 ATOM 2730 C CG . ASN A 1 349 ? 85.451 123.807 9.059 1.00 105.73 ? 363 ASN A CG 1 ATOM 2731 O OD1 . ASN A 1 349 ? 86.648 123.887 9.342 1.00 103.34 ? 363 ASN A OD1 1 ATOM 2732 N ND2 . ASN A 1 349 ? 84.551 124.672 9.499 1.00 120.47 ? 363 ASN A ND2 1 ATOM 2733 N N . LEU A 1 350 ? 85.813 121.175 5.564 1.00 66.38 ? 364 LEU A N 1 ATOM 2734 C CA . LEU A 1 350 ? 85.774 119.978 4.735 1.00 65.70 ? 364 LEU A CA 1 ATOM 2735 C C . LEU A 1 350 ? 86.722 118.919 5.285 1.00 65.95 ? 364 LEU A C 1 ATOM 2736 O O . LEU A 1 350 ? 87.841 119.233 5.690 1.00 66.12 ? 364 LEU A O 1 ATOM 2737 C CB . LEU A 1 350 ? 86.150 120.321 3.288 1.00 66.63 ? 364 LEU A CB 1 ATOM 2738 C CG . LEU A 1 350 ? 86.501 119.171 2.334 1.00 63.39 ? 364 LEU A CG 1 ATOM 2739 C CD1 . LEU A 1 350 ? 85.287 118.324 1.987 1.00 62.75 ? 364 LEU A CD1 1 ATOM 2740 C CD2 . LEU A 1 350 ? 87.170 119.713 1.059 1.00 64.22 ? 364 LEU A CD2 1 ATOM 2741 N N . THR A 1 351 ? 86.274 117.667 5.305 1.00 66.33 ? 365 THR A N 1 ATOM 2742 C CA . THR A 1 351 ? 87.136 116.569 5.721 1.00 66.97 ? 365 THR A CA 1 ATOM 2743 C C . THR A 1 351 ? 87.231 115.512 4.636 1.00 61.14 ? 365 THR A C 1 ATOM 2744 O O . THR A 1 351 ? 86.217 115.099 4.077 1.00 63.09 ? 365 THR A O 1 ATOM 2745 C CB . THR A 1 351 ? 86.628 115.908 7.014 1.00 67.00 ? 365 THR A CB 1 ATOM 2746 O OG1 . THR A 1 351 ? 86.523 116.905 8.036 1.00 67.45 ? 365 THR A OG1 1 ATOM 2747 C CG2 . THR A 1 351 ? 87.591 114.810 7.457 1.00 60.25 ? 365 THR A CG2 1 ATOM 2748 N N . ILE A 1 352 ? 88.451 115.080 4.340 1.00 69.39 ? 366 ILE A N 1 ATOM 2749 C CA . ILE A 1 352 ? 88.664 114.005 3.379 1.00 69.94 ? 366 ILE A CA 1 ATOM 2750 C C . ILE A 1 352 ? 89.375 112.832 4.052 1.00 68.14 ? 366 ILE A C 1 ATOM 2751 O O . ILE A 1 352 ? 90.427 113.003 4.679 1.00 66.00 ? 366 ILE A O 1 ATOM 2752 C CB . ILE A 1 352 ? 89.465 114.495 2.154 1.00 73.75 ? 366 ILE A CB 1 ATOM 2753 C CG1 . ILE A 1 352 ? 88.674 115.571 1.405 1.00 62.50 ? 366 ILE A CG1 1 ATOM 2754 C CG2 . ILE A 1 352 ? 89.790 113.336 1.227 1.00 61.93 ? 366 ILE A CG2 1 ATOM 2755 C CD1 . ILE A 1 352 ? 89.503 116.349 0.398 1.00 63.41 ? 366 ILE A CD1 1 ATOM 2756 N N . ILE A 1 353 ? 88.777 111.648 3.947 1.00 65.73 ? 367 ILE A N 1 ATOM 2757 C CA . ILE A 1 353 ? 89.349 110.447 4.547 1.00 64.57 ? 367 ILE A CA 1 ATOM 2758 C C . ILE A 1 353 ? 89.584 109.416 3.454 1.00 64.71 ? 367 ILE A C 1 ATOM 2759 O O . ILE A 1 353 ? 88.649 109.011 2.755 1.00 61.55 ? 367 ILE A O 1 ATOM 2760 C CB . ILE A 1 353 ? 88.436 109.856 5.648 1.00 61.42 ? 367 ILE A CB 1 ATOM 2761 C CG1 . ILE A 1 353 ? 88.160 110.905 6.726 1.00 62.43 ? 367 ILE A CG1 1 ATOM 2762 C CG2 . ILE A 1 353 ? 89.062 108.600 6.255 1.00 58.96 ? 367 ILE A CG2 1 ATOM 2763 C CD1 . ILE A 1 353 ? 86.796 110.763 7.412 1.00 61.44 ? 367 ILE A CD1 1 ATOM 2764 N N . ILE A 1 354 ? 90.839 109.005 3.306 1.00 66.45 ? 368 ILE A N 1 ATOM 2765 C CA . ILE A 1 354 ? 91.224 108.077 2.258 1.00 67.44 ? 368 ILE A CA 1 ATOM 2766 C C . ILE A 1 354 ? 91.849 106.830 2.870 1.00 66.16 ? 368 ILE A C 1 ATOM 2767 O O . ILE A 1 354 ? 92.627 106.923 3.815 1.00 65.63 ? 368 ILE A O 1 ATOM 2768 C CB . ILE A 1 354 ? 92.211 108.756 1.286 1.00 69.54 ? 368 ILE A CB 1 ATOM 2769 C CG1 . ILE A 1 354 ? 91.604 110.066 0.786 1.00 61.41 ? 368 ILE A CG1 1 ATOM 2770 C CG2 . ILE A 1 354 ? 92.555 107.837 0.123 1.00 61.22 ? 368 ILE A CG2 1 ATOM 2771 C CD1 . ILE A 1 354 ? 92.562 110.942 0.027 1.00 62.31 ? 368 ILE A CD1 1 ATOM 2772 N N . GLU A 1 355 ? 91.504 105.664 2.334 1.00 59.45 ? 369 GLU A N 1 ATOM 2773 C CA . GLU A 1 355 ? 92.019 104.401 2.855 1.00 63.49 ? 369 GLU A CA 1 ATOM 2774 C C . GLU A 1 355 ? 92.449 103.484 1.708 1.00 63.62 ? 369 GLU A C 1 ATOM 2775 O O . GLU A 1 355 ? 91.810 103.467 0.657 1.00 64.74 ? 369 GLU A O 1 ATOM 2776 C CB . GLU A 1 355 ? 90.962 103.741 3.763 1.00 63.25 ? 369 GLU A CB 1 ATOM 2777 C CG . GLU A 1 355 ? 90.912 102.213 3.719 1.00 64.46 ? 369 GLU A CG 1 ATOM 2778 C CD . GLU A 1 355 ? 90.037 101.674 2.607 1.00 64.23 ? 369 GLU A CD 1 ATOM 2779 O OE1 . GLU A 1 355 ? 89.173 102.423 2.102 1.00 62.04 ? 369 GLU A OE1 1 ATOM 2780 O OE2 . GLU A 1 355 ? 90.209 100.492 2.238 1.00 69.85 ? 369 GLU A OE2 1 ATOM 2781 N N . THR A 1 356 ? 93.535 102.737 1.899 1.00 59.61 ? 370 THR A N 1 ATOM 2782 C CA . THR A 1 356 ? 94.020 101.818 0.864 1.00 59.94 ? 370 THR A CA 1 ATOM 2783 C C . THR A 1 356 ? 94.291 100.412 1.402 1.00 59.58 ? 370 THR A C 1 ATOM 2784 O O . THR A 1 356 ? 95.316 99.803 1.086 1.00 64.10 ? 370 THR A O 1 ATOM 2785 C CB . THR A 1 356 ? 95.299 102.367 0.147 1.00 64.19 ? 370 THR A CB 1 ATOM 2786 O OG1 . THR A 1 356 ? 96.320 102.662 1.113 1.00 65.52 ? 370 THR A OG1 1 ATOM 2787 C CG2 . THR A 1 356 ? 94.976 103.626 -0.641 1.00 61.27 ? 370 THR A CG2 1 ATOM 2788 N N . MET A 1 357 ? 93.358 99.887 2.192 1.00 58.80 ? 371 MET A N 1 ATOM 2789 C CA . MET A 1 357 ? 93.587 98.632 2.902 1.00 63.15 ? 371 MET A CA 1 ATOM 2790 C C . MET A 1 357 ? 93.707 97.395 2.001 1.00 62.68 ? 371 MET A C 1 ATOM 2791 O O . MET A 1 357 ? 92.777 97.042 1.260 1.00 60.05 ? 371 MET A O 1 ATOM 2792 C CB . MET A 1 357 ? 92.517 98.414 3.984 1.00 62.44 ? 371 MET A CB 1 ATOM 2793 C CG . MET A 1 357 ? 92.554 99.450 5.111 1.00 65.67 ? 371 MET A CG 1 ATOM 2794 S SD . MET A 1 357 ? 94.166 99.644 5.911 1.00 67.14 ? 371 MET A SD 1 ATOM 2795 C CE . MET A 1 357 ? 94.303 101.430 5.956 1.00 58.52 ? 371 MET A CE 1 ATOM 2796 N N . SER A 1 358 ? 94.864 96.739 2.077 1.00 64.44 ? 372 SER A N 1 ATOM 2797 C CA . SER A 1 358 ? 95.108 95.510 1.318 1.00 64.36 ? 372 SER A CA 1 ATOM 2798 C C . SER A 1 358 ? 94.250 94.379 1.876 1.00 63.12 ? 372 SER A C 1 ATOM 2799 O O . SER A 1 358 ? 94.061 94.270 3.090 1.00 62.23 ? 372 SER A O 1 ATOM 2800 C CB . SER A 1 358 ? 96.586 95.101 1.377 1.00 62.76 ? 372 SER A CB 1 ATOM 2801 O OG . SER A 1 358 ? 96.857 94.311 2.529 1.00 61.19 ? 372 SER A OG 1 ATOM 2802 N N . HIS A 1 359 ? 93.740 93.538 0.984 1.00 60.87 ? 373 HIS A N 1 ATOM 2803 C CA . HIS A 1 359 ? 92.934 92.390 1.374 1.00 62.63 ? 373 HIS A CA 1 ATOM 2804 C C . HIS A 1 359 ? 93.565 91.543 2.483 1.00 63.90 ? 373 HIS A C 1 ATOM 2805 O O . HIS A 1 359 ? 92.888 91.131 3.435 1.00 65.04 ? 373 HIS A O 1 ATOM 2806 C CB . HIS A 1 359 ? 92.683 91.495 0.165 1.00 63.55 ? 373 HIS A CB 1 ATOM 2807 C CG . HIS A 1 359 ? 92.014 90.205 0.518 1.00 65.00 ? 373 HIS A CG 1 ATOM 2808 N ND1 . HIS A 1 359 ? 92.716 89.075 0.876 1.00 66.32 ? 373 HIS A ND1 1 ATOM 2809 C CD2 . HIS A 1 359 ? 90.702 89.876 0.597 1.00 64.44 ? 373 HIS A CD2 1 ATOM 2810 C CE1 . HIS A 1 359 ? 91.865 88.101 1.153 1.00 66.68 ? 373 HIS A CE1 1 ATOM 2811 N NE2 . HIS A 1 359 ? 90.637 88.561 0.989 1.00 65.31 ? 373 HIS A NE2 1 ATOM 2812 N N . GLN A 1 360 ? 94.857 91.266 2.341 1.00 61.63 ? 374 GLN A N 1 ATOM 2813 C CA . GLN A 1 360 ? 95.565 90.390 3.272 1.00 61.21 ? 374 GLN A CA 1 ATOM 2814 C C . GLN A 1 360 ? 95.624 90.972 4.680 1.00 63.07 ? 374 GLN A C 1 ATOM 2815 O O . GLN A 1 360 ? 95.771 90.228 5.653 1.00 66.26 ? 374 GLN A O 1 ATOM 2816 C CB . GLN A 1 360 ? 96.988 90.112 2.770 1.00 59.16 ? 374 GLN A CB 1 ATOM 2817 N N . HIS A 1 361 ? 95.498 92.295 4.782 1.00 63.27 ? 375 HIS A N 1 ATOM 2818 C CA . HIS A 1 361 ? 95.655 92.995 6.058 1.00 67.09 ? 375 HIS A CA 1 ATOM 2819 C C . HIS A 1 361 ? 94.413 93.750 6.512 1.00 66.85 ? 375 HIS A C 1 ATOM 2820 O O . HIS A 1 361 ? 94.524 94.708 7.280 1.00 69.11 ? 375 HIS A O 1 ATOM 2821 C CB . HIS A 1 361 ? 96.812 93.996 5.980 1.00 67.72 ? 375 HIS A CB 1 ATOM 2822 C CG . HIS A 1 361 ? 98.137 93.367 5.693 1.00 70.81 ? 375 HIS A CG 1 ATOM 2823 N ND1 . HIS A 1 361 ? 99.206 94.079 5.193 1.00 70.14 ? 375 HIS A ND1 1 ATOM 2824 C CD2 . HIS A 1 361 ? 98.567 92.091 5.839 1.00 72.07 ? 375 HIS A CD2 1 ATOM 2825 C CE1 . HIS A 1 361 ? 100.238 93.268 5.043 1.00 72.10 ? 375 HIS A CE1 1 ATOM 2826 N NE2 . HIS A 1 361 ? 99.877 92.056 5.427 1.00 72.74 ? 375 HIS A NE2 1 ATOM 2827 N N . SER A 1 362 ? 93.238 93.338 6.052 1.00 64.40 ? 376 SER A N 1 ATOM 2828 C CA . SER A 1 362 ? 92.018 94.047 6.429 1.00 61.67 ? 376 SER A CA 1 ATOM 2829 C C . SER A 1 362 ? 90.825 93.116 6.568 1.00 59.24 ? 376 SER A C 1 ATOM 2830 O O . SER A 1 362 ? 89.679 93.569 6.560 1.00 59.71 ? 376 SER A O 1 ATOM 2831 C CB . SER A 1 362 ? 91.707 95.169 5.426 1.00 62.02 ? 376 SER A CB 1 ATOM 2832 O OG . SER A 1 362 ? 91.173 94.658 4.213 1.00 58.35 ? 376 SER A OG 1 ATOM 2833 N N . MET A 1 363 ? 91.094 91.820 6.704 1.00 57.65 ? 377 MET A N 1 ATOM 2834 C CA . MET A 1 363 ? 90.031 90.833 6.834 1.00 59.94 ? 377 MET A CA 1 ATOM 2835 C C . MET A 1 363 ? 89.306 91.026 8.163 1.00 61.07 ? 377 MET A C 1 ATOM 2836 O O . MET A 1 363 ? 89.930 91.024 9.233 1.00 58.93 ? 377 MET A O 1 ATOM 2837 C CB . MET A 1 363 ? 90.600 89.411 6.789 1.00 65.02 ? 377 MET A CB 1 ATOM 2838 C CG . MET A 1 363 ? 91.443 89.084 5.564 1.00 68.91 ? 377 MET A CG 1 ATOM 2839 S SD . MET A 1 363 ? 92.933 88.147 5.984 1.00 132.45 ? 377 MET A SD 1 ATOM 2840 C CE . MET A 1 363 ? 92.293 86.994 7.205 1.00 84.63 ? 377 MET A CE 1 ATOM 2841 N N . CYS A 1 364 ? 87.990 91.203 8.085 1.00 59.44 ? 378 CYS A N 1 ATOM 2842 C CA . CYS A 1 364 ? 87.135 91.179 9.261 1.00 58.29 ? 378 CYS A CA 1 ATOM 2843 C C . CYS A 1 364 ? 86.712 89.734 9.425 1.00 56.89 ? 378 CYS A C 1 ATOM 2844 O O . CYS A 1 364 ? 86.799 88.952 8.475 1.00 56.76 ? 378 CYS A O 1 ATOM 2845 C CB . CYS A 1 364 ? 85.900 92.045 9.028 1.00 58.06 ? 378 CYS A CB 1 ATOM 2846 S SG . CYS A 1 364 ? 86.247 93.755 8.570 1.00 65.07 ? 378 CYS A SG 1 ATOM 2847 N N . ILE A 1 365 ? 86.256 89.358 10.613 1.00 56.96 ? 379 ILE A N 1 ATOM 2848 C CA . ILE A 1 365 ? 85.859 87.971 10.820 1.00 53.58 ? 379 ILE A CA 1 ATOM 2849 C C . ILE A 1 365 ? 84.505 87.662 10.176 1.00 51.77 ? 379 ILE A C 1 ATOM 2850 O O . ILE A 1 365 ? 84.161 86.494 9.977 1.00 52.65 ? 379 ILE A O 1 ATOM 2851 C CB . ILE A 1 365 ? 85.845 87.588 12.315 1.00 54.93 ? 379 ILE A CB 1 ATOM 2852 C CG1 . ILE A 1 365 ? 84.769 88.366 13.062 1.00 53.19 ? 379 ILE A CG1 1 ATOM 2853 C CG2 . ILE A 1 365 ? 87.201 87.865 12.935 1.00 60.33 ? 379 ILE A CG2 1 ATOM 2854 C CD1 . ILE A 1 365 ? 84.285 87.658 14.301 1.00 56.27 ? 379 ILE A CD1 1 ATOM 2855 N N . ARG A 1 366 ? 83.751 88.705 9.828 1.00 51.45 ? 380 ARG A N 1 ATOM 2856 C CA . ARG A 1 366 ? 82.350 88.541 9.409 1.00 53.06 ? 380 ARG A CA 1 ATOM 2857 C C . ARG A 1 366 ? 81.860 89.739 8.580 1.00 53.04 ? 380 ARG A C 1 ATOM 2858 O O . ARG A 1 366 ? 81.674 90.830 9.116 1.00 54.72 ? 380 ARG A O 1 ATOM 2859 C CB . ARG A 1 366 ? 81.461 88.354 10.650 1.00 56.88 ? 380 ARG A CB 1 ATOM 2860 C CG . ARG A 1 366 ? 80.016 87.993 10.336 1.00 62.97 ? 380 ARG A CG 1 ATOM 2861 C CD . ARG A 1 366 ? 79.163 87.826 11.599 1.00 66.82 ? 380 ARG A CD 1 ATOM 2862 N NE . ARG A 1 366 ? 79.739 86.903 12.574 1.00 68.55 ? 380 ARG A NE 1 ATOM 2863 C CZ . ARG A 1 366 ? 80.226 87.276 13.756 1.00 73.00 ? 380 ARG A CZ 1 ATOM 2864 N NH1 . ARG A 1 366 ? 80.208 88.553 14.111 1.00 74.51 ? 380 ARG A NH1 1 ATOM 2865 N NH2 . ARG A 1 366 ? 80.729 86.377 14.593 1.00 74.46 ? 380 ARG A NH2 1 ATOM 2866 N N . PRO A 1 367 ? 81.679 89.556 7.262 1.00 50.83 ? 381 PRO A N 1 ATOM 2867 C CA . PRO A 1 367 ? 81.968 88.354 6.480 1.00 56.34 ? 381 PRO A CA 1 ATOM 2868 C C . PRO A 1 367 ? 83.404 88.404 5.943 1.00 62.52 ? 381 PRO A C 1 ATOM 2869 O O . PRO A 1 367 ? 84.038 89.463 5.983 1.00 62.89 ? 381 PRO A O 1 ATOM 2870 C CB . PRO A 1 367 ? 80.980 88.468 5.309 1.00 55.78 ? 381 PRO A CB 1 ATOM 2871 C CG . PRO A 1 367 ? 80.894 89.954 5.058 1.00 56.46 ? 381 PRO A CG 1 ATOM 2872 C CD . PRO A 1 367 ? 81.092 90.624 6.430 1.00 54.46 ? 381 PRO A CD 1 ATOM 2873 N N . TYR A 1 368 ? 83.906 87.273 5.454 1.00 66.94 ? 382 TYR A N 1 ATOM 2874 C CA . TYR A 1 368 ? 85.235 87.218 4.853 1.00 70.50 ? 382 TYR A CA 1 ATOM 2875 C C . TYR A 1 368 ? 85.127 87.590 3.375 1.00 69.17 ? 382 TYR A C 1 ATOM 2876 O O . TYR A 1 368 ? 84.313 87.018 2.656 1.00 68.96 ? 382 TYR A O 1 ATOM 2877 C CB . TYR A 1 368 ? 85.833 85.815 5.019 1.00 73.07 ? 382 TYR A CB 1 ATOM 2878 C CG . TYR A 1 368 ? 87.220 85.643 4.427 1.00 75.65 ? 382 TYR A CG 1 ATOM 2879 C CD1 . TYR A 1 368 ? 88.358 85.893 5.187 1.00 75.35 ? 382 TYR A CD1 1 ATOM 2880 C CD2 . TYR A 1 368 ? 87.388 85.219 3.113 1.00 75.38 ? 382 TYR A CD2 1 ATOM 2881 C CE1 . TYR A 1 368 ? 89.625 85.733 4.653 1.00 76.15 ? 382 TYR A CE1 1 ATOM 2882 C CE2 . TYR A 1 368 ? 88.650 85.057 2.569 1.00 76.49 ? 382 TYR A CE2 1 ATOM 2883 C CZ . TYR A 1 368 ? 89.765 85.315 3.342 1.00 76.93 ? 382 TYR A CZ 1 ATOM 2884 O OH . TYR A 1 368 ? 91.022 85.155 2.796 1.00 77.01 ? 382 TYR A OH 1 ATOM 2885 N N . LEU A 1 369 ? 85.936 88.551 2.928 1.00 68.71 ? 383 LEU A N 1 ATOM 2886 C CA . LEU A 1 369 ? 85.861 89.042 1.546 1.00 69.69 ? 383 LEU A CA 1 ATOM 2887 C C . LEU A 1 369 ? 86.753 88.263 0.593 1.00 68.77 ? 383 LEU A C 1 ATOM 2888 O O . LEU A 1 369 ? 87.915 87.985 0.913 1.00 65.35 ? 383 LEU A O 1 ATOM 2889 C CB . LEU A 1 369 ? 86.256 90.519 1.456 1.00 72.95 ? 383 LEU A CB 1 ATOM 2890 C CG . LEU A 1 369 ? 85.418 91.569 2.175 1.00 74.29 ? 383 LEU A CG 1 ATOM 2891 C CD1 . LEU A 1 369 ? 85.659 92.956 1.570 1.00 73.24 ? 383 LEU A CD1 1 ATOM 2892 C CD2 . LEU A 1 369 ? 83.941 91.190 2.146 1.00 73.98 ? 383 LEU A CD2 1 ATOM 2893 N N . PRO A 1 370 ? 86.218 87.927 -0.595 1.00 69.78 ? 384 PRO A N 1 ATOM 2894 C CA . PRO A 1 370 ? 87.048 87.346 -1.657 1.00 68.16 ? 384 PRO A CA 1 ATOM 2895 C C . PRO A 1 370 ? 88.111 88.358 -2.034 1.00 65.96 ? 384 PRO A C 1 ATOM 2896 O O . PRO A 1 370 ? 87.896 89.565 -1.853 1.00 62.59 ? 384 PRO A O 1 ATOM 2897 C CB . PRO A 1 370 ? 86.070 87.166 -2.823 1.00 69.75 ? 384 PRO A CB 1 ATOM 2898 C CG . PRO A 1 370 ? 84.699 87.203 -2.203 1.00 69.70 ? 384 PRO A CG 1 ATOM 2899 C CD . PRO A 1 370 ? 84.823 88.126 -1.024 1.00 69.86 ? 384 PRO A CD 1 ATOM 2900 N N . TYR A 1 371 ? 89.237 87.878 -2.546 1.00 67.89 ? 385 TYR A N 1 ATOM 2901 C CA . TYR A 1 371 ? 90.357 88.752 -2.864 1.00 68.81 ? 385 TYR A CA 1 ATOM 2902 C C . TYR A 1 371 ? 89.978 89.973 -3.705 1.00 66.89 ? 385 TYR A C 1 ATOM 2903 O O . TYR A 1 371 ? 89.100 89.903 -4.573 1.00 64.16 ? 385 TYR A O 1 ATOM 2904 C CB . TYR A 1 371 ? 91.483 87.968 -3.549 1.00 71.02 ? 385 TYR A CB 1 ATOM 2905 C CG . TYR A 1 371 ? 92.633 88.850 -3.968 1.00 72.62 ? 385 TYR A CG 1 ATOM 2906 C CD1 . TYR A 1 371 ? 93.530 89.341 -3.028 1.00 75.06 ? 385 TYR A CD1 1 ATOM 2907 C CD2 . TYR A 1 371 ? 92.810 89.214 -5.297 1.00 71.85 ? 385 TYR A CD2 1 ATOM 2908 C CE1 . TYR A 1 371 ? 94.582 90.162 -3.409 1.00 77.60 ? 385 TYR A CE1 1 ATOM 2909 C CE2 . TYR A 1 371 ? 93.852 90.032 -5.682 1.00 73.95 ? 385 TYR A CE2 1 ATOM 2910 C CZ . TYR A 1 371 ? 94.735 90.503 -4.737 1.00 77.09 ? 385 TYR A CZ 1 ATOM 2911 O OH . TYR A 1 371 ? 95.772 91.319 -5.126 1.00 80.77 ? 385 TYR A OH 1 ATOM 2912 N N . TYR A 1 372 ? 90.635 91.092 -3.405 1.00 68.39 ? 386 TYR A N 1 ATOM 2913 C CA . TYR A 1 372 ? 90.625 92.280 -4.254 1.00 68.68 ? 386 TYR A CA 1 ATOM 2914 C C . TYR A 1 372 ? 92.020 92.902 -4.238 1.00 70.60 ? 386 TYR A C 1 ATOM 2915 O O . TYR A 1 372 ? 92.756 92.762 -3.261 1.00 69.30 ? 386 TYR A O 1 ATOM 2916 C CB . TYR A 1 372 ? 89.583 93.293 -3.782 1.00 69.34 ? 386 TYR A CB 1 ATOM 2917 C CG . TYR A 1 372 ? 89.867 93.867 -2.413 1.00 69.46 ? 386 TYR A CG 1 ATOM 2918 C CD1 . TYR A 1 372 ? 89.507 93.172 -1.264 1.00 69.39 ? 386 TYR A CD1 1 ATOM 2919 C CD2 . TYR A 1 372 ? 90.485 95.108 -2.265 1.00 69.78 ? 386 TYR A CD2 1 ATOM 2920 C CE1 . TYR A 1 372 ? 89.765 93.686 -0.012 1.00 68.10 ? 386 TYR A CE1 1 ATOM 2921 C CE2 . TYR A 1 372 ? 90.742 95.632 -1.008 1.00 68.30 ? 386 TYR A CE2 1 ATOM 2922 C CZ . TYR A 1 372 ? 90.377 94.912 0.106 1.00 67.52 ? 386 TYR A CZ 1 ATOM 2923 O OH . TYR A 1 372 ? 90.620 95.414 1.354 1.00 68.16 ? 386 TYR A OH 1 ATOM 2924 N N . ASN A 1 373 ? 92.372 93.589 -5.320 1.00 73.81 ? 387 ASN A N 1 ATOM 2925 C CA . ASN A 1 373 ? 93.727 94.080 -5.531 1.00 77.38 ? 387 ASN A CA 1 ATOM 2926 C C . ASN A 1 373 ? 93.870 95.508 -5.013 1.00 70.45 ? 387 ASN A C 1 ATOM 2927 O O . ASN A 1 373 ? 92.945 96.316 -5.150 1.00 66.62 ? 387 ASN A O 1 ATOM 2928 C CB . ASN A 1 373 ? 94.054 94.023 -7.033 1.00 90.20 ? 387 ASN A CB 1 ATOM 2929 C CG . ASN A 1 373 ? 95.532 93.776 -7.316 1.00 105.17 ? 387 ASN A CG 1 ATOM 2930 O OD1 . ASN A 1 373 ? 96.405 94.308 -6.631 1.00 104.55 ? 387 ASN A OD1 1 ATOM 2931 N ND2 . ASN A 1 373 ? 95.813 92.960 -8.339 1.00 121.60 ? 387 ASN A ND2 1 ATOM 2932 N N . VAL A 1 374 ? 95.011 95.812 -4.392 1.00 69.75 ? 388 VAL A N 1 ATOM 2933 C CA . VAL A 1 374 ? 95.385 97.198 -4.099 1.00 72.17 ? 388 VAL A CA 1 ATOM 2934 C C . VAL A 1 374 ? 96.849 97.421 -4.473 1.00 76.22 ? 388 VAL A C 1 ATOM 2935 O O . VAL A 1 374 ? 97.738 96.705 -4.009 1.00 79.32 ? 388 VAL A O 1 ATOM 2936 C CB . VAL A 1 374 ? 95.196 97.577 -2.616 1.00 70.49 ? 388 VAL A CB 1 ATOM 2937 C CG1 . VAL A 1 374 ? 95.672 99.013 -2.377 1.00 68.66 ? 388 VAL A CG1 1 ATOM 2938 C CG2 . VAL A 1 374 ? 93.733 97.407 -2.182 1.00 69.71 ? 388 VAL A CG2 1 ATOM 2939 N N . SER A 1 375 ? 97.110 98.416 -5.306 1.00 76.40 ? 389 SER A N 1 ATOM 2940 C CA . SER A 1 375 ? 98.477 98.655 -5.742 1.00 77.02 ? 389 SER A CA 1 ATOM 2941 C C . SER A 1 375 ? 98.805 100.140 -5.740 1.00 78.20 ? 389 SER A C 1 ATOM 2942 O O . SER A 1 375 ? 97.922 100.978 -5.540 1.00 74.18 ? 389 SER A O 1 ATOM 2943 C CB . SER A 1 375 ? 98.712 98.040 -7.124 1.00 76.50 ? 389 SER A CB 1 ATOM 2944 O OG . SER A 1 375 ? 97.748 98.490 -8.059 1.00 77.48 ? 389 SER A OG 1 ATOM 2945 N N . HIS A 1 376 ? 100.077 100.464 -5.951 1.00 83.20 ? 390 HIS A N 1 ATOM 2946 C CA . HIS A 1 376 ? 100.506 101.853 -5.925 1.00 89.36 ? 390 HIS A CA 1 ATOM 2947 C C . HIS A 1 376 ? 99.720 102.663 -6.940 1.00 84.80 ? 390 HIS A C 1 ATOM 2948 O O . HIS A 1 376 ? 99.479 102.211 -8.062 1.00 83.76 ? 390 HIS A O 1 ATOM 2949 C CB . HIS A 1 376 ? 102.007 101.950 -6.182 1.00 100.81 ? 390 HIS A CB 1 ATOM 2950 C CG . HIS A 1 376 ? 102.819 101.088 -5.270 1.00 111.53 ? 390 HIS A CG 1 ATOM 2951 N ND1 . HIS A 1 376 ? 103.124 101.454 -3.976 1.00 116.39 ? 390 HIS A ND1 1 ATOM 2952 C CD2 . HIS A 1 376 ? 103.367 99.863 -5.454 1.00 115.69 ? 390 HIS A CD2 1 ATOM 2953 C CE1 . HIS A 1 376 ? 103.836 100.498 -3.406 1.00 118.22 ? 390 HIS A CE1 1 ATOM 2954 N NE2 . HIS A 1 376 ? 103.998 99.522 -4.281 1.00 118.16 ? 390 HIS A NE2 1 ATOM 2955 N N . GLN A 1 377 ? 99.282 103.845 -6.526 1.00 81.04 ? 391 GLN A N 1 ATOM 2956 C CA . GLN A 1 377 ? 98.543 104.720 -7.418 1.00 79.70 ? 391 GLN A CA 1 ATOM 2957 C C . GLN A 1 377 ? 98.697 106.176 -7.026 1.00 78.41 ? 391 GLN A C 1 ATOM 2958 O O . GLN A 1 377 ? 99.280 106.510 -5.995 1.00 77.29 ? 391 GLN A O 1 ATOM 2959 C CB . GLN A 1 377 ? 97.059 104.338 -7.470 1.00 81.07 ? 391 GLN A CB 1 ATOM 2960 C CG . GLN A 1 377 ? 96.376 104.238 -6.107 1.00 80.24 ? 391 GLN A CG 1 ATOM 2961 C CD . GLN A 1 377 ? 94.890 103.919 -6.221 1.00 80.49 ? 391 GLN A CD 1 ATOM 2962 O OE1 . GLN A 1 377 ? 94.206 104.387 -7.137 1.00 80.45 ? 391 GLN A OE1 1 ATOM 2963 N NE2 . GLN A 1 377 ? 94.385 103.115 -5.289 1.00 78.64 ? 391 GLN A NE2 1 ATOM 2964 N N . LEU A 1 378 ? 98.171 107.037 -7.880 1.00 78.82 ? 392 LEU A N 1 ATOM 2965 C CA . LEU A 1 378 ? 98.177 108.464 -7.649 1.00 79.36 ? 392 LEU A CA 1 ATOM 2966 C C . LEU A 1 378 ? 96.736 108.920 -7.725 1.00 77.61 ? 392 LEU A C 1 ATOM 2967 O O . LEU A 1 378 ? 95.941 108.356 -8.485 1.00 77.25 ? 392 LEU A O 1 ATOM 2968 C CB . LEU A 1 378 ? 99.011 109.160 -8.721 1.00 82.03 ? 392 LEU A CB 1 ATOM 2969 C CG . LEU A 1 378 ? 100.509 108.839 -8.669 1.00 84.07 ? 392 LEU A CG 1 ATOM 2970 C CD1 . LEU A 1 378 ? 101.114 108.681 -10.066 1.00 84.93 ? 392 LEU A CD1 1 ATOM 2971 C CD2 . LEU A 1 378 ? 101.241 109.916 -7.884 1.00 84.58 ? 392 LEU A CD2 1 ATOM 2972 N N . ALA A 1 379 ? 96.388 109.930 -6.937 1.00 77.47 ? 393 ALA A N 1 ATOM 2973 C CA . ALA A 1 379 ? 95.016 110.422 -6.916 1.00 77.28 ? 393 ALA A CA 1 ATOM 2974 C C . ALA A 1 379 ? 94.975 111.938 -6.997 1.00 76.74 ? 393 ALA A C 1 ATOM 2975 O O . ALA A 1 379 ? 95.678 112.623 -6.258 1.00 77.32 ? 393 ALA A O 1 ATOM 2976 C CB . ALA A 1 379 ? 94.293 109.938 -5.668 1.00 74.14 ? 393 ALA A CB 1 ATOM 2977 N N . THR A 1 380 ? 94.141 112.456 -7.892 1.00 77.36 ? 394 THR A N 1 ATOM 2978 C CA . THR A 1 380 ? 93.991 113.895 -8.050 1.00 79.07 ? 394 THR A CA 1 ATOM 2979 C C . THR A 1 380 ? 92.603 114.323 -7.595 1.00 77.56 ? 394 THR A C 1 ATOM 2980 O O . THR A 1 380 ? 91.596 113.761 -8.034 1.00 79.58 ? 394 THR A O 1 ATOM 2981 C CB . THR A 1 380 ? 94.218 114.328 -9.514 1.00 81.12 ? 394 THR A CB 1 ATOM 2982 O OG1 . THR A 1 380 ? 95.502 113.867 -9.959 1.00 80.56 ? 394 THR A OG1 1 ATOM 2983 C CG2 . THR A 1 380 ? 94.156 115.849 -9.638 1.00 81.65 ? 394 THR A CG2 1 ATOM 2984 N N . PHE A 1 381 ? 92.545 115.309 -6.710 1.00 75.52 ? 395 PHE A N 1 ATOM 2985 C CA . PHE A 1 381 ? 91.260 115.814 -6.242 1.00 76.48 ? 395 PHE A CA 1 ATOM 2986 C C . PHE A 1 381 ? 91.089 117.268 -6.646 1.00 76.40 ? 395 PHE A C 1 ATOM 2987 O O . PHE A 1 381 ? 92.051 118.043 -6.624 1.00 76.11 ? 395 PHE A O 1 ATOM 2988 C CB . PHE A 1 381 ? 91.132 115.655 -4.723 1.00 76.58 ? 395 PHE A CB 1 ATOM 2989 C CG . PHE A 1 381 ? 91.110 114.220 -4.265 1.00 75.82 ? 395 PHE A CG 1 ATOM 2990 C CD1 . PHE A 1 381 ? 92.298 113.525 -4.060 1.00 75.85 ? 395 PHE A CD1 1 ATOM 2991 C CD2 . PHE A 1 381 ? 89.902 113.566 -4.040 1.00 73.31 ? 395 PHE A CD2 1 ATOM 2992 C CE1 . PHE A 1 381 ? 92.285 112.203 -3.642 1.00 74.02 ? 395 PHE A CE1 1 ATOM 2993 C CE2 . PHE A 1 381 ? 89.879 112.241 -3.621 1.00 72.26 ? 395 PHE A CE2 1 ATOM 2994 C CZ . PHE A 1 381 ? 91.076 111.560 -3.421 1.00 72.06 ? 395 PHE A CZ 1 ATOM 2995 N N . THR A 1 382 ? 89.868 117.629 -7.029 1.00 77.70 ? 396 THR A N 1 ATOM 2996 C CA . THR A 1 382 ? 89.573 118.998 -7.441 1.00 81.77 ? 396 THR A CA 1 ATOM 2997 C C . THR A 1 382 ? 88.364 119.511 -6.687 1.00 82.85 ? 396 THR A C 1 ATOM 2998 O O . THR A 1 382 ? 87.282 118.924 -6.764 1.00 83.41 ? 396 THR A O 1 ATOM 2999 C CB . THR A 1 382 ? 89.314 119.106 -8.968 1.00 83.01 ? 396 THR A CB 1 ATOM 3000 O OG1 . THR A 1 382 ? 90.552 118.974 -9.680 1.00 83.00 ? 396 THR A OG1 1 ATOM 3001 C CG2 . THR A 1 382 ? 88.684 120.451 -9.314 1.00 83.85 ? 396 THR A CG2 1 ATOM 3002 N N . LEU A 1 383 ? 88.554 120.598 -5.944 1.00 83.77 ? 397 LEU A N 1 ATOM 3003 C CA . LEU A 1 383 ? 87.449 121.223 -5.228 1.00 83.87 ? 397 LEU A CA 1 ATOM 3004 C C . LEU A 1 383 ? 86.585 122.018 -6.203 1.00 87.01 ? 397 LEU A C 1 ATOM 3005 O O . LEU A 1 383 ? 86.896 123.170 -6.531 1.00 89.44 ? 397 LEU A O 1 ATOM 3006 C CB . LEU A 1 383 ? 87.961 122.130 -4.103 1.00 82.01 ? 397 LEU A CB 1 ATOM 3007 C CG . LEU A 1 383 ? 88.758 121.485 -2.967 1.00 80.86 ? 397 LEU A CG 1 ATOM 3008 C CD1 . LEU A 1 383 ? 88.843 122.410 -1.754 1.00 79.84 ? 397 LEU A CD1 1 ATOM 3009 C CD2 . LEU A 1 383 ? 88.139 120.152 -2.586 1.00 81.02 ? 397 LEU A CD2 1 ATOM 3010 N N . LYS A 1 384 ? 85.517 121.391 -6.687 1.00 85.82 ? 398 LYS A N 1 ATOM 3011 C CA . LYS A 1 384 ? 84.540 122.094 -7.504 1.00 87.65 ? 398 LYS A CA 1 ATOM 3012 C C . LYS A 1 384 ? 83.525 122.733 -6.560 1.00 89.75 ? 398 LYS A C 1 ATOM 3013 O O . LYS A 1 384 ? 83.661 122.625 -5.338 1.00 90.73 ? 398 LYS A O 1 ATOM 3014 C CB . LYS A 1 384 ? 83.863 121.142 -8.494 1.00 86.78 ? 398 LYS A CB 1 ATOM 3015 N N . GLY A 1 385 ? 82.524 123.405 -7.122 1.00 91.31 ? 399 GLY A N 1 ATOM 3016 C CA . GLY A 1 385 ? 81.506 124.072 -6.326 1.00 92.96 ? 399 GLY A CA 1 ATOM 3017 C C . GLY A 1 385 ? 82.054 125.012 -5.270 1.00 95.12 ? 399 GLY A C 1 ATOM 3018 O O . GLY A 1 385 ? 83.130 125.591 -5.427 1.00 95.80 ? 399 GLY A O 1 ATOM 3019 N N . SER A 1 386 ? 81.319 125.140 -4.172 1.00 95.93 ? 400 SER A N 1 ATOM 3020 C CA . SER A 1 386 ? 81.672 126.078 -3.109 1.00 97.67 ? 400 SER A CA 1 ATOM 3021 C C . SER A 1 386 ? 82.819 125.580 -2.229 1.00 94.39 ? 400 SER A C 1 ATOM 3022 O O . SER A 1 386 ? 83.012 126.068 -1.114 1.00 95.76 ? 400 SER A O 1 ATOM 3023 C CB . SER A 1 386 ? 80.442 126.386 -2.247 1.00 99.38 ? 400 SER A CB 1 ATOM 3024 O OG . SER A 1 386 ? 79.383 126.905 -3.037 1.00 101.65 ? 400 SER A OG 1 ATOM 3025 N N . LEU A 1 387 ? 83.573 124.607 -2.729 1.00 89.89 ? 401 LEU A N 1 ATOM 3026 C CA . LEU A 1 387 ? 84.728 124.099 -2.006 1.00 87.68 ? 401 LEU A CA 1 ATOM 3027 C C . LEU A 1 387 ? 85.985 124.790 -2.522 1.00 89.91 ? 401 LEU A C 1 ATOM 3028 O O . LEU A 1 387 ? 86.936 124.991 -1.770 1.00 89.28 ? 401 LEU A O 1 ATOM 3029 C CB . LEU A 1 387 ? 84.841 122.572 -2.148 1.00 84.10 ? 401 LEU A CB 1 ATOM 3030 C CG . LEU A 1 387 ? 83.699 121.716 -1.562 1.00 81.46 ? 401 LEU A CG 1 ATOM 3031 C CD1 . LEU A 1 387 ? 83.936 120.197 -1.703 1.00 77.26 ? 401 LEU A CD1 1 ATOM 3032 C CD2 . LEU A 1 387 ? 83.445 122.083 -0.107 1.00 65.06 ? 401 LEU A CD2 1 ATOM 3033 N N . ARG A 1 388 ? 85.965 125.174 -3.801 1.00 93.44 ? 402 ARG A N 1 ATOM 3034 C CA . ARG A 1 388 ? 87.114 125.801 -4.476 1.00 95.25 ? 402 ARG A CA 1 ATOM 3035 C C . ARG A 1 388 ? 87.744 126.954 -3.695 1.00 96.24 ? 402 ARG A C 1 ATOM 3036 O O . ARG A 1 388 ? 88.948 127.198 -3.799 1.00 94.42 ? 402 ARG A O 1 ATOM 3037 C CB . ARG A 1 388 ? 86.717 126.289 -5.876 1.00 95.62 ? 402 ARG A CB 1 ATOM 3038 N N . GLU A 1 389 ? 86.925 127.644 -2.903 1.00 99.45 ? 403 GLU A N 1 ATOM 3039 C CA . GLU A 1 389 ? 87.365 128.817 -2.149 1.00 103.15 ? 403 GLU A CA 1 ATOM 3040 C C . GLU A 1 389 ? 88.246 128.481 -0.937 1.00 105.20 ? 403 GLU A C 1 ATOM 3041 O O . GLU A 1 389 ? 88.632 129.376 -0.177 1.00 106.39 ? 403 GLU A O 1 ATOM 3042 C CB . GLU A 1 389 ? 86.152 129.638 -1.702 1.00 102.93 ? 403 GLU A CB 1 ATOM 3043 N N . ILE A 1 390 ? 88.556 127.197 -0.764 1.00 105.09 ? 404 ILE A N 1 ATOM 3044 C CA . ILE A 1 390 ? 89.448 126.738 0.305 1.00 105.06 ? 404 ILE A CA 1 ATOM 3045 C C . ILE A 1 390 ? 90.890 126.716 -0.203 1.00 105.26 ? 404 ILE A C 1 ATOM 3046 O O . ILE A 1 390 ? 91.133 126.357 -1.352 1.00 106.74 ? 404 ILE A O 1 ATOM 3047 C CB . ILE A 1 390 ? 89.031 125.333 0.812 1.00 96.85 ? 404 ILE A CB 1 ATOM 3048 C CG1 . ILE A 1 390 ? 87.601 125.377 1.364 1.00 96.10 ? 404 ILE A CG1 1 ATOM 3049 C CG2 . ILE A 1 390 ? 90.011 124.808 1.865 1.00 95.49 ? 404 ILE A CG2 1 ATOM 3050 C CD1 . ILE A 1 390 ? 87.044 124.025 1.774 1.00 94.88 ? 404 ILE A CD1 1 ATOM 3051 N N . GLN A 1 391 ? 91.839 127.107 0.646 1.00 104.37 ? 405 GLN A N 1 ATOM 3052 C CA . GLN A 1 391 ? 93.235 127.256 0.230 1.00 103.40 ? 405 GLN A CA 1 ATOM 3053 C C . GLN A 1 391 ? 94.211 126.331 0.950 1.00 99.36 ? 405 GLN A C 1 ATOM 3054 O O . GLN A 1 391 ? 95.358 126.174 0.522 1.00 98.53 ? 405 GLN A O 1 ATOM 3055 C CB . GLN A 1 391 ? 93.695 128.696 0.458 1.00 105.10 ? 405 GLN A CB 1 ATOM 3056 C CG . GLN A 1 391 ? 93.498 129.618 -0.721 1.00 107.93 ? 405 GLN A CG 1 ATOM 3057 C CD . GLN A 1 391 ? 94.626 130.623 -0.844 1.00 111.01 ? 405 GLN A CD 1 ATOM 3058 O OE1 . GLN A 1 391 ? 95.087 131.181 0.155 1.00 111.69 ? 405 GLN A OE1 1 ATOM 3059 N NE2 . GLN A 1 391 ? 95.092 130.844 -2.069 1.00 112.55 ? 405 GLN A NE2 1 ATOM 3060 N N . GLU A 1 392 ? 93.758 125.727 2.043 1.00 95.40 ? 406 GLU A N 1 ATOM 3061 C CA . GLU A 1 392 ? 94.666 125.088 2.985 1.00 92.16 ? 406 GLU A CA 1 ATOM 3062 C C . GLU A 1 392 ? 94.028 123.869 3.676 1.00 90.65 ? 406 GLU A C 1 ATOM 3063 O O . GLU A 1 392 ? 92.840 123.880 4.026 1.00 89.87 ? 406 GLU A O 1 ATOM 3064 C CB . GLU A 1 392 ? 95.104 126.127 4.021 1.00 91.14 ? 406 GLU A CB 1 ATOM 3065 C CG . GLU A 1 392 ? 96.237 125.705 4.924 1.00 92.49 ? 406 GLU A CG 1 ATOM 3066 C CD . GLU A 1 392 ? 96.303 126.537 6.196 1.00 93.94 ? 406 GLU A CD 1 ATOM 3067 O OE1 . GLU A 1 392 ? 95.465 127.454 6.355 1.00 93.19 ? 406 GLU A OE1 1 ATOM 3068 O OE2 . GLU A 1 392 ? 97.185 126.269 7.043 1.00 94.64 ? 406 GLU A OE2 1 ATOM 3069 N N . LEU A 1 393 ? 94.834 122.827 3.871 1.00 86.33 ? 407 LEU A N 1 ATOM 3070 C CA . LEU A 1 393 ? 94.367 121.565 4.426 1.00 79.81 ? 407 LEU A CA 1 ATOM 3071 C C . LEU A 1 393 ? 95.388 121.012 5.399 1.00 75.33 ? 407 LEU A C 1 ATOM 3072 O O . LEU A 1 393 ? 96.574 120.914 5.067 1.00 73.09 ? 407 LEU A O 1 ATOM 3073 C CB . LEU A 1 393 ? 94.178 120.526 3.318 1.00 80.06 ? 407 LEU A CB 1 ATOM 3074 C CG . LEU A 1 393 ? 93.119 120.671 2.225 1.00 79.69 ? 407 LEU A CG 1 ATOM 3075 C CD1 . LEU A 1 393 ? 93.029 119.373 1.441 1.00 78.67 ? 407 LEU A CD1 1 ATOM 3076 C CD2 . LEU A 1 393 ? 91.754 121.049 2.784 1.00 80.23 ? 407 LEU A CD2 1 ATOM 3077 N N . GLN A 1 394 ? 94.928 120.633 6.590 1.00 71.73 ? 408 GLN A N 1 ATOM 3078 C CA . GLN A 1 394 ? 95.769 119.893 7.523 1.00 70.25 ? 408 GLN A CA 1 ATOM 3079 C C . GLN A 1 394 ? 95.858 118.433 7.094 1.00 69.33 ? 408 GLN A C 1 ATOM 3080 O O . GLN A 1 394 ? 94.903 117.884 6.539 1.00 68.36 ? 408 GLN A O 1 ATOM 3081 C CB . GLN A 1 394 ? 95.237 120.008 8.956 1.00 71.00 ? 408 GLN A CB 1 ATOM 3082 C CG . GLN A 1 394 ? 95.498 121.365 9.576 1.00 72.21 ? 408 GLN A CG 1 ATOM 3083 C CD . GLN A 1 394 ? 96.895 121.872 9.259 1.00 73.49 ? 408 GLN A CD 1 ATOM 3084 O OE1 . GLN A 1 394 ? 97.891 121.205 9.543 1.00 74.87 ? 408 GLN A OE1 1 ATOM 3085 N NE2 . GLN A 1 394 ? 96.972 123.046 8.651 1.00 72.90 ? 408 GLN A NE2 1 ATOM 3086 N N . VAL A 1 395 ? 97.004 117.808 7.353 1.00 70.68 ? 409 VAL A N 1 ATOM 3087 C CA . VAL A 1 395 ? 97.263 116.456 6.855 1.00 71.14 ? 409 VAL A CA 1 ATOM 3088 C C . VAL A 1 395 ? 97.637 115.476 7.970 1.00 69.61 ? 409 VAL A C 1 ATOM 3089 O O . VAL A 1 395 ? 98.626 115.673 8.677 1.00 65.91 ? 409 VAL A O 1 ATOM 3090 C CB . VAL A 1 395 ? 98.353 116.459 5.751 1.00 81.58 ? 409 VAL A CB 1 ATOM 3091 C CG1 . VAL A 1 395 ? 98.801 115.038 5.427 1.00 81.41 ? 409 VAL A CG1 1 ATOM 3092 C CG2 . VAL A 1 395 ? 97.837 117.162 4.499 1.00 81.47 ? 409 VAL A CG2 1 ATOM 3093 N N . TRP A 1 396 ? 96.829 114.427 8.124 1.00 69.93 ? 410 TRP A N 1 ATOM 3094 C CA . TRP A 1 396 ? 97.103 113.385 9.105 1.00 65.65 ? 410 TRP A CA 1 ATOM 3095 C C . TRP A 1 396 ? 97.341 112.043 8.426 1.00 65.16 ? 410 TRP A C 1 ATOM 3096 O O . TRP A 1 396 ? 96.599 111.649 7.520 1.00 62.29 ? 410 TRP A O 1 ATOM 3097 C CB . TRP A 1 396 ? 95.956 113.287 10.105 1.00 65.14 ? 410 TRP A CB 1 ATOM 3098 C CG . TRP A 1 396 ? 95.802 114.533 10.919 1.00 66.41 ? 410 TRP A CG 1 ATOM 3099 C CD1 . TRP A 1 396 ? 95.104 115.660 10.579 1.00 65.40 ? 410 TRP A CD1 1 ATOM 3100 C CD2 . TRP A 1 396 ? 96.363 114.783 12.217 1.00 67.21 ? 410 TRP A CD2 1 ATOM 3101 N NE1 . TRP A 1 396 ? 95.193 116.593 11.591 1.00 63.17 ? 410 TRP A NE1 1 ATOM 3102 C CE2 . TRP A 1 396 ? 95.962 116.080 12.604 1.00 63.16 ? 410 TRP A CE2 1 ATOM 3103 C CE3 . TRP A 1 396 ? 97.161 114.032 13.089 1.00 62.76 ? 410 TRP A CE3 1 ATOM 3104 C CZ2 . TRP A 1 396 ? 96.338 116.644 13.826 1.00 65.69 ? 410 TRP A CZ2 1 ATOM 3105 C CZ3 . TRP A 1 396 ? 97.533 114.593 14.302 1.00 67.53 ? 410 TRP A CZ3 1 ATOM 3106 C CH2 . TRP A 1 396 ? 97.118 115.886 14.661 1.00 66.15 ? 410 TRP A CH2 1 ATOM 3107 N N . TYR A 1 397 ? 98.373 111.334 8.868 1.00 65.76 ? 411 TYR A N 1 ATOM 3108 C CA . TYR A 1 397 ? 98.802 110.135 8.162 1.00 68.42 ? 411 TYR A CA 1 ATOM 3109 C C . TYR A 1 397 ? 98.967 108.938 9.080 1.00 62.18 ? 411 TYR A C 1 ATOM 3110 O O . TYR A 1 397 ? 99.484 109.060 10.193 1.00 62.31 ? 411 TYR A O 1 ATOM 3111 C CB . TYR A 1 397 ? 100.117 110.412 7.413 1.00 71.66 ? 411 TYR A CB 1 ATOM 3112 C CG . TYR A 1 397 ? 100.732 109.185 6.778 1.00 74.78 ? 411 TYR A CG 1 ATOM 3113 C CD1 . TYR A 1 397 ? 100.347 108.774 5.510 1.00 76.87 ? 411 TYR A CD1 1 ATOM 3114 C CD2 . TYR A 1 397 ? 101.693 108.432 7.447 1.00 74.95 ? 411 TYR A CD2 1 ATOM 3115 C CE1 . TYR A 1 397 ? 100.901 107.649 4.922 1.00 77.45 ? 411 TYR A CE1 1 ATOM 3116 C CE2 . TYR A 1 397 ? 102.251 107.305 6.868 1.00 75.99 ? 411 TYR A CE2 1 ATOM 3117 C CZ . TYR A 1 397 ? 101.852 106.920 5.603 1.00 76.82 ? 411 TYR A CZ 1 ATOM 3118 O OH . TYR A 1 397 ? 102.399 105.802 5.016 1.00 76.17 ? 411 TYR A OH 1 ATOM 3119 N N . THR A 1 398 ? 98.527 107.776 8.602 1.00 61.68 ? 412 THR A N 1 ATOM 3120 C CA . THR A 1 398 ? 98.709 106.526 9.334 1.00 61.28 ? 412 THR A CA 1 ATOM 3121 C C . THR A 1 398 ? 99.126 105.426 8.373 1.00 61.34 ? 412 THR A C 1 ATOM 3122 O O . THR A 1 398 ? 98.608 105.344 7.258 1.00 61.26 ? 412 THR A O 1 ATOM 3123 C CB . THR A 1 398 ? 97.421 106.099 10.107 1.00 61.31 ? 412 THR A CB 1 ATOM 3124 O OG1 . THR A 1 398 ? 97.091 107.094 11.090 1.00 60.42 ? 412 THR A OG1 1 ATOM 3125 C CG2 . THR A 1 398 ? 97.618 104.752 10.811 1.00 60.03 ? 412 THR A CG2 1 ATOM 3126 N N . LYS A 1 399 ? 100.064 104.589 8.808 1.00 68.37 ? 413 LYS A N 1 ATOM 3127 C CA . LYS A 1 399 ? 100.577 103.491 7.999 1.00 72.12 ? 413 LYS A CA 1 ATOM 3128 C C . LYS A 1 399 ? 100.547 102.215 8.825 1.00 72.79 ? 413 LYS A C 1 ATOM 3129 O O . LYS A 1 399 ? 101.258 102.107 9.823 1.00 76.91 ? 413 LYS A O 1 ATOM 3130 C CB . LYS A 1 399 ? 102.014 103.799 7.559 1.00 78.63 ? 413 LYS A CB 1 ATOM 3131 C CG . LYS A 1 399 ? 102.769 102.622 6.953 1.00 81.81 ? 413 LYS A CG 1 ATOM 3132 C CD . LYS A 1 399 ? 102.243 102.244 5.575 1.00 83.63 ? 413 LYS A CD 1 ATOM 3133 C CE . LYS A 1 399 ? 102.905 100.963 5.090 1.00 85.67 ? 413 LYS A CE 1 ATOM 3134 N NZ . LYS A 1 399 ? 102.352 100.484 3.795 1.00 86.48 ? 413 LYS A NZ 1 ATOM 3135 N N . LEU A 1 400 ? 99.729 101.251 8.411 1.00 68.61 ? 414 LEU A N 1 ATOM 3136 C CA . LEU A 1 400 ? 99.548 100.021 9.182 1.00 71.28 ? 414 LEU A CA 1 ATOM 3137 C C . LEU A 1 400 ? 100.468 98.893 8.703 1.00 72.20 ? 414 LEU A C 1 ATOM 3138 O O . LEU A 1 400 ? 100.818 98.832 7.531 1.00 67.60 ? 414 LEU A O 1 ATOM 3139 C CB . LEU A 1 400 ? 98.073 99.582 9.158 1.00 72.31 ? 414 LEU A CB 1 ATOM 3140 C CG . LEU A 1 400 ? 97.104 100.477 9.945 1.00 71.79 ? 414 LEU A CG 1 ATOM 3141 C CD1 . LEU A 1 400 ? 95.670 100.348 9.460 1.00 69.44 ? 414 LEU A CD1 1 ATOM 3142 C CD2 . LEU A 1 400 ? 97.190 100.169 11.434 1.00 72.89 ? 414 LEU A CD2 1 ATOM 3143 N N . GLY A 1 401 ? 100.852 98.004 9.619 1.00 78.69 ? 415 GLY A N 1 ATOM 3144 C CA . GLY A 1 401 ? 101.770 96.921 9.303 1.00 83.59 ? 415 GLY A CA 1 ATOM 3145 C C . GLY A 1 401 ? 103.146 97.091 9.927 1.00 87.07 ? 415 GLY A C 1 ATOM 3146 O O . GLY A 1 401 ? 103.710 96.151 10.494 1.00 88.59 ? 415 GLY A O 1 ATOM 3147 N N . ARG A 1 406 ? 105.450 100.353 11.514 1.00 95.70 ? 420 ARG A N 1 ATOM 3148 C CA . ARG A 1 406 ? 104.188 101.091 11.509 1.00 96.07 ? 420 ARG A CA 1 ATOM 3149 C C . ARG A 1 406 ? 104.299 102.510 12.102 1.00 98.27 ? 420 ARG A C 1 ATOM 3150 O O . ARG A 1 406 ? 105.104 102.762 13.006 1.00 101.15 ? 420 ARG A O 1 ATOM 3151 C CB . ARG A 1 406 ? 103.102 100.291 12.235 1.00 93.77 ? 420 ARG A CB 1 ATOM 3152 N N . LEU A 1 407 ? 103.488 103.427 11.568 1.00 95.85 ? 421 LEU A N 1 ATOM 3153 C CA . LEU A 1 407 ? 103.412 104.829 12.011 1.00 91.43 ? 421 LEU A CA 1 ATOM 3154 C C . LEU A 1 407 ? 101.947 105.169 12.272 1.00 87.90 ? 421 LEU A C 1 ATOM 3155 O O . LEU A 1 407 ? 101.092 104.881 11.433 1.00 86.49 ? 421 LEU A O 1 ATOM 3156 C CB . LEU A 1 407 ? 103.915 105.771 10.916 1.00 89.35 ? 421 LEU A CB 1 ATOM 3157 C CG . LEU A 1 407 ? 105.386 105.945 10.533 1.00 89.72 ? 421 LEU A CG 1 ATOM 3158 C CD1 . LEU A 1 407 ? 106.080 104.637 10.202 1.00 90.22 ? 421 LEU A CD1 1 ATOM 3159 C CD2 . LEU A 1 407 ? 105.463 106.889 9.346 1.00 89.13 ? 421 LEU A CD2 1 ATOM 3160 N N . HIS A 1 408 ? 101.644 105.796 13.406 1.00 84.82 ? 422 HIS A N 1 ATOM 3161 C CA . HIS A 1 408 ? 100.242 105.999 13.780 1.00 78.91 ? 422 HIS A CA 1 ATOM 3162 C C . HIS A 1 408 ? 99.841 107.466 14.000 1.00 74.43 ? 422 HIS A C 1 ATOM 3163 O O . HIS A 1 408 ? 100.457 108.170 14.801 1.00 76.46 ? 422 HIS A O 1 ATOM 3164 C CB . HIS A 1 408 ? 99.901 105.164 15.018 1.00 78.07 ? 422 HIS A CB 1 ATOM 3165 C CG . HIS A 1 408 ? 100.062 103.685 14.818 1.00 76.80 ? 422 HIS A CG 1 ATOM 3166 N ND1 . HIS A 1 408 ? 100.116 103.105 13.569 1.00 77.43 ? 422 HIS A ND1 1 ATOM 3167 C CD2 . HIS A 1 408 ? 100.179 102.675 15.709 1.00 73.46 ? 422 HIS A CD2 1 ATOM 3168 C CE1 . HIS A 1 408 ? 100.254 101.795 13.701 1.00 75.30 ? 422 HIS A CE1 1 ATOM 3169 N NE2 . HIS A 1 408 ? 100.297 101.509 14.988 1.00 72.91 ? 422 HIS A NE2 1 ATOM 3170 N N . PHE A 1 409 ? 98.802 107.900 13.282 1.00 69.11 ? 423 PHE A N 1 ATOM 3171 C CA . PHE A 1 409 ? 98.181 109.221 13.443 1.00 68.34 ? 423 PHE A CA 1 ATOM 3172 C C . PHE A 1 409 ? 99.193 110.380 13.523 1.00 69.37 ? 423 PHE A C 1 ATOM 3173 O O . PHE A 1 409 ? 99.120 111.226 14.417 1.00 65.28 ? 423 PHE A O 1 ATOM 3174 C CB . PHE A 1 409 ? 97.223 109.214 14.649 1.00 68.31 ? 423 PHE A CB 1 ATOM 3175 C CG . PHE A 1 409 ? 96.141 110.259 14.579 1.00 60.69 ? 423 PHE A CG 1 ATOM 3176 C CD1 . PHE A 1 409 ? 95.221 110.262 13.535 1.00 66.06 ? 423 PHE A CD1 1 ATOM 3177 C CD2 . PHE A 1 409 ? 96.030 111.225 15.569 1.00 60.95 ? 423 PHE A CD2 1 ATOM 3178 C CE1 . PHE A 1 409 ? 94.219 111.224 13.472 1.00 60.28 ? 423 PHE A CE1 1 ATOM 3179 C CE2 . PHE A 1 409 ? 95.032 112.191 15.516 1.00 63.78 ? 423 PHE A CE2 1 ATOM 3180 C CZ . PHE A 1 409 ? 94.123 112.188 14.468 1.00 60.54 ? 423 PHE A CZ 1 ATOM 3181 N N . LYS A 1 410 ? 100.126 110.414 12.572 1.00 74.18 ? 424 LYS A N 1 ATOM 3182 C CA . LYS A 1 410 ? 101.176 111.435 12.550 1.00 74.82 ? 424 LYS A CA 1 ATOM 3183 C C . LYS A 1 410 ? 100.756 112.621 11.683 1.00 72.35 ? 424 LYS A C 1 ATOM 3184 O O . LYS A 1 410 ? 100.291 112.436 10.554 1.00 70.61 ? 424 LYS A O 1 ATOM 3185 C CB . LYS A 1 410 ? 102.500 110.835 12.044 1.00 77.79 ? 424 LYS A CB 1 ATOM 3186 C CG . LYS A 1 410 ? 102.783 109.421 12.575 1.00 80.74 ? 424 LYS A CG 1 ATOM 3187 C CD . LYS A 1 410 ? 104.245 109.228 12.996 1.00 82.10 ? 424 LYS A CD 1 ATOM 3188 C CE . LYS A 1 410 ? 104.436 107.951 13.828 1.00 81.74 ? 424 LYS A CE 1 ATOM 3189 N NZ . LYS A 1 410 ? 103.786 108.014 15.175 1.00 80.47 ? 424 LYS A NZ 1 ATOM 3190 N N . GLN A 1 411 ? 100.901 113.836 12.208 1.00 70.12 ? 425 GLN A N 1 ATOM 3191 C CA . GLN A 1 411 ? 100.541 115.016 11.435 1.00 70.98 ? 425 GLN A CA 1 ATOM 3192 C C . GLN A 1 411 ? 101.680 115.355 10.483 1.00 71.19 ? 425 GLN A C 1 ATOM 3193 O O . GLN A 1 411 ? 102.837 115.448 10.892 1.00 73.05 ? 425 GLN A O 1 ATOM 3194 C CB . GLN A 1 411 ? 100.214 116.212 12.338 1.00 73.37 ? 425 GLN A CB 1 ATOM 3195 C CG . GLN A 1 411 ? 99.560 117.387 11.596 1.00 75.82 ? 425 GLN A CG 1 ATOM 3196 C CD . GLN A 1 411 ? 99.121 118.509 12.524 1.00 78.16 ? 425 GLN A CD 1 ATOM 3197 O OE1 . GLN A 1 411 ? 99.655 118.664 13.620 1.00 80.29 ? 425 GLN A OE1 1 ATOM 3198 N NE2 . GLN A 1 411 ? 98.137 119.290 12.090 1.00 77.65 ? 425 GLN A NE2 1 ATOM 3199 N N . LEU A 1 412 ? 101.341 115.518 9.208 1.00 69.49 ? 426 LEU A N 1 ATOM 3200 C CA . LEU A 1 412 ? 102.323 115.832 8.181 1.00 73.52 ? 426 LEU A CA 1 ATOM 3201 C C . LEU A 1 412 ? 102.221 117.297 7.814 1.00 75.63 ? 426 LEU A C 1 ATOM 3202 O O . LEU A 1 412 ? 101.314 117.995 8.270 1.00 73.14 ? 426 LEU A O 1 ATOM 3203 C CB . LEU A 1 412 ? 102.091 114.974 6.936 1.00 74.61 ? 426 LEU A CB 1 ATOM 3204 C CG . LEU A 1 412 ? 102.254 113.464 7.088 1.00 74.92 ? 426 LEU A CG 1 ATOM 3205 C CD1 . LEU A 1 412 ? 102.119 112.791 5.738 1.00 72.14 ? 426 LEU A CD1 1 ATOM 3206 C CD2 . LEU A 1 412 ? 103.598 113.136 7.724 1.00 78.33 ? 426 LEU A CD2 1 ATOM 3207 N N . ASP A 1 413 ? 103.150 117.757 6.981 1.00 81.42 ? 427 ASP A N 1 ATOM 3208 C CA . ASP A 1 413 ? 103.191 119.157 6.597 1.00 84.90 ? 427 ASP A CA 1 ATOM 3209 C C . ASP A 1 413 ? 101.907 119.549 5.892 1.00 80.51 ? 427 ASP A C 1 ATOM 3210 O O . ASP A 1 413 ? 101.379 118.793 5.078 1.00 81.79 ? 427 ASP A O 1 ATOM 3211 C CB . ASP A 1 413 ? 104.405 119.437 5.709 1.00 92.78 ? 427 ASP A CB 1 ATOM 3212 C CG . ASP A 1 413 ? 105.715 119.050 6.379 1.00 98.56 ? 427 ASP A CG 1 ATOM 3213 O OD1 . ASP A 1 413 ? 106.123 119.744 7.339 1.00 99.88 ? 427 ASP A OD1 1 ATOM 3214 O OD2 . ASP A 1 413 ? 106.333 118.050 5.944 1.00 100.44 ? 427 ASP A OD2 1 ATOM 3215 N N . THR A 1 414 ? 101.400 120.725 6.242 1.00 76.74 ? 428 THR A N 1 ATOM 3216 C CA . THR A 1 414 ? 100.182 121.268 5.662 1.00 75.93 ? 428 THR A CA 1 ATOM 3217 C C . THR A 1 414 ? 100.214 121.232 4.136 1.00 79.32 ? 428 THR A C 1 ATOM 3218 O O . THR A 1 414 ? 101.269 121.419 3.525 1.00 79.30 ? 428 THR A O 1 ATOM 3219 C CB . THR A 1 414 ? 99.960 122.713 6.145 1.00 68.65 ? 428 THR A CB 1 ATOM 3220 O OG1 . THR A 1 414 ? 99.723 122.708 7.558 1.00 68.58 ? 428 THR A OG1 1 ATOM 3221 C CG2 . THR A 1 414 ? 98.769 123.343 5.461 1.00 85.57 ? 428 THR A CG2 1 ATOM 3222 N N . LEU A 1 415 ? 99.063 120.953 3.527 1.00 79.95 ? 429 LEU A N 1 ATOM 3223 C CA . LEU A 1 415 ? 98.927 121.075 2.085 1.00 82.08 ? 429 LEU A CA 1 ATOM 3224 C C . LEU A 1 415 ? 98.333 122.422 1.692 1.00 87.31 ? 429 LEU A C 1 ATOM 3225 O O . LEU A 1 415 ? 97.163 122.715 1.955 1.00 86.56 ? 429 LEU A O 1 ATOM 3226 C CB . LEU A 1 415 ? 98.114 119.919 1.501 1.00 79.45 ? 429 LEU A CB 1 ATOM 3227 C CG . LEU A 1 415 ? 99.003 118.879 0.820 1.00 76.68 ? 429 LEU A CG 1 ATOM 3228 C CD1 . LEU A 1 415 ? 98.189 117.768 0.170 1.00 75.36 ? 429 LEU A CD1 1 ATOM 3229 C CD2 . LEU A 1 415 ? 99.896 119.570 -0.200 1.00 72.37 ? 429 LEU A CD2 1 ATOM 3230 N N . TRP A 1 416 ? 99.170 123.248 1.075 1.00 93.23 ? 430 TRP A N 1 ATOM 3231 C CA . TRP A 1 416 ? 98.728 124.509 0.511 1.00 95.76 ? 430 TRP A CA 1 ATOM 3232 C C . TRP A 1 416 ? 98.334 124.279 -0.927 1.00 99.80 ? 430 TRP A C 1 ATOM 3233 O O . TRP A 1 416 ? 99.065 123.644 -1.690 1.00 100.29 ? 430 TRP A O 1 ATOM 3234 C CB . TRP A 1 416 ? 99.838 125.547 0.599 1.00 93.86 ? 430 TRP A CB 1 ATOM 3235 C CG . TRP A 1 416 ? 100.164 125.855 2.007 1.00 93.54 ? 430 TRP A CG 1 ATOM 3236 C CD1 . TRP A 1 416 ? 101.089 125.232 2.792 1.00 93.27 ? 430 TRP A CD1 1 ATOM 3237 C CD2 . TRP A 1 416 ? 99.539 126.847 2.827 1.00 94.69 ? 430 TRP A CD2 1 ATOM 3238 N NE1 . TRP A 1 416 ? 101.087 125.787 4.050 1.00 94.37 ? 430 TRP A NE1 1 ATOM 3239 C CE2 . TRP A 1 416 ? 100.145 126.782 4.097 1.00 95.38 ? 430 TRP A CE2 1 ATOM 3240 C CE3 . TRP A 1 416 ? 98.530 127.790 2.608 1.00 95.90 ? 430 TRP A CE3 1 ATOM 3241 C CZ2 . TRP A 1 416 ? 99.775 127.627 5.146 1.00 97.43 ? 430 TRP A CZ2 1 ATOM 3242 C CZ3 . TRP A 1 416 ? 98.165 128.629 3.646 1.00 97.65 ? 430 TRP A CZ3 1 ATOM 3243 C CH2 . TRP A 1 416 ? 98.785 128.541 4.900 1.00 98.42 ? 430 TRP A CH2 1 ATOM 3244 N N . LEU A 1 417 ? 97.161 124.775 -1.291 1.00 103.45 ? 431 LEU A N 1 ATOM 3245 C CA . LEU A 1 417 ? 96.698 124.638 -2.655 1.00 106.77 ? 431 LEU A CA 1 ATOM 3246 C C . LEU A 1 417 ? 97.525 125.563 -3.536 1.00 113.16 ? 431 LEU A C 1 ATOM 3247 O O . LEU A 1 417 ? 97.827 125.231 -4.686 1.00 115.27 ? 431 LEU A O 1 ATOM 3248 C CB . LEU A 1 417 ? 95.195 124.901 -2.729 1.00 103.82 ? 431 LEU A CB 1 ATOM 3249 C CG . LEU A 1 417 ? 94.527 123.821 -1.869 1.00 99.77 ? 431 LEU A CG 1 ATOM 3250 C CD1 . LEU A 1 417 ? 93.035 124.010 -1.731 1.00 99.32 ? 431 LEU A CD1 1 ATOM 3251 C CD2 . LEU A 1 417 ? 94.843 122.439 -2.426 1.00 96.53 ? 431 LEU A CD2 1 ATOM 3252 N N . LEU A 1 418 ? 97.902 126.714 -2.980 1.00 116.24 ? 432 LEU A N 1 ATOM 3253 C CA . LEU A 1 418 ? 98.907 127.604 -3.575 1.00 117.98 ? 432 LEU A CA 1 ATOM 3254 C C . LEU A 1 418 ? 98.606 128.073 -5.008 1.00 119.32 ? 432 LEU A C 1 ATOM 3255 O O . LEU A 1 418 ? 99.360 128.860 -5.587 1.00 119.52 ? 432 LEU A O 1 ATOM 3256 C CB . LEU A 1 418 ? 100.294 126.952 -3.510 1.00 117.63 ? 432 LEU A CB 1 ATOM 3257 N N . ASP A 1 419 ? 97.508 127.582 -5.570 1.00 119.44 ? 433 ASP A N 1 ATOM 3258 C CA . ASP A 1 419 ? 97.080 127.958 -6.907 1.00 120.32 ? 433 ASP A CA 1 ATOM 3259 C C . ASP A 1 419 ? 95.898 128.911 -6.791 1.00 117.86 ? 433 ASP A C 1 ATOM 3260 O O . ASP A 1 419 ? 95.739 129.616 -5.790 1.00 118.06 ? 433 ASP A O 1 ATOM 3261 C CB . ASP A 1 419 ? 96.636 126.710 -7.683 1.00 121.30 ? 433 ASP A CB 1 ATOM 3262 C CG . ASP A 1 419 ? 97.785 125.998 -8.378 1.00 122.67 ? 433 ASP A CG 1 ATOM 3263 O OD1 . ASP A 1 419 ? 98.952 126.211 -7.988 1.00 123.80 ? 433 ASP A OD1 1 ATOM 3264 O OD2 . ASP A 1 419 ? 97.511 125.214 -9.316 1.00 122.22 ? 433 ASP A OD2 1 ATOM 3265 N N . GLY A 1 420 ? 95.086 128.931 -7.843 1.00 114.56 ? 434 GLY A N 1 ATOM 3266 C CA . GLY A 1 420 ? 93.735 129.459 -7.791 1.00 110.36 ? 434 GLY A CA 1 ATOM 3267 C C . GLY A 1 420 ? 92.885 128.334 -8.345 1.00 104.40 ? 434 GLY A C 1 ATOM 3268 O O . GLY A 1 420 ? 91.683 128.479 -8.590 1.00 101.47 ? 434 GLY A O 1 ATOM 3269 N N . SER A 1 421 ? 93.554 127.198 -8.538 1.00 102.18 ? 435 SER A N 1 ATOM 3270 C CA . SER A 1 421 ? 92.986 125.999 -9.144 1.00 99.58 ? 435 SER A CA 1 ATOM 3271 C C . SER A 1 421 ? 91.905 125.377 -8.262 1.00 98.74 ? 435 SER A C 1 ATOM 3272 O O . SER A 1 421 ? 90.747 125.244 -8.670 1.00 97.90 ? 435 SER A O 1 ATOM 3273 C CB . SER A 1 421 ? 94.106 124.979 -9.405 1.00 96.85 ? 435 SER A CB 1 ATOM 3274 O OG . SER A 1 421 ? 93.636 123.827 -10.080 1.00 95.79 ? 435 SER A OG 1 ATOM 3275 N N . GLY A 1 422 ? 92.288 125.006 -7.046 1.00 98.45 ? 436 GLY A N 1 ATOM 3276 C CA . GLY A 1 422 ? 91.391 124.278 -6.168 1.00 96.14 ? 436 GLY A CA 1 ATOM 3277 C C . GLY A 1 422 ? 91.565 122.794 -6.417 1.00 93.92 ? 436 GLY A C 1 ATOM 3278 O O . GLY A 1 422 ? 90.615 122.009 -6.315 1.00 93.04 ? 436 GLY A O 1 ATOM 3279 N N . SER A 1 423 ? 92.796 122.415 -6.754 1.00 91.59 ? 437 SER A N 1 ATOM 3280 C CA . SER A 1 423 ? 93.122 121.026 -7.052 1.00 87.17 ? 437 SER A CA 1 ATOM 3281 C C . SER A 1 423 ? 94.453 120.599 -6.433 1.00 82.41 ? 437 SER A C 1 ATOM 3282 O O . SER A 1 423 ? 95.335 121.429 -6.200 1.00 79.31 ? 437 SER A O 1 ATOM 3283 C CB . SER A 1 423 ? 93.152 120.801 -8.565 1.00 87.48 ? 437 SER A CB 1 ATOM 3284 O OG . SER A 1 423 ? 93.715 119.539 -8.875 1.00 86.94 ? 437 SER A OG 1 ATOM 3285 N N . PHE A 1 424 ? 94.583 119.296 -6.175 1.00 80.82 ? 438 PHE A N 1 ATOM 3286 C CA . PHE A 1 424 ? 95.788 118.724 -5.572 1.00 79.94 ? 438 PHE A CA 1 ATOM 3287 C C . PHE A 1 424 ? 95.913 117.220 -5.850 1.00 77.44 ? 438 PHE A C 1 ATOM 3288 O O . PHE A 1 424 ? 94.935 116.557 -6.218 1.00 73.55 ? 438 PHE A O 1 ATOM 3289 C CB . PHE A 1 424 ? 95.821 118.989 -4.058 1.00 82.79 ? 438 PHE A CB 1 ATOM 3290 C CG . PHE A 1 424 ? 94.689 118.340 -3.293 1.00 83.28 ? 438 PHE A CG 1 ATOM 3291 C CD1 . PHE A 1 424 ? 93.438 118.945 -3.228 1.00 84.13 ? 438 PHE A CD1 1 ATOM 3292 C CD2 . PHE A 1 424 ? 94.880 117.144 -2.623 1.00 81.66 ? 438 PHE A CD2 1 ATOM 3293 C CE1 . PHE A 1 424 ? 92.391 118.357 -2.522 1.00 83.33 ? 438 PHE A CE1 1 ATOM 3294 C CE2 . PHE A 1 424 ? 93.836 116.552 -1.910 1.00 82.50 ? 438 PHE A CE2 1 ATOM 3295 C CZ . PHE A 1 424 ? 92.592 117.160 -1.862 1.00 81.79 ? 438 PHE A CZ 1 ATOM 3296 N N . THR A 1 425 ? 97.113 116.684 -5.647 1.00 79.71 ? 439 THR A N 1 ATOM 3297 C CA . THR A 1 425 ? 97.412 115.303 -6.019 1.00 82.86 ? 439 THR A CA 1 ATOM 3298 C C . THR A 1 425 ? 98.170 114.582 -4.900 1.00 87.24 ? 439 THR A C 1 ATOM 3299 O O . THR A 1 425 ? 98.922 115.212 -4.151 1.00 88.66 ? 439 THR A O 1 ATOM 3300 C CB . THR A 1 425 ? 98.241 115.275 -7.315 1.00 83.12 ? 439 THR A CB 1 ATOM 3301 O OG1 . THR A 1 425 ? 97.635 116.147 -8.277 1.00 85.50 ? 439 THR A OG1 1 ATOM 3302 C CG2 . THR A 1 425 ? 98.332 113.867 -7.889 1.00 80.68 ? 439 THR A CG2 1 ATOM 3303 N N . LEU A 1 426 ? 97.961 113.268 -4.784 1.00 86.89 ? 440 LEU A N 1 ATOM 3304 C CA . LEU A 1 426 ? 98.612 112.457 -3.751 1.00 87.87 ? 440 LEU A CA 1 ATOM 3305 C C . LEU A 1 426 ? 99.163 111.140 -4.291 1.00 88.56 ? 440 LEU A C 1 ATOM 3306 O O . LEU A 1 426 ? 98.600 110.555 -5.221 1.00 89.06 ? 440 LEU A O 1 ATOM 3307 C CB . LEU A 1 426 ? 97.633 112.111 -2.627 1.00 89.77 ? 440 LEU A CB 1 ATOM 3308 C CG . LEU A 1 426 ? 97.055 113.189 -1.717 1.00 91.33 ? 440 LEU A CG 1 ATOM 3309 C CD1 . LEU A 1 426 ? 96.003 113.987 -2.439 1.00 91.07 ? 440 LEU A CD1 1 ATOM 3310 C CD2 . LEU A 1 426 ? 96.464 112.546 -0.467 1.00 92.15 ? 440 LEU A CD2 1 ATOM 3311 N N . GLU A 1 427 ? 100.245 110.665 -3.678 1.00 90.14 ? 441 GLU A N 1 ATOM 3312 C CA . GLU A 1 427 ? 100.771 109.331 -3.955 1.00 92.75 ? 441 GLU A CA 1 ATOM 3313 C C . GLU A 1 427 ? 100.288 108.387 -2.866 1.00 90.52 ? 441 GLU A C 1 ATOM 3314 O O . GLU A 1 427 ? 100.566 108.597 -1.686 1.00 90.86 ? 441 GLU A O 1 ATOM 3315 C CB . GLU A 1 427 ? 102.303 109.351 -3.988 1.00 98.51 ? 441 GLU A CB 1 ATOM 3316 C CG . GLU A 1 427 ? 102.951 108.043 -4.451 1.00 103.45 ? 441 GLU A CG 1 ATOM 3317 C CD . GLU A 1 427 ? 104.451 108.180 -4.717 1.00 108.23 ? 441 GLU A CD 1 ATOM 3318 O OE1 . GLU A 1 427 ? 105.040 109.226 -4.362 1.00 109.70 ? 441 GLU A OE1 1 ATOM 3319 O OE2 . GLU A 1 427 ? 105.043 107.238 -5.286 1.00 109.69 ? 441 GLU A OE2 1 ATOM 3320 N N . LEU A 1 428 ? 99.559 107.349 -3.254 1.00 87.55 ? 442 LEU A N 1 ATOM 3321 C CA . LEU A 1 428 ? 98.998 106.429 -2.276 1.00 84.25 ? 442 LEU A CA 1 ATOM 3322 C C . LEU A 1 428 ? 99.584 105.038 -2.458 1.00 84.20 ? 442 LEU A C 1 ATOM 3323 O O . LEU A 1 428 ? 99.555 104.481 -3.554 1.00 87.37 ? 442 LEU A O 1 ATOM 3324 C CB . LEU A 1 428 ? 97.476 106.371 -2.410 1.00 81.86 ? 442 LEU A CB 1 ATOM 3325 C CG . LEU A 1 428 ? 96.733 107.696 -2.603 1.00 80.89 ? 442 LEU A CG 1 ATOM 3326 C CD1 . LEU A 1 428 ? 95.286 107.429 -2.992 1.00 78.62 ? 442 LEU A CD1 1 ATOM 3327 C CD2 . LEU A 1 428 ? 96.807 108.591 -1.367 1.00 80.59 ? 442 LEU A CD2 1 ATOM 3328 N N . GLU A 1 429 ? 100.131 104.485 -1.384 1.00 81.23 ? 443 GLU A N 1 ATOM 3329 C CA . GLU A 1 429 ? 100.595 103.108 -1.403 1.00 81.83 ? 443 GLU A CA 1 ATOM 3330 C C . GLU A 1 429 ? 99.544 102.258 -0.692 1.00 80.43 ? 443 GLU A C 1 ATOM 3331 O O . GLU A 1 429 ? 98.401 102.687 -0.543 1.00 76.10 ? 443 GLU A O 1 ATOM 3332 C CB . GLU A 1 429 ? 101.962 103.004 -0.728 1.00 86.34 ? 443 GLU A CB 1 ATOM 3333 C CG . GLU A 1 429 ? 102.811 104.280 -0.894 1.00 90.58 ? 443 GLU A CG 1 ATOM 3334 C CD . GLU A 1 429 ? 104.278 104.000 -1.190 1.00 93.61 ? 443 GLU A CD 1 ATOM 3335 O OE1 . GLU A 1 429 ? 104.679 102.818 -1.138 1.00 94.40 ? 443 GLU A OE1 1 ATOM 3336 O OE2 . GLU A 1 429 ? 105.027 104.966 -1.477 1.00 95.01 ? 443 GLU A OE2 1 ATOM 3337 N N . GLU A 1 430 ? 99.919 101.062 -0.254 1.00 82.04 ? 444 GLU A N 1 ATOM 3338 C CA . GLU A 1 430 ? 98.955 100.149 0.351 1.00 82.96 ? 444 GLU A CA 1 ATOM 3339 C C . GLU A 1 430 ? 98.888 100.314 1.870 1.00 79.17 ? 444 GLU A C 1 ATOM 3340 O O . GLU A 1 430 ? 99.852 100.751 2.505 1.00 79.12 ? 444 GLU A O 1 ATOM 3341 C CB . GLU A 1 430 ? 99.302 98.704 -0.012 1.00 89.25 ? 444 GLU A CB 1 ATOM 3342 C CG . GLU A 1 430 ? 99.656 98.524 -1.486 1.00 97.21 ? 444 GLU A CG 1 ATOM 3343 C CD . GLU A 1 430 ? 100.329 97.192 -1.777 1.00 101.89 ? 444 GLU A CD 1 ATOM 3344 O OE1 . GLU A 1 430 ? 100.087 96.223 -1.021 1.00 102.52 ? 444 GLU A OE1 1 ATOM 3345 O OE2 . GLU A 1 430 ? 101.101 97.121 -2.761 1.00 103.38 ? 444 GLU A OE2 1 ATOM 3346 N N . ASP A 1 431 ? 97.737 99.967 2.435 1.00 73.13 ? 445 ASP A N 1 ATOM 3347 C CA . ASP A 1 431 ? 97.512 100.015 3.877 1.00 69.01 ? 445 ASP A CA 1 ATOM 3348 C C . ASP A 1 431 ? 97.711 101.396 4.499 1.00 65.29 ? 445 ASP A C 1 ATOM 3349 O O . ASP A 1 431 ? 98.275 101.512 5.586 1.00 64.31 ? 445 ASP A O 1 ATOM 3350 C CB . ASP A 1 431 ? 98.374 98.970 4.606 1.00 70.59 ? 445 ASP A CB 1 ATOM 3351 C CG . ASP A 1 431 ? 98.123 97.562 4.108 1.00 73.27 ? 445 ASP A CG 1 ATOM 3352 O OD1 . ASP A 1 431 ? 97.056 97.337 3.502 1.00 76.07 ? 445 ASP A OD1 1 ATOM 3353 O OD2 . ASP A 1 431 ? 98.983 96.682 4.329 1.00 73.28 ? 445 ASP A OD2 1 ATOM 3354 N N . GLU A 1 432 ? 97.216 102.435 3.836 1.00 65.39 ? 446 GLU A N 1 ATOM 3355 C CA . GLU A 1 432 ? 97.380 103.798 4.351 1.00 66.09 ? 446 GLU A CA 1 ATOM 3356 C C . GLU A 1 432 ? 96.057 104.521 4.605 1.00 65.23 ? 446 GLU A C 1 ATOM 3357 O O . GLU A 1 432 ? 95.050 104.252 3.938 1.00 62.33 ? 446 GLU A O 1 ATOM 3358 C CB . GLU A 1 432 ? 98.262 104.628 3.407 1.00 65.76 ? 446 GLU A CB 1 ATOM 3359 C CG . GLU A 1 432 ? 99.688 104.129 3.332 1.00 68.04 ? 446 GLU A CG 1 ATOM 3360 C CD . GLU A 1 432 ? 100.508 104.796 2.244 1.00 74.29 ? 446 GLU A CD 1 ATOM 3361 O OE1 . GLU A 1 432 ? 100.010 105.728 1.568 1.00 75.34 ? 446 GLU A OE1 1 ATOM 3362 O OE2 . GLU A 1 432 ? 101.669 104.375 2.069 1.00 76.88 ? 446 GLU A OE2 1 ATOM 3363 N N . ILE A 1 433 ? 96.069 105.434 5.576 1.00 64.56 ? 447 ILE A N 1 ATOM 3364 C CA . ILE A 1 433 ? 94.935 106.324 5.795 1.00 63.43 ? 447 ILE A CA 1 ATOM 3365 C C . ILE A 1 433 ? 95.424 107.752 5.759 1.00 64.75 ? 447 ILE A C 1 ATOM 3366 O O . ILE A 1 433 ? 96.445 108.077 6.364 1.00 61.23 ? 447 ILE A O 1 ATOM 3367 C CB . ILE A 1 433 ? 94.254 106.125 7.163 1.00 59.48 ? 447 ILE A CB 1 ATOM 3368 C CG1 . ILE A 1 433 ? 93.882 104.664 7.393 1.00 58.84 ? 447 ILE A CG1 1 ATOM 3369 C CG2 . ILE A 1 433 ? 93.024 107.006 7.259 1.00 63.33 ? 447 ILE A CG2 1 ATOM 3370 C CD1 . ILE A 1 433 ? 93.300 104.396 8.781 1.00 58.21 ? 447 ILE A CD1 1 ATOM 3371 N N . PHE A 1 434 ? 94.682 108.605 5.066 1.00 60.92 ? 448 PHE A N 1 ATOM 3372 C CA . PHE A 1 434 ? 94.988 110.022 5.028 1.00 69.18 ? 448 PHE A CA 1 ATOM 3373 C C . PHE A 1 434 ? 93.745 110.783 5.422 1.00 65.44 ? 448 PHE A C 1 ATOM 3374 O O . PHE A 1 434 ? 92.679 110.577 4.848 1.00 60.86 ? 448 PHE A O 1 ATOM 3375 C CB . PHE A 1 434 ? 95.393 110.454 3.610 1.00 72.66 ? 448 PHE A CB 1 ATOM 3376 C CG . PHE A 1 434 ? 96.772 110.015 3.196 1.00 74.47 ? 448 PHE A CG 1 ATOM 3377 C CD1 . PHE A 1 434 ? 97.016 108.700 2.824 1.00 73.22 ? 448 PHE A CD1 1 ATOM 3378 C CD2 . PHE A 1 434 ? 97.821 110.932 3.146 1.00 76.42 ? 448 PHE A CD2 1 ATOM 3379 C CE1 . PHE A 1 434 ? 98.286 108.297 2.428 1.00 73.84 ? 448 PHE A CE1 1 ATOM 3380 C CE2 . PHE A 1 434 ? 99.094 110.537 2.752 1.00 76.03 ? 448 PHE A CE2 1 ATOM 3381 C CZ . PHE A 1 434 ? 99.325 109.218 2.387 1.00 75.56 ? 448 PHE A CZ 1 ATOM 3382 N N . THR A 1 435 ? 93.866 111.668 6.398 1.00 63.91 ? 449 THR A N 1 ATOM 3383 C CA . THR A 1 435 ? 92.781 112.601 6.642 1.00 64.81 ? 449 THR A CA 1 ATOM 3384 C C . THR A 1 435 ? 93.232 114.004 6.276 1.00 66.79 ? 449 THR A C 1 ATOM 3385 O O . THR A 1 435 ? 94.276 114.488 6.737 1.00 67.26 ? 449 THR A O 1 ATOM 3386 C CB . THR A 1 435 ? 92.216 112.525 8.075 1.00 64.79 ? 449 THR A CB 1 ATOM 3387 O OG1 . THR A 1 435 ? 91.843 111.169 8.361 1.00 60.01 ? 449 THR A OG1 1 ATOM 3388 C CG2 . THR A 1 435 ? 90.972 113.418 8.202 1.00 64.99 ? 449 THR A CG2 1 ATOM 3389 N N . LEU A 1 436 ? 92.455 114.633 5.405 1.00 66.59 ? 450 LEU A N 1 ATOM 3390 C CA . LEU A 1 436 ? 92.747 115.983 4.960 1.00 69.53 ? 450 LEU A CA 1 ATOM 3391 C C . LEU A 1 436 ? 91.564 116.831 5.368 1.00 68.76 ? 450 LEU A C 1 ATOM 3392 O O . LEU A 1 436 ? 90.426 116.547 4.997 1.00 67.84 ? 450 LEU A O 1 ATOM 3393 C CB . LEU A 1 436 ? 92.934 116.015 3.444 1.00 69.17 ? 450 LEU A CB 1 ATOM 3394 C CG . LEU A 1 436 ? 93.718 114.835 2.856 1.00 70.58 ? 450 LEU A CG 1 ATOM 3395 C CD1 . LEU A 1 436 ? 93.293 114.576 1.422 1.00 72.76 ? 450 LEU A CD1 1 ATOM 3396 C CD2 . LEU A 1 436 ? 95.217 115.061 2.912 1.00 70.42 ? 450 LEU A CD2 1 ATOM 3397 N N . THR A 1 437 ? 91.830 117.866 6.149 1.00 68.64 ? 451 THR A N 1 ATOM 3398 C CA . THR A 1 437 ? 90.750 118.659 6.694 1.00 69.15 ? 451 THR A CA 1 ATOM 3399 C C . THR A 1 437 ? 91.154 120.099 6.925 1.00 68.56 ? 451 THR A C 1 ATOM 3400 O O . THR A 1 437 ? 92.325 120.405 7.162 1.00 68.24 ? 451 THR A O 1 ATOM 3401 C CB . THR A 1 437 ? 90.231 118.050 8.024 1.00 70.21 ? 451 THR A CB 1 ATOM 3402 O OG1 . THR A 1 437 ? 89.357 118.979 8.678 1.00 70.25 ? 451 THR A OG1 1 ATOM 3403 C CG2 . THR A 1 437 ? 91.392 117.718 8.941 1.00 62.63 ? 451 THR A CG2 1 ATOM 3404 N N . THR A 1 438 ? 90.166 120.981 6.851 1.00 69.12 ? 452 THR A N 1 ATOM 3405 C CA . THR A 1 438 ? 90.348 122.378 7.205 1.00 71.43 ? 452 THR A CA 1 ATOM 3406 C C . THR A 1 438 ? 90.561 122.532 8.719 1.00 75.65 ? 452 THR A C 1 ATOM 3407 O O . THR A 1 438 ? 91.132 123.523 9.177 1.00 77.67 ? 452 THR A O 1 ATOM 3408 C CB . THR A 1 438 ? 89.139 123.217 6.748 1.00 71.64 ? 452 THR A CB 1 ATOM 3409 O OG1 . THR A 1 438 ? 87.946 122.703 7.345 1.00 72.58 ? 452 THR A OG1 1 ATOM 3410 C CG2 . THR A 1 438 ? 88.992 123.146 5.243 1.00 72.36 ? 452 THR A CG2 1 ATOM 3411 N N . LEU A 1 439 ? 90.114 121.537 9.485 1.00 66.07 ? 453 LEU A N 1 ATOM 3412 C CA . LEU A 1 439 ? 90.169 121.595 10.947 1.00 65.63 ? 453 LEU A CA 1 ATOM 3413 C C . LEU A 1 439 ? 91.584 121.507 11.524 1.00 64.32 ? 453 LEU A C 1 ATOM 3414 O O . LEU A 1 439 ? 92.403 120.694 11.089 1.00 61.58 ? 453 LEU A O 1 ATOM 3415 C CB . LEU A 1 439 ? 89.306 120.488 11.564 1.00 65.25 ? 453 LEU A CB 1 ATOM 3416 C CG . LEU A 1 439 ? 87.802 120.518 11.307 1.00 64.22 ? 453 LEU A CG 1 ATOM 3417 C CD1 . LEU A 1 439 ? 87.162 119.244 11.848 1.00 63.61 ? 453 LEU A CD1 1 ATOM 3418 C CD2 . LEU A 1 439 ? 87.182 121.747 11.950 1.00 64.30 ? 453 LEU A CD2 1 ATOM 3419 N N . THR A 1 440 ? 91.823 122.322 12.548 1.00 67.14 ? 454 THR A N 1 ATOM 3420 C CA . THR A 1 440 ? 93.132 122.487 13.170 1.00 72.31 ? 454 THR A CA 1 ATOM 3421 C C . THR A 1 440 ? 93.201 121.846 14.558 1.00 71.66 ? 454 THR A C 1 ATOM 3422 O O . THR A 1 440 ? 94.239 121.900 15.233 1.00 68.87 ? 454 THR A O 1 ATOM 3423 C CB . THR A 1 440 ? 93.431 123.980 13.336 1.00 75.34 ? 454 THR A CB 1 ATOM 3424 O OG1 . THR A 1 440 ? 92.370 124.591 14.085 1.00 76.77 ? 454 THR A OG1 1 ATOM 3425 C CG2 . THR A 1 440 ? 93.536 124.660 11.975 1.00 75.50 ? 454 THR A CG2 1 ATOM 3426 N N . THR A 1 441 ? 92.091 121.235 14.970 1.00 72.61 ? 455 THR A N 1 ATOM 3427 C CA . THR A 1 441 ? 91.915 120.769 16.345 1.00 70.24 ? 455 THR A CA 1 ATOM 3428 C C . THR A 1 441 ? 92.537 119.399 16.609 1.00 69.66 ? 455 THR A C 1 ATOM 3429 O O . THR A 1 441 ? 92.523 118.910 17.739 1.00 73.17 ? 455 THR A O 1 ATOM 3430 C CB . THR A 1 441 ? 90.404 120.738 16.740 1.00 86.40 ? 455 THR A CB 1 ATOM 3431 O OG1 . THR A 1 441 ? 89.725 119.699 16.023 1.00 86.80 ? 455 THR A OG1 1 ATOM 3432 C CG2 . THR A 1 441 ? 89.733 122.068 16.430 1.00 85.42 ? 455 THR A CG2 1 ATOM 3433 N N . GLY A 1 442 ? 93.080 118.778 15.571 1.00 67.78 ? 456 GLY A N 1 ATOM 3434 C CA . GLY A 1 442 ? 93.560 117.414 15.688 1.00 68.10 ? 456 GLY A CA 1 ATOM 3435 C C . GLY A 1 442 ? 94.740 117.254 16.625 1.00 68.69 ? 456 GLY A C 1 ATOM 3436 O O . GLY A 1 442 ? 95.585 118.140 16.736 1.00 69.18 ? 456 GLY A O 1 ATOM 3437 N N . ARG A 1 443 ? 94.808 116.108 17.296 1.00 67.68 ? 457 ARG A N 1 ATOM 3438 C CA . ARG A 1 443 ? 95.907 115.845 18.213 1.00 65.54 ? 457 ARG A CA 1 ATOM 3439 C C . ARG A 1 443 ? 96.059 114.363 18.500 1.00 63.08 ? 457 ARG A C 1 ATOM 3440 O O . ARG A 1 443 ? 95.077 113.682 18.822 1.00 64.73 ? 457 ARG A O 1 ATOM 3441 C CB . ARG A 1 443 ? 95.686 116.602 19.523 1.00 67.95 ? 457 ARG A CB 1 ATOM 3442 C CG . ARG A 1 443 ? 96.579 116.146 20.655 1.00 73.27 ? 457 ARG A CG 1 ATOM 3443 C CD . ARG A 1 443 ? 96.261 116.899 21.935 1.00 80.36 ? 457 ARG A CD 1 ATOM 3444 N NE . ARG A 1 443 ? 97.012 116.373 23.074 1.00 85.53 ? 457 ARG A NE 1 ATOM 3445 C CZ . ARG A 1 443 ? 96.747 116.657 24.347 1.00 86.92 ? 457 ARG A CZ 1 ATOM 3446 N NH1 . ARG A 1 443 ? 95.743 117.468 24.655 1.00 86.30 ? 457 ARG A NH1 1 ATOM 3447 N NH2 . ARG A 1 443 ? 97.486 116.125 25.314 1.00 87.50 ? 457 ARG A NH2 1 ATOM 3448 N N . LYS A 1 444 ? 97.277 113.849 18.372 1.00 57.73 ? 458 LYS A N 1 ATOM 3449 C CA . LYS A 1 444 ? 97.529 112.489 18.820 1.00 56.32 ? 458 LYS A CA 1 ATOM 3450 C C . LYS A 1 444 ? 97.776 112.527 20.321 1.00 58.13 ? 458 LYS A C 1 ATOM 3451 O O . LYS A 1 444 ? 98.906 112.715 20.779 1.00 56.55 ? 458 LYS A O 1 ATOM 3452 C CB . LYS A 1 444 ? 98.710 111.847 18.095 1.00 55.80 ? 458 LYS A CB 1 ATOM 3453 C CG . LYS A 1 444 ? 98.883 110.386 18.481 1.00 60.55 ? 458 LYS A CG 1 ATOM 3454 C CD . LYS A 1 444 ? 100.100 109.742 17.828 1.00 63.91 ? 458 LYS A CD 1 ATOM 3455 C CE . LYS A 1 444 ? 100.235 108.299 18.313 1.00 65.62 ? 458 LYS A CE 1 ATOM 3456 N NZ . LYS A 1 444 ? 101.378 107.592 17.689 1.00 66.68 ? 458 LYS A NZ 1 ATOM 3457 N N . GLY A 1 445 ? 96.698 112.371 21.083 1.00 56.11 ? 459 GLY A N 1 ATOM 3458 C CA . GLY A 1 445 ? 96.777 112.442 22.528 1.00 51.40 ? 459 GLY A CA 1 ATOM 3459 C C . GLY A 1 445 ? 97.763 111.437 23.076 1.00 51.75 ? 459 GLY A C 1 ATOM 3460 O O . GLY A 1 445 ? 97.907 110.330 22.545 1.00 54.06 ? 459 GLY A O 1 ATOM 3461 N N . SER A 1 446 ? 98.443 111.820 24.149 1.00 49.93 ? 460 SER A N 1 ATOM 3462 C CA . SER A 1 446 ? 99.507 110.993 24.691 1.00 54.90 ? 460 SER A CA 1 ATOM 3463 C C . SER A 1 446 ? 99.587 111.105 26.214 1.00 57.89 ? 460 SER A C 1 ATOM 3464 O O . SER A 1 446 ? 99.550 112.205 26.774 1.00 58.63 ? 460 SER A O 1 ATOM 3465 C CB . SER A 1 446 ? 100.850 111.379 24.056 1.00 56.54 ? 460 SER A CB 1 ATOM 3466 O OG . SER A 1 446 ? 101.916 110.727 24.710 1.00 57.82 ? 460 SER A OG 1 ATOM 3467 N N . TYR A 1 447 ? 99.649 109.950 26.865 1.00 48.64 ? 461 TYR A N 1 ATOM 3468 C CA . TYR A 1 447 ? 99.997 109.850 28.269 1.00 54.88 ? 461 TYR A CA 1 ATOM 3469 C C . TYR A 1 447 ? 101.242 108.994 28.297 1.00 57.21 ? 461 TYR A C 1 ATOM 3470 O O . TYR A 1 447 ? 101.499 108.245 27.350 1.00 56.48 ? 461 TYR A O 1 ATOM 3471 C CB . TYR A 1 447 ? 98.877 109.188 29.092 1.00 51.57 ? 461 TYR A CB 1 ATOM 3472 C CG . TYR A 1 447 ? 97.715 110.114 29.361 1.00 54.49 ? 461 TYR A CG 1 ATOM 3473 C CD1 . TYR A 1 447 ? 97.903 111.311 30.046 1.00 53.07 ? 461 TYR A CD1 1 ATOM 3474 C CD2 . TYR A 1 447 ? 96.418 109.793 28.935 1.00 53.81 ? 461 TYR A CD2 1 ATOM 3475 C CE1 . TYR A 1 447 ? 96.841 112.172 30.290 1.00 55.83 ? 461 TYR A CE1 1 ATOM 3476 C CE2 . TYR A 1 447 ? 95.351 110.644 29.180 1.00 53.43 ? 461 TYR A CE2 1 ATOM 3477 C CZ . TYR A 1 447 ? 95.567 111.830 29.860 1.00 56.46 ? 461 TYR A CZ 1 ATOM 3478 O OH . TYR A 1 447 ? 94.515 112.688 30.103 1.00 56.80 ? 461 TYR A OH 1 ATOM 3479 N N . PRO A 1 448 ? 102.031 109.112 29.370 1.00 61.06 ? 462 PRO A N 1 ATOM 3480 C CA . PRO A 1 448 ? 103.214 108.262 29.540 1.00 62.79 ? 462 PRO A CA 1 ATOM 3481 C C . PRO A 1 448 ? 102.861 106.781 29.404 1.00 60.87 ? 462 PRO A C 1 ATOM 3482 O O . PRO A 1 448 ? 101.702 106.426 29.609 1.00 61.50 ? 462 PRO A O 1 ATOM 3483 C CB . PRO A 1 448 ? 103.648 108.580 30.972 1.00 63.80 ? 462 PRO A CB 1 ATOM 3484 C CG . PRO A 1 448 ? 103.261 110.037 31.144 1.00 64.84 ? 462 PRO A CG 1 ATOM 3485 C CD . PRO A 1 448 ? 101.934 110.149 30.418 1.00 63.31 ? 462 PRO A CD 1 ATOM 3486 N N . PRO A 1 449 ? 103.844 105.931 29.050 1.00 60.52 ? 463 PRO A N 1 ATOM 3487 C CA . PRO A 1 449 ? 103.586 104.490 28.947 1.00 56.11 ? 463 PRO A CA 1 ATOM 3488 C C . PRO A 1 449 ? 103.204 103.951 30.318 1.00 56.83 ? 463 PRO A C 1 ATOM 3489 O O . PRO A 1 449 ? 103.749 104.444 31.310 1.00 55.81 ? 463 PRO A O 1 ATOM 3490 C CB . PRO A 1 449 ? 104.949 103.905 28.536 1.00 56.28 ? 463 PRO A CB 1 ATOM 3491 C CG . PRO A 1 449 ? 105.789 105.079 28.081 1.00 58.67 ? 463 PRO A CG 1 ATOM 3492 C CD . PRO A 1 449 ? 105.275 106.253 28.871 1.00 60.09 ? 463 PRO A CD 1 ATOM 3493 N N . PRO A 1 450 ? 102.275 102.977 30.370 1.00 59.28 ? 464 PRO A N 1 ATOM 3494 C CA . PRO A 1 450 ? 101.790 102.320 31.589 1.00 59.48 ? 464 PRO A CA 1 ATOM 3495 C C . PRO A 1 450 ? 102.598 101.046 31.872 1.00 60.80 ? 464 PRO A C 1 ATOM 3496 O O . PRO A 1 450 ? 103.245 100.534 30.947 1.00 58.77 ? 464 PRO A O 1 ATOM 3497 C CB . PRO A 1 450 ? 100.347 101.959 31.213 1.00 58.99 ? 464 PRO A CB 1 ATOM 3498 C CG . PRO A 1 450 ? 100.437 101.637 29.745 1.00 57.39 ? 464 PRO A CG 1 ATOM 3499 C CD . PRO A 1 450 ? 101.536 102.512 29.175 1.00 58.44 ? 464 PRO A CD 1 ATOM 3500 N N . PRO A 1 451 ? 102.557 100.544 33.124 1.00 62.20 ? 465 PRO A N 1 ATOM 3501 C CA . PRO A 1 451 ? 103.362 99.396 33.576 1.00 64.12 ? 465 PRO A CA 1 ATOM 3502 C C . PRO A 1 451 ? 103.373 98.183 32.633 1.00 66.46 ? 465 PRO A C 1 ATOM 3503 O O . PRO A 1 451 ? 102.383 97.928 31.932 1.00 64.56 ? 465 PRO A O 1 ATOM 3504 C CB . PRO A 1 451 ? 102.681 99.001 34.893 1.00 63.42 ? 465 PRO A CB 1 ATOM 3505 C CG . PRO A 1 451 ? 102.138 100.288 35.418 1.00 64.31 ? 465 PRO A CG 1 ATOM 3506 C CD . PRO A 1 451 ? 101.695 101.068 34.207 1.00 62.41 ? 465 PRO A CD 1 ATOM 3507 N N . SER A 1 452 ? 104.479 97.437 32.636 1.00 66.19 ? 466 SER A N 1 ATOM 3508 C CA . SER A 1 452 ? 104.571 96.188 31.873 1.00 67.14 ? 466 SER A CA 1 ATOM 3509 C C . SER A 1 452 ? 103.468 95.215 32.264 1.00 66.42 ? 466 SER A C 1 ATOM 3510 O O . SER A 1 452 ? 102.976 95.244 33.392 1.00 65.59 ? 466 SER A O 1 ATOM 3511 C CB . SER A 1 452 ? 105.930 95.516 32.091 1.00 67.81 ? 466 SER A CB 1 ATOM 3512 O OG . SER A 1 452 ? 106.062 95.020 33.413 1.00 66.38 ? 466 SER A OG 1 ATOM 3513 N N . SER A 1 453 ? 103.077 94.355 31.328 1.00 67.08 ? 467 SER A N 1 ATOM 3514 C CA . SER A 1 453 ? 102.122 93.291 31.626 1.00 64.04 ? 467 SER A CA 1 ATOM 3515 C C . SER A 1 453 ? 102.693 92.329 32.651 1.00 62.56 ? 467 SER A C 1 ATOM 3516 O O . SER A 1 453 ? 103.872 91.975 32.586 1.00 61.95 ? 467 SER A O 1 ATOM 3517 C CB . SER A 1 453 ? 101.783 92.491 30.374 1.00 61.67 ? 467 SER A CB 1 ATOM 3518 O OG . SER A 1 453 ? 101.432 91.163 30.738 1.00 57.68 ? 467 SER A OG 1 ATOM 3519 N N . LYS A 1 454 ? 101.849 91.908 33.591 1.00 59.55 ? 468 LYS A N 1 ATOM 3520 C CA . LYS A 1 454 ? 102.231 90.931 34.602 1.00 58.92 ? 468 LYS A CA 1 ATOM 3521 C C . LYS A 1 454 ? 101.104 89.933 34.727 1.00 60.46 ? 468 LYS A C 1 ATOM 3522 O O . LYS A 1 454 ? 99.936 90.308 34.608 1.00 61.12 ? 468 LYS A O 1 ATOM 3523 C CB . LYS A 1 454 ? 102.464 91.617 35.954 1.00 57.22 ? 468 LYS A CB 1 ATOM 3524 C CG . LYS A 1 454 ? 103.444 92.770 35.882 1.00 57.03 ? 468 LYS A CG 1 ATOM 3525 C CD . LYS A 1 454 ? 103.375 93.677 37.100 1.00 58.99 ? 468 LYS A CD 1 ATOM 3526 C CE . LYS A 1 454 ? 104.479 94.730 37.052 1.00 59.03 ? 468 LYS A CE 1 ATOM 3527 N NZ . LYS A 1 454 ? 104.442 95.603 35.830 1.00 58.42 ? 468 LYS A NZ 1 ATOM 3528 N N . PRO A 1 455 ? 101.438 88.656 34.973 1.00 60.65 ? 469 PRO A N 1 ATOM 3529 C CA . PRO A 1 455 ? 100.366 87.660 35.112 1.00 57.06 ? 469 PRO A CA 1 ATOM 3530 C C . PRO A 1 455 ? 99.484 87.984 36.322 1.00 56.70 ? 469 PRO A C 1 ATOM 3531 O O . PRO A 1 455 ? 99.880 88.801 37.153 1.00 56.39 ? 469 PRO A O 1 ATOM 3532 C CB . PRO A 1 455 ? 101.130 86.348 35.356 1.00 57.40 ? 469 PRO A CB 1 ATOM 3533 C CG . PRO A 1 455 ? 102.553 86.611 34.914 1.00 58.08 ? 469 PRO A CG 1 ATOM 3534 C CD . PRO A 1 455 ? 102.782 88.076 35.172 1.00 56.60 ? 469 PRO A CD 1 ATOM 3535 N N . PHE A 1 456 ? 98.309 87.365 36.413 1.00 55.58 ? 470 PHE A N 1 ATOM 3536 C CA . PHE A 1 456 ? 97.439 87.546 37.565 1.00 58.35 ? 470 PHE A CA 1 ATOM 3537 C C . PHE A 1 456 ? 98.199 87.085 38.814 1.00 62.10 ? 470 PHE A C 1 ATOM 3538 O O . PHE A 1 456 ? 98.854 86.037 38.785 1.00 62.88 ? 470 PHE A O 1 ATOM 3539 C CB . PHE A 1 456 ? 96.159 86.726 37.386 1.00 56.53 ? 470 PHE A CB 1 ATOM 3540 C CG . PHE A 1 456 ? 95.080 87.038 38.396 1.00 57.29 ? 470 PHE A CG 1 ATOM 3541 C CD1 . PHE A 1 456 ? 95.035 86.374 39.621 1.00 56.95 ? 470 PHE A CD1 1 ATOM 3542 C CD2 . PHE A 1 456 ? 94.100 87.987 38.114 1.00 55.57 ? 470 PHE A CD2 1 ATOM 3543 C CE1 . PHE A 1 456 ? 94.037 86.653 40.553 1.00 54.70 ? 470 PHE A CE1 1 ATOM 3544 C CE2 . PHE A 1 456 ? 93.105 88.278 39.033 1.00 53.18 ? 470 PHE A CE2 1 ATOM 3545 C CZ . PHE A 1 456 ? 93.074 87.613 40.259 1.00 56.46 ? 470 PHE A CZ 1 ATOM 3546 N N . PRO A 1 457 ? 98.131 87.877 39.901 1.00 61.22 ? 471 PRO A N 1 ATOM 3547 C CA . PRO A 1 457 ? 98.773 87.552 41.187 1.00 61.31 ? 471 PRO A CA 1 ATOM 3548 C C . PRO A 1 457 ? 98.654 86.071 41.576 1.00 57.51 ? 471 PRO A C 1 ATOM 3549 O O . PRO A 1 457 ? 97.540 85.521 41.573 1.00 55.72 ? 471 PRO A O 1 ATOM 3550 C CB . PRO A 1 457 ? 98.007 88.431 42.176 1.00 61.36 ? 471 PRO A CB 1 ATOM 3551 C CG . PRO A 1 457 ? 97.672 89.664 41.369 1.00 61.45 ? 471 PRO A CG 1 ATOM 3552 C CD . PRO A 1 457 ? 97.498 89.211 39.922 1.00 59.69 ? 471 PRO A CD 1 ATOM 3553 N N . THR A 1 458 ? 99.797 85.448 41.883 1.00 60.54 ? 472 THR A N 1 ATOM 3554 C CA . THR A 1 458 ? 99.881 84.020 42.214 1.00 63.36 ? 472 THR A CA 1 ATOM 3555 C C . THR A 1 458 ? 99.453 83.750 43.654 1.00 64.95 ? 472 THR A C 1 ATOM 3556 O O . THR A 1 458 ? 99.335 82.596 44.084 1.00 65.78 ? 472 THR A O 1 ATOM 3557 C CB . THR A 1 458 ? 101.313 83.466 42.021 1.00 66.84 ? 472 THR A CB 1 ATOM 3558 O OG1 . THR A 1 458 ? 102.245 84.247 42.784 1.00 71.60 ? 472 THR A OG1 1 ATOM 3559 C CG2 . THR A 1 458 ? 101.713 83.492 40.561 1.00 66.99 ? 472 THR A CG2 1 ATOM 3560 N N . ASN A 1 459 ? 99.265 84.832 44.398 1.00 63.08 ? 473 ASN A N 1 ATOM 3561 C CA . ASN A 1 459 ? 98.589 84.788 45.681 1.00 66.87 ? 473 ASN A CA 1 ATOM 3562 C C . ASN A 1 459 ? 97.569 85.905 45.706 1.00 65.25 ? 473 ASN A C 1 ATOM 3563 O O . ASN A 1 459 ? 97.902 87.073 45.479 1.00 69.34 ? 473 ASN A O 1 ATOM 3564 C CB . ASN A 1 459 ? 99.575 84.922 46.837 1.00 72.79 ? 473 ASN A CB 1 ATOM 3565 C CG . ASN A 1 459 ? 99.907 83.589 47.459 1.00 78.25 ? 473 ASN A CG 1 ATOM 3566 O OD1 . ASN A 1 459 ? 100.869 82.927 47.062 1.00 81.51 ? 473 ASN A OD1 1 ATOM 3567 N ND2 . ASN A 1 459 ? 99.094 83.171 48.425 1.00 79.38 ? 473 ASN A ND2 1 ATOM 3568 N N . TYR A 1 460 ? 96.320 85.537 45.948 1.00 57.24 ? 474 TYR A N 1 ATOM 3569 C CA . TYR A 1 460 ? 95.221 86.479 45.843 1.00 53.72 ? 474 TYR A CA 1 ATOM 3570 C C . TYR A 1 460 ? 94.154 86.111 46.861 1.00 52.60 ? 474 TYR A C 1 ATOM 3571 O O . TYR A 1 460 ? 93.876 84.929 47.089 1.00 53.66 ? 474 TYR A O 1 ATOM 3572 C CB . TYR A 1 460 ? 94.630 86.456 44.424 1.00 49.89 ? 474 TYR A CB 1 ATOM 3573 C CG . TYR A 1 460 ? 93.570 87.509 44.195 1.00 50.60 ? 474 TYR A CG 1 ATOM 3574 C CD1 . TYR A 1 460 ? 93.917 88.828 43.928 1.00 53.06 ? 474 TYR A CD1 1 ATOM 3575 C CD2 . TYR A 1 460 ? 92.228 87.184 44.238 1.00 50.12 ? 474 TYR A CD2 1 ATOM 3576 C CE1 . TYR A 1 460 ? 92.952 89.792 43.717 1.00 54.02 ? 474 TYR A CE1 1 ATOM 3577 C CE2 . TYR A 1 460 ? 91.256 88.137 44.032 1.00 51.25 ? 474 TYR A CE2 1 ATOM 3578 C CZ . TYR A 1 460 ? 91.623 89.440 43.768 1.00 53.95 ? 474 TYR A CZ 1 ATOM 3579 O OH . TYR A 1 460 ? 90.644 90.390 43.558 1.00 56.42 ? 474 TYR A OH 1 ATOM 3580 N N . LYS A 1 461 ? 93.569 87.127 47.480 1.00 51.92 ? 475 LYS A N 1 ATOM 3581 C CA . LYS A 1 461 ? 92.514 86.919 48.457 1.00 52.55 ? 475 LYS A CA 1 ATOM 3582 C C . LYS A 1 461 ? 91.584 88.116 48.408 1.00 53.22 ? 475 LYS A C 1 ATOM 3583 O O . LYS A 1 461 ? 92.002 89.237 48.084 1.00 54.77 ? 475 LYS A O 1 ATOM 3584 C CB . LYS A 1 461 ? 93.102 86.744 49.868 1.00 54.18 ? 475 LYS A CB 1 ATOM 3585 N N . ASP A 1 462 ? 90.315 87.859 48.698 1.00 51.64 ? 476 ASP A N 1 ATOM 3586 C CA . ASP A 1 462 ? 89.324 88.907 48.862 1.00 53.42 ? 476 ASP A CA 1 ATOM 3587 C C . ASP A 1 462 ? 88.400 88.416 49.963 1.00 55.02 ? 476 ASP A C 1 ATOM 3588 O O . ASP A 1 462 ? 87.834 87.314 49.870 1.00 54.02 ? 476 ASP A O 1 ATOM 3589 C CB . ASP A 1 462 ? 88.539 89.142 47.557 1.00 54.11 ? 476 ASP A CB 1 ATOM 3590 C CG . ASP A 1 462 ? 87.707 90.426 47.589 1.00 56.90 ? 476 ASP A CG 1 ATOM 3591 O OD1 . ASP A 1 462 ? 87.442 90.947 48.693 1.00 57.93 ? 476 ASP A OD1 1 ATOM 3592 O OD2 . ASP A 1 462 ? 87.300 90.910 46.508 1.00 60.97 ? 476 ASP A OD2 1 ATOM 3593 N N . ASP A 1 463 ? 88.267 89.213 51.019 1.00 55.22 ? 477 ASP A N 1 ATOM 3594 C CA . ASP A 1 463 ? 87.371 88.856 52.108 1.00 55.50 ? 477 ASP A CA 1 ATOM 3595 C C . ASP A 1 463 ? 86.013 89.541 51.957 1.00 55.95 ? 477 ASP A C 1 ATOM 3596 O O . ASP A 1 463 ? 85.136 89.374 52.797 1.00 55.83 ? 477 ASP A O 1 ATOM 3597 C CB . ASP A 1 463 ? 88.009 89.154 53.475 1.00 58.25 ? 477 ASP A CB 1 ATOM 3598 C CG . ASP A 1 463 ? 88.620 90.546 53.557 1.00 58.25 ? 477 ASP A CG 1 ATOM 3599 O OD1 . ASP A 1 463 ? 88.213 91.439 52.784 1.00 56.29 ? 477 ASP A OD1 1 ATOM 3600 O OD2 . ASP A 1 463 ? 89.494 90.761 54.427 1.00 62.49 ? 477 ASP A OD2 1 ATOM 3601 N N . PHE A 1 464 ? 85.848 90.302 50.874 1.00 56.74 ? 478 PHE A N 1 ATOM 3602 C CA . PHE A 1 464 ? 84.601 91.016 50.587 1.00 53.73 ? 478 PHE A CA 1 ATOM 3603 C C . PHE A 1 464 ? 84.170 91.965 51.705 1.00 55.87 ? 478 PHE A C 1 ATOM 3604 O O . PHE A 1 464 ? 83.021 92.404 51.733 1.00 55.76 ? 478 PHE A O 1 ATOM 3605 C CB . PHE A 1 464 ? 83.471 90.036 50.256 1.00 52.77 ? 478 PHE A CB 1 ATOM 3606 C CG . PHE A 1 464 ? 83.883 88.937 49.320 1.00 51.61 ? 478 PHE A CG 1 ATOM 3607 C CD1 . PHE A 1 464 ? 84.324 89.225 48.030 1.00 48.78 ? 478 PHE A CD1 1 ATOM 3608 C CD2 . PHE A 1 464 ? 83.834 87.615 49.730 1.00 52.13 ? 478 PHE A CD2 1 ATOM 3609 C CE1 . PHE A 1 464 ? 84.709 88.208 47.171 1.00 50.07 ? 478 PHE A CE1 1 ATOM 3610 C CE2 . PHE A 1 464 ? 84.211 86.594 48.880 1.00 52.94 ? 478 PHE A CE2 1 ATOM 3611 C CZ . PHE A 1 464 ? 84.655 86.889 47.595 1.00 51.87 ? 478 PHE A CZ 1 ATOM 3612 N N . ASN A 1 465 ? 85.093 92.296 52.609 1.00 57.96 ? 479 ASN A N 1 ATOM 3613 C CA . ASN A 1 465 ? 84.782 93.218 53.694 1.00 61.41 ? 479 ASN A CA 1 ATOM 3614 C C . ASN A 1 465 ? 84.835 94.662 53.215 1.00 61.71 ? 479 ASN A C 1 ATOM 3615 O O . ASN A 1 465 ? 85.800 95.385 53.465 1.00 64.90 ? 479 ASN A O 1 ATOM 3616 C CB . ASN A 1 465 ? 85.722 93.008 54.888 1.00 60.39 ? 479 ASN A CB 1 ATOM 3617 C CG . ASN A 1 465 ? 85.627 91.614 55.458 1.00 59.15 ? 479 ASN A CG 1 ATOM 3618 O OD1 . ASN A 1 465 ? 84.563 90.989 55.416 1.00 53.72 ? 479 ASN A OD1 1 ATOM 3619 N ND2 . ASN A 1 465 ? 86.741 91.112 55.997 1.00 61.24 ? 479 ASN A ND2 1 ATOM 3620 N N . VAL A 1 466 ? 83.784 95.067 52.519 1.00 58.93 ? 480 VAL A N 1 ATOM 3621 C CA . VAL A 1 466 ? 83.665 96.410 51.969 1.00 60.48 ? 480 VAL A CA 1 ATOM 3622 C C . VAL A 1 466 ? 82.248 96.850 52.290 1.00 62.14 ? 480 VAL A C 1 ATOM 3623 O O . VAL A 1 466 ? 81.286 96.185 51.897 1.00 62.93 ? 480 VAL A O 1 ATOM 3624 C CB . VAL A 1 466 ? 83.886 96.404 50.429 1.00 61.49 ? 480 VAL A CB 1 ATOM 3625 C CG1 . VAL A 1 466 ? 83.561 97.763 49.823 1.00 58.94 ? 480 VAL A CG1 1 ATOM 3626 C CG2 . VAL A 1 466 ? 85.317 95.980 50.098 1.00 60.74 ? 480 VAL A CG2 1 ATOM 3627 N N . GLU A 1 467 ? 82.105 97.952 53.014 1.00 65.22 ? 481 GLU A N 1 ATOM 3628 C CA . GLU A 1 467 ? 80.800 98.308 53.565 1.00 70.86 ? 481 GLU A CA 1 ATOM 3629 C C . GLU A 1 467 ? 79.982 99.146 52.599 1.00 72.66 ? 481 GLU A C 1 ATOM 3630 O O . GLU A 1 467 ? 78.771 98.950 52.459 1.00 74.49 ? 481 GLU A O 1 ATOM 3631 C CB . GLU A 1 467 ? 80.971 99.055 54.883 1.00 75.98 ? 481 GLU A CB 1 ATOM 3632 C CG . GLU A 1 467 ? 79.690 99.226 55.670 1.00 76.91 ? 481 GLU A CG 1 ATOM 3633 C CD . GLU A 1 467 ? 79.927 99.948 56.980 1.00 79.27 ? 481 GLU A CD 1 ATOM 3634 O OE1 . GLU A 1 467 ? 81.099 100.287 57.274 1.00 75.75 ? 481 GLU A OE1 1 ATOM 3635 O OE2 . GLU A 1 467 ? 78.940 100.175 57.711 1.00 83.93 ? 481 GLU A OE2 1 ATOM 3636 N N . TYR A 1 468 ? 80.652 100.085 51.939 1.00 72.87 ? 482 TYR A N 1 ATOM 3637 C CA . TYR A 1 468 ? 80.012 100.909 50.921 1.00 72.87 ? 482 TYR A CA 1 ATOM 3638 C C . TYR A 1 468 ? 80.714 100.748 49.572 1.00 64.45 ? 482 TYR A C 1 ATOM 3639 O O . TYR A 1 468 ? 81.432 101.651 49.132 1.00 61.99 ? 482 TYR A O 1 ATOM 3640 C CB . TYR A 1 468 ? 80.014 102.376 51.359 1.00 78.67 ? 482 TYR A CB 1 ATOM 3641 C CG . TYR A 1 468 ? 79.196 102.628 52.607 1.00 84.96 ? 482 TYR A CG 1 ATOM 3642 C CD1 . TYR A 1 468 ? 77.804 102.551 52.576 1.00 86.93 ? 482 TYR A CD1 1 ATOM 3643 C CD2 . TYR A 1 468 ? 79.812 102.944 53.815 1.00 87.11 ? 482 TYR A CD2 1 ATOM 3644 C CE1 . TYR A 1 468 ? 77.051 102.780 53.717 1.00 88.98 ? 482 TYR A CE1 1 ATOM 3645 C CE2 . TYR A 1 468 ? 79.069 103.176 54.957 1.00 89.12 ? 482 TYR A CE2 1 ATOM 3646 C CZ . TYR A 1 468 ? 77.691 103.094 54.905 1.00 90.32 ? 482 TYR A CZ 1 ATOM 3647 O OH . TYR A 1 468 ? 76.951 103.328 56.045 1.00 92.03 ? 482 TYR A OH 1 ATOM 3648 N N . PRO A 1 469 ? 80.510 99.596 48.911 1.00 58.15 ? 483 PRO A N 1 ATOM 3649 C CA . PRO A 1 469 ? 81.233 99.353 47.656 1.00 55.07 ? 483 PRO A CA 1 ATOM 3650 C C . PRO A 1 469 ? 80.864 100.339 46.550 1.00 50.85 ? 483 PRO A C 1 ATOM 3651 O O . PRO A 1 469 ? 79.706 100.742 46.432 1.00 49.75 ? 483 PRO A O 1 ATOM 3652 C CB . PRO A 1 469 ? 80.819 97.926 47.279 1.00 52.81 ? 483 PRO A CB 1 ATOM 3653 C CG . PRO A 1 469 ? 79.573 97.658 48.037 1.00 50.99 ? 483 PRO A CG 1 ATOM 3654 C CD . PRO A 1 469 ? 79.650 98.461 49.288 1.00 54.74 ? 483 PRO A CD 1 ATOM 3655 N N . LEU A 1 470 ? 81.859 100.744 45.771 1.00 52.25 ? 484 LEU A N 1 ATOM 3656 C CA . LEU A 1 470 ? 81.624 101.624 44.632 1.00 54.17 ? 484 LEU A CA 1 ATOM 3657 C C . LEU A 1 470 ? 80.894 100.882 43.514 1.00 51.35 ? 484 LEU A C 1 ATOM 3658 O O . LEU A 1 470 ? 80.005 101.450 42.868 1.00 54.37 ? 484 LEU A O 1 ATOM 3659 C CB . LEU A 1 470 ? 82.945 102.207 44.137 1.00 56.90 ? 484 LEU A CB 1 ATOM 3660 C CG . LEU A 1 470 ? 83.580 103.104 45.202 1.00 61.14 ? 484 LEU A CG 1 ATOM 3661 C CD1 . LEU A 1 470 ? 85.033 103.425 44.873 1.00 58.25 ? 484 LEU A CD1 1 ATOM 3662 C CD2 . LEU A 1 470 ? 82.744 104.376 45.365 1.00 62.71 ? 484 LEU A CD2 1 ATOM 3663 N N . PHE A 1 471 ? 81.250 99.614 43.301 1.00 46.33 ? 485 PHE A N 1 ATOM 3664 C CA . PHE A 1 471 ? 80.505 98.754 42.358 1.00 45.28 ? 485 PHE A CA 1 ATOM 3665 C C . PHE A 1 471 ? 79.850 97.574 43.063 1.00 46.03 ? 485 PHE A C 1 ATOM 3666 O O . PHE A 1 471 ? 80.301 97.160 44.134 1.00 42.85 ? 485 PHE A O 1 ATOM 3667 C CB . PHE A 1 471 ? 81.425 98.239 41.253 1.00 45.40 ? 485 PHE A CB 1 ATOM 3668 C CG . PHE A 1 471 ? 82.027 99.327 40.421 1.00 47.11 ? 485 PHE A CG 1 ATOM 3669 C CD1 . PHE A 1 471 ? 83.227 99.916 40.794 1.00 47.37 ? 485 PHE A CD1 1 ATOM 3670 C CD2 . PHE A 1 471 ? 81.377 99.780 39.274 1.00 48.17 ? 485 PHE A CD2 1 ATOM 3671 C CE1 . PHE A 1 471 ? 83.786 100.928 40.019 1.00 47.85 ? 485 PHE A CE1 1 ATOM 3672 C CE2 . PHE A 1 471 ? 81.923 100.793 38.499 1.00 47.53 ? 485 PHE A CE2 1 ATOM 3673 C CZ . PHE A 1 471 ? 83.132 101.364 38.871 1.00 45.25 ? 485 PHE A CZ 1 ATOM 3674 N N . SER A 1 472 ? 78.812 97.017 42.435 1.00 44.70 ? 486 SER A N 1 ATOM 3675 C CA . SER A 1 472 ? 77.951 96.006 43.067 1.00 45.24 ? 486 SER A CA 1 ATOM 3676 C C . SER A 1 472 ? 78.591 94.620 43.225 1.00 44.48 ? 486 SER A C 1 ATOM 3677 O O . SER A 1 472 ? 78.066 93.783 43.959 1.00 47.36 ? 486 SER A O 1 ATOM 3678 C CB . SER A 1 472 ? 76.630 95.880 42.303 1.00 47.35 ? 486 SER A CB 1 ATOM 3679 O OG . SER A 1 472 ? 76.859 95.456 40.966 1.00 38.86 ? 486 SER A OG 1 ATOM 3680 N N . GLU A 1 473 ? 79.704 94.371 42.532 1.00 44.62 ? 487 GLU A N 1 ATOM 3681 C CA . GLU A 1 473 ? 80.406 93.092 42.665 1.00 44.76 ? 487 GLU A CA 1 ATOM 3682 C C . GLU A 1 473 ? 81.907 93.272 42.928 1.00 43.54 ? 487 GLU A C 1 ATOM 3683 O O . GLU A 1 473 ? 82.511 94.266 42.506 1.00 43.00 ? 487 GLU A O 1 ATOM 3684 C CB . GLU A 1 473 ? 80.200 92.227 41.418 1.00 44.73 ? 487 GLU A CB 1 ATOM 3685 C CG . GLU A 1 473 ? 80.920 90.879 41.483 1.00 45.54 ? 487 GLU A CG 1 ATOM 3686 C CD . GLU A 1 473 ? 80.620 89.978 40.297 1.00 53.57 ? 487 GLU A CD 1 ATOM 3687 O OE1 . GLU A 1 473 ? 80.155 90.473 39.238 1.00 54.40 ? 487 GLU A OE1 1 ATOM 3688 O OE2 . GLU A 1 473 ? 80.861 88.761 40.433 1.00 53.83 ? 487 GLU A OE2 1 ATOM 3689 N N . ALA A 1 474 ? 82.508 92.308 43.628 1.00 44.45 ? 488 ALA A N 1 ATOM 3690 C CA . ALA A 1 474 ? 83.945 92.335 43.907 1.00 45.46 ? 488 ALA A CA 1 ATOM 3691 C C . ALA A 1 474 ? 84.748 92.299 42.601 1.00 44.68 ? 488 ALA A C 1 ATOM 3692 O O . ALA A 1 474 ? 84.294 91.730 41.606 1.00 43.65 ? 488 ALA A O 1 ATOM 3693 C CB . ALA A 1 474 ? 84.335 91.174 44.809 1.00 43.17 ? 488 ALA A CB 1 ATOM 3694 N N . PRO A 1 475 ? 85.939 92.919 42.606 1.00 45.72 ? 489 PRO A N 1 ATOM 3695 C CA . PRO A 1 475 ? 86.801 92.994 41.418 1.00 46.99 ? 489 PRO A CA 1 ATOM 3696 C C . PRO A 1 475 ? 87.213 91.624 40.896 1.00 47.33 ? 489 PRO A C 1 ATOM 3697 O O . PRO A 1 475 ? 87.333 90.672 41.682 1.00 46.08 ? 489 PRO A O 1 ATOM 3698 C CB . PRO A 1 475 ? 88.060 93.718 41.942 1.00 49.00 ? 489 PRO A CB 1 ATOM 3699 C CG . PRO A 1 475 ? 87.998 93.589 43.441 1.00 46.41 ? 489 PRO A CG 1 ATOM 3700 C CD . PRO A 1 475 ? 86.523 93.641 43.749 1.00 44.87 ? 489 PRO A CD 1 ATOM 3701 N N . ASN A 1 476 ? 87.400 91.533 39.580 1.00 48.00 ? 490 ASN A N 1 ATOM 3702 C CA . ASN A 1 476 ? 87.993 90.359 38.950 1.00 47.51 ? 490 ASN A CA 1 ATOM 3703 C C . ASN A 1 476 ? 87.150 89.089 38.898 1.00 47.11 ? 490 ASN A C 1 ATOM 3704 O O . ASN A 1 476 ? 87.485 88.162 38.163 1.00 42.34 ? 490 ASN A O 1 ATOM 3705 C CB . ASN A 1 476 ? 89.359 90.081 39.563 1.00 50.16 ? 490 ASN A CB 1 ATOM 3706 C CG . ASN A 1 476 ? 90.239 91.306 39.548 1.00 50.67 ? 490 ASN A CG 1 ATOM 3707 O OD1 . ASN A 1 476 ? 90.316 92.006 38.532 1.00 47.51 ? 490 ASN A OD1 1 ATOM 3708 N ND2 . ASN A 1 476 ? 90.874 91.605 40.688 1.00 48.77 ? 490 ASN A ND2 1 ATOM 3709 N N . PHE A 1 477 ? 86.065 89.034 39.666 1.00 41.79 ? 491 PHE A N 1 ATOM 3710 C CA . PHE A 1 477 ? 85.126 87.936 39.503 1.00 43.56 ? 491 PHE A CA 1 ATOM 3711 C C . PHE A 1 477 ? 84.257 88.228 38.299 1.00 42.08 ? 491 PHE A C 1 ATOM 3712 O O . PHE A 1 477 ? 83.424 89.137 38.349 1.00 43.37 ? 491 PHE A O 1 ATOM 3713 C CB . PHE A 1 477 ? 84.237 87.770 40.734 1.00 40.65 ? 491 PHE A CB 1 ATOM 3714 C CG . PHE A 1 477 ? 84.891 87.022 41.853 1.00 46.10 ? 491 PHE A CG 1 ATOM 3715 C CD1 . PHE A 1 477 ? 84.884 85.633 41.868 1.00 46.38 ? 491 PHE A CD1 1 ATOM 3716 C CD2 . PHE A 1 477 ? 85.518 87.702 42.886 1.00 47.63 ? 491 PHE A CD2 1 ATOM 3717 C CE1 . PHE A 1 477 ? 85.498 84.928 42.904 1.00 50.38 ? 491 PHE A CE1 1 ATOM 3718 C CE2 . PHE A 1 477 ? 86.137 87.005 43.927 1.00 51.07 ? 491 PHE A CE2 1 ATOM 3719 C CZ . PHE A 1 477 ? 86.123 85.616 43.935 1.00 51.30 ? 491 PHE A CZ 1 ATOM 3720 N N . ALA A 1 478 ? 84.462 87.462 37.227 1.00 39.83 ? 492 ALA A N 1 ATOM 3721 C CA . ALA A 1 478 ? 83.652 87.563 36.009 1.00 41.04 ? 492 ALA A CA 1 ATOM 3722 C C . ALA A 1 478 ? 82.571 86.489 35.989 1.00 40.25 ? 492 ALA A C 1 ATOM 3723 O O . ALA A 1 478 ? 82.867 85.333 35.679 1.00 38.29 ? 492 ALA A O 1 ATOM 3724 C CB . ALA A 1 478 ? 84.540 87.424 34.756 1.00 41.02 ? 492 ALA A CB 1 ATOM 3725 N N . ASP A 1 479 ? 81.328 86.866 36.301 1.00 37.51 ? 493 ASP A N 1 ATOM 3726 C CA . ASP A 1 479 ? 80.220 85.906 36.292 1.00 36.75 ? 493 ASP A CA 1 ATOM 3727 C C . ASP A 1 479 ? 79.962 85.356 34.878 1.00 43.93 ? 493 ASP A C 1 ATOM 3728 O O . ASP A 1 479 ? 79.947 86.117 33.921 1.00 42.29 ? 493 ASP A O 1 ATOM 3729 C CB . ASP A 1 479 ? 78.952 86.555 36.838 1.00 39.02 ? 493 ASP A CB 1 ATOM 3730 C CG . ASP A 1 479 ? 79.167 87.206 38.193 1.00 41.46 ? 493 ASP A CG 1 ATOM 3731 O OD1 . ASP A 1 479 ? 80.222 86.936 38.828 1.00 41.55 ? 493 ASP A OD1 1 ATOM 3732 O OD2 . ASP A 1 479 ? 78.279 87.981 38.621 1.00 39.92 ? 493 ASP A OD2 1 ATOM 3733 N N . GLN A 1 480 ? 79.788 84.041 34.755 1.00 36.17 ? 494 GLN A N 1 ATOM 3734 C CA . GLN A 1 480 ? 79.554 83.408 33.449 1.00 38.77 ? 494 GLN A CA 1 ATOM 3735 C C . GLN A 1 480 ? 78.174 82.747 33.358 1.00 42.13 ? 494 GLN A C 1 ATOM 3736 O O . GLN A 1 480 ? 77.679 82.499 32.268 1.00 42.17 ? 494 GLN A O 1 ATOM 3737 C CB . GLN A 1 480 ? 80.661 82.409 33.120 1.00 37.65 ? 494 GLN A CB 1 ATOM 3738 C CG . GLN A 1 480 ? 82.055 83.042 33.054 1.00 39.16 ? 494 GLN A CG 1 ATOM 3739 C CD . GLN A 1 480 ? 82.126 84.202 32.057 1.00 39.24 ? 494 GLN A CD 1 ATOM 3740 O OE1 . GLN A 1 480 ? 81.523 84.149 30.969 1.00 41.36 ? 494 GLN A OE1 1 ATOM 3741 N NE2 . GLN A 1 480 ? 82.843 85.256 32.431 1.00 38.02 ? 494 GLN A NE2 1 ATOM 3742 N N . THR A 1 481 ? 77.572 82.448 34.511 1.00 34.92 ? 495 THR A N 1 ATOM 3743 C CA . THR A 1 481 ? 76.144 82.127 34.588 1.00 39.02 ? 495 THR A CA 1 ATOM 3744 C C . THR A 1 481 ? 75.714 82.525 35.999 1.00 40.49 ? 495 THR A C 1 ATOM 3745 O O . THR A 1 481 ? 76.459 82.306 36.958 1.00 34.85 ? 495 THR A O 1 ATOM 3746 C CB . THR A 1 481 ? 75.813 80.630 34.265 1.00 34.14 ? 495 THR A CB 1 ATOM 3747 O OG1 . THR A 1 481 ? 76.039 80.366 32.869 1.00 42.47 ? 495 THR A OG1 1 ATOM 3748 C CG2 . THR A 1 481 ? 74.360 80.330 34.556 1.00 33.53 ? 495 THR A CG2 1 ATOM 3749 N N . GLY A 1 482 ? 74.551 83.160 36.114 1.00 38.69 ? 496 GLY A N 1 ATOM 3750 C CA . GLY A 1 482 ? 74.135 83.729 37.380 1.00 38.76 ? 496 GLY A CA 1 ATOM 3751 C C . GLY A 1 482 ? 74.796 85.088 37.614 1.00 36.91 ? 496 GLY A C 1 ATOM 3752 O O . GLY A 1 482 ? 75.530 85.593 36.761 1.00 36.82 ? 496 GLY A O 1 ATOM 3753 N N . VAL A 1 483 ? 74.511 85.688 38.765 1.00 35.94 ? 497 VAL A N 1 ATOM 3754 C CA . VAL A 1 483 ? 74.998 87.029 39.095 1.00 35.01 ? 497 VAL A CA 1 ATOM 3755 C C . VAL A 1 483 ? 75.422 87.058 40.563 1.00 39.64 ? 497 VAL A C 1 ATOM 3756 O O . VAL A 1 483 ? 74.641 86.649 41.438 1.00 40.77 ? 497 VAL A O 1 ATOM 3757 C CB . VAL A 1 483 ? 73.879 88.064 38.860 1.00 36.51 ? 497 VAL A CB 1 ATOM 3758 C CG1 . VAL A 1 483 ? 74.274 89.434 39.421 1.00 35.59 ? 497 VAL A CG1 1 ATOM 3759 C CG2 . VAL A 1 483 ? 73.531 88.153 37.367 1.00 33.97 ? 497 VAL A CG2 1 ATOM 3760 N N . PHE A 1 484 ? 76.642 87.523 40.839 1.00 40.29 ? 498 PHE A N 1 ATOM 3761 C CA . PHE A 1 484 ? 77.181 87.514 42.202 1.00 40.92 ? 498 PHE A CA 1 ATOM 3762 C C . PHE A 1 484 ? 77.415 88.945 42.680 1.00 45.43 ? 498 PHE A C 1 ATOM 3763 O O . PHE A 1 484 ? 78.007 89.751 41.951 1.00 46.48 ? 498 PHE A O 1 ATOM 3764 C CB . PHE A 1 484 ? 78.505 86.733 42.271 1.00 39.44 ? 498 PHE A CB 1 ATOM 3765 C CG . PHE A 1 484 ? 78.388 85.284 41.833 1.00 39.99 ? 498 PHE A CG 1 ATOM 3766 C CD1 . PHE A 1 484 ? 78.093 84.958 40.504 1.00 36.78 ? 498 PHE A CD1 1 ATOM 3767 C CD2 . PHE A 1 484 ? 78.584 84.249 42.746 1.00 38.63 ? 498 PHE A CD2 1 ATOM 3768 C CE1 . PHE A 1 484 ? 77.986 83.637 40.106 1.00 40.94 ? 498 PHE A CE1 1 ATOM 3769 C CE2 . PHE A 1 484 ? 78.483 82.917 42.355 1.00 42.32 ? 498 PHE A CE2 1 ATOM 3770 C CZ . PHE A 1 484 ? 78.182 82.611 41.025 1.00 43.41 ? 498 PHE A CZ 1 ATOM 3771 N N . GLU A 1 485 ? 76.961 89.262 43.898 1.00 41.46 ? 499 GLU A N 1 ATOM 3772 C CA . GLU A 1 485 ? 76.989 90.638 44.393 1.00 42.06 ? 499 GLU A CA 1 ATOM 3773 C C . GLU A 1 485 ? 77.535 90.721 45.823 1.00 46.55 ? 499 GLU A C 1 ATOM 3774 O O . GLU A 1 485 ? 77.430 89.752 46.580 1.00 47.06 ? 499 GLU A O 1 ATOM 3775 C CB . GLU A 1 485 ? 75.572 91.236 44.348 1.00 39.96 ? 499 GLU A CB 1 ATOM 3776 C CG . GLU A 1 485 ? 74.915 91.162 42.990 1.00 44.35 ? 499 GLU A CG 1 ATOM 3777 C CD . GLU A 1 485 ? 73.564 91.852 42.946 1.00 51.75 ? 499 GLU A CD 1 ATOM 3778 O OE1 . GLU A 1 485 ? 72.893 91.934 44.006 1.00 50.99 ? 499 GLU A OE1 1 ATOM 3779 O OE2 . GLU A 1 485 ? 73.176 92.315 41.844 1.00 50.96 ? 499 GLU A OE2 1 ATOM 3780 N N . TYR A 1 486 ? 78.110 91.871 46.183 1.00 44.99 ? 500 TYR A N 1 ATOM 3781 C CA . TYR A 1 486 ? 78.449 92.152 47.580 1.00 49.07 ? 500 TYR A CA 1 ATOM 3782 C C . TYR A 1 486 ? 77.161 92.015 48.357 1.00 48.77 ? 500 TYR A C 1 ATOM 3783 O O . TYR A 1 486 ? 76.108 92.464 47.888 1.00 41.49 ? 500 TYR A O 1 ATOM 3784 C CB . TYR A 1 486 ? 78.967 93.582 47.755 1.00 42.91 ? 500 TYR A CB 1 ATOM 3785 C CG . TYR A 1 486 ? 80.413 93.791 47.366 1.00 43.39 ? 500 TYR A CG 1 ATOM 3786 C CD1 . TYR A 1 486 ? 81.435 93.193 48.085 1.00 49.13 ? 500 TYR A CD1 1 ATOM 3787 C CD2 . TYR A 1 486 ? 80.762 94.625 46.309 1.00 45.59 ? 500 TYR A CD2 1 ATOM 3788 C CE1 . TYR A 1 486 ? 82.764 93.389 47.742 1.00 48.11 ? 500 TYR A CE1 1 ATOM 3789 C CE2 . TYR A 1 486 ? 82.091 94.829 45.960 1.00 43.77 ? 500 TYR A CE2 1 ATOM 3790 C CZ . TYR A 1 486 ? 83.087 94.203 46.686 1.00 49.00 ? 500 TYR A CZ 1 ATOM 3791 O OH . TYR A 1 486 ? 84.426 94.392 46.380 1.00 53.44 ? 500 TYR A OH 1 ATOM 3792 N N . TYR A 1 487 ? 77.238 91.392 49.530 1.00 48.31 ? 501 TYR A N 1 ATOM 3793 C CA . TYR A 1 487 ? 76.052 91.212 50.364 1.00 49.80 ? 501 TYR A CA 1 ATOM 3794 C C . TYR A 1 487 ? 76.368 91.504 51.841 1.00 44.44 ? 501 TYR A C 1 ATOM 3795 O O . TYR A 1 487 ? 77.343 90.994 52.395 1.00 45.10 ? 501 TYR A O 1 ATOM 3796 C CB . TYR A 1 487 ? 75.456 89.807 50.172 1.00 47.58 ? 501 TYR A CB 1 ATOM 3797 C CG . TYR A 1 487 ? 74.213 89.545 51.004 1.00 50.42 ? 501 TYR A CG 1 ATOM 3798 C CD1 . TYR A 1 487 ? 72.999 90.119 50.662 1.00 52.10 ? 501 TYR A CD1 1 ATOM 3799 C CD2 . TYR A 1 487 ? 74.256 88.720 52.128 1.00 51.74 ? 501 TYR A CD2 1 ATOM 3800 C CE1 . TYR A 1 487 ? 71.866 89.892 51.411 1.00 51.27 ? 501 TYR A CE1 1 ATOM 3801 C CE2 . TYR A 1 487 ? 73.120 88.479 52.879 1.00 54.65 ? 501 TYR A CE2 1 ATOM 3802 C CZ . TYR A 1 487 ? 71.930 89.072 52.515 1.00 55.21 ? 501 TYR A CZ 1 ATOM 3803 O OH . TYR A 1 487 ? 70.786 88.852 53.253 1.00 59.77 ? 501 TYR A OH 1 ATOM 3804 N N . MET A 1 488 ? 75.567 92.361 52.465 1.00 47.95 ? 502 MET A N 1 ATOM 3805 C CA . MET A 1 488 ? 75.762 92.638 53.886 1.00 53.98 ? 502 MET A CA 1 ATOM 3806 C C . MET A 1 488 ? 74.694 91.914 54.688 1.00 55.83 ? 502 MET A C 1 ATOM 3807 O O . MET A 1 488 ? 73.508 92.025 54.383 1.00 54.07 ? 502 MET A O 1 ATOM 3808 C CB . MET A 1 488 ? 75.711 94.134 54.180 1.00 54.61 ? 502 MET A CB 1 ATOM 3809 C CG . MET A 1 488 ? 75.648 94.448 55.679 1.00 58.09 ? 502 MET A CG 1 ATOM 3810 S SD . MET A 1 488 ? 75.874 96.197 56.079 1.00 74.76 ? 502 MET A SD 1 ATOM 3811 C CE . MET A 1 488 ? 74.474 96.955 55.252 1.00 78.56 ? 502 MET A CE 1 ATOM 3812 N N . ASN A 1 489 ? 75.119 91.152 55.689 1.00 60.23 ? 503 ASN A N 1 ATOM 3813 C CA . ASN A 1 489 ? 74.186 90.446 56.551 1.00 65.91 ? 503 ASN A CA 1 ATOM 3814 C C . ASN A 1 489 ? 74.434 90.824 58.000 1.00 71.77 ? 503 ASN A C 1 ATOM 3815 O O . ASN A 1 489 ? 75.244 90.189 58.671 1.00 68.74 ? 503 ASN A O 1 ATOM 3816 C CB . ASN A 1 489 ? 74.328 88.934 56.361 1.00 66.91 ? 503 ASN A CB 1 ATOM 3817 C CG . ASN A 1 489 ? 73.516 88.134 57.371 1.00 70.85 ? 503 ASN A CG 1 ATOM 3818 O OD1 . ASN A 1 489 ? 72.584 88.647 57.998 1.00 72.85 ? 503 ASN A OD1 1 ATOM 3819 N ND2 . ASN A 1 489 ? 73.871 86.865 57.532 1.00 71.22 ? 503 ASN A ND2 1 ATOM 3820 N N . ASN A 1 490 ? 73.733 91.853 58.476 1.00 82.58 ? 504 ASN A N 1 ATOM 3821 C CA . ASN A 1 490 ? 73.900 92.356 59.847 1.00 93.93 ? 504 ASN A CA 1 ATOM 3822 C C . ASN A 1 490 ? 73.679 91.299 60.931 1.00 97.96 ? 504 ASN A C 1 ATOM 3823 O O . ASN A 1 490 ? 74.309 91.346 61.991 1.00 99.50 ? 504 ASN A O 1 ATOM 3824 C CB . ASN A 1 490 ? 72.971 93.549 60.109 1.00 98.27 ? 504 ASN A CB 1 ATOM 3825 C CG . ASN A 1 490 ? 73.465 94.833 59.466 1.00 101.00 ? 504 ASN A CG 1 ATOM 3826 O OD1 . ASN A 1 490 ? 74.653 95.154 59.519 1.00 102.26 ? 504 ASN A OD1 1 ATOM 3827 N ND2 . ASN A 1 490 ? 72.548 95.576 58.855 1.00 102.03 ? 504 ASN A ND2 1 ATOM 3828 N N . GLU A 1 491 ? 72.790 90.346 60.651 1.00 99.17 ? 505 GLU A N 1 ATOM 3829 C CA . GLU A 1 491 ? 72.412 89.317 61.621 1.00 101.96 ? 505 GLU A CA 1 ATOM 3830 C C . GLU A 1 491 ? 73.458 88.203 61.776 1.00 97.74 ? 505 GLU A C 1 ATOM 3831 O O . GLU A 1 491 ? 73.168 87.131 62.309 1.00 97.06 ? 505 GLU A O 1 ATOM 3832 C CB . GLU A 1 491 ? 71.054 88.721 61.250 1.00 107.32 ? 505 GLU A CB 1 ATOM 3833 C CG . GLU A 1 491 ? 69.974 89.755 60.965 1.00 112.47 ? 505 GLU A CG 1 ATOM 3834 C CD . GLU A 1 491 ? 68.781 89.153 60.238 1.00 116.18 ? 505 GLU A CD 1 ATOM 3835 O OE1 . GLU A 1 491 ? 68.562 87.930 60.367 1.00 118.04 ? 505 GLU A OE1 1 ATOM 3836 O OE2 . GLU A 1 491 ? 68.066 89.895 59.530 1.00 116.87 ? 505 GLU A OE2 1 ATOM 3837 N N . ASP A 1 492 ? 74.669 88.465 61.297 1.00 93.72 ? 506 ASP A N 1 ATOM 3838 C CA . ASP A 1 492 ? 75.817 87.606 61.559 1.00 90.36 ? 506 ASP A CA 1 ATOM 3839 C C . ASP A 1 492 ? 77.031 88.507 61.759 1.00 88.09 ? 506 ASP A C 1 ATOM 3840 O O . ASP A 1 492 ? 77.212 89.484 61.022 1.00 88.13 ? 506 ASP A O 1 ATOM 3841 C CB . ASP A 1 492 ? 76.057 86.637 60.394 1.00 87.77 ? 506 ASP A CB 1 ATOM 3842 C CG . ASP A 1 492 ? 77.063 85.538 60.732 1.00 86.32 ? 506 ASP A CG 1 ATOM 3843 O OD1 . ASP A 1 492 ? 78.122 85.834 61.325 1.00 86.58 ? 506 ASP A OD1 1 ATOM 3844 O OD2 . ASP A 1 492 ? 76.792 84.366 60.397 1.00 84.83 ? 506 ASP A OD2 1 ATOM 3845 N N . ARG A 1 493 ? 77.849 88.187 62.760 1.00 80.95 ? 507 ARG A N 1 ATOM 3846 C CA . ARG A 1 493 ? 79.077 88.928 63.009 1.00 74.32 ? 507 ARG A CA 1 ATOM 3847 C C . ARG A 1 493 ? 80.278 88.322 62.277 1.00 71.97 ? 507 ARG A C 1 ATOM 3848 O O . ARG A 1 493 ? 81.123 89.056 61.763 1.00 73.67 ? 507 ARG A O 1 ATOM 3849 C CB . ARG A 1 493 ? 79.358 89.020 64.515 1.00 74.93 ? 507 ARG A CB 1 ATOM 3850 N N . GLU A 1 494 ? 80.359 86.992 62.221 1.00 71.80 ? 508 GLU A N 1 ATOM 3851 C CA . GLU A 1 494 ? 81.505 86.328 61.577 1.00 76.13 ? 508 GLU A CA 1 ATOM 3852 C C . GLU A 1 494 ? 81.458 86.379 60.038 1.00 71.22 ? 508 GLU A C 1 ATOM 3853 O O . GLU A 1 494 ? 82.492 86.306 59.368 1.00 72.26 ? 508 GLU A O 1 ATOM 3854 C CB . GLU A 1 494 ? 81.661 84.878 62.074 1.00 82.87 ? 508 GLU A CB 1 ATOM 3855 C CG . GLU A 1 494 ? 83.029 84.254 61.748 1.00 89.22 ? 508 GLU A CG 1 ATOM 3856 C CD . GLU A 1 494 ? 83.231 82.863 62.347 1.00 93.73 ? 508 GLU A CD 1 ATOM 3857 O OE1 . GLU A 1 494 ? 82.694 82.593 63.446 1.00 95.92 ? 508 GLU A OE1 1 ATOM 3858 O OE2 . GLU A 1 494 ? 83.935 82.043 61.710 1.00 93.09 ? 508 GLU A OE2 1 ATOM 3859 N N . HIS A 1 495 ? 80.256 86.504 59.485 1.00 64.56 ? 509 HIS A N 1 ATOM 3860 C CA . HIS A 1 495 ? 80.090 86.585 58.032 1.00 59.73 ? 509 HIS A CA 1 ATOM 3861 C C . HIS A 1 495 ? 79.165 87.732 57.669 1.00 55.67 ? 509 HIS A C 1 ATOM 3862 O O . HIS A 1 495 ? 78.129 87.535 57.037 1.00 55.34 ? 509 HIS A O 1 ATOM 3863 C CB . HIS A 1 495 ? 79.561 85.256 57.478 1.00 59.32 ? 509 HIS A CB 1 ATOM 3864 C CG . HIS A 1 495 ? 80.476 84.101 57.746 1.00 61.87 ? 509 HIS A CG 1 ATOM 3865 N ND1 . HIS A 1 495 ? 81.597 83.848 56.982 1.00 60.16 ? 509 HIS A ND1 1 ATOM 3866 C CD2 . HIS A 1 495 ? 80.460 83.155 58.715 1.00 63.37 ? 509 HIS A CD2 1 ATOM 3867 C CE1 . HIS A 1 495 ? 82.219 82.784 57.456 1.00 61.88 ? 509 HIS A CE1 1 ATOM 3868 N NE2 . HIS A 1 495 ? 81.553 82.348 58.512 1.00 65.47 ? 509 HIS A NE2 1 ATOM 3869 N N . ARG A 1 496 ? 79.542 88.937 58.085 1.00 56.62 ? 510 ARG A N 1 ATOM 3870 C CA . ARG A 1 496 ? 78.692 90.106 57.893 1.00 56.95 ? 510 ARG A CA 1 ATOM 3871 C C . ARG A 1 496 ? 78.756 90.599 56.454 1.00 53.40 ? 510 ARG A C 1 ATOM 3872 O O . ARG A 1 496 ? 77.761 91.081 55.902 1.00 49.83 ? 510 ARG A O 1 ATOM 3873 C CB . ARG A 1 496 ? 79.119 91.218 58.841 1.00 60.15 ? 510 ARG A CB 1 ATOM 3874 C CG . ARG A 1 496 ? 78.190 92.414 58.836 1.00 66.84 ? 510 ARG A CG 1 ATOM 3875 C CD . ARG A 1 496 ? 78.695 93.490 59.784 1.00 73.68 ? 510 ARG A CD 1 ATOM 3876 N NE . ARG A 1 496 ? 77.803 94.647 59.829 1.00 78.78 ? 510 ARG A NE 1 ATOM 3877 C CZ . ARG A 1 496 ? 78.214 95.898 60.016 1.00 81.64 ? 510 ARG A CZ 1 ATOM 3878 N NH1 . ARG A 1 496 ? 79.508 96.159 60.164 1.00 80.77 ? 510 ARG A NH1 1 ATOM 3879 N NH2 . ARG A 1 496 ? 77.334 96.889 60.045 1.00 83.44 ? 510 ARG A NH2 1 ATOM 3880 N N . PHE A 1 497 ? 79.932 90.468 55.851 1.00 52.40 ? 511 PHE A N 1 ATOM 3881 C CA . PHE A 1 497 ? 80.136 90.932 54.478 1.00 51.11 ? 511 PHE A CA 1 ATOM 3882 C C . PHE A 1 497 ? 80.554 89.775 53.588 1.00 48.85 ? 511 PHE A C 1 ATOM 3883 O O . PHE A 1 497 ? 81.645 89.240 53.727 1.00 53.16 ? 511 PHE A O 1 ATOM 3884 C CB . PHE A 1 497 ? 81.179 92.054 54.449 1.00 49.57 ? 511 PHE A CB 1 ATOM 3885 C CG . PHE A 1 497 ? 80.768 93.263 55.243 1.00 53.85 ? 511 PHE A CG 1 ATOM 3886 C CD1 . PHE A 1 497 ? 79.730 94.078 54.799 1.00 55.05 ? 511 PHE A CD1 1 ATOM 3887 C CD2 . PHE A 1 497 ? 81.390 93.570 56.441 1.00 53.53 ? 511 PHE A CD2 1 ATOM 3888 C CE1 . PHE A 1 497 ? 79.337 95.185 55.529 1.00 55.48 ? 511 PHE A CE1 1 ATOM 3889 C CE2 . PHE A 1 497 ? 81.000 94.675 57.176 1.00 55.80 ? 511 PHE A CE2 1 ATOM 3890 C CZ . PHE A 1 497 ? 79.975 95.484 56.717 1.00 56.16 ? 511 PHE A CZ 1 ATOM 3891 N N . THR A 1 498 ? 79.672 89.372 52.687 1.00 45.80 ? 512 THR A N 1 ATOM 3892 C CA . THR A 1 498 ? 79.939 88.201 51.871 1.00 54.19 ? 512 THR A CA 1 ATOM 3893 C C . THR A 1 498 ? 79.689 88.499 50.392 1.00 48.69 ? 512 THR A C 1 ATOM 3894 O O . THR A 1 498 ? 79.347 89.626 50.029 1.00 47.34 ? 512 THR A O 1 ATOM 3895 C CB . THR A 1 498 ? 79.035 87.041 52.287 1.00 44.75 ? 512 THR A CB 1 ATOM 3896 O OG1 . THR A 1 498 ? 77.681 87.408 52.034 1.00 44.09 ? 512 THR A OG1 1 ATOM 3897 C CG2 . THR A 1 498 ? 79.200 86.721 53.790 1.00 47.02 ? 512 THR A CG2 1 ATOM 3898 N N . LEU A 1 499 ? 79.874 87.479 49.557 1.00 47.54 ? 513 LEU A N 1 ATOM 3899 C CA . LEU A 1 499 ? 79.505 87.529 48.148 1.00 47.78 ? 513 LEU A CA 1 ATOM 3900 C C . LEU A 1 499 ? 78.356 86.535 47.942 1.00 50.50 ? 513 LEU A C 1 ATOM 3901 O O . LEU A 1 499 ? 78.466 85.368 48.330 1.00 52.74 ? 513 LEU A O 1 ATOM 3902 C CB . LEU A 1 499 ? 80.705 87.157 47.273 1.00 48.59 ? 513 LEU A CB 1 ATOM 3903 C CG . LEU A 1 499 ? 80.617 87.521 45.779 1.00 44.78 ? 513 LEU A CG 1 ATOM 3904 C CD1 . LEU A 1 499 ? 80.826 89.009 45.586 1.00 43.08 ? 513 LEU A CD1 1 ATOM 3905 C CD2 . LEU A 1 499 ? 81.633 86.742 44.945 1.00 40.80 ? 513 LEU A CD2 1 ATOM 3906 N N . ARG A 1 500 ? 77.251 86.997 47.359 1.00 40.26 ? 514 ARG A N 1 ATOM 3907 C CA . ARG A 1 500 ? 76.046 86.185 47.200 1.00 39.59 ? 514 ARG A CA 1 ATOM 3908 C C . ARG A 1 500 ? 75.641 86.038 45.722 1.00 42.27 ? 514 ARG A C 1 ATOM 3909 O O . ARG A 1 500 ? 75.647 87.026 44.984 1.00 41.07 ? 514 ARG A O 1 ATOM 3910 C CB . ARG A 1 500 ? 74.898 86.861 47.954 1.00 39.82 ? 514 ARG A CB 1 ATOM 3911 C CG . ARG A 1 500 ? 73.708 85.998 48.262 1.00 39.68 ? 514 ARG A CG 1 ATOM 3912 C CD . ARG A 1 500 ? 72.673 86.830 49.024 1.00 44.03 ? 514 ARG A CD 1 ATOM 3913 N NE . ARG A 1 500 ? 71.581 86.025 49.564 1.00 48.02 ? 514 ARG A NE 1 ATOM 3914 C CZ . ARG A 1 500 ? 70.299 86.386 49.536 1.00 53.69 ? 514 ARG A CZ 1 ATOM 3915 N NH1 . ARG A 1 500 ? 69.939 87.542 48.982 1.00 51.95 ? 514 ARG A NH1 1 ATOM 3916 N NH2 . ARG A 1 500 ? 69.371 85.590 50.057 1.00 56.45 ? 514 ARG A NH2 1 ATOM 3917 N N . GLN A 1 501 ? 75.293 84.820 45.299 1.00 39.84 ? 515 GLN A N 1 ATOM 3918 C CA . GLN A 1 501 ? 74.698 84.621 43.982 1.00 38.66 ? 515 GLN A CA 1 ATOM 3919 C C . GLN A 1 501 ? 73.231 84.903 44.176 1.00 36.61 ? 515 GLN A C 1 ATOM 3920 O O . GLN A 1 501 ? 72.600 84.306 45.056 1.00 36.93 ? 515 GLN A O 1 ATOM 3921 C CB . GLN A 1 501 ? 74.909 83.196 43.488 1.00 36.76 ? 515 GLN A CB 1 ATOM 3922 C CG . GLN A 1 501 ? 74.717 83.021 41.970 1.00 37.71 ? 515 GLN A CG 1 ATOM 3923 C CD . GLN A 1 501 ? 73.265 83.163 41.538 1.00 36.60 ? 515 GLN A CD 1 ATOM 3924 O OE1 . GLN A 1 501 ? 72.961 83.875 40.592 1.00 37.68 ? 515 GLN A OE1 1 ATOM 3925 N NE2 . GLN A 1 501 ? 72.366 82.484 42.239 1.00 35.25 ? 515 GLN A NE2 1 ATOM 3926 N N . VAL A 1 502 ? 72.695 85.831 43.387 1.00 36.05 ? 516 VAL A N 1 ATOM 3927 C CA . VAL A 1 502 ? 71.362 86.373 43.645 1.00 37.78 ? 516 VAL A CA 1 ATOM 3928 C C . VAL A 1 502 ? 70.250 85.933 42.685 1.00 40.28 ? 516 VAL A C 1 ATOM 3929 O O . VAL A 1 502 ? 69.081 86.242 42.936 1.00 34.88 ? 516 VAL A O 1 ATOM 3930 C CB . VAL A 1 502 ? 71.402 87.912 43.704 1.00 41.82 ? 516 VAL A CB 1 ATOM 3931 C CG1 . VAL A 1 502 ? 72.306 88.379 44.852 1.00 40.47 ? 516 VAL A CG1 1 ATOM 3932 C CG2 . VAL A 1 502 ? 71.899 88.482 42.375 1.00 35.60 ? 516 VAL A CG2 1 ATOM 3933 N N . LEU A 1 503 ? 70.573 85.223 41.602 1.00 36.83 ? 517 LEU A N 1 ATOM 3934 C CA . LEU A 1 503 ? 69.475 84.739 40.738 1.00 37.97 ? 517 LEU A CA 1 ATOM 3935 C C . LEU A 1 503 ? 68.749 83.543 41.339 1.00 37.36 ? 517 LEU A C 1 ATOM 3936 O O . LEU A 1 503 ? 69.390 82.567 41.726 1.00 37.92 ? 517 LEU A O 1 ATOM 3937 C CB . LEU A 1 503 ? 69.974 84.366 39.335 1.00 38.14 ? 517 LEU A CB 1 ATOM 3938 C CG . LEU A 1 503 ? 70.716 85.447 38.551 1.00 37.07 ? 517 LEU A CG 1 ATOM 3939 C CD1 . LEU A 1 503 ? 70.799 85.056 37.077 1.00 32.58 ? 517 LEU A CD1 1 ATOM 3940 C CD2 . LEU A 1 503 ? 70.041 86.802 38.714 1.00 33.08 ? 517 LEU A CD2 1 ATOM 3941 N N . ASN A 1 504 ? 67.419 83.610 41.415 1.00 33.56 ? 518 ASN A N 1 ATOM 3942 C CA . ASN A 1 504 ? 66.645 82.471 41.864 1.00 38.68 ? 518 ASN A CA 1 ATOM 3943 C C . ASN A 1 504 ? 65.873 81.799 40.709 1.00 37.51 ? 518 ASN A C 1 ATOM 3944 O O . ASN A 1 504 ? 65.064 80.922 40.944 1.00 33.05 ? 518 ASN A O 1 ATOM 3945 C CB . ASN A 1 504 ? 65.705 82.840 43.039 1.00 38.74 ? 518 ASN A CB 1 ATOM 3946 C CG . ASN A 1 504 ? 64.571 83.795 42.624 1.00 42.75 ? 518 ASN A CG 1 ATOM 3947 O OD1 . ASN A 1 504 ? 64.559 84.332 41.507 1.00 40.33 ? 518 ASN A OD1 1 ATOM 3948 N ND2 . ASN A 1 504 ? 63.624 84.024 43.544 1.00 40.62 ? 518 ASN A ND2 1 ATOM 3949 N N . GLN A 1 505 ? 66.119 82.223 39.470 1.00 36.79 ? 519 GLN A N 1 ATOM 3950 C CA . GLN A 1 505 ? 65.563 81.511 38.305 1.00 33.57 ? 519 GLN A CA 1 ATOM 3951 C C . GLN A 1 505 ? 66.320 81.815 37.007 1.00 33.03 ? 519 GLN A C 1 ATOM 3952 O O . GLN A 1 505 ? 66.926 82.886 36.857 1.00 32.22 ? 519 GLN A O 1 ATOM 3953 C CB . GLN A 1 505 ? 64.057 81.745 38.141 1.00 37.60 ? 519 GLN A CB 1 ATOM 3954 C CG . GLN A 1 505 ? 63.640 83.059 37.512 1.00 41.01 ? 519 GLN A CG 1 ATOM 3955 C CD . GLN A 1 505 ? 62.130 83.124 37.264 1.00 43.76 ? 519 GLN A CD 1 ATOM 3956 O OE1 . GLN A 1 505 ? 61.615 82.520 36.319 1.00 46.46 ? 519 GLN A OE1 1 ATOM 3957 N NE2 . GLN A 1 505 ? 61.421 83.864 38.109 1.00 41.89 ? 519 GLN A NE2 1 ATOM 3958 N N . ARG A 1 506 ? 66.312 80.855 36.085 1.00 34.25 ? 520 ARG A N 1 ATOM 3959 C CA . ARG A 1 506 ? 67.005 81.022 34.809 1.00 34.60 ? 520 ARG A CA 1 ATOM 3960 C C . ARG A 1 506 ? 66.482 82.273 34.077 1.00 30.51 ? 520 ARG A C 1 ATOM 3961 O O . ARG A 1 506 ? 65.270 82.499 34.017 1.00 30.64 ? 520 ARG A O 1 ATOM 3962 C CB . ARG A 1 506 ? 66.807 79.759 33.952 1.00 36.83 ? 520 ARG A CB 1 ATOM 3963 C CG . ARG A 1 506 ? 67.584 79.781 32.618 1.00 35.98 ? 520 ARG A CG 1 ATOM 3964 C CD . ARG A 1 506 ? 67.402 78.476 31.849 1.00 34.30 ? 520 ARG A CD 1 ATOM 3965 N NE . ARG A 1 506 ? 68.342 78.400 30.723 1.00 38.78 ? 520 ARG A NE 1 ATOM 3966 C CZ . ARG A 1 506 ? 69.618 78.017 30.822 1.00 35.58 ? 520 ARG A CZ 1 ATOM 3967 N NH1 . ARG A 1 506 ? 70.118 77.669 31.998 1.00 38.13 ? 520 ARG A NH1 1 ATOM 3968 N NH2 . ARG A 1 506 ? 70.405 77.991 29.743 1.00 33.09 ? 520 ARG A NH2 1 ATOM 3969 N N . PRO A 1 507 ? 67.387 83.106 33.533 1.00 30.58 ? 521 PRO A N 1 ATOM 3970 C CA . PRO A 1 507 ? 66.926 84.243 32.712 1.00 30.27 ? 521 PRO A CA 1 ATOM 3971 C C . PRO A 1 507 ? 66.243 83.796 31.404 1.00 34.58 ? 521 PRO A C 1 ATOM 3972 O O . PRO A 1 507 ? 66.327 82.618 31.043 1.00 32.96 ? 521 PRO A O 1 ATOM 3973 C CB . PRO A 1 507 ? 68.229 84.943 32.328 1.00 30.59 ? 521 PRO A CB 1 ATOM 3974 C CG . PRO A 1 507 ? 69.237 84.528 33.402 1.00 31.09 ? 521 PRO A CG 1 ATOM 3975 C CD . PRO A 1 507 ? 68.853 83.114 33.730 1.00 31.05 ? 521 PRO A CD 1 ATOM 3976 N N . ILE A 1 508 ? 65.572 84.728 30.723 1.00 31.66 ? 522 ILE A N 1 ATOM 3977 C CA . ILE A 1 508 ? 65.273 84.585 29.301 1.00 29.39 ? 522 ILE A CA 1 ATOM 3978 C C . ILE A 1 508 ? 66.607 84.720 28.601 1.00 30.55 ? 522 ILE A C 1 ATOM 3979 O O . ILE A 1 508 ? 67.120 85.828 28.404 1.00 33.74 ? 522 ILE A O 1 ATOM 3980 C CB . ILE A 1 508 ? 64.297 85.677 28.804 1.00 29.56 ? 522 ILE A CB 1 ATOM 3981 C CG1 . ILE A 1 508 ? 62.935 85.509 29.501 1.00 29.62 ? 522 ILE A CG1 1 ATOM 3982 C CG2 . ILE A 1 508 ? 64.107 85.585 27.286 1.00 30.26 ? 522 ILE A CG2 1 ATOM 3983 C CD1 . ILE A 1 508 ? 61.936 86.571 29.158 1.00 31.29 ? 522 ILE A CD1 1 ATOM 3984 N N . THR A 1 509 ? 67.193 83.580 28.256 1.00 29.91 ? 523 THR A N 1 ATOM 3985 C CA . THR A 1 509 ? 68.619 83.527 27.905 1.00 32.29 ? 523 THR A CA 1 ATOM 3986 C C . THR A 1 509 ? 68.817 84.020 26.486 1.00 36.49 ? 523 THR A C 1 ATOM 3987 O O . THR A 1 509 ? 67.913 83.922 25.667 1.00 30.28 ? 523 THR A O 1 ATOM 3988 C CB . THR A 1 509 ? 69.157 82.084 27.996 1.00 34.40 ? 523 THR A CB 1 ATOM 3989 O OG1 . THR A 1 509 ? 68.260 81.189 27.305 1.00 35.44 ? 523 THR A OG1 1 ATOM 3990 C CG2 . THR A 1 509 ? 69.293 81.649 29.469 1.00 34.61 ? 523 THR A CG2 1 ATOM 3991 N N . TRP A 1 510 ? 70.005 84.544 26.206 1.00 33.87 ? 524 TRP A N 1 ATOM 3992 C CA . TRP A 1 510 ? 70.387 84.928 24.862 1.00 35.69 ? 524 TRP A CA 1 ATOM 3993 C C . TRP A 1 510 ? 71.313 83.822 24.370 1.00 40.76 ? 524 TRP A C 1 ATOM 3994 O O . TRP A 1 510 ? 71.194 83.332 23.252 1.00 41.03 ? 524 TRP A O 1 ATOM 3995 C CB . TRP A 1 510 ? 71.164 86.256 24.896 1.00 33.83 ? 524 TRP A CB 1 ATOM 3996 C CG . TRP A 1 510 ? 71.612 86.727 23.535 1.00 32.65 ? 524 TRP A CG 1 ATOM 3997 C CD1 . TRP A 1 510 ? 70.847 87.374 22.599 1.00 32.19 ? 524 TRP A CD1 1 ATOM 3998 C CD2 . TRP A 1 510 ? 72.922 86.589 22.956 1.00 33.10 ? 524 TRP A CD2 1 ATOM 3999 N NE1 . TRP A 1 510 ? 71.601 87.646 21.488 1.00 32.90 ? 524 TRP A NE1 1 ATOM 4000 C CE2 . TRP A 1 510 ? 72.875 87.173 21.673 1.00 33.48 ? 524 TRP A CE2 1 ATOM 4001 C CE3 . TRP A 1 510 ? 74.122 86.032 23.399 1.00 34.92 ? 524 TRP A CE3 1 ATOM 4002 C CZ2 . TRP A 1 510 ? 73.994 87.218 20.823 1.00 39.79 ? 524 TRP A CZ2 1 ATOM 4003 C CZ3 . TRP A 1 510 ? 75.241 86.071 22.543 1.00 34.51 ? 524 TRP A CZ3 1 ATOM 4004 C CH2 . TRP A 1 510 ? 75.166 86.662 21.282 1.00 34.91 ? 524 TRP A CH2 1 ATOM 4005 N N . ALA A 1 511 ? 72.248 83.448 25.236 1.00 41.09 ? 525 ALA A N 1 ATOM 4006 C CA . ALA A 1 511 ? 73.204 82.395 24.954 1.00 41.01 ? 525 ALA A CA 1 ATOM 4007 C C . ALA A 1 511 ? 72.760 81.132 25.664 1.00 36.58 ? 525 ALA A C 1 ATOM 4008 O O . ALA A 1 511 ? 71.686 81.092 26.264 1.00 38.01 ? 525 ALA A O 1 ATOM 4009 C CB . ALA A 1 511 ? 74.584 82.804 25.444 1.00 45.28 ? 525 ALA A CB 1 ATOM 4010 N N . ALA A 1 512 ? 73.595 80.100 25.624 1.00 35.89 ? 526 ALA A N 1 ATOM 4011 C CA . ALA A 1 512 ? 73.272 78.866 26.331 1.00 38.38 ? 526 ALA A CA 1 ATOM 4012 C C . ALA A 1 512 ? 73.916 78.863 27.713 1.00 38.80 ? 526 ALA A C 1 ATOM 4013 O O . ALA A 1 512 ? 74.954 78.224 27.914 1.00 39.62 ? 526 ALA A O 1 ATOM 4014 C CB . ALA A 1 512 ? 73.734 77.657 25.535 1.00 38.55 ? 526 ALA A CB 1 ATOM 4015 N N . ASP A 1 513 ? 73.303 79.569 28.658 1.00 38.85 ? 527 ASP A N 1 ATOM 4016 C CA . ASP A 1 513 ? 73.812 79.605 30.028 1.00 40.31 ? 527 ASP A CA 1 ATOM 4017 C C . ASP A 1 513 ? 73.911 78.173 30.576 1.00 39.08 ? 527 ASP A C 1 ATOM 4018 O O . ASP A 1 513 ? 73.147 77.295 30.174 1.00 35.96 ? 527 ASP A O 1 ATOM 4019 C CB . ASP A 1 513 ? 72.890 80.449 30.920 1.00 35.70 ? 527 ASP A CB 1 ATOM 4020 C CG . ASP A 1 513 ? 72.735 81.879 30.427 1.00 38.68 ? 527 ASP A CG 1 ATOM 4021 O OD1 . ASP A 1 513 ? 72.566 82.106 29.191 1.00 40.89 ? 527 ASP A OD1 1 ATOM 4022 O OD2 . ASP A 1 513 ? 72.767 82.790 31.289 1.00 38.83 ? 527 ASP A OD2 1 ATOM 4023 N N . ALA A 1 514 ? 74.869 77.937 31.468 1.00 40.91 ? 528 ALA A N 1 ATOM 4024 C CA . ALA A 1 514 ? 74.978 76.645 32.146 1.00 41.14 ? 528 ALA A CA 1 ATOM 4025 C C . ALA A 1 514 ? 73.760 76.438 33.023 1.00 38.49 ? 528 ALA A C 1 ATOM 4026 O O . ALA A 1 514 ? 73.007 77.386 33.265 1.00 33.29 ? 528 ALA A O 1 ATOM 4027 C CB . ALA A 1 514 ? 76.251 76.591 33.002 1.00 35.00 ? 528 ALA A CB 1 ATOM 4028 N N . SER A 1 515 ? 73.585 75.214 33.522 1.00 39.70 ? 529 SER A N 1 ATOM 4029 C CA . SER A 1 515 ? 72.499 74.897 34.447 1.00 42.42 ? 529 SER A CA 1 ATOM 4030 C C . SER A 1 515 ? 72.877 75.260 35.873 1.00 40.05 ? 529 SER A C 1 ATOM 4031 O O . SER A 1 515 ? 72.015 75.339 36.759 1.00 39.71 ? 529 SER A O 1 ATOM 4032 C CB . SER A 1 515 ? 72.160 73.413 34.373 1.00 45.75 ? 529 SER A CB 1 ATOM 4033 O OG . SER A 1 515 ? 71.524 73.137 33.138 1.00 54.59 ? 529 SER A OG 1 ATOM 4034 N N . SER A 1 516 ? 74.172 75.466 36.074 1.00 36.18 ? 530 SER A N 1 ATOM 4035 C CA . SER A 1 516 ? 74.736 75.875 37.354 1.00 39.13 ? 530 SER A CA 1 ATOM 4036 C C . SER A 1 516 ? 75.323 77.280 37.233 1.00 39.16 ? 530 SER A C 1 ATOM 4037 O O . SER A 1 516 ? 75.792 77.665 36.160 1.00 38.49 ? 530 SER A O 1 ATOM 4038 C CB . SER A 1 516 ? 75.835 74.889 37.778 1.00 39.85 ? 530 SER A CB 1 ATOM 4039 O OG . SER A 1 516 ? 75.320 73.568 37.894 1.00 41.20 ? 530 SER A OG 1 ATOM 4040 N N . THR A 1 517 ? 75.300 78.052 38.321 1.00 38.15 ? 531 THR A N 1 ATOM 4041 C CA . THR A 1 517 ? 75.899 79.386 38.278 1.00 36.55 ? 531 THR A CA 1 ATOM 4042 C C . THR A 1 517 ? 77.407 79.281 38.484 1.00 38.04 ? 531 THR A C 1 ATOM 4043 O O . THR A 1 517 ? 77.900 78.311 39.081 1.00 37.93 ? 531 THR A O 1 ATOM 4044 C CB . THR A 1 517 ? 75.263 80.348 39.295 1.00 35.20 ? 531 THR A CB 1 ATOM 4045 O OG1 . THR A 1 517 ? 75.658 79.979 40.617 1.00 38.69 ? 531 THR A OG1 1 ATOM 4046 C CG2 . THR A 1 517 ? 73.731 80.304 39.183 1.00 34.54 ? 531 THR A CG2 1 ATOM 4047 N N . ILE A 1 518 ? 78.145 80.264 37.972 1.00 40.11 ? 532 ILE A N 1 ATOM 4048 C CA . ILE A 1 518 ? 79.600 80.216 38.045 1.00 38.60 ? 532 ILE A CA 1 ATOM 4049 C C . ILE A 1 518 ? 80.225 81.572 37.766 1.00 39.47 ? 532 ILE A C 1 ATOM 4050 O O . ILE A 1 518 ? 79.786 82.297 36.868 1.00 42.36 ? 532 ILE A O 1 ATOM 4051 C CB . ILE A 1 518 ? 80.171 79.149 37.061 1.00 44.98 ? 532 ILE A CB 1 ATOM 4052 C CG1 . ILE A 1 518 ? 81.693 79.044 37.171 1.00 41.89 ? 532 ILE A CG1 1 ATOM 4053 C CG2 . ILE A 1 518 ? 79.740 79.440 35.624 1.00 42.26 ? 532 ILE A CG2 1 ATOM 4054 C CD1 . ILE A 1 518 ? 82.239 77.733 36.631 1.00 41.62 ? 532 ILE A CD1 1 ATOM 4055 N N . SER A 1 519 ? 81.256 81.908 38.541 1.00 42.27 ? 533 SER A N 1 ATOM 4056 C CA . SER A 1 519 ? 82.046 83.101 38.307 1.00 45.88 ? 533 SER A CA 1 ATOM 4057 C C . SER A 1 519 ? 83.503 82.648 38.251 1.00 47.39 ? 533 SER A C 1 ATOM 4058 O O . SER A 1 519 ? 83.929 81.851 39.086 1.00 47.53 ? 533 SER A O 1 ATOM 4059 C CB . SER A 1 519 ? 81.836 84.103 39.452 1.00 48.54 ? 533 SER A CB 1 ATOM 4060 O OG . SER A 1 519 ? 82.286 85.398 39.094 1.00 47.25 ? 533 SER A OG 1 ATOM 4061 N N . VAL A 1 520 ? 84.259 83.129 37.266 1.00 45.94 ? 534 VAL A N 1 ATOM 4062 C CA . VAL A 1 520 ? 85.659 82.738 37.142 1.00 46.95 ? 534 VAL A CA 1 ATOM 4063 C C . VAL A 1 520 ? 86.583 83.905 37.446 1.00 45.06 ? 534 VAL A C 1 ATOM 4064 O O . VAL A 1 520 ? 86.190 85.072 37.323 1.00 40.90 ? 534 VAL A O 1 ATOM 4065 C CB . VAL A 1 520 ? 85.988 82.182 35.732 1.00 45.09 ? 534 VAL A CB 1 ATOM 4066 C CG1 . VAL A 1 520 ? 85.094 80.978 35.417 1.00 41.35 ? 534 VAL A CG1 1 ATOM 4067 C CG2 . VAL A 1 520 ? 85.875 83.288 34.676 1.00 40.33 ? 534 VAL A CG2 1 ATOM 4068 N N . ILE A 1 521 ? 87.814 83.578 37.834 1.00 46.79 ? 535 ILE A N 1 ATOM 4069 C CA . ILE A 1 521 ? 88.777 84.583 38.275 1.00 47.88 ? 535 ILE A CA 1 ATOM 4070 C C . ILE A 1 521 ? 90.214 84.069 38.133 1.00 48.33 ? 535 ILE A C 1 ATOM 4071 O O . ILE A 1 521 ? 90.468 82.865 38.272 1.00 47.92 ? 535 ILE A O 1 ATOM 4072 C CB . ILE A 1 521 ? 88.491 85.019 39.751 1.00 49.36 ? 535 ILE A CB 1 ATOM 4073 C CG1 . ILE A 1 521 ? 89.385 86.194 40.171 1.00 49.60 ? 535 ILE A CG1 1 ATOM 4074 C CG2 . ILE A 1 521 ? 88.683 83.855 40.712 1.00 48.73 ? 535 ILE A CG2 1 ATOM 4075 C CD1 . ILE A 1 521 ? 89.052 86.748 41.565 1.00 49.23 ? 535 ILE A CD1 1 ATOM 4076 N N . GLY A 1 522 ? 91.148 84.970 37.835 1.00 51.73 ? 536 GLY A N 1 ATOM 4077 C CA . GLY A 1 522 ? 92.560 84.632 37.887 1.00 52.74 ? 536 GLY A CA 1 ATOM 4078 C C . GLY A 1 522 ? 93.284 84.589 36.553 1.00 55.23 ? 536 GLY A C 1 ATOM 4079 O O . GLY A 1 522 ? 93.166 85.505 35.725 1.00 54.51 ? 536 GLY A O 1 ATOM 4080 N N . ASP A 1 523 ? 94.047 83.515 36.356 1.00 56.09 ? 537 ASP A N 1 ATOM 4081 C CA . ASP A 1 523 ? 94.884 83.345 35.172 1.00 53.52 ? 537 ASP A CA 1 ATOM 4082 C C . ASP A 1 523 ? 94.611 81.981 34.527 1.00 51.51 ? 537 ASP A C 1 ATOM 4083 O O . ASP A 1 523 ? 94.876 80.934 35.125 1.00 53.13 ? 537 ASP A O 1 ATOM 4084 C CB . ASP A 1 523 ? 96.366 83.462 35.563 1.00 56.58 ? 537 ASP A CB 1 ATOM 4085 C CG . ASP A 1 523 ? 97.268 83.753 34.370 1.00 60.41 ? 537 ASP A CG 1 ATOM 4086 O OD1 . ASP A 1 523 ? 97.032 83.190 33.268 1.00 60.72 ? 537 ASP A OD1 1 ATOM 4087 O OD2 . ASP A 1 523 ? 98.211 84.556 34.535 1.00 60.60 ? 537 ASP A OD2 1 ATOM 4088 N N . HIS A 1 524 ? 94.088 82.006 33.303 1.00 49.46 ? 538 HIS A N 1 ATOM 4089 C CA . HIS A 1 524 ? 93.764 80.801 32.534 1.00 49.58 ? 538 HIS A CA 1 ATOM 4090 C C . HIS A 1 524 ? 94.973 79.869 32.317 1.00 53.52 ? 538 HIS A C 1 ATOM 4091 O O . HIS A 1 524 ? 94.805 78.683 32.014 1.00 53.55 ? 538 HIS A O 1 ATOM 4092 C CB . HIS A 1 524 ? 93.144 81.220 31.193 1.00 51.65 ? 538 HIS A CB 1 ATOM 4093 C CG . HIS A 1 524 ? 92.611 80.084 30.370 1.00 54.77 ? 538 HIS A CG 1 ATOM 4094 N ND1 . HIS A 1 524 ? 93.370 79.430 29.422 1.00 56.49 ? 538 HIS A ND1 1 ATOM 4095 C CD2 . HIS A 1 524 ? 91.383 79.511 30.330 1.00 55.62 ? 538 HIS A CD2 1 ATOM 4096 C CE1 . HIS A 1 524 ? 92.639 78.490 28.847 1.00 57.54 ? 538 HIS A CE1 1 ATOM 4097 N NE2 . HIS A 1 524 ? 91.430 78.518 29.381 1.00 58.03 ? 538 HIS A NE2 1 ATOM 4098 N N . HIS A 1 525 ? 96.182 80.402 32.482 1.00 54.70 ? 539 HIS A N 1 ATOM 4099 C CA . HIS A 1 525 ? 97.397 79.600 32.362 1.00 61.51 ? 539 HIS A CA 1 ATOM 4100 C C . HIS A 1 525 ? 97.698 78.768 33.606 1.00 62.27 ? 539 HIS A C 1 ATOM 4101 O O . HIS A 1 525 ? 98.539 77.865 33.548 1.00 65.39 ? 539 HIS A O 1 ATOM 4102 C CB . HIS A 1 525 ? 98.610 80.482 32.067 1.00 65.78 ? 539 HIS A CB 1 ATOM 4103 C CG . HIS A 1 525 ? 98.553 81.166 30.742 1.00 68.97 ? 539 HIS A CG 1 ATOM 4104 N ND1 . HIS A 1 525 ? 98.047 82.439 30.586 1.00 70.14 ? 539 HIS A ND1 1 ATOM 4105 C CD2 . HIS A 1 525 ? 98.940 80.759 29.509 1.00 71.30 ? 539 HIS A CD2 1 ATOM 4106 C CE1 . HIS A 1 525 ? 98.123 82.785 29.311 1.00 72.42 ? 539 HIS A CE1 1 ATOM 4107 N NE2 . HIS A 1 525 ? 98.660 81.782 28.637 1.00 71.61 ? 539 HIS A NE2 1 ATOM 4108 N N . TRP A 1 526 ? 97.046 79.086 34.727 1.00 57.50 ? 540 TRP A N 1 ATOM 4109 C CA . TRP A 1 526 ? 97.274 78.350 35.968 1.00 56.69 ? 540 TRP A CA 1 ATOM 4110 C C . TRP A 1 526 ? 97.064 76.861 35.741 1.00 60.45 ? 540 TRP A C 1 ATOM 4111 O O . TRP A 1 526 ? 96.118 76.462 35.060 1.00 59.88 ? 540 TRP A O 1 ATOM 4112 C CB . TRP A 1 526 ? 96.327 78.835 37.060 1.00 56.11 ? 540 TRP A CB 1 ATOM 4113 C CG . TRP A 1 526 ? 96.726 80.130 37.672 1.00 55.27 ? 540 TRP A CG 1 ATOM 4114 C CD1 . TRP A 1 526 ? 97.950 80.735 37.595 1.00 59.01 ? 540 TRP A CD1 1 ATOM 4115 C CD2 . TRP A 1 526 ? 95.898 80.991 38.459 1.00 54.99 ? 540 TRP A CD2 1 ATOM 4116 N NE1 . TRP A 1 526 ? 97.931 81.921 38.294 1.00 59.20 ? 540 TRP A NE1 1 ATOM 4117 C CE2 . TRP A 1 526 ? 96.683 82.098 38.836 1.00 55.94 ? 540 TRP A CE2 1 ATOM 4118 C CE3 . TRP A 1 526 ? 94.571 80.928 38.894 1.00 53.58 ? 540 TRP A CE3 1 ATOM 4119 C CZ2 . TRP A 1 526 ? 96.180 83.139 39.628 1.00 54.86 ? 540 TRP A CZ2 1 ATOM 4120 C CZ3 . TRP A 1 526 ? 94.075 81.959 39.675 1.00 52.22 ? 540 TRP A CZ3 1 ATOM 4121 C CH2 . TRP A 1 526 ? 94.879 83.047 40.036 1.00 53.28 ? 540 TRP A CH2 1 ATOM 4122 N N . THR A 1 527 ? 97.952 76.038 36.288 1.00 64.67 ? 541 THR A N 1 ATOM 4123 C CA . THR A 1 527 ? 97.843 74.592 36.109 1.00 66.22 ? 541 THR A CA 1 ATOM 4124 C C . THR A 1 527 ? 97.924 73.859 37.451 1.00 66.85 ? 541 THR A C 1 ATOM 4125 O O . THR A 1 527 ? 97.246 72.852 37.661 1.00 68.34 ? 541 THR A O 1 ATOM 4126 C CB . THR A 1 527 ? 98.875 74.049 35.081 1.00 65.66 ? 541 THR A CB 1 ATOM 4127 O OG1 . THR A 1 527 ? 98.816 72.618 35.043 1.00 66.31 ? 541 THR A OG1 1 ATOM 4128 C CG2 . THR A 1 527 ? 100.292 74.490 35.440 1.00 68.36 ? 541 THR A CG2 1 ATOM 4129 N N . ASN A 1 528 ? 98.743 74.373 38.360 1.00 67.89 ? 542 ASN A N 1 ATOM 4130 C CA . ASN A 1 528 ? 98.745 73.880 39.731 1.00 72.59 ? 542 ASN A CA 1 ATOM 4131 C C . ASN A 1 528 ? 98.201 74.949 40.656 1.00 66.47 ? 542 ASN A C 1 ATOM 4132 O O . ASN A 1 528 ? 98.700 76.076 40.669 1.00 66.35 ? 542 ASN A O 1 ATOM 4133 C CB . ASN A 1 528 ? 100.154 73.505 40.180 1.00 83.81 ? 542 ASN A CB 1 ATOM 4134 C CG . ASN A 1 528 ? 100.745 72.390 39.365 1.00 93.71 ? 542 ASN A CG 1 ATOM 4135 O OD1 . ASN A 1 528 ? 100.038 71.473 38.932 1.00 91.42 ? 542 ASN A OD1 1 ATOM 4136 N ND2 . ASN A 1 528 ? 102.056 72.460 39.148 1.00 106.44 ? 542 ASN A ND2 1 ATOM 4137 N N . MET A 1 529 ? 97.190 74.606 41.443 1.00 61.07 ? 543 MET A N 1 ATOM 4138 C CA . MET A 1 529 ? 96.547 75.622 42.255 1.00 58.46 ? 543 MET A CA 1 ATOM 4139 C C . MET A 1 529 ? 95.832 75.074 43.473 1.00 58.87 ? 543 MET A C 1 ATOM 4140 O O . MET A 1 529 ? 95.352 73.933 43.481 1.00 59.66 ? 543 MET A O 1 ATOM 4141 C CB . MET A 1 529 ? 95.555 76.398 41.397 1.00 57.24 ? 543 MET A CB 1 ATOM 4142 C CG . MET A 1 529 ? 94.362 75.568 40.935 1.00 58.28 ? 543 MET A CG 1 ATOM 4143 S SD . MET A 1 529 ? 93.684 76.271 39.425 1.00 64.90 ? 543 MET A SD 1 ATOM 4144 C CE . MET A 1 529 ? 93.262 77.895 40.039 1.00 70.46 ? 543 MET A CE 1 ATOM 4145 N N . THR A 1 530 ? 95.772 75.907 44.506 1.00 59.84 ? 544 THR A N 1 ATOM 4146 C CA . THR A 1 530 ? 94.960 75.624 45.677 1.00 59.50 ? 544 THR A CA 1 ATOM 4147 C C . THR A 1 530 ? 93.925 76.734 45.827 1.00 58.03 ? 544 THR A C 1 ATOM 4148 O O . THR A 1 530 ? 94.263 77.926 45.898 1.00 59.32 ? 544 THR A O 1 ATOM 4149 C CB . THR A 1 530 ? 95.811 75.521 46.945 1.00 59.57 ? 544 THR A CB 1 ATOM 4150 O OG1 . THR A 1 530 ? 96.801 74.508 46.757 1.00 61.30 ? 544 THR A OG1 1 ATOM 4151 C CG2 . THR A 1 530 ? 94.939 75.141 48.129 1.00 62.54 ? 544 THR A CG2 1 ATOM 4152 N N . VAL A 1 531 ? 92.657 76.344 45.851 1.00 54.27 ? 545 VAL A N 1 ATOM 4153 C CA . VAL A 1 531 ? 91.582 77.310 45.987 1.00 53.31 ? 545 VAL A CA 1 ATOM 4154 C C . VAL A 1 531 ? 90.849 77.063 47.291 1.00 53.84 ? 545 VAL A C 1 ATOM 4155 O O . VAL A 1 531 ? 90.545 75.913 47.627 1.00 54.34 ? 545 VAL A O 1 ATOM 4156 C CB . VAL A 1 531 ? 90.611 77.224 44.802 1.00 50.72 ? 545 VAL A CB 1 ATOM 4157 C CG1 . VAL A 1 531 ? 89.414 78.132 45.015 1.00 48.46 ? 545 VAL A CG1 1 ATOM 4158 C CG2 . VAL A 1 531 ? 91.345 77.588 43.499 1.00 50.00 ? 545 VAL A CG2 1 ATOM 4159 N N . GLN A 1 532 ? 90.583 78.136 48.034 1.00 52.66 ? 546 GLN A N 1 ATOM 4160 C CA . GLN A 1 532 ? 89.846 78.021 49.286 1.00 53.82 ? 546 GLN A CA 1 ATOM 4161 C C . GLN A 1 532 ? 88.747 79.072 49.384 1.00 53.59 ? 546 GLN A C 1 ATOM 4162 O O . GLN A 1 532 ? 88.907 80.200 48.902 1.00 51.71 ? 546 GLN A O 1 ATOM 4163 C CB . GLN A 1 532 ? 90.792 78.134 50.484 1.00 54.47 ? 546 GLN A CB 1 ATOM 4164 C CG . GLN A 1 532 ? 90.120 77.901 51.822 1.00 57.45 ? 546 GLN A CG 1 ATOM 4165 C CD . GLN A 1 532 ? 91.103 77.877 52.970 1.00 64.81 ? 546 GLN A CD 1 ATOM 4166 O OE1 . GLN A 1 532 ? 91.844 76.908 53.146 1.00 68.82 ? 546 GLN A OE1 1 ATOM 4167 N NE2 . GLN A 1 532 ? 91.116 78.944 53.762 1.00 65.84 ? 546 GLN A NE2 1 ATOM 4168 N N . CYS A 1 533 ? 87.637 78.698 50.018 1.00 53.52 ? 547 CYS A N 1 ATOM 4169 C CA . CYS A 1 533 ? 86.507 79.605 50.187 1.00 50.18 ? 547 CYS A CA 1 ATOM 4170 C C . CYS A 1 533 ? 85.553 79.104 51.265 1.00 48.38 ? 547 CYS A C 1 ATOM 4171 O O . CYS A 1 533 ? 85.346 77.897 51.417 1.00 48.27 ? 547 CYS A O 1 ATOM 4172 C CB . CYS A 1 533 ? 85.741 79.746 48.861 1.00 48.77 ? 547 CYS A CB 1 ATOM 4173 S SG . CYS A 1 533 ? 84.655 81.191 48.754 1.00 51.07 ? 547 CYS A SG 1 ATOM 4174 N N . ASP A 1 534 ? 84.969 80.033 52.011 1.00 50.66 ? 548 ASP A N 1 ATOM 4175 C CA . ASP A 1 534 ? 83.870 79.690 52.898 1.00 53.60 ? 548 ASP A CA 1 ATOM 4176 C C . ASP A 1 534 ? 82.598 79.696 52.071 1.00 53.17 ? 548 ASP A C 1 ATOM 4177 O O . ASP A 1 534 ? 82.346 80.652 51.338 1.00 56.56 ? 548 ASP A O 1 ATOM 4178 C CB . ASP A 1 534 ? 83.771 80.692 54.045 1.00 53.02 ? 548 ASP A CB 1 ATOM 4179 C CG . ASP A 1 534 ? 85.007 80.686 54.927 1.00 60.47 ? 548 ASP A CG 1 ATOM 4180 O OD1 . ASP A 1 534 ? 85.777 79.696 54.879 1.00 61.15 ? 548 ASP A OD1 1 ATOM 4181 O OD2 . ASP A 1 534 ? 85.217 81.674 55.665 1.00 62.42 ? 548 ASP A OD2 1 ATOM 4182 N N . VAL A 1 535 ? 81.807 78.630 52.162 1.00 51.23 ? 549 VAL A N 1 ATOM 4183 C CA . VAL A 1 535 ? 80.579 78.539 51.373 1.00 49.42 ? 549 VAL A CA 1 ATOM 4184 C C . VAL A 1 535 ? 79.358 78.367 52.280 1.00 47.53 ? 549 VAL A C 1 ATOM 4185 O O . VAL A 1 535 ? 79.490 77.910 53.417 1.00 51.87 ? 549 VAL A O 1 ATOM 4186 C CB . VAL A 1 535 ? 80.661 77.411 50.301 1.00 44.09 ? 549 VAL A CB 1 ATOM 4187 C CG1 . VAL A 1 535 ? 81.880 77.608 49.422 1.00 44.01 ? 549 VAL A CG1 1 ATOM 4188 C CG2 . VAL A 1 535 ? 80.737 76.045 50.959 1.00 44.92 ? 549 VAL A CG2 1 ATOM 4189 N N . TYR A 1 536 ? 78.179 78.742 51.779 1.00 47.55 ? 550 TYR A N 1 ATOM 4190 C CA . TYR A 1 536 ? 76.938 78.751 52.569 1.00 46.08 ? 550 TYR A CA 1 ATOM 4191 C C . TYR A 1 536 ? 75.721 78.488 51.661 1.00 46.12 ? 550 TYR A C 1 ATOM 4192 O O . TYR A 1 536 ? 75.408 79.285 50.772 1.00 46.52 ? 550 TYR A O 1 ATOM 4193 C CB . TYR A 1 536 ? 76.803 80.099 53.281 1.00 44.65 ? 550 TYR A CB 1 ATOM 4194 C CG . TYR A 1 536 ? 75.627 80.255 54.233 1.00 46.58 ? 550 TYR A CG 1 ATOM 4195 C CD1 . TYR A 1 536 ? 75.744 79.911 55.572 1.00 46.56 ? 550 TYR A CD1 1 ATOM 4196 C CD2 . TYR A 1 536 ? 74.419 80.789 53.802 1.00 47.18 ? 550 TYR A CD2 1 ATOM 4197 C CE1 . TYR A 1 536 ? 74.686 80.075 56.467 1.00 47.21 ? 550 TYR A CE1 1 ATOM 4198 C CE2 . TYR A 1 536 ? 73.347 80.960 54.683 1.00 51.17 ? 550 TYR A CE2 1 ATOM 4199 C CZ . TYR A 1 536 ? 73.491 80.599 56.019 1.00 51.92 ? 550 TYR A CZ 1 ATOM 4200 O OH . TYR A 1 536 ? 72.444 80.760 56.898 1.00 49.92 ? 550 TYR A OH 1 ATOM 4201 N N . ILE A 1 537 ? 75.053 77.360 51.889 1.00 44.81 ? 551 ILE A N 1 ATOM 4202 C CA . ILE A 1 537 ? 73.915 76.930 51.076 1.00 45.99 ? 551 ILE A CA 1 ATOM 4203 C C . ILE A 1 537 ? 72.603 77.421 51.696 1.00 45.07 ? 551 ILE A C 1 ATOM 4204 O O . ILE A 1 537 ? 72.324 77.129 52.865 1.00 44.44 ? 551 ILE A O 1 ATOM 4205 C CB . ILE A 1 537 ? 73.875 75.390 50.975 1.00 44.22 ? 551 ILE A CB 1 ATOM 4206 C CG1 . ILE A 1 537 ? 75.158 74.866 50.325 1.00 45.85 ? 551 ILE A CG1 1 ATOM 4207 C CG2 . ILE A 1 537 ? 72.637 74.925 50.217 1.00 41.85 ? 551 ILE A CG2 1 ATOM 4208 C CD1 . ILE A 1 537 ? 75.442 73.399 50.622 1.00 46.70 ? 551 ILE A CD1 1 ATOM 4209 N N . GLU A 1 538 ? 71.796 78.156 50.932 1.00 42.39 ? 552 GLU A N 1 ATOM 4210 C CA . GLU A 1 538 ? 70.570 78.731 51.508 1.00 47.14 ? 552 GLU A CA 1 ATOM 4211 C C . GLU A 1 538 ? 69.315 77.855 51.389 1.00 48.46 ? 552 GLU A C 1 ATOM 4212 O O . GLU A 1 538 ? 68.362 78.020 52.157 1.00 52.73 ? 552 GLU A O 1 ATOM 4213 C CB . GLU A 1 538 ? 70.309 80.155 50.978 1.00 48.63 ? 552 GLU A CB 1 ATOM 4214 C CG . GLU A 1 538 ? 71.483 81.122 51.235 1.00 49.54 ? 552 GLU A CG 1 ATOM 4215 C CD . GLU A 1 538 ? 71.127 82.603 51.069 1.00 49.45 ? 552 GLU A CD 1 ATOM 4216 O OE1 . GLU A 1 538 ? 69.916 82.947 51.100 1.00 47.53 ? 552 GLU A OE1 1 ATOM 4217 O OE2 . GLU A 1 538 ? 72.071 83.424 50.920 1.00 50.74 ? 552 GLU A OE2 1 ATOM 4218 N N . THR A 1 539 ? 69.330 76.909 50.454 1.00 47.35 ? 553 THR A N 1 ATOM 4219 C CA . THR A 1 539 ? 68.145 76.103 50.152 1.00 49.42 ? 553 THR A CA 1 ATOM 4220 C C . THR A 1 539 ? 68.217 74.708 50.796 1.00 52.02 ? 553 THR A C 1 ATOM 4221 O O . THR A 1 539 ? 69.112 73.916 50.493 1.00 48.40 ? 553 THR A O 1 ATOM 4222 C CB . THR A 1 539 ? 67.964 75.987 48.635 1.00 48.17 ? 553 THR A CB 1 ATOM 4223 O OG1 . THR A 1 539 ? 68.167 77.279 48.045 1.00 50.89 ? 553 THR A OG1 1 ATOM 4224 C CG2 . THR A 1 539 ? 66.588 75.477 48.289 1.00 48.14 ? 553 THR A CG2 1 ATOM 4225 N N . PRO A 1 540 ? 67.269 74.406 51.696 1.00 55.94 ? 554 PRO A N 1 ATOM 4226 C CA . PRO A 1 540 ? 67.287 73.138 52.439 1.00 60.17 ? 554 PRO A CA 1 ATOM 4227 C C . PRO A 1 540 ? 67.172 71.917 51.530 1.00 60.65 ? 554 PRO A C 1 ATOM 4228 O O . PRO A 1 540 ? 66.479 71.974 50.508 1.00 59.87 ? 554 PRO A O 1 ATOM 4229 C CB . PRO A 1 540 ? 66.049 73.242 53.341 1.00 61.04 ? 554 PRO A CB 1 ATOM 4230 C CG . PRO A 1 540 ? 65.809 74.717 53.483 1.00 61.29 ? 554 PRO A CG 1 ATOM 4231 C CD . PRO A 1 540 ? 66.168 75.283 52.128 1.00 57.28 ? 554 PRO A CD 1 ATOM 4232 N N . ARG A 1 541 ? 67.875 70.844 51.890 1.00 59.64 ? 555 ARG A N 1 ATOM 4233 C CA . ARG A 1 541 ? 67.761 69.556 51.202 1.00 60.33 ? 555 ARG A CA 1 ATOM 4234 C C . ARG A 1 541 ? 68.288 69.534 49.754 1.00 57.18 ? 555 ARG A C 1 ATOM 4235 O O . ARG A 1 541 ? 69.042 68.631 49.389 1.00 56.15 ? 555 ARG A O 1 ATOM 4236 C CB . ARG A 1 541 ? 66.315 69.034 51.263 1.00 64.12 ? 555 ARG A CB 1 ATOM 4237 C CG . ARG A 1 541 ? 65.715 69.009 52.675 1.00 72.31 ? 555 ARG A CG 1 ATOM 4238 C CD . ARG A 1 541 ? 64.204 68.741 52.660 1.00 79.71 ? 555 ARG A CD 1 ATOM 4239 N NE . ARG A 1 541 ? 63.460 69.770 51.927 1.00 83.91 ? 555 ARG A NE 1 ATOM 4240 C CZ . ARG A 1 541 ? 62.754 70.747 52.497 1.00 85.13 ? 555 ARG A CZ 1 ATOM 4241 N NH1 . ARG A 1 541 ? 62.676 70.839 53.822 1.00 86.98 ? 555 ARG A NH1 1 ATOM 4242 N NH2 . ARG A 1 541 ? 62.120 71.633 51.737 1.00 82.59 ? 555 ARG A NH2 1 ATOM 4243 N N . SER A 1 542 ? 67.903 70.520 48.940 1.00 53.07 ? 556 SER A N 1 ATOM 4244 C CA . SER A 1 542 ? 68.214 70.501 47.505 1.00 47.41 ? 556 SER A CA 1 ATOM 4245 C C . SER A 1 542 ? 69.439 71.311 47.104 1.00 46.54 ? 556 SER A C 1 ATOM 4246 O O . SER A 1 542 ? 69.936 71.163 45.985 1.00 45.34 ? 556 SER A O 1 ATOM 4247 C CB . SER A 1 542 ? 67.011 70.984 46.678 1.00 48.68 ? 556 SER A CB 1 ATOM 4248 O OG . SER A 1 542 ? 66.590 72.276 47.089 1.00 49.64 ? 556 SER A OG 1 ATOM 4249 N N . GLY A 1 543 ? 69.937 72.154 48.009 1.00 45.64 ? 557 GLY A N 1 ATOM 4250 C CA . GLY A 1 543 ? 71.000 73.090 47.666 1.00 40.10 ? 557 GLY A CA 1 ATOM 4251 C C . GLY A 1 543 ? 72.387 72.513 47.452 1.00 46.52 ? 557 GLY A C 1 ATOM 4252 O O . GLY A 1 543 ? 72.754 71.485 48.039 1.00 49.61 ? 557 GLY A O 1 ATOM 4253 N N . GLY A 1 544 ? 73.178 73.198 46.628 1.00 44.67 ? 558 GLY A N 1 ATOM 4254 C CA . GLY A 1 544 ? 74.535 72.774 46.341 1.00 40.29 ? 558 GLY A CA 1 ATOM 4255 C C . GLY A 1 544 ? 75.452 73.898 45.888 1.00 46.29 ? 558 GLY A C 1 ATOM 4256 O O . GLY A 1 544 ? 75.026 74.831 45.201 1.00 43.85 ? 558 GLY A O 1 ATOM 4257 N N . VAL A 1 545 ? 76.724 73.807 46.272 1.00 45.16 ? 559 VAL A N 1 ATOM 4258 C CA . VAL A 1 545 ? 77.722 74.774 45.842 1.00 40.51 ? 559 VAL A CA 1 ATOM 4259 C C . VAL A 1 545 ? 79.004 74.057 45.451 1.00 42.65 ? 559 VAL A C 1 ATOM 4260 O O . VAL A 1 545 ? 79.172 72.869 45.728 1.00 43.67 ? 559 VAL A O 1 ATOM 4261 C CB . VAL A 1 545 ? 78.058 75.809 46.944 1.00 41.03 ? 559 VAL A CB 1 ATOM 4262 C CG1 . VAL A 1 545 ? 76.863 76.688 47.244 1.00 42.89 ? 559 VAL A CG1 1 ATOM 4263 C CG2 . VAL A 1 545 ? 78.540 75.119 48.205 1.00 42.24 ? 559 VAL A CG2 1 ATOM 4264 N N . PHE A 1 546 ? 79.917 74.783 44.817 1.00 43.74 ? 560 PHE A N 1 ATOM 4265 C CA . PHE A 1 546 ? 81.207 74.219 44.455 1.00 44.09 ? 560 PHE A CA 1 ATOM 4266 C C . PHE A 1 546 ? 82.286 75.275 44.440 1.00 44.64 ? 560 PHE A C 1 ATOM 4267 O O . PHE A 1 546 ? 81.996 76.477 44.405 1.00 44.24 ? 560 PHE A O 1 ATOM 4268 C CB . PHE A 1 546 ? 81.156 73.550 43.069 1.00 47.05 ? 560 PHE A CB 1 ATOM 4269 C CG . PHE A 1 546 ? 80.960 74.514 41.921 1.00 45.86 ? 560 PHE A CG 1 ATOM 4270 C CD1 . PHE A 1 546 ? 82.050 75.150 41.317 1.00 44.95 ? 560 PHE A CD1 1 ATOM 4271 C CD2 . PHE A 1 546 ? 79.685 74.764 41.426 1.00 43.65 ? 560 PHE A CD2 1 ATOM 4272 C CE1 . PHE A 1 546 ? 81.862 76.030 40.252 1.00 44.71 ? 560 PHE A CE1 1 ATOM 4273 C CE2 . PHE A 1 546 ? 79.489 75.634 40.356 1.00 42.47 ? 560 PHE A CE2 1 ATOM 4274 C CZ . PHE A 1 546 ? 80.574 76.269 39.767 1.00 38.79 ? 560 PHE A CZ 1 ATOM 4275 N N . ILE A 1 547 ? 83.533 74.808 44.484 1.00 42.76 ? 561 ILE A N 1 ATOM 4276 C CA . ILE A 1 547 ? 84.675 75.614 44.097 1.00 51.59 ? 561 ILE A CA 1 ATOM 4277 C C . ILE A 1 547 ? 85.410 74.811 43.025 1.00 49.49 ? 561 ILE A C 1 ATOM 4278 O O . ILE A 1 547 ? 85.288 73.581 42.975 1.00 48.00 ? 561 ILE A O 1 ATOM 4279 C CB . ILE A 1 547 ? 85.605 75.933 45.295 1.00 51.75 ? 561 ILE A CB 1 ATOM 4280 C CG1 . ILE A 1 547 ? 86.151 74.646 45.926 1.00 45.15 ? 561 ILE A CG1 1 ATOM 4281 C CG2 . ILE A 1 547 ? 84.870 76.794 46.310 1.00 49.26 ? 561 ILE A CG2 1 ATOM 4282 C CD1 . ILE A 1 547 ? 87.222 74.892 47.029 1.00 46.35 ? 561 ILE A CD1 1 ATOM 4283 N N . ALA A 1 548 ? 86.153 75.488 42.158 1.00 48.11 ? 562 ALA A N 1 ATOM 4284 C CA . ALA A 1 548 ? 86.783 74.789 41.038 1.00 51.60 ? 562 ALA A CA 1 ATOM 4285 C C . ALA A 1 548 ? 88.129 75.377 40.641 1.00 50.60 ? 562 ALA A C 1 ATOM 4286 O O . ALA A 1 548 ? 88.445 76.517 40.987 1.00 48.21 ? 562 ALA A O 1 ATOM 4287 C CB . ALA A 1 548 ? 85.844 74.762 39.831 1.00 42.62 ? 562 ALA A CB 1 ATOM 4288 N N . GLY A 1 549 ? 88.904 74.587 39.898 1.00 52.33 ? 563 GLY A N 1 ATOM 4289 C CA . GLY A 1 549 ? 90.177 75.024 39.340 1.00 54.08 ? 563 GLY A CA 1 ATOM 4290 C C . GLY A 1 549 ? 90.374 74.434 37.950 1.00 53.02 ? 563 GLY A C 1 ATOM 4291 O O . GLY A 1 549 ? 89.655 73.498 37.561 1.00 46.99 ? 563 GLY A O 1 ATOM 4292 N N . ARG A 1 550 ? 91.341 74.969 37.205 1.00 53.67 ? 564 ARG A N 1 ATOM 4293 C CA . ARG A 1 550 ? 91.537 74.590 35.805 1.00 52.40 ? 564 ARG A CA 1 ATOM 4294 C C . ARG A 1 550 ? 90.262 74.736 34.958 1.00 53.76 ? 564 ARG A C 1 ATOM 4295 O O . ARG A 1 550 ? 90.004 73.926 34.058 1.00 50.88 ? 564 ARG A O 1 ATOM 4296 C CB . ARG A 1 550 ? 92.094 73.162 35.696 1.00 53.56 ? 564 ARG A CB 1 ATOM 4297 C CG . ARG A 1 550 ? 93.527 73.015 36.203 1.00 56.04 ? 564 ARG A CG 1 ATOM 4298 C CD . ARG A 1 550 ? 93.986 71.557 36.171 1.00 56.53 ? 564 ARG A CD 1 ATOM 4299 N NE . ARG A 1 550 ? 95.295 71.371 36.804 1.00 55.40 ? 564 ARG A NE 1 ATOM 4300 C CZ . ARG A 1 550 ? 95.850 70.185 37.043 1.00 56.38 ? 564 ARG A CZ 1 ATOM 4301 N NH1 . ARG A 1 550 ? 95.204 69.074 36.718 1.00 57.52 ? 564 ARG A NH1 1 ATOM 4302 N NH2 . ARG A 1 550 ? 97.043 70.106 37.622 1.00 57.39 ? 564 ARG A NH2 1 ATOM 4303 N N . VAL A 1 551 ? 89.459 75.762 35.232 1.00 51.98 ? 565 VAL A N 1 ATOM 4304 C CA . VAL A 1 551 ? 88.255 75.984 34.420 1.00 50.62 ? 565 VAL A CA 1 ATOM 4305 C C . VAL A 1 551 ? 88.646 76.640 33.085 1.00 51.61 ? 565 VAL A C 1 ATOM 4306 O O . VAL A 1 551 ? 89.174 77.753 33.067 1.00 49.16 ? 565 VAL A O 1 ATOM 4307 C CB . VAL A 1 551 ? 87.202 76.813 35.181 1.00 46.05 ? 565 VAL A CB 1 ATOM 4308 C CG1 . VAL A 1 551 ? 85.965 77.028 34.327 1.00 41.27 ? 565 VAL A CG1 1 ATOM 4309 C CG2 . VAL A 1 551 ? 86.835 76.114 36.492 1.00 44.88 ? 565 VAL A CG2 1 ATOM 4310 N N . ASN A 1 552 ? 88.380 75.957 31.973 1.00 53.16 ? 566 ASN A N 1 ATOM 4311 C CA . ASN A 1 552 ? 89.060 76.280 30.711 1.00 56.19 ? 566 ASN A CA 1 ATOM 4312 C C . ASN A 1 552 ? 88.285 77.123 29.695 1.00 54.60 ? 566 ASN A C 1 ATOM 4313 O O . ASN A 1 552 ? 88.883 77.710 28.783 1.00 55.88 ? 566 ASN A O 1 ATOM 4314 C CB . ASN A 1 552 ? 89.537 74.995 30.033 1.00 58.39 ? 566 ASN A CB 1 ATOM 4315 C CG . ASN A 1 552 ? 88.402 74.036 29.731 1.00 62.90 ? 566 ASN A CG 1 ATOM 4316 O OD1 . ASN A 1 552 ? 87.223 74.348 29.940 1.00 60.07 ? 566 ASN A OD1 1 ATOM 4317 N ND2 . ASN A 1 552 ? 88.753 72.863 29.213 1.00 69.50 ? 566 ASN A ND2 1 ATOM 4318 N N . LYS A 1 553 ? 86.963 77.166 29.844 1.00 52.98 ? 567 LYS A N 1 ATOM 4319 C CA . LYS A 1 553 ? 86.106 77.883 28.909 1.00 49.97 ? 567 LYS A CA 1 ATOM 4320 C C . LYS A 1 553 ? 85.069 78.668 29.685 1.00 49.20 ? 567 LYS A C 1 ATOM 4321 O O . LYS A 1 553 ? 84.680 78.265 30.784 1.00 52.07 ? 567 LYS A O 1 ATOM 4322 C CB . LYS A 1 553 ? 85.401 76.891 27.973 1.00 50.85 ? 567 LYS A CB 1 ATOM 4323 C CG . LYS A 1 553 ? 86.305 76.253 26.924 1.00 59.31 ? 567 LYS A CG 1 ATOM 4324 C CD . LYS A 1 553 ? 86.793 77.290 25.910 1.00 66.07 ? 567 LYS A CD 1 ATOM 4325 C CE . LYS A 1 553 ? 87.902 76.756 24.999 1.00 70.21 ? 567 LYS A CE 1 ATOM 4326 N NZ . LYS A 1 553 ? 89.222 76.692 25.707 1.00 73.39 ? 567 LYS A NZ 1 ATOM 4327 N N . GLY A 1 554 ? 84.631 79.793 29.130 1.00 45.96 ? 568 GLY A N 1 ATOM 4328 C CA . GLY A 1 554 ? 83.485 80.510 29.664 1.00 42.10 ? 568 GLY A CA 1 ATOM 4329 C C . GLY A 1 554 ? 82.797 81.277 28.557 1.00 45.13 ? 568 GLY A C 1 ATOM 4330 O O . GLY A 1 554 ? 82.991 80.971 27.368 1.00 46.52 ? 568 GLY A O 1 ATOM 4331 N N . GLY A 1 555 ? 81.998 82.274 28.922 1.00 39.95 ? 569 GLY A N 1 ATOM 4332 C CA . GLY A 1 555 ? 81.327 83.080 27.919 1.00 38.59 ? 569 GLY A CA 1 ATOM 4333 C C . GLY A 1 555 ? 80.228 82.302 27.220 1.00 41.30 ? 569 GLY A C 1 ATOM 4334 O O . GLY A 1 555 ? 79.461 81.590 27.869 1.00 36.89 ? 569 GLY A O 1 ATOM 4335 N N . ILE A 1 556 ? 80.127 82.425 25.898 1.00 44.51 ? 570 ILE A N 1 ATOM 4336 C CA . ILE A 1 556 ? 79.090 81.669 25.209 1.00 47.26 ? 570 ILE A CA 1 ATOM 4337 C C . ILE A 1 556 ? 79.368 80.167 25.250 1.00 45.71 ? 570 ILE A C 1 ATOM 4338 O O . ILE A 1 556 ? 78.473 79.377 25.006 1.00 36.37 ? 570 ILE A O 1 ATOM 4339 C CB . ILE A 1 556 ? 78.883 82.118 23.763 1.00 52.62 ? 570 ILE A CB 1 ATOM 4340 C CG1 . ILE A 1 556 ? 80.217 82.475 23.116 1.00 51.37 ? 570 ILE A CG1 1 ATOM 4341 C CG2 . ILE A 1 556 ? 77.922 83.306 23.690 1.00 55.88 ? 570 ILE A CG2 1 ATOM 4342 C CD1 . ILE A 1 556 ? 80.065 82.849 21.678 1.00 54.54 ? 570 ILE A CD1 1 ATOM 4343 N N . LEU A 1 557 ? 80.600 79.780 25.576 1.00 44.87 ? 571 LEU A N 1 ATOM 4344 C CA . LEU A 1 557 ? 80.943 78.364 25.695 1.00 45.21 ? 571 LEU A CA 1 ATOM 4345 C C . LEU A 1 557 ? 80.952 77.834 27.141 1.00 45.70 ? 571 LEU A C 1 ATOM 4346 O O . LEU A 1 557 ? 81.552 76.786 27.397 1.00 48.88 ? 571 LEU A O 1 ATOM 4347 C CB . LEU A 1 557 ? 82.313 78.092 25.065 1.00 45.18 ? 571 LEU A CB 1 ATOM 4348 C CG . LEU A 1 557 ? 82.548 78.429 23.593 1.00 51.14 ? 571 LEU A CG 1 ATOM 4349 C CD1 . LEU A 1 557 ? 83.919 77.896 23.125 1.00 55.52 ? 571 LEU A CD1 1 ATOM 4350 C CD2 . LEU A 1 557 ? 81.437 77.891 22.710 1.00 50.94 ? 571 LEU A CD2 1 ATOM 4351 N N . ILE A 1 558 ? 80.296 78.527 28.075 1.00 40.46 ? 572 ILE A N 1 ATOM 4352 C CA . ILE A 1 558 ? 80.397 78.173 29.498 1.00 42.73 ? 572 ILE A CA 1 ATOM 4353 C C . ILE A 1 558 ? 79.863 76.757 29.819 1.00 45.70 ? 572 ILE A C 1 ATOM 4354 O O . ILE A 1 558 ? 80.354 76.098 30.729 1.00 48.20 ? 572 ILE A O 1 ATOM 4355 C CB . ILE A 1 558 ? 79.704 79.236 30.396 1.00 41.49 ? 572 ILE A CB 1 ATOM 4356 C CG1 . ILE A 1 558 ? 79.910 78.926 31.890 1.00 40.74 ? 572 ILE A CG1 1 ATOM 4357 C CG2 . ILE A 1 558 ? 78.213 79.329 30.070 1.00 35.44 ? 572 ILE A CG2 1 ATOM 4358 C CD1 . ILE A 1 558 ? 81.361 78.915 32.319 1.00 37.48 ? 572 ILE A CD1 1 ATOM 4359 N N . ARG A 1 559 ? 78.889 76.285 29.045 1.00 44.33 ? 573 ARG A N 1 ATOM 4360 C CA . ARG A 1 559 ? 78.358 74.920 29.197 1.00 46.81 ? 573 ARG A CA 1 ATOM 4361 C C . ARG A 1 559 ? 79.400 73.851 28.888 1.00 48.09 ? 573 ARG A C 1 ATOM 4362 O O . ARG A 1 559 ? 79.249 72.687 29.267 1.00 49.89 ? 573 ARG A O 1 ATOM 4363 C CB . ARG A 1 559 ? 77.152 74.694 28.269 1.00 46.51 ? 573 ARG A CB 1 ATOM 4364 C CG . ARG A 1 559 ? 75.803 74.971 28.915 1.00 47.15 ? 573 ARG A CG 1 ATOM 4365 C CD . ARG A 1 559 ? 74.656 74.381 28.096 1.00 47.85 ? 573 ARG A CD 1 ATOM 4366 N NE . ARG A 1 559 ? 73.412 74.495 28.841 1.00 53.93 ? 573 ARG A NE 1 ATOM 4367 C CZ . ARG A 1 559 ? 72.950 73.561 29.663 1.00 59.28 ? 573 ARG A CZ 1 ATOM 4368 N NH1 . ARG A 1 559 ? 73.620 72.429 29.820 1.00 62.27 ? 573 ARG A NH1 1 ATOM 4369 N NH2 . ARG A 1 559 ? 71.813 73.754 30.321 1.00 62.40 ? 573 ARG A NH2 1 ATOM 4370 N N . SER A 1 560 ? 80.447 74.251 28.181 1.00 49.09 ? 574 SER A N 1 ATOM 4371 C CA . SER A 1 560 ? 81.503 73.338 27.771 1.00 56.06 ? 574 SER A CA 1 ATOM 4372 C C . SER A 1 560 ? 82.659 73.248 28.763 1.00 54.67 ? 574 SER A C 1 ATOM 4373 O O . SER A 1 560 ? 83.623 72.509 28.531 1.00 56.05 ? 574 SER A O 1 ATOM 4374 C CB . SER A 1 560 ? 82.074 73.806 26.435 1.00 61.77 ? 574 SER A CB 1 ATOM 4375 O OG . SER A 1 560 ? 81.032 74.020 25.506 1.00 65.98 ? 574 SER A OG 1 ATOM 4376 N N . ALA A 1 561 ? 82.582 74.015 29.848 1.00 48.90 ? 575 ALA A N 1 ATOM 4377 C CA . ALA A 1 561 ? 83.742 74.169 30.721 1.00 45.59 ? 575 ALA A CA 1 ATOM 4378 C C . ALA A 1 561 ? 84.150 72.850 31.357 1.00 43.33 ? 575 ALA A C 1 ATOM 4379 O O . ALA A 1 561 ? 83.326 72.159 31.951 1.00 45.15 ? 575 ALA A O 1 ATOM 4380 C CB . ALA A 1 561 ? 83.486 75.230 31.792 1.00 41.52 ? 575 ALA A CB 1 ATOM 4381 N N . THR A 1 562 ? 85.417 72.490 31.205 1.00 42.47 ? 576 THR A N 1 ATOM 4382 C CA . THR A 1 562 ? 85.971 71.386 31.969 1.00 45.91 ? 576 THR A CA 1 ATOM 4383 C C . THR A 1 562 ? 86.898 71.948 33.024 1.00 48.17 ? 576 THR A C 1 ATOM 4384 O O . THR A 1 562 ? 87.179 73.158 33.038 1.00 46.17 ? 576 THR A O 1 ATOM 4385 C CB . THR A 1 562 ? 86.726 70.359 31.091 1.00 50.87 ? 576 THR A CB 1 ATOM 4386 O OG1 . THR A 1 562 ? 87.679 71.031 30.271 1.00 55.98 ? 576 THR A OG1 1 ATOM 4387 C CG2 . THR A 1 562 ? 85.769 69.604 30.201 1.00 53.74 ? 576 THR A CG2 1 ATOM 4388 N N . GLY A 1 563 ? 87.375 71.067 33.899 1.00 52.91 ? 577 GLY A N 1 ATOM 4389 C CA . GLY A 1 563 ? 88.255 71.454 34.988 1.00 54.06 ? 577 GLY A CA 1 ATOM 4390 C C . GLY A 1 563 ? 88.161 70.444 36.124 1.00 53.25 ? 577 GLY A C 1 ATOM 4391 O O . GLY A 1 563 ? 87.923 69.253 35.885 1.00 54.74 ? 577 GLY A O 1 ATOM 4392 N N . VAL A 1 564 ? 88.359 70.907 37.358 1.00 48.32 ? 578 VAL A N 1 ATOM 4393 C CA . VAL A 1 564 ? 88.117 70.063 38.526 1.00 47.12 ? 578 VAL A CA 1 ATOM 4394 C C . VAL A 1 564 ? 87.091 70.749 39.425 1.00 47.75 ? 578 VAL A C 1 ATOM 4395 O O . VAL A 1 564 ? 87.334 71.844 39.933 1.00 45.78 ? 578 VAL A O 1 ATOM 4396 C CB . VAL A 1 564 ? 89.416 69.776 39.321 1.00 47.29 ? 578 VAL A CB 1 ATOM 4397 C CG1 . VAL A 1 564 ? 89.159 68.740 40.388 1.00 47.84 ? 578 VAL A CG1 1 ATOM 4398 C CG2 . VAL A 1 564 ? 90.511 69.294 38.381 1.00 53.19 ? 578 VAL A CG2 1 ATOM 4399 N N . PHE A 1 565 ? 85.940 70.112 39.616 1.00 47.84 ? 579 PHE A N 1 ATOM 4400 C CA . PHE A 1 565 ? 84.859 70.738 40.361 1.00 43.65 ? 579 PHE A CA 1 ATOM 4401 C C . PHE A 1 565 ? 84.543 70.003 41.665 1.00 44.18 ? 579 PHE A C 1 ATOM 4402 O O . PHE A 1 565 ? 84.147 68.834 41.642 1.00 46.90 ? 579 PHE A O 1 ATOM 4403 C CB . PHE A 1 565 ? 83.596 70.815 39.491 1.00 42.54 ? 579 PHE A CB 1 ATOM 4404 C CG . PHE A 1 565 ? 83.767 71.617 38.232 1.00 45.72 ? 579 PHE A CG 1 ATOM 4405 C CD1 . PHE A 1 565 ? 84.314 71.031 37.084 1.00 47.34 ? 579 PHE A CD1 1 ATOM 4406 C CD2 . PHE A 1 565 ? 83.364 72.950 38.178 1.00 42.99 ? 579 PHE A CD2 1 ATOM 4407 C CE1 . PHE A 1 565 ? 84.461 71.765 35.899 1.00 42.07 ? 579 PHE A CE1 1 ATOM 4408 C CE2 . PHE A 1 565 ? 83.503 73.695 37.001 1.00 41.60 ? 579 PHE A CE2 1 ATOM 4409 C CZ . PHE A 1 565 ? 84.059 73.097 35.854 1.00 41.23 ? 579 PHE A CZ 1 ATOM 4410 N N . PHE A 1 566 ? 84.689 70.706 42.789 1.00 44.34 ? 580 PHE A N 1 ATOM 4411 C CA . PHE A 1 566 ? 84.443 70.147 44.125 1.00 44.98 ? 580 PHE A CA 1 ATOM 4412 C C . PHE A 1 566 ? 83.073 70.612 44.635 1.00 44.17 ? 580 PHE A C 1 ATOM 4413 O O . PHE A 1 566 ? 82.925 71.746 45.083 1.00 43.80 ? 580 PHE A O 1 ATOM 4414 C CB . PHE A 1 566 ? 85.590 70.572 45.068 1.00 45.94 ? 580 PHE A CB 1 ATOM 4415 C CG . PHE A 1 566 ? 85.511 69.987 46.471 1.00 55.71 ? 580 PHE A CG 1 ATOM 4416 C CD1 . PHE A 1 566 ? 84.632 68.953 46.781 1.00 53.59 ? 580 PHE A CD1 1 ATOM 4417 C CD2 . PHE A 1 566 ? 86.331 70.485 47.479 1.00 56.23 ? 580 PHE A CD2 1 ATOM 4418 C CE1 . PHE A 1 566 ? 84.559 68.437 48.071 1.00 54.85 ? 580 PHE A CE1 1 ATOM 4419 C CE2 . PHE A 1 566 ? 86.272 69.973 48.771 1.00 57.87 ? 580 PHE A CE2 1 ATOM 4420 C CZ . PHE A 1 566 ? 85.387 68.947 49.067 1.00 57.67 ? 580 PHE A CZ 1 ATOM 4421 N N . TRP A 1 567 ? 82.074 69.734 44.551 1.00 46.95 ? 581 TRP A N 1 ATOM 4422 C CA . TRP A 1 567 ? 80.692 70.082 44.912 1.00 47.04 ? 581 TRP A CA 1 ATOM 4423 C C . TRP A 1 567 ? 80.340 69.621 46.320 1.00 51.00 ? 581 TRP A C 1 ATOM 4424 O O . TRP A 1 567 ? 80.773 68.546 46.744 1.00 53.63 ? 581 TRP A O 1 ATOM 4425 C CB . TRP A 1 567 ? 79.701 69.401 43.970 1.00 45.24 ? 581 TRP A CB 1 ATOM 4426 C CG . TRP A 1 567 ? 79.928 69.644 42.498 1.00 47.80 ? 581 TRP A CG 1 ATOM 4427 C CD1 . TRP A 1 567 ? 80.855 69.035 41.705 1.00 48.97 ? 581 TRP A CD1 1 ATOM 4428 C CD2 . TRP A 1 567 ? 79.180 70.526 41.637 1.00 48.10 ? 581 TRP A CD2 1 ATOM 4429 N NE1 . TRP A 1 567 ? 80.749 69.497 40.414 1.00 50.24 ? 581 TRP A NE1 1 ATOM 4430 C CE2 . TRP A 1 567 ? 79.728 70.411 40.345 1.00 48.68 ? 581 TRP A CE2 1 ATOM 4431 C CE3 . TRP A 1 567 ? 78.110 71.410 41.840 1.00 46.65 ? 581 TRP A CE3 1 ATOM 4432 C CZ2 . TRP A 1 567 ? 79.247 71.157 39.254 1.00 46.18 ? 581 TRP A CZ2 1 ATOM 4433 C CZ3 . TRP A 1 567 ? 77.628 72.143 40.755 1.00 44.27 ? 581 TRP A CZ3 1 ATOM 4434 C CH2 . TRP A 1 567 ? 78.198 72.010 39.482 1.00 43.20 ? 581 TRP A CH2 1 ATOM 4435 N N . ILE A 1 568 ? 79.547 70.413 47.042 1.00 48.68 ? 582 ILE A N 1 ATOM 4436 C CA . ILE A 1 568 ? 78.897 69.902 48.252 1.00 44.40 ? 582 ILE A CA 1 ATOM 4437 C C . ILE A 1 568 ? 77.396 70.178 48.234 1.00 44.35 ? 582 ILE A C 1 ATOM 4438 O O . ILE A 1 568 ? 76.940 71.219 47.735 1.00 44.52 ? 582 ILE A O 1 ATOM 4439 C CB . ILE A 1 568 ? 79.553 70.380 49.584 1.00 46.23 ? 582 ILE A CB 1 ATOM 4440 C CG1 . ILE A 1 568 ? 79.538 71.900 49.726 1.00 45.55 ? 582 ILE A CG1 1 ATOM 4441 C CG2 . ILE A 1 568 ? 80.979 69.859 49.715 1.00 46.35 ? 582 ILE A CG2 1 ATOM 4442 C CD1 . ILE A 1 568 ? 79.993 72.353 51.116 1.00 45.87 ? 582 ILE A CD1 1 ATOM 4443 N N . PHE A 1 569 ? 76.625 69.237 48.766 1.00 45.70 ? 583 PHE A N 1 ATOM 4444 C CA . PHE A 1 569 ? 75.167 69.333 48.695 1.00 45.58 ? 583 PHE A CA 1 ATOM 4445 C C . PHE A 1 569 ? 74.527 69.305 50.077 1.00 47.49 ? 583 PHE A C 1 ATOM 4446 O O . PHE A 1 569 ? 75.063 68.698 51.003 1.00 49.23 ? 583 PHE A O 1 ATOM 4447 C CB . PHE A 1 569 ? 74.619 68.207 47.827 1.00 46.34 ? 583 PHE A CB 1 ATOM 4448 C CG . PHE A 1 569 ? 75.060 68.289 46.390 1.00 46.62 ? 583 PHE A CG 1 ATOM 4449 C CD1 . PHE A 1 569 ? 76.295 67.783 45.997 1.00 47.63 ? 583 PHE A CD1 1 ATOM 4450 C CD2 . PHE A 1 569 ? 74.238 68.875 45.432 1.00 45.99 ? 583 PHE A CD2 1 ATOM 4451 C CE1 . PHE A 1 569 ? 76.710 67.857 44.668 1.00 48.16 ? 583 PHE A CE1 1 ATOM 4452 C CE2 . PHE A 1 569 ? 74.642 68.962 44.095 1.00 42.32 ? 583 PHE A CE2 1 ATOM 4453 C CZ . PHE A 1 569 ? 75.880 68.454 43.714 1.00 44.11 ? 583 PHE A CZ 1 ATOM 4454 N N . ALA A 1 570 ? 73.377 69.960 50.209 1.00 50.67 ? 584 ALA A N 1 ATOM 4455 C CA . ALA A 1 570 ? 72.660 70.048 51.485 1.00 53.20 ? 584 ALA A CA 1 ATOM 4456 C C . ALA A 1 570 ? 72.035 68.726 51.936 1.00 54.73 ? 584 ALA A C 1 ATOM 4457 O O . ALA A 1 570 ? 71.474 68.649 53.032 1.00 57.63 ? 584 ALA A O 1 ATOM 4458 C CB . ALA A 1 570 ? 71.588 71.145 51.418 1.00 52.13 ? 584 ALA A CB 1 ATOM 4459 N N . ASN A 1 571 ? 72.100 67.699 51.091 1.00 51.18 ? 585 ASN A N 1 ATOM 4460 C CA . ASN A 1 571 ? 71.588 66.382 51.465 1.00 51.40 ? 585 ASN A CA 1 ATOM 4461 C C . ASN A 1 571 ? 72.676 65.507 52.096 1.00 54.78 ? 585 ASN A C 1 ATOM 4462 O O . ASN A 1 571 ? 72.469 64.318 52.343 1.00 60.80 ? 585 ASN A O 1 ATOM 4463 C CB . ASN A 1 571 ? 70.966 65.687 50.250 1.00 53.14 ? 585 ASN A CB 1 ATOM 4464 C CG . ASN A 1 571 ? 72.013 65.186 49.257 1.00 54.93 ? 585 ASN A CG 1 ATOM 4465 O OD1 . ASN A 1 571 ? 73.137 65.688 49.210 1.00 52.34 ? 585 ASN A OD1 1 ATOM 4466 N ND2 . ASN A 1 571 ? 71.643 64.183 48.462 1.00 56.04 ? 585 ASN A ND2 1 ATOM 4467 N N . GLY A 1 572 ? 73.838 66.102 52.351 1.00 51.41 ? 586 GLY A N 1 ATOM 4468 C CA . GLY A 1 572 ? 74.938 65.383 52.964 1.00 53.26 ? 586 GLY A CA 1 ATOM 4469 C C . GLY A 1 572 ? 75.778 64.570 51.997 1.00 55.10 ? 586 GLY A C 1 ATOM 4470 O O . GLY A 1 572 ? 76.107 63.415 52.272 1.00 58.84 ? 586 GLY A O 1 ATOM 4471 N N . SER A 1 573 ? 76.134 65.167 50.864 1.00 52.82 ? 587 SER A N 1 ATOM 4472 C CA . SER A 1 573 ? 76.932 64.471 49.863 1.00 52.60 ? 587 SER A CA 1 ATOM 4473 C C . SER A 1 573 ? 77.944 65.403 49.203 1.00 52.08 ? 587 SER A C 1 ATOM 4474 O O . SER A 1 573 ? 77.820 66.625 49.289 1.00 50.36 ? 587 SER A O 1 ATOM 4475 C CB . SER A 1 573 ? 76.024 63.857 48.799 1.00 54.41 ? 587 SER A CB 1 ATOM 4476 O OG . SER A 1 573 ? 75.247 64.858 48.156 1.00 54.66 ? 587 SER A OG 1 ATOM 4477 N N . TYR A 1 574 ? 78.954 64.814 48.564 1.00 50.97 ? 588 TYR A N 1 ATOM 4478 C CA . TYR A 1 574 ? 79.886 65.561 47.734 1.00 48.35 ? 588 TYR A CA 1 ATOM 4479 C C . TYR A 1 574 ? 80.122 64.844 46.407 1.00 47.70 ? 588 TYR A C 1 ATOM 4480 O O . TYR A 1 574 ? 79.810 63.666 46.259 1.00 48.42 ? 588 TYR A O 1 ATOM 4481 C CB . TYR A 1 574 ? 81.216 65.793 48.452 1.00 51.79 ? 588 TYR A CB 1 ATOM 4482 C CG . TYR A 1 574 ? 82.160 64.601 48.498 1.00 57.82 ? 588 TYR A CG 1 ATOM 4483 C CD1 . TYR A 1 574 ? 82.032 63.617 49.480 1.00 59.77 ? 588 TYR A CD1 1 ATOM 4484 C CD2 . TYR A 1 574 ? 83.212 64.484 47.588 1.00 59.28 ? 588 TYR A CD2 1 ATOM 4485 C CE1 . TYR A 1 574 ? 82.913 62.542 49.540 1.00 59.65 ? 588 TYR A CE1 1 ATOM 4486 C CE2 . TYR A 1 574 ? 84.095 63.410 47.637 1.00 60.87 ? 588 TYR A CE2 1 ATOM 4487 C CZ . TYR A 1 574 ? 83.940 62.442 48.616 1.00 62.10 ? 588 TYR A CZ 1 ATOM 4488 O OH . TYR A 1 574 ? 84.816 61.376 48.671 1.00 61.52 ? 588 TYR A OH 1 ATOM 4489 N N . ARG A 1 575 ? 80.666 65.572 45.442 1.00 50.08 ? 589 ARG A N 1 ATOM 4490 C CA . ARG A 1 575 ? 81.048 65.005 44.160 1.00 53.73 ? 589 ARG A CA 1 ATOM 4491 C C . ARG A 1 575 ? 82.239 65.775 43.635 1.00 52.59 ? 589 ARG A C 1 ATOM 4492 O O . ARG A 1 575 ? 82.337 66.990 43.839 1.00 51.81 ? 589 ARG A O 1 ATOM 4493 C CB . ARG A 1 575 ? 79.916 65.122 43.141 1.00 57.74 ? 589 ARG A CB 1 ATOM 4494 C CG . ARG A 1 575 ? 78.836 64.068 43.245 1.00 66.24 ? 589 ARG A CG 1 ATOM 4495 C CD . ARG A 1 575 ? 77.846 64.209 42.090 1.00 71.66 ? 589 ARG A CD 1 ATOM 4496 N NE . ARG A 1 575 ? 76.494 63.769 42.444 1.00 80.79 ? 589 ARG A NE 1 ATOM 4497 C CZ . ARG A 1 575 ? 75.962 62.597 42.101 1.00 86.51 ? 589 ARG A CZ 1 ATOM 4498 N NH1 . ARG A 1 575 ? 76.663 61.726 41.385 1.00 90.33 ? 589 ARG A NH1 1 ATOM 4499 N NH2 . ARG A 1 575 ? 74.722 62.298 42.470 1.00 86.56 ? 589 ARG A NH2 1 ATOM 4500 N N . VAL A 1 576 ? 83.148 65.072 42.965 1.00 53.55 ? 590 VAL A N 1 ATOM 4501 C CA . VAL A 1 576 ? 84.213 65.739 42.224 1.00 53.14 ? 590 VAL A CA 1 ATOM 4502 C C . VAL A 1 576 ? 84.013 65.424 40.743 1.00 53.60 ? 590 VAL A C 1 ATOM 4503 O O . VAL A 1 576 ? 83.902 64.249 40.359 1.00 53.47 ? 590 VAL A O 1 ATOM 4504 C CB . VAL A 1 576 ? 85.596 65.296 42.686 1.00 53.87 ? 590 VAL A CB 1 ATOM 4505 C CG1 . VAL A 1 576 ? 86.669 66.183 42.065 1.00 49.56 ? 590 VAL A CG1 1 ATOM 4506 C CG2 . VAL A 1 576 ? 85.676 65.355 44.206 1.00 54.26 ? 590 VAL A CG2 1 ATOM 4507 N N . THR A 1 577 ? 83.932 66.461 39.913 1.00 48.33 ? 591 THR A N 1 ATOM 4508 C CA . THR A 1 577 ? 83.684 66.232 38.492 1.00 48.36 ? 591 THR A CA 1 ATOM 4509 C C . THR A 1 577 ? 84.726 66.892 37.592 1.00 48.47 ? 591 THR A C 1 ATOM 4510 O O . THR A 1 577 ? 85.437 67.817 38.005 1.00 51.36 ? 591 THR A O 1 ATOM 4511 C CB . THR A 1 577 ? 82.256 66.671 38.065 1.00 43.58 ? 591 THR A CB 1 ATOM 4512 O OG1 . THR A 1 577 ? 82.144 68.099 38.137 1.00 46.36 ? 591 THR A OG1 1 ATOM 4513 C CG2 . THR A 1 577 ? 81.206 66.029 38.952 1.00 43.54 ? 591 THR A CG2 1 ATOM 4514 N N . ALA A 1 578 ? 84.806 66.396 36.361 1.00 47.22 ? 592 ALA A N 1 ATOM 4515 C CA . ALA A 1 578 ? 85.701 66.935 35.349 1.00 50.29 ? 592 ALA A CA 1 ATOM 4516 C C . ALA A 1 578 ? 85.033 68.059 34.547 1.00 46.64 ? 592 ALA A C 1 ATOM 4517 O O . ALA A 1 578 ? 85.699 68.785 33.806 1.00 48.89 ? 592 ALA A O 1 ATOM 4518 C CB . ALA A 1 578 ? 86.153 65.819 34.415 1.00 52.40 ? 592 ALA A CB 1 ATOM 4519 N N . ASP A 1 579 ? 83.722 68.205 34.707 1.00 44.28 ? 593 ASP A N 1 ATOM 4520 C CA . ASP A 1 579 ? 82.949 69.145 33.896 1.00 45.36 ? 593 ASP A CA 1 ATOM 4521 C C . ASP A 1 579 ? 81.911 69.892 34.730 1.00 47.38 ? 593 ASP A C 1 ATOM 4522 O O . ASP A 1 579 ? 81.405 69.367 35.731 1.00 48.47 ? 593 ASP A O 1 ATOM 4523 C CB . ASP A 1 579 ? 82.235 68.402 32.753 1.00 45.22 ? 593 ASP A CB 1 ATOM 4524 C CG . ASP A 1 579 ? 81.358 67.267 33.257 1.00 46.91 ? 593 ASP A CG 1 ATOM 4525 O OD1 . ASP A 1 579 ? 81.796 66.510 34.156 1.00 50.78 ? 593 ASP A OD1 1 ATOM 4526 O OD2 . ASP A 1 579 ? 80.226 67.123 32.767 1.00 44.52 ? 593 ASP A OD2 1 ATOM 4527 N N . LEU A 1 580 ? 81.587 71.110 34.304 1.00 45.08 ? 594 LEU A N 1 ATOM 4528 C CA . LEU A 1 580 ? 80.574 71.921 34.977 1.00 42.70 ? 594 LEU A CA 1 ATOM 4529 C C . LEU A 1 580 ? 79.196 71.278 34.908 1.00 44.12 ? 594 LEU A C 1 ATOM 4530 O O . LEU A 1 580 ? 78.382 71.473 35.808 1.00 44.64 ? 594 LEU A O 1 ATOM 4531 C CB . LEU A 1 580 ? 80.550 73.336 34.384 1.00 42.19 ? 594 LEU A CB 1 ATOM 4532 C CG . LEU A 1 580 ? 79.486 74.339 34.836 1.00 43.44 ? 594 LEU A CG 1 ATOM 4533 C CD1 . LEU A 1 580 ? 79.512 74.510 36.354 1.00 44.21 ? 594 LEU A CD1 1 ATOM 4534 C CD2 . LEU A 1 580 ? 79.723 75.667 34.139 1.00 41.03 ? 594 LEU A CD2 1 ATOM 4535 N N . GLY A 1 581 ? 78.929 70.519 33.842 1.00 43.38 ? 595 GLY A N 1 ATOM 4536 C CA . GLY A 1 581 ? 77.653 69.824 33.709 1.00 40.14 ? 595 GLY A CA 1 ATOM 4537 C C . GLY A 1 581 ? 77.569 68.593 34.601 1.00 42.28 ? 595 GLY A C 1 ATOM 4538 O O . GLY A 1 581 ? 76.519 67.960 34.687 1.00 43.73 ? 595 GLY A O 1 ATOM 4539 N N . GLY A 1 582 ? 78.679 68.244 35.252 1.00 46.12 ? 596 GLY A N 1 ATOM 4540 C CA . GLY A 1 582 ? 78.705 67.119 36.179 1.00 47.12 ? 596 GLY A CA 1 ATOM 4541 C C . GLY A 1 582 ? 78.378 65.740 35.618 1.00 50.20 ? 596 GLY A C 1 ATOM 4542 O O . GLY A 1 582 ? 77.831 64.899 36.332 1.00 53.02 ? 596 GLY A O 1 ATOM 4543 N N . TRP A 1 583 ? 78.710 65.495 34.351 1.00 50.40 ? 597 TRP A N 1 ATOM 4544 C CA . TRP A 1 583 ? 78.495 64.182 33.753 1.00 48.86 ? 597 TRP A CA 1 ATOM 4545 C C . TRP A 1 583 ? 79.648 63.231 34.051 1.00 48.11 ? 597 TRP A C 1 ATOM 4546 O O . TRP A 1 583 ? 79.437 62.023 34.134 1.00 50.73 ? 597 TRP A O 1 ATOM 4547 C CB . TRP A 1 583 ? 78.331 64.283 32.233 1.00 49.13 ? 597 TRP A CB 1 ATOM 4548 C CG . TRP A 1 583 ? 77.123 65.015 31.766 1.00 53.42 ? 597 TRP A CG 1 ATOM 4549 C CD1 . TRP A 1 583 ? 76.962 66.368 31.690 1.00 56.11 ? 597 TRP A CD1 1 ATOM 4550 C CD2 . TRP A 1 583 ? 75.908 64.437 31.260 1.00 55.85 ? 597 TRP A CD2 1 ATOM 4551 N NE1 . TRP A 1 583 ? 75.718 66.669 31.189 1.00 54.55 ? 597 TRP A NE1 1 ATOM 4552 C CE2 . TRP A 1 583 ? 75.052 65.503 30.916 1.00 54.52 ? 597 TRP A CE2 1 ATOM 4553 C CE3 . TRP A 1 583 ? 75.462 63.123 31.072 1.00 56.31 ? 597 TRP A CE3 1 ATOM 4554 C CZ2 . TRP A 1 583 ? 73.769 65.294 30.402 1.00 55.63 ? 597 TRP A CZ2 1 ATOM 4555 C CZ3 . TRP A 1 583 ? 74.196 62.917 30.558 1.00 56.67 ? 597 TRP A CZ3 1 ATOM 4556 C CH2 . TRP A 1 583 ? 73.359 63.996 30.232 1.00 56.23 ? 597 TRP A CH2 1 ATOM 4557 N N . ILE A 1 584 ? 80.861 63.773 34.198 1.00 44.15 ? 598 ILE A N 1 ATOM 4558 C CA . ILE A 1 584 ? 82.069 62.958 34.350 1.00 51.83 ? 598 ILE A CA 1 ATOM 4559 C C . ILE A 1 584 ? 82.633 62.950 35.781 1.00 54.70 ? 598 ILE A C 1 ATOM 4560 O O . ILE A 1 584 ? 83.282 63.907 36.207 1.00 53.90 ? 598 ILE A O 1 ATOM 4561 C CB . ILE A 1 584 ? 83.189 63.397 33.360 1.00 45.98 ? 598 ILE A CB 1 ATOM 4562 C CG1 . ILE A 1 584 ? 82.673 63.401 31.910 1.00 50.71 ? 598 ILE A CG1 1 ATOM 4563 C CG2 . ILE A 1 584 ? 84.365 62.451 33.420 1.00 47.55 ? 598 ILE A CG2 1 ATOM 4564 C CD1 . ILE A 1 584 ? 83.791 63.600 30.876 1.00 49.47 ? 598 ILE A CD1 1 ATOM 4565 N N . THR A 1 585 ? 82.427 61.845 36.496 1.00 58.85 ? 599 THR A N 1 ATOM 4566 C CA . THR A 1 585 ? 82.811 61.733 37.912 1.00 59.54 ? 599 THR A CA 1 ATOM 4567 C C . THR A 1 585 ? 84.270 61.343 38.148 1.00 61.85 ? 599 THR A C 1 ATOM 4568 O O . THR A 1 585 ? 84.736 60.327 37.627 1.00 65.33 ? 599 THR A O 1 ATOM 4569 C CB . THR A 1 585 ? 81.948 60.678 38.625 1.00 60.51 ? 599 THR A CB 1 ATOM 4570 O OG1 . THR A 1 585 ? 80.558 61.006 38.487 1.00 60.34 ? 599 THR A OG1 1 ATOM 4571 C CG2 . THR A 1 585 ? 82.317 60.592 40.099 1.00 62.33 ? 599 THR A CG2 1 ATOM 4572 N N . TYR A 1 586 ? 84.972 62.138 38.957 1.00 60.10 ? 600 TYR A N 1 ATOM 4573 C CA . TYR A 1 586 ? 86.322 61.823 39.404 1.00 60.95 ? 600 TYR A CA 1 ATOM 4574 C C . TYR A 1 586 ? 86.251 61.123 40.764 1.00 62.74 ? 600 TYR A C 1 ATOM 4575 O O . TYR A 1 586 ? 87.025 60.202 41.052 1.00 58.97 ? 600 TYR A O 1 ATOM 4576 C CB . TYR A 1 586 ? 87.146 63.106 39.564 1.00 61.82 ? 600 TYR A CB 1 ATOM 4577 C CG . TYR A 1 586 ? 87.786 63.659 38.305 1.00 62.33 ? 600 TYR A CG 1 ATOM 4578 C CD1 . TYR A 1 586 ? 88.212 62.820 37.277 1.00 63.81 ? 600 TYR A CD1 1 ATOM 4579 C CD2 . TYR A 1 586 ? 87.985 65.031 38.160 1.00 60.85 ? 600 TYR A CD2 1 ATOM 4580 C CE1 . TYR A 1 586 ? 88.811 63.341 36.125 1.00 63.33 ? 600 TYR A CE1 1 ATOM 4581 C CE2 . TYR A 1 586 ? 88.577 65.560 37.019 1.00 59.62 ? 600 TYR A CE2 1 ATOM 4582 C CZ . TYR A 1 586 ? 88.991 64.711 36.009 1.00 58.93 ? 600 TYR A CZ 1 ATOM 4583 O OH . TYR A 1 586 ? 89.573 65.246 34.890 1.00 53.71 ? 600 TYR A OH 1 ATOM 4584 N N . ALA A 1 587 ? 85.326 61.594 41.600 1.00 63.07 ? 601 ALA A N 1 ATOM 4585 C CA . ALA A 1 587 ? 85.076 61.018 42.924 1.00 61.46 ? 601 ALA A CA 1 ATOM 4586 C C . ALA A 1 587 ? 83.726 61.482 43.463 1.00 61.12 ? 601 ALA A C 1 ATOM 4587 O O . ALA A 1 587 ? 83.247 62.574 43.128 1.00 60.25 ? 601 ALA A O 1 ATOM 4588 C CB . ALA A 1 587 ? 86.168 61.401 43.890 1.00 58.21 ? 601 ALA A CB 1 ATOM 4589 N N . SER A 1 588 ? 83.117 60.653 44.301 1.00 58.59 ? 602 SER A N 1 ATOM 4590 C CA . SER A 1 588 ? 81.869 61.018 44.948 1.00 60.11 ? 602 SER A CA 1 ATOM 4591 C C . SER A 1 588 ? 81.755 60.309 46.291 1.00 63.68 ? 602 SER A C 1 ATOM 4592 O O . SER A 1 588 ? 82.462 59.331 46.546 1.00 63.70 ? 602 SER A O 1 ATOM 4593 C CB . SER A 1 588 ? 80.681 60.659 44.054 1.00 59.54 ? 602 SER A CB 1 ATOM 4594 O OG . SER A 1 588 ? 80.731 59.295 43.677 1.00 60.89 ? 602 SER A OG 1 ATOM 4595 N N . GLY A 1 589 ? 80.865 60.801 47.149 1.00 66.28 ? 603 GLY A N 1 ATOM 4596 C CA . GLY A 1 589 ? 80.651 60.189 48.447 1.00 70.22 ? 603 GLY A CA 1 ATOM 4597 C C . GLY A 1 589 ? 79.786 60.992 49.401 1.00 71.08 ? 603 GLY A C 1 ATOM 4598 O O . GLY A 1 589 ? 79.082 61.924 49.004 1.00 68.63 ? 603 GLY A O 1 ATOM 4599 N N . HIS A 1 590 ? 79.838 60.615 50.673 1.00 73.51 ? 604 HIS A N 1 ATOM 4600 C CA . HIS A 1 590 ? 79.059 61.284 51.707 1.00 72.58 ? 604 HIS A CA 1 ATOM 4601 C C . HIS A 1 590 ? 79.897 62.309 52.458 1.00 70.53 ? 604 HIS A C 1 ATOM 4602 O O . HIS A 1 590 ? 81.129 62.233 52.475 1.00 70.34 ? 604 HIS A O 1 ATOM 4603 C CB . HIS A 1 590 ? 78.497 60.257 52.685 1.00 73.93 ? 604 HIS A CB 1 ATOM 4604 C CG . HIS A 1 590 ? 77.645 59.217 52.033 1.00 78.20 ? 604 HIS A CG 1 ATOM 4605 N ND1 . HIS A 1 590 ? 76.535 59.532 51.278 1.00 79.75 ? 604 HIS A ND1 1 ATOM 4606 C CD2 . HIS A 1 590 ? 77.739 57.866 52.022 1.00 81.10 ? 604 HIS A CD2 1 ATOM 4607 C CE1 . HIS A 1 590 ? 75.981 58.419 50.829 1.00 81.30 ? 604 HIS A CE1 1 ATOM 4608 N NE2 . HIS A 1 590 ? 76.691 57.395 51.268 1.00 82.84 ? 604 HIS A NE2 1 ATOM 4609 N N . ALA A 1 591 ? 79.213 63.267 53.075 1.00 68.43 ? 605 ALA A N 1 ATOM 4610 C CA . ALA A 1 591 ? 79.858 64.312 53.860 1.00 66.28 ? 605 ALA A CA 1 ATOM 4611 C C . ALA A 1 591 ? 78.845 64.935 54.802 1.00 64.74 ? 605 ALA A C 1 ATOM 4612 O O . ALA A 1 591 ? 77.652 64.992 54.492 1.00 59.97 ? 605 ALA A O 1 ATOM 4613 C CB . ALA A 1 591 ? 80.443 65.377 52.949 1.00 66.96 ? 605 ALA A CB 1 ATOM 4614 N N . ASP A 1 592 ? 79.330 65.409 55.947 1.00 70.09 ? 606 ASP A N 1 ATOM 4615 C CA . ASP A 1 592 ? 78.482 66.060 56.938 1.00 71.91 ? 606 ASP A CA 1 ATOM 4616 C C . ASP A 1 592 ? 78.170 67.502 56.519 1.00 64.63 ? 606 ASP A C 1 ATOM 4617 O O . ASP A 1 592 ? 78.797 68.454 56.996 1.00 62.41 ? 606 ASP A O 1 ATOM 4618 C CB . ASP A 1 592 ? 79.159 66.041 58.305 1.00 80.42 ? 606 ASP A CB 1 ATOM 4619 C CG . ASP A 1 592 ? 78.184 66.266 59.437 1.00 88.88 ? 606 ASP A CG 1 ATOM 4620 O OD1 . ASP A 1 592 ? 77.230 65.468 59.568 1.00 92.14 ? 606 ASP A OD1 1 ATOM 4621 O OD2 . ASP A 1 592 ? 78.373 67.239 60.199 1.00 92.35 ? 606 ASP A OD2 1 ATOM 4622 N N . VAL A 1 593 ? 77.195 67.650 55.629 1.00 58.84 ? 607 VAL A N 1 ATOM 4623 C CA . VAL A 1 593 ? 76.853 68.949 55.074 1.00 56.28 ? 607 VAL A CA 1 ATOM 4624 C C . VAL A 1 593 ? 75.337 69.159 55.071 1.00 53.45 ? 607 VAL A C 1 ATOM 4625 O O . VAL A 1 593 ? 74.575 68.279 54.650 1.00 51.82 ? 607 VAL A O 1 ATOM 4626 C CB . VAL A 1 593 ? 77.422 69.099 53.647 1.00 57.89 ? 607 VAL A CB 1 ATOM 4627 C CG1 . VAL A 1 593 ? 76.849 70.333 52.967 1.00 58.37 ? 607 VAL A CG1 1 ATOM 4628 C CG2 . VAL A 1 593 ? 78.952 69.156 53.689 1.00 58.01 ? 607 VAL A CG2 1 ATOM 4629 N N . THR A 1 594 ? 74.907 70.322 55.556 1.00 53.27 ? 608 THR A N 1 ATOM 4630 C CA . THR A 1 594 ? 73.490 70.685 55.569 1.00 53.19 ? 608 THR A CA 1 ATOM 4631 C C . THR A 1 594 ? 73.324 72.113 55.033 1.00 56.12 ? 608 THR A C 1 ATOM 4632 O O . THR A 1 594 ? 74.318 72.775 54.711 1.00 57.23 ? 608 THR A O 1 ATOM 4633 C CB . THR A 1 594 ? 72.896 70.564 57.001 1.00 60.90 ? 608 THR A CB 1 ATOM 4634 O OG1 . THR A 1 594 ? 71.465 70.624 56.940 1.00 64.24 ? 608 THR A OG1 1 ATOM 4635 C CG2 . THR A 1 594 ? 73.410 71.675 57.896 1.00 56.56 ? 608 THR A CG2 1 ATOM 4636 N N . ALA A 1 595 ? 72.083 72.587 54.925 1.00 55.89 ? 609 ALA A N 1 ATOM 4637 C CA . ALA A 1 595 ? 71.823 73.969 54.493 1.00 53.32 ? 609 ALA A CA 1 ATOM 4638 C C . ALA A 1 595 ? 71.982 74.936 55.667 1.00 53.05 ? 609 ALA A C 1 ATOM 4639 O O . ALA A 1 595 ? 71.836 74.534 56.822 1.00 52.03 ? 609 ALA A O 1 ATOM 4640 C CB . ALA A 1 595 ? 70.431 74.096 53.903 1.00 50.30 ? 609 ALA A CB 1 ATOM 4641 N N . LYS A 1 596 ? 72.277 76.201 55.359 1.00 50.29 ? 610 LYS A N 1 ATOM 4642 C CA . LYS A 1 596 ? 72.391 77.262 56.363 1.00 52.91 ? 610 LYS A CA 1 ATOM 4643 C C . LYS A 1 596 ? 73.455 76.991 57.409 1.00 55.23 ? 610 LYS A C 1 ATOM 4644 O O . LYS A 1 596 ? 73.253 77.244 58.599 1.00 56.83 ? 610 LYS A O 1 ATOM 4645 C CB . LYS A 1 596 ? 71.039 77.529 57.033 1.00 56.10 ? 610 LYS A CB 1 ATOM 4646 C CG . LYS A 1 596 ? 69.955 77.895 56.034 1.00 57.56 ? 610 LYS A CG 1 ATOM 4647 C CD . LYS A 1 596 ? 68.595 77.902 56.689 1.00 59.60 ? 610 LYS A CD 1 ATOM 4648 C CE . LYS A 1 596 ? 67.493 77.893 55.651 1.00 61.98 ? 610 LYS A CE 1 ATOM 4649 N NZ . LYS A 1 596 ? 66.203 77.529 56.303 1.00 66.92 ? 610 LYS A NZ 1 ATOM 4650 N N . ARG A 1 597 ? 74.592 76.474 56.957 1.00 56.65 ? 611 ARG A N 1 ATOM 4651 C CA . ARG A 1 597 ? 75.753 76.297 57.820 1.00 60.78 ? 611 ARG A CA 1 ATOM 4652 C C . ARG A 1 597 ? 76.995 76.692 57.033 1.00 57.96 ? 611 ARG A C 1 ATOM 4653 O O . ARG A 1 597 ? 77.142 76.310 55.866 1.00 57.90 ? 611 ARG A O 1 ATOM 4654 C CB . ARG A 1 597 ? 75.843 74.846 58.310 1.00 67.44 ? 611 ARG A CB 1 ATOM 4655 C CG . ARG A 1 597 ? 76.860 74.630 59.431 1.00 76.80 ? 611 ARG A CG 1 ATOM 4656 C CD . ARG A 1 597 ? 76.599 73.338 60.205 1.00 83.24 ? 611 ARG A CD 1 ATOM 4657 N NE . ARG A 1 597 ? 75.239 73.291 60.737 1.00 87.88 ? 611 ARG A NE 1 ATOM 4658 C CZ . ARG A 1 597 ? 74.666 72.207 61.255 1.00 90.47 ? 611 ARG A CZ 1 ATOM 4659 N NH1 . ARG A 1 597 ? 75.330 71.061 61.313 1.00 90.89 ? 611 ARG A NH1 1 ATOM 4660 N NH2 . ARG A 1 597 ? 73.422 72.266 61.712 1.00 91.20 ? 611 ARG A NH2 1 ATOM 4661 N N . TRP A 1 598 ? 77.869 77.476 57.652 1.00 56.38 ? 612 TRP A N 1 ATOM 4662 C CA . TRP A 1 598 ? 79.122 77.903 57.018 1.00 55.40 ? 612 TRP A CA 1 ATOM 4663 C C . TRP A 1 598 ? 80.199 76.811 56.996 1.00 56.12 ? 612 TRP A C 1 ATOM 4664 O O . TRP A 1 598 ? 80.564 76.276 58.041 1.00 58.90 ? 612 TRP A O 1 ATOM 4665 C CB . TRP A 1 598 ? 79.659 79.162 57.718 1.00 56.97 ? 612 TRP A CB 1 ATOM 4666 C CG . TRP A 1 598 ? 78.984 80.398 57.206 1.00 56.97 ? 612 TRP A CG 1 ATOM 4667 C CD1 . TRP A 1 598 ? 77.986 81.118 57.814 1.00 55.95 ? 612 TRP A CD1 1 ATOM 4668 C CD2 . TRP A 1 598 ? 79.229 81.034 55.948 1.00 50.51 ? 612 TRP A CD2 1 ATOM 4669 N NE1 . TRP A 1 598 ? 77.610 82.170 57.010 1.00 52.77 ? 612 TRP A NE1 1 ATOM 4670 C CE2 . TRP A 1 598 ? 78.356 82.140 55.858 1.00 50.23 ? 612 TRP A CE2 1 ATOM 4671 C CE3 . TRP A 1 598 ? 80.108 80.776 54.891 1.00 47.25 ? 612 TRP A CE3 1 ATOM 4672 C CZ2 . TRP A 1 598 ? 78.333 82.988 54.737 1.00 49.05 ? 612 TRP A CZ2 1 ATOM 4673 C CZ3 . TRP A 1 598 ? 80.088 81.614 53.784 1.00 50.43 ? 612 TRP A CZ3 1 ATOM 4674 C CH2 . TRP A 1 598 ? 79.207 82.707 53.714 1.00 50.92 ? 612 TRP A CH2 1 ATOM 4675 N N . TYR A 1 599 ? 80.703 76.476 55.808 1.00 54.47 ? 613 TYR A N 1 ATOM 4676 C CA . TYR A 1 599 ? 81.793 75.500 55.695 1.00 55.21 ? 613 TYR A CA 1 ATOM 4677 C C . TYR A 1 599 ? 83.001 76.107 54.989 1.00 56.79 ? 613 TYR A C 1 ATOM 4678 O O . TYR A 1 599 ? 82.846 76.918 54.076 1.00 59.84 ? 613 TYR A O 1 ATOM 4679 C CB . TYR A 1 599 ? 81.335 74.254 54.914 1.00 53.91 ? 613 TYR A CB 1 ATOM 4680 C CG . TYR A 1 599 ? 80.182 73.496 55.531 1.00 53.06 ? 613 TYR A CG 1 ATOM 4681 C CD1 . TYR A 1 599 ? 80.367 72.688 56.652 1.00 53.65 ? 613 TYR A CD1 1 ATOM 4682 C CD2 . TYR A 1 599 ? 78.918 73.576 54.985 1.00 48.80 ? 613 TYR A CD2 1 ATOM 4683 C CE1 . TYR A 1 599 ? 79.305 71.990 57.208 1.00 54.18 ? 613 TYR A CE1 1 ATOM 4684 C CE2 . TYR A 1 599 ? 77.858 72.886 55.528 1.00 51.85 ? 613 TYR A CE2 1 ATOM 4685 C CZ . TYR A 1 599 ? 78.053 72.096 56.636 1.00 53.32 ? 613 TYR A CZ 1 ATOM 4686 O OH . TYR A 1 599 ? 76.981 71.415 57.165 1.00 53.96 ? 613 TYR A OH 1 ATOM 4687 N N . THR A 1 600 ? 84.206 75.723 55.398 1.00 57.90 ? 614 THR A N 1 ATOM 4688 C CA . THR A 1 600 ? 85.383 76.083 54.606 1.00 57.85 ? 614 THR A CA 1 ATOM 4689 C C . THR A 1 600 ? 85.749 74.963 53.632 1.00 57.83 ? 614 THR A C 1 ATOM 4690 O O . THR A 1 600 ? 86.006 73.825 54.049 1.00 60.12 ? 614 THR A O 1 ATOM 4691 C CB . THR A 1 600 ? 86.615 76.430 55.457 1.00 56.99 ? 614 THR A CB 1 ATOM 4692 O OG1 . THR A 1 600 ? 86.310 77.543 56.305 1.00 55.79 ? 614 THR A OG1 1 ATOM 4693 C CG2 . THR A 1 600 ? 87.785 76.804 54.547 1.00 53.97 ? 614 THR A CG2 1 ATOM 4694 N N . LEU A 1 601 ? 85.762 75.291 52.340 1.00 52.85 ? 615 LEU A N 1 ATOM 4695 C CA . LEU A 1 601 ? 86.163 74.339 51.306 1.00 54.55 ? 615 LEU A CA 1 ATOM 4696 C C . LEU A 1 601 ? 87.580 74.609 50.793 1.00 55.70 ? 615 LEU A C 1 ATOM 4697 O O . LEU A 1 601 ? 87.936 75.745 50.480 1.00 48.64 ? 615 LEU A O 1 ATOM 4698 C CB . LEU A 1 601 ? 85.188 74.366 50.128 1.00 53.58 ? 615 LEU A CB 1 ATOM 4699 C CG . LEU A 1 601 ? 83.852 73.637 50.285 1.00 52.00 ? 615 LEU A CG 1 ATOM 4700 C CD1 . LEU A 1 601 ? 82.994 73.824 49.041 1.00 45.32 ? 615 LEU A CD1 1 ATOM 4701 C CD2 . LEU A 1 601 ? 84.077 72.163 50.556 1.00 50.97 ? 615 LEU A CD2 1 ATOM 4702 N N . THR A 1 602 ? 88.385 73.558 50.709 1.00 49.74 ? 616 THR A N 1 ATOM 4703 C CA . THR A 1 602 ? 89.696 73.670 50.083 1.00 57.92 ? 616 THR A CA 1 ATOM 4704 C C . THR A 1 602 ? 89.829 72.661 48.935 1.00 55.09 ? 616 THR A C 1 ATOM 4705 O O . THR A 1 602 ? 89.398 71.506 49.045 1.00 53.66 ? 616 THR A O 1 ATOM 4706 C CB . THR A 1 602 ? 90.839 73.502 51.109 1.00 59.10 ? 616 THR A CB 1 ATOM 4707 O OG1 . THR A 1 602 ? 90.585 74.334 52.252 1.00 59.71 ? 616 THR A OG1 1 ATOM 4708 C CG2 . THR A 1 602 ? 92.174 73.895 50.492 1.00 57.94 ? 616 THR A CG2 1 ATOM 4709 N N . LEU A 1 603 ? 90.402 73.113 47.823 1.00 52.33 ? 617 LEU A N 1 ATOM 4710 C CA . LEU A 1 603 ? 90.602 72.261 46.653 1.00 50.72 ? 617 LEU A CA 1 ATOM 4711 C C . LEU A 1 603 ? 92.045 72.400 46.201 1.00 51.81 ? 617 LEU A C 1 ATOM 4712 O O . LEU A 1 603 ? 92.487 73.500 45.857 1.00 51.93 ? 617 LEU A O 1 ATOM 4713 C CB . LEU A 1 603 ? 89.647 72.679 45.532 1.00 51.08 ? 617 LEU A CB 1 ATOM 4714 C CG . LEU A 1 603 ? 89.832 72.009 44.163 1.00 54.98 ? 617 LEU A CG 1 ATOM 4715 C CD1 . LEU A 1 603 ? 89.700 70.506 44.290 1.00 54.59 ? 617 LEU A CD1 1 ATOM 4716 C CD2 . LEU A 1 603 ? 88.840 72.549 43.122 1.00 55.62 ? 617 LEU A CD2 1 ATOM 4717 N N . GLY A 1 604 ? 92.796 71.300 46.236 1.00 55.06 ? 618 GLY A N 1 ATOM 4718 C CA . GLY A 1 604 ? 94.186 71.320 45.804 1.00 54.23 ? 618 GLY A CA 1 ATOM 4719 C C . GLY A 1 604 ? 94.383 70.554 44.507 1.00 56.50 ? 618 GLY A C 1 ATOM 4720 O O . GLY A 1 604 ? 93.983 69.395 44.388 1.00 58.82 ? 618 GLY A O 1 ATOM 4721 N N . ILE A 1 605 ? 94.992 71.193 43.520 1.00 56.17 ? 619 ILE A N 1 ATOM 4722 C CA . ILE A 1 605 ? 95.222 70.514 42.258 1.00 56.08 ? 619 ILE A CA 1 ATOM 4723 C C . ILE A 1 605 ? 96.697 70.600 41.887 1.00 58.41 ? 619 ILE A C 1 ATOM 4724 O O . ILE A 1 605 ? 97.260 71.700 41.806 1.00 58.09 ? 619 ILE A O 1 ATOM 4725 C CB . ILE A 1 605 ? 94.361 71.096 41.120 1.00 51.34 ? 619 ILE A CB 1 ATOM 4726 C CG1 . ILE A 1 605 ? 92.906 71.269 41.566 1.00 50.03 ? 619 ILE A CG1 1 ATOM 4727 C CG2 . ILE A 1 605 ? 94.398 70.172 39.934 1.00 51.59 ? 619 ILE A CG2 1 ATOM 4728 C CD1 . ILE A 1 605 ? 92.022 71.996 40.553 1.00 48.71 ? 619 ILE A CD1 1 ATOM 4729 N N . LYS A 1 606 ? 97.313 69.441 41.655 1.00 58.85 ? 620 LYS A N 1 ATOM 4730 C CA . LYS A 1 606 ? 98.738 69.362 41.328 1.00 60.63 ? 620 LYS A CA 1 ATOM 4731 C C . LYS A 1 606 ? 99.017 68.183 40.393 1.00 60.35 ? 620 LYS A C 1 ATOM 4732 O O . LYS A 1 606 ? 98.791 67.023 40.761 1.00 61.10 ? 620 LYS A O 1 ATOM 4733 C CB . LYS A 1 606 ? 99.557 69.223 42.611 1.00 65.50 ? 620 LYS A CB 1 ATOM 4734 C CG . LYS A 1 606 ? 101.055 69.121 42.397 1.00 70.03 ? 620 LYS A CG 1 ATOM 4735 C CD . LYS A 1 606 ? 101.760 68.847 43.717 1.00 73.03 ? 620 LYS A CD 1 ATOM 4736 C CE . LYS A 1 606 ? 103.254 69.073 43.591 1.00 76.09 ? 620 LYS A CE 1 ATOM 4737 N NZ . LYS A 1 606 ? 103.945 68.931 44.911 1.00 80.35 ? 620 LYS A NZ 1 ATOM 4738 N N . GLY A 1 607 ? 99.507 68.478 39.187 1.00 61.06 ? 621 GLY A N 1 ATOM 4739 C CA . GLY A 1 607 ? 99.751 67.451 38.186 1.00 58.43 ? 621 GLY A CA 1 ATOM 4740 C C . GLY A 1 607 ? 98.514 66.610 37.902 1.00 57.57 ? 621 GLY A C 1 ATOM 4741 O O . GLY A 1 607 ? 97.458 67.146 37.572 1.00 59.53 ? 621 GLY A O 1 ATOM 4742 N N . TYR A 1 608 ? 98.654 65.294 38.058 1.00 66.11 ? 622 TYR A N 1 ATOM 4743 C CA . TYR A 1 608 ? 97.585 64.328 37.824 1.00 67.97 ? 622 TYR A CA 1 ATOM 4744 C C . TYR A 1 608 ? 96.599 64.208 38.979 1.00 70.40 ? 622 TYR A C 1 ATOM 4745 O O . TYR A 1 608 ? 95.585 63.512 38.859 1.00 71.34 ? 622 TYR A O 1 ATOM 4746 C CB . TYR A 1 608 ? 98.186 62.943 37.589 1.00 72.45 ? 622 TYR A CB 1 ATOM 4747 C CG . TYR A 1 608 ? 98.776 62.754 36.218 1.00 78.48 ? 622 TYR A CG 1 ATOM 4748 C CD1 . TYR A 1 608 ? 97.964 62.427 35.136 1.00 80.28 ? 622 TYR A CD1 1 ATOM 4749 C CD2 . TYR A 1 608 ? 100.143 62.893 36.002 1.00 80.80 ? 622 TYR A CD2 1 ATOM 4750 C CE1 . TYR A 1 608 ? 98.493 62.253 33.875 1.00 83.10 ? 622 TYR A CE1 1 ATOM 4751 C CE2 . TYR A 1 608 ? 100.683 62.721 34.743 1.00 84.06 ? 622 TYR A CE2 1 ATOM 4752 C CZ . TYR A 1 608 ? 99.853 62.399 33.684 1.00 84.91 ? 622 TYR A CZ 1 ATOM 4753 O OH . TYR A 1 608 ? 100.381 62.223 32.428 1.00 86.31 ? 622 TYR A OH 1 ATOM 4754 N N . PHE A 1 609 ? 96.888 64.876 40.093 1.00 71.39 ? 623 PHE A N 1 ATOM 4755 C CA . PHE A 1 609 ? 96.165 64.580 41.329 1.00 70.48 ? 623 PHE A CA 1 ATOM 4756 C C . PHE A 1 609 ? 95.460 65.737 42.026 1.00 66.23 ? 623 PHE A C 1 ATOM 4757 O O . PHE A 1 609 ? 95.934 66.876 42.024 1.00 66.14 ? 623 PHE A O 1 ATOM 4758 C CB . PHE A 1 609 ? 97.085 63.834 42.298 1.00 72.46 ? 623 PHE A CB 1 ATOM 4759 C CG . PHE A 1 609 ? 97.440 62.459 41.820 1.00 76.25 ? 623 PHE A CG 1 ATOM 4760 C CD1 . PHE A 1 609 ? 96.606 61.380 42.102 1.00 75.21 ? 623 PHE A CD1 1 ATOM 4761 C CD2 . PHE A 1 609 ? 98.577 62.249 41.045 1.00 79.66 ? 623 PHE A CD2 1 ATOM 4762 C CE1 . PHE A 1 609 ? 96.910 60.110 41.646 1.00 76.94 ? 623 PHE A CE1 1 ATOM 4763 C CE2 . PHE A 1 609 ? 98.890 60.981 40.578 1.00 81.36 ? 623 PHE A CE2 1 ATOM 4764 C CZ . PHE A 1 609 ? 98.055 59.908 40.882 1.00 80.34 ? 623 PHE A CZ 1 ATOM 4765 N N . ALA A 1 610 ? 94.320 65.419 42.628 1.00 62.82 ? 624 ALA A N 1 ATOM 4766 C CA . ALA A 1 610 ? 93.564 66.392 43.402 1.00 64.27 ? 624 ALA A CA 1 ATOM 4767 C C . ALA A 1 610 ? 93.244 65.893 44.814 1.00 65.45 ? 624 ALA A C 1 ATOM 4768 O O . ALA A 1 610 ? 93.300 64.689 45.098 1.00 65.98 ? 624 ALA A O 1 ATOM 4769 C CB . ALA A 1 610 ? 92.286 66.766 42.673 1.00 59.71 ? 624 ALA A CB 1 ATOM 4770 N N . PHE A 1 611 ? 92.911 66.836 45.690 1.00 63.79 ? 625 PHE A N 1 ATOM 4771 C CA . PHE A 1 611 ? 92.427 66.526 47.035 1.00 61.75 ? 625 PHE A CA 1 ATOM 4772 C C . PHE A 1 611 ? 91.489 67.643 47.451 1.00 57.80 ? 625 PHE A C 1 ATOM 4773 O O . PHE A 1 611 ? 91.661 68.786 47.021 1.00 55.68 ? 625 PHE A O 1 ATOM 4774 C CB . PHE A 1 611 ? 93.575 66.359 48.048 1.00 59.16 ? 625 PHE A CB 1 ATOM 4775 C CG . PHE A 1 611 ? 94.168 67.658 48.545 1.00 59.93 ? 625 PHE A CG 1 ATOM 4776 C CD1 . PHE A 1 611 ? 93.620 68.327 49.635 1.00 61.50 ? 625 PHE A CD1 1 ATOM 4777 C CD2 . PHE A 1 611 ? 95.303 68.187 47.951 1.00 62.80 ? 625 PHE A CD2 1 ATOM 4778 C CE1 . PHE A 1 611 ? 94.180 69.518 50.103 1.00 62.80 ? 625 PHE A CE1 1 ATOM 4779 C CE2 . PHE A 1 611 ? 95.867 69.374 48.413 1.00 63.84 ? 625 PHE A CE2 1 ATOM 4780 C CZ . PHE A 1 611 ? 95.304 70.038 49.492 1.00 63.12 ? 625 PHE A CZ 1 ATOM 4781 N N . GLY A 1 612 ? 90.502 67.317 48.277 1.00 56.90 ? 626 GLY A N 1 ATOM 4782 C CA . GLY A 1 612 ? 89.588 68.318 48.801 1.00 56.45 ? 626 GLY A CA 1 ATOM 4783 C C . GLY A 1 612 ? 89.517 68.273 50.323 1.00 57.89 ? 626 GLY A C 1 ATOM 4784 O O . GLY A 1 612 ? 89.556 67.194 50.930 1.00 55.62 ? 626 GLY A O 1 ATOM 4785 N N . MET A 1 613 ? 89.417 69.440 50.951 1.00 58.04 ? 627 MET A N 1 ATOM 4786 C CA . MET A 1 613 ? 89.215 69.476 52.394 1.00 61.47 ? 627 MET A CA 1 ATOM 4787 C C . MET A 1 613 ? 87.891 70.132 52.775 1.00 61.37 ? 627 MET A C 1 ATOM 4788 O O . MET A 1 613 ? 87.412 71.041 52.089 1.00 57.53 ? 627 MET A O 1 ATOM 4789 C CB . MET A 1 613 ? 90.376 70.177 53.091 1.00 61.90 ? 627 MET A CB 1 ATOM 4790 C CG . MET A 1 613 ? 91.647 69.347 53.151 1.00 62.93 ? 627 MET A CG 1 ATOM 4791 S SD . MET A 1 613 ? 92.931 70.130 54.137 1.00 85.04 ? 627 MET A SD 1 ATOM 4792 C CE . MET A 1 613 ? 93.198 71.644 53.223 1.00 59.80 ? 627 MET A CE 1 ATOM 4793 N N . LEU A 1 614 ? 87.314 69.650 53.872 1.00 60.52 ? 628 LEU A N 1 ATOM 4794 C CA . LEU A 1 614 ? 86.130 70.238 54.475 1.00 59.59 ? 628 LEU A CA 1 ATOM 4795 C C . LEU A 1 614 ? 86.523 70.684 55.881 1.00 64.48 ? 628 LEU A C 1 ATOM 4796 O O . LEU A 1 614 ? 86.971 69.864 56.698 1.00 66.96 ? 628 LEU A O 1 ATOM 4797 C CB . LEU A 1 614 ? 85.007 69.202 54.544 1.00 59.34 ? 628 LEU A CB 1 ATOM 4798 C CG . LEU A 1 614 ? 83.628 69.695 54.986 1.00 58.16 ? 628 LEU A CG 1 ATOM 4799 C CD1 . LEU A 1 614 ? 83.139 70.773 54.051 1.00 53.95 ? 628 LEU A CD1 1 ATOM 4800 C CD2 . LEU A 1 614 ? 82.613 68.557 55.047 1.00 59.20 ? 628 LEU A CD2 1 ATOM 4801 N N . ASN A 1 615 ? 86.387 71.980 56.157 1.00 63.44 ? 629 ASN A N 1 ATOM 4802 C CA . ASN A 1 615 ? 86.812 72.551 57.439 1.00 62.14 ? 629 ASN A CA 1 ATOM 4803 C C . ASN A 1 615 ? 88.245 72.204 57.851 1.00 63.29 ? 629 ASN A C 1 ATOM 4804 O O . ASN A 1 615 ? 88.512 71.972 59.027 1.00 63.59 ? 629 ASN A O 1 ATOM 4805 C CB . ASN A 1 615 ? 85.839 72.167 58.572 1.00 61.03 ? 629 ASN A CB 1 ATOM 4806 C CG . ASN A 1 615 ? 84.469 72.793 58.401 1.00 59.39 ? 629 ASN A CG 1 ATOM 4807 O OD1 . ASN A 1 615 ? 84.332 73.855 57.784 1.00 56.72 ? 629 ASN A OD1 1 ATOM 4808 N ND2 . ASN A 1 615 ? 83.439 72.133 58.941 1.00 57.99 ? 629 ASN A ND2 1 ATOM 4809 N N . GLY A 1 616 ? 89.161 72.164 56.887 1.00 62.61 ? 630 GLY A N 1 ATOM 4810 C CA . GLY A 1 616 ? 90.552 71.881 57.185 1.00 64.45 ? 630 GLY A CA 1 ATOM 4811 C C . GLY A 1 616 ? 90.863 70.403 57.339 1.00 68.18 ? 630 GLY A C 1 ATOM 4812 O O . GLY A 1 616 ? 92.017 70.028 57.558 1.00 70.24 ? 630 GLY A O 1 ATOM 4813 N N . THR A 1 617 ? 89.839 69.561 57.225 1.00 68.20 ? 631 THR A N 1 ATOM 4814 C CA . THR A 1 617 ? 90.019 68.113 57.311 1.00 68.43 ? 631 THR A CA 1 ATOM 4815 C C . THR A 1 617 ? 89.834 67.458 55.938 1.00 66.66 ? 631 THR A C 1 ATOM 4816 O O . THR A 1 617 ? 88.863 67.751 55.234 1.00 64.66 ? 631 THR A O 1 ATOM 4817 C CB . THR A 1 617 ? 89.037 67.494 58.321 1.00 68.88 ? 631 THR A CB 1 ATOM 4818 O OG1 . THR A 1 617 ? 89.359 67.959 59.642 1.00 68.43 ? 631 THR A OG1 1 ATOM 4819 C CG2 . THR A 1 617 ? 89.114 65.975 58.284 1.00 71.45 ? 631 THR A CG2 1 ATOM 4820 N N . ILE A 1 618 ? 90.770 66.585 55.563 1.00 66.85 ? 632 ILE A N 1 ATOM 4821 C CA . ILE A 1 618 ? 90.713 65.852 54.292 1.00 65.29 ? 632 ILE A CA 1 ATOM 4822 C C . ILE A 1 618 ? 89.407 65.068 54.083 1.00 65.08 ? 632 ILE A C 1 ATOM 4823 O O . ILE A 1 618 ? 89.018 64.236 54.916 1.00 63.19 ? 632 ILE A O 1 ATOM 4824 C CB . ILE A 1 618 ? 91.894 64.877 54.163 1.00 66.80 ? 632 ILE A CB 1 ATOM 4825 C CG1 . ILE A 1 618 ? 93.207 65.647 54.038 1.00 68.29 ? 632 ILE A CG1 1 ATOM 4826 C CG2 . ILE A 1 618 ? 91.702 63.965 52.958 1.00 66.27 ? 632 ILE A CG2 1 ATOM 4827 C CD1 . ILE A 1 618 ? 93.492 66.131 52.625 1.00 69.01 ? 632 ILE A CD1 1 ATOM 4828 N N . LEU A 1 619 ? 88.738 65.336 52.964 1.00 60.69 ? 633 LEU A N 1 ATOM 4829 C CA . LEU A 1 619 ? 87.533 64.604 52.611 1.00 62.20 ? 633 LEU A CA 1 ATOM 4830 C C . LEU A 1 619 ? 87.862 63.551 51.559 1.00 64.15 ? 633 LEU A C 1 ATOM 4831 O O . LEU A 1 619 ? 87.360 62.425 51.619 1.00 65.21 ? 633 LEU A O 1 ATOM 4832 C CB . LEU A 1 619 ? 86.455 65.558 52.094 1.00 60.47 ? 633 LEU A CB 1 ATOM 4833 C CG . LEU A 1 619 ? 85.141 64.888 51.701 1.00 58.05 ? 633 LEU A CG 1 ATOM 4834 C CD1 . LEU A 1 619 ? 84.534 64.194 52.912 1.00 55.40 ? 633 LEU A CD1 1 ATOM 4835 C CD2 . LEU A 1 619 ? 84.169 65.894 51.107 1.00 55.76 ? 633 LEU A CD2 1 ATOM 4836 N N . TRP A 1 620 ? 88.709 63.936 50.601 1.00 63.33 ? 634 TRP A N 1 ATOM 4837 C CA . TRP A 1 620 ? 89.213 63.037 49.561 1.00 60.59 ? 634 TRP A CA 1 ATOM 4838 C C . TRP A 1 620 ? 90.622 63.477 49.153 1.00 59.60 ? 634 TRP A C 1 ATOM 4839 O O . TRP A 1 620 ? 90.950 64.666 49.228 1.00 60.78 ? 634 TRP A O 1 ATOM 4840 C CB . TRP A 1 620 ? 88.263 63.003 48.358 1.00 60.53 ? 634 TRP A CB 1 ATOM 4841 C CG . TRP A 1 620 ? 87.893 64.362 47.839 1.00 59.01 ? 634 TRP A CG 1 ATOM 4842 C CD1 . TRP A 1 620 ? 86.900 65.166 48.298 1.00 57.73 ? 634 TRP A CD1 1 ATOM 4843 C CD2 . TRP A 1 620 ? 88.518 65.070 46.759 1.00 59.57 ? 634 TRP A CD2 1 ATOM 4844 N NE1 . TRP A 1 620 ? 86.862 66.334 47.572 1.00 56.05 ? 634 TRP A NE1 1 ATOM 4845 C CE2 . TRP A 1 620 ? 87.845 66.300 46.621 1.00 55.87 ? 634 TRP A CE2 1 ATOM 4846 C CE3 . TRP A 1 620 ? 89.579 64.783 45.898 1.00 60.74 ? 634 TRP A CE3 1 ATOM 4847 C CZ2 . TRP A 1 620 ? 88.198 67.240 45.655 1.00 53.76 ? 634 TRP A CZ2 1 ATOM 4848 C CZ3 . TRP A 1 620 ? 89.919 65.711 44.934 1.00 59.82 ? 634 TRP A CZ3 1 ATOM 4849 C CH2 . TRP A 1 620 ? 89.244 66.927 44.826 1.00 56.15 ? 634 TRP A CH2 1 ATOM 4850 N N . LYS A 1 621 ? 91.460 62.522 48.744 1.00 60.36 ? 635 LYS A N 1 ATOM 4851 C CA . LYS A 1 621 ? 92.884 62.787 48.493 1.00 62.75 ? 635 LYS A CA 1 ATOM 4852 C C . LYS A 1 621 ? 93.435 61.901 47.376 1.00 63.37 ? 635 LYS A C 1 ATOM 4853 O O . LYS A 1 621 ? 92.908 60.815 47.125 1.00 62.87 ? 635 LYS A O 1 ATOM 4854 C CB . LYS A 1 621 ? 93.708 62.560 49.768 1.00 59.04 ? 635 LYS A CB 1 ATOM 4855 N N . ASN A 1 622 ? 94.506 62.356 46.730 1.00 65.22 ? 636 ASN A N 1 ATOM 4856 C CA . ASN A 1 622 ? 95.082 61.652 45.579 1.00 71.71 ? 636 ASN A CA 1 ATOM 4857 C C . ASN A 1 622 ? 94.066 61.112 44.562 1.00 71.79 ? 636 ASN A C 1 ATOM 4858 O O . ASN A 1 622 ? 94.170 59.972 44.106 1.00 72.36 ? 636 ASN A O 1 ATOM 4859 C CB . ASN A 1 622 ? 96.049 60.554 46.022 1.00 78.40 ? 636 ASN A CB 1 ATOM 4860 C CG . ASN A 1 622 ? 97.460 61.078 46.216 1.00 86.29 ? 636 ASN A CG 1 ATOM 4861 O OD1 . ASN A 1 622 ? 97.706 62.277 46.063 1.00 88.85 ? 636 ASN A OD1 1 ATOM 4862 N ND2 . ASN A 1 622 ? 98.393 60.190 46.559 1.00 87.75 ? 636 ASN A ND2 1 ATOM 4863 N N . VAL A 1 623 ? 93.077 61.933 44.226 1.00 70.44 ? 637 VAL A N 1 ATOM 4864 C CA . VAL A 1 623 ? 92.144 61.588 43.159 1.00 69.62 ? 637 VAL A CA 1 ATOM 4865 C C . VAL A 1 623 ? 92.730 62.024 41.810 1.00 69.22 ? 637 VAL A C 1 ATOM 4866 O O . VAL A 1 623 ? 93.216 63.152 41.661 1.00 67.31 ? 637 VAL A O 1 ATOM 4867 C CB . VAL A 1 623 ? 90.748 62.187 43.409 1.00 67.29 ? 637 VAL A CB 1 ATOM 4868 C CG1 . VAL A 1 623 ? 89.806 61.852 42.274 1.00 64.67 ? 637 VAL A CG1 1 ATOM 4869 C CG2 . VAL A 1 623 ? 90.187 61.644 44.705 1.00 67.09 ? 637 VAL A CG2 1 ATOM 4870 N N . ARG A 1 624 ? 92.727 61.105 40.848 1.00 70.69 ? 638 ARG A N 1 ATOM 4871 C CA . ARG A 1 624 ? 93.282 61.374 39.526 1.00 72.83 ? 638 ARG A CA 1 ATOM 4872 C C . ARG A 1 624 ? 92.415 62.355 38.744 1.00 67.88 ? 638 ARG A C 1 ATOM 4873 O O . ARG A 1 624 ? 91.199 62.172 38.631 1.00 61.65 ? 638 ARG A O 1 ATOM 4874 C CB . ARG A 1 624 ? 93.417 60.081 38.719 1.00 77.32 ? 638 ARG A CB 1 ATOM 4875 C CG . ARG A 1 624 ? 94.653 59.264 39.026 1.00 84.58 ? 638 ARG A CG 1 ATOM 4876 C CD . ARG A 1 624 ? 95.028 58.427 37.816 1.00 90.37 ? 638 ARG A CD 1 ATOM 4877 N NE . ARG A 1 624 ? 95.158 59.263 36.622 1.00 92.80 ? 638 ARG A NE 1 ATOM 4878 C CZ . ARG A 1 624 ? 95.533 58.821 35.424 1.00 95.09 ? 638 ARG A CZ 1 ATOM 4879 N NH1 . ARG A 1 624 ? 95.821 57.537 35.243 1.00 97.83 ? 638 ARG A NH1 1 ATOM 4880 N NH2 . ARG A 1 624 ? 95.625 59.667 34.405 1.00 94.29 ? 638 ARG A NH2 1 ATOM 4881 N N . VAL A 1 625 ? 93.049 63.399 38.215 1.00 68.18 ? 639 VAL A N 1 ATOM 4882 C CA . VAL A 1 625 ? 92.382 64.326 37.303 1.00 64.93 ? 639 VAL A CA 1 ATOM 4883 C C . VAL A 1 625 ? 93.103 64.267 35.963 1.00 64.47 ? 639 VAL A C 1 ATOM 4884 O O . VAL A 1 625 ? 94.216 63.740 35.887 1.00 65.59 ? 639 VAL A O 1 ATOM 4885 C CB . VAL A 1 625 ? 92.411 65.774 37.835 1.00 62.29 ? 639 VAL A CB 1 ATOM 4886 C CG1 . VAL A 1 625 ? 91.531 65.909 39.060 1.00 60.90 ? 639 VAL A CG1 1 ATOM 4887 C CG2 . VAL A 1 625 ? 93.843 66.203 38.146 1.00 62.39 ? 639 VAL A CG2 1 ATOM 4888 N N . LYS A 1 626 ? 92.485 64.791 34.908 1.00 63.85 ? 640 LYS A N 1 ATOM 4889 C CA . LYS A 1 626 ? 93.183 64.855 33.628 1.00 65.83 ? 640 LYS A CA 1 ATOM 4890 C C . LYS A 1 626 ? 94.342 65.831 33.709 1.00 66.04 ? 640 LYS A C 1 ATOM 4891 O O . LYS A 1 626 ? 94.242 66.885 34.360 1.00 63.41 ? 640 LYS A O 1 ATOM 4892 C CB . LYS A 1 626 ? 92.248 65.214 32.477 1.00 66.20 ? 640 LYS A CB 1 ATOM 4893 C CG . LYS A 1 626 ? 91.611 63.991 31.843 1.00 70.46 ? 640 LYS A CG 1 ATOM 4894 C CD . LYS A 1 626 ? 90.691 64.361 30.689 1.00 72.17 ? 640 LYS A CD 1 ATOM 4895 C CE . LYS A 1 626 ? 91.467 64.952 29.519 1.00 74.03 ? 640 LYS A CE 1 ATOM 4896 N NZ . LYS A 1 626 ? 91.053 66.356 29.220 1.00 71.66 ? 640 LYS A NZ 1 ATOM 4897 N N . TYR A 1 627 ? 95.451 65.450 33.075 1.00 67.46 ? 641 TYR A N 1 ATOM 4898 C CA . TYR A 1 627 ? 96.648 66.276 33.020 1.00 70.01 ? 641 TYR A CA 1 ATOM 4899 C C . TYR A 1 627 ? 97.341 66.013 31.688 1.00 74.37 ? 641 TYR A C 1 ATOM 4900 O O . TYR A 1 627 ? 97.320 64.885 31.199 1.00 76.43 ? 641 TYR A O 1 ATOM 4901 C CB . TYR A 1 627 ? 97.585 65.955 34.190 1.00 70.17 ? 641 TYR A CB 1 ATOM 4902 C CG . TYR A 1 627 ? 98.740 66.919 34.323 1.00 69.79 ? 641 TYR A CG 1 ATOM 4903 C CD1 . TYR A 1 627 ? 98.549 68.194 34.840 1.00 69.04 ? 641 TYR A CD1 1 ATOM 4904 C CD2 . TYR A 1 627 ? 100.024 66.559 33.923 1.00 70.66 ? 641 TYR A CD2 1 ATOM 4905 C CE1 . TYR A 1 627 ? 99.608 69.086 34.958 1.00 70.67 ? 641 TYR A CE1 1 ATOM 4906 C CE2 . TYR A 1 627 ? 101.082 67.438 34.040 1.00 71.91 ? 641 TYR A CE2 1 ATOM 4907 C CZ . TYR A 1 627 ? 100.873 68.700 34.557 1.00 71.95 ? 641 TYR A CZ 1 ATOM 4908 O OH . TYR A 1 627 ? 101.935 69.578 34.672 1.00 73.24 ? 641 TYR A OH 1 ATOM 4909 N N . PRO A 1 628 ? 97.926 67.055 31.072 1.00 76.71 ? 642 PRO A N 1 ATOM 4910 C CA . PRO A 1 628 ? 97.920 68.458 31.501 1.00 77.08 ? 642 PRO A CA 1 ATOM 4911 C C . PRO A 1 628 ? 96.563 69.127 31.340 1.00 74.82 ? 642 PRO A C 1 ATOM 4912 O O . PRO A 1 628 ? 95.761 68.745 30.483 1.00 74.76 ? 642 PRO A O 1 ATOM 4913 C CB . PRO A 1 628 ? 98.937 69.116 30.562 1.00 79.44 ? 642 PRO A CB 1 ATOM 4914 C CG . PRO A 1 628 ? 98.924 68.266 29.344 1.00 79.60 ? 642 PRO A CG 1 ATOM 4915 C CD . PRO A 1 628 ? 98.725 66.863 29.847 1.00 79.50 ? 642 PRO A CD 1 ATOM 4916 N N . GLY A 1 629 ? 96.313 70.114 32.191 1.00 73.74 ? 643 GLY A N 1 ATOM 4917 C CA . GLY A 1 629 ? 95.116 70.927 32.106 1.00 69.43 ? 643 GLY A CA 1 ATOM 4918 C C . GLY A 1 629 ? 95.452 72.277 32.704 1.00 67.29 ? 643 GLY A C 1 ATOM 4919 O O . GLY A 1 629 ? 96.301 72.363 33.607 1.00 66.06 ? 643 GLY A O 1 ATOM 4920 N N . HIS A 1 630 ? 94.819 73.330 32.192 1.00 65.19 ? 644 HIS A N 1 ATOM 4921 C CA . HIS A 1 630 ? 95.015 74.680 32.724 1.00 64.49 ? 644 HIS A CA 1 ATOM 4922 C C . HIS A 1 630 ? 93.706 75.465 32.671 1.00 61.79 ? 644 HIS A C 1 ATOM 4923 O O . HIS A 1 630 ? 92.817 75.128 31.888 1.00 60.18 ? 644 HIS A O 1 ATOM 4924 C CB . HIS A 1 630 ? 96.145 75.415 31.981 1.00 66.98 ? 644 HIS A CB 1 ATOM 4925 C CG . HIS A 1 630 ? 95.924 75.547 30.503 1.00 68.23 ? 644 HIS A CG 1 ATOM 4926 N ND1 . HIS A 1 630 ? 95.219 76.593 29.944 1.00 67.99 ? 644 HIS A ND1 1 ATOM 4927 C CD2 . HIS A 1 630 ? 96.322 74.771 29.469 1.00 70.06 ? 644 HIS A CD2 1 ATOM 4928 C CE1 . HIS A 1 630 ? 95.191 76.454 28.629 1.00 67.55 ? 644 HIS A CE1 1 ATOM 4929 N NE2 . HIS A 1 630 ? 95.847 75.350 28.315 1.00 69.44 ? 644 HIS A NE2 1 ATOM 4930 N N . GLY A 1 631 ? 93.572 76.492 33.508 1.00 60.06 ? 645 GLY A N 1 ATOM 4931 C CA . GLY A 1 631 ? 92.337 77.264 33.537 1.00 58.64 ? 645 GLY A CA 1 ATOM 4932 C C . GLY A 1 631 ? 92.107 78.011 34.839 1.00 57.76 ? 645 GLY A C 1 ATOM 4933 O O . GLY A 1 631 ? 92.855 77.831 35.798 1.00 60.27 ? 645 GLY A O 1 ATOM 4934 N N . TRP A 1 632 ? 91.063 78.837 34.877 1.00 54.12 ? 646 TRP A N 1 ATOM 4935 C CA . TRP A 1 632 ? 90.791 79.700 36.026 1.00 54.32 ? 646 TRP A CA 1 ATOM 4936 C C . TRP A 1 632 ? 90.361 78.956 37.293 1.00 52.20 ? 646 TRP A C 1 ATOM 4937 O O . TRP A 1 632 ? 90.075 77.753 37.261 1.00 52.78 ? 646 TRP A O 1 ATOM 4938 C CB . TRP A 1 632 ? 89.682 80.706 35.681 1.00 53.53 ? 646 TRP A CB 1 ATOM 4939 C CG . TRP A 1 632 ? 90.025 81.656 34.566 1.00 53.81 ? 646 TRP A CG 1 ATOM 4940 C CD1 . TRP A 1 632 ? 90.939 82.673 34.599 1.00 55.53 ? 646 TRP A CD1 1 ATOM 4941 C CD2 . TRP A 1 632 ? 89.426 81.695 33.261 1.00 50.70 ? 646 TRP A CD2 1 ATOM 4942 N NE1 . TRP A 1 632 ? 90.954 83.331 33.387 1.00 55.19 ? 646 TRP A NE1 1 ATOM 4943 C CE2 . TRP A 1 632 ? 90.036 82.752 32.550 1.00 52.03 ? 646 TRP A CE2 1 ATOM 4944 C CE3 . TRP A 1 632 ? 88.440 80.934 32.627 1.00 47.62 ? 646 TRP A CE3 1 ATOM 4945 C CZ2 . TRP A 1 632 ? 89.696 83.061 31.226 1.00 51.89 ? 646 TRP A CZ2 1 ATOM 4946 C CZ3 . TRP A 1 632 ? 88.096 81.245 31.306 1.00 52.85 ? 646 TRP A CZ3 1 ATOM 4947 C CH2 . TRP A 1 632 ? 88.725 82.300 30.624 1.00 53.62 ? 646 TRP A CH2 1 ATOM 4948 N N . ALA A 1 633 ? 90.311 79.696 38.401 1.00 48.02 ? 647 ALA A N 1 ATOM 4949 C CA . ALA A 1 633 ? 89.594 79.256 39.598 1.00 49.37 ? 647 ALA A CA 1 ATOM 4950 C C . ALA A 1 633 ? 88.164 79.741 39.462 1.00 47.43 ? 647 ALA A C 1 ATOM 4951 O O . ALA A 1 633 ? 87.895 80.687 38.708 1.00 46.27 ? 647 ALA A O 1 ATOM 4952 C CB . ALA A 1 633 ? 90.220 79.834 40.859 1.00 51.11 ? 647 ALA A CB 1 ATOM 4953 N N . ALA A 1 634 ? 87.248 79.100 40.182 1.00 48.46 ? 648 ALA A N 1 ATOM 4954 C CA . ALA A 1 634 ? 85.853 79.508 40.138 1.00 46.10 ? 648 ALA A CA 1 ATOM 4955 C C . ALA A 1 634 ? 85.064 79.150 41.406 1.00 44.82 ? 648 ALA A C 1 ATOM 4956 O O . ALA A 1 634 ? 85.489 78.329 42.225 1.00 46.41 ? 648 ALA A O 1 ATOM 4957 C CB . ALA A 1 634 ? 85.164 78.914 38.904 1.00 43.15 ? 648 ALA A CB 1 ATOM 4958 N N . ILE A 1 635 ? 83.904 79.779 41.545 1.00 42.54 ? 649 ILE A N 1 ATOM 4959 C CA . ILE A 1 635 ? 82.949 79.430 42.580 1.00 46.47 ? 649 ILE A CA 1 ATOM 4960 C C . ILE A 1 635 ? 81.579 79.375 41.908 1.00 44.02 ? 649 ILE A C 1 ATOM 4961 O O . ILE A 1 635 ? 81.401 79.953 40.820 1.00 42.64 ? 649 ILE A O 1 ATOM 4962 C CB . ILE A 1 635 ? 82.922 80.489 43.690 1.00 40.86 ? 649 ILE A CB 1 ATOM 4963 C CG1 . ILE A 1 635 ? 82.498 81.837 43.096 1.00 41.32 ? 649 ILE A CG1 1 ATOM 4964 C CG2 . ILE A 1 635 ? 84.292 80.611 44.363 1.00 41.98 ? 649 ILE A CG2 1 ATOM 4965 C CD1 . ILE A 1 635 ? 82.403 82.960 44.123 1.00 42.85 ? 649 ILE A CD1 1 ATOM 4966 N N . GLY A 1 636 ? 80.611 78.701 42.535 1.00 42.70 ? 650 GLY A N 1 ATOM 4967 C CA . GLY A 1 636 ? 79.264 78.678 41.990 1.00 39.97 ? 650 GLY A CA 1 ATOM 4968 C C . GLY A 1 636 ? 78.224 77.912 42.793 1.00 42.41 ? 650 GLY A C 1 ATOM 4969 O O . GLY A 1 636 ? 78.482 77.457 43.922 1.00 44.13 ? 650 GLY A O 1 ATOM 4970 N N . THR A 1 637 ? 77.038 77.773 42.200 1.00 42.30 ? 651 THR A N 1 ATOM 4971 C CA . THR A 1 637 ? 75.910 77.108 42.855 1.00 44.89 ? 651 THR A CA 1 ATOM 4972 C C . THR A 1 637 ? 75.298 76.060 41.928 1.00 43.95 ? 651 THR A C 1 ATOM 4973 O O . THR A 1 637 ? 75.362 76.183 40.695 1.00 39.83 ? 651 THR A O 1 ATOM 4974 C CB . THR A 1 637 ? 74.810 78.109 43.266 1.00 45.40 ? 651 THR A CB 1 ATOM 4975 O OG1 . THR A 1 637 ? 74.080 78.528 42.107 1.00 45.79 ? 651 THR A OG1 1 ATOM 4976 C CG2 . THR A 1 637 ? 75.415 79.328 43.936 1.00 46.65 ? 651 THR A CG2 1 ATOM 4977 N N . HIS A 1 638 ? 74.705 75.026 42.517 1.00 43.01 ? 652 HIS A N 1 ATOM 4978 C CA . HIS A 1 638 ? 74.209 73.917 41.720 1.00 43.98 ? 652 HIS A CA 1 ATOM 4979 C C . HIS A 1 638 ? 73.160 74.348 40.690 1.00 43.90 ? 652 HIS A C 1 ATOM 4980 O O . HIS A 1 638 ? 73.273 74.004 39.513 1.00 44.09 ? 652 HIS A O 1 ATOM 4981 C CB . HIS A 1 638 ? 73.663 72.801 42.602 1.00 45.59 ? 652 HIS A CB 1 ATOM 4982 C CG . HIS A 1 638 ? 73.224 71.603 41.827 1.00 46.29 ? 652 HIS A CG 1 ATOM 4983 N ND1 . HIS A 1 638 ? 71.905 71.211 41.747 1.00 47.07 ? 652 HIS A ND1 1 ATOM 4984 C CD2 . HIS A 1 638 ? 73.922 70.736 41.059 1.00 48.24 ? 652 HIS A CD2 1 ATOM 4985 C CE1 . HIS A 1 638 ? 71.814 70.147 40.969 1.00 48.49 ? 652 HIS A CE1 1 ATOM 4986 N NE2 . HIS A 1 638 ? 73.025 69.837 40.541 1.00 50.09 ? 652 HIS A NE2 1 ATOM 4987 N N . THR A 1 639 ? 72.147 75.095 41.126 1.00 42.81 ? 653 THR A N 1 ATOM 4988 C CA . THR A 1 639 ? 71.191 75.689 40.189 1.00 40.13 ? 653 THR A CA 1 ATOM 4989 C C . THR A 1 639 ? 71.108 77.210 40.373 1.00 39.63 ? 653 THR A C 1 ATOM 4990 O O . THR A 1 639 ? 72.012 77.819 40.947 1.00 40.19 ? 653 THR A O 1 ATOM 4991 C CB . THR A 1 639 ? 69.797 75.046 40.294 1.00 40.99 ? 653 THR A CB 1 ATOM 4992 O OG1 . THR A 1 639 ? 68.956 75.559 39.250 1.00 51.53 ? 653 THR A OG1 1 ATOM 4993 C CG2 . THR A 1 639 ? 69.165 75.333 41.638 1.00 36.92 ? 653 THR A CG2 1 ATOM 4994 N N . PHE A 1 640 ? 70.048 77.823 39.858 1.00 35.75 ? 654 PHE A N 1 ATOM 4995 C CA . PHE A 1 640 ? 69.809 79.242 40.100 1.00 36.98 ? 654 PHE A CA 1 ATOM 4996 C C . PHE A 1 640 ? 69.219 79.376 41.500 1.00 37.59 ? 654 PHE A C 1 ATOM 4997 O O . PHE A 1 640 ? 67.997 79.296 41.686 1.00 35.03 ? 654 PHE A O 1 ATOM 4998 C CB . PHE A 1 640 ? 68.905 79.829 38.998 1.00 32.99 ? 654 PHE A CB 1 ATOM 4999 C CG . PHE A 1 640 ? 69.580 79.869 37.636 1.00 36.05 ? 654 PHE A CG 1 ATOM 5000 C CD1 . PHE A 1 640 ? 70.418 80.915 37.295 1.00 33.82 ? 654 PHE A CD1 1 ATOM 5001 C CD2 . PHE A 1 640 ? 69.415 78.831 36.727 1.00 36.42 ? 654 PHE A CD2 1 ATOM 5002 C CE1 . PHE A 1 640 ? 71.073 80.942 36.066 1.00 33.47 ? 654 PHE A CE1 1 ATOM 5003 C CE2 . PHE A 1 640 ? 70.054 78.850 35.503 1.00 36.00 ? 654 PHE A CE2 1 ATOM 5004 C CZ . PHE A 1 640 ? 70.893 79.908 35.169 1.00 36.15 ? 654 PHE A CZ 1 ATOM 5005 N N . GLU A 1 641 ? 70.104 79.534 42.486 1.00 35.60 ? 655 GLU A N 1 ATOM 5006 C CA . GLU A 1 641 ? 69.713 79.467 43.896 1.00 40.85 ? 655 GLU A CA 1 ATOM 5007 C C . GLU A 1 641 ? 70.602 80.385 44.737 1.00 40.97 ? 655 GLU A C 1 ATOM 5008 O O . GLU A 1 641 ? 71.766 80.604 44.393 1.00 38.69 ? 655 GLU A O 1 ATOM 5009 C CB . GLU A 1 641 ? 69.869 78.026 44.399 1.00 44.66 ? 655 GLU A CB 1 ATOM 5010 C CG . GLU A 1 641 ? 71.341 77.581 44.469 1.00 51.31 ? 655 GLU A CG 1 ATOM 5011 C CD . GLU A 1 641 ? 71.532 76.111 44.790 1.00 55.41 ? 655 GLU A CD 1 ATOM 5012 O OE1 . GLU A 1 641 ? 71.617 75.777 45.987 1.00 57.76 ? 655 GLU A OE1 1 ATOM 5013 O OE2 . GLU A 1 641 ? 71.627 75.295 43.846 1.00 57.81 ? 655 GLU A OE2 1 ATOM 5014 N N . PHE A 1 642 ? 70.063 80.892 45.849 1.00 36.89 ? 656 PHE A N 1 ATOM 5015 C CA . PHE A 1 642 ? 70.831 81.752 46.748 1.00 43.60 ? 656 PHE A CA 1 ATOM 5016 C C . PHE A 1 642 ? 71.939 80.972 47.463 1.00 42.60 ? 656 PHE A C 1 ATOM 5017 O O . PHE A 1 642 ? 71.750 79.821 47.868 1.00 42.40 ? 656 PHE A O 1 ATOM 5018 C CB . PHE A 1 642 ? 69.911 82.444 47.774 1.00 47.44 ? 656 PHE A CB 1 ATOM 5019 C CG . PHE A 1 642 ? 68.864 83.351 47.156 1.00 48.52 ? 656 PHE A CG 1 ATOM 5020 C CD1 . PHE A 1 642 ? 69.238 84.529 46.509 1.00 52.12 ? 656 PHE A CD1 1 ATOM 5021 C CD2 . PHE A 1 642 ? 67.510 83.043 47.247 1.00 48.39 ? 656 PHE A CD2 1 ATOM 5022 C CE1 . PHE A 1 642 ? 68.280 85.369 45.938 1.00 51.02 ? 656 PHE A CE1 1 ATOM 5023 C CE2 . PHE A 1 642 ? 66.551 83.876 46.683 1.00 48.48 ? 656 PHE A CE2 1 ATOM 5024 C CZ . PHE A 1 642 ? 66.942 85.043 46.028 1.00 48.14 ? 656 PHE A CZ 1 ATOM 5025 N N . ALA A 1 643 ? 73.095 81.609 47.607 1.00 42.35 ? 657 ALA A N 1 ATOM 5026 C CA . ALA A 1 643 ? 74.254 81.010 48.262 1.00 43.40 ? 657 ALA A CA 1 ATOM 5027 C C . ALA A 1 643 ? 75.207 82.132 48.551 1.00 44.98 ? 657 ALA A C 1 ATOM 5028 O O . ALA A 1 643 ? 75.201 83.134 47.831 1.00 46.34 ? 657 ALA A O 1 ATOM 5029 C CB . ALA A 1 643 ? 74.921 80.005 47.362 1.00 45.94 ? 657 ALA A CB 1 ATOM 5030 N N . GLN A 1 644 ? 76.029 81.973 49.583 1.00 41.17 ? 658 GLN A N 1 ATOM 5031 C CA . GLN A 1 644 ? 77.027 82.982 49.914 1.00 43.21 ? 658 GLN A CA 1 ATOM 5032 C C . GLN A 1 644 ? 78.438 82.413 49.972 1.00 45.47 ? 658 GLN A C 1 ATOM 5033 O O . GLN A 1 644 ? 78.639 81.215 50.187 1.00 46.25 ? 658 GLN A O 1 ATOM 5034 C CB . GLN A 1 644 ? 76.693 83.661 51.249 1.00 42.73 ? 658 GLN A CB 1 ATOM 5035 C CG . GLN A 1 644 ? 75.405 84.454 51.212 1.00 42.32 ? 658 GLN A CG 1 ATOM 5036 C CD . GLN A 1 644 ? 74.989 84.930 52.590 1.00 46.30 ? 658 GLN A CD 1 ATOM 5037 O OE1 . GLN A 1 644 ? 75.796 85.503 53.339 1.00 47.91 ? 658 GLN A OE1 1 ATOM 5038 N NE2 . GLN A 1 644 ? 73.734 84.678 52.943 1.00 43.43 ? 658 GLN A NE2 1 ATOM 5039 N N . PHE A 1 645 ? 79.413 83.295 49.800 1.00 47.30 ? 659 PHE A N 1 ATOM 5040 C CA . PHE A 1 645 ? 80.810 82.914 49.774 1.00 43.21 ? 659 PHE A CA 1 ATOM 5041 C C . PHE A 1 645 ? 81.544 83.982 50.575 1.00 44.75 ? 659 PHE A C 1 ATOM 5042 O O . PHE A 1 645 ? 81.122 85.142 50.601 1.00 44.06 ? 659 PHE A O 1 ATOM 5043 C CB . PHE A 1 645 ? 81.298 82.878 48.322 1.00 42.43 ? 659 PHE A CB 1 ATOM 5044 C CG . PHE A 1 645 ? 80.496 81.953 47.434 1.00 41.49 ? 659 PHE A CG 1 ATOM 5045 C CD1 . PHE A 1 645 ? 79.326 82.387 46.823 1.00 40.54 ? 659 PHE A CD1 1 ATOM 5046 C CD2 . PHE A 1 645 ? 80.917 80.645 47.214 1.00 47.95 ? 659 PHE A CD2 1 ATOM 5047 C CE1 . PHE A 1 645 ? 78.584 81.535 45.997 1.00 39.74 ? 659 PHE A CE1 1 ATOM 5048 C CE2 . PHE A 1 645 ? 80.185 79.788 46.400 1.00 40.89 ? 659 PHE A CE2 1 ATOM 5049 C CZ . PHE A 1 645 ? 79.016 80.233 45.789 1.00 42.15 ? 659 PHE A CZ 1 ATOM 5050 N N . ASP A 1 646 ? 82.630 83.600 51.238 1.00 47.00 ? 660 ASP A N 1 ATOM 5051 C CA . ASP A 1 646 ? 83.354 84.531 52.089 1.00 49.09 ? 660 ASP A CA 1 ATOM 5052 C C . ASP A 1 646 ? 84.802 84.090 52.146 1.00 49.41 ? 660 ASP A C 1 ATOM 5053 O O . ASP A 1 646 ? 85.081 82.905 51.960 1.00 50.31 ? 660 ASP A O 1 ATOM 5054 C CB . ASP A 1 646 ? 82.753 84.514 53.500 1.00 51.55 ? 660 ASP A CB 1 ATOM 5055 C CG . ASP A 1 646 ? 83.070 85.764 54.276 1.00 52.66 ? 660 ASP A CG 1 ATOM 5056 O OD1 . ASP A 1 646 ? 83.888 86.563 53.789 1.00 51.08 ? 660 ASP A OD1 1 ATOM 5057 O OD2 . ASP A 1 646 ? 82.509 85.956 55.378 1.00 58.65 ? 660 ASP A OD2 1 ATOM 5058 N N . ASN A 1 647 ? 85.711 85.029 52.421 1.00 50.41 ? 661 ASN A N 1 ATOM 5059 C CA . ASN A 1 647 ? 87.130 84.732 52.610 1.00 52.84 ? 661 ASN A CA 1 ATOM 5060 C C . ASN A 1 647 ? 87.729 83.871 51.497 1.00 54.33 ? 661 ASN A C 1 ATOM 5061 O O . ASN A 1 647 ? 88.271 82.797 51.752 1.00 56.34 ? 661 ASN A O 1 ATOM 5062 C CB . ASN A 1 647 ? 87.376 84.084 53.981 1.00 56.25 ? 661 ASN A CB 1 ATOM 5063 C CG . ASN A 1 647 ? 86.661 84.809 55.109 1.00 59.71 ? 661 ASN A CG 1 ATOM 5064 O OD1 . ASN A 1 647 ? 86.765 86.027 55.249 1.00 61.86 ? 661 ASN A OD1 1 ATOM 5065 N ND2 . ASN A 1 647 ? 85.923 84.061 55.914 1.00 50.88 ? 661 ASN A ND2 1 ATOM 5066 N N . PHE A 1 648 ? 87.624 84.353 50.262 1.00 51.69 ? 662 PHE A N 1 ATOM 5067 C CA . PHE A 1 648 ? 88.146 83.644 49.105 1.00 48.35 ? 662 PHE A CA 1 ATOM 5068 C C . PHE A 1 648 ? 89.646 83.786 49.050 1.00 49.50 ? 662 PHE A C 1 ATOM 5069 O O . PHE A 1 648 ? 90.163 84.883 49.251 1.00 49.41 ? 662 PHE A O 1 ATOM 5070 C CB . PHE A 1 648 ? 87.567 84.250 47.825 1.00 47.81 ? 662 PHE A CB 1 ATOM 5071 C CG . PHE A 1 648 ? 88.056 83.590 46.566 1.00 51.74 ? 662 PHE A CG 1 ATOM 5072 C CD1 . PHE A 1 648 ? 87.404 82.479 46.059 1.00 49.34 ? 662 PHE A CD1 1 ATOM 5073 C CD2 . PHE A 1 648 ? 89.166 84.083 45.885 1.00 53.98 ? 662 PHE A CD2 1 ATOM 5074 C CE1 . PHE A 1 648 ? 87.843 81.870 44.894 1.00 49.74 ? 662 PHE A CE1 1 ATOM 5075 C CE2 . PHE A 1 648 ? 89.610 83.473 44.712 1.00 54.33 ? 662 PHE A CE2 1 ATOM 5076 C CZ . PHE A 1 648 ? 88.947 82.365 44.221 1.00 51.44 ? 662 PHE A CZ 1 ATOM 5077 N N . ARG A 1 649 ? 90.338 82.690 48.743 1.00 49.67 ? 663 ARG A N 1 ATOM 5078 C CA . ARG A 1 649 ? 91.793 82.725 48.567 1.00 52.78 ? 663 ARG A CA 1 ATOM 5079 C C . ARG A 1 649 ? 92.225 81.774 47.458 1.00 54.48 ? 663 ARG A C 1 ATOM 5080 O O . ARG A 1 649 ? 91.631 80.707 47.264 1.00 55.01 ? 663 ARG A O 1 ATOM 5081 C CB . ARG A 1 649 ? 92.517 82.366 49.868 1.00 50.60 ? 663 ARG A CB 1 ATOM 5082 N N . VAL A 1 650 ? 93.263 82.167 46.731 1.00 53.82 ? 664 VAL A N 1 ATOM 5083 C CA . VAL A 1 650 ? 93.819 81.313 45.694 1.00 55.84 ? 664 VAL A CA 1 ATOM 5084 C C . VAL A 1 650 ? 95.343 81.426 45.671 1.00 57.52 ? 664 VAL A C 1 ATOM 5085 O O . VAL A 1 650 ? 95.916 82.521 45.761 1.00 55.12 ? 664 VAL A O 1 ATOM 5086 C CB . VAL A 1 650 ? 93.211 81.615 44.286 1.00 58.21 ? 664 VAL A CB 1 ATOM 5087 C CG1 . VAL A 1 650 ? 93.542 83.035 43.842 1.00 53.14 ? 664 VAL A CG1 1 ATOM 5088 C CG2 . VAL A 1 650 ? 93.700 80.598 43.260 1.00 57.59 ? 664 VAL A CG2 1 ATOM 5089 N N . GLU A 1 651 ? 95.987 80.271 45.578 1.00 58.20 ? 665 GLU A N 1 ATOM 5090 C CA . GLU A 1 651 ? 97.430 80.189 45.524 1.00 63.25 ? 665 GLU A CA 1 ATOM 5091 C C . GLU A 1 651 ? 97.717 79.331 44.314 1.00 60.57 ? 665 GLU A C 1 ATOM 5092 O O . GLU A 1 651 ? 97.296 78.172 44.266 1.00 61.89 ? 665 GLU A O 1 ATOM 5093 C CB . GLU A 1 651 ? 97.928 79.494 46.785 1.00 67.64 ? 665 GLU A CB 1 ATOM 5094 C CG . GLU A 1 651 ? 99.414 79.593 47.053 1.00 74.70 ? 665 GLU A CG 1 ATOM 5095 C CD . GLU A 1 651 ? 99.726 79.298 48.517 1.00 81.12 ? 665 GLU A CD 1 ATOM 5096 O OE1 . GLU A 1 651 ? 99.187 78.303 49.060 1.00 80.60 ? 665 GLU A OE1 1 ATOM 5097 O OE2 . GLU A 1 651 ? 100.484 80.078 49.134 1.00 86.36 ? 665 GLU A OE2 1 ATOM 5098 N N . ALA A 1 652 ? 98.414 79.877 43.325 1.00 60.12 ? 666 ALA A N 1 ATOM 5099 C CA . ALA A 1 652 ? 98.554 79.142 42.065 1.00 63.82 ? 666 ALA A CA 1 ATOM 5100 C C . ALA A 1 652 ? 99.899 79.318 41.373 1.00 69.34 ? 666 ALA A C 1 ATOM 5101 O O . ALA A 1 652 ? 100.591 80.319 41.565 1.00 70.35 ? 666 ALA A O 1 ATOM 5102 C CB . ALA A 1 652 ? 97.413 79.489 41.109 1.00 58.08 ? 666 ALA A CB 1 ATOM 5103 N N . ALA A 1 653 ? 100.256 78.324 40.569 1.00 72.30 ? 667 ALA A N 1 ATOM 5104 C CA . ALA A 1 653 ? 101.470 78.384 39.767 1.00 76.51 ? 667 ALA A CA 1 ATOM 5105 C C . ALA A 1 653 ? 101.100 78.345 38.285 1.00 77.08 ? 667 ALA A C 1 ATOM 5106 O O . ALA A 1 653 ? 100.333 77.483 37.841 1.00 71.84 ? 667 ALA A O 1 ATOM 5107 C CB . ALA A 1 653 ? 102.409 77.242 40.127 1.00 76.80 ? 667 ALA A CB 1 ATOM 5108 N N . ARG A 1 654 ? 101.643 79.292 37.528 1.00 81.82 ? 668 ARG A N 1 ATOM 5109 C CA . ARG A 1 654 ? 101.312 79.432 36.117 1.00 85.10 ? 668 ARG A CA 1 ATOM 5110 C C . ARG A 1 654 ? 102.117 78.465 35.244 1.00 90.22 ? 668 ARG A C 1 ATOM 5111 O O . ARG A 1 654 ? 101.651 77.356 34.963 1.00 92.05 ? 668 ARG A O 1 ATOM 5112 C CB . ARG A 1 654 ? 101.507 80.887 35.678 1.00 83.65 ? 668 ARG A CB 1 ATOM 5113 C CG . ARG A 1 654 ? 101.292 81.132 34.207 1.00 82.55 ? 668 ARG A CG 1 ATOM 5114 C CD . ARG A 1 654 ? 101.056 82.598 33.924 1.00 82.26 ? 668 ARG A CD 1 ATOM 5115 N NE . ARG A 1 654 ? 101.373 82.931 32.539 1.00 82.67 ? 668 ARG A NE 1 ATOM 5116 C CZ . ARG A 1 654 ? 100.958 84.032 31.921 1.00 83.60 ? 668 ARG A CZ 1 ATOM 5117 N NH1 . ARG A 1 654 ? 100.193 84.906 32.563 1.00 82.41 ? 668 ARG A NH1 1 ATOM 5118 N NH2 . ARG A 1 654 ? 101.302 84.255 30.658 1.00 85.16 ? 668 ARG A NH2 1 ATOM 5119 O OXT . ARG A 1 654 ? 103.240 78.744 34.808 1.00 90.87 ? 668 ARG A OXT 1 HETATM 5120 C C1 . 147 B 2 . ? 77.180 89.443 17.986 1.00 48.18 ? 1001 147 A C1 1 HETATM 5121 C C2 . 147 B 2 . ? 76.760 89.676 19.414 1.00 40.17 ? 1001 147 A C2 1 HETATM 5122 O O2 . 147 B 2 . ? 75.715 90.656 19.329 1.00 34.27 ? 1001 147 A O2 1 HETATM 5123 C C3 . 147 B 2 . ? 77.842 90.152 20.249 1.00 41.15 ? 1001 147 A C3 1 HETATM 5124 O O3 . 147 B 2 . ? 77.498 90.037 21.663 1.00 40.41 ? 1001 147 A O3 1 HETATM 5125 C C4 . 147 B 2 . ? 79.086 89.405 20.083 1.00 40.10 ? 1001 147 A C4 1 HETATM 5126 O O4 . 147 B 2 . ? 78.811 88.155 20.610 1.00 38.45 ? 1001 147 A O4 1 HETATM 5127 C C5 . 147 B 2 . ? 79.460 89.273 18.614 1.00 46.19 ? 1001 147 A C5 1 HETATM 5128 C C6 . 147 B 2 . ? 80.718 88.485 18.382 1.00 47.66 ? 1001 147 A C6 1 HETATM 5129 O O6 . 147 B 2 . ? 81.269 88.600 17.098 1.00 50.23 ? 1001 147 A O6 1 HETATM 5130 O O5 . 147 B 2 . ? 78.407 88.655 17.879 1.00 46.77 ? 1001 147 A O5 1 HETATM 5131 O "O1'" . 147 B 2 . ? 76.112 88.980 17.243 1.00 58.34 ? 1001 147 A "O1'" 1 HETATM 5132 C "C1'" . 147 B 2 . ? 76.342 87.778 16.533 1.00 63.87 ? 1001 147 A "C1'" 1 HETATM 5133 C "C2'" . 147 B 2 . ? 76.384 86.542 17.200 1.00 66.51 ? 1001 147 A "C2'" 1 HETATM 5134 C "C3'" . 147 B 2 . ? 76.592 85.335 16.471 1.00 67.56 ? 1001 147 A "C3'" 1 HETATM 5135 C "C4'" . 147 B 2 . ? 76.740 85.385 15.078 1.00 69.96 ? 1001 147 A "C4'" 1 HETATM 5136 C "C5'" . 147 B 2 . ? 76.686 86.615 14.415 1.00 68.32 ? 1001 147 A "C5'" 1 HETATM 5137 C "C6'" . 147 B 2 . ? 76.478 87.826 15.138 1.00 65.51 ? 1001 147 A "C6'" 1 HETATM 5138 N "N1'" . 147 B 2 . ? 76.950 84.171 14.322 1.00 73.68 1 1001 147 A "N1'" 1 HETATM 5139 O "O2'" . 147 B 2 . ? 77.019 83.021 14.939 1.00 72.14 -1 1001 147 A "O2'" 1 HETATM 5140 O "O3'" . 147 B 2 . ? 77.055 84.245 13.088 1.00 72.73 ? 1001 147 A "O3'" 1 HETATM 5141 C C1 . NAG C 3 . ? 73.092 104.723 -1.751 1.00 70.83 ? 1284 NAG A C1 1 HETATM 5142 C C2 . NAG C 3 . ? 72.227 105.767 -2.446 1.00 78.23 ? 1284 NAG A C2 1 HETATM 5143 C C3 . NAG C 3 . ? 72.512 105.980 -3.937 1.00 82.52 ? 1284 NAG A C3 1 HETATM 5144 C C4 . NAG C 3 . ? 73.792 105.350 -4.509 1.00 87.87 ? 1284 NAG A C4 1 HETATM 5145 C C5 . NAG C 3 . ? 74.446 104.340 -3.571 1.00 83.99 ? 1284 NAG A C5 1 HETATM 5146 C C6 . NAG C 3 . ? 75.898 104.060 -3.948 1.00 85.00 ? 1284 NAG A C6 1 HETATM 5147 C C7 . NAG C 3 . ? 69.954 106.215 -1.691 1.00 84.08 ? 1284 NAG A C7 1 HETATM 5148 C C8 . NAG C 3 . ? 70.492 107.463 -1.041 1.00 83.76 ? 1284 NAG A C8 1 HETATM 5149 N N2 . NAG C 3 . ? 70.831 105.408 -2.290 1.00 80.88 ? 1284 NAG A N2 1 HETATM 5150 O O3 . NAG C 3 . ? 72.523 107.375 -4.160 1.00 80.98 ? 1284 NAG A O3 1 HETATM 5151 O O4 . NAG C 3 . ? 73.439 104.623 -5.669 1.00 98.73 ? 1284 NAG A O4 1 HETATM 5152 O O5 . NAG C 3 . ? 74.399 104.815 -2.251 1.00 76.93 ? 1284 NAG A O5 1 HETATM 5153 O O6 . NAG C 3 . ? 76.401 103.020 -3.136 1.00 85.25 ? 1284 NAG A O6 1 HETATM 5154 O O7 . NAG C 3 . ? 68.746 105.965 -1.658 1.00 84.96 ? 1284 NAG A O7 1 HETATM 5155 C C1 . NAG D 3 . ? 73.961 105.126 -6.929 1.00 107.24 ? 1285 NAG A C1 1 HETATM 5156 C C2 . NAG D 3 . ? 73.635 106.605 -7.206 1.00 111.22 ? 1285 NAG A C2 1 HETATM 5157 C C3 . NAG D 3 . ? 74.534 107.296 -8.244 1.00 112.96 ? 1285 NAG A C3 1 HETATM 5158 C C4 . NAG D 3 . ? 75.927 106.686 -8.406 1.00 113.85 ? 1285 NAG A C4 1 HETATM 5159 C C5 . NAG D 3 . ? 75.852 105.167 -8.322 1.00 112.80 ? 1285 NAG A C5 1 HETATM 5160 C C6 . NAG D 3 . ? 77.208 104.491 -8.516 1.00 113.25 ? 1285 NAG A C6 1 HETATM 5161 C C7 . NAG D 3 . ? 71.350 107.526 -7.140 1.00 111.06 ? 1285 NAG A C7 1 HETATM 5162 C C8 . NAG D 3 . ? 70.099 106.904 -6.590 1.00 110.88 ? 1285 NAG A C8 1 HETATM 5163 N N2 . NAG D 3 . ? 72.253 106.693 -7.663 1.00 111.92 ? 1285 NAG A N2 1 HETATM 5164 O O3 . NAG D 3 . ? 74.672 108.659 -7.899 1.00 112.81 ? 1285 NAG A O3 1 HETATM 5165 O O4 . NAG D 3 . ? 76.467 107.071 -9.655 1.00 114.74 ? 1285 NAG A O4 1 HETATM 5166 O O5 . NAG D 3 . ? 75.341 104.840 -7.052 1.00 110.52 ? 1285 NAG A O5 1 HETATM 5167 O O6 . NAG D 3 . ? 78.025 104.704 -7.386 1.00 113.70 ? 1285 NAG A O6 1 HETATM 5168 O O7 . NAG D 3 . ? 71.502 108.747 -7.108 1.00 110.14 ? 1285 NAG A O7 1 HETATM 5169 C C1 . NAG E 3 . ? 85.009 125.199 10.753 1.00 71.13 ? 1363 NAG A C1 1 HETATM 5170 C C2 . NAG E 3 . ? 84.253 126.527 10.649 1.00 79.57 ? 1363 NAG A C2 1 HETATM 5171 C C3 . NAG E 3 . ? 84.278 127.299 11.967 1.00 83.59 ? 1363 NAG A C3 1 HETATM 5172 C C4 . NAG E 3 . ? 84.020 126.408 13.182 1.00 86.29 ? 1363 NAG A C4 1 HETATM 5173 C C5 . NAG E 3 . ? 84.753 125.067 13.103 1.00 81.00 ? 1363 NAG A C5 1 HETATM 5174 C C6 . NAG E 3 . ? 84.264 124.139 14.210 1.00 80.40 ? 1363 NAG A C6 1 HETATM 5175 C C7 . NAG E 3 . ? 86.136 127.541 9.463 1.00 80.53 ? 1363 NAG A C7 1 HETATM 5176 C C8 . NAG E 3 . ? 86.746 127.089 8.167 1.00 79.25 ? 1363 NAG A C8 1 HETATM 5177 N N2 . NAG E 3 . ? 84.820 127.362 9.599 1.00 80.36 ? 1363 NAG A N2 1 HETATM 5178 O O3 . NAG E 3 . ? 83.313 128.330 11.903 1.00 84.77 ? 1363 NAG A O3 1 HETATM 5179 O O4 . NAG E 3 . ? 84.442 127.073 14.358 1.00 93.24 ? 1363 NAG A O4 1 HETATM 5180 O O5 . NAG E 3 . ? 84.568 124.431 11.853 1.00 75.89 ? 1363 NAG A O5 1 HETATM 5181 O O6 . NAG E 3 . ? 82.889 124.367 14.434 1.00 79.46 ? 1363 NAG A O6 1 HETATM 5182 O O7 . NAG E 3 . ? 86.842 128.057 10.334 1.00 81.35 ? 1363 NAG A O7 1 HETATM 5183 C C1 . NAG F 3 . ? 83.326 127.658 15.064 1.00 98.06 ? 1364 NAG A C1 1 HETATM 5184 C C2 . NAG F 3 . ? 83.855 128.367 16.313 1.00 99.30 ? 1364 NAG A C2 1 HETATM 5185 C C3 . NAG F 3 . ? 82.707 128.995 17.103 1.00 100.91 ? 1364 NAG A C3 1 HETATM 5186 C C4 . NAG F 3 . ? 81.961 129.943 16.170 1.00 101.37 ? 1364 NAG A C4 1 HETATM 5187 C C5 . NAG F 3 . ? 81.471 129.171 14.942 1.00 101.47 ? 1364 NAG A C5 1 HETATM 5188 C C6 . NAG F 3 . ? 80.741 130.076 13.952 1.00 102.29 ? 1364 NAG A C6 1 HETATM 5189 C C7 . NAG F 3 . ? 85.991 127.545 17.044 1.00 96.16 ? 1364 NAG A C7 1 HETATM 5190 C C8 . NAG F 3 . ? 86.783 126.294 17.287 1.00 95.02 ? 1364 NAG A C8 1 HETATM 5191 N N2 . NAG F 3 . ? 84.666 127.455 17.104 1.00 97.66 ? 1364 NAG A N2 1 HETATM 5192 O O3 . NAG F 3 . ? 83.182 129.679 18.243 1.00 101.63 ? 1364 NAG A O3 1 HETATM 5193 O O4 . NAG F 3 . ? 80.881 130.564 16.837 1.00 101.57 ? 1364 NAG A O4 1 HETATM 5194 O O5 . NAG F 3 . ? 82.548 128.538 14.271 1.00 99.99 ? 1364 NAG A O5 1 HETATM 5195 O O6 . NAG F 3 . ? 81.027 129.655 12.634 1.00 102.55 ? 1364 NAG A O6 1 HETATM 5196 O O7 . NAG F 3 . ? 86.560 128.604 16.790 1.00 96.18 ? 1364 NAG A O7 1 HETATM 5197 C C1 . NAG G 3 . ? 97.132 93.221 -8.889 1.00 74.11 ? 1387 NAG A C1 1 HETATM 5198 C C2 . NAG G 3 . ? 98.011 92.028 -9.299 1.00 80.78 ? 1387 NAG A C2 1 HETATM 5199 C C3 . NAG G 3 . ? 99.361 92.452 -9.888 1.00 81.71 ? 1387 NAG A C3 1 HETATM 5200 C C4 . NAG G 3 . ? 99.235 93.609 -10.880 1.00 82.47 ? 1387 NAG A C4 1 HETATM 5201 C C5 . NAG G 3 . ? 98.349 94.707 -10.304 1.00 84.41 ? 1387 NAG A C5 1 HETATM 5202 C C6 . NAG G 3 . ? 98.168 95.862 -11.292 1.00 86.25 ? 1387 NAG A C6 1 HETATM 5203 C C7 . NAG G 3 . ? 97.530 89.997 -8.015 1.00 88.33 ? 1387 NAG A C7 1 HETATM 5204 C C8 . NAG G 3 . ? 98.267 88.839 -7.404 1.00 87.72 ? 1387 NAG A C8 1 HETATM 5205 N N2 . NAG G 3 . ? 98.220 91.132 -8.168 1.00 85.37 ? 1387 NAG A N2 1 HETATM 5206 O O3 . NAG G 3 . ? 99.950 91.336 -10.522 1.00 80.20 ? 1387 NAG A O3 1 HETATM 5207 O O4 . NAG G 3 . ? 100.504 94.160 -11.169 1.00 81.60 ? 1387 NAG A O4 1 HETATM 5208 O O5 . NAG G 3 . ? 97.087 94.169 -9.944 1.00 81.32 ? 1387 NAG A O5 1 HETATM 5209 O O6 . NAG G 3 . ? 97.111 95.594 -12.191 1.00 87.03 ? 1387 NAG A O6 1 HETATM 5210 O O7 . NAG G 3 . ? 96.346 89.878 -8.342 1.00 89.71 ? 1387 NAG A O7 1 HETATM 5211 C C1 . NAG H 3 . ? 102.491 71.393 38.289 1.00 59.65 ? 1542 NAG A C1 1 HETATM 5212 C C2 . NAG H 3 . ? 103.782 72.036 37.786 1.00 65.33 ? 1542 NAG A C2 1 HETATM 5213 C C3 . NAG H 3 . ? 104.623 71.006 37.054 1.00 71.48 ? 1542 NAG A C3 1 HETATM 5214 C C4 . NAG H 3 . ? 104.766 69.703 37.831 1.00 73.84 ? 1542 NAG A C4 1 HETATM 5215 C C5 . NAG H 3 . ? 103.423 69.198 38.366 1.00 68.66 ? 1542 NAG A C5 1 HETATM 5216 C C6 . NAG H 3 . ? 103.574 68.044 39.357 1.00 68.39 ? 1542 NAG A C6 1 HETATM 5217 C C7 . NAG H 3 . ? 103.768 74.422 37.232 1.00 66.22 ? 1542 NAG A C7 1 HETATM 5218 C C8 . NAG H 3 . ? 104.146 75.391 36.149 1.00 63.03 ? 1542 NAG A C8 1 HETATM 5219 N N2 . NAG H 3 . ? 103.517 73.156 36.888 1.00 65.77 ? 1542 NAG A N2 1 HETATM 5220 O O3 . NAG H 3 . ? 105.901 71.547 36.817 1.00 74.76 ? 1542 NAG A O3 1 HETATM 5221 O O4 . NAG H 3 . ? 105.330 68.775 36.929 1.00 79.82 ? 1542 NAG A O4 1 HETATM 5222 O O5 . NAG H 3 . ? 102.745 70.228 39.044 1.00 64.65 ? 1542 NAG A O5 1 HETATM 5223 O O6 . NAG H 3 . ? 104.285 68.493 40.493 1.00 69.23 ? 1542 NAG A O6 1 HETATM 5224 O O7 . NAG H 3 . ? 103.698 74.817 38.393 1.00 70.06 ? 1542 NAG A O7 1 HETATM 5225 C C1 . NAG I 3 . ? 106.495 68.135 37.484 1.00 85.31 ? 1543 NAG A C1 1 HETATM 5226 C C2 . NAG I 3 . ? 106.567 66.773 36.806 1.00 88.01 ? 1543 NAG A C2 1 HETATM 5227 C C3 . NAG I 3 . ? 107.820 66.004 37.202 1.00 91.23 ? 1543 NAG A C3 1 HETATM 5228 C C4 . NAG I 3 . ? 109.043 66.891 36.979 1.00 91.07 ? 1543 NAG A C4 1 HETATM 5229 C C5 . NAG I 3 . ? 108.878 68.201 37.751 1.00 89.68 ? 1543 NAG A C5 1 HETATM 5230 C C6 . NAG I 3 . ? 110.101 69.098 37.554 1.00 89.66 ? 1543 NAG A C6 1 HETATM 5231 C C7 . NAG I 3 . ? 104.610 65.556 36.068 1.00 86.87 ? 1543 NAG A C7 1 HETATM 5232 C C8 . NAG I 3 . ? 103.582 64.524 36.428 1.00 86.62 ? 1543 NAG A C8 1 HETATM 5233 N N2 . NAG I 3 . ? 105.357 66.018 37.072 1.00 87.68 ? 1543 NAG A N2 1 HETATM 5234 O O3 . NAG I 3 . ? 107.901 64.834 36.416 1.00 92.77 ? 1543 NAG A O3 1 HETATM 5235 O O4 . NAG I 3 . ? 110.238 66.230 37.348 1.00 91.12 ? 1543 NAG A O4 1 HETATM 5236 O O5 . NAG I 3 . ? 107.697 68.875 37.339 1.00 87.83 ? 1543 NAG A O5 1 HETATM 5237 O O6 . NAG I 3 . ? 109.794 70.439 37.874 1.00 89.04 ? 1543 NAG A O6 1 HETATM 5238 O O7 . NAG I 3 . ? 104.737 65.930 34.899 1.00 85.21 ? 1543 NAG A O7 1 HETATM 5239 CA CA . CA J 4 . ? 83.715 88.881 54.705 1.00 72.25 ? 1669 CA A CA 1 HETATM 5240 O O . HOH K 5 . ? 77.816 116.597 -2.522 1.00 59.98 ? 2001 HOH A O 1 HETATM 5241 O O . HOH K 5 . ? 75.290 114.125 -8.595 1.00 63.60 ? 2002 HOH A O 1 HETATM 5242 O O . HOH K 5 . ? 66.954 104.260 3.535 1.00 40.06 ? 2003 HOH A O 1 HETATM 5243 O O . HOH K 5 . ? 71.897 106.500 6.461 1.00 39.07 ? 2004 HOH A O 1 HETATM 5244 O O . HOH K 5 . ? 71.368 109.738 7.815 1.00 54.14 ? 2005 HOH A O 1 HETATM 5245 O O . HOH K 5 . ? 80.438 95.830 29.163 1.00 36.78 ? 2006 HOH A O 1 HETATM 5246 O O . HOH K 5 . ? 84.275 89.195 31.442 1.00 32.66 ? 2007 HOH A O 1 HETATM 5247 O O . HOH K 5 . ? 83.962 97.325 26.476 1.00 43.11 ? 2008 HOH A O 1 HETATM 5248 O O . HOH K 5 . ? 86.671 94.325 37.790 1.00 39.71 ? 2009 HOH A O 1 HETATM 5249 O O . HOH K 5 . ? 80.831 89.572 36.553 1.00 39.80 ? 2010 HOH A O 1 HETATM 5250 O O . HOH K 5 . ? 83.863 95.198 40.346 1.00 37.08 ? 2011 HOH A O 1 HETATM 5251 O O . HOH K 5 . ? 101.959 101.745 39.006 1.00 50.12 ? 2012 HOH A O 1 HETATM 5252 O O . HOH K 5 . ? 73.816 96.059 44.965 1.00 57.42 ? 2013 HOH A O 1 HETATM 5253 O O . HOH K 5 . ? 80.304 110.208 37.567 1.00 53.38 ? 2014 HOH A O 1 HETATM 5254 O O . HOH K 5 . ? 79.247 111.933 36.590 1.00 51.59 ? 2015 HOH A O 1 HETATM 5255 O O . HOH K 5 . ? 89.212 110.342 22.689 1.00 44.80 ? 2016 HOH A O 1 HETATM 5256 O O . HOH K 5 . ? 100.029 104.774 25.514 1.00 50.29 ? 2017 HOH A O 1 HETATM 5257 O O . HOH K 5 . ? 96.933 109.877 25.975 1.00 118.39 ? 2018 HOH A O 1 HETATM 5258 O O . HOH K 5 . ? 84.056 111.532 22.730 1.00 69.83 ? 2019 HOH A O 1 HETATM 5259 O O . HOH K 5 . ? 87.532 115.042 18.832 1.00 53.42 ? 2020 HOH A O 1 HETATM 5260 O O . HOH K 5 . ? 93.314 116.787 23.516 1.00 56.15 ? 2021 HOH A O 1 HETATM 5261 O O . HOH K 5 . ? 90.091 117.464 16.037 1.00 88.70 ? 2022 HOH A O 1 HETATM 5262 O O . HOH K 5 . ? 65.017 82.160 22.031 1.00 49.92 ? 2023 HOH A O 1 HETATM 5263 O O . HOH K 5 . ? 78.042 112.779 19.690 1.00 47.41 ? 2024 HOH A O 1 HETATM 5264 O O . HOH K 5 . ? 71.221 99.212 18.625 1.00 34.73 ? 2025 HOH A O 1 HETATM 5265 O O . HOH K 5 . ? 74.359 94.984 19.129 1.00 34.02 ? 2026 HOH A O 1 HETATM 5266 O O . HOH K 5 . ? 71.925 98.140 31.882 1.00 63.01 ? 2027 HOH A O 1 HETATM 5267 O O . HOH K 5 . ? 73.530 96.833 31.746 1.00 30.34 ? 2028 HOH A O 1 HETATM 5268 O O . HOH K 5 . ? 71.127 91.777 28.342 1.00 29.09 ? 2029 HOH A O 1 HETATM 5269 O O . HOH K 5 . ? 72.833 90.123 30.584 1.00 28.69 ? 2030 HOH A O 1 HETATM 5270 O O . HOH K 5 . ? 67.652 93.299 29.897 1.00 25.83 ? 2031 HOH A O 1 HETATM 5271 O O . HOH K 5 . ? 69.445 96.454 33.309 1.00 29.35 ? 2032 HOH A O 1 HETATM 5272 O O . HOH K 5 . ? 72.774 83.486 34.069 1.00 34.60 ? 2033 HOH A O 1 HETATM 5273 O O . HOH K 5 . ? 66.892 87.656 37.315 1.00 31.28 ? 2034 HOH A O 1 HETATM 5274 O O . HOH K 5 . ? 71.764 84.570 28.190 1.00 31.75 ? 2035 HOH A O 1 HETATM 5275 O O . HOH K 5 . ? 64.357 89.192 12.879 1.00 47.97 ? 2036 HOH A O 1 HETATM 5276 O O . HOH K 5 . ? 51.527 102.400 16.566 1.00 45.30 ? 2037 HOH A O 1 HETATM 5277 O O . HOH K 5 . ? 52.469 105.400 18.898 1.00 53.98 ? 2038 HOH A O 1 HETATM 5278 O O . HOH K 5 . ? 77.171 89.785 36.640 1.00 34.56 ? 2039 HOH A O 1 HETATM 5279 O O . HOH K 5 . ? 79.074 91.814 35.095 1.00 55.47 ? 2040 HOH A O 1 HETATM 5280 O O . HOH K 5 . ? 74.529 95.812 33.796 1.00 28.62 ? 2041 HOH A O 1 HETATM 5281 O O . HOH K 5 . ? 77.112 96.114 33.891 1.00 38.86 ? 2042 HOH A O 1 HETATM 5282 O O . HOH K 5 . ? 71.354 97.294 35.214 1.00 31.46 ? 2043 HOH A O 1 HETATM 5283 O O . HOH K 5 . ? 66.769 83.165 17.258 1.00 50.81 ? 2044 HOH A O 1 HETATM 5284 O O . HOH K 5 . ? 67.519 90.288 2.485 1.00 49.11 ? 2045 HOH A O 1 HETATM 5285 O O . HOH K 5 . ? 67.678 87.735 5.368 1.00 46.39 ? 2046 HOH A O 1 HETATM 5286 O O . HOH K 5 . ? 71.341 90.185 4.768 1.00 46.00 ? 2047 HOH A O 1 HETATM 5287 O O . HOH K 5 . ? 73.502 91.020 6.019 1.00 44.69 ? 2048 HOH A O 1 HETATM 5288 O O . HOH K 5 . ? 65.645 87.946 2.878 1.00 48.71 ? 2049 HOH A O 1 HETATM 5289 O O . HOH K 5 . ? 63.734 86.400 37.273 1.00 40.48 ? 2050 HOH A O 1 HETATM 5290 O O . HOH K 5 . ? 66.304 85.796 39.574 1.00 32.34 ? 2051 HOH A O 1 HETATM 5291 O O . HOH K 5 . ? 60.217 87.164 40.770 1.00 28.37 ? 2052 HOH A O 1 HETATM 5292 O O . HOH K 5 . ? 58.119 95.159 39.326 1.00 45.33 ? 2053 HOH A O 1 HETATM 5293 O O . HOH K 5 . ? 64.153 93.756 45.775 1.00 47.58 ? 2054 HOH A O 1 HETATM 5294 O O . HOH K 5 . ? 67.604 100.008 44.910 1.00 45.94 ? 2055 HOH A O 1 HETATM 5295 O O . HOH K 5 . ? 71.118 98.746 37.785 1.00 31.27 ? 2056 HOH A O 1 HETATM 5296 O O . HOH K 5 . ? 71.679 94.728 44.107 1.00 48.78 ? 2057 HOH A O 1 HETATM 5297 O O . HOH K 5 . ? 71.565 100.900 45.740 1.00 41.45 ? 2058 HOH A O 1 HETATM 5298 O O . HOH K 5 . ? 77.330 86.889 8.900 1.00 48.12 ? 2059 HOH A O 1 HETATM 5299 O O . HOH K 5 . ? 82.182 94.653 6.825 1.00 45.45 ? 2060 HOH A O 1 HETATM 5300 O O . HOH K 5 . ? 67.798 102.200 42.809 1.00 38.43 ? 2061 HOH A O 1 HETATM 5301 O O . HOH K 5 . ? 62.740 103.966 36.604 1.00 36.52 ? 2062 HOH A O 1 HETATM 5302 O O . HOH K 5 . ? 77.978 98.580 40.497 1.00 47.88 ? 2063 HOH A O 1 HETATM 5303 O O . HOH K 5 . ? 71.751 90.714 2.225 1.00 49.55 ? 2064 HOH A O 1 HETATM 5304 O O . HOH K 5 . ? 75.223 98.831 34.747 1.00 35.91 ? 2065 HOH A O 1 HETATM 5305 O O . HOH K 5 . ? 77.488 101.162 37.159 1.00 47.81 ? 2066 HOH A O 1 HETATM 5306 O O . HOH K 5 . ? 72.561 99.208 33.684 1.00 44.71 ? 2067 HOH A O 1 HETATM 5307 O O . HOH K 5 . ? 81.003 107.964 36.699 1.00 58.10 ? 2068 HOH A O 1 HETATM 5308 O O . HOH K 5 . ? 78.346 112.606 33.562 1.00 51.78 ? 2069 HOH A O 1 HETATM 5309 O O . HOH K 5 . ? 77.233 105.101 39.736 1.00 46.91 ? 2070 HOH A O 1 HETATM 5310 O O . HOH K 5 . ? 79.600 105.792 39.319 1.00 58.42 ? 2071 HOH A O 1 HETATM 5311 O O . HOH K 5 . ? 87.080 110.178 35.591 1.00 53.93 ? 2072 HOH A O 1 HETATM 5312 O O . HOH K 5 . ? 72.685 112.886 28.982 1.00 40.78 ? 2073 HOH A O 1 HETATM 5313 O O . HOH K 5 . ? 82.203 116.811 20.819 1.00 58.48 ? 2074 HOH A O 1 HETATM 5314 O O . HOH K 5 . ? 80.489 113.897 19.580 1.00 64.41 ? 2075 HOH A O 1 HETATM 5315 O O . HOH K 5 . ? 75.136 112.438 26.713 1.00 61.90 ? 2076 HOH A O 1 HETATM 5316 O O . HOH K 5 . ? 75.998 114.648 18.862 1.00 60.38 ? 2077 HOH A O 1 HETATM 5317 O O . HOH K 5 . ? 73.228 113.324 23.007 1.00 52.81 ? 2078 HOH A O 1 HETATM 5318 O O . HOH K 5 . ? 69.977 100.777 21.033 1.00 48.03 ? 2079 HOH A O 1 HETATM 5319 O O . HOH K 5 . ? 66.041 85.407 36.145 1.00 33.47 ? 2080 HOH A O 1 HETATM 5320 O O . HOH K 5 . ? 60.646 82.642 32.201 1.00 44.23 ? 2081 HOH A O 1 HETATM 5321 O O . HOH K 5 . ? 57.050 85.955 36.655 1.00 45.51 ? 2082 HOH A O 1 HETATM 5322 O O . HOH K 5 . ? 56.871 89.110 28.441 1.00 41.98 ? 2083 HOH A O 1 HETATM 5323 O O . HOH K 5 . ? 55.916 76.551 31.146 1.00 61.87 ? 2084 HOH A O 1 HETATM 5324 O O . HOH K 5 . ? 79.930 119.402 16.227 1.00 52.40 ? 2085 HOH A O 1 HETATM 5325 O O . HOH K 5 . ? 65.619 82.282 25.313 1.00 43.22 ? 2086 HOH A O 1 HETATM 5326 O O . HOH K 5 . ? 66.587 79.353 28.493 1.00 47.36 ? 2087 HOH A O 1 HETATM 5327 O O . HOH K 5 . ? 56.898 80.999 22.425 1.00 49.27 ? 2088 HOH A O 1 HETATM 5328 O O . HOH K 5 . ? 50.601 85.680 25.372 1.00 56.49 ? 2089 HOH A O 1 HETATM 5329 O O . HOH K 5 . ? 50.809 93.909 26.965 1.00 46.87 ? 2090 HOH A O 1 HETATM 5330 O O . HOH K 5 . ? 50.569 91.311 25.807 1.00 53.49 ? 2091 HOH A O 1 HETATM 5331 O O . HOH K 5 . ? 51.228 101.669 30.672 1.00 46.46 ? 2092 HOH A O 1 HETATM 5332 O O . HOH K 5 . ? 57.060 106.078 36.030 1.00 65.28 ? 2093 HOH A O 1 HETATM 5333 O O . HOH K 5 . ? 60.165 106.732 37.501 1.00 55.77 ? 2094 HOH A O 1 HETATM 5334 O O . HOH K 5 . ? 67.388 108.476 30.060 1.00 30.91 ? 2095 HOH A O 1 HETATM 5335 O O . HOH K 5 . ? 66.003 113.094 39.781 1.00 47.84 ? 2096 HOH A O 1 HETATM 5336 O O . HOH K 5 . ? 62.669 106.279 37.817 1.00 49.77 ? 2097 HOH A O 1 HETATM 5337 O O . HOH K 5 . ? 65.987 103.989 44.373 1.00 51.23 ? 2098 HOH A O 1 HETATM 5338 O O . HOH K 5 . ? 72.144 111.952 25.244 1.00 46.12 ? 2099 HOH A O 1 HETATM 5339 O O . HOH K 5 . ? 66.910 111.155 20.223 1.00 55.73 ? 2100 HOH A O 1 HETATM 5340 O O . HOH K 5 . ? 63.442 96.438 23.902 1.00 29.46 ? 2101 HOH A O 1 HETATM 5341 O O . HOH K 5 . ? 67.046 96.827 17.804 1.00 32.76 ? 2102 HOH A O 1 HETATM 5342 O O . HOH K 5 . ? 65.176 92.508 17.783 1.00 29.53 ? 2103 HOH A O 1 HETATM 5343 O O . HOH K 5 . ? 71.926 88.809 12.508 1.00 69.36 ? 2104 HOH A O 1 HETATM 5344 O O . HOH K 5 . ? 74.159 88.452 12.543 1.00 78.09 ? 2105 HOH A O 1 HETATM 5345 O O . HOH K 5 . ? 65.138 90.866 14.531 1.00 36.45 ? 2106 HOH A O 1 HETATM 5346 O O . HOH K 5 . ? 67.906 83.491 22.869 1.00 33.08 ? 2107 HOH A O 1 HETATM 5347 O O . HOH K 5 . ? 73.035 85.410 17.802 1.00 60.56 ? 2108 HOH A O 1 HETATM 5348 O O . HOH K 5 . ? 61.937 88.959 13.522 1.00 49.84 ? 2109 HOH A O 1 HETATM 5349 O O . HOH K 5 . ? 56.319 87.263 18.738 1.00 52.68 ? 2110 HOH A O 1 HETATM 5350 O O . HOH K 5 . ? 55.859 90.821 14.335 1.00 44.97 ? 2111 HOH A O 1 HETATM 5351 O O . HOH K 5 . ? 50.780 97.470 20.400 1.00 62.75 ? 2112 HOH A O 1 HETATM 5352 O O . HOH K 5 . ? 51.402 95.213 14.505 1.00 45.85 ? 2113 HOH A O 1 HETATM 5353 O O . HOH K 5 . ? 49.855 97.116 18.172 1.00 58.04 ? 2114 HOH A O 1 HETATM 5354 O O . HOH K 5 . ? 52.841 102.971 19.057 1.00 48.90 ? 2115 HOH A O 1 HETATM 5355 O O . HOH K 5 . ? 60.431 106.248 17.215 1.00 40.51 ? 2116 HOH A O 1 HETATM 5356 O O . HOH K 5 . ? 51.118 107.126 24.555 1.00 51.08 ? 2117 HOH A O 1 HETATM 5357 O O . HOH K 5 . ? 51.332 109.515 25.658 1.00 52.29 ? 2118 HOH A O 1 HETATM 5358 O O . HOH K 5 . ? 57.238 110.415 19.859 1.00 59.66 ? 2119 HOH A O 1 HETATM 5359 O O . HOH K 5 . ? 52.197 107.595 21.112 1.00 51.81 ? 2120 HOH A O 1 HETATM 5360 O O . HOH K 5 . ? 59.934 111.372 31.734 1.00 48.89 ? 2121 HOH A O 1 HETATM 5361 O O . HOH K 5 . ? 53.038 102.612 32.816 1.00 47.07 ? 2122 HOH A O 1 HETATM 5362 O O . HOH K 5 . ? 60.576 113.327 25.782 1.00 43.79 ? 2123 HOH A O 1 HETATM 5363 O O . HOH K 5 . ? 61.613 110.593 18.943 1.00 63.30 ? 2124 HOH A O 1 HETATM 5364 O O . HOH K 5 . ? 63.728 87.427 46.843 1.00 52.81 ? 2125 HOH A O 1 HETATM 5365 O O . HOH K 5 . ? 65.736 76.485 34.916 1.00 61.55 ? 2126 HOH A O 1 HETATM 5366 O O . HOH K 5 . ? 68.064 94.715 11.907 1.00 37.41 ? 2127 HOH A O 1 HETATM 5367 O O . HOH K 5 . ? 65.448 92.261 10.766 1.00 36.57 ? 2128 HOH A O 1 HETATM 5368 O O . HOH K 5 . ? 65.035 86.657 13.218 1.00 65.51 ? 2129 HOH A O 1 HETATM 5369 O O . HOH K 5 . ? 66.996 85.478 15.005 1.00 62.20 ? 2130 HOH A O 1 HETATM 5370 O O . HOH K 5 . ? 66.811 89.537 11.165 1.00 40.84 ? 2131 HOH A O 1 HETATM 5371 O O . HOH K 5 . ? 68.550 90.138 5.232 1.00 42.41 ? 2132 HOH A O 1 HETATM 5372 O O . HOH K 5 . ? 72.607 92.797 8.194 1.00 40.28 ? 2133 HOH A O 1 HETATM 5373 O O . HOH K 5 . ? 74.395 93.223 4.143 1.00 37.53 ? 2134 HOH A O 1 HETATM 5374 O O . HOH K 5 . ? 65.472 92.206 1.097 1.00 45.44 ? 2135 HOH A O 1 HETATM 5375 O O . HOH K 5 . ? 64.263 80.838 45.744 1.00 53.61 ? 2136 HOH A O 1 HETATM 5376 O O . HOH K 5 . ? 54.983 100.475 5.636 1.00 65.80 ? 2137 HOH A O 1 HETATM 5377 O O . HOH K 5 . ? 49.858 99.484 6.468 1.00 52.54 ? 2138 HOH A O 1 HETATM 5378 O O . HOH K 5 . ? 54.120 94.419 10.969 1.00 50.46 ? 2139 HOH A O 1 HETATM 5379 O O . HOH K 5 . ? 47.438 105.950 5.055 1.00 53.22 ? 2140 HOH A O 1 HETATM 5380 O O . HOH K 5 . ? 52.122 104.065 14.568 1.00 44.58 ? 2141 HOH A O 1 HETATM 5381 O O . HOH K 5 . ? 59.591 108.959 14.827 1.00 81.11 ? 2142 HOH A O 1 HETATM 5382 O O . HOH K 5 . ? 65.037 108.068 9.720 1.00 55.45 ? 2143 HOH A O 1 HETATM 5383 O O . HOH K 5 . ? 74.572 89.949 10.838 1.00 49.15 ? 2144 HOH A O 1 HETATM 5384 O O . HOH K 5 . ? 75.902 89.344 9.005 1.00 65.26 ? 2145 HOH A O 1 HETATM 5385 O O . HOH K 5 . ? 77.798 75.653 62.238 1.00 72.29 ? 2146 HOH A O 1 HETATM 5386 O O . HOH K 5 . ? 80.564 93.283 8.486 1.00 42.24 ? 2147 HOH A O 1 HETATM 5387 O O . HOH K 5 . ? 80.450 96.221 7.267 1.00 37.71 ? 2148 HOH A O 1 HETATM 5388 O O . HOH K 5 . ? 74.237 98.328 -0.818 1.00 41.02 ? 2149 HOH A O 1 HETATM 5389 O O . HOH K 5 . ? 73.128 93.040 1.545 1.00 45.11 ? 2150 HOH A O 1 HETATM 5390 O O . HOH K 5 . ? 65.377 94.339 -0.690 1.00 44.08 ? 2151 HOH A O 1 HETATM 5391 O O . HOH K 5 . ? 68.484 94.061 -2.446 1.00 45.53 ? 2152 HOH A O 1 HETATM 5392 O O . HOH K 5 . ? 63.392 93.439 -2.338 1.00 49.61 ? 2153 HOH A O 1 HETATM 5393 O O . HOH K 5 . ? 61.088 91.942 -0.219 1.00 59.19 ? 2154 HOH A O 1 HETATM 5394 O O . HOH K 5 . ? 72.863 100.352 -4.398 1.00 67.45 ? 2155 HOH A O 1 HETATM 5395 O O . HOH K 5 . ? 61.891 107.198 0.000 0.50 57.28 ? 2156 HOH A O 1 HETATM 5396 O O . HOH K 5 . ? 62.329 105.184 -2.432 1.00 62.90 ? 2157 HOH A O 1 HETATM 5397 O O . HOH K 5 . ? 83.986 90.757 11.169 1.00 68.00 ? 2158 HOH A O 1 HETATM 5398 O O . HOH K 5 . ? 87.874 87.966 16.868 1.00 46.34 ? 2159 HOH A O 1 HETATM 5399 O O . HOH K 5 . ? 89.911 88.440 14.610 1.00 51.74 ? 2160 HOH A O 1 HETATM 5400 O O . HOH K 5 . ? 97.157 97.758 17.618 1.00 57.06 ? 2161 HOH A O 1 HETATM 5401 O O . HOH K 5 . ? 96.465 94.577 22.494 1.00 47.01 ? 2162 HOH A O 1 HETATM 5402 O O . HOH K 5 . ? 99.468 95.383 15.333 1.00 54.85 ? 2163 HOH A O 1 HETATM 5403 O O . HOH K 5 . ? 88.869 104.404 7.120 1.00 53.36 ? 2164 HOH A O 1 HETATM 5404 O O . HOH K 5 . ? 84.027 94.088 4.955 1.00 57.50 ? 2165 HOH A O 1 HETATM 5405 O O . HOH K 5 . ? 85.319 96.444 1.486 1.00 50.92 ? 2166 HOH A O 1 HETATM 5406 O O . HOH K 5 . ? 85.566 91.748 5.584 1.00 48.06 ? 2167 HOH A O 1 HETATM 5407 O O . HOH K 5 . ? 80.629 104.220 9.035 1.00 40.73 ? 2168 HOH A O 1 HETATM 5408 O O . HOH K 5 . ? 85.430 107.552 7.441 1.00 45.19 ? 2169 HOH A O 1 HETATM 5409 O O . HOH K 5 . ? 88.253 98.624 -0.730 1.00 56.65 ? 2170 HOH A O 1 HETATM 5410 O O . HOH K 5 . ? 76.327 110.190 -1.601 1.00 67.25 ? 2171 HOH A O 1 HETATM 5411 O O . HOH K 5 . ? 79.355 105.905 8.200 1.00 46.31 ? 2172 HOH A O 1 HETATM 5412 O O . HOH K 5 . ? 90.377 90.102 26.032 1.00 43.20 ? 2173 HOH A O 1 HETATM 5413 O O . HOH K 5 . ? 86.843 88.955 32.241 1.00 29.81 ? 2174 HOH A O 1 HETATM 5414 O O . HOH K 5 . ? 93.846 88.065 29.455 1.00 55.49 ? 2175 HOH A O 1 HETATM 5415 O O . HOH K 5 . ? 89.531 83.904 22.719 1.00 39.25 ? 2176 HOH A O 1 HETATM 5416 O O . HOH K 5 . ? 86.008 80.754 26.637 1.00 46.71 ? 2177 HOH A O 1 HETATM 5417 O O . HOH K 5 . ? 90.584 79.708 25.494 1.00 65.40 ? 2178 HOH A O 1 HETATM 5418 O O . HOH K 5 . ? 93.119 84.541 32.271 1.00 48.22 ? 2179 HOH A O 1 HETATM 5419 O O . HOH K 5 . ? 87.530 82.551 21.044 1.00 60.49 ? 2180 HOH A O 1 HETATM 5420 O O . HOH K 5 . ? 95.853 95.189 29.192 1.00 49.35 ? 2181 HOH A O 1 HETATM 5421 O O . HOH K 5 . ? 97.062 92.331 28.621 1.00 51.96 ? 2182 HOH A O 1 HETATM 5422 O O . HOH K 5 . ? 98.049 89.198 32.809 1.00 57.27 ? 2183 HOH A O 1 HETATM 5423 O O . HOH K 5 . ? 100.204 100.973 25.052 1.00 50.87 ? 2184 HOH A O 1 HETATM 5424 O O . HOH K 5 . ? 99.980 104.989 27.918 1.00 68.88 ? 2185 HOH A O 1 HETATM 5425 O O . HOH K 5 . ? 99.314 103.879 20.812 1.00 50.89 ? 2186 HOH A O 1 HETATM 5426 O O . HOH K 5 . ? 89.084 106.348 9.769 1.00 54.07 ? 2187 HOH A O 1 HETATM 5427 O O . HOH K 5 . ? 77.225 116.565 17.174 1.00 59.07 ? 2188 HOH A O 1 HETATM 5428 O O . HOH K 5 . ? 82.301 119.641 13.875 1.00 67.19 ? 2189 HOH A O 1 HETATM 5429 O O . HOH K 5 . ? 91.059 98.700 0.803 1.00 62.74 ? 2190 HOH A O 1 HETATM 5430 O O . HOH K 5 . ? 96.026 92.392 -0.429 1.00 54.77 ? 2191 HOH A O 1 HETATM 5431 O O . HOH K 5 . ? 94.723 94.012 -1.729 1.00 57.17 ? 2192 HOH A O 1 HETATM 5432 O O . HOH K 5 . ? 72.750 80.716 17.536 1.00 64.29 ? 2193 HOH A O 1 HETATM 5433 O O . HOH K 5 . ? 81.899 87.193 1.657 1.00 47.20 ? 2194 HOH A O 1 HETATM 5434 O O . HOH K 5 . ? 88.618 89.490 4.058 1.00 49.57 ? 2195 HOH A O 1 HETATM 5435 O O . HOH K 5 . ? 99.143 119.321 8.704 1.00 74.14 ? 2196 HOH A O 1 HETATM 5436 O O . HOH K 5 . ? 93.918 124.071 8.236 1.00 54.14 ? 2197 HOH A O 1 HETATM 5437 O O . HOH K 5 . ? 94.106 118.727 12.375 1.00 53.05 ? 2198 HOH A O 1 HETATM 5438 O O . HOH K 5 . ? 100.830 113.227 15.497 1.00 68.25 ? 2199 HOH A O 1 HETATM 5439 O O . HOH K 5 . ? 104.931 115.838 4.640 1.00 70.81 ? 2200 HOH A O 1 HETATM 5440 O O . HOH K 5 . ? 105.781 111.167 -5.223 1.00 93.28 ? 2201 HOH A O 1 HETATM 5441 O O . HOH K 5 . ? 101.270 105.201 32.575 1.00 61.92 ? 2202 HOH A O 1 HETATM 5442 O O . HOH K 5 . ? 104.460 94.380 28.876 1.00 62.43 ? 2203 HOH A O 1 HETATM 5443 O O . HOH K 5 . ? 96.994 86.970 33.929 1.00 41.06 ? 2204 HOH A O 1 HETATM 5444 O O . HOH K 5 . ? 99.386 84.077 37.379 1.00 51.80 ? 2205 HOH A O 1 HETATM 5445 O O . HOH K 5 . ? 88.191 89.807 44.207 1.00 36.87 ? 2206 HOH A O 1 HETATM 5446 O O . HOH K 5 . ? 90.122 86.051 51.969 1.00 45.36 ? 2207 HOH A O 1 HETATM 5447 O O . HOH K 5 . ? 80.277 92.360 51.000 1.00 46.54 ? 2208 HOH A O 1 HETATM 5448 O O . HOH K 5 . ? 82.891 88.381 56.941 1.00 60.81 ? 2209 HOH A O 1 HETATM 5449 O O . HOH K 5 . ? 78.984 94.602 51.311 1.00 48.48 ? 2210 HOH A O 1 HETATM 5450 O O . HOH K 5 . ? 84.360 99.572 45.901 1.00 61.23 ? 2211 HOH A O 1 HETATM 5451 O O . HOH K 5 . ? 75.822 94.664 45.673 1.00 47.75 ? 2212 HOH A O 1 HETATM 5452 O O . HOH K 5 . ? 75.271 93.263 40.467 1.00 34.84 ? 2213 HOH A O 1 HETATM 5453 O O . HOH K 5 . ? 76.960 91.398 39.550 1.00 55.12 ? 2214 HOH A O 1 HETATM 5454 O O . HOH K 5 . ? 79.055 92.583 37.931 1.00 46.12 ? 2215 HOH A O 1 HETATM 5455 O O . HOH K 5 . ? 85.160 97.118 46.106 1.00 52.05 ? 2216 HOH A O 1 HETATM 5456 O O . HOH K 5 . ? 70.592 88.501 55.615 1.00 55.32 ? 2217 HOH A O 1 HETATM 5457 O O . HOH K 5 . ? 68.077 89.505 51.787 1.00 46.00 ? 2218 HOH A O 1 HETATM 5458 O O . HOH K 5 . ? 73.670 94.077 51.254 1.00 50.85 ? 2219 HOH A O 1 HETATM 5459 O O . HOH K 5 . ? 75.913 86.083 56.049 1.00 43.29 ? 2220 HOH A O 1 HETATM 5460 O O . HOH K 5 . ? 75.245 84.031 57.934 1.00 56.96 ? 2221 HOH A O 1 HETATM 5461 O O . HOH K 5 . ? 66.596 86.225 49.567 1.00 45.30 ? 2222 HOH A O 1 HETATM 5462 O O . HOH K 5 . ? 71.284 89.566 47.799 1.00 34.97 ? 2223 HOH A O 1 HETATM 5463 O O . HOH K 5 . ? 65.888 77.761 39.920 1.00 45.49 ? 2224 HOH A O 1 HETATM 5464 O O . HOH K 5 . ? 62.818 85.447 40.063 1.00 35.85 ? 2225 HOH A O 1 HETATM 5465 O O . HOH K 5 . ? 61.113 86.247 43.604 1.00 48.93 ? 2226 HOH A O 1 HETATM 5466 O O . HOH K 5 . ? 62.322 86.672 45.377 1.00 71.32 ? 2227 HOH A O 1 HETATM 5467 O O . HOH K 5 . ? 60.863 81.478 41.561 1.00 54.34 ? 2228 HOH A O 1 HETATM 5468 O O . HOH K 5 . ? 62.854 81.027 34.409 1.00 46.06 ? 2229 HOH A O 1 HETATM 5469 O O . HOH K 5 . ? 58.560 83.866 38.246 1.00 49.14 ? 2230 HOH A O 1 HETATM 5470 O O . HOH K 5 . ? 65.384 77.805 36.815 1.00 42.64 ? 2231 HOH A O 1 HETATM 5471 O O . HOH K 5 . ? 69.456 74.226 31.897 1.00 66.51 ? 2232 HOH A O 1 HETATM 5472 O O . HOH K 5 . ? 68.737 75.861 34.121 1.00 37.67 ? 2233 HOH A O 1 HETATM 5473 O O . HOH K 5 . ? 69.468 80.953 24.813 1.00 53.95 ? 2234 HOH A O 1 HETATM 5474 O O . HOH K 5 . ? 75.797 79.868 23.998 1.00 35.16 ? 2235 HOH A O 1 HETATM 5475 O O . HOH K 5 . ? 77.574 77.374 26.849 1.00 35.92 ? 2236 HOH A O 1 HETATM 5476 O O . HOH K 5 . ? 75.474 73.136 33.106 1.00 47.64 ? 2237 HOH A O 1 HETATM 5477 O O . HOH K 5 . ? 69.470 74.878 36.617 1.00 38.42 ? 2238 HOH A O 1 HETATM 5478 O O . HOH K 5 . ? 75.963 71.896 35.737 1.00 54.24 ? 2239 HOH A O 1 HETATM 5479 O O . HOH K 5 . ? 94.315 86.687 33.608 1.00 44.75 ? 2240 HOH A O 1 HETATM 5480 O O . HOH K 5 . ? 92.489 75.389 29.203 1.00 67.48 ? 2241 HOH A O 1 HETATM 5481 O O . HOH K 5 . ? 103.813 72.354 41.918 1.00 68.38 ? 2242 HOH A O 1 HETATM 5482 O O . HOH K 5 . ? 88.429 80.647 53.232 1.00 58.13 ? 2243 HOH A O 1 HETATM 5483 O O . HOH K 5 . ? 75.229 75.204 53.997 1.00 54.18 ? 2244 HOH A O 1 HETATM 5484 O O . HOH K 5 . ? 70.910 77.225 47.966 1.00 47.68 ? 2245 HOH A O 1 HETATM 5485 O O . HOH K 5 . ? 67.263 82.188 50.942 1.00 51.41 ? 2246 HOH A O 1 HETATM 5486 O O . HOH K 5 . ? 68.040 85.208 54.138 1.00 58.32 ? 2247 HOH A O 1 HETATM 5487 O O . HOH K 5 . ? 67.482 79.623 46.386 1.00 59.70 ? 2248 HOH A O 1 HETATM 5488 O O . HOH K 5 . ? 66.724 76.436 45.100 1.00 65.65 ? 2249 HOH A O 1 HETATM 5489 O O . HOH K 5 . ? 66.355 79.857 49.021 1.00 58.01 ? 2250 HOH A O 1 HETATM 5490 O O . HOH K 5 . ? 69.938 70.812 54.257 1.00 42.68 ? 2251 HOH A O 1 HETATM 5491 O O . HOH K 5 . ? 62.478 75.129 51.953 1.00 73.11 ? 2252 HOH A O 1 HETATM 5492 O O . HOH K 5 . ? 70.153 72.916 44.044 1.00 42.63 ? 2253 HOH A O 1 HETATM 5493 O O . HOH K 5 . ? 90.883 71.697 32.418 1.00 63.46 ? 2254 HOH A O 1 HETATM 5494 O O . HOH K 5 . ? 92.525 68.717 35.308 1.00 53.80 ? 2255 HOH A O 1 HETATM 5495 O O . HOH K 5 . ? 80.257 70.440 31.004 1.00 61.43 ? 2256 HOH A O 1 HETATM 5496 O O . HOH K 5 . ? 89.675 67.938 34.485 1.00 54.93 ? 2257 HOH A O 1 HETATM 5497 O O . HOH K 5 . ? 71.678 66.031 45.108 1.00 56.97 ? 2258 HOH A O 1 HETATM 5498 O O . HOH K 5 . ? 75.626 63.736 45.270 1.00 54.04 ? 2259 HOH A O 1 HETATM 5499 O O . HOH K 5 . ? 84.497 59.549 50.673 1.00 53.02 ? 2260 HOH A O 1 HETATM 5500 O O . HOH K 5 . ? 77.422 59.512 41.829 1.00 53.30 ? 2261 HOH A O 1 HETATM 5501 O O . HOH K 5 . ? 81.869 59.260 51.986 1.00 53.20 ? 2262 HOH A O 1 HETATM 5502 O O . HOH K 5 . ? 77.417 78.249 60.405 1.00 44.70 ? 2263 HOH A O 1 HETATM 5503 O O . HOH K 5 . ? 88.832 73.272 54.183 1.00 54.33 ? 2264 HOH A O 1 HETATM 5504 O O . HOH K 5 . ? 96.594 65.051 46.244 1.00 53.71 ? 2265 HOH A O 1 HETATM 5505 O O . HOH K 5 . ? 92.788 72.642 30.280 1.00 59.20 ? 2266 HOH A O 1 HETATM 5506 O O . HOH K 5 . ? 94.917 72.868 25.068 1.00 53.10 ? 2267 HOH A O 1 HETATM 5507 O O . HOH K 5 . ? 72.101 71.374 37.360 1.00 55.75 ? 2268 HOH A O 1 HETATM 5508 O O . HOH K 5 . ? 66.366 77.879 43.484 1.00 51.30 ? 2269 HOH A O 1 HETATM 5509 O O . HOH K 5 . ? 74.566 81.647 14.936 1.00 59.22 ? 2270 HOH A O 1 HETATM 5510 O O . HOH K 5 . ? 76.047 86.336 11.602 1.00 50.61 ? 2271 HOH A O 1 HETATM 5511 O O . HOH K 5 . ? 76.993 107.897 -12.006 1.00 59.80 ? 2272 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 . GLY A 11 ? 0.9265 1.1009 0.6616 -0.4065 0.1942 0.1215 25 GLY A N 2 C CA . GLY A 11 ? 0.9789 1.1514 0.7196 -0.4089 0.1987 0.1269 25 GLY A CA 3 C C . GLY A 11 ? 1.0346 1.2003 0.7792 -0.4096 0.1957 0.1312 25 GLY A C 4 O O . GLY A 11 ? 1.0543 1.2188 0.8089 -0.4111 0.1951 0.1296 25 GLY A O 5 N N . ALA A 12 ? 1.0489 1.2103 0.7858 -0.4086 0.1941 0.1370 26 ALA A N 6 C CA . ALA A 12 ? 1.0318 1.1859 0.7720 -0.4089 0.1917 0.1415 26 ALA A CA 7 C C . ALA A 12 ? 1.0404 1.1918 0.7767 -0.4066 0.1852 0.1389 26 ALA A C 8 O O . ALA A 12 ? 1.0703 1.2240 0.7973 -0.4044 0.1827 0.1379 26 ALA A O 9 C CB . ALA A 12 ? 1.0318 1.1826 0.7678 -0.4091 0.1945 0.1504 26 ALA A CB 10 N N . TYR A 13 ? 1.0202 1.1669 0.7636 -0.4075 0.1826 0.1377 27 TYR A N 11 C CA . TYR A 13 ? 0.9843 1.1276 0.7250 -0.4056 0.1767 0.1354 27 TYR A CA 12 C C . TYR A 13 ? 1.0123 1.1470 0.7561 -0.4062 0.1762 0.1409 27 TYR A C 13 O O . TYR A 13 ? 1.0425 1.1737 0.7954 -0.4087 0.1776 0.1404 27 TYR A O 14 C CB . TYR A 13 ? 0.9202 1.0661 0.6665 -0.4062 0.1735 0.1271 27 TYR A CB 15 C CG . TYR A 13 ? 0.9029 1.0570 0.6493 -0.4059 0.1748 0.1216 27 TYR A CG 16 C CD1 . TYR A 13 ? 0.8788 1.0367 0.6171 -0.4033 0.1723 0.1180 27 TYR A CD1 17 C CD2 . TYR A 13 ? 0.9064 1.0642 0.6616 -0.4082 0.1788 0.1199 27 TYR A CD2 18 C CE1 . TYR A 13 ? 0.8771 1.0420 0.6164 -0.4030 0.1743 0.1128 27 TYR A CE1 19 C CE2 . TYR A 13 ? 0.9053 1.0704 0.6620 -0.4078 0.1806 0.1152 27 TYR A CE2 20 C CZ . TYR A 13 ? 0.9095 1.0779 0.6583 -0.4052 0.1786 0.1117 27 TYR A CZ 21 O OH . TYR A 13 ? 0.9170 1.0921 0.6682 -0.4048 0.1813 0.1070 27 TYR A OH 22 N N . VAL A 14 ? 1.0014 1.1329 0.7383 -0.4039 0.1745 0.1461 28 VAL A N 23 C CA . VAL A 14 ? 1.0093 1.1323 0.7497 -0.4041 0.1748 0.1522 28 VAL A CA 24 C C . VAL A 14 ? 1.0252 1.1436 0.7685 -0.4038 0.1702 0.1476 28 VAL A C 25 O O . VAL A 14 ? 0.9856 1.1064 0.7232 -0.4018 0.1655 0.1433 28 VAL A O 26 C CB . VAL A 14 ? 1.0248 1.1464 0.7576 -0.4016 0.1749 0.1607 28 VAL A CB 27 C CG1 . VAL A 14 ? 1.0219 1.1345 0.7596 -0.4014 0.1754 0.1671 28 VAL A CG1 28 C CG2 . VAL A 14 ? 1.0641 1.1899 0.7940 -0.4024 0.1796 0.1658 28 VAL A CG2 29 N N . LEU A 15 ? 1.0447 1.1565 0.7968 -0.4061 0.1718 0.1482 29 LEU A N 30 C CA . LEU A 15 ? 1.0318 1.1377 0.7864 -0.4062 0.1681 0.1448 29 LEU A CA 31 C C . LEU A 15 ? 1.0730 1.1700 0.8299 -0.4056 0.1702 0.1527 29 LEU A C 32 O O . LEU A 15 ? 1.0639 1.1562 0.8280 -0.4078 0.1750 0.1569 29 LEU A O 33 C CB . LEU A 15 ? 0.9904 1.0959 0.7536 -0.4097 0.1678 0.1378 29 LEU A CB 34 C CG . LEU A 15 ? 0.9651 1.0798 0.7283 -0.4104 0.1666 0.1312 29 LEU A CG 35 C CD1 . LEU A 15 ? 0.9504 1.0652 0.7235 -0.4144 0.1674 0.1267 29 LEU A CD1 36 C CD2 . LEU A 15 ? 0.9420 1.0611 0.6985 -0.4079 0.1610 0.1256 29 LEU A CD2 37 N N . ASP A 16 ? 1.0953 1.1900 0.8467 -0.4026 0.1670 0.1550 30 ASP A N 38 C CA . ASP A 16 ? 1.1514 1.2385 0.9048 -0.4013 0.1692 0.1638 30 ASP A CA 39 C C . ASP A 16 ? 1.1723 1.2542 0.9244 -0.3994 0.1652 0.1625 30 ASP A C 40 O O . ASP A 16 ? 1.1314 1.2176 0.8768 -0.3977 0.1600 0.1573 30 ASP A O 41 C CB . ASP A 16 ? 1.2232 1.3140 0.9702 -0.3989 0.1709 0.1725 30 ASP A CB 42 C CG . ASP A 16 ? 1.2947 1.3784 1.0442 -0.3973 0.1733 0.1829 30 ASP A CG 43 O OD1 . ASP A 16 ? 1.3209 1.3960 1.0793 -0.3986 0.1757 0.1840 30 ASP A OD1 44 O OD2 . ASP A 16 ? 1.3154 1.4024 1.0584 -0.3947 0.1728 0.1901 30 ASP A OD2 45 N N . ASP A 17 ? 1.2056 1.2781 0.9648 -0.3999 0.1681 0.1673 31 ASP A N 46 C CA . ASP A 17 ? 1.1956 1.2620 0.9551 -0.3982 0.1654 0.1671 31 ASP A CA 47 C C . ASP A 17 ? 1.1798 1.2425 0.9390 -0.3950 0.1674 0.1786 31 ASP A C 48 O O . ASP A 17 ? 1.1588 1.2152 0.9200 -0.3935 0.1665 0.1805 31 ASP A O 49 C CB . ASP A 17 ? 1.2135 1.2713 0.9828 -0.4016 0.1674 0.1623 31 ASP A CB 50 C CG . ASP A 17 ? 1.2474 1.2992 1.0265 -0.4041 0.1744 0.1676 31 ASP A CG 51 O OD1 . ASP A 17 ? 1.2553 1.3093 1.0337 -0.4030 0.1777 0.1758 31 ASP A OD1 52 O OD2 . ASP A 17 ? 1.2432 1.2881 1.0306 -0.4074 0.1766 0.1636 31 ASP A OD2 53 N N . SER A 18 ? 1.1825 1.2491 0.9392 -0.3941 0.1701 0.1864 32 SER A N 54 C CA . SER A 18 ? 1.1923 1.2557 0.9500 -0.3915 0.1727 0.1985 32 SER A CA 55 C C . SER A 18 ? 1.2090 1.2759 0.9583 -0.3875 0.1675 0.2013 32 SER A C 56 O O . SER A 18 ? 1.1860 1.2474 0.9384 -0.3853 0.1684 0.2090 32 SER A O 57 C CB . SER A 18 ? 1.1937 1.2610 0.9505 -0.3919 0.1768 0.2059 32 SER A CB 58 O OG . SER A 18 ? 1.1938 1.2561 0.9550 -0.3901 0.1805 0.2181 32 SER A OG 59 N N . ASP A 19 ? 1.2508 1.3267 0.9899 -0.3867 0.1624 0.1952 33 ASP A N 60 C CA . ASP A 19 ? 1.2799 1.3598 1.0104 -0.3832 0.1570 0.1965 33 ASP A CA 61 C C . ASP A 19 ? 1.2605 1.3374 0.9913 -0.3829 0.1527 0.1882 33 ASP A C 62 O O . ASP A 19 ? 1.2703 1.3519 0.9931 -0.3807 0.1472 0.1851 33 ASP A O 63 C CB . ASP A 19 ? 1.3267 1.4177 1.0461 -0.3825 0.1540 0.1943 33 ASP A CB 64 C CG . ASP A 19 ? 1.3651 1.4607 1.0759 -0.3790 0.1494 0.1988 33 ASP A CG 65 O OD1 . ASP A 19 ? 1.3804 1.4716 1.0942 -0.3770 0.1499 0.2080 33 ASP A OD1 66 O OD2 . ASP A 19 ? 1.3699 1.4735 1.0715 -0.3783 0.1453 0.1932 33 ASP A OD2 67 N N . GLY A 20 ? 1.2106 1.2793 0.9505 -0.3853 0.1552 0.1844 34 GLY A N 68 C CA . GLY A 20 ? 1.1546 1.2193 0.8954 -0.3854 0.1516 0.1768 34 GLY A CA 69 C C . GLY A 20 ? 1.1015 1.1696 0.8411 -0.3882 0.1490 0.1645 34 GLY A C 70 O O . GLY A 20 ? 1.0912 1.1633 0.8317 -0.3905 0.1509 0.1617 34 GLY A O 71 N N . LEU A 21 ? 1.0691 1.1359 0.8071 -0.3879 0.1446 0.1573 35 LEU A N 72 C CA . LEU A 21 ? 1.0232 1.0924 0.7614 -0.3907 0.1421 0.1459 35 LEU A CA 73 C C . LEU A 21 ? 1.0009 1.0772 0.7302 -0.3887 0.1356 0.1395 35 LEU A C 74 O O . LEU A 21 ? 0.9996 1.0770 0.7230 -0.3853 0.1326 0.1428 35 LEU A O 75 C CB . LEU A 21 ? 1.0041 1.0639 0.7505 -0.3935 0.1434 0.1417 35 LEU A CB 76 C CG . LEU A 21 ? 0.9969 1.0501 0.7533 -0.3965 0.1501 0.1456 35 LEU A CG 77 C CD1 . LEU A 21 ? 0.9873 1.0299 0.7516 -0.3988 0.1519 0.1427 35 LEU A CD1 78 C CD2 . LEU A 21 ? 0.9638 1.0225 0.7218 -0.3996 0.1514 0.1412 35 LEU A CD2 79 N N . GLY A 22 ? 0.9848 1.0661 0.7135 -0.3907 0.1334 0.1305 36 GLY A N 80 C CA . GLY A 22 ? 0.9539 1.0416 0.6755 -0.3891 0.1277 0.1236 36 GLY A CA 81 C C . GLY A 22 ? 0.9192 1.0017 0.6418 -0.3895 0.1241 0.1181 36 GLY A C 82 O O . GLY A 22 ? 0.9136 0.9877 0.6399 -0.3894 0.1256 0.1219 36 GLY A O 83 N N . ARG A 23 ? 0.8741 0.9615 0.5939 -0.3899 0.1195 0.1094 37 ARG A N 84 C CA . ARG A 23 ? 0.8742 0.9573 0.5942 -0.3903 0.1157 0.1037 37 ARG A CA 85 C C . ARG A 23 ? 0.7776 0.8551 0.5055 -0.3948 0.1174 0.0990 37 ARG A C 86 O O . ARG A 23 ? 0.7795 0.8592 0.5122 -0.3976 0.1199 0.0975 37 ARG A O 87 C CB . ARG A 23 ? 0.7664 0.8571 0.4801 -0.3889 0.1100 0.0965 37 ARG A CB 88 C CG . ARG A 23 ? 0.7658 0.8596 0.4714 -0.3845 0.1073 0.1000 37 ARG A CG 89 C CD . ARG A 23 ? 0.7542 0.8530 0.4546 -0.3831 0.1015 0.0925 37 ARG A CD 90 N NE . ARG A 23 ? 0.8946 0.9958 0.5877 -0.3789 0.0988 0.0958 37 ARG A NE 91 C CZ . ARG A 23 ? 0.9136 1.0176 0.6016 -0.3769 0.0937 0.0909 37 ARG A CZ 92 N NH1 . ARG A 23 ? 0.9688 1.0736 0.6584 -0.3786 0.0907 0.0825 37 ARG A NH1 93 N NH2 . ARG A 23 ? 0.8998 1.0061 0.5815 -0.3733 0.0915 0.0945 37 ARG A NH2 94 N N . GLU A 24 ? 0.7830 0.8533 0.5124 -0.3954 0.1160 0.0964 38 GLU A N 95 C CA . GLU A 24 ? 0.8146 0.8796 0.5505 -0.3998 0.1168 0.0905 38 GLU A CA 96 C C . GLU A 24 ? 0.7648 0.8374 0.4997 -0.4019 0.1125 0.0817 38 GLU A C 97 O O . GLU A 24 ? 0.7559 0.8341 0.4849 -0.3998 0.1076 0.0779 38 GLU A O 98 C CB . GLU A 24 ? 0.8667 0.9226 0.6034 -0.3997 0.1161 0.0893 38 GLU A CB 99 C CG . GLU A 24 ? 0.9331 0.9832 0.6756 -0.4044 0.1167 0.0823 38 GLU A CG 100 C CD . GLU A 24 ? 0.9741 1.0144 0.7178 -0.4043 0.1169 0.0811 38 GLU A CD 101 O OE1 . GLU A 24 ? 1.0059 1.0459 0.7445 -0.4006 0.1145 0.0836 38 GLU A OE1 102 O OE2 . GLU A 24 ? 0.9731 1.0060 0.7229 -0.4081 0.1196 0.0775 38 GLU A OE2 103 N N . PHE A 25 ? 0.7665 0.8397 0.5077 -0.4059 0.1145 0.0788 39 PHE A N 104 C CA . PHE A 25 ? 0.7580 0.8385 0.5001 -0.4083 0.1109 0.0713 39 PHE A CA 105 C C . PHE A 25 ? 0.8196 0.8955 0.5622 -0.4106 0.1075 0.0645 39 PHE A C 106 O O . PHE A 25 ? 0.8122 0.8789 0.5588 -0.4129 0.1103 0.0645 39 PHE A O 107 C CB . PHE A 25 ? 0.7628 0.8457 0.5119 -0.4118 0.1145 0.0717 39 PHE A CB 108 C CG . PHE A 25 ? 0.8849 0.9749 0.6369 -0.4147 0.1111 0.0648 39 PHE A CG 109 C CD1 . PHE A 25 ? 0.8640 0.9645 0.6138 -0.4130 0.1081 0.0629 39 PHE A CD1 110 C CD2 . PHE A 25 ? 0.8860 0.9725 0.6437 -0.4194 0.1114 0.0607 39 PHE A CD2 111 C CE1 . PHE A 25 ? 0.7410 0.8485 0.4946 -0.4155 0.1052 0.0576 39 PHE A CE1 112 C CE2 . PHE A 25 ? 0.8729 0.9669 0.6335 -0.4221 0.1080 0.0552 39 PHE A CE2 113 C CZ . PHE A 25 ? 0.8453 0.9500 0.6043 -0.4200 0.1049 0.0540 39 PHE A CZ 114 N N . ASP A 26 ? 0.7895 0.8717 0.5281 -0.4100 0.1018 0.0586 40 ASP A N 115 C CA . ASP A 26 ? 0.7378 0.8165 0.4755 -0.4118 0.0981 0.0521 40 ASP A CA 116 C C . ASP A 26 ? 0.7574 0.8409 0.4988 -0.4159 0.0955 0.0455 40 ASP A C 117 O O . ASP A 26 ? 0.7904 0.8703 0.5317 -0.4182 0.0931 0.0401 40 ASP A O 118 C CB . ASP A 26 ? 0.7293 0.8105 0.4594 -0.4080 0.0931 0.0503 40 ASP A CB 119 C CG . ASP A 26 ? 0.8488 0.9244 0.5751 -0.4042 0.0951 0.0566 40 ASP A CG 120 O OD1 . ASP A 26 ? 0.8614 0.9274 0.5907 -0.4050 0.0989 0.0597 40 ASP A OD1 121 O OD2 . ASP A 26 ? 0.8578 0.9388 0.5784 -0.4003 0.0929 0.0586 40 ASP A OD2 122 N N . GLY A 27 ? 0.6266 0.7201 0.3911 -0.3980 0.0292 0.0002 41 GLY A N 123 C CA . GLY A 27 ? 0.6217 0.7299 0.3921 -0.3990 0.0302 -0.0037 41 GLY A CA 124 C C . GLY A 27 ? 0.6037 0.7369 0.3851 -0.3941 0.0304 -0.0073 41 GLY A C 125 O O . GLY A 27 ? 0.6107 0.7485 0.3979 -0.3867 0.0294 -0.0075 41 GLY A O 126 N N . ILE A 28 ? 0.6046 0.7540 0.3892 -0.3982 0.0319 -0.0100 42 ILE A N 127 C CA . ILE A 28 ? 0.5874 0.7598 0.3844 -0.3926 0.0320 -0.0135 42 ILE A CA 128 C C . ILE A 28 ? 0.6692 0.8416 0.4749 -0.3861 0.0307 -0.0152 42 ILE A C 129 O O . ILE A 28 ? 0.6979 0.8610 0.4986 -0.3906 0.0308 -0.0150 42 ILE A O 130 C CB . ILE A 28 ? 0.6031 0.7958 0.3996 -0.4012 0.0344 -0.0153 42 ILE A CB 131 C CG1 . ILE A 28 ? 0.6186 0.8122 0.4056 -0.4091 0.0359 -0.0136 42 ILE A CG1 132 C CG2 . ILE A 28 ? 0.5775 0.7938 0.3885 -0.3946 0.0346 -0.0188 42 ILE A CG2 133 C CD1 . ILE A 28 ? 0.6268 0.8185 0.4150 -0.4031 0.0351 -0.0127 42 ILE A CD1 134 N N . GLY A 29 ? 0.6075 0.7907 0.4262 -0.3759 0.0295 -0.0169 43 GLY A N 135 C CA . GLY A 29 ? 0.6415 0.8269 0.4693 -0.3696 0.0281 -0.0183 43 GLY A CA 136 C C . GLY A 29 ? 0.6267 0.8332 0.4701 -0.3617 0.0276 -0.0205 43 GLY A C 137 O O . GLY A 29 ? 0.5951 0.8177 0.4427 -0.3623 0.0289 -0.0218 43 GLY A O 138 N N . ALA A 30 ? 0.5816 0.7882 0.4341 -0.3543 0.0257 -0.0211 44 ALA A N 139 C CA . ALA A 30 ? 0.5095 0.7347 0.3783 -0.3460 0.0248 -0.0227 44 ALA A CA 140 C C . ALA A 30 ? 0.5004 0.7180 0.3782 -0.3354 0.0221 -0.0222 44 ALA A C 141 O O . ALA A 30 ? 0.4845 0.6843 0.3554 -0.3357 0.0212 -0.0210 44 ALA A O 142 C CB . ALA A 30 ? 0.5049 0.7481 0.3771 -0.3513 0.0257 -0.0242 44 ALA A CB 143 N N . VAL A 31 ? 0.4617 0.6928 0.3552 -0.3260 0.0210 -0.0231 45 VAL A N 144 C CA . VAL A 31 ? 0.5365 0.7616 0.4399 -0.3155 0.0183 -0.0224 45 VAL A CA 145 C C . VAL A 31 ? 0.5295 0.7662 0.4424 -0.3131 0.0169 -0.0228 45 VAL A C 146 O O . VAL A 31 ? 0.4357 0.6916 0.3580 -0.3127 0.0173 -0.0239 45 VAL A O 147 C CB . VAL A 31 ? 0.5169 0.7468 0.4328 -0.3054 0.0174 -0.0228 45 VAL A CB 148 C CG1 . VAL A 31 ? 0.4131 0.6382 0.3407 -0.2943 0.0145 -0.0221 45 VAL A CG1 149 C CG2 . VAL A 31 ? 0.4349 0.6528 0.3416 -0.3072 0.0184 -0.0221 45 VAL A CG2 150 N N . SER A 32 ? 0.4399 0.6652 0.3503 -0.3115 0.0154 -0.0220 46 SER A N 151 C CA . SER A 32 ? 0.4525 0.6893 0.3707 -0.3092 0.0136 -0.0222 46 SER A CA 152 C C . SER A 32 ? 0.4393 0.6714 0.3683 -0.2977 0.0111 -0.0213 46 SER A C 153 O O . SER A 32 ? 0.4174 0.6319 0.3408 -0.2956 0.0103 -0.0205 46 SER A O 154 C CB . SER A 32 ? 0.4691 0.6997 0.3756 -0.3173 0.0138 -0.0222 46 SER A CB 155 O OG . SER A 32 ? 0.4816 0.7195 0.3955 -0.3134 0.0116 -0.0219 46 SER A OG 156 N N . GLY A 33 ? 0.4132 0.6606 0.3580 -0.2902 0.0100 -0.0215 47 GLY A N 157 C CA . GLY A 33 ? 0.3861 0.6298 0.3425 -0.2790 0.0076 -0.0207 47 GLY A CA 158 C C . GLY A 33 ? 0.3997 0.6523 0.3695 -0.2716 0.0077 -0.0216 47 GLY A C 159 O O . GLY A 33 ? 0.4118 0.6734 0.3813 -0.2753 0.0098 -0.0229 47 GLY A O 160 N N . GLY A 34 ? 0.4052 0.6552 0.3870 -0.2611 0.0054 -0.0210 48 GLY A N 161 C CA . GLY A 34 ? 0.3894 0.6486 0.3861 -0.2530 0.0052 -0.0221 48 GLY A CA 162 C C . GLY A 34 ? 0.4338 0.7154 0.4413 -0.2537 0.0060 -0.0234 48 GLY A C 163 O O . GLY A 34 ? 0.3563 0.6454 0.3663 -0.2545 0.0080 -0.0252 48 GLY A O 164 N N . GLY A 35 ? 0.4509 0.7436 0.4653 -0.2532 0.0043 -0.0224 49 GLY A N 165 C CA . GLY A 35 ? 0.4604 0.7461 0.4732 -0.2515 0.0018 -0.0204 49 GLY A CA 166 C C . GLY A 35 ? 0.4298 0.7289 0.4421 -0.2573 0.0013 -0.0195 49 GLY A C 167 O O . GLY A 35 ? 0.4118 0.7289 0.4354 -0.2564 0.0013 -0.0199 49 GLY A O 168 N N . ALA A 36 ? 0.3998 0.6903 0.3993 -0.2633 0.0009 -0.0185 50 ALA A N 169 C CA . ALA A 36 ? 0.4113 0.7136 0.4085 -0.2696 0.0003 -0.0177 50 ALA A CA 170 C C . ALA A 36 ? 0.4253 0.7410 0.4194 -0.2779 0.0026 -0.0190 50 ALA A C 171 O O . ALA A 36 ? 0.4064 0.7391 0.4073 -0.2798 0.0019 -0.0184 50 ALA A O 172 C CB . ALA A 36 ? 0.3865 0.7013 0.4002 -0.2619 -0.0028 -0.0158 50 ALA A CB 173 N N . THR A 37 ? 0.4351 0.7434 0.4193 -0.2828 0.0054 -0.0206 51 THR A N 174 C CA . THR A 37 ? 0.3929 0.7137 0.3747 -0.2903 0.0078 -0.0220 51 THR A CA 175 C C . THR A 37 ? 0.4573 0.7808 0.4269 -0.3015 0.0083 -0.0219 51 THR A C 176 O O . THR A 37 ? 0.4160 0.7542 0.3865 -0.3073 0.0095 -0.0226 51 THR A O 177 C CB . THR A 37 ? 0.3970 0.7099 0.3719 -0.2926 0.0105 -0.0236 51 THR A CB 178 O OG1 . THR A 37 ? 0.4388 0.7313 0.3969 -0.2977 0.0113 -0.0232 51 THR A OG1 179 C CG2 . THR A 37 ? 0.3816 0.6940 0.3693 -0.2820 0.0101 -0.0242 51 THR A CG2 180 N N . SER A 38 ? 0.4148 0.7243 0.3731 -0.3044 0.0076 -0.0212 52 SER A N 181 C CA . SER A 38 ? 0.4510 0.7613 0.3970 -0.3150 0.0081 -0.0214 52 SER A CA 182 C C . SER A 38 ? 0.4774 0.7965 0.4285 -0.3137 0.0054 -0.0199 52 SER A C 183 O O . SER A 38 ? 0.4530 0.7695 0.3932 -0.3215 0.0055 -0.0200 52 SER A O 184 C CB . SER A 38 ? 0.4659 0.7540 0.3946 -0.3205 0.0095 -0.0220 52 SER A CB 185 O OG . SER A 38 ? 0.5057 0.7852 0.4289 -0.3223 0.0117 -0.0228 52 SER A OG 186 N N . ARG A 39 ? 0.4369 0.7666 0.4047 -0.3042 0.0032 -0.0184 53 ARG A N 187 C CA . ARG A 39 ? 0.4650 0.8020 0.4392 -0.3013 0.0002 -0.0163 53 ARG A CA 188 C C . ARG A 39 ? 0.4682 0.8199 0.4388 -0.3102 -0.0002 -0.0159 53 ARG A C 189 O O . ARG A 39 ? 0.4471 0.7979 0.4128 -0.3128 -0.0017 -0.0148 53 ARG A O 190 C CB . ARG A 39 ? 0.3900 0.7374 0.3845 -0.2897 -0.0021 -0.0148 53 ARG A CB 191 C CG . ARG A 39 ? 0.4732 0.8288 0.4758 -0.2859 -0.0054 -0.0120 53 ARG A CG 192 C CD . ARG A 39 ? 0.4870 0.8255 0.4820 -0.2837 -0.0066 -0.0113 53 ARG A CD 193 N NE . ARG A 39 ? 0.4668 0.8133 0.4668 -0.2820 -0.0096 -0.0086 53 ARG A NE 194 C CZ . ARG A 39 ? 0.4500 0.8000 0.4397 -0.2904 -0.0100 -0.0081 53 ARG A CZ 195 N NH1 . ARG A 39 ? 0.4865 0.8322 0.4607 -0.3011 -0.0074 -0.0104 53 ARG A NH1 196 N NH2 . ARG A 39 ? 0.4021 0.7599 0.3968 -0.2884 -0.0129 -0.0053 53 ARG A NH2 197 N N . LEU A 40 ? 0.4652 0.8307 0.4382 -0.3151 0.0013 -0.0168 54 LEU A N 198 C CA . LEU A 40 ? 0.4643 0.8466 0.4370 -0.3227 0.0007 -0.0161 54 LEU A CA 199 C C . LEU A 40 ? 0.4535 0.8300 0.4079 -0.3355 0.0031 -0.0181 54 LEU A C 200 O O . LEU A 40 ? 0.5577 0.9468 0.5097 -0.3433 0.0029 -0.0179 54 LEU A O 201 C CB . LEU A 40 ? 0.4585 0.8614 0.4470 -0.3200 0.0006 -0.0157 54 LEU A CB 202 C CG . LEU A 40 ? 0.4117 0.8230 0.4206 -0.3077 -0.0018 -0.0138 54 LEU A CG 203 C CD1 . LEU A 40 ? 0.4085 0.8375 0.4319 -0.3058 -0.0008 -0.0145 54 LEU A CD1 204 C CD2 . LEU A 40 ? 0.4085 0.8273 0.4232 -0.3054 -0.0053 -0.0106 54 LEU A CD2 205 N N . LEU A 41 ? 0.5264 0.8837 0.4685 -0.3378 0.0053 -0.0198 55 LEU A N 206 C CA . LEU A 41 ? 0.5254 0.8753 0.4506 -0.3498 0.0077 -0.0217 55 LEU A CA 207 C C . LEU A 41 ? 0.5094 0.8527 0.4241 -0.3550 0.0068 -0.0217 55 LEU A C 208 O O . LEU A 41 ? 0.5589 0.9053 0.4638 -0.3655 0.0079 -0.0229 55 LEU A O 209 C CB . LEU A 41 ? 0.5259 0.8567 0.4417 -0.3504 0.0102 -0.0232 55 LEU A CB 210 C CG . LEU A 41 ? 0.5661 0.8871 0.4647 -0.3626 0.0128 -0.0250 55 LEU A CG 211 C CD1 . LEU A 41 ? 0.5687 0.9070 0.4676 -0.3710 0.0140 -0.0257 55 LEU A CD1 212 C CD2 . LEU A 41 ? 0.5289 0.8299 0.4190 -0.3625 0.0148 -0.0258 55 LEU A CD2 213 N N . VAL A 42 ? 0.4944 0.8291 0.4117 -0.3479 0.0050 -0.0206 56 VAL A N 214 C CA . VAL A 42 ? 0.5156 0.8396 0.4214 -0.3523 0.0047 -0.0212 56 VAL A CA 215 C C . VAL A 42 ? 0.5597 0.8988 0.4640 -0.3591 0.0034 -0.0206 56 VAL A C 216 O O . VAL A 42 ? 0.5066 0.8384 0.3979 -0.3672 0.0044 -0.0222 56 VAL A O 217 C CB . VAL A 42 ? 0.4723 0.7840 0.3820 -0.3426 0.0030 -0.0200 56 VAL A CB 218 C CG1 . VAL A 42 ? 0.4875 0.7821 0.3963 -0.3371 0.0044 -0.0208 56 VAL A CG1 219 C CG2 . VAL A 42 ? 0.4564 0.7835 0.3828 -0.3334 -0.0004 -0.0171 56 VAL A CG2 220 N N . ASN A 43 ? 0.5545 0.9144 0.4723 -0.3558 0.0012 -0.0184 57 ASN A N 221 C CA . ASN A 43 ? 0.5570 0.9331 0.4746 -0.3620 -0.0004 -0.0172 57 ASN A CA 222 C C . ASN A 43 ? 0.5856 0.9765 0.5021 -0.3710 0.0008 -0.0181 57 ASN A C 223 O O . ASN A 43 ? 0.5750 0.9837 0.4956 -0.3746 -0.0009 -0.0166 57 ASN A O 224 C CB . ASN A 43 ? 0.5258 0.9158 0.4590 -0.3532 -0.0042 -0.0136 57 ASN A CB 225 C CG . ASN A 43 ? 0.5259 0.9262 0.4768 -0.3440 -0.0050 -0.0120 57 ASN A CG 226 O OD1 . ASN A 43 ? 0.5390 0.9304 0.4908 -0.3407 -0.0030 -0.0136 57 ASN A OD1 227 N ND2 . ASN A 43 ? 0.5290 0.9481 0.4943 -0.3399 -0.0079 -0.0089 57 ASN A ND2 228 N N . TYR A 44 ? 0.5688 0.9529 0.4799 -0.3747 0.0038 -0.0203 58 TYR A N 229 C CA . TYR A 44 ? 0.5738 0.9692 0.4806 -0.3851 0.0054 -0.0216 58 TYR A CA 230 C C . TYR A 44 ? 0.6130 1.0054 0.5054 -0.3962 0.0059 -0.0230 58 TYR A C 231 O O . TYR A 44 ? 0.6124 0.9867 0.4935 -0.3979 0.0069 -0.0246 58 TYR A O 232 C CB . TYR A 44 ? 0.5296 0.9161 0.4312 -0.3879 0.0086 -0.0237 58 TYR A CB 233 C CG . TYR A 44 ? 0.5703 0.9708 0.4861 -0.3826 0.0087 -0.0229 58 TYR A CG 234 C CD1 . TYR A 44 ? 0.5020 0.9021 0.4307 -0.3704 0.0075 -0.0215 58 TYR A CD1 235 C CD2 . TYR A 44 ? 0.5791 0.9933 0.4957 -0.3898 0.0103 -0.0238 58 TYR A CD2 236 C CE1 . TYR A 44 ? 0.5710 0.9839 0.5133 -0.3654 0.0079 -0.0213 58 TYR A CE1 237 C CE2 . TYR A 44 ? 0.5584 0.9858 0.4885 -0.3849 0.0107 -0.0234 58 TYR A CE2 238 C CZ . TYR A 44 ? 0.5628 0.9893 0.5058 -0.3726 0.0096 -0.0223 58 TYR A CZ 239 O OH . TYR A 44 ? 0.4942 0.9336 0.4513 -0.3675 0.0103 -0.0224 58 TYR A OH 240 N N . PRO A 45 ? 0.6548 1.0654 0.5483 -0.4036 0.0052 -0.0226 59 PRO A N 241 C CA . PRO A 45 ? 0.6687 1.0777 0.5482 -0.4156 0.0062 -0.0245 59 PRO A CA 242 C C . PRO A 45 ? 0.6885 1.0836 0.5547 -0.4243 0.0099 -0.0279 59 PRO A C 243 O O . PRO A 45 ? 0.6894 1.0842 0.5589 -0.4231 0.0115 -0.0282 59 PRO A O 244 C CB . PRO A 45 ? 0.6767 1.1108 0.5637 -0.4203 0.0044 -0.0229 59 PRO A CB 245 C CG . PRO A 45 ? 0.6860 1.1339 0.5918 -0.4088 0.0017 -0.0194 59 PRO A CG 246 C CD . PRO A 45 ? 0.6706 1.1049 0.5799 -0.4004 0.0032 -0.0201 59 PRO A CD 247 N N . GLU A 46 ? 0.7302 1.1137 0.5818 -0.4331 0.0115 -0.0304 60 GLU A N 248 C CA . GLU A 46 ? 0.8049 1.1782 0.6444 -0.4433 0.0149 -0.0333 60 GLU A CA 249 C C . GLU A 46 ? 0.7860 1.1794 0.6275 -0.4519 0.0150 -0.0333 60 GLU A C 250 O O . GLU A 46 ? 0.7902 1.2023 0.6385 -0.4523 0.0125 -0.0317 60 GLU A O 251 C CB . GLU A 46 ? 0.8479 1.2030 0.6722 -0.4502 0.0167 -0.0363 60 GLU A CB 252 C CG . GLU A 46 ? 0.8650 1.1992 0.6871 -0.4420 0.0169 -0.0364 60 GLU A CG 253 C CD . GLU A 46 ? 0.9003 1.2180 0.7217 -0.4375 0.0187 -0.0365 60 GLU A CD 254 O OE1 . GLU A 46 ? 0.8876 1.2112 0.7119 -0.4392 0.0196 -0.0361 60 GLU A OE1 255 O OE2 . GLU A 46 ? 0.9314 1.2303 0.7496 -0.4322 0.0191 -0.0370 60 GLU A OE2 256 N N . PRO A 47 ? 0.7793 1.1695 0.6155 -0.4590 0.0177 -0.0350 61 PRO A N 257 C CA . PRO A 47 ? 0.7611 1.1299 0.5887 -0.4601 0.0206 -0.0367 61 PRO A CA 258 C C . PRO A 47 ? 0.7087 1.0762 0.5458 -0.4499 0.0205 -0.0349 61 PRO A C 259 O O . PRO A 47 ? 0.7233 1.0734 0.5545 -0.4494 0.0225 -0.0357 61 PRO A O 260 C CB . PRO A 47 ? 0.6611 1.0342 0.4817 -0.4726 0.0230 -0.0384 61 PRO A CB 261 C CG . PRO A 47 ? 0.6560 1.0555 0.4884 -0.4725 0.0212 -0.0367 61 PRO A CG 262 C CD . PRO A 47 ? 0.6462 1.0558 0.4850 -0.4672 0.0179 -0.0351 61 PRO A CD 263 N N . TYR A 48 ? 0.6624 1.0481 0.5142 -0.4423 0.0182 -0.0326 62 TYR A N 264 C CA . TYR A 48 ? 0.6659 1.0550 0.5280 -0.4343 0.0184 -0.0315 62 TYR A CA 265 C C . TYR A 48 ? 0.6548 1.0240 0.5158 -0.4254 0.0187 -0.0312 62 TYR A C 266 O O . TYR A 48 ? 0.6640 1.0261 0.5249 -0.4234 0.0204 -0.0314 62 TYR A O 267 C CB . TYR A 48 ? 0.7332 1.1451 0.6125 -0.4272 0.0158 -0.0291 62 TYR A CB 268 C CG . TYR A 48 ? 0.8261 1.2592 0.7084 -0.4350 0.0150 -0.0289 62 TYR A CG 269 C CD1 . TYR A 48 ? 0.9103 1.3452 0.7832 -0.4472 0.0174 -0.0308 62 TYR A CD1 270 C CD2 . TYR A 48 ? 0.8388 1.2905 0.7339 -0.4302 0.0119 -0.0264 62 TYR A CD2 271 C CE1 . TYR A 48 ? 0.9372 1.3919 0.8132 -0.4545 0.0166 -0.0305 62 TYR A CE1 272 C CE2 . TYR A 48 ? 0.8845 1.3561 0.7829 -0.4373 0.0110 -0.0259 62 TYR A CE2 273 C CZ . TYR A 48 ? 0.9270 1.4001 0.8157 -0.4495 0.0133 -0.0280 62 TYR A CZ 274 O OH . TYR A 48 ? 0.9492 1.4424 0.8414 -0.4567 0.0124 -0.0274 62 TYR A OH 275 N N . ARG A 49 ? 0.6048 0.9653 0.4649 -0.4203 0.0170 -0.0307 63 ARG A N 276 C CA . ARG A 49 ? 0.5781 0.9197 0.4376 -0.4116 0.0170 -0.0303 63 ARG A CA 277 C C . ARG A 49 ? 0.6100 0.9308 0.4561 -0.4173 0.0199 -0.0321 63 ARG A C 278 O O . ARG A 49 ? 0.5891 0.9003 0.4365 -0.4123 0.0208 -0.0316 63 ARG A O 279 C CB . ARG A 49 ? 0.5665 0.9020 0.4257 -0.4069 0.0149 -0.0298 63 ARG A CB 280 C CG . ARG A 49 ? 0.6280 0.9550 0.4957 -0.3938 0.0135 -0.0282 63 ARG A CG 281 C CD . ARG A 49 ? 0.6530 0.9740 0.5203 -0.3895 0.0116 -0.0276 63 ARG A CD 282 N NE . ARG A 49 ? 0.6714 0.9743 0.5235 -0.3967 0.0135 -0.0299 63 ARG A NE 283 C CZ . ARG A 49 ? 0.6630 0.9572 0.5117 -0.3947 0.0126 -0.0303 63 ARG A CZ 284 N NH1 . ARG A 49 ? 0.6391 0.9408 0.4982 -0.3858 0.0098 -0.0280 63 ARG A NH1 285 N NH2 . ARG A 49 ? 0.6698 0.9475 0.5051 -0.4015 0.0148 -0.0329 63 ARG A NH2 286 N N . SER A 50 ? 0.6733 0.9878 0.5071 -0.4282 0.0215 -0.0340 64 SER A N 287 C CA . SER A 50 ? 0.7205 1.0148 0.5416 -0.4346 0.0243 -0.0356 64 SER A CA 288 C C . SER A 50 ? 0.7258 1.0240 0.5467 -0.4388 0.0262 -0.0353 64 SER A C 289 O O . SER A 50 ? 0.6704 0.9524 0.4856 -0.4390 0.0279 -0.0352 64 SER A O 290 C CB . SER A 50 ? 0.7412 1.0294 0.5504 -0.4454 0.0256 -0.0380 64 SER A CB 291 O OG . SER A 50 ? 0.7555 1.0225 0.5533 -0.4510 0.0282 -0.0393 64 SER A OG 292 N N . GLU A 51 ? 0.7443 1.0641 0.5715 -0.4421 0.0259 -0.0351 65 GLU A N 293 C CA . GLU A 51 ? 0.7099 1.0365 0.5388 -0.4454 0.0277 -0.0349 65 GLU A CA 294 C C . GLU A 51 ? 0.6783 1.0019 0.5150 -0.4349 0.0275 -0.0334 65 GLU A C 295 O O . GLU A 51 ? 0.6739 0.9881 0.5061 -0.4366 0.0294 -0.0333 65 GLU A O 296 C CB . GLU A 51 ? 0.7227 1.0751 0.5596 -0.4493 0.0271 -0.0349 65 GLU A CB 297 C CG . GLU A 51 ? 0.7780 1.1351 0.6066 -0.4615 0.0277 -0.0364 65 GLU A CG 298 C CD . GLU A 51 ? 0.8205 1.2041 0.6586 -0.4641 0.0266 -0.0360 65 GLU A CD 299 O OE1 . GLU A 51 ? 0.8086 1.2065 0.6597 -0.4570 0.0258 -0.0346 65 GLU A OE1 300 O OE2 . GLU A 51 ? 0.8774 1.2676 0.7106 -0.4732 0.0266 -0.0370 65 GLU A OE2 301 N N . ILE A 52 ? 0.6541 0.9864 0.5030 -0.4243 0.0251 -0.0323 66 ILE A N 302 C CA . ILE A 52 ? 0.6464 0.9769 0.5041 -0.4138 0.0248 -0.0311 66 ILE A CA 303 C C . ILE A 52 ? 0.6227 0.9282 0.4713 -0.4117 0.0257 -0.0309 66 ILE A C 304 O O . ILE A 52 ? 0.5793 0.8794 0.4272 -0.4105 0.0271 -0.0305 66 ILE A O 305 C CB . ILE A 52 ? 0.5995 0.9403 0.4714 -0.4024 0.0219 -0.0299 66 ILE A CB 306 C CG1 . ILE A 52 ? 0.5665 0.9332 0.4503 -0.4030 0.0210 -0.0295 66 ILE A CG1 307 C CG2 . ILE A 52 ? 0.5429 0.8772 0.4224 -0.3914 0.0216 -0.0290 66 ILE A CG2 308 C CD1 . ILE A 52 ? 0.5403 0.9174 0.4366 -0.3942 0.0177 -0.0279 66 ILE A CD1 309 N N . LEU A 53 ? 0.6459 0.9366 0.4877 -0.4117 0.0250 -0.0312 67 LEU A N 310 C CA . LEU A 53 ? 0.6666 0.9330 0.5001 -0.4100 0.0258 -0.0310 67 LEU A CA 311 C C . LEU A 53 ? 0.6643 0.9194 0.4864 -0.4193 0.0285 -0.0314 67 LEU A C 312 O O . LEU A 53 ? 0.6034 0.8438 0.4225 -0.4165 0.0292 -0.0303 67 LEU A O 313 C CB . LEU A 53 ? 0.6838 0.9382 0.5119 -0.4099 0.0249 -0.0318 67 LEU A CB 314 C CG . LEU A 53 ? 0.5699 0.8302 0.4088 -0.3989 0.0221 -0.0308 67 LEU A CG 315 C CD1 . LEU A 53 ? 0.5740 0.8276 0.4078 -0.4005 0.0213 -0.0317 67 LEU A CD1 316 C CD2 . LEU A 53 ? 0.5562 0.8052 0.4001 -0.3885 0.0215 -0.0294 67 LEU A CD2 317 N N . ASP A 54 ? 0.7025 0.9645 0.5186 -0.4304 0.0299 -0.0326 68 ASP A N 318 C CA . ASP A 54 ? 0.7349 0.9885 0.5413 -0.4399 0.0324 -0.0327 68 ASP A CA 319 C C . ASP A 54 ? 0.6795 0.9412 0.4908 -0.4382 0.0333 -0.0315 68 ASP A C 320 O O . ASP A 54 ? 0.6603 0.9085 0.4654 -0.4401 0.0348 -0.0304 68 ASP A O 321 C CB . ASP A 54 ? 0.8002 1.0623 0.6008 -0.4520 0.0336 -0.0344 68 ASP A CB 322 C CG . ASP A 54 ? 0.8822 1.1314 0.6743 -0.4565 0.0338 -0.0361 68 ASP A CG 323 O OD1 . ASP A 54 ? 0.8586 1.0892 0.6477 -0.4514 0.0335 -0.0358 68 ASP A OD1 324 O OD2 . ASP A 54 ? 0.9056 1.1633 0.6941 -0.4655 0.0344 -0.0377 68 ASP A OD2 325 N N . TYR A 55 ? 0.6214 0.9052 0.4439 -0.4345 0.0325 -0.0316 69 TYR A N 326 C CA . TYR A 55 ? 0.7024 0.9958 0.5305 -0.4327 0.0336 -0.0309 69 TYR A CA 327 C C . TYR A 55 ? 0.6490 0.9282 0.4781 -0.4239 0.0333 -0.0295 69 TYR A C 328 O O . TYR A 55 ? 0.6201 0.8981 0.4456 -0.4264 0.0349 -0.0290 69 TYR A O 329 C CB . TYR A 55 ? 0.6923 1.0112 0.5347 -0.4281 0.0327 -0.0314 69 TYR A CB 330 C CG . TYR A 55 ? 0.6653 1.0019 0.5078 -0.4378 0.0338 -0.0325 69 TYR A CG 331 C CD1 . TYR A 55 ? 0.6697 1.0102 0.5081 -0.4456 0.0363 -0.0327 69 TYR A CD1 332 C CD2 . TYR A 55 ? 0.6856 1.0357 0.5329 -0.4390 0.0322 -0.0331 69 TYR A CD2 333 C CE1 . TYR A 55 ? 0.7243 1.0814 0.5634 -0.4545 0.0374 -0.0337 69 TYR A CE1 334 C CE2 . TYR A 55 ? 0.6944 1.0612 0.5424 -0.4477 0.0330 -0.0339 69 TYR A CE2 335 C CZ . TYR A 55 ? 0.7184 1.0886 0.5626 -0.4553 0.0357 -0.0343 69 TYR A CZ 336 O OH . TYR A 55 ? 0.7634 1.1503 0.6086 -0.4641 0.0366 -0.0351 69 TYR A OH 337 N N . LEU A 56 ? 0.6291 0.8985 0.4607 -0.4157 0.0313 -0.0292 70 LEU A N 338 C CA . LEU A 56 ? 0.6356 0.8920 0.4690 -0.4067 0.0306 -0.0278 70 LEU A CA 339 C C . LEU A 56 ? 0.6371 0.8686 0.4572 -0.4107 0.0315 -0.0269 70 LEU A C 340 O O . LEU A 56 ? 0.6218 0.8450 0.4381 -0.4100 0.0322 -0.0256 70 LEU A O 341 C CB . LEU A 56 ? 0.5950 0.8532 0.4385 -0.3955 0.0280 -0.0277 70 LEU A CB 342 C CG . LEU A 56 ? 0.5638 0.8458 0.4220 -0.3900 0.0269 -0.0282 70 LEU A CG 343 C CD1 . LEU A 56 ? 0.5567 0.8403 0.4233 -0.3813 0.0242 -0.0279 70 LEU A CD1 344 C CD2 . LEU A 56 ? 0.5411 0.8304 0.4075 -0.3844 0.0277 -0.0280 70 LEU A CD2 345 N N . PHE A 57 ? 0.6271 0.8470 0.4403 -0.4152 0.0315 -0.0275 71 PHE A N 346 C CA . PHE A 57 ? 0.6608 0.8555 0.4646 -0.4159 0.0319 -0.0266 71 PHE A CA 347 C C . PHE A 57 ? 0.7091 0.8922 0.5005 -0.4280 0.0341 -0.0269 71 PHE A C 348 O O . PHE A 57 ? 0.7424 0.9054 0.5261 -0.4296 0.0349 -0.0256 71 PHE A O 349 C CB . PHE A 57 ? 0.6715 0.8581 0.4779 -0.4090 0.0301 -0.0272 71 PHE A CB 350 C CG . PHE A 57 ? 0.6757 0.8694 0.4941 -0.3965 0.0279 -0.0265 71 PHE A CG 351 C CD1 . PHE A 57 ? 0.6257 0.8138 0.4474 -0.3898 0.0276 -0.0248 71 PHE A CD1 352 C CD2 . PHE A 57 ? 0.6735 0.8794 0.4999 -0.3917 0.0261 -0.0274 71 PHE A CD2 353 C CE1 . PHE A 57 ? 0.5549 0.7494 0.3883 -0.3784 0.0257 -0.0243 71 PHE A CE1 354 C CE2 . PHE A 57 ? 0.6820 0.8942 0.5203 -0.3802 0.0241 -0.0266 71 PHE A CE2 355 C CZ . PHE A 57 ? 0.5432 0.7496 0.3855 -0.3734 0.0239 -0.0252 71 PHE A CZ 356 N N . LYS A 58 ? 0.6929 0.8883 0.4825 -0.4366 0.0350 -0.0285 72 LYS A N 357 C CA . LYS A 58 ? 0.7581 0.9442 0.5369 -0.4485 0.0373 -0.0290 72 LYS A CA 358 C C . LYS A 58 ? 0.7481 0.9298 0.5211 -0.4541 0.0390 -0.0269 72 LYS A C 359 O O . LYS A 58 ? 0.6916 0.8899 0.4683 -0.4551 0.0394 -0.0266 72 LYS A O 360 C CB . LYS A 58 ? 0.8028 1.0067 0.5817 -0.4566 0.0378 -0.0312 72 LYS A CB 361 C CG . LYS A 58 ? 0.8399 1.0353 0.6084 -0.4692 0.0400 -0.0322 72 LYS A CG 362 C CD . LYS A 58 ? 0.8838 1.0983 0.6536 -0.4760 0.0401 -0.0345 72 LYS A CD 363 C CE . LYS A 58 ? 0.9347 1.1425 0.6948 -0.4890 0.0424 -0.0358 72 LYS A CE 364 N NZ . LYS A 58 ? 1.0061 1.2340 0.7681 -0.4953 0.0422 -0.0379 72 LYS A NZ 365 N N . PRO A 59 ? 0.7820 0.9415 0.5461 -0.4579 0.0401 -0.0255 73 PRO A N 366 C CA . PRO A 59 ? 0.8009 0.9525 0.5578 -0.4639 0.0417 -0.0229 73 PRO A CA 367 C C . PRO A 59 ? 0.7934 0.9575 0.5467 -0.4757 0.0438 -0.0234 73 PRO A C 368 O O . PRO A 59 ? 0.7705 0.9394 0.5230 -0.4816 0.0445 -0.0255 73 PRO A O 369 C CB . PRO A 59 ? 0.8086 0.9335 0.5580 -0.4661 0.0425 -0.0217 73 PRO A CB 370 C CG . PRO A 59 ? 0.7790 0.8972 0.5333 -0.4570 0.0408 -0.0234 73 PRO A CG 371 C CD . PRO A 59 ? 0.7865 0.9263 0.5474 -0.4561 0.0399 -0.0263 73 PRO A CD 372 N N . ASN A 60 ? 0.7883 0.9579 0.5394 -0.4792 0.0448 -0.0213 74 ASN A N 373 C CA . ASN A 60 ? 0.8308 1.0128 0.5787 -0.4903 0.0469 -0.0215 74 ASN A CA 374 C C . ASN A 60 ? 0.8057 1.0108 0.5608 -0.4913 0.0466 -0.0246 74 ASN A C 375 O O . ASN A 60 ? 0.7584 0.9675 0.5106 -0.5004 0.0479 -0.0258 74 ASN A O 376 C CB . ASN A 60 ? 0.8718 1.0364 0.6100 -0.5009 0.0489 -0.0204 74 ASN A CB 377 C CG . ASN A 60 ? 0.9111 1.0523 0.6428 -0.5002 0.0491 -0.0167 74 ASN A CG 378 O OD1 . ASN A 60 ? 0.9084 1.0507 0.6396 -0.4976 0.0488 -0.0142 74 ASN A OD1 379 N ND2 . ASN A 60 ? 0.7892 0.9095 0.5164 -0.5024 0.0497 -0.0164 74 ASN A ND2 380 N N . PHE A 61 ? 0.7887 1.0089 0.5538 -0.4818 0.0449 -0.0256 75 PHE A N 381 C CA . PHE A 61 ? 0.7646 1.0063 0.5383 -0.4810 0.0442 -0.0280 75 PHE A CA 382 C C . PHE A 61 ? 0.7633 1.0250 0.5480 -0.4733 0.0434 -0.0283 75 PHE A C 383 O O . PHE A 61 ? 0.7284 1.0084 0.5164 -0.4777 0.0446 -0.0288 75 PHE A O 384 C CB . PHE A 61 ? 0.7679 1.0037 0.5443 -0.4759 0.0424 -0.0294 75 PHE A CB 385 C CG . PHE A 61 ? 0.7876 1.0416 0.5694 -0.4788 0.0419 -0.0316 75 PHE A CG 386 C CD1 . PHE A 61 ? 0.7762 1.0284 0.5505 -0.4902 0.0433 -0.0329 75 PHE A CD1 387 C CD2 . PHE A 61 ? 0.7704 1.0438 0.5638 -0.4712 0.0401 -0.0322 75 PHE A CD2 388 C CE1 . PHE A 61 ? 0.7290 0.9991 0.5066 -0.4943 0.0428 -0.0349 75 PHE A CE1 389 C CE2 . PHE A 61 ? 0.7451 1.0361 0.5423 -0.4750 0.0395 -0.0339 75 PHE A CE2 390 C CZ . PHE A 61 ? 0.7408 1.0305 0.5298 -0.4867 0.0408 -0.0352 75 PHE A CZ 391 N N . GLY A 62 ? 0.7573 1.0157 0.5484 -0.4616 0.0414 -0.0280 76 GLY A N 392 C CA . GLY A 62 ? 0.7157 0.9922 0.5187 -0.4533 0.0406 -0.0285 76 GLY A CA 393 C C . GLY A 62 ? 0.7242 0.9916 0.5266 -0.4467 0.0404 -0.0270 76 GLY A C 394 O O . GLY A 62 ? 0.7246 0.9826 0.5180 -0.4522 0.0418 -0.0255 76 GLY A O 395 N N . ALA A 63 ? 0.6826 0.9528 0.4951 -0.4350 0.0384 -0.0273 77 ALA A N 396 C CA . ALA A 63 ? 0.6418 0.9038 0.4549 -0.4278 0.0379 -0.0261 77 ALA A CA 397 C C . ALA A 63 ? 0.6499 0.8853 0.4517 -0.4290 0.0376 -0.0240 77 ALA A C 398 O O . ALA A 63 ? 0.6405 0.8669 0.4394 -0.4261 0.0376 -0.0224 77 ALA A O 399 C CB . ALA A 63 ? 0.5988 0.8689 0.4258 -0.4149 0.0359 -0.0268 77 ALA A CB 400 N N . SER A 64 ? 0.6538 0.8772 0.4499 -0.4331 0.0374 -0.0241 78 SER A N 401 C CA . SER A 64 ? 0.7009 0.8986 0.4865 -0.4356 0.0375 -0.0223 78 SER A CA 402 C C . SER A 64 ? 0.6912 0.8756 0.4777 -0.4265 0.0362 -0.0205 78 SER A C 403 O O . SER A 64 ? 0.6827 0.8536 0.4612 -0.4297 0.0368 -0.0181 78 SER A O 404 C CB . SER A 64 ? 0.7342 0.9258 0.5085 -0.4477 0.0398 -0.0209 78 SER A CB 405 O OG . SER A 64 ? 0.7141 0.9220 0.4885 -0.4563 0.0413 -0.0225 78 SER A OG 406 N N . LEU A 65 ? 0.6296 0.8181 0.4262 -0.4155 0.0342 -0.0213 79 LEU A N 407 C CA . LEU A 65 ? 0.6557 0.8360 0.4555 -0.4062 0.0328 -0.0199 79 LEU A CA 408 C C . LEU A 65 ? 0.6133 0.7671 0.4052 -0.4054 0.0323 -0.0178 79 LEU A C 409 O O . LEU A 65 ? 0.6204 0.7627 0.4089 -0.4074 0.0323 -0.0183 79 LEU A O 410 C CB . LEU A 65 ? 0.6260 0.8179 0.4397 -0.3947 0.0309 -0.0212 79 LEU A CB 411 C CG . LEU A 65 ? 0.5998 0.8172 0.4236 -0.3931 0.0313 -0.0228 79 LEU A CG 412 C CD1 . LEU A 65 ? 0.5657 0.7931 0.4042 -0.3820 0.0293 -0.0238 79 LEU A CD1 413 C CD2 . LEU A 65 ? 0.6325 0.8538 0.4552 -0.3933 0.0324 -0.0221 79 LEU A CD2 414 N N . HIS A 66 ? 0.6124 0.7569 0.4016 -0.4027 0.0319 -0.0155 80 HIS A N 415 C CA . HIS A 66 ? 0.7032 0.8226 0.4858 -0.4015 0.0314 -0.0131 80 HIS A CA 416 C C . HIS A 66 ? 0.6694 0.7814 0.4599 -0.3893 0.0291 -0.0133 80 HIS A C 417 O O . HIS A 66 ? 0.6912 0.7831 0.4787 -0.3868 0.0285 -0.0121 80 HIS A O 418 C CB . HIS A 66 ? 0.7381 0.8516 0.5138 -0.4047 0.0318 -0.0100 80 HIS A CB 419 C CG . HIS A 66 ? 0.7353 0.8581 0.5041 -0.4162 0.0340 -0.0096 80 HIS A CG 420 N ND1 . HIS A 66 ? 0.7496 0.8822 0.5166 -0.4186 0.0347 -0.0085 80 HIS A ND1 421 C CD2 . HIS A 66 ? 0.7480 0.8722 0.5113 -0.4261 0.0358 -0.0103 80 HIS A CD2 422 C CE1 . HIS A 66 ? 0.7436 0.8832 0.5044 -0.4295 0.0367 -0.0083 80 HIS A CE1 423 N NE2 . HIS A 66 ? 0.7257 0.8602 0.4844 -0.4341 0.0374 -0.0093 80 HIS A NE2 424 N N . ILE A 67 ? 0.6057 0.7342 0.4073 -0.3815 0.0280 -0.0147 81 ILE A N 425 C CA . ILE A 67 ? 0.6219 0.7454 0.4322 -0.3695 0.0258 -0.0146 81 ILE A CA 426 C C . ILE A 67 ? 0.6186 0.7595 0.4413 -0.3632 0.0248 -0.0170 81 ILE A C 427 O O . ILE A 67 ? 0.5438 0.7051 0.3716 -0.3651 0.0255 -0.0184 81 ILE A O 428 C CB . ILE A 67 ? 0.6127 0.7374 0.4254 -0.3645 0.0251 -0.0131 81 ILE A CB 429 C CG1 . ILE A 67 ? 0.6226 0.7301 0.4231 -0.3704 0.0257 -0.0100 81 ILE A CG1 430 C CG2 . ILE A 67 ? 0.5365 0.6568 0.3592 -0.3521 0.0229 -0.0131 81 ILE A CG2 431 C CD1 . ILE A 67 ? 0.6460 0.7547 0.4472 -0.3668 0.0251 -0.0084 81 ILE A CD1 432 N N . LEU A 68 ? 0.5896 0.7227 0.4178 -0.3557 0.0231 -0.0173 82 LEU A N 433 C CA . LEU A 68 ? 0.5627 0.7110 0.4039 -0.3482 0.0217 -0.0188 82 LEU A CA 434 C C . LEU A 68 ? 0.5506 0.6918 0.4005 -0.3363 0.0195 -0.0180 82 LEU A C 435 O O . LEU A 68 ? 0.5041 0.6271 0.3509 -0.3334 0.0187 -0.0172 82 LEU A O 436 C CB . LEU A 68 ? 0.5632 0.7124 0.4032 -0.3516 0.0216 -0.0203 82 LEU A CB 437 C CG . LEU A 68 ? 0.5170 0.6782 0.3696 -0.3436 0.0197 -0.0212 82 LEU A CG 438 C CD1 . LEU A 68 ? 0.4979 0.6829 0.3611 -0.3416 0.0195 -0.0218 82 LEU A CD1 439 C CD2 . LEU A 68 ? 0.5181 0.6780 0.3648 -0.3495 0.0199 -0.0226 82 LEU A CD2 440 N N . LYS A 69 ? 0.5565 0.7118 0.4176 -0.3294 0.0187 -0.0183 83 LYS A N 441 C CA . LYS A 69 ? 0.5646 0.7153 0.4357 -0.3179 0.0165 -0.0176 83 LYS A CA 442 C C . LYS A 69 ? 0.5081 0.6719 0.3928 -0.3107 0.0149 -0.0187 83 LYS A C 443 O O . LYS A 69 ? 0.4511 0.6339 0.3421 -0.3121 0.0153 -0.0198 83 LYS A O 444 C CB . LYS A 69 ? 0.5620 0.7190 0.4371 -0.3147 0.0168 -0.0173 83 LYS A CB 445 C CG . LYS A 69 ? 0.4445 0.5972 0.3305 -0.3028 0.0146 -0.0168 83 LYS A CG 446 C CD . LYS A 69 ? 0.4417 0.5977 0.3283 -0.3017 0.0151 -0.0166 83 LYS A CD 447 C CE . LYS A 69 ? 0.4897 0.6585 0.3933 -0.2910 0.0138 -0.0178 83 LYS A CE 448 N NZ . LYS A 69 ? 0.5152 0.6841 0.4198 -0.2886 0.0140 -0.0178 83 LYS A NZ 449 N N . VAL A 70 ? 0.4447 0.5985 0.3344 -0.3032 0.0129 -0.0182 84 VAL A N 450 C CA . VAL A 70 ? 0.4317 0.5978 0.3330 -0.2972 0.0111 -0.0188 84 VAL A CA 451 C C . VAL A 70 ? 0.4193 0.5823 0.3327 -0.2853 0.0088 -0.0181 84 VAL A C 452 O O . VAL A 70 ? 0.4465 0.5929 0.3577 -0.2814 0.0083 -0.0171 84 VAL A O 453 C CB . VAL A 70 ? 0.5700 0.7318 0.4642 -0.3022 0.0110 -0.0194 84 VAL A CB 454 C CG1 . VAL A 70 ? 0.4598 0.6248 0.3424 -0.3145 0.0133 -0.0203 84 VAL A CG1 455 C CG2 . VAL A 70 ? 0.4435 0.5833 0.3320 -0.2997 0.0105 -0.0188 84 VAL A CG2 456 N N . GLU A 71 ? 0.4243 0.6032 0.3509 -0.2795 0.0073 -0.0185 85 GLU A N 457 C CA . GLU A 71 ? 0.4138 0.5912 0.3532 -0.2682 0.0048 -0.0178 85 GLU A CA 458 C C . GLU A 71 ? 0.4317 0.5960 0.3676 -0.2664 0.0035 -0.0172 85 GLU A C 459 O O . GLU A 71 ? 0.4603 0.6265 0.3899 -0.2723 0.0038 -0.0176 85 GLU A O 460 C CB . GLU A 71 ? 0.3699 0.5682 0.3249 -0.2629 0.0036 -0.0182 85 GLU A CB 461 C CG . GLU A 71 ? 0.3535 0.5511 0.3217 -0.2521 0.0007 -0.0174 85 GLU A CG 462 C CD . GLU A 71 ? 0.3874 0.6052 0.3724 -0.2465 -0.0006 -0.0176 85 GLU A CD 463 O OE1 . GLU A 71 ? 0.4144 0.6472 0.4002 -0.2514 0.0007 -0.0184 85 GLU A OE1 464 O OE2 . GLU A 71 ? 0.3545 0.5729 0.3521 -0.2371 -0.0030 -0.0168 85 GLU A OE2 465 N N . ILE A 72 ? 0.3906 0.5418 0.3304 -0.2587 0.0020 -0.0165 86 ILE A N 466 C CA . ILE A 72 ? 0.4455 0.5868 0.3856 -0.2550 0.0005 -0.0161 86 ILE A CA 467 C C . ILE A 72 ? 0.4075 0.5625 0.3641 -0.2463 -0.0020 -0.0156 86 ILE A C 468 O O . ILE A 72 ? 0.3671 0.5214 0.3348 -0.2374 -0.0035 -0.0152 86 ILE A O 469 C CB . ILE A 72 ? 0.4724 0.5927 0.4092 -0.2509 0.0001 -0.0154 86 ILE A CB 470 C CG1 . ILE A 72 ? 0.4479 0.5545 0.3689 -0.2596 0.0024 -0.0154 86 ILE A CG1 471 C CG2 . ILE A 72 ? 0.4099 0.5211 0.3483 -0.2465 -0.0015 -0.0152 86 ILE A CG2 472 C CD1 . ILE A 72 ? 0.4003 0.4877 0.3190 -0.2555 0.0020 -0.0143 86 ILE A CD1 473 N N . GLY A 73 ? 0.4092 0.5767 0.3673 -0.2491 -0.0025 -0.0157 87 GLY A N 474 C CA . GLY A 73 ? 0.4056 0.5882 0.3791 -0.2420 -0.0048 -0.0149 87 GLY A CA 475 C C . GLY A 73 ? 0.3719 0.5459 0.3547 -0.2319 -0.0072 -0.0140 87 GLY A C 476 O O . GLY A 73 ? 0.3845 0.5435 0.3603 -0.2320 -0.0074 -0.0139 87 GLY A O 477 N N . GLY A 74 ? 0.3491 0.5325 0.3482 -0.2231 -0.0090 -0.0135 88 GLY A N 478 C CA . GLY A 74 ? 0.3225 0.4989 0.3320 -0.2131 -0.0115 -0.0126 88 GLY A CA 479 C C . GLY A 74 ? 0.3549 0.5464 0.3797 -0.2071 -0.0139 -0.0114 88 GLY A C 480 O O . GLY A 74 ? 0.4593 0.6497 0.4972 -0.1976 -0.0161 -0.0108 88 GLY A O 481 N N . ASP A 75 ? 0.3472 0.5528 0.3704 -0.2127 -0.0137 -0.0109 89 ASP A N 482 C CA . ASP A 75 ? 0.3467 0.5676 0.3834 -0.2082 -0.0161 -0.0091 89 ASP A CA 483 C C . ASP A 75 ? 0.3368 0.5708 0.3910 -0.2012 -0.0170 -0.0092 89 ASP A C 484 O O . ASP A 75 ? 0.2808 0.5276 0.3477 -0.1969 -0.0190 -0.0076 89 ASP A O 485 C CB . ASP A 75 ? 0.3507 0.5645 0.3919 -0.2021 -0.0185 -0.0075 89 ASP A CB 486 C CG . ASP A 75 ? 0.3561 0.5607 0.3818 -0.2092 -0.0178 -0.0075 89 ASP A CG 487 O OD1 . ASP A 75 ? 0.3349 0.5427 0.3481 -0.2190 -0.0159 -0.0083 89 ASP A OD1 488 O OD2 . ASP A 75 ? 0.3390 0.5332 0.3652 -0.2050 -0.0191 -0.0069 89 ASP A OD2 489 N N . GLY A 76 ? 0.3536 0.5846 0.4087 -0.2000 -0.0154 -0.0111 90 GLY A N 490 C CA . GLY A 76 ? 0.3134 0.5569 0.3850 -0.1938 -0.0159 -0.0118 90 GLY A CA 491 C C . GLY A 76 ? 0.3063 0.5643 0.3761 -0.2004 -0.0137 -0.0129 90 GLY A C 492 O O . GLY A 76 ? 0.2839 0.5396 0.3383 -0.2099 -0.0115 -0.0135 90 GLY A O 493 N N . GLN A 77 ? 0.2631 0.5359 0.3492 -0.1953 -0.0142 -0.0134 91 GLN A N 494 C CA . GLN A 77 ? 0.3299 0.6175 0.4167 -0.2005 -0.0121 -0.0148 91 GLN A CA 495 C C . GLN A 77 ? 0.3441 0.6247 0.4220 -0.2039 -0.0092 -0.0174 91 GLN A C 496 O O . GLN A 77 ? 0.2941 0.5668 0.3771 -0.1975 -0.0095 -0.0185 91 GLN A O 497 C CB . GLN A 77 ? 0.2597 0.5631 0.3679 -0.1930 -0.0133 -0.0149 91 GLN A CB 498 C CG . GLN A 77 ? 0.3105 0.6262 0.4219 -0.1959 -0.0106 -0.0176 91 GLN A CG 499 C CD . GLN A 77 ? 0.3257 0.6538 0.4302 -0.2052 -0.0093 -0.0171 91 GLN A CD 500 O OE1 . GLN A 77 ? 0.2954 0.6264 0.3904 -0.2126 -0.0064 -0.0190 91 GLN A OE1 501 N NE2 . GLN A 77 ? 0.3133 0.6491 0.4224 -0.2052 -0.0115 -0.0144 91 GLN A NE2 502 N N . THR A 78 ? 0.3235 0.6067 0.3877 -0.2140 -0.0066 -0.0182 92 THR A N 503 C CA . THR A 78 ? 0.3735 0.6489 0.4269 -0.2184 -0.0038 -0.0202 92 THR A CA 504 C C . THR A 78 ? 0.3619 0.6507 0.4132 -0.2250 -0.0009 -0.0221 92 THR A C 505 O O . THR A 78 ? 0.3264 0.6085 0.3652 -0.2310 0.0015 -0.0232 92 THR A O 506 C CB . THR A 78 ? 0.3473 0.6038 0.3818 -0.2244 -0.0033 -0.0193 92 THR A CB 507 O OG1 . THR A 78 ? 0.3442 0.6034 0.3687 -0.2326 -0.0030 -0.0183 92 THR A OG1 508 C CG2 . THR A 78 ? 0.3100 0.5522 0.3481 -0.2166 -0.0058 -0.0180 92 THR A CG2 509 N N . THR A 79 ? 0.3370 0.6443 0.4009 -0.2236 -0.0012 -0.0223 93 THR A N 510 C CA . THR A 79 ? 0.3027 0.6264 0.3727 -0.2260 0.0011 -0.0246 93 THR A CA 511 C C . THR A 79 ? 0.3220 0.6631 0.3978 -0.2294 0.0007 -0.0237 93 THR A C 512 O O . THR A 79 ? 0.3688 0.7255 0.4609 -0.2251 0.0006 -0.0245 93 THR A O 513 C CB . THR A 79 ? 0.3134 0.6334 0.3693 -0.2339 0.0046 -0.0266 93 THR A CB 514 O OG1 . THR A 79 ? 0.3069 0.6158 0.3631 -0.2288 0.0049 -0.0278 93 THR A OG1 515 C CG2 . THR A 79 ? 0.3175 0.6565 0.3796 -0.2372 0.0071 -0.0289 93 THR A CG2 516 N N . ASP A 80 ? 0.3233 0.6618 0.3864 -0.2372 0.0004 -0.0219 94 ASP A N 517 C CA . ASP A 80 ? 0.3224 0.6768 0.3897 -0.2411 -0.0004 -0.0206 94 ASP A CA 518 C C . ASP A 80 ? 0.3409 0.6911 0.4062 -0.2404 -0.0035 -0.0175 94 ASP A C 519 O O . ASP A 80 ? 0.3734 0.7329 0.4358 -0.2463 -0.0041 -0.0162 94 ASP A O 520 C CB . ASP A 80 ? 0.3516 0.7111 0.4053 -0.2529 0.0024 -0.0218 94 ASP A CB 521 C CG . ASP A 80 ? 0.4008 0.7666 0.4569 -0.2539 0.0055 -0.0248 94 ASP A CG 522 O OD1 . ASP A 80 ? 0.3673 0.7486 0.4400 -0.2491 0.0056 -0.0258 94 ASP A OD1 523 O OD2 . ASP A 80 ? 0.3780 0.7335 0.4198 -0.2594 0.0079 -0.0261 94 ASP A OD2 524 N N . GLY A 81 ? 0.3122 0.6493 0.3799 -0.2332 -0.0054 -0.0165 95 GLY A N 525 C CA . GLY A 81 ? 0.3106 0.6429 0.3767 -0.2319 -0.0082 -0.0138 95 GLY A CA 526 C C . GLY A 81 ? 0.4102 0.7220 0.4693 -0.2282 -0.0089 -0.0136 95 GLY A C 527 O O . GLY A 81 ? 0.3209 0.6225 0.3775 -0.2262 -0.0074 -0.0154 95 GLY A O 528 N N . THR A 82 ? 0.3903 0.6963 0.4466 -0.2273 -0.0110 -0.0114 96 THR A N 529 C CA . THR A 82 ? 0.3347 0.6210 0.3828 -0.2251 -0.0115 -0.0113 96 THR A CA 530 C C . THR A 82 ? 0.3468 0.6238 0.3742 -0.2359 -0.0097 -0.0118 96 THR A C 531 O O . THR A 82 ? 0.3381 0.6251 0.3598 -0.2438 -0.0090 -0.0117 96 THR A O 532 C CB . THR A 82 ? 0.3319 0.6166 0.3890 -0.2178 -0.0147 -0.0089 96 THR A CB 533 O OG1 . THR A 82 ? 0.3444 0.6349 0.3949 -0.2239 -0.0156 -0.0071 96 THR A OG1 534 C CG2 . THR A 82 ? 0.3069 0.6036 0.3857 -0.2080 -0.0166 -0.0081 96 THR A CG2 535 N N . GLU A 83 ? 0.3514 0.6093 0.3680 -0.2365 -0.0089 -0.0125 97 GLU A N 536 C CA . GLU A 83 ? 0.4229 0.6706 0.4211 -0.2461 -0.0075 -0.0130 97 GLU A CA 537 C C . GLU A 83 ? 0.4194 0.6516 0.4143 -0.2424 -0.0088 -0.0122 97 GLU A C 538 O O . GLU A 83 ? 0.3463 0.5678 0.3462 -0.2350 -0.0095 -0.0122 97 GLU A O 539 C CB . GLU A 83 ? 0.4366 0.6755 0.4218 -0.2531 -0.0044 -0.0149 97 GLU A CB 540 C CG . GLU A 83 ? 0.4690 0.7234 0.4532 -0.2599 -0.0026 -0.0158 97 GLU A CG 541 C CD . GLU A 83 ? 0.4869 0.7324 0.4554 -0.2692 0.0004 -0.0173 97 GLU A CD 542 O OE1 . GLU A 83 ? 0.4985 0.7284 0.4536 -0.2739 0.0011 -0.0175 97 GLU A OE1 543 O OE2 . GLU A 83 ? 0.4664 0.7204 0.4361 -0.2718 0.0021 -0.0183 97 GLU A OE2 544 N N . PRO A 84 ? 0.3878 0.6193 0.3744 -0.2476 -0.0092 -0.0117 98 PRO A N 545 C CA . PRO A 84 ? 0.3777 0.5969 0.3621 -0.2443 -0.0105 -0.0111 98 PRO A CA 546 C C . PRO A 84 ? 0.3467 0.5437 0.3212 -0.2444 -0.0090 -0.0125 98 PRO A C 547 O O . PRO A 84 ? 0.3724 0.5613 0.3342 -0.2518 -0.0065 -0.0140 98 PRO A O 548 C CB . PRO A 84 ? 0.3504 0.5752 0.3255 -0.2525 -0.0105 -0.0109 98 PRO A CB 549 C CG . PRO A 84 ? 0.3837 0.6177 0.3515 -0.2618 -0.0084 -0.0121 98 PRO A CG 550 C CD . PRO A 84 ? 0.4187 0.6629 0.3988 -0.2569 -0.0085 -0.0118 98 PRO A CD 551 N N . SER A 85 ? 0.3405 0.5278 0.3214 -0.2361 -0.0107 -0.0118 99 SER A N 552 C CA . SER A 85 ? 0.3565 0.5226 0.3300 -0.2349 -0.0097 -0.0128 99 SER A CA 553 C C . SER A 85 ? 0.4226 0.5779 0.3838 -0.2403 -0.0088 -0.0136 99 SER A C 554 O O . SER A 85 ? 0.4276 0.5915 0.3883 -0.2428 -0.0096 -0.0132 99 SER A O 555 C CB . SER A 85 ? 0.3175 0.4786 0.3045 -0.2232 -0.0119 -0.0117 99 SER A CB 556 O OG . SER A 85 ? 0.3287 0.4697 0.3095 -0.2215 -0.0114 -0.0124 99 SER A OG 557 N N . HIS A 86 ? 0.4385 0.5747 0.3896 -0.2423 -0.0071 -0.0149 100 HIS A N 558 C CA . HIS A 86 ? 0.4485 0.5725 0.3891 -0.2465 -0.0061 -0.0162 100 HIS A CA 559 C C . HIS A 86 ? 0.4555 0.5737 0.4041 -0.2379 -0.0082 -0.0154 100 HIS A C 560 O O . HIS A 86 ? 0.4296 0.5417 0.3720 -0.2405 -0.0077 -0.0164 100 HIS A O 561 C CB . HIS A 86 ? 0.4274 0.5326 0.3549 -0.2517 -0.0034 -0.0178 100 HIS A CB 562 C CG . HIS A 86 ? 0.4303 0.5230 0.3623 -0.2447 -0.0039 -0.0170 100 HIS A CG 563 N ND1 . HIS A 86 ? 0.4362 0.5355 0.3748 -0.2417 -0.0044 -0.0160 100 HIS A ND1 564 C CD2 . HIS A 86 ? 0.3830 0.4573 0.3138 -0.2403 -0.0039 -0.0171 100 HIS A CD2 565 C CE1 . HIS A 86 ? 0.4555 0.5412 0.3965 -0.2358 -0.0048 -0.0154 100 HIS A CE1 566 N NE2 . HIS A 86 ? 0.4376 0.5079 0.3740 -0.2348 -0.0047 -0.0160 100 HIS A NE2 567 N N . MET A 87 ? 0.4255 0.5453 0.3878 -0.2280 -0.0104 -0.0138 101 MET A N 568 C CA . MET A 87 ? 0.4052 0.5208 0.3767 -0.2194 -0.0126 -0.0129 101 MET A CA 569 C C . MET A 87 ? 0.3994 0.5307 0.3882 -0.2113 -0.0155 -0.0108 101 MET A C 570 O O . MET A 87 ? 0.3342 0.4639 0.3336 -0.2036 -0.0167 -0.0102 101 MET A O 571 C CB . MET A 87 ? 0.3773 0.4735 0.3490 -0.2139 -0.0125 -0.0134 101 MET A CB 572 C CG . MET A 87 ? 0.4091 0.4878 0.3655 -0.2206 -0.0096 -0.0152 101 MET A CG 573 S SD . MET A 87 ? 0.4829 0.5403 0.4418 -0.2128 -0.0100 -0.0151 101 MET A SD 574 C CE . MET A 87 ? 0.4550 0.5070 0.4188 -0.2073 -0.0114 -0.0153 101 MET A CE 575 N N . HIS A 88 ? 0.3868 0.5329 0.3786 -0.2130 -0.0167 -0.0096 102 HIS A N 576 C CA . HIS A 88 ? 0.3569 0.5184 0.3655 -0.2056 -0.0195 -0.0073 102 HIS A CA 577 C C . HIS A 88 ? 0.3321 0.4862 0.3522 -0.1951 -0.0217 -0.0063 102 HIS A C 578 O O . HIS A 88 ? 0.3987 0.5586 0.4337 -0.1869 -0.0236 -0.0052 102 HIS A O 579 C CB . HIS A 88 ? 0.3291 0.5067 0.3378 -0.2097 -0.0206 -0.0057 102 HIS A CB 580 C CG . HIS A 88 ? 0.3372 0.5265 0.3386 -0.2188 -0.0190 -0.0062 102 HIS A CG 581 N ND1 . HIS A 88 ? 0.3222 0.5163 0.3257 -0.2197 -0.0180 -0.0069 102 HIS A ND1 582 C CD2 . HIS A 88 ? 0.3445 0.5425 0.3368 -0.2274 -0.0185 -0.0062 102 HIS A CD2 583 C CE1 . HIS A 88 ? 0.3593 0.5643 0.3555 -0.2284 -0.0168 -0.0072 102 HIS A CE1 584 N NE2 . HIS A 88 ? 0.3816 0.5890 0.3709 -0.2333 -0.0171 -0.0068 102 HIS A NE2 585 N N . TYR A 89 ? 0.3017 0.4434 0.3154 -0.1955 -0.0215 -0.0069 103 TYR A N 586 C CA . TYR A 89 ? 0.3504 0.4847 0.3741 -0.1863 -0.0234 -0.0061 103 TYR A CA 587 C C . TYR A 89 ? 0.3699 0.4833 0.3844 -0.1868 -0.0217 -0.0082 103 TYR A C 588 O O . TYR A 89 ? 0.3788 0.4845 0.3790 -0.1948 -0.0192 -0.0100 103 TYR A O 589 C CB . TYR A 89 ? 0.3394 0.4813 0.3656 -0.1859 -0.0250 -0.0044 103 TYR A CB 590 C CG . TYR A 89 ? 0.3625 0.5234 0.3886 -0.1910 -0.0256 -0.0027 103 TYR A CG 591 C CD1 . TYR A 89 ? 0.3735 0.5498 0.4139 -0.1860 -0.0277 -0.0005 103 TYR A CD1 592 C CD2 . TYR A 89 ? 0.3771 0.5410 0.3894 -0.2008 -0.0242 -0.0035 103 TYR A CD2 593 C CE1 . TYR A 89 ? 0.3186 0.5126 0.3595 -0.1906 -0.0283 0.0013 103 TYR A CE1 594 C CE2 . TYR A 89 ? 0.3852 0.5671 0.3974 -0.2058 -0.0249 -0.0018 103 TYR A CE2 595 C CZ . TYR A 89 ? 0.3695 0.5664 0.3962 -0.2004 -0.0271 0.0008 103 TYR A CZ 596 O OH . TYR A 89 ? 0.3619 0.5768 0.3895 -0.2050 -0.0279 0.0028 103 TYR A OH 597 N N . GLU A 90 ? 0.3340 0.4380 0.3572 -0.1782 -0.0232 -0.0079 104 GLU A N 598 C CA . GLU A 90 ? 0.4593 0.5438 0.4749 -0.1781 -0.0219 -0.0096 104 GLU A CA 599 C C . GLU A 90 ? 0.4915 0.5737 0.4949 -0.1855 -0.0203 -0.0107 104 GLU A C 600 O O . GLU A 90 ? 0.4685 0.5628 0.4748 -0.1863 -0.0215 -0.0095 104 GLU A O 601 C CB . GLU A 90 ? 0.4715 0.5497 0.5002 -0.1674 -0.0241 -0.0089 104 GLU A CB 602 C CG . GLU A 90 ? 0.5900 0.6483 0.6156 -0.1644 -0.0231 -0.0103 104 GLU A CG 603 C CD . GLU A 90 ? 0.7129 0.7668 0.7529 -0.1536 -0.0254 -0.0098 104 GLU A CD 604 O OE1 . GLU A 90 ? 0.7131 0.7791 0.7653 -0.1486 -0.0275 -0.0084 104 GLU A OE1 605 O OE2 . GLU A 90 ? 0.7754 0.8138 0.8147 -0.1500 -0.0249 -0.0107 104 GLU A OE2 606 N N . LEU A 91 ? 0.4790 0.5458 0.4692 -0.1909 -0.0176 -0.0130 105 LEU A N 607 C CA . LEU A 91 ? 0.4444 0.5070 0.4220 -0.1985 -0.0155 -0.0150 105 LEU A CA 608 C C . LEU A 91 ? 0.4817 0.5567 0.4498 -0.2086 -0.0141 -0.0155 105 LEU A C 609 O O . LEU A 91 ? 0.5248 0.5988 0.4825 -0.2158 -0.0123 -0.0173 105 LEU A O 610 C CB . LEU A 91 ? 0.4858 0.5497 0.4688 -0.1946 -0.0169 -0.0145 105 LEU A CB 611 C CG . LEU A 91 ? 0.4781 0.5300 0.4707 -0.1847 -0.0182 -0.0142 105 LEU A CG 612 C CD1 . LEU A 91 ? 0.4945 0.5465 0.4887 -0.1834 -0.0187 -0.0144 105 LEU A CD1 613 C CD2 . LEU A 91 ? 0.4800 0.5121 0.4658 -0.1849 -0.0161 -0.0161 105 LEU A CD2 614 N N . ASP A 92 ? 0.4122 0.4998 0.3842 -0.2093 -0.0149 -0.0141 106 ASP A N 615 C CA . ASP A 92 ? 0.4447 0.5441 0.4079 -0.2190 -0.0136 -0.0146 106 ASP A CA 616 C C . ASP A 92 ? 0.4466 0.5377 0.3986 -0.2256 -0.0108 -0.0164 106 ASP A C 617 O O . ASP A 92 ? 0.4359 0.5226 0.3920 -0.2218 -0.0110 -0.0158 106 ASP A O 618 C CB . ASP A 92 ? 0.4827 0.6028 0.4569 -0.2164 -0.0160 -0.0118 106 ASP A CB 619 C CG . ASP A 92 ? 0.5478 0.6802 0.5138 -0.2260 -0.0147 -0.0122 106 ASP A CG 620 O OD1 . ASP A 92 ? 0.5845 0.7200 0.5411 -0.2334 -0.0137 -0.0133 106 ASP A OD1 621 O OD2 . ASP A 92 ? 0.5576 0.6969 0.5266 -0.2264 -0.0146 -0.0117 106 ASP A OD2 622 N N . GLU A 93 ? 0.4161 0.5043 0.3540 -0.2357 -0.0081 -0.0187 107 GLU A N 623 C CA . GLU A 93 ? 0.3981 0.4807 0.3255 -0.2430 -0.0055 -0.0202 107 GLU A CA 624 C C . GLU A 93 ? 0.4670 0.5618 0.3853 -0.2535 -0.0041 -0.0214 107 GLU A C 625 O O . GLU A 93 ? 0.4932 0.5892 0.4055 -0.2582 -0.0033 -0.0228 107 GLU A O 626 C CB . GLU A 93 ? 0.4636 0.5235 0.3817 -0.2447 -0.0029 -0.0225 107 GLU A CB 627 C CG . GLU A 93 ? 0.6264 0.6729 0.5519 -0.2353 -0.0041 -0.0213 107 GLU A CG 628 C CD . GLU A 93 ? 0.6531 0.6776 0.5692 -0.2376 -0.0015 -0.0231 107 GLU A CD 629 O OE1 . GLU A 93 ? 0.6302 0.6506 0.5351 -0.2463 0.0010 -0.0245 107 GLU A OE1 630 O OE2 . GLU A 93 ? 0.6762 0.6876 0.5967 -0.2306 -0.0022 -0.0229 107 GLU A OE2 631 N N . ASN A 94 ? 0.4333 0.5376 0.3507 -0.2575 -0.0037 -0.0208 108 ASN A N 632 C CA . ASN A 94 ? 0.4416 0.5572 0.3501 -0.2680 -0.0023 -0.0219 108 ASN A CA 633 C C . ASN A 94 ? 0.4639 0.5797 0.3674 -0.2731 -0.0006 -0.0223 108 ASN A C 634 O O . ASN A 94 ? 0.3996 0.5226 0.3119 -0.2683 -0.0020 -0.0204 108 ASN A O 635 C CB . ASN A 94 ? 0.4581 0.5956 0.3753 -0.2665 -0.0049 -0.0196 108 ASN A CB 636 C CG . ASN A 94 ? 0.5008 0.6509 0.4091 -0.2773 -0.0038 -0.0207 108 ASN A CG 637 O OD1 . ASN A 94 ? 0.5096 0.6592 0.4096 -0.2849 -0.0016 -0.0221 108 ASN A OD1 638 N ND2 . ASN A 94 ? 0.5816 0.7436 0.4919 -0.2781 -0.0053 -0.0197 108 ASN A ND2 639 N N . TYR A 95 ? 0.4285 0.5368 0.3183 -0.2830 0.0024 -0.0248 109 TYR A N 640 C CA . TYR A 95 ? 0.4495 0.5550 0.3336 -0.2881 0.0041 -0.0252 109 TYR A CA 641 C C . TYR A 95 ? 0.4484 0.5691 0.3267 -0.2980 0.0051 -0.0260 109 TYR A C 642 O O . TYR A 95 ? 0.4951 0.6118 0.3641 -0.3059 0.0074 -0.0273 109 TYR A O 643 C CB . TYR A 95 ? 0.4504 0.5329 0.3247 -0.2908 0.0067 -0.0270 109 TYR A CB 644 C CG . TYR A 95 ? 0.4391 0.5076 0.3202 -0.2806 0.0055 -0.0259 109 TYR A CG 645 C CD1 . TYR A 95 ? 0.4968 0.5621 0.3837 -0.2751 0.0046 -0.0239 109 TYR A CD1 646 C CD2 . TYR A 95 ? 0.4364 0.4957 0.3187 -0.2766 0.0052 -0.0268 109 TYR A CD2 647 C CE1 . TYR A 95 ? 0.4676 0.5206 0.3611 -0.2657 0.0032 -0.0227 109 TYR A CE1 648 C CE2 . TYR A 95 ? 0.4681 0.5151 0.3573 -0.2671 0.0039 -0.0257 109 TYR A CE2 649 C CZ . TYR A 95 ? 0.4611 0.5049 0.3560 -0.2617 0.0029 -0.0236 109 TYR A CZ 650 O OH . TYR A 95 ? 0.5119 0.5441 0.4141 -0.2523 0.0014 -0.0224 109 TYR A OH 651 N N . PHE A 96 ? 0.4415 0.5801 0.3259 -0.2972 0.0031 -0.0248 110 PHE A N 652 C CA . PHE A 96 ? 0.5074 0.6624 0.3874 -0.3061 0.0036 -0.0253 110 PHE A CA 653 C C . PHE A 96 ? 0.5159 0.6926 0.4085 -0.3020 0.0009 -0.0224 110 PHE A C 654 O O . PHE A 96 ? 0.5234 0.7160 0.4145 -0.3084 0.0008 -0.0223 110 PHE A O 655 C CB . PHE A 96 ? 0.5077 0.6634 0.3791 -0.3131 0.0046 -0.0273 110 PHE A CB 656 C CG . PHE A 96 ? 0.5116 0.6473 0.3698 -0.3193 0.0080 -0.0308 110 PHE A CG 657 C CD1 . PHE A 96 ? 0.5466 0.6799 0.3936 -0.3300 0.0107 -0.0331 110 PHE A CD1 658 C CD2 . PHE A 96 ? 0.5257 0.6445 0.3835 -0.3143 0.0084 -0.0318 110 PHE A CD2 659 C CE1 . PHE A 96 ? 0.5606 0.6748 0.3965 -0.3356 0.0139 -0.0364 110 PHE A CE1 660 C CE2 . PHE A 96 ? 0.5581 0.6580 0.4049 -0.3196 0.0116 -0.0351 110 PHE A CE2 661 C CZ . PHE A 96 ? 0.5487 0.6461 0.3848 -0.3301 0.0144 -0.0373 110 PHE A CZ 662 N N . ARG A 97 ? 0.4254 0.6029 0.3308 -0.2914 -0.0011 -0.0202 111 ARG A N 663 C CA . ARG A 97 ? 0.4317 0.6287 0.3503 -0.2868 -0.0034 -0.0177 111 ARG A CA 664 C C . ARG A 97 ? 0.4417 0.6438 0.3603 -0.2897 -0.0021 -0.0180 111 ARG A C 665 O O . ARG A 97 ? 0.5051 0.6934 0.4160 -0.2922 0.0001 -0.0194 111 ARG A O 666 C CB . ARG A 97 ? 0.4529 0.6492 0.3861 -0.2743 -0.0061 -0.0155 111 ARG A CB 667 C CG . ARG A 97 ? 0.4415 0.6328 0.3758 -0.2707 -0.0075 -0.0150 111 ARG A CG 668 C CD . ARG A 97 ? 0.4412 0.6303 0.3900 -0.2584 -0.0100 -0.0130 111 ARG A CD 669 N NE . ARG A 97 ? 0.4415 0.6274 0.3924 -0.2546 -0.0116 -0.0122 111 ARG A NE 670 C CZ . ARG A 97 ? 0.4628 0.6344 0.4171 -0.2475 -0.0121 -0.0123 111 ARG A CZ 671 N NH1 . ARG A 97 ? 0.3497 0.5089 0.3056 -0.2432 -0.0113 -0.0130 111 ARG A NH1 672 N NH2 . ARG A 97 ? 0.4539 0.6242 0.4102 -0.2446 -0.0135 -0.0116 111 ARG A NH2 673 N N . GLY A 98 ? 0.4471 0.6692 0.3746 -0.2894 -0.0034 -0.0165 112 GLY A N 674 C CA . GLY A 98 ? 0.4079 0.6371 0.3379 -0.2909 -0.0022 -0.0167 112 GLY A CA 675 C C . GLY A 98 ? 0.4389 0.6678 0.3553 -0.3028 0.0005 -0.0187 112 GLY A C 676 O O . GLY A 98 ? 0.4944 0.7237 0.4012 -0.3106 0.0011 -0.0198 112 GLY A O 677 N N . TYR A 99 ? 0.4518 0.6803 0.3670 -0.3047 0.0021 -0.0193 113 TYR A N 678 C CA . TYR A 99 ? 0.5012 0.7311 0.4046 -0.3161 0.0046 -0.0210 113 TYR A CA 679 C C . TYR A 99 ? 0.5338 0.7479 0.4284 -0.3191 0.0070 -0.0221 113 TYR A C 680 O O . TYR A 99 ? 0.4724 0.6854 0.3566 -0.3287 0.0092 -0.0235 113 TYR A O 681 C CB . TYR A 99 ? 0.5064 0.7591 0.4172 -0.3186 0.0041 -0.0204 113 TYR A CB 682 C CG . TYR A 99 ? 0.4967 0.7608 0.4248 -0.3082 0.0022 -0.0186 113 TYR A CG 683 C CD1 . TYR A 99 ? 0.4762 0.7397 0.4083 -0.3054 0.0035 -0.0190 113 TYR A CD1 684 C CD2 . TYR A 99 ? 0.4875 0.7629 0.4280 -0.3014 -0.0007 -0.0167 113 TYR A CD2 685 C CE1 . TYR A 99 ? 0.5125 0.7861 0.4608 -0.2960 0.0020 -0.0180 113 TYR A CE1 686 C CE2 . TYR A 99 ? 0.5504 0.8355 0.5075 -0.2918 -0.0023 -0.0153 113 TYR A CE2 687 C CZ . TYR A 99 ? 0.5526 0.8367 0.5137 -0.2891 -0.0008 -0.0162 113 TYR A CZ 688 O OH . TYR A 99 ? 0.5456 0.8393 0.5236 -0.2797 -0.0021 -0.0153 113 TYR A OH 689 N N . GLU A 100 ? 0.5216 0.7230 0.4201 -0.3110 0.0066 -0.0214 114 GLU A N 690 C CA . GLU A 100 ? 0.5120 0.6984 0.4026 -0.3134 0.0087 -0.0219 114 GLU A CA 691 C C . GLU A 100 ? 0.5266 0.6942 0.4024 -0.3204 0.0104 -0.0233 114 GLU A C 692 O O . GLU A 100 ? 0.5421 0.7006 0.4085 -0.3269 0.0125 -0.0239 114 GLU A O 693 C CB . GLU A 100 ? 0.4673 0.6461 0.3665 -0.3029 0.0076 -0.0207 114 GLU A CB 694 C CG . GLU A 100 ? 0.5455 0.7417 0.4610 -0.2948 0.0059 -0.0196 114 GLU A CG 695 C CD . GLU A 100 ? 0.5599 0.7724 0.4773 -0.2996 0.0072 -0.0201 114 GLU A CD 696 O OE1 . GLU A 100 ? 0.5800 0.7895 0.4861 -0.3088 0.0095 -0.0210 114 GLU A OE1 697 O OE2 . GLU A 100 ? 0.5184 0.7472 0.4494 -0.2940 0.0060 -0.0197 114 GLU A OE2 698 N N . TRP A 101 ? 0.5081 0.6697 0.3822 -0.3193 0.0097 -0.0239 115 TRP A N 699 C CA . TRP A 101 ? 0.5305 0.6750 0.3912 -0.3263 0.0117 -0.0258 115 TRP A CA 700 C C . TRP A 101 ? 0.5707 0.7221 0.4217 -0.3386 0.0138 -0.0274 115 TRP A C 701 O O . TRP A 101 ? 0.5842 0.7238 0.4250 -0.3457 0.0161 -0.0284 115 TRP A O 702 C CB . TRP A 101 ? 0.5318 0.6725 0.3928 -0.3238 0.0108 -0.0265 115 TRP A CB 703 C CG . TRP A 101 ? 0.5219 0.6579 0.3933 -0.3119 0.0085 -0.0249 115 TRP A CG 704 C CD1 . TRP A 101 ? 0.5203 0.6685 0.4024 -0.3052 0.0059 -0.0237 115 TRP A CD1 705 C CD2 . TRP A 101 ? 0.5287 0.6465 0.4010 -0.3054 0.0085 -0.0243 115 TRP A CD2 706 N NE1 . TRP A 101 ? 0.4606 0.5992 0.3504 -0.2951 0.0044 -0.0225 115 TRP A NE1 707 C CE2 . TRP A 101 ? 0.4821 0.6022 0.3660 -0.2950 0.0059 -0.0229 115 TRP A CE2 708 C CE3 . TRP A 101 ? 0.5605 0.6604 0.4254 -0.3075 0.0103 -0.0246 115 TRP A CE3 709 C CZ2 . TRP A 101 ? 0.4566 0.5619 0.3447 -0.2867 0.0051 -0.0221 115 TRP A CZ2 710 C CZ3 . TRP A 101 ? 0.5198 0.6050 0.3888 -0.2991 0.0094 -0.0234 115 TRP A CZ3 711 C CH2 . TRP A 101 ? 0.4914 0.5795 0.3718 -0.2889 0.0069 -0.0223 115 TRP A CH2 712 N N . TRP A 102 ? 0.5018 0.6724 0.3565 -0.3412 0.0128 -0.0275 116 TRP A N 713 C CA . TRP A 102 ? 0.5612 0.7416 0.4084 -0.3524 0.0143 -0.0289 116 TRP A CA 714 C C . TRP A 102 ? 0.6057 0.7875 0.4505 -0.3566 0.0159 -0.0287 116 TRP A C 715 O O . TRP A 102 ? 0.5793 0.7546 0.4134 -0.3662 0.0182 -0.0301 116 TRP A O 716 C CB . TRP A 102 ? 0.5499 0.7532 0.4050 -0.3520 0.0123 -0.0281 116 TRP A CB 717 C CG . TRP A 102 ? 0.5856 0.8024 0.4356 -0.3625 0.0134 -0.0292 116 TRP A CG 718 C CD1 . TRP A 102 ? 0.5916 0.8078 0.4311 -0.3726 0.0147 -0.0314 116 TRP A CD1 719 C CD2 . TRP A 102 ? 0.6098 0.8435 0.4655 -0.3642 0.0132 -0.0283 116 TRP A CD2 720 N NE1 . TRP A 102 ? 0.5991 0.8307 0.4374 -0.3805 0.0153 -0.0317 116 TRP A NE1 721 C CE2 . TRP A 102 ? 0.5915 0.8341 0.4397 -0.3754 0.0144 -0.0298 116 TRP A CE2 722 C CE3 . TRP A 102 ? 0.5831 0.8253 0.4498 -0.3573 0.0124 -0.0266 116 TRP A CE3 723 C CZ2 . TRP A 102 ? 0.6145 0.8743 0.4661 -0.3799 0.0147 -0.0294 116 TRP A CZ2 724 C CZ3 . TRP A 102 ? 0.6124 0.8716 0.4823 -0.3617 0.0128 -0.0265 116 TRP A CZ3 725 C CH2 . TRP A 102 ? 0.5918 0.8596 0.4542 -0.3728 0.0139 -0.0278 116 TRP A CH2 726 N N . LEU A 103 ? 0.5854 0.7751 0.4404 -0.3495 0.0147 -0.0268 117 LEU A N 727 C CA . LEU A 103 ? 0.6221 0.8154 0.4755 -0.3535 0.0162 -0.0266 117 LEU A CA 728 C C . LEU A 103 ? 0.6027 0.7747 0.4455 -0.3571 0.0182 -0.0268 117 LEU A C 729 O O . LEU A 103 ? 0.6502 0.8210 0.4847 -0.3662 0.0203 -0.0275 117 LEU A O 730 C CB . LEU A 103 ? 0.5755 0.7811 0.4424 -0.3447 0.0148 -0.0250 117 LEU A CB 731 C CG . LEU A 103 ? 0.5744 0.7875 0.4414 -0.3483 0.0164 -0.0249 117 LEU A CG 732 C CD1 . LEU A 103 ? 0.5800 0.8100 0.4448 -0.3575 0.0173 -0.0259 117 LEU A CD1 733 C CD2 . LEU A 103 ? 0.5206 0.7432 0.4017 -0.3382 0.0151 -0.0238 117 LEU A CD2 734 N N . MET A 104 ? 0.5752 0.7305 0.4188 -0.3500 0.0176 -0.0261 118 MET A N 735 C CA . MET A 104 ? 0.5476 0.6817 0.3819 -0.3528 0.0193 -0.0259 118 MET A CA 736 C C . MET A 104 ? 0.5946 0.7193 0.4165 -0.3635 0.0214 -0.0278 118 MET A C 737 O O . MET A 104 ? 0.6072 0.7238 0.4208 -0.3708 0.0234 -0.0278 118 MET A O 738 C CB . MET A 104 ? 0.5215 0.6398 0.3596 -0.3430 0.0180 -0.0248 118 MET A CB 739 C CG . MET A 104 ? 0.5030 0.6282 0.3526 -0.3332 0.0162 -0.0229 118 MET A CG 740 S SD . MET A 104 ? 0.5377 0.6427 0.3907 -0.3228 0.0149 -0.0214 118 MET A SD 741 C CE . MET A 104 ? 0.5866 0.6969 0.4482 -0.3154 0.0127 -0.0221 118 MET A CE 742 N N . LYS A 105 ? 0.5920 0.7183 0.4127 -0.3648 0.0211 -0.0296 119 LYS A N 743 C CA . LYS A 105 ? 0.6146 0.7334 0.4239 -0.3753 0.0234 -0.0321 119 LYS A CA 744 C C . LYS A 105 ? 0.6196 0.7513 0.4242 -0.3859 0.0248 -0.0329 119 LYS A C 745 O O . LYS A 105 ? 0.6062 0.7279 0.4011 -0.3950 0.0271 -0.0342 119 LYS A O 746 C CB . LYS A 105 ? 0.6106 0.7306 0.4197 -0.3748 0.0229 -0.0340 119 LYS A CB 747 C CG . LYS A 105 ? 0.6501 0.7490 0.4571 -0.3702 0.0233 -0.0347 119 LYS A CG 748 C CD . LYS A 105 ? 0.6614 0.7645 0.4692 -0.3692 0.0226 -0.0365 119 LYS A CD 749 C CE . LYS A 105 ? 0.6380 0.7616 0.4571 -0.3623 0.0196 -0.0346 119 LYS A CE 750 N NZ . LYS A 105 ? 0.6503 0.7786 0.4708 -0.3608 0.0187 -0.0357 119 LYS A NZ 751 N N . GLU A 106 ? 0.5781 0.7318 0.3901 -0.3849 0.0235 -0.0322 120 GLU A N 752 C CA . GLU A 106 ? 0.6098 0.7767 0.4184 -0.3946 0.0247 -0.0328 120 GLU A CA 753 C C . GLU A 106 ? 0.6752 0.8353 0.4802 -0.3974 0.0262 -0.0316 120 GLU A C 754 O O . GLU A 106 ? 0.6635 0.8230 0.4607 -0.4077 0.0282 -0.0325 120 GLU A O 755 C CB . GLU A 106 ? 0.5849 0.7772 0.4037 -0.3919 0.0228 -0.0321 120 GLU A CB 756 C CG . GLU A 106 ? 0.6201 0.8220 0.4415 -0.3913 0.0213 -0.0330 120 GLU A CG 757 C CD . GLU A 106 ? 0.6823 0.8825 0.4928 -0.4029 0.0231 -0.0356 120 GLU A CD 758 O OE1 . GLU A 106 ? 0.7090 0.9102 0.5130 -0.4122 0.0250 -0.0365 120 GLU A OE1 759 O OE2 . GLU A 106 ? 0.7058 0.9041 0.5144 -0.4030 0.0226 -0.0368 120 GLU A OE2 760 N N . ALA A 107 ? 0.6680 0.8234 0.4789 -0.3887 0.0252 -0.0295 121 ALA A N 761 C CA . ALA A 107 ? 0.6525 0.8013 0.4603 -0.3907 0.0265 -0.0280 121 ALA A CA 762 C C . ALA A 107 ? 0.6842 0.8103 0.4807 -0.3968 0.0284 -0.0282 121 ALA A C 763 O O . ALA A 107 ? 0.6842 0.8075 0.4736 -0.4057 0.0303 -0.0280 121 ALA A O 764 C CB . ALA A 107 ? 0.5716 0.7191 0.3880 -0.3797 0.0249 -0.0259 121 ALA A CB 765 N N . LYS A 108 ? 0.6687 0.7784 0.4641 -0.3921 0.0279 -0.0285 122 LYS A N 766 C CA . LYS A 108 ? 0.7579 0.8447 0.5441 -0.3967 0.0297 -0.0288 122 LYS A CA 767 C C . LYS A 108 ? 0.8295 0.9155 0.6068 -0.4088 0.0320 -0.0313 122 LYS A C 768 O O . LYS A 108 ? 0.8647 0.9359 0.6343 -0.4157 0.0340 -0.0311 122 LYS A O 769 C CB . LYS A 108 ? 0.8039 0.8751 0.5921 -0.3886 0.0288 -0.0290 122 LYS A CB 770 C CG . LYS A 108 ? 0.8667 0.9129 0.6482 -0.3905 0.0303 -0.0283 122 LYS A CG 771 C CD . LYS A 108 ? 0.9089 0.9410 0.6922 -0.3836 0.0297 -0.0293 122 LYS A CD 772 C CE . LYS A 108 ? 0.9547 0.9624 0.7311 -0.3871 0.0317 -0.0293 122 LYS A CE 773 N NZ . LYS A 108 ? 0.9374 0.9323 0.7153 -0.3816 0.0316 -0.0311 122 LYS A NZ 774 N N . LYS A 109 ? 0.8041 0.9059 0.5827 -0.4117 0.0317 -0.0336 123 LYS A N 775 C CA . LYS A 109 ? 0.8348 0.9379 0.6053 -0.4236 0.0338 -0.0362 123 LYS A CA 776 C C . LYS A 109 ? 0.8369 0.9460 0.6035 -0.4325 0.0353 -0.0354 123 LYS A C 777 O O . LYS A 109 ? 0.8277 0.9291 0.5862 -0.4425 0.0376 -0.0368 123 LYS A O 778 C CB . LYS A 109 ? 0.8472 0.9685 0.6204 -0.4249 0.0328 -0.0384 123 LYS A CB 779 C CG . LYS A 109 ? 0.9250 1.0372 0.6962 -0.4232 0.0330 -0.0407 123 LYS A CG 780 C CD . LYS A 109 ? 1.0053 1.1355 0.7768 -0.4277 0.0325 -0.0428 123 LYS A CD 781 C CE . LYS A 109 ? 1.0387 1.1920 0.8204 -0.4218 0.0297 -0.0407 123 LYS A CE 782 N NZ . LYS A 109 ? 1.0811 1.2521 0.8640 -0.4253 0.0288 -0.0422 123 LYS A NZ 783 N N . ARG A 110 ? 0.7767 0.8997 0.5493 -0.4290 0.0341 -0.0333 124 ARG A N 784 C CA . ARG A 110 ? 0.7668 0.8981 0.5367 -0.4372 0.0355 -0.0325 124 ARG A CA 785 C C . ARG A 110 ? 0.7893 0.9040 0.5553 -0.4374 0.0365 -0.0299 124 ARG A C 786 O O . ARG A 110 ? 0.7843 0.8954 0.5441 -0.4465 0.0384 -0.0293 124 ARG A O 787 C CB . ARG A 110 ? 0.7466 0.9024 0.5254 -0.4336 0.0340 -0.0318 124 ARG A CB 788 C CG . ARG A 110 ? 0.7180 0.8922 0.4997 -0.4364 0.0333 -0.0340 124 ARG A CG 789 C CD . ARG A 110 ? 0.6724 0.8683 0.4659 -0.4291 0.0312 -0.0331 124 ARG A CD 790 N NE . ARG A 110 ? 0.6365 0.8502 0.4328 -0.4324 0.0304 -0.0347 124 ARG A NE 791 C CZ . ARG A 110 ? 0.6622 0.8765 0.4602 -0.4289 0.0290 -0.0356 124 ARG A CZ 792 N NH1 . ARG A 110 ? 0.6649 0.8630 0.4628 -0.4217 0.0283 -0.0353 124 ARG A NH1 793 N NH2 . ARG A 110 ? 0.6524 0.8840 0.4528 -0.4327 0.0282 -0.0366 124 ARG A NH2 794 N N . ASN A 111 ? 0.8025 0.9071 0.5726 -0.4273 0.0351 -0.0280 125 ASN A N 795 C CA . ASN A 111 ? 0.8007 0.8886 0.5675 -0.4266 0.0357 -0.0251 125 ASN A CA 796 C C . ASN A 111 ? 0.8195 0.8872 0.5871 -0.4185 0.0348 -0.0243 125 ASN A C 797 O O . ASN A 111 ? 0.8265 0.8962 0.6013 -0.4081 0.0328 -0.0232 125 ASN A O 798 C CB . ASN A 111 ? 0.7672 0.8675 0.5381 -0.4240 0.0350 -0.0228 125 ASN A CB 799 C CG . ASN A 111 ? 0.7994 0.8834 0.5653 -0.4237 0.0354 -0.0195 125 ASN A CG 800 O OD1 . ASN A 111 ? 0.8402 0.9040 0.6001 -0.4269 0.0364 -0.0185 125 ASN A OD1 801 N ND2 . ASN A 111 ? 0.8104 0.9035 0.5794 -0.4199 0.0345 -0.0177 125 ASN A ND2 802 N N . PRO A 112 ? 0.8381 0.8863 0.5988 -0.4234 0.0364 -0.0248 126 PRO A N 803 C CA . PRO A 112 ? 0.8398 0.8673 0.6007 -0.4170 0.0360 -0.0244 126 PRO A CA 804 C C . PRO A 112 ? 0.8221 0.8399 0.5860 -0.4094 0.0347 -0.0204 126 PRO A C 805 O O . PRO A 112 ? 0.8437 0.8508 0.6114 -0.4006 0.0334 -0.0199 126 PRO A O 806 C CB . PRO A 112 ? 0.8473 0.8578 0.6000 -0.4264 0.0387 -0.0254 126 PRO A CB 807 C CG . PRO A 112 ? 0.8668 0.8921 0.6156 -0.4370 0.0402 -0.0277 126 PRO A CG 808 C CD . PRO A 112 ? 0.8510 0.8958 0.6036 -0.4360 0.0390 -0.0258 126 PRO A CD 809 N N . ASP A 113 ? 0.8241 0.8460 0.5861 -0.4131 0.0351 -0.0177 127 ASP A N 810 C CA . ASP A 113 ? 0.8304 0.8439 0.5924 -0.4083 0.0340 -0.0139 127 ASP A CA 811 C C . ASP A 113 ? 0.7416 0.7721 0.5103 -0.4008 0.0319 -0.0134 127 ASP A C 812 O O . ASP A 113 ? 0.6587 0.6855 0.4271 -0.3975 0.0310 -0.0105 127 ASP A O 813 C CB . ASP A 113 ? 0.8959 0.9034 0.6497 -0.4178 0.0356 -0.0108 127 ASP A CB 814 C CG . ASP A 113 ? 0.9885 0.9752 0.7369 -0.4239 0.0376 -0.0103 127 ASP A CG 815 O OD1 . ASP A 113 ? 1.0041 0.9711 0.7528 -0.4193 0.0372 -0.0079 127 ASP A OD1 816 O OD2 . ASP A 113 ? 1.0547 1.0448 0.7991 -0.4333 0.0396 -0.0121 127 ASP A OD2 817 N N . ILE A 114 ? 0.7025 0.7514 0.4776 -0.3981 0.0312 -0.0162 128 ILE A N 818 C CA . ILE A 114 ? 0.6885 0.7537 0.4717 -0.3904 0.0294 -0.0159 128 ILE A CA 819 C C . ILE A 114 ? 0.6607 0.7141 0.4488 -0.3794 0.0274 -0.0143 128 ILE A C 820 O O . ILE A 114 ? 0.6402 0.6779 0.4288 -0.3754 0.0271 -0.0146 128 ILE A O 821 C CB . ILE A 114 ? 0.6702 0.7563 0.4613 -0.3881 0.0287 -0.0188 128 ILE A CB 822 C CG1 . ILE A 114 ? 0.6601 0.7642 0.4599 -0.3818 0.0274 -0.0184 128 ILE A CG1 823 C CG2 . ILE A 114 ? 0.6104 0.6897 0.4058 -0.3819 0.0277 -0.0205 128 ILE A CG2 824 C CD1 . ILE A 114 ? 0.6466 0.7743 0.4537 -0.3820 0.0272 -0.0205 128 ILE A CD1 825 N N . ILE A 115 ? 0.6466 0.7076 0.4385 -0.3747 0.0264 -0.0127 129 ILE A N 826 C CA . ILE A 115 ? 0.6390 0.6904 0.4360 -0.3644 0.0244 -0.0111 129 ILE A CA 827 C C . ILE A 115 ? 0.6168 0.6820 0.4262 -0.3546 0.0226 -0.0130 129 ILE A C 828 O O . ILE A 115 ? 0.6285 0.7141 0.4434 -0.3543 0.0225 -0.0142 129 ILE A O 829 C CB . ILE A 115 ? 0.5858 0.6371 0.3797 -0.3649 0.0241 -0.0083 129 ILE A CB 830 C CG1 . ILE A 115 ? 0.6088 0.6460 0.3909 -0.3746 0.0257 -0.0057 129 ILE A CG1 831 C CG2 . ILE A 115 ? 0.5721 0.6142 0.3716 -0.3543 0.0220 -0.0067 129 ILE A CG2 832 C CD1 . ILE A 115 ? 0.6438 0.6844 0.4211 -0.3779 0.0258 -0.0028 129 ILE A CD1 833 N N . LEU A 116 ? 0.5529 0.6073 0.3673 -0.3465 0.0212 -0.0133 130 LEU A N 834 C CA . LEU A 116 ? 0.5773 0.6432 0.4036 -0.3373 0.0194 -0.0148 130 LEU A CA 835 C C . LEU A 116 ? 0.5646 0.6279 0.3990 -0.3266 0.0173 -0.0133 130 LEU A C 836 O O . LEU A 116 ? 0.5733 0.6183 0.4053 -0.3231 0.0166 -0.0115 130 LEU A O 837 C CB . LEU A 116 ? 0.5983 0.6576 0.4258 -0.3357 0.0192 -0.0166 130 LEU A CB 838 C CG . LEU A 116 ? 0.5866 0.6499 0.4062 -0.3463 0.0211 -0.0188 130 LEU A CG 839 C CD1 . LEU A 116 ? 0.5553 0.6118 0.3739 -0.3455 0.0210 -0.0209 130 LEU A CD1 840 C CD2 . LEU A 116 ? 0.5490 0.6363 0.3723 -0.3497 0.0213 -0.0198 130 LEU A CD2 841 N N . MET A 117 ? 0.5029 0.5845 0.3477 -0.3211 0.0163 -0.0140 131 MET A N 842 C CA . MET A 117 ? 0.4823 0.5637 0.3362 -0.3110 0.0144 -0.0130 131 MET A CA 843 C C . MET A 117 ? 0.4628 0.5560 0.3308 -0.3019 0.0126 -0.0143 131 MET A C 844 O O . MET A 117 ? 0.5168 0.6267 0.3892 -0.3038 0.0129 -0.0158 131 MET A O 845 C CB . MET A 117 ? 0.4808 0.5739 0.3350 -0.3128 0.0149 -0.0124 131 MET A CB 846 C CG . MET A 117 ? 0.5149 0.6021 0.3556 -0.3232 0.0168 -0.0111 131 MET A CG 847 S SD . MET A 117 ? 0.5662 0.6696 0.4077 -0.3253 0.0177 -0.0109 131 MET A SD 848 C CE . MET A 117 ? 0.5185 0.6154 0.3689 -0.3132 0.0152 -0.0098 131 MET A CE 849 N N . GLY A 118 ? 0.4498 0.5346 0.3253 -0.2921 0.0106 -0.0136 132 GLY A N 850 C CA . GLY A 118 ? 0.4612 0.5560 0.3512 -0.2825 0.0085 -0.0144 132 GLY A CA 851 C C . GLY A 118 ? 0.4564 0.5549 0.3568 -0.2737 0.0070 -0.0137 132 GLY A C 852 O O . GLY A 118 ? 0.4466 0.5323 0.3427 -0.2727 0.0067 -0.0123 132 GLY A O 853 N N . LEU A 119 ? 0.4158 0.5316 0.3301 -0.2676 0.0059 -0.0147 133 LEU A N 854 C CA . LEU A 119 ? 0.3830 0.5031 0.3090 -0.2587 0.0043 -0.0145 133 LEU A CA 855 C C . LEU A 119 ? 0.3645 0.4967 0.3076 -0.2493 0.0022 -0.0153 133 LEU A C 856 O O . LEU A 119 ? 0.4469 0.5946 0.3942 -0.2513 0.0025 -0.0162 133 LEU A O 857 C CB . LEU A 119 ? 0.3863 0.5182 0.3106 -0.2630 0.0060 -0.0151 133 LEU A CB 858 C CG . LEU A 119 ? 0.4717 0.6129 0.4084 -0.2554 0.0051 -0.0159 133 LEU A CG 859 C CD1 . LEU A 119 ? 0.3841 0.5090 0.3199 -0.2502 0.0036 -0.0146 133 LEU A CD1 860 C CD2 . LEU A 119 ? 0.5091 0.6650 0.4427 -0.2618 0.0075 -0.0172 133 LEU A CD2 861 N N . PRO A 120 ? 0.3663 0.4919 0.3191 -0.2394 -0.0001 -0.0148 134 PRO A N 862 C CA . PRO A 120 ? 0.3673 0.5052 0.3360 -0.2313 -0.0021 -0.0153 134 PRO A CA 863 C C . PRO A 120 ? 0.3936 0.5480 0.3756 -0.2266 -0.0023 -0.0165 134 PRO A C 864 O O . PRO A 120 ? 0.3823 0.5349 0.3635 -0.2261 -0.0017 -0.0169 134 PRO A O 865 C CB . PRO A 120 ? 0.3785 0.5019 0.3521 -0.2230 -0.0045 -0.0145 134 PRO A CB 866 C CG . PRO A 120 ? 0.3377 0.4410 0.2975 -0.2271 -0.0035 -0.0135 134 PRO A CG 867 C CD . PRO A 120 ? 0.3512 0.4574 0.3000 -0.2361 -0.0010 -0.0136 134 PRO A CD 868 N N . TRP A 121 ? 0.3751 0.5462 0.3678 -0.2243 -0.0030 -0.0171 135 TRP A N 869 C CA . TRP A 121 ? 0.3039 0.4913 0.3123 -0.2183 -0.0035 -0.0184 135 TRP A CA 870 C C . TRP A 121 ? 0.3337 0.5211 0.3575 -0.2074 -0.0066 -0.0179 135 TRP A C 871 O O . TRP A 121 ? 0.3573 0.5460 0.3926 -0.1997 -0.0078 -0.0188 135 TRP A O 872 C CB . TRP A 121 ? 0.3126 0.5192 0.3234 -0.2232 -0.0023 -0.0191 135 TRP A CB 873 C CG . TRP A 121 ? 0.3179 0.5336 0.3226 -0.2307 0.0007 -0.0205 135 TRP A CG 874 C CD1 . TRP A 121 ? 0.3131 0.5458 0.3283 -0.2290 0.0016 -0.0223 135 TRP A CD1 875 C CD2 . TRP A 121 ? 0.3799 0.5884 0.3669 -0.2413 0.0031 -0.0202 135 TRP A CD2 876 N NE1 . TRP A 121 ? 0.3902 0.6272 0.3951 -0.2379 0.0046 -0.0232 135 TRP A NE1 877 C CE2 . TRP A 121 ? 0.3398 0.5625 0.3265 -0.2461 0.0055 -0.0219 135 TRP A CE2 878 C CE3 . TRP A 121 ? 0.3474 0.5390 0.3185 -0.2475 0.0036 -0.0189 135 TRP A CE3 879 C CZ2 . TRP A 121 ? 0.4518 0.6730 0.4220 -0.2577 0.0083 -0.0221 135 TRP A CZ2 880 C CZ3 . TRP A 121 ? 0.3648 0.5540 0.3203 -0.2585 0.0062 -0.0191 135 TRP A CZ3 881 C CH2 . TRP A 121 ? 0.3699 0.5739 0.3247 -0.2637 0.0084 -0.0205 135 TRP A CH2 882 N N . SER A 122 ? 0.3029 0.4889 0.3268 -0.2068 -0.0081 -0.0167 136 SER A N 883 C CA . SER A 122 ? 0.2729 0.4585 0.3107 -0.1971 -0.0111 -0.0159 136 SER A CA 884 C C . SER A 122 ? 0.3135 0.4825 0.3430 -0.1973 -0.0121 -0.0146 136 SER A C 885 O O . SER A 122 ? 0.3620 0.5212 0.3757 -0.2051 -0.0104 -0.0144 136 SER A O 886 C CB . SER A 122 ? 0.2806 0.4842 0.3296 -0.1954 -0.0122 -0.0154 136 SER A CB 887 O OG . SER A 122 ? 0.3591 0.5642 0.3981 -0.2026 -0.0117 -0.0143 136 SER A OG 888 N N . PHE A 123 ? 0.2748 0.4402 0.3148 -0.1888 -0.0147 -0.0138 137 PHE A N 889 C CA . PHE A 123 ? 0.2781 0.4287 0.3116 -0.1883 -0.0156 -0.0128 137 PHE A CA 890 C C . PHE A 123 ? 0.3419 0.5000 0.3869 -0.1827 -0.0180 -0.0116 137 PHE A C 891 O O . PHE A 123 ? 0.2743 0.4446 0.3349 -0.1762 -0.0196 -0.0115 137 PHE A O 892 C CB . PHE A 123 ? 0.2698 0.4037 0.3042 -0.1826 -0.0165 -0.0130 137 PHE A CB 893 C CG . PHE A 123 ? 0.3630 0.4880 0.3864 -0.1875 -0.0145 -0.0136 137 PHE A CG 894 C CD1 . PHE A 123 ? 0.3501 0.4604 0.3570 -0.1945 -0.0128 -0.0132 137 PHE A CD1 895 C CD2 . PHE A 123 ? 0.3772 0.5081 0.4068 -0.1851 -0.0143 -0.0146 137 PHE A CD2 896 C CE1 . PHE A 123 ? 0.3218 0.4232 0.3186 -0.1990 -0.0111 -0.0132 137 PHE A CE1 897 C CE2 . PHE A 123 ? 0.3724 0.4954 0.3914 -0.1899 -0.0125 -0.0149 137 PHE A CE2 898 C CZ . PHE A 123 ? 0.3798 0.4878 0.3823 -0.1969 -0.0110 -0.0139 137 PHE A CZ 899 N N . PRO A 124 ? 0.3461 0.4969 0.3839 -0.1849 -0.0184 -0.0107 138 PRO A N 900 C CA . PRO A 124 ? 0.3031 0.4598 0.3515 -0.1793 -0.0208 -0.0093 138 PRO A CA 901 C C . PRO A 124 ? 0.3135 0.4645 0.3760 -0.1683 -0.0232 -0.0092 138 PRO A C 902 O O . PRO A 124 ? 0.3071 0.4437 0.3668 -0.1659 -0.0230 -0.0101 138 PRO A O 903 C CB . PRO A 124 ? 0.3096 0.4564 0.3448 -0.1847 -0.0202 -0.0090 138 PRO A CB 904 C CG . PRO A 124 ? 0.3568 0.4993 0.3753 -0.1950 -0.0172 -0.0102 138 PRO A CG 905 C CD . PRO A 124 ? 0.3192 0.4572 0.3390 -0.1933 -0.0164 -0.0111 138 PRO A CD 906 N N . GLY A 125 ? 0.2858 0.4477 0.3636 -0.1615 -0.0254 -0.0081 139 GLY A N 907 C CA . GLY A 125 ? 0.3156 0.4739 0.4085 -0.1509 -0.0276 -0.0083 139 GLY A CA 908 C C . GLY A 125 ? 0.3108 0.4521 0.4007 -0.1475 -0.0284 -0.0083 139 GLY A C 909 O O . GLY A 125 ? 0.2930 0.4266 0.3909 -0.1404 -0.0295 -0.0093 139 GLY A O 910 N N . TRP A 126 ? 0.2877 0.4230 0.3663 -0.1525 -0.0278 -0.0075 140 TRP A N 911 C CA . TRP A 126 ? 0.3176 0.4378 0.3947 -0.1488 -0.0285 -0.0076 140 TRP A CA 912 C C . TRP A 126 ? 0.3682 0.4717 0.4385 -0.1487 -0.0274 -0.0091 140 TRP A C 913 O O . TRP A 126 ? 0.3519 0.4435 0.4258 -0.1429 -0.0284 -0.0095 140 TRP A O 914 C CB . TRP A 126 ? 0.3287 0.4466 0.3949 -0.1547 -0.0278 -0.0068 140 TRP A CB 915 C CG . TRP A 126 ? 0.3774 0.4904 0.4252 -0.1654 -0.0250 -0.0077 140 TRP A CG 916 C CD1 . TRP A 126 ? 0.3863 0.5108 0.4269 -0.1735 -0.0237 -0.0076 140 TRP A CD1 917 C CD2 . TRP A 126 ? 0.3904 0.4853 0.4249 -0.1692 -0.0232 -0.0090 140 TRP A CD2 918 N NE1 . TRP A 126 ? 0.3997 0.5143 0.4233 -0.1822 -0.0210 -0.0089 140 TRP A NE1 919 C CE2 . TRP A 126 ? 0.4318 0.5280 0.4515 -0.1797 -0.0207 -0.0098 140 TRP A CE2 920 C CE3 . TRP A 126 ? 0.3701 0.4479 0.4043 -0.1646 -0.0234 -0.0096 140 TRP A CE3 921 C CZ2 . TRP A 126 ? 0.4591 0.5395 0.4639 -0.1856 -0.0183 -0.0111 140 TRP A CZ2 922 C CZ3 . TRP A 126 ? 0.4524 0.5148 0.4720 -0.1703 -0.0211 -0.0108 140 TRP A CZ3 923 C CH2 . TRP A 126 ? 0.4539 0.5174 0.4591 -0.1806 -0.0186 -0.0115 140 TRP A CH2 924 N N . LEU A 127 ? 0.3491 0.4522 0.4099 -0.1550 -0.0255 -0.0098 141 LEU A N 925 C CA . LEU A 127 ? 0.4199 0.5081 0.4739 -0.1553 -0.0245 -0.0108 141 LEU A CA 926 C C . LEU A 127 ? 0.3705 0.4577 0.4383 -0.1461 -0.0264 -0.0115 141 LEU A C 927 O O . LEU A 127 ? 0.4212 0.4949 0.4860 -0.1443 -0.0264 -0.0121 141 LEU A O 928 C CB . LEU A 127 ? 0.4074 0.4974 0.4491 -0.1640 -0.0220 -0.0112 141 LEU A CB 929 C CG . LEU A 127 ? 0.4640 0.5523 0.4892 -0.1746 -0.0195 -0.0112 141 LEU A CG 930 C CD1 . LEU A 127 ? 0.4564 0.5459 0.4717 -0.1820 -0.0172 -0.0117 141 LEU A CD1 931 C CD2 . LEU A 127 ? 0.4495 0.5200 0.4649 -0.1761 -0.0189 -0.0112 141 LEU A CD2 932 N N . GLY A 128 ? 0.3168 0.4184 0.3998 -0.1407 -0.0280 -0.0116 142 GLY A N 933 C CA . GLY A 128 ? 0.3482 0.4510 0.4449 -0.1326 -0.0297 -0.0130 142 GLY A CA 934 C C . GLY A 128 ? 0.3770 0.4734 0.4852 -0.1234 -0.0318 -0.0135 142 GLY A C 935 O O . GLY A 128 ? 0.3966 0.4913 0.5155 -0.1163 -0.0331 -0.0153 142 GLY A O 936 N N . LYS A 129 ? 0.3870 0.4803 0.4925 -0.1238 -0.0318 -0.0124 143 LYS A N 937 C CA . LYS A 129 ? 0.4868 0.5734 0.6007 -0.1162 -0.0330 -0.0132 143 LYS A CA 938 C C . LYS A 129 ? 0.5329 0.6286 0.6656 -0.1067 -0.0344 -0.0154 143 LYS A C 939 O O . LYS A 129 ? 0.5606 0.6498 0.6990 -0.1002 -0.0340 -0.0186 143 LYS A O 940 C CB . LYS A 129 ? 0.5239 0.5918 0.6301 -0.1154 -0.0322 -0.0142 143 LYS A CB 941 C CG . LYS A 129 ? 0.6005 0.6570 0.6896 -0.1231 -0.0306 -0.0127 143 LYS A CG 942 C CD . LYS A 129 ? 0.6860 0.7458 0.7750 -0.1239 -0.0308 -0.0116 143 LYS A CD 943 C CE . LYS A 129 ? 0.7577 0.8072 0.8295 -0.1320 -0.0289 -0.0109 143 LYS A CE 944 N NZ . LYS A 129 ? 0.7593 0.8142 0.8293 -0.1345 -0.0290 -0.0099 143 LYS A NZ 945 N N . GLY A 130 ? 0.5312 0.6425 0.6724 -0.1064 -0.0352 -0.0146 144 GLY A N 946 C CA . GLY A 130 ? 0.5610 0.6812 0.7198 -0.0976 -0.0361 -0.0174 144 GLY A CA 947 C C . GLY A 130 ? 0.6222 0.7498 0.7884 -0.0967 -0.0368 -0.0183 144 GLY A C 948 O O . GLY A 130 ? 0.6542 0.7910 0.8331 -0.0899 -0.0372 -0.0199 144 GLY A O 949 N N . PHE A 131 ? 0.6167 0.7397 0.7716 -0.1029 -0.0361 -0.0173 145 PHE A N 950 C CA . PHE A 131 ? 0.6016 0.7326 0.7610 -0.1034 -0.0363 -0.0178 145 PHE A CA 951 C C . PHE A 131 ? 0.5729 0.7115 0.7197 -0.1133 -0.0341 -0.0162 145 PHE A C 952 O O . PHE A 131 ? 0.5671 0.7008 0.6990 -0.1205 -0.0325 -0.0148 145 PHE A O 953 C CB . PHE A 131 ? 0.6608 0.7811 0.8185 -0.1013 -0.0369 -0.0198 145 PHE A CB 954 C CG . PHE A 131 ? 0.7172 0.8279 0.8802 -0.0916 -0.0370 -0.0227 145 PHE A CG 955 C CD1 . PHE A 131 ? 0.7433 0.8588 0.9164 -0.0813 -0.0365 -0.0258 145 PHE A CD1 956 C CD2 . PHE A 131 ? 0.7438 0.8411 0.8967 -0.0926 -0.0354 -0.0239 145 PHE A CD2 957 C CE1 . PHE A 131 ? 0.7584 0.8790 0.9139 -0.0790 -0.0286 -0.0350 145 PHE A CE1 958 C CE2 . PHE A 131 ? 0.7683 0.8615 0.9166 -0.0857 -0.0315 -0.0292 145 PHE A CE2 959 C CZ . PHE A 131 ? 0.7718 0.8800 0.9140 -0.0826 -0.0284 -0.0321 145 PHE A CZ 960 N N . SER A 132 ? 0.5505 0.7014 0.7032 -0.1138 -0.0337 -0.0168 146 SER A N 961 C CA . SER A 132 ? 0.5296 0.6885 0.6706 -0.1231 -0.0309 -0.0165 146 SER A CA 962 C C . SER A 132 ? 0.4827 0.6327 0.6112 -0.1278 -0.0293 -0.0178 146 SER A C 963 O O . SER A 132 ? 0.5085 0.6663 0.6376 -0.1297 -0.0281 -0.0193 146 SER A O 964 C CB . SER A 132 ? 0.5385 0.7156 0.6917 -0.1217 -0.0307 -0.0170 146 SER A CB 965 O OG . SER A 132 ? 0.5573 0.7435 0.7000 -0.1307 -0.0278 -0.0172 146 SER A OG 966 N N . TRP A 133 ? 0.4188 0.5526 0.5358 -0.1298 -0.0292 -0.0173 147 TRP A N 967 C CA . TRP A 133 ? 0.4107 0.5339 0.5164 -0.1335 -0.0281 -0.0181 147 TRP A CA 968 C C . TRP A 133 ? 0.4061 0.5139 0.4946 -0.1396 -0.0267 -0.0167 147 TRP A C 969 O O . TRP A 133 ? 0.4480 0.5458 0.5374 -0.1360 -0.0280 -0.0159 147 TRP A O 970 C CB . TRP A 133 ? 0.3861 0.5026 0.5024 -0.1249 -0.0307 -0.0196 147 TRP A CB 971 C CG . TRP A 133 ? 0.3827 0.4923 0.4909 -0.1276 -0.0301 -0.0206 147 TRP A CG 972 C CD1 . TRP A 133 ? 0.4149 0.5083 0.5177 -0.1260 -0.0310 -0.0207 147 TRP A CD1 973 C CD2 . TRP A 133 ? 0.3532 0.4724 0.4583 -0.1321 -0.0283 -0.0218 147 TRP A CD2 974 N NE1 . TRP A 133 ? 0.4310 0.5238 0.5258 -0.1305 -0.0301 -0.0215 147 TRP A NE1 975 C CE2 . TRP A 133 ? 0.3804 0.4894 0.4760 -0.1346 -0.0283 -0.0224 147 TRP A CE2 976 C CE3 . TRP A 133 ? 0.3458 0.4822 0.4540 -0.1352 -0.0264 -0.0227 147 TRP A CE3 977 C CZ2 . TRP A 133 ? 0.3528 0.4691 0.4407 -0.1410 -0.0263 -0.0238 147 TRP A CZ2 978 C CZ3 . TRP A 133 ? 0.3309 0.4739 0.4332 -0.1403 -0.0243 -0.0244 147 TRP A CZ3 979 C CH2 . TRP A 133 ? 0.3745 0.5082 0.4660 -0.1438 -0.0241 -0.0250 147 TRP A CH2 980 N N . PRO A 134 ? 0.3806 0.4860 0.4536 -0.1486 -0.0240 -0.0163 148 PRO A N 981 C CA . PRO A 134 ? 0.3774 0.4690 0.4331 -0.1557 -0.0224 -0.0148 148 PRO A CA 982 C C . PRO A 134 ? 0.3735 0.4461 0.4232 -0.1539 -0.0230 -0.0144 148 PRO A C 983 O O . PRO A 134 ? 0.3758 0.4347 0.4127 -0.1583 -0.0218 -0.0132 148 PRO A O 984 C CB . PRO A 134 ? 0.3584 0.4568 0.4021 -0.1656 -0.0194 -0.0149 148 PRO A CB 985 C CG . PRO A 134 ? 0.3509 0.4593 0.4026 -0.1633 -0.0194 -0.0165 148 PRO A CG 986 C CD . PRO A 134 ? 0.3655 0.4825 0.4370 -0.1530 -0.0222 -0.0175 148 PRO A CD 987 N N . TYR A 135 ? 0.3132 0.3850 0.3724 -0.1474 -0.0248 -0.0156 149 TYR A N 988 C CA . TYR A 135 ? 0.3903 0.4448 0.4440 -0.1457 -0.0255 -0.0152 149 TYR A CA 989 C C . TYR A 135 ? 0.4378 0.4849 0.5031 -0.1359 -0.0281 -0.0159 149 TYR A C 990 O O . TYR A 135 ? 0.4773 0.5133 0.5431 -0.1320 -0.0292 -0.0163 149 TYR A O 991 C CB . TYR A 135 ? 0.3830 0.4404 0.4326 -0.1489 -0.0253 -0.0158 149 TYR A CB 992 C CG . TYR A 135 ? 0.3595 0.4251 0.3960 -0.1598 -0.0222 -0.0154 149 TYR A CG 993 C CD1 . TYR A 135 ? 0.3050 0.3628 0.3256 -0.1683 -0.0198 -0.0135 149 TYR A CD1 994 C CD2 . TYR A 135 ? 0.3784 0.4596 0.4187 -0.1616 -0.0215 -0.0172 149 TYR A CD2 995 C CE1 . TYR A 135 ? 0.3526 0.4178 0.3612 -0.1785 -0.0168 -0.0132 149 TYR A CE1 996 C CE2 . TYR A 135 ? 0.3634 0.4528 0.3919 -0.1717 -0.0182 -0.0171 149 TYR A CE2 997 C CZ . TYR A 135 ? 0.3454 0.4267 0.3581 -0.1801 -0.0160 -0.0150 149 TYR A CZ 998 O OH . TYR A 135 ? 0.4043 0.4937 0.4055 -0.1902 -0.0129 -0.0150 149 TYR A OH 999 N N . VAL A 136 ? 0.4558 0.5095 0.5303 -0.1321 -0.0289 -0.0161 150 VAL A N 1000 C CA . VAL A 136 ? 0.4690 0.5165 0.5544 -0.1232 -0.0308 -0.0171 150 VAL A CA 1001 C C . VAL A 136 ? 0.4283 0.4574 0.5022 -0.1248 -0.0297 -0.0157 150 VAL A C 1002 O O . VAL A 136 ? 0.4230 0.4410 0.4994 -0.1193 -0.0301 -0.0166 150 VAL A O 1003 C CB . VAL A 136 ? 0.4666 0.5265 0.5647 -0.1190 -0.0317 -0.0175 150 VAL A CB 1004 C CG1 . VAL A 136 ? 0.5122 0.5652 0.6190 -0.1109 -0.0325 -0.0190 150 VAL A CG1 1005 C CG2 . VAL A 136 ? 0.4120 0.4885 0.5235 -0.1157 -0.0330 -0.0188 150 VAL A CG2 1006 N N . ASN A 137 ? 0.4106 0.4369 0.4718 -0.1324 -0.0279 -0.0139 151 ASN A N 1007 C CA . ASN A 137 ? 0.4065 0.4154 0.4559 -0.1347 -0.0267 -0.0127 151 ASN A CA 1008 C C . ASN A 137 ? 0.3740 0.3788 0.4067 -0.1447 -0.0244 -0.0114 151 ASN A C 1009 O O . ASN A 137 ? 0.3389 0.3507 0.3650 -0.1515 -0.0229 -0.0111 151 ASN A O 1010 C CB . ASN A 137 ? 0.4977 0.5071 0.5487 -0.1340 -0.0265 -0.0125 151 ASN A CB 1011 C CG . ASN A 137 ? 0.4836 0.4752 0.5237 -0.1358 -0.0252 -0.0117 151 ASN A CG 1012 O OD1 . ASN A 137 ? 0.4752 0.4558 0.5028 -0.1410 -0.0237 -0.0108 151 ASN A OD1 1013 N ND2 . ASN A 137 ? 0.4623 0.4515 0.5075 -0.1317 -0.0255 -0.0122 151 ASN A ND2 1014 N N . LEU A 138 ? 0.4040 0.3980 0.4300 -0.1458 -0.0241 -0.0106 152 LEU A N 1015 C CA . LEU A 138 ? 0.4390 0.4289 0.4499 -0.1550 -0.0220 -0.0093 152 LEU A CA 1016 C C . LEU A 138 ? 0.4040 0.3849 0.4023 -0.1614 -0.0199 -0.0085 152 LEU A C 1017 O O . LEU A 138 ? 0.3836 0.3693 0.3723 -0.1699 -0.0179 -0.0084 152 LEU A O 1018 C CB . LEU A 138 ? 0.3936 0.3712 0.3998 -0.1541 -0.0224 -0.0081 152 LEU A CB 1019 C CG . LEU A 138 ? 0.4562 0.4422 0.4716 -0.1499 -0.0243 -0.0092 152 LEU A CG 1020 C CD1 . LEU A 138 ? 0.4671 0.4401 0.4732 -0.1516 -0.0249 -0.0073 152 LEU A CD1 1021 C CD2 . LEU A 138 ? 0.4619 0.4670 0.4784 -0.1551 -0.0236 -0.0102 152 LEU A CD2 1022 N N . GLN A 139 ? 0.4157 0.3836 0.4142 -0.1574 -0.0202 -0.0083 153 GLN A N 1023 C CA . GLN A 139 ? 0.4483 0.4071 0.4355 -0.1633 -0.0181 -0.0082 153 GLN A CA 1024 C C . GLN A 139 ? 0.4134 0.3855 0.4005 -0.1676 -0.0173 -0.0094 153 GLN A C 1025 O O . GLN A 139 ? 0.4227 0.3939 0.3982 -0.1761 -0.0151 -0.0096 153 GLN A O 1026 C CB . GLN A 139 ? 0.5275 0.4706 0.5162 -0.1576 -0.0185 -0.0080 153 GLN A CB 1027 C CG . GLN A 139 ? 0.6559 0.5886 0.6326 -0.1641 -0.0161 -0.0083 153 GLN A CG 1028 C CD . GLN A 139 ? 0.7147 0.6337 0.6936 -0.1587 -0.0161 -0.0087 153 GLN A CD 1029 O OE1 . GLN A 139 ? 0.7180 0.6359 0.7078 -0.1499 -0.0178 -0.0087 153 GLN A OE1 1030 N NE2 . GLN A 139 ? 0.7149 0.6233 0.6836 -0.1642 -0.0138 -0.0092 153 GLN A NE2 1031 N N . LEU A 140 ? 0.3785 0.3632 0.3786 -0.1619 -0.0191 -0.0101 154 LEU A N 1032 C CA . LEU A 140 ? 0.3814 0.3799 0.3822 -0.1655 -0.0186 -0.0108 154 LEU A CA 1033 C C . LEU A 140 ? 0.3372 0.3482 0.3320 -0.1735 -0.0172 -0.0109 154 LEU A C 1034 O O . LEU A 140 ? 0.3662 0.3813 0.3524 -0.1810 -0.0154 -0.0113 154 LEU A O 1035 C CB . LEU A 140 ? 0.3826 0.3926 0.3999 -0.1573 -0.0211 -0.0111 154 LEU A CB 1036 C CG . LEU A 140 ? 0.3994 0.4247 0.4188 -0.1603 -0.0211 -0.0113 154 LEU A CG 1037 C CD1 . LEU A 140 ? 0.4495 0.4679 0.4582 -0.1657 -0.0195 -0.0117 154 LEU A CD1 1038 C CD2 . LEU A 140 ? 0.3713 0.4068 0.4080 -0.1515 -0.0237 -0.0112 154 LEU A CD2 1039 N N . THR A 141 ? 0.3128 0.3305 0.3124 -0.1720 -0.0178 -0.0107 155 THR A N 1040 C CA . THR A 141 ? 0.3926 0.4227 0.3869 -0.1794 -0.0162 -0.0108 155 THR A CA 1041 C C . THR A 141 ? 0.4096 0.4290 0.3867 -0.1888 -0.0135 -0.0104 155 THR A C 1042 O O . THR A 141 ? 0.4298 0.4567 0.3990 -0.1969 -0.0116 -0.0108 155 THR A O 1043 C CB . THR A 141 ? 0.4094 0.4489 0.4126 -0.1757 -0.0172 -0.0110 155 THR A CB 1044 O OG1 . THR A 141 ? 0.3673 0.4181 0.3874 -0.1673 -0.0195 -0.0117 155 THR A OG1 1045 C CG2 . THR A 141 ? 0.3341 0.3855 0.3308 -0.1839 -0.0150 -0.0113 155 THR A CG2 1046 N N . ALA A 142 ? 0.4108 0.4128 0.3824 -0.1877 -0.0134 -0.0095 156 ALA A N 1047 C CA . ALA A 142 ? 0.4450 0.4357 0.4009 -0.1964 -0.0110 -0.0088 156 ALA A CA 1048 C C . ALA A 142 ? 0.4497 0.4358 0.3980 -0.2013 -0.0094 -0.0099 156 ALA A C 1049 O O . ALA A 142 ? 0.4663 0.4520 0.4033 -0.2104 -0.0071 -0.0103 156 ALA A O 1050 C CB . ALA A 142 ? 0.4042 0.3767 0.3566 -0.1937 -0.0115 -0.0072 156 ALA A CB 1051 N N . TYR A 143 ? 0.4360 0.4190 0.3908 -0.1955 -0.0106 -0.0105 157 TYR A N 1052 C CA . TYR A 143 ? 0.4280 0.4075 0.3765 -0.1997 -0.0092 -0.0119 157 TYR A CA 1053 C C . TYR A 143 ? 0.4063 0.4028 0.3523 -0.2064 -0.0081 -0.0129 157 TYR A C 1054 O O . TYR A 143 ? 0.3719 0.3663 0.3069 -0.2148 -0.0059 -0.0141 157 TYR A O 1055 C CB . TYR A 143 ? 0.4711 0.4475 0.4292 -0.1913 -0.0109 -0.0123 157 TYR A CB 1056 C CG . TYR A 143 ? 0.5951 0.5712 0.5491 -0.1947 -0.0097 -0.0140 157 TYR A CG 1057 C CD1 . TYR A 143 ? 0.6774 0.6367 0.6235 -0.1966 -0.0080 -0.0150 157 TYR A CD1 1058 C CD2 . TYR A 143 ? 0.6275 0.6202 0.5860 -0.1956 -0.0104 -0.0145 157 TYR A CD2 1059 C CE1 . TYR A 143 ? 0.7171 0.6762 0.6593 -0.1999 -0.0067 -0.0169 157 TYR A CE1 1060 C CE2 . TYR A 143 ? 0.6915 0.6842 0.6457 -0.1991 -0.0093 -0.0161 157 TYR A CE2 1061 C CZ . TYR A 143 ? 0.7394 0.7152 0.6851 -0.2013 -0.0074 -0.0175 157 TYR A CZ 1062 O OH . TYR A 143 ? 0.8266 0.8024 0.7678 -0.2050 -0.0061 -0.0194 157 TYR A OH 1063 N N . TYR A 144 ? 0.3854 0.3988 0.3421 -0.2027 -0.0098 -0.0126 158 TYR A N 1064 C CA . TYR A 144 ? 0.4012 0.4326 0.3572 -0.2083 -0.0091 -0.0132 158 TYR A CA 1065 C C . TYR A 144 ? 0.3912 0.4246 0.3357 -0.2180 -0.0067 -0.0134 158 TYR A C 1066 O O . TYR A 144 ? 0.3863 0.4245 0.3224 -0.2261 -0.0050 -0.0145 158 TYR A O 1067 C CB . TYR A 144 ? 0.3165 0.3647 0.2879 -0.2014 -0.0114 -0.0126 158 TYR A CB 1068 C CG . TYR A 144 ? 0.4154 0.4834 0.3880 -0.2063 -0.0109 -0.0128 158 TYR A CG 1069 C CD1 . TYR A 144 ? 0.3680 0.4475 0.3435 -0.2073 -0.0115 -0.0130 158 TYR A CD1 1070 C CD2 . TYR A 144 ? 0.3469 0.4227 0.3184 -0.2095 -0.0099 -0.0128 158 TYR A CD2 1071 C CE1 . TYR A 144 ? 0.3733 0.4712 0.3508 -0.2113 -0.0112 -0.0129 158 TYR A CE1 1072 C CE2 . TYR A 144 ? 0.3852 0.4792 0.3587 -0.2135 -0.0094 -0.0131 158 TYR A CE2 1073 C CZ . TYR A 144 ? 0.3994 0.5045 0.3762 -0.2142 -0.0101 -0.0131 158 TYR A CZ 1074 O OH . TYR A 144 ? 0.4054 0.5291 0.3846 -0.2182 -0.0097 -0.0132 158 TYR A OH 1075 N N . VAL A 145 ? 0.3883 0.4189 0.3327 -0.2173 -0.0066 -0.0125 159 VAL A N 1076 C CA . VAL A 145 ? 0.3633 0.3958 0.2971 -0.2264 -0.0044 -0.0125 159 VAL A CA 1077 C C . VAL A 145 ? 0.3827 0.3997 0.3021 -0.2339 -0.0022 -0.0129 159 VAL A C 1078 O O . VAL A 145 ? 0.4454 0.4669 0.3557 -0.2430 -0.0002 -0.0138 159 VAL A O 1079 C CB . VAL A 145 ? 0.4297 0.4608 0.3651 -0.2245 -0.0047 -0.0112 159 VAL A CB 1080 C CG1 . VAL A 145 ? 0.3754 0.4098 0.2999 -0.2344 -0.0023 -0.0111 159 VAL A CG1 1081 C CG2 . VAL A 145 ? 0.3420 0.3888 0.2925 -0.2171 -0.0066 -0.0113 159 VAL A CG2 1082 N N . VAL A 146 ? 0.4883 0.4870 0.4060 -0.2302 -0.0025 -0.0124 160 VAL A N 1083 C CA . VAL A 146 ? 0.4825 0.4656 0.3875 -0.2370 -0.0003 -0.0129 160 VAL A CA 1084 C C . VAL A 146 ? 0.4552 0.4414 0.3555 -0.2422 0.0011 -0.0153 160 VAL A C 1085 O O . VAL A 146 ? 0.4716 0.4540 0.3609 -0.2514 0.0035 -0.0164 160 VAL A O 1086 C CB . VAL A 146 ? 0.4946 0.4574 0.3996 -0.2317 -0.0009 -0.0118 160 VAL A CB 1087 C CG1 . VAL A 146 ? 0.4873 0.4344 0.3807 -0.2385 0.0016 -0.0127 160 VAL A CG1 1088 C CG2 . VAL A 146 ? 0.4934 0.4529 0.3996 -0.2294 -0.0018 -0.0094 160 VAL A CG2 1089 N N . ARG A 147 ? 0.4491 0.4429 0.3577 -0.2369 -0.0003 -0.0161 161 ARG A N 1090 C CA . ARG A 147 ? 0.4979 0.4983 0.4026 -0.2421 0.0008 -0.0182 161 ARG A CA 1091 C C . ARG A 147 ? 0.4485 0.4616 0.3462 -0.2518 0.0024 -0.0189 161 ARG A C 1092 O O . ARG A 147 ? 0.5127 0.5240 0.4009 -0.2598 0.0045 -0.0209 161 ARG A O 1093 C CB . ARG A 147 ? 0.5488 0.5625 0.4651 -0.2355 -0.0016 -0.0181 161 ARG A CB 1094 C CG . ARG A 147 ? 0.6564 0.6601 0.5787 -0.2278 -0.0028 -0.0183 161 ARG A CG 1095 C CD . ARG A 147 ? 0.7497 0.7364 0.6620 -0.2319 -0.0005 -0.0202 161 ARG A CD 1096 N NE . ARG A 147 ? 0.8184 0.7873 0.7303 -0.2278 -0.0005 -0.0191 161 ARG A NE 1097 C CZ . ARG A 147 ? 0.8896 0.8408 0.7937 -0.2306 0.0016 -0.0203 161 ARG A CZ 1098 N NH1 . ARG A 147 ? 0.9259 0.8746 0.8215 -0.2378 0.0040 -0.0230 161 ARG A NH1 1099 N NH2 . ARG A 147 ? 0.9031 0.8392 0.8081 -0.2261 0.0012 -0.0188 161 ARG A NH2 1100 N N . TRP A 148 ? 0.4067 0.4336 0.3096 -0.2509 0.0015 -0.0176 162 TRP A N 1101 C CA . TRP A 148 ? 0.4146 0.4556 0.3124 -0.2595 0.0028 -0.0182 162 TRP A CA 1102 C C . TRP A 148 ? 0.5225 0.5520 0.4066 -0.2688 0.0055 -0.0188 162 TRP A C 1103 O O . TRP A 148 ? 0.5246 0.5594 0.4006 -0.2779 0.0074 -0.0203 162 TRP A O 1104 C CB . TRP A 148 ? 0.4024 0.4590 0.3092 -0.2562 0.0016 -0.0168 162 TRP A CB 1105 C CG . TRP A 148 ? 0.4221 0.4961 0.3256 -0.2642 0.0028 -0.0175 162 TRP A CG 1106 C CD1 . TRP A 148 ? 0.4407 0.5319 0.3484 -0.2656 0.0021 -0.0180 162 TRP A CD1 1107 C CD2 . TRP A 148 ? 0.4440 0.5201 0.3399 -0.2718 0.0047 -0.0174 162 TRP A CD2 1108 N NE1 . TRP A 148 ? 0.4209 0.5246 0.3244 -0.2733 0.0035 -0.0185 162 TRP A NE1 1109 C CE2 . TRP A 148 ? 0.4380 0.5328 0.3342 -0.2773 0.0052 -0.0183 162 TRP A CE2 1110 C CE3 . TRP A 148 ? 0.4331 0.4972 0.3221 -0.2745 0.0059 -0.0166 162 TRP A CE3 1111 C CZ2 . TRP A 148 ? 0.4329 0.5349 0.3229 -0.2854 0.0070 -0.0185 162 TRP A CZ2 1112 C CZ3 . TRP A 148 ? 0.4401 0.5112 0.3225 -0.2829 0.0077 -0.0167 162 TRP A CZ3 1113 C CH2 . TRP A 148 ? 0.4416 0.5314 0.3246 -0.2881 0.0083 -0.0178 162 TRP A CH2 1114 N N . ILE A 149 ? 0.5218 0.5358 0.4036 -0.2667 0.0057 -0.0175 163 ILE A N 1115 C CA . ILE A 149 ? 0.4982 0.5014 0.3682 -0.2752 0.0080 -0.0174 163 ILE A CA 1116 C C . ILE A 149 ? 0.5610 0.5509 0.4225 -0.2802 0.0100 -0.0195 163 ILE A C 1117 O O . ILE A 149 ? 0.4896 0.4785 0.3414 -0.2899 0.0123 -0.0209 163 ILE A O 1118 C CB . ILE A 149 ? 0.5380 0.5285 0.4078 -0.2718 0.0075 -0.0149 163 ILE A CB 1119 C CG1 . ILE A 149 ? 0.5158 0.5207 0.3927 -0.2687 0.0062 -0.0134 163 ILE A CG1 1120 C CG2 . ILE A 149 ? 0.5522 0.5304 0.4096 -0.2810 0.0099 -0.0145 163 ILE A CG2 1121 C CD1 . ILE A 149 ? 0.5207 0.5153 0.4010 -0.2623 0.0048 -0.0109 163 ILE A CD1 1122 N N . LEU A 150 ? 0.5161 0.4961 0.3817 -0.2736 0.0091 -0.0201 164 LEU A N 1123 C CA . LEU A 150 ? 0.5440 0.5128 0.4031 -0.2776 0.0111 -0.0226 164 LEU A CA 1124 C C . LEU A 150 ? 0.5284 0.5112 0.3834 -0.2850 0.0123 -0.0252 164 LEU A C 1125 O O . LEU A 150 ? 0.5232 0.4999 0.3685 -0.2936 0.0149 -0.0274 164 LEU A O 1126 C CB . LEU A 150 ? 0.5189 0.4783 0.3849 -0.2685 0.0098 -0.0228 164 LEU A CB 1127 C CG . LEU A 150 ? 0.4963 0.4394 0.3656 -0.2615 0.0088 -0.0205 164 LEU A CG 1128 C CD1 . LEU A 150 ? 0.4940 0.4298 0.3712 -0.2521 0.0073 -0.0207 164 LEU A CD1 1129 C CD2 . LEU A 150 ? 0.4891 0.4147 0.3484 -0.2680 0.0112 -0.0206 164 LEU A CD2 1130 N N . GLY A 151 ? 0.5342 0.5356 0.3969 -0.2817 0.0104 -0.0248 165 GLY A N 1131 C CA . GLY A 151 ? 0.5055 0.5219 0.3656 -0.2879 0.0110 -0.0267 165 GLY A CA 1132 C C . GLY A 151 ? 0.5042 0.5266 0.3553 -0.2986 0.0130 -0.0274 165 GLY A C 1133 O O . GLY A 151 ? 0.5017 0.5258 0.3449 -0.3070 0.0150 -0.0299 165 GLY A O 1134 N N . ALA A 152 ? 0.4971 0.5227 0.3493 -0.2986 0.0126 -0.0254 166 ALA A N 1135 C CA . ALA A 152 ? 0.5011 0.5315 0.3450 -0.3088 0.0146 -0.0258 166 ALA A CA 1136 C C . ALA A 152 ? 0.5227 0.5364 0.3550 -0.3170 0.0175 -0.0278 166 ALA A C 1137 O O . ALA A 152 ? 0.5363 0.5552 0.3611 -0.3266 0.0193 -0.0299 166 ALA A O 1138 C CB . ALA A 152 ? 0.4971 0.5296 0.3434 -0.3071 0.0140 -0.0233 166 ALA A CB 1139 N N . LYS A 153 ? 0.5659 0.5595 0.3971 -0.3132 0.0178 -0.0273 167 LYS A N 1140 C CA . LYS A 153 ? 0.5470 0.5232 0.3687 -0.3201 0.0206 -0.0292 167 LYS A CA 1141 C C . LYS A 153 ? 0.5773 0.5537 0.3961 -0.3232 0.0220 -0.0328 167 LYS A C 1142 O O . LYS A 153 ? 0.6103 0.5870 0.4208 -0.3330 0.0244 -0.0354 167 LYS A O 1143 C CB . LYS A 153 ? 0.5490 0.5040 0.3718 -0.3144 0.0205 -0.0275 167 LYS A CB 1144 C CG . LYS A 153 ? 0.7690 0.7054 0.5830 -0.3215 0.0234 -0.0289 167 LYS A CG 1145 C CD . LYS A 153 ? 0.8519 0.7932 0.6577 -0.3327 0.0253 -0.0292 167 LYS A CD 1146 C CE . LYS A 153 ? 0.8898 0.8115 0.6881 -0.3395 0.0281 -0.0299 167 LYS A CE 1147 N NZ . LYS A 153 ? 0.8968 0.8042 0.6964 -0.3356 0.0273 -0.0259 167 LYS A NZ 1148 N N . HIS A 154 ? 0.6215 0.5980 0.4471 -0.3151 0.0205 -0.0332 168 HIS A N 1149 C CA . HIS A 154 ? 0.6254 0.5993 0.4480 -0.3176 0.0220 -0.0367 168 HIS A CA 1150 C C . HIS A 154 ? 0.6273 0.6199 0.4470 -0.3245 0.0224 -0.0387 168 HIS A C 1151 O O . HIS A 154 ? 0.6522 0.6417 0.4644 -0.3321 0.0249 -0.0422 168 HIS A O 1152 C CB . HIS A 154 ? 0.6171 0.5848 0.4476 -0.3072 0.0204 -0.0363 168 HIS A CB 1153 C CG . HIS A 154 ? 0.6360 0.5842 0.4688 -0.3011 0.0202 -0.0346 168 HIS A CG 1154 N ND1 . HIS A 154 ? 0.6214 0.5661 0.4638 -0.2899 0.0178 -0.0327 168 HIS A ND1 1155 C CD2 . HIS A 154 ? 0.6677 0.5992 0.4950 -0.3045 0.0220 -0.0343 168 HIS A CD2 1156 C CE1 . HIS A 154 ? 0.6546 0.5813 0.4969 -0.2868 0.0181 -0.0313 168 HIS A CE1 1157 N NE2 . HIS A 154 ? 0.6680 0.5865 0.5014 -0.2954 0.0206 -0.0321 168 HIS A NE2 1158 N N . TYR A 155 ? 0.6018 0.6139 0.4274 -0.3224 0.0200 -0.0366 169 TYR A N 1159 C CA . TYR A 155 ? 0.5934 0.6243 0.4171 -0.3285 0.0200 -0.0380 169 TYR A CA 1160 C C . TYR A 155 ? 0.6460 0.6864 0.4636 -0.3381 0.0212 -0.0382 169 TYR A C 1161 O O . TYR A 155 ? 0.6345 0.6872 0.4480 -0.3454 0.0219 -0.0400 169 TYR A O 1162 C CB . TYR A 155 ? 0.5546 0.6026 0.3894 -0.3204 0.0167 -0.0358 169 TYR A CB 1163 C CG . TYR A 155 ? 0.6090 0.6491 0.4491 -0.3125 0.0157 -0.0361 169 TYR A CG 1164 C CD1 . TYR A 155 ? 0.5801 0.6202 0.4160 -0.3159 0.0169 -0.0389 169 TYR A CD1 1165 C CD2 . TYR A 155 ? 0.5786 0.6111 0.4275 -0.3018 0.0137 -0.0337 169 TYR A CD2 1166 C CE1 . TYR A 155 ? 0.5511 0.5839 0.3917 -0.3087 0.0161 -0.0393 169 TYR A CE1 1167 C CE2 . TYR A 155 ? 0.5779 0.6031 0.4319 -0.2945 0.0128 -0.0340 169 TYR A CE2 1168 C CZ . TYR A 155 ? 0.5984 0.6237 0.4483 -0.2980 0.0141 -0.0367 169 TYR A CZ 1169 O OH . TYR A 155 ? 0.6236 0.6418 0.4786 -0.2907 0.0132 -0.0370 169 TYR A OH 1170 N N . HIS A 156 ? 0.6199 0.6547 0.4367 -0.3384 0.0215 -0.0363 170 HIS A N 1171 C CA . HIS A 156 ? 0.6203 0.6660 0.4327 -0.3468 0.0223 -0.0362 170 HIS A CA 1172 C C . HIS A 156 ? 0.5761 0.6067 0.3800 -0.3536 0.0248 -0.0364 170 HIS A C 1173 O O . HIS A 156 ? 0.5853 0.6237 0.3848 -0.3613 0.0257 -0.0364 170 HIS A O 1174 C CB . HIS A 156 ? 0.5794 0.6424 0.4012 -0.3411 0.0197 -0.0331 170 HIS A CB 1175 C CG . HIS A 156 ? 0.5484 0.6275 0.3791 -0.3353 0.0172 -0.0326 170 HIS A CG 1176 N ND1 . HIS A 156 ? 0.5619 0.6556 0.3906 -0.3410 0.0173 -0.0341 170 HIS A ND1 1177 C CD2 . HIS A 156 ? 0.5514 0.6338 0.3932 -0.3243 0.0146 -0.0306 170 HIS A CD2 1178 C CE1 . HIS A 156 ? 0.5123 0.6179 0.3506 -0.3338 0.0147 -0.0327 170 HIS A CE1 1179 N NE2 . HIS A 156 ? 0.5993 0.6982 0.4459 -0.3236 0.0131 -0.0307 170 HIS A NE2 1180 N N . ASP A 157 ? 0.6111 0.6203 0.4131 -0.3507 0.0257 -0.0365 171 ASP A N 1181 C CA . ASP A 157 ? 0.6703 0.6631 0.4657 -0.3559 0.0278 -0.0360 171 ASP A CA 1182 C C . ASP A 157 ? 0.6573 0.6560 0.4551 -0.3546 0.0265 -0.0325 171 ASP A C 1183 O O . ASP A 157 ? 0.6708 0.6683 0.4625 -0.3625 0.0280 -0.0321 171 ASP A O 1184 C CB . ASP A 157 ? 0.7477 0.7385 0.5331 -0.3684 0.0309 -0.0392 171 ASP A CB 1185 C CG . ASP A 157 ? 0.8695 0.8397 0.6488 -0.3733 0.0332 -0.0389 171 ASP A CG 1186 O OD1 . ASP A 157 ? 0.9115 0.8637 0.6927 -0.3674 0.0332 -0.0381 171 ASP A OD1 1187 O OD2 . ASP A 157 ? 0.9274 0.8993 0.7004 -0.3827 0.0348 -0.0392 171 ASP A OD2 1188 N N . LEU A 158 ? 0.6561 0.6616 0.4632 -0.3447 0.0238 -0.0300 172 LEU A N 1189 C CA . LEU A 158 ? 0.6617 0.6743 0.4722 -0.3426 0.0226 -0.0270 172 LEU A CA 1190 C C . LEU A 158 ? 0.6968 0.6938 0.5105 -0.3349 0.0215 -0.0243 172 LEU A C 1191 O O . LEU A 158 ? 0.5485 0.5395 0.3683 -0.3259 0.0200 -0.0240 172 LEU A O 1192 C CB . LEU A 158 ? 0.6024 0.6377 0.4218 -0.3379 0.0204 -0.0264 172 LEU A CB 1193 C CG . LEU A 158 ? 0.6429 0.6966 0.4600 -0.3456 0.0211 -0.0284 172 LEU A CG 1194 C CD1 . LEU A 158 ? 0.6389 0.7139 0.4669 -0.3393 0.0186 -0.0273 172 LEU A CD1 1195 C CD2 . LEU A 158 ? 0.6206 0.6761 0.4297 -0.3561 0.0231 -0.0284 172 LEU A CD2 1196 N N . ASP A 159 ? 0.7231 0.7138 0.5324 -0.3387 0.0223 -0.0221 173 ASP A N 1197 C CA . ASP A 159 ? 0.7433 0.7203 0.5547 -0.3327 0.0213 -0.0190 173 ASP A CA 1198 C C . ASP A 159 ? 0.7091 0.7006 0.5264 -0.3289 0.0196 -0.0168 173 ASP A C 1199 O O . ASP A 159 ? 0.7388 0.7386 0.5523 -0.3354 0.0205 -0.0160 173 ASP A O 1200 C CB . ASP A 159 ? 0.8175 0.7782 0.6201 -0.3403 0.0233 -0.0177 173 ASP A CB 1201 C CG . ASP A 159 ? 0.9063 0.8502 0.7041 -0.3434 0.0252 -0.0199 173 ASP A CG 1202 O OD1 . ASP A 159 ? 0.9468 0.8847 0.7491 -0.3365 0.0244 -0.0212 173 ASP A OD1 1203 O OD2 . ASP A 159 ? 0.9610 0.8979 0.7511 -0.3528 0.0275 -0.0205 173 ASP A OD2 1204 N N . ILE A 160 ? 0.5947 0.5897 0.4215 -0.3184 0.0172 -0.0160 174 ILE A N 1205 C CA . ILE A 160 ? 0.5195 0.5275 0.3532 -0.3139 0.0157 -0.0142 174 ILE A CA 1206 C C . ILE A 160 ? 0.5257 0.5203 0.3560 -0.3136 0.0157 -0.0111 174 ILE A C 1207 O O . ILE A 160 ? 0.5736 0.5506 0.4040 -0.3089 0.0150 -0.0097 174 ILE A O 1208 C CB . ILE A 160 ? 0.5171 0.5319 0.3629 -0.3026 0.0133 -0.0143 174 ILE A CB 1209 C CG1 . ILE A 160 ? 0.4918 0.5191 0.3410 -0.3028 0.0131 -0.0169 174 ILE A CG1 1210 C CG2 . ILE A 160 ? 0.4864 0.5138 0.3399 -0.2978 0.0120 -0.0128 174 ILE A CG2 1211 C CD1 . ILE A 160 ? 0.5113 0.5574 0.3579 -0.3110 0.0143 -0.0183 174 ILE A CD1 1212 N N . ASP A 161 ? 0.5320 0.5349 0.3575 -0.3198 0.0165 -0.0099 175 ASP A N 1213 C CA . ASP A 161 ? 0.6361 0.6274 0.4555 -0.3216 0.0165 -0.0066 175 ASP A CA 1214 C C . ASP A 161 ? 0.5773 0.5718 0.4031 -0.3135 0.0143 -0.0049 175 ASP A C 1215 O O . ASP A 161 ? 0.6013 0.5808 0.4254 -0.3103 0.0133 -0.0022 175 ASP A O 1216 C CB . ASP A 161 ? 0.6258 0.6237 0.4358 -0.3331 0.0184 -0.0060 175 ASP A CB 1217 C CG . ASP A 161 ? 0.7038 0.6982 0.5076 -0.3416 0.0206 -0.0077 175 ASP A CG 1218 O OD1 . ASP A 161 ? 0.7554 0.7306 0.5544 -0.3436 0.0214 -0.0067 175 ASP A OD1 1219 O OD2 . ASP A 161 ? 0.6990 0.7098 0.5034 -0.3460 0.0215 -0.0102 175 ASP A OD2 1220 N N . TYR A 162 ? 0.5528 0.5670 0.3866 -0.3100 0.0136 -0.0064 176 TYR A N 1221 C CA . TYR A 162 ? 0.5749 0.5939 0.4154 -0.3028 0.0118 -0.0053 176 TYR A CA 1222 C C . TYR A 162 ? 0.5196 0.5488 0.3741 -0.2927 0.0101 -0.0071 176 TYR A C 1223 O O . TYR A 162 ? 0.5573 0.5998 0.4165 -0.2931 0.0105 -0.0093 176 TYR A O 1224 C CB . TYR A 162 ? 0.5627 0.5965 0.3995 -0.3089 0.0128 -0.0049 176 TYR A CB 1225 C CG . TYR A 162 ? 0.5654 0.5881 0.3889 -0.3180 0.0140 -0.0022 176 TYR A CG 1226 C CD1 . TYR A 162 ? 0.6135 0.6349 0.4281 -0.3280 0.0162 -0.0025 176 TYR A CD1 1227 C CD2 . TYR A 162 ? 0.6024 0.6159 0.4224 -0.3166 0.0129 0.0008 176 TYR A CD2 1228 C CE1 . TYR A 162 ? 0.6382 0.6492 0.4411 -0.3365 0.0172 0.0003 176 TYR A CE1 1229 C CE2 . TYR A 162 ? 0.6430 0.6464 0.4508 -0.3252 0.0139 0.0039 176 TYR A CE2 1230 C CZ . TYR A 162 ? 0.6531 0.6552 0.4528 -0.3349 0.0160 0.0037 176 TYR A CZ 1231 O OH . TYR A 162 ? 0.7252 0.7170 0.5138 -0.3431 0.0168 0.0071 176 TYR A OH 1232 N N . ILE A 163 ? 0.4717 0.4942 0.3328 -0.2838 0.0080 -0.0059 177 ILE A N 1233 C CA . ILE A 163 ? 0.5134 0.5449 0.3890 -0.2734 0.0061 -0.0073 177 ILE A CA 1234 C C . ILE A 163 ? 0.4293 0.4692 0.3113 -0.2688 0.0049 -0.0067 177 ILE A C 1235 O O . ILE A 163 ? 0.4433 0.4727 0.3199 -0.2693 0.0044 -0.0046 177 ILE A O 1236 C CB . ILE A 163 ? 0.4705 0.4860 0.3506 -0.2656 0.0045 -0.0071 177 ILE A CB 1237 C CG1 . ILE A 163 ? 0.4718 0.4979 0.3671 -0.2557 0.0025 -0.0085 177 ILE A CG1 1238 C CG2 . ILE A 163 ? 0.4387 0.4358 0.3158 -0.2623 0.0033 -0.0045 177 ILE A CG2 1239 C CD1 . ILE A 163 ? 0.4546 0.4988 0.3542 -0.2581 0.0032 -0.0106 177 ILE A CD1 1240 N N . GLY A 164 ? 0.4141 0.4733 0.3078 -0.2645 0.0044 -0.0086 178 GLY A N 1241 C CA . GLY A 164 ? 0.4024 0.4712 0.3040 -0.2597 0.0035 -0.0088 178 GLY A CA 1242 C C . GLY A 164 ? 0.4385 0.5058 0.3547 -0.2475 0.0008 -0.0092 178 GLY A C 1243 O O . GLY A 164 ? 0.4272 0.4834 0.3461 -0.2427 -0.0005 -0.0089 178 GLY A O 1244 N N . ILE A 165 ? 0.4587 0.5376 0.3849 -0.2425 0.0000 -0.0102 179 ILE A N 1245 C CA . ILE A 165 ? 0.3531 0.4292 0.2929 -0.2311 -0.0028 -0.0104 179 ILE A CA 1246 C C . ILE A 165 ? 0.4119 0.5058 0.3690 -0.2240 -0.0037 -0.0126 179 ILE A C 1247 O O . ILE A 165 ? 0.4130 0.5049 0.3763 -0.2194 -0.0050 -0.0127 179 ILE A O 1248 C CB . ILE A 165 ? 0.3519 0.4250 0.2910 -0.2297 -0.0036 -0.0099 179 ILE A CB 1249 C CG1 . ILE A 165 ? 0.3845 0.4389 0.3064 -0.2367 -0.0031 -0.0069 179 ILE A CG1 1250 C CG2 . ILE A 165 ? 0.3474 0.4179 0.3016 -0.2177 -0.0067 -0.0105 179 ILE A CG2 1251 C CD1 . ILE A 165 ? 0.3988 0.4323 0.3164 -0.2346 -0.0041 -0.0051 179 ILE A CD1 1252 N N . TRP A 166 ? 0.3606 0.4716 0.3256 -0.2229 -0.0032 -0.0145 180 TRP A N 1253 C CA . TRP A 166 ? 0.3769 0.5050 0.3593 -0.2159 -0.0041 -0.0164 180 TRP A CA 1254 C C . TRP A 166 ? 0.3784 0.5258 0.3629 -0.2200 -0.0019 -0.0184 180 TRP A C 1255 O O . TRP A 166 ? 0.3659 0.5183 0.3531 -0.2189 -0.0016 -0.0198 180 TRP A O 1256 C CB . TRP A 166 ? 0.3166 0.4427 0.3151 -0.2038 -0.0073 -0.0169 180 TRP A CB 1257 C CG . TRP A 166 ? 0.2787 0.4195 0.2964 -0.1955 -0.0089 -0.0183 180 TRP A CG 1258 C CD1 . TRP A 166 ? 0.2992 0.4519 0.3200 -0.1975 -0.0081 -0.0184 180 TRP A CD1 1259 C CD2 . TRP A 166 ? 0.3015 0.4453 0.3373 -0.1840 -0.0117 -0.0193 180 TRP A CD2 1260 N NE1 . TRP A 166 ? 0.2762 0.4392 0.3154 -0.1884 -0.0102 -0.0191 180 TRP A NE1 1261 C CE2 . TRP A 166 ? 0.2767 0.4339 0.3260 -0.1796 -0.0125 -0.0197 180 TRP A CE2 1262 C CE3 . TRP A 166 ? 0.2827 0.4192 0.3249 -0.1772 -0.0138 -0.0198 180 TRP A CE3 1263 C CZ2 . TRP A 166 ? 0.2603 0.4240 0.3281 -0.1695 -0.0151 -0.0205 180 TRP A CZ2 1264 C CZ3 . TRP A 166 ? 0.2493 0.3918 0.3114 -0.1661 -0.0166 -0.0210 180 TRP A CZ3 1265 C CH2 . TRP A 166 ? 0.2660 0.4215 0.3408 -0.1623 -0.0172 -0.0212 180 TRP A CH2 1266 N N . ASN A 167 ? 0.3642 0.5228 0.3473 -0.2250 -0.0003 -0.0189 181 ASN A N 1267 C CA . ASN A 167 ? 0.3246 0.5009 0.3073 -0.2307 0.0023 -0.0208 181 ASN A CA 1268 C C . ASN A 167 ? 0.3817 0.5729 0.3797 -0.2239 0.0021 -0.0234 181 ASN A C 1269 O O . ASN A 167 ? 0.3662 0.5641 0.3811 -0.2146 0.0000 -0.0241 181 ASN A O 1270 C CB . ASN A 167 ? 0.3278 0.5155 0.3118 -0.2342 0.0031 -0.0210 181 ASN A CB 1271 C CG . ASN A 167 ? 0.4347 0.6398 0.4169 -0.2409 0.0060 -0.0229 181 ASN A CG 1272 O OD1 . ASN A 167 ? 0.4394 0.6418 0.4067 -0.2504 0.0084 -0.0228 181 ASN A OD1 1273 N ND2 . ASN A 167 ? 0.3243 0.5472 0.3223 -0.2358 0.0058 -0.0247 181 ASN A ND2 1274 N N . GLU A 168 ? 0.4139 0.6103 0.4059 -0.2287 0.0043 -0.0249 182 GLU A N 1275 C CA . GLU A 168 ? 0.3775 0.5894 0.3830 -0.2234 0.0048 -0.0283 182 GLU A CA 1276 C C . GLU A 168 ? 0.3592 0.5666 0.3800 -0.2113 0.0015 -0.0289 182 GLU A C 1277 O O . GLU A 168 ? 0.3876 0.6082 0.4245 -0.2043 0.0012 -0.0317 182 GLU A O 1278 C CB . GLU A 168 ? 0.3758 0.6078 0.3924 -0.2228 0.0060 -0.0303 182 GLU A CB 1279 C CG . GLU A 168 ? 0.4362 0.6776 0.4401 -0.2346 0.0096 -0.0309 182 GLU A CG 1280 C CD . GLU A 168 ? 0.5642 0.8178 0.5663 -0.2384 0.0126 -0.0342 182 GLU A CD 1281 O OE1 . GLU A 168 ? 0.5693 0.8285 0.5840 -0.2306 0.0119 -0.0367 182 GLU A OE1 1282 O OE2 . GLU A 168 ? 0.6089 0.8670 0.5973 -0.2491 0.0155 -0.0344 182 GLU A OE2 1283 N N . ARG A 169 ? 0.3195 0.5081 0.3360 -0.2086 -0.0009 -0.0264 183 ARG A N 1284 C CA . ARG A 169 ? 0.3169 0.4998 0.3480 -0.1970 -0.0044 -0.0267 183 ARG A CA 1285 C C . ARG A 169 ? 0.3422 0.5077 0.3630 -0.1980 -0.0055 -0.0254 183 ARG A C 1286 O O . ARG A 169 ? 0.3616 0.5181 0.3643 -0.2074 -0.0038 -0.0235 183 ARG A O 1287 C CB . ARG A 169 ? 0.2974 0.4751 0.3371 -0.1906 -0.0070 -0.0248 183 ARG A CB 1288 C CG . ARG A 169 ? 0.2869 0.4809 0.3392 -0.1879 -0.0068 -0.0256 183 ARG A CG 1289 C CD . ARG A 169 ? 0.3053 0.5115 0.3781 -0.1782 -0.0082 -0.0281 183 ARG A CD 1290 N NE . ARG A 169 ? 0.3202 0.5415 0.4043 -0.1764 -0.0079 -0.0284 183 ARG A NE 1291 C CZ . ARG A 169 ? 0.3198 0.5561 0.4021 -0.1824 -0.0049 -0.0301 183 ARG A CZ 1292 N NH1 . ARG A 169 ? 0.3843 0.6234 0.4535 -0.1907 -0.0017 -0.0319 183 ARG A NH1 1293 N NH2 . ARG A 169 ? 0.3039 0.5539 0.3966 -0.1809 -0.0049 -0.0301 183 ARG A NH2 1294 N N . PRO A 170 ? 0.3575 0.5177 0.3900 -0.1884 -0.0086 -0.0261 184 PRO A N 1295 C CA . PRO A 170 ? 0.4346 0.5794 0.4570 -0.1900 -0.0098 -0.0248 184 PRO A CA 1296 C C . PRO A 170 ? 0.4541 0.5778 0.4631 -0.1933 -0.0105 -0.0209 184 PRO A C 1297 O O . PRO A 170 ? 0.4360 0.5558 0.4483 -0.1907 -0.0113 -0.0196 184 PRO A O 1298 C CB . PRO A 170 ? 0.4440 0.5883 0.4840 -0.1780 -0.0134 -0.0267 184 PRO A CB 1299 C CG . PRO A 170 ? 0.3910 0.5549 0.4488 -0.1721 -0.0131 -0.0298 184 PRO A CG 1300 C CD . PRO A 170 ? 0.3722 0.5409 0.4267 -0.1765 -0.0112 -0.0281 184 PRO A CD 1301 N N . PHE A 171 ? 0.4478 0.5584 0.4417 -0.1993 -0.0103 -0.0189 185 PHE A N 1302 C CA . PHE A 171 ? 0.4473 0.5359 0.4300 -0.2009 -0.0114 -0.0152 185 PHE A CA 1303 C C . PHE A 171 ? 0.4944 0.5693 0.4834 -0.1924 -0.0150 -0.0147 185 PHE A C 1304 O O . PHE A 171 ? 0.4827 0.5641 0.4809 -0.1875 -0.0166 -0.0169 185 PHE A O 1305 C CB . PHE A 171 ? 0.4671 0.5469 0.4284 -0.2130 -0.0091 -0.0125 185 PHE A CB 1306 C CG . PHE A 171 ? 0.4267 0.5046 0.3805 -0.2166 -0.0093 -0.0120 185 PHE A CG 1307 C CD1 . PHE A 171 ? 0.4201 0.4796 0.3699 -0.2138 -0.0121 -0.0096 185 PHE A CD1 1308 C CD2 . PHE A 171 ? 0.4226 0.5173 0.3728 -0.2234 -0.0066 -0.0140 185 PHE A CD2 1309 C CE1 . PHE A 171 ? 0.4816 0.5395 0.4235 -0.2178 -0.0127 -0.0088 185 PHE A CE1 1310 C CE2 . PHE A 171 ? 0.4644 0.5584 0.4067 -0.2276 -0.0067 -0.0137 185 PHE A CE2 1311 C CZ . PHE A 171 ? 0.4600 0.5355 0.3980 -0.2250 -0.0100 -0.0108 185 PHE A CZ 1312 N N . ASP A 172 ? 0.4867 0.5431 0.4711 -0.1906 -0.0163 -0.0120 186 ASP A N 1313 C CA . ASP A 172 ? 0.4478 0.4892 0.4362 -0.1832 -0.0195 -0.0111 186 ASP A CA 1314 C C . ASP A 172 ? 0.4514 0.4726 0.4217 -0.1896 -0.0190 -0.0072 186 ASP A C 1315 O O . ASP A 172 ? 0.3872 0.4007 0.3493 -0.1936 -0.0174 -0.0056 186 ASP A O 1316 C CB . ASP A 172 ? 0.4812 0.5198 0.4838 -0.1733 -0.0214 -0.0119 186 ASP A CB 1317 C CG . ASP A 172 ? 0.5439 0.5676 0.5520 -0.1649 -0.0246 -0.0114 186 ASP A CG 1318 O OD1 . ASP A 172 ? 0.6020 0.6075 0.5983 -0.1672 -0.0247 -0.0086 186 ASP A OD1 1319 O OD2 . ASP A 172 ? 0.5656 0.5955 0.5905 -0.1556 -0.0270 -0.0138 186 ASP A OD2 1320 N N . ALA A 173 ? 0.4390 0.4517 0.4028 -0.1908 -0.0206 -0.0057 187 ALA A N 1321 C CA . ALA A 173 ? 0.4470 0.4412 0.3928 -0.1977 -0.0201 -0.0013 187 ALA A CA 1322 C C . ALA A 173 ? 0.4196 0.3952 0.3665 -0.1919 -0.0211 0.0004 187 ALA A C 1323 O O . ALA A 173 ? 0.4570 0.4202 0.3921 -0.1971 -0.0196 0.0030 187 ALA A O 1324 C CB . ALA A 173 ? 0.4272 0.4158 0.3664 -0.1996 -0.0221 0.0005 187 ALA A CB 1325 N N . ASN A 174 ? 0.4028 0.3771 0.3645 -0.1810 -0.0234 -0.0014 188 ASN A N 1326 C CA . ASN A 174 ? 0.4525 0.4119 0.4168 -0.1751 -0.0237 -0.0004 188 ASN A CA 1327 C C . ASN A 174 ? 0.4713 0.4346 0.4349 -0.1778 -0.0211 -0.0013 188 ASN A C 1328 O O . ASN A 174 ? 0.5007 0.4503 0.4588 -0.1782 -0.0201 0.0001 188 ASN A O 1329 C CB . ASN A 174 ? 0.4419 0.4002 0.4224 -0.1630 -0.0265 -0.0023 188 ASN A CB 1330 C CG . ASN A 174 ? 0.5508 0.4985 0.5292 -0.1600 -0.0292 -0.0007 188 ASN A CG 1331 O OD1 . ASN A 174 ? 0.5947 0.5275 0.5600 -0.1641 -0.0292 0.0030 188 ASN A OD1 1332 N ND2 . ASN A 174 ? 0.5405 0.4961 0.5321 -0.1529 -0.0317 -0.0034 188 ASN A ND2 1333 N N . TYR A 175 ? 0.3736 0.3558 0.3429 -0.1799 -0.0200 -0.0038 189 TYR A N 1334 C CA . TYR A 175 ? 0.4208 0.4079 0.3880 -0.1837 -0.0178 -0.0045 189 TYR A CA 1335 C C . TYR A 175 ? 0.4394 0.4194 0.3890 -0.1945 -0.0152 -0.0025 189 TYR A C 1336 O O . TYR A 175 ? 0.4292 0.4011 0.3738 -0.1966 -0.0138 -0.0021 189 TYR A O 1337 C CB . TYR A 175 ? 0.3694 0.3788 0.3462 -0.1837 -0.0172 -0.0071 189 TYR A CB 1338 C CG . TYR A 175 ? 0.3734 0.3882 0.3453 -0.1894 -0.0148 -0.0074 189 TYR A CG 1339 C CD1 . TYR A 175 ? 0.3619 0.3724 0.3386 -0.1853 -0.0152 -0.0079 189 TYR A CD1 1340 C CD2 . TYR A 175 ? 0.3316 0.3557 0.2937 -0.1992 -0.0123 -0.0075 189 TYR A CD2 1341 C CE1 . TYR A 175 ? 0.3756 0.3910 0.3473 -0.1909 -0.0133 -0.0083 189 TYR A CE1 1342 C CE2 . TYR A 175 ? 0.4050 0.4338 0.3624 -0.2046 -0.0103 -0.0080 189 TYR A CE2 1343 C CZ . TYR A 175 ? 0.4235 0.4478 0.3856 -0.2005 -0.0109 -0.0084 189 TYR A CZ 1344 O OH . TYR A 175 ? 0.4104 0.4397 0.3676 -0.2062 -0.0092 -0.0091 189 TYR A OH 1345 N N . ILE A 176 ? 0.4403 0.4237 0.3805 -0.2017 -0.0144 -0.0013 190 ILE A N 1346 C CA . ILE A 176 ? 0.4358 0.4136 0.3596 -0.2125 -0.0120 0.0006 190 ILE A CA 1347 C C . ILE A 176 ? 0.4858 0.4403 0.4021 -0.2118 -0.0124 0.0034 190 ILE A C 1348 O O . ILE A 176 ? 0.4831 0.4302 0.3908 -0.2174 -0.0104 0.0040 190 ILE A O 1349 C CB . ILE A 176 ? 0.4641 0.4492 0.3788 -0.2204 -0.0112 0.0016 190 ILE A CB 1350 C CG1 . ILE A 176 ? 0.4479 0.4573 0.3714 -0.2208 -0.0102 -0.0017 190 ILE A CG1 1351 C CG2 . ILE A 176 ? 0.4344 0.4125 0.3324 -0.2315 -0.0088 0.0038 190 ILE A CG2 1352 C CD1 . ILE A 176 ? 0.4349 0.4546 0.3500 -0.2290 -0.0088 -0.0014 190 ILE A CD1 1353 N N . LYS A 177 ? 0.4570 0.4004 0.3771 -0.2049 -0.0149 0.0048 191 LYS A N 1354 C CA . LYS A 177 ? 0.5347 0.4566 0.4504 -0.2023 -0.0154 0.0074 191 LYS A CA 1355 C C . LYS A 177 ? 0.5242 0.4410 0.4469 -0.1972 -0.0145 0.0055 191 LYS A C 1356 O O . LYS A 177 ? 0.4975 0.4019 0.4134 -0.2003 -0.0129 0.0066 191 LYS A O 1357 C CB . LYS A 177 ? 0.5534 0.4662 0.4734 -0.1950 -0.0185 0.0092 191 LYS A CB 1358 C CG . LYS A 177 ? 0.4959 0.4072 0.4045 -0.2016 -0.0195 0.0123 191 LYS A CG 1359 C CD . LYS A 177 ? 0.4724 0.3805 0.3873 -0.1942 -0.0231 0.0131 191 LYS A CD 1360 C CE . LYS A 177 ? 0.5705 0.4813 0.4743 -0.2018 -0.0242 0.0156 191 LYS A CE 1361 N NZ . LYS A 177 ? 0.5695 0.4753 0.4779 -0.1953 -0.0282 0.0167 191 LYS A NZ 1362 N N A GLU A 178 ? 0.4984 0.4250 0.4347 -0.1897 -0.0155 0.0028 192 GLU A N 1363 N N B GLU A 178 ? 0.4997 0.4262 0.4359 -0.1898 -0.0155 0.0028 192 GLU A N 1364 C CA A GLU A 178 ? 0.4724 0.3964 0.4152 -0.1854 -0.0147 0.0009 192 GLU A CA 1365 C CA B GLU A 178 ? 0.4715 0.3954 0.4144 -0.1853 -0.0147 0.0009 192 GLU A CA 1366 C C A GLU A 178 ? 0.4584 0.3872 0.3930 -0.1943 -0.0120 -0.0001 192 GLU A C 1367 C C B GLU A 178 ? 0.4568 0.3861 0.3918 -0.1941 -0.0121 -0.0002 192 GLU A C 1368 O O A GLU A 178 ? 0.4776 0.3964 0.4069 -0.1964 -0.0108 -0.0004 192 GLU A O 1369 O O B GLU A 178 ? 0.4773 0.3972 0.4074 -0.1961 -0.0108 -0.0006 192 GLU A O 1370 C CB A GLU A 178 ? 0.4719 0.4077 0.4302 -0.1769 -0.0165 -0.0016 192 GLU A CB 1371 C CB B GLU A 178 ? 0.4702 0.4050 0.4287 -0.1764 -0.0166 -0.0015 192 GLU A CB 1372 C CG A GLU A 178 ? 0.5031 0.4321 0.4713 -0.1667 -0.0190 -0.0013 192 GLU A CG 1373 C CG B GLU A 178 ? 0.5083 0.4432 0.4696 -0.1749 -0.0161 -0.0032 192 GLU A CG 1374 C CD A GLU A 178 ? 0.5892 0.4991 0.5540 -0.1636 -0.0188 0.0000 192 GLU A CD 1375 C CD B GLU A 178 ? 0.6034 0.5200 0.5631 -0.1709 -0.0161 -0.0025 192 GLU A CD 1376 O OE1 A GLU A 178 ? 0.6161 0.5226 0.5799 -0.1642 -0.0177 -0.0010 192 GLU A OE1 1377 O OE1 B GLU A 178 ? 0.6167 0.5243 0.5808 -0.1643 -0.0176 -0.0013 192 GLU A OE1 1378 O OE2 A GLU A 178 ? 0.5913 0.4898 0.5545 -0.1606 -0.0198 0.0021 192 GLU A OE2 1379 O OE2 B GLU A 178 ? 0.6404 0.5522 0.5948 -0.1745 -0.0144 -0.0034 192 GLU A OE2 1380 N N . LEU A 179 ? 0.4251 0.3691 0.3562 -0.2009 -0.0111 -0.0007 193 LEU A N 1381 C CA . LEU A 179 ? 0.4804 0.4304 0.4035 -0.2098 -0.0085 -0.0018 193 LEU A CA 1382 C C . LEU A 179 ? 0.5405 0.4747 0.4501 -0.2170 -0.0067 0.0001 193 LEU A C 1383 O O . LEU A 179 ? 0.4954 0.4257 0.3995 -0.2218 -0.0048 -0.0010 193 LEU A O 1384 C CB . LEU A 179 ? 0.4862 0.4556 0.4080 -0.2156 -0.0078 -0.0026 193 LEU A CB 1385 C CG . LEU A 179 ? 0.4885 0.4651 0.4018 -0.2253 -0.0051 -0.0036 193 LEU A CG 1386 C CD1 . LEU A 179 ? 0.4895 0.4709 0.4090 -0.2227 -0.0049 -0.0058 193 LEU A CD1 1387 C CD2 . LEU A 179 ? 0.4169 0.4118 0.3285 -0.2311 -0.0041 -0.0042 193 LEU A CD2 1388 N N . ARG A 180 ? 0.5212 0.4459 0.4244 -0.2186 -0.0074 0.0030 194 ARG A N 1389 C CA . ARG A 180 ? 0.5439 0.4524 0.4356 -0.2247 -0.0059 0.0054 194 ARG A CA 1390 C C . ARG A 180 ? 0.5100 0.4017 0.4051 -0.2192 -0.0058 0.0053 194 ARG A C 1391 O O . ARG A 180 ? 0.5327 0.4163 0.4202 -0.2252 -0.0037 0.0049 194 ARG A O 1392 C CB . ARG A 180 ? 0.5563 0.4580 0.4408 -0.2270 -0.0071 0.0091 194 ARG A CB 1393 C CG . ARG A 180 ? 0.5190 0.4037 0.3923 -0.2332 -0.0059 0.0123 194 ARG A CG 1394 C CD . ARG A 180 ? 0.5230 0.4137 0.3856 -0.2450 -0.0032 0.0119 194 ARG A CD 1395 N NE . ARG A 180 ? 0.5279 0.4155 0.3909 -0.2470 -0.0010 0.0095 194 ARG A NE 1396 C CZ . ARG A 180 ? 0.5642 0.4592 0.4202 -0.2562 0.0014 0.0081 194 ARG A CZ 1397 N NH1 . ARG A 180 ? 0.5705 0.4768 0.4191 -0.2641 0.0020 0.0088 194 ARG A NH1 1398 N NH2 . ARG A 180 ? 0.5312 0.4229 0.3877 -0.2579 0.0032 0.0056 194 ARG A NH2 1399 N N . LYS A 181 ? 0.4934 0.3802 0.3977 -0.2093 -0.0080 0.0054 195 LYS A N 1400 C CA . LYS A 181 ? 0.5426 0.4144 0.4492 -0.2043 -0.0082 0.0052 195 LYS A CA 1401 C C . LYS A 181 ? 0.5741 0.4492 0.4803 -0.2067 -0.0064 0.0019 195 LYS A C 1402 O O . LYS A 181 ? 0.5680 0.4307 0.4689 -0.2097 -0.0047 0.0014 195 LYS A O 1403 C CB . LYS A 181 ? 0.5902 0.4613 0.5084 -0.1930 -0.0109 0.0054 195 LYS A CB 1404 C CG . LYS A 181 ? 0.6778 0.5361 0.6007 -0.1864 -0.0112 0.0048 195 LYS A CG 1405 C CD . LYS A 181 ? 0.7704 0.6275 0.7042 -0.1756 -0.0139 0.0055 195 LYS A CD 1406 C CE . LYS A 181 ? 0.8020 0.6646 0.7463 -0.1686 -0.0145 0.0026 195 LYS A CE 1407 N NZ . LYS A 181 ? 0.8277 0.6898 0.7830 -0.1582 -0.0170 0.0029 195 LYS A NZ 1408 N N . MET A 182 ? 0.5738 0.4658 0.4858 -0.2057 -0.0069 -0.0005 196 MET A N 1409 C CA . MET A 182 ? 0.5359 0.4341 0.4473 -0.2086 -0.0054 -0.0035 196 MET A CA 1410 C C . MET A 182 ? 0.5427 0.4406 0.4420 -0.2199 -0.0026 -0.0042 196 MET A C 1411 O O . MET A 182 ? 0.5146 0.4067 0.4097 -0.2233 -0.0008 -0.0062 196 MET A O 1412 C CB . MET A 182 ? 0.5140 0.4318 0.4347 -0.2052 -0.0068 -0.0051 196 MET A CB 1413 C CG . MET A 182 ? 0.5729 0.5000 0.4930 -0.2088 -0.0055 -0.0078 196 MET A CG 1414 S SD . MET A 182 ? 0.7916 0.7139 0.7202 -0.2008 -0.0066 -0.0094 196 MET A SD 1415 C CE . MET A 182 ? 0.5014 0.4344 0.4459 -0.1899 -0.0100 -0.0086 196 MET A CE 1416 N N . LEU A 183 ? 0.5378 0.4421 0.4316 -0.2261 -0.0020 -0.0029 197 LEU A N 1417 C CA . LEU A 183 ? 0.5409 0.4443 0.4233 -0.2371 0.0008 -0.0034 197 LEU A CA 1418 C C . LEU A 183 ? 0.5521 0.4347 0.4280 -0.2393 0.0021 -0.0025 197 LEU A C 1419 O O . LEU A 183 ? 0.5627 0.4406 0.4329 -0.2450 0.0044 -0.0046 197 LEU A O 1420 C CB . LEU A 183 ? 0.5546 0.4666 0.4322 -0.2429 0.0011 -0.0016 197 LEU A CB 1421 C CG . LEU A 183 ? 0.5165 0.4509 0.3980 -0.2444 0.0010 -0.0030 197 LEU A CG 1422 C CD1 . LEU A 183 ? 0.4613 0.4011 0.3374 -0.2497 0.0012 -0.0009 197 LEU A CD1 1423 C CD2 . LEU A 183 ? 0.4553 0.3991 0.3327 -0.2513 0.0029 -0.0058 197 LEU A CD2 1424 N N . ASP A 184 ? 0.5737 0.4437 0.4508 -0.2349 0.0008 0.0007 198 ASP A N 1425 C CA . ASP A 184 ? 0.6353 0.4851 0.5076 -0.2364 0.0020 0.0021 198 ASP A CA 1426 C C . ASP A 184 ? 0.6473 0.4890 0.5233 -0.2325 0.0027 -0.0006 198 ASP A C 1427 O O . ASP A 184 ? 0.6435 0.4745 0.5140 -0.2377 0.0050 -0.0018 198 ASP A O 1428 C CB . ASP A 184 ? 0.6493 0.4882 0.5238 -0.2312 0.0000 0.0063 198 ASP A CB 1429 C CG . ASP A 184 ? 0.6564 0.5022 0.5261 -0.2358 -0.0005 0.0093 198 ASP A CG 1430 O OD1 . ASP A 184 ? 0.5929 0.4469 0.4556 -0.2448 0.0013 0.0086 198 ASP A OD1 1431 O OD2 . ASP A 184 ? 0.6557 0.4988 0.5287 -0.2305 -0.0026 0.0123 198 ASP A OD2 1432 N N . TYR A 185 ? 0.6228 0.4698 0.5084 -0.2237 0.0008 -0.0018 199 TYR A N 1433 C CA . TYR A 185 ? 0.6480 0.4884 0.5379 -0.2194 0.0013 -0.0044 199 TYR A CA 1434 C C . TYR A 185 ? 0.6027 0.4479 0.4869 -0.2269 0.0040 -0.0081 199 TYR A C 1435 O O . TYR A 185 ? 0.5484 0.3832 0.4313 -0.2277 0.0058 -0.0102 199 TYR A O 1436 C CB . TYR A 185 ? 0.6714 0.5196 0.5730 -0.2091 -0.0013 -0.0049 199 TYR A CB 1437 C CG . TYR A 185 ? 0.7617 0.6029 0.6686 -0.2037 -0.0010 -0.0071 199 TYR A CG 1438 C CD1 . TYR A 185 ? 0.7932 0.6166 0.7007 -0.2007 -0.0003 -0.0063 199 TYR A CD1 1439 C CD2 . TYR A 185 ? 0.7924 0.6455 0.7046 -0.2014 -0.0014 -0.0097 199 TYR A CD2 1440 C CE1 . TYR A 185 ? 0.8095 0.6271 0.7223 -0.1958 0.0001 -0.0085 199 TYR A CE1 1441 C CE2 . TYR A 185 ? 0.7845 0.6317 0.7014 -0.1967 -0.0010 -0.0117 199 TYR A CE2 1442 C CZ . TYR A 185 ? 0.7996 0.6292 0.7167 -0.1939 -0.0002 -0.0113 199 TYR A CZ 1443 O OH . TYR A 185 ? 0.7933 0.6177 0.7154 -0.1894 0.0003 -0.0134 199 TYR A OH 1444 N N . GLN A 186 ? 0.6043 0.4658 0.4854 -0.2326 0.0043 -0.0091 200 GLN A N 1445 C CA . GLN A 186 ? 0.6121 0.4805 0.4876 -0.2401 0.0067 -0.0126 200 GLN A CA 1446 C C . GLN A 186 ? 0.6655 0.5282 0.5299 -0.2510 0.0094 -0.0127 200 GLN A C 1447 O O . GLN A 186 ? 0.6817 0.5524 0.5404 -0.2587 0.0113 -0.0154 200 GLN A O 1448 C CB . GLN A 186 ? 0.5723 0.4625 0.4515 -0.2402 0.0055 -0.0136 200 GLN A CB 1449 C CG . GLN A 186 ? 0.5715 0.4682 0.4626 -0.2299 0.0029 -0.0137 200 GLN A CG 1450 C CD . GLN A 186 ? 0.6024 0.4936 0.4949 -0.2280 0.0039 -0.0164 200 GLN A CD 1451 O OE1 . GLN A 186 ? 0.6649 0.5547 0.5497 -0.2356 0.0064 -0.0190 200 GLN A OE1 1452 N NE2 . GLN A 186 ? 0.5178 0.4060 0.4199 -0.2183 0.0019 -0.0160 200 GLN A NE2 1453 N N . GLY A 187 ? 0.6945 0.5436 0.5559 -0.2518 0.0095 -0.0098 201 GLY A N 1454 C CA . GLY A 187 ? 0.6885 0.5296 0.5403 -0.2617 0.0121 -0.0095 201 GLY A CA 1455 C C . GLY A 187 ? 0.6958 0.5500 0.5419 -0.2692 0.0124 -0.0085 201 GLY A C 1456 O O . GLY A 187 ? 0.6652 0.5178 0.5030 -0.2789 0.0148 -0.0094 201 GLY A O 1457 N N . LEU A 188 ? 0.6256 0.4927 0.4765 -0.2648 0.0100 -0.0068 202 LEU A N 1458 C CA . LEU A 188 ? 0.6488 0.5301 0.4953 -0.2714 0.0103 -0.0060 202 LEU A CA 1459 C C . LEU A 188 ? 0.6723 0.5491 0.5177 -0.2708 0.0092 -0.0016 202 LEU A C 1460 O O . LEU A 188 ? 0.6332 0.5237 0.4806 -0.2703 0.0080 -0.0005 202 LEU A O 1461 C CB . LEU A 188 ? 0.6239 0.5264 0.4767 -0.2684 0.0090 -0.0078 202 LEU A CB 1462 C CG . LEU A 188 ? 0.5822 0.4907 0.4357 -0.2696 0.0100 -0.0116 202 LEU A CG 1463 C CD1 . LEU A 188 ? 0.5649 0.4933 0.4269 -0.2648 0.0082 -0.0125 202 LEU A CD1 1464 C CD2 . LEU A 188 ? 0.5860 0.4957 0.4295 -0.2811 0.0130 -0.0137 202 LEU A CD2 1465 N N . GLN A 189 ? 0.7135 0.5714 0.5559 -0.2711 0.0096 0.0008 203 GLN A N 1466 C CA . GLN A 189 ? 0.7035 0.5558 0.5436 -0.2716 0.0086 0.0054 203 GLN A CA 1467 C C . GLN A 189 ? 0.6620 0.5250 0.4947 -0.2812 0.0099 0.0062 203 GLN A C 1468 O O . GLN A 189 ? 0.7010 0.5683 0.5330 -0.2812 0.0088 0.0093 203 GLN A O 1469 C CB . GLN A 189 ? 0.7330 0.5630 0.5710 -0.2715 0.0092 0.0082 203 GLN A CB 1470 C CG . GLN A 189 ? 0.7689 0.5878 0.6151 -0.2611 0.0077 0.0080 203 GLN A CG 1471 C CD . GLN A 189 ? 0.8046 0.6213 0.6524 -0.2608 0.0094 0.0034 203 GLN A CD 1472 O OE1 . GLN A 189 ? 0.8195 0.6446 0.6627 -0.2679 0.0114 0.0002 203 GLN A OE1 1473 N NE2 . GLN A 189 ? 0.8506 0.6560 0.7048 -0.2530 0.0087 0.0031 203 GLN A NE2 1474 N N . ARG A 190 ? 0.6706 0.5387 0.4978 -0.2895 0.0123 0.0034 204 ARG A N 1475 C CA . ARG A 190 ? 0.7464 0.6242 0.5665 -0.2992 0.0137 0.0042 204 ARG A CA 1476 C C . ARG A 190 ? 0.6982 0.5986 0.5209 -0.2987 0.0128 0.0030 204 ARG A C 1477 O O . ARG A 190 ? 0.7680 0.6772 0.5836 -0.3066 0.0135 0.0041 204 ARG A O 1478 C CB . ARG A 190 ? 0.8424 0.7185 0.6555 -0.3089 0.0167 0.0014 204 ARG A CB 1479 C CG . ARG A 190 ? 0.9482 0.8395 0.7633 -0.3096 0.0172 -0.0033 204 ARG A CG 1480 C CD . ARG A 190 ? 1.0659 0.9589 0.8732 -0.3207 0.0201 -0.0059 204 ARG A CD 1481 N NE . ARG A 190 ? 1.1519 1.0493 0.9527 -0.3292 0.0212 -0.0036 204 ARG A NE 1482 C CZ . ARG A 190 ? 1.1857 1.1026 0.9861 -0.3327 0.0211 -0.0042 204 ARG A CZ 1483 N NH1 . ARG A 190 ? 1.1898 1.1235 0.9961 -0.3283 0.0200 -0.0068 204 ARG A NH1 1484 N NH2 . ARG A 190 ? 1.2026 1.1224 0.9966 -0.3409 0.0222 -0.0022 204 ARG A NH2 1485 N N . VAL A 191 ? 0.6043 0.5140 0.4363 -0.2904 0.0112 0.0008 205 VAL A N 1486 C CA . VAL A 191 ? 0.5953 0.5264 0.4304 -0.2900 0.0104 -0.0005 205 VAL A CA 1487 C C . VAL A 191 ? 0.5861 0.5191 0.4210 -0.2877 0.0086 0.0025 205 VAL A C 1488 O O . VAL A 191 ? 0.6006 0.5227 0.4399 -0.2800 0.0068 0.0044 205 VAL A O 1489 C CB . VAL A 191 ? 0.5732 0.5133 0.4196 -0.2813 0.0091 -0.0033 205 VAL A CB 1490 C CG1 . VAL A 191 ? 0.4872 0.4491 0.3386 -0.2802 0.0082 -0.0041 205 VAL A CG1 1491 C CG2 . VAL A 191 ? 0.5440 0.4839 0.3871 -0.2859 0.0108 -0.0065 205 VAL A CG2 1492 N N . ARG A 192 ? 0.5577 0.5050 0.3877 -0.2944 0.0093 0.0028 206 ARG A N 1493 C CA . ARG A 192 ? 0.5997 0.5513 0.4290 -0.2931 0.0079 0.0052 206 ARG A CA 1494 C C . ARG A 192 ? 0.5823 0.5523 0.4223 -0.2865 0.0066 0.0031 206 ARG A C 1495 O O . ARG A 192 ? 0.5990 0.5832 0.4446 -0.2859 0.0072 0.0000 206 ARG A O 1496 C CB . ARG A 192 ? 0.5818 0.5388 0.4000 -0.3043 0.0095 0.0069 206 ARG A CB 1497 C CG . ARG A 192 ? 0.6652 0.6040 0.4736 -0.3108 0.0106 0.0097 206 ARG A CG 1498 C CD . ARG A 192 ? 0.8387 0.7839 0.6367 -0.3217 0.0120 0.0117 206 ARG A CD 1499 N NE . ARG A 192 ? 0.9727 0.9170 0.7646 -0.3307 0.0145 0.0107 206 ARG A NE 1500 C CZ . ARG A 192 ? 1.0453 0.9725 0.8304 -0.3360 0.0156 0.0134 206 ARG A CZ 1501 N NH1 . ARG A 192 ? 1.0662 0.9757 0.8497 -0.3328 0.0142 0.0176 206 ARG A NH1 1502 N NH2 . ARG A 192 ? 1.0316 0.9593 0.8120 -0.3444 0.0180 0.0120 206 ARG A NH2 1503 N N . ILE A 193 ? 0.5597 0.5293 0.4023 -0.2818 0.0047 0.0048 207 ILE A N 1504 C CA . ILE A 193 ? 0.5287 0.5152 0.3823 -0.2753 0.0035 0.0029 207 ILE A CA 1505 C C . ILE A 193 ? 0.5543 0.5566 0.4040 -0.2815 0.0044 0.0029 207 ILE A C 1506 O O . ILE A 193 ? 0.5492 0.5448 0.3893 -0.2865 0.0044 0.0058 207 ILE A O 1507 C CB . ILE A 193 ? 0.5053 0.4817 0.3669 -0.2647 0.0007 0.0041 207 ILE A CB 1508 C CG1 . ILE A 193 ? 0.5105 0.4740 0.3782 -0.2577 -0.0001 0.0033 207 ILE A CG1 1509 C CG2 . ILE A 193 ? 0.4760 0.4696 0.3494 -0.2584 -0.0006 0.0021 207 ILE A CG2 1510 C CD1 . ILE A 193 ? 0.4719 0.4265 0.3487 -0.2467 -0.0029 0.0042 207 ILE A CD1 1511 N N . ILE A 194 ? 0.5405 0.5641 0.3978 -0.2809 0.0053 -0.0002 208 ILE A N 1512 C CA . ILE A 194 ? 0.5468 0.5883 0.4036 -0.2850 0.0064 -0.0010 208 ILE A CA 1513 C C . ILE A 194 ? 0.5521 0.6062 0.4238 -0.2755 0.0049 -0.0030 208 ILE A C 1514 O O . ILE A 194 ? 0.4667 0.5248 0.3508 -0.2674 0.0038 -0.0049 208 ILE A O 1515 C CB . ILE A 194 ? 0.5341 0.5920 0.3880 -0.2932 0.0091 -0.0031 208 ILE A CB 1516 C CG1 . ILE A 194 ? 0.4612 0.5386 0.3154 -0.2972 0.0106 -0.0044 208 ILE A CG1 1517 C CG2 . ILE A 194 ? 0.4841 0.5515 0.3494 -0.2880 0.0090 -0.0059 208 ILE A CG2 1518 C CD1 . ILE A 194 ? 0.5594 0.6521 0.4102 -0.3056 0.0132 -0.0063 208 ILE A CD1 1519 N N . ALA A 195 ? 0.5335 0.5938 0.4039 -0.2766 0.0049 -0.0027 209 ALA A N 1520 C CA . ALA A 195 ? 0.4144 0.4856 0.2991 -0.2676 0.0035 -0.0048 209 ALA A CA 1521 C C . ALA A 195 ? 0.4145 0.5048 0.2990 -0.2720 0.0054 -0.0068 209 ALA A C 1522 O O . ALA A 195 ? 0.4384 0.5278 0.3094 -0.2815 0.0068 -0.0051 209 ALA A O 1523 C CB . ALA A 195 ? 0.4672 0.5205 0.3534 -0.2606 0.0004 -0.0026 209 ALA A CB 1524 N N . SER A 196 ? 0.4538 0.5619 0.3539 -0.2651 0.0054 -0.0104 210 SER A N 1525 C CA . SER A 196 ? 0.4273 0.5373 0.3444 -0.2538 0.0034 -0.0121 210 SER A CA 1526 C C . SER A 196 ? 0.3712 0.5021 0.2981 -0.2533 0.0052 -0.0153 210 SER A C 1527 O O . SER A 196 ? 0.4008 0.5400 0.3443 -0.2441 0.0038 -0.0173 210 SER A O 1528 C CB . SER A 196 ? 0.4369 0.5481 0.3661 -0.2445 0.0011 -0.0134 210 SER A CB 1529 O OG . SER A 196 ? 0.4647 0.5966 0.4006 -0.2448 0.0028 -0.0170 210 SER A OG 1530 N N . ASP A 197 ? 0.3848 0.5238 0.3017 -0.2634 0.0080 -0.0155 211 ASP A N 1531 C CA . ASP A 197 ? 0.4258 0.5844 0.3504 -0.2642 0.0098 -0.0183 211 ASP A CA 1532 C C . ASP A 197 ? 0.4508 0.6283 0.3927 -0.2565 0.0098 -0.0219 211 ASP A C 1533 O O . ASP A 197 ? 0.3797 0.5680 0.3366 -0.2497 0.0091 -0.0237 211 ASP A O 1534 C CB . ASP A 197 ? 0.4200 0.5735 0.3479 -0.2618 0.0086 -0.0175 211 ASP A CB 1535 C CG . ASP A 197 ? 0.4898 0.6333 0.4010 -0.2722 0.0100 -0.0155 211 ASP A CG 1536 O OD1 . ASP A 197 ? 0.4801 0.6352 0.3854 -0.2805 0.0124 -0.0165 211 ASP A OD1 1537 O OD2 . ASP A 197 ? 0.5355 0.6599 0.4400 -0.2720 0.0087 -0.0132 211 ASP A OD2 1538 N N . ASN A 198 ? 0.4904 0.6718 0.4301 -0.2579 0.0107 -0.0231 212 ASN A N 1539 C CA . ASN A 198 ? 0.4684 0.6675 0.4235 -0.2513 0.0111 -0.0272 212 ASN A CA 1540 C C . ASN A 198 ? 0.4922 0.7002 0.4371 -0.2597 0.0141 -0.0289 212 ASN A C 1541 O O . ASN A 198 ? 0.5417 0.7549 0.4747 -0.2699 0.0168 -0.0285 212 ASN A O 1542 C CB . ASN A 198 ? 0.4531 0.6438 0.4208 -0.2396 0.0077 -0.0274 212 ASN A CB 1543 C CG . ASN A 198 ? 0.4816 0.6892 0.4712 -0.2293 0.0071 -0.0315 212 ASN A CG 1544 O OD1 . ASN A 198 ? 0.5582 0.7847 0.5533 -0.2310 0.0096 -0.0348 212 ASN A OD1 1545 N ND2 . ASN A 198 ? 0.4967 0.6973 0.4995 -0.2184 0.0036 -0.0314 212 ASN A ND2 1546 N N . LEU A 199 ? 0.4823 0.6928 0.4316 -0.2558 0.0136 -0.0308 213 LEU A N 1547 C CA . LEU A 199 ? 0.5025 0.7217 0.4412 -0.2642 0.0164 -0.0324 213 LEU A CA 1548 C C . LEU A 199 ? 0.4968 0.6961 0.4163 -0.2714 0.0152 -0.0275 213 LEU A C 1549 O O . LEU A 199 ? 0.4891 0.6681 0.4056 -0.2686 0.0122 -0.0235 213 LEU A O 1550 C CB . LEU A 199 ? 0.5072 0.7418 0.4605 -0.2570 0.0169 -0.0379 213 LEU A CB 1551 C CG . LEU A 199 ? 0.4857 0.7401 0.4600 -0.2485 0.0178 -0.0431 213 LEU A CG 1552 C CD1 . LEU A 199 ? 0.4790 0.7456 0.4668 -0.2411 0.0180 -0.0486 213 LEU A CD1 1553 C CD2 . LEU A 199 ? 0.4734 0.7440 0.4442 -0.2561 0.0216 -0.0448 213 LEU A CD2 1554 N N . TRP A 200 ? 0.4498 0.6547 0.3567 -0.2806 0.0173 -0.0277 214 TRP A N 1555 C CA . TRP A 200 ? 0.4436 0.6290 0.3320 -0.2878 0.0158 -0.0223 214 TRP A CA 1556 C C . TRP A 200 ? 0.4772 0.6487 0.3707 -0.2796 0.0119 -0.0209 214 TRP A C 1557 O O . TRP A 200 ? 0.5406 0.6899 0.4230 -0.2817 0.0092 -0.0155 214 TRP A O 1558 C CB . TRP A 200 ? 0.4827 0.6782 0.3569 -0.2992 0.0186 -0.0227 214 TRP A CB 1559 C CG . TRP A 200 ? 0.4661 0.6721 0.3328 -0.3085 0.0218 -0.0233 214 TRP A CG 1560 C CD1 . TRP A 200 ? 0.4487 0.6793 0.3209 -0.3109 0.0256 -0.0287 214 TRP A CD1 1561 C CD2 . TRP A 200 ? 0.4995 0.6918 0.3525 -0.3164 0.0215 -0.0186 214 TRP A CD2 1562 N NE1 . TRP A 200 ? 0.4721 0.7050 0.3346 -0.3201 0.0274 -0.0274 214 TRP A NE1 1563 C CE2 . TRP A 200 ? 0.4636 0.6735 0.3143 -0.3237 0.0250 -0.0213 214 TRP A CE2 1564 C CE3 . TRP A 200 ? 0.5045 0.6715 0.3478 -0.3177 0.0187 -0.0128 214 TRP A CE3 1565 C CZ2 . TRP A 200 ? 0.4798 0.6827 0.3188 -0.3324 0.0255 -0.0183 214 TRP A CZ2 1566 C CZ3 . TRP A 200 ? 0.5393 0.6995 0.3713 -0.3261 0.0195 -0.0101 214 TRP A CZ3 1567 C CH2 . TRP A 200 ? 0.5358 0.7139 0.3658 -0.3335 0.0228 -0.0129 214 TRP A CH2 1568 N N . GLU A 201 ? 0.4372 0.6215 0.3484 -0.2700 0.0115 -0.0260 215 GLU A N 1569 C CA . GLU A 201 ? 0.4713 0.6449 0.3905 -0.2609 0.0075 -0.0258 215 GLU A CA 1570 C C . GLU A 201 ? 0.4478 0.6222 0.3881 -0.2476 0.0053 -0.0282 215 GLU A C 1571 O O . GLU A 201 ? 0.4395 0.6301 0.3915 -0.2444 0.0074 -0.0318 215 GLU A O 1572 C CB . GLU A 201 ? 0.4831 0.6709 0.4052 -0.2609 0.0083 -0.0302 215 GLU A CB 1573 C CG . GLU A 201 ? 0.5125 0.7009 0.4133 -0.2747 0.0102 -0.0276 215 GLU A CG 1574 C CD . GLU A 201 ? 0.5685 0.7309 0.4534 -0.2788 0.0064 -0.0201 215 GLU A CD 1575 O OE1 . GLU A 201 ? 0.6262 0.7699 0.5162 -0.2712 0.0027 -0.0173 215 GLU A OE1 1576 O OE2 . GLU A 201 ? 0.5765 0.7370 0.4441 -0.2896 0.0071 -0.0170 215 GLU A OE2 1577 N N . PRO A 202 ? 0.4127 0.5699 0.3581 -0.2396 0.0010 -0.0260 216 PRO A N 1578 C CA . PRO A 202 ? 0.4409 0.5795 0.3743 -0.2421 -0.0019 -0.0220 216 PRO A CA 1579 C C . PRO A 202 ? 0.4544 0.5692 0.3703 -0.2485 -0.0029 -0.0150 216 PRO A C 1580 O O . PRO A 202 ? 0.5194 0.6171 0.4272 -0.2490 -0.0059 -0.0112 216 PRO A O 1581 C CB . PRO A 202 ? 0.4014 0.5346 0.3523 -0.2286 -0.0062 -0.0240 216 PRO A CB 1582 C CG . PRO A 202 ? 0.4444 0.5816 0.4103 -0.2206 -0.0062 -0.0254 216 PRO A CG 1583 C CD . PRO A 202 ? 0.3945 0.5514 0.3599 -0.2266 -0.0016 -0.0279 216 PRO A CD 1584 N N . ILE A 203 ? 0.4540 0.5674 0.3643 -0.2531 -0.0008 -0.0133 217 ILE A N 1585 C CA . ILE A 203 ? 0.4418 0.5319 0.3370 -0.2580 -0.0019 -0.0074 217 ILE A CA 1586 C C . ILE A 203 ? 0.4976 0.5776 0.3730 -0.2685 -0.0020 -0.0029 217 ILE A C 1587 O O . ILE A 203 ? 0.5527 0.6106 0.4201 -0.2680 -0.0049 0.0019 217 ILE A O 1588 C CB . ILE A 203 ? 0.4829 0.5738 0.3753 -0.2616 0.0004 -0.0071 217 ILE A CB 1589 C CG1 . ILE A 203 ? 0.4375 0.5031 0.3194 -0.2630 -0.0013 -0.0021 217 ILE A CG1 1590 C CG2 . ILE A 203 ? 0.4783 0.5842 0.3605 -0.2731 0.0043 -0.0080 217 ILE A CG2 1591 C CD1 . ILE A 203 ? 0.4033 0.4539 0.2954 -0.2516 -0.0048 -0.0014 217 ILE A CD1 1592 N N . SER A 204 ? 0.4921 0.5887 0.3605 -0.2773 0.0011 -0.0045 218 SER A N 1593 C CA . SER A 204 ? 0.5155 0.6048 0.3643 -0.2885 0.0012 0.0000 218 SER A CA 1594 C C . SER A 204 ? 0.5194 0.5965 0.3646 -0.2865 -0.0026 0.0030 218 SER A C 1595 O O . SER A 204 ? 0.5523 0.6084 0.3837 -0.2906 -0.0050 0.0094 218 SER A O 1596 C CB . SER A 204 ? 0.5056 0.6183 0.3495 -0.2977 0.0053 -0.0032 218 SER A CB 1597 O OG . SER A 204 ? 0.5126 0.6323 0.3553 -0.3018 0.0083 -0.0043 218 SER A OG 1598 N N . SER A 205 ? 0.5202 0.6097 0.3781 -0.2799 -0.0035 -0.0015 219 SER A N 1599 C CA . SER A 205 ? 0.5591 0.6372 0.4141 -0.2778 -0.0077 0.0010 219 SER A CA 1600 C C . SER A 205 ? 0.5899 0.6434 0.4499 -0.2682 -0.0122 0.0044 219 SER A C 1601 O O . SER A 205 ? 0.5920 0.6272 0.4434 -0.2687 -0.0160 0.0095 219 SER A O 1602 C CB . SER A 205 ? 0.5850 0.6843 0.4528 -0.2732 -0.0076 -0.0059 219 SER A CB 1603 O OG . SER A 205 ? 0.6277 0.7379 0.5174 -0.2613 -0.0073 -0.0121 219 SER A OG 1604 N N . SER A 206 ? 0.5994 0.6528 0.4732 -0.2595 -0.0119 0.0017 220 SER A N 1605 C CA . SER A 206 ? 0.5699 0.6011 0.4484 -0.2506 -0.0154 0.0045 220 SER A CA 1606 C C . SER A 206 ? 0.4994 0.5069 0.3608 -0.2565 -0.0162 0.0116 220 SER A C 1607 O O . SER A 206 ? 0.5007 0.4872 0.3598 -0.2519 -0.0199 0.0156 220 SER A O 1608 C CB . SER A 206 ? 0.5724 0.6099 0.4670 -0.2422 -0.0143 0.0007 220 SER A CB 1609 O OG . SER A 206 ? 0.4857 0.5414 0.3986 -0.2341 -0.0147 -0.0054 220 SER A OG 1610 N N . LEU A 207 ? 0.4686 0.4796 0.3190 -0.2660 -0.0128 0.0129 221 LEU A N 1611 C CA . LEU A 207 ? 0.5828 0.5730 0.4179 -0.2719 -0.0133 0.0190 221 LEU A CA 1612 C C . LEU A 207 ? 0.6338 0.6127 0.4543 -0.2780 -0.0158 0.0249 221 LEU A C 1613 O O . LEU A 207 ? 0.6647 0.6230 0.4753 -0.2799 -0.0173 0.0305 221 LEU A O 1614 C CB . LEU A 207 ? 0.5995 0.5980 0.4272 -0.2809 -0.0092 0.0183 221 LEU A CB 1615 C CG . LEU A 207 ? 0.6578 0.6626 0.4960 -0.2766 -0.0070 0.0143 221 LEU A CG 1616 C CD1 . LEU A 207 ? 0.6784 0.6885 0.5065 -0.2869 -0.0037 0.0146 221 LEU A CD1 1617 C CD2 . LEU A 207 ? 0.6623 0.6469 0.5060 -0.2678 -0.0093 0.0158 221 LEU A CD2 1618 N N . LEU A 208 ? 0.6160 0.6085 0.4355 -0.2810 -0.0163 0.0236 222 LEU A N 1619 C CA . LEU A 208 ? 0.6391 0.6223 0.4435 -0.2880 -0.0189 0.0297 222 LEU A CA 1620 C C . LEU A 208 ? 0.6412 0.6096 0.4505 -0.2793 -0.0242 0.0319 222 LEU A C 1621 O O . LEU A 208 ? 0.6897 0.6416 0.4877 -0.2818 -0.0276 0.0386 222 LEU A O 1622 C CB . LEU A 208 ? 0.6486 0.6555 0.4474 -0.2974 -0.0164 0.0273 222 LEU A CB 1623 C CG . LEU A 208 ? 0.6708 0.6924 0.4609 -0.3083 -0.0116 0.0262 222 LEU A CG 1624 C CD1 . LEU A 208 ? 0.6809 0.7278 0.4682 -0.3156 -0.0092 0.0227 222 LEU A CD1 1625 C CD2 . LEU A 208 ? 0.6669 0.6696 0.4403 -0.3160 -0.0124 0.0338 222 LEU A CD2 1626 N N . LEU A 209 ? 0.6190 0.5934 0.4463 -0.2683 -0.0251 0.0262 223 LEU A N 1627 C CA . LEU A 209 ? 0.6478 0.6118 0.4827 -0.2590 -0.0302 0.0266 223 LEU A CA 1628 C C . LEU A 209 ? 0.6757 0.6171 0.5168 -0.2486 -0.0324 0.0289 223 LEU A C 1629 O O . LEU A 209 ? 0.6339 0.5616 0.4792 -0.2407 -0.0370 0.0308 223 LEU A O 1630 C CB . LEU A 209 ? 0.6890 0.6750 0.5421 -0.2521 -0.0301 0.0181 223 LEU A CB 1631 C CG . LEU A 209 ? 0.7501 0.7605 0.6018 -0.2590 -0.0286 0.0138 223 LEU A CG 1632 C CD1 . LEU A 209 ? 0.7513 0.7847 0.6245 -0.2501 -0.0271 0.0041 223 LEU A CD1 1633 C CD2 . LEU A 209 ? 0.7181 0.7205 0.5616 -0.2611 -0.0338 0.0171 223 LEU A CD2 1634 N N . ASP A 210 ? 0.6594 0.5981 0.5017 -0.2483 -0.0291 0.0283 224 ASP A N 1635 C CA . ASP A 210 ? 0.6498 0.5717 0.5002 -0.2383 -0.0301 0.0288 224 ASP A CA 1636 C C . ASP A 210 ? 0.6604 0.5692 0.4997 -0.2438 -0.0278 0.0328 224 ASP A C 1637 O O . ASP A 210 ? 0.6435 0.5619 0.4815 -0.2490 -0.0240 0.0304 224 ASP A O 1638 C CB . ASP A 210 ? 0.6835 0.6192 0.5518 -0.2304 -0.0282 0.0220 224 ASP A CB 1639 C CG . ASP A 210 ? 0.6916 0.6124 0.5690 -0.2201 -0.0289 0.0220 224 ASP A CG 1640 O OD1 . ASP A 210 ? 0.6690 0.5701 0.5390 -0.2198 -0.0296 0.0265 224 ASP A OD1 1641 O OD2 . ASP A 210 ? 0.6733 0.6033 0.5663 -0.2121 -0.0284 0.0172 224 ASP A OD2 1642 N N . GLN A 211 ? 0.6650 0.5524 0.4971 -0.2425 -0.0304 0.0386 225 GLN A N 1643 C CA . GLN A 211 ? 0.6814 0.5556 0.5044 -0.2472 -0.0285 0.0424 225 GLN A CA 1644 C C . GLN A 211 ? 0.6353 0.5063 0.4683 -0.2412 -0.0258 0.0387 225 GLN A C 1645 O O . GLN A 211 ? 0.5543 0.4249 0.3821 -0.2473 -0.0226 0.0387 225 GLN A O 1646 C CB . GLN A 211 ? 0.7052 0.5580 0.5216 -0.2450 -0.0319 0.0492 225 GLN A CB 1647 C CG . GLN A 211 ? 0.7880 0.6272 0.5965 -0.2497 -0.0300 0.0534 225 GLN A CG 1648 C CD . GLN A 211 ? 0.8761 0.6949 0.6809 -0.2461 -0.0332 0.0601 225 GLN A CD 1649 O OE1 . GLN A 211 ? 0.9194 0.7344 0.7261 -0.2406 -0.0374 0.0621 225 GLN A OE1 1650 N NE2 . GLN A 211 ? 0.9230 0.7290 0.7237 -0.2488 -0.0314 0.0637 225 GLN A NE2 1651 N N . GLU A 212 ? 0.6192 0.4881 0.4664 -0.2296 -0.0271 0.0356 226 GLU A N 1652 C CA . GLU A 212 ? 0.6848 0.5511 0.5413 -0.2240 -0.0246 0.0323 226 GLU A CA 1653 C C . GLU A 212 ? 0.6442 0.5294 0.5026 -0.2293 -0.0213 0.0277 226 GLU A C 1654 O O . GLU A 212 ? 0.6484 0.5320 0.5065 -0.2313 -0.0185 0.0264 226 GLU A O 1655 C CB . GLU A 212 ? 0.7560 0.6178 0.6279 -0.2104 -0.0267 0.0300 226 GLU A CB 1656 C CG . GLU A 212 ? 0.8535 0.6953 0.7255 -0.2037 -0.0293 0.0343 226 GLU A CG 1657 C CD . GLU A 212 ? 0.9781 0.8045 0.8420 -0.2078 -0.0274 0.0382 226 GLU A CD 1658 O OE1 . GLU A 212 ? 1.0237 0.8501 0.8898 -0.2092 -0.0240 0.0359 226 GLU A OE1 1659 O OE2 . GLU A 212 ? 1.0246 0.8392 0.8804 -0.2098 -0.0294 0.0437 226 GLU A OE2 1660 N N . LEU A 213 ? 0.5501 0.4539 0.4108 -0.2316 -0.0214 0.0251 227 LEU A N 1661 C CA . LEU A 213 ? 0.5190 0.4428 0.3824 -0.2362 -0.0182 0.0208 227 LEU A CA 1662 C C . LEU A 213 ? 0.5674 0.4934 0.4161 -0.2488 -0.0154 0.0228 227 LEU A C 1663 O O . LEU A 213 ? 0.5711 0.5036 0.4193 -0.2528 -0.0125 0.0206 227 LEU A O 1664 C CB . LEU A 213 ? 0.4750 0.4188 0.3466 -0.2347 -0.0188 0.0173 227 LEU A CB 1665 C CG . LEU A 213 ? 0.5415 0.5079 0.4199 -0.2370 -0.0157 0.0124 227 LEU A CG 1666 C CD1 . LEU A 213 ? 0.4602 0.4253 0.3498 -0.2298 -0.0150 0.0099 227 LEU A CD1 1667 C CD2 . LEU A 213 ? 0.5966 0.5826 0.4851 -0.2343 -0.0163 0.0087 227 LEU A CD2 1668 N N . TRP A 214 ? 0.5816 0.5021 0.4180 -0.2554 -0.0166 0.0272 228 TRP A N 1669 C CA . TRP A 214 ? 0.5836 0.5047 0.4055 -0.2675 -0.0143 0.0298 228 TRP A CA 1670 C C . TRP A 214 ? 0.5428 0.4496 0.3618 -0.2686 -0.0127 0.0310 228 TRP A C 1671 O O . TRP A 214 ? 0.5485 0.4614 0.3615 -0.2769 -0.0097 0.0303 228 TRP A O 1672 C CB . TRP A 214 ? 0.6514 0.5648 0.4610 -0.2730 -0.0167 0.0355 228 TRP A CB 1673 C CG . TRP A 214 ? 0.6762 0.5936 0.4713 -0.2860 -0.0144 0.0381 228 TRP A CG 1674 C CD1 . TRP A 214 ? 0.6933 0.6302 0.4824 -0.2948 -0.0127 0.0368 228 TRP A CD1 1675 C CD2 . TRP A 214 ? 0.7046 0.6069 0.4904 -0.2915 -0.0135 0.0424 228 TRP A CD2 1676 N NE1 . TRP A 214 ? 0.6693 0.6040 0.4456 -0.3055 -0.0109 0.0401 228 TRP A NE1 1677 C CE2 . TRP A 214 ? 0.6748 0.5881 0.4490 -0.3037 -0.0114 0.0437 228 TRP A CE2 1678 C CE3 . TRP A 214 ? 0.7198 0.6013 0.5072 -0.2871 -0.0138 0.0448 228 TRP A CE3 1679 C CZ2 . TRP A 214 ? 0.7363 0.6395 0.5004 -0.3117 -0.0101 0.0478 228 TRP A CZ2 1680 C CZ3 . TRP A 214 ? 0.7909 0.6628 0.5689 -0.2949 -0.0122 0.0486 228 TRP A CZ3 1681 C CH2 . TRP A 214 ? 0.7882 0.6705 0.5545 -0.3071 -0.0105 0.0503 228 TRP A CH2 1682 N N . LYS A 215 ? 0.5873 0.4759 0.4116 -0.2602 -0.0144 0.0326 229 LYS A N 1683 C CA . LYS A 215 ? 0.6695 0.5449 0.4923 -0.2612 -0.0124 0.0333 229 LYS A CA 1684 C C . LYS A 215 ? 0.6269 0.5128 0.4562 -0.2611 -0.0095 0.0280 229 LYS A C 1685 O O . LYS A 215 ? 0.6306 0.5139 0.4544 -0.2676 -0.0070 0.0279 229 LYS A O 1686 C CB . LYS A 215 ? 0.7339 0.5886 0.5621 -0.2520 -0.0143 0.0358 229 LYS A CB 1687 C CG . LYS A 215 ? 0.8096 0.6519 0.6303 -0.2527 -0.0173 0.0420 229 LYS A CG 1688 C CD . LYS A 215 ? 0.8649 0.6882 0.6931 -0.2424 -0.0190 0.0443 229 LYS A CD 1689 C CE . LYS A 215 ? 0.9280 0.7406 0.7491 -0.2427 -0.0225 0.0507 229 LYS A CE 1690 N NZ . LYS A 215 ? 0.9590 0.7541 0.7882 -0.2322 -0.0241 0.0532 229 LYS A NZ 1691 N N . VAL A 216 ? 0.5457 0.4440 0.3866 -0.2541 -0.0100 0.0238 230 VAL A N 1692 C CA . VAL A 216 ? 0.5029 0.4101 0.3511 -0.2525 -0.0079 0.0192 230 VAL A CA 1693 C C . VAL A 216 ? 0.5704 0.4985 0.4160 -0.2604 -0.0055 0.0164 230 VAL A C 1694 O O . VAL A 216 ? 0.6069 0.5421 0.4561 -0.2611 -0.0037 0.0134 230 VAL A O 1695 C CB . VAL A 216 ? 0.5155 0.4247 0.3790 -0.2405 -0.0096 0.0164 230 VAL A CB 1696 C CG1 . VAL A 216 ? 0.5434 0.4322 0.4099 -0.2326 -0.0115 0.0189 230 VAL A CG1 1697 C CG2 . VAL A 216 ? 0.4770 0.4011 0.3469 -0.2372 -0.0113 0.0150 230 VAL A CG2 1698 N N . VAL A 217 ? 0.5826 0.5210 0.4216 -0.2668 -0.0054 0.0175 231 VAL A N 1699 C CA . VAL A 217 ? 0.5588 0.5188 0.3966 -0.2737 -0.0029 0.0146 231 VAL A CA 1700 C C . VAL A 217 ? 0.6408 0.5990 0.4641 -0.2859 -0.0008 0.0169 231 VAL A C 1701 O O . VAL A 217 ? 0.6428 0.5957 0.4564 -0.2912 -0.0015 0.0206 231 VAL A O 1702 C CB . VAL A 217 ? 0.5209 0.4982 0.3636 -0.2723 -0.0036 0.0131 231 VAL A CB 1703 C CG1 . VAL A 217 ? 0.5136 0.5141 0.3553 -0.2797 -0.0006 0.0100 231 VAL A CG1 1704 C CG2 . VAL A 217 ? 0.4957 0.4759 0.3544 -0.2601 -0.0057 0.0105 231 VAL A CG2 1705 N N . ASP A 218 ? 0.6581 0.6210 0.4798 -0.2908 0.0017 0.0148 232 ASP A N 1706 C CA . ASP A 218 ? 0.6666 0.6264 0.4755 -0.3022 0.0036 0.0170 232 ASP A CA 1707 C C . ASP A 218 ? 0.6514 0.6324 0.4559 -0.3104 0.0055 0.0155 232 ASP A C 1708 O O . ASP A 218 ? 0.6817 0.6614 0.4748 -0.3197 0.0064 0.0183 232 ASP A O 1709 C CB . ASP A 218 ? 0.6730 0.6251 0.4812 -0.3043 0.0054 0.0158 232 ASP A CB 1710 C CG . ASP A 218 ? 0.7222 0.6554 0.5363 -0.2956 0.0040 0.0164 232 ASP A CG 1711 O OD1 . ASP A 218 ? 0.7832 0.6977 0.5923 -0.2957 0.0031 0.0203 232 ASP A OD1 1712 O OD2 . ASP A 218 ? 0.7006 0.6381 0.5249 -0.2884 0.0037 0.0130 232 ASP A OD2 1713 N N . VAL A 219 ? 0.5951 0.5962 0.4096 -0.3068 0.0062 0.0112 233 VAL A N 1714 C CA . VAL A 219 ? 0.5782 0.6015 0.3908 -0.3139 0.0085 0.0089 233 VAL A CA 1715 C C . VAL A 219 ? 0.5813 0.6230 0.4054 -0.3075 0.0081 0.0057 233 VAL A C 1716 O O . VAL A 219 ? 0.4971 0.5411 0.3343 -0.2977 0.0069 0.0035 233 VAL A O 1717 C CB . VAL A 219 ? 0.5749 0.6075 0.3882 -0.3185 0.0109 0.0061 233 VAL A CB 1718 C CG1 . VAL A 219 ? 0.5414 0.5977 0.3538 -0.3252 0.0132 0.0036 233 VAL A CG1 1719 C CG2 . VAL A 219 ? 0.5872 0.6025 0.3897 -0.3255 0.0116 0.0087 233 VAL A CG2 1720 N N . ILE A 220 ? 0.5787 0.6338 0.3987 -0.3128 0.0092 0.0055 234 ILE A N 1721 C CA . ILE A 220 ? 0.5802 0.6557 0.4124 -0.3073 0.0096 0.0016 234 ILE A CA 1722 C C . ILE A 220 ? 0.5276 0.6251 0.3647 -0.3106 0.0125 -0.0025 234 ILE A C 1723 O O . ILE A 220 ? 0.5424 0.6487 0.3705 -0.3203 0.0148 -0.0026 234 ILE A O 1724 C CB . ILE A 220 ? 0.5502 0.6309 0.3772 -0.3103 0.0094 0.0025 234 ILE A CB 1725 C CG1 . ILE A 220 ? 0.5710 0.6293 0.3928 -0.3072 0.0060 0.0071 234 ILE A CG1 1726 C CG2 . ILE A 220 ? 0.4626 0.5650 0.3045 -0.3037 0.0101 -0.0025 234 ILE A CG2 1727 C CD1 . ILE A 220 ? 0.6221 0.6837 0.4363 -0.3116 0.0054 0.0089 234 ILE A CD1 1728 N N . GLY A 221 ? 0.4784 0.5845 0.3301 -0.3025 0.0123 -0.0057 235 GLY A N 1729 C CA . GLY A 221 ? 0.4660 0.5924 0.3238 -0.3046 0.0147 -0.0092 235 GLY A CA 1730 C C . GLY A 221 ? 0.5003 0.6477 0.3726 -0.2981 0.0153 -0.0132 235 GLY A C 1731 O O . GLY A 221 ? 0.5204 0.6672 0.4062 -0.2875 0.0133 -0.0143 235 GLY A O 1732 N N . ALA A 222 ? 0.4974 0.6634 0.3680 -0.3043 0.0181 -0.0156 236 ALA A N 1733 C CA . ALA A 222 ? 0.5152 0.7022 0.4000 -0.2986 0.0192 -0.0200 236 ALA A CA 1734 C C . ALA A 222 ? 0.4733 0.6805 0.3668 -0.2993 0.0214 -0.0235 236 ALA A C 1735 O O . ALA A 222 ? 0.4383 0.6464 0.3227 -0.3077 0.0228 -0.0226 236 ALA A O 1736 C CB . ALA A 222 ? 0.5378 0.7311 0.4147 -0.3042 0.0208 -0.0207 236 ALA A CB 1737 N N . HIS A 223 ? 0.4734 0.6966 0.3849 -0.2904 0.0215 -0.0273 237 HIS A N 1738 C CA . HIS A 223 ? 0.5080 0.7503 0.4301 -0.2895 0.0231 -0.0304 237 HIS A CA 1739 C C . HIS A 223 ? 0.5019 0.7667 0.4280 -0.2924 0.0264 -0.0348 237 HIS A C 1740 O O . HIS A 223 ? 0.4976 0.7688 0.4297 -0.2882 0.0269 -0.0374 237 HIS A O 1741 C CB . HIS A 223 ? 0.4744 0.7187 0.4157 -0.2769 0.0206 -0.0313 237 HIS A CB 1742 C CG . HIS A 223 ? 0.4982 0.7253 0.4367 -0.2751 0.0180 -0.0278 237 HIS A CG 1743 N ND1 . HIS A 223 ? 0.4868 0.7149 0.4402 -0.2656 0.0156 -0.0279 237 HIS A ND1 1744 C CD2 . HIS A 223 ? 0.5123 0.7213 0.4350 -0.2818 0.0175 -0.0243 237 HIS A CD2 1745 C CE1 . HIS A 223 ? 0.5000 0.7121 0.4464 -0.2667 0.0140 -0.0249 237 HIS A CE1 1746 N NE2 . HIS A 223 ? 0.5129 0.7129 0.4410 -0.2762 0.0151 -0.0228 237 HIS A NE2 1747 N N . TYR A 224 ? 0.5123 0.7893 0.4356 -0.2995 0.0287 -0.0359 238 TYR A N 1748 C CA . TYR A 224 ? 0.4865 0.7863 0.4147 -0.3022 0.0321 -0.0404 238 TYR A CA 1749 C C . TYR A 224 ? 0.4904 0.7930 0.4111 -0.3058 0.0339 -0.0422 238 TYR A C 1750 O O . TYR A 224 ? 0.4476 0.7643 0.3803 -0.2999 0.0351 -0.0468 238 TYR A O 1751 C CB . TYR A 224 ? 0.4881 0.8035 0.4394 -0.2910 0.0318 -0.0441 238 TYR A CB 1752 C CG . TYR A 224 ? 0.4968 0.8100 0.4548 -0.2881 0.0297 -0.0420 238 TYR A CG 1753 C CD1 . TYR A 224 ? 0.4912 0.8161 0.4484 -0.2942 0.0314 -0.0425 238 TYR A CD1 1754 C CD2 . TYR A 224 ? 0.4142 0.7134 0.3783 -0.2799 0.0262 -0.0393 238 TYR A CD2 1755 C CE1 . TYR A 224 ? 0.4947 0.8181 0.4571 -0.2924 0.0295 -0.0405 238 TYR A CE1 1756 C CE2 . TYR A 224 ? 0.4568 0.7544 0.4258 -0.2780 0.0244 -0.0374 238 TYR A CE2 1757 C CZ . TYR A 224 ? 0.4716 0.7816 0.4395 -0.2844 0.0261 -0.0380 238 TYR A CZ 1758 O OH . TYR A 224 ? 0.4909 0.8005 0.4631 -0.2834 0.0243 -0.0362 238 TYR A OH 1759 N N . PRO A 225 ? 0.5265 0.8155 0.4274 -0.3156 0.0339 -0.0385 239 PRO A N 1760 C CA . PRO A 225 ? 0.5790 0.8672 0.4713 -0.3190 0.0347 -0.0390 239 PRO A CA 1761 C C . PRO A 225 ? 0.5671 0.8749 0.4544 -0.3275 0.0386 -0.0427 239 PRO A C 1762 O O . PRO A 225 ? 0.5476 0.8564 0.4256 -0.3323 0.0396 -0.0431 239 PRO A O 1763 C CB . PRO A 225 ? 0.5937 0.8580 0.4668 -0.3265 0.0327 -0.0326 239 PRO A CB 1764 C CG . PRO A 225 ? 0.5839 0.8468 0.4510 -0.3333 0.0332 -0.0309 239 PRO A CG 1765 C CD . PRO A 225 ? 0.5705 0.8450 0.4561 -0.3245 0.0331 -0.0339 239 PRO A CD 1766 N N . GLY A 226 ? 0.5352 0.8584 0.4284 -0.3296 0.0408 -0.0453 240 GLY A N 1767 C CA . GLY A 226 ? 0.5275 0.8708 0.4179 -0.3370 0.0447 -0.0494 240 GLY A CA 1768 C C . GLY A 226 ? 0.5735 0.9098 0.4421 -0.3504 0.0454 -0.0462 240 GLY A C 1769 O O . GLY A 226 ? 0.6157 0.9637 0.4795 -0.3552 0.0478 -0.0490 240 GLY A O 1770 N N . THR A 227 ? 0.5718 0.8890 0.4278 -0.3561 0.0432 -0.0402 241 THR A N 1771 C CA . THR A 227 ? 0.5513 0.8586 0.3869 -0.3690 0.0433 -0.0360 241 THR A CA 1772 C C . THR A 227 ? 0.5852 0.8793 0.4094 -0.3710 0.0417 -0.0328 241 THR A C 1773 O O . THR A 227 ? 0.6173 0.9002 0.4250 -0.3809 0.0410 -0.0281 241 THR A O 1774 C CB . THR A 227 ? 0.6325 0.9591 0.4638 -0.3790 0.0469 -0.0388 241 THR A CB 1775 O OG1 . THR A 227 ? 0.6083 0.9533 0.4427 -0.3790 0.0496 -0.0438 241 THR A OG1 1776 C CG2 . THR A 227 ? 0.5790 0.9184 0.4222 -0.3767 0.0483 -0.0416 241 THR A CG2 1777 N N . TYR A 228 ? 0.5638 0.8584 0.3976 -0.3613 0.0407 -0.0348 242 TYR A N 1778 C CA . TYR A 228 ? 0.6150 0.8991 0.4395 -0.3626 0.0391 -0.0322 242 TYR A CA 1779 C C . TYR A 228 ? 0.6115 0.8730 0.4381 -0.3544 0.0352 -0.0280 242 TYR A C 1780 O O . TYR A 228 ? 0.6567 0.9160 0.4970 -0.3447 0.0341 -0.0293 242 TYR A O 1781 C CB . TYR A 228 ? 0.6346 0.9399 0.4667 -0.3597 0.0417 -0.0386 242 TYR A CB 1782 C CG . TYR A 228 ? 0.6954 1.0216 0.5226 -0.3691 0.0455 -0.0423 242 TYR A CG 1783 C CD1 . TYR A 228 ? 0.7767 1.0987 0.5853 -0.3815 0.0455 -0.0385 242 TYR A CD1 1784 C CD2 . TYR A 228 ? 0.7150 1.0647 0.5567 -0.3654 0.0490 -0.0495 242 TYR A CD2 1785 C CE1 . TYR A 228 ? 0.7901 1.1316 0.5945 -0.3902 0.0490 -0.0420 242 TYR A CE1 1786 C CE2 . TYR A 228 ? 0.7399 1.1087 0.5776 -0.3738 0.0526 -0.0532 242 TYR A CE2 1787 C CZ . TYR A 228 ? 0.7826 1.1477 0.6016 -0.3863 0.0526 -0.0496 242 TYR A CZ 1788 O OH . TYR A 228 ? 0.8247 1.2093 0.6404 -0.3946 0.0562 -0.0533 242 TYR A OH 1789 N N . THR A 229 ? 0.5505 0.7952 0.3637 -0.3585 0.0328 -0.0229 243 THR A N 1790 C CA . THR A 229 ? 0.5046 0.7290 0.3200 -0.3506 0.0291 -0.0193 243 THR A CA 1791 C C . THR A 229 ? 0.6002 0.8304 0.4159 -0.3487 0.0289 -0.0209 243 THR A C 1792 O O . THR A 229 ? 0.6108 0.8633 0.4295 -0.3510 0.0320 -0.0263 243 THR A O 1793 C CB . THR A 229 ? 0.5577 0.7545 0.3584 -0.3558 0.0260 -0.0115 243 THR A CB 1794 O OG1 . THR A 229 ? 0.5769 0.7543 0.3819 -0.3469 0.0225 -0.0087 243 THR A OG1 1795 C CG2 . THR A 229 ? 0.5423 0.7339 0.3246 -0.3675 0.0257 -0.0070 243 THR A CG2 1796 N N . VAL A 230 ? 0.5750 0.7865 0.3887 -0.3443 0.0252 -0.0169 244 VAL A N 1797 C CA . VAL A 230 ? 0.5874 0.8036 0.4017 -0.3424 0.0246 -0.0182 244 VAL A CA 1798 C C . VAL A 230 ? 0.6481 0.8398 0.4455 -0.3478 0.0207 -0.0098 244 VAL A C 1799 O O . VAL A 230 ? 0.6392 0.8095 0.4292 -0.3495 0.0184 -0.0039 244 VAL A O 1800 C CB . VAL A 230 ? 0.6286 0.8470 0.4628 -0.3281 0.0233 -0.0224 244 VAL A CB 1801 C CG1 . VAL A 230 ? 0.6384 0.8791 0.4919 -0.3207 0.0265 -0.0302 244 VAL A CG1 1802 C CG2 . VAL A 230 ? 0.5713 0.7635 0.4074 -0.3213 0.0189 -0.0171 244 VAL A CG2 1803 N N . TRP A 231 ? 0.6648 0.8595 0.4572 -0.3499 0.0198 -0.0093 245 TRP A N 1804 C CA . TRP A 231 ? 0.6590 0.8328 0.4337 -0.3567 0.0161 -0.0008 245 TRP A CA 1805 C C . TRP A 231 ? 0.5763 0.7204 0.3513 -0.3499 0.0113 0.0054 245 TRP A C 1806 O O . TRP A 231 ? 0.6158 0.7388 0.3782 -0.3548 0.0090 0.0127 245 TRP A O 1807 C CB . TRP A 231 ? 0.6917 0.8764 0.4614 -0.3602 0.0160 -0.0016 245 TRP A CB 1808 C CG . TRP A 231 ? 0.7056 0.8739 0.4555 -0.3698 0.0130 0.0074 245 TRP A CG 1809 C CD1 . TRP A 231 ? 0.7591 0.9287 0.4948 -0.3812 0.0141 0.0111 245 TRP A CD1 1810 C CD2 . TRP A 231 ? 0.6803 0.8272 0.4234 -0.3681 0.0080 0.0146 245 TRP A CD2 1811 N NE1 . TRP A 231 ? 0.7868 0.9372 0.5077 -0.3862 0.0102 0.0204 245 TRP A NE1 1812 C CE2 . TRP A 231 ? 0.7268 0.8627 0.4514 -0.3784 0.0063 0.0228 245 TRP A CE2 1813 C CE3 . TRP A 231 ? 0.6875 0.8230 0.4391 -0.3585 0.0045 0.0150 245 TRP A CE3 1814 C CZ2 . TRP A 231 ? 0.7487 0.8628 0.4631 -0.3788 0.0014 0.0317 245 TRP A CZ2 1815 C CZ3 . TRP A 231 ? 0.7674 0.8812 0.5082 -0.3597 -0.0006 0.0235 245 TRP A CZ3 1816 C CH2 . TRP A 231 ? 0.7579 0.8610 0.4799 -0.3696 -0.0020 0.0320 245 TRP A CH2 1817 N N . ASN A 232 ? 0.5062 0.6488 0.2968 -0.3381 0.0098 0.0022 246 ASN A N 1818 C CA . ASN A 232 ? 0.5094 0.6253 0.3027 -0.3301 0.0054 0.0069 246 ASN A CA 1819 C C . ASN A 232 ? 0.5969 0.6975 0.3870 -0.3308 0.0054 0.0101 246 ASN A C 1820 O O . ASN A 232 ? 0.6166 0.6920 0.4016 -0.3287 0.0020 0.0159 246 ASN A O 1821 C CB . ASN A 232 ? 0.4769 0.5979 0.2910 -0.3165 0.0042 0.0015 246 ASN A CB 1822 C CG . ASN A 232 ? 0.5696 0.6961 0.3865 -0.3142 0.0022 -0.0002 246 ASN A CG 1823 O OD1 . ASN A 232 ? 0.5746 0.6974 0.3764 -0.3227 0.0010 0.0042 246 ASN A OD1 1824 N ND2 . ASN A 232 ? 0.5007 0.6357 0.3375 -0.3022 0.0013 -0.0064 246 ASN A ND2 1825 N N . ALA A 233 ? 0.5763 0.6924 0.3697 -0.3337 0.0092 0.0060 247 ALA A N 1826 C CA . ALA A 233 ? 0.6295 0.7344 0.4211 -0.3347 0.0095 0.0078 247 ALA A CA 1827 C C . ALA A 233 ? 0.6446 0.7356 0.4179 -0.3457 0.0090 0.0142 247 ALA A C 1828 O O . ALA A 233 ? 0.6010 0.6701 0.3699 -0.3449 0.0071 0.0186 247 ALA A O 1829 C CB . ALA A 233 ? 0.5706 0.6972 0.3721 -0.3342 0.0134 0.0015 247 ALA A CB 1830 N N . LYS A 234 ? 0.6541 0.7586 0.4176 -0.3556 0.0108 0.0143 248 LYS A N 1831 C CA . LYS A 234 ? 0.6876 0.7798 0.4343 -0.3660 0.0100 0.0209 248 LYS A CA 1832 C C . LYS A 234 ? 0.6524 0.7182 0.3920 -0.3636 0.0055 0.0284 248 LYS A C 1833 O O . LYS A 234 ? 0.6512 0.6963 0.3833 -0.3660 0.0040 0.0342 248 LYS A O 1834 C CB . LYS A 234 ? 0.7529 0.8654 0.4914 -0.3760 0.0124 0.0198 248 LYS A CB 1835 C CG . LYS A 234 ? 0.8174 0.9587 0.5642 -0.3777 0.0170 0.0117 248 LYS A CG 1836 C CD . LYS A 234 ? 0.9153 1.0746 0.6526 -0.3883 0.0192 0.0110 248 LYS A CD 1837 C CE . LYS A 234 ? 0.9598 1.1496 0.7068 -0.3887 0.0239 0.0021 248 LYS A CE 1838 N NZ . LYS A 234 ? 0.9811 1.1774 0.7254 -0.3958 0.0265 0.0013 248 LYS A NZ 1839 N N . MET A 235 ? 0.6687 0.7356 0.4117 -0.3585 0.0034 0.0282 249 MET A N 1840 C CA . MET A 235 ? 0.7431 0.7860 0.4805 -0.3553 -0.0014 0.0353 249 MET A CA 1841 C C . MET A 235 ? 0.8137 0.8321 0.5567 -0.3466 -0.0037 0.0376 249 MET A C 1842 O O . MET A 235 ? 0.8438 0.8391 0.5801 -0.3455 -0.0072 0.0445 249 MET A O 1843 C CB . MET A 235 ? 0.6894 0.7400 0.4317 -0.3506 -0.0032 0.0334 249 MET A CB 1844 C CG . MET A 235 ? 0.7662 0.8348 0.4990 -0.3600 -0.0018 0.0335 249 MET A CG 1845 S SD . MET A 235 ? 1.0760 1.1251 0.7884 -0.3695 -0.0049 0.0449 249 MET A SD 1846 C CE . MET A 235 ? 0.6507 0.6757 0.3641 -0.3604 -0.0111 0.0508 249 MET A CE 1847 N N . SER A 236 ? 0.7713 0.7952 0.5270 -0.3399 -0.0019 0.0319 250 SER A N 1848 C CA . SER A 236 ? 0.7302 0.7337 0.4927 -0.3311 -0.0038 0.0330 250 SER A CA 1849 C C . SER A 236 ? 0.7216 0.7084 0.4745 -0.3368 -0.0033 0.0377 250 SER A C 1850 O O . SER A 236 ? 0.7610 0.7251 0.5140 -0.3319 -0.0055 0.0415 250 SER A O 1851 C CB . SER A 236 ? 0.6243 0.6400 0.4022 -0.3237 -0.0016 0.0260 250 SER A CB 1852 O OG . SER A 236 ? 0.6738 0.7008 0.4497 -0.3303 0.0020 0.0235 250 SER A OG 1853 N N . GLY A 237 ? 0.6817 0.6803 0.4272 -0.3470 -0.0003 0.0372 251 GLY A N 1854 C CA . GLY A 237 ? 0.7375 0.7227 0.4753 -0.3529 0.0006 0.0409 251 GLY A CA 1855 C C . GLY A 237 ? 0.7769 0.7592 0.5237 -0.3481 0.0022 0.0369 251 GLY A C 1856 O O . GLY A 237 ? 0.8335 0.8015 0.5765 -0.3508 0.0028 0.0394 251 GLY A O 1857 N N . LYS A 238 ? 0.7154 0.7115 0.4746 -0.3410 0.0030 0.0308 252 LYS A N 1858 C CA . LYS A 238 ? 0.6521 0.6497 0.4197 -0.3373 0.0047 0.0267 252 LYS A CA 1859 C C . LYS A 238 ? 0.6313 0.6472 0.3965 -0.3459 0.0082 0.0235 252 LYS A C 1860 O O . LYS A 238 ? 0.6653 0.6987 0.4266 -0.3523 0.0097 0.0224 252 LYS A O 1861 C CB . LYS A 238 ? 0.6354 0.6404 0.4182 -0.3258 0.0039 0.0221 252 LYS A CB 1862 C CG . LYS A 238 ? 0.6598 0.6464 0.4471 -0.3162 0.0003 0.0247 252 LYS A CG 1863 C CD . LYS A 238 ? 0.6753 0.6381 0.4611 -0.3135 -0.0006 0.0276 252 LYS A CD 1864 C CE . LYS A 238 ? 0.6698 0.6157 0.4613 -0.3031 -0.0041 0.0298 252 LYS A CE 1865 N NZ . LYS A 238 ? 0.6481 0.5720 0.4402 -0.2993 -0.0046 0.0320 252 LYS A NZ 1866 N N . LYS A 239 ? 0.6042 0.6162 0.3716 -0.3463 0.0096 0.0219 253 LYS A N 1867 C CA . LYS A 239 ? 0.6021 0.6323 0.3700 -0.3525 0.0128 0.0181 253 LYS A CA 1868 C C . LYS A 239 ? 0.5785 0.6327 0.3580 -0.3475 0.0138 0.0125 253 LYS A C 1869 O O . LYS A 239 ? 0.5714 0.6253 0.3622 -0.3372 0.0123 0.0106 253 LYS A O 1870 C CB . LYS A 239 ? 0.6009 0.6222 0.3714 -0.3517 0.0136 0.0169 253 LYS A CB 1871 C CG . LYS A 239 ? 0.6585 0.6600 0.4182 -0.3588 0.0139 0.0215 253 LYS A CG 1872 C CD . LYS A 239 ? 0.7048 0.6999 0.4681 -0.3581 0.0151 0.0192 253 LYS A CD 1873 C CE . LYS A 239 ? 0.7729 0.7476 0.5277 -0.3641 0.0157 0.0234 253 LYS A CE 1874 N NZ . LYS A 239 ? 0.8789 0.8581 0.6229 -0.3757 0.0171 0.0264 253 LYS A NZ 1875 N N . LEU A 240 ? 0.5635 0.6387 0.3413 -0.3543 0.0163 0.0099 254 LEU A N 1876 C CA . LEU A 240 ? 0.5721 0.6712 0.3619 -0.3496 0.0177 0.0045 254 LEU A CA 1877 C C . LEU A 240 ? 0.6052 0.7191 0.3996 -0.3522 0.0201 0.0008 254 LEU A C 1878 O O . LEU A 240 ? 0.6161 0.7345 0.4020 -0.3622 0.0220 0.0013 254 LEU A O 1879 C CB . LEU A 240 ? 0.5668 0.6809 0.3524 -0.3545 0.0188 0.0039 254 LEU A CB 1880 C CG . LEU A 240 ? 0.5586 0.6592 0.3363 -0.3546 0.0163 0.0083 254 LEU A CG 1881 C CD1 . LEU A 240 ? 0.5746 0.6936 0.3484 -0.3603 0.0179 0.0069 254 LEU A CD1 1882 C CD2 . LEU A 240 ? 0.5444 0.6353 0.3321 -0.3427 0.0136 0.0082 254 LEU A CD2 1883 N N . TRP A 241 ? 0.5750 0.6962 0.3834 -0.3434 0.0199 -0.0027 255 TRP A N 1884 C CA . TRP A 241 ? 0.5900 0.7256 0.4042 -0.3450 0.0218 -0.0060 255 TRP A CA 1885 C C . TRP A 241 ? 0.5544 0.7140 0.3834 -0.3388 0.0230 -0.0108 255 TRP A C 1886 O O . TRP A 241 ? 0.5649 0.7256 0.4041 -0.3293 0.0216 -0.0119 255 TRP A O 1887 C CB . TRP A 241 ? 0.5474 0.6704 0.3659 -0.3400 0.0205 -0.0057 255 TRP A CB 1888 C CG . TRP A 241 ? 0.6040 0.7048 0.4101 -0.3459 0.0199 -0.0020 255 TRP A CG 1889 C CD1 . TRP A 241 ? 0.5532 0.6420 0.3459 -0.3538 0.0200 0.0019 255 TRP A CD1 1890 C CD2 . TRP A 241 ? 0.6167 0.7047 0.4237 -0.3440 0.0193 -0.0017 255 TRP A CD2 1891 N NE1 . TRP A 241 ? 0.5968 0.6658 0.3829 -0.3565 0.0196 0.0044 255 TRP A NE1 1892 C CE2 . TRP A 241 ? 0.6301 0.6985 0.4246 -0.3508 0.0193 0.0019 255 TRP A CE2 1893 C CE3 . TRP A 241 ? 0.5737 0.6654 0.3911 -0.3374 0.0188 -0.0043 255 TRP A CE3 1894 C CZ2 . TRP A 241 ? 0.6288 0.6814 0.4212 -0.3510 0.0191 0.0025 255 TRP A CZ2 1895 C CZ3 . TRP A 241 ? 0.5666 0.6432 0.3808 -0.3382 0.0185 -0.0036 255 TRP A CZ3 1896 C CH2 . TRP A 241 ? 0.6538 0.7112 0.4559 -0.3448 0.0188 -0.0005 255 TRP A CH2 1897 N N . SER A 242 ? 0.5303 0.7087 0.3611 -0.3439 0.0255 -0.0137 256 SER A N 1898 C CA . SER A 242 ? 0.5268 0.7264 0.3742 -0.3368 0.0264 -0.0182 256 SER A CA 1899 C C . SER A 242 ? 0.5160 0.7107 0.3712 -0.3312 0.0249 -0.0182 256 SER A C 1900 O O . SER A 242 ? 0.5012 0.7016 0.3549 -0.3363 0.0260 -0.0189 256 SER A O 1901 C CB . SER A 242 ? 0.5228 0.7442 0.3697 -0.3441 0.0296 -0.0212 256 SER A CB 1902 O OG . SER A 242 ? 0.5487 0.7906 0.4127 -0.3365 0.0305 -0.0256 256 SER A OG 1903 N N . SER A 243 ? 0.5341 0.7182 0.3973 -0.3212 0.0224 -0.0175 257 SER A N 1904 C CA . SER A 243 ? 0.5240 0.7007 0.3927 -0.3164 0.0207 -0.0170 257 SER A CA 1905 C C . SER A 243 ? 0.5277 0.7236 0.4121 -0.3108 0.0210 -0.0201 257 SER A C 1906 O O . SER A 243 ? 0.5380 0.7310 0.4268 -0.3079 0.0197 -0.0199 257 SER A O 1907 C CB . SER A 243 ? 0.5275 0.6848 0.3984 -0.3082 0.0179 -0.0149 257 SER A CB 1908 O OG . SER A 243 ? 0.5009 0.6646 0.3847 -0.2985 0.0168 -0.0163 257 SER A OG 1909 N N . GLU A 244 ? 0.5190 0.7347 0.4122 -0.3091 0.0225 -0.0230 258 GLU A N 1910 C CA . GLU A 244 ? 0.5224 0.7578 0.4293 -0.3058 0.0230 -0.0257 258 GLU A CA 1911 C C . GLU A 244 ? 0.5460 0.8020 0.4562 -0.3091 0.0259 -0.0289 258 GLU A C 1912 O O . GLU A 244 ? 0.5281 0.7887 0.4426 -0.3053 0.0264 -0.0306 258 GLU A O 1913 C CB . GLU A 244 ? 0.5115 0.7489 0.4364 -0.2928 0.0205 -0.0264 258 GLU A CB 1914 C CG . GLU A 244 ? 0.5338 0.7870 0.4709 -0.2904 0.0204 -0.0278 258 GLU A CG 1915 C CD . GLU A 244 ? 0.5078 0.7656 0.4643 -0.2776 0.0179 -0.0285 258 GLU A CD 1916 O OE1 . GLU A 244 ? 0.5114 0.7546 0.4693 -0.2717 0.0154 -0.0266 258 GLU A OE1 1917 O OE2 . GLU A 244 ? 0.4982 0.7741 0.4690 -0.2733 0.0185 -0.0309 258 GLU A OE2 1918 N N . ASP A 245 ? 0.5446 0.8131 0.4528 -0.3161 0.0278 -0.0300 259 ASP A N 1919 C CA . ASP A 245 ? 0.5379 0.8266 0.4488 -0.3200 0.0308 -0.0333 259 ASP A CA 1920 C C . ASP A 245 ? 0.5830 0.8882 0.5028 -0.3210 0.0315 -0.0349 259 ASP A C 1921 O O . ASP A 245 ? 0.5399 0.8414 0.4652 -0.3173 0.0294 -0.0335 259 ASP A O 1922 C CB . ASP A 245 ? 0.5937 0.8774 0.4856 -0.3324 0.0328 -0.0321 259 ASP A CB 1923 C CG . ASP A 245 ? 0.5808 0.8772 0.4729 -0.3341 0.0352 -0.0349 259 ASP A CG 1924 O OD1 . ASP A 245 ? 0.5399 0.8560 0.4463 -0.3292 0.0367 -0.0390 259 ASP A OD1 1925 O OD2 . ASP A 245 ? 0.5859 0.8727 0.4639 -0.3403 0.0357 -0.0332 259 ASP A OD2 1926 N N . PHE A 246 ? 0.5573 0.8806 0.4781 -0.3263 0.0345 -0.0377 260 PHE A N 1927 C CA . PHE A 246 ? 0.5579 0.8985 0.4869 -0.3283 0.0355 -0.0392 260 PHE A CA 1928 C C . PHE A 246 ? 0.5400 0.8940 0.4914 -0.3165 0.0343 -0.0412 260 PHE A C 1929 O O . PHE A 246 ? 0.5028 0.8708 0.4652 -0.3121 0.0360 -0.0446 260 PHE A O 1930 C CB . PHE A 246 ? 0.5684 0.8999 0.4874 -0.3353 0.0345 -0.0364 260 PHE A CB 1931 C CG . PHE A 246 ? 0.5910 0.9398 0.5153 -0.3398 0.0357 -0.0377 260 PHE A CG 1932 C CD1 . PHE A 246 ? 0.5800 0.9421 0.4996 -0.3485 0.0389 -0.0397 260 PHE A CD1 1933 C CD2 . PHE A 246 ? 0.5766 0.9280 0.5101 -0.3358 0.0336 -0.0367 260 PHE A CD2 1934 C CE1 . PHE A 246 ? 0.5589 0.9368 0.4835 -0.3528 0.0400 -0.0408 260 PHE A CE1 1935 C CE2 . PHE A 246 ? 0.5748 0.9422 0.5131 -0.3403 0.0345 -0.0376 260 PHE A CE2 1936 C CZ . PHE A 246 ? 0.5564 0.9371 0.4905 -0.3487 0.0378 -0.0397 260 PHE A CZ 1937 N N . SER A 247 ? 0.4525 0.8021 0.4109 -0.3116 0.0315 -0.0391 261 SER A N 1938 C CA . SER A 247 ? 0.4259 0.7867 0.4059 -0.3004 0.0298 -0.0401 261 SER A CA 1939 C C . SER A 247 ? 0.4410 0.8252 0.4332 -0.3008 0.0322 -0.0434 261 SER A C 1940 O O . SER A 247 ? 0.4171 0.8120 0.4278 -0.2913 0.0319 -0.0454 261 SER A O 1941 C CB . SER A 247 ? 0.4688 0.8227 0.4583 -0.2893 0.0282 -0.0406 261 SER A CB 1942 O OG . SER A 247 ? 0.5081 0.8714 0.5190 -0.2783 0.0263 -0.0412 261 SER A OG 1943 N N . THR A 248 ? 0.4201 0.8119 0.4027 -0.3117 0.0346 -0.0439 262 THR A N 1944 C CA . THR A 248 ? 0.4924 0.9063 0.4855 -0.3131 0.0372 -0.0470 262 THR A CA 1945 C C . THR A 248 ? 0.5306 0.9529 0.5265 -0.3174 0.0366 -0.0455 262 THR A C 1946 O O . THR A 248 ? 0.5230 0.9351 0.5050 -0.3249 0.0357 -0.0429 262 THR A O 1947 C CB . THR A 248 ? 0.5325 0.9520 0.5137 -0.3221 0.0412 -0.0497 262 THR A CB 1948 O OG1 . THR A 248 ? 0.5334 0.9437 0.5104 -0.3186 0.0414 -0.0506 262 THR A OG1 1949 C CG2 . THR A 248 ? 0.5323 0.9753 0.5267 -0.3218 0.0442 -0.0537 262 THR A CG2 1950 N N . ILE A 249 ? 0.5436 0.9840 0.5579 -0.3125 0.0369 -0.0471 263 ILE A N 1951 C CA . ILE A 249 ? 0.5534 1.0043 0.5721 -0.3165 0.0364 -0.0458 263 ILE A CA 1952 C C . ILE A 249 ? 0.5748 1.0256 0.5751 -0.3307 0.0386 -0.0457 263 ILE A C 1953 O O . ILE A 249 ? 0.4540 0.9090 0.4460 -0.3371 0.0419 -0.0480 263 ILE A O 1954 C CB . ILE A 249 ? 0.5865 1.0588 0.6276 -0.3105 0.0373 -0.0481 263 ILE A CB 1955 C CG1 . ILE A 249 ? 0.6064 1.0771 0.6659 -0.2964 0.0347 -0.0480 263 ILE A CG1 1956 C CG2 . ILE A 249 ? 0.5600 1.0443 0.6052 -0.3154 0.0365 -0.0465 263 ILE A CG2 1957 C CD1 . ILE A 249 ? 0.6162 1.1072 0.6984 -0.2901 0.0349 -0.0497 263 ILE A CD1 1958 N N . ASN A 250 ? 0.4516 0.8972 0.4451 -0.3358 0.0368 -0.0429 264 ASN A N 1959 C CA . ASN A 250 ? 0.5004 0.9417 0.4751 -0.3492 0.0384 -0.0423 264 ASN A CA 1960 C C . ASN A 250 ? 0.5216 0.9822 0.4992 -0.3569 0.0411 -0.0440 264 ASN A C 1961 O O . ASN A 250 ? 0.4943 0.9544 0.4622 -0.3663 0.0412 -0.0428 264 ASN A O 1962 C CB . ASN A 250 ? 0.4815 0.9064 0.4447 -0.3526 0.0358 -0.0391 264 ASN A CB 1963 C CG . ASN A 250 ? 0.5215 0.9542 0.4961 -0.3492 0.0331 -0.0376 264 ASN A CG 1964 O OD1 . ASN A 250 ? 0.5447 0.9969 0.5332 -0.3475 0.0334 -0.0387 264 ASN A OD1 1965 N ND2 . ASN A 250 ? 0.4999 0.9191 0.4664 -0.3501 0.0305 -0.0354 264 ASN A ND2 1966 N N . SER A 251 ? 0.5366 1.0141 0.5280 -0.3528 0.0433 -0.0470 265 SER A N 1967 C CA . SER A 251 ? 0.5588 1.0543 0.5514 -0.3606 0.0466 -0.0492 265 SER A CA 1968 C C . SER A 251 ? 0.5945 1.0841 0.5679 -0.3710 0.0497 -0.0503 265 SER A C 1969 O O . SER A 251 ? 0.5905 1.0618 0.5499 -0.3724 0.0489 -0.0489 265 SER A O 1970 C CB . SER A 251 ? 0.5369 1.0509 0.5500 -0.3525 0.0484 -0.0525 265 SER A CB 1971 O OG . SER A 251 ? 0.6020 1.1118 0.6144 -0.3478 0.0498 -0.0550 265 SER A OG 1972 N N . ASN A 252 ? 0.6291 1.1342 0.6023 -0.3785 0.0531 -0.0526 266 ASN A N 1973 C CA . ASN A 252 ? 0.6575 1.1594 0.6141 -0.3882 0.0562 -0.0537 266 ASN A CA 1974 C C . ASN A 252 ? 0.6016 1.0986 0.5573 -0.3826 0.0572 -0.0558 266 ASN A C 1975 O O . ASN A 252 ? 0.6037 1.0884 0.5426 -0.3888 0.0579 -0.0550 266 ASN A O 1976 C CB . ASN A 252 ? 0.7380 1.2601 0.6975 -0.3959 0.0599 -0.0563 266 ASN A CB 1977 C CG . ASN A 252 ? 0.7994 1.3415 0.7794 -0.3877 0.0620 -0.0602 266 ASN A CG 1978 O OD1 . ASN A 252 ? 0.8320 1.3831 0.8297 -0.3800 0.0604 -0.0600 266 ASN A OD1 1979 N ND2 . ASN A 252 ? 0.8204 1.3693 0.7982 -0.3891 0.0655 -0.0638 266 ASN A ND2 1980 N N . VAL A 253 ? 0.5875 1.0939 0.5615 -0.3712 0.0571 -0.0582 267 VAL A N 1981 C CA . VAL A 253 ? 0.6206 1.1230 0.5955 -0.3649 0.0578 -0.0605 267 VAL A CA 1982 C C . VAL A 253 ? 0.6407 1.1191 0.6027 -0.3635 0.0548 -0.0572 267 VAL A C 1983 O O . VAL A 253 ? 0.6681 1.1375 0.6170 -0.3671 0.0559 -0.0574 267 VAL A O 1984 C CB . VAL A 253 ? 0.7722 1.2866 0.7710 -0.3515 0.0575 -0.0634 267 VAL A CB 1985 C CG1 . VAL A 253 ? 0.7653 1.2711 0.7652 -0.3436 0.0571 -0.0649 267 VAL A CG1 1986 C CG2 . VAL A 253 ? 0.7487 1.2867 0.7597 -0.3528 0.0614 -0.0677 267 VAL A CG2 1987 N N . GLY A 254 ? 0.6235 1.0917 0.5893 -0.3584 0.0511 -0.0539 268 GLY A N 1988 C CA . GLY A 254 ? 0.5757 1.0210 0.5305 -0.3567 0.0482 -0.0506 268 GLY A CA 1989 C C . GLY A 254 ? 0.5496 0.9808 0.4818 -0.3690 0.0487 -0.0482 268 GLY A C 1990 O O . GLY A 254 ? 0.5519 0.9661 0.4721 -0.3700 0.0480 -0.0465 268 GLY A O 1991 N N . ALA A 255 ? 0.5439 0.9818 0.4709 -0.3786 0.0499 -0.0477 269 ALA A N 1992 C CA . ALA A 255 ? 0.5599 0.9850 0.4666 -0.3906 0.0505 -0.0454 269 ALA A CA 1993 C C . ALA A 255 ? 0.5855 1.0097 0.4815 -0.3961 0.0531 -0.0466 269 ALA A C 1994 O O . ALA A 255 ? 0.6095 1.0166 0.4891 -0.4024 0.0526 -0.0439 269 ALA A O 1995 C CB . ALA A 255 ? 0.5606 0.9952 0.4655 -0.3996 0.0515 -0.0452 269 ALA A CB 1996 N N . GLY A 256 ? 0.5388 0.9815 0.4443 -0.3937 0.0558 -0.0505 270 GLY A N 1997 C CA . GLY A 256 ? 0.5583 1.0027 0.4541 -0.3992 0.0584 -0.0519 270 GLY A CA 1998 C C . GLY A 256 ? 0.5652 0.9943 0.4568 -0.3932 0.0568 -0.0510 270 GLY A C 1999 O O . GLY A 256 ? 0.5953 1.0131 0.4715 -0.3996 0.0571 -0.0492 270 GLY A O 2000 N N . CYS A 257 ? 0.5459 0.9748 0.4519 -0.3807 0.0548 -0.0519 271 CYS A N 2001 C CA . CYS A 257 ? 0.5113 0.9262 0.4159 -0.3736 0.0530 -0.0511 271 CYS A CA 2002 C C . CYS A 257 ? 0.5622 0.9520 0.4500 -0.3783 0.0504 -0.0460 271 CYS A C 2003 O O . CYS A 257 ? 0.5906 0.9682 0.4670 -0.3806 0.0502 -0.0445 271 CYS A O 2004 C CB . CYS A 257 ? 0.5280 0.9469 0.4525 -0.3595 0.0511 -0.0525 271 CYS A CB 2005 S SG . CYS A 257 ? 0.6712 1.0670 0.5955 -0.3495 0.0471 -0.0495 271 CYS A SG 2006 N N . TRP A 258 ? 0.5452 0.9279 0.4319 -0.3799 0.0486 -0.0434 272 TRP A N 2007 C CA . TRP A 258 ? 0.5318 0.8909 0.4045 -0.3837 0.0462 -0.0390 272 TRP A CA 2008 C C . TRP A 258 ? 0.5530 0.9053 0.4074 -0.3965 0.0479 -0.0372 272 TRP A C 2009 O O . TRP A 258 ? 0.5855 0.9200 0.4282 -0.3984 0.0468 -0.0344 272 TRP A O 2010 C CB . TRP A 258 ? 0.5543 0.9119 0.4306 -0.3838 0.0446 -0.0378 272 TRP A CB 2011 C CG . TRP A 258 ? 0.5863 0.9206 0.4512 -0.3862 0.0422 -0.0341 272 TRP A CG 2012 C CD1 . TRP A 258 ? 0.5639 0.8931 0.4212 -0.3941 0.0420 -0.0326 272 TRP A CD1 2013 C CD2 . TRP A 258 ? 0.5866 0.9003 0.4477 -0.3804 0.0398 -0.0317 272 TRP A CD2 2014 N NE1 . TRP A 258 ? 0.5860 0.8926 0.4350 -0.3935 0.0399 -0.0298 272 TRP A NE1 2015 C CE2 . TRP A 258 ? 0.6173 0.9140 0.4684 -0.3852 0.0385 -0.0291 272 TRP A CE2 2016 C CE3 . TRP A 258 ? 0.5935 0.9014 0.4588 -0.3717 0.0388 -0.0318 272 TRP A CE3 2017 C CZ2 . TRP A 258 ? 0.6035 0.8779 0.4492 -0.3813 0.0362 -0.0265 272 TRP A CZ2 2018 C CZ3 . TRP A 258 ? 0.5948 0.8806 0.4545 -0.3681 0.0364 -0.0289 272 TRP A CZ3 2019 C CH2 . TRP A 258 ? 0.5866 0.8559 0.4368 -0.3728 0.0352 -0.0264 272 TRP A CH2 2020 N N . SER A 259 ? 0.5645 0.9313 0.4172 -0.4050 0.0504 -0.0387 273 SER A N 2021 C CA . SER A 259 ? 0.6405 1.0033 0.4772 -0.4174 0.0522 -0.0370 273 SER A CA 2022 C C . SER A 259 ? 0.5869 0.9454 0.4166 -0.4177 0.0527 -0.0367 273 SER A C 2023 O O . SER A 259 ? 0.6260 0.9661 0.4415 -0.4230 0.0516 -0.0328 273 SER A O 2024 C CB . SER A 259 ? 0.5942 0.9780 0.4334 -0.4250 0.0553 -0.0394 273 SER A CB 2025 O OG . SER A 259 ? 0.6430 1.0224 0.4670 -0.4370 0.0569 -0.0374 273 SER A OG 2026 N N . ARG A 260 ? 0.5754 0.9508 0.4156 -0.4119 0.0544 -0.0408 274 ARG A N 2027 C CA . ARG A 260 ? 0.6721 1.0467 0.5064 -0.4124 0.0552 -0.0413 274 ARG A CA 2028 C C . ARG A 260 ? 0.6634 1.0154 0.4923 -0.4070 0.0519 -0.0378 274 ARG A C 2029 O O . ARG A 260 ? 0.6686 1.0078 0.4834 -0.4131 0.0514 -0.0345 274 ARG A O 2030 C CB . ARG A 260 ? 0.6683 1.0661 0.5172 -0.4059 0.0577 -0.0473 274 ARG A CB 2031 C CG . ARG A 260 ? 0.6937 1.0949 0.5366 -0.4077 0.0591 -0.0489 274 ARG A CG 2032 C CD . ARG A 260 ? 0.6694 1.0952 0.5276 -0.4018 0.0622 -0.0558 274 ARG A CD 2033 N NE . ARG A 260 ? 0.6439 1.0745 0.5210 -0.3892 0.0612 -0.0581 274 ARG A NE 2034 C CZ . ARG A 260 ? 0.6112 1.0328 0.4956 -0.3786 0.0589 -0.0580 274 ARG A CZ 2035 N NH1 . ARG A 260 ? 0.6175 1.0254 0.4915 -0.3790 0.0575 -0.0560 274 ARG A NH1 2036 N NH2 . ARG A 260 ? 0.5706 0.9969 0.4730 -0.3675 0.0577 -0.0597 274 ARG A NH2 2037 N N . ILE A 261 ? 0.6294 0.9759 0.4694 -0.3959 0.0497 -0.0381 275 ILE A N 2038 C CA . ILE A 261 ? 0.5842 0.9105 0.4206 -0.3901 0.0468 -0.0351 275 ILE A CA 2039 C C . ILE A 261 ? 0.5936 0.8952 0.4151 -0.3961 0.0446 -0.0295 275 ILE A C 2040 O O . ILE A 261 ? 0.5994 0.8837 0.4125 -0.3957 0.0429 -0.0263 275 ILE A O 2041 C CB . ILE A 261 ? 0.5865 0.9134 0.4395 -0.3762 0.0450 -0.0369 275 ILE A CB 2042 C CG1 . ILE A 261 ? 0.5805 0.9048 0.4397 -0.3737 0.0435 -0.0359 275 ILE A CG1 2043 C CG2 . ILE A 261 ? 0.5125 0.8620 0.3805 -0.3697 0.0472 -0.0424 275 ILE A CG2 2044 C CD1 . ILE A 261 ? 0.5722 0.8980 0.4487 -0.3602 0.0415 -0.0372 275 ILE A CD1 2045 N N . LEU A 262 ? 0.5717 0.8716 0.3903 -0.4018 0.0448 -0.0285 276 LEU A N 2046 C CA . LEU A 262 ? 0.7464 1.0236 0.5515 -0.4082 0.0432 -0.0237 276 LEU A CA 2047 C C . LEU A 262 ? 0.7419 1.0099 0.5315 -0.4175 0.0438 -0.0203 276 LEU A C 2048 O O . LEU A 262 ? 0.7830 1.0291 0.5636 -0.4179 0.0417 -0.0161 276 LEU A O 2049 C CB . LEU A 262 ? 0.5953 0.8752 0.3998 -0.4140 0.0439 -0.0238 276 LEU A CB 2050 C CG . LEU A 262 ? 0.6842 0.9655 0.5003 -0.4062 0.0424 -0.0252 276 LEU A CG 2051 C CD1 . LEU A 262 ? 0.5914 0.8809 0.4070 -0.4135 0.0436 -0.0259 276 LEU A CD1 2052 C CD2 . LEU A 262 ? 0.5775 0.8353 0.3910 -0.4005 0.0394 -0.0224 276 LEU A CD2 2053 N N . ASN A 263 ? 0.6646 0.9494 0.4515 -0.4249 0.0465 -0.0220 277 ASN A N 2054 C CA . ASN A 263 ? 0.6975 0.9771 0.4712 -0.4333 0.0471 -0.0190 277 ASN A CA 2055 C C . ASN A 263 ? 0.6833 0.9604 0.4571 -0.4275 0.0460 -0.0190 277 ASN A C 2056 O O . ASN A 263 ? 0.7405 0.9981 0.5044 -0.4289 0.0439 -0.0142 277 ASN A O 2057 C CB . ASN A 263 ? 0.6406 0.9414 0.4127 -0.4424 0.0505 -0.0214 277 ASN A CB 2058 C CG . ASN A 263 ? 0.7276 1.0232 0.4908 -0.4533 0.0514 -0.0185 277 ASN A CG 2059 O OD1 . ASN A 263 ? 0.8192 1.1155 0.5720 -0.4634 0.0528 -0.0161 277 ASN A OD1 2060 N ND2 . ASN A 263 ? 0.6579 0.9485 0.4251 -0.4517 0.0506 -0.0187 277 ASN A ND2 2061 N N . GLN A 264 ? 0.6256 0.9225 0.4113 -0.4209 0.0474 -0.0243 278 GLN A N 2062 C CA . GLN A 264 ? 0.6321 0.9314 0.4174 -0.4175 0.0472 -0.0251 278 GLN A CA 2063 C C . GLN A 264 ? 0.6582 0.9405 0.4466 -0.4074 0.0440 -0.0232 278 GLN A C 2064 O O . GLN A 264 ? 0.5850 0.8648 0.3700 -0.4060 0.0434 -0.0226 278 GLN A O 2065 C CB . GLN A 264 ? 0.6285 0.9555 0.4257 -0.4142 0.0504 -0.0320 278 GLN A CB 2066 C CG . GLN A 264 ? 0.6849 1.0304 0.4798 -0.4238 0.0538 -0.0343 278 GLN A CG 2067 C CD . GLN A 264 ? 0.6584 1.0290 0.4623 -0.4215 0.0570 -0.0409 278 GLN A CD 2068 O OE1 . GLN A 264 ? 0.6856 1.0577 0.4913 -0.4167 0.0568 -0.0426 278 GLN A OE1 2069 N NE2 . GLN A 264 ? 0.6540 1.0447 0.4642 -0.4248 0.0602 -0.0449 278 GLN A NE2 2070 N N . ASN A 265 ? 0.6126 0.8839 0.4074 -0.4007 0.0421 -0.0224 279 ASN A N 2071 C CA . ASN A 265 ? 0.5947 0.8481 0.3918 -0.3917 0.0390 -0.0201 279 ASN A CA 2072 C C . ASN A 265 ? 0.5880 0.8187 0.3691 -0.3976 0.0370 -0.0139 279 ASN A C 2073 O O . ASN A 265 ? 0.6244 0.8451 0.4041 -0.3931 0.0351 -0.0121 279 ASN A O 2074 C CB . ASN A 265 ? 0.5827 0.8279 0.3886 -0.3844 0.0374 -0.0200 279 ASN A CB 2075 C CG . ASN A 265 ? 0.6046 0.8679 0.4292 -0.3742 0.0381 -0.0252 279 ASN A CG 2076 O OD1 . ASN A 265 ? 0.5622 0.8407 0.3943 -0.3704 0.0395 -0.0288 279 ASN A OD1 2077 N ND2 . ASN A 265 ? 0.6265 0.8879 0.4591 -0.3695 0.0371 -0.0255 279 ASN A ND2 2078 N N . TYR A 266 ? 0.6110 0.8334 0.3806 -0.4077 0.0374 -0.0104 280 TYR A N 2079 C CA . TYR A 266 ? 0.6816 0.8836 0.4368 -0.4138 0.0356 -0.0041 280 TYR A CA 2080 C C . TYR A 266 ? 0.6851 0.8971 0.4326 -0.4205 0.0368 -0.0035 280 TYR A C 2081 O O . TYR A 266 ? 0.6906 0.8921 0.4327 -0.4192 0.0348 -0.0002 280 TYR A O 2082 C CB . TYR A 266 ? 0.6867 0.8744 0.4327 -0.4220 0.0357 -0.0002 280 TYR A CB 2083 C CG . TYR A 266 ? 0.7097 0.8755 0.4425 -0.4269 0.0338 0.0068 280 TYR A CG 2084 C CD1 . TYR A 266 ? 0.6977 0.8426 0.4302 -0.4197 0.0307 0.0101 280 TYR A CD1 2085 C CD2 . TYR A 266 ? 0.7685 0.9352 0.4899 -0.4384 0.0351 0.0103 280 TYR A CD2 2086 C CE1 . TYR A 266 ? 0.7464 0.8711 0.4679 -0.4234 0.0289 0.0168 280 TYR A CE1 2087 C CE2 . TYR A 266 ? 0.7699 0.9165 0.4801 -0.4423 0.0333 0.0174 280 TYR A CE2 2088 C CZ . TYR A 266 ? 0.7658 0.8913 0.4761 -0.4347 0.0301 0.0207 280 TYR A CZ 2089 O OH . TYR A 266 ? 0.7625 0.8675 0.4628 -0.4377 0.0281 0.0281 280 TYR A OH 2090 N N . ILE A 267 ? 0.7090 0.9417 0.4563 -0.4276 0.0399 -0.0066 281 ILE A N 2091 C CA . ILE A 267 ? 0.7479 0.9924 0.4881 -0.4346 0.0414 -0.0064 281 ILE A CA 2092 C C . ILE A 267 ? 0.7594 1.0111 0.5045 -0.4276 0.0408 -0.0091 281 ILE A C 2093 O O . ILE A 267 ? 0.8031 1.0450 0.5392 -0.4300 0.0390 -0.0049 281 ILE A O 2094 C CB . ILE A 267 ? 0.7453 1.0150 0.4881 -0.4413 0.0453 -0.0110 281 ILE A CB 2095 C CG1 . ILE A 267 ? 0.7302 0.9931 0.4671 -0.4496 0.0460 -0.0081 281 ILE A CG1 2096 C CG2 . ILE A 267 ? 0.7337 1.0171 0.4698 -0.4483 0.0470 -0.0114 281 ILE A CG2 2097 C CD1 . ILE A 267 ? 0.7230 1.0096 0.4654 -0.4542 0.0496 -0.0130 281 ILE A CD1 2098 N N . ASN A 268 ? 0.6990 0.9675 0.4589 -0.4189 0.0422 -0.0158 282 ASN A N 2099 C CA . ASN A 268 ? 0.6812 0.9594 0.4474 -0.4123 0.0423 -0.0194 282 ASN A CA 2100 C C . ASN A 268 ? 0.6686 0.9280 0.4375 -0.4029 0.0388 -0.0168 282 ASN A C 2101 O O . ASN A 268 ? 0.6338 0.8947 0.4024 -0.4001 0.0381 -0.0173 282 ASN A O 2102 C CB . ASN A 268 ? 0.7288 1.0332 0.5113 -0.4061 0.0456 -0.0279 282 ASN A CB 2103 C CG . ASN A 268 ? 0.7705 1.0951 0.5518 -0.4147 0.0492 -0.0311 282 ASN A CG 2104 O OD1 . ASN A 268 ? 0.7999 1.1196 0.5678 -0.4256 0.0494 -0.0270 282 ASN A OD1 2105 N ND2 . ASN A 268 ? 0.7816 1.1285 0.5776 -0.4095 0.0522 -0.0382 282 ASN A ND2 2106 N N . GLY A 269 ? 0.6867 0.9291 0.4587 -0.3979 0.0367 -0.0142 283 GLY A N 2107 C CA . GLY A 269 ? 0.6405 0.8670 0.4179 -0.3877 0.0337 -0.0126 283 GLY A CA 2108 C C . GLY A 269 ? 0.6409 0.8379 0.4094 -0.3881 0.0302 -0.0056 283 GLY A C 2109 O O . GLY A 269 ? 0.6485 0.8320 0.4228 -0.3790 0.0278 -0.0045 283 GLY A O 2110 N N . ASN A 270 ? 0.6885 0.8757 0.4440 -0.3982 0.0302 -0.0010 284 ASN A N 2111 C CA . ASN A 270 ? 0.8046 0.9635 0.5518 -0.3990 0.0274 0.0055 284 ASN A CA 2112 C C . ASN A 270 ? 0.7596 0.9085 0.5158 -0.3911 0.0264 0.0044 284 ASN A C 2113 O O . ASN A 270 ? 0.6016 0.7272 0.3543 -0.3885 0.0240 0.0087 284 ASN A O 2114 C CB . ASN A 270 ? 0.9693 1.1119 0.7110 -0.3961 0.0242 0.0103 284 ASN A CB 2115 C CG . ASN A 270 ? 1.1745 1.3279 0.9079 -0.4031 0.0249 0.0114 284 ASN A CG 2116 O OD1 . ASN A 270 ? 1.1633 1.3348 0.9029 -0.4000 0.0260 0.0067 284 ASN A OD1 2117 N ND2 . ASN A 270 ? 1.3685 1.5109 1.0883 -0.4125 0.0242 0.0176 284 ASN A ND2 2118 N N . MET A 271 ? 0.6895 0.8559 0.4573 -0.3873 0.0284 -0.0012 285 MET A N 2119 C CA . MET A 271 ? 0.6500 0.8091 0.4267 -0.3801 0.0275 -0.0024 285 MET A CA 2120 C C . MET A 271 ? 0.6489 0.8010 0.4191 -0.3875 0.0283 -0.0007 285 MET A C 2121 O O . MET A 271 ? 0.6798 0.8467 0.4481 -0.3951 0.0308 -0.0026 285 MET A O 2122 C CB . MET A 271 ? 0.5692 0.7493 0.3623 -0.3720 0.0288 -0.0084 285 MET A CB 2123 C CG . MET A 271 ? 0.5582 0.7420 0.3604 -0.3625 0.0277 -0.0101 285 MET A CG 2124 S SD . MET A 271 ? 0.6037 0.8149 0.4260 -0.3540 0.0298 -0.0173 285 MET A SD 2125 C CE . MET A 271 ? 0.6072 0.8410 0.4259 -0.3611 0.0331 -0.0206 285 MET A CE 2126 N N . THR A 272 ? 0.6571 0.7868 0.4247 -0.3852 0.0264 0.0024 286 THR A N 2127 C CA . THR A 272 ? 0.6648 0.7839 0.4250 -0.3926 0.0271 0.0045 286 THR A CA 2128 C C . THR A 272 ? 0.6985 0.8203 0.4672 -0.3887 0.0275 0.0013 286 THR A C 2129 O O . THR A 272 ? 0.7287 0.8420 0.4925 -0.3942 0.0282 0.0023 286 THR A O 2130 C CB . THR A 272 ? 0.6841 0.7762 0.4346 -0.3943 0.0252 0.0104 286 THR A CB 2131 O OG1 . THR A 272 ? 0.6370 0.7162 0.3934 -0.3835 0.0226 0.0111 286 THR A OG1 2132 C CG2 . THR A 272 ? 0.6671 0.7586 0.4067 -0.4019 0.0252 0.0145 286 THR A CG2 2133 N N . SER A 273 ? 0.6606 0.7946 0.4423 -0.3793 0.0271 -0.0025 287 SER A N 2134 C CA . SER A 273 ? 0.6412 0.7837 0.4318 -0.3764 0.0276 -0.0058 287 SER A CA 2135 C C . SER A 273 ? 0.5777 0.7443 0.3820 -0.3701 0.0284 -0.0102 287 SER A C 2136 O O . SER A 273 ? 0.5922 0.7634 0.4021 -0.3639 0.0278 -0.0110 287 SER A O 2137 C CB . SER A 273 ? 0.6696 0.7937 0.4635 -0.3691 0.0255 -0.0048 287 SER A CB 2138 O OG . SER A 273 ? 0.7206 0.8542 0.5236 -0.3658 0.0258 -0.0079 287 SER A OG 2139 N N . THR A 274 ? 0.5723 0.7544 0.3823 -0.3720 0.0299 -0.0131 288 THR A N 2140 C CA . THR A 274 ? 0.5437 0.7475 0.3688 -0.3650 0.0305 -0.0171 288 THR A CA 2141 C C . THR A 274 ? 0.5737 0.7791 0.4071 -0.3609 0.0296 -0.0183 288 THR A C 2142 O O . THR A 274 ? 0.5584 0.7608 0.3855 -0.3680 0.0302 -0.0178 288 THR A O 2143 C CB . THR A 274 ? 0.5876 0.8136 0.4130 -0.3715 0.0333 -0.0197 288 THR A CB 2144 O OG1 . THR A 274 ? 0.5626 0.7872 0.3794 -0.3759 0.0341 -0.0186 288 THR A OG1 2145 C CG2 . THR A 274 ? 0.5714 0.8193 0.4143 -0.3632 0.0339 -0.0239 288 THR A CG2 2146 N N . ILE A 275 ? 0.5750 0.7851 0.4225 -0.3497 0.0281 -0.0198 289 ILE A N 2147 C CA . ILE A 275 ? 0.5326 0.7444 0.3884 -0.3453 0.0269 -0.0206 289 ILE A CA 2148 C C . ILE A 275 ? 0.5209 0.7560 0.3933 -0.3391 0.0273 -0.0237 289 ILE A C 2149 O O . ILE A 275 ? 0.4851 0.7263 0.3686 -0.3303 0.0266 -0.0249 289 ILE A O 2150 C CB . ILE A 275 ? 0.5237 0.7169 0.3817 -0.3372 0.0242 -0.0188 289 ILE A CB 2151 C CG1 . ILE A 275 ? 0.5055 0.6753 0.3481 -0.3430 0.0240 -0.0157 289 ILE A CG1 2152 C CG2 . ILE A 275 ? 0.4821 0.6774 0.3479 -0.3332 0.0230 -0.0196 289 ILE A CG2 2153 C CD1 . ILE A 275 ? 0.5542 0.7047 0.3985 -0.3350 0.0216 -0.0139 289 ILE A CD1 2154 N N . ALA A 276 ? 0.4866 0.7347 0.3611 -0.3437 0.0283 -0.0250 290 ALA A N 2155 C CA . ALA A 276 ? 0.4990 0.7695 0.3897 -0.3384 0.0286 -0.0276 290 ALA A CA 2156 C C . ALA A 276 ? 0.4710 0.7418 0.3759 -0.3276 0.0259 -0.0275 290 ALA A C 2157 O O . ALA A 276 ? 0.4592 0.7203 0.3608 -0.3282 0.0244 -0.0261 290 ALA A O 2158 C CB . ALA A 276 ? 0.4970 0.7813 0.3851 -0.3475 0.0304 -0.0287 290 ALA A CB 2159 N N . TRP A 277 ? 0.4742 0.7564 0.3951 -0.3178 0.0253 -0.0291 291 TRP A N 2160 C CA . TRP A 277 ? 0.4787 0.7675 0.4153 -0.3089 0.0230 -0.0291 291 TRP A CA 2161 C C . TRP A 277 ? 0.4987 0.8096 0.4442 -0.3112 0.0244 -0.0310 291 TRP A C 2162 O O . TRP A 277 ? 0.4699 0.7946 0.4219 -0.3103 0.0262 -0.0333 291 TRP A O 2163 C CB . TRP A 277 ? 0.4315 0.7208 0.3826 -0.2966 0.0214 -0.0297 291 TRP A CB 2164 C CG . TRP A 277 ? 0.4226 0.7153 0.3889 -0.2873 0.0186 -0.0290 291 TRP A CG 2165 C CD1 . TRP A 277 ? 0.4023 0.6808 0.3679 -0.2832 0.0159 -0.0268 291 TRP A CD1 2166 C CD2 . TRP A 277 ? 0.4330 0.7443 0.4175 -0.2813 0.0180 -0.0302 291 TRP A CD2 2167 N NE1 . TRP A 277 ? 0.4069 0.6942 0.3885 -0.2753 0.0137 -0.0265 291 TRP A NE1 2168 C CE2 . TRP A 277 ? 0.3859 0.6932 0.3795 -0.2741 0.0148 -0.0284 291 TRP A CE2 2169 C CE3 . TRP A 277 ? 0.4761 0.8072 0.4705 -0.2815 0.0199 -0.0327 291 TRP A CE3 2170 C CZ2 . TRP A 277 ? 0.3748 0.6984 0.3848 -0.2686 0.0133 -0.0287 291 TRP A CZ2 2171 C CZ3 . TRP A 277 ? 0.4745 0.8195 0.4879 -0.2742 0.0184 -0.0329 291 TRP A CZ3 2172 C CH2 . TRP A 277 ? 0.4444 0.7864 0.4644 -0.2686 0.0151 -0.0309 291 TRP A CH2 2173 N N . ASN A 278 ? 0.4911 0.8061 0.4374 -0.3141 0.0235 -0.0302 292 ASN A N 2174 C CA . ASN A 278 ? 0.4757 0.7760 0.4151 -0.3149 0.0214 -0.0280 292 ASN A CA 2175 C C . ASN A 278 ? 0.4933 0.7937 0.4199 -0.3268 0.0227 -0.0277 292 ASN A C 2176 O O . ASN A 278 ? 0.5113 0.8242 0.4356 -0.3340 0.0249 -0.0290 292 ASN A O 2177 C CB . ASN A 278 ? 0.4565 0.7622 0.4115 -0.3054 0.0185 -0.0272 292 ASN A CB 2178 C CG . ASN A 278 ? 0.4553 0.7841 0.4213 -0.3065 0.0187 -0.0283 292 ASN A CG 2179 O OD1 . ASN A 278 ? 0.4545 0.7892 0.4138 -0.3151 0.0193 -0.0282 292 ASN A OD1 2180 N ND2 . ASN A 278 ? 0.4021 0.7437 0.3854 -0.2978 0.0182 -0.0293 292 ASN A ND2 2181 N N . LEU A 279 ? 0.5127 0.7996 0.4316 -0.3289 0.0213 -0.0263 293 LEU A N 2182 C CA . LEU A 279 ? 0.5330 0.8162 0.4382 -0.3405 0.0224 -0.0262 293 LEU A CA 2183 C C . LEU A 279 ? 0.5491 0.8521 0.4594 -0.3453 0.0228 -0.0272 293 LEU A C 2184 O O . LEU A 279 ? 0.5252 0.8336 0.4282 -0.3548 0.0249 -0.0279 293 LEU A O 2185 C CB . LEU A 279 ? 0.5200 0.7853 0.4177 -0.3405 0.0209 -0.0250 293 LEU A CB 2186 C CG . LEU A 279 ? 0.5383 0.7997 0.4231 -0.3517 0.0217 -0.0253 293 LEU A CG 2187 C CD1 . LEU A 279 ? 0.5122 0.7604 0.3823 -0.3605 0.0239 -0.0251 293 LEU A CD1 2188 C CD2 . LEU A 279 ? 0.4948 0.7452 0.3766 -0.3499 0.0199 -0.0249 293 LEU A CD2 2189 N N . VAL A 280 ? 0.5244 0.8388 0.4464 -0.3396 0.0207 -0.0270 294 VAL A N 2190 C CA . VAL A 280 ? 0.4935 0.8279 0.4213 -0.3438 0.0207 -0.0276 294 VAL A CA 2191 C C . VAL A 280 ? 0.5217 0.8702 0.4681 -0.3335 0.0186 -0.0272 294 VAL A C 2192 O O . VAL A 280 ? 0.6011 0.9420 0.5523 -0.3255 0.0163 -0.0261 294 VAL A O 2193 C CB . VAL A 280 ? 0.5283 0.8586 0.4452 -0.3521 0.0200 -0.0271 294 VAL A CB 2194 C CG1 . VAL A 280 ? 0.4773 0.7944 0.3931 -0.3467 0.0176 -0.0259 294 VAL A CG1 2195 C CG2 . VAL A 280 ? 0.5157 0.8678 0.4392 -0.3564 0.0196 -0.0274 294 VAL A CG2 2196 N N . ALA A 281 ? 0.4636 0.8323 0.4213 -0.3332 0.0193 -0.0282 295 ALA A N 2197 C CA . ALA A 281 ? 0.4357 0.8181 0.4123 -0.3235 0.0172 -0.0277 295 ALA A CA 2198 C C . ALA A 281 ? 0.5546 0.9433 0.5327 -0.3253 0.0146 -0.0259 295 ALA A C 2199 O O . ALA A 281 ? 0.4436 0.8488 0.4255 -0.3303 0.0147 -0.0259 295 ALA A O 2200 C CB . ALA A 281 ? 0.4325 0.8344 0.4221 -0.3221 0.0189 -0.0294 295 ALA A CB 2201 N N . SER A 282 ? 0.5694 0.9449 0.5439 -0.3216 0.0124 -0.0244 296 SER A N 2202 C CA . SER A 282 ? 0.5488 0.9300 0.5253 -0.3223 0.0097 -0.0226 296 SER A CA 2203 C C . SER A 282 ? 0.4691 0.8529 0.4612 -0.3103 0.0068 -0.0209 296 SER A C 2204 O O . SER A 282 ? 0.4800 0.8547 0.4695 -0.3076 0.0047 -0.0193 296 SER A O 2205 C CB . SER A 282 ? 0.5526 0.9174 0.5112 -0.3293 0.0097 -0.0223 296 SER A CB 2206 O OG . SER A 282 ? 0.5512 0.9165 0.4969 -0.3412 0.0120 -0.0237 296 SER A OG 2207 N N . TYR A 283 ? 0.4061 0.8028 0.4149 -0.3033 0.0068 -0.0213 297 TYR A N 2208 C CA . TYR A 283 ? 0.4224 0.8232 0.4484 -0.2918 0.0040 -0.0196 297 TYR A CA 2209 C C . TYR A 283 ? 0.3861 0.8087 0.4296 -0.2892 0.0041 -0.0198 297 TYR A C 2210 O O . TYR A 283 ? 0.4567 0.8868 0.4996 -0.2936 0.0068 -0.0220 297 TYR A O 2211 C CB . TYR A 283 ? 0.3786 0.7651 0.4074 -0.2832 0.0043 -0.0205 297 TYR A CB 2212 C CG . TYR A 283 ? 0.4070 0.7932 0.4351 -0.2839 0.0075 -0.0233 297 TYR A CG 2213 C CD1 . TYR A 283 ? 0.3920 0.7673 0.4023 -0.2924 0.0102 -0.0246 297 TYR A CD1 2214 C CD2 . TYR A 283 ? 0.4134 0.8101 0.4585 -0.2761 0.0080 -0.0246 297 TYR A CD2 2215 C CE1 . TYR A 283 ? 0.3934 0.7688 0.4025 -0.2934 0.0131 -0.0269 297 TYR A CE1 2216 C CE2 . TYR A 283 ? 0.4433 0.8403 0.4871 -0.2770 0.0111 -0.0274 297 TYR A CE2 2217 C CZ . TYR A 283 ? 0.4475 0.8342 0.4731 -0.2858 0.0136 -0.0283 297 TYR A CZ 2218 O OH . TYR A 283 ? 0.4738 0.8614 0.4979 -0.2870 0.0166 -0.0308 297 TYR A OH 2219 N N . TYR A 284 ? 0.3767 0.8094 0.4360 -0.2822 0.0011 -0.0175 298 TYR A N 2220 C CA . TYR A 284 ? 0.3727 0.8264 0.4510 -0.2789 0.0008 -0.0173 298 TYR A CA 2221 C C . TYR A 284 ? 0.3686 0.8261 0.4549 -0.2756 0.0038 -0.0206 298 TYR A C 2222 O O . TYR A 284 ? 0.3783 0.8253 0.4676 -0.2685 0.0042 -0.0218 298 TYR A O 2223 C CB . TYR A 284 ? 0.3603 0.8190 0.4559 -0.2689 -0.0030 -0.0143 298 TYR A CB 2224 C CG . TYR A 284 ? 0.3645 0.8238 0.4546 -0.2722 -0.0061 -0.0107 298 TYR A CG 2225 C CD1 . TYR A 284 ? 0.3983 0.8684 0.4812 -0.2821 -0.0062 -0.0099 298 TYR A CD1 2226 C CD2 . TYR A 284 ? 0.3896 0.8391 0.4817 -0.2655 -0.0090 -0.0083 298 TYR A CD2 2227 C CE1 . TYR A 284 ? 0.3820 0.8533 0.4594 -0.2854 -0.0090 -0.0068 298 TYR A CE1 2228 C CE2 . TYR A 284 ? 0.3604 0.8109 0.4467 -0.2689 -0.0118 -0.0052 298 TYR A CE2 2229 C CZ . TYR A 284 ? 0.3735 0.8352 0.4524 -0.2789 -0.0117 -0.0044 298 TYR A CZ 2230 O OH . TYR A 284 ? 0.3877 0.8513 0.4604 -0.2826 -0.0144 -0.0014 298 TYR A OH 2231 N N . GLU A 285 ? 0.4081 0.8808 0.4980 -0.2808 0.0060 -0.0222 299 GLU A N 2232 C CA . GLU A 285 ? 0.4632 0.9383 0.5566 -0.2796 0.0096 -0.0259 299 GLU A CA 2233 C C . GLU A 285 ? 0.4329 0.9135 0.5476 -0.2677 0.0091 -0.0268 299 GLU A C 2234 O O . GLU A 285 ? 0.3753 0.8541 0.4922 -0.2650 0.0118 -0.0300 299 GLU A O 2235 C CB . GLU A 285 ? 0.5150 1.0047 0.6059 -0.2888 0.0125 -0.0277 299 GLU A CB 2236 C CG . GLU A 285 ? 0.5816 1.0934 0.6917 -0.2868 0.0116 -0.0268 299 GLU A CG 2237 C CD . GLU A 285 ? 0.6328 1.1593 0.7412 -0.2958 0.0148 -0.0289 299 GLU A CD 2238 O OE1 . GLU A 285 ? 0.6163 1.1373 0.7119 -0.3018 0.0182 -0.0316 299 GLU A OE1 2239 O OE2 . GLU A 285 ? 0.6530 1.1970 0.7735 -0.2968 0.0137 -0.0275 299 GLU A OE2 2240 N N . GLU A 286 ? 0.4518 0.9389 0.5822 -0.2606 0.0057 -0.0241 300 GLU A N 2241 C CA . GLU A 286 ? 0.4226 0.9142 0.5746 -0.2488 0.0049 -0.0247 300 GLU A CA 2242 C C . GLU A 286 ? 0.3962 0.8694 0.5461 -0.2412 0.0035 -0.0245 300 GLU A C 2243 O O . GLU A 286 ? 0.3826 0.8565 0.5492 -0.2311 0.0028 -0.0252 300 GLU A O 2244 C CB . GLU A 286 ? 0.4488 0.9555 0.6198 -0.2446 0.0018 -0.0215 300 GLU A CB 2245 C CG . GLU A 286 ? 0.5277 1.0545 0.7046 -0.2510 0.0032 -0.0217 300 GLU A CG 2246 C CD . GLU A 286 ? 0.5933 1.1226 0.7550 -0.2616 0.0020 -0.0191 300 GLU A CD 2247 O OE1 . GLU A 286 ? 0.5716 1.0861 0.7157 -0.2652 0.0009 -0.0178 300 GLU A OE1 2248 O OE2 . GLU A 286 ? 0.6178 1.1641 0.7857 -0.2664 0.0023 -0.0186 300 GLU A OE2 2249 N N . LEU A 287 ? 0.3694 0.8263 0.4995 -0.2459 0.0031 -0.0235 301 LEU A N 2250 C CA . LEU A 287 ? 0.4309 0.8688 0.5558 -0.2403 0.0025 -0.0239 301 LEU A CA 2251 C C . LEU A 287 ? 0.3241 0.7573 0.4442 -0.2409 0.0061 -0.0278 301 LEU A C 2252 O O . LEU A 287 ? 0.3335 0.7749 0.4483 -0.2480 0.0091 -0.0299 301 LEU A O 2253 C CB . LEU A 287 ? 0.4106 0.8331 0.5160 -0.2459 0.0012 -0.0217 301 LEU A CB 2254 C CG . LEU A 287 ? 0.3973 0.8206 0.5063 -0.2437 -0.0027 -0.0178 301 LEU A CG 2255 C CD1 . LEU A 287 ? 0.3356 0.7447 0.4239 -0.2508 -0.0032 -0.0165 301 LEU A CD1 2256 C CD2 . LEU A 287 ? 0.3118 0.7314 0.4371 -0.2314 -0.0053 -0.0165 301 LEU A CD2 2257 N N . PRO A 288 ? 0.3144 0.7348 0.4364 -0.2335 0.0057 -0.0288 302 PRO A N 2258 C CA . PRO A 288 ? 0.3144 0.7312 0.4329 -0.2336 0.0089 -0.0325 302 PRO A CA 2259 C C . PRO A 288 ? 0.3803 0.7922 0.4778 -0.2450 0.0120 -0.0336 302 PRO A C 2260 O O . PRO A 288 ? 0.3688 0.7691 0.4501 -0.2510 0.0112 -0.0315 302 PRO A O 2261 C CB . PRO A 288 ? 0.3040 0.7037 0.4222 -0.2259 0.0072 -0.0321 302 PRO A CB 2262 C CG . PRO A 288 ? 0.3664 0.7675 0.4991 -0.2178 0.0032 -0.0291 302 PRO A CG 2263 C CD . PRO A 288 ? 0.3028 0.7131 0.4319 -0.2246 0.0022 -0.0265 302 PRO A CD 2264 N N . TYR A 289 ? 0.3640 0.7847 0.4620 -0.2480 0.0154 -0.0368 303 TYR A N 2265 C CA . TYR A 289 ? 0.3732 0.7901 0.4524 -0.2588 0.0185 -0.0379 303 TYR A CA 2266 C C . TYR A 289 ? 0.4132 0.8348 0.4823 -0.2688 0.0185 -0.0360 303 TYR A C 2267 O O . TYR A 289 ? 0.4557 0.8664 0.5059 -0.2774 0.0194 -0.0353 303 TYR A O 2268 C CB . TYR A 289 ? 0.3748 0.7705 0.4385 -0.2596 0.0186 -0.0374 303 TYR A CB 2269 C CG . TYR A 289 ? 0.4224 0.8131 0.4942 -0.2508 0.0188 -0.0394 303 TYR A CG 2270 C CD1 . TYR A 289 ? 0.4352 0.8303 0.5055 -0.2525 0.0221 -0.0427 303 TYR A CD1 2271 C CD2 . TYR A 289 ? 0.4146 0.7962 0.4951 -0.2410 0.0156 -0.0381 303 TYR A CD2 2272 C CE1 . TYR A 289 ? 0.4480 0.8401 0.5243 -0.2456 0.0224 -0.0450 303 TYR A CE1 2273 C CE2 . TYR A 289 ? 0.4228 0.7998 0.5107 -0.2332 0.0157 -0.0400 303 TYR A CE2 2274 C CZ . TYR A 289 ? 0.4458 0.8277 0.5319 -0.2352 0.0190 -0.0435 303 TYR A CZ 2275 O OH . TYR A 289 ? 0.4334 0.8126 0.5256 -0.2285 0.0192 -0.0460 303 TYR A OH 2276 N N . GLY A 290 ? 0.4326 0.8705 0.5144 -0.2680 0.0174 -0.0353 304 GLY A N 2277 C CA . GLY A 290 ? 0.4593 0.9041 0.5332 -0.2774 0.0172 -0.0337 304 GLY A CA 2278 C C . GLY A 290 ? 0.4522 0.8977 0.5106 -0.2887 0.0207 -0.0354 304 GLY A C 2279 O O . GLY A 290 ? 0.4130 0.8639 0.4733 -0.2893 0.0238 -0.0384 304 GLY A O 2280 N N . ARG A 291 ? 0.4291 0.8691 0.4722 -0.2979 0.0203 -0.0337 305 ARG A N 2281 C CA . ARG A 291 ? 0.4469 0.8871 0.4747 -0.3097 0.0232 -0.0348 305 ARG A CA 2282 C C . ARG A 291 ? 0.4961 0.9236 0.5120 -0.3119 0.0259 -0.0364 305 ARG A C 2283 O O . ARG A 291 ? 0.5010 0.9343 0.5110 -0.3192 0.0290 -0.0382 305 ARG A O 2284 C CB . ARG A 291 ? 0.5044 0.9670 0.5421 -0.3133 0.0252 -0.0364 305 ARG A CB 2285 C CG . ARG A 291 ? 0.5652 1.0395 0.6055 -0.3180 0.0233 -0.0344 305 ARG A CG 2286 C CD . ARG A 291 ? 0.6009 1.0962 0.6496 -0.3225 0.0257 -0.0362 305 ARG A CD 2287 N NE . ARG A 291 ? 0.6433 1.1365 0.6802 -0.3301 0.0296 -0.0386 305 ARG A NE 2288 C CZ . ARG A 291 ? 0.6698 1.1780 0.7147 -0.3313 0.0327 -0.0413 305 ARG A CZ 2289 N NH1 . ARG A 291 ? 0.6811 1.2072 0.7466 -0.3251 0.0325 -0.0421 305 ARG A NH1 2290 N NH2 . ARG A 291 ? 0.6720 1.1772 0.7047 -0.3388 0.0362 -0.0432 305 ARG A NH2 2291 N N . SER A 292 ? 0.4835 0.8939 0.4959 -0.3061 0.0246 -0.0356 306 SER A N 2292 C CA . SER A 292 ? 0.4381 0.8350 0.4381 -0.3087 0.0267 -0.0365 306 SER A CA 2293 C C . SER A 292 ? 0.4403 0.8172 0.4206 -0.3154 0.0259 -0.0343 306 SER A C 2294 O O . SER A 292 ? 0.4322 0.7931 0.4044 -0.3136 0.0256 -0.0338 306 SER A O 2295 C CB . SER A 292 ? 0.4695 0.8628 0.4787 -0.2986 0.0264 -0.0378 306 SER A CB 2296 O OG . SER A 292 ? 0.5069 0.9173 0.5370 -0.2907 0.0264 -0.0395 306 SER A OG 2297 N N . GLY A 293 ? 0.4592 0.8374 0.4319 -0.3234 0.0256 -0.0332 307 GLY A N 2298 C CA . GLY A 293 ? 0.4720 0.8324 0.4261 -0.3312 0.0255 -0.0316 307 GLY A CA 2299 C C . GLY A 293 ? 0.5107 0.8742 0.4511 -0.3439 0.0285 -0.0326 307 GLY A C 2300 O O . GLY A 293 ? 0.4772 0.8581 0.4236 -0.3466 0.0305 -0.0344 307 GLY A O 2301 N N . LEU A 294 ? 0.5303 0.8770 0.4530 -0.3518 0.0289 -0.0315 308 LEU A N 2302 C CA . LEU A 294 ? 0.5550 0.9030 0.4644 -0.3642 0.0316 -0.0321 308 LEU A CA 2303 C C . LEU A 294 ? 0.6429 1.0069 0.5561 -0.3700 0.0320 -0.0327 308 LEU A C 2304 O O . LEU A 294 ? 0.6764 1.0525 0.5876 -0.3773 0.0344 -0.0340 308 LEU A O 2305 C CB . LEU A 294 ? 0.5831 0.9084 0.4742 -0.3708 0.0316 -0.0305 308 LEU A CB 2306 C CG . LEU A 294 ? 0.5731 0.8822 0.4579 -0.3676 0.0316 -0.0296 308 LEU A CG 2307 C CD1 . LEU A 294 ? 0.5888 0.8766 0.4554 -0.3759 0.0320 -0.0279 308 LEU A CD1 2308 C CD2 . LEU A 294 ? 0.5832 0.9035 0.4708 -0.3675 0.0338 -0.0312 308 LEU A CD2 2309 N N . MET A 295 ? 0.6253 0.9895 0.5438 -0.3669 0.0295 -0.0316 309 MET A N 2310 C CA . MET A 295 ? 0.5920 0.9743 0.5157 -0.3717 0.0294 -0.0321 309 MET A CA 2311 C C . MET A 295 ? 0.5650 0.9567 0.5033 -0.3627 0.0265 -0.0314 309 MET A C 2312 O O . MET A 295 ? 0.5335 0.9184 0.4786 -0.3527 0.0250 -0.0309 309 MET A O 2313 C CB . MET A 295 ? 0.5814 0.9562 0.4902 -0.3829 0.0295 -0.0316 309 MET A CB 2314 C CG . MET A 295 ? 0.5251 0.8812 0.4257 -0.3817 0.0274 -0.0303 309 MET A CG 2315 S SD . MET A 295 ? 0.6004 0.9502 0.4846 -0.3959 0.0282 -0.0305 309 MET A SD 2316 C CE . MET A 295 ? 0.7086 1.0835 0.6034 -0.3977 0.0269 -0.0308 309 MET A CE 2317 N N . THR A 296 ? 0.5098 0.9170 0.4532 -0.3662 0.0256 -0.0312 310 THR A N 2318 C CA . THR A 296 ? 0.5095 0.9281 0.4682 -0.3580 0.0228 -0.0302 310 THR A CA 2319 C C . THR A 296 ? 0.5603 0.9785 0.5132 -0.3630 0.0206 -0.0288 310 THR A C 2320 O O . THR A 296 ? 0.5767 0.9997 0.5214 -0.3733 0.0216 -0.0292 310 THR A O 2321 C CB . THR A 296 ? 0.5433 0.9860 0.5186 -0.3560 0.0235 -0.0311 310 THR A CB 2322 O OG1 . THR A 296 ? 0.5185 0.9628 0.5016 -0.3498 0.0254 -0.0328 310 THR A OG1 2323 C CG2 . THR A 296 ? 0.5234 0.9787 0.5142 -0.3491 0.0203 -0.0294 310 THR A CG2 2324 N N . ALA A 297 ? 0.5463 0.9589 0.5033 -0.3560 0.0177 -0.0271 311 ALA A N 2325 C CA . ALA A 297 ? 0.5509 0.9656 0.5042 -0.3599 0.0154 -0.0257 311 ALA A CA 2326 C C . ALA A 297 ? 0.5070 0.9275 0.4747 -0.3495 0.0121 -0.0237 311 ALA A C 2327 O O . ALA A 297 ? 0.4659 0.8737 0.4294 -0.3461 0.0103 -0.0226 311 ALA A O 2328 C CB . ALA A 297 ? 0.4962 0.8899 0.4309 -0.3660 0.0159 -0.0260 311 ALA A CB 2329 N N . GLN A 298 ? 0.4902 0.9299 0.4752 -0.3445 0.0113 -0.0232 312 GLN A N 2330 C CA . GLN A 298 ? 0.4464 0.8921 0.4473 -0.3338 0.0082 -0.0210 312 GLN A CA 2331 C C . GLN A 298 ? 0.5834 1.0458 0.5917 -0.3356 0.0054 -0.0186 312 GLN A C 2332 O O . GLN A 298 ? 0.4368 0.9105 0.4624 -0.3273 0.0031 -0.0167 312 GLN A O 2333 C CB . GLN A 298 ? 0.4336 0.8875 0.4516 -0.3247 0.0090 -0.0219 312 GLN A CB 2334 C CG . GLN A 298 ? 0.5303 1.0016 0.5545 -0.3292 0.0113 -0.0235 312 GLN A CG 2335 C CD . GLN A 298 ? 0.5688 1.0465 0.6084 -0.3207 0.0128 -0.0252 312 GLN A CD 2336 O OE1 . GLN A 298 ? 0.5958 1.0607 0.6353 -0.3142 0.0132 -0.0260 312 GLN A OE1 2337 N NE2 . GLN A 298 ? 0.5293 1.0271 0.5827 -0.3208 0.0136 -0.0258 312 GLN A NE2 2338 N N . GLU A 299 ? 0.5953 1.0593 0.5909 -0.3465 0.0056 -0.0186 313 GLU A N 2339 C CA . GLU A 299 ? 0.6079 1.0879 0.6089 -0.3493 0.0029 -0.0162 313 GLU A CA 2340 C C . GLU A 299 ? 0.5646 1.0365 0.5484 -0.3583 0.0022 -0.0159 313 GLU A C 2341 O O . GLU A 299 ? 0.5343 1.0127 0.5099 -0.3689 0.0033 -0.0168 313 GLU A O 2342 C CB . GLU A 299 ? 0.6498 1.1504 0.6585 -0.3546 0.0041 -0.0167 313 GLU A CB 2343 C CG . GLU A 299 ? 0.6607 1.1752 0.6903 -0.3459 0.0043 -0.0166 313 GLU A CG 2344 C CD . GLU A 299 ? 0.6907 1.2257 0.7273 -0.3520 0.0056 -0.0172 313 GLU A CD 2345 O OE1 . GLU A 299 ? 0.6660 1.2083 0.6955 -0.3612 0.0048 -0.0163 313 GLU A OE1 2346 O OE2 . GLU A 299 ? 0.7124 1.2562 0.7614 -0.3479 0.0075 -0.0187 313 GLU A OE2 2347 N N . PRO A 300 ? 0.5556 1.0136 0.5344 -0.3543 0.0006 -0.0149 314 PRO A N 2348 C CA . PRO A 300 ? 0.5845 1.0341 0.5468 -0.3628 0.0002 -0.0152 314 PRO A CA 2349 C C . PRO A 300 ? 0.5860 1.0536 0.5512 -0.3680 -0.0022 -0.0130 314 PRO A C 2350 O O . PRO A 300 ? 0.5927 1.0576 0.5440 -0.3779 -0.0017 -0.0140 314 PRO A O 2351 C CB . PRO A 300 ? 0.5498 0.9830 0.5104 -0.3551 -0.0012 -0.0143 314 PRO A CB 2352 C CG . PRO A 300 ? 0.5511 0.9917 0.5311 -0.3425 -0.0032 -0.0121 314 PRO A CG 2353 C CD . PRO A 300 ? 0.5739 1.0233 0.5618 -0.3421 -0.0009 -0.0137 314 PRO A CD 2354 N N . TRP A 301 ? 0.5591 1.0443 0.5424 -0.3613 -0.0048 -0.0101 315 TRP A N 2355 C CA . TRP A 301 ? 0.5353 1.0391 0.5238 -0.3650 -0.0076 -0.0072 315 TRP A CA 2356 C C . TRP A 301 ? 0.5693 1.0880 0.5563 -0.3750 -0.0061 -0.0084 315 TRP A C 2357 O O . TRP A 301 ? 0.5321 1.0652 0.5199 -0.3806 -0.0081 -0.0064 315 TRP A O 2358 C CB . TRP A 301 ? 0.5012 1.0186 0.5114 -0.3539 -0.0108 -0.0035 315 TRP A CB 2359 C CG . TRP A 301 ? 0.5322 1.0552 0.5571 -0.3473 -0.0091 -0.0046 315 TRP A CG 2360 C CD1 . TRP A 301 ? 0.4678 1.0074 0.5014 -0.3503 -0.0080 -0.0051 315 TRP A CD1 2361 C CD2 . TRP A 301 ? 0.5424 1.0543 0.5746 -0.3368 -0.0083 -0.0055 315 TRP A CD2 2362 N NE1 . TRP A 301 ? 0.4573 0.9969 0.5032 -0.3425 -0.0063 -0.0066 315 TRP A NE1 2363 C CE2 . TRP A 301 ? 0.5460 1.0689 0.5912 -0.3341 -0.0065 -0.0069 315 TRP A CE2 2364 C CE3 . TRP A 301 ? 0.5342 1.0285 0.5637 -0.3295 -0.0089 -0.0055 315 TRP A CE3 2365 C CZ2 . TRP A 301 ? 0.5297 1.0465 0.5847 -0.3247 -0.0052 -0.0083 315 TRP A CZ2 2366 C CZ3 . TRP A 301 ? 0.5360 1.0240 0.5753 -0.3201 -0.0077 -0.0067 315 TRP A CZ3 2367 C CH2 . TRP A 301 ? 0.5277 1.0269 0.5794 -0.3178 -0.0059 -0.0081 315 TRP A CH2 2368 N N . SER A 302 ? 0.5744 1.0904 0.5598 -0.3772 -0.0028 -0.0113 316 SER A N 2369 C CA . SER A 302 ? 0.5855 1.1149 0.5692 -0.3869 -0.0011 -0.0126 316 SER A CA 2370 C C . SER A 302 ? 0.6343 1.1488 0.5985 -0.3969 0.0024 -0.0162 316 SER A C 2371 O O . SER A 302 ? 0.6764 1.1981 0.6334 -0.4077 0.0036 -0.0174 316 SER A O 2372 C CB . SER A 302 ? 0.5502 1.0935 0.5512 -0.3815 -0.0001 -0.0127 316 SER A CB 2373 O OG . SER A 302 ? 0.5290 1.0590 0.5270 -0.3785 0.0031 -0.0155 316 SER A OG 2374 N N . GLY A 303 ? 0.5814 1.0750 0.5377 -0.3933 0.0041 -0.0179 317 GLY A N 2375 C CA . GLY A 303 ? 0.5758 1.0533 0.5145 -0.4018 0.0074 -0.0210 317 GLY A CA 2376 C C . GLY A 303 ? 0.5757 1.0546 0.5168 -0.4025 0.0105 -0.0229 317 GLY A C 2377 O O . GLY A 303 ? 0.5518 1.0172 0.4795 -0.4089 0.0134 -0.0252 317 GLY A O 2378 N N . HIS A 304 ? 0.5530 1.0482 0.5115 -0.3959 0.0100 -0.0219 318 HIS A N 2379 C CA . HIS A 304 ? 0.5550 1.0542 0.5174 -0.3962 0.0131 -0.0238 318 HIS A CA 2380 C C . HIS A 304 ? 0.5639 1.0436 0.5216 -0.3904 0.0148 -0.0251 318 HIS A C 2381 O O . HIS A 304 ? 0.5612 1.0339 0.5252 -0.3803 0.0130 -0.0239 318 HIS A O 2382 C CB . HIS A 304 ? 0.5614 1.0824 0.5452 -0.3895 0.0122 -0.0226 318 HIS A CB 2383 C CG . HIS A 304 ? 0.6227 1.1495 0.6119 -0.3895 0.0155 -0.0248 318 HIS A CG 2384 N ND1 . HIS A 304 ? 0.6562 1.1881 0.6611 -0.3790 0.0159 -0.0251 318 HIS A ND1 2385 C CD2 . HIS A 304 ? 0.6445 1.1730 0.6254 -0.3988 0.0188 -0.0270 318 HIS A CD2 2386 C CE1 . HIS A 304 ? 0.6213 1.1579 0.6270 -0.3819 0.0194 -0.0274 318 HIS A CE1 2387 N NE2 . HIS A 304 ? 0.6543 1.1890 0.6454 -0.3939 0.0211 -0.0285 318 HIS A NE2 2388 N N . TYR A 305 ? 0.5861 1.0570 0.5326 -0.3969 0.0180 -0.0272 319 TYR A N 2389 C CA . TYR A 305 ? 0.5932 1.0485 0.5365 -0.3919 0.0198 -0.0283 319 TYR A CA 2390 C C . TYR A 305 ? 0.6513 1.1128 0.5939 -0.3969 0.0233 -0.0301 319 TYR A C 2391 O O . TYR A 305 ? 0.6925 1.1652 0.6326 -0.4061 0.0244 -0.0307 319 TYR A O 2392 C CB . TYR A 305 ? 0.5903 1.0211 0.5161 -0.3950 0.0201 -0.0285 319 TYR A CB 2393 C CG . TYR A 305 ? 0.6487 1.0732 0.5580 -0.4084 0.0219 -0.0298 319 TYR A CG 2394 C CD1 . TYR A 305 ? 0.6508 1.0687 0.5514 -0.4148 0.0250 -0.0312 319 TYR A CD1 2395 C CD2 . TYR A 305 ? 0.6372 1.0620 0.5395 -0.4150 0.0206 -0.0295 319 TYR A CD2 2396 C CE1 . TYR A 305 ? 0.6657 1.0773 0.5520 -0.4269 0.0267 -0.0321 319 TYR A CE1 2397 C CE2 . TYR A 305 ? 0.6655 1.0842 0.5533 -0.4272 0.0224 -0.0309 319 TYR A CE2 2398 C CZ . TYR A 305 ? 0.6953 1.1072 0.5755 -0.4330 0.0254 -0.0322 319 TYR A CZ 2399 O OH . TYR A 305 ? 0.6137 1.0191 0.4802 -0.4453 0.0272 -0.0335 319 TYR A OH 2400 N N . VAL A 306 ? 0.6307 1.0855 0.5758 -0.3910 0.0249 -0.0310 320 VAL A N 2401 C CA . VAL A 306 ? 0.6234 1.0835 0.5673 -0.3955 0.0283 -0.0328 320 VAL A CA 2402 C C . VAL A 306 ? 0.5901 1.0289 0.5189 -0.3984 0.0302 -0.0333 320 VAL A C 2403 O O . VAL A 306 ? 0.5639 0.9894 0.4929 -0.3906 0.0296 -0.0329 320 VAL A O 2404 C CB . VAL A 306 ? 0.5843 1.0599 0.5469 -0.3865 0.0290 -0.0336 320 VAL A CB 2405 C CG1 . VAL A 306 ? 0.5689 1.0508 0.5300 -0.3914 0.0328 -0.0357 320 VAL A CG1 2406 C CG2 . VAL A 306 ? 0.5553 1.0518 0.5342 -0.3834 0.0269 -0.0326 320 VAL A CG2 2407 N N . VAL A 307 ? 0.5959 1.0314 0.5120 -0.4097 0.0325 -0.0340 321 VAL A N 2408 C CA . VAL A 307 ? 0.5979 1.0146 0.5004 -0.4134 0.0345 -0.0341 321 VAL A CA 2409 C C . VAL A 307 ? 0.6221 1.0462 0.5309 -0.4104 0.0369 -0.0353 321 VAL A C 2410 O O . VAL A 307 ? 0.5713 1.0043 0.4775 -0.4182 0.0395 -0.0362 321 VAL A O 2411 C CB . VAL A 307 ? 0.6435 1.0541 0.5306 -0.4270 0.0360 -0.0343 321 VAL A CB 2412 C CG1 . VAL A 307 ? 0.6656 1.0532 0.5384 -0.4300 0.0373 -0.0337 321 VAL A CG1 2413 C CG2 . VAL A 307 ? 0.6383 1.0482 0.5215 -0.4312 0.0340 -0.0339 321 VAL A CG2 2414 N N . ALA A 308 ? 0.6431 1.0639 0.5601 -0.3995 0.0362 -0.0353 322 ALA A N 2415 C CA . ALA A 308 ? 0.5997 1.0310 0.5243 -0.3960 0.0385 -0.0370 322 ALA A CA 2416 C C . ALA A 308 ? 0.6540 1.0765 0.5633 -0.4041 0.0413 -0.0376 322 ALA A C 2417 O O . ALA A 308 ? 0.6437 1.0475 0.5376 -0.4095 0.0410 -0.0362 322 ALA A O 2418 C CB . ALA A 308 ? 0.5748 1.0044 0.5121 -0.3823 0.0368 -0.0370 322 ALA A CB 2419 N N . SER A 309 ? 0.6612 1.0975 0.5755 -0.4046 0.0440 -0.0396 323 SER A N 2420 C CA . SER A 309 ? 0.7044 1.1355 0.6055 -0.4122 0.0468 -0.0402 323 SER A CA 2421 C C . SER A 309 ? 0.6710 1.0784 0.5588 -0.4114 0.0459 -0.0385 323 SER A C 2422 O O . SER A 309 ? 0.6624 1.0583 0.5345 -0.4210 0.0470 -0.0373 323 SER A O 2423 C CB . SER A 309 ? 0.7372 1.1862 0.6481 -0.4095 0.0496 -0.0431 323 SER A CB 2424 O OG . SER A 309 ? 0.7828 1.2539 0.7080 -0.4090 0.0506 -0.0448 323 SER A OG 2425 N N . PRO A 310 ? 0.6254 1.0253 0.5202 -0.4000 0.0438 -0.0382 324 PRO A N 2426 C CA . PRO A 310 ? 0.5836 0.9614 0.4665 -0.3992 0.0429 -0.0364 324 PRO A CA 2427 C C . PRO A 310 ? 0.5981 0.9560 0.4660 -0.4063 0.0418 -0.0339 324 PRO A C 2428 O O . PRO A 310 ? 0.6137 0.9548 0.4687 -0.4100 0.0421 -0.0324 324 PRO A O 2429 C CB . PRO A 310 ? 0.5776 0.9526 0.4731 -0.3855 0.0405 -0.0364 324 PRO A CB 2430 C CG . PRO A 310 ? 0.5757 0.9736 0.4891 -0.3795 0.0414 -0.0389 324 PRO A CG 2431 C CD . PRO A 310 ? 0.5723 0.9839 0.4865 -0.3876 0.0424 -0.0393 324 PRO A CD 2432 N N . ILE A 311 ? 0.5675 0.9273 0.4370 -0.4085 0.0406 -0.0336 325 ILE A N 2433 C CA . ILE A 311 ? 0.5824 0.9251 0.4380 -0.4163 0.0401 -0.0319 325 ILE A CA 2434 C C . ILE A 311 ? 0.6689 1.0062 0.5101 -0.4283 0.0426 -0.0313 325 ILE A C 2435 O O . ILE A 311 ? 0.6695 0.9865 0.4981 -0.4321 0.0425 -0.0295 325 ILE A O 2436 C CB . ILE A 311 ? 0.6162 0.9667 0.4753 -0.4194 0.0391 -0.0323 325 ILE A CB 2437 C CG1 . ILE A 311 ? 0.6078 0.9619 0.4802 -0.4081 0.0363 -0.0322 325 ILE A CG1 2438 C CG2 . ILE A 311 ? 0.6029 0.9362 0.4472 -0.4286 0.0392 -0.0312 325 ILE A CG2 2439 C CD1 . ILE A 311 ? 0.5606 0.8936 0.4288 -0.4018 0.0342 -0.0308 325 ILE A CD1 2440 N N . TRP A 312 ? 0.6086 0.9642 0.4525 -0.4340 0.0450 -0.0328 326 TRP A N 2441 C CA . TRP A 312 ? 0.6783 1.0308 0.5092 -0.4462 0.0474 -0.0320 326 TRP A CA 2442 C C . TRP A 312 ? 0.6722 1.0171 0.4965 -0.4460 0.0484 -0.0312 326 TRP A C 2443 O O . TRP A 312 ? 0.6743 1.0065 0.4852 -0.4545 0.0494 -0.0291 326 TRP A O 2444 C CB . TRP A 312 ? 0.6358 1.0106 0.4717 -0.4531 0.0496 -0.0338 326 TRP A CB 2445 C CG . TRP A 312 ? 0.6347 1.0158 0.4764 -0.4535 0.0482 -0.0342 326 TRP A CG 2446 C CD1 . TRP A 312 ? 0.6232 1.0242 0.4800 -0.4484 0.0476 -0.0358 326 TRP A CD1 2447 C CD2 . TRP A 312 ? 0.6456 1.0125 0.4783 -0.4591 0.0471 -0.0330 326 TRP A CD2 2448 N NE1 . TRP A 312 ? 0.6266 1.0270 0.4836 -0.4509 0.0461 -0.0354 326 TRP A NE1 2449 C CE2 . TRP A 312 ? 0.6402 1.0199 0.4823 -0.4575 0.0458 -0.0340 326 TRP A CE2 2450 C CE3 . TRP A 312 ? 0.6600 1.0043 0.4779 -0.4654 0.0471 -0.0312 326 TRP A CE3 2451 C CZ2 . TRP A 312 ? 0.6841 1.0555 0.5206 -0.4623 0.0446 -0.0336 326 TRP A CZ2 2452 C CZ3 . TRP A 312 ? 0.6681 1.0038 0.4813 -0.4697 0.0462 -0.0310 326 TRP A CZ3 2453 C CH2 . TRP A 312 ? 0.7253 1.0747 0.5473 -0.4683 0.0450 -0.0324 326 TRP A CH2 2454 N N . VAL A 313 ? 0.6476 0.9999 0.4817 -0.4363 0.0481 -0.0325 327 VAL A N 2455 C CA . VAL A 313 ? 0.6457 0.9908 0.4736 -0.4357 0.0488 -0.0317 327 VAL A CA 2456 C C . VAL A 313 ? 0.6905 1.0088 0.5079 -0.4346 0.0467 -0.0286 327 VAL A C 2457 O O . VAL A 313 ? 0.6765 0.9823 0.4815 -0.4408 0.0474 -0.0263 327 VAL A O 2458 C CB . VAL A 313 ? 0.6305 0.9889 0.4719 -0.4251 0.0489 -0.0342 327 VAL A CB 2459 C CG1 . VAL A 313 ? 0.6059 0.9552 0.4403 -0.4241 0.0492 -0.0334 327 VAL A CG1 2460 C CG2 . VAL A 313 ? 0.5948 0.9793 0.4464 -0.4268 0.0514 -0.0375 327 VAL A CG2 2461 N N . SER A 314 ? 0.6073 0.9169 0.4298 -0.4268 0.0442 -0.0283 328 SER A N 2462 C CA . SER A 314 ? 0.6365 0.9209 0.4501 -0.4257 0.0424 -0.0256 328 SER A CA 2463 C C . SER A 314 ? 0.6756 0.9466 0.4747 -0.4378 0.0434 -0.0235 328 SER A C 2464 O O . SER A 314 ? 0.7127 0.9663 0.5012 -0.4410 0.0434 -0.0208 328 SER A O 2465 C CB . SER A 314 ? 0.5978 0.8783 0.4196 -0.4174 0.0400 -0.0261 328 SER A CB 2466 O OG . SER A 314 ? 0.5772 0.8712 0.4139 -0.4066 0.0391 -0.0278 328 SER A OG 2467 N N . ALA A 315 ? 0.6631 0.9426 0.4624 -0.4444 0.0443 -0.0245 329 ALA A N 2468 C CA . ALA A 315 ? 0.7090 0.9776 0.4961 -0.4561 0.0455 -0.0229 329 ALA A CA 2469 C C . ALA A 315 ? 0.7258 0.9895 0.5025 -0.4642 0.0473 -0.0206 329 ALA A C 2470 O O . ALA A 315 ? 0.7360 0.9803 0.5017 -0.4700 0.0474 -0.0178 329 ALA A O 2471 C CB . ALA A 315 ? 0.7079 0.9926 0.4986 -0.4624 0.0466 -0.0249 329 ALA A CB 2472 N N . HIS A 316 ? 0.7255 1.0066 0.5060 -0.4643 0.0488 -0.0218 330 HIS A N 2473 C CA . HIS A 316 ? 0.7825 1.0616 0.5535 -0.4721 0.0506 -0.0197 330 HIS A CA 2474 C C . HIS A 316 ? 0.7929 1.0491 0.5552 -0.4701 0.0492 -0.0161 330 HIS A C 2475 O O . HIS A 316 ? 0.7863 1.0347 0.5384 -0.4778 0.0502 -0.0130 330 HIS A O 2476 C CB . HIS A 316 ? 0.8030 1.1049 0.5810 -0.4704 0.0523 -0.0222 330 HIS A CB 2477 C CG . HIS A 316 ? 0.8774 1.2004 0.6589 -0.4777 0.0548 -0.0244 330 HIS A CG 2478 N ND1 . HIS A 316 ? 0.9341 1.2579 0.7060 -0.4899 0.0570 -0.0227 330 HIS A ND1 2479 C CD2 . HIS A 316 ? 0.8988 1.2428 0.6927 -0.4746 0.0554 -0.0279 330 HIS A CD2 2480 C CE1 . HIS A 316 ? 0.9388 1.2835 0.7169 -0.4940 0.0590 -0.0253 330 HIS A CE1 2481 N NE2 . HIS A 316 ? 0.9347 1.2919 0.7263 -0.4848 0.0580 -0.0284 330 HIS A NE2 2482 N N . THR A 317 ? 0.7557 1.0017 0.5227 -0.4596 0.0468 -0.0162 331 THR A N 2483 C CA . THR A 317 ? 0.7142 0.9372 0.4738 -0.4570 0.0452 -0.0127 331 THR A CA 2484 C C . THR A 317 ? 0.7550 0.9572 0.5118 -0.4558 0.0437 -0.0114 331 THR A C 2485 O O . THR A 317 ? 0.8161 0.9985 0.5630 -0.4609 0.0438 -0.0078 331 THR A O 2486 C CB . THR A 317 ? 0.7144 0.9401 0.4809 -0.4461 0.0437 -0.0135 331 THR A CB 2487 O OG1 . THR A 317 ? 0.7058 0.9507 0.4745 -0.4478 0.0455 -0.0151 331 THR A OG1 2488 C CG2 . THR A 317 ? 0.6940 0.8955 0.4528 -0.4438 0.0420 -0.0095 331 THR A CG2 2489 N N . THR A 318 ? 0.7050 0.9120 0.4706 -0.4493 0.0426 -0.0141 332 THR A N 2490 C CA . THR A 318 ? 0.7234 0.9116 0.4873 -0.4468 0.0412 -0.0135 332 THR A CA 2491 C C . THR A 318 ? 0.7541 0.9315 0.5093 -0.4573 0.0426 -0.0124 332 THR A C 2492 O O . THR A 318 ? 0.7595 0.9149 0.5090 -0.4575 0.0420 -0.0104 332 THR A O 2493 C CB . THR A 318 ? 0.7008 0.8974 0.4765 -0.4373 0.0396 -0.0165 332 THR A CB 2494 O OG1 . THR A 318 ? 0.6528 0.8706 0.4342 -0.4408 0.0407 -0.0192 332 THR A OG1 2495 C CG2 . THR A 318 ? 0.6567 0.8587 0.4413 -0.4258 0.0381 -0.0170 332 THR A CG2 2496 N N . GLN A 319 ? 0.7844 0.9767 0.5389 -0.4659 0.0445 -0.0138 333 GLN A N 2497 C CA . GLN A 319 ? 0.7972 0.9802 0.5438 -0.4765 0.0460 -0.0129 333 GLN A CA 2498 C C . GLN A 319 ? 0.8119 0.9774 0.5476 -0.4836 0.0470 -0.0086 333 GLN A C 2499 O O . GLN A 319 ? 0.8395 0.9889 0.5687 -0.4899 0.0478 -0.0070 333 GLN A O 2500 C CB . GLN A 319 ? 0.7777 0.9820 0.5267 -0.4842 0.0477 -0.0153 333 GLN A CB 2501 C CG . GLN A 319 ? 0.7826 1.0048 0.5430 -0.4777 0.0466 -0.0190 333 GLN A CG 2502 C CD . GLN A 319 ? 0.8281 1.0602 0.5888 -0.4856 0.0477 -0.0210 333 GLN A CD 2503 O OE1 . GLN A 319 ? 0.9025 1.1257 0.6548 -0.4958 0.0493 -0.0198 333 GLN A OE1 2504 N NE2 . GLN A 319 ? 0.7809 1.0315 0.5519 -0.4811 0.0468 -0.0237 333 GLN A NE2 2505 N N . PHE A 320 ? 0.7981 0.9664 0.5321 -0.4824 0.0470 -0.0065 334 PHE A N 2506 C CA . PHE A 320 ? 0.8201 0.9769 0.5440 -0.4904 0.0482 -0.0020 334 PHE A CA 2507 C C . PHE A 320 ? 0.8410 0.9803 0.5618 -0.4843 0.0464 0.0016 334 PHE A C 2508 O O . PHE A 320 ? 0.8219 0.9525 0.5350 -0.4897 0.0470 0.0061 334 PHE A O 2509 C CB . PHE A 320 ? 0.7661 0.9436 0.4891 -0.4974 0.0501 -0.0022 334 PHE A CB 2510 C CG . PHE A 320 ? 0.8431 1.0401 0.5708 -0.5023 0.0517 -0.0059 334 PHE A CG 2511 C CD1 . PHE A 320 ? 0.8683 1.0591 0.5915 -0.5114 0.0531 -0.0055 334 PHE A CD1 2512 C CD2 . PHE A 320 ? 0.8066 1.0278 0.5438 -0.4978 0.0518 -0.0098 334 PHE A CD2 2513 C CE1 . PHE A 320 ? 0.8787 1.0876 0.6062 -0.5162 0.0544 -0.0088 334 PHE A CE1 2514 C CE2 . PHE A 320 ? 0.8324 1.0717 0.5746 -0.5022 0.0531 -0.0129 334 PHE A CE2 2515 C CZ . PHE A 320 ? 0.7692 1.0024 0.5062 -0.5116 0.0543 -0.0123 334 PHE A CZ 2516 N N . THR A 321 ? 0.8057 0.9405 0.5329 -0.4730 0.0442 0.0000 335 THR A N 2517 C CA . THR A 321 ? 0.8125 0.9290 0.5379 -0.4662 0.0423 0.0031 335 THR A CA 2518 C C . THR A 321 ? 0.8107 0.9125 0.5404 -0.4582 0.0407 0.0018 335 THR A C 2519 O O . THR A 321 ? 0.7946 0.9053 0.5303 -0.4560 0.0407 -0.0020 335 THR A O 2520 C CB . THR A 321 ? 0.8118 0.9408 0.5418 -0.4589 0.0411 0.0024 335 THR A CB 2521 O OG1 . THR A 321 ? 0.8064 0.9516 0.5475 -0.4511 0.0405 -0.0024 335 THR A OG1 2522 C CG2 . THR A 321 ? 0.7566 0.9007 0.4824 -0.4666 0.0429 0.0033 335 THR A CG2 2523 N N . GLN A 322 ? 0.8375 0.9173 0.5642 -0.4540 0.0394 0.0052 336 GLN A N 2524 C CA . GLN A 322 ? 0.8403 0.9056 0.5716 -0.4454 0.0378 0.0041 336 GLN A CA 2525 C C . GLN A 322 ? 0.8574 0.9093 0.5892 -0.4371 0.0357 0.0071 336 GLN A C 2526 O O . GLN A 322 ? 0.8962 0.9413 0.6217 -0.4403 0.0356 0.0114 336 GLN A O 2527 C CB . GLN A 322 ? 0.8869 0.9340 0.6138 -0.4509 0.0390 0.0050 336 GLN A CB 2528 C CG . GLN A 322 ? 0.8946 0.9530 0.6222 -0.4577 0.0408 0.0013 336 GLN A CG 2529 C CD . GLN A 322 ? 0.8978 0.9669 0.6340 -0.4502 0.0397 -0.0034 336 GLN A CD 2530 O OE1 . GLN A 322 ? 0.8675 0.9274 0.6083 -0.4407 0.0380 -0.0039 336 GLN A OE1 2531 N NE2 . GLN A 322 ? 0.9003 0.9891 0.6391 -0.4545 0.0407 -0.0066 336 GLN A NE2 2532 N N . PRO A 323 ? 0.8111 0.8595 0.5505 -0.4263 0.0338 0.0050 337 PRO A N 2533 C CA . PRO A 323 ? 0.7769 0.8109 0.5174 -0.4179 0.0317 0.0078 337 PRO A CA 2534 C C . PRO A 323 ? 0.7896 0.7991 0.5225 -0.4218 0.0319 0.0127 337 PRO A C 2535 O O . PRO A 323 ? 0.8682 0.8661 0.5993 -0.4256 0.0332 0.0125 337 PRO A O 2536 C CB . PRO A 323 ? 0.7381 0.7691 0.4875 -0.4078 0.0303 0.0046 337 PRO A CB 2537 C CG . PRO A 323 ? 0.7203 0.7736 0.4753 -0.4088 0.0312 0.0000 337 PRO A CG 2538 C CD . PRO A 323 ? 0.7782 0.8370 0.5258 -0.4214 0.0336 0.0003 337 PRO A CD 2539 N N . GLY A 324 ? 0.8014 0.8475 0.5609 -0.4202 0.1188 0.0628 338 GLY A N 2540 C CA . GLY A 324 ? 0.7867 0.8225 0.5500 -0.4190 0.1247 0.0694 338 GLY A CA 2541 C C . GLY A 324 ? 0.8203 0.8574 0.5872 -0.4182 0.1297 0.0775 338 GLY A C 2542 O O . GLY A 324 ? 0.8301 0.8606 0.5995 -0.4162 0.1343 0.0850 338 GLY A O 2543 N N . TRP A 325 ? 0.8191 0.8647 0.5867 -0.4198 0.1290 0.0763 339 TRP A N 2544 C CA . TRP A 325 ? 0.8548 0.9036 0.6243 -0.4187 0.1330 0.0836 339 TRP A CA 2545 C C . TRP A 325 ? 0.8492 0.9028 0.6115 -0.4134 0.1312 0.0891 339 TRP A C 2546 O O . TRP A 325 ? 0.8159 0.8706 0.5722 -0.4109 0.1267 0.0868 339 TRP A O 2547 C CB . TRP A 325 ? 0.9011 0.9591 0.6727 -0.4214 0.1319 0.0803 339 TRP A CB 2548 C CG . TRP A 325 ? 0.9539 1.0080 0.7334 -0.4266 0.1351 0.0775 339 TRP A CG 2549 C CD1 . TRP A 325 ? 0.9721 1.0178 0.7553 -0.4299 0.1361 0.0730 339 TRP A CD1 2550 C CD2 . TRP A 325 ? 0.9919 1.0505 0.7768 -0.4293 0.1380 0.0788 339 TRP A CD2 2551 N NE1 . TRP A 325 ? 1.0061 1.0510 0.7962 -0.4346 0.1392 0.0713 339 TRP A NE1 2552 C CE2 . TRP A 325 ? 1.0015 1.0543 0.7929 -0.4342 0.1403 0.0750 339 TRP A CE2 2553 C CE3 . TRP A 325 ? 1.0356 1.1025 0.8204 -0.4280 0.1390 0.0826 339 TRP A CE3 2554 C CZ2 . TRP A 325 ? 1.0376 1.0929 0.8354 -0.4380 0.1433 0.0752 339 TRP A CZ2 2555 C CZ3 . TRP A 325 ? 1.0308 1.0999 0.8223 -0.4316 0.1422 0.0829 339 TRP A CZ3 2556 C CH2 . TRP A 325 ? 1.0297 1.0932 0.8276 -0.4365 0.1441 0.0793 339 TRP A CH2 2557 N N . TYR A 326 ? 0.8237 0.8802 0.5862 -0.4118 0.1346 0.0962 340 TYR A N 2558 C CA . TYR A 326 ? 0.8401 0.9024 0.5951 -0.4071 0.1328 0.1010 340 TYR A CA 2559 C C . TYR A 326 ? 0.8309 0.9032 0.5841 -0.4067 0.1330 0.1018 340 TYR A C 2560 O O . TYR A 326 ? 0.8345 0.9075 0.5933 -0.4093 0.1368 0.1030 340 TYR A O 2561 C CB . TYR A 326 ? 0.8515 0.9075 0.6069 -0.4042 0.1367 0.1108 340 TYR A CB 2562 C CG . TYR A 326 ? 0.8591 0.9073 0.6139 -0.4027 0.1355 0.1111 340 TYR A CG 2563 C CD1 . TYR A 326 ? 0.8856 0.9240 0.6474 -0.4057 0.1380 0.1083 340 TYR A CD1 2564 C CD2 . TYR A 326 ? 0.8655 0.9160 0.6131 -0.3983 0.1321 0.1143 340 TYR A CD2 2565 C CE1 . TYR A 326 ? 0.9021 0.9331 0.6641 -0.4043 0.1375 0.1086 340 TYR A CE1 2566 C CE2 . TYR A 326 ? 0.9035 0.9470 0.6511 -0.3968 0.1312 0.1149 340 TYR A CE2 2567 C CZ . TYR A 326 ? 0.9383 0.9719 0.6934 -0.3998 0.1341 0.1121 340 TYR A CZ 2568 O OH . TYR A 326 ? 0.9982 1.0245 0.7540 -0.3983 0.1337 0.1126 340 TYR A OH 2569 N N . TYR A 327 ? 0.8550 0.9350 0.6006 -0.4036 0.1291 0.1008 341 TYR A N 2570 C CA . TYR A 327 ? 0.8942 0.9829 0.6375 -0.4026 0.1302 0.1025 341 TYR A CA 2571 C C . TYR A 327 ? 0.8891 0.9757 0.6314 -0.4006 0.1347 0.1122 341 TYR A C 2572 O O . TYR A 327 ? 0.8077 0.8888 0.5479 -0.3983 0.1350 0.1175 341 TYR A O 2573 C CB . TYR A 327 ? 0.8737 0.9706 0.6095 -0.3997 0.1252 0.0984 341 TYR A CB 2574 C CG . TYR A 327 ? 0.8461 0.9484 0.5839 -0.4017 0.1216 0.0897 341 TYR A CG 2575 C CD1 . TYR A 327 ? 0.8392 0.9483 0.5812 -0.4036 0.1232 0.0877 341 TYR A CD1 2576 C CD2 . TYR A 327 ? 0.8272 0.9282 0.5630 -0.4017 0.1166 0.0839 341 TYR A CD2 2577 C CE1 . TYR A 327 ? 0.8028 0.9175 0.5477 -0.4053 0.1199 0.0807 341 TYR A CE1 2578 C CE2 . TYR A 327 ? 0.8188 0.9254 0.5568 -0.4035 0.1131 0.0766 341 TYR A CE2 2579 C CZ . TYR A 327 ? 0.8261 0.9397 0.5688 -0.4052 0.1148 0.0753 341 TYR A CZ 2580 O OH . TYR A 327 ? 0.7938 0.9136 0.5397 -0.4069 0.1114 0.0691 341 TYR A OH 2581 N N . LEU A 328 ? 0.8088 0.8996 0.5530 -0.4015 0.1384 0.1150 342 LEU A N 2582 C CA . LEU A 328 ? 0.8190 0.9094 0.5610 -0.3994 0.1422 0.1241 342 LEU A CA 2583 C C . LEU A 328 ? 0.9086 1.0060 0.6407 -0.3957 0.1391 0.1250 342 LEU A C 2584 O O . LEU A 328 ? 0.8067 0.9099 0.5351 -0.3950 0.1351 0.1182 342 LEU A O 2585 C CB . LEU A 328 ? 0.8257 0.9184 0.5728 -0.4019 0.1472 0.1264 342 LEU A CB 2586 C CG . LEU A 328 ? 0.9280 1.0140 0.6850 -0.4058 0.1508 0.1261 342 LEU A CG 2587 C CD1 . LEU A 328 ? 0.9694 1.0590 0.7306 -0.4079 0.1555 0.1285 342 LEU A CD1 2588 C CD2 . LEU A 328 ? 0.9248 1.0009 0.6849 -0.4053 0.1535 0.1325 342 LEU A CD2 2589 N N . LYS A 329 ? 0.9234 1.0206 0.6516 -0.3933 0.1411 0.1333 343 LYS A N 2590 C CA . LYS A 329 ? 0.9454 1.0500 0.6642 -0.3903 0.1387 0.1342 343 LYS A CA 2591 C C . LYS A 329 ? 0.9375 1.0499 0.6558 -0.3916 0.1409 0.1313 343 LYS A C 2592 O O . LYS A 329 ? 0.9569 1.0762 0.6685 -0.3900 0.1389 0.1282 343 LYS A O 2593 C CB . LYS A 329 ? 0.9694 1.0724 0.6844 -0.3878 0.1401 0.1444 343 LYS A CB 2594 C CG . LYS A 329 ? 1.0023 1.0987 0.7175 -0.3859 0.1377 0.1475 343 LYS A CG 2595 C CD . LYS A 329 ? 1.0154 1.1121 0.7262 -0.3829 0.1382 0.1578 343 LYS A CD 2596 C CE . LYS A 329 ? 1.0490 1.1391 0.7613 -0.3809 0.1361 0.1610 343 LYS A CE 2597 N NZ . LYS A 329 ? 1.0731 1.1650 0.7806 -0.3776 0.1352 0.1708 343 LYS A NZ 2598 N N . THR A 330 ? 0.8987 1.0095 0.6244 -0.3946 0.1453 0.1321 344 THR A N 2599 C CA . THR A 330 ? 0.8899 1.0074 0.6161 -0.3959 0.1483 0.1306 344 THR A CA 2600 C C . THR A 330 ? 0.8583 0.9801 0.5887 -0.3978 0.1468 0.1215 344 THR A C 2601 O O . THR A 330 ? 0.8593 0.9798 0.5980 -0.4009 0.1490 0.1198 344 THR A O 2602 C CB . THR A 330 ? 0.9325 1.0471 0.6643 -0.3980 0.1544 0.1372 344 THR A CB 2603 O OG1 . THR A 330 ? 0.9478 1.0547 0.6884 -0.4004 0.1557 0.1373 344 THR A OG1 2604 C CG2 . THR A 330 ? 0.8915 1.0049 0.6179 -0.3958 0.1561 0.1466 344 THR A CG2 2605 N N . VAL A 331 ? 0.8121 0.9394 0.5371 -0.3959 0.1430 0.1160 345 VAL A N 2606 C CA . VAL A 331 ? 0.8598 0.9928 0.5885 -0.3971 0.1419 0.1083 345 VAL A CA 2607 C C . VAL A 331 ? 0.8570 0.9976 0.5791 -0.3949 0.1417 0.1060 345 VAL A C 2608 O O . VAL A 331 ? 0.8046 0.9454 0.5183 -0.3924 0.1406 0.1088 345 VAL A O 2609 C CB . VAL A 331 ? 0.8399 0.9708 0.5707 -0.3975 0.1366 0.1022 345 VAL A CB 2610 C CG1 . VAL A 331 ? 0.8334 0.9558 0.5697 -0.3997 0.1368 0.1041 345 VAL A CG1 2611 C CG2 . VAL A 331 ? 0.7870 0.9186 0.5093 -0.3941 0.1320 0.1006 345 VAL A CG2 2612 N N . GLY A 332 ? 0.8321 0.9788 0.5582 -0.3959 0.1429 0.1009 346 GLY A N 2613 C CA . GLY A 332 ? 0.8167 0.9701 0.5375 -0.3939 0.1433 0.0977 346 GLY A CA 2614 C C . GLY A 332 ? 0.8329 0.9927 0.5608 -0.3953 0.1462 0.0933 346 GLY A C 2615 O O . GLY A 332 ? 0.8330 0.9928 0.5700 -0.3976 0.1463 0.0916 346 GLY A O 2616 N N . HIS A 333 ? 0.8337 0.9990 0.5577 -0.3939 0.1487 0.0914 347 HIS A N 2617 C CA . HIS A 333 ? 0.8371 1.0088 0.5681 -0.3948 0.1522 0.0875 347 HIS A CA 2618 C C . HIS A 333 ? 0.8785 1.0515 0.6132 -0.3967 0.1588 0.0914 347 HIS A C 2619 O O . HIS A 333 ? 0.8923 1.0631 0.6210 -0.3967 0.1612 0.0965 347 HIS A O 2620 C CB . HIS A 333 ? 0.8548 1.0313 0.5805 -0.3924 0.1521 0.0827 347 HIS A CB 2621 C CG . HIS A 333 ? 0.9196 1.0961 0.6440 -0.3907 0.1461 0.0778 347 HIS A CG 2622 N ND1 . HIS A 333 ? 0.9498 1.1314 0.6798 -0.3901 0.1457 0.0721 347 HIS A ND1 2623 C CD2 . HIS A 333 ? 0.9391 1.1112 0.6576 -0.3894 0.1404 0.0780 347 HIS A CD2 2624 C CE1 . HIS A 333 ? 0.9258 1.1061 0.6530 -0.3887 0.1398 0.0688 347 HIS A CE1 2625 N NE2 . HIS A 333 ? 0.9314 1.1058 0.6515 -0.3882 0.1366 0.0721 347 HIS A NE2 2626 N N . LEU A 334 ? 0.8754 1.0526 0.6205 -0.3984 0.1618 0.0895 348 LEU A N 2627 C CA . LEU A 334 ? 0.8599 1.0391 0.6094 -0.4002 0.1683 0.0927 348 LEU A CA 2628 C C . LEU A 334 ? 0.8548 1.0389 0.5998 -0.3989 0.1729 0.0908 348 LEU A C 2629 O O . LEU A 334 ? 0.8733 1.0606 0.6162 -0.3970 0.1715 0.0859 348 LEU A O 2630 C CB . LEU A 334 ? 0.8250 1.0069 0.5880 -0.4027 0.1697 0.0917 348 LEU A CB 2631 C CG . LEU A 334 ? 0.8152 0.9917 0.5822 -0.4046 0.1656 0.0932 348 LEU A CG 2632 C CD1 . LEU A 334 ? 0.8092 0.9892 0.5894 -0.4071 0.1657 0.0915 348 LEU A CD1 2633 C CD2 . LEU A 334 ? 0.8345 1.0048 0.5979 -0.4057 0.1677 0.0996 348 LEU A CD2 2634 N N . GLU A 335 ? 0.8512 1.0357 0.5948 -0.4001 0.1786 0.0946 349 GLU A N 2635 C CA . GLU A 335 ? 0.8425 1.0311 0.5809 -0.3994 0.1836 0.0931 349 GLU A CA 2636 C C . GLU A 335 ? 0.8338 1.0284 0.5796 -0.3987 0.1864 0.0872 349 GLU A C 2637 O O . GLU A 335 ? 0.8305 1.0275 0.5706 -0.3970 0.1872 0.0832 349 GLU A O 2638 C CB . GLU A 335 ? 0.8395 1.0278 0.5772 -0.4014 0.1896 0.0983 349 GLU A CB 2639 N N . LYS A 336 ? 0.8675 1.0648 0.6265 -0.4001 0.1880 0.0869 350 LYS A N 2640 C CA . LYS A 336 ? 0.8827 1.0862 0.6513 -0.3996 0.1913 0.0826 350 LYS A CA 2641 C C . LYS A 336 ? 0.8615 1.0667 0.6365 -0.3985 0.1855 0.0789 350 LYS A C 2642 O O . LYS A 336 ? 0.8223 1.0329 0.6088 -0.3984 0.1874 0.0766 350 LYS A O 2643 C CB . LYS A 336 ? 0.9152 1.1220 0.6956 -0.4017 0.1973 0.0850 350 LYS A CB 2644 C CG . LYS A 336 ? 0.9554 1.1607 0.7304 -0.4031 0.2031 0.0890 350 LYS A CG 2645 C CD . LYS A 336 ? 1.0167 1.2240 0.7835 -0.4020 0.2080 0.0864 350 LYS A CD 2646 C CE . LYS A 336 ? 1.0563 1.2698 0.8338 -0.4016 0.2144 0.0828 350 LYS A CE 2647 N NZ . LYS A 336 ? 1.0825 1.2976 0.8521 -0.4007 0.2196 0.0793 350 LYS A NZ 2648 N N . GLY A 337 ? 0.8526 1.0533 0.6204 -0.3977 0.1786 0.0786 351 GLY A N 2649 C CA . GLY A 337 ? 0.8505 1.0523 0.6224 -0.3968 0.1727 0.0749 351 GLY A CA 2650 C C . GLY A 337 ? 0.8139 1.0125 0.5905 -0.3988 0.1676 0.0769 351 GLY A C 2651 O O . GLY A 337 ? 0.8060 1.0033 0.5878 -0.4013 0.1696 0.0806 351 GLY A O 2652 N N . GLY A 338 ? 0.8434 1.0406 0.6183 -0.3979 0.1610 0.0740 352 GLY A N 2653 C CA . GLY A 338 ? 0.8323 1.0258 0.6104 -0.4000 0.1559 0.0751 352 GLY A CA 2654 C C . GLY A 338 ? 0.8322 1.0177 0.5995 -0.3998 0.1532 0.0778 352 GLY A C 2655 O O . GLY A 338 ? 0.8507 1.0345 0.6081 -0.3978 0.1545 0.0788 352 GLY A O 2656 N N . SER A 339 ? 0.8019 0.9826 0.5714 -0.4018 0.1495 0.0790 353 SER A N 2657 C CA . SER A 339 ? 0.8162 0.9892 0.5769 -0.4013 0.1467 0.0814 353 SER A CA 2658 C C . SER A 339 ? 0.8237 0.9910 0.5891 -0.4044 0.1464 0.0845 353 SER A C 2659 O O . SER A 339 ? 0.7717 0.9413 0.5469 -0.4071 0.1470 0.0837 353 SER A O 2660 C CB . SER A 339 ? 0.8405 1.0122 0.5956 -0.3993 0.1404 0.0774 353 SER A CB 2661 O OG . SER A 339 ? 0.7511 0.9254 0.5138 -0.4007 0.1367 0.0734 353 SER A OG 2662 N N . TYR A 340 ? 0.7792 0.9392 0.5380 -0.4039 0.1457 0.0882 354 TYR A N 2663 C CA . TYR A 340 ? 0.8426 0.9960 0.6055 -0.4067 0.1460 0.0912 354 TYR A CA 2664 C C . TYR A 340 ? 0.8791 1.0249 0.6354 -0.4055 0.1421 0.0920 354 TYR A C 2665 O O . TYR A 340 ? 0.9015 1.0459 0.6491 -0.4026 0.1416 0.0943 354 TYR A O 2666 C CB . TYR A 340 ? 0.8725 1.0241 0.6366 -0.4078 0.1520 0.0972 354 TYR A CB 2667 C CG . TYR A 340 ? 0.8888 1.0379 0.6434 -0.4053 0.1539 0.1022 354 TYR A CG 2668 C CD1 . TYR A 340 ? 0.9084 1.0630 0.6576 -0.4032 0.1561 0.1021 354 TYR A CD1 2669 C CD2 . TYR A 340 ? 0.9115 1.0528 0.6628 -0.4051 0.1537 0.1073 354 TYR A CD2 2670 C CE1 . TYR A 340 ? 0.9250 1.0779 0.6650 -0.4012 0.1574 0.1068 354 TYR A CE1 2671 C CE2 . TYR A 340 ? 0.9259 1.0656 0.6689 -0.4028 0.1550 0.1127 354 TYR A CE2 2672 C CZ . TYR A 340 ? 0.9167 1.0625 0.6537 -0.4010 0.1566 0.1123 354 TYR A CZ 2673 O OH . TYR A 340 ? 0.9088 1.0538 0.6372 -0.3990 0.1576 0.1177 354 TYR A OH 2674 N N . VAL A 341 ? 0.8745 1.0159 0.6351 -0.4078 0.1393 0.0900 355 VAL A N 2675 C CA . VAL A 341 ? 0.7818 0.9149 0.5381 -0.4072 0.1369 0.0915 355 VAL A CA 2676 C C . VAL A 341 ? 0.8892 1.0152 0.6515 -0.4104 0.1400 0.0949 355 VAL A C 2677 O O . VAL A 341 ? 0.7911 0.9191 0.5613 -0.4135 0.1422 0.0941 355 VAL A O 2678 C CB . VAL A 341 ? 0.8356 0.9681 0.5901 -0.4068 0.1308 0.0856 355 VAL A CB 2679 C CG1 . VAL A 341 ? 0.8214 0.9612 0.5711 -0.4038 0.1280 0.0819 355 VAL A CG1 2680 C CG2 . VAL A 341 ? 0.7673 0.9000 0.5303 -0.4108 0.1291 0.0813 355 VAL A CG2 2681 N N . ALA A 342 ? 0.8938 1.0116 0.6528 -0.4095 0.1404 0.0989 356 ALA A N 2682 C CA . ALA A 342 ? 0.8669 0.9768 0.6317 -0.4122 0.1438 0.1024 356 ALA A CA 2683 C C . ALA A 342 ? 0.8538 0.9550 0.6168 -0.4118 0.1416 0.1023 356 ALA A C 2684 O O . ALA A 342 ? 0.8012 0.9015 0.5570 -0.4084 0.1392 0.1037 356 ALA A O 2685 C CB . ALA A 342 ? 0.8146 0.9230 0.5791 -0.4115 0.1494 0.1102 356 ALA A CB 2686 N N . LEU A 343 ? 0.8541 0.9490 0.6236 -0.4153 0.1425 0.1004 357 LEU A N 2687 C CA . LEU A 343 ? 0.8587 0.9446 0.6277 -0.4153 0.1411 0.0998 357 LEU A CA 2688 C C . LEU A 343 ? 0.8632 0.9401 0.6397 -0.4184 0.1462 0.1029 357 LEU A C 2689 O O . LEU A 343 ? 0.8199 0.8980 0.6027 -0.4215 0.1494 0.1029 357 LEU A O 2690 C CB . LEU A 343 ? 0.7954 0.8828 0.5640 -0.4168 0.1356 0.0912 357 LEU A CB 2691 C CG . LEU A 343 ? 0.7843 0.8805 0.5470 -0.4143 0.1302 0.0869 357 LEU A CG 2692 C CD1 . LEU A 343 ? 0.7800 0.8857 0.5468 -0.4162 0.1298 0.0836 357 LEU A CD1 2693 C CD2 . LEU A 343 ? 0.7765 0.8701 0.5364 -0.4144 0.1250 0.0810 357 LEU A CD2 2694 N N . THR A 344 ? 0.8643 0.9319 0.6406 -0.4174 0.1473 0.1056 358 THR A N 2695 C CA . THR A 344 ? 0.8719 0.9296 0.6560 -0.4201 0.1524 0.1081 358 THR A CA 2696 C C . THR A 344 ? 0.8669 0.9172 0.6517 -0.4212 0.1503 0.1032 358 THR A C 2697 O O . THR A 344 ? 0.8916 0.9454 0.6710 -0.4201 0.1448 0.0978 358 THR A O 2698 C CB . THR A 344 ? 0.8679 0.9207 0.6529 -0.4175 0.1576 0.1185 358 THR A CB 2699 O OG1 . THR A 344 ? 0.8768 0.9271 0.6559 -0.4134 0.1554 0.1216 358 THR A OG1 2700 C CG2 . THR A 344 ? 0.8509 0.9115 0.6338 -0.4162 0.1595 0.1233 358 THR A CG2 2701 N N . ASP A 345 ? 0.8957 0.9356 0.6873 -0.4232 0.1550 0.1050 359 ASP A N 2702 C CA . ASP A 345 ? 0.9496 0.9813 0.7427 -0.4245 0.1540 0.1001 359 ASP A CA 2703 C C . ASP A 345 ? 0.9989 1.0191 0.7965 -0.4229 0.1594 0.1070 359 ASP A C 2704 O O . ASP A 345 ? 1.0057 1.0176 0.8059 -0.4240 0.1599 0.1037 359 ASP A O 2705 C CB . ASP A 345 ? 0.9586 0.9888 0.7570 -0.4302 0.1540 0.0921 359 ASP A CB 2706 C CG . ASP A 345 ? 1.0279 1.0537 0.8349 -0.4334 0.1606 0.0954 359 ASP A CG 2707 O OD1 . ASP A 345 ? 1.0552 1.0810 0.8638 -0.4313 0.1647 0.1039 359 ASP A OD1 2708 O OD2 . ASP A 345 ? 1.0293 1.0517 0.8413 -0.4383 0.1616 0.0895 359 ASP A OD2 2709 N N . GLY A 346 ? 1.0548 1.0747 0.8539 -0.4204 0.1636 0.1168 360 GLY A N 2710 C CA . GLY A 346 ? 1.0880 1.0976 0.8935 -0.4190 0.1695 0.1248 360 GLY A CA 2711 C C . GLY A 346 ? 1.0912 1.0923 0.9075 -0.4234 0.1758 0.1240 360 GLY A C 2712 O O . GLY A 346 ? 1.1024 1.0939 0.9260 -0.4227 0.1815 0.1302 360 GLY A O 2713 N N . LEU A 347 ? 1.0754 1.0802 0.8932 -0.4279 0.1749 0.1167 361 LEU A N 2714 C CA . LEU A 347 ? 1.0903 1.0878 0.9177 -0.4327 0.1804 0.1149 361 LEU A CA 2715 C C . LEU A 347 ? 1.0939 1.0973 0.9239 -0.4345 0.1829 0.1178 361 LEU A C 2716 O O . LEU A 347 ? 1.1284 1.1297 0.9645 -0.4392 0.1856 0.1140 361 LEU A O 2717 C CB . LEU A 347 ? 1.0881 1.0838 0.9160 -0.4373 0.1776 0.1033 361 LEU A CB 2718 C CG . LEU A 347 ? 1.0672 1.0554 0.8940 -0.4365 0.1762 0.0993 361 LEU A CG 2719 C CD1 . LEU A 347 ? 1.0163 1.0031 0.8435 -0.4417 0.1737 0.0877 361 LEU A CD1 2720 C CD2 . LEU A 347 ? 1.0951 1.0711 0.9299 -0.4348 0.1832 0.1067 361 LEU A CD2 2721 N N . GLY A 348 ? 1.0552 1.0659 0.8803 -0.4308 0.1820 0.1244 362 GLY A N 2722 C CA . GLY A 348 ? 1.0631 1.0791 0.8904 -0.4320 0.1848 0.1281 362 GLY A CA 2723 C C . GLY A 348 ? 1.0747 1.1015 0.8986 -0.4344 0.1804 0.1210 362 GLY A C 2724 O O . GLY A 348 ? 1.0711 1.1037 0.8963 -0.4351 0.1822 0.1237 362 GLY A O 2725 N N . ASN A 349 ? 1.0851 1.1150 0.9052 -0.4356 0.1746 0.1123 363 ASN A N 2726 C CA . ASN A 349 ? 1.0901 1.1311 0.9075 -0.4373 0.1700 0.1064 363 ASN A CA 2727 C C . ASN A 349 ? 0.9614 1.0119 0.7706 -0.4328 0.1661 0.1086 363 ASN A C 2728 O O . ASN A 349 ? 0.9160 0.9648 0.7196 -0.4286 0.1648 0.1120 363 ASN A O 2729 C CB . ASN A 349 ? 1.2373 1.2787 1.0545 -0.4406 0.1653 0.0965 363 ASN A CB 2730 C CG . ASN A 349 ? 1.3859 1.4202 1.2111 -0.4461 0.1689 0.0930 363 ASN A CG 2731 O OD1 . ASN A 349 ? 1.3528 1.3918 1.1819 -0.4500 0.1692 0.0902 363 ASN A OD1 2732 N ND2 . ASN A 349 ? 1.5755 1.5983 1.4033 -0.4464 0.1720 0.0933 363 ASN A ND2 2733 N N . LEU A 350 ? 0.8842 0.9447 0.6930 -0.4337 0.1646 0.1067 364 LEU A N 2734 C CA . LEU A 350 ? 0.8750 0.9449 0.6766 -0.4299 0.1615 0.1079 364 LEU A CA 2735 C C . LEU A 350 ? 0.8746 0.9547 0.6766 -0.4317 0.1573 0.1012 364 LEU A C 2736 O O . LEU A 350 ? 0.8738 0.9561 0.6824 -0.4356 0.1587 0.0990 364 LEU A O 2737 C CB . LEU A 350 ? 0.8862 0.9579 0.6876 -0.4279 0.1663 0.1162 364 LEU A CB 2738 C CG . LEU A 350 ? 0.8436 0.9258 0.6391 -0.4250 0.1645 0.1172 364 LEU A CG 2739 C CD1 . LEU A 350 ? 0.8380 0.9218 0.6242 -0.4205 0.1606 0.1177 364 LEU A CD1 2740 C CD2 . LEU A 350 ? 0.8532 0.9367 0.6502 -0.4245 0.1701 0.1245 364 LEU A CD2 2741 N N . THR A 351 ? 0.8794 0.9658 0.6749 -0.4289 0.1522 0.0981 365 THR A N 2742 C CA . THR A 351 ? 0.8837 0.9805 0.6803 -0.4299 0.1484 0.0928 365 THR A CA 2743 C C . THR A 351 ? 0.8088 0.9139 0.6003 -0.4260 0.1480 0.0950 365 THR A C 2744 O O . THR A 351 ? 0.8364 0.9405 0.6203 -0.4221 0.1466 0.0970 365 THR A O 2745 C CB . THR A 351 ? 0.8845 0.9821 0.6793 -0.4307 0.1423 0.0854 365 THR A CB 2746 O OG1 . THR A 351 ? 0.8914 0.9808 0.6904 -0.4346 0.1431 0.0828 365 THR A OG1 2747 C CG2 . THR A 351 ? 0.7944 0.9031 0.5917 -0.4319 0.1387 0.0808 365 THR A CG2 2748 N N . ILE A 352 ? 0.9091 1.0224 0.7048 -0.4271 0.1493 0.0946 366 ILE A N 2749 C CA . ILE A 352 ? 0.9147 1.0362 0.7064 -0.4239 0.1493 0.0957 366 ILE A CA 2750 C C . ILE A 352 ? 0.8876 1.0186 0.6827 -0.4246 0.1457 0.0900 366 ILE A C 2751 O O . ILE A 352 ? 0.8567 0.9911 0.6599 -0.4281 0.1460 0.0881 366 ILE A O 2752 C CB . ILE A 352 ? 0.9618 1.0847 0.7556 -0.4238 0.1554 0.1016 366 ILE A CB 2753 C CG1 . ILE A 352 ? 0.8235 0.9377 0.6137 -0.4225 0.1589 0.1083 366 ILE A CG1 2754 C CG2 . ILE A 352 ? 0.8104 0.9421 0.6006 -0.4209 0.1559 0.1018 366 ILE A CG2 2755 C CD1 . ILE A 352 ? 0.8340 0.9479 0.6276 -0.4235 0.1651 0.1143 366 ILE A CD1 2756 N N . ILE A 353 ? 0.8575 0.9930 0.6468 -0.4213 0.1422 0.0875 367 ILE A N 2757 C CA . ILE A 353 ? 0.8386 0.9833 0.6313 -0.4214 0.1388 0.0826 367 ILE A CA 2758 C C . ILE A 353 ? 0.8389 0.9907 0.6289 -0.4180 0.1409 0.0838 367 ILE A C 2759 O O . ILE A 353 ? 0.8024 0.9527 0.5837 -0.4145 0.1405 0.0848 367 ILE A O 2760 C CB . ILE A 353 ? 0.8002 0.9441 0.5895 -0.4209 0.1324 0.0774 367 ILE A CB 2761 C CG1 . ILE A 353 ? 0.8148 0.9510 0.6064 -0.4244 0.1309 0.0758 367 ILE A CG1 2762 C CG2 . ILE A 353 ? 0.7641 0.9180 0.5579 -0.4208 0.1291 0.0731 367 ILE A CG2 2763 C CD1 . ILE A 353 ? 0.8063 0.9369 0.5911 -0.4231 0.1263 0.0727 367 ILE A CD1 2764 N N . ILE A 354 ? 0.8559 1.0153 0.6535 -0.4191 0.1433 0.0837 368 ILE A N 2765 C CA . ILE A 354 ? 0.8667 1.0327 0.6631 -0.4164 0.1465 0.0846 368 ILE A CA 2766 C C . ILE A 354 ? 0.8451 1.0204 0.6480 -0.4160 0.1443 0.0805 368 ILE A C 2767 O O . ILE A 354 ? 0.8344 1.0131 0.6463 -0.4189 0.1426 0.0790 368 ILE A O 2768 C CB . ILE A 354 ? 0.8918 1.0583 0.6921 -0.4176 0.1530 0.0894 368 ILE A CB 2769 C CG1 . ILE A 354 ? 0.7937 0.9509 0.5889 -0.4181 0.1551 0.0940 368 ILE A CG1 2770 C CG2 . ILE A 354 ? 0.7852 0.9577 0.5834 -0.4149 0.1570 0.0902 368 ILE A CG2 2771 C CD1 . ILE A 354 ? 0.8037 0.9603 0.6036 -0.4200 0.1611 0.0988 368 ILE A CD1 2772 N N . GLU A 355 ? 0.7602 0.9398 0.5588 -0.4126 0.1443 0.0788 369 GLU A N 2773 C CA . GLU A 355 ? 0.8064 0.9947 0.6114 -0.4117 0.1428 0.0753 369 GLU A CA 2774 C C . GLU A 355 ? 0.8062 0.9999 0.6111 -0.4090 0.1480 0.0759 369 GLU A C 2775 O O . GLU A 355 ? 0.8246 1.0151 0.6200 -0.4068 0.1503 0.0772 369 GLU A O 2776 C CB . GLU A 355 ? 0.8051 0.9927 0.6054 -0.4103 0.1362 0.0710 369 GLU A CB 2777 C CG . GLU A 355 ? 0.8178 1.0125 0.6189 -0.4072 0.1354 0.0678 369 GLU A CG 2778 C CD . GLU A 355 ? 0.8191 1.0118 0.6093 -0.4036 0.1373 0.0676 369 GLU A CD 2779 O OE1 . GLU A 355 ? 0.7970 0.9824 0.5778 -0.4032 0.1371 0.0696 369 GLU A OE1 2780 O OE2 . GLU A 355 ? 0.8881 1.0864 0.6794 -0.4012 0.1392 0.0656 369 GLU A OE2 2781 N N . THR A 356 ? 0.7491 0.9512 0.5648 -0.4093 0.1501 0.0751 370 THR A N 2782 C CA . THR A 356 ? 0.7511 0.9583 0.5680 -0.4069 0.1559 0.0752 370 THR A CA 2783 C C . THR A 356 ? 0.7415 0.9566 0.5656 -0.4050 0.1548 0.0719 370 THR A C 2784 O O . THR A 356 ? 0.7933 1.0151 0.6271 -0.4046 0.1596 0.0726 370 THR A O 2785 C CB . THR A 356 ? 0.8017 1.0112 0.6262 -0.4087 0.1626 0.0791 370 THR A CB 2786 O OG1 . THR A 356 ? 0.8127 1.0265 0.6503 -0.4116 0.1613 0.0798 370 THR A OG1 2787 C CG2 . THR A 356 ? 0.7700 0.9718 0.5863 -0.4099 0.1647 0.0828 370 THR A CG2 2788 N N . MET A 357 ? 0.7333 0.9476 0.5532 -0.4038 0.1487 0.0685 371 MET A N 2789 C CA . MET A 357 ? 0.7832 1.0050 0.6110 -0.4022 0.1468 0.0657 371 MET A CA 2790 C C . MET A 357 ? 0.7759 1.0019 0.6038 -0.3989 0.1523 0.0642 371 MET A C 2791 O O . MET A 357 ? 0.7477 0.9699 0.5639 -0.3965 0.1530 0.0624 371 MET A O 2792 C CB . MET A 357 ? 0.7768 0.9963 0.5993 -0.4019 0.1389 0.0624 371 MET A CB 2793 C CG . MET A 357 ? 0.8179 1.0346 0.6429 -0.4056 0.1336 0.0630 371 MET A CG 2794 S SD . MET A 357 ? 0.8278 1.0527 0.6706 -0.4089 0.1342 0.0654 371 MET A SD 2795 C CE . MET A 357 ? 0.7221 0.9391 0.5621 -0.4132 0.1343 0.0680 371 MET A CE 2796 N N . SER A 358 ? 0.7910 1.0249 0.6327 -0.3987 0.1562 0.0651 372 SER A N 2797 C CA . SER A 358 ? 0.7875 1.0258 0.6320 -0.3957 0.1623 0.0635 372 SER A CA 2798 C C . SER A 358 ? 0.7722 1.0120 0.6140 -0.3930 0.1582 0.0594 372 SER A C 2799 O O . SER A 358 ? 0.7589 1.0008 0.6050 -0.3936 0.1518 0.0587 372 SER A O 2800 C CB . SER A 358 ? 0.7586 1.0053 0.6208 -0.3961 0.1676 0.0660 372 SER A CB 2801 O OG . SER A 358 ? 0.7324 0.9860 0.6065 -0.3955 0.1638 0.0653 372 SER A OG 2802 N N . HIS A 359 ? 0.7465 0.9852 0.5811 -0.3901 0.1622 0.0567 373 HIS A N 2803 C CA . HIS A 359 ? 0.7693 1.0092 0.6011 -0.3874 0.1594 0.0526 373 HIS A CA 2804 C C . HIS A 359 ? 0.7774 1.0254 0.6250 -0.3868 0.1576 0.0526 373 HIS A C 2805 O O . HIS A 359 ? 0.7920 1.0407 0.6386 -0.3861 0.1512 0.0505 373 HIS A O 2806 C CB . HIS A 359 ? 0.7833 1.0225 0.6090 -0.3847 0.1661 0.0499 373 HIS A CB 2807 C CG . HIS A 359 ? 0.8012 1.0423 0.6261 -0.3818 0.1645 0.0455 373 HIS A CG 2808 N ND1 . HIS A 359 ? 0.8108 1.0590 0.6499 -0.3801 0.1681 0.0449 373 HIS A ND1 2809 C CD2 . HIS A 359 ? 0.7997 1.0366 0.6120 -0.3803 0.1597 0.0419 373 HIS A CD2 2810 C CE1 . HIS A 359 ? 0.8168 1.0649 0.6517 -0.3777 0.1657 0.0409 373 HIS A CE1 2811 N NE2 . HIS A 359 ? 0.8072 1.0486 0.6257 -0.3778 0.1606 0.0388 373 HIS A NE2 2812 N N . GLN A 360 ? 0.7414 0.9960 0.6042 -0.3870 0.1635 0.0553 374 GLN A N 2813 C CA . GLN A 360 ? 0.7275 0.9908 0.6075 -0.3861 0.1629 0.0563 374 GLN A CA 2814 C C . GLN A 360 ? 0.7486 1.0140 0.6337 -0.3886 0.1541 0.0580 374 GLN A C 2815 O O . GLN A 360 ? 0.7836 1.0553 0.6789 -0.3877 0.1507 0.0582 374 GLN A O 2816 C CB . GLN A 360 ? 0.6941 0.9637 0.5901 -0.3859 0.1714 0.0596 374 GLN A CB 2817 N N . HIS A 361 ? 0.7552 1.0154 0.6332 -0.3918 0.1507 0.0594 375 HIS A N 2818 C CA . HIS A 361 ? 0.8016 1.0633 0.6841 -0.3949 0.1432 0.0609 375 HIS A CA 2819 C C . HIS A 361 ? 0.8064 1.0599 0.6736 -0.3962 0.1360 0.0584 375 HIS A C 2820 O O . HIS A 361 ? 0.8355 1.0873 0.7031 -0.3996 0.1312 0.0596 375 HIS A O 2821 C CB . HIS A 361 ? 0.8063 1.0696 0.6973 -0.3982 0.1457 0.0651 375 HIS A CB 2822 C CG . HIS A 361 ? 0.8366 1.1087 0.7450 -0.3973 0.1522 0.0683 375 HIS A CG 2823 N ND1 . HIS A 361 ? 0.8254 1.0988 0.7408 -0.3994 0.1572 0.0719 375 HIS A ND1 2824 C CD2 . HIS A 361 ? 0.8459 1.1257 0.7668 -0.3945 0.1549 0.0686 375 HIS A CD2 2825 C CE1 . HIS A 361 ? 0.8421 1.1237 0.7737 -0.3979 0.1626 0.0743 375 HIS A CE1 2826 N NE2 . HIS A 361 ? 0.8475 1.1332 0.7832 -0.3949 0.1616 0.0725 375 HIS A NE2 2827 N N . SER A 362 ? 0.7816 1.0298 0.6355 -0.3938 0.1354 0.0549 376 SER A N 2828 C CA . SER A 362 ? 0.7543 0.9945 0.5943 -0.3948 0.1290 0.0528 376 SER A CA 2829 C C . SER A 362 ? 0.7269 0.9655 0.5583 -0.3918 0.1258 0.0487 376 SER A C 2830 O O . SER A 362 ? 0.7396 0.9710 0.5580 -0.3918 0.1220 0.0468 376 SER A O 2831 C CB . SER A 362 ? 0.7651 0.9971 0.5942 -0.3958 0.1320 0.0542 376 SER A CB 2832 O OG . SER A 362 ? 0.7225 0.9520 0.5427 -0.3929 0.1366 0.0529 376 SER A OG 2833 N N . MET A 363 ? 0.7019 0.9473 0.5413 -0.3892 0.1275 0.0475 377 MET A N 2834 C CA . MET A 363 ? 0.7336 0.9780 0.5660 -0.3863 0.1249 0.0434 377 MET A CA 2835 C C . MET A 363 ? 0.7491 0.9924 0.5787 -0.3876 0.1157 0.0418 377 MET A C 2836 O O . MET A 363 ? 0.7167 0.9656 0.5570 -0.3893 0.1121 0.0434 377 MET A O 2837 C CB . MET A 363 ? 0.7914 1.0437 0.6355 -0.3834 0.1292 0.0429 377 MET A CB 2838 C CG . MET A 363 ? 0.8382 1.0925 0.6875 -0.3822 0.1390 0.0442 377 MET A CG 2839 S SD . MET A 363 ? 1.6312 1.8971 1.5043 -0.3812 0.1437 0.0474 377 MET A SD 2840 C CE . MET A 363 ? 1.0226 1.2929 0.8998 -0.3791 0.1373 0.0451 377 MET A CE 2841 N N . CYS A 364 ? 0.7358 0.9720 0.5509 -0.3869 0.1120 0.0388 378 CYS A N 2842 C CA . CYS A 364 ? 0.7230 0.9577 0.5341 -0.3875 0.1038 0.0364 378 CYS A CA 2843 C C . CYS A 364 ? 0.7034 0.9423 0.5158 -0.3841 0.1033 0.0334 378 CYS A C 2844 O O . CYS A 364 ? 0.7013 0.9416 0.5138 -0.3814 0.1093 0.0325 378 CYS A O 2845 C CB . CYS A 364 ? 0.7285 0.9533 0.5242 -0.3880 0.1007 0.0349 378 CYS A CB 2846 S SG . CYS A 364 ? 0.8204 1.0387 0.6132 -0.3914 0.1028 0.0386 378 CYS A SG 2847 N N . ILE A 365 ? 0.7034 0.9442 0.5168 -0.3843 0.0966 0.0316 379 ILE A N 2848 C CA . ILE A 365 ? 0.6585 0.9035 0.4739 -0.3811 0.0961 0.0289 379 ILE A CA 2849 C C . ILE A 365 ? 0.6428 0.8810 0.4433 -0.3787 0.0956 0.0249 379 ILE A C 2850 O O . ILE A 365 ? 0.6531 0.8937 0.4538 -0.3757 0.0972 0.0223 379 ILE A O 2851 C CB . ILE A 365 ? 0.6717 0.9216 0.4936 -0.3819 0.0889 0.0287 379 ILE A CB 2852 C CG1 . ILE A 365 ? 0.6559 0.8990 0.4660 -0.3840 0.0814 0.0264 379 ILE A CG1 2853 C CG2 . ILE A 365 ? 0.7325 0.9898 0.5698 -0.3842 0.0890 0.0331 379 ILE A CG2 2854 C CD1 . ILE A 365 ? 0.6933 0.9398 0.5048 -0.3835 0.0747 0.0244 379 ILE A CD1 2855 N N . ARG A 366 ? 0.6455 0.8755 0.4339 -0.3801 0.0938 0.0246 380 ARG A N 2856 C CA . ARG A 366 ? 0.6726 0.8963 0.4471 -0.3781 0.0916 0.0212 380 ARG A CA 2857 C C . ARG A 366 ? 0.6786 0.8942 0.4427 -0.3791 0.0926 0.0228 380 ARG A C 2858 O O . ARG A 366 ? 0.7020 0.9134 0.4638 -0.3818 0.0890 0.0242 380 ARG A O 2859 C CB . ARG A 366 ? 0.7224 0.9451 0.4937 -0.3785 0.0835 0.0185 380 ARG A CB 2860 C CG . ARG A 366 ? 0.8054 1.0228 0.5643 -0.3762 0.0809 0.0148 380 ARG A CG 2861 C CD . ARG A 366 ? 0.8554 1.0718 0.6115 -0.3768 0.0730 0.0120 380 ARG A CD 2862 N NE . ARG A 366 ? 0.8713 1.0956 0.6376 -0.3765 0.0712 0.0115 380 ARG A NE 2863 C CZ . ARG A 366 ? 0.9246 1.1518 0.6971 -0.3792 0.0669 0.0129 380 ARG A CZ 2864 N NH1 . ARG A 366 ? 0.9465 1.1688 0.7158 -0.3824 0.0645 0.0142 380 ARG A NH1 2865 N NH2 . ARG A 366 ? 0.9373 1.1723 0.7196 -0.3786 0.0651 0.0131 380 ARG A NH2 2866 N N . PRO A 367 ? 0.6531 0.8667 0.4114 -0.3772 0.0978 0.0228 381 PRO A N 2867 C CA . PRO A 367 ? 0.7207 0.9385 0.4813 -0.3744 0.1035 0.0209 381 PRO A CA 2868 C C . PRO A 367 ? 0.7940 1.0164 0.5649 -0.3752 0.1107 0.0240 381 PRO A C 2869 O O . PRO A 367 ? 0.7980 1.0195 0.5720 -0.3778 0.1113 0.0276 381 PRO A O 2870 C CB . PRO A 367 ? 0.7200 0.9320 0.4674 -0.3726 0.1048 0.0199 381 PRO A CB 2871 C CG . PRO A 367 ? 0.7320 0.9384 0.4747 -0.3749 0.1038 0.0238 381 PRO A CG 2872 C CD . PRO A 367 ? 0.7049 0.9112 0.4531 -0.3777 0.0984 0.0248 381 PRO A CD 2873 N N . TYR A 368 ? 0.8465 1.0738 0.6232 -0.3730 0.1165 0.0225 382 TYR A N 2874 C CA . TYR A 368 ? 0.8867 1.1184 0.6737 -0.3735 0.1243 0.0251 382 TYR A CA 2875 C C . TYR A 368 ? 0.8745 1.1017 0.6521 -0.3732 0.1299 0.0255 382 TYR A C 2876 O O . TYR A 368 ? 0.8759 1.1003 0.6440 -0.3712 0.1312 0.0223 382 TYR A O 2877 C CB . TYR A 368 ? 0.9130 1.1516 0.7116 -0.3712 0.1286 0.0235 382 TYR A CB 2878 C CG . TYR A 368 ? 0.9399 1.1835 0.7509 -0.3713 0.1372 0.0263 382 TYR A CG 2879 C CD1 . TYR A 368 ? 0.9290 1.1787 0.7554 -0.3729 0.1370 0.0303 382 TYR A CD1 2880 C CD2 . TYR A 368 ? 0.9381 1.1803 0.7457 -0.3700 0.1454 0.0248 382 TYR A CD2 2881 C CE1 . TYR A 368 ? 0.9335 1.1878 0.7722 -0.3730 0.1449 0.0331 382 TYR A CE1 2882 C CE2 . TYR A 368 ? 0.9469 1.1934 0.7661 -0.3701 0.1536 0.0272 382 TYR A CE2 2883 C CZ . TYR A 368 ? 0.9451 1.1977 0.7803 -0.3715 0.1534 0.0314 382 TYR A CZ 2884 O OH . TYR A 368 ? 0.9405 1.1975 0.7882 -0.3715 0.1617 0.0341 382 TYR A OH 2885 N N . LEU A 369 ? 0.8679 1.0945 0.6483 -0.3754 0.1332 0.0294 383 LEU A N 2886 C CA . LEU A 369 ? 0.8847 1.1072 0.6561 -0.3755 0.1382 0.0305 383 LEU A CA 2887 C C . LEU A 369 ? 0.8699 1.0962 0.6470 -0.3745 0.1475 0.0298 383 LEU A C 2888 O O . LEU A 369 ? 0.8199 1.0519 0.6112 -0.3749 0.1514 0.0315 383 LEU A O 2889 C CB . LEU A 369 ? 0.9272 1.1466 0.6981 -0.3784 0.1375 0.0352 383 LEU A CB 2890 C CG . LEU A 369 ? 0.9480 1.1620 0.7125 -0.3799 0.1298 0.0365 383 LEU A CG 2891 C CD1 . LEU A 369 ? 0.9374 1.1470 0.6984 -0.3821 0.1315 0.0411 383 LEU A CD1 2892 C CD2 . LEU A 369 ? 0.9495 1.1594 0.7019 -0.3778 0.1250 0.0333 383 LEU A CD2 2893 N N . PRO A 370 ? 0.8871 1.1105 0.6536 -0.3733 0.1513 0.0276 384 PRO A N 2894 C CA . PRO A 370 ? 0.8646 1.0904 0.6347 -0.3728 0.1609 0.0269 384 PRO A CA 2895 C C . PRO A 370 ? 0.8347 1.0611 0.6103 -0.3753 0.1647 0.0318 384 PRO A C 2896 O O . PRO A 370 ? 0.7947 1.0177 0.5659 -0.3771 0.1602 0.0352 384 PRO A O 2897 C CB . PRO A 370 ? 0.8914 1.1126 0.6460 -0.3720 0.1620 0.0242 384 PRO A CB 2898 C CG . PRO A 370 ? 0.8950 1.1127 0.6404 -0.3710 0.1532 0.0224 384 PRO A CG 2899 C CD . PRO A 370 ? 0.8954 1.1130 0.6462 -0.3725 0.1467 0.0259 384 PRO A CD 2900 N N . TYR A 371 ? 0.8545 1.0851 0.6399 -0.3752 0.1731 0.0321 385 TYR A N 2901 C CA . TYR A 371 ? 0.8634 1.0953 0.6558 -0.3775 0.1772 0.0367 385 TYR A CA 2902 C C . TYR A 371 ? 0.8452 1.0714 0.6250 -0.3794 0.1763 0.0394 385 TYR A C 2903 O O . TYR A 371 ? 0.8165 1.0388 0.5826 -0.3788 0.1764 0.0376 385 TYR A O 2904 C CB . TYR A 371 ? 0.8864 1.1228 0.6892 -0.3769 0.1875 0.0361 385 TYR A CB 2905 C CG . TYR A 371 ? 0.9040 1.1417 0.7137 -0.3792 0.1921 0.0407 385 TYR A CG 2906 C CD1 . TYR A 371 ? 0.9287 1.1706 0.7527 -0.3805 0.1902 0.0447 385 TYR A CD1 2907 C CD2 . TYR A 371 ? 0.8977 1.1327 0.6995 -0.3803 0.1981 0.0412 385 TYR A CD2 2908 C CE1 . TYR A 371 ? 0.9583 1.2014 0.7887 -0.3827 0.1943 0.0489 385 TYR A CE1 2909 C CE2 . TYR A 371 ? 0.9219 1.1581 0.7299 -0.3824 0.2024 0.0455 385 TYR A CE2 2910 C CZ . TYR A 371 ? 0.9555 1.1956 0.7780 -0.3835 0.2005 0.0493 385 TYR A CZ 2911 O OH . TYR A 371 ? 0.9996 1.2408 0.8284 -0.3857 0.2047 0.0535 385 TYR A OH 2912 N N . TYR A 372 ? 0.8625 1.0886 0.6476 -0.3817 0.1753 0.0441 386 TYR A N 2913 C CA . TYR A 372 ? 0.8702 1.0921 0.6473 -0.3837 0.1764 0.0478 386 TYR A CA 2914 C C . TYR A 372 ? 0.8894 1.1143 0.6788 -0.3858 0.1809 0.0519 386 TYR A C 2915 O O . TYR A 372 ? 0.8668 1.0963 0.6699 -0.3862 0.1799 0.0527 386 TYR A O 2916 C CB . TYR A 372 ? 0.8835 1.0997 0.6512 -0.3845 0.1681 0.0497 386 TYR A CB 2917 C CG . TYR A 372 ? 0.8817 1.0988 0.6585 -0.3859 0.1626 0.0514 386 TYR A CG 2918 C CD1 . TYR A 372 ? 0.8787 1.0980 0.6598 -0.3847 0.1574 0.0485 386 TYR A CD1 2919 C CD2 . TYR A 372 ? 0.8850 1.1005 0.6659 -0.3886 0.1625 0.0560 386 TYR A CD2 2920 C CE1 . TYR A 372 ? 0.8594 1.0798 0.6483 -0.3864 0.1521 0.0499 386 TYR A CE1 2921 C CE2 . TYR A 372 ? 0.8634 1.0796 0.6522 -0.3903 0.1574 0.0572 386 TYR A CE2 2922 C CZ . TYR A 372 ? 0.8514 1.0701 0.6439 -0.3893 0.1522 0.0541 386 TYR A CZ 2923 O OH . TYR A 372 ? 0.8568 1.0764 0.6565 -0.3913 0.1470 0.0550 386 TYR A OH 2924 N N . ASN A 373 ? 0.9322 1.1551 0.7170 -0.3873 0.1857 0.0546 387 ASN A N 2925 C CA . ASN A 373 ? 0.9728 1.1986 0.7687 -0.3892 0.1913 0.0581 387 ASN A CA 2926 C C . ASN A 373 ? 0.8856 1.1086 0.6827 -0.3917 0.1869 0.0628 387 ASN A C 2927 O O . ASN A 373 ? 0.8429 1.0601 0.6285 -0.3922 0.1824 0.0642 387 ASN A O 2928 C CB . ASN A 373 ? 1.1374 1.3625 0.9274 -0.3897 0.1994 0.0583 387 ASN A CB 2929 C CG . ASN A 373 ? 1.3204 1.5508 1.1246 -0.3904 0.2077 0.0596 387 ASN A CG 2930 O OD1 . ASN A 373 ? 1.3076 1.5407 1.1241 -0.3918 0.2072 0.0629 387 ASN A OD1 2931 N ND2 . ASN A 373 ? 1.5286 1.7604 1.3313 -0.3897 0.2156 0.0570 387 ASN A ND2 2932 N N . VAL A 374 ? 0.8705 1.0976 0.6821 -0.3933 0.1882 0.0652 388 VAL A N 2933 C CA . VAL A 374 ? 0.9014 1.1258 0.7151 -0.3962 0.1861 0.0697 388 VAL A CA 2934 C C . VAL A 374 ? 0.9471 1.1759 0.7730 -0.3978 0.1930 0.0726 388 VAL A C 2935 O O . VAL A 374 ? 0.9794 1.2149 0.8194 -0.3974 0.1955 0.0721 388 VAL A O 2936 C CB . VAL A 374 ? 0.8782 1.1027 0.6974 -0.3973 0.1782 0.0698 388 VAL A CB 2937 C CG1 . VAL A 374 ? 0.8551 1.0766 0.6770 -0.4006 0.1771 0.0741 388 VAL A CG1 2938 C CG2 . VAL A 374 ? 0.8738 1.0937 0.6812 -0.3958 0.1712 0.0669 388 VAL A CG2 2939 N N . SER A 375 ? 0.9520 1.1774 0.7735 -0.3996 0.1962 0.0761 389 SER A N 2940 C CA . SER A 375 ? 0.9550 1.1842 0.7873 -0.4012 0.2031 0.0790 389 SER A CA 2941 C C . SER A 375 ? 0.9711 1.1966 0.8035 -0.4042 0.2021 0.0836 389 SER A C 2942 O O . SER A 375 ? 0.9254 1.1448 0.7483 -0.4049 0.1969 0.0847 389 SER A O 2943 C CB . SER A 375 ? 0.9496 1.1797 0.7775 -0.4002 0.2114 0.0779 389 SER A CB 2944 O OG . SER A 375 ? 0.9695 1.1937 0.7806 -0.4001 0.2108 0.0782 389 SER A OG 2945 N N . HIS A 376 ? 1.0296 1.2587 0.8731 -0.4060 0.2074 0.0864 390 HIS A N 2946 C CA . HIS A 376 ? 1.1082 1.3341 0.9531 -0.4090 0.2071 0.0908 390 HIS A CA 2947 C C . HIS A 376 ? 1.0579 1.2766 0.8875 -0.4093 0.2078 0.0929 390 HIS A C 2948 O O . HIS A 376 ? 1.0476 1.2659 0.8690 -0.4080 0.2122 0.0921 390 HIS A O 2949 C CB . HIS A 376 ? 1.2467 1.4780 1.1055 -0.4106 0.2136 0.0934 390 HIS A CB 2950 C CG . HIS A 376 ? 1.3743 1.6138 1.2496 -0.4101 0.2135 0.0922 390 HIS A CG 2951 N ND1 . HIS A 376 ? 1.4319 1.6736 1.3167 -0.4119 0.2077 0.0930 390 HIS A ND1 2952 C CD2 . HIS A 376 ? 1.4218 1.6677 1.3060 -0.4080 0.2183 0.0904 390 HIS A CD2 2953 C CE1 . HIS A 376 ? 1.4477 1.6975 1.3468 -0.4109 0.2087 0.0923 390 HIS A CE1 2954 N NE2 . HIS A 376 ? 1.4459 1.6982 1.3454 -0.4083 0.2153 0.0909 390 HIS A NE2 2955 N N . GLN A 377 ? 1.0135 1.2265 0.8394 -0.4110 0.2033 0.0955 391 GLN A N 2956 C CA . GLN A 377 ? 1.0030 1.2093 0.8160 -0.4113 0.2037 0.0986 391 GLN A CA 2957 C C . GLN A 377 ? 0.9875 1.1889 0.8028 -0.4140 0.2019 0.1028 391 GLN A C 2958 O O . GLN A 377 ? 0.9694 1.1721 0.7951 -0.4160 0.1996 0.1027 391 GLN A O 2959 C CB . GLN A 377 ? 1.0261 1.2286 0.8258 -0.4089 0.1988 0.0964 391 GLN A CB 2960 C CG . GLN A 377 ? 1.0156 1.2166 0.8168 -0.4084 0.1911 0.0938 391 GLN A CG 2961 C CD . GLN A 377 ? 1.0245 1.2215 0.8124 -0.4060 0.1865 0.0920 391 GLN A CD 2962 O OE1 . GLN A 377 ? 1.0289 1.2218 0.8061 -0.4055 0.1872 0.0948 391 GLN A OE1 2963 N NE2 . GLN A 377 ? 1.0001 1.1988 0.7892 -0.4046 0.1815 0.0877 391 GLN A NE2 2964 N N . LEU A 378 ? 0.9977 1.1935 0.8034 -0.4143 0.2032 0.1067 392 LEU A N 2965 C CA . LEU A 378 ? 1.0063 1.1962 0.8130 -0.4167 0.2022 0.1111 392 LEU A CA 2966 C C . LEU A 378 ? 0.9904 1.1734 0.7851 -0.4153 0.1977 0.1126 392 LEU A C 2967 O O . LEU A 378 ? 0.9893 1.1723 0.7736 -0.4130 0.1976 0.1121 392 LEU A O 2968 C CB . LEU A 378 ? 1.0396 1.2295 0.8475 -0.4183 0.2089 0.1158 392 LEU A CB 2969 C CG . LEU A 378 ? 1.0590 1.2555 0.8799 -0.4199 0.2138 0.1151 392 LEU A CG 2970 C CD1 . LEU A 378 ? 1.0699 1.2689 0.8883 -0.4199 0.2214 0.1171 392 LEU A CD1 2971 C CD2 . LEU A 378 ? 1.0625 1.2575 0.8937 -0.4231 0.2131 0.1174 392 LEU A CD2 2972 N N . ALA A 379 ? 0.9899 1.1673 0.7865 -0.4167 0.1942 0.1144 393 ALA A N 2973 C CA . ALA A 379 ? 0.9929 1.1635 0.7798 -0.4154 0.1902 0.1162 393 ALA A CA 2974 C C . ALA A 379 ? 0.9881 1.1517 0.7761 -0.4173 0.1916 0.1220 393 ALA A C 2975 O O . ALA A 379 ? 0.9928 1.1550 0.7900 -0.4201 0.1919 0.1221 393 ALA A O 2976 C CB . ALA A 379 ? 0.9534 1.1232 0.7406 -0.4145 0.1835 0.1114 393 ALA A CB 2977 N N . THR A 380 ? 1.0004 1.1597 0.7791 -0.4160 0.1924 0.1268 394 THR A N 2978 C CA . THR A 380 ? 1.0242 1.1764 0.8039 -0.4174 0.1941 0.1331 394 THR A CA 2979 C C . THR A 380 ? 1.0090 1.1545 0.7833 -0.4159 0.1894 0.1345 394 THR A C 2980 O O . THR A 380 ? 1.0377 1.1836 0.8025 -0.4131 0.1869 0.1346 394 THR A O 2981 C CB . THR A 380 ? 1.0516 1.2042 0.8265 -0.4173 0.1995 0.1393 394 THR A CB 2982 O OG1 . THR A 380 ? 1.0407 1.1997 0.8207 -0.4187 0.2042 0.1376 394 THR A OG1 2983 C CG2 . THR A 380 ? 1.0598 1.2052 0.8374 -0.4189 0.2017 0.1462 394 THR A CG2 2984 N N . PHE A 381 ? 0.9833 1.1226 0.7637 -0.4178 0.1885 0.1355 395 PHE A N 2985 C CA . PHE A 381 ? 0.9991 1.1312 0.7757 -0.4165 0.1849 0.1372 395 PHE A CA 2986 C C . PHE A 381 ? 1.0000 1.1246 0.7784 -0.4174 0.1885 0.1449 395 PHE A C 2987 O O . PHE A 381 ? 0.9942 1.1175 0.7803 -0.4202 0.1925 0.1468 395 PHE A O 2988 C CB . PHE A 381 ? 0.9992 1.1295 0.7810 -0.4178 0.1803 0.1310 395 PHE A CB 2989 C CG . PHE A 381 ? 0.9880 1.1251 0.7677 -0.4165 0.1762 0.1240 395 PHE A CG 2990 C CD1 . PHE A 381 ? 0.9838 1.1283 0.7700 -0.4179 0.1773 0.1199 395 PHE A CD1 2991 C CD2 . PHE A 381 ? 0.9590 1.0954 0.7312 -0.4137 0.1713 0.1217 395 PHE A CD2 2992 C CE1 . PHE A 381 ? 0.9587 1.1095 0.7441 -0.4165 0.1740 0.1140 395 PHE A CE1 2993 C CE2 . PHE A 381 ? 0.9440 1.0866 0.7148 -0.4124 0.1678 0.1154 395 PHE A CE2 2994 C CZ . PHE A 381 ? 0.9369 1.0867 0.7145 -0.4138 0.1692 0.1116 395 PHE A CZ 2995 N N . THR A 382 ? 1.0200 1.1400 0.7920 -0.4150 0.1872 0.1497 396 THR A N 2996 C CA . THR A 382 ? 1.0733 1.1860 0.8475 -0.4154 0.1908 0.1580 396 THR A CA 2997 C C . THR A 382 ? 1.0896 1.1945 0.8638 -0.4143 0.1878 0.1591 396 THR A C 2998 O O . THR A 382 ? 1.0990 1.2045 0.8657 -0.4113 0.1839 0.1588 396 THR A O 2999 C CB . THR A 382 ? 1.0908 1.2058 0.8575 -0.4135 0.1936 0.1655 396 THR A CB 3000 O OG1 . THR A 382 ? 1.0883 1.2086 0.8568 -0.4152 0.1980 0.1656 396 THR A OG1 3001 C CG2 . THR A 382 ? 1.1035 1.2106 0.8719 -0.4130 0.1963 0.1748 396 THR A CG2 3002 N N . LEU A 383 ? 1.1009 1.1984 0.8838 -0.4167 0.1900 0.1601 397 LEU A N 3003 C CA . LEU A 383 ? 1.1044 1.1934 0.8888 -0.4159 0.1883 0.1615 397 LEU A CA 3004 C C . LEU A 383 ? 1.1466 1.2312 0.9283 -0.4134 0.1910 0.1719 397 LEU A C 3005 O O . LEU A 383 ? 1.1770 1.2565 0.9649 -0.4147 0.1962 0.1783 397 LEU A O 3006 C CB . LEU A 383 ? 1.0795 1.1618 0.8745 -0.4197 0.1903 0.1587 397 LEU A CB 3007 C CG . LEU A 383 ? 1.0624 1.1486 0.8613 -0.4227 0.1872 0.1489 397 LEU A CG 3008 C CD1 . LEU A 383 ? 1.0493 1.1274 0.8569 -0.4262 0.1881 0.1460 397 LEU A CD1 3009 C CD2 . LEU A 383 ? 1.0651 1.1565 0.8567 -0.4204 0.1809 0.1428 397 LEU A CD2 3010 N N . LYS A 384 ? 1.1338 1.2207 0.9064 -0.4098 0.1875 0.1738 398 LYS A N 3011 C CA . LYS A 384 ? 1.1591 1.2422 0.9292 -0.4072 0.1891 0.1839 398 LYS A CA 3012 C C . LYS A 384 ? 1.1871 1.2611 0.9620 -0.4065 0.1881 0.1848 398 LYS A C 3013 O O . LYS A 384 ? 1.1990 1.2699 0.9783 -0.4085 0.1863 0.1772 398 LYS A O 3014 C CB . LYS A 384 ? 1.1496 1.2400 0.9079 -0.4039 0.1857 0.1858 398 LYS A CB 3015 N N . GLY A 385 ? 1.2085 1.2782 0.9828 -0.4040 0.1895 0.1942 399 GLY A N 3016 C CA . GLY A 385 ? 1.2306 1.2912 1.0102 -0.4031 0.1894 0.1961 399 GLY A CA 3017 C C . GLY A 385 ? 1.2569 1.3089 1.0483 -0.4066 0.1932 0.1931 399 GLY A C 3018 O O . GLY A 385 ? 1.2637 1.3152 1.0610 -0.4094 0.1977 0.1938 399 GLY A O 3019 N N . SER A 386 ? 1.2682 1.3136 1.0630 -0.4067 0.1915 0.1892 400 SER A N 3020 C CA . SER A 386 ? 1.2896 1.3260 1.0956 -0.4102 0.1952 0.1861 400 SER A CA 3021 C C . SER A 386 ? 1.2463 1.2862 1.0537 -0.4143 0.1933 0.1750 400 SER A C 3022 O O . SER A 386 ? 1.2635 1.2970 1.0780 -0.4175 0.1944 0.1695 400 SER A O 3023 C CB . SER A 386 ? 1.3130 1.3410 1.1221 -0.4090 0.1942 0.1857 400 SER A CB 3024 O OG . SER A 386 ? 1.3427 1.3674 1.1520 -0.4051 0.1962 0.1968 400 SER A OG 3025 N N . LEU A 387 ? 1.1882 1.2382 0.9891 -0.4144 0.1907 0.1717 401 LEU A N 3026 C CA . LEU A 387 ? 1.1580 1.2125 0.9608 -0.4180 0.1891 0.1623 401 LEU A CA 3027 C C . LEU A 387 ? 1.1839 1.2393 0.9928 -0.4208 0.1945 0.1654 401 LEU A C 3028 O O . LEU A 387 ? 1.1740 1.2292 0.9892 -0.4247 0.1954 0.1597 401 LEU A O 3029 C CB . LEU A 387 ? 1.1122 1.1773 0.9058 -0.4165 0.1833 0.1565 401 LEU A CB 3030 C CG . LEU A 387 ? 1.0809 1.1463 0.8681 -0.4140 0.1773 0.1521 401 LEU A CG 3031 C CD1 . LEU A 387 ? 1.0268 1.1028 0.8060 -0.4127 0.1721 0.1460 401 LEU A CD1 3032 C CD2 . LEU A 387 ? 0.8736 0.9319 0.6665 -0.4166 0.1760 0.1459 401 LEU A CD2 3033 N N . ARG A 388 ? 1.2288 1.2854 1.0359 -0.4187 0.1980 0.1745 402 ARG A N 3034 C CA . ARG A 388 ? 1.2498 1.3077 1.0617 -0.4209 0.2034 0.1784 402 ARG A CA 3035 C C . ARG A 388 ? 1.2609 1.3111 1.0846 -0.4250 0.2079 0.1773 402 ARG A C 3036 O O . ARG A 388 ? 1.2356 1.2883 1.0637 -0.4280 0.2107 0.1761 402 ARG A O 3037 C CB . ARG A 388 ? 1.2555 1.3133 1.0645 -0.4180 0.2069 0.1898 402 ARG A CB 3038 N N . GLU A 389 ? 1.3031 1.3439 1.1317 -0.4252 0.2086 0.1775 403 GLU A N 3039 C CA . GLU A 389 ? 1.3490 1.3812 1.1889 -0.4291 0.2132 0.1765 403 GLU A CA 3040 C C . GLU A 389 ? 1.3734 1.4076 1.2162 -0.4337 0.2106 0.1654 403 GLU A C 3041 O O . GLU A 389 ? 1.3877 1.4153 1.2393 -0.4376 0.2138 0.1630 403 GLU A O 3042 C CB . GLU A 389 ? 1.3484 1.3696 1.1931 -0.4278 0.2153 0.1802 403 GLU A CB 3043 N N . ILE A 390 ? 1.3711 1.4148 1.2070 -0.4334 0.2049 0.1587 404 ILE A N 3044 C CA . ILE A 390 ? 1.3686 1.4162 1.2069 -0.4375 0.2019 0.1489 404 ILE A CA 3045 C C . ILE A 390 ? 1.3679 1.4224 1.2092 -0.4398 0.2043 0.1492 404 ILE A C 3046 O O . ILE A 390 ? 1.3861 1.4463 1.2233 -0.4374 0.2054 0.1542 404 ILE A O 3047 C CB . ILE A 390 ? 1.2650 1.3194 1.0953 -0.4358 0.1945 0.1418 404 ILE A CB 3048 C CG1 . ILE A 390 ? 1.2588 1.3062 1.0864 -0.4336 0.1922 0.1412 404 ILE A CG1 3049 C CG2 . ILE A 390 ? 1.2450 1.3048 1.0783 -0.4399 0.1912 0.1326 404 ILE A CG2 3050 C CD1 . ILE A 390 ? 1.2440 1.2975 1.0634 -0.4315 0.1851 0.1352 404 ILE A CD1 3051 N N . GLN A 391 ? 1.3543 1.4083 1.2028 -0.4447 0.2051 0.1440 405 GLN A N 3052 C CA . GLN A 391 ? 1.3387 1.3983 1.1918 -0.4474 0.2080 0.1447 405 GLN A CA 3053 C C . GLN A 391 ? 1.2841 1.3531 1.1380 -0.4501 0.2037 0.1366 405 GLN A C 3054 O O . GLN A 391 ? 1.2704 1.3461 1.1272 -0.4516 0.2053 0.1372 405 GLN A O 3055 C CB . GLN A 391 ? 1.3597 1.4111 1.2224 -0.4512 0.2139 0.1472 405 GLN A CB 3056 C CG . GLN A 391 ? 1.3966 1.4431 1.2612 -0.4491 0.2202 0.1575 405 GLN A CG 3057 C CD . GLN A 391 ? 1.4333 1.4779 1.3068 -0.4532 0.2258 0.1596 405 GLN A CD 3058 O OE1 . GLN A 391 ? 1.4409 1.4817 1.3210 -0.4577 0.2265 0.1544 405 GLN A OE1 3059 N NE2 . GLN A 391 ? 1.4519 1.4992 1.3252 -0.4517 0.2298 0.1669 405 GLN A NE2 3060 N N . GLU A 392 ? 1.2345 1.3041 1.0862 -0.4507 0.1982 0.1295 406 GLU A N 3061 C CA . GLU A 392 ? 1.1900 1.2670 1.0446 -0.4542 0.1943 0.1219 406 GLU A CA 3062 C C . GLU A 392 ? 1.1714 1.2530 1.0198 -0.4524 0.1872 0.1159 406 GLU A C 3063 O O . GLU A 392 ? 1.1650 1.2406 1.0091 -0.4505 0.1852 0.1150 406 GLU A O 3064 C CB . GLU A 392 ? 1.1766 1.2475 1.0389 -0.4598 0.1961 0.1184 406 GLU A CB 3065 C CG . GLU A 392 ? 1.1895 1.2683 1.0562 -0.4642 0.1929 0.1120 406 GLU A CG 3066 C CD . GLU A 392 ? 1.2085 1.2809 1.0800 -0.4696 0.1928 0.1066 406 GLU A CD 3067 O OE1 . GLU A 392 ? 1.2026 1.2638 1.0745 -0.4697 0.1958 0.1079 406 GLU A OE1 3068 O OE2 . GLU A 392 ? 1.2140 1.2927 1.0891 -0.4737 0.1899 0.1014 406 GLU A OE2 3069 N N . LEU A 393 ? 1.1129 1.2054 0.9618 -0.4529 0.1837 0.1121 407 LEU A N 3070 C CA . LEU A 393 ? 1.0301 1.1284 0.8738 -0.4509 0.1772 0.1069 407 LEU A CA 3071 C C . LEU A 393 ? 0.9688 1.0755 0.8179 -0.4546 0.1736 0.1011 407 LEU A C 3072 O O . LEU A 393 ? 0.9363 1.0498 0.7909 -0.4562 0.1755 0.1023 407 LEU A O 3073 C CB . LEU A 393 ? 1.0331 1.1381 0.8706 -0.4460 0.1767 0.1099 407 LEU A CB 3074 C CG . LEU A 393 ? 1.0325 1.1326 0.8626 -0.4414 0.1788 0.1159 407 LEU A CG 3075 C CD1 . LEU A 393 ? 1.0190 1.1277 0.8426 -0.4374 0.1768 0.1161 407 LEU A CD1 3076 C CD2 . LEU A 393 ? 1.0438 1.1348 0.8700 -0.4403 0.1768 0.1151 407 LEU A CD2 3077 N N . GLN A 394 ? 0.9237 1.0302 0.7714 -0.4559 0.1683 0.0950 408 GLN A N 3078 C CA . GLN A 394 ? 0.9004 1.0164 0.7523 -0.4587 0.1637 0.0898 408 GLN A CA 3079 C C . GLN A 394 ? 0.8862 1.0125 0.7354 -0.4548 0.1605 0.0896 408 GLN A C 3080 O O . GLN A 394 ? 0.8769 1.0018 0.7187 -0.4503 0.1596 0.0908 408 GLN A O 3081 C CB . GLN A 394 ? 0.9115 1.0238 0.7624 -0.4617 0.1592 0.0834 408 GLN A CB 3082 C CG . GLN A 394 ? 0.9280 1.0321 0.7835 -0.4669 0.1623 0.0822 408 GLN A CG 3083 C CD . GLN A 394 ? 0.9400 1.0485 0.8037 -0.4703 0.1661 0.0847 408 GLN A CD 3084 O OE1 . GLN A 394 ? 0.9525 1.0717 0.8206 -0.4719 0.1634 0.0833 408 GLN A OE1 3085 N NE2 . GLN A 394 ? 0.9344 1.0349 0.8006 -0.4712 0.1724 0.0889 408 GLN A NE2 3086 N N . VAL A 395 ? 0.8977 1.0345 0.7534 -0.4565 0.1591 0.0883 409 VAL A N 3087 C CA . VAL A 395 ? 0.9004 1.0473 0.7555 -0.4528 0.1574 0.0887 409 VAL A CA 3088 C C . VAL A 395 ? 0.8767 1.0327 0.7357 -0.4541 0.1513 0.0839 409 VAL A C 3089 O O . VAL A 395 ? 0.8255 0.9864 0.6925 -0.4582 0.1503 0.0827 409 VAL A O 3090 C CB . VAL A 395 ? 1.0291 1.1813 0.8895 -0.4523 0.1628 0.0934 409 VAL A CB 3091 C CG1 . VAL A 395 ? 1.0225 1.1859 0.8847 -0.4493 0.1614 0.0930 409 VAL A CG1 3092 C CG2 . VAL A 395 ? 1.0320 1.1765 0.8869 -0.4498 0.1682 0.0987 409 VAL A CG2 3093 N N . TRP A 396 ? 0.8817 1.0401 0.7351 -0.4506 0.1471 0.0816 410 TRP A N 3094 C CA . TRP A 396 ? 0.8233 0.9908 0.6802 -0.4511 0.1413 0.0777 410 TRP A CA 3095 C C . TRP A 396 ? 0.8137 0.9904 0.6716 -0.4467 0.1413 0.0790 410 TRP A C 3096 O O . TRP A 396 ? 0.7806 0.9548 0.6313 -0.4425 0.1430 0.0803 410 TRP A O 3097 C CB . TRP A 396 ? 0.8208 0.9833 0.6709 -0.4512 0.1358 0.0730 410 TRP A CB 3098 C CG . TRP A 396 ? 0.8397 0.9937 0.6899 -0.4559 0.1359 0.0710 410 TRP A CG 3099 C CD1 . TRP A 396 ? 0.8324 0.9745 0.6782 -0.4562 0.1397 0.0723 410 TRP A CD1 3100 C CD2 . TRP A 396 ? 0.8473 1.0041 0.7024 -0.4610 0.1324 0.0673 410 TRP A CD2 3101 N NE1 . TRP A 396 ? 0.8051 0.9420 0.6531 -0.4613 0.1391 0.0692 410 TRP A NE1 3102 C CE2 . TRP A 396 ? 0.8003 0.9461 0.6534 -0.4645 0.1346 0.0659 410 TRP A CE2 3103 C CE3 . TRP A 396 ? 0.7851 0.9529 0.6463 -0.4631 0.1277 0.0652 410 TRP A CE3 3104 C CZ2 . TRP A 396 ? 0.8316 0.9768 0.6876 -0.4701 0.1324 0.0619 410 TRP A CZ2 3105 C CZ3 . TRP A 396 ? 0.8447 1.0125 0.7087 -0.4687 0.1250 0.0619 410 TRP A CZ3 3106 C CH2 . TRP A 396 ? 0.8320 0.9884 0.6929 -0.4722 0.1274 0.0599 410 TRP A CH2 3107 N N . TYR A 397 ? 0.8146 1.0021 0.6818 -0.4479 0.1397 0.0786 411 TYR A N 3108 C CA . TYR A 397 ? 0.8442 1.0406 0.7148 -0.4441 0.1413 0.0803 411 TYR A CA 3109 C C . TYR A 397 ? 0.7603 0.9662 0.6360 -0.4434 0.1358 0.0776 411 TYR A C 3110 O O . TYR A 397 ? 0.7585 0.9686 0.6405 -0.4471 0.1318 0.0762 411 TYR A O 3111 C CB . TYR A 397 ? 0.8807 1.0818 0.7604 -0.4452 0.1471 0.0844 411 TYR A CB 3112 C CG . TYR A 397 ? 0.9149 1.1258 0.8005 -0.4418 0.1494 0.0860 411 TYR A CG 3113 C CD1 . TYR A 397 ? 0.9440 1.1531 0.8235 -0.4376 0.1539 0.0876 411 TYR A CD1 3114 C CD2 . TYR A 397 ? 0.9094 1.1314 0.8069 -0.4428 0.1473 0.0859 411 TYR A CD2 3115 C CE1 . TYR A 397 ? 0.9468 1.1642 0.8317 -0.4346 0.1568 0.0886 411 TYR A CE1 3116 C CE2 . TYR A 397 ? 0.9176 1.1481 0.8216 -0.4395 0.1502 0.0875 411 TYR A CE2 3117 C CZ . TYR A 397 ? 0.9312 1.1590 0.8287 -0.4355 0.1552 0.0885 411 TYR A CZ 3118 O OH . TYR A 397 ? 0.9181 1.1538 0.8222 -0.4323 0.1588 0.0896 411 TYR A OH 3119 N N . THR A 398 ? 0.7537 0.9632 0.6266 -0.4388 0.1356 0.0772 412 THR A N 3120 C CA . THR A 398 ? 0.7436 0.9626 0.6223 -0.4375 0.1312 0.0754 412 THR A CA 3121 C C . THR A 398 ? 0.7406 0.9665 0.6235 -0.4333 0.1355 0.0775 412 THR A C 3122 O O . THR A 398 ? 0.7437 0.9651 0.6190 -0.4302 0.1396 0.0782 412 THR A O 3123 C CB . THR A 398 ? 0.7481 0.9636 0.6178 -0.4361 0.1250 0.0712 412 THR A CB 3124 O OG1 . THR A 398 ? 0.7399 0.9492 0.6064 -0.4403 0.1213 0.0689 412 THR A OG1 3125 C CG2 . THR A 398 ? 0.7263 0.9520 0.6024 -0.4344 0.1206 0.0698 412 THR A CG2 3126 N N . LYS A 399 ? 0.8218 1.0587 0.7172 -0.4333 0.1347 0.0784 413 LYS A N 3127 C CA . LYS A 399 ? 0.8648 1.1088 0.7666 -0.4295 0.1393 0.0803 413 LYS A CA 3128 C C . LYS A 399 ? 0.8683 1.1208 0.7766 -0.4276 0.1348 0.0788 413 LYS A C 3129 O O . LYS A 399 ? 0.9145 1.1743 0.8334 -0.4301 0.1311 0.0797 413 LYS A O 3130 C CB . LYS A 399 ? 0.9412 1.1909 0.8555 -0.4313 0.1447 0.0844 413 LYS A CB 3131 C CG . LYS A 399 ? 0.9749 1.2336 0.8998 -0.4280 0.1496 0.0864 413 LYS A CG 3132 C CD . LYS A 399 ? 1.0024 1.2567 0.9185 -0.4240 0.1557 0.0861 413 LYS A CD 3133 C CE . LYS A 399 ? 1.0218 1.2848 0.9485 -0.4206 0.1606 0.0873 413 LYS A CE 3134 N NZ . LYS A 399 ? 1.0366 1.2954 0.9539 -0.4169 0.1664 0.0862 413 LYS A NZ 3135 N N . LEU A 400 ? 0.8177 1.0695 0.7198 -0.4233 0.1351 0.0768 414 LEU A N 3136 C CA . LEU A 400 ? 0.8473 1.1063 0.7546 -0.4211 0.1308 0.0753 414 LEU A CA 3137 C C . LEU A 400 ? 0.8513 1.1200 0.7721 -0.4183 0.1359 0.0778 414 LEU A C 3138 O O . LEU A 400 ? 0.7932 1.0610 0.7143 -0.4165 0.1433 0.0793 414 LEU A O 3139 C CB . LEU A 400 ? 0.8672 1.1199 0.7604 -0.4183 0.1277 0.0712 414 LEU A CB 3140 C CG . LEU A 400 ? 0.8670 1.1114 0.7491 -0.4209 0.1215 0.0684 414 LEU A CG 3141 C CD1 . LEU A 400 ? 0.8452 1.0812 0.7120 -0.4180 0.1208 0.0654 414 LEU A CD1 3142 C CD2 . LEU A 400 ? 0.8772 1.1272 0.7650 -0.4229 0.1141 0.0670 414 LEU A CD2 3143 N N . GLY A 401 ? 0.9266 1.2045 0.8589 -0.4177 0.1322 0.0785 415 GLY A N 3144 C CA . GLY A 401 ? 0.9802 1.2679 0.9279 -0.4150 0.1371 0.0813 415 GLY A CA 3145 C C . GLY A 401 ? 1.0153 1.3124 0.9806 -0.4179 0.1366 0.0858 415 GLY A C 3146 O O . GLY A 401 ? 1.0265 1.3334 1.0061 -0.4166 0.1355 0.0880 415 GLY A O 3147 N N . ARG A 406 ? 1.1191 1.4194 1.0977 -0.4333 0.1305 0.0918 420 ARG A N 3148 C CA . ARG A 406 ? 1.1341 1.4223 1.0940 -0.4341 0.1278 0.0873 420 ARG A CA 3149 C C . ARG A 406 ? 1.1652 1.4482 1.1204 -0.4398 0.1248 0.0865 420 ARG A C 3150 O O . ARG A 406 ? 1.1964 1.4861 1.1609 -0.4437 0.1212 0.0881 420 ARG A O 3151 C CB . ARG A 406 ? 1.1072 1.3950 1.0604 -0.4318 0.1216 0.0838 420 ARG A CB 3152 N N . LEU A 407 ? 1.1433 1.4144 1.0844 -0.4403 0.1265 0.0841 421 LEU A N 3153 C CA . LEU A 407 ? 1.0917 1.3555 1.0268 -0.4454 0.1247 0.0828 421 LEU A CA 3154 C C . LEU A 407 ? 1.0558 1.3089 0.9750 -0.4449 0.1212 0.0782 421 LEU A C 3155 O O . LEU A 407 ? 1.0429 1.2903 0.9532 -0.4410 0.1238 0.0772 421 LEU A O 3156 C CB . LEU A 407 ? 1.0671 1.3258 1.0018 -0.4464 0.1319 0.0852 421 LEU A CB 3157 C CG . LEU A 407 ? 1.0647 1.3308 1.0134 -0.4481 0.1367 0.0897 421 LEU A CG 3158 C CD1 . LEU A 407 ? 1.0633 1.3404 1.0245 -0.4444 0.1392 0.0925 421 LEU A CD1 3159 C CD2 . LEU A 407 ? 1.0617 1.3197 1.0051 -0.4483 0.1436 0.0912 421 LEU A CD2 3160 N N . HIS A 408 ? 1.0190 1.2693 0.9346 -0.4490 0.1156 0.0755 422 HIS A N 3161 C CA . HIS A 408 ? 0.9519 1.1927 0.8536 -0.4484 0.1120 0.0711 422 HIS A CA 3162 C C . HIS A 408 ? 0.9016 1.1312 0.7954 -0.4525 0.1125 0.0691 422 HIS A C 3163 O O . HIS A 408 ? 0.9254 1.1563 0.8234 -0.4575 0.1107 0.0687 422 HIS A O 3164 C CB . HIS A 408 ? 0.9390 1.1856 0.8415 -0.4484 0.1045 0.0686 422 HIS A CB 3165 C CG . HIS A 408 ? 0.9175 1.1737 0.8268 -0.4438 0.1040 0.0702 422 HIS A CG 3166 N ND1 . HIS A 408 ? 0.9249 1.1817 0.8354 -0.4393 0.1099 0.0723 422 HIS A ND1 3167 C CD2 . HIS A 408 ? 0.8701 1.1354 0.7855 -0.4430 0.0987 0.0702 422 HIS A CD2 3168 C CE1 . HIS A 408 ? 0.8927 1.1582 0.8102 -0.4359 0.1087 0.0731 422 HIS A CE1 3169 N NE2 . HIS A 408 ? 0.8594 1.1303 0.7804 -0.4379 0.1018 0.0722 422 HIS A NE2 3170 N N . PHE A 409 ? 0.8415 1.0603 0.7242 -0.4503 0.1152 0.0679 423 PHE A N 3171 C CA . PHE A 409 ? 0.8384 1.0451 0.7132 -0.4532 0.1160 0.0660 423 PHE A CA 3172 C C . PHE A 409 ? 0.8497 1.0554 0.7308 -0.4583 0.1192 0.0678 423 PHE A C 3173 O O . PHE A 409 ? 0.7998 1.0011 0.6794 -0.4629 0.1171 0.0651 423 PHE A O 3174 C CB . PHE A 409 ? 0.8417 1.0445 0.7094 -0.4547 0.1098 0.0611 423 PHE A CB 3175 C CG . PHE A 409 ? 0.7532 0.9421 0.6107 -0.4554 0.1113 0.0589 423 PHE A CG 3176 C CD1 . PHE A 409 ? 0.8261 1.0078 0.6759 -0.4511 0.1146 0.0601 423 PHE A CD1 3177 C CD2 . PHE A 409 ? 0.7589 0.9421 0.6148 -0.4604 0.1097 0.0557 423 PHE A CD2 3178 C CE1 . PHE A 409 ? 0.7598 0.9291 0.6016 -0.4516 0.1161 0.0589 423 PHE A CE1 3179 C CE2 . PHE A 409 ? 0.8018 0.9719 0.6497 -0.4609 0.1117 0.0539 423 PHE A CE2 3180 C CZ . PHE A 409 ? 0.7653 0.9285 0.6066 -0.4564 0.1149 0.0558 423 PHE A CZ 3181 N N . LYS A 410 ? 0.9069 1.1166 0.7949 -0.4576 0.1245 0.0721 424 LYS A N 3182 C CA . LYS A 410 ? 0.9127 1.1226 0.8077 -0.4622 0.1278 0.0742 424 LYS A CA 3183 C C . LYS A 410 ? 0.8875 1.0853 0.7762 -0.4624 0.1336 0.0755 424 LYS A C 3184 O O . LYS A 410 ? 0.8682 1.0625 0.7521 -0.4581 0.1374 0.0777 424 LYS A O 3185 C CB . LYS A 410 ? 0.9425 1.1637 0.8496 -0.4615 0.1305 0.0784 424 LYS A CB 3186 C CG . LYS A 410 ? 0.9735 1.2068 0.8874 -0.4593 0.1261 0.0783 424 LYS A CG 3187 C CD . LYS A 410 ? 0.9819 1.2270 0.9105 -0.4622 0.1257 0.0813 424 LYS A CD 3188 C CE . LYS A 410 ? 0.9712 1.2278 0.9068 -0.4608 0.1200 0.0812 424 LYS A CE 3189 N NZ . LYS A 410 ? 0.9574 1.2127 0.8873 -0.4636 0.1125 0.0771 424 LYS A NZ 3190 N N . GLN A 411 ? 0.8614 1.0529 0.7501 -0.4673 0.1343 0.0742 425 GLN A N 3191 C CA . GLN A 411 ? 0.8775 1.0576 0.7617 -0.4676 0.1400 0.0760 425 GLN A CA 3192 C C . GLN A 411 ? 0.8765 1.0601 0.7682 -0.4681 0.1459 0.0808 425 GLN A C 3193 O O . GLN A 411 ? 0.8945 1.0855 0.7955 -0.4717 0.1456 0.0815 425 GLN A O 3194 C CB . GLN A 411 ? 0.9117 1.0828 0.7933 -0.4727 0.1393 0.0727 425 GLN A CB 3195 C CG . GLN A 411 ? 0.9488 1.1067 0.8253 -0.4722 0.1450 0.0745 425 GLN A CG 3196 C CD . GLN A 411 ? 0.9825 1.1307 0.8567 -0.4769 0.1448 0.0707 425 GLN A CD 3197 O OE1 . GLN A 411 ? 1.0071 1.1588 0.8848 -0.4818 0.1417 0.0673 425 GLN A OE1 3198 N NE2 . GLN A 411 ? 0.9820 1.1179 0.8504 -0.4754 0.1484 0.0715 425 GLN A NE2 3199 N N . LEU A 412 ? 0.8580 1.0367 0.7456 -0.4645 0.1511 0.0843 426 LEU A N 3200 C CA . LEU A 412 ? 0.9062 1.0875 0.7997 -0.4645 0.1572 0.0890 426 LEU A CA 3201 C C . LEU A 412 ? 0.9372 1.1078 0.8288 -0.4670 0.1620 0.0909 426 LEU A C 3202 O O . LEU A 412 ? 0.9109 1.0718 0.7965 -0.4681 0.1610 0.0888 426 LEU A O 3203 C CB . LEU A 412 ? 0.9203 1.1041 0.8104 -0.4588 0.1601 0.0919 426 LEU A CB 3204 C CG . LEU A 412 ? 0.9198 1.1142 0.8128 -0.4557 0.1569 0.0907 426 LEU A CG 3205 C CD1 . LEU A 412 ? 0.8851 1.0810 0.7749 -0.4507 0.1613 0.0935 426 LEU A CD1 3206 C CD2 . LEU A 412 ? 0.9548 1.1603 0.8609 -0.4587 0.1556 0.0911 426 LEU A CD2 3207 N N . ASP A 413 ? 1.0082 1.1803 0.9052 -0.4677 0.1676 0.0951 427 ASP A N 3208 C CA . ASP A 413 ? 1.0555 1.2182 0.9522 -0.4702 0.1726 0.0975 427 ASP A CA 3209 C C . ASP A 413 ? 1.0067 1.1587 0.8935 -0.4667 0.1748 0.0993 427 ASP A C 3210 O O . ASP A 413 ? 1.0243 1.1777 0.9056 -0.4618 0.1752 0.1010 427 ASP A O 3211 C CB . ASP A 413 ? 1.1513 1.3184 1.0554 -0.4710 0.1783 0.1021 427 ASP A CB 3212 C CG . ASP A 413 ? 1.2172 1.3956 1.1322 -0.4745 0.1763 0.1011 427 ASP A CG 3213 O OD1 . ASP A 413 ? 1.2327 1.4102 1.1519 -0.4798 0.1746 0.0988 427 ASP A OD1 3214 O OD2 . ASP A 413 ? 1.2362 1.4243 1.1559 -0.4720 0.1767 0.1027 427 ASP A OD2 3215 N N . THR A 414 ? 0.9631 1.1045 0.8480 -0.4692 0.1763 0.0988 428 THR A N 3216 C CA . THR A 414 ? 0.9591 1.0896 0.8362 -0.4663 0.1786 0.1011 428 THR A CA 3217 C C . THR A 414 ? 1.0029 1.1335 0.8775 -0.4623 0.1837 0.1074 428 THR A C 3218 O O . THR A 414 ? 0.9992 1.1342 0.8795 -0.4634 0.1877 0.1105 428 THR A O 3219 C CB . THR A 414 ? 0.8700 0.9895 0.7489 -0.4702 0.1814 0.1008 428 THR A CB 3220 O OG1 . THR A 414 ? 0.8693 0.9879 0.7485 -0.4737 0.1765 0.0945 428 THR A OG1 3221 C CG2 . THR A 414 ? 1.0899 1.1985 0.9627 -0.4670 0.1847 0.1046 428 THR A CG2 3222 N N . LEU A 415 ? 1.0152 1.1415 0.8811 -0.4578 0.1835 0.1092 429 LEU A N 3223 C CA . LEU A 415 ? 1.0438 1.1688 0.9060 -0.4543 0.1884 0.1155 429 LEU A CA 3224 C C . LEU A 415 ? 1.1143 1.2277 0.9752 -0.4547 0.1928 0.1201 429 LEU A C 3225 O O . LEU A 415 ? 1.1090 1.2147 0.9651 -0.4532 0.1914 0.1199 429 LEU A O 3226 C CB . LEU A 415 ? 1.0122 1.1407 0.8658 -0.4491 0.1859 0.1155 429 LEU A CB 3227 C CG . LEU A 415 ? 0.9730 1.1123 0.8283 -0.4475 0.1869 0.1159 429 LEU A CG 3228 C CD1 . LEU A 415 ? 0.9582 1.1004 0.8047 -0.4425 0.1851 0.1158 429 LEU A CD1 3229 C CD2 . LEU A 415 ? 0.9170 1.0564 0.7762 -0.4485 0.1935 0.1214 429 LEU A CD2 3230 N N . TRP A 416 ? 1.1879 1.3004 1.0542 -0.4566 0.1984 0.1244 430 TRP A N 3231 C CA . TRP A 416 ? 1.2232 1.3256 1.0894 -0.4566 0.2035 0.1302 430 TRP A CA 3232 C C . TRP A 416 ? 1.2764 1.3795 1.1362 -0.4520 0.2064 0.1366 430 TRP A C 3233 O O . TRP A 416 ? 1.2800 1.3911 1.1394 -0.4509 0.2077 0.1379 430 TRP A O 3234 C CB . TRP A 416 ? 1.1968 1.2976 1.0721 -0.4612 0.2081 0.1316 430 TRP A CB 3235 C CG . TRP A 416 ? 1.1912 1.2909 1.0721 -0.4661 0.2053 0.1253 430 TRP A CG 3236 C CD1 . TRP A 416 ? 1.1833 1.2918 1.0688 -0.4690 0.2017 0.1201 430 TRP A CD1 3237 C CD2 . TRP A 416 ? 1.2087 1.2979 1.0912 -0.4686 0.2058 0.1235 430 TRP A CD2 3238 N NE1 . TRP A 416 ? 1.1975 1.3019 1.0864 -0.4736 0.1997 0.1151 430 TRP A NE1 3239 C CE2 . TRP A 416 ? 1.2149 1.3072 1.1020 -0.4735 0.2024 0.1167 430 TRP A CE2 3240 C CE3 . TRP A 416 ? 1.2284 1.3061 1.1093 -0.4674 0.2092 0.1272 430 TRP A CE3 3241 C CZ2 . TRP A 416 ? 1.2429 1.3269 1.1322 -0.4773 0.2023 0.1128 430 TRP A CZ2 3242 C CZ3 . TRP A 416 ? 1.2524 1.3214 1.1366 -0.4709 0.2094 0.1236 430 TRP A CZ3 3243 C CH2 . TRP A 416 ? 1.2598 1.3319 1.1477 -0.4759 0.2061 0.1161 430 TRP A CH2 3244 N N . LEU A 417 ? 1.3270 1.4221 1.1817 -0.4494 0.2073 0.1407 431 LEU A N 3245 C CA . LEU A 417 ? 1.3712 1.4667 1.2191 -0.4453 0.2098 0.1474 431 LEU A CA 3246 C C . LEU A 417 ? 1.4508 1.5451 1.3035 -0.4468 0.2164 0.1537 431 LEU A C 3247 O O . LEU A 417 ? 1.4771 1.5762 1.3262 -0.4448 0.2189 0.1578 431 LEU A O 3248 C CB . LEU A 417 ? 1.3382 1.4261 1.1801 -0.4421 0.2086 0.1504 431 LEU A CB 3249 C CG . LEU A 417 ? 1.2877 1.3785 1.1247 -0.4408 0.2018 0.1434 431 LEU A CG 3250 C CD1 . LEU A 417 ? 1.2862 1.3697 1.1180 -0.4379 0.2000 0.1452 431 LEU A CD1 3251 C CD2 . LEU A 417 ? 1.2449 1.3464 1.0764 -0.4383 0.1993 0.1413 431 LEU A CD2 3252 N N . LEU A 418 ? 1.4892 1.5771 1.3501 -0.4506 0.2194 0.1541 432 LEU A N 3253 C CA . LEU A 418 ? 1.5094 1.5965 1.3768 -0.4530 0.2254 0.1588 432 LEU A CA 3254 C C . LEU A 418 ? 1.5283 1.6132 1.3920 -0.4501 0.2303 0.1681 432 LEU A C 3255 O O . LEU A 418 ? 1.5296 1.6134 1.3983 -0.4519 0.2356 0.1727 432 LEU A O 3256 C CB . LEU A 418 ? 1.5001 1.5974 1.3717 -0.4554 0.2251 0.1549 432 LEU A CB 3257 N N . ASP A 419 ? 1.5330 1.6176 1.3878 -0.4457 0.2283 0.1709 433 ASP A N 3258 C CA . ASP A 419 ? 1.5462 1.6292 1.3963 -0.4428 0.2320 0.1799 433 ASP A CA 3259 C C . ASP A 419 ? 1.5182 1.5908 1.3691 -0.4414 0.2333 0.1853 433 ASP A C 3260 O O . ASP A 419 ? 1.5208 1.5863 1.3785 -0.4437 0.2336 0.1829 433 ASP A O 3261 C CB . ASP A 419 ? 1.5597 1.6503 1.3989 -0.4389 0.2289 0.1796 433 ASP A CB 3262 C CG . ASP A 419 ? 1.5742 1.6743 1.4125 -0.4396 0.2305 0.1782 433 ASP A CG 3263 O OD1 . ASP A 419 ? 1.5850 1.6874 1.4314 -0.4431 0.2324 0.1755 433 ASP A OD1 3264 O OD2 . ASP A 419 ? 1.5695 1.6750 1.3992 -0.4367 0.2299 0.1799 433 ASP A OD2 3265 N N . GLY A 420 ? 1.4788 1.5508 1.3229 -0.4376 0.2343 0.1927 434 GLY A N 3266 C CA . GLY A 420 ? 1.4287 1.4929 1.2715 -0.4350 0.2340 0.1978 434 GLY A CA 3267 C C . GLY A 420 ? 1.3553 1.4252 1.1862 -0.4309 0.2293 0.1978 434 GLY A C 3268 O O . GLY A 420 ? 1.3207 1.3869 1.1478 -0.4277 0.2282 0.2028 434 GLY A O 3269 N N . SER A 421 ? 1.3257 1.4051 1.1516 -0.4310 0.2267 0.1922 435 SER A N 3270 C CA . SER A 421 ? 1.2942 1.3806 1.1089 -0.4277 0.2227 0.1911 435 SER A CA 3271 C C . SER A 421 ? 1.2853 1.3701 1.0962 -0.4258 0.2167 0.1861 435 SER A C 3272 O O . SER A 421 ? 1.2774 1.3608 1.0816 -0.4225 0.2147 0.1902 435 SER A O 3273 C CB . SER A 421 ? 1.2570 1.3533 1.0697 -0.4289 0.2222 0.1854 435 SER A CB 3274 O OG . SER A 421 ? 1.2448 1.3478 1.0470 -0.4259 0.2191 0.1843 435 SER A OG 3275 N N . GLY A 422 ? 1.2801 1.3653 1.0953 -0.4280 0.2138 0.1775 436 GLY A N 3276 C CA . GLY A 422 ? 1.2523 1.3370 1.0636 -0.4265 0.2079 0.1716 436 GLY A CA 3277 C C . GLY A 422 ? 1.2234 1.3181 1.0272 -0.4249 0.2039 0.1663 436 GLY A C 3278 O O . GLY A 422 ? 1.2141 1.3103 1.0107 -0.4221 0.1993 0.1642 436 GLY A O 3279 N N . SER A 423 ? 1.1908 1.2923 0.9969 -0.4267 0.2059 0.1642 437 SER A N 3280 C CA . SER A 423 ? 1.1334 1.2444 0.9341 -0.4254 0.2034 0.1593 437 SER A CA 3281 C C . SER A 423 ? 1.0687 1.1854 0.8770 -0.4284 0.2037 0.1530 437 SER A C 3282 O O . SER A 423 ? 1.0274 1.1420 0.8441 -0.4317 0.2072 0.1541 437 SER A O 3283 C CB . SER A 423 ? 1.1383 1.2536 0.9318 -0.4234 0.2064 0.1648 437 SER A CB 3284 O OG . SER A 423 ? 1.1296 1.2539 0.9198 -0.4228 0.2055 0.1598 437 SER A OG 3285 N N . PHE A 424 ? 1.0470 1.1710 0.8527 -0.4274 0.2002 0.1469 438 PHE A N 3286 C CA . PHE A 424 ? 1.0312 1.1617 0.8444 -0.4298 0.2000 0.1412 438 PHE A CA 3287 C C . PHE A 424 ? 0.9980 1.1374 0.8070 -0.4275 0.1981 0.1368 438 PHE A C 3288 O O . PHE A 424 ? 0.9516 1.0915 0.7515 -0.4244 0.1955 0.1365 438 PHE A O 3289 C CB . PHE A 424 ? 1.0660 1.1936 0.8861 -0.4324 0.1964 0.1362 438 PHE A CB 3290 C CG . PHE A 424 ? 1.0745 1.2007 0.8892 -0.4304 0.1903 0.1319 438 PHE A CG 3291 C CD1 . PHE A 424 ? 1.0897 1.2076 0.8994 -0.4289 0.1890 0.1347 438 PHE A CD1 3292 C CD2 . PHE A 424 ? 1.0514 1.1845 0.8667 -0.4301 0.1860 0.1254 438 PHE A CD2 3293 C CE1 . PHE A 424 ? 1.0816 1.1982 0.8865 -0.4271 0.1836 0.1307 438 PHE A CE1 3294 C CE2 . PHE A 424 ? 1.0642 1.1960 0.8744 -0.4283 0.1804 0.1214 438 PHE A CE2 3295 C CZ . PHE A 424 ? 1.0597 1.1832 0.8646 -0.4269 0.1792 0.1239 438 PHE A CZ 3296 N N . THR A 425 ? 1.0220 1.1685 0.8382 -0.4293 0.1994 0.1336 439 THR A N 3297 C CA . THR A 425 ? 1.0597 1.2147 0.8739 -0.4273 0.1992 0.1300 439 THR A CA 3298 C C . THR A 425 ? 1.1102 1.2712 0.9335 -0.4288 0.1965 0.1241 439 THR A C 3299 O O . THR A 425 ? 1.1252 1.2858 0.9577 -0.4321 0.1967 0.1237 439 THR A O 3300 C CB . THR A 425 ? 1.0618 1.2207 0.8757 -0.4273 0.2056 0.1336 439 THR A CB 3301 O OG1 . THR A 425 ? 1.0962 1.2493 0.9030 -0.4265 0.2081 0.1400 439 THR A OG1 3302 C CG2 . THR A 425 ? 1.0297 1.1960 0.8396 -0.4249 0.2062 0.1303 439 THR A CG2 3303 N N . LEU A 426 ? 1.1045 1.2714 0.9254 -0.4265 0.1939 0.1198 440 LEU A N 3304 C CA . LEU A 426 ? 1.1119 1.2854 0.9416 -0.4274 0.1911 0.1147 440 LEU A CA 3305 C C . LEU A 426 ? 1.1172 1.2993 0.9484 -0.4254 0.1935 0.1126 440 LEU A C 3306 O O . LEU A 426 ? 1.1263 1.3089 0.9487 -0.4225 0.1950 0.1128 440 LEU A O 3307 C CB . LEU A 426 ? 1.1375 1.3089 0.9643 -0.4267 0.1842 0.1105 440 LEU A CB 3308 C CG . LEU A 426 ? 1.1600 1.3233 0.9868 -0.4289 0.1808 0.1107 440 LEU A CG 3309 C CD1 . LEU A 426 ? 1.1627 1.3175 0.9802 -0.4274 0.1820 0.1150 440 LEU A CD1 3310 C CD2 . LEU A 426 ? 1.1700 1.3343 0.9968 -0.4287 0.1741 0.1052 440 LEU A CD2 3311 N N . GLU A 427 ? 1.1308 1.3201 0.9738 -0.4269 0.1939 0.1105 441 GLU A N 3312 C CA . GLU A 427 ? 1.1598 1.3575 1.0067 -0.4248 0.1959 0.1080 441 GLU A CA 3313 C C . GLU A 427 ? 1.1300 1.3309 0.9784 -0.4236 0.1898 0.1033 441 GLU A C 3314 O O . GLU A 427 ? 1.1314 1.3336 0.9873 -0.4258 0.1857 0.1018 441 GLU A O 3315 C CB . GLU A 427 ? 1.2261 1.4303 1.0865 -0.4270 0.2005 0.1095 441 GLU A CB 3316 C CG . GLU A 427 ? 1.2840 1.4967 1.1499 -0.4248 0.2045 0.1079 441 GLU A CG 3317 C CD . GLU A 427 ? 1.3383 1.5568 1.2171 -0.4268 0.2102 0.1103 441 GLU A CD 3318 O OE1 . GLU A 427 ? 1.3556 1.5725 1.2402 -0.4301 0.2102 0.1128 441 GLU A OE1 3319 O OE2 . GLU A 427 ? 1.3532 1.5778 1.2367 -0.4251 0.2150 0.1097 441 GLU A OE2 3320 N N . LEU A 428 ? 1.0944 1.2967 0.9355 -0.4202 0.1892 0.1008 442 LEU A N 3321 C CA . LEU A 428 ? 1.0515 1.2564 0.8931 -0.4187 0.1834 0.0963 442 LEU A CA 3322 C C . LEU A 428 ? 1.0458 1.2593 0.8939 -0.4165 0.1861 0.0941 442 LEU A C 3323 O O . LEU A 428 ? 1.0873 1.3018 0.9306 -0.4144 0.1911 0.0941 442 LEU A O 3324 C CB . LEU A 428 ? 1.0282 1.2267 0.8556 -0.4164 0.1794 0.0950 442 LEU A CB 3325 C CG . LEU A 428 ? 1.0215 1.2108 0.8410 -0.4175 0.1784 0.0982 442 LEU A CG 3326 C CD1 . LEU A 428 ? 0.9989 1.1835 0.8050 -0.4146 0.1756 0.0974 442 LEU A CD1 3327 C CD2 . LEU A 428 ? 1.0170 1.2028 0.8421 -0.4207 0.1742 0.0979 442 LEU A CD2 3328 N N . GLU A 429 ? 1.0024 1.2221 0.8617 -0.4172 0.1832 0.0922 443 GLU A N 3329 C CA . GLU A 429 ? 1.0048 1.2326 0.8717 -0.4149 0.1854 0.0902 443 GLU A CA 3330 C C . GLU A 429 ? 0.9889 1.2166 0.8505 -0.4126 0.1793 0.0861 443 GLU A C 3331 O O . GLU A 429 ? 0.9402 1.1611 0.7902 -0.4123 0.1749 0.0850 443 GLU A O 3332 C CB . GLU A 429 ? 1.0534 1.2892 0.9379 -0.4169 0.1864 0.0917 443 GLU A CB 3333 C CG . GLU A 429 ? 1.1062 1.3402 0.9953 -0.4205 0.1890 0.0956 443 GLU A CG 3334 C CD . GLU A 429 ? 1.1369 1.3788 1.0409 -0.4212 0.1951 0.0982 443 GLU A CD 3335 O OE1 . GLU A 429 ? 1.1417 1.3909 1.0542 -0.4190 0.1970 0.0971 443 GLU A OE1 3336 O OE2 . GLU A 429 ? 1.1538 1.3946 1.0616 -0.4240 0.1981 0.1014 443 GLU A OE2 3337 N N . GLU A 430 ? 1.0037 1.2390 0.8744 -0.4109 0.1793 0.0841 444 GLU A N 3338 C CA . GLU A 430 ? 1.0167 1.2525 0.8829 -0.4085 0.1742 0.0803 444 GLU A CA 3339 C C . GLU A 430 ? 0.9662 1.2038 0.8382 -0.4104 0.1664 0.0794 444 GLU A C 3340 O O . GLU A 430 ? 0.9602 1.2019 0.8438 -0.4132 0.1658 0.0815 444 GLU A O 3341 C CB . GLU A 430 ? 1.0920 1.3346 0.9646 -0.4053 0.1786 0.0786 444 GLU A CB 3342 C CG . GLU A 430 ? 1.1940 1.4359 1.0634 -0.4041 0.1874 0.0794 444 GLU A CG 3343 C CD . GLU A 430 ? 1.2474 1.4967 1.1274 -0.4016 0.1933 0.0783 444 GLU A CD 3344 O OE1 . GLU A 430 ? 1.2523 1.5057 1.1373 -0.3997 0.1902 0.0759 444 GLU A OE1 3345 O OE2 . GLU A 430 ? 1.2645 1.5154 1.1480 -0.4015 0.2012 0.0798 444 GLU A OE2 3346 N N . ASP A 431 ? 0.8935 1.1281 0.7571 -0.4090 0.1605 0.0761 445 ASP A N 3347 C CA . ASP A 431 ? 0.8395 1.0756 0.7068 -0.4107 0.1528 0.0746 445 ASP A CA 3348 C C . ASP A 431 ? 0.7938 1.0256 0.6615 -0.4150 0.1498 0.0762 445 ASP A C 3349 O O . ASP A 431 ? 0.7767 1.0130 0.6537 -0.4175 0.1459 0.0763 445 ASP A O 3350 C CB . ASP A 431 ? 0.8510 1.0976 0.7336 -0.4101 0.1522 0.0746 445 ASP A CB 3351 C CG . ASP A 431 ? 0.8836 1.1340 0.7665 -0.4059 0.1552 0.0727 445 ASP A CG 3352 O OD1 . ASP A 431 ? 0.9254 1.1701 0.7949 -0.4036 0.1554 0.0701 445 ASP A OD1 3353 O OD2 . ASP A 431 ? 0.8760 1.1352 0.7731 -0.4048 0.1576 0.0737 445 ASP A OD2 3354 N N . GLU A 432 ? 0.8012 1.0244 0.6589 -0.4158 0.1514 0.0774 446 GLU A N 3355 C CA . GLU A 432 ? 0.8116 1.0298 0.6697 -0.4199 0.1496 0.0789 446 GLU A CA 3356 C C . GLU A 432 ? 0.8082 1.0165 0.6536 -0.4202 0.1455 0.0773 446 GLU A C 3357 O O . GLU A 432 ? 0.7766 0.9805 0.6112 -0.4172 0.1458 0.0766 446 GLU A O 3358 C CB . GLU A 432 ? 0.8068 1.0238 0.6680 -0.4214 0.1562 0.0829 446 GLU A CB 3359 C CG . GLU A 432 ? 0.8276 1.0542 0.7033 -0.4220 0.1601 0.0849 446 GLU A CG 3360 C CD . GLU A 432 ? 0.9064 1.1320 0.7844 -0.4230 0.1674 0.0887 446 GLU A CD 3361 O OE1 . GLU A 432 ? 0.9255 1.1430 0.7940 -0.4234 0.1693 0.0902 446 GLU A OE1 3362 O OE2 . GLU A 432 ? 0.9327 1.1659 0.8226 -0.4232 0.1714 0.0904 446 GLU A OE2 3363 N N . ILE A 433 ? 0.8003 1.0051 0.6475 -0.4238 0.1418 0.0769 447 ILE A N 3364 C CA . ILE A 433 ? 0.7928 0.9874 0.6298 -0.4245 0.1392 0.0760 447 ILE A CA 3365 C C . ILE A 433 ? 0.8105 0.9996 0.6500 -0.4283 0.1419 0.0787 447 ILE A C 3366 O O . ILE A 433 ? 0.7613 0.9545 0.6105 -0.4317 0.1418 0.0791 447 ILE A O 3367 C CB . ILE A 433 ? 0.7437 0.9374 0.5791 -0.4256 0.1319 0.0718 447 ILE A CB 3368 C CG1 . ILE A 433 ? 0.7335 0.9337 0.5684 -0.4223 0.1287 0.0690 447 ILE A CG1 3369 C CG2 . ILE A 433 ? 0.7996 0.9822 0.6246 -0.4259 0.1302 0.0711 447 ILE A CG2 3370 C CD1 . ILE A 433 ? 0.7259 0.9262 0.5598 -0.4234 0.1214 0.0650 447 ILE A CD1 3371 N N . PHE A 434 ? 0.7679 0.9480 0.5990 -0.4277 0.1442 0.0808 448 PHE A N 3372 C CA . PHE A 434 ? 0.8740 1.0475 0.7069 -0.4310 0.1470 0.0835 448 PHE A CA 3373 C C . PHE A 434 ? 0.8328 0.9960 0.6577 -0.4313 0.1445 0.0826 448 PHE A C 3374 O O . PHE A 434 ? 0.7792 0.9383 0.5950 -0.4279 0.1443 0.0833 448 PHE A O 3375 C CB . PHE A 434 ? 0.9189 1.0911 0.7507 -0.4299 0.1538 0.0885 448 PHE A CB 3376 C CG . PHE A 434 ? 0.9358 1.1169 0.7770 -0.4305 0.1577 0.0900 448 PHE A CG 3377 C CD1 . PHE A 434 ? 0.9167 1.1058 0.7594 -0.4275 0.1582 0.0889 448 PHE A CD1 3378 C CD2 . PHE A 434 ? 0.9578 1.1389 0.8068 -0.4340 0.1612 0.0927 448 PHE A CD2 3379 C CE1 . PHE A 434 ? 0.9188 1.1158 0.7711 -0.4279 0.1624 0.0905 448 PHE A CE1 3380 C CE2 . PHE A 434 ? 0.9471 1.1364 0.8054 -0.4345 0.1650 0.0944 448 PHE A CE2 3381 C CZ . PHE A 434 ? 0.9379 1.1351 0.7980 -0.4314 0.1657 0.0934 448 PHE A CZ 3382 N N . THR A 435 ? 0.8137 0.9726 0.6421 -0.4353 0.1429 0.0811 449 THR A N 3383 C CA . THR A 435 ? 0.8308 0.9787 0.6530 -0.4358 0.1424 0.0811 449 THR A CA 3384 C C . THR A 435 ? 0.8569 0.9983 0.6826 -0.4386 0.1476 0.0849 449 THR A C 3385 O O . THR A 435 ? 0.8593 1.0030 0.6931 -0.4426 0.1488 0.0845 449 THR A O 3386 C CB . THR A 435 ? 0.8315 0.9773 0.6528 -0.4378 0.1365 0.0756 449 THR A CB 3387 O OG1 . THR A 435 ? 0.7696 0.9221 0.5882 -0.4350 0.1317 0.0725 449 THR A OG1 3388 C CG2 . THR A 435 ? 0.8402 0.9741 0.6550 -0.4376 0.1367 0.0758 449 THR A CG2 3389 N N . LEU A 436 ? 0.8590 0.9926 0.6787 -0.4364 0.1509 0.0890 450 LEU A N 3390 C CA . LEU A 436 ? 0.8975 1.0241 0.7202 -0.4385 0.1563 0.0934 450 LEU A CA 3391 C C . LEU A 436 ? 0.8928 1.0083 0.7115 -0.4387 0.1559 0.0935 450 LEU A C 3392 O O . LEU A 436 ? 0.8848 0.9970 0.6960 -0.4350 0.1546 0.0947 450 LEU A O 3393 C CB . LEU A 436 ? 0.8934 1.0212 0.7136 -0.4357 0.1614 0.0995 450 LEU A CB 3394 C CG . LEU A 436 ? 0.9071 1.0459 0.7285 -0.4339 0.1616 0.0991 450 LEU A CG 3395 C CD1 . LEU A 436 ? 0.9372 1.0761 0.7513 -0.4299 0.1649 0.1037 450 LEU A CD1 3396 C CD2 . LEU A 436 ? 0.8999 1.0443 0.7313 -0.4372 0.1646 0.0996 450 LEU A CD2 3397 N N . THR A 437 ? 0.8914 1.0010 0.7155 -0.4429 0.1571 0.0921 451 THR A N 3398 C CA . THR A 437 ? 0.9024 1.0011 0.7240 -0.4434 0.1571 0.0914 451 THR A CA 3399 C C . THR A 437 ? 0.8954 0.9862 0.7236 -0.4475 0.1619 0.0930 451 THR A C 3400 O O . THR A 437 ? 0.8878 0.9822 0.7227 -0.4512 0.1634 0.0921 451 THR A O 3401 C CB . THR A 437 ? 0.9162 1.0157 0.7358 -0.4445 0.1508 0.0841 451 THR A CB 3402 O OG1 . THR A 437 ? 0.9206 1.0090 0.7396 -0.4460 0.1516 0.0828 451 THR A OG1 3403 C CG2 . THR A 437 ? 0.8156 0.9229 0.6413 -0.4487 0.1481 0.0794 451 THR A CG2 3404 N N . THR A 438 ? 0.9065 0.9864 0.7332 -0.4466 0.1646 0.0956 452 THR A N 3405 C CA . THR A 438 ? 0.9367 1.0074 0.7698 -0.4504 0.1694 0.0965 452 THR A CA 3406 C C . THR A 438 ? 0.9897 1.0590 0.8257 -0.4553 0.1664 0.0885 452 THR A C 3407 O O . THR A 438 ? 1.0147 1.0794 0.8570 -0.4598 0.1697 0.0874 452 THR A O 3408 C CB . THR A 438 ? 0.9437 1.0031 0.7750 -0.4477 0.1731 0.1017 452 THR A CB 3409 O OG1 . THR A 438 ? 0.9585 1.0151 0.7842 -0.4457 0.1688 0.0982 452 THR A OG1 3410 C CG2 . THR A 438 ? 0.9532 1.0145 0.7815 -0.4433 0.1761 0.1101 452 THR A CG2 3411 N N . LEU A 439 ? 0.6935 1.0145 0.8024 -0.3702 0.0385 0.1020 453 LEU A N 3412 C CA . LEU A 439 ? 0.6881 1.0032 0.8024 -0.3687 0.0370 0.0956 453 LEU A CA 3413 C C . LEU A 439 ? 0.6709 0.9831 0.7900 -0.3688 0.0378 0.0898 453 LEU A C 3414 O O . LEU A 439 ? 0.6365 0.9524 0.7511 -0.3684 0.0401 0.0868 453 LEU A O 3415 C CB . LEU A 439 ? 0.6853 1.0021 0.7917 -0.3654 0.0368 0.0898 453 LEU A CB 3416 C CG . LEU A 439 ? 0.6730 0.9920 0.7750 -0.3647 0.0357 0.0939 453 LEU A CG 3417 C CD1 . LEU A 439 ? 0.6675 0.9888 0.7607 -0.3615 0.0361 0.0873 453 LEU A CD1 3418 C CD2 . LEU A 439 ? 0.6726 0.9864 0.7843 -0.3660 0.0329 0.0971 453 LEU A CD2 3419 N N . THR A 440 ? 0.7054 1.0114 0.8340 -0.3694 0.0360 0.0880 454 THR A N 3420 C CA . THR A 440 ? 0.7700 1.0727 0.9049 -0.3699 0.0363 0.0832 454 THR A CA 3421 C C . THR A 440 ? 0.7626 1.0628 0.8973 -0.3674 0.0353 0.0743 454 THR A C 3422 O O . THR A 440 ? 0.7264 1.0240 0.8662 -0.3674 0.0353 0.0696 454 THR A O 3423 C CB . THR A 440 ? 0.8061 1.1033 0.9530 -0.3728 0.0348 0.0875 454 THR A CB 3424 O OG1 . THR A 440 ? 0.8241 1.1175 0.9755 -0.3726 0.0322 0.0880 454 THR A OG1 3425 C CG2 . THR A 440 ? 0.8072 1.1066 0.9550 -0.3757 0.0356 0.0966 454 THR A CG2 3426 N N . THR A 441 ? 0.7762 1.0776 0.9050 -0.3652 0.0345 0.0722 455 THR A N 3427 C CA . THR A 441 ? 0.7471 1.0460 0.8758 -0.3630 0.0330 0.0646 455 THR A CA 3428 C C . THR A 441 ? 0.7410 1.0427 0.8631 -0.3606 0.0343 0.0582 455 THR A C 3429 O O . THR A 441 ? 0.7861 1.0862 0.9077 -0.3588 0.0330 0.0519 455 THR A O 3430 C CB . THR A 441 ? 0.9528 1.2518 1.0782 -0.3618 0.0313 0.0650 455 THR A CB 3431 O OG1 . THR A 441 ? 0.9597 1.2641 1.0743 -0.3601 0.0327 0.0660 455 THR A OG1 3432 C CG2 . THR A 441 ? 0.9388 1.2353 1.0715 -0.3642 0.0299 0.0717 455 THR A CG2 3433 N N . GLY A 442 ? 0.7174 1.0234 0.8347 -0.3607 0.0367 0.0597 456 GLY A N 3434 C CA . GLY A 442 ? 0.7224 1.0315 0.8337 -0.3585 0.0381 0.0541 456 GLY A CA 3435 C C . GLY A 442 ? 0.7289 1.0354 0.8457 -0.3580 0.0376 0.0481 456 GLY A C 3436 O O . GLY A 442 ? 0.7334 1.0371 0.8582 -0.3599 0.0373 0.0490 456 GLY A O 3437 N N . ARG A 443 ? 0.7172 1.0248 0.8297 -0.3555 0.0374 0.0422 457 ARG A N 3438 C CA . ARG A 443 ? 0.6891 0.9947 0.8063 -0.3549 0.0366 0.0366 457 ARG A CA 3439 C C . ARG A 443 ? 0.6589 0.9674 0.7705 -0.3523 0.0371 0.0315 457 ARG A C 3440 O O . ARG A 443 ? 0.6817 0.9910 0.7868 -0.3505 0.0364 0.0301 457 ARG A O 3441 C CB . ARG A 443 ? 0.7194 1.0201 0.8422 -0.3550 0.0337 0.0342 457 ARG A CB 3442 C CG . ARG A 443 ? 0.7862 1.0855 0.9122 -0.3538 0.0323 0.0278 457 ARG A CG 3443 C CD . ARG A 443 ? 0.8758 1.1708 1.0066 -0.3540 0.0294 0.0251 457 ARG A CD 3444 N NE . ARG A 443 ? 0.9409 1.2353 1.0737 -0.3528 0.0279 0.0190 457 ARG A NE 3445 C CZ . ARG A 443 ? 0.9585 1.2504 1.0935 -0.3524 0.0252 0.0150 457 ARG A CZ 3446 N NH1 . ARG A 443 ? 0.9510 1.2407 1.0872 -0.3531 0.0240 0.0161 457 ARG A NH1 3447 N NH2 . ARG A 443 ? 0.9655 1.2575 1.1019 -0.3513 0.0237 0.0100 457 ARG A NH2 3448 N N . LYS A 444 ? 0.5897 0.8998 0.7040 -0.3522 0.0383 0.0288 458 LYS A N 3449 C CA . LYS A 444 ? 0.5723 0.8843 0.6832 -0.3499 0.0384 0.0236 458 LYS A CA 3450 C C . LYS A 444 ? 0.5951 0.9035 0.7099 -0.3489 0.0354 0.0192 458 LYS A C 3451 O O . LYS A 444 ? 0.5733 0.8806 0.6947 -0.3494 0.0348 0.0168 458 LYS A O 3452 C CB . LYS A 444 ? 0.5639 0.8794 0.6767 -0.3502 0.0408 0.0222 458 LYS A CB 3453 C CG . LYS A 444 ? 0.6243 0.9421 0.7343 -0.3477 0.0409 0.0172 458 LYS A CG 3454 C CD . LYS A 444 ? 0.6646 0.9859 0.7778 -0.3480 0.0432 0.0151 458 LYS A CD 3455 C CE . LYS A 444 ? 0.6861 1.0092 0.7979 -0.3456 0.0430 0.0102 458 LYS A CE 3456 N NZ . LYS A 444 ? 0.6970 1.0239 0.8127 -0.3458 0.0453 0.0077 458 LYS A NZ 3457 N N . GLY A 445 ? 0.5715 0.8785 0.6820 -0.3476 0.0334 0.0181 459 GLY A N 3458 C CA . GLY A 445 ? 0.5119 0.8160 0.6252 -0.3469 0.0304 0.0140 459 GLY A CA 3459 C C . GLY A 445 ? 0.5154 0.8207 0.6302 -0.3455 0.0299 0.0095 459 GLY A C 3460 O O . GLY A 445 ? 0.5447 0.8533 0.6560 -0.3443 0.0315 0.0087 459 GLY A O 3461 N N . SER A 446 ? 0.4911 0.7941 0.6118 -0.3458 0.0276 0.0065 460 SER A N 3462 C CA . SER A 446 ? 0.5527 0.8569 0.6764 -0.3447 0.0268 0.0027 460 SER A CA 3463 C C . SER A 446 ? 0.5905 0.8926 0.7165 -0.3442 0.0232 -0.0011 460 SER A C 3464 O O . SER A 446 ? 0.5994 0.8988 0.7294 -0.3455 0.0218 -0.0013 460 SER A O 3465 C CB . SER A 446 ? 0.5709 0.8758 0.7018 -0.3462 0.0285 0.0033 460 SER A CB 3466 O OG . SER A 446 ? 0.5853 0.8911 0.7205 -0.3454 0.0274 -0.0005 460 SER A OG 3467 N N . TYR A 447 ? 0.4736 0.7773 0.5969 -0.3424 0.0217 -0.0040 461 TYR A N 3468 C CA . TYR A 447 ? 0.5522 0.8550 0.6779 -0.3419 0.0183 -0.0076 461 TYR A CA 3469 C C . TYR A 447 ? 0.5795 0.8845 0.7097 -0.3413 0.0183 -0.0095 461 TYR A C 3470 O O . TYR A 447 ? 0.5697 0.8770 0.6991 -0.3407 0.0207 -0.0085 461 TYR A O 3471 C CB . TYR A 447 ? 0.5126 0.8157 0.6311 -0.3405 0.0161 -0.0091 461 TYR A CB 3472 C CG . TYR A 447 ? 0.5513 0.8523 0.6669 -0.3412 0.0154 -0.0083 461 TYR A CG 3473 C CD1 . TYR A 447 ? 0.5322 0.8309 0.6532 -0.3427 0.0139 -0.0097 461 TYR A CD1 3474 C CD2 . TYR A 447 ? 0.5450 0.8467 0.6528 -0.3405 0.0163 -0.0066 461 TYR A CD2 3475 C CE1 . TYR A 447 ? 0.5683 0.8651 0.6877 -0.3434 0.0133 -0.0094 461 TYR A CE1 3476 C CE2 . TYR A 447 ? 0.5414 0.8413 0.6472 -0.3412 0.0157 -0.0060 461 TYR A CE2 3477 C CZ . TYR A 447 ? 0.5785 0.8761 0.6905 -0.3427 0.0141 -0.0075 461 TYR A CZ 3478 O OH . TYR A 447 ? 0.5835 0.8796 0.6948 -0.3434 0.0135 -0.0074 461 TYR A OH 3479 N N . PRO A 448 ? 0.6267 0.9313 0.7621 -0.3414 0.0155 -0.0123 462 PRO A N 3480 C CA . PRO A 448 ? 0.6462 0.9531 0.7865 -0.3407 0.0149 -0.0141 462 PRO A CA 3481 C C . PRO A 448 ? 0.6226 0.9318 0.7583 -0.3389 0.0150 -0.0144 462 PRO A C 3482 O O . PRO A 448 ? 0.6331 0.9420 0.7615 -0.3380 0.0144 -0.0139 462 PRO A O 3483 C CB . PRO A 448 ? 0.6580 0.9641 0.8018 -0.3410 0.0111 -0.0169 462 PRO A CB 3484 C CG . PRO A 448 ? 0.6719 0.9751 0.8168 -0.3426 0.0111 -0.0166 462 PRO A CG 3485 C CD . PRO A 448 ? 0.6551 0.9574 0.7929 -0.3425 0.0130 -0.0139 462 PRO A CD 3486 N N . PRO A 449 ? 0.6157 0.9275 0.7563 -0.3383 0.0159 -0.0153 463 PRO A N 3487 C CA . PRO A 449 ? 0.5601 0.8740 0.6979 -0.3366 0.0159 -0.0158 463 PRO A CA 3488 C C . PRO A 449 ? 0.5702 0.8838 0.7055 -0.3357 0.0117 -0.0172 463 PRO A C 3489 O O . PRO A 449 ? 0.5560 0.8691 0.6953 -0.3363 0.0088 -0.0186 463 PRO A O 3490 C CB . PRO A 449 ? 0.5585 0.8750 0.7048 -0.3366 0.0169 -0.0172 463 PRO A CB 3491 C CG . PRO A 449 ? 0.5872 0.9030 0.7390 -0.3383 0.0185 -0.0168 463 PRO A CG 3492 C CD . PRO A 449 ? 0.6069 0.9196 0.7566 -0.3393 0.0164 -0.0163 463 PRO A CD 3493 N N . PRO A 450 ? 0.6031 0.9173 0.7320 -0.3344 0.0114 -0.0168 464 PRO A N 3494 C CA . PRO A 450 ? 0.6067 0.9210 0.7322 -0.3336 0.0075 -0.0177 464 PRO A CA 3495 C C . PRO A 450 ? 0.6208 0.9375 0.7518 -0.3327 0.0060 -0.0187 464 PRO A C 3496 O O . PRO A 450 ? 0.5930 0.9112 0.7287 -0.3324 0.0086 -0.0189 464 PRO A O 3497 C CB . PRO A 450 ? 0.6038 0.9177 0.7197 -0.3329 0.0088 -0.0164 464 PRO A CB 3498 C CG . PRO A 450 ? 0.5830 0.8981 0.6994 -0.3327 0.0132 -0.0154 464 PRO A CG 3499 C CD . PRO A 450 ? 0.5939 0.9090 0.7176 -0.3339 0.0150 -0.0154 464 PRO A CD 3500 N N . PRO A 451 ? 0.6386 0.9558 0.7691 -0.3324 0.0018 -0.0193 465 PRO A N 3501 C CA . PRO A 451 ? 0.6601 0.9794 0.7968 -0.3317 -0.0006 -0.0199 465 PRO A CA 3502 C C . PRO A 451 ? 0.6886 1.0095 0.8271 -0.3306 0.0020 -0.0197 465 PRO A C 3503 O O . PRO A 451 ? 0.6670 0.9873 0.7986 -0.3301 0.0046 -0.0189 465 PRO A O 3504 C CB . PRO A 451 ? 0.6530 0.9724 0.7844 -0.3316 -0.0050 -0.0196 465 PRO A CB 3505 C CG . PRO A 451 ? 0.6665 0.9841 0.7930 -0.3326 -0.0057 -0.0200 465 PRO A CG 3506 C CD . PRO A 451 ? 0.6438 0.9597 0.7678 -0.3328 -0.0012 -0.0194 465 PRO A CD 3507 N N . SER A 452 ? 0.6814 1.0043 0.8294 -0.3304 0.0012 -0.0206 466 SER A N 3508 C CA . SER A 452 ? 0.6916 1.0164 0.8430 -0.3294 0.0032 -0.0210 466 SER A CA 3509 C C . SER A 452 ? 0.6849 1.0093 0.8296 -0.3285 0.0017 -0.0199 466 SER A C 3510 O O . SER A 452 ? 0.6761 0.9996 0.8162 -0.3287 -0.0022 -0.0190 466 SER A O 3511 C CB . SER A 452 ? 0.6951 1.0223 0.8589 -0.3292 0.0015 -0.0222 466 SER A CB 3512 O OG . SER A 452 ? 0.6762 1.0039 0.8418 -0.3292 -0.0038 -0.0214 466 SER A OG 3513 N N . SER A 453 ? 0.6933 1.0184 0.8372 -0.3277 0.0048 -0.0202 467 SER A N 3514 C CA . SER A 453 ? 0.6565 0.9815 0.7953 -0.3269 0.0036 -0.0194 467 SER A CA 3515 C C . SER A 453 ? 0.6350 0.9611 0.7808 -0.3268 -0.0010 -0.0191 467 SER A C 3516 O O . SER A 453 ? 0.6230 0.9509 0.7800 -0.3268 -0.0015 -0.0201 467 SER A O 3517 C CB . SER A 453 ? 0.6260 0.9522 0.7648 -0.3262 0.0081 -0.0204 467 SER A CB 3518 O OG . SER A 453 ? 0.5750 0.9017 0.7148 -0.3255 0.0063 -0.0202 467 SER A OG 3519 N N . LYS A 454 ? 0.5993 0.9246 0.7386 -0.3268 -0.0044 -0.0175 468 LYS A N 3520 C CA . LYS A 454 ? 0.5891 0.9155 0.7340 -0.3268 -0.0092 -0.0164 468 LYS A CA 3521 C C . LYS A 454 ? 0.6110 0.9368 0.7493 -0.3264 -0.0097 -0.0152 468 LYS A C 3522 O O . LYS A 454 ? 0.6236 0.9479 0.7507 -0.3263 -0.0083 -0.0148 468 LYS A O 3523 C CB . LYS A 454 ? 0.5681 0.8945 0.7114 -0.3278 -0.0141 -0.0153 468 LYS A CB 3524 C CG . LYS A 454 ? 0.5640 0.8907 0.7122 -0.3284 -0.0135 -0.0167 468 LYS A CG 3525 C CD . LYS A 454 ? 0.5904 0.9168 0.7342 -0.3294 -0.0173 -0.0161 468 LYS A CD 3526 C CE . LYS A 454 ? 0.5885 0.9153 0.7389 -0.3301 -0.0168 -0.0176 468 LYS A CE 3527 N NZ . LYS A 454 ? 0.5817 0.9070 0.7310 -0.3300 -0.0115 -0.0189 468 LYS A NZ 3528 N N . PRO A 455 ? 0.6105 0.9375 0.7562 -0.3261 -0.0118 -0.0145 469 PRO A N 3529 C CA . PRO A 455 ? 0.5673 0.8936 0.7072 -0.3259 -0.0124 -0.0132 469 PRO A CA 3530 C C . PRO A 455 ? 0.5666 0.8920 0.6958 -0.3266 -0.0165 -0.0110 469 PRO A C 3531 O O . PRO A 455 ? 0.5627 0.8884 0.6914 -0.3274 -0.0194 -0.0105 469 PRO A O 3532 C CB . PRO A 455 ? 0.5669 0.8948 0.7192 -0.3258 -0.0150 -0.0127 469 PRO A CB 3533 C CG . PRO A 455 ? 0.5707 0.9004 0.7357 -0.3257 -0.0140 -0.0146 469 PRO A CG 3534 C CD . PRO A 455 ? 0.5538 0.8829 0.7139 -0.3262 -0.0140 -0.0149 469 PRO A CD 3535 N N . PHE A 456 ? 0.5554 0.8799 0.6763 -0.3265 -0.0165 -0.0099 470 PHE A N 3536 C CA . PHE A 456 ? 0.5940 0.9181 0.7049 -0.3273 -0.0203 -0.0080 470 PHE A CA 3537 C C . PHE A 456 ? 0.6388 0.9646 0.7561 -0.3283 -0.0263 -0.0057 470 PHE A C 3538 O O . PHE A 456 ? 0.6450 0.9717 0.7724 -0.3282 -0.0279 -0.0048 470 PHE A O 3539 C CB . PHE A 456 ? 0.5740 0.8972 0.6767 -0.3271 -0.0192 -0.0072 470 PHE A CB 3540 C CG . PHE A 456 ? 0.5877 0.9107 0.6783 -0.3279 -0.0221 -0.0057 470 PHE A CG 3541 C CD1 . PHE A 456 ? 0.5832 0.9072 0.6734 -0.3290 -0.0275 -0.0030 470 PHE A CD1 3542 C CD2 . PHE A 456 ? 0.5699 0.8918 0.6496 -0.3277 -0.0193 -0.0070 470 PHE A CD2 3543 C CE1 . PHE A 456 ? 0.5585 0.8827 0.6372 -0.3299 -0.0299 -0.0019 470 PHE A CE1 3544 C CE2 . PHE A 456 ? 0.5432 0.8652 0.6123 -0.3285 -0.0217 -0.0061 470 PHE A CE2 3545 C CZ . PHE A 456 ? 0.5846 0.9078 0.6528 -0.3296 -0.0269 -0.0038 470 PHE A CZ 3546 N N . PRO A 457 ? 0.6293 0.9556 0.7412 -0.3293 -0.0298 -0.0049 471 PRO A N 3547 C CA . PRO A 457 ? 0.6283 0.9568 0.7446 -0.3305 -0.0359 -0.0025 471 PRO A CA 3548 C C . PRO A 457 ? 0.5787 0.9079 0.6986 -0.3309 -0.0392 0.0005 471 PRO A C 3549 O O . PRO A 457 ? 0.5590 0.8872 0.6708 -0.3309 -0.0387 0.0015 471 PRO A O 3550 C CB . PRO A 457 ? 0.6327 0.9615 0.7372 -0.3316 -0.0380 -0.0024 471 PRO A CB 3551 C CG . PRO A 457 ? 0.6359 0.9630 0.7357 -0.3309 -0.0331 -0.0054 471 PRO A CG 3552 C CD . PRO A 457 ? 0.6134 0.9388 0.7156 -0.3295 -0.0280 -0.0065 471 PRO A CD 3553 N N . THR A 458 ? 0.4411 1.2234 0.6358 -0.1557 -0.0940 -0.0338 472 THR A N 3554 C CA . THR A 458 ? 0.4734 1.2641 0.6698 -0.1423 -0.0976 -0.0342 472 THR A CA 3555 C C . THR A 458 ? 0.5004 1.2808 0.6865 -0.1410 -0.1056 -0.0344 472 THR A C 3556 O O . THR A 458 ? 0.5104 1.2932 0.6955 -0.1305 -0.1098 -0.0336 472 THR A O 3557 C CB . THR A 458 ? 0.5027 1.3210 0.7159 -0.1356 -0.1007 -0.0343 472 THR A CB 3558 O OG1 . THR A 458 ? 0.5583 1.3849 0.7772 -0.1429 -0.1071 -0.0340 472 THR A OG1 3559 C CG2 . THR A 458 ? 0.4969 1.3289 0.7195 -0.1347 -0.0923 -0.0343 472 THR A CG2 3560 N N . ASN A 459 ? 0.4828 1.2525 0.6616 -0.1515 -0.1082 -0.0354 473 ASN A N 3561 C CA . ASN A 459 ? 0.5397 1.2965 0.7045 -0.1523 -0.1139 -0.0361 473 ASN A CA 3562 C C . ASN A 459 ? 0.5298 1.2657 0.6838 -0.1628 -0.1097 -0.0380 473 ASN A C 3563 O O . ASN A 459 ? 0.5809 1.3147 0.7389 -0.1724 -0.1089 -0.0394 473 ASN A O 3564 C CB . ASN A 459 ? 0.6101 1.3783 0.7774 -0.1533 -0.1242 -0.0369 473 ASN A CB 3565 C CG . ASN A 459 ? 0.6755 1.4537 0.8438 -0.1416 -0.1311 -0.0346 473 ASN A CG 3566 O OD1 . ASN A 459 ? 0.7060 1.5021 0.8887 -0.1344 -0.1330 -0.0335 473 ASN A OD1 3567 N ND2 . ASN A 459 ? 0.6985 1.4655 0.8520 -0.1393 -0.1349 -0.0337 473 ASN A ND2 3568 N N . TYR A 460 ? 0.4377 1.1579 0.5793 -0.1607 -0.1073 -0.0378 474 TYR A N 3569 C CA . TYR A 460 ? 0.4030 1.1026 0.5354 -0.1692 -0.1025 -0.0398 474 TYR A CA 3570 C C . TYR A 460 ? 0.3977 1.0859 0.5151 -0.1675 -0.1045 -0.0403 474 TYR A C 3571 O O . TYR A 460 ? 0.4110 1.1025 0.5254 -0.1585 -0.1060 -0.0373 474 TYR A O 3572 C CB . TYR A 460 ? 0.3559 1.0478 0.4920 -0.1689 -0.0933 -0.0380 474 TYR A CB 3573 C CG . TYR A 460 ? 0.3743 1.0447 0.5036 -0.1779 -0.0887 -0.0396 474 TYR A CG 3574 C CD1 . TYR A 460 ? 0.4053 1.0713 0.5392 -0.1880 -0.0885 -0.0410 474 TYR A CD1 3575 C CD2 . TYR A 460 ? 0.3767 1.0310 0.4965 -0.1763 -0.0852 -0.0393 474 TYR A CD2 3576 C CE1 . TYR A 460 ? 0.4260 1.0712 0.5552 -0.1955 -0.0852 -0.0425 474 TYR A CE1 3577 C CE2 . TYR A 460 ? 0.3992 1.0338 0.5142 -0.1841 -0.0812 -0.0410 474 TYR A CE2 3578 C CZ . TYR A 460 ? 0.4335 1.0631 0.5532 -0.1934 -0.0814 -0.0428 474 TYR A CZ 3579 O OH . TYR A 460 ? 0.4728 1.0818 0.5892 -0.2004 -0.0783 -0.0445 474 TYR A OH 3580 N N . LYS A 461 ? 0.3964 1.0716 0.5046 -0.1761 -0.1049 -0.0443 475 LYS A N 3581 C CA . LYS A 461 ? 0.4127 1.0782 0.5057 -0.1757 -0.1060 -0.0455 475 LYS A CA 3582 C C . LYS A 461 ? 0.4291 1.0765 0.5166 -0.1852 -0.1018 -0.0501 475 LYS A C 3583 O O . LYS A 461 ? 0.4478 1.0914 0.5418 -0.1928 -0.1020 -0.0532 475 LYS A O 3584 C CB . LYS A 461 ? 0.4326 1.1082 0.5178 -0.1745 -0.1154 -0.0469 475 LYS A CB 3585 N N . ASP A 462 ? 0.4163 1.0525 0.4932 -0.1845 -0.0985 -0.0502 476 ASP A N 3586 C CA . ASP A 462 ? 0.4466 1.0660 0.5171 -0.1925 -0.0953 -0.0555 476 ASP A CA 3587 C C . ASP A 462 ? 0.4724 1.0907 0.5274 -0.1905 -0.0964 -0.0565 476 ASP A C 3588 O O . ASP A 462 ? 0.4601 1.0801 0.5122 -0.1838 -0.0943 -0.0508 476 ASP A O 3589 C CB . ASP A 462 ? 0.4579 1.0626 0.5353 -0.1942 -0.0871 -0.0534 476 ASP A CB 3590 C CG . ASP A 462 ? 0.5001 1.0866 0.5752 -0.2031 -0.0847 -0.0592 476 ASP A CG 3591 O OD1 . ASP A 462 ? 0.5168 1.1017 0.5827 -0.2068 -0.0882 -0.0655 476 ASP A OD1 3592 O OD2 . ASP A 462 ? 0.5535 1.1272 0.6360 -0.2059 -0.0796 -0.0577 476 ASP A OD2 3593 N N . ASP A 463 ? 0.4791 1.0952 0.5238 -0.1959 -0.1000 -0.0636 477 ASP A N 3594 C CA . ASP A 463 ? 0.4883 1.1046 0.5160 -0.1947 -0.1006 -0.0652 477 ASP A CA 3595 C C . ASP A 463 ? 0.5004 1.1010 0.5244 -0.2003 -0.0940 -0.0702 477 ASP A C 3596 O O . ASP A 463 ? 0.5036 1.1042 0.5134 -0.2004 -0.0932 -0.0724 477 ASP A O 3597 C CB . ASP A 463 ? 0.5241 1.1494 0.5395 -0.1959 -0.1088 -0.0705 477 ASP A CB 3598 C CG . ASP A 463 ? 0.5242 1.1443 0.5448 -0.2037 -0.1125 -0.0793 477 ASP A CG 3599 O OD1 . ASP A 463 ? 0.5009 1.1077 0.5304 -0.2095 -0.1081 -0.0827 477 ASP A OD1 3600 O OD2 . ASP A 463 ? 0.5768 1.2053 0.5924 -0.2042 -0.1207 -0.0826 477 ASP A OD2 3601 N N . PHE A 464 ? 0.5105 1.0981 0.5471 -0.2048 -0.0895 -0.0714 478 PHE A N 3602 C CA . PHE A 464 ? 0.4781 1.0488 0.5147 -0.2100 -0.0837 -0.0759 478 PHE A CA 3603 C C . PHE A 464 ? 0.5103 1.0772 0.5355 -0.2157 -0.0862 -0.0871 478 PHE A C 3604 O O . PHE A 464 ? 0.5134 1.0691 0.5360 -0.2190 -0.0815 -0.0919 478 PHE A O 3605 C CB . PHE A 464 ? 0.4675 1.0354 0.5020 -0.2058 -0.0777 -0.0696 478 PHE A CB 3606 C CG . PHE A 464 ? 0.4482 1.0211 0.4915 -0.1987 -0.0765 -0.0596 478 PHE A CG 3607 C CD1 . PHE A 464 ? 0.4102 0.9761 0.4670 -0.1991 -0.0739 -0.0571 478 PHE A CD1 3608 C CD2 . PHE A 464 ? 0.4527 1.0374 0.4905 -0.1912 -0.0785 -0.0529 478 PHE A CD2 3609 C CE1 . PHE A 464 ? 0.4223 0.9938 0.4863 -0.1920 -0.0728 -0.0496 478 PHE A CE1 3610 C CE2 . PHE A 464 ? 0.4586 1.0473 0.5055 -0.1839 -0.0782 -0.0449 478 PHE A CE2 3611 C CZ . PHE A 464 ? 0.4428 1.0255 0.5026 -0.1841 -0.0751 -0.0441 478 PHE A CZ 3612 N N . ASN A 465 ? 0.5358 1.1119 0.5547 -0.2165 -0.0937 -0.0920 479 ASN A N 3613 C CA . ASN A 465 ? 0.5845 1.1572 0.5916 -0.2211 -0.0971 -0.1041 479 ASN A CA 3614 C C . ASN A 465 ? 0.5896 1.1464 0.6086 -0.2285 -0.0983 -0.1116 479 ASN A C 3615 O O . ASN A 465 ? 0.6284 1.1862 0.6515 -0.2316 -0.1057 -0.1157 479 ASN A O 3616 C CB . ASN A 465 ? 0.5710 1.1581 0.5656 -0.2187 -0.1056 -0.1065 479 ASN A CB 3617 C CG . ASN A 465 ? 0.5548 1.1560 0.5365 -0.2112 -0.1055 -0.0984 479 ASN A CG 3618 O OD1 . ASN A 465 ? 0.4885 1.0887 0.4639 -0.2089 -0.0994 -0.0948 479 ASN A OD1 3619 N ND2 . ASN A 465 ? 0.5780 1.1922 0.5566 -0.2073 -0.1129 -0.0947 479 ASN A ND2 3620 N N . VAL A 466 ? 0.5573 1.0989 0.5829 -0.2313 -0.0918 -0.1127 480 VAL A N 3621 C CA . VAL A 466 ? 0.5787 1.1024 0.6169 -0.2378 -0.0929 -0.1182 480 VAL A CA 3622 C C . VAL A 466 ? 0.6055 1.1175 0.6382 -0.2401 -0.0881 -0.1269 480 VAL A C 3623 O O . VAL A 466 ? 0.6163 1.1262 0.6484 -0.2378 -0.0805 -0.1222 480 VAL A O 3624 C CB . VAL A 466 ? 0.5885 1.1035 0.6444 -0.2380 -0.0892 -0.1077 480 VAL A CB 3625 C CG1 . VAL A 466 ? 0.5589 1.0532 0.6274 -0.2443 -0.0902 -0.1117 480 VAL A CG1 3626 C CG2 . VAL A 466 ? 0.5724 1.1011 0.6343 -0.2357 -0.0934 -0.1002 480 VAL A CG2 3627 N N . GLU A 467 ? 0.6479 1.1527 0.6774 -0.2444 -0.0927 -0.1401 481 GLU A N 3628 C CA . GLU A 467 ? 0.7244 1.2221 0.7459 -0.2457 -0.0883 -0.1511 481 GLU A CA 3629 C C . GLU A 467 ? 0.7488 1.2245 0.7873 -0.2496 -0.0847 -0.1519 481 GLU A C 3630 O O . GLU A 467 ? 0.7740 1.2442 0.8121 -0.2492 -0.0773 -0.1534 481 GLU A O 3631 C CB . GLU A 467 ? 0.7929 1.2931 0.8007 -0.2471 -0.0950 -0.1669 481 GLU A CB 3632 C CG . GLU A 467 ? 0.8097 1.3083 0.8040 -0.2467 -0.0898 -0.1797 481 GLU A CG 3633 C CD . GLU A 467 ? 0.8442 1.3452 0.8226 -0.2467 -0.0965 -0.1962 481 GLU A CD 3634 O OE1 . GLU A 467 ? 0.7987 1.3021 0.7774 -0.2474 -0.1060 -0.1966 481 GLU A OE1 3635 O OE2 . GLU A 467 ? 0.9078 1.4081 0.8731 -0.2456 -0.0922 -0.2091 481 GLU A OE2 3636 N N . TYR A 468 ? 0.7506 1.2139 0.8043 -0.2533 -0.0905 -0.1504 482 TYR A N 3637 C CA . TYR A 468 ? 0.7522 1.1934 0.8231 -0.2565 -0.0887 -0.1485 482 TYR A CA 3638 C C . TYR A 468 ? 0.6420 1.0794 0.7273 -0.2562 -0.0886 -0.1333 482 TYR A C 3639 O O . TYR A 468 ? 0.6095 1.0388 0.7070 -0.2600 -0.0954 -0.1320 482 TYR A O 3640 C CB . TYR A 468 ? 0.8284 1.2554 0.9053 -0.2615 -0.0969 -0.1616 482 TYR A CB 3641 C CG . TYR A 468 ? 0.9121 1.3411 0.9748 -0.2611 -0.0961 -0.1789 482 TYR A CG 3642 C CD1 . TYR A 468 ? 0.9396 1.3616 1.0018 -0.2604 -0.0877 -0.1838 482 TYR A CD1 3643 C CD2 . TYR A 468 ? 0.9408 1.3789 0.9902 -0.2612 -0.1035 -0.1908 482 TYR A CD2 3644 C CE1 . TYR A 468 ? 0.9689 1.3946 1.0175 -0.2596 -0.0859 -0.2009 482 TYR A CE1 3645 C CE2 . TYR A 468 ? 0.9706 1.4111 1.0045 -0.2599 -0.1023 -0.2077 482 TYR A CE2 3646 C CZ . TYR A 468 ? 0.9878 1.4228 1.0211 -0.2590 -0.0931 -0.2132 482 TYR A CZ 3647 O OH . TYR A 468 ? 1.0136 1.4526 1.0307 -0.2571 -0.0909 -0.2312 482 TYR A OH 3648 N N . PRO A 469 ? 0.5608 1.0043 0.6444 -0.2516 -0.0812 -0.1221 483 PRO A N 3649 C CA . PRO A 469 ? 0.5186 0.9610 0.6129 -0.2503 -0.0806 -0.1090 483 PRO A CA 3650 C C . PRO A 469 ? 0.4671 0.8876 0.5774 -0.2537 -0.0811 -0.1054 483 PRO A C 3651 O O . PRO A 469 ? 0.4573 0.8620 0.5709 -0.2545 -0.0782 -0.1088 483 PRO A O 3652 C CB . PRO A 469 ? 0.4892 0.9402 0.5772 -0.2441 -0.0727 -0.1003 483 PRO A CB 3653 C CG . PRO A 469 ? 0.4696 0.9192 0.5486 -0.2434 -0.0682 -0.1071 483 PRO A CG 3654 C CD . PRO A 469 ? 0.5184 0.9710 0.5903 -0.2472 -0.0737 -0.1211 483 PRO A CD 3655 N N . LEU A 470 ? 0.4813 0.9018 0.6021 -0.2557 -0.0852 -0.0986 484 LEU A N 3656 C CA . LEU A 470 ? 0.5067 0.9085 0.6429 -0.2587 -0.0862 -0.0931 484 LEU A CA 3657 C C . LEU A 470 ? 0.4731 0.8682 0.6098 -0.2542 -0.0778 -0.0834 484 LEU A C 3658 O O . LEU A 470 ? 0.5150 0.8907 0.6601 -0.2551 -0.0767 -0.0818 484 LEU A O 3659 C CB . LEU A 470 ? 0.5360 0.9432 0.6829 -0.2625 -0.0926 -0.0883 484 LEU A CB 3660 C CG . LEU A 470 ? 0.5881 0.9979 0.7370 -0.2675 -0.1026 -0.0983 484 LEU A CG 3661 C CD1 . LEU A 470 ? 0.5447 0.9656 0.7030 -0.2709 -0.1087 -0.0931 484 LEU A CD1 3662 C CD2 . LEU A 470 ? 0.6124 0.9999 0.7706 -0.2718 -0.1078 -0.1060 484 LEU A CD2 3663 N N . PHE A 471 ? 0.4072 0.8177 0.5356 -0.2489 -0.0728 -0.0773 485 PHE A N 3664 C CA . PHE A 471 ? 0.3962 0.8011 0.5232 -0.2439 -0.0654 -0.0694 485 PHE A CA 3665 C C . PHE A 471 ? 0.4069 0.8203 0.5218 -0.2389 -0.0604 -0.0713 485 PHE A C 3666 O O . PHE A 471 ? 0.3641 0.7939 0.4702 -0.2383 -0.0622 -0.0763 485 PHE A O 3667 C CB . PHE A 471 ? 0.3937 0.8079 0.5233 -0.2417 -0.0640 -0.0596 485 PHE A CB 3668 C CG . PHE A 471 ? 0.4136 0.8210 0.5555 -0.2469 -0.0681 -0.0560 485 PHE A CG 3669 C CD1 . PHE A 471 ? 0.4115 0.8301 0.5581 -0.2513 -0.0742 -0.0579 485 PHE A CD1 3670 C CD2 . PHE A 471 ? 0.4302 0.8203 0.5797 -0.2476 -0.0662 -0.0504 485 PHE A CD2 3671 C CE1 . PHE A 471 ? 0.4151 0.8285 0.5744 -0.2567 -0.0782 -0.0538 485 PHE A CE1 3672 C CE2 . PHE A 471 ? 0.4199 0.8049 0.5812 -0.2527 -0.0702 -0.0465 485 PHE A CE2 3673 C CZ . PHE A 471 ? 0.3852 0.7823 0.5518 -0.2575 -0.0760 -0.0480 485 PHE A CZ 3674 N N . SER A 472 ? 0.3934 0.7963 0.5085 -0.2354 -0.0546 -0.0667 486 SER A N 3675 C CA . SER A 472 ? 0.4014 0.8095 0.5079 -0.2315 -0.0499 -0.0680 486 SER A CA 3676 C C . SER A 472 ? 0.3876 0.8162 0.4862 -0.2259 -0.0488 -0.0633 486 SER A C 3677 O O . SER A 472 ? 0.4237 0.8607 0.5150 -0.2233 -0.0465 -0.0643 486 SER A O 3678 C CB . SER A 472 ? 0.4328 0.8218 0.5445 -0.2297 -0.0449 -0.0639 486 SER A CB 3679 O OG . SER A 472 ? 0.3255 0.7099 0.4412 -0.2262 -0.0436 -0.0545 486 SER A OG 3680 N N . GLU A 473 ? 0.3856 0.8231 0.4865 -0.2241 -0.0506 -0.0579 487 GLU A N 3681 C CA . GLU A 473 ? 0.3825 0.8400 0.4781 -0.2181 -0.0505 -0.0539 487 GLU A CA 3682 C C . GLU A 473 ? 0.3612 0.8358 0.4573 -0.2191 -0.0555 -0.0549 487 GLU A C 3683 O O . GLU A 473 ? 0.3536 0.8239 0.4565 -0.2239 -0.0581 -0.0553 487 GLU A O 3684 C CB . GLU A 473 ? 0.3823 0.8363 0.4810 -0.2127 -0.0468 -0.0458 487 GLU A CB 3685 C CG . GLU A 473 ? 0.3869 0.8610 0.4823 -0.2057 -0.0475 -0.0422 487 GLU A CG 3686 C CD . GLU A 473 ? 0.4888 0.9594 0.5873 -0.2001 -0.0444 -0.0358 487 GLU A CD 3687 O OE1 . GLU A 473 ? 0.5030 0.9579 0.6060 -0.2020 -0.0420 -0.0334 487 GLU A OE1 3688 O OE2 . GLU A 473 ? 0.4881 0.9723 0.5849 -0.1934 -0.0451 -0.0332 487 GLU A OE2 3689 N N . ALA A 474 ? 0.3682 0.8623 0.4583 -0.2145 -0.0574 -0.0545 488 ALA A N 3690 C CA . ALA A 474 ? 0.3747 0.8863 0.4661 -0.2144 -0.0623 -0.0549 488 ALA A CA 3691 C C . ALA A 474 ? 0.3608 0.8756 0.4612 -0.2133 -0.0610 -0.0490 488 ALA A C 3692 O O . ALA A 474 ? 0.3490 0.8584 0.4512 -0.2096 -0.0566 -0.0440 488 ALA A O 3693 C CB . ALA A 474 ? 0.3417 0.8726 0.4258 -0.2083 -0.0648 -0.0544 488 ALA A CB 3694 N N . PRO A 475 ? 0.3689 0.8933 0.4748 -0.2169 -0.0651 -0.0497 489 PRO A N 3695 C CA . PRO A 475 ? 0.3801 0.9109 0.4946 -0.2171 -0.0639 -0.0443 489 PRO A CA 3696 C C . PRO A 475 ? 0.3792 0.9258 0.4934 -0.2085 -0.0613 -0.0400 489 PRO A C 3697 O O . PRO A 475 ? 0.3612 0.9192 0.4706 -0.2026 -0.0631 -0.0410 489 PRO A O 3698 C CB . PRO A 475 ? 0.3996 0.9427 0.5196 -0.2219 -0.0701 -0.0466 489 PRO A CB 3699 C CG . PRO A 475 ? 0.3678 0.9155 0.4799 -0.2214 -0.0748 -0.0529 489 PRO A CG 3700 C CD . PRO A 475 ? 0.3567 0.8867 0.4614 -0.2215 -0.0715 -0.0558 489 PRO A CD 3701 N N . ASN A 476 ? 0.3858 0.9329 0.5051 -0.2077 -0.0576 -0.0353 490 ASN A N 3702 C CA . ASN A 476 ? 0.3731 0.9376 0.4944 -0.1999 -0.0557 -0.0323 490 ASN A CA 3703 C C . ASN A 476 ? 0.3705 0.9325 0.4869 -0.1915 -0.0534 -0.0314 490 ASN A C 3704 O O . ASN A 476 ? 0.3053 0.8788 0.4246 -0.1848 -0.0517 -0.0292 490 ASN A O 3705 C CB . ASN A 476 ? 0.3976 0.9855 0.5228 -0.1979 -0.0601 -0.0334 490 ASN A CB 3706 C CG . ASN A 476 ? 0.4006 0.9918 0.5326 -0.2065 -0.0629 -0.0336 490 ASN A CG 3707 O OD1 . ASN A 476 ? 0.3606 0.9470 0.4974 -0.2115 -0.0604 -0.0305 490 ASN A OD1 3708 N ND2 . ASN A 476 ? 0.3739 0.9728 0.5064 -0.2086 -0.0689 -0.0371 490 ASN A ND2 3709 N N . PHE A 477 ? 0.3098 0.8581 0.4200 -0.1917 -0.0537 -0.0331 491 PHE A N 3710 C CA . PHE A 477 ? 0.3349 0.8779 0.4421 -0.1850 -0.0516 -0.0311 491 PHE A CA 3711 C C . PHE A 477 ? 0.3216 0.8469 0.4304 -0.1870 -0.0471 -0.0286 491 PHE A C 3712 O O . PHE A 477 ? 0.3447 0.8511 0.4521 -0.1930 -0.0458 -0.0295 491 PHE A O 3713 C CB . PHE A 477 ? 0.3026 0.8390 0.4030 -0.1852 -0.0532 -0.0331 491 PHE A CB 3714 C CG . PHE A 477 ? 0.3666 0.9212 0.4639 -0.1804 -0.0581 -0.0338 491 PHE A CG 3715 C CD1 . PHE A 477 ? 0.3667 0.9309 0.4647 -0.1711 -0.0597 -0.0305 491 PHE A CD1 3716 C CD2 . PHE A 477 ? 0.3847 0.9464 0.4788 -0.1849 -0.0621 -0.0378 491 PHE A CD2 3717 C CE1 . PHE A 477 ? 0.4128 0.9932 0.5083 -0.1662 -0.0653 -0.0302 491 PHE A CE1 3718 C CE2 . PHE A 477 ? 0.4238 1.0022 0.5143 -0.1804 -0.0675 -0.0380 491 PHE A CE2 3719 C CZ . PHE A 477 ? 0.4236 1.0110 0.5146 -0.1709 -0.0691 -0.0337 491 PHE A CZ 3720 N N . ALA A 478 ? 0.2898 0.8218 0.4018 -0.1816 -0.0452 -0.0260 492 ALA A N 3721 C CA . ALA A 478 ? 0.3099 0.8269 0.4226 -0.1825 -0.0416 -0.0234 492 ALA A CA 3722 C C . ALA A 478 ? 0.3030 0.8118 0.4145 -0.1763 -0.0412 -0.0221 492 ALA A C 3723 O O . ALA A 478 ? 0.2731 0.7948 0.3870 -0.1683 -0.0422 -0.0216 492 ALA A O 3724 C CB . ALA A 478 ? 0.3035 0.8349 0.4201 -0.1812 -0.0398 -0.0218 492 ALA A CB 3725 N N . ASP A 479 ? 0.2761 0.7640 0.3852 -0.1797 -0.0401 -0.0217 493 ASP A N 3726 C CA . ASP A 479 ? 0.2693 0.7483 0.3788 -0.1749 -0.0399 -0.0195 493 ASP A CA 3727 C C . ASP A 479 ? 0.3603 0.8359 0.4730 -0.1714 -0.0386 -0.0172 493 ASP A C 3728 O O . ASP A 479 ? 0.3421 0.8098 0.4550 -0.1759 -0.0364 -0.0164 493 ASP A O 3729 C CB . ASP A 479 ? 0.3057 0.7635 0.4134 -0.1801 -0.0383 -0.0196 493 ASP A CB 3730 C CG . ASP A 479 ? 0.3365 0.7986 0.4403 -0.1844 -0.0395 -0.0234 493 ASP A CG 3731 O OD1 . ASP A 479 ? 0.3317 0.8131 0.4337 -0.1824 -0.0424 -0.0250 493 ASP A OD1 3732 O OD2 . ASP A 479 ? 0.3224 0.7691 0.4253 -0.1895 -0.0379 -0.0251 493 ASP A OD2 3733 N N . GLN A 480 ? 0.2588 0.7414 0.3743 -0.1634 -0.0407 -0.0161 494 GLN A N 3734 C CA . GLN A 480 ? 0.2909 0.7726 0.4097 -0.1594 -0.0404 -0.0151 494 GLN A CA 3735 C C . GLN A 480 ? 0.3381 0.8029 0.4596 -0.1572 -0.0416 -0.0122 494 GLN A C 3736 O O . GLN A 480 ? 0.3404 0.7977 0.4640 -0.1564 -0.0415 -0.0113 494 GLN A O 3737 C CB . GLN A 480 ? 0.2672 0.7738 0.3897 -0.1507 -0.0429 -0.0174 494 GLN A CB 3738 C CG . GLN A 480 ? 0.2805 0.8053 0.4021 -0.1530 -0.0413 -0.0196 494 GLN A CG 3739 C CD . GLN A 480 ? 0.2846 0.8027 0.4038 -0.1614 -0.0372 -0.0186 494 GLN A CD 3740 O OE1 . GLN A 480 ? 0.3142 0.8240 0.4332 -0.1622 -0.0357 -0.0173 494 GLN A OE1 3741 N NE2 . GLN A 480 ? 0.2684 0.7901 0.3861 -0.1680 -0.0363 -0.0188 494 GLN A NE2 3742 N N . THR A 481 ? 0.2484 0.7086 0.3699 -0.1568 -0.0431 -0.0105 495 THR A N 3743 C CA . THR A 481 ? 0.3056 0.7470 0.4301 -0.1575 -0.0432 -0.0067 495 THR A CA 3744 C C . THR A 481 ? 0.3262 0.7645 0.4478 -0.1614 -0.0420 -0.0059 495 THR A C 3745 O O . THR A 481 ? 0.2501 0.7052 0.3689 -0.1596 -0.0441 -0.0070 495 THR A O 3746 C CB . THR A 481 ? 0.2399 0.6858 0.3713 -0.1489 -0.0484 -0.0040 495 THR A CB 3747 O OG1 . THR A 481 ? 0.3442 0.7916 0.4777 -0.1461 -0.0492 -0.0060 495 THR A OG1 3748 C CG2 . THR A 481 ? 0.2370 0.6646 0.3726 -0.1507 -0.0487 0.0014 495 THR A CG2 3749 N N . GLY A 482 ? 0.3100 0.7280 0.4320 -0.1669 -0.0387 -0.0044 496 GLY A N 3750 C CA . GLY A 482 ? 0.3125 0.7288 0.4314 -0.1715 -0.0365 -0.0052 496 GLY A CA 3751 C C . GLY A 482 ? 0.2907 0.7074 0.4043 -0.1774 -0.0347 -0.0109 496 GLY A C 3752 O O . GLY A 482 ? 0.2896 0.7068 0.4027 -0.1782 -0.0348 -0.0126 496 GLY A O 3753 N N . VAL A 483 ? 0.2794 0.6965 0.3897 -0.1819 -0.0332 -0.0136 497 VAL A N 3754 C CA . VAL A 483 ? 0.2692 0.6849 0.3760 -0.1880 -0.0326 -0.0195 497 VAL A CA 3755 C C . VAL A 483 ? 0.3242 0.7571 0.4248 -0.1898 -0.0340 -0.0232 497 VAL A C 3756 O O . VAL A 483 ? 0.3380 0.7735 0.4375 -0.1902 -0.0327 -0.0220 497 VAL A O 3757 C CB . VAL A 483 ? 0.2949 0.6870 0.4054 -0.1929 -0.0293 -0.0209 497 VAL A CB 3758 C CG1 . VAL A 483 ? 0.2842 0.6753 0.3927 -0.1992 -0.0297 -0.0276 497 VAL A CG1 3759 C CG2 . VAL A 483 ? 0.2666 0.6418 0.3823 -0.1915 -0.0289 -0.0171 497 VAL A CG2 3760 N N . PHE A 484 ? 0.3294 0.7753 0.4264 -0.1911 -0.0368 -0.0271 498 PHE A N 3761 C CA . PHE A 484 ? 0.3336 0.7974 0.4238 -0.1924 -0.0395 -0.0308 498 PHE A CA 3762 C C . PHE A 484 ? 0.3929 0.8524 0.4809 -0.1998 -0.0398 -0.0384 498 PHE A C 3763 O O . PHE A 484 ? 0.4070 0.8602 0.4987 -0.2022 -0.0405 -0.0395 498 PHE A O 3764 C CB . PHE A 484 ? 0.3083 0.7930 0.3970 -0.1868 -0.0440 -0.0291 498 PHE A CB 3765 C CG . PHE A 484 ? 0.3122 0.8027 0.4045 -0.1785 -0.0454 -0.0225 498 PHE A CG 3766 C CD1 . PHE A 484 ? 0.2731 0.7525 0.3719 -0.1755 -0.0435 -0.0193 498 PHE A CD1 3767 C CD2 . PHE A 484 ? 0.2905 0.7976 0.3797 -0.1735 -0.0496 -0.0194 498 PHE A CD2 3768 C CE1 . PHE A 484 ? 0.3226 0.8071 0.4257 -0.1677 -0.0458 -0.0143 498 PHE A CE1 3769 C CE2 . PHE A 484 ? 0.3341 0.8456 0.4284 -0.1653 -0.0523 -0.0131 498 PHE A CE2 3770 C CZ . PHE A 484 ? 0.3492 0.8493 0.4510 -0.1624 -0.0504 -0.0112 498 PHE A CZ 3771 N N . GLU A 485 ? 0.3430 0.8071 0.4254 -0.2037 -0.0397 -0.0435 499 GLU A N 3772 C CA . GLU A 485 ? 0.3529 0.8110 0.4342 -0.2107 -0.0404 -0.0522 499 GLU A CA 3773 C C . GLU A 485 ? 0.4068 0.8839 0.4781 -0.2128 -0.0443 -0.0587 499 GLU A C 3774 O O . GLU A 485 ? 0.4103 0.9030 0.4749 -0.2096 -0.0451 -0.0562 499 GLU A O 3775 C CB . GLU A 485 ? 0.3311 0.7705 0.4167 -0.2144 -0.0357 -0.0548 499 GLU A CB 3776 C CG . GLU A 485 ? 0.3905 0.8094 0.4851 -0.2121 -0.0326 -0.0483 499 GLU A CG 3777 C CD . GLU A 485 ? 0.4888 0.8882 0.5893 -0.2154 -0.0286 -0.0509 499 GLU A CD 3778 O OE1 . GLU A 485 ? 0.4781 0.8833 0.5758 -0.2183 -0.0262 -0.0563 499 GLU A OE1 3779 O OE2 . GLU A 485 ? 0.4827 0.8623 0.5912 -0.2150 -0.0280 -0.0477 499 GLU A OE2 3780 N N . TYR A 486 ? 0.3876 0.8634 0.4582 -0.2179 -0.0476 -0.0665 500 TYR A N 3781 C CA . TYR A 486 ? 0.4380 0.9283 0.4980 -0.2206 -0.0516 -0.0748 500 TYR A CA 3782 C C . TYR A 486 ? 0.4360 0.9268 0.4903 -0.2225 -0.0477 -0.0790 500 TYR A C 3783 O O . TYR A 486 ? 0.3468 0.8210 0.4085 -0.2250 -0.0427 -0.0801 500 TYR A O 3784 C CB . TYR A 486 ? 0.3617 0.8445 0.4243 -0.2265 -0.0556 -0.0837 500 TYR A CB 3785 C CG . TYR A 486 ? 0.3643 0.8530 0.4312 -0.2260 -0.0608 -0.0810 500 TYR A CG 3786 C CD1 . TYR A 486 ? 0.4328 0.9416 0.4924 -0.2231 -0.0656 -0.0804 500 TYR A CD1 3787 C CD2 . TYR A 486 ? 0.3927 0.8679 0.4715 -0.2288 -0.0614 -0.0787 500 TYR A CD2 3788 C CE1 . TYR A 486 ? 0.4157 0.9313 0.4811 -0.2229 -0.0701 -0.0781 500 TYR A CE1 3789 C CE2 . TYR A 486 ? 0.3654 0.8485 0.4491 -0.2291 -0.0658 -0.0759 500 TYR A CE2 3790 C CZ . TYR A 486 ? 0.4269 0.9305 0.5045 -0.2263 -0.0699 -0.0759 500 TYR A CZ 3791 O OH . TYR A 486 ? 0.4778 0.9909 0.5617 -0.2268 -0.0742 -0.0734 500 TYR A OH 3792 N N . TYR A 487 ? 0.4280 0.9384 0.4691 -0.2212 -0.0500 -0.0807 501 TYR A N 3793 C CA . TYR A 487 ? 0.4540 0.9546 0.4837 -0.2164 -0.0424 -0.0815 501 TYR A CA 3794 C C . TYR A 487 ? 0.3892 0.8998 0.3996 -0.2154 -0.0450 -0.0901 501 TYR A C 3795 O O . TYR A 487 ? 0.3951 0.9224 0.3962 -0.2130 -0.0513 -0.0880 501 TYR A O 3796 C CB . TYR A 487 ? 0.4277 0.9248 0.4554 -0.2070 -0.0370 -0.0675 501 TYR A CB 3797 C CG . TYR A 487 ? 0.4703 0.9581 0.4874 -0.2018 -0.0282 -0.0660 501 TYR A CG 3798 C CD1 . TYR A 487 ? 0.4947 0.9649 0.5200 -0.2038 -0.0207 -0.0689 501 TYR A CD1 3799 C CD2 . TYR A 487 ? 0.4896 0.9873 0.4891 -0.1951 -0.0274 -0.0609 501 TYR A CD2 3800 C CE1 . TYR A 487 ? 0.4890 0.9529 0.5061 -0.1991 -0.0120 -0.0673 501 TYR A CE1 3801 C CE2 . TYR A 487 ? 0.5317 1.0231 0.5216 -0.1908 -0.0186 -0.0585 501 TYR A CE2 3802 C CZ . TYR A 487 ? 0.5412 1.0162 0.5404 -0.1927 -0.0106 -0.0619 501 TYR A CZ 3803 O OH . TYR A 487 ? 0.6030 1.0736 0.5943 -0.1885 -0.0011 -0.0595 501 TYR A OH 3804 N N . MET A 488 ? 0.4386 0.9396 0.4436 -0.2172 -0.0406 -0.1005 502 MET A N 3805 C CA . MET A 488 ? 0.5189 1.0289 0.5034 -0.2156 -0.0424 -0.1096 502 MET A CA 3806 C C . MET A 488 ? 0.5481 1.0552 0.5179 -0.2073 -0.0324 -0.1043 502 MET A C 3807 O O . MET A 488 ? 0.5283 1.0211 0.5050 -0.2059 -0.0234 -0.1033 502 MET A O 3808 C CB . MET A 488 ? 0.5282 1.0319 0.5147 -0.2228 -0.0453 -0.1271 502 MET A CB 3809 C CG . MET A 488 ? 0.5778 1.0882 0.5413 -0.2199 -0.0454 -0.1383 502 MET A CG 3810 S SD . MET A 488 ? 0.7901 1.2947 0.7556 -0.2282 -0.0526 -0.1610 502 MET A SD 3811 C CE . MET A 488 ? 0.8399 1.3203 0.8249 -0.2301 -0.0437 -0.1649 502 MET A CE 3812 N N . ASN A 489 ? 0.6054 1.1269 0.5560 -0.2020 -0.0343 -0.0997 503 ASN A N 3813 C CA . ASN A 489 ? 0.6825 1.2043 0.6176 -0.1948 -0.0253 -0.0933 503 ASN A CA 3814 C C . ASN A 489 ? 0.7609 1.2945 0.6714 -0.1939 -0.0270 -0.1034 503 ASN A C 3815 O O . ASN A 489 ? 0.7224 1.2711 0.6185 -0.1914 -0.0333 -0.0983 503 ASN A O 3816 C CB . ASN A 489 ? 0.6935 1.2208 0.6281 -0.1885 -0.0255 -0.0745 503 ASN A CB 3817 C CG . ASN A 489 ? 0.7481 1.2788 0.6653 -0.1818 -0.0178 -0.0657 503 ASN A CG 3818 O OD1 . ASN A 489 ? 0.7775 1.3042 0.6864 -0.1813 -0.0091 -0.0724 503 ASN A OD1 3819 N ND2 . ASN A 489 ? 0.7517 1.2903 0.6641 -0.1767 -0.0210 -0.0504 503 ASN A ND2 3820 N N . ASN A 490 ? 0.9016 1.4286 0.8076 -0.1955 -0.0217 -0.1179 504 ASN A N 3821 C CA . ASN A 490 ? 1.0500 1.5873 0.9317 -0.1945 -0.0231 -0.1306 504 ASN A CA 3822 C C . ASN A 490 ? 1.1046 1.6550 0.9624 -0.1874 -0.0185 -0.1198 504 ASN A C 3823 O O . ASN A 490 ? 1.1269 1.6912 0.9627 -0.1867 -0.0242 -0.1250 504 ASN A O 3824 C CB . ASN A 490 ? 1.1083 1.6345 0.9909 -0.1957 -0.0163 -0.1478 504 ASN A CB 3825 C CG . ASN A 490 ? 1.1405 1.6572 1.0400 -0.2038 -0.0248 -0.1627 504 ASN A CG 3826 O OD1 . ASN A 490 ? 1.1542 1.6786 1.0525 -0.2086 -0.0371 -0.1677 504 ASN A OD1 3827 N ND2 . ASN A 490 ? 1.1534 1.6533 1.0700 -0.2057 -0.0189 -0.1693 504 ASN A ND2 3828 N N . GLU A 491 ? 1.1198 1.6658 0.9823 -0.1827 -0.0090 -0.1040 505 GLU A N 3829 C CA . GLU A 491 ? 1.1581 1.7154 1.0003 -0.1765 -0.0035 -0.0913 505 GLU A CA 3830 C C . GLU A 491 ? 1.1028 1.6726 0.9382 -0.1745 -0.0136 -0.0767 505 GLU A C 3831 O O . GLU A 491 ? 1.0956 1.6724 0.9200 -0.1697 -0.0104 -0.0613 505 GLU A O 3832 C CB . GLU A 491 ? 1.2259 1.7734 1.0783 -0.1728 0.0096 -0.0791 505 GLU A CB 3833 C CG . GLU A 491 ? 1.2919 1.8261 1.1553 -0.1742 0.0193 -0.0920 505 GLU A CG 3834 C CD . GLU A 491 ? 1.3369 1.8592 1.2183 -0.1717 0.0296 -0.0787 505 GLU A CD 3835 O OE1 . GLU A 491 ? 1.3600 1.8869 1.2382 -0.1679 0.0319 -0.0600 505 GLU A OE1 3836 O OE2 . GLU A 491 ? 1.3444 1.8521 1.2441 -0.1739 0.0344 -0.0864 505 GLU A OE2 3837 N N . ASP A 492 ? 1.0481 1.6210 0.8918 -0.1784 -0.0259 -0.0813 506 ASP A N 3838 C CA . ASP A 492 ? 1.0032 1.5901 0.8401 -0.1767 -0.0371 -0.0714 506 ASP A CA 3839 C C . ASP A 492 ? 0.9726 1.5679 0.8067 -0.1821 -0.0493 -0.0864 506 ASP A C 3840 O O . ASP A 492 ? 0.9704 1.5575 0.8206 -0.1878 -0.0514 -0.0982 506 ASP A O 3841 C CB . ASP A 492 ? 0.9648 1.5465 0.8236 -0.1747 -0.0398 -0.0562 506 ASP A CB 3842 C CG . ASP A 492 ? 0.9438 1.5396 0.7962 -0.1709 -0.0502 -0.0434 506 ASP A CG 3843 O OD1 . ASP A 492 ? 0.9462 1.5555 0.7881 -0.1729 -0.0604 -0.0501 506 ASP A OD1 3844 O OD2 . ASP A 492 ? 0.9236 1.5167 0.7827 -0.1659 -0.0489 -0.0267 506 ASP A OD2 3845 N N . ARG A 493 ? 0.8835 1.4948 0.6975 -0.1808 -0.0579 -0.0852 507 ARG A N 3846 C CA . ARG A 493 ? 0.7972 1.4181 0.6086 -0.1858 -0.0710 -0.0978 507 ARG A CA 3847 C C . ARG A 493 ? 0.7592 1.3878 0.5875 -0.1865 -0.0823 -0.0888 507 ARG A C 3848 O O . ARG A 493 ? 0.7755 1.4061 0.6174 -0.1924 -0.0905 -0.0981 507 ARG A O 3849 C CB . ARG A 493 ? 0.8107 1.4455 0.5908 -0.1844 -0.0754 -0.1035 507 ARG A CB 3850 N N . GLU A 494 ? 0.7553 1.3887 0.5839 -0.1804 -0.0829 -0.0706 508 GLU A N 3851 C CA . GLU A 494 ? 0.8019 1.4441 0.6464 -0.1794 -0.0935 -0.0622 508 GLU A CA 3852 C C . GLU A 494 ? 0.7334 1.3652 0.6073 -0.1811 -0.0906 -0.0605 508 GLU A C 3853 O O . GLU A 494 ? 0.7386 1.3784 0.6286 -0.1826 -0.0990 -0.0600 508 GLU A O 3854 C CB . GLU A 494 ? 0.8875 1.5380 0.7230 -0.1718 -0.0969 -0.0438 508 GLU A CB 3855 C CG . GLU A 494 ? 0.9595 1.6231 0.8074 -0.1699 -0.1102 -0.0376 508 GLU A CG 3856 C CD . GLU A 494 ? 1.0170 1.6883 0.8559 -0.1624 -0.1154 -0.0199 508 GLU A CD 3857 O OE1 . GLU A 494 ? 1.0519 1.7262 0.8665 -0.1607 -0.1130 -0.0151 508 GLU A OE1 3858 O OE2 . GLU A 494 ? 1.0021 1.6758 0.8590 -0.1577 -0.1215 -0.0108 508 GLU A OE2 3859 N N . HIS A 495 ? 0.6523 1.2676 0.5331 -0.1807 -0.0786 -0.0596 509 HIS A N 3860 C CA . HIS A 495 ? 0.5863 1.1905 0.4928 -0.1825 -0.0753 -0.0582 509 HIS A CA 3861 C C . HIS A 495 ? 0.5382 1.1269 0.4502 -0.1880 -0.0667 -0.0698 509 HIS A C 3862 O O . HIS A 495 ? 0.5358 1.1100 0.4569 -0.1863 -0.0573 -0.0648 509 HIS A O 3863 C CB . HIS A 495 ? 0.5805 1.1783 0.4949 -0.1751 -0.0709 -0.0411 509 HIS A CB 3864 C CG . HIS A 495 ? 0.6089 1.2206 0.5213 -0.1691 -0.0803 -0.0296 509 HIS A CG 3865 N ND1 . HIS A 495 ? 0.5788 1.1996 0.5075 -0.1688 -0.0890 -0.0286 509 HIS A ND1 3866 C CD2 . HIS A 495 ? 0.6309 1.2495 0.5273 -0.1634 -0.0829 -0.0186 509 HIS A CD2 3867 C CE1 . HIS A 495 ? 0.5983 1.2304 0.5224 -0.1624 -0.0967 -0.0181 509 HIS A CE1 3868 N NE2 . HIS A 495 ? 0.6510 1.2813 0.5552 -0.1594 -0.0937 -0.0114 509 HIS A NE2 3869 N N . ARG A 496 ? 0.5509 1.1424 0.4581 -0.1945 -0.0709 -0.0854 510 ARG A N 3870 C CA . ARG A 496 ? 0.5585 1.1353 0.4700 -0.1995 -0.0641 -0.0981 510 ARG A CA 3871 C C . ARG A 496 ? 0.5081 1.0751 0.4459 -0.2051 -0.0641 -0.0991 510 ARG A C 3872 O O . ARG A 496 ? 0.4651 1.0159 0.4124 -0.2068 -0.0561 -0.1019 510 ARG A O 3873 C CB . ARG A 496 ? 0.6017 1.1841 0.4996 -0.2044 -0.0702 -0.1151 510 ARG A CB 3874 C CG . ARG A 496 ? 0.6907 1.2579 0.5911 -0.2082 -0.0637 -0.1295 510 ARG A CG 3875 C CD . ARG A 496 ? 0.7800 1.3525 0.6671 -0.2125 -0.0715 -0.1476 510 ARG A CD 3876 N NE . ARG A 496 ? 0.8486 1.4061 0.7385 -0.2153 -0.0660 -0.1627 510 ARG A NE 3877 C CZ . ARG A 496 ? 0.8850 1.4395 0.7776 -0.2220 -0.0740 -0.1800 510 ARG A CZ 3878 N NH1 . ARG A 496 ? 0.8704 1.4345 0.7642 -0.2262 -0.0869 -0.1828 510 ARG A NH1 3879 N NH2 . ARG A 496 ? 0.9114 1.4511 0.8079 -0.2234 -0.0689 -0.1936 510 ARG A NH2 3880 N N . PHE A 497 ? 0.4878 1.0656 0.4375 -0.2079 -0.0732 -0.0964 511 PHE A N 3881 C CA . PHE A 497 ? 0.4653 1.0373 0.4391 -0.2138 -0.0739 -0.0966 511 PHE A CA 3882 C C . PHE A 497 ? 0.4310 1.0089 0.4163 -0.2088 -0.0746 -0.0826 511 PHE A C 3883 O O . PHE A 497 ? 0.4822 1.0709 0.4669 -0.2046 -0.0805 -0.0775 511 PHE A O 3884 C CB . PHE A 497 ? 0.4446 1.0139 0.4249 -0.2187 -0.0803 -0.1054 511 PHE A CB 3885 C CG . PHE A 497 ? 0.5040 1.0667 0.4754 -0.2239 -0.0812 -0.1210 511 PHE A CG 3886 C CD1 . PHE A 497 ? 0.5215 1.0690 0.5011 -0.2289 -0.0757 -0.1283 511 PHE A CD1 3887 C CD2 . PHE A 497 ? 0.5026 1.0733 0.4579 -0.2232 -0.0877 -0.1287 511 PHE A CD2 3888 C CE1 . PHE A 497 ? 0.5315 1.0725 0.5039 -0.2329 -0.0768 -0.1441 511 PHE A CE1 3889 C CE2 . PHE A 497 ? 0.5366 1.1004 0.4832 -0.2270 -0.0887 -0.1444 511 PHE A CE2 3890 C CZ . PHE A 497 ? 0.5431 1.0923 0.4985 -0.2316 -0.0833 -0.1526 511 PHE A CZ 3891 N N . THR A 498 ? 0.3936 0.9575 0.3890 -0.2063 -0.0666 -0.0754 512 THR A N 3892 C CA . THR A 498 ? 0.4955 1.0630 0.5005 -0.2001 -0.0669 -0.0628 512 THR A CA 3893 C C . THR A 498 ? 0.4227 0.9799 0.4476 -0.2039 -0.0636 -0.0615 512 THR A C 3894 O O . THR A 498 ? 0.4085 0.9513 0.4390 -0.2099 -0.0604 -0.0687 512 THR A O 3895 C CB . THR A 498 ? 0.3816 0.9417 0.3770 -0.1908 -0.0609 -0.0519 512 THR A CB 3896 O OG1 . THR A 498 ? 0.3789 0.9197 0.3766 -0.1920 -0.0512 -0.0530 512 THR A OG1 3897 C CG2 . THR A 498 ? 0.4143 0.9843 0.3878 -0.1871 -0.0635 -0.0516 512 THR A CG2 3898 N N . LEU A 499 ? 0.4050 0.9629 0.4385 -0.1975 -0.0632 -0.0515 513 LEU A N 3899 C CA . LEU A 499 ? 0.4086 0.9504 0.4563 -0.1972 -0.0580 -0.0479 513 LEU A CA 3900 C C . LEU A 499 ? 0.4453 0.9793 0.4941 -0.1921 -0.0534 -0.0395 513 LEU A C 3901 O O . LEU A 499 ? 0.4741 1.0126 0.5172 -0.1833 -0.0550 -0.0314 513 LEU A O 3902 C CB . LEU A 499 ? 0.4152 0.9605 0.4707 -0.1919 -0.0606 -0.0438 513 LEU A CB 3903 C CG . LEU A 499 ? 0.3684 0.8975 0.4355 -0.1925 -0.0561 -0.0421 513 LEU A CG 3904 C CD1 . LEU A 499 ? 0.3497 0.8679 0.4192 -0.2001 -0.0553 -0.0490 513 LEU A CD1 3905 C CD2 . LEU A 499 ? 0.3129 0.8506 0.3866 -0.1855 -0.0582 -0.0370 513 LEU A CD2 3906 N N . ARG A 500 ? 0.3198 0.8350 0.3748 -0.1953 -0.0468 -0.0402 514 ARG A N 3907 C CA . ARG A 500 ? 0.3168 0.8157 0.3719 -0.1889 -0.0405 -0.0317 514 ARG A CA 3908 C C . ARG A 500 ? 0.3495 0.8368 0.4198 -0.1895 -0.0387 -0.0279 514 ARG A C 3909 O O . ARG A 500 ? 0.3335 0.8150 0.4120 -0.1970 -0.0381 -0.0333 514 ARG A O 3910 C CB . ARG A 500 ? 0.3262 0.8122 0.3745 -0.1916 -0.0337 -0.0360 514 ARG A CB 3911 C CG . ARG A 500 ? 0.3297 0.8036 0.3745 -0.1848 -0.0272 -0.0269 514 ARG A CG 3912 C CD . ARG A 500 ? 0.3898 0.8545 0.4288 -0.1878 -0.0199 -0.0332 514 ARG A CD 3913 N NE . ARG A 500 ? 0.4444 0.9017 0.4784 -0.1816 -0.0131 -0.0241 514 ARG A NE 3914 C CZ . ARG A 500 ? 0.5194 0.9623 0.5583 -0.1826 -0.0050 -0.0245 514 ARG A CZ 3915 N NH1 . ARG A 500 ? 0.4974 0.9304 0.5463 -0.1892 -0.0031 -0.0340 514 ARG A NH1 3916 N NH2 . ARG A 500 ? 0.5570 0.9958 0.5921 -0.1771 0.0010 -0.0149 514 ARG A NH2 3917 N N . GLN A 501 ? 0.3197 0.8014 0.3928 -0.1812 -0.0382 -0.0183 515 GLN A N 3918 C CA . GLN A 501 ? 0.3052 0.7731 0.3906 -0.1810 -0.0362 -0.0147 515 GLN A CA 3919 C C . GLN A 501 ? 0.2858 0.7336 0.3717 -0.1825 -0.0293 -0.0131 515 GLN A C 3920 O O . GLN A 501 ? 0.2936 0.7374 0.3722 -0.1774 -0.0264 -0.0079 515 GLN A O 3921 C CB . GLN A 501 ? 0.2797 0.7488 0.3682 -0.1710 -0.0396 -0.0062 515 GLN A CB 3922 C CG . GLN A 501 ? 0.2906 0.7511 0.3911 -0.1709 -0.0398 -0.0047 515 GLN A CG 3923 C CD . GLN A 501 ? 0.2828 0.7197 0.3883 -0.1727 -0.0346 -0.0015 515 GLN A CD 3924 O OE1 . GLN A 501 ? 0.2969 0.7251 0.4096 -0.1786 -0.0330 -0.0043 515 GLN A OE1 3925 N NE2 . GLN A 501 ? 0.2703 0.6967 0.3723 -0.1674 -0.0320 0.0052 515 GLN A NE2 3926 N N . VAL A 502 ? 0.2795 0.7157 0.3746 -0.1898 -0.0267 -0.0172 516 VAL A N 3927 C CA . VAL A 502 ? 0.3065 0.7252 0.4037 -0.1925 -0.0202 -0.0181 516 VAL A CA 3928 C C . VAL A 502 ? 0.3409 0.7405 0.4490 -0.1905 -0.0175 -0.0111 516 VAL A C 3929 O O . VAL A 502 ? 0.2761 0.6618 0.3874 -0.1916 -0.0119 -0.0106 516 VAL A O 3930 C CB . VAL A 502 ? 0.3571 0.7746 0.4572 -0.2026 -0.0196 -0.0289 516 VAL A CB 3931 C CG1 . VAL A 502 ? 0.3384 0.7725 0.4267 -0.2043 -0.0223 -0.0366 516 VAL A CG1 3932 C CG2 . VAL A 502 ? 0.2817 0.6845 0.3866 -0.2023 -0.0223 -0.0294 516 VAL A CG2 3933 N N . LEU A 503 ? 0.2955 0.6943 0.4097 -0.1874 -0.0214 -0.0062 517 LEU A N 3934 C CA . LEU A 503 ? 0.3132 0.6928 0.4368 -0.1851 -0.0199 0.0005 517 LEU A CA 3935 C C . LEU A 503 ? 0.3083 0.6814 0.4297 -0.1765 -0.0182 0.0097 517 LEU A C 3936 O O . LEU A 503 ? 0.3141 0.6971 0.4294 -0.1695 -0.0218 0.0139 517 LEU A O 3937 C CB . LEU A 503 ? 0.3150 0.6910 0.4432 -0.1825 -0.0245 0.0021 517 LEU A CB 3938 C CG . LEU A 503 ? 0.3047 0.6743 0.4297 -0.1844 -0.0253 -0.0043 517 LEU A CG 3939 C CD1 . LEU A 503 ? 0.2496 0.6098 0.3784 -0.1807 -0.0278 -0.0014 517 LEU A CD1 3940 C CD2 . LEU A 503 ? 0.2591 0.6123 0.3855 -0.1900 -0.0216 -0.0089 517 LEU A CD2 3941 N N . ASN A 504 ? 0.2637 0.6202 0.3911 -0.1771 -0.0132 0.0135 518 ASN A N 3942 C CA . ASN A 504 ? 0.3308 0.6802 0.4587 -0.1699 -0.0118 0.0240 518 ASN A CA 3943 C C . ASN A 504 ? 0.3177 0.6493 0.4581 -0.1673 -0.0144 0.0309 518 ASN A C 3944 O O . ASN A 504 ? 0.2630 0.5855 0.4074 -0.1625 -0.0137 0.0402 518 ASN A O 3945 C CB . ASN A 504 ? 0.3333 0.6806 0.4581 -0.1711 -0.0037 0.0248 518 ASN A CB 3946 C CG . ASN A 504 ? 0.3853 0.7174 0.5215 -0.1769 0.0016 0.0214 518 ASN A CG 3947 O OD1 . ASN A 504 ? 0.3545 0.6781 0.4998 -0.1814 -0.0012 0.0179 518 ASN A OD1 3948 N ND2 . ASN A 504 ? 0.3593 0.6891 0.4952 -0.1769 0.0093 0.0225 518 ASN A ND2 3949 N N . GLN A 505 ? 0.3080 0.6351 0.4546 -0.1710 -0.0178 0.0266 519 GLN A N 3950 C CA . GLN A 505 ? 0.2692 0.5809 0.4254 -0.1679 -0.0220 0.0322 519 GLN A CA 3951 C C . GLN A 505 ? 0.2610 0.5756 0.4185 -0.1705 -0.0269 0.0269 519 GLN A C 3952 O O . GLN A 505 ? 0.2496 0.5710 0.4038 -0.1764 -0.0257 0.0194 519 GLN A O 3953 C CB . GLN A 505 ? 0.3230 0.6150 0.4905 -0.1706 -0.0182 0.0367 519 GLN A CB 3954 C CG . GLN A 505 ? 0.3667 0.6505 0.5409 -0.1794 -0.0159 0.0305 519 GLN A CG 3955 C CD . GLN A 505 ? 0.4052 0.6663 0.5912 -0.1790 -0.0132 0.0354 519 GLN A CD 3956 O OE1 . GLN A 505 ? 0.4420 0.6883 0.6351 -0.1760 -0.0176 0.0403 519 GLN A OE1 3957 N NE2 . GLN A 505 ? 0.3811 0.6404 0.5700 -0.1819 -0.0061 0.0333 519 GLN A NE2 3958 N N . ARG A 506 ? 0.2775 0.5854 0.4386 -0.1645 -0.0326 0.0306 520 ARG A N 3959 C CA . ARG A 506 ? 0.2805 0.5925 0.4417 -0.1660 -0.0368 0.0260 520 ARG A CA 3960 C C . ARG A 506 ? 0.2341 0.5289 0.3964 -0.1717 -0.0337 0.0223 520 ARG A C 3961 O O . ARG A 506 ? 0.2399 0.5151 0.4091 -0.1728 -0.0316 0.0255 520 ARG A O 3962 C CB . ARG A 506 ? 0.3109 0.6130 0.4755 -0.1572 -0.0432 0.0301 520 ARG A CB 3963 C CG . ARG A 506 ? 0.2985 0.6073 0.4612 -0.1570 -0.0475 0.0248 520 ARG A CG 3964 C CD . ARG A 506 ? 0.2798 0.5786 0.4450 -0.1469 -0.0544 0.0273 520 ARG A CD 3965 N NE . ARG A 506 ? 0.3340 0.6445 0.4950 -0.1449 -0.0577 0.0210 520 ARG A NE 3966 C CZ . ARG A 506 ? 0.2881 0.6199 0.4440 -0.1392 -0.0592 0.0163 520 ARG A CZ 3967 N NH1 . ARG A 506 ? 0.3176 0.6599 0.4714 -0.1352 -0.0585 0.0176 520 ARG A NH1 3968 N NH2 . ARG A 506 ? 0.2537 0.5973 0.4064 -0.1375 -0.0612 0.0104 520 ARG A NH2 3969 N N . PRO A 507 ? 0.2359 0.5349 0.3911 -0.1730 -0.0333 0.0160 521 PRO A N 3970 C CA . PRO A 507 ? 0.2384 0.5177 0.3941 -0.1757 -0.0316 0.0138 521 PRO A CA 3971 C C . PRO A 507 ? 0.2964 0.5603 0.4571 -0.1740 -0.0353 0.0171 521 PRO A C 3972 O O . PRO A 507 ? 0.2730 0.5435 0.4359 -0.1708 -0.0399 0.0199 521 PRO A O 3973 C CB . PRO A 507 ? 0.2410 0.5327 0.3885 -0.1773 -0.0319 0.0088 521 PRO A CB 3974 C CG . PRO A 507 ? 0.2411 0.5568 0.3834 -0.1763 -0.0317 0.0066 521 PRO A CG 3975 C CD . PRO A 507 ? 0.2369 0.5588 0.3840 -0.1721 -0.0344 0.0115 521 PRO A CD 3976 N N . ILE A 508 ? 0.2651 0.5094 0.4284 -0.1758 -0.0343 0.0166 522 ILE A N 3977 C CA . ILE A 508 ? 0.2396 0.4730 0.4039 -0.1751 -0.0381 0.0180 522 ILE A CA 3978 C C . ILE A 508 ? 0.2516 0.5025 0.4067 -0.1762 -0.0396 0.0150 522 ILE A C 3979 O O . ILE A 508 ? 0.2932 0.5446 0.4440 -0.1793 -0.0376 0.0127 522 ILE A O 3980 C CB . ILE A 508 ? 0.2479 0.4581 0.4173 -0.1766 -0.0365 0.0180 522 ILE A CB 3981 C CG1 . ILE A 508 ? 0.2503 0.4450 0.4302 -0.1749 -0.0340 0.0204 522 ILE A CG1 3982 C CG2 . ILE A 508 ? 0.2600 0.4616 0.4279 -0.1766 -0.0408 0.0194 522 ILE A CG2 3983 C CD1 . ILE A 508 ? 0.2760 0.4501 0.4629 -0.1752 -0.0318 0.0189 522 ILE A CD1 3984 N N . THR A 509 ? 0.2389 0.5056 0.3921 -0.1734 -0.0435 0.0151 523 THR A N 3985 C CA . THR A 509 ? 0.2637 0.5542 0.4092 -0.1732 -0.0438 0.0114 523 THR A CA 3986 C C . THR A 509 ? 0.3191 0.6073 0.4601 -0.1760 -0.0450 0.0112 523 THR A C 3987 O O . THR A 509 ? 0.2450 0.5167 0.3887 -0.1766 -0.0478 0.0137 523 THR A O 3988 C CB . THR A 509 ? 0.2832 0.5934 0.4303 -0.1677 -0.0483 0.0105 523 THR A CB 3989 O OG1 . THR A 509 ? 0.2981 0.5971 0.4515 -0.1656 -0.0541 0.0134 523 THR A OG1 3990 C CG2 . THR A 509 ? 0.2821 0.6013 0.4318 -0.1653 -0.0472 0.0112 523 THR A CG2 3991 N N . TRP A 510 ? 0.2824 0.5879 0.4164 -0.1780 -0.0430 0.0086 524 TRP A N 3992 C CA . TRP A 510 ? 0.3059 0.6157 0.4344 -0.1813 -0.0437 0.0091 524 TRP A CA 3993 C C . TRP A 510 ? 0.3621 0.6988 0.4880 -0.1773 -0.0460 0.0055 524 TRP A C 3994 O O . TRP A 510 ? 0.3647 0.7052 0.4889 -0.1770 -0.0494 0.0051 524 TRP A O 3995 C CB . TRP A 510 ? 0.2825 0.5966 0.4064 -0.1864 -0.0400 0.0091 524 TRP A CB 3996 C CG . TRP A 510 ? 0.2672 0.5882 0.3852 -0.1910 -0.0403 0.0110 524 TRP A CG 3997 C CD1 . TRP A 510 ? 0.2674 0.5707 0.3850 -0.1951 -0.0419 0.0150 524 TRP A CD1 3998 C CD2 . TRP A 510 ? 0.2655 0.6148 0.3772 -0.1922 -0.0389 0.0094 524 TRP A CD2 3999 N NE1 . TRP A 510 ? 0.2735 0.5927 0.3839 -0.1997 -0.0418 0.0166 524 TRP A NE1 4000 C CE2 . TRP A 510 ? 0.2724 0.6205 0.3793 -0.1980 -0.0395 0.0131 524 TRP A CE2 4001 C CE3 . TRP A 510 ? 0.2800 0.6563 0.3904 -0.1886 -0.0372 0.0052 524 TRP A CE3 4002 C CZ2 . TRP A 510 ? 0.3456 0.7204 0.4458 -0.2010 -0.0377 0.0129 524 TRP A CZ2 4003 C CZ3 . TRP A 510 ? 0.2679 0.6703 0.3730 -0.1906 -0.0354 0.0044 524 TRP A CZ3 4004 C CH2 . TRP A 510 ? 0.2748 0.6769 0.3747 -0.1970 -0.0353 0.0083 524 TRP A CH2 4005 N N . ALA A 511 ? 0.3596 0.7160 0.4855 -0.1735 -0.0445 0.0023 525 ALA A N 4006 C CA . ALA A 511 ? 0.3496 0.7334 0.4751 -0.1673 -0.0467 -0.0024 525 ALA A CA 4007 C C . ALA A 511 ? 0.2911 0.6747 0.4240 -0.1598 -0.0516 -0.0032 525 ALA A C 4008 O O . ALA A 511 ? 0.3146 0.6773 0.4523 -0.1610 -0.0527 0.0007 525 ALA A O 4009 C CB . ALA A 511 ? 0.3975 0.8036 0.5195 -0.1671 -0.0427 -0.0050 525 ALA A CB 4010 N N . ALA A 512 ? 0.2738 0.6813 0.4085 -0.1516 -0.0549 -0.0081 526 ALA A N 4011 C CA . ALA A 512 ? 0.3058 0.7071 0.4453 -0.1409 -0.0599 -0.0080 526 ALA A CA 4012 C C . ALA A 512 ? 0.3062 0.7205 0.4476 -0.1395 -0.0582 -0.0077 526 ALA A C 4013 O O . ALA A 512 ? 0.3102 0.7438 0.4513 -0.1309 -0.0596 -0.0118 526 ALA A O 4014 C CB . ALA A 512 ? 0.3071 0.7138 0.4440 -0.1269 -0.0646 -0.0137 526 ALA A CB 4015 N N . ASP A 513 ? 0.3101 0.7130 0.4531 -0.1473 -0.0552 -0.0032 527 ASP A N 4016 C CA . ASP A 513 ? 0.3256 0.7378 0.4680 -0.1461 -0.0536 -0.0027 527 ASP A CA 4017 C C . ASP A 513 ? 0.3095 0.7217 0.4539 -0.1327 -0.0589 -0.0017 527 ASP A C 4018 O O . ASP A 513 ? 0.2754 0.6689 0.4219 -0.1255 -0.0629 0.0005 527 ASP A O 4019 C CB . ASP A 513 ? 0.2742 0.6664 0.4158 -0.1533 -0.0494 0.0015 527 ASP A CB 4020 C CG . ASP A 513 ? 0.3184 0.6965 0.4546 -0.1612 -0.0441 0.0009 527 ASP A CG 4021 O OD1 . ASP A 513 ? 0.3489 0.7205 0.4842 -0.1629 -0.0445 0.0007 527 ASP A OD1 4022 O OD2 . ASP A 513 ? 0.3229 0.6966 0.4560 -0.1656 -0.0404 0.0006 527 ASP A OD2 4023 N N . ALA A 514 ? 0.3266 0.7575 0.4701 -0.1287 -0.0595 -0.0031 528 ALA A N 4024 C CA . ALA A 514 ? 0.3300 0.7584 0.4749 -0.1161 -0.0648 -0.0008 528 ALA A CA 4025 C C . ALA A 514 ? 0.3038 0.7093 0.4495 -0.1171 -0.0647 0.0071 528 ALA A C 4026 O O . ALA A 514 ? 0.2414 0.6372 0.3862 -0.1274 -0.0597 0.0094 528 ALA A O 4027 C CB . ALA A 514 ? 0.2441 0.6979 0.3879 -0.1134 -0.0656 -0.0032 528 ALA A CB 4028 N N . SER A 515 ? 0.3209 0.7186 0.4690 -0.1065 -0.0702 0.0115 529 SER A N 4029 C CA . SER A 515 ? 0.3612 0.7401 0.5105 -0.1069 -0.0701 0.0206 529 SER A CA 4030 C C . SER A 515 ? 0.3288 0.7202 0.4728 -0.1103 -0.0672 0.0232 529 SER A C 4031 O O . SER A 515 ? 0.3286 0.7089 0.4714 -0.1134 -0.0644 0.0301 529 SER A O 4032 C CB . SER A 515 ? 0.4059 0.7712 0.5610 -0.0948 -0.0783 0.0255 529 SER A CB 4033 O OG . SER A 515 ? 0.5219 0.8708 0.6814 -0.0928 -0.0811 0.0236 529 SER A OG 4034 N N . SER A 516 ? 0.2729 0.6881 0.4137 -0.1093 -0.0679 0.0176 530 SER A N 4035 C CA . SER A 516 ? 0.3073 0.7374 0.4420 -0.1126 -0.0663 0.0184 530 SER A CA 4036 C C . SER A 516 ? 0.3037 0.7490 0.4352 -0.1237 -0.0610 0.0112 530 SER A C 4037 O O . SER A 516 ? 0.2917 0.7446 0.4262 -0.1259 -0.0604 0.0055 530 SER A O 4038 C CB . SER A 516 ? 0.3108 0.7569 0.4463 -0.1021 -0.0733 0.0185 530 SER A CB 4039 O OG . SER A 516 ? 0.3314 0.7627 0.4713 -0.0919 -0.0796 0.0257 530 SER A OG 4040 N N . THR A 517 ? 0.2913 0.7414 0.4167 -0.1308 -0.0575 0.0115 531 THR A N 4041 C CA . THR A 517 ? 0.2671 0.7311 0.3907 -0.1415 -0.0541 0.0045 531 THR A CA 4042 C C . THR A 517 ? 0.2771 0.7678 0.4003 -0.1387 -0.0581 0.0003 531 THR A C 4043 O O . THR A 517 ? 0.2737 0.7717 0.3958 -0.1295 -0.0631 0.0031 531 THR A O 4044 C CB . THR A 517 ? 0.2540 0.7117 0.3717 -0.1503 -0.0492 0.0045 531 THR A CB 4045 O OG1 . THR A 517 ? 0.2976 0.7647 0.4076 -0.1467 -0.0512 0.0067 531 THR A OG1 4046 C CG2 . THR A 517 ? 0.2535 0.6856 0.3733 -0.1515 -0.0452 0.0096 531 THR A CG2 4047 N N . ILE A 518 ? 0.3023 0.7980 0.4236 -0.1439 -0.0548 -0.0055 532 ILE A N 4048 C CA . ILE A 518 ? 0.2771 0.7923 0.3974 -0.1400 -0.0570 -0.0092 532 ILE A CA 4049 C C . ILE A 518 ? 0.2897 0.8041 0.4058 -0.1479 -0.0522 -0.0137 532 ILE A C 4050 O O . ILE A 518 ? 0.3309 0.8314 0.4470 -0.1530 -0.0480 -0.0144 532 ILE A O 4051 C CB . ILE A 518 ? 0.3520 0.8773 0.4797 -0.1297 -0.0607 -0.0101 532 ILE A CB 4052 C CG1 . ILE A 518 ? 0.3053 0.8523 0.4339 -0.1250 -0.0626 -0.0138 532 ILE A CG1 4053 C CG2 . ILE A 518 ? 0.3205 0.8348 0.4505 -0.1319 -0.0569 -0.0117 532 ILE A CG2 4054 C CD1 . ILE A 518 ? 0.2949 0.8547 0.4317 -0.1121 -0.0682 -0.0148 532 ILE A CD1 4055 N N . SER A 519 ? 0.3215 0.8503 0.4345 -0.1487 -0.0539 -0.0161 533 SER A N 4056 C CA . SER A 519 ? 0.3670 0.8982 0.4781 -0.1554 -0.0510 -0.0197 533 SER A CA 4057 C C . SER A 519 ? 0.3773 0.9314 0.4920 -0.1496 -0.0540 -0.0213 533 SER A C 4058 O O . SER A 519 ? 0.3747 0.9414 0.4898 -0.1434 -0.0589 -0.0205 533 SER A O 4059 C CB . SER A 519 ? 0.4046 0.9305 0.5092 -0.1634 -0.0507 -0.0216 533 SER A CB 4060 O OG . SER A 519 ? 0.3899 0.9113 0.4941 -0.1709 -0.0483 -0.0245 533 SER A OG 4061 N N . VAL A 520 ? 0.3558 0.9159 0.4736 -0.1513 -0.0513 -0.0230 534 VAL A N 4062 C CA . VAL A 520 ? 0.3592 0.9426 0.4821 -0.1460 -0.0533 -0.0247 534 VAL A CA 4063 C C . VAL A 520 ? 0.3333 0.9232 0.4554 -0.1539 -0.0527 -0.0263 534 VAL A C 4064 O O . VAL A 520 ? 0.2864 0.8623 0.4052 -0.1633 -0.0499 -0.0262 534 VAL A O 4065 C CB . VAL A 520 ? 0.3307 0.9230 0.4595 -0.1404 -0.0511 -0.0256 534 VAL A CB 4066 C CG1 . VAL A 520 ? 0.2847 0.8705 0.4158 -0.1319 -0.0533 -0.0246 534 VAL A CG1 4067 C CG2 . VAL A 520 ? 0.2738 0.8580 0.4007 -0.1493 -0.0456 -0.0251 534 VAL A CG2 4068 N N . ILE A 521 ? 0.3468 0.9576 0.4733 -0.1498 -0.0559 -0.0275 535 ILE A N 4069 C CA . ILE A 521 ? 0.3577 0.9766 0.4850 -0.1568 -0.0569 -0.0288 535 ILE A CA 4070 C C . ILE A 521 ? 0.3519 0.9967 0.4877 -0.1509 -0.0592 -0.0297 535 ILE A C 4071 O O . ILE A 521 ? 0.3418 0.9977 0.4813 -0.1404 -0.0623 -0.0300 535 ILE A O 4072 C CB . ILE A 521 ? 0.3808 0.9930 0.5015 -0.1612 -0.0609 -0.0298 535 ILE A CB 4073 C CG1 . ILE A 521 ? 0.3816 0.9993 0.5037 -0.1695 -0.0626 -0.0317 535 ILE A CG1 4074 C CG2 . ILE A 521 ? 0.3696 0.9926 0.4895 -0.1523 -0.0666 -0.0292 535 ILE A CG2 4075 C CD1 . ILE A 521 ? 0.3818 0.9924 0.4965 -0.1745 -0.0666 -0.0342 535 ILE A CD1 4076 N N . GLY A 522 ? 0.3905 1.0447 0.5305 -0.1574 -0.0580 -0.0300 536 GLY A N 4077 C CA . GLY A 522 ? 0.3918 1.0711 0.5407 -0.1531 -0.0606 -0.0308 536 GLY A CA 4078 C C . GLY A 522 ? 0.4155 1.1110 0.5719 -0.1517 -0.0560 -0.0306 536 GLY A C 4079 O O . GLY A 522 ? 0.4086 1.0985 0.5639 -0.1600 -0.0515 -0.0288 536 GLY A O 4080 N N . ASP A 523 ? 0.4169 1.1333 0.5811 -0.1410 -0.0574 -0.0324 537 ASP A N 4081 C CA . ASP A 523 ? 0.3746 1.1121 0.5467 -0.1381 -0.0531 -0.0332 537 ASP A CA 4082 C C . ASP A 523 ? 0.3459 1.0903 0.5209 -0.1248 -0.0524 -0.0363 537 ASP A C 4083 O O . ASP A 523 ? 0.3623 1.1142 0.5423 -0.1141 -0.0577 -0.0383 537 ASP A O 4084 C CB . ASP A 523 ? 0.4018 1.1636 0.5845 -0.1377 -0.0561 -0.0337 537 ASP A CB 4085 C CG . ASP A 523 ? 0.4405 1.2240 0.6307 -0.1394 -0.0506 -0.0333 537 ASP A CG 4086 O OD1 . ASP A 523 ? 0.4424 1.2322 0.6325 -0.1337 -0.0458 -0.0351 537 ASP A OD1 4087 O OD2 . ASP A 523 ? 0.4371 1.2320 0.6335 -0.1466 -0.0515 -0.0313 537 ASP A OD2 4088 N N . HIS A 524 ? 0.3219 1.0634 0.4940 -0.1255 -0.0467 -0.0366 538 HIS A N 4089 C CA . HIS A 524 ? 0.3205 1.0680 0.4953 -0.1134 -0.0460 -0.0404 538 HIS A CA 4090 C C . HIS A 524 ? 0.3565 1.1335 0.5434 -0.1011 -0.0474 -0.0451 538 HIS A C 4091 O O . HIS A 524 ? 0.3538 1.1358 0.5452 -0.0881 -0.0496 -0.0494 538 HIS A O 4092 C CB . HIS A 524 ? 0.3503 1.0926 0.5194 -0.1184 -0.0394 -0.0399 538 HIS A CB 4093 C CG . HIS A 524 ? 0.3885 1.1335 0.5589 -0.1071 -0.0390 -0.0444 538 HIS A CG 4094 N ND1 . HIS A 524 ? 0.3993 1.1706 0.5765 -0.0980 -0.0365 -0.0497 538 HIS A ND1 4095 C CD2 . HIS A 524 ? 0.4073 1.1325 0.5737 -0.1034 -0.0412 -0.0448 538 HIS A CD2 4096 C CE1 . HIS A 524 ? 0.4140 1.1812 0.5912 -0.0886 -0.0377 -0.0540 538 HIS A CE1 4097 N NE2 . HIS A 524 ? 0.4316 1.1705 0.6026 -0.0919 -0.0408 -0.0506 538 HIS A NE2 4098 N N . HIS A 525 ? 0.3630 1.1589 0.5563 -0.1049 -0.0469 -0.0443 539 HIS A N 4099 C CA . HIS A 525 ? 0.4353 1.2599 0.6417 -0.0937 -0.0484 -0.0485 539 HIS A CA 4100 C C . HIS A 525 ? 0.4429 1.2675 0.6555 -0.0847 -0.0573 -0.0494 539 HIS A C 4101 O O . HIS A 525 ? 0.4718 1.3167 0.6962 -0.0726 -0.0600 -0.0534 539 HIS A O 4102 C CB . HIS A 525 ? 0.4802 1.3263 0.6928 -0.1015 -0.0448 -0.0466 539 HIS A CB 4103 C CG . HIS A 525 ? 0.5198 1.3723 0.7282 -0.1088 -0.0365 -0.0454 539 HIS A CG 4104 N ND1 . HIS A 525 ? 0.5434 1.3789 0.7428 -0.1239 -0.0338 -0.0395 539 HIS A ND1 4105 C CD2 . HIS A 525 ? 0.5409 1.4153 0.7527 -0.1030 -0.0308 -0.0491 539 HIS A CD2 4106 C CE1 . HIS A 525 ? 0.5694 1.4156 0.7665 -0.1276 -0.0272 -0.0387 539 HIS A CE1 4107 N NE2 . HIS A 525 ? 0.5488 1.4195 0.7527 -0.1152 -0.0249 -0.0446 539 HIS A NE2 4108 N N . TRP A 526 ? 0.3922 1.1952 0.5972 -0.0904 -0.0620 -0.0455 540 TRP A N 4109 C CA . TRP A 526 ? 0.3809 1.1831 0.5898 -0.0831 -0.0711 -0.0450 540 TRP A CA 4110 C C . TRP A 526 ? 0.4255 1.2304 0.6408 -0.0666 -0.0753 -0.0486 540 TRP A C 4111 O O . TRP A 526 ? 0.4237 1.2171 0.6345 -0.0632 -0.0729 -0.0500 540 TRP A O 4112 C CB . TRP A 526 ? 0.3860 1.1631 0.5827 -0.0912 -0.0745 -0.0407 540 TRP A CB 4113 C CG . TRP A 526 ? 0.3771 1.1527 0.5702 -0.1046 -0.0741 -0.0382 540 TRP A CG 4114 C CD1 . TRP A 526 ? 0.4153 1.2100 0.6167 -0.1089 -0.0736 -0.0384 540 TRP A CD1 4115 C CD2 . TRP A 526 ? 0.3847 1.1386 0.5659 -0.1152 -0.0748 -0.0356 540 TRP A CD2 4116 N NE1 . TRP A 526 ? 0.4229 1.2079 0.6184 -0.1216 -0.0747 -0.0361 540 TRP A NE1 4117 C CE2 . TRP A 526 ? 0.3941 1.1543 0.5770 -0.1253 -0.0753 -0.0348 540 TRP A CE2 4118 C CE3 . TRP A 526 ? 0.3785 1.1090 0.5484 -0.1169 -0.0753 -0.0340 540 TRP A CE3 4119 C CZ2 . TRP A 526 ? 0.3891 1.1324 0.5627 -0.1363 -0.0766 -0.0336 540 TRP A CZ2 4120 C CZ3 . TRP A 526 ? 0.3695 1.0847 0.5300 -0.1279 -0.0757 -0.0326 540 TRP A CZ3 4121 C CH2 . TRP A 526 ? 0.3803 1.1017 0.5425 -0.1372 -0.0765 -0.0329 540 TRP A CH2 4122 N N . THR A 527 ? 0.4703 1.2899 0.6968 -0.0560 -0.0822 -0.0501 541 THR A N 4123 C CA . THR A 527 ? 0.4866 1.3082 0.7212 -0.0392 -0.0878 -0.0536 541 THR A CA 4124 C C . THR A 527 ? 0.4958 1.3109 0.7331 -0.0329 -0.0994 -0.0499 541 THR A C 4125 O O . THR A 527 ? 0.5189 1.3214 0.7565 -0.0232 -0.1057 -0.0491 541 THR A O 4126 C CB . THR A 527 ? 0.4656 1.3146 0.7145 -0.0284 -0.0848 -0.0608 541 THR A CB 4127 O OG1 . THR A 527 ? 0.4706 1.3199 0.7288 -0.0108 -0.0921 -0.0649 541 THR A OG1 4128 C CG2 . THR A 527 ? 0.4887 1.3608 0.7476 -0.0311 -0.0852 -0.0605 541 THR A CG2 4129 N N . ASN A 528 ? 0.5058 1.3291 0.7448 -0.0386 -0.1028 -0.0471 542 ASN A N 4130 C CA . ASN A 528 ? 0.5682 1.3839 0.8061 -0.0356 -0.1136 -0.0423 542 ASN A CA 4131 C C . ASN A 528 ? 0.5007 1.3015 0.7233 -0.0504 -0.1130 -0.0373 542 ASN A C 4132 O O . ASN A 528 ? 0.4976 1.3049 0.7183 -0.0616 -0.1085 -0.0376 542 ASN A O 4133 C CB . ASN A 528 ? 0.6982 1.5355 0.9508 -0.0290 -0.1202 -0.0433 542 ASN A CB 4134 C CG . ASN A 528 ? 0.8128 1.6657 1.0820 -0.0128 -0.1217 -0.0490 542 ASN A CG 4135 O OD1 . ASN A 528 ? 0.7869 1.6297 1.0568 -0.0027 -0.1236 -0.0508 542 ASN A OD1 4136 N ND2 . ASN A 528 ? 0.9610 1.8388 1.2444 -0.0100 -0.1212 -0.0523 542 ASN A ND2 4137 N N . MET A 529 ? 0.4423 1.2235 0.6544 -0.0504 -0.1179 -0.0327 543 MET A N 4138 C CA . MET A 529 ? 0.4193 1.1862 0.6158 -0.0639 -0.1163 -0.0292 543 MET A CA 4139 C C . MET A 529 ? 0.4322 1.1853 0.6191 -0.0619 -0.1245 -0.0233 543 MET A C 4140 O O . MET A 529 ? 0.4435 1.1902 0.6331 -0.0514 -0.1298 -0.0206 543 MET A O 4141 C CB . MET A 529 ? 0.4111 1.1644 0.5992 -0.0726 -0.1062 -0.0305 543 MET A CB 4142 C CG . MET A 529 ? 0.4304 1.1682 0.6157 -0.0660 -0.1059 -0.0294 543 MET A CG 4143 S SD . MET A 529 ? 0.5174 1.2482 0.7002 -0.0726 -0.0941 -0.0330 543 MET A SD 4144 C CE . MET A 529 ? 0.5965 1.3147 0.7658 -0.0907 -0.0893 -0.0308 543 MET A CE 4145 N N . THR A 530 ? 0.4498 1.1986 0.6254 -0.0721 -0.1259 -0.0211 544 THR A N 4146 C CA . THR A 530 ? 0.4542 1.1901 0.6166 -0.0731 -0.1317 -0.0153 544 THR A CA 4147 C C . THR A 530 ? 0.4455 1.1663 0.5930 -0.0861 -0.1245 -0.0157 544 THR A C 4148 O O . THR A 530 ? 0.4623 1.1852 0.6066 -0.0965 -0.1204 -0.0192 544 THR A O 4149 C CB . THR A 530 ? 0.4524 1.1978 0.6133 -0.0725 -0.1415 -0.0126 544 THR A CB 4150 O OG1 . THR A 530 ? 0.4643 1.2236 0.6411 -0.0602 -0.1485 -0.0125 544 THR A OG1 4151 C CG2 . THR A 530 ? 0.4992 1.2324 0.6448 -0.0729 -0.1474 -0.0057 544 THR A CG2 4152 N N . VAL A 531 ? 0.4057 1.1109 0.5454 -0.0853 -0.1232 -0.0121 545 VAL A N 4153 C CA . VAL A 531 ? 0.4027 1.0933 0.5294 -0.0966 -0.1166 -0.0126 545 VAL A CA 4154 C C . VAL A 531 ? 0.4164 1.1001 0.5291 -0.0980 -0.1217 -0.0068 545 VAL A C 4155 O O . VAL A 531 ? 0.4232 1.1052 0.5363 -0.0892 -0.1281 -0.0003 545 VAL A O 4156 C CB . VAL A 531 ? 0.3731 1.0515 0.5026 -0.0963 -0.1092 -0.0134 545 VAL A CB 4157 C CG1 . VAL A 531 ? 0.3539 1.0162 0.4712 -0.1073 -0.1033 -0.0133 545 VAL A CG1 4158 C CG2 . VAL A 531 ? 0.3575 1.0442 0.4983 -0.0962 -0.1033 -0.0190 545 VAL A CG2 4159 N N . GLN A 532 ? 0.4069 1.0869 0.5071 -0.1088 -0.1194 -0.0089 546 GLN A N 4160 C CA . GLN A 532 ? 0.4285 1.1036 0.5129 -0.1112 -0.1232 -0.0041 546 GLN A CA 4161 C C . GLN A 532 ? 0.4334 1.0961 0.5066 -0.1222 -0.1156 -0.0074 546 GLN A C 4162 O O . GLN A 532 ? 0.4098 1.0697 0.4852 -0.1302 -0.1098 -0.0143 546 GLN A O 4163 C CB . GLN A 532 ? 0.4351 1.1215 0.5131 -0.1117 -0.1312 -0.0039 546 GLN A CB 4164 C CG . GLN A 532 ? 0.4799 1.1635 0.5396 -0.1130 -0.1357 0.0019 546 GLN A CG 4165 C CD . GLN A 532 ? 0.5715 1.2661 0.6249 -0.1123 -0.1448 0.0027 546 GLN A CD 4166 O OE1 . GLN A 532 ? 0.6173 1.3196 0.6780 -0.1033 -0.1530 0.0079 546 GLN A OE1 4167 N NE2 . GLN A 532 ? 0.5888 1.2836 0.6291 -0.1215 -0.1440 -0.0027 546 GLN A NE2 4168 N N . CYS A 533 ? 0.4386 1.0944 0.5005 -0.1226 -0.1162 -0.0019 547 CYS A N 4169 C CA . CYS A 533 ? 0.4032 1.0484 0.4549 -0.1324 -0.1094 -0.0049 547 CYS A CA 4170 C C . CYS A 533 ? 0.3858 1.0299 0.4224 -0.1322 -0.1121 0.0023 547 CYS A C 4171 O O . CYS A 533 ? 0.3836 1.0290 0.4213 -0.1240 -0.1173 0.0120 547 CYS A O 4172 C CB . CYS A 533 ? 0.3860 1.0190 0.4479 -0.1337 -0.1015 -0.0064 547 CYS A CB 4173 S SG . CYS A 533 ? 0.4220 1.0410 0.4774 -0.1468 -0.0924 -0.0133 547 CYS A SG 4174 N N . ASP A 534 ? 0.4203 1.0620 0.4425 -0.1410 -0.1089 -0.0023 548 ASP A N 4175 C CA . ASP A 534 ? 0.4653 1.0995 0.4715 -0.1408 -0.1070 0.0044 548 ASP A CA 4176 C C . ASP A 534 ? 0.4653 1.0778 0.4771 -0.1411 -0.0966 0.0062 548 ASP A C 4177 O O . ASP A 534 ? 0.5079 1.1148 0.5264 -0.1481 -0.0908 -0.0022 548 ASP A O 4178 C CB . ASP A 534 ? 0.4632 1.1008 0.4505 -0.1485 -0.1062 -0.0027 548 ASP A CB 4179 C CG . ASP A 534 ? 0.5543 1.2084 0.5349 -0.1475 -0.1160 -0.0041 548 ASP A CG 4180 O OD1 . ASP A 534 ? 0.5585 1.2187 0.5464 -0.1392 -0.1228 0.0033 548 ASP A OD1 4181 O OD2 . ASP A 534 ? 0.5824 1.2381 0.5513 -0.1538 -0.1159 -0.0128 548 ASP A OD2 4182 N N . VAL A 535 ? 0.4454 1.0455 0.4557 -0.1340 -0.0950 0.0177 549 VAL A N 4183 C CA . VAL A 535 ? 0.4272 1.0063 0.4441 -0.1338 -0.0861 0.0204 549 VAL A CA 4184 C C . VAL A 535 ? 0.4122 0.9789 0.4149 -0.1341 -0.0799 0.0278 549 VAL A C 4185 O O . VAL A 535 ? 0.4694 1.0432 0.4584 -0.1317 -0.0837 0.0344 549 VAL A O 4186 C CB . VAL A 535 ? 0.3560 0.9296 0.3897 -0.1250 -0.0894 0.0270 549 VAL A CB 4187 C CG1 . VAL A 535 ? 0.3453 0.9342 0.3925 -0.1245 -0.0944 0.0192 549 VAL A CG1 4188 C CG2 . VAL A 535 ? 0.3673 0.9415 0.3982 -0.1157 -0.0967 0.0399 549 VAL A CG2 4189 N N . TYR A 536 ? 0.4171 0.9663 0.4234 -0.1372 -0.0704 0.0270 550 TYR A N 4190 C CA . TYR A 536 ? 0.4059 0.9444 0.4006 -0.1385 -0.0625 0.0326 550 TYR A CA 4191 C C . TYR A 536 ? 0.4091 0.9269 0.4163 -0.1375 -0.0554 0.0374 550 TYR A C 4192 O O . TYR A 536 ? 0.4138 0.9234 0.4304 -0.1423 -0.0507 0.0291 550 TYR A O 4193 C CB . TYR A 536 ? 0.3907 0.9336 0.3723 -0.1467 -0.0572 0.0207 550 TYR A CB 4194 C CG . TYR A 536 ? 0.4220 0.9583 0.3895 -0.1480 -0.0483 0.0240 550 TYR A CG 4195 C CD1 . TYR A 536 ? 0.4245 0.9718 0.3728 -0.1461 -0.0501 0.0295 550 TYR A CD1 4196 C CD2 . TYR A 536 ? 0.4328 0.9535 0.4064 -0.1511 -0.0381 0.0215 550 TYR A CD2 4197 C CE1 . TYR A 536 ? 0.4385 0.9826 0.3729 -0.1473 -0.0411 0.0322 550 TYR A CE1 4198 C CE2 . TYR A 536 ? 0.4884 1.0055 0.4502 -0.1520 -0.0291 0.0239 550 TYR A CE2 4199 C CZ . TYR A 536 ? 0.5004 1.0300 0.4422 -0.1500 -0.0302 0.0292 550 TYR A CZ 4200 O OH . TYR A 536 ? 0.4796 1.0080 0.4090 -0.1506 -0.0205 0.0316 550 TYR A OH 4201 N N . ILE A 537 ? 0.3951 0.9046 0.4030 -0.1317 -0.0557 0.0515 551 ILE A N 4202 C CA . ILE A 537 ? 0.4122 0.9021 0.4330 -0.1301 -0.0508 0.0579 551 ILE A CA 4203 C C . ILE A 537 ? 0.4059 0.8872 0.4194 -0.1345 -0.0398 0.0599 551 ILE A C 4204 O O . ILE A 537 ? 0.4005 0.8879 0.4003 -0.1338 -0.0380 0.0673 551 ILE A O 4205 C CB . ILE A 537 ? 0.3892 0.8737 0.4171 -0.1214 -0.0581 0.0728 551 ILE A CB 4206 C CG1 . ILE A 537 ? 0.4039 0.8973 0.4407 -0.1156 -0.0688 0.0698 551 ILE A CG1 4207 C CG2 . ILE A 537 ? 0.3618 0.8254 0.4029 -0.1200 -0.0538 0.0800 551 ILE A CG2 4208 C CD1 . ILE A 537 ? 0.4135 0.9070 0.4537 -0.1066 -0.0786 0.0833 551 ILE A CD1 4209 N N . GLU A 538 ? 0.3731 0.8415 0.3960 -0.1389 -0.0325 0.0536 552 GLU A N 4210 C CA . GLU A 538 ? 0.4373 0.8990 0.4550 -0.1428 -0.0216 0.0537 552 GLU A CA 4211 C C . GLU A 538 ? 0.4558 0.9032 0.4822 -0.1398 -0.0174 0.0680 552 GLU A C 4212 O O . GLU A 538 ? 0.5123 0.9588 0.5324 -0.1415 -0.0089 0.0720 552 GLU A O 4213 C CB . GLU A 538 ? 0.4563 0.9127 0.4785 -0.1500 -0.0156 0.0387 552 GLU A CB 4214 C CG . GLU A 538 ? 0.4659 0.9368 0.4795 -0.1543 -0.0196 0.0248 552 GLU A CG 4215 C CD . GLU A 538 ? 0.4657 0.9320 0.4811 -0.1619 -0.0136 0.0105 552 GLU A CD 4216 O OE1 . GLU A 538 ? 0.4442 0.8988 0.4631 -0.1634 -0.0050 0.0106 552 GLU A OE1 4217 O OE2 . GLU A 538 ? 0.4796 0.9543 0.4940 -0.1664 -0.0182 -0.0007 552 GLU A OE2 4218 N N . THR A 539 ? 0.4404 0.8774 0.4812 -0.1351 -0.0238 0.0755 553 THR A N 4219 C CA . THR A 539 ? 0.4681 0.8891 0.5206 -0.1327 -0.0214 0.0885 553 THR A CA 4220 C C . THR A 539 ? 0.5009 0.9245 0.5511 -0.1267 -0.0279 0.1054 553 THR A C 4221 O O . THR A 539 ? 0.4531 0.8793 0.5066 -0.1213 -0.0385 0.1081 553 THR A O 4222 C CB . THR A 539 ? 0.4514 0.8565 0.5223 -0.1318 -0.0247 0.0856 553 THR A CB 4223 O OG1 . THR A 539 ? 0.4854 0.8908 0.5574 -0.1377 -0.0209 0.0703 553 THR A OG1 4224 C CG2 . THR A 539 ? 0.4526 0.8399 0.5365 -0.1313 -0.0210 0.0961 553 THR A CG2 4225 N N . PRO A 540 ? 0.5522 0.9758 0.5976 -0.1277 -0.0215 0.1171 554 PRO A N 4226 C CA . PRO A 540 ? 0.6056 1.0326 0.6479 -0.1233 -0.0275 0.1349 554 PRO A CA 4227 C C . PRO A 540 ? 0.6107 1.0220 0.6718 -0.1176 -0.0373 0.1453 554 PRO A C 4228 O O . PRO A 540 ? 0.6010 0.9959 0.6778 -0.1181 -0.0357 0.1433 554 PRO A O 4229 C CB . PRO A 540 ? 0.6180 1.0462 0.6549 -0.1269 -0.0161 0.1445 554 PRO A CB 4230 C CG . PRO A 540 ? 0.6222 1.0554 0.6512 -0.1325 -0.0050 0.1279 554 PRO A CG 4231 C CD . PRO A 540 ? 0.5706 0.9930 0.6129 -0.1332 -0.0083 0.1141 554 PRO A CD 4232 N N . ARG A 541 ? 0.5969 1.0127 0.6566 -0.1120 -0.0483 0.1554 555 ARG A N 4233 C CA . ARG A 541 ? 0.6047 1.0056 0.6819 -0.1057 -0.0591 0.1665 555 ARG A CA 4234 C C . ARG A 541 ? 0.5635 0.9543 0.6547 -0.1015 -0.0658 0.1545 555 ARG A C 4235 O O . ARG A 541 ? 0.5486 0.9379 0.6468 -0.0943 -0.0779 0.1567 555 ARG A O 4236 C CB . ARG A 541 ? 0.6539 1.0406 0.7420 -0.1078 -0.0546 0.1817 555 ARG A CB 4237 C CG . ARG A 541 ? 0.7581 1.1565 0.8329 -0.1119 -0.0469 0.1950 555 ARG A CG 4238 C CD . ARG A 541 ? 0.8517 1.2382 0.9388 -0.1153 -0.0396 0.2080 555 ARG A CD 4239 N NE . ARG A 541 ? 0.9053 1.2835 0.9995 -0.1194 -0.0293 0.1953 555 ARG A NE 4240 C CZ . ARG A 541 ? 0.9207 1.3068 1.0068 -0.1251 -0.0151 0.1909 555 ARG A CZ 4241 N NH1 . ARG A 541 ? 0.9442 1.3476 1.0130 -0.1273 -0.0085 0.1978 555 ARG A NH1 4242 N NH2 . ARG A 541 ? 0.8887 1.2655 0.9839 -0.1282 -0.0077 0.1795 555 ARG A NH2 4243 N N . SER A 542 ? 0.5122 0.8969 0.6074 -0.1059 -0.0582 0.1418 556 SER A N 4244 C CA . SER A 542 ? 0.4396 0.8139 0.5479 -0.1027 -0.0633 0.1318 556 SER A CA 4245 C C . SER A 542 ? 0.4261 0.8142 0.5279 -0.1031 -0.0642 0.1152 556 SER A C 4246 O O . SER A 542 ? 0.4093 0.7932 0.5203 -0.0993 -0.0696 0.1075 556 SER A O 4247 C CB . SER A 542 ? 0.4578 0.8149 0.5770 -0.1071 -0.0562 0.1296 556 SER A CB 4248 O OG . SER A 542 ? 0.4708 0.8341 0.5813 -0.1151 -0.0441 0.1222 556 SER A OG 4249 N N . GLY A 543 ? 0.4142 0.8194 0.5006 -0.1078 -0.0591 0.1096 557 GLY A N 4250 C CA . GLY A 543 ? 0.3413 0.7598 0.4226 -0.1102 -0.0589 0.0940 557 GLY A CA 4251 C C . GLY A 543 ? 0.4181 0.8487 0.5008 -0.1034 -0.0697 0.0909 557 GLY A C 4252 O O . GLY A 543 ? 0.4563 0.8907 0.5382 -0.0972 -0.0777 0.1008 557 GLY A O 4253 N N . GLY A 544 ? 0.3912 0.8292 0.4768 -0.1048 -0.0700 0.0775 558 GLY A N 4254 C CA . GLY A 544 ? 0.3301 0.7822 0.4186 -0.0986 -0.0790 0.0728 558 GLY A CA 4255 C C . GLY A 544 ? 0.4017 0.8688 0.4884 -0.1038 -0.0766 0.0583 558 GLY A C 4256 O O . GLY A 544 ? 0.3719 0.8331 0.4609 -0.1105 -0.0698 0.0509 558 GLY A O 4257 N N . VAL A 545 ? 0.3817 0.8686 0.4655 -0.1010 -0.0829 0.0550 559 VAL A N 4258 C CA . VAL A 545 ? 0.3172 0.8207 0.4014 -0.1056 -0.0820 0.0424 559 VAL A CA 4259 C C . VAL A 545 ? 0.3363 0.8552 0.4288 -0.0971 -0.0912 0.0401 559 VAL A C 4260 O O . VAL A 545 ? 0.3486 0.8660 0.4446 -0.0878 -0.0989 0.0480 559 VAL A O 4261 C CB . VAL A 545 ? 0.3239 0.8407 0.3942 -0.1139 -0.0790 0.0380 559 VAL A CB 4262 C CG1 . VAL A 545 ? 0.3543 0.8579 0.4176 -0.1223 -0.0691 0.0372 559 VAL A CG1 4263 C CG2 . VAL A 545 ? 0.3389 0.8662 0.3999 -0.1094 -0.0857 0.0457 559 VAL A CG2 4264 N N . PHE A 546 ? 0.3436 0.8780 0.4404 -0.1003 -0.0905 0.0296 560 PHE A N 4265 C CA . PHE A 546 ? 0.3389 0.8917 0.4445 -0.0926 -0.0983 0.0262 560 PHE A CA 4266 C C . PHE A 546 ? 0.3384 0.9140 0.4437 -0.0996 -0.0973 0.0166 560 PHE A C 4267 O O . PHE A 546 ? 0.3352 0.9098 0.4357 -0.1106 -0.0905 0.0115 560 PHE A O 4268 C CB . PHE A 546 ? 0.3743 0.9202 0.4932 -0.0848 -0.0995 0.0236 560 PHE A CB 4269 C CG . PHE A 546 ? 0.3585 0.9031 0.4808 -0.0923 -0.0919 0.0153 560 PHE A CG 4270 C CD1 . PHE A 546 ? 0.3380 0.9044 0.4654 -0.0951 -0.0912 0.0064 560 PHE A CD1 4271 C CD2 . PHE A 546 ? 0.3385 0.8603 0.4596 -0.0966 -0.0859 0.0173 560 PHE A CD2 4272 C CE1 . PHE A 546 ? 0.3344 0.8997 0.4646 -0.1027 -0.0846 0.0003 560 PHE A CE1 4273 C CE2 . PHE A 546 ? 0.3233 0.8431 0.4474 -0.1036 -0.0798 0.0107 560 PHE A CE2 4274 C CZ . PHE A 546 ? 0.2680 0.8094 0.3962 -0.1068 -0.0792 0.0025 560 PHE A CZ 4275 N N . ILE A 547 ? 0.3055 0.9018 0.4175 -0.0932 -0.1047 0.0146 561 ILE A N 4276 C CA . ILE A 547 ? 0.4106 1.0232 0.5262 -0.0968 -0.1027 0.0057 561 ILE A CA 4277 C C . ILE A 547 ? 0.3775 0.9961 0.5068 -0.0858 -0.1053 0.0025 561 ILE A C 4278 O O . ILE A 547 ? 0.3566 0.9743 0.4927 -0.0750 -0.1126 0.0072 561 ILE A O 4279 C CB . ILE A 547 ? 0.4109 1.0365 0.5189 -0.0988 -0.1068 0.0054 561 ILE A CB 4280 C CG1 . ILE A 547 ? 0.3234 0.9572 0.4348 -0.0872 -0.1175 0.0120 561 ILE A CG1 4281 C CG2 . ILE A 547 ? 0.3859 1.0068 0.4792 -0.1096 -0.1039 0.0066 561 ILE A CG2 4282 C CD1 . ILE A 547 ? 0.3362 0.9834 0.4414 -0.0882 -0.1226 0.0116 561 ILE A CD1 4283 N N . ALA A 548 ? 0.3566 0.9813 0.4901 -0.0882 -0.0996 -0.0052 562 ALA A N 4284 C CA . ALA A 548 ? 0.3941 1.0264 0.5400 -0.0782 -0.1007 -0.0093 562 ALA A CA 4285 C C . ALA A 548 ? 0.3745 1.0235 0.5246 -0.0793 -0.0975 -0.0157 562 ALA A C 4286 O O . ALA A 548 ? 0.3457 0.9967 0.4896 -0.0897 -0.0931 -0.0174 562 ALA A O 4287 C CB . ALA A 548 ? 0.2837 0.9033 0.4323 -0.0787 -0.0959 -0.0110 562 ALA A CB 4288 N N . GLY A 549 ? 0.3885 1.0497 0.5502 -0.0683 -0.1000 -0.0194 563 GLY A N 4289 C CA . GLY A 549 ? 0.4023 1.0821 0.5704 -0.0683 -0.0965 -0.0252 563 GLY A CA 4290 C C . GLY A 549 ? 0.3833 1.0703 0.5611 -0.0595 -0.0943 -0.0306 563 GLY A C 4291 O O . GLY A 549 ? 0.3087 0.9868 0.4899 -0.0510 -0.0980 -0.0303 563 GLY A O 4292 N N . ARG A 550 ? 0.3843 1.0882 0.5667 -0.0613 -0.0887 -0.0357 564 ARG A N 4293 C CA . ARG A 550 ? 0.3626 1.0762 0.5521 -0.0546 -0.0848 -0.0417 564 ARG A CA 4294 C C . ARG A 550 ? 0.3878 1.0836 0.5711 -0.0584 -0.0805 -0.0416 564 ARG A C 4295 O O . ARG A 550 ? 0.3491 1.0463 0.5377 -0.0487 -0.0817 -0.0458 564 ARG A O 4296 C CB . ARG A 550 ? 0.3692 1.0943 0.5714 -0.0369 -0.0926 -0.0453 564 ARG A CB 4297 C CG . ARG A 550 ? 0.3904 1.1372 0.6017 -0.0321 -0.0958 -0.0469 564 ARG A CG 4298 C CD . ARG A 550 ? 0.3894 1.1442 0.6142 -0.0138 -0.1048 -0.0502 564 ARG A CD 4299 N NE . ARG A 550 ? 0.3657 1.1392 0.6001 -0.0092 -0.1093 -0.0507 564 ARG A NE 4300 C CZ . ARG A 550 ? 0.3717 1.1519 0.6187 0.0059 -0.1186 -0.0525 564 ARG A CZ 4301 N NH1 . ARG A 550 ? 0.3883 1.1571 0.6399 0.0182 -0.1247 -0.0540 564 ARG A NH1 4302 N NH2 . ARG A 550 ? 0.3758 1.1729 0.6319 0.0088 -0.1227 -0.0525 564 ARG A NH2 4303 N N . VAL A 551 ? 0.3744 1.0534 0.5471 -0.0720 -0.0761 -0.0374 565 VAL A N 4304 C CA . VAL A 551 ? 0.3648 1.0264 0.5323 -0.0765 -0.0721 -0.0369 565 VAL A CA 4305 C C . VAL A 551 ? 0.3739 1.0457 0.5412 -0.0810 -0.0641 -0.0410 565 VAL A C 4306 O O . VAL A 551 ? 0.3425 1.0193 0.5062 -0.0913 -0.0588 -0.0400 565 VAL A O 4307 C CB . VAL A 551 ? 0.3177 0.9570 0.4750 -0.0886 -0.0704 -0.0313 565 VAL A CB 4308 C CG1 . VAL A 551 ? 0.2645 0.8854 0.4181 -0.0932 -0.0668 -0.0305 565 VAL A CG1 4309 C CG2 . VAL A 551 ? 0.3052 0.9380 0.4618 -0.0842 -0.0781 -0.0267 565 VAL A CG2 4310 N N . ASN A 552 ? 0.3911 1.0664 0.5622 -0.0732 -0.0639 -0.0453 566 ASN A N 4311 C CA . ASN A 552 ? 0.4228 1.1169 0.5954 -0.0737 -0.0574 -0.0502 566 ASN A CA 4312 C C . ASN A 552 ? 0.4090 1.0923 0.5735 -0.0843 -0.0509 -0.0488 566 ASN A C 4313 O O . ASN A 552 ? 0.4204 1.1191 0.5836 -0.0888 -0.0446 -0.0504 566 ASN A O 4314 C CB . ASN A 552 ? 0.4414 1.1533 0.6238 -0.0567 -0.0611 -0.0580 566 ASN A CB 4315 C CG . ASN A 552 ? 0.5037 1.1989 0.6872 -0.0483 -0.0671 -0.0596 566 ASN A CG 4316 O OD1 . ASN A 552 ? 0.4781 1.1492 0.6550 -0.0561 -0.0677 -0.0543 566 ASN A OD1 4317 N ND2 . ASN A 552 ? 0.5803 1.2877 0.7727 -0.0320 -0.0721 -0.0673 566 ASN A ND2 4318 N N . LYS A 553 ? 0.3987 1.0561 0.5581 -0.0885 -0.0526 -0.0451 567 LYS A N 4319 C CA . LYS A 553 ? 0.3673 1.0114 0.5199 -0.0980 -0.0478 -0.0433 567 LYS A CA 4320 C C . LYS A 553 ? 0.3691 0.9851 0.5151 -0.1090 -0.0476 -0.0367 567 LYS A C 4321 O O . LYS A 553 ? 0.4085 1.0143 0.5556 -0.1063 -0.0523 -0.0344 567 LYS A O 4322 C CB . LYS A 553 ? 0.3783 1.0201 0.5336 -0.0888 -0.0513 -0.0477 567 LYS A CB 4323 C CG . LYS A 553 ? 0.4742 1.1445 0.6346 -0.0783 -0.0502 -0.0560 567 LYS A CG 4324 C CD . LYS A 553 ? 0.5573 1.2414 0.7118 -0.0884 -0.0414 -0.0556 567 LYS A CD 4325 C CE . LYS A 553 ? 0.5965 1.3149 0.7562 -0.0784 -0.0387 -0.0639 567 LYS A CE 4326 N NZ . LYS A 553 ? 0.6279 1.3662 0.7943 -0.0741 -0.0383 -0.0650 567 LYS A NZ 4327 N N . GLY A 554 ? 0.3342 0.9383 0.4735 -0.1209 -0.0424 -0.0335 568 GLY A N 4328 C CA . GLY A 554 ? 0.2966 0.8723 0.4306 -0.1301 -0.0420 -0.0284 568 GLY A CA 4329 C C . GLY A 554 ? 0.3410 0.9037 0.4701 -0.1386 -0.0382 -0.0262 568 GLY A C 4330 O O . GLY A 554 ? 0.3544 0.9292 0.4838 -0.1360 -0.0368 -0.0287 568 GLY A O 4331 N N . GLY A 555 ? 0.2849 0.8237 0.4094 -0.1483 -0.0366 -0.0218 569 GLY A N 4332 C CA . GLY A 555 ? 0.2740 0.7979 0.3942 -0.1564 -0.0339 -0.0188 569 GLY A CA 4333 C C . GLY A 555 ? 0.3117 0.8241 0.4333 -0.1527 -0.0363 -0.0189 569 GLY A C 4334 O O . GLY A 555 ? 0.2585 0.7595 0.3835 -0.1482 -0.0401 -0.0187 569 GLY A O 4335 N N . ILE A 556 ? 0.3521 0.8679 0.4711 -0.1551 -0.0348 -0.0189 570 ILE A N 4336 C CA . ILE A 556 ? 0.3900 0.8952 0.5105 -0.1517 -0.0384 -0.0196 570 ILE A CA 4337 C C . ILE A 556 ? 0.3626 0.8847 0.4894 -0.1384 -0.0435 -0.0258 570 ILE A C 4338 O O . ILE A 556 ? 0.2470 0.7581 0.3768 -0.1339 -0.0488 -0.0266 570 ILE A O 4339 C CB . ILE A 556 ? 0.4593 0.9653 0.5747 -0.1575 -0.0365 -0.0184 570 ILE A CB 4340 C CG1 . ILE A 556 ? 0.4346 0.9701 0.5471 -0.1589 -0.0320 -0.0202 570 ILE A CG1 4341 C CG2 . ILE A 556 ? 0.5118 0.9882 0.6234 -0.1684 -0.0352 -0.0115 570 ILE A CG2 4342 C CD1 . ILE A 556 ? 0.4750 1.0157 0.5816 -0.1648 -0.0302 -0.0186 570 ILE A CD1 4343 N N . LEU A 557 ? 0.3426 0.8900 0.4721 -0.1316 -0.0428 -0.0299 571 LEU A N 4344 C CA . LEU A 557 ? 0.3394 0.9021 0.4761 -0.1170 -0.0487 -0.0362 571 LEU A CA 4345 C C . LEU A 557 ? 0.3457 0.9032 0.4874 -0.1116 -0.0530 -0.0345 571 LEU A C 4346 O O . LEU A 557 ? 0.3788 0.9517 0.5268 -0.0992 -0.0578 -0.0390 571 LEU A O 4347 C CB . LEU A 557 ? 0.3273 0.9236 0.4657 -0.1104 -0.0461 -0.0427 571 LEU A CB 4348 C CG . LEU A 557 ? 0.3993 1.0107 0.5330 -0.1137 -0.0417 -0.0454 571 LEU A CG 4349 C CD1 . LEU A 557 ? 0.4413 1.0894 0.5789 -0.1037 -0.0396 -0.0532 571 LEU A CD1 4350 C CD2 . LEU A 557 ? 0.4015 1.0003 0.5336 -0.1114 -0.0466 -0.0476 571 LEU A CD2 4351 N N . ILE A 558 ? 0.2872 0.8240 0.4261 -0.1202 -0.0516 -0.0283 572 ILE A N 4352 C CA . ILE A 558 ? 0.3155 0.8509 0.4570 -0.1168 -0.0548 -0.0262 572 ILE A CA 4353 C C . ILE A 558 ? 0.3517 0.8842 0.5005 -0.1054 -0.0634 -0.0263 572 ILE A C 4354 O O . ILE A 558 ? 0.3801 0.9194 0.5319 -0.0976 -0.0674 -0.0260 572 ILE A O 4355 C CB . ILE A 558 ? 0.3084 0.8231 0.4448 -0.1281 -0.0514 -0.0206 572 ILE A CB 4356 C CG1 . ILE A 558 ? 0.2975 0.8154 0.4350 -0.1253 -0.0544 -0.0187 572 ILE A CG1 4357 C CG2 . ILE A 558 ? 0.2404 0.7295 0.3768 -0.1327 -0.0519 -0.0168 572 ILE A CG2 4358 C CD1 . ILE A 558 ? 0.2484 0.7896 0.3863 -0.1216 -0.0544 -0.0218 572 ILE A CD1 4359 N N . ARG A 559 ? 0.3424 0.8525 0.4895 -0.1018 -0.0652 -0.0258 573 ARG A N 4360 C CA . ARG A 559 ? 0.3793 0.8706 0.5287 -0.0880 -0.0722 -0.0250 573 ARG A CA 4361 C C . ARG A 559 ? 0.3880 0.8974 0.5417 -0.0727 -0.0768 -0.0321 573 ARG A C 4362 O O . ARG A 559 ? 0.4132 0.9116 0.5709 -0.0605 -0.0840 -0.0314 573 ARG A O 4363 C CB . ARG A 559 ? 0.3852 0.8496 0.5324 -0.0878 -0.0737 -0.0239 573 ARG A CB 4364 C CG . ARG A 559 ? 0.4027 0.8390 0.5499 -0.0949 -0.0734 -0.0153 573 ARG A CG 4365 C CD . ARG A 559 ? 0.4204 0.8295 0.5683 -0.0911 -0.0777 -0.0140 573 ARG A CD 4366 N NE . ARG A 559 ? 0.5048 0.8891 0.6551 -0.0963 -0.0777 -0.0052 573 ARG A NE 4367 C CZ . ARG A 559 ? 0.5757 0.9464 0.7305 -0.0891 -0.0825 0.0003 573 ARG A CZ 4368 N NH1 . ARG A 559 ? 0.6102 0.9876 0.7680 -0.0760 -0.0890 -0.0022 573 ARG A NH1 4369 N NH2 . ARG A 559 ? 0.6210 0.9719 0.7782 -0.0948 -0.0811 0.0087 573 ARG A NH2 4370 N N . SER A 560 ? 0.3914 0.9286 0.5452 -0.0735 -0.0730 -0.0387 574 SER A N 4371 C CA . SER A 560 ? 0.4709 1.0291 0.6298 -0.0590 -0.0762 -0.0469 574 SER A CA 4372 C C . SER A 560 ? 0.4431 1.0257 0.6084 -0.0560 -0.0774 -0.0472 574 SER A C 4373 O O . SER A 560 ? 0.4519 1.0543 0.6236 -0.0436 -0.0803 -0.0541 574 SER A O 4374 C CB . SER A 560 ? 0.5372 1.1165 0.6932 -0.0612 -0.0705 -0.0538 574 SER A CB 4375 O OG . SER A 560 ? 0.6001 1.1579 0.7490 -0.0658 -0.0695 -0.0529 574 SER A OG 4376 N N . ALA A 561 ? 0.3706 0.9528 0.5346 -0.0670 -0.0755 -0.0405 575 ALA A N 4377 C CA . ALA A 561 ? 0.3197 0.9249 0.4876 -0.0665 -0.0758 -0.0408 575 ALA A CA 4378 C C . ALA A 561 ? 0.2874 0.8960 0.4631 -0.0509 -0.0849 -0.0417 575 ALA A C 4379 O O . ALA A 561 ? 0.3192 0.9028 0.4936 -0.0463 -0.0903 -0.0362 575 ALA A O 4380 C CB . ALA A 561 ? 0.2744 0.8683 0.4350 -0.0799 -0.0717 -0.0338 575 ALA A CB 4381 N N . THR A 562 ? 0.2656 0.8999 0.4482 -0.0423 -0.0859 -0.0478 576 THR A N 4382 C CA . THR A 562 ? 0.3042 0.9445 0.4955 -0.0287 -0.0951 -0.0479 576 THR A CA 4383 C C . THR A 562 ? 0.3299 0.9810 0.5195 -0.0341 -0.0931 -0.0445 576 THR A C 4384 O O . THR A 562 ? 0.3055 0.9606 0.4881 -0.0471 -0.0847 -0.0434 576 THR A O 4385 C CB . THR A 562 ? 0.3584 1.0147 0.5597 -0.0116 -0.0991 -0.0580 576 THR A CB 4386 O OG1 . THR A 562 ? 0.4155 1.0954 0.6161 -0.0148 -0.0900 -0.0645 576 THR A OG1 4387 C CG2 . THR A 562 ? 0.4044 1.0345 0.6028 -0.0035 -0.1017 -0.0610 576 THR A CG2 4388 N N . GLY A 563 ? 0.3864 1.0414 0.5827 -0.0241 -0.1017 -0.0426 577 GLY A N 4389 C CA . GLY A 563 ? 0.3978 1.0630 0.5930 -0.0278 -0.1020 -0.0392 577 GLY A CA 4390 C C . GLY A 563 ? 0.3884 1.0471 0.5876 -0.0192 -0.1135 -0.0331 577 GLY A C 4391 O O . GLY A 563 ? 0.4062 1.0599 0.6140 -0.0058 -0.1219 -0.0340 577 GLY A O 4392 N N . VAL A 564 ? 0.3281 0.9867 0.5212 -0.0266 -0.1144 -0.0268 578 VAL A N 4393 C CA . VAL A 564 ? 0.3150 0.9663 0.5090 -0.0209 -0.1250 -0.0186 578 VAL A CA 4394 C C . VAL A 564 ? 0.3323 0.9690 0.5130 -0.0339 -0.1226 -0.0102 578 VAL A C 4395 O O . VAL A 564 ? 0.3090 0.9496 0.4808 -0.0455 -0.1165 -0.0102 578 VAL A O 4396 C CB . VAL A 564 ? 0.3100 0.9776 0.5092 -0.0154 -0.1307 -0.0184 578 VAL A CB 4397 C CG1 . VAL A 564 ? 0.3190 0.9785 0.5200 -0.0079 -0.1429 -0.0093 578 VAL A CG1 4398 C CG2 . VAL A 564 ? 0.3743 1.0597 0.5871 -0.0040 -0.1309 -0.0279 578 VAL A CG2 4399 N N . PHE A 565 ? 0.3401 0.9580 0.5195 -0.0316 -0.1269 -0.0032 579 PHE A N 4400 C CA . PHE A 565 ? 0.2979 0.8969 0.4637 -0.0432 -0.1222 0.0044 579 PHE A CA 4401 C C . PHE A 565 ? 0.3097 0.8982 0.4708 -0.0398 -0.1297 0.0158 579 PHE A C 4402 O O . PHE A 565 ? 0.3474 0.9205 0.5140 -0.0295 -0.1368 0.0213 579 PHE A O 4403 C CB . PHE A 565 ? 0.2931 0.8668 0.4564 -0.0459 -0.1164 0.0047 579 PHE A CB 4404 C CG . PHE A 565 ? 0.3298 0.9119 0.4953 -0.0510 -0.1086 -0.0048 579 PHE A CG 4405 C CD1 . PHE A 565 ? 0.3442 0.9350 0.5195 -0.0408 -0.1105 -0.0126 579 PHE A CD1 4406 C CD2 . PHE A 565 ? 0.2982 0.8794 0.4559 -0.0658 -0.0998 -0.0059 579 PHE A CD2 4407 C CE1 . PHE A 565 ? 0.2742 0.8741 0.4502 -0.0459 -0.1031 -0.0204 579 PHE A CE1 4408 C CE2 . PHE A 565 ? 0.2775 0.8660 0.4372 -0.0713 -0.0932 -0.0130 579 PHE A CE2 4409 C CZ . PHE A 565 ? 0.2667 0.8649 0.4348 -0.0616 -0.0946 -0.0198 579 PHE A CZ 4410 N N . PHE A 566 ? 0.3127 0.9090 0.4632 -0.0488 -0.1284 0.0194 580 PHE A N 4411 C CA . PHE A 566 ? 0.3254 0.9152 0.4685 -0.0473 -0.1348 0.0307 580 PHE A CA 4412 C C . PHE A 566 ? 0.3267 0.8950 0.4564 -0.0567 -0.1277 0.0376 580 PHE A C 4413 O O . PHE A 566 ? 0.3241 0.8969 0.4431 -0.0681 -0.1207 0.0350 580 PHE A O 4414 C CB . PHE A 566 ? 0.3303 0.9453 0.4698 -0.0502 -0.1391 0.0294 580 PHE A CB 4415 C CG . PHE A 566 ? 0.4580 1.0701 0.5887 -0.0484 -0.1468 0.0411 580 PHE A CG 4416 C CD1 . PHE A 566 ? 0.4384 1.0292 0.5685 -0.0426 -0.1510 0.0527 580 PHE A CD1 4417 C CD2 . PHE A 566 ? 0.4606 1.0921 0.5838 -0.0531 -0.1503 0.0409 580 PHE A CD2 4418 C CE1 . PHE A 566 ? 0.4578 1.0473 0.5791 -0.0418 -0.1579 0.0648 580 PHE A CE1 4419 C CE2 . PHE A 566 ? 0.4852 1.1151 0.5985 -0.0519 -0.1575 0.0520 580 PHE A CE2 4420 C CZ . PHE A 566 ? 0.4899 1.0993 0.6020 -0.0463 -0.1611 0.0644 580 PHE A CZ 4421 N N . TRP A 567 ? 0.3690 0.9142 0.5008 -0.0517 -0.1296 0.0461 581 TRP A N 4422 C CA . TRP A 567 ? 0.3801 0.9049 0.5024 -0.0596 -0.1224 0.0531 581 TRP A CA 4423 C C . TRP A 567 ? 0.4348 0.9559 0.5472 -0.0601 -0.1261 0.0662 581 TRP A C 4424 O O . TRP A 567 ? 0.4658 0.9888 0.5831 -0.0512 -0.1367 0.0737 581 TRP A O 4425 C CB . TRP A 567 ? 0.3623 0.8633 0.4935 -0.0548 -0.1222 0.0558 581 TRP A CB 4426 C CG . TRP A 567 ? 0.3913 0.8932 0.5317 -0.0528 -0.1195 0.0441 581 TRP A CG 4427 C CD1 . TRP A 567 ? 0.3988 0.9113 0.5505 -0.0425 -0.1257 0.0370 581 TRP A CD1 4428 C CD2 . TRP A 567 ? 0.3990 0.8909 0.5377 -0.0609 -0.1100 0.0386 581 TRP A CD2 4429 N NE1 . TRP A 567 ? 0.4141 0.9251 0.5697 -0.0441 -0.1202 0.0275 581 TRP A NE1 4430 C CE2 . TRP A 567 ? 0.4013 0.8992 0.5491 -0.0556 -0.1110 0.0288 581 TRP A CE2 4431 C CE3 . TRP A 567 ? 0.3875 0.8668 0.5184 -0.0720 -0.1009 0.0409 581 TRP A CE3 4432 C CZ2 . TRP A 567 ? 0.3717 0.8631 0.5197 -0.0617 -0.1036 0.0222 581 TRP A CZ2 4433 C CZ3 . TRP A 567 ? 0.3591 0.8309 0.4921 -0.0777 -0.0942 0.0342 581 TRP A CZ3 4434 C CH2 . TRP A 567 ? 0.3409 0.8186 0.4818 -0.0729 -0.0957 0.0255 581 TRP A CH2 4435 N N . ILE A 568 ? 0.4116 0.9277 0.5104 -0.0702 -0.1178 0.0693 582 ILE A N 4436 C CA . ILE A 568 ? 0.3630 0.8720 0.4521 -0.0708 -0.1195 0.0835 582 ILE A CA 4437 C C . ILE A 568 ? 0.3702 0.8593 0.4557 -0.0769 -0.1100 0.0888 582 ILE A C 4438 O O . ILE A 568 ? 0.3742 0.8597 0.4578 -0.0844 -0.1003 0.0802 582 ILE A O 4439 C CB . ILE A 568 ? 0.3851 0.9130 0.4585 -0.0753 -0.1209 0.0846 582 ILE A CB 4440 C CG1 . ILE A 568 ? 0.3775 0.9134 0.4399 -0.0865 -0.1108 0.0734 582 ILE A CG1 4441 C CG2 . ILE A 568 ? 0.3785 0.9250 0.4577 -0.0679 -0.1325 0.0827 582 ILE A CG2 4442 C CD1 . ILE A 568 ? 0.3822 0.9336 0.4270 -0.0912 -0.1122 0.0747 582 ILE A CD1 4443 N N . PHE A 569 ? 0.3913 0.8676 0.4773 -0.0738 -0.1132 0.1036 583 PHE A N 4444 C CA . PHE A 569 ? 0.3961 0.8534 0.4822 -0.0785 -0.1050 0.1102 583 PHE A CA 4445 C C . PHE A 569 ? 0.4246 0.8835 0.4966 -0.0832 -0.1013 0.1228 583 PHE A C 4446 O O . PHE A 569 ? 0.4454 0.9140 0.5110 -0.0801 -0.1088 0.1316 583 PHE A O 4447 C CB . PHE A 569 ? 0.4066 0.8441 0.5098 -0.0710 -0.1114 0.1168 583 PHE A CB 4448 C CG . PHE A 569 ? 0.4071 0.8418 0.5225 -0.0668 -0.1132 0.1038 583 PHE A CG 4449 C CD1 . PHE A 569 ? 0.4137 0.8601 0.5360 -0.0582 -0.1226 0.0976 583 PHE A CD1 4450 C CD2 . PHE A 569 ? 0.4020 0.8234 0.5220 -0.0713 -0.1055 0.0977 583 PHE A CD2 4451 C CE1 . PHE A 569 ? 0.4171 0.8632 0.5496 -0.0540 -0.1235 0.0854 583 PHE A CE1 4452 C CE2 . PHE A 569 ? 0.3529 0.7728 0.4823 -0.0677 -0.1070 0.0860 583 PHE A CE2 4453 C CZ . PHE A 569 ? 0.3693 0.8022 0.5044 -0.0590 -0.1155 0.0797 583 PHE A CZ 4454 N N . ALA A 570 ? 0.4693 0.9194 0.5367 -0.0905 -0.0899 0.1238 584 ALA A N 4455 C CA . ALA A 570 ? 0.5050 0.9581 0.5582 -0.0954 -0.0840 0.1347 584 ALA A CA 4456 C C . ALA A 570 ? 0.5259 0.9691 0.5846 -0.0912 -0.0899 0.1549 584 ALA A C 4457 O O . ALA A 570 ? 0.5650 1.0126 0.6120 -0.0948 -0.0856 0.1663 584 ALA A O 4458 C CB . ALA A 570 ? 0.4947 0.9417 0.5441 -0.1036 -0.0697 0.1288 584 ALA A CB 4459 N N . ASN A 571 ? 0.4792 0.9094 0.5558 -0.0838 -0.0997 0.1593 585 ASN A N 4460 C CA . ASN A 571 ? 0.4830 0.9026 0.5674 -0.0796 -0.1077 0.1788 585 ASN A CA 4461 C C . ASN A 571 ? 0.5229 0.9532 0.6051 -0.0731 -0.1214 0.1861 585 ASN A C 4462 O O . ASN A 571 ? 0.5991 1.0208 0.6900 -0.0685 -0.1313 0.2022 585 ASN A O 4463 C CB . ASN A 571 ? 0.5054 0.9025 0.6113 -0.0750 -0.1123 0.1804 585 ASN A CB 4464 C CG . ASN A 571 ? 0.5244 0.9203 0.6424 -0.0657 -0.1238 0.1702 585 ASN A CG 4465 O OD1 . ASN A 571 ? 0.4882 0.9003 0.5999 -0.0642 -0.1249 0.1579 585 ASN A OD1 4466 N ND2 . ASN A 571 ? 0.5387 0.9157 0.6748 -0.0591 -0.1327 0.1751 585 ASN A ND2 4467 N N . GLY A 572 ? 0.4774 0.9265 0.5493 -0.0728 -0.1228 0.1746 586 GLY A N 4468 C CA . GLY A 572 ? 0.4976 0.9587 0.5674 -0.0668 -0.1358 0.1802 586 GLY A CA 4469 C C . GLY A 572 ? 0.5159 0.9727 0.6049 -0.0561 -0.1487 0.1750 586 GLY A C 4470 O O . GLY A 572 ? 0.5616 1.0153 0.6589 -0.0490 -0.1619 0.1867 586 GLY A O 4471 N N . SER A 573 ? 0.4846 0.9415 0.5810 -0.0548 -0.1451 0.1574 587 SER A N 4472 C CA . SER A 573 ? 0.4766 0.9313 0.5907 -0.0442 -0.1558 0.1502 587 SER A CA 4473 C C . SER A 573 ? 0.4647 0.9359 0.5780 -0.0445 -0.1520 0.1306 587 SER A C 4474 O O . SER A 573 ? 0.4443 0.9232 0.5460 -0.0536 -0.1406 0.1221 587 SER A O 4475 C CB . SER A 573 ? 0.5021 0.9327 0.6325 -0.0403 -0.1569 0.1518 587 SER A CB 4476 O OG . SER A 573 ? 0.5085 0.9325 0.6358 -0.0479 -0.1436 0.1429 587 SER A OG 4477 N N . TYR A 574 ? 0.4442 0.9215 0.5708 -0.0344 -0.1619 0.1238 588 TYR A N 4478 C CA . TYR A 574 ? 0.4049 0.8975 0.5347 -0.0337 -0.1587 0.1059 588 TYR A CA 4479 C C . TYR A 574 ? 0.3930 0.8777 0.5415 -0.0230 -0.1645 0.0983 588 TYR A C 4480 O O . TYR A 574 ? 0.4035 0.8728 0.5634 -0.0144 -0.1742 0.1064 588 TYR A O 4481 C CB . TYR A 574 ? 0.4417 0.9598 0.5664 -0.0328 -0.1640 0.1025 588 TYR A CB 4482 C CG . TYR A 574 ? 0.5115 1.0355 0.6499 -0.0200 -0.1794 0.1059 588 TYR A CG 4483 C CD1 . TYR A 574 ? 0.5383 1.0567 0.6760 -0.0162 -0.1899 0.1224 588 TYR A CD1 4484 C CD2 . TYR A 574 ? 0.5210 1.0578 0.6734 -0.0116 -0.1835 0.0928 588 TYR A CD2 4485 C CE1 . TYR A 574 ? 0.5305 1.0538 0.6820 -0.0043 -0.2050 0.1255 588 TYR A CE1 4486 C CE2 . TYR A 574 ? 0.5345 1.0775 0.7009 0.0009 -0.1977 0.0948 588 TYR A CE2 4487 C CZ . TYR A 574 ? 0.5526 1.0879 0.7190 0.0046 -0.2089 0.1111 588 TYR A CZ 4488 O OH . TYR A 574 ? 0.5384 1.0790 0.7202 0.0173 -0.2241 0.1132 588 TYR A OH 4489 N N . ARG A 575 ? 0.4187 0.9141 0.5702 -0.0236 -0.1588 0.0826 589 ARG A N 4490 C CA . ARG A 575 ? 0.4605 0.9533 0.6276 -0.0132 -0.1634 0.0729 589 ARG A CA 4491 C C . ARG A 575 ? 0.4372 0.9556 0.6056 -0.0135 -0.1598 0.0580 589 ARG A C 4492 O O . ARG A 575 ? 0.4270 0.9569 0.5846 -0.0247 -0.1502 0.0534 589 ARG A O 4493 C CB . ARG A 575 ? 0.5177 0.9887 0.6875 -0.0155 -0.1571 0.0704 589 ARG A CB 4494 C CG . ARG A 575 ? 0.6322 1.0764 0.8083 -0.0115 -0.1636 0.0831 589 ARG A CG 4495 C CD . ARG A 575 ? 0.7060 1.1304 0.8863 -0.0131 -0.1584 0.0784 589 ARG A CD 4496 N NE . ARG A 575 ? 0.8295 1.2296 1.0107 -0.0166 -0.1588 0.0924 589 ARG A NE 4497 C CZ . ARG A 575 ? 0.9045 1.2838 1.0986 -0.0086 -0.1690 0.0989 589 ARG A CZ 4498 N NH1 . ARG A 575 ? 0.9489 1.3278 1.1556 0.0044 -0.1799 0.0915 589 ARG A NH1 4499 N NH2 . ARG A 575 ? 0.9114 1.2706 1.1067 -0.0134 -0.1686 0.1126 589 ARG A NH2 4500 N N . VAL A 576 ? 0.4414 0.9693 0.6239 -0.0013 -0.1676 0.0506 590 VAL A N 4501 C CA . VAL A 576 ? 0.4268 0.9790 0.6133 -0.0008 -0.1632 0.0360 590 VAL A CA 4502 C C . VAL A 576 ? 0.4321 0.9763 0.6283 0.0063 -0.1617 0.0260 590 VAL A C 4503 O O . VAL A 576 ? 0.4308 0.9624 0.6383 0.0189 -0.1710 0.0267 590 VAL A O 4504 C CB . VAL A 576 ? 0.4252 1.0014 0.6202 0.0076 -0.1725 0.0340 590 VAL A CB 4505 C CG1 . VAL A 576 ? 0.3601 0.9648 0.5583 0.0050 -0.1662 0.0204 590 VAL A CG1 4506 C CG2 . VAL A 576 ? 0.4322 1.0122 0.6171 0.0021 -0.1768 0.0459 590 VAL A CG2 4507 N N . THR A 577 ? 0.3648 0.9151 0.5564 -0.0018 -0.1506 0.0169 591 THR A N 4508 C CA . THR A 577 ? 0.3656 0.9084 0.5635 0.0039 -0.1485 0.0076 591 THR A CA 4509 C C . THR A 577 ? 0.3567 0.9269 0.5582 0.0039 -0.1426 -0.0059 591 THR A C 4510 O O . THR A 577 ? 0.3872 0.9796 0.5847 -0.0045 -0.1376 -0.0076 591 THR A O 4511 C CB . THR A 577 ? 0.3163 0.8333 0.5063 -0.0050 -0.1414 0.0111 591 THR A CB 4512 O OG1 . THR A 577 ? 0.3521 0.8778 0.5315 -0.0201 -0.1299 0.0092 591 THR A OG1 4513 C CG2 . THR A 577 ? 0.3248 0.8167 0.5126 -0.0055 -0.1464 0.0253 591 THR A CG2 4514 N N . ALA A 578 ? 0.3388 0.9076 0.5477 0.0134 -0.1434 -0.0152 592 ALA A N 4515 C CA . ALA A 578 ? 0.3680 0.9625 0.5803 0.0141 -0.1371 -0.0278 592 ALA A CA 4516 C C . ALA A 578 ? 0.3268 0.9163 0.5291 0.0009 -0.1254 -0.0304 592 ALA A C 4517 O O . ALA A 578 ? 0.3478 0.9597 0.5503 -0.0030 -0.1183 -0.0384 592 ALA A O 4518 C CB . ALA A 578 ? 0.3897 0.9870 0.6143 0.0318 -0.1438 -0.0376 592 ALA A CB 4519 N N . ASP A 579 ? 0.3091 0.8699 0.5035 -0.0062 -0.1238 -0.0228 593 ASP A N 4520 C CA . ASP A 579 ? 0.3285 0.8801 0.5148 -0.0175 -0.1144 -0.0246 593 ASP A CA 4521 C C . ASP A 579 ? 0.3633 0.8968 0.5401 -0.0312 -0.1100 -0.0146 593 ASP A C 4522 O O . ASP A 579 ? 0.3823 0.9012 0.5583 -0.0297 -0.1150 -0.0054 593 ASP A O 4523 C CB . ASP A 579 ? 0.3328 0.8641 0.5214 -0.0090 -0.1173 -0.0289 593 ASP A CB 4524 C CG . ASP A 579 ? 0.3625 0.8650 0.5549 -0.0013 -0.1269 -0.0209 593 ASP A CG 4525 O OD1 . ASP A 579 ? 0.4086 0.9139 0.6069 0.0062 -0.1349 -0.0164 593 ASP A OD1 4526 O OD2 . ASP A 579 ? 0.3414 0.8184 0.5316 -0.0030 -0.1271 -0.0184 593 ASP A OD2 4527 N N . LEU A 580 ? 0.3360 0.8708 0.5060 -0.0445 -0.1007 -0.0162 594 LEU A N 4528 C CA . LEU A 580 ? 0.3141 0.8323 0.4760 -0.0575 -0.0957 -0.0086 594 LEU A CA 4529 C C . LEU A 580 ? 0.3428 0.8288 0.5045 -0.0550 -0.0983 -0.0019 594 LEU A C 4530 O O . LEU A 580 ? 0.3557 0.8275 0.5130 -0.0610 -0.0969 0.0066 594 LEU A O 4531 C CB . LEU A 580 ? 0.3066 0.8325 0.4638 -0.0714 -0.0865 -0.0126 594 LEU A CB 4532 C CG . LEU A 580 ? 0.3305 0.8395 0.4806 -0.0851 -0.0805 -0.0072 594 LEU A CG 4533 C CD1 . LEU A 580 ? 0.3411 0.8519 0.4866 -0.0886 -0.0812 -0.0014 594 LEU A CD1 4534 C CD2 . LEU A 580 ? 0.2969 0.8171 0.4451 -0.0974 -0.0733 -0.0121 594 LEU A CD2 4535 N N . GLY A 581 ? 0.3354 0.8106 0.5021 -0.0461 -0.1022 -0.0059 595 GLY A N 4536 C CA . GLY A 581 ? 0.3041 0.7485 0.4727 -0.0432 -0.1063 0.0003 595 GLY A CA 4537 C C . GLY A 581 ? 0.3324 0.7672 0.5067 -0.0332 -0.1159 0.0080 595 GLY A C 4538 O O . GLY A 581 ? 0.3581 0.7680 0.5356 -0.0312 -0.1201 0.0154 595 GLY A O 4539 N N . GLY A 582 ? 0.3735 0.8285 0.5504 -0.0271 -0.1200 0.0070 596 GLY A N 4540 C CA . GLY A 582 ? 0.3866 0.8346 0.5690 -0.0183 -0.1298 0.0155 596 GLY A CA 4541 C C . GLY A 582 ? 0.4283 0.8576 0.6214 -0.0046 -0.1409 0.0155 596 GLY A C 4542 O O . GLY A 582 ? 0.4682 0.8809 0.6656 -0.0011 -0.1484 0.0264 596 GLY A O 4543 N N . TRP A 583 ? 0.4285 0.8606 0.6258 0.0030 -0.1423 0.0036 597 TRP A N 4544 C CA . TRP A 583 ? 0.4112 0.8263 0.6190 0.0172 -0.1538 0.0011 597 TRP A CA 4545 C C . TRP A 583 ? 0.3934 0.8233 0.6113 0.0315 -0.1636 -0.0027 597 TRP A C 4546 O O . TRP A 583 ? 0.4286 0.8420 0.6568 0.0427 -0.1758 0.0004 597 TRP A O 4547 C CB . TRP A 583 ? 0.4162 0.8275 0.6232 0.0203 -0.1516 -0.0113 597 TRP A CB 4548 C CG . TRP A 583 ? 0.4791 0.8718 0.6789 0.0084 -0.1448 -0.0079 597 TRP A CG 4549 C CD1 . TRP A 583 ? 0.5135 0.9150 0.7033 -0.0060 -0.1327 -0.0078 597 TRP A CD1 4550 C CD2 . TRP A 583 ? 0.5189 0.8808 0.7223 0.0101 -0.1505 -0.0044 597 TRP A CD2 4551 N NE1 . TRP A 583 ? 0.5025 0.8807 0.6896 -0.0131 -0.1304 -0.0043 597 TRP A NE1 4552 C CE2 . TRP A 583 ? 0.5075 0.8615 0.7027 -0.0036 -0.1411 -0.0021 597 TRP A CE2 4553 C CE3 . TRP A 583 ? 0.5287 0.8682 0.7425 0.0218 -0.1636 -0.0028 597 TRP A CE3 4554 C CZ2 . TRP A 583 ? 0.5302 0.8559 0.7274 -0.0060 -0.1440 0.0019 597 TRP A CZ2 4555 C CZ3 . TRP A 583 ? 0.5421 0.8534 0.7578 0.0191 -0.1667 0.0011 597 TRP A CZ3 4556 C CH2 . TRP A 583 ? 0.5414 0.8463 0.7488 0.0053 -0.1567 0.0036 597 TRP A CH2 4557 N N . ILE A 584 ? 0.3334 0.7941 0.5498 0.0312 -0.1591 -0.0093 598 ILE A N 4558 C CA . ILE A 584 ? 0.4210 0.8997 0.6485 0.0453 -0.1677 -0.0149 598 ILE A CA 4559 C C . ILE A 584 ? 0.4532 0.9440 0.6811 0.0429 -0.1710 -0.0050 598 ILE A C 4560 O O . ILE A 584 ? 0.4376 0.9514 0.6591 0.0343 -0.1634 -0.0059 598 ILE A O 4561 C CB . ILE A 584 ? 0.3366 0.8448 0.5654 0.0496 -0.1617 -0.0310 598 ILE A CB 4562 C CG1 . ILE A 584 ? 0.4008 0.8988 0.6271 0.0522 -0.1586 -0.0412 598 ILE A CG1 4563 C CG2 . ILE A 584 ? 0.3461 0.8716 0.5889 0.0660 -0.1713 -0.0379 598 ILE A CG2 4564 C CD1 . ILE A 584 ? 0.3743 0.9020 0.6031 0.0591 -0.1539 -0.0571 598 ILE A CD1 4565 N N . THR A 585 ? 0.5082 0.9838 0.7441 0.0508 -0.1834 0.0045 599 THR A N 4566 C CA . THR A 585 ? 0.5146 0.9981 0.7497 0.0484 -0.1880 0.0163 599 THR A CA 4567 C C . THR A 585 ? 0.5317 1.0416 0.7768 0.0589 -0.1947 0.0101 599 THR A C 4568 O O . THR A 585 ? 0.5713 1.0803 0.8307 0.0744 -0.2048 0.0033 599 THR A O 4569 C CB . THR A 585 ? 0.5344 0.9903 0.7744 0.0517 -0.1992 0.0314 599 THR A CB 4570 O OG1 . THR A 585 ? 0.5427 0.9746 0.7752 0.0418 -0.1932 0.0384 599 THR A OG1 4571 C CG2 . THR A 585 ? 0.5555 1.0203 0.7924 0.0483 -0.2036 0.0446 599 THR A CG2 4572 N N . TYR A 586 ? 0.5041 1.0371 0.7425 0.0508 -0.1899 0.0124 600 TYR A N 4573 C CA . TYR A 586 ? 0.5031 1.0617 0.7510 0.0590 -0.1970 0.0093 600 TYR A CA 4574 C C . TYR A 586 ? 0.5283 1.0786 0.7771 0.0603 -0.2083 0.0249 600 TYR A C 4575 O O . TYR A 586 ? 0.4737 1.0308 0.7360 0.0727 -0.2209 0.0255 600 TYR A O 4576 C CB . TYR A 586 ? 0.5066 1.0953 0.7470 0.0485 -0.1865 0.0037 600 TYR A CB 4577 C CG . TYR A 586 ? 0.5048 1.1139 0.7494 0.0502 -0.1780 -0.0123 600 TYR A CG 4578 C CD1 . TYR A 586 ? 0.5178 1.1302 0.7763 0.0658 -0.1828 -0.0235 600 TYR A CD1 4579 C CD2 . TYR A 586 ? 0.4837 1.1099 0.7185 0.0361 -0.1654 -0.0160 600 TYR A CD2 4580 C CE1 . TYR A 586 ? 0.5039 1.1377 0.7649 0.0672 -0.1740 -0.0377 600 TYR A CE1 4581 C CE2 . TYR A 586 ? 0.4602 1.1064 0.6986 0.0366 -0.1574 -0.0288 600 TYR A CE2 4582 C CZ . TYR A 586 ? 0.4458 1.0967 0.6967 0.0520 -0.1612 -0.0394 600 TYR A CZ 4583 O OH . TYR A 586 ? 0.3738 1.0416 0.6251 0.0517 -0.1514 -0.0511 600 TYR A OH 4584 N N . ALA A 587 ? 0.5419 1.0785 0.7761 0.0474 -0.2038 0.0378 601 ALA A N 4585 C CA . ALA A 587 ? 0.5254 1.0530 0.7568 0.0463 -0.2128 0.0547 601 ALA A CA 4586 C C . ALA A 587 ? 0.5328 1.0403 0.7490 0.0329 -0.2053 0.0668 601 ALA A C 4587 O O . ALA A 587 ? 0.5253 1.0335 0.7303 0.0218 -0.1919 0.0619 601 ALA A O 4588 C CB . ALA A 587 ? 0.4766 1.0306 0.7044 0.0438 -0.2152 0.0564 601 ALA A CB 4589 N N . SER A 588 ? 0.5064 0.9966 0.7231 0.0340 -0.2140 0.0831 602 SER A N 4590 C CA . SER A 588 ? 0.5356 1.0095 0.7388 0.0219 -0.2071 0.0961 602 SER A CA 4591 C C . SER A 588 ? 0.5831 1.0530 0.7835 0.0217 -0.2168 0.1149 602 SER A C 4592 O O . SER A 588 ? 0.5784 1.0512 0.7907 0.0323 -0.2310 0.1187 602 SER A O 4593 C CB . SER A 588 ? 0.5355 0.9821 0.7447 0.0228 -0.2054 0.0966 602 SER A CB 4594 O OG . SER A 588 ? 0.5515 0.9835 0.7785 0.0364 -0.2202 0.0991 602 SER A OG 4595 N N . GLY A 589 ? 0.6231 1.0871 0.8080 0.0097 -0.2092 0.1268 603 GLY A N 4596 C CA . GLY A 589 ? 0.6757 1.1368 0.8554 0.0079 -0.2169 0.1461 603 GLY A CA 4597 C C . GLY A 589 ? 0.6935 1.1547 0.8526 -0.0062 -0.2053 0.1559 603 GLY A C 4598 O O . GLY A 589 ? 0.6663 1.1236 0.8176 -0.0146 -0.1915 0.1493 603 GLY A O 4599 N N . HIS A 590 ? 0.7256 1.1915 0.8760 -0.0085 -0.2112 0.1718 604 HIS A N 4600 C CA . HIS A 590 ? 0.7198 1.1880 0.8497 -0.0209 -0.2008 0.1819 604 HIS A CA 4601 C C . HIS A 590 ? 0.6915 1.1849 0.8032 -0.0270 -0.1958 0.1744 604 HIS A C 4602 O O . HIS A 590 ? 0.6825 1.1920 0.7983 -0.0212 -0.2039 0.1674 604 HIS A O 4603 C CB . HIS A 590 ? 0.7405 1.1989 0.8698 -0.0209 -0.2097 0.2054 604 HIS A CB 4604 C CG . HIS A 590 ? 0.7967 1.2295 0.9450 -0.0157 -0.2162 0.2143 604 HIS A CG 4605 N ND1 . HIS A 590 ? 0.8207 1.2369 0.9726 -0.0199 -0.2061 0.2112 604 HIS A ND1 4606 C CD2 . HIS A 590 ? 0.8320 1.2520 0.9974 -0.0067 -0.2328 0.2263 604 HIS A CD2 4607 C CE1 . HIS A 590 ? 0.8414 1.2360 1.0116 -0.0139 -0.2162 0.2206 604 HIS A CE1 4608 N NE2 . HIS A 590 ? 0.8576 1.2536 1.0365 -0.0058 -0.2326 0.2298 604 HIS A NE2 4609 N N . ALA A 591 ? 0.6703 1.1668 0.7628 -0.0384 -0.1826 0.1756 605 ALA A N 4610 C CA . ALA A 591 ? 0.6422 1.1605 0.7156 -0.0453 -0.1775 0.1685 605 ALA A CA 4611 C C . ALA A 591 ? 0.6300 1.1472 0.6827 -0.0560 -0.1659 0.1763 605 ALA A C 4612 O O . ALA A 591 ? 0.5742 1.0755 0.6288 -0.0596 -0.1572 0.1803 605 ALA A O 4613 C CB . ALA A 591 ? 0.6468 1.1746 0.7230 -0.0470 -0.1702 0.1471 605 ALA A CB 4614 N N . ASP A 592 ? 0.6984 1.2333 0.7315 -0.0608 -0.1661 0.1779 606 ASP A N 4615 C CA . ASP A 592 ? 0.7279 1.2654 0.7388 -0.0704 -0.1550 0.1835 606 ASP A CA 4616 C C . ASP A 592 ? 0.6374 1.1771 0.6410 -0.0780 -0.1401 0.1655 606 ASP A C 4617 O O . ASP A 592 ? 0.6087 1.1644 0.5982 -0.0827 -0.1375 0.1545 606 ASP A O 4618 C CB . ASP A 592 ? 0.8362 1.3922 0.8274 -0.0723 -0.1616 0.1907 606 ASP A CB 4619 C CG . ASP A 592 ? 0.9502 1.5076 0.9194 -0.0800 -0.1527 0.2024 606 ASP A CG 4620 O OD1 . ASP A 592 ? 0.9943 1.5388 0.9680 -0.0796 -0.1520 0.2194 606 ASP A OD1 4621 O OD2 . ASP A 592 ? 0.9965 1.5684 0.9441 -0.0863 -0.1465 0.1946 606 ASP A OD2 4622 N N . VAL A 593 ? 0.5661 1.0889 0.5805 -0.0793 -0.1313 0.1628 607 VAL A N 4623 C CA . VAL A 593 ? 0.5350 1.0569 0.5465 -0.0859 -0.1183 0.1463 607 VAL A CA 4624 C C . VAL A 593 ? 0.5047 1.0117 0.5144 -0.0911 -0.1060 0.1521 607 VAL A C 4625 O O . VAL A 593 ? 0.4851 0.9758 0.5081 -0.0878 -0.1078 0.1635 607 VAL A O 4626 C CB . VAL A 593 ? 0.5503 1.0686 0.5806 -0.0819 -0.1205 0.1324 607 VAL A CB 4627 C CG1 . VAL A 593 ? 0.5584 1.0714 0.5882 -0.0891 -0.1074 0.1185 607 VAL A CG1 4628 C CG2 . VAL A 593 ? 0.5452 1.0825 0.5765 -0.0781 -0.1303 0.1241 607 VAL A CG2 4629 N N . THR A 594 ? 0.5056 1.0184 0.5001 -0.0991 -0.0941 0.1440 608 THR A N 4630 C CA . THR A 594 ? 0.5089 1.0100 0.5022 -0.1042 -0.0812 0.1473 608 THR A CA 4631 C C . THR A 594 ? 0.5466 1.0474 0.5385 -0.1103 -0.0707 0.1283 608 THR A C 4632 O O . THR A 594 ? 0.5577 1.0678 0.5489 -0.1111 -0.0737 0.1141 608 THR A O 4633 C CB . THR A 594 ? 0.6104 1.1196 0.5841 -0.1077 -0.0764 0.1602 608 THR A CB 4634 O OG1 . THR A 594 ? 0.6553 1.1526 0.6328 -0.1111 -0.0651 0.1669 608 THR A OG1 4635 C CG2 . THR A 594 ? 0.5568 1.0841 0.5079 -0.1128 -0.0720 0.1482 608 THR A CG2 4636 N N . ALA A 595 ? 0.5468 1.0370 0.5399 -0.1148 -0.0588 0.1284 609 ALA A N 4637 C CA . ALA A 595 ? 0.5150 1.0037 0.5072 -0.1209 -0.0490 0.1112 609 ALA A CA 4638 C C . ALA A 595 ? 0.5138 1.0182 0.4837 -0.1260 -0.0432 0.1035 609 ALA A C 4639 O O . ALA A 595 ? 0.5030 1.0164 0.4575 -0.1257 -0.0429 0.1138 609 ALA A O 4640 C CB . ALA A 595 ? 0.4786 0.9499 0.4826 -0.1231 -0.0394 0.1140 609 ALA A CB 4641 N N . LYS A 596 ? 0.4785 0.9857 0.4466 -0.1309 -0.0392 0.0857 610 LYS A N 4642 C CA . LYS A 596 ? 0.5142 1.0339 0.4624 -0.1359 -0.0339 0.0751 610 LYS A CA 4643 C C . LYS A 596 ? 0.5433 1.0814 0.4738 -0.1344 -0.0426 0.0772 610 LYS A C 4644 O O . LYS A 596 ? 0.5669 1.1152 0.4770 -0.1363 -0.0388 0.0780 610 LYS A O 4645 C CB . LYS A 596 ? 0.5585 1.0744 0.4987 -0.1384 -0.0211 0.0790 610 LYS A CB 4646 C CG . LYS A 596 ? 0.5769 1.0749 0.5353 -0.1403 -0.0126 0.0761 610 LYS A CG 4647 C CD . LYS A 596 ? 0.6051 1.1005 0.5589 -0.1414 -0.0006 0.0833 610 LYS A CD 4648 C CE . LYS A 596 ? 0.6345 1.1109 0.6098 -0.1420 0.0054 0.0857 610 LYS A CE 4649 N NZ . LYS A 596 ? 0.6978 1.1732 0.6716 -0.1420 0.0155 0.0980 610 LYS A NZ 4650 N N . ARG A 597 ? 0.5570 1.1000 0.4955 -0.1308 -0.0545 0.0778 611 ARG A N 4651 C CA . ARG A 597 ? 0.6079 1.1689 0.5326 -0.1295 -0.0644 0.0782 611 ARG A CA 4652 C C . ARG A 597 ? 0.5663 1.1336 0.5023 -0.1296 -0.0726 0.0662 611 ARG A C 4653 O O . ARG A 597 ? 0.5616 1.1208 0.5176 -0.1265 -0.0751 0.0664 611 ARG A O 4654 C CB . ARG A 597 ? 0.6920 1.2548 0.6156 -0.1232 -0.0725 0.0979 611 ARG A CB 4655 C CG . ARG A 597 ? 0.8102 1.3917 0.7161 -0.1222 -0.0824 0.1008 611 ARG A CG 4656 C CD . ARG A 597 ? 0.8935 1.4760 0.7931 -0.1179 -0.0876 0.1224 611 ARG A CD 4657 N NE . ARG A 597 ? 0.9574 1.5337 0.8479 -0.1206 -0.0757 0.1316 611 ARG A NE 4658 C CZ . ARG A 597 ? 0.9917 1.5654 0.8803 -0.1181 -0.0772 0.1521 611 ARG A CZ 4659 N NH1 . ARG A 597 ? 0.9944 1.5695 0.8895 -0.1127 -0.0909 0.1656 611 ARG A NH1 4660 N NH2 . ARG A 597 ? 1.0046 1.5747 0.8859 -0.1212 -0.0652 0.1597 611 ARG A NH2 4661 N N . TRP A 598 ? 0.5454 1.1278 0.4691 -0.1333 -0.0765 0.0554 612 TRP A N 4662 C CA . TRP A 598 ? 0.5264 1.1182 0.4606 -0.1343 -0.0845 0.0445 612 TRP A CA 4663 C C . TRP A 598 ? 0.5297 1.1318 0.4708 -0.1272 -0.0977 0.0532 612 TRP A C 4664 O O . TRP A 598 ? 0.5661 1.1783 0.4935 -0.1248 -0.1044 0.0614 612 TRP A O 4665 C CB . TRP A 598 ? 0.5470 1.1509 0.4668 -0.1413 -0.0850 0.0297 612 TRP A CB 4666 C CG . TRP A 598 ? 0.5491 1.1427 0.4727 -0.1482 -0.0751 0.0165 612 TRP A CG 4667 C CD1 . TRP A 598 ? 0.5426 1.1300 0.4531 -0.1521 -0.0652 0.0114 612 TRP A CD1 4668 C CD2 . TRP A 598 ? 0.4626 1.0509 0.4055 -0.1516 -0.0741 0.0072 612 TRP A CD2 4669 N NE1 . TRP A 598 ? 0.5021 1.0794 0.4237 -0.1576 -0.0590 -0.0008 612 TRP A NE1 4670 C CE2 . TRP A 598 ? 0.4633 1.0410 0.4044 -0.1579 -0.0645 -0.0029 612 TRP A CE2 4671 C CE3 . TRP A 598 ? 0.4137 1.0064 0.3754 -0.1499 -0.0804 0.0065 612 TRP A CE3 4672 C CZ2 . TRP A 598 ? 0.4454 1.0154 0.4029 -0.1632 -0.0618 -0.0123 612 TRP A CZ2 4673 C CZ3 . TRP A 598 ? 0.4510 1.0377 0.4275 -0.1552 -0.0768 -0.0029 612 TRP A CZ3 4674 C CH2 . TRP A 598 ? 0.4619 1.0368 0.4362 -0.1621 -0.0680 -0.0116 612 TRP A CH2 4675 N N . TYR A 599 ? 0.5024 1.1024 0.4648 -0.1236 -0.1015 0.0516 613 TYR A N 4676 C CA . TYR A 599 ? 0.5050 1.1158 0.4769 -0.1161 -0.1140 0.0576 613 TYR A CA 4677 C C . TYR A 599 ? 0.5163 1.1408 0.5007 -0.1177 -0.1188 0.0449 613 TYR A C 4678 O O . TYR A 599 ? 0.5534 1.1733 0.5470 -0.1225 -0.1123 0.0348 613 TYR A O 4679 C CB . TYR A 599 ? 0.4878 1.0848 0.4758 -0.1076 -0.1156 0.0689 613 TYR A CB 4680 C CG . TYR A 599 ? 0.4841 1.0679 0.4639 -0.1057 -0.1123 0.0840 613 TYR A CG 4681 C CD1 . TYR A 599 ? 0.4933 1.0838 0.4613 -0.1024 -0.1198 0.0972 613 TYR A CD1 4682 C CD2 . TYR A 599 ? 0.4348 1.0001 0.4193 -0.1075 -0.1020 0.0860 613 TYR A CD2 4683 C CE1 . TYR A 599 ? 0.5060 1.0856 0.4672 -0.1015 -0.1166 0.1125 613 TYR A CE1 4684 C CE2 . TYR A 599 ? 0.4789 1.0334 0.4579 -0.1063 -0.0987 0.1005 613 TYR A CE2 4685 C CZ . TYR A 599 ? 0.4989 1.0608 0.4663 -0.1034 -0.1057 0.1140 613 TYR A CZ 4686 O OH . TYR A 599 ? 0.5117 1.0640 0.4744 -0.1030 -0.1021 0.1299 613 TYR A OH 4687 N N . THR A 600 ? 0.5241 1.1662 0.5097 -0.1142 -0.1304 0.0461 614 THR A N 4688 C CA . THR A 600 ? 0.5131 1.1698 0.5151 -0.1143 -0.1353 0.0363 614 THR A CA 4689 C C . THR A 600 ? 0.5062 1.1620 0.5291 -0.1040 -0.1402 0.0415 614 THR A C 4690 O O . THR A 600 ? 0.5341 1.1916 0.5585 -0.0955 -0.1490 0.0522 614 THR A O 4691 C CB . THR A 600 ? 0.4998 1.1704 0.4952 -0.1153 -0.1426 0.0320 614 THR A CB 4692 O OG1 . THR A 600 ? 0.4906 1.1622 0.4670 -0.1247 -0.1386 0.0249 614 THR A OG1 4693 C CG2 . THR A 600 ? 0.4540 1.1286 0.4682 -0.1138 -0.1426 0.0226 614 THR A CG2 4694 N N . LEU A 601 ? 0.4388 1.0917 0.4776 -0.1046 -0.1349 0.0339 615 LEU A N 4695 C CA . LEU A 601 ? 0.4542 1.1058 0.5126 -0.0944 -0.1383 0.0357 615 LEU A CA 4696 C C . LEU A 601 ? 0.4617 1.1227 0.5320 -0.0915 -0.1394 0.0268 615 LEU A C 4697 O O . LEU A 601 ? 0.3716 1.0348 0.4418 -0.0992 -0.1331 0.0171 615 LEU A O 4698 C CB . LEU A 601 ? 0.4448 1.0794 0.5116 -0.0947 -0.1295 0.0341 615 LEU A CB 4699 C CG . LEU A 601 ? 0.4345 1.0452 0.4961 -0.0915 -0.1260 0.0449 615 LEU A CG 4700 C CD1 . LEU A 601 ? 0.3525 0.9462 0.4233 -0.0926 -0.1174 0.0413 615 LEU A CD1 4701 C CD2 . LEU A 601 ? 0.4200 1.0290 0.4876 -0.0798 -0.1364 0.0562 615 LEU A CD2 4702 N N . THR A 602 ? 0.3807 1.0473 0.4621 -0.0805 -0.1479 0.0306 616 THR A N 4703 C CA . THR A 602 ? 0.4759 1.1531 0.5716 -0.0765 -0.1489 0.0227 616 THR A CA 4704 C C . THR A 602 ? 0.4345 1.1100 0.5487 -0.0650 -0.1507 0.0227 616 THR A C 4705 O O . THR A 602 ? 0.4173 1.0867 0.5350 -0.0563 -0.1576 0.0311 616 THR A O 4706 C CB . THR A 602 ? 0.4876 1.1770 0.5808 -0.0741 -0.1581 0.0245 616 THR A CB 4707 O OG1 . THR A 602 ? 0.5018 1.1915 0.5756 -0.0839 -0.1573 0.0248 616 THR A OG1 4708 C CG2 . THR A 602 ? 0.4640 1.1661 0.5715 -0.0728 -0.1575 0.0156 616 THR A CG2 4709 N N . LEU A 603 ? 0.3941 1.0746 0.5196 -0.0651 -0.1446 0.0134 617 LEU A N 4710 C CA . LEU A 603 ? 0.3679 1.0489 0.5102 -0.0542 -0.1455 0.0109 617 LEU A CA 4711 C C . LEU A 603 ? 0.3718 1.0700 0.5267 -0.0504 -0.1459 0.0036 617 LEU A C 4712 O O . LEU A 603 ? 0.3716 1.0760 0.5254 -0.0590 -0.1384 -0.0029 617 LEU A O 4713 C CB . LEU A 603 ? 0.3760 1.0460 0.5189 -0.0584 -0.1358 0.0071 617 LEU A CB 4714 C CG . LEU A 603 ? 0.4199 1.0911 0.5782 -0.0485 -0.1348 0.0022 617 LEU A CG 4715 C CD1 . LEU A 603 ? 0.4133 1.0805 0.5803 -0.0345 -0.1457 0.0081 617 LEU A CD1 4716 C CD2 . LEU A 603 ? 0.4325 1.0920 0.5889 -0.0545 -0.1253 -0.0012 617 LEU A CD2 4717 N N . GLY A 604 ? 0.4063 1.1121 0.5737 -0.0378 -0.1551 0.0052 618 GLY A N 4718 C CA . GLY A 604 ? 0.3850 1.1091 0.5666 -0.0331 -0.1560 -0.0014 618 GLY A CA 4719 C C . GLY A 604 ? 0.4070 1.1347 0.6049 -0.0216 -0.1549 -0.0069 618 GLY A C 4720 O O . GLY A 604 ? 0.4370 1.1568 0.6413 -0.0104 -0.1619 -0.0036 618 GLY A O 4721 N N . ILE A 605 ? 0.3967 1.1365 0.6013 -0.0241 -0.1463 -0.0152 619 ILE A N 4722 C CA . ILE A 605 ? 0.3887 1.1346 0.6074 -0.0131 -0.1445 -0.0216 619 ILE A CA 4723 C C . ILE A 605 ? 0.4055 1.1756 0.6382 -0.0090 -0.1438 -0.0278 619 ILE A C 4724 O O . ILE A 605 ? 0.3988 1.1795 0.6290 -0.0194 -0.1369 -0.0303 619 ILE A O 4725 C CB . ILE A 605 ? 0.3332 1.0710 0.5465 -0.0190 -0.1333 -0.0257 619 ILE A CB 4726 C CG1 . ILE A 605 ? 0.3290 1.0440 0.5280 -0.0261 -0.1327 -0.0193 619 ILE A CG1 4727 C CG2 . ILE A 605 ? 0.3310 1.0724 0.5569 -0.0057 -0.1336 -0.0318 619 ILE A CG2 4728 C CD1 . ILE A 605 ? 0.3175 1.0230 0.5105 -0.0341 -0.1220 -0.0226 619 ILE A CD1 4729 N N . LYS A 606 ? 0.4030 1.1815 0.6516 0.0063 -0.1513 -0.0301 620 LYS A N 4730 C CA . LYS A 606 ? 0.4122 1.2151 0.6765 0.0121 -0.1516 -0.0359 620 LYS A CA 4731 C C . LYS A 606 ? 0.4008 1.2104 0.6817 0.0295 -0.1544 -0.0426 620 LYS A C 4732 O O . LYS A 606 ? 0.4116 1.2111 0.6989 0.0413 -0.1655 -0.0396 620 LYS A O 4733 C CB . LYS A 606 ? 0.4706 1.2798 0.7381 0.0123 -0.1619 -0.0305 620 LYS A CB 4734 C CG . LYS A 606 ? 0.5135 1.3483 0.7989 0.0182 -0.1635 -0.0356 620 LYS A CG 4735 C CD . LYS A 606 ? 0.5492 1.3875 0.8381 0.0193 -0.1759 -0.0294 620 LYS A CD 4736 C CE . LYS A 606 ? 0.5738 1.4383 0.8792 0.0210 -0.1761 -0.0338 620 LYS A CE 4737 N NZ . LYS A 606 ? 0.6258 1.4936 0.9336 0.0204 -0.1885 -0.0276 620 LYS A NZ 4738 N N . GLY A 607 ? 0.4020 1.2283 0.6896 0.0311 -0.1448 -0.0514 621 GLY A N 4739 C CA . GLY A 607 ? 0.3613 1.1954 0.6632 0.0476 -0.1459 -0.0598 621 GLY A CA 4740 C C . GLY A 607 ? 0.3595 1.1703 0.6576 0.0551 -0.1504 -0.0593 621 GLY A C 4741 O O . GLY A 607 ? 0.3936 1.1901 0.6781 0.0463 -0.1441 -0.0577 621 GLY A O 4742 N N . TYR A 608 ? 0.4649 1.2709 0.7761 0.0714 -0.1621 -0.0601 622 TYR A N 4743 C CA . TYR A 608 ? 0.4962 1.2793 0.8072 0.0807 -0.1690 -0.0594 622 TYR A CA 4744 C C . TYR A 608 ? 0.5388 1.2974 0.8388 0.0743 -0.1772 -0.0462 622 TYR A C 4745 O O . TYR A 608 ? 0.5581 1.2959 0.8567 0.0796 -0.1828 -0.0434 622 TYR A O 4746 C CB . TYR A 608 ? 0.5452 1.3315 0.8761 0.1011 -0.1798 -0.0651 622 TYR A CB 4747 C CG . TYR A 608 ? 0.6120 1.4172 0.9528 0.1115 -0.1724 -0.0800 622 TYR A CG 4748 C CD1 . TYR A 608 ? 0.6389 1.4345 0.9768 0.1177 -0.1692 -0.0876 622 TYR A CD1 4749 C CD2 . TYR A 608 ? 0.6278 1.4614 0.9809 0.1155 -0.1687 -0.0865 622 TYR A CD2 4750 C CE1 . TYR A 608 ? 0.6660 1.4803 1.0112 0.1276 -0.1623 -0.1020 622 TYR A CE1 4751 C CE2 . TYR A 608 ? 0.6598 1.5130 1.0210 0.1253 -0.1612 -0.1003 622 TYR A CE2 4752 C CZ . TYR A 608 ? 0.6753 1.5190 1.0318 0.1315 -0.1579 -0.1083 622 TYR A CZ 4753 O OH . TYR A 608 ? 0.6840 1.5484 1.0470 0.1416 -0.1504 -0.1228 622 TYR A OH 4754 N N . PHE A 609 ? 0.5531 1.3145 0.8451 0.0630 -0.1780 -0.0381 623 PHE A N 4755 C CA . PHE A 609 ? 0.5509 1.2931 0.8340 0.0594 -0.1876 -0.0254 623 PHE A CA 4756 C C . PHE A 609 ? 0.5064 1.2410 0.7689 0.0413 -0.1808 -0.0184 623 PHE A C 4757 O O . PHE A 609 ? 0.5034 1.2503 0.7595 0.0300 -0.1717 -0.0214 623 PHE A O 4758 C CB . PHE A 609 ? 0.5703 1.3183 0.8646 0.0673 -0.2009 -0.0204 623 PHE A CB 4759 C CG . PHE A 609 ? 0.6121 1.3588 0.9263 0.0862 -0.2111 -0.0245 623 PHE A CG 4760 C CD1 . PHE A 609 ? 0.6055 1.3296 0.9223 0.0945 -0.2228 -0.0172 623 PHE A CD1 4761 C CD2 . PHE A 609 ? 0.6427 1.4104 0.9737 0.0959 -0.2087 -0.0357 623 PHE A CD2 4762 C CE1 . PHE A 609 ? 0.6224 1.3426 0.9583 0.1122 -0.2329 -0.0214 623 PHE A CE1 4763 C CE2 . PHE A 609 ? 0.6586 1.4244 1.0083 0.1142 -0.2178 -0.0408 623 PHE A CE2 4764 C CZ . PHE A 609 ? 0.6532 1.3940 1.0055 0.1223 -0.2303 -0.0338 623 PHE A CZ 4765 N N . ALA A 610 ? 0.4734 1.1872 0.7260 0.0389 -0.1857 -0.0089 624 ALA A N 4766 C CA . ALA A 610 ? 0.5011 1.2067 0.7341 0.0231 -0.1804 -0.0019 624 ALA A CA 4767 C C . ALA A 610 ? 0.5219 1.2175 0.7474 0.0226 -0.1914 0.0112 624 ALA A C 4768 O O . ALA A 610 ? 0.5274 1.2167 0.7628 0.0345 -0.2037 0.0166 624 ALA A O 4769 C CB . ALA A 610 ? 0.4511 1.1422 0.6756 0.0172 -0.1720 -0.0028 624 ALA A CB 4770 N N . PHE A 611 ? 0.5072 1.2015 0.7152 0.0088 -0.1870 0.0162 625 PHE A N 4771 C CA . PHE A 611 ? 0.4883 1.1734 0.6843 0.0059 -0.1950 0.0291 625 PHE A CA 4772 C C . PHE A 611 ? 0.4471 1.1259 0.6229 -0.0095 -0.1854 0.0316 625 PHE A C 4773 O O . PHE A 611 ? 0.4196 1.1049 0.5910 -0.0188 -0.1747 0.0232 625 PHE A O 4774 C CB . PHE A 611 ? 0.4509 1.1482 0.6487 0.0080 -0.2042 0.0321 625 PHE A CB 4775 C CG . PHE A 611 ? 0.4601 1.1699 0.6469 -0.0045 -0.1975 0.0276 625 PHE A CG 4776 C CD1 . PHE A 611 ? 0.4885 1.1936 0.6546 -0.0159 -0.1961 0.0340 625 PHE A CD1 4777 C CD2 . PHE A 611 ? 0.4872 1.2138 0.6849 -0.0044 -0.1932 0.0173 625 PHE A CD2 4778 C CE1 . PHE A 611 ? 0.5046 1.2200 0.6614 -0.0268 -0.1911 0.0291 625 PHE A CE1 4779 C CE2 . PHE A 611 ? 0.4999 1.2368 0.6890 -0.0159 -0.1882 0.0139 625 PHE A CE2 4780 C CZ . PHE A 611 ? 0.4996 1.2300 0.6685 -0.0269 -0.1877 0.0193 625 PHE A CZ 4781 N N . GLY A 612 ? 0.4439 1.1102 0.6080 -0.0123 -0.1892 0.0435 626 GLY A N 4782 C CA . GLY A 612 ? 0.4463 1.1076 0.5911 -0.0263 -0.1808 0.0463 626 GLY A CA 4783 C C . GLY A 612 ? 0.4696 1.1316 0.5984 -0.0306 -0.1870 0.0572 626 GLY A C 4784 O O . GLY A 612 ? 0.4413 1.0994 0.5727 -0.0228 -0.1983 0.0681 626 GLY A O 4785 N N . MET A 613 ? 0.4754 1.1420 0.5876 -0.0430 -0.1802 0.0544 627 MET A N 4786 C CA . MET A 613 ? 0.5248 1.1923 0.6185 -0.0479 -0.1849 0.0641 627 MET A CA 4787 C C . MET A 613 ? 0.5320 1.1919 0.6079 -0.0586 -0.1768 0.0679 627 MET A C 4788 O O . MET A 613 ? 0.4845 1.1418 0.5597 -0.0658 -0.1663 0.0592 627 MET A O 4789 C CB . MET A 613 ? 0.5275 1.2087 0.6156 -0.0520 -0.1868 0.0580 627 MET A CB 4790 C CG . MET A 613 ? 0.5328 1.2224 0.6358 -0.0413 -0.1980 0.0586 627 MET A CG 4791 S SD . MET A 613 ? 0.8102 1.5152 0.9058 -0.0468 -0.2019 0.0537 627 MET A SD 4792 C CE . MET A 613 ? 0.4875 1.1985 0.5862 -0.0566 -0.1884 0.0379 627 MET A CE 4793 N N . LEU A 614 ? 0.5271 1.1836 0.5887 -0.0595 -0.1819 0.0814 628 LEU A N 4794 C CA . LEU A 614 ? 0.5254 1.1715 0.5671 -0.0689 -0.1727 0.0854 628 LEU A CA 4795 C C . LEU A 614 ? 0.5898 1.2495 0.6108 -0.0748 -0.1770 0.0880 628 LEU A C 4796 O O . LEU A 614 ? 0.6210 1.2845 0.6386 -0.0696 -0.1877 0.0986 628 LEU A O 4797 C CB . LEU A 614 ? 0.5295 1.1538 0.5713 -0.0642 -0.1724 0.1001 628 LEU A CB 4798 C CG . LEU A 614 ? 0.5252 1.1345 0.5501 -0.0725 -0.1604 0.1045 628 LEU A CG 4799 C CD1 . LEU A 614 ? 0.4730 1.0761 0.5009 -0.0790 -0.1475 0.0909 628 LEU A CD1 4800 C CD2 . LEU A 614 ? 0.5437 1.1334 0.5721 -0.0676 -0.1618 0.1208 628 LEU A CD2 4801 N N . ASN A 615 ? 0.5796 1.2441 0.5868 -0.0852 -0.1688 0.0778 629 ASN A N 4802 C CA . ASN A 615 ? 0.5668 1.2407 0.5535 -0.0908 -0.1712 0.0767 629 ASN A CA 4803 C C . ASN A 615 ? 0.5766 1.2591 0.5691 -0.0852 -0.1816 0.0758 629 ASN A C 4804 O O . ASN A 615 ? 0.5840 1.2707 0.5615 -0.0853 -0.1881 0.0828 629 ASN A O 4805 C CB . ASN A 615 ? 0.5619 1.2306 0.5264 -0.0928 -0.1708 0.0905 629 ASN A CB 4806 C CG . ASN A 615 ? 0.5496 1.2016 0.5052 -0.0990 -0.1553 0.0880 629 ASN A CG 4807 O OD1 . ASN A 615 ? 0.5153 1.1657 0.4740 -0.1050 -0.1467 0.0741 629 ASN A OD1 4808 N ND2 . ASN A 615 ? 0.5391 1.1791 0.4850 -0.0978 -0.1520 0.1022 629 ASN A ND2 4809 N N . GLY A 616 ? 0.5597 1.2453 0.5739 -0.0803 -0.1829 0.0676 630 GLY A N 4810 C CA . GLY A 616 ? 0.5771 1.2722 0.5994 -0.0750 -0.1925 0.0659 630 GLY A CA 4811 C C . GLY A 616 ? 0.6215 1.3148 0.6541 -0.0634 -0.2045 0.0784 630 GLY A C 4812 O O . GLY A 616 ? 0.6421 1.3430 0.6838 -0.0577 -0.2137 0.0778 630 GLY A O 4813 N N . THR A 617 ? 0.6255 1.3080 0.6577 -0.0598 -0.2050 0.0900 631 THR A N 4814 C CA . THR A 617 ? 0.6263 1.3038 0.6701 -0.0485 -0.2169 0.1027 631 THR A CA 4815 C C . THR A 617 ? 0.5983 1.2683 0.6660 -0.0399 -0.2161 0.1002 631 THR A C 4816 O O . THR A 617 ? 0.5754 1.2380 0.6435 -0.0433 -0.2071 0.0981 631 THR A O 4817 C CB . THR A 617 ? 0.6404 1.3100 0.6667 -0.0502 -0.2202 0.1207 631 THR A CB 4818 O OG1 . THR A 617 ? 0.6396 1.3170 0.6436 -0.0565 -0.2225 0.1231 631 THR A OG1 4819 C CG2 . THR A 617 ? 0.6710 1.3317 0.7120 -0.0388 -0.2326 0.1346 631 THR A CG2 4820 N N . ILE A 618 ? 0.5935 1.2655 0.6811 -0.0285 -0.2259 0.0996 632 ILE A N 4821 C CA . ILE A 618 ? 0.5682 1.2336 0.6789 -0.0184 -0.2269 0.0961 632 ILE A CA 4822 C C . ILE A 618 ? 0.5709 1.2194 0.6823 -0.0159 -0.2276 0.1082 632 ILE A C 4823 O O . ILE A 618 ? 0.5516 1.1921 0.6574 -0.0137 -0.2362 0.1241 632 ILE A O 4824 C CB . ILE A 618 ? 0.5792 1.2491 0.7100 -0.0055 -0.2397 0.0955 632 ILE A CB 4825 C CG1 . ILE A 618 ? 0.5904 1.2777 0.7267 -0.0071 -0.2379 0.0821 632 ILE A CG1 4826 C CG2 . ILE A 618 ? 0.5679 1.2289 0.7211 0.0063 -0.2422 0.0930 632 ILE A CG2 4827 C CD1 . ILE A 618 ? 0.5926 1.2853 0.7441 -0.0055 -0.2283 0.0671 632 ILE A CD1 4828 N N . LEU A 619 ? 0.5149 1.1574 0.6335 -0.0167 -0.2188 0.1013 633 LEU A N 4829 C CA . LEU A 619 ? 0.5381 1.1641 0.6609 -0.0140 -0.2198 0.1117 633 LEU A CA 4830 C C . LEU A 619 ? 0.5569 1.1759 0.7047 0.0002 -0.2272 0.1082 633 LEU A C 4831 O O . LEU A 619 ? 0.5731 1.1759 0.7288 0.0074 -0.2360 0.1200 633 LEU A O 4832 C CB . LEU A 619 ? 0.5235 1.1377 0.6363 -0.0239 -0.2033 0.1057 633 LEU A CB 4833 C CG . LEU A 619 ? 0.5011 1.0878 0.6169 -0.0220 -0.2002 0.1145 633 LEU A CG 4834 C CD1 . LEU A 619 ? 0.4744 1.0515 0.5791 -0.0233 -0.2063 0.1340 633 LEU A CD1 4835 C CD2 . LEU A 619 ? 0.4781 1.0544 0.5862 -0.0314 -0.1842 0.1071 633 LEU A CD2 4836 N N . TRP A 620 ? 0.5391 1.1682 0.6990 0.0040 -0.2231 0.0916 634 TRP A N 4837 C CA . TRP A 620 ? 0.4974 1.1241 0.6807 0.0183 -0.2295 0.0847 634 TRP A CA 4838 C C . TRP A 620 ? 0.4757 1.1209 0.6680 0.0214 -0.2277 0.0698 634 TRP A C 4839 O O . TRP A 620 ? 0.4902 1.1471 0.6723 0.0111 -0.2177 0.0622 634 TRP A O 4840 C CB . TRP A 620 ? 0.4981 1.1136 0.6882 0.0196 -0.2231 0.0801 634 TRP A CB 4841 C CG . TRP A 620 ? 0.4813 1.1007 0.6603 0.0074 -0.2068 0.0699 634 TRP A CG 4842 C CD1 . TRP A 620 ? 0.4750 1.0833 0.6352 -0.0056 -0.1966 0.0746 634 TRP A CD1 4843 C CD2 . TRP A 620 ? 0.4819 1.1139 0.6678 0.0071 -0.1983 0.0535 634 TRP A CD2 4844 N NE1 . TRP A 620 ? 0.4528 1.0677 0.6093 -0.0139 -0.1840 0.0622 634 TRP A NE1 4845 C CE2 . TRP A 620 ? 0.4397 1.0713 0.6119 -0.0068 -0.1853 0.0501 634 TRP A CE2 4846 C CE3 . TRP A 620 ? 0.4877 1.1302 0.6899 0.0171 -0.1998 0.0416 634 TRP A CE3 4847 C CZ2 . TRP A 620 ? 0.4098 1.0492 0.5838 -0.0114 -0.1744 0.0363 634 TRP A CZ2 4848 C CZ3 . TRP A 620 ? 0.4725 1.1247 0.6756 0.0125 -0.1880 0.0283 634 TRP A CZ3 4849 C CH2 . TRP A 620 ? 0.4314 1.0814 0.6204 -0.0019 -0.1757 0.0263 634 TRP A CH2 4850 N N . LYS A 621 ? 0.4778 1.1256 0.6902 0.0355 -0.2376 0.0661 635 LYS A N 4851 C CA . LYS A 621 ? 0.4981 1.1649 0.7213 0.0393 -0.2376 0.0545 635 LYS A CA 4852 C C . LYS A 621 ? 0.4973 1.1658 0.7447 0.0548 -0.2425 0.0452 635 LYS A C 4853 O O . LYS A 621 ? 0.4927 1.1461 0.7501 0.0650 -0.2514 0.0501 635 LYS A O 4854 C CB . LYS A 621 ? 0.4499 1.1236 0.6699 0.0394 -0.2482 0.0623 635 LYS A CB 4855 N N . ASN A 622 ? 0.5114 1.1983 0.7685 0.0567 -0.2369 0.0322 636 ASN A N 4856 C CA . ASN A 622 ? 0.5845 1.2766 0.8634 0.0710 -0.2388 0.0213 636 ASN A CA 4857 C C . ASN A 622 ? 0.5895 1.2656 0.8727 0.0775 -0.2373 0.0184 636 ASN A C 4858 O O . ASN A 622 ? 0.5934 1.2624 0.8936 0.0922 -0.2470 0.0165 636 ASN A O 4859 C CB . ASN A 622 ? 0.6621 1.3578 0.9592 0.0842 -0.2543 0.0240 636 ASN A CB 4860 C CG . ASN A 622 ? 0.7519 1.4715 1.0554 0.0827 -0.2525 0.0176 636 ASN A CG 4861 O OD1 . ASN A 622 ? 0.7832 1.5158 1.0768 0.0714 -0.2400 0.0119 636 ASN A OD1 4862 N ND2 . ASN A 622 ? 0.7627 1.4875 1.0838 0.0939 -0.2657 0.0192 636 ASN A ND2 4863 N N . VAL A 623 ? 0.5794 1.2491 0.8478 0.0664 -0.2258 0.0180 637 VAL A N 4864 C CA . VAL A 623 ? 0.5724 1.2287 0.8442 0.0713 -0.2231 0.0137 637 VAL A CA 4865 C C . VAL A 623 ? 0.5600 1.2311 0.8390 0.0744 -0.2124 -0.0030 637 VAL A C 4866 O O . VAL A 623 ? 0.5330 1.2200 0.8046 0.0641 -0.2008 -0.0085 637 VAL A O 4867 C CB . VAL A 623 ? 0.5537 1.1954 0.8078 0.0584 -0.2166 0.0221 637 VAL A CB 4868 C CG1 . VAL A 623 ? 0.5235 1.1516 0.7821 0.0632 -0.2144 0.0173 637 VAL A CG1 4869 C CG2 . VAL A 623 ? 0.5577 1.1863 0.8051 0.0564 -0.2270 0.0395 637 VAL A CG2 4870 N N . ARG A 624 ? 0.5753 1.2416 0.8689 0.0890 -0.2170 -0.0108 638 ARG A N 4871 C CA . ARG A 624 ? 0.5953 1.2766 0.8954 0.0938 -0.2075 -0.0267 638 ARG A CA 4872 C C . ARG A 624 ? 0.5380 1.2165 0.8245 0.0824 -0.1939 -0.0306 638 ARG A C 4873 O O . ARG A 624 ? 0.4678 1.1262 0.7484 0.0805 -0.1956 -0.0258 638 ARG A O 4874 C CB . ARG A 624 ? 0.6485 1.3231 0.9663 0.1133 -0.2165 -0.0348 638 ARG A CB 4875 C CG . ARG A 624 ? 0.7308 1.4165 1.0663 0.1262 -0.2261 -0.0372 638 ARG A CG 4876 C CD . ARG A 624 ? 0.7982 1.4865 1.1491 0.1436 -0.2277 -0.0521 638 ARG A CD 4877 N NE . ARG A 624 ? 0.8252 1.5306 1.1702 0.1401 -0.2120 -0.0655 638 ARG A NE 4878 C CZ . ARG A 624 ? 0.8484 1.5623 1.2025 0.1533 -0.2092 -0.0809 638 ARG A CZ 4879 N NH1 . ARG A 624 ? 0.8804 1.5857 1.2509 0.1714 -0.2211 -0.0861 638 ARG A NH1 4880 N NH2 . ARG A 624 ? 0.8349 1.5660 1.1816 0.1481 -0.1947 -0.0911 638 ARG A NH2 4881 N N . VAL A 625 ? 0.5367 1.2351 0.8188 0.0745 -0.1809 -0.0385 639 VAL A N 4882 C CA . VAL A 625 ? 0.4995 1.1971 0.7706 0.0645 -0.1681 -0.0434 639 VAL A CA 4883 C C . VAL A 625 ? 0.4846 1.2004 0.7645 0.0730 -0.1616 -0.0580 639 VAL A C 4884 O O . VAL A 625 ? 0.4890 1.2210 0.7821 0.0840 -0.1651 -0.0638 639 VAL A O 4885 C CB . VAL A 625 ? 0.4688 1.1728 0.7251 0.0452 -0.1575 -0.0388 639 VAL A CB 4886 C CG1 . VAL A 625 ? 0.4609 1.1471 0.7058 0.0362 -0.1621 -0.0256 639 VAL A CG1 4887 C CG2 . VAL A 625 ? 0.4604 1.1883 0.7220 0.0439 -0.1551 -0.0418 639 VAL A CG2 4888 N N . LYS A 626 ? 0.4797 1.1940 0.7524 0.0682 -0.1523 -0.0638 640 LYS A N 4889 C CA . LYS A 626 ? 0.4959 1.2309 0.7743 0.0748 -0.1448 -0.0773 640 LYS A CA 4890 C C . LYS A 626 ? 0.4901 1.2513 0.7679 0.0660 -0.1352 -0.0787 640 LYS A C 4891 O O . LYS A 626 ? 0.4608 1.2206 0.7279 0.0497 -0.1298 -0.0709 640 LYS A O 4892 C CB . LYS A 626 ? 0.5057 1.2338 0.7756 0.0710 -0.1376 -0.0825 640 LYS A CB 4893 C CG . LYS A 626 ? 0.5626 1.2749 0.8396 0.0874 -0.1472 -0.0889 640 LYS A CG 4894 C CD . LYS A 626 ? 0.5893 1.2952 0.8575 0.0834 -0.1409 -0.0943 640 LYS A CD 4895 C CE . LYS A 626 ? 0.6039 1.3380 0.8708 0.0830 -0.1288 -0.1058 640 LYS A CE 4896 N NZ . LYS A 626 ? 0.5777 1.3150 0.8302 0.0629 -0.1163 -0.1010 640 LYS A NZ 4897 N N . TYR A 627 ? 0.4963 1.2808 0.7862 0.0773 -0.1336 -0.0888 641 TYR A N 4898 C CA . TYR A 627 ? 0.5187 1.3306 0.8108 0.0706 -0.1249 -0.0908 641 TYR A CA 4899 C C . TYR A 627 ? 0.5633 1.3992 0.8634 0.0814 -0.1184 -0.1044 641 TYR A C 4900 O O . TYR A 627 ? 0.5867 1.4206 0.8965 0.0989 -0.1249 -0.1129 641 TYR A O 4901 C CB . TYR A 627 ? 0.5153 1.3337 0.8173 0.0738 -0.1333 -0.0857 641 TYR A CB 4902 C CG . TYR A 627 ? 0.5016 1.3451 0.8052 0.0643 -0.1255 -0.0855 641 TYR A CG 4903 C CD1 . TYR A 627 ? 0.4976 1.3376 0.7880 0.0453 -0.1193 -0.0776 641 TYR A CD1 4904 C CD2 . TYR A 627 ? 0.4985 1.3686 0.8175 0.0747 -0.1247 -0.0933 641 TYR A CD2 4905 C CE1 . TYR A 627 ? 0.5104 1.3717 0.8030 0.0366 -0.1133 -0.0772 641 TYR A CE1 4906 C CE2 . TYR A 627 ? 0.5058 1.3989 0.8275 0.0657 -0.1182 -0.0923 641 TYR A CE2 4907 C CZ . TYR A 627 ? 0.5124 1.4005 0.8210 0.0466 -0.1129 -0.0840 641 TYR A CZ 4908 O OH . TYR A 627 ? 0.5204 1.4299 0.8325 0.0376 -0.1075 -0.0828 641 TYR A OH 4909 N N . PRO A 628 ? 0.5870 1.4452 0.8826 0.0711 -0.1057 -0.1067 642 PRO A N 4910 C CA . PRO A 628 ? 0.5953 1.4540 0.8793 0.0503 -0.0980 -0.0976 642 PRO A CA 4911 C C . PRO A 628 ? 0.5799 1.4154 0.8475 0.0373 -0.0941 -0.0922 642 PRO A C 4912 O O . PRO A 628 ? 0.5831 1.4102 0.8474 0.0425 -0.0934 -0.0972 642 PRO A O 4913 C CB . PRO A 628 ? 0.6138 1.5039 0.9006 0.0472 -0.0865 -0.1035 642 PRO A CB 4914 C CG . PRO A 628 ? 0.6104 1.5113 0.9026 0.0630 -0.0850 -0.1160 642 PRO A CG 4915 C CD . PRO A 628 ? 0.6105 1.4966 0.9134 0.0808 -0.0985 -0.1192 642 PRO A CD 4916 N N . GLY A 629 ? 0.5731 1.3978 0.8309 0.0210 -0.0923 -0.0823 643 GLY A N 4917 C CA . GLY A 629 ? 0.5306 1.3343 0.7733 0.0069 -0.0878 -0.0768 643 GLY A CA 4918 C C . GLY A 629 ? 0.5055 1.3109 0.7405 -0.0107 -0.0822 -0.0699 643 GLY A C 4919 O O . GLY A 629 ? 0.4853 1.2992 0.7255 -0.0113 -0.0859 -0.0671 643 GLY A O 4920 N N . HIS A 630 ? 0.4855 1.2826 0.7089 -0.0247 -0.0740 -0.0673 644 HIS A N 4921 C CA . HIS A 630 ? 0.4801 1.2744 0.6957 -0.0416 -0.0694 -0.0610 644 HIS A CA 4922 C C . HIS A 630 ? 0.4591 1.2276 0.6609 -0.0543 -0.0659 -0.0561 644 HIS A C 4923 O O . HIS A 630 ? 0.4430 1.2017 0.6417 -0.0515 -0.0645 -0.0581 644 HIS A O 4924 C CB . HIS A 630 ? 0.5018 1.3218 0.7212 -0.0466 -0.0616 -0.0634 644 HIS A CB 4925 C CG . HIS A 630 ? 0.5158 1.3443 0.7324 -0.0467 -0.0537 -0.0677 644 HIS A CG 4926 N ND1 . HIS A 630 ? 0.5207 1.3371 0.7256 -0.0607 -0.0471 -0.0637 644 HIS A ND1 4927 C CD2 . HIS A 630 ? 0.5299 1.3784 0.7535 -0.0343 -0.0515 -0.0759 644 HIS A CD2 4928 C CE1 . HIS A 630 ? 0.5111 1.3403 0.7153 -0.0576 -0.0414 -0.0685 644 HIS A CE1 4929 N NE2 . HIS A 630 ? 0.5247 1.3742 0.7398 -0.0414 -0.0437 -0.0765 644 HIS A NE2 4930 N N . GLY A 631 ? 0.4435 1.2008 0.6378 -0.0675 -0.0651 -0.0502 645 GLY A N 4931 C CA . GLY A 631 ? 0.4379 1.1700 0.6201 -0.0790 -0.0620 -0.0460 645 GLY A CA 4932 C C . GLY A 631 ? 0.4337 1.1519 0.6091 -0.0888 -0.0645 -0.0407 645 GLY A C 4933 O O . GLY A 631 ? 0.4612 1.1883 0.6404 -0.0862 -0.0697 -0.0400 645 GLY A O 4934 N N . TRP A 632 ? 0.3981 1.0946 0.5635 -0.0996 -0.0613 -0.0375 646 TRP A N 4935 C CA . TRP A 632 ? 0.4076 1.0910 0.5655 -0.1095 -0.0626 -0.0340 646 TRP A CA 4936 C C . TRP A 632 ? 0.3838 1.0598 0.5396 -0.1042 -0.0700 -0.0317 646 TRP A C 4937 O O . TRP A 632 ? 0.3897 1.0659 0.5498 -0.0931 -0.0746 -0.0316 646 TRP A O 4938 C CB . TRP A 632 ? 0.4081 1.0690 0.5569 -0.1210 -0.0574 -0.0318 646 TRP A CB 4939 C CG . TRP A 632 ? 0.4104 1.0752 0.5590 -0.1287 -0.0510 -0.0322 646 TRP A CG 4940 C CD1 . TRP A 632 ? 0.4286 1.1028 0.5785 -0.1368 -0.0492 -0.0316 646 TRP A CD1 4941 C CD2 . TRP A 632 ? 0.3734 1.0326 0.5204 -0.1298 -0.0461 -0.0323 646 TRP A CD2 4942 N NE1 . TRP A 632 ? 0.4243 1.0994 0.5734 -0.1427 -0.0436 -0.0306 646 TRP A NE1 4943 C CE2 . TRP A 632 ? 0.3880 1.0542 0.5346 -0.1386 -0.0415 -0.0312 646 TRP A CE2 4944 C CE3 . TRP A 632 ? 0.3380 0.9871 0.4841 -0.1242 -0.0460 -0.0330 646 TRP A CE3 4945 C CZ2 . TRP A 632 ? 0.3877 1.0521 0.5319 -0.1421 -0.0365 -0.0304 646 TRP A CZ2 4946 C CZ3 . TRP A 632 ? 0.4057 1.0528 0.5496 -0.1276 -0.0411 -0.0331 646 TRP A CZ3 4947 C CH2 . TRP A 632 ? 0.4133 1.0684 0.5557 -0.1365 -0.0363 -0.0316 646 TRP A CH2 4948 N N . ALA A 633 ? 0.3353 1.0050 0.4845 -0.1122 -0.0716 -0.0296 647 ALA A N 4949 C CA . ALA A 633 ? 0.3578 1.0170 0.5008 -0.1107 -0.0771 -0.0264 647 ALA A CA 4950 C C . ALA A 633 ? 0.3436 0.9801 0.4784 -0.1179 -0.0729 -0.0246 647 ALA A C 4951 O O . ALA A 633 ? 0.3323 0.9606 0.4651 -0.1260 -0.0666 -0.0259 647 ALA A O 4952 C CB . ALA A 633 ? 0.3794 1.0445 0.5182 -0.1159 -0.0809 -0.0260 647 ALA A CB 4953 N N . ALA A 634 ? 0.3613 0.9879 0.4920 -0.1149 -0.0767 -0.0209 648 ALA A N 4954 C CA . ALA A 634 ? 0.3404 0.9465 0.4647 -0.1215 -0.0730 -0.0190 648 ALA A CA 4955 C C . ALA A 634 ? 0.3285 0.9285 0.4458 -0.1218 -0.0772 -0.0144 648 ALA A C 4956 O O . ALA A 634 ? 0.3452 0.9554 0.4627 -0.1149 -0.0841 -0.0115 648 ALA A O 4957 C CB . ALA A 634 ? 0.3040 0.9018 0.4337 -0.1169 -0.0708 -0.0187 648 ALA A CB 4958 N N . ILE A 635 ? 0.3071 0.8910 0.4184 -0.1298 -0.0730 -0.0135 649 ILE A N 4959 C CA . ILE A 635 ? 0.3606 0.9391 0.4658 -0.1307 -0.0756 -0.0086 649 ILE A CA 4960 C C . ILE A 635 ? 0.3348 0.8954 0.4424 -0.1331 -0.0715 -0.0061 649 ILE A C 4961 O O . ILE A 635 ? 0.3195 0.8702 0.4302 -0.1365 -0.0661 -0.0093 649 ILE A O 4962 C CB . ILE A 635 ? 0.2929 0.8720 0.3876 -0.1401 -0.0743 -0.0112 649 ILE A CB 4963 C CG1 . ILE A 635 ? 0.3038 0.8688 0.3975 -0.1502 -0.0669 -0.0162 649 ILE A CG1 4964 C CG2 . ILE A 635 ? 0.3022 0.8981 0.3948 -0.1385 -0.0790 -0.0136 649 ILE A CG2 4965 C CD1 . ILE A 635 ? 0.3266 0.8905 0.4111 -0.1593 -0.0659 -0.0204 649 ILE A CD1 4966 N N . GLY A 636 ? 0.3214 0.8744 0.4264 -0.1308 -0.0735 0.0004 650 GLY A N 4967 C CA . GLY A 636 ? 0.2948 0.8232 0.4006 -0.1320 -0.0681 0.0035 650 GLY A CA 4968 C C . GLY A 636 ? 0.3336 0.8444 0.4335 -0.1272 -0.0679 0.0125 650 GLY A C 4969 O O . GLY A 636 ? 0.3557 0.8728 0.4484 -0.1237 -0.0715 0.0169 650 GLY A O 4970 N N . THR A 637 ? 0.3383 0.8275 0.4416 -0.1274 -0.0639 0.0159 651 THR A N 4971 C CA . THR A 637 ? 0.3780 0.8496 0.4780 -0.1241 -0.0627 0.0253 651 THR A CA 4972 C C . THR A 637 ? 0.3684 0.8235 0.4780 -0.1163 -0.0654 0.0306 651 THR A C 4973 O O . THR A 637 ? 0.3148 0.7668 0.4318 -0.1163 -0.0653 0.0257 651 THR A O 4974 C CB . THR A 637 ? 0.3902 0.8495 0.4851 -0.1334 -0.0543 0.0247 651 THR A CB 4975 O OG1 . THR A 637 ? 0.3973 0.8419 0.5007 -0.1372 -0.0505 0.0223 651 THR A OG1 4976 C CG2 . THR A 637 ? 0.4039 0.8778 0.4908 -0.1419 -0.0520 0.0165 651 THR A CG2 4977 N N . HIS A 638 ? 0.3601 0.8046 0.4695 -0.1100 -0.0684 0.0408 652 HIS A N 4978 C CA . HIS A 638 ? 0.3743 0.8031 0.4938 -0.1018 -0.0732 0.0460 652 HIS A CA 4979 C C . HIS A 638 ? 0.3774 0.7875 0.5029 -0.1063 -0.0683 0.0443 652 HIS A C 4980 O O . HIS A 638 ? 0.3790 0.7841 0.5120 -0.1022 -0.0716 0.0405 652 HIS A O 4981 C CB . HIS A 638 ? 0.3978 0.8173 0.5170 -0.0958 -0.0775 0.0589 652 HIS A CB 4982 C CG . HIS A 638 ? 0.4084 0.8113 0.5392 -0.0870 -0.0845 0.0642 652 HIS A CG 4983 N ND1 . HIS A 638 ? 0.4237 0.8049 0.5599 -0.0877 -0.0831 0.0730 652 HIS A ND1 4984 C CD2 . HIS A 638 ? 0.4297 0.8345 0.5688 -0.0772 -0.0931 0.0609 652 HIS A CD2 4985 C CE1 . HIS A 638 ? 0.4421 0.8112 0.5890 -0.0791 -0.0915 0.0751 652 HIS A CE1 4986 N NE2 . HIS A 638 ? 0.4573 0.8402 0.6057 -0.0722 -0.0975 0.0673 652 HIS A NE2 4987 N N . THR A 639 ? 0.3680 0.7682 0.4903 -0.1144 -0.0608 0.0466 653 THR A N 4988 C CA . THR A 639 ? 0.3374 0.7213 0.4659 -0.1200 -0.0561 0.0444 653 THR A CA 4989 C C . THR A 639 ? 0.3311 0.7201 0.4546 -0.1313 -0.0483 0.0371 653 THR A C 4990 O O . THR A 639 ? 0.3347 0.7415 0.4510 -0.1345 -0.0476 0.0315 653 THR A O 4991 C CB . THR A 639 ? 0.3536 0.7157 0.4882 -0.1183 -0.0554 0.0548 653 THR A CB 4992 O OG1 . THR A 639 ? 0.4898 0.8362 0.6317 -0.1230 -0.0526 0.0522 653 THR A OG1 4993 C CG2 . THR A 639 ? 0.3040 0.6668 0.4321 -0.1223 -0.0493 0.0610 653 THR A CG2 4994 N N . PHE A 640 ? 0.2855 0.6585 0.4142 -0.1372 -0.0434 0.0369 654 PHE A N 4995 C CA . PHE A 640 ? 0.3015 0.6762 0.4275 -0.1475 -0.0366 0.0306 654 PHE A CA 4996 C C . PHE A 640 ? 0.3114 0.6862 0.4308 -0.1488 -0.0314 0.0346 654 PHE A C 4997 O O . PHE A 640 ? 0.2824 0.6425 0.4062 -0.1495 -0.0271 0.0404 654 PHE A O 4998 C CB . PHE A 640 ? 0.2535 0.6111 0.3888 -0.1530 -0.0342 0.0292 654 PHE A CB 4999 C CG . PHE A 640 ? 0.2900 0.6508 0.4290 -0.1530 -0.0385 0.0243 654 PHE A CG 5000 C CD1 . PHE A 640 ? 0.2580 0.6323 0.3949 -0.1602 -0.0376 0.0162 654 PHE A CD1 5001 C CD2 . PHE A 640 ? 0.2959 0.6475 0.4402 -0.1456 -0.0438 0.0278 654 PHE A CD2 5002 C CE1 . PHE A 640 ? 0.2506 0.6308 0.3902 -0.1605 -0.0408 0.0126 654 PHE A CE1 5003 C CE2 . PHE A 640 ? 0.2885 0.6451 0.4345 -0.1450 -0.0472 0.0227 654 PHE A CE2 5004 C CZ . PHE A 640 ? 0.2861 0.6581 0.4294 -0.1526 -0.0452 0.0155 654 PHE A CZ 5005 N N . GLU A 641 ? 0.2837 0.6763 0.3924 -0.1487 -0.0320 0.0318 655 GLU A N 5006 C CA . GLU A 641 ? 0.3522 0.7485 0.4516 -0.1483 -0.0281 0.0362 655 GLU A CA 5007 C C . GLU A 641 ? 0.3516 0.7657 0.4393 -0.1530 -0.0271 0.0273 655 GLU A C 5008 O O . GLU A 641 ? 0.3186 0.7459 0.4056 -0.1537 -0.0320 0.0211 655 GLU A O 5009 C CB . GLU A 641 ? 0.4004 0.7988 0.4977 -0.1392 -0.0334 0.0473 655 GLU A CB 5010 C CG . GLU A 641 ? 0.4802 0.8963 0.5730 -0.1345 -0.0414 0.0447 655 GLU A CG 5011 C CD . GLU A 641 ? 0.5317 0.9480 0.6255 -0.1249 -0.0486 0.0556 655 GLU A CD 5012 O OE1 . GLU A 641 ? 0.5621 0.9861 0.6463 -0.1234 -0.0491 0.0618 655 GLU A OE1 5013 O OE2 . GLU A 641 ? 0.5613 0.9701 0.6653 -0.1189 -0.0545 0.0577 655 GLU A OE2 5014 N N . PHE A 642 ? 0.3024 0.7180 0.3813 -0.1560 -0.0211 0.0265 656 PHE A N 5015 C CA . PHE A 642 ? 0.3862 0.8176 0.4528 -0.1602 -0.0209 0.0175 656 PHE A CA 5016 C C . PHE A 642 ? 0.3710 0.8197 0.4278 -0.1548 -0.0278 0.0210 656 PHE A C 5017 O O . PHE A 642 ? 0.3695 0.8173 0.4241 -0.1480 -0.0299 0.0321 656 PHE A O 5018 C CB . PHE A 642 ? 0.4385 0.8670 0.4972 -0.1636 -0.0124 0.0149 656 PHE A CB 5019 C CG . PHE A 642 ? 0.4537 0.8664 0.5233 -0.1691 -0.0060 0.0100 656 PHE A CG 5020 C CD1 . PHE A 642 ? 0.4978 0.9095 0.5730 -0.1763 -0.0072 -0.0013 656 PHE A CD1 5021 C CD2 . PHE A 642 ? 0.4547 0.8540 0.5299 -0.1674 0.0007 0.0172 656 PHE A CD2 5022 C CE1 . PHE A 642 ? 0.4852 0.8818 0.5714 -0.1814 -0.0024 -0.0054 656 PHE A CE1 5023 C CE2 . PHE A 642 ? 0.4568 0.8418 0.5433 -0.1721 0.0059 0.0127 656 PHE A CE2 5024 C CZ . PHE A 642 ? 0.4514 0.8346 0.5433 -0.1790 0.0041 0.0013 656 PHE A CZ 5025 N N . ALA A 643 ? 0.3643 0.8284 0.4164 -0.1582 -0.0320 0.0120 657 ALA A N 5026 C CA . ALA A 643 ? 0.3744 0.8564 0.4183 -0.1538 -0.0394 0.0140 657 ALA A CA 5027 C C . ALA A 643 ? 0.3913 0.8876 0.4300 -0.1605 -0.0417 0.0020 657 ALA A C 5028 O O . ALA A 643 ? 0.4073 0.8999 0.4537 -0.1675 -0.0397 -0.0064 657 ALA A O 5029 C CB . ALA A 643 ? 0.4023 0.8867 0.4566 -0.1471 -0.0464 0.0189 657 ALA A CB 5030 N N . GLN A 644 ? 0.3418 0.8542 0.3684 -0.1589 -0.0467 0.0016 658 GLN A N 5031 C CA . GLN A 644 ? 0.3642 0.8913 0.3865 -0.1653 -0.0506 -0.0097 658 GLN A CA 5032 C C . GLN A 644 ? 0.3860 0.9324 0.4093 -0.1615 -0.0604 -0.0083 658 GLN A C 5033 O O . GLN A 644 ? 0.3951 0.9449 0.4173 -0.1532 -0.0645 0.0014 658 GLN A O 5034 C CB . GLN A 644 ? 0.3629 0.8926 0.3679 -0.1687 -0.0476 -0.0150 658 GLN A CB 5035 C CG . GLN A 644 ? 0.3630 0.8762 0.3686 -0.1731 -0.0379 -0.0195 658 GLN A CG 5036 C CD . GLN A 644 ? 0.4184 0.9350 0.4057 -0.1742 -0.0341 -0.0242 658 GLN A CD 5037 O OE1 . GLN A 644 ? 0.4381 0.9677 0.4146 -0.1772 -0.0390 -0.0326 658 GLN A OE1 5038 N NE2 . GLN A 644 ? 0.3869 0.8927 0.3705 -0.1717 -0.0253 -0.0189 658 GLN A NE2 5039 N N . PHE A 645 ? 0.4039 0.9630 0.4305 -0.1678 -0.0645 -0.0178 659 PHE A N 5040 C CA . PHE A 645 ? 0.3440 0.9234 0.3745 -0.1652 -0.0736 -0.0178 659 PHE A CA 5041 C C . PHE A 645 ? 0.3618 0.9543 0.3843 -0.1729 -0.0778 -0.0278 659 PHE A C 5042 O O . PHE A 645 ? 0.3558 0.9411 0.3770 -0.1812 -0.0739 -0.0364 659 PHE A O 5043 C CB . PHE A 645 ? 0.3270 0.9093 0.3759 -0.1654 -0.0744 -0.0188 659 PHE A CB 5044 C CG . PHE A 645 ? 0.3176 0.8846 0.3743 -0.1585 -0.0705 -0.0110 659 PHE A CG 5045 C CD1 . PHE A 645 ? 0.3110 0.8582 0.3712 -0.1623 -0.0628 -0.0114 659 PHE A CD1 5046 C CD2 . PHE A 645 ? 0.3962 0.9681 0.4577 -0.1481 -0.0755 -0.0035 659 PHE A CD2 5047 C CE1 . PHE A 645 ? 0.3033 0.8358 0.3709 -0.1562 -0.0602 -0.0044 659 PHE A CE1 5048 C CE2 . PHE A 645 ? 0.3092 0.8661 0.3782 -0.1416 -0.0732 0.0029 659 PHE A CE2 5049 C CZ . PHE A 645 ? 0.3308 0.8680 0.4026 -0.1459 -0.0656 0.0025 659 PHE A CZ 5050 N N . ASP A 646 ? 0.3858 0.9962 0.4037 -0.1699 -0.0863 -0.0268 660 ASP A N 5051 C CA . ASP A 646 ? 0.4137 1.0292 0.4223 -0.1745 -0.0894 -0.0352 660 ASP A CA 5052 C C . ASP A 646 ? 0.4125 1.0390 0.4259 -0.1688 -0.0961 -0.0328 660 ASP A C 5053 O O . ASP A 646 ? 0.4203 1.0529 0.4384 -0.1604 -0.0996 -0.0242 660 ASP A O 5054 C CB . ASP A 646 ? 0.4507 1.0703 0.4378 -0.1756 -0.0908 -0.0357 660 ASP A CB 5055 C CG . ASP A 646 ? 0.4675 1.0886 0.4447 -0.1829 -0.0923 -0.0479 660 ASP A CG 5056 O OD1 . ASP A 646 ? 0.4451 1.0627 0.4331 -0.1861 -0.0932 -0.0540 660 ASP A OD1 5057 O OD2 . ASP A 646 ? 0.5497 1.1712 0.5077 -0.1839 -0.0915 -0.0509 660 ASP A OD2 5058 N N . ASN A 647 ? 0.4241 1.0534 0.4378 -0.1732 -0.0987 -0.0404 661 ASN A N 5059 C CA . ASN A 647 ? 0.4493 1.0906 0.4678 -0.1690 -0.1058 -0.0389 661 ASN A CA 5060 C C . ASN A 647 ? 0.4614 1.1064 0.4967 -0.1616 -0.1056 -0.0328 661 ASN A C 5061 O O . ASN A 647 ? 0.4831 1.1380 0.5197 -0.1533 -0.1113 -0.0265 661 ASN A O 5062 C CB . ASN A 647 ? 0.4941 1.1460 0.4970 -0.1648 -0.1133 -0.0353 661 ASN A CB 5063 C CG . ASN A 647 ? 0.5456 1.1945 0.5286 -0.1709 -0.1128 -0.0415 661 ASN A CG 5064 O OD1 . ASN A 647 ? 0.5749 1.2190 0.5566 -0.1782 -0.1119 -0.0516 661 ASN A OD1 5065 N ND2 . ASN A 647 ? 0.4381 1.0899 0.4052 -0.1675 -0.1136 -0.0352 661 ASN A ND2 5066 N N . PHE A 648 ? 0.4266 1.0633 0.4742 -0.1644 -0.0993 -0.0350 662 PHE A N 5067 C CA . PHE A 648 ? 0.3782 1.0183 0.4406 -0.1577 -0.0980 -0.0309 662 PHE A CA 5068 C C . PHE A 648 ? 0.3854 1.0390 0.4565 -0.1563 -0.1027 -0.0325 662 PHE A C 5069 O O . PHE A 648 ? 0.3840 1.0379 0.4553 -0.1637 -0.1033 -0.0380 662 PHE A O 5070 C CB . PHE A 648 ? 0.3732 0.9998 0.4435 -0.1620 -0.0897 -0.0329 662 PHE A CB 5071 C CG . PHE A 648 ? 0.4173 1.0476 0.5009 -0.1554 -0.0877 -0.0298 662 PHE A CG 5072 C CD1 . PHE A 648 ? 0.3871 1.0141 0.4735 -0.1478 -0.0867 -0.0247 662 PHE A CD1 5073 C CD2 . PHE A 648 ? 0.4399 1.0778 0.5334 -0.1569 -0.0872 -0.0321 662 PHE A CD2 5074 C CE1 . PHE A 648 ? 0.3870 1.0179 0.4851 -0.1412 -0.0852 -0.0234 662 PHE A CE1 5075 C CE2 . PHE A 648 ? 0.4387 1.0823 0.5434 -0.1507 -0.0849 -0.0302 662 PHE A CE2 5076 C CZ . PHE A 648 ? 0.4026 1.0426 0.5092 -0.1426 -0.0839 -0.0265 662 PHE A CZ 5077 N N . ARG A 649 ? 0.3810 1.0456 0.4606 -0.1467 -0.1062 -0.0279 663 ARG A N 5078 C CA . ARG A 649 ? 0.4118 1.0913 0.5024 -0.1446 -0.1103 -0.0292 663 ARG A CA 5079 C C . ARG A 649 ? 0.4262 1.1128 0.5310 -0.1353 -0.1089 -0.0263 663 ARG A C 5080 O O . ARG A 649 ? 0.4339 1.1173 0.5389 -0.1273 -0.1093 -0.0221 663 ARG A O 5081 C CB . ARG A 649 ? 0.3824 1.0732 0.4671 -0.1417 -0.1201 -0.0279 663 ARG A CB 5082 N N . VAL A 650 ? 0.4105 1.1073 0.5273 -0.1364 -0.1076 -0.0288 664 VAL A N 5083 C CA . VAL A 650 ? 0.4281 1.1351 0.5585 -0.1273 -0.1063 -0.0276 664 VAL A CA 5084 C C . VAL A 650 ? 0.4387 1.1656 0.5811 -0.1261 -0.1102 -0.0291 664 VAL A C 5085 O O . VAL A 650 ? 0.4069 1.1369 0.5507 -0.1350 -0.1098 -0.0317 664 VAL A O 5086 C CB . VAL A 650 ? 0.4599 1.1579 0.5939 -0.1296 -0.0968 -0.0287 664 VAL A CB 5087 C CG1 . VAL A 650 ? 0.3959 1.0920 0.5314 -0.1411 -0.0921 -0.0317 664 VAL A CG1 5088 C CG2 . VAL A 650 ? 0.4440 1.1536 0.5905 -0.1189 -0.0959 -0.0284 664 VAL A CG2 5089 N N . GLU A 651 ? 0.4399 1.1798 0.5918 -0.1146 -0.1149 -0.0273 665 GLU A N 5090 C CA . GLU A 651 ? 0.4924 1.2529 0.6578 -0.1116 -0.1190 -0.0285 665 GLU A CA 5091 C C . GLU A 651 ? 0.4509 1.2211 0.6294 -0.1017 -0.1155 -0.0293 665 GLU A C 5092 O O . GLU A 651 ? 0.4682 1.2355 0.6478 -0.0911 -0.1183 -0.0275 665 GLU A O 5093 C CB . GLU A 651 ? 0.5463 1.3135 0.7104 -0.1058 -0.1302 -0.0258 665 GLU A CB 5094 C CG . GLU A 651 ? 0.6249 1.4120 0.8015 -0.1049 -0.1363 -0.0269 665 GLU A CG 5095 C CD . GLU A 651 ? 0.7078 1.4966 0.8778 -0.1034 -0.1477 -0.0242 665 GLU A CD 5096 O OE1 . GLU A 651 ? 0.7055 1.4880 0.8690 -0.0957 -0.1528 -0.0200 665 GLU A OE1 5097 O OE2 . GLU A 651 ? 0.7718 1.5674 0.9423 -0.1104 -0.1521 -0.0259 665 GLU A OE2 5098 N N . ALA A 652 ? 0.4379 1.2199 0.6264 -0.1048 -0.1096 -0.0319 666 ALA A N 5099 C CA . ALA A 652 ? 0.4784 1.2694 0.6770 -0.0959 -0.1047 -0.0337 666 ALA A CA 5100 C C . ALA A 652 ? 0.5350 1.3504 0.7490 -0.0948 -0.1027 -0.0360 666 ALA A C 5101 O O . ALA A 652 ? 0.5447 1.3672 0.7612 -0.1043 -0.1025 -0.0358 666 ALA A O 5102 C CB . ALA A 652 ? 0.4136 1.1887 0.6044 -0.1002 -0.0958 -0.0342 666 ALA A CB 5103 N N . ALA A 653 ? 0.5645 1.3931 0.7895 -0.0828 -0.1017 -0.0384 667 ALA A N 5104 C CA . ALA A 653 ? 0.6043 1.4584 0.8444 -0.0804 -0.0984 -0.0411 667 ALA A CA 5105 C C . ALA A 653 ? 0.6105 1.4673 0.8508 -0.0788 -0.0885 -0.0439 667 ALA A C 5106 O O . ALA A 653 ? 0.5478 1.3963 0.7856 -0.0699 -0.0877 -0.0458 667 ALA A O 5107 C CB . ALA A 653 ? 0.5972 1.4690 0.8521 -0.0666 -0.1064 -0.0425 667 ALA A CB 5108 N N . ARG A 654 ? 0.6657 1.5341 0.9089 -0.0876 -0.0815 -0.0439 668 ARG A N 5109 C CA . ARG A 654 ? 0.7068 1.5785 0.9481 -0.0883 -0.0719 -0.0458 668 ARG A CA 5110 C C . ARG A 654 ? 0.7584 1.6562 1.0134 -0.0749 -0.0698 -0.0510 668 ARG A C 5111 O O . ARG A 654 ? 0.7821 1.6772 1.0382 -0.0622 -0.0713 -0.0549 668 ARG A O 5112 C CB . ARG A 654 ? 0.6896 1.5615 0.9274 -0.1041 -0.0660 -0.0424 668 ARG A CB 5113 C CG . ARG A 654 ? 0.6744 1.5523 0.9099 -0.1061 -0.0565 -0.0431 668 ARG A CG 5114 C CD . ARG A 654 ? 0.6767 1.5439 0.9050 -0.1227 -0.0524 -0.0381 668 ARG A CD 5115 N NE . ARG A 654 ? 0.6760 1.5588 0.9061 -0.1256 -0.0442 -0.0375 668 ARG A NE 5116 C CZ . ARG A 654 ? 0.6938 1.5661 0.9164 -0.1382 -0.0397 -0.0330 668 ARG A CZ 5117 N NH1 . ARG A 654 ? 0.6907 1.5360 0.9044 -0.1484 -0.0423 -0.0296 668 ARG A NH1 5118 N NH2 . ARG A 654 ? 0.7076 1.5967 0.9316 -0.1403 -0.0327 -0.0319 668 ARG A NH2 5119 O OXT . ARG A 654 ? 0.7548 1.6772 1.0209 -0.0758 -0.0670 -0.0517 668 ARG A OXT # 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 HIS 1 15 ? ? ? A . n A 1 2 HIS 2 16 ? ? ? A . n A 1 3 HIS 3 17 ? ? ? A . n A 1 4 HIS 4 18 ? ? ? A . n A 1 5 HIS 5 19 ? ? ? A . n A 1 6 HIS 6 20 ? ? ? A . n A 1 7 ILE 7 21 ? ? ? A . n A 1 8 GLU 8 22 ? ? ? A . n A 1 9 GLY 9 23 ? ? ? A . n A 1 10 ARG 10 24 ? ? ? A . n A 1 11 GLY 11 25 25 GLY GLY A . n A 1 12 ALA 12 26 26 ALA ALA A . n A 1 13 TYR 13 27 27 TYR TYR A . n A 1 14 VAL 14 28 28 VAL VAL A . n A 1 15 LEU 15 29 29 LEU LEU A . n A 1 16 ASP 16 30 30 ASP ASP A . n A 1 17 ASP 17 31 31 ASP ASP A . n A 1 18 SER 18 32 32 SER SER A . n A 1 19 ASP 19 33 33 ASP ASP A . n A 1 20 GLY 20 34 34 GLY GLY A . n A 1 21 LEU 21 35 35 LEU LEU A . n A 1 22 GLY 22 36 36 GLY GLY A . n A 1 23 ARG 23 37 37 ARG ARG A . n A 1 24 GLU 24 38 38 GLU GLU A . n A 1 25 PHE 25 39 39 PHE PHE A . n A 1 26 ASP 26 40 40 ASP ASP A . n A 1 27 GLY 27 41 41 GLY GLY A . n A 1 28 ILE 28 42 42 ILE ILE A . n A 1 29 GLY 29 43 43 GLY GLY A . n A 1 30 ALA 30 44 44 ALA ALA A . n A 1 31 VAL 31 45 45 VAL VAL A . n A 1 32 SER 32 46 46 SER SER A . n A 1 33 GLY 33 47 47 GLY GLY A . n A 1 34 GLY 34 48 48 GLY GLY A . n A 1 35 GLY 35 49 49 GLY GLY A . n A 1 36 ALA 36 50 50 ALA ALA A . n A 1 37 THR 37 51 51 THR THR A . n A 1 38 SER 38 52 52 SER SER A . n A 1 39 ARG 39 53 53 ARG ARG A . n A 1 40 LEU 40 54 54 LEU LEU A . n A 1 41 LEU 41 55 55 LEU LEU A . n A 1 42 VAL 42 56 56 VAL VAL A . n A 1 43 ASN 43 57 57 ASN ASN A . n A 1 44 TYR 44 58 58 TYR TYR A . n A 1 45 PRO 45 59 59 PRO PRO A . n A 1 46 GLU 46 60 60 GLU GLU A . n A 1 47 PRO 47 61 61 PRO PRO A . n A 1 48 TYR 48 62 62 TYR TYR A . n A 1 49 ARG 49 63 63 ARG ARG A . n A 1 50 SER 50 64 64 SER SER A . n A 1 51 GLU 51 65 65 GLU GLU A . n A 1 52 ILE 52 66 66 ILE ILE A . n A 1 53 LEU 53 67 67 LEU LEU A . n A 1 54 ASP 54 68 68 ASP ASP A . n A 1 55 TYR 55 69 69 TYR TYR A . n A 1 56 LEU 56 70 70 LEU LEU A . n A 1 57 PHE 57 71 71 PHE PHE A . n A 1 58 LYS 58 72 72 LYS LYS A . n A 1 59 PRO 59 73 73 PRO PRO A . n A 1 60 ASN 60 74 74 ASN ASN A . n A 1 61 PHE 61 75 75 PHE PHE A . n A 1 62 GLY 62 76 76 GLY GLY A . n A 1 63 ALA 63 77 77 ALA ALA A . n A 1 64 SER 64 78 78 SER SER A . n A 1 65 LEU 65 79 79 LEU LEU A . n A 1 66 HIS 66 80 80 HIS HIS A . n A 1 67 ILE 67 81 81 ILE ILE A . n A 1 68 LEU 68 82 82 LEU LEU A . n A 1 69 LYS 69 83 83 LYS LYS A . n A 1 70 VAL 70 84 84 VAL VAL A . n A 1 71 GLU 71 85 85 GLU GLU A . n A 1 72 ILE 72 86 86 ILE ILE A . n A 1 73 GLY 73 87 87 GLY GLY A . n A 1 74 GLY 74 88 88 GLY GLY A . n A 1 75 ASP 75 89 89 ASP ASP A . n A 1 76 GLY 76 90 90 GLY GLY A . n A 1 77 GLN 77 91 91 GLN GLN A . n A 1 78 THR 78 92 92 THR THR A . n A 1 79 THR 79 93 93 THR THR A . n A 1 80 ASP 80 94 94 ASP ASP A . n A 1 81 GLY 81 95 95 GLY GLY A . n A 1 82 THR 82 96 96 THR THR A . n A 1 83 GLU 83 97 97 GLU GLU A . n A 1 84 PRO 84 98 98 PRO PRO A . n A 1 85 SER 85 99 99 SER SER A . n A 1 86 HIS 86 100 100 HIS HIS A . n A 1 87 MET 87 101 101 MET MET A . n A 1 88 HIS 88 102 102 HIS HIS A . n A 1 89 TYR 89 103 103 TYR TYR A . n A 1 90 GLU 90 104 104 GLU GLU A . n A 1 91 LEU 91 105 105 LEU LEU A . n A 1 92 ASP 92 106 106 ASP ASP A . n A 1 93 GLU 93 107 107 GLU GLU A . n A 1 94 ASN 94 108 108 ASN ASN A . n A 1 95 TYR 95 109 109 TYR TYR A . n A 1 96 PHE 96 110 110 PHE PHE A . n A 1 97 ARG 97 111 111 ARG ARG A . n A 1 98 GLY 98 112 112 GLY GLY A . n A 1 99 TYR 99 113 113 TYR TYR A . n A 1 100 GLU 100 114 114 GLU GLU A . n A 1 101 TRP 101 115 115 TRP TRP A . n A 1 102 TRP 102 116 116 TRP TRP A . n A 1 103 LEU 103 117 117 LEU LEU A . n A 1 104 MET 104 118 118 MET MET A . n A 1 105 LYS 105 119 119 LYS LYS A . n A 1 106 GLU 106 120 120 GLU GLU A . n A 1 107 ALA 107 121 121 ALA ALA A . n A 1 108 LYS 108 122 122 LYS LYS A . n A 1 109 LYS 109 123 123 LYS LYS A . n A 1 110 ARG 110 124 124 ARG ARG A . n A 1 111 ASN 111 125 125 ASN ASN A . n A 1 112 PRO 112 126 126 PRO PRO A . n A 1 113 ASP 113 127 127 ASP ASP A . n A 1 114 ILE 114 128 128 ILE ILE A . n A 1 115 ILE 115 129 129 ILE ILE A . n A 1 116 LEU 116 130 130 LEU LEU A . n A 1 117 MET 117 131 131 MET MET A . n A 1 118 GLY 118 132 132 GLY GLY A . n A 1 119 LEU 119 133 133 LEU LEU A . n A 1 120 PRO 120 134 134 PRO PRO A . n A 1 121 TRP 121 135 135 TRP TRP A . n A 1 122 SER 122 136 136 SER SER A . n A 1 123 PHE 123 137 137 PHE PHE A . n A 1 124 PRO 124 138 138 PRO PRO A . n A 1 125 GLY 125 139 139 GLY GLY A . n A 1 126 TRP 126 140 140 TRP TRP A . n A 1 127 LEU 127 141 141 LEU LEU A . n A 1 128 GLY 128 142 142 GLY GLY A . n A 1 129 LYS 129 143 143 LYS LYS A . n A 1 130 GLY 130 144 144 GLY GLY A . n A 1 131 PHE 131 145 145 PHE PHE A . n A 1 132 SER 132 146 146 SER SER A . n A 1 133 TRP 133 147 147 TRP TRP A . n A 1 134 PRO 134 148 148 PRO PRO A . n A 1 135 TYR 135 149 149 TYR TYR A . n A 1 136 VAL 136 150 150 VAL VAL A . n A 1 137 ASN 137 151 151 ASN ASN A . n A 1 138 LEU 138 152 152 LEU LEU A . n A 1 139 GLN 139 153 153 GLN GLN A . n A 1 140 LEU 140 154 154 LEU LEU A . n A 1 141 THR 141 155 155 THR THR A . n A 1 142 ALA 142 156 156 ALA ALA A . n A 1 143 TYR 143 157 157 TYR TYR A . n A 1 144 TYR 144 158 158 TYR TYR A . n A 1 145 VAL 145 159 159 VAL VAL A . n A 1 146 VAL 146 160 160 VAL VAL A . n A 1 147 ARG 147 161 161 ARG ARG A . n A 1 148 TRP 148 162 162 TRP TRP A . n A 1 149 ILE 149 163 163 ILE ILE A . n A 1 150 LEU 150 164 164 LEU LEU A . n A 1 151 GLY 151 165 165 GLY GLY A . n A 1 152 ALA 152 166 166 ALA ALA A . n A 1 153 LYS 153 167 167 LYS LYS A . n A 1 154 HIS 154 168 168 HIS HIS A . n A 1 155 TYR 155 169 169 TYR TYR A . n A 1 156 HIS 156 170 170 HIS HIS A . n A 1 157 ASP 157 171 171 ASP ASP A . n A 1 158 LEU 158 172 172 LEU LEU A . n A 1 159 ASP 159 173 173 ASP ASP A . n A 1 160 ILE 160 174 174 ILE ILE A . n A 1 161 ASP 161 175 175 ASP ASP A . n A 1 162 TYR 162 176 176 TYR TYR A . n A 1 163 ILE 163 177 177 ILE ILE A . n A 1 164 GLY 164 178 178 GLY GLY A . n A 1 165 ILE 165 179 179 ILE ILE A . n A 1 166 TRP 166 180 180 TRP TRP A . n A 1 167 ASN 167 181 181 ASN ASN A . n A 1 168 GLU 168 182 182 GLU GLU A . n A 1 169 ARG 169 183 183 ARG ARG A . n A 1 170 PRO 170 184 184 PRO PRO A . n A 1 171 PHE 171 185 185 PHE PHE A . n A 1 172 ASP 172 186 186 ASP ASP A . n A 1 173 ALA 173 187 187 ALA ALA A . n A 1 174 ASN 174 188 188 ASN ASN A . n A 1 175 TYR 175 189 189 TYR TYR A . n A 1 176 ILE 176 190 190 ILE ILE A . n A 1 177 LYS 177 191 191 LYS LYS A . n A 1 178 GLU 178 192 192 GLU GLU A . n A 1 179 LEU 179 193 193 LEU LEU A . n A 1 180 ARG 180 194 194 ARG ARG A . n A 1 181 LYS 181 195 195 LYS LYS A . n A 1 182 MET 182 196 196 MET MET A . n A 1 183 LEU 183 197 197 LEU LEU A . n A 1 184 ASP 184 198 198 ASP ASP A . n A 1 185 TYR 185 199 199 TYR TYR A . n A 1 186 GLN 186 200 200 GLN GLN A . n A 1 187 GLY 187 201 201 GLY GLY A . n A 1 188 LEU 188 202 202 LEU LEU A . n A 1 189 GLN 189 203 203 GLN GLN A . n A 1 190 ARG 190 204 204 ARG ARG A . n A 1 191 VAL 191 205 205 VAL VAL A . n A 1 192 ARG 192 206 206 ARG ARG A . n A 1 193 ILE 193 207 207 ILE ILE A . n A 1 194 ILE 194 208 208 ILE ILE A . n A 1 195 ALA 195 209 209 ALA ALA A . n A 1 196 SER 196 210 210 SER SER A . n A 1 197 ASP 197 211 211 ASP ASP A . n A 1 198 ASN 198 212 212 ASN ASN A . n A 1 199 LEU 199 213 213 LEU LEU A . n A 1 200 TRP 200 214 214 TRP TRP A . n A 1 201 GLU 201 215 215 GLU GLU A . n A 1 202 PRO 202 216 216 PRO PRO A . n A 1 203 ILE 203 217 217 ILE ILE A . n A 1 204 SER 204 218 218 SER SER A . n A 1 205 SER 205 219 219 SER SER A . n A 1 206 SER 206 220 220 SER SER A . n A 1 207 LEU 207 221 221 LEU LEU A . n A 1 208 LEU 208 222 222 LEU LEU A . n A 1 209 LEU 209 223 223 LEU LEU A . n A 1 210 ASP 210 224 224 ASP ASP A . n A 1 211 GLN 211 225 225 GLN GLN A . n A 1 212 GLU 212 226 226 GLU GLU A . n A 1 213 LEU 213 227 227 LEU LEU A . n A 1 214 TRP 214 228 228 TRP TRP A . n A 1 215 LYS 215 229 229 LYS LYS A . n A 1 216 VAL 216 230 230 VAL VAL A . n A 1 217 VAL 217 231 231 VAL VAL A . n A 1 218 ASP 218 232 232 ASP ASP A . n A 1 219 VAL 219 233 233 VAL VAL A . n A 1 220 ILE 220 234 234 ILE ILE A . n A 1 221 GLY 221 235 235 GLY GLY A . n A 1 222 ALA 222 236 236 ALA ALA A . n A 1 223 HIS 223 237 237 HIS HIS A . n A 1 224 TYR 224 238 238 TYR TYR A . n A 1 225 PRO 225 239 239 PRO PRO A . n A 1 226 GLY 226 240 240 GLY GLY A . n A 1 227 THR 227 241 241 THR THR A . n A 1 228 TYR 228 242 242 TYR TYR A . n A 1 229 THR 229 243 243 THR THR A . n A 1 230 VAL 230 244 244 VAL VAL A . n A 1 231 TRP 231 245 245 TRP TRP A . n A 1 232 ASN 232 246 246 ASN ASN A . n A 1 233 ALA 233 247 247 ALA ALA A . n A 1 234 LYS 234 248 248 LYS LYS A . n A 1 235 MET 235 249 249 MET MET A . n A 1 236 SER 236 250 250 SER SER A . n A 1 237 GLY 237 251 251 GLY GLY A . n A 1 238 LYS 238 252 252 LYS LYS A . n A 1 239 LYS 239 253 253 LYS LYS A . n A 1 240 LEU 240 254 254 LEU LEU A . n A 1 241 TRP 241 255 255 TRP TRP A . n A 1 242 SER 242 256 256 SER SER A . n A 1 243 SER 243 257 257 SER SER A . n A 1 244 GLU 244 258 258 GLU GLU A . n A 1 245 ASP 245 259 259 ASP ASP A . n A 1 246 PHE 246 260 260 PHE PHE A . n A 1 247 SER 247 261 261 SER SER A . n A 1 248 THR 248 262 262 THR THR A . n A 1 249 ILE 249 263 263 ILE ILE A . n A 1 250 ASN 250 264 264 ASN ASN A . n A 1 251 SER 251 265 265 SER SER A . n A 1 252 ASN 252 266 266 ASN ASN A . n A 1 253 VAL 253 267 267 VAL VAL A . n A 1 254 GLY 254 268 268 GLY GLY A . n A 1 255 ALA 255 269 269 ALA ALA A . n A 1 256 GLY 256 270 270 GLY GLY A . n A 1 257 CYS 257 271 271 CYS CYS A . n A 1 258 TRP 258 272 272 TRP TRP A . n A 1 259 SER 259 273 273 SER SER A . n A 1 260 ARG 260 274 274 ARG ARG A . n A 1 261 ILE 261 275 275 ILE ILE A . n A 1 262 LEU 262 276 276 LEU LEU A . n A 1 263 ASN 263 277 277 ASN ASN A . n A 1 264 GLN 264 278 278 GLN GLN A . n A 1 265 ASN 265 279 279 ASN ASN A . n A 1 266 TYR 266 280 280 TYR TYR A . n A 1 267 ILE 267 281 281 ILE ILE A . n A 1 268 ASN 268 282 282 ASN ASN A . n A 1 269 GLY 269 283 283 GLY GLY A . n A 1 270 ASN 270 284 284 ASN ASN A . n A 1 271 MET 271 285 285 MET MET A . n A 1 272 THR 272 286 286 THR THR A . n A 1 273 SER 273 287 287 SER SER A . n A 1 274 THR 274 288 288 THR THR A . n A 1 275 ILE 275 289 289 ILE ILE A . n A 1 276 ALA 276 290 290 ALA ALA A . n A 1 277 TRP 277 291 291 TRP TRP A . n A 1 278 ASN 278 292 292 ASN ASN A . n A 1 279 LEU 279 293 293 LEU LEU A . n A 1 280 VAL 280 294 294 VAL VAL A . n A 1 281 ALA 281 295 295 ALA ALA A . n A 1 282 SER 282 296 296 SER SER A . n A 1 283 TYR 283 297 297 TYR TYR A . n A 1 284 TYR 284 298 298 TYR TYR A . n A 1 285 GLU 285 299 299 GLU GLU A . n A 1 286 GLU 286 300 300 GLU GLU A . n A 1 287 LEU 287 301 301 LEU LEU A . n A 1 288 PRO 288 302 302 PRO PRO A . n A 1 289 TYR 289 303 303 TYR TYR A . n A 1 290 GLY 290 304 304 GLY GLY A . n A 1 291 ARG 291 305 305 ARG ARG A . n A 1 292 SER 292 306 306 SER SER A . n A 1 293 GLY 293 307 307 GLY GLY A . n A 1 294 LEU 294 308 308 LEU LEU A . n A 1 295 MET 295 309 309 MET MET A . n A 1 296 THR 296 310 310 THR THR A . n A 1 297 ALA 297 311 311 ALA ALA A . n A 1 298 GLN 298 312 312 GLN GLN A . n A 1 299 GLU 299 313 313 GLU GLU A . n A 1 300 PRO 300 314 314 PRO PRO A . n A 1 301 TRP 301 315 315 TRP TRP A . n A 1 302 SER 302 316 316 SER SER A . n A 1 303 GLY 303 317 317 GLY GLY A . n A 1 304 HIS 304 318 318 HIS HIS A . n A 1 305 TYR 305 319 319 TYR TYR A . n A 1 306 VAL 306 320 320 VAL VAL A . n A 1 307 VAL 307 321 321 VAL VAL A . n A 1 308 ALA 308 322 322 ALA ALA A . n A 1 309 SER 309 323 323 SER SER A . n A 1 310 PRO 310 324 324 PRO PRO A . n A 1 311 ILE 311 325 325 ILE ILE A . n A 1 312 TRP 312 326 326 TRP TRP A . n A 1 313 VAL 313 327 327 VAL VAL A . n A 1 314 SER 314 328 328 SER SER A . n A 1 315 ALA 315 329 329 ALA ALA A . n A 1 316 HIS 316 330 330 HIS HIS A . n A 1 317 THR 317 331 331 THR THR A . n A 1 318 THR 318 332 332 THR THR A . n A 1 319 GLN 319 333 333 GLN GLN A . n A 1 320 PHE 320 334 334 PHE PHE A . n A 1 321 THR 321 335 335 THR THR A . n A 1 322 GLN 322 336 336 GLN GLN A . n A 1 323 PRO 323 337 337 PRO PRO A . n A 1 324 GLY 324 338 338 GLY GLY A . n A 1 325 TRP 325 339 339 TRP TRP A . n A 1 326 TYR 326 340 340 TYR TYR A . n A 1 327 TYR 327 341 341 TYR TYR A . n A 1 328 LEU 328 342 342 LEU LEU A . n A 1 329 LYS 329 343 343 LYS LYS A . n A 1 330 THR 330 344 344 THR THR A . n A 1 331 VAL 331 345 345 VAL VAL A . n A 1 332 GLY 332 346 346 GLY GLY A . n A 1 333 HIS 333 347 347 HIS HIS A . n A 1 334 LEU 334 348 348 LEU LEU A . n A 1 335 GLU 335 349 349 GLU GLU A . n A 1 336 LYS 336 350 350 LYS LYS A . n A 1 337 GLY 337 351 351 GLY GLY A . n A 1 338 GLY 338 352 352 GLY GLY A . n A 1 339 SER 339 353 353 SER SER A . n A 1 340 TYR 340 354 354 TYR TYR A . n A 1 341 VAL 341 355 355 VAL VAL A . n A 1 342 ALA 342 356 356 ALA ALA A . n A 1 343 LEU 343 357 357 LEU LEU A . n A 1 344 THR 344 358 358 THR THR A . n A 1 345 ASP 345 359 359 ASP ASP A . n A 1 346 GLY 346 360 360 GLY GLY A . n A 1 347 LEU 347 361 361 LEU LEU A . n A 1 348 GLY 348 362 362 GLY GLY A . n A 1 349 ASN 349 363 363 ASN ASN A . n A 1 350 LEU 350 364 364 LEU LEU A . n A 1 351 THR 351 365 365 THR THR A . n A 1 352 ILE 352 366 366 ILE ILE A . n A 1 353 ILE 353 367 367 ILE ILE A . n A 1 354 ILE 354 368 368 ILE ILE A . n A 1 355 GLU 355 369 369 GLU GLU A . n A 1 356 THR 356 370 370 THR THR A . n A 1 357 MET 357 371 371 MET MET A . n A 1 358 SER 358 372 372 SER SER A . n A 1 359 HIS 359 373 373 HIS HIS A . n A 1 360 GLN 360 374 374 GLN GLN A . n A 1 361 HIS 361 375 375 HIS HIS A . n A 1 362 SER 362 376 376 SER SER A . n A 1 363 MET 363 377 377 MET MET A . n A 1 364 CYS 364 378 378 CYS CYS A . n A 1 365 ILE 365 379 379 ILE ILE A . n A 1 366 ARG 366 380 380 ARG ARG A . n A 1 367 PRO 367 381 381 PRO PRO A . n A 1 368 TYR 368 382 382 TYR TYR A . n A 1 369 LEU 369 383 383 LEU LEU A . n A 1 370 PRO 370 384 384 PRO PRO A . n A 1 371 TYR 371 385 385 TYR TYR A . n A 1 372 TYR 372 386 386 TYR TYR A . n A 1 373 ASN 373 387 387 ASN ASN A . n A 1 374 VAL 374 388 388 VAL VAL A . n A 1 375 SER 375 389 389 SER SER A . n A 1 376 HIS 376 390 390 HIS HIS A . n A 1 377 GLN 377 391 391 GLN GLN A . n A 1 378 LEU 378 392 392 LEU LEU A . n A 1 379 ALA 379 393 393 ALA ALA A . n A 1 380 THR 380 394 394 THR THR A . n A 1 381 PHE 381 395 395 PHE PHE A . n A 1 382 THR 382 396 396 THR THR A . n A 1 383 LEU 383 397 397 LEU LEU A . n A 1 384 LYS 384 398 398 LYS LYS A . n A 1 385 GLY 385 399 399 GLY GLY A . n A 1 386 SER 386 400 400 SER SER A . n A 1 387 LEU 387 401 401 LEU LEU A . n A 1 388 ARG 388 402 402 ARG ARG A . n A 1 389 GLU 389 403 403 GLU GLU A . n A 1 390 ILE 390 404 404 ILE ILE A . n A 1 391 GLN 391 405 405 GLN GLN A . n A 1 392 GLU 392 406 406 GLU GLU A . n A 1 393 LEU 393 407 407 LEU LEU A . n A 1 394 GLN 394 408 408 GLN GLN A . n A 1 395 VAL 395 409 409 VAL VAL A . n A 1 396 TRP 396 410 410 TRP TRP A . n A 1 397 TYR 397 411 411 TYR TYR A . n A 1 398 THR 398 412 412 THR THR A . n A 1 399 LYS 399 413 413 LYS LYS A . n A 1 400 LEU 400 414 414 LEU LEU A . n A 1 401 GLY 401 415 415 GLY GLY A . n A 1 402 THR 402 416 ? ? ? A . n A 1 403 PRO 403 417 ? ? ? A . n A 1 404 GLN 404 418 ? ? ? A . n A 1 405 GLN 405 419 ? ? ? A . n A 1 406 ARG 406 420 420 ARG ARG A . n A 1 407 LEU 407 421 421 LEU LEU A . n A 1 408 HIS 408 422 422 HIS HIS A . n A 1 409 PHE 409 423 423 PHE PHE A . n A 1 410 LYS 410 424 424 LYS LYS A . n A 1 411 GLN 411 425 425 GLN GLN A . n A 1 412 LEU 412 426 426 LEU LEU A . n A 1 413 ASP 413 427 427 ASP ASP A . n A 1 414 THR 414 428 428 THR THR A . n A 1 415 LEU 415 429 429 LEU LEU A . n A 1 416 TRP 416 430 430 TRP TRP A . n A 1 417 LEU 417 431 431 LEU LEU A . n A 1 418 LEU 418 432 432 LEU LEU A . n A 1 419 ASP 419 433 433 ASP ASP A . n A 1 420 GLY 420 434 434 GLY GLY A . n A 1 421 SER 421 435 435 SER SER A . n A 1 422 GLY 422 436 436 GLY GLY A . n A 1 423 SER 423 437 437 SER SER A . n A 1 424 PHE 424 438 438 PHE PHE A . n A 1 425 THR 425 439 439 THR THR A . n A 1 426 LEU 426 440 440 LEU LEU A . n A 1 427 GLU 427 441 441 GLU GLU A . n A 1 428 LEU 428 442 442 LEU LEU A . n A 1 429 GLU 429 443 443 GLU GLU A . n A 1 430 GLU 430 444 444 GLU GLU A . n A 1 431 ASP 431 445 445 ASP ASP A . n A 1 432 GLU 432 446 446 GLU GLU A . n A 1 433 ILE 433 447 447 ILE ILE A . n A 1 434 PHE 434 448 448 PHE PHE A . n A 1 435 THR 435 449 449 THR THR A . n A 1 436 LEU 436 450 450 LEU LEU A . n A 1 437 THR 437 451 451 THR THR A . n A 1 438 THR 438 452 452 THR THR A . n A 1 439 LEU 439 453 453 LEU LEU A . n A 1 440 THR 440 454 454 THR THR A . n A 1 441 THR 441 455 455 THR THR A . n A 1 442 GLY 442 456 456 GLY GLY A . n A 1 443 ARG 443 457 457 ARG ARG A . n A 1 444 LYS 444 458 458 LYS LYS A . n A 1 445 GLY 445 459 459 GLY GLY A . n A 1 446 SER 446 460 460 SER SER A . n A 1 447 TYR 447 461 461 TYR TYR A . n A 1 448 PRO 448 462 462 PRO PRO A . n A 1 449 PRO 449 463 463 PRO PRO A . n A 1 450 PRO 450 464 464 PRO PRO A . n A 1 451 PRO 451 465 465 PRO PRO A . n A 1 452 SER 452 466 466 SER SER A . n A 1 453 SER 453 467 467 SER SER A . n A 1 454 LYS 454 468 468 LYS LYS A . n A 1 455 PRO 455 469 469 PRO PRO A . n A 1 456 PHE 456 470 470 PHE PHE A . n A 1 457 PRO 457 471 471 PRO PRO A . n A 1 458 THR 458 472 472 THR THR A . n A 1 459 ASN 459 473 473 ASN ASN A . n A 1 460 TYR 460 474 474 TYR TYR A . n A 1 461 LYS 461 475 475 LYS LYS A . n A 1 462 ASP 462 476 476 ASP ASP A . n A 1 463 ASP 463 477 477 ASP ASP A . n A 1 464 PHE 464 478 478 PHE PHE A . n A 1 465 ASN 465 479 479 ASN ASN A . n A 1 466 VAL 466 480 480 VAL VAL A . n A 1 467 GLU 467 481 481 GLU GLU A . n A 1 468 TYR 468 482 482 TYR TYR A . n A 1 469 PRO 469 483 483 PRO PRO A . n A 1 470 LEU 470 484 484 LEU LEU A . n A 1 471 PHE 471 485 485 PHE PHE A . n A 1 472 SER 472 486 486 SER SER A . n A 1 473 GLU 473 487 487 GLU GLU A . n A 1 474 ALA 474 488 488 ALA ALA A . n A 1 475 PRO 475 489 489 PRO PRO A . n A 1 476 ASN 476 490 490 ASN ASN A . n A 1 477 PHE 477 491 491 PHE PHE A . n A 1 478 ALA 478 492 492 ALA ALA A . n A 1 479 ASP 479 493 493 ASP ASP A . n A 1 480 GLN 480 494 494 GLN GLN A . n A 1 481 THR 481 495 495 THR THR A . n A 1 482 GLY 482 496 496 GLY GLY A . n A 1 483 VAL 483 497 497 VAL VAL A . n A 1 484 PHE 484 498 498 PHE PHE A . n A 1 485 GLU 485 499 499 GLU GLU A . n A 1 486 TYR 486 500 500 TYR TYR A . n A 1 487 TYR 487 501 501 TYR TYR A . n A 1 488 MET 488 502 502 MET MET A . n A 1 489 ASN 489 503 503 ASN ASN A . n A 1 490 ASN 490 504 504 ASN ASN A . n A 1 491 GLU 491 505 505 GLU GLU A . n A 1 492 ASP 492 506 506 ASP ASP A . n A 1 493 ARG 493 507 507 ARG ARG A . n A 1 494 GLU 494 508 508 GLU GLU A . n A 1 495 HIS 495 509 509 HIS HIS A . n A 1 496 ARG 496 510 510 ARG ARG A . n A 1 497 PHE 497 511 511 PHE PHE A . n A 1 498 THR 498 512 512 THR THR A . n A 1 499 LEU 499 513 513 LEU LEU A . n A 1 500 ARG 500 514 514 ARG ARG A . n A 1 501 GLN 501 515 515 GLN GLN A . n A 1 502 VAL 502 516 516 VAL VAL A . n A 1 503 LEU 503 517 517 LEU LEU A . n A 1 504 ASN 504 518 518 ASN ASN A . n A 1 505 GLN 505 519 519 GLN GLN A . n A 1 506 ARG 506 520 520 ARG ARG A . n A 1 507 PRO 507 521 521 PRO PRO A . n A 1 508 ILE 508 522 522 ILE ILE A . n A 1 509 THR 509 523 523 THR THR A . n A 1 510 TRP 510 524 524 TRP TRP A . n A 1 511 ALA 511 525 525 ALA ALA A . n A 1 512 ALA 512 526 526 ALA ALA A . n A 1 513 ASP 513 527 527 ASP ASP A . n A 1 514 ALA 514 528 528 ALA ALA A . n A 1 515 SER 515 529 529 SER SER A . n A 1 516 SER 516 530 530 SER SER A . n A 1 517 THR 517 531 531 THR THR A . n A 1 518 ILE 518 532 532 ILE ILE A . n A 1 519 SER 519 533 533 SER SER A . n A 1 520 VAL 520 534 534 VAL VAL A . n A 1 521 ILE 521 535 535 ILE ILE A . n A 1 522 GLY 522 536 536 GLY GLY A . n A 1 523 ASP 523 537 537 ASP ASP A . n A 1 524 HIS 524 538 538 HIS HIS A . n A 1 525 HIS 525 539 539 HIS HIS A . n A 1 526 TRP 526 540 540 TRP TRP A . n A 1 527 THR 527 541 541 THR THR A . n A 1 528 ASN 528 542 542 ASN ASN A . n A 1 529 MET 529 543 543 MET MET A . n A 1 530 THR 530 544 544 THR THR A . n A 1 531 VAL 531 545 545 VAL VAL A . n A 1 532 GLN 532 546 546 GLN GLN A . n A 1 533 CYS 533 547 547 CYS CYS A . n A 1 534 ASP 534 548 548 ASP ASP A . n A 1 535 VAL 535 549 549 VAL VAL A . n A 1 536 TYR 536 550 550 TYR TYR A . n A 1 537 ILE 537 551 551 ILE ILE A . n A 1 538 GLU 538 552 552 GLU GLU A . n A 1 539 THR 539 553 553 THR THR A . n A 1 540 PRO 540 554 554 PRO PRO A . n A 1 541 ARG 541 555 555 ARG ARG A . n A 1 542 SER 542 556 556 SER SER A . n A 1 543 GLY 543 557 557 GLY GLY A . n A 1 544 GLY 544 558 558 GLY GLY A . n A 1 545 VAL 545 559 559 VAL VAL A . n A 1 546 PHE 546 560 560 PHE PHE A . n A 1 547 ILE 547 561 561 ILE ILE A . n A 1 548 ALA 548 562 562 ALA ALA A . n A 1 549 GLY 549 563 563 GLY GLY A . n A 1 550 ARG 550 564 564 ARG ARG A . n A 1 551 VAL 551 565 565 VAL VAL A . n A 1 552 ASN 552 566 566 ASN ASN A . n A 1 553 LYS 553 567 567 LYS LYS A . n A 1 554 GLY 554 568 568 GLY GLY A . n A 1 555 GLY 555 569 569 GLY GLY A . n A 1 556 ILE 556 570 570 ILE ILE A . n A 1 557 LEU 557 571 571 LEU LEU A . n A 1 558 ILE 558 572 572 ILE ILE A . n A 1 559 ARG 559 573 573 ARG ARG A . n A 1 560 SER 560 574 574 SER SER A . n A 1 561 ALA 561 575 575 ALA ALA A . n A 1 562 THR 562 576 576 THR THR A . n A 1 563 GLY 563 577 577 GLY GLY A . n A 1 564 VAL 564 578 578 VAL VAL A . n A 1 565 PHE 565 579 579 PHE PHE A . n A 1 566 PHE 566 580 580 PHE PHE A . n A 1 567 TRP 567 581 581 TRP TRP A . n A 1 568 ILE 568 582 582 ILE ILE A . n A 1 569 PHE 569 583 583 PHE PHE A . n A 1 570 ALA 570 584 584 ALA ALA A . n A 1 571 ASN 571 585 585 ASN ASN A . n A 1 572 GLY 572 586 586 GLY GLY A . n A 1 573 SER 573 587 587 SER SER A . n A 1 574 TYR 574 588 588 TYR TYR A . n A 1 575 ARG 575 589 589 ARG ARG A . n A 1 576 VAL 576 590 590 VAL VAL A . n A 1 577 THR 577 591 591 THR THR A . n A 1 578 ALA 578 592 592 ALA ALA A . n A 1 579 ASP 579 593 593 ASP ASP A . n A 1 580 LEU 580 594 594 LEU LEU A . n A 1 581 GLY 581 595 595 GLY GLY A . n A 1 582 GLY 582 596 596 GLY GLY A . n A 1 583 TRP 583 597 597 TRP TRP A . n A 1 584 ILE 584 598 598 ILE ILE A . n A 1 585 THR 585 599 599 THR THR A . n A 1 586 TYR 586 600 600 TYR TYR A . n A 1 587 ALA 587 601 601 ALA ALA A . n A 1 588 SER 588 602 602 SER SER A . n A 1 589 GLY 589 603 603 GLY GLY A . n A 1 590 HIS 590 604 604 HIS HIS A . n A 1 591 ALA 591 605 605 ALA ALA A . n A 1 592 ASP 592 606 606 ASP ASP A . n A 1 593 VAL 593 607 607 VAL VAL A . n A 1 594 THR 594 608 608 THR THR A . n A 1 595 ALA 595 609 609 ALA ALA A . n A 1 596 LYS 596 610 610 LYS LYS A . n A 1 597 ARG 597 611 611 ARG ARG A . n A 1 598 TRP 598 612 612 TRP TRP A . n A 1 599 TYR 599 613 613 TYR TYR A . n A 1 600 THR 600 614 614 THR THR A . n A 1 601 LEU 601 615 615 LEU LEU A . n A 1 602 THR 602 616 616 THR THR A . n A 1 603 LEU 603 617 617 LEU LEU A . n A 1 604 GLY 604 618 618 GLY GLY A . n A 1 605 ILE 605 619 619 ILE ILE A . n A 1 606 LYS 606 620 620 LYS LYS A . n A 1 607 GLY 607 621 621 GLY GLY A . n A 1 608 TYR 608 622 622 TYR TYR A . n A 1 609 PHE 609 623 623 PHE PHE A . n A 1 610 ALA 610 624 624 ALA ALA A . n A 1 611 PHE 611 625 625 PHE PHE A . n A 1 612 GLY 612 626 626 GLY GLY A . n A 1 613 MET 613 627 627 MET MET A . n A 1 614 LEU 614 628 628 LEU LEU A . n A 1 615 ASN 615 629 629 ASN ASN A . n A 1 616 GLY 616 630 630 GLY GLY A . n A 1 617 THR 617 631 631 THR THR A . n A 1 618 ILE 618 632 632 ILE ILE A . n A 1 619 LEU 619 633 633 LEU LEU A . n A 1 620 TRP 620 634 634 TRP TRP A . n A 1 621 LYS 621 635 635 LYS LYS A . n A 1 622 ASN 622 636 636 ASN ASN A . n A 1 623 VAL 623 637 637 VAL VAL A . n A 1 624 ARG 624 638 638 ARG ARG A . n A 1 625 VAL 625 639 639 VAL VAL A . n A 1 626 LYS 626 640 640 LYS LYS A . n A 1 627 TYR 627 641 641 TYR TYR A . n A 1 628 PRO 628 642 642 PRO PRO A . n A 1 629 GLY 629 643 643 GLY GLY A . n A 1 630 HIS 630 644 644 HIS HIS A . n A 1 631 GLY 631 645 645 GLY GLY A . n A 1 632 TRP 632 646 646 TRP TRP A . n A 1 633 ALA 633 647 647 ALA ALA A . n A 1 634 ALA 634 648 648 ALA ALA A . n A 1 635 ILE 635 649 649 ILE ILE A . n A 1 636 GLY 636 650 650 GLY GLY A . n A 1 637 THR 637 651 651 THR THR A . n A 1 638 HIS 638 652 652 HIS HIS A . n A 1 639 THR 639 653 653 THR THR A . n A 1 640 PHE 640 654 654 PHE PHE A . n A 1 641 GLU 641 655 655 GLU GLU A . n A 1 642 PHE 642 656 656 PHE PHE A . n A 1 643 ALA 643 657 657 ALA ALA A . n A 1 644 GLN 644 658 658 GLN GLN A . n A 1 645 PHE 645 659 659 PHE PHE A . n A 1 646 ASP 646 660 660 ASP ASP A . n A 1 647 ASN 647 661 661 ASN ASN A . n A 1 648 PHE 648 662 662 PHE PHE A . n A 1 649 ARG 649 663 663 ARG ARG A . n A 1 650 VAL 650 664 664 VAL VAL A . n A 1 651 GLU 651 665 665 GLU GLU A . n A 1 652 ALA 652 666 666 ALA ALA A . n A 1 653 ALA 653 667 667 ALA ALA A . n A 1 654 ARG 654 668 668 ARG ARG 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 2 147 1 1001 1001 147 147 A . C 3 NAG 1 1284 1284 NAG NAG A . D 3 NAG 2 1285 1285 NAG NAG A . E 3 NAG 1 1363 1363 NAG NAG A . F 3 NAG 2 1364 1364 NAG NAG A . G 3 NAG 1 1387 1387 NAG NAG A . H 3 NAG 1 1542 1542 NAG NAG A . I 3 NAG 2 1543 1543 NAG NAG A . J 4 CA 1 1669 1669 CA CA A . K 5 HOH 1 2001 2001 HOH HOH A . K 5 HOH 2 2002 2002 HOH HOH A . K 5 HOH 3 2003 2003 HOH HOH A . K 5 HOH 4 2004 2004 HOH HOH A . K 5 HOH 5 2005 2005 HOH HOH A . K 5 HOH 6 2006 2006 HOH HOH A . K 5 HOH 7 2007 2007 HOH HOH A . K 5 HOH 8 2008 2008 HOH HOH A . K 5 HOH 9 2009 2009 HOH HOH A . K 5 HOH 10 2010 2010 HOH HOH A . K 5 HOH 11 2011 2011 HOH HOH A . K 5 HOH 12 2012 2012 HOH HOH A . K 5 HOH 13 2013 2013 HOH HOH A . K 5 HOH 14 2014 2014 HOH HOH A . K 5 HOH 15 2015 2015 HOH HOH A . K 5 HOH 16 2016 2016 HOH HOH A . K 5 HOH 17 2017 2017 HOH HOH A . K 5 HOH 18 2018 2018 HOH HOH A . K 5 HOH 19 2019 2019 HOH HOH A . K 5 HOH 20 2020 2020 HOH HOH A . K 5 HOH 21 2021 2021 HOH HOH A . K 5 HOH 22 2022 2022 HOH HOH A . K 5 HOH 23 2023 2023 HOH HOH A . K 5 HOH 24 2024 2024 HOH HOH A . K 5 HOH 25 2025 2025 HOH HOH A . K 5 HOH 26 2026 2026 HOH HOH A . K 5 HOH 27 2027 2027 HOH HOH A . K 5 HOH 28 2028 2028 HOH HOH A . K 5 HOH 29 2029 2029 HOH HOH A . K 5 HOH 30 2030 2030 HOH HOH A . K 5 HOH 31 2031 2031 HOH HOH A . K 5 HOH 32 2032 2032 HOH HOH A . K 5 HOH 33 2033 2033 HOH HOH A . K 5 HOH 34 2034 2034 HOH HOH A . K 5 HOH 35 2035 2035 HOH HOH A . K 5 HOH 36 2036 2036 HOH HOH A . K 5 HOH 37 2037 2037 HOH HOH A . K 5 HOH 38 2038 2038 HOH HOH A . K 5 HOH 39 2039 2039 HOH HOH A . K 5 HOH 40 2040 2040 HOH HOH A . K 5 HOH 41 2041 2041 HOH HOH A . K 5 HOH 42 2042 2042 HOH HOH A . K 5 HOH 43 2043 2043 HOH HOH A . K 5 HOH 44 2044 2044 HOH HOH A . K 5 HOH 45 2045 2045 HOH HOH A . K 5 HOH 46 2046 2046 HOH HOH A . K 5 HOH 47 2047 2047 HOH HOH A . K 5 HOH 48 2048 2048 HOH HOH A . K 5 HOH 49 2049 2049 HOH HOH A . K 5 HOH 50 2050 2050 HOH HOH A . K 5 HOH 51 2051 2051 HOH HOH A . K 5 HOH 52 2052 2052 HOH HOH A . K 5 HOH 53 2053 2053 HOH HOH A . K 5 HOH 54 2054 2054 HOH HOH A . K 5 HOH 55 2055 2055 HOH HOH A . K 5 HOH 56 2056 2056 HOH HOH A . K 5 HOH 57 2057 2057 HOH HOH A . K 5 HOH 58 2058 2058 HOH HOH A . K 5 HOH 59 2059 2059 HOH HOH A . K 5 HOH 60 2060 2060 HOH HOH A . K 5 HOH 61 2061 2061 HOH HOH A . K 5 HOH 62 2062 2062 HOH HOH A . K 5 HOH 63 2063 2063 HOH HOH A . K 5 HOH 64 2064 2064 HOH HOH A . K 5 HOH 65 2065 2065 HOH HOH A . K 5 HOH 66 2066 2066 HOH HOH A . K 5 HOH 67 2067 2067 HOH HOH A . K 5 HOH 68 2068 2068 HOH HOH A . K 5 HOH 69 2069 2069 HOH HOH A . K 5 HOH 70 2070 2070 HOH HOH A . K 5 HOH 71 2071 2071 HOH HOH A . K 5 HOH 72 2072 2072 HOH HOH A . K 5 HOH 73 2073 2073 HOH HOH A . K 5 HOH 74 2074 2074 HOH HOH A . K 5 HOH 75 2075 2075 HOH HOH A . K 5 HOH 76 2076 2076 HOH HOH A . K 5 HOH 77 2077 2077 HOH HOH A . K 5 HOH 78 2078 2078 HOH HOH A . K 5 HOH 79 2079 2079 HOH HOH A . K 5 HOH 80 2080 2080 HOH HOH A . K 5 HOH 81 2081 2081 HOH HOH A . K 5 HOH 82 2082 2082 HOH HOH A . K 5 HOH 83 2083 2083 HOH HOH A . K 5 HOH 84 2084 2084 HOH HOH A . K 5 HOH 85 2085 2085 HOH HOH A . K 5 HOH 86 2086 2086 HOH HOH A . K 5 HOH 87 2087 2087 HOH HOH A . K 5 HOH 88 2088 2088 HOH HOH A . K 5 HOH 89 2089 2089 HOH HOH A . K 5 HOH 90 2090 2090 HOH HOH A . K 5 HOH 91 2091 2091 HOH HOH A . K 5 HOH 92 2092 2092 HOH HOH A . K 5 HOH 93 2093 2093 HOH HOH A . K 5 HOH 94 2094 2094 HOH HOH A . K 5 HOH 95 2095 2095 HOH HOH A . K 5 HOH 96 2096 2096 HOH HOH A . K 5 HOH 97 2097 2097 HOH HOH A . K 5 HOH 98 2098 2098 HOH HOH A . K 5 HOH 99 2099 2099 HOH HOH A . K 5 HOH 100 2100 2100 HOH HOH A . K 5 HOH 101 2101 2101 HOH HOH A . K 5 HOH 102 2102 2102 HOH HOH A . K 5 HOH 103 2103 2103 HOH HOH A . K 5 HOH 104 2104 2104 HOH HOH A . K 5 HOH 105 2105 2105 HOH HOH A . K 5 HOH 106 2106 2106 HOH HOH A . K 5 HOH 107 2107 2107 HOH HOH A . K 5 HOH 108 2108 2108 HOH HOH A . K 5 HOH 109 2109 2109 HOH HOH A . K 5 HOH 110 2110 2110 HOH HOH A . K 5 HOH 111 2111 2111 HOH HOH A . K 5 HOH 112 2112 2112 HOH HOH A . K 5 HOH 113 2113 2113 HOH HOH A . K 5 HOH 114 2114 2114 HOH HOH A . K 5 HOH 115 2115 2115 HOH HOH A . K 5 HOH 116 2116 2116 HOH HOH A . K 5 HOH 117 2117 2117 HOH HOH A . K 5 HOH 118 2118 2118 HOH HOH A . K 5 HOH 119 2119 2119 HOH HOH A . K 5 HOH 120 2120 2120 HOH HOH A . K 5 HOH 121 2121 2121 HOH HOH A . K 5 HOH 122 2122 2122 HOH HOH A . K 5 HOH 123 2123 2123 HOH HOH A . K 5 HOH 124 2124 2124 HOH HOH A . K 5 HOH 125 2125 2125 HOH HOH A . K 5 HOH 126 2126 2126 HOH HOH A . K 5 HOH 127 2127 2127 HOH HOH A . K 5 HOH 128 2128 2128 HOH HOH A . K 5 HOH 129 2129 2129 HOH HOH A . K 5 HOH 130 2130 2130 HOH HOH A . K 5 HOH 131 2131 2131 HOH HOH A . K 5 HOH 132 2132 2132 HOH HOH A . K 5 HOH 133 2133 2133 HOH HOH A . K 5 HOH 134 2134 2134 HOH HOH A . K 5 HOH 135 2135 2135 HOH HOH A . K 5 HOH 136 2136 2136 HOH HOH A . K 5 HOH 137 2137 2137 HOH HOH A . K 5 HOH 138 2138 2138 HOH HOH A . K 5 HOH 139 2139 2139 HOH HOH A . K 5 HOH 140 2140 2140 HOH HOH A . K 5 HOH 141 2141 2141 HOH HOH A . K 5 HOH 142 2142 2142 HOH HOH A . K 5 HOH 143 2143 2143 HOH HOH A . K 5 HOH 144 2144 2144 HOH HOH A . K 5 HOH 145 2145 2145 HOH HOH A . K 5 HOH 146 2146 2146 HOH HOH A . K 5 HOH 147 2147 2147 HOH HOH A . K 5 HOH 148 2148 2148 HOH HOH A . K 5 HOH 149 2149 2149 HOH HOH A . K 5 HOH 150 2150 2150 HOH HOH A . K 5 HOH 151 2151 2151 HOH HOH A . K 5 HOH 152 2152 2152 HOH HOH A . K 5 HOH 153 2153 2153 HOH HOH A . K 5 HOH 154 2154 2154 HOH HOH A . K 5 HOH 155 2155 2155 HOH HOH A . K 5 HOH 156 2156 2156 HOH HOH A . K 5 HOH 157 2157 2157 HOH HOH A . K 5 HOH 158 2158 2158 HOH HOH A . K 5 HOH 159 2159 2159 HOH HOH A . K 5 HOH 160 2160 2160 HOH HOH A . K 5 HOH 161 2161 2161 HOH HOH A . K 5 HOH 162 2162 2162 HOH HOH A . K 5 HOH 163 2163 2163 HOH HOH A . K 5 HOH 164 2164 2164 HOH HOH A . K 5 HOH 165 2165 2165 HOH HOH A . K 5 HOH 166 2166 2166 HOH HOH A . K 5 HOH 167 2167 2167 HOH HOH A . K 5 HOH 168 2168 2168 HOH HOH A . K 5 HOH 169 2169 2169 HOH HOH A . K 5 HOH 170 2170 2170 HOH HOH A . K 5 HOH 171 2171 2171 HOH HOH A . K 5 HOH 172 2172 2172 HOH HOH A . K 5 HOH 173 2173 2173 HOH HOH A . K 5 HOH 174 2174 2174 HOH HOH A . K 5 HOH 175 2175 2175 HOH HOH A . K 5 HOH 176 2176 2176 HOH HOH A . K 5 HOH 177 2177 2177 HOH HOH A . K 5 HOH 178 2178 2178 HOH HOH A . K 5 HOH 179 2179 2179 HOH HOH A . K 5 HOH 180 2180 2180 HOH HOH A . K 5 HOH 181 2181 2181 HOH HOH A . K 5 HOH 182 2182 2182 HOH HOH A . K 5 HOH 183 2183 2183 HOH HOH A . K 5 HOH 184 2184 2184 HOH HOH A . K 5 HOH 185 2185 2185 HOH HOH A . K 5 HOH 186 2186 2186 HOH HOH A . K 5 HOH 187 2187 2187 HOH HOH A . K 5 HOH 188 2188 2188 HOH HOH A . K 5 HOH 189 2189 2189 HOH HOH A . K 5 HOH 190 2190 2190 HOH HOH A . K 5 HOH 191 2191 2191 HOH HOH A . K 5 HOH 192 2192 2192 HOH HOH A . K 5 HOH 193 2193 2193 HOH HOH A . K 5 HOH 194 2194 2194 HOH HOH A . K 5 HOH 195 2195 2195 HOH HOH A . K 5 HOH 196 2196 2196 HOH HOH A . K 5 HOH 197 2197 2197 HOH HOH A . K 5 HOH 198 2198 2198 HOH HOH A . K 5 HOH 199 2199 2199 HOH HOH A . K 5 HOH 200 2200 2200 HOH HOH A . K 5 HOH 201 2201 2201 HOH HOH A . K 5 HOH 202 2202 2202 HOH HOH A . K 5 HOH 203 2203 2203 HOH HOH A . K 5 HOH 204 2204 2204 HOH HOH A . K 5 HOH 205 2205 2205 HOH HOH A . K 5 HOH 206 2206 2206 HOH HOH A . K 5 HOH 207 2207 2207 HOH HOH A . K 5 HOH 208 2208 2208 HOH HOH A . K 5 HOH 209 2209 2209 HOH HOH A . K 5 HOH 210 2210 2210 HOH HOH A . K 5 HOH 211 2211 2211 HOH HOH A . K 5 HOH 212 2212 2212 HOH HOH A . K 5 HOH 213 2213 2213 HOH HOH A . K 5 HOH 214 2214 2214 HOH HOH A . K 5 HOH 215 2215 2215 HOH HOH A . K 5 HOH 216 2216 2216 HOH HOH A . K 5 HOH 217 2217 2217 HOH HOH A . K 5 HOH 218 2218 2218 HOH HOH A . K 5 HOH 219 2219 2219 HOH HOH A . K 5 HOH 220 2220 2220 HOH HOH A . K 5 HOH 221 2221 2221 HOH HOH A . K 5 HOH 222 2222 2222 HOH HOH A . K 5 HOH 223 2223 2223 HOH HOH A . K 5 HOH 224 2224 2224 HOH HOH A . K 5 HOH 225 2225 2225 HOH HOH A . K 5 HOH 226 2226 2226 HOH HOH A . K 5 HOH 227 2227 2227 HOH HOH A . K 5 HOH 228 2228 2228 HOH HOH A . K 5 HOH 229 2229 2229 HOH HOH A . K 5 HOH 230 2230 2230 HOH HOH A . K 5 HOH 231 2231 2231 HOH HOH A . K 5 HOH 232 2232 2232 HOH HOH A . K 5 HOH 233 2233 2233 HOH HOH A . K 5 HOH 234 2234 2234 HOH HOH A . K 5 HOH 235 2235 2235 HOH HOH A . K 5 HOH 236 2236 2236 HOH HOH A . K 5 HOH 237 2237 2237 HOH HOH A . K 5 HOH 238 2238 2238 HOH HOH A . K 5 HOH 239 2239 2239 HOH HOH A . K 5 HOH 240 2240 2240 HOH HOH A . K 5 HOH 241 2241 2241 HOH HOH A . K 5 HOH 242 2242 2242 HOH HOH A . K 5 HOH 243 2243 2243 HOH HOH A . K 5 HOH 244 2244 2244 HOH HOH A . K 5 HOH 245 2245 2245 HOH HOH A . K 5 HOH 246 2246 2246 HOH HOH A . K 5 HOH 247 2247 2247 HOH HOH A . K 5 HOH 248 2248 2248 HOH HOH A . K 5 HOH 249 2249 2249 HOH HOH A . K 5 HOH 250 2250 2250 HOH HOH A . K 5 HOH 251 2251 2251 HOH HOH A . K 5 HOH 252 2252 2252 HOH HOH A . K 5 HOH 253 2253 2253 HOH HOH A . K 5 HOH 254 2254 2254 HOH HOH A . K 5 HOH 255 2255 2255 HOH HOH A . K 5 HOH 256 2256 2256 HOH HOH A . K 5 HOH 257 2257 2257 HOH HOH A . K 5 HOH 258 2258 2258 HOH HOH A . K 5 HOH 259 2259 2259 HOH HOH A . K 5 HOH 260 2260 2260 HOH HOH A . K 5 HOH 261 2261 2261 HOH HOH A . K 5 HOH 262 2262 2262 HOH HOH A . K 5 HOH 263 2263 2263 HOH HOH A . K 5 HOH 264 2264 2264 HOH HOH A . K 5 HOH 265 2265 2265 HOH HOH A . K 5 HOH 266 2266 2266 HOH HOH A . K 5 HOH 267 2267 2267 HOH HOH A . K 5 HOH 268 2268 2268 HOH HOH A . K 5 HOH 269 2269 2269 HOH HOH A . K 5 HOH 270 2270 2270 HOH HOH A . K 5 HOH 271 2271 2271 HOH HOH A . K 5 HOH 272 2272 2272 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 270 A ASN 284 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 349 A ASN 363 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 373 A ASN 387 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 528 A ASN 542 ? 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 # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2156 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id K _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # 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 OD1 ? A ASN 465 ? A ASN 479 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? A ASP 463 ? A ASP 477 ? 1_555 81.2 ? 2 OD1 ? A ASN 465 ? A ASN 479 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 OD1 ? A ASP 646 ? A ASP 660 ? 1_555 155.0 ? 3 O ? A ASP 463 ? A ASP 477 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 OD1 ? A ASP 646 ? A ASP 660 ? 1_555 81.9 ? 4 OD1 ? A ASN 465 ? A ASN 479 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? K HOH . ? A HOH 2209 ? 1_555 91.6 ? 5 O ? A ASP 463 ? A ASP 477 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? K HOH . ? A HOH 2209 ? 1_555 163.9 ? 6 OD1 ? A ASP 646 ? A ASP 660 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? K HOH . ? A HOH 2209 ? 1_555 99.8 ? 7 OD1 ? A ASN 465 ? A ASN 479 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? A PHE 497 ? A PHE 511 ? 1_555 107.9 ? 8 O ? A ASP 463 ? A ASP 477 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? A PHE 497 ? A PHE 511 ? 1_555 99.2 ? 9 OD1 ? A ASP 646 ? A ASP 660 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? A PHE 497 ? A PHE 511 ? 1_555 92.9 ? 10 O ? K HOH . ? A HOH 2209 ? 1_555 CA ? J CA . ? A CA 1669 ? 1_555 O ? A PHE 497 ? A PHE 511 ? 1_555 96.7 ? # 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 2014-01-08 # _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' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 82.7985 77.9050 43.6671 0.2889 0.8808 0.3946 -0.1216 -0.0866 -0.0000 1.5179 1.0034 0.7112 0.0141 0.6738 -0.1509 0.0841 -0.2609 -0.1419 0.2273 0.0439 -0.1180 0.0743 0.5205 -0.1474 'X-RAY DIFFRACTION' 2 ? refined 98.5264 105.0819 27.2817 0.4437 0.7923 0.5692 -0.3764 0.0233 -0.0092 0.6459 0.1377 0.1597 0.2508 0.0208 0.0878 -0.0219 0.0587 0.0990 -0.0035 0.0404 -0.1801 -0.0667 0.0344 0.0300 'X-RAY DIFFRACTION' 3 ? refined 74.7910 99.5360 22.3856 0.3854 0.6437 0.3300 -0.4844 0.0189 -0.0242 0.8458 0.3768 0.2710 0.2261 -0.0630 -0.0359 0.0585 0.0893 0.0608 -0.1162 -0.0007 -0.1116 -0.4757 0.5820 0.0682 'X-RAY DIFFRACTION' 4 ? refined 90.3200 110.3145 1.6237 0.7903 0.9817 0.5378 -0.5282 0.2015 0.1271 0.6343 0.3645 0.2364 0.4071 -0.3161 -0.1906 0.0666 0.1747 0.2130 -0.1604 -0.0333 -0.2194 -0.1917 0.1584 -0.0125 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'CHAIN A AND ((RESSEQ 472:668))' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'CHAIN A AND ((RESSEQ 453:471))' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'CHAIN A AND ((RESSEQ 41:337))' 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'CHAIN A AND ((RESSEQ 25:40) OR (RESSEQ 338:452))' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal PHENIX refinement '(PHENIX.REFINE)' ? 1 iMOSFLM 'data reduction' . ? 2 Aimless 'data scaling' . ? 3 PHENIX phasing . ? 4 # _pdbx_database_remark.id 700 _pdbx_database_remark.text ; SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. ; # _pdbx_entry_details.entry_id 4CCC _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ;4-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE (4NG): A RESTRAINT FILE FOR REFINEMENT WAS GENERATED USING ELBOW WITH A SMILES STRING. AFTER REFINEMENT, LIGAND ATOMS WERE RENUMBERED TO BE CONSISTENT WITH OTHER STRUCTURES DEPOSITED FOR THIS PUBLICATION. N-ACETYL-D-GLUCOSAMINE (NAG): N-LINKED GLYCOSYLATION SITES ; _pdbx_entry_details.sequence_details ;FRAGMENT CORRESPONDS TO RESIDUES 25-668 BASED ON NUMBERING STARTING AT SECOND UNIPROT INITIATION SITE. ; # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 2027 ? ? O A HOH 2028 ? ? 2.07 2 1 O A HOH 2125 ? ? O A HOH 2227 ? ? 2.17 3 1 O A HOH 2226 ? ? O A HOH 2227 ? ? 2.19 4 1 O A HOH 2027 ? ? O A HOH 2067 ? ? 2.19 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 2096 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 2096 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 4_556 _pdbx_validate_symm_contact.dist 2.16 # 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 PHE A 75 ? ? -149.58 -71.93 2 1 SER A 78 ? ? 38.48 54.24 3 1 ASP A 89 ? ? 70.60 -0.62 4 1 THR A 93 ? ? 147.89 -48.33 5 1 ILE A 179 ? ? -107.27 -82.40 6 1 ASN A 212 ? ? -148.51 -128.59 7 1 THR A 241 ? ? 72.39 -2.99 8 1 THR A 243 ? ? -114.56 -165.21 9 1 PHE A 260 ? ? 74.01 -99.88 10 1 ASN A 264 ? ? -82.99 36.92 11 1 ASN A 284 ? ? 58.61 18.04 12 1 SER A 296 ? ? -113.59 54.06 13 1 SER A 306 ? ? -106.36 44.13 14 1 SER A 376 ? ? -145.85 17.98 15 1 LEU A 432 ? ? 56.64 -2.75 16 1 ASP A 433 ? ? -104.95 -154.77 17 1 GLU A 443 ? ? -101.99 -161.07 18 1 PHE A 478 ? ? 56.85 16.65 19 1 ASN A 490 ? ? 71.69 -14.13 20 1 ILE A 522 ? ? -69.70 98.84 21 1 ARG A 555 ? ? 67.37 -47.74 22 1 THR A 653 ? ? -124.31 -162.46 # 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 GLU 349 ? CG ? A GLU 335 CG 2 1 Y 1 A GLU 349 ? CD ? A GLU 335 CD 3 1 Y 1 A GLU 349 ? OE1 ? A GLU 335 OE1 4 1 Y 1 A GLU 349 ? OE2 ? A GLU 335 OE2 5 1 Y 1 A GLN 374 ? CG ? A GLN 360 CG 6 1 Y 1 A GLN 374 ? CD ? A GLN 360 CD 7 1 Y 1 A GLN 374 ? OE1 ? A GLN 360 OE1 8 1 Y 1 A GLN 374 ? NE2 ? A GLN 360 NE2 9 1 Y 1 A LYS 398 ? CG ? A LYS 384 CG 10 1 Y 1 A LYS 398 ? CD ? A LYS 384 CD 11 1 Y 1 A LYS 398 ? CE ? A LYS 384 CE 12 1 Y 1 A LYS 398 ? NZ ? A LYS 384 NZ 13 1 Y 1 A ARG 402 ? CG ? A ARG 388 CG 14 1 Y 1 A ARG 402 ? CD ? A ARG 388 CD 15 1 Y 1 A ARG 402 ? NE ? A ARG 388 NE 16 1 Y 1 A ARG 402 ? CZ ? A ARG 388 CZ 17 1 Y 1 A ARG 402 ? NH1 ? A ARG 388 NH1 18 1 Y 1 A ARG 402 ? NH2 ? A ARG 388 NH2 19 1 Y 1 A GLU 403 ? CG ? A GLU 389 CG 20 1 Y 1 A GLU 403 ? CD ? A GLU 389 CD 21 1 Y 1 A GLU 403 ? OE1 ? A GLU 389 OE1 22 1 Y 1 A GLU 403 ? OE2 ? A GLU 389 OE2 23 1 Y 1 A ARG 420 ? CG ? A ARG 406 CG 24 1 Y 1 A ARG 420 ? CD ? A ARG 406 CD 25 1 Y 1 A ARG 420 ? NE ? A ARG 406 NE 26 1 Y 1 A ARG 420 ? CZ ? A ARG 406 CZ 27 1 Y 1 A ARG 420 ? NH1 ? A ARG 406 NH1 28 1 Y 1 A ARG 420 ? NH2 ? A ARG 406 NH2 29 1 Y 1 A LEU 432 ? CG ? A LEU 418 CG 30 1 Y 1 A LEU 432 ? CD1 ? A LEU 418 CD1 31 1 Y 1 A LEU 432 ? CD2 ? A LEU 418 CD2 32 1 Y 1 A LYS 475 ? CG ? A LYS 461 CG 33 1 Y 1 A LYS 475 ? CD ? A LYS 461 CD 34 1 Y 1 A LYS 475 ? CE ? A LYS 461 CE 35 1 Y 1 A LYS 475 ? NZ ? A LYS 461 NZ 36 1 Y 1 A ARG 507 ? CG ? A ARG 493 CG 37 1 Y 1 A ARG 507 ? CD ? A ARG 493 CD 38 1 Y 1 A ARG 507 ? NE ? A ARG 493 NE 39 1 Y 1 A ARG 507 ? CZ ? A ARG 493 CZ 40 1 Y 1 A ARG 507 ? NH1 ? A ARG 493 NH1 41 1 Y 1 A ARG 507 ? NH2 ? A ARG 493 NH2 42 1 Y 1 A LYS 635 ? CG ? A LYS 621 CG 43 1 Y 1 A LYS 635 ? CD ? A LYS 621 CD 44 1 Y 1 A LYS 635 ? CE ? A LYS 621 CE 45 1 Y 1 A LYS 635 ? NZ ? A LYS 621 NZ 46 1 Y 1 A ARG 663 ? CG ? A ARG 649 CG 47 1 Y 1 A ARG 663 ? CD ? A ARG 649 CD 48 1 Y 1 A ARG 663 ? NE ? A ARG 649 NE 49 1 Y 1 A ARG 663 ? CZ ? A ARG 649 CZ 50 1 Y 1 A ARG 663 ? NH1 ? A ARG 649 NH1 51 1 Y 1 A ARG 663 ? NH2 ? A ARG 649 NH2 # 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 HIS 15 ? A HIS 1 2 1 Y 1 A HIS 16 ? A HIS 2 3 1 Y 1 A HIS 17 ? A HIS 3 4 1 Y 1 A HIS 18 ? A HIS 4 5 1 Y 1 A HIS 19 ? A HIS 5 6 1 Y 1 A HIS 20 ? A HIS 6 7 1 Y 1 A ILE 21 ? A ILE 7 8 1 Y 1 A GLU 22 ? A GLU 8 9 1 Y 1 A GLY 23 ? A GLY 9 10 1 Y 1 A ARG 24 ? A ARG 10 11 1 Y 1 A THR 416 ? A THR 402 12 1 Y 1 A PRO 417 ? A PRO 403 13 1 Y 1 A GLN 418 ? A GLN 404 14 1 Y 1 A GLN 419 ? A GLN 405 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 '1-O-[P-NITROPHENYL]-BETA-D-GALACTOPYRANOSE' 147 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'CALCIUM ION' CA 5 water HOH #